data_9NRB
# 
_entry.id   9NRB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9NRB         pdb_00009nrb 10.2210/pdb9nrb/pdb 
WWPDB D_1000294075 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-23 ? 
2 'Structure model' 1 1 2025-04-30 ? 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_first'              
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
4 2 'Structure model' '_citation.title'                   
5 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9NRB 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              wilson@scripps.edu 
_pdbx_contact_author.name_first         Ian 
_pdbx_contact_author.name_last          Wilson 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6469-2419 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lin, T.H.'    1 ? 
'Zhu, Y.'      2 ? 
'Wilson, I.A.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2419800122 
_citation.page_last                 e2419800122 
_citation.title                     
'The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2419800122 
_citation.pdbx_database_id_PubMed   40232794 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rios Carrasco, M.'    1  0000-0001-7000-2018 
primary 'Lin, T.H.'            2  0000-0002-0937-9972 
primary 'Zhu, X.'              3  0000-0002-6021-3740 
primary 'Gabarroca Garcia, A.' 4  0009-0005-4266-3712 
primary 'Uslu, E.'             5  0009-0009-3678-1893 
primary 'Liang, R.'            6  ?                   
primary 'Spruit, C.M.'         7  ?                   
primary 'Richard, M.'          8  0000-0003-0240-9312 
primary 'Boons, G.J.'          9  0000-0003-3111-5954 
primary 'Wilson, I.A.'         10 0000-0002-6469-2419 
primary 'de Vries, R.P.'       11 0000-0002-1586-4464 
# 
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 HA1 chain' 36976.926 3  ? Q226L ? ? 
2 polymer     man 'Hemagglutinin HA2 chain' 20414.504 3  ? ?     ? ? 
3 branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   3  
? ?     ? ? 
4 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   1  ? ?     ? 
? 
5 branched    syn 
;N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose
;
836.744   1  ? ?     ? ? 
6 non-polymer nat 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   6  ? ?     ? ? 
7 water       nat water 18.015    62 ? ?     ? ? 
# 
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 
;DPGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLNGVKPLILKDCSVAGWLLGNPMCDEFIRVPEWS
YIVERANPANDLCYPGSLNDYEELKHLLSRINHFEKILIIPKSSWPNHETSLGVSAACPYQGTPSFFRNVVWLIKKNDAY
PTIKISYNNTNREDLLILWGIHHSNNAEEQTNLYKNPTTYISVGTSTLNQRLVPKIATRSQVNGLRGRMDFFWTILKPND
AIHFESNGNFIAPEYAYKIVKKGDSTIMKSGVEYGHCNTKCQTPVGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATGL
RNSPQRET
;
;DPGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLNGVKPLILKDCSVAGWLLGNPMCDEFIRVPEWS
YIVERANPANDLCYPGSLNDYEELKHLLSRINHFEKILIIPKSSWPNHETSLGVSAACPYQGTPSFFRNVVWLIKKNDAY
PTIKISYNNTNREDLLILWGIHHSNNAEEQTNLYKNPTTYISVGTSTLNQRLVPKIATRSQVNGLRGRMDFFWTILKPND
AIHFESNGNFIAPEYAYKIVKKGDSTIMKSGVEYGHCNTKCQTPVGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATGL
RNSPQRET
;
A,C,E ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEARLKREEISSGR
;
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEARLKREEISSGR
;
B,D,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
6 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
7 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   PRO n 
1 3   GLY n 
1 4   ASP n 
1 5   GLN n 
1 6   ILE n 
1 7   CYS n 
1 8   ILE n 
1 9   GLY n 
1 10  TYR n 
1 11  HIS n 
1 12  ALA n 
1 13  ASN n 
1 14  ASN n 
1 15  SER n 
1 16  THR n 
1 17  GLU n 
1 18  GLN n 
1 19  VAL n 
1 20  ASP n 
1 21  THR n 
1 22  ILE n 
1 23  MET n 
1 24  GLU n 
1 25  LYS n 
1 26  ASN n 
1 27  VAL n 
1 28  THR n 
1 29  VAL n 
1 30  THR n 
1 31  HIS n 
1 32  ALA n 
1 33  GLN n 
1 34  ASP n 
1 35  ILE n 
1 36  LEU n 
1 37  GLU n 
1 38  LYS n 
1 39  THR n 
1 40  HIS n 
1 41  ASN n 
1 42  GLY n 
1 43  LYS n 
1 44  LEU n 
1 45  CYS n 
1 46  ASP n 
1 47  LEU n 
1 48  ASN n 
1 49  GLY n 
1 50  VAL n 
1 51  LYS n 
1 52  PRO n 
1 53  LEU n 
1 54  ILE n 
1 55  LEU n 
1 56  LYS n 
1 57  ASP n 
1 58  CYS n 
1 59  SER n 
1 60  VAL n 
1 61  ALA n 
1 62  GLY n 
1 63  TRP n 
1 64  LEU n 
1 65  LEU n 
1 66  GLY n 
1 67  ASN n 
1 68  PRO n 
1 69  MET n 
1 70  CYS n 
1 71  ASP n 
1 72  GLU n 
1 73  PHE n 
1 74  ILE n 
1 75  ARG n 
1 76  VAL n 
1 77  PRO n 
1 78  GLU n 
1 79  TRP n 
1 80  SER n 
1 81  TYR n 
1 82  ILE n 
1 83  VAL n 
1 84  GLU n 
1 85  ARG n 
1 86  ALA n 
1 87  ASN n 
1 88  PRO n 
1 89  ALA n 
1 90  ASN n 
1 91  ASP n 
1 92  LEU n 
1 93  CYS n 
1 94  TYR n 
1 95  PRO n 
1 96  GLY n 
1 97  SER n 
1 98  LEU n 
1 99  ASN n 
1 100 ASP n 
1 101 TYR n 
1 102 GLU n 
1 103 GLU n 
1 104 LEU n 
1 105 LYS n 
1 106 HIS n 
1 107 LEU n 
1 108 LEU n 
1 109 SER n 
1 110 ARG n 
1 111 ILE n 
1 112 ASN n 
1 113 HIS n 
1 114 PHE n 
1 115 GLU n 
1 116 LYS n 
1 117 ILE n 
1 118 LEU n 
1 119 ILE n 
1 120 ILE n 
1 121 PRO n 
1 122 LYS n 
1 123 SER n 
1 124 SER n 
1 125 TRP n 
1 126 PRO n 
1 127 ASN n 
1 128 HIS n 
1 129 GLU n 
1 130 THR n 
1 131 SER n 
1 132 LEU n 
1 133 GLY n 
1 134 VAL n 
1 135 SER n 
1 136 ALA n 
1 137 ALA n 
1 138 CYS n 
1 139 PRO n 
1 140 TYR n 
1 141 GLN n 
1 142 GLY n 
1 143 THR n 
1 144 PRO n 
1 145 SER n 
1 146 PHE n 
1 147 PHE n 
1 148 ARG n 
1 149 ASN n 
1 150 VAL n 
1 151 VAL n 
1 152 TRP n 
1 153 LEU n 
1 154 ILE n 
1 155 LYS n 
1 156 LYS n 
1 157 ASN n 
1 158 ASP n 
1 159 ALA n 
1 160 TYR n 
1 161 PRO n 
1 162 THR n 
1 163 ILE n 
1 164 LYS n 
1 165 ILE n 
1 166 SER n 
1 167 TYR n 
1 168 ASN n 
1 169 ASN n 
1 170 THR n 
1 171 ASN n 
1 172 ARG n 
1 173 GLU n 
1 174 ASP n 
1 175 LEU n 
1 176 LEU n 
1 177 ILE n 
1 178 LEU n 
1 179 TRP n 
1 180 GLY n 
1 181 ILE n 
1 182 HIS n 
1 183 HIS n 
1 184 SER n 
1 185 ASN n 
1 186 ASN n 
1 187 ALA n 
1 188 GLU n 
1 189 GLU n 
1 190 GLN n 
1 191 THR n 
1 192 ASN n 
1 193 LEU n 
1 194 TYR n 
1 195 LYS n 
1 196 ASN n 
1 197 PRO n 
1 198 THR n 
1 199 THR n 
1 200 TYR n 
1 201 ILE n 
1 202 SER n 
1 203 VAL n 
1 204 GLY n 
1 205 THR n 
1 206 SER n 
1 207 THR n 
1 208 LEU n 
1 209 ASN n 
1 210 GLN n 
1 211 ARG n 
1 212 LEU n 
1 213 VAL n 
1 214 PRO n 
1 215 LYS n 
1 216 ILE n 
1 217 ALA n 
1 218 THR n 
1 219 ARG n 
1 220 SER n 
1 221 GLN n 
1 222 VAL n 
1 223 ASN n 
1 224 GLY n 
1 225 LEU n 
1 226 ARG n 
1 227 GLY n 
1 228 ARG n 
1 229 MET n 
1 230 ASP n 
1 231 PHE n 
1 232 PHE n 
1 233 TRP n 
1 234 THR n 
1 235 ILE n 
1 236 LEU n 
1 237 LYS n 
1 238 PRO n 
1 239 ASN n 
1 240 ASP n 
1 241 ALA n 
1 242 ILE n 
1 243 HIS n 
1 244 PHE n 
1 245 GLU n 
1 246 SER n 
1 247 ASN n 
1 248 GLY n 
1 249 ASN n 
1 250 PHE n 
1 251 ILE n 
1 252 ALA n 
1 253 PRO n 
1 254 GLU n 
1 255 TYR n 
1 256 ALA n 
1 257 TYR n 
1 258 LYS n 
1 259 ILE n 
1 260 VAL n 
1 261 LYS n 
1 262 LYS n 
1 263 GLY n 
1 264 ASP n 
1 265 SER n 
1 266 THR n 
1 267 ILE n 
1 268 MET n 
1 269 LYS n 
1 270 SER n 
1 271 GLY n 
1 272 VAL n 
1 273 GLU n 
1 274 TYR n 
1 275 GLY n 
1 276 HIS n 
1 277 CYS n 
1 278 ASN n 
1 279 THR n 
1 280 LYS n 
1 281 CYS n 
1 282 GLN n 
1 283 THR n 
1 284 PRO n 
1 285 VAL n 
1 286 GLY n 
1 287 ALA n 
1 288 ILE n 
1 289 ASN n 
1 290 SER n 
1 291 SER n 
1 292 MET n 
1 293 PRO n 
1 294 PHE n 
1 295 HIS n 
1 296 ASN n 
1 297 ILE n 
1 298 HIS n 
1 299 PRO n 
1 300 LEU n 
1 301 THR n 
1 302 ILE n 
1 303 GLY n 
1 304 GLU n 
1 305 CYS n 
1 306 PRO n 
1 307 LYS n 
1 308 TYR n 
1 309 VAL n 
1 310 LYS n 
1 311 SER n 
1 312 ASN n 
1 313 LYS n 
1 314 LEU n 
1 315 VAL n 
1 316 LEU n 
1 317 ALA n 
1 318 THR n 
1 319 GLY n 
1 320 LEU n 
1 321 ARG n 
1 322 ASN n 
1 323 SER n 
1 324 PRO n 
1 325 GLN n 
1 326 ARG n 
1 327 GLU n 
1 328 THR 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 LYS 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 ARG 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 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 328 ? ? HA ? 'A/duck/France/161108h/2016(H5N8)' ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? 
? 'Spodoptera aff. frugiperda 1 BOLD-2017' 2449148 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 177 ? ? HA ? 'A/duck/France/161108h/2016(H5N8)' ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? 
? 'Spodoptera aff. frugiperda 1 BOLD-2017' 2449148 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
3 oligosaccharide 
4 oligosaccharide 
5 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 3 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                              
'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1'                                     WURCS 
PDB2Glycan 1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'                                               LINUCS 
PDB-CARE   ?     
4 4 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                                       
'Glycam Condensed Sequence' GMML       1.0   
5 4 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                                            WURCS 
PDB2Glycan 1.1.0 
6 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                                                                  LINUCS 
PDB-CARE   ?     
7 5 DNeup5Aca2-3DGalpb1-3DGlcpNAcb1-3DGalpb1-ROH                                                                     
'Glycam Condensed Sequence' GMML       1.0   
8 5 'WURCS=2.0/3,4,3/[a2112h-1b_1-5][a2122h-1b_1-5_2*NCC/3=O][Aad21122h-2a_2-6_5*NCC/3=O]/1-2-1-3/a3-b1_b3-c1_c3-d2' WURCS 
PDB2Glycan 1.1.0 
9 5 '[][b-D-Galp]{[(3+1)][b-D-GlcpNAc]{[(3+1)][b-D-Galp]{[(3+2)][a-D-Neup5Ac]{}}}}'                                  LINUCS 
PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
4 5 2 NAG C1 O1 1 GAL O3 HO3 sing ? 
5 5 3 GAL C1 O1 2 NAG O3 HO3 sing ? 
6 5 4 SIA C2 O2 3 GAL O3 HO3 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'           y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'           y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      
180.156 
CYS 'L-peptide linking'           y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GAL 'D-saccharide, beta linking'  . beta-D-galactopyranose                   'beta-D-galactose; D-galactose; galactose' 
'C6 H12 O6'      180.156 
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, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; 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 
SIA 'D-saccharide, alpha linking' . 'N-acetyl-alpha-neuraminic acid'         
'N-acetylneuraminic acid; sialic acid; alpha-sialic acid; O-SIALIC ACID' 'C11 H19 N O9'   309.270 
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 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
GAL 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGalpb                         
GAL 'COMMON NAME'                         GMML     1.0 b-D-galactopyranose            
GAL 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Galp                       
GAL 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Gal                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
SIA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DNeup5Aca                      
SIA 'COMMON NAME'                         GMML     1.0 'N-acetyl-a-D-neuraminic acid' 
SIA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Neup5Ac                    
SIA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Neu5Ac                         
# 
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   ASP 1   8   ?   ?   ?   A . n 
A 1 2   PRO 2   9   9   PRO PRO A . n 
A 1 3   GLY 3   10  10  GLY GLY A . n 
A 1 4   ASP 4   11  11  ASP ASP A . n 
A 1 5   GLN 5   12  12  GLN GLN A . n 
A 1 6   ILE 6   13  13  ILE ILE A . n 
A 1 7   CYS 7   14  14  CYS CYS A . n 
A 1 8   ILE 8   15  15  ILE ILE A . n 
A 1 9   GLY 9   16  16  GLY GLY A . n 
A 1 10  TYR 10  17  17  TYR TYR A . n 
A 1 11  HIS 11  18  18  HIS HIS A . n 
A 1 12  ALA 12  19  19  ALA ALA A . n 
A 1 13  ASN 13  20  20  ASN ASN A . n 
A 1 14  ASN 14  21  21  ASN ASN A . n 
A 1 15  SER 15  22  22  SER SER A . n 
A 1 16  THR 16  23  23  THR THR A . n 
A 1 17  GLU 17  24  24  GLU GLU A . n 
A 1 18  GLN 18  25  25  GLN GLN A . n 
A 1 19  VAL 19  26  26  VAL VAL A . n 
A 1 20  ASP 20  27  27  ASP ASP A . n 
A 1 21  THR 21  28  28  THR THR A . n 
A 1 22  ILE 22  29  29  ILE ILE A . n 
A 1 23  MET 23  30  30  MET MET A . n 
A 1 24  GLU 24  31  31  GLU GLU A . n 
A 1 25  LYS 25  32  32  LYS LYS A . n 
A 1 26  ASN 26  33  33  ASN ASN A . n 
A 1 27  VAL 27  34  34  VAL VAL A . n 
A 1 28  THR 28  35  35  THR THR A . n 
A 1 29  VAL 29  36  36  VAL VAL A . n 
A 1 30  THR 30  37  37  THR THR A . n 
A 1 31  HIS 31  38  38  HIS HIS A . n 
A 1 32  ALA 32  39  39  ALA ALA A . n 
A 1 33  GLN 33  40  40  GLN GLN A . n 
A 1 34  ASP 34  41  41  ASP ASP A . n 
A 1 35  ILE 35  42  42  ILE ILE A . n 
A 1 36  LEU 36  43  43  LEU LEU A . n 
A 1 37  GLU 37  44  44  GLU GLU A . n 
A 1 38  LYS 38  45  45  LYS LYS A . n 
A 1 39  THR 39  46  46  THR THR A . n 
A 1 40  HIS 40  47  47  HIS HIS A . n 
A 1 41  ASN 41  48  48  ASN ASN A . n 
A 1 42  GLY 42  49  49  GLY GLY A . n 
A 1 43  LYS 43  50  50  LYS LYS A . n 
A 1 44  LEU 44  51  51  LEU LEU A . n 
A 1 45  CYS 45  52  52  CYS CYS A . n 
A 1 46  ASP 46  53  53  ASP ASP A . n 
A 1 47  LEU 47  54  54  LEU LEU A . n 
A 1 48  ASN 48  55  55  ASN ASN A . n 
A 1 49  GLY 49  55  55  GLY GLY A A n 
A 1 50  VAL 50  56  56  VAL VAL A . n 
A 1 51  LYS 51  57  57  LYS LYS A . n 
A 1 52  PRO 52  58  58  PRO PRO A . n 
A 1 53  LEU 53  59  59  LEU LEU A . n 
A 1 54  ILE 54  60  60  ILE ILE A . n 
A 1 55  LEU 55  61  61  LEU LEU A . n 
A 1 56  LYS 56  62  62  LYS LYS A . n 
A 1 57  ASP 57  63  63  ASP ASP A . n 
A 1 58  CYS 58  64  64  CYS CYS A . n 
A 1 59  SER 59  65  65  SER SER A . n 
A 1 60  VAL 60  66  66  VAL VAL A . n 
A 1 61  ALA 61  67  67  ALA ALA A . n 
A 1 62  GLY 62  68  68  GLY GLY A . n 
A 1 63  TRP 63  69  69  TRP TRP A . n 
A 1 64  LEU 64  70  70  LEU LEU A . n 
A 1 65  LEU 65  71  71  LEU LEU A . n 
A 1 66  GLY 66  72  72  GLY GLY A . n 
A 1 67  ASN 67  73  73  ASN ASN A . n 
A 1 68  PRO 68  74  74  PRO PRO A . n 
A 1 69  MET 69  75  75  MET MET A . n 
A 1 70  CYS 70  76  76  CYS CYS A . n 
A 1 71  ASP 71  77  77  ASP ASP A . n 
A 1 72  GLU 72  78  78  GLU GLU A . n 
A 1 73  PHE 73  79  79  PHE PHE A . n 
A 1 74  ILE 74  80  80  ILE ILE A . n 
A 1 75  ARG 75  81  81  ARG ARG A . n 
A 1 76  VAL 76  82  82  VAL VAL A . n 
A 1 77  PRO 77  83  83  PRO PRO A . n 
A 1 78  GLU 78  83  83  GLU GLU A A n 
A 1 79  TRP 79  84  84  TRP TRP A . n 
A 1 80  SER 80  85  85  SER SER A . n 
A 1 81  TYR 81  86  86  TYR TYR A . n 
A 1 82  ILE 82  87  87  ILE ILE A . n 
A 1 83  VAL 83  88  88  VAL VAL A . n 
A 1 84  GLU 84  89  89  GLU GLU A . n 
A 1 85  ARG 85  90  90  ARG ARG A . n 
A 1 86  ALA 86  91  91  ALA ALA A . n 
A 1 87  ASN 87  92  92  ASN ASN A . n 
A 1 88  PRO 88  93  93  PRO PRO A . n 
A 1 89  ALA 89  94  94  ALA ALA A . n 
A 1 90  ASN 90  95  95  ASN ASN A . n 
A 1 91  ASP 91  96  96  ASP ASP A . n 
A 1 92  LEU 92  96  96  LEU LEU A A n 
A 1 93  CYS 93  97  97  CYS CYS A . n 
A 1 94  TYR 94  98  98  TYR TYR A . n 
A 1 95  PRO 95  99  99  PRO PRO A . n 
A 1 96  GLY 96  100 100 GLY GLY A . n 
A 1 97  SER 97  101 101 SER SER A . n 
A 1 98  LEU 98  102 102 LEU LEU A . n 
A 1 99  ASN 99  103 103 ASN ASN A . n 
A 1 100 ASP 100 104 104 ASP ASP A . n 
A 1 101 TYR 101 105 105 TYR TYR A . n 
A 1 102 GLU 102 106 106 GLU GLU A . n 
A 1 103 GLU 103 107 107 GLU GLU A . n 
A 1 104 LEU 104 108 108 LEU LEU A . n 
A 1 105 LYS 105 109 109 LYS LYS A . n 
A 1 106 HIS 106 110 110 HIS HIS A . n 
A 1 107 LEU 107 111 111 LEU LEU A . n 
A 1 108 LEU 108 112 112 LEU LEU A . n 
A 1 109 SER 109 113 113 SER SER A . n 
A 1 110 ARG 110 114 114 ARG ARG A . n 
A 1 111 ILE 111 115 115 ILE ILE A . n 
A 1 112 ASN 112 116 116 ASN ASN A . n 
A 1 113 HIS 113 117 117 HIS HIS A . n 
A 1 114 PHE 114 118 118 PHE PHE A . n 
A 1 115 GLU 115 119 119 GLU GLU A . n 
A 1 116 LYS 116 120 120 LYS LYS A . n 
A 1 117 ILE 117 121 121 ILE ILE A . n 
A 1 118 LEU 118 122 122 LEU LEU A . n 
A 1 119 ILE 119 123 123 ILE ILE A . n 
A 1 120 ILE 120 124 124 ILE ILE A . n 
A 1 121 PRO 121 125 125 PRO PRO A . n 
A 1 122 LYS 122 125 125 LYS LYS A A n 
A 1 123 SER 123 125 125 SER SER A B n 
A 1 124 SER 124 126 126 SER SER A . n 
A 1 125 TRP 125 127 127 TRP TRP A . n 
A 1 126 PRO 126 128 128 PRO PRO A . n 
A 1 127 ASN 127 129 129 ASN ASN A . n 
A 1 128 HIS 128 130 130 HIS HIS A . n 
A 1 129 GLU 129 131 131 GLU GLU A . n 
A 1 130 THR 130 132 132 THR THR A . n 
A 1 131 SER 131 133 133 SER SER A . n 
A 1 132 LEU 132 133 133 LEU LEU A A n 
A 1 133 GLY 133 134 134 GLY GLY A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 SER 135 136 136 SER SER A . n 
A 1 136 ALA 136 137 137 ALA ALA A . n 
A 1 137 ALA 137 138 138 ALA ALA A . n 
A 1 138 CYS 138 139 139 CYS CYS A . n 
A 1 139 PRO 139 140 140 PRO PRO A . n 
A 1 140 TYR 140 141 141 TYR TYR A . n 
A 1 141 GLN 141 142 142 GLN GLN A . n 
A 1 142 GLY 142 143 143 GLY GLY A . n 
A 1 143 THR 143 144 144 THR THR A . n 
A 1 144 PRO 144 145 145 PRO PRO A . n 
A 1 145 SER 145 146 146 SER SER A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 PHE 147 148 148 PHE PHE A . n 
A 1 148 ARG 148 149 149 ARG ARG A . n 
A 1 149 ASN 149 150 150 ASN ASN A . n 
A 1 150 VAL 150 151 151 VAL VAL A . n 
A 1 151 VAL 151 152 152 VAL VAL A . n 
A 1 152 TRP 152 153 153 TRP TRP A . n 
A 1 153 LEU 153 154 154 LEU LEU A . n 
A 1 154 ILE 154 155 155 ILE ILE A . n 
A 1 155 LYS 155 156 156 LYS LYS A . n 
A 1 156 LYS 156 157 157 LYS LYS A . n 
A 1 157 ASN 157 158 158 ASN ASN A . n 
A 1 158 ASP 158 159 159 ASP ASP A . n 
A 1 159 ALA 159 160 160 ALA ALA A . n 
A 1 160 TYR 160 161 161 TYR TYR A . n 
A 1 161 PRO 161 162 162 PRO PRO A . n 
A 1 162 THR 162 163 163 THR THR A . n 
A 1 163 ILE 163 164 164 ILE ILE A . n 
A 1 164 LYS 164 165 165 LYS LYS A . n 
A 1 165 ILE 165 166 166 ILE ILE A . n 
A 1 166 SER 166 167 167 SER SER A . n 
A 1 167 TYR 167 168 168 TYR TYR A . n 
A 1 168 ASN 168 169 169 ASN ASN A . n 
A 1 169 ASN 169 170 170 ASN ASN A . n 
A 1 170 THR 170 171 171 THR THR A . n 
A 1 171 ASN 171 172 172 ASN ASN A . n 
A 1 172 ARG 172 173 173 ARG ARG A . n 
A 1 173 GLU 173 174 174 GLU GLU A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 LEU 175 176 176 LEU LEU A . n 
A 1 176 LEU 176 177 177 LEU LEU A . n 
A 1 177 ILE 177 178 178 ILE ILE A . n 
A 1 178 LEU 178 179 179 LEU LEU A . n 
A 1 179 TRP 179 180 180 TRP TRP A . n 
A 1 180 GLY 180 181 181 GLY GLY A . n 
A 1 181 ILE 181 182 182 ILE ILE A . n 
A 1 182 HIS 182 183 183 HIS HIS A . n 
A 1 183 HIS 183 184 184 HIS HIS A . n 
A 1 184 SER 184 185 185 SER SER A . n 
A 1 185 ASN 185 186 186 ASN ASN A . n 
A 1 186 ASN 186 187 187 ASN ASN A . n 
A 1 187 ALA 187 188 188 ALA ALA A . n 
A 1 188 GLU 188 189 189 GLU GLU A . n 
A 1 189 GLU 189 190 190 GLU GLU A . n 
A 1 190 GLN 190 191 191 GLN GLN A . n 
A 1 191 THR 191 192 192 THR THR A . n 
A 1 192 ASN 192 193 193 ASN ASN A . n 
A 1 193 LEU 193 194 194 LEU LEU A . n 
A 1 194 TYR 194 195 195 TYR TYR A . n 
A 1 195 LYS 195 196 196 LYS LYS A . n 
A 1 196 ASN 196 197 197 ASN ASN A . n 
A 1 197 PRO 197 198 198 PRO PRO A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 TYR 200 201 201 TYR TYR A . n 
A 1 201 ILE 201 202 202 ILE ILE A . n 
A 1 202 SER 202 203 203 SER SER A . n 
A 1 203 VAL 203 204 204 VAL VAL A . n 
A 1 204 GLY 204 205 205 GLY GLY A . n 
A 1 205 THR 205 206 206 THR THR A . n 
A 1 206 SER 206 207 207 SER SER A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 LEU 208 209 209 LEU LEU A . n 
A 1 209 ASN 209 210 210 ASN ASN A . n 
A 1 210 GLN 210 211 211 GLN GLN A . n 
A 1 211 ARG 211 212 212 ARG ARG A . n 
A 1 212 LEU 212 213 213 LEU LEU A . n 
A 1 213 VAL 213 214 214 VAL VAL A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 LYS 215 216 216 LYS LYS A . n 
A 1 216 ILE 216 217 217 ILE ILE A . n 
A 1 217 ALA 217 218 218 ALA ALA A . n 
A 1 218 THR 218 219 219 THR THR A . n 
A 1 219 ARG 219 220 220 ARG ARG A . n 
A 1 220 SER 220 221 221 SER SER A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 ASN 223 224 224 ASN ASN A . n 
A 1 224 GLY 224 225 225 GLY GLY A . n 
A 1 225 LEU 225 226 226 LEU LEU A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 GLY 227 228 228 GLY GLY A . n 
A 1 228 ARG 228 229 229 ARG ARG A . n 
A 1 229 MET 229 230 230 MET MET A . n 
A 1 230 ASP 230 231 231 ASP ASP A . n 
A 1 231 PHE 231 232 232 PHE PHE A . n 
A 1 232 PHE 232 233 233 PHE PHE A . n 
A 1 233 TRP 233 234 234 TRP TRP A . n 
A 1 234 THR 234 235 235 THR THR A . n 
A 1 235 ILE 235 236 236 ILE ILE A . n 
A 1 236 LEU 236 237 237 LEU LEU A . n 
A 1 237 LYS 237 238 238 LYS LYS A . n 
A 1 238 PRO 238 239 239 PRO PRO A . n 
A 1 239 ASN 239 240 240 ASN ASN A . n 
A 1 240 ASP 240 241 241 ASP ASP A . n 
A 1 241 ALA 241 242 242 ALA ALA A . n 
A 1 242 ILE 242 243 243 ILE ILE A . n 
A 1 243 HIS 243 244 244 HIS HIS A . n 
A 1 244 PHE 244 245 245 PHE PHE A . n 
A 1 245 GLU 245 246 246 GLU GLU A . n 
A 1 246 SER 246 247 247 SER SER A . n 
A 1 247 ASN 247 248 248 ASN ASN A . n 
A 1 248 GLY 248 249 249 GLY GLY A . n 
A 1 249 ASN 249 250 250 ASN ASN A . n 
A 1 250 PHE 250 251 251 PHE PHE A . n 
A 1 251 ILE 251 252 252 ILE ILE A . n 
A 1 252 ALA 252 253 253 ALA ALA A . n 
A 1 253 PRO 253 254 254 PRO PRO A . n 
A 1 254 GLU 254 255 255 GLU GLU A . n 
A 1 255 TYR 255 256 256 TYR TYR A . n 
A 1 256 ALA 256 257 257 ALA ALA A . n 
A 1 257 TYR 257 258 258 TYR TYR A . n 
A 1 258 LYS 258 259 259 LYS LYS A . n 
A 1 259 ILE 259 260 260 ILE ILE A . n 
A 1 260 VAL 260 260 260 VAL VAL A A n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 LYS 262 262 262 LYS LYS A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 MET 268 268 268 MET MET A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 TYR 274 274 274 TYR TYR A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 HIS 276 276 276 HIS HIS A . n 
A 1 277 CYS 277 277 277 CYS CYS A . n 
A 1 278 ASN 278 278 278 ASN ASN A . n 
A 1 279 THR 279 279 279 THR THR A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 CYS 281 281 281 CYS CYS A . n 
A 1 282 GLN 282 282 282 GLN GLN A . n 
A 1 283 THR 283 283 283 THR THR A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 GLY 286 286 286 GLY GLY A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 SER 291 291 291 SER SER A . n 
A 1 292 MET 292 292 292 MET MET A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 HIS 295 295 295 HIS HIS A . n 
A 1 296 ASN 296 296 296 ASN ASN A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 HIS 298 298 298 HIS HIS A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 THR 301 301 301 THR THR A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 GLY 303 303 303 GLY GLY A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 CYS 305 305 305 CYS CYS A . n 
A 1 306 PRO 306 306 306 PRO PRO A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 TYR 308 308 308 TYR TYR A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ASN 312 312 312 ASN ASN A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 VAL 315 315 315 VAL VAL A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 ALA 317 317 317 ALA ALA A . n 
A 1 318 THR 318 318 318 THR THR A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 ARG 321 321 321 ARG ARG A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 PRO 324 324 ?   ?   ?   A . n 
A 1 325 GLN 325 325 ?   ?   ?   A . n 
A 1 326 ARG 326 326 ?   ?   ?   A . n 
A 1 327 GLU 327 327 ?   ?   ?   A . n 
A 1 328 THR 328 328 ?   ?   ?   A . n 
B 2 1   GLY 1   1   ?   ?   ?   B . n 
B 2 2   LEU 2   2   ?   ?   ?   B . n 
B 2 3   PHE 3   3   ?   ?   ?   B . n 
B 2 4   GLY 4   4   ?   ?   ?   B . n 
B 2 5   ALA 5   5   ?   ?   ?   B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  ILE 10  10  10  ILE ILE B . n 
B 2 11  GLU 11  11  11  GLU GLU B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  TRP 14  14  14  TRP TRP B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  MET 17  17  17  MET MET B . n 
B 2 18  VAL 18  18  18  VAL VAL B . n 
B 2 19  ASP 19  19  19  ASP ASP B . n 
B 2 20  GLY 20  20  20  GLY GLY B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  TYR 22  22  22  TYR TYR B . n 
B 2 23  GLY 23  23  23  GLY GLY B . n 
B 2 24  TYR 24  24  24  TYR TYR B . n 
B 2 25  HIS 25  25  25  HIS HIS B . n 
B 2 26  HIS 26  26  26  HIS HIS B . n 
B 2 27  SER 27  27  27  SER SER B . n 
B 2 28  ASN 28  28  28  ASN ASN B . n 
B 2 29  GLU 29  29  29  GLU GLU B . n 
B 2 30  GLN 30  30  30  GLN GLN B . n 
B 2 31  GLY 31  31  31  GLY GLY B . n 
B 2 32  SER 32  32  32  SER SER B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  TYR 34  34  34  TYR TYR B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  ASP 37  37  37  ASP ASP B . n 
B 2 38  LYS 38  38  38  LYS LYS B . n 
B 2 39  GLU 39  39  39  GLU GLU B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  THR 41  41  41  THR THR B . n 
B 2 42  GLN 42  42  42  GLN GLN B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  ALA 44  44  44  ALA ALA B . n 
B 2 45  ILE 45  45  45  ILE ILE B . n 
B 2 46  ASP 46  46  46  ASP ASP B . n 
B 2 47  GLY 47  47  47  GLY GLY B . n 
B 2 48  VAL 48  48  48  VAL VAL B . n 
B 2 49  THR 49  49  49  THR THR B . n 
B 2 50  ASN 50  50  50  ASN ASN B . n 
B 2 51  LYS 51  51  51  LYS LYS B . n 
B 2 52  VAL 52  52  52  VAL VAL B . n 
B 2 53  ASN 53  53  53  ASN ASN B . n 
B 2 54  SER 54  54  54  SER SER B . n 
B 2 55  ILE 55  55  55  ILE ILE B . n 
B 2 56  ILE 56  56  56  ILE ILE B . n 
B 2 57  ASP 57  57  57  ASP ASP B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  MET 59  59  59  MET MET B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  THR 61  61  61  THR THR B . n 
B 2 62  GLN 62  62  62  GLN GLN B . n 
B 2 63  PHE 63  63  63  PHE PHE B . n 
B 2 64  GLU 64  64  64  GLU GLU B . n 
B 2 65  ALA 65  65  65  ALA ALA B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  ARG 68  68  68  ARG ARG B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PHE 70  70  70  PHE PHE B . n 
B 2 71  ASN 71  71  71  ASN ASN B . n 
B 2 72  ASN 72  72  72  ASN ASN B . n 
B 2 73  LEU 73  73  73  LEU LEU B . n 
B 2 74  GLU 74  74  74  GLU GLU B . n 
B 2 75  ARG 75  75  75  ARG ARG B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  ASN 81  81  81  ASN ASN B . n 
B 2 82  LYS 82  82  82  LYS LYS B . n 
B 2 83  LYS 83  83  83  LYS LYS B . n 
B 2 84  MET 84  84  84  MET MET B . n 
B 2 85  GLU 85  85  85  GLU GLU B . n 
B 2 86  ASP 86  86  86  ASP ASP B . n 
B 2 87  GLY 87  87  87  GLY GLY B . n 
B 2 88  PHE 88  88  88  PHE PHE B . n 
B 2 89  LEU 89  89  89  LEU LEU B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  TRP 92  92  92  TRP TRP B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  ASN 95  95  95  ASN ASN B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  GLU 97  97  97  GLU GLU B . n 
B 2 98  LEU 98  98  98  LEU LEU B . n 
B 2 99  LEU 99  99  99  LEU LEU B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 LEU 101 101 101 LEU LEU B . n 
B 2 102 MET 102 102 102 MET MET B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 ASN 104 104 104 ASN ASN B . n 
B 2 105 GLU 105 105 105 GLU GLU B . n 
B 2 106 ARG 106 106 106 ARG ARG B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 ASP 109 109 109 ASP ASP B . n 
B 2 110 PHE 110 110 110 PHE PHE B . n 
B 2 111 HIS 111 111 111 HIS HIS B . n 
B 2 112 ASP 112 112 112 ASP ASP B . n 
B 2 113 SER 113 113 113 SER SER B . n 
B 2 114 ASN 114 114 114 ASN ASN B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 ASN 117 117 117 ASN ASN B . n 
B 2 118 LEU 118 118 118 LEU LEU B . n 
B 2 119 TYR 119 119 119 TYR TYR B . n 
B 2 120 ASP 120 120 120 ASP ASP B . n 
B 2 121 LYS 121 121 121 LYS LYS B . n 
B 2 122 VAL 122 122 122 VAL VAL B . n 
B 2 123 ARG 123 123 123 ARG ARG B . n 
B 2 124 LEU 124 124 124 LEU LEU B . n 
B 2 125 GLN 125 125 125 GLN GLN B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 ARG 127 127 127 ARG ARG B . n 
B 2 128 ASP 128 128 128 ASP ASP B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 ALA 130 130 130 ALA ALA B . n 
B 2 131 LYS 131 131 131 LYS LYS B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 LEU 133 133 133 LEU LEU B . n 
B 2 134 GLY 134 134 134 GLY GLY B . n 
B 2 135 ASN 135 135 135 ASN ASN B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 CYS 137 137 137 CYS CYS B . n 
B 2 138 PHE 138 138 138 PHE PHE B . n 
B 2 139 GLU 139 139 139 GLU GLU B . n 
B 2 140 PHE 140 140 140 PHE PHE B . n 
B 2 141 TYR 141 141 141 TYR TYR B . n 
B 2 142 HIS 142 142 142 HIS HIS B . n 
B 2 143 LYS 143 143 143 LYS LYS B . n 
B 2 144 CYS 144 144 144 CYS CYS B . n 
B 2 145 ASP 145 145 145 ASP ASP B . n 
B 2 146 ASN 146 146 146 ASN ASN B . n 
B 2 147 GLU 147 147 147 GLU GLU B . n 
B 2 148 CYS 148 148 148 CYS CYS B . n 
B 2 149 MET 149 149 149 MET MET B . n 
B 2 150 GLU 150 150 150 GLU GLU B . n 
B 2 151 SER 151 151 151 SER SER B . n 
B 2 152 VAL 152 152 152 VAL VAL B . n 
B 2 153 ARG 153 153 153 ARG ARG B . n 
B 2 154 ASN 154 154 154 ASN ASN B . n 
B 2 155 GLY 155 155 155 GLY GLY B . n 
B 2 156 THR 156 156 156 THR THR B . n 
B 2 157 TYR 157 157 157 TYR TYR B . n 
B 2 158 ASP 158 158 158 ASP ASP B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 PRO 160 160 160 PRO PRO B . n 
B 2 161 GLN 161 161 161 GLN GLN B . n 
B 2 162 TYR 162 162 162 TYR TYR B . n 
B 2 163 SER 163 163 163 SER SER B . n 
B 2 164 GLU 164 164 164 GLU GLU B . n 
B 2 165 GLU 165 165 165 GLU GLU B . n 
B 2 166 ALA 166 166 166 ALA ALA B . n 
B 2 167 ARG 167 167 167 ARG ARG B . n 
B 2 168 LEU 168 168 168 LEU LEU B . n 
B 2 169 LYS 169 169 169 LYS LYS B . n 
B 2 170 ARG 170 170 170 ARG ARG B . n 
B 2 171 GLU 171 171 171 GLU GLU B . n 
B 2 172 GLU 172 172 172 GLU GLU B . n 
B 2 173 ILE 173 173 173 ILE ILE B . n 
B 2 174 SER 174 174 174 SER SER B . n 
B 2 175 SER 175 175 ?   ?   ?   B . n 
B 2 176 GLY 176 176 ?   ?   ?   B . n 
B 2 177 ARG 177 177 ?   ?   ?   B . n 
C 1 1   ASP 1   8   8   ASP ASP C . n 
C 1 2   PRO 2   9   9   PRO PRO C . n 
C 1 3   GLY 3   10  10  GLY GLY C . n 
C 1 4   ASP 4   11  11  ASP ASP C . n 
C 1 5   GLN 5   12  12  GLN GLN C . n 
C 1 6   ILE 6   13  13  ILE ILE C . n 
C 1 7   CYS 7   14  14  CYS CYS C . n 
C 1 8   ILE 8   15  15  ILE ILE C . n 
C 1 9   GLY 9   16  16  GLY GLY C . n 
C 1 10  TYR 10  17  17  TYR TYR C . n 
C 1 11  HIS 11  18  18  HIS HIS C . n 
C 1 12  ALA 12  19  19  ALA ALA C . n 
C 1 13  ASN 13  20  20  ASN ASN C . n 
C 1 14  ASN 14  21  21  ASN ASN C . n 
C 1 15  SER 15  22  22  SER SER C . n 
C 1 16  THR 16  23  23  THR THR C . n 
C 1 17  GLU 17  24  24  GLU GLU C . n 
C 1 18  GLN 18  25  25  GLN GLN C . n 
C 1 19  VAL 19  26  26  VAL VAL C . n 
C 1 20  ASP 20  27  27  ASP ASP C . n 
C 1 21  THR 21  28  28  THR THR C . n 
C 1 22  ILE 22  29  29  ILE ILE C . n 
C 1 23  MET 23  30  30  MET MET C . n 
C 1 24  GLU 24  31  31  GLU GLU C . n 
C 1 25  LYS 25  32  32  LYS LYS C . n 
C 1 26  ASN 26  33  33  ASN ASN C . n 
C 1 27  VAL 27  34  34  VAL VAL C . n 
C 1 28  THR 28  35  35  THR THR C . n 
C 1 29  VAL 29  36  36  VAL VAL C . n 
C 1 30  THR 30  37  37  THR THR C . n 
C 1 31  HIS 31  38  38  HIS HIS C . n 
C 1 32  ALA 32  39  39  ALA ALA C . n 
C 1 33  GLN 33  40  40  GLN GLN C . n 
C 1 34  ASP 34  41  41  ASP ASP C . n 
C 1 35  ILE 35  42  42  ILE ILE C . n 
C 1 36  LEU 36  43  43  LEU LEU C . n 
C 1 37  GLU 37  44  44  GLU GLU C . n 
C 1 38  LYS 38  45  45  LYS LYS C . n 
C 1 39  THR 39  46  46  THR THR C . n 
C 1 40  HIS 40  47  47  HIS HIS C . n 
C 1 41  ASN 41  48  48  ASN ASN C . n 
C 1 42  GLY 42  49  49  GLY GLY C . n 
C 1 43  LYS 43  50  50  LYS LYS C . n 
C 1 44  LEU 44  51  51  LEU LEU C . n 
C 1 45  CYS 45  52  52  CYS CYS C . n 
C 1 46  ASP 46  53  53  ASP ASP C . n 
C 1 47  LEU 47  54  54  LEU LEU C . n 
C 1 48  ASN 48  55  55  ASN ASN C . n 
C 1 49  GLY 49  55  55  GLY GLY C A n 
C 1 50  VAL 50  56  56  VAL VAL C . n 
C 1 51  LYS 51  57  57  LYS LYS C . n 
C 1 52  PRO 52  58  58  PRO PRO C . n 
C 1 53  LEU 53  59  59  LEU LEU C . n 
C 1 54  ILE 54  60  60  ILE ILE C . n 
C 1 55  LEU 55  61  61  LEU LEU C . n 
C 1 56  LYS 56  62  62  LYS LYS C . n 
C 1 57  ASP 57  63  63  ASP ASP C . n 
C 1 58  CYS 58  64  64  CYS CYS C . n 
C 1 59  SER 59  65  65  SER SER C . n 
C 1 60  VAL 60  66  66  VAL VAL C . n 
C 1 61  ALA 61  67  67  ALA ALA C . n 
C 1 62  GLY 62  68  68  GLY GLY C . n 
C 1 63  TRP 63  69  69  TRP TRP C . n 
C 1 64  LEU 64  70  70  LEU LEU C . n 
C 1 65  LEU 65  71  71  LEU LEU C . n 
C 1 66  GLY 66  72  72  GLY GLY C . n 
C 1 67  ASN 67  73  73  ASN ASN C . n 
C 1 68  PRO 68  74  74  PRO PRO C . n 
C 1 69  MET 69  75  75  MET MET C . n 
C 1 70  CYS 70  76  76  CYS CYS C . n 
C 1 71  ASP 71  77  77  ASP ASP C . n 
C 1 72  GLU 72  78  78  GLU GLU C . n 
C 1 73  PHE 73  79  79  PHE PHE C . n 
C 1 74  ILE 74  80  80  ILE ILE C . n 
C 1 75  ARG 75  81  81  ARG ARG C . n 
C 1 76  VAL 76  82  82  VAL VAL C . n 
C 1 77  PRO 77  83  83  PRO PRO C . n 
C 1 78  GLU 78  83  83  GLU GLU C A n 
C 1 79  TRP 79  84  84  TRP TRP C . n 
C 1 80  SER 80  85  85  SER SER C . n 
C 1 81  TYR 81  86  86  TYR TYR C . n 
C 1 82  ILE 82  87  87  ILE ILE C . n 
C 1 83  VAL 83  88  88  VAL VAL C . n 
C 1 84  GLU 84  89  89  GLU GLU C . n 
C 1 85  ARG 85  90  90  ARG ARG C . n 
C 1 86  ALA 86  91  91  ALA ALA C . n 
C 1 87  ASN 87  92  92  ASN ASN C . n 
C 1 88  PRO 88  93  93  PRO PRO C . n 
C 1 89  ALA 89  94  94  ALA ALA C . n 
C 1 90  ASN 90  95  95  ASN ASN C . n 
C 1 91  ASP 91  96  96  ASP ASP C . n 
C 1 92  LEU 92  96  96  LEU LEU C A n 
C 1 93  CYS 93  97  97  CYS CYS C . n 
C 1 94  TYR 94  98  98  TYR TYR C . n 
C 1 95  PRO 95  99  99  PRO PRO C . n 
C 1 96  GLY 96  100 100 GLY GLY C . n 
C 1 97  SER 97  101 101 SER SER C . n 
C 1 98  LEU 98  102 102 LEU LEU C . n 
C 1 99  ASN 99  103 103 ASN ASN C . n 
C 1 100 ASP 100 104 104 ASP ASP C . n 
C 1 101 TYR 101 105 105 TYR TYR C . n 
C 1 102 GLU 102 106 106 GLU GLU C . n 
C 1 103 GLU 103 107 107 GLU GLU C . n 
C 1 104 LEU 104 108 108 LEU LEU C . n 
C 1 105 LYS 105 109 109 LYS LYS C . n 
C 1 106 HIS 106 110 110 HIS HIS C . n 
C 1 107 LEU 107 111 111 LEU LEU C . n 
C 1 108 LEU 108 112 112 LEU LEU C . n 
C 1 109 SER 109 113 113 SER SER C . n 
C 1 110 ARG 110 114 114 ARG ARG C . n 
C 1 111 ILE 111 115 115 ILE ILE C . n 
C 1 112 ASN 112 116 116 ASN ASN C . n 
C 1 113 HIS 113 117 117 HIS HIS C . n 
C 1 114 PHE 114 118 118 PHE PHE C . n 
C 1 115 GLU 115 119 119 GLU GLU C . n 
C 1 116 LYS 116 120 120 LYS LYS C . n 
C 1 117 ILE 117 121 121 ILE ILE C . n 
C 1 118 LEU 118 122 122 LEU LEU C . n 
C 1 119 ILE 119 123 123 ILE ILE C . n 
C 1 120 ILE 120 124 124 ILE ILE C . n 
C 1 121 PRO 121 125 125 PRO PRO C . n 
C 1 122 LYS 122 125 125 LYS LYS C A n 
C 1 123 SER 123 125 125 SER SER C B n 
C 1 124 SER 124 126 126 SER SER C . n 
C 1 125 TRP 125 127 127 TRP TRP C . n 
C 1 126 PRO 126 128 128 PRO PRO C . n 
C 1 127 ASN 127 129 129 ASN ASN C . n 
C 1 128 HIS 128 130 130 HIS HIS C . n 
C 1 129 GLU 129 131 131 GLU GLU C . n 
C 1 130 THR 130 132 132 THR THR C . n 
C 1 131 SER 131 133 133 SER SER C . n 
C 1 132 LEU 132 133 133 LEU LEU C A n 
C 1 133 GLY 133 134 134 GLY GLY C . n 
C 1 134 VAL 134 135 135 VAL VAL C . n 
C 1 135 SER 135 136 136 SER SER C . n 
C 1 136 ALA 136 137 137 ALA ALA C . n 
C 1 137 ALA 137 138 138 ALA ALA C . n 
C 1 138 CYS 138 139 139 CYS CYS C . n 
C 1 139 PRO 139 140 140 PRO PRO C . n 
C 1 140 TYR 140 141 141 TYR TYR C . n 
C 1 141 GLN 141 142 142 GLN GLN C . n 
C 1 142 GLY 142 143 143 GLY GLY C . n 
C 1 143 THR 143 144 144 THR THR C . n 
C 1 144 PRO 144 145 145 PRO PRO C . n 
C 1 145 SER 145 146 146 SER SER C . n 
C 1 146 PHE 146 147 147 PHE PHE C . n 
C 1 147 PHE 147 148 148 PHE PHE C . n 
C 1 148 ARG 148 149 149 ARG ARG C . n 
C 1 149 ASN 149 150 150 ASN ASN C . n 
C 1 150 VAL 150 151 151 VAL VAL C . n 
C 1 151 VAL 151 152 152 VAL VAL C . n 
C 1 152 TRP 152 153 153 TRP TRP C . n 
C 1 153 LEU 153 154 154 LEU LEU C . n 
C 1 154 ILE 154 155 155 ILE ILE C . n 
C 1 155 LYS 155 156 156 LYS LYS C . n 
C 1 156 LYS 156 157 157 LYS LYS C . n 
C 1 157 ASN 157 158 158 ASN ASN C . n 
C 1 158 ASP 158 159 159 ASP ASP C . n 
C 1 159 ALA 159 160 160 ALA ALA C . n 
C 1 160 TYR 160 161 161 TYR TYR C . n 
C 1 161 PRO 161 162 162 PRO PRO C . n 
C 1 162 THR 162 163 163 THR THR C . n 
C 1 163 ILE 163 164 164 ILE ILE C . n 
C 1 164 LYS 164 165 165 LYS LYS C . n 
C 1 165 ILE 165 166 166 ILE ILE C . n 
C 1 166 SER 166 167 167 SER SER C . n 
C 1 167 TYR 167 168 168 TYR TYR C . n 
C 1 168 ASN 168 169 169 ASN ASN C . n 
C 1 169 ASN 169 170 170 ASN ASN C . n 
C 1 170 THR 170 171 171 THR THR C . n 
C 1 171 ASN 171 172 172 ASN ASN C . n 
C 1 172 ARG 172 173 173 ARG ARG C . n 
C 1 173 GLU 173 174 174 GLU GLU C . n 
C 1 174 ASP 174 175 175 ASP ASP C . n 
C 1 175 LEU 175 176 176 LEU LEU C . n 
C 1 176 LEU 176 177 177 LEU LEU C . n 
C 1 177 ILE 177 178 178 ILE ILE C . n 
C 1 178 LEU 178 179 179 LEU LEU C . n 
C 1 179 TRP 179 180 180 TRP TRP C . n 
C 1 180 GLY 180 181 181 GLY GLY C . n 
C 1 181 ILE 181 182 182 ILE ILE C . n 
C 1 182 HIS 182 183 183 HIS HIS C . n 
C 1 183 HIS 183 184 184 HIS HIS C . n 
C 1 184 SER 184 185 185 SER SER C . n 
C 1 185 ASN 185 186 186 ASN ASN C . n 
C 1 186 ASN 186 187 187 ASN ASN C . n 
C 1 187 ALA 187 188 188 ALA ALA C . n 
C 1 188 GLU 188 189 189 GLU GLU C . n 
C 1 189 GLU 189 190 190 GLU GLU C . n 
C 1 190 GLN 190 191 191 GLN GLN C . n 
C 1 191 THR 191 192 192 THR THR C . n 
C 1 192 ASN 192 193 193 ASN ASN C . n 
C 1 193 LEU 193 194 194 LEU LEU C . n 
C 1 194 TYR 194 195 195 TYR TYR C . n 
C 1 195 LYS 195 196 196 LYS LYS C . n 
C 1 196 ASN 196 197 197 ASN ASN C . n 
C 1 197 PRO 197 198 198 PRO PRO C . n 
C 1 198 THR 198 199 199 THR THR C . n 
C 1 199 THR 199 200 200 THR THR C . n 
C 1 200 TYR 200 201 201 TYR TYR C . n 
C 1 201 ILE 201 202 202 ILE ILE C . n 
C 1 202 SER 202 203 203 SER SER C . n 
C 1 203 VAL 203 204 204 VAL VAL C . n 
C 1 204 GLY 204 205 205 GLY GLY C . n 
C 1 205 THR 205 206 206 THR THR C . n 
C 1 206 SER 206 207 207 SER SER C . n 
C 1 207 THR 207 208 208 THR THR C . n 
C 1 208 LEU 208 209 209 LEU LEU C . n 
C 1 209 ASN 209 210 210 ASN ASN C . n 
C 1 210 GLN 210 211 211 GLN GLN C . n 
C 1 211 ARG 211 212 212 ARG ARG C . n 
C 1 212 LEU 212 213 213 LEU LEU C . n 
C 1 213 VAL 213 214 214 VAL VAL C . n 
C 1 214 PRO 214 215 215 PRO PRO C . n 
C 1 215 LYS 215 216 216 LYS LYS C . n 
C 1 216 ILE 216 217 217 ILE ILE C . n 
C 1 217 ALA 217 218 218 ALA ALA C . n 
C 1 218 THR 218 219 219 THR THR C . n 
C 1 219 ARG 219 220 220 ARG ARG C . n 
C 1 220 SER 220 221 221 SER SER C . n 
C 1 221 GLN 221 222 222 GLN GLN C . n 
C 1 222 VAL 222 223 223 VAL VAL C . n 
C 1 223 ASN 223 224 224 ASN ASN C . n 
C 1 224 GLY 224 225 225 GLY GLY C . n 
C 1 225 LEU 225 226 226 LEU LEU C . n 
C 1 226 ARG 226 227 227 ARG ARG C . n 
C 1 227 GLY 227 228 228 GLY GLY C . n 
C 1 228 ARG 228 229 229 ARG ARG C . n 
C 1 229 MET 229 230 230 MET MET C . n 
C 1 230 ASP 230 231 231 ASP ASP C . n 
C 1 231 PHE 231 232 232 PHE PHE C . n 
C 1 232 PHE 232 233 233 PHE PHE C . n 
C 1 233 TRP 233 234 234 TRP TRP C . n 
C 1 234 THR 234 235 235 THR THR C . n 
C 1 235 ILE 235 236 236 ILE ILE C . n 
C 1 236 LEU 236 237 237 LEU LEU C . n 
C 1 237 LYS 237 238 238 LYS LYS C . n 
C 1 238 PRO 238 239 239 PRO PRO C . n 
C 1 239 ASN 239 240 240 ASN ASN C . n 
C 1 240 ASP 240 241 241 ASP ASP C . n 
C 1 241 ALA 241 242 242 ALA ALA C . n 
C 1 242 ILE 242 243 243 ILE ILE C . n 
C 1 243 HIS 243 244 244 HIS HIS C . n 
C 1 244 PHE 244 245 245 PHE PHE C . n 
C 1 245 GLU 245 246 246 GLU GLU C . n 
C 1 246 SER 246 247 247 SER SER C . n 
C 1 247 ASN 247 248 248 ASN ASN C . n 
C 1 248 GLY 248 249 249 GLY GLY C . n 
C 1 249 ASN 249 250 250 ASN ASN C . n 
C 1 250 PHE 250 251 251 PHE PHE C . n 
C 1 251 ILE 251 252 252 ILE ILE C . n 
C 1 252 ALA 252 253 253 ALA ALA C . n 
C 1 253 PRO 253 254 254 PRO PRO C . n 
C 1 254 GLU 254 255 255 GLU GLU C . n 
C 1 255 TYR 255 256 256 TYR TYR C . n 
C 1 256 ALA 256 257 257 ALA ALA C . n 
C 1 257 TYR 257 258 258 TYR TYR C . n 
C 1 258 LYS 258 259 259 LYS LYS C . n 
C 1 259 ILE 259 260 260 ILE ILE C . n 
C 1 260 VAL 260 260 260 VAL VAL C A n 
C 1 261 LYS 261 261 261 LYS LYS C . n 
C 1 262 LYS 262 262 262 LYS LYS C . n 
C 1 263 GLY 263 263 263 GLY GLY C . n 
C 1 264 ASP 264 264 264 ASP ASP C . n 
C 1 265 SER 265 265 265 SER SER C . n 
C 1 266 THR 266 266 266 THR THR C . n 
C 1 267 ILE 267 267 267 ILE ILE C . n 
C 1 268 MET 268 268 268 MET MET C . n 
C 1 269 LYS 269 269 269 LYS LYS C . n 
C 1 270 SER 270 270 270 SER SER C . n 
C 1 271 GLY 271 271 271 GLY GLY C . n 
C 1 272 VAL 272 272 272 VAL VAL C . n 
C 1 273 GLU 273 273 273 GLU GLU C . n 
C 1 274 TYR 274 274 274 TYR TYR C . n 
C 1 275 GLY 275 275 275 GLY GLY C . n 
C 1 276 HIS 276 276 276 HIS HIS C . n 
C 1 277 CYS 277 277 277 CYS CYS C . n 
C 1 278 ASN 278 278 278 ASN ASN C . n 
C 1 279 THR 279 279 279 THR THR C . n 
C 1 280 LYS 280 280 280 LYS LYS C . n 
C 1 281 CYS 281 281 281 CYS CYS C . n 
C 1 282 GLN 282 282 282 GLN GLN C . n 
C 1 283 THR 283 283 283 THR THR C . n 
C 1 284 PRO 284 284 284 PRO PRO C . n 
C 1 285 VAL 285 285 285 VAL VAL C . n 
C 1 286 GLY 286 286 286 GLY GLY C . n 
C 1 287 ALA 287 287 287 ALA ALA C . n 
C 1 288 ILE 288 288 288 ILE ILE C . n 
C 1 289 ASN 289 289 289 ASN ASN C . n 
C 1 290 SER 290 290 290 SER SER C . n 
C 1 291 SER 291 291 291 SER SER C . n 
C 1 292 MET 292 292 292 MET MET C . n 
C 1 293 PRO 293 293 293 PRO PRO C . n 
C 1 294 PHE 294 294 294 PHE PHE C . n 
C 1 295 HIS 295 295 295 HIS HIS C . n 
C 1 296 ASN 296 296 296 ASN ASN C . n 
C 1 297 ILE 297 297 297 ILE ILE C . n 
C 1 298 HIS 298 298 298 HIS HIS C . n 
C 1 299 PRO 299 299 299 PRO PRO C . n 
C 1 300 LEU 300 300 300 LEU LEU C . n 
C 1 301 THR 301 301 301 THR THR C . n 
C 1 302 ILE 302 302 302 ILE ILE C . n 
C 1 303 GLY 303 303 303 GLY GLY C . n 
C 1 304 GLU 304 304 304 GLU GLU C . n 
C 1 305 CYS 305 305 305 CYS CYS C . n 
C 1 306 PRO 306 306 306 PRO PRO C . n 
C 1 307 LYS 307 307 307 LYS LYS C . n 
C 1 308 TYR 308 308 308 TYR TYR C . n 
C 1 309 VAL 309 309 309 VAL VAL C . n 
C 1 310 LYS 310 310 310 LYS LYS C . n 
C 1 311 SER 311 311 311 SER SER C . n 
C 1 312 ASN 312 312 312 ASN ASN C . n 
C 1 313 LYS 313 313 313 LYS LYS C . n 
C 1 314 LEU 314 314 314 LEU LEU C . n 
C 1 315 VAL 315 315 315 VAL VAL C . n 
C 1 316 LEU 316 316 316 LEU LEU C . n 
C 1 317 ALA 317 317 317 ALA ALA C . n 
C 1 318 THR 318 318 318 THR THR C . n 
C 1 319 GLY 319 319 319 GLY GLY C . n 
C 1 320 LEU 320 320 320 LEU LEU C . n 
C 1 321 ARG 321 321 321 ARG ARG C . n 
C 1 322 ASN 322 322 322 ASN ASN C . n 
C 1 323 SER 323 323 323 SER SER C . n 
C 1 324 PRO 324 324 324 PRO PRO C . n 
C 1 325 GLN 325 325 ?   ?   ?   C . n 
C 1 326 ARG 326 326 ?   ?   ?   C . n 
C 1 327 GLU 327 327 ?   ?   ?   C . n 
C 1 328 THR 328 328 ?   ?   ?   C . n 
D 2 1   GLY 1   1   ?   ?   ?   D . n 
D 2 2   LEU 2   2   ?   ?   ?   D . n 
D 2 3   PHE 3   3   ?   ?   ?   D . n 
D 2 4   GLY 4   4   ?   ?   ?   D . n 
D 2 5   ALA 5   5   ?   ?   ?   D . n 
D 2 6   ILE 6   6   6   ILE ILE D . n 
D 2 7   ALA 7   7   7   ALA ALA D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   PHE 9   9   9   PHE PHE D . n 
D 2 10  ILE 10  10  10  ILE ILE D . n 
D 2 11  GLU 11  11  11  GLU GLU D . n 
D 2 12  GLY 12  12  12  GLY GLY D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  TRP 14  14  14  TRP TRP D . n 
D 2 15  GLN 15  15  15  GLN GLN D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  MET 17  17  17  MET MET D . n 
D 2 18  VAL 18  18  18  VAL VAL D . n 
D 2 19  ASP 19  19  19  ASP ASP D . n 
D 2 20  GLY 20  20  20  GLY GLY D . n 
D 2 21  TRP 21  21  21  TRP TRP D . n 
D 2 22  TYR 22  22  22  TYR TYR D . n 
D 2 23  GLY 23  23  23  GLY GLY D . n 
D 2 24  TYR 24  24  24  TYR TYR D . n 
D 2 25  HIS 25  25  25  HIS HIS D . n 
D 2 26  HIS 26  26  26  HIS HIS D . n 
D 2 27  SER 27  27  27  SER SER D . n 
D 2 28  ASN 28  28  28  ASN ASN D . n 
D 2 29  GLU 29  29  29  GLU GLU D . n 
D 2 30  GLN 30  30  30  GLN GLN D . n 
D 2 31  GLY 31  31  31  GLY GLY D . n 
D 2 32  SER 32  32  32  SER SER D . n 
D 2 33  GLY 33  33  33  GLY GLY D . n 
D 2 34  TYR 34  34  34  TYR TYR D . n 
D 2 35  ALA 35  35  35  ALA ALA D . n 
D 2 36  ALA 36  36  36  ALA ALA D . n 
D 2 37  ASP 37  37  37  ASP ASP D . n 
D 2 38  LYS 38  38  38  LYS LYS D . n 
D 2 39  GLU 39  39  39  GLU GLU D . n 
D 2 40  SER 40  40  40  SER SER D . n 
D 2 41  THR 41  41  41  THR THR D . n 
D 2 42  GLN 42  42  42  GLN GLN D . n 
D 2 43  LYS 43  43  43  LYS LYS D . n 
D 2 44  ALA 44  44  44  ALA ALA D . n 
D 2 45  ILE 45  45  45  ILE ILE D . n 
D 2 46  ASP 46  46  46  ASP ASP D . n 
D 2 47  GLY 47  47  47  GLY GLY D . n 
D 2 48  VAL 48  48  48  VAL VAL D . n 
D 2 49  THR 49  49  49  THR THR D . n 
D 2 50  ASN 50  50  50  ASN ASN D . n 
D 2 51  LYS 51  51  51  LYS LYS D . n 
D 2 52  VAL 52  52  52  VAL VAL D . n 
D 2 53  ASN 53  53  53  ASN ASN D . n 
D 2 54  SER 54  54  54  SER SER D . n 
D 2 55  ILE 55  55  55  ILE ILE D . n 
D 2 56  ILE 56  56  56  ILE ILE D . n 
D 2 57  ASP 57  57  57  ASP ASP D . n 
D 2 58  LYS 58  58  58  LYS LYS D . n 
D 2 59  MET 59  59  59  MET MET D . n 
D 2 60  ASN 60  60  60  ASN ASN D . n 
D 2 61  THR 61  61  61  THR THR D . n 
D 2 62  GLN 62  62  62  GLN GLN D . n 
D 2 63  PHE 63  63  63  PHE PHE D . n 
D 2 64  GLU 64  64  64  GLU GLU D . n 
D 2 65  ALA 65  65  65  ALA ALA D . n 
D 2 66  VAL 66  66  66  VAL VAL D . n 
D 2 67  GLY 67  67  67  GLY GLY D . n 
D 2 68  ARG 68  68  68  ARG ARG D . n 
D 2 69  GLU 69  69  69  GLU GLU D . n 
D 2 70  PHE 70  70  70  PHE PHE D . n 
D 2 71  ASN 71  71  71  ASN ASN D . n 
D 2 72  ASN 72  72  72  ASN ASN D . n 
D 2 73  LEU 73  73  73  LEU LEU D . n 
D 2 74  GLU 74  74  74  GLU GLU D . n 
D 2 75  ARG 75  75  75  ARG ARG D . n 
D 2 76  ARG 76  76  76  ARG ARG D . n 
D 2 77  ILE 77  77  77  ILE ILE D . n 
D 2 78  GLU 78  78  78  GLU GLU D . n 
D 2 79  ASN 79  79  79  ASN ASN D . n 
D 2 80  LEU 80  80  80  LEU LEU D . n 
D 2 81  ASN 81  81  81  ASN ASN D . n 
D 2 82  LYS 82  82  82  LYS LYS D . n 
D 2 83  LYS 83  83  83  LYS LYS D . n 
D 2 84  MET 84  84  84  MET MET D . n 
D 2 85  GLU 85  85  85  GLU GLU D . n 
D 2 86  ASP 86  86  86  ASP ASP D . n 
D 2 87  GLY 87  87  87  GLY GLY D . n 
D 2 88  PHE 88  88  88  PHE PHE D . n 
D 2 89  LEU 89  89  89  LEU LEU D . n 
D 2 90  ASP 90  90  90  ASP ASP D . n 
D 2 91  VAL 91  91  91  VAL VAL D . n 
D 2 92  TRP 92  92  92  TRP TRP D . n 
D 2 93  THR 93  93  93  THR THR D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  ASN 95  95  95  ASN ASN D . n 
D 2 96  ALA 96  96  96  ALA ALA D . n 
D 2 97  GLU 97  97  97  GLU GLU D . n 
D 2 98  LEU 98  98  98  LEU LEU D . n 
D 2 99  LEU 99  99  99  LEU LEU D . n 
D 2 100 VAL 100 100 100 VAL VAL D . n 
D 2 101 LEU 101 101 101 LEU LEU D . n 
D 2 102 MET 102 102 102 MET MET D . n 
D 2 103 GLU 103 103 103 GLU GLU D . n 
D 2 104 ASN 104 104 104 ASN ASN D . n 
D 2 105 GLU 105 105 105 GLU GLU D . n 
D 2 106 ARG 106 106 106 ARG ARG D . n 
D 2 107 THR 107 107 107 THR THR D . n 
D 2 108 LEU 108 108 108 LEU LEU D . n 
D 2 109 ASP 109 109 109 ASP ASP D . n 
D 2 110 PHE 110 110 110 PHE PHE D . n 
D 2 111 HIS 111 111 111 HIS HIS D . n 
D 2 112 ASP 112 112 112 ASP ASP D . n 
D 2 113 SER 113 113 113 SER SER D . n 
D 2 114 ASN 114 114 114 ASN ASN D . n 
D 2 115 VAL 115 115 115 VAL VAL D . n 
D 2 116 LYS 116 116 116 LYS LYS D . n 
D 2 117 ASN 117 117 117 ASN ASN D . n 
D 2 118 LEU 118 118 118 LEU LEU D . n 
D 2 119 TYR 119 119 119 TYR TYR D . n 
D 2 120 ASP 120 120 120 ASP ASP D . n 
D 2 121 LYS 121 121 121 LYS LYS D . n 
D 2 122 VAL 122 122 122 VAL VAL D . n 
D 2 123 ARG 123 123 123 ARG ARG D . n 
D 2 124 LEU 124 124 124 LEU LEU D . n 
D 2 125 GLN 125 125 125 GLN GLN D . n 
D 2 126 LEU 126 126 126 LEU LEU D . n 
D 2 127 ARG 127 127 127 ARG ARG D . n 
D 2 128 ASP 128 128 128 ASP ASP D . n 
D 2 129 ASN 129 129 129 ASN ASN D . n 
D 2 130 ALA 130 130 130 ALA ALA D . n 
D 2 131 LYS 131 131 131 LYS LYS D . n 
D 2 132 GLU 132 132 132 GLU GLU D . n 
D 2 133 LEU 133 133 133 LEU LEU D . n 
D 2 134 GLY 134 134 134 GLY GLY D . n 
D 2 135 ASN 135 135 135 ASN ASN D . n 
D 2 136 GLY 136 136 136 GLY GLY D . n 
D 2 137 CYS 137 137 137 CYS CYS D . n 
D 2 138 PHE 138 138 138 PHE PHE D . n 
D 2 139 GLU 139 139 139 GLU GLU D . n 
D 2 140 PHE 140 140 140 PHE PHE D . n 
D 2 141 TYR 141 141 141 TYR TYR D . n 
D 2 142 HIS 142 142 142 HIS HIS D . n 
D 2 143 LYS 143 143 143 LYS LYS D . n 
D 2 144 CYS 144 144 144 CYS CYS D . n 
D 2 145 ASP 145 145 145 ASP ASP D . n 
D 2 146 ASN 146 146 146 ASN ASN D . n 
D 2 147 GLU 147 147 147 GLU GLU D . n 
D 2 148 CYS 148 148 148 CYS CYS D . n 
D 2 149 MET 149 149 149 MET MET D . n 
D 2 150 GLU 150 150 150 GLU GLU D . n 
D 2 151 SER 151 151 151 SER SER D . n 
D 2 152 VAL 152 152 152 VAL VAL D . n 
D 2 153 ARG 153 153 153 ARG ARG D . n 
D 2 154 ASN 154 154 154 ASN ASN D . n 
D 2 155 GLY 155 155 155 GLY GLY D . n 
D 2 156 THR 156 156 156 THR THR D . n 
D 2 157 TYR 157 157 157 TYR TYR D . n 
D 2 158 ASP 158 158 158 ASP ASP D . n 
D 2 159 TYR 159 159 159 TYR TYR D . n 
D 2 160 PRO 160 160 160 PRO PRO D . n 
D 2 161 GLN 161 161 161 GLN GLN D . n 
D 2 162 TYR 162 162 162 TYR TYR D . n 
D 2 163 SER 163 163 163 SER SER D . n 
D 2 164 GLU 164 164 164 GLU GLU D . n 
D 2 165 GLU 165 165 165 GLU GLU D . n 
D 2 166 ALA 166 166 166 ALA ALA D . n 
D 2 167 ARG 167 167 167 ARG ARG D . n 
D 2 168 LEU 168 168 168 LEU LEU D . n 
D 2 169 LYS 169 169 169 LYS LYS D . n 
D 2 170 ARG 170 170 170 ARG ARG D . n 
D 2 171 GLU 171 171 171 GLU GLU D . n 
D 2 172 GLU 172 172 172 GLU GLU D . n 
D 2 173 ILE 173 173 173 ILE ILE D . n 
D 2 174 SER 174 174 174 SER SER D . n 
D 2 175 SER 175 175 ?   ?   ?   D . n 
D 2 176 GLY 176 176 ?   ?   ?   D . n 
D 2 177 ARG 177 177 ?   ?   ?   D . n 
E 1 1   ASP 1   8   8   ASP ASP E . n 
E 1 2   PRO 2   9   9   PRO PRO E . n 
E 1 3   GLY 3   10  10  GLY GLY E . n 
E 1 4   ASP 4   11  11  ASP ASP E . n 
E 1 5   GLN 5   12  12  GLN GLN E . n 
E 1 6   ILE 6   13  13  ILE ILE E . n 
E 1 7   CYS 7   14  14  CYS CYS E . n 
E 1 8   ILE 8   15  15  ILE ILE E . n 
E 1 9   GLY 9   16  16  GLY GLY E . n 
E 1 10  TYR 10  17  17  TYR TYR E . n 
E 1 11  HIS 11  18  18  HIS HIS E . n 
E 1 12  ALA 12  19  19  ALA ALA E . n 
E 1 13  ASN 13  20  20  ASN ASN E . n 
E 1 14  ASN 14  21  21  ASN ASN E . n 
E 1 15  SER 15  22  22  SER SER E . n 
E 1 16  THR 16  23  23  THR THR E . n 
E 1 17  GLU 17  24  24  GLU GLU E . n 
E 1 18  GLN 18  25  25  GLN GLN E . n 
E 1 19  VAL 19  26  26  VAL VAL E . n 
E 1 20  ASP 20  27  27  ASP ASP E . n 
E 1 21  THR 21  28  28  THR THR E . n 
E 1 22  ILE 22  29  29  ILE ILE E . n 
E 1 23  MET 23  30  30  MET MET E . n 
E 1 24  GLU 24  31  31  GLU GLU E . n 
E 1 25  LYS 25  32  32  LYS LYS E . n 
E 1 26  ASN 26  33  33  ASN ASN E . n 
E 1 27  VAL 27  34  34  VAL VAL E . n 
E 1 28  THR 28  35  35  THR THR E . n 
E 1 29  VAL 29  36  36  VAL VAL E . n 
E 1 30  THR 30  37  37  THR THR E . n 
E 1 31  HIS 31  38  38  HIS HIS E . n 
E 1 32  ALA 32  39  39  ALA ALA E . n 
E 1 33  GLN 33  40  40  GLN GLN E . n 
E 1 34  ASP 34  41  41  ASP ASP E . n 
E 1 35  ILE 35  42  42  ILE ILE E . n 
E 1 36  LEU 36  43  43  LEU LEU E . n 
E 1 37  GLU 37  44  44  GLU GLU E . n 
E 1 38  LYS 38  45  45  LYS LYS E . n 
E 1 39  THR 39  46  46  THR THR E . n 
E 1 40  HIS 40  47  47  HIS HIS E . n 
E 1 41  ASN 41  48  48  ASN ASN E . n 
E 1 42  GLY 42  49  49  GLY GLY E . n 
E 1 43  LYS 43  50  50  LYS LYS E . n 
E 1 44  LEU 44  51  51  LEU LEU E . n 
E 1 45  CYS 45  52  52  CYS CYS E . n 
E 1 46  ASP 46  53  53  ASP ASP E . n 
E 1 47  LEU 47  54  54  LEU LEU E . n 
E 1 48  ASN 48  55  55  ASN ASN E . n 
E 1 49  GLY 49  55  55  GLY GLY E A n 
E 1 50  VAL 50  56  56  VAL VAL E . n 
E 1 51  LYS 51  57  57  LYS LYS E . n 
E 1 52  PRO 52  58  58  PRO PRO E . n 
E 1 53  LEU 53  59  59  LEU LEU E . n 
E 1 54  ILE 54  60  60  ILE ILE E . n 
E 1 55  LEU 55  61  61  LEU LEU E . n 
E 1 56  LYS 56  62  62  LYS LYS E . n 
E 1 57  ASP 57  63  63  ASP ASP E . n 
E 1 58  CYS 58  64  64  CYS CYS E . n 
E 1 59  SER 59  65  65  SER SER E . n 
E 1 60  VAL 60  66  66  VAL VAL E . n 
E 1 61  ALA 61  67  67  ALA ALA E . n 
E 1 62  GLY 62  68  68  GLY GLY E . n 
E 1 63  TRP 63  69  69  TRP TRP E . n 
E 1 64  LEU 64  70  70  LEU LEU E . n 
E 1 65  LEU 65  71  71  LEU LEU E . n 
E 1 66  GLY 66  72  72  GLY GLY E . n 
E 1 67  ASN 67  73  73  ASN ASN E . n 
E 1 68  PRO 68  74  74  PRO PRO E . n 
E 1 69  MET 69  75  75  MET MET E . n 
E 1 70  CYS 70  76  76  CYS CYS E . n 
E 1 71  ASP 71  77  77  ASP ASP E . n 
E 1 72  GLU 72  78  78  GLU GLU E . n 
E 1 73  PHE 73  79  79  PHE PHE E . n 
E 1 74  ILE 74  80  80  ILE ILE E . n 
E 1 75  ARG 75  81  81  ARG ARG E . n 
E 1 76  VAL 76  82  82  VAL VAL E . n 
E 1 77  PRO 77  83  83  PRO PRO E . n 
E 1 78  GLU 78  83  83  GLU GLU E A n 
E 1 79  TRP 79  84  84  TRP TRP E . n 
E 1 80  SER 80  85  85  SER SER E . n 
E 1 81  TYR 81  86  86  TYR TYR E . n 
E 1 82  ILE 82  87  87  ILE ILE E . n 
E 1 83  VAL 83  88  88  VAL VAL E . n 
E 1 84  GLU 84  89  89  GLU GLU E . n 
E 1 85  ARG 85  90  90  ARG ARG E . n 
E 1 86  ALA 86  91  91  ALA ALA E . n 
E 1 87  ASN 87  92  92  ASN ASN E . n 
E 1 88  PRO 88  93  93  PRO PRO E . n 
E 1 89  ALA 89  94  94  ALA ALA E . n 
E 1 90  ASN 90  95  95  ASN ASN E . n 
E 1 91  ASP 91  96  96  ASP ASP E . n 
E 1 92  LEU 92  96  96  LEU LEU E A n 
E 1 93  CYS 93  97  97  CYS CYS E . n 
E 1 94  TYR 94  98  98  TYR TYR E . n 
E 1 95  PRO 95  99  99  PRO PRO E . n 
E 1 96  GLY 96  100 100 GLY GLY E . n 
E 1 97  SER 97  101 101 SER SER E . n 
E 1 98  LEU 98  102 102 LEU LEU E . n 
E 1 99  ASN 99  103 103 ASN ASN E . n 
E 1 100 ASP 100 104 104 ASP ASP E . n 
E 1 101 TYR 101 105 105 TYR TYR E . n 
E 1 102 GLU 102 106 106 GLU GLU E . n 
E 1 103 GLU 103 107 107 GLU GLU E . n 
E 1 104 LEU 104 108 108 LEU LEU E . n 
E 1 105 LYS 105 109 109 LYS LYS E . n 
E 1 106 HIS 106 110 110 HIS HIS E . n 
E 1 107 LEU 107 111 111 LEU LEU E . n 
E 1 108 LEU 108 112 112 LEU LEU E . n 
E 1 109 SER 109 113 113 SER SER E . n 
E 1 110 ARG 110 114 114 ARG ARG E . n 
E 1 111 ILE 111 115 115 ILE ILE E . n 
E 1 112 ASN 112 116 116 ASN ASN E . n 
E 1 113 HIS 113 117 117 HIS HIS E . n 
E 1 114 PHE 114 118 118 PHE PHE E . n 
E 1 115 GLU 115 119 119 GLU GLU E . n 
E 1 116 LYS 116 120 120 LYS LYS E . n 
E 1 117 ILE 117 121 121 ILE ILE E . n 
E 1 118 LEU 118 122 122 LEU LEU E . n 
E 1 119 ILE 119 123 123 ILE ILE E . n 
E 1 120 ILE 120 124 124 ILE ILE E . n 
E 1 121 PRO 121 125 125 PRO PRO E . n 
E 1 122 LYS 122 125 125 LYS LYS E A n 
E 1 123 SER 123 125 125 SER SER E B n 
E 1 124 SER 124 126 126 SER SER E . n 
E 1 125 TRP 125 127 127 TRP TRP E . n 
E 1 126 PRO 126 128 128 PRO PRO E . n 
E 1 127 ASN 127 129 129 ASN ASN E . n 
E 1 128 HIS 128 130 130 HIS HIS E . n 
E 1 129 GLU 129 131 131 GLU GLU E . n 
E 1 130 THR 130 132 132 THR THR E . n 
E 1 131 SER 131 133 133 SER SER E . n 
E 1 132 LEU 132 133 133 LEU LEU E A n 
E 1 133 GLY 133 134 134 GLY GLY E . n 
E 1 134 VAL 134 135 135 VAL VAL E . n 
E 1 135 SER 135 136 136 SER SER E . n 
E 1 136 ALA 136 137 137 ALA ALA E . n 
E 1 137 ALA 137 138 138 ALA ALA E . n 
E 1 138 CYS 138 139 139 CYS CYS E . n 
E 1 139 PRO 139 140 140 PRO PRO E . n 
E 1 140 TYR 140 141 141 TYR TYR E . n 
E 1 141 GLN 141 142 142 GLN GLN E . n 
E 1 142 GLY 142 143 143 GLY GLY E . n 
E 1 143 THR 143 144 144 THR THR E . n 
E 1 144 PRO 144 145 145 PRO PRO E . n 
E 1 145 SER 145 146 146 SER SER E . n 
E 1 146 PHE 146 147 147 PHE PHE E . n 
E 1 147 PHE 147 148 148 PHE PHE E . n 
E 1 148 ARG 148 149 149 ARG ARG E . n 
E 1 149 ASN 149 150 150 ASN ASN E . n 
E 1 150 VAL 150 151 151 VAL VAL E . n 
E 1 151 VAL 151 152 152 VAL VAL E . n 
E 1 152 TRP 152 153 153 TRP TRP E . n 
E 1 153 LEU 153 154 154 LEU LEU E . n 
E 1 154 ILE 154 155 155 ILE ILE E . n 
E 1 155 LYS 155 156 156 LYS LYS E . n 
E 1 156 LYS 156 157 157 LYS LYS E . n 
E 1 157 ASN 157 158 158 ASN ASN E . n 
E 1 158 ASP 158 159 159 ASP ASP E . n 
E 1 159 ALA 159 160 160 ALA ALA E . n 
E 1 160 TYR 160 161 161 TYR TYR E . n 
E 1 161 PRO 161 162 162 PRO PRO E . n 
E 1 162 THR 162 163 163 THR THR E . n 
E 1 163 ILE 163 164 164 ILE ILE E . n 
E 1 164 LYS 164 165 165 LYS LYS E . n 
E 1 165 ILE 165 166 166 ILE ILE E . n 
E 1 166 SER 166 167 167 SER SER E . n 
E 1 167 TYR 167 168 168 TYR TYR E . n 
E 1 168 ASN 168 169 169 ASN ASN E . n 
E 1 169 ASN 169 170 170 ASN ASN E . n 
E 1 170 THR 170 171 171 THR THR E . n 
E 1 171 ASN 171 172 172 ASN ASN E . n 
E 1 172 ARG 172 173 173 ARG ARG E . n 
E 1 173 GLU 173 174 174 GLU GLU E . n 
E 1 174 ASP 174 175 175 ASP ASP E . n 
E 1 175 LEU 175 176 176 LEU LEU E . n 
E 1 176 LEU 176 177 177 LEU LEU E . n 
E 1 177 ILE 177 178 178 ILE ILE E . n 
E 1 178 LEU 178 179 179 LEU LEU E . n 
E 1 179 TRP 179 180 180 TRP TRP E . n 
E 1 180 GLY 180 181 181 GLY GLY E . n 
E 1 181 ILE 181 182 182 ILE ILE E . n 
E 1 182 HIS 182 183 183 HIS HIS E . n 
E 1 183 HIS 183 184 184 HIS HIS E . n 
E 1 184 SER 184 185 185 SER SER E . n 
E 1 185 ASN 185 186 186 ASN ASN E . n 
E 1 186 ASN 186 187 187 ASN ASN E . n 
E 1 187 ALA 187 188 188 ALA ALA E . n 
E 1 188 GLU 188 189 189 GLU GLU E . n 
E 1 189 GLU 189 190 190 GLU GLU E . n 
E 1 190 GLN 190 191 191 GLN GLN E . n 
E 1 191 THR 191 192 192 THR THR E . n 
E 1 192 ASN 192 193 193 ASN ASN E . n 
E 1 193 LEU 193 194 194 LEU LEU E . n 
E 1 194 TYR 194 195 195 TYR TYR E . n 
E 1 195 LYS 195 196 196 LYS LYS E . n 
E 1 196 ASN 196 197 197 ASN ASN E . n 
E 1 197 PRO 197 198 198 PRO PRO E . n 
E 1 198 THR 198 199 199 THR THR E . n 
E 1 199 THR 199 200 200 THR THR E . n 
E 1 200 TYR 200 201 201 TYR TYR E . n 
E 1 201 ILE 201 202 202 ILE ILE E . n 
E 1 202 SER 202 203 203 SER SER E . n 
E 1 203 VAL 203 204 204 VAL VAL E . n 
E 1 204 GLY 204 205 205 GLY GLY E . n 
E 1 205 THR 205 206 206 THR THR E . n 
E 1 206 SER 206 207 207 SER SER E . n 
E 1 207 THR 207 208 208 THR THR E . n 
E 1 208 LEU 208 209 209 LEU LEU E . n 
E 1 209 ASN 209 210 210 ASN ASN E . n 
E 1 210 GLN 210 211 211 GLN GLN E . n 
E 1 211 ARG 211 212 212 ARG ARG E . n 
E 1 212 LEU 212 213 213 LEU LEU E . n 
E 1 213 VAL 213 214 214 VAL VAL E . n 
E 1 214 PRO 214 215 215 PRO PRO E . n 
E 1 215 LYS 215 216 216 LYS LYS E . n 
E 1 216 ILE 216 217 217 ILE ILE E . n 
E 1 217 ALA 217 218 218 ALA ALA E . n 
E 1 218 THR 218 219 219 THR THR E . n 
E 1 219 ARG 219 220 220 ARG ARG E . n 
E 1 220 SER 220 221 221 SER SER E . n 
E 1 221 GLN 221 222 222 GLN GLN E . n 
E 1 222 VAL 222 223 223 VAL VAL E . n 
E 1 223 ASN 223 224 224 ASN ASN E . n 
E 1 224 GLY 224 225 225 GLY GLY E . n 
E 1 225 LEU 225 226 226 LEU LEU E . n 
E 1 226 ARG 226 227 227 ARG ARG E . n 
E 1 227 GLY 227 228 228 GLY GLY E . n 
E 1 228 ARG 228 229 229 ARG ARG E . n 
E 1 229 MET 229 230 230 MET MET E . n 
E 1 230 ASP 230 231 231 ASP ASP E . n 
E 1 231 PHE 231 232 232 PHE PHE E . n 
E 1 232 PHE 232 233 233 PHE PHE E . n 
E 1 233 TRP 233 234 234 TRP TRP E . n 
E 1 234 THR 234 235 235 THR THR E . n 
E 1 235 ILE 235 236 236 ILE ILE E . n 
E 1 236 LEU 236 237 237 LEU LEU E . n 
E 1 237 LYS 237 238 238 LYS LYS E . n 
E 1 238 PRO 238 239 239 PRO PRO E . n 
E 1 239 ASN 239 240 240 ASN ASN E . n 
E 1 240 ASP 240 241 241 ASP ASP E . n 
E 1 241 ALA 241 242 242 ALA ALA E . n 
E 1 242 ILE 242 243 243 ILE ILE E . n 
E 1 243 HIS 243 244 244 HIS HIS E . n 
E 1 244 PHE 244 245 245 PHE PHE E . n 
E 1 245 GLU 245 246 246 GLU GLU E . n 
E 1 246 SER 246 247 247 SER SER E . n 
E 1 247 ASN 247 248 248 ASN ASN E . n 
E 1 248 GLY 248 249 249 GLY GLY E . n 
E 1 249 ASN 249 250 250 ASN ASN E . n 
E 1 250 PHE 250 251 251 PHE PHE E . n 
E 1 251 ILE 251 252 252 ILE ILE E . n 
E 1 252 ALA 252 253 253 ALA ALA E . n 
E 1 253 PRO 253 254 254 PRO PRO E . n 
E 1 254 GLU 254 255 255 GLU GLU E . n 
E 1 255 TYR 255 256 256 TYR TYR E . n 
E 1 256 ALA 256 257 257 ALA ALA E . n 
E 1 257 TYR 257 258 258 TYR TYR E . n 
E 1 258 LYS 258 259 259 LYS LYS E . n 
E 1 259 ILE 259 260 260 ILE ILE E . n 
E 1 260 VAL 260 260 260 VAL VAL E A n 
E 1 261 LYS 261 261 261 LYS LYS E . n 
E 1 262 LYS 262 262 262 LYS LYS E . n 
E 1 263 GLY 263 263 263 GLY GLY E . n 
E 1 264 ASP 264 264 264 ASP ASP E . n 
E 1 265 SER 265 265 265 SER SER E . n 
E 1 266 THR 266 266 266 THR THR E . n 
E 1 267 ILE 267 267 267 ILE ILE E . n 
E 1 268 MET 268 268 268 MET MET E . n 
E 1 269 LYS 269 269 269 LYS LYS E . n 
E 1 270 SER 270 270 270 SER SER E . n 
E 1 271 GLY 271 271 271 GLY GLY E . n 
E 1 272 VAL 272 272 272 VAL VAL E . n 
E 1 273 GLU 273 273 273 GLU GLU E . n 
E 1 274 TYR 274 274 274 TYR TYR E . n 
E 1 275 GLY 275 275 275 GLY GLY E . n 
E 1 276 HIS 276 276 276 HIS HIS E . n 
E 1 277 CYS 277 277 277 CYS CYS E . n 
E 1 278 ASN 278 278 278 ASN ASN E . n 
E 1 279 THR 279 279 279 THR THR E . n 
E 1 280 LYS 280 280 280 LYS LYS E . n 
E 1 281 CYS 281 281 281 CYS CYS E . n 
E 1 282 GLN 282 282 282 GLN GLN E . n 
E 1 283 THR 283 283 283 THR THR E . n 
E 1 284 PRO 284 284 284 PRO PRO E . n 
E 1 285 VAL 285 285 285 VAL VAL E . n 
E 1 286 GLY 286 286 286 GLY GLY E . n 
E 1 287 ALA 287 287 287 ALA ALA E . n 
E 1 288 ILE 288 288 288 ILE ILE E . n 
E 1 289 ASN 289 289 289 ASN ASN E . n 
E 1 290 SER 290 290 290 SER SER E . n 
E 1 291 SER 291 291 291 SER SER E . n 
E 1 292 MET 292 292 292 MET MET E . n 
E 1 293 PRO 293 293 293 PRO PRO E . n 
E 1 294 PHE 294 294 294 PHE PHE E . n 
E 1 295 HIS 295 295 295 HIS HIS E . n 
E 1 296 ASN 296 296 296 ASN ASN E . n 
E 1 297 ILE 297 297 297 ILE ILE E . n 
E 1 298 HIS 298 298 298 HIS HIS E . n 
E 1 299 PRO 299 299 299 PRO PRO E . n 
E 1 300 LEU 300 300 300 LEU LEU E . n 
E 1 301 THR 301 301 301 THR THR E . n 
E 1 302 ILE 302 302 302 ILE ILE E . n 
E 1 303 GLY 303 303 303 GLY GLY E . n 
E 1 304 GLU 304 304 304 GLU GLU E . n 
E 1 305 CYS 305 305 305 CYS CYS E . n 
E 1 306 PRO 306 306 306 PRO PRO E . n 
E 1 307 LYS 307 307 307 LYS LYS E . n 
E 1 308 TYR 308 308 308 TYR TYR E . n 
E 1 309 VAL 309 309 309 VAL VAL E . n 
E 1 310 LYS 310 310 310 LYS LYS E . n 
E 1 311 SER 311 311 311 SER SER E . n 
E 1 312 ASN 312 312 312 ASN ASN E . n 
E 1 313 LYS 313 313 313 LYS LYS E . n 
E 1 314 LEU 314 314 314 LEU LEU E . n 
E 1 315 VAL 315 315 315 VAL VAL E . n 
E 1 316 LEU 316 316 316 LEU LEU E . n 
E 1 317 ALA 317 317 317 ALA ALA E . n 
E 1 318 THR 318 318 318 THR THR E . n 
E 1 319 GLY 319 319 319 GLY GLY E . n 
E 1 320 LEU 320 320 320 LEU LEU E . n 
E 1 321 ARG 321 321 321 ARG ARG E . n 
E 1 322 ASN 322 322 322 ASN ASN E . n 
E 1 323 SER 323 323 323 SER SER E . n 
E 1 324 PRO 324 324 ?   ?   ?   E . n 
E 1 325 GLN 325 325 ?   ?   ?   E . n 
E 1 326 ARG 326 326 ?   ?   ?   E . n 
E 1 327 GLU 327 327 ?   ?   ?   E . n 
E 1 328 THR 328 328 ?   ?   ?   E . n 
F 2 1   GLY 1   1   ?   ?   ?   F . n 
F 2 2   LEU 2   2   ?   ?   ?   F . n 
F 2 3   PHE 3   3   ?   ?   ?   F . n 
F 2 4   GLY 4   4   ?   ?   ?   F . n 
F 2 5   ALA 5   5   ?   ?   ?   F . n 
F 2 6   ILE 6   6   6   ILE ILE F . n 
F 2 7   ALA 7   7   7   ALA ALA F . n 
F 2 8   GLY 8   8   8   GLY GLY F . n 
F 2 9   PHE 9   9   9   PHE PHE F . n 
F 2 10  ILE 10  10  10  ILE ILE F . n 
F 2 11  GLU 11  11  11  GLU GLU F . n 
F 2 12  GLY 12  12  12  GLY GLY F . n 
F 2 13  GLY 13  13  13  GLY GLY F . n 
F 2 14  TRP 14  14  14  TRP TRP F . n 
F 2 15  GLN 15  15  15  GLN GLN F . n 
F 2 16  GLY 16  16  16  GLY GLY F . n 
F 2 17  MET 17  17  17  MET MET F . n 
F 2 18  VAL 18  18  18  VAL VAL F . n 
F 2 19  ASP 19  19  19  ASP ASP F . n 
F 2 20  GLY 20  20  20  GLY GLY F . n 
F 2 21  TRP 21  21  21  TRP TRP F . n 
F 2 22  TYR 22  22  22  TYR TYR F . n 
F 2 23  GLY 23  23  23  GLY GLY F . n 
F 2 24  TYR 24  24  24  TYR TYR F . n 
F 2 25  HIS 25  25  25  HIS HIS F . n 
F 2 26  HIS 26  26  26  HIS HIS F . n 
F 2 27  SER 27  27  27  SER SER F . n 
F 2 28  ASN 28  28  28  ASN ASN F . n 
F 2 29  GLU 29  29  29  GLU GLU F . n 
F 2 30  GLN 30  30  30  GLN GLN F . n 
F 2 31  GLY 31  31  31  GLY GLY F . n 
F 2 32  SER 32  32  32  SER SER F . n 
F 2 33  GLY 33  33  33  GLY GLY F . n 
F 2 34  TYR 34  34  34  TYR TYR F . n 
F 2 35  ALA 35  35  35  ALA ALA F . n 
F 2 36  ALA 36  36  36  ALA ALA F . n 
F 2 37  ASP 37  37  37  ASP ASP F . n 
F 2 38  LYS 38  38  38  LYS LYS F . n 
F 2 39  GLU 39  39  39  GLU GLU F . n 
F 2 40  SER 40  40  40  SER SER F . n 
F 2 41  THR 41  41  41  THR THR F . n 
F 2 42  GLN 42  42  42  GLN GLN F . n 
F 2 43  LYS 43  43  43  LYS LYS F . n 
F 2 44  ALA 44  44  44  ALA ALA F . n 
F 2 45  ILE 45  45  45  ILE ILE F . n 
F 2 46  ASP 46  46  46  ASP ASP F . n 
F 2 47  GLY 47  47  47  GLY GLY F . n 
F 2 48  VAL 48  48  48  VAL VAL F . n 
F 2 49  THR 49  49  49  THR THR F . n 
F 2 50  ASN 50  50  50  ASN ASN F . n 
F 2 51  LYS 51  51  51  LYS LYS F . n 
F 2 52  VAL 52  52  52  VAL VAL F . n 
F 2 53  ASN 53  53  53  ASN ASN F . n 
F 2 54  SER 54  54  54  SER SER F . n 
F 2 55  ILE 55  55  55  ILE ILE F . n 
F 2 56  ILE 56  56  56  ILE ILE F . n 
F 2 57  ASP 57  57  57  ASP ASP F . n 
F 2 58  LYS 58  58  58  LYS LYS F . n 
F 2 59  MET 59  59  59  MET MET F . n 
F 2 60  ASN 60  60  60  ASN ASN F . n 
F 2 61  THR 61  61  61  THR THR F . n 
F 2 62  GLN 62  62  62  GLN GLN F . n 
F 2 63  PHE 63  63  63  PHE PHE F . n 
F 2 64  GLU 64  64  64  GLU GLU F . n 
F 2 65  ALA 65  65  65  ALA ALA F . n 
F 2 66  VAL 66  66  66  VAL VAL F . n 
F 2 67  GLY 67  67  67  GLY GLY F . n 
F 2 68  ARG 68  68  68  ARG ARG F . n 
F 2 69  GLU 69  69  69  GLU GLU F . n 
F 2 70  PHE 70  70  70  PHE PHE F . n 
F 2 71  ASN 71  71  71  ASN ASN F . n 
F 2 72  ASN 72  72  72  ASN ASN F . n 
F 2 73  LEU 73  73  73  LEU LEU F . n 
F 2 74  GLU 74  74  74  GLU GLU F . n 
F 2 75  ARG 75  75  75  ARG ARG F . n 
F 2 76  ARG 76  76  76  ARG ARG F . n 
F 2 77  ILE 77  77  77  ILE ILE F . n 
F 2 78  GLU 78  78  78  GLU GLU F . n 
F 2 79  ASN 79  79  79  ASN ASN F . n 
F 2 80  LEU 80  80  80  LEU LEU F . n 
F 2 81  ASN 81  81  81  ASN ASN F . n 
F 2 82  LYS 82  82  82  LYS LYS F . n 
F 2 83  LYS 83  83  83  LYS LYS F . n 
F 2 84  MET 84  84  84  MET MET F . n 
F 2 85  GLU 85  85  85  GLU GLU F . n 
F 2 86  ASP 86  86  86  ASP ASP F . n 
F 2 87  GLY 87  87  87  GLY GLY F . n 
F 2 88  PHE 88  88  88  PHE PHE F . n 
F 2 89  LEU 89  89  89  LEU LEU F . n 
F 2 90  ASP 90  90  90  ASP ASP F . n 
F 2 91  VAL 91  91  91  VAL VAL F . n 
F 2 92  TRP 92  92  92  TRP TRP F . n 
F 2 93  THR 93  93  93  THR THR F . n 
F 2 94  TYR 94  94  94  TYR TYR F . n 
F 2 95  ASN 95  95  95  ASN ASN F . n 
F 2 96  ALA 96  96  96  ALA ALA F . n 
F 2 97  GLU 97  97  97  GLU GLU F . n 
F 2 98  LEU 98  98  98  LEU LEU F . n 
F 2 99  LEU 99  99  99  LEU LEU F . n 
F 2 100 VAL 100 100 100 VAL VAL F . n 
F 2 101 LEU 101 101 101 LEU LEU F . n 
F 2 102 MET 102 102 102 MET MET F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 ASN 104 104 104 ASN ASN F . n 
F 2 105 GLU 105 105 105 GLU GLU F . n 
F 2 106 ARG 106 106 106 ARG ARG F . n 
F 2 107 THR 107 107 107 THR THR F . n 
F 2 108 LEU 108 108 108 LEU LEU F . n 
F 2 109 ASP 109 109 109 ASP ASP F . n 
F 2 110 PHE 110 110 110 PHE PHE F . n 
F 2 111 HIS 111 111 111 HIS HIS F . n 
F 2 112 ASP 112 112 112 ASP ASP F . n 
F 2 113 SER 113 113 113 SER SER F . n 
F 2 114 ASN 114 114 114 ASN ASN F . n 
F 2 115 VAL 115 115 115 VAL VAL F . n 
F 2 116 LYS 116 116 116 LYS LYS F . n 
F 2 117 ASN 117 117 117 ASN ASN F . n 
F 2 118 LEU 118 118 118 LEU LEU F . n 
F 2 119 TYR 119 119 119 TYR TYR F . n 
F 2 120 ASP 120 120 120 ASP ASP F . n 
F 2 121 LYS 121 121 121 LYS LYS F . n 
F 2 122 VAL 122 122 122 VAL VAL F . n 
F 2 123 ARG 123 123 123 ARG ARG F . n 
F 2 124 LEU 124 124 124 LEU LEU F . n 
F 2 125 GLN 125 125 125 GLN GLN F . n 
F 2 126 LEU 126 126 126 LEU LEU F . n 
F 2 127 ARG 127 127 127 ARG ARG F . n 
F 2 128 ASP 128 128 128 ASP ASP F . n 
F 2 129 ASN 129 129 129 ASN ASN F . n 
F 2 130 ALA 130 130 130 ALA ALA F . n 
F 2 131 LYS 131 131 131 LYS LYS F . n 
F 2 132 GLU 132 132 132 GLU GLU F . n 
F 2 133 LEU 133 133 133 LEU LEU F . n 
F 2 134 GLY 134 134 134 GLY GLY F . n 
F 2 135 ASN 135 135 135 ASN ASN F . n 
F 2 136 GLY 136 136 136 GLY GLY F . n 
F 2 137 CYS 137 137 137 CYS CYS F . n 
F 2 138 PHE 138 138 138 PHE PHE F . n 
F 2 139 GLU 139 139 139 GLU GLU F . n 
F 2 140 PHE 140 140 140 PHE PHE F . n 
F 2 141 TYR 141 141 141 TYR TYR F . n 
F 2 142 HIS 142 142 142 HIS HIS F . n 
F 2 143 LYS 143 143 143 LYS LYS F . n 
F 2 144 CYS 144 144 144 CYS CYS F . n 
F 2 145 ASP 145 145 145 ASP ASP F . n 
F 2 146 ASN 146 146 146 ASN ASN F . n 
F 2 147 GLU 147 147 147 GLU GLU F . n 
F 2 148 CYS 148 148 148 CYS CYS F . n 
F 2 149 MET 149 149 149 MET MET F . n 
F 2 150 GLU 150 150 150 GLU GLU F . n 
F 2 151 SER 151 151 151 SER SER F . n 
F 2 152 VAL 152 152 152 VAL VAL F . n 
F 2 153 ARG 153 153 153 ARG ARG F . n 
F 2 154 ASN 154 154 154 ASN ASN F . n 
F 2 155 GLY 155 155 155 GLY GLY F . n 
F 2 156 THR 156 156 156 THR THR F . n 
F 2 157 TYR 157 157 157 TYR TYR F . n 
F 2 158 ASP 158 158 158 ASP ASP F . n 
F 2 159 TYR 159 159 159 TYR TYR F . n 
F 2 160 PRO 160 160 160 PRO PRO F . n 
F 2 161 GLN 161 161 161 GLN GLN F . n 
F 2 162 TYR 162 162 162 TYR TYR F . n 
F 2 163 SER 163 163 163 SER SER F . n 
F 2 164 GLU 164 164 164 GLU GLU F . n 
F 2 165 GLU 165 165 165 GLU GLU F . n 
F 2 166 ALA 166 166 166 ALA ALA F . n 
F 2 167 ARG 167 167 167 ARG ARG F . n 
F 2 168 LEU 168 168 168 LEU LEU F . n 
F 2 169 LYS 169 169 169 LYS LYS F . n 
F 2 170 ARG 170 170 170 ARG ARG F . n 
F 2 171 GLU 171 171 171 GLU GLU F . n 
F 2 172 GLU 172 172 172 GLU GLU F . n 
F 2 173 ILE 173 173 173 ILE ILE F . n 
F 2 174 SER 174 174 174 SER SER F . n 
F 2 175 SER 175 175 175 SER SER F . n 
F 2 176 GLY 176 176 176 GLY GLY F . n 
F 2 177 ARG 177 177 177 ARG ARG F . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
G 3 NAG 1 G NAG 1 G NAG 1 n 
G 3 NAG 2 G NAG 2 G NAG 2 n 
G 3 BMA 3 G BMA 3 G BMA 3 n 
H 3 NAG 1 H NAG 1 H NAG 1 n 
H 3 NAG 2 H NAG 2 H NAG 2 n 
H 3 BMA 3 H BMA 3 H BMA 3 n 
I 4 NAG 1 I NAG 1 I NAG 1 n 
I 4 NAG 2 I NAG 2 I NAG 2 n 
J 3 NAG 1 J NAG 1 J NAG 1 n 
J 3 NAG 2 J NAG 2 J NAG 2 n 
J 3 BMA 3 J BMA 3 J BMA 3 n 
K 5 GAL 1 K GAL 1 K GAL 1 n 
K 5 NAG 2 K NAG 2 K NAG 2 n 
K 5 GAL 3 K GAL 3 K GAL 3 n 
K 5 SIA 4 K SIA 4 K SIA 4 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 BMA ? ? BMA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GAL ? ? GAL ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
4 SIA ? ? SIA ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
L 6 NAG 1  401 324 NAG NAG A . 
M 6 NAG 1  402 328 NAG NAG A . 
N 6 NAG 1  401 328 NAG NAG C . 
O 6 NAG 1  402 329 NAG NAG C . 
P 6 NAG 1  201 175 NAG NAG D . 
Q 6 NAG 1  401 426 NAG NAG E . 
R 7 HOH 1  501 31  HOH HOH A . 
R 7 HOH 2  502 58  HOH HOH A . 
R 7 HOH 3  503 18  HOH HOH A . 
R 7 HOH 4  504 47  HOH HOH A . 
R 7 HOH 5  505 43  HOH HOH A . 
R 7 HOH 6  506 12  HOH HOH A . 
R 7 HOH 7  507 37  HOH HOH A . 
R 7 HOH 8  508 59  HOH HOH A . 
R 7 HOH 9  509 42  HOH HOH A . 
R 7 HOH 10 510 16  HOH HOH A . 
R 7 HOH 11 511 1   HOH HOH A . 
R 7 HOH 12 512 8   HOH HOH A . 
R 7 HOH 13 513 15  HOH HOH A . 
S 7 HOH 1  201 26  HOH HOH B . 
S 7 HOH 2  202 9   HOH HOH B . 
S 7 HOH 3  203 48  HOH HOH B . 
T 7 HOH 1  501 22  HOH HOH C . 
T 7 HOH 2  502 33  HOH HOH C . 
T 7 HOH 3  503 60  HOH HOH C . 
T 7 HOH 4  504 23  HOH HOH C . 
T 7 HOH 5  505 51  HOH HOH C . 
T 7 HOH 6  506 29  HOH HOH C . 
T 7 HOH 7  507 4   HOH HOH C . 
T 7 HOH 8  508 53  HOH HOH C . 
T 7 HOH 9  509 36  HOH HOH C . 
T 7 HOH 10 510 7   HOH HOH C . 
T 7 HOH 11 511 40  HOH HOH C . 
T 7 HOH 12 512 38  HOH HOH C . 
T 7 HOH 13 513 20  HOH HOH C . 
T 7 HOH 14 514 41  HOH HOH C . 
U 7 HOH 1  301 6   HOH HOH D . 
U 7 HOH 2  302 28  HOH HOH D . 
U 7 HOH 3  303 30  HOH HOH D . 
V 7 HOH 1  501 35  HOH HOH E . 
V 7 HOH 2  502 44  HOH HOH E . 
V 7 HOH 3  503 46  HOH HOH E . 
V 7 HOH 4  504 32  HOH HOH E . 
V 7 HOH 5  505 52  HOH HOH E . 
V 7 HOH 6  506 61  HOH HOH E . 
V 7 HOH 7  507 14  HOH HOH E . 
V 7 HOH 8  508 19  HOH HOH E . 
V 7 HOH 9  509 2   HOH HOH E . 
V 7 HOH 10 510 55  HOH HOH E . 
V 7 HOH 11 511 13  HOH HOH E . 
V 7 HOH 12 512 49  HOH HOH E . 
V 7 HOH 13 513 21  HOH HOH E . 
V 7 HOH 14 514 39  HOH HOH E . 
V 7 HOH 15 515 17  HOH HOH E . 
V 7 HOH 16 516 34  HOH HOH E . 
V 7 HOH 17 517 5   HOH HOH E . 
V 7 HOH 18 518 10  HOH HOH E . 
V 7 HOH 19 519 3   HOH HOH E . 
V 7 HOH 20 520 50  HOH HOH E . 
V 7 HOH 21 521 57  HOH HOH E . 
V 7 HOH 22 522 56  HOH HOH E . 
V 7 HOH 23 523 54  HOH HOH E . 
V 7 HOH 24 524 24  HOH HOH E . 
V 7 HOH 25 525 27  HOH HOH E . 
W 7 HOH 1  201 25  HOH HOH F . 
W 7 HOH 2  202 45  HOH HOH F . 
W 7 HOH 3  203 11  HOH HOH F . 
W 7 HOH 4  204 62  HOH HOH F . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.21.2_5419: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NRB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     95.915 
_cell.length_a_esd                 ? 
_cell.length_b                     176.398 
_cell.length_b_esd                 ? 
_cell.length_c                     226.377 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9NRB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9NRB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Tris, 2M ammonium sulfate, 0.2M lithium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9NRB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.65 
_reflns.d_resolution_low                               26.81 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     110745 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.29 
_reflns.pdbx_Rpim_I_all                                0.085 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.65 
_reflns_shell.d_res_low                                     2.7 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10532 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               2.9 
_reflns_shell.pdbx_Rpim_I_all                               0.85 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.39 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NRB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.65 
_refine.ls_d_res_low                             26.81 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     110720 
_refine.ls_number_reflns_R_free                  5538 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.16 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2107 
_refine.ls_R_factor_R_free                       0.2381 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2093 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.31 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.38 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.65 
_refine_hist.d_res_low                        26.81 
_refine_hist.number_atoms_solvent             62 
_refine_hist.number_atoms_total               12173 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        11825 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         286 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? 12382 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.555  ? 16776 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.649 ? 4922  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.044  ? 1859  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 2162  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.65 2.68  . . 156 2997 86.00  . . . . 0.4050 . . . . . . . . . . . . . . . 0.3831 
'X-RAY DIFFRACTION' 2.68 2.71  . . 208 3484 100.00 . . . . 0.3726 . . . . . . . . . . . . . . . 0.4127 
'X-RAY DIFFRACTION' 2.71 2.75  . . 188 3495 100.00 . . . . 0.3342 . . . . . . . . . . . . . . . 0.3443 
'X-RAY DIFFRACTION' 2.75 2.78  . . 170 3473 100.00 . . . . 0.2922 . . . . . . . . . . . . . . . 0.3164 
'X-RAY DIFFRACTION' 2.78 2.82  . . 187 3502 100.00 . . . . 0.2873 . . . . . . . . . . . . . . . 0.3134 
'X-RAY DIFFRACTION' 2.82 2.86  . . 167 3519 100.00 . . . . 0.2848 . . . . . . . . . . . . . . . 0.3171 
'X-RAY DIFFRACTION' 2.86 2.90  . . 186 3518 100.00 . . . . 0.2839 . . . . . . . . . . . . . . . 0.3154 
'X-RAY DIFFRACTION' 2.90 2.94  . . 191 3469 100.00 . . . . 0.2772 . . . . . . . . . . . . . . . 0.3581 
'X-RAY DIFFRACTION' 2.94 2.99  . . 185 3502 100.00 . . . . 0.2817 . . . . . . . . . . . . . . . 0.3089 
'X-RAY DIFFRACTION' 2.99 3.04  . . 174 3515 100.00 . . . . 0.2812 . . . . . . . . . . . . . . . 0.3123 
'X-RAY DIFFRACTION' 3.04 3.09  . . 211 3500 100.00 . . . . 0.2683 . . . . . . . . . . . . . . . 0.3021 
'X-RAY DIFFRACTION' 3.09 3.14  . . 175 3461 100.00 . . . . 0.2404 . . . . . . . . . . . . . . . 0.2861 
'X-RAY DIFFRACTION' 3.14 3.20  . . 188 3527 100.00 . . . . 0.2344 . . . . . . . . . . . . . . . 0.2661 
'X-RAY DIFFRACTION' 3.20 3.27  . . 200 3467 100.00 . . . . 0.2319 . . . . . . . . . . . . . . . 0.2647 
'X-RAY DIFFRACTION' 3.27 3.34  . . 175 3540 100.00 . . . . 0.2263 . . . . . . . . . . . . . . . 0.2491 
'X-RAY DIFFRACTION' 3.34 3.42  . . 182 3532 100.00 . . . . 0.2241 . . . . . . . . . . . . . . . 0.2817 
'X-RAY DIFFRACTION' 3.42 3.50  . . 180 3481 100.00 . . . . 0.2222 . . . . . . . . . . . . . . . 0.2603 
'X-RAY DIFFRACTION' 3.50 3.60  . . 179 3565 100.00 . . . . 0.2116 . . . . . . . . . . . . . . . 0.2456 
'X-RAY DIFFRACTION' 3.60 3.70  . . 195 3476 99.00  . . . . 0.2107 . . . . . . . . . . . . . . . 0.2632 
'X-RAY DIFFRACTION' 3.70 3.82  . . 172 3533 100.00 . . . . 0.1980 . . . . . . . . . . . . . . . 0.2402 
'X-RAY DIFFRACTION' 3.82 3.96  . . 180 3520 100.00 . . . . 0.1811 . . . . . . . . . . . . . . . 0.2024 
'X-RAY DIFFRACTION' 3.96 4.12  . . 202 3533 100.00 . . . . 0.1774 . . . . . . . . . . . . . . . 0.2046 
'X-RAY DIFFRACTION' 4.12 4.30  . . 181 3543 100.00 . . . . 0.1677 . . . . . . . . . . . . . . . 0.1812 
'X-RAY DIFFRACTION' 4.30 4.53  . . 176 3540 100.00 . . . . 0.1592 . . . . . . . . . . . . . . . 0.1843 
'X-RAY DIFFRACTION' 4.53 4.81  . . 189 3524 99.00  . . . . 0.1613 . . . . . . . . . . . . . . . 0.2010 
'X-RAY DIFFRACTION' 4.81 5.18  . . 182 3547 100.00 . . . . 0.1724 . . . . . . . . . . . . . . . 0.2068 
'X-RAY DIFFRACTION' 5.18 5.70  . . 197 3585 100.00 . . . . 0.1726 . . . . . . . . . . . . . . . 0.2019 
'X-RAY DIFFRACTION' 5.70 6.51  . . 184 3603 100.00 . . . . 0.1935 . . . . . . . . . . . . . . . 0.1898 
'X-RAY DIFFRACTION' 6.51 8.16  . . 174 3636 99.00  . . . . 0.2202 . . . . . . . . . . . . . . . 0.2282 
'X-RAY DIFFRACTION' 8.17 26.81 . . 204 3595 95.00  . . . . 0.2116 . . . . . . . . . . . . . . . 0.2352 
# 
_struct.entry_id                     9NRB 
_struct.title                        
'Crystal structure of H5 hemagglutinin Q226L mutant from the influenza virus A/duck/France/1611008h/16 with LSTc' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9NRB 
_struct_keywords.text            'H1N1, Antibody, Hemagglutinin, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   '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 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 1 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 3 ? 
K N N 5 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 6 ? 
P N N 6 ? 
Q N N 6 ? 
R N N 7 ? 
S N N 7 ? 
T N N 7 ? 
U N N 7 ? 
V N N 7 ? 
W N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A0A6M2RJB8_9INFA A0A6M2RJB8 ? 1 
;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLNGVKPLILKDCSVAGWLLGNPMCDEFIRVPEWSYIV
ERANPANDLCYPGSLNDYEELKHLLSRINHFEKILIIPKSSWPNHETSLGVSAACPYQGTPSFFRNVVWLIKKNDAYPTI
KISYNNTNREDLLILWGIHHSNNAEEQTNLYKNPTTYISVGTSTLNQRLVPKIATRSQVNGQRGRMDFFWTILKPNDAIH
FESNGNFIAPEYAYKIVKKGDSTIMKSGVEYGHCNTKCQTPVGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATGLRNS
PQRET
;
17  
2 UNP A0A6M2RJB8_9INFA A0A6M2RJB8 ? 2 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEARLKREEI
;
343 
# 
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 9NRB A 4 ? 328 ? A0A6M2RJB8 17  ? 341 ? 11 328 
2 2 9NRB B 1 ? 173 ? A0A6M2RJB8 343 ? 515 ? 1  173 
3 1 9NRB C 4 ? 328 ? A0A6M2RJB8 17  ? 341 ? 11 328 
4 2 9NRB D 1 ? 173 ? A0A6M2RJB8 343 ? 515 ? 1  173 
5 1 9NRB E 4 ? 328 ? A0A6M2RJB8 17  ? 341 ? 11 328 
6 2 9NRB F 1 ? 173 ? A0A6M2RJB8 343 ? 515 ? 1  173 
# 
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 9NRB ASP A 1   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      8   1  
1 9NRB PRO A 2   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      9   2  
1 9NRB GLY A 3   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      10  3  
1 9NRB LEU A 225 ? UNP A0A6M2RJB8 GLN 238 'engineered mutation' 226 4  
2 9NRB SER B 174 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      174 5  
2 9NRB SER B 175 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      175 6  
2 9NRB GLY B 176 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      176 7  
2 9NRB ARG B 177 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      177 8  
3 9NRB ASP C 1   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      8   9  
3 9NRB PRO C 2   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      9   10 
3 9NRB GLY C 3   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      10  11 
3 9NRB LEU C 225 ? UNP A0A6M2RJB8 GLN 238 'engineered mutation' 226 12 
4 9NRB SER D 174 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      174 13 
4 9NRB SER D 175 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      175 14 
4 9NRB GLY D 176 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      176 15 
4 9NRB ARG D 177 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      177 16 
5 9NRB ASP E 1   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      8   17 
5 9NRB PRO E 2   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      9   18 
5 9NRB GLY E 3   ? UNP A0A6M2RJB8 ?   ?   'expression tag'      10  19 
5 9NRB LEU E 225 ? UNP A0A6M2RJB8 GLN 238 'engineered mutation' 226 20 
6 9NRB SER F 174 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      174 21 
6 9NRB SER F 175 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      175 22 
6 9NRB GLY F 176 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      176 23 
6 9NRB ARG F 177 ? UNP A0A6M2RJB8 ?   ?   'expression tag'      177 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
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)' 34930 ? 
1 MORE         -119  ? 
1 'SSA (A^2)'  63440 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 59  ? GLY A 66  ? SER A 65  GLY A 72  1 ? 8  
HELX_P HELX_P2  AA2 ASP A 100 ? SER A 109 ? ASP A 104 SER A 113 1 ? 10 
HELX_P HELX_P3  AA3 PRO A 121 ? TRP A 125 ? PRO A 125 TRP A 127 5 ? 5  
HELX_P HELX_P4  AA4 ASN A 186 ? LYS A 195 ? ASN A 187 LYS A 196 1 ? 10 
HELX_P HELX_P5  AA5 ASP B 37  ? LYS B 58  ? ASP B 37  LYS B 58  1 ? 22 
HELX_P HELX_P6  AA6 GLU B 74  ? ARG B 127 ? GLU B 74  ARG B 127 1 ? 54 
HELX_P HELX_P7  AA7 ASP B 145 ? GLY B 155 ? ASP B 145 GLY B 155 1 ? 11 
HELX_P HELX_P8  AA8 ASP B 158 ? GLU B 172 ? ASP B 158 GLU B 172 1 ? 15 
HELX_P HELX_P9  AA9 SER C 59  ? GLY C 66  ? SER C 65  GLY C 72  1 ? 8  
HELX_P HELX_P10 AB1 ASP C 100 ? LEU C 108 ? ASP C 104 LEU C 112 1 ? 9  
HELX_P HELX_P11 AB2 PRO C 121 ? TRP C 125 ? PRO C 125 TRP C 127 5 ? 5  
HELX_P HELX_P12 AB3 ASN C 186 ? TYR C 194 ? ASN C 187 TYR C 195 1 ? 9  
HELX_P HELX_P13 AB4 ASP D 37  ? LYS D 58  ? ASP D 37  LYS D 58  1 ? 22 
HELX_P HELX_P14 AB5 GLU D 74  ? ARG D 127 ? GLU D 74  ARG D 127 1 ? 54 
HELX_P HELX_P15 AB6 ASP D 145 ? ASN D 154 ? ASP D 145 ASN D 154 1 ? 10 
HELX_P HELX_P16 AB7 ASP D 158 ? ILE D 173 ? ASP D 158 ILE D 173 1 ? 16 
HELX_P HELX_P17 AB8 SER E 59  ? GLY E 66  ? SER E 65  GLY E 72  1 ? 8  
HELX_P HELX_P18 AB9 ASP E 100 ? LEU E 108 ? ASP E 104 LEU E 112 1 ? 9  
HELX_P HELX_P19 AC1 PRO E 121 ? TRP E 125 ? PRO E 125 TRP E 127 5 ? 5  
HELX_P HELX_P20 AC2 ASN E 186 ? LYS E 195 ? ASN E 187 LYS E 196 1 ? 10 
HELX_P HELX_P21 AC3 ASP F 37  ? LYS F 58  ? ASP F 37  LYS F 58  1 ? 22 
HELX_P HELX_P22 AC4 GLU F 74  ? ARG F 127 ? GLU F 74  ARG F 127 1 ? 54 
HELX_P HELX_P23 AC5 ASP F 145 ? ASN F 154 ? ASP F 145 ASN F 154 1 ? 10 
HELX_P HELX_P24 AC6 ASP F 158 ? GLY F 176 ? ASP F 158 GLY F 176 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 7   SG  ? ? ? 1_555 B CYS 137 SG ? ? A CYS 14  B CYS 137 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf2  disulf ?    ? A CYS 45  SG  ? ? ? 1_555 A CYS 277 SG ? ? A CYS 52  A CYS 277 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf3  disulf ?    ? A CYS 58  SG  ? ? ? 1_555 A CYS 70  SG ? ? A CYS 64  A CYS 76  1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf4  disulf ?    ? A CYS 93  SG  ? ? ? 1_555 A CYS 138 SG ? ? A CYS 97  A CYS 139 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf5  disulf ?    ? A CYS 281 SG  ? ? ? 1_555 A CYS 305 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf6  disulf ?    ? B CYS 144 SG  ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf7  disulf ?    ? C CYS 7   SG  ? ? ? 1_555 D CYS 137 SG ? ? C CYS 14  D CYS 137 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf8  disulf ?    ? C CYS 45  SG  ? ? ? 1_555 C CYS 277 SG ? ? C CYS 52  C CYS 277 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf9  disulf ?    ? C CYS 58  SG  ? ? ? 1_555 C CYS 70  SG ? ? C CYS 64  C CYS 76  1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf10 disulf ?    ? C CYS 93  SG  ? ? ? 1_555 C CYS 138 SG ? ? C CYS 97  C CYS 139 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf11 disulf ?    ? C CYS 281 SG  ? ? ? 1_555 C CYS 305 SG ? ? C CYS 281 C CYS 305 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf12 disulf ?    ? D CYS 144 SG  ? ? ? 1_555 D CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf13 disulf ?    ? E CYS 7   SG  ? ? ? 1_555 F CYS 137 SG ? ? E CYS 14  F CYS 137 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf14 disulf ?    ? E CYS 45  SG  ? ? ? 1_555 E CYS 277 SG ? ? E CYS 52  E CYS 277 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf15 disulf ?    ? E CYS 58  SG  ? ? ? 1_555 E CYS 70  SG ? ? E CYS 64  E CYS 76  1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf16 disulf ?    ? E CYS 93  SG  ? ? ? 1_555 E CYS 138 SG ? ? E CYS 97  E CYS 139 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf17 disulf ?    ? E CYS 281 SG  ? ? ? 1_555 E CYS 305 SG ? ? E CYS 281 E CYS 305 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf18 disulf ?    ? F CYS 144 SG  ? ? ? 1_555 F CYS 148 SG ? ? F CYS 144 F CYS 148 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
covale1  covale one  ? A ASN 26  ND2 ? ? ? 1_555 L NAG .   C1 ? ? A ASN 33  A NAG 401 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale2  covale one  ? A ASN 168 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 169 G NAG 1   1_555 ? ? ? ? ? ? ? 1.434 ? N-Glycosylation 
covale3  covale one  ? A ASN 289 ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 289 A NAG 402 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale4  covale one  ? C ASN 26  ND2 ? ? ? 1_555 N NAG .   C1 ? ? C ASN 33  C NAG 401 1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale5  covale one  ? C ASN 168 ND2 ? ? ? 1_555 H NAG .   C1 ? ? C ASN 169 H NAG 1   1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
covale6  covale one  ? C ASN 289 ND2 ? ? ? 1_555 O NAG .   C1 ? ? C ASN 289 C NAG 402 1_555 ? ? ? ? ? ? ? 1.444 ? N-Glycosylation 
covale7  covale one  ? D ASN 154 ND2 ? ? ? 1_555 P NAG .   C1 ? ? D ASN 154 D NAG 201 1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
covale8  covale one  ? E ASN 168 ND2 ? ? ? 1_555 I NAG .   C1 ? ? E ASN 169 I NAG 1   1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale9  covale one  ? E ASN 289 ND2 ? ? ? 1_555 Q NAG .   C1 ? ? E ASN 289 E NAG 401 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale10 covale one  ? F ASN 154 ND2 ? ? ? 1_555 J NAG .   C1 ? ? F ASN 154 J NAG 1   1_555 ? ? ? ? ? ? ? 1.454 ? N-Glycosylation 
covale11 covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.439 ? ?               
covale12 covale both ? G NAG .   O4  ? ? ? 1_555 G BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.451 ? ?               
covale13 covale both ? H NAG .   O4  ? ? ? 1_555 H NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.444 ? ?               
covale14 covale both ? H NAG .   O4  ? ? ? 1_555 H BMA .   C1 ? ? H NAG 2   H BMA 3   1_555 ? ? ? ? ? ? ? 1.452 ? ?               
covale15 covale both ? I NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? I NAG 1   I NAG 2   1_555 ? ? ? ? ? ? ? 1.441 ? ?               
covale16 covale both ? J NAG .   O4  ? ? ? 1_555 J NAG .   C1 ? ? J NAG 1   J NAG 2   1_555 ? ? ? ? ? ? ? 1.451 ? ?               
covale17 covale both ? J NAG .   O4  ? ? ? 1_555 J BMA .   C1 ? ? J NAG 2   J BMA 3   1_555 ? ? ? ? ? ? ? 1.454 ? ?               
covale18 covale both ? K GAL .   O3  ? ? ? 1_555 K NAG .   C1 ? ? K GAL 1   K NAG 2   1_555 ? ? ? ? ? ? ? 1.441 ? ?               
covale19 covale both ? K NAG .   O3  ? ? ? 1_555 K GAL .   C1 ? ? K NAG 2   K GAL 3   1_555 ? ? ? ? ? ? ? 1.439 ? ?               
covale20 covale both ? K GAL .   O3  ? ? ? 1_555 K SIA .   C2 ? ? K GAL 3   K SIA 4   1_555 ? ? ? ? ? ? ? 1.444 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG G .   ? ASN A 168 ? NAG G 1   ? 1_555 ASN A 169 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG H .   ? ASN C 168 ? NAG H 1   ? 1_555 ASN C 169 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG I .   ? ASN E 168 ? NAG I 1   ? 1_555 ASN E 169 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG J .   ? ASN F 154 ? NAG J 1   ? 1_555 ASN F 154 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG L .   ? ASN A 26  ? NAG A 401 ? 1_555 ASN A 33  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG M .   ? ASN A 289 ? NAG A 402 ? 1_555 ASN A 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG N .   ? ASN C 26  ? NAG C 401 ? 1_555 ASN C 33  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG O .   ? ASN C 289 ? NAG C 402 ? 1_555 ASN C 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG P .   ? ASN D 154 ? NAG D 201 ? 1_555 ASN D 154 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG Q .   ? ASN E 289 ? NAG E 401 ? 1_555 ASN E 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 CYS A 7   ? CYS B 137 ? CYS A 14  ? 1_555 CYS B 137 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS A 45  ? CYS A 277 ? CYS A 52  ? 1_555 CYS A 277 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 58  ? CYS A 70  ? CYS A 64  ? 1_555 CYS A 76  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 93  ? CYS A 138 ? CYS A 97  ? 1_555 CYS A 139 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS A 281 ? CYS A 305 ? CYS A 281 ? 1_555 CYS A 305 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS B 144 ? CYS B 148 ? CYS B 144 ? 1_555 CYS B 148 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS C 7   ? CYS D 137 ? CYS C 14  ? 1_555 CYS D 137 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
18 CYS C 45  ? CYS C 277 ? CYS C 52  ? 1_555 CYS C 277 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
19 CYS C 58  ? CYS C 70  ? CYS C 64  ? 1_555 CYS C 76  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
20 CYS C 93  ? CYS C 138 ? CYS C 97  ? 1_555 CYS C 139 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
21 CYS C 281 ? CYS C 305 ? CYS C 281 ? 1_555 CYS C 305 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
22 CYS D 144 ? CYS D 148 ? CYS D 144 ? 1_555 CYS D 148 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
23 CYS E 7   ? CYS F 137 ? CYS E 14  ? 1_555 CYS F 137 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
24 CYS E 45  ? CYS E 277 ? CYS E 52  ? 1_555 CYS E 277 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
25 CYS E 58  ? CYS E 70  ? CYS E 64  ? 1_555 CYS E 76  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
26 CYS E 93  ? CYS E 138 ? CYS E 97  ? 1_555 CYS E 139 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
27 CYS E 281 ? CYS E 305 ? CYS E 281 ? 1_555 CYS E 305 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
28 CYS F 144 ? CYS F 148 ? CYS F 144 ? 1_555 CYS F 148 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 5 ? 
AA8 ? 5 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 3 ? 
AB4 ? 5 ? 
AB5 ? 2 ? 
AB6 ? 2 ? 
AB7 ? 3 ? 
AB8 ? 2 ? 
AB9 ? 3 ? 
AC1 ? 5 ? 
AC2 ? 5 ? 
AC3 ? 2 ? 
AC4 ? 4 ? 
AC5 ? 4 ? 
AC6 ? 5 ? 
AC7 ? 2 ? 
AC8 ? 2 ? 
AC9 ? 3 ? 
AD1 ? 2 ? 
AD2 ? 3 ? 
AD3 ? 5 ? 
AD4 ? 5 ? 
AD5 ? 2 ? 
AD6 ? 4 ? 
AD7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? parallel      
AB8 1 2 ? parallel      
AB9 1 2 ? parallel      
AB9 2 3 ? parallel      
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? parallel      
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC2 4 5 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC6 4 5 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC9 1 2 ? parallel      
AC9 2 3 ? parallel      
AD1 1 2 ? parallel      
AD2 1 2 ? parallel      
AD2 2 3 ? parallel      
AD3 1 2 ? parallel      
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD3 4 5 ? anti-parallel 
AD4 1 2 ? parallel      
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD4 4 5 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
AD7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 31  ? ALA B 36  ? GLY B 31  ALA B 36  
AA1 2 TYR B 22  ? ASN B 28  ? TYR B 22  ASN B 28  
AA1 3 GLN A 5   ? TYR A 10  ? GLN A 12  TYR A 17  
AA1 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 
AA1 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 
AA2 1 GLN A 18  ? VAL A 19  ? GLN A 25  VAL A 26  
AA2 2 VAL A 27  ? THR A 28  ? VAL A 34  THR A 35  
AA3 1 ALA A 32  ? ASP A 34  ? ALA A 39  ASP A 41  
AA3 2 VAL A 315 ? ALA A 317 ? VAL A 315 ALA A 317 
AA4 1 LEU A 36  ? GLU A 37  ? LEU A 43  GLU A 44  
AA4 2 PHE A 294 ? HIS A 295 ? PHE A 294 HIS A 295 
AA4 3 LYS A 307 ? TYR A 308 ? LYS A 307 TYR A 308 
AA5 1 LEU A 44  ? LEU A 47  ? LEU A 51  LEU A 54  
AA5 2 TYR A 274 ? THR A 279 ? TYR A 274 THR A 279 
AA6 1 LEU A 53  ? LEU A 55  ? LEU A 59  LEU A 61  
AA6 2 ILE A 82  ? GLU A 84  ? ILE A 87  GLU A 89  
AA6 3 ILE A 267 ? LYS A 269 ? ILE A 267 LYS A 269 
AA7 1 GLY A 96  ? LEU A 98  ? GLY A 100 LEU A 102 
AA7 2 ARG A 228 ? LEU A 236 ? ARG A 229 LEU A 237 
AA7 3 ASP A 174 ? HIS A 183 ? ASP A 175 HIS A 184 
AA7 4 TYR A 255 ? VAL A 260 A TYR A 256 VAL A 260 
AA7 5 HIS A 113 ? LEU A 118 ? HIS A 117 LEU A 122 
AA8 1 GLY A 96  ? LEU A 98  ? GLY A 100 LEU A 102 
AA8 2 ARG A 228 ? LEU A 236 ? ARG A 229 LEU A 237 
AA8 3 ASP A 174 ? HIS A 183 ? ASP A 175 HIS A 184 
AA8 4 PHE A 250 ? PRO A 253 ? PHE A 251 PRO A 254 
AA8 5 VAL A 150 ? TRP A 152 ? VAL A 151 TRP A 153 
AA9 1 SER A 135 ? PRO A 139 ? SER A 136 PRO A 140 
AA9 2 PRO A 144 ? SER A 145 ? PRO A 145 SER A 146 
AB1 1 ILE A 163 ? ASN A 168 ? ILE A 164 ASN A 169 
AB1 2 ALA A 241 ? SER A 246 ? ALA A 242 SER A 247 
AB1 3 ILE A 201 ? GLY A 204 ? ILE A 202 GLY A 205 
AB1 4 ASN A 209 ? LEU A 212 ? ASN A 210 LEU A 213 
AB2 1 GLY A 286 ? ALA A 287 ? GLY A 286 ALA A 287 
AB2 2 CYS A 281 ? THR A 283 ? CYS A 281 THR A 283 
AB2 3 ILE A 302 ? GLU A 304 ? ILE A 302 GLU A 304 
AB2 4 PHE B 63  ? ALA B 65  ? PHE B 63  ALA B 65  
AB3 1 GLY D 31  ? SER D 32  ? GLY D 31  SER D 32  
AB3 2 TYR D 22  ? ASN D 28  ? TYR D 22  ASN D 28  
AB3 3 ALA D 35  ? ALA D 36  ? ALA D 35  ALA D 36  
AB4 1 GLY D 31  ? SER D 32  ? GLY D 31  SER D 32  
AB4 2 TYR D 22  ? ASN D 28  ? TYR D 22  ASN D 28  
AB4 3 GLN C 5   ? TYR C 10  ? GLN C 12  TYR C 17  
AB4 4 CYS D 137 ? PHE D 140 ? CYS D 137 PHE D 140 
AB4 5 ALA D 130 ? GLU D 132 ? ALA D 130 GLU D 132 
AB5 1 GLN C 18  ? VAL C 19  ? GLN C 25  VAL C 26  
AB5 2 VAL C 27  ? THR C 28  ? VAL C 34  THR C 35  
AB6 1 ALA C 32  ? ASP C 34  ? ALA C 39  ASP C 41  
AB6 2 VAL C 315 ? ALA C 317 ? VAL C 315 ALA C 317 
AB7 1 LEU C 36  ? GLU C 37  ? LEU C 43  GLU C 44  
AB7 2 PHE C 294 ? HIS C 295 ? PHE C 294 HIS C 295 
AB7 3 LYS C 307 ? TYR C 308 ? LYS C 307 TYR C 308 
AB8 1 LEU C 44  ? LEU C 47  ? LEU C 51  LEU C 54  
AB8 2 TYR C 274 ? THR C 279 ? TYR C 274 THR C 279 
AB9 1 LEU C 53  ? ILE C 54  ? LEU C 59  ILE C 60  
AB9 2 ILE C 82  ? GLU C 84  ? ILE C 87  GLU C 89  
AB9 3 ILE C 267 ? LYS C 269 ? ILE C 267 LYS C 269 
AC1 1 GLY C 96  ? LEU C 98  ? GLY C 100 LEU C 102 
AC1 2 ARG C 228 ? LEU C 236 ? ARG C 229 LEU C 237 
AC1 3 ASP C 174 ? HIS C 183 ? ASP C 175 HIS C 184 
AC1 4 TYR C 255 ? VAL C 260 A TYR C 256 VAL C 260 
AC1 5 HIS C 113 ? LEU C 118 ? HIS C 117 LEU C 122 
AC2 1 GLY C 96  ? LEU C 98  ? GLY C 100 LEU C 102 
AC2 2 ARG C 228 ? LEU C 236 ? ARG C 229 LEU C 237 
AC2 3 ASP C 174 ? HIS C 183 ? ASP C 175 HIS C 184 
AC2 4 PHE C 250 ? PRO C 253 ? PHE C 251 PRO C 254 
AC2 5 VAL C 150 ? TRP C 152 ? VAL C 151 TRP C 153 
AC3 1 SER C 135 ? TYR C 140 ? SER C 136 TYR C 141 
AC3 2 THR C 143 ? SER C 145 ? THR C 144 SER C 146 
AC4 1 ILE C 163 ? ASN C 168 ? ILE C 164 ASN C 169 
AC4 2 ALA C 241 ? SER C 246 ? ALA C 242 SER C 247 
AC4 3 ILE C 201 ? GLY C 204 ? ILE C 202 GLY C 205 
AC4 4 ASN C 209 ? LEU C 212 ? ASN C 210 LEU C 213 
AC5 1 GLY C 286 ? ALA C 287 ? GLY C 286 ALA C 287 
AC5 2 CYS C 281 ? THR C 283 ? CYS C 281 THR C 283 
AC5 3 ILE C 302 ? GLU C 304 ? ILE C 302 GLU C 304 
AC5 4 PHE D 63  ? ALA D 65  ? PHE D 63  ALA D 65  
AC6 1 GLY F 31  ? ALA F 36  ? GLY F 31  ALA F 36  
AC6 2 TYR F 22  ? ASN F 28  ? TYR F 22  ASN F 28  
AC6 3 GLN E 5   ? TYR E 10  ? GLN E 12  TYR E 17  
AC6 4 CYS F 137 ? PHE F 140 ? CYS F 137 PHE F 140 
AC6 5 ALA F 130 ? GLU F 132 ? ALA F 130 GLU F 132 
AC7 1 GLN E 18  ? VAL E 19  ? GLN E 25  VAL E 26  
AC7 2 VAL E 27  ? THR E 28  ? VAL E 34  THR E 35  
AC8 1 ALA E 32  ? ASP E 34  ? ALA E 39  ASP E 41  
AC8 2 VAL E 315 ? ALA E 317 ? VAL E 315 ALA E 317 
AC9 1 LEU E 36  ? GLU E 37  ? LEU E 43  GLU E 44  
AC9 2 PHE E 294 ? HIS E 295 ? PHE E 294 HIS E 295 
AC9 3 LYS E 307 ? TYR E 308 ? LYS E 307 TYR E 308 
AD1 1 LEU E 44  ? LEU E 47  ? LEU E 51  LEU E 54  
AD1 2 TYR E 274 ? THR E 279 ? TYR E 274 THR E 279 
AD2 1 LEU E 53  ? ILE E 54  ? LEU E 59  ILE E 60  
AD2 2 ILE E 82  ? GLU E 84  ? ILE E 87  GLU E 89  
AD2 3 ILE E 267 ? LYS E 269 ? ILE E 267 LYS E 269 
AD3 1 GLY E 96  ? LEU E 98  ? GLY E 100 LEU E 102 
AD3 2 ARG E 228 ? LEU E 236 ? ARG E 229 LEU E 237 
AD3 3 ASP E 174 ? HIS E 183 ? ASP E 175 HIS E 184 
AD3 4 TYR E 255 ? VAL E 260 A TYR E 256 VAL E 260 
AD3 5 HIS E 113 ? LEU E 118 ? HIS E 117 LEU E 122 
AD4 1 GLY E 96  ? LEU E 98  ? GLY E 100 LEU E 102 
AD4 2 ARG E 228 ? LEU E 236 ? ARG E 229 LEU E 237 
AD4 3 ASP E 174 ? HIS E 183 ? ASP E 175 HIS E 184 
AD4 4 PHE E 250 ? PRO E 253 ? PHE E 251 PRO E 254 
AD4 5 VAL E 150 ? TRP E 152 ? VAL E 151 TRP E 153 
AD5 1 SER E 135 ? TYR E 140 ? SER E 136 TYR E 141 
AD5 2 THR E 143 ? SER E 145 ? THR E 144 SER E 146 
AD6 1 ILE E 163 ? ASN E 168 ? ILE E 164 ASN E 169 
AD6 2 ALA E 241 ? SER E 246 ? ALA E 242 SER E 247 
AD6 3 ILE E 201 ? GLY E 204 ? ILE E 202 GLY E 205 
AD6 4 ASN E 209 ? LEU E 212 ? ASN E 210 LEU E 213 
AD7 1 GLY E 286 ? ALA E 287 ? GLY E 286 ALA E 287 
AD7 2 CYS E 281 ? THR E 283 ? CYS E 281 THR E 283 
AD7 3 ILE E 302 ? GLU E 304 ? ILE E 302 GLU E 304 
AD7 4 PHE F 63  ? ALA F 65  ? PHE F 63  ALA F 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 
AA1 1 2 O ALA B 35  ? O ALA B 35  N TYR B 24  ? N TYR B 24  
AA1 2 3 O HIS B 25  ? O HIS B 25  N CYS A 7   ? N CYS A 14  
AA1 3 4 N ILE A 6   ? N ILE A 13  O PHE B 138 ? O PHE B 138 
AA1 4 5 O GLU B 139 ? O GLU B 139 N LYS B 131 ? N LYS B 131 
AA2 1 2 N VAL A 19  ? N VAL A 26  O VAL A 27  ? O VAL A 34  
AA3 1 2 N GLN A 33  ? N GLN A 40  O LEU A 316 ? O LEU A 316 
AA4 1 2 N GLU A 37  ? N GLU A 44  O PHE A 294 ? O PHE A 294 
AA4 2 3 N HIS A 295 ? N HIS A 295 O LYS A 307 ? O LYS A 307 
AA5 1 2 N ASP A 46  ? N ASP A 53  O CYS A 277 ? O CYS A 277 
AA6 1 2 N LEU A 53  ? N LEU A 59  O VAL A 83  ? O VAL A 88  
AA6 2 3 N ILE A 82  ? N ILE A 87  O MET A 268 ? O MET A 268 
AA7 1 2 N SER A 97  ? N SER A 101 O PHE A 231 ? O PHE A 232 
AA7 2 3 O LEU A 236 ? O LEU A 237 N LEU A 175 ? N LEU A 176 
AA7 3 4 N ASP A 174 ? N ASP A 175 O ILE A 259 ? O ILE A 260 
AA7 4 5 O LYS A 258 ? O LYS A 259 N GLU A 115 ? N GLU A 119 
AA8 1 2 N SER A 97  ? N SER A 101 O PHE A 231 ? O PHE A 232 
AA8 2 3 O LEU A 236 ? O LEU A 237 N LEU A 175 ? N LEU A 176 
AA8 3 4 N GLY A 180 ? N GLY A 181 O ILE A 251 ? O ILE A 252 
AA8 4 5 O ALA A 252 ? O ALA A 253 N VAL A 151 ? N VAL A 152 
AA9 1 2 N SER A 135 ? N SER A 136 O SER A 145 ? O SER A 146 
AB1 1 2 N ILE A 163 ? N ILE A 164 O SER A 246 ? O SER A 247 
AB1 2 3 O GLU A 245 ? O GLU A 246 N SER A 202 ? N SER A 203 
AB1 3 4 N ILE A 201 ? N ILE A 202 O LEU A 212 ? O LEU A 213 
AB2 1 2 O GLY A 286 ? O GLY A 286 N THR A 283 ? N THR A 283 
AB2 2 3 N GLN A 282 ? N GLN A 282 O ILE A 302 ? O ILE A 302 
AB2 3 4 N GLY A 303 ? N GLY A 303 O GLU B 64  ? O GLU B 64  
AB3 1 2 O GLY D 31  ? O GLY D 31  N ASN D 28  ? N ASN D 28  
AB3 2 3 N TYR D 24  ? N TYR D 24  O ALA D 35  ? O ALA D 35  
AB4 1 2 O GLY D 31  ? O GLY D 31  N ASN D 28  ? N ASN D 28  
AB4 2 3 O SER D 27  ? O SER D 27  N GLN C 5   ? N GLN C 12  
AB4 3 4 N ILE C 6   ? N ILE C 13  O PHE D 138 ? O PHE D 138 
AB4 4 5 O GLU D 139 ? O GLU D 139 N LYS D 131 ? N LYS D 131 
AB5 1 2 N VAL C 19  ? N VAL C 26  O VAL C 27  ? O VAL C 34  
AB6 1 2 N GLN C 33  ? N GLN C 40  O LEU C 316 ? O LEU C 316 
AB7 1 2 N GLU C 37  ? N GLU C 44  O PHE C 294 ? O PHE C 294 
AB7 2 3 N HIS C 295 ? N HIS C 295 O LYS C 307 ? O LYS C 307 
AB8 1 2 N ASP C 46  ? N ASP C 53  O CYS C 277 ? O CYS C 277 
AB9 1 2 N LEU C 53  ? N LEU C 59  O VAL C 83  ? O VAL C 88  
AB9 2 3 N ILE C 82  ? N ILE C 87  O MET C 268 ? O MET C 268 
AC1 1 2 N SER C 97  ? N SER C 101 O PHE C 231 ? O PHE C 232 
AC1 2 3 O PHE C 232 ? O PHE C 233 N TRP C 179 ? N TRP C 180 
AC1 3 4 N LEU C 176 ? N LEU C 177 O TYR C 257 ? O TYR C 258 
AC1 4 5 O LYS C 258 ? O LYS C 259 N GLU C 115 ? N GLU C 119 
AC2 1 2 N SER C 97  ? N SER C 101 O PHE C 231 ? O PHE C 232 
AC2 2 3 O PHE C 232 ? O PHE C 233 N TRP C 179 ? N TRP C 180 
AC2 3 4 N GLY C 180 ? N GLY C 181 O ILE C 251 ? O ILE C 252 
AC2 4 5 O ALA C 252 ? O ALA C 253 N VAL C 151 ? N VAL C 152 
AC3 1 2 N TYR C 140 ? N TYR C 141 O THR C 143 ? O THR C 144 
AC4 1 2 N ILE C 163 ? N ILE C 164 O SER C 246 ? O SER C 247 
AC4 2 3 O GLU C 245 ? O GLU C 246 N SER C 202 ? N SER C 203 
AC4 3 4 N VAL C 203 ? N VAL C 204 O GLN C 210 ? O GLN C 211 
AC5 1 2 O GLY C 286 ? O GLY C 286 N THR C 283 ? N THR C 283 
AC5 2 3 N GLN C 282 ? N GLN C 282 O ILE C 302 ? O ILE C 302 
AC5 3 4 N GLY C 303 ? N GLY C 303 O GLU D 64  ? O GLU D 64  
AC6 1 2 O ALA F 35  ? O ALA F 35  N TYR F 24  ? N TYR F 24  
AC6 2 3 O SER F 27  ? O SER F 27  N GLN E 5   ? N GLN E 12  
AC6 3 4 N ILE E 6   ? N ILE E 13  O PHE F 138 ? O PHE F 138 
AC6 4 5 O GLU F 139 ? O GLU F 139 N LYS F 131 ? N LYS F 131 
AC7 1 2 N VAL E 19  ? N VAL E 26  O VAL E 27  ? O VAL E 34  
AC8 1 2 N GLN E 33  ? N GLN E 40  O LEU E 316 ? O LEU E 316 
AC9 1 2 N GLU E 37  ? N GLU E 44  O PHE E 294 ? O PHE E 294 
AC9 2 3 N HIS E 295 ? N HIS E 295 O LYS E 307 ? O LYS E 307 
AD1 1 2 N ASP E 46  ? N ASP E 53  O CYS E 277 ? O CYS E 277 
AD2 1 2 N LEU E 53  ? N LEU E 59  O VAL E 83  ? O VAL E 88  
AD2 2 3 N ILE E 82  ? N ILE E 87  O MET E 268 ? O MET E 268 
AD3 1 2 N SER E 97  ? N SER E 101 O PHE E 231 ? O PHE E 232 
AD3 2 3 O PHE E 232 ? O PHE E 233 N TRP E 179 ? N TRP E 180 
AD3 3 4 N LEU E 176 ? N LEU E 177 O TYR E 257 ? O TYR E 258 
AD3 4 5 O ALA E 256 ? O ALA E 257 N ILE E 117 ? N ILE E 121 
AD4 1 2 N SER E 97  ? N SER E 101 O PHE E 231 ? O PHE E 232 
AD4 2 3 O PHE E 232 ? O PHE E 233 N TRP E 179 ? N TRP E 180 
AD4 3 4 N GLY E 180 ? N GLY E 181 O ILE E 251 ? O ILE E 252 
AD4 4 5 O ALA E 252 ? O ALA E 253 N VAL E 151 ? N VAL E 152 
AD5 1 2 N TYR E 140 ? N TYR E 141 O THR E 143 ? O THR E 144 
AD6 1 2 N ILE E 163 ? N ILE E 164 O SER E 246 ? O SER E 247 
AD6 2 3 O GLU E 245 ? O GLU E 246 N SER E 202 ? N SER E 203 
AD6 3 4 N ILE E 201 ? N ILE E 202 O LEU E 212 ? O LEU E 213 
AD7 1 2 O GLY E 286 ? O GLY E 286 N THR E 283 ? N THR E 283 
AD7 2 3 N GLN E 282 ? N GLN E 282 O ILE E 302 ? O ILE E 302 
AD7 3 4 N GLY E 303 ? N GLY E 303 O GLU F 64  ? O GLU F 64  
# 
_pdbx_entry_details.entry_id                   9NRB 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ASP A 96  ? ? -118.76 -166.97 
2  1 LEU A 96  A ? -55.89  107.52  
3  1 TRP A 127 ? ? -117.79 73.97   
4  1 ARG A 173 ? ? 67.06   -0.04   
5  1 LYS A 196 ? ? 71.04   -9.70   
6  1 THR A 206 ? ? -126.60 -169.15 
7  1 ARG B 127 ? ? 58.14   -128.07 
8  1 TRP C 127 ? ? -116.43 79.85   
9  1 LYS C 196 ? ? 71.99   -9.97   
10 1 LYS C 310 ? ? -95.95  57.88   
11 1 ARG D 127 ? ? 58.50   -127.32 
12 1 LYS E 196 ? ? 70.77   -10.28  
13 1 THR E 206 ? ? -125.71 -166.94 
14 1 ASN E 240 ? ? 68.99   -1.70   
15 1 ASN F 28  ? ? -127.16 -169.59 
16 1 ARG F 127 ? ? 56.16   -128.10 
# 
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 ASP 8   ? A ASP 1   
2  1 Y 1 A PRO 324 ? A PRO 324 
3  1 Y 1 A GLN 325 ? A GLN 325 
4  1 Y 1 A ARG 326 ? A ARG 326 
5  1 Y 1 A GLU 327 ? A GLU 327 
6  1 Y 1 A THR 328 ? A THR 328 
7  1 Y 1 B GLY 1   ? B GLY 1   
8  1 Y 1 B LEU 2   ? B LEU 2   
9  1 Y 1 B PHE 3   ? B PHE 3   
10 1 Y 1 B GLY 4   ? B GLY 4   
11 1 Y 1 B ALA 5   ? B ALA 5   
12 1 Y 1 B SER 175 ? B SER 175 
13 1 Y 1 B GLY 176 ? B GLY 176 
14 1 Y 1 B ARG 177 ? B ARG 177 
15 1 Y 1 C GLN 325 ? C GLN 325 
16 1 Y 1 C ARG 326 ? C ARG 326 
17 1 Y 1 C GLU 327 ? C GLU 327 
18 1 Y 1 C THR 328 ? C THR 328 
19 1 Y 1 D GLY 1   ? D GLY 1   
20 1 Y 1 D LEU 2   ? D LEU 2   
21 1 Y 1 D PHE 3   ? D PHE 3   
22 1 Y 1 D GLY 4   ? D GLY 4   
23 1 Y 1 D ALA 5   ? D ALA 5   
24 1 Y 1 D SER 175 ? D SER 175 
25 1 Y 1 D GLY 176 ? D GLY 176 
26 1 Y 1 D ARG 177 ? D ARG 177 
27 1 Y 1 E PRO 324 ? E PRO 324 
28 1 Y 1 E GLN 325 ? E GLN 325 
29 1 Y 1 E ARG 326 ? E ARG 326 
30 1 Y 1 E GLU 327 ? E GLU 327 
31 1 Y 1 E THR 328 ? E THR 328 
32 1 Y 1 F GLY 1   ? F GLY 1   
33 1 Y 1 F LEU 2   ? F LEU 2   
34 1 Y 1 F PHE 3   ? F PHE 3   
35 1 Y 1 F GLY 4   ? F GLY 4   
36 1 Y 1 F ALA 5   ? F ALA 5   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
BMA C1   C N R 74  
BMA C2   C N S 75  
BMA C3   C N S 76  
BMA C4   C N S 77  
BMA C5   C N R 78  
BMA C6   C N N 79  
BMA O1   O N N 80  
BMA O2   O N N 81  
BMA O3   O N N 82  
BMA O4   O N N 83  
BMA O5   O N N 84  
BMA O6   O N N 85  
BMA H1   H N N 86  
BMA H2   H N N 87  
BMA H3   H N N 88  
BMA H4   H N N 89  
BMA H5   H N N 90  
BMA H61  H N N 91  
BMA H62  H N N 92  
BMA HO1  H N N 93  
BMA HO2  H N N 94  
BMA HO3  H N N 95  
BMA HO4  H N N 96  
BMA HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
GAL C1   C N R 112 
GAL C2   C N R 113 
GAL C3   C N S 114 
GAL C4   C N R 115 
GAL C5   C N R 116 
GAL C6   C N N 117 
GAL O1   O N N 118 
GAL O2   O N N 119 
GAL O3   O N N 120 
GAL O4   O N N 121 
GAL O5   O N N 122 
GAL O6   O N N 123 
GAL H1   H N N 124 
GAL H2   H N N 125 
GAL H3   H N N 126 
GAL H4   H N N 127 
GAL H5   H N N 128 
GAL H61  H N N 129 
GAL H62  H N N 130 
GAL HO1  H N N 131 
GAL HO2  H N N 132 
GAL HO3  H N N 133 
GAL HO4  H N N 134 
GAL HO6  H N N 135 
GLN N    N N N 136 
GLN CA   C N S 137 
GLN C    C N N 138 
GLN O    O N N 139 
GLN CB   C N N 140 
GLN CG   C N N 141 
GLN CD   C N N 142 
GLN OE1  O N N 143 
GLN NE2  N N N 144 
GLN OXT  O N N 145 
GLN H    H N N 146 
GLN H2   H N N 147 
GLN HA   H N N 148 
GLN HB2  H N N 149 
GLN HB3  H N N 150 
GLN HG2  H N N 151 
GLN HG3  H N N 152 
GLN HE21 H N N 153 
GLN HE22 H N N 154 
GLN HXT  H N N 155 
GLU N    N N N 156 
GLU CA   C N S 157 
GLU C    C N N 158 
GLU O    O N N 159 
GLU CB   C N N 160 
GLU CG   C N N 161 
GLU CD   C N N 162 
GLU OE1  O N N 163 
GLU OE2  O N N 164 
GLU OXT  O N N 165 
GLU H    H N N 166 
GLU H2   H N N 167 
GLU HA   H N N 168 
GLU HB2  H N N 169 
GLU HB3  H N N 170 
GLU HG2  H N N 171 
GLU HG3  H N N 172 
GLU HE2  H N N 173 
GLU HXT  H N N 174 
GLY N    N N N 175 
GLY CA   C N N 176 
GLY C    C N N 177 
GLY O    O N N 178 
GLY OXT  O N N 179 
GLY H    H N N 180 
GLY H2   H N N 181 
GLY HA2  H N N 182 
GLY HA3  H N N 183 
GLY HXT  H N N 184 
HIS N    N N N 185 
HIS CA   C N S 186 
HIS C    C N N 187 
HIS O    O N N 188 
HIS CB   C N N 189 
HIS CG   C Y N 190 
HIS ND1  N Y N 191 
HIS CD2  C Y N 192 
HIS CE1  C Y N 193 
HIS NE2  N Y N 194 
HIS OXT  O N N 195 
HIS H    H N N 196 
HIS H2   H N N 197 
HIS HA   H N N 198 
HIS HB2  H N N 199 
HIS HB3  H N N 200 
HIS HD1  H N N 201 
HIS HD2  H N N 202 
HIS HE1  H N N 203 
HIS HE2  H N N 204 
HIS HXT  H N N 205 
HOH O    O N N 206 
HOH H1   H N N 207 
HOH H2   H N N 208 
ILE N    N N N 209 
ILE CA   C N S 210 
ILE C    C N N 211 
ILE O    O N N 212 
ILE CB   C N S 213 
ILE CG1  C N N 214 
ILE CG2  C N N 215 
ILE CD1  C N N 216 
ILE OXT  O N N 217 
ILE H    H N N 218 
ILE H2   H N N 219 
ILE HA   H N N 220 
ILE HB   H N N 221 
ILE HG12 H N N 222 
ILE HG13 H N N 223 
ILE HG21 H N N 224 
ILE HG22 H N N 225 
ILE HG23 H N N 226 
ILE HD11 H N N 227 
ILE HD12 H N N 228 
ILE HD13 H N N 229 
ILE HXT  H N N 230 
LEU N    N N N 231 
LEU CA   C N S 232 
LEU C    C N N 233 
LEU O    O N N 234 
LEU CB   C N N 235 
LEU CG   C N N 236 
LEU CD1  C N N 237 
LEU CD2  C N N 238 
LEU OXT  O N N 239 
LEU H    H N N 240 
LEU H2   H N N 241 
LEU HA   H N N 242 
LEU HB2  H N N 243 
LEU HB3  H N N 244 
LEU HG   H N N 245 
LEU HD11 H N N 246 
LEU HD12 H N N 247 
LEU HD13 H N N 248 
LEU HD21 H N N 249 
LEU HD22 H N N 250 
LEU HD23 H N N 251 
LEU HXT  H N N 252 
LYS N    N N N 253 
LYS CA   C N S 254 
LYS C    C N N 255 
LYS O    O N N 256 
LYS CB   C N N 257 
LYS CG   C N N 258 
LYS CD   C N N 259 
LYS CE   C N N 260 
LYS NZ   N N N 261 
LYS OXT  O N N 262 
LYS H    H N N 263 
LYS H2   H N N 264 
LYS HA   H N N 265 
LYS HB2  H N N 266 
LYS HB3  H N N 267 
LYS HG2  H N N 268 
LYS HG3  H N N 269 
LYS HD2  H N N 270 
LYS HD3  H N N 271 
LYS HE2  H N N 272 
LYS HE3  H N N 273 
LYS HZ1  H N N 274 
LYS HZ2  H N N 275 
LYS HZ3  H N N 276 
LYS HXT  H N N 277 
MET N    N N N 278 
MET CA   C N S 279 
MET C    C N N 280 
MET O    O N N 281 
MET CB   C N N 282 
MET CG   C N N 283 
MET SD   S N N 284 
MET CE   C N N 285 
MET OXT  O N N 286 
MET H    H N N 287 
MET H2   H N N 288 
MET HA   H N N 289 
MET HB2  H N N 290 
MET HB3  H N N 291 
MET HG2  H N N 292 
MET HG3  H N N 293 
MET HE1  H N N 294 
MET HE2  H N N 295 
MET HE3  H N N 296 
MET HXT  H N N 297 
NAG C1   C N R 298 
NAG C2   C N R 299 
NAG C3   C N R 300 
NAG C4   C N S 301 
NAG C5   C N R 302 
NAG C6   C N N 303 
NAG C7   C N N 304 
NAG C8   C N N 305 
NAG N2   N N N 306 
NAG O1   O N N 307 
NAG O3   O N N 308 
NAG O4   O N N 309 
NAG O5   O N N 310 
NAG O6   O N N 311 
NAG O7   O N N 312 
NAG H1   H N N 313 
NAG H2   H N N 314 
NAG H3   H N N 315 
NAG H4   H N N 316 
NAG H5   H N N 317 
NAG H61  H N N 318 
NAG H62  H N N 319 
NAG H81  H N N 320 
NAG H82  H N N 321 
NAG H83  H N N 322 
NAG HN2  H N N 323 
NAG HO1  H N N 324 
NAG HO3  H N N 325 
NAG HO4  H N N 326 
NAG HO6  H N N 327 
PHE N    N N N 328 
PHE CA   C N S 329 
PHE C    C N N 330 
PHE O    O N N 331 
PHE CB   C N N 332 
PHE CG   C Y N 333 
PHE CD1  C Y N 334 
PHE CD2  C Y N 335 
PHE CE1  C Y N 336 
PHE CE2  C Y N 337 
PHE CZ   C Y N 338 
PHE OXT  O N N 339 
PHE H    H N N 340 
PHE H2   H N N 341 
PHE HA   H N N 342 
PHE HB2  H N N 343 
PHE HB3  H N N 344 
PHE HD1  H N N 345 
PHE HD2  H N N 346 
PHE HE1  H N N 347 
PHE HE2  H N N 348 
PHE HZ   H N N 349 
PHE HXT  H N N 350 
PRO N    N N N 351 
PRO CA   C N S 352 
PRO C    C N N 353 
PRO O    O N N 354 
PRO CB   C N N 355 
PRO CG   C N N 356 
PRO CD   C N N 357 
PRO OXT  O N N 358 
PRO H    H N N 359 
PRO HA   H N N 360 
PRO HB2  H N N 361 
PRO HB3  H N N 362 
PRO HG2  H N N 363 
PRO HG3  H N N 364 
PRO HD2  H N N 365 
PRO HD3  H N N 366 
PRO HXT  H N N 367 
SER N    N N N 368 
SER CA   C N S 369 
SER C    C N N 370 
SER O    O N N 371 
SER CB   C N N 372 
SER OG   O N N 373 
SER OXT  O N N 374 
SER H    H N N 375 
SER H2   H N N 376 
SER HA   H N N 377 
SER HB2  H N N 378 
SER HB3  H N N 379 
SER HG   H N N 380 
SER HXT  H N N 381 
SIA C1   C N N 382 
SIA C2   C N R 383 
SIA C3   C N N 384 
SIA C4   C N S 385 
SIA C5   C N R 386 
SIA C6   C N R 387 
SIA C7   C N R 388 
SIA C8   C N R 389 
SIA C9   C N N 390 
SIA C10  C N N 391 
SIA C11  C N N 392 
SIA N5   N N N 393 
SIA O1A  O N N 394 
SIA O1B  O N N 395 
SIA O2   O N N 396 
SIA O4   O N N 397 
SIA O6   O N N 398 
SIA O7   O N N 399 
SIA O8   O N N 400 
SIA O9   O N N 401 
SIA O10  O N N 402 
SIA H32  H N N 403 
SIA H31  H N N 404 
SIA H4   H N N 405 
SIA H5   H N N 406 
SIA H6   H N N 407 
SIA H7   H N N 408 
SIA H8   H N N 409 
SIA H92  H N N 410 
SIA H91  H N N 411 
SIA H111 H N N 412 
SIA H113 H N N 413 
SIA H112 H N N 414 
SIA HN5  H N N 415 
SIA HO1B H N N 416 
SIA HO2  H N N 417 
SIA HO4  H N N 418 
SIA HO7  H N N 419 
SIA HO8  H N N 420 
SIA HO9  H N N 421 
THR N    N N N 422 
THR CA   C N S 423 
THR C    C N N 424 
THR O    O N N 425 
THR CB   C N R 426 
THR OG1  O N N 427 
THR CG2  C N N 428 
THR OXT  O N N 429 
THR H    H N N 430 
THR H2   H N N 431 
THR HA   H N N 432 
THR HB   H N N 433 
THR HG1  H N N 434 
THR HG21 H N N 435 
THR HG22 H N N 436 
THR HG23 H N N 437 
THR HXT  H N N 438 
TRP N    N N N 439 
TRP CA   C N S 440 
TRP C    C N N 441 
TRP O    O N N 442 
TRP CB   C N N 443 
TRP CG   C Y N 444 
TRP CD1  C Y N 445 
TRP CD2  C Y N 446 
TRP NE1  N Y N 447 
TRP CE2  C Y N 448 
TRP CE3  C Y N 449 
TRP CZ2  C Y N 450 
TRP CZ3  C Y N 451 
TRP CH2  C Y N 452 
TRP OXT  O N N 453 
TRP H    H N N 454 
TRP H2   H N N 455 
TRP HA   H N N 456 
TRP HB2  H N N 457 
TRP HB3  H N N 458 
TRP HD1  H N N 459 
TRP HE1  H N N 460 
TRP HE3  H N N 461 
TRP HZ2  H N N 462 
TRP HZ3  H N N 463 
TRP HH2  H N N 464 
TRP HXT  H N N 465 
TYR N    N N N 466 
TYR CA   C N S 467 
TYR C    C N N 468 
TYR O    O N N 469 
TYR CB   C N N 470 
TYR CG   C Y N 471 
TYR CD1  C Y N 472 
TYR CD2  C Y N 473 
TYR CE1  C Y N 474 
TYR CE2  C Y N 475 
TYR CZ   C Y N 476 
TYR OH   O N N 477 
TYR OXT  O N N 478 
TYR H    H N N 479 
TYR H2   H N N 480 
TYR HA   H N N 481 
TYR HB2  H N N 482 
TYR HB3  H N N 483 
TYR HD1  H N N 484 
TYR HD2  H N N 485 
TYR HE1  H N N 486 
TYR HE2  H N N 487 
TYR HH   H N N 488 
TYR HXT  H N N 489 
VAL N    N N N 490 
VAL CA   C N S 491 
VAL C    C N N 492 
VAL O    O N N 493 
VAL CB   C N N 494 
VAL CG1  C N N 495 
VAL CG2  C N N 496 
VAL OXT  O N N 497 
VAL H    H N N 498 
VAL H2   H N N 499 
VAL HA   H N N 500 
VAL HB   H N N 501 
VAL HG11 H N N 502 
VAL HG12 H N N 503 
VAL HG13 H N N 504 
VAL HG21 H N N 505 
VAL HG22 H N N 506 
VAL HG23 H N N 507 
VAL HXT  H N N 508 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GAL C1  C2   sing N N 107 
GAL C1  O1   sing N N 108 
GAL C1  O5   sing N N 109 
GAL C1  H1   sing N N 110 
GAL C2  C3   sing N N 111 
GAL C2  O2   sing N N 112 
GAL C2  H2   sing N N 113 
GAL C3  C4   sing N N 114 
GAL C3  O3   sing N N 115 
GAL C3  H3   sing N N 116 
GAL C4  C5   sing N N 117 
GAL C4  O4   sing N N 118 
GAL C4  H4   sing N N 119 
GAL C5  C6   sing N N 120 
GAL C5  O5   sing N N 121 
GAL C5  H5   sing N N 122 
GAL C6  O6   sing N N 123 
GAL C6  H61  sing N N 124 
GAL C6  H62  sing N N 125 
GAL O1  HO1  sing N N 126 
GAL O2  HO2  sing N N 127 
GAL O3  HO3  sing N N 128 
GAL O4  HO4  sing N N 129 
GAL O6  HO6  sing N N 130 
GLN N   CA   sing N N 131 
GLN N   H    sing N N 132 
GLN N   H2   sing N N 133 
GLN CA  C    sing N N 134 
GLN CA  CB   sing N N 135 
GLN CA  HA   sing N N 136 
GLN C   O    doub N N 137 
GLN C   OXT  sing N N 138 
GLN CB  CG   sing N N 139 
GLN CB  HB2  sing N N 140 
GLN CB  HB3  sing N N 141 
GLN CG  CD   sing N N 142 
GLN CG  HG2  sing N N 143 
GLN CG  HG3  sing N N 144 
GLN CD  OE1  doub N N 145 
GLN CD  NE2  sing N N 146 
GLN NE2 HE21 sing N N 147 
GLN NE2 HE22 sing N N 148 
GLN OXT HXT  sing N N 149 
GLU N   CA   sing N N 150 
GLU N   H    sing N N 151 
GLU N   H2   sing N N 152 
GLU CA  C    sing N N 153 
GLU CA  CB   sing N N 154 
GLU CA  HA   sing N N 155 
GLU C   O    doub N N 156 
GLU C   OXT  sing N N 157 
GLU CB  CG   sing N N 158 
GLU CB  HB2  sing N N 159 
GLU CB  HB3  sing N N 160 
GLU CG  CD   sing N N 161 
GLU CG  HG2  sing N N 162 
GLU CG  HG3  sing N N 163 
GLU CD  OE1  doub N N 164 
GLU CD  OE2  sing N N 165 
GLU OE2 HE2  sing N N 166 
GLU OXT HXT  sing N N 167 
GLY N   CA   sing N N 168 
GLY N   H    sing N N 169 
GLY N   H2   sing N N 170 
GLY CA  C    sing N N 171 
GLY CA  HA2  sing N N 172 
GLY CA  HA3  sing N N 173 
GLY C   O    doub N N 174 
GLY C   OXT  sing N N 175 
GLY OXT HXT  sing N N 176 
HIS N   CA   sing N N 177 
HIS N   H    sing N N 178 
HIS N   H2   sing N N 179 
HIS CA  C    sing N N 180 
HIS CA  CB   sing N N 181 
HIS CA  HA   sing N N 182 
HIS C   O    doub N N 183 
HIS C   OXT  sing N N 184 
HIS CB  CG   sing N N 185 
HIS CB  HB2  sing N N 186 
HIS CB  HB3  sing N N 187 
HIS CG  ND1  sing Y N 188 
HIS CG  CD2  doub Y N 189 
HIS ND1 CE1  doub Y N 190 
HIS ND1 HD1  sing N N 191 
HIS CD2 NE2  sing Y N 192 
HIS CD2 HD2  sing N N 193 
HIS CE1 NE2  sing Y N 194 
HIS CE1 HE1  sing N N 195 
HIS NE2 HE2  sing N N 196 
HIS OXT HXT  sing N N 197 
HOH O   H1   sing N N 198 
HOH O   H2   sing N N 199 
ILE N   CA   sing N N 200 
ILE N   H    sing N N 201 
ILE N   H2   sing N N 202 
ILE CA  C    sing N N 203 
ILE CA  CB   sing N N 204 
ILE CA  HA   sing N N 205 
ILE C   O    doub N N 206 
ILE C   OXT  sing N N 207 
ILE CB  CG1  sing N N 208 
ILE CB  CG2  sing N N 209 
ILE CB  HB   sing N N 210 
ILE CG1 CD1  sing N N 211 
ILE CG1 HG12 sing N N 212 
ILE CG1 HG13 sing N N 213 
ILE CG2 HG21 sing N N 214 
ILE CG2 HG22 sing N N 215 
ILE CG2 HG23 sing N N 216 
ILE CD1 HD11 sing N N 217 
ILE CD1 HD12 sing N N 218 
ILE CD1 HD13 sing N N 219 
ILE OXT HXT  sing N N 220 
LEU N   CA   sing N N 221 
LEU N   H    sing N N 222 
LEU N   H2   sing N N 223 
LEU CA  C    sing N N 224 
LEU CA  CB   sing N N 225 
LEU CA  HA   sing N N 226 
LEU C   O    doub N N 227 
LEU C   OXT  sing N N 228 
LEU CB  CG   sing N N 229 
LEU CB  HB2  sing N N 230 
LEU CB  HB3  sing N N 231 
LEU CG  CD1  sing N N 232 
LEU CG  CD2  sing N N 233 
LEU CG  HG   sing N N 234 
LEU CD1 HD11 sing N N 235 
LEU CD1 HD12 sing N N 236 
LEU CD1 HD13 sing N N 237 
LEU CD2 HD21 sing N N 238 
LEU CD2 HD22 sing N N 239 
LEU CD2 HD23 sing N N 240 
LEU OXT HXT  sing N N 241 
LYS N   CA   sing N N 242 
LYS N   H    sing N N 243 
LYS N   H2   sing N N 244 
LYS CA  C    sing N N 245 
LYS CA  CB   sing N N 246 
LYS CA  HA   sing N N 247 
LYS C   O    doub N N 248 
LYS C   OXT  sing N N 249 
LYS CB  CG   sing N N 250 
LYS CB  HB2  sing N N 251 
LYS CB  HB3  sing N N 252 
LYS CG  CD   sing N N 253 
LYS CG  HG2  sing N N 254 
LYS CG  HG3  sing N N 255 
LYS CD  CE   sing N N 256 
LYS CD  HD2  sing N N 257 
LYS CD  HD3  sing N N 258 
LYS CE  NZ   sing N N 259 
LYS CE  HE2  sing N N 260 
LYS CE  HE3  sing N N 261 
LYS NZ  HZ1  sing N N 262 
LYS NZ  HZ2  sing N N 263 
LYS NZ  HZ3  sing N N 264 
LYS OXT HXT  sing N N 265 
MET N   CA   sing N N 266 
MET N   H    sing N N 267 
MET N   H2   sing N N 268 
MET CA  C    sing N N 269 
MET CA  CB   sing N N 270 
MET CA  HA   sing N N 271 
MET C   O    doub N N 272 
MET C   OXT  sing N N 273 
MET CB  CG   sing N N 274 
MET CB  HB2  sing N N 275 
MET CB  HB3  sing N N 276 
MET CG  SD   sing N N 277 
MET CG  HG2  sing N N 278 
MET CG  HG3  sing N N 279 
MET SD  CE   sing N N 280 
MET CE  HE1  sing N N 281 
MET CE  HE2  sing N N 282 
MET CE  HE3  sing N N 283 
MET OXT HXT  sing N N 284 
NAG C1  C2   sing N N 285 
NAG C1  O1   sing N N 286 
NAG C1  O5   sing N N 287 
NAG C1  H1   sing N N 288 
NAG C2  C3   sing N N 289 
NAG C2  N2   sing N N 290 
NAG C2  H2   sing N N 291 
NAG C3  C4   sing N N 292 
NAG C3  O3   sing N N 293 
NAG C3  H3   sing N N 294 
NAG C4  C5   sing N N 295 
NAG C4  O4   sing N N 296 
NAG C4  H4   sing N N 297 
NAG C5  C6   sing N N 298 
NAG C5  O5   sing N N 299 
NAG C5  H5   sing N N 300 
NAG C6  O6   sing N N 301 
NAG C6  H61  sing N N 302 
NAG C6  H62  sing N N 303 
NAG C7  C8   sing N N 304 
NAG C7  N2   sing N N 305 
NAG C7  O7   doub N N 306 
NAG C8  H81  sing N N 307 
NAG C8  H82  sing N N 308 
NAG C8  H83  sing N N 309 
NAG N2  HN2  sing N N 310 
NAG O1  HO1  sing N N 311 
NAG O3  HO3  sing N N 312 
NAG O4  HO4  sing N N 313 
NAG O6  HO6  sing N N 314 
PHE N   CA   sing N N 315 
PHE N   H    sing N N 316 
PHE N   H2   sing N N 317 
PHE CA  C    sing N N 318 
PHE CA  CB   sing N N 319 
PHE CA  HA   sing N N 320 
PHE C   O    doub N N 321 
PHE C   OXT  sing N N 322 
PHE CB  CG   sing N N 323 
PHE CB  HB2  sing N N 324 
PHE CB  HB3  sing N N 325 
PHE CG  CD1  doub Y N 326 
PHE CG  CD2  sing Y N 327 
PHE CD1 CE1  sing Y N 328 
PHE CD1 HD1  sing N N 329 
PHE CD2 CE2  doub Y N 330 
PHE CD2 HD2  sing N N 331 
PHE CE1 CZ   doub Y N 332 
PHE CE1 HE1  sing N N 333 
PHE CE2 CZ   sing Y N 334 
PHE CE2 HE2  sing N N 335 
PHE CZ  HZ   sing N N 336 
PHE OXT HXT  sing N N 337 
PRO N   CA   sing N N 338 
PRO N   CD   sing N N 339 
PRO N   H    sing N N 340 
PRO CA  C    sing N N 341 
PRO CA  CB   sing N N 342 
PRO CA  HA   sing N N 343 
PRO C   O    doub N N 344 
PRO C   OXT  sing N N 345 
PRO CB  CG   sing N N 346 
PRO CB  HB2  sing N N 347 
PRO CB  HB3  sing N N 348 
PRO CG  CD   sing N N 349 
PRO CG  HG2  sing N N 350 
PRO CG  HG3  sing N N 351 
PRO CD  HD2  sing N N 352 
PRO CD  HD3  sing N N 353 
PRO OXT HXT  sing N N 354 
SER N   CA   sing N N 355 
SER N   H    sing N N 356 
SER N   H2   sing N N 357 
SER CA  C    sing N N 358 
SER CA  CB   sing N N 359 
SER CA  HA   sing N N 360 
SER C   O    doub N N 361 
SER C   OXT  sing N N 362 
SER CB  OG   sing N N 363 
SER CB  HB2  sing N N 364 
SER CB  HB3  sing N N 365 
SER OG  HG   sing N N 366 
SER OXT HXT  sing N N 367 
SIA C1  C2   sing N N 368 
SIA C1  O1A  doub N N 369 
SIA C1  O1B  sing N N 370 
SIA C2  C3   sing N N 371 
SIA C2  O2   sing N N 372 
SIA C2  O6   sing N N 373 
SIA C3  C4   sing N N 374 
SIA C3  H32  sing N N 375 
SIA C3  H31  sing N N 376 
SIA C4  C5   sing N N 377 
SIA C4  O4   sing N N 378 
SIA C4  H4   sing N N 379 
SIA C5  C6   sing N N 380 
SIA C5  N5   sing N N 381 
SIA C5  H5   sing N N 382 
SIA C6  C7   sing N N 383 
SIA C6  O6   sing N N 384 
SIA C6  H6   sing N N 385 
SIA C7  C8   sing N N 386 
SIA C7  O7   sing N N 387 
SIA C7  H7   sing N N 388 
SIA C8  C9   sing N N 389 
SIA C8  O8   sing N N 390 
SIA C8  H8   sing N N 391 
SIA C9  O9   sing N N 392 
SIA C9  H92  sing N N 393 
SIA C9  H91  sing N N 394 
SIA C10 C11  sing N N 395 
SIA C10 N5   sing N N 396 
SIA C10 O10  doub N N 397 
SIA C11 H111 sing N N 398 
SIA C11 H113 sing N N 399 
SIA C11 H112 sing N N 400 
SIA N5  HN5  sing N N 401 
SIA O1B HO1B sing N N 402 
SIA O2  HO2  sing N N 403 
SIA O4  HO4  sing N N 404 
SIA O7  HO7  sing N N 405 
SIA O8  HO8  sing N N 406 
SIA O9  HO9  sing N N 407 
THR N   CA   sing N N 408 
THR N   H    sing N N 409 
THR N   H2   sing N N 410 
THR CA  C    sing N N 411 
THR CA  CB   sing N N 412 
THR CA  HA   sing N N 413 
THR C   O    doub N N 414 
THR C   OXT  sing N N 415 
THR CB  OG1  sing N N 416 
THR CB  CG2  sing N N 417 
THR CB  HB   sing N N 418 
THR OG1 HG1  sing N N 419 
THR CG2 HG21 sing N N 420 
THR CG2 HG22 sing N N 421 
THR CG2 HG23 sing N N 422 
THR OXT HXT  sing N N 423 
TRP N   CA   sing N N 424 
TRP N   H    sing N N 425 
TRP N   H2   sing N N 426 
TRP CA  C    sing N N 427 
TRP CA  CB   sing N N 428 
TRP CA  HA   sing N N 429 
TRP C   O    doub N N 430 
TRP C   OXT  sing N N 431 
TRP CB  CG   sing N N 432 
TRP CB  HB2  sing N N 433 
TRP CB  HB3  sing N N 434 
TRP CG  CD1  doub Y N 435 
TRP CG  CD2  sing Y N 436 
TRP CD1 NE1  sing Y N 437 
TRP CD1 HD1  sing N N 438 
TRP CD2 CE2  doub Y N 439 
TRP CD2 CE3  sing Y N 440 
TRP NE1 CE2  sing Y N 441 
TRP NE1 HE1  sing N N 442 
TRP CE2 CZ2  sing Y N 443 
TRP CE3 CZ3  doub Y N 444 
TRP CE3 HE3  sing N N 445 
TRP CZ2 CH2  doub Y N 446 
TRP CZ2 HZ2  sing N N 447 
TRP CZ3 CH2  sing Y N 448 
TRP CZ3 HZ3  sing N N 449 
TRP CH2 HH2  sing N N 450 
TRP OXT HXT  sing N N 451 
TYR N   CA   sing N N 452 
TYR N   H    sing N N 453 
TYR N   H2   sing N N 454 
TYR CA  C    sing N N 455 
TYR CA  CB   sing N N 456 
TYR CA  HA   sing N N 457 
TYR C   O    doub N N 458 
TYR C   OXT  sing N N 459 
TYR CB  CG   sing N N 460 
TYR CB  HB2  sing N N 461 
TYR CB  HB3  sing N N 462 
TYR CG  CD1  doub Y N 463 
TYR CG  CD2  sing Y N 464 
TYR CD1 CE1  sing Y N 465 
TYR CD1 HD1  sing N N 466 
TYR CD2 CE2  doub Y N 467 
TYR CD2 HD2  sing N N 468 
TYR CE1 CZ   doub Y N 469 
TYR CE1 HE1  sing N N 470 
TYR CE2 CZ   sing Y N 471 
TYR CE2 HE2  sing N N 472 
TYR CZ  OH   sing N N 473 
TYR OH  HH   sing N N 474 
TYR OXT HXT  sing N N 475 
VAL N   CA   sing N N 476 
VAL N   H    sing N N 477 
VAL N   H2   sing N N 478 
VAL CA  C    sing N N 479 
VAL CA  CB   sing N N 480 
VAL CA  HA   sing N N 481 
VAL C   O    doub N N 482 
VAL C   OXT  sing N N 483 
VAL CB  CG1  sing N N 484 
VAL CB  CG2  sing N N 485 
VAL CB  HB   sing N N 486 
VAL CG1 HG11 sing N N 487 
VAL CG1 HG12 sing N N 488 
VAL CG1 HG13 sing N N 489 
VAL CG2 HG21 sing N N 490 
VAL CG2 HG22 sing N N 491 
VAL CG2 HG23 sing N N 492 
VAL OXT HXT  sing N N 493 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           75N93021C00015 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
3 BMA 3 n 
4 NAG 1 n 
4 NAG 2 n 
5 GAL 1 n 
5 NAG 2 n 
5 GAL 3 n 
5 SIA 4 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5E30 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9NRB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.010426 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005669 
_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]   0.004417 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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   . PRO A 1 2   ? 34.471  7.069   -102.218 1.00 115.37 ? 9   PRO A N   1 
ATOM   2     C CA  . PRO A 1 2   ? 34.903  7.594   -100.919 1.00 121.81 ? 9   PRO A CA  1 
ATOM   3     C C   . PRO A 1 2   ? 36.301  7.125   -100.525 1.00 120.62 ? 9   PRO A C   1 
ATOM   4     O O   . PRO A 1 2   ? 37.056  6.653   -101.375 1.00 101.00 ? 9   PRO A O   1 
ATOM   5     C CB  . PRO A 1 2   ? 33.853  7.039   -99.958  1.00 98.30  ? 9   PRO A CB  1 
ATOM   6     C CG  . PRO A 1 2   ? 32.630  6.915   -100.787 1.00 84.04  ? 9   PRO A CG  1 
ATOM   7     C CD  . PRO A 1 2   ? 33.107  6.512   -102.158 1.00 97.09  ? 9   PRO A CD  1 
ATOM   8     N N   . GLY A 1 3   ? 36.635  7.263   -99.247  1.00 114.39 ? 10  GLY A N   1 
ATOM   9     C CA  . GLY A 1 3   ? 37.920  6.811   -98.754  1.00 98.23  ? 10  GLY A CA  1 
ATOM   10    C C   . GLY A 1 3   ? 38.204  7.386   -97.384  1.00 82.80  ? 10  GLY A C   1 
ATOM   11    O O   . GLY A 1 3   ? 37.423  8.172   -96.836  1.00 95.32  ? 10  GLY A O   1 
ATOM   12    N N   . ASP A 1 4   ? 39.353  6.977   -96.841  1.00 89.81  ? 11  ASP A N   1 
ATOM   13    C CA  . ASP A 1 4   ? 39.868  7.468   -95.560  1.00 91.32  ? 11  ASP A CA  1 
ATOM   14    C C   . ASP A 1 4   ? 38.874  7.204   -94.423  1.00 85.79  ? 11  ASP A C   1 
ATOM   15    O O   . ASP A 1 4   ? 38.260  8.111   -93.859  1.00 93.31  ? 11  ASP A O   1 
ATOM   16    C CB  . ASP A 1 4   ? 40.241  8.952   -95.645  1.00 87.47  ? 11  ASP A CB  1 
ATOM   17    C CG  . ASP A 1 4   ? 41.569  9.176   -96.338  1.00 79.77  ? 11  ASP A CG  1 
ATOM   18    O OD1 . ASP A 1 4   ? 41.982  8.299   -97.126  1.00 77.42  ? 11  ASP A OD1 1 
ATOM   19    O OD2 . ASP A 1 4   ? 42.206  10.220  -96.085  1.00 81.63  ? 11  ASP A OD2 1 
ATOM   20    N N   . GLN A 1 5   ? 38.713  5.917   -94.125  1.00 80.07  ? 12  GLN A N   1 
ATOM   21    C CA  . GLN A 1 5   ? 37.869  5.462   -93.031  1.00 80.11  ? 12  GLN A CA  1 
ATOM   22    C C   . GLN A 1 5   ? 38.699  5.066   -91.813  1.00 75.62  ? 12  GLN A C   1 
ATOM   23    O O   . GLN A 1 5   ? 39.859  4.665   -91.930  1.00 82.40  ? 12  GLN A O   1 
ATOM   24    C CB  . GLN A 1 5   ? 37.013  4.269   -93.459  1.00 74.34  ? 12  GLN A CB  1 
ATOM   25    C CG  . GLN A 1 5   ? 35.856  4.615   -94.372  1.00 85.06  ? 12  GLN A CG  1 
ATOM   26    C CD  . GLN A 1 5   ? 35.216  3.380   -94.970  1.00 82.95  ? 12  GLN A CD  1 
ATOM   27    O OE1 . GLN A 1 5   ? 35.781  2.288   -94.916  1.00 93.10  ? 12  GLN A OE1 1 
ATOM   28    N NE2 . GLN A 1 5   ? 34.032  3.546   -95.546  1.00 100.42 ? 12  GLN A NE2 1 
ATOM   29    N N   . ILE A 1 6   ? 38.084  5.190   -90.637  1.00 75.28  ? 13  ILE A N   1 
ATOM   30    C CA  . ILE A 1 6   ? 38.600  4.615   -89.399  1.00 67.07  ? 13  ILE A CA  1 
ATOM   31    C C   . ILE A 1 6   ? 37.434  3.964   -88.666  1.00 75.50  ? 13  ILE A C   1 
ATOM   32    O O   . ILE A 1 6   ? 36.323  4.507   -88.635  1.00 80.97  ? 13  ILE A O   1 
ATOM   33    C CB  . ILE A 1 6   ? 39.315  5.665   -88.518  1.00 71.21  ? 13  ILE A CB  1 
ATOM   34    C CG1 . ILE A 1 6   ? 40.037  4.983   -87.352  1.00 64.26  ? 13  ILE A CG1 1 
ATOM   35    C CG2 . ILE A 1 6   ? 38.339  6.722   -88.011  1.00 53.69  ? 13  ILE A CG2 1 
ATOM   36    C CD1 . ILE A 1 6   ? 40.933  5.909   -86.551  1.00 56.96  ? 13  ILE A CD1 1 
ATOM   37    N N   . CYS A 1 7   ? 37.679  2.784   -88.098  1.00 70.68  ? 14  CYS A N   1 
ATOM   38    C CA  . CYS A 1 7   ? 36.623  1.961   -87.526  1.00 73.86  ? 14  CYS A CA  1 
ATOM   39    C C   . CYS A 1 7   ? 36.978  1.555   -86.102  1.00 68.09  ? 14  CYS A C   1 
ATOM   40    O O   . CYS A 1 7   ? 38.145  1.546   -85.703  1.00 80.30  ? 14  CYS A O   1 
ATOM   41    C CB  . CYS A 1 7   ? 36.366  0.701   -88.367  1.00 62.81  ? 14  CYS A CB  1 
ATOM   42    S SG  . CYS A 1 7   ? 35.937  0.990   -90.102  1.00 113.71 ? 14  CYS A SG  1 
ATOM   43    N N   . ILE A 1 8   ? 35.941  1.229   -85.333  1.00 74.64  ? 15  ILE A N   1 
ATOM   44    C CA  . ILE A 1 8   ? 36.076  0.725   -83.970  1.00 68.44  ? 15  ILE A CA  1 
ATOM   45    C C   . ILE A 1 8   ? 35.597  -0.721  -83.953  1.00 69.38  ? 15  ILE A C   1 
ATOM   46    O O   . ILE A 1 8   ? 34.499  -1.022  -84.436  1.00 75.73  ? 15  ILE A O   1 
ATOM   47    C CB  . ILE A 1 8   ? 35.274  1.573   -82.968  1.00 74.27  ? 15  ILE A CB  1 
ATOM   48    C CG1 . ILE A 1 8   ? 35.474  3.066   -83.246  1.00 84.72  ? 15  ILE A CG1 1 
ATOM   49    C CG2 . ILE A 1 8   ? 35.692  1.237   -81.530  1.00 70.20  ? 15  ILE A CG2 1 
ATOM   50    C CD1 . ILE A 1 8   ? 36.868  3.571   -82.956  1.00 71.24  ? 15  ILE A CD1 1 
ATOM   51    N N   . GLY A 1 9   ? 36.419  -1.613  -83.407  1.00 74.59  ? 16  GLY A N   1 
ATOM   52    C CA  . GLY A 1 9   ? 36.090  -3.021  -83.333  1.00 69.78  ? 16  GLY A CA  1 
ATOM   53    C C   . GLY A 1 9   ? 36.745  -3.639  -82.123  1.00 76.30  ? 16  GLY A C   1 
ATOM   54    O O   . GLY A 1 9   ? 37.371  -2.951  -81.318  1.00 74.03  ? 16  GLY A O   1 
ATOM   55    N N   . TYR A 1 10  ? 36.596  -4.954  -82.000  1.00 68.51  ? 17  TYR A N   1 
ATOM   56    C CA  . TYR A 1 10  ? 37.082  -5.671  -80.832  1.00 71.47  ? 17  TYR A CA  1 
ATOM   57    C C   . TYR A 1 10  ? 37.591  -7.049  -81.236  1.00 73.51  ? 17  TYR A C   1 
ATOM   58    O O   . TYR A 1 10  ? 37.415  -7.497  -82.371  1.00 63.57  ? 17  TYR A O   1 
ATOM   59    C CB  . TYR A 1 10  ? 35.999  -5.807  -79.756  1.00 70.62  ? 17  TYR A CB  1 
ATOM   60    C CG  . TYR A 1 10  ? 34.727  -6.501  -80.197  1.00 81.79  ? 17  TYR A CG  1 
ATOM   61    C CD1 . TYR A 1 10  ? 33.646  -5.769  -80.684  1.00 77.91  ? 17  TYR A CD1 1 
ATOM   62    C CD2 . TYR A 1 10  ? 34.603  -7.880  -80.118  1.00 82.47  ? 17  TYR A CD2 1 
ATOM   63    C CE1 . TYR A 1 10  ? 32.479  -6.403  -81.080  1.00 83.29  ? 17  TYR A CE1 1 
ATOM   64    C CE2 . TYR A 1 10  ? 33.450  -8.516  -80.513  1.00 88.06  ? 17  TYR A CE2 1 
ATOM   65    C CZ  . TYR A 1 10  ? 32.390  -7.776  -80.993  1.00 94.37  ? 17  TYR A CZ  1 
ATOM   66    O OH  . TYR A 1 10  ? 31.237  -8.413  -81.387  1.00 96.02  ? 17  TYR A OH  1 
ATOM   67    N N   . HIS A 1 11  ? 38.216  -7.721  -80.268  1.00 79.35  ? 18  HIS A N   1 
ATOM   68    C CA  . HIS A 1 11  ? 38.911  -8.981  -80.496  1.00 76.60  ? 18  HIS A CA  1 
ATOM   69    C C   . HIS A 1 11  ? 37.937  -10.138 -80.674  1.00 74.88  ? 18  HIS A C   1 
ATOM   70    O O   . HIS A 1 11  ? 36.887  -10.200 -80.028  1.00 72.59  ? 18  HIS A O   1 
ATOM   71    C CB  . HIS A 1 11  ? 39.850  -9.265  -79.315  1.00 78.10  ? 18  HIS A CB  1 
ATOM   72    C CG  . HIS A 1 11  ? 40.555  -10.583 -79.387  1.00 88.86  ? 18  HIS A CG  1 
ATOM   73    N ND1 . HIS A 1 11  ? 40.897  -11.299 -78.260  1.00 89.78  ? 18  HIS A ND1 1 
ATOM   74    C CD2 . HIS A 1 11  ? 41.001  -11.303 -80.442  1.00 97.15  ? 18  HIS A CD2 1 
ATOM   75    C CE1 . HIS A 1 11  ? 41.512  -12.411 -78.620  1.00 93.93  ? 18  HIS A CE1 1 
ATOM   76    N NE2 . HIS A 1 11  ? 41.586  -12.438 -79.938  1.00 110.47 ? 18  HIS A NE2 1 
ATOM   77    N N   . ALA A 1 12  ? 38.297  -11.056 -81.570  1.00 71.63  ? 19  ALA A N   1 
ATOM   78    C CA  . ALA A 1 12  ? 37.622  -12.333 -81.721  1.00 73.84  ? 19  ALA A CA  1 
ATOM   79    C C   . ALA A 1 12  ? 38.664  -13.393 -82.045  1.00 85.65  ? 19  ALA A C   1 
ATOM   80    O O   . ALA A 1 12  ? 39.704  -13.099 -82.639  1.00 93.48  ? 19  ALA A O   1 
ATOM   81    C CB  . ALA A 1 12  ? 36.550  -12.290 -82.817  1.00 66.00  ? 19  ALA A CB  1 
ATOM   82    N N   . ASN A 1 13  ? 38.379  -14.631 -81.648  1.00 84.77  ? 20  ASN A N   1 
ATOM   83    C CA  . ASN A 1 13  ? 39.286  -15.746 -81.903  1.00 71.60  ? 20  ASN A CA  1 
ATOM   84    C C   . ASN A 1 13  ? 38.455  -16.996 -82.176  1.00 69.20  ? 20  ASN A C   1 
ATOM   85    O O   . ASN A 1 13  ? 37.228  -16.938 -82.303  1.00 77.88  ? 20  ASN A O   1 
ATOM   86    C CB  . ASN A 1 13  ? 40.271  -15.931 -80.739  1.00 71.94  ? 20  ASN A CB  1 
ATOM   87    C CG  . ASN A 1 13  ? 39.583  -15.998 -79.387  1.00 94.51  ? 20  ASN A CG  1 
ATOM   88    O OD1 . ASN A 1 13  ? 38.400  -16.325 -79.291  1.00 83.81  ? 20  ASN A OD1 1 
ATOM   89    N ND2 . ASN A 1 13  ? 40.327  -15.687 -78.331  1.00 96.70  ? 20  ASN A ND2 1 
ATOM   90    N N   . ASN A 1 14  ? 39.133  -18.139 -82.263  1.00 76.45  ? 21  ASN A N   1 
ATOM   91    C CA  . ASN A 1 14  ? 38.505  -19.413 -82.584  1.00 86.46  ? 21  ASN A CA  1 
ATOM   92    C C   . ASN A 1 14  ? 38.029  -20.170 -81.350  1.00 99.48  ? 21  ASN A C   1 
ATOM   93    O O   . ASN A 1 14  ? 37.637  -21.336 -81.468  1.00 96.97  ? 21  ASN A O   1 
ATOM   94    C CB  . ASN A 1 14  ? 39.475  -20.287 -83.387  1.00 93.68  ? 21  ASN A CB  1 
ATOM   95    C CG  . ASN A 1 14  ? 40.886  -20.259 -82.826  1.00 111.19 ? 21  ASN A CG  1 
ATOM   96    O OD1 . ASN A 1 14  ? 41.136  -19.670 -81.774  1.00 103.72 ? 21  ASN A OD1 1 
ATOM   97    N ND2 . ASN A 1 14  ? 41.816  -20.898 -83.527  1.00 104.84 ? 21  ASN A ND2 1 
ATOM   98    N N   . SER A 1 15  ? 38.065  -19.541 -80.178  1.00 89.12  ? 22  SER A N   1 
ATOM   99    C CA  . SER A 1 15  ? 37.658  -20.210 -78.950  1.00 93.47  ? 22  SER A CA  1 
ATOM   100   C C   . SER A 1 15  ? 36.197  -20.639 -79.011  1.00 88.82  ? 22  SER A C   1 
ATOM   101   O O   . SER A 1 15  ? 35.324  -19.883 -79.447  1.00 88.51  ? 22  SER A O   1 
ATOM   102   C CB  . SER A 1 15  ? 37.877  -19.289 -77.751  1.00 96.55  ? 22  SER A CB  1 
ATOM   103   O OG  . SER A 1 15  ? 37.242  -19.800 -76.591  1.00 80.09  ? 22  SER A OG  1 
ATOM   104   N N   . THR A 1 16  ? 35.938  -21.871 -78.573  1.00 89.43  ? 23  THR A N   1 
ATOM   105   C CA  . THR A 1 16  ? 34.587  -22.400 -78.447  1.00 85.94  ? 23  THR A CA  1 
ATOM   106   C C   . THR A 1 16  ? 34.126  -22.477 -76.997  1.00 94.56  ? 23  THR A C   1 
ATOM   107   O O   . THR A 1 16  ? 33.056  -23.036 -76.727  1.00 90.62  ? 23  THR A O   1 
ATOM   108   C CB  . THR A 1 16  ? 34.493  -23.783 -79.098  1.00 87.69  ? 23  THR A CB  1 
ATOM   109   O OG1 . THR A 1 16  ? 35.572  -24.607 -78.637  1.00 82.88  ? 23  THR A OG1 1 
ATOM   110   C CG2 . THR A 1 16  ? 34.556  -23.668 -80.615  1.00 89.33  ? 23  THR A CG2 1 
ATOM   111   N N   . GLU A 1 17  ? 34.905  -21.933 -76.061  1.00 100.69 ? 24  GLU A N   1 
ATOM   112   C CA  . GLU A 1 17  ? 34.544  -21.985 -74.650  1.00 85.37  ? 24  GLU A CA  1 
ATOM   113   C C   . GLU A 1 17  ? 33.219  -21.275 -74.405  1.00 80.23  ? 24  GLU A C   1 
ATOM   114   O O   . GLU A 1 17  ? 32.986  -20.173 -74.910  1.00 84.01  ? 24  GLU A O   1 
ATOM   115   C CB  . GLU A 1 17  ? 35.646  -21.352 -73.799  1.00 81.10  ? 24  GLU A CB  1 
ATOM   116   C CG  . GLU A 1 17  ? 36.724  -22.324 -73.348  1.00 99.97  ? 24  GLU A CG  1 
ATOM   117   C CD  . GLU A 1 17  ? 36.291  -23.166 -72.162  1.00 125.20 ? 24  GLU A CD  1 
ATOM   118   O OE1 . GLU A 1 17  ? 35.186  -22.927 -71.630  1.00 107.20 ? 24  GLU A OE1 1 
ATOM   119   O OE2 . GLU A 1 17  ? 37.060  -24.064 -71.758  1.00 124.73 ? 24  GLU A OE2 1 
ATOM   120   N N   . GLN A 1 18  ? 32.353  -21.912 -73.624  1.00 84.40  ? 25  GLN A N   1 
ATOM   121   C CA  . GLN A 1 18  ? 31.022  -21.402 -73.338  1.00 78.45  ? 25  GLN A CA  1 
ATOM   122   C C   . GLN A 1 18  ? 30.853  -21.179 -71.843  1.00 78.26  ? 25  GLN A C   1 
ATOM   123   O O   . GLN A 1 18  ? 31.314  -21.982 -71.026  1.00 89.78  ? 25  GLN A O   1 
ATOM   124   C CB  . GLN A 1 18  ? 29.941  -22.359 -73.848  1.00 68.83  ? 25  GLN A CB  1 
ATOM   125   C CG  . GLN A 1 18  ? 29.684  -22.253 -75.340  1.00 86.08  ? 25  GLN A CG  1 
ATOM   126   C CD  . GLN A 1 18  ? 28.772  -23.346 -75.855  1.00 96.25  ? 25  GLN A CD  1 
ATOM   127   O OE1 . GLN A 1 18  ? 28.100  -24.028 -75.081  1.00 91.21  ? 25  GLN A OE1 1 
ATOM   128   N NE2 . GLN A 1 18  ? 28.747  -23.523 -77.170  1.00 122.15 ? 25  GLN A NE2 1 
ATOM   129   N N   . VAL A 1 19  ? 30.191  -20.075 -71.498  1.00 69.17  ? 26  VAL A N   1 
ATOM   130   C CA  . VAL A 1 19  ? 29.839  -19.754 -70.124  1.00 64.79  ? 26  VAL A CA  1 
ATOM   131   C C   . VAL A 1 19  ? 28.346  -19.466 -70.080  1.00 63.13  ? 26  VAL A C   1 
ATOM   132   O O   . VAL A 1 19  ? 27.706  -19.210 -71.102  1.00 71.10  ? 26  VAL A O   1 
ATOM   133   C CB  . VAL A 1 19  ? 30.632  -18.550 -69.569  1.00 66.35  ? 26  VAL A CB  1 
ATOM   134   C CG1 . VAL A 1 19  ? 32.121  -18.724 -69.822  1.00 63.42  ? 26  VAL A CG1 1 
ATOM   135   C CG2 . VAL A 1 19  ? 30.124  -17.255 -70.182  1.00 53.24  ? 26  VAL A CG2 1 
ATOM   136   N N   . ASP A 1 20  ? 27.791  -19.523 -68.875  1.00 75.67  ? 27  ASP A N   1 
ATOM   137   C CA  . ASP A 1 20  ? 26.385  -19.233 -68.640  1.00 70.87  ? 27  ASP A CA  1 
ATOM   138   C C   . ASP A 1 20  ? 26.253  -17.917 -67.886  1.00 68.20  ? 27  ASP A C   1 
ATOM   139   O O   . ASP A 1 20  ? 27.034  -17.631 -66.973  1.00 76.06  ? 27  ASP A O   1 
ATOM   140   C CB  . ASP A 1 20  ? 25.710  -20.362 -67.853  1.00 72.15  ? 27  ASP A CB  1 
ATOM   141   C CG  . ASP A 1 20  ? 25.160  -21.458 -68.750  1.00 91.41  ? 27  ASP A CG  1 
ATOM   142   O OD1 . ASP A 1 20  ? 24.301  -21.150 -69.603  1.00 111.53 ? 27  ASP A OD1 1 
ATOM   143   O OD2 . ASP A 1 20  ? 25.588  -22.626 -68.596  1.00 95.27  ? 27  ASP A OD2 1 
ATOM   144   N N   . THR A 1 21  ? 25.273  -17.114 -68.282  1.00 65.38  ? 28  THR A N   1 
ATOM   145   C CA  . THR A 1 21  ? 24.964  -15.854 -67.624  1.00 74.40  ? 28  THR A CA  1 
ATOM   146   C C   . THR A 1 21  ? 23.557  -15.925 -67.038  1.00 65.16  ? 28  THR A C   1 
ATOM   147   O O   . THR A 1 21  ? 22.829  -16.904 -67.223  1.00 71.22  ? 28  THR A O   1 
ATOM   148   C CB  . THR A 1 21  ? 25.093  -14.676 -68.595  1.00 79.48  ? 28  THR A CB  1 
ATOM   149   O OG1 . THR A 1 21  ? 23.923  -14.605 -69.420  1.00 72.53  ? 28  THR A OG1 1 
ATOM   150   C CG2 . THR A 1 21  ? 26.318  -14.848 -69.480  1.00 69.31  ? 28  THR A CG2 1 
ATOM   151   N N   . ILE A 1 22  ? 23.178  -14.866 -66.320  1.00 70.59  ? 29  ILE A N   1 
ATOM   152   C CA  . ILE A 1 22  ? 21.887  -14.858 -65.639  1.00 57.70  ? 29  ILE A CA  1 
ATOM   153   C C   . ILE A 1 22  ? 20.743  -14.803 -66.647  1.00 66.96  ? 29  ILE A C   1 
ATOM   154   O O   . ILE A 1 22  ? 19.679  -15.395 -66.429  1.00 66.38  ? 29  ILE A O   1 
ATOM   155   C CB  . ILE A 1 22  ? 21.825  -13.698 -64.626  1.00 58.13  ? 29  ILE A CB  1 
ATOM   156   C CG1 . ILE A 1 22  ? 20.550  -13.785 -63.784  1.00 64.67  ? 29  ILE A CG1 1 
ATOM   157   C CG2 . ILE A 1 22  ? 21.940  -12.346 -65.323  1.00 82.06  ? 29  ILE A CG2 1 
ATOM   158   C CD1 . ILE A 1 22  ? 20.489  -15.013 -62.898  1.00 61.78  ? 29  ILE A CD1 1 
ATOM   159   N N   . MET A 1 23  ? 20.937  -14.099 -67.764  1.00 68.83  ? 30  MET A N   1 
ATOM   160   C CA  . MET A 1 23  ? 19.874  -13.906 -68.742  1.00 68.84  ? 30  MET A CA  1 
ATOM   161   C C   . MET A 1 23  ? 20.037  -14.739 -70.006  1.00 55.10  ? 30  MET A C   1 
ATOM   162   O O   . MET A 1 23  ? 19.070  -14.869 -70.763  1.00 72.26  ? 30  MET A O   1 
ATOM   163   C CB  . MET A 1 23  ? 19.761  -12.423 -69.125  1.00 61.38  ? 30  MET A CB  1 
ATOM   164   C CG  . MET A 1 23  ? 19.073  -11.557 -68.080  1.00 88.54  ? 30  MET A CG  1 
ATOM   165   S SD  . MET A 1 23  ? 18.565  -9.955  -68.738  1.00 82.65  ? 30  MET A SD  1 
ATOM   166   C CE  . MET A 1 23  ? 19.660  -8.847  -67.853  1.00 95.53  ? 30  MET A CE  1 
ATOM   167   N N   . GLU A 1 24  ? 21.215  -15.305 -70.257  1.00 61.87  ? 31  GLU A N   1 
ATOM   168   C CA  . GLU A 1 24  ? 21.440  -16.065 -71.478  1.00 67.74  ? 31  GLU A CA  1 
ATOM   169   C C   . GLU A 1 24  ? 22.235  -17.323 -71.159  1.00 73.99  ? 31  GLU A C   1 
ATOM   170   O O   . GLU A 1 24  ? 23.002  -17.366 -70.194  1.00 75.68  ? 31  GLU A O   1 
ATOM   171   C CB  . GLU A 1 24  ? 22.174  -15.223 -72.532  1.00 83.44  ? 31  GLU A CB  1 
ATOM   172   C CG  . GLU A 1 24  ? 22.074  -15.771 -73.944  1.00 93.97  ? 31  GLU A CG  1 
ATOM   173   C CD  . GLU A 1 24  ? 22.851  -14.946 -74.950  1.00 102.40 ? 31  GLU A CD  1 
ATOM   174   O OE1 . GLU A 1 24  ? 23.357  -13.867 -74.575  1.00 103.56 ? 31  GLU A OE1 1 
ATOM   175   O OE2 . GLU A 1 24  ? 22.958  -15.382 -76.116  1.00 105.24 ? 31  GLU A OE2 1 
ATOM   176   N N   . LYS A 1 25  ? 22.047  -18.348 -71.986  1.00 80.42  ? 32  LYS A N   1 
ATOM   177   C CA  . LYS A 1 25  ? 22.680  -19.645 -71.794  1.00 75.29  ? 32  LYS A CA  1 
ATOM   178   C C   . LYS A 1 25  ? 23.630  -19.952 -72.943  1.00 82.80  ? 32  LYS A C   1 
ATOM   179   O O   . LYS A 1 25  ? 23.347  -19.620 -74.099  1.00 99.64  ? 32  LYS A O   1 
ATOM   180   C CB  . LYS A 1 25  ? 21.634  -20.753 -71.682  1.00 85.61  ? 32  LYS A CB  1 
ATOM   181   C CG  . LYS A 1 25  ? 20.697  -20.597 -70.501  1.00 98.05  ? 32  LYS A CG  1 
ATOM   182   C CD  . LYS A 1 25  ? 20.915  -21.697 -69.478  1.00 101.97 ? 32  LYS A CD  1 
ATOM   183   C CE  . LYS A 1 25  ? 20.037  -21.487 -68.263  1.00 105.46 ? 32  LYS A CE  1 
ATOM   184   N NZ  . LYS A 1 25  ? 18.712  -20.939 -68.638  1.00 98.34  ? 32  LYS A NZ  1 
ATOM   185   N N   . ASN A 1 26  ? 24.758  -20.588 -72.607  1.00 88.18  ? 33  ASN A N   1 
ATOM   186   C CA  . ASN A 1 26  ? 25.726  -21.088 -73.589  1.00 92.78  ? 33  ASN A CA  1 
ATOM   187   C C   . ASN A 1 26  ? 26.305  -19.963 -74.448  1.00 78.10  ? 33  ASN A C   1 
ATOM   188   O O   . ASN A 1 26  ? 26.397  -20.079 -75.672  1.00 74.99  ? 33  ASN A O   1 
ATOM   189   C CB  . ASN A 1 26  ? 25.102  -22.175 -74.469  1.00 86.16  ? 33  ASN A CB  1 
ATOM   190   C CG  . ASN A 1 26  ? 24.957  -23.505 -73.748  1.00 100.03 ? 33  ASN A CG  1 
ATOM   191   O OD1 . ASN A 1 26  ? 24.908  -23.560 -72.520  1.00 101.82 ? 33  ASN A OD1 1 
ATOM   192   N ND2 . ASN A 1 26  ? 24.889  -24.585 -74.519  1.00 119.60 ? 33  ASN A ND2 1 
ATOM   193   N N   . VAL A 1 27  ? 26.705  -18.867 -73.809  1.00 72.84  ? 34  VAL A N   1 
ATOM   194   C CA  . VAL A 1 27  ? 27.272  -17.726 -74.524  1.00 52.68  ? 34  VAL A CA  1 
ATOM   195   C C   . VAL A 1 27  ? 28.752  -18.004 -74.777  1.00 67.66  ? 34  VAL A C   1 
ATOM   196   O O   . VAL A 1 27  ? 29.546  -18.094 -73.837  1.00 82.65  ? 34  VAL A O   1 
ATOM   197   C CB  . VAL A 1 27  ? 27.079  -16.420 -73.746  1.00 67.91  ? 34  VAL A CB  1 
ATOM   198   C CG1 . VAL A 1 27  ? 27.470  -15.229 -74.608  1.00 65.70  ? 34  VAL A CG1 1 
ATOM   199   C CG2 . VAL A 1 27  ? 25.640  -16.293 -73.273  1.00 68.76  ? 34  VAL A CG2 1 
ATOM   200   N N   . THR A 1 28  ? 29.126  -18.133 -76.048  1.00 82.20  ? 35  THR A N   1 
ATOM   201   C CA  . THR A 1 28  ? 30.514  -18.399 -76.403  1.00 71.05  ? 35  THR A CA  1 
ATOM   202   C C   . THR A 1 28  ? 31.373  -17.160 -76.176  1.00 72.25  ? 35  THR A C   1 
ATOM   203   O O   . THR A 1 28  ? 30.988  -16.044 -76.536  1.00 77.67  ? 35  THR A O   1 
ATOM   204   C CB  . THR A 1 28  ? 30.614  -18.847 -77.863  1.00 66.68  ? 35  THR A CB  1 
ATOM   205   O OG1 . THR A 1 28  ? 29.704  -19.929 -78.095  1.00 78.15  ? 35  THR A OG1 1 
ATOM   206   C CG2 . THR A 1 28  ? 32.027  -19.309 -78.184  1.00 77.38  ? 35  THR A CG2 1 
ATOM   207   N N   . VAL A 1 29  ? 32.547  -17.362 -75.575  1.00 71.60  ? 36  VAL A N   1 
ATOM   208   C CA  . VAL A 1 29  ? 33.451  -16.273 -75.234  1.00 62.41  ? 36  VAL A CA  1 
ATOM   209   C C   . VAL A 1 29  ? 34.853  -16.603 -75.730  1.00 72.30  ? 36  VAL A C   1 
ATOM   210   O O   . VAL A 1 29  ? 35.172  -17.746 -76.061  1.00 75.90  ? 36  VAL A O   1 
ATOM   211   C CB  . VAL A 1 29  ? 33.477  -15.981 -73.718  1.00 72.48  ? 36  VAL A CB  1 
ATOM   212   C CG1 . VAL A 1 29  ? 32.116  -15.484 -73.250  1.00 68.77  ? 36  VAL A CG1 1 
ATOM   213   C CG2 . VAL A 1 29  ? 33.893  -17.222 -72.947  1.00 67.03  ? 36  VAL A CG2 1 
ATOM   214   N N   . THR A 1 30  ? 35.697  -15.568 -75.781  1.00 77.17  ? 37  THR A N   1 
ATOM   215   C CA  . THR A 1 30  ? 37.061  -15.743 -76.271  1.00 79.93  ? 37  THR A CA  1 
ATOM   216   C C   . THR A 1 30  ? 37.947  -16.447 -75.252  1.00 74.67  ? 37  THR A C   1 
ATOM   217   O O   . THR A 1 30  ? 38.866  -17.180 -75.636  1.00 88.90  ? 37  THR A O   1 
ATOM   218   C CB  . THR A 1 30  ? 37.668  -14.390 -76.650  1.00 85.15  ? 37  THR A CB  1 
ATOM   219   O OG1 . THR A 1 30  ? 37.855  -13.601 -75.469  1.00 78.04  ? 37  THR A OG1 1 
ATOM   220   C CG2 . THR A 1 30  ? 36.753  -13.650 -77.612  1.00 73.44  ? 37  THR A CG2 1 
ATOM   221   N N   . HIS A 1 31  ? 37.710  -16.229 -73.961  1.00 88.61  ? 38  HIS A N   1 
ATOM   222   C CA  . HIS A 1 31  ? 38.488  -16.895 -72.927  1.00 88.48  ? 38  HIS A CA  1 
ATOM   223   C C   . HIS A 1 31  ? 37.619  -17.062 -71.690  1.00 94.38  ? 38  HIS A C   1 
ATOM   224   O O   . HIS A 1 31  ? 36.737  -16.243 -71.418  1.00 93.62  ? 38  HIS A O   1 
ATOM   225   C CB  . HIS A 1 31  ? 39.762  -16.113 -72.588  1.00 89.08  ? 38  HIS A CB  1 
ATOM   226   C CG  . HIS A 1 31  ? 40.862  -16.965 -72.039  1.00 108.42 ? 38  HIS A CG  1 
ATOM   227   N ND1 . HIS A 1 31  ? 40.930  -18.325 -72.257  1.00 110.82 ? 38  HIS A ND1 1 
ATOM   228   C CD2 . HIS A 1 31  ? 41.938  -16.652 -71.279  1.00 98.34  ? 38  HIS A CD2 1 
ATOM   229   C CE1 . HIS A 1 31  ? 42.002  -18.811 -71.656  1.00 107.47 ? 38  HIS A CE1 1 
ATOM   230   N NE2 . HIS A 1 31  ? 42.630  -17.817 -71.055  1.00 111.29 ? 38  HIS A NE2 1 
ATOM   231   N N   . ALA A 1 32  ? 37.878  -18.134 -70.942  1.00 93.70  ? 39  ALA A N   1 
ATOM   232   C CA  . ALA A 1 32  ? 37.097  -18.471 -69.761  1.00 90.57  ? 39  ALA A CA  1 
ATOM   233   C C   . ALA A 1 32  ? 38.036  -18.971 -68.671  1.00 87.54  ? 39  ALA A C   1 
ATOM   234   O O   . ALA A 1 32  ? 39.251  -19.078 -68.867  1.00 92.97  ? 39  ALA A O   1 
ATOM   235   C CB  . ALA A 1 32  ? 36.020  -19.508 -70.096  1.00 80.62  ? 39  ALA A CB  1 
ATOM   236   N N   . GLN A 1 33  ? 37.463  -19.280 -67.508  1.00 91.83  ? 40  GLN A N   1 
ATOM   237   C CA  . GLN A 1 33  ? 38.244  -19.751 -66.368  1.00 88.67  ? 40  GLN A CA  1 
ATOM   238   C C   . GLN A 1 33  ? 37.342  -20.551 -65.441  1.00 80.77  ? 40  GLN A C   1 
ATOM   239   O O   . GLN A 1 33  ? 36.303  -20.049 -65.000  1.00 70.39  ? 40  GLN A O   1 
ATOM   240   C CB  . GLN A 1 33  ? 38.879  -18.580 -65.610  1.00 70.61  ? 40  GLN A CB  1 
ATOM   241   C CG  . GLN A 1 33  ? 39.480  -18.969 -64.264  1.00 79.26  ? 40  GLN A CG  1 
ATOM   242   C CD  . GLN A 1 33  ? 40.996  -18.928 -64.261  1.00 88.96  ? 40  GLN A CD  1 
ATOM   243   O OE1 . GLN A 1 33  ? 41.599  -17.859 -64.343  1.00 94.16  ? 40  GLN A OE1 1 
ATOM   244   N NE2 . GLN A 1 33  ? 41.620  -20.098 -64.167  1.00 99.80  ? 40  GLN A NE2 1 
ATOM   245   N N   . ASP A 1 34  ? 37.743  -21.782 -65.144  1.00 72.40  ? 41  ASP A N   1 
ATOM   246   C CA  . ASP A 1 34  ? 37.000  -22.643 -64.235  1.00 82.69  ? 41  ASP A CA  1 
ATOM   247   C C   . ASP A 1 34  ? 37.472  -22.402 -62.805  1.00 79.24  ? 41  ASP A C   1 
ATOM   248   O O   . ASP A 1 34  ? 38.678  -22.379 -62.540  1.00 86.38  ? 41  ASP A O   1 
ATOM   249   C CB  . ASP A 1 34  ? 37.188  -24.110 -64.622  1.00 80.61  ? 41  ASP A CB  1 
ATOM   250   C CG  . ASP A 1 34  ? 36.134  -25.018 -64.020  1.00 95.87  ? 41  ASP A CG  1 
ATOM   251   O OD1 . ASP A 1 34  ? 35.093  -24.507 -63.558  1.00 91.57  ? 41  ASP A OD1 1 
ATOM   252   O OD2 . ASP A 1 34  ? 36.347  -26.247 -64.008  1.00 94.85  ? 41  ASP A OD2 1 
ATOM   253   N N   . ILE A 1 35  ? 36.524  -22.210 -61.891  1.00 70.77  ? 42  ILE A N   1 
ATOM   254   C CA  . ILE A 1 35  ? 36.837  -22.011 -60.482  1.00 73.36  ? 42  ILE A CA  1 
ATOM   255   C C   . ILE A 1 35  ? 36.344  -23.182 -59.633  1.00 73.56  ? 42  ILE A C   1 
ATOM   256   O O   . ILE A 1 35  ? 36.187  -23.045 -58.421  1.00 67.59  ? 42  ILE A O   1 
ATOM   257   C CB  . ILE A 1 35  ? 36.277  -20.677 -59.962  1.00 61.45  ? 42  ILE A CB  1 
ATOM   258   C CG1 . ILE A 1 35  ? 34.747  -20.689 -59.993  1.00 65.30  ? 42  ILE A CG1 1 
ATOM   259   C CG2 . ILE A 1 35  ? 36.822  -19.516 -60.777  1.00 64.81  ? 42  ILE A CG2 1 
ATOM   260   C CD1 . ILE A 1 35  ? 34.116  -19.551 -59.220  1.00 60.09  ? 42  ILE A CD1 1 
ATOM   261   N N   . LEU A 1 36  ? 36.101  -24.335 -60.251  1.00 72.69  ? 43  LEU A N   1 
ATOM   262   C CA  . LEU A 1 36  ? 35.597  -25.512 -59.556  1.00 57.48  ? 43  LEU A CA  1 
ATOM   263   C C   . LEU A 1 36  ? 36.636  -26.619 -59.637  1.00 63.17  ? 43  LEU A C   1 
ATOM   264   O O   . LEU A 1 36  ? 37.020  -27.033 -60.736  1.00 75.74  ? 43  LEU A O   1 
ATOM   265   C CB  . LEU A 1 36  ? 34.270  -25.978 -60.161  1.00 56.48  ? 43  LEU A CB  1 
ATOM   266   C CG  . LEU A 1 36  ? 33.612  -27.189 -59.495  1.00 67.57  ? 43  LEU A CG  1 
ATOM   267   C CD1 . LEU A 1 36  ? 33.092  -26.819 -58.114  1.00 55.94  ? 43  LEU A CD1 1 
ATOM   268   C CD2 . LEU A 1 36  ? 32.498  -27.753 -60.362  1.00 67.37  ? 43  LEU A CD2 1 
ATOM   269   N N   . GLU A 1 37  ? 37.090  -27.093 -58.478  1.00 65.25  ? 44  GLU A N   1 
ATOM   270   C CA  . GLU A 1 37  ? 37.950  -28.267 -58.437  1.00 65.48  ? 44  GLU A CA  1 
ATOM   271   C C   . GLU A 1 37  ? 37.110  -29.511 -58.699  1.00 66.60  ? 44  GLU A C   1 
ATOM   272   O O   . GLU A 1 37  ? 36.078  -29.722 -58.056  1.00 76.73  ? 44  GLU A O   1 
ATOM   273   C CB  . GLU A 1 37  ? 38.651  -28.370 -57.082  1.00 67.67  ? 44  GLU A CB  1 
ATOM   274   C CG  . GLU A 1 37  ? 39.871  -29.278 -57.072  1.00 71.05  ? 44  GLU A CG  1 
ATOM   275   C CD  . GLU A 1 37  ? 41.171  -28.508 -57.199  1.00 104.90 ? 44  GLU A CD  1 
ATOM   276   O OE1 . GLU A 1 37  ? 41.304  -27.456 -56.537  1.00 90.69  ? 44  GLU A OE1 1 
ATOM   277   O OE2 . GLU A 1 37  ? 42.055  -28.949 -57.965  1.00 125.56 ? 44  GLU A OE2 1 
ATOM   278   N N   . LYS A 1 38  ? 37.545  -30.334 -59.653  1.00 74.91  ? 45  LYS A N   1 
ATOM   279   C CA  . LYS A 1 38  ? 36.749  -31.472 -60.085  1.00 70.21  ? 45  LYS A CA  1 
ATOM   280   C C   . LYS A 1 38  ? 37.524  -32.780 -60.161  1.00 70.15  ? 45  LYS A C   1 
ATOM   281   O O   . LYS A 1 38  ? 36.954  -33.786 -60.597  1.00 71.83  ? 45  LYS A O   1 
ATOM   282   C CB  . LYS A 1 38  ? 36.116  -31.190 -61.458  1.00 65.72  ? 45  LYS A CB  1 
ATOM   283   C CG  . LYS A 1 38  ? 35.279  -29.920 -61.521  1.00 79.05  ? 45  LYS A CG  1 
ATOM   284   C CD  . LYS A 1 38  ? 34.639  -29.745 -62.889  1.00 91.45  ? 45  LYS A CD  1 
ATOM   285   C CE  . LYS A 1 38  ? 35.688  -29.591 -63.978  1.00 70.80  ? 45  LYS A CE  1 
ATOM   286   N NZ  . LYS A 1 38  ? 35.074  -29.513 -65.334  1.00 84.92  ? 45  LYS A NZ  1 
ATOM   287   N N   . THR A 1 39  ? 38.790  -32.807 -59.748  1.00 72.26  ? 46  THR A N   1 
ATOM   288   C CA  . THR A 1 39  ? 39.636  -33.976 -59.931  1.00 79.19  ? 46  THR A CA  1 
ATOM   289   C C   . THR A 1 39  ? 40.365  -34.326 -58.640  1.00 74.59  ? 46  THR A C   1 
ATOM   290   O O   . THR A 1 39  ? 40.654  -33.457 -57.813  1.00 73.24  ? 46  THR A O   1 
ATOM   291   C CB  . THR A 1 39  ? 40.659  -33.752 -61.055  1.00 90.69  ? 46  THR A CB  1 
ATOM   292   O OG1 . THR A 1 39  ? 41.177  -32.418 -60.970  1.00 82.63  ? 46  THR A OG1 1 
ATOM   293   C CG2 . THR A 1 39  ? 40.010  -33.958 -62.416  1.00 73.42  ? 46  THR A CG2 1 
ATOM   294   N N   . HIS A 1 40  ? 40.653  -35.618 -58.481  1.00 77.19  ? 47  HIS A N   1 
ATOM   295   C CA  . HIS A 1 40  ? 41.418  -36.135 -57.355  1.00 85.12  ? 47  HIS A CA  1 
ATOM   296   C C   . HIS A 1 40  ? 42.443  -37.134 -57.876  1.00 82.42  ? 47  HIS A C   1 
ATOM   297   O O   . HIS A 1 40  ? 42.227  -37.784 -58.903  1.00 95.16  ? 47  HIS A O   1 
ATOM   298   C CB  . HIS A 1 40  ? 40.509  -36.797 -56.311  1.00 72.95  ? 47  HIS A CB  1 
ATOM   299   C CG  . HIS A 1 40  ? 39.689  -37.925 -56.853  1.00 68.05  ? 47  HIS A CG  1 
ATOM   300   N ND1 . HIS A 1 40  ? 40.158  -39.219 -56.923  1.00 69.82  ? 47  HIS A ND1 1 
ATOM   301   C CD2 . HIS A 1 40  ? 38.433  -37.953 -57.357  1.00 65.17  ? 47  HIS A CD2 1 
ATOM   302   C CE1 . HIS A 1 40  ? 39.225  -39.997 -57.443  1.00 73.77  ? 47  HIS A CE1 1 
ATOM   303   N NE2 . HIS A 1 40  ? 38.168  -39.253 -57.716  1.00 74.49  ? 47  HIS A NE2 1 
ATOM   304   N N   . ASN A 1 41  ? 43.566  -37.253 -57.161  1.00 69.01  ? 48  ASN A N   1 
ATOM   305   C CA  . ASN A 1 41  ? 44.660  -38.099 -57.628  1.00 77.17  ? 48  ASN A CA  1 
ATOM   306   C C   . ASN A 1 41  ? 44.475  -39.572 -57.282  1.00 76.36  ? 48  ASN A C   1 
ATOM   307   O O   . ASN A 1 41  ? 45.264  -40.402 -57.746  1.00 88.27  ? 48  ASN A O   1 
ATOM   308   C CB  . ASN A 1 41  ? 46.002  -37.603 -57.071  1.00 79.20  ? 48  ASN A CB  1 
ATOM   309   C CG  . ASN A 1 41  ? 46.069  -37.639 -55.552  1.00 79.96  ? 48  ASN A CG  1 
ATOM   310   O OD1 . ASN A 1 41  ? 45.196  -38.190 -54.882  1.00 84.31  ? 48  ASN A OD1 1 
ATOM   311   N ND2 . ASN A 1 41  ? 47.125  -37.051 -55.003  1.00 86.38  ? 48  ASN A ND2 1 
ATOM   312   N N   . GLY A 1 42  ? 43.469  -39.911 -56.480  1.00 76.16  ? 49  GLY A N   1 
ATOM   313   C CA  . GLY A 1 42  ? 43.159  -41.302 -56.206  1.00 73.41  ? 49  GLY A CA  1 
ATOM   314   C C   . GLY A 1 42  ? 44.098  -42.007 -55.250  1.00 78.28  ? 49  GLY A C   1 
ATOM   315   O O   . GLY A 1 42  ? 44.273  -43.225 -55.357  1.00 75.51  ? 49  GLY A O   1 
ATOM   316   N N   . LYS A 1 43  ? 44.714  -41.277 -54.319  1.00 74.77  ? 50  LYS A N   1 
ATOM   317   C CA  . LYS A 1 43  ? 45.593  -41.874 -53.322  1.00 78.12  ? 50  LYS A CA  1 
ATOM   318   C C   . LYS A 1 43  ? 45.438  -41.139 -51.996  1.00 78.15  ? 50  LYS A C   1 
ATOM   319   O O   . LYS A 1 43  ? 45.050  -39.968 -51.961  1.00 68.37  ? 50  LYS A O   1 
ATOM   320   C CB  . LYS A 1 43  ? 47.068  -41.847 -53.759  1.00 82.06  ? 50  LYS A CB  1 
ATOM   321   C CG  . LYS A 1 43  ? 47.343  -42.578 -55.064  1.00 81.35  ? 50  LYS A CG  1 
ATOM   322   C CD  . LYS A 1 43  ? 48.532  -43.509 -54.965  1.00 90.98  ? 50  LYS A CD  1 
ATOM   323   C CE  . LYS A 1 43  ? 48.444  -44.592 -56.029  1.00 91.76  ? 50  LYS A CE  1 
ATOM   324   N NZ  . LYS A 1 43  ? 49.766  -45.215 -56.319  1.00 97.44  ? 50  LYS A NZ  1 
ATOM   325   N N   . LEU A 1 44  ? 45.729  -41.845 -50.900  1.00 80.37  ? 51  LEU A N   1 
ATOM   326   C CA  . LEU A 1 44  ? 45.906  -41.186 -49.613  1.00 75.45  ? 51  LEU A CA  1 
ATOM   327   C C   . LEU A 1 44  ? 47.305  -40.589 -49.555  1.00 77.81  ? 51  LEU A C   1 
ATOM   328   O O   . LEU A 1 44  ? 48.291  -41.252 -49.895  1.00 89.05  ? 51  LEU A O   1 
ATOM   329   C CB  . LEU A 1 44  ? 45.715  -42.148 -48.435  1.00 90.11  ? 51  LEU A CB  1 
ATOM   330   C CG  . LEU A 1 44  ? 44.435  -42.936 -48.148  1.00 76.92  ? 51  LEU A CG  1 
ATOM   331   C CD1 . LEU A 1 44  ? 43.166  -42.160 -48.481  1.00 76.68  ? 51  LEU A CD1 1 
ATOM   332   C CD2 . LEU A 1 44  ? 44.502  -44.231 -48.914  1.00 93.17  ? 51  LEU A CD2 1 
ATOM   333   N N   . CYS A 1 45  ? 47.395  -39.345 -49.109  1.00 75.92  ? 52  CYS A N   1 
ATOM   334   C CA  . CYS A 1 45  ? 48.669  -38.657 -49.017  1.00 85.28  ? 52  CYS A CA  1 
ATOM   335   C C   . CYS A 1 45  ? 48.932  -38.224 -47.582  1.00 69.51  ? 52  CYS A C   1 
ATOM   336   O O   . CYS A 1 45  ? 48.082  -38.354 -46.698  1.00 81.28  ? 52  CYS A O   1 
ATOM   337   C CB  . CYS A 1 45  ? 48.704  -37.439 -49.946  1.00 80.76  ? 52  CYS A CB  1 
ATOM   338   S SG  . CYS A 1 45  ? 48.396  -37.804 -51.683  1.00 113.98 ? 52  CYS A SG  1 
ATOM   339   N N   . ASP A 1 46  ? 50.139  -37.710 -47.358  1.00 67.97  ? 53  ASP A N   1 
ATOM   340   C CA  . ASP A 1 46  ? 50.421  -37.024 -46.107  1.00 62.15  ? 53  ASP A CA  1 
ATOM   341   C C   . ASP A 1 46  ? 49.562  -35.771 -46.010  1.00 67.89  ? 53  ASP A C   1 
ATOM   342   O O   . ASP A 1 46  ? 49.231  -35.139 -47.016  1.00 76.76  ? 53  ASP A O   1 
ATOM   343   C CB  . ASP A 1 46  ? 51.901  -36.651 -46.014  1.00 70.21  ? 53  ASP A CB  1 
ATOM   344   C CG  . ASP A 1 46  ? 52.811  -37.862 -46.007  1.00 85.85  ? 53  ASP A CG  1 
ATOM   345   O OD1 . ASP A 1 46  ? 52.304  -38.990 -46.183  1.00 87.61  ? 53  ASP A OD1 1 
ATOM   346   O OD2 . ASP A 1 46  ? 54.033  -37.682 -45.819  1.00 83.44  ? 53  ASP A OD2 1 
ATOM   347   N N   . LEU A 1 47  ? 49.188  -35.418 -44.789  1.00 61.25  ? 54  LEU A N   1 
ATOM   348   C CA  . LEU A 1 47  ? 48.403  -34.217 -44.536  1.00 63.12  ? 54  LEU A CA  1 
ATOM   349   C C   . LEU A 1 47  ? 49.318  -33.189 -43.887  1.00 72.18  ? 54  LEU A C   1 
ATOM   350   O O   . LEU A 1 47  ? 49.693  -33.334 -42.718  1.00 81.78  ? 54  LEU A O   1 
ATOM   351   C CB  . LEU A 1 47  ? 47.193  -34.520 -43.659  1.00 69.89  ? 54  LEU A CB  1 
ATOM   352   C CG  . LEU A 1 47  ? 46.089  -33.469 -43.738  1.00 61.94  ? 54  LEU A CG  1 
ATOM   353   C CD1 . LEU A 1 47  ? 45.675  -33.242 -45.185  1.00 78.67  ? 54  LEU A CD1 1 
ATOM   354   C CD2 . LEU A 1 47  ? 44.897  -33.885 -42.900  1.00 78.62  ? 54  LEU A CD2 1 
ATOM   355   N N   . ASN A 1 48  ? 49.670  -32.154 -44.650  1.00 73.75  ? 55  ASN A N   1 
ATOM   356   C CA  . ASN A 1 48  ? 50.584  -31.109 -44.194  1.00 72.46  ? 55  ASN A CA  1 
ATOM   357   C C   . ASN A 1 48  ? 51.909  -31.705 -43.723  1.00 75.95  ? 55  ASN A C   1 
ATOM   358   O O   . ASN A 1 48  ? 52.464  -31.317 -42.692  1.00 72.86  ? 55  ASN A O   1 
ATOM   359   C CB  . ASN A 1 48  ? 49.938  -30.257 -43.102  1.00 65.89  ? 55  ASN A CB  1 
ATOM   360   C CG  . ASN A 1 48  ? 48.624  -29.641 -43.548  1.00 90.18  ? 55  ASN A CG  1 
ATOM   361   O OD1 . ASN A 1 48  ? 47.552  -30.031 -43.082  1.00 98.57  ? 55  ASN A OD1 1 
ATOM   362   N ND2 . ASN A 1 48  ? 48.702  -28.672 -44.451  1.00 80.69  ? 55  ASN A ND2 1 
ATOM   363   N N   . GLY A 1 49  A 52.416  -32.669 -44.490  1.00 73.87  ? 55  GLY A N   1 
ATOM   364   C CA  . GLY A 1 49  A 53.718  -33.253 -44.251  1.00 71.71  ? 55  GLY A CA  1 
ATOM   365   C C   . GLY A 1 49  A 53.767  -34.387 -43.249  1.00 68.40  ? 55  GLY A C   1 
ATOM   366   O O   . GLY A 1 49  A 54.865  -34.876 -42.954  1.00 80.69  ? 55  GLY A O   1 
ATOM   367   N N   . VAL A 1 50  ? 52.628  -34.823 -42.716  1.00 81.46  ? 56  VAL A N   1 
ATOM   368   C CA  . VAL A 1 50  ? 52.581  -35.880 -41.711  1.00 76.27  ? 56  VAL A CA  1 
ATOM   369   C C   . VAL A 1 50  ? 51.803  -37.057 -42.283  1.00 61.39  ? 56  VAL A C   1 
ATOM   370   O O   . VAL A 1 50  ? 50.681  -36.888 -42.774  1.00 70.03  ? 56  VAL A O   1 
ATOM   371   C CB  . VAL A 1 50  ? 51.944  -35.390 -40.398  1.00 78.15  ? 56  VAL A CB  1 
ATOM   372   C CG1 . VAL A 1 50  ? 52.346  -36.297 -39.243  1.00 71.61  ? 56  VAL A CG1 1 
ATOM   373   C CG2 . VAL A 1 50  ? 52.337  -33.945 -40.118  1.00 63.45  ? 56  VAL A CG2 1 
ATOM   374   N N   . LYS A 1 51  ? 52.400  -38.246 -42.217  1.00 67.59  ? 57  LYS A N   1 
ATOM   375   C CA  . LYS A 1 51  ? 51.768  -39.437 -42.762  1.00 54.83  ? 57  LYS A CA  1 
ATOM   376   C C   . LYS A 1 51  ? 50.575  -39.856 -41.901  1.00 66.95  ? 57  LYS A C   1 
ATOM   377   O O   . LYS A 1 51  ? 50.595  -39.697 -40.678  1.00 69.97  ? 57  LYS A O   1 
ATOM   378   C CB  . LYS A 1 51  ? 52.775  -40.584 -42.836  1.00 66.99  ? 57  LYS A CB  1 
ATOM   379   C CG  . LYS A 1 51  ? 52.353  -41.731 -43.742  1.00 78.56  ? 57  LYS A CG  1 
ATOM   380   C CD  . LYS A 1 51  ? 53.010  -43.044 -43.352  1.00 89.11  ? 57  LYS A CD  1 
ATOM   381   C CE  . LYS A 1 51  ? 52.482  -44.185 -44.211  1.00 67.58  ? 57  LYS A CE  1 
ATOM   382   N NZ  . LYS A 1 51  ? 52.975  -45.512 -43.752  1.00 102.41 ? 57  LYS A NZ  1 
ATOM   383   N N   . PRO A 1 52  ? 49.520  -40.384 -42.515  1.00 72.16  ? 58  PRO A N   1 
ATOM   384   C CA  . PRO A 1 52  ? 48.413  -40.943 -41.735  1.00 67.36  ? 58  PRO A CA  1 
ATOM   385   C C   . PRO A 1 52  ? 48.769  -42.290 -41.121  1.00 59.23  ? 58  PRO A C   1 
ATOM   386   O O   . PRO A 1 52  ? 49.698  -42.980 -41.545  1.00 60.41  ? 58  PRO A O   1 
ATOM   387   C CB  . PRO A 1 52  ? 47.293  -41.098 -42.769  1.00 65.74  ? 58  PRO A CB  1 
ATOM   388   C CG  . PRO A 1 52  ? 48.008  -41.244 -44.067  1.00 62.37  ? 58  PRO A CG  1 
ATOM   389   C CD  . PRO A 1 52  ? 49.209  -40.346 -43.955  1.00 66.56  ? 58  PRO A CD  1 
ATOM   390   N N   . LEU A 1 53  ? 47.999  -42.654 -40.097  1.00 68.86  ? 59  LEU A N   1 
ATOM   391   C CA  . LEU A 1 53  ? 48.081  -43.975 -39.483  1.00 64.38  ? 59  LEU A CA  1 
ATOM   392   C C   . LEU A 1 53  ? 47.063  -44.878 -40.168  1.00 65.63  ? 59  LEU A C   1 
ATOM   393   O O   . LEU A 1 53  ? 45.852  -44.679 -40.028  1.00 70.70  ? 59  LEU A O   1 
ATOM   394   C CB  . LEU A 1 53  ? 47.822  -43.896 -37.980  1.00 67.79  ? 59  LEU A CB  1 
ATOM   395   C CG  . LEU A 1 53  ? 47.810  -45.230 -37.229  1.00 69.20  ? 59  LEU A CG  1 
ATOM   396   C CD1 . LEU A 1 53  ? 49.203  -45.844 -37.177  1.00 64.45  ? 59  LEU A CD1 1 
ATOM   397   C CD2 . LEU A 1 53  ? 47.236  -45.062 -35.829  1.00 65.40  ? 59  LEU A CD2 1 
ATOM   398   N N   . ILE A 1 54  ? 47.550  -45.871 -40.904  1.00 69.72  ? 60  ILE A N   1 
ATOM   399   C CA  . ILE A 1 54  ? 46.706  -46.741 -41.711  1.00 62.87  ? 60  ILE A CA  1 
ATOM   400   C C   . ILE A 1 54  ? 46.671  -48.109 -41.047  1.00 67.84  ? 60  ILE A C   1 
ATOM   401   O O   . ILE A 1 54  ? 47.650  -48.865 -41.099  1.00 67.59  ? 60  ILE A O   1 
ATOM   402   C CB  . ILE A 1 54  ? 47.204  -46.831 -43.159  1.00 57.99  ? 60  ILE A CB  1 
ATOM   403   C CG1 . ILE A 1 54  ? 47.020  -45.479 -43.856  1.00 71.65  ? 60  ILE A CG1 1 
ATOM   404   C CG2 . ILE A 1 54  ? 46.478  -47.939 -43.912  1.00 65.27  ? 60  ILE A CG2 1 
ATOM   405   C CD1 . ILE A 1 54  ? 48.170  -45.089 -44.754  1.00 70.89  ? 60  ILE A CD1 1 
ATOM   406   N N   . LEU A 1 55  ? 45.545  -48.426 -40.412  1.00 66.77  ? 61  LEU A N   1 
ATOM   407   C CA  . LEU A 1 55  ? 45.309  -49.764 -39.883  1.00 66.90  ? 61  LEU A CA  1 
ATOM   408   C C   . LEU A 1 55  ? 44.780  -50.632 -41.018  1.00 80.81  ? 61  LEU A C   1 
ATOM   409   O O   . LEU A 1 55  ? 43.652  -50.439 -41.484  1.00 91.29  ? 61  LEU A O   1 
ATOM   410   C CB  . LEU A 1 55  ? 44.328  -49.726 -38.715  1.00 77.91  ? 61  LEU A CB  1 
ATOM   411   C CG  . LEU A 1 55  ? 44.673  -48.939 -37.446  1.00 75.16  ? 61  LEU A CG  1 
ATOM   412   C CD1 . LEU A 1 55  ? 46.158  -49.023 -37.121  1.00 69.60  ? 61  LEU A CD1 1 
ATOM   413   C CD2 . LEU A 1 55  ? 44.214  -47.495 -37.551  1.00 76.59  ? 61  LEU A CD2 1 
ATOM   414   N N   . LYS A 1 56  ? 45.593  -51.588 -41.466  1.00 85.30  ? 62  LYS A N   1 
ATOM   415   C CA  . LYS A 1 56  ? 45.237  -52.372 -42.644  1.00 95.44  ? 62  LYS A CA  1 
ATOM   416   C C   . LYS A 1 56  ? 44.047  -53.282 -42.363  1.00 88.80  ? 62  LYS A C   1 
ATOM   417   O O   . LYS A 1 56  ? 42.992  -53.159 -42.995  1.00 104.48 ? 62  LYS A O   1 
ATOM   418   C CB  . LYS A 1 56  ? 46.443  -53.188 -43.112  1.00 101.53 ? 62  LYS A CB  1 
ATOM   419   C CG  . LYS A 1 56  ? 46.326  -53.719 -44.534  1.00 109.30 ? 62  LYS A CG  1 
ATOM   420   C CD  . LYS A 1 56  ? 46.484  -52.598 -45.552  1.00 96.94  ? 62  LYS A CD  1 
ATOM   421   C CE  . LYS A 1 56  ? 46.290  -53.103 -46.973  1.00 102.83 ? 62  LYS A CE  1 
ATOM   422   N NZ  . LYS A 1 56  ? 46.450  -52.021 -47.984  1.00 88.40  ? 62  LYS A NZ  1 
ATOM   423   N N   . ASP A 1 57  ? 44.199  -54.205 -41.415  1.00 83.24  ? 63  ASP A N   1 
ATOM   424   C CA  . ASP A 1 57  ? 43.154  -55.174 -41.108  1.00 89.52  ? 63  ASP A CA  1 
ATOM   425   C C   . ASP A 1 57  ? 42.752  -55.132 -39.637  1.00 96.38  ? 63  ASP A C   1 
ATOM   426   O O   . ASP A 1 57  ? 42.108  -56.065 -39.147  1.00 101.78 ? 63  ASP A O   1 
ATOM   427   C CB  . ASP A 1 57  ? 43.608  -56.583 -41.502  1.00 88.93  ? 63  ASP A CB  1 
ATOM   428   C CG  . ASP A 1 57  ? 42.493  -57.403 -42.130  1.00 117.09 ? 63  ASP A CG  1 
ATOM   429   O OD1 . ASP A 1 57  ? 41.374  -56.870 -42.290  1.00 125.67 ? 63  ASP A OD1 1 
ATOM   430   O OD2 . ASP A 1 57  ? 42.735  -58.586 -42.454  1.00 120.88 ? 63  ASP A OD2 1 
ATOM   431   N N   . CYS A 1 58  ? 43.112  -54.067 -38.924  1.00 84.72  ? 64  CYS A N   1 
ATOM   432   C CA  . CYS A 1 58  ? 42.857  -53.943 -37.496  1.00 77.00  ? 64  CYS A CA  1 
ATOM   433   C C   . CYS A 1 58  ? 41.996  -52.720 -37.220  1.00 76.47  ? 64  CYS A C   1 
ATOM   434   O O   . CYS A 1 58  ? 42.129  -51.689 -37.885  1.00 82.90  ? 64  CYS A O   1 
ATOM   435   C CB  . CYS A 1 58  ? 44.179  -53.857 -36.712  1.00 78.74  ? 64  CYS A CB  1 
ATOM   436   S SG  . CYS A 1 58  ? 45.078  -55.429 -36.723  1.00 151.50 ? 64  CYS A SG  1 
ATOM   437   N N   . SER A 1 59  ? 41.089  -52.851 -36.258  1.00 82.85  ? 65  SER A N   1 
ATOM   438   C CA  . SER A 1 59  ? 40.388  -51.701 -35.716  1.00 75.05  ? 65  SER A CA  1 
ATOM   439   C C   . SER A 1 59  ? 41.235  -51.065 -34.617  1.00 62.92  ? 65  SER A C   1 
ATOM   440   O O   . SER A 1 59  ? 42.263  -51.603 -34.201  1.00 64.39  ? 65  SER A O   1 
ATOM   441   C CB  . SER A 1 59  ? 39.013  -52.105 -35.181  1.00 59.97  ? 65  SER A CB  1 
ATOM   442   O OG  . SER A 1 59  ? 39.122  -53.101 -34.179  1.00 71.33  ? 65  SER A OG  1 
ATOM   443   N N   . VAL A 1 60  ? 40.799  -49.892 -34.154  1.00 54.06  ? 66  VAL A N   1 
ATOM   444   C CA  . VAL A 1 60  ? 41.536  -49.203 -33.098  1.00 51.24  ? 66  VAL A CA  1 
ATOM   445   C C   . VAL A 1 60  ? 41.566  -50.049 -31.831  1.00 56.06  ? 66  VAL A C   1 
ATOM   446   O O   . VAL A 1 60  ? 42.608  -50.176 -31.176  1.00 59.57  ? 66  VAL A O   1 
ATOM   447   C CB  . VAL A 1 60  ? 40.929  -47.811 -32.841  1.00 54.93  ? 66  VAL A CB  1 
ATOM   448   C CG1 . VAL A 1 60  ? 41.629  -47.130 -31.676  1.00 59.08  ? 66  VAL A CG1 1 
ATOM   449   C CG2 . VAL A 1 60  ? 41.022  -46.953 -34.095  1.00 57.33  ? 66  VAL A CG2 1 
ATOM   450   N N   . ALA A 1 61  ? 40.428  -50.647 -31.470  1.00 56.86  ? 67  ALA A N   1 
ATOM   451   C CA  . ALA A 1 61  ? 40.367  -51.471 -30.266  1.00 56.40  ? 67  ALA A CA  1 
ATOM   452   C C   . ALA A 1 61  ? 41.283  -52.685 -30.378  1.00 61.39  ? 67  ALA A C   1 
ATOM   453   O O   . ALA A 1 61  ? 42.038  -52.996 -29.450  1.00 62.28  ? 67  ALA A O   1 
ATOM   454   C CB  . ALA A 1 61  ? 38.925  -51.904 -30.003  1.00 62.64  ? 67  ALA A CB  1 
ATOM   455   N N   . GLY A 1 62  ? 41.229  -53.386 -31.513  1.00 67.67  ? 68  GLY A N   1 
ATOM   456   C CA  . GLY A 1 62  ? 42.105  -54.529 -31.707  1.00 60.02  ? 68  GLY A CA  1 
ATOM   457   C C   . GLY A 1 62  ? 43.570  -54.147 -31.757  1.00 61.69  ? 68  GLY A C   1 
ATOM   458   O O   . GLY A 1 62  ? 44.435  -54.924 -31.343  1.00 64.50  ? 68  GLY A O   1 
ATOM   459   N N   . TRP A 1 63  ? 43.870  -52.954 -32.272  1.00 60.98  ? 69  TRP A N   1 
ATOM   460   C CA  . TRP A 1 63  ? 45.250  -52.487 -32.317  1.00 65.37  ? 69  TRP A CA  1 
ATOM   461   C C   . TRP A 1 63  ? 45.741  -52.062 -30.936  1.00 63.23  ? 69  TRP A C   1 
ATOM   462   O O   . TRP A 1 63  ? 46.873  -52.376 -30.552  1.00 64.11  ? 69  TRP A O   1 
ATOM   463   C CB  . TRP A 1 63  ? 45.372  -51.339 -33.321  1.00 58.73  ? 69  TRP A CB  1 
ATOM   464   C CG  . TRP A 1 63  ? 46.594  -50.492 -33.160  1.00 67.94  ? 69  TRP A CG  1 
ATOM   465   C CD1 . TRP A 1 63  ? 47.893  -50.898 -33.248  1.00 77.47  ? 69  TRP A CD1 1 
ATOM   466   C CD2 . TRP A 1 63  ? 46.630  -49.082 -32.909  1.00 69.80  ? 69  TRP A CD2 1 
ATOM   467   N NE1 . TRP A 1 63  ? 48.736  -49.830 -33.055  1.00 89.07  ? 69  TRP A NE1 1 
ATOM   468   C CE2 . TRP A 1 63  ? 47.985  -48.704 -32.845  1.00 77.87  ? 69  TRP A CE2 1 
ATOM   469   C CE3 . TRP A 1 63  ? 45.647  -48.104 -32.727  1.00 71.60  ? 69  TRP A CE3 1 
ATOM   470   C CZ2 . TRP A 1 63  ? 48.383  -47.390 -32.607  1.00 75.81  ? 69  TRP A CZ2 1 
ATOM   471   C CZ3 . TRP A 1 63  ? 46.044  -46.801 -32.490  1.00 75.12  ? 69  TRP A CZ3 1 
ATOM   472   C CH2 . TRP A 1 63  ? 47.400  -46.456 -32.432  1.00 76.73  ? 69  TRP A CH2 1 
ATOM   473   N N   . LEU A 1 64  ? 44.903  -51.352 -30.174  1.00 63.18  ? 70  LEU A N   1 
ATOM   474   C CA  . LEU A 1 64  ? 45.322  -50.868 -28.862  1.00 52.15  ? 70  LEU A CA  1 
ATOM   475   C C   . LEU A 1 64  ? 45.495  -52.015 -27.873  1.00 61.13  ? 70  LEU A C   1 
ATOM   476   O O   . LEU A 1 64  ? 46.519  -52.108 -27.187  1.00 58.47  ? 70  LEU A O   1 
ATOM   477   C CB  . LEU A 1 64  ? 44.310  -49.857 -28.325  1.00 54.88  ? 70  LEU A CB  1 
ATOM   478   C CG  . LEU A 1 64  ? 44.263  -48.480 -28.982  1.00 62.12  ? 70  LEU A CG  1 
ATOM   479   C CD1 . LEU A 1 64  ? 43.163  -47.652 -28.347  1.00 56.61  ? 70  LEU A CD1 1 
ATOM   480   C CD2 . LEU A 1 64  ? 45.607  -47.780 -28.859  1.00 59.74  ? 70  LEU A CD2 1 
ATOM   481   N N   . LEU A 1 65  ? 44.501  -52.899 -27.784  1.00 56.10  ? 71  LEU A N   1 
ATOM   482   C CA  . LEU A 1 65  ? 44.563  -53.992 -26.822  1.00 50.43  ? 71  LEU A CA  1 
ATOM   483   C C   . LEU A 1 65  ? 45.536  -55.084 -27.239  1.00 60.51  ? 71  LEU A C   1 
ATOM   484   O O   . LEU A 1 65  ? 45.886  -55.928 -26.407  1.00 57.74  ? 71  LEU A O   1 
ATOM   485   C CB  . LEU A 1 65  ? 43.171  -54.587 -26.611  1.00 70.92  ? 71  LEU A CB  1 
ATOM   486   C CG  . LEU A 1 65  ? 42.157  -53.648 -25.954  1.00 54.40  ? 71  LEU A CG  1 
ATOM   487   C CD1 . LEU A 1 65  ? 40.843  -54.362 -25.717  1.00 53.95  ? 71  LEU A CD1 1 
ATOM   488   C CD2 . LEU A 1 65  ? 42.711  -53.100 -24.650  1.00 46.97  ? 71  LEU A CD2 1 
ATOM   489   N N   . GLY A 1 66  ? 45.980  -55.087 -28.492  1.00 63.11  ? 72  GLY A N   1 
ATOM   490   C CA  . GLY A 1 66  ? 46.947  -56.066 -28.937  1.00 64.34  ? 72  GLY A CA  1 
ATOM   491   C C   . GLY A 1 66  ? 46.334  -57.398 -29.310  1.00 54.24  ? 72  GLY A C   1 
ATOM   492   O O   . GLY A 1 66  ? 46.668  -58.427 -28.716  1.00 55.57  ? 72  GLY A O   1 
ATOM   493   N N   . ASN A 1 67  ? 45.429  -57.386 -30.283  1.00 62.53  ? 73  ASN A N   1 
ATOM   494   C CA  . ASN A 1 67  ? 44.900  -58.630 -30.819  1.00 62.77  ? 73  ASN A CA  1 
ATOM   495   C C   . ASN A 1 67  ? 46.063  -59.489 -31.304  1.00 72.22  ? 73  ASN A C   1 
ATOM   496   O O   . ASN A 1 67  ? 46.924  -58.993 -32.043  1.00 72.61  ? 73  ASN A O   1 
ATOM   497   C CB  . ASN A 1 67  ? 43.925  -58.342 -31.966  1.00 71.30  ? 73  ASN A CB  1 
ATOM   498   C CG  . ASN A 1 67  ? 43.199  -59.588 -32.464  1.00 76.68  ? 73  ASN A CG  1 
ATOM   499   O OD1 . ASN A 1 67  ? 43.818  -60.603 -32.784  1.00 72.14  ? 73  ASN A OD1 1 
ATOM   500   N ND2 . ASN A 1 67  ? 41.875  -59.505 -32.540  1.00 73.36  ? 73  ASN A ND2 1 
ATOM   501   N N   . PRO A 1 68  ? 46.136  -60.762 -30.906  1.00 69.44  ? 74  PRO A N   1 
ATOM   502   C CA  . PRO A 1 68  ? 47.294  -61.582 -31.297  1.00 60.72  ? 74  PRO A CA  1 
ATOM   503   C C   . PRO A 1 68  ? 47.468  -61.709 -32.797  1.00 75.72  ? 74  PRO A C   1 
ATOM   504   O O   . PRO A 1 68  ? 48.584  -61.986 -33.252  1.00 82.73  ? 74  PRO A O   1 
ATOM   505   C CB  . PRO A 1 68  ? 47.002  -62.942 -30.646  1.00 66.90  ? 74  PRO A CB  1 
ATOM   506   C CG  . PRO A 1 68  ? 45.523  -62.935 -30.378  1.00 84.13  ? 74  PRO A CG  1 
ATOM   507   C CD  . PRO A 1 68  ? 45.186  -61.510 -30.066  1.00 65.42  ? 74  PRO A CD  1 
ATOM   508   N N   . MET A 1 69  ? 46.408  -61.513 -33.581  1.00 74.26  ? 75  MET A N   1 
ATOM   509   C CA  . MET A 1 69  ? 46.535  -61.506 -35.031  1.00 73.55  ? 75  MET A CA  1 
ATOM   510   C C   . MET A 1 69  ? 46.968  -60.153 -35.591  1.00 75.91  ? 75  MET A C   1 
ATOM   511   O O   . MET A 1 69  ? 47.459  -60.100 -36.724  1.00 100.89 ? 75  MET A O   1 
ATOM   512   C CB  . MET A 1 69  ? 45.217  -61.930 -35.674  1.00 84.37  ? 75  MET A CB  1 
ATOM   513   C CG  . MET A 1 69  ? 44.775  -63.342 -35.334  1.00 87.92  ? 75  MET A CG  1 
ATOM   514   S SD  . MET A 1 69  ? 46.003  -64.533 -35.900  1.00 122.27 ? 75  MET A SD  1 
ATOM   515   C CE  . MET A 1 69  ? 44.972  -65.918 -36.375  1.00 101.12 ? 75  MET A CE  1 
ATOM   516   N N   . CYS A 1 70  ? 46.794  -59.064 -34.845  1.00 84.28  ? 76  CYS A N   1 
ATOM   517   C CA  . CYS A 1 70  ? 47.189  -57.755 -35.355  1.00 95.31  ? 76  CYS A CA  1 
ATOM   518   C C   . CYS A 1 70  ? 48.704  -57.647 -35.464  1.00 98.63  ? 76  CYS A C   1 
ATOM   519   O O   . CYS A 1 70  ? 49.441  -58.056 -34.562  1.00 105.63 ? 76  CYS A O   1 
ATOM   520   C CB  . CYS A 1 70  ? 46.654  -56.638 -34.453  1.00 84.03  ? 76  CYS A CB  1 
ATOM   521   S SG  . CYS A 1 70  ? 44.963  -56.154 -34.826  1.00 114.41 ? 76  CYS A SG  1 
ATOM   522   N N   . ASP A 1 71  ? 49.170  -57.095 -36.585  1.00 104.06 ? 77  ASP A N   1 
ATOM   523   C CA  . ASP A 1 71  ? 50.572  -56.711 -36.741  1.00 113.72 ? 77  ASP A CA  1 
ATOM   524   C C   . ASP A 1 71  ? 50.679  -55.225 -36.416  1.00 119.41 ? 77  ASP A C   1 
ATOM   525   O O   . ASP A 1 71  ? 50.733  -54.364 -37.294  1.00 112.52 ? 77  ASP A O   1 
ATOM   526   C CB  . ASP A 1 71  ? 51.081  -57.022 -38.145  1.00 102.25 ? 77  ASP A CB  1 
ATOM   527   C CG  . ASP A 1 71  ? 51.784  -58.359 -38.226  1.00 125.11 ? 77  ASP A CG  1 
ATOM   528   O OD1 . ASP A 1 71  ? 52.033  -58.834 -39.354  1.00 132.03 ? 77  ASP A OD1 1 
ATOM   529   O OD2 . ASP A 1 71  ? 52.078  -58.938 -37.159  1.00 139.50 ? 77  ASP A OD2 1 
ATOM   530   N N   . GLU A 1 72  ? 50.714  -54.928 -35.118  1.00 128.62 ? 78  GLU A N   1 
ATOM   531   C CA  . GLU A 1 72  ? 50.703  -53.545 -34.664  1.00 135.51 ? 78  GLU A CA  1 
ATOM   532   C C   . GLU A 1 72  ? 52.043  -52.871 -34.921  1.00 139.39 ? 78  GLU A C   1 
ATOM   533   O O   . GLU A 1 72  ? 52.811  -52.632 -33.984  1.00 141.20 ? 78  GLU A O   1 
ATOM   534   C CB  . GLU A 1 72  ? 50.362  -53.467 -33.174  1.00 128.14 ? 78  GLU A CB  1 
ATOM   535   C CG  . GLU A 1 72  ? 49.069  -54.159 -32.789  1.00 112.92 ? 78  GLU A CG  1 
ATOM   536   C CD  . GLU A 1 72  ? 49.307  -55.495 -32.118  1.00 118.76 ? 78  GLU A CD  1 
ATOM   537   O OE1 . GLU A 1 72  ? 50.484  -55.864 -31.926  1.00 131.19 ? 78  GLU A OE1 1 
ATOM   538   O OE2 . GLU A 1 72  ? 48.317  -56.176 -31.778  1.00 108.96 ? 78  GLU A OE2 1 
ATOM   539   N N   . PHE A 1 73  ? 52.338  -52.565 -36.181  1.00 137.47 ? 79  PHE A N   1 
ATOM   540   C CA  . PHE A 1 73  ? 53.522  -51.772 -36.474  1.00 134.32 ? 79  PHE A CA  1 
ATOM   541   C C   . PHE A 1 73  ? 53.268  -50.330 -36.053  1.00 140.01 ? 79  PHE A C   1 
ATOM   542   O O   . PHE A 1 73  ? 52.247  -49.731 -36.406  1.00 159.33 ? 79  PHE A O   1 
ATOM   543   C CB  . PHE A 1 73  ? 53.890  -51.870 -37.959  1.00 131.92 ? 79  PHE A CB  1 
ATOM   544   C CG  . PHE A 1 73  ? 53.330  -50.763 -38.812  1.00 158.86 ? 79  PHE A CG  1 
ATOM   545   C CD1 . PHE A 1 73  ? 52.040  -50.840 -39.313  1.00 156.51 ? 79  PHE A CD1 1 
ATOM   546   C CD2 . PHE A 1 73  ? 54.099  -49.651 -39.120  1.00 155.48 ? 79  PHE A CD2 1 
ATOM   547   C CE1 . PHE A 1 73  ? 51.525  -49.824 -40.098  1.00 140.43 ? 79  PHE A CE1 1 
ATOM   548   C CE2 . PHE A 1 73  ? 53.589  -48.632 -39.902  1.00 153.82 ? 79  PHE A CE2 1 
ATOM   549   C CZ  . PHE A 1 73  ? 52.300  -48.719 -40.393  1.00 146.72 ? 79  PHE A CZ  1 
ATOM   550   N N   . ILE A 1 74  ? 54.177  -49.793 -35.248  1.00 119.15 ? 80  ILE A N   1 
ATOM   551   C CA  . ILE A 1 74  ? 54.086  -48.419 -34.775  1.00 131.42 ? 80  ILE A CA  1 
ATOM   552   C C   . ILE A 1 74  ? 55.355  -47.719 -35.238  1.00 132.13 ? 80  ILE A C   1 
ATOM   553   O O   . ILE A 1 74  ? 55.918  -46.872 -34.534  1.00 128.91 ? 80  ILE A O   1 
ATOM   554   C CB  . ILE A 1 74  ? 53.882  -48.357 -33.249  1.00 139.27 ? 80  ILE A CB  1 
ATOM   555   C CG1 . ILE A 1 74  ? 52.784  -49.342 -32.844  1.00 126.88 ? 80  ILE A CG1 1 
ATOM   556   C CG2 . ILE A 1 74  ? 53.468  -46.957 -32.808  1.00 119.46 ? 80  ILE A CG2 1 
ATOM   557   C CD1 . ILE A 1 74  ? 52.625  -49.517 -31.357  1.00 83.79  ? 80  ILE A CD1 1 
ATOM   558   N N   . ARG A 1 75  ? 55.827  -48.108 -36.428  1.00 129.49 ? 81  ARG A N   1 
ATOM   559   C CA  . ARG A 1 75  ? 56.977  -47.450 -37.040  1.00 134.09 ? 81  ARG A CA  1 
ATOM   560   C C   . ARG A 1 75  ? 56.751  -45.949 -37.163  1.00 133.88 ? 81  ARG A C   1 
ATOM   561   O O   . ARG A 1 75  ? 57.712  -45.176 -37.153  1.00 119.03 ? 81  ARG A O   1 
ATOM   562   C CB  . ARG A 1 75  ? 57.261  -48.070 -38.414  1.00 136.58 ? 81  ARG A CB  1 
ATOM   563   C CG  . ARG A 1 75  ? 58.541  -47.581 -39.097  1.00 145.42 ? 81  ARG A CG  1 
ATOM   564   C CD  . ARG A 1 75  ? 58.286  -46.394 -40.027  1.00 153.35 ? 81  ARG A CD  1 
ATOM   565   N NE  . ARG A 1 75  ? 59.522  -45.827 -40.556  1.00 147.11 ? 81  ARG A NE  1 
ATOM   566   C CZ  . ARG A 1 75  ? 59.885  -45.875 -41.830  1.00 124.62 ? 81  ARG A CZ  1 
ATOM   567   N NH1 . ARG A 1 75  ? 59.117  -46.439 -42.748  1.00 126.19 ? 81  ARG A NH1 1 
ATOM   568   N NH2 . ARG A 1 75  ? 61.045  -45.335 -42.195  1.00 109.13 ? 81  ARG A NH2 1 
ATOM   569   N N   . VAL A 1 76  ? 55.496  -45.521 -37.281  1.00 144.41 ? 82  VAL A N   1 
ATOM   570   C CA  . VAL A 1 76  ? 55.143  -44.104 -37.273  1.00 133.84 ? 82  VAL A CA  1 
ATOM   571   C C   . VAL A 1 76  ? 54.934  -43.684 -35.818  1.00 114.16 ? 82  VAL A C   1 
ATOM   572   O O   . VAL A 1 76  ? 53.996  -44.181 -35.175  1.00 124.53 ? 82  VAL A O   1 
ATOM   573   C CB  . VAL A 1 76  ? 53.901  -43.828 -38.133  1.00 130.83 ? 82  VAL A CB  1 
ATOM   574   C CG1 . VAL A 1 76  ? 54.259  -43.903 -39.609  1.00 126.57 ? 82  VAL A CG1 1 
ATOM   575   C CG2 . VAL A 1 76  ? 52.779  -44.820 -37.828  1.00 111.79 ? 82  VAL A CG2 1 
ATOM   576   N N   . PRO A 1 77  ? 55.776  -42.818 -35.263  1.00 95.24  ? 83  PRO A N   1 
ATOM   577   C CA  . PRO A 1 77  ? 55.499  -42.255 -33.934  1.00 84.01  ? 83  PRO A CA  1 
ATOM   578   C C   . PRO A 1 77  ? 54.612  -41.019 -33.949  1.00 73.66  ? 83  PRO A C   1 
ATOM   579   O O   . PRO A 1 77  ? 54.426  -40.408 -32.892  1.00 67.21  ? 83  PRO A O   1 
ATOM   580   C CB  . PRO A 1 77  ? 56.903  -41.896 -33.426  1.00 74.90  ? 83  PRO A CB  1 
ATOM   581   C CG  . PRO A 1 77  ? 57.652  -41.560 -34.665  1.00 94.05  ? 83  PRO A CG  1 
ATOM   582   C CD  . PRO A 1 77  ? 57.120  -42.440 -35.747  1.00 90.08  ? 83  PRO A CD  1 
ATOM   583   N N   . GLU A 1 78  A 54.068  -40.652 -35.106  1.00 80.49  ? 83  GLU A N   1 
ATOM   584   C CA  . GLU A 1 78  A 53.212  -39.483 -35.237  1.00 61.68  ? 83  GLU A CA  1 
ATOM   585   C C   . GLU A 1 78  A 52.339  -39.665 -36.470  1.00 73.44  ? 83  GLU A C   1 
ATOM   586   O O   . GLU A 1 78  A 52.767  -40.263 -37.459  1.00 74.06  ? 83  GLU A O   1 
ATOM   587   C CB  . GLU A 1 78  A 54.041  -38.196 -35.350  1.00 72.86  ? 83  GLU A CB  1 
ATOM   588   C CG  . GLU A 1 78  A 53.231  -36.916 -35.521  1.00 98.16  ? 83  GLU A CG  1 
ATOM   589   C CD  . GLU A 1 78  A 54.104  -35.719 -35.842  1.00 105.12 ? 83  GLU A CD  1 
ATOM   590   O OE1 . GLU A 1 78  A 55.299  -35.919 -36.150  1.00 106.97 ? 83  GLU A OE1 1 
ATOM   591   O OE2 . GLU A 1 78  A 53.595  -34.580 -35.786  1.00 99.43  ? 83  GLU A OE2 1 
ATOM   592   N N   . TRP A 1 79  ? 51.112  -39.148 -36.404  1.00 55.37  ? 84  TRP A N   1 
ATOM   593   C CA  . TRP A 1 79  ? 50.227  -39.192 -37.558  1.00 63.42  ? 84  TRP A CA  1 
ATOM   594   C C   . TRP A 1 79  ? 49.285  -37.998 -37.520  1.00 59.21  ? 84  TRP A C   1 
ATOM   595   O O   . TRP A 1 79  ? 49.041  -37.404 -36.467  1.00 66.87  ? 84  TRP A O   1 
ATOM   596   C CB  . TRP A 1 79  ? 49.435  -40.506 -37.626  1.00 47.89  ? 84  TRP A CB  1 
ATOM   597   C CG  . TRP A 1 79  ? 48.664  -40.836 -36.385  1.00 77.41  ? 84  TRP A CG  1 
ATOM   598   C CD1 . TRP A 1 79  ? 47.414  -40.402 -36.058  1.00 70.17  ? 84  TRP A CD1 1 
ATOM   599   C CD2 . TRP A 1 79  ? 49.087  -41.687 -35.313  1.00 72.77  ? 84  TRP A CD2 1 
ATOM   600   N NE1 . TRP A 1 79  ? 47.034  -40.922 -34.845  1.00 67.45  ? 84  TRP A NE1 1 
ATOM   601   C CE2 . TRP A 1 79  ? 48.043  -41.715 -34.367  1.00 75.63  ? 84  TRP A CE2 1 
ATOM   602   C CE3 . TRP A 1 79  ? 50.247  -42.425 -35.059  1.00 80.42  ? 84  TRP A CE3 1 
ATOM   603   C CZ2 . TRP A 1 79  ? 48.125  -42.452 -33.187  1.00 71.43  ? 84  TRP A CZ2 1 
ATOM   604   C CZ3 . TRP A 1 79  ? 50.326  -43.155 -33.886  1.00 74.18  ? 84  TRP A CZ3 1 
ATOM   605   C CH2 . TRP A 1 79  ? 49.271  -43.163 -32.966  1.00 65.88  ? 84  TRP A CH2 1 
ATOM   606   N N   . SER A 1 80  ? 48.763  -37.650 -38.696  1.00 60.76  ? 85  SER A N   1 
ATOM   607   C CA  . SER A 1 80  ? 47.849  -36.526 -38.848  1.00 67.55  ? 85  SER A CA  1 
ATOM   608   C C   . SER A 1 80  ? 46.388  -36.946 -38.870  1.00 66.97  ? 85  SER A C   1 
ATOM   609   O O   . SER A 1 80  ? 45.524  -36.162 -38.464  1.00 67.82  ? 85  SER A O   1 
ATOM   610   C CB  . SER A 1 80  ? 48.172  -35.755 -40.133  1.00 71.15  ? 85  SER A CB  1 
ATOM   611   O OG  . SER A 1 80  ? 48.176  -36.620 -41.255  1.00 58.72  ? 85  SER A OG  1 
ATOM   612   N N   . TYR A 1 81  ? 46.096  -38.158 -39.333  1.00 55.70  ? 86  TYR A N   1 
ATOM   613   C CA  . TYR A 1 81  ? 44.749  -38.711 -39.286  1.00 65.13  ? 86  TYR A CA  1 
ATOM   614   C C   . TYR A 1 81  ? 44.864  -40.229 -39.362  1.00 63.30  ? 86  TYR A C   1 
ATOM   615   O O   . TYR A 1 81  ? 45.957  -40.780 -39.519  1.00 54.37  ? 86  TYR A O   1 
ATOM   616   C CB  . TYR A 1 81  ? 43.864  -38.136 -40.398  1.00 54.28  ? 86  TYR A CB  1 
ATOM   617   C CG  . TYR A 1 81  ? 44.307  -38.455 -41.808  1.00 66.54  ? 86  TYR A CG  1 
ATOM   618   C CD1 . TYR A 1 81  ? 45.372  -37.780 -42.394  1.00 67.68  ? 86  TYR A CD1 1 
ATOM   619   C CD2 . TYR A 1 81  ? 43.644  -39.413 -42.565  1.00 66.04  ? 86  TYR A CD2 1 
ATOM   620   C CE1 . TYR A 1 81  ? 45.774  -38.062 -43.685  1.00 71.06  ? 86  TYR A CE1 1 
ATOM   621   C CE2 . TYR A 1 81  ? 44.037  -39.701 -43.857  1.00 62.33  ? 86  TYR A CE2 1 
ATOM   622   C CZ  . TYR A 1 81  ? 45.102  -39.023 -44.412  1.00 65.05  ? 86  TYR A CZ  1 
ATOM   623   O OH  . TYR A 1 81  ? 45.495  -39.311 -45.699  1.00 58.55  ? 86  TYR A OH  1 
ATOM   624   N N   . ILE A 1 82  ? 43.725  -40.905 -39.242  1.00 68.37  ? 87  ILE A N   1 
ATOM   625   C CA  . ILE A 1 82  ? 43.670  -42.361 -39.165  1.00 61.67  ? 87  ILE A CA  1 
ATOM   626   C C   . ILE A 1 82  ? 42.801  -42.880 -40.302  1.00 62.11  ? 87  ILE A C   1 
ATOM   627   O O   . ILE A 1 82  ? 41.698  -42.370 -40.529  1.00 63.13  ? 87  ILE A O   1 
ATOM   628   C CB  . ILE A 1 82  ? 43.132  -42.834 -37.802  1.00 66.45  ? 87  ILE A CB  1 
ATOM   629   C CG1 . ILE A 1 82  ? 44.184  -42.633 -36.710  1.00 59.37  ? 87  ILE A CG1 1 
ATOM   630   C CG2 . ILE A 1 82  ? 42.684  -44.284 -37.867  1.00 64.68  ? 87  ILE A CG2 1 
ATOM   631   C CD1 . ILE A 1 82  ? 43.774  -43.182 -35.363  1.00 50.52  ? 87  ILE A CD1 1 
ATOM   632   N N   . VAL A 1 83  ? 43.298  -43.891 -41.010  1.00 61.47  ? 88  VAL A N   1 
ATOM   633   C CA  . VAL A 1 83  ? 42.576  -44.529 -42.102  1.00 70.41  ? 88  VAL A CA  1 
ATOM   634   C C   . VAL A 1 83  ? 42.151  -45.916 -41.641  1.00 61.43  ? 88  VAL A C   1 
ATOM   635   O O   . VAL A 1 83  ? 42.995  -46.758 -41.311  1.00 71.72  ? 88  VAL A O   1 
ATOM   636   C CB  . VAL A 1 83  ? 43.425  -44.613 -43.378  1.00 70.11  ? 88  VAL A CB  1 
ATOM   637   C CG1 . VAL A 1 83  ? 42.659  -45.318 -44.484  1.00 57.97  ? 88  VAL A CG1 1 
ATOM   638   C CG2 . VAL A 1 83  ? 43.853  -43.224 -43.825  1.00 57.05  ? 88  VAL A CG2 1 
ATOM   639   N N   . GLU A 1 84  ? 40.843  -46.152 -41.619  1.00 64.14  ? 89  GLU A N   1 
ATOM   640   C CA  . GLU A 1 84  ? 40.272  -47.460 -41.337  1.00 70.72  ? 89  GLU A CA  1 
ATOM   641   C C   . GLU A 1 84  ? 39.623  -48.009 -42.600  1.00 74.07  ? 89  GLU A C   1 
ATOM   642   O O   . GLU A 1 84  ? 39.059  -47.255 -43.398  1.00 81.92  ? 89  GLU A O   1 
ATOM   643   C CB  . GLU A 1 84  ? 39.235  -47.382 -40.214  1.00 88.85  ? 89  GLU A CB  1 
ATOM   644   C CG  . GLU A 1 84  ? 39.804  -47.563 -38.816  1.00 81.29  ? 89  GLU A CG  1 
ATOM   645   C CD  . GLU A 1 84  ? 38.731  -47.523 -37.744  1.00 106.16 ? 89  GLU A CD  1 
ATOM   646   O OE1 . GLU A 1 84  ? 37.710  -46.829 -37.949  1.00 94.08  ? 89  GLU A OE1 1 
ATOM   647   O OE2 . GLU A 1 84  ? 38.906  -48.186 -36.700  1.00 109.86 ? 89  GLU A OE2 1 
ATOM   648   N N   . ARG A 1 85  ? 39.704  -49.322 -42.785  1.00 90.77  ? 90  ARG A N   1 
ATOM   649   C CA  . ARG A 1 85  ? 39.100  -49.953 -43.948  1.00 75.97  ? 90  ARG A CA  1 
ATOM   650   C C   . ARG A 1 85  ? 37.640  -50.286 -43.641  1.00 104.26 ? 90  ARG A C   1 
ATOM   651   O O   . ARG A 1 85  ? 37.095  -49.894 -42.606  1.00 103.17 ? 90  ARG A O   1 
ATOM   652   C CB  . ARG A 1 85  ? 39.910  -51.178 -44.372  1.00 66.22  ? 90  ARG A CB  1 
ATOM   653   C CG  . ARG A 1 85  ? 41.040  -50.869 -45.353  1.00 91.25  ? 90  ARG A CG  1 
ATOM   654   C CD  . ARG A 1 85  ? 42.168  -50.082 -44.697  1.00 101.58 ? 90  ARG A CD  1 
ATOM   655   N NE  . ARG A 1 85  ? 42.737  -49.077 -45.588  1.00 107.31 ? 90  ARG A NE  1 
ATOM   656   C CZ  . ARG A 1 85  ? 43.699  -49.313 -46.470  1.00 109.58 ? 90  ARG A CZ  1 
ATOM   657   N NH1 . ARG A 1 85  ? 44.216  -50.521 -46.623  1.00 111.07 ? 90  ARG A NH1 1 
ATOM   658   N NH2 . ARG A 1 85  ? 44.152  -48.311 -47.218  1.00 81.60  ? 90  ARG A NH2 1 
ATOM   659   N N   . ALA A 1 86  ? 36.989  -51.024 -44.544  1.00 124.78 ? 91  ALA A N   1 
ATOM   660   C CA  . ALA A 1 86  ? 35.554  -51.264 -44.418  1.00 129.56 ? 91  ALA A CA  1 
ATOM   661   C C   . ALA A 1 86  ? 35.246  -52.291 -43.333  1.00 127.68 ? 91  ALA A C   1 
ATOM   662   O O   . ALA A 1 86  ? 34.464  -52.018 -42.416  1.00 99.47  ? 91  ALA A O   1 
ATOM   663   C CB  . ALA A 1 86  ? 34.975  -51.712 -45.762  1.00 101.29 ? 91  ALA A CB  1 
ATOM   664   N N   . ASN A 1 87  ? 35.848  -53.476 -43.422  1.00 122.71 ? 92  ASN A N   1 
ATOM   665   C CA  . ASN A 1 87  ? 35.607  -54.560 -42.471  1.00 121.69 ? 92  ASN A CA  1 
ATOM   666   C C   . ASN A 1 87  ? 36.935  -55.022 -41.889  1.00 119.12 ? 92  ASN A C   1 
ATOM   667   O O   . ASN A 1 87  ? 37.604  -55.900 -42.453  1.00 117.49 ? 92  ASN A O   1 
ATOM   668   C CB  . ASN A 1 87  ? 34.862  -55.720 -43.130  1.00 124.89 ? 92  ASN A CB  1 
ATOM   669   C CG  . ASN A 1 87  ? 33.452  -55.347 -43.548  1.00 138.86 ? 92  ASN A CG  1 
ATOM   670   O OD1 . ASN A 1 87  ? 32.950  -55.815 -44.570  1.00 136.01 ? 92  ASN A OD1 1 
ATOM   671   N ND2 . ASN A 1 87  ? 32.806  -54.497 -42.757  1.00 114.99 ? 92  ASN A ND2 1 
ATOM   672   N N   . PRO A 1 88  ? 37.349  -54.458 -40.753  1.00 113.02 ? 93  PRO A N   1 
ATOM   673   C CA  . PRO A 1 88  ? 38.594  -54.906 -40.112  1.00 96.07  ? 93  PRO A CA  1 
ATOM   674   C C   . PRO A 1 88  ? 38.393  -56.282 -39.495  1.00 102.30 ? 93  PRO A C   1 
ATOM   675   O O   . PRO A 1 88  ? 37.548  -56.460 -38.616  1.00 106.63 ? 93  PRO A O   1 
ATOM   676   C CB  . PRO A 1 88  ? 38.849  -53.838 -39.038  1.00 84.87  ? 93  PRO A CB  1 
ATOM   677   C CG  . PRO A 1 88  ? 37.790  -52.765 -39.251  1.00 88.29  ? 93  PRO A CG  1 
ATOM   678   C CD  . PRO A 1 88  ? 36.658  -53.441 -39.949  1.00 109.11 ? 93  PRO A CD  1 
ATOM   679   N N   . ALA A 1 89  ? 39.166  -57.260 -39.968  1.00 99.67  ? 94  ALA A N   1 
ATOM   680   C CA  . ALA A 1 89  ? 39.048  -58.610 -39.428  1.00 106.71 ? 94  ALA A CA  1 
ATOM   681   C C   . ALA A 1 89  ? 39.430  -58.647 -37.957  1.00 100.91 ? 94  ALA A C   1 
ATOM   682   O O   . ALA A 1 89  ? 38.749  -59.281 -37.143  1.00 108.68 ? 94  ALA A O   1 
ATOM   683   C CB  . ALA A 1 89  ? 39.924  -59.570 -40.229  1.00 100.86 ? 94  ALA A CB  1 
ATOM   684   N N   . ASN A 1 90  ? 40.505  -57.953 -37.597  1.00 101.88 ? 95  ASN A N   1 
ATOM   685   C CA  . ASN A 1 90  ? 41.044  -57.998 -36.240  1.00 95.70  ? 95  ASN A CA  1 
ATOM   686   C C   . ASN A 1 90  ? 40.422  -56.876 -35.413  1.00 91.06  ? 95  ASN A C   1 
ATOM   687   O O   . ASN A 1 90  ? 40.898  -55.738 -35.398  1.00 89.71  ? 95  ASN A O   1 
ATOM   688   C CB  . ASN A 1 90  ? 42.562  -57.901 -36.270  1.00 97.95  ? 95  ASN A CB  1 
ATOM   689   C CG  . ASN A 1 90  ? 43.170  -58.760 -37.348  1.00 104.62 ? 95  ASN A CG  1 
ATOM   690   O OD1 . ASN A 1 90  ? 43.457  -59.936 -37.141  1.00 114.78 ? 95  ASN A OD1 1 
ATOM   691   N ND2 . ASN A 1 90  ? 43.369  -58.172 -38.516  1.00 116.79 ? 95  ASN A ND2 1 
ATOM   692   N N   . ASP A 1 91  ? 39.355  -57.220 -34.702  1.00 88.07  ? 96  ASP A N   1 
ATOM   693   C CA  . ASP A 1 91  ? 38.621  -56.358 -33.796  1.00 93.26  ? 96  ASP A CA  1 
ATOM   694   C C   . ASP A 1 91  ? 38.716  -56.986 -32.412  1.00 91.78  ? 96  ASP A C   1 
ATOM   695   O O   . ASP A 1 91  ? 39.549  -57.876 -32.183  1.00 88.40  ? 96  ASP A O   1 
ATOM   696   C CB  . ASP A 1 91  ? 37.167  -56.187 -34.245  1.00 98.97  ? 96  ASP A CB  1 
ATOM   697   C CG  . ASP A 1 91  ? 36.497  -54.990 -33.595  1.00 106.77 ? 96  ASP A CG  1 
ATOM   698   O OD1 . ASP A 1 91  ? 37.215  -54.057 -33.171  1.00 87.56  ? 96  ASP A OD1 1 
ATOM   699   O OD2 . ASP A 1 91  ? 35.257  -54.979 -33.493  1.00 95.17  ? 96  ASP A OD2 1 
ATOM   700   N N   . LEU A 1 92  A 37.895  -56.512 -31.469  1.00 77.78  ? 96  LEU A N   1 
ATOM   701   C CA  . LEU A 1 92  A 37.835  -57.169 -30.167  1.00 68.46  ? 96  LEU A CA  1 
ATOM   702   C C   . LEU A 1 92  A 37.496  -58.634 -30.406  1.00 66.53  ? 96  LEU A C   1 
ATOM   703   O O   . LEU A 1 92  A 36.360  -58.965 -30.759  1.00 68.19  ? 96  LEU A O   1 
ATOM   704   C CB  . LEU A 1 92  A 36.785  -56.518 -29.264  1.00 69.96  ? 96  LEU A CB  1 
ATOM   705   C CG  . LEU A 1 92  A 36.949  -55.046 -28.879  1.00 81.89  ? 96  LEU A CG  1 
ATOM   706   C CD1 . LEU A 1 92  A 35.693  -54.558 -28.178  1.00 67.99  ? 96  LEU A CD1 1 
ATOM   707   C CD2 . LEU A 1 92  A 38.151  -54.887 -27.980  1.00 59.51  ? 96  LEU A CD2 1 
ATOM   708   N N   . CYS A 1 93  ? 38.477  -59.518 -30.220  1.00 60.04  ? 97  CYS A N   1 
ATOM   709   C CA  . CYS A 1 93  ? 38.261  -60.925 -30.532  1.00 57.12  ? 97  CYS A CA  1 
ATOM   710   C C   . CYS A 1 93  ? 37.388  -61.585 -29.476  1.00 56.13  ? 97  CYS A C   1 
ATOM   711   O O   . CYS A 1 93  ? 36.455  -62.329 -29.801  1.00 64.30  ? 97  CYS A O   1 
ATOM   712   C CB  . CYS A 1 93  ? 39.606  -61.642 -30.672  1.00 54.10  ? 97  CYS A CB  1 
ATOM   713   S SG  . CYS A 1 93  ? 40.817  -61.240 -29.394  1.00 92.01  ? 97  CYS A SG  1 
ATOM   714   N N   . TYR A 1 94  ? 37.668  -61.316 -28.210  1.00 59.91  ? 98  TYR A N   1 
ATOM   715   C CA  . TYR A 1 94  ? 36.765  -61.748 -27.156  1.00 58.24  ? 98  TYR A CA  1 
ATOM   716   C C   . TYR A 1 94  ? 35.564  -60.812 -27.113  1.00 56.12  ? 98  TYR A C   1 
ATOM   717   O O   . TYR A 1 94  ? 35.743  -59.592 -27.038  1.00 60.72  ? 98  TYR A O   1 
ATOM   718   C CB  . TYR A 1 94  ? 37.470  -61.765 -25.805  1.00 47.14  ? 98  TYR A CB  1 
ATOM   719   C CG  . TYR A 1 94  ? 36.828  -62.695 -24.805  1.00 65.30  ? 98  TYR A CG  1 
ATOM   720   C CD1 . TYR A 1 94  ? 35.722  -62.298 -24.069  1.00 57.88  ? 98  TYR A CD1 1 
ATOM   721   C CD2 . TYR A 1 94  ? 37.324  -63.976 -24.603  1.00 55.25  ? 98  TYR A CD2 1 
ATOM   722   C CE1 . TYR A 1 94  ? 35.129  -63.147 -23.155  1.00 50.71  ? 98  TYR A CE1 1 
ATOM   723   C CE2 . TYR A 1 94  ? 36.740  -64.831 -23.689  1.00 48.49  ? 98  TYR A CE2 1 
ATOM   724   C CZ  . TYR A 1 94  ? 35.641  -64.413 -22.971  1.00 43.01  ? 98  TYR A CZ  1 
ATOM   725   O OH  . TYR A 1 94  ? 35.055  -65.263 -22.062  1.00 47.64  ? 98  TYR A OH  1 
ATOM   726   N N   . PRO A 1 95  ? 34.339  -61.334 -27.174  1.00 56.10  ? 99  PRO A N   1 
ATOM   727   C CA  . PRO A 1 95  ? 33.166  -60.455 -27.252  1.00 54.43  ? 99  PRO A CA  1 
ATOM   728   C C   . PRO A 1 95  ? 33.058  -59.547 -26.038  1.00 55.66  ? 99  PRO A C   1 
ATOM   729   O O   . PRO A 1 95  ? 33.411  -59.921 -24.916  1.00 53.31  ? 99  PRO A O   1 
ATOM   730   C CB  . PRO A 1 95  ? 31.990  -61.438 -27.326  1.00 46.97  ? 99  PRO A CB  1 
ATOM   731   C CG  . PRO A 1 95  ? 32.517  -62.703 -26.741  1.00 47.70  ? 99  PRO A CG  1 
ATOM   732   C CD  . PRO A 1 95  ? 33.963  -62.756 -27.121  1.00 54.95  ? 99  PRO A CD  1 
ATOM   733   N N   . GLY A 1 96  ? 32.568  -58.339 -26.281  1.00 50.05  ? 100 GLY A N   1 
ATOM   734   C CA  . GLY A 1 96  ? 32.455  -57.337 -25.243  1.00 47.40  ? 100 GLY A CA  1 
ATOM   735   C C   . GLY A 1 96  ? 32.392  -55.942 -25.832  1.00 58.18  ? 100 GLY A C   1 
ATOM   736   O O   . GLY A 1 96  ? 31.796  -55.737 -26.887  1.00 61.39  ? 100 GLY A O   1 
ATOM   737   N N   . SER A 1 97  ? 33.022  -54.979 -25.152  1.00 54.62  ? 101 SER A N   1 
ATOM   738   C CA  . SER A 1 97  ? 32.985  -53.592 -25.592  1.00 56.89  ? 101 SER A CA  1 
ATOM   739   C C   . SER A 1 97  ? 34.195  -52.846 -25.048  1.00 49.23  ? 101 SER A C   1 
ATOM   740   O O   . SER A 1 97  ? 34.935  -53.349 -24.197  1.00 57.21  ? 101 SER A O   1 
ATOM   741   C CB  . SER A 1 97  ? 31.692  -52.897 -25.148  1.00 56.80  ? 101 SER A CB  1 
ATOM   742   O OG  . SER A 1 97  ? 31.606  -52.812 -23.734  1.00 59.62  ? 101 SER A OG  1 
ATOM   743   N N   . LEU A 1 98  ? 34.387  -51.631 -25.561  1.00 45.22  ? 102 LEU A N   1 
ATOM   744   C CA  . LEU A 1 98  ? 35.392  -50.693 -25.076  1.00 54.26  ? 102 LEU A CA  1 
ATOM   745   C C   . LEU A 1 98  ? 34.693  -49.377 -24.772  1.00 54.19  ? 102 LEU A C   1 
ATOM   746   O O   . LEU A 1 98  ? 34.130  -48.750 -25.675  1.00 52.92  ? 102 LEU A O   1 
ATOM   747   C CB  . LEU A 1 98  ? 36.513  -50.491 -26.102  1.00 45.69  ? 102 LEU A CB  1 
ATOM   748   C CG  . LEU A 1 98  ? 37.577  -49.444 -25.766  1.00 50.21  ? 102 LEU A CG  1 
ATOM   749   C CD1 . LEU A 1 98  ? 38.186  -49.694 -24.391  1.00 54.60  ? 102 LEU A CD1 1 
ATOM   750   C CD2 . LEU A 1 98  ? 38.654  -49.441 -26.836  1.00 50.12  ? 102 LEU A CD2 1 
ATOM   751   N N   . ASN A 1 99  ? 34.722  -48.968 -23.506  1.00 51.92  ? 103 ASN A N   1 
ATOM   752   C CA  . ASN A 1 99  ? 33.950  -47.811 -23.072  1.00 41.18  ? 103 ASN A CA  1 
ATOM   753   C C   . ASN A 1 99  ? 34.478  -46.531 -23.710  1.00 59.69  ? 103 ASN A C   1 
ATOM   754   O O   . ASN A 1 99  ? 35.689  -46.348 -23.864  1.00 59.12  ? 103 ASN A O   1 
ATOM   755   C CB  . ASN A 1 99  ? 33.987  -47.700 -21.548  1.00 51.22  ? 103 ASN A CB  1 
ATOM   756   C CG  . ASN A 1 99  ? 32.817  -46.911 -20.988  1.00 53.54  ? 103 ASN A CG  1 
ATOM   757   O OD1 . ASN A 1 99  ? 32.934  -45.715 -20.730  1.00 63.62  ? 103 ASN A OD1 1 
ATOM   758   N ND2 . ASN A 1 99  ? 31.683  -47.581 -20.792  1.00 62.66  ? 103 ASN A ND2 1 
ATOM   759   N N   . ASP A 1 100 ? 33.551  -45.643 -24.082  1.00 51.52  ? 104 ASP A N   1 
ATOM   760   C CA  . ASP A 1 100 ? 33.885  -44.362 -24.709  1.00 57.07  ? 104 ASP A CA  1 
ATOM   761   C C   . ASP A 1 100 ? 34.773  -44.565 -25.934  1.00 51.85  ? 104 ASP A C   1 
ATOM   762   O O   . ASP A 1 100 ? 35.770  -43.866 -26.133  1.00 54.91  ? 104 ASP A O   1 
ATOM   763   C CB  . ASP A 1 100 ? 34.539  -43.413 -23.703  1.00 46.03  ? 104 ASP A CB  1 
ATOM   764   C CG  . ASP A 1 100 ? 33.612  -43.046 -22.561  1.00 59.04  ? 104 ASP A CG  1 
ATOM   765   O OD1 . ASP A 1 100 ? 32.378  -43.108 -22.751  1.00 67.70  ? 104 ASP A OD1 1 
ATOM   766   O OD2 . ASP A 1 100 ? 34.116  -42.688 -21.476  1.00 76.69  ? 104 ASP A OD2 1 
ATOM   767   N N   . TYR A 1 101 ? 34.403  -45.545 -26.761  1.00 42.19  ? 105 TYR A N   1 
ATOM   768   C CA  . TYR A 1 101 ? 35.223  -45.910 -27.912  1.00 57.38  ? 105 TYR A CA  1 
ATOM   769   C C   . TYR A 1 101 ? 35.291  -44.774 -28.927  1.00 43.22  ? 105 TYR A C   1 
ATOM   770   O O   . TYR A 1 101 ? 36.366  -44.450 -29.446  1.00 68.51  ? 105 TYR A O   1 
ATOM   771   C CB  . TYR A 1 101 ? 34.668  -47.181 -28.556  1.00 41.81  ? 105 TYR A CB  1 
ATOM   772   C CG  . TYR A 1 101 ? 35.589  -47.825 -29.569  1.00 53.53  ? 105 TYR A CG  1 
ATOM   773   C CD1 . TYR A 1 101 ? 36.959  -47.620 -29.524  1.00 56.97  ? 105 TYR A CD1 1 
ATOM   774   C CD2 . TYR A 1 101 ? 35.081  -48.641 -30.572  1.00 61.52  ? 105 TYR A CD2 1 
ATOM   775   C CE1 . TYR A 1 101 ? 37.800  -48.211 -30.448  1.00 58.39  ? 105 TYR A CE1 1 
ATOM   776   C CE2 . TYR A 1 101 ? 35.913  -49.235 -31.500  1.00 54.05  ? 105 TYR A CE2 1 
ATOM   777   C CZ  . TYR A 1 101 ? 37.270  -49.018 -31.435  1.00 56.67  ? 105 TYR A CZ  1 
ATOM   778   O OH  . TYR A 1 101 ? 38.107  -49.607 -32.356  1.00 77.07  ? 105 TYR A OH  1 
ATOM   779   N N   . GLU A 1 102 ? 34.143  -44.159 -29.226  1.00 47.03  ? 106 GLU A N   1 
ATOM   780   C CA  . GLU A 1 102 ? 34.111  -43.079 -30.211  1.00 57.80  ? 106 GLU A CA  1 
ATOM   781   C C   . GLU A 1 102 ? 34.938  -41.881 -29.756  1.00 54.15  ? 106 GLU A C   1 
ATOM   782   O O   . GLU A 1 102 ? 35.679  -41.291 -30.552  1.00 70.20  ? 106 GLU A O   1 
ATOM   783   C CB  . GLU A 1 102 ? 32.664  -42.663 -30.487  1.00 58.53  ? 106 GLU A CB  1 
ATOM   784   C CG  . GLU A 1 102 ? 31.879  -43.643 -31.355  1.00 58.20  ? 106 GLU A CG  1 
ATOM   785   C CD  . GLU A 1 102 ? 32.225  -43.544 -32.835  1.00 87.11  ? 106 GLU A CD  1 
ATOM   786   O OE1 . GLU A 1 102 ? 33.118  -42.747 -33.197  1.00 104.78 ? 106 GLU A OE1 1 
ATOM   787   O OE2 . GLU A 1 102 ? 31.597  -44.264 -33.640  1.00 91.64  ? 106 GLU A OE2 1 
ATOM   788   N N   . GLU A 1 103 ? 34.823  -41.504 -28.481  1.00 64.61  ? 107 GLU A N   1 
ATOM   789   C CA  . GLU A 1 103 ? 35.662  -40.434 -27.952  1.00 64.51  ? 107 GLU A CA  1 
ATOM   790   C C   . GLU A 1 103 ? 37.131  -40.833 -27.938  1.00 58.00  ? 107 GLU A C   1 
ATOM   791   O O   . GLU A 1 103 ? 38.004  -39.979 -28.128  1.00 52.30  ? 107 GLU A O   1 
ATOM   792   C CB  . GLU A 1 103 ? 35.199  -40.045 -26.548  1.00 51.55  ? 107 GLU A CB  1 
ATOM   793   C CG  . GLU A 1 103 ? 33.923  -39.220 -26.527  1.00 69.76  ? 107 GLU A CG  1 
ATOM   794   C CD  . GLU A 1 103 ? 34.141  -37.799 -27.011  1.00 72.78  ? 107 GLU A CD  1 
ATOM   795   O OE1 . GLU A 1 103 ? 35.230  -37.245 -26.747  1.00 67.98  ? 107 GLU A OE1 1 
ATOM   796   O OE2 . GLU A 1 103 ? 33.227  -37.238 -27.653  1.00 63.01  ? 107 GLU A OE2 1 
ATOM   797   N N   . LEU A 1 104 ? 37.423  -42.116 -27.706  1.00 52.29  ? 108 LEU A N   1 
ATOM   798   C CA  . LEU A 1 104 ? 38.805  -42.580 -27.753  1.00 49.85  ? 108 LEU A CA  1 
ATOM   799   C C   . LEU A 1 104 ? 39.368  -42.508 -29.169  1.00 60.78  ? 108 LEU A C   1 
ATOM   800   O O   . LEU A 1 104 ? 40.516  -42.092 -29.365  1.00 58.44  ? 108 LEU A O   1 
ATOM   801   C CB  . LEU A 1 104 ? 38.900  -44.006 -27.212  1.00 56.42  ? 108 LEU A CB  1 
ATOM   802   C CG  . LEU A 1 104 ? 40.298  -44.625 -27.207  1.00 49.32  ? 108 LEU A CG  1 
ATOM   803   C CD1 . LEU A 1 104 ? 41.236  -43.837 -26.304  1.00 58.91  ? 108 LEU A CD1 1 
ATOM   804   C CD2 . LEU A 1 104 ? 40.235  -46.081 -26.782  1.00 55.13  ? 108 LEU A CD2 1 
ATOM   805   N N   . LYS A 1 105 ? 38.580  -42.916 -30.167  1.00 56.48  ? 109 LYS A N   1 
ATOM   806   C CA  . LYS A 1 105 ? 39.042  -42.838 -31.550  1.00 49.44  ? 109 LYS A CA  1 
ATOM   807   C C   . LYS A 1 105 ? 39.247  -41.391 -31.979  1.00 56.41  ? 109 LYS A C   1 
ATOM   808   O O   . LYS A 1 105 ? 40.191  -41.081 -32.716  1.00 64.03  ? 109 LYS A O   1 
ATOM   809   C CB  . LYS A 1 105 ? 38.055  -43.543 -32.480  1.00 50.11  ? 109 LYS A CB  1 
ATOM   810   C CG  . LYS A 1 105 ? 38.057  -45.060 -32.364  1.00 60.39  ? 109 LYS A CG  1 
ATOM   811   C CD  . LYS A 1 105 ? 37.189  -45.688 -33.443  1.00 58.32  ? 109 LYS A CD  1 
ATOM   812   C CE  . LYS A 1 105 ? 35.735  -45.283 -33.279  1.00 63.87  ? 109 LYS A CE  1 
ATOM   813   N NZ  . LYS A 1 105 ? 35.122  -44.891 -34.579  1.00 89.85  ? 109 LYS A NZ  1 
ATOM   814   N N   . HIS A 1 106 ? 38.364  -40.492 -31.537  1.00 51.14  ? 110 HIS A N   1 
ATOM   815   C CA  . HIS A 1 106 ? 38.535  -39.075 -31.838  1.00 59.11  ? 110 HIS A CA  1 
ATOM   816   C C   . HIS A 1 106 ? 39.814  -38.531 -31.213  1.00 56.52  ? 110 HIS A C   1 
ATOM   817   O O   . HIS A 1 106 ? 40.515  -37.714 -31.822  1.00 67.93  ? 110 HIS A O   1 
ATOM   818   C CB  . HIS A 1 106 ? 37.321  -38.287 -31.346  1.00 58.22  ? 110 HIS A CB  1 
ATOM   819   C CG  . HIS A 1 106 ? 37.333  -36.845 -31.750  1.00 62.67  ? 110 HIS A CG  1 
ATOM   820   N ND1 . HIS A 1 106 ? 36.907  -36.416 -32.988  1.00 64.34  ? 110 HIS A ND1 1 
ATOM   821   C CD2 . HIS A 1 106 ? 37.720  -35.734 -31.079  1.00 65.41  ? 110 HIS A CD2 1 
ATOM   822   C CE1 . HIS A 1 106 ? 37.029  -35.103 -33.063  1.00 78.10  ? 110 HIS A CE1 1 
ATOM   823   N NE2 . HIS A 1 106 ? 37.520  -34.664 -31.918  1.00 73.18  ? 110 HIS A NE2 1 
ATOM   824   N N   . LEU A 1 107 ? 40.129  -38.969 -29.991  1.00 58.46  ? 111 LEU A N   1 
ATOM   825   C CA  . LEU A 1 107 ? 41.349  -38.521 -29.325  1.00 59.24  ? 111 LEU A CA  1 
ATOM   826   C C   . LEU A 1 107 ? 42.593  -38.985 -30.073  1.00 61.30  ? 111 LEU A C   1 
ATOM   827   O O   . LEU A 1 107 ? 43.562  -38.230 -30.212  1.00 67.46  ? 111 LEU A O   1 
ATOM   828   C CB  . LEU A 1 107 ? 41.376  -39.034 -27.885  1.00 57.46  ? 111 LEU A CB  1 
ATOM   829   C CG  . LEU A 1 107 ? 42.529  -38.550 -27.002  1.00 44.99  ? 111 LEU A CG  1 
ATOM   830   C CD1 . LEU A 1 107 ? 42.230  -37.171 -26.430  1.00 59.82  ? 111 LEU A CD1 1 
ATOM   831   C CD2 . LEU A 1 107 ? 42.832  -39.547 -25.891  1.00 56.05  ? 111 LEU A CD2 1 
ATOM   832   N N   . LEU A 1 108 ? 42.586  -40.225 -30.557  1.00 59.78  ? 112 LEU A N   1 
ATOM   833   C CA  . LEU A 1 108 ? 43.740  -40.807 -31.228  1.00 61.40  ? 112 LEU A CA  1 
ATOM   834   C C   . LEU A 1 108 ? 43.823  -40.446 -32.705  1.00 59.19  ? 112 LEU A C   1 
ATOM   835   O O   . LEU A 1 108 ? 44.762  -40.888 -33.375  1.00 69.07  ? 112 LEU A O   1 
ATOM   836   C CB  . LEU A 1 108 ? 43.717  -42.329 -31.077  1.00 54.77  ? 112 LEU A CB  1 
ATOM   837   C CG  . LEU A 1 108 ? 43.924  -42.881 -29.667  1.00 59.82  ? 112 LEU A CG  1 
ATOM   838   C CD1 . LEU A 1 108 ? 43.627  -44.365 -29.644  1.00 60.49  ? 112 LEU A CD1 1 
ATOM   839   C CD2 . LEU A 1 108 ? 45.343  -42.613 -29.190  1.00 62.36  ? 112 LEU A CD2 1 
ATOM   840   N N   . SER A 1 109 ? 42.874  -39.664 -33.223  1.00 62.64  ? 113 SER A N   1 
ATOM   841   C CA  . SER A 1 109 ? 42.859  -39.356 -34.650  1.00 71.59  ? 113 SER A CA  1 
ATOM   842   C C   . SER A 1 109 ? 44.132  -38.633 -35.080  1.00 69.76  ? 113 SER A C   1 
ATOM   843   O O   . SER A 1 109 ? 44.727  -38.971 -36.108  1.00 62.99  ? 113 SER A O   1 
ATOM   844   C CB  . SER A 1 109 ? 41.625  -38.519 -34.986  1.00 53.54  ? 113 SER A CB  1 
ATOM   845   O OG  . SER A 1 109 ? 41.609  -37.315 -34.239  1.00 75.20  ? 113 SER A OG  1 
ATOM   846   N N   . ARG A 1 110 ? 44.574  -37.648 -34.300  1.00 71.92  ? 114 ARG A N   1 
ATOM   847   C CA  . ARG A 1 110 ? 45.820  -36.934 -34.564  1.00 63.44  ? 114 ARG A CA  1 
ATOM   848   C C   . ARG A 1 110 ? 46.657  -36.942 -33.292  1.00 72.56  ? 114 ARG A C   1 
ATOM   849   O O   . ARG A 1 110 ? 46.278  -36.325 -32.290  1.00 75.33  ? 114 ARG A O   1 
ATOM   850   C CB  . ARG A 1 110 ? 45.551  -35.505 -35.038  1.00 73.48  ? 114 ARG A CB  1 
ATOM   851   C CG  . ARG A 1 110 ? 46.778  -34.607 -35.002  1.00 76.33  ? 114 ARG A CG  1 
ATOM   852   C CD  . ARG A 1 110 ? 46.689  -33.478 -36.016  1.00 88.11  ? 114 ARG A CD  1 
ATOM   853   N NE  . ARG A 1 110 ? 47.773  -32.519 -35.840  1.00 122.45 ? 114 ARG A NE  1 
ATOM   854   C CZ  . ARG A 1 110 ? 47.605  -31.257 -35.471  1.00 119.69 ? 114 ARG A CZ  1 
ATOM   855   N NH1 . ARG A 1 110 ? 46.399  -30.742 -35.296  1.00 96.72  ? 114 ARG A NH1 1 
ATOM   856   N NH2 . ARG A 1 110 ? 48.675  -30.489 -35.281  1.00 88.74  ? 114 ARG A NH2 1 
ATOM   857   N N   . ILE A 1 111 ? 47.791  -37.636 -33.332  1.00 60.69  ? 115 ILE A N   1 
ATOM   858   C CA  . ILE A 1 111 ? 48.658  -37.813 -32.173  1.00 69.80  ? 115 ILE A CA  1 
ATOM   859   C C   . ILE A 1 111 ? 50.048  -37.306 -32.524  1.00 65.04  ? 115 ILE A C   1 
ATOM   860   O O   . ILE A 1 111 ? 50.627  -37.713 -33.538  1.00 77.51  ? 115 ILE A O   1 
ATOM   861   C CB  . ILE A 1 111 ? 48.702  -39.283 -31.723  1.00 76.49  ? 115 ILE A CB  1 
ATOM   862   C CG1 . ILE A 1 111 ? 47.475  -39.609 -30.870  1.00 76.72  ? 115 ILE A CG1 1 
ATOM   863   C CG2 . ILE A 1 111 ? 49.986  -39.584 -30.969  1.00 67.43  ? 115 ILE A CG2 1 
ATOM   864   C CD1 . ILE A 1 111 ? 47.312  -38.697 -29.670  1.00 78.66  ? 115 ILE A CD1 1 
ATOM   865   N N   . ASN A 1 112 ? 50.578  -36.411 -31.688  1.00 71.97  ? 116 ASN A N   1 
ATOM   866   C CA  . ASN A 1 112 ? 51.900  -35.850 -31.947  1.00 65.70  ? 116 ASN A CA  1 
ATOM   867   C C   . ASN A 1 112 ? 53.007  -36.845 -31.612  1.00 75.55  ? 116 ASN A C   1 
ATOM   868   O O   . ASN A 1 112 ? 53.992  -36.953 -32.352  1.00 90.91  ? 116 ASN A O   1 
ATOM   869   C CB  . ASN A 1 112 ? 52.076  -34.547 -31.165  1.00 74.25  ? 116 ASN A CB  1 
ATOM   870   C CG  . ASN A 1 112 ? 53.399  -33.871 -31.449  1.00 99.24  ? 116 ASN A CG  1 
ATOM   871   O OD1 . ASN A 1 112 ? 54.049  -33.356 -30.543  1.00 105.02 ? 116 ASN A OD1 1 
ATOM   872   N ND2 . ASN A 1 112 ? 53.808  -33.875 -32.715  1.00 103.73 ? 116 ASN A ND2 1 
ATOM   873   N N   . HIS A 1 113 ? 52.870  -37.575 -30.507  1.00 81.77  ? 117 HIS A N   1 
ATOM   874   C CA  . HIS A 1 113 ? 53.873  -38.546 -30.096  1.00 81.00  ? 117 HIS A CA  1 
ATOM   875   C C   . HIS A 1 113 ? 53.188  -39.778 -29.525  1.00 80.97  ? 117 HIS A C   1 
ATOM   876   O O   . HIS A 1 113 ? 52.255  -39.664 -28.726  1.00 72.89  ? 117 HIS A O   1 
ATOM   877   C CB  . HIS A 1 113 ? 54.834  -37.954 -29.060  1.00 79.10  ? 117 HIS A CB  1 
ATOM   878   C CG  . HIS A 1 113 ? 56.120  -38.708 -28.931  1.00 95.71  ? 117 HIS A CG  1 
ATOM   879   N ND1 . HIS A 1 113 ? 56.237  -39.860 -28.186  1.00 97.46  ? 117 HIS A ND1 1 
ATOM   880   C CD2 . HIS A 1 113 ? 57.347  -38.472 -29.455  1.00 106.43 ? 117 HIS A CD2 1 
ATOM   881   C CE1 . HIS A 1 113 ? 57.480  -40.303 -28.255  1.00 112.70 ? 117 HIS A CE1 1 
ATOM   882   N NE2 . HIS A 1 113 ? 58.174  -39.479 -29.019  1.00 118.55 ? 117 HIS A NE2 1 
ATOM   883   N N   . PHE A 1 114 ? 53.667  -40.954 -29.927  1.00 68.82  ? 118 PHE A N   1 
ATOM   884   C CA  . PHE A 1 114 ? 53.047  -42.221 -29.554  1.00 63.00  ? 118 PHE A CA  1 
ATOM   885   C C   . PHE A 1 114 ? 54.145  -43.243 -29.315  1.00 77.43  ? 118 PHE A C   1 
ATOM   886   O O   . PHE A 1 114 ? 54.932  -43.529 -30.222  1.00 92.33  ? 118 PHE A O   1 
ATOM   887   C CB  . PHE A 1 114 ? 52.095  -42.701 -30.653  1.00 73.29  ? 118 PHE A CB  1 
ATOM   888   C CG  . PHE A 1 114 ? 51.204  -43.835 -30.239  1.00 76.89  ? 118 PHE A CG  1 
ATOM   889   C CD1 . PHE A 1 114 ? 49.966  -43.587 -29.674  1.00 70.11  ? 118 PHE A CD1 1 
ATOM   890   C CD2 . PHE A 1 114 ? 51.598  -45.149 -30.431  1.00 77.24  ? 118 PHE A CD2 1 
ATOM   891   C CE1 . PHE A 1 114 ? 49.137  -44.626 -29.297  1.00 67.60  ? 118 PHE A CE1 1 
ATOM   892   C CE2 . PHE A 1 114 ? 50.775  -46.194 -30.057  1.00 71.88  ? 118 PHE A CE2 1 
ATOM   893   C CZ  . PHE A 1 114 ? 49.542  -45.931 -29.490  1.00 73.17  ? 118 PHE A CZ  1 
ATOM   894   N N   . GLU A 1 115 ? 54.200  -43.791 -28.103  1.00 57.56  ? 119 GLU A N   1 
ATOM   895   C CA  . GLU A 1 115 ? 55.175  -44.830 -27.796  1.00 65.97  ? 119 GLU A CA  1 
ATOM   896   C C   . GLU A 1 115 ? 54.570  -45.820 -26.814  1.00 61.99  ? 119 GLU A C   1 
ATOM   897   O O   . GLU A 1 115 ? 54.081  -45.426 -25.751  1.00 63.44  ? 119 GLU A O   1 
ATOM   898   C CB  . GLU A 1 115 ? 56.466  -44.239 -27.225  1.00 66.27  ? 119 GLU A CB  1 
ATOM   899   C CG  . GLU A 1 115 ? 57.687  -45.098 -27.515  1.00 86.23  ? 119 GLU A CG  1 
ATOM   900   C CD  . GLU A 1 115 ? 58.799  -44.917 -26.503  1.00 102.62 ? 119 GLU A CD  1 
ATOM   901   O OE1 . GLU A 1 115 ? 58.742  -43.952 -25.712  1.00 106.73 ? 119 GLU A OE1 1 
ATOM   902   O OE2 . GLU A 1 115 ? 59.731  -45.750 -26.497  1.00 100.82 ? 119 GLU A OE2 1 
ATOM   903   N N   . LYS A 1 116 ? 54.608  -47.099 -27.176  1.00 53.01  ? 120 LYS A N   1 
ATOM   904   C CA  . LYS A 1 116 ? 54.137  -48.161 -26.297  1.00 51.40  ? 120 LYS A CA  1 
ATOM   905   C C   . LYS A 1 116 ? 55.228  -48.530 -25.300  1.00 59.54  ? 120 LYS A C   1 
ATOM   906   O O   . LYS A 1 116 ? 56.372  -48.790 -25.688  1.00 62.79  ? 120 LYS A O   1 
ATOM   907   C CB  . LYS A 1 116 ? 53.728  -49.379 -27.123  1.00 51.79  ? 120 LYS A CB  1 
ATOM   908   C CG  . LYS A 1 116 ? 53.570  -50.669 -26.335  1.00 58.35  ? 120 LYS A CG  1 
ATOM   909   C CD  . LYS A 1 116 ? 52.898  -51.735 -27.190  1.00 45.40  ? 120 LYS A CD  1 
ATOM   910   C CE  . LYS A 1 116 ? 53.482  -53.115 -26.938  1.00 65.11  ? 120 LYS A CE  1 
ATOM   911   N NZ  . LYS A 1 116 ? 52.744  -54.165 -27.694  1.00 71.32  ? 120 LYS A NZ  1 
ATOM   912   N N   . ILE A 1 117 ? 54.876  -48.552 -24.014  1.00 60.57  ? 121 ILE A N   1 
ATOM   913   C CA  . ILE A 1 117 ? 55.825  -48.863 -22.954  1.00 58.31  ? 121 ILE A CA  1 
ATOM   914   C C   . ILE A 1 117 ? 55.228  -49.921 -22.037  1.00 54.80  ? 121 ILE A C   1 
ATOM   915   O O   . ILE A 1 117 ? 54.009  -50.086 -21.941  1.00 68.14  ? 121 ILE A O   1 
ATOM   916   C CB  . ILE A 1 117 ? 56.230  -47.620 -22.131  1.00 55.24  ? 121 ILE A CB  1 
ATOM   917   C CG1 . ILE A 1 117 ? 55.056  -47.126 -21.284  1.00 62.16  ? 121 ILE A CG1 1 
ATOM   918   C CG2 . ILE A 1 117 ? 56.749  -46.520 -23.044  1.00 65.55  ? 121 ILE A CG2 1 
ATOM   919   C CD1 . ILE A 1 117 ? 55.445  -46.081 -20.257  1.00 53.68  ? 121 ILE A CD1 1 
ATOM   920   N N   . LEU A 1 118 ? 56.118  -50.637 -21.355  1.00 60.33  ? 122 LEU A N   1 
ATOM   921   C CA  . LEU A 1 118 ? 55.741  -51.661 -20.393  1.00 63.11  ? 122 LEU A CA  1 
ATOM   922   C C   . LEU A 1 118 ? 55.680  -51.038 -19.004  1.00 63.24  ? 122 LEU A C   1 
ATOM   923   O O   . LEU A 1 118 ? 56.674  -50.481 -18.527  1.00 68.43  ? 122 LEU A O   1 
ATOM   924   C CB  . LEU A 1 118 ? 56.746  -52.812 -20.428  1.00 55.85  ? 122 LEU A CB  1 
ATOM   925   C CG  . LEU A 1 118 ? 56.642  -53.901 -19.358  1.00 56.47  ? 122 LEU A CG  1 
ATOM   926   C CD1 . LEU A 1 118 ? 55.324  -54.634 -19.466  1.00 60.81  ? 122 LEU A CD1 1 
ATOM   927   C CD2 . LEU A 1 118 ? 57.805  -54.873 -19.465  1.00 78.92  ? 122 LEU A CD2 1 
ATOM   928   N N   . ILE A 1 119 ? 54.517  -51.124 -18.359  1.00 59.77  ? 123 ILE A N   1 
ATOM   929   C CA  . ILE A 1 119 ? 54.324  -50.506 -17.058  1.00 50.53  ? 123 ILE A CA  1 
ATOM   930   C C   . ILE A 1 119 ? 54.125  -51.529 -15.942  1.00 62.92  ? 123 ILE A C   1 
ATOM   931   O O   . ILE A 1 119 ? 54.504  -51.255 -14.798  1.00 54.64  ? 123 ILE A O   1 
ATOM   932   C CB  . ILE A 1 119 ? 53.150  -49.504 -17.092  1.00 65.70  ? 123 ILE A CB  1 
ATOM   933   C CG1 . ILE A 1 119 ? 51.838  -50.222 -17.414  1.00 62.66  ? 123 ILE A CG1 1 
ATOM   934   C CG2 . ILE A 1 119 ? 53.419  -48.401 -18.105  1.00 53.56  ? 123 ILE A CG2 1 
ATOM   935   C CD1 . ILE A 1 119 ? 50.611  -49.372 -17.177  1.00 39.47  ? 123 ILE A CD1 1 
ATOM   936   N N   . ILE A 1 120 ? 53.547  -52.690 -16.232  1.00 59.49  ? 124 ILE A N   1 
ATOM   937   C CA  . ILE A 1 120 ? 53.370  -53.735 -15.226  1.00 52.55  ? 124 ILE A CA  1 
ATOM   938   C C   . ILE A 1 120 ? 53.753  -55.078 -15.838  1.00 57.92  ? 124 ILE A C   1 
ATOM   939   O O   . ILE A 1 120 ? 52.967  -55.661 -16.597  1.00 60.16  ? 124 ILE A O   1 
ATOM   940   C CB  . ILE A 1 120 ? 51.933  -53.758 -14.677  1.00 65.90  ? 124 ILE A CB  1 
ATOM   941   C CG1 . ILE A 1 120 ? 51.639  -52.490 -13.870  1.00 56.43  ? 124 ILE A CG1 1 
ATOM   942   C CG2 . ILE A 1 120 ? 51.717  -54.978 -13.797  1.00 69.26  ? 124 ILE A CG2 1 
ATOM   943   C CD1 . ILE A 1 120 ? 50.266  -52.475 -13.223  1.00 67.43  ? 124 ILE A CD1 1 
ATOM   944   N N   . PRO A 1 121 ? 54.948  -55.592 -15.554  1.00 59.54  ? 125 PRO A N   1 
ATOM   945   C CA  . PRO A 1 121 ? 55.328  -56.911 -16.069  1.00 49.50  ? 125 PRO A CA  1 
ATOM   946   C C   . PRO A 1 121 ? 54.550  -58.020 -15.379  1.00 55.35  ? 125 PRO A C   1 
ATOM   947   O O   . PRO A 1 121 ? 53.996  -57.849 -14.291  1.00 58.18  ? 125 PRO A O   1 
ATOM   948   C CB  . PRO A 1 121 ? 56.824  -57.000 -15.751  1.00 58.11  ? 125 PRO A CB  1 
ATOM   949   C CG  . PRO A 1 121 ? 57.008  -56.089 -14.581  1.00 47.81  ? 125 PRO A CG  1 
ATOM   950   C CD  . PRO A 1 121 ? 56.028  -54.966 -14.771  1.00 54.89  ? 125 PRO A CD  1 
ATOM   951   N N   . LYS A 1 122 A 54.512  -59.181 -16.042  1.00 62.20  ? 125 LYS A N   1 
ATOM   952   C CA  . LYS A 1 122 A 53.800  -60.331 -15.495  1.00 61.13  ? 125 LYS A CA  1 
ATOM   953   C C   . LYS A 1 122 A 54.400  -60.816 -14.181  1.00 59.86  ? 125 LYS A C   1 
ATOM   954   O O   . LYS A 1 122 A 53.732  -61.544 -13.439  1.00 67.29  ? 125 LYS A O   1 
ATOM   955   C CB  . LYS A 1 122 A 53.787  -61.479 -16.507  1.00 63.47  ? 125 LYS A CB  1 
ATOM   956   C CG  . LYS A 1 122 A 52.918  -61.236 -17.730  1.00 63.69  ? 125 LYS A CG  1 
ATOM   957   C CD  . LYS A 1 122 A 52.658  -62.536 -18.476  1.00 70.95  ? 125 LYS A CD  1 
ATOM   958   C CE  . LYS A 1 122 A 51.792  -62.311 -19.706  1.00 80.18  ? 125 LYS A CE  1 
ATOM   959   N NZ  . LYS A 1 122 A 51.370  -63.602 -20.321  1.00 67.33  ? 125 LYS A NZ  1 
ATOM   960   N N   . SER A 1 123 B 55.642  -60.434 -13.880  1.00 55.65  ? 125 SER A N   1 
ATOM   961   C CA  . SER A 1 123 B 56.247  -60.792 -12.602  1.00 71.61  ? 125 SER A CA  1 
ATOM   962   C C   . SER A 1 123 B 55.532  -60.147 -11.423  1.00 62.82  ? 125 SER A C   1 
ATOM   963   O O   . SER A 1 123 B 55.701  -60.600 -10.286  1.00 76.29  ? 125 SER A O   1 
ATOM   964   C CB  . SER A 1 123 B 57.723  -60.395 -12.597  1.00 65.32  ? 125 SER A CB  1 
ATOM   965   O OG  . SER A 1 123 B 57.896  -59.066 -13.059  1.00 71.80  ? 125 SER A OG  1 
ATOM   966   N N   . SER A 1 124 ? 54.735  -59.105 -11.667  1.00 68.33  ? 126 SER A N   1 
ATOM   967   C CA  . SER A 1 124 ? 54.058  -58.381 -10.600  1.00 58.04  ? 126 SER A CA  1 
ATOM   968   C C   . SER A 1 124 ? 52.931  -59.178 -9.956   1.00 62.86  ? 126 SER A C   1 
ATOM   969   O O   . SER A 1 124 ? 52.384  -58.729 -8.943   1.00 62.87  ? 126 SER A O   1 
ATOM   970   C CB  . SER A 1 124 ? 53.509  -57.058 -11.137  1.00 60.64  ? 126 SER A CB  1 
ATOM   971   O OG  . SER A 1 124 ? 54.530  -56.297 -11.759  1.00 61.53  ? 126 SER A OG  1 
ATOM   972   N N   . TRP A 1 125 ? 52.564  -60.333 -10.514  1.00 73.55  ? 127 TRP A N   1 
ATOM   973   C CA  . TRP A 1 125 ? 51.486  -61.169 -9.990   1.00 79.57  ? 127 TRP A CA  1 
ATOM   974   C C   . TRP A 1 125 ? 52.061  -62.520 -9.571   1.00 84.24  ? 127 TRP A C   1 
ATOM   975   O O   . TRP A 1 125 ? 51.855  -63.534 -10.251  1.00 81.03  ? 127 TRP A O   1 
ATOM   976   C CB  . TRP A 1 125 ? 50.378  -61.350 -11.025  1.00 72.72  ? 127 TRP A CB  1 
ATOM   977   C CG  . TRP A 1 125 ? 50.192  -60.161 -11.914  1.00 64.86  ? 127 TRP A CG  1 
ATOM   978   C CD1 . TRP A 1 125 ? 50.653  -60.011 -13.189  1.00 65.74  ? 127 TRP A CD1 1 
ATOM   979   C CD2 . TRP A 1 125 ? 49.501  -58.949 -11.593  1.00 63.72  ? 127 TRP A CD2 1 
ATOM   980   N NE1 . TRP A 1 125 ? 50.288  -58.782 -13.683  1.00 52.95  ? 127 TRP A NE1 1 
ATOM   981   C CE2 . TRP A 1 125 ? 49.580  -58.110 -12.722  1.00 54.09  ? 127 TRP A CE2 1 
ATOM   982   C CE3 . TRP A 1 125 ? 48.822  -58.491 -10.460  1.00 46.83  ? 127 TRP A CE3 1 
ATOM   983   C CZ2 . TRP A 1 125 ? 49.005  -56.842 -12.752  1.00 49.49  ? 127 TRP A CZ2 1 
ATOM   984   C CZ3 . TRP A 1 125 ? 48.253  -57.232 -10.492  1.00 55.27  ? 127 TRP A CZ3 1 
ATOM   985   C CH2 . TRP A 1 125 ? 48.347  -56.423 -11.630  1.00 58.09  ? 127 TRP A CH2 1 
ATOM   986   N N   . PRO A 1 126 ? 52.786  -62.569 -8.449   1.00 91.42  ? 128 PRO A N   1 
ATOM   987   C CA  . PRO A 1 126 ? 53.420  -63.835 -8.048   1.00 88.01  ? 128 PRO A CA  1 
ATOM   988   C C   . PRO A 1 126 ? 52.445  -64.861 -7.500   1.00 91.38  ? 128 PRO A C   1 
ATOM   989   O O   . PRO A 1 126 ? 52.767  -66.055 -7.503   1.00 75.15  ? 128 PRO A O   1 
ATOM   990   C CB  . PRO A 1 126 ? 54.422  -63.394 -6.975   1.00 80.13  ? 128 PRO A CB  1 
ATOM   991   C CG  . PRO A 1 126 ? 53.776  -62.202 -6.357   1.00 82.37  ? 128 PRO A CG  1 
ATOM   992   C CD  . PRO A 1 126 ? 53.032  -61.497 -7.468   1.00 81.48  ? 128 PRO A CD  1 
ATOM   993   N N   . ASN A 1 127 ? 51.272  -64.440 -7.027   1.00 78.13  ? 129 ASN A N   1 
ATOM   994   C CA  . ASN A 1 127 ? 50.303  -65.347 -6.426   1.00 72.68  ? 129 ASN A CA  1 
ATOM   995   C C   . ASN A 1 127 ? 49.084  -65.580 -7.311   1.00 79.18  ? 129 ASN A C   1 
ATOM   996   O O   . ASN A 1 127 ? 48.094  -66.156 -6.848   1.00 70.69  ? 129 ASN A O   1 
ATOM   997   C CB  . ASN A 1 127 ? 49.872  -64.822 -5.055   1.00 74.30  ? 129 ASN A CB  1 
ATOM   998   C CG  . ASN A 1 127 ? 50.970  -64.943 -4.014   1.00 90.01  ? 129 ASN A CG  1 
ATOM   999   O OD1 . ASN A 1 127 ? 51.159  -66.003 -3.415   1.00 82.33  ? 129 ASN A OD1 1 
ATOM   1000  N ND2 . ASN A 1 127 ? 51.701  -63.857 -3.794   1.00 82.23  ? 129 ASN A ND2 1 
ATOM   1001  N N   . HIS A 1 128 ? 49.129  -65.146 -8.568   1.00 73.25  ? 130 HIS A N   1 
ATOM   1002  C CA  . HIS A 1 128 ? 48.067  -65.407 -9.527   1.00 61.62  ? 130 HIS A CA  1 
ATOM   1003  C C   . HIS A 1 128 ? 48.674  -66.009 -10.785  1.00 59.40  ? 130 HIS A C   1 
ATOM   1004  O O   . HIS A 1 128 ? 49.861  -65.830 -11.072  1.00 76.33  ? 130 HIS A O   1 
ATOM   1005  C CB  . HIS A 1 128 ? 47.286  -64.131 -9.880   1.00 50.33  ? 130 HIS A CB  1 
ATOM   1006  C CG  . HIS A 1 128 ? 46.779  -63.379 -8.689   1.00 58.83  ? 130 HIS A CG  1 
ATOM   1007  N ND1 . HIS A 1 128 ? 47.599  -62.613 -7.889   1.00 77.29  ? 130 HIS A ND1 1 
ATOM   1008  C CD2 . HIS A 1 128 ? 45.535  -63.273 -8.163   1.00 63.07  ? 130 HIS A CD2 1 
ATOM   1009  C CE1 . HIS A 1 128 ? 46.884  -62.069 -6.920   1.00 69.16  ? 130 HIS A CE1 1 
ATOM   1010  N NE2 . HIS A 1 128 ? 45.628  -62.453 -7.064   1.00 66.73  ? 130 HIS A NE2 1 
ATOM   1011  N N   . GLU A 1 129 ? 47.849  -66.736 -11.535  1.00 70.00  ? 131 GLU A N   1 
ATOM   1012  C CA  . GLU A 1 129 ? 48.295  -67.320 -12.792  1.00 50.39  ? 131 GLU A CA  1 
ATOM   1013  C C   . GLU A 1 129 ? 48.256  -66.274 -13.897  1.00 51.16  ? 131 GLU A C   1 
ATOM   1014  O O   . GLU A 1 129 ? 47.247  -65.585 -14.078  1.00 62.63  ? 131 GLU A O   1 
ATOM   1015  C CB  . GLU A 1 129 ? 47.432  -68.525 -13.164  1.00 62.39  ? 131 GLU A CB  1 
ATOM   1016  C CG  . GLU A 1 129 ? 47.894  -69.816 -12.516  1.00 78.70  ? 131 GLU A CG  1 
ATOM   1017  C CD  . GLU A 1 129 ? 49.342  -70.137 -12.839  1.00 103.29 ? 131 GLU A CD  1 
ATOM   1018  O OE1 . GLU A 1 129 ? 49.759  -69.911 -13.996  1.00 103.82 ? 131 GLU A OE1 1 
ATOM   1019  O OE2 . GLU A 1 129 ? 50.064  -70.609 -11.935  1.00 105.90 ? 131 GLU A OE2 1 
ATOM   1020  N N   . THR A 1 130 ? 49.358  -66.156 -14.635  1.00 61.40  ? 132 THR A N   1 
ATOM   1021  C CA  . THR A 1 130 ? 49.498  -65.152 -15.680  1.00 55.34  ? 132 THR A CA  1 
ATOM   1022  C C   . THR A 1 130 ? 49.564  -65.748 -17.079  1.00 64.06  ? 132 THR A C   1 
ATOM   1023  O O   . THR A 1 130 ? 49.606  -64.991 -18.056  1.00 79.67  ? 132 THR A O   1 
ATOM   1024  C CB  . THR A 1 130 ? 50.750  -64.302 -15.432  1.00 68.17  ? 132 THR A CB  1 
ATOM   1025  O OG1 . THR A 1 130 ? 51.920  -65.110 -15.610  1.00 70.31  ? 132 THR A OG1 1 
ATOM   1026  C CG2 . THR A 1 130 ? 50.742  -63.742 -14.018  1.00 65.42  ? 132 THR A CG2 1 
ATOM   1027  N N   . SER A 1 131 ? 49.577  -67.075 -17.208  1.00 53.79  ? 133 SER A N   1 
ATOM   1028  C CA  . SER A 1 131 ? 49.720  -67.720 -18.505  1.00 78.30  ? 133 SER A CA  1 
ATOM   1029  C C   . SER A 1 131 ? 48.492  -68.503 -18.942  1.00 66.34  ? 133 SER A C   1 
ATOM   1030  O O   . SER A 1 131 ? 48.457  -68.974 -20.085  1.00 75.99  ? 133 SER A O   1 
ATOM   1031  C CB  . SER A 1 131 ? 50.934  -68.661 -18.501  1.00 72.77  ? 133 SER A CB  1 
ATOM   1032  O OG  . SER A 1 131 ? 50.775  -69.693 -17.544  1.00 92.39  ? 133 SER A OG  1 
ATOM   1033  N N   . LEU A 1 132 A 47.492  -68.660 -18.080  1.00 67.97  ? 133 LEU A N   1 
ATOM   1034  C CA  . LEU A 1 132 A 46.272  -69.370 -18.438  1.00 62.89  ? 133 LEU A CA  1 
ATOM   1035  C C   . LEU A 1 132 A 45.181  -68.453 -18.976  1.00 69.19  ? 133 LEU A C   1 
ATOM   1036  O O   . LEU A 1 132 A 44.119  -68.946 -19.366  1.00 54.01  ? 133 LEU A O   1 
ATOM   1037  C CB  . LEU A 1 132 A 45.737  -70.144 -17.228  1.00 57.92  ? 133 LEU A CB  1 
ATOM   1038  C CG  . LEU A 1 132 A 46.670  -71.176 -16.590  1.00 74.87  ? 133 LEU A CG  1 
ATOM   1039  C CD1 . LEU A 1 132 A 45.969  -71.891 -15.442  1.00 52.30  ? 133 LEU A CD1 1 
ATOM   1040  C CD2 . LEU A 1 132 A 47.169  -72.174 -17.623  1.00 55.96  ? 133 LEU A CD2 1 
ATOM   1041  N N   . GLY A 1 133 ? 45.417  -67.144 -19.026  1.00 82.34  ? 134 GLY A N   1 
ATOM   1042  C CA  . GLY A 1 133 ? 44.415  -66.209 -19.503  1.00 66.22  ? 134 GLY A CA  1 
ATOM   1043  C C   . GLY A 1 133 ? 44.273  -66.277 -21.007  1.00 63.07  ? 134 GLY A C   1 
ATOM   1044  O O   . GLY A 1 133 ? 44.706  -65.378 -21.733  1.00 64.30  ? 134 GLY A O   1 
ATOM   1045  N N   . VAL A 1 134 ? 43.657  -67.358 -21.478  1.00 62.14  ? 135 VAL A N   1 
ATOM   1046  C CA  . VAL A 1 134 ? 43.722  -67.772 -22.873  1.00 55.96  ? 135 VAL A CA  1 
ATOM   1047  C C   . VAL A 1 134 ? 42.329  -68.186 -23.334  1.00 72.27  ? 135 VAL A C   1 
ATOM   1048  O O   . VAL A 1 134 ? 41.557  -68.770 -22.566  1.00 73.55  ? 135 VAL A O   1 
ATOM   1049  C CB  . VAL A 1 134 ? 44.754  -68.909 -23.029  1.00 59.93  ? 135 VAL A CB  1 
ATOM   1050  C CG1 . VAL A 1 134 ? 44.397  -69.845 -24.151  1.00 64.85  ? 135 VAL A CG1 1 
ATOM   1051  C CG2 . VAL A 1 134 ? 46.149  -68.335 -23.232  1.00 61.67  ? 135 VAL A CG2 1 
ATOM   1052  N N   . SER A 1 135 ? 42.002  -67.878 -24.590  1.00 51.95  ? 136 SER A N   1 
ATOM   1053  C CA  . SER A 1 135 ? 40.666  -68.140 -25.109  1.00 58.72  ? 136 SER A CA  1 
ATOM   1054  C C   . SER A 1 135 ? 40.729  -68.445 -26.599  1.00 65.07  ? 136 SER A C   1 
ATOM   1055  O O   . SER A 1 135 ? 41.599  -67.942 -27.318  1.00 62.50  ? 136 SER A O   1 
ATOM   1056  C CB  . SER A 1 135 ? 39.730  -66.953 -24.858  1.00 67.10  ? 136 SER A CB  1 
ATOM   1057  O OG  . SER A 1 135 ? 38.528  -67.105 -25.585  1.00 62.41  ? 136 SER A OG  1 
ATOM   1058  N N   . ALA A 1 136 ? 39.783  -69.274 -27.053  1.00 63.27  ? 137 ALA A N   1 
ATOM   1059  C CA  . ALA A 1 136 ? 39.681  -69.626 -28.465  1.00 56.83  ? 137 ALA A CA  1 
ATOM   1060  C C   . ALA A 1 136 ? 39.084  -68.509 -29.311  1.00 57.17  ? 137 ALA A C   1 
ATOM   1061  O O   . ALA A 1 136 ? 39.251  -68.523 -30.536  1.00 64.35  ? 137 ALA A O   1 
ATOM   1062  C CB  . ALA A 1 136 ? 38.844  -70.896 -28.634  1.00 39.56  ? 137 ALA A CB  1 
ATOM   1063  N N   . ALA A 1 137 ? 38.387  -67.550 -28.696  1.00 70.26  ? 138 ALA A N   1 
ATOM   1064  C CA  . ALA A 1 137 ? 37.896  -66.400 -29.446  1.00 63.47  ? 138 ALA A CA  1 
ATOM   1065  C C   . ALA A 1 137 ? 39.023  -65.485 -29.894  1.00 67.87  ? 138 ALA A C   1 
ATOM   1066  O O   . ALA A 1 137 ? 38.808  -64.646 -30.773  1.00 56.10  ? 138 ALA A O   1 
ATOM   1067  C CB  . ALA A 1 137 ? 36.893  -65.604 -28.613  1.00 55.24  ? 138 ALA A CB  1 
ATOM   1068  N N   . CYS A 1 138 ? 40.219  -65.640 -29.327  1.00 71.16  ? 139 CYS A N   1 
ATOM   1069  C CA  . CYS A 1 138 ? 41.382  -64.829 -29.673  1.00 72.91  ? 139 CYS A CA  1 
ATOM   1070  C C   . CYS A 1 138 ? 42.519  -65.758 -30.088  1.00 73.31  ? 139 CYS A C   1 
ATOM   1071  O O   . CYS A 1 138 ? 43.512  -65.902 -29.364  1.00 69.32  ? 139 CYS A O   1 
ATOM   1072  C CB  . CYS A 1 138 ? 41.806  -63.943 -28.503  1.00 59.66  ? 139 CYS A CB  1 
ATOM   1073  S SG  . CYS A 1 138 ? 40.584  -62.710 -28.014  1.00 85.48  ? 139 CYS A SG  1 
ATOM   1074  N N   . PRO A 1 139 ? 42.405  -66.403 -31.245  1.00 73.45  ? 140 PRO A N   1 
ATOM   1075  C CA  . PRO A 1 139 ? 43.457  -67.323 -31.680  1.00 68.60  ? 140 PRO A CA  1 
ATOM   1076  C C   . PRO A 1 139 ? 44.679  -66.575 -32.192  1.00 68.41  ? 140 PRO A C   1 
ATOM   1077  O O   . PRO A 1 139 ? 44.610  -65.421 -32.618  1.00 70.64  ? 140 PRO A O   1 
ATOM   1078  C CB  . PRO A 1 139 ? 42.784  -68.114 -32.804  1.00 69.85  ? 140 PRO A CB  1 
ATOM   1079  C CG  . PRO A 1 139 ? 41.826  -67.142 -33.392  1.00 62.98  ? 140 PRO A CG  1 
ATOM   1080  C CD  . PRO A 1 139 ? 41.329  -66.291 -32.246  1.00 61.72  ? 140 PRO A CD  1 
ATOM   1081  N N   . TYR A 1 140 ? 45.818  -67.263 -32.139  1.00 63.79  ? 141 TYR A N   1 
ATOM   1082  C CA  . TYR A 1 140 ? 47.073  -66.741 -32.665  1.00 84.77  ? 141 TYR A CA  1 
ATOM   1083  C C   . TYR A 1 140 ? 47.526  -67.474 -33.917  1.00 99.69  ? 141 TYR A C   1 
ATOM   1084  O O   . TYR A 1 140 ? 47.819  -66.840 -34.934  1.00 107.76 ? 141 TYR A O   1 
ATOM   1085  C CB  . TYR A 1 140 ? 48.168  -66.809 -31.590  1.00 83.91  ? 141 TYR A CB  1 
ATOM   1086  C CG  . TYR A 1 140 ? 49.540  -66.419 -32.092  1.00 94.60  ? 141 TYR A CG  1 
ATOM   1087  C CD1 . TYR A 1 140 ? 49.725  -65.256 -32.832  1.00 77.78  ? 141 TYR A CD1 1 
ATOM   1088  C CD2 . TYR A 1 140 ? 50.651  -67.207 -31.818  1.00 85.73  ? 141 TYR A CD2 1 
ATOM   1089  C CE1 . TYR A 1 140 ? 50.977  -64.896 -33.294  1.00 82.69  ? 141 TYR A CE1 1 
ATOM   1090  C CE2 . TYR A 1 140 ? 51.907  -66.853 -32.273  1.00 82.48  ? 141 TYR A CE2 1 
ATOM   1091  C CZ  . TYR A 1 140 ? 52.064  -65.696 -33.010  1.00 89.21  ? 141 TYR A CZ  1 
ATOM   1092  O OH  . TYR A 1 140 ? 53.312  -65.338 -33.467  1.00 78.05  ? 141 TYR A OH  1 
ATOM   1093  N N   . GLN A 1 141 ? 47.599  -68.801 -33.868  1.00 82.68  ? 142 GLN A N   1 
ATOM   1094  C CA  . GLN A 1 141 ? 47.880  -69.638 -35.032  1.00 78.24  ? 142 GLN A CA  1 
ATOM   1095  C C   . GLN A 1 141 ? 46.927  -70.824 -35.054  1.00 71.95  ? 142 GLN A C   1 
ATOM   1096  O O   . GLN A 1 141 ? 47.316  -71.977 -35.245  1.00 67.04  ? 142 GLN A O   1 
ATOM   1097  C CB  . GLN A 1 141 ? 49.336  -70.098 -35.035  1.00 84.61  ? 142 GLN A CB  1 
ATOM   1098  C CG  . GLN A 1 141 ? 50.338  -68.969 -35.238  1.00 77.35  ? 142 GLN A CG  1 
ATOM   1099  C CD  . GLN A 1 141 ? 51.780  -69.445 -35.213  1.00 93.63  ? 142 GLN A CD  1 
ATOM   1100  O OE1 . GLN A 1 141 ? 52.256  -69.973 -34.207  1.00 98.09  ? 142 GLN A OE1 1 
ATOM   1101  N NE2 . GLN A 1 141 ? 52.483  -69.259 -36.325  1.00 101.04 ? 142 GLN A NE2 1 
ATOM   1102  N N   . GLY A 1 142 ? 45.645  -70.540 -34.838  1.00 77.61  ? 143 GLY A N   1 
ATOM   1103  C CA  . GLY A 1 142 ? 44.667  -71.571 -34.569  1.00 68.45  ? 143 GLY A CA  1 
ATOM   1104  C C   . GLY A 1 142 ? 44.654  -72.051 -33.138  1.00 62.35  ? 143 GLY A C   1 
ATOM   1105  O O   . GLY A 1 142 ? 43.732  -72.782 -32.748  1.00 77.73  ? 143 GLY A O   1 
ATOM   1106  N N   . THR A 1 143 ? 45.633  -71.663 -32.342  1.00 75.19  ? 144 THR A N   1 
ATOM   1107  C CA  . THR A 1 143 ? 45.840  -71.978 -30.934  1.00 74.40  ? 144 THR A CA  1 
ATOM   1108  C C   . THR A 1 143 ? 45.201  -70.898 -30.065  1.00 63.91  ? 144 THR A C   1 
ATOM   1109  O O   . THR A 1 143 ? 45.337  -69.708 -30.370  1.00 65.89  ? 144 THR A O   1 
ATOM   1110  C CB  . THR A 1 143 ? 47.328  -72.078 -30.626  1.00 67.86  ? 144 THR A CB  1 
ATOM   1111  O OG1 . THR A 1 143 ? 47.897  -73.185 -31.339  1.00 77.64  ? 144 THR A OG1 1 
ATOM   1112  C CG2 . THR A 1 143 ? 47.573  -72.265 -29.133  1.00 51.76  ? 144 THR A CG2 1 
ATOM   1113  N N   . PRO A 1 144 ? 44.490  -71.264 -28.999  1.00 53.83  ? 145 PRO A N   1 
ATOM   1114  C CA  . PRO A 1 144 ? 43.881  -70.239 -28.145  1.00 60.80  ? 145 PRO A CA  1 
ATOM   1115  C C   . PRO A 1 144 ? 44.936  -69.312 -27.555  1.00 57.49  ? 145 PRO A C   1 
ATOM   1116  O O   . PRO A 1 144 ? 46.001  -69.751 -27.117  1.00 66.71  ? 145 PRO A O   1 
ATOM   1117  C CB  . PRO A 1 144 ? 43.164  -71.054 -27.064  1.00 48.81  ? 145 PRO A CB  1 
ATOM   1118  C CG  . PRO A 1 144 ? 42.932  -72.390 -27.672  1.00 58.31  ? 145 PRO A CG  1 
ATOM   1119  C CD  . PRO A 1 144 ? 44.100  -72.624 -28.591  1.00 67.86  ? 145 PRO A CD  1 
ATOM   1120  N N   . SER A 1 145 ? 44.622  -68.021 -27.542  1.00 69.75  ? 146 SER A N   1 
ATOM   1121  C CA  . SER A 1 145 ? 45.548  -66.979 -27.106  1.00 66.06  ? 146 SER A CA  1 
ATOM   1122  C C   . SER A 1 145 ? 44.723  -65.840 -26.511  1.00 61.81  ? 146 SER A C   1 
ATOM   1123  O O   . SER A 1 145 ? 43.560  -66.030 -26.140  1.00 57.75  ? 146 SER A O   1 
ATOM   1124  C CB  . SER A 1 145 ? 46.446  -66.539 -28.277  1.00 70.68  ? 146 SER A CB  1 
ATOM   1125  O OG  . SER A 1 145 ? 47.420  -65.599 -27.858  1.00 69.11  ? 146 SER A OG  1 
ATOM   1126  N N   . PHE A 1 146 ? 45.323  -64.656 -26.401  1.00 46.98  ? 147 PHE A N   1 
ATOM   1127  C CA  . PHE A 1 146 ? 44.637  -63.520 -25.797  1.00 54.18  ? 147 PHE A CA  1 
ATOM   1128  C C   . PHE A 1 146 ? 45.294  -62.231 -26.274  1.00 52.50  ? 147 PHE A C   1 
ATOM   1129  O O   . PHE A 1 146 ? 46.311  -62.249 -26.972  1.00 58.50  ? 147 PHE A O   1 
ATOM   1130  C CB  . PHE A 1 146 ? 44.657  -63.614 -24.268  1.00 59.75  ? 147 PHE A CB  1 
ATOM   1131  C CG  . PHE A 1 146 ? 43.665  -62.713 -23.586  1.00 64.73  ? 147 PHE A CG  1 
ATOM   1132  C CD1 . PHE A 1 146 ? 42.306  -62.952 -23.695  1.00 50.94  ? 147 PHE A CD1 1 
ATOM   1133  C CD2 . PHE A 1 146 ? 44.094  -61.633 -22.833  1.00 50.45  ? 147 PHE A CD2 1 
ATOM   1134  C CE1 . PHE A 1 146 ? 41.392  -62.128 -23.068  1.00 56.14  ? 147 PHE A CE1 1 
ATOM   1135  C CE2 . PHE A 1 146 ? 43.183  -60.806 -22.204  1.00 53.12  ? 147 PHE A CE2 1 
ATOM   1136  C CZ  . PHE A 1 146 ? 41.831  -61.054 -22.322  1.00 60.78  ? 147 PHE A CZ  1 
ATOM   1137  N N   . PHE A 1 147 ? 44.684  -61.107 -25.895  1.00 60.74  ? 148 PHE A N   1 
ATOM   1138  C CA  . PHE A 1 147 ? 45.273  -59.802 -26.168  1.00 57.87  ? 148 PHE A CA  1 
ATOM   1139  C C   . PHE A 1 147 ? 46.664  -59.715 -25.552  1.00 46.73  ? 148 PHE A C   1 
ATOM   1140  O O   . PHE A 1 147 ? 46.900  -60.188 -24.437  1.00 65.60  ? 148 PHE A O   1 
ATOM   1141  C CB  . PHE A 1 147 ? 44.386  -58.685 -25.614  1.00 57.89  ? 148 PHE A CB  1 
ATOM   1142  C CG  . PHE A 1 147 ? 42.983  -58.682 -26.160  1.00 57.73  ? 148 PHE A CG  1 
ATOM   1143  C CD1 . PHE A 1 147 ? 42.710  -58.154 -27.411  1.00 60.89  ? 148 PHE A CD1 1 
ATOM   1144  C CD2 . PHE A 1 147 ? 41.933  -59.183 -25.406  1.00 64.82  ? 148 PHE A CD2 1 
ATOM   1145  C CE1 . PHE A 1 147 ? 41.418  -58.142 -27.908  1.00 72.52  ? 148 PHE A CE1 1 
ATOM   1146  C CE2 . PHE A 1 147 ? 40.639  -59.173 -25.896  1.00 52.23  ? 148 PHE A CE2 1 
ATOM   1147  C CZ  . PHE A 1 147 ? 40.381  -58.652 -27.148  1.00 65.59  ? 148 PHE A CZ  1 
ATOM   1148  N N   . ARG A 1 148 ? 47.591  -59.107 -26.290  1.00 48.08  ? 149 ARG A N   1 
ATOM   1149  C CA  . ARG A 1 148 ? 48.995  -59.098 -25.896  1.00 54.82  ? 149 ARG A CA  1 
ATOM   1150  C C   . ARG A 1 148 ? 49.345  -57.977 -24.925  1.00 53.82  ? 149 ARG A C   1 
ATOM   1151  O O   . ARG A 1 148 ? 50.232  -58.157 -24.084  1.00 57.21  ? 149 ARG A O   1 
ATOM   1152  C CB  . ARG A 1 148 ? 49.881  -59.000 -27.140  1.00 43.10  ? 149 ARG A CB  1 
ATOM   1153  C CG  . ARG A 1 148 ? 49.842  -60.243 -28.018  1.00 47.39  ? 149 ARG A CG  1 
ATOM   1154  C CD  . ARG A 1 148 ? 50.940  -61.221 -27.630  1.00 71.24  ? 149 ARG A CD  1 
ATOM   1155  N NE  . ARG A 1 148 ? 50.524  -62.612 -27.767  1.00 58.90  ? 149 ARG A NE  1 
ATOM   1156  C CZ  . ARG A 1 148 ? 50.571  -63.305 -28.897  1.00 75.46  ? 149 ARG A CZ  1 
ATOM   1157  N NH1 . ARG A 1 148 ? 50.987  -62.759 -30.029  1.00 71.93  ? 149 ARG A NH1 1 
ATOM   1158  N NH2 . ARG A 1 148 ? 50.190  -64.580 -28.892  1.00 72.68  ? 149 ARG A NH2 1 
ATOM   1159  N N   . ASN A 1 149 ? 48.670  -56.833 -25.011  1.00 54.67  ? 150 ASN A N   1 
ATOM   1160  C CA  . ASN A 1 149 ? 48.976  -55.687 -24.163  1.00 56.48  ? 150 ASN A CA  1 
ATOM   1161  C C   . ASN A 1 149 ? 48.280  -55.743 -22.809  1.00 51.53  ? 150 ASN A C   1 
ATOM   1162  O O   . ASN A 1 149 ? 48.491  -54.850 -21.983  1.00 50.70  ? 150 ASN A O   1 
ATOM   1163  C CB  . ASN A 1 149 ? 48.593  -54.386 -24.877  1.00 59.26  ? 150 ASN A CB  1 
ATOM   1164  C CG  . ASN A 1 149 ? 49.307  -54.218 -26.201  1.00 62.13  ? 150 ASN A CG  1 
ATOM   1165  O OD1 . ASN A 1 149 ? 50.499  -54.501 -26.319  1.00 64.16  ? 150 ASN A OD1 1 
ATOM   1166  N ND2 . ASN A 1 149 ? 48.578  -53.757 -27.209  1.00 65.30  ? 150 ASN A ND2 1 
ATOM   1167  N N   . VAL A 1 150 ? 47.469  -56.768 -22.561  1.00 58.81  ? 151 VAL A N   1 
ATOM   1168  C CA  . VAL A 1 150 ? 46.687  -56.882 -21.337  1.00 52.60  ? 151 VAL A CA  1 
ATOM   1169  C C   . VAL A 1 150 ? 46.720  -58.338 -20.889  1.00 43.54  ? 151 VAL A C   1 
ATOM   1170  O O   . VAL A 1 150 ? 46.870  -59.253 -21.705  1.00 64.22  ? 151 VAL A O   1 
ATOM   1171  C CB  . VAL A 1 150 ? 45.242  -56.371 -21.552  1.00 46.02  ? 151 VAL A CB  1 
ATOM   1172  C CG1 . VAL A 1 150 ? 44.363  -57.447 -22.178  1.00 56.97  ? 151 VAL A CG1 1 
ATOM   1173  C CG2 . VAL A 1 150 ? 44.644  -55.839 -20.262  1.00 59.31  ? 151 VAL A CG2 1 
ATOM   1174  N N   . VAL A 1 151 ? 46.595  -58.555 -19.581  1.00 47.81  ? 152 VAL A N   1 
ATOM   1175  C CA  . VAL A 1 151 ? 46.798  -59.870 -18.980  1.00 41.31  ? 152 VAL A CA  1 
ATOM   1176  C C   . VAL A 1 151 ? 45.527  -60.295 -18.257  1.00 47.09  ? 152 VAL A C   1 
ATOM   1177  O O   . VAL A 1 151 ? 44.963  -59.525 -17.471  1.00 58.73  ? 152 VAL A O   1 
ATOM   1178  C CB  . VAL A 1 151 ? 48.000  -59.874 -18.016  1.00 46.33  ? 152 VAL A CB  1 
ATOM   1179  C CG1 . VAL A 1 151 ? 48.167  -61.247 -17.382  1.00 43.01  ? 152 VAL A CG1 1 
ATOM   1180  C CG2 . VAL A 1 151 ? 49.265  -59.475 -18.754  1.00 63.12  ? 152 VAL A CG2 1 
ATOM   1181  N N   . TRP A 1 152 ? 45.089  -61.526 -18.522  1.00 47.15  ? 153 TRP A N   1 
ATOM   1182  C CA  . TRP A 1 152 ? 43.908  -62.122 -17.896  1.00 44.36  ? 153 TRP A CA  1 
ATOM   1183  C C   . TRP A 1 152 ? 44.386  -63.000 -16.743  1.00 56.68  ? 153 TRP A C   1 
ATOM   1184  O O   . TRP A 1 152 ? 44.826  -64.133 -16.952  1.00 58.81  ? 153 TRP A O   1 
ATOM   1185  C CB  . TRP A 1 152 ? 43.114  -62.917 -18.927  1.00 56.70  ? 153 TRP A CB  1 
ATOM   1186  C CG  . TRP A 1 152 ? 41.815  -63.496 -18.443  1.00 57.80  ? 153 TRP A CG  1 
ATOM   1187  C CD1 . TRP A 1 152 ? 41.259  -63.361 -17.203  1.00 51.74  ? 153 TRP A CD1 1 
ATOM   1188  C CD2 . TRP A 1 152 ? 40.909  -64.304 -19.203  1.00 60.84  ? 153 TRP A CD2 1 
ATOM   1189  N NE1 . TRP A 1 152 ? 40.062  -64.035 -17.146  1.00 47.56  ? 153 TRP A NE1 1 
ATOM   1190  C CE2 . TRP A 1 152 ? 39.825  -64.622 -18.361  1.00 51.77  ? 153 TRP A CE2 1 
ATOM   1191  C CE3 . TRP A 1 152 ? 40.911  -64.789 -20.515  1.00 49.68  ? 153 TRP A CE3 1 
ATOM   1192  C CZ2 . TRP A 1 152 ? 38.753  -65.403 -18.789  1.00 56.03  ? 153 TRP A CZ2 1 
ATOM   1193  C CZ3 . TRP A 1 152 ? 39.845  -65.563 -20.937  1.00 61.09  ? 153 TRP A CZ3 1 
ATOM   1194  C CH2 . TRP A 1 152 ? 38.781  -65.863 -20.077  1.00 51.10  ? 153 TRP A CH2 1 
ATOM   1195  N N   . LEU A 1 153 ? 44.293  -62.475 -15.523  1.00 62.55  ? 154 LEU A N   1 
ATOM   1196  C CA  . LEU A 1 153 ? 44.796  -63.175 -14.349  1.00 50.68  ? 154 LEU A CA  1 
ATOM   1197  C C   . LEU A 1 153 ? 43.796  -64.222 -13.869  1.00 52.41  ? 154 LEU A C   1 
ATOM   1198  O O   . LEU A 1 153 ? 42.586  -63.981 -13.840  1.00 57.83  ? 154 LEU A O   1 
ATOM   1199  C CB  . LEU A 1 153 ? 45.095  -62.179 -13.229  1.00 47.75  ? 154 LEU A CB  1 
ATOM   1200  C CG  . LEU A 1 153 ? 46.111  -61.082 -13.563  1.00 41.35  ? 154 LEU A CG  1 
ATOM   1201  C CD1 . LEU A 1 153 ? 46.142  -60.031 -12.468  1.00 53.79  ? 154 LEU A CD1 1 
ATOM   1202  C CD2 . LEU A 1 153 ? 47.498  -61.670 -13.782  1.00 47.97  ? 154 LEU A CD2 1 
ATOM   1203  N N   . ILE A 1 154 ? 44.317  -65.390 -13.486  1.00 53.25  ? 155 ILE A N   1 
ATOM   1204  C CA  . ILE A 1 154 ? 43.513  -66.526 -13.055  1.00 49.57  ? 155 ILE A CA  1 
ATOM   1205  C C   . ILE A 1 154 ? 44.038  -66.998 -11.703  1.00 58.65  ? 155 ILE A C   1 
ATOM   1206  O O   . ILE A 1 154 ? 45.186  -66.743 -11.333  1.00 70.25  ? 155 ILE A O   1 
ATOM   1207  C CB  . ILE A 1 154 ? 43.537  -67.673 -14.098  1.00 53.92  ? 155 ILE A CB  1 
ATOM   1208  C CG1 . ILE A 1 154 ? 43.122  -67.149 -15.474  1.00 57.95  ? 155 ILE A CG1 1 
ATOM   1209  C CG2 . ILE A 1 154 ? 42.601  -68.813 -13.716  1.00 46.85  ? 155 ILE A CG2 1 
ATOM   1210  C CD1 . ILE A 1 154 ? 41.685  -66.669 -15.534  1.00 64.59  ? 155 ILE A CD1 1 
ATOM   1211  N N   . LYS A 1 155 ? 43.170  -67.683 -10.956  1.00 49.23  ? 156 LYS A N   1 
ATOM   1212  C CA  . LYS A 1 155 ? 43.527  -68.178 -9.633   1.00 54.56  ? 156 LYS A CA  1 
ATOM   1213  C C   . LYS A 1 155 ? 44.693  -69.159 -9.710   1.00 60.20  ? 156 LYS A C   1 
ATOM   1214  O O   . LYS A 1 155 ? 44.878  -69.866 -10.704  1.00 71.34  ? 156 LYS A O   1 
ATOM   1215  C CB  . LYS A 1 155 ? 42.323  -68.862 -8.979   1.00 56.04  ? 156 LYS A CB  1 
ATOM   1216  C CG  . LYS A 1 155 ? 41.925  -70.176 -9.643   1.00 55.46  ? 156 LYS A CG  1 
ATOM   1217  C CD  . LYS A 1 155 ? 40.796  -70.872 -8.900   1.00 66.56  ? 156 LYS A CD  1 
ATOM   1218  C CE  . LYS A 1 155 ? 40.503  -72.240 -9.503   1.00 49.19  ? 156 LYS A CE  1 
ATOM   1219  N NZ  . LYS A 1 155 ? 39.428  -72.962 -8.764   1.00 67.12  ? 156 LYS A NZ  1 
ATOM   1220  N N   . LYS A 1 156 ? 45.494  -69.184 -8.646   1.00 68.78  ? 157 LYS A N   1 
ATOM   1221  C CA  . LYS A 1 156 ? 46.565  -70.158 -8.483   1.00 70.50  ? 157 LYS A CA  1 
ATOM   1222  C C   . LYS A 1 156 ? 46.363  -70.890 -7.165   1.00 72.58  ? 157 LYS A C   1 
ATOM   1223  O O   . LYS A 1 156 ? 46.076  -70.260 -6.142   1.00 79.67  ? 157 LYS A O   1 
ATOM   1224  C CB  . LYS A 1 156 ? 47.945  -69.492 -8.512   1.00 52.09  ? 157 LYS A CB  1 
ATOM   1225  C CG  . LYS A 1 156 ? 49.097  -70.490 -8.446   1.00 67.21  ? 157 LYS A CG  1 
ATOM   1226  C CD  . LYS A 1 156 ? 50.352  -69.881 -7.837   1.00 67.70  ? 157 LYS A CD  1 
ATOM   1227  C CE  . LYS A 1 156 ? 51.113  -69.019 -8.828   1.00 73.34  ? 157 LYS A CE  1 
ATOM   1228  N NZ  . LYS A 1 156 ? 52.380  -68.506 -8.232   1.00 77.51  ? 157 LYS A NZ  1 
ATOM   1229  N N   . ASN A 1 157 ? 46.517  -72.216 -7.196   1.00 63.42  ? 158 ASN A N   1 
ATOM   1230  C CA  . ASN A 1 157 ? 46.343  -73.065 -6.015   1.00 63.61  ? 158 ASN A CA  1 
ATOM   1231  C C   . ASN A 1 157 ? 44.960  -72.881 -5.395   1.00 68.90  ? 158 ASN A C   1 
ATOM   1232  O O   . ASN A 1 157 ? 44.810  -72.828 -4.172   1.00 68.45  ? 158 ASN A O   1 
ATOM   1233  C CB  . ASN A 1 157 ? 47.443  -72.809 -4.980   1.00 62.13  ? 158 ASN A CB  1 
ATOM   1234  C CG  . ASN A 1 157 ? 48.798  -73.325 -5.430   1.00 72.38  ? 158 ASN A CG  1 
ATOM   1235  O OD1 . ASN A 1 157 ? 49.694  -72.547 -5.761   1.00 67.53  ? 158 ASN A OD1 1 
ATOM   1236  N ND2 . ASN A 1 157 ? 48.954  -74.644 -5.443   1.00 74.98  ? 158 ASN A ND2 1 
ATOM   1237  N N   . ASP A 1 158 ? 43.942  -72.781 -6.253   1.00 72.75  ? 159 ASP A N   1 
ATOM   1238  C CA  . ASP A 1 158 ? 42.548  -72.628 -5.829   1.00 73.18  ? 159 ASP A CA  1 
ATOM   1239  C C   . ASP A 1 158 ? 42.378  -71.423 -4.906   1.00 66.24  ? 159 ASP A C   1 
ATOM   1240  O O   . ASP A 1 158 ? 41.635  -71.466 -3.924   1.00 68.49  ? 159 ASP A O   1 
ATOM   1241  C CB  . ASP A 1 158 ? 42.030  -73.905 -5.163   1.00 61.87  ? 159 ASP A CB  1 
ATOM   1242  C CG  . ASP A 1 158 ? 40.515  -73.995 -5.171   1.00 83.15  ? 159 ASP A CG  1 
ATOM   1243  O OD1 . ASP A 1 158 ? 39.921  -74.009 -6.271   1.00 89.88  ? 159 ASP A OD1 1 
ATOM   1244  O OD2 . ASP A 1 158 ? 39.916  -74.059 -4.077   1.00 82.29  ? 159 ASP A OD2 1 
ATOM   1245  N N   . ALA A 1 159 ? 43.081  -70.338 -5.222   1.00 67.09  ? 160 ALA A N   1 
ATOM   1246  C CA  . ALA A 1 159 ? 43.006  -69.118 -4.435   1.00 68.31  ? 160 ALA A CA  1 
ATOM   1247  C C   . ALA A 1 159 ? 43.255  -67.924 -5.343   1.00 73.78  ? 160 ALA A C   1 
ATOM   1248  O O   . ALA A 1 159 ? 44.080  -67.991 -6.258   1.00 62.10  ? 160 ALA A O   1 
ATOM   1249  C CB  . ALA A 1 159 ? 44.018  -69.130 -3.284   1.00 58.99  ? 160 ALA A CB  1 
ATOM   1250  N N   . TYR A 1 160 ? 42.532  -66.836 -5.085   1.00 63.14  ? 161 TYR A N   1 
ATOM   1251  C CA  . TYR A 1 160 ? 42.706  -65.570 -5.795   1.00 72.45  ? 161 TYR A CA  1 
ATOM   1252  C C   . TYR A 1 160 ? 42.869  -64.489 -4.739   1.00 51.33  ? 161 TYR A C   1 
ATOM   1253  O O   . TYR A 1 160 ? 41.898  -63.813 -4.372   1.00 62.91  ? 161 TYR A O   1 
ATOM   1254  C CB  . TYR A 1 160 ? 41.524  -65.273 -6.719   1.00 57.87  ? 161 TYR A CB  1 
ATOM   1255  C CG  . TYR A 1 160 ? 41.783  -64.198 -7.756   1.00 52.77  ? 161 TYR A CG  1 
ATOM   1256  C CD1 . TYR A 1 160 ? 41.928  -62.866 -7.390   1.00 62.25  ? 161 TYR A CD1 1 
ATOM   1257  C CD2 . TYR A 1 160 ? 41.863  -64.516 -9.105   1.00 56.58  ? 161 TYR A CD2 1 
ATOM   1258  C CE1 . TYR A 1 160 ? 42.160  -61.884 -8.335   1.00 56.76  ? 161 TYR A CE1 1 
ATOM   1259  C CE2 . TYR A 1 160 ? 42.092  -63.538 -10.057  1.00 49.73  ? 161 TYR A CE2 1 
ATOM   1260  C CZ  . TYR A 1 160 ? 42.239  -62.225 -9.666   1.00 41.36  ? 161 TYR A CZ  1 
ATOM   1261  O OH  . TYR A 1 160 ? 42.467  -61.251 -10.611  1.00 58.52  ? 161 TYR A OH  1 
ATOM   1262  N N   . PRO A 1 161 ? 44.079  -64.317 -4.207   1.00 61.76  ? 162 PRO A N   1 
ATOM   1263  C CA  . PRO A 1 161 ? 44.296  -63.269 -3.205   1.00 58.68  ? 162 PRO A CA  1 
ATOM   1264  C C   . PRO A 1 161 ? 44.011  -61.889 -3.776   1.00 54.29  ? 162 PRO A C   1 
ATOM   1265  O O   . PRO A 1 161 ? 44.197  -61.635 -4.968   1.00 56.67  ? 162 PRO A O   1 
ATOM   1266  C CB  . PRO A 1 161 ? 45.775  -63.430 -2.834   1.00 46.35  ? 162 PRO A CB  1 
ATOM   1267  C CG  . PRO A 1 161 ? 46.381  -64.200 -3.970   1.00 62.23  ? 162 PRO A CG  1 
ATOM   1268  C CD  . PRO A 1 161 ? 45.295  -65.108 -4.454   1.00 73.88  ? 162 PRO A CD  1 
ATOM   1269  N N   . THR A 1 162 ? 43.536  -60.999 -2.904   1.00 64.76  ? 163 THR A N   1 
ATOM   1270  C CA  . THR A 1 162 ? 43.151  -59.659 -3.330   1.00 55.27  ? 163 THR A CA  1 
ATOM   1271  C C   . THR A 1 162 ? 44.351  -58.917 -3.905   1.00 50.03  ? 163 THR A C   1 
ATOM   1272  O O   . THR A 1 162 ? 45.437  -58.913 -3.318   1.00 64.20  ? 163 THR A O   1 
ATOM   1273  C CB  . THR A 1 162 ? 42.558  -58.879 -2.154   1.00 58.31  ? 163 THR A CB  1 
ATOM   1274  O OG1 . THR A 1 162 ? 41.365  -59.530 -1.700   1.00 56.14  ? 163 THR A OG1 1 
ATOM   1275  C CG2 . THR A 1 162 ? 42.220  -57.451 -2.566   1.00 52.31  ? 163 THR A CG2 1 
ATOM   1276  N N   . ILE A 1 163 ? 44.148  -58.293 -5.057   1.00 61.79  ? 164 ILE A N   1 
ATOM   1277  C CA  . ILE A 1 163 ? 45.190  -57.534 -5.735   1.00 50.80  ? 164 ILE A CA  1 
ATOM   1278  C C   . ILE A 1 163 ? 45.098  -56.081 -5.296   1.00 52.73  ? 164 ILE A C   1 
ATOM   1279  O O   . ILE A 1 163 ? 44.008  -55.501 -5.269   1.00 57.51  ? 164 ILE A O   1 
ATOM   1280  C CB  . ILE A 1 163 ? 45.050  -57.660 -7.261   1.00 60.86  ? 164 ILE A CB  1 
ATOM   1281  C CG1 . ILE A 1 163 ? 45.361  -59.090 -7.704   1.00 46.70  ? 164 ILE A CG1 1 
ATOM   1282  C CG2 . ILE A 1 163 ? 45.941  -56.648 -7.968   1.00 59.10  ? 164 ILE A CG2 1 
ATOM   1283  C CD1 . ILE A 1 163 ? 44.806  -59.441 -9.067   1.00 68.56  ? 164 ILE A CD1 1 
ATOM   1284  N N   . LYS A 1 164 ? 46.240  -55.493 -4.935   1.00 47.74  ? 165 LYS A N   1 
ATOM   1285  C CA  . LYS A 1 164 ? 46.316  -54.074 -4.579   1.00 52.52  ? 165 LYS A CA  1 
ATOM   1286  C C   . LYS A 1 164 ? 47.634  -53.545 -5.144   1.00 50.70  ? 165 LYS A C   1 
ATOM   1287  O O   . LYS A 1 164 ? 48.685  -53.654 -4.506   1.00 67.37  ? 165 LYS A O   1 
ATOM   1288  C CB  . LYS A 1 164 ? 46.218  -53.867 -3.072   1.00 70.79  ? 165 LYS A CB  1 
ATOM   1289  C CG  . LYS A 1 164 ? 45.907  -52.434 -2.667   1.00 76.39  ? 165 LYS A CG  1 
ATOM   1290  C CD  . LYS A 1 164 ? 45.913  -52.267 -1.156   1.00 80.65  ? 165 LYS A CD  1 
ATOM   1291  C CE  . LYS A 1 164 ? 47.289  -52.551 -0.576   1.00 93.51  ? 165 LYS A CE  1 
ATOM   1292  N NZ  . LYS A 1 164 ? 47.355  -52.226 0.875    1.00 89.48  ? 165 LYS A NZ  1 
ATOM   1293  N N   . ILE A 1 165 ? 47.569  -52.971 -6.342   1.00 49.97  ? 166 ILE A N   1 
ATOM   1294  C CA  . ILE A 1 165 ? 48.755  -52.497 -7.039   1.00 48.47  ? 166 ILE A CA  1 
ATOM   1295  C C   . ILE A 1 165 ? 48.554  -51.042 -7.437   1.00 47.83  ? 166 ILE A C   1 
ATOM   1296  O O   . ILE A 1 165 ? 47.426  -50.575 -7.623   1.00 57.46  ? 166 ILE A O   1 
ATOM   1297  C CB  . ILE A 1 165 ? 49.080  -53.370 -8.275   1.00 49.39  ? 166 ILE A CB  1 
ATOM   1298  C CG1 . ILE A 1 165 ? 50.504  -53.098 -8.769   1.00 56.09  ? 166 ILE A CG1 1 
ATOM   1299  C CG2 . ILE A 1 165 ? 48.062  -53.135 -9.386   1.00 51.68  ? 166 ILE A CG2 1 
ATOM   1300  C CD1 . ILE A 1 165 ? 51.140  -54.268 -9.491   1.00 67.50  ? 166 ILE A CD1 1 
ATOM   1301  N N   . SER A 1 166 ? 49.665  -50.320 -7.549   1.00 54.61  ? 167 SER A N   1 
ATOM   1302  C CA  . SER A 1 166 ? 49.669  -48.931 -7.974   1.00 53.13  ? 167 SER A CA  1 
ATOM   1303  C C   . SER A 1 166 ? 50.756  -48.723 -9.016   1.00 43.28  ? 167 SER A C   1 
ATOM   1304  O O   . SER A 1 166 ? 51.798  -49.383 -8.990   1.00 57.03  ? 167 SER A O   1 
ATOM   1305  C CB  . SER A 1 166 ? 49.898  -47.983 -6.788   1.00 50.37  ? 167 SER A CB  1 
ATOM   1306  O OG  . SER A 1 166 ? 50.184  -46.667 -7.230   1.00 79.36  ? 167 SER A OG  1 
ATOM   1307  N N   . TYR A 1 167 ? 50.502  -47.800 -9.940   1.00 47.23  ? 168 TYR A N   1 
ATOM   1308  C CA  . TYR A 1 167 ? 51.514  -47.350 -10.884  1.00 36.29  ? 168 TYR A CA  1 
ATOM   1309  C C   . TYR A 1 167 ? 51.500  -45.832 -10.931  1.00 45.02  ? 168 TYR A C   1 
ATOM   1310  O O   . TYR A 1 167 ? 50.435  -45.220 -11.055  1.00 61.53  ? 168 TYR A O   1 
ATOM   1311  C CB  . TYR A 1 167 ? 51.291  -47.918 -12.289  1.00 42.96  ? 168 TYR A CB  1 
ATOM   1312  C CG  . TYR A 1 167 ? 52.274  -47.373 -13.301  1.00 54.66  ? 168 TYR A CG  1 
ATOM   1313  C CD1 . TYR A 1 167 ? 53.554  -47.901 -13.409  1.00 51.12  ? 168 TYR A CD1 1 
ATOM   1314  C CD2 . TYR A 1 167 ? 51.928  -46.320 -14.136  1.00 51.49  ? 168 TYR A CD2 1 
ATOM   1315  C CE1 . TYR A 1 167 ? 54.459  -47.400 -14.325  1.00 35.97  ? 168 TYR A CE1 1 
ATOM   1316  C CE2 . TYR A 1 167 ? 52.824  -45.812 -15.053  1.00 55.40  ? 168 TYR A CE2 1 
ATOM   1317  C CZ  . TYR A 1 167 ? 54.088  -46.355 -15.145  1.00 72.23  ? 168 TYR A CZ  1 
ATOM   1318  O OH  . TYR A 1 167 ? 54.984  -45.851 -16.061  1.00 55.35  ? 168 TYR A OH  1 
ATOM   1319  N N   . ASN A 1 168 ? 52.683  -45.234 -10.846  1.00 59.16  ? 169 ASN A N   1 
ATOM   1320  C CA  . ASN A 1 168 ? 52.852  -43.788 -10.871  1.00 58.80  ? 169 ASN A CA  1 
ATOM   1321  C C   . ASN A 1 168 ? 53.498  -43.380 -12.187  1.00 51.08  ? 169 ASN A C   1 
ATOM   1322  O O   . ASN A 1 168 ? 54.487  -43.988 -12.611  1.00 59.69  ? 169 ASN A O   1 
ATOM   1323  C CB  . ASN A 1 168 ? 53.708  -43.326 -9.692   1.00 51.33  ? 169 ASN A CB  1 
ATOM   1324  C CG  . ASN A 1 168 ? 53.991  -41.847 -9.730   1.00 61.01  ? 169 ASN A CG  1 
ATOM   1325  O OD1 . ASN A 1 168 ? 53.128  -41.043 -10.087  1.00 65.39  ? 169 ASN A OD1 1 
ATOM   1326  N ND2 . ASN A 1 168 ? 55.209  -41.475 -9.368   1.00 70.40  ? 169 ASN A ND2 1 
ATOM   1327  N N   . ASN A 1 169 ? 52.946  -42.350 -12.826  1.00 54.80  ? 170 ASN A N   1 
ATOM   1328  C CA  . ASN A 1 169 ? 53.413  -41.910 -14.141  1.00 57.63  ? 170 ASN A CA  1 
ATOM   1329  C C   . ASN A 1 169 ? 54.678  -41.077 -13.970  1.00 58.78  ? 170 ASN A C   1 
ATOM   1330  O O   . ASN A 1 169 ? 54.621  -39.900 -13.604  1.00 58.86  ? 170 ASN A O   1 
ATOM   1331  C CB  . ASN A 1 169 ? 52.324  -41.123 -14.863  1.00 49.54  ? 170 ASN A CB  1 
ATOM   1332  C CG  . ASN A 1 169 ? 52.716  -40.750 -16.281  1.00 61.11  ? 170 ASN A CG  1 
ATOM   1333  O OD1 . ASN A 1 169 ? 53.710  -41.243 -16.814  1.00 54.70  ? 170 ASN A OD1 1 
ATOM   1334  N ND2 . ASN A 1 169 ? 51.929  -39.880 -16.904  1.00 63.81  ? 170 ASN A ND2 1 
ATOM   1335  N N   . THR A 1 170 ? 55.830  -41.692 -14.244  1.00 73.72  ? 171 THR A N   1 
ATOM   1336  C CA  . THR A 1 170 ? 57.127  -41.031 -14.186  1.00 66.27  ? 171 THR A CA  1 
ATOM   1337  C C   . THR A 1 170 ? 57.685  -40.729 -15.572  1.00 74.53  ? 171 THR A C   1 
ATOM   1338  O O   . THR A 1 170 ? 58.906  -40.598 -15.730  1.00 83.19  ? 171 THR A O   1 
ATOM   1339  C CB  . THR A 1 170 ? 58.122  -41.887 -13.396  1.00 69.36  ? 171 THR A CB  1 
ATOM   1340  O OG1 . THR A 1 170 ? 58.440  -43.067 -14.145  1.00 72.10  ? 171 THR A OG1 1 
ATOM   1341  C CG2 . THR A 1 170 ? 57.534  -42.300 -12.054  1.00 55.70  ? 171 THR A CG2 1 
ATOM   1342  N N   . ASN A 1 171 ? 56.817  -40.610 -16.576  1.00 70.32  ? 172 ASN A N   1 
ATOM   1343  C CA  . ASN A 1 171 ? 57.229  -40.567 -17.975  1.00 61.13  ? 172 ASN A CA  1 
ATOM   1344  C C   . ASN A 1 171 ? 57.185  -39.177 -18.596  1.00 79.34  ? 172 ASN A C   1 
ATOM   1345  O O   . ASN A 1 171 ? 57.558  -39.035 -19.764  1.00 85.24  ? 172 ASN A O   1 
ATOM   1346  C CB  . ASN A 1 171 ? 56.356  -41.522 -18.803  1.00 53.08  ? 172 ASN A CB  1 
ATOM   1347  C CG  . ASN A 1 171 ? 56.497  -42.974 -18.366  1.00 67.77  ? 172 ASN A CG  1 
ATOM   1348  O OD1 . ASN A 1 171 ? 57.302  -43.724 -18.917  1.00 83.18  ? 172 ASN A OD1 1 
ATOM   1349  N ND2 . ASN A 1 171 ? 55.704  -43.376 -17.377  1.00 68.17  ? 172 ASN A ND2 1 
ATOM   1350  N N   . ARG A 1 172 ? 56.741  -38.159 -17.854  1.00 74.73  ? 173 ARG A N   1 
ATOM   1351  C CA  . ARG A 1 172 ? 56.734  -36.774 -18.317  1.00 81.58  ? 173 ARG A CA  1 
ATOM   1352  C C   . ARG A 1 172 ? 55.752  -36.563 -19.463  1.00 81.87  ? 173 ARG A C   1 
ATOM   1353  O O   . ARG A 1 172 ? 55.566  -35.428 -19.920  1.00 83.87  ? 173 ARG A O   1 
ATOM   1354  C CB  . ARG A 1 172 ? 58.142  -36.354 -18.763  1.00 67.34  ? 173 ARG A CB  1 
ATOM   1355  C CG  . ARG A 1 172 ? 59.048  -35.906 -17.632  1.00 84.61  ? 173 ARG A CG  1 
ATOM   1356  C CD  . ARG A 1 172 ? 60.290  -35.214 -18.147  1.00 99.96  ? 173 ARG A CD  1 
ATOM   1357  N NE  . ARG A 1 172 ? 61.500  -35.962 -17.833  1.00 121.90 ? 173 ARG A NE  1 
ATOM   1358  C CZ  . ARG A 1 172 ? 62.114  -35.924 -16.659  1.00 131.60 ? 173 ARG A CZ  1 
ATOM   1359  N NH1 . ARG A 1 172 ? 61.645  -35.197 -15.659  1.00 120.82 ? 173 ARG A NH1 1 
ATOM   1360  N NH2 . ARG A 1 172 ? 63.222  -36.638 -16.483  1.00 121.10 ? 173 ARG A NH2 1 
ATOM   1361  N N   . GLU A 1 173 ? 55.059  -37.622 -19.876  1.00 78.38  ? 174 GLU A N   1 
ATOM   1362  C CA  . GLU A 1 173 ? 54.050  -37.541 -20.922  1.00 66.31  ? 174 GLU A CA  1 
ATOM   1363  C C   . GLU A 1 173 ? 52.788  -38.244 -20.448  1.00 64.18  ? 174 GLU A C   1 
ATOM   1364  O O   . GLU A 1 173 ? 52.830  -39.105 -19.566  1.00 70.45  ? 174 GLU A O   1 
ATOM   1365  C CB  . GLU A 1 173 ? 54.537  -38.159 -22.245  1.00 57.83  ? 174 GLU A CB  1 
ATOM   1366  C CG  . GLU A 1 173 ? 55.787  -37.509 -22.832  1.00 84.17  ? 174 GLU A CG  1 
ATOM   1367  C CD  . GLU A 1 173 ? 56.173  -38.103 -24.175  1.00 93.62  ? 174 GLU A CD  1 
ATOM   1368  O OE1 . GLU A 1 173 ? 55.360  -38.867 -24.735  1.00 93.37  ? 174 GLU A OE1 1 
ATOM   1369  O OE2 . GLU A 1 173 ? 57.283  -37.812 -24.671  1.00 102.37 ? 174 GLU A OE2 1 
ATOM   1370  N N   . ASP A 1 174 ? 51.657  -37.857 -21.036  1.00 62.84  ? 175 ASP A N   1 
ATOM   1371  C CA  . ASP A 1 174 ? 50.397  -38.509 -20.715  1.00 57.03  ? 175 ASP A CA  1 
ATOM   1372  C C   . ASP A 1 174 ? 50.450  -39.982 -21.097  1.00 58.13  ? 175 ASP A C   1 
ATOM   1373  O O   . ASP A 1 174 ? 51.035  -40.357 -22.116  1.00 60.01  ? 175 ASP A O   1 
ATOM   1374  C CB  . ASP A 1 174 ? 49.236  -37.819 -21.439  1.00 62.98  ? 175 ASP A CB  1 
ATOM   1375  C CG  . ASP A 1 174 ? 48.884  -36.479 -20.829  1.00 77.56  ? 175 ASP A CG  1 
ATOM   1376  O OD1 . ASP A 1 174 ? 49.621  -36.018 -19.931  1.00 77.28  ? 175 ASP A OD1 1 
ATOM   1377  O OD2 . ASP A 1 174 ? 47.866  -35.888 -21.245  1.00 65.90  ? 175 ASP A OD2 1 
ATOM   1378  N N   . LEU A 1 175 ? 49.847  -40.818 -20.258  1.00 54.37  ? 176 LEU A N   1 
ATOM   1379  C CA  . LEU A 1 175 ? 49.821  -42.258 -20.460  1.00 52.02  ? 176 LEU A CA  1 
ATOM   1380  C C   . LEU A 1 175 ? 48.387  -42.711 -20.680  1.00 61.31  ? 176 LEU A C   1 
ATOM   1381  O O   . LEU A 1 175 ? 47.494  -42.367 -19.897  1.00 69.34  ? 176 LEU A O   1 
ATOM   1382  C CB  . LEU A 1 175 ? 50.432  -42.992 -19.264  1.00 55.76  ? 176 LEU A CB  1 
ATOM   1383  C CG  . LEU A 1 175 ? 51.791  -43.647 -19.514  1.00 67.21  ? 176 LEU A CG  1 
ATOM   1384  C CD1 . LEU A 1 175 ? 52.771  -42.641 -20.095  1.00 65.48  ? 176 LEU A CD1 1 
ATOM   1385  C CD2 . LEU A 1 175 ? 52.339  -44.252 -18.233  1.00 65.53  ? 176 LEU A CD2 1 
ATOM   1386  N N   . LEU A 1 176 ? 48.172  -43.476 -21.748  1.00 60.49  ? 177 LEU A N   1 
ATOM   1387  C CA  . LEU A 1 176 ? 46.882  -44.088 -22.044  1.00 58.34  ? 177 LEU A CA  1 
ATOM   1388  C C   . LEU A 1 176 ? 46.914  -45.517 -21.515  1.00 52.40  ? 177 LEU A C   1 
ATOM   1389  O O   . LEU A 1 176 ? 47.626  -46.369 -22.056  1.00 57.76  ? 177 LEU A O   1 
ATOM   1390  C CB  . LEU A 1 176 ? 46.594  -44.057 -23.544  1.00 50.04  ? 177 LEU A CB  1 
ATOM   1391  C CG  . LEU A 1 176 ? 45.442  -44.927 -24.054  1.00 55.41  ? 177 LEU A CG  1 
ATOM   1392  C CD1 . LEU A 1 176 ? 44.111  -44.494 -23.452  1.00 62.66  ? 177 LEU A CD1 1 
ATOM   1393  C CD2 . LEU A 1 176 ? 45.385  -44.898 -25.574  1.00 60.58  ? 177 LEU A CD2 1 
ATOM   1394  N N   . ILE A 1 177 ? 46.153  -45.774 -20.456  1.00 54.06  ? 178 ILE A N   1 
ATOM   1395  C CA  . ILE A 1 177 ? 46.119  -47.075 -19.799  1.00 46.19  ? 178 ILE A CA  1 
ATOM   1396  C C   . ILE A 1 177 ? 44.760  -47.711 -20.045  1.00 56.20  ? 178 ILE A C   1 
ATOM   1397  O O   . ILE A 1 177 ? 43.724  -47.041 -19.955  1.00 53.57  ? 178 ILE A O   1 
ATOM   1398  C CB  . ILE A 1 177 ? 46.401  -46.952 -18.288  1.00 40.77  ? 178 ILE A CB  1 
ATOM   1399  C CG1 . ILE A 1 177 ? 47.685  -46.157 -18.048  1.00 54.66  ? 178 ILE A CG1 1 
ATOM   1400  C CG2 . ILE A 1 177 ? 46.496  -48.331 -17.652  1.00 43.93  ? 178 ILE A CG2 1 
ATOM   1401  C CD1 . ILE A 1 177 ? 48.098  -46.086 -16.593  1.00 60.32  ? 178 ILE A CD1 1 
ATOM   1402  N N   . LEU A 1 178 ? 44.764  -49.004 -20.359  1.00 52.41  ? 179 LEU A N   1 
ATOM   1403  C CA  . LEU A 1 178 ? 43.541  -49.754 -20.595  1.00 36.42  ? 179 LEU A CA  1 
ATOM   1404  C C   . LEU A 1 178 ? 43.492  -50.973 -19.685  1.00 53.13  ? 179 LEU A C   1 
ATOM   1405  O O   . LEU A 1 178 ? 44.522  -51.572 -19.361  1.00 52.50  ? 179 LEU A O   1 
ATOM   1406  C CB  . LEU A 1 178 ? 43.418  -50.195 -22.059  1.00 54.95  ? 179 LEU A CB  1 
ATOM   1407  C CG  . LEU A 1 178 ? 43.321  -49.089 -23.114  1.00 65.53  ? 179 LEU A CG  1 
ATOM   1408  C CD1 . LEU A 1 178 ? 44.682  -48.808 -23.738  1.00 50.92  ? 179 LEU A CD1 1 
ATOM   1409  C CD2 . LEU A 1 178 ? 42.292  -49.437 -24.182  1.00 63.49  ? 179 LEU A CD2 1 
ATOM   1410  N N   . TRP A 1 179 ? 42.277  -51.331 -19.279  1.00 51.42  ? 180 TRP A N   1 
ATOM   1411  C CA  . TRP A 1 179 ? 42.039  -52.503 -18.450  1.00 39.18  ? 180 TRP A CA  1 
ATOM   1412  C C   . TRP A 1 179 ? 40.623  -52.987 -18.719  1.00 51.27  ? 180 TRP A C   1 
ATOM   1413  O O   . TRP A 1 179 ? 39.846  -52.333 -19.420  1.00 51.27  ? 180 TRP A O   1 
ATOM   1414  C CB  . TRP A 1 179 ? 42.242  -52.195 -16.963  1.00 51.42  ? 180 TRP A CB  1 
ATOM   1415  C CG  . TRP A 1 179 ? 41.195  -51.287 -16.399  1.00 45.87  ? 180 TRP A CG  1 
ATOM   1416  C CD1 . TRP A 1 179 ? 40.051  -51.658 -15.755  1.00 40.88  ? 180 TRP A CD1 1 
ATOM   1417  C CD2 . TRP A 1 179 ? 41.190  -49.855 -16.436  1.00 43.23  ? 180 TRP A CD2 1 
ATOM   1418  N NE1 . TRP A 1 179 ? 39.335  -50.546 -15.385  1.00 48.39  ? 180 TRP A NE1 1 
ATOM   1419  C CE2 . TRP A 1 179 ? 40.012  -49.426 -15.792  1.00 42.54  ? 180 TRP A CE2 1 
ATOM   1420  C CE3 . TRP A 1 179 ? 42.066  -48.894 -16.949  1.00 52.39  ? 180 TRP A CE3 1 
ATOM   1421  C CZ2 . TRP A 1 179 ? 39.689  -48.079 -15.647  1.00 43.25  ? 180 TRP A CZ2 1 
ATOM   1422  C CZ3 . TRP A 1 179 ? 41.742  -47.556 -16.804  1.00 54.94  ? 180 TRP A CZ3 1 
ATOM   1423  C CH2 . TRP A 1 179 ? 40.565  -47.162 -16.158  1.00 43.30  ? 180 TRP A CH2 1 
ATOM   1424  N N   . GLY A 1 180 ? 40.287  -54.145 -18.151  1.00 47.16  ? 181 GLY A N   1 
ATOM   1425  C CA  . GLY A 1 180 ? 38.981  -54.722 -18.395  1.00 46.11  ? 181 GLY A CA  1 
ATOM   1426  C C   . GLY A 1 180 ? 38.492  -55.578 -17.248  1.00 45.99  ? 181 GLY A C   1 
ATOM   1427  O O   . GLY A 1 180 ? 39.235  -55.921 -16.326  1.00 46.68  ? 181 GLY A O   1 
ATOM   1428  N N   . ILE A 1 181 ? 37.207  -55.913 -17.323  1.00 43.27  ? 182 ILE A N   1 
ATOM   1429  C CA  . ILE A 1 181 ? 36.551  -56.818 -16.388  1.00 50.29  ? 182 ILE A CA  1 
ATOM   1430  C C   . ILE A 1 181 ? 35.894  -57.928 -17.194  1.00 55.89  ? 182 ILE A C   1 
ATOM   1431  O O   . ILE A 1 181 ? 35.337  -57.679 -18.269  1.00 51.24  ? 182 ILE A O   1 
ATOM   1432  C CB  . ILE A 1 181 ? 35.517  -56.086 -15.503  1.00 52.67  ? 182 ILE A CB  1 
ATOM   1433  C CG1 . ILE A 1 181 ? 34.841  -57.065 -14.539  1.00 49.73  ? 182 ILE A CG1 1 
ATOM   1434  C CG2 . ILE A 1 181 ? 34.490  -55.351 -16.361  1.00 45.58  ? 182 ILE A CG2 1 
ATOM   1435  C CD1 . ILE A 1 181 ? 33.816  -56.427 -13.626  1.00 48.53  ? 182 ILE A CD1 1 
ATOM   1436  N N   . HIS A 1 182 ? 35.977  -59.153 -16.687  1.00 37.48  ? 183 HIS A N   1 
ATOM   1437  C CA  . HIS A 1 182 ? 35.403  -60.311 -17.355  1.00 47.39  ? 183 HIS A CA  1 
ATOM   1438  C C   . HIS A 1 182 ? 34.087  -60.695 -16.693  1.00 50.43  ? 183 HIS A C   1 
ATOM   1439  O O   . HIS A 1 182 ? 34.032  -60.884 -15.474  1.00 56.94  ? 183 HIS A O   1 
ATOM   1440  C CB  . HIS A 1 182 ? 36.368  -61.496 -17.327  1.00 39.26  ? 183 HIS A CB  1 
ATOM   1441  C CG  . HIS A 1 182 ? 35.761  -62.773 -17.815  1.00 49.25  ? 183 HIS A CG  1 
ATOM   1442  N ND1 . HIS A 1 182 ? 35.525  -63.848 -16.987  1.00 52.92  ? 183 HIS A ND1 1 
ATOM   1443  C CD2 . HIS A 1 182 ? 35.325  -63.140 -19.043  1.00 52.37  ? 183 HIS A CD2 1 
ATOM   1444  C CE1 . HIS A 1 182 ? 34.979  -64.827 -17.686  1.00 50.62  ? 183 HIS A CE1 1 
ATOM   1445  N NE2 . HIS A 1 182 ? 34.846  -64.423 -18.936  1.00 49.75  ? 183 HIS A NE2 1 
ATOM   1446  N N   . HIS A 1 183 ? 33.035  -60.806 -17.500  1.00 46.42  ? 184 HIS A N   1 
ATOM   1447  C CA  . HIS A 1 183 ? 31.726  -61.252 -17.036  1.00 55.13  ? 184 HIS A CA  1 
ATOM   1448  C C   . HIS A 1 183 ? 31.613  -62.749 -17.308  1.00 48.03  ? 184 HIS A C   1 
ATOM   1449  O O   . HIS A 1 183 ? 31.495  -63.169 -18.464  1.00 68.66  ? 184 HIS A O   1 
ATOM   1450  C CB  . HIS A 1 183 ? 30.608  -60.479 -17.734  1.00 48.99  ? 184 HIS A CB  1 
ATOM   1451  C CG  . HIS A 1 183 ? 30.681  -58.995 -17.539  1.00 41.71  ? 184 HIS A CG  1 
ATOM   1452  N ND1 . HIS A 1 183 ? 30.345  -58.383 -16.351  1.00 47.38  ? 184 HIS A ND1 1 
ATOM   1453  C CD2 . HIS A 1 183 ? 31.040  -58.000 -18.385  1.00 56.43  ? 184 HIS A CD2 1 
ATOM   1454  C CE1 . HIS A 1 183 ? 30.499  -57.077 -16.470  1.00 56.12  ? 184 HIS A CE1 1 
ATOM   1455  N NE2 . HIS A 1 183 ? 30.921  -56.818 -17.695  1.00 42.16  ? 184 HIS A NE2 1 
ATOM   1456  N N   . SER A 1 184 ? 31.654  -63.550 -16.246  1.00 54.23  ? 185 SER A N   1 
ATOM   1457  C CA  . SER A 1 184 ? 31.574  -64.993 -16.390  1.00 53.50  ? 185 SER A CA  1 
ATOM   1458  C C   . SER A 1 184 ? 30.124  -65.429 -16.596  1.00 61.57  ? 185 SER A C   1 
ATOM   1459  O O   . SER A 1 184 ? 29.178  -64.653 -16.435  1.00 61.81  ? 185 SER A O   1 
ATOM   1460  C CB  . SER A 1 184 ? 32.193  -65.690 -15.178  1.00 59.69  ? 185 SER A CB  1 
ATOM   1461  O OG  . SER A 1 184 ? 31.633  -65.220 -13.966  1.00 67.80  ? 185 SER A OG  1 
ATOM   1462  N N   . ASN A 1 185 ? 29.959  -66.700 -16.964  1.00 59.72  ? 186 ASN A N   1 
ATOM   1463  C CA  . ASN A 1 185 ? 28.678  -67.210 -17.437  1.00 62.34  ? 186 ASN A CA  1 
ATOM   1464  C C   . ASN A 1 185 ? 27.787  -67.738 -16.317  1.00 57.80  ? 186 ASN A C   1 
ATOM   1465  O O   . ASN A 1 185 ? 26.563  -67.579 -16.382  1.00 57.03  ? 186 ASN A O   1 
ATOM   1466  C CB  . ASN A 1 185 ? 28.912  -68.307 -18.481  1.00 52.06  ? 186 ASN A CB  1 
ATOM   1467  C CG  . ASN A 1 185 ? 29.524  -67.770 -19.760  1.00 54.89  ? 186 ASN A CG  1 
ATOM   1468  O OD1 . ASN A 1 185 ? 29.074  -66.757 -20.296  1.00 62.60  ? 186 ASN A OD1 1 
ATOM   1469  N ND2 . ASN A 1 185 ? 30.562  -68.440 -20.248  1.00 60.83  ? 186 ASN A ND2 1 
ATOM   1470  N N   . ASN A 1 186 ? 28.361  -68.365 -15.295  1.00 60.96  ? 187 ASN A N   1 
ATOM   1471  C CA  . ASN A 1 186 ? 27.562  -68.968 -14.235  1.00 55.53  ? 187 ASN A CA  1 
ATOM   1472  C C   . ASN A 1 186 ? 28.401  -69.035 -12.965  1.00 68.23  ? 187 ASN A C   1 
ATOM   1473  O O   . ASN A 1 186 ? 29.573  -68.650 -12.946  1.00 69.69  ? 187 ASN A O   1 
ATOM   1474  C CB  . ASN A 1 186 ? 27.047  -70.350 -14.647  1.00 54.68  ? 187 ASN A CB  1 
ATOM   1475  C CG  . ASN A 1 186 ? 28.153  -71.260 -15.135  1.00 60.25  ? 187 ASN A CG  1 
ATOM   1476  O OD1 . ASN A 1 186 ? 28.964  -71.750 -14.349  1.00 78.31  ? 187 ASN A OD1 1 
ATOM   1477  N ND2 . ASN A 1 186 ? 28.187  -71.500 -16.439  1.00 63.67  ? 187 ASN A ND2 1 
ATOM   1478  N N   . ALA A 1 187 ? 27.775  -69.527 -11.892  1.00 64.25  ? 188 ALA A N   1 
ATOM   1479  C CA  . ALA A 1 187 ? 28.441  -69.569 -10.594  1.00 49.04  ? 188 ALA A CA  1 
ATOM   1480  C C   . ALA A 1 187 ? 29.645  -70.505 -10.609  1.00 69.91  ? 188 ALA A C   1 
ATOM   1481  O O   . ALA A 1 187 ? 30.707  -70.166 -10.073  1.00 68.77  ? 188 ALA A O   1 
ATOM   1482  C CB  . ALA A 1 187 ? 27.446  -69.989 -9.514   1.00 57.25  ? 188 ALA A CB  1 
ATOM   1483  N N   . GLU A 1 188 ? 29.501  -71.689 -11.213  1.00 59.05  ? 189 GLU A N   1 
ATOM   1484  C CA  . GLU A 1 188 ? 30.604  -72.645 -11.216  1.00 68.28  ? 189 GLU A CA  1 
ATOM   1485  C C   . GLU A 1 188 ? 31.782  -72.134 -12.037  1.00 69.91  ? 189 GLU A C   1 
ATOM   1486  O O   . GLU A 1 188 ? 32.943  -72.317 -11.648  1.00 72.65  ? 189 GLU A O   1 
ATOM   1487  C CB  . GLU A 1 188 ? 30.132  -74.003 -11.736  1.00 64.00  ? 189 GLU A CB  1 
ATOM   1488  C CG  . GLU A 1 188 ? 31.253  -75.022 -11.885  1.00 81.65  ? 189 GLU A CG  1 
ATOM   1489  C CD  . GLU A 1 188 ? 30.759  -76.453 -11.847  1.00 108.60 ? 189 GLU A CD  1 
ATOM   1490  O OE1 . GLU A 1 188 ? 29.725  -76.709 -11.193  1.00 112.03 ? 189 GLU A OE1 1 
ATOM   1491  O OE2 . GLU A 1 188 ? 31.406  -77.323 -12.469  1.00 106.34 ? 189 GLU A OE2 1 
ATOM   1492  N N   . GLU A 1 189 ? 31.508  -71.492 -13.174  1.00 63.80  ? 190 GLU A N   1 
ATOM   1493  C CA  . GLU A 1 189 ? 32.585  -70.919 -13.974  1.00 55.12  ? 190 GLU A CA  1 
ATOM   1494  C C   . GLU A 1 189 ? 33.299  -69.805 -13.217  1.00 65.41  ? 190 GLU A C   1 
ATOM   1495  O O   . GLU A 1 189 ? 34.520  -69.648 -13.332  1.00 66.94  ? 190 GLU A O   1 
ATOM   1496  C CB  . GLU A 1 189 ? 32.035  -70.403 -15.304  1.00 64.39  ? 190 GLU A CB  1 
ATOM   1497  C CG  . GLU A 1 189 ? 33.068  -69.712 -16.178  1.00 67.61  ? 190 GLU A CG  1 
ATOM   1498  C CD  . GLU A 1 189 ? 32.495  -69.253 -17.503  1.00 77.96  ? 190 GLU A CD  1 
ATOM   1499  O OE1 . GLU A 1 189 ? 32.112  -70.118 -18.320  1.00 86.35  ? 190 GLU A OE1 1 
ATOM   1500  O OE2 . GLU A 1 189 ? 32.416  -68.026 -17.721  1.00 68.99  ? 190 GLU A OE2 1 
ATOM   1501  N N   . GLN A 1 190 ? 32.549  -69.019 -12.438  1.00 64.08  ? 191 GLN A N   1 
ATOM   1502  C CA  . GLN A 1 190 ? 33.159  -67.952 -11.650  1.00 46.00  ? 191 GLN A CA  1 
ATOM   1503  C C   . GLN A 1 190 ? 34.156  -68.508 -10.640  1.00 60.19  ? 191 GLN A C   1 
ATOM   1504  O O   . GLN A 1 190 ? 35.259  -67.970 -10.486  1.00 64.39  ? 191 GLN A O   1 
ATOM   1505  C CB  . GLN A 1 190 ? 32.073  -67.139 -10.944  1.00 48.99  ? 191 GLN A CB  1 
ATOM   1506  C CG  . GLN A 1 190 ? 32.596  -66.127 -9.934   1.00 51.00  ? 191 GLN A CG  1 
ATOM   1507  C CD  . GLN A 1 190 ? 33.329  -64.968 -10.582  1.00 59.33  ? 191 GLN A CD  1 
ATOM   1508  O OE1 . GLN A 1 190 ? 33.223  -64.744 -11.788  1.00 50.84  ? 191 GLN A OE1 1 
ATOM   1509  N NE2 . GLN A 1 190 ? 34.079  -64.223 -9.779   1.00 55.46  ? 191 GLN A NE2 1 
ATOM   1510  N N   . THR A 1 191 ? 33.790  -69.587 -9.945   1.00 54.81  ? 192 THR A N   1 
ATOM   1511  C CA  . THR A 1 191 ? 34.694  -70.176 -8.962   1.00 65.42  ? 192 THR A CA  1 
ATOM   1512  C C   . THR A 1 191 ? 35.808  -70.982 -9.618   1.00 59.36  ? 192 THR A C   1 
ATOM   1513  O O   . THR A 1 191 ? 36.902  -71.090 -9.053   1.00 74.48  ? 192 THR A O   1 
ATOM   1514  C CB  . THR A 1 191 ? 33.919  -71.063 -7.985   1.00 59.97  ? 192 THR A CB  1 
ATOM   1515  O OG1 . THR A 1 191 ? 33.517  -72.270 -8.644   1.00 81.64  ? 192 THR A OG1 1 
ATOM   1516  C CG2 . THR A 1 191 ? 32.683  -70.336 -7.471   1.00 55.35  ? 192 THR A CG2 1 
ATOM   1517  N N   . ASN A 1 192 ? 35.554  -71.556 -10.797  1.00 56.95  ? 193 ASN A N   1 
ATOM   1518  C CA  . ASN A 1 192 ? 36.592  -72.301 -11.499  1.00 59.87  ? 193 ASN A CA  1 
ATOM   1519  C C   . ASN A 1 192 ? 37.704  -71.398 -12.016  1.00 56.39  ? 193 ASN A C   1 
ATOM   1520  O O   . ASN A 1 192 ? 38.812  -71.884 -12.267  1.00 66.85  ? 193 ASN A O   1 
ATOM   1521  C CB  . ASN A 1 192 ? 35.985  -73.093 -12.658  1.00 60.27  ? 193 ASN A CB  1 
ATOM   1522  C CG  . ASN A 1 192 ? 35.266  -74.345 -12.196  1.00 88.51  ? 193 ASN A CG  1 
ATOM   1523  O OD1 . ASN A 1 192 ? 35.080  -74.562 -10.998  1.00 87.21  ? 193 ASN A OD1 1 
ATOM   1524  N ND2 . ASN A 1 192 ? 34.857  -75.177 -13.146  1.00 84.57  ? 193 ASN A ND2 1 
ATOM   1525  N N   . LEU A 1 193 ? 37.438  -70.104 -12.180  1.00 65.46  ? 194 LEU A N   1 
ATOM   1526  C CA  . LEU A 1 193 ? 38.437  -69.153 -12.651  1.00 62.35  ? 194 LEU A CA  1 
ATOM   1527  C C   . LEU A 1 193 ? 39.019  -68.296 -11.537  1.00 61.31  ? 194 LEU A C   1 
ATOM   1528  O O   . LEU A 1 193 ? 40.235  -68.082 -11.500  1.00 62.54  ? 194 LEU A O   1 
ATOM   1529  C CB  . LEU A 1 193 ? 37.837  -68.235 -13.724  1.00 55.23  ? 194 LEU A CB  1 
ATOM   1530  C CG  . LEU A 1 193 ? 37.893  -68.681 -15.186  1.00 55.61  ? 194 LEU A CG  1 
ATOM   1531  C CD1 . LEU A 1 193 ? 37.076  -69.944 -15.421  1.00 48.64  ? 194 LEU A CD1 1 
ATOM   1532  C CD2 . LEU A 1 193 ? 37.422  -67.557 -16.097  1.00 58.72  ? 194 LEU A CD2 1 
ATOM   1533  N N   . TYR A 1 194 ? 38.183  -67.801 -10.624  1.00 60.27  ? 195 TYR A N   1 
ATOM   1534  C CA  . TYR A 1 194 ? 38.621  -66.840 -9.625   1.00 61.22  ? 195 TYR A CA  1 
ATOM   1535  C C   . TYR A 1 194 ? 38.371  -67.277 -8.189   1.00 61.27  ? 195 TYR A C   1 
ATOM   1536  O O   . TYR A 1 194 ? 38.808  -66.575 -7.271   1.00 63.73  ? 195 TYR A O   1 
ATOM   1537  C CB  . TYR A 1 194 ? 37.941  -65.484 -9.870   1.00 55.63  ? 195 TYR A CB  1 
ATOM   1538  C CG  . TYR A 1 194 ? 37.927  -65.089 -11.330  1.00 50.54  ? 195 TYR A CG  1 
ATOM   1539  C CD1 . TYR A 1 194 ? 39.096  -64.717 -11.979  1.00 47.65  ? 195 TYR A CD1 1 
ATOM   1540  C CD2 . TYR A 1 194 ? 36.748  -65.098 -12.060  1.00 55.70  ? 195 TYR A CD2 1 
ATOM   1541  C CE1 . TYR A 1 194 ? 39.091  -64.361 -13.315  1.00 46.29  ? 195 TYR A CE1 1 
ATOM   1542  C CE2 . TYR A 1 194 ? 36.732  -64.743 -13.396  1.00 49.35  ? 195 TYR A CE2 1 
ATOM   1543  C CZ  . TYR A 1 194 ? 37.906  -64.375 -14.018  1.00 51.88  ? 195 TYR A CZ  1 
ATOM   1544  O OH  . TYR A 1 194 ? 37.896  -64.019 -15.349  1.00 50.15  ? 195 TYR A OH  1 
ATOM   1545  N N   . LYS A 1 195 ? 37.630  -68.366 -7.966   1.00 66.27  ? 196 LYS A N   1 
ATOM   1546  C CA  . LYS A 1 195 ? 37.504  -69.017 -6.663   1.00 56.17  ? 196 LYS A CA  1 
ATOM   1547  C C   . LYS A 1 195 ? 36.680  -68.174 -5.690   1.00 64.98  ? 196 LYS A C   1 
ATOM   1548  O O   . LYS A 1 195 ? 36.257  -68.658 -4.635   1.00 86.82  ? 196 LYS A O   1 
ATOM   1549  C CB  . LYS A 1 195 ? 38.901  -69.320 -6.098   1.00 73.23  ? 196 LYS A CB  1 
ATOM   1550  C CG  . LYS A 1 195 ? 38.957  -69.803 -4.655   1.00 69.26  ? 196 LYS A CG  1 
ATOM   1551  C CD  . LYS A 1 195 ? 38.271  -71.147 -4.474   1.00 69.25  ? 196 LYS A CD  1 
ATOM   1552  C CE  . LYS A 1 195 ? 37.838  -71.340 -3.026   1.00 84.20  ? 196 LYS A CE  1 
ATOM   1553  N NZ  . LYS A 1 195 ? 38.333  -72.617 -2.439   1.00 96.79  ? 196 LYS A NZ  1 
ATOM   1554  N N   . ASN A 1 196 ? 36.382  -66.938 -6.071   1.00 66.44  ? 197 ASN A N   1 
ATOM   1555  C CA  . ASN A 1 196 ? 35.629  -66.027 -5.218   1.00 54.88  ? 197 ASN A CA  1 
ATOM   1556  C C   . ASN A 1 196 ? 34.280  -65.751 -5.862   1.00 63.02  ? 197 ASN A C   1 
ATOM   1557  O O   . ASN A 1 196 ? 34.230  -65.116 -6.928   1.00 68.89  ? 197 ASN A O   1 
ATOM   1558  C CB  . ASN A 1 196 ? 36.401  -64.725 -5.003   1.00 66.17  ? 197 ASN A CB  1 
ATOM   1559  C CG  . ASN A 1 196 ? 37.798  -64.957 -4.454   1.00 62.13  ? 197 ASN A CG  1 
ATOM   1560  O OD1 . ASN A 1 196 ? 38.042  -65.924 -3.732   1.00 60.08  ? 197 ASN A OD1 1 
ATOM   1561  N ND2 . ASN A 1 196 ? 38.722  -64.066 -4.795   1.00 55.75  ? 197 ASN A ND2 1 
ATOM   1562  N N   . PRO A 1 197 ? 33.173  -66.212 -5.275   1.00 61.43  ? 198 PRO A N   1 
ATOM   1563  C CA  . PRO A 1 197 ? 31.867  -66.036 -5.937   1.00 67.55  ? 198 PRO A CA  1 
ATOM   1564  C C   . PRO A 1 197 ? 31.498  -64.585 -6.200   1.00 65.75  ? 198 PRO A C   1 
ATOM   1565  O O   . PRO A 1 197 ? 30.933  -64.278 -7.257   1.00 64.52  ? 198 PRO A O   1 
ATOM   1566  C CB  . PRO A 1 197 ? 30.891  -66.707 -4.958   1.00 48.24  ? 198 PRO A CB  1 
ATOM   1567  C CG  . PRO A 1 197 ? 31.606  -66.717 -3.645   1.00 53.45  ? 198 PRO A CG  1 
ATOM   1568  C CD  . PRO A 1 197 ? 33.052  -66.893 -3.976   1.00 64.56  ? 198 PRO A CD  1 
ATOM   1569  N N   . THR A 1 198 ? 31.810  -63.680 -5.276   1.00 45.42  ? 199 THR A N   1 
ATOM   1570  C CA  . THR A 1 198 ? 31.489  -62.264 -5.418   1.00 61.12  ? 199 THR A CA  1 
ATOM   1571  C C   . THR A 1 198 ? 32.786  -61.472 -5.499   1.00 59.91  ? 199 THR A C   1 
ATOM   1572  O O   . THR A 1 198 ? 33.622  -61.550 -4.592   1.00 62.28  ? 199 THR A O   1 
ATOM   1573  C CB  . THR A 1 198 ? 30.624  -61.774 -4.254   1.00 50.42  ? 199 THR A CB  1 
ATOM   1574  O OG1 . THR A 1 198 ? 31.078  -62.369 -3.032   1.00 89.03  ? 199 THR A OG1 1 
ATOM   1575  C CG2 . THR A 1 198 ? 29.164  -62.141 -4.483   1.00 61.34  ? 199 THR A CG2 1 
ATOM   1576  N N   . THR A 1 199 ? 32.946  -60.705 -6.576   1.00 51.54  ? 200 THR A N   1 
ATOM   1577  C CA  . THR A 1 199 ? 34.191  -60.010 -6.867   1.00 52.52  ? 200 THR A CA  1 
ATOM   1578  C C   . THR A 1 199 ? 33.905  -58.570 -7.271   1.00 50.09  ? 200 THR A C   1 
ATOM   1579  O O   . THR A 1 199 ? 32.756  -58.169 -7.475   1.00 56.56  ? 200 THR A O   1 
ATOM   1580  C CB  . THR A 1 199 ? 34.986  -60.720 -7.972   1.00 62.31  ? 200 THR A CB  1 
ATOM   1581  O OG1 . THR A 1 199 ? 34.155  -60.890 -9.127   1.00 57.69  ? 200 THR A OG1 1 
ATOM   1582  C CG2 . THR A 1 199 ? 35.469  -62.082 -7.497   1.00 45.64  ? 200 THR A CG2 1 
ATOM   1583  N N   . TYR A 1 200 ? 34.980  -57.793 -7.386   1.00 54.39  ? 201 TYR A N   1 
ATOM   1584  C CA  . TYR A 1 200 ? 34.891  -56.373 -7.697   1.00 54.52  ? 201 TYR A CA  1 
ATOM   1585  C C   . TYR A 1 200 ? 36.211  -55.921 -8.303   1.00 52.52  ? 201 TYR A C   1 
ATOM   1586  O O   . TYR A 1 200 ? 37.235  -56.599 -8.182   1.00 50.07  ? 201 TYR A O   1 
ATOM   1587  C CB  . TYR A 1 200 ? 34.576  -55.544 -6.449   1.00 43.47  ? 201 TYR A CB  1 
ATOM   1588  C CG  . TYR A 1 200 ? 35.703  -55.552 -5.442   1.00 49.04  ? 201 TYR A CG  1 
ATOM   1589  C CD1 . TYR A 1 200 ? 35.822  -56.580 -4.517   1.00 48.44  ? 201 TYR A CD1 1 
ATOM   1590  C CD2 . TYR A 1 200 ? 36.658  -54.540 -5.426   1.00 47.52  ? 201 TYR A CD2 1 
ATOM   1591  C CE1 . TYR A 1 200 ? 36.855  -56.601 -3.601   1.00 52.60  ? 201 TYR A CE1 1 
ATOM   1592  C CE2 . TYR A 1 200 ? 37.695  -54.552 -4.513   1.00 50.30  ? 201 TYR A CE2 1 
ATOM   1593  C CZ  . TYR A 1 200 ? 37.789  -55.583 -3.602   1.00 55.83  ? 201 TYR A CZ  1 
ATOM   1594  O OH  . TYR A 1 200 ? 38.820  -55.594 -2.691   1.00 63.40  ? 201 TYR A OH  1 
ATOM   1595  N N   . ILE A 1 201 ? 36.174  -54.761 -8.954   1.00 44.63  ? 202 ILE A N   1 
ATOM   1596  C CA  . ILE A 1 201 ? 37.374  -54.063 -9.402   1.00 44.10  ? 202 ILE A CA  1 
ATOM   1597  C C   . ILE A 1 201 ? 37.241  -52.598 -9.016   1.00 47.29  ? 202 ILE A C   1 
ATOM   1598  O O   . ILE A 1 201 ? 36.249  -51.949 -9.365   1.00 51.03  ? 202 ILE A O   1 
ATOM   1599  C CB  . ILE A 1 201 ? 37.594  -54.197 -10.921  1.00 58.17  ? 202 ILE A CB  1 
ATOM   1600  C CG1 . ILE A 1 201 ? 37.772  -55.663 -11.315  1.00 53.12  ? 202 ILE A CG1 1 
ATOM   1601  C CG2 . ILE A 1 201 ? 38.800  -53.377 -11.354  1.00 37.83  ? 202 ILE A CG2 1 
ATOM   1602  C CD1 . ILE A 1 201 ? 37.968  -55.871 -12.798  1.00 53.51  ? 202 ILE A CD1 1 
ATOM   1603  N N   . SER A 1 202 ? 38.235  -52.077 -8.304   1.00 46.54  ? 203 SER A N   1 
ATOM   1604  C CA  . SER A 1 202 ? 38.288  -50.666 -7.937   1.00 43.72  ? 203 SER A CA  1 
ATOM   1605  C C   . SER A 1 202 ? 39.465  -50.017 -8.651   1.00 54.66  ? 203 SER A C   1 
ATOM   1606  O O   . SER A 1 202 ? 40.609  -50.460 -8.498   1.00 60.35  ? 203 SER A O   1 
ATOM   1607  C CB  . SER A 1 202 ? 38.410  -50.490 -6.424   1.00 43.95  ? 203 SER A CB  1 
ATOM   1608  O OG  . SER A 1 202 ? 37.181  -50.768 -5.776   1.00 79.86  ? 203 SER A OG  1 
ATOM   1609  N N   . VAL A 1 203 ? 39.184  -48.972 -9.424   1.00 44.09  ? 204 VAL A N   1 
ATOM   1610  C CA  . VAL A 1 203 ? 40.200  -48.209 -10.138  1.00 42.49  ? 204 VAL A CA  1 
ATOM   1611  C C   . VAL A 1 203 ? 40.143  -46.772 -9.641   1.00 46.03  ? 204 VAL A C   1 
ATOM   1612  O O   . VAL A 1 203 ? 39.073  -46.152 -9.641   1.00 50.82  ? 204 VAL A O   1 
ATOM   1613  C CB  . VAL A 1 203 ? 39.995  -48.272 -11.663  1.00 49.26  ? 204 VAL A CB  1 
ATOM   1614  C CG1 . VAL A 1 203 ? 41.197  -47.682 -12.384  1.00 43.50  ? 204 VAL A CG1 1 
ATOM   1615  C CG2 . VAL A 1 203 ? 39.747  -49.706 -12.108  1.00 49.48  ? 204 VAL A CG2 1 
ATOM   1616  N N   . GLY A 1 204 ? 41.291  -46.246 -9.218   1.00 49.03  ? 205 GLY A N   1 
ATOM   1617  C CA  . GLY A 1 204 ? 41.343  -44.912 -8.654   1.00 44.10  ? 205 GLY A CA  1 
ATOM   1618  C C   . GLY A 1 204 ? 42.524  -44.077 -9.104   1.00 55.80  ? 205 GLY A C   1 
ATOM   1619  O O   . GLY A 1 204 ? 43.679  -44.507 -9.015   1.00 62.33  ? 205 GLY A O   1 
ATOM   1620  N N   . THR A 1 205 ? 42.239  -42.873 -9.602   1.00 59.93  ? 206 THR A N   1 
ATOM   1621  C CA  . THR A 1 205 ? 43.262  -41.883 -9.920   1.00 63.18  ? 206 THR A CA  1 
ATOM   1622  C C   . THR A 1 205 ? 42.905  -40.584 -9.208   1.00 72.00  ? 206 THR A C   1 
ATOM   1623  O O   . THR A 1 205 ? 42.022  -40.565 -8.344   1.00 78.26  ? 206 THR A O   1 
ATOM   1624  C CB  . THR A 1 205 ? 43.388  -41.660 -11.434  1.00 70.61  ? 206 THR A CB  1 
ATOM   1625  O OG1 . THR A 1 205 ? 42.263  -40.904 -11.905  1.00 70.06  ? 206 THR A OG1 1 
ATOM   1626  C CG2 . THR A 1 205 ? 43.450  -42.989 -12.178  1.00 62.75  ? 206 THR A CG2 1 
ATOM   1627  N N   . SER A 1 206 ? 43.595  -39.495 -9.549   1.00 73.36  ? 207 SER A N   1 
ATOM   1628  C CA  . SER A 1 206 ? 43.225  -38.192 -9.011   1.00 85.30  ? 207 SER A CA  1 
ATOM   1629  C C   . SER A 1 206 ? 41.874  -37.715 -9.534   1.00 82.96  ? 207 SER A C   1 
ATOM   1630  O O   . SER A 1 206 ? 41.260  -36.838 -8.916   1.00 82.45  ? 207 SER A O   1 
ATOM   1631  C CB  . SER A 1 206 ? 44.302  -37.158 -9.338   1.00 65.05  ? 207 SER A CB  1 
ATOM   1632  O OG  . SER A 1 206 ? 44.423  -36.972 -10.738  1.00 78.74  ? 207 SER A OG  1 
ATOM   1633  N N   . THR A 1 207 ? 41.398  -38.267 -10.654  1.00 66.29  ? 208 THR A N   1 
ATOM   1634  C CA  . THR A 1 207 ? 40.129  -37.861 -11.241  1.00 53.99  ? 208 THR A CA  1 
ATOM   1635  C C   . THR A 1 207 ? 39.147  -39.006 -11.456  1.00 73.91  ? 208 THR A C   1 
ATOM   1636  O O   . THR A 1 207 ? 37.990  -38.741 -11.800  1.00 91.02  ? 208 THR A O   1 
ATOM   1637  C CB  . THR A 1 207 ? 40.359  -37.162 -12.592  1.00 59.63  ? 208 THR A CB  1 
ATOM   1638  O OG1 . THR A 1 207 ? 40.920  -38.092 -13.526  1.00 72.04  ? 208 THR A OG1 1 
ATOM   1639  C CG2 . THR A 1 207 ? 41.302  -35.977 -12.432  1.00 70.06  ? 208 THR A CG2 1 
ATOM   1640  N N   . LEU A 1 208 ? 39.563  -40.256 -11.266  1.00 67.00  ? 209 LEU A N   1 
ATOM   1641  C CA  . LEU A 1 208 ? 38.742  -41.421 -11.564  1.00 61.42  ? 209 LEU A CA  1 
ATOM   1642  C C   . LEU A 1 208 ? 38.454  -42.190 -10.283  1.00 65.81  ? 209 LEU A C   1 
ATOM   1643  O O   . LEU A 1 208 ? 39.374  -42.499 -9.519   1.00 75.99  ? 209 LEU A O   1 
ATOM   1644  C CB  . LEU A 1 208 ? 39.437  -42.330 -12.584  1.00 64.90  ? 209 LEU A CB  1 
ATOM   1645  C CG  . LEU A 1 208 ? 38.826  -43.702 -12.878  1.00 64.59  ? 209 LEU A CG  1 
ATOM   1646  C CD1 . LEU A 1 208 ? 37.504  -43.574 -13.623  1.00 44.02  ? 209 LEU A CD1 1 
ATOM   1647  C CD2 . LEU A 1 208 ? 39.810  -44.551 -13.664  1.00 43.25  ? 209 LEU A CD2 1 
ATOM   1648  N N   . ASN A 1 209 ? 37.177  -42.492 -10.050  1.00 54.42  ? 210 ASN A N   1 
ATOM   1649  C CA  . ASN A 1 209 ? 36.736  -43.299 -8.911   1.00 52.00  ? 210 ASN A CA  1 
ATOM   1650  C C   . ASN A 1 209 ? 35.718  -44.300 -9.454   1.00 60.19  ? 210 ASN A C   1 
ATOM   1651  O O   . ASN A 1 209 ? 34.512  -44.041 -9.452   1.00 59.13  ? 210 ASN A O   1 
ATOM   1652  C CB  . ASN A 1 209 ? 36.157  -42.417 -7.805   1.00 51.00  ? 210 ASN A CB  1 
ATOM   1653  C CG  . ASN A 1 209 ? 35.862  -43.186 -6.530   1.00 67.54  ? 210 ASN A CG  1 
ATOM   1654  O OD1 . ASN A 1 209 ? 35.106  -42.724 -5.677   1.00 59.96  ? 210 ASN A OD1 1 
ATOM   1655  N ND2 . ASN A 1 209 ? 36.459  -44.366 -6.395   1.00 76.45  ? 210 ASN A ND2 1 
ATOM   1656  N N   . GLN A 1 210 ? 36.211  -45.448 -9.909   1.00 54.53  ? 211 GLN A N   1 
ATOM   1657  C CA  . GLN A 1 210 ? 35.410  -46.435 -10.618  1.00 61.06  ? 211 GLN A CA  1 
ATOM   1658  C C   . GLN A 1 210 ? 35.349  -47.737 -9.833   1.00 47.48  ? 211 GLN A C   1 
ATOM   1659  O O   . GLN A 1 210 ? 36.355  -48.186 -9.277   1.00 57.35  ? 211 GLN A O   1 
ATOM   1660  C CB  . GLN A 1 210 ? 35.987  -46.697 -12.013  1.00 55.48  ? 211 GLN A CB  1 
ATOM   1661  C CG  . GLN A 1 210 ? 35.688  -48.080 -12.568  1.00 63.88  ? 211 GLN A CG  1 
ATOM   1662  C CD  . GLN A 1 210 ? 36.233  -48.274 -13.967  1.00 72.16  ? 211 GLN A CD  1 
ATOM   1663  O OE1 . GLN A 1 210 ? 37.091  -49.125 -14.204  1.00 54.71  ? 211 GLN A OE1 1 
ATOM   1664  N NE2 . GLN A 1 210 ? 35.732  -47.484 -14.907  1.00 60.56  ? 211 GLN A NE2 1 
ATOM   1665  N N   . ARG A 1 211 ? 34.162  -48.338 -9.789   1.00 57.88  ? 212 ARG A N   1 
ATOM   1666  C CA  . ARG A 1 211 ? 33.969  -49.655 -9.200   1.00 35.84  ? 212 ARG A CA  1 
ATOM   1667  C C   . ARG A 1 211 ? 33.174  -50.515 -10.172  1.00 51.12  ? 212 ARG A C   1 
ATOM   1668  O O   . ARG A 1 211 ? 32.112  -50.099 -10.647  1.00 50.10  ? 212 ARG A O   1 
ATOM   1669  C CB  . ARG A 1 211 ? 33.254  -49.561 -7.848   1.00 37.14  ? 212 ARG A CB  1 
ATOM   1670  C CG  . ARG A 1 211 ? 33.123  -50.890 -7.127   1.00 54.79  ? 212 ARG A CG  1 
ATOM   1671  C CD  . ARG A 1 211 ? 32.448  -50.733 -5.774   1.00 65.62  ? 212 ARG A CD  1 
ATOM   1672  N NE  . ARG A 1 211 ? 31.910  -52.001 -5.297   1.00 70.00  ? 212 ARG A NE  1 
ATOM   1673  C CZ  . ARG A 1 211 ? 32.611  -52.913 -4.636   1.00 73.41  ? 212 ARG A CZ  1 
ATOM   1674  N NH1 . ARG A 1 211 ? 33.886  -52.722 -4.337   1.00 61.01  ? 212 ARG A NH1 1 
ATOM   1675  N NH2 . ARG A 1 211 ? 32.019  -54.047 -4.271   1.00 60.51  ? 212 ARG A NH2 1 
ATOM   1676  N N   . LEU A 1 212 ? 33.688  -51.708 -10.464  1.00 50.82  ? 213 LEU A N   1 
ATOM   1677  C CA  . LEU A 1 212 ? 33.098  -52.614 -11.439  1.00 42.59  ? 213 LEU A CA  1 
ATOM   1678  C C   . LEU A 1 212 ? 32.786  -53.949 -10.779  1.00 51.99  ? 213 LEU A C   1 
ATOM   1679  O O   . LEU A 1 212 ? 33.592  -54.473 -10.004  1.00 67.27  ? 213 LEU A O   1 
ATOM   1680  C CB  . LEU A 1 212 ? 34.040  -52.836 -12.626  1.00 51.72  ? 213 LEU A CB  1 
ATOM   1681  C CG  . LEU A 1 212 ? 34.580  -51.607 -13.360  1.00 56.34  ? 213 LEU A CG  1 
ATOM   1682  C CD1 . LEU A 1 212 ? 35.674  -52.030 -14.323  1.00 43.85  ? 213 LEU A CD1 1 
ATOM   1683  C CD2 . LEU A 1 212 ? 33.469  -50.879 -14.099  1.00 37.86  ? 213 LEU A CD2 1 
ATOM   1684  N N   . VAL A 1 213 ? 31.614  -54.497 -11.088  1.00 56.11  ? 214 VAL A N   1 
ATOM   1685  C CA  . VAL A 1 213 ? 31.196  -55.795 -10.562  1.00 54.87  ? 214 VAL A CA  1 
ATOM   1686  C C   . VAL A 1 213 ? 30.781  -56.684 -11.730  1.00 48.74  ? 214 VAL A C   1 
ATOM   1687  O O   . VAL A 1 213 ? 30.080  -56.218 -12.641  1.00 53.63  ? 214 VAL A O   1 
ATOM   1688  C CB  . VAL A 1 213 ? 30.056  -55.646 -9.540   1.00 54.25  ? 214 VAL A CB  1 
ATOM   1689  C CG1 . VAL A 1 213 ? 29.638  -57.006 -8.993   1.00 48.34  ? 214 VAL A CG1 1 
ATOM   1690  C CG2 . VAL A 1 213 ? 30.473  -54.722 -8.406   1.00 59.42  ? 214 VAL A CG2 1 
ATOM   1691  N N   . PRO A 1 214 ? 31.197  -57.951 -11.757  1.00 56.09  ? 215 PRO A N   1 
ATOM   1692  C CA  . PRO A 1 214 ? 30.788  -58.838 -12.853  1.00 56.55  ? 215 PRO A CA  1 
ATOM   1693  C C   . PRO A 1 214 ? 29.282  -59.056 -12.880  1.00 59.25  ? 215 PRO A C   1 
ATOM   1694  O O   . PRO A 1 214 ? 28.612  -59.074 -11.845  1.00 64.17  ? 215 PRO A O   1 
ATOM   1695  C CB  . PRO A 1 214 ? 31.534  -60.143 -12.550  1.00 48.04  ? 215 PRO A CB  1 
ATOM   1696  C CG  . PRO A 1 214 ? 32.684  -59.732 -11.706  1.00 54.14  ? 215 PRO A CG  1 
ATOM   1697  C CD  . PRO A 1 214 ? 32.195  -58.584 -10.879  1.00 51.77  ? 215 PRO A CD  1 
ATOM   1698  N N   . LYS A 1 215 ? 28.756  -59.219 -14.089  1.00 63.49  ? 216 LYS A N   1 
ATOM   1699  C CA  . LYS A 1 215 ? 27.341  -59.494 -14.323  1.00 52.48  ? 216 LYS A CA  1 
ATOM   1700  C C   . LYS A 1 215 ? 27.222  -60.916 -14.866  1.00 46.57  ? 216 LYS A C   1 
ATOM   1701  O O   . LYS A 1 215 ? 27.339  -61.149 -16.070  1.00 70.90  ? 216 LYS A O   1 
ATOM   1702  C CB  . LYS A 1 215 ? 26.729  -58.475 -15.284  1.00 41.08  ? 216 LYS A CB  1 
ATOM   1703  C CG  . LYS A 1 215 ? 26.387  -57.141 -14.639  1.00 54.62  ? 216 LYS A CG  1 
ATOM   1704  C CD  . LYS A 1 215 ? 25.798  -56.161 -15.644  1.00 40.86  ? 216 LYS A CD  1 
ATOM   1705  C CE  . LYS A 1 215 ? 26.840  -55.706 -16.651  1.00 52.68  ? 216 LYS A CE  1 
ATOM   1706  N NZ  . LYS A 1 215 ? 26.318  -54.639 -17.551  1.00 63.63  ? 216 LYS A NZ  1 
ATOM   1707  N N   . ILE A 1 216 ? 26.993  -61.870 -13.966  1.00 62.29  ? 217 ILE A N   1 
ATOM   1708  C CA  . ILE A 1 216 ? 26.745  -63.246 -14.381  1.00 55.71  ? 217 ILE A CA  1 
ATOM   1709  C C   . ILE A 1 216 ? 25.347  -63.318 -14.977  1.00 67.83  ? 217 ILE A C   1 
ATOM   1710  O O   . ILE A 1 216 ? 24.360  -62.948 -14.329  1.00 87.32  ? 217 ILE A O   1 
ATOM   1711  C CB  . ILE A 1 216 ? 26.910  -64.219 -13.205  1.00 61.87  ? 217 ILE A CB  1 
ATOM   1712  C CG1 . ILE A 1 216 ? 28.372  -64.655 -13.067  1.00 66.10  ? 217 ILE A CG1 1 
ATOM   1713  C CG2 . ILE A 1 216 ? 26.019  -65.443 -13.379  1.00 73.09  ? 217 ILE A CG2 1 
ATOM   1714  C CD1 . ILE A 1 216 ? 29.296  -63.578 -12.533  1.00 69.33  ? 217 ILE A CD1 1 
ATOM   1715  N N   . ALA A 1 217 ? 25.260  -63.771 -16.225  1.00 76.80  ? 218 ALA A N   1 
ATOM   1716  C CA  . ALA A 1 217 ? 23.983  -63.865 -16.918  1.00 64.45  ? 218 ALA A CA  1 
ATOM   1717  C C   . ALA A 1 217 ? 24.157  -64.751 -18.141  1.00 64.89  ? 218 ALA A C   1 
ATOM   1718  O O   . ALA A 1 217 ? 25.261  -64.891 -18.676  1.00 72.58  ? 218 ALA A O   1 
ATOM   1719  C CB  . ALA A 1 217 ? 23.454  -62.485 -17.324  1.00 50.54  ? 218 ALA A CB  1 
ATOM   1720  N N   . THR A 1 218 ? 23.048  -65.344 -18.578  1.00 72.58  ? 219 THR A N   1 
ATOM   1721  C CA  . THR A 1 218 ? 23.041  -66.136 -19.799  1.00 63.55  ? 219 THR A CA  1 
ATOM   1722  C C   . THR A 1 218 ? 22.977  -65.211 -21.007  1.00 62.35  ? 219 THR A C   1 
ATOM   1723  O O   . THR A 1 218 ? 22.103  -64.342 -21.089  1.00 65.16  ? 219 THR A O   1 
ATOM   1724  C CB  . THR A 1 218 ? 21.857  -67.102 -19.807  1.00 58.88  ? 219 THR A CB  1 
ATOM   1725  O OG1 . THR A 1 218 ? 22.037  -68.090 -18.785  1.00 62.47  ? 219 THR A OG1 1 
ATOM   1726  C CG2 . THR A 1 218 ? 21.739  -67.789 -21.159  1.00 60.47  ? 219 THR A CG2 1 
ATOM   1727  N N   . ARG A 1 219 ? 23.910  -65.394 -21.936  1.00 54.74  ? 220 ARG A N   1 
ATOM   1728  C CA  . ARG A 1 219 ? 24.022  -64.558 -23.120  1.00 54.94  ? 220 ARG A CA  1 
ATOM   1729  C C   . ARG A 1 219 ? 24.190  -65.440 -24.349  1.00 60.73  ? 220 ARG A C   1 
ATOM   1730  O O   . ARG A 1 219 ? 24.461  -66.640 -24.252  1.00 55.97  ? 220 ARG A O   1 
ATOM   1731  C CB  . ARG A 1 219 ? 25.195  -63.575 -22.998  1.00 57.18  ? 220 ARG A CB  1 
ATOM   1732  C CG  . ARG A 1 219 ? 25.026  -62.542 -21.895  1.00 47.50  ? 220 ARG A CG  1 
ATOM   1733  C CD  . ARG A 1 219 ? 26.340  -61.845 -21.597  1.00 51.63  ? 220 ARG A CD  1 
ATOM   1734  N NE  . ARG A 1 219 ? 27.301  -62.747 -20.972  1.00 49.71  ? 220 ARG A NE  1 
ATOM   1735  C CZ  . ARG A 1 219 ? 27.543  -62.797 -19.669  1.00 58.17  ? 220 ARG A CZ  1 
ATOM   1736  N NH1 . ARG A 1 219 ? 26.925  -61.993 -18.820  1.00 48.23  ? 220 ARG A NH1 1 
ATOM   1737  N NH2 . ARG A 1 219 ? 28.430  -63.674 -19.207  1.00 56.26  ? 220 ARG A NH2 1 
ATOM   1738  N N   . SER A 1 220 ? 24.016  -64.830 -25.518  1.00 47.28  ? 221 SER A N   1 
ATOM   1739  C CA  . SER A 1 220 ? 24.191  -65.538 -26.777  1.00 54.43  ? 221 SER A CA  1 
ATOM   1740  C C   . SER A 1 220 ? 25.671  -65.644 -27.126  1.00 60.75  ? 221 SER A C   1 
ATOM   1741  O O   . SER A 1 220 ? 26.467  -64.749 -26.829  1.00 67.64  ? 221 SER A O   1 
ATOM   1742  C CB  . SER A 1 220 ? 23.435  -64.829 -27.901  1.00 59.49  ? 221 SER A CB  1 
ATOM   1743  O OG  . SER A 1 220 ? 22.047  -64.764 -27.621  1.00 74.49  ? 221 SER A OG  1 
ATOM   1744  N N   . GLN A 1 221 ? 26.038  -66.757 -27.759  1.00 66.92  ? 222 GLN A N   1 
ATOM   1745  C CA  . GLN A 1 221 ? 27.430  -66.979 -28.126  1.00 61.82  ? 222 GLN A CA  1 
ATOM   1746  C C   . GLN A 1 221 ? 27.873  -65.986 -29.194  1.00 61.31  ? 222 GLN A C   1 
ATOM   1747  O O   . GLN A 1 221 ? 27.196  -65.805 -30.210  1.00 62.13  ? 222 GLN A O   1 
ATOM   1748  C CB  . GLN A 1 221 ? 27.630  -68.409 -28.626  1.00 56.26  ? 222 GLN A CB  1 
ATOM   1749  C CG  . GLN A 1 221 ? 28.078  -69.386 -27.552  1.00 87.28  ? 222 GLN A CG  1 
ATOM   1750  C CD  . GLN A 1 221 ? 28.133  -70.816 -28.050  1.00 93.98  ? 222 GLN A CD  1 
ATOM   1751  O OE1 . GLN A 1 221 ? 28.154  -71.065 -29.256  1.00 80.25  ? 222 GLN A OE1 1 
ATOM   1752  N NE2 . GLN A 1 221 ? 28.149  -71.767 -27.122  1.00 101.83 ? 222 GLN A NE2 1 
ATOM   1753  N N   . VAL A 1 222 ? 29.012  -65.342 -28.957  1.00 52.36  ? 223 VAL A N   1 
ATOM   1754  C CA  . VAL A 1 222 ? 29.666  -64.487 -29.939  1.00 44.00  ? 223 VAL A CA  1 
ATOM   1755  C C   . VAL A 1 222 ? 31.119  -64.926 -30.033  1.00 63.69  ? 223 VAL A C   1 
ATOM   1756  O O   . VAL A 1 222 ? 31.816  -64.988 -29.014  1.00 54.41  ? 223 VAL A O   1 
ATOM   1757  C CB  . VAL A 1 222 ? 29.569  -62.995 -29.568  1.00 51.08  ? 223 VAL A CB  1 
ATOM   1758  C CG1 . VAL A 1 222 ? 30.321  -62.146 -30.583  1.00 48.81  ? 223 VAL A CG1 1 
ATOM   1759  C CG2 . VAL A 1 222 ? 28.116  -62.563 -29.481  1.00 52.72  ? 223 VAL A CG2 1 
ATOM   1760  N N   . ASN A 1 223 ? 31.568  -65.232 -31.250  1.00 51.20  ? 224 ASN A N   1 
ATOM   1761  C CA  . ASN A 1 223 ? 32.887  -65.825 -31.475  1.00 45.44  ? 224 ASN A CA  1 
ATOM   1762  C C   . ASN A 1 223 ? 33.064  -67.088 -30.634  1.00 53.19  ? 224 ASN A C   1 
ATOM   1763  O O   . ASN A 1 223 ? 34.155  -67.396 -30.150  1.00 53.26  ? 224 ASN A O   1 
ATOM   1764  C CB  . ASN A 1 223 ? 34.005  -64.815 -31.202  1.00 42.31  ? 224 ASN A CB  1 
ATOM   1765  C CG  . ASN A 1 223 ? 33.954  -63.621 -32.138  1.00 56.38  ? 224 ASN A CG  1 
ATOM   1766  O OD1 . ASN A 1 223 ? 33.213  -63.621 -33.121  1.00 65.49  ? 224 ASN A OD1 1 
ATOM   1767  N ND2 . ASN A 1 223 ? 34.752  -62.602 -31.843  1.00 68.40  ? 224 ASN A ND2 1 
ATOM   1768  N N   . GLY A 1 224 ? 31.966  -67.822 -30.454  1.00 53.83  ? 225 GLY A N   1 
ATOM   1769  C CA  . GLY A 1 224 ? 31.982  -69.094 -29.763  1.00 46.46  ? 225 GLY A CA  1 
ATOM   1770  C C   . GLY A 1 224 ? 31.903  -69.035 -28.254  1.00 63.31  ? 225 GLY A C   1 
ATOM   1771  O O   . GLY A 1 224 ? 32.082  -70.073 -27.606  1.00 66.31  ? 225 GLY A O   1 
ATOM   1772  N N   . LEU A 1 225 ? 31.640  -67.868 -27.666  1.00 67.51  ? 226 LEU A N   1 
ATOM   1773  C CA  . LEU A 1 225 ? 31.678  -67.724 -26.216  1.00 68.11  ? 226 LEU A CA  1 
ATOM   1774  C C   . LEU A 1 225 ? 30.522  -66.871 -25.718  1.00 47.44  ? 226 LEU A C   1 
ATOM   1775  O O   . LEU A 1 225 ? 30.211  -65.824 -26.295  1.00 51.21  ? 226 LEU A O   1 
ATOM   1776  C CB  . LEU A 1 225 ? 33.000  -67.103 -25.761  1.00 55.72  ? 226 LEU A CB  1 
ATOM   1777  C CG  . LEU A 1 225 ? 34.224  -67.979 -25.998  1.00 55.28  ? 226 LEU A CG  1 
ATOM   1778  C CD1 . LEU A 1 225 ? 35.461  -67.156 -25.818  1.00 69.41  ? 226 LEU A CD1 1 
ATOM   1779  C CD2 . LEU A 1 225 ? 34.214  -69.146 -25.037  1.00 50.35  ? 226 LEU A CD2 1 
ATOM   1780  N N   . ARG A 1 226 ? 29.899  -67.325 -24.628  1.00 49.07  ? 227 ARG A N   1 
ATOM   1781  C CA  . ARG A 1 226 ? 28.853  -66.557 -23.966  1.00 55.15  ? 227 ARG A CA  1 
ATOM   1782  C C   . ARG A 1 226 ? 29.412  -65.517 -23.006  1.00 51.10  ? 227 ARG A C   1 
ATOM   1783  O O   . ARG A 1 226 ? 28.691  -64.584 -22.638  1.00 53.61  ? 227 ARG A O   1 
ATOM   1784  C CB  . ARG A 1 226 ? 27.908  -67.499 -23.216  1.00 55.41  ? 227 ARG A CB  1 
ATOM   1785  C CG  . ARG A 1 226 ? 27.445  -68.678 -24.053  1.00 60.58  ? 227 ARG A CG  1 
ATOM   1786  C CD  . ARG A 1 226 ? 26.177  -69.304 -23.501  1.00 50.15  ? 227 ARG A CD  1 
ATOM   1787  N NE  . ARG A 1 226 ? 25.169  -69.453 -24.544  1.00 94.98  ? 227 ARG A NE  1 
ATOM   1788  C CZ  . ARG A 1 226 ? 25.017  -70.538 -25.290  1.00 111.78 ? 227 ARG A CZ  1 
ATOM   1789  N NH1 . ARG A 1 226 ? 25.778  -71.607 -25.117  1.00 101.50 ? 227 ARG A NH1 1 
ATOM   1790  N NH2 . ARG A 1 226 ? 24.080  -70.552 -26.233  1.00 99.88  ? 227 ARG A NH2 1 
ATOM   1791  N N   . GLY A 1 227 ? 30.672  -65.656 -22.594  1.00 50.37  ? 228 GLY A N   1 
ATOM   1792  C CA  . GLY A 1 227 ? 31.276  -64.674 -21.719  1.00 40.77  ? 228 GLY A CA  1 
ATOM   1793  C C   . GLY A 1 227 ? 31.557  -63.368 -22.436  1.00 45.80  ? 228 GLY A C   1 
ATOM   1794  O O   . GLY A 1 227 ? 31.557  -63.282 -23.664  1.00 45.40  ? 228 GLY A O   1 
ATOM   1795  N N   . ARG A 1 228 ? 31.800  -62.326 -21.643  1.00 42.59  ? 229 ARG A N   1 
ATOM   1796  C CA  . ARG A 1 228 ? 32.024  -60.990 -22.173  1.00 49.51  ? 229 ARG A CA  1 
ATOM   1797  C C   . ARG A 1 228 ? 33.166  -60.325 -21.418  1.00 43.01  ? 229 ARG A C   1 
ATOM   1798  O O   . ARG A 1 228 ? 33.478  -60.681 -20.279  1.00 54.40  ? 229 ARG A O   1 
ATOM   1799  C CB  . ARG A 1 228 ? 30.761  -60.120 -22.075  1.00 39.58  ? 229 ARG A CB  1 
ATOM   1800  C CG  . ARG A 1 228 ? 29.556  -60.647 -22.843  1.00 38.13  ? 229 ARG A CG  1 
ATOM   1801  C CD  . ARG A 1 228 ? 29.775  -60.608 -24.348  1.00 44.77  ? 229 ARG A CD  1 
ATOM   1802  N NE  . ARG A 1 228 ? 28.587  -61.041 -25.075  1.00 55.72  ? 229 ARG A NE  1 
ATOM   1803  C CZ  . ARG A 1 228 ? 28.359  -62.289 -25.464  1.00 60.72  ? 229 ARG A CZ  1 
ATOM   1804  N NH1 . ARG A 1 228 ? 29.228  -63.258 -25.226  1.00 55.73  ? 229 ARG A NH1 1 
ATOM   1805  N NH2 . ARG A 1 228 ? 27.230  -62.571 -26.108  1.00 62.14  ? 229 ARG A NH2 1 
ATOM   1806  N N   . MET A 1 229 ? 33.789  -59.347 -22.072  1.00 42.05  ? 230 MET A N   1 
ATOM   1807  C CA  . MET A 1 229 ? 34.824  -58.524 -21.451  1.00 47.89  ? 230 MET A CA  1 
ATOM   1808  C C   . MET A 1 229 ? 34.576  -57.068 -21.809  1.00 51.42  ? 230 MET A C   1 
ATOM   1809  O O   . MET A 1 229 ? 34.559  -56.711 -22.990  1.00 54.78  ? 230 MET A O   1 
ATOM   1810  C CB  . MET A 1 229 ? 36.226  -58.951 -21.894  1.00 43.53  ? 230 MET A CB  1 
ATOM   1811  C CG  . MET A 1 229 ? 36.669  -60.289 -21.337  1.00 54.11  ? 230 MET A CG  1 
ATOM   1812  S SD  . MET A 1 229 ? 38.425  -60.595 -21.597  1.00 65.98  ? 230 MET A SD  1 
ATOM   1813  C CE  . MET A 1 229 ? 38.584  -62.209 -20.842  1.00 58.87  ? 230 MET A CE  1 
ATOM   1814  N N   . ASP A 1 230 ? 34.393  -56.233 -20.791  1.00 51.06  ? 231 ASP A N   1 
ATOM   1815  C CA  . ASP A 1 230 ? 34.212  -54.800 -20.972  1.00 57.23  ? 231 ASP A CA  1 
ATOM   1816  C C   . ASP A 1 230 ? 35.519  -54.097 -20.630  1.00 52.42  ? 231 ASP A C   1 
ATOM   1817  O O   . ASP A 1 230 ? 36.004  -54.200 -19.498  1.00 52.77  ? 231 ASP A O   1 
ATOM   1818  C CB  . ASP A 1 230 ? 33.073  -54.280 -20.099  1.00 60.07  ? 231 ASP A CB  1 
ATOM   1819  C CG  . ASP A 1 230 ? 31.731  -54.860 -20.491  1.00 61.43  ? 231 ASP A CG  1 
ATOM   1820  O OD1 . ASP A 1 230 ? 31.535  -55.140 -21.692  1.00 62.36  ? 231 ASP A OD1 1 
ATOM   1821  O OD2 . ASP A 1 230 ? 30.873  -55.039 -19.601  1.00 76.22  ? 231 ASP A OD2 1 
ATOM   1822  N N   . PHE A 1 231 ? 36.083  -53.392 -21.603  1.00 40.58  ? 232 PHE A N   1 
ATOM   1823  C CA  . PHE A 1 231 ? 37.355  -52.711 -21.432  1.00 56.76  ? 232 PHE A CA  1 
ATOM   1824  C C   . PHE A 1 231 ? 37.143  -51.219 -21.206  1.00 56.91  ? 232 PHE A C   1 
ATOM   1825  O O   . PHE A 1 231 ? 36.208  -50.615 -21.737  1.00 52.52  ? 232 PHE A O   1 
ATOM   1826  C CB  . PHE A 1 231 ? 38.259  -52.937 -22.645  1.00 50.06  ? 232 PHE A CB  1 
ATOM   1827  C CG  . PHE A 1 231 ? 38.795  -54.336 -22.745  1.00 52.26  ? 232 PHE A CG  1 
ATOM   1828  C CD1 . PHE A 1 231 ? 39.948  -54.701 -22.066  1.00 51.93  ? 232 PHE A CD1 1 
ATOM   1829  C CD2 . PHE A 1 231 ? 38.145  -55.289 -23.512  1.00 45.58  ? 232 PHE A CD2 1 
ATOM   1830  C CE1 . PHE A 1 231 ? 40.444  -55.989 -22.154  1.00 54.36  ? 232 PHE A CE1 1 
ATOM   1831  C CE2 . PHE A 1 231 ? 38.637  -56.578 -23.604  1.00 58.78  ? 232 PHE A CE2 1 
ATOM   1832  C CZ  . PHE A 1 231 ? 39.788  -56.929 -22.923  1.00 62.50  ? 232 PHE A CZ  1 
ATOM   1833  N N   . PHE A 1 232 ? 38.029  -50.634 -20.405  1.00 42.34  ? 233 PHE A N   1 
ATOM   1834  C CA  . PHE A 1 232 ? 37.950  -49.233 -20.024  1.00 53.80  ? 233 PHE A CA  1 
ATOM   1835  C C   . PHE A 1 232 ? 39.322  -48.596 -20.187  1.00 52.13  ? 233 PHE A C   1 
ATOM   1836  O O   . PHE A 1 232 ? 40.346  -49.282 -20.215  1.00 59.34  ? 233 PHE A O   1 
ATOM   1837  C CB  . PHE A 1 232 ? 37.457  -49.068 -18.578  1.00 47.81  ? 233 PHE A CB  1 
ATOM   1838  C CG  . PHE A 1 232 ? 36.080  -49.621 -18.338  1.00 50.98  ? 233 PHE A CG  1 
ATOM   1839  C CD1 . PHE A 1 232 ? 35.892  -50.971 -18.084  1.00 44.87  ? 233 PHE A CD1 1 
ATOM   1840  C CD2 . PHE A 1 232 ? 34.974  -48.790 -18.362  1.00 52.63  ? 233 PHE A CD2 1 
ATOM   1841  C CE1 . PHE A 1 232 ? 34.626  -51.479 -17.864  1.00 52.23  ? 233 PHE A CE1 1 
ATOM   1842  C CE2 . PHE A 1 232 ? 33.706  -49.292 -18.143  1.00 46.53  ? 233 PHE A CE2 1 
ATOM   1843  C CZ  . PHE A 1 232 ? 33.532  -50.637 -17.893  1.00 42.47  ? 233 PHE A CZ  1 
ATOM   1844  N N   . TRP A 1 233 ? 39.334  -47.270 -20.301  1.00 50.10  ? 234 TRP A N   1 
ATOM   1845  C CA  . TRP A 1 233 ? 40.577  -46.538 -20.485  1.00 45.17  ? 234 TRP A CA  1 
ATOM   1846  C C   . TRP A 1 233 ? 40.540  -45.236 -19.699  1.00 56.63  ? 234 TRP A C   1 
ATOM   1847  O O   . TRP A 1 233 ? 39.475  -44.709 -19.366  1.00 59.27  ? 234 TRP A O   1 
ATOM   1848  C CB  . TRP A 1 233 ? 40.851  -46.246 -21.967  1.00 43.65  ? 234 TRP A CB  1 
ATOM   1849  C CG  . TRP A 1 233 ? 39.779  -45.444 -22.643  1.00 48.59  ? 234 TRP A CG  1 
ATOM   1850  C CD1 . TRP A 1 233 ? 38.617  -45.919 -23.173  1.00 59.99  ? 234 TRP A CD1 1 
ATOM   1851  C CD2 . TRP A 1 233 ? 39.777  -44.029 -22.875  1.00 56.53  ? 234 TRP A CD2 1 
ATOM   1852  N NE1 . TRP A 1 233 ? 37.887  -44.889 -23.715  1.00 50.33  ? 234 TRP A NE1 1 
ATOM   1853  C CE2 . TRP A 1 233 ? 38.577  -43.719 -23.546  1.00 56.65  ? 234 TRP A CE2 1 
ATOM   1854  C CE3 . TRP A 1 233 ? 40.671  -42.995 -22.579  1.00 52.64  ? 234 TRP A CE3 1 
ATOM   1855  C CZ2 . TRP A 1 233 ? 38.247  -42.419 -23.925  1.00 46.75  ? 234 TRP A CZ2 1 
ATOM   1856  C CZ3 . TRP A 1 233 ? 40.341  -41.703 -22.958  1.00 54.30  ? 234 TRP A CZ3 1 
ATOM   1857  C CH2 . TRP A 1 233 ? 39.139  -41.427 -23.623  1.00 39.53  ? 234 TRP A CH2 1 
ATOM   1858  N N   . THR A 1 234 ? 41.733  -44.729 -19.401  1.00 61.19  ? 235 THR A N   1 
ATOM   1859  C CA  . THR A 1 234 ? 41.901  -43.414 -18.803  1.00 46.99  ? 235 THR A CA  1 
ATOM   1860  C C   . THR A 1 234 ? 43.226  -42.841 -19.281  1.00 57.27  ? 235 THR A C   1 
ATOM   1861  O O   . THR A 1 234 ? 44.130  -43.574 -19.690  1.00 61.86  ? 235 THR A O   1 
ATOM   1862  C CB  . THR A 1 234 ? 41.862  -43.469 -17.270  1.00 59.91  ? 235 THR A CB  1 
ATOM   1863  O OG1 . THR A 1 234 ? 41.905  -42.137 -16.742  1.00 64.69  ? 235 THR A OG1 1 
ATOM   1864  C CG2 . THR A 1 234 ? 43.050  -44.254 -16.731  1.00 58.23  ? 235 THR A CG2 1 
ATOM   1865  N N   . ILE A 1 235 ? 43.329  -41.518 -19.236  1.00 59.60  ? 236 ILE A N   1 
ATOM   1866  C CA  . ILE A 1 235 ? 44.564  -40.815 -19.558  1.00 58.22  ? 236 ILE A CA  1 
ATOM   1867  C C   . ILE A 1 235 ? 45.215  -40.424 -18.239  1.00 62.69  ? 236 ILE A C   1 
ATOM   1868  O O   . ILE A 1 235 ? 44.679  -39.599 -17.492  1.00 63.81  ? 236 ILE A O   1 
ATOM   1869  C CB  . ILE A 1 235 ? 44.307  -39.586 -20.441  1.00 58.60  ? 236 ILE A CB  1 
ATOM   1870  C CG1 . ILE A 1 235 ? 43.684  -39.999 -21.777  1.00 58.37  ? 236 ILE A CG1 1 
ATOM   1871  C CG2 . ILE A 1 235 ? 45.598  -38.820 -20.673  1.00 50.53  ? 236 ILE A CG2 1 
ATOM   1872  C CD1 . ILE A 1 235 ? 44.662  -40.628 -22.748  1.00 54.00  ? 236 ILE A CD1 1 
ATOM   1873  N N   . LEU A 1 236 ? 46.370  -41.015 -17.947  1.00 72.58  ? 237 LEU A N   1 
ATOM   1874  C CA  . LEU A 1 236 ? 47.071  -40.767 -16.693  1.00 58.86  ? 237 LEU A CA  1 
ATOM   1875  C C   . LEU A 1 236 ? 48.042  -39.610 -16.885  1.00 66.11  ? 237 LEU A C   1 
ATOM   1876  O O   . LEU A 1 236 ? 48.996  -39.715 -17.664  1.00 66.08  ? 237 LEU A O   1 
ATOM   1877  C CB  . LEU A 1 236 ? 47.808  -42.021 -16.226  1.00 46.24  ? 237 LEU A CB  1 
ATOM   1878  C CG  . LEU A 1 236 ? 48.384  -41.980 -14.808  1.00 62.35  ? 237 LEU A CG  1 
ATOM   1879  C CD1 . LEU A 1 236 ? 47.270  -41.871 -13.776  1.00 63.85  ? 237 LEU A CD1 1 
ATOM   1880  C CD2 . LEU A 1 236 ? 49.250  -43.201 -14.540  1.00 58.20  ? 237 LEU A CD2 1 
ATOM   1881  N N   . LYS A 1 237 ? 47.798  -38.512 -16.175  1.00 58.06  ? 238 LYS A N   1 
ATOM   1882  C CA  . LYS A 1 237 ? 48.645  -37.339 -16.279  1.00 61.97  ? 238 LYS A CA  1 
ATOM   1883  C C   . LYS A 1 237 ? 49.983  -37.585 -15.586  1.00 66.82  ? 238 LYS A C   1 
ATOM   1884  O O   . LYS A 1 237 ? 50.091  -38.449 -14.713  1.00 68.23  ? 238 LYS A O   1 
ATOM   1885  C CB  . LYS A 1 237 ? 47.940  -36.129 -15.672  1.00 54.92  ? 238 LYS A CB  1 
ATOM   1886  C CG  . LYS A 1 237 ? 47.422  -35.148 -16.708  1.00 72.36  ? 238 LYS A CG  1 
ATOM   1887  C CD  . LYS A 1 237 ? 46.320  -34.262 -16.158  1.00 69.84  ? 238 LYS A CD  1 
ATOM   1888  C CE  . LYS A 1 237 ? 45.945  -33.187 -17.168  1.00 84.28  ? 238 LYS A CE  1 
ATOM   1889  N NZ  . LYS A 1 237 ? 44.600  -32.602 -16.897  1.00 97.52  ? 238 LYS A NZ  1 
ATOM   1890  N N   . PRO A 1 238 ? 51.026  -36.849 -15.977  1.00 58.63  ? 239 PRO A N   1 
ATOM   1891  C CA  . PRO A 1 238 ? 52.329  -37.014 -15.322  1.00 52.63  ? 239 PRO A CA  1 
ATOM   1892  C C   . PRO A 1 238 ? 52.245  -36.696 -13.838  1.00 61.80  ? 239 PRO A C   1 
ATOM   1893  O O   . PRO A 1 238 ? 51.481  -35.829 -13.409  1.00 78.01  ? 239 PRO A O   1 
ATOM   1894  C CB  . PRO A 1 238 ? 53.228  -36.014 -16.061  1.00 55.67  ? 239 PRO A CB  1 
ATOM   1895  C CG  . PRO A 1 238 ? 52.559  -35.803 -17.376  1.00 58.89  ? 239 PRO A CG  1 
ATOM   1896  C CD  . PRO A 1 238 ? 51.091  -35.895 -17.098  1.00 62.33  ? 239 PRO A CD  1 
ATOM   1897  N N   . ASN A 1 239 ? 53.030  -37.434 -13.053  1.00 60.26  ? 240 ASN A N   1 
ATOM   1898  C CA  . ASN A 1 239 ? 53.135  -37.339 -11.598  1.00 54.44  ? 240 ASN A CA  1 
ATOM   1899  C C   . ASN A 1 239 ? 51.885  -37.838 -10.884  1.00 56.62  ? 240 ASN A C   1 
ATOM   1900  O O   . ASN A 1 239 ? 51.841  -37.802 -9.647   1.00 65.92  ? 240 ASN A O   1 
ATOM   1901  C CB  . ASN A 1 239 ? 53.446  -35.911 -11.125  1.00 57.79  ? 240 ASN A CB  1 
ATOM   1902  C CG  . ASN A 1 239 ? 54.561  -35.265 -11.923  1.00 65.81  ? 240 ASN A CG  1 
ATOM   1903  O OD1 . ASN A 1 239 ? 55.523  -35.925 -12.315  1.00 67.14  ? 240 ASN A OD1 1 
ATOM   1904  N ND2 . ASN A 1 239 ? 54.429  -33.969 -12.181  1.00 65.41  ? 240 ASN A ND2 1 
ATOM   1905  N N   . ASP A 1 240 ? 50.873  -38.303 -11.611  1.00 59.28  ? 241 ASP A N   1 
ATOM   1906  C CA  . ASP A 1 240 ? 49.678  -38.885 -11.019  1.00 54.64  ? 241 ASP A CA  1 
ATOM   1907  C C   . ASP A 1 240 ? 49.793  -40.404 -11.016  1.00 54.67  ? 241 ASP A C   1 
ATOM   1908  O O   . ASP A 1 240 ? 50.493  -40.995 -11.843  1.00 55.99  ? 241 ASP A O   1 
ATOM   1909  C CB  . ASP A 1 240 ? 48.419  -38.459 -11.779  1.00 64.78  ? 241 ASP A CB  1 
ATOM   1910  C CG  . ASP A 1 240 ? 47.143  -38.816 -11.038  1.00 91.33  ? 241 ASP A CG  1 
ATOM   1911  O OD1 . ASP A 1 240 ? 47.204  -39.005 -9.804   1.00 67.14  ? 241 ASP A OD1 1 
ATOM   1912  O OD2 . ASP A 1 240 ? 46.083  -38.917 -11.692  1.00 79.07  ? 241 ASP A OD2 1 
ATOM   1913  N N   . ALA A 1 241 ? 49.100  -41.032 -10.072  1.00 48.76  ? 242 ALA A N   1 
ATOM   1914  C CA  . ALA A 1 241 ? 49.133  -42.477 -9.910   1.00 56.98  ? 242 ALA A CA  1 
ATOM   1915  C C   . ALA A 1 241 ? 47.750  -43.069 -10.143  1.00 53.15  ? 242 ALA A C   1 
ATOM   1916  O O   . ALA A 1 241 ? 46.728  -42.408 -9.935   1.00 58.87  ? 242 ALA A O   1 
ATOM   1917  C CB  . ALA A 1 241 ? 49.636  -42.868 -8.516   1.00 44.45  ? 242 ALA A CB  1 
ATOM   1918  N N   . ILE A 1 242 ? 47.730  -44.322 -10.586  1.00 40.61  ? 243 ILE A N   1 
ATOM   1919  C CA  . ILE A 1 242 ? 46.501  -45.087 -10.745  1.00 48.17  ? 243 ILE A CA  1 
ATOM   1920  C C   . ILE A 1 242 ? 46.554  -46.263 -9.779   1.00 52.80  ? 243 ILE A C   1 
ATOM   1921  O O   . ILE A 1 242 ? 47.587  -46.932 -9.662   1.00 54.19  ? 243 ILE A O   1 
ATOM   1922  C CB  . ILE A 1 242 ? 46.298  -45.554 -12.198  1.00 50.35  ? 243 ILE A CB  1 
ATOM   1923  C CG1 . ILE A 1 242 ? 44.986  -46.331 -12.327  1.00 55.19  ? 243 ILE A CG1 1 
ATOM   1924  C CG2 . ILE A 1 242 ? 47.486  -46.379 -12.686  1.00 55.24  ? 243 ILE A CG2 1 
ATOM   1925  C CD1 . ILE A 1 242 ? 44.468  -46.414 -13.745  1.00 43.13  ? 243 ILE A CD1 1 
ATOM   1926  N N   . HIS A 1 243 ? 45.456  -46.491 -9.064   1.00 56.72  ? 244 HIS A N   1 
ATOM   1927  C CA  . HIS A 1 243 ? 45.398  -47.505 -8.020   1.00 40.33  ? 244 HIS A CA  1 
ATOM   1928  C C   . HIS A 1 243 ? 44.372  -48.560 -8.408   1.00 44.77  ? 244 HIS A C   1 
ATOM   1929  O O   . HIS A 1 243 ? 43.205  -48.236 -8.653   1.00 44.20  ? 244 HIS A O   1 
ATOM   1930  C CB  . HIS A 1 243 ? 45.048  -46.874 -6.669   1.00 45.86  ? 244 HIS A CB  1 
ATOM   1931  C CG  . HIS A 1 243 ? 45.953  -45.745 -6.278   1.00 56.23  ? 244 HIS A CG  1 
ATOM   1932  N ND1 . HIS A 1 243 ? 47.010  -45.904 -5.408   1.00 56.00  ? 244 HIS A ND1 1 
ATOM   1933  C CD2 . HIS A 1 243 ? 45.957  -44.439 -6.639   1.00 56.06  ? 244 HIS A CD2 1 
ATOM   1934  C CE1 . HIS A 1 243 ? 47.627  -44.746 -5.251   1.00 68.07  ? 244 HIS A CE1 1 
ATOM   1935  N NE2 . HIS A 1 243 ? 47.009  -43.841 -5.987   1.00 68.93  ? 244 HIS A NE2 1 
ATOM   1936  N N   . PHE A 1 244 ? 44.808  -49.816 -8.458   1.00 51.96  ? 245 PHE A N   1 
ATOM   1937  C CA  . PHE A 1 244 ? 43.949  -50.946 -8.785   1.00 43.37  ? 245 PHE A CA  1 
ATOM   1938  C C   . PHE A 1 244 ? 43.751  -51.818 -7.554   1.00 38.17  ? 245 PHE A C   1 
ATOM   1939  O O   . PHE A 1 244 ? 44.704  -52.098 -6.820   1.00 58.76  ? 245 PHE A O   1 
ATOM   1940  C CB  . PHE A 1 244 ? 44.544  -51.796 -9.913   1.00 46.02  ? 245 PHE A CB  1 
ATOM   1941  C CG  . PHE A 1 244 ? 44.507  -51.138 -11.261  1.00 39.74  ? 245 PHE A CG  1 
ATOM   1942  C CD1 . PHE A 1 244 ? 43.347  -51.148 -12.018  1.00 46.96  ? 245 PHE A CD1 1 
ATOM   1943  C CD2 . PHE A 1 244 ? 45.638  -50.528 -11.780  1.00 43.74  ? 245 PHE A CD2 1 
ATOM   1944  C CE1 . PHE A 1 244 ? 43.308  -50.551 -13.265  1.00 41.44  ? 245 PHE A CE1 1 
ATOM   1945  C CE2 . PHE A 1 244 ? 45.607  -49.929 -13.027  1.00 46.04  ? 245 PHE A CE2 1 
ATOM   1946  C CZ  . PHE A 1 244 ? 44.440  -49.941 -13.770  1.00 38.46  ? 245 PHE A CZ  1 
ATOM   1947  N N   . GLU A 1 245 ? 42.508  -52.240 -7.329   1.00 43.54  ? 246 GLU A N   1 
ATOM   1948  C CA  . GLU A 1 245 ? 42.195  -53.233 -6.311   1.00 44.39  ? 246 GLU A CA  1 
ATOM   1949  C C   . GLU A 1 245 ? 41.112  -54.155 -6.845   1.00 58.91  ? 246 GLU A C   1 
ATOM   1950  O O   . GLU A 1 245 ? 40.075  -53.686 -7.322   1.00 60.07  ? 246 GLU A O   1 
ATOM   1951  C CB  . GLU A 1 245 ? 41.742  -52.582 -5.000   1.00 40.04  ? 246 GLU A CB  1 
ATOM   1952  C CG  . GLU A 1 245 ? 41.423  -53.584 -3.900   1.00 69.26  ? 246 GLU A CG  1 
ATOM   1953  C CD  . GLU A 1 245 ? 41.417  -52.960 -2.517   1.00 75.53  ? 246 GLU A CD  1 
ATOM   1954  O OE1 . GLU A 1 245 ? 42.395  -52.264 -2.175   1.00 97.59  ? 246 GLU A OE1 1 
ATOM   1955  O OE2 . GLU A 1 245 ? 40.434  -53.162 -1.773   1.00 76.40  ? 246 GLU A OE2 1 
ATOM   1956  N N   . SER A 1 246 ? 41.355  -55.462 -6.764   1.00 52.07  ? 247 SER A N   1 
ATOM   1957  C CA  . SER A 1 246 ? 40.412  -56.437 -7.291   1.00 50.82  ? 247 SER A CA  1 
ATOM   1958  C C   . SER A 1 246 ? 40.653  -57.784 -6.629   1.00 54.94  ? 247 SER A C   1 
ATOM   1959  O O   . SER A 1 246 ? 41.757  -58.071 -6.156   1.00 55.90  ? 247 SER A O   1 
ATOM   1960  C CB  . SER A 1 246 ? 40.538  -56.565 -8.814   1.00 56.37  ? 247 SER A CB  1 
ATOM   1961  O OG  . SER A 1 246 ? 39.728  -57.617 -9.306   1.00 61.37  ? 247 SER A OG  1 
ATOM   1962  N N   . ASN A 1 247 ? 39.600  -58.607 -6.605   1.00 54.01  ? 248 ASN A N   1 
ATOM   1963  C CA  . ASN A 1 247 ? 39.688  -59.977 -6.109   1.00 46.80  ? 248 ASN A CA  1 
ATOM   1964  C C   . ASN A 1 247 ? 39.128  -60.981 -7.114   1.00 60.85  ? 248 ASN A C   1 
ATOM   1965  O O   . ASN A 1 247 ? 38.703  -62.070 -6.719   1.00 61.98  ? 248 ASN A O   1 
ATOM   1966  C CB  . ASN A 1 247 ? 38.963  -60.121 -4.765   1.00 40.72  ? 248 ASN A CB  1 
ATOM   1967  C CG  . ASN A 1 247 ? 37.472  -59.894 -4.880   1.00 52.36  ? 248 ASN A CG  1 
ATOM   1968  O OD1 . ASN A 1 247 ? 37.013  -59.144 -5.739   1.00 63.54  ? 248 ASN A OD1 1 
ATOM   1969  N ND2 . ASN A 1 247 ? 36.704  -60.543 -4.011   1.00 39.22  ? 248 ASN A ND2 1 
ATOM   1970  N N   . GLY A 1 248 ? 39.119  -60.643 -8.393   1.00 54.74  ? 249 GLY A N   1 
ATOM   1971  C CA  . GLY A 1 248 ? 38.668  -61.552 -9.429   1.00 52.68  ? 249 GLY A CA  1 
ATOM   1972  C C   . GLY A 1 248 ? 38.170  -60.806 -10.648  1.00 52.50  ? 249 GLY A C   1 
ATOM   1973  O O   . GLY A 1 248 ? 37.851  -59.617 -10.608  1.00 55.46  ? 249 GLY A O   1 
ATOM   1974  N N   . ASN A 1 249 ? 38.112  -61.532 -11.768  1.00 48.75  ? 250 ASN A N   1 
ATOM   1975  C CA  . ASN A 1 249 ? 37.556  -61.025 -13.029  1.00 43.91  ? 250 ASN A CA  1 
ATOM   1976  C C   . ASN A 1 249 ? 38.317  -59.808 -13.544  1.00 51.40  ? 250 ASN A C   1 
ATOM   1977  O O   . ASN A 1 249 ? 37.758  -58.973 -14.259  1.00 49.48  ? 250 ASN A O   1 
ATOM   1978  C CB  . ASN A 1 249 ? 36.064  -60.698 -12.885  1.00 45.69  ? 250 ASN A CB  1 
ATOM   1979  C CG  . ASN A 1 249 ? 35.282  -61.831 -12.248  1.00 48.71  ? 250 ASN A CG  1 
ATOM   1980  O OD1 . ASN A 1 249 ? 35.432  -62.111 -11.055  1.00 60.73  ? 250 ASN A OD1 1 
ATOM   1981  N ND2 . ASN A 1 249 ? 34.430  -62.474 -13.031  1.00 55.28  ? 250 ASN A ND2 1 
ATOM   1982  N N   . PHE A 1 250 ? 39.595  -59.697 -13.196  1.00 50.69  ? 251 PHE A N   1 
ATOM   1983  C CA  . PHE A 1 250 ? 40.399  -58.526 -13.522  1.00 48.19  ? 251 PHE A CA  1 
ATOM   1984  C C   . PHE A 1 250 ? 41.249  -58.808 -14.756  1.00 54.58  ? 251 PHE A C   1 
ATOM   1985  O O   . PHE A 1 250 ? 42.023  -59.772 -14.777  1.00 57.87  ? 251 PHE A O   1 
ATOM   1986  C CB  . PHE A 1 250 ? 41.289  -58.138 -12.341  1.00 48.56  ? 251 PHE A CB  1 
ATOM   1987  C CG  . PHE A 1 250 ? 42.055  -56.861 -12.549  1.00 47.48  ? 251 PHE A CG  1 
ATOM   1988  C CD1 . PHE A 1 250 ? 41.525  -55.834 -13.314  1.00 51.57  ? 251 PHE A CD1 1 
ATOM   1989  C CD2 . PHE A 1 250 ? 43.309  -56.692 -11.984  1.00 42.63  ? 251 PHE A CD2 1 
ATOM   1990  C CE1 . PHE A 1 250 ? 42.226  -54.658 -13.507  1.00 42.65  ? 251 PHE A CE1 1 
ATOM   1991  C CE2 . PHE A 1 250 ? 44.017  -55.518 -12.173  1.00 43.05  ? 251 PHE A CE2 1 
ATOM   1992  C CZ  . PHE A 1 250 ? 43.474  -54.499 -12.938  1.00 44.02  ? 251 PHE A CZ  1 
ATOM   1993  N N   . ILE A 1 251 ? 41.107  -57.967 -15.774  1.00 41.76  ? 252 ILE A N   1 
ATOM   1994  C CA  . ILE A 1 251 ? 41.959  -58.013 -16.959  1.00 47.09  ? 252 ILE A CA  1 
ATOM   1995  C C   . ILE A 1 251 ? 42.996  -56.913 -16.754  1.00 48.45  ? 252 ILE A C   1 
ATOM   1996  O O   . ILE A 1 251 ? 42.794  -55.755 -17.124  1.00 46.19  ? 252 ILE A O   1 
ATOM   1997  C CB  . ILE A 1 251 ? 41.160  -57.835 -18.248  1.00 43.81  ? 252 ILE A CB  1 
ATOM   1998  C CG1 . ILE A 1 251 ? 39.933  -58.750 -18.238  1.00 50.65  ? 252 ILE A CG1 1 
ATOM   1999  C CG2 . ILE A 1 251 ? 42.022  -58.147 -19.453  1.00 38.49  ? 252 ILE A CG2 1 
ATOM   2000  C CD1 . ILE A 1 251 ? 40.269  -60.225 -18.191  1.00 40.96  ? 252 ILE A CD1 1 
ATOM   2001  N N   . ALA A 1 252 ? 44.124  -57.285 -16.147  1.00 49.42  ? 253 ALA A N   1 
ATOM   2002  C CA  . ALA A 1 252 ? 45.121  -56.332 -15.674  1.00 46.28  ? 253 ALA A CA  1 
ATOM   2003  C C   . ALA A 1 252 ? 45.940  -55.772 -16.835  1.00 47.62  ? 253 ALA A C   1 
ATOM   2004  O O   . ALA A 1 252 ? 46.312  -56.512 -17.748  1.00 48.86  ? 253 ALA A O   1 
ATOM   2005  C CB  . ALA A 1 252 ? 46.054  -56.994 -14.666  1.00 41.71  ? 253 ALA A CB  1 
ATOM   2006  N N   . PRO A 1 253 ? 46.250  -54.477 -16.810  1.00 56.13  ? 254 PRO A N   1 
ATOM   2007  C CA  . PRO A 1 253 ? 47.113  -53.907 -17.849  1.00 59.07  ? 254 PRO A CA  1 
ATOM   2008  C C   . PRO A 1 253 ? 48.548  -54.390 -17.713  1.00 54.01  ? 254 PRO A C   1 
ATOM   2009  O O   . PRO A 1 253 ? 49.055  -54.603 -16.609  1.00 68.90  ? 254 PRO A O   1 
ATOM   2010  C CB  . PRO A 1 253 ? 47.013  -52.398 -17.599  1.00 49.14  ? 254 PRO A CB  1 
ATOM   2011  C CG  . PRO A 1 253 ? 46.734  -52.290 -16.142  1.00 51.31  ? 254 PRO A CG  1 
ATOM   2012  C CD  . PRO A 1 253 ? 45.854  -53.470 -15.811  1.00 54.70  ? 254 PRO A CD  1 
ATOM   2013  N N   . GLU A 1 254 ? 49.197  -54.562 -18.862  1.00 60.13  ? 255 GLU A N   1 
ATOM   2014  C CA  . GLU A 1 254 ? 50.630  -54.824 -18.925  1.00 60.07  ? 255 GLU A CA  1 
ATOM   2015  C C   . GLU A 1 254 ? 51.381  -53.743 -19.685  1.00 62.46  ? 255 GLU A C   1 
ATOM   2016  O O   . GLU A 1 254 ? 52.418  -53.262 -19.209  1.00 57.59  ? 255 GLU A O   1 
ATOM   2017  C CB  . GLU A 1 254 ? 50.898  -56.197 -19.566  1.00 56.19  ? 255 GLU A CB  1 
ATOM   2018  C CG  . GLU A 1 254 ? 52.315  -56.339 -20.093  1.00 74.67  ? 255 GLU A CG  1 
ATOM   2019  C CD  . GLU A 1 254 ? 52.939  -57.691 -19.804  1.00 88.08  ? 255 GLU A CD  1 
ATOM   2020  O OE1 . GLU A 1 254 ? 52.229  -58.713 -19.893  1.00 97.97  ? 255 GLU A OE1 1 
ATOM   2021  O OE2 . GLU A 1 254 ? 54.149  -57.727 -19.489  1.00 84.88  ? 255 GLU A OE2 1 
ATOM   2022  N N   . TYR A 1 255 ? 50.881  -53.334 -20.847  1.00 56.54  ? 256 TYR A N   1 
ATOM   2023  C CA  . TYR A 1 255 ? 51.486  -52.273 -21.635  1.00 55.82  ? 256 TYR A CA  1 
ATOM   2024  C C   . TYR A 1 255 ? 50.574  -51.054 -21.667  1.00 55.57  ? 256 TYR A C   1 
ATOM   2025  O O   . TYR A 1 255 ? 49.345  -51.172 -21.641  1.00 58.73  ? 256 TYR A O   1 
ATOM   2026  C CB  . TYR A 1 255 ? 51.772  -52.737 -23.067  1.00 56.69  ? 256 TYR A CB  1 
ATOM   2027  C CG  . TYR A 1 255 ? 52.870  -53.771 -23.179  1.00 74.17  ? 256 TYR A CG  1 
ATOM   2028  C CD1 . TYR A 1 255 ? 54.207  -53.395 -23.181  1.00 66.26  ? 256 TYR A CD1 1 
ATOM   2029  C CD2 . TYR A 1 255 ? 52.568  -55.122 -23.287  1.00 68.54  ? 256 TYR A CD2 1 
ATOM   2030  C CE1 . TYR A 1 255 ? 55.213  -54.337 -23.283  1.00 71.57  ? 256 TYR A CE1 1 
ATOM   2031  C CE2 . TYR A 1 255 ? 53.569  -56.072 -23.389  1.00 60.72  ? 256 TYR A CE2 1 
ATOM   2032  C CZ  . TYR A 1 255 ? 54.888  -55.672 -23.387  1.00 72.17  ? 256 TYR A CZ  1 
ATOM   2033  O OH  . TYR A 1 255 ? 55.891  -56.607 -23.489  1.00 76.47  ? 256 TYR A OH  1 
ATOM   2034  N N   . ALA A 1 256 ? 51.193  -49.877 -21.719  1.00 58.49  ? 257 ALA A N   1 
ATOM   2035  C CA  . ALA A 1 256 ? 50.494  -48.607 -21.855  1.00 45.18  ? 257 ALA A CA  1 
ATOM   2036  C C   . ALA A 1 256 ? 51.116  -47.832 -23.011  1.00 61.82  ? 257 ALA A C   1 
ATOM   2037  O O   . ALA A 1 256 ? 52.042  -48.306 -23.675  1.00 70.14  ? 257 ALA A O   1 
ATOM   2038  C CB  . ALA A 1 256 ? 50.548  -47.795 -20.554  1.00 49.21  ? 257 ALA A CB  1 
ATOM   2039  N N   . TYR A 1 257 ? 50.607  -46.626 -23.252  1.00 48.58  ? 258 TYR A N   1 
ATOM   2040  C CA  . TYR A 1 257 ? 51.023  -45.827 -24.398  1.00 55.45  ? 258 TYR A CA  1 
ATOM   2041  C C   . TYR A 1 257 ? 51.311  -44.401 -23.956  1.00 58.80  ? 258 TYR A C   1 
ATOM   2042  O O   . TYR A 1 257 ? 50.424  -43.722 -23.426  1.00 64.42  ? 258 TYR A O   1 
ATOM   2043  C CB  . TYR A 1 257 ? 49.950  -45.845 -25.491  1.00 55.41  ? 258 TYR A CB  1 
ATOM   2044  C CG  . TYR A 1 257 ? 49.651  -47.229 -26.017  1.00 63.13  ? 258 TYR A CG  1 
ATOM   2045  C CD1 . TYR A 1 257 ? 50.502  -47.846 -26.922  1.00 60.33  ? 258 TYR A CD1 1 
ATOM   2046  C CD2 . TYR A 1 257 ? 48.519  -47.921 -25.607  1.00 61.38  ? 258 TYR A CD2 1 
ATOM   2047  C CE1 . TYR A 1 257 ? 50.235  -49.111 -27.409  1.00 58.82  ? 258 TYR A CE1 1 
ATOM   2048  C CE2 . TYR A 1 257 ? 48.244  -49.188 -26.087  1.00 61.70  ? 258 TYR A CE2 1 
ATOM   2049  C CZ  . TYR A 1 257 ? 49.107  -49.778 -26.988  1.00 55.43  ? 258 TYR A CZ  1 
ATOM   2050  O OH  . TYR A 1 257 ? 48.841  -51.038 -27.471  1.00 73.33  ? 258 TYR A OH  1 
ATOM   2051  N N   . LYS A 1 258 ? 52.544  -43.949 -24.179  1.00 50.92  ? 259 LYS A N   1 
ATOM   2052  C CA  . LYS A 1 258 ? 52.872  -42.544 -23.983  1.00 60.32  ? 259 LYS A CA  1 
ATOM   2053  C C   . LYS A 1 258 ? 52.208  -41.715 -25.075  1.00 60.85  ? 259 LYS A C   1 
ATOM   2054  O O   . LYS A 1 258 ? 52.353  -42.006 -26.266  1.00 65.53  ? 259 LYS A O   1 
ATOM   2055  C CB  . LYS A 1 258 ? 54.388  -42.342 -24.000  1.00 70.08  ? 259 LYS A CB  1 
ATOM   2056  C CG  . LYS A 1 258 ? 55.126  -43.094 -22.902  1.00 73.74  ? 259 LYS A CG  1 
ATOM   2057  C CD  . LYS A 1 258 ? 56.635  -42.900 -22.992  1.00 76.38  ? 259 LYS A CD  1 
ATOM   2058  C CE  . LYS A 1 258 ? 57.047  -41.477 -22.655  1.00 96.90  ? 259 LYS A CE  1 
ATOM   2059  N NZ  . LYS A 1 258 ? 58.531  -41.335 -22.624  1.00 83.13  ? 259 LYS A NZ  1 
ATOM   2060  N N   . ILE A 1 259 ? 51.475  -40.682 -24.670  1.00 65.85  ? 260 ILE A N   1 
ATOM   2061  C CA  . ILE A 1 259 ? 50.629  -39.917 -25.576  1.00 63.31  ? 260 ILE A CA  1 
ATOM   2062  C C   . ILE A 1 259 ? 50.962  -38.439 -25.445  1.00 70.82  ? 260 ILE A C   1 
ATOM   2063  O O   . ILE A 1 259 ? 50.986  -37.899 -24.334  1.00 65.27  ? 260 ILE A O   1 
ATOM   2064  C CB  . ILE A 1 259 ? 49.132  -40.155 -25.292  1.00 67.47  ? 260 ILE A CB  1 
ATOM   2065  C CG1 . ILE A 1 259 ? 48.714  -41.553 -25.747  1.00 73.40  ? 260 ILE A CG1 1 
ATOM   2066  C CG2 . ILE A 1 259 ? 48.277  -39.090 -25.968  1.00 68.42  ? 260 ILE A CG2 1 
ATOM   2067  C CD1 . ILE A 1 259 ? 48.555  -41.682 -27.239  1.00 63.34  ? 260 ILE A CD1 1 
ATOM   2068  N N   . VAL A 1 260 A 51.221  -37.793 -26.579  1.00 64.22  ? 260 VAL A N   1 
ATOM   2069  C CA  . VAL A 1 260 A 51.262  -36.339 -26.676  1.00 66.55  ? 260 VAL A CA  1 
ATOM   2070  C C   . VAL A 1 260 A 50.308  -35.938 -27.791  1.00 71.84  ? 260 VAL A C   1 
ATOM   2071  O O   . VAL A 1 260 A 50.484  -36.358 -28.940  1.00 75.58  ? 260 VAL A O   1 
ATOM   2072  C CB  . VAL A 1 260 A 52.677  -35.808 -26.957  1.00 70.95  ? 260 VAL A CB  1 
ATOM   2073  C CG1 . VAL A 1 260 A 52.665  -34.289 -27.033  1.00 58.64  ? 260 VAL A CG1 1 
ATOM   2074  C CG2 . VAL A 1 260 A 53.647  -36.284 -25.891  1.00 67.75  ? 260 VAL A CG2 1 
ATOM   2075  N N   . LYS A 1 261 ? 49.300  -35.137 -27.457  1.00 77.11  ? 261 LYS A N   1 
ATOM   2076  C CA  . LYS A 1 261 ? 48.287  -34.714 -28.415  1.00 75.21  ? 261 LYS A CA  1 
ATOM   2077  C C   . LYS A 1 261 ? 48.286  -33.196 -28.499  1.00 79.74  ? 261 LYS A C   1 
ATOM   2078  O O   . LYS A 1 261 ? 48.138  -32.514 -27.479  1.00 72.52  ? 261 LYS A O   1 
ATOM   2079  C CB  . LYS A 1 261 ? 46.904  -35.230 -28.021  1.00 64.97  ? 261 LYS A CB  1 
ATOM   2080  C CG  . LYS A 1 261 ? 45.823  -34.860 -29.016  1.00 89.69  ? 261 LYS A CG  1 
ATOM   2081  C CD  . LYS A 1 261 ? 44.468  -35.365 -28.573  1.00 94.67  ? 261 LYS A CD  1 
ATOM   2082  C CE  . LYS A 1 261 ? 43.396  -34.983 -29.575  1.00 91.75  ? 261 LYS A CE  1 
ATOM   2083  N NZ  . LYS A 1 261 ? 43.726  -35.473 -30.943  1.00 92.75  ? 261 LYS A NZ  1 
ATOM   2084  N N   . LYS A 1 262 ? 48.439  -32.670 -29.715  1.00 83.85  ? 262 LYS A N   1 
ATOM   2085  C CA  . LYS A 1 262 ? 48.453  -31.233 -29.944  1.00 92.52  ? 262 LYS A CA  1 
ATOM   2086  C C   . LYS A 1 262 ? 47.312  -30.733 -30.817  1.00 95.88  ? 262 LYS A C   1 
ATOM   2087  O O   . LYS A 1 262 ? 47.143  -29.513 -30.936  1.00 102.86 ? 262 LYS A O   1 
ATOM   2088  C CB  . LYS A 1 262 ? 49.782  -30.803 -30.583  1.00 100.35 ? 262 LYS A CB  1 
ATOM   2089  C CG  . LYS A 1 262 ? 50.943  -30.703 -29.607  1.00 97.99  ? 262 LYS A CG  1 
ATOM   2090  C CD  . LYS A 1 262 ? 52.192  -30.186 -30.299  1.00 102.74 ? 262 LYS A CD  1 
ATOM   2091  C CE  . LYS A 1 262 ? 53.224  -29.708 -29.293  1.00 104.20 ? 262 LYS A CE  1 
ATOM   2092  N NZ  . LYS A 1 262 ? 54.408  -29.106 -29.965  1.00 105.35 ? 262 LYS A NZ  1 
ATOM   2093  N N   . GLY A 1 263 ? 46.534  -31.621 -31.427  1.00 78.40  ? 263 GLY A N   1 
ATOM   2094  C CA  . GLY A 1 263 ? 45.455  -31.195 -32.299  1.00 86.93  ? 263 GLY A CA  1 
ATOM   2095  C C   . GLY A 1 263 ? 44.503  -32.340 -32.556  1.00 102.37 ? 263 GLY A C   1 
ATOM   2096  O O   . GLY A 1 263 ? 44.765  -33.490 -32.198  1.00 101.74 ? 263 GLY A O   1 
ATOM   2097  N N   . ASP A 1 264 ? 43.389  -32.010 -33.206  1.00 88.65  ? 264 ASP A N   1 
ATOM   2098  C CA  . ASP A 1 264 ? 42.314  -32.960 -33.442  1.00 78.10  ? 264 ASP A CA  1 
ATOM   2099  C C   . ASP A 1 264 ? 42.129  -33.219 -34.931  1.00 77.97  ? 264 ASP A C   1 
ATOM   2100  O O   . ASP A 1 264 ? 42.438  -32.373 -35.776  1.00 95.40  ? 264 ASP A O   1 
ATOM   2101  C CB  . ASP A 1 264 ? 40.991  -32.467 -32.838  1.00 99.72  ? 264 ASP A CB  1 
ATOM   2102  C CG  . ASP A 1 264 ? 40.596  -33.241 -31.593  1.00 120.44 ? 264 ASP A CG  1 
ATOM   2103  O OD1 . ASP A 1 264 ? 40.930  -34.442 -31.502  1.00 96.50  ? 264 ASP A OD1 1 
ATOM   2104  O OD2 . ASP A 1 264 ? 39.945  -32.649 -30.707  1.00 127.73 ? 264 ASP A OD2 1 
ATOM   2105  N N   . SER A 1 265 ? 41.615  -34.405 -35.230  1.00 78.51  ? 265 SER A N   1 
ATOM   2106  C CA  . SER A 1 265 ? 41.340  -34.861 -36.587  1.00 61.12  ? 265 SER A CA  1 
ATOM   2107  C C   . SER A 1 265 ? 40.136  -35.795 -36.517  1.00 73.79  ? 265 SER A C   1 
ATOM   2108  O O   . SER A 1 265 ? 39.390  -35.789 -35.532  1.00 81.46  ? 265 SER A O   1 
ATOM   2109  C CB  . SER A 1 265 ? 42.583  -35.529 -37.196  1.00 60.87  ? 265 SER A CB  1 
ATOM   2110  O OG  . SER A 1 265 ? 42.255  -36.200 -38.399  1.00 80.78  ? 265 SER A OG  1 
ATOM   2111  N N   . THR A 1 266 ? 39.935  -36.595 -37.561  1.00 63.79  ? 266 THR A N   1 
ATOM   2112  C CA  . THR A 1 266 ? 38.864  -37.578 -37.569  1.00 72.92  ? 266 THR A CA  1 
ATOM   2113  C C   . THR A 1 266 ? 39.373  -38.873 -38.186  1.00 66.64  ? 266 THR A C   1 
ATOM   2114  O O   . THR A 1 266 ? 40.450  -38.923 -38.787  1.00 57.16  ? 266 THR A O   1 
ATOM   2115  C CB  . THR A 1 266 ? 37.633  -37.071 -38.328  1.00 75.66  ? 266 THR A CB  1 
ATOM   2116  O OG1 . THR A 1 266 ? 36.489  -37.848 -37.955  1.00 76.30  ? 266 THR A OG1 1 
ATOM   2117  C CG2 . THR A 1 266 ? 37.845  -37.193 -39.827  1.00 65.06  ? 266 THR A CG2 1 
ATOM   2118  N N   . ILE A 1 267 ? 38.589  -39.931 -38.019  1.00 65.95  ? 267 ILE A N   1 
ATOM   2119  C CA  . ILE A 1 267 ? 38.879  -41.221 -38.632  1.00 60.37  ? 267 ILE A CA  1 
ATOM   2120  C C   . ILE A 1 267 ? 38.309  -41.220 -40.043  1.00 60.08  ? 267 ILE A C   1 
ATOM   2121  O O   . ILE A 1 267 ? 37.147  -40.852 -40.253  1.00 65.77  ? 267 ILE A O   1 
ATOM   2122  C CB  . ILE A 1 267 ? 38.291  -42.374 -37.802  1.00 60.89  ? 267 ILE A CB  1 
ATOM   2123  C CG1 . ILE A 1 267 ? 38.612  -42.192 -36.316  1.00 61.70  ? 267 ILE A CG1 1 
ATOM   2124  C CG2 . ILE A 1 267 ? 38.816  -43.709 -38.304  1.00 55.04  ? 267 ILE A CG2 1 
ATOM   2125  C CD1 . ILE A 1 267 ? 40.086  -42.233 -35.993  1.00 63.27  ? 267 ILE A CD1 1 
ATOM   2126  N N   . MET A 1 268 ? 39.125  -41.622 -41.012  1.00 62.75  ? 268 MET A N   1 
ATOM   2127  C CA  . MET A 1 268 ? 38.711  -41.710 -42.405  1.00 56.23  ? 268 MET A CA  1 
ATOM   2128  C C   . MET A 1 268 ? 38.533  -43.170 -42.794  1.00 59.86  ? 268 MET A C   1 
ATOM   2129  O O   . MET A 1 268 ? 39.411  -43.998 -42.530  1.00 73.59  ? 268 MET A O   1 
ATOM   2130  C CB  . MET A 1 268 ? 39.731  -41.044 -43.330  1.00 71.41  ? 268 MET A CB  1 
ATOM   2131  C CG  . MET A 1 268 ? 39.589  -41.455 -44.787  1.00 68.23  ? 268 MET A CG  1 
ATOM   2132  S SD  . MET A 1 268 ? 40.372  -40.280 -45.899  1.00 84.37  ? 268 MET A SD  1 
ATOM   2133  C CE  . MET A 1 268 ? 39.571  -38.773 -45.364  1.00 72.67  ? 268 MET A CE  1 
ATOM   2134  N N   . LYS A 1 269 ? 37.402  -43.481 -43.420  1.00 61.14  ? 269 LYS A N   1 
ATOM   2135  C CA  . LYS A 1 269 ? 37.120  -44.822 -43.914  1.00 70.74  ? 269 LYS A CA  1 
ATOM   2136  C C   . LYS A 1 269 ? 37.341  -44.841 -45.424  1.00 74.64  ? 269 LYS A C   1 
ATOM   2137  O O   . LYS A 1 269 ? 36.610  -44.185 -46.173  1.00 75.40  ? 269 LYS A O   1 
ATOM   2138  C CB  . LYS A 1 269 ? 35.696  -45.241 -43.553  1.00 71.90  ? 269 LYS A CB  1 
ATOM   2139  C CG  . LYS A 1 269 ? 35.538  -45.694 -42.110  1.00 82.80  ? 269 LYS A CG  1 
ATOM   2140  C CD  . LYS A 1 269 ? 34.075  -45.750 -41.719  1.00 96.69  ? 269 LYS A CD  1 
ATOM   2141  C CE  . LYS A 1 269 ? 33.772  -46.969 -40.871  1.00 104.26 ? 269 LYS A CE  1 
ATOM   2142  N NZ  . LYS A 1 269 ? 32.610  -47.713 -41.428  1.00 104.01 ? 269 LYS A NZ  1 
ATOM   2143  N N   . SER A 1 270 ? 38.349  -45.593 -45.864  1.00 74.41  ? 270 SER A N   1 
ATOM   2144  C CA  . SER A 1 270 ? 38.713  -45.644 -47.273  1.00 70.25  ? 270 SER A CA  1 
ATOM   2145  C C   . SER A 1 270 ? 39.514  -46.908 -47.541  1.00 75.30  ? 270 SER A C   1 
ATOM   2146  O O   . SER A 1 270 ? 40.282  -47.363 -46.689  1.00 87.46  ? 270 SER A O   1 
ATOM   2147  C CB  . SER A 1 270 ? 39.518  -44.407 -47.684  1.00 79.40  ? 270 SER A CB  1 
ATOM   2148  O OG  . SER A 1 270 ? 40.047  -44.559 -48.990  1.00 85.06  ? 270 SER A OG  1 
ATOM   2149  N N   . GLY A 1 271 ? 39.328  -47.463 -48.736  1.00 77.53  ? 271 GLY A N   1 
ATOM   2150  C CA  . GLY A 1 271 ? 40.068  -48.615 -49.205  1.00 91.99  ? 271 GLY A CA  1 
ATOM   2151  C C   . GLY A 1 271 ? 41.194  -48.309 -50.169  1.00 89.55  ? 271 GLY A C   1 
ATOM   2152  O O   . GLY A 1 271 ? 41.933  -49.223 -50.548  1.00 91.44  ? 271 GLY A O   1 
ATOM   2153  N N   . VAL A 1 272 ? 41.346  -47.045 -50.573  1.00 87.61  ? 272 VAL A N   1 
ATOM   2154  C CA  . VAL A 1 272 ? 42.411  -46.645 -51.487  1.00 89.71  ? 272 VAL A CA  1 
ATOM   2155  C C   . VAL A 1 272 ? 43.781  -46.876 -50.833  1.00 87.32  ? 272 VAL A C   1 
ATOM   2156  O O   . VAL A 1 272 ? 43.892  -47.080 -49.618  1.00 86.53  ? 272 VAL A O   1 
ATOM   2157  C CB  . VAL A 1 272 ? 42.176  -45.179 -51.895  1.00 71.62  ? 272 VAL A CB  1 
ATOM   2158  C CG1 . VAL A 1 272 ? 43.436  -44.483 -52.355  1.00 84.72  ? 272 VAL A CG1 1 
ATOM   2159  C CG2 . VAL A 1 272 ? 41.114  -45.126 -52.993  1.00 79.18  ? 272 VAL A CG2 1 
ATOM   2160  N N   . GLU A 1 273 ? 44.823  -46.925 -51.665  1.00 89.55  ? 273 GLU A N   1 
ATOM   2161  C CA  . GLU A 1 273 ? 46.187  -47.172 -51.219  1.00 88.20  ? 273 GLU A CA  1 
ATOM   2162  C C   . GLU A 1 273 ? 46.910  -45.870 -50.887  1.00 80.34  ? 273 GLU A C   1 
ATOM   2163  O O   . GLU A 1 273 ? 46.568  -44.794 -51.382  1.00 85.18  ? 273 GLU A O   1 
ATOM   2164  C CB  . GLU A 1 273 ? 46.977  -47.922 -52.292  1.00 100.11 ? 273 GLU A CB  1 
ATOM   2165  C CG  . GLU A 1 273 ? 46.170  -48.945 -53.065  1.00 116.80 ? 273 GLU A CG  1 
ATOM   2166  C CD  . GLU A 1 273 ? 47.011  -49.687 -54.081  1.00 119.83 ? 273 GLU A CD  1 
ATOM   2167  O OE1 . GLU A 1 273 ? 47.941  -49.072 -54.642  1.00 106.06 ? 273 GLU A OE1 1 
ATOM   2168  O OE2 . GLU A 1 273 ? 46.749  -50.886 -54.310  1.00 127.47 ? 273 GLU A OE2 1 
ATOM   2169  N N   . TYR A 1 274 ? 47.926  -45.986 -50.033  1.00 72.26  ? 274 TYR A N   1 
ATOM   2170  C CA  . TYR A 1 274 ? 48.838  -44.887 -49.748  1.00 76.04  ? 274 TYR A CA  1 
ATOM   2171  C C   . TYR A 1 274 ? 49.790  -44.678 -50.922  1.00 92.93  ? 274 TYR A C   1 
ATOM   2172  O O   . TYR A 1 274 ? 50.176  -45.628 -51.611  1.00 99.14  ? 274 TYR A O   1 
ATOM   2173  C CB  . TYR A 1 274 ? 49.626  -45.171 -48.467  1.00 77.05  ? 274 TYR A CB  1 
ATOM   2174  C CG  . TYR A 1 274 ? 50.571  -44.067 -48.050  1.00 76.08  ? 274 TYR A CG  1 
ATOM   2175  C CD1 . TYR A 1 274 ? 50.087  -42.844 -47.605  1.00 79.34  ? 274 TYR A CD1 1 
ATOM   2176  C CD2 . TYR A 1 274 ? 51.947  -44.253 -48.085  1.00 79.04  ? 274 TYR A CD2 1 
ATOM   2177  C CE1 . TYR A 1 274 ? 50.947  -41.834 -47.219  1.00 81.46  ? 274 TYR A CE1 1 
ATOM   2178  C CE2 . TYR A 1 274 ? 52.814  -43.249 -47.699  1.00 76.12  ? 274 TYR A CE2 1 
ATOM   2179  C CZ  . TYR A 1 274 ? 52.308  -42.042 -47.267  1.00 81.17  ? 274 TYR A CZ  1 
ATOM   2180  O OH  . TYR A 1 274 ? 53.166  -41.039 -46.883  1.00 84.34  ? 274 TYR A OH  1 
ATOM   2181  N N   . GLY A 1 275 ? 50.176  -43.421 -51.147  1.00 93.76  ? 275 GLY A N   1 
ATOM   2182  C CA  . GLY A 1 275 ? 50.907  -43.094 -52.358  1.00 97.85  ? 275 GLY A CA  1 
ATOM   2183  C C   . GLY A 1 275 ? 52.124  -42.200 -52.233  1.00 105.76 ? 275 GLY A C   1 
ATOM   2184  O O   . GLY A 1 275 ? 52.610  -41.684 -53.244  1.00 117.35 ? 275 GLY A O   1 
ATOM   2185  N N   . HIS A 1 276 ? 52.630  -42.015 -51.013  1.00 107.33 ? 276 HIS A N   1 
ATOM   2186  C CA  . HIS A 1 276 ? 53.861  -41.254 -50.776  1.00 108.78 ? 276 HIS A CA  1 
ATOM   2187  C C   . HIS A 1 276 ? 53.769  -39.848 -51.366  1.00 94.86  ? 276 HIS A C   1 
ATOM   2188  O O   . HIS A 1 276 ? 54.645  -39.395 -52.106  1.00 98.02  ? 276 HIS A O   1 
ATOM   2189  C CB  . HIS A 1 276 ? 55.083  -41.995 -51.331  1.00 90.60  ? 276 HIS A CB  1 
ATOM   2190  C CG  . HIS A 1 276 ? 55.142  -43.441 -50.949  1.00 110.97 ? 276 HIS A CG  1 
ATOM   2191  N ND1 . HIS A 1 276 ? 54.360  -44.404 -51.551  1.00 121.33 ? 276 HIS A ND1 1 
ATOM   2192  C CD2 . HIS A 1 276 ? 55.897  -44.091 -50.030  1.00 105.90 ? 276 HIS A CD2 1 
ATOM   2193  C CE1 . HIS A 1 276 ? 54.626  -45.582 -51.017  1.00 108.23 ? 276 HIS A CE1 1 
ATOM   2194  N NE2 . HIS A 1 276 ? 55.555  -45.420 -50.092  1.00 114.34 ? 276 HIS A NE2 1 
ATOM   2195  N N   . CYS A 1 277 ? 52.684  -39.155 -51.034  1.00 88.45  ? 277 CYS A N   1 
ATOM   2196  C CA  . CYS A 1 277 ? 52.421  -37.818 -51.539  1.00 77.48  ? 277 CYS A CA  1 
ATOM   2197  C C   . CYS A 1 277 ? 52.067  -36.899 -50.377  1.00 75.82  ? 277 CYS A C   1 
ATOM   2198  O O   . CYS A 1 277 ? 51.916  -37.336 -49.233  1.00 83.67  ? 277 CYS A O   1 
ATOM   2199  C CB  . CYS A 1 277 ? 51.299  -37.834 -52.590  1.00 82.86  ? 277 CYS A CB  1 
ATOM   2200  S SG  . CYS A 1 277 ? 49.953  -38.989 -52.227  1.00 139.06 ? 277 CYS A SG  1 
ATOM   2201  N N   . ASN A 1 278 ? 51.947  -35.609 -50.681  1.00 78.28  ? 278 ASN A N   1 
ATOM   2202  C CA  . ASN A 1 278 ? 51.579  -34.602 -49.699  1.00 72.45  ? 278 ASN A CA  1 
ATOM   2203  C C   . ASN A 1 278 ? 50.443  -33.753 -50.251  1.00 72.78  ? 278 ASN A C   1 
ATOM   2204  O O   . ASN A 1 278 ? 50.368  -33.496 -51.456  1.00 81.99  ? 278 ASN A O   1 
ATOM   2205  C CB  . ASN A 1 278 ? 52.770  -33.705 -49.331  1.00 68.03  ? 278 ASN A CB  1 
ATOM   2206  C CG  . ASN A 1 278 ? 52.509  -32.870 -48.094  1.00 76.52  ? 278 ASN A CG  1 
ATOM   2207  O OD1 . ASN A 1 278 ? 51.817  -33.305 -47.175  1.00 75.45  ? 278 ASN A OD1 1 
ATOM   2208  N ND2 . ASN A 1 278 ? 53.059  -31.661 -48.066  1.00 73.30  ? 278 ASN A ND2 1 
ATOM   2209  N N   . THR A 1 279 ? 49.560  -33.316 -49.356  1.00 78.72  ? 279 THR A N   1 
ATOM   2210  C CA  . THR A 1 279 ? 48.400  -32.533 -49.755  1.00 71.22  ? 279 THR A CA  1 
ATOM   2211  C C   . THR A 1 279 ? 47.916  -31.718 -48.566  1.00 62.68  ? 279 THR A C   1 
ATOM   2212  O O   . THR A 1 279 ? 48.276  -31.987 -47.418  1.00 74.68  ? 279 THR A O   1 
ATOM   2213  C CB  . THR A 1 279 ? 47.271  -33.427 -50.280  1.00 75.46  ? 279 THR A CB  1 
ATOM   2214  O OG1 . THR A 1 279 ? 46.189  -32.609 -50.741  1.00 80.56  ? 279 THR A OG1 1 
ATOM   2215  C CG2 . THR A 1 279 ? 46.766  -34.344 -49.176  1.00 72.70  ? 279 THR A CG2 1 
ATOM   2216  N N   . LYS A 1 280 ? 47.094  -30.711 -48.860  1.00 64.83  ? 280 LYS A N   1 
ATOM   2217  C CA  . LYS A 1 280 ? 46.424  -29.928 -47.831  1.00 67.94  ? 280 LYS A CA  1 
ATOM   2218  C C   . LYS A 1 280 ? 44.959  -30.307 -47.663  1.00 77.40  ? 280 LYS A C   1 
ATOM   2219  O O   . LYS A 1 280 ? 44.286  -29.753 -46.787  1.00 74.76  ? 280 LYS A O   1 
ATOM   2220  C CB  . LYS A 1 280 ? 46.531  -28.430 -48.140  1.00 63.12  ? 280 LYS A CB  1 
ATOM   2221  C CG  . LYS A 1 280 ? 47.951  -27.892 -48.136  1.00 73.75  ? 280 LYS A CG  1 
ATOM   2222  C CD  . LYS A 1 280 ? 47.980  -26.385 -47.923  1.00 78.74  ? 280 LYS A CD  1 
ATOM   2223  C CE  . LYS A 1 280 ? 47.411  -26.005 -46.563  1.00 106.99 ? 280 LYS A CE  1 
ATOM   2224  N NZ  . LYS A 1 280 ? 47.822  -24.630 -46.157  1.00 107.90 ? 280 LYS A NZ  1 
ATOM   2225  N N   . CYS A 1 281 ? 44.451  -31.230 -48.475  1.00 74.56  ? 281 CYS A N   1 
ATOM   2226  C CA  . CYS A 1 281 ? 43.050  -31.631 -48.403  1.00 66.78  ? 281 CYS A CA  1 
ATOM   2227  C C   . CYS A 1 281 ? 42.933  -33.068 -48.883  1.00 62.71  ? 281 CYS A C   1 
ATOM   2228  O O   . CYS A 1 281 ? 43.238  -33.360 -50.043  1.00 77.73  ? 281 CYS A O   1 
ATOM   2229  C CB  . CYS A 1 281 ? 42.167  -30.703 -49.241  1.00 56.14  ? 281 CYS A CB  1 
ATOM   2230  S SG  . CYS A 1 281 ? 40.417  -31.128 -49.183  1.00 97.31  ? 281 CYS A SG  1 
ATOM   2231  N N   . GLN A 1 282 ? 42.490  -33.957 -47.997  1.00 60.89  ? 282 GLN A N   1 
ATOM   2232  C CA  . GLN A 1 282 ? 42.380  -35.381 -48.284  1.00 60.73  ? 282 GLN A CA  1 
ATOM   2233  C C   . GLN A 1 282 ? 40.920  -35.811 -48.245  1.00 68.65  ? 282 GLN A C   1 
ATOM   2234  O O   . GLN A 1 282 ? 40.154  -35.369 -47.383  1.00 74.85  ? 282 GLN A O   1 
ATOM   2235  C CB  . GLN A 1 282 ? 43.194  -36.211 -47.280  1.00 58.85  ? 282 GLN A CB  1 
ATOM   2236  C CG  . GLN A 1 282 ? 43.198  -37.709 -47.556  1.00 65.66  ? 282 GLN A CG  1 
ATOM   2237  C CD  . GLN A 1 282 ? 43.965  -38.072 -48.813  1.00 73.43  ? 282 GLN A CD  1 
ATOM   2238  O OE1 . GLN A 1 282 ? 45.132  -37.713 -48.967  1.00 74.19  ? 282 GLN A OE1 1 
ATOM   2239  N NE2 . GLN A 1 282 ? 43.309  -38.786 -49.721  1.00 70.24  ? 282 GLN A NE2 1 
ATOM   2240  N N   . THR A 1 283 ? 40.545  -36.676 -49.177  1.00 62.22  ? 283 THR A N   1 
ATOM   2241  C CA  . THR A 1 283 ? 39.216  -37.256 -49.278  1.00 54.29  ? 283 THR A CA  1 
ATOM   2242  C C   . THR A 1 283 ? 39.352  -38.769 -49.328  1.00 63.75  ? 283 THR A C   1 
ATOM   2243  O O   . THR A 1 283 ? 40.423  -39.290 -49.659  1.00 62.73  ? 283 THR A O   1 
ATOM   2244  C CB  . THR A 1 283 ? 38.472  -36.760 -50.530  1.00 68.21  ? 283 THR A CB  1 
ATOM   2245  O OG1 . THR A 1 283 ? 38.963  -37.448 -51.686  1.00 69.68  ? 283 THR A OG1 1 
ATOM   2246  C CG2 . THR A 1 283 ? 38.667  -35.262 -50.718  1.00 66.92  ? 283 THR A CG2 1 
ATOM   2247  N N   . PRO A 1 284 ? 38.289  -39.508 -48.995  1.00 71.84  ? 284 PRO A N   1 
ATOM   2248  C CA  . PRO A 1 284 ? 38.380  -40.978 -49.039  1.00 70.99  ? 284 PRO A CA  1 
ATOM   2249  C C   . PRO A 1 284 ? 38.687  -41.535 -50.419  1.00 71.18  ? 284 PRO A C   1 
ATOM   2250  O O   . PRO A 1 284 ? 39.156  -42.677 -50.514  1.00 80.97  ? 284 PRO A O   1 
ATOM   2251  C CB  . PRO A 1 284 ? 36.996  -41.429 -48.549  1.00 67.54  ? 284 PRO A CB  1 
ATOM   2252  C CG  . PRO A 1 284 ? 36.508  -40.293 -47.722  1.00 59.77  ? 284 PRO A CG  1 
ATOM   2253  C CD  . PRO A 1 284 ? 37.014  -39.061 -48.408  1.00 55.87  ? 284 PRO A CD  1 
ATOM   2254  N N   . VAL A 1 285 ? 38.433  -40.778 -51.490  1.00 63.92  ? 285 VAL A N   1 
ATOM   2255  C CA  . VAL A 1 285 ? 38.727  -41.244 -52.840  1.00 68.90  ? 285 VAL A CA  1 
ATOM   2256  C C   . VAL A 1 285 ? 40.044  -40.702 -53.376  1.00 62.07  ? 285 VAL A C   1 
ATOM   2257  O O   . VAL A 1 285 ? 40.518  -41.182 -54.412  1.00 78.96  ? 285 VAL A O   1 
ATOM   2258  C CB  . VAL A 1 285 ? 37.583  -40.890 -53.815  1.00 60.58  ? 285 VAL A CB  1 
ATOM   2259  C CG1 . VAL A 1 285 ? 36.323  -41.646 -53.439  1.00 55.33  ? 285 VAL A CG1 1 
ATOM   2260  C CG2 . VAL A 1 285 ? 37.330  -39.389 -53.821  1.00 66.54  ? 285 VAL A CG2 1 
ATOM   2261  N N   . GLY A 1 286 ? 40.646  -39.732 -52.717  1.00 67.99  ? 286 GLY A N   1 
ATOM   2262  C CA  . GLY A 1 286 ? 41.918  -39.193 -53.154  1.00 51.65  ? 286 GLY A CA  1 
ATOM   2263  C C   . GLY A 1 286 ? 42.075  -37.748 -52.725  1.00 60.41  ? 286 GLY A C   1 
ATOM   2264  O O   . GLY A 1 286 ? 41.129  -37.066 -52.326  1.00 71.26  ? 286 GLY A O   1 
ATOM   2265  N N   . ALA A 1 287 ? 43.310  -37.279 -52.818  1.00 57.17  ? 287 ALA A N   1 
ATOM   2266  C CA  . ALA A 1 287 ? 43.632  -35.907 -52.465  1.00 67.24  ? 287 ALA A CA  1 
ATOM   2267  C C   . ALA A 1 287 ? 43.226  -34.954 -53.582  1.00 68.58  ? 287 ALA A C   1 
ATOM   2268  O O   . ALA A 1 287 ? 43.181  -35.322 -54.760  1.00 84.35  ? 287 ALA A O   1 
ATOM   2269  C CB  . ALA A 1 287 ? 45.133  -35.767 -52.180  1.00 69.37  ? 287 ALA A CB  1 
ATOM   2270  N N   . ILE A 1 288 ? 42.921  -33.715 -53.197  1.00 67.12  ? 288 ILE A N   1 
ATOM   2271  C CA  . ILE A 1 288 ? 42.567  -32.666 -54.142  1.00 80.55  ? 288 ILE A CA  1 
ATOM   2272  C C   . ILE A 1 288 ? 43.400  -31.429 -53.830  1.00 79.03  ? 288 ILE A C   1 
ATOM   2273  O O   . ILE A 1 288 ? 43.912  -31.259 -52.722  1.00 75.92  ? 288 ILE A O   1 
ATOM   2274  C CB  . ILE A 1 288 ? 41.061  -32.313 -54.111  1.00 71.69  ? 288 ILE A CB  1 
ATOM   2275  C CG1 . ILE A 1 288 ? 40.710  -31.580 -52.816  1.00 68.42  ? 288 ILE A CG1 1 
ATOM   2276  C CG2 . ILE A 1 288 ? 40.210  -33.568 -54.262  1.00 73.39  ? 288 ILE A CG2 1 
ATOM   2277  C CD1 . ILE A 1 288 ? 39.283  -31.087 -52.764  1.00 72.39  ? 288 ILE A CD1 1 
ATOM   2278  N N   . ASN A 1 289 ? 43.539  -30.562 -54.834  1.00 82.11  ? 289 ASN A N   1 
ATOM   2279  C CA  . ASN A 1 289 ? 44.209  -29.285 -54.636  1.00 91.28  ? 289 ASN A CA  1 
ATOM   2280  C C   . ASN A 1 289 ? 43.307  -28.319 -53.873  1.00 87.43  ? 289 ASN A C   1 
ATOM   2281  O O   . ASN A 1 289 ? 42.077  -28.430 -53.892  1.00 85.03  ? 289 ASN A O   1 
ATOM   2282  C CB  . ASN A 1 289 ? 44.613  -28.666 -55.974  1.00 92.07  ? 289 ASN A CB  1 
ATOM   2283  C CG  . ASN A 1 289 ? 45.743  -29.425 -56.656  1.00 105.12 ? 289 ASN A CG  1 
ATOM   2284  O OD1 . ASN A 1 289 ? 46.867  -29.465 -56.159  1.00 97.96  ? 289 ASN A OD1 1 
ATOM   2285  N ND2 . ASN A 1 289 ? 45.448  -30.023 -57.807  1.00 130.00 ? 289 ASN A ND2 1 
ATOM   2286  N N   . SER A 1 290 ? 43.939  -27.365 -53.192  1.00 77.97  ? 290 SER A N   1 
ATOM   2287  C CA  . SER A 1 290 ? 43.245  -26.404 -52.346  1.00 76.78  ? 290 SER A CA  1 
ATOM   2288  C C   . SER A 1 290 ? 43.218  -25.001 -52.939  1.00 82.96  ? 290 SER A C   1 
ATOM   2289  O O   . SER A 1 290 ? 42.815  -24.056 -52.251  1.00 75.98  ? 290 SER A O   1 
ATOM   2290  C CB  . SER A 1 290 ? 43.889  -26.369 -50.957  1.00 78.36  ? 290 SER A CB  1 
ATOM   2291  O OG  . SER A 1 290 ? 43.439  -25.249 -50.217  1.00 113.48 ? 290 SER A OG  1 
ATOM   2292  N N   . SER A 1 291 ? 43.637  -24.839 -54.195  1.00 87.38  ? 291 SER A N   1 
ATOM   2293  C CA  . SER A 1 291 ? 43.712  -23.506 -54.785  1.00 68.32  ? 291 SER A CA  1 
ATOM   2294  C C   . SER A 1 291 ? 42.326  -22.949 -55.089  1.00 77.91  ? 291 SER A C   1 
ATOM   2295  O O   . SER A 1 291 ? 42.032  -21.788 -54.782  1.00 67.30  ? 291 SER A O   1 
ATOM   2296  C CB  . SER A 1 291 ? 44.567  -23.546 -56.050  1.00 70.74  ? 291 SER A CB  1 
ATOM   2297  O OG  . SER A 1 291 ? 44.050  -24.479 -56.983  1.00 98.90  ? 291 SER A OG  1 
ATOM   2298  N N   . MET A 1 292 ? 41.458  -23.759 -55.689  1.00 79.48  ? 292 MET A N   1 
ATOM   2299  C CA  . MET A 1 292 ? 40.147  -23.268 -56.080  1.00 75.47  ? 292 MET A CA  1 
ATOM   2300  C C   . MET A 1 292 ? 39.251  -23.063 -54.859  1.00 79.81  ? 292 MET A C   1 
ATOM   2301  O O   . MET A 1 292 ? 39.443  -23.698 -53.820  1.00 87.17  ? 292 MET A O   1 
ATOM   2302  C CB  . MET A 1 292 ? 39.487  -24.235 -57.057  1.00 77.64  ? 292 MET A CB  1 
ATOM   2303  C CG  . MET A 1 292 ? 40.146  -24.233 -58.416  1.00 86.44  ? 292 MET A CG  1 
ATOM   2304  S SD  . MET A 1 292 ? 40.292  -22.550 -59.043  1.00 101.25 ? 292 MET A SD  1 
ATOM   2305  C CE  . MET A 1 292 ? 41.516  -22.773 -60.328  1.00 90.28  ? 292 MET A CE  1 
ATOM   2306  N N   . PRO A 1 293 ? 38.269  -22.162 -54.958  1.00 71.53  ? 293 PRO A N   1 
ATOM   2307  C CA  . PRO A 1 293 ? 37.364  -21.919 -53.826  1.00 70.45  ? 293 PRO A CA  1 
ATOM   2308  C C   . PRO A 1 293 ? 36.255  -22.945 -53.677  1.00 73.26  ? 293 PRO A C   1 
ATOM   2309  O O   . PRO A 1 293 ? 35.629  -22.994 -52.610  1.00 72.41  ? 293 PRO A O   1 
ATOM   2310  C CB  . PRO A 1 293 ? 36.783  -20.538 -54.147  1.00 67.95  ? 293 PRO A CB  1 
ATOM   2311  C CG  . PRO A 1 293 ? 36.793  -20.482 -55.643  1.00 67.88  ? 293 PRO A CG  1 
ATOM   2312  C CD  . PRO A 1 293 ? 38.022  -21.234 -56.076  1.00 72.97  ? 293 PRO A CD  1 
ATOM   2313  N N   . PHE A 1 294 ? 35.985  -23.760 -54.695  1.00 54.85  ? 294 PHE A N   1 
ATOM   2314  C CA  . PHE A 1 294 ? 34.914  -24.742 -54.618  1.00 56.94  ? 294 PHE A CA  1 
ATOM   2315  C C   . PHE A 1 294 ? 35.389  -26.068 -55.194  1.00 66.21  ? 294 PHE A C   1 
ATOM   2316  O O   . PHE A 1 294 ? 36.306  -26.118 -56.019  1.00 75.14  ? 294 PHE A O   1 
ATOM   2317  C CB  . PHE A 1 294 ? 33.654  -24.274 -55.364  1.00 59.65  ? 294 PHE A CB  1 
ATOM   2318  C CG  . PHE A 1 294 ? 33.145  -22.938 -54.914  1.00 64.23  ? 294 PHE A CG  1 
ATOM   2319  C CD1 . PHE A 1 294 ? 32.529  -22.794 -53.683  1.00 56.14  ? 294 PHE A CD1 1 
ATOM   2320  C CD2 . PHE A 1 294 ? 33.277  -21.826 -55.727  1.00 61.03  ? 294 PHE A CD2 1 
ATOM   2321  C CE1 . PHE A 1 294 ? 32.060  -21.560 -53.269  1.00 65.35  ? 294 PHE A CE1 1 
ATOM   2322  C CE2 . PHE A 1 294 ? 32.808  -20.592 -55.320  1.00 60.00  ? 294 PHE A CE2 1 
ATOM   2323  C CZ  . PHE A 1 294 ? 32.199  -20.458 -54.090  1.00 52.69  ? 294 PHE A CZ  1 
ATOM   2324  N N   . HIS A 1 295 ? 34.745  -27.146 -54.749  1.00 56.17  ? 295 HIS A N   1 
ATOM   2325  C CA  . HIS A 1 295 ? 35.001  -28.476 -55.280  1.00 55.87  ? 295 HIS A CA  1 
ATOM   2326  C C   . HIS A 1 295 ? 33.727  -29.301 -55.156  1.00 60.28  ? 295 HIS A C   1 
ATOM   2327  O O   . HIS A 1 295 ? 32.790  -28.933 -54.444  1.00 58.40  ? 295 HIS A O   1 
ATOM   2328  C CB  . HIS A 1 295 ? 36.171  -29.158 -54.562  1.00 62.46  ? 295 HIS A CB  1 
ATOM   2329  C CG  . HIS A 1 295 ? 35.793  -29.817 -53.272  1.00 74.60  ? 295 HIS A CG  1 
ATOM   2330  N ND1 . HIS A 1 295 ? 35.549  -31.170 -53.175  1.00 71.71  ? 295 HIS A ND1 1 
ATOM   2331  C CD2 . HIS A 1 295 ? 35.623  -29.314 -52.027  1.00 67.68  ? 295 HIS A CD2 1 
ATOM   2332  C CE1 . HIS A 1 295 ? 35.245  -31.472 -51.925  1.00 67.05  ? 295 HIS A CE1 1 
ATOM   2333  N NE2 . HIS A 1 295 ? 35.282  -30.363 -51.208  1.00 65.13  ? 295 HIS A NE2 1 
ATOM   2334  N N   . ASN A 1 296 ? 33.700  -30.431 -55.867  1.00 53.57  ? 296 ASN A N   1 
ATOM   2335  C CA  . ASN A 1 296 ? 32.534  -31.304 -55.867  1.00 51.81  ? 296 ASN A CA  1 
ATOM   2336  C C   . ASN A 1 296 ? 32.925  -32.775 -55.742  1.00 62.16  ? 296 ASN A C   1 
ATOM   2337  O O   . ASN A 1 296 ? 32.187  -33.651 -56.199  1.00 70.86  ? 296 ASN A O   1 
ATOM   2338  C CB  . ASN A 1 296 ? 31.701  -31.100 -57.139  1.00 63.16  ? 296 ASN A CB  1 
ATOM   2339  C CG  . ASN A 1 296 ? 32.508  -31.340 -58.416  1.00 65.79  ? 296 ASN A CG  1 
ATOM   2340  O OD1 . ASN A 1 296 ? 33.650  -31.802 -58.371  1.00 69.30  ? 296 ASN A OD1 1 
ATOM   2341  N ND2 . ASN A 1 296 ? 31.910  -31.030 -59.559  1.00 69.45  ? 296 ASN A ND2 1 
ATOM   2342  N N   . ILE A 1 297 ? 34.072  -33.067 -55.129  1.00 58.32  ? 297 ILE A N   1 
ATOM   2343  C CA  . ILE A 1 297 ? 34.598  -34.432 -55.138  1.00 61.83  ? 297 ILE A CA  1 
ATOM   2344  C C   . ILE A 1 297 ? 33.942  -35.282 -54.054  1.00 70.80  ? 297 ILE A C   1 
ATOM   2345  O O   . ILE A 1 297 ? 33.335  -36.320 -54.342  1.00 69.36  ? 297 ILE A O   1 
ATOM   2346  C CB  . ILE A 1 297 ? 36.132  -34.423 -55.003  1.00 69.33  ? 297 ILE A CB  1 
ATOM   2347  C CG1 . ILE A 1 297 ? 36.768  -33.992 -56.324  1.00 77.23  ? 297 ILE A CG1 1 
ATOM   2348  C CG2 . ILE A 1 297 ? 36.662  -35.775 -54.543  1.00 65.46  ? 297 ILE A CG2 1 
ATOM   2349  C CD1 . ILE A 1 297 ? 36.755  -32.487 -56.519  1.00 75.13  ? 297 ILE A CD1 1 
ATOM   2350  N N   . HIS A 1 298 ? 34.065  -34.868 -52.787  1.00 75.01  ? 298 HIS A N   1 
ATOM   2351  C CA  . HIS A 1 298 ? 33.558  -35.683 -51.690  1.00 69.99  ? 298 HIS A CA  1 
ATOM   2352  C C   . HIS A 1 298 ? 33.285  -34.792 -50.491  1.00 65.06  ? 298 HIS A C   1 
ATOM   2353  O O   . HIS A 1 298 ? 34.060  -33.858 -50.247  1.00 70.73  ? 298 HIS A O   1 
ATOM   2354  C CB  . HIS A 1 298 ? 34.565  -36.776 -51.318  1.00 77.53  ? 298 HIS A CB  1 
ATOM   2355  C CG  . HIS A 1 298 ? 33.943  -38.002 -50.726  1.00 66.03  ? 298 HIS A CG  1 
ATOM   2356  N ND1 . HIS A 1 298 ? 33.462  -38.046 -49.435  1.00 71.91  ? 298 HIS A ND1 1 
ATOM   2357  C CD2 . HIS A 1 298 ? 33.745  -39.237 -51.244  1.00 77.11  ? 298 HIS A CD2 1 
ATOM   2358  C CE1 . HIS A 1 298 ? 32.986  -39.253 -49.187  1.00 72.48  ? 298 HIS A CE1 1 
ATOM   2359  N NE2 . HIS A 1 298 ? 33.147  -39.995 -50.268  1.00 80.91  ? 298 HIS A NE2 1 
ATOM   2360  N N   . PRO A 1 299 ? 32.208  -35.030 -49.736  1.00 58.40  ? 299 PRO A N   1 
ATOM   2361  C CA  . PRO A 1 299 ? 31.942  -34.194 -48.553  1.00 61.00  ? 299 PRO A CA  1 
ATOM   2362  C C   . PRO A 1 299 ? 32.788  -34.532 -47.335  1.00 69.70  ? 299 PRO A C   1 
ATOM   2363  O O   . PRO A 1 299 ? 32.863  -33.704 -46.417  1.00 64.01  ? 299 PRO A O   1 
ATOM   2364  C CB  . PRO A 1 299 ? 30.455  -34.451 -48.271  1.00 56.82  ? 299 PRO A CB  1 
ATOM   2365  C CG  . PRO A 1 299 ? 30.210  -35.813 -48.820  1.00 52.98  ? 299 PRO A CG  1 
ATOM   2366  C CD  . PRO A 1 299 ? 31.086  -35.937 -50.035  1.00 60.96  ? 299 PRO A CD  1 
ATOM   2367  N N   . LEU A 1 300 ? 33.419  -35.705 -47.286  1.00 66.51  ? 300 LEU A N   1 
ATOM   2368  C CA  . LEU A 1 300 ? 34.153  -36.141 -46.095  1.00 69.44  ? 300 LEU A CA  1 
ATOM   2369  C C   . LEU A 1 300 ? 35.640  -35.816 -46.246  1.00 68.66  ? 300 LEU A C   1 
ATOM   2370  O O   . LEU A 1 300 ? 36.487  -36.683 -46.457  1.00 76.98  ? 300 LEU A O   1 
ATOM   2371  C CB  . LEU A 1 300 ? 33.927  -37.632 -45.852  1.00 60.87  ? 300 LEU A CB  1 
ATOM   2372  C CG  . LEU A 1 300 ? 32.478  -38.111 -45.729  1.00 62.92  ? 300 LEU A CG  1 
ATOM   2373  C CD1 . LEU A 1 300 ? 32.430  -39.607 -45.458  1.00 62.78  ? 300 LEU A CD1 1 
ATOM   2374  C CD2 . LEU A 1 300 ? 31.745  -37.345 -44.641  1.00 43.59  ? 300 LEU A CD2 1 
ATOM   2375  N N   . THR A 1 301 ? 35.950  -34.531 -46.113  1.00 65.32  ? 301 THR A N   1 
ATOM   2376  C CA  . THR A 1 301 ? 37.301  -34.034 -46.324  1.00 75.82  ? 301 THR A CA  1 
ATOM   2377  C C   . THR A 1 301 ? 38.022  -33.816 -44.998  1.00 61.89  ? 301 THR A C   1 
ATOM   2378  O O   . THR A 1 301 ? 37.400  -33.557 -43.965  1.00 72.24  ? 301 THR A O   1 
ATOM   2379  C CB  . THR A 1 301 ? 37.284  -32.722 -47.110  1.00 68.32  ? 301 THR A CB  1 
ATOM   2380  O OG1 . THR A 1 301 ? 36.718  -31.685 -46.299  1.00 84.04  ? 301 THR A OG1 1 
ATOM   2381  C CG2 . THR A 1 301 ? 36.459  -32.869 -48.375  1.00 62.44  ? 301 THR A CG2 1 
ATOM   2382  N N   . ILE A 1 302 ? 39.349  -33.930 -45.039  1.00 70.90  ? 302 ILE A N   1 
ATOM   2383  C CA  . ILE A 1 302 ? 40.216  -33.554 -43.930  1.00 69.14  ? 302 ILE A CA  1 
ATOM   2384  C C   . ILE A 1 302 ? 41.277  -32.603 -44.465  1.00 65.43  ? 302 ILE A C   1 
ATOM   2385  O O   . ILE A 1 302 ? 41.960  -32.918 -45.447  1.00 64.90  ? 302 ILE A O   1 
ATOM   2386  C CB  . ILE A 1 302 ? 40.881  -34.774 -43.264  1.00 67.49  ? 302 ILE A CB  1 
ATOM   2387  C CG1 . ILE A 1 302 ? 39.872  -35.899 -43.028  1.00 68.63  ? 302 ILE A CG1 1 
ATOM   2388  C CG2 . ILE A 1 302 ? 41.498  -34.375 -41.939  1.00 66.99  ? 302 ILE A CG2 1 
ATOM   2389  C CD1 . ILE A 1 302 ? 40.463  -37.080 -42.282  1.00 72.00  ? 302 ILE A CD1 1 
ATOM   2390  N N   . GLY A 1 303 ? 41.414  -31.448 -43.826  1.00 66.66  ? 303 GLY A N   1 
ATOM   2391  C CA  . GLY A 1 303 ? 42.410  -30.461 -44.197  1.00 65.46  ? 303 GLY A CA  1 
ATOM   2392  C C   . GLY A 1 303 ? 41.774  -29.118 -44.484  1.00 76.28  ? 303 GLY A C   1 
ATOM   2393  O O   . GLY A 1 303 ? 40.600  -28.875 -44.188  1.00 78.03  ? 303 GLY A O   1 
ATOM   2394  N N   . GLU A 1 304 ? 42.574  -28.226 -45.069  1.00 85.06  ? 304 GLU A N   1 
ATOM   2395  C CA  . GLU A 1 304 ? 42.089  -26.937 -45.552  1.00 86.93  ? 304 GLU A CA  1 
ATOM   2396  C C   . GLU A 1 304 ? 41.599  -27.141 -46.980  1.00 73.56  ? 304 GLU A C   1 
ATOM   2397  O O   . GLU A 1 304 ? 42.403  -27.359 -47.893  1.00 82.87  ? 304 GLU A O   1 
ATOM   2398  C CB  . GLU A 1 304 ? 43.185  -25.876 -45.487  1.00 75.67  ? 304 GLU A CB  1 
ATOM   2399  C CG  . GLU A 1 304 ? 43.756  -25.639 -44.097  1.00 85.62  ? 304 GLU A CG  1 
ATOM   2400  C CD  . GLU A 1 304 ? 45.108  -26.296 -43.901  1.00 98.46  ? 304 GLU A CD  1 
ATOM   2401  O OE1 . GLU A 1 304 ? 45.220  -27.516 -44.146  1.00 90.83  ? 304 GLU A OE1 1 
ATOM   2402  O OE2 . GLU A 1 304 ? 46.064  -25.588 -43.516  1.00 109.00 ? 304 GLU A OE2 1 
ATOM   2403  N N   . CYS A 1 305 ? 40.291  -27.070 -47.174  1.00 71.73  ? 305 CYS A N   1 
ATOM   2404  C CA  . CYS A 1 305 ? 39.647  -27.533 -48.391  1.00 81.43  ? 305 CYS A CA  1 
ATOM   2405  C C   . CYS A 1 305 ? 38.752  -26.459 -48.983  1.00 70.50  ? 305 CYS A C   1 
ATOM   2406  O O   . CYS A 1 305 ? 38.304  -25.549 -48.277  1.00 74.14  ? 305 CYS A O   1 
ATOM   2407  C CB  . CYS A 1 305 ? 38.813  -28.793 -48.115  1.00 75.45  ? 305 CYS A CB  1 
ATOM   2408  S SG  . CYS A 1 305 ? 39.746  -30.210 -47.500  1.00 89.09  ? 305 CYS A SG  1 
ATOM   2409  N N   . PRO A 1 306 ? 38.482  -26.532 -50.284  1.00 64.88  ? 306 PRO A N   1 
ATOM   2410  C CA  . PRO A 1 306 ? 37.463  -25.663 -50.877  1.00 66.38  ? 306 PRO A CA  1 
ATOM   2411  C C   . PRO A 1 306 ? 36.074  -26.039 -50.386  1.00 60.96  ? 306 PRO A C   1 
ATOM   2412  O O   . PRO A 1 306 ? 35.832  -27.146 -49.899  1.00 64.31  ? 306 PRO A O   1 
ATOM   2413  C CB  . PRO A 1 306 ? 37.602  -25.918 -52.383  1.00 66.16  ? 306 PRO A CB  1 
ATOM   2414  C CG  . PRO A 1 306 ? 38.936  -26.583 -52.552  1.00 56.16  ? 306 PRO A CG  1 
ATOM   2415  C CD  . PRO A 1 306 ? 39.167  -27.351 -51.296  1.00 68.40  ? 306 PRO A CD  1 
ATOM   2416  N N   . LYS A 1 307 ? 35.154  -25.089 -50.514  1.00 55.07  ? 307 LYS A N   1 
ATOM   2417  C CA  . LYS A 1 307 ? 33.776  -25.336 -50.112  1.00 54.09  ? 307 LYS A CA  1 
ATOM   2418  C C   . LYS A 1 307 ? 33.138  -26.373 -51.031  1.00 53.51  ? 307 LYS A C   1 
ATOM   2419  O O   . LYS A 1 307 ? 33.202  -26.257 -52.258  1.00 65.83  ? 307 LYS A O   1 
ATOM   2420  C CB  . LYS A 1 307 ? 32.978  -24.034 -50.136  1.00 47.13  ? 307 LYS A CB  1 
ATOM   2421  C CG  . LYS A 1 307 ? 33.543  -22.958 -49.225  1.00 62.74  ? 307 LYS A CG  1 
ATOM   2422  C CD  . LYS A 1 307 ? 33.537  -23.408 -47.774  1.00 62.24  ? 307 LYS A CD  1 
ATOM   2423  C CE  . LYS A 1 307 ? 34.295  -22.431 -46.892  1.00 68.47  ? 307 LYS A CE  1 
ATOM   2424  N NZ  . LYS A 1 307 ? 35.754  -22.461 -47.190  1.00 73.69  ? 307 LYS A NZ  1 
ATOM   2425  N N   . TYR A 1 308 ? 32.527  -27.391 -50.431  1.00 54.72  ? 308 TYR A N   1 
ATOM   2426  C CA  . TYR A 1 308 ? 31.904  -28.465 -51.191  1.00 54.04  ? 308 TYR A CA  1 
ATOM   2427  C C   . TYR A 1 308 ? 30.548  -28.007 -51.716  1.00 58.58  ? 308 TYR A C   1 
ATOM   2428  O O   . TYR A 1 308 ? 29.705  -27.534 -50.948  1.00 57.69  ? 308 TYR A O   1 
ATOM   2429  C CB  . TYR A 1 308 ? 31.755  -29.710 -50.315  1.00 53.16  ? 308 TYR A CB  1 
ATOM   2430  C CG  . TYR A 1 308 ? 31.096  -30.894 -50.989  1.00 60.10  ? 308 TYR A CG  1 
ATOM   2431  C CD1 . TYR A 1 308 ? 31.667  -31.490 -52.107  1.00 60.15  ? 308 TYR A CD1 1 
ATOM   2432  C CD2 . TYR A 1 308 ? 29.916  -31.432 -50.491  1.00 60.23  ? 308 TYR A CD2 1 
ATOM   2433  C CE1 . TYR A 1 308 ? 31.069  -32.578 -52.720  1.00 60.19  ? 308 TYR A CE1 1 
ATOM   2434  C CE2 . TYR A 1 308 ? 29.312  -32.519 -51.097  1.00 61.88  ? 308 TYR A CE2 1 
ATOM   2435  C CZ  . TYR A 1 308 ? 29.893  -33.088 -52.210  1.00 61.42  ? 308 TYR A CZ  1 
ATOM   2436  O OH  . TYR A 1 308 ? 29.298  -34.169 -52.817  1.00 66.66  ? 308 TYR A OH  1 
ATOM   2437  N N   . VAL A 1 309 ? 30.342  -28.141 -53.028  1.00 58.38  ? 309 VAL A N   1 
ATOM   2438  C CA  . VAL A 1 309 ? 29.120  -27.690 -53.678  1.00 56.67  ? 309 VAL A CA  1 
ATOM   2439  C C   . VAL A 1 309 ? 28.576  -28.806 -54.559  1.00 59.99  ? 309 VAL A C   1 
ATOM   2440  O O   . VAL A 1 309 ? 29.297  -29.719 -54.968  1.00 57.46  ? 309 VAL A O   1 
ATOM   2441  C CB  . VAL A 1 309 ? 29.335  -26.408 -54.514  1.00 54.01  ? 309 VAL A CB  1 
ATOM   2442  C CG1 . VAL A 1 309 ? 29.724  -25.243 -53.619  1.00 65.92  ? 309 VAL A CG1 1 
ATOM   2443  C CG2 . VAL A 1 309 ? 30.387  -26.639 -55.586  1.00 53.22  ? 309 VAL A CG2 1 
ATOM   2444  N N   . LYS A 1 310 ? 27.280  -28.722 -54.841  1.00 58.32  ? 310 LYS A N   1 
ATOM   2445  C CA  . LYS A 1 310 ? 26.604  -29.670 -55.726  1.00 65.28  ? 310 LYS A CA  1 
ATOM   2446  C C   . LYS A 1 310 ? 26.523  -29.102 -57.142  1.00 68.79  ? 310 LYS A C   1 
ATOM   2447  O O   . LYS A 1 310 ? 25.448  -28.864 -57.691  1.00 94.46  ? 310 LYS A O   1 
ATOM   2448  C CB  . LYS A 1 310 ? 25.217  -29.999 -55.182  1.00 73.98  ? 310 LYS A CB  1 
ATOM   2449  C CG  . LYS A 1 310 ? 24.784  -31.442 -55.370  1.00 83.72  ? 310 LYS A CG  1 
ATOM   2450  C CD  . LYS A 1 310 ? 23.340  -31.621 -54.940  1.00 96.84  ? 310 LYS A CD  1 
ATOM   2451  C CE  . LYS A 1 310 ? 23.006  -33.077 -54.684  1.00 108.58 ? 310 LYS A CE  1 
ATOM   2452  N NZ  . LYS A 1 310 ? 22.399  -33.245 -53.334  1.00 106.30 ? 310 LYS A NZ  1 
ATOM   2453  N N   . SER A 1 311 ? 27.693  -28.880 -57.735  1.00 73.51  ? 311 SER A N   1 
ATOM   2454  C CA  . SER A 1 311 ? 27.780  -28.256 -59.046  1.00 62.71  ? 311 SER A CA  1 
ATOM   2455  C C   . SER A 1 311 ? 28.783  -29.012 -59.903  1.00 63.94  ? 311 SER A C   1 
ATOM   2456  O O   . SER A 1 311 ? 29.791  -29.510 -59.394  1.00 75.65  ? 311 SER A O   1 
ATOM   2457  C CB  . SER A 1 311 ? 28.187  -26.781 -58.925  1.00 66.25  ? 311 SER A CB  1 
ATOM   2458  O OG  . SER A 1 311 ? 27.705  -26.022 -60.020  1.00 97.53  ? 311 SER A OG  1 
ATOM   2459  N N   . ASN A 1 312 ? 28.502  -29.099 -61.202  1.00 78.21  ? 312 ASN A N   1 
ATOM   2460  C CA  . ASN A 1 312 ? 29.396  -29.754 -62.149  1.00 80.71  ? 312 ASN A CA  1 
ATOM   2461  C C   . ASN A 1 312 ? 30.199  -28.771 -62.989  1.00 66.83  ? 312 ASN A C   1 
ATOM   2462  O O   . ASN A 1 312 ? 31.055  -29.202 -63.768  1.00 79.95  ? 312 ASN A O   1 
ATOM   2463  C CB  . ASN A 1 312 ? 28.608  -30.684 -63.081  1.00 69.63  ? 312 ASN A CB  1 
ATOM   2464  C CG  . ASN A 1 312 ? 28.217  -31.988 -62.415  1.00 93.48  ? 312 ASN A CG  1 
ATOM   2465  O OD1 . ASN A 1 312 ? 29.060  -32.851 -62.169  1.00 105.12 ? 312 ASN A OD1 1 
ATOM   2466  N ND2 . ASN A 1 312 ? 26.930  -32.144 -62.132  1.00 94.60  ? 312 ASN A ND2 1 
ATOM   2467  N N   . LYS A 1 313 ? 29.951  -27.470 -62.852  1.00 66.77  ? 313 LYS A N   1 
ATOM   2468  C CA  . LYS A 1 313 ? 30.587  -26.483 -63.714  1.00 67.14  ? 313 LYS A CA  1 
ATOM   2469  C C   . LYS A 1 313 ? 30.463  -25.108 -63.074  1.00 75.30  ? 313 LYS A C   1 
ATOM   2470  O O   . LYS A 1 313 ? 29.357  -24.682 -62.728  1.00 87.94  ? 313 LYS A O   1 
ATOM   2471  C CB  . LYS A 1 313 ? 29.945  -26.494 -65.108  1.00 78.59  ? 313 LYS A CB  1 
ATOM   2472  C CG  . LYS A 1 313 ? 30.616  -25.590 -66.119  1.00 83.59  ? 313 LYS A CG  1 
ATOM   2473  C CD  . LYS A 1 313 ? 29.816  -25.511 -67.407  1.00 98.44  ? 313 LYS A CD  1 
ATOM   2474  C CE  . LYS A 1 313 ? 30.225  -24.292 -68.217  1.00 104.58 ? 313 LYS A CE  1 
ATOM   2475  N NZ  . LYS A 1 313 ? 29.489  -24.184 -69.506  1.00 89.16  ? 313 LYS A NZ  1 
ATOM   2476  N N   . LEU A 1 314 ? 31.600  -24.424 -62.908  1.00 66.54  ? 314 LEU A N   1 
ATOM   2477  C CA  . LEU A 1 314 ? 31.643  -23.044 -62.411  1.00 75.39  ? 314 LEU A CA  1 
ATOM   2478  C C   . LEU A 1 314 ? 32.684  -22.303 -63.248  1.00 78.23  ? 314 LEU A C   1 
ATOM   2479  O O   . LEU A 1 314 ? 33.854  -22.216 -62.867  1.00 83.73  ? 314 LEU A O   1 
ATOM   2480  C CB  . LEU A 1 314 ? 31.975  -22.989 -60.926  1.00 80.58  ? 314 LEU A CB  1 
ATOM   2481  C CG  . LEU A 1 314 ? 30.883  -23.394 -59.935  1.00 61.56  ? 314 LEU A CG  1 
ATOM   2482  C CD1 . LEU A 1 314 ? 31.422  -23.384 -58.511  1.00 68.35  ? 314 LEU A CD1 1 
ATOM   2483  C CD2 . LEU A 1 314 ? 29.681  -22.473 -60.060  1.00 65.31  ? 314 LEU A CD2 1 
ATOM   2484  N N   . VAL A 1 315 ? 32.247  -21.746 -64.373  1.00 73.57  ? 315 VAL A N   1 
ATOM   2485  C CA  . VAL A 1 315 ? 33.146  -21.147 -65.353  1.00 65.35  ? 315 VAL A CA  1 
ATOM   2486  C C   . VAL A 1 315 ? 32.886  -19.648 -65.393  1.00 71.35  ? 315 VAL A C   1 
ATOM   2487  O O   . VAL A 1 315 ? 31.755  -19.210 -65.640  1.00 65.68  ? 315 VAL A O   1 
ATOM   2488  C CB  . VAL A 1 315 ? 32.969  -21.782 -66.739  1.00 64.49  ? 315 VAL A CB  1 
ATOM   2489  C CG1 . VAL A 1 315 ? 33.873  -21.105 -67.745  1.00 79.24  ? 315 VAL A CG1 1 
ATOM   2490  C CG2 . VAL A 1 315 ? 33.279  -23.266 -66.674  1.00 74.30  ? 315 VAL A CG2 1 
ATOM   2491  N N   . LEU A 1 316 ? 33.934  -18.865 -65.149  1.00 69.44  ? 316 LEU A N   1 
ATOM   2492  C CA  . LEU A 1 316 ? 33.856  -17.412 -65.203  1.00 59.57  ? 316 LEU A CA  1 
ATOM   2493  C C   . LEU A 1 316 ? 34.264  -16.924 -66.585  1.00 80.26  ? 316 LEU A C   1 
ATOM   2494  O O   . LEU A 1 316 ? 35.285  -17.359 -67.129  1.00 73.64  ? 316 LEU A O   1 
ATOM   2495  C CB  . LEU A 1 316 ? 34.758  -16.778 -64.142  1.00 52.61  ? 316 LEU A CB  1 
ATOM   2496  C CG  . LEU A 1 316 ? 34.156  -16.518 -62.763  1.00 66.13  ? 316 LEU A CG  1 
ATOM   2497  C CD1 . LEU A 1 316 ? 35.182  -15.855 -61.859  1.00 59.06  ? 316 LEU A CD1 1 
ATOM   2498  C CD2 . LEU A 1 316 ? 32.915  -15.656 -62.890  1.00 57.48  ? 316 LEU A CD2 1 
ATOM   2499  N N   . ALA A 1 317 ? 33.467  -16.021 -67.148  1.00 82.85  ? 317 ALA A N   1 
ATOM   2500  C CA  . ALA A 1 317 ? 33.808  -15.389 -68.416  1.00 82.61  ? 317 ALA A CA  1 
ATOM   2501  C C   . ALA A 1 317 ? 34.853  -14.308 -68.171  1.00 81.28  ? 317 ALA A C   1 
ATOM   2502  O O   . ALA A 1 317 ? 34.610  -13.365 -67.410  1.00 85.98  ? 317 ALA A O   1 
ATOM   2503  C CB  . ALA A 1 317 ? 32.562  -14.798 -69.071  1.00 64.18  ? 317 ALA A CB  1 
ATOM   2504  N N   . THR A 1 318 ? 36.018  -14.447 -68.807  1.00 79.08  ? 318 THR A N   1 
ATOM   2505  C CA  . THR A 1 318 ? 37.070  -13.445 -68.713  1.00 83.99  ? 318 THR A CA  1 
ATOM   2506  C C   . THR A 1 318 ? 37.357  -12.737 -70.029  1.00 80.85  ? 318 THR A C   1 
ATOM   2507  O O   . THR A 1 318 ? 37.948  -11.653 -70.009  1.00 89.09  ? 318 THR A O   1 
ATOM   2508  C CB  . THR A 1 318 ? 38.371  -14.076 -68.192  1.00 71.63  ? 318 THR A CB  1 
ATOM   2509  O OG1 . THR A 1 318 ? 39.411  -13.091 -68.180  1.00 98.53  ? 318 THR A OG1 1 
ATOM   2510  C CG2 . THR A 1 318 ? 38.799  -15.239 -69.070  1.00 70.39  ? 318 THR A CG2 1 
ATOM   2511  N N   . GLY A 1 319 ? 36.952  -13.311 -71.163  1.00 82.76  ? 319 GLY A N   1 
ATOM   2512  C CA  . GLY A 1 319 ? 37.158  -12.702 -72.457  1.00 90.58  ? 319 GLY A CA  1 
ATOM   2513  C C   . GLY A 1 319 ? 35.897  -12.058 -73.008  1.00 82.63  ? 319 GLY A C   1 
ATOM   2514  O O   . GLY A 1 319 ? 34.881  -11.911 -72.326  1.00 74.07  ? 319 GLY A O   1 
ATOM   2515  N N   . LEU A 1 320 ? 35.976  -11.666 -74.278  1.00 76.48  ? 320 LEU A N   1 
ATOM   2516  C CA  . LEU A 1 320 ? 34.848  -11.027 -74.936  1.00 74.48  ? 320 LEU A CA  1 
ATOM   2517  C C   . LEU A 1 320 ? 33.869  -12.073 -75.457  1.00 73.36  ? 320 LEU A C   1 
ATOM   2518  O O   . LEU A 1 320 ? 34.192  -13.256 -75.587  1.00 66.88  ? 320 LEU A O   1 
ATOM   2519  C CB  . LEU A 1 320 ? 35.302  -10.149 -76.106  1.00 73.62  ? 320 LEU A CB  1 
ATOM   2520  C CG  . LEU A 1 320 ? 36.477  -9.168  -76.030  1.00 75.53  ? 320 LEU A CG  1 
ATOM   2521  C CD1 . LEU A 1 320 ? 36.266  -8.057  -77.041  1.00 82.50  ? 320 LEU A CD1 1 
ATOM   2522  C CD2 . LEU A 1 320 ? 36.680  -8.585  -74.647  1.00 84.66  ? 320 LEU A CD2 1 
ATOM   2523  N N   . ARG A 1 321 ? 32.656  -11.618 -75.760  1.00 67.74  ? 321 ARG A N   1 
ATOM   2524  C CA  . ARG A 1 321 ? 31.693  -12.462 -76.453  1.00 70.73  ? 321 ARG A CA  1 
ATOM   2525  C C   . ARG A 1 321 ? 32.197  -12.765 -77.859  1.00 81.28  ? 321 ARG A C   1 
ATOM   2526  O O   . ARG A 1 321 ? 32.772  -11.901 -78.528  1.00 95.23  ? 321 ARG A O   1 
ATOM   2527  C CB  . ARG A 1 321 ? 30.329  -11.771 -76.508  1.00 69.52  ? 321 ARG A CB  1 
ATOM   2528  C CG  . ARG A 1 321 ? 29.151  -12.699 -76.768  1.00 80.69  ? 321 ARG A CG  1 
ATOM   2529  C CD  . ARG A 1 321 ? 27.862  -11.903 -76.933  1.00 101.66 ? 321 ARG A CD  1 
ATOM   2530  N NE  . ARG A 1 321 ? 27.563  -11.082 -75.764  1.00 91.36  ? 321 ARG A NE  1 
ATOM   2531  C CZ  . ARG A 1 321 ? 26.565  -11.310 -74.921  1.00 90.49  ? 321 ARG A CZ  1 
ATOM   2532  N NH1 . ARG A 1 321 ? 25.726  -12.318 -75.097  1.00 88.58  ? 321 ARG A NH1 1 
ATOM   2533  N NH2 . ARG A 1 321 ? 26.399  -10.500 -73.878  1.00 74.01  ? 321 ARG A NH2 1 
ATOM   2534  N N   . ASN A 1 322 ? 31.989  -13.999 -78.307  1.00 88.83  ? 322 ASN A N   1 
ATOM   2535  C CA  . ASN A 1 322 ? 32.542  -14.473 -79.567  1.00 83.41  ? 322 ASN A CA  1 
ATOM   2536  C C   . ASN A 1 322 ? 31.425  -14.949 -80.486  1.00 98.31  ? 322 ASN A C   1 
ATOM   2537  O O   . ASN A 1 322 ? 30.469  -15.590 -80.038  1.00 116.82 ? 322 ASN A O   1 
ATOM   2538  C CB  . ASN A 1 322 ? 33.547  -15.606 -79.335  1.00 75.29  ? 322 ASN A CB  1 
ATOM   2539  C CG  . ASN A 1 322 ? 34.752  -15.514 -80.251  1.00 79.45  ? 322 ASN A CG  1 
ATOM   2540  O OD1 . ASN A 1 322 ? 34.717  -14.833 -81.276  1.00 98.02  ? 322 ASN A OD1 1 
ATOM   2541  N ND2 . ASN A 1 322 ? 35.826  -16.203 -79.886  1.00 88.90  ? 322 ASN A ND2 1 
ATOM   2542  N N   . SER A 1 323 ? 31.553  -14.629 -81.770  1.00 112.20 ? 323 SER A N   1 
ATOM   2543  C CA  . SER A 1 323 ? 30.575  -15.044 -82.771  1.00 114.92 ? 323 SER A CA  1 
ATOM   2544  C C   . SER A 1 323 ? 31.254  -15.357 -84.101  1.00 108.46 ? 323 SER A C   1 
ATOM   2545  O O   . SER A 1 323 ? 32.199  -16.145 -84.157  1.00 111.57 ? 323 SER A O   1 
ATOM   2546  C CB  . SER A 1 323 ? 29.512  -13.962 -82.965  1.00 104.90 ? 323 SER A CB  1 
ATOM   2547  O OG  . SER A 1 323 ? 28.828  -13.695 -81.753  1.00 118.65 ? 323 SER A OG  1 
ATOM   2548  N N   . ILE B 2 6   ? 28.107  -3.641  -81.215  1.00 137.31 ? 6   ILE B N   1 
ATOM   2549  C CA  . ILE B 2 6   ? 27.817  -4.159  -79.884  1.00 137.30 ? 6   ILE B CA  1 
ATOM   2550  C C   . ILE B 2 6   ? 26.415  -3.745  -79.437  1.00 144.79 ? 6   ILE B C   1 
ATOM   2551  O O   . ILE B 2 6   ? 25.520  -4.583  -79.323  1.00 147.86 ? 6   ILE B O   1 
ATOM   2552  C CB  . ILE B 2 6   ? 28.881  -3.700  -78.871  1.00 109.45 ? 6   ILE B CB  1 
ATOM   2553  C CG1 . ILE B 2 6   ? 29.329  -2.270  -79.173  1.00 122.89 ? 6   ILE B CG1 1 
ATOM   2554  C CG2 . ILE B 2 6   ? 30.080  -4.628  -78.910  1.00 80.40  ? 6   ILE B CG2 1 
ATOM   2555  C CD1 . ILE B 2 6   ? 29.805  -1.522  -77.969  1.00 97.37  ? 6   ILE B CD1 1 
ATOM   2556  N N   . ALA B 2 7   ? 26.225  -2.448  -79.189  1.00 137.43 ? 7   ALA B N   1 
ATOM   2557  C CA  . ALA B 2 7   ? 24.937  -1.916  -78.743  1.00 134.33 ? 7   ALA B CA  1 
ATOM   2558  C C   . ALA B 2 7   ? 24.030  -1.651  -79.948  1.00 144.99 ? 7   ALA B C   1 
ATOM   2559  O O   . ALA B 2 7   ? 23.623  -0.525  -80.232  1.00 137.15 ? 7   ALA B O   1 
ATOM   2560  C CB  . ALA B 2 7   ? 25.147  -0.655  -77.914  1.00 86.12  ? 7   ALA B CB  1 
ATOM   2561  N N   . GLY B 2 8   ? 23.721  -2.731  -80.665  1.00 149.70 ? 8   GLY B N   1 
ATOM   2562  C CA  . GLY B 2 8   ? 23.012  -2.608  -81.924  1.00 128.89 ? 8   GLY B CA  1 
ATOM   2563  C C   . GLY B 2 8   ? 23.760  -1.805  -82.959  1.00 136.84 ? 8   GLY B C   1 
ATOM   2564  O O   . GLY B 2 8   ? 23.159  -1.334  -83.927  1.00 132.52 ? 8   GLY B O   1 
ATOM   2565  N N   . PHE B 2 9   ? 25.071  -1.643  -82.780  1.00 142.83 ? 9   PHE B N   1 
ATOM   2566  C CA  . PHE B 2 9   ? 25.864  -0.701  -83.559  1.00 126.73 ? 9   PHE B CA  1 
ATOM   2567  C C   . PHE B 2 9   ? 26.900  -1.401  -84.427  1.00 116.82 ? 9   PHE B C   1 
ATOM   2568  O O   . PHE B 2 9   ? 26.898  -1.224  -85.649  1.00 102.60 ? 9   PHE B O   1 
ATOM   2569  C CB  . PHE B 2 9   ? 26.545  0.283   -82.599  1.00 127.92 ? 9   PHE B CB  1 
ATOM   2570  C CG  . PHE B 2 9   ? 26.787  1.641   -83.183  1.00 130.29 ? 9   PHE B CG  1 
ATOM   2571  C CD1 . PHE B 2 9   ? 27.588  1.801   -84.301  1.00 122.27 ? 9   PHE B CD1 1 
ATOM   2572  C CD2 . PHE B 2 9   ? 26.228  2.762   -82.594  1.00 117.88 ? 9   PHE B CD2 1 
ATOM   2573  C CE1 . PHE B 2 9   ? 27.814  3.053   -84.831  1.00 120.28 ? 9   PHE B CE1 1 
ATOM   2574  C CE2 . PHE B 2 9   ? 26.452  4.015   -83.116  1.00 117.76 ? 9   PHE B CE2 1 
ATOM   2575  C CZ  . PHE B 2 9   ? 27.246  4.162   -84.235  1.00 131.74 ? 9   PHE B CZ  1 
ATOM   2576  N N   . ILE B 2 10  ? 27.778  -2.201  -83.829  1.00 121.79 ? 10  ILE B N   1 
ATOM   2577  C CA  . ILE B 2 10  ? 28.881  -2.848  -84.528  1.00 119.49 ? 10  ILE B CA  1 
ATOM   2578  C C   . ILE B 2 10  ? 28.560  -4.329  -84.649  1.00 130.89 ? 10  ILE B C   1 
ATOM   2579  O O   . ILE B 2 10  ? 28.242  -4.982  -83.648  1.00 130.97 ? 10  ILE B O   1 
ATOM   2580  C CB  . ILE B 2 10  ? 30.219  -2.634  -83.796  1.00 109.98 ? 10  ILE B CB  1 
ATOM   2581  C CG1 . ILE B 2 10  ? 30.519  -1.142  -83.632  1.00 104.96 ? 10  ILE B CG1 1 
ATOM   2582  C CG2 . ILE B 2 10  ? 31.353  -3.326  -84.535  1.00 100.74 ? 10  ILE B CG2 1 
ATOM   2583  C CD1 . ILE B 2 10  ? 30.193  -0.594  -82.261  1.00 72.87  ? 10  ILE B CD1 1 
ATOM   2584  N N   . GLU B 2 11  ? 28.634  -4.855  -85.876  1.00 129.19 ? 11  GLU B N   1 
ATOM   2585  C CA  . GLU B 2 11  ? 28.479  -6.293  -86.064  1.00 122.56 ? 11  GLU B CA  1 
ATOM   2586  C C   . GLU B 2 11  ? 29.513  -7.055  -85.247  1.00 127.84 ? 11  GLU B C   1 
ATOM   2587  O O   . GLU B 2 11  ? 29.193  -8.063  -84.605  1.00 135.25 ? 11  GLU B O   1 
ATOM   2588  C CB  . GLU B 2 11  ? 28.592  -6.649  -87.546  1.00 121.59 ? 11  GLU B CB  1 
ATOM   2589  C CG  . GLU B 2 11  ? 28.755  -8.138  -87.804  1.00 134.17 ? 11  GLU B CG  1 
ATOM   2590  C CD  . GLU B 2 11  ? 28.533  -8.512  -89.256  1.00 147.94 ? 11  GLU B CD  1 
ATOM   2591  O OE1 . GLU B 2 11  ? 28.151  -7.628  -90.051  1.00 147.90 ? 11  GLU B OE1 1 
ATOM   2592  O OE2 . GLU B 2 11  ? 28.738  -9.695  -89.602  1.00 134.43 ? 11  GLU B OE2 1 
ATOM   2593  N N   . GLY B 2 12  ? 30.753  -6.588  -85.258  1.00 127.49 ? 12  GLY B N   1 
ATOM   2594  C CA  . GLY B 2 12  ? 31.744  -7.032  -84.307  1.00 110.30 ? 12  GLY B CA  1 
ATOM   2595  C C   . GLY B 2 12  ? 32.433  -8.322  -84.713  1.00 99.08  ? 12  GLY B C   1 
ATOM   2596  O O   . GLY B 2 12  ? 31.929  -9.122  -85.500  1.00 107.04 ? 12  GLY B O   1 
ATOM   2597  N N   . GLY B 2 13  ? 33.618  -8.517  -84.145  1.00 92.37  ? 13  GLY B N   1 
ATOM   2598  C CA  . GLY B 2 13  ? 34.416  -9.694  -84.414  1.00 90.97  ? 13  GLY B CA  1 
ATOM   2599  C C   . GLY B 2 13  ? 35.528  -9.410  -85.398  1.00 86.35  ? 13  GLY B C   1 
ATOM   2600  O O   . GLY B 2 13  ? 35.304  -9.390  -86.612  1.00 100.00 ? 13  GLY B O   1 
ATOM   2601  N N   . TRP B 2 14  ? 36.735  -9.190  -84.886  1.00 83.90  ? 14  TRP B N   1 
ATOM   2602  C CA  . TRP B 2 14  ? 37.914  -8.936  -85.709  1.00 84.52  ? 14  TRP B CA  1 
ATOM   2603  C C   . TRP B 2 14  ? 38.917  -10.052 -85.444  1.00 84.98  ? 14  TRP B C   1 
ATOM   2604  O O   . TRP B 2 14  ? 39.674  -9.997  -84.470  1.00 86.31  ? 14  TRP B O   1 
ATOM   2605  C CB  . TRP B 2 14  ? 38.520  -7.567  -85.412  1.00 85.81  ? 14  TRP B CB  1 
ATOM   2606  C CG  . TRP B 2 14  ? 37.824  -6.427  -86.094  1.00 76.42  ? 14  TRP B CG  1 
ATOM   2607  C CD1 . TRP B 2 14  ? 36.801  -6.508  -86.994  1.00 62.89  ? 14  TRP B CD1 1 
ATOM   2608  C CD2 . TRP B 2 14  ? 38.105  -5.032  -85.929  1.00 68.63  ? 14  TRP B CD2 1 
ATOM   2609  N NE1 . TRP B 2 14  ? 36.426  -5.249  -87.398  1.00 54.17  ? 14  TRP B NE1 1 
ATOM   2610  C CE2 . TRP B 2 14  ? 37.211  -4.326  -86.759  1.00 69.14  ? 14  TRP B CE2 1 
ATOM   2611  C CE3 . TRP B 2 14  ? 39.024  -4.313  -85.159  1.00 70.41  ? 14  TRP B CE3 1 
ATOM   2612  C CZ2 . TRP B 2 14  ? 37.210  -2.935  -86.840  1.00 70.03  ? 14  TRP B CZ2 1 
ATOM   2613  C CZ3 . TRP B 2 14  ? 39.022  -2.932  -85.242  1.00 79.98  ? 14  TRP B CZ3 1 
ATOM   2614  C CH2 . TRP B 2 14  ? 38.121  -2.258  -86.076  1.00 77.39  ? 14  TRP B CH2 1 
ATOM   2615  N N   . GLN B 2 15  ? 38.917  -11.069 -86.310  1.00 90.05  ? 15  GLN B N   1 
ATOM   2616  C CA  . GLN B 2 15  ? 39.954  -12.091 -86.237  1.00 84.31  ? 15  GLN B CA  1 
ATOM   2617  C C   . GLN B 2 15  ? 41.331  -11.495 -86.494  1.00 93.42  ? 15  GLN B C   1 
ATOM   2618  O O   . GLN B 2 15  ? 42.329  -11.976 -85.944  1.00 96.76  ? 15  GLN B O   1 
ATOM   2619  C CB  . GLN B 2 15  ? 39.661  -13.212 -87.236  1.00 84.01  ? 15  GLN B CB  1 
ATOM   2620  C CG  . GLN B 2 15  ? 38.407  -14.014 -86.922  1.00 78.54  ? 15  GLN B CG  1 
ATOM   2621  C CD  . GLN B 2 15  ? 38.578  -14.913 -85.713  1.00 93.28  ? 15  GLN B CD  1 
ATOM   2622  O OE1 . GLN B 2 15  ? 39.644  -15.492 -85.501  1.00 94.12  ? 15  GLN B OE1 1 
ATOM   2623  N NE2 . GLN B 2 15  ? 37.527  -15.033 -84.910  1.00 93.49  ? 15  GLN B NE2 1 
ATOM   2624  N N   . GLY B 2 16  ? 41.404  -10.451 -87.322  1.00 106.10 ? 16  GLY B N   1 
ATOM   2625  C CA  . GLY B 2 16  ? 42.684  -9.817  -87.594  1.00 105.15 ? 16  GLY B CA  1 
ATOM   2626  C C   . GLY B 2 16  ? 43.289  -9.167  -86.366  1.00 97.20  ? 16  GLY B C   1 
ATOM   2627  O O   . GLY B 2 16  ? 44.512  -9.164  -86.191  1.00 110.68 ? 16  GLY B O   1 
ATOM   2628  N N   . MET B 2 17  ? 42.447  -8.609  -85.500  1.00 93.60  ? 17  MET B N   1 
ATOM   2629  C CA  . MET B 2 17  ? 42.924  -8.012  -84.261  1.00 101.46 ? 17  MET B CA  1 
ATOM   2630  C C   . MET B 2 17  ? 43.304  -9.117  -83.285  1.00 114.03 ? 17  MET B C   1 
ATOM   2631  O O   . MET B 2 17  ? 42.441  -9.865  -82.817  1.00 111.12 ? 17  MET B O   1 
ATOM   2632  C CB  . MET B 2 17  ? 41.863  -7.111  -83.649  1.00 83.15  ? 17  MET B CB  1 
ATOM   2633  C CG  . MET B 2 17  ? 42.287  -6.638  -82.289  1.00 100.20 ? 17  MET B CG  1 
ATOM   2634  S SD  . MET B 2 17  ? 42.760  -4.910  -82.305  1.00 108.45 ? 17  MET B SD  1 
ATOM   2635  C CE  . MET B 2 17  ? 41.181  -4.206  -81.905  1.00 89.04  ? 17  MET B CE  1 
ATOM   2636  N N   . VAL B 2 18  ? 44.591  -9.204  -82.955  1.00 115.19 ? 18  VAL B N   1 
ATOM   2637  C CA  . VAL B 2 18  ? 45.084  -10.277 -82.099  1.00 117.73 ? 18  VAL B CA  1 
ATOM   2638  C C   . VAL B 2 18  ? 45.951  -9.707  -80.985  1.00 110.71 ? 18  VAL B C   1 
ATOM   2639  O O   . VAL B 2 18  ? 46.363  -10.435 -80.076  1.00 117.79 ? 18  VAL B O   1 
ATOM   2640  C CB  . VAL B 2 18  ? 45.868  -11.320 -82.917  1.00 116.01 ? 18  VAL B CB  1 
ATOM   2641  C CG1 . VAL B 2 18  ? 44.949  -12.036 -83.895  1.00 98.60  ? 18  VAL B CG1 1 
ATOM   2642  C CG2 . VAL B 2 18  ? 47.025  -10.658 -83.651  1.00 101.52 ? 18  VAL B CG2 1 
ATOM   2643  N N   . ASP B 2 19  ? 46.240  -8.409  -81.047  1.00 110.32 ? 19  ASP B N   1 
ATOM   2644  C CA  . ASP B 2 19  ? 47.148  -7.779  -80.099  1.00 128.71 ? 19  ASP B CA  1 
ATOM   2645  C C   . ASP B 2 19  ? 46.433  -6.994  -79.005  1.00 124.74 ? 19  ASP B C   1 
ATOM   2646  O O   . ASP B 2 19  ? 47.101  -6.372  -78.174  1.00 120.19 ? 19  ASP B O   1 
ATOM   2647  C CB  . ASP B 2 19  ? 48.124  -6.859  -80.841  1.00 134.78 ? 19  ASP B CB  1 
ATOM   2648  C CG  . ASP B 2 19  ? 49.490  -6.810  -80.184  1.00 147.04 ? 19  ASP B CG  1 
ATOM   2649  O OD1 . ASP B 2 19  ? 50.151  -7.867  -80.111  1.00 140.39 ? 19  ASP B OD1 1 
ATOM   2650  O OD2 . ASP B 2 19  ? 49.903  -5.716  -79.744  1.00 144.43 ? 19  ASP B OD2 1 
ATOM   2651  N N   . GLY B 2 20  ? 45.104  -7.005  -78.979  1.00 111.56 ? 20  GLY B N   1 
ATOM   2652  C CA  . GLY B 2 20  ? 44.378  -6.285  -77.952  1.00 83.16  ? 20  GLY B CA  1 
ATOM   2653  C C   . GLY B 2 20  ? 42.909  -6.637  -77.965  1.00 82.66  ? 20  GLY B C   1 
ATOM   2654  O O   . GLY B 2 20  ? 42.396  -7.212  -78.929  1.00 96.08  ? 20  GLY B O   1 
ATOM   2655  N N   . TRP B 2 21  ? 42.238  -6.287  -76.866  1.00 83.88  ? 21  TRP B N   1 
ATOM   2656  C CA  . TRP B 2 21  ? 40.800  -6.515  -76.762  1.00 80.62  ? 21  TRP B CA  1 
ATOM   2657  C C   . TRP B 2 21  ? 40.002  -5.500  -77.576  1.00 83.22  ? 21  TRP B C   1 
ATOM   2658  O O   . TRP B 2 21  ? 39.060  -5.874  -78.282  1.00 68.81  ? 21  TRP B O   1 
ATOM   2659  C CB  . TRP B 2 21  ? 40.367  -6.478  -75.294  1.00 78.62  ? 21  TRP B CB  1 
ATOM   2660  C CG  . TRP B 2 21  ? 40.544  -7.787  -74.581  1.00 79.12  ? 21  TRP B CG  1 
ATOM   2661  C CD1 . TRP B 2 21  ? 40.872  -8.988  -75.142  1.00 84.12  ? 21  TRP B CD1 1 
ATOM   2662  C CD2 . TRP B 2 21  ? 40.399  -8.027  -73.176  1.00 79.66  ? 21  TRP B CD2 1 
ATOM   2663  N NE1 . TRP B 2 21  ? 40.940  -9.960  -74.172  1.00 81.96  ? 21  TRP B NE1 1 
ATOM   2664  C CE2 . TRP B 2 21  ? 40.654  -9.395  -72.957  1.00 82.52  ? 21  TRP B CE2 1 
ATOM   2665  C CE3 . TRP B 2 21  ? 40.079  -7.218  -72.082  1.00 85.44  ? 21  TRP B CE3 1 
ATOM   2666  C CZ2 . TRP B 2 21  ? 40.599  -9.972  -71.690  1.00 74.90  ? 21  TRP B CZ2 1 
ATOM   2667  C CZ3 . TRP B 2 21  ? 40.024  -7.793  -70.824  1.00 80.07  ? 21  TRP B CZ3 1 
ATOM   2668  C CH2 . TRP B 2 21  ? 40.283  -9.156  -70.639  1.00 78.19  ? 21  TRP B CH2 1 
ATOM   2669  N N   . TYR B 2 22  ? 40.362  -4.218  -77.490  1.00 86.83  ? 22  TYR B N   1 
ATOM   2670  C CA  . TYR B 2 22  ? 39.677  -3.157  -78.216  1.00 85.21  ? 22  TYR B CA  1 
ATOM   2671  C C   . TYR B 2 22  ? 40.693  -2.334  -78.995  1.00 89.22  ? 22  TYR B C   1 
ATOM   2672  O O   . TYR B 2 22  ? 41.885  -2.316  -78.680  1.00 90.34  ? 22  TYR B O   1 
ATOM   2673  C CB  . TYR B 2 22  ? 38.880  -2.236  -77.278  1.00 80.17  ? 22  TYR B CB  1 
ATOM   2674  C CG  . TYR B 2 22  ? 38.394  -2.890  -76.001  1.00 90.32  ? 22  TYR B CG  1 
ATOM   2675  C CD1 . TYR B 2 22  ? 37.504  -3.957  -76.034  1.00 81.53  ? 22  TYR B CD1 1 
ATOM   2676  C CD2 . TYR B 2 22  ? 38.814  -2.427  -74.760  1.00 80.57  ? 22  TYR B CD2 1 
ATOM   2677  C CE1 . TYR B 2 22  ? 37.059  -4.553  -74.869  1.00 80.75  ? 22  TYR B CE1 1 
ATOM   2678  C CE2 . TYR B 2 22  ? 38.373  -3.014  -73.592  1.00 78.77  ? 22  TYR B CE2 1 
ATOM   2679  C CZ  . TYR B 2 22  ? 37.497  -4.076  -73.652  1.00 80.88  ? 22  TYR B CZ  1 
ATOM   2680  O OH  . TYR B 2 22  ? 37.056  -4.662  -72.488  1.00 83.46  ? 22  TYR B OH  1 
ATOM   2681  N N   . GLY B 2 23  ? 40.207  -1.647  -80.023  1.00 83.23  ? 23  GLY B N   1 
ATOM   2682  C CA  . GLY B 2 23  ? 41.087  -0.849  -80.857  1.00 87.56  ? 23  GLY B CA  1 
ATOM   2683  C C   . GLY B 2 23  ? 40.420  -0.487  -82.172  1.00 72.57  ? 23  GLY B C   1 
ATOM   2684  O O   . GLY B 2 23  ? 39.192  -0.460  -82.276  1.00 74.29  ? 23  GLY B O   1 
ATOM   2685  N N   . TYR B 2 24  ? 41.256  -0.233  -83.179  1.00 75.68  ? 24  TYR B N   1 
ATOM   2686  C CA  . TYR B 2 24  ? 40.823  0.429   -84.401  1.00 54.76  ? 24  TYR B CA  1 
ATOM   2687  C C   . TYR B 2 24  ? 41.251  -0.339  -85.646  1.00 66.30  ? 24  TYR B C   1 
ATOM   2688  O O   . TYR B 2 24  ? 42.109  -1.226  -85.605  1.00 75.34  ? 24  TYR B O   1 
ATOM   2689  C CB  . TYR B 2 24  ? 41.391  1.853   -84.488  1.00 61.11  ? 24  TYR B CB  1 
ATOM   2690  C CG  . TYR B 2 24  ? 41.379  2.618   -83.185  1.00 59.17  ? 24  TYR B CG  1 
ATOM   2691  C CD1 . TYR B 2 24  ? 42.403  2.466   -82.259  1.00 58.32  ? 24  TYR B CD1 1 
ATOM   2692  C CD2 . TYR B 2 24  ? 40.356  3.508   -82.888  1.00 56.98  ? 24  TYR B CD2 1 
ATOM   2693  C CE1 . TYR B 2 24  ? 42.401  3.167   -81.071  1.00 60.21  ? 24  TYR B CE1 1 
ATOM   2694  C CE2 . TYR B 2 24  ? 40.345  4.216   -81.700  1.00 57.93  ? 24  TYR B CE2 1 
ATOM   2695  C CZ  . TYR B 2 24  ? 41.371  4.042   -80.796  1.00 55.36  ? 24  TYR B CZ  1 
ATOM   2696  O OH  . TYR B 2 24  ? 41.368  4.744   -79.613  1.00 69.99  ? 24  TYR B OH  1 
ATOM   2697  N N   . HIS B 2 25  ? 40.621  0.024   -86.762  1.00 71.60  ? 25  HIS B N   1 
ATOM   2698  C CA  . HIS B 2 25  ? 41.073  -0.331  -88.099  1.00 65.04  ? 25  HIS B CA  1 
ATOM   2699  C C   . HIS B 2 25  ? 40.944  0.901   -88.981  1.00 73.20  ? 25  HIS B C   1 
ATOM   2700  O O   . HIS B 2 25  ? 39.934  1.609   -88.922  1.00 73.99  ? 25  HIS B O   1 
ATOM   2701  C CB  . HIS B 2 25  ? 40.270  -1.494  -88.694  1.00 60.79  ? 25  HIS B CB  1 
ATOM   2702  C CG  . HIS B 2 25  ? 40.680  -1.861  -90.087  1.00 66.90  ? 25  HIS B CG  1 
ATOM   2703  N ND1 . HIS B 2 25  ? 40.058  -1.349  -91.205  1.00 81.98  ? 25  HIS B ND1 1 
ATOM   2704  C CD2 . HIS B 2 25  ? 41.652  -2.687  -90.543  1.00 70.71  ? 25  HIS B CD2 1 
ATOM   2705  C CE1 . HIS B 2 25  ? 40.626  -1.845  -92.289  1.00 79.22  ? 25  HIS B CE1 1 
ATOM   2706  N NE2 . HIS B 2 25  ? 41.596  -2.660  -91.915  1.00 80.27  ? 25  HIS B NE2 1 
ATOM   2707  N N   . HIS B 2 26  ? 41.968  1.160   -89.789  1.00 80.27  ? 26  HIS B N   1 
ATOM   2708  C CA  . HIS B 2 26  ? 42.006  2.347   -90.630  1.00 69.32  ? 26  HIS B CA  1 
ATOM   2709  C C   . HIS B 2 26  ? 42.257  1.942   -92.076  1.00 78.80  ? 26  HIS B C   1 
ATOM   2710  O O   . HIS B 2 26  ? 42.625  0.803   -92.374  1.00 77.16  ? 26  HIS B O   1 
ATOM   2711  C CB  . HIS B 2 26  ? 43.081  3.336   -90.159  1.00 63.67  ? 26  HIS B CB  1 
ATOM   2712  C CG  . HIS B 2 26  ? 44.479  2.904   -90.473  1.00 79.48  ? 26  HIS B CG  1 
ATOM   2713  N ND1 . HIS B 2 26  ? 45.102  3.210   -91.664  1.00 88.63  ? 26  HIS B ND1 1 
ATOM   2714  C CD2 . HIS B 2 26  ? 45.372  2.184   -89.755  1.00 92.37  ? 26  HIS B CD2 1 
ATOM   2715  C CE1 . HIS B 2 26  ? 46.321  2.701   -91.664  1.00 90.15  ? 26  HIS B CE1 1 
ATOM   2716  N NE2 . HIS B 2 26  ? 46.509  2.073   -90.517  1.00 85.60  ? 26  HIS B NE2 1 
ATOM   2717  N N   . SER B 2 27  ? 42.039  2.896   -92.978  1.00 82.92  ? 27  SER B N   1 
ATOM   2718  C CA  . SER B 2 27  ? 42.248  2.682   -94.407  1.00 88.50  ? 27  SER B CA  1 
ATOM   2719  C C   . SER B 2 27  ? 42.378  4.040   -95.074  1.00 85.23  ? 27  SER B C   1 
ATOM   2720  O O   . SER B 2 27  ? 41.448  4.848   -95.004  1.00 69.76  ? 27  SER B O   1 
ATOM   2721  C CB  . SER B 2 27  ? 41.094  1.889   -95.020  1.00 86.47  ? 27  SER B CB  1 
ATOM   2722  O OG  . SER B 2 27  ? 40.960  2.177   -96.401  1.00 91.75  ? 27  SER B OG  1 
ATOM   2723  N N   . ASN B 2 28  ? 43.512  4.291   -95.717  1.00 78.90  ? 28  ASN B N   1 
ATOM   2724  C CA  . ASN B 2 28  ? 43.732  5.556   -96.410  1.00 79.79  ? 28  ASN B CA  1 
ATOM   2725  C C   . ASN B 2 28  ? 44.624  5.289   -97.619  1.00 84.01  ? 28  ASN B C   1 
ATOM   2726  O O   . ASN B 2 28  ? 44.791  4.140   -98.041  1.00 76.96  ? 28  ASN B O   1 
ATOM   2727  C CB  . ASN B 2 28  ? 44.311  6.611   -95.449  1.00 70.18  ? 28  ASN B CB  1 
ATOM   2728  C CG  . ASN B 2 28  ? 45.603  6.167   -94.786  1.00 67.94  ? 28  ASN B CG  1 
ATOM   2729  O OD1 . ASN B 2 28  ? 46.242  5.206   -95.213  1.00 64.67  ? 28  ASN B OD1 1 
ATOM   2730  N ND2 . ASN B 2 28  ? 45.997  6.876   -93.735  1.00 60.58  ? 28  ASN B ND2 1 
ATOM   2731  N N   . GLU B 2 29  ? 45.189  6.358   -98.186  1.00 91.90  ? 29  GLU B N   1 
ATOM   2732  C CA  . GLU B 2 29  ? 46.054  6.213   -99.353  1.00 87.60  ? 29  GLU B CA  1 
ATOM   2733  C C   . GLU B 2 29  ? 47.310  5.417   -99.013  1.00 84.08  ? 29  GLU B C   1 
ATOM   2734  O O   . GLU B 2 29  ? 47.778  4.607   -99.821  1.00 93.51  ? 29  GLU B O   1 
ATOM   2735  C CB  . GLU B 2 29  ? 46.414  7.593   -99.903  1.00 83.50  ? 29  GLU B CB  1 
ATOM   2736  C CG  . GLU B 2 29  ? 46.655  7.642   -101.407 1.00 108.36 ? 29  GLU B CG  1 
ATOM   2737  C CD  . GLU B 2 29  ? 48.055  7.211   -101.796 1.00 125.43 ? 29  GLU B CD  1 
ATOM   2738  O OE1 . GLU B 2 29  ? 48.187  6.268   -102.605 1.00 130.67 ? 29  GLU B OE1 1 
ATOM   2739  O OE2 . GLU B 2 29  ? 49.025  7.816   -101.293 1.00 122.51 ? 29  GLU B OE2 1 
ATOM   2740  N N   . GLN B 2 30  ? 47.867  5.632   -97.817  1.00 84.67  ? 30  GLN B N   1 
ATOM   2741  C CA  . GLN B 2 30  ? 49.069  4.915   -97.405  1.00 71.68  ? 30  GLN B CA  1 
ATOM   2742  C C   . GLN B 2 30  ? 48.818  3.432   -97.166  1.00 78.68  ? 30  GLN B C   1 
ATOM   2743  O O   . GLN B 2 30  ? 49.778  2.655   -97.118  1.00 84.31  ? 30  GLN B O   1 
ATOM   2744  C CB  . GLN B 2 30  ? 49.650  5.555   -96.144  1.00 61.50  ? 30  GLN B CB  1 
ATOM   2745  C CG  . GLN B 2 30  ? 50.573  6.728   -96.418  1.00 59.99  ? 30  GLN B CG  1 
ATOM   2746  C CD  . GLN B 2 30  ? 50.522  7.775   -95.323  1.00 76.41  ? 30  GLN B CD  1 
ATOM   2747  O OE1 . GLN B 2 30  ? 51.556  8.251   -94.857  1.00 84.10  ? 30  GLN B OE1 1 
ATOM   2748  N NE2 . GLN B 2 30  ? 49.313  8.145   -94.912  1.00 85.75  ? 30  GLN B NE2 1 
ATOM   2749  N N   . GLY B 2 31  ? 47.560  3.019   -97.014  1.00 89.25  ? 31  GLY B N   1 
ATOM   2750  C CA  . GLY B 2 31  ? 47.228  1.627   -96.821  1.00 86.74  ? 31  GLY B CA  1 
ATOM   2751  C C   . GLY B 2 31  ? 46.216  1.460   -95.711  1.00 91.61  ? 31  GLY B C   1 
ATOM   2752  O O   . GLY B 2 31  ? 45.520  2.407   -95.328  1.00 91.71  ? 31  GLY B O   1 
ATOM   2753  N N   . SER B 2 32  ? 46.137  0.236   -95.194  1.00 92.24  ? 32  SER B N   1 
ATOM   2754  C CA  . SER B 2 32  ? 45.195  -0.114  -94.143  1.00 91.31  ? 32  SER B CA  1 
ATOM   2755  C C   . SER B 2 32  ? 45.897  -0.984  -93.110  1.00 89.51  ? 32  SER B C   1 
ATOM   2756  O O   . SER B 2 32  ? 47.011  -1.470  -93.326  1.00 104.03 ? 32  SER B O   1 
ATOM   2757  C CB  . SER B 2 32  ? 43.966  -0.835  -94.714  1.00 87.88  ? 32  SER B CB  1 
ATOM   2758  O OG  . SER B 2 32  ? 44.346  -1.912  -95.554  1.00 88.75  ? 32  SER B OG  1 
ATOM   2759  N N   . GLY B 2 33  ? 45.237  -1.174  -91.974  1.00 90.85  ? 33  GLY B N   1 
ATOM   2760  C CA  . GLY B 2 33  ? 45.783  -2.017  -90.929  1.00 97.15  ? 33  GLY B CA  1 
ATOM   2761  C C   . GLY B 2 33  ? 44.995  -1.872  -89.649  1.00 82.47  ? 33  GLY B C   1 
ATOM   2762  O O   . GLY B 2 33  ? 44.140  -0.993  -89.506  1.00 85.29  ? 33  GLY B O   1 
ATOM   2763  N N   . TYR B 2 34  ? 45.305  -2.760  -88.709  1.00 81.92  ? 34  TYR B N   1 
ATOM   2764  C CA  . TYR B 2 34  ? 44.688  -2.767  -87.391  1.00 77.89  ? 34  TYR B CA  1 
ATOM   2765  C C   . TYR B 2 34  ? 45.625  -2.145  -86.364  1.00 69.79  ? 34  TYR B C   1 
ATOM   2766  O O   . TYR B 2 34  ? 46.849  -2.169  -86.514  1.00 72.76  ? 34  TYR B O   1 
ATOM   2767  C CB  . TYR B 2 34  ? 44.328  -4.190  -86.956  1.00 66.47  ? 34  TYR B CB  1 
ATOM   2768  C CG  . TYR B 2 34  ? 43.254  -4.849  -87.789  1.00 73.66  ? 34  TYR B CG  1 
ATOM   2769  C CD1 . TYR B 2 34  ? 41.909  -4.639  -87.516  1.00 67.64  ? 34  TYR B CD1 1 
ATOM   2770  C CD2 . TYR B 2 34  ? 43.585  -5.695  -88.841  1.00 70.42  ? 34  TYR B CD2 1 
ATOM   2771  C CE1 . TYR B 2 34  ? 40.924  -5.246  -88.271  1.00 78.49  ? 34  TYR B CE1 1 
ATOM   2772  C CE2 . TYR B 2 34  ? 42.607  -6.307  -89.602  1.00 69.80  ? 34  TYR B CE2 1 
ATOM   2773  C CZ  . TYR B 2 34  ? 41.278  -6.079  -89.312  1.00 61.78  ? 34  TYR B CZ  1 
ATOM   2774  O OH  . TYR B 2 34  ? 40.301  -6.685  -90.066  1.00 84.53  ? 34  TYR B OH  1 
ATOM   2775  N N   . ALA B 2 35  ? 45.031  -1.586  -85.313  1.00 61.84  ? 35  ALA B N   1 
ATOM   2776  C CA  . ALA B 2 35  ? 45.794  -1.014  -84.209  1.00 60.09  ? 35  ALA B CA  1 
ATOM   2777  C C   . ALA B 2 35  ? 44.967  -1.142  -82.941  1.00 77.90  ? 35  ALA B C   1 
ATOM   2778  O O   . ALA B 2 35  ? 43.872  -0.577  -82.854  1.00 85.04  ? 35  ALA B O   1 
ATOM   2779  C CB  . ALA B 2 35  ? 46.151  0.448   -84.480  1.00 65.30  ? 35  ALA B CB  1 
ATOM   2780  N N   . ALA B 2 36  ? 45.485  -1.884  -81.968  1.00 70.57  ? 36  ALA B N   1 
ATOM   2781  C CA  . ALA B 2 36  ? 44.791  -2.060  -80.702  1.00 75.24  ? 36  ALA B CA  1 
ATOM   2782  C C   . ALA B 2 36  ? 44.948  -0.822  -79.831  1.00 77.07  ? 36  ALA B C   1 
ATOM   2783  O O   . ALA B 2 36  ? 46.017  -0.205  -79.788  1.00 80.94  ? 36  ALA B O   1 
ATOM   2784  C CB  . ALA B 2 36  ? 45.326  -3.288  -79.965  1.00 68.18  ? 36  ALA B CB  1 
ATOM   2785  N N   . ASP B 2 37  ? 43.872  -0.458  -79.138  1.00 86.16  ? 37  ASP B N   1 
ATOM   2786  C CA  . ASP B 2 37  ? 43.915  0.630   -78.165  1.00 78.59  ? 37  ASP B CA  1 
ATOM   2787  C C   . ASP B 2 37  ? 44.510  0.070   -76.881  1.00 79.69  ? 37  ASP B C   1 
ATOM   2788  O O   . ASP B 2 37  ? 43.822  -0.589  -76.097  1.00 91.92  ? 37  ASP B O   1 
ATOM   2789  C CB  . ASP B 2 37  ? 42.526  1.211   -77.934  1.00 58.27  ? 37  ASP B CB  1 
ATOM   2790  C CG  . ASP B 2 37  ? 42.537  2.376   -76.966  1.00 83.12  ? 37  ASP B CG  1 
ATOM   2791  O OD1 . ASP B 2 37  ? 42.858  3.505   -77.395  1.00 84.64  ? 37  ASP B OD1 1 
ATOM   2792  O OD2 . ASP B 2 37  ? 42.232  2.162   -75.775  1.00 97.27  ? 37  ASP B OD2 1 
ATOM   2793  N N   . LYS B 2 38  ? 45.805  0.325   -76.671  1.00 88.57  ? 38  LYS B N   1 
ATOM   2794  C CA  . LYS B 2 38  ? 46.508  -0.279  -75.544  1.00 74.37  ? 38  LYS B CA  1 
ATOM   2795  C C   . LYS B 2 38  ? 45.957  0.196   -74.207  1.00 81.39  ? 38  LYS B C   1 
ATOM   2796  O O   . LYS B 2 38  ? 45.997  -0.552  -73.223  1.00 94.20  ? 38  LYS B O   1 
ATOM   2797  C CB  . LYS B 2 38  ? 48.005  0.023   -75.628  1.00 79.44  ? 38  LYS B CB  1 
ATOM   2798  C CG  . LYS B 2 38  ? 48.706  -0.583  -76.830  1.00 101.29 ? 38  LYS B CG  1 
ATOM   2799  C CD  . LYS B 2 38  ? 48.506  -2.089  -76.900  1.00 115.21 ? 38  LYS B CD  1 
ATOM   2800  C CE  . LYS B 2 38  ? 49.520  -2.724  -77.838  1.00 112.72 ? 38  LYS B CE  1 
ATOM   2801  N NZ  . LYS B 2 38  ? 49.902  -1.792  -78.937  1.00 115.25 ? 38  LYS B NZ  1 
ATOM   2802  N N   . GLU B 2 39  ? 45.449  1.427   -74.143  1.00 78.32  ? 39  GLU B N   1 
ATOM   2803  C CA  . GLU B 2 39  ? 44.943  1.949   -72.878  1.00 97.78  ? 39  GLU B CA  1 
ATOM   2804  C C   . GLU B 2 39  ? 43.728  1.160   -72.402  1.00 96.56  ? 39  GLU B C   1 
ATOM   2805  O O   . GLU B 2 39  ? 43.738  0.580   -71.309  1.00 93.20  ? 39  GLU B O   1 
ATOM   2806  C CB  . GLU B 2 39  ? 44.605  3.434   -73.017  1.00 101.45 ? 39  GLU B CB  1 
ATOM   2807  C CG  . GLU B 2 39  ? 44.165  4.080   -71.711  1.00 113.04 ? 39  GLU B CG  1 
ATOM   2808  C CD  . GLU B 2 39  ? 43.897  5.567   -71.844  1.00 126.76 ? 39  GLU B CD  1 
ATOM   2809  O OE1 . GLU B 2 39  ? 44.049  6.100   -72.962  1.00 129.42 ? 39  GLU B OE1 1 
ATOM   2810  O OE2 . GLU B 2 39  ? 43.535  6.200   -70.828  1.00 124.59 ? 39  GLU B OE2 1 
ATOM   2811  N N   . SER B 2 40  ? 42.674  1.112   -73.222  1.00 89.19  ? 40  SER B N   1 
ATOM   2812  C CA  . SER B 2 40  ? 41.442  0.445   -72.807  1.00 83.66  ? 40  SER B CA  1 
ATOM   2813  C C   . SER B 2 40  ? 41.669  -1.041  -72.561  1.00 83.19  ? 40  SER B C   1 
ATOM   2814  O O   . SER B 2 40  ? 41.096  -1.616  -71.628  1.00 89.27  ? 40  SER B O   1 
ATOM   2815  C CB  . SER B 2 40  ? 40.351  0.650   -73.856  1.00 73.55  ? 40  SER B CB  1 
ATOM   2816  O OG  . SER B 2 40  ? 40.229  2.017   -74.208  1.00 96.56  ? 40  SER B OG  1 
ATOM   2817  N N   . THR B 2 41  ? 42.494  -1.681  -73.394  1.00 68.40  ? 41  THR B N   1 
ATOM   2818  C CA  . THR B 2 41  ? 42.773  -3.103  -73.215  1.00 78.01  ? 41  THR B CA  1 
ATOM   2819  C C   . THR B 2 41  ? 43.434  -3.376  -71.869  1.00 85.04  ? 41  THR B C   1 
ATOM   2820  O O   . THR B 2 41  ? 43.057  -4.319  -71.163  1.00 88.98  ? 41  THR B O   1 
ATOM   2821  C CB  . THR B 2 41  ? 43.653  -3.609  -74.360  1.00 71.50  ? 41  THR B CB  1 
ATOM   2822  O OG1 . THR B 2 41  ? 42.842  -3.856  -75.516  1.00 69.87  ? 41  THR B OG1 1 
ATOM   2823  C CG2 . THR B 2 41  ? 44.382  -4.889  -73.968  1.00 76.75  ? 41  THR B CG2 1 
ATOM   2824  N N   . GLN B 2 42  ? 44.414  -2.553  -71.489  1.00 85.04  ? 42  GLN B N   1 
ATOM   2825  C CA  . GLN B 2 42  ? 45.135  -2.800  -70.245  1.00 86.14  ? 42  GLN B CA  1 
ATOM   2826  C C   . GLN B 2 42  ? 44.240  -2.587  -69.030  1.00 84.01  ? 42  GLN B C   1 
ATOM   2827  O O   . GLN B 2 42  ? 44.308  -3.354  -68.062  1.00 100.42 ? 42  GLN B O   1 
ATOM   2828  C CB  . GLN B 2 42  ? 46.372  -1.908  -70.168  1.00 92.03  ? 42  GLN B CB  1 
ATOM   2829  C CG  . GLN B 2 42  ? 47.427  -2.431  -69.214  1.00 94.55  ? 42  GLN B CG  1 
ATOM   2830  C CD  . GLN B 2 42  ? 47.840  -3.853  -69.541  1.00 103.68 ? 42  GLN B CD  1 
ATOM   2831  O OE1 . GLN B 2 42  ? 47.890  -4.715  -68.664  1.00 104.39 ? 42  GLN B OE1 1 
ATOM   2832  N NE2 . GLN B 2 42  ? 48.139  -4.107  -70.811  1.00 111.53 ? 42  GLN B NE2 1 
ATOM   2833  N N   . LYS B 2 43  ? 43.403  -1.548  -69.060  1.00 77.67  ? 43  LYS B N   1 
ATOM   2834  C CA  . LYS B 2 43  ? 42.482  -1.305  -67.953  1.00 76.92  ? 43  LYS B CA  1 
ATOM   2835  C C   . LYS B 2 43  ? 41.459  -2.425  -67.830  1.00 76.52  ? 43  LYS B C   1 
ATOM   2836  O O   . LYS B 2 43  ? 41.118  -2.845  -66.718  1.00 82.40  ? 43  LYS B O   1 
ATOM   2837  C CB  . LYS B 2 43  ? 41.790  0.043   -68.142  1.00 68.31  ? 43  LYS B CB  1 
ATOM   2838  C CG  . LYS B 2 43  ? 42.768  1.165   -68.404  1.00 88.88  ? 43  LYS B CG  1 
ATOM   2839  C CD  . LYS B 2 43  ? 42.099  2.518   -68.398  1.00 100.30 ? 43  LYS B CD  1 
ATOM   2840  C CE  . LYS B 2 43  ? 43.143  3.609   -68.265  1.00 95.73  ? 43  LYS B CE  1 
ATOM   2841  N NZ  . LYS B 2 43  ? 42.751  4.636   -67.267  1.00 98.35  ? 43  LYS B NZ  1 
ATOM   2842  N N   . ALA B 2 44  ? 40.953  -2.915  -68.963  1.00 62.40  ? 44  ALA B N   1 
ATOM   2843  C CA  . ALA B 2 44  ? 40.022  -4.036  -68.935  1.00 72.74  ? 44  ALA B CA  1 
ATOM   2844  C C   . ALA B 2 44  ? 40.705  -5.312  -68.458  1.00 79.07  ? 44  ALA B C   1 
ATOM   2845  O O   . ALA B 2 44  ? 40.147  -6.051  -67.639  1.00 88.14  ? 44  ALA B O   1 
ATOM   2846  C CB  . ALA B 2 44  ? 39.403  -4.234  -70.317  1.00 65.14  ? 44  ALA B CB  1 
ATOM   2847  N N   . ILE B 2 45  ? 41.918  -5.583  -68.951  1.00 72.13  ? 45  ILE B N   1 
ATOM   2848  C CA  . ILE B 2 45  ? 42.640  -6.779  -68.523  1.00 75.13  ? 45  ILE B CA  1 
ATOM   2849  C C   . ILE B 2 45  ? 42.946  -6.713  -67.032  1.00 80.23  ? 45  ILE B C   1 
ATOM   2850  O O   . ILE B 2 45  ? 42.760  -7.694  -66.302  1.00 77.03  ? 45  ILE B O   1 
ATOM   2851  C CB  . ILE B 2 45  ? 43.919  -6.969  -69.361  1.00 68.24  ? 45  ILE B CB  1 
ATOM   2852  C CG1 . ILE B 2 45  ? 43.597  -7.693  -70.671  1.00 86.33  ? 45  ILE B CG1 1 
ATOM   2853  C CG2 . ILE B 2 45  ? 44.981  -7.726  -68.569  1.00 71.58  ? 45  ILE B CG2 1 
ATOM   2854  C CD1 . ILE B 2 45  ? 44.819  -8.142  -71.446  1.00 81.69  ? 45  ILE B CD1 1 
ATOM   2855  N N   . ASP B 2 46  ? 43.412  -5.556  -66.553  1.00 72.28  ? 46  ASP B N   1 
ATOM   2856  C CA  . ASP B 2 46  ? 43.673  -5.411  -65.126  1.00 75.03  ? 46  ASP B CA  1 
ATOM   2857  C C   . ASP B 2 46  ? 42.389  -5.529  -64.315  1.00 85.63  ? 46  ASP B C   1 
ATOM   2858  O O   . ASP B 2 46  ? 42.376  -6.152  -63.246  1.00 93.90  ? 46  ASP B O   1 
ATOM   2859  C CB  . ASP B 2 46  ? 44.359  -4.074  -64.841  1.00 81.45  ? 46  ASP B CB  1 
ATOM   2860  C CG  . ASP B 2 46  ? 45.816  -4.065  -65.254  1.00 104.20 ? 46  ASP B CG  1 
ATOM   2861  O OD1 . ASP B 2 46  ? 46.217  -4.950  -66.039  1.00 95.11  ? 46  ASP B OD1 1 
ATOM   2862  O OD2 . ASP B 2 46  ? 46.563  -3.178  -64.788  1.00 108.78 ? 46  ASP B OD2 1 
ATOM   2863  N N   . GLY B 2 47  ? 41.303  -4.924  -64.798  1.00 81.14  ? 47  GLY B N   1 
ATOM   2864  C CA  . GLY B 2 47  ? 40.045  -5.006  -64.074  1.00 73.18  ? 47  GLY B CA  1 
ATOM   2865  C C   . GLY B 2 47  ? 39.504  -6.421  -64.001  1.00 80.70  ? 47  GLY B C   1 
ATOM   2866  O O   . GLY B 2 47  ? 39.135  -6.903  -62.928  1.00 79.94  ? 47  GLY B O   1 
ATOM   2867  N N   . VAL B 2 48  ? 39.474  -7.117  -65.141  1.00 74.72  ? 48  VAL B N   1 
ATOM   2868  C CA  . VAL B 2 48  ? 38.947  -8.479  -65.161  1.00 68.16  ? 48  VAL B CA  1 
ATOM   2869  C C   . VAL B 2 48  ? 39.811  -9.396  -64.304  1.00 81.34  ? 48  VAL B C   1 
ATOM   2870  O O   . VAL B 2 48  ? 39.295  -10.216 -63.535  1.00 83.35  ? 48  VAL B O   1 
ATOM   2871  C CB  . VAL B 2 48  ? 38.829  -8.993  -66.607  1.00 64.04  ? 48  VAL B CB  1 
ATOM   2872  C CG1 . VAL B 2 48  ? 38.400  -10.449 -66.612  1.00 61.48  ? 48  VAL B CG1 1 
ATOM   2873  C CG2 . VAL B 2 48  ? 37.832  -8.151  -67.390  1.00 78.90  ? 48  VAL B CG2 1 
ATOM   2874  N N   . THR B 2 49  ? 41.137  -9.262  -64.413  1.00 77.32  ? 49  THR B N   1 
ATOM   2875  C CA  . THR B 2 49  ? 42.038  -10.062 -63.587  1.00 77.24  ? 49  THR B CA  1 
ATOM   2876  C C   . THR B 2 49  ? 41.753  -9.861  -62.103  1.00 72.43  ? 49  THR B C   1 
ATOM   2877  O O   . THR B 2 49  ? 41.790  -10.819 -61.322  1.00 66.00  ? 49  THR B O   1 
ATOM   2878  C CB  . THR B 2 49  ? 43.493  -9.712  -63.908  1.00 77.40  ? 49  THR B CB  1 
ATOM   2879  O OG1 . THR B 2 49  ? 43.801  -10.119 -65.247  1.00 79.71  ? 49  THR B OG1 1 
ATOM   2880  C CG2 . THR B 2 49  ? 44.444  -10.405 -62.940  1.00 69.93  ? 49  THR B CG2 1 
ATOM   2881  N N   . ASN B 2 50  ? 41.453  -8.624  -61.698  1.00 71.13  ? 50  ASN B N   1 
ATOM   2882  C CA  . ASN B 2 50  ? 41.116  -8.363  -60.302  1.00 68.71  ? 50  ASN B CA  1 
ATOM   2883  C C   . ASN B 2 50  ? 39.837  -9.085  -59.895  1.00 77.66  ? 50  ASN B C   1 
ATOM   2884  O O   . ASN B 2 50  ? 39.746  -9.620  -58.784  1.00 82.69  ? 50  ASN B O   1 
ATOM   2885  C CB  . ASN B 2 50  ? 40.978  -6.859  -60.064  1.00 82.40  ? 50  ASN B CB  1 
ATOM   2886  C CG  . ASN B 2 50  ? 42.280  -6.215  -59.631  1.00 95.70  ? 50  ASN B CG  1 
ATOM   2887  O OD1 . ASN B 2 50  ? 43.358  -6.780  -59.816  1.00 102.47 ? 50  ASN B OD1 1 
ATOM   2888  N ND2 . ASN B 2 50  ? 42.185  -5.026  -59.050  1.00 95.31  ? 50  ASN B ND2 1 
ATOM   2889  N N   . LYS B 2 51  ? 38.834  -9.101  -60.778  1.00 73.70  ? 51  LYS B N   1 
ATOM   2890  C CA  . LYS B 2 51  ? 37.570  -9.755  -60.452  1.00 73.39  ? 51  LYS B CA  1 
ATOM   2891  C C   . LYS B 2 51  ? 37.760  -11.248 -60.216  1.00 73.99  ? 51  LYS B C   1 
ATOM   2892  O O   . LYS B 2 51  ? 37.228  -11.807 -59.249  1.00 76.44  ? 51  LYS B O   1 
ATOM   2893  C CB  . LYS B 2 51  ? 36.549  -9.525  -61.566  1.00 77.30  ? 51  LYS B CB  1 
ATOM   2894  C CG  . LYS B 2 51  ? 35.306  -10.394 -61.415  1.00 69.60  ? 51  LYS B CG  1 
ATOM   2895  C CD  . LYS B 2 51  ? 34.427  -10.354 -62.652  1.00 67.22  ? 51  LYS B CD  1 
ATOM   2896  C CE  . LYS B 2 51  ? 33.797  -8.987  -62.835  1.00 69.41  ? 51  LYS B CE  1 
ATOM   2897  N NZ  . LYS B 2 51  ? 32.492  -9.080  -63.545  1.00 67.00  ? 51  LYS B NZ  1 
ATOM   2898  N N   . VAL B 2 52  ? 38.508  -11.915 -61.100  1.00 63.97  ? 52  VAL B N   1 
ATOM   2899  C CA  . VAL B 2 52  ? 38.725  -13.351 -60.951  1.00 71.11  ? 52  VAL B CA  1 
ATOM   2900  C C   . VAL B 2 52  ? 39.498  -13.640 -59.671  1.00 79.00  ? 52  VAL B C   1 
ATOM   2901  O O   . VAL B 2 52  ? 39.173  -14.575 -58.929  1.00 78.77  ? 52  VAL B O   1 
ATOM   2902  C CB  . VAL B 2 52  ? 39.441  -13.923 -62.189  1.00 60.69  ? 52  VAL B CB  1 
ATOM   2903  C CG1 . VAL B 2 52  ? 39.265  -15.431 -62.237  1.00 75.01  ? 52  VAL B CG1 1 
ATOM   2904  C CG2 . VAL B 2 52  ? 38.907  -13.279 -63.460  1.00 70.66  ? 52  VAL B CG2 1 
ATOM   2905  N N   . ASN B 2 53  ? 40.531  -12.841 -59.391  1.00 73.73  ? 53  ASN B N   1 
ATOM   2906  C CA  . ASN B 2 53  ? 41.292  -13.019 -58.158  1.00 69.96  ? 53  ASN B CA  1 
ATOM   2907  C C   . ASN B 2 53  ? 40.427  -12.762 -56.931  1.00 71.58  ? 53  ASN B C   1 
ATOM   2908  O O   . ASN B 2 53  ? 40.487  -13.517 -55.955  1.00 77.22  ? 53  ASN B O   1 
ATOM   2909  C CB  . ASN B 2 53  ? 42.514  -12.100 -58.154  1.00 53.85  ? 53  ASN B CB  1 
ATOM   2910  C CG  . ASN B 2 53  ? 43.523  -12.467 -59.224  1.00 70.63  ? 53  ASN B CG  1 
ATOM   2911  O OD1 . ASN B 2 53  ? 43.520  -13.584 -59.741  1.00 68.27  ? 53  ASN B OD1 1 
ATOM   2912  N ND2 . ASN B 2 53  ? 44.398  -11.526 -59.557  1.00 73.90  ? 53  ASN B ND2 1 
ATOM   2913  N N   . SER B 2 54  ? 39.608  -11.706 -56.964  1.00 68.23  ? 54  SER B N   1 
ATOM   2914  C CA  . SER B 2 54  ? 38.781  -11.372 -55.808  1.00 66.28  ? 54  SER B CA  1 
ATOM   2915  C C   . SER B 2 54  ? 37.775  -12.476 -55.507  1.00 66.69  ? 54  SER B C   1 
ATOM   2916  O O   . SER B 2 54  ? 37.551  -12.822 -54.342  1.00 64.47  ? 54  SER B O   1 
ATOM   2917  C CB  . SER B 2 54  ? 38.067  -10.040 -56.039  1.00 64.41  ? 54  SER B CB  1 
ATOM   2918  O OG  . SER B 2 54  ? 38.993  -8.970  -56.117  1.00 82.91  ? 54  SER B OG  1 
ATOM   2919  N N   . ILE B 2 55  ? 37.159  -13.044 -56.545  1.00 64.76  ? 55  ILE B N   1 
ATOM   2920  C CA  . ILE B 2 55  ? 36.232  -14.152 -56.339  1.00 70.48  ? 55  ILE B CA  1 
ATOM   2921  C C   . ILE B 2 55  ? 36.951  -15.348 -55.727  1.00 59.20  ? 55  ILE B C   1 
ATOM   2922  O O   . ILE B 2 55  ? 36.357  -16.119 -54.963  1.00 79.31  ? 55  ILE B O   1 
ATOM   2923  C CB  . ILE B 2 55  ? 35.538  -14.497 -57.676  1.00 75.02  ? 55  ILE B CB  1 
ATOM   2924  C CG1 . ILE B 2 55  ? 34.328  -13.579 -57.885  1.00 66.76  ? 55  ILE B CG1 1 
ATOM   2925  C CG2 . ILE B 2 55  ? 35.145  -15.972 -57.749  1.00 53.33  ? 55  ILE B CG2 1 
ATOM   2926  C CD1 . ILE B 2 55  ? 33.952  -13.363 -59.334  1.00 76.96  ? 55  ILE B CD1 1 
ATOM   2927  N N   . ILE B 2 56  ? 38.240  -15.499 -56.014  1.00 73.63  ? 56  ILE B N   1 
ATOM   2928  C CA  . ILE B 2 56  ? 39.020  -16.617 -55.492  1.00 69.32  ? 56  ILE B CA  1 
ATOM   2929  C C   . ILE B 2 56  ? 39.708  -16.259 -54.179  1.00 75.29  ? 56  ILE B C   1 
ATOM   2930  O O   . ILE B 2 56  ? 39.659  -17.026 -53.214  1.00 76.45  ? 56  ILE B O   1 
ATOM   2931  C CB  . ILE B 2 56  ? 40.038  -17.079 -56.557  1.00 61.97  ? 56  ILE B CB  1 
ATOM   2932  C CG1 . ILE B 2 56  ? 39.304  -17.598 -57.797  1.00 68.14  ? 56  ILE B CG1 1 
ATOM   2933  C CG2 . ILE B 2 56  ? 40.968  -18.139 -55.986  1.00 70.71  ? 56  ILE B CG2 1 
ATOM   2934  C CD1 . ILE B 2 56  ? 40.176  -17.704 -59.029  1.00 60.76  ? 56  ILE B CD1 1 
ATOM   2935  N N   . ASP B 2 57  ? 40.360  -15.093 -54.116  1.00 80.72  ? 57  ASP B N   1 
ATOM   2936  C CA  . ASP B 2 57  ? 41.164  -14.756 -52.941  1.00 75.32  ? 57  ASP B CA  1 
ATOM   2937  C C   . ASP B 2 57  ? 40.304  -14.551 -51.699  1.00 69.50  ? 57  ASP B C   1 
ATOM   2938  O O   . ASP B 2 57  ? 40.701  -14.945 -50.596  1.00 77.33  ? 57  ASP B O   1 
ATOM   2939  C CB  . ASP B 2 57  ? 42.006  -13.506 -53.205  1.00 65.42  ? 57  ASP B CB  1 
ATOM   2940  C CG  . ASP B 2 57  ? 43.193  -13.781 -54.103  1.00 86.89  ? 57  ASP B CG  1 
ATOM   2941  O OD1 . ASP B 2 57  ? 44.057  -12.887 -54.240  1.00 100.76 ? 57  ASP B OD1 1 
ATOM   2942  O OD2 . ASP B 2 57  ? 43.257  -14.887 -54.681  1.00 100.00 ? 57  ASP B OD2 1 
ATOM   2943  N N   . LYS B 2 58  ? 39.131  -13.933 -51.848  1.00 74.08  ? 58  LYS B N   1 
ATOM   2944  C CA  . LYS B 2 58  ? 38.345  -13.544 -50.682  1.00 65.81  ? 58  LYS B CA  1 
ATOM   2945  C C   . LYS B 2 58  ? 37.788  -14.729 -49.903  1.00 76.43  ? 58  LYS B C   1 
ATOM   2946  O O   . LYS B 2 58  ? 37.271  -14.528 -48.799  1.00 65.69  ? 58  LYS B O   1 
ATOM   2947  C CB  . LYS B 2 58  ? 37.198  -12.617 -51.094  1.00 67.27  ? 58  LYS B CB  1 
ATOM   2948  C CG  . LYS B 2 58  ? 37.645  -11.285 -51.677  1.00 76.30  ? 58  LYS B CG  1 
ATOM   2949  C CD  . LYS B 2 58  ? 38.793  -10.684 -50.887  1.00 82.79  ? 58  LYS B CD  1 
ATOM   2950  C CE  . LYS B 2 58  ? 38.415  -9.337  -50.294  1.00 85.69  ? 58  LYS B CE  1 
ATOM   2951  N NZ  . LYS B 2 58  ? 39.585  -8.669  -49.654  1.00 90.66  ? 58  LYS B NZ  1 
ATOM   2952  N N   . MET B 2 59  ? 37.867  -15.945 -50.438  1.00 77.02  ? 59  MET B N   1 
ATOM   2953  C CA  . MET B 2 59  ? 37.375  -17.108 -49.714  1.00 65.59  ? 59  MET B CA  1 
ATOM   2954  C C   . MET B 2 59  ? 38.328  -17.467 -48.584  1.00 70.99  ? 59  MET B C   1 
ATOM   2955  O O   . MET B 2 59  ? 39.531  -17.647 -48.805  1.00 83.09  ? 59  MET B O   1 
ATOM   2956  C CB  . MET B 2 59  ? 37.205  -18.294 -50.661  1.00 68.71  ? 59  MET B CB  1 
ATOM   2957  C CG  . MET B 2 59  ? 36.694  -19.570 -50.008  1.00 73.69  ? 59  MET B CG  1 
ATOM   2958  S SD  . MET B 2 59  ? 34.908  -19.588 -49.761  1.00 80.25  ? 59  MET B SD  1 
ATOM   2959  C CE  . MET B 2 59  ? 34.764  -18.759 -48.181  1.00 68.90  ? 59  MET B CE  1 
ATOM   2960  N N   . ASN B 2 60  ? 37.785  -17.575 -47.374  1.00 88.38  ? 60  ASN B N   1 
ATOM   2961  C CA  . ASN B 2 60  ? 38.541  -17.986 -46.200  1.00 70.43  ? 60  ASN B CA  1 
ATOM   2962  C C   . ASN B 2 60  ? 38.345  -19.477 -45.970  1.00 66.34  ? 60  ASN B C   1 
ATOM   2963  O O   . ASN B 2 60  ? 37.208  -19.954 -45.893  1.00 74.85  ? 60  ASN B O   1 
ATOM   2964  C CB  . ASN B 2 60  ? 38.104  -17.192 -44.970  1.00 65.30  ? 60  ASN B CB  1 
ATOM   2965  C CG  . ASN B 2 60  ? 38.768  -17.676 -43.695  1.00 85.53  ? 60  ASN B CG  1 
ATOM   2966  O OD1 . ASN B 2 60  ? 39.976  -17.527 -43.519  1.00 96.77  ? 60  ASN B OD1 1 
ATOM   2967  N ND2 . ASN B 2 60  ? 37.977  -18.254 -42.794  1.00 85.07  ? 60  ASN B ND2 1 
ATOM   2968  N N   . THR B 2 61  ? 39.452  -20.209 -45.865  1.00 73.56  ? 61  THR B N   1 
ATOM   2969  C CA  . THR B 2 61  ? 39.423  -21.646 -45.628  1.00 76.28  ? 61  THR B CA  1 
ATOM   2970  C C   . THR B 2 61  ? 40.277  -21.960 -44.410  1.00 71.76  ? 61  THR B C   1 
ATOM   2971  O O   . THR B 2 61  ? 41.416  -21.493 -44.310  1.00 88.41  ? 61  THR B O   1 
ATOM   2972  C CB  . THR B 2 61  ? 39.942  -22.433 -46.839  1.00 83.72  ? 61  THR B CB  1 
ATOM   2973  O OG1 . THR B 2 61  ? 41.366  -22.555 -46.756  1.00 86.76  ? 61  THR B OG1 1 
ATOM   2974  C CG2 . THR B 2 61  ? 39.580  -21.726 -48.140  1.00 84.29  ? 61  THR B CG2 1 
ATOM   2975  N N   . GLN B 2 62  ? 39.727  -22.747 -43.491  1.00 76.36  ? 62  GLN B N   1 
ATOM   2976  C CA  . GLN B 2 62  ? 40.439  -23.205 -42.308  1.00 67.40  ? 62  GLN B CA  1 
ATOM   2977  C C   . GLN B 2 62  ? 40.430  -24.728 -42.265  1.00 72.39  ? 62  GLN B C   1 
ATOM   2978  O O   . GLN B 2 62  ? 39.706  -25.391 -43.012  1.00 86.35  ? 62  GLN B O   1 
ATOM   2979  C CB  . GLN B 2 62  ? 39.820  -22.632 -41.024  1.00 74.17  ? 62  GLN B CB  1 
ATOM   2980  C CG  . GLN B 2 62  ? 38.383  -23.062 -40.769  1.00 73.87  ? 62  GLN B CG  1 
ATOM   2981  C CD  . GLN B 2 62  ? 37.373  -22.131 -41.409  1.00 79.40  ? 62  GLN B CD  1 
ATOM   2982  O OE1 . GLN B 2 62  ? 37.222  -20.979 -40.998  1.00 79.87  ? 62  GLN B OE1 1 
ATOM   2983  N NE2 . GLN B 2 62  ? 36.676  -22.624 -42.426  1.00 79.10  ? 62  GLN B NE2 1 
ATOM   2984  N N   . PHE B 2 63  ? 41.255  -25.281 -41.380  1.00 70.51  ? 63  PHE B N   1 
ATOM   2985  C CA  . PHE B 2 63  ? 41.337  -26.729 -41.244  1.00 69.89  ? 63  PHE B CA  1 
ATOM   2986  C C   . PHE B 2 63  ? 40.050  -27.278 -40.645  1.00 76.69  ? 63  PHE B C   1 
ATOM   2987  O O   . PHE B 2 63  ? 39.548  -26.763 -39.640  1.00 72.20  ? 63  PHE B O   1 
ATOM   2988  C CB  . PHE B 2 63  ? 42.529  -27.121 -40.372  1.00 55.59  ? 63  PHE B CB  1 
ATOM   2989  C CG  . PHE B 2 63  ? 42.668  -28.605 -40.168  1.00 65.92  ? 63  PHE B CG  1 
ATOM   2990  C CD1 . PHE B 2 63  ? 43.387  -29.376 -41.065  1.00 80.10  ? 63  PHE B CD1 1 
ATOM   2991  C CD2 . PHE B 2 63  ? 42.077  -29.231 -39.080  1.00 62.92  ? 63  PHE B CD2 1 
ATOM   2992  C CE1 . PHE B 2 63  ? 43.514  -30.742 -40.881  1.00 74.23  ? 63  PHE B CE1 1 
ATOM   2993  C CE2 . PHE B 2 63  ? 42.200  -30.595 -38.893  1.00 61.37  ? 63  PHE B CE2 1 
ATOM   2994  C CZ  . PHE B 2 63  ? 42.920  -31.351 -39.794  1.00 67.21  ? 63  PHE B CZ  1 
ATOM   2995  N N   . GLU B 2 64  ? 39.517  -28.328 -41.265  1.00 70.67  ? 64  GLU B N   1 
ATOM   2996  C CA  . GLU B 2 64  ? 38.363  -29.044 -40.744  1.00 63.62  ? 64  GLU B CA  1 
ATOM   2997  C C   . GLU B 2 64  ? 38.549  -30.530 -41.006  1.00 68.84  ? 64  GLU B C   1 
ATOM   2998  O O   . GLU B 2 64  ? 39.167  -30.930 -41.996  1.00 72.04  ? 64  GLU B O   1 
ATOM   2999  C CB  . GLU B 2 64  ? 37.044  -28.566 -41.377  1.00 56.29  ? 64  GLU B CB  1 
ATOM   3000  C CG  . GLU B 2 64  ? 36.726  -27.088 -41.180  1.00 61.83  ? 64  GLU B CG  1 
ATOM   3001  C CD  . GLU B 2 64  ? 36.431  -26.721 -39.735  1.00 79.91  ? 64  GLU B CD  1 
ATOM   3002  O OE1 . GLU B 2 64  ? 36.225  -27.631 -38.904  1.00 88.24  ? 64  GLU B OE1 1 
ATOM   3003  O OE2 . GLU B 2 64  ? 36.403  -25.510 -39.431  1.00 76.68  ? 64  GLU B OE2 1 
ATOM   3004  N N   . ALA B 2 65  ? 38.010  -31.346 -40.104  1.00 76.21  ? 65  ALA B N   1 
ATOM   3005  C CA  . ALA B 2 65  ? 38.011  -32.798 -40.248  1.00 65.88  ? 65  ALA B CA  1 
ATOM   3006  C C   . ALA B 2 65  ? 36.568  -33.278 -40.186  1.00 62.00  ? 65  ALA B C   1 
ATOM   3007  O O   . ALA B 2 65  ? 35.915  -33.165 -39.143  1.00 64.60  ? 65  ALA B O   1 
ATOM   3008  C CB  . ALA B 2 65  ? 38.862  -33.459 -39.164  1.00 63.53  ? 65  ALA B CB  1 
ATOM   3009  N N   . VAL B 2 66  ? 36.072  -33.816 -41.297  1.00 62.48  ? 66  VAL B N   1 
ATOM   3010  C CA  . VAL B 2 66  ? 34.695  -34.282 -41.405  1.00 59.86  ? 66  VAL B CA  1 
ATOM   3011  C C   . VAL B 2 66  ? 34.707  -35.804 -41.421  1.00 62.80  ? 66  VAL B C   1 
ATOM   3012  O O   . VAL B 2 66  ? 35.292  -36.420 -42.320  1.00 65.26  ? 66  VAL B O   1 
ATOM   3013  C CB  . VAL B 2 66  ? 34.003  -33.721 -42.656  1.00 49.84  ? 66  VAL B CB  1 
ATOM   3014  C CG1 . VAL B 2 66  ? 32.624  -34.334 -42.817  1.00 60.49  ? 66  VAL B CG1 1 
ATOM   3015  C CG2 . VAL B 2 66  ? 33.907  -32.206 -42.571  1.00 49.62  ? 66  VAL B CG2 1 
ATOM   3016  N N   . GLY B 2 67  ? 34.058  -36.409 -40.427  1.00 71.65  ? 67  GLY B N   1 
ATOM   3017  C CA  . GLY B 2 67  ? 33.933  -37.851 -40.350  1.00 63.10  ? 67  GLY B CA  1 
ATOM   3018  C C   . GLY B 2 67  ? 32.565  -38.282 -39.863  1.00 76.17  ? 67  GLY B C   1 
ATOM   3019  O O   . GLY B 2 67  ? 31.664  -37.450 -39.719  1.00 82.68  ? 67  GLY B O   1 
ATOM   3020  N N   . ARG B 2 68  ? 32.393  -39.578 -39.608  1.00 73.83  ? 68  ARG B N   1 
ATOM   3021  C CA  . ARG B 2 68  ? 31.141  -40.144 -39.100  1.00 63.28  ? 68  ARG B CA  1 
ATOM   3022  C C   . ARG B 2 68  ? 31.471  -40.832 -37.776  1.00 75.49  ? 68  ARG B C   1 
ATOM   3023  O O   . ARG B 2 68  ? 31.815  -42.016 -37.742  1.00 82.06  ? 68  ARG B O   1 
ATOM   3024  C CB  . ARG B 2 68  ? 30.511  -41.114 -40.106  1.00 73.54  ? 68  ARG B CB  1 
ATOM   3025  C CG  . ARG B 2 68  ? 30.128  -40.478 -41.439  1.00 68.78  ? 68  ARG B CG  1 
ATOM   3026  C CD  . ARG B 2 68  ? 29.442  -39.137 -41.231  1.00 68.51  ? 68  ARG B CD  1 
ATOM   3027  N NE  . ARG B 2 68  ? 28.428  -38.863 -42.242  1.00 86.42  ? 68  ARG B NE  1 
ATOM   3028  C CZ  . ARG B 2 68  ? 28.128  -37.651 -42.688  1.00 93.06  ? 68  ARG B CZ  1 
ATOM   3029  N NH1 . ARG B 2 68  ? 28.773  -36.577 -42.260  1.00 73.47  ? 68  ARG B NH1 1 
ATOM   3030  N NH2 . ARG B 2 68  ? 27.166  -37.513 -43.596  1.00 106.19 ? 68  ARG B NH2 1 
ATOM   3031  N N   . GLU B 2 69  ? 31.352  -40.085 -36.682  1.00 61.11  ? 69  GLU B N   1 
ATOM   3032  C CA  . GLU B 2 69  ? 31.865  -40.480 -35.378  1.00 73.32  ? 69  GLU B CA  1 
ATOM   3033  C C   . GLU B 2 69  ? 30.755  -40.647 -34.345  1.00 65.20  ? 69  GLU B C   1 
ATOM   3034  O O   . GLU B 2 69  ? 30.947  -40.358 -33.163  1.00 67.09  ? 69  GLU B O   1 
ATOM   3035  C CB  . GLU B 2 69  ? 32.889  -39.464 -34.885  1.00 79.45  ? 69  GLU B CB  1 
ATOM   3036  C CG  . GLU B 2 69  ? 33.641  -38.745 -35.995  1.00 91.70  ? 69  GLU B CG  1 
ATOM   3037  C CD  . GLU B 2 69  ? 34.509  -37.615 -35.476  1.00 107.65 ? 69  GLU B CD  1 
ATOM   3038  O OE1 . GLU B 2 69  ? 34.244  -36.444 -35.825  1.00 106.80 ? 69  GLU B OE1 1 
ATOM   3039  O OE2 . GLU B 2 69  ? 35.448  -37.899 -34.703  1.00 93.20  ? 69  GLU B OE2 1 
ATOM   3040  N N   . PHE B 2 70  ? 29.583  -41.117 -34.766  1.00 63.95  ? 70  PHE B N   1 
ATOM   3041  C CA  . PHE B 2 70  ? 28.457  -41.276 -33.854  1.00 57.17  ? 70  PHE B CA  1 
ATOM   3042  C C   . PHE B 2 70  ? 27.862  -42.669 -33.994  1.00 53.21  ? 70  PHE B C   1 
ATOM   3043  O O   . PHE B 2 70  ? 27.583  -43.123 -35.108  1.00 60.21  ? 70  PHE B O   1 
ATOM   3044  C CB  . PHE B 2 70  ? 27.397  -40.201 -34.103  1.00 49.38  ? 70  PHE B CB  1 
ATOM   3045  C CG  . PHE B 2 70  ? 27.855  -38.818 -33.743  1.00 61.90  ? 70  PHE B CG  1 
ATOM   3046  C CD1 . PHE B 2 70  ? 28.151  -38.496 -32.428  1.00 62.84  ? 70  PHE B CD1 1 
ATOM   3047  C CD2 . PHE B 2 70  ? 28.006  -37.847 -34.718  1.00 61.90  ? 70  PHE B CD2 1 
ATOM   3048  C CE1 . PHE B 2 70  ? 28.583  -37.225 -32.090  1.00 65.75  ? 70  PHE B CE1 1 
ATOM   3049  C CE2 . PHE B 2 70  ? 28.434  -36.575 -34.385  1.00 63.60  ? 70  PHE B CE2 1 
ATOM   3050  C CZ  . PHE B 2 70  ? 28.725  -36.264 -33.072  1.00 53.09  ? 70  PHE B CZ  1 
ATOM   3051  N N   . ASN B 2 71  ? 27.675  -43.339 -32.860  1.00 65.22  ? 71  ASN B N   1 
ATOM   3052  C CA  . ASN B 2 71  ? 27.213  -44.720 -32.831  1.00 58.94  ? 71  ASN B CA  1 
ATOM   3053  C C   . ASN B 2 71  ? 25.697  -44.778 -33.036  1.00 65.72  ? 71  ASN B C   1 
ATOM   3054  O O   . ASN B 2 71  ? 25.035  -43.768 -33.292  1.00 61.37  ? 71  ASN B O   1 
ATOM   3055  C CB  . ASN B 2 71  ? 27.650  -45.393 -31.531  1.00 61.23  ? 71  ASN B CB  1 
ATOM   3056  C CG  . ASN B 2 71  ? 27.200  -44.630 -30.292  1.00 65.98  ? 71  ASN B CG  1 
ATOM   3057  O OD1 . ASN B 2 71  ? 26.006  -44.533 -30.008  1.00 60.22  ? 71  ASN B OD1 1 
ATOM   3058  N ND2 . ASN B 2 71  ? 28.160  -44.099 -29.539  1.00 89.24  ? 71  ASN B ND2 1 
ATOM   3059  N N   . ASN B 2 72  ? 25.133  -45.983 -32.913  1.00 55.56  ? 72  ASN B N   1 
ATOM   3060  C CA  . ASN B 2 72  ? 23.732  -46.226 -33.237  1.00 68.52  ? 72  ASN B CA  1 
ATOM   3061  C C   . ASN B 2 72  ? 22.761  -45.626 -32.229  1.00 75.57  ? 72  ASN B C   1 
ATOM   3062  O O   . ASN B 2 72  ? 21.565  -45.550 -32.528  1.00 84.40  ? 72  ASN B O   1 
ATOM   3063  C CB  . ASN B 2 72  ? 23.478  -47.729 -33.357  1.00 60.42  ? 72  ASN B CB  1 
ATOM   3064  C CG  . ASN B 2 72  ? 22.931  -48.122 -34.718  1.00 113.24 ? 72  ASN B CG  1 
ATOM   3065  O OD1 . ASN B 2 72  ? 22.926  -47.323 -35.655  1.00 107.94 ? 72  ASN B OD1 1 
ATOM   3066  N ND2 . ASN B 2 72  ? 22.473  -49.363 -34.834  1.00 112.21 ? 72  ASN B ND2 1 
ATOM   3067  N N   . LEU B 2 73  ? 23.229  -45.209 -31.051  1.00 69.85  ? 73  LEU B N   1 
ATOM   3068  C CA  . LEU B 2 73  ? 22.376  -44.550 -30.071  1.00 73.73  ? 73  LEU B CA  1 
ATOM   3069  C C   . LEU B 2 73  ? 22.655  -43.054 -29.979  1.00 71.26  ? 73  LEU B C   1 
ATOM   3070  O O   . LEU B 2 73  ? 22.311  -42.418 -28.975  1.00 60.84  ? 73  LEU B O   1 
ATOM   3071  C CB  . LEU B 2 73  ? 22.521  -45.213 -28.702  1.00 65.15  ? 73  LEU B CB  1 
ATOM   3072  C CG  . LEU B 2 73  ? 21.775  -46.545 -28.585  1.00 59.92  ? 73  LEU B CG  1 
ATOM   3073  C CD1 . LEU B 2 73  ? 21.785  -47.054 -27.155  1.00 54.76  ? 73  LEU B CD1 1 
ATOM   3074  C CD2 . LEU B 2 73  ? 20.348  -46.403 -29.102  1.00 65.94  ? 73  LEU B CD2 1 
ATOM   3075  N N   . GLU B 2 74  ? 23.278  -42.483 -31.010  1.00 65.14  ? 74  GLU B N   1 
ATOM   3076  C CA  . GLU B 2 74  ? 23.474  -41.043 -31.125  1.00 61.30  ? 74  GLU B CA  1 
ATOM   3077  C C   . GLU B 2 74  ? 22.919  -40.541 -32.454  1.00 58.01  ? 74  GLU B C   1 
ATOM   3078  O O   . GLU B 2 74  ? 23.473  -39.622 -33.063  1.00 61.99  ? 74  GLU B O   1 
ATOM   3079  C CB  . GLU B 2 74  ? 24.953  -40.682 -30.974  1.00 57.72  ? 74  GLU B CB  1 
ATOM   3080  C CG  . GLU B 2 74  ? 25.535  -41.070 -29.625  1.00 57.69  ? 74  GLU B CG  1 
ATOM   3081  C CD  . GLU B 2 74  ? 27.050  -41.048 -29.617  1.00 72.44  ? 74  GLU B CD  1 
ATOM   3082  O OE1 . GLU B 2 74  ? 27.662  -41.307 -30.676  1.00 70.97  ? 74  GLU B OE1 1 
ATOM   3083  O OE2 . GLU B 2 74  ? 27.630  -40.774 -28.547  1.00 65.90  ? 74  GLU B OE2 1 
ATOM   3084  N N   . ARG B 2 75  ? 21.815  -41.140 -32.908  1.00 65.23  ? 75  ARG B N   1 
ATOM   3085  C CA  . ARG B 2 75  ? 21.243  -40.797 -34.206  1.00 62.98  ? 75  ARG B CA  1 
ATOM   3086  C C   . ARG B 2 75  ? 20.692  -39.379 -34.228  1.00 67.46  ? 75  ARG B C   1 
ATOM   3087  O O   . ARG B 2 75  ? 20.714  -38.725 -35.276  1.00 66.05  ? 75  ARG B O   1 
ATOM   3088  C CB  . ARG B 2 75  ? 20.138  -41.794 -34.571  1.00 54.62  ? 75  ARG B CB  1 
ATOM   3089  C CG  . ARG B 2 75  ? 20.568  -43.259 -34.607  1.00 49.80  ? 75  ARG B CG  1 
ATOM   3090  C CD  . ARG B 2 75  ? 21.360  -43.593 -35.864  1.00 64.84  ? 75  ARG B CD  1 
ATOM   3091  N NE  . ARG B 2 75  ? 22.757  -43.183 -35.783  1.00 82.84  ? 75  ARG B NE  1 
ATOM   3092  C CZ  . ARG B 2 75  ? 23.521  -42.928 -36.836  1.00 81.70  ? 75  ARG B CZ  1 
ATOM   3093  N NH1 . ARG B 2 75  ? 23.040  -42.981 -38.068  1.00 90.42  ? 75  ARG B NH1 1 
ATOM   3094  N NH2 . ARG B 2 75  ? 24.797  -42.602 -36.650  1.00 64.33  ? 75  ARG B NH2 1 
ATOM   3095  N N   . ARG B 2 76  ? 20.177  -38.896 -33.095  1.00 56.03  ? 76  ARG B N   1 
ATOM   3096  C CA  . ARG B 2 76  ? 19.702  -37.518 -33.023  1.00 59.62  ? 76  ARG B CA  1 
ATOM   3097  C C   . ARG B 2 76  ? 20.846  -36.532 -33.227  1.00 58.27  ? 76  ARG B C   1 
ATOM   3098  O O   . ARG B 2 76  ? 20.675  -35.493 -33.877  1.00 66.03  ? 76  ARG B O   1 
ATOM   3099  C CB  . ARG B 2 76  ? 19.004  -37.282 -31.682  1.00 47.08  ? 76  ARG B CB  1 
ATOM   3100  C CG  . ARG B 2 76  ? 17.698  -38.053 -31.545  1.00 53.12  ? 76  ARG B CG  1 
ATOM   3101  C CD  . ARG B 2 76  ? 17.187  -38.081 -30.113  1.00 60.13  ? 76  ARG B CD  1 
ATOM   3102  N NE  . ARG B 2 76  ? 18.196  -38.566 -29.179  1.00 66.58  ? 76  ARG B NE  1 
ATOM   3103  C CZ  . ARG B 2 76  ? 18.543  -37.943 -28.061  1.00 62.59  ? 76  ARG B CZ  1 
ATOM   3104  N NH1 . ARG B 2 76  ? 17.946  -36.826 -27.679  1.00 57.18  ? 76  ARG B NH1 1 
ATOM   3105  N NH2 . ARG B 2 76  ? 19.507  -38.459 -27.303  1.00 48.68  ? 76  ARG B NH2 1 
ATOM   3106  N N   . ILE B 2 77  ? 22.023  -36.841 -32.679  1.00 60.17  ? 77  ILE B N   1 
ATOM   3107  C CA  . ILE B 2 77  ? 23.190  -35.997 -32.908  1.00 62.83  ? 77  ILE B CA  1 
ATOM   3108  C C   . ILE B 2 77  ? 23.646  -36.092 -34.357  1.00 62.16  ? 77  ILE B C   1 
ATOM   3109  O O   . ILE B 2 77  ? 24.006  -35.084 -34.976  1.00 58.48  ? 77  ILE B O   1 
ATOM   3110  C CB  . ILE B 2 77  ? 24.324  -36.372 -31.940  1.00 51.66  ? 77  ILE B CB  1 
ATOM   3111  C CG1 . ILE B 2 77  ? 23.869  -36.165 -30.503  1.00 64.72  ? 77  ILE B CG1 1 
ATOM   3112  C CG2 . ILE B 2 77  ? 25.532  -35.503 -32.197  1.00 53.80  ? 77  ILE B CG2 1 
ATOM   3113  C CD1 . ILE B 2 77  ? 23.626  -34.723 -30.182  1.00 75.37  ? 77  ILE B CD1 1 
ATOM   3114  N N   . GLU B 2 78  ? 23.650  -37.305 -34.918  1.00 53.86  ? 78  GLU B N   1 
ATOM   3115  C CA  . GLU B 2 78  ? 24.067  -37.476 -36.306  1.00 61.70  ? 78  GLU B CA  1 
ATOM   3116  C C   . GLU B 2 78  ? 23.138  -36.728 -37.253  1.00 59.59  ? 78  GLU B C   1 
ATOM   3117  O O   . GLU B 2 78  ? 23.594  -36.113 -38.225  1.00 64.41  ? 78  GLU B O   1 
ATOM   3118  C CB  . GLU B 2 78  ? 24.122  -38.964 -36.658  1.00 57.35  ? 78  GLU B CB  1 
ATOM   3119  C CG  . GLU B 2 78  ? 24.442  -39.248 -38.118  1.00 65.76  ? 78  GLU B CG  1 
ATOM   3120  C CD  . GLU B 2 78  ? 23.227  -39.701 -38.905  1.00 110.51 ? 78  GLU B CD  1 
ATOM   3121  O OE1 . GLU B 2 78  ? 22.448  -40.522 -38.377  1.00 118.87 ? 78  GLU B OE1 1 
ATOM   3122  O OE2 . GLU B 2 78  ? 23.049  -39.232 -40.050  1.00 110.90 ? 78  GLU B OE2 1 
ATOM   3123  N N   . ASN B 2 79  ? 21.830  -36.768 -36.987  1.00 54.62  ? 79  ASN B N   1 
ATOM   3124  C CA  . ASN B 2 79  ? 20.891  -36.002 -37.798  1.00 61.54  ? 79  ASN B CA  1 
ATOM   3125  C C   . ASN B 2 79  ? 21.132  -34.505 -37.662  1.00 53.76  ? 79  ASN B C   1 
ATOM   3126  O O   . ASN B 2 79  ? 20.916  -33.752 -38.619  1.00 68.06  ? 79  ASN B O   1 
ATOM   3127  C CB  . ASN B 2 79  ? 19.453  -36.353 -37.411  1.00 54.77  ? 79  ASN B CB  1 
ATOM   3128  C CG  . ASN B 2 79  ? 18.432  -35.743 -38.351  1.00 67.56  ? 79  ASN B CG  1 
ATOM   3129  O OD1 . ASN B 2 79  ? 18.267  -36.194 -39.486  1.00 84.79  ? 79  ASN B OD1 1 
ATOM   3130  N ND2 . ASN B 2 79  ? 17.736  -34.717 -37.880  1.00 57.22  ? 79  ASN B ND2 1 
ATOM   3131  N N   . LEU B 2 80  ? 21.573  -34.055 -36.484  1.00 63.21  ? 80  LEU B N   1 
ATOM   3132  C CA  . LEU B 2 80  ? 21.939  -32.652 -36.315  1.00 52.91  ? 80  LEU B CA  1 
ATOM   3133  C C   . LEU B 2 80  ? 23.122  -32.283 -37.201  1.00 60.06  ? 80  LEU B C   1 
ATOM   3134  O O   . LEU B 2 80  ? 23.124  -31.224 -37.838  1.00 70.85  ? 80  LEU B O   1 
ATOM   3135  C CB  . LEU B 2 80  ? 22.259  -32.368 -34.848  1.00 58.04  ? 80  LEU B CB  1 
ATOM   3136  C CG  . LEU B 2 80  ? 22.435  -30.894 -34.486  1.00 50.55  ? 80  LEU B CG  1 
ATOM   3137  C CD1 . LEU B 2 80  ? 21.106  -30.175 -34.614  1.00 76.26  ? 80  LEU B CD1 1 
ATOM   3138  C CD2 . LEU B 2 80  ? 23.012  -30.730 -33.087  1.00 70.23  ? 80  LEU B CD2 1 
ATOM   3139  N N   . ASN B 2 81  ? 24.139  -33.148 -37.250  1.00 62.51  ? 81  ASN B N   1 
ATOM   3140  C CA  . ASN B 2 81  ? 25.281  -32.908 -38.128  1.00 55.95  ? 81  ASN B CA  1 
ATOM   3141  C C   . ASN B 2 81  ? 24.871  -32.963 -39.595  1.00 62.72  ? 81  ASN B C   1 
ATOM   3142  O O   . ASN B 2 81  ? 25.356  -32.170 -40.411  1.00 59.75  ? 81  ASN B O   1 
ATOM   3143  C CB  . ASN B 2 81  ? 26.386  -33.924 -37.837  1.00 60.89  ? 81  ASN B CB  1 
ATOM   3144  C CG  . ASN B 2 81  ? 27.506  -33.878 -38.860  1.00 62.99  ? 81  ASN B CG  1 
ATOM   3145  O OD1 . ASN B 2 81  ? 28.336  -32.969 -38.847  1.00 71.63  ? 81  ASN B OD1 1 
ATOM   3146  N ND2 . ASN B 2 81  ? 27.538  -34.865 -39.749  1.00 69.12  ? 81  ASN B ND2 1 
ATOM   3147  N N   . LYS B 2 82  ? 23.985  -33.898 -39.947  1.00 63.01  ? 82  LYS B N   1 
ATOM   3148  C CA  . LYS B 2 82  ? 23.521  -33.998 -41.327  1.00 55.99  ? 82  LYS B CA  1 
ATOM   3149  C C   . LYS B 2 82  ? 22.800  -32.728 -41.762  1.00 56.60  ? 82  LYS B C   1 
ATOM   3150  O O   . LYS B 2 82  ? 23.012  -32.236 -42.877  1.00 68.87  ? 82  LYS B O   1 
ATOM   3151  C CB  . LYS B 2 82  ? 22.606  -35.212 -41.489  1.00 60.17  ? 82  LYS B CB  1 
ATOM   3152  C CG  . LYS B 2 82  ? 21.766  -35.160 -42.750  1.00 52.34  ? 82  LYS B CG  1 
ATOM   3153  C CD  . LYS B 2 82  ? 20.782  -36.310 -42.843  1.00 64.56  ? 82  LYS B CD  1 
ATOM   3154  C CE  . LYS B 2 82  ? 19.826  -36.075 -44.002  1.00 70.14  ? 82  LYS B CE  1 
ATOM   3155  N NZ  . LYS B 2 82  ? 20.512  -35.348 -45.112  1.00 86.49  ? 82  LYS B NZ  1 
ATOM   3156  N N   . LYS B 2 83  ? 21.947  -32.179 -40.894  1.00 63.06  ? 83  LYS B N   1 
ATOM   3157  C CA  . LYS B 2 83  ? 21.251  -30.941 -41.228  1.00 61.14  ? 83  LYS B CA  1 
ATOM   3158  C C   . LYS B 2 83  ? 22.232  -29.789 -41.410  1.00 59.89  ? 83  LYS B C   1 
ATOM   3159  O O   . LYS B 2 83  ? 22.037  -28.929 -42.276  1.00 65.78  ? 83  LYS B O   1 
ATOM   3160  C CB  . LYS B 2 83  ? 20.216  -30.607 -40.152  1.00 52.32  ? 83  LYS B CB  1 
ATOM   3161  C CG  . LYS B 2 83  ? 18.929  -31.415 -40.253  1.00 60.60  ? 83  LYS B CG  1 
ATOM   3162  C CD  . LYS B 2 83  ? 17.810  -30.772 -39.450  1.00 74.20  ? 83  LYS B CD  1 
ATOM   3163  C CE  . LYS B 2 83  ? 17.992  -31.001 -37.959  1.00 81.46  ? 83  LYS B CE  1 
ATOM   3164  N NZ  . LYS B 2 83  ? 17.234  -29.999 -37.154  1.00 82.77  ? 83  LYS B NZ  1 
ATOM   3165  N N   . MET B 2 84  ? 23.293  -29.753 -40.597  1.00 63.68  ? 84  MET B N   1 
ATOM   3166  C CA  . MET B 2 84  ? 24.286  -28.690 -40.721  1.00 64.51  ? 84  MET B CA  1 
ATOM   3167  C C   . MET B 2 84  ? 25.068  -28.806 -42.026  1.00 67.49  ? 84  MET B C   1 
ATOM   3168  O O   . MET B 2 84  ? 25.287  -27.802 -42.713  1.00 63.59  ? 84  MET B O   1 
ATOM   3169  C CB  . MET B 2 84  ? 25.239  -28.718 -39.526  1.00 69.13  ? 84  MET B CB  1 
ATOM   3170  C CG  . MET B 2 84  ? 26.217  -27.551 -39.478  1.00 60.27  ? 84  MET B CG  1 
ATOM   3171  S SD  . MET B 2 84  ? 27.878  -28.038 -38.967  1.00 87.66  ? 84  MET B SD  1 
ATOM   3172  C CE  . MET B 2 84  ? 28.513  -28.735 -40.491  1.00 82.10  ? 84  MET B CE  1 
ATOM   3173  N N   . GLU B 2 85  ? 25.503  -30.017 -42.380  1.00 71.06  ? 85  GLU B N   1 
ATOM   3174  C CA  . GLU B 2 85  ? 26.269  -30.198 -43.611  1.00 62.13  ? 85  GLU B CA  1 
ATOM   3175  C C   . GLU B 2 85  ? 25.429  -29.862 -44.837  1.00 50.33  ? 85  GLU B C   1 
ATOM   3176  O O   . GLU B 2 85  ? 25.897  -29.186 -45.761  1.00 63.95  ? 85  GLU B O   1 
ATOM   3177  C CB  . GLU B 2 85  ? 26.795  -31.631 -43.702  1.00 60.30  ? 85  GLU B CB  1 
ATOM   3178  C CG  . GLU B 2 85  ? 27.920  -31.957 -42.734  1.00 66.56  ? 85  GLU B CG  1 
ATOM   3179  C CD  . GLU B 2 85  ? 28.533  -33.321 -42.996  1.00 81.26  ? 85  GLU B CD  1 
ATOM   3180  O OE1 . GLU B 2 85  ? 28.137  -33.973 -43.986  1.00 78.16  ? 85  GLU B OE1 1 
ATOM   3181  O OE2 . GLU B 2 85  ? 29.410  -33.741 -42.212  1.00 93.74  ? 85  GLU B OE2 1 
ATOM   3182  N N   . ASP B 2 86  ? 24.183  -30.335 -44.866  1.00 62.41  ? 86  ASP B N   1 
ATOM   3183  C CA  . ASP B 2 86  ? 23.323  -30.078 -46.016  1.00 69.12  ? 86  ASP B CA  1 
ATOM   3184  C C   . ASP B 2 86  ? 22.975  -28.599 -46.129  1.00 64.29  ? 86  ASP B C   1 
ATOM   3185  O O   . ASP B 2 86  ? 22.847  -28.071 -47.240  1.00 68.79  ? 86  ASP B O   1 
ATOM   3186  C CB  . ASP B 2 86  ? 22.058  -30.930 -45.921  1.00 64.50  ? 86  ASP B CB  1 
ATOM   3187  C CG  . ASP B 2 86  ? 22.353  -32.416 -45.996  1.00 74.23  ? 86  ASP B CG  1 
ATOM   3188  O OD1 . ASP B 2 86  ? 23.509  -32.775 -46.299  1.00 79.37  ? 86  ASP B OD1 1 
ATOM   3189  O OD2 . ASP B 2 86  ? 21.432  -33.224 -45.748  1.00 73.85  ? 86  ASP B OD2 1 
ATOM   3190  N N   . GLY B 2 87  ? 22.809  -27.918 -44.993  1.00 56.68  ? 87  GLY B N   1 
ATOM   3191  C CA  . GLY B 2 87  ? 22.530  -26.492 -45.032  1.00 54.00  ? 87  GLY B CA  1 
ATOM   3192  C C   . GLY B 2 87  ? 23.663  -25.691 -45.645  1.00 62.60  ? 87  GLY B C   1 
ATOM   3193  O O   . GLY B 2 87  ? 23.434  -24.799 -46.465  1.00 69.06  ? 87  GLY B O   1 
ATOM   3194  N N   . PHE B 2 88  ? 24.904  -26.002 -45.260  1.00 55.82  ? 88  PHE B N   1 
ATOM   3195  C CA  . PHE B 2 88  ? 26.053  -25.327 -45.854  1.00 54.77  ? 88  PHE B CA  1 
ATOM   3196  C C   . PHE B 2 88  ? 26.261  -25.744 -47.304  1.00 57.54  ? 88  PHE B C   1 
ATOM   3197  O O   . PHE B 2 88  ? 26.735  -24.942 -48.116  1.00 59.17  ? 88  PHE B O   1 
ATOM   3198  C CB  . PHE B 2 88  ? 27.310  -25.603 -45.029  1.00 43.53  ? 88  PHE B CB  1 
ATOM   3199  C CG  . PHE B 2 88  ? 27.398  -24.785 -43.775  1.00 52.54  ? 88  PHE B CG  1 
ATOM   3200  C CD1 . PHE B 2 88  ? 27.227  -23.411 -43.817  1.00 50.85  ? 88  PHE B CD1 1 
ATOM   3201  C CD2 . PHE B 2 88  ? 27.634  -25.389 -42.552  1.00 57.89  ? 88  PHE B CD2 1 
ATOM   3202  C CE1 . PHE B 2 88  ? 27.301  -22.654 -42.666  1.00 62.44  ? 88  PHE B CE1 1 
ATOM   3203  C CE2 . PHE B 2 88  ? 27.708  -24.636 -41.398  1.00 63.10  ? 88  PHE B CE2 1 
ATOM   3204  C CZ  . PHE B 2 88  ? 27.541  -23.267 -41.455  1.00 61.74  ? 88  PHE B CZ  1 
ATOM   3205  N N   . LEU B 2 89  ? 25.923  -26.990 -47.644  1.00 56.69  ? 89  LEU B N   1 
ATOM   3206  C CA  . LEU B 2 89  ? 25.992  -27.421 -49.036  1.00 51.00  ? 89  LEU B CA  1 
ATOM   3207  C C   . LEU B 2 89  ? 25.061  -26.592 -49.905  1.00 63.23  ? 89  LEU B C   1 
ATOM   3208  O O   . LEU B 2 89  ? 25.415  -26.213 -51.028  1.00 66.16  ? 89  LEU B O   1 
ATOM   3209  C CB  . LEU B 2 89  ? 25.639  -28.904 -49.147  1.00 47.06  ? 89  LEU B CB  1 
ATOM   3210  C CG  . LEU B 2 89  ? 25.550  -29.452 -50.574  1.00 51.52  ? 89  LEU B CG  1 
ATOM   3211  C CD1 . LEU B 2 89  ? 26.935  -29.738 -51.141  1.00 49.20  ? 89  LEU B CD1 1 
ATOM   3212  C CD2 . LEU B 2 89  ? 24.664  -30.688 -50.644  1.00 59.13  ? 89  LEU B CD2 1 
ATOM   3213  N N   . ASP B 2 90  ? 23.865  -26.304 -49.400  1.00 55.01  ? 90  ASP B N   1 
ATOM   3214  C CA  . ASP B 2 90  ? 22.900  -25.543 -50.182  1.00 57.31  ? 90  ASP B CA  1 
ATOM   3215  C C   . ASP B 2 90  ? 23.285  -24.071 -50.270  1.00 56.51  ? 90  ASP B C   1 
ATOM   3216  O O   . ASP B 2 90  ? 23.082  -23.435 -51.311  1.00 67.18  ? 90  ASP B O   1 
ATOM   3217  C CB  . ASP B 2 90  ? 21.506  -25.687 -49.577  1.00 63.46  ? 90  ASP B CB  1 
ATOM   3218  C CG  . ASP B 2 90  ? 20.990  -27.108 -49.633  1.00 68.25  ? 90  ASP B CG  1 
ATOM   3219  O OD1 . ASP B 2 90  ? 21.647  -27.955 -50.274  1.00 86.02  ? 90  ASP B OD1 1 
ATOM   3220  O OD2 . ASP B 2 90  ? 19.922  -27.374 -49.043  1.00 84.18  ? 90  ASP B OD2 1 
ATOM   3221  N N   . VAL B 2 91  ? 23.792  -23.498 -49.175  1.00 51.10  ? 91  VAL B N   1 
ATOM   3222  C CA  . VAL B 2 91  ? 24.177  -22.090 -49.185  1.00 60.41  ? 91  VAL B CA  1 
ATOM   3223  C C   . VAL B 2 91  ? 25.290  -21.848 -50.198  1.00 58.55  ? 91  VAL B C   1 
ATOM   3224  O O   . VAL B 2 91  ? 25.223  -20.918 -51.010  1.00 55.31  ? 91  VAL B O   1 
ATOM   3225  C CB  . VAL B 2 91  ? 24.592  -21.636 -47.775  1.00 48.67  ? 91  VAL B CB  1 
ATOM   3226  C CG1 . VAL B 2 91  ? 25.270  -20.282 -47.841  1.00 47.45  ? 91  VAL B CG1 1 
ATOM   3227  C CG2 . VAL B 2 91  ? 23.384  -21.581 -46.857  1.00 44.39  ? 91  VAL B CG2 1 
ATOM   3228  N N   . TRP B 2 92  ? 26.333  -22.681 -50.167  1.00 55.71  ? 92  TRP B N   1 
ATOM   3229  C CA  . TRP B 2 92  ? 27.457  -22.475 -51.076  1.00 59.86  ? 92  TRP B CA  1 
ATOM   3230  C C   . TRP B 2 92  ? 27.075  -22.775 -52.521  1.00 65.94  ? 92  TRP B C   1 
ATOM   3231  O O   . TRP B 2 92  ? 27.467  -22.041 -53.435  1.00 65.12  ? 92  TRP B O   1 
ATOM   3232  C CB  . TRP B 2 92  ? 28.649  -23.330 -50.649  1.00 54.14  ? 92  TRP B CB  1 
ATOM   3233  C CG  . TRP B 2 92  ? 29.374  -22.784 -49.459  1.00 51.53  ? 92  TRP B CG  1 
ATOM   3234  C CD1 . TRP B 2 92  ? 29.595  -23.420 -48.274  1.00 53.60  ? 92  TRP B CD1 1 
ATOM   3235  C CD2 . TRP B 2 92  ? 29.967  -21.485 -49.335  1.00 54.72  ? 92  TRP B CD2 1 
ATOM   3236  N NE1 . TRP B 2 92  ? 30.293  -22.600 -47.421  1.00 63.52  ? 92  TRP B NE1 1 
ATOM   3237  C CE2 . TRP B 2 92  ? 30.533  -21.407 -48.048  1.00 57.33  ? 92  TRP B CE2 1 
ATOM   3238  C CE3 . TRP B 2 92  ? 30.076  -20.381 -50.187  1.00 62.40  ? 92  TRP B CE3 1 
ATOM   3239  C CZ2 . TRP B 2 92  ? 31.199  -20.271 -47.593  1.00 62.52  ? 92  TRP B CZ2 1 
ATOM   3240  C CZ3 . TRP B 2 92  ? 30.736  -19.255 -49.733  1.00 61.83  ? 92  TRP B CZ3 1 
ATOM   3241  C CH2 . TRP B 2 92  ? 31.287  -19.208 -48.447  1.00 59.05  ? 92  TRP B CH2 1 
ATOM   3242  N N   . THR B 2 93  ? 26.314  -23.848 -52.749  1.00 59.09  ? 93  THR B N   1 
ATOM   3243  C CA  . THR B 2 93  ? 25.926  -24.199 -54.111  1.00 57.97  ? 93  THR B CA  1 
ATOM   3244  C C   . THR B 2 93  ? 25.068  -23.106 -54.736  1.00 62.07  ? 93  THR B C   1 
ATOM   3245  O O   . THR B 2 93  ? 25.282  -22.715 -55.889  1.00 70.90  ? 93  THR B O   1 
ATOM   3246  C CB  . THR B 2 93  ? 25.180  -25.535 -54.123  1.00 58.71  ? 93  THR B CB  1 
ATOM   3247  O OG1 . THR B 2 93  ? 26.042  -26.570 -53.634  1.00 60.59  ? 93  THR B OG1 1 
ATOM   3248  C CG2 . THR B 2 93  ? 24.727  -25.883 -55.534  1.00 49.77  ? 93  THR B CG2 1 
ATOM   3249  N N   . TYR B 2 94  ? 24.092  -22.595 -53.984  1.00 61.13  ? 94  TYR B N   1 
ATOM   3250  C CA  . TYR B 2 94  ? 23.223  -21.549 -54.512  1.00 59.47  ? 94  TYR B CA  1 
ATOM   3251  C C   . TYR B 2 94  ? 23.993  -20.253 -54.737  1.00 64.37  ? 94  TYR B C   1 
ATOM   3252  O O   . TYR B 2 94  ? 23.856  -19.613 -55.786  1.00 59.14  ? 94  TYR B O   1 
ATOM   3253  C CB  . TYR B 2 94  ? 22.045  -21.322 -53.563  1.00 58.13  ? 94  TYR B CB  1 
ATOM   3254  C CG  . TYR B 2 94  ? 20.972  -20.409 -54.115  1.00 58.89  ? 94  TYR B CG  1 
ATOM   3255  C CD1 . TYR B 2 94  ? 20.062  -20.869 -55.057  1.00 54.48  ? 94  TYR B CD1 1 
ATOM   3256  C CD2 . TYR B 2 94  ? 20.863  -19.092 -53.687  1.00 61.10  ? 94  TYR B CD2 1 
ATOM   3257  C CE1 . TYR B 2 94  ? 19.076  -20.043 -55.563  1.00 64.52  ? 94  TYR B CE1 1 
ATOM   3258  C CE2 . TYR B 2 94  ? 19.879  -18.256 -54.187  1.00 63.76  ? 94  TYR B CE2 1 
ATOM   3259  C CZ  . TYR B 2 94  ? 18.989  -18.738 -55.125  1.00 66.06  ? 94  TYR B CZ  1 
ATOM   3260  O OH  . TYR B 2 94  ? 18.007  -17.915 -55.629  1.00 62.13  ? 94  TYR B OH  1 
ATOM   3261  N N   . ASN B 2 95  ? 24.807  -19.848 -53.758  1.00 63.54  ? 95  ASN B N   1 
ATOM   3262  C CA  . ASN B 2 95  ? 25.546  -18.595 -53.883  1.00 68.29  ? 95  ASN B CA  1 
ATOM   3263  C C   . ASN B 2 95  ? 26.564  -18.657 -55.015  1.00 69.48  ? 95  ASN B C   1 
ATOM   3264  O O   . ASN B 2 95  ? 26.696  -17.704 -55.793  1.00 71.46  ? 95  ASN B O   1 
ATOM   3265  C CB  . ASN B 2 95  ? 26.238  -18.251 -52.562  1.00 61.10  ? 95  ASN B CB  1 
ATOM   3266  C CG  . ASN B 2 95  ? 25.260  -17.845 -51.473  1.00 79.89  ? 95  ASN B CG  1 
ATOM   3267  O OD1 . ASN B 2 95  ? 25.649  -17.637 -50.322  1.00 86.74  ? 95  ASN B OD1 1 
ATOM   3268  N ND2 . ASN B 2 95  ? 23.985  -17.738 -51.828  1.00 83.36  ? 95  ASN B ND2 1 
ATOM   3269  N N   . ALA B 2 96  ? 27.298  -19.768 -55.122  1.00 60.24  ? 96  ALA B N   1 
ATOM   3270  C CA  . ALA B 2 96  ? 28.317  -19.884 -56.162  1.00 61.82  ? 96  ALA B CA  1 
ATOM   3271  C C   . ALA B 2 96  ? 27.697  -19.879 -57.554  1.00 66.54  ? 96  ALA B C   1 
ATOM   3272  O O   . ALA B 2 96  ? 28.209  -19.222 -58.468  1.00 74.72  ? 96  ALA B O   1 
ATOM   3273  C CB  . ALA B 2 96  ? 29.145  -21.151 -55.951  1.00 47.22  ? 96  ALA B CB  1 
ATOM   3274  N N   . GLU B 2 97  ? 26.594  -20.611 -57.736  1.00 68.24  ? 97  GLU B N   1 
ATOM   3275  C CA  . GLU B 2 97  ? 25.947  -20.666 -59.043  1.00 63.10  ? 97  GLU B CA  1 
ATOM   3276  C C   . GLU B 2 97  ? 25.431  -19.296 -59.466  1.00 63.67  ? 97  GLU B C   1 
ATOM   3277  O O   . GLU B 2 97  ? 25.596  -18.892 -60.623  1.00 78.80  ? 97  GLU B O   1 
ATOM   3278  C CB  . GLU B 2 97  ? 24.804  -21.682 -59.022  1.00 62.34  ? 97  GLU B CB  1 
ATOM   3279  C CG  . GLU B 2 97  ? 25.243  -23.141 -59.017  1.00 69.00  ? 97  GLU B CG  1 
ATOM   3280  C CD  . GLU B 2 97  ? 25.477  -23.694 -60.410  1.00 100.83 ? 97  GLU B CD  1 
ATOM   3281  O OE1 . GLU B 2 97  ? 25.551  -22.895 -61.368  1.00 102.62 ? 97  GLU B OE1 1 
ATOM   3282  O OE2 . GLU B 2 97  ? 25.579  -24.932 -60.548  1.00 112.02 ? 97  GLU B OE2 1 
ATOM   3283  N N   . LEU B 2 98  ? 24.806  -18.565 -58.542  1.00 57.92  ? 98  LEU B N   1 
ATOM   3284  C CA  . LEU B 2 98  ? 24.218  -17.274 -58.880  1.00 64.63  ? 98  LEU B CA  1 
ATOM   3285  C C   . LEU B 2 98  ? 25.270  -16.182 -59.026  1.00 65.32  ? 98  LEU B C   1 
ATOM   3286  O O   . LEU B 2 98  ? 25.104  -15.279 -59.854  1.00 72.84  ? 98  LEU B O   1 
ATOM   3287  C CB  . LEU B 2 98  ? 23.181  -16.874 -57.826  1.00 54.56  ? 98  LEU B CB  1 
ATOM   3288  C CG  . LEU B 2 98  ? 21.728  -17.323 -58.029  1.00 54.48  ? 98  LEU B CG  1 
ATOM   3289  C CD1 . LEU B 2 98  ? 21.045  -16.476 -59.090  1.00 65.45  ? 98  LEU B CD1 1 
ATOM   3290  C CD2 . LEU B 2 98  ? 21.636  -18.799 -58.392  1.00 63.39  ? 98  LEU B CD2 1 
ATOM   3291  N N   . LEU B 2 99  ? 26.346  -16.240 -58.237  1.00 69.11  ? 99  LEU B N   1 
ATOM   3292  C CA  . LEU B 2 99  ? 27.422  -15.263 -58.378  1.00 65.48  ? 99  LEU B CA  1 
ATOM   3293  C C   . LEU B 2 99  ? 28.082  -15.367 -59.747  1.00 72.77  ? 99  LEU B C   1 
ATOM   3294  O O   . LEU B 2 99  ? 28.368  -14.348 -60.386  1.00 78.72  ? 99  LEU B O   1 
ATOM   3295  C CB  . LEU B 2 99  ? 28.459  -15.458 -57.273  1.00 60.97  ? 99  LEU B CB  1 
ATOM   3296  C CG  . LEU B 2 99  ? 29.718  -14.596 -57.391  1.00 72.35  ? 99  LEU B CG  1 
ATOM   3297  C CD1 . LEU B 2 99  ? 29.618  -13.355 -56.513  1.00 75.98  ? 99  LEU B CD1 1 
ATOM   3298  C CD2 . LEU B 2 99  ? 30.966  -15.403 -57.064  1.00 66.14  ? 99  LEU B CD2 1 
ATOM   3299  N N   . VAL B 2 100 ? 28.332  -16.593 -60.211  1.00 66.44  ? 100 VAL B N   1 
ATOM   3300  C CA  . VAL B 2 100 ? 28.923  -16.787 -61.531  1.00 61.67  ? 100 VAL B CA  1 
ATOM   3301  C C   . VAL B 2 100 ? 27.994  -16.259 -62.617  1.00 66.44  ? 100 VAL B C   1 
ATOM   3302  O O   . VAL B 2 100 ? 28.433  -15.573 -63.549  1.00 72.17  ? 100 VAL B O   1 
ATOM   3303  C CB  . VAL B 2 100 ? 29.270  -18.273 -61.747  1.00 64.41  ? 100 VAL B CB  1 
ATOM   3304  C CG1 . VAL B 2 100 ? 29.443  -18.577 -63.227  1.00 65.64  ? 100 VAL B CG1 1 
ATOM   3305  C CG2 . VAL B 2 100 ? 30.534  -18.639 -60.982  1.00 65.97  ? 100 VAL B CG2 1 
ATOM   3306  N N   . LEU B 2 101 ? 26.698  -16.564 -62.520  1.00 68.36  ? 101 LEU B N   1 
ATOM   3307  C CA  . LEU B 2 101 ? 25.751  -16.069 -63.516  1.00 61.40  ? 101 LEU B CA  1 
ATOM   3308  C C   . LEU B 2 101 ? 25.689  -14.547 -63.513  1.00 66.68  ? 101 LEU B C   1 
ATOM   3309  O O   . LEU B 2 101 ? 25.648  -13.916 -64.576  1.00 72.78  ? 101 LEU B O   1 
ATOM   3310  C CB  . LEU B 2 101 ? 24.361  -16.654 -63.267  1.00 55.92  ? 101 LEU B CB  1 
ATOM   3311  C CG  . LEU B 2 101 ? 24.177  -18.154 -63.495  1.00 60.49  ? 101 LEU B CG  1 
ATOM   3312  C CD1 . LEU B 2 101 ? 22.700  -18.526 -63.479  1.00 61.10  ? 101 LEU B CD1 1 
ATOM   3313  C CD2 . LEU B 2 101 ? 24.825  -18.584 -64.797  1.00 64.48  ? 101 LEU B CD2 1 
ATOM   3314  N N   . MET B 2 102 ? 25.674  -13.940 -62.325  1.00 66.42  ? 102 MET B N   1 
ATOM   3315  C CA  . MET B 2 102 ? 25.592  -12.486 -62.232  1.00 63.92  ? 102 MET B CA  1 
ATOM   3316  C C   . MET B 2 102 ? 26.864  -11.823 -62.746  1.00 72.07  ? 102 MET B C   1 
ATOM   3317  O O   . MET B 2 102 ? 26.804  -10.865 -63.524  1.00 75.03  ? 102 MET B O   1 
ATOM   3318  C CB  . MET B 2 102 ? 25.311  -12.074 -60.787  1.00 71.22  ? 102 MET B CB  1 
ATOM   3319  C CG  . MET B 2 102 ? 23.867  -12.270 -60.356  1.00 81.86  ? 102 MET B CG  1 
ATOM   3320  S SD  . MET B 2 102 ? 23.696  -12.420 -58.568  1.00 105.18 ? 102 MET B SD  1 
ATOM   3321  C CE  . MET B 2 102 ? 24.776  -11.104 -58.013  1.00 77.25  ? 102 MET B CE  1 
ATOM   3322  N N   . GLU B 2 103 ? 28.030  -12.320 -62.324  1.00 72.54  ? 103 GLU B N   1 
ATOM   3323  C CA  . GLU B 2 103 ? 29.283  -11.689 -62.728  1.00 73.34  ? 103 GLU B CA  1 
ATOM   3324  C C   . GLU B 2 103 ? 29.596  -11.925 -64.200  1.00 73.49  ? 103 GLU B C   1 
ATOM   3325  O O   . GLU B 2 103 ? 30.202  -11.061 -64.846  1.00 81.57  ? 103 GLU B O   1 
ATOM   3326  C CB  . GLU B 2 103 ? 30.430  -12.183 -61.848  1.00 70.13  ? 103 GLU B CB  1 
ATOM   3327  C CG  . GLU B 2 103 ? 30.424  -11.555 -60.470  1.00 73.21  ? 103 GLU B CG  1 
ATOM   3328  C CD  . GLU B 2 103 ? 30.207  -10.055 -60.529  1.00 90.36  ? 103 GLU B CD  1 
ATOM   3329  O OE1 . GLU B 2 103 ? 31.077  -9.347  -61.078  1.00 96.02  ? 103 GLU B OE1 1 
ATOM   3330  O OE2 . GLU B 2 103 ? 29.157  -9.586  -60.041  1.00 99.86  ? 103 GLU B OE2 1 
ATOM   3331  N N   . ASN B 2 104 ? 29.207  -13.079 -64.746  1.00 64.79  ? 104 ASN B N   1 
ATOM   3332  C CA  . ASN B 2 104 ? 29.379  -13.304 -66.178  1.00 62.65  ? 104 ASN B CA  1 
ATOM   3333  C C   . ASN B 2 104 ? 28.557  -12.309 -66.987  1.00 65.46  ? 104 ASN B C   1 
ATOM   3334  O O   . ASN B 2 104 ? 28.995  -11.845 -68.046  1.00 74.83  ? 104 ASN B O   1 
ATOM   3335  C CB  . ASN B 2 104 ? 28.997  -14.738 -66.543  1.00 55.68  ? 104 ASN B CB  1 
ATOM   3336  C CG  . ASN B 2 104 ? 30.119  -15.726 -66.283  1.00 62.04  ? 104 ASN B CG  1 
ATOM   3337  O OD1 . ASN B 2 104 ? 31.188  -15.356 -65.797  1.00 68.96  ? 104 ASN B OD1 1 
ATOM   3338  N ND2 . ASN B 2 104 ? 29.879  -16.993 -66.604  1.00 62.22  ? 104 ASN B ND2 1 
ATOM   3339  N N   . GLU B 2 105 ? 27.358  -11.975 -66.506  1.00 72.05  ? 105 GLU B N   1 
ATOM   3340  C CA  . GLU B 2 105 ? 26.551  -10.959 -67.171  1.00 76.47  ? 105 GLU B CA  1 
ATOM   3341  C C   . GLU B 2 105 ? 27.242  -9.601  -67.133  1.00 74.05  ? 105 GLU B C   1 
ATOM   3342  O O   . GLU B 2 105 ? 27.294  -8.889  -68.143  1.00 81.89  ? 105 GLU B O   1 
ATOM   3343  C CB  . GLU B 2 105 ? 25.172  -10.876 -66.516  1.00 72.85  ? 105 GLU B CB  1 
ATOM   3344  C CG  . GLU B 2 105 ? 24.166  -10.047 -67.296  1.00 71.60  ? 105 GLU B CG  1 
ATOM   3345  C CD  . GLU B 2 105 ? 23.622  -10.785 -68.503  1.00 105.28 ? 105 GLU B CD  1 
ATOM   3346  O OE1 . GLU B 2 105 ? 23.310  -11.987 -68.370  1.00 100.23 ? 105 GLU B OE1 1 
ATOM   3347  O OE2 . GLU B 2 105 ? 23.513  -10.167 -69.583  1.00 102.67 ? 105 GLU B OE2 1 
ATOM   3348  N N   . ARG B 2 106 ? 27.788  -9.227  -65.973  1.00 69.65  ? 106 ARG B N   1 
ATOM   3349  C CA  . ARG B 2 106 ? 28.400  -7.909  -65.838  1.00 78.03  ? 106 ARG B CA  1 
ATOM   3350  C C   . ARG B 2 106 ? 29.701  -7.816  -66.626  1.00 77.91  ? 106 ARG B C   1 
ATOM   3351  O O   . ARG B 2 106 ? 30.014  -6.763  -67.192  1.00 77.93  ? 106 ARG B O   1 
ATOM   3352  C CB  . ARG B 2 106 ? 28.642  -7.587  -64.364  1.00 66.25  ? 106 ARG B CB  1 
ATOM   3353  C CG  . ARG B 2 106 ? 28.374  -6.134  -64.010  1.00 89.78  ? 106 ARG B CG  1 
ATOM   3354  C CD  . ARG B 2 106 ? 28.884  -5.789  -62.623  1.00 123.27 ? 106 ARG B CD  1 
ATOM   3355  N NE  . ARG B 2 106 ? 30.328  -5.959  -62.523  1.00 123.42 ? 106 ARG B NE  1 
ATOM   3356  C CZ  . ARG B 2 106 ? 31.218  -5.082  -62.969  1.00 115.33 ? 106 ARG B CZ  1 
ATOM   3357  N NH1 . ARG B 2 106 ? 30.845  -3.957  -63.559  1.00 115.38 ? 106 ARG B NH1 1 
ATOM   3358  N NH2 . ARG B 2 106 ? 32.514  -5.342  -62.824  1.00 94.24  ? 106 ARG B NH2 1 
ATOM   3359  N N   . THR B 2 107 ? 30.477  -8.903  -66.665  1.00 74.20  ? 107 THR B N   1 
ATOM   3360  C CA  . THR B 2 107 ? 31.735  -8.886  -67.404  1.00 70.05  ? 107 THR B CA  1 
ATOM   3361  C C   . THR B 2 107 ? 31.497  -8.671  -68.894  1.00 68.40  ? 107 THR B C   1 
ATOM   3362  O O   . THR B 2 107 ? 32.220  -7.907  -69.544  1.00 67.47  ? 107 THR B O   1 
ATOM   3363  C CB  . THR B 2 107 ? 32.501  -10.189 -67.171  1.00 66.67  ? 107 THR B CB  1 
ATOM   3364  O OG1 . THR B 2 107 ? 32.652  -10.413 -65.763  1.00 77.11  ? 107 THR B OG1 1 
ATOM   3365  C CG2 . THR B 2 107 ? 33.876  -10.124 -67.816  1.00 65.79  ? 107 THR B CG2 1 
ATOM   3366  N N   . LEU B 2 108 ? 30.489  -9.341  -69.452  1.00 68.90  ? 108 LEU B N   1 
ATOM   3367  C CA  . LEU B 2 108 ? 30.184  -9.174  -70.869  1.00 61.94  ? 108 LEU B CA  1 
ATOM   3368  C C   . LEU B 2 108 ? 29.602  -7.793  -71.150  1.00 67.52  ? 108 LEU B C   1 
ATOM   3369  O O   . LEU B 2 108 ? 29.920  -7.177  -72.173  1.00 76.11  ? 108 LEU B O   1 
ATOM   3370  C CB  . LEU B 2 108 ? 29.230  -10.274 -71.331  1.00 48.35  ? 108 LEU B CB  1 
ATOM   3371  C CG  . LEU B 2 108 ? 29.837  -11.586 -71.843  1.00 58.68  ? 108 LEU B CG  1 
ATOM   3372  C CD1 . LEU B 2 108 ? 31.078  -11.998 -71.064  1.00 53.51  ? 108 LEU B CD1 1 
ATOM   3373  C CD2 . LEU B 2 108 ? 28.795  -12.693 -71.795  1.00 61.72  ? 108 LEU B CD2 1 
ATOM   3374  N N   . ASP B 2 109 ? 28.744  -7.292  -70.257  1.00 63.64  ? 109 ASP B N   1 
ATOM   3375  C CA  . ASP B 2 109 ? 28.288  -5.911  -70.374  1.00 73.42  ? 109 ASP B CA  1 
ATOM   3376  C C   . ASP B 2 109 ? 29.446  -4.934  -70.218  1.00 73.55  ? 109 ASP B C   1 
ATOM   3377  O O   . ASP B 2 109 ? 29.452  -3.868  -70.844  1.00 73.96  ? 109 ASP B O   1 
ATOM   3378  C CB  . ASP B 2 109 ? 27.206  -5.615  -69.332  1.00 79.43  ? 109 ASP B CB  1 
ATOM   3379  C CG  . ASP B 2 109 ? 25.926  -6.392  -69.577  1.00 90.48  ? 109 ASP B CG  1 
ATOM   3380  O OD1 . ASP B 2 109 ? 25.991  -7.467  -70.209  1.00 98.16  ? 109 ASP B OD1 1 
ATOM   3381  O OD2 . ASP B 2 109 ? 24.852  -5.918  -69.142  1.00 93.99  ? 109 ASP B OD2 1 
ATOM   3382  N N   . PHE B 2 110 ? 30.425  -5.277  -69.378  1.00 76.51  ? 110 PHE B N   1 
ATOM   3383  C CA  . PHE B 2 110 ? 31.599  -4.430  -69.200  1.00 68.73  ? 110 PHE B CA  1 
ATOM   3384  C C   . PHE B 2 110 ? 32.383  -4.294  -70.500  1.00 76.38  ? 110 PHE B C   1 
ATOM   3385  O O   . PHE B 2 110 ? 32.849  -3.200  -70.841  1.00 73.64  ? 110 PHE B O   1 
ATOM   3386  C CB  . PHE B 2 110 ? 32.476  -5.002  -68.085  1.00 58.08  ? 110 PHE B CB  1 
ATOM   3387  C CG  . PHE B 2 110 ? 33.861  -4.428  -68.036  1.00 57.43  ? 110 PHE B CG  1 
ATOM   3388  C CD1 . PHE B 2 110 ? 34.077  -3.141  -67.575  1.00 60.80  ? 110 PHE B CD1 1 
ATOM   3389  C CD2 . PHE B 2 110 ? 34.951  -5.190  -68.427  1.00 64.85  ? 110 PHE B CD2 1 
ATOM   3390  C CE1 . PHE B 2 110 ? 35.352  -2.615  -67.523  1.00 63.53  ? 110 PHE B CE1 1 
ATOM   3391  C CE2 . PHE B 2 110 ? 36.229  -4.671  -68.376  1.00 74.21  ? 110 PHE B CE2 1 
ATOM   3392  C CZ  . PHE B 2 110 ? 36.430  -3.381  -67.922  1.00 75.89  ? 110 PHE B CZ  1 
ATOM   3393  N N   . HIS B 2 111 ? 32.541  -5.396  -71.237  1.00 65.55  ? 111 HIS B N   1 
ATOM   3394  C CA  . HIS B 2 111 ? 33.237  -5.341  -72.518  1.00 60.93  ? 111 HIS B CA  1 
ATOM   3395  C C   . HIS B 2 111 ? 32.489  -4.470  -73.520  1.00 76.65  ? 111 HIS B C   1 
ATOM   3396  O O   . HIS B 2 111 ? 33.104  -3.696  -74.263  1.00 79.64  ? 111 HIS B O   1 
ATOM   3397  C CB  . HIS B 2 111 ? 33.430  -6.754  -73.069  1.00 53.68  ? 111 HIS B CB  1 
ATOM   3398  C CG  . HIS B 2 111 ? 34.475  -7.545  -72.347  1.00 69.50  ? 111 HIS B CG  1 
ATOM   3399  N ND1 . HIS B 2 111 ? 35.646  -6.982  -71.887  1.00 66.22  ? 111 HIS B ND1 1 
ATOM   3400  C CD2 . HIS B 2 111 ? 34.528  -8.855  -72.007  1.00 77.26  ? 111 HIS B CD2 1 
ATOM   3401  C CE1 . HIS B 2 111 ? 36.375  -7.910  -71.294  1.00 74.85  ? 111 HIS B CE1 1 
ATOM   3402  N NE2 . HIS B 2 111 ? 35.720  -9.055  -71.354  1.00 87.46  ? 111 HIS B NE2 1 
ATOM   3403  N N   . ASP B 2 112 ? 31.160  -4.589  -73.562  1.00 83.60  ? 112 ASP B N   1 
ATOM   3404  C CA  . ASP B 2 112 ? 30.368  -3.755  -74.459  1.00 62.57  ? 112 ASP B CA  1 
ATOM   3405  C C   . ASP B 2 112 ? 30.495  -2.281  -74.096  1.00 64.74  ? 112 ASP B C   1 
ATOM   3406  O O   . ASP B 2 112 ? 30.582  -1.421  -74.980  1.00 75.54  ? 112 ASP B O   1 
ATOM   3407  C CB  . ASP B 2 112 ? 28.904  -4.194  -74.427  1.00 73.88  ? 112 ASP B CB  1 
ATOM   3408  C CG  . ASP B 2 112 ? 28.707  -5.608  -74.939  1.00 94.86  ? 112 ASP B CG  1 
ATOM   3409  O OD1 . ASP B 2 112 ? 29.683  -6.197  -75.449  1.00 110.66 ? 112 ASP B OD1 1 
ATOM   3410  O OD2 . ASP B 2 112 ? 27.576  -6.131  -74.832  1.00 109.76 ? 112 ASP B OD2 1 
ATOM   3411  N N   . SER B 2 113 ? 30.505  -1.970  -72.799  1.00 62.12  ? 113 SER B N   1 
ATOM   3412  C CA  . SER B 2 113 ? 30.623  -0.579  -72.373  1.00 67.75  ? 113 SER B CA  1 
ATOM   3413  C C   . SER B 2 113 ? 31.932  0.040   -72.850  1.00 73.38  ? 113 SER B C   1 
ATOM   3414  O O   . SER B 2 113 ? 31.971  1.220   -73.218  1.00 67.98  ? 113 SER B O   1 
ATOM   3415  C CB  . SER B 2 113 ? 30.512  -0.487  -70.851  1.00 75.13  ? 113 SER B CB  1 
ATOM   3416  O OG  . SER B 2 113 ? 30.672  0.849   -70.408  1.00 81.81  ? 113 SER B OG  1 
ATOM   3417  N N   . ASN B 2 114 ? 33.015  -0.740  -72.846  1.00 70.90  ? 114 ASN B N   1 
ATOM   3418  C CA  . ASN B 2 114 ? 34.315  -0.207  -73.244  1.00 80.49  ? 114 ASN B CA  1 
ATOM   3419  C C   . ASN B 2 114 ? 34.362  0.114   -74.734  1.00 74.11  ? 114 ASN B C   1 
ATOM   3420  O O   . ASN B 2 114 ? 34.899  1.155   -75.131  1.00 68.58  ? 114 ASN B O   1 
ATOM   3421  C CB  . ASN B 2 114 ? 35.421  -1.193  -72.874  1.00 68.41  ? 114 ASN B CB  1 
ATOM   3422  C CG  . ASN B 2 114 ? 35.547  -1.389  -71.378  1.00 76.31  ? 114 ASN B CG  1 
ATOM   3423  O OD1 . ASN B 2 114 ? 35.169  -0.520  -70.592  1.00 70.55  ? 114 ASN B OD1 1 
ATOM   3424  N ND2 . ASN B 2 114 ? 36.083  -2.534  -70.976  1.00 69.56  ? 114 ASN B ND2 1 
ATOM   3425  N N   . VAL B 2 115 ? 33.819  -0.769  -75.574  1.00 65.56  ? 115 VAL B N   1 
ATOM   3426  C CA  . VAL B 2 115 ? 33.842  -0.528  -77.014  1.00 72.97  ? 115 VAL B CA  1 
ATOM   3427  C C   . VAL B 2 115 ? 32.973  0.674   -77.367  1.00 68.82  ? 115 VAL B C   1 
ATOM   3428  O O   . VAL B 2 115 ? 33.317  1.469   -78.249  1.00 70.83  ? 115 VAL B O   1 
ATOM   3429  C CB  . VAL B 2 115 ? 33.404  -1.793  -77.774  1.00 58.39  ? 115 VAL B CB  1 
ATOM   3430  C CG1 . VAL B 2 115 ? 33.349  -1.530  -79.274  1.00 52.98  ? 115 VAL B CG1 1 
ATOM   3431  C CG2 . VAL B 2 115 ? 34.343  -2.948  -77.467  1.00 55.15  ? 115 VAL B CG2 1 
ATOM   3432  N N   . LYS B 2 116 ? 31.836  0.825   -76.686  1.00 66.59  ? 116 LYS B N   1 
ATOM   3433  C CA  . LYS B 2 116 ? 30.956  1.959   -76.953  1.00 62.67  ? 116 LYS B CA  1 
ATOM   3434  C C   . LYS B 2 116 ? 31.624  3.278   -76.579  1.00 71.57  ? 116 LYS B C   1 
ATOM   3435  O O   . LYS B 2 116 ? 31.515  4.267   -77.313  1.00 80.40  ? 116 LYS B O   1 
ATOM   3436  C CB  . LYS B 2 116 ? 29.638  1.781   -76.196  1.00 73.79  ? 116 LYS B CB  1 
ATOM   3437  C CG  . LYS B 2 116 ? 28.429  2.409   -76.874  1.00 78.31  ? 116 LYS B CG  1 
ATOM   3438  C CD  . LYS B 2 116 ? 28.157  3.813   -76.363  1.00 94.38  ? 116 LYS B CD  1 
ATOM   3439  C CE  . LYS B 2 116 ? 27.040  4.471   -77.156  1.00 98.77  ? 116 LYS B CE  1 
ATOM   3440  N NZ  . LYS B 2 116 ? 27.411  4.593   -78.593  1.00 83.62  ? 116 LYS B NZ  1 
ATOM   3441  N N   . ASN B 2 117 ? 32.317  3.313   -75.437  1.00 71.45  ? 117 ASN B N   1 
ATOM   3442  C CA  . ASN B 2 117 ? 33.033  4.522   -75.041  1.00 73.63  ? 117 ASN B CA  1 
ATOM   3443  C C   . ASN B 2 117 ? 34.153  4.849   -76.021  1.00 72.72  ? 117 ASN B C   1 
ATOM   3444  O O   . ASN B 2 117 ? 34.393  6.021   -76.333  1.00 84.62  ? 117 ASN B O   1 
ATOM   3445  C CB  . ASN B 2 117 ? 33.590  4.371   -73.624  1.00 64.50  ? 117 ASN B CB  1 
ATOM   3446  C CG  . ASN B 2 117 ? 32.522  4.512   -72.556  1.00 86.87  ? 117 ASN B CG  1 
ATOM   3447  O OD1 . ASN B 2 117 ? 32.824  4.536   -71.363  1.00 105.29 ? 117 ASN B OD1 1 
ATOM   3448  N ND2 . ASN B 2 117 ? 31.267  4.605   -72.979  1.00 99.75  ? 117 ASN B ND2 1 
ATOM   3449  N N   . LEU B 2 118 ? 34.855  3.824   -76.512  1.00 64.58  ? 118 LEU B N   1 
ATOM   3450  C CA  . LEU B 2 118 ? 35.915  4.052   -77.489  1.00 65.36  ? 118 LEU B CA  1 
ATOM   3451  C C   . LEU B 2 118 ? 35.358  4.670   -78.765  1.00 76.29  ? 118 LEU B C   1 
ATOM   3452  O O   . LEU B 2 118 ? 35.972  5.572   -79.347  1.00 76.76  ? 118 LEU B O   1 
ATOM   3453  C CB  . LEU B 2 118 ? 36.635  2.739   -77.796  1.00 58.87  ? 118 LEU B CB  1 
ATOM   3454  C CG  . LEU B 2 118 ? 37.965  2.846   -78.541  1.00 76.12  ? 118 LEU B CG  1 
ATOM   3455  C CD1 . LEU B 2 118 ? 38.982  3.593   -77.695  1.00 70.61  ? 118 LEU B CD1 1 
ATOM   3456  C CD2 . LEU B 2 118 ? 38.481  1.466   -78.914  1.00 67.71  ? 118 LEU B CD2 1 
ATOM   3457  N N   . TYR B 2 119 ? 34.193  4.195   -79.215  1.00 73.59  ? 119 TYR B N   1 
ATOM   3458  C CA  . TYR B 2 119 ? 33.546  4.792   -80.378  1.00 68.95  ? 119 TYR B CA  1 
ATOM   3459  C C   . TYR B 2 119 ? 33.155  6.238   -80.105  1.00 73.88  ? 119 TYR B C   1 
ATOM   3460  O O   . TYR B 2 119 ? 33.280  7.101   -80.983  1.00 79.49  ? 119 TYR B O   1 
ATOM   3461  C CB  . TYR B 2 119 ? 32.320  3.967   -80.775  1.00 57.67  ? 119 TYR B CB  1 
ATOM   3462  C CG  . TYR B 2 119 ? 31.565  4.515   -81.965  1.00 67.45  ? 119 TYR B CG  1 
ATOM   3463  C CD1 . TYR B 2 119 ? 30.540  5.440   -81.798  1.00 59.11  ? 119 TYR B CD1 1 
ATOM   3464  C CD2 . TYR B 2 119 ? 31.874  4.106   -83.256  1.00 79.88  ? 119 TYR B CD2 1 
ATOM   3465  C CE1 . TYR B 2 119 ? 29.851  5.947   -82.883  1.00 66.48  ? 119 TYR B CE1 1 
ATOM   3466  C CE2 . TYR B 2 119 ? 31.187  4.604   -84.346  1.00 77.26  ? 119 TYR B CE2 1 
ATOM   3467  C CZ  . TYR B 2 119 ? 30.180  5.525   -84.155  1.00 71.77  ? 119 TYR B CZ  1 
ATOM   3468  O OH  . TYR B 2 119 ? 29.495  6.023   -85.240  1.00 77.50  ? 119 TYR B OH  1 
ATOM   3469  N N   . ASP B 2 120 ? 32.673  6.522   -78.893  1.00 64.91  ? 120 ASP B N   1 
ATOM   3470  C CA  . ASP B 2 120 ? 32.240  7.876   -78.566  1.00 68.25  ? 120 ASP B CA  1 
ATOM   3471  C C   . ASP B 2 120 ? 33.414  8.846   -78.516  1.00 71.70  ? 120 ASP B C   1 
ATOM   3472  O O   . ASP B 2 120 ? 33.271  10.013  -78.897  1.00 82.91  ? 120 ASP B O   1 
ATOM   3473  C CB  . ASP B 2 120 ? 31.481  7.878   -77.238  1.00 89.00  ? 120 ASP B CB  1 
ATOM   3474  C CG  . ASP B 2 120 ? 30.119  7.219   -77.342  1.00 89.11  ? 120 ASP B CG  1 
ATOM   3475  O OD1 . ASP B 2 120 ? 29.743  6.806   -78.460  1.00 88.60  ? 120 ASP B OD1 1 
ATOM   3476  O OD2 . ASP B 2 120 ? 29.424  7.112   -76.311  1.00 88.52  ? 120 ASP B OD2 1 
ATOM   3477  N N   . LYS B 2 121 ? 34.577  8.391   -78.045  1.00 81.79  ? 121 LYS B N   1 
ATOM   3478  C CA  . LYS B 2 121 ? 35.735  9.278   -77.987  1.00 86.13  ? 121 LYS B CA  1 
ATOM   3479  C C   . LYS B 2 121 ? 36.195  9.683   -79.383  1.00 77.23  ? 121 LYS B C   1 
ATOM   3480  O O   . LYS B 2 121 ? 36.574  10.839  -79.603  1.00 79.34  ? 121 LYS B O   1 
ATOM   3481  C CB  . LYS B 2 121 ? 36.875  8.618   -77.210  1.00 74.49  ? 121 LYS B CB  1 
ATOM   3482  C CG  . LYS B 2 121 ? 36.533  8.338   -75.758  1.00 87.10  ? 121 LYS B CG  1 
ATOM   3483  C CD  . LYS B 2 121 ? 35.737  9.488   -75.164  1.00 106.23 ? 121 LYS B CD  1 
ATOM   3484  C CE  . LYS B 2 121 ? 34.756  8.990   -74.120  1.00 105.11 ? 121 LYS B CE  1 
ATOM   3485  N NZ  . LYS B 2 121 ? 33.528  9.831   -74.094  1.00 97.65  ? 121 LYS B NZ  1 
ATOM   3486  N N   . VAL B 2 122 ? 36.175  8.749   -80.335  1.00 67.29  ? 122 VAL B N   1 
ATOM   3487  C CA  . VAL B 2 122 ? 36.522  9.090   -81.713  1.00 68.58  ? 122 VAL B CA  1 
ATOM   3488  C C   . VAL B 2 122 ? 35.484  10.036  -82.306  1.00 70.98  ? 122 VAL B C   1 
ATOM   3489  O O   . VAL B 2 122 ? 35.826  11.033  -82.952  1.00 74.47  ? 122 VAL B O   1 
ATOM   3490  C CB  . VAL B 2 122 ? 36.677  7.816   -82.564  1.00 58.53  ? 122 VAL B CB  1 
ATOM   3491  C CG1 . VAL B 2 122 ? 36.790  8.175   -84.037  1.00 60.27  ? 122 VAL B CG1 1 
ATOM   3492  C CG2 . VAL B 2 122 ? 37.898  7.028   -82.118  1.00 56.12  ? 122 VAL B CG2 1 
ATOM   3493  N N   . ARG B 2 123 ? 34.199  9.739   -82.091  1.00 78.47  ? 123 ARG B N   1 
ATOM   3494  C CA  . ARG B 2 123 ? 33.138  10.610  -82.591  1.00 73.79  ? 123 ARG B CA  1 
ATOM   3495  C C   . ARG B 2 123 ? 33.221  11.992  -81.959  1.00 70.30  ? 123 ARG B C   1 
ATOM   3496  O O   . ARG B 2 123 ? 32.941  13.004  -82.613  1.00 64.60  ? 123 ARG B O   1 
ATOM   3497  C CB  . ARG B 2 123 ? 31.771  9.982   -82.316  1.00 67.50  ? 123 ARG B CB  1 
ATOM   3498  C CG  . ARG B 2 123 ? 30.597  10.763  -82.886  1.00 69.96  ? 123 ARG B CG  1 
ATOM   3499  C CD  . ARG B 2 123 ? 29.278  10.269  -82.316  1.00 64.41  ? 123 ARG B CD  1 
ATOM   3500  N NE  . ARG B 2 123 ? 29.161  10.536  -80.887  1.00 94.45  ? 123 ARG B NE  1 
ATOM   3501  C CZ  . ARG B 2 123 ? 28.188  10.070  -80.116  1.00 100.68 ? 123 ARG B CZ  1 
ATOM   3502  N NH1 . ARG B 2 123 ? 27.248  9.273   -80.597  1.00 84.14  ? 123 ARG B NH1 1 
ATOM   3503  N NH2 . ARG B 2 123 ? 28.155  10.415  -78.832  1.00 89.70  ? 123 ARG B NH2 1 
ATOM   3504  N N   . LEU B 2 124 ? 33.595  12.050  -80.680  1.00 67.70  ? 124 LEU B N   1 
ATOM   3505  C CA  . LEU B 2 124 ? 33.732  13.333  -80.003  1.00 68.02  ? 124 LEU B CA  1 
ATOM   3506  C C   . LEU B 2 124 ? 34.833  14.177  -80.638  1.00 76.00  ? 124 LEU B C   1 
ATOM   3507  O O   . LEU B 2 124 ? 34.723  15.407  -80.703  1.00 73.80  ? 124 LEU B O   1 
ATOM   3508  C CB  . LEU B 2 124 ? 34.005  13.102  -78.517  1.00 74.52  ? 124 LEU B CB  1 
ATOM   3509  C CG  . LEU B 2 124 ? 33.870  14.288  -77.565  1.00 87.27  ? 124 LEU B CG  1 
ATOM   3510  C CD1 . LEU B 2 124 ? 32.575  15.033  -77.828  1.00 80.98  ? 124 LEU B CD1 1 
ATOM   3511  C CD2 . LEU B 2 124 ? 33.926  13.807  -76.123  1.00 89.31  ? 124 LEU B CD2 1 
ATOM   3512  N N   . GLN B 2 125 ? 35.904  13.534  -81.113  1.00 80.94  ? 125 GLN B N   1 
ATOM   3513  C CA  . GLN B 2 125 ? 36.986  14.275  -81.754  1.00 63.30  ? 125 GLN B CA  1 
ATOM   3514  C C   . GLN B 2 125 ? 36.581  14.767  -83.139  1.00 74.00  ? 125 GLN B C   1 
ATOM   3515  O O   . GLN B 2 125 ? 36.735  15.952  -83.458  1.00 64.51  ? 125 GLN B O   1 
ATOM   3516  C CB  . GLN B 2 125 ? 38.237  13.404  -81.864  1.00 69.72  ? 125 GLN B CB  1 
ATOM   3517  C CG  . GLN B 2 125 ? 38.798  12.896  -80.555  1.00 65.73  ? 125 GLN B CG  1 
ATOM   3518  C CD  . GLN B 2 125 ? 39.945  11.928  -80.775  1.00 67.24  ? 125 GLN B CD  1 
ATOM   3519  O OE1 . GLN B 2 125 ? 41.075  12.340  -81.033  1.00 69.76  ? 125 GLN B OE1 1 
ATOM   3520  N NE2 . GLN B 2 125 ? 39.654  10.633  -80.698  1.00 65.93  ? 125 GLN B NE2 1 
ATOM   3521  N N   . LEU B 2 126 ? 36.073  13.863  -83.981  1.00 68.96  ? 126 LEU B N   1 
ATOM   3522  C CA  . LEU B 2 126 ? 35.927  14.167  -85.402  1.00 61.18  ? 126 LEU B CA  1 
ATOM   3523  C C   . LEU B 2 126 ? 34.807  15.171  -85.653  1.00 70.47  ? 126 LEU B C   1 
ATOM   3524  O O   . LEU B 2 126 ? 34.994  16.147  -86.391  1.00 78.32  ? 126 LEU B O   1 
ATOM   3525  C CB  . LEU B 2 126 ? 35.688  12.876  -86.185  1.00 61.96  ? 126 LEU B CB  1 
ATOM   3526  C CG  . LEU B 2 126 ? 36.763  11.803  -85.996  1.00 60.72  ? 126 LEU B CG  1 
ATOM   3527  C CD1 . LEU B 2 126 ? 36.501  10.599  -86.888  1.00 52.34  ? 126 LEU B CD1 1 
ATOM   3528  C CD2 . LEU B 2 126 ? 38.150  12.377  -86.250  1.00 57.75  ? 126 LEU B CD2 1 
ATOM   3529  N N   . ARG B 2 127 ? 33.641  14.950  -85.049  1.00 74.20  ? 127 ARG B N   1 
ATOM   3530  C CA  . ARG B 2 127 ? 32.466  15.824  -85.197  1.00 62.56  ? 127 ARG B CA  1 
ATOM   3531  C C   . ARG B 2 127 ? 32.111  15.895  -86.682  1.00 70.52  ? 127 ARG B C   1 
ATOM   3532  O O   . ARG B 2 127 ? 31.968  14.840  -87.320  1.00 73.27  ? 127 ARG B O   1 
ATOM   3533  C CB  . ARG B 2 127 ? 32.747  17.157  -84.516  1.00 61.21  ? 127 ARG B CB  1 
ATOM   3534  C CG  . ARG B 2 127 ? 32.677  17.109  -82.998  1.00 77.38  ? 127 ARG B CG  1 
ATOM   3535  C CD  . ARG B 2 127 ? 33.571  18.175  -82.400  1.00 85.90  ? 127 ARG B CD  1 
ATOM   3536  N NE  . ARG B 2 127 ? 33.379  19.466  -83.048  1.00 102.92 ? 127 ARG B NE  1 
ATOM   3537  C CZ  . ARG B 2 127 ? 34.236  20.475  -82.977  1.00 113.65 ? 127 ARG B CZ  1 
ATOM   3538  N NH1 . ARG B 2 127 ? 35.382  20.364  -82.324  1.00 90.02  ? 127 ARG B NH1 1 
ATOM   3539  N NH2 . ARG B 2 127 ? 33.937  21.623  -83.577  1.00 104.43 ? 127 ARG B NH2 1 
ATOM   3540  N N   . ASP B 2 128 ? 31.961  17.083  -87.269  1.00 67.36  ? 128 ASP B N   1 
ATOM   3541  C CA  . ASP B 2 128 ? 31.525  17.212  -88.655  1.00 67.00  ? 128 ASP B CA  1 
ATOM   3542  C C   . ASP B 2 128 ? 32.640  16.978  -89.667  1.00 74.41  ? 128 ASP B C   1 
ATOM   3543  O O   . ASP B 2 128 ? 32.364  16.976  -90.872  1.00 68.71  ? 128 ASP B O   1 
ATOM   3544  C CB  . ASP B 2 128 ? 30.905  18.593  -88.895  1.00 59.16  ? 128 ASP B CB  1 
ATOM   3545  C CG  . ASP B 2 128 ? 31.596  19.688  -88.109  1.00 100.59 ? 128 ASP B CG  1 
ATOM   3546  O OD1 . ASP B 2 128 ? 30.887  20.525  -87.511  1.00 106.09 ? 128 ASP B OD1 1 
ATOM   3547  O OD2 . ASP B 2 128 ? 32.844  19.700  -88.076  1.00 94.59  ? 128 ASP B OD2 1 
ATOM   3548  N N   . ASN B 2 129 ? 33.884  16.792  -89.221  1.00 70.71  ? 129 ASN B N   1 
ATOM   3549  C CA  . ASN B 2 129 ? 34.964  16.476  -90.147  1.00 65.52  ? 129 ASN B CA  1 
ATOM   3550  C C   . ASN B 2 129 ? 34.866  15.062  -90.703  1.00 65.14  ? 129 ASN B C   1 
ATOM   3551  O O   . ASN B 2 129 ? 35.572  14.744  -91.666  1.00 63.32  ? 129 ASN B O   1 
ATOM   3552  C CB  . ASN B 2 129 ? 36.318  16.669  -89.463  1.00 69.08  ? 129 ASN B CB  1 
ATOM   3553  C CG  . ASN B 2 129 ? 36.732  18.125  -89.396  1.00 79.26  ? 129 ASN B CG  1 
ATOM   3554  O OD1 . ASN B 2 129 ? 35.955  19.019  -89.730  1.00 90.13  ? 129 ASN B OD1 1 
ATOM   3555  N ND2 . ASN B 2 129 ? 37.963  18.372  -88.963  1.00 79.75  ? 129 ASN B ND2 1 
ATOM   3556  N N   . ALA B 2 130 ? 34.019  14.212  -90.126  1.00 65.89  ? 130 ALA B N   1 
ATOM   3557  C CA  . ALA B 2 130 ? 33.848  12.848  -90.598  1.00 60.65  ? 130 ALA B CA  1 
ATOM   3558  C C   . ALA B 2 130 ? 32.377  12.468  -90.520  1.00 79.18  ? 130 ALA B C   1 
ATOM   3559  O O   . ALA B 2 130 ? 31.589  13.086  -89.800  1.00 73.87  ? 130 ALA B O   1 
ATOM   3560  C CB  . ALA B 2 130 ? 34.697  11.856  -89.794  1.00 63.63  ? 130 ALA B CB  1 
ATOM   3561  N N   . LYS B 2 131 ? 32.019  11.433  -91.272  1.00 73.10  ? 131 LYS B N   1 
ATOM   3562  C CA  . LYS B 2 131 ? 30.643  10.974  -91.405  1.00 75.71  ? 131 LYS B CA  1 
ATOM   3563  C C   . LYS B 2 131 ? 30.504  9.612   -90.738  1.00 82.39  ? 131 LYS B C   1 
ATOM   3564  O O   . LYS B 2 131 ? 31.251  8.681   -91.061  1.00 85.92  ? 131 LYS B O   1 
ATOM   3565  C CB  . LYS B 2 131 ? 30.249  10.905  -92.880  1.00 69.99  ? 131 LYS B CB  1 
ATOM   3566  C CG  . LYS B 2 131 ? 29.143  9.918   -93.207  1.00 68.55  ? 131 LYS B CG  1 
ATOM   3567  C CD  . LYS B 2 131 ? 28.933  9.838   -94.712  1.00 69.96  ? 131 LYS B CD  1 
ATOM   3568  C CE  . LYS B 2 131 ? 27.671  9.067   -95.055  1.00 83.40  ? 131 LYS B CE  1 
ATOM   3569  N NZ  . LYS B 2 131 ? 27.418  9.053   -96.522  1.00 90.71  ? 131 LYS B NZ  1 
ATOM   3570  N N   . GLU B 2 132 ? 29.555  9.499   -89.809  1.00 68.48  ? 132 GLU B N   1 
ATOM   3571  C CA  . GLU B 2 132 ? 29.266  8.210   -89.194  1.00 66.39  ? 132 GLU B CA  1 
ATOM   3572  C C   . GLU B 2 132 ? 28.554  7.314   -90.198  1.00 68.08  ? 132 GLU B C   1 
ATOM   3573  O O   . GLU B 2 132 ? 27.538  7.703   -90.783  1.00 76.62  ? 132 GLU B O   1 
ATOM   3574  C CB  . GLU B 2 132 ? 28.405  8.387   -87.944  1.00 60.87  ? 132 GLU B CB  1 
ATOM   3575  C CG  . GLU B 2 132 ? 28.967  9.343   -86.907  1.00 81.28  ? 132 GLU B CG  1 
ATOM   3576  C CD  . GLU B 2 132 ? 28.149  9.349   -85.629  1.00 79.60  ? 132 GLU B CD  1 
ATOM   3577  O OE1 . GLU B 2 132 ? 27.836  8.253   -85.118  1.00 93.24  ? 132 GLU B OE1 1 
ATOM   3578  O OE2 . GLU B 2 132 ? 27.807  10.447  -85.142  1.00 90.88  ? 132 GLU B OE2 1 
ATOM   3579  N N   . LEU B 2 133 ? 29.086  6.113   -90.399  1.00 67.11  ? 133 LEU B N   1 
ATOM   3580  C CA  . LEU B 2 133 ? 28.524  5.177   -91.362  1.00 64.59  ? 133 LEU B CA  1 
ATOM   3581  C C   . LEU B 2 133 ? 27.492  4.238   -90.751  1.00 70.87  ? 133 LEU B C   1 
ATOM   3582  O O   . LEU B 2 133 ? 26.873  3.461   -91.485  1.00 81.81  ? 133 LEU B O   1 
ATOM   3583  C CB  . LEU B 2 133 ? 29.640  4.363   -92.016  1.00 67.89  ? 133 LEU B CB  1 
ATOM   3584  C CG  . LEU B 2 133 ? 30.643  5.169   -92.843  1.00 74.65  ? 133 LEU B CG  1 
ATOM   3585  C CD1 . LEU B 2 133 ? 31.476  4.235   -93.696  1.00 74.53  ? 133 LEU B CD1 1 
ATOM   3586  C CD2 . LEU B 2 133 ? 29.937  6.204   -93.707  1.00 72.29  ? 133 LEU B CD2 1 
ATOM   3587  N N   . GLY B 2 134 ? 27.292  4.289   -89.436  1.00 84.16  ? 134 GLY B N   1 
ATOM   3588  C CA  . GLY B 2 134 ? 26.289  3.476   -88.785  1.00 85.70  ? 134 GLY B CA  1 
ATOM   3589  C C   . GLY B 2 134 ? 26.711  2.066   -88.441  1.00 81.21  ? 134 GLY B C   1 
ATOM   3590  O O   . GLY B 2 134 ? 25.891  1.306   -87.910  1.00 90.62  ? 134 GLY B O   1 
ATOM   3591  N N   . ASN B 2 135 ? 27.958  1.684   -88.724  1.00 82.56  ? 135 ASN B N   1 
ATOM   3592  C CA  . ASN B 2 135 ? 28.450  0.343   -88.429  1.00 83.76  ? 135 ASN B CA  1 
ATOM   3593  C C   . ASN B 2 135 ? 29.687  0.367   -87.537  1.00 85.59  ? 135 ASN B C   1 
ATOM   3594  O O   . ASN B 2 135 ? 30.405  -0.635  -87.451  1.00 76.44  ? 135 ASN B O   1 
ATOM   3595  C CB  . ASN B 2 135 ? 28.749  -0.414  -89.725  1.00 82.12  ? 135 ASN B CB  1 
ATOM   3596  C CG  . ASN B 2 135 ? 29.740  0.317   -90.615  1.00 88.73  ? 135 ASN B CG  1 
ATOM   3597  O OD1 . ASN B 2 135 ? 30.244  1.384   -90.263  1.00 95.56  ? 135 ASN B OD1 1 
ATOM   3598  N ND2 . ASN B 2 135 ? 30.028  -0.261  -91.775  1.00 76.41  ? 135 ASN B ND2 1 
ATOM   3599  N N   . GLY B 2 136 ? 29.949  1.486   -86.868  1.00 81.21  ? 136 GLY B N   1 
ATOM   3600  C CA  . GLY B 2 136 ? 31.156  1.644   -86.090  1.00 79.80  ? 136 GLY B CA  1 
ATOM   3601  C C   . GLY B 2 136 ? 32.313  2.278   -86.830  1.00 79.63  ? 136 GLY B C   1 
ATOM   3602  O O   . GLY B 2 136 ? 33.391  2.435   -86.241  1.00 76.45  ? 136 GLY B O   1 
ATOM   3603  N N   . CYS B 2 137 ? 32.129  2.648   -88.094  1.00 72.04  ? 137 CYS B N   1 
ATOM   3604  C CA  . CYS B 2 137 ? 33.170  3.263   -88.901  1.00 75.02  ? 137 CYS B CA  1 
ATOM   3605  C C   . CYS B 2 137 ? 32.853  4.732   -89.147  1.00 71.01  ? 137 CYS B C   1 
ATOM   3606  O O   . CYS B 2 137 ? 31.688  5.138   -89.190  1.00 77.50  ? 137 CYS B O   1 
ATOM   3607  C CB  . CYS B 2 137 ? 33.328  2.545   -90.247  1.00 62.42  ? 137 CYS B CB  1 
ATOM   3608  S SG  . CYS B 2 137 ? 33.911  0.836   -90.159  1.00 115.16 ? 137 CYS B SG  1 
ATOM   3609  N N   . PHE B 2 138 ? 33.908  5.525   -89.304  1.00 71.03  ? 138 PHE B N   1 
ATOM   3610  C CA  . PHE B 2 138 ? 33.809  6.929   -89.672  1.00 75.86  ? 138 PHE B CA  1 
ATOM   3611  C C   . PHE B 2 138 ? 34.482  7.129   -91.021  1.00 76.83  ? 138 PHE B C   1 
ATOM   3612  O O   . PHE B 2 138 ? 35.539  6.550   -91.285  1.00 62.10  ? 138 PHE B O   1 
ATOM   3613  C CB  . PHE B 2 138 ? 34.475  7.835   -88.633  1.00 60.62  ? 138 PHE B CB  1 
ATOM   3614  C CG  . PHE B 2 138 ? 33.902  7.708   -87.253  1.00 63.88  ? 138 PHE B CG  1 
ATOM   3615  C CD1 . PHE B 2 138 ? 34.353  6.724   -86.391  1.00 86.15  ? 138 PHE B CD1 1 
ATOM   3616  C CD2 . PHE B 2 138 ? 32.929  8.588   -86.810  1.00 67.66  ? 138 PHE B CD2 1 
ATOM   3617  C CE1 . PHE B 2 138 ? 33.835  6.610   -85.117  1.00 70.98  ? 138 PHE B CE1 1 
ATOM   3618  C CE2 . PHE B 2 138 ? 32.407  8.480   -85.536  1.00 73.99  ? 138 PHE B CE2 1 
ATOM   3619  C CZ  . PHE B 2 138 ? 32.862  7.492   -84.688  1.00 73.11  ? 138 PHE B CZ  1 
ATOM   3620  N N   . GLU B 2 139 ? 33.869  7.938   -91.876  1.00 79.30  ? 139 GLU B N   1 
ATOM   3621  C CA  . GLU B 2 139 ? 34.440  8.275   -93.173  1.00 76.26  ? 139 GLU B CA  1 
ATOM   3622  C C   . GLU B 2 139 ? 34.872  9.734   -93.145  1.00 81.44  ? 139 GLU B C   1 
ATOM   3623  O O   . GLU B 2 139 ? 34.035  10.629  -92.979  1.00 66.94  ? 139 GLU B O   1 
ATOM   3624  C CB  . GLU B 2 139 ? 33.440  8.016   -94.298  1.00 73.20  ? 139 GLU B CB  1 
ATOM   3625  C CG  . GLU B 2 139 ? 34.003  8.235   -95.688  1.00 91.62  ? 139 GLU B CG  1 
ATOM   3626  C CD  . GLU B 2 139 ? 33.022  7.858   -96.781  1.00 98.74  ? 139 GLU B CD  1 
ATOM   3627  O OE1 . GLU B 2 139 ? 32.659  6.666   -96.874  1.00 109.94 ? 139 GLU B OE1 1 
ATOM   3628  O OE2 . GLU B 2 139 ? 32.612  8.755   -97.547  1.00 91.05  ? 139 GLU B OE2 1 
ATOM   3629  N N   . PHE B 2 140 ? 36.172  9.968   -93.303  1.00 75.57  ? 140 PHE B N   1 
ATOM   3630  C CA  . PHE B 2 140 ? 36.710  11.317  -93.208  1.00 77.82  ? 140 PHE B CA  1 
ATOM   3631  C C   . PHE B 2 140 ? 36.289  12.161  -94.404  1.00 80.56  ? 140 PHE B C   1 
ATOM   3632  O O   . PHE B 2 140 ? 36.216  11.675  -95.536  1.00 70.55  ? 140 PHE B O   1 
ATOM   3633  C CB  . PHE B 2 140 ? 38.235  11.276  -93.113  1.00 77.87  ? 140 PHE B CB  1 
ATOM   3634  C CG  . PHE B 2 140 ? 38.751  10.964  -91.739  1.00 71.80  ? 140 PHE B CG  1 
ATOM   3635  C CD1 . PHE B 2 140 ? 38.955  11.976  -90.817  1.00 72.06  ? 140 PHE B CD1 1 
ATOM   3636  C CD2 . PHE B 2 140 ? 39.039  9.661   -91.368  1.00 69.31  ? 140 PHE B CD2 1 
ATOM   3637  C CE1 . PHE B 2 140 ? 39.432  11.695  -89.549  1.00 76.46  ? 140 PHE B CE1 1 
ATOM   3638  C CE2 . PHE B 2 140 ? 39.517  9.373   -90.104  1.00 64.93  ? 140 PHE B CE2 1 
ATOM   3639  C CZ  . PHE B 2 140 ? 39.713  10.391  -89.193  1.00 61.38  ? 140 PHE B CZ  1 
ATOM   3640  N N   . TYR B 2 141 ? 36.015  13.436  -94.143  1.00 76.67  ? 141 TYR B N   1 
ATOM   3641  C CA  . TYR B 2 141 ? 35.728  14.412  -95.185  1.00 76.18  ? 141 TYR B CA  1 
ATOM   3642  C C   . TYR B 2 141 ? 36.982  15.097  -95.707  1.00 79.18  ? 141 TYR B C   1 
ATOM   3643  O O   . TYR B 2 141 ? 36.872  16.030  -96.507  1.00 82.30  ? 141 TYR B O   1 
ATOM   3644  C CB  . TYR B 2 141 ? 34.748  15.471  -94.666  1.00 69.27  ? 141 TYR B CB  1 
ATOM   3645  C CG  . TYR B 2 141 ? 33.303  15.029  -94.655  1.00 65.66  ? 141 TYR B CG  1 
ATOM   3646  C CD1 . TYR B 2 141 ? 32.741  14.396  -95.757  1.00 64.54  ? 141 TYR B CD1 1 
ATOM   3647  C CD2 . TYR B 2 141 ? 32.499  15.242  -93.542  1.00 66.78  ? 141 TYR B CD2 1 
ATOM   3648  C CE1 . TYR B 2 141 ? 31.420  13.992  -95.753  1.00 50.34  ? 141 TYR B CE1 1 
ATOM   3649  C CE2 . TYR B 2 141 ? 31.178  14.839  -93.526  1.00 73.40  ? 141 TYR B CE2 1 
ATOM   3650  C CZ  . TYR B 2 141 ? 30.643  14.216  -94.635  1.00 69.63  ? 141 TYR B CZ  1 
ATOM   3651  O OH  . TYR B 2 141 ? 29.328  13.813  -94.626  1.00 80.61  ? 141 TYR B OH  1 
ATOM   3652  N N   . HIS B 2 142 ? 38.164  14.677  -95.263  1.00 84.43  ? 142 HIS B N   1 
ATOM   3653  C CA  . HIS B 2 142 ? 39.423  15.251  -95.716  1.00 71.58  ? 142 HIS B CA  1 
ATOM   3654  C C   . HIS B 2 142 ? 40.446  14.133  -95.864  1.00 68.91  ? 142 HIS B C   1 
ATOM   3655  O O   . HIS B 2 142 ? 40.138  12.952  -95.681  1.00 73.61  ? 142 HIS B O   1 
ATOM   3656  C CB  . HIS B 2 142 ? 39.916  16.336  -94.751  1.00 74.90  ? 142 HIS B CB  1 
ATOM   3657  C CG  . HIS B 2 142 ? 40.152  15.841  -93.358  1.00 76.91  ? 142 HIS B CG  1 
ATOM   3658  N ND1 . HIS B 2 142 ? 41.327  15.231  -92.974  1.00 75.92  ? 142 HIS B ND1 1 
ATOM   3659  C CD2 . HIS B 2 142 ? 39.362  15.859  -92.259  1.00 72.90  ? 142 HIS B CD2 1 
ATOM   3660  C CE1 . HIS B 2 142 ? 41.252  14.900  -91.697  1.00 64.96  ? 142 HIS B CE1 1 
ATOM   3661  N NE2 . HIS B 2 142 ? 40.070  15.271  -91.240  1.00 69.41  ? 142 HIS B NE2 1 
ATOM   3662  N N   . LYS B 2 143 ? 41.675  14.512  -96.205  1.00 86.17  ? 143 LYS B N   1 
ATOM   3663  C CA  . LYS B 2 143 ? 42.774  13.563  -96.333  1.00 76.10  ? 143 LYS B CA  1 
ATOM   3664  C C   . LYS B 2 143 ? 43.416  13.368  -94.964  1.00 79.92  ? 143 LYS B C   1 
ATOM   3665  O O   . LYS B 2 143 ? 43.977  14.312  -94.398  1.00 96.44  ? 143 LYS B O   1 
ATOM   3666  C CB  . LYS B 2 143 ? 43.807  14.064  -97.343  1.00 85.56  ? 143 LYS B CB  1 
ATOM   3667  C CG  . LYS B 2 143 ? 44.144  13.082  -98.458  1.00 92.43  ? 143 LYS B CG  1 
ATOM   3668  C CD  . LYS B 2 143 ? 43.010  12.965  -99.466  1.00 86.90  ? 143 LYS B CD  1 
ATOM   3669  C CE  . LYS B 2 143 ? 43.473  12.270  -100.738 1.00 93.43  ? 143 LYS B CE  1 
ATOM   3670  N NZ  . LYS B 2 143 ? 44.531  13.054  -101.436 1.00 83.89  ? 143 LYS B NZ  1 
ATOM   3671  N N   . CYS B 2 144 ? 43.325  12.152  -94.430  1.00 74.15  ? 144 CYS B N   1 
ATOM   3672  C CA  . CYS B 2 144 ? 43.871  11.824  -93.114  1.00 82.05  ? 144 CYS B CA  1 
ATOM   3673  C C   . CYS B 2 144 ? 44.976  10.793  -93.297  1.00 78.16  ? 144 CYS B C   1 
ATOM   3674  O O   . CYS B 2 144 ? 44.701  9.617   -93.560  1.00 71.39  ? 144 CYS B O   1 
ATOM   3675  C CB  . CYS B 2 144 ? 42.778  11.310  -92.178  1.00 67.74  ? 144 CYS B CB  1 
ATOM   3676  S SG  . CYS B 2 144 ? 43.331  10.824  -90.517  1.00 83.35  ? 144 CYS B SG  1 
ATOM   3677  N N   . ASP B 2 145 ? 46.221  11.237  -93.162  1.00 75.88  ? 145 ASP B N   1 
ATOM   3678  C CA  . ASP B 2 145 ? 47.373  10.363  -93.308  1.00 78.42  ? 145 ASP B CA  1 
ATOM   3679  C C   . ASP B 2 145 ? 47.589  9.558   -92.026  1.00 79.03  ? 145 ASP B C   1 
ATOM   3680  O O   . ASP B 2 145 ? 46.821  9.649   -91.064  1.00 75.04  ? 145 ASP B O   1 
ATOM   3681  C CB  . ASP B 2 145 ? 48.604  11.185  -93.684  1.00 65.30  ? 145 ASP B CB  1 
ATOM   3682  C CG  . ASP B 2 145 ? 48.694  12.486  -92.906  1.00 81.09  ? 145 ASP B CG  1 
ATOM   3683  O OD1 . ASP B 2 145 ? 49.818  13.004  -92.735  1.00 94.35  ? 145 ASP B OD1 1 
ATOM   3684  O OD2 . ASP B 2 145 ? 47.641  12.985  -92.456  1.00 109.07 ? 145 ASP B OD2 1 
ATOM   3685  N N   . ASN B 2 146 ? 48.653  8.750   -92.015  1.00 70.09  ? 146 ASN B N   1 
ATOM   3686  C CA  . ASN B 2 146 ? 48.921  7.895   -90.862  1.00 64.58  ? 146 ASN B CA  1 
ATOM   3687  C C   . ASN B 2 146 ? 49.200  8.720   -89.611  1.00 64.47  ? 146 ASN B C   1 
ATOM   3688  O O   . ASN B 2 146 ? 48.822  8.325   -88.501  1.00 64.63  ? 146 ASN B O   1 
ATOM   3689  C CB  . ASN B 2 146 ? 50.089  6.958   -91.166  1.00 51.78  ? 146 ASN B CB  1 
ATOM   3690  C CG  . ASN B 2 146 ? 49.702  5.834   -92.109  1.00 60.50  ? 146 ASN B CG  1 
ATOM   3691  O OD1 . ASN B 2 146 ? 48.558  5.750   -92.557  1.00 74.87  ? 146 ASN B OD1 1 
ATOM   3692  N ND2 . ASN B 2 146 ? 50.657  4.965   -92.418  1.00 61.19  ? 146 ASN B ND2 1 
ATOM   3693  N N   . GLU B 2 147 ? 49.869  9.864   -89.769  1.00 68.40  ? 147 GLU B N   1 
ATOM   3694  C CA  . GLU B 2 147 ? 50.070  10.763  -88.638  1.00 71.11  ? 147 GLU B CA  1 
ATOM   3695  C C   . GLU B 2 147 ? 48.740  11.295  -88.119  1.00 77.78  ? 147 GLU B C   1 
ATOM   3696  O O   . GLU B 2 147 ? 48.531  11.394  -86.904  1.00 75.79  ? 147 GLU B O   1 
ATOM   3697  C CB  . GLU B 2 147 ? 50.997  11.909  -89.043  1.00 62.41  ? 147 GLU B CB  1 
ATOM   3698  C CG  . GLU B 2 147 ? 51.097  13.041  -88.032  1.00 84.65  ? 147 GLU B CG  1 
ATOM   3699  C CD  . GLU B 2 147 ? 50.202  14.216  -88.383  1.00 89.91  ? 147 GLU B CD  1 
ATOM   3700  O OE1 . GLU B 2 147 ? 49.820  14.971  -87.464  1.00 94.14  ? 147 GLU B OE1 1 
ATOM   3701  O OE2 . GLU B 2 147 ? 49.879  14.383  -89.578  1.00 105.17 ? 147 GLU B OE2 1 
ATOM   3702  N N   . CYS B 2 148 ? 47.826  11.641  -89.028  1.00 78.53  ? 148 CYS B N   1 
ATOM   3703  C CA  . CYS B 2 148 ? 46.492  12.063  -88.617  1.00 73.69  ? 148 CYS B CA  1 
ATOM   3704  C C   . CYS B 2 148 ? 45.744  10.932  -87.920  1.00 71.68  ? 148 CYS B C   1 
ATOM   3705  O O   . CYS B 2 148 ? 45.043  11.161  -86.926  1.00 59.91  ? 148 CYS B O   1 
ATOM   3706  C CB  . CYS B 2 148 ? 45.708  12.569  -89.831  1.00 76.98  ? 148 CYS B CB  1 
ATOM   3707  S SG  . CYS B 2 148 ? 43.915  12.555  -89.625  1.00 74.12  ? 148 CYS B SG  1 
ATOM   3708  N N   . MET B 2 149 ? 45.884  9.703   -88.426  1.00 61.79  ? 149 MET B N   1 
ATOM   3709  C CA  . MET B 2 149 ? 45.187  8.563   -87.835  1.00 55.57  ? 149 MET B CA  1 
ATOM   3710  C C   . MET B 2 149 ? 45.648  8.313   -86.402  1.00 71.36  ? 149 MET B C   1 
ATOM   3711  O O   . MET B 2 149 ? 44.838  7.968   -85.533  1.00 83.02  ? 149 MET B O   1 
ATOM   3712  C CB  . MET B 2 149 ? 45.400  7.318   -88.699  1.00 48.04  ? 149 MET B CB  1 
ATOM   3713  C CG  . MET B 2 149 ? 44.694  7.360   -90.052  1.00 66.57  ? 149 MET B CG  1 
ATOM   3714  S SD  . MET B 2 149 ? 42.898  7.225   -89.933  1.00 77.21  ? 149 MET B SD  1 
ATOM   3715  C CE  . MET B 2 149 ? 42.441  7.189   -91.667  1.00 71.54  ? 149 MET B CE  1 
ATOM   3716  N N   . GLU B 2 150 ? 46.949  8.478   -86.144  1.00 65.59  ? 150 GLU B N   1 
ATOM   3717  C CA  . GLU B 2 150 ? 47.483  8.315   -84.795  1.00 70.95  ? 150 GLU B CA  1 
ATOM   3718  C C   . GLU B 2 150 ? 46.829  9.289   -83.824  1.00 62.84  ? 150 GLU B C   1 
ATOM   3719  O O   . GLU B 2 150 ? 46.442  8.909   -82.710  1.00 83.12  ? 150 GLU B O   1 
ATOM   3720  C CB  . GLU B 2 150 ? 48.999  8.523   -84.803  1.00 81.53  ? 150 GLU B CB  1 
ATOM   3721  C CG  . GLU B 2 150 ? 49.831  7.294   -84.449  1.00 80.35  ? 150 GLU B CG  1 
ATOM   3722  C CD  . GLU B 2 150 ? 49.594  6.805   -83.039  1.00 106.18 ? 150 GLU B CD  1 
ATOM   3723  O OE1 . GLU B 2 150 ? 49.138  5.647   -82.867  1.00 118.88 ? 150 GLU B OE1 1 
ATOM   3724  O OE2 . GLU B 2 150 ? 49.886  7.595   -82.108  1.00 112.17 ? 150 GLU B OE2 1 
ATOM   3725  N N   . SER B 2 151 ? 46.716  10.561  -84.230  1.00 65.34  ? 151 SER B N   1 
ATOM   3726  C CA  . SER B 2 151 ? 46.110  11.580  -83.374  1.00 78.42  ? 151 SER B CA  1 
ATOM   3727  C C   . SER B 2 151 ? 44.695  11.191  -82.970  1.00 72.56  ? 151 SER B C   1 
ATOM   3728  O O   . SER B 2 151 ? 44.273  11.451  -81.838  1.00 72.22  ? 151 SER B O   1 
ATOM   3729  C CB  . SER B 2 151 ? 46.106  12.937  -84.081  1.00 68.77  ? 151 SER B CB  1 
ATOM   3730  O OG  . SER B 2 151 ? 45.234  12.923  -85.196  1.00 69.98  ? 151 SER B OG  1 
ATOM   3731  N N   . VAL B 2 152 ? 43.946  10.569  -83.883  1.00 71.65  ? 152 VAL B N   1 
ATOM   3732  C CA  . VAL B 2 152 ? 42.626  10.051  -83.531  1.00 73.38  ? 152 VAL B CA  1 
ATOM   3733  C C   . VAL B 2 152 ? 42.752  8.919   -82.517  1.00 74.81  ? 152 VAL B C   1 
ATOM   3734  O O   . VAL B 2 152 ? 42.032  8.880   -81.513  1.00 78.04  ? 152 VAL B O   1 
ATOM   3735  C CB  . VAL B 2 152 ? 41.872  9.595   -84.793  1.00 65.60  ? 152 VAL B CB  1 
ATOM   3736  C CG1 . VAL B 2 152 ? 40.583  8.883   -84.413  1.00 68.97  ? 152 VAL B CG1 1 
ATOM   3737  C CG2 . VAL B 2 152 ? 41.578  10.784  -85.692  1.00 56.24  ? 152 VAL B CG2 1 
ATOM   3738  N N   . ARG B 2 153 ? 43.667  7.977   -82.767  1.00 71.87  ? 153 ARG B N   1 
ATOM   3739  C CA  . ARG B 2 153 ? 43.877  6.885   -81.822  1.00 67.55  ? 153 ARG B CA  1 
ATOM   3740  C C   . ARG B 2 153 ? 44.420  7.402   -80.496  1.00 53.43  ? 153 ARG B C   1 
ATOM   3741  O O   . ARG B 2 153 ? 44.034  6.920   -79.425  1.00 76.69  ? 153 ARG B O   1 
ATOM   3742  C CB  . ARG B 2 153 ? 44.821  5.842   -82.422  1.00 61.60  ? 153 ARG B CB  1 
ATOM   3743  C CG  . ARG B 2 153 ? 44.252  5.130   -83.639  1.00 62.22  ? 153 ARG B CG  1 
ATOM   3744  C CD  . ARG B 2 153 ? 45.134  3.973   -84.089  1.00 66.65  ? 153 ARG B CD  1 
ATOM   3745  N NE  . ARG B 2 153 ? 45.694  4.199   -85.417  1.00 82.69  ? 153 ARG B NE  1 
ATOM   3746  C CZ  . ARG B 2 153 ? 46.951  4.551   -85.650  1.00 73.15  ? 153 ARG B CZ  1 
ATOM   3747  N NH1 . ARG B 2 153 ? 47.822  4.701   -84.665  1.00 83.94  ? 153 ARG B NH1 1 
ATOM   3748  N NH2 . ARG B 2 153 ? 47.346  4.755   -86.904  1.00 83.86  ? 153 ARG B NH2 1 
ATOM   3749  N N   . ASN B 2 154 ? 45.320  8.384   -80.549  1.00 67.11  ? 154 ASN B N   1 
ATOM   3750  C CA  . ASN B 2 154 ? 45.868  8.979   -79.338  1.00 66.90  ? 154 ASN B CA  1 
ATOM   3751  C C   . ASN B 2 154 ? 44.874  9.893   -78.632  1.00 72.58  ? 154 ASN B C   1 
ATOM   3752  O O   . ASN B 2 154 ? 45.144  10.320  -77.504  1.00 72.80  ? 154 ASN B O   1 
ATOM   3753  C CB  . ASN B 2 154 ? 47.145  9.754   -79.671  1.00 63.43  ? 154 ASN B CB  1 
ATOM   3754  C CG  . ASN B 2 154 ? 48.159  9.717   -78.547  1.00 84.96  ? 154 ASN B CG  1 
ATOM   3755  O OD1 . ASN B 2 154 ? 47.848  9.315   -77.426  1.00 98.23  ? 154 ASN B OD1 1 
ATOM   3756  N ND2 . ASN B 2 154 ? 49.381  10.143  -78.841  1.00 100.34 ? 154 ASN B ND2 1 
ATOM   3757  N N   . GLY B 2 155 ? 43.738  10.195  -79.257  1.00 68.74  ? 155 GLY B N   1 
ATOM   3758  C CA  . GLY B 2 155 ? 42.763  11.081  -78.654  1.00 60.82  ? 155 GLY B CA  1 
ATOM   3759  C C   . GLY B 2 155 ? 43.094  12.550  -78.753  1.00 69.83  ? 155 GLY B C   1 
ATOM   3760  O O   . GLY B 2 155 ? 42.519  13.354  -78.012  1.00 73.98  ? 155 GLY B O   1 
ATOM   3761  N N   . THR B 2 156 ? 44.003  12.930  -79.648  1.00 78.70  ? 156 THR B N   1 
ATOM   3762  C CA  . THR B 2 156 ? 44.470  14.305  -79.783  1.00 75.31  ? 156 THR B CA  1 
ATOM   3763  C C   . THR B 2 156 ? 44.320  14.787  -81.220  1.00 78.92  ? 156 THR B C   1 
ATOM   3764  O O   . THR B 2 156 ? 45.204  15.448  -81.773  1.00 71.23  ? 156 THR B O   1 
ATOM   3765  C CB  . THR B 2 156 ? 45.918  14.433  -79.315  1.00 70.38  ? 156 THR B CB  1 
ATOM   3766  O OG1 . THR B 2 156 ? 46.701  13.375  -79.881  1.00 80.51  ? 156 THR B OG1 1 
ATOM   3767  C CG2 . THR B 2 156 ? 45.990  14.354  -77.797  1.00 78.19  ? 156 THR B CG2 1 
ATOM   3768  N N   . TYR B 2 157 ? 43.188  14.461  -81.840  1.00 80.87  ? 157 TYR B N   1 
ATOM   3769  C CA  . TYR B 2 157 ? 42.924  14.869  -83.214  1.00 67.70  ? 157 TYR B CA  1 
ATOM   3770  C C   . TYR B 2 157 ? 42.811  16.387  -83.315  1.00 78.99  ? 157 TYR B C   1 
ATOM   3771  O O   . TYR B 2 157 ? 42.187  17.040  -82.473  1.00 66.55  ? 157 TYR B O   1 
ATOM   3772  C CB  . TYR B 2 157 ? 41.641  14.194  -83.707  1.00 68.66  ? 157 TYR B CB  1 
ATOM   3773  C CG  . TYR B 2 157 ? 41.086  14.708  -85.017  1.00 67.36  ? 157 TYR B CG  1 
ATOM   3774  C CD1 . TYR B 2 157 ? 41.605  14.280  -86.232  1.00 66.35  ? 157 TYR B CD1 1 
ATOM   3775  C CD2 . TYR B 2 157 ? 40.018  15.596  -85.038  1.00 74.32  ? 157 TYR B CD2 1 
ATOM   3776  C CE1 . TYR B 2 157 ? 41.088  14.738  -87.430  1.00 58.40  ? 157 TYR B CE1 1 
ATOM   3777  C CE2 . TYR B 2 157 ? 39.495  16.059  -86.229  1.00 63.08  ? 157 TYR B CE2 1 
ATOM   3778  C CZ  . TYR B 2 157 ? 40.033  15.628  -87.422  1.00 62.18  ? 157 TYR B CZ  1 
ATOM   3779  O OH  . TYR B 2 157 ? 39.514  16.088  -88.609  1.00 67.16  ? 157 TYR B OH  1 
ATOM   3780  N N   . ASP B 2 158 ? 43.427  16.949  -84.356  1.00 74.93  ? 158 ASP B N   1 
ATOM   3781  C CA  . ASP B 2 158 ? 43.468  18.399  -84.553  1.00 65.70  ? 158 ASP B CA  1 
ATOM   3782  C C   . ASP B 2 158 ? 42.303  18.795  -85.452  1.00 72.21  ? 158 ASP B C   1 
ATOM   3783  O O   . ASP B 2 158 ? 42.418  18.834  -86.678  1.00 77.38  ? 158 ASP B O   1 
ATOM   3784  C CB  . ASP B 2 158 ? 44.807  18.824  -85.143  1.00 65.67  ? 158 ASP B CB  1 
ATOM   3785  C CG  . ASP B 2 158 ? 45.028  20.324  -85.069  1.00 77.88  ? 158 ASP B CG  1 
ATOM   3786  O OD1 . ASP B 2 158 ? 44.213  21.018  -84.424  1.00 75.03  ? 158 ASP B OD1 1 
ATOM   3787  O OD2 . ASP B 2 158 ? 46.019  20.808  -85.658  1.00 74.22  ? 158 ASP B OD2 1 
ATOM   3788  N N   . TYR B 2 159 ? 41.162  19.089  -84.829  1.00 74.46  ? 159 TYR B N   1 
ATOM   3789  C CA  . TYR B 2 159 ? 39.982  19.493  -85.591  1.00 76.56  ? 159 TYR B CA  1 
ATOM   3790  C C   . TYR B 2 159 ? 40.175  20.790  -86.369  1.00 76.45  ? 159 TYR B C   1 
ATOM   3791  O O   . TYR B 2 159 ? 39.806  20.828  -87.556  1.00 68.26  ? 159 TYR B O   1 
ATOM   3792  C CB  . TYR B 2 159 ? 38.769  19.582  -84.659  1.00 78.98  ? 159 TYR B CB  1 
ATOM   3793  C CG  . TYR B 2 159 ? 37.547  20.172  -85.326  1.00 91.43  ? 159 TYR B CG  1 
ATOM   3794  C CD1 . TYR B 2 159 ? 36.720  19.387  -86.116  1.00 83.74  ? 159 TYR B CD1 1 
ATOM   3795  C CD2 . TYR B 2 159 ? 37.225  21.517  -85.171  1.00 93.73  ? 159 TYR B CD2 1 
ATOM   3796  C CE1 . TYR B 2 159 ? 35.607  19.920  -86.732  1.00 85.26  ? 159 TYR B CE1 1 
ATOM   3797  C CE2 . TYR B 2 159 ? 36.113  22.059  -85.784  1.00 98.12  ? 159 TYR B CE2 1 
ATOM   3798  C CZ  . TYR B 2 159 ? 35.308  21.256  -86.563  1.00 96.02  ? 159 TYR B CZ  1 
ATOM   3799  O OH  . TYR B 2 159 ? 34.199  21.793  -87.175  1.00 91.52  ? 159 TYR B OH  1 
ATOM   3800  N N   . PRO B 2 160 ? 40.707  21.877  -85.791  1.00 62.61  ? 160 PRO B N   1 
ATOM   3801  C CA  . PRO B 2 160 ? 40.832  23.118  -86.578  1.00 61.14  ? 160 PRO B CA  1 
ATOM   3802  C C   . PRO B 2 160 ? 41.713  22.978  -87.806  1.00 66.69  ? 160 PRO B C   1 
ATOM   3803  O O   . PRO B 2 160 ? 41.552  23.748  -88.761  1.00 74.00  ? 160 PRO B O   1 
ATOM   3804  C CB  . PRO B 2 160 ? 41.427  24.113  -85.571  1.00 52.27  ? 160 PRO B CB  1 
ATOM   3805  C CG  . PRO B 2 160 ? 41.044  23.580  -84.242  1.00 73.16  ? 160 PRO B CG  1 
ATOM   3806  C CD  . PRO B 2 160 ? 41.103  22.093  -84.386  1.00 60.18  ? 160 PRO B CD  1 
ATOM   3807  N N   . GLN B 2 161 ? 42.641  22.018  -87.809  1.00 70.51  ? 161 GLN B N   1 
ATOM   3808  C CA  . GLN B 2 161 ? 43.543  21.855  -88.945  1.00 71.45  ? 161 GLN B CA  1 
ATOM   3809  C C   . GLN B 2 161 ? 42.781  21.511  -90.219  1.00 64.34  ? 161 GLN B C   1 
ATOM   3810  O O   . GLN B 2 161 ? 43.110  22.009  -91.302  1.00 69.81  ? 161 GLN B O   1 
ATOM   3811  C CB  . GLN B 2 161 ? 44.581  20.775  -88.634  1.00 74.15  ? 161 GLN B CB  1 
ATOM   3812  C CG  . GLN B 2 161 ? 45.464  20.378  -89.812  1.00 66.43  ? 161 GLN B CG  1 
ATOM   3813  C CD  . GLN B 2 161 ? 46.427  21.476  -90.225  1.00 74.19  ? 161 GLN B CD  1 
ATOM   3814  O OE1 . GLN B 2 161 ? 46.801  22.326  -89.417  1.00 67.64  ? 161 GLN B OE1 1 
ATOM   3815  N NE2 . GLN B 2 161 ? 46.833  21.462  -91.491  1.00 64.16  ? 161 GLN B NE2 1 
ATOM   3816  N N   . TYR B 2 162 ? 41.760  20.663  -90.112  1.00 55.08  ? 162 TYR B N   1 
ATOM   3817  C CA  . TYR B 2 162 ? 41.066  20.129  -91.274  1.00 75.25  ? 162 TYR B CA  1 
ATOM   3818  C C   . TYR B 2 162 ? 39.636  20.631  -91.418  1.00 67.17  ? 162 TYR B C   1 
ATOM   3819  O O   . TYR B 2 162 ? 38.932  20.179  -92.327  1.00 74.82  ? 162 TYR B O   1 
ATOM   3820  C CB  . TYR B 2 162 ? 41.060  18.597  -91.220  1.00 75.70  ? 162 TYR B CB  1 
ATOM   3821  C CG  . TYR B 2 162 ? 42.414  17.981  -90.954  1.00 76.59  ? 162 TYR B CG  1 
ATOM   3822  C CD1 . TYR B 2 162 ? 43.294  17.714  -91.994  1.00 61.43  ? 162 TYR B CD1 1 
ATOM   3823  C CD2 . TYR B 2 162 ? 42.813  17.661  -89.660  1.00 66.94  ? 162 TYR B CD2 1 
ATOM   3824  C CE1 . TYR B 2 162 ? 44.534  17.150  -91.756  1.00 66.54  ? 162 TYR B CE1 1 
ATOM   3825  C CE2 . TYR B 2 162 ? 44.051  17.097  -89.412  1.00 60.51  ? 162 TYR B CE2 1 
ATOM   3826  C CZ  . TYR B 2 162 ? 44.907  16.844  -90.463  1.00 59.71  ? 162 TYR B CZ  1 
ATOM   3827  O OH  . TYR B 2 162 ? 46.137  16.283  -90.213  1.00 75.18  ? 162 TYR B OH  1 
ATOM   3828  N N   . SER B 2 163 ? 39.182  21.539  -90.549  1.00 59.10  ? 163 SER B N   1 
ATOM   3829  C CA  . SER B 2 163 ? 37.776  21.935  -90.561  1.00 63.41  ? 163 SER B CA  1 
ATOM   3830  C C   . SER B 2 163 ? 37.404  22.614  -91.874  1.00 72.10  ? 163 SER B C   1 
ATOM   3831  O O   . SER B 2 163 ? 36.351  22.332  -92.459  1.00 79.91  ? 163 SER B O   1 
ATOM   3832  C CB  . SER B 2 163 ? 37.475  22.855  -89.376  1.00 67.73  ? 163 SER B CB  1 
ATOM   3833  O OG  . SER B 2 163 ? 37.918  24.181  -89.629  1.00 89.84  ? 163 SER B OG  1 
ATOM   3834  N N   . GLU B 2 164 ? 38.257  23.527  -92.347  1.00 78.26  ? 164 GLU B N   1 
ATOM   3835  C CA  . GLU B 2 164 ? 37.958  24.258  -93.574  1.00 59.23  ? 164 GLU B CA  1 
ATOM   3836  C C   . GLU B 2 164 ? 37.923  23.330  -94.783  1.00 60.27  ? 164 GLU B C   1 
ATOM   3837  O O   . GLU B 2 164 ? 37.019  23.427  -95.623  1.00 81.62  ? 164 GLU B O   1 
ATOM   3838  C CB  . GLU B 2 164 ? 38.984  25.374  -93.774  1.00 83.00  ? 164 GLU B CB  1 
ATOM   3839  C CG  . GLU B 2 164 ? 38.424  26.772  -93.582  1.00 84.07  ? 164 GLU B CG  1 
ATOM   3840  C CD  . GLU B 2 164 ? 39.509  27.827  -93.499  1.00 104.24 ? 164 GLU B CD  1 
ATOM   3841  O OE1 . GLU B 2 164 ? 40.324  27.768  -92.554  1.00 112.43 ? 164 GLU B OE1 1 
ATOM   3842  O OE2 . GLU B 2 164 ? 39.554  28.709  -94.383  1.00 103.76 ? 164 GLU B OE2 1 
ATOM   3843  N N   . GLU B 2 165 ? 38.895  22.422  -94.889  1.00 68.27  ? 165 GLU B N   1 
ATOM   3844  C CA  . GLU B 2 165 ? 38.919  21.489  -96.012  1.00 73.24  ? 165 GLU B CA  1 
ATOM   3845  C C   . GLU B 2 165 ? 37.751  20.511  -95.947  1.00 80.14  ? 165 GLU B C   1 
ATOM   3846  O O   . GLU B 2 165 ? 37.178  20.151  -96.983  1.00 80.09  ? 165 GLU B O   1 
ATOM   3847  C CB  . GLU B 2 165 ? 40.245  20.731  -96.039  1.00 86.76  ? 165 GLU B CB  1 
ATOM   3848  C CG  . GLU B 2 165 ? 40.452  19.902  -97.296  1.00 103.28 ? 165 GLU B CG  1 
ATOM   3849  C CD  . GLU B 2 165 ? 41.650  18.980  -97.194  1.00 113.19 ? 165 GLU B CD  1 
ATOM   3850  O OE1 . GLU B 2 165 ? 42.235  18.891  -96.096  1.00 98.72  ? 165 GLU B OE1 1 
ATOM   3851  O OE2 . GLU B 2 165 ? 42.005  18.344  -98.210  1.00 93.42  ? 165 GLU B OE2 1 
ATOM   3852  N N   . ALA B 2 166 ? 37.397  20.059  -94.741  1.00 84.50  ? 166 ALA B N   1 
ATOM   3853  C CA  . ALA B 2 166 ? 36.277  19.133  -94.594  1.00 82.37  ? 166 ALA B CA  1 
ATOM   3854  C C   . ALA B 2 166 ? 34.962  19.785  -94.999  1.00 78.11  ? 166 ALA B C   1 
ATOM   3855  O O   . ALA B 2 166 ? 34.122  19.148  -95.645  1.00 73.63  ? 166 ALA B O   1 
ATOM   3856  C CB  . ALA B 2 166 ? 36.201  18.623  -93.156  1.00 66.40  ? 166 ALA B CB  1 
ATOM   3857  N N   . ARG B 2 167 ? 34.764  21.050  -94.622  1.00 78.98  ? 167 ARG B N   1 
ATOM   3858  C CA  . ARG B 2 167 ? 33.530  21.746  -94.975  1.00 72.89  ? 167 ARG B CA  1 
ATOM   3859  C C   . ARG B 2 167 ? 33.378  21.866  -96.487  1.00 75.91  ? 167 ARG B C   1 
ATOM   3860  O O   . ARG B 2 167 ? 32.278  21.694  -97.024  1.00 73.41  ? 167 ARG B O   1 
ATOM   3861  C CB  . ARG B 2 167 ? 33.501  23.123  -94.315  1.00 80.12  ? 167 ARG B CB  1 
ATOM   3862  C CG  . ARG B 2 167 ? 32.417  24.045  -94.837  1.00 74.81  ? 167 ARG B CG  1 
ATOM   3863  C CD  . ARG B 2 167 ? 32.529  25.416  -94.198  1.00 103.52 ? 167 ARG B CD  1 
ATOM   3864  N NE  . ARG B 2 167 ? 31.304  26.192  -94.346  1.00 107.13 ? 167 ARG B NE  1 
ATOM   3865  C CZ  . ARG B 2 167 ? 31.064  27.335  -93.718  1.00 116.30 ? 167 ARG B CZ  1 
ATOM   3866  N NH1 . ARG B 2 167 ? 31.942  27.860  -92.878  1.00 118.71 ? 167 ARG B NH1 1 
ATOM   3867  N NH2 . ARG B 2 167 ? 29.915  27.967  -93.938  1.00 117.32 ? 167 ARG B NH2 1 
ATOM   3868  N N   . LEU B 2 168 ? 34.476  22.155  -97.191  1.00 80.18  ? 168 LEU B N   1 
ATOM   3869  C CA  . LEU B 2 168 ? 34.422  22.241  -98.648  1.00 83.43  ? 168 LEU B CA  1 
ATOM   3870  C C   . LEU B 2 168 ? 34.028  20.908  -99.270  1.00 88.73  ? 168 LEU B C   1 
ATOM   3871  O O   . LEU B 2 168 ? 33.210  20.866  -100.196 1.00 89.06  ? 168 LEU B O   1 
ATOM   3872  C CB  . LEU B 2 168 ? 35.772  22.707  -99.191  1.00 90.83  ? 168 LEU B CB  1 
ATOM   3873  C CG  . LEU B 2 168 ? 35.952  24.215  -99.342  1.00 91.93  ? 168 LEU B CG  1 
ATOM   3874  C CD1 . LEU B 2 168 ? 37.426  24.563  -99.366  1.00 77.19  ? 168 LEU B CD1 1 
ATOM   3875  C CD2 . LEU B 2 168 ? 35.269  24.690  -100.613 1.00 85.87  ? 168 LEU B CD2 1 
ATOM   3876  N N   . LYS B 2 169 ? 34.598  19.806  -98.775  1.00 80.28  ? 169 LYS B N   1 
ATOM   3877  C CA  . LYS B 2 169 ? 34.278  18.495  -99.329  1.00 82.44  ? 169 LYS B CA  1 
ATOM   3878  C C   . LYS B 2 169 ? 32.832  18.104  -99.049  1.00 83.15  ? 169 LYS B C   1 
ATOM   3879  O O   . LYS B 2 169 ? 32.236  17.346  -99.822  1.00 95.43  ? 169 LYS B O   1 
ATOM   3880  C CB  . LYS B 2 169 ? 35.233  17.444  -98.767  1.00 72.14  ? 169 LYS B CB  1 
ATOM   3881  C CG  . LYS B 2 169 ? 35.188  16.097  -99.476  1.00 69.52  ? 169 LYS B CG  1 
ATOM   3882  C CD  . LYS B 2 169 ? 36.417  15.897  -100.349 1.00 95.27  ? 169 LYS B CD  1 
ATOM   3883  C CE  . LYS B 2 169 ? 37.693  16.128  -99.551  1.00 107.35 ? 169 LYS B CE  1 
ATOM   3884  N NZ  . LYS B 2 169 ? 38.913  15.686  -100.280 1.00 85.23  ? 169 LYS B NZ  1 
ATOM   3885  N N   . ARG B 2 170 ? 32.255  18.607  -97.955  1.00 70.33  ? 170 ARG B N   1 
ATOM   3886  C CA  . ARG B 2 170 ? 30.856  18.316  -97.654  1.00 79.00  ? 170 ARG B CA  1 
ATOM   3887  C C   . ARG B 2 170 ? 29.931  18.892  -98.720  1.00 85.42  ? 170 ARG B C   1 
ATOM   3888  O O   . ARG B 2 170 ? 29.080  18.184  -99.269  1.00 80.81  ? 170 ARG B O   1 
ATOM   3889  C CB  . ARG B 2 170 ? 30.493  18.868  -96.276  1.00 54.52  ? 170 ARG B CB  1 
ATOM   3890  C CG  . ARG B 2 170 ? 30.514  17.840  -95.158  1.00 59.21  ? 170 ARG B CG  1 
ATOM   3891  C CD  . ARG B 2 170 ? 30.038  18.454  -93.851  1.00 56.55  ? 170 ARG B CD  1 
ATOM   3892  N NE  . ARG B 2 170 ? 31.114  19.124  -93.130  1.00 72.65  ? 170 ARG B NE  1 
ATOM   3893  C CZ  . ARG B 2 170 ? 30.966  20.246  -92.439  1.00 83.08  ? 170 ARG B CZ  1 
ATOM   3894  N NH1 . ARG B 2 170 ? 29.812  20.892  -92.408  1.00 96.89  ? 170 ARG B NH1 1 
ATOM   3895  N NH2 . ARG B 2 170 ? 32.005  20.737  -91.769  1.00 94.36  ? 170 ARG B NH2 1 
ATOM   3896  N N   . GLU B 2 171 ? 30.090  20.181  -99.031  1.00 83.84  ? 171 GLU B N   1 
ATOM   3897  C CA  . GLU B 2 171 ? 29.204  20.826  -99.992  1.00 83.18  ? 171 GLU B CA  1 
ATOM   3898  C C   . GLU B 2 171 ? 29.486  20.398  -101.426 1.00 89.67  ? 171 GLU B C   1 
ATOM   3899  O O   . GLU B 2 171 ? 28.640  20.614  -102.300 1.00 101.32 ? 171 GLU B O   1 
ATOM   3900  C CB  . GLU B 2 171 ? 29.305  22.346  -99.863  1.00 83.66  ? 171 GLU B CB  1 
ATOM   3901  C CG  . GLU B 2 171 ? 30.714  22.893  -99.977  1.00 84.67  ? 171 GLU B CG  1 
ATOM   3902  C CD  . GLU B 2 171 ? 30.806  24.345  -99.551  1.00 91.24  ? 171 GLU B CD  1 
ATOM   3903  O OE1 . GLU B 2 171 ? 29.745  24.984  -99.382  1.00 73.90  ? 171 GLU B OE1 1 
ATOM   3904  O OE2 . GLU B 2 171 ? 31.938  24.845  -99.379  1.00 84.31  ? 171 GLU B OE2 1 
ATOM   3905  N N   . GLU B 2 172 ? 30.645  19.798  -101.692 1.00 91.98  ? 172 GLU B N   1 
ATOM   3906  C CA  . GLU B 2 172 ? 30.920  19.220  -103.001 1.00 95.18  ? 172 GLU B CA  1 
ATOM   3907  C C   . GLU B 2 172 ? 30.263  17.858  -103.187 1.00 88.84  ? 172 GLU B C   1 
ATOM   3908  O O   . GLU B 2 172 ? 30.493  17.206  -104.212 1.00 87.52  ? 172 GLU B O   1 
ATOM   3909  C CB  . GLU B 2 172 ? 32.430  19.105  -103.230 1.00 100.48 ? 172 GLU B CB  1 
ATOM   3910  C CG  . GLU B 2 172 ? 33.162  20.437  -103.278 1.00 105.94 ? 172 GLU B CG  1 
ATOM   3911  C CD  . GLU B 2 172 ? 34.547  20.322  -103.887 1.00 115.47 ? 172 GLU B CD  1 
ATOM   3912  O OE1 . GLU B 2 172 ? 34.640  20.118  -105.116 1.00 116.21 ? 172 GLU B OE1 1 
ATOM   3913  O OE2 . GLU B 2 172 ? 35.540  20.429  -103.136 1.00 101.70 ? 172 GLU B OE2 1 
ATOM   3914  N N   . ILE B 2 173 ? 29.462  17.415  -102.219 1.00 108.57 ? 173 ILE B N   1 
ATOM   3915  C CA  . ILE B 2 173 ? 28.750  16.146  -102.305 1.00 118.24 ? 173 ILE B CA  1 
ATOM   3916  C C   . ILE B 2 173 ? 27.250  16.409  -102.301 1.00 117.58 ? 173 ILE B C   1 
ATOM   3917  O O   . ILE B 2 173 ? 26.544  16.063  -103.255 1.00 134.08 ? 173 ILE B O   1 
ATOM   3918  C CB  . ILE B 2 173 ? 29.146  15.206  -101.153 1.00 104.14 ? 173 ILE B CB  1 
ATOM   3919  C CG1 . ILE B 2 173 ? 30.643  14.894  -101.213 1.00 95.98  ? 173 ILE B CG1 1 
ATOM   3920  C CG2 . ILE B 2 173 ? 28.321  13.929  -101.199 1.00 105.13 ? 173 ILE B CG2 1 
ATOM   3921  C CD1 . ILE B 2 173 ? 31.149  14.095  -100.034 1.00 71.92  ? 173 ILE B CD1 1 
ATOM   3922  N N   . SER B 2 174 ? 26.755  17.026  -101.233 1.00 107.91 ? 174 SER B N   1 
ATOM   3923  C CA  . SER B 2 174 ? 25.332  17.323  -101.109 1.00 126.35 ? 174 SER B CA  1 
ATOM   3924  C C   . SER B 2 174 ? 25.061  18.809  -101.316 1.00 117.35 ? 174 SER B C   1 
ATOM   3925  O O   . SER B 2 174 ? 25.259  19.618  -100.410 1.00 118.40 ? 174 SER B O   1 
ATOM   3926  C CB  . SER B 2 174 ? 24.809  16.877  -99.742  1.00 134.53 ? 174 SER B CB  1 
ATOM   3927  O OG  . SER B 2 174 ? 25.483  17.549  -98.692  1.00 117.80 ? 174 SER B OG  1 
ATOM   3928  N N   . ASP C 1 1   ? 33.245  39.190  -76.908  1.00 136.12 ? 8   ASP C N   1 
ATOM   3929  C CA  . ASP C 1 1   ? 33.875  38.748  -78.150  1.00 158.52 ? 8   ASP C CA  1 
ATOM   3930  C C   . ASP C 1 1   ? 34.207  37.242  -78.155  1.00 163.11 ? 8   ASP C C   1 
ATOM   3931  O O   . ASP C 1 1   ? 33.947  36.571  -79.154  1.00 155.56 ? 8   ASP C O   1 
ATOM   3932  C CB  . ASP C 1 1   ? 35.135  39.577  -78.433  1.00 151.08 ? 8   ASP C CB  1 
ATOM   3933  C CG  . ASP C 1 1   ? 35.252  39.979  -79.891  1.00 143.36 ? 8   ASP C CG  1 
ATOM   3934  O OD1 . ASP C 1 1   ? 34.988  39.131  -80.769  1.00 147.34 ? 8   ASP C OD1 1 
ATOM   3935  O OD2 . ASP C 1 1   ? 35.599  41.149  -80.159  1.00 133.53 ? 8   ASP C OD2 1 
ATOM   3936  N N   . PRO C 1 2   ? 34.779  36.703  -77.072  1.00 161.21 ? 9   PRO C N   1 
ATOM   3937  C CA  . PRO C 1 2   ? 34.942  35.247  -77.003  1.00 143.48 ? 9   PRO C CA  1 
ATOM   3938  C C   . PRO C 1 2   ? 33.597  34.543  -76.916  1.00 145.05 ? 9   PRO C C   1 
ATOM   3939  O O   . PRO C 1 2   ? 32.623  35.074  -76.376  1.00 152.43 ? 9   PRO C O   1 
ATOM   3940  C CB  . PRO C 1 2   ? 35.765  35.036  -75.726  1.00 142.63 ? 9   PRO C CB  1 
ATOM   3941  C CG  . PRO C 1 2   ? 35.495  36.237  -74.906  1.00 145.27 ? 9   PRO C CG  1 
ATOM   3942  C CD  . PRO C 1 2   ? 35.384  37.355  -75.894  1.00 156.56 ? 9   PRO C CD  1 
ATOM   3943  N N   . GLY C 1 3   ? 33.554  33.333  -77.467  1.00 125.16 ? 10  GLY C N   1 
ATOM   3944  C CA  . GLY C 1 3   ? 32.323  32.558  -77.446  1.00 111.91 ? 10  GLY C CA  1 
ATOM   3945  C C   . GLY C 1 3   ? 31.957  32.145  -76.032  1.00 122.62 ? 10  GLY C C   1 
ATOM   3946  O O   . GLY C 1 3   ? 32.792  31.618  -75.286  1.00 115.32 ? 10  GLY C O   1 
ATOM   3947  N N   . ASP C 1 4   ? 30.704  32.386  -75.655  1.00 116.35 ? 11  ASP C N   1 
ATOM   3948  C CA  . ASP C 1 4   ? 30.218  31.966  -74.349  1.00 114.96 ? 11  ASP C CA  1 
ATOM   3949  C C   . ASP C 1 4   ? 30.159  30.444  -74.271  1.00 108.37 ? 11  ASP C C   1 
ATOM   3950  O O   . ASP C 1 4   ? 29.990  29.754  -75.281  1.00 97.82  ? 11  ASP C O   1 
ATOM   3951  C CB  . ASP C 1 4   ? 28.839  32.563  -74.073  1.00 119.37 ? 11  ASP C CB  1 
ATOM   3952  C CG  . ASP C 1 4   ? 28.819  34.072  -74.215  1.00 117.39 ? 11  ASP C CG  1 
ATOM   3953  O OD1 . ASP C 1 4   ? 29.902  34.692  -74.146  1.00 113.39 ? 11  ASP C OD1 1 
ATOM   3954  O OD2 . ASP C 1 4   ? 27.719  34.639  -74.394  1.00 105.40 ? 11  ASP C OD2 1 
ATOM   3955  N N   . GLN C 1 5   ? 30.305  29.919  -73.056  1.00 105.76 ? 12  GLN C N   1 
ATOM   3956  C CA  . GLN C 1 5   ? 30.421  28.481  -72.862  1.00 95.96  ? 12  GLN C CA  1 
ATOM   3957  C C   . GLN C 1 5   ? 29.591  28.021  -71.672  1.00 89.66  ? 12  GLN C C   1 
ATOM   3958  O O   . GLN C 1 5   ? 29.416  28.751  -70.694  1.00 101.32 ? 12  GLN C O   1 
ATOM   3959  C CB  . GLN C 1 5   ? 31.880  28.061  -72.652  1.00 85.51  ? 12  GLN C CB  1 
ATOM   3960  C CG  . GLN C 1 5   ? 32.736  28.114  -73.901  1.00 85.68  ? 12  GLN C CG  1 
ATOM   3961  C CD  . GLN C 1 5   ? 34.215  28.081  -73.580  1.00 92.66  ? 12  GLN C CD  1 
ATOM   3962  O OE1 . GLN C 1 5   ? 35.000  27.439  -74.277  1.00 104.77 ? 12  GLN C OE1 1 
ATOM   3963  N NE2 . GLN C 1 5   ? 34.604  28.779  -72.519  1.00 114.69 ? 12  GLN C NE2 1 
ATOM   3964  N N   . ILE C 1 6   ? 29.094  26.790  -71.771  1.00 85.78  ? 13  ILE C N   1 
ATOM   3965  C CA  . ILE C 1 6   ? 28.465  26.080  -70.665  1.00 88.03  ? 13  ILE C CA  1 
ATOM   3966  C C   . ILE C 1 6   ? 29.122  24.709  -70.572  1.00 96.35  ? 13  ILE C C   1 
ATOM   3967  O O   . ILE C 1 6   ? 29.413  24.080  -71.596  1.00 83.46  ? 13  ILE C O   1 
ATOM   3968  C CB  . ILE C 1 6   ? 26.934  25.965  -70.849  1.00 73.30  ? 13  ILE C CB  1 
ATOM   3969  C CG1 . ILE C 1 6   ? 26.273  25.407  -69.587  1.00 84.06  ? 13  ILE C CG1 1 
ATOM   3970  C CG2 . ILE C 1 6   ? 26.581  25.126  -72.075  1.00 76.02  ? 13  ILE C CG2 1 
ATOM   3971  C CD1 . ILE C 1 6   ? 26.228  26.389  -68.438  1.00 98.09  ? 13  ILE C CD1 1 
ATOM   3972  N N   . CYS C 1 7   ? 29.386  24.258  -69.347  1.00 95.84  ? 14  CYS C N   1 
ATOM   3973  C CA  . CYS C 1 7   ? 30.171  23.052  -69.119  1.00 89.61  ? 14  CYS C CA  1 
ATOM   3974  C C   . CYS C 1 7   ? 29.437  22.109  -68.176  1.00 87.75  ? 14  CYS C C   1 
ATOM   3975  O O   . CYS C 1 7   ? 28.615  22.528  -67.358  1.00 81.00  ? 14  CYS C O   1 
ATOM   3976  C CB  . CYS C 1 7   ? 31.553  23.387  -68.540  1.00 88.22  ? 14  CYS C CB  1 
ATOM   3977  S SG  . CYS C 1 7   ? 32.651  24.318  -69.633  1.00 130.06 ? 14  CYS C SG  1 
ATOM   3978  N N   . ILE C 1 8   ? 29.757  20.820  -68.290  1.00 89.01  ? 15  ILE C N   1 
ATOM   3979  C CA  . ILE C 1 8   ? 29.203  19.782  -67.429  1.00 77.56  ? 15  ILE C CA  1 
ATOM   3980  C C   . ILE C 1 8   ? 30.336  19.194  -66.597  1.00 93.47  ? 15  ILE C C   1 
ATOM   3981  O O   . ILE C 1 8   ? 31.340  18.737  -67.152  1.00 92.86  ? 15  ILE C O   1 
ATOM   3982  C CB  . ILE C 1 8   ? 28.506  18.681  -68.249  1.00 91.46  ? 15  ILE C CB  1 
ATOM   3983  C CG1 . ILE C 1 8   ? 27.484  19.284  -69.227  1.00 87.39  ? 15  ILE C CG1 1 
ATOM   3984  C CG2 . ILE C 1 8   ? 27.924  17.613  -67.315  1.00 89.58  ? 15  ILE C CG2 1 
ATOM   3985  C CD1 . ILE C 1 8   ? 26.450  20.207  -68.587  1.00 91.18  ? 15  ILE C CD1 1 
ATOM   3986  N N   . GLY C 1 9   ? 30.171  19.191  -65.272  1.00 91.63  ? 16  GLY C N   1 
ATOM   3987  C CA  . GLY C 1 9   ? 31.197  18.673  -64.387  1.00 93.70  ? 16  GLY C CA  1 
ATOM   3988  C C   . GLY C 1 9   ? 30.591  18.076  -63.136  1.00 94.42  ? 16  GLY C C   1 
ATOM   3989  O O   . GLY C 1 9   ? 29.377  18.122  -62.925  1.00 90.05  ? 16  GLY C O   1 
ATOM   3990  N N   . TYR C 1 10  ? 31.459  17.511  -62.299  1.00 97.79  ? 17  TYR C N   1 
ATOM   3991  C CA  . TYR C 1 10  ? 31.036  16.837  -61.082  1.00 94.68  ? 17  TYR C CA  1 
ATOM   3992  C C   . TYR C 1 10  ? 31.909  17.257  -59.905  1.00 97.29  ? 17  TYR C C   1 
ATOM   3993  O O   . TYR C 1 10  ? 32.901  17.976  -60.054  1.00 97.94  ? 17  TYR C O   1 
ATOM   3994  C CB  . TYR C 1 10  ? 31.054  15.310  -61.253  1.00 95.22  ? 17  TYR C CB  1 
ATOM   3995  C CG  . TYR C 1 10  ? 32.343  14.738  -61.799  1.00 89.29  ? 17  TYR C CG  1 
ATOM   3996  C CD1 . TYR C 1 10  ? 32.560  14.641  -63.168  1.00 91.27  ? 17  TYR C CD1 1 
ATOM   3997  C CD2 . TYR C 1 10  ? 33.334  14.274  -60.945  1.00 84.21  ? 17  TYR C CD2 1 
ATOM   3998  C CE1 . TYR C 1 10  ? 33.734  14.111  -63.668  1.00 96.79  ? 17  TYR C CE1 1 
ATOM   3999  C CE2 . TYR C 1 10  ? 34.508  13.739  -61.437  1.00 78.48  ? 17  TYR C CE2 1 
ATOM   4000  C CZ  . TYR C 1 10  ? 34.704  13.662  -62.799  1.00 82.54  ? 17  TYR C CZ  1 
ATOM   4001  O OH  . TYR C 1 10  ? 35.871  13.133  -63.299  1.00 85.18  ? 17  TYR C OH  1 
ATOM   4002  N N   . HIS C 1 11  ? 31.509  16.791  -58.723  1.00 91.59  ? 18  HIS C N   1 
ATOM   4003  C CA  . HIS C 1 11  ? 32.135  17.199  -57.472  1.00 96.12  ? 18  HIS C CA  1 
ATOM   4004  C C   . HIS C 1 11  ? 33.506  16.554  -57.304  1.00 99.81  ? 18  HIS C C   1 
ATOM   4005  O O   . HIS C 1 11  ? 33.697  15.369  -57.591  1.00 96.87  ? 18  HIS C O   1 
ATOM   4006  C CB  . HIS C 1 11  ? 31.224  16.820  -56.296  1.00 89.50  ? 18  HIS C CB  1 
ATOM   4007  C CG  . HIS C 1 11  ? 31.613  17.426  -54.979  1.00 95.00  ? 18  HIS C CG  1 
ATOM   4008  N ND1 . HIS C 1 11  ? 32.894  17.840  -54.684  1.00 102.74 ? 18  HIS C ND1 1 
ATOM   4009  C CD2 . HIS C 1 11  ? 30.877  17.677  -53.870  1.00 107.13 ? 18  HIS C CD2 1 
ATOM   4010  C CE1 . HIS C 1 11  ? 32.931  18.322  -53.455  1.00 109.63 ? 18  HIS C CE1 1 
ATOM   4011  N NE2 . HIS C 1 11  ? 31.719  18.235  -52.938  1.00 113.93 ? 18  HIS C NE2 1 
ATOM   4012  N N   . ALA C 1 12  ? 34.466  17.356  -56.847  1.00 96.46  ? 19  ALA C N   1 
ATOM   4013  C CA  . ALA C 1 12  ? 35.736  16.868  -56.332  1.00 91.35  ? 19  ALA C CA  1 
ATOM   4014  C C   . ALA C 1 12  ? 36.073  17.639  -55.065  1.00 100.94 ? 19  ALA C C   1 
ATOM   4015  O O   . ALA C 1 12  ? 35.797  18.838  -54.971  1.00 102.86 ? 19  ALA C O   1 
ATOM   4016  C CB  . ALA C 1 12  ? 36.863  17.021  -57.360  1.00 87.55  ? 19  ALA C CB  1 
ATOM   4017  N N   . ASN C 1 13  ? 36.658  16.949  -54.089  1.00 115.40 ? 20  ASN C N   1 
ATOM   4018  C CA  . ASN C 1 13  ? 37.123  17.592  -52.864  1.00 103.30 ? 20  ASN C CA  1 
ATOM   4019  C C   . ASN C 1 13  ? 38.489  17.009  -52.509  1.00 106.94 ? 20  ASN C C   1 
ATOM   4020  O O   . ASN C 1 13  ? 39.107  16.294  -53.304  1.00 113.51 ? 20  ASN C O   1 
ATOM   4021  C CB  . ASN C 1 13  ? 36.091  17.450  -51.733  1.00 92.28  ? 20  ASN C CB  1 
ATOM   4022  C CG  . ASN C 1 13  ? 35.658  16.012  -51.497  1.00 100.56 ? 20  ASN C CG  1 
ATOM   4023  O OD1 . ASN C 1 13  ? 36.413  15.073  -51.734  1.00 98.45  ? 20  ASN C OD1 1 
ATOM   4024  N ND2 . ASN C 1 13  ? 34.431  15.838  -51.015  1.00 89.83  ? 20  ASN C ND2 1 
ATOM   4025  N N   . ASN C 1 14  ? 38.972  17.327  -51.307  1.00 115.50 ? 21  ASN C N   1 
ATOM   4026  C CA  . ASN C 1 14  ? 40.289  16.900  -50.853  1.00 122.64 ? 21  ASN C CA  1 
ATOM   4027  C C   . ASN C 1 14  ? 40.248  15.603  -50.053  1.00 117.41 ? 21  ASN C C   1 
ATOM   4028  O O   . ASN C 1 14  ? 41.151  15.355  -49.245  1.00 124.82 ? 21  ASN C O   1 
ATOM   4029  C CB  . ASN C 1 14  ? 40.942  18.006  -50.020  1.00 131.74 ? 21  ASN C CB  1 
ATOM   4030  C CG  . ASN C 1 14  ? 41.348  19.204  -50.857  1.00 133.00 ? 21  ASN C CG  1 
ATOM   4031  O OD1 . ASN C 1 14  ? 41.898  19.055  -51.948  1.00 120.29 ? 21  ASN C OD1 1 
ATOM   4032  N ND2 . ASN C 1 14  ? 41.074  20.402  -50.351  1.00 130.74 ? 21  ASN C ND2 1 
ATOM   4033  N N   . SER C 1 15  ? 39.228  14.774  -50.258  1.00 114.85 ? 22  SER C N   1 
ATOM   4034  C CA  . SER C 1 15  ? 39.125  13.522  -49.524  1.00 102.18 ? 22  SER C CA  1 
ATOM   4035  C C   . SER C 1 15  ? 40.141  12.510  -50.039  1.00 102.48 ? 22  SER C C   1 
ATOM   4036  O O   . SER C 1 15  ? 40.342  12.363  -51.248  1.00 104.69 ? 22  SER C O   1 
ATOM   4037  C CB  . SER C 1 15  ? 37.712  12.952  -49.639  1.00 107.35 ? 22  SER C CB  1 
ATOM   4038  O OG  . SER C 1 15  ? 37.580  11.759  -48.888  1.00 107.07 ? 22  SER C OG  1 
ATOM   4039  N N   . THR C 1 16  ? 40.790  11.816  -49.108  1.00 103.99 ? 23  THR C N   1 
ATOM   4040  C CA  . THR C 1 16  ? 41.697  10.725  -49.434  1.00 98.81  ? 23  THR C CA  1 
ATOM   4041  C C   . THR C 1 16  ? 41.088  9.358   -49.158  1.00 91.76  ? 23  THR C C   1 
ATOM   4042  O O   . THR C 1 16  ? 41.758  8.343   -49.375  1.00 89.39  ? 23  THR C O   1 
ATOM   4043  C CB  . THR C 1 16  ? 43.005  10.867  -48.649  1.00 96.89  ? 23  THR C CB  1 
ATOM   4044  O OG1 . THR C 1 16  ? 42.808  10.407  -47.307  1.00 94.14  ? 23  THR C OG1 1 
ATOM   4045  C CG2 . THR C 1 16  ? 43.448  12.320  -48.615  1.00 84.96  ? 23  THR C CG2 1 
ATOM   4046  N N   . GLU C 1 17  ? 39.844  9.311   -48.683  1.00 86.06  ? 24  GLU C N   1 
ATOM   4047  C CA  . GLU C 1 17  ? 39.214  8.044   -48.336  1.00 87.94  ? 24  GLU C CA  1 
ATOM   4048  C C   . GLU C 1 17  ? 39.127  7.143   -49.561  1.00 83.16  ? 24  GLU C C   1 
ATOM   4049  O O   . GLU C 1 17  ? 38.855  7.601   -50.674  1.00 91.91  ? 24  GLU C O   1 
ATOM   4050  C CB  . GLU C 1 17  ? 37.822  8.293   -47.747  1.00 82.94  ? 24  GLU C CB  1 
ATOM   4051  C CG  . GLU C 1 17  ? 37.115  7.043   -47.243  1.00 99.39  ? 24  GLU C CG  1 
ATOM   4052  C CD  . GLU C 1 17  ? 37.610  6.577   -45.881  1.00 111.77 ? 24  GLU C CD  1 
ATOM   4053  O OE1 . GLU C 1 17  ? 38.739  6.941   -45.485  1.00 105.74 ? 24  GLU C OE1 1 
ATOM   4054  O OE2 . GLU C 1 17  ? 36.861  5.845   -45.199  1.00 106.87 ? 24  GLU C OE2 1 
ATOM   4055  N N   . GLN C 1 18  ? 39.368  5.852   -49.352  1.00 81.16  ? 25  GLN C N   1 
ATOM   4056  C CA  . GLN C 1 18  ? 39.442  4.900   -50.447  1.00 79.47  ? 25  GLN C CA  1 
ATOM   4057  C C   . GLN C 1 18  ? 38.551  3.689   -50.205  1.00 81.00  ? 25  GLN C C   1 
ATOM   4058  O O   . GLN C 1 18  ? 38.284  3.300   -49.064  1.00 94.34  ? 25  GLN C O   1 
ATOM   4059  C CB  . GLN C 1 18  ? 40.864  4.429   -50.652  1.00 73.24  ? 25  GLN C CB  1 
ATOM   4060  C CG  . GLN C 1 18  ? 41.756  5.382   -51.368  1.00 95.76  ? 25  GLN C CG  1 
ATOM   4061  C CD  . GLN C 1 18  ? 43.044  4.702   -51.846  1.00 106.31 ? 25  GLN C CD  1 
ATOM   4062  O OE1 . GLN C 1 18  ? 43.029  3.674   -52.511  1.00 106.30 ? 25  GLN C OE1 1 
ATOM   4063  N NE2 . GLN C 1 18  ? 44.155  5.270   -51.483  1.00 99.39  ? 25  GLN C NE2 1 
ATOM   4064  N N   . VAL C 1 19  ? 38.077  3.112   -51.309  1.00 72.38  ? 26  VAL C N   1 
ATOM   4065  C CA  . VAL C 1 19  ? 37.283  1.894   -51.311  1.00 67.25  ? 26  VAL C CA  1 
ATOM   4066  C C   . VAL C 1 19  ? 37.878  0.949   -52.346  1.00 71.74  ? 26  VAL C C   1 
ATOM   4067  O O   . VAL C 1 19  ? 38.756  1.317   -53.130  1.00 81.77  ? 26  VAL C O   1 
ATOM   4068  C CB  . VAL C 1 19  ? 35.793  2.161   -51.614  1.00 81.12  ? 26  VAL C CB  1 
ATOM   4069  C CG1 . VAL C 1 19  ? 35.272  3.314   -50.758  1.00 75.68  ? 26  VAL C CG1 1 
ATOM   4070  C CG2 . VAL C 1 19  ? 35.603  2.453   -53.093  1.00 75.71  ? 26  VAL C CG2 1 
ATOM   4071  N N   . ASP C 1 20  ? 37.392  -0.286  -52.332  1.00 70.39  ? 27  ASP C N   1 
ATOM   4072  C CA  . ASP C 1 20  ? 37.725  -1.270  -53.345  1.00 78.25  ? 27  ASP C CA  1 
ATOM   4073  C C   . ASP C 1 20  ? 36.477  -1.645  -54.133  1.00 76.20  ? 27  ASP C C   1 
ATOM   4074  O O   . ASP C 1 20  ? 35.358  -1.623  -53.612  1.00 75.58  ? 27  ASP C O   1 
ATOM   4075  C CB  . ASP C 1 20  ? 38.337  -2.533  -52.727  1.00 80.20  ? 27  ASP C CB  1 
ATOM   4076  C CG  . ASP C 1 20  ? 39.730  -2.300  -52.173  1.00 105.09 ? 27  ASP C CG  1 
ATOM   4077  O OD1 . ASP C 1 20  ? 39.923  -2.476  -50.952  1.00 117.65 ? 27  ASP C OD1 1 
ATOM   4078  O OD2 . ASP C 1 20  ? 40.635  -1.953  -52.963  1.00 124.41 ? 27  ASP C OD2 1 
ATOM   4079  N N   . THR C 1 21  ? 36.681  -1.979  -55.401  1.00 68.27  ? 28  THR C N   1 
ATOM   4080  C CA  . THR C 1 21  ? 35.636  -2.507  -56.263  1.00 76.67  ? 28  THR C CA  1 
ATOM   4081  C C   . THR C 1 21  ? 36.030  -3.913  -56.706  1.00 77.89  ? 28  THR C C   1 
ATOM   4082  O O   . THR C 1 21  ? 37.124  -4.401  -56.404  1.00 80.75  ? 28  THR C O   1 
ATOM   4083  C CB  . THR C 1 21  ? 35.398  -1.595  -57.472  1.00 75.66  ? 28  THR C CB  1 
ATOM   4084  O OG1 . THR C 1 21  ? 36.532  -1.649  -58.347  1.00 89.30  ? 28  THR C OG1 1 
ATOM   4085  C CG2 . THR C 1 21  ? 35.180  -0.159  -57.027  1.00 63.50  ? 28  THR C CG2 1 
ATOM   4086  N N   . ILE C 1 22  ? 35.120  -4.572  -57.426  1.00 89.45  ? 29  ILE C N   1 
ATOM   4087  C CA  . ILE C 1 22  ? 35.403  -5.921  -57.901  1.00 80.61  ? 29  ILE C CA  1 
ATOM   4088  C C   . ILE C 1 22  ? 36.510  -5.906  -58.947  1.00 82.64  ? 29  ILE C C   1 
ATOM   4089  O O   . ILE C 1 22  ? 37.256  -6.882  -59.082  1.00 85.78  ? 29  ILE C O   1 
ATOM   4090  C CB  . ILE C 1 22  ? 34.118  -6.585  -58.436  1.00 81.70  ? 29  ILE C CB  1 
ATOM   4091  C CG1 . ILE C 1 22  ? 34.369  -8.062  -58.733  1.00 80.45  ? 29  ILE C CG1 1 
ATOM   4092  C CG2 . ILE C 1 22  ? 33.610  -5.870  -59.675  1.00 82.47  ? 29  ILE C CG2 1 
ATOM   4093  C CD1 . ILE C 1 22  ? 35.021  -8.794  -57.583  1.00 78.64  ? 29  ILE C CD1 1 
ATOM   4094  N N   . MET C 1 23  ? 36.645  -4.809  -59.697  1.00 81.08  ? 30  MET C N   1 
ATOM   4095  C CA  . MET C 1 23  ? 37.641  -4.719  -60.755  1.00 87.10  ? 30  MET C CA  1 
ATOM   4096  C C   . MET C 1 23  ? 38.777  -3.752  -60.456  1.00 82.80  ? 30  MET C C   1 
ATOM   4097  O O   . MET C 1 23  ? 39.846  -3.885  -61.056  1.00 82.71  ? 30  MET C O   1 
ATOM   4098  C CB  . MET C 1 23  ? 36.983  -4.307  -62.080  1.00 80.82  ? 30  MET C CB  1 
ATOM   4099  C CG  . MET C 1 23  ? 36.337  -5.467  -62.822  1.00 80.40  ? 30  MET C CG  1 
ATOM   4100  S SD  . MET C 1 23  ? 35.214  -4.968  -64.141  1.00 94.08  ? 30  MET C SD  1 
ATOM   4101  C CE  . MET C 1 23  ? 35.385  -3.186  -64.092  1.00 92.14  ? 30  MET C CE  1 
ATOM   4102  N N   . GLU C 1 24  ? 38.586  -2.794  -59.558  1.00 88.17  ? 31  GLU C N   1 
ATOM   4103  C CA  . GLU C 1 24  ? 39.629  -1.846  -59.203  1.00 83.12  ? 31  GLU C CA  1 
ATOM   4104  C C   . GLU C 1 24  ? 39.897  -1.914  -57.710  1.00 87.40  ? 31  GLU C C   1 
ATOM   4105  O O   . GLU C 1 24  ? 38.971  -1.791  -56.904  1.00 90.79  ? 31  GLU C O   1 
ATOM   4106  C CB  . GLU C 1 24  ? 39.232  -0.421  -59.601  1.00 95.17  ? 31  GLU C CB  1 
ATOM   4107  C CG  . GLU C 1 24  ? 39.619  -0.029  -61.013  1.00 107.43 ? 31  GLU C CG  1 
ATOM   4108  C CD  . GLU C 1 24  ? 39.114  1.346   -61.387  1.00 117.77 ? 31  GLU C CD  1 
ATOM   4109  O OE1 . GLU C 1 24  ? 37.880  1.539   -61.394  1.00 110.43 ? 31  GLU C OE1 1 
ATOM   4110  O OE2 . GLU C 1 24  ? 39.948  2.234   -61.662  1.00 110.64 ? 31  GLU C OE2 1 
ATOM   4111  N N   . LYS C 1 25  ? 41.157  -2.103  -57.344  1.00 90.32  ? 32  LYS C N   1 
ATOM   4112  C CA  . LYS C 1 25  ? 41.591  -1.967  -55.963  1.00 92.26  ? 32  LYS C CA  1 
ATOM   4113  C C   . LYS C 1 25  ? 42.126  -0.558  -55.752  1.00 89.68  ? 32  LYS C C   1 
ATOM   4114  O O   . LYS C 1 25  ? 42.650  0.062   -56.683  1.00 94.65  ? 32  LYS C O   1 
ATOM   4115  C CB  . LYS C 1 25  ? 42.670  -3.002  -55.636  1.00 81.51  ? 32  LYS C CB  1 
ATOM   4116  C CG  . LYS C 1 25  ? 42.216  -4.429  -55.847  1.00 106.58 ? 32  LYS C CG  1 
ATOM   4117  C CD  . LYS C 1 25  ? 43.021  -5.391  -55.003  1.00 93.80  ? 32  LYS C CD  1 
ATOM   4118  C CE  . LYS C 1 25  ? 42.304  -6.723  -54.947  1.00 115.65 ? 32  LYS C CE  1 
ATOM   4119  N NZ  . LYS C 1 25  ? 40.866  -6.513  -54.599  1.00 102.88 ? 32  LYS C NZ  1 
ATOM   4120  N N   . ASN C 1 26  ? 41.983  -0.057  -54.520  1.00 84.21  ? 33  ASN C N   1 
ATOM   4121  C CA  . ASN C 1 26  ? 42.562  1.221   -54.096  1.00 89.16  ? 33  ASN C CA  1 
ATOM   4122  C C   . ASN C 1 26  ? 42.029  2.377   -54.955  1.00 89.53  ? 33  ASN C C   1 
ATOM   4123  O O   . ASN C 1 26  ? 42.742  2.961   -55.766  1.00 103.60 ? 33  ASN C O   1 
ATOM   4124  C CB  . ASN C 1 26  ? 44.097  1.174   -54.146  1.00 101.27 ? 33  ASN C CB  1 
ATOM   4125  C CG  . ASN C 1 26  ? 44.728  0.400   -52.994  1.00 112.67 ? 33  ASN C CG  1 
ATOM   4126  O OD1 . ASN C 1 26  ? 44.047  -0.119  -52.110  1.00 106.73 ? 33  ASN C OD1 1 
ATOM   4127  N ND2 . ASN C 1 26  ? 46.058  0.334   -53.018  1.00 129.36 ? 33  ASN C ND2 1 
ATOM   4128  N N   . VAL C 1 27  ? 40.730  2.652   -54.799  1.00 90.17  ? 34  VAL C N   1 
ATOM   4129  C CA  . VAL C 1 27  ? 40.054  3.732   -55.524  1.00 75.01  ? 34  VAL C CA  1 
ATOM   4130  C C   . VAL C 1 27  ? 39.716  4.854   -54.549  1.00 72.53  ? 34  VAL C C   1 
ATOM   4131  O O   . VAL C 1 27  ? 39.059  4.616   -53.529  1.00 84.44  ? 34  VAL C O   1 
ATOM   4132  C CB  . VAL C 1 27  ? 38.786  3.237   -56.242  1.00 81.09  ? 34  VAL C CB  1 
ATOM   4133  C CG1 . VAL C 1 27  ? 37.893  4.419   -56.615  1.00 65.87  ? 34  VAL C CG1 1 
ATOM   4134  C CG2 . VAL C 1 27  ? 39.173  2.461   -57.481  1.00 78.31  ? 34  VAL C CG2 1 
ATOM   4135  N N   . THR C 1 28  ? 40.160  6.073   -54.866  1.00 74.94  ? 35  THR C N   1 
ATOM   4136  C CA  . THR C 1 28  ? 39.882  7.246   -54.039  1.00 85.62  ? 35  THR C CA  1 
ATOM   4137  C C   . THR C 1 28  ? 38.509  7.831   -54.369  1.00 78.53  ? 35  THR C C   1 
ATOM   4138  O O   . THR C 1 28  ? 38.164  8.004   -55.542  1.00 84.49  ? 35  THR C O   1 
ATOM   4139  C CB  . THR C 1 28  ? 40.962  8.311   -54.244  1.00 85.25  ? 35  THR C CB  1 
ATOM   4140  O OG1 . THR C 1 28  ? 42.255  7.696   -54.190  1.00 81.35  ? 35  THR C OG1 1 
ATOM   4141  C CG2 . THR C 1 28  ? 40.875  9.382   -53.160  1.00 65.68  ? 35  THR C CG2 1 
ATOM   4142  N N   . VAL C 1 29  ? 37.731  8.147   -53.331  1.00 79.07  ? 36  VAL C N   1 
ATOM   4143  C CA  . VAL C 1 29  ? 36.373  8.656   -53.483  1.00 77.76  ? 36  VAL C CA  1 
ATOM   4144  C C   . VAL C 1 29  ? 36.222  9.917   -52.639  1.00 80.24  ? 36  VAL C C   1 
ATOM   4145  O O   . VAL C 1 29  ? 37.045  10.218  -51.774  1.00 85.10  ? 36  VAL C O   1 
ATOM   4146  C CB  . VAL C 1 29  ? 35.304  7.615   -53.083  1.00 79.90  ? 36  VAL C CB  1 
ATOM   4147  C CG1 . VAL C 1 29  ? 35.623  6.252   -53.684  1.00 75.57  ? 36  VAL C CG1 1 
ATOM   4148  C CG2 . VAL C 1 29  ? 35.188  7.527   -51.569  1.00 83.12  ? 36  VAL C CG2 1 
ATOM   4149  N N   . THR C 1 30  ? 35.145  10.662  -52.909  1.00 82.80  ? 37  THR C N   1 
ATOM   4150  C CA  . THR C 1 30  ? 34.859  11.879  -52.158  1.00 87.42  ? 37  THR C CA  1 
ATOM   4151  C C   . THR C 1 30  ? 34.230  11.604  -50.798  1.00 82.18  ? 37  THR C C   1 
ATOM   4152  O O   . THR C 1 30  ? 34.340  12.447  -49.901  1.00 88.45  ? 37  THR C O   1 
ATOM   4153  C CB  . THR C 1 30  ? 33.936  12.801  -52.959  1.00 84.48  ? 37  THR C CB  1 
ATOM   4154  O OG1 . THR C 1 30  ? 32.644  12.195  -53.088  1.00 81.29  ? 37  THR C OG1 1 
ATOM   4155  C CG2 . THR C 1 30  ? 34.508  13.060  -54.345  1.00 82.98  ? 37  THR C CG2 1 
ATOM   4156  N N   . HIS C 1 31  ? 33.575  10.457  -50.624  1.00 89.32  ? 38  HIS C N   1 
ATOM   4157  C CA  . HIS C 1 31  ? 32.930  10.126  -49.361  1.00 89.34  ? 38  HIS C CA  1 
ATOM   4158  C C   . HIS C 1 31  ? 32.627  8.636   -49.341  1.00 89.70  ? 38  HIS C C   1 
ATOM   4159  O O   . HIS C 1 31  ? 32.265  8.058   -50.369  1.00 89.78  ? 38  HIS C O   1 
ATOM   4160  C CB  . HIS C 1 31  ? 31.644  10.935  -49.158  1.00 87.12  ? 38  HIS C CB  1 
ATOM   4161  C CG  . HIS C 1 31  ? 31.114  10.890  -47.759  1.00 103.00 ? 38  HIS C CG  1 
ATOM   4162  N ND1 . HIS C 1 31  ? 31.887  10.514  -46.682  1.00 103.60 ? 38  HIS C ND1 1 
ATOM   4163  C CD2 . HIS C 1 31  ? 29.887  11.175  -47.260  1.00 100.04 ? 38  HIS C CD2 1 
ATOM   4164  C CE1 . HIS C 1 31  ? 31.160  10.569  -45.580  1.00 104.35 ? 38  HIS C CE1 1 
ATOM   4165  N NE2 . HIS C 1 31  ? 29.943  10.967  -45.903  1.00 102.71 ? 38  HIS C NE2 1 
ATOM   4166  N N   . ALA C 1 32  ? 32.764  8.025   -48.166  1.00 100.70 ? 39  ALA C N   1 
ATOM   4167  C CA  . ALA C 1 32  ? 32.537  6.595   -48.021  1.00 90.16  ? 39  ALA C CA  1 
ATOM   4168  C C   . ALA C 1 32  ? 32.086  6.305   -46.597  1.00 90.75  ? 39  ALA C C   1 
ATOM   4169  O O   . ALA C 1 32  ? 32.278  7.115   -45.687  1.00 96.89  ? 39  ALA C O   1 
ATOM   4170  C CB  . ALA C 1 32  ? 33.794  5.793   -48.369  1.00 87.51  ? 39  ALA C CB  1 
ATOM   4171  N N   . GLN C 1 33  ? 31.476  5.136   -46.414  1.00 99.63  ? 40  GLN C N   1 
ATOM   4172  C CA  . GLN C 1 33  ? 30.910  4.746   -45.130  1.00 93.63  ? 40  GLN C CA  1 
ATOM   4173  C C   . GLN C 1 33  ? 31.322  3.321   -44.793  1.00 90.38  ? 40  GLN C C   1 
ATOM   4174  O O   . GLN C 1 33  ? 31.236  2.425   -45.642  1.00 81.65  ? 40  GLN C O   1 
ATOM   4175  C CB  . GLN C 1 33  ? 29.382  4.876   -45.146  1.00 88.74  ? 40  GLN C CB  1 
ATOM   4176  C CG  . GLN C 1 33  ? 28.715  4.597   -43.811  1.00 91.89  ? 40  GLN C CG  1 
ATOM   4177  C CD  . GLN C 1 33  ? 27.344  5.235   -43.710  1.00 110.12 ? 40  GLN C CD  1 
ATOM   4178  O OE1 . GLN C 1 33  ? 27.005  6.130   -44.485  1.00 109.96 ? 40  GLN C OE1 1 
ATOM   4179  N NE2 . GLN C 1 33  ? 26.547  4.777   -42.753  1.00 100.39 ? 40  GLN C NE2 1 
ATOM   4180  N N   . ASP C 1 34  ? 31.772  3.124   -43.556  1.00 92.53  ? 41  ASP C N   1 
ATOM   4181  C CA  . ASP C 1 34  ? 32.141  1.809   -43.056  1.00 86.04  ? 41  ASP C CA  1 
ATOM   4182  C C   . ASP C 1 34  ? 30.908  1.100   -42.508  1.00 85.43  ? 41  ASP C C   1 
ATOM   4183  O O   . ASP C 1 34  ? 30.041  1.723   -41.889  1.00 85.32  ? 41  ASP C O   1 
ATOM   4184  C CB  . ASP C 1 34  ? 33.207  1.938   -41.966  1.00 81.16  ? 41  ASP C CB  1 
ATOM   4185  C CG  . ASP C 1 34  ? 34.113  0.722   -41.879  1.00 102.21 ? 41  ASP C CG  1 
ATOM   4186  O OD1 . ASP C 1 34  ? 33.927  -0.220  -42.674  1.00 98.38  ? 41  ASP C OD1 1 
ATOM   4187  O OD2 . ASP C 1 34  ? 35.018  0.710   -41.017  1.00 105.72 ? 41  ASP C OD2 1 
ATOM   4188  N N   . ILE C 1 35  ? 30.834  -0.211  -42.741  1.00 80.62  ? 42  ILE C N   1 
ATOM   4189  C CA  . ILE C 1 35  ? 29.756  -1.040  -42.221  1.00 81.83  ? 42  ILE C CA  1 
ATOM   4190  C C   . ILE C 1 35  ? 30.271  -2.120  -41.278  1.00 85.95  ? 42  ILE C C   1 
ATOM   4191  O O   . ILE C 1 35  ? 29.539  -3.055  -40.955  1.00 86.48  ? 42  ILE C O   1 
ATOM   4192  C CB  . ILE C 1 35  ? 28.927  -1.667  -43.359  1.00 72.48  ? 42  ILE C CB  1 
ATOM   4193  C CG1 . ILE C 1 35  ? 29.793  -2.607  -44.200  1.00 59.61  ? 42  ILE C CG1 1 
ATOM   4194  C CG2 . ILE C 1 35  ? 28.304  -0.583  -44.226  1.00 72.34  ? 42  ILE C CG2 1 
ATOM   4195  C CD1 . ILE C 1 35  ? 29.013  -3.422  -45.210  1.00 60.71  ? 42  ILE C CD1 1 
ATOM   4196  N N   . LEU C 1 36  ? 31.516  -2.009  -40.828  1.00 86.82  ? 43  LEU C N   1 
ATOM   4197  C CA  . LEU C 1 36  ? 32.153  -3.023  -39.999  1.00 71.44  ? 43  LEU C CA  1 
ATOM   4198  C C   . LEU C 1 36  ? 32.403  -2.448  -38.612  1.00 78.44  ? 43  LEU C C   1 
ATOM   4199  O O   . LEU C 1 36  ? 33.047  -1.402  -38.479  1.00 84.60  ? 43  LEU C O   1 
ATOM   4200  C CB  . LEU C 1 36  ? 33.464  -3.491  -40.631  1.00 73.29  ? 43  LEU C CB  1 
ATOM   4201  C CG  . LEU C 1 36  ? 34.241  -4.575  -39.886  1.00 71.20  ? 43  LEU C CG  1 
ATOM   4202  C CD1 . LEU C 1 36  ? 33.426  -5.852  -39.806  1.00 63.91  ? 43  LEU C CD1 1 
ATOM   4203  C CD2 . LEU C 1 36  ? 35.581  -4.830  -40.556  1.00 60.12  ? 43  LEU C CD2 1 
ATOM   4204  N N   . GLU C 1 37  ? 31.896  -3.129  -37.587  1.00 74.79  ? 44  GLU C N   1 
ATOM   4205  C CA  . GLU C 1 37  ? 32.200  -2.759  -36.210  1.00 76.43  ? 44  GLU C CA  1 
ATOM   4206  C C   . GLU C 1 37  ? 33.573  -3.303  -35.842  1.00 79.32  ? 44  GLU C C   1 
ATOM   4207  O O   . GLU C 1 37  ? 33.820  -4.509  -35.954  1.00 76.97  ? 44  GLU C O   1 
ATOM   4208  C CB  . GLU C 1 37  ? 31.135  -3.288  -35.253  1.00 87.45  ? 44  GLU C CB  1 
ATOM   4209  C CG  . GLU C 1 37  ? 29.860  -2.456  -35.211  1.00 100.28 ? 44  GLU C CG  1 
ATOM   4210  C CD  . GLU C 1 37  ? 30.048  -1.092  -34.562  1.00 115.41 ? 44  GLU C CD  1 
ATOM   4211  O OE1 . GLU C 1 37  ? 29.098  -0.282  -34.618  1.00 123.04 ? 44  GLU C OE1 1 
ATOM   4212  O OE2 . GLU C 1 37  ? 31.134  -0.829  -33.995  1.00 118.40 ? 44  GLU C OE2 1 
ATOM   4213  N N   . LYS C 1 38  ? 34.464  -2.416  -35.399  1.00 83.96  ? 45  LYS C N   1 
ATOM   4214  C CA  . LYS C 1 38  ? 35.848  -2.788  -35.141  1.00 74.32  ? 45  LYS C CA  1 
ATOM   4215  C C   . LYS C 1 38  ? 36.334  -2.372  -33.757  1.00 77.26  ? 45  LYS C C   1 
ATOM   4216  O O   . LYS C 1 38  ? 37.523  -2.539  -33.461  1.00 72.10  ? 45  LYS C O   1 
ATOM   4217  C CB  . LYS C 1 38  ? 36.764  -2.186  -36.216  1.00 71.49  ? 45  LYS C CB  1 
ATOM   4218  C CG  . LYS C 1 38  ? 36.437  -2.638  -37.633  1.00 84.62  ? 45  LYS C CG  1 
ATOM   4219  C CD  . LYS C 1 38  ? 37.385  -2.017  -38.643  1.00 88.17  ? 45  LYS C CD  1 
ATOM   4220  C CE  . LYS C 1 38  ? 37.078  -0.542  -38.845  1.00 85.47  ? 45  LYS C CE  1 
ATOM   4221  N NZ  . LYS C 1 38  ? 38.300  0.236   -39.200  1.00 101.88 ? 45  LYS C NZ  1 
ATOM   4222  N N   . THR C 1 39  ? 35.460  -1.851  -32.901  1.00 79.99  ? 46  THR C N   1 
ATOM   4223  C CA  . THR C 1 39  ? 35.852  -1.349  -31.593  1.00 77.10  ? 46  THR C CA  1 
ATOM   4224  C C   . THR C 1 39  ? 35.059  -2.042  -30.491  1.00 93.60  ? 46  THR C C   1 
ATOM   4225  O O   . THR C 1 39  ? 34.013  -2.651  -30.734  1.00 101.63 ? 46  THR C O   1 
ATOM   4226  C CB  . THR C 1 39  ? 35.646  0.170   -31.496  1.00 78.13  ? 46  THR C CB  1 
ATOM   4227  O OG1 . THR C 1 39  ? 34.279  0.491   -31.780  1.00 104.91 ? 46  THR C OG1 1 
ATOM   4228  C CG2 . THR C 1 39  ? 36.549  0.897   -32.483  1.00 60.00  ? 46  THR C CG2 1 
ATOM   4229  N N   . HIS C 1 40  ? 35.576  -1.940  -29.266  1.00 85.82  ? 47  HIS C N   1 
ATOM   4230  C CA  . HIS C 1 40  ? 34.900  -2.450  -28.082  1.00 72.89  ? 47  HIS C CA  1 
ATOM   4231  C C   . HIS C 1 40  ? 35.307  -1.596  -26.890  1.00 89.92  ? 47  HIS C C   1 
ATOM   4232  O O   . HIS C 1 40  ? 36.448  -1.134  -26.816  1.00 84.32  ? 47  HIS C O   1 
ATOM   4233  C CB  . HIS C 1 40  ? 35.235  -3.926  -27.833  1.00 74.46  ? 47  HIS C CB  1 
ATOM   4234  C CG  . HIS C 1 40  ? 36.686  -4.183  -27.579  1.00 72.66  ? 47  HIS C CG  1 
ATOM   4235  N ND1 . HIS C 1 40  ? 37.264  -4.025  -26.338  1.00 77.90  ? 47  HIS C ND1 1 
ATOM   4236  C CD2 . HIS C 1 40  ? 37.678  -4.588  -28.407  1.00 80.19  ? 47  HIS C CD2 1 
ATOM   4237  C CE1 . HIS C 1 40  ? 38.549  -4.321  -26.411  1.00 83.95  ? 47  HIS C CE1 1 
ATOM   4238  N NE2 . HIS C 1 40  ? 38.826  -4.666  -27.656  1.00 76.80  ? 47  HIS C NE2 1 
ATOM   4239  N N   . ASN C 1 41  ? 34.370  -1.386  -25.960  1.00 89.17  ? 48  ASN C N   1 
ATOM   4240  C CA  . ASN C 1 41  ? 34.639  -0.493  -24.837  1.00 73.81  ? 48  ASN C CA  1 
ATOM   4241  C C   . ASN C 1 41  ? 35.571  -1.107  -23.800  1.00 87.91  ? 48  ASN C C   1 
ATOM   4242  O O   . ASN C 1 41  ? 36.006  -0.396  -22.890  1.00 101.82 ? 48  ASN C O   1 
ATOM   4243  C CB  . ASN C 1 41  ? 33.328  -0.058  -24.167  1.00 76.38  ? 48  ASN C CB  1 
ATOM   4244  C CG  . ASN C 1 41  ? 32.600  -1.202  -23.482  1.00 81.92  ? 48  ASN C CG  1 
ATOM   4245  O OD1 . ASN C 1 41  ? 33.033  -2.355  -23.519  1.00 99.11  ? 48  ASN C OD1 1 
ATOM   4246  N ND2 . ASN C 1 41  ? 31.482  -0.881  -22.843  1.00 83.47  ? 48  ASN C ND2 1 
ATOM   4247  N N   . GLY C 1 42  ? 35.877  -2.397  -23.912  1.00 81.41  ? 49  GLY C N   1 
ATOM   4248  C CA  . GLY C 1 42  ? 36.776  -3.045  -22.976  1.00 78.88  ? 49  GLY C CA  1 
ATOM   4249  C C   . GLY C 1 42  ? 36.251  -3.152  -21.563  1.00 85.03  ? 49  GLY C C   1 
ATOM   4250  O O   . GLY C 1 42  ? 37.038  -3.094  -20.613  1.00 85.01  ? 49  GLY C O   1 
ATOM   4251  N N   . LYS C 1 43  ? 34.940  -3.319  -21.397  1.00 87.67  ? 50  LYS C N   1 
ATOM   4252  C CA  . LYS C 1 43  ? 34.327  -3.462  -20.086  1.00 87.59  ? 50  LYS C CA  1 
ATOM   4253  C C   . LYS C 1 43  ? 33.245  -4.528  -20.143  1.00 90.67  ? 50  LYS C C   1 
ATOM   4254  O O   . LYS C 1 43  ? 32.781  -4.920  -21.218  1.00 96.15  ? 50  LYS C O   1 
ATOM   4255  C CB  . LYS C 1 43  ? 33.720  -2.144  -19.582  1.00 76.99  ? 50  LYS C CB  1 
ATOM   4256  C CG  . LYS C 1 43  ? 34.734  -1.152  -19.054  1.00 87.61  ? 50  LYS C CG  1 
ATOM   4257  C CD  . LYS C 1 43  ? 35.678  -1.809  -18.062  1.00 95.15  ? 50  LYS C CD  1 
ATOM   4258  C CE  . LYS C 1 43  ? 36.509  -0.774  -17.316  1.00 104.09 ? 50  LYS C CE  1 
ATOM   4259  N NZ  . LYS C 1 43  ? 37.771  -1.366  -16.777  1.00 110.23 ? 50  LYS C NZ  1 
ATOM   4260  N N   . LEU C 1 44  ? 32.856  -5.002  -18.962  1.00 74.64  ? 51  LEU C N   1 
ATOM   4261  C CA  . LEU C 1 44  ? 31.727  -5.909  -18.802  1.00 74.37  ? 51  LEU C CA  1 
ATOM   4262  C C   . LEU C 1 44  ? 30.509  -5.098  -18.373  1.00 82.93  ? 51  LEU C C   1 
ATOM   4263  O O   . LEU C 1 44  ? 30.532  -4.440  -17.325  1.00 94.57  ? 51  LEU C O   1 
ATOM   4264  C CB  . LEU C 1 44  ? 32.041  -7.001  -17.780  1.00 81.29  ? 51  LEU C CB  1 
ATOM   4265  C CG  . LEU C 1 44  ? 32.497  -8.360  -18.318  1.00 80.16  ? 51  LEU C CG  1 
ATOM   4266  C CD1 . LEU C 1 44  ? 33.733  -8.228  -19.195  1.00 73.41  ? 51  LEU C CD1 1 
ATOM   4267  C CD2 . LEU C 1 44  ? 32.762  -9.297  -17.160  1.00 67.25  ? 51  LEU C CD2 1 
ATOM   4268  N N   . CYS C 1 45  ? 29.452  -5.154  -19.176  1.00 80.19  ? 52  CYS C N   1 
ATOM   4269  C CA  . CYS C 1 45  ? 28.270  -4.326  -19.002  1.00 85.66  ? 52  CYS C CA  1 
ATOM   4270  C C   . CYS C 1 45  ? 27.049  -5.191  -18.723  1.00 75.03  ? 52  CYS C C   1 
ATOM   4271  O O   . CYS C 1 45  ? 27.082  -6.419  -18.835  1.00 70.04  ? 52  CYS C O   1 
ATOM   4272  C CB  . CYS C 1 45  ? 28.011  -3.468  -20.246  1.00 75.37  ? 52  CYS C CB  1 
ATOM   4273  S SG  . CYS C 1 45  ? 29.412  -2.496  -20.824  1.00 105.72 ? 52  CYS C SG  1 
ATOM   4274  N N   . ASP C 1 46  ? 25.959  -4.522  -18.357  1.00 75.07  ? 53  ASP C N   1 
ATOM   4275  C CA  . ASP C 1 46  ? 24.660  -5.173  -18.299  1.00 65.84  ? 53  ASP C CA  1 
ATOM   4276  C C   . ASP C 1 46  ? 24.216  -5.572  -19.701  1.00 75.57  ? 53  ASP C C   1 
ATOM   4277  O O   . ASP C 1 46  ? 24.580  -4.939  -20.696  1.00 80.78  ? 53  ASP C O   1 
ATOM   4278  C CB  . ASP C 1 46  ? 23.621  -4.245  -17.669  1.00 76.62  ? 53  ASP C CB  1 
ATOM   4279  C CG  . ASP C 1 46  ? 24.028  -3.758  -16.293  1.00 82.06  ? 53  ASP C CG  1 
ATOM   4280  O OD1 . ASP C 1 46  ? 25.050  -4.243  -15.764  1.00 94.91  ? 53  ASP C OD1 1 
ATOM   4281  O OD2 . ASP C 1 46  ? 23.324  -2.886  -15.740  1.00 87.46  ? 53  ASP C OD2 1 
ATOM   4282  N N   . LEU C 1 47  ? 23.429  -6.638  -19.778  1.00 79.99  ? 54  LEU C N   1 
ATOM   4283  C CA  . LEU C 1 47  ? 22.887  -7.119  -21.044  1.00 72.74  ? 54  LEU C CA  1 
ATOM   4284  C C   . LEU C 1 47  ? 21.377  -6.925  -21.015  1.00 70.46  ? 54  LEU C C   1 
ATOM   4285  O O   . LEU C 1 47  ? 20.676  -7.584  -20.239  1.00 79.06  ? 54  LEU C O   1 
ATOM   4286  C CB  . LEU C 1 47  ? 23.258  -8.579  -21.280  1.00 66.85  ? 54  LEU C CB  1 
ATOM   4287  C CG  . LEU C 1 47  ? 23.056  -9.061  -22.714  1.00 83.20  ? 54  LEU C CG  1 
ATOM   4288  C CD1 . LEU C 1 47  ? 23.781  -8.144  -23.685  1.00 74.93  ? 54  LEU C CD1 1 
ATOM   4289  C CD2 . LEU C 1 47  ? 23.546  -10.483 -22.857  1.00 87.71  ? 54  LEU C CD2 1 
ATOM   4290  N N   . ASN C 1 48  ? 20.885  -6.017  -21.862  1.00 73.06  ? 55  ASN C N   1 
ATOM   4291  C CA  . ASN C 1 48  ? 19.465  -5.665  -21.922  1.00 79.63  ? 55  ASN C CA  1 
ATOM   4292  C C   . ASN C 1 48  ? 18.947  -5.197  -20.563  1.00 73.85  ? 55  ASN C C   1 
ATOM   4293  O O   . ASN C 1 48  ? 17.824  -5.510  -20.163  1.00 83.79  ? 55  ASN C O   1 
ATOM   4294  C CB  . ASN C 1 48  ? 18.624  -6.828  -22.456  1.00 82.92  ? 55  ASN C CB  1 
ATOM   4295  C CG  . ASN C 1 48  ? 19.010  -7.226  -23.868  1.00 83.30  ? 55  ASN C CG  1 
ATOM   4296  O OD1 . ASN C 1 48  ? 19.671  -6.469  -24.579  1.00 82.56  ? 55  ASN C OD1 1 
ATOM   4297  N ND2 . ASN C 1 48  ? 18.594  -8.417  -24.282  1.00 92.36  ? 55  ASN C ND2 1 
ATOM   4298  N N   . GLY C 1 49  A 19.776  -4.437  -19.845  1.00 84.40  ? 55  GLY C N   1 
ATOM   4299  C CA  . GLY C 1 49  A 19.383  -3.841  -18.588  1.00 80.84  ? 55  GLY C CA  1 
ATOM   4300  C C   . GLY C 1 49  A 19.640  -4.678  -17.353  1.00 81.94  ? 55  GLY C C   1 
ATOM   4301  O O   . GLY C 1 49  A 19.423  -4.185  -16.239  1.00 86.65  ? 55  GLY C O   1 
ATOM   4302  N N   . VAL C 1 50  ? 20.102  -5.917  -17.506  1.00 83.82  ? 56  VAL C N   1 
ATOM   4303  C CA  . VAL C 1 50  ? 20.280  -6.840  -16.390  1.00 83.73  ? 56  VAL C CA  1 
ATOM   4304  C C   . VAL C 1 50  ? 21.770  -7.038  -16.150  1.00 81.57  ? 56  VAL C C   1 
ATOM   4305  O O   . VAL C 1 50  ? 22.514  -7.387  -17.075  1.00 80.38  ? 56  VAL C O   1 
ATOM   4306  C CB  . VAL C 1 50  ? 19.579  -8.183  -16.656  1.00 74.67  ? 56  VAL C CB  1 
ATOM   4307  C CG1 . VAL C 1 50  ? 19.729  -9.101  -15.457  1.00 75.26  ? 56  VAL C CG1 1 
ATOM   4308  C CG2 . VAL C 1 50  ? 18.110  -7.956  -16.978  1.00 65.95  ? 56  VAL C CG2 1 
ATOM   4309  N N   . LYS C 1 51  ? 22.201  -6.814  -14.912  1.00 74.79  ? 57  LYS C N   1 
ATOM   4310  C CA  . LYS C 1 51  ? 23.606  -6.973  -14.564  1.00 79.51  ? 57  LYS C CA  1 
ATOM   4311  C C   . LYS C 1 51  ? 23.988  -8.453  -14.544  1.00 79.96  ? 57  LYS C C   1 
ATOM   4312  O O   . LYS C 1 51  ? 23.184  -9.298  -14.137  1.00 86.73  ? 57  LYS C O   1 
ATOM   4313  C CB  . LYS C 1 51  ? 23.889  -6.332  -13.202  1.00 87.61  ? 57  LYS C CB  1 
ATOM   4314  C CG  . LYS C 1 51  ? 25.075  -6.925  -12.459  1.00 85.51  ? 57  LYS C CG  1 
ATOM   4315  C CD  . LYS C 1 51  ? 25.932  -5.863  -11.799  1.00 93.06  ? 57  LYS C CD  1 
ATOM   4316  C CE  . LYS C 1 51  ? 27.165  -6.487  -11.167  1.00 90.94  ? 57  LYS C CE  1 
ATOM   4317  N NZ  . LYS C 1 51  ? 27.509  -5.830  -9.878   1.00 79.47  ? 57  LYS C NZ  1 
ATOM   4318  N N   . PRO C 1 52  ? 25.194  -8.798  -14.986  1.00 82.89  ? 58  PRO C N   1 
ATOM   4319  C CA  . PRO C 1 52  ? 25.638  -10.194 -14.932  1.00 75.82  ? 58  PRO C CA  1 
ATOM   4320  C C   . PRO C 1 52  ? 26.007  -10.630 -13.521  1.00 72.06  ? 58  PRO C C   1 
ATOM   4321  O O   . PRO C 1 52  ? 26.243  -9.820  -12.623  1.00 69.38  ? 58  PRO C O   1 
ATOM   4322  C CB  . PRO C 1 52  ? 26.872  -10.203 -15.841  1.00 65.88  ? 58  PRO C CB  1 
ATOM   4323  C CG  . PRO C 1 52  ? 27.399  -8.811  -15.748  1.00 75.64  ? 58  PRO C CG  1 
ATOM   4324  C CD  . PRO C 1 52  ? 26.186  -7.929  -15.644  1.00 75.78  ? 58  PRO C CD  1 
ATOM   4325  N N   . LEU C 1 53  ? 26.058  -11.948 -13.342  1.00 72.32  ? 59  LEU C N   1 
ATOM   4326  C CA  . LEU C 1 53  ? 26.537  -12.552 -12.104  1.00 59.31  ? 59  LEU C CA  1 
ATOM   4327  C C   . LEU C 1 53  ? 28.028  -12.829 -12.260  1.00 65.31  ? 59  LEU C C   1 
ATOM   4328  O O   . LEU C 1 53  ? 28.428  -13.674 -13.068  1.00 67.01  ? 59  LEU C O   1 
ATOM   4329  C CB  . LEU C 1 53  ? 25.763  -13.830 -11.791  1.00 64.30  ? 59  LEU C CB  1 
ATOM   4330  C CG  . LEU C 1 53  ? 26.163  -14.596 -10.529  1.00 62.93  ? 59  LEU C CG  1 
ATOM   4331  C CD1 . LEU C 1 53  ? 25.924  -13.756 -9.285   1.00 52.23  ? 59  LEU C CD1 1 
ATOM   4332  C CD2 . LEU C 1 53  ? 25.409  -15.915 -10.444  1.00 62.47  ? 59  LEU C CD2 1 
ATOM   4333  N N   . ILE C 1 54  ? 28.850  -12.121 -11.492  1.00 67.60  ? 60  ILE C N   1 
ATOM   4334  C CA  . ILE C 1 54  ? 30.302  -12.180 -11.622  1.00 65.74  ? 60  ILE C CA  1 
ATOM   4335  C C   . ILE C 1 54  ? 30.855  -12.935 -10.422  1.00 72.61  ? 60  ILE C C   1 
ATOM   4336  O O   . ILE C 1 54  ? 30.805  -12.444 -9.287   1.00 74.63  ? 60  ILE C O   1 
ATOM   4337  C CB  . ILE C 1 54  ? 30.920  -10.779 -11.731  1.00 64.29  ? 60  ILE C CB  1 
ATOM   4338  C CG1 . ILE C 1 54  ? 30.473  -10.106 -13.032  1.00 78.71  ? 60  ILE C CG1 1 
ATOM   4339  C CG2 . ILE C 1 54  ? 32.440  -10.855 -11.647  1.00 61.96  ? 60  ILE C CG2 1 
ATOM   4340  C CD1 . ILE C 1 54  ? 30.845  -8.641  -13.128  1.00 63.88  ? 60  ILE C CD1 1 
ATOM   4341  N N   . LEU C 1 55  ? 31.390  -14.127 -10.675  1.00 75.37  ? 61  LEU C N   1 
ATOM   4342  C CA  . LEU C 1 55  ? 32.069  -14.917 -9.655   1.00 64.40  ? 61  LEU C CA  1 
ATOM   4343  C C   . LEU C 1 55  ? 33.560  -14.608 -9.740   1.00 79.18  ? 61  LEU C C   1 
ATOM   4344  O O   . LEU C 1 55  ? 34.217  -14.948 -10.729  1.00 84.57  ? 61  LEU C O   1 
ATOM   4345  C CB  . LEU C 1 55  ? 31.798  -16.405 -9.852   1.00 59.27  ? 61  LEU C CB  1 
ATOM   4346  C CG  . LEU C 1 55  ? 30.338  -16.843 -9.993   1.00 64.23  ? 61  LEU C CG  1 
ATOM   4347  C CD1 . LEU C 1 55  ? 30.248  -18.355 -10.148  1.00 53.45  ? 61  LEU C CD1 1 
ATOM   4348  C CD2 . LEU C 1 55  ? 29.501  -16.373 -8.812   1.00 59.58  ? 61  LEU C CD2 1 
ATOM   4349  N N   . LYS C 1 56  ? 34.093  -13.963 -8.702   1.00 78.59  ? 62  LYS C N   1 
ATOM   4350  C CA  . LYS C 1 56  ? 35.455  -13.445 -8.760   1.00 89.42  ? 62  LYS C CA  1 
ATOM   4351  C C   . LYS C 1 56  ? 36.485  -14.561 -8.632   1.00 91.37  ? 62  LYS C C   1 
ATOM   4352  O O   . LYS C 1 56  ? 37.272  -14.807 -9.552   1.00 102.35 ? 62  LYS C O   1 
ATOM   4353  C CB  . LYS C 1 56  ? 35.659  -12.403 -7.657   1.00 91.36  ? 62  LYS C CB  1 
ATOM   4354  C CG  . LYS C 1 56  ? 34.681  -11.240 -7.703   1.00 82.61  ? 62  LYS C CG  1 
ATOM   4355  C CD  . LYS C 1 56  ? 35.249  -10.068 -8.486   1.00 92.64  ? 62  LYS C CD  1 
ATOM   4356  C CE  . LYS C 1 56  ? 34.473  -8.793  -8.198   1.00 82.65  ? 62  LYS C CE  1 
ATOM   4357  N NZ  . LYS C 1 56  ? 35.346  -7.589  -8.278   1.00 98.95  ? 62  LYS C NZ  1 
ATOM   4358  N N   . ASP C 1 57  ? 36.484  -15.252 -7.495   1.00 82.13  ? 63  ASP C N   1 
ATOM   4359  C CA  . ASP C 1 57  ? 37.474  -16.280 -7.202   1.00 80.88  ? 63  ASP C CA  1 
ATOM   4360  C C   . ASP C 1 57  ? 36.837  -17.648 -7.004   1.00 92.99  ? 63  ASP C C   1 
ATOM   4361  O O   . ASP C 1 57  ? 37.532  -18.597 -6.624   1.00 93.86  ? 63  ASP C O   1 
ATOM   4362  C CB  . ASP C 1 57  ? 38.286  -15.883 -5.966   1.00 97.60  ? 63  ASP C CB  1 
ATOM   4363  C CG  . ASP C 1 57  ? 37.418  -15.677 -4.735   1.00 115.71 ? 63  ASP C CG  1 
ATOM   4364  O OD1 . ASP C 1 57  ? 37.978  -15.589 -3.620   1.00 121.47 ? 63  ASP C OD1 1 
ATOM   4365  O OD2 . ASP C 1 57  ? 36.178  -15.619 -4.878   1.00 117.14 ? 63  ASP C OD2 1 
ATOM   4366  N N   . CYS C 1 58  ? 35.538  -17.774 -7.265   1.00 76.63  ? 64  CYS C N   1 
ATOM   4367  C CA  . CYS C 1 58  ? 34.775  -18.979 -6.984   1.00 70.93  ? 64  CYS C CA  1 
ATOM   4368  C C   . CYS C 1 58  ? 34.198  -19.539 -8.276   1.00 65.92  ? 64  CYS C C   1 
ATOM   4369  O O   . CYS C 1 58  ? 33.798  -18.784 -9.168   1.00 87.25  ? 64  CYS C O   1 
ATOM   4370  C CB  . CYS C 1 58  ? 33.641  -18.680 -5.997   1.00 75.66  ? 64  CYS C CB  1 
ATOM   4371  S SG  . CYS C 1 58  ? 33.111  -20.076 -4.979   1.00 118.27 ? 64  CYS C SG  1 
ATOM   4372  N N   . SER C 1 59  ? 34.163  -20.864 -8.376   1.00 69.78  ? 65  SER C N   1 
ATOM   4373  C CA  . SER C 1 59  ? 33.449  -21.503 -9.467   1.00 65.36  ? 65  SER C CA  1 
ATOM   4374  C C   . SER C 1 59  ? 31.969  -21.625 -9.114   1.00 62.00  ? 65  SER C C   1 
ATOM   4375  O O   . SER C 1 59  ? 31.546  -21.349 -7.987   1.00 67.96  ? 65  SER C O   1 
ATOM   4376  C CB  . SER C 1 59  ? 34.042  -22.876 -9.777   1.00 66.17  ? 65  SER C CB  1 
ATOM   4377  O OG  . SER C 1 59  ? 33.588  -23.848 -8.851   1.00 71.36  ? 65  SER C OG  1 
ATOM   4378  N N   . VAL C 1 60  ? 31.171  -22.040 -10.100  1.00 56.26  ? 66  VAL C N   1 
ATOM   4379  C CA  . VAL C 1 60  ? 29.735  -22.192 -9.875   1.00 59.00  ? 66  VAL C CA  1 
ATOM   4380  C C   . VAL C 1 60  ? 29.467  -23.262 -8.825   1.00 57.35  ? 66  VAL C C   1 
ATOM   4381  O O   . VAL C 1 60  ? 28.624  -23.083 -7.937   1.00 65.02  ? 66  VAL C O   1 
ATOM   4382  C CB  . VAL C 1 60  ? 29.016  -22.500 -11.202  1.00 57.48  ? 66  VAL C CB  1 
ATOM   4383  C CG1 . VAL C 1 60  ? 27.550  -22.820 -10.952  1.00 44.55  ? 66  VAL C CG1 1 
ATOM   4384  C CG2 . VAL C 1 60  ? 29.152  -21.326 -12.159  1.00 63.72  ? 66  VAL C CG2 1 
ATOM   4385  N N   . ALA C 1 61  ? 30.184  -24.387 -8.903   1.00 64.07  ? 67  ALA C N   1 
ATOM   4386  C CA  . ALA C 1 61  ? 29.969  -25.472 -7.948   1.00 61.09  ? 67  ALA C CA  1 
ATOM   4387  C C   . ALA C 1 61  ? 30.303  -25.039 -6.525   1.00 70.32  ? 67  ALA C C   1 
ATOM   4388  O O   . ALA C 1 61  ? 29.560  -25.344 -5.585   1.00 67.53  ? 67  ALA C O   1 
ATOM   4389  C CB  . ALA C 1 61  ? 30.797  -26.693 -8.346   1.00 60.38  ? 67  ALA C CB  1 
ATOM   4390  N N   . GLY C 1 62  ? 31.420  -24.331 -6.344   1.00 68.02  ? 68  GLY C N   1 
ATOM   4391  C CA  . GLY C 1 62  ? 31.758  -23.834 -5.020   1.00 69.23  ? 68  GLY C CA  1 
ATOM   4392  C C   . GLY C 1 62  ? 30.800  -22.765 -4.534   1.00 68.94  ? 68  GLY C C   1 
ATOM   4393  O O   . GLY C 1 62  ? 30.470  -22.706 -3.346   1.00 61.10  ? 68  GLY C O   1 
ATOM   4394  N N   . TRP C 1 63  ? 30.351  -21.897 -5.444   1.00 58.04  ? 69  TRP C N   1 
ATOM   4395  C CA  . TRP C 1 63  ? 29.390  -20.862 -5.080   1.00 58.46  ? 69  TRP C CA  1 
ATOM   4396  C C   . TRP C 1 63  ? 28.066  -21.470 -4.631   1.00 54.84  ? 69  TRP C C   1 
ATOM   4397  O O   . TRP C 1 63  ? 27.465  -21.014 -3.651   1.00 55.04  ? 69  TRP C O   1 
ATOM   4398  C CB  . TRP C 1 63  ? 29.191  -19.916 -6.265   1.00 68.08  ? 69  TRP C CB  1 
ATOM   4399  C CG  . TRP C 1 63  ? 27.966  -19.067 -6.198   1.00 63.52  ? 69  TRP C CG  1 
ATOM   4400  C CD1 . TRP C 1 63  ? 27.743  -18.011 -5.365   1.00 63.90  ? 69  TRP C CD1 1 
ATOM   4401  C CD2 . TRP C 1 63  ? 26.801  -19.182 -7.023   1.00 66.84  ? 69  TRP C CD2 1 
ATOM   4402  N NE1 . TRP C 1 63  ? 26.504  -17.470 -5.609   1.00 59.20  ? 69  TRP C NE1 1 
ATOM   4403  C CE2 . TRP C 1 63  ? 25.905  -18.171 -6.623   1.00 58.40  ? 69  TRP C CE2 1 
ATOM   4404  C CE3 . TRP C 1 63  ? 26.426  -20.046 -8.056   1.00 65.34  ? 69  TRP C CE3 1 
ATOM   4405  C CZ2 . TRP C 1 63  ? 24.658  -18.000 -7.220   1.00 58.01  ? 69  TRP C CZ2 1 
ATOM   4406  C CZ3 . TRP C 1 63  ? 25.188  -19.876 -8.648   1.00 73.19  ? 69  TRP C CZ3 1 
ATOM   4407  C CH2 . TRP C 1 63  ? 24.318  -18.861 -8.228   1.00 74.72  ? 69  TRP C CH2 1 
ATOM   4408  N N   . LEU C 1 64  ? 27.598  -22.504 -5.333   1.00 55.25  ? 70  LEU C N   1 
ATOM   4409  C CA  . LEU C 1 64  ? 26.338  -23.146 -4.968   1.00 55.65  ? 70  LEU C CA  1 
ATOM   4410  C C   . LEU C 1 64  ? 26.447  -23.878 -3.636   1.00 60.61  ? 70  LEU C C   1 
ATOM   4411  O O   . LEU C 1 64  ? 25.610  -23.694 -2.745   1.00 60.50  ? 70  LEU C O   1 
ATOM   4412  C CB  . LEU C 1 64  ? 25.905  -24.111 -6.072   1.00 49.81  ? 70  LEU C CB  1 
ATOM   4413  C CG  . LEU C 1 64  ? 25.290  -23.494 -7.325   1.00 54.12  ? 70  LEU C CG  1 
ATOM   4414  C CD1 . LEU C 1 64  ? 25.078  -24.561 -8.384   1.00 44.27  ? 70  LEU C CD1 1 
ATOM   4415  C CD2 . LEU C 1 64  ? 23.977  -22.817 -6.977   1.00 47.53  ? 70  LEU C CD2 1 
ATOM   4416  N N   . LEU C 1 65  ? 27.479  -24.711 -3.478   1.00 58.19  ? 71  LEU C N   1 
ATOM   4417  C CA  . LEU C 1 65  ? 27.590  -25.542 -2.285   1.00 49.99  ? 71  LEU C CA  1 
ATOM   4418  C C   . LEU C 1 65  ? 28.014  -24.750 -1.057   1.00 54.61  ? 71  LEU C C   1 
ATOM   4419  O O   . LEU C 1 65  ? 27.878  -25.251 0.065    1.00 54.22  ? 71  LEU C O   1 
ATOM   4420  C CB  . LEU C 1 65  ? 28.572  -26.686 -2.538   1.00 44.43  ? 71  LEU C CB  1 
ATOM   4421  C CG  . LEU C 1 65  ? 28.108  -27.733 -3.551   1.00 49.18  ? 71  LEU C CG  1 
ATOM   4422  C CD1 . LEU C 1 65  ? 29.254  -28.642 -3.959   1.00 54.33  ? 71  LEU C CD1 1 
ATOM   4423  C CD2 . LEU C 1 65  ? 26.960  -28.547 -2.977   1.00 49.69  ? 71  LEU C CD2 1 
ATOM   4424  N N   . GLY C 1 66  ? 28.519  -23.533 -1.236   1.00 53.54  ? 72  GLY C N   1 
ATOM   4425  C CA  . GLY C 1 66  ? 28.926  -22.722 -0.107   1.00 51.15  ? 72  GLY C CA  1 
ATOM   4426  C C   . GLY C 1 66  ? 30.331  -23.025 0.366    1.00 57.05  ? 72  GLY C C   1 
ATOM   4427  O O   . GLY C 1 66  ? 30.548  -23.299 1.550    1.00 59.54  ? 72  GLY C O   1 
ATOM   4428  N N   . ASN C 1 67  ? 31.289  -22.989 -0.552   1.00 51.44  ? 73  ASN C N   1 
ATOM   4429  C CA  . ASN C 1 67  ? 32.687  -23.178 -0.196   1.00 46.44  ? 73  ASN C CA  1 
ATOM   4430  C C   . ASN C 1 67  ? 33.091  -22.092 0.797    1.00 62.69  ? 73  ASN C C   1 
ATOM   4431  O O   . ASN C 1 67  ? 32.962  -20.900 0.482    1.00 58.52  ? 73  ASN C O   1 
ATOM   4432  C CB  . ASN C 1 67  ? 33.557  -23.125 -1.453   1.00 58.43  ? 73  ASN C CB  1 
ATOM   4433  C CG  . ASN C 1 67  ? 35.002  -23.532 -1.198   1.00 56.03  ? 73  ASN C CG  1 
ATOM   4434  O OD1 . ASN C 1 67  ? 35.611  -23.133 -0.206   1.00 72.27  ? 73  ASN C OD1 1 
ATOM   4435  N ND2 . ASN C 1 67  ? 35.560  -24.325 -2.108   1.00 62.96  ? 73  ASN C ND2 1 
ATOM   4436  N N   . PRO C 1 68  ? 33.567  -22.448 1.993    1.00 59.98  ? 74  PRO C N   1 
ATOM   4437  C CA  . PRO C 1 68  ? 33.840  -21.419 3.009    1.00 53.44  ? 74  PRO C CA  1 
ATOM   4438  C C   . PRO C 1 68  ? 34.925  -20.440 2.610    1.00 67.66  ? 74  PRO C C   1 
ATOM   4439  O O   . PRO C 1 68  ? 34.959  -19.324 3.147    1.00 73.92  ? 74  PRO C O   1 
ATOM   4440  C CB  . PRO C 1 68  ? 34.250  -22.239 4.240    1.00 42.37  ? 74  PRO C CB  1 
ATOM   4441  C CG  . PRO C 1 68  ? 34.748  -23.531 3.679    1.00 63.31  ? 74  PRO C CG  1 
ATOM   4442  C CD  . PRO C 1 68  ? 33.899  -23.801 2.472    1.00 58.36  ? 74  PRO C CD  1 
ATOM   4443  N N   . MET C 1 69  ? 35.807  -20.810 1.684    1.00 72.76  ? 75  MET C N   1 
ATOM   4444  C CA  . MET C 1 69  ? 36.863  -19.918 1.227    1.00 68.57  ? 75  MET C CA  1 
ATOM   4445  C C   . MET C 1 69  ? 36.399  -18.962 0.138    1.00 73.20  ? 75  MET C C   1 
ATOM   4446  O O   . MET C 1 69  ? 37.184  -18.106 -0.285   1.00 89.86  ? 75  MET C O   1 
ATOM   4447  C CB  . MET C 1 69  ? 38.060  -20.740 0.739    1.00 70.59  ? 75  MET C CB  1 
ATOM   4448  C CG  . MET C 1 69  ? 38.647  -21.634 1.822    1.00 88.65  ? 75  MET C CG  1 
ATOM   4449  S SD  . MET C 1 69  ? 39.042  -23.303 1.263    1.00 97.37  ? 75  MET C SD  1 
ATOM   4450  C CE  . MET C 1 69  ? 40.670  -23.059 0.561    1.00 63.50  ? 75  MET C CE  1 
ATOM   4451  N N   . CYS C 1 70  ? 35.154  -19.079 -0.319   1.00 74.46  ? 76  CYS C N   1 
ATOM   4452  C CA  . CYS C 1 70  ? 34.599  -18.170 -1.315   1.00 77.25  ? 76  CYS C CA  1 
ATOM   4453  C C   . CYS C 1 70  ? 33.916  -17.016 -0.592   1.00 92.70  ? 76  CYS C C   1 
ATOM   4454  O O   . CYS C 1 70  ? 32.870  -17.200 0.040    1.00 99.58  ? 76  CYS C O   1 
ATOM   4455  C CB  . CYS C 1 70  ? 33.621  -18.896 -2.236   1.00 60.14  ? 76  CYS C CB  1 
ATOM   4456  S SG  . CYS C 1 70  ? 34.393  -20.036 -3.404   1.00 112.84 ? 76  CYS C SG  1 
ATOM   4457  N N   . ASP C 1 71  ? 34.511  -15.827 -0.682   1.00 103.55 ? 77  ASP C N   1 
ATOM   4458  C CA  . ASP C 1 71  ? 33.899  -14.624 -0.134   1.00 112.59 ? 77  ASP C CA  1 
ATOM   4459  C C   . ASP C 1 71  ? 32.610  -14.320 -0.886   1.00 115.78 ? 77  ASP C C   1 
ATOM   4460  O O   . ASP C 1 71  ? 32.641  -13.906 -2.049   1.00 127.87 ? 77  ASP C O   1 
ATOM   4461  C CB  . ASP C 1 71  ? 34.879  -13.450 -0.203   1.00 106.34 ? 77  ASP C CB  1 
ATOM   4462  C CG  . ASP C 1 71  ? 35.696  -13.445 -1.484   1.00 122.73 ? 77  ASP C CG  1 
ATOM   4463  O OD1 . ASP C 1 71  ? 36.326  -12.409 -1.789   1.00 130.24 ? 77  ASP C OD1 1 
ATOM   4464  O OD2 . ASP C 1 71  ? 35.696  -14.475 -2.191   1.00 127.64 ? 77  ASP C OD2 1 
ATOM   4465  N N   . GLU C 1 72  ? 31.474  -14.534 -0.232   1.00 125.66 ? 78  GLU C N   1 
ATOM   4466  C CA  . GLU C 1 72  ? 30.172  -14.492 -0.878   1.00 138.24 ? 78  GLU C CA  1 
ATOM   4467  C C   . GLU C 1 72  ? 29.422  -13.223 -0.501   1.00 146.69 ? 78  GLU C C   1 
ATOM   4468  O O   . GLU C 1 72  ? 29.678  -12.601 0.534    1.00 137.36 ? 78  GLU C O   1 
ATOM   4469  C CB  . GLU C 1 72  ? 29.336  -15.720 -0.496   1.00 129.55 ? 78  GLU C CB  1 
ATOM   4470  C CG  . GLU C 1 72  ? 28.599  -15.606 0.839    1.00 131.21 ? 78  GLU C CG  1 
ATOM   4471  C CD  . GLU C 1 72  ? 29.522  -15.639 2.048    1.00 141.52 ? 78  GLU C CD  1 
ATOM   4472  O OE1 . GLU C 1 72  ? 30.736  -15.888 1.881    1.00 149.21 ? 78  GLU C OE1 1 
ATOM   4473  O OE2 . GLU C 1 72  ? 29.028  -15.418 3.174    1.00 118.86 ? 78  GLU C OE2 1 
ATOM   4474  N N   . PHE C 1 73  ? 28.498  -12.842 -1.368   1.00 148.60 ? 79  PHE C N   1 
ATOM   4475  C CA  . PHE C 1 73  ? 27.610  -11.712 -1.123   1.00 139.13 ? 79  PHE C CA  1 
ATOM   4476  C C   . PHE C 1 73  ? 26.142  -12.087 -1.249   1.00 130.77 ? 79  PHE C C   1 
ATOM   4477  O O   . PHE C 1 73  ? 25.332  -11.634 -0.437   1.00 142.63 ? 79  PHE C O   1 
ATOM   4478  C CB  . PHE C 1 73  ? 27.943  -10.568 -2.091   1.00 131.30 ? 79  PHE C CB  1 
ATOM   4479  C CG  . PHE C 1 73  ? 27.862  -9.205  -1.472   1.00 153.56 ? 79  PHE C CG  1 
ATOM   4480  C CD1 . PHE C 1 73  ? 26.657  -8.528  -1.408   1.00 151.52 ? 79  PHE C CD1 1 
ATOM   4481  C CD2 . PHE C 1 73  ? 28.994  -8.600  -0.950   1.00 153.23 ? 79  PHE C CD2 1 
ATOM   4482  C CE1 . PHE C 1 73  ? 26.580  -7.271  -0.839   1.00 149.41 ? 79  PHE C CE1 1 
ATOM   4483  C CE2 . PHE C 1 73  ? 28.925  -7.344  -0.379   1.00 140.74 ? 79  PHE C CE2 1 
ATOM   4484  C CZ  . PHE C 1 73  ? 27.716  -6.678  -0.323   1.00 144.55 ? 79  PHE C CZ  1 
ATOM   4485  N N   . ILE C 1 74  ? 25.791  -12.931 -2.222   1.00 130.89 ? 80  ILE C N   1 
ATOM   4486  C CA  . ILE C 1 74  ? 24.418  -13.362 -2.479   1.00 137.77 ? 80  ILE C CA  1 
ATOM   4487  C C   . ILE C 1 74  ? 23.486  -12.155 -2.485   1.00 114.18 ? 80  ILE C C   1 
ATOM   4488  O O   . ILE C 1 74  ? 22.480  -12.118 -1.768   1.00 109.32 ? 80  ILE C O   1 
ATOM   4489  C CB  . ILE C 1 74  ? 23.977  -14.419 -1.453   1.00 142.93 ? 80  ILE C CB  1 
ATOM   4490  C CG1 . ILE C 1 74  ? 25.116  -15.411 -1.217   1.00 124.66 ? 80  ILE C CG1 1 
ATOM   4491  C CG2 . ILE C 1 74  ? 22.744  -15.174 -1.950   1.00 97.48  ? 80  ILE C CG2 1 
ATOM   4492  C CD1 . ILE C 1 74  ? 24.969  -16.217 0.054    1.00 101.86 ? 80  ILE C CD1 1 
ATOM   4493  N N   . ARG C 1 75  ? 23.831  -11.154 -3.292   1.00 116.73 ? 81  ARG C N   1 
ATOM   4494  C CA  . ARG C 1 75  ? 23.018  -9.961  -3.474   1.00 115.68 ? 81  ARG C CA  1 
ATOM   4495  C C   . ARG C 1 75  ? 22.248  -9.977  -4.786   1.00 109.87 ? 81  ARG C C   1 
ATOM   4496  O O   . ARG C 1 75  ? 21.352  -9.148  -4.974   1.00 127.32 ? 81  ARG C O   1 
ATOM   4497  C CB  . ARG C 1 75  ? 23.908  -8.708  -3.414   1.00 130.33 ? 81  ARG C CB  1 
ATOM   4498  C CG  . ARG C 1 75  ? 23.169  -7.374  -3.393   1.00 129.83 ? 81  ARG C CG  1 
ATOM   4499  C CD  . ARG C 1 75  ? 24.133  -6.199  -3.318   1.00 146.47 ? 81  ARG C CD  1 
ATOM   4500  N NE  . ARG C 1 75  ? 25.108  -6.205  -4.403   1.00 166.46 ? 81  ARG C NE  1 
ATOM   4501  C CZ  . ARG C 1 75  ? 24.930  -5.617  -5.579   1.00 157.23 ? 81  ARG C CZ  1 
ATOM   4502  N NH1 . ARG C 1 75  ? 23.809  -4.977  -5.870   1.00 131.63 ? 81  ARG C NH1 1 
ATOM   4503  N NH2 . ARG C 1 75  ? 25.901  -5.673  -6.486   1.00 153.63 ? 81  ARG C NH2 1 
ATOM   4504  N N   . VAL C 1 76  ? 22.551  -10.917 -5.675   1.00 104.09 ? 82  VAL C N   1 
ATOM   4505  C CA  . VAL C 1 76  ? 22.046  -10.905 -7.044   1.00 94.95  ? 82  VAL C CA  1 
ATOM   4506  C C   . VAL C 1 76  ? 20.850  -11.852 -7.112   1.00 91.50  ? 82  VAL C C   1 
ATOM   4507  O O   . VAL C 1 76  ? 21.043  -13.079 -7.068   1.00 94.34  ? 82  VAL C O   1 
ATOM   4508  C CB  . VAL C 1 76  ? 23.136  -11.317 -8.042   1.00 94.88  ? 82  VAL C CB  1 
ATOM   4509  C CG1 . VAL C 1 76  ? 22.806  -10.814 -9.432   1.00 92.23  ? 82  VAL C CG1 1 
ATOM   4510  C CG2 . VAL C 1 76  ? 24.493  -10.800 -7.586   1.00 89.30  ? 82  VAL C CG2 1 
ATOM   4511  N N   . PRO C 1 77  ? 19.618  -11.346 -7.220   1.00 78.49  ? 83  PRO C N   1 
ATOM   4512  C CA  . PRO C 1 77  ? 18.464  -12.227 -7.418   1.00 70.06  ? 83  PRO C CA  1 
ATOM   4513  C C   . PRO C 1 77  ? 18.148  -12.506 -8.877   1.00 76.05  ? 83  PRO C C   1 
ATOM   4514  O O   . PRO C 1 77  ? 17.272  -13.337 -9.154   1.00 75.37  ? 83  PRO C O   1 
ATOM   4515  C CB  . PRO C 1 77  ? 17.328  -11.436 -6.757   1.00 75.10  ? 83  PRO C CB  1 
ATOM   4516  C CG  . PRO C 1 77  ? 17.694  -10.013 -7.026   1.00 67.45  ? 83  PRO C CG  1 
ATOM   4517  C CD  . PRO C 1 77  ? 19.208  -9.941  -7.047   1.00 65.88  ? 83  PRO C CD  1 
ATOM   4518  N N   . GLU C 1 78  A 18.825  -11.838 -9.807   1.00 78.10  ? 83  GLU C N   1 
ATOM   4519  C CA  . GLU C 1 78  A 18.599  -12.045 -11.230  1.00 78.08  ? 83  GLU C CA  1 
ATOM   4520  C C   . GLU C 1 78  A 19.853  -11.629 -11.982  1.00 77.50  ? 83  GLU C C   1 
ATOM   4521  O O   . GLU C 1 78  A 20.555  -10.699 -11.577  1.00 78.67  ? 83  GLU C O   1 
ATOM   4522  C CB  . GLU C 1 78  A 17.384  -11.251 -11.727  1.00 77.07  ? 83  GLU C CB  1 
ATOM   4523  C CG  . GLU C 1 78  A 17.649  -9.764  -11.925  1.00 81.62  ? 83  GLU C CG  1 
ATOM   4524  C CD  . GLU C 1 78  A 16.391  -8.925  -11.852  1.00 110.93 ? 83  GLU C CD  1 
ATOM   4525  O OE1 . GLU C 1 78  A 15.495  -9.268  -11.052  1.00 110.41 ? 83  GLU C OE1 1 
ATOM   4526  O OE2 . GLU C 1 78  A 16.301  -7.922  -12.591  1.00 116.05 ? 83  GLU C OE2 1 
ATOM   4527  N N   . TRP C 1 79  ? 20.131  -12.331 -13.076  1.00 65.47  ? 84  TRP C N   1 
ATOM   4528  C CA  . TRP C 1 79  ? 21.276  -11.996 -13.907  1.00 59.00  ? 84  TRP C CA  1 
ATOM   4529  C C   . TRP C 1 79  ? 21.021  -12.473 -15.328  1.00 67.45  ? 84  TRP C C   1 
ATOM   4530  O O   . TRP C 1 79  ? 20.202  -13.365 -15.569  1.00 72.90  ? 84  TRP C O   1 
ATOM   4531  C CB  . TRP C 1 79  ? 22.575  -12.598 -13.354  1.00 59.49  ? 84  TRP C CB  1 
ATOM   4532  C CG  . TRP C 1 79  ? 22.550  -14.088 -13.202  1.00 62.55  ? 84  TRP C CG  1 
ATOM   4533  C CD1 . TRP C 1 79  ? 22.871  -15.015 -14.151  1.00 62.49  ? 84  TRP C CD1 1 
ATOM   4534  C CD2 . TRP C 1 79  ? 22.198  -14.825 -12.024  1.00 61.31  ? 84  TRP C CD2 1 
ATOM   4535  N NE1 . TRP C 1 79  ? 22.734  -16.283 -13.641  1.00 57.27  ? 84  TRP C NE1 1 
ATOM   4536  C CE2 . TRP C 1 79  ? 22.322  -16.194 -12.337  1.00 59.52  ? 84  TRP C CE2 1 
ATOM   4537  C CE3 . TRP C 1 79  ? 21.787  -14.461 -10.739  1.00 65.32  ? 84  TRP C CE3 1 
ATOM   4538  C CZ2 . TRP C 1 79  ? 22.052  -17.198 -11.410  1.00 60.80  ? 84  TRP C CZ2 1 
ATOM   4539  C CZ3 . TRP C 1 79  ? 21.517  -15.460 -9.820   1.00 62.87  ? 84  TRP C CZ3 1 
ATOM   4540  C CH2 . TRP C 1 79  ? 21.650  -16.812 -10.161  1.00 55.03  ? 84  TRP C CH2 1 
ATOM   4541  N N   . SER C 1 80  ? 21.737  -11.862 -16.270  1.00 65.48  ? 85  SER C N   1 
ATOM   4542  C CA  . SER C 1 80  ? 21.614  -12.195 -17.683  1.00 70.70  ? 85  SER C CA  1 
ATOM   4543  C C   . SER C 1 80  ? 22.658  -13.195 -18.156  1.00 78.20  ? 85  SER C C   1 
ATOM   4544  O O   . SER C 1 80  ? 22.370  -13.997 -19.051  1.00 75.28  ? 85  SER C O   1 
ATOM   4545  C CB  . SER C 1 80  ? 21.706  -10.925 -18.536  1.00 61.57  ? 85  SER C CB  1 
ATOM   4546  O OG  . SER C 1 80  ? 22.846  -10.159 -18.189  1.00 61.26  ? 85  SER C OG  1 
ATOM   4547  N N   . TYR C 1 81  ? 23.859  -13.164 -17.584  1.00 54.46  ? 86  TYR C N   1 
ATOM   4548  C CA  . TYR C 1 81  ? 24.890  -14.142 -17.902  1.00 63.91  ? 86  TYR C CA  1 
ATOM   4549  C C   . TYR C 1 81  ? 25.864  -14.209 -16.735  1.00 70.13  ? 86  TYR C C   1 
ATOM   4550  O O   . TYR C 1 81  ? 25.911  -13.310 -15.892  1.00 66.97  ? 86  TYR C O   1 
ATOM   4551  C CB  . TYR C 1 81  ? 25.612  -13.803 -19.215  1.00 61.01  ? 86  TYR C CB  1 
ATOM   4552  C CG  . TYR C 1 81  ? 26.360  -12.486 -19.218  1.00 70.64  ? 86  TYR C CG  1 
ATOM   4553  C CD1 . TYR C 1 81  ? 25.682  -11.277 -19.302  1.00 67.57  ? 86  TYR C CD1 1 
ATOM   4554  C CD2 . TYR C 1 81  ? 27.749  -12.456 -19.165  1.00 65.40  ? 86  TYR C CD2 1 
ATOM   4555  C CE1 . TYR C 1 81  ? 26.362  -10.075 -19.314  1.00 69.06  ? 86  TYR C CE1 1 
ATOM   4556  C CE2 . TYR C 1 81  ? 28.440  -11.257 -19.178  1.00 60.22  ? 86  TYR C CE2 1 
ATOM   4557  C CZ  . TYR C 1 81  ? 27.741  -10.071 -19.252  1.00 66.09  ? 86  TYR C CZ  1 
ATOM   4558  O OH  . TYR C 1 81  ? 28.420  -8.874  -19.266  1.00 66.11  ? 86  TYR C OH  1 
ATOM   4559  N N   . ILE C 1 82  ? 26.635  -15.293 -16.693  1.00 62.91  ? 87  ILE C N   1 
ATOM   4560  C CA  . ILE C 1 82  ? 27.556  -15.573 -15.597  1.00 61.67  ? 87  ILE C CA  1 
ATOM   4561  C C   . ILE C 1 82  ? 28.979  -15.390 -16.099  1.00 68.14  ? 87  ILE C C   1 
ATOM   4562  O O   . ILE C 1 82  ? 29.349  -15.927 -17.151  1.00 66.78  ? 87  ILE C O   1 
ATOM   4563  C CB  . ILE C 1 82  ? 27.354  -16.991 -15.036  1.00 64.86  ? 87  ILE C CB  1 
ATOM   4564  C CG1 . ILE C 1 82  ? 25.969  -17.124 -14.402  1.00 61.87  ? 87  ILE C CG1 1 
ATOM   4565  C CG2 . ILE C 1 82  ? 28.444  -17.325 -14.027  1.00 60.59  ? 87  ILE C CG2 1 
ATOM   4566  C CD1 . ILE C 1 82  ? 25.745  -18.454 -13.720  1.00 63.09  ? 87  ILE C CD1 1 
ATOM   4567  N N   . VAL C 1 83  ? 29.777  -14.635 -15.349  1.00 60.70  ? 88  VAL C N   1 
ATOM   4568  C CA  . VAL C 1 83  ? 31.179  -14.406 -15.674  1.00 58.07  ? 88  VAL C CA  1 
ATOM   4569  C C   . VAL C 1 83  ? 32.029  -15.223 -14.713  1.00 63.93  ? 88  VAL C C   1 
ATOM   4570  O O   . VAL C 1 83  ? 32.014  -14.988 -13.498  1.00 77.09  ? 88  VAL C O   1 
ATOM   4571  C CB  . VAL C 1 83  ? 31.546  -12.918 -15.604  1.00 59.76  ? 88  VAL C CB  1 
ATOM   4572  C CG1 . VAL C 1 83  ? 32.958  -12.704 -16.133  1.00 70.10  ? 88  VAL C CG1 1 
ATOM   4573  C CG2 . VAL C 1 83  ? 30.539  -12.088 -16.384  1.00 70.36  ? 88  VAL C CG2 1 
ATOM   4574  N N   . GLU C 1 84  ? 32.767  -16.181 -15.260  1.00 76.66  ? 89  GLU C N   1 
ATOM   4575  C CA  . GLU C 1 84  ? 33.721  -16.986 -14.520  1.00 63.92  ? 89  GLU C CA  1 
ATOM   4576  C C   . GLU C 1 84  ? 35.117  -16.697 -15.051  1.00 69.65  ? 89  GLU C C   1 
ATOM   4577  O O   . GLU C 1 84  ? 35.282  -16.119 -16.128  1.00 86.77  ? 89  GLU C O   1 
ATOM   4578  C CB  . GLU C 1 84  ? 33.410  -18.483 -14.660  1.00 69.79  ? 89  GLU C CB  1 
ATOM   4579  C CG  . GLU C 1 84  ? 33.275  -19.242 -13.349  1.00 76.68  ? 89  GLU C CG  1 
ATOM   4580  C CD  . GLU C 1 84  ? 32.913  -20.702 -13.567  1.00 88.78  ? 89  GLU C CD  1 
ATOM   4581  O OE1 . GLU C 1 84  ? 33.013  -21.171 -14.720  1.00 86.86  ? 89  GLU C OE1 1 
ATOM   4582  O OE2 . GLU C 1 84  ? 32.526  -21.379 -12.590  1.00 92.09  ? 89  GLU C OE2 1 
ATOM   4583  N N   . ARG C 1 85  ? 36.125  -17.086 -14.283  1.00 73.12  ? 90  ARG C N   1 
ATOM   4584  C CA  . ARG C 1 85  ? 37.482  -17.064 -14.800  1.00 82.02  ? 90  ARG C CA  1 
ATOM   4585  C C   . ARG C 1 85  ? 37.801  -18.414 -15.435  1.00 90.44  ? 90  ARG C C   1 
ATOM   4586  O O   . ARG C 1 85  ? 37.108  -19.411 -15.215  1.00 86.99  ? 90  ARG C O   1 
ATOM   4587  C CB  . ARG C 1 85  ? 38.491  -16.731 -13.697  1.00 64.65  ? 90  ARG C CB  1 
ATOM   4588  C CG  . ARG C 1 85  ? 39.509  -15.649 -14.071  1.00 104.60 ? 90  ARG C CG  1 
ATOM   4589  C CD  . ARG C 1 85  ? 40.638  -16.186 -14.945  1.00 117.03 ? 90  ARG C CD  1 
ATOM   4590  N NE  . ARG C 1 85  ? 41.541  -17.070 -14.215  1.00 114.13 ? 90  ARG C NE  1 
ATOM   4591  C CZ  . ARG C 1 85  ? 42.607  -17.656 -14.745  1.00 104.80 ? 90  ARG C CZ  1 
ATOM   4592  N NH1 . ARG C 1 85  ? 42.935  -17.477 -16.014  1.00 108.09 ? 90  ARG C NH1 1 
ATOM   4593  N NH2 . ARG C 1 85  ? 43.360  -18.444 -13.983  1.00 108.91 ? 90  ARG C NH2 1 
ATOM   4594  N N   . ALA C 1 86  ? 38.857  -18.428 -16.250  1.00 87.42  ? 91  ALA C N   1 
ATOM   4595  C CA  . ALA C 1 86  ? 39.295  -19.675 -16.866  1.00 95.28  ? 91  ALA C CA  1 
ATOM   4596  C C   . ALA C 1 86  ? 39.693  -20.698 -15.812  1.00 97.95  ? 91  ALA C C   1 
ATOM   4597  O O   . ALA C 1 86  ? 39.398  -21.891 -15.951  1.00 94.04  ? 91  ALA C O   1 
ATOM   4598  C CB  . ALA C 1 86  ? 40.459  -19.408 -17.819  1.00 94.49  ? 91  ALA C CB  1 
ATOM   4599  N N   . ASN C 1 87  ? 40.364  -20.252 -14.751  1.00 97.78  ? 92  ASN C N   1 
ATOM   4600  C CA  . ASN C 1 87  ? 40.810  -21.118 -13.662  1.00 100.25 ? 92  ASN C CA  1 
ATOM   4601  C C   . ASN C 1 87  ? 40.355  -20.514 -12.341  1.00 95.47  ? 92  ASN C C   1 
ATOM   4602  O O   . ASN C 1 87  ? 41.129  -19.821 -11.666  1.00 85.48  ? 92  ASN C O   1 
ATOM   4603  C CB  . ASN C 1 87  ? 42.330  -21.291 -13.682  1.00 112.69 ? 92  ASN C CB  1 
ATOM   4604  C CG  . ASN C 1 87  ? 42.889  -21.344 -15.088  1.00 115.35 ? 92  ASN C CG  1 
ATOM   4605  O OD1 . ASN C 1 87  ? 42.865  -20.353 -15.819  1.00 125.54 ? 92  ASN C OD1 1 
ATOM   4606  N ND2 . ASN C 1 87  ? 43.399  -22.506 -15.476  1.00 112.39 ? 92  ASN C ND2 1 
ATOM   4607  N N   . PRO C 1 88  ? 39.097  -20.733 -11.951  1.00 85.81  ? 93  PRO C N   1 
ATOM   4608  C CA  . PRO C 1 88  ? 38.635  -20.230 -10.651  1.00 75.31  ? 93  PRO C CA  1 
ATOM   4609  C C   . PRO C 1 88  ? 39.459  -20.812 -9.510   1.00 89.13  ? 93  PRO C C   1 
ATOM   4610  O O   . PRO C 1 88  ? 39.787  -22.000 -9.497   1.00 88.99  ? 93  PRO C O   1 
ATOM   4611  C CB  . PRO C 1 88  ? 37.175  -20.693 -10.589  1.00 85.41  ? 93  PRO C CB  1 
ATOM   4612  C CG  . PRO C 1 88  ? 36.782  -20.906 -12.015  1.00 84.15  ? 93  PRO C CG  1 
ATOM   4613  C CD  . PRO C 1 88  ? 38.018  -21.385 -12.711  1.00 94.98  ? 93  PRO C CD  1 
ATOM   4614  N N   . ALA C 1 89  ? 39.790  -19.955 -8.542   1.00 78.92  ? 94  ALA C N   1 
ATOM   4615  C CA  . ALA C 1 89  ? 40.706  -20.352 -7.478   1.00 66.31  ? 94  ALA C CA  1 
ATOM   4616  C C   . ALA C 1 89  ? 40.075  -21.379 -6.542   1.00 82.36  ? 94  ALA C C   1 
ATOM   4617  O O   . ALA C 1 89  ? 40.685  -22.410 -6.235   1.00 73.57  ? 94  ALA C O   1 
ATOM   4618  C CB  . ALA C 1 89  ? 41.159  -19.119 -6.698   1.00 77.89  ? 94  ALA C CB  1 
ATOM   4619  N N   . ASN C 1 90  ? 38.856  -21.117 -6.076   1.00 81.52  ? 95  ASN C N   1 
ATOM   4620  C CA  . ASN C 1 90  ? 38.176  -21.980 -5.115   1.00 80.13  ? 95  ASN C CA  1 
ATOM   4621  C C   . ASN C 1 90  ? 36.999  -22.651 -5.813   1.00 71.59  ? 95  ASN C C   1 
ATOM   4622  O O   . ASN C 1 90  ? 36.029  -21.982 -6.187   1.00 77.26  ? 95  ASN C O   1 
ATOM   4623  C CB  . ASN C 1 90  ? 37.703  -21.183 -3.900   1.00 74.17  ? 95  ASN C CB  1 
ATOM   4624  C CG  . ASN C 1 90  ? 38.761  -20.231 -3.375   1.00 76.78  ? 95  ASN C CG  1 
ATOM   4625  O OD1 . ASN C 1 90  ? 39.712  -20.646 -2.714   1.00 87.11  ? 95  ASN C OD1 1 
ATOM   4626  N ND2 . ASN C 1 90  ? 38.593  -18.943 -3.658   1.00 84.24  ? 95  ASN C ND2 1 
ATOM   4627  N N   . ASP C 1 91  ? 37.081  -23.971 -5.994   1.00 57.31  ? 96  ASP C N   1 
ATOM   4628  C CA  . ASP C 1 91  ? 35.981  -24.723 -6.591   1.00 68.77  ? 96  ASP C CA  1 
ATOM   4629  C C   . ASP C 1 91  ? 35.380  -25.737 -5.626   1.00 65.02  ? 96  ASP C C   1 
ATOM   4630  O O   . ASP C 1 91  ? 34.186  -25.660 -5.330   1.00 79.42  ? 96  ASP C O   1 
ATOM   4631  C CB  . ASP C 1 91  ? 36.456  -25.415 -7.874   1.00 69.51  ? 96  ASP C CB  1 
ATOM   4632  C CG  . ASP C 1 91  ? 35.418  -26.362 -8.444   1.00 84.16  ? 96  ASP C CG  1 
ATOM   4633  O OD1 . ASP C 1 91  ? 34.234  -25.973 -8.522   1.00 94.72  ? 96  ASP C OD1 1 
ATOM   4634  O OD2 . ASP C 1 91  ? 35.787  -27.495 -8.819   1.00 87.02  ? 96  ASP C OD2 1 
ATOM   4635  N N   . LEU C 1 92  A 36.171  -26.678 -5.115   1.00 64.59  ? 96  LEU C N   1 
ATOM   4636  C CA  . LEU C 1 92  A 35.671  -27.723 -4.223   1.00 61.08  ? 96  LEU C CA  1 
ATOM   4637  C C   . LEU C 1 92  A 36.777  -28.017 -3.216   1.00 66.96  ? 96  LEU C C   1 
ATOM   4638  O O   . LEU C 1 92  A 37.729  -28.740 -3.526   1.00 63.78  ? 96  LEU C O   1 
ATOM   4639  C CB  . LEU C 1 92  A 35.269  -28.980 -4.991   1.00 45.79  ? 96  LEU C CB  1 
ATOM   4640  C CG  . LEU C 1 92  A 34.006  -28.936 -5.858   1.00 57.48  ? 96  LEU C CG  1 
ATOM   4641  C CD1 . LEU C 1 92  A 33.795  -30.267 -6.564   1.00 55.11  ? 96  LEU C CD1 1 
ATOM   4642  C CD2 . LEU C 1 92  A 32.784  -28.573 -5.030   1.00 55.37  ? 96  LEU C CD2 1 
ATOM   4643  N N   . CYS C 1 93  ? 36.646  -27.450 -2.014   1.00 60.63  ? 97  CYS C N   1 
ATOM   4644  C CA  . CYS C 1 93  ? 37.690  -27.592 -1.005   1.00 47.11  ? 97  CYS C CA  1 
ATOM   4645  C C   . CYS C 1 93  ? 37.934  -29.058 -0.667   1.00 52.17  ? 97  CYS C C   1 
ATOM   4646  O O   . CYS C 1 93  ? 39.083  -29.512 -0.610   1.00 65.32  ? 97  CYS C O   1 
ATOM   4647  C CB  . CYS C 1 93  ? 37.311  -26.794 0.241    1.00 59.90  ? 97  CYS C CB  1 
ATOM   4648  S SG  . CYS C 1 93  ? 35.672  -27.167 0.901    1.00 85.56  ? 97  CYS C SG  1 
ATOM   4649  N N   . TYR C 1 94  ? 36.864  -29.816 -0.448   1.00 42.28  ? 98  TYR C N   1 
ATOM   4650  C CA  . TYR C 1 94  ? 36.973  -31.263 -0.329   1.00 49.08  ? 98  TYR C CA  1 
ATOM   4651  C C   . TYR C 1 94  ? 36.845  -31.873 -1.718   1.00 58.85  ? 98  TYR C C   1 
ATOM   4652  O O   . TYR C 1 94  ? 35.829  -31.644 -2.387   1.00 63.87  ? 98  TYR C O   1 
ATOM   4653  C CB  . TYR C 1 94  ? 35.897  -31.815 0.591    1.00 55.66  ? 98  TYR C CB  1 
ATOM   4654  C CG  . TYR C 1 94  ? 36.193  -33.199 1.128    1.00 49.55  ? 98  TYR C CG  1 
ATOM   4655  C CD1 . TYR C 1 94  ? 35.911  -34.331 0.379    1.00 56.51  ? 98  TYR C CD1 1 
ATOM   4656  C CD2 . TYR C 1 94  ? 36.749  -33.372 2.390    1.00 49.09  ? 98  TYR C CD2 1 
ATOM   4657  C CE1 . TYR C 1 94  ? 36.178  -35.597 0.866    1.00 56.51  ? 98  TYR C CE1 1 
ATOM   4658  C CE2 . TYR C 1 94  ? 37.019  -34.636 2.886    1.00 60.25  ? 98  TYR C CE2 1 
ATOM   4659  C CZ  . TYR C 1 94  ? 36.731  -35.745 2.120    1.00 43.54  ? 98  TYR C CZ  1 
ATOM   4660  O OH  . TYR C 1 94  ? 36.998  -37.003 2.610    1.00 55.56  ? 98  TYR C OH  1 
ATOM   4661  N N   . PRO C 1 95  ? 37.835  -32.629 -2.193   1.00 57.28  ? 99  PRO C N   1 
ATOM   4662  C CA  . PRO C 1 95  ? 37.809  -33.086 -3.587   1.00 37.80  ? 99  PRO C CA  1 
ATOM   4663  C C   . PRO C 1 95  ? 36.597  -33.955 -3.881   1.00 54.20  ? 99  PRO C C   1 
ATOM   4664  O O   . PRO C 1 95  ? 36.132  -34.724 -3.038   1.00 50.13  ? 99  PRO C O   1 
ATOM   4665  C CB  . PRO C 1 95  ? 39.113  -33.880 -3.725   1.00 33.65  ? 99  PRO C CB  1 
ATOM   4666  C CG  . PRO C 1 95  ? 39.451  -34.295 -2.331   1.00 48.34  ? 99  PRO C CG  1 
ATOM   4667  C CD  . PRO C 1 95  ? 38.990  -33.168 -1.454   1.00 51.35  ? 99  PRO C CD  1 
ATOM   4668  N N   . GLY C 1 96  ? 36.088  -33.821 -5.103   1.00 49.55  ? 100 GLY C N   1 
ATOM   4669  C CA  . GLY C 1 96  ? 34.912  -34.557 -5.519   1.00 47.52  ? 100 GLY C CA  1 
ATOM   4670  C C   . GLY C 1 96  ? 34.374  -34.088 -6.855   1.00 49.58  ? 100 GLY C C   1 
ATOM   4671  O O   . GLY C 1 96  ? 35.147  -33.717 -7.742   1.00 60.72  ? 100 GLY C O   1 
ATOM   4672  N N   . SER C 1 97  ? 33.053  -34.099 -7.014   1.00 51.65  ? 101 SER C N   1 
ATOM   4673  C CA  . SER C 1 97  ? 32.449  -33.720 -8.284   1.00 52.99  ? 101 SER C CA  1 
ATOM   4674  C C   . SER C 1 97  ? 31.004  -33.304 -8.056   1.00 52.81  ? 101 SER C C   1 
ATOM   4675  O O   . SER C 1 97  ? 30.387  -33.656 -7.047   1.00 63.28  ? 101 SER C O   1 
ATOM   4676  C CB  . SER C 1 97  ? 32.518  -34.866 -9.298   1.00 55.60  ? 101 SER C CB  1 
ATOM   4677  O OG  . SER C 1 97  ? 31.817  -36.005 -8.824   1.00 56.39  ? 101 SER C OG  1 
ATOM   4678  N N   . LEU C 1 98  ? 30.475  -32.549 -9.016   1.00 65.62  ? 102 LEU C N   1 
ATOM   4679  C CA  . LEU C 1 98  ? 29.063  -32.190 -9.068   1.00 50.14  ? 102 LEU C CA  1 
ATOM   4680  C C   . LEU C 1 98  ? 28.480  -32.784 -10.342  1.00 51.28  ? 102 LEU C C   1 
ATOM   4681  O O   . LEU C 1 98  ? 28.918  -32.442 -11.445  1.00 56.95  ? 102 LEU C O   1 
ATOM   4682  C CB  . LEU C 1 98  ? 28.876  -30.671 -9.032   1.00 42.72  ? 102 LEU C CB  1 
ATOM   4683  C CG  . LEU C 1 98  ? 27.445  -30.130 -9.087   1.00 47.04  ? 102 LEU C CG  1 
ATOM   4684  C CD1 . LEU C 1 98  ? 26.547  -30.850 -8.091   1.00 49.15  ? 102 LEU C CD1 1 
ATOM   4685  C CD2 . LEU C 1 98  ? 27.446  -28.635 -8.818   1.00 40.00  ? 102 LEU C CD2 1 
ATOM   4686  N N   . ASN C 1 99  ? 27.505  -33.677 -10.187  1.00 56.50  ? 103 ASN C N   1 
ATOM   4687  C CA  . ASN C 1 99  ? 26.985  -34.431 -11.320  1.00 45.84  ? 103 ASN C CA  1 
ATOM   4688  C C   . ASN C 1 99  ? 26.194  -33.526 -12.257  1.00 56.34  ? 103 ASN C C   1 
ATOM   4689  O O   . ASN C 1 99  ? 25.467  -32.632 -11.815  1.00 53.58  ? 103 ASN C O   1 
ATOM   4690  C CB  . ASN C 1 99  ? 26.111  -35.585 -10.829  1.00 49.59  ? 103 ASN C CB  1 
ATOM   4691  C CG  . ASN C 1 99  ? 25.780  -36.575 -11.926  1.00 52.85  ? 103 ASN C CG  1 
ATOM   4692  O OD1 . ASN C 1 99  ? 24.642  -36.641 -12.384  1.00 69.06  ? 103 ASN C OD1 1 
ATOM   4693  N ND2 . ASN C 1 99  ? 26.775  -37.351 -12.357  1.00 69.77  ? 103 ASN C ND2 1 
ATOM   4694  N N   . ASP C 1 100 ? 26.341  -33.770 -13.561  1.00 53.40  ? 104 ASP C N   1 
ATOM   4695  C CA  . ASP C 1 100 ? 25.711  -32.954 -14.601  1.00 48.30  ? 104 ASP C CA  1 
ATOM   4696  C C   . ASP C 1 100 ? 26.066  -31.478 -14.427  1.00 53.46  ? 104 ASP C C   1 
ATOM   4697  O O   . ASP C 1 100 ? 25.211  -30.591 -14.482  1.00 57.87  ? 104 ASP C O   1 
ATOM   4698  C CB  . ASP C 1 100 ? 24.194  -33.159 -14.618  1.00 54.95  ? 104 ASP C CB  1 
ATOM   4699  C CG  . ASP C 1 100 ? 23.802  -34.566 -15.022  1.00 68.46  ? 104 ASP C CG  1 
ATOM   4700  O OD1 . ASP C 1 100 ? 24.610  -35.235 -15.700  1.00 62.41  ? 104 ASP C OD1 1 
ATOM   4701  O OD2 . ASP C 1 100 ? 22.684  -35.000 -14.666  1.00 60.11  ? 104 ASP C OD2 1 
ATOM   4702  N N   . TYR C 1 101 ? 27.358  -31.224 -14.209  1.00 45.71  ? 105 TYR C N   1 
ATOM   4703  C CA  . TYR C 1 101 ? 27.822  -29.870 -13.918  1.00 51.66  ? 105 TYR C CA  1 
ATOM   4704  C C   . TYR C 1 101 ? 27.592  -28.931 -15.096  1.00 59.91  ? 105 TYR C C   1 
ATOM   4705  O O   . TYR C 1 101 ? 27.129  -27.798 -14.914  1.00 61.10  ? 105 TYR C O   1 
ATOM   4706  C CB  . TYR C 1 101 ? 29.302  -29.909 -13.539  1.00 40.83  ? 105 TYR C CB  1 
ATOM   4707  C CG  . TYR C 1 101 ? 29.861  -28.602 -13.029  1.00 55.49  ? 105 TYR C CG  1 
ATOM   4708  C CD1 . TYR C 1 101 ? 29.111  -27.781 -12.195  1.00 53.78  ? 105 TYR C CD1 1 
ATOM   4709  C CD2 . TYR C 1 101 ? 31.147  -28.198 -13.363  1.00 55.29  ? 105 TYR C CD2 1 
ATOM   4710  C CE1 . TYR C 1 101 ? 29.623  -26.586 -11.721  1.00 49.09  ? 105 TYR C CE1 1 
ATOM   4711  C CE2 . TYR C 1 101 ? 31.668  -27.007 -12.892  1.00 59.22  ? 105 TYR C CE2 1 
ATOM   4712  C CZ  . TYR C 1 101 ? 30.901  -26.206 -12.071  1.00 62.50  ? 105 TYR C CZ  1 
ATOM   4713  O OH  . TYR C 1 101 ? 31.414  -25.019 -11.601  1.00 70.20  ? 105 TYR C OH  1 
ATOM   4714  N N   . GLU C 1 102 ? 27.910  -29.381 -16.312  1.00 56.59  ? 106 GLU C N   1 
ATOM   4715  C CA  . GLU C 1 102 ? 27.767  -28.516 -17.479  1.00 56.55  ? 106 GLU C CA  1 
ATOM   4716  C C   . GLU C 1 102 ? 26.307  -28.168 -17.741  1.00 54.00  ? 106 GLU C C   1 
ATOM   4717  O O   . GLU C 1 102 ? 25.989  -27.020 -18.070  1.00 58.16  ? 106 GLU C O   1 
ATOM   4718  C CB  . GLU C 1 102 ? 28.389  -29.180 -18.706  1.00 54.93  ? 106 GLU C CB  1 
ATOM   4719  C CG  . GLU C 1 102 ? 29.904  -29.348 -18.645  1.00 69.91  ? 106 GLU C CG  1 
ATOM   4720  C CD  . GLU C 1 102 ? 30.665  -28.067 -18.952  1.00 79.23  ? 106 GLU C CD  1 
ATOM   4721  O OE1 . GLU C 1 102 ? 30.038  -26.987 -18.998  1.00 79.22  ? 106 GLU C OE1 1 
ATOM   4722  O OE2 . GLU C 1 102 ? 31.896  -28.140 -19.154  1.00 86.71  ? 106 GLU C OE2 1 
ATOM   4723  N N   . GLU C 1 103 ? 25.408  -29.148 -17.619  1.00 44.93  ? 107 GLU C N   1 
ATOM   4724  C CA  . GLU C 1 103 ? 23.984  -28.865 -17.775  1.00 43.49  ? 107 GLU C CA  1 
ATOM   4725  C C   . GLU C 1 103 ? 23.493  -27.906 -16.697  1.00 57.49  ? 107 GLU C C   1 
ATOM   4726  O O   . GLU C 1 103 ? 22.688  -27.008 -16.973  1.00 58.39  ? 107 GLU C O   1 
ATOM   4727  C CB  . GLU C 1 103 ? 23.181  -30.165 -17.747  1.00 37.55  ? 107 GLU C CB  1 
ATOM   4728  C CG  . GLU C 1 103 ? 23.207  -30.933 -19.060  1.00 71.14  ? 107 GLU C CG  1 
ATOM   4729  C CD  . GLU C 1 103 ? 22.492  -30.201 -20.181  1.00 75.58  ? 107 GLU C CD  1 
ATOM   4730  O OE1 . GLU C 1 103 ? 21.432  -29.594 -19.913  1.00 70.92  ? 107 GLU C OE1 1 
ATOM   4731  O OE2 . GLU C 1 103 ? 22.992  -30.230 -21.327  1.00 70.46  ? 107 GLU C OE2 1 
ATOM   4732  N N   . LEU C 1 104 ? 23.961  -28.087 -15.459  1.00 51.97  ? 108 LEU C N   1 
ATOM   4733  C CA  . LEU C 1 104 ? 23.585  -27.176 -14.383  1.00 51.87  ? 108 LEU C CA  1 
ATOM   4734  C C   . LEU C 1 104 ? 24.086  -25.761 -14.651  1.00 54.28  ? 108 LEU C C   1 
ATOM   4735  O O   . LEU C 1 104 ? 23.367  -24.784 -14.409  1.00 58.53  ? 108 LEU C O   1 
ATOM   4736  C CB  . LEU C 1 104 ? 24.121  -27.694 -13.049  1.00 53.00  ? 108 LEU C CB  1 
ATOM   4737  C CG  . LEU C 1 104 ? 23.791  -26.839 -11.825  1.00 49.21  ? 108 LEU C CG  1 
ATOM   4738  C CD1 . LEU C 1 104 ? 22.286  -26.676 -11.673  1.00 47.60  ? 108 LEU C CD1 1 
ATOM   4739  C CD2 . LEU C 1 104 ? 24.399  -27.446 -10.573  1.00 37.00  ? 108 LEU C CD2 1 
ATOM   4740  N N   . LYS C 1 105 ? 25.317  -25.628 -15.151  1.00 56.63  ? 109 LYS C N   1 
ATOM   4741  C CA  . LYS C 1 105 ? 25.837  -24.305 -15.487  1.00 55.79  ? 109 LYS C CA  1 
ATOM   4742  C C   . LYS C 1 105 ? 25.010  -23.651 -16.586  1.00 63.85  ? 109 LYS C C   1 
ATOM   4743  O O   . LYS C 1 105 ? 24.774  -22.437 -16.560  1.00 67.15  ? 109 LYS C O   1 
ATOM   4744  C CB  . LYS C 1 105 ? 27.307  -24.408 -15.897  1.00 46.04  ? 109 LYS C CB  1 
ATOM   4745  C CG  . LYS C 1 105 ? 28.278  -24.308 -14.726  1.00 56.22  ? 109 LYS C CG  1 
ATOM   4746  C CD  . LYS C 1 105 ? 29.611  -24.994 -15.008  1.00 54.11  ? 109 LYS C CD  1 
ATOM   4747  C CE  . LYS C 1 105 ? 30.567  -24.123 -15.808  1.00 76.28  ? 109 LYS C CE  1 
ATOM   4748  N NZ  . LYS C 1 105 ? 31.925  -24.737 -15.842  1.00 95.46  ? 109 LYS C NZ  1 
ATOM   4749  N N   . HIS C 1 106 ? 24.566  -24.440 -17.566  1.00 51.77  ? 110 HIS C N   1 
ATOM   4750  C CA  . HIS C 1 106 ? 23.691  -23.907 -18.603  1.00 52.34  ? 110 HIS C CA  1 
ATOM   4751  C C   . HIS C 1 106 ? 22.354  -23.465 -18.020  1.00 52.36  ? 110 HIS C C   1 
ATOM   4752  O O   . HIS C 1 106 ? 21.782  -22.456 -18.451  1.00 67.74  ? 110 HIS C O   1 
ATOM   4753  C CB  . HIS C 1 106 ? 23.483  -24.954 -19.697  1.00 63.76  ? 110 HIS C CB  1 
ATOM   4754  C CG  . HIS C 1 106 ? 22.857  -24.412 -20.944  1.00 66.75  ? 110 HIS C CG  1 
ATOM   4755  N ND1 . HIS C 1 106 ? 23.560  -23.665 -21.864  1.00 74.37  ? 110 HIS C ND1 1 
ATOM   4756  C CD2 . HIS C 1 106 ? 21.595  -24.509 -21.423  1.00 64.30  ? 110 HIS C CD2 1 
ATOM   4757  C CE1 . HIS C 1 106 ? 22.758  -23.325 -22.857  1.00 81.02  ? 110 HIS C CE1 1 
ATOM   4758  N NE2 . HIS C 1 106 ? 21.559  -23.824 -22.613  1.00 74.41  ? 110 HIS C NE2 1 
ATOM   4759  N N   . LEU C 1 107 ? 21.840  -24.210 -17.038  1.00 71.19  ? 111 LEU C N   1 
ATOM   4760  C CA  . LEU C 1 107 ? 20.557  -23.867 -16.430  1.00 50.85  ? 111 LEU C CA  1 
ATOM   4761  C C   . LEU C 1 107 ? 20.625  -22.539 -15.683  1.00 51.75  ? 111 LEU C C   1 
ATOM   4762  O O   . LEU C 1 107 ? 19.671  -21.754 -15.716  1.00 72.30  ? 111 LEU C O   1 
ATOM   4763  C CB  . LEU C 1 107 ? 20.111  -24.988 -15.491  1.00 58.30  ? 111 LEU C CB  1 
ATOM   4764  C CG  . LEU C 1 107 ? 18.722  -24.847 -14.866  1.00 59.52  ? 111 LEU C CG  1 
ATOM   4765  C CD1 . LEU C 1 107 ? 17.639  -24.958 -15.926  1.00 64.68  ? 111 LEU C CD1 1 
ATOM   4766  C CD2 . LEU C 1 107 ? 18.514  -25.883 -13.772  1.00 62.91  ? 111 LEU C CD2 1 
ATOM   4767  N N   . LEU C 1 108 ? 21.737  -22.271 -15.003  1.00 53.30  ? 112 LEU C N   1 
ATOM   4768  C CA  . LEU C 1 108 ? 21.876  -21.086 -14.166  1.00 65.84  ? 112 LEU C CA  1 
ATOM   4769  C C   . LEU C 1 108 ? 22.448  -19.884 -14.906  1.00 60.07  ? 112 LEU C C   1 
ATOM   4770  O O   . LEU C 1 108 ? 22.639  -18.834 -14.284  1.00 74.51  ? 112 LEU C O   1 
ATOM   4771  C CB  . LEU C 1 108 ? 22.758  -21.400 -12.954  1.00 58.62  ? 112 LEU C CB  1 
ATOM   4772  C CG  . LEU C 1 108 ? 22.204  -22.388 -11.929  1.00 55.04  ? 112 LEU C CG  1 
ATOM   4773  C CD1 . LEU C 1 108 ? 23.217  -22.614 -10.824  1.00 58.69  ? 112 LEU C CD1 1 
ATOM   4774  C CD2 . LEU C 1 108 ? 20.889  -21.881 -11.358  1.00 62.31  ? 112 LEU C CD2 1 
ATOM   4775  N N   . SER C 1 109 ? 22.715  -20.005 -16.209  1.00 54.92  ? 113 SER C N   1 
ATOM   4776  C CA  . SER C 1 109 ? 23.351  -18.913 -16.941  1.00 69.90  ? 113 SER C CA  1 
ATOM   4777  C C   . SER C 1 109 ? 22.479  -17.661 -16.950  1.00 65.24  ? 113 SER C C   1 
ATOM   4778  O O   . SER C 1 109 ? 22.992  -16.541 -16.848  1.00 66.73  ? 113 SER C O   1 
ATOM   4779  C CB  . SER C 1 109 ? 23.676  -19.358 -18.367  1.00 66.88  ? 113 SER C CB  1 
ATOM   4780  O OG  . SER C 1 109 ? 22.523  -19.859 -19.018  1.00 76.82  ? 113 SER C OG  1 
ATOM   4781  N N   . ARG C 1 110 ? 21.162  -17.824 -17.068  1.00 59.08  ? 114 ARG C N   1 
ATOM   4782  C CA  . ARG C 1 110 ? 20.226  -16.709 -16.969  1.00 63.83  ? 114 ARG C CA  1 
ATOM   4783  C C   . ARG C 1 110 ? 19.101  -17.097 -16.023  1.00 65.99  ? 114 ARG C C   1 
ATOM   4784  O O   . ARG C 1 110 ? 18.384  -18.070 -16.276  1.00 66.81  ? 114 ARG C O   1 
ATOM   4785  C CB  . ARG C 1 110 ? 19.663  -16.320 -18.338  1.00 80.12  ? 114 ARG C CB  1 
ATOM   4786  C CG  . ARG C 1 110 ? 18.553  -15.284 -18.256  1.00 78.40  ? 114 ARG C CG  1 
ATOM   4787  C CD  . ARG C 1 110 ? 18.596  -14.339 -19.440  1.00 79.19  ? 114 ARG C CD  1 
ATOM   4788  N NE  . ARG C 1 110 ? 18.144  -14.972 -20.672  1.00 92.91  ? 114 ARG C NE  1 
ATOM   4789  C CZ  . ARG C 1 110 ? 18.399  -14.505 -21.886  1.00 101.09 ? 114 ARG C CZ  1 
ATOM   4790  N NH1 . ARG C 1 110 ? 19.138  -13.423 -22.069  1.00 92.78  ? 114 ARG C NH1 1 
ATOM   4791  N NH2 . ARG C 1 110 ? 17.904  -15.142 -22.944  1.00 82.90  ? 114 ARG C NH2 1 
ATOM   4792  N N   . ILE C 1 111 ? 18.945  -16.333 -14.944  1.00 57.45  ? 115 ILE C N   1 
ATOM   4793  C CA  . ILE C 1 111 ? 17.947  -16.605 -13.918  1.00 66.92  ? 115 ILE C CA  1 
ATOM   4794  C C   . ILE C 1 111 ? 17.119  -15.349 -13.693  1.00 64.86  ? 115 ILE C C   1 
ATOM   4795  O O   . ILE C 1 111 ? 17.672  -14.252 -13.551  1.00 69.37  ? 115 ILE C O   1 
ATOM   4796  C CB  . ILE C 1 111 ? 18.602  -17.074 -12.604  1.00 63.12  ? 115 ILE C CB  1 
ATOM   4797  C CG1 . ILE C 1 111 ? 19.149  -18.491 -12.771  1.00 60.55  ? 115 ILE C CG1 1 
ATOM   4798  C CG2 . ILE C 1 111 ? 17.614  -17.013 -11.456  1.00 65.19  ? 115 ILE C CG2 1 
ATOM   4799  C CD1 . ILE C 1 111 ? 18.120  -19.481 -13.260  1.00 62.49  ? 115 ILE C CD1 1 
ATOM   4800  N N   . ASN C 1 112 ? 15.796  -15.509 -13.668  1.00 67.34  ? 116 ASN C N   1 
ATOM   4801  C CA  . ASN C 1 112 ? 14.889  -14.391 -13.439  1.00 70.21  ? 116 ASN C CA  1 
ATOM   4802  C C   . ASN C 1 112 ? 14.692  -14.098 -11.956  1.00 79.23  ? 116 ASN C C   1 
ATOM   4803  O O   . ASN C 1 112 ? 14.589  -12.930 -11.569  1.00 86.77  ? 116 ASN C O   1 
ATOM   4804  C CB  . ASN C 1 112 ? 13.538  -14.668 -14.106  1.00 81.70  ? 116 ASN C CB  1 
ATOM   4805  C CG  . ASN C 1 112 ? 12.537  -13.552 -13.881  1.00 106.61 ? 116 ASN C CG  1 
ATOM   4806  O OD1 . ASN C 1 112 ? 11.572  -13.710 -13.134  1.00 108.55 ? 116 ASN C OD1 1 
ATOM   4807  N ND2 . ASN C 1 112 ? 12.764  -12.414 -14.528  1.00 108.92 ? 116 ASN C ND2 1 
ATOM   4808  N N   . HIS C 1 113 ? 14.631  -15.131 -11.116  1.00 74.67  ? 117 HIS C N   1 
ATOM   4809  C CA  . HIS C 1 113 ? 14.551  -14.941 -9.673   1.00 87.04  ? 117 HIS C CA  1 
ATOM   4810  C C   . HIS C 1 113 ? 15.378  -16.010 -8.976   1.00 81.62  ? 117 HIS C C   1 
ATOM   4811  O O   . HIS C 1 113 ? 15.265  -17.196 -9.300   1.00 74.92  ? 117 HIS C O   1 
ATOM   4812  C CB  . HIS C 1 113 ? 13.104  -14.989 -9.173   1.00 76.00  ? 117 HIS C CB  1 
ATOM   4813  C CG  . HIS C 1 113 ? 12.939  -14.495 -7.770   1.00 95.36  ? 117 HIS C CG  1 
ATOM   4814  N ND1 . HIS C 1 113 ? 13.065  -13.165 -7.432   1.00 101.40 ? 117 HIS C ND1 1 
ATOM   4815  C CD2 . HIS C 1 113 ? 12.673  -15.153 -6.616   1.00 94.03  ? 117 HIS C CD2 1 
ATOM   4816  C CE1 . HIS C 1 113 ? 12.876  -13.023 -6.132   1.00 100.51 ? 117 HIS C CE1 1 
ATOM   4817  N NE2 . HIS C 1 113 ? 12.637  -14.214 -5.614   1.00 107.48 ? 117 HIS C NE2 1 
ATOM   4818  N N   . PHE C 1 114 ? 16.200  -15.588 -8.017   1.00 65.32  ? 118 PHE C N   1 
ATOM   4819  C CA  . PHE C 1 114 ? 17.074  -16.491 -7.280   1.00 66.14  ? 118 PHE C CA  1 
ATOM   4820  C C   . PHE C 1 114 ? 17.082  -16.071 -5.819   1.00 72.31  ? 118 PHE C C   1 
ATOM   4821  O O   . PHE C 1 114 ? 17.340  -14.904 -5.512   1.00 87.48  ? 118 PHE C O   1 
ATOM   4822  C CB  . PHE C 1 114 ? 18.495  -16.469 -7.856   1.00 75.23  ? 118 PHE C CB  1 
ATOM   4823  C CG  . PHE C 1 114 ? 19.268  -17.737 -7.625   1.00 79.49  ? 118 PHE C CG  1 
ATOM   4824  C CD1 . PHE C 1 114 ? 18.841  -18.936 -8.175   1.00 73.39  ? 118 PHE C CD1 1 
ATOM   4825  C CD2 . PHE C 1 114 ? 20.434  -17.726 -6.877   1.00 59.17  ? 118 PHE C CD2 1 
ATOM   4826  C CE1 . PHE C 1 114 ? 19.554  -20.103 -7.971   1.00 71.81  ? 118 PHE C CE1 1 
ATOM   4827  C CE2 . PHE C 1 114 ? 21.152  -18.887 -6.670   1.00 61.11  ? 118 PHE C CE2 1 
ATOM   4828  C CZ  . PHE C 1 114 ? 20.713  -20.078 -7.218   1.00 67.82  ? 118 PHE C CZ  1 
ATOM   4829  N N   . GLU C 1 115 ? 16.799  -17.016 -4.924   1.00 61.23  ? 119 GLU C N   1 
ATOM   4830  C CA  . GLU C 1 115 ? 16.745  -16.718 -3.495   1.00 61.33  ? 119 GLU C CA  1 
ATOM   4831  C C   . GLU C 1 115 ? 17.065  -17.979 -2.710   1.00 62.34  ? 119 GLU C C   1 
ATOM   4832  O O   . GLU C 1 115 ? 16.350  -18.979 -2.826   1.00 60.06  ? 119 GLU C O   1 
ATOM   4833  C CB  . GLU C 1 115 ? 15.370  -16.177 -3.098   1.00 62.48  ? 119 GLU C CB  1 
ATOM   4834  C CG  . GLU C 1 115 ? 15.266  -15.798 -1.630   1.00 84.85  ? 119 GLU C CG  1 
ATOM   4835  C CD  . GLU C 1 115 ? 13.832  -15.620 -1.166   1.00 107.58 ? 119 GLU C CD  1 
ATOM   4836  O OE1 . GLU C 1 115 ? 12.934  -15.507 -2.026   1.00 98.78  ? 119 GLU C OE1 1 
ATOM   4837  O OE2 . GLU C 1 115 ? 13.605  -15.598 0.063    1.00 105.94 ? 119 GLU C OE2 1 
ATOM   4838  N N   . LYS C 1 116 ? 18.132  -17.929 -1.916   1.00 61.11  ? 120 LYS C N   1 
ATOM   4839  C CA  . LYS C 1 116 ? 18.482  -19.044 -1.045   1.00 52.03  ? 120 LYS C CA  1 
ATOM   4840  C C   . LYS C 1 116 ? 17.560  -19.069 0.166    1.00 53.14  ? 120 LYS C C   1 
ATOM   4841  O O   . LYS C 1 116 ? 17.344  -18.041 0.815    1.00 56.49  ? 120 LYS C O   1 
ATOM   4842  C CB  . LYS C 1 116 ? 19.940  -18.944 -0.595   1.00 43.61  ? 120 LYS C CB  1 
ATOM   4843  C CG  . LYS C 1 116 ? 20.308  -19.938 0.500    1.00 61.99  ? 120 LYS C CG  1 
ATOM   4844  C CD  . LYS C 1 116 ? 21.804  -20.211 0.549    1.00 61.79  ? 120 LYS C CD  1 
ATOM   4845  C CE  . LYS C 1 116 ? 22.586  -19.007 1.042    1.00 55.59  ? 120 LYS C CE  1 
ATOM   4846  N NZ  . LYS C 1 116 ? 24.050  -19.280 1.059    1.00 74.06  ? 120 LYS C NZ  1 
ATOM   4847  N N   . ILE C 1 117 ? 17.011  -20.247 0.466    1.00 56.92  ? 121 ILE C N   1 
ATOM   4848  C CA  . ILE C 1 117 ? 16.163  -20.437 1.633    1.00 57.61  ? 121 ILE C CA  1 
ATOM   4849  C C   . ILE C 1 117 ? 16.632  -21.679 2.382    1.00 46.84  ? 121 ILE C C   1 
ATOM   4850  O O   . ILE C 1 117 ? 17.301  -22.555 1.831    1.00 58.12  ? 121 ILE C O   1 
ATOM   4851  C CB  . ILE C 1 117 ? 14.665  -20.571 1.272    1.00 55.63  ? 121 ILE C CB  1 
ATOM   4852  C CG1 . ILE C 1 117 ? 14.383  -21.932 0.631    1.00 61.29  ? 121 ILE C CG1 1 
ATOM   4853  C CG2 . ILE C 1 117 ? 14.223  -19.433 0.361    1.00 72.66  ? 121 ILE C CG2 1 
ATOM   4854  C CD1 . ILE C 1 117 ? 12.918  -22.289 0.568    1.00 63.43  ? 121 ILE C CD1 1 
ATOM   4855  N N   . LEU C 1 118 ? 16.268  -21.741 3.658    1.00 52.97  ? 122 LEU C N   1 
ATOM   4856  C CA  . LEU C 1 118 ? 16.564  -22.891 4.497    1.00 58.73  ? 122 LEU C CA  1 
ATOM   4857  C C   . LEU C 1 118 ? 15.396  -23.866 4.435    1.00 49.85  ? 122 LEU C C   1 
ATOM   4858  O O   . LEU C 1 118 ? 14.255  -23.489 4.725    1.00 64.41  ? 122 LEU C O   1 
ATOM   4859  C CB  . LEU C 1 118 ? 16.816  -22.446 5.937    1.00 52.71  ? 122 LEU C CB  1 
ATOM   4860  C CG  . LEU C 1 118 ? 17.162  -23.530 6.960    1.00 53.28  ? 122 LEU C CG  1 
ATOM   4861  C CD1 . LEU C 1 118 ? 18.596  -24.000 6.787    1.00 51.19  ? 122 LEU C CD1 1 
ATOM   4862  C CD2 . LEU C 1 118 ? 16.924  -23.035 8.379    1.00 45.63  ? 122 LEU C CD2 1 
ATOM   4863  N N   . ILE C 1 119 ? 15.677  -25.117 4.073    1.00 54.51  ? 123 ILE C N   1 
ATOM   4864  C CA  . ILE C 1 119 ? 14.636  -26.126 3.958    1.00 52.52  ? 123 ILE C CA  1 
ATOM   4865  C C   . ILE C 1 119 ? 14.770  -27.224 5.007    1.00 51.10  ? 123 ILE C C   1 
ATOM   4866  O O   . ILE C 1 119 ? 13.751  -27.778 5.437    1.00 67.57  ? 123 ILE C O   1 
ATOM   4867  C CB  . ILE C 1 119 ? 14.609  -26.734 2.537    1.00 59.05  ? 123 ILE C CB  1 
ATOM   4868  C CG1 . ILE C 1 119 ? 15.953  -27.390 2.205    1.00 57.33  ? 123 ILE C CG1 1 
ATOM   4869  C CG2 . ILE C 1 119 ? 14.260  -25.671 1.506    1.00 41.36  ? 123 ILE C CG2 1 
ATOM   4870  C CD1 . ILE C 1 119 ? 15.918  -28.286 0.991    1.00 49.34  ? 123 ILE C CD1 1 
ATOM   4871  N N   . ILE C 1 120 ? 15.985  -27.549 5.437    1.00 48.53  ? 124 ILE C N   1 
ATOM   4872  C CA  . ILE C 1 120 ? 16.200  -28.558 6.470    1.00 50.52  ? 124 ILE C CA  1 
ATOM   4873  C C   . ILE C 1 120 ? 17.170  -28.000 7.504    1.00 56.75  ? 124 ILE C C   1 
ATOM   4874  O O   . ILE C 1 120 ? 18.391  -28.140 7.341    1.00 58.33  ? 124 ILE C O   1 
ATOM   4875  C CB  . ILE C 1 120 ? 16.724  -29.879 5.882    1.00 49.20  ? 124 ILE C CB  1 
ATOM   4876  C CG1 . ILE C 1 120 ? 15.814  -30.370 4.753    1.00 45.11  ? 124 ILE C CG1 1 
ATOM   4877  C CG2 . ILE C 1 120 ? 16.825  -30.957 6.973    1.00 41.16  ? 124 ILE C CG2 1 
ATOM   4878  C CD1 . ILE C 1 120 ? 16.297  -31.632 4.076    1.00 42.97  ? 124 ILE C CD1 1 
ATOM   4879  N N   . PRO C 1 121 ? 16.687  -27.368 8.570    1.00 66.14  ? 125 PRO C N   1 
ATOM   4880  C CA  . PRO C 1 121 ? 17.599  -26.853 9.595    1.00 55.01  ? 125 PRO C CA  1 
ATOM   4881  C C   . PRO C 1 121 ? 18.266  -27.992 10.347   1.00 62.26  ? 125 PRO C C   1 
ATOM   4882  O O   . PRO C 1 121 ? 17.781  -29.125 10.375   1.00 69.66  ? 125 PRO C O   1 
ATOM   4883  C CB  . PRO C 1 121 ? 16.680  -26.041 10.515   1.00 45.63  ? 125 PRO C CB  1 
ATOM   4884  C CG  . PRO C 1 121 ? 15.343  -26.675 10.346   1.00 51.69  ? 125 PRO C CG  1 
ATOM   4885  C CD  . PRO C 1 121 ? 15.275  -27.122 8.911    1.00 44.72  ? 125 PRO C CD  1 
ATOM   4886  N N   . LYS C 1 122 A 19.406  -27.672 10.962   1.00 54.26  ? 125 LYS C N   1 
ATOM   4887  C CA  . LYS C 1 122 A 20.177  -28.679 11.683   1.00 55.13  ? 125 LYS C CA  1 
ATOM   4888  C C   . LYS C 1 122 A 19.448  -29.219 12.906   1.00 51.68  ? 125 LYS C C   1 
ATOM   4889  O O   . LYS C 1 122 A 19.868  -30.246 13.452   1.00 67.27  ? 125 LYS C O   1 
ATOM   4890  C CB  . LYS C 1 122 A 21.540  -28.102 12.078   1.00 47.38  ? 125 LYS C CB  1 
ATOM   4891  C CG  . LYS C 1 122 A 22.491  -27.976 10.891   1.00 63.97  ? 125 LYS C CG  1 
ATOM   4892  C CD  . LYS C 1 122 A 23.632  -26.997 11.136   1.00 54.11  ? 125 LYS C CD  1 
ATOM   4893  C CE  . LYS C 1 122 A 24.754  -27.611 11.952   1.00 83.77  ? 125 LYS C CE  1 
ATOM   4894  N NZ  . LYS C 1 122 A 26.030  -26.864 11.748   1.00 68.58  ? 125 LYS C NZ  1 
ATOM   4895  N N   . SER C 1 123 B 18.370  -28.564 13.343   1.00 61.91  ? 125 SER C N   1 
ATOM   4896  C CA  . SER C 1 123 B 17.538  -29.117 14.406   1.00 62.87  ? 125 SER C CA  1 
ATOM   4897  C C   . SER C 1 123 B 16.809  -30.381 13.969   1.00 72.73  ? 125 SER C C   1 
ATOM   4898  O O   . SER C 1 123 B 16.353  -31.146 14.825   1.00 63.77  ? 125 SER C O   1 
ATOM   4899  C CB  . SER C 1 123 B 16.524  -28.075 14.879   1.00 54.53  ? 125 SER C CB  1 
ATOM   4900  O OG  . SER C 1 123 B 17.172  -26.901 15.334   1.00 88.20  ? 125 SER C OG  1 
ATOM   4901  N N   . SER C 1 124 ? 16.693  -30.619 12.660   1.00 66.21  ? 126 SER C N   1 
ATOM   4902  C CA  . SER C 1 124 ? 15.959  -31.769 12.148   1.00 52.53  ? 126 SER C CA  1 
ATOM   4903  C C   . SER C 1 124 ? 16.662  -33.095 12.412   1.00 56.10  ? 126 SER C C   1 
ATOM   4904  O O   . SER C 1 124 ? 16.058  -34.149 12.184   1.00 57.34  ? 126 SER C O   1 
ATOM   4905  C CB  . SER C 1 124 ? 15.723  -31.607 10.644   1.00 58.90  ? 126 SER C CB  1 
ATOM   4906  O OG  . SER C 1 124 ? 15.095  -30.371 10.353   1.00 89.05  ? 126 SER C OG  1 
ATOM   4907  N N   . TRP C 1 125 ? 17.914  -33.073 12.877   1.00 52.91  ? 127 TRP C N   1 
ATOM   4908  C CA  . TRP C 1 125 ? 18.707  -34.278 13.108   1.00 62.55  ? 127 TRP C CA  1 
ATOM   4909  C C   . TRP C 1 125 ? 19.014  -34.380 14.598   1.00 61.86  ? 127 TRP C C   1 
ATOM   4910  O O   . TRP C 1 125 ? 20.119  -34.030 15.040   1.00 63.98  ? 127 TRP C O   1 
ATOM   4911  C CB  . TRP C 1 125 ? 19.996  -34.259 12.287   1.00 67.92  ? 127 TRP C CB  1 
ATOM   4912  C CG  . TRP C 1 125 ? 19.833  -33.679 10.915   1.00 54.74  ? 127 TRP C CG  1 
ATOM   4913  C CD1 . TRP C 1 125 ? 20.121  -32.401 10.526   1.00 56.17  ? 127 TRP C CD1 1 
ATOM   4914  C CD2 . TRP C 1 125 ? 19.346  -34.353 9.750    1.00 50.16  ? 127 TRP C CD2 1 
ATOM   4915  N NE1 . TRP C 1 125 ? 19.841  -32.240 9.190    1.00 51.72  ? 127 TRP C NE1 1 
ATOM   4916  C CE2 . TRP C 1 125 ? 19.364  -33.423 8.691    1.00 54.29  ? 127 TRP C CE2 1 
ATOM   4917  C CE3 . TRP C 1 125 ? 18.894  -35.652 9.500    1.00 56.54  ? 127 TRP C CE3 1 
ATOM   4918  C CZ2 . TRP C 1 125 ? 18.949  -33.753 7.402    1.00 41.43  ? 127 TRP C CZ2 1 
ATOM   4919  C CZ3 . TRP C 1 125 ? 18.483  -35.975 8.220    1.00 51.31  ? 127 TRP C CZ3 1 
ATOM   4920  C CH2 . TRP C 1 125 ? 18.513  -35.031 7.187    1.00 42.42  ? 127 TRP C CH2 1 
ATOM   4921  N N   . PRO C 1 126 ? 18.061  -34.857 15.407   1.00 67.14  ? 128 PRO C N   1 
ATOM   4922  C CA  . PRO C 1 126 ? 18.327  -34.986 16.847   1.00 71.78  ? 128 PRO C CA  1 
ATOM   4923  C C   . PRO C 1 126 ? 19.213  -36.166 17.204   1.00 57.89  ? 128 PRO C C   1 
ATOM   4924  O O   . PRO C 1 126 ? 19.837  -36.145 18.273   1.00 74.40  ? 128 PRO C O   1 
ATOM   4925  C CB  . PRO C 1 126 ? 16.924  -35.151 17.445   1.00 80.98  ? 128 PRO C CB  1 
ATOM   4926  C CG  . PRO C 1 126 ? 16.158  -35.830 16.364   1.00 54.21  ? 128 PRO C CG  1 
ATOM   4927  C CD  . PRO C 1 126 ? 16.697  -35.293 15.059   1.00 68.22  ? 128 PRO C CD  1 
ATOM   4928  N N   . ASN C 1 127 ? 19.291  -37.187 16.350   1.00 71.58  ? 129 ASN C N   1 
ATOM   4929  C CA  . ASN C 1 127 ? 20.051  -38.397 16.637   1.00 59.99  ? 129 ASN C CA  1 
ATOM   4930  C C   . ASN C 1 127 ? 21.311  -38.508 15.785   1.00 60.69  ? 129 ASN C C   1 
ATOM   4931  O O   . ASN C 1 127 ? 21.876  -39.599 15.660   1.00 61.02  ? 129 ASN C O   1 
ATOM   4932  C CB  . ASN C 1 127 ? 19.165  -39.629 16.445   1.00 66.86  ? 129 ASN C CB  1 
ATOM   4933  C CG  . ASN C 1 127 ? 17.916  -39.583 17.303   1.00 77.22  ? 129 ASN C CG  1 
ATOM   4934  O OD1 . ASN C 1 127 ? 17.956  -39.145 18.452   1.00 72.10  ? 129 ASN C OD1 1 
ATOM   4935  N ND2 . ASN C 1 127 ? 16.795  -40.028 16.744   1.00 83.88  ? 129 ASN C ND2 1 
ATOM   4936  N N   . HIS C 1 128 ? 21.758  -37.404 15.192   1.00 55.84  ? 130 HIS C N   1 
ATOM   4937  C CA  . HIS C 1 128 ? 22.998  -37.375 14.433   1.00 55.70  ? 130 HIS C CA  1 
ATOM   4938  C C   . HIS C 1 128 ? 23.761  -36.105 14.775   1.00 56.58  ? 130 HIS C C   1 
ATOM   4939  O O   . HIS C 1 128 ? 23.159  -35.049 14.985   1.00 65.79  ? 130 HIS C O   1 
ATOM   4940  C CB  . HIS C 1 128 ? 22.742  -37.438 12.920   1.00 51.84  ? 130 HIS C CB  1 
ATOM   4941  C CG  . HIS C 1 128 ? 22.048  -38.688 12.474   1.00 54.74  ? 130 HIS C CG  1 
ATOM   4942  N ND1 . HIS C 1 128 ? 20.677  -38.828 12.500   1.00 70.99  ? 130 HIS C ND1 1 
ATOM   4943  C CD2 . HIS C 1 128 ? 22.537  -39.854 11.989   1.00 58.15  ? 130 HIS C CD2 1 
ATOM   4944  C CE1 . HIS C 1 128 ? 20.351  -40.027 12.052   1.00 54.30  ? 130 HIS C CE1 1 
ATOM   4945  N NE2 . HIS C 1 128 ? 21.461  -40.670 11.736   1.00 50.14  ? 130 HIS C NE2 1 
ATOM   4946  N N   . GLU C 1 129 ? 25.086  -36.214 14.832   1.00 56.08  ? 131 GLU C N   1 
ATOM   4947  C CA  . GLU C 1 129 ? 25.919  -35.044 15.072   1.00 50.76  ? 131 GLU C CA  1 
ATOM   4948  C C   . GLU C 1 129 ? 25.911  -34.135 13.850   1.00 56.59  ? 131 GLU C C   1 
ATOM   4949  O O   . GLU C 1 129 ? 26.092  -34.595 12.718   1.00 56.33  ? 131 GLU C O   1 
ATOM   4950  C CB  . GLU C 1 129 ? 27.347  -35.467 15.412   1.00 42.90  ? 131 GLU C CB  1 
ATOM   4951  C CG  . GLU C 1 129 ? 27.653  -35.469 16.902   1.00 64.36  ? 131 GLU C CG  1 
ATOM   4952  C CD  . GLU C 1 129 ? 27.733  -34.069 17.480   1.00 94.56  ? 131 GLU C CD  1 
ATOM   4953  O OE1 . GLU C 1 129 ? 28.035  -33.127 16.716   1.00 84.50  ? 131 GLU C OE1 1 
ATOM   4954  O OE2 . GLU C 1 129 ? 27.492  -33.910 18.697   1.00 96.31  ? 131 GLU C OE2 1 
ATOM   4955  N N   . THR C 1 130 ? 25.701  -32.840 14.081   1.00 56.97  ? 132 THR C N   1 
ATOM   4956  C CA  . THR C 1 130 ? 25.646  -31.854 13.011   1.00 57.19  ? 132 THR C CA  1 
ATOM   4957  C C   . THR C 1 130 ? 26.784  -30.845 13.073   1.00 65.00  ? 132 THR C C   1 
ATOM   4958  O O   . THR C 1 130 ? 26.889  -29.996 12.181   1.00 67.02  ? 132 THR C O   1 
ATOM   4959  C CB  . THR C 1 130 ? 24.302  -31.113 13.043   1.00 53.88  ? 132 THR C CB  1 
ATOM   4960  O OG1 . THR C 1 130 ? 24.192  -30.370 14.263   1.00 57.72  ? 132 THR C OG1 1 
ATOM   4961  C CG2 . THR C 1 130 ? 23.147  -32.101 12.953   1.00 51.54  ? 132 THR C CG2 1 
ATOM   4962  N N   . SER C 1 131 ? 27.641  -30.916 14.091   1.00 58.93  ? 133 SER C N   1 
ATOM   4963  C CA  . SER C 1 131 ? 28.730  -29.965 14.257   1.00 65.41  ? 133 SER C CA  1 
ATOM   4964  C C   . SER C 1 131 ? 30.103  -30.546 13.948   1.00 58.61  ? 133 SER C C   1 
ATOM   4965  O O   . SER C 1 131 ? 31.074  -29.784 13.874   1.00 57.98  ? 133 SER C O   1 
ATOM   4966  C CB  . SER C 1 131 ? 28.727  -29.405 15.688   1.00 72.96  ? 133 SER C CB  1 
ATOM   4967  O OG  . SER C 1 131 ? 28.679  -30.448 16.647   1.00 78.91  ? 133 SER C OG  1 
ATOM   4968  N N   . LEU C 1 132 A 30.212  -31.862 13.770   1.00 61.81  ? 133 LEU C N   1 
ATOM   4969  C CA  . LEU C 1 132 A 31.493  -32.517 13.545   1.00 57.90  ? 133 LEU C CA  1 
ATOM   4970  C C   . LEU C 1 132 A 31.798  -32.772 12.074   1.00 51.98  ? 133 LEU C C   1 
ATOM   4971  O O   . LEU C 1 132 A 32.929  -33.151 11.753   1.00 52.75  ? 133 LEU C O   1 
ATOM   4972  C CB  . LEU C 1 132 A 31.543  -33.846 14.309   1.00 47.57  ? 133 LEU C CB  1 
ATOM   4973  C CG  . LEU C 1 132 A 31.428  -33.770 15.832   1.00 51.96  ? 133 LEU C CG  1 
ATOM   4974  C CD1 . LEU C 1 132 A 31.316  -35.167 16.417   1.00 50.40  ? 133 LEU C CD1 1 
ATOM   4975  C CD2 . LEU C 1 132 A 32.617  -33.032 16.427   1.00 55.63  ? 133 LEU C CD2 1 
ATOM   4976  N N   . GLY C 1 133 ? 30.838  -32.555 11.178   1.00 58.05  ? 134 GLY C N   1 
ATOM   4977  C CA  . GLY C 1 133 ? 31.051  -32.809 9.764    1.00 49.51  ? 134 GLY C CA  1 
ATOM   4978  C C   . GLY C 1 133 ? 31.960  -31.771 9.144    1.00 44.94  ? 134 GLY C C   1 
ATOM   4979  O O   . GLY C 1 133 ? 31.530  -30.935 8.343    1.00 61.71  ? 134 GLY C O   1 
ATOM   4980  N N   . VAL C 1 134 ? 33.233  -31.830 9.519    1.00 53.90  ? 135 VAL C N   1 
ATOM   4981  C CA  . VAL C 1 134 ? 34.171  -30.732 9.340    1.00 42.71  ? 135 VAL C CA  1 
ATOM   4982  C C   . VAL C 1 134 ? 35.500  -31.287 8.838    1.00 38.48  ? 135 VAL C C   1 
ATOM   4983  O O   . VAL C 1 134 ? 35.912  -32.389 9.212    1.00 64.61  ? 135 VAL C O   1 
ATOM   4984  C CB  . VAL C 1 134 ? 34.324  -29.968 10.676   1.00 54.42  ? 135 VAL C CB  1 
ATOM   4985  C CG1 . VAL C 1 134 ? 35.526  -29.093 10.667   1.00 60.09  ? 135 VAL C CG1 1 
ATOM   4986  C CG2 . VAL C 1 134 ? 33.078  -29.142 10.965   1.00 58.27  ? 135 VAL C CG2 1 
ATOM   4987  N N   . SER C 1 135 ? 36.172  -30.519 7.976    1.00 40.81  ? 136 SER C N   1 
ATOM   4988  C CA  . SER C 1 135 ? 37.414  -30.968 7.358    1.00 47.86  ? 136 SER C CA  1 
ATOM   4989  C C   . SER C 1 135 ? 38.447  -29.851 7.346    1.00 54.19  ? 136 SER C C   1 
ATOM   4990  O O   . SER C 1 135 ? 38.110  -28.667 7.258    1.00 55.32  ? 136 SER C O   1 
ATOM   4991  C CB  . SER C 1 135 ? 37.183  -31.460 5.922    1.00 63.67  ? 136 SER C CB  1 
ATOM   4992  O OG  . SER C 1 135 ? 38.417  -31.710 5.268    1.00 49.70  ? 136 SER C OG  1 
ATOM   4993  N N   . ALA C 1 136 ? 39.722  -30.250 7.425    1.00 48.57  ? 137 ALA C N   1 
ATOM   4994  C CA  . ALA C 1 136 ? 40.822  -29.301 7.309    1.00 47.76  ? 137 ALA C CA  1 
ATOM   4995  C C   . ALA C 1 136 ? 41.043  -28.849 5.871    1.00 56.17  ? 137 ALA C C   1 
ATOM   4996  O O   . ALA C 1 136 ? 41.710  -27.833 5.650    1.00 54.89  ? 137 ALA C O   1 
ATOM   4997  C CB  . ALA C 1 136 ? 42.109  -29.910 7.872    1.00 51.27  ? 137 ALA C CB  1 
ATOM   4998  N N   . ALA C 1 137 ? 40.502  -29.580 4.892    1.00 51.61  ? 138 ALA C N   1 
ATOM   4999  C CA  . ALA C 1 137 ? 40.563  -29.152 3.501    1.00 48.77  ? 138 ALA C CA  1 
ATOM   5000  C C   . ALA C 1 137 ? 39.629  -27.986 3.209    1.00 54.15  ? 138 ALA C C   1 
ATOM   5001  O O   . ALA C 1 137 ? 39.782  -27.339 2.169    1.00 62.48  ? 138 ALA C O   1 
ATOM   5002  C CB  . ALA C 1 137 ? 40.225  -30.319 2.572    1.00 49.96  ? 138 ALA C CB  1 
ATOM   5003  N N   . CYS C 1 138 ? 38.682  -27.696 4.099    1.00 64.93  ? 139 CYS C N   1 
ATOM   5004  C CA  . CYS C 1 138 ? 37.745  -26.586 3.939    1.00 63.68  ? 139 CYS C CA  1 
ATOM   5005  C C   . CYS C 1 138 ? 37.880  -25.617 5.109    1.00 59.95  ? 139 CYS C C   1 
ATOM   5006  O O   . CYS C 1 138 ? 36.932  -25.424 5.877    1.00 52.81  ? 139 CYS C O   1 
ATOM   5007  C CB  . CYS C 1 138 ? 36.313  -27.103 3.837    1.00 37.56  ? 139 CYS C CB  1 
ATOM   5008  S SG  . CYS C 1 138 ? 36.052  -28.314 2.533    1.00 86.23  ? 139 CYS C SG  1 
ATOM   5009  N N   . PRO C 1 139 ? 39.039  -24.980 5.268    1.00 58.34  ? 140 PRO C N   1 
ATOM   5010  C CA  . PRO C 1 139 ? 39.246  -24.130 6.442    1.00 51.90  ? 140 PRO C CA  1 
ATOM   5011  C C   . PRO C 1 139 ? 38.478  -22.823 6.340    1.00 48.60  ? 140 PRO C C   1 
ATOM   5012  O O   . PRO C 1 139 ? 38.204  -22.314 5.250    1.00 56.51  ? 140 PRO C O   1 
ATOM   5013  C CB  . PRO C 1 139 ? 40.757  -23.886 6.433    1.00 50.10  ? 140 PRO C CB  1 
ATOM   5014  C CG  . PRO C 1 139 ? 41.104  -23.907 4.985    1.00 45.16  ? 140 PRO C CG  1 
ATOM   5015  C CD  . PRO C 1 139 ? 40.182  -24.915 4.339    1.00 50.86  ? 140 PRO C CD  1 
ATOM   5016  N N   . TYR C 1 140 ? 38.124  -22.284 7.503    1.00 55.00  ? 141 TYR C N   1 
ATOM   5017  C CA  . TYR C 1 140 ? 37.576  -20.936 7.602    1.00 57.93  ? 141 TYR C CA  1 
ATOM   5018  C C   . TYR C 1 140 ? 38.207  -20.255 8.804    1.00 63.32  ? 141 TYR C C   1 
ATOM   5019  O O   . TYR C 1 140 ? 38.016  -20.702 9.939    1.00 57.70  ? 141 TYR C O   1 
ATOM   5020  C CB  . TYR C 1 140 ? 36.050  -20.947 7.732    1.00 54.24  ? 141 TYR C CB  1 
ATOM   5021  C CG  . TYR C 1 140 ? 35.469  -19.565 7.932    1.00 64.58  ? 141 TYR C CG  1 
ATOM   5022  C CD1 . TYR C 1 140 ? 35.272  -18.711 6.854    1.00 52.16  ? 141 TYR C CD1 1 
ATOM   5023  C CD2 . TYR C 1 140 ? 35.128  -19.111 9.200    1.00 52.83  ? 141 TYR C CD2 1 
ATOM   5024  C CE1 . TYR C 1 140 ? 34.746  -17.445 7.033    1.00 58.24  ? 141 TYR C CE1 1 
ATOM   5025  C CE2 . TYR C 1 140 ? 34.602  -17.848 9.390    1.00 51.80  ? 141 TYR C CE2 1 
ATOM   5026  C CZ  . TYR C 1 140 ? 34.414  -17.019 8.303    1.00 71.41  ? 141 TYR C CZ  1 
ATOM   5027  O OH  . TYR C 1 140 ? 33.889  -15.759 8.483    1.00 77.78  ? 141 TYR C OH  1 
ATOM   5028  N N   . GLN C 1 141 ? 38.949  -19.176 8.550    1.00 62.84  ? 142 GLN C N   1 
ATOM   5029  C CA  . GLN C 1 141 ? 39.621  -18.411 9.601    1.00 69.54  ? 142 GLN C CA  1 
ATOM   5030  C C   . GLN C 1 141 ? 40.518  -19.307 10.452   1.00 62.27  ? 142 GLN C C   1 
ATOM   5031  O O   . GLN C 1 141 ? 40.556  -19.204 11.681   1.00 70.06  ? 142 GLN C O   1 
ATOM   5032  C CB  . GLN C 1 141 ? 38.604  -17.667 10.472   1.00 68.14  ? 142 GLN C CB  1 
ATOM   5033  C CG  . GLN C 1 141 ? 37.810  -16.588 9.742    1.00 62.73  ? 142 GLN C CG  1 
ATOM   5034  C CD  . GLN C 1 141 ? 38.627  -15.342 9.454    1.00 71.10  ? 142 GLN C CD  1 
ATOM   5035  O OE1 . GLN C 1 141 ? 39.746  -15.190 9.943    1.00 87.33  ? 142 GLN C OE1 1 
ATOM   5036  N NE2 . GLN C 1 141 ? 38.067  -14.439 8.655    1.00 77.63  ? 142 GLN C NE2 1 
ATOM   5037  N N   . GLY C 1 142 ? 41.240  -20.210 9.790    1.00 58.72  ? 143 GLY C N   1 
ATOM   5038  C CA  . GLY C 1 142 ? 42.174  -21.090 10.458   1.00 56.47  ? 143 GLY C CA  1 
ATOM   5039  C C   . GLY C 1 142 ? 41.552  -22.275 11.160   1.00 63.66  ? 143 GLY C C   1 
ATOM   5040  O O   . GLY C 1 142 ? 42.289  -23.159 11.618   1.00 73.18  ? 143 GLY C O   1 
ATOM   5041  N N   . THR C 1 143 ? 40.228  -22.330 11.262   1.00 60.91  ? 144 THR C N   1 
ATOM   5042  C CA  . THR C 1 143 ? 39.466  -23.418 11.853   1.00 59.60  ? 144 THR C CA  1 
ATOM   5043  C C   . THR C 1 143 ? 38.930  -24.328 10.759   1.00 55.05  ? 144 THR C C   1 
ATOM   5044  O O   . THR C 1 143 ? 38.455  -23.841 9.727    1.00 46.12  ? 144 THR C O   1 
ATOM   5045  C CB  . THR C 1 143 ? 38.297  -22.877 12.680   1.00 51.39  ? 144 THR C CB  1 
ATOM   5046  O OG1 . THR C 1 143 ? 38.781  -21.901 13.611   1.00 83.90  ? 144 THR C OG1 1 
ATOM   5047  C CG2 . THR C 1 143 ? 37.603  -23.997 13.447   1.00 57.86  ? 144 THR C CG2 1 
ATOM   5048  N N   . PRO C 1 144 ? 39.013  -25.646 10.928   1.00 58.00  ? 145 PRO C N   1 
ATOM   5049  C CA  . PRO C 1 144 ? 38.411  -26.542 9.936    1.00 50.91  ? 145 PRO C CA  1 
ATOM   5050  C C   . PRO C 1 144 ? 36.916  -26.277 9.816    1.00 51.31  ? 145 PRO C C   1 
ATOM   5051  O O   . PRO C 1 144 ? 36.237  -25.982 10.802   1.00 60.39  ? 145 PRO C O   1 
ATOM   5052  C CB  . PRO C 1 144 ? 38.706  -27.939 10.493   1.00 40.62  ? 145 PRO C CB  1 
ATOM   5053  C CG  . PRO C 1 144 ? 39.882  -27.757 11.390   1.00 38.17  ? 145 PRO C CG  1 
ATOM   5054  C CD  . PRO C 1 144 ? 39.735  -26.385 11.978   1.00 52.84  ? 145 PRO C CD  1 
ATOM   5055  N N   . SER C 1 145 ? 36.409  -26.373 8.593    1.00 59.07  ? 146 SER C N   1 
ATOM   5056  C CA  . SER C 1 145 ? 35.010  -26.074 8.299    1.00 52.28  ? 146 SER C CA  1 
ATOM   5057  C C   . SER C 1 145 ? 34.576  -26.952 7.128    1.00 55.15  ? 146 SER C C   1 
ATOM   5058  O O   . SER C 1 145 ? 35.226  -27.956 6.818    1.00 53.82  ? 146 SER C O   1 
ATOM   5059  C CB  . SER C 1 145 ? 34.824  -24.570 8.029    1.00 52.23  ? 146 SER C CB  1 
ATOM   5060  O OG  . SER C 1 145 ? 33.476  -24.274 7.705    1.00 53.78  ? 146 SER C OG  1 
ATOM   5061  N N   . PHE C 1 146 ? 33.473  -26.585 6.482    1.00 51.27  ? 147 PHE C N   1 
ATOM   5062  C CA  . PHE C 1 146 ? 32.900  -27.400 5.419    1.00 47.90  ? 147 PHE C CA  1 
ATOM   5063  C C   . PHE C 1 146 ? 32.028  -26.508 4.540    1.00 46.21  ? 147 PHE C C   1 
ATOM   5064  O O   . PHE C 1 146 ? 31.881  -25.309 4.795    1.00 51.69  ? 147 PHE C O   1 
ATOM   5065  C CB  . PHE C 1 146 ? 32.115  -28.573 6.015    1.00 50.99  ? 147 PHE C CB  1 
ATOM   5066  C CG  . PHE C 1 146 ? 31.729  -29.617 5.015    1.00 46.56  ? 147 PHE C CG  1 
ATOM   5067  C CD1 . PHE C 1 146 ? 32.694  -30.384 4.385    1.00 53.04  ? 147 PHE C CD1 1 
ATOM   5068  C CD2 . PHE C 1 146 ? 30.397  -29.839 4.709    1.00 47.34  ? 147 PHE C CD2 1 
ATOM   5069  C CE1 . PHE C 1 146 ? 32.336  -31.348 3.465    1.00 46.65  ? 147 PHE C CE1 1 
ATOM   5070  C CE2 . PHE C 1 146 ? 30.033  -30.800 3.790    1.00 48.46  ? 147 PHE C CE2 1 
ATOM   5071  C CZ  . PHE C 1 146 ? 31.002  -31.555 3.169    1.00 56.51  ? 147 PHE C CZ  1 
ATOM   5072  N N   . PHE C 1 147 ? 31.469  -27.099 3.482    1.00 48.02  ? 148 PHE C N   1 
ATOM   5073  C CA  . PHE C 1 147 ? 30.503  -26.394 2.650    1.00 48.07  ? 148 PHE C CA  1 
ATOM   5074  C C   . PHE C 1 147 ? 29.343  -25.907 3.508    1.00 54.07  ? 148 PHE C C   1 
ATOM   5075  O O   . PHE C 1 147 ? 28.806  -26.657 4.328    1.00 56.43  ? 148 PHE C O   1 
ATOM   5076  C CB  . PHE C 1 147 ? 29.985  -27.306 1.535    1.00 52.34  ? 148 PHE C CB  1 
ATOM   5077  C CG  . PHE C 1 147 ? 31.042  -27.745 0.560    1.00 44.94  ? 148 PHE C CG  1 
ATOM   5078  C CD1 . PHE C 1 147 ? 31.497  -26.884 -0.426   1.00 53.47  ? 148 PHE C CD1 1 
ATOM   5079  C CD2 . PHE C 1 147 ? 31.564  -29.027 0.615    1.00 46.08  ? 148 PHE C CD2 1 
ATOM   5080  C CE1 . PHE C 1 147 ? 32.464  -27.289 -1.331   1.00 58.99  ? 148 PHE C CE1 1 
ATOM   5081  C CE2 . PHE C 1 147 ? 32.531  -29.439 -0.285   1.00 51.81  ? 148 PHE C CE2 1 
ATOM   5082  C CZ  . PHE C 1 147 ? 32.981  -28.569 -1.260   1.00 53.16  ? 148 PHE C CZ  1 
ATOM   5083  N N   . ARG C 1 148 ? 28.959  -24.647 3.321    1.00 51.69  ? 149 ARG C N   1 
ATOM   5084  C CA  . ARG C 1 148 ? 28.037  -23.989 4.237    1.00 45.71  ? 149 ARG C CA  1 
ATOM   5085  C C   . ARG C 1 148 ? 26.565  -24.203 3.900    1.00 58.91  ? 149 ARG C C   1 
ATOM   5086  O O   . ARG C 1 148 ? 25.707  -23.859 4.721    1.00 74.88  ? 149 ARG C O   1 
ATOM   5087  C CB  . ARG C 1 148 ? 28.350  -22.489 4.293    1.00 56.98  ? 149 ARG C CB  1 
ATOM   5088  C CG  . ARG C 1 148 ? 29.402  -22.157 5.339    1.00 60.53  ? 149 ARG C CG  1 
ATOM   5089  C CD  . ARG C 1 148 ? 30.166  -20.866 5.057    1.00 77.92  ? 149 ARG C CD  1 
ATOM   5090  N NE  . ARG C 1 148 ? 29.326  -19.675 4.982    1.00 97.36  ? 149 ARG C NE  1 
ATOM   5091  C CZ  . ARG C 1 148 ? 28.670  -19.141 6.004    1.00 96.72  ? 149 ARG C CZ  1 
ATOM   5092  N NH1 . ARG C 1 148 ? 28.634  -19.731 7.188    1.00 73.41  ? 149 ARG C NH1 1 
ATOM   5093  N NH2 . ARG C 1 148 ? 28.031  -17.987 5.833    1.00 110.16 ? 149 ARG C NH2 1 
ATOM   5094  N N   . ASN C 1 149 ? 26.245  -24.766 2.737    1.00 55.96  ? 150 ASN C N   1 
ATOM   5095  C CA  . ASN C 1 149 ? 24.858  -24.985 2.349    1.00 39.84  ? 150 ASN C CA  1 
ATOM   5096  C C   . ASN C 1 149 ? 24.417  -26.436 2.489    1.00 52.93  ? 150 ASN C C   1 
ATOM   5097  O O   . ASN C 1 149 ? 23.252  -26.744 2.219    1.00 47.24  ? 150 ASN C O   1 
ATOM   5098  C CB  . ASN C 1 149 ? 24.632  -24.504 0.913    1.00 51.85  ? 150 ASN C CB  1 
ATOM   5099  C CG  . ASN C 1 149 ? 24.743  -22.998 0.784    1.00 44.35  ? 150 ASN C CG  1 
ATOM   5100  O OD1 . ASN C 1 149 ? 24.314  -22.256 1.669    1.00 63.47  ? 150 ASN C OD1 1 
ATOM   5101  N ND2 . ASN C 1 149 ? 25.326  -22.538 -0.315   1.00 57.89  ? 150 ASN C ND2 1 
ATOM   5102  N N   . VAL C 1 150 ? 25.313  -27.332 2.904    1.00 54.06  ? 151 VAL C N   1 
ATOM   5103  C CA  . VAL C 1 150 ? 24.976  -28.720 3.183    1.00 38.97  ? 151 VAL C CA  1 
ATOM   5104  C C   . VAL C 1 150 ? 25.591  -29.101 4.522    1.00 52.09  ? 151 VAL C C   1 
ATOM   5105  O O   . VAL C 1 150 ? 26.531  -28.466 5.002    1.00 55.74  ? 151 VAL C O   1 
ATOM   5106  C CB  . VAL C 1 150 ? 25.452  -29.680 2.072    1.00 49.99  ? 151 VAL C CB  1 
ATOM   5107  C CG1 . VAL C 1 150 ? 24.672  -29.441 0.789    1.00 35.16  ? 151 VAL C CG1 1 
ATOM   5108  C CG2 . VAL C 1 150 ? 26.942  -29.511 1.832    1.00 41.03  ? 151 VAL C CG2 1 
ATOM   5109  N N   . VAL C 1 151 ? 25.046  -30.153 5.127    1.00 53.59  ? 152 VAL C N   1 
ATOM   5110  C CA  . VAL C 1 151 ? 25.489  -30.624 6.433    1.00 46.91  ? 152 VAL C CA  1 
ATOM   5111  C C   . VAL C 1 151 ? 26.052  -32.032 6.284    1.00 47.41  ? 152 VAL C C   1 
ATOM   5112  O O   . VAL C 1 151 ? 25.410  -32.907 5.692    1.00 50.71  ? 152 VAL C O   1 
ATOM   5113  C CB  . VAL C 1 151 ? 24.353  -30.586 7.474    1.00 47.07  ? 152 VAL C CB  1 
ATOM   5114  C CG1 . VAL C 1 151 ? 23.088  -31.229 6.923    1.00 48.98  ? 152 VAL C CG1 1 
ATOM   5115  C CG2 . VAL C 1 151 ? 24.791  -31.269 8.761    1.00 43.59  ? 152 VAL C CG2 1 
ATOM   5116  N N   . TRP C 1 152 ? 27.257  -32.237 6.809    1.00 49.96  ? 153 TRP C N   1 
ATOM   5117  C CA  . TRP C 1 152 ? 27.916  -33.541 6.806    1.00 44.47  ? 153 TRP C CA  1 
ATOM   5118  C C   . TRP C 1 152 ? 27.545  -34.244 8.107    1.00 55.72  ? 153 TRP C C   1 
ATOM   5119  O O   . TRP C 1 152 ? 28.131  -33.982 9.161    1.00 53.93  ? 153 TRP C O   1 
ATOM   5120  C CB  . TRP C 1 152 ? 29.423  -33.370 6.651    1.00 39.55  ? 153 TRP C CB  1 
ATOM   5121  C CG  . TRP C 1 152 ? 30.223  -34.643 6.567    1.00 47.07  ? 153 TRP C CG  1 
ATOM   5122  C CD1 . TRP C 1 152 ? 29.755  -35.924 6.636    1.00 47.10  ? 153 TRP C CD1 1 
ATOM   5123  C CD2 . TRP C 1 152 ? 31.643  -34.745 6.397    1.00 39.60  ? 153 TRP C CD2 1 
ATOM   5124  N NE1 . TRP C 1 152 ? 30.795  -36.815 6.520    1.00 45.28  ? 153 TRP C NE1 1 
ATOM   5125  C CE2 . TRP C 1 152 ? 31.964  -36.116 6.372    1.00 42.71  ? 153 TRP C CE2 1 
ATOM   5126  C CE3 . TRP C 1 152 ? 32.673  -33.808 6.262    1.00 45.49  ? 153 TRP C CE3 1 
ATOM   5127  C CZ2 . TRP C 1 152 ? 33.271  -36.574 6.218    1.00 48.24  ? 153 TRP C CZ2 1 
ATOM   5128  C CZ3 . TRP C 1 152 ? 33.971  -34.265 6.109    1.00 39.06  ? 153 TRP C CZ3 1 
ATOM   5129  C CH2 . TRP C 1 152 ? 34.257  -35.635 6.088    1.00 47.64  ? 153 TRP C CH2 1 
ATOM   5130  N N   . LEU C 1 153 ? 26.562  -35.136 8.034    1.00 46.53  ? 154 LEU C N   1 
ATOM   5131  C CA  . LEU C 1 153 ? 26.070  -35.808 9.227    1.00 55.50  ? 154 LEU C CA  1 
ATOM   5132  C C   . LEU C 1 153 ? 27.072  -36.847 9.715    1.00 53.70  ? 154 LEU C C   1 
ATOM   5133  O O   . LEU C 1 153 ? 27.686  -37.568 8.924    1.00 49.74  ? 154 LEU C O   1 
ATOM   5134  C CB  . LEU C 1 153 ? 24.718  -36.461 8.944    1.00 55.36  ? 154 LEU C CB  1 
ATOM   5135  C CG  . LEU C 1 153 ? 23.590  -35.488 8.594    1.00 54.25  ? 154 LEU C CG  1 
ATOM   5136  C CD1 . LEU C 1 153 ? 22.357  -36.239 8.131    1.00 42.34  ? 154 LEU C CD1 1 
ATOM   5137  C CD2 . LEU C 1 153 ? 23.256  -34.592 9.780    1.00 42.35  ? 154 LEU C CD2 1 
ATOM   5138  N N   . ILE C 1 154 ? 27.233  -36.914 11.035   1.00 53.71  ? 155 ILE C N   1 
ATOM   5139  C CA  . ILE C 1 154 ? 28.174  -37.814 11.685   1.00 40.15  ? 155 ILE C CA  1 
ATOM   5140  C C   . ILE C 1 154 ? 27.417  -38.592 12.752   1.00 46.48  ? 155 ILE C C   1 
ATOM   5141  O O   . ILE C 1 154 ? 26.390  -38.138 13.267   1.00 53.57  ? 155 ILE C O   1 
ATOM   5142  C CB  . ILE C 1 154 ? 29.375  -37.038 12.286   1.00 47.29  ? 155 ILE C CB  1 
ATOM   5143  C CG1 . ILE C 1 154 ? 30.176  -36.353 11.178   1.00 47.09  ? 155 ILE C CG1 1 
ATOM   5144  C CG2 . ILE C 1 154 ? 30.308  -37.944 13.080   1.00 25.95  ? 155 ILE C CG2 1 
ATOM   5145  C CD1 . ILE C 1 154 ? 30.844  -37.319 10.222   1.00 42.26  ? 155 ILE C CD1 1 
ATOM   5146  N N   . LYS C 1 155 ? 27.920  -39.783 13.068   1.00 41.53  ? 156 LYS C N   1 
ATOM   5147  C CA  . LYS C 1 155 ? 27.305  -40.614 14.092   1.00 53.38  ? 156 LYS C CA  1 
ATOM   5148  C C   . LYS C 1 155 ? 27.288  -39.892 15.437   1.00 57.55  ? 156 LYS C C   1 
ATOM   5149  O O   . LYS C 1 155 ? 28.146  -39.054 15.734   1.00 43.30  ? 156 LYS C O   1 
ATOM   5150  C CB  . LYS C 1 155 ? 28.056  -41.940 14.222   1.00 42.59  ? 156 LYS C CB  1 
ATOM   5151  C CG  . LYS C 1 155 ? 29.388  -41.826 14.946   1.00 36.84  ? 156 LYS C CG  1 
ATOM   5152  C CD  . LYS C 1 155 ? 30.095  -43.165 15.048   1.00 55.35  ? 156 LYS C CD  1 
ATOM   5153  C CE  . LYS C 1 155 ? 31.304  -43.063 15.964   1.00 45.80  ? 156 LYS C CE  1 
ATOM   5154  N NZ  . LYS C 1 155 ? 32.164  -44.273 15.888   1.00 42.25  ? 156 LYS C NZ  1 
ATOM   5155  N N   . LYS C 1 156 ? 26.282  -40.212 16.247   1.00 47.57  ? 157 LYS C N   1 
ATOM   5156  C CA  . LYS C 1 156 ? 26.150  -39.688 17.600   1.00 56.46  ? 157 LYS C CA  1 
ATOM   5157  C C   . LYS C 1 156 ? 26.072  -40.856 18.570   1.00 56.80  ? 157 LYS C C   1 
ATOM   5158  O O   . LYS C 1 156 ? 25.294  -41.793 18.356   1.00 61.39  ? 157 LYS C O   1 
ATOM   5159  C CB  . LYS C 1 156 ? 24.912  -38.795 17.739   1.00 58.28  ? 157 LYS C CB  1 
ATOM   5160  C CG  . LYS C 1 156 ? 24.695  -38.264 19.153   1.00 62.80  ? 157 LYS C CG  1 
ATOM   5161  C CD  . LYS C 1 156 ? 23.446  -37.404 19.250   1.00 63.79  ? 157 LYS C CD  1 
ATOM   5162  C CE  . LYS C 1 156 ? 23.572  -36.140 18.414   1.00 82.24  ? 157 LYS C CE  1 
ATOM   5163  N NZ  . LYS C 1 156 ? 22.421  -35.219 18.637   1.00 92.87  ? 157 LYS C NZ  1 
ATOM   5164  N N   . ASN C 1 157 ? 26.883  -40.800 19.629   1.00 43.20  ? 158 ASN C N   1 
ATOM   5165  C CA  . ASN C 1 157 ? 26.940  -41.861 20.637   1.00 61.77  ? 158 ASN C CA  1 
ATOM   5166  C C   . ASN C 1 157 ? 27.261  -43.213 20.003   1.00 63.84  ? 158 ASN C C   1 
ATOM   5167  O O   . ASN C 1 157 ? 26.688  -44.242 20.366   1.00 61.05  ? 158 ASN C O   1 
ATOM   5168  C CB  . ASN C 1 157 ? 25.639  -41.932 21.438   1.00 58.59  ? 158 ASN C CB  1 
ATOM   5169  C CG  . ASN C 1 157 ? 25.278  -40.608 22.079   1.00 67.30  ? 158 ASN C CG  1 
ATOM   5170  O OD1 . ASN C 1 157 ? 26.150  -39.869 22.536   1.00 72.01  ? 158 ASN C OD1 1 
ATOM   5171  N ND2 . ASN C 1 157 ? 23.987  -40.300 22.114   1.00 65.73  ? 158 ASN C ND2 1 
ATOM   5172  N N   . ASP C 1 158 ? 28.194  -43.204 19.050   1.00 58.16  ? 159 ASP C N   1 
ATOM   5173  C CA  . ASP C 1 158 ? 28.599  -44.405 18.316   1.00 69.33  ? 159 ASP C CA  1 
ATOM   5174  C C   . ASP C 1 158 ? 27.399  -45.083 17.654   1.00 62.25  ? 159 ASP C C   1 
ATOM   5175  O O   . ASP C 1 158 ? 27.279  -46.310 17.648   1.00 60.69  ? 159 ASP C O   1 
ATOM   5176  C CB  . ASP C 1 158 ? 29.352  -45.383 19.225   1.00 51.49  ? 159 ASP C CB  1 
ATOM   5177  C CG  . ASP C 1 158 ? 30.282  -46.302 18.451   1.00 78.11  ? 159 ASP C CG  1 
ATOM   5178  O OD1 . ASP C 1 158 ? 30.542  -46.025 17.261   1.00 73.95  ? 159 ASP C OD1 1 
ATOM   5179  O OD2 . ASP C 1 158 ? 30.749  -47.304 19.033   1.00 96.12  ? 159 ASP C OD2 1 
ATOM   5180  N N   . ALA C 1 159 ? 26.504  -44.277 17.085   1.00 54.81  ? 160 ALA C N   1 
ATOM   5181  C CA  . ALA C 1 159 ? 25.322  -44.794 16.410   1.00 56.27  ? 160 ALA C CA  1 
ATOM   5182  C C   . ALA C 1 159 ? 24.923  -43.845 15.290   1.00 52.30  ? 160 ALA C C   1 
ATOM   5183  O O   . ALA C 1 159 ? 25.008  -42.623 15.445   1.00 59.03  ? 160 ALA C O   1 
ATOM   5184  C CB  . ALA C 1 159 ? 24.158  -44.977 17.390   1.00 37.57  ? 160 ALA C CB  1 
ATOM   5185  N N   . TYR C 1 160 ? 24.494  -44.417 14.165   1.00 47.26  ? 161 TYR C N   1 
ATOM   5186  C CA  . TYR C 1 160 ? 24.004  -43.663 13.010   1.00 46.13  ? 161 TYR C CA  1 
ATOM   5187  C C   . TYR C 1 160 ? 22.664  -44.268 12.620   1.00 53.12  ? 161 TYR C C   1 
ATOM   5188  O O   . TYR C 1 160 ? 22.597  -45.141 11.744   1.00 60.41  ? 161 TYR C O   1 
ATOM   5189  C CB  . TYR C 1 160 ? 24.997  -43.709 11.848   1.00 43.98  ? 161 TYR C CB  1 
ATOM   5190  C CG  . TYR C 1 160 ? 24.771  -42.670 10.768   1.00 49.34  ? 161 TYR C CG  1 
ATOM   5191  C CD1 . TYR C 1 160 ? 23.673  -42.743 9.921    1.00 42.45  ? 161 TYR C CD1 1 
ATOM   5192  C CD2 . TYR C 1 160 ? 25.671  -41.625 10.584   1.00 51.35  ? 161 TYR C CD2 1 
ATOM   5193  C CE1 . TYR C 1 160 ? 23.465  -41.800 8.931    1.00 44.35  ? 161 TYR C CE1 1 
ATOM   5194  C CE2 . TYR C 1 160 ? 25.474  -40.675 9.592    1.00 50.38  ? 161 TYR C CE2 1 
ATOM   5195  C CZ  . TYR C 1 160 ? 24.369  -40.769 8.768    1.00 53.72  ? 161 TYR C CZ  1 
ATOM   5196  O OH  . TYR C 1 160 ? 24.168  -39.828 7.782    1.00 57.72  ? 161 TYR C OH  1 
ATOM   5197  N N   . PRO C 1 161 ? 21.579  -43.853 13.271   1.00 56.27  ? 162 PRO C N   1 
ATOM   5198  C CA  . PRO C 1 161 ? 20.264  -44.406 12.932   1.00 54.69  ? 162 PRO C CA  1 
ATOM   5199  C C   . PRO C 1 161 ? 19.871  -44.078 11.499   1.00 49.89  ? 162 PRO C C   1 
ATOM   5200  O O   . PRO C 1 161 ? 20.298  -43.072 10.929   1.00 56.23  ? 162 PRO C O   1 
ATOM   5201  C CB  . PRO C 1 161 ? 19.321  -43.731 13.937   1.00 44.52  ? 162 PRO C CB  1 
ATOM   5202  C CG  . PRO C 1 161 ? 20.203  -43.274 15.051   1.00 43.96  ? 162 PRO C CG  1 
ATOM   5203  C CD  . PRO C 1 161 ? 21.523  -42.942 14.426   1.00 54.46  ? 162 PRO C CD  1 
ATOM   5204  N N   . THR C 1 162 ? 19.058  -44.957 10.914   1.00 51.39  ? 163 THR C N   1 
ATOM   5205  C CA  . THR C 1 162 ? 18.626  -44.770 9.534    1.00 44.24  ? 163 THR C CA  1 
ATOM   5206  C C   . THR C 1 162 ? 17.793  -43.502 9.403    1.00 39.82  ? 163 THR C C   1 
ATOM   5207  O O   . THR C 1 162 ? 16.847  -43.281 10.164   1.00 58.65  ? 163 THR C O   1 
ATOM   5208  C CB  . THR C 1 162 ? 17.823  -45.984 9.061    1.00 45.43  ? 163 THR C CB  1 
ATOM   5209  O OG1 . THR C 1 162 ? 18.705  -47.096 8.876    1.00 63.14  ? 163 THR C OG1 1 
ATOM   5210  C CG2 . THR C 1 162 ? 17.112  -45.682 7.749    1.00 56.18  ? 163 THR C CG2 1 
ATOM   5211  N N   . ILE C 1 163 ? 18.157  -42.666 8.439    1.00 51.62  ? 164 ILE C N   1 
ATOM   5212  C CA  . ILE C 1 163 ? 17.441  -41.427 8.165    1.00 44.13  ? 164 ILE C CA  1 
ATOM   5213  C C   . ILE C 1 163 ? 16.322  -41.719 7.177    1.00 50.97  ? 164 ILE C C   1 
ATOM   5214  O O   . ILE C 1 163 ? 16.550  -42.340 6.134    1.00 60.91  ? 164 ILE C O   1 
ATOM   5215  C CB  . ILE C 1 163 ? 18.397  -40.356 7.616    1.00 52.98  ? 164 ILE C CB  1 
ATOM   5216  C CG1 . ILE C 1 163 ? 19.434  -39.980 8.677    1.00 49.71  ? 164 ILE C CG1 1 
ATOM   5217  C CG2 . ILE C 1 163 ? 17.622  -39.138 7.155    1.00 47.91  ? 164 ILE C CG2 1 
ATOM   5218  C CD1 . ILE C 1 163 ? 20.736  -39.460 8.104    1.00 48.81  ? 164 ILE C CD1 1 
ATOM   5219  N N   . LYS C 1 164 ? 15.105  -41.289 7.511    1.00 53.26  ? 165 LYS C N   1 
ATOM   5220  C CA  . LYS C 1 164 ? 13.963  -41.356 6.592    1.00 50.95  ? 165 LYS C CA  1 
ATOM   5221  C C   . LYS C 1 164 ? 13.253  -40.008 6.687    1.00 46.36  ? 165 LYS C C   1 
ATOM   5222  O O   . LYS C 1 164 ? 12.383  -39.810 7.539    1.00 78.39  ? 165 LYS C O   1 
ATOM   5223  C CB  . LYS C 1 164 ? 13.025  -42.512 6.918    1.00 47.89  ? 165 LYS C CB  1 
ATOM   5224  C CG  . LYS C 1 164 ? 13.565  -43.899 6.594    1.00 62.75  ? 165 LYS C CG  1 
ATOM   5225  C CD  . LYS C 1 164 ? 12.483  -44.948 6.831    1.00 75.07  ? 165 LYS C CD  1 
ATOM   5226  C CE  . LYS C 1 164 ? 13.051  -46.359 6.940    1.00 85.39  ? 165 LYS C CE  1 
ATOM   5227  N NZ  . LYS C 1 164 ? 13.235  -47.022 5.619    1.00 78.41  ? 165 LYS C NZ  1 
ATOM   5228  N N   . ILE C 1 165 ? 13.626  -39.086 5.804    1.00 56.48  ? 166 ILE C N   1 
ATOM   5229  C CA  . ILE C 1 165 ? 13.127  -37.721 5.857    1.00 40.44  ? 166 ILE C CA  1 
ATOM   5230  C C   . ILE C 1 165 ? 12.492  -37.375 4.516    1.00 56.14  ? 166 ILE C C   1 
ATOM   5231  O O   . ILE C 1 165 ? 12.749  -38.011 3.490    1.00 48.27  ? 166 ILE C O   1 
ATOM   5232  C CB  . ILE C 1 165 ? 14.245  -36.720 6.218    1.00 48.97  ? 166 ILE C CB  1 
ATOM   5233  C CG1 . ILE C 1 165 ? 13.661  -35.477 6.892    1.00 76.73  ? 166 ILE C CG1 1 
ATOM   5234  C CG2 . ILE C 1 165 ? 15.051  -36.340 4.981    1.00 33.57  ? 166 ILE C CG2 1 
ATOM   5235  C CD1 . ILE C 1 165 ? 14.703  -34.591 7.546    1.00 79.01  ? 166 ILE C CD1 1 
ATOM   5236  N N   . SER C 1 166 ? 11.639  -36.352 4.539    1.00 58.42  ? 167 SER C N   1 
ATOM   5237  C CA  . SER C 1 166 ? 10.909  -35.923 3.356    1.00 44.60  ? 167 SER C CA  1 
ATOM   5238  C C   . SER C 1 166 ? 10.668  -34.423 3.436    1.00 50.35  ? 167 SER C C   1 
ATOM   5239  O O   . SER C 1 166 ? 10.423  -33.886 4.520    1.00 65.16  ? 167 SER C O   1 
ATOM   5240  C CB  . SER C 1 166 ? 9.575   -36.666 3.226    1.00 46.84  ? 167 SER C CB  1 
ATOM   5241  O OG  . SER C 1 166 ? 8.810   -36.159 2.147    1.00 73.86  ? 167 SER C OG  1 
ATOM   5242  N N   . TYR C 1 167 ? 10.734  -33.757 2.286    1.00 51.48  ? 168 TYR C N   1 
ATOM   5243  C CA  . TYR C 1 167 ? 10.473  -32.326 2.196    1.00 49.32  ? 168 TYR C CA  1 
ATOM   5244  C C   . TYR C 1 167 ? 9.552   -32.050 1.017    1.00 56.69  ? 168 TYR C C   1 
ATOM   5245  O O   . TYR C 1 167 ? 9.806   -32.521 -0.096   1.00 60.84  ? 168 TYR C O   1 
ATOM   5246  C CB  . TYR C 1 167 ? 11.769  -31.524 2.045    1.00 46.89  ? 168 TYR C CB  1 
ATOM   5247  C CG  . TYR C 1 167 ? 11.529  -30.063 1.740    1.00 57.39  ? 168 TYR C CG  1 
ATOM   5248  C CD1 . TYR C 1 167 ? 11.255  -29.157 2.755    1.00 43.58  ? 168 TYR C CD1 1 
ATOM   5249  C CD2 . TYR C 1 167 ? 11.569  -29.592 0.435    1.00 49.05  ? 168 TYR C CD2 1 
ATOM   5250  C CE1 . TYR C 1 167 ? 11.030  -27.821 2.480    1.00 43.99  ? 168 TYR C CE1 1 
ATOM   5251  C CE2 . TYR C 1 167 ? 11.344  -28.263 0.151    1.00 66.92  ? 168 TYR C CE2 1 
ATOM   5252  C CZ  . TYR C 1 167 ? 11.077  -27.380 1.175    1.00 64.88  ? 168 TYR C CZ  1 
ATOM   5253  O OH  . TYR C 1 167 ? 10.855  -26.053 0.885    1.00 70.18  ? 168 TYR C OH  1 
ATOM   5254  N N   . ASN C 1 168 ? 8.503   -31.270 1.263    1.00 59.89  ? 169 ASN C N   1 
ATOM   5255  C CA  . ASN C 1 168 ? 7.535   -30.884 0.248    1.00 61.24  ? 169 ASN C CA  1 
ATOM   5256  C C   . ASN C 1 168 ? 7.783   -29.432 -0.143   1.00 57.23  ? 169 ASN C C   1 
ATOM   5257  O O   . ASN C 1 168 ? 7.875   -28.555 0.723    1.00 59.71  ? 169 ASN C O   1 
ATOM   5258  C CB  . ASN C 1 168 ? 6.107   -31.075 0.769    1.00 41.84  ? 169 ASN C CB  1 
ATOM   5259  C CG  . ASN C 1 168 ? 5.034   -30.772 -0.274   1.00 67.73  ? 169 ASN C CG  1 
ATOM   5260  O OD1 . ASN C 1 168 ? 5.312   -30.201 -1.332   1.00 81.84  ? 169 ASN C OD1 1 
ATOM   5261  N ND2 . ASN C 1 168 ? 3.798   -31.153 0.029    1.00 66.86  ? 169 ASN C ND2 1 
ATOM   5262  N N   . ASN C 1 169 ? 7.904   -29.186 -1.449   1.00 59.57  ? 170 ASN C N   1 
ATOM   5263  C CA  . ASN C 1 169 ? 8.130   -27.839 -1.964   1.00 57.57  ? 170 ASN C CA  1 
ATOM   5264  C C   . ASN C 1 169 ? 6.817   -27.084 -1.910   1.00 67.99  ? 170 ASN C C   1 
ATOM   5265  O O   . ASN C 1 169 ? 6.054   -27.054 -2.875   1.00 66.30  ? 170 ASN C O   1 
ATOM   5266  C CB  . ASN C 1 169 ? 8.698   -27.882 -3.377   1.00 56.08  ? 170 ASN C CB  1 
ATOM   5267  C CG  . ASN C 1 169 ? 8.992   -26.497 -3.937   1.00 55.22  ? 170 ASN C CG  1 
ATOM   5268  O OD1 . ASN C 1 169 ? 9.080   -25.518 -3.191   1.00 58.27  ? 170 ASN C OD1 1 
ATOM   5269  N ND2 . ASN C 1 169 ? 9.153   -26.411 -5.252   1.00 63.77  ? 170 ASN C ND2 1 
ATOM   5270  N N   . THR C 1 170 ? 6.552   -26.464 -0.760   1.00 68.62  ? 171 THR C N   1 
ATOM   5271  C CA  . THR C 1 170 ? 5.339   -25.680 -0.568   1.00 74.76  ? 171 THR C CA  1 
ATOM   5272  C C   . THR C 1 170 ? 5.480   -24.254 -1.078   1.00 72.95  ? 171 THR C C   1 
ATOM   5273  O O   . THR C 1 170 ? 4.538   -23.467 -0.940   1.00 86.82  ? 171 THR C O   1 
ATOM   5274  C CB  . THR C 1 170 ? 4.946   -25.670 0.908    1.00 59.53  ? 171 THR C CB  1 
ATOM   5275  O OG1 . THR C 1 170 ? 6.097   -25.381 1.717    1.00 73.66  ? 171 THR C OG1 1 
ATOM   5276  C CG2 . THR C 1 170 ? 4.369   -27.022 1.320    1.00 54.69  ? 171 THR C CG2 1 
ATOM   5277  N N   . ASN C 1 171 ? 6.627   -23.905 -1.657   1.00 59.84  ? 172 ASN C N   1 
ATOM   5278  C CA  . ASN C 1 171 ? 6.797   -22.604 -2.281   1.00 67.67  ? 172 ASN C CA  1 
ATOM   5279  C C   . ASN C 1 171 ? 6.121   -22.587 -3.652   1.00 85.73  ? 172 ASN C C   1 
ATOM   5280  O O   . ASN C 1 171 ? 5.717   -23.621 -4.190   1.00 87.62  ? 172 ASN C O   1 
ATOM   5281  C CB  . ASN C 1 171 ? 8.281   -22.262 -2.415   1.00 66.71  ? 172 ASN C CB  1 
ATOM   5282  C CG  . ASN C 1 171 ? 9.042   -22.461 -1.122   1.00 83.81  ? 172 ASN C CG  1 
ATOM   5283  O OD1 . ASN C 1 171 ? 9.162   -21.542 -0.311   1.00 73.23  ? 172 ASN C OD1 1 
ATOM   5284  N ND2 . ASN C 1 171 ? 9.552   -23.670 -0.915   1.00 65.42  ? 172 ASN C ND2 1 
ATOM   5285  N N   . ARG C 1 172 ? 5.998   -21.389 -4.220   1.00 87.54  ? 173 ARG C N   1 
ATOM   5286  C CA  . ARG C 1 172 ? 5.356   -21.231 -5.519   1.00 72.37  ? 173 ARG C CA  1 
ATOM   5287  C C   . ARG C 1 172 ? 6.308   -21.427 -6.689   1.00 79.63  ? 173 ARG C C   1 
ATOM   5288  O O   . ARG C 1 172 ? 5.857   -21.417 -7.840   1.00 80.39  ? 173 ARG C O   1 
ATOM   5289  C CB  . ARG C 1 172 ? 4.713   -19.844 -5.639   1.00 78.29  ? 173 ARG C CB  1 
ATOM   5290  C CG  . ARG C 1 172 ? 3.903   -19.400 -4.436   1.00 103.32 ? 173 ARG C CG  1 
ATOM   5291  C CD  . ARG C 1 172 ? 2.879   -20.439 -4.016   1.00 100.34 ? 173 ARG C CD  1 
ATOM   5292  N NE  . ARG C 1 172 ? 1.642   -19.811 -3.570   1.00 123.82 ? 173 ARG C NE  1 
ATOM   5293  C CZ  . ARG C 1 172 ? 0.875   -20.273 -2.593   1.00 126.49 ? 173 ARG C CZ  1 
ATOM   5294  N NH1 . ARG C 1 172 ? 1.216   -21.343 -1.892   1.00 110.32 ? 173 ARG C NH1 1 
ATOM   5295  N NH2 . ARG C 1 172 ? -0.261  -19.643 -2.307   1.00 97.57  ? 173 ARG C NH2 1 
ATOM   5296  N N   . GLU C 1 173 ? 7.600   -21.607 -6.431   1.00 76.46  ? 174 GLU C N   1 
ATOM   5297  C CA  . GLU C 1 173 ? 8.612   -21.653 -7.473   1.00 81.35  ? 174 GLU C CA  1 
ATOM   5298  C C   . GLU C 1 173 ? 9.396   -22.958 -7.406   1.00 73.95  ? 174 GLU C C   1 
ATOM   5299  O O   . GLU C 1 173 ? 9.352   -23.687 -6.411   1.00 72.21  ? 174 GLU C O   1 
ATOM   5300  C CB  . GLU C 1 173 ? 9.568   -20.459 -7.355   1.00 68.83  ? 174 GLU C CB  1 
ATOM   5301  C CG  . GLU C 1 173 ? 8.869   -19.116 -7.490   1.00 91.55  ? 174 GLU C CG  1 
ATOM   5302  C CD  . GLU C 1 173 ? 9.549   -18.009 -6.704   1.00 105.16 ? 174 GLU C CD  1 
ATOM   5303  O OE1 . GLU C 1 173 ? 10.274  -18.318 -5.736   1.00 103.16 ? 174 GLU C OE1 1 
ATOM   5304  O OE2 . GLU C 1 173 ? 9.358   -16.826 -7.058   1.00 110.25 ? 174 GLU C OE2 1 
ATOM   5305  N N   . ASP C 1 174 ? 10.115  -23.243 -8.491   1.00 64.00  ? 175 ASP C N   1 
ATOM   5306  C CA  . ASP C 1 174 ? 10.982  -24.411 -8.532   1.00 62.97  ? 175 ASP C CA  1 
ATOM   5307  C C   . ASP C 1 174 ? 12.092  -24.284 -7.495   1.00 65.02  ? 175 ASP C C   1 
ATOM   5308  O O   . ASP C 1 174 ? 12.549  -23.185 -7.168   1.00 68.11  ? 175 ASP C O   1 
ATOM   5309  C CB  . ASP C 1 174 ? 11.585  -24.581 -9.927   1.00 85.33  ? 175 ASP C CB  1 
ATOM   5310  C CG  . ASP C 1 174 ? 10.624  -25.233 -10.903  1.00 79.60  ? 175 ASP C CG  1 
ATOM   5311  O OD1 . ASP C 1 174 ? 9.581   -25.752 -10.455  1.00 83.59  ? 175 ASP C OD1 1 
ATOM   5312  O OD2 . ASP C 1 174 ? 10.915  -25.229 -12.118  1.00 81.03  ? 175 ASP C OD2 1 
ATOM   5313  N N   . LEU C 1 175 ? 12.519  -25.426 -6.966   1.00 55.54  ? 176 LEU C N   1 
ATOM   5314  C CA  . LEU C 1 175 ? 13.524  -25.471 -5.914   1.00 57.47  ? 176 LEU C CA  1 
ATOM   5315  C C   . LEU C 1 175 ? 14.725  -26.265 -6.405   1.00 54.71  ? 176 LEU C C   1 
ATOM   5316  O O   . LEU C 1 175 ? 14.582  -27.419 -6.824   1.00 56.92  ? 176 LEU C O   1 
ATOM   5317  C CB  . LEU C 1 175 ? 12.950  -26.091 -4.640   1.00 56.57  ? 176 LEU C CB  1 
ATOM   5318  C CG  . LEU C 1 175 ? 13.498  -25.517 -3.336   1.00 56.73  ? 176 LEU C CG  1 
ATOM   5319  C CD1 . LEU C 1 175 ? 13.296  -24.012 -3.299   1.00 63.23  ? 176 LEU C CD1 1 
ATOM   5320  C CD2 . LEU C 1 175 ? 12.833  -26.171 -2.143   1.00 57.56  ? 176 LEU C CD2 1 
ATOM   5321  N N   . LEU C 1 176 ? 15.901  -25.647 -6.351   1.00 58.49  ? 177 LEU C N   1 
ATOM   5322  C CA  . LEU C 1 176 ? 17.156  -26.320 -6.658   1.00 54.26  ? 177 LEU C CA  1 
ATOM   5323  C C   . LEU C 1 176 ? 17.732  -26.880 -5.363   1.00 53.92  ? 177 LEU C C   1 
ATOM   5324  O O   . LEU C 1 176 ? 18.065  -26.119 -4.448   1.00 54.68  ? 177 LEU C O   1 
ATOM   5325  C CB  . LEU C 1 176 ? 18.137  -25.355 -7.321   1.00 47.43  ? 177 LEU C CB  1 
ATOM   5326  C CG  . LEU C 1 176 ? 19.567  -25.843 -7.567   1.00 57.04  ? 177 LEU C CG  1 
ATOM   5327  C CD1 . LEU C 1 176 ? 19.580  -27.062 -8.476   1.00 51.46  ? 177 LEU C CD1 1 
ATOM   5328  C CD2 . LEU C 1 176 ? 20.414  -24.725 -8.155   1.00 40.91  ? 177 LEU C CD2 1 
ATOM   5329  N N   . ILE C 1 177 ? 17.843  -28.203 -5.285   1.00 41.52  ? 178 ILE C N   1 
ATOM   5330  C CA  . ILE C 1 177 ? 18.275  -28.896 -4.076   1.00 53.99  ? 178 ILE C CA  1 
ATOM   5331  C C   . ILE C 1 177 ? 19.519  -29.708 -4.401   1.00 53.87  ? 178 ILE C C   1 
ATOM   5332  O O   . ILE C 1 177 ? 19.543  -30.440 -5.396   1.00 58.82  ? 178 ILE C O   1 
ATOM   5333  C CB  . ILE C 1 177 ? 17.162  -29.802 -3.515   1.00 47.30  ? 178 ILE C CB  1 
ATOM   5334  C CG1 . ILE C 1 177 ? 15.936  -28.967 -3.144   1.00 51.34  ? 178 ILE C CG1 1 
ATOM   5335  C CG2 . ILE C 1 177 ? 17.667  -30.589 -2.314   1.00 46.38  ? 178 ILE C CG2 1 
ATOM   5336  C CD1 . ILE C 1 177 ? 14.796  -29.774 -2.553   1.00 60.00  ? 178 ILE C CD1 1 
ATOM   5337  N N   . LEU C 1 178 ? 20.545  -29.580 -3.563   1.00 59.33  ? 179 LEU C N   1 
ATOM   5338  C CA  . LEU C 1 178 ? 21.796  -30.300 -3.742   1.00 51.79  ? 179 LEU C CA  1 
ATOM   5339  C C   . LEU C 1 178 ? 22.064  -31.211 -2.552   1.00 57.48  ? 179 LEU C C   1 
ATOM   5340  O O   . LEU C 1 178 ? 21.700  -30.901 -1.413   1.00 53.65  ? 179 LEU C O   1 
ATOM   5341  C CB  . LEU C 1 178 ? 22.979  -29.340 -3.929   1.00 45.85  ? 179 LEU C CB  1 
ATOM   5342  C CG  . LEU C 1 178 ? 23.012  -28.533 -5.229   1.00 53.33  ? 179 LEU C CG  1 
ATOM   5343  C CD1 . LEU C 1 178 ? 22.343  -27.173 -5.059   1.00 55.75  ? 179 LEU C CD1 1 
ATOM   5344  C CD2 . LEU C 1 178 ? 24.439  -28.382 -5.736   1.00 56.83  ? 179 LEU C CD2 1 
ATOM   5345  N N   . TRP C 1 179 ? 22.708  -32.341 -2.833   1.00 53.89  ? 180 TRP C N   1 
ATOM   5346  C CA  . TRP C 1 179 ? 23.095  -33.305 -1.813   1.00 48.51  ? 180 TRP C CA  1 
ATOM   5347  C C   . TRP C 1 179 ? 24.275  -34.100 -2.353   1.00 49.19  ? 180 TRP C C   1 
ATOM   5348  O O   . TRP C 1 179 ? 24.613  -34.015 -3.535   1.00 57.18  ? 180 TRP C O   1 
ATOM   5349  C CB  . TRP C 1 179 ? 21.930  -34.226 -1.437   1.00 48.29  ? 180 TRP C CB  1 
ATOM   5350  C CG  . TRP C 1 179 ? 21.526  -35.149 -2.541   1.00 50.93  ? 180 TRP C CG  1 
ATOM   5351  C CD1 . TRP C 1 179 ? 21.953  -36.432 -2.735   1.00 51.43  ? 180 TRP C CD1 1 
ATOM   5352  C CD2 . TRP C 1 179 ? 20.617  -34.863 -3.612   1.00 50.62  ? 180 TRP C CD2 1 
ATOM   5353  N NE1 . TRP C 1 179 ? 21.365  -36.962 -3.857   1.00 42.53  ? 180 TRP C NE1 1 
ATOM   5354  C CE2 . TRP C 1 179 ? 20.540  -36.020 -4.414   1.00 49.40  ? 180 TRP C CE2 1 
ATOM   5355  C CE3 . TRP C 1 179 ? 19.861  -33.743 -3.969   1.00 49.86  ? 180 TRP C CE3 1 
ATOM   5356  C CZ2 . TRP C 1 179 ? 19.739  -36.088 -5.551   1.00 53.26  ? 180 TRP C CZ2 1 
ATOM   5357  C CZ3 . TRP C 1 179 ? 19.063  -33.813 -5.100   1.00 51.93  ? 180 TRP C CZ3 1 
ATOM   5358  C CH2 . TRP C 1 179 ? 19.009  -34.978 -5.876   1.00 50.82  ? 180 TRP C CH2 1 
ATOM   5359  N N   . GLY C 1 180 ? 24.905  -34.876 -1.470   1.00 42.56  ? 181 GLY C N   1 
ATOM   5360  C CA  . GLY C 1 180 ? 26.080  -35.625 -1.866   1.00 40.19  ? 181 GLY C CA  1 
ATOM   5361  C C   . GLY C 1 180 ? 26.279  -36.887 -1.056   1.00 43.21  ? 181 GLY C C   1 
ATOM   5362  O O   . GLY C 1 180 ? 25.567  -37.159 -0.086   1.00 41.55  ? 181 GLY C O   1 
ATOM   5363  N N   . ILE C 1 181 ? 27.271  -37.666 -1.485   1.00 42.31  ? 182 ILE C N   1 
ATOM   5364  C CA  . ILE C 1 181 ? 27.707  -38.873 -0.795   1.00 45.45  ? 182 ILE C CA  1 
ATOM   5365  C C   . ILE C 1 181 ? 29.208  -38.770 -0.571   1.00 55.08  ? 182 ILE C C   1 
ATOM   5366  O O   . ILE C 1 181 ? 29.933  -38.228 -1.413   1.00 49.81  ? 182 ILE C O   1 
ATOM   5367  C CB  . ILE C 1 181 ? 27.352  -40.154 -1.586   1.00 41.45  ? 182 ILE C CB  1 
ATOM   5368  C CG1 . ILE C 1 181 ? 27.754  -41.403 -0.797   1.00 47.01  ? 182 ILE C CG1 1 
ATOM   5369  C CG2 . ILE C 1 181 ? 28.005  -40.145 -2.966   1.00 42.70  ? 182 ILE C CG2 1 
ATOM   5370  C CD1 . ILE C 1 181 ? 27.532  -42.702 -1.540   1.00 44.39  ? 182 ILE C CD1 1 
ATOM   5371  N N   . HIS C 1 182 ? 29.672  -39.264 0.573    1.00 51.32  ? 183 HIS C N   1 
ATOM   5372  C CA  . HIS C 1 182 ? 31.087  -39.240 0.918    1.00 47.12  ? 183 HIS C CA  1 
ATOM   5373  C C   . HIS C 1 182 ? 31.685  -40.621 0.682    1.00 55.43  ? 183 HIS C C   1 
ATOM   5374  O O   . HIS C 1 182 ? 31.187  -41.618 1.216    1.00 51.93  ? 183 HIS C O   1 
ATOM   5375  C CB  . HIS C 1 182 ? 31.291  -38.806 2.368    1.00 44.12  ? 183 HIS C CB  1 
ATOM   5376  C CG  . HIS C 1 182 ? 32.691  -38.998 2.860    1.00 52.20  ? 183 HIS C CG  1 
ATOM   5377  N ND1 . HIS C 1 182 ? 33.008  -39.863 3.885    1.00 53.41  ? 183 HIS C ND1 1 
ATOM   5378  C CD2 . HIS C 1 182 ? 33.861  -38.448 2.459    1.00 48.56  ? 183 HIS C CD2 1 
ATOM   5379  C CE1 . HIS C 1 182 ? 34.312  -39.832 4.099    1.00 51.29  ? 183 HIS C CE1 1 
ATOM   5380  N NE2 . HIS C 1 182 ? 34.853  -38.981 3.246    1.00 54.44  ? 183 HIS C NE2 1 
ATOM   5381  N N   . HIS C 1 183 ? 32.745  -40.676 -0.119   1.00 45.17  ? 184 HIS C N   1 
ATOM   5382  C CA  . HIS C 1 183 ? 33.456  -41.920 -0.383   1.00 52.28  ? 184 HIS C CA  1 
ATOM   5383  C C   . HIS C 1 183 ? 34.603  -42.052 0.614    1.00 54.92  ? 184 HIS C C   1 
ATOM   5384  O O   . HIS C 1 183 ? 35.534  -41.238 0.611    1.00 56.23  ? 184 HIS C O   1 
ATOM   5385  C CB  . HIS C 1 183 ? 33.971  -41.956 -1.820   1.00 46.35  ? 184 HIS C CB  1 
ATOM   5386  C CG  . HIS C 1 183 ? 32.888  -41.894 -2.855   1.00 51.72  ? 184 HIS C CG  1 
ATOM   5387  N ND1 . HIS C 1 183 ? 31.975  -42.909 -3.041   1.00 49.22  ? 184 HIS C ND1 1 
ATOM   5388  C CD2 . HIS C 1 183 ? 32.582  -40.942 -3.768   1.00 57.82  ? 184 HIS C CD2 1 
ATOM   5389  C CE1 . HIS C 1 183 ? 31.149  -42.583 -4.019   1.00 53.44  ? 184 HIS C CE1 1 
ATOM   5390  N NE2 . HIS C 1 183 ? 31.496  -41.393 -4.477   1.00 56.28  ? 184 HIS C NE2 1 
ATOM   5391  N N   . SER C 1 184 ? 34.534  -43.074 1.464    1.00 53.48  ? 185 SER C N   1 
ATOM   5392  C CA  . SER C 1 184 ? 35.513  -43.269 2.520    1.00 48.65  ? 185 SER C CA  1 
ATOM   5393  C C   . SER C 1 184 ? 36.802  -43.858 1.949    1.00 51.33  ? 185 SER C C   1 
ATOM   5394  O O   . SER C 1 184 ? 36.903  -44.176 0.761    1.00 63.38  ? 185 SER C O   1 
ATOM   5395  C CB  . SER C 1 184 ? 34.934  -44.165 3.612    1.00 52.64  ? 185 SER C CB  1 
ATOM   5396  O OG  . SER C 1 184 ? 33.603  -43.788 3.918    1.00 62.04  ? 185 SER C OG  1 
ATOM   5397  N N   . ASN C 1 185 ? 37.804  -44.010 2.814    1.00 48.32  ? 186 ASN C N   1 
ATOM   5398  C CA  . ASN C 1 185 ? 39.111  -44.520 2.416    1.00 49.41  ? 186 ASN C CA  1 
ATOM   5399  C C   . ASN C 1 185 ? 39.343  -45.970 2.814    1.00 40.96  ? 186 ASN C C   1 
ATOM   5400  O O   . ASN C 1 185 ? 40.016  -46.701 2.079    1.00 53.39  ? 186 ASN C O   1 
ATOM   5401  C CB  . ASN C 1 185 ? 40.222  -43.653 3.018    1.00 41.09  ? 186 ASN C CB  1 
ATOM   5402  C CG  . ASN C 1 185 ? 40.154  -42.213 2.549    1.00 50.23  ? 186 ASN C CG  1 
ATOM   5403  O OD1 . ASN C 1 185 ? 39.875  -41.939 1.382    1.00 73.33  ? 186 ASN C OD1 1 
ATOM   5404  N ND2 . ASN C 1 185 ? 40.408  -41.284 3.461    1.00 55.44  ? 186 ASN C ND2 1 
ATOM   5405  N N   . ASN C 1 186 ? 38.806  -46.405 3.950    1.00 44.71  ? 187 ASN C N   1 
ATOM   5406  C CA  . ASN C 1 186 ? 38.988  -47.772 4.421    1.00 45.09  ? 187 ASN C CA  1 
ATOM   5407  C C   . ASN C 1 186 ? 37.846  -48.113 5.371    1.00 46.92  ? 187 ASN C C   1 
ATOM   5408  O O   . ASN C 1 186 ? 36.986  -47.278 5.667    1.00 52.23  ? 187 ASN C O   1 
ATOM   5409  C CB  . ASN C 1 186 ? 40.354  -47.956 5.089    1.00 48.49  ? 187 ASN C CB  1 
ATOM   5410  C CG  . ASN C 1 186 ? 40.636  -46.906 6.148    1.00 54.51  ? 187 ASN C CG  1 
ATOM   5411  O OD1 . ASN C 1 186 ? 40.004  -46.887 7.205    1.00 62.37  ? 187 ASN C OD1 1 
ATOM   5412  N ND2 . ASN C 1 186 ? 41.599  -46.033 5.873    1.00 41.00  ? 187 ASN C ND2 1 
ATOM   5413  N N   . ALA C 1 187 ? 37.842  -49.362 5.842    1.00 55.57  ? 188 ALA C N   1 
ATOM   5414  C CA  . ALA C 1 187 ? 36.793  -49.810 6.752    1.00 47.70  ? 188 ALA C CA  1 
ATOM   5415  C C   . ALA C 1 187 ? 36.846  -49.056 8.074    1.00 60.37  ? 188 ALA C C   1 
ATOM   5416  O O   . ALA C 1 187 ? 35.803  -48.726 8.650    1.00 52.83  ? 188 ALA C O   1 
ATOM   5417  C CB  . ALA C 1 187 ? 36.910  -51.316 6.991    1.00 49.00  ? 188 ALA C CB  1 
ATOM   5418  N N   . GLU C 1 188 ? 38.053  -48.784 8.576    1.00 58.39  ? 189 GLU C N   1 
ATOM   5419  C CA  . GLU C 1 188 ? 38.183  -48.109 9.864    1.00 58.93  ? 189 GLU C CA  1 
ATOM   5420  C C   . GLU C 1 188 ? 37.613  -46.696 9.809    1.00 62.99  ? 189 GLU C C   1 
ATOM   5421  O O   . GLU C 1 188 ? 36.891  -46.271 10.718   1.00 59.56  ? 189 GLU C O   1 
ATOM   5422  C CB  . GLU C 1 188 ? 39.648  -48.087 10.297   1.00 72.69  ? 189 GLU C CB  1 
ATOM   5423  C CG  . GLU C 1 188 ? 39.883  -47.409 11.637   1.00 77.40  ? 189 GLU C CG  1 
ATOM   5424  C CD  . GLU C 1 188 ? 39.274  -48.172 12.798   1.00 104.00 ? 189 GLU C CD  1 
ATOM   5425  O OE1 . GLU C 1 188 ? 39.086  -49.402 12.678   1.00 115.12 ? 189 GLU C OE1 1 
ATOM   5426  O OE2 . GLU C 1 188 ? 38.983  -47.539 13.835   1.00 123.80 ? 189 GLU C OE2 1 
ATOM   5427  N N   . GLU C 1 189 ? 37.924  -45.950 8.743    1.00 53.12  ? 190 GLU C N   1 
ATOM   5428  C CA  . GLU C 1 189 ? 37.367  -44.608 8.606    1.00 39.90  ? 190 GLU C CA  1 
ATOM   5429  C C   . GLU C 1 189 ? 35.860  -44.649 8.398    1.00 55.40  ? 190 GLU C C   1 
ATOM   5430  O O   . GLU C 1 189 ? 35.153  -43.722 8.811    1.00 53.48  ? 190 GLU C O   1 
ATOM   5431  C CB  . GLU C 1 189 ? 38.032  -43.866 7.446    1.00 52.65  ? 190 GLU C CB  1 
ATOM   5432  C CG  . GLU C 1 189 ? 37.746  -42.370 7.435    1.00 53.15  ? 190 GLU C CG  1 
ATOM   5433  C CD  . GLU C 1 189 ? 37.958  -41.740 6.072    1.00 72.88  ? 190 GLU C CD  1 
ATOM   5434  O OE1 . GLU C 1 189 ? 37.922  -42.475 5.064    1.00 69.91  ? 190 GLU C OE1 1 
ATOM   5435  O OE2 . GLU C 1 189 ? 38.160  -40.509 6.008    1.00 86.68  ? 190 GLU C OE2 1 
ATOM   5436  N N   . GLN C 1 190 ? 35.357  -45.704 7.754    1.00 49.05  ? 191 GLN C N   1 
ATOM   5437  C CA  . GLN C 1 190 ? 33.922  -45.821 7.528    1.00 52.55  ? 191 GLN C CA  1 
ATOM   5438  C C   . GLN C 1 190 ? 33.165  -45.948 8.845    1.00 50.82  ? 191 GLN C C   1 
ATOM   5439  O O   . GLN C 1 190 ? 32.162  -45.259 9.068    1.00 57.22  ? 191 GLN C O   1 
ATOM   5440  C CB  . GLN C 1 190 ? 33.635  -47.017 6.620    1.00 50.18  ? 191 GLN C CB  1 
ATOM   5441  C CG  . GLN C 1 190 ? 32.158  -47.304 6.410    1.00 40.34  ? 191 GLN C CG  1 
ATOM   5442  C CD  . GLN C 1 190 ? 31.437  -46.187 5.682    1.00 40.79  ? 191 GLN C CD  1 
ATOM   5443  O OE1 . GLN C 1 190 ? 32.059  -45.349 5.029    1.00 55.20  ? 191 GLN C OE1 1 
ATOM   5444  N NE2 . GLN C 1 190 ? 30.113  -46.172 5.787    1.00 44.58  ? 191 GLN C NE2 1 
ATOM   5445  N N   . THR C 1 191 ? 33.634  -46.824 9.736    1.00 55.80  ? 192 THR C N   1 
ATOM   5446  C CA  . THR C 1 191 ? 32.964  -47.022 11.015   1.00 59.34  ? 192 THR C CA  1 
ATOM   5447  C C   . THR C 1 191 ? 33.274  -45.923 12.022   1.00 50.24  ? 192 THR C C   1 
ATOM   5448  O O   . THR C 1 191 ? 32.498  -45.728 12.963   1.00 56.30  ? 192 THR C O   1 
ATOM   5449  C CB  . THR C 1 191 ? 33.339  -48.382 11.609   1.00 55.01  ? 192 THR C CB  1 
ATOM   5450  O OG1 . THR C 1 191 ? 34.759  -48.455 11.786   1.00 53.79  ? 192 THR C OG1 1 
ATOM   5451  C CG2 . THR C 1 191 ? 32.884  -49.508 10.689   1.00 51.58  ? 192 THR C CG2 1 
ATOM   5452  N N   . ASN C 1 192 ? 34.389  -45.208 11.861   1.00 49.72  ? 193 ASN C N   1 
ATOM   5453  C CA  . ASN C 1 192 ? 34.654  -44.064 12.727   1.00 50.37  ? 193 ASN C CA  1 
ATOM   5454  C C   . ASN C 1 192 ? 33.627  -42.962 12.499   1.00 53.55  ? 193 ASN C C   1 
ATOM   5455  O O   . ASN C 1 192 ? 33.030  -42.444 13.449   1.00 66.44  ? 193 ASN C O   1 
ATOM   5456  C CB  . ASN C 1 192 ? 36.070  -43.538 12.489   1.00 56.83  ? 193 ASN C CB  1 
ATOM   5457  C CG  . ASN C 1 192 ? 37.129  -44.372 13.183   1.00 50.45  ? 193 ASN C CG  1 
ATOM   5458  O OD1 . ASN C 1 192 ? 36.834  -45.422 13.755   1.00 55.13  ? 193 ASN C OD1 1 
ATOM   5459  N ND2 . ASN C 1 192 ? 38.372  -43.908 13.133   1.00 51.02  ? 193 ASN C ND2 1 
ATOM   5460  N N   . LEU C 1 193 ? 33.398  -42.602 11.236   1.00 58.19  ? 194 LEU C N   1 
ATOM   5461  C CA  . LEU C 1 193 ? 32.485  -41.510 10.922   1.00 45.98  ? 194 LEU C CA  1 
ATOM   5462  C C   . LEU C 1 193 ? 31.024  -41.927 11.052   1.00 49.56  ? 194 LEU C C   1 
ATOM   5463  O O   . LEU C 1 193 ? 30.184  -41.125 11.474   1.00 41.00  ? 194 LEU C O   1 
ATOM   5464  C CB  . LEU C 1 193 ? 32.765  -40.992 9.512    1.00 50.64  ? 194 LEU C CB  1 
ATOM   5465  C CG  . LEU C 1 193 ? 34.187  -40.496 9.240    1.00 51.50  ? 194 LEU C CG  1 
ATOM   5466  C CD1 . LEU C 1 193 ? 34.399  -40.279 7.752    1.00 36.88  ? 194 LEU C CD1 1 
ATOM   5467  C CD2 . LEU C 1 193 ? 34.471  -39.216 10.015   1.00 49.24  ? 194 LEU C CD2 1 
ATOM   5468  N N   . TYR C 1 194 ? 30.698  -43.173 10.702   1.00 49.03  ? 195 TYR C N   1 
ATOM   5469  C CA  . TYR C 1 194 ? 29.305  -43.575 10.549   1.00 41.97  ? 195 TYR C CA  1 
ATOM   5470  C C   . TYR C 1 194 ? 28.912  -44.844 11.293   1.00 58.07  ? 195 TYR C C   1 
ATOM   5471  O O   . TYR C 1 194 ? 27.709  -45.101 11.415   1.00 50.08  ? 195 TYR C O   1 
ATOM   5472  C CB  . TYR C 1 194 ? 28.969  -43.757 9.060    1.00 39.82  ? 195 TYR C CB  1 
ATOM   5473  C CG  . TYR C 1 194 ? 29.523  -42.661 8.176    1.00 39.11  ? 195 TYR C CG  1 
ATOM   5474  C CD1 . TYR C 1 194 ? 29.002  -41.373 8.223    1.00 40.25  ? 195 TYR C CD1 1 
ATOM   5475  C CD2 . TYR C 1 194 ? 30.567  -42.914 7.295    1.00 46.24  ? 195 TYR C CD2 1 
ATOM   5476  C CE1 . TYR C 1 194 ? 29.508  -40.367 7.417    1.00 36.27  ? 195 TYR C CE1 1 
ATOM   5477  C CE2 . TYR C 1 194 ? 31.077  -41.916 6.488    1.00 52.14  ? 195 TYR C CE2 1 
ATOM   5478  C CZ  . TYR C 1 194 ? 30.544  -40.646 6.552    1.00 43.78  ? 195 TYR C CZ  1 
ATOM   5479  O OH  . TYR C 1 194 ? 31.054  -39.654 5.747    1.00 44.67  ? 195 TYR C OH  1 
ATOM   5480  N N   . LYS C 1 195 ? 29.867  -45.671 11.731   1.00 59.05  ? 196 LYS C N   1 
ATOM   5481  C CA  . LYS C 1 195 ? 29.612  -46.848 12.564   1.00 53.91  ? 196 LYS C CA  1 
ATOM   5482  C C   . LYS C 1 195 ? 28.940  -47.965 11.768   1.00 48.82  ? 196 LYS C C   1 
ATOM   5483  O O   . LYS C 1 195 ? 28.881  -49.115 12.217   1.00 78.31  ? 196 LYS C O   1 
ATOM   5484  C CB  . LYS C 1 195 ? 28.778  -46.444 13.792   1.00 59.64  ? 196 LYS C CB  1 
ATOM   5485  C CG  . LYS C 1 195 ? 28.164  -47.567 14.624   1.00 56.69  ? 196 LYS C CG  1 
ATOM   5486  C CD  . LYS C 1 195 ? 29.215  -48.458 15.262   1.00 64.58  ? 196 LYS C CD  1 
ATOM   5487  C CE  . LYS C 1 195 ? 28.679  -49.099 16.532   1.00 69.07  ? 196 LYS C CE  1 
ATOM   5488  N NZ  . LYS C 1 195 ? 27.187  -49.146 16.549   1.00 96.71  ? 196 LYS C NZ  1 
ATOM   5489  N N   . ASN C 1 196 ? 28.506  -47.658 10.548   1.00 63.69  ? 197 ASN C N   1 
ATOM   5490  C CA  . ASN C 1 196 ? 27.843  -48.634 9.696    1.00 44.08  ? 197 ASN C CA  1 
ATOM   5491  C C   . ASN C 1 196 ? 28.759  -48.994 8.538    1.00 43.61  ? 197 ASN C C   1 
ATOM   5492  O O   . ASN C 1 196 ? 29.078  -48.120 7.717    1.00 54.03  ? 197 ASN C O   1 
ATOM   5493  C CB  . ASN C 1 196 ? 26.511  -48.089 9.180    1.00 60.38  ? 197 ASN C CB  1 
ATOM   5494  C CG  . ASN C 1 196 ? 25.502  -47.858 10.294   1.00 52.10  ? 197 ASN C CG  1 
ATOM   5495  O OD1 . ASN C 1 196 ? 25.431  -48.626 11.253   1.00 59.98  ? 197 ASN C OD1 1 
ATOM   5496  N ND2 . ASN C 1 196 ? 24.716  -46.794 10.169   1.00 46.18  ? 197 ASN C ND2 1 
ATOM   5497  N N   . PRO C 1 197 ? 29.208  -50.246 8.431    1.00 54.25  ? 198 PRO C N   1 
ATOM   5498  C CA  . PRO C 1 197 ? 30.164  -50.604 7.373    1.00 51.91  ? 198 PRO C CA  1 
ATOM   5499  C C   . PRO C 1 197 ? 29.585  -50.500 5.972    1.00 52.77  ? 198 PRO C C   1 
ATOM   5500  O O   . PRO C 1 197 ? 30.229  -49.952 5.072    1.00 70.81  ? 198 PRO C O   1 
ATOM   5501  C CB  . PRO C 1 197 ? 30.540  -52.052 7.718    1.00 53.69  ? 198 PRO C CB  1 
ATOM   5502  C CG  . PRO C 1 197 ? 29.407  -52.561 8.555    1.00 49.92  ? 198 PRO C CG  1 
ATOM   5503  C CD  . PRO C 1 197 ? 28.906  -51.379 9.323    1.00 36.32  ? 198 PRO C CD  1 
ATOM   5504  N N   . THR C 1 198 ? 28.378  -51.022 5.772    1.00 48.76  ? 199 THR C N   1 
ATOM   5505  C CA  . THR C 1 198 ? 27.710  -51.003 4.475    1.00 56.94  ? 199 THR C CA  1 
ATOM   5506  C C   . THR C 1 198 ? 26.558  -50.011 4.537    1.00 48.92  ? 199 THR C C   1 
ATOM   5507  O O   . THR C 1 198 ? 25.627  -50.183 5.330    1.00 57.97  ? 199 THR C O   1 
ATOM   5508  C CB  . THR C 1 198 ? 27.202  -52.393 4.089    1.00 54.58  ? 199 THR C CB  1 
ATOM   5509  O OG1 . THR C 1 198 ? 26.150  -52.784 4.980    1.00 85.55  ? 199 THR C OG1 1 
ATOM   5510  C CG2 . THR C 1 198 ? 28.331  -53.413 4.173    1.00 67.16  ? 199 THR C CG2 1 
ATOM   5511  N N   . THR C 1 199 ? 26.618  -48.981 3.695    1.00 46.93  ? 200 THR C N   1 
ATOM   5512  C CA  . THR C 1 199 ? 25.666  -47.881 3.732    1.00 49.82  ? 200 THR C CA  1 
ATOM   5513  C C   . THR C 1 199 ? 25.111  -47.614 2.339    1.00 50.60  ? 200 THR C C   1 
ATOM   5514  O O   . THR C 1 199 ? 25.562  -48.180 1.339    1.00 57.17  ? 200 THR C O   1 
ATOM   5515  C CB  . THR C 1 199 ? 26.307  -46.604 4.293    1.00 51.64  ? 200 THR C CB  1 
ATOM   5516  O OG1 . THR C 1 199 ? 27.481  -46.282 3.537    1.00 53.61  ? 200 THR C OG1 1 
ATOM   5517  C CG2 . THR C 1 199 ? 26.685  -46.792 5.752    1.00 45.16  ? 200 THR C CG2 1 
ATOM   5518  N N   . TYR C 1 200 ? 24.119  -46.728 2.293    1.00 43.98  ? 201 TYR C N   1 
ATOM   5519  C CA  . TYR C 1 200 ? 23.436  -46.367 1.060    1.00 50.12  ? 201 TYR C CA  1 
ATOM   5520  C C   . TYR C 1 200 ? 22.774  -45.011 1.251    1.00 45.49  ? 201 TYR C C   1 
ATOM   5521  O O   . TYR C 1 200 ? 22.600  -44.539 2.377    1.00 54.29  ? 201 TYR C O   1 
ATOM   5522  C CB  . TYR C 1 200 ? 22.386  -47.414 0.671    1.00 46.70  ? 201 TYR C CB  1 
ATOM   5523  C CG  . TYR C 1 200 ? 21.214  -47.461 1.628    1.00 50.33  ? 201 TYR C CG  1 
ATOM   5524  C CD1 . TYR C 1 200 ? 21.260  -48.250 2.768    1.00 55.02  ? 201 TYR C CD1 1 
ATOM   5525  C CD2 . TYR C 1 200 ? 20.066  -46.710 1.395    1.00 47.81  ? 201 TYR C CD2 1 
ATOM   5526  C CE1 . TYR C 1 200 ? 20.198  -48.294 3.651    1.00 57.92  ? 201 TYR C CE1 1 
ATOM   5527  C CE2 . TYR C 1 200 ? 18.999  -46.746 2.273    1.00 61.16  ? 201 TYR C CE2 1 
ATOM   5528  C CZ  . TYR C 1 200 ? 19.070  -47.541 3.398    1.00 51.39  ? 201 TYR C CZ  1 
ATOM   5529  O OH  . TYR C 1 200 ? 18.009  -47.583 4.274    1.00 70.14  ? 201 TYR C OH  1 
ATOM   5530  N N   . ILE C 1 201 ? 22.405  -44.390 0.134    1.00 51.01  ? 202 ILE C N   1 
ATOM   5531  C CA  . ILE C 1 201 ? 21.562  -43.200 0.132    1.00 40.37  ? 202 ILE C CA  1 
ATOM   5532  C C   . ILE C 1 201 ? 20.458  -43.406 -0.893   1.00 55.42  ? 202 ILE C C   1 
ATOM   5533  O O   . ILE C 1 201 ? 20.738  -43.691 -2.063   1.00 57.85  ? 202 ILE C O   1 
ATOM   5534  C CB  . ILE C 1 201 ? 22.356  -41.920 -0.188   1.00 46.30  ? 202 ILE C CB  1 
ATOM   5535  C CG1 . ILE C 1 201 ? 23.492  -41.728 0.816    1.00 52.17  ? 202 ILE C CG1 1 
ATOM   5536  C CG2 . ILE C 1 201 ? 21.433  -40.712 -0.178   1.00 31.77  ? 202 ILE C CG2 1 
ATOM   5537  C CD1 . ILE C 1 201 ? 24.374  -40.543 0.505    1.00 45.46  ? 202 ILE C CD1 1 
ATOM   5538  N N   . SER C 1 202 ? 19.210  -43.263 -0.458   1.00 58.75  ? 203 SER C N   1 
ATOM   5539  C CA  . SER C 1 202 ? 18.052  -43.344 -1.338   1.00 48.73  ? 203 SER C CA  1 
ATOM   5540  C C   . SER C 1 202 ? 17.462  -41.949 -1.491   1.00 49.42  ? 203 SER C C   1 
ATOM   5541  O O   . SER C 1 202 ? 17.111  -41.307 -0.495   1.00 50.04  ? 203 SER C O   1 
ATOM   5542  C CB  . SER C 1 202 ? 17.004  -44.315 -0.790   1.00 45.61  ? 203 SER C CB  1 
ATOM   5543  O OG  . SER C 1 202 ? 17.507  -45.639 -0.737   1.00 73.62  ? 203 SER C OG  1 
ATOM   5544  N N   . VAL C 1 203 ? 17.368  -41.481 -2.733   1.00 38.42  ? 204 VAL C N   1 
ATOM   5545  C CA  . VAL C 1 203 ? 16.761  -40.196 -3.055   1.00 42.08  ? 204 VAL C CA  1 
ATOM   5546  C C   . VAL C 1 203 ? 15.616  -40.447 -4.023   1.00 47.85  ? 204 VAL C C   1 
ATOM   5547  O O   . VAL C 1 203 ? 15.785  -41.154 -5.023   1.00 55.83  ? 204 VAL C O   1 
ATOM   5548  C CB  . VAL C 1 203 ? 17.779  -39.210 -3.655   1.00 49.66  ? 204 VAL C CB  1 
ATOM   5549  C CG1 . VAL C 1 203 ? 17.121  -37.863 -3.915   1.00 48.96  ? 204 VAL C CG1 1 
ATOM   5550  C CG2 . VAL C 1 203 ? 18.974  -39.053 -2.730   1.00 53.65  ? 204 VAL C CG2 1 
ATOM   5551  N N   . GLY C 1 204 ? 14.457  -39.875 -3.722   1.00 55.92  ? 205 GLY C N   1 
ATOM   5552  C CA  . GLY C 1 204 ? 13.297  -40.076 -4.561   1.00 53.65  ? 205 GLY C CA  1 
ATOM   5553  C C   . GLY C 1 204 ? 12.383  -38.870 -4.673   1.00 57.48  ? 205 GLY C C   1 
ATOM   5554  O O   . GLY C 1 204 ? 12.011  -38.256 -3.670   1.00 62.64  ? 205 GLY C O   1 
ATOM   5555  N N   . THR C 1 205 ? 12.022  -38.530 -5.903   1.00 62.68  ? 206 THR C N   1 
ATOM   5556  C CA  . THR C 1 205 ? 10.996  -37.552 -6.210   1.00 65.61  ? 206 THR C CA  1 
ATOM   5557  C C   . THR C 1 205 ? 9.970   -38.223 -7.123   1.00 74.02  ? 206 THR C C   1 
ATOM   5558  O O   . THR C 1 205 ? 10.008  -39.446 -7.344   1.00 79.80  ? 206 THR C O   1 
ATOM   5559  C CB  . THR C 1 205 ? 11.589  -36.297 -6.867   1.00 59.99  ? 206 THR C CB  1 
ATOM   5560  O OG1 . THR C 1 205 ? 11.942  -36.590 -8.232   1.00 76.52  ? 206 THR C OG1 1 
ATOM   5561  C CG2 . THR C 1 205 ? 12.813  -35.832 -6.121   1.00 53.15  ? 206 THR C CG2 1 
ATOM   5562  N N   . SER C 1 206 ? 9.037   -37.431 -7.652   1.00 73.07  ? 207 SER C N   1 
ATOM   5563  C CA  . SER C 1 206 ? 8.111   -37.952 -8.652   1.00 72.61  ? 207 SER C CA  1 
ATOM   5564  C C   . SER C 1 206 ? 8.826   -38.333 -9.945   1.00 70.42  ? 207 SER C C   1 
ATOM   5565  O O   . SER C 1 206 ? 8.319   -39.169 -10.703  1.00 86.39  ? 207 SER C O   1 
ATOM   5566  C CB  . SER C 1 206 ? 7.010   -36.929 -8.938   1.00 60.73  ? 207 SER C CB  1 
ATOM   5567  O OG  . SER C 1 206 ? 7.543   -35.779 -9.576   1.00 65.42  ? 207 SER C OG  1 
ATOM   5568  N N   . THR C 1 207 ? 9.998   -37.751 -10.205  1.00 68.40  ? 208 THR C N   1 
ATOM   5569  C CA  . THR C 1 207 ? 10.753  -38.009 -11.422  1.00 71.24  ? 208 THR C CA  1 
ATOM   5570  C C   . THR C 1 207 ? 12.100  -38.678 -11.183  1.00 73.31  ? 208 THR C C   1 
ATOM   5571  O O   . THR C 1 207 ? 12.729  -39.119 -12.152  1.00 74.77  ? 208 THR C O   1 
ATOM   5572  C CB  . THR C 1 207 ? 10.996  -36.701 -12.190  1.00 62.53  ? 208 THR C CB  1 
ATOM   5573  O OG1 . THR C 1 207 ? 12.194  -36.078 -11.706  1.00 71.27  ? 208 THR C OG1 1 
ATOM   5574  C CG2 . THR C 1 207 ? 9.832   -35.743 -11.997  1.00 69.75  ? 208 THR C CG2 1 
ATOM   5575  N N   . LEU C 1 208 ? 12.557  -38.769 -9.936   1.00 65.75  ? 209 LEU C N   1 
ATOM   5576  C CA  . LEU C 1 208 ? 13.891  -39.250 -9.606   1.00 48.46  ? 209 LEU C CA  1 
ATOM   5577  C C   . LEU C 1 208 ? 13.801  -40.481 -8.716   1.00 62.18  ? 209 LEU C C   1 
ATOM   5578  O O   . LEU C 1 208 ? 12.985  -40.534 -7.790   1.00 61.57  ? 209 LEU C O   1 
ATOM   5579  C CB  . LEU C 1 208 ? 14.705  -38.153 -8.905   1.00 53.04  ? 209 LEU C CB  1 
ATOM   5580  C CG  . LEU C 1 208 ? 16.089  -38.502 -8.351   1.00 61.47  ? 209 LEU C CG  1 
ATOM   5581  C CD1 . LEU C 1 208 ? 17.045  -38.918 -9.460   1.00 56.47  ? 209 LEU C CD1 1 
ATOM   5582  C CD2 . LEU C 1 208 ? 16.650  -37.326 -7.565   1.00 48.89  ? 209 LEU C CD2 1 
ATOM   5583  N N   . ASN C 1 209 ? 14.647  -41.471 -9.008   1.00 57.11  ? 210 ASN C N   1 
ATOM   5584  C CA  . ASN C 1 209 ? 14.742  -42.706 -8.223   1.00 40.12  ? 210 ASN C CA  1 
ATOM   5585  C C   . ASN C 1 209 ? 16.218  -43.104 -8.224   1.00 58.81  ? 210 ASN C C   1 
ATOM   5586  O O   . ASN C 1 209 ? 16.692  -43.780 -9.144   1.00 63.31  ? 210 ASN C O   1 
ATOM   5587  C CB  . ASN C 1 209 ? 13.855  -43.802 -8.794   1.00 41.87  ? 210 ASN C CB  1 
ATOM   5588  C CG  . ASN C 1 209 ? 13.580  -44.908 -7.797   1.00 79.91  ? 210 ASN C CG  1 
ATOM   5589  O OD1 . ASN C 1 209 ? 13.437  -44.658 -6.600   1.00 92.26  ? 210 ASN C OD1 1 
ATOM   5590  N ND2 . ASN C 1 209 ? 13.506  -46.142 -8.285   1.00 82.74  ? 210 ASN C ND2 1 
ATOM   5591  N N   . GLN C 1 210 ? 16.934  -42.698 -7.178   1.00 63.07  ? 211 GLN C N   1 
ATOM   5592  C CA  . GLN C 1 210 ? 18.387  -42.780 -7.122   1.00 39.46  ? 211 GLN C CA  1 
ATOM   5593  C C   . GLN C 1 210 ? 18.828  -43.598 -5.916   1.00 47.35  ? 211 GLN C C   1 
ATOM   5594  O O   . GLN C 1 210 ? 18.255  -43.478 -4.829   1.00 47.37  ? 211 GLN C O   1 
ATOM   5595  C CB  . GLN C 1 210 ? 18.995  -41.375 -7.050   1.00 32.07  ? 211 GLN C CB  1 
ATOM   5596  C CG  . GLN C 1 210 ? 20.506  -41.326 -6.927   1.00 41.74  ? 211 GLN C CG  1 
ATOM   5597  C CD  . GLN C 1 210 ? 21.014  -39.913 -6.713   1.00 68.11  ? 211 GLN C CD  1 
ATOM   5598  O OE1 . GLN C 1 210 ? 20.668  -39.259 -5.728   1.00 66.93  ? 211 GLN C OE1 1 
ATOM   5599  N NE2 . GLN C 1 210 ? 21.828  -39.429 -7.643   1.00 62.99  ? 211 GLN C NE2 1 
ATOM   5600  N N   . ARG C 1 211 ? 19.852  -44.428 -6.112   1.00 53.52  ? 212 ARG C N   1 
ATOM   5601  C CA  . ARG C 1 211 ? 20.470  -45.169 -5.019   1.00 46.08  ? 212 ARG C CA  1 
ATOM   5602  C C   . ARG C 1 211 ? 21.981  -45.084 -5.168   1.00 46.90  ? 212 ARG C C   1 
ATOM   5603  O O   . ARG C 1 211 ? 22.526  -45.464 -6.209   1.00 55.75  ? 212 ARG C O   1 
ATOM   5604  C CB  . ARG C 1 211 ? 20.012  -46.630 -4.995   1.00 36.95  ? 212 ARG C CB  1 
ATOM   5605  C CG  . ARG C 1 211 ? 20.548  -47.407 -3.803   1.00 51.81  ? 212 ARG C CG  1 
ATOM   5606  C CD  . ARG C 1 211 ? 19.872  -48.757 -3.652   1.00 59.08  ? 212 ARG C CD  1 
ATOM   5607  N NE  . ARG C 1 211 ? 19.886  -49.206 -2.265   1.00 65.78  ? 212 ARG C NE  1 
ATOM   5608  C CZ  . ARG C 1 211 ? 20.861  -49.916 -1.713   1.00 74.50  ? 212 ARG C CZ  1 
ATOM   5609  N NH1 . ARG C 1 211 ? 21.919  -50.297 -2.411   1.00 47.11  ? 212 ARG C NH1 1 
ATOM   5610  N NH2 . ARG C 1 211 ? 20.773  -50.251 -0.429   1.00 68.74  ? 212 ARG C NH2 1 
ATOM   5611  N N   . LEU C 1 212 ? 22.651  -44.592 -4.129   1.00 53.44  ? 213 LEU C N   1 
ATOM   5612  C CA  . LEU C 1 212 ? 24.091  -44.382 -4.135   1.00 44.55  ? 213 LEU C CA  1 
ATOM   5613  C C   . LEU C 1 212 ? 24.738  -45.241 -3.058   1.00 49.36  ? 213 LEU C C   1 
ATOM   5614  O O   . LEU C 1 212 ? 24.180  -45.410 -1.969   1.00 57.16  ? 213 LEU C O   1 
ATOM   5615  C CB  . LEU C 1 212 ? 24.427  -42.907 -3.901   1.00 44.90  ? 213 LEU C CB  1 
ATOM   5616  C CG  . LEU C 1 212 ? 23.657  -41.905 -4.764   1.00 65.50  ? 213 LEU C CG  1 
ATOM   5617  C CD1 . LEU C 1 212 ? 23.797  -40.503 -4.199   1.00 53.69  ? 213 LEU C CD1 1 
ATOM   5618  C CD2 . LEU C 1 212 ? 24.135  -41.953 -6.207   1.00 36.97  ? 213 LEU C CD2 1 
ATOM   5619  N N   . VAL C 1 213 ? 25.911  -45.786 -3.369   1.00 45.81  ? 214 VAL C N   1 
ATOM   5620  C CA  . VAL C 1 213 ? 26.666  -46.618 -2.433   1.00 48.38  ? 214 VAL C CA  1 
ATOM   5621  C C   . VAL C 1 213 ? 28.121  -46.163 -2.439   1.00 40.05  ? 214 VAL C C   1 
ATOM   5622  O O   . VAL C 1 213 ? 28.711  -45.992 -3.517   1.00 56.54  ? 214 VAL C O   1 
ATOM   5623  C CB  . VAL C 1 213 ? 26.542  -48.110 -2.786   1.00 40.68  ? 214 VAL C CB  1 
ATOM   5624  C CG1 . VAL C 1 213 ? 27.499  -48.941 -1.946   1.00 39.59  ? 214 VAL C CG1 1 
ATOM   5625  C CG2 . VAL C 1 213 ? 25.110  -48.586 -2.582   1.00 38.15  ? 214 VAL C CG2 1 
ATOM   5626  N N   . PRO C 1 214 ? 28.731  -45.944 -1.274   1.00 58.21  ? 215 PRO C N   1 
ATOM   5627  C CA  . PRO C 1 214 ? 30.111  -45.443 -1.242   1.00 51.10  ? 215 PRO C CA  1 
ATOM   5628  C C   . PRO C 1 214 ? 31.089  -46.406 -1.902   1.00 50.53  ? 215 PRO C C   1 
ATOM   5629  O O   . PRO C 1 214 ? 30.952  -47.627 -1.809   1.00 49.85  ? 215 PRO C O   1 
ATOM   5630  C CB  . PRO C 1 214 ? 30.398  -45.295 0.256    1.00 48.04  ? 215 PRO C CB  1 
ATOM   5631  C CG  . PRO C 1 214 ? 29.055  -45.209 0.899    1.00 51.82  ? 215 PRO C CG  1 
ATOM   5632  C CD  . PRO C 1 214 ? 28.158  -46.074 0.075    1.00 56.52  ? 215 PRO C CD  1 
ATOM   5633  N N   . LYS C 1 215 ? 32.086  -45.836 -2.577   1.00 44.90  ? 216 LYS C N   1 
ATOM   5634  C CA  . LYS C 1 215 ? 33.178  -46.604 -3.174   1.00 53.98  ? 216 LYS C CA  1 
ATOM   5635  C C   . LYS C 1 215 ? 34.395  -46.440 -2.270   1.00 46.04  ? 216 LYS C C   1 
ATOM   5636  O O   . LYS C 1 215 ? 35.216  -45.541 -2.454   1.00 60.63  ? 216 LYS C O   1 
ATOM   5637  C CB  . LYS C 1 215 ? 33.471  -46.141 -4.596   1.00 37.70  ? 216 LYS C CB  1 
ATOM   5638  C CG  . LYS C 1 215 ? 32.285  -46.198 -5.542   1.00 57.99  ? 216 LYS C CG  1 
ATOM   5639  C CD  . LYS C 1 215 ? 32.703  -45.753 -6.931   1.00 52.97  ? 216 LYS C CD  1 
ATOM   5640  C CE  . LYS C 1 215 ? 31.555  -45.100 -7.676   1.00 46.03  ? 216 LYS C CE  1 
ATOM   5641  N NZ  . LYS C 1 215 ? 31.997  -43.829 -8.317   1.00 54.02  ? 216 LYS C NZ  1 
ATOM   5642  N N   . ILE C 1 216 ? 34.509  -47.323 -1.284   1.00 49.18  ? 217 ILE C N   1 
ATOM   5643  C CA  . ILE C 1 216 ? 35.612  -47.277 -0.330   1.00 48.54  ? 217 ILE C CA  1 
ATOM   5644  C C   . ILE C 1 216 ? 36.828  -47.922 -0.987   1.00 47.71  ? 217 ILE C C   1 
ATOM   5645  O O   . ILE C 1 216 ? 36.880  -49.143 -1.147   1.00 58.21  ? 217 ILE C O   1 
ATOM   5646  C CB  . ILE C 1 216 ? 35.246  -47.982 0.980    1.00 44.49  ? 217 ILE C CB  1 
ATOM   5647  C CG1 . ILE C 1 216 ? 34.047  -47.285 1.626    1.00 43.55  ? 217 ILE C CG1 1 
ATOM   5648  C CG2 . ILE C 1 216 ? 36.435  -48.006 1.922    1.00 51.43  ? 217 ILE C CG2 1 
ATOM   5649  C CD1 . ILE C 1 216 ? 33.433  -48.043 2.785    1.00 56.84  ? 217 ILE C CD1 1 
ATOM   5650  N N   . ALA C 1 217 ? 37.809  -47.104 -1.362   1.00 58.47  ? 218 ALA C N   1 
ATOM   5651  C CA  . ALA C 1 217 ? 38.967  -47.585 -2.105   1.00 47.98  ? 218 ALA C CA  1 
ATOM   5652  C C   . ALA C 1 217 ? 40.116  -46.605 -1.913   1.00 54.64  ? 218 ALA C C   1 
ATOM   5653  O O   . ALA C 1 217 ? 39.943  -45.509 -1.376   1.00 59.47  ? 218 ALA C O   1 
ATOM   5654  C CB  . ALA C 1 217 ? 38.640  -47.764 -3.590   1.00 42.95  ? 218 ALA C CB  1 
ATOM   5655  N N   . THR C 1 218 ? 41.299  -47.023 -2.361   1.00 53.83  ? 219 THR C N   1 
ATOM   5656  C CA  . THR C 1 218 ? 42.515  -46.226 -2.240   1.00 62.37  ? 219 THR C CA  1 
ATOM   5657  C C   . THR C 1 218 ? 42.628  -45.289 -3.437   1.00 53.41  ? 219 THR C C   1 
ATOM   5658  O O   . THR C 1 218 ? 42.592  -45.737 -4.588   1.00 68.71  ? 219 THR C O   1 
ATOM   5659  C CB  . THR C 1 218 ? 43.745  -47.127 -2.147   1.00 59.49  ? 219 THR C CB  1 
ATOM   5660  O OG1 . THR C 1 218 ? 43.639  -47.962 -0.986   1.00 58.13  ? 219 THR C OG1 1 
ATOM   5661  C CG2 . THR C 1 218 ? 45.015  -46.291 -2.051   1.00 65.47  ? 219 THR C CG2 1 
ATOM   5662  N N   . ARG C 1 219 ? 42.766  -43.992 -3.164   1.00 53.68  ? 220 ARG C N   1 
ATOM   5663  C CA  . ARG C 1 219 ? 42.856  -42.971 -4.197   1.00 58.95  ? 220 ARG C CA  1 
ATOM   5664  C C   . ARG C 1 219 ? 44.044  -42.061 -3.922   1.00 67.91  ? 220 ARG C C   1 
ATOM   5665  O O   . ARG C 1 219 ? 44.624  -42.062 -2.833   1.00 61.66  ? 220 ARG C O   1 
ATOM   5666  C CB  . ARG C 1 219 ? 41.574  -42.131 -4.276   1.00 55.59  ? 220 ARG C CB  1 
ATOM   5667  C CG  . ARG C 1 219 ? 40.305  -42.944 -4.386   1.00 61.40  ? 220 ARG C CG  1 
ATOM   5668  C CD  . ARG C 1 219 ? 39.083  -42.063 -4.233   1.00 66.00  ? 220 ARG C CD  1 
ATOM   5669  N NE  . ARG C 1 219 ? 37.949  -42.822 -3.723   1.00 70.02  ? 220 ARG C NE  1 
ATOM   5670  C CZ  . ARG C 1 219 ? 37.714  -43.034 -2.436   1.00 48.27  ? 220 ARG C CZ  1 
ATOM   5671  N NH1 . ARG C 1 219 ? 38.505  -42.539 -1.500   1.00 61.63  ? 220 ARG C NH1 1 
ATOM   5672  N NH2 . ARG C 1 219 ? 36.661  -43.763 -2.080   1.00 68.71  ? 220 ARG C NH2 1 
ATOM   5673  N N   . SER C 1 220 ? 44.400  -41.276 -4.935   1.00 79.91  ? 221 SER C N   1 
ATOM   5674  C CA  . SER C 1 220 ? 45.459  -40.290 -4.791   1.00 62.76  ? 221 SER C CA  1 
ATOM   5675  C C   . SER C 1 220 ? 44.984  -39.116 -3.943   1.00 61.44  ? 221 SER C C   1 
ATOM   5676  O O   . SER C 1 220 ? 43.801  -38.763 -3.935   1.00 63.60  ? 221 SER C O   1 
ATOM   5677  C CB  . SER C 1 220 ? 45.910  -39.790 -6.163   1.00 82.78  ? 221 SER C CB  1 
ATOM   5678  O OG  . SER C 1 220 ? 45.919  -40.844 -7.109   1.00 87.12  ? 221 SER C OG  1 
ATOM   5679  N N   . GLN C 1 221 ? 45.922  -38.507 -3.224   1.00 61.36  ? 222 GLN C N   1 
ATOM   5680  C CA  . GLN C 1 221 ? 45.597  -37.349 -2.402   1.00 55.81  ? 222 GLN C CA  1 
ATOM   5681  C C   . GLN C 1 221 ? 45.323  -36.136 -3.283   1.00 68.58  ? 222 GLN C C   1 
ATOM   5682  O O   . GLN C 1 221 ? 46.134  -35.783 -4.146   1.00 69.16  ? 222 GLN C O   1 
ATOM   5683  C CB  . GLN C 1 221 ? 46.739  -37.053 -1.431   1.00 53.46  ? 222 GLN C CB  1 
ATOM   5684  C CG  . GLN C 1 221 ? 46.363  -37.192 0.035    1.00 78.02  ? 222 GLN C CG  1 
ATOM   5685  C CD  . GLN C 1 221 ? 47.482  -36.773 0.968    1.00 64.96  ? 222 GLN C CD  1 
ATOM   5686  O OE1 . GLN C 1 221 ? 48.620  -36.578 0.542    1.00 81.19  ? 222 GLN C OE1 1 
ATOM   5687  N NE2 . GLN C 1 221 ? 47.162  -36.629 2.249    1.00 82.96  ? 222 GLN C NE2 1 
ATOM   5688  N N   . VAL C 1 222 ? 44.171  -35.503 -3.071   1.00 66.02  ? 223 VAL C N   1 
ATOM   5689  C CA  . VAL C 1 222 ? 43.827  -34.237 -3.710   1.00 53.28  ? 223 VAL C CA  1 
ATOM   5690  C C   . VAL C 1 222 ? 43.426  -33.260 -2.613   1.00 55.37  ? 223 VAL C C   1 
ATOM   5691  O O   . VAL C 1 222 ? 42.548  -33.567 -1.798   1.00 55.50  ? 223 VAL C O   1 
ATOM   5692  C CB  . VAL C 1 222 ? 42.689  -34.394 -4.740   1.00 52.70  ? 223 VAL C CB  1 
ATOM   5693  C CG1 . VAL C 1 222 ? 42.436  -33.072 -5.447   1.00 44.09  ? 223 VAL C CG1 1 
ATOM   5694  C CG2 . VAL C 1 222 ? 43.024  -35.484 -5.744   1.00 58.33  ? 223 VAL C CG2 1 
ATOM   5695  N N   . ASN C 1 223 ? 44.071  -32.091 -2.594   1.00 56.55  ? 224 ASN C N   1 
ATOM   5696  C CA  . ASN C 1 223 ? 43.900  -31.105 -1.526   1.00 60.58  ? 224 ASN C CA  1 
ATOM   5697  C C   . ASN C 1 223 ? 44.166  -31.715 -0.151   1.00 51.72  ? 224 ASN C C   1 
ATOM   5698  O O   . ASN C 1 223 ? 43.535  -31.339 0.840    1.00 67.97  ? 224 ASN C O   1 
ATOM   5699  C CB  . ASN C 1 223 ? 42.511  -30.460 -1.561   1.00 55.52  ? 224 ASN C CB  1 
ATOM   5700  C CG  . ASN C 1 223 ? 42.355  -29.472 -2.699   1.00 80.37  ? 224 ASN C CG  1 
ATOM   5701  O OD1 . ASN C 1 223 ? 43.094  -29.517 -3.682   1.00 92.71  ? 224 ASN C OD1 1 
ATOM   5702  N ND2 . ASN C 1 223 ? 41.388  -28.571 -2.571   1.00 77.20  ? 224 ASN C ND2 1 
ATOM   5703  N N   . GLY C 1 224 ? 45.092  -32.672 -0.084   1.00 54.50  ? 225 GLY C N   1 
ATOM   5704  C CA  . GLY C 1 224 ? 45.461  -33.307 1.162    1.00 51.76  ? 225 GLY C CA  1 
ATOM   5705  C C   . GLY C 1 224 ? 44.539  -34.407 1.641    1.00 60.72  ? 225 GLY C C   1 
ATOM   5706  O O   . GLY C 1 224 ? 44.758  -34.937 2.736    1.00 69.05  ? 225 GLY C O   1 
ATOM   5707  N N   . LEU C 1 225 ? 43.519  -34.769 0.866    1.00 59.10  ? 226 LEU C N   1 
ATOM   5708  C CA  . LEU C 1 225 ? 42.544  -35.775 1.266    1.00 57.49  ? 226 LEU C CA  1 
ATOM   5709  C C   . LEU C 1 225 ? 42.434  -36.842 0.188    1.00 45.28  ? 226 LEU C C   1 
ATOM   5710  O O   . LEU C 1 225 ? 42.347  -36.520 -1.001   1.00 51.89  ? 226 LEU C O   1 
ATOM   5711  C CB  . LEU C 1 225 ? 41.169  -35.145 1.521    1.00 53.06  ? 226 LEU C CB  1 
ATOM   5712  C CG  . LEU C 1 225 ? 40.846  -34.640 2.931    1.00 65.53  ? 226 LEU C CG  1 
ATOM   5713  C CD1 . LEU C 1 225 ? 40.905  -35.785 3.928    1.00 49.11  ? 226 LEU C CD1 1 
ATOM   5714  C CD2 . LEU C 1 225 ? 41.770  -33.509 3.355    1.00 59.15  ? 226 LEU C CD2 1 
ATOM   5715  N N   . ARG C 1 226 ? 42.432  -38.107 0.607    1.00 53.43  ? 227 ARG C N   1 
ATOM   5716  C CA  . ARG C 1 226 ? 42.260  -39.226 -0.309   1.00 52.74  ? 227 ARG C CA  1 
ATOM   5717  C C   . ARG C 1 226 ? 40.802  -39.622 -0.495   1.00 47.80  ? 227 ARG C C   1 
ATOM   5718  O O   . ARG C 1 226 ? 40.510  -40.466 -1.349   1.00 58.65  ? 227 ARG C O   1 
ATOM   5719  C CB  . ARG C 1 226 ? 43.057  -40.441 0.183    1.00 58.59  ? 227 ARG C CB  1 
ATOM   5720  C CG  . ARG C 1 226 ? 44.460  -40.112 0.675    1.00 69.83  ? 227 ARG C CG  1 
ATOM   5721  C CD  . ARG C 1 226 ? 45.366  -41.335 0.643    1.00 67.84  ? 227 ARG C CD  1 
ATOM   5722  N NE  . ARG C 1 226 ? 46.271  -41.313 -0.501   1.00 105.63 ? 227 ARG C NE  1 
ATOM   5723  C CZ  . ARG C 1 226 ? 47.577  -41.093 -0.420   1.00 106.51 ? 227 ARG C CZ  1 
ATOM   5724  N NH1 . ARG C 1 226 ? 48.175  -40.907 0.746    1.00 88.74  ? 227 ARG C NH1 1 
ATOM   5725  N NH2 . ARG C 1 226 ? 48.301  -41.065 -1.535   1.00 88.05  ? 227 ARG C NH2 1 
ATOM   5726  N N   . GLY C 1 227 ? 39.887  -39.047 0.286    1.00 54.12  ? 228 GLY C N   1 
ATOM   5727  C CA  . GLY C 1 227 ? 38.477  -39.293 0.089    1.00 46.81  ? 228 GLY C CA  1 
ATOM   5728  C C   . GLY C 1 227 ? 37.882  -38.380 -0.965   1.00 50.67  ? 228 GLY C C   1 
ATOM   5729  O O   . GLY C 1 227 ? 38.514  -37.440 -1.446   1.00 50.06  ? 228 GLY C O   1 
ATOM   5730  N N   . ARG C 1 228 ? 36.634  -38.672 -1.326   1.00 47.76  ? 229 ARG C N   1 
ATOM   5731  C CA  . ARG C 1 228 ? 35.920  -37.897 -2.329   1.00 46.10  ? 229 ARG C CA  1 
ATOM   5732  C C   . ARG C 1 228 ? 34.497  -37.637 -1.855   1.00 46.70  ? 229 ARG C C   1 
ATOM   5733  O O   . ARG C 1 228 ? 33.947  -38.390 -1.047   1.00 51.51  ? 229 ARG C O   1 
ATOM   5734  C CB  . ARG C 1 228 ? 35.885  -38.608 -3.689   1.00 53.21  ? 229 ARG C CB  1 
ATOM   5735  C CG  . ARG C 1 228 ? 37.251  -38.928 -4.278   1.00 33.40  ? 229 ARG C CG  1 
ATOM   5736  C CD  . ARG C 1 228 ? 37.992  -37.671 -4.687   1.00 39.68  ? 229 ARG C CD  1 
ATOM   5737  N NE  . ARG C 1 228 ? 39.310  -37.984 -5.223   1.00 56.65  ? 229 ARG C NE  1 
ATOM   5738  C CZ  . ARG C 1 228 ? 40.414  -38.071 -4.494   1.00 51.57  ? 229 ARG C CZ  1 
ATOM   5739  N NH1 . ARG C 1 228 ? 40.400  -37.850 -3.190   1.00 50.19  ? 229 ARG C NH1 1 
ATOM   5740  N NH2 . ARG C 1 228 ? 41.560  -38.388 -5.089   1.00 41.66  ? 229 ARG C NH2 1 
ATOM   5741  N N   . MET C 1 229 ? 33.906  -36.559 -2.367   1.00 42.91  ? 230 MET C N   1 
ATOM   5742  C CA  . MET C 1 229 ? 32.502  -36.235 -2.124   1.00 42.50  ? 230 MET C CA  1 
ATOM   5743  C C   . MET C 1 229 ? 31.852  -35.854 -3.446   1.00 52.00  ? 230 MET C C   1 
ATOM   5744  O O   . MET C 1 229 ? 32.126  -34.778 -3.989   1.00 65.12  ? 230 MET C O   1 
ATOM   5745  C CB  . MET C 1 229 ? 32.359  -35.106 -1.106   1.00 46.06  ? 230 MET C CB  1 
ATOM   5746  C CG  . MET C 1 229 ? 32.065  -35.593 0.296    1.00 50.86  ? 230 MET C CG  1 
ATOM   5747  S SD  . MET C 1 229 ? 32.024  -34.251 1.490    1.00 66.04  ? 230 MET C SD  1 
ATOM   5748  C CE  . MET C 1 229 ? 32.618  -35.097 2.949    1.00 65.46  ? 230 MET C CE  1 
ATOM   5749  N N   . ASP C 1 230 ? 30.982  -36.723 -3.949   1.00 40.54  ? 231 ASP C N   1 
ATOM   5750  C CA  . ASP C 1 230 ? 30.261  -36.489 -5.192   1.00 46.80  ? 231 ASP C CA  1 
ATOM   5751  C C   . ASP C 1 230 ? 28.899  -35.891 -4.875   1.00 40.74  ? 231 ASP C C   1 
ATOM   5752  O O   . ASP C 1 230 ? 28.158  -36.431 -4.048   1.00 46.83  ? 231 ASP C O   1 
ATOM   5753  C CB  . ASP C 1 230 ? 30.107  -37.789 -5.980   1.00 58.84  ? 231 ASP C CB  1 
ATOM   5754  C CG  . ASP C 1 230 ? 31.439  -38.393 -6.362   1.00 69.18  ? 231 ASP C CG  1 
ATOM   5755  O OD1 . ASP C 1 230 ? 32.386  -37.617 -6.614   1.00 64.69  ? 231 ASP C OD1 1 
ATOM   5756  O OD2 . ASP C 1 230 ? 31.543  -39.637 -6.403   1.00 71.16  ? 231 ASP C OD2 1 
ATOM   5757  N N   . PHE C 1 231 ? 28.576  -34.780 -5.527   1.00 47.92  ? 232 PHE C N   1 
ATOM   5758  C CA  . PHE C 1 231 ? 27.350  -34.049 -5.256   1.00 43.94  ? 232 PHE C CA  1 
ATOM   5759  C C   . PHE C 1 231 ? 26.375  -34.175 -6.419   1.00 51.12  ? 232 PHE C C   1 
ATOM   5760  O O   . PHE C 1 231 ? 26.771  -34.306 -7.580   1.00 51.20  ? 232 PHE C O   1 
ATOM   5761  C CB  . PHE C 1 231 ? 27.644  -32.573 -4.974   1.00 44.61  ? 232 PHE C CB  1 
ATOM   5762  C CG  . PHE C 1 231 ? 28.286  -32.331 -3.638   1.00 52.22  ? 232 PHE C CG  1 
ATOM   5763  C CD1 . PHE C 1 231 ? 27.513  -32.207 -2.496   1.00 47.86  ? 232 PHE C CD1 1 
ATOM   5764  C CD2 . PHE C 1 231 ? 29.661  -32.228 -3.524   1.00 35.01  ? 232 PHE C CD2 1 
ATOM   5765  C CE1 . PHE C 1 231 ? 28.101  -31.983 -1.266   1.00 41.15  ? 232 PHE C CE1 1 
ATOM   5766  C CE2 . PHE C 1 231 ? 30.253  -32.003 -2.298   1.00 42.16  ? 232 PHE C CE2 1 
ATOM   5767  C CZ  . PHE C 1 231 ? 29.472  -31.881 -1.168   1.00 50.09  ? 232 PHE C CZ  1 
ATOM   5768  N N   . PHE C 1 232 ? 25.088  -34.131 -6.087   1.00 49.58  ? 233 PHE C N   1 
ATOM   5769  C CA  . PHE C 1 232 ? 24.016  -34.278 -7.055   1.00 41.67  ? 233 PHE C CA  1 
ATOM   5770  C C   . PHE C 1 232 ? 22.984  -33.184 -6.828   1.00 38.20  ? 233 PHE C C   1 
ATOM   5771  O O   . PHE C 1 232 ? 22.899  -32.597 -5.747   1.00 53.60  ? 233 PHE C O   1 
ATOM   5772  C CB  . PHE C 1 232 ? 23.351  -35.657 -6.951   1.00 35.45  ? 233 PHE C CB  1 
ATOM   5773  C CG  . PHE C 1 232 ? 24.313  -36.806 -7.072   1.00 51.08  ? 233 PHE C CG  1 
ATOM   5774  C CD1 . PHE C 1 232 ? 25.014  -37.261 -5.967   1.00 45.03  ? 233 PHE C CD1 1 
ATOM   5775  C CD2 . PHE C 1 232 ? 24.507  -37.439 -8.287   1.00 56.48  ? 233 PHE C CD2 1 
ATOM   5776  C CE1 . PHE C 1 232 ? 25.896  -38.318 -6.073   1.00 49.19  ? 233 PHE C CE1 1 
ATOM   5777  C CE2 . PHE C 1 232 ? 25.388  -38.499 -8.400   1.00 58.95  ? 233 PHE C CE2 1 
ATOM   5778  C CZ  . PHE C 1 232 ? 26.082  -38.939 -7.290   1.00 46.11  ? 233 PHE C CZ  1 
ATOM   5779  N N   . TRP C 1 233 ? 22.196  -32.910 -7.864   1.00 48.08  ? 234 TRP C N   1 
ATOM   5780  C CA  . TRP C 1 233 ? 21.180  -31.873 -7.793   1.00 47.47  ? 234 TRP C CA  1 
ATOM   5781  C C   . TRP C 1 233 ? 19.924  -32.326 -8.522   1.00 55.53  ? 234 TRP C C   1 
ATOM   5782  O O   . TRP C 1 233 ? 19.961  -33.198 -9.393   1.00 64.73  ? 234 TRP C O   1 
ATOM   5783  C CB  . TRP C 1 233 ? 21.679  -30.550 -8.387   1.00 54.20  ? 234 TRP C CB  1 
ATOM   5784  C CG  . TRP C 1 233 ? 22.082  -30.652 -9.825   1.00 53.79  ? 234 TRP C CG  1 
ATOM   5785  C CD1 . TRP C 1 233 ? 23.274  -31.106 -10.309  1.00 54.57  ? 234 TRP C CD1 1 
ATOM   5786  C CD2 . TRP C 1 233 ? 21.298  -30.285 -10.967  1.00 52.66  ? 234 TRP C CD2 1 
ATOM   5787  N NE1 . TRP C 1 233 ? 23.280  -31.048 -11.682  1.00 57.51  ? 234 TRP C NE1 1 
ATOM   5788  C CE2 . TRP C 1 233 ? 22.079  -30.547 -12.111  1.00 50.75  ? 234 TRP C CE2 1 
ATOM   5789  C CE3 . TRP C 1 233 ? 20.011  -29.762 -11.133  1.00 54.98  ? 234 TRP C CE3 1 
ATOM   5790  C CZ2 . TRP C 1 233 ? 21.616  -30.304 -13.404  1.00 47.25  ? 234 TRP C CZ2 1 
ATOM   5791  C CZ3 . TRP C 1 233 ? 19.553  -29.520 -12.419  1.00 56.42  ? 234 TRP C CZ3 1 
ATOM   5792  C CH2 . TRP C 1 233 ? 20.354  -29.792 -13.537  1.00 40.78  ? 234 TRP C CH2 1 
ATOM   5793  N N   . THR C 1 234 ? 18.802  -31.720 -8.140   1.00 46.88  ? 235 THR C N   1 
ATOM   5794  C CA  . THR C 1 234 ? 17.541  -31.897 -8.840   1.00 55.98  ? 235 THR C CA  1 
ATOM   5795  C C   . THR C 1 234 ? 16.719  -30.628 -8.668   1.00 55.38  ? 235 THR C C   1 
ATOM   5796  O O   . THR C 1 234 ? 16.961  -29.827 -7.760   1.00 57.79  ? 235 THR C O   1 
ATOM   5797  C CB  . THR C 1 234 ? 16.764  -33.120 -8.329   1.00 63.44  ? 235 THR C CB  1 
ATOM   5798  O OG1 . THR C 1 234 ? 15.808  -33.524 -9.317   1.00 61.47  ? 235 THR C OG1 1 
ATOM   5799  C CG2 . THR C 1 234 ? 16.030  -32.793 -7.035   1.00 47.97  ? 235 THR C CG2 1 
ATOM   5800  N N   . ILE C 1 235 ? 15.751  -30.444 -9.559   1.00 47.01  ? 236 ILE C N   1 
ATOM   5801  C CA  . ILE C 1 235 ? 14.838  -29.307 -9.510   1.00 55.70  ? 236 ILE C CA  1 
ATOM   5802  C C   . ILE C 1 235 ? 13.498  -29.830 -9.015   1.00 55.36  ? 236 ILE C C   1 
ATOM   5803  O O   . ILE C 1 235 ? 12.807  -30.571 -9.726   1.00 61.55  ? 236 ILE C O   1 
ATOM   5804  C CB  . ILE C 1 235 ? 14.700  -28.621 -10.876  1.00 59.57  ? 236 ILE C CB  1 
ATOM   5805  C CG1 . ILE C 1 235 ? 16.058  -28.111 -11.365  1.00 50.29  ? 236 ILE C CG1 1 
ATOM   5806  C CG2 . ILE C 1 235 ? 13.707  -27.473 -10.793  1.00 59.29  ? 236 ILE C CG2 1 
ATOM   5807  C CD1 . ILE C 1 235 ? 16.555  -26.879 -10.634  1.00 55.28  ? 236 ILE C CD1 1 
ATOM   5808  N N   . LEU C 1 236 ? 13.127  -29.446 -7.796   1.00 52.97  ? 237 LEU C N   1 
ATOM   5809  C CA  . LEU C 1 236 ? 11.885  -29.900 -7.179   1.00 54.39  ? 237 LEU C CA  1 
ATOM   5810  C C   . LEU C 1 236 ? 10.766  -28.951 -7.594   1.00 59.85  ? 237 LEU C C   1 
ATOM   5811  O O   . LEU C 1 236 ? 10.749  -27.784 -7.188   1.00 57.35  ? 237 LEU C O   1 
ATOM   5812  C CB  . LEU C 1 236 ? 12.027  -29.961 -5.661   1.00 44.20  ? 237 LEU C CB  1 
ATOM   5813  C CG  . LEU C 1 236 ? 10.972  -30.766 -4.899   1.00 48.36  ? 237 LEU C CG  1 
ATOM   5814  C CD1 . LEU C 1 236 ? 10.970  -32.217 -5.354   1.00 52.28  ? 237 LEU C CD1 1 
ATOM   5815  C CD2 . LEU C 1 236 ? 11.212  -30.674 -3.399   1.00 50.98  ? 237 LEU C CD2 1 
ATOM   5816  N N   . LYS C 1 237 ? 9.839   -29.450 -8.406   1.00 62.67  ? 238 LYS C N   1 
ATOM   5817  C CA  . LYS C 1 237 ? 8.718   -28.639 -8.845   1.00 67.24  ? 238 LYS C CA  1 
ATOM   5818  C C   . LYS C 1 237 ? 7.771   -28.367 -7.676   1.00 66.81  ? 238 LYS C C   1 
ATOM   5819  O O   . LYS C 1 237 ? 7.739   -29.127 -6.705   1.00 64.63  ? 238 LYS C O   1 
ATOM   5820  C CB  . LYS C 1 237 ? 7.976   -29.333 -9.984   1.00 54.33  ? 238 LYS C CB  1 
ATOM   5821  C CG  . LYS C 1 237 ? 8.415   -28.861 -11.360  1.00 72.97  ? 238 LYS C CG  1 
ATOM   5822  C CD  . LYS C 1 237 ? 8.451   -29.997 -12.366  1.00 83.62  ? 238 LYS C CD  1 
ATOM   5823  C CE  . LYS C 1 237 ? 8.887   -29.497 -13.736  1.00 96.57  ? 238 LYS C CE  1 
ATOM   5824  N NZ  . LYS C 1 237 ? 10.191  -28.774 -13.681  1.00 97.55  ? 238 LYS C NZ  1 
ATOM   5825  N N   . PRO C 1 238 ? 7.006   -27.274 -7.735   1.00 71.83  ? 239 PRO C N   1 
ATOM   5826  C CA  . PRO C 1 238 ? 6.119   -26.937 -6.615   1.00 66.86  ? 239 PRO C CA  1 
ATOM   5827  C C   . PRO C 1 238 ? 5.116   -28.047 -6.343   1.00 64.72  ? 239 PRO C C   1 
ATOM   5828  O O   . PRO C 1 238 ? 4.636   -28.717 -7.261   1.00 68.94  ? 239 PRO C O   1 
ATOM   5829  C CB  . PRO C 1 238 ? 5.427   -25.653 -7.085   1.00 56.93  ? 239 PRO C CB  1 
ATOM   5830  C CG  . PRO C 1 238 ? 6.361   -25.067 -8.089   1.00 64.40  ? 239 PRO C CG  1 
ATOM   5831  C CD  . PRO C 1 238 ? 6.976   -26.242 -8.786   1.00 58.38  ? 239 PRO C CD  1 
ATOM   5832  N N   . ASN C 1 239 ? 4.821   -28.245 -5.057   1.00 55.07  ? 240 ASN C N   1 
ATOM   5833  C CA  . ASN C 1 239 ? 3.897   -29.251 -4.537   1.00 63.78  ? 240 ASN C CA  1 
ATOM   5834  C C   . ASN C 1 239 ? 4.411   -30.674 -4.705   1.00 65.83  ? 240 ASN C C   1 
ATOM   5835  O O   . ASN C 1 239 ? 3.676   -31.628 -4.416   1.00 74.11  ? 240 ASN C O   1 
ATOM   5836  C CB  . ASN C 1 239 ? 2.505   -29.128 -5.169   1.00 71.96  ? 240 ASN C CB  1 
ATOM   5837  C CG  . ASN C 1 239 ? 1.878   -27.768 -4.934   1.00 74.77  ? 240 ASN C CG  1 
ATOM   5838  O OD1 . ASN C 1 239 ? 1.897   -27.247 -3.819   1.00 66.41  ? 240 ASN C OD1 1 
ATOM   5839  N ND2 . ASN C 1 239 ? 1.325   -27.181 -5.990   1.00 94.28  ? 240 ASN C ND2 1 
ATOM   5840  N N   . ASP C 1 240 ? 5.647   -30.851 -5.160   1.00 68.96  ? 241 ASP C N   1 
ATOM   5841  C CA  . ASP C 1 240 ? 6.294   -32.153 -5.192   1.00 58.91  ? 241 ASP C CA  1 
ATOM   5842  C C   . ASP C 1 240 ? 7.188   -32.310 -3.967   1.00 62.07  ? 241 ASP C C   1 
ATOM   5843  O O   . ASP C 1 240 ? 7.635   -31.331 -3.364   1.00 55.15  ? 241 ASP C O   1 
ATOM   5844  C CB  . ASP C 1 240 ? 7.116   -32.330 -6.473   1.00 64.30  ? 241 ASP C CB  1 
ATOM   5845  C CG  . ASP C 1 240 ? 7.554   -33.768 -6.690   1.00 81.53  ? 241 ASP C CG  1 
ATOM   5846  O OD1 . ASP C 1 240 ? 7.034   -34.659 -5.987   1.00 73.21  ? 241 ASP C OD1 1 
ATOM   5847  O OD2 . ASP C 1 240 ? 8.421   -34.005 -7.559   1.00 80.28  ? 241 ASP C OD2 1 
ATOM   5848  N N   . ALA C 1 241 ? 7.445   -33.562 -3.602   1.00 57.90  ? 242 ALA C N   1 
ATOM   5849  C CA  . ALA C 1 241 ? 8.235   -33.882 -2.424   1.00 70.60  ? 242 ALA C CA  1 
ATOM   5850  C C   . ALA C 1 241 ? 9.430   -34.743 -2.805   1.00 63.54  ? 242 ALA C C   1 
ATOM   5851  O O   . ALA C 1 241 ? 9.321   -35.635 -3.654   1.00 68.29  ? 242 ALA C O   1 
ATOM   5852  C CB  . ALA C 1 241 ? 7.391   -34.600 -1.366   1.00 52.48  ? 242 ALA C CB  1 
ATOM   5853  N N   . ILE C 1 242 ? 10.568  -34.472 -2.174   1.00 57.47  ? 243 ILE C N   1 
ATOM   5854  C CA  . ILE C 1 242 ? 11.778  -35.265 -2.347   1.00 60.16  ? 243 ILE C CA  1 
ATOM   5855  C C   . ILE C 1 242 ? 11.992  -36.086 -1.083   1.00 52.71  ? 243 ILE C C   1 
ATOM   5856  O O   . ILE C 1 242 ? 11.832  -35.580 0.034    1.00 54.25  ? 243 ILE C O   1 
ATOM   5857  C CB  . ILE C 1 242 ? 13.000  -34.377 -2.663   1.00 42.95  ? 243 ILE C CB  1 
ATOM   5858  C CG1 . ILE C 1 242 ? 14.248  -35.236 -2.877   1.00 60.21  ? 243 ILE C CG1 1 
ATOM   5859  C CG2 . ILE C 1 242 ? 13.227  -33.333 -1.570   1.00 52.84  ? 243 ILE C CG2 1 
ATOM   5860  C CD1 . ILE C 1 242 ? 15.398  -34.491 -3.523   1.00 43.96  ? 243 ILE C CD1 1 
ATOM   5861  N N   . HIS C 1 243 ? 12.322  -37.363 -1.258   1.00 63.09  ? 244 HIS C N   1 
ATOM   5862  C CA  . HIS C 1 243 ? 12.467  -38.298 -0.150   1.00 44.60  ? 244 HIS C CA  1 
ATOM   5863  C C   . HIS C 1 243 ? 13.921  -38.737 -0.038   1.00 50.85  ? 244 HIS C C   1 
ATOM   5864  O O   . HIS C 1 243 ? 14.532  -39.129 -1.037   1.00 61.79  ? 244 HIS C O   1 
ATOM   5865  C CB  . HIS C 1 243 ? 11.557  -39.514 -0.340   1.00 50.40  ? 244 HIS C CB  1 
ATOM   5866  C CG  . HIS C 1 243 ? 10.098  -39.178 -0.379   1.00 69.52  ? 244 HIS C CG  1 
ATOM   5867  N ND1 . HIS C 1 243 ? 9.265   -39.359 0.703    1.00 74.42  ? 244 HIS C ND1 1 
ATOM   5868  C CD2 . HIS C 1 243 ? 9.325   -38.673 -1.369   1.00 71.01  ? 244 HIS C CD2 1 
ATOM   5869  C CE1 . HIS C 1 243 ? 8.040   -38.980 0.382    1.00 74.08  ? 244 HIS C CE1 1 
ATOM   5870  N NE2 . HIS C 1 243 ? 8.050   -38.559 -0.870   1.00 55.94  ? 244 HIS C NE2 1 
ATOM   5871  N N   . PHE C 1 244 ? 14.466  -38.671 1.175    1.00 53.03  ? 245 PHE C N   1 
ATOM   5872  C CA  . PHE C 1 244 ? 15.833  -39.083 1.458    1.00 42.26  ? 245 PHE C CA  1 
ATOM   5873  C C   . PHE C 1 244 ? 15.833  -40.260 2.424    1.00 38.54  ? 245 PHE C C   1 
ATOM   5874  O O   . PHE C 1 244 ? 15.027  -40.310 3.358    1.00 50.65  ? 245 PHE C O   1 
ATOM   5875  C CB  . PHE C 1 244 ? 16.654  -37.936 2.053    1.00 36.68  ? 245 PHE C CB  1 
ATOM   5876  C CG  . PHE C 1 244 ? 16.980  -36.851 1.070    1.00 50.47  ? 245 PHE C CG  1 
ATOM   5877  C CD1 . PHE C 1 244 ? 18.038  -36.994 0.188    1.00 46.58  ? 245 PHE C CD1 1 
ATOM   5878  C CD2 . PHE C 1 244 ? 16.236  -35.682 1.036    1.00 46.31  ? 245 PHE C CD2 1 
ATOM   5879  C CE1 . PHE C 1 244 ? 18.345  -35.993 -0.715   1.00 55.20  ? 245 PHE C CE1 1 
ATOM   5880  C CE2 . PHE C 1 244 ? 16.538  -34.677 0.136    1.00 45.56  ? 245 PHE C CE2 1 
ATOM   5881  C CZ  . PHE C 1 244 ? 17.594  -34.832 -0.741   1.00 41.25  ? 245 PHE C CZ  1 
ATOM   5882  N N   . GLU C 1 245 ? 16.739  -41.208 2.187    1.00 45.96  ? 246 GLU C N   1 
ATOM   5883  C CA  . GLU C 1 245 ? 16.934  -42.337 3.087    1.00 42.88  ? 246 GLU C CA  1 
ATOM   5884  C C   . GLU C 1 245 ? 18.403  -42.729 3.068    1.00 48.55  ? 246 GLU C C   1 
ATOM   5885  O O   . GLU C 1 245 ? 18.977  -42.916 1.992    1.00 54.11  ? 246 GLU C O   1 
ATOM   5886  C CB  . GLU C 1 245 ? 16.056  -43.527 2.686    1.00 48.65  ? 246 GLU C CB  1 
ATOM   5887  C CG  . GLU C 1 245 ? 15.987  -44.627 3.733    1.00 61.38  ? 246 GLU C CG  1 
ATOM   5888  C CD  . GLU C 1 245 ? 14.973  -45.701 3.388    1.00 98.08  ? 246 GLU C CD  1 
ATOM   5889  O OE1 . GLU C 1 245 ? 15.196  -46.874 3.759    1.00 80.10  ? 246 GLU C OE1 1 
ATOM   5890  O OE2 . GLU C 1 245 ? 13.951  -45.370 2.747    1.00 95.96  ? 246 GLU C OE2 1 
ATOM   5891  N N   . SER C 1 246 ? 19.002  -42.855 4.251    1.00 54.22  ? 247 SER C N   1 
ATOM   5892  C CA  . SER C 1 246 ? 20.427  -43.141 4.345    1.00 50.00  ? 247 SER C CA  1 
ATOM   5893  C C   . SER C 1 246 ? 20.759  -43.663 5.735    1.00 50.90  ? 247 SER C C   1 
ATOM   5894  O O   . SER C 1 246 ? 20.081  -43.346 6.716    1.00 62.28  ? 247 SER C O   1 
ATOM   5895  C CB  . SER C 1 246 ? 21.267  -41.897 4.030    1.00 54.27  ? 247 SER C CB  1 
ATOM   5896  O OG  . SER C 1 246 ? 22.635  -42.111 4.333    1.00 61.17  ? 247 SER C OG  1 
ATOM   5897  N N   . ASN C 1 247 ? 21.812  -44.480 5.798    1.00 42.68  ? 248 ASN C N   1 
ATOM   5898  C CA  . ASN C 1 247 ? 22.363  -44.985 7.049    1.00 47.48  ? 248 ASN C CA  1 
ATOM   5899  C C   . ASN C 1 247 ? 23.855  -44.690 7.148    1.00 50.55  ? 248 ASN C C   1 
ATOM   5900  O O   . ASN C 1 247 ? 24.587  -45.378 7.866    1.00 51.98  ? 248 ASN C O   1 
ATOM   5901  C CB  . ASN C 1 247 ? 22.097  -46.481 7.202    1.00 32.62  ? 248 ASN C CB  1 
ATOM   5902  C CG  . ASN C 1 247 ? 22.830  -47.318 6.169    1.00 50.37  ? 248 ASN C CG  1 
ATOM   5903  O OD1 . ASN C 1 247 ? 22.921  -46.943 5.000    1.00 55.79  ? 248 ASN C OD1 1 
ATOM   5904  N ND2 . ASN C 1 247 ? 23.355  -48.460 6.597    1.00 43.02  ? 248 ASN C ND2 1 
ATOM   5905  N N   . GLY C 1 248 ? 24.316  -43.677 6.436    1.00 42.97  ? 249 GLY C N   1 
ATOM   5906  C CA  . GLY C 1 248 ? 25.700  -43.254 6.508    1.00 42.16  ? 249 GLY C CA  1 
ATOM   5907  C C   . GLY C 1 248 ? 26.157  -42.617 5.212    1.00 45.30  ? 249 GLY C C   1 
ATOM   5908  O O   . GLY C 1 248 ? 25.540  -42.756 4.155    1.00 41.66  ? 249 GLY C O   1 
ATOM   5909  N N   . ASN C 1 249 ? 27.272  -41.888 5.311    1.00 46.05  ? 250 ASN C N   1 
ATOM   5910  C CA  . ASN C 1 249 ? 27.942  -41.248 4.181    1.00 46.50  ? 250 ASN C CA  1 
ATOM   5911  C C   . ASN C 1 249 ? 27.064  -40.202 3.505    1.00 40.73  ? 250 ASN C C   1 
ATOM   5912  O O   . ASN C 1 249 ? 27.321  -39.822 2.362    1.00 43.63  ? 250 ASN C O   1 
ATOM   5913  C CB  . ASN C 1 249 ? 28.412  -42.287 3.156    1.00 39.18  ? 250 ASN C CB  1 
ATOM   5914  C CG  . ASN C 1 249 ? 29.234  -43.402 3.786    1.00 51.20  ? 250 ASN C CG  1 
ATOM   5915  O OD1 . ASN C 1 249 ? 28.693  -44.295 4.441    1.00 47.26  ? 250 ASN C OD1 1 
ATOM   5916  N ND2 . ASN C 1 249 ? 30.546  -43.362 3.577    1.00 45.66  ? 250 ASN C ND2 1 
ATOM   5917  N N   . PHE C 1 250 ? 26.037  -39.723 4.201    1.00 47.96  ? 251 PHE C N   1 
ATOM   5918  C CA  . PHE C 1 250 ? 25.057  -38.812 3.626    1.00 41.86  ? 251 PHE C CA  1 
ATOM   5919  C C   . PHE C 1 250 ? 25.495  -37.371 3.869    1.00 46.19  ? 251 PHE C C   1 
ATOM   5920  O O   . PHE C 1 250 ? 25.728  -36.971 5.015    1.00 53.16  ? 251 PHE C O   1 
ATOM   5921  C CB  . PHE C 1 250 ? 23.679  -39.074 4.234    1.00 42.05  ? 251 PHE C CB  1 
ATOM   5922  C CG  . PHE C 1 250 ? 22.574  -38.255 3.633    1.00 43.98  ? 251 PHE C CG  1 
ATOM   5923  C CD1 . PHE C 1 250 ? 22.649  -37.794 2.329    1.00 54.50  ? 251 PHE C CD1 1 
ATOM   5924  C CD2 . PHE C 1 250 ? 21.454  -37.944 4.384    1.00 43.67  ? 251 PHE C CD2 1 
ATOM   5925  C CE1 . PHE C 1 250 ? 21.623  -37.037 1.784    1.00 45.56  ? 251 PHE C CE1 1 
ATOM   5926  C CE2 . PHE C 1 250 ? 20.426  -37.190 3.847    1.00 47.61  ? 251 PHE C CE2 1 
ATOM   5927  C CZ  . PHE C 1 250 ? 20.511  -36.735 2.545    1.00 44.72  ? 251 PHE C CZ  1 
ATOM   5928  N N   . ILE C 1 251 ? 25.614  -36.602 2.793    1.00 43.77  ? 252 ILE C N   1 
ATOM   5929  C CA  . ILE C 1 251 ? 25.836  -35.162 2.880    1.00 41.31  ? 252 ILE C CA  1 
ATOM   5930  C C   . ILE C 1 251 ? 24.475  -34.527 2.612    1.00 41.99  ? 252 ILE C C   1 
ATOM   5931  O O   . ILE C 1 251 ? 24.094  -34.280 1.464    1.00 46.93  ? 252 ILE C O   1 
ATOM   5932  C CB  . ILE C 1 251 ? 26.906  -34.683 1.898    1.00 42.27  ? 252 ILE C CB  1 
ATOM   5933  C CG1 . ILE C 1 251 ? 28.171  -35.535 2.014    1.00 43.11  ? 252 ILE C CG1 1 
ATOM   5934  C CG2 . ILE C 1 251 ? 27.243  -33.228 2.163    1.00 39.41  ? 252 ILE C CG2 1 
ATOM   5935  C CD1 . ILE C 1 251 ? 28.915  -35.355 3.318    1.00 50.26  ? 252 ILE C CD1 1 
ATOM   5936  N N   . ALA C 1 252 ? 23.734  -34.257 3.686    1.00 41.33  ? 253 ALA C N   1 
ATOM   5937  C CA  . ALA C 1 252 ? 22.341  -33.853 3.587    1.00 53.06  ? 253 ALA C CA  1 
ATOM   5938  C C   . ALA C 1 252 ? 22.206  -32.399 3.136    1.00 42.85  ? 253 ALA C C   1 
ATOM   5939  O O   . ALA C 1 252 ? 23.087  -31.574 3.394    1.00 53.04  ? 253 ALA C O   1 
ATOM   5940  C CB  . ALA C 1 252 ? 21.641  -34.035 4.929    1.00 46.78  ? 253 ALA C CB  1 
ATOM   5941  N N   . PRO C 1 253 ? 21.112  -32.067 2.450    1.00 47.97  ? 254 PRO C N   1 
ATOM   5942  C CA  . PRO C 1 253 ? 20.849  -30.661 2.127    1.00 49.50  ? 254 PRO C CA  1 
ATOM   5943  C C   . PRO C 1 253 ? 20.447  -29.883 3.368    1.00 49.24  ? 254 PRO C C   1 
ATOM   5944  O O   . PRO C 1 253 ? 19.760  -30.398 4.253    1.00 54.43  ? 254 PRO C O   1 
ATOM   5945  C CB  . PRO C 1 253 ? 19.692  -30.731 1.121    1.00 48.04  ? 254 PRO C CB  1 
ATOM   5946  C CG  . PRO C 1 253 ? 19.605  -32.172 0.698    1.00 43.97  ? 254 PRO C CG  1 
ATOM   5947  C CD  . PRO C 1 253 ? 20.107  -32.965 1.859    1.00 52.41  ? 254 PRO C CD  1 
ATOM   5948  N N   . GLU C 1 254 ? 20.890  -28.631 3.430    1.00 55.04  ? 255 GLU C N   1 
ATOM   5949  C CA  . GLU C 1 254 ? 20.410  -27.696 4.438    1.00 49.32  ? 255 GLU C CA  1 
ATOM   5950  C C   . GLU C 1 254 ? 19.724  -26.493 3.813    1.00 54.64  ? 255 GLU C C   1 
ATOM   5951  O O   . GLU C 1 254 ? 18.594  -26.162 4.190    1.00 58.81  ? 255 GLU C O   1 
ATOM   5952  C CB  . GLU C 1 254 ? 21.569  -27.238 5.338    1.00 57.19  ? 255 GLU C CB  1 
ATOM   5953  C CG  . GLU C 1 254 ? 21.112  -26.525 6.600    1.00 60.93  ? 255 GLU C CG  1 
ATOM   5954  C CD  . GLU C 1 254 ? 22.265  -26.014 7.441    1.00 75.56  ? 255 GLU C CD  1 
ATOM   5955  O OE1 . GLU C 1 254 ? 23.430  -26.181 7.024    1.00 82.98  ? 255 GLU C OE1 1 
ATOM   5956  O OE2 . GLU C 1 254 ? 22.002  -25.443 8.521    1.00 77.88  ? 255 GLU C OE2 1 
ATOM   5957  N N   . TYR C 1 255 ? 20.374  -25.836 2.856    1.00 51.10  ? 256 TYR C N   1 
ATOM   5958  C CA  . TYR C 1 255 ? 19.795  -24.721 2.125    1.00 56.41  ? 256 TYR C CA  1 
ATOM   5959  C C   . TYR C 1 255 ? 19.521  -25.134 0.686    1.00 47.60  ? 256 TYR C C   1 
ATOM   5960  O O   . TYR C 1 255 ? 20.307  -25.869 0.079    1.00 52.52  ? 256 TYR C O   1 
ATOM   5961  C CB  . TYR C 1 255 ? 20.725  -23.504 2.143    1.00 48.43  ? 256 TYR C CB  1 
ATOM   5962  C CG  . TYR C 1 255 ? 20.927  -22.896 3.512    1.00 57.71  ? 256 TYR C CG  1 
ATOM   5963  C CD1 . TYR C 1 255 ? 21.899  -23.389 4.375    1.00 70.51  ? 256 TYR C CD1 1 
ATOM   5964  C CD2 . TYR C 1 255 ? 20.153  -21.825 3.940    1.00 61.11  ? 256 TYR C CD2 1 
ATOM   5965  C CE1 . TYR C 1 255 ? 22.091  -22.836 5.627    1.00 51.45  ? 256 TYR C CE1 1 
ATOM   5966  C CE2 . TYR C 1 255 ? 20.338  -21.264 5.191    1.00 52.13  ? 256 TYR C CE2 1 
ATOM   5967  C CZ  . TYR C 1 255 ? 21.307  -21.774 6.029    1.00 58.82  ? 256 TYR C CZ  1 
ATOM   5968  O OH  . TYR C 1 255 ? 21.494  -21.219 7.274    1.00 64.52  ? 256 TYR C OH  1 
ATOM   5969  N N   . ALA C 1 256 ? 18.405  -24.658 0.146    1.00 50.87  ? 257 ALA C N   1 
ATOM   5970  C CA  . ALA C 1 256 ? 18.045  -24.837 -1.254   1.00 48.22  ? 257 ALA C CA  1 
ATOM   5971  C C   . ALA C 1 256 ? 17.870  -23.465 -1.894   1.00 51.01  ? 257 ALA C C   1 
ATOM   5972  O O   . ALA C 1 256 ? 17.949  -22.430 -1.227   1.00 59.71  ? 257 ALA C O   1 
ATOM   5973  C CB  . ALA C 1 256 ? 16.776  -25.683 -1.396   1.00 65.35  ? 257 ALA C CB  1 
ATOM   5974  N N   . TYR C 1 257 ? 17.631  -23.455 -3.202   1.00 64.81  ? 258 TYR C N   1 
ATOM   5975  C CA  . TYR C 1 257 ? 17.538  -22.217 -3.966   1.00 62.78  ? 258 TYR C CA  1 
ATOM   5976  C C   . TYR C 1 257 ? 16.178  -22.128 -4.643   1.00 65.70  ? 258 TYR C C   1 
ATOM   5977  O O   . TYR C 1 257 ? 15.834  -22.980 -5.470   1.00 64.38  ? 258 TYR C O   1 
ATOM   5978  C CB  . TYR C 1 257 ? 18.664  -22.132 -4.999   1.00 56.39  ? 258 TYR C CB  1 
ATOM   5979  C CG  . TYR C 1 257 ? 20.044  -22.046 -4.383   1.00 57.91  ? 258 TYR C CG  1 
ATOM   5980  C CD1 . TYR C 1 257 ? 20.549  -20.832 -3.937   1.00 49.45  ? 258 TYR C CD1 1 
ATOM   5981  C CD2 . TYR C 1 257 ? 20.838  -23.178 -4.242   1.00 49.87  ? 258 TYR C CD2 1 
ATOM   5982  C CE1 . TYR C 1 257 ? 21.807  -20.744 -3.373   1.00 52.55  ? 258 TYR C CE1 1 
ATOM   5983  C CE2 . TYR C 1 257 ? 22.099  -23.100 -3.677   1.00 47.88  ? 258 TYR C CE2 1 
ATOM   5984  C CZ  . TYR C 1 257 ? 22.578  -21.880 -3.244   1.00 56.21  ? 258 TYR C CZ  1 
ATOM   5985  O OH  . TYR C 1 257 ? 23.831  -21.792 -2.682   1.00 53.11  ? 258 TYR C OH  1 
ATOM   5986  N N   . LYS C 1 258 ? 15.410  -21.097 -4.290   1.00 66.49  ? 259 LYS C N   1 
ATOM   5987  C CA  . LYS C 1 258 ? 14.201  -20.759 -5.031   1.00 58.71  ? 259 LYS C CA  1 
ATOM   5988  C C   . LYS C 1 258 ? 14.599  -20.113 -6.351   1.00 65.55  ? 259 LYS C C   1 
ATOM   5989  O O   . LYS C 1 258 ? 15.259  -19.069 -6.363   1.00 79.39  ? 259 LYS C O   1 
ATOM   5990  C CB  . LYS C 1 258 ? 13.321  -19.817 -4.214   1.00 56.66  ? 259 LYS C CB  1 
ATOM   5991  C CG  . LYS C 1 258 ? 12.259  -20.512 -3.377   1.00 62.13  ? 259 LYS C CG  1 
ATOM   5992  C CD  . LYS C 1 258 ? 11.672  -19.569 -2.340   1.00 67.72  ? 259 LYS C CD  1 
ATOM   5993  C CE  . LYS C 1 258 ? 11.420  -18.186 -2.914   1.00 74.59  ? 259 LYS C CE  1 
ATOM   5994  N NZ  . LYS C 1 258 ? 10.770  -17.295 -1.917   1.00 93.82  ? 259 LYS C NZ  1 
ATOM   5995  N N   . ILE C 1 259 ? 14.204  -20.730 -7.462   1.00 52.66  ? 260 ILE C N   1 
ATOM   5996  C CA  . ILE C 1 259 ? 14.726  -20.385 -8.779   1.00 61.90  ? 260 ILE C CA  1 
ATOM   5997  C C   . ILE C 1 259 ? 13.574  -20.261 -9.768   1.00 70.62  ? 260 ILE C C   1 
ATOM   5998  O O   . ILE C 1 259 ? 12.718  -21.149 -9.848   1.00 69.79  ? 260 ILE C O   1 
ATOM   5999  C CB  . ILE C 1 259 ? 15.757  -21.431 -9.253   1.00 61.69  ? 260 ILE C CB  1 
ATOM   6000  C CG1 . ILE C 1 259 ? 16.064  -21.269 -10.742  1.00 65.13  ? 260 ILE C CG1 1 
ATOM   6001  C CG2 . ILE C 1 259 ? 15.282  -22.847 -8.924   1.00 73.94  ? 260 ILE C CG2 1 
ATOM   6002  C CD1 . ILE C 1 259 ? 17.076  -22.271 -11.264  1.00 87.02  ? 260 ILE C CD1 1 
ATOM   6003  N N   . VAL C 1 260 A 13.552  -19.156 -10.510  1.00 71.59  ? 260 VAL C N   1 
ATOM   6004  C CA  . VAL C 1 260 A 12.613  -18.934 -11.606  1.00 69.40  ? 260 VAL C CA  1 
ATOM   6005  C C   . VAL C 1 260 A 13.423  -18.663 -12.865  1.00 68.20  ? 260 VAL C C   1 
ATOM   6006  O O   . VAL C 1 260 A 14.303  -17.796 -12.866  1.00 68.75  ? 260 VAL C O   1 
ATOM   6007  C CB  . VAL C 1 260 A 11.648  -17.768 -11.311  1.00 65.15  ? 260 VAL C CB  1 
ATOM   6008  C CG1 . VAL C 1 260 A 11.162  -17.133 -12.605  1.00 67.10  ? 260 VAL C CG1 1 
ATOM   6009  C CG2 . VAL C 1 260 A 10.470  -18.261 -10.500  1.00 63.60  ? 260 VAL C CG2 1 
ATOM   6010  N N   . LYS C 1 261 ? 13.135  -19.408 -13.928  1.00 61.66  ? 261 LYS C N   1 
ATOM   6011  C CA  . LYS C 1 261 ? 13.882  -19.299 -15.172  1.00 79.39  ? 261 LYS C CA  1 
ATOM   6012  C C   . LYS C 1 261 ? 12.932  -19.028 -16.331  1.00 90.30  ? 261 LYS C C   1 
ATOM   6013  O O   . LYS C 1 261 ? 11.928  -19.729 -16.493  1.00 99.62  ? 261 LYS C O   1 
ATOM   6014  C CB  . LYS C 1 261 ? 14.686  -20.575 -15.442  1.00 64.55  ? 261 LYS C CB  1 
ATOM   6015  C CG  . LYS C 1 261 ? 15.558  -20.492 -16.676  1.00 84.17  ? 261 LYS C CG  1 
ATOM   6016  C CD  . LYS C 1 261 ? 16.414  -21.732 -16.823  1.00 67.48  ? 261 LYS C CD  1 
ATOM   6017  C CE  . LYS C 1 261 ? 17.399  -21.581 -17.964  1.00 81.47  ? 261 LYS C CE  1 
ATOM   6018  N NZ  . LYS C 1 261 ? 18.249  -20.372 -17.777  1.00 75.63  ? 261 LYS C NZ  1 
ATOM   6019  N N   . LYS C 1 262 ? 13.254  -18.012 -17.132  1.00 87.60  ? 262 LYS C N   1 
ATOM   6020  C CA  . LYS C 1 262 ? 12.523  -17.724 -18.360  1.00 88.99  ? 262 LYS C CA  1 
ATOM   6021  C C   . LYS C 1 262 ? 13.395  -17.910 -19.594  1.00 100.55 ? 262 LYS C C   1 
ATOM   6022  O O   . LYS C 1 262 ? 13.037  -18.687 -20.485  1.00 125.06 ? 262 LYS C O   1 
ATOM   6023  C CB  . LYS C 1 262 ? 11.962  -16.295 -18.319  1.00 81.56  ? 262 LYS C CB  1 
ATOM   6024  C CG  . LYS C 1 262 ? 10.907  -16.055 -17.255  1.00 100.83 ? 262 LYS C CG  1 
ATOM   6025  C CD  . LYS C 1 262 ? 10.487  -14.595 -17.253  1.00 117.53 ? 262 LYS C CD  1 
ATOM   6026  C CE  . LYS C 1 262 ? 9.466   -14.307 -16.169  1.00 115.72 ? 262 LYS C CE  1 
ATOM   6027  N NZ  . LYS C 1 262 ? 9.150   -12.853 -16.079  1.00 120.98 ? 262 LYS C NZ  1 
ATOM   6028  N N   . GLY C 1 263 ? 14.538  -17.226 -19.673  1.00 90.11  ? 263 GLY C N   1 
ATOM   6029  C CA  . GLY C 1 263 ? 15.407  -17.303 -20.825  1.00 87.10  ? 263 GLY C CA  1 
ATOM   6030  C C   . GLY C 1 263 ? 16.588  -18.240 -20.613  1.00 85.56  ? 263 GLY C C   1 
ATOM   6031  O O   . GLY C 1 263 ? 16.718  -18.919 -19.597  1.00 91.30  ? 263 GLY C O   1 
ATOM   6032  N N   . ASP C 1 264 ? 17.464  -18.262 -21.616  1.00 104.11 ? 264 ASP C N   1 
ATOM   6033  C CA  . ASP C 1 264 ? 18.670  -19.075 -21.575  1.00 88.52  ? 264 ASP C CA  1 
ATOM   6034  C C   . ASP C 1 264 ? 19.856  -18.242 -22.039  1.00 77.32  ? 264 ASP C C   1 
ATOM   6035  O O   . ASP C 1 264 ? 19.711  -17.309 -22.832  1.00 85.67  ? 264 ASP C O   1 
ATOM   6036  C CB  . ASP C 1 264 ? 18.550  -20.331 -22.449  1.00 101.12 ? 264 ASP C CB  1 
ATOM   6037  C CG  . ASP C 1 264 ? 19.019  -21.583 -21.732  1.00 114.13 ? 264 ASP C CG  1 
ATOM   6038  O OD1 . ASP C 1 264 ? 19.007  -22.665 -22.357  1.00 118.88 ? 264 ASP C OD1 1 
ATOM   6039  O OD2 . ASP C 1 264 ? 19.380  -21.486 -20.540  1.00 102.59 ? 264 ASP C OD2 1 
ATOM   6040  N N   . SER C 1 265 ? 21.033  -18.595 -21.537  1.00 70.12  ? 265 SER C N   1 
ATOM   6041  C CA  . SER C 1 265 ? 22.264  -17.870 -21.829  1.00 68.16  ? 265 SER C CA  1 
ATOM   6042  C C   . SER C 1 265 ? 23.417  -18.868 -21.777  1.00 66.31  ? 265 SER C C   1 
ATOM   6043  O O   . SER C 1 265 ? 23.204  -20.083 -21.851  1.00 87.37  ? 265 SER C O   1 
ATOM   6044  C CB  . SER C 1 265 ? 22.439  -16.695 -20.850  1.00 65.74  ? 265 SER C CB  1 
ATOM   6045  O OG  . SER C 1 265 ? 23.597  -15.940 -21.159  1.00 61.74  ? 265 SER C OG  1 
ATOM   6046  N N   . THR C 1 266 ? 24.643  -18.360 -21.667  1.00 60.29  ? 266 THR C N   1 
ATOM   6047  C CA  . THR C 1 266 ? 25.815  -19.205 -21.487  1.00 75.44  ? 266 THR C CA  1 
ATOM   6048  C C   . THR C 1 266 ? 26.735  -18.553 -20.461  1.00 73.04  ? 266 THR C C   1 
ATOM   6049  O O   . THR C 1 266 ? 26.447  -17.474 -19.931  1.00 60.64  ? 266 THR C O   1 
ATOM   6050  C CB  . THR C 1 266 ? 26.538  -19.452 -22.818  1.00 76.04  ? 266 THR C CB  1 
ATOM   6051  O OG1 . THR C 1 266 ? 27.443  -20.554 -22.675  1.00 80.24  ? 266 THR C OG1 1 
ATOM   6052  C CG2 . THR C 1 266 ? 27.316  -18.220 -23.248  1.00 62.80  ? 266 THR C CG2 1 
ATOM   6053  N N   . ILE C 1 267 ? 27.848  -19.222 -20.169  1.00 56.20  ? 267 ILE C N   1 
ATOM   6054  C CA  . ILE C 1 267 ? 28.820  -18.749 -19.188  1.00 61.19  ? 267 ILE C CA  1 
ATOM   6055  C C   . ILE C 1 267 ? 30.012  -18.155 -19.927  1.00 65.07  ? 267 ILE C C   1 
ATOM   6056  O O   . ILE C 1 267 ? 30.535  -18.761 -20.872  1.00 62.68  ? 267 ILE C O   1 
ATOM   6057  C CB  . ILE C 1 267 ? 29.255  -19.881 -18.240  1.00 61.12  ? 267 ILE C CB  1 
ATOM   6058  C CG1 . ILE C 1 267 ? 28.093  -20.275 -17.318  1.00 56.93  ? 267 ILE C CG1 1 
ATOM   6059  C CG2 . ILE C 1 267 ? 30.479  -19.467 -17.430  1.00 51.01  ? 267 ILE C CG2 1 
ATOM   6060  C CD1 . ILE C 1 267 ? 28.518  -20.944 -16.016  1.00 75.67  ? 267 ILE C CD1 1 
ATOM   6061  N N   . MET C 1 268 ? 30.439  -16.970 -19.497  1.00 66.21  ? 268 MET C N   1 
ATOM   6062  C CA  . MET C 1 268 ? 31.532  -16.234 -20.116  1.00 68.45  ? 268 MET C CA  1 
ATOM   6063  C C   . MET C 1 268 ? 32.783  -16.335 -19.255  1.00 70.43  ? 268 MET C C   1 
ATOM   6064  O O   . MET C 1 268 ? 32.730  -16.100 -18.044  1.00 82.00  ? 268 MET C O   1 
ATOM   6065  C CB  . MET C 1 268 ? 31.156  -14.766 -20.319  1.00 64.94  ? 268 MET C CB  1 
ATOM   6066  C CG  . MET C 1 268 ? 32.343  -13.856 -20.583  1.00 64.40  ? 268 MET C CG  1 
ATOM   6067  S SD  . MET C 1 268 ? 31.832  -12.340 -21.403  1.00 84.75  ? 268 MET C SD  1 
ATOM   6068  C CE  . MET C 1 268 ? 30.881  -13.036 -22.749  1.00 75.57  ? 268 MET C CE  1 
ATOM   6069  N N   . LYS C 1 269 ? 33.905  -16.674 -19.885  1.00 62.96  ? 269 LYS C N   1 
ATOM   6070  C CA  . LYS C 1 269 ? 35.210  -16.705 -19.230  1.00 67.98  ? 269 LYS C CA  1 
ATOM   6071  C C   . LYS C 1 269 ? 35.939  -15.413 -19.588  1.00 67.78  ? 269 LYS C C   1 
ATOM   6072  O O   . LYS C 1 269 ? 36.432  -15.260 -20.708  1.00 69.43  ? 269 LYS C O   1 
ATOM   6073  C CB  . LYS C 1 269 ? 36.007  -17.930 -19.672  1.00 61.03  ? 269 LYS C CB  1 
ATOM   6074  C CG  . LYS C 1 269 ? 35.292  -19.262 -19.484  1.00 84.49  ? 269 LYS C CG  1 
ATOM   6075  C CD  . LYS C 1 269 ? 35.218  -19.663 -18.021  1.00 96.89  ? 269 LYS C CD  1 
ATOM   6076  C CE  . LYS C 1 269 ? 35.125  -21.175 -17.883  1.00 94.12  ? 269 LYS C CE  1 
ATOM   6077  N NZ  . LYS C 1 269 ? 35.145  -21.613 -16.461  1.00 99.97  ? 269 LYS C NZ  1 
ATOM   6078  N N   . SER C 1 270 ? 36.006  -14.479 -18.638  1.00 79.59  ? 270 SER C N   1 
ATOM   6079  C CA  . SER C 1 270 ? 36.649  -13.194 -18.875  1.00 70.21  ? 270 SER C CA  1 
ATOM   6080  C C   . SER C 1 270 ? 37.167  -12.626 -17.562  1.00 77.74  ? 270 SER C C   1 
ATOM   6081  O O   . SER C 1 270 ? 36.563  -12.818 -16.503  1.00 71.73  ? 270 SER C O   1 
ATOM   6082  C CB  . SER C 1 270 ? 35.692  -12.195 -19.534  1.00 72.79  ? 270 SER C CB  1 
ATOM   6083  O OG  . SER C 1 270 ? 36.274  -10.905 -19.587  1.00 67.69  ? 270 SER C OG  1 
ATOM   6084  N N   . GLY C 1 271 ? 38.298  -11.927 -17.644  1.00 82.27  ? 271 GLY C N   1 
ATOM   6085  C CA  . GLY C 1 271 ? 38.887  -11.280 -16.488  1.00 72.32  ? 271 GLY C CA  1 
ATOM   6086  C C   . GLY C 1 271 ? 38.654  -9.783  -16.451  1.00 81.56  ? 271 GLY C C   1 
ATOM   6087  O O   . GLY C 1 271 ? 39.000  -9.126  -15.466  1.00 93.72  ? 271 GLY C O   1 
ATOM   6088  N N   . VAL C 1 272 ? 38.076  -9.231  -17.520  1.00 86.94  ? 272 VAL C N   1 
ATOM   6089  C CA  . VAL C 1 272 ? 37.845  -7.794  -17.595  1.00 86.67  ? 272 VAL C CA  1 
ATOM   6090  C C   . VAL C 1 272 ? 36.793  -7.392  -16.569  1.00 84.46  ? 272 VAL C C   1 
ATOM   6091  O O   . VAL C 1 272 ? 35.848  -8.138  -16.284  1.00 82.14  ? 272 VAL C O   1 
ATOM   6092  C CB  . VAL C 1 272 ? 37.433  -7.397  -19.026  1.00 87.44  ? 272 VAL C CB  1 
ATOM   6093  C CG1 . VAL C 1 272 ? 36.645  -6.101  -19.040  1.00 90.54  ? 272 VAL C CG1 1 
ATOM   6094  C CG2 . VAL C 1 272 ? 38.660  -7.263  -19.902  1.00 82.20  ? 272 VAL C CG2 1 
ATOM   6095  N N   . GLU C 1 273 ? 36.967  -6.202  -16.000  1.00 80.96  ? 273 GLU C N   1 
ATOM   6096  C CA  . GLU C 1 273 ? 36.169  -5.741  -14.876  1.00 90.09  ? 273 GLU C CA  1 
ATOM   6097  C C   . GLU C 1 273 ? 34.831  -5.168  -15.334  1.00 90.67  ? 273 GLU C C   1 
ATOM   6098  O O   . GLU C 1 273 ? 34.642  -4.795  -16.495  1.00 92.19  ? 273 GLU C O   1 
ATOM   6099  C CB  . GLU C 1 273 ? 36.943  -4.687  -14.081  1.00 98.63  ? 273 GLU C CB  1 
ATOM   6100  C CG  . GLU C 1 273 ? 36.964  -4.938  -12.588  1.00 115.46 ? 273 GLU C CG  1 
ATOM   6101  C CD  . GLU C 1 273 ? 37.409  -3.725  -11.796  1.00 133.00 ? 273 GLU C CD  1 
ATOM   6102  O OE1 . GLU C 1 273 ? 38.541  -3.248  -12.021  1.00 135.51 ? 273 GLU C OE1 1 
ATOM   6103  O OE2 . GLU C 1 273 ? 36.619  -3.248  -10.952  1.00 125.63 ? 273 GLU C OE2 1 
ATOM   6104  N N   . TYR C 1 274 ? 33.895  -5.108  -14.389  1.00 84.68  ? 274 TYR C N   1 
ATOM   6105  C CA  . TYR C 1 274 ? 32.590  -4.507  -14.624  1.00 84.89  ? 274 TYR C CA  1 
ATOM   6106  C C   . TYR C 1 274 ? 32.717  -2.991  -14.744  1.00 94.25  ? 274 TYR C C   1 
ATOM   6107  O O   . TYR C 1 274 ? 33.548  -2.362  -14.084  1.00 91.12  ? 274 TYR C O   1 
ATOM   6108  C CB  . TYR C 1 274 ? 31.638  -4.876  -13.486  1.00 69.76  ? 274 TYR C CB  1 
ATOM   6109  C CG  . TYR C 1 274 ? 30.209  -4.416  -13.667  1.00 88.00  ? 274 TYR C CG  1 
ATOM   6110  C CD1 . TYR C 1 274 ? 29.321  -5.137  -14.455  1.00 88.28  ? 274 TYR C CD1 1 
ATOM   6111  C CD2 . TYR C 1 274 ? 29.742  -3.274  -13.030  1.00 93.08  ? 274 TYR C CD2 1 
ATOM   6112  C CE1 . TYR C 1 274 ? 28.011  -4.723  -14.616  1.00 89.80  ? 274 TYR C CE1 1 
ATOM   6113  C CE2 . TYR C 1 274 ? 28.434  -2.856  -13.182  1.00 105.78 ? 274 TYR C CE2 1 
ATOM   6114  C CZ  . TYR C 1 274 ? 27.574  -3.582  -13.978  1.00 95.63  ? 274 TYR C CZ  1 
ATOM   6115  O OH  . TYR C 1 274 ? 26.272  -3.167  -14.133  1.00 82.99  ? 274 TYR C OH  1 
ATOM   6116  N N   . GLY C 1 275 ? 31.880  -2.400  -15.597  1.00 94.45  ? 275 GLY C N   1 
ATOM   6117  C CA  . GLY C 1 275 ? 32.027  -0.991  -15.911  1.00 100.22 ? 275 GLY C CA  1 
ATOM   6118  C C   . GLY C 1 275 ? 30.795  -0.120  -15.757  1.00 95.56  ? 275 GLY C C   1 
ATOM   6119  O O   . GLY C 1 275 ? 30.804  1.036   -16.196  1.00 108.64 ? 275 GLY C O   1 
ATOM   6120  N N   . HIS C 1 276 ? 29.736  -0.648  -15.138  1.00 88.10  ? 276 HIS C N   1 
ATOM   6121  C CA  . HIS C 1 276 ? 28.493  0.096   -14.909  1.00 103.07 ? 276 HIS C CA  1 
ATOM   6122  C C   . HIS C 1 276 ? 27.927  0.658   -16.213  1.00 102.13 ? 276 HIS C C   1 
ATOM   6123  O O   . HIS C 1 276 ? 27.514  1.817   -16.292  1.00 98.04  ? 276 HIS C O   1 
ATOM   6124  C CB  . HIS C 1 276 ? 28.694  1.207   -13.875  1.00 103.53 ? 276 HIS C CB  1 
ATOM   6125  C CG  . HIS C 1 276 ? 28.980  0.701   -12.495  1.00 109.69 ? 276 HIS C CG  1 
ATOM   6126  N ND1 . HIS C 1 276 ? 30.185  0.131   -12.147  1.00 107.93 ? 276 HIS C ND1 1 
ATOM   6127  C CD2 . HIS C 1 276 ? 28.215  0.675   -11.379  1.00 97.72  ? 276 HIS C CD2 1 
ATOM   6128  C CE1 . HIS C 1 276 ? 30.151  -0.224  -10.875  1.00 107.86 ? 276 HIS C CE1 1 
ATOM   6129  N NE2 . HIS C 1 276 ? 28.966  0.095   -10.386  1.00 114.31 ? 276 HIS C NE2 1 
ATOM   6130  N N   . CYS C 1 277 ? 27.911  -0.178  -17.242  1.00 93.45  ? 277 CYS C N   1 
ATOM   6131  C CA  . CYS C 1 277 ? 27.432  0.185   -18.567  1.00 83.44  ? 277 CYS C CA  1 
ATOM   6132  C C   . CYS C 1 277 ? 26.302  -0.754  -18.980  1.00 89.10  ? 277 CYS C C   1 
ATOM   6133  O O   . CYS C 1 277 ? 25.942  -1.688  -18.258  1.00 99.62  ? 277 CYS C O   1 
ATOM   6134  C CB  . CYS C 1 277 ? 28.583  0.157   -19.577  1.00 88.82  ? 277 CYS C CB  1 
ATOM   6135  S SG  . CYS C 1 277 ? 29.768  -1.189  -19.312  1.00 140.90 ? 277 CYS C SG  1 
ATOM   6136  N N   . ASN C 1 278 ? 25.729  -0.487  -20.151  1.00 86.03  ? 278 ASN C N   1 
ATOM   6137  C CA  . ASN C 1 278 ? 24.693  -1.335  -20.718  1.00 76.15  ? 278 ASN C CA  1 
ATOM   6138  C C   . ASN C 1 278 ? 24.964  -1.529  -22.202  1.00 77.28  ? 278 ASN C C   1 
ATOM   6139  O O   . ASN C 1 278 ? 25.486  -0.637  -22.875  1.00 95.44  ? 278 ASN C O   1 
ATOM   6140  C CB  . ASN C 1 278 ? 23.292  -0.745  -20.515  1.00 76.62  ? 278 ASN C CB  1 
ATOM   6141  C CG  . ASN C 1 278 ? 22.193  -1.719  -20.886  1.00 82.25  ? 278 ASN C CG  1 
ATOM   6142  O OD1 . ASN C 1 278 ? 21.789  -2.549  -20.075  1.00 83.58  ? 278 ASN C OD1 1 
ATOM   6143  N ND2 . ASN C 1 278 ? 21.705  -1.626  -22.119  1.00 97.98  ? 278 ASN C ND2 1 
ATOM   6144  N N   . THR C 1 279 ? 24.602  -2.705  -22.707  1.00 87.92  ? 279 THR C N   1 
ATOM   6145  C CA  . THR C 1 279 ? 24.852  -3.036  -24.102  1.00 76.94  ? 279 THR C CA  1 
ATOM   6146  C C   . THR C 1 279 ? 23.888  -4.132  -24.529  1.00 76.66  ? 279 THR C C   1 
ATOM   6147  O O   . THR C 1 279 ? 23.239  -4.776  -23.701  1.00 81.14  ? 279 THR C O   1 
ATOM   6148  C CB  . THR C 1 279 ? 26.303  -3.481  -24.321  1.00 78.19  ? 279 THR C CB  1 
ATOM   6149  O OG1 . THR C 1 279 ? 26.658  -3.301  -25.698  1.00 89.79  ? 279 THR C OG1 1 
ATOM   6150  C CG2 . THR C 1 279 ? 26.467  -4.949  -23.953  1.00 76.89  ? 279 THR C CG2 1 
ATOM   6151  N N   . LYS C 1 280 ? 23.793  -4.324  -25.843  1.00 78.86  ? 280 LYS C N   1 
ATOM   6152  C CA  . LYS C 1 280 ? 23.035  -5.424  -26.419  1.00 69.42  ? 280 LYS C CA  1 
ATOM   6153  C C   . LYS C 1 280 ? 23.929  -6.534  -26.953  1.00 77.10  ? 280 LYS C C   1 
ATOM   6154  O O   . LYS C 1 280 ? 23.415  -7.547  -27.438  1.00 73.20  ? 280 LYS C O   1 
ATOM   6155  C CB  . LYS C 1 280 ? 22.121  -4.908  -27.536  1.00 73.40  ? 280 LYS C CB  1 
ATOM   6156  C CG  . LYS C 1 280 ? 21.009  -4.008  -27.033  1.00 92.92  ? 280 LYS C CG  1 
ATOM   6157  C CD  . LYS C 1 280 ? 20.799  -2.818  -27.948  1.00 94.66  ? 280 LYS C CD  1 
ATOM   6158  C CE  . LYS C 1 280 ? 20.230  -1.647  -27.169  1.00 108.40 ? 280 LYS C CE  1 
ATOM   6159  N NZ  . LYS C 1 280 ? 21.146  -1.263  -26.057  1.00 91.26  ? 280 LYS C NZ  1 
ATOM   6160  N N   . CYS C 1 281 ? 25.247  -6.373  -26.867  1.00 64.24  ? 281 CYS C N   1 
ATOM   6161  C CA  . CYS C 1 281 ? 26.183  -7.386  -27.342  1.00 64.88  ? 281 CYS C CA  1 
ATOM   6162  C C   . CYS C 1 281 ? 27.452  -7.304  -26.509  1.00 67.28  ? 281 CYS C C   1 
ATOM   6163  O O   . CYS C 1 281 ? 28.119  -6.264  -26.497  1.00 71.79  ? 281 CYS C O   1 
ATOM   6164  C CB  . CYS C 1 281 ? 26.500  -7.193  -28.825  1.00 77.18  ? 281 CYS C CB  1 
ATOM   6165  S SG  . CYS C 1 281 ? 27.662  -8.407  -29.468  1.00 99.00  ? 281 CYS C SG  1 
ATOM   6166  N N   . GLN C 1 282 ? 27.785  -8.397  -25.823  1.00 57.23  ? 282 GLN C N   1 
ATOM   6167  C CA  . GLN C 1 282 ? 28.937  -8.466  -24.937  1.00 67.57  ? 282 GLN C CA  1 
ATOM   6168  C C   . GLN C 1 282 ? 29.912  -9.529  -25.422  1.00 66.15  ? 282 GLN C C   1 
ATOM   6169  O O   . GLN C 1 282 ? 29.506  -10.638 -25.784  1.00 74.37  ? 282 GLN C O   1 
ATOM   6170  C CB  . GLN C 1 282 ? 28.514  -8.788  -23.500  1.00 66.02  ? 282 GLN C CB  1 
ATOM   6171  C CG  . GLN C 1 282 ? 29.678  -8.915  -22.531  1.00 72.99  ? 282 GLN C CG  1 
ATOM   6172  C CD  . GLN C 1 282 ? 30.119  -7.574  -21.985  1.00 80.73  ? 282 GLN C CD  1 
ATOM   6173  O OE1 . GLN C 1 282 ? 31.301  -7.231  -22.021  1.00 84.40  ? 282 GLN C OE1 1 
ATOM   6174  N NE2 . GLN C 1 282 ? 29.163  -6.801  -21.479  1.00 78.47  ? 282 GLN C NE2 1 
ATOM   6175  N N   . THR C 1 283 ? 31.196  -9.190  -25.412  1.00 65.21  ? 283 THR C N   1 
ATOM   6176  C CA  . THR C 1 283 ? 32.285  -10.094 -25.737  1.00 66.33  ? 283 THR C CA  1 
ATOM   6177  C C   . THR C 1 283 ? 33.213  -10.212 -24.533  1.00 67.96  ? 283 THR C C   1 
ATOM   6178  O O   . THR C 1 283 ? 33.216  -9.339  -23.657  1.00 65.19  ? 283 THR C O   1 
ATOM   6179  C CB  . THR C 1 283 ? 33.075  -9.595  -26.958  1.00 67.24  ? 283 THR C CB  1 
ATOM   6180  O OG1 . THR C 1 283 ? 33.918  -8.504  -26.570  1.00 72.11  ? 283 THR C OG1 1 
ATOM   6181  C CG2 . THR C 1 283 ? 32.128  -9.130  -28.054  1.00 63.56  ? 283 THR C CG2 1 
ATOM   6182  N N   . PRO C 1 284 ? 34.008  -11.284 -24.448  1.00 75.22  ? 284 PRO C N   1 
ATOM   6183  C CA  . PRO C 1 284 ? 34.912  -11.429 -23.293  1.00 64.54  ? 284 PRO C CA  1 
ATOM   6184  C C   . PRO C 1 284 ? 35.941  -10.320 -23.184  1.00 72.91  ? 284 PRO C C   1 
ATOM   6185  O O   . PRO C 1 284 ? 36.520  -10.141 -22.104  1.00 76.77  ? 284 PRO C O   1 
ATOM   6186  C CB  . PRO C 1 284 ? 35.579  -12.791 -23.536  1.00 70.80  ? 284 PRO C CB  1 
ATOM   6187  C CG  . PRO C 1 284 ? 34.631  -13.521 -24.427  1.00 66.41  ? 284 PRO C CG  1 
ATOM   6188  C CD  . PRO C 1 284 ? 34.052  -12.469 -25.321  1.00 69.78  ? 284 PRO C CD  1 
ATOM   6189  N N   . VAL C 1 285 ? 36.199  -9.577  -24.265  1.00 74.47  ? 285 VAL C N   1 
ATOM   6190  C CA  . VAL C 1 285 ? 37.136  -8.461  -24.217  1.00 67.85  ? 285 VAL C CA  1 
ATOM   6191  C C   . VAL C 1 285 ? 36.438  -7.119  -24.050  1.00 69.85  ? 285 VAL C C   1 
ATOM   6192  O O   . VAL C 1 285 ? 37.116  -6.110  -23.818  1.00 83.09  ? 285 VAL C O   1 
ATOM   6193  C CB  . VAL C 1 285 ? 38.032  -8.427  -25.474  1.00 59.29  ? 285 VAL C CB  1 
ATOM   6194  C CG1 . VAL C 1 285 ? 38.664  -9.788  -25.705  1.00 60.17  ? 285 VAL C CG1 1 
ATOM   6195  C CG2 . VAL C 1 285 ? 37.235  -7.978  -26.690  1.00 60.06  ? 285 VAL C CG2 1 
ATOM   6196  N N   . GLY C 1 286 ? 35.124  -7.071  -24.157  1.00 74.41  ? 286 GLY C N   1 
ATOM   6197  C CA  . GLY C 1 286 ? 34.394  -5.829  -24.007  1.00 75.38  ? 286 GLY C CA  1 
ATOM   6198  C C   . GLY C 1 286 ? 33.132  -5.834  -24.846  1.00 72.97  ? 286 GLY C C   1 
ATOM   6199  O O   . GLY C 1 286 ? 32.943  -6.644  -25.754  1.00 76.28  ? 286 GLY C O   1 
ATOM   6200  N N   . ALA C 1 287 ? 32.256  -4.892  -24.525  1.00 70.14  ? 287 ALA C N   1 
ATOM   6201  C CA  . ALA C 1 287 ? 30.995  -4.755  -25.232  1.00 75.61  ? 287 ALA C CA  1 
ATOM   6202  C C   . ALA C 1 287 ? 31.191  -3.989  -26.534  1.00 81.94  ? 287 ALA C C   1 
ATOM   6203  O O   . ALA C 1 287 ? 32.065  -3.125  -26.647  1.00 81.81  ? 287 ALA C O   1 
ATOM   6204  C CB  . ALA C 1 287 ? 29.970  -4.029  -24.351  1.00 78.10  ? 287 ALA C CB  1 
ATOM   6205  N N   . ILE C 1 288 ? 30.360  -4.317  -27.525  1.00 78.93  ? 288 ILE C N   1 
ATOM   6206  C CA  . ILE C 1 288 ? 30.422  -3.694  -28.839  1.00 82.43  ? 288 ILE C CA  1 
ATOM   6207  C C   . ILE C 1 288 ? 29.033  -3.196  -29.216  1.00 89.41  ? 288 ILE C C   1 
ATOM   6208  O O   . ILE C 1 288 ? 28.017  -3.649  -28.686  1.00 83.81  ? 288 ILE C O   1 
ATOM   6209  C CB  . ILE C 1 288 ? 30.952  -4.651  -29.931  1.00 71.63  ? 288 ILE C CB  1 
ATOM   6210  C CG1 . ILE C 1 288 ? 29.887  -5.684  -30.305  1.00 62.84  ? 288 ILE C CG1 1 
ATOM   6211  C CG2 . ILE C 1 288 ? 32.223  -5.347  -29.465  1.00 73.14  ? 288 ILE C CG2 1 
ATOM   6212  C CD1 . ILE C 1 288 ? 30.312  -6.622  -31.417  1.00 67.53  ? 288 ILE C CD1 1 
ATOM   6213  N N   . ASN C 1 289 ? 29.003  -2.243  -30.145  1.00 93.73  ? 289 ASN C N   1 
ATOM   6214  C CA  . ASN C 1 289 ? 27.743  -1.741  -30.669  1.00 102.16 ? 289 ASN C CA  1 
ATOM   6215  C C   . ASN C 1 289 ? 27.173  -2.716  -31.697  1.00 94.62  ? 289 ASN C C   1 
ATOM   6216  O O   . ASN C 1 289 ? 27.891  -3.520  -32.300  1.00 91.52  ? 289 ASN C O   1 
ATOM   6217  C CB  . ASN C 1 289 ? 27.932  -0.358  -31.295  1.00 99.51  ? 289 ASN C CB  1 
ATOM   6218  C CG  . ASN C 1 289 ? 28.435  0.673   -30.297  1.00 110.59 ? 289 ASN C CG  1 
ATOM   6219  O OD1 . ASN C 1 289 ? 28.104  0.620   -29.113  1.00 122.20 ? 289 ASN C OD1 1 
ATOM   6220  N ND2 . ASN C 1 289 ? 29.237  1.621   -30.775  1.00 121.89 ? 289 ASN C ND2 1 
ATOM   6221  N N   . SER C 1 290 ? 25.856  -2.637  -31.890  1.00 81.03  ? 290 SER C N   1 
ATOM   6222  C CA  . SER C 1 290 ? 25.142  -3.537  -32.787  1.00 98.48  ? 290 SER C CA  1 
ATOM   6223  C C   . SER C 1 290 ? 24.471  -2.794  -33.938  1.00 101.50 ? 290 SER C C   1 
ATOM   6224  O O   . SER C 1 290 ? 23.548  -3.328  -34.561  1.00 97.30  ? 290 SER C O   1 
ATOM   6225  C CB  . SER C 1 290 ? 24.111  -4.354  -32.005  1.00 92.70  ? 290 SER C CB  1 
ATOM   6226  O OG  . SER C 1 290 ? 23.470  -3.557  -31.025  1.00 105.83 ? 290 SER C OG  1 
ATOM   6227  N N   . SER C 1 291 ? 24.912  -1.569  -34.229  1.00 110.22 ? 291 SER C N   1 
ATOM   6228  C CA  . SER C 1 291 ? 24.326  -0.811  -35.329  1.00 88.23  ? 291 SER C CA  1 
ATOM   6229  C C   . SER C 1 291 ? 24.685  -1.428  -36.676  1.00 89.67  ? 291 SER C C   1 
ATOM   6230  O O   . SER C 1 291 ? 23.814  -1.641  -37.528  1.00 87.23  ? 291 SER C O   1 
ATOM   6231  C CB  . SER C 1 291 ? 24.794  0.643   -35.266  1.00 94.68  ? 291 SER C CB  1 
ATOM   6232  O OG  . SER C 1 291 ? 24.870  1.096   -33.926  1.00 106.35 ? 291 SER C OG  1 
ATOM   6233  N N   . MET C 1 292 ? 25.964  -1.723  -36.883  1.00 87.14  ? 292 MET C N   1 
ATOM   6234  C CA  . MET C 1 292 ? 26.444  -2.249  -38.148  1.00 86.86  ? 292 MET C CA  1 
ATOM   6235  C C   . MET C 1 292 ? 26.119  -3.734  -38.282  1.00 76.89  ? 292 MET C C   1 
ATOM   6236  O O   . MET C 1 292 ? 25.936  -4.436  -37.284  1.00 82.65  ? 292 MET C O   1 
ATOM   6237  C CB  . MET C 1 292 ? 27.947  -2.018  -38.266  1.00 91.11  ? 292 MET C CB  1 
ATOM   6238  C CG  . MET C 1 292 ? 28.334  -0.549  -38.297  1.00 91.32  ? 292 MET C CG  1 
ATOM   6239  S SD  . MET C 1 292 ? 27.505  0.342   -39.629  1.00 121.03 ? 292 MET C SD  1 
ATOM   6240  C CE  . MET C 1 292 ? 26.822  1.734   -38.733  1.00 106.45 ? 292 MET C CE  1 
ATOM   6241  N N   . PRO C 1 293 ? 26.033  -4.240  -39.517  1.00 71.69  ? 293 PRO C N   1 
ATOM   6242  C CA  . PRO C 1 293 ? 25.695  -5.657  -39.709  1.00 67.40  ? 293 PRO C CA  1 
ATOM   6243  C C   . PRO C 1 293 ? 26.851  -6.619  -39.487  1.00 71.34  ? 293 PRO C C   1 
ATOM   6244  O O   . PRO C 1 293 ? 26.609  -7.833  -39.427  1.00 73.80  ? 293 PRO C O   1 
ATOM   6245  C CB  . PRO C 1 293 ? 25.225  -5.701  -41.169  1.00 64.38  ? 293 PRO C CB  1 
ATOM   6246  C CG  . PRO C 1 293 ? 25.980  -4.598  -41.826  1.00 66.40  ? 293 PRO C CG  1 
ATOM   6247  C CD  . PRO C 1 293 ? 26.102  -3.509  -40.795  1.00 63.20  ? 293 PRO C CD  1 
ATOM   6248  N N   . PHE C 1 294 ? 28.087  -6.136  -39.365  1.00 65.16  ? 294 PHE C N   1 
ATOM   6249  C CA  . PHE C 1 294 ? 29.239  -7.018  -39.238  1.00 69.36  ? 294 PHE C CA  1 
ATOM   6250  C C   . PHE C 1 294 ? 30.188  -6.488  -38.172  1.00 71.62  ? 294 PHE C C   1 
ATOM   6251  O O   . PHE C 1 294 ? 30.216  -5.292  -37.872  1.00 77.00  ? 294 PHE C O   1 
ATOM   6252  C CB  . PHE C 1 294 ? 29.981  -7.170  -40.573  1.00 65.90  ? 294 PHE C CB  1 
ATOM   6253  C CG  . PHE C 1 294 ? 29.108  -7.643  -41.700  1.00 76.63  ? 294 PHE C CG  1 
ATOM   6254  C CD1 . PHE C 1 294 ? 28.764  -8.979  -41.813  1.00 72.93  ? 294 PHE C CD1 1 
ATOM   6255  C CD2 . PHE C 1 294 ? 28.630  -6.751  -42.645  1.00 73.60  ? 294 PHE C CD2 1 
ATOM   6256  C CE1 . PHE C 1 294 ? 27.959  -9.418  -42.847  1.00 72.01  ? 294 PHE C CE1 1 
ATOM   6257  C CE2 . PHE C 1 294 ? 27.824  -7.183  -43.681  1.00 65.85  ? 294 PHE C CE2 1 
ATOM   6258  C CZ  . PHE C 1 294 ? 27.488  -8.519  -43.782  1.00 71.28  ? 294 PHE C CZ  1 
ATOM   6259  N N   . HIS C 1 295 ? 30.969  -7.405  -37.601  1.00 64.01  ? 295 HIS C N   1 
ATOM   6260  C CA  . HIS C 1 295 ? 31.993  -7.058  -36.626  1.00 54.56  ? 295 HIS C CA  1 
ATOM   6261  C C   . HIS C 1 295 ? 33.092  -8.111  -36.677  1.00 67.30  ? 295 HIS C C   1 
ATOM   6262  O O   . HIS C 1 295 ? 32.897  -9.215  -37.192  1.00 58.08  ? 295 HIS C O   1 
ATOM   6263  C CB  . HIS C 1 295 ? 31.417  -6.944  -35.209  1.00 71.59  ? 295 HIS C CB  1 
ATOM   6264  C CG  . HIS C 1 295 ? 31.241  -8.260  -34.519  1.00 77.40  ? 295 HIS C CG  1 
ATOM   6265  N ND1 . HIS C 1 295 ? 32.205  -8.806  -33.700  1.00 72.47  ? 295 HIS C ND1 1 
ATOM   6266  C CD2 . HIS C 1 295 ? 30.214  -9.142  -34.530  1.00 73.86  ? 295 HIS C CD2 1 
ATOM   6267  C CE1 . HIS C 1 295 ? 31.779  -9.966  -33.234  1.00 72.14  ? 295 HIS C CE1 1 
ATOM   6268  N NE2 . HIS C 1 295 ? 30.573  -10.194 -33.723  1.00 72.49  ? 295 HIS C NE2 1 
ATOM   6269  N N   . ASN C 1 296 ? 34.261  -7.754  -36.136  1.00 56.02  ? 296 ASN C N   1 
ATOM   6270  C CA  . ASN C 1 296 ? 35.416  -8.646  -36.147  1.00 62.27  ? 296 ASN C CA  1 
ATOM   6271  C C   . ASN C 1 296 ? 36.104  -8.723  -34.787  1.00 64.59  ? 296 ASN C C   1 
ATOM   6272  O O   . ASN C 1 296 ? 37.266  -9.136  -34.713  1.00 73.20  ? 296 ASN C O   1 
ATOM   6273  C CB  . ASN C 1 296 ? 36.425  -8.214  -37.215  1.00 62.14  ? 296 ASN C CB  1 
ATOM   6274  C CG  . ASN C 1 296 ? 36.942  -6.799  -36.999  1.00 73.21  ? 296 ASN C CG  1 
ATOM   6275  O OD1 . ASN C 1 296 ? 36.580  -6.129  -36.031  1.00 83.41  ? 296 ASN C OD1 1 
ATOM   6276  N ND2 . ASN C 1 296 ? 37.802  -6.343  -37.902  1.00 72.29  ? 296 ASN C ND2 1 
ATOM   6277  N N   . ILE C 1 297 ? 35.414  -8.342  -33.712  1.00 63.87  ? 297 ILE C N   1 
ATOM   6278  C CA  . ILE C 1 297 ? 36.065  -8.232  -32.409  1.00 66.52  ? 297 ILE C CA  1 
ATOM   6279  C C   . ILE C 1 297 ? 36.360  -9.614  -31.835  1.00 74.35  ? 297 ILE C C   1 
ATOM   6280  O O   . ILE C 1 297 ? 37.516  -9.957  -31.559  1.00 72.35  ? 297 ILE C O   1 
ATOM   6281  C CB  . ILE C 1 297 ? 35.206  -7.398  -31.441  1.00 67.05  ? 297 ILE C CB  1 
ATOM   6282  C CG1 . ILE C 1 297 ? 35.176  -5.928  -31.872  1.00 59.89  ? 297 ILE C CG1 1 
ATOM   6283  C CG2 . ILE C 1 297 ? 35.729  -7.531  -30.020  1.00 64.96  ? 297 ILE C CG2 1 
ATOM   6284  C CD1 . ILE C 1 297 ? 33.999  -5.561  -32.753  1.00 71.88  ? 297 ILE C CD1 1 
ATOM   6285  N N   . HIS C 1 298 ? 35.324  -10.429 -31.649  1.00 78.56  ? 298 HIS C N   1 
ATOM   6286  C CA  . HIS C 1 298 ? 35.475  -11.682 -30.924  1.00 73.77  ? 298 HIS C CA  1 
ATOM   6287  C C   . HIS C 1 298 ? 34.356  -12.621 -31.344  1.00 75.70  ? 298 HIS C C   1 
ATOM   6288  O O   . HIS C 1 298 ? 33.255  -12.157 -31.655  1.00 83.93  ? 298 HIS C O   1 
ATOM   6289  C CB  . HIS C 1 298 ? 35.430  -11.438 -29.408  1.00 76.95  ? 298 HIS C CB  1 
ATOM   6290  C CG  . HIS C 1 298 ? 36.127  -12.487 -28.603  1.00 73.08  ? 298 HIS C CG  1 
ATOM   6291  N ND1 . HIS C 1 298 ? 35.516  -13.661 -28.219  1.00 79.78  ? 298 HIS C ND1 1 
ATOM   6292  C CD2 . HIS C 1 298 ? 37.383  -12.534 -28.100  1.00 75.35  ? 298 HIS C CD2 1 
ATOM   6293  C CE1 . HIS C 1 298 ? 36.367  -14.389 -27.519  1.00 79.19  ? 298 HIS C CE1 1 
ATOM   6294  N NE2 . HIS C 1 298 ? 37.507  -13.728 -27.432  1.00 85.62  ? 298 HIS C NE2 1 
ATOM   6295  N N   . PRO C 1 299 ? 34.600  -13.938 -31.366  1.00 67.97  ? 299 PRO C N   1 
ATOM   6296  C CA  . PRO C 1 299 ? 33.521  -14.877 -31.717  1.00 62.83  ? 299 PRO C CA  1 
ATOM   6297  C C   . PRO C 1 299 ? 32.624  -15.274 -30.552  1.00 72.51  ? 299 PRO C C   1 
ATOM   6298  O O   . PRO C 1 299 ? 31.489  -15.707 -30.790  1.00 60.58  ? 299 PRO C O   1 
ATOM   6299  C CB  . PRO C 1 299 ? 34.289  -16.090 -32.263  1.00 55.80  ? 299 PRO C CB  1 
ATOM   6300  C CG  . PRO C 1 299 ? 35.571  -16.063 -31.519  1.00 52.73  ? 299 PRO C CG  1 
ATOM   6301  C CD  . PRO C 1 299 ? 35.916  -14.604 -31.325  1.00 53.17  ? 299 PRO C CD  1 
ATOM   6302  N N   . LEU C 1 300 ? 33.083  -15.141 -29.310  1.00 68.43  ? 300 LEU C N   1 
ATOM   6303  C CA  . LEU C 1 300 ? 32.325  -15.613 -28.148  1.00 65.72  ? 300 LEU C CA  1 
ATOM   6304  C C   . LEU C 1 300 ? 31.433  -14.489 -27.617  1.00 67.38  ? 300 LEU C C   1 
ATOM   6305  O O   . LEU C 1 300 ? 31.630  -13.946 -26.530  1.00 85.19  ? 300 LEU C O   1 
ATOM   6306  C CB  . LEU C 1 300 ? 33.273  -16.131 -27.074  1.00 62.17  ? 300 LEU C CB  1 
ATOM   6307  C CG  . LEU C 1 300 ? 34.147  -17.325 -27.461  1.00 68.15  ? 300 LEU C CG  1 
ATOM   6308  C CD1 . LEU C 1 300 ? 35.207  -17.586 -26.403  1.00 60.27  ? 300 LEU C CD1 1 
ATOM   6309  C CD2 . LEU C 1 300 ? 33.296  -18.564 -27.685  1.00 55.75  ? 300 LEU C CD2 1 
ATOM   6310  N N   . THR C 1 301 ? 30.411  -14.172 -28.401  1.00 82.58  ? 301 THR C N   1 
ATOM   6311  C CA  . THR C 1 301 ? 29.518  -13.064 -28.100  1.00 71.56  ? 301 THR C CA  1 
ATOM   6312  C C   . THR C 1 301 ? 28.255  -13.550 -27.396  1.00 65.77  ? 301 THR C C   1 
ATOM   6313  O O   . THR C 1 301 ? 27.809  -14.684 -27.589  1.00 70.83  ? 301 THR C O   1 
ATOM   6314  C CB  . THR C 1 301 ? 29.135  -12.316 -29.378  1.00 72.41  ? 301 THR C CB  1 
ATOM   6315  O OG1 . THR C 1 301 ? 28.518  -13.222 -30.300  1.00 82.93  ? 301 THR C OG1 1 
ATOM   6316  C CG2 . THR C 1 301 ? 30.362  -11.695 -30.028  1.00 70.04  ? 301 THR C CG2 1 
ATOM   6317  N N   . ILE C 1 302 ? 27.684  -12.676 -26.569  1.00 67.28  ? 302 ILE C N   1 
ATOM   6318  C CA  . ILE C 1 302 ? 26.389  -12.906 -25.936  1.00 55.73  ? 302 ILE C CA  1 
ATOM   6319  C C   . ILE C 1 302 ? 25.531  -11.671 -26.168  1.00 69.37  ? 302 ILE C C   1 
ATOM   6320  O O   . ILE C 1 302 ? 25.940  -10.555 -25.824  1.00 70.10  ? 302 ILE C O   1 
ATOM   6321  C CB  . ILE C 1 302 ? 26.509  -13.193 -24.429  1.00 70.65  ? 302 ILE C CB  1 
ATOM   6322  C CG1 . ILE C 1 302 ? 27.448  -14.369 -24.164  1.00 71.41  ? 302 ILE C CG1 1 
ATOM   6323  C CG2 . ILE C 1 302 ? 25.142  -13.495 -23.841  1.00 68.48  ? 302 ILE C CG2 1 
ATOM   6324  C CD1 . ILE C 1 302 ? 27.562  -14.721 -22.692  1.00 65.44  ? 302 ILE C CD1 1 
ATOM   6325  N N   . GLY C 1 303 ? 24.343  -11.865 -26.747  1.00 76.79  ? 303 GLY C N   1 
ATOM   6326  C CA  . GLY C 1 303 ? 23.403  -10.792 -26.978  1.00 72.38  ? 303 GLY C CA  1 
ATOM   6327  C C   . GLY C 1 303 ? 22.956  -10.764 -28.424  1.00 65.82  ? 303 GLY C C   1 
ATOM   6328  O O   . GLY C 1 303 ? 23.093  -11.749 -29.158  1.00 78.58  ? 303 GLY C O   1 
ATOM   6329  N N   . GLU C 1 304 ? 22.406  -9.622  -28.830  1.00 71.50  ? 304 GLU C N   1 
ATOM   6330  C CA  . GLU C 1 304 ? 22.006  -9.389  -30.217  1.00 76.50  ? 304 GLU C CA  1 
ATOM   6331  C C   . GLU C 1 304 ? 23.181  -8.711  -30.910  1.00 73.61  ? 304 GLU C C   1 
ATOM   6332  O O   . GLU C 1 304 ? 23.419  -7.514  -30.731  1.00 82.23  ? 304 GLU C O   1 
ATOM   6333  C CB  . GLU C 1 304 ? 20.740  -8.542  -30.285  1.00 73.06  ? 304 GLU C CB  1 
ATOM   6334  C CG  . GLU C 1 304 ? 19.581  -9.079  -29.458  1.00 72.65  ? 304 GLU C CG  1 
ATOM   6335  C CD  . GLU C 1 304 ? 19.625  -8.601  -28.020  1.00 91.32  ? 304 GLU C CD  1 
ATOM   6336  O OE1 . GLU C 1 304 ? 20.121  -7.481  -27.784  1.00 95.19  ? 304 GLU C OE1 1 
ATOM   6337  O OE2 . GLU C 1 304 ? 19.174  -9.347  -27.126  1.00 91.26  ? 304 GLU C OE2 1 
ATOM   6338  N N   . CYS C 1 305 ? 23.918  -9.474  -31.707  1.00 71.05  ? 305 CYS C N   1 
ATOM   6339  C CA  . CYS C 1 305 ? 25.225  -9.059  -32.183  1.00 73.51  ? 305 CYS C CA  1 
ATOM   6340  C C   . CYS C 1 305 ? 25.290  -9.046  -33.704  1.00 74.63  ? 305 CYS C C   1 
ATOM   6341  O O   . CYS C 1 305 ? 24.521  -9.744  -34.377  1.00 75.88  ? 305 CYS C O   1 
ATOM   6342  C CB  . CYS C 1 305 ? 26.315  -9.998  -31.647  1.00 78.97  ? 305 CYS C CB  1 
ATOM   6343  S SG  . CYS C 1 305 ? 26.496  -10.021 -29.856  1.00 91.40  ? 305 CYS C SG  1 
ATOM   6344  N N   . PRO C 1 306 ? 26.196  -8.256  -34.279  1.00 71.11  ? 306 PRO C N   1 
ATOM   6345  C CA  . PRO C 1 306 ? 26.461  -8.364  -35.716  1.00 57.13  ? 306 PRO C CA  1 
ATOM   6346  C C   . PRO C 1 306 ? 27.085  -9.709  -36.054  1.00 60.60  ? 306 PRO C C   1 
ATOM   6347  O O   . PRO C 1 306 ? 27.583  -10.432 -35.188  1.00 77.22  ? 306 PRO C O   1 
ATOM   6348  C CB  . PRO C 1 306 ? 27.438  -7.212  -35.991  1.00 64.10  ? 306 PRO C CB  1 
ATOM   6349  C CG  . PRO C 1 306 ? 27.267  -6.276  -34.842  1.00 70.39  ? 306 PRO C CG  1 
ATOM   6350  C CD  . PRO C 1 306 ? 26.928  -7.135  -33.665  1.00 69.38  ? 306 PRO C CD  1 
ATOM   6351  N N   . LYS C 1 307 ? 27.037  -10.051 -37.337  1.00 61.93  ? 307 LYS C N   1 
ATOM   6352  C CA  . LYS C 1 307 ? 27.639  -11.294 -37.796  1.00 59.71  ? 307 LYS C CA  1 
ATOM   6353  C C   . LYS C 1 307 ? 29.159  -11.185 -37.755  1.00 68.83  ? 307 LYS C C   1 
ATOM   6354  O O   . LYS C 1 307 ? 29.735  -10.207 -38.239  1.00 66.65  ? 307 LYS C O   1 
ATOM   6355  C CB  . LYS C 1 307 ? 27.164  -11.622 -39.208  1.00 65.14  ? 307 LYS C CB  1 
ATOM   6356  C CG  . LYS C 1 307 ? 25.653  -11.704 -39.340  1.00 63.00  ? 307 LYS C CG  1 
ATOM   6357  C CD  . LYS C 1 307 ? 25.066  -12.714 -38.368  1.00 65.86  ? 307 LYS C CD  1 
ATOM   6358  C CE  . LYS C 1 307 ? 23.550  -12.627 -38.340  1.00 62.36  ? 307 LYS C CE  1 
ATOM   6359  N NZ  . LYS C 1 307 ? 23.093  -11.290 -37.870  1.00 70.11  ? 307 LYS C NZ  1 
ATOM   6360  N N   . TYR C 1 308 ? 29.806  -12.188 -37.169  1.00 67.24  ? 308 TYR C N   1 
ATOM   6361  C CA  . TYR C 1 308 ? 31.258  -12.173 -37.043  1.00 64.00  ? 308 TYR C CA  1 
ATOM   6362  C C   . TYR C 1 308 ? 31.900  -12.499 -38.386  1.00 62.78  ? 308 TYR C C   1 
ATOM   6363  O O   . TYR C 1 308 ? 31.517  -13.467 -39.049  1.00 70.96  ? 308 TYR C O   1 
ATOM   6364  C CB  . TYR C 1 308 ? 31.700  -13.172 -35.971  1.00 57.39  ? 308 TYR C CB  1 
ATOM   6365  C CG  . TYR C 1 308 ? 33.180  -13.152 -35.661  1.00 54.05  ? 308 TYR C CG  1 
ATOM   6366  C CD1 . TYR C 1 308 ? 33.813  -11.981 -35.262  1.00 69.22  ? 308 TYR C CD1 1 
ATOM   6367  C CD2 . TYR C 1 308 ? 33.939  -14.311 -35.741  1.00 55.60  ? 308 TYR C CD2 1 
ATOM   6368  C CE1 . TYR C 1 308 ? 35.165  -11.965 -34.968  1.00 67.86  ? 308 TYR C CE1 1 
ATOM   6369  C CE2 . TYR C 1 308 ? 35.290  -14.305 -35.449  1.00 48.74  ? 308 TYR C CE2 1 
ATOM   6370  C CZ  . TYR C 1 308 ? 35.898  -13.129 -35.063  1.00 61.74  ? 308 TYR C CZ  1 
ATOM   6371  O OH  . TYR C 1 308 ? 37.242  -13.114 -34.770  1.00 72.97  ? 308 TYR C OH  1 
ATOM   6372  N N   . VAL C 1 309 ? 32.869  -11.680 -38.794  1.00 58.51  ? 309 VAL C N   1 
ATOM   6373  C CA  . VAL C 1 309 ? 33.539  -11.842 -40.076  1.00 73.96  ? 309 VAL C CA  1 
ATOM   6374  C C   . VAL C 1 309 ? 35.046  -11.765 -39.879  1.00 67.58  ? 309 VAL C C   1 
ATOM   6375  O O   . VAL C 1 309 ? 35.540  -11.134 -38.939  1.00 67.70  ? 309 VAL C O   1 
ATOM   6376  C CB  . VAL C 1 309 ? 33.079  -10.789 -41.109  1.00 59.64  ? 309 VAL C CB  1 
ATOM   6377  C CG1 . VAL C 1 309 ? 31.636  -11.036 -41.512  1.00 58.86  ? 309 VAL C CG1 1 
ATOM   6378  C CG2 . VAL C 1 309 ? 33.248  -9.390  -40.545  1.00 57.32  ? 309 VAL C CG2 1 
ATOM   6379  N N   . LYS C 1 310 ? 35.776  -12.421 -40.776  1.00 75.55  ? 310 LYS C N   1 
ATOM   6380  C CA  . LYS C 1 310 ? 37.239  -12.387 -40.774  1.00 70.39  ? 310 LYS C CA  1 
ATOM   6381  C C   . LYS C 1 310 ? 37.746  -11.323 -41.747  1.00 68.33  ? 310 LYS C C   1 
ATOM   6382  O O   . LYS C 1 310 ? 38.503  -11.597 -42.679  1.00 86.62  ? 310 LYS C O   1 
ATOM   6383  C CB  . LYS C 1 310 ? 37.801  -13.762 -41.118  1.00 73.25  ? 310 LYS C CB  1 
ATOM   6384  C CG  . LYS C 1 310 ? 39.020  -14.154 -40.296  1.00 79.97  ? 310 LYS C CG  1 
ATOM   6385  C CD  . LYS C 1 310 ? 39.906  -15.141 -41.038  1.00 91.84  ? 310 LYS C CD  1 
ATOM   6386  C CE  . LYS C 1 310 ? 40.819  -14.422 -42.020  1.00 93.37  ? 310 LYS C CE  1 
ATOM   6387  N NZ  . LYS C 1 310 ? 41.597  -15.370 -42.865  1.00 98.20  ? 310 LYS C NZ  1 
ATOM   6388  N N   . SER C 1 311 ? 37.314  -10.088 -41.512  1.00 65.18  ? 311 SER C N   1 
ATOM   6389  C CA  . SER C 1 311 ? 37.670  -8.962  -42.361  1.00 66.24  ? 311 SER C CA  1 
ATOM   6390  C C   . SER C 1 311 ? 38.107  -7.790  -41.496  1.00 71.21  ? 311 SER C C   1 
ATOM   6391  O O   . SER C 1 311 ? 37.664  -7.640  -40.354  1.00 87.51  ? 311 SER C O   1 
ATOM   6392  C CB  . SER C 1 311 ? 36.497  -8.541  -43.257  1.00 72.59  ? 311 SER C CB  1 
ATOM   6393  O OG  . SER C 1 311 ? 36.016  -9.638  -44.014  1.00 82.88  ? 311 SER C OG  1 
ATOM   6394  N N   . ASN C 1 312 ? 38.984  -6.959  -42.053  1.00 79.74  ? 312 ASN C N   1 
ATOM   6395  C CA  . ASN C 1 312 ? 39.483  -5.779  -41.363  1.00 80.95  ? 312 ASN C CA  1 
ATOM   6396  C C   . ASN C 1 312 ? 38.885  -4.483  -41.890  1.00 81.12  ? 312 ASN C C   1 
ATOM   6397  O O   . ASN C 1 312 ? 39.166  -3.418  -41.329  1.00 85.48  ? 312 ASN C O   1 
ATOM   6398  C CB  . ASN C 1 312 ? 41.013  -5.717  -41.461  1.00 84.53  ? 312 ASN C CB  1 
ATOM   6399  C CG  . ASN C 1 312 ? 41.695  -6.794  -40.639  1.00 101.01 ? 312 ASN C CG  1 
ATOM   6400  O OD1 . ASN C 1 312 ? 42.199  -6.532  -39.546  1.00 99.79  ? 312 ASN C OD1 1 
ATOM   6401  N ND2 . ASN C 1 312 ? 41.711  -8.014  -41.160  1.00 96.12  ? 312 ASN C ND2 1 
ATOM   6402  N N   . LYS C 1 313 ? 38.065  -4.541  -42.941  1.00 90.41  ? 313 LYS C N   1 
ATOM   6403  C CA  . LYS C 1 313 ? 37.555  -3.324  -43.560  1.00 77.22  ? 313 LYS C CA  1 
ATOM   6404  C C   . LYS C 1 313 ? 36.426  -3.620  -44.544  1.00 83.39  ? 313 LYS C C   1 
ATOM   6405  O O   . LYS C 1 313 ? 36.576  -4.468  -45.431  1.00 80.81  ? 313 LYS C O   1 
ATOM   6406  C CB  . LYS C 1 313 ? 38.703  -2.592  -44.259  1.00 85.93  ? 313 LYS C CB  1 
ATOM   6407  C CG  . LYS C 1 313 ? 38.368  -1.218  -44.775  1.00 103.80 ? 313 LYS C CG  1 
ATOM   6408  C CD  . LYS C 1 313 ? 39.636  -0.448  -45.084  1.00 94.18  ? 313 LYS C CD  1 
ATOM   6409  C CE  . LYS C 1 313 ? 40.621  -1.313  -45.859  1.00 103.17 ? 313 LYS C CE  1 
ATOM   6410  N NZ  . LYS C 1 313 ? 41.953  -0.657  -45.963  1.00 102.71 ? 313 LYS C NZ  1 
ATOM   6411  N N   . LEU C 1 314 ? 35.289  -2.928  -44.396  1.00 70.70  ? 314 LEU C N   1 
ATOM   6412  C CA  . LEU C 1 314 ? 34.157  -3.036  -45.326  1.00 79.72  ? 314 LEU C CA  1 
ATOM   6413  C C   . LEU C 1 314 ? 33.586  -1.631  -45.524  1.00 83.52  ? 314 LEU C C   1 
ATOM   6414  O O   . LEU C 1 314 ? 32.662  -1.223  -44.817  1.00 84.67  ? 314 LEU C O   1 
ATOM   6415  C CB  . LEU C 1 314 ? 33.093  -3.998  -44.806  1.00 71.01  ? 314 LEU C CB  1 
ATOM   6416  C CG  . LEU C 1 314 ? 33.430  -5.479  -44.620  1.00 73.90  ? 314 LEU C CG  1 
ATOM   6417  C CD1 . LEU C 1 314 ? 32.231  -6.220  -44.046  1.00 73.11  ? 314 LEU C CD1 1 
ATOM   6418  C CD2 . LEU C 1 314 ? 33.868  -6.108  -45.933  1.00 75.91  ? 314 LEU C CD2 1 
ATOM   6419  N N   . VAL C 1 315 ? 34.116  -0.907  -46.508  1.00 81.39  ? 315 VAL C N   1 
ATOM   6420  C CA  . VAL C 1 315 ? 33.738  0.481   -46.757  1.00 80.20  ? 315 VAL C CA  1 
ATOM   6421  C C   . VAL C 1 315 ? 32.898  0.542   -48.023  1.00 77.02  ? 315 VAL C C   1 
ATOM   6422  O O   . VAL C 1 315 ? 33.305  0.029   -49.073  1.00 81.10  ? 315 VAL C O   1 
ATOM   6423  C CB  . VAL C 1 315 ? 34.969  1.394   -46.879  1.00 80.66  ? 315 VAL C CB  1 
ATOM   6424  C CG1 . VAL C 1 315 ? 34.576  2.834   -46.640  1.00 88.96  ? 315 VAL C CG1 1 
ATOM   6425  C CG2 . VAL C 1 315 ? 36.032  0.978   -45.901  1.00 76.14  ? 315 VAL C CG2 1 
ATOM   6426  N N   . LEU C 1 316 ? 31.732  1.175   -47.926  1.00 71.01  ? 316 LEU C N   1 
ATOM   6427  C CA  . LEU C 1 316 ? 30.856  1.395   -49.068  1.00 67.84  ? 316 LEU C CA  1 
ATOM   6428  C C   . LEU C 1 316 ? 31.109  2.789   -49.626  1.00 81.16  ? 316 LEU C C   1 
ATOM   6429  O O   . LEU C 1 316 ? 30.996  3.782   -48.898  1.00 78.15  ? 316 LEU C O   1 
ATOM   6430  C CB  . LEU C 1 316 ? 29.388  1.242   -48.676  1.00 58.61  ? 316 LEU C CB  1 
ATOM   6431  C CG  . LEU C 1 316 ? 28.866  -0.176  -48.456  1.00 69.65  ? 316 LEU C CG  1 
ATOM   6432  C CD1 . LEU C 1 316 ? 27.366  -0.147  -48.220  1.00 65.87  ? 316 LEU C CD1 1 
ATOM   6433  C CD2 . LEU C 1 316 ? 29.211  -1.057  -49.644  1.00 67.74  ? 316 LEU C CD2 1 
ATOM   6434  N N   . ALA C 1 317 ? 31.447  2.861   -50.910  1.00 84.54  ? 317 ALA C N   1 
ATOM   6435  C CA  . ALA C 1 317 ? 31.623  4.147   -51.569  1.00 78.88  ? 317 ALA C CA  1 
ATOM   6436  C C   . ALA C 1 317 ? 30.267  4.806   -51.771  1.00 77.23  ? 317 ALA C C   1 
ATOM   6437  O O   . ALA C 1 317 ? 29.381  4.234   -52.414  1.00 88.27  ? 317 ALA C O   1 
ATOM   6438  C CB  . ALA C 1 317 ? 32.335  3.965   -52.906  1.00 75.83  ? 317 ALA C CB  1 
ATOM   6439  N N   . THR C 1 318 ? 30.098  6.003   -51.213  1.00 75.78  ? 318 THR C N   1 
ATOM   6440  C CA  . THR C 1 318 ? 28.886  6.786   -51.407  1.00 85.21  ? 318 THR C CA  1 
ATOM   6441  C C   . THR C 1 318 ? 29.088  7.994   -52.305  1.00 98.57  ? 318 THR C C   1 
ATOM   6442  O O   . THR C 1 318 ? 28.165  8.370   -53.029  1.00 105.78 ? 318 THR C O   1 
ATOM   6443  C CB  . THR C 1 318 ? 28.329  7.259   -50.058  1.00 75.38  ? 318 THR C CB  1 
ATOM   6444  O OG1 . THR C 1 318 ? 29.258  8.163   -49.447  1.00 93.80  ? 318 THR C OG1 1 
ATOM   6445  C CG2 . THR C 1 318 ? 28.100  6.074   -49.133  1.00 85.85  ? 318 THR C CG2 1 
ATOM   6446  N N   . GLY C 1 319 ? 30.272  8.603   -52.278  1.00 95.57  ? 319 GLY C N   1 
ATOM   6447  C CA  . GLY C 1 319 ? 30.573  9.745   -53.113  1.00 80.75  ? 319 GLY C CA  1 
ATOM   6448  C C   . GLY C 1 319 ? 31.096  9.338   -54.478  1.00 82.86  ? 319 GLY C C   1 
ATOM   6449  O O   . GLY C 1 319 ? 31.060  8.172   -54.875  1.00 86.48  ? 319 GLY C O   1 
ATOM   6450  N N   . LEU C 1 320 ? 31.596  10.333  -55.204  1.00 82.76  ? 320 LEU C N   1 
ATOM   6451  C CA  . LEU C 1 320 ? 32.081  10.127  -56.559  1.00 87.71  ? 320 LEU C CA  1 
ATOM   6452  C C   . LEU C 1 320 ? 33.578  9.832   -56.562  1.00 77.37  ? 320 LEU C C   1 
ATOM   6453  O O   . LEU C 1 320 ? 34.278  9.994   -55.561  1.00 79.27  ? 320 LEU C O   1 
ATOM   6454  C CB  . LEU C 1 320 ? 31.793  11.350  -57.433  1.00 83.43  ? 320 LEU C CB  1 
ATOM   6455  C CG  . LEU C 1 320 ? 30.378  11.927  -57.454  1.00 86.57  ? 320 LEU C CG  1 
ATOM   6456  C CD1 . LEU C 1 320 ? 30.249  13.038  -56.428  1.00 93.03  ? 320 LEU C CD1 1 
ATOM   6457  C CD2 . LEU C 1 320 ? 30.033  12.433  -58.845  1.00 90.90  ? 320 LEU C CD2 1 
ATOM   6458  N N   . ARG C 1 321 ? 34.062  9.381   -57.717  1.00 75.19  ? 321 ARG C N   1 
ATOM   6459  C CA  . ARG C 1 321 ? 35.493  9.197   -57.909  1.00 90.44  ? 321 ARG C CA  1 
ATOM   6460  C C   . ARG C 1 321 ? 36.203  10.544  -57.816  1.00 95.18  ? 321 ARG C C   1 
ATOM   6461  O O   . ARG C 1 321 ? 35.723  11.555  -58.336  1.00 97.44  ? 321 ARG C O   1 
ATOM   6462  C CB  . ARG C 1 321 ? 35.756  8.535   -59.263  1.00 65.55  ? 321 ARG C CB  1 
ATOM   6463  C CG  . ARG C 1 321 ? 36.995  7.651   -59.317  1.00 74.13  ? 321 ARG C CG  1 
ATOM   6464  C CD  . ARG C 1 321 ? 37.133  6.991   -60.686  1.00 89.15  ? 321 ARG C CD  1 
ATOM   6465  N NE  . ARG C 1 321 ? 36.166  5.917   -60.893  1.00 71.89  ? 321 ARG C NE  1 
ATOM   6466  C CZ  . ARG C 1 321 ? 36.479  4.629   -60.951  1.00 96.17  ? 321 ARG C CZ  1 
ATOM   6467  N NH1 . ARG C 1 321 ? 37.731  4.216   -60.836  1.00 94.71  ? 321 ARG C NH1 1 
ATOM   6468  N NH2 . ARG C 1 321 ? 35.513  3.734   -61.137  1.00 82.76  ? 321 ARG C NH2 1 
ATOM   6469  N N   . ASN C 1 322 ? 37.353  10.557  -57.146  1.00 102.82 ? 322 ASN C N   1 
ATOM   6470  C CA  . ASN C 1 322 ? 38.029  11.796  -56.794  1.00 101.52 ? 322 ASN C CA  1 
ATOM   6471  C C   . ASN C 1 322 ? 39.488  11.752  -57.229  1.00 109.77 ? 322 ASN C C   1 
ATOM   6472  O O   . ASN C 1 322 ? 40.113  10.688  -57.261  1.00 100.05 ? 322 ASN C O   1 
ATOM   6473  C CB  . ASN C 1 322 ? 37.953  12.050  -55.282  1.00 91.95  ? 322 ASN C CB  1 
ATOM   6474  C CG  . ASN C 1 322 ? 37.971  13.525  -54.931  1.00 103.03 ? 322 ASN C CG  1 
ATOM   6475  O OD1 . ASN C 1 322 ? 37.739  13.898  -53.783  1.00 104.88 ? 322 ASN C OD1 1 
ATOM   6476  N ND2 . ASN C 1 322 ? 38.232  14.372  -55.917  1.00 106.38 ? 322 ASN C ND2 1 
ATOM   6477  N N   . SER C 1 323 ? 40.023  12.926  -57.564  1.00 125.64 ? 323 SER C N   1 
ATOM   6478  C CA  . SER C 1 323 ? 41.438  13.107  -57.884  1.00 125.51 ? 323 SER C CA  1 
ATOM   6479  C C   . SER C 1 323 ? 41.953  14.297  -57.085  1.00 134.75 ? 323 SER C C   1 
ATOM   6480  O O   . SER C 1 323 ? 41.988  15.429  -57.587  1.00 133.58 ? 323 SER C O   1 
ATOM   6481  C CB  . SER C 1 323 ? 41.649  13.311  -59.384  1.00 107.73 ? 323 SER C CB  1 
ATOM   6482  O OG  . SER C 1 323 ? 43.023  13.482  -59.688  1.00 105.61 ? 323 SER C OG  1 
ATOM   6483  N N   . PRO C 1 324 ? 42.354  14.080  -55.822  1.00 146.80 ? 324 PRO C N   1 
ATOM   6484  C CA  . PRO C 1 324 ? 42.829  15.162  -54.955  1.00 141.03 ? 324 PRO C CA  1 
ATOM   6485  C C   . PRO C 1 324 ? 44.238  15.630  -55.311  1.00 121.50 ? 324 PRO C C   1 
ATOM   6486  O O   . PRO C 1 324 ? 44.641  16.705  -54.864  1.00 115.10 ? 324 PRO C O   1 
ATOM   6487  C CB  . PRO C 1 324 ? 42.802  14.525  -53.565  1.00 131.77 ? 324 PRO C CB  1 
ATOM   6488  C CG  . PRO C 1 324 ? 43.058  13.082  -53.827  1.00 132.26 ? 324 PRO C CG  1 
ATOM   6489  C CD  . PRO C 1 324 ? 42.382  12.774  -55.140  1.00 136.20 ? 324 PRO C CD  1 
ATOM   6490  N N   . ILE D 2 6   ? 35.761  25.227  -66.203  1.00 110.77 ? 6   ILE D N   1 
ATOM   6491  C CA  . ILE D 2 6   ? 36.372  25.603  -67.471  1.00 120.83 ? 6   ILE D CA  1 
ATOM   6492  C C   . ILE D 2 6   ? 36.862  24.349  -68.187  1.00 120.91 ? 6   ILE D C   1 
ATOM   6493  O O   . ILE D 2 6   ? 37.285  24.403  -69.342  1.00 115.83 ? 6   ILE D O   1 
ATOM   6494  C CB  . ILE D 2 6   ? 37.522  26.610  -67.258  1.00 111.36 ? 6   ILE D CB  1 
ATOM   6495  C CG1 . ILE D 2 6   ? 37.823  27.371  -68.551  1.00 105.47 ? 6   ILE D CG1 1 
ATOM   6496  C CG2 . ILE D 2 6   ? 38.769  25.897  -66.761  1.00 92.48  ? 6   ILE D CG2 1 
ATOM   6497  C CD1 . ILE D 2 6   ? 36.659  28.192  -69.059  1.00 115.99 ? 6   ILE D CD1 1 
ATOM   6498  N N   . ALA D 2 7   ? 36.784  23.211  -67.494  1.00 127.67 ? 7   ALA D N   1 
ATOM   6499  C CA  . ALA D 2 7   ? 37.319  21.950  -68.000  1.00 125.18 ? 7   ALA D CA  1 
ATOM   6500  C C   . ALA D 2 7   ? 36.247  21.050  -68.611  1.00 131.63 ? 7   ALA D C   1 
ATOM   6501  O O   . ALA D 2 7   ? 36.356  20.671  -69.780  1.00 141.26 ? 7   ALA D O   1 
ATOM   6502  C CB  . ALA D 2 7   ? 38.066  21.216  -66.876  1.00 119.63 ? 7   ALA D CB  1 
ATOM   6503  N N   . GLY D 2 8   ? 35.210  20.700  -67.848  1.00 126.66 ? 8   GLY D N   1 
ATOM   6504  C CA  . GLY D 2 8   ? 34.221  19.724  -68.283  1.00 107.89 ? 8   GLY D CA  1 
ATOM   6505  C C   . GLY D 2 8   ? 34.469  18.358  -67.664  1.00 121.37 ? 8   GLY D C   1 
ATOM   6506  O O   . GLY D 2 8   ? 35.433  18.140  -66.927  1.00 135.73 ? 8   GLY D O   1 
ATOM   6507  N N   . PHE D 2 9   ? 33.572  17.411  -67.966  1.00 113.48 ? 9   PHE D N   1 
ATOM   6508  C CA  . PHE D 2 9   ? 33.694  16.097  -67.339  1.00 104.91 ? 9   PHE D CA  1 
ATOM   6509  C C   . PHE D 2 9   ? 34.812  15.265  -67.968  1.00 102.65 ? 9   PHE D C   1 
ATOM   6510  O O   . PHE D 2 9   ? 35.370  14.381  -67.303  1.00 114.94 ? 9   PHE D O   1 
ATOM   6511  C CB  . PHE D 2 9   ? 32.353  15.343  -67.345  1.00 95.73  ? 9   PHE D CB  1 
ATOM   6512  C CG  . PHE D 2 9   ? 31.886  14.840  -68.696  1.00 97.48  ? 9   PHE D CG  1 
ATOM   6513  C CD1 . PHE D 2 9   ? 30.677  15.283  -69.240  1.00 98.49  ? 9   PHE D CD1 1 
ATOM   6514  C CD2 . PHE D 2 9   ? 32.630  13.887  -69.395  1.00 111.95 ? 9   PHE D CD2 1 
ATOM   6515  C CE1 . PHE D 2 9   ? 30.224  14.807  -70.473  1.00 103.46 ? 9   PHE D CE1 1 
ATOM   6516  C CE2 . PHE D 2 9   ? 32.209  13.414  -70.620  1.00 113.03 ? 9   PHE D CE2 1 
ATOM   6517  C CZ  . PHE D 2 9   ? 30.996  13.865  -71.169  1.00 94.47  ? 9   PHE D CZ  1 
ATOM   6518  N N   . ILE D 2 10  ? 35.166  15.534  -69.232  1.00 100.60 ? 10  ILE D N   1 
ATOM   6519  C CA  . ILE D 2 10  ? 36.188  14.733  -69.908  1.00 119.65 ? 10  ILE D CA  1 
ATOM   6520  C C   . ILE D 2 10  ? 37.523  14.829  -69.174  1.00 128.30 ? 10  ILE D C   1 
ATOM   6521  O O   . ILE D 2 10  ? 38.236  13.829  -69.019  1.00 135.85 ? 10  ILE D O   1 
ATOM   6522  C CB  . ILE D 2 10  ? 36.306  15.160  -71.383  1.00 119.09 ? 10  ILE D CB  1 
ATOM   6523  C CG1 . ILE D 2 10  ? 35.136  14.590  -72.193  1.00 102.92 ? 10  ILE D CG1 1 
ATOM   6524  C CG2 . ILE D 2 10  ? 37.632  14.707  -71.975  1.00 117.32 ? 10  ILE D CG2 1 
ATOM   6525  C CD1 . ILE D 2 10  ? 35.228  13.097  -72.444  1.00 95.22  ? 10  ILE D CD1 1 
ATOM   6526  N N   . GLU D 2 11  ? 37.867  16.021  -68.685  1.00 120.32 ? 11  GLU D N   1 
ATOM   6527  C CA  . GLU D 2 11  ? 39.114  16.186  -67.946  1.00 124.58 ? 11  GLU D CA  1 
ATOM   6528  C C   . GLU D 2 11  ? 39.016  15.563  -66.557  1.00 125.82 ? 11  GLU D C   1 
ATOM   6529  O O   . GLU D 2 11  ? 39.760  14.631  -66.226  1.00 133.36 ? 11  GLU D O   1 
ATOM   6530  C CB  . GLU D 2 11  ? 39.475  17.669  -67.852  1.00 136.04 ? 11  GLU D CB  1 
ATOM   6531  C CG  . GLU D 2 11  ? 40.876  17.920  -67.325  1.00 144.22 ? 11  GLU D CG  1 
ATOM   6532  C CD  . GLU D 2 11  ? 41.949  17.304  -68.207  1.00 136.09 ? 11  GLU D CD  1 
ATOM   6533  O OE1 . GLU D 2 11  ? 41.743  17.235  -69.437  1.00 137.46 ? 11  GLU D OE1 1 
ATOM   6534  O OE2 . GLU D 2 11  ? 43.000  16.889  -67.672  1.00 126.37 ? 11  GLU D OE2 1 
ATOM   6535  N N   . GLY D 2 12  ? 38.092  16.050  -65.736  1.00 104.03 ? 12  GLY D N   1 
ATOM   6536  C CA  . GLY D 2 12  ? 37.950  15.526  -64.390  1.00 89.17  ? 12  GLY D CA  1 
ATOM   6537  C C   . GLY D 2 12  ? 36.957  16.342  -63.585  1.00 101.49 ? 12  GLY D C   1 
ATOM   6538  O O   . GLY D 2 12  ? 36.170  17.110  -64.139  1.00 111.45 ? 12  GLY D O   1 
ATOM   6539  N N   . GLY D 2 13  ? 37.012  16.157  -62.264  1.00 86.20  ? 13  GLY D N   1 
ATOM   6540  C CA  . GLY D 2 13  ? 36.091  16.825  -61.371  1.00 84.01  ? 13  GLY D CA  1 
ATOM   6541  C C   . GLY D 2 13  ? 36.418  18.289  -61.145  1.00 92.66  ? 13  GLY D C   1 
ATOM   6542  O O   . GLY D 2 13  ? 37.507  18.774  -61.453  1.00 85.79  ? 13  GLY D O   1 
ATOM   6543  N N   . TRP D 2 14  ? 35.438  18.999  -60.590  1.00 98.85  ? 14  TRP D N   1 
ATOM   6544  C CA  . TRP D 2 14  ? 35.544  20.429  -60.313  1.00 99.55  ? 14  TRP D CA  1 
ATOM   6545  C C   . TRP D 2 14  ? 35.634  20.628  -58.806  1.00 105.31 ? 14  TRP D C   1 
ATOM   6546  O O   . TRP D 2 14  ? 34.638  20.465  -58.092  1.00 101.81 ? 14  TRP D O   1 
ATOM   6547  C CB  . TRP D 2 14  ? 34.350  21.185  -60.886  1.00 95.02  ? 14  TRP D CB  1 
ATOM   6548  C CG  . TRP D 2 14  ? 34.321  21.242  -62.375  1.00 88.78  ? 14  TRP D CG  1 
ATOM   6549  C CD1 . TRP D 2 14  ? 35.351  20.978  -63.228  1.00 99.09  ? 14  TRP D CD1 1 
ATOM   6550  C CD2 . TRP D 2 14  ? 33.198  21.585  -63.193  1.00 81.17  ? 14  TRP D CD2 1 
ATOM   6551  N NE1 . TRP D 2 14  ? 34.939  21.136  -64.529  1.00 92.82  ? 14  TRP D NE1 1 
ATOM   6552  C CE2 . TRP D 2 14  ? 33.621  21.508  -64.534  1.00 97.82  ? 14  TRP D CE2 1 
ATOM   6553  C CE3 . TRP D 2 14  ? 31.875  21.949  -62.921  1.00 83.04  ? 14  TRP D CE3 1 
ATOM   6554  C CZ2 . TRP D 2 14  ? 32.769  21.782  -65.600  1.00 101.46 ? 14  TRP D CZ2 1 
ATOM   6555  C CZ3 . TRP D 2 14  ? 31.031  22.219  -63.981  1.00 95.14  ? 14  TRP D CZ3 1 
ATOM   6556  C CH2 . TRP D 2 14  ? 31.481  22.135  -65.303  1.00 98.22  ? 14  TRP D CH2 1 
ATOM   6557  N N   . GLN D 2 15  ? 36.828  20.978  -58.323  1.00 99.49  ? 15  GLN D N   1 
ATOM   6558  C CA  . GLN D 2 15  ? 36.972  21.353  -56.921  1.00 93.93  ? 15  GLN D CA  1 
ATOM   6559  C C   . GLN D 2 15  ? 36.177  22.612  -56.600  1.00 104.22 ? 15  GLN D C   1 
ATOM   6560  O O   . GLN D 2 15  ? 35.793  22.825  -55.444  1.00 94.31  ? 15  GLN D O   1 
ATOM   6561  C CB  . GLN D 2 15  ? 38.451  21.558  -56.581  1.00 87.99  ? 15  GLN D CB  1 
ATOM   6562  C CG  . GLN D 2 15  ? 39.304  20.300  -56.683  1.00 106.10 ? 15  GLN D CG  1 
ATOM   6563  C CD  . GLN D 2 15  ? 39.623  19.697  -55.326  1.00 116.24 ? 15  GLN D CD  1 
ATOM   6564  O OE1 . GLN D 2 15  ? 39.171  20.191  -54.293  1.00 109.53 ? 15  GLN D OE1 1 
ATOM   6565  N NE2 . GLN D 2 15  ? 40.409  18.625  -55.323  1.00 120.57 ? 15  GLN D NE2 1 
ATOM   6566  N N   . GLY D 2 16  ? 35.927  23.455  -57.604  1.00 105.22 ? 16  GLY D N   1 
ATOM   6567  C CA  . GLY D 2 16  ? 35.152  24.663  -57.371  1.00 94.36  ? 16  GLY D CA  1 
ATOM   6568  C C   . GLY D 2 16  ? 33.703  24.381  -57.018  1.00 101.30 ? 16  GLY D C   1 
ATOM   6569  O O   . GLY D 2 16  ? 33.134  25.027  -56.134  1.00 108.19 ? 16  GLY D O   1 
ATOM   6570  N N   . MET D 2 17  ? 33.086  23.417  -57.699  1.00 106.98 ? 17  MET D N   1 
ATOM   6571  C CA  . MET D 2 17  ? 31.693  23.070  -57.439  1.00 109.74 ? 17  MET D CA  1 
ATOM   6572  C C   . MET D 2 17  ? 31.630  22.241  -56.162  1.00 122.26 ? 17  MET D C   1 
ATOM   6573  O O   . MET D 2 17  ? 32.112  21.104  -56.127  1.00 124.40 ? 17  MET D O   1 
ATOM   6574  C CB  . MET D 2 17  ? 31.095  22.310  -58.619  1.00 102.23 ? 17  MET D CB  1 
ATOM   6575  C CG  . MET D 2 17  ? 29.584  22.445  -58.735  1.00 103.35 ? 17  MET D CG  1 
ATOM   6576  S SD  . MET D 2 17  ? 28.764  20.890  -59.135  1.00 122.41 ? 17  MET D SD  1 
ATOM   6577  C CE  . MET D 2 17  ? 29.754  20.331  -60.517  1.00 105.77 ? 17  MET D CE  1 
ATOM   6578  N N   . VAL D 2 18  ? 31.034  22.806  -55.114  1.00 123.71 ? 18  VAL D N   1 
ATOM   6579  C CA  . VAL D 2 18  ? 31.011  22.165  -53.804  1.00 124.11 ? 18  VAL D CA  1 
ATOM   6580  C C   . VAL D 2 18  ? 29.591  22.136  -53.255  1.00 110.11 ? 18  VAL D C   1 
ATOM   6581  O O   . VAL D 2 18  ? 29.366  21.730  -52.109  1.00 119.75 ? 18  VAL D O   1 
ATOM   6582  C CB  . VAL D 2 18  ? 31.961  22.880  -52.826  1.00 122.12 ? 18  VAL D CB  1 
ATOM   6583  C CG1 . VAL D 2 18  ? 33.407  22.555  -53.160  1.00 118.22 ? 18  VAL D CG1 1 
ATOM   6584  C CG2 . VAL D 2 18  ? 31.728  24.382  -52.869  1.00 104.17 ? 18  VAL D CG2 1 
ATOM   6585  N N   . ASP D 2 19  ? 28.623  22.563  -54.064  1.00 102.66 ? 19  ASP D N   1 
ATOM   6586  C CA  . ASP D 2 19  ? 27.231  22.612  -53.644  1.00 116.62 ? 19  ASP D CA  1 
ATOM   6587  C C   . ASP D 2 19  ? 26.396  21.479  -54.231  1.00 122.53 ? 19  ASP D C   1 
ATOM   6588  O O   . ASP D 2 19  ? 25.167  21.501  -54.106  1.00 109.07 ? 19  ASP D O   1 
ATOM   6589  C CB  . ASP D 2 19  ? 26.615  23.963  -54.012  1.00 126.50 ? 19  ASP D CB  1 
ATOM   6590  C CG  . ASP D 2 19  ? 25.624  24.455  -52.974  1.00 136.76 ? 19  ASP D CG  1 
ATOM   6591  O OD1 . ASP D 2 19  ? 25.093  23.619  -52.211  1.00 139.55 ? 19  ASP D OD1 1 
ATOM   6592  O OD2 . ASP D 2 19  ? 25.377  25.677  -52.918  1.00 129.25 ? 19  ASP D OD2 1 
ATOM   6593  N N   . GLY D 2 20  ? 27.026  20.498  -54.866  1.00 114.38 ? 20  GLY D N   1 
ATOM   6594  C CA  . GLY D 2 20  ? 26.285  19.375  -55.414  1.00 85.96  ? 20  GLY D CA  1 
ATOM   6595  C C   . GLY D 2 20  ? 27.224  18.365  -56.036  1.00 99.91  ? 20  GLY D C   1 
ATOM   6596  O O   . GLY D 2 20  ? 28.425  18.606  -56.195  1.00 105.64 ? 20  GLY D O   1 
ATOM   6597  N N   . TRP D 2 21  ? 26.647  17.210  -56.378  1.00 96.98  ? 21  TRP D N   1 
ATOM   6598  C CA  . TRP D 2 21  ? 27.393  16.161  -57.066  1.00 104.02 ? 21  TRP D CA  1 
ATOM   6599  C C   . TRP D 2 21  ? 27.576  16.472  -58.547  1.00 95.84  ? 21  TRP D C   1 
ATOM   6600  O O   . TRP D 2 21  ? 28.661  16.261  -59.098  1.00 98.28  ? 21  TRP D O   1 
ATOM   6601  C CB  . TRP D 2 21  ? 26.684  14.817  -56.898  1.00 113.73 ? 21  TRP D CB  1 
ATOM   6602  C CG  . TRP D 2 21  ? 26.965  14.133  -55.597  1.00 108.56 ? 21  TRP D CG  1 
ATOM   6603  C CD1 . TRP D 2 21  ? 27.831  14.540  -54.625  1.00 99.49  ? 21  TRP D CD1 1 
ATOM   6604  C CD2 . TRP D 2 21  ? 26.379  12.913  -55.127  1.00 109.49 ? 21  TRP D CD2 1 
ATOM   6605  N NE1 . TRP D 2 21  ? 27.821  13.649  -53.579  1.00 105.89 ? 21  TRP D NE1 1 
ATOM   6606  C CE2 . TRP D 2 21  ? 26.937  12.642  -53.862  1.00 102.29 ? 21  TRP D CE2 1 
ATOM   6607  C CE3 . TRP D 2 21  ? 25.435  12.025  -55.653  1.00 105.53 ? 21  TRP D CE3 1 
ATOM   6608  C CZ2 . TRP D 2 21  ? 26.583  11.521  -53.116  1.00 95.49  ? 21  TRP D CZ2 1 
ATOM   6609  C CZ3 . TRP D 2 21  ? 25.084  10.913  -54.909  1.00 99.18  ? 21  TRP D CZ3 1 
ATOM   6610  C CH2 . TRP D 2 21  ? 25.658  10.670  -53.655  1.00 98.27  ? 21  TRP D CH2 1 
ATOM   6611  N N   . TYR D 2 22  ? 26.528  16.963  -59.206  1.00 109.09 ? 22  TYR D N   1 
ATOM   6612  C CA  . TYR D 2 22  ? 26.546  17.258  -60.631  1.00 96.21  ? 22  TYR D CA  1 
ATOM   6613  C C   . TYR D 2 22  ? 26.052  18.679  -60.851  1.00 102.88 ? 22  TYR D C   1 
ATOM   6614  O O   . TYR D 2 22  ? 25.141  19.141  -60.157  1.00 95.72  ? 22  TYR D O   1 
ATOM   6615  C CB  . TYR D 2 22  ? 25.667  16.276  -61.419  1.00 85.64  ? 22  TYR D CB  1 
ATOM   6616  C CG  . TYR D 2 22  ? 25.751  14.845  -60.938  1.00 90.40  ? 22  TYR D CG  1 
ATOM   6617  C CD1 . TYR D 2 22  ? 26.844  14.050  -61.252  1.00 86.35  ? 22  TYR D CD1 1 
ATOM   6618  C CD2 . TYR D 2 22  ? 24.732  14.286  -60.174  1.00 91.50  ? 22  TYR D CD2 1 
ATOM   6619  C CE1 . TYR D 2 22  ? 26.925  12.741  -60.817  1.00 99.48  ? 22  TYR D CE1 1 
ATOM   6620  C CE2 . TYR D 2 22  ? 24.803  12.977  -59.734  1.00 88.53  ? 22  TYR D CE2 1 
ATOM   6621  C CZ  . TYR D 2 22  ? 25.902  12.210  -60.058  1.00 94.99  ? 22  TYR D CZ  1 
ATOM   6622  O OH  . TYR D 2 22  ? 25.980  10.906  -59.625  1.00 92.23  ? 22  TYR D OH  1 
ATOM   6623  N N   . GLY D 2 23  ? 26.646  19.365  -61.818  1.00 89.78  ? 23  GLY D N   1 
ATOM   6624  C CA  . GLY D 2 23  ? 26.250  20.734  -62.070  1.00 97.11  ? 23  GLY D CA  1 
ATOM   6625  C C   . GLY D 2 23  ? 26.880  21.281  -63.331  1.00 105.62 ? 23  GLY D C   1 
ATOM   6626  O O   . GLY D 2 23  ? 27.442  20.543  -64.142  1.00 92.79  ? 23  GLY D O   1 
ATOM   6627  N N   . TYR D 2 24  ? 26.777  22.598  -63.479  1.00 106.86 ? 24  TYR D N   1 
ATOM   6628  C CA  . TYR D 2 24  ? 27.238  23.313  -64.660  1.00 99.19  ? 24  TYR D CA  1 
ATOM   6629  C C   . TYR D 2 24  ? 28.327  24.313  -64.281  1.00 96.92  ? 24  TYR D C   1 
ATOM   6630  O O   . TYR D 2 24  ? 28.676  24.480  -63.110  1.00 99.55  ? 24  TYR D O   1 
ATOM   6631  C CB  . TYR D 2 24  ? 26.077  24.034  -65.352  1.00 93.66  ? 24  TYR D CB  1 
ATOM   6632  C CG  . TYR D 2 24  ? 24.834  23.195  -65.535  1.00 82.93  ? 24  TYR D CG  1 
ATOM   6633  C CD1 . TYR D 2 24  ? 24.701  22.345  -66.622  1.00 80.66  ? 24  TYR D CD1 1 
ATOM   6634  C CD2 . TYR D 2 24  ? 23.786  23.265  -64.627  1.00 87.74  ? 24  TYR D CD2 1 
ATOM   6635  C CE1 . TYR D 2 24  ? 23.564  21.578  -66.797  1.00 91.41  ? 24  TYR D CE1 1 
ATOM   6636  C CE2 . TYR D 2 24  ? 22.644  22.504  -64.792  1.00 86.62  ? 24  TYR D CE2 1 
ATOM   6637  C CZ  . TYR D 2 24  ? 22.539  21.663  -65.880  1.00 82.06  ? 24  TYR D CZ  1 
ATOM   6638  O OH  . TYR D 2 24  ? 21.405  20.904  -66.051  1.00 100.12 ? 24  TYR D OH  1 
ATOM   6639  N N   . HIS D 2 25  ? 28.865  24.981  -65.302  1.00 92.51  ? 25  HIS D N   1 
ATOM   6640  C CA  . HIS D 2 25  ? 29.808  26.084  -65.109  1.00 106.98 ? 25  HIS D CA  1 
ATOM   6641  C C   . HIS D 2 25  ? 29.638  27.030  -66.294  1.00 107.44 ? 25  HIS D C   1 
ATOM   6642  O O   . HIS D 2 25  ? 30.186  26.781  -67.372  1.00 97.48  ? 25  HIS D O   1 
ATOM   6643  C CB  . HIS D 2 25  ? 31.242  25.583  -64.997  1.00 109.01 ? 25  HIS D CB  1 
ATOM   6644  C CG  . HIS D 2 25  ? 32.271  26.655  -65.183  1.00 112.56 ? 25  HIS D CG  1 
ATOM   6645  N ND1 . HIS D 2 25  ? 32.498  27.640  -64.246  1.00 104.16 ? 25  HIS D ND1 1 
ATOM   6646  C CD2 . HIS D 2 25  ? 33.126  26.902  -66.203  1.00 108.55 ? 25  HIS D CD2 1 
ATOM   6647  C CE1 . HIS D 2 25  ? 33.453  28.444  -64.678  1.00 99.69  ? 25  HIS D CE1 1 
ATOM   6648  N NE2 . HIS D 2 25  ? 33.851  28.018  -65.864  1.00 105.69 ? 25  HIS D NE2 1 
ATOM   6649  N N   . HIS D 2 26  ? 28.879  28.103  -66.090  1.00 123.30 ? 26  HIS D N   1 
ATOM   6650  C CA  . HIS D 2 26  ? 28.647  29.063  -67.157  1.00 113.77 ? 26  HIS D CA  1 
ATOM   6651  C C   . HIS D 2 26  ? 29.818  30.031  -67.268  1.00 109.20 ? 26  HIS D C   1 
ATOM   6652  O O   . HIS D 2 26  ? 30.480  30.359  -66.278  1.00 107.20 ? 26  HIS D O   1 
ATOM   6653  C CB  . HIS D 2 26  ? 27.342  29.830  -66.923  1.00 106.32 ? 26  HIS D CB  1 
ATOM   6654  C CG  . HIS D 2 26  ? 27.477  31.014  -66.015  1.00 107.30 ? 26  HIS D CG  1 
ATOM   6655  N ND1 . HIS D 2 26  ? 28.003  32.218  -66.432  1.00 112.15 ? 26  HIS D ND1 1 
ATOM   6656  C CD2 . HIS D 2 26  ? 27.133  31.184  -64.717  1.00 112.62 ? 26  HIS D CD2 1 
ATOM   6657  C CE1 . HIS D 2 26  ? 27.989  33.074  -65.426  1.00 125.37 ? 26  HIS D CE1 1 
ATOM   6658  N NE2 . HIS D 2 26  ? 27.464  32.472  -64.374  1.00 127.19 ? 26  HIS D NE2 1 
ATOM   6659  N N   . SER D 2 27  ? 30.074  30.484  -68.495  1.00 117.33 ? 27  SER D N   1 
ATOM   6660  C CA  . SER D 2 27  ? 31.134  31.462  -68.751  1.00 113.22 ? 27  SER D CA  1 
ATOM   6661  C C   . SER D 2 27  ? 30.694  32.326  -69.935  1.00 115.31 ? 27  SER D C   1 
ATOM   6662  O O   . SER D 2 27  ? 30.925  31.976  -71.094  1.00 110.54 ? 27  SER D O   1 
ATOM   6663  C CB  . SER D 2 27  ? 32.468  30.782  -69.018  1.00 116.81 ? 27  SER D CB  1 
ATOM   6664  O OG  . SER D 2 27  ? 33.395  31.693  -69.583  1.00 118.09 ? 27  SER D OG  1 
ATOM   6665  N N   . ASN D 2 28  ? 30.068  33.456  -69.625  1.00 120.14 ? 28  ASN D N   1 
ATOM   6666  C CA  . ASN D 2 28  ? 29.688  34.450  -70.614  1.00 112.75 ? 28  ASN D CA  1 
ATOM   6667  C C   . ASN D 2 28  ? 30.472  35.737  -70.359  1.00 118.48 ? 28  ASN D C   1 
ATOM   6668  O O   . ASN D 2 28  ? 31.369  35.783  -69.510  1.00 121.05 ? 28  ASN D O   1 
ATOM   6669  C CB  . ASN D 2 28  ? 28.172  34.677  -70.592  1.00 95.86  ? 28  ASN D CB  1 
ATOM   6670  C CG  . ASN D 2 28  ? 27.647  35.029  -69.213  1.00 106.46 ? 28  ASN D CG  1 
ATOM   6671  O OD1 . ASN D 2 28  ? 28.413  35.316  -68.293  1.00 122.91 ? 28  ASN D OD1 1 
ATOM   6672  N ND2 . ASN D 2 28  ? 26.328  35.014  -69.065  1.00 94.12  ? 28  ASN D ND2 1 
ATOM   6673  N N   . GLU D 2 29  ? 30.135  36.789  -71.107  1.00 116.58 ? 29  GLU D N   1 
ATOM   6674  C CA  . GLU D 2 29  ? 30.837  38.058  -70.947  1.00 128.77 ? 29  GLU D CA  1 
ATOM   6675  C C   . GLU D 2 29  ? 30.608  38.675  -69.572  1.00 127.85 ? 29  GLU D C   1 
ATOM   6676  O O   . GLU D 2 29  ? 31.422  39.492  -69.129  1.00 125.21 ? 29  GLU D O   1 
ATOM   6677  C CB  . GLU D 2 29  ? 30.411  39.038  -72.045  1.00 129.20 ? 29  GLU D CB  1 
ATOM   6678  C CG  . GLU D 2 29  ? 29.034  39.663  -71.851  1.00 136.17 ? 29  GLU D CG  1 
ATOM   6679  C CD  . GLU D 2 29  ? 29.099  41.046  -71.228  1.00 140.40 ? 29  GLU D CD  1 
ATOM   6680  O OE1 . GLU D 2 29  ? 30.194  41.446  -70.776  1.00 139.21 ? 29  GLU D OE1 1 
ATOM   6681  O OE2 . GLU D 2 29  ? 28.057  41.735  -71.194  1.00 134.26 ? 29  GLU D OE2 1 
ATOM   6682  N N   . GLN D 2 30  ? 29.530  38.296  -68.885  1.00 121.46 ? 30  GLN D N   1 
ATOM   6683  C CA  . GLN D 2 30  ? 29.209  38.872  -67.586  1.00 108.94 ? 30  GLN D CA  1 
ATOM   6684  C C   . GLN D 2 30  ? 30.033  38.281  -66.450  1.00 113.87 ? 30  GLN D C   1 
ATOM   6685  O O   . GLN D 2 30  ? 29.926  38.762  -65.316  1.00 108.87 ? 30  GLN D O   1 
ATOM   6686  C CB  . GLN D 2 30  ? 27.720  38.693  -67.286  1.00 87.09  ? 30  GLN D CB  1 
ATOM   6687  C CG  . GLN D 2 30  ? 26.801  39.205  -68.384  1.00 85.67  ? 30  GLN D CG  1 
ATOM   6688  C CD  . GLN D 2 30  ? 25.342  39.201  -67.972  1.00 104.68 ? 30  GLN D CD  1 
ATOM   6689  O OE1 . GLN D 2 30  ? 24.959  39.850  -66.998  1.00 108.09 ? 30  GLN D OE1 1 
ATOM   6690  N NE2 . GLN D 2 30  ? 24.520  38.463  -68.708  1.00 104.34 ? 30  GLN D NE2 1 
ATOM   6691  N N   . GLY D 2 31  ? 30.841  37.259  -66.717  1.00 114.95 ? 31  GLY D N   1 
ATOM   6692  C CA  . GLY D 2 31  ? 31.686  36.637  -65.724  1.00 118.68 ? 31  GLY D CA  1 
ATOM   6693  C C   . GLY D 2 31  ? 31.586  35.132  -65.793  1.00 123.84 ? 31  GLY D C   1 
ATOM   6694  O O   . GLY D 2 31  ? 31.026  34.560  -66.734  1.00 120.44 ? 31  GLY D O   1 
ATOM   6695  N N   . SER D 2 32  ? 32.142  34.476  -64.780  1.00 121.62 ? 32  SER D N   1 
ATOM   6696  C CA  . SER D 2 32  ? 32.134  33.026  -64.669  1.00 113.40 ? 32  SER D CA  1 
ATOM   6697  C C   . SER D 2 32  ? 31.461  32.616  -63.365  1.00 120.66 ? 32  SER D C   1 
ATOM   6698  O O   . SER D 2 32  ? 31.242  33.433  -62.467  1.00 128.32 ? 32  SER D O   1 
ATOM   6699  C CB  . SER D 2 32  ? 33.558  32.458  -64.736  1.00 101.78 ? 32  SER D CB  1 
ATOM   6700  O OG  . SER D 2 32  ? 34.208  32.846  -65.934  1.00 121.59 ? 32  SER D OG  1 
ATOM   6701  N N   . GLY D 2 33  ? 31.128  31.336  -63.271  1.00 126.03 ? 33  GLY D N   1 
ATOM   6702  C CA  . GLY D 2 33  ? 30.508  30.819  -62.064  1.00 122.03 ? 33  GLY D CA  1 
ATOM   6703  C C   . GLY D 2 33  ? 30.180  29.352  -62.220  1.00 108.59 ? 33  GLY D C   1 
ATOM   6704  O O   . GLY D 2 33  ? 30.324  28.766  -63.298  1.00 105.64 ? 33  GLY D O   1 
ATOM   6705  N N   . TYR D 2 34  ? 29.733  28.765  -61.113  1.00 105.73 ? 34  TYR D N   1 
ATOM   6706  C CA  . TYR D 2 34  ? 29.307  27.376  -61.067  1.00 93.72  ? 34  TYR D CA  1 
ATOM   6707  C C   . TYR D 2 34  ? 27.840  27.299  -60.674  1.00 92.29  ? 34  TYR D C   1 
ATOM   6708  O O   . TYR D 2 34  ? 27.330  28.148  -59.937  1.00 91.85  ? 34  TYR D O   1 
ATOM   6709  C CB  . TYR D 2 34  ? 30.135  26.555  -60.068  1.00 84.78  ? 34  TYR D CB  1 
ATOM   6710  C CG  . TYR D 2 34  ? 31.600  26.414  -60.415  1.00 93.59  ? 34  TYR D CG  1 
ATOM   6711  C CD1 . TYR D 2 34  ? 32.025  25.488  -61.360  1.00 90.43  ? 34  TYR D CD1 1 
ATOM   6712  C CD2 . TYR D 2 34  ? 32.560  27.191  -59.781  1.00 104.42 ? 34  TYR D CD2 1 
ATOM   6713  C CE1 . TYR D 2 34  ? 33.365  25.351  -61.673  1.00 93.15  ? 34  TYR D CE1 1 
ATOM   6714  C CE2 . TYR D 2 34  ? 33.900  27.062  -60.086  1.00 101.74 ? 34  TYR D CE2 1 
ATOM   6715  C CZ  . TYR D 2 34  ? 34.297  26.140  -61.033  1.00 97.66  ? 34  TYR D CZ  1 
ATOM   6716  O OH  . TYR D 2 34  ? 35.632  26.008  -61.339  1.00 105.10 ? 34  TYR D OH  1 
ATOM   6717  N N   . ALA D 2 35  ? 27.167  26.271  -61.179  1.00 95.14  ? 35  ALA D N   1 
ATOM   6718  C CA  . ALA D 2 35  ? 25.809  25.954  -60.769  1.00 98.40  ? 35  ALA D CA  1 
ATOM   6719  C C   . ALA D 2 35  ? 25.714  24.455  -60.536  1.00 112.09 ? 35  ALA D C   1 
ATOM   6720  O O   . ALA D 2 35  ? 26.468  23.674  -61.120  1.00 110.43 ? 35  ALA D O   1 
ATOM   6721  C CB  . ALA D 2 35  ? 24.779  26.401  -61.814  1.00 89.48  ? 35  ALA D CB  1 
ATOM   6722  N N   . ALA D 2 36  ? 24.789  24.060  -59.668  1.00 100.43 ? 36  ALA D N   1 
ATOM   6723  C CA  . ALA D 2 36  ? 24.578  22.661  -59.327  1.00 106.01 ? 36  ALA D CA  1 
ATOM   6724  C C   . ALA D 2 36  ? 23.163  22.255  -59.709  1.00 108.47 ? 36  ALA D C   1 
ATOM   6725  O O   . ALA D 2 36  ? 22.202  22.947  -59.354  1.00 103.05 ? 36  ALA D O   1 
ATOM   6726  C CB  . ALA D 2 36  ? 24.815  22.421  -57.834  1.00 99.31  ? 36  ALA D CB  1 
ATOM   6727  N N   . ASP D 2 37  ? 23.038  21.137  -60.426  1.00 104.12 ? 37  ASP D N   1 
ATOM   6728  C CA  . ASP D 2 37  ? 21.734  20.571  -60.765  1.00 110.31 ? 37  ASP D CA  1 
ATOM   6729  C C   . ASP D 2 37  ? 21.170  19.919  -59.511  1.00 111.94 ? 37  ASP D C   1 
ATOM   6730  O O   . ASP D 2 37  ? 21.600  18.835  -59.115  1.00 116.68 ? 37  ASP D O   1 
ATOM   6731  C CB  . ASP D 2 37  ? 21.863  19.566  -61.909  1.00 92.39  ? 37  ASP D CB  1 
ATOM   6732  C CG  . ASP D 2 37  ? 20.522  18.969  -62.338  1.00 113.19 ? 37  ASP D CG  1 
ATOM   6733  O OD1 . ASP D 2 37  ? 19.779  18.442  -61.480  1.00 117.77 ? 37  ASP D OD1 1 
ATOM   6734  O OD2 . ASP D 2 37  ? 20.218  19.028  -63.551  1.00 117.44 ? 37  ASP D OD2 1 
ATOM   6735  N N   . LYS D 2 38  ? 20.196  20.582  -58.881  1.00 106.41 ? 38  LYS D N   1 
ATOM   6736  C CA  . LYS D 2 38  ? 19.598  20.060  -57.656  1.00 104.23 ? 38  LYS D CA  1 
ATOM   6737  C C   . LYS D 2 38  ? 18.905  18.721  -57.895  1.00 111.36 ? 38  LYS D C   1 
ATOM   6738  O O   . LYS D 2 38  ? 19.002  17.807  -57.067  1.00 115.93 ? 38  LYS D O   1 
ATOM   6739  C CB  . LYS D 2 38  ? 18.614  21.086  -57.086  1.00 110.83 ? 38  LYS D CB  1 
ATOM   6740  C CG  . LYS D 2 38  ? 17.358  20.496  -56.467  1.00 124.41 ? 38  LYS D CG  1 
ATOM   6741  C CD  . LYS D 2 38  ? 17.525  20.204  -54.985  1.00 120.05 ? 38  LYS D CD  1 
ATOM   6742  C CE  . LYS D 2 38  ? 16.236  19.635  -54.404  1.00 114.62 ? 38  LYS D CE  1 
ATOM   6743  N NZ  . LYS D 2 38  ? 16.260  19.571  -52.917  1.00 104.30 ? 38  LYS D NZ  1 
ATOM   6744  N N   . GLU D 2 39  ? 18.215  18.579  -59.030  1.00 106.85 ? 39  GLU D N   1 
ATOM   6745  C CA  . GLU D 2 39  ? 17.353  17.418  -59.226  1.00 105.88 ? 39  GLU D CA  1 
ATOM   6746  C C   . GLU D 2 39  ? 18.158  16.128  -59.340  1.00 107.05 ? 39  GLU D C   1 
ATOM   6747  O O   . GLU D 2 39  ? 17.859  15.138  -58.661  1.00 113.50 ? 39  GLU D O   1 
ATOM   6748  C CB  . GLU D 2 39  ? 16.473  17.612  -60.460  1.00 115.70 ? 39  GLU D CB  1 
ATOM   6749  C CG  . GLU D 2 39  ? 15.030  17.179  -60.244  1.00 130.04 ? 39  GLU D CG  1 
ATOM   6750  C CD  . GLU D 2 39  ? 14.272  16.987  -61.542  1.00 141.44 ? 39  GLU D CD  1 
ATOM   6751  O OE1 . GLU D 2 39  ? 14.911  17.002  -62.615  1.00 140.62 ? 39  GLU D OE1 1 
ATOM   6752  O OE2 . GLU D 2 39  ? 13.036  16.817  -61.486  1.00 133.43 ? 39  GLU D OE2 1 
ATOM   6753  N N   . SER D 2 40  ? 19.184  16.113  -60.194  1.00 95.93  ? 40  SER D N   1 
ATOM   6754  C CA  . SER D 2 40  ? 19.932  14.876  -60.395  1.00 106.42 ? 40  SER D CA  1 
ATOM   6755  C C   . SER D 2 40  ? 20.840  14.559  -59.211  1.00 104.03 ? 40  SER D C   1 
ATOM   6756  O O   . SER D 2 40  ? 21.106  13.383  -58.938  1.00 107.98 ? 40  SER D O   1 
ATOM   6757  C CB  . SER D 2 40  ? 20.732  14.946  -61.698  1.00 94.51  ? 40  SER D CB  1 
ATOM   6758  O OG  . SER D 2 40  ? 21.349  16.208  -61.871  1.00 112.40 ? 40  SER D OG  1 
ATOM   6759  N N   . THR D 2 41  ? 21.328  15.579  -58.502  1.00 90.63  ? 41  THR D N   1 
ATOM   6760  C CA  . THR D 2 41  ? 22.096  15.321  -57.288  1.00 99.74  ? 41  THR D CA  1 
ATOM   6761  C C   . THR D 2 41  ? 21.215  14.716  -56.205  1.00 104.39 ? 41  THR D C   1 
ATOM   6762  O O   . THR D 2 41  ? 21.582  13.716  -55.577  1.00 110.68 ? 41  THR D O   1 
ATOM   6763  C CB  . THR D 2 41  ? 22.744  16.607  -56.777  1.00 93.89  ? 41  THR D CB  1 
ATOM   6764  O OG1 . THR D 2 41  ? 21.734  17.597  -56.547  1.00 114.63 ? 41  THR D OG1 1 
ATOM   6765  C CG2 . THR D 2 41  ? 23.741  17.127  -57.778  1.00 91.02  ? 41  THR D CG2 1 
ATOM   6766  N N   . GLN D 2 42  ? 20.045  15.312  -55.971  1.00 97.25  ? 42  GLN D N   1 
ATOM   6767  C CA  . GLN D 2 42  ? 19.157  14.802  -54.933  1.00 94.85  ? 42  GLN D CA  1 
ATOM   6768  C C   . GLN D 2 42  ? 18.612  13.428  -55.300  1.00 99.76  ? 42  GLN D C   1 
ATOM   6769  O O   . GLN D 2 42  ? 18.501  12.549  -54.438  1.00 104.67 ? 42  GLN D O   1 
ATOM   6770  C CB  . GLN D 2 42  ? 18.023  15.795  -54.684  1.00 100.02 ? 42  GLN D CB  1 
ATOM   6771  C CG  . GLN D 2 42  ? 17.452  15.724  -53.280  1.00 103.01 ? 42  GLN D CG  1 
ATOM   6772  C CD  . GLN D 2 42  ? 18.529  15.807  -52.211  1.00 113.68 ? 42  GLN D CD  1 
ATOM   6773  O OE1 . GLN D 2 42  ? 18.530  15.034  -51.252  1.00 108.25 ? 42  GLN D OE1 1 
ATOM   6774  N NE2 . GLN D 2 42  ? 19.450  16.751  -52.369  1.00 105.25 ? 42  GLN D NE2 1 
ATOM   6775  N N   . LYS D 2 43  ? 18.277  13.220  -56.576  1.00 97.64  ? 43  LYS D N   1 
ATOM   6776  C CA  . LYS D 2 43  ? 17.818  11.906  -57.014  1.00 88.66  ? 43  LYS D CA  1 
ATOM   6777  C C   . LYS D 2 43  ? 18.911  10.858  -56.832  1.00 96.84  ? 43  LYS D C   1 
ATOM   6778  O O   . LYS D 2 43  ? 18.632  9.723   -56.429  1.00 94.74  ? 43  LYS D O   1 
ATOM   6779  C CB  . LYS D 2 43  ? 17.357  11.977  -58.471  1.00 81.64  ? 43  LYS D CB  1 
ATOM   6780  C CG  . LYS D 2 43  ? 16.673  10.725  -58.999  1.00 96.14  ? 43  LYS D CG  1 
ATOM   6781  C CD  . LYS D 2 43  ? 15.512  11.096  -59.913  1.00 114.42 ? 43  LYS D CD  1 
ATOM   6782  C CE  . LYS D 2 43  ? 15.312  10.082  -61.027  1.00 112.49 ? 43  LYS D CE  1 
ATOM   6783  N NZ  . LYS D 2 43  ? 16.066  10.465  -62.254  1.00 98.62  ? 43  LYS D NZ  1 
ATOM   6784  N N   . ALA D 2 44  ? 20.164  11.223  -57.115  1.00 91.23  ? 44  ALA D N   1 
ATOM   6785  C CA  . ALA D 2 44  ? 21.273  10.304  -56.881  1.00 85.51  ? 44  ALA D CA  1 
ATOM   6786  C C   . ALA D 2 44  ? 21.567  10.136  -55.394  1.00 95.41  ? 44  ALA D C   1 
ATOM   6787  O O   . ALA D 2 44  ? 21.959  9.045   -54.963  1.00 100.90 ? 44  ALA D O   1 
ATOM   6788  C CB  . ALA D 2 44  ? 22.524  10.788  -57.616  1.00 84.02  ? 44  ALA D CB  1 
ATOM   6789  N N   . ILE D 2 45  ? 21.402  11.198  -54.602  1.00 95.13  ? 45  ILE D N   1 
ATOM   6790  C CA  . ILE D 2 45  ? 21.663  11.108  -53.166  1.00 83.81  ? 45  ILE D CA  1 
ATOM   6791  C C   . ILE D 2 45  ? 20.669  10.163  -52.504  1.00 88.28  ? 45  ILE D C   1 
ATOM   6792  O O   . ILE D 2 45  ? 21.042  9.304   -51.694  1.00 95.06  ? 45  ILE D O   1 
ATOM   6793  C CB  . ILE D 2 45  ? 21.632  12.507  -52.523  1.00 97.96  ? 45  ILE D CB  1 
ATOM   6794  C CG1 . ILE D 2 45  ? 23.003  13.175  -52.656  1.00 91.74  ? 45  ILE D CG1 1 
ATOM   6795  C CG2 . ILE D 2 45  ? 21.196  12.431  -51.062  1.00 87.41  ? 45  ILE D CG2 1 
ATOM   6796  C CD1 . ILE D 2 45  ? 23.038  14.610  -52.173  1.00 92.59  ? 45  ILE D CD1 1 
ATOM   6797  N N   . ASP D 2 46  ? 19.387  10.299  -52.849  1.00 96.91  ? 46  ASP D N   1 
ATOM   6798  C CA  . ASP D 2 46  ? 18.373  9.385   -52.337  1.00 94.92  ? 46  ASP D CA  1 
ATOM   6799  C C   . ASP D 2 46  ? 18.614  7.955   -52.796  1.00 90.24  ? 46  ASP D C   1 
ATOM   6800  O O   . ASP D 2 46  ? 18.092  7.020   -52.179  1.00 95.78  ? 46  ASP D O   1 
ATOM   6801  C CB  . ASP D 2 46  ? 16.983  9.839   -52.787  1.00 101.42 ? 46  ASP D CB  1 
ATOM   6802  C CG  . ASP D 2 46  ? 16.720  11.295  -52.478  1.00 113.13 ? 46  ASP D CG  1 
ATOM   6803  O OD1 . ASP D 2 46  ? 17.598  11.936  -51.863  1.00 116.58 ? 46  ASP D OD1 1 
ATOM   6804  O OD2 . ASP D 2 46  ? 15.638  11.795  -52.852  1.00 119.15 ? 46  ASP D OD2 1 
ATOM   6805  N N   . GLY D 2 47  ? 19.394  7.765   -53.858  1.00 83.96  ? 47  GLY D N   1 
ATOM   6806  C CA  . GLY D 2 47  ? 19.706  6.442   -54.348  1.00 73.04  ? 47  GLY D CA  1 
ATOM   6807  C C   . GLY D 2 47  ? 20.714  5.721   -53.479  1.00 87.74  ? 47  GLY D C   1 
ATOM   6808  O O   . GLY D 2 47  ? 20.403  4.675   -52.902  1.00 105.12 ? 47  GLY D O   1 
ATOM   6809  N N   . VAL D 2 48  ? 21.925  6.275   -53.364  1.00 86.77  ? 48  VAL D N   1 
ATOM   6810  C CA  . VAL D 2 48  ? 22.972  5.613   -52.589  1.00 80.90  ? 48  VAL D CA  1 
ATOM   6811  C C   . VAL D 2 48  ? 22.577  5.519   -51.121  1.00 80.66  ? 48  VAL D C   1 
ATOM   6812  O O   . VAL D 2 48  ? 23.022  4.611   -50.407  1.00 95.03  ? 48  VAL D O   1 
ATOM   6813  C CB  . VAL D 2 48  ? 24.323  6.335   -52.773  1.00 75.94  ? 48  VAL D CB  1 
ATOM   6814  C CG1 . VAL D 2 48  ? 24.552  6.663   -54.242  1.00 80.38  ? 48  VAL D CG1 1 
ATOM   6815  C CG2 . VAL D 2 48  ? 24.398  7.591   -51.916  1.00 85.16  ? 48  VAL D CG2 1 
ATOM   6816  N N   . THR D 2 49  ? 21.739  6.443   -50.647  1.00 73.92  ? 49  THR D N   1 
ATOM   6817  C CA  . THR D 2 49  ? 21.256  6.365   -49.273  1.00 84.20  ? 49  THR D CA  1 
ATOM   6818  C C   . THR D 2 49  ? 20.383  5.133   -49.069  1.00 89.05  ? 49  THR D C   1 
ATOM   6819  O O   . THR D 2 49  ? 20.470  4.468   -48.030  1.00 98.14  ? 49  THR D O   1 
ATOM   6820  C CB  . THR D 2 49  ? 20.488  7.635   -48.913  1.00 96.28  ? 49  THR D CB  1 
ATOM   6821  O OG1 . THR D 2 49  ? 21.110  8.765   -49.538  1.00 96.61  ? 49  THR D OG1 1 
ATOM   6822  C CG2 . THR D 2 49  ? 20.489  7.844   -47.409  1.00 82.51  ? 49  THR D CG2 1 
ATOM   6823  N N   . ASN D 2 50  ? 19.530  4.820   -50.047  1.00 87.32  ? 50  ASN D N   1 
ATOM   6824  C CA  . ASN D 2 50  ? 18.757  3.583   -49.987  1.00 89.25  ? 50  ASN D CA  1 
ATOM   6825  C C   . ASN D 2 50  ? 19.664  2.361   -50.050  1.00 87.38  ? 50  ASN D C   1 
ATOM   6826  O O   . ASN D 2 50  ? 19.445  1.381   -49.328  1.00 97.73  ? 50  ASN D O   1 
ATOM   6827  C CB  . ASN D 2 50  ? 17.730  3.546   -51.120  1.00 91.10  ? 50  ASN D CB  1 
ATOM   6828  C CG  . ASN D 2 50  ? 16.364  4.038   -50.687  1.00 103.04 ? 50  ASN D CG  1 
ATOM   6829  O OD1 . ASN D 2 50  ? 15.548  3.269   -50.179  1.00 106.15 ? 50  ASN D OD1 1 
ATOM   6830  N ND2 . ASN D 2 50  ? 16.107  5.325   -50.888  1.00 106.61 ? 50  ASN D ND2 1 
ATOM   6831  N N   . LYS D 2 51  ? 20.685  2.397   -50.912  1.00 82.58  ? 51  LYS D N   1 
ATOM   6832  C CA  . LYS D 2 51  ? 21.584  1.255   -51.044  1.00 83.68  ? 51  LYS D CA  1 
ATOM   6833  C C   . LYS D 2 51  ? 22.334  0.984   -49.746  1.00 87.70  ? 51  LYS D C   1 
ATOM   6834  O O   . LYS D 2 51  ? 22.481  -0.173  -49.335  1.00 89.43  ? 51  LYS D O   1 
ATOM   6835  C CB  . LYS D 2 51  ? 22.572  1.484   -52.188  1.00 69.48  ? 51  LYS D CB  1 
ATOM   6836  C CG  . LYS D 2 51  ? 23.586  0.359   -52.338  1.00 85.14  ? 51  LYS D CG  1 
ATOM   6837  C CD  . LYS D 2 51  ? 24.710  0.710   -53.300  1.00 82.71  ? 51  LYS D CD  1 
ATOM   6838  C CE  . LYS D 2 51  ? 24.217  0.815   -54.731  1.00 75.09  ? 51  LYS D CE  1 
ATOM   6839  N NZ  . LYS D 2 51  ? 25.334  0.619   -55.699  1.00 81.64  ? 51  LYS D NZ  1 
ATOM   6840  N N   . VAL D 2 52  ? 22.819  2.038   -49.088  1.00 76.52  ? 52  VAL D N   1 
ATOM   6841  C CA  . VAL D 2 52  ? 23.510  1.867   -47.813  1.00 84.74  ? 52  VAL D CA  1 
ATOM   6842  C C   . VAL D 2 52  ? 22.553  1.323   -46.758  1.00 79.48  ? 52  VAL D C   1 
ATOM   6843  O O   . VAL D 2 52  ? 22.887  0.398   -46.007  1.00 83.52  ? 52  VAL D O   1 
ATOM   6844  C CB  . VAL D 2 52  ? 24.150  3.196   -47.368  1.00 82.05  ? 52  VAL D CB  1 
ATOM   6845  C CG1 . VAL D 2 52  ? 24.288  3.249   -45.852  1.00 75.45  ? 52  VAL D CG1 1 
ATOM   6846  C CG2 . VAL D 2 52  ? 25.508  3.372   -48.027  1.00 72.30  ? 52  VAL D CG2 1 
ATOM   6847  N N   . ASN D 2 53  ? 21.346  1.888   -46.689  1.00 81.15  ? 53  ASN D N   1 
ATOM   6848  C CA  . ASN D 2 53  ? 20.369  1.430   -45.705  1.00 75.21  ? 53  ASN D CA  1 
ATOM   6849  C C   . ASN D 2 53  ? 19.929  -0.004  -45.982  1.00 74.99  ? 53  ASN D C   1 
ATOM   6850  O O   . ASN D 2 53  ? 19.781  -0.802  -45.050  1.00 85.75  ? 53  ASN D O   1 
ATOM   6851  C CB  . ASN D 2 53  ? 19.164  2.371   -45.683  1.00 78.66  ? 53  ASN D CB  1 
ATOM   6852  C CG  . ASN D 2 53  ? 19.511  3.750   -45.154  1.00 84.76  ? 53  ASN D CG  1 
ATOM   6853  O OD1 . ASN D 2 53  ? 20.547  3.940   -44.516  1.00 85.27  ? 53  ASN D OD1 1 
ATOM   6854  N ND2 . ASN D 2 53  ? 18.640  4.719   -45.409  1.00 89.95  ? 53  ASN D ND2 1 
ATOM   6855  N N   . SER D 2 54  ? 19.718  -0.349  -47.255  1.00 74.98  ? 54  SER D N   1 
ATOM   6856  C CA  . SER D 2 54  ? 19.277  -1.698  -47.597  1.00 79.44  ? 54  SER D CA  1 
ATOM   6857  C C   . SER D 2 54  ? 20.312  -2.736  -47.188  1.00 81.27  ? 54  SER D C   1 
ATOM   6858  O O   . SER D 2 54  ? 19.964  -3.796  -46.657  1.00 80.33  ? 54  SER D O   1 
ATOM   6859  C CB  . SER D 2 54  ? 18.993  -1.791  -49.095  1.00 83.86  ? 54  SER D CB  1 
ATOM   6860  O OG  . SER D 2 54  ? 18.244  -0.674  -49.537  1.00 96.64  ? 54  SER D OG  1 
ATOM   6861  N N   . ILE D 2 55  ? 21.592  -2.444  -47.422  1.00 80.43  ? 55  ILE D N   1 
ATOM   6862  C CA  . ILE D 2 55  ? 22.658  -3.354  -47.015  1.00 63.07  ? 55  ILE D CA  1 
ATOM   6863  C C   . ILE D 2 55  ? 22.684  -3.514  -45.500  1.00 75.70  ? 55  ILE D C   1 
ATOM   6864  O O   . ILE D 2 55  ? 22.984  -4.598  -44.984  1.00 72.49  ? 55  ILE D O   1 
ATOM   6865  C CB  . ILE D 2 55  ? 24.001  -2.849  -47.580  1.00 63.01  ? 55  ILE D CB  1 
ATOM   6866  C CG1 . ILE D 2 55  ? 24.124  -3.247  -49.054  1.00 75.28  ? 55  ILE D CG1 1 
ATOM   6867  C CG2 . ILE D 2 55  ? 25.179  -3.359  -46.758  1.00 64.85  ? 55  ILE D CG2 1 
ATOM   6868  C CD1 . ILE D 2 55  ? 24.989  -2.322  -49.882  1.00 60.74  ? 55  ILE D CD1 1 
ATOM   6869  N N   . ILE D 2 56  ? 22.343  -2.459  -44.767  1.00 72.06  ? 56  ILE D N   1 
ATOM   6870  C CA  . ILE D 2 56  ? 22.382  -2.494  -43.308  1.00 61.80  ? 56  ILE D CA  1 
ATOM   6871  C C   . ILE D 2 56  ? 21.056  -2.963  -42.718  1.00 73.22  ? 56  ILE D C   1 
ATOM   6872  O O   . ILE D 2 56  ? 21.030  -3.830  -41.840  1.00 78.86  ? 56  ILE D O   1 
ATOM   6873  C CB  . ILE D 2 56  ? 22.787  -1.106  -42.767  1.00 65.59  ? 56  ILE D CB  1 
ATOM   6874  C CG1 . ILE D 2 56  ? 24.310  -0.945  -42.829  1.00 73.77  ? 56  ILE D CG1 1 
ATOM   6875  C CG2 . ILE D 2 56  ? 22.262  -0.895  -41.351  1.00 63.21  ? 56  ILE D CG2 1 
ATOM   6876  C CD1 . ILE D 2 56  ? 24.783  0.491   -42.726  1.00 69.14  ? 56  ILE D CD1 1 
ATOM   6877  N N   . ASP D 2 57  ? 19.932  -2.412  -43.187  1.00 89.45  ? 57  ASP D N   1 
ATOM   6878  C CA  . ASP D 2 57  ? 18.658  -2.670  -42.521  1.00 76.56  ? 57  ASP D CA  1 
ATOM   6879  C C   . ASP D 2 57  ? 18.124  -4.070  -42.800  1.00 72.98  ? 57  ASP D C   1 
ATOM   6880  O O   . ASP D 2 57  ? 17.359  -4.606  -41.990  1.00 75.91  ? 57  ASP D O   1 
ATOM   6881  C CB  . ASP D 2 57  ? 17.617  -1.630  -42.936  1.00 87.55  ? 57  ASP D CB  1 
ATOM   6882  C CG  . ASP D 2 57  ? 18.001  -0.225  -42.523  1.00 104.88 ? 57  ASP D CG  1 
ATOM   6883  O OD1 . ASP D 2 57  ? 17.169  0.692   -42.680  1.00 111.26 ? 57  ASP D OD1 1 
ATOM   6884  O OD2 . ASP D 2 57  ? 19.140  -0.036  -42.050  1.00 101.02 ? 57  ASP D OD2 1 
ATOM   6885  N N   . LYS D 2 58  ? 18.497  -4.676  -43.928  1.00 75.31  ? 58  LYS D N   1 
ATOM   6886  C CA  . LYS D 2 58  ? 17.971  -5.998  -44.243  1.00 82.97  ? 58  LYS D CA  1 
ATOM   6887  C C   . LYS D 2 58  ? 18.583  -7.100  -43.391  1.00 85.33  ? 58  LYS D C   1 
ATOM   6888  O O   . LYS D 2 58  ? 18.119  -8.242  -43.465  1.00 77.07  ? 58  LYS D O   1 
ATOM   6889  C CB  . LYS D 2 58  ? 18.176  -6.325  -45.725  1.00 72.02  ? 58  LYS D CB  1 
ATOM   6890  C CG  . LYS D 2 58  ? 17.342  -5.476  -46.679  1.00 80.75  ? 58  LYS D CG  1 
ATOM   6891  C CD  . LYS D 2 58  ? 15.950  -5.220  -46.118  1.00 92.58  ? 58  LYS D CD  1 
ATOM   6892  C CE  . LYS D 2 58  ? 15.047  -4.515  -47.120  1.00 89.52  ? 58  LYS D CE  1 
ATOM   6893  N NZ  . LYS D 2 58  ? 14.231  -5.478  -47.914  1.00 85.99  ? 58  LYS D NZ  1 
ATOM   6894  N N   . MET D 2 59  ? 19.608  -6.804  -42.598  1.00 85.79  ? 59  MET D N   1 
ATOM   6895  C CA  . MET D 2 59  ? 20.197  -7.829  -41.751  1.00 76.56  ? 59  MET D CA  1 
ATOM   6896  C C   . MET D 2 59  ? 19.264  -8.147  -40.591  1.00 65.70  ? 59  MET D C   1 
ATOM   6897  O O   . MET D 2 59  ? 18.782  -7.243  -39.902  1.00 66.43  ? 59  MET D O   1 
ATOM   6898  C CB  . MET D 2 59  ? 21.555  -7.373  -41.228  1.00 66.33  ? 59  MET D CB  1 
ATOM   6899  C CG  . MET D 2 59  ? 22.319  -8.432  -40.459  1.00 64.69  ? 59  MET D CG  1 
ATOM   6900  S SD  . MET D 2 59  ? 23.019  -9.714  -41.516  1.00 87.72  ? 59  MET D SD  1 
ATOM   6901  C CE  . MET D 2 59  ? 21.737  -10.966 -41.464  1.00 86.37  ? 59  MET D CE  1 
ATOM   6902  N N   . ASN D 2 60  ? 19.010  -9.436  -40.381  1.00 59.68  ? 60  ASN D N   1 
ATOM   6903  C CA  . ASN D 2 60  ? 18.157  -9.913  -39.300  1.00 74.21  ? 60  ASN D CA  1 
ATOM   6904  C C   . ASN D 2 60  ? 19.029  -10.460 -38.180  1.00 85.30  ? 60  ASN D C   1 
ATOM   6905  O O   . ASN D 2 60  ? 19.882  -11.322 -38.414  1.00 95.91  ? 60  ASN D O   1 
ATOM   6906  C CB  . ASN D 2 60  ? 17.190  -10.992 -39.794  1.00 77.24  ? 60  ASN D CB  1 
ATOM   6907  C CG  . ASN D 2 60  ? 16.352  -11.589 -38.670  1.00 89.01  ? 60  ASN D CG  1 
ATOM   6908  O OD1 . ASN D 2 60  ? 15.470  -10.929 -38.119  1.00 92.46  ? 60  ASN D OD1 1 
ATOM   6909  N ND2 . ASN D 2 60  ? 16.625  -12.845 -38.329  1.00 83.21  ? 60  ASN D ND2 1 
ATOM   6910  N N   . THR D 2 61  ? 18.811  -9.958  -36.969  1.00 74.19  ? 61  THR D N   1 
ATOM   6911  C CA  . THR D 2 61  ? 19.599  -10.338 -35.807  1.00 82.13  ? 61  THR D CA  1 
ATOM   6912  C C   . THR D 2 61  ? 18.681  -10.791 -34.681  1.00 83.94  ? 61  THR D C   1 
ATOM   6913  O O   . THR D 2 61  ? 17.617  -10.203 -34.458  1.00 85.42  ? 61  THR D O   1 
ATOM   6914  C CB  . THR D 2 61  ? 20.481  -9.174  -35.329  1.00 85.45  ? 61  THR D CB  1 
ATOM   6915  O OG1 . THR D 2 61  ? 20.982  -9.455  -34.016  1.00 96.79  ? 61  THR D OG1 1 
ATOM   6916  C CG2 . THR D 2 61  ? 19.687  -7.873  -35.302  1.00 87.45  ? 61  THR D CG2 1 
ATOM   6917  N N   . GLN D 2 62  ? 19.100  -11.840 -33.976  1.00 80.94  ? 62  GLN D N   1 
ATOM   6918  C CA  . GLN D 2 62  ? 18.386  -12.356 -32.820  1.00 76.37  ? 62  GLN D CA  1 
ATOM   6919  C C   . GLN D 2 62  ? 19.384  -12.631 -31.703  1.00 71.08  ? 62  GLN D C   1 
ATOM   6920  O O   . GLN D 2 62  ? 20.597  -12.685 -31.925  1.00 76.69  ? 62  GLN D O   1 
ATOM   6921  C CB  . GLN D 2 62  ? 17.599  -13.631 -33.146  1.00 67.46  ? 62  GLN D CB  1 
ATOM   6922  C CG  . GLN D 2 62  ? 18.459  -14.808 -33.589  1.00 68.97  ? 62  GLN D CG  1 
ATOM   6923  C CD  . GLN D 2 62  ? 18.584  -14.910 -35.096  1.00 81.75  ? 62  GLN D CD  1 
ATOM   6924  O OE1 . GLN D 2 62  ? 17.584  -15.004 -35.810  1.00 97.95  ? 62  GLN D OE1 1 
ATOM   6925  N NE2 . GLN D 2 62  ? 19.816  -14.889 -35.590  1.00 85.17  ? 62  GLN D NE2 1 
ATOM   6926  N N   . PHE D 2 63  ? 18.859  -12.802 -30.492  1.00 71.23  ? 63  PHE D N   1 
ATOM   6927  C CA  . PHE D 2 63  ? 19.712  -13.081 -29.343  1.00 68.84  ? 63  PHE D CA  1 
ATOM   6928  C C   . PHE D 2 63  ? 20.360  -14.452 -29.488  1.00 72.56  ? 63  PHE D C   1 
ATOM   6929  O O   . PHE D 2 63  ? 19.686  -15.442 -29.790  1.00 75.24  ? 63  PHE D O   1 
ATOM   6930  C CB  . PHE D 2 63  ? 18.903  -13.015 -28.047  1.00 65.16  ? 63  PHE D CB  1 
ATOM   6931  C CG  . PHE D 2 63  ? 19.701  -13.357 -26.818  1.00 71.64  ? 63  PHE D CG  1 
ATOM   6932  C CD1 . PHE D 2 63  ? 19.766  -14.663 -26.358  1.00 62.12  ? 63  PHE D CD1 1 
ATOM   6933  C CD2 . PHE D 2 63  ? 20.384  -12.374 -26.122  1.00 73.19  ? 63  PHE D CD2 1 
ATOM   6934  C CE1 . PHE D 2 63  ? 20.500  -14.982 -25.233  1.00 62.82  ? 63  PHE D CE1 1 
ATOM   6935  C CE2 . PHE D 2 63  ? 21.119  -12.689 -24.993  1.00 67.89  ? 63  PHE D CE2 1 
ATOM   6936  C CZ  . PHE D 2 63  ? 21.177  -13.994 -24.549  1.00 76.00  ? 63  PHE D CZ  1 
ATOM   6937  N N   . GLU D 2 64  ? 21.671  -14.506 -29.266  1.00 60.89  ? 64  GLU D N   1 
ATOM   6938  C CA  . GLU D 2 64  ? 22.414  -15.756 -29.262  1.00 63.81  ? 64  GLU D CA  1 
ATOM   6939  C C   . GLU D 2 64  ? 23.457  -15.710 -28.157  1.00 64.49  ? 64  GLU D C   1 
ATOM   6940  O O   . GLU D 2 64  ? 23.990  -14.647 -27.829  1.00 69.04  ? 64  GLU D O   1 
ATOM   6941  C CB  . GLU D 2 64  ? 23.095  -16.028 -30.613  1.00 53.24  ? 64  GLU D CB  1 
ATOM   6942  C CG  . GLU D 2 64  ? 22.137  -16.228 -31.777  1.00 72.28  ? 64  GLU D CG  1 
ATOM   6943  C CD  . GLU D 2 64  ? 21.262  -17.458 -31.619  1.00 87.63  ? 64  GLU D CD  1 
ATOM   6944  O OE1 . GLU D 2 64  ? 21.626  -18.360 -30.835  1.00 99.25  ? 64  GLU D OE1 1 
ATOM   6945  O OE2 . GLU D 2 64  ? 20.208  -17.523 -32.283  1.00 82.41  ? 64  GLU D OE2 1 
ATOM   6946  N N   . ALA D 2 65  ? 23.742  -16.878 -27.587  1.00 74.18  ? 65  ALA D N   1 
ATOM   6947  C CA  . ALA D 2 65  ? 24.738  -17.028 -26.531  1.00 66.80  ? 65  ALA D CA  1 
ATOM   6948  C C   . ALA D 2 65  ? 25.798  -18.009 -27.014  1.00 68.21  ? 65  ALA D C   1 
ATOM   6949  O O   . ALA D 2 65  ? 25.527  -19.207 -27.149  1.00 66.17  ? 65  ALA D O   1 
ATOM   6950  C CB  . ALA D 2 65  ? 24.095  -17.505 -25.230  1.00 68.52  ? 65  ALA D CB  1 
ATOM   6951  N N   . VAL D 2 66  ? 27.002  -17.504 -27.264  1.00 65.92  ? 66  VAL D N   1 
ATOM   6952  C CA  . VAL D 2 66  ? 28.110  -18.314 -27.758  1.00 68.14  ? 66  VAL D CA  1 
ATOM   6953  C C   . VAL D 2 66  ? 29.080  -18.553 -26.610  1.00 72.24  ? 66  VAL D C   1 
ATOM   6954  O O   . VAL D 2 66  ? 29.601  -17.602 -26.015  1.00 77.54  ? 66  VAL D O   1 
ATOM   6955  C CB  . VAL D 2 66  ? 28.815  -17.639 -28.945  1.00 72.52  ? 66  VAL D CB  1 
ATOM   6956  C CG1 . VAL D 2 66  ? 29.993  -18.481 -29.405  1.00 64.77  ? 66  VAL D CG1 1 
ATOM   6957  C CG2 . VAL D 2 66  ? 27.835  -17.415 -30.086  1.00 56.90  ? 66  VAL D CG2 1 
ATOM   6958  N N   . GLY D 2 67  ? 29.322  -19.825 -26.298  1.00 75.26  ? 67  GLY D N   1 
ATOM   6959  C CA  . GLY D 2 67  ? 30.262  -20.211 -25.268  1.00 54.32  ? 67  GLY D CA  1 
ATOM   6960  C C   . GLY D 2 67  ? 30.781  -21.606 -25.540  1.00 77.08  ? 67  GLY D C   1 
ATOM   6961  O O   . GLY D 2 67  ? 30.389  -22.257 -26.510  1.00 87.69  ? 67  GLY D O   1 
ATOM   6962  N N   . ARG D 2 68  ? 31.683  -22.060 -24.673  1.00 61.58  ? 68  ARG D N   1 
ATOM   6963  C CA  . ARG D 2 68  ? 32.232  -23.413 -24.730  1.00 69.76  ? 68  ARG D CA  1 
ATOM   6964  C C   . ARG D 2 68  ? 31.743  -24.161 -23.496  1.00 69.05  ? 68  ARG D C   1 
ATOM   6965  O O   . ARG D 2 68  ? 32.215  -23.922 -22.381  1.00 93.77  ? 68  ARG D O   1 
ATOM   6966  C CB  . ARG D 2 68  ? 33.754  -23.392 -24.810  1.00 80.44  ? 68  ARG D CB  1 
ATOM   6967  C CG  . ARG D 2 68  ? 34.292  -23.232 -26.220  1.00 86.29  ? 68  ARG D CG  1 
ATOM   6968  C CD  . ARG D 2 68  ? 35.703  -23.775 -26.305  1.00 114.57 ? 68  ARG D CD  1 
ATOM   6969  N NE  . ARG D 2 68  ? 35.879  -24.909 -25.406  1.00 118.70 ? 68  ARG D NE  1 
ATOM   6970  C CZ  . ARG D 2 68  ? 36.932  -25.715 -25.407  1.00 88.73  ? 68  ARG D CZ  1 
ATOM   6971  N NH1 . ARG D 2 68  ? 37.911  -25.572 -26.284  1.00 100.05 ? 68  ARG D NH1 1 
ATOM   6972  N NH2 . ARG D 2 68  ? 37.002  -26.690 -24.505  1.00 77.55  ? 68  ARG D NH2 1 
ATOM   6973  N N   . GLU D 2 69  ? 30.799  -25.076 -23.702  1.00 68.77  ? 69  GLU D N   1 
ATOM   6974  C CA  . GLU D 2 69  ? 30.061  -25.703 -22.614  1.00 73.77  ? 69  GLU D CA  1 
ATOM   6975  C C   . GLU D 2 69  ? 30.109  -27.227 -22.679  1.00 69.96  ? 69  GLU D C   1 
ATOM   6976  O O   . GLU D 2 69  ? 29.199  -27.897 -22.186  1.00 76.56  ? 69  GLU D O   1 
ATOM   6977  C CB  . GLU D 2 69  ? 28.618  -25.205 -22.612  1.00 74.74  ? 69  GLU D CB  1 
ATOM   6978  C CG  . GLU D 2 69  ? 28.078  -24.882 -24.009  1.00 85.15  ? 69  GLU D CG  1 
ATOM   6979  C CD  . GLU D 2 69  ? 26.857  -23.978 -23.972  1.00 107.51 ? 69  GLU D CD  1 
ATOM   6980  O OE1 . GLU D 2 69  ? 25.906  -24.223 -24.746  1.00 95.09  ? 69  GLU D OE1 1 
ATOM   6981  O OE2 . GLU D 2 69  ? 26.848  -23.023 -23.164  1.00 99.44  ? 69  GLU D OE2 1 
ATOM   6982  N N   . PHE D 2 70  ? 31.159  -27.789 -23.276  1.00 66.11  ? 70  PHE D N   1 
ATOM   6983  C CA  . PHE D 2 70  ? 31.313  -29.232 -23.401  1.00 69.87  ? 70  PHE D CA  1 
ATOM   6984  C C   . PHE D 2 70  ? 32.598  -29.680 -22.715  1.00 79.11  ? 70  PHE D C   1 
ATOM   6985  O O   . PHE D 2 70  ? 33.633  -29.013 -22.817  1.00 81.86  ? 70  PHE D O   1 
ATOM   6986  C CB  . PHE D 2 70  ? 31.313  -29.649 -24.872  1.00 67.88  ? 70  PHE D CB  1 
ATOM   6987  C CG  . PHE D 2 70  ? 30.101  -29.187 -25.630  1.00 60.30  ? 70  PHE D CG  1 
ATOM   6988  C CD1 . PHE D 2 70  ? 28.842  -29.661 -25.300  1.00 73.41  ? 70  PHE D CD1 1 
ATOM   6989  C CD2 . PHE D 2 70  ? 30.218  -28.275 -26.664  1.00 64.07  ? 70  PHE D CD2 1 
ATOM   6990  C CE1 . PHE D 2 70  ? 27.720  -29.236 -25.990  1.00 64.39  ? 70  PHE D CE1 1 
ATOM   6991  C CE2 . PHE D 2 70  ? 29.099  -27.850 -27.358  1.00 80.06  ? 70  PHE D CE2 1 
ATOM   6992  C CZ  . PHE D 2 70  ? 27.850  -28.331 -27.020  1.00 56.17  ? 70  PHE D CZ  1 
ATOM   6993  N N   . ASN D 2 71  ? 32.523  -30.808 -22.010  1.00 70.50  ? 71  ASN D N   1 
ATOM   6994  C CA  . ASN D 2 71  ? 33.626  -31.277 -21.182  1.00 60.85  ? 71  ASN D CA  1 
ATOM   6995  C C   . ASN D 2 71  ? 34.646  -32.030 -22.033  1.00 61.40  ? 71  ASN D C   1 
ATOM   6996  O O   . ASN D 2 71  ? 34.601  -32.024 -23.266  1.00 70.20  ? 71  ASN D O   1 
ATOM   6997  C CB  . ASN D 2 71  ? 33.099  -32.124 -20.022  1.00 57.11  ? 71  ASN D CB  1 
ATOM   6998  C CG  . ASN D 2 71  ? 32.384  -33.394 -20.477  1.00 58.53  ? 71  ASN D CG  1 
ATOM   6999  O OD1 . ASN D 2 71  ? 32.827  -34.092 -21.390  1.00 64.78  ? 71  ASN D OD1 1 
ATOM   7000  N ND2 . ASN D 2 71  ? 31.272  -33.701 -19.822  1.00 64.54  ? 71  ASN D ND2 1 
ATOM   7001  N N   . ASN D 2 72  ? 35.585  -32.703 -21.364  1.00 64.54  ? 72  ASN D N   1 
ATOM   7002  C CA  . ASN D 2 72  ? 36.693  -33.347 -22.060  1.00 62.52  ? 72  ASN D CA  1 
ATOM   7003  C C   . ASN D 2 72  ? 36.272  -34.620 -22.787  1.00 64.13  ? 72  ASN D C   1 
ATOM   7004  O O   . ASN D 2 72  ? 36.968  -35.042 -23.717  1.00 71.71  ? 72  ASN D O   1 
ATOM   7005  C CB  . ASN D 2 72  ? 37.823  -33.652 -21.076  1.00 71.41  ? 72  ASN D CB  1 
ATOM   7006  C CG  . ASN D 2 72  ? 39.131  -33.967 -21.772  1.00 96.25  ? 72  ASN D CG  1 
ATOM   7007  O OD1 . ASN D 2 72  ? 39.564  -33.239 -22.669  1.00 92.42  ? 72  ASN D OD1 1 
ATOM   7008  N ND2 . ASN D 2 72  ? 39.766  -35.058 -21.366  1.00 108.24 ? 72  ASN D ND2 1 
ATOM   7009  N N   . LEU D 2 73  ? 35.160  -35.240 -22.393  1.00 56.88  ? 73  LEU D N   1 
ATOM   7010  C CA  . LEU D 2 73  ? 34.641  -36.420 -23.072  1.00 58.19  ? 73  LEU D CA  1 
ATOM   7011  C C   . LEU D 2 73  ? 33.492  -36.084 -24.018  1.00 62.96  ? 73  LEU D C   1 
ATOM   7012  O O   . LEU D 2 73  ? 32.739  -36.980 -24.417  1.00 57.69  ? 73  LEU D O   1 
ATOM   7013  C CB  . LEU D 2 73  ? 34.205  -37.471 -22.052  1.00 58.41  ? 73  LEU D CB  1 
ATOM   7014  C CG  . LEU D 2 73  ? 35.286  -38.493 -21.694  1.00 58.97  ? 73  LEU D CG  1 
ATOM   7015  C CD1 . LEU D 2 73  ? 34.754  -39.526 -20.715  1.00 49.36  ? 73  LEU D CD1 1 
ATOM   7016  C CD2 . LEU D 2 73  ? 35.816  -39.167 -22.953  1.00 61.86  ? 73  LEU D CD2 1 
ATOM   7017  N N   . GLU D 2 74  ? 33.338  -34.811 -24.370  1.00 58.39  ? 74  GLU D N   1 
ATOM   7018  C CA  . GLU D 2 74  ? 32.354  -34.350 -25.340  1.00 60.00  ? 74  GLU D CA  1 
ATOM   7019  C C   . GLU D 2 74  ? 33.039  -33.599 -26.476  1.00 64.63  ? 74  GLU D C   1 
ATOM   7020  O O   . GLU D 2 74  ? 32.554  -32.570 -26.952  1.00 65.96  ? 74  GLU D O   1 
ATOM   7021  C CB  . GLU D 2 74  ? 31.297  -33.475 -24.667  1.00 53.12  ? 74  GLU D CB  1 
ATOM   7022  C CG  . GLU D 2 74  ? 30.453  -34.213 -23.643  1.00 48.16  ? 74  GLU D CG  1 
ATOM   7023  C CD  . GLU D 2 74  ? 29.625  -33.278 -22.789  1.00 74.65  ? 74  GLU D CD  1 
ATOM   7024  O OE1 . GLU D 2 74  ? 30.096  -32.157 -22.502  1.00 69.36  ? 74  GLU D OE1 1 
ATOM   7025  O OE2 . GLU D 2 74  ? 28.499  -33.663 -22.408  1.00 70.61  ? 74  GLU D OE2 1 
ATOM   7026  N N   . ARG D 2 75  ? 34.187  -34.116 -26.923  1.00 62.56  ? 75  ARG D N   1 
ATOM   7027  C CA  . ARG D 2 75  ? 34.956  -33.438 -27.962  1.00 66.31  ? 75  ARG D CA  1 
ATOM   7028  C C   . ARG D 2 75  ? 34.298  -33.552 -29.332  1.00 66.14  ? 75  ARG D C   1 
ATOM   7029  O O   . ARG D 2 75  ? 34.409  -32.628 -30.145  1.00 53.36  ? 75  ARG D O   1 
ATOM   7030  C CB  . ARG D 2 75  ? 36.379  -34.000 -28.011  1.00 49.41  ? 75  ARG D CB  1 
ATOM   7031  C CG  . ARG D 2 75  ? 37.215  -33.744 -26.757  1.00 47.37  ? 75  ARG D CG  1 
ATOM   7032  C CD  . ARG D 2 75  ? 37.631  -32.279 -26.627  1.00 65.98  ? 75  ARG D CD  1 
ATOM   7033  N NE  . ARG D 2 75  ? 36.594  -31.433 -26.044  1.00 73.45  ? 75  ARG D NE  1 
ATOM   7034  C CZ  . ARG D 2 75  ? 36.681  -30.114 -25.933  1.00 90.43  ? 75  ARG D CZ  1 
ATOM   7035  N NH1 . ARG D 2 75  ? 37.736  -29.450 -26.379  1.00 84.31  ? 75  ARG D NH1 1 
ATOM   7036  N NH2 . ARG D 2 75  ? 35.685  -29.443 -25.360  1.00 74.85  ? 75  ARG D NH2 1 
ATOM   7037  N N   . ARG D 2 76  ? 33.621  -34.669 -29.609  1.00 57.99  ? 76  ARG D N   1 
ATOM   7038  C CA  . ARG D 2 76  ? 32.930  -34.810 -30.886  1.00 54.45  ? 76  ARG D CA  1 
ATOM   7039  C C   . ARG D 2 76  ? 31.828  -33.768 -31.032  1.00 63.22  ? 76  ARG D C   1 
ATOM   7040  O O   . ARG D 2 76  ? 31.669  -33.166 -32.101  1.00 70.71  ? 76  ARG D O   1 
ATOM   7041  C CB  . ARG D 2 76  ? 32.352  -36.219 -31.020  1.00 44.37  ? 76  ARG D CB  1 
ATOM   7042  C CG  . ARG D 2 76  ? 33.384  -37.334 -31.030  1.00 46.19  ? 76  ARG D CG  1 
ATOM   7043  C CD  . ARG D 2 76  ? 32.692  -38.682 -30.956  1.00 56.62  ? 76  ARG D CD  1 
ATOM   7044  N NE  . ARG D 2 76  ? 31.964  -38.837 -29.702  1.00 52.14  ? 76  ARG D NE  1 
ATOM   7045  C CZ  . ARG D 2 76  ? 30.901  -39.611 -29.538  1.00 60.82  ? 76  ARG D CZ  1 
ATOM   7046  N NH1 . ARG D 2 76  ? 30.381  -40.295 -30.545  1.00 62.62  ? 76  ARG D NH1 1 
ATOM   7047  N NH2 . ARG D 2 76  ? 30.339  -39.696 -28.336  1.00 49.38  ? 76  ARG D NH2 1 
ATOM   7048  N N   . ILE D 2 77  ? 31.058  -33.542 -29.967  1.00 65.34  ? 77  ILE D N   1 
ATOM   7049  C CA  . ILE D 2 77  ? 30.011  -32.526 -30.007  1.00 63.13  ? 77  ILE D CA  1 
ATOM   7050  C C   . ILE D 2 77  ? 30.621  -31.130 -30.072  1.00 59.65  ? 77  ILE D C   1 
ATOM   7051  O O   . ILE D 2 77  ? 30.100  -30.242 -30.760  1.00 62.24  ? 77  ILE D O   1 
ATOM   7052  C CB  . ILE D 2 77  ? 29.068  -32.700 -28.803  1.00 63.66  ? 77  ILE D CB  1 
ATOM   7053  C CG1 . ILE D 2 77  ? 28.173  -33.923 -29.022  1.00 70.19  ? 77  ILE D CG1 1 
ATOM   7054  C CG2 . ILE D 2 77  ? 28.228  -31.457 -28.587  1.00 57.03  ? 77  ILE D CG2 1 
ATOM   7055  C CD1 . ILE D 2 77  ? 28.027  -34.811 -27.807  1.00 83.46  ? 77  ILE D CD1 1 
ATOM   7056  N N   . GLU D 2 78  ? 31.739  -30.914 -29.374  1.00 50.31  ? 78  GLU D N   1 
ATOM   7057  C CA  . GLU D 2 78  ? 32.437  -29.637 -29.480  1.00 65.49  ? 78  GLU D CA  1 
ATOM   7058  C C   . GLU D 2 78  ? 32.934  -29.399 -30.902  1.00 66.83  ? 78  GLU D C   1 
ATOM   7059  O O   . GLU D 2 78  ? 32.874  -28.273 -31.408  1.00 67.26  ? 78  GLU D O   1 
ATOM   7060  C CB  . GLU D 2 78  ? 33.598  -29.582 -28.484  1.00 57.54  ? 78  GLU D CB  1 
ATOM   7061  C CG  . GLU D 2 78  ? 34.597  -28.460 -28.745  1.00 72.91  ? 78  GLU D CG  1 
ATOM   7062  C CD  . GLU D 2 78  ? 33.951  -27.086 -28.776  1.00 113.33 ? 78  GLU D CD  1 
ATOM   7063  O OE1 . GLU D 2 78  ? 33.015  -26.844 -27.984  1.00 111.94 ? 78  GLU D OE1 1 
ATOM   7064  O OE2 . GLU D 2 78  ? 34.373  -26.249 -29.602  1.00 106.03 ? 78  GLU D OE2 1 
ATOM   7065  N N   . ASN D 2 79  ? 33.422  -30.452 -31.563  1.00 59.66  ? 79  ASN D N   1 
ATOM   7066  C CA  . ASN D 2 79  ? 33.870  -30.318 -32.945  1.00 61.33  ? 79  ASN D CA  1 
ATOM   7067  C C   . ASN D 2 79  ? 32.722  -29.931 -33.868  1.00 69.40  ? 79  ASN D C   1 
ATOM   7068  O O   . ASN D 2 79  ? 32.929  -29.196 -34.841  1.00 69.09  ? 79  ASN D O   1 
ATOM   7069  C CB  . ASN D 2 79  ? 34.512  -31.621 -33.419  1.00 60.30  ? 79  ASN D CB  1 
ATOM   7070  C CG  . ASN D 2 79  ? 35.201  -31.476 -34.761  1.00 79.52  ? 79  ASN D CG  1 
ATOM   7071  O OD1 . ASN D 2 79  ? 35.854  -30.467 -35.026  1.00 85.05  ? 79  ASN D OD1 1 
ATOM   7072  N ND2 . ASN D 2 79  ? 35.054  -32.481 -35.618  1.00 69.77  ? 79  ASN D ND2 1 
ATOM   7073  N N   . LEU D 2 80  ? 31.513  -30.423 -33.590  1.00 58.24  ? 80  LEU D N   1 
ATOM   7074  C CA  . LEU D 2 80  ? 30.356  -30.034 -34.388  1.00 56.77  ? 80  LEU D CA  1 
ATOM   7075  C C   . LEU D 2 80  ? 30.076  -28.542 -34.255  1.00 63.05  ? 80  LEU D C   1 
ATOM   7076  O O   . LEU D 2 80  ? 29.742  -27.876 -35.242  1.00 66.66  ? 80  LEU D O   1 
ATOM   7077  C CB  . LEU D 2 80  ? 29.135  -30.856 -33.969  1.00 43.97  ? 80  LEU D CB  1 
ATOM   7078  C CG  . LEU D 2 80  ? 28.062  -31.161 -35.017  1.00 61.58  ? 80  LEU D CG  1 
ATOM   7079  C CD1 . LEU D 2 80  ? 27.265  -32.386 -34.598  1.00 60.76  ? 80  LEU D CD1 1 
ATOM   7080  C CD2 . LEU D 2 80  ? 27.132  -29.977 -35.232  1.00 64.14  ? 80  LEU D CD2 1 
ATOM   7081  N N   . ASN D 2 81  ? 30.200  -28.003 -33.038  1.00 62.18  ? 81  ASN D N   1 
ATOM   7082  C CA  . ASN D 2 81  ? 30.037  -26.566 -32.838  1.00 66.38  ? 81  ASN D CA  1 
ATOM   7083  C C   . ASN D 2 81  ? 31.107  -25.779 -33.584  1.00 64.70  ? 81  ASN D C   1 
ATOM   7084  O O   . ASN D 2 81  ? 30.822  -24.723 -34.163  1.00 62.48  ? 81  ASN D O   1 
ATOM   7085  C CB  . ASN D 2 81  ? 30.074  -26.236 -31.345  1.00 57.03  ? 81  ASN D CB  1 
ATOM   7086  C CG  . ASN D 2 81  ? 30.049  -24.742 -31.074  1.00 67.72  ? 81  ASN D CG  1 
ATOM   7087  O OD1 . ASN D 2 81  ? 29.060  -24.062 -31.352  1.00 69.97  ? 81  ASN D OD1 1 
ATOM   7088  N ND2 . ASN D 2 81  ? 31.138  -24.225 -30.519  1.00 79.65  ? 81  ASN D ND2 1 
ATOM   7089  N N   . LYS D 2 82  ? 32.349  -26.269 -33.569  1.00 57.51  ? 82  LYS D N   1 
ATOM   7090  C CA  . LYS D 2 82  ? 33.426  -25.595 -34.288  1.00 65.30  ? 82  LYS D CA  1 
ATOM   7091  C C   . LYS D 2 82  ? 33.143  -25.543 -35.784  1.00 61.45  ? 82  LYS D C   1 
ATOM   7092  O O   . LYS D 2 82  ? 33.306  -24.498 -36.423  1.00 69.53  ? 82  LYS D O   1 
ATOM   7093  C CB  . LYS D 2 82  ? 34.756  -26.300 -34.019  1.00 56.51  ? 82  LYS D CB  1 
ATOM   7094  C CG  . LYS D 2 82  ? 35.804  -26.082 -35.100  1.00 69.41  ? 82  LYS D CG  1 
ATOM   7095  C CD  . LYS D 2 82  ? 37.103  -26.793 -34.758  1.00 73.02  ? 82  LYS D CD  1 
ATOM   7096  C CE  . LYS D 2 82  ? 38.084  -26.763 -35.921  1.00 76.62  ? 82  LYS D CE  1 
ATOM   7097  N NZ  . LYS D 2 82  ? 38.336  -28.134 -36.451  1.00 91.17  ? 82  LYS D NZ  1 
ATOM   7098  N N   . LYS D 2 83  ? 32.717  -26.668 -36.361  1.00 58.66  ? 83  LYS D N   1 
ATOM   7099  C CA  . LYS D 2 83  ? 32.429  -26.693 -37.791  1.00 61.44  ? 83  LYS D CA  1 
ATOM   7100  C C   . LYS D 2 83  ? 31.263  -25.774 -38.135  1.00 61.61  ? 83  LYS D C   1 
ATOM   7101  O O   . LYS D 2 83  ? 31.273  -25.113 -39.179  1.00 69.86  ? 83  LYS D O   1 
ATOM   7102  C CB  . LYS D 2 83  ? 32.150  -28.126 -38.247  1.00 50.61  ? 83  LYS D CB  1 
ATOM   7103  C CG  . LYS D 2 83  ? 33.369  -29.035 -38.167  1.00 61.58  ? 83  LYS D CG  1 
ATOM   7104  C CD  . LYS D 2 83  ? 33.157  -30.361 -38.884  1.00 61.02  ? 83  LYS D CD  1 
ATOM   7105  C CE  . LYS D 2 83  ? 32.420  -31.363 -38.014  1.00 65.63  ? 83  LYS D CE  1 
ATOM   7106  N NZ  . LYS D 2 83  ? 32.660  -32.759 -38.479  1.00 72.02  ? 83  LYS D NZ  1 
ATOM   7107  N N   . MET D 2 84  ? 30.247  -25.722 -37.270  1.00 64.17  ? 84  MET D N   1 
ATOM   7108  C CA  . MET D 2 84  ? 29.121  -24.822 -37.501  1.00 68.45  ? 84  MET D CA  1 
ATOM   7109  C C   . MET D 2 84  ? 29.559  -23.363 -37.429  1.00 61.44  ? 84  MET D C   1 
ATOM   7110  O O   . MET D 2 84  ? 29.239  -22.563 -38.316  1.00 69.16  ? 84  MET D O   1 
ATOM   7111  C CB  . MET D 2 84  ? 28.011  -25.100 -36.485  1.00 64.36  ? 84  MET D CB  1 
ATOM   7112  C CG  . MET D 2 84  ? 26.739  -24.301 -36.721  1.00 62.21  ? 84  MET D CG  1 
ATOM   7113  S SD  . MET D 2 84  ? 25.859  -23.907 -35.196  1.00 80.14  ? 84  MET D SD  1 
ATOM   7114  C CE  . MET D 2 84  ? 26.842  -22.544 -34.574  1.00 74.29  ? 84  MET D CE  1 
ATOM   7115  N N   . GLU D 2 85  ? 30.296  -22.999 -36.376  1.00 68.67  ? 85  GLU D N   1 
ATOM   7116  C CA  . GLU D 2 85  ? 30.723  -21.611 -36.214  1.00 69.91  ? 85  GLU D CA  1 
ATOM   7117  C C   . GLU D 2 85  ? 31.687  -21.187 -37.316  1.00 69.79  ? 85  GLU D C   1 
ATOM   7118  O O   . GLU D 2 85  ? 31.576  -20.078 -37.852  1.00 76.19  ? 85  GLU D O   1 
ATOM   7119  C CB  . GLU D 2 85  ? 31.356  -21.411 -34.838  1.00 73.11  ? 85  GLU D CB  1 
ATOM   7120  C CG  . GLU D 2 85  ? 30.350  -21.128 -33.737  1.00 84.64  ? 85  GLU D CG  1 
ATOM   7121  C CD  . GLU D 2 85  ? 30.996  -21.009 -32.371  1.00 104.19 ? 85  GLU D CD  1 
ATOM   7122  O OE1 . GLU D 2 85  ? 32.240  -20.907 -32.304  1.00 87.91  ? 85  GLU D OE1 1 
ATOM   7123  O OE2 . GLU D 2 85  ? 30.257  -21.024 -31.365  1.00 107.71 ? 85  GLU D OE2 1 
ATOM   7124  N N   . ASP D 2 86  ? 32.644  -22.050 -37.664  1.00 66.84  ? 86  ASP D N   1 
ATOM   7125  C CA  . ASP D 2 86  ? 33.557  -21.726 -38.753  1.00 59.57  ? 86  ASP D CA  1 
ATOM   7126  C C   . ASP D 2 86  ? 32.830  -21.660 -40.089  1.00 67.50  ? 86  ASP D C   1 
ATOM   7127  O O   . ASP D 2 86  ? 33.191  -20.849 -40.950  1.00 67.66  ? 86  ASP D O   1 
ATOM   7128  C CB  . ASP D 2 86  ? 34.695  -22.745 -38.813  1.00 62.84  ? 86  ASP D CB  1 
ATOM   7129  C CG  . ASP D 2 86  ? 35.636  -22.636 -37.627  1.00 78.77  ? 86  ASP D CG  1 
ATOM   7130  O OD1 . ASP D 2 86  ? 35.542  -21.639 -36.881  1.00 79.03  ? 86  ASP D OD1 1 
ATOM   7131  O OD2 . ASP D 2 86  ? 36.466  -23.550 -37.436  1.00 73.23  ? 86  ASP D OD2 1 
ATOM   7132  N N   . GLY D 2 87  ? 31.811  -22.500 -40.281  1.00 66.69  ? 87  GLY D N   1 
ATOM   7133  C CA  . GLY D 2 87  ? 31.052  -22.457 -41.520  1.00 53.33  ? 87  GLY D CA  1 
ATOM   7134  C C   . GLY D 2 87  ? 30.321  -21.143 -41.715  1.00 58.29  ? 87  GLY D C   1 
ATOM   7135  O O   . GLY D 2 87  ? 30.312  -20.584 -42.815  1.00 78.29  ? 87  GLY D O   1 
ATOM   7136  N N   . PHE D 2 88  ? 29.694  -20.632 -40.653  1.00 55.74  ? 88  PHE D N   1 
ATOM   7137  C CA  . PHE D 2 88  ? 29.019  -19.342 -40.755  1.00 61.72  ? 88  PHE D CA  1 
ATOM   7138  C C   . PHE D 2 88  ? 30.015  -18.194 -40.839  1.00 63.48  ? 88  PHE D C   1 
ATOM   7139  O O   . PHE D 2 88  ? 29.700  -17.144 -41.412  1.00 69.87  ? 88  PHE D O   1 
ATOM   7140  C CB  . PHE D 2 88  ? 28.071  -19.142 -39.573  1.00 48.76  ? 88  PHE D CB  1 
ATOM   7141  C CG  . PHE D 2 88  ? 26.823  -19.972 -39.653  1.00 63.37  ? 88  PHE D CG  1 
ATOM   7142  C CD1 . PHE D 2 88  ? 25.904  -19.763 -40.667  1.00 71.00  ? 88  PHE D CD1 1 
ATOM   7143  C CD2 . PHE D 2 88  ? 26.564  -20.955 -38.713  1.00 62.98  ? 88  PHE D CD2 1 
ATOM   7144  C CE1 . PHE D 2 88  ? 24.753  -20.523 -40.747  1.00 69.38  ? 88  PHE D CE1 1 
ATOM   7145  C CE2 . PHE D 2 88  ? 25.413  -21.718 -38.788  1.00 65.33  ? 88  PHE D CE2 1 
ATOM   7146  C CZ  . PHE D 2 88  ? 24.507  -21.502 -39.806  1.00 65.35  ? 88  PHE D CZ  1 
ATOM   7147  N N   . LEU D 2 89  ? 31.210  -18.365 -40.270  1.00 61.89  ? 89  LEU D N   1 
ATOM   7148  C CA  . LEU D 2 89  ? 32.251  -17.355 -40.428  1.00 63.48  ? 89  LEU D CA  1 
ATOM   7149  C C   . LEU D 2 89  ? 32.682  -17.237 -41.884  1.00 68.25  ? 89  LEU D C   1 
ATOM   7150  O O   . LEU D 2 89  ? 32.867  -16.128 -42.397  1.00 72.33  ? 89  LEU D O   1 
ATOM   7151  C CB  . LEU D 2 89  ? 33.452  -17.690 -39.543  1.00 53.48  ? 89  LEU D CB  1 
ATOM   7152  C CG  . LEU D 2 89  ? 34.622  -16.708 -39.634  1.00 60.75  ? 89  LEU D CG  1 
ATOM   7153  C CD1 . LEU D 2 89  ? 34.235  -15.363 -39.041  1.00 58.62  ? 89  LEU D CD1 1 
ATOM   7154  C CD2 . LEU D 2 89  ? 35.869  -17.262 -38.960  1.00 72.53  ? 89  LEU D CD2 1 
ATOM   7155  N N   . ASP D 2 90  ? 32.846  -18.373 -42.567  1.00 60.62  ? 90  ASP D N   1 
ATOM   7156  C CA  . ASP D 2 90  ? 33.255  -18.347 -43.968  1.00 63.10  ? 90  ASP D CA  1 
ATOM   7157  C C   . ASP D 2 90  ? 32.155  -17.785 -44.861  1.00 66.22  ? 90  ASP D C   1 
ATOM   7158  O O   . ASP D 2 90  ? 32.439  -17.049 -45.812  1.00 70.86  ? 90  ASP D O   1 
ATOM   7159  C CB  . ASP D 2 90  ? 33.656  -19.750 -44.421  1.00 59.78  ? 90  ASP D CB  1 
ATOM   7160  C CG  . ASP D 2 90  ? 34.884  -20.268 -43.698  1.00 66.93  ? 90  ASP D CG  1 
ATOM   7161  O OD1 . ASP D 2 90  ? 35.486  -19.499 -42.920  1.00 67.64  ? 90  ASP D OD1 1 
ATOM   7162  O OD2 . ASP D 2 90  ? 35.249  -21.443 -43.906  1.00 74.78  ? 90  ASP D OD2 1 
ATOM   7163  N N   . VAL D 2 91  ? 30.896  -18.127 -44.576  1.00 62.07  ? 91  VAL D N   1 
ATOM   7164  C CA  . VAL D 2 91  ? 29.789  -17.637 -45.396  1.00 53.52  ? 91  VAL D CA  1 
ATOM   7165  C C   . VAL D 2 91  ? 29.667  -16.123 -45.279  1.00 52.62  ? 91  VAL D C   1 
ATOM   7166  O O   . VAL D 2 91  ? 29.580  -15.408 -46.285  1.00 53.75  ? 91  VAL D O   1 
ATOM   7167  C CB  . VAL D 2 91  ? 28.476  -18.339 -45.004  1.00 46.01  ? 91  VAL D CB  1 
ATOM   7168  C CG1 . VAL D 2 91  ? 27.277  -17.529 -45.476  1.00 47.76  ? 91  VAL D CG1 1 
ATOM   7169  C CG2 . VAL D 2 91  ? 28.425  -19.740 -45.587  1.00 42.49  ? 91  VAL D CG2 1 
ATOM   7170  N N   . TRP D 2 92  ? 29.661  -15.610 -44.047  1.00 55.06  ? 92  TRP D N   1 
ATOM   7171  C CA  . TRP D 2 92  ? 29.477  -14.175 -43.851  1.00 60.31  ? 92  TRP D CA  1 
ATOM   7172  C C   . TRP D 2 92  ? 30.668  -13.380 -44.373  1.00 66.58  ? 92  TRP D C   1 
ATOM   7173  O O   . TRP D 2 92  ? 30.488  -12.326 -44.993  1.00 67.34  ? 92  TRP D O   1 
ATOM   7174  C CB  . TRP D 2 92  ? 29.231  -13.868 -42.374  1.00 59.05  ? 92  TRP D CB  1 
ATOM   7175  C CG  . TRP D 2 92  ? 27.841  -14.200 -41.916  1.00 68.78  ? 92  TRP D CG  1 
ATOM   7176  C CD1 . TRP D 2 92  ? 27.491  -15.035 -40.895  1.00 61.72  ? 92  TRP D CD1 1 
ATOM   7177  C CD2 . TRP D 2 92  ? 26.614  -13.708 -42.470  1.00 58.96  ? 92  TRP D CD2 1 
ATOM   7178  N NE1 . TRP D 2 92  ? 26.123  -15.089 -40.775  1.00 65.31  ? 92  TRP D NE1 1 
ATOM   7179  C CE2 . TRP D 2 92  ? 25.562  -14.285 -41.732  1.00 65.99  ? 92  TRP D CE2 1 
ATOM   7180  C CE3 . TRP D 2 92  ? 26.302  -12.835 -43.518  1.00 56.89  ? 92  TRP D CE3 1 
ATOM   7181  C CZ2 . TRP D 2 92  ? 24.224  -14.017 -42.005  1.00 74.56  ? 92  TRP D CZ2 1 
ATOM   7182  C CZ3 . TRP D 2 92  ? 24.973  -12.572 -43.789  1.00 65.77  ? 92  TRP D CZ3 1 
ATOM   7183  C CH2 . TRP D 2 92  ? 23.950  -13.162 -43.037  1.00 73.98  ? 92  TRP D CH2 1 
ATOM   7184  N N   . THR D 2 93  ? 31.889  -13.862 -44.132  1.00 69.22  ? 93  THR D N   1 
ATOM   7185  C CA  . THR D 2 93  ? 33.071  -13.141 -44.596  1.00 78.17  ? 93  THR D CA  1 
ATOM   7186  C C   . THR D 2 93  ? 33.106  -13.058 -46.117  1.00 77.70  ? 93  THR D C   1 
ATOM   7187  O O   . THR D 2 93  ? 33.414  -12.001 -46.682  1.00 85.51  ? 93  THR D O   1 
ATOM   7188  C CB  . THR D 2 93  ? 34.340  -13.814 -44.069  1.00 60.17  ? 93  THR D CB  1 
ATOM   7189  O OG1 . THR D 2 93  ? 34.389  -13.697 -42.642  1.00 64.87  ? 93  THR D OG1 1 
ATOM   7190  C CG2 . THR D 2 93  ? 35.584  -13.171 -44.667  1.00 63.47  ? 93  THR D CG2 1 
ATOM   7191  N N   . TYR D 2 94  ? 32.791  -14.161 -46.797  1.00 69.28  ? 94  TYR D N   1 
ATOM   7192  C CA  . TYR D 2 94  ? 32.840  -14.178 -48.255  1.00 61.58  ? 94  TYR D CA  1 
ATOM   7193  C C   . TYR D 2 94  ? 31.764  -13.279 -48.855  1.00 68.28  ? 94  TYR D C   1 
ATOM   7194  O O   . TYR D 2 94  ? 32.040  -12.488 -49.765  1.00 72.17  ? 94  TYR D O   1 
ATOM   7195  C CB  . TYR D 2 94  ? 32.696  -15.613 -48.763  1.00 63.04  ? 94  TYR D CB  1 
ATOM   7196  C CG  . TYR D 2 94  ? 32.997  -15.789 -50.235  1.00 65.45  ? 94  TYR D CG  1 
ATOM   7197  C CD1 . TYR D 2 94  ? 34.290  -15.651 -50.719  1.00 63.67  ? 94  TYR D CD1 1 
ATOM   7198  C CD2 . TYR D 2 94  ? 31.990  -16.109 -51.137  1.00 59.54  ? 94  TYR D CD2 1 
ATOM   7199  C CE1 . TYR D 2 94  ? 34.572  -15.816 -52.062  1.00 62.38  ? 94  TYR D CE1 1 
ATOM   7200  C CE2 . TYR D 2 94  ? 32.263  -16.277 -52.482  1.00 64.28  ? 94  TYR D CE2 1 
ATOM   7201  C CZ  . TYR D 2 94  ? 33.556  -16.129 -52.938  1.00 64.59  ? 94  TYR D CZ  1 
ATOM   7202  O OH  . TYR D 2 94  ? 33.837  -16.294 -54.275  1.00 70.16  ? 94  TYR D OH  1 
ATOM   7203  N N   . ASN D 2 95  ? 30.530  -13.385 -48.356  1.00 69.03  ? 95  ASN D N   1 
ATOM   7204  C CA  . ASN D 2 95  ? 29.435  -12.604 -48.924  1.00 66.14  ? 95  ASN D CA  1 
ATOM   7205  C C   . ASN D 2 95  ? 29.587  -11.118 -48.624  1.00 75.68  ? 95  ASN D C   1 
ATOM   7206  O O   . ASN D 2 95  ? 29.313  -10.277 -49.487  1.00 81.89  ? 95  ASN D O   1 
ATOM   7207  C CB  . ASN D 2 95  ? 28.092  -13.119 -48.405  1.00 66.01  ? 95  ASN D CB  1 
ATOM   7208  C CG  . ASN D 2 95  ? 27.690  -14.435 -49.040  1.00 82.33  ? 95  ASN D CG  1 
ATOM   7209  O OD1 . ASN D 2 95  ? 28.285  -14.870 -50.026  1.00 76.14  ? 95  ASN D OD1 1 
ATOM   7210  N ND2 . ASN D 2 95  ? 26.666  -15.072 -48.484  1.00 87.10  ? 95  ASN D ND2 1 
ATOM   7211  N N   . ALA D 2 96  ? 30.013  -10.772 -47.407  1.00 72.17  ? 96  ALA D N   1 
ATOM   7212  C CA  . ALA D 2 96  ? 30.123  -9.365  -47.036  1.00 76.00  ? 96  ALA D CA  1 
ATOM   7213  C C   . ALA D 2 96  ? 31.151  -8.640  -47.895  1.00 77.54  ? 96  ALA D C   1 
ATOM   7214  O O   . ALA D 2 96  ? 30.924  -7.501  -48.320  1.00 78.92  ? 96  ALA D O   1 
ATOM   7215  C CB  . ALA D 2 96  ? 30.481  -9.234  -45.557  1.00 68.75  ? 96  ALA D CB  1 
ATOM   7216  N N   . GLU D 2 97  ? 32.291  -9.280  -48.159  1.00 74.87  ? 97  GLU D N   1 
ATOM   7217  C CA  . GLU D 2 97  ? 33.343  -8.614  -48.920  1.00 79.67  ? 97  GLU D CA  1 
ATOM   7218  C C   . GLU D 2 97  ? 32.976  -8.492  -50.395  1.00 81.14  ? 97  GLU D C   1 
ATOM   7219  O O   . GLU D 2 97  ? 33.185  -7.436  -51.003  1.00 91.09  ? 97  GLU D O   1 
ATOM   7220  C CB  . GLU D 2 97  ? 34.668  -9.353  -48.741  1.00 85.11  ? 97  GLU D CB  1 
ATOM   7221  C CG  . GLU D 2 97  ? 35.187  -9.296  -47.313  1.00 79.75  ? 97  GLU D CG  1 
ATOM   7222  C CD  . GLU D 2 97  ? 36.689  -9.466  -47.218  1.00 104.44 ? 97  GLU D CD  1 
ATOM   7223  O OE1 . GLU D 2 97  ? 37.194  -10.557 -47.562  1.00 100.22 ? 97  GLU D OE1 1 
ATOM   7224  O OE2 . GLU D 2 97  ? 37.366  -8.503  -46.798  1.00 108.31 ? 97  GLU D OE2 1 
ATOM   7225  N N   . LEU D 2 98  ? 32.427  -9.555  -50.989  1.00 71.39  ? 98  LEU D N   1 
ATOM   7226  C CA  . LEU D 2 98  ? 32.040  -9.484  -52.395  1.00 73.26  ? 98  LEU D CA  1 
ATOM   7227  C C   . LEU D 2 98  ? 30.881  -8.515  -52.605  1.00 74.29  ? 98  LEU D C   1 
ATOM   7228  O O   . LEU D 2 98  ? 30.834  -7.808  -53.620  1.00 74.92  ? 98  LEU D O   1 
ATOM   7229  C CB  . LEU D 2 98  ? 31.687  -10.876 -52.918  1.00 45.99  ? 98  LEU D CB  1 
ATOM   7230  C CG  . LEU D 2 98  ? 32.854  -11.858 -53.066  1.00 60.11  ? 98  LEU D CG  1 
ATOM   7231  C CD1 . LEU D 2 98  ? 32.494  -12.970 -54.040  1.00 59.52  ? 98  LEU D CD1 1 
ATOM   7232  C CD2 . LEU D 2 98  ? 34.129  -11.145 -53.503  1.00 61.45  ? 98  LEU D CD2 1 
ATOM   7233  N N   . LEU D 2 99  ? 29.939  -8.469  -51.659  1.00 62.13  ? 99  LEU D N   1 
ATOM   7234  C CA  . LEU D 2 99  ? 28.833  -7.519  -51.756  1.00 66.64  ? 99  LEU D CA  1 
ATOM   7235  C C   . LEU D 2 99  ? 29.342  -6.085  -51.774  1.00 71.50  ? 99  LEU D C   1 
ATOM   7236  O O   . LEU D 2 99  ? 28.872  -5.258  -52.564  1.00 82.97  ? 99  LEU D O   1 
ATOM   7237  C CB  . LEU D 2 99  ? 27.861  -7.721  -50.595  1.00 69.29  ? 99  LEU D CB  1 
ATOM   7238  C CG  . LEU D 2 99  ? 26.928  -6.553  -50.262  1.00 70.70  ? 99  LEU D CG  1 
ATOM   7239  C CD1 . LEU D 2 99  ? 25.701  -6.546  -51.165  1.00 64.40  ? 99  LEU D CD1 1 
ATOM   7240  C CD2 . LEU D 2 99  ? 26.531  -6.585  -48.793  1.00 78.49  ? 99  LEU D CD2 1 
ATOM   7241  N N   . VAL D 2 100 ? 30.308  -5.772  -50.909  1.00 66.60  ? 100 VAL D N   1 
ATOM   7242  C CA  . VAL D 2 100 ? 30.893  -4.436  -50.898  1.00 65.28  ? 100 VAL D CA  1 
ATOM   7243  C C   . VAL D 2 100 ? 31.624  -4.160  -52.207  1.00 75.35  ? 100 VAL D C   1 
ATOM   7244  O O   . VAL D 2 100 ? 31.510  -3.068  -52.777  1.00 76.63  ? 100 VAL D O   1 
ATOM   7245  C CB  . VAL D 2 100 ? 31.817  -4.275  -49.677  1.00 61.36  ? 100 VAL D CB  1 
ATOM   7246  C CG1 . VAL D 2 100 ? 32.709  -3.058  -49.835  1.00 71.73  ? 100 VAL D CG1 1 
ATOM   7247  C CG2 . VAL D 2 100 ? 30.994  -4.169  -48.402  1.00 68.09  ? 100 VAL D CG2 1 
ATOM   7248  N N   . LEU D 2 101 ? 32.383  -5.138  -52.706  1.00 68.37  ? 101 LEU D N   1 
ATOM   7249  C CA  . LEU D 2 101 ? 33.105  -4.944  -53.960  1.00 68.82  ? 101 LEU D CA  1 
ATOM   7250  C C   . LEU D 2 101 ? 32.143  -4.718  -55.120  1.00 76.64  ? 101 LEU D C   1 
ATOM   7251  O O   . LEU D 2 101 ? 32.341  -3.814  -55.940  1.00 80.76  ? 101 LEU D O   1 
ATOM   7252  C CB  . LEU D 2 101 ? 34.004  -6.148  -54.243  1.00 68.31  ? 101 LEU D CB  1 
ATOM   7253  C CG  . LEU D 2 101 ? 35.165  -6.405  -53.282  1.00 65.34  ? 101 LEU D CG  1 
ATOM   7254  C CD1 . LEU D 2 101 ? 36.086  -7.487  -53.828  1.00 62.21  ? 101 LEU D CD1 1 
ATOM   7255  C CD2 . LEU D 2 101 ? 35.930  -5.124  -53.021  1.00 55.30  ? 101 LEU D CD2 1 
ATOM   7256  N N   . MET D 2 102 ? 31.092  -5.535  -55.203  1.00 79.45  ? 102 MET D N   1 
ATOM   7257  C CA  . MET D 2 102 ? 30.156  -5.437  -56.317  1.00 69.15  ? 102 MET D CA  1 
ATOM   7258  C C   . MET D 2 102 ? 29.336  -4.153  -56.250  1.00 67.03  ? 102 MET D C   1 
ATOM   7259  O O   . MET D 2 102 ? 29.096  -3.509  -57.279  1.00 79.44  ? 102 MET D O   1 
ATOM   7260  C CB  . MET D 2 102 ? 29.243  -6.663  -56.337  1.00 67.12  ? 102 MET D CB  1 
ATOM   7261  C CG  . MET D 2 102 ? 29.963  -7.960  -56.690  1.00 75.95  ? 102 MET D CG  1 
ATOM   7262  S SD  . MET D 2 102 ? 28.901  -9.414  -56.570  1.00 92.02  ? 102 MET D SD  1 
ATOM   7263  C CE  . MET D 2 102 ? 27.276  -8.660  -56.624  1.00 82.22  ? 102 MET D CE  1 
ATOM   7264  N N   . GLU D 2 103 ? 28.902  -3.759  -55.050  1.00 58.48  ? 103 GLU D N   1 
ATOM   7265  C CA  . GLU D 2 103 ? 28.078  -2.561  -54.923  1.00 72.59  ? 103 GLU D CA  1 
ATOM   7266  C C   . GLU D 2 103 ? 28.889  -1.280  -55.072  1.00 79.83  ? 103 GLU D C   1 
ATOM   7267  O O   . GLU D 2 103 ? 28.350  -0.266  -55.530  1.00 90.90  ? 103 GLU D O   1 
ATOM   7268  C CB  . GLU D 2 103 ? 27.339  -2.572  -53.584  1.00 69.20  ? 103 GLU D CB  1 
ATOM   7269  C CG  . GLU D 2 103 ? 26.183  -3.556  -53.550  1.00 89.54  ? 103 GLU D CG  1 
ATOM   7270  C CD  . GLU D 2 103 ? 25.263  -3.399  -54.745  1.00 97.00  ? 103 GLU D CD  1 
ATOM   7271  O OE1 . GLU D 2 103 ? 24.782  -2.272  -54.982  1.00 91.51  ? 103 GLU D OE1 1 
ATOM   7272  O OE2 . GLU D 2 103 ? 25.032  -4.398  -55.455  1.00 100.40 ? 103 GLU D OE2 1 
ATOM   7273  N N   . ASN D 2 104 ? 30.170  -1.295  -54.695  1.00 73.87  ? 104 ASN D N   1 
ATOM   7274  C CA  . ASN D 2 104 ? 31.013  -0.131  -54.948  1.00 68.53  ? 104 ASN D CA  1 
ATOM   7275  C C   . ASN D 2 104 ? 31.210  0.086   -56.441  1.00 81.80  ? 104 ASN D C   1 
ATOM   7276  O O   . ASN D 2 104 ? 31.227  1.230   -56.910  1.00 79.65  ? 104 ASN D O   1 
ATOM   7277  C CB  . ASN D 2 104 ? 32.363  -0.281  -54.246  1.00 77.18  ? 104 ASN D CB  1 
ATOM   7278  C CG  . ASN D 2 104 ? 32.306  0.114   -52.784  1.00 69.48  ? 104 ASN D CG  1 
ATOM   7279  O OD1 . ASN D 2 104 ? 31.362  0.770   -52.343  1.00 73.26  ? 104 ASN D OD1 1 
ATOM   7280  N ND2 . ASN D 2 104 ? 33.324  -0.277  -52.024  1.00 70.62  ? 104 ASN D ND2 1 
ATOM   7281  N N   . GLU D 2 105 ? 31.372  -0.999  -57.202  1.00 81.26  ? 105 GLU D N   1 
ATOM   7282  C CA  . GLU D 2 105 ? 31.471  -0.875  -58.652  1.00 67.25  ? 105 GLU D CA  1 
ATOM   7283  C C   . GLU D 2 105 ? 30.196  -0.284  -59.240  1.00 71.16  ? 105 GLU D C   1 
ATOM   7284  O O   . GLU D 2 105 ? 30.251  0.580   -60.123  1.00 72.78  ? 105 GLU D O   1 
ATOM   7285  C CB  . GLU D 2 105 ? 31.763  -2.240  -59.275  1.00 67.28  ? 105 GLU D CB  1 
ATOM   7286  C CG  . GLU D 2 105 ? 32.029  -2.196  -60.771  1.00 86.20  ? 105 GLU D CG  1 
ATOM   7287  C CD  . GLU D 2 105 ? 33.451  -1.788  -61.099  1.00 108.21 ? 105 GLU D CD  1 
ATOM   7288  O OE1 . GLU D 2 105 ? 34.379  -2.550  -60.755  1.00 106.60 ? 105 GLU D OE1 1 
ATOM   7289  O OE2 . GLU D 2 105 ? 33.640  -0.706  -61.693  1.00 104.23 ? 105 GLU D OE2 1 
ATOM   7290  N N   . ARG D 2 106 ? 29.035  -0.743  -58.764  1.00 79.92  ? 106 ARG D N   1 
ATOM   7291  C CA  . ARG D 2 106 ? 27.768  -0.204  -59.247  1.00 67.32  ? 106 ARG D CA  1 
ATOM   7292  C C   . ARG D 2 106 ? 27.605  1.265   -58.874  1.00 70.96  ? 106 ARG D C   1 
ATOM   7293  O O   . ARG D 2 106 ? 27.126  2.066   -59.684  1.00 87.80  ? 106 ARG D O   1 
ATOM   7294  C CB  . ARG D 2 106 ? 26.605  -1.025  -58.693  1.00 73.42  ? 106 ARG D CB  1 
ATOM   7295  C CG  . ARG D 2 106 ? 26.109  -2.109  -59.627  1.00 73.53  ? 106 ARG D CG  1 
ATOM   7296  C CD  . ARG D 2 106 ? 24.594  -2.081  -59.702  1.00 117.38 ? 106 ARG D CD  1 
ATOM   7297  N NE  . ARG D 2 106 ? 24.087  -2.745  -60.895  1.00 132.57 ? 106 ARG D NE  1 
ATOM   7298  C CZ  . ARG D 2 106 ? 23.009  -2.354  -61.560  1.00 111.93 ? 106 ARG D CZ  1 
ATOM   7299  N NH1 . ARG D 2 106 ? 22.317  -1.289  -61.188  1.00 103.84 ? 106 ARG D NH1 1 
ATOM   7300  N NH2 . ARG D 2 106 ? 22.621  -3.041  -62.630  1.00 98.00  ? 106 ARG D NH2 1 
ATOM   7301  N N   . THR D 2 107 ? 27.985  1.634   -57.648  1.00 78.81  ? 107 THR D N   1 
ATOM   7302  C CA  . THR D 2 107 ? 27.808  3.012   -57.203  1.00 79.15  ? 107 THR D CA  1 
ATOM   7303  C C   . THR D 2 107 ? 28.654  3.975   -58.027  1.00 87.38  ? 107 THR D C   1 
ATOM   7304  O O   . THR D 2 107 ? 28.195  5.066   -58.386  1.00 79.83  ? 107 THR D O   1 
ATOM   7305  C CB  . THR D 2 107 ? 28.149  3.136   -55.717  1.00 81.26  ? 107 THR D CB  1 
ATOM   7306  O OG1 . THR D 2 107 ? 27.437  2.136   -54.978  1.00 84.95  ? 107 THR D OG1 1 
ATOM   7307  C CG2 . THR D 2 107 ? 27.757  4.511   -55.197  1.00 66.80  ? 107 THR D CG2 1 
ATOM   7308  N N   . LEU D 2 108 ? 29.897  3.593   -58.333  1.00 85.55  ? 108 LEU D N   1 
ATOM   7309  C CA  . LEU D 2 108 ? 30.747  4.448   -59.155  1.00 82.11  ? 108 LEU D CA  1 
ATOM   7310  C C   . LEU D 2 108 ? 30.234  4.529   -60.589  1.00 85.03  ? 108 LEU D C   1 
ATOM   7311  O O   . LEU D 2 108 ? 30.227  5.610   -61.189  1.00 81.82  ? 108 LEU D O   1 
ATOM   7312  C CB  . LEU D 2 108 ? 32.190  3.947   -59.124  1.00 78.59  ? 108 LEU D CB  1 
ATOM   7313  C CG  . LEU D 2 108 ? 32.888  3.975   -57.762  1.00 73.59  ? 108 LEU D CG  1 
ATOM   7314  C CD1 . LEU D 2 108 ? 34.394  3.853   -57.932  1.00 68.07  ? 108 LEU D CD1 1 
ATOM   7315  C CD2 . LEU D 2 108 ? 32.530  5.237   -56.990  1.00 59.68  ? 108 LEU D CD2 1 
ATOM   7316  N N   . ASP D 2 109 ? 29.807  3.398   -61.158  1.00 89.12  ? 109 ASP D N   1 
ATOM   7317  C CA  . ASP D 2 109 ? 29.215  3.426   -62.493  1.00 71.07  ? 109 ASP D CA  1 
ATOM   7318  C C   . ASP D 2 109 ? 27.923  4.229   -62.510  1.00 73.74  ? 109 ASP D C   1 
ATOM   7319  O O   . ASP D 2 109 ? 27.601  4.867   -63.519  1.00 86.76  ? 109 ASP D O   1 
ATOM   7320  C CB  . ASP D 2 109 ? 28.957  2.003   -62.989  1.00 70.53  ? 109 ASP D CB  1 
ATOM   7321  C CG  . ASP D 2 109 ? 30.061  1.489   -63.890  1.00 99.02  ? 109 ASP D CG  1 
ATOM   7322  O OD1 . ASP D 2 109 ? 30.885  2.307   -64.350  1.00 112.68 ? 109 ASP D OD1 1 
ATOM   7323  O OD2 . ASP D 2 109 ? 30.101  0.265   -64.140  1.00 100.45 ? 109 ASP D OD2 1 
ATOM   7324  N N   . PHE D 2 110 ? 27.168  4.200   -61.410  1.00 75.10  ? 110 PHE D N   1 
ATOM   7325  C CA  . PHE D 2 110 ? 25.953  4.999   -61.311  1.00 70.64  ? 110 PHE D CA  1 
ATOM   7326  C C   . PHE D 2 110 ? 26.251  6.488   -61.427  1.00 80.51  ? 110 PHE D C   1 
ATOM   7327  O O   . PHE D 2 110 ? 25.428  7.248   -61.951  1.00 86.49  ? 110 PHE D O   1 
ATOM   7328  C CB  . PHE D 2 110 ? 25.241  4.684   -59.994  1.00 70.26  ? 110 PHE D CB  1 
ATOM   7329  C CG  . PHE D 2 110 ? 24.079  5.584   -59.691  1.00 68.72  ? 110 PHE D CG  1 
ATOM   7330  C CD1 . PHE D 2 110 ? 22.892  5.470   -60.395  1.00 64.84  ? 110 PHE D CD1 1 
ATOM   7331  C CD2 . PHE D 2 110 ? 24.166  6.529   -58.682  1.00 74.46  ? 110 PHE D CD2 1 
ATOM   7332  C CE1 . PHE D 2 110 ? 21.819  6.295   -60.109  1.00 61.72  ? 110 PHE D CE1 1 
ATOM   7333  C CE2 . PHE D 2 110 ? 23.097  7.355   -58.390  1.00 73.40  ? 110 PHE D CE2 1 
ATOM   7334  C CZ  . PHE D 2 110 ? 21.922  7.238   -59.104  1.00 76.20  ? 110 PHE D CZ  1 
ATOM   7335  N N   . HIS D 2 111 ? 27.421  6.924   -60.953  1.00 90.75  ? 111 HIS D N   1 
ATOM   7336  C CA  . HIS D 2 111 ? 27.785  8.334   -61.057  1.00 94.52  ? 111 HIS D CA  1 
ATOM   7337  C C   . HIS D 2 111 ? 28.160  8.713   -62.486  1.00 88.61  ? 111 HIS D C   1 
ATOM   7338  O O   . HIS D 2 111 ? 27.849  9.820   -62.939  1.00 88.69  ? 111 HIS D O   1 
ATOM   7339  C CB  . HIS D 2 111 ? 28.929  8.652   -60.094  1.00 91.20  ? 111 HIS D CB  1 
ATOM   7340  C CG  . HIS D 2 111 ? 28.496  8.776   -58.665  1.00 83.86  ? 111 HIS D CG  1 
ATOM   7341  N ND1 . HIS D 2 111 ? 27.338  9.424   -58.294  1.00 91.14  ? 111 HIS D ND1 1 
ATOM   7342  C CD2 . HIS D 2 111 ? 29.063  8.332   -57.518  1.00 85.73  ? 111 HIS D CD2 1 
ATOM   7343  C CE1 . HIS D 2 111 ? 27.211  9.377   -56.980  1.00 86.21  ? 111 HIS D CE1 1 
ATOM   7344  N NE2 . HIS D 2 111 ? 28.244  8.719   -56.485  1.00 86.93  ? 111 HIS D NE2 1 
ATOM   7345  N N   . ASP D 2 112 ? 28.839  7.815   -63.207  1.00 88.25  ? 112 ASP D N   1 
ATOM   7346  C CA  . ASP D 2 112 ? 29.210  8.109   -64.589  1.00 87.09  ? 112 ASP D CA  1 
ATOM   7347  C C   . ASP D 2 112 ? 27.977  8.287   -65.466  1.00 93.08  ? 112 ASP D C   1 
ATOM   7348  O O   . ASP D 2 112 ? 27.934  9.183   -66.317  1.00 99.79  ? 112 ASP D O   1 
ATOM   7349  C CB  . ASP D 2 112 ? 30.101  7.000   -65.150  1.00 85.86  ? 112 ASP D CB  1 
ATOM   7350  C CG  . ASP D 2 112 ? 31.398  6.843   -64.383  1.00 110.47 ? 112 ASP D CG  1 
ATOM   7351  O OD1 . ASP D 2 112 ? 32.106  5.836   -64.608  1.00 110.00 ? 112 ASP D OD1 1 
ATOM   7352  O OD2 . ASP D 2 112 ? 31.704  7.720   -63.547  1.00 120.18 ? 112 ASP D OD2 1 
ATOM   7353  N N   . SER D 2 113 ? 26.966  7.438   -65.271  1.00 94.22  ? 113 SER D N   1 
ATOM   7354  C CA  . SER D 2 113 ? 25.744  7.533   -66.063  1.00 86.59  ? 113 SER D CA  1 
ATOM   7355  C C   . SER D 2 113 ? 25.031  8.859   -65.832  1.00 88.98  ? 113 SER D C   1 
ATOM   7356  O O   . SER D 2 113 ? 24.495  9.456   -66.774  1.00 99.38  ? 113 SER D O   1 
ATOM   7357  C CB  . SER D 2 113 ? 24.816  6.365   -65.730  1.00 91.48  ? 113 SER D CB  1 
ATOM   7358  O OG  . SER D 2 113 ? 23.476  6.666   -66.079  1.00 115.75 ? 113 SER D OG  1 
ATOM   7359  N N   . ASN D 2 114 ? 25.000  9.328   -64.583  1.00 84.72  ? 114 ASN D N   1 
ATOM   7360  C CA  . ASN D 2 114 ? 24.327  10.588  -64.285  1.00 86.26  ? 114 ASN D CA  1 
ATOM   7361  C C   . ASN D 2 114 ? 25.016  11.762  -64.969  1.00 90.63  ? 114 ASN D C   1 
ATOM   7362  O O   . ASN D 2 114 ? 24.349  12.673  -65.475  1.00 90.07  ? 114 ASN D O   1 
ATOM   7363  C CB  . ASN D 2 114 ? 24.265  10.807  -62.773  1.00 81.31  ? 114 ASN D CB  1 
ATOM   7364  C CG  . ASN D 2 114 ? 23.356  9.812   -62.076  1.00 83.99  ? 114 ASN D CG  1 
ATOM   7365  O OD1 . ASN D 2 114 ? 22.598  9.088   -62.721  1.00 80.93  ? 114 ASN D OD1 1 
ATOM   7366  N ND2 . ASN D 2 114 ? 23.419  9.782   -60.749  1.00 96.84  ? 114 ASN D ND2 1 
ATOM   7367  N N   . VAL D 2 115 ? 26.351  11.767  -64.984  1.00 76.85  ? 115 VAL D N   1 
ATOM   7368  C CA  . VAL D 2 115 ? 27.084  12.852  -65.633  1.00 84.02  ? 115 VAL D CA  1 
ATOM   7369  C C   . VAL D 2 115 ? 26.805  12.863  -67.131  1.00 88.84  ? 115 VAL D C   1 
ATOM   7370  O O   . VAL D 2 115 ? 26.539  13.915  -67.724  1.00 85.49  ? 115 VAL D O   1 
ATOM   7371  C CB  . VAL D 2 115 ? 28.591  12.732  -65.342  1.00 89.76  ? 115 VAL D CB  1 
ATOM   7372  C CG1 . VAL D 2 115 ? 29.376  13.676  -66.235  1.00 82.23  ? 115 VAL D CG1 1 
ATOM   7373  C CG2 . VAL D 2 115 ? 28.877  13.029  -63.882  1.00 88.18  ? 115 VAL D CG2 1 
ATOM   7374  N N   . LYS D 2 116 ? 26.862  11.689  -67.766  1.00 82.12  ? 116 LYS D N   1 
ATOM   7375  C CA  . LYS D 2 116 ? 26.636  11.610  -69.206  1.00 79.18  ? 116 LYS D CA  1 
ATOM   7376  C C   . LYS D 2 116 ? 25.217  12.033  -69.569  1.00 87.44  ? 116 LYS D C   1 
ATOM   7377  O O   . LYS D 2 116 ? 25.004  12.721  -70.575  1.00 99.80  ? 116 LYS D O   1 
ATOM   7378  C CB  . LYS D 2 116 ? 26.922  10.193  -69.701  1.00 76.14  ? 116 LYS D CB  1 
ATOM   7379  C CG  . LYS D 2 116 ? 26.386  9.888   -71.086  1.00 103.91 ? 116 LYS D CG  1 
ATOM   7380  C CD  . LYS D 2 116 ? 26.857  8.524   -71.559  1.00 102.44 ? 116 LYS D CD  1 
ATOM   7381  C CE  . LYS D 2 116 ? 26.045  8.034   -72.745  1.00 95.33  ? 116 LYS D CE  1 
ATOM   7382  N NZ  . LYS D 2 116 ? 26.283  6.586   -72.999  1.00 103.95 ? 116 LYS D NZ  1 
ATOM   7383  N N   . ASN D 2 117 ? 24.233  11.634  -68.761  1.00 75.89  ? 117 ASN D N   1 
ATOM   7384  C CA  . ASN D 2 117 ? 22.850  11.999  -69.043  1.00 87.00  ? 117 ASN D CA  1 
ATOM   7385  C C   . ASN D 2 117 ? 22.640  13.505  -68.951  1.00 77.95  ? 117 ASN D C   1 
ATOM   7386  O O   . ASN D 2 117 ? 21.865  14.075  -69.728  1.00 82.95  ? 117 ASN D O   1 
ATOM   7387  C CB  . ASN D 2 117 ? 21.908  11.262  -68.090  1.00 90.12  ? 117 ASN D CB  1 
ATOM   7388  C CG  . ASN D 2 117 ? 21.810  9.781   -68.401  1.00 94.21  ? 117 ASN D CG  1 
ATOM   7389  O OD1 . ASN D 2 117 ? 22.397  9.301   -69.371  1.00 93.84  ? 117 ASN D OD1 1 
ATOM   7390  N ND2 . ASN D 2 117 ? 21.076  9.048   -67.573  1.00 99.26  ? 117 ASN D ND2 1 
ATOM   7391  N N   . LEU D 2 118 ? 23.309  14.167  -68.005  1.00 82.77  ? 118 LEU D N   1 
ATOM   7392  C CA  . LEU D 2 118 ? 23.190  15.618  -67.903  1.00 81.53  ? 118 LEU D CA  1 
ATOM   7393  C C   . LEU D 2 118 ? 23.801  16.310  -69.116  1.00 83.01  ? 118 LEU D C   1 
ATOM   7394  O O   . LEU D 2 118 ? 23.258  17.305  -69.611  1.00 87.79  ? 118 LEU D O   1 
ATOM   7395  C CB  . LEU D 2 118 ? 23.846  16.111  -66.615  1.00 73.95  ? 118 LEU D CB  1 
ATOM   7396  C CG  . LEU D 2 118 ? 23.519  17.552  -66.228  1.00 80.96  ? 118 LEU D CG  1 
ATOM   7397  C CD1 . LEU D 2 118 ? 22.017  17.766  -66.275  1.00 95.50  ? 118 LEU D CD1 1 
ATOM   7398  C CD2 . LEU D 2 118 ? 24.060  17.874  -64.845  1.00 90.35  ? 118 LEU D CD2 1 
ATOM   7399  N N   . TYR D 2 119 ? 24.936  15.803  -69.600  1.00 85.37  ? 119 TYR D N   1 
ATOM   7400  C CA  . TYR D 2 119 ? 25.542  16.350  -70.810  1.00 85.91  ? 119 TYR D CA  1 
ATOM   7401  C C   . TYR D 2 119 ? 24.642  16.139  -72.022  1.00 90.30  ? 119 TYR D C   1 
ATOM   7402  O O   . TYR D 2 119 ? 24.486  17.041  -72.853  1.00 90.63  ? 119 TYR D O   1 
ATOM   7403  C CB  . TYR D 2 119 ? 26.914  15.712  -71.033  1.00 80.16  ? 119 TYR D CB  1 
ATOM   7404  C CG  . TYR D 2 119 ? 27.639  16.167  -72.282  1.00 73.13  ? 119 TYR D CG  1 
ATOM   7405  C CD1 . TYR D 2 119 ? 28.386  17.337  -72.290  1.00 83.31  ? 119 TYR D CD1 1 
ATOM   7406  C CD2 . TYR D 2 119 ? 27.597  15.411  -73.448  1.00 80.04  ? 119 TYR D CD2 1 
ATOM   7407  C CE1 . TYR D 2 119 ? 29.058  17.749  -73.426  1.00 76.37  ? 119 TYR D CE1 1 
ATOM   7408  C CE2 . TYR D 2 119 ? 28.265  15.816  -74.589  1.00 65.64  ? 119 TYR D CE2 1 
ATOM   7409  C CZ  . TYR D 2 119 ? 28.993  16.986  -74.572  1.00 72.61  ? 119 TYR D CZ  1 
ATOM   7410  O OH  . TYR D 2 119 ? 29.661  17.397  -75.703  1.00 91.11  ? 119 TYR D OH  1 
ATOM   7411  N N   . ASP D 2 120 ? 24.040  14.952  -72.138  1.00 89.31  ? 120 ASP D N   1 
ATOM   7412  C CA  . ASP D 2 120 ? 23.178  14.669  -73.282  1.00 84.85  ? 120 ASP D CA  1 
ATOM   7413  C C   . ASP D 2 120 ? 21.884  15.474  -73.229  1.00 90.86  ? 120 ASP D C   1 
ATOM   7414  O O   . ASP D 2 120 ? 21.318  15.800  -74.279  1.00 89.92  ? 120 ASP D O   1 
ATOM   7415  C CB  . ASP D 2 120 ? 22.877  13.172  -73.353  1.00 76.40  ? 120 ASP D CB  1 
ATOM   7416  C CG  . ASP D 2 120 ? 24.126  12.336  -73.565  1.00 98.69  ? 120 ASP D CG  1 
ATOM   7417  O OD1 . ASP D 2 120 ? 25.217  12.923  -73.732  1.00 103.83 ? 120 ASP D OD1 1 
ATOM   7418  O OD2 . ASP D 2 120 ? 24.019  11.092  -73.567  1.00 98.22  ? 120 ASP D OD2 1 
ATOM   7419  N N   . LYS D 2 121 ? 21.395  15.788  -72.027  1.00 85.01  ? 121 LYS D N   1 
ATOM   7420  C CA  . LYS D 2 121 ? 20.208  16.628  -71.908  1.00 79.93  ? 121 LYS D CA  1 
ATOM   7421  C C   . LYS D 2 121 ? 20.466  18.020  -72.475  1.00 95.00  ? 121 LYS D C   1 
ATOM   7422  O O   . LYS D 2 121 ? 19.639  18.566  -73.216  1.00 91.81  ? 121 LYS D O   1 
ATOM   7423  C CB  . LYS D 2 121 ? 19.772  16.694  -70.441  1.00 85.04  ? 121 LYS D CB  1 
ATOM   7424  C CG  . LYS D 2 121 ? 18.609  17.637  -70.137  1.00 90.44  ? 121 LYS D CG  1 
ATOM   7425  C CD  . LYS D 2 121 ? 19.108  19.022  -69.743  1.00 112.15 ? 121 LYS D CD  1 
ATOM   7426  C CE  . LYS D 2 121 ? 18.300  19.607  -68.600  1.00 115.29 ? 121 LYS D CE  1 
ATOM   7427  N NZ  . LYS D 2 121 ? 18.851  20.919  -68.158  1.00 100.93 ? 121 LYS D NZ  1 
ATOM   7428  N N   . VAL D 2 122 ? 21.614  18.611  -72.135  1.00 93.78  ? 122 VAL D N   1 
ATOM   7429  C CA  . VAL D 2 122 ? 21.953  19.937  -72.642  1.00 91.81  ? 122 VAL D CA  1 
ATOM   7430  C C   . VAL D 2 122 ? 22.227  19.883  -74.141  1.00 77.47  ? 122 VAL D C   1 
ATOM   7431  O O   . VAL D 2 122 ? 21.862  20.801  -74.887  1.00 76.92  ? 122 VAL D O   1 
ATOM   7432  C CB  . VAL D 2 122 ? 23.147  20.512  -71.858  1.00 81.53  ? 122 VAL D CB  1 
ATOM   7433  C CG1 . VAL D 2 122 ? 23.715  21.732  -72.559  1.00 77.83  ? 122 VAL D CG1 1 
ATOM   7434  C CG2 . VAL D 2 122 ? 22.721  20.865  -70.442  1.00 75.49  ? 122 VAL D CG2 1 
ATOM   7435  N N   . ARG D 2 123 ? 22.859  18.800  -74.605  1.00 76.39  ? 123 ARG D N   1 
ATOM   7436  C CA  . ARG D 2 123 ? 23.164  18.663  -76.025  1.00 71.76  ? 123 ARG D CA  1 
ATOM   7437  C C   . ARG D 2 123 ? 21.895  18.668  -76.864  1.00 85.70  ? 123 ARG D C   1 
ATOM   7438  O O   . ARG D 2 123 ? 21.844  19.306  -77.922  1.00 71.95  ? 123 ARG D O   1 
ATOM   7439  C CB  . ARG D 2 123 ? 23.957  17.378  -76.279  1.00 80.53  ? 123 ARG D CB  1 
ATOM   7440  C CG  . ARG D 2 123 ? 24.328  17.175  -77.740  1.00 93.50  ? 123 ARG D CG  1 
ATOM   7441  C CD  . ARG D 2 123 ? 24.892  15.786  -78.018  1.00 90.07  ? 123 ARG D CD  1 
ATOM   7442  N NE  . ARG D 2 123 ? 23.990  14.698  -77.650  1.00 110.28 ? 123 ARG D NE  1 
ATOM   7443  C CZ  . ARG D 2 123 ? 22.906  14.345  -78.329  1.00 112.69 ? 123 ARG D CZ  1 
ATOM   7444  N NH1 . ARG D 2 123 ? 22.482  15.044  -79.368  1.00 100.65 ? 123 ARG D NH1 1 
ATOM   7445  N NH2 . ARG D 2 123 ? 22.229  13.263  -77.953  1.00 110.57 ? 123 ARG D NH2 1 
ATOM   7446  N N   . LEU D 2 124 ? 20.860  17.958  -76.409  1.00 94.94  ? 124 LEU D N   1 
ATOM   7447  C CA  . LEU D 2 124 ? 19.583  17.965  -77.115  1.00 87.85  ? 124 LEU D CA  1 
ATOM   7448  C C   . LEU D 2 124 ? 18.951  19.351  -77.109  1.00 75.84  ? 124 LEU D C   1 
ATOM   7449  O O   . LEU D 2 124 ? 18.353  19.773  -78.106  1.00 94.81  ? 124 LEU D O   1 
ATOM   7450  C CB  . LEU D 2 124 ? 18.634  16.942  -76.491  1.00 92.25  ? 124 LEU D CB  1 
ATOM   7451  C CG  . LEU D 2 124 ? 18.746  15.502  -76.991  1.00 105.02 ? 124 LEU D CG  1 
ATOM   7452  C CD1 . LEU D 2 124 ? 17.920  14.566  -76.123  1.00 103.34 ? 124 LEU D CD1 1 
ATOM   7453  C CD2 . LEU D 2 124 ? 18.294  15.423  -78.437  1.00 97.60  ? 124 LEU D CD2 1 
ATOM   7454  N N   . GLN D 2 125 ? 19.067  20.072  -75.992  1.00 80.28  ? 125 GLN D N   1 
ATOM   7455  C CA  . GLN D 2 125 ? 18.446  21.388  -75.891  1.00 82.64  ? 125 GLN D CA  1 
ATOM   7456  C C   . GLN D 2 125 ? 19.079  22.382  -76.859  1.00 92.23  ? 125 GLN D C   1 
ATOM   7457  O O   . GLN D 2 125 ? 18.373  23.103  -77.570  1.00 87.23  ? 125 GLN D O   1 
ATOM   7458  C CB  . GLN D 2 125 ? 18.542  21.907  -74.457  1.00 81.88  ? 125 GLN D CB  1 
ATOM   7459  C CG  . GLN D 2 125 ? 17.231  21.860  -73.693  1.00 84.37  ? 125 GLN D CG  1 
ATOM   7460  C CD  . GLN D 2 125 ? 17.202  22.836  -72.532  1.00 100.71 ? 125 GLN D CD  1 
ATOM   7461  O OE1 . GLN D 2 125 ? 18.100  22.842  -71.691  1.00 84.63  ? 125 GLN D OE1 1 
ATOM   7462  N NE2 . GLN D 2 125 ? 16.172  23.676  -72.489  1.00 89.63  ? 125 GLN D NE2 1 
ATOM   7463  N N   . LEU D 2 126 ? 20.410  22.447  -76.890  1.00 85.18  ? 126 LEU D N   1 
ATOM   7464  C CA  . LEU D 2 126 ? 21.070  23.466  -77.701  1.00 80.82  ? 126 LEU D CA  1 
ATOM   7465  C C   . LEU D 2 126 ? 21.017  23.120  -79.183  1.00 83.46  ? 126 LEU D C   1 
ATOM   7466  O O   . LEU D 2 126 ? 20.831  24.008  -80.026  1.00 94.94  ? 126 LEU D O   1 
ATOM   7467  C CB  . LEU D 2 126 ? 22.516  23.656  -77.242  1.00 71.01  ? 126 LEU D CB  1 
ATOM   7468  C CG  . LEU D 2 126 ? 22.695  24.145  -75.801  1.00 75.49  ? 126 LEU D CG  1 
ATOM   7469  C CD1 . LEU D 2 126 ? 24.132  24.576  -75.555  1.00 72.37  ? 126 LEU D CD1 1 
ATOM   7470  C CD2 . LEU D 2 126 ? 21.728  25.276  -75.490  1.00 84.27  ? 126 LEU D CD2 1 
ATOM   7471  N N   . ARG D 2 127 ? 21.181  21.842  -79.519  1.00 85.25  ? 127 ARG D N   1 
ATOM   7472  C CA  . ARG D 2 127 ? 21.227  21.363  -80.907  1.00 88.91  ? 127 ARG D CA  1 
ATOM   7473  C C   . ARG D 2 127 ? 22.376  22.088  -81.605  1.00 80.04  ? 127 ARG D C   1 
ATOM   7474  O O   . ARG D 2 127 ? 23.504  22.075  -81.085  1.00 86.15  ? 127 ARG D O   1 
ATOM   7475  C CB  . ARG D 2 127 ? 19.860  21.519  -81.562  1.00 96.04  ? 127 ARG D CB  1 
ATOM   7476  C CG  . ARG D 2 127 ? 19.033  20.253  -81.597  1.00 97.37  ? 127 ARG D CG  1 
ATOM   7477  C CD  . ARG D 2 127 ? 17.771  20.476  -82.407  1.00 111.12 ? 127 ARG D CD  1 
ATOM   7478  N NE  . ARG D 2 127 ? 16.868  21.406  -81.740  1.00 101.28 ? 127 ARG D NE  1 
ATOM   7479  C CZ  . ARG D 2 127 ? 15.997  22.186  -82.368  1.00 105.31 ? 127 ARG D CZ  1 
ATOM   7480  N NH1 . ARG D 2 127 ? 15.914  22.208  -83.689  1.00 100.97 ? 127 ARG D NH1 1 
ATOM   7481  N NH2 . ARG D 2 127 ? 15.196  22.971  -81.653  1.00 112.48 ? 127 ARG D NH2 1 
ATOM   7482  N N   . ASP D 2 128 ? 22.148  22.725  -82.748  1.00 91.94  ? 128 ASP D N   1 
ATOM   7483  C CA  . ASP D 2 128 ? 23.208  23.372  -83.505  1.00 81.45  ? 128 ASP D CA  1 
ATOM   7484  C C   . ASP D 2 128 ? 23.393  24.839  -83.140  1.00 79.09  ? 128 ASP D C   1 
ATOM   7485  O O   . ASP D 2 128 ? 24.214  25.517  -83.765  1.00 94.99  ? 128 ASP D O   1 
ATOM   7486  C CB  . ASP D 2 128 ? 22.935  23.220  -85.009  1.00 80.50  ? 128 ASP D CB  1 
ATOM   7487  C CG  . ASP D 2 128 ? 21.538  23.665  -85.399  1.00 103.61 ? 128 ASP D CG  1 
ATOM   7488  O OD1 . ASP D 2 128 ? 21.194  23.570  -86.596  1.00 109.58 ? 128 ASP D OD1 1 
ATOM   7489  O OD2 . ASP D 2 128 ? 20.791  24.127  -84.514  1.00 107.60 ? 128 ASP D OD2 1 
ATOM   7490  N N   . ASN D 2 129 ? 22.662  25.341  -82.142  1.00 82.82  ? 129 ASN D N   1 
ATOM   7491  C CA  . ASN D 2 129 ? 22.883  26.696  -81.651  1.00 89.00  ? 129 ASN D CA  1 
ATOM   7492  C C   . ASN D 2 129 ? 24.232  26.862  -80.964  1.00 91.64  ? 129 ASN D C   1 
ATOM   7493  O O   . ASN D 2 129 ? 24.650  28.002  -80.730  1.00 93.37  ? 129 ASN D O   1 
ATOM   7494  C CB  . ASN D 2 129 ? 21.765  27.097  -80.687  1.00 93.95  ? 129 ASN D CB  1 
ATOM   7495  C CG  . ASN D 2 129 ? 20.603  27.765  -81.391  1.00 94.51  ? 129 ASN D CG  1 
ATOM   7496  O OD1 . ASN D 2 129 ? 20.525  27.759  -82.619  1.00 87.90  ? 129 ASN D OD1 1 
ATOM   7497  N ND2 . ASN D 2 129 ? 19.694  28.350  -80.618  1.00 96.76  ? 129 ASN D ND2 1 
ATOM   7498  N N   . ALA D 2 130 ? 24.915  25.767  -80.633  1.00 85.65  ? 130 ALA D N   1 
ATOM   7499  C CA  . ALA D 2 130 ? 26.217  25.819  -79.988  1.00 81.42  ? 130 ALA D CA  1 
ATOM   7500  C C   . ALA D 2 130 ? 27.124  24.775  -80.626  1.00 90.02  ? 130 ALA D C   1 
ATOM   7501  O O   . ALA D 2 130 ? 26.713  24.015  -81.507  1.00 80.34  ? 130 ALA D O   1 
ATOM   7502  C CB  . ALA D 2 130 ? 26.095  25.610  -78.473  1.00 88.03  ? 130 ALA D CB  1 
ATOM   7503  N N   . LYS D 2 131 ? 28.373  24.742  -80.172  1.00 92.02  ? 131 LYS D N   1 
ATOM   7504  C CA  . LYS D 2 131 ? 29.401  23.871  -80.725  1.00 82.85  ? 131 LYS D CA  1 
ATOM   7505  C C   . LYS D 2 131 ? 29.892  22.920  -79.642  1.00 94.48  ? 131 LYS D C   1 
ATOM   7506  O O   . LYS D 2 131 ? 30.159  23.344  -78.512  1.00 93.53  ? 131 LYS D O   1 
ATOM   7507  C CB  . LYS D 2 131 ? 30.565  24.700  -81.274  1.00 89.12  ? 131 LYS D CB  1 
ATOM   7508  C CG  . LYS D 2 131 ? 31.401  24.022  -82.344  1.00 104.52 ? 131 LYS D CG  1 
ATOM   7509  C CD  . LYS D 2 131 ? 32.680  24.813  -82.591  1.00 115.61 ? 131 LYS D CD  1 
ATOM   7510  C CE  . LYS D 2 131 ? 32.398  26.306  -82.657  1.00 110.36 ? 131 LYS D CE  1 
ATOM   7511  N NZ  . LYS D 2 131 ? 33.647  27.109  -82.588  1.00 96.89  ? 131 LYS D NZ  1 
ATOM   7512  N N   . GLU D 2 132 ? 30.013  21.640  -79.983  1.00 90.19  ? 132 GLU D N   1 
ATOM   7513  C CA  . GLU D 2 132 ? 30.552  20.655  -79.053  1.00 95.30  ? 132 GLU D CA  1 
ATOM   7514  C C   . GLU D 2 132 ? 32.073  20.725  -79.071  1.00 105.68 ? 132 GLU D C   1 
ATOM   7515  O O   . GLU D 2 132 ? 32.700  20.472  -80.106  1.00 103.44 ? 132 GLU D O   1 
ATOM   7516  C CB  . GLU D 2 132 ? 30.074  19.249  -79.411  1.00 95.52  ? 132 GLU D CB  1 
ATOM   7517  C CG  . GLU D 2 132 ? 28.860  18.785  -78.625  1.00 102.76 ? 132 GLU D CG  1 
ATOM   7518  C CD  . GLU D 2 132 ? 28.631  17.289  -78.732  1.00 109.19 ? 132 GLU D CD  1 
ATOM   7519  O OE1 . GLU D 2 132 ? 28.421  16.797  -79.861  1.00 107.38 ? 132 GLU D OE1 1 
ATOM   7520  O OE2 . GLU D 2 132 ? 28.668  16.606  -77.686  1.00 99.89  ? 132 GLU D OE2 1 
ATOM   7521  N N   . LEU D 2 133 ? 32.667  21.066  -77.926  1.00 98.33  ? 133 LEU D N   1 
ATOM   7522  C CA  . LEU D 2 133 ? 34.108  21.266  -77.849  1.00 86.65  ? 133 LEU D CA  1 
ATOM   7523  C C   . LEU D 2 133 ? 34.886  19.989  -77.568  1.00 95.97  ? 133 LEU D C   1 
ATOM   7524  O O   . LEU D 2 133 ? 36.107  19.971  -77.762  1.00 100.50 ? 133 LEU D O   1 
ATOM   7525  C CB  . LEU D 2 133 ? 34.441  22.304  -76.773  1.00 90.05  ? 133 LEU D CB  1 
ATOM   7526  C CG  . LEU D 2 133 ? 33.884  23.712  -76.997  1.00 94.65  ? 133 LEU D CG  1 
ATOM   7527  C CD1 . LEU D 2 133 ? 34.637  24.719  -76.143  1.00 96.81  ? 133 LEU D CD1 1 
ATOM   7528  C CD2 . LEU D 2 133 ? 33.942  24.097  -78.469  1.00 84.43  ? 133 LEU D CD2 1 
ATOM   7529  N N   . GLY D 2 134 ? 34.220  18.927  -77.121  1.00 101.91 ? 134 GLY D N   1 
ATOM   7530  C CA  . GLY D 2 134 ? 34.875  17.662  -76.872  1.00 96.35  ? 134 GLY D CA  1 
ATOM   7531  C C   . GLY D 2 134 ? 35.394  17.460  -75.465  1.00 97.10  ? 134 GLY D C   1 
ATOM   7532  O O   . GLY D 2 134 ? 35.768  16.331  -75.120  1.00 91.52  ? 134 GLY D O   1 
ATOM   7533  N N   . ASN D 2 135 ? 35.433  18.505  -74.640  1.00 83.03  ? 135 ASN D N   1 
ATOM   7534  C CA  . ASN D 2 135 ? 35.844  18.379  -73.248  1.00 96.05  ? 135 ASN D CA  1 
ATOM   7535  C C   . ASN D 2 135 ? 34.665  18.299  -72.288  1.00 100.49 ? 135 ASN D C   1 
ATOM   7536  O O   . ASN D 2 135 ? 34.874  18.260  -71.072  1.00 108.50 ? 135 ASN D O   1 
ATOM   7537  C CB  . ASN D 2 135 ? 36.758  19.548  -72.854  1.00 92.03  ? 135 ASN D CB  1 
ATOM   7538  C CG  . ASN D 2 135 ? 36.075  20.904  -72.971  1.00 108.47 ? 135 ASN D CG  1 
ATOM   7539  O OD1 . ASN D 2 135 ? 34.851  21.002  -73.046  1.00 114.13 ? 135 ASN D OD1 1 
ATOM   7540  N ND2 . ASN D 2 135 ? 36.877  21.962  -72.984  1.00 107.87 ? 135 ASN D ND2 1 
ATOM   7541  N N   . GLY D 2 136 ? 33.440  18.269  -72.801  1.00 97.19  ? 136 GLY D N   1 
ATOM   7542  C CA  . GLY D 2 136 ? 32.258  18.363  -71.977  1.00 86.79  ? 136 GLY D CA  1 
ATOM   7543  C C   . GLY D 2 136 ? 31.625  19.735  -71.918  1.00 93.36  ? 136 GLY D C   1 
ATOM   7544  O O   . GLY D 2 136 ? 30.687  19.929  -71.136  1.00 95.16  ? 136 GLY D O   1 
ATOM   7545  N N   . CYS D 2 137 ? 32.105  20.690  -72.712  1.00 99.97  ? 137 CYS D N   1 
ATOM   7546  C CA  . CYS D 2 137 ? 31.565  22.039  -72.746  1.00 99.37  ? 137 CYS D CA  1 
ATOM   7547  C C   . CYS D 2 137 ? 30.994  22.340  -74.125  1.00 95.70  ? 137 CYS D C   1 
ATOM   7548  O O   . CYS D 2 137 ? 31.447  21.795  -75.136  1.00 87.62  ? 137 CYS D O   1 
ATOM   7549  C CB  . CYS D 2 137 ? 32.631  23.094  -72.408  1.00 95.35  ? 137 CYS D CB  1 
ATOM   7550  S SG  . CYS D 2 137 ? 33.476  22.895  -70.825  1.00 133.46 ? 137 CYS D SG  1 
ATOM   7551  N N   . PHE D 2 138 ? 29.993  23.215  -74.154  1.00 90.33  ? 138 PHE D N   1 
ATOM   7552  C CA  . PHE D 2 138 ? 29.420  23.728  -75.389  1.00 85.36  ? 138 PHE D CA  1 
ATOM   7553  C C   . PHE D 2 138 ? 29.767  25.204  -75.517  1.00 92.83  ? 138 PHE D C   1 
ATOM   7554  O O   . PHE D 2 138 ? 29.627  25.961  -74.552  1.00 89.19  ? 138 PHE D O   1 
ATOM   7555  C CB  . PHE D 2 138 ? 27.899  23.552  -75.413  1.00 75.22  ? 138 PHE D CB  1 
ATOM   7556  C CG  . PHE D 2 138 ? 27.440  22.139  -75.199  1.00 79.80  ? 138 PHE D CG  1 
ATOM   7557  C CD1 . PHE D 2 138 ? 27.198  21.661  -73.922  1.00 78.47  ? 138 PHE D CD1 1 
ATOM   7558  C CD2 . PHE D 2 138 ? 27.233  21.293  -76.276  1.00 82.49  ? 138 PHE D CD2 1 
ATOM   7559  C CE1 . PHE D 2 138 ? 26.768  20.363  -73.722  1.00 74.88  ? 138 PHE D CE1 1 
ATOM   7560  C CE2 . PHE D 2 138 ? 26.802  19.995  -76.082  1.00 86.78  ? 138 PHE D CE2 1 
ATOM   7561  C CZ  . PHE D 2 138 ? 26.569  19.530  -74.804  1.00 81.52  ? 138 PHE D CZ  1 
ATOM   7562  N N   . GLU D 2 139 ? 30.215  25.612  -76.701  1.00 90.97  ? 139 GLU D N   1 
ATOM   7563  C CA  . GLU D 2 139 ? 30.449  27.019  -77.000  1.00 88.92  ? 139 GLU D CA  1 
ATOM   7564  C C   . GLU D 2 139 ? 29.320  27.532  -77.883  1.00 93.47  ? 139 GLU D C   1 
ATOM   7565  O O   . GLU D 2 139 ? 29.059  26.970  -78.952  1.00 92.80  ? 139 GLU D O   1 
ATOM   7566  C CB  . GLU D 2 139 ? 31.795  27.229  -77.692  1.00 97.61  ? 139 GLU D CB  1 
ATOM   7567  C CG  . GLU D 2 139 ? 32.082  28.689  -78.006  1.00 98.79  ? 139 GLU D CG  1 
ATOM   7568  C CD  . GLU D 2 139 ? 33.212  28.868  -78.998  1.00 117.14 ? 139 GLU D CD  1 
ATOM   7569  O OE1 . GLU D 2 139 ? 34.387  28.725  -78.600  1.00 119.09 ? 139 GLU D OE1 1 
ATOM   7570  O OE2 . GLU D 2 139 ? 32.922  29.149  -80.180  1.00 121.39 ? 139 GLU D OE2 1 
ATOM   7571  N N   . PHE D 2 140 ? 28.666  28.601  -77.439  1.00 90.99  ? 140 PHE D N   1 
ATOM   7572  C CA  . PHE D 2 140 ? 27.490  29.104  -78.135  1.00 92.93  ? 140 PHE D CA  1 
ATOM   7573  C C   . PHE D 2 140 ? 27.872  29.817  -79.426  1.00 96.14  ? 140 PHE D C   1 
ATOM   7574  O O   . PHE D 2 140 ? 28.890  30.512  -79.497  1.00 94.08  ? 140 PHE D O   1 
ATOM   7575  C CB  . PHE D 2 140 ? 26.705  30.055  -77.231  1.00 92.27  ? 140 PHE D CB  1 
ATOM   7576  C CG  . PHE D 2 140 ? 26.092  29.387  -76.035  1.00 95.26  ? 140 PHE D CG  1 
ATOM   7577  C CD1 . PHE D 2 140 ? 26.738  29.399  -74.811  1.00 95.29  ? 140 PHE D CD1 1 
ATOM   7578  C CD2 . PHE D 2 140 ? 24.867  28.749  -76.136  1.00 84.68  ? 140 PHE D CD2 1 
ATOM   7579  C CE1 . PHE D 2 140 ? 26.174  28.787  -73.709  1.00 90.02  ? 140 PHE D CE1 1 
ATOM   7580  C CE2 . PHE D 2 140 ? 24.298  28.134  -75.038  1.00 86.05  ? 140 PHE D CE2 1 
ATOM   7581  C CZ  . PHE D 2 140 ? 24.952  28.153  -73.823  1.00 90.57  ? 140 PHE D CZ  1 
ATOM   7582  N N   . TYR D 2 141 ? 27.039  29.642  -80.451  1.00 94.51  ? 141 TYR D N   1 
ATOM   7583  C CA  . TYR D 2 141 ? 27.142  30.419  -81.679  1.00 92.74  ? 141 TYR D CA  1 
ATOM   7584  C C   . TYR D 2 141 ? 26.456  31.773  -81.570  1.00 99.34  ? 141 TYR D C   1 
ATOM   7585  O O   . TYR D 2 141 ? 26.466  32.535  -82.541  1.00 116.18 ? 141 TYR D O   1 
ATOM   7586  C CB  . TYR D 2 141 ? 26.545  29.643  -82.857  1.00 88.23  ? 141 TYR D CB  1 
ATOM   7587  C CG  . TYR D 2 141 ? 27.425  28.537  -83.395  1.00 88.85  ? 141 TYR D CG  1 
ATOM   7588  C CD1 . TYR D 2 141 ? 28.648  28.823  -83.985  1.00 97.75  ? 141 TYR D CD1 1 
ATOM   7589  C CD2 . TYR D 2 141 ? 27.021  27.209  -83.333  1.00 87.89  ? 141 TYR D CD2 1 
ATOM   7590  C CE1 . TYR D 2 141 ? 29.453  27.817  -84.486  1.00 98.58  ? 141 TYR D CE1 1 
ATOM   7591  C CE2 . TYR D 2 141 ? 27.819  26.196  -83.832  1.00 91.21  ? 141 TYR D CE2 1 
ATOM   7592  C CZ  . TYR D 2 141 ? 29.033  26.506  -84.408  1.00 91.19  ? 141 TYR D CZ  1 
ATOM   7593  O OH  . TYR D 2 141 ? 29.832  25.504  -84.907  1.00 97.24  ? 141 TYR D OH  1 
ATOM   7594  N N   . HIS D 2 142 ? 25.853  32.079  -80.424  1.00 84.05  ? 142 HIS D N   1 
ATOM   7595  C CA  . HIS D 2 142 ? 25.141  33.330  -80.217  1.00 87.00  ? 142 HIS D CA  1 
ATOM   7596  C C   . HIS D 2 142 ? 25.455  33.850  -78.822  1.00 92.43  ? 142 HIS D C   1 
ATOM   7597  O O   . HIS D 2 142 ? 26.000  33.133  -77.978  1.00 101.87 ? 142 HIS D O   1 
ATOM   7598  C CB  . HIS D 2 142 ? 23.629  33.146  -80.399  1.00 102.08 ? 142 HIS D CB  1 
ATOM   7599  C CG  . HIS D 2 142 ? 23.018  32.180  -79.432  1.00 99.40  ? 142 HIS D CG  1 
ATOM   7600  N ND1 . HIS D 2 142 ? 22.665  32.536  -78.149  1.00 89.35  ? 142 HIS D ND1 1 
ATOM   7601  C CD2 . HIS D 2 142 ? 22.702  30.869  -79.559  1.00 89.35  ? 142 HIS D CD2 1 
ATOM   7602  C CE1 . HIS D 2 142 ? 22.154  31.487  -77.528  1.00 96.88  ? 142 HIS D CE1 1 
ATOM   7603  N NE2 . HIS D 2 142 ? 22.165  30.463  -78.362  1.00 92.68  ? 142 HIS D NE2 1 
ATOM   7604  N N   . LYS D 2 143 ? 25.114  35.115  -78.584  1.00 96.42  ? 143 LYS D N   1 
ATOM   7605  C CA  . LYS D 2 143 ? 25.272  35.693  -77.256  1.00 94.78  ? 143 LYS D CA  1 
ATOM   7606  C C   . LYS D 2 143 ? 24.293  35.034  -76.293  1.00 109.04 ? 143 LYS D C   1 
ATOM   7607  O O   . LYS D 2 143 ? 23.081  35.035  -76.530  1.00 101.89 ? 143 LYS D O   1 
ATOM   7608  C CB  . LYS D 2 143 ? 25.047  37.202  -77.293  1.00 88.96  ? 143 LYS D CB  1 
ATOM   7609  C CG  . LYS D 2 143 ? 26.266  38.009  -77.697  1.00 95.76  ? 143 LYS D CG  1 
ATOM   7610  C CD  . LYS D 2 143 ? 26.192  39.418  -77.127  1.00 113.41 ? 143 LYS D CD  1 
ATOM   7611  C CE  . LYS D 2 143 ? 27.447  40.215  -77.445  1.00 112.54 ? 143 LYS D CE  1 
ATOM   7612  N NZ  . LYS D 2 143 ? 27.444  41.540  -76.763  1.00 96.00  ? 143 LYS D NZ  1 
ATOM   7613  N N   . CYS D 2 144 ? 24.818  34.472  -75.208  1.00 103.05 ? 144 CYS D N   1 
ATOM   7614  C CA  . CYS D 2 144 ? 24.010  33.792  -74.202  1.00 108.82 ? 144 CYS D CA  1 
ATOM   7615  C C   . CYS D 2 144 ? 24.306  34.436  -72.854  1.00 106.23 ? 144 CYS D C   1 
ATOM   7616  O O   . CYS D 2 144 ? 25.373  34.213  -72.273  1.00 96.28  ? 144 CYS D O   1 
ATOM   7617  C CB  . CYS D 2 144 ? 24.302  32.292  -74.197  1.00 97.34  ? 144 CYS D CB  1 
ATOM   7618  S SG  . CYS D 2 144 ? 23.124  31.249  -73.292  1.00 142.14 ? 144 CYS D SG  1 
ATOM   7619  N N   . ASP D 2 145 ? 23.364  35.243  -72.370  1.00 110.88 ? 145 ASP D N   1 
ATOM   7620  C CA  . ASP D 2 145 ? 23.516  35.985  -71.129  1.00 101.53 ? 145 ASP D CA  1 
ATOM   7621  C C   . ASP D 2 145 ? 23.199  35.090  -69.932  1.00 105.07 ? 145 ASP D C   1 
ATOM   7622  O O   . ASP D 2 145 ? 22.924  33.896  -70.069  1.00 105.74 ? 145 ASP D O   1 
ATOM   7623  C CB  . ASP D 2 145 ? 22.619  37.220  -71.149  1.00 101.64 ? 145 ASP D CB  1 
ATOM   7624  C CG  . ASP D 2 145 ? 21.240  36.927  -71.711  1.00 104.44 ? 145 ASP D CG  1 
ATOM   7625  O OD1 . ASP D 2 145 ? 20.414  36.339  -70.983  1.00 118.12 ? 145 ASP D OD1 1 
ATOM   7626  O OD2 . ASP D 2 145 ? 20.985  37.278  -72.883  1.00 92.54  ? 145 ASP D OD2 1 
ATOM   7627  N N   . ASN D 2 146 ? 23.234  35.683  -68.733  1.00 111.53 ? 146 ASN D N   1 
ATOM   7628  C CA  . ASN D 2 146 ? 22.985  34.914  -67.517  1.00 103.03 ? 146 ASN D CA  1 
ATOM   7629  C C   . ASN D 2 146 ? 21.561  34.374  -67.472  1.00 109.44 ? 146 ASN D C   1 
ATOM   7630  O O   . ASN D 2 146 ? 21.334  33.272  -66.959  1.00 112.04 ? 146 ASN D O   1 
ATOM   7631  C CB  . ASN D 2 146 ? 23.276  35.767  -66.282  1.00 98.86  ? 146 ASN D CB  1 
ATOM   7632  C CG  . ASN D 2 146 ? 24.759  36.015  -66.083  1.00 107.68 ? 146 ASN D CG  1 
ATOM   7633  O OD1 . ASN D 2 146 ? 25.598  35.354  -66.697  1.00 91.92  ? 146 ASN D OD1 1 
ATOM   7634  N ND2 . ASN D 2 146 ? 25.090  36.963  -65.215  1.00 113.05 ? 146 ASN D ND2 1 
ATOM   7635  N N   . GLU D 2 147 ? 20.590  35.133  -67.984  1.00 95.47  ? 147 GLU D N   1 
ATOM   7636  C CA  . GLU D 2 147 ? 19.243  34.591  -68.131  1.00 106.22 ? 147 GLU D CA  1 
ATOM   7637  C C   . GLU D 2 147 ? 19.208  33.504  -69.198  1.00 109.12 ? 147 GLU D C   1 
ATOM   7638  O O   . GLU D 2 147 ? 18.474  32.518  -69.066  1.00 107.41 ? 147 GLU D O   1 
ATOM   7639  C CB  . GLU D 2 147 ? 18.257  35.709  -68.463  1.00 117.23 ? 147 GLU D CB  1 
ATOM   7640  C CG  . GLU D 2 147 ? 18.069  36.718  -67.340  1.00 137.72 ? 147 GLU D CG  1 
ATOM   7641  C CD  . GLU D 2 147 ? 17.051  37.790  -67.678  1.00 150.61 ? 147 GLU D CD  1 
ATOM   7642  O OE1 . GLU D 2 147 ? 16.600  37.835  -68.842  1.00 150.27 ? 147 GLU D OE1 1 
ATOM   7643  O OE2 . GLU D 2 147 ? 16.703  38.585  -66.779  1.00 149.34 ? 147 GLU D OE2 1 
ATOM   7644  N N   . CYS D 2 148 ? 19.997  33.667  -70.262  1.00 112.48 ? 148 CYS D N   1 
ATOM   7645  C CA  . CYS D 2 148 ? 20.110  32.618  -71.270  1.00 103.30 ? 148 CYS D CA  1 
ATOM   7646  C C   . CYS D 2 148 ? 20.747  31.362  -70.684  1.00 110.14 ? 148 CYS D C   1 
ATOM   7647  O O   . CYS D 2 148 ? 20.370  30.241  -71.046  1.00 100.53 ? 148 CYS D O   1 
ATOM   7648  C CB  . CYS D 2 148 ? 20.907  33.139  -72.468  1.00 107.55 ? 148 CYS D CB  1 
ATOM   7649  S SG  . CYS D 2 148 ? 21.276  31.940  -73.774  1.00 136.82 ? 148 CYS D SG  1 
ATOM   7650  N N   . MET D 2 149 ? 21.714  31.529  -69.776  1.00 110.20 ? 149 MET D N   1 
ATOM   7651  C CA  . MET D 2 149 ? 22.309  30.375  -69.106  1.00 99.38  ? 149 MET D CA  1 
ATOM   7652  C C   . MET D 2 149 ? 21.278  29.630  -68.266  1.00 98.52  ? 149 MET D C   1 
ATOM   7653  O O   . MET D 2 149 ? 21.247  28.393  -68.261  1.00 93.95  ? 149 MET D O   1 
ATOM   7654  C CB  . MET D 2 149 ? 23.484  30.812  -68.229  1.00 93.47  ? 149 MET D CB  1 
ATOM   7655  C CG  . MET D 2 149 ? 24.617  31.478  -68.986  1.00 101.23 ? 149 MET D CG  1 
ATOM   7656  S SD  . MET D 2 149 ? 24.929  30.662  -70.559  1.00 113.27 ? 149 MET D SD  1 
ATOM   7657  C CE  . MET D 2 149 ? 26.610  30.103  -70.353  1.00 95.54  ? 149 MET D CE  1 
ATOM   7658  N N   . GLU D 2 150 ? 20.431  30.366  -67.544  1.00 91.31  ? 150 GLU D N   1 
ATOM   7659  C CA  . GLU D 2 150 ? 19.451  29.724  -66.676  1.00 97.11  ? 150 GLU D CA  1 
ATOM   7660  C C   . GLU D 2 150 ? 18.433  28.922  -67.475  1.00 95.49  ? 150 GLU D C   1 
ATOM   7661  O O   . GLU D 2 150 ? 17.956  27.883  -67.005  1.00 103.85 ? 150 GLU D O   1 
ATOM   7662  C CB  . GLU D 2 150 ? 18.747  30.770  -65.811  1.00 105.31 ? 150 GLU D CB  1 
ATOM   7663  C CG  . GLU D 2 150 ? 17.962  30.179  -64.653  1.00 105.18 ? 150 GLU D CG  1 
ATOM   7664  C CD  . GLU D 2 150 ? 18.845  29.418  -63.682  1.00 110.75 ? 150 GLU D CD  1 
ATOM   7665  O OE1 . GLU D 2 150 ? 20.009  29.828  -63.488  1.00 100.63 ? 150 GLU D OE1 1 
ATOM   7666  O OE2 . GLU D 2 150 ? 18.375  28.408  -63.116  1.00 108.91 ? 150 GLU D OE2 1 
ATOM   7667  N N   . SER D 2 151 ? 18.094  29.383  -68.682  1.00 99.83  ? 151 SER D N   1 
ATOM   7668  C CA  . SER D 2 151 ? 17.168  28.636  -69.527  1.00 105.16 ? 151 SER D CA  1 
ATOM   7669  C C   . SER D 2 151 ? 17.736  27.270  -69.892  1.00 99.52  ? 151 SER D C   1 
ATOM   7670  O O   . SER D 2 151 ? 16.995  26.283  -69.972  1.00 95.71  ? 151 SER D O   1 
ATOM   7671  C CB  . SER D 2 151 ? 16.841  29.440  -70.785  1.00 106.38 ? 151 SER D CB  1 
ATOM   7672  O OG  . SER D 2 151 ? 18.022  29.820  -71.470  1.00 107.24 ? 151 SER D OG  1 
ATOM   7673  N N   . VAL D 2 152 ? 19.047  27.196  -70.128  1.00 96.25  ? 152 VAL D N   1 
ATOM   7674  C CA  . VAL D 2 152 ? 19.692  25.906  -70.357  1.00 96.98  ? 152 VAL D CA  1 
ATOM   7675  C C   . VAL D 2 152 ? 19.612  25.043  -69.104  1.00 98.90  ? 152 VAL D C   1 
ATOM   7676  O O   . VAL D 2 152 ? 19.265  23.858  -69.165  1.00 104.17 ? 152 VAL D O   1 
ATOM   7677  C CB  . VAL D 2 152 ? 21.151  26.109  -70.805  1.00 86.45  ? 152 VAL D CB  1 
ATOM   7678  C CG1 . VAL D 2 152 ? 21.887  24.776  -70.847  1.00 87.23  ? 152 VAL D CG1 1 
ATOM   7679  C CG2 . VAL D 2 152 ? 21.201  26.795  -72.159  1.00 99.31  ? 152 VAL D CG2 1 
ATOM   7680  N N   . ARG D 2 153 ? 19.929  25.628  -67.947  1.00 96.17  ? 153 ARG D N   1 
ATOM   7681  C CA  . ARG D 2 153 ? 19.971  24.854  -66.711  1.00 86.90  ? 153 ARG D CA  1 
ATOM   7682  C C   . ARG D 2 153 ? 18.582  24.382  -66.292  1.00 95.83  ? 153 ARG D C   1 
ATOM   7683  O O   . ARG D 2 153 ? 18.411  23.221  -65.902  1.00 105.47 ? 153 ARG D O   1 
ATOM   7684  C CB  . ARG D 2 153 ? 20.620  25.680  -65.602  1.00 79.11  ? 153 ARG D CB  1 
ATOM   7685  C CG  . ARG D 2 153 ? 22.053  26.105  -65.894  1.00 86.70  ? 153 ARG D CG  1 
ATOM   7686  C CD  . ARG D 2 153 ? 22.665  26.796  -64.687  1.00 78.05  ? 153 ARG D CD  1 
ATOM   7687  N NE  . ARG D 2 153 ? 22.170  28.157  -64.518  1.00 102.79 ? 153 ARG D NE  1 
ATOM   7688  C CZ  . ARG D 2 153 ? 22.927  29.242  -64.600  1.00 104.99 ? 153 ARG D CZ  1 
ATOM   7689  N NH1 . ARG D 2 153 ? 24.231  29.160  -64.810  1.00 104.25 ? 153 ARG D NH1 1 
ATOM   7690  N NH2 . ARG D 2 153 ? 22.364  30.439  -64.459  1.00 106.23 ? 153 ARG D NH2 1 
ATOM   7691  N N   . ASN D 2 154 ? 17.577  25.258  -66.366  1.00 85.83  ? 154 ASN D N   1 
ATOM   7692  C CA  . ASN D 2 154 ? 16.237  24.906  -65.911  1.00 78.92  ? 154 ASN D CA  1 
ATOM   7693  C C   . ASN D 2 154 ? 15.345  24.376  -67.031  1.00 98.80  ? 154 ASN D C   1 
ATOM   7694  O O   . ASN D 2 154 ? 14.140  24.207  -66.820  1.00 94.95  ? 154 ASN D O   1 
ATOM   7695  C CB  . ASN D 2 154 ? 15.573  26.094  -65.189  1.00 93.08  ? 154 ASN D CB  1 
ATOM   7696  C CG  . ASN D 2 154 ? 15.105  27.210  -66.124  1.00 115.26 ? 154 ASN D CG  1 
ATOM   7697  O OD1 . ASN D 2 154 ? 15.270  27.162  -67.341  1.00 121.03 ? 154 ASN D OD1 1 
ATOM   7698  N ND2 . ASN D 2 154 ? 14.505  28.236  -65.523  1.00 128.17 ? 154 ASN D ND2 1 
ATOM   7699  N N   . GLY D 2 155 ? 15.909  24.108  -68.208  1.00 103.58 ? 155 GLY D N   1 
ATOM   7700  C CA  . GLY D 2 155 ? 15.199  23.398  -69.253  1.00 86.53  ? 155 GLY D CA  1 
ATOM   7701  C C   . GLY D 2 155 ? 14.278  24.227  -70.119  1.00 89.09  ? 155 GLY D C   1 
ATOM   7702  O O   . GLY D 2 155 ? 13.472  23.649  -70.858  1.00 89.19  ? 155 GLY D O   1 
ATOM   7703  N N   . THR D 2 156 ? 14.366  25.553  -70.065  1.00 100.49 ? 156 THR D N   1 
ATOM   7704  C CA  . THR D 2 156 ? 13.503  26.431  -70.848  1.00 99.12  ? 156 THR D CA  1 
ATOM   7705  C C   . THR D 2 156 ? 14.286  27.196  -71.912  1.00 108.23 ? 156 THR D C   1 
ATOM   7706  O O   . THR D 2 156 ? 14.007  28.365  -72.190  1.00 121.72 ? 156 THR D O   1 
ATOM   7707  C CB  . THR D 2 156 ? 12.753  27.403  -69.941  1.00 102.12 ? 156 THR D CB  1 
ATOM   7708  O OG1 . THR D 2 156 ? 13.688  28.280  -69.301  1.00 103.38 ? 156 THR D OG1 1 
ATOM   7709  C CG2 . THR D 2 156 ? 11.970  26.643  -68.880  1.00 92.95  ? 156 THR D CG2 1 
ATOM   7710  N N   . TYR D 2 157 ? 15.275  26.546  -72.521  1.00 104.64 ? 157 TYR D N   1 
ATOM   7711  C CA  . TYR D 2 157 ? 16.043  27.180  -73.584  1.00 104.34 ? 157 TYR D CA  1 
ATOM   7712  C C   . TYR D 2 157 ? 15.194  27.289  -74.844  1.00 100.92 ? 157 TYR D C   1 
ATOM   7713  O O   . TYR D 2 157 ? 14.631  26.296  -75.313  1.00 103.19 ? 157 TYR D O   1 
ATOM   7714  C CB  . TYR D 2 157 ? 17.317  26.385  -73.865  1.00 103.23 ? 157 TYR D CB  1 
ATOM   7715  C CG  . TYR D 2 157 ? 18.167  26.943  -74.985  1.00 98.88  ? 157 TYR D CG  1 
ATOM   7716  C CD1 . TYR D 2 157 ? 19.050  27.994  -74.758  1.00 89.91  ? 157 TYR D CD1 1 
ATOM   7717  C CD2 . TYR D 2 157 ? 18.094  26.414  -76.267  1.00 94.59  ? 157 TYR D CD2 1 
ATOM   7718  C CE1 . TYR D 2 157 ? 19.831  28.503  -75.780  1.00 91.98  ? 157 TYR D CE1 1 
ATOM   7719  C CE2 . TYR D 2 157 ? 18.870  26.916  -77.293  1.00 88.39  ? 157 TYR D CE2 1 
ATOM   7720  C CZ  . TYR D 2 157 ? 19.736  27.960  -77.044  1.00 89.65  ? 157 TYR D CZ  1 
ATOM   7721  O OH  . TYR D 2 157 ? 20.512  28.464  -78.061  1.00 77.79  ? 157 TYR D OH  1 
ATOM   7722  N N   . ASP D 2 158 ? 15.106  28.498  -75.394  1.00 109.51 ? 158 ASP D N   1 
ATOM   7723  C CA  . ASP D 2 158 ? 14.267  28.780  -76.557  1.00 108.74 ? 158 ASP D CA  1 
ATOM   7724  C C   . ASP D 2 158 ? 15.157  28.771  -77.796  1.00 102.36 ? 158 ASP D C   1 
ATOM   7725  O O   . ASP D 2 158 ? 15.840  29.755  -78.093  1.00 97.64  ? 158 ASP D O   1 
ATOM   7726  C CB  . ASP D 2 158 ? 13.541  30.109  -76.384  1.00 113.09 ? 158 ASP D CB  1 
ATOM   7727  C CG  . ASP D 2 158 ? 12.386  30.275  -77.350  1.00 116.67 ? 158 ASP D CG  1 
ATOM   7728  O OD1 . ASP D 2 158 ? 11.598  29.318  -77.510  1.00 108.82 ? 158 ASP D OD1 1 
ATOM   7729  O OD2 . ASP D 2 158 ? 12.257  31.367  -77.940  1.00 124.53 ? 158 ASP D OD2 1 
ATOM   7730  N N   . TYR D 2 159 ? 15.152  27.641  -78.515  1.00 97.27  ? 159 TYR D N   1 
ATOM   7731  C CA  . TYR D 2 159 ? 16.024  27.502  -79.681  1.00 92.14  ? 159 TYR D CA  1 
ATOM   7732  C C   . TYR D 2 159 ? 15.680  28.478  -80.802  1.00 93.71  ? 159 TYR D C   1 
ATOM   7733  O O   . TYR D 2 159 ? 16.600  29.142  -81.312  1.00 101.05 ? 159 TYR D O   1 
ATOM   7734  C CB  . TYR D 2 159 ? 16.008  26.047  -80.163  1.00 93.14  ? 159 TYR D CB  1 
ATOM   7735  C CG  . TYR D 2 159 ? 16.670  25.825  -81.502  1.00 104.72 ? 159 TYR D CG  1 
ATOM   7736  C CD1 . TYR D 2 159 ? 15.937  25.885  -82.681  1.00 86.17  ? 159 TYR D CD1 1 
ATOM   7737  C CD2 . TYR D 2 159 ? 18.026  25.545  -81.588  1.00 104.20 ? 159 TYR D CD2 1 
ATOM   7738  C CE1 . TYR D 2 159 ? 16.537  25.681  -83.906  1.00 85.80  ? 159 TYR D CE1 1 
ATOM   7739  C CE2 . TYR D 2 159 ? 18.633  25.338  -82.807  1.00 95.46  ? 159 TYR D CE2 1 
ATOM   7740  C CZ  . TYR D 2 159 ? 17.886  25.407  -83.964  1.00 97.83  ? 159 TYR D CZ  1 
ATOM   7741  O OH  . TYR D 2 159 ? 18.492  25.202  -85.183  1.00 105.11 ? 159 TYR D OH  1 
ATOM   7742  N N   . PRO D 2 160 ? 14.422  28.617  -81.243  1.00 106.46 ? 160 PRO D N   1 
ATOM   7743  C CA  . PRO D 2 160 ? 14.146  29.544  -82.357  1.00 105.83 ? 160 PRO D CA  1 
ATOM   7744  C C   . PRO D 2 160 ? 14.460  31.001  -82.054  1.00 104.09 ? 160 PRO D C   1 
ATOM   7745  O O   . PRO D 2 160 ? 14.571  31.796  -82.996  1.00 99.06  ? 160 PRO D O   1 
ATOM   7746  C CB  . PRO D 2 160 ? 12.647  29.341  -82.631  1.00 95.48  ? 160 PRO D CB  1 
ATOM   7747  C CG  . PRO D 2 160 ? 12.108  28.633  -81.437  1.00 102.77 ? 160 PRO D CG  1 
ATOM   7748  C CD  . PRO D 2 160 ? 13.232  27.807  -80.914  1.00 101.03 ? 160 PRO D CD  1 
ATOM   7749  N N   . GLN D 2 161 ? 14.589  31.383  -80.781  1.00 100.65 ? 161 GLN D N   1 
ATOM   7750  C CA  . GLN D 2 161 ? 14.932  32.765  -80.459  1.00 105.88 ? 161 GLN D CA  1 
ATOM   7751  C C   . GLN D 2 161 ? 16.292  33.146  -81.034  1.00 107.31 ? 161 GLN D C   1 
ATOM   7752  O O   . GLN D 2 161 ? 16.488  34.281  -81.486  1.00 116.49 ? 161 GLN D O   1 
ATOM   7753  C CB  . GLN D 2 161 ? 14.908  32.974  -78.944  1.00 109.63 ? 161 GLN D CB  1 
ATOM   7754  C CG  . GLN D 2 161 ? 15.369  34.354  -78.495  1.00 102.92 ? 161 GLN D CG  1 
ATOM   7755  C CD  . GLN D 2 161 ? 15.215  34.568  -77.001  1.00 114.05 ? 161 GLN D CD  1 
ATOM   7756  O OE1 . GLN D 2 161 ? 14.331  33.993  -76.366  1.00 110.01 ? 161 GLN D OE1 1 
ATOM   7757  N NE2 . GLN D 2 161 ? 16.081  35.398  -76.430  1.00 91.33  ? 161 GLN D NE2 1 
ATOM   7758  N N   . TYR D 2 162 ? 17.239  32.210  -81.031  1.00 104.83 ? 162 TYR D N   1 
ATOM   7759  C CA  . TYR D 2 162 ? 18.592  32.451  -81.517  1.00 93.59  ? 162 TYR D CA  1 
ATOM   7760  C C   . TYR D 2 162 ? 18.917  31.644  -82.768  1.00 95.42  ? 162 TYR D C   1 
ATOM   7761  O O   . TYR D 2 162 ? 20.085  31.583  -83.167  1.00 102.03 ? 162 TYR D O   1 
ATOM   7762  C CB  . TYR D 2 162 ? 19.612  32.130  -80.420  1.00 85.93  ? 162 TYR D CB  1 
ATOM   7763  C CG  . TYR D 2 162 ? 19.165  32.487  -79.019  1.00 98.10  ? 162 TYR D CG  1 
ATOM   7764  C CD1 . TYR D 2 162 ? 18.407  31.599  -78.263  1.00 105.56 ? 162 TYR D CD1 1 
ATOM   7765  C CD2 . TYR D 2 162 ? 19.512  33.703  -78.446  1.00 98.49  ? 162 TYR D CD2 1 
ATOM   7766  C CE1 . TYR D 2 162 ? 17.998  31.917  -76.984  1.00 99.93  ? 162 TYR D CE1 1 
ATOM   7767  C CE2 . TYR D 2 162 ? 19.109  34.029  -77.163  1.00 101.70 ? 162 TYR D CE2 1 
ATOM   7768  C CZ  . TYR D 2 162 ? 18.352  33.132  -76.438  1.00 105.66 ? 162 TYR D CZ  1 
ATOM   7769  O OH  . TYR D 2 162 ? 17.946  33.448  -75.162  1.00 105.73 ? 162 TYR D OH  1 
ATOM   7770  N N   . SER D 2 163 ? 17.912  31.026  -83.395  1.00 93.61  ? 163 SER D N   1 
ATOM   7771  C CA  . SER D 2 163 ? 18.171  30.104  -84.499  1.00 94.86  ? 163 SER D CA  1 
ATOM   7772  C C   . SER D 2 163 ? 18.823  30.808  -85.684  1.00 105.81 ? 163 SER D C   1 
ATOM   7773  O O   . SER D 2 163 ? 19.766  30.280  -86.284  1.00 97.08  ? 163 SER D O   1 
ATOM   7774  C CB  . SER D 2 163 ? 16.871  29.427  -84.932  1.00 83.54  ? 163 SER D CB  1 
ATOM   7775  O OG  . SER D 2 163 ? 17.090  28.570  -86.039  1.00 94.32  ? 163 SER D OG  1 
ATOM   7776  N N   . GLU D 2 164 ? 18.333  31.997  -86.039  1.00 111.50 ? 164 GLU D N   1 
ATOM   7777  C CA  . GLU D 2 164 ? 18.890  32.707  -87.186  1.00 108.84 ? 164 GLU D CA  1 
ATOM   7778  C C   . GLU D 2 164 ? 20.234  33.345  -86.852  1.00 105.99 ? 164 GLU D C   1 
ATOM   7779  O O   . GLU D 2 164 ? 21.126  33.401  -87.706  1.00 109.84 ? 164 GLU D O   1 
ATOM   7780  C CB  . GLU D 2 164 ? 17.899  33.760  -87.687  1.00 97.02  ? 164 GLU D CB  1 
ATOM   7781  C CG  . GLU D 2 164 ? 18.419  34.646  -88.821  1.00 105.24 ? 164 GLU D CG  1 
ATOM   7782  C CD  . GLU D 2 164 ? 18.487  33.939  -90.170  1.00 113.39 ? 164 GLU D CD  1 
ATOM   7783  O OE1 . GLU D 2 164 ? 18.469  32.691  -90.211  1.00 114.75 ? 164 GLU D OE1 1 
ATOM   7784  O OE2 . GLU D 2 164 ? 18.558  34.641  -91.201  1.00 114.16 ? 164 GLU D OE2 1 
ATOM   7785  N N   . GLU D 2 165 ? 20.397  33.828  -85.618  1.00 101.91 ? 165 GLU D N   1 
ATOM   7786  C CA  . GLU D 2 165 ? 21.681  34.390  -85.211  1.00 104.77 ? 165 GLU D CA  1 
ATOM   7787  C C   . GLU D 2 165 ? 22.775  33.331  -85.237  1.00 108.68 ? 165 GLU D C   1 
ATOM   7788  O O   . GLU D 2 165 ? 23.908  33.605  -85.651  1.00 119.92 ? 165 GLU D O   1 
ATOM   7789  C CB  . GLU D 2 165 ? 21.568  35.008  -83.818  1.00 100.11 ? 165 GLU D CB  1 
ATOM   7790  C CG  . GLU D 2 165 ? 22.875  35.568  -83.278  1.00 90.44  ? 165 GLU D CG  1 
ATOM   7791  C CD  . GLU D 2 165 ? 22.744  36.100  -81.864  1.00 123.60 ? 165 GLU D CD  1 
ATOM   7792  O OE1 . GLU D 2 165 ? 21.618  36.081  -81.324  1.00 113.00 ? 165 GLU D OE1 1 
ATOM   7793  O OE2 . GLU D 2 165 ? 23.768  36.530  -81.291  1.00 110.08 ? 165 GLU D OE2 1 
ATOM   7794  N N   . ALA D 2 166 ? 22.457  32.115  -84.791  1.00 107.57 ? 166 ALA D N   1 
ATOM   7795  C CA  . ALA D 2 166 ? 23.438  31.037  -84.813  1.00 103.79 ? 166 ALA D CA  1 
ATOM   7796  C C   . ALA D 2 166 ? 23.766  30.612  -86.238  1.00 97.61  ? 166 ALA D C   1 
ATOM   7797  O O   . ALA D 2 166 ? 24.928  30.332  -86.556  1.00 104.15 ? 166 ALA D O   1 
ATOM   7798  C CB  . ALA D 2 166 ? 22.928  29.845  -84.004  1.00 94.30  ? 166 ALA D CB  1 
ATOM   7799  N N   . ARG D 2 167 ? 22.757  30.552  -87.110  1.00 113.81 ? 167 ARG D N   1 
ATOM   7800  C CA  . ARG D 2 167 ? 22.987  30.058  -88.464  1.00 110.95 ? 167 ARG D CA  1 
ATOM   7801  C C   . ARG D 2 167 ? 23.869  31.011  -89.263  1.00 101.78 ? 167 ARG D C   1 
ATOM   7802  O O   . ARG D 2 167 ? 24.686  30.565  -90.077  1.00 97.72  ? 167 ARG D O   1 
ATOM   7803  C CB  . ARG D 2 167 ? 21.654  29.818  -89.173  1.00 99.76  ? 167 ARG D CB  1 
ATOM   7804  C CG  . ARG D 2 167 ? 21.738  28.816  -90.315  1.00 96.40  ? 167 ARG D CG  1 
ATOM   7805  C CD  . ARG D 2 167 ? 20.368  28.563  -90.916  1.00 94.97  ? 167 ARG D CD  1 
ATOM   7806  N NE  . ARG D 2 167 ? 19.780  29.787  -91.443  1.00 112.22 ? 167 ARG D NE  1 
ATOM   7807  C CZ  . ARG D 2 167 ? 19.804  30.137  -92.722  1.00 106.64 ? 167 ARG D CZ  1 
ATOM   7808  N NH1 . ARG D 2 167 ? 20.351  29.358  -93.641  1.00 94.60  ? 167 ARG D NH1 1 
ATOM   7809  N NH2 . ARG D 2 167 ? 19.265  31.296  -93.088  1.00 95.68  ? 167 ARG D NH2 1 
ATOM   7810  N N   . LEU D 2 168 ? 23.720  32.324  -89.054  1.00 102.71 ? 168 LEU D N   1 
ATOM   7811  C CA  . LEU D 2 168 ? 24.629  33.262  -89.710  1.00 110.71 ? 168 LEU D CA  1 
ATOM   7812  C C   . LEU D 2 168 ? 26.053  33.091  -89.196  1.00 112.62 ? 168 LEU D C   1 
ATOM   7813  O O   . LEU D 2 168 ? 27.009  33.142  -89.977  1.00 119.60 ? 168 LEU D O   1 
ATOM   7814  C CB  . LEU D 2 168 ? 24.144  34.709  -89.537  1.00 108.30 ? 168 LEU D CB  1 
ATOM   7815  C CG  . LEU D 2 168 ? 24.289  35.541  -88.253  1.00 114.44 ? 168 LEU D CG  1 
ATOM   7816  C CD1 . LEU D 2 168 ? 25.693  36.116  -88.065  1.00 107.54 ? 168 LEU D CD1 1 
ATOM   7817  C CD2 . LEU D 2 168 ? 23.267  36.667  -88.257  1.00 108.34 ? 168 LEU D CD2 1 
ATOM   7818  N N   . LYS D 2 169 ? 26.218  32.878  -87.887  1.00 112.02 ? 169 LYS D N   1 
ATOM   7819  C CA  . LYS D 2 169 ? 27.559  32.665  -87.349  1.00 108.06 ? 169 LYS D CA  1 
ATOM   7820  C C   . LYS D 2 169 ? 28.102  31.291  -87.716  1.00 105.49 ? 169 LYS D C   1 
ATOM   7821  O O   . LYS D 2 169 ? 29.319  31.127  -87.852  1.00 115.05 ? 169 LYS D O   1 
ATOM   7822  C CB  . LYS D 2 169 ? 27.564  32.844  -85.830  1.00 95.83  ? 169 LYS D CB  1 
ATOM   7823  C CG  . LYS D 2 169 ? 27.846  34.268  -85.368  1.00 106.65 ? 169 LYS D CG  1 
ATOM   7824  C CD  . LYS D 2 169 ? 28.605  34.285  -84.045  1.00 106.30 ? 169 LYS D CD  1 
ATOM   7825  C CE  . LYS D 2 169 ? 30.112  34.221  -84.254  1.00 97.93  ? 169 LYS D CE  1 
ATOM   7826  N NZ  . LYS D 2 169 ? 30.714  35.582  -84.350  1.00 99.12  ? 169 LYS D NZ  1 
ATOM   7827  N N   . ARG D 2 170 ? 27.228  30.292  -87.861  1.00 106.87 ? 170 ARG D N   1 
ATOM   7828  C CA  . ARG D 2 170 ? 27.678  28.989  -88.341  1.00 99.04  ? 170 ARG D CA  1 
ATOM   7829  C C   . ARG D 2 170 ? 28.187  29.083  -89.774  1.00 109.73 ? 170 ARG D C   1 
ATOM   7830  O O   . ARG D 2 170 ? 29.239  28.528  -90.110  1.00 114.85 ? 170 ARG D O   1 
ATOM   7831  C CB  . ARG D 2 170 ? 26.544  27.964  -88.243  1.00 104.12 ? 170 ARG D CB  1 
ATOM   7832  C CG  . ARG D 2 170 ? 26.407  27.319  -86.875  1.00 98.83  ? 170 ARG D CG  1 
ATOM   7833  C CD  . ARG D 2 170 ? 25.456  26.124  -86.887  1.00 98.01  ? 170 ARG D CD  1 
ATOM   7834  N NE  . ARG D 2 170 ? 24.068  26.501  -86.644  1.00 106.23 ? 170 ARG D NE  1 
ATOM   7835  C CZ  . ARG D 2 170 ? 23.125  26.543  -87.576  1.00 106.65 ? 170 ARG D CZ  1 
ATOM   7836  N NH1 . ARG D 2 170 ? 23.383  26.231  -88.835  1.00 91.44  ? 170 ARG D NH1 1 
ATOM   7837  N NH2 . ARG D 2 170 ? 21.891  26.904  -87.234  1.00 111.24 ? 170 ARG D NH2 1 
ATOM   7838  N N   . GLU D 2 171 ? 27.449  29.789  -90.634  1.00 123.04 ? 171 GLU D N   1 
ATOM   7839  C CA  . GLU D 2 171 ? 27.792  29.831  -92.051  1.00 126.24 ? 171 GLU D CA  1 
ATOM   7840  C C   . GLU D 2 171 ? 29.029  30.689  -92.300  1.00 127.84 ? 171 GLU D C   1 
ATOM   7841  O O   . GLU D 2 171 ? 29.933  30.295  -93.049  1.00 132.07 ? 171 GLU D O   1 
ATOM   7842  C CB  . GLU D 2 171 ? 26.602  30.353  -92.858  1.00 116.64 ? 171 GLU D CB  1 
ATOM   7843  C CG  . GLU D 2 171 ? 26.828  30.367  -94.360  1.00 130.67 ? 171 GLU D CG  1 
ATOM   7844  C CD  . GLU D 2 171 ? 26.242  29.152  -95.054  1.00 130.74 ? 171 GLU D CD  1 
ATOM   7845  O OE1 . GLU D 2 171 ? 25.170  28.677  -94.621  1.00 129.55 ? 171 GLU D OE1 1 
ATOM   7846  O OE2 . GLU D 2 171 ? 26.850  28.674  -96.036  1.00 102.37 ? 171 GLU D OE2 1 
ATOM   7847  N N   . GLU D 2 172 ? 29.087  31.871  -91.682  1.00 131.67 ? 172 GLU D N   1 
ATOM   7848  C CA  . GLU D 2 172 ? 30.151  32.816  -91.998  1.00 129.38 ? 172 GLU D CA  1 
ATOM   7849  C C   . GLU D 2 172 ? 31.494  32.411  -91.401  1.00 125.11 ? 172 GLU D C   1 
ATOM   7850  O O   . GLU D 2 172 ? 32.536  32.843  -91.908  1.00 120.27 ? 172 GLU D O   1 
ATOM   7851  C CB  . GLU D 2 172 ? 29.770  34.221  -91.526  1.00 130.31 ? 172 GLU D CB  1 
ATOM   7852  C CG  . GLU D 2 172 ? 29.861  34.432  -90.026  1.00 146.99 ? 172 GLU D CG  1 
ATOM   7853  C CD  . GLU D 2 172 ? 29.189  35.716  -89.584  1.00 145.65 ? 172 GLU D CD  1 
ATOM   7854  O OE1 . GLU D 2 172 ? 28.607  36.410  -90.445  1.00 149.40 ? 172 GLU D OE1 1 
ATOM   7855  O OE2 . GLU D 2 172 ? 29.241  36.031  -88.377  1.00 136.56 ? 172 GLU D OE2 1 
ATOM   7856  N N   . ILE D 2 173 ? 31.498  31.594  -90.349  1.00 135.71 ? 173 ILE D N   1 
ATOM   7857  C CA  . ILE D 2 173 ? 32.753  31.125  -89.771  1.00 153.41 ? 173 ILE D CA  1 
ATOM   7858  C C   . ILE D 2 173 ? 33.434  30.196  -90.768  1.00 144.74 ? 173 ILE D C   1 
ATOM   7859  O O   . ILE D 2 173 ? 32.842  29.214  -91.230  1.00 127.58 ? 173 ILE D O   1 
ATOM   7860  C CB  . ILE D 2 173 ? 32.514  30.427  -88.425  1.00 141.70 ? 173 ILE D CB  1 
ATOM   7861  C CG1 . ILE D 2 173 ? 32.418  31.456  -87.296  1.00 129.59 ? 173 ILE D CG1 1 
ATOM   7862  C CG2 . ILE D 2 173 ? 33.625  29.424  -88.133  1.00 111.99 ? 173 ILE D CG2 1 
ATOM   7863  C CD1 . ILE D 2 173 ? 33.724  32.164  -87.004  1.00 112.15 ? 173 ILE D CD1 1 
ATOM   7864  N N   . SER D 2 174 ? 34.679  30.510  -91.109  1.00 125.26 ? 174 SER D N   1 
ATOM   7865  C CA  . SER D 2 174 ? 35.445  29.694  -92.043  1.00 107.20 ? 174 SER D CA  1 
ATOM   7866  C C   . SER D 2 174 ? 36.708  29.160  -91.378  1.00 112.76 ? 174 SER D C   1 
ATOM   7867  O O   . SER D 2 174 ? 36.766  29.026  -90.155  1.00 114.29 ? 174 SER D O   1 
ATOM   7868  C CB  . SER D 2 174 ? 35.803  30.498  -93.294  1.00 110.17 ? 174 SER D CB  1 
ATOM   7869  O OG  . SER D 2 174 ? 34.638  30.908  -93.990  1.00 108.25 ? 174 SER D OG  1 
ATOM   7870  N N   . ASP E 1 1   ? 2.608   23.456  -86.560  1.00 98.64  ? 8   ASP E N   1 
ATOM   7871  C CA  . ASP E 1 1   ? 3.905   23.158  -85.958  1.00 86.66  ? 8   ASP E CA  1 
ATOM   7872  C C   . ASP E 1 1   ? 4.365   21.706  -86.170  1.00 86.37  ? 8   ASP E C   1 
ATOM   7873  O O   . ASP E 1 1   ? 5.443   21.489  -86.723  1.00 103.53 ? 8   ASP E O   1 
ATOM   7874  C CB  . ASP E 1 1   ? 3.890   23.493  -84.458  1.00 102.80 ? 8   ASP E CB  1 
ATOM   7875  C CG  . ASP E 1 1   ? 4.078   24.970  -84.189  1.00 114.14 ? 8   ASP E CG  1 
ATOM   7876  O OD1 . ASP E 1 1   ? 4.945   25.585  -84.845  1.00 114.34 ? 8   ASP E OD1 1 
ATOM   7877  O OD2 . ASP E 1 1   ? 3.357   25.516  -83.325  1.00 97.98  ? 8   ASP E OD2 1 
ATOM   7878  N N   . PRO E 1 2   ? 3.578   20.709  -85.745  1.00 92.99  ? 9   PRO E N   1 
ATOM   7879  C CA  . PRO E 1 2   ? 4.072   19.328  -85.819  1.00 95.53  ? 9   PRO E CA  1 
ATOM   7880  C C   . PRO E 1 2   ? 4.025   18.803  -87.247  1.00 104.98 ? 9   PRO E C   1 
ATOM   7881  O O   . PRO E 1 2   ? 3.016   18.943  -87.943  1.00 121.83 ? 9   PRO E O   1 
ATOM   7882  C CB  . PRO E 1 2   ? 3.113   18.559  -84.904  1.00 90.61  ? 9   PRO E CB  1 
ATOM   7883  C CG  . PRO E 1 2   ? 1.833   19.284  -85.052  1.00 81.86  ? 9   PRO E CG  1 
ATOM   7884  C CD  . PRO E 1 2   ? 2.184   20.743  -85.253  1.00 104.56 ? 9   PRO E CD  1 
ATOM   7885  N N   . GLY E 1 3   ? 5.127   18.203  -87.677  1.00 87.65  ? 10  GLY E N   1 
ATOM   7886  C CA  . GLY E 1 3   ? 5.214   17.531  -88.957  1.00 76.35  ? 10  GLY E CA  1 
ATOM   7887  C C   . GLY E 1 3   ? 5.026   16.035  -88.815  1.00 81.85  ? 10  GLY E C   1 
ATOM   7888  O O   . GLY E 1 3   ? 4.394   15.549  -87.868  1.00 86.74  ? 10  GLY E O   1 
ATOM   7889  N N   . ASP E 1 4   ? 5.568   15.288  -89.771  1.00 74.03  ? 11  ASP E N   1 
ATOM   7890  C CA  . ASP E 1 4   ? 5.590   13.838  -89.648  1.00 66.87  ? 11  ASP E CA  1 
ATOM   7891  C C   . ASP E 1 4   ? 6.575   13.426  -88.563  1.00 71.73  ? 11  ASP E C   1 
ATOM   7892  O O   . ASP E 1 4   ? 7.694   13.942  -88.491  1.00 68.01  ? 11  ASP E O   1 
ATOM   7893  C CB  . ASP E 1 4   ? 5.962   13.194  -90.982  1.00 73.66  ? 11  ASP E CB  1 
ATOM   7894  C CG  . ASP E 1 4   ? 4.908   13.416  -92.048  1.00 88.28  ? 11  ASP E CG  1 
ATOM   7895  O OD1 . ASP E 1 4   ? 3.855   14.009  -91.727  1.00 89.16  ? 11  ASP E OD1 1 
ATOM   7896  O OD2 . ASP E 1 4   ? 5.130   12.999  -93.206  1.00 92.03  ? 11  ASP E OD2 1 
ATOM   7897  N N   . GLN E 1 5   ? 6.155   12.495  -87.707  1.00 70.74  ? 12  GLN E N   1 
ATOM   7898  C CA  . GLN E 1 5   ? 6.946   12.115  -86.546  1.00 60.20  ? 12  GLN E CA  1 
ATOM   7899  C C   . GLN E 1 5   ? 7.030   10.602  -86.403  1.00 61.94  ? 12  GLN E C   1 
ATOM   7900  O O   . GLN E 1 5   ? 6.114   9.866   -86.779  1.00 63.21  ? 12  GLN E O   1 
ATOM   7901  C CB  . GLN E 1 5   ? 6.371   12.709  -85.253  1.00 55.37  ? 12  GLN E CB  1 
ATOM   7902  C CG  . GLN E 1 5   ? 6.479   14.220  -85.157  1.00 63.51  ? 12  GLN E CG  1 
ATOM   7903  C CD  . GLN E 1 5   ? 6.185   14.737  -83.762  1.00 64.20  ? 12  GLN E CD  1 
ATOM   7904  O OE1 . GLN E 1 5   ? 5.917   13.962  -82.844  1.00 75.04  ? 12  GLN E OE1 1 
ATOM   7905  N NE2 . GLN E 1 5   ? 6.237   16.054  -83.596  1.00 69.37  ? 12  GLN E NE2 1 
ATOM   7906  N N   . ILE E 1 6   ? 8.153   10.153  -85.844  1.00 61.62  ? 13  ILE E N   1 
ATOM   7907  C CA  . ILE E 1 6   ? 8.354   8.773   -85.421  1.00 63.50  ? 13  ILE E CA  1 
ATOM   7908  C C   . ILE E 1 6   ? 8.875   8.810   -83.989  1.00 64.28  ? 13  ILE E C   1 
ATOM   7909  O O   . ILE E 1 6   ? 9.693   9.669   -83.641  1.00 67.57  ? 13  ILE E O   1 
ATOM   7910  C CB  . ILE E 1 6   ? 9.326   8.017   -86.356  1.00 60.12  ? 13  ILE E CB  1 
ATOM   7911  C CG1 . ILE E 1 6   ? 9.433   6.540   -85.963  1.00 63.40  ? 13  ILE E CG1 1 
ATOM   7912  C CG2 . ILE E 1 6   ? 10.700  8.683   -86.379  1.00 72.65  ? 13  ILE E CG2 1 
ATOM   7913  C CD1 . ILE E 1 6   ? 8.370   5.661   -86.582  1.00 54.71  ? 13  ILE E CD1 1 
ATOM   7914  N N   . CYS E 1 7   ? 8.382   7.901   -83.151  1.00 78.62  ? 14  CYS E N   1 
ATOM   7915  C CA  . CYS E 1 7   ? 8.669   7.941   -81.724  1.00 63.58  ? 14  CYS E CA  1 
ATOM   7916  C C   . CYS E 1 7   ? 9.135   6.578   -81.232  1.00 64.69  ? 14  CYS E C   1 
ATOM   7917  O O   . CYS E 1 7   ? 8.853   5.541   -81.838  1.00 67.34  ? 14  CYS E O   1 
ATOM   7918  C CB  . CYS E 1 7   ? 7.442   8.389   -80.915  1.00 56.56  ? 14  CYS E CB  1 
ATOM   7919  S SG  . CYS E 1 7   ? 6.861   10.071  -81.245  1.00 107.12 ? 14  CYS E SG  1 
ATOM   7920  N N   . ILE E 1 8   ? 9.860   6.600   -80.116  1.00 72.23  ? 15  ILE E N   1 
ATOM   7921  C CA  . ILE E 1 8   ? 10.332  5.399   -79.438  1.00 73.04  ? 15  ILE E CA  1 
ATOM   7922  C C   . ILE E 1 8   ? 9.706   5.371   -78.048  1.00 66.79  ? 15  ILE E C   1 
ATOM   7923  O O   . ILE E 1 8   ? 9.764   6.367   -77.317  1.00 68.80  ? 15  ILE E O   1 
ATOM   7924  C CB  . ILE E 1 8   ? 11.869  5.363   -79.341  1.00 71.58  ? 15  ILE E CB  1 
ATOM   7925  C CG1 . ILE E 1 8   ? 12.517  5.860   -80.640  1.00 69.91  ? 15  ILE E CG1 1 
ATOM   7926  C CG2 . ILE E 1 8   ? 12.346  3.956   -79.019  1.00 63.29  ? 15  ILE E CG2 1 
ATOM   7927  C CD1 . ILE E 1 8   ? 12.511  4.849   -81.774  1.00 66.84  ? 15  ILE E CD1 1 
ATOM   7928  N N   . GLY E 1 9   ? 9.117   4.236   -77.683  1.00 63.97  ? 16  GLY E N   1 
ATOM   7929  C CA  . GLY E 1 9   ? 8.430   4.121   -76.415  1.00 77.03  ? 16  GLY E CA  1 
ATOM   7930  C C   . GLY E 1 9   ? 8.319   2.677   -75.978  1.00 76.42  ? 16  GLY E C   1 
ATOM   7931  O O   . GLY E 1 9   ? 8.861   1.773   -76.617  1.00 58.14  ? 16  GLY E O   1 
ATOM   7932  N N   . TYR E 1 10  ? 7.599   2.466   -74.876  1.00 71.87  ? 17  TYR E N   1 
ATOM   7933  C CA  . TYR E 1 10  ? 7.545   1.145   -74.264  1.00 69.86  ? 17  TYR E CA  1 
ATOM   7934  C C   . TYR E 1 10  ? 6.170   0.890   -73.656  1.00 72.90  ? 17  TYR E C   1 
ATOM   7935  O O   . TYR E 1 10  ? 5.348   1.797   -73.504  1.00 69.55  ? 17  TYR E O   1 
ATOM   7936  C CB  . TYR E 1 10  ? 8.651   0.970   -73.215  1.00 71.70  ? 17  TYR E CB  1 
ATOM   7937  C CG  . TYR E 1 10  ? 8.664   2.009   -72.115  1.00 75.97  ? 17  TYR E CG  1 
ATOM   7938  C CD1 . TYR E 1 10  ? 9.251   3.254   -72.313  1.00 81.03  ? 17  TYR E CD1 1 
ATOM   7939  C CD2 . TYR E 1 10  ? 8.112   1.736   -70.871  1.00 74.60  ? 17  TYR E CD2 1 
ATOM   7940  C CE1 . TYR E 1 10  ? 9.271   4.203   -71.307  1.00 85.11  ? 17  TYR E CE1 1 
ATOM   7941  C CE2 . TYR E 1 10  ? 8.129   2.676   -69.860  1.00 78.82  ? 17  TYR E CE2 1 
ATOM   7942  C CZ  . TYR E 1 10  ? 8.709   3.908   -70.083  1.00 85.85  ? 17  TYR E CZ  1 
ATOM   7943  O OH  . TYR E 1 10  ? 8.729   4.849   -69.080  1.00 89.56  ? 17  TYR E OH  1 
ATOM   7944  N N   . HIS E 1 11  ? 5.946   -0.377  -73.308  1.00 80.87  ? 18  HIS E N   1 
ATOM   7945  C CA  . HIS E 1 11  ? 4.653   -0.853  -72.828  1.00 66.87  ? 18  HIS E CA  1 
ATOM   7946  C C   . HIS E 1 11  ? 4.317   -0.270  -71.457  1.00 75.93  ? 18  HIS E C   1 
ATOM   7947  O O   . HIS E 1 11  ? 5.167   -0.200  -70.565  1.00 86.76  ? 18  HIS E O   1 
ATOM   7948  C CB  . HIS E 1 11  ? 4.677   -2.387  -72.765  1.00 76.38  ? 18  HIS E CB  1 
ATOM   7949  C CG  . HIS E 1 11  ? 3.346   -3.034  -72.513  1.00 105.58 ? 18  HIS E CG  1 
ATOM   7950  N ND1 . HIS E 1 11  ? 2.347   -2.450  -71.765  1.00 101.49 ? 18  HIS E ND1 1 
ATOM   7951  C CD2 . HIS E 1 11  ? 2.863   -4.240  -72.898  1.00 107.05 ? 18  HIS E CD2 1 
ATOM   7952  C CE1 . HIS E 1 11  ? 1.304   -3.259  -71.709  1.00 107.04 ? 18  HIS E CE1 1 
ATOM   7953  N NE2 . HIS E 1 11  ? 1.592   -4.353  -72.389  1.00 120.22 ? 18  HIS E NE2 1 
ATOM   7954  N N   . ALA E 1 12  ? 3.063   0.153   -71.301  1.00 77.94  ? 19  ALA E N   1 
ATOM   7955  C CA  . ALA E 1 12  ? 2.483   0.460   -70.002  1.00 71.51  ? 19  ALA E CA  1 
ATOM   7956  C C   . ALA E 1 12  ? 1.069   -0.106  -69.952  1.00 78.13  ? 19  ALA E C   1 
ATOM   7957  O O   . ALA E 1 12  ? 0.390   -0.200  -70.978  1.00 88.40  ? 19  ALA E O   1 
ATOM   7958  C CB  . ALA E 1 12  ? 2.461   1.969   -69.726  1.00 62.88  ? 19  ALA E CB  1 
ATOM   7959  N N   . ASN E 1 13  ? 0.632   -0.492  -68.754  1.00 84.34  ? 20  ASN E N   1 
ATOM   7960  C CA  . ASN E 1 13  ? -0.716  -1.021  -68.561  1.00 74.81  ? 20  ASN E CA  1 
ATOM   7961  C C   . ASN E 1 13  ? -1.267  -0.484  -67.243  1.00 63.43  ? 20  ASN E C   1 
ATOM   7962  O O   . ASN E 1 13  ? -0.724  0.456   -66.655  1.00 79.06  ? 20  ASN E O   1 
ATOM   7963  C CB  . ASN E 1 13  ? -0.730  -2.558  -68.627  1.00 66.00  ? 20  ASN E CB  1 
ATOM   7964  C CG  . ASN E 1 13  ? 0.152   -3.211  -67.575  1.00 83.88  ? 20  ASN E CG  1 
ATOM   7965  O OD1 . ASN E 1 13  ? 0.536   -2.591  -66.585  1.00 77.36  ? 20  ASN E OD1 1 
ATOM   7966  N ND2 . ASN E 1 13  ? 0.473   -4.483  -67.789  1.00 75.13  ? 20  ASN E ND2 1 
ATOM   7967  N N   . ASN E 1 14  ? -2.359  -1.088  -66.779  1.00 81.00  ? 21  ASN E N   1 
ATOM   7968  C CA  . ASN E 1 14  ? -3.074  -0.643  -65.589  1.00 103.87 ? 21  ASN E CA  1 
ATOM   7969  C C   . ASN E 1 14  ? -2.597  -1.326  -64.313  1.00 96.09  ? 21  ASN E C   1 
ATOM   7970  O O   . ASN E 1 14  ? -3.193  -1.110  -63.253  1.00 86.76  ? 21  ASN E O   1 
ATOM   7971  C CB  . ASN E 1 14  ? -4.578  -0.871  -65.763  1.00 94.82  ? 21  ASN E CB  1 
ATOM   7972  C CG  . ASN E 1 14  ? -4.914  -2.301  -66.164  1.00 105.75 ? 21  ASN E CG  1 
ATOM   7973  O OD1 . ASN E 1 14  ? -4.040  -3.169  -66.200  1.00 102.97 ? 21  ASN E OD1 1 
ATOM   7974  N ND2 . ASN E 1 14  ? -6.184  -2.551  -66.463  1.00 108.27 ? 21  ASN E ND2 1 
ATOM   7975  N N   . SER E 1 15  ? -1.552  -2.147  -64.392  1.00 95.83  ? 22  SER E N   1 
ATOM   7976  C CA  . SER E 1 15  ? -1.086  -2.885  -63.225  1.00 75.00  ? 22  SER E CA  1 
ATOM   7977  C C   . SER E 1 15  ? -0.602  -1.939  -62.133  1.00 72.79  ? 22  SER E C   1 
ATOM   7978  O O   . SER E 1 15  ? -0.015  -0.888  -62.406  1.00 83.21  ? 22  SER E O   1 
ATOM   7979  C CB  . SER E 1 15  ? 0.036   -3.845  -63.619  1.00 83.90  ? 22  SER E CB  1 
ATOM   7980  O OG  . SER E 1 15  ? 0.573   -4.494  -62.479  1.00 83.76  ? 22  SER E OG  1 
ATOM   7981  N N   . THR E 1 16  ? -0.862  -2.322  -60.884  1.00 81.46  ? 23  THR E N   1 
ATOM   7982  C CA  . THR E 1 16  ? -0.385  -1.585  -59.721  1.00 87.99  ? 23  THR E CA  1 
ATOM   7983  C C   . THR E 1 16  ? 0.608   -2.392  -58.893  1.00 85.52  ? 23  THR E C   1 
ATOM   7984  O O   . THR E 1 16  ? 0.912   -2.001  -57.760  1.00 77.37  ? 23  THR E O   1 
ATOM   7985  C CB  . THR E 1 16  ? -1.562  -1.146  -58.842  1.00 78.37  ? 23  THR E CB  1 
ATOM   7986  O OG1 . THR E 1 16  ? -2.513  -2.213  -58.746  1.00 84.65  ? 23  THR E OG1 1 
ATOM   7987  C CG2 . THR E 1 16  ? -2.237  0.085   -59.429  1.00 81.46  ? 23  THR E CG2 1 
ATOM   7988  N N   . GLU E 1 17  ? 1.112   -3.507  -59.420  1.00 83.85  ? 24  GLU E N   1 
ATOM   7989  C CA  . GLU E 1 17  ? 2.097   -4.296  -58.693  1.00 71.56  ? 24  GLU E CA  1 
ATOM   7990  C C   . GLU E 1 17  ? 3.351   -3.473  -58.427  1.00 80.71  ? 24  GLU E C   1 
ATOM   7991  O O   . GLU E 1 17  ? 3.812   -2.716  -59.285  1.00 85.21  ? 24  GLU E O   1 
ATOM   7992  C CB  . GLU E 1 17  ? 2.456   -5.558  -59.477  1.00 81.94  ? 24  GLU E CB  1 
ATOM   7993  C CG  . GLU E 1 17  ? 1.298   -6.513  -59.687  1.00 107.92 ? 24  GLU E CG  1 
ATOM   7994  C CD  . GLU E 1 17  ? 1.756   -7.947  -59.842  1.00 124.06 ? 24  GLU E CD  1 
ATOM   7995  O OE1 . GLU E 1 17  ? 1.947   -8.394  -60.994  1.00 111.21 ? 24  GLU E OE1 1 
ATOM   7996  O OE2 . GLU E 1 17  ? 1.924   -8.626  -58.806  1.00 119.44 ? 24  GLU E OE2 1 
ATOM   7997  N N   . GLN E 1 18  ? 3.903   -3.626  -57.227  1.00 83.17  ? 25  GLN E N   1 
ATOM   7998  C CA  . GLN E 1 18  ? 5.068   -2.868  -56.800  1.00 76.01  ? 25  GLN E CA  1 
ATOM   7999  C C   . GLN E 1 18  ? 6.207   -3.805  -56.430  1.00 76.58  ? 25  GLN E C   1 
ATOM   8000  O O   . GLN E 1 18  ? 6.002   -4.819  -55.755  1.00 99.33  ? 25  GLN E O   1 
ATOM   8001  C CB  . GLN E 1 18  ? 4.736   -1.965  -55.608  1.00 69.52  ? 25  GLN E CB  1 
ATOM   8002  C CG  . GLN E 1 18  ? 3.840   -0.790  -55.955  1.00 75.58  ? 25  GLN E CG  1 
ATOM   8003  C CD  . GLN E 1 18  ? 3.827   0.274   -54.873  1.00 94.29  ? 25  GLN E CD  1 
ATOM   8004  O OE1 . GLN E 1 18  ? 3.804   1.470   -55.166  1.00 97.82  ? 25  GLN E OE1 1 
ATOM   8005  N NE2 . GLN E 1 18  ? 3.842   -0.156  -53.616  1.00 84.98  ? 25  GLN E NE2 1 
ATOM   8006  N N   . VAL E 1 19  ? 7.407   -3.453  -56.884  1.00 74.65  ? 26  VAL E N   1 
ATOM   8007  C CA  . VAL E 1 19  ? 8.637   -4.122  -56.492  1.00 71.96  ? 26  VAL E CA  1 
ATOM   8008  C C   . VAL E 1 19  ? 9.582   -3.068  -55.926  1.00 71.82  ? 26  VAL E C   1 
ATOM   8009  O O   . VAL E 1 19  ? 9.373   -1.864  -56.079  1.00 75.74  ? 26  VAL E O   1 
ATOM   8010  C CB  . VAL E 1 19  ? 9.298   -4.877  -57.661  1.00 70.78  ? 26  VAL E CB  1 
ATOM   8011  C CG1 . VAL E 1 19  ? 8.306   -5.834  -58.309  1.00 82.18  ? 26  VAL E CG1 1 
ATOM   8012  C CG2 . VAL E 1 19  ? 9.851   -3.892  -58.681  1.00 69.27  ? 26  VAL E CG2 1 
ATOM   8013  N N   . ASP E 1 20  ? 10.628  -3.539  -55.257  1.00 70.29  ? 27  ASP E N   1 
ATOM   8014  C CA  . ASP E 1 20  ? 11.651  -2.672  -54.695  1.00 80.27  ? 27  ASP E CA  1 
ATOM   8015  C C   . ASP E 1 20  ? 13.004  -3.023  -55.294  1.00 76.36  ? 27  ASP E C   1 
ATOM   8016  O O   . ASP E 1 20  ? 13.293  -4.195  -55.558  1.00 75.67  ? 27  ASP E O   1 
ATOM   8017  C CB  . ASP E 1 20  ? 11.713  -2.790  -53.166  1.00 81.13  ? 27  ASP E CB  1 
ATOM   8018  C CG  . ASP E 1 20  ? 10.490  -2.207  -52.481  1.00 100.98 ? 27  ASP E CG  1 
ATOM   8019  O OD1 . ASP E 1 20  ? 9.417   -2.141  -53.116  1.00 104.55 ? 27  ASP E OD1 1 
ATOM   8020  O OD2 . ASP E 1 20  ? 10.606  -1.807  -51.303  1.00 89.67  ? 27  ASP E OD2 1 
ATOM   8021  N N   . THR E 1 21  ? 13.827  -2.005  -55.509  1.00 70.81  ? 28  THR E N   1 
ATOM   8022  C CA  . THR E 1 21  ? 15.185  -2.168  -55.998  1.00 81.97  ? 28  THR E CA  1 
ATOM   8023  C C   . THR E 1 21  ? 16.166  -1.760  -54.901  1.00 74.59  ? 28  THR E C   1 
ATOM   8024  O O   . THR E 1 21  ? 15.778  -1.278  -53.833  1.00 79.98  ? 28  THR E O   1 
ATOM   8025  C CB  . THR E 1 21  ? 15.408  -1.353  -57.273  1.00 86.24  ? 28  THR E CB  1 
ATOM   8026  O OG1 . THR E 1 21  ? 15.219  0.042   -56.991  1.00 78.09  ? 28  THR E OG1 1 
ATOM   8027  C CG2 . THR E 1 21  ? 14.435  -1.779  -58.358  1.00 70.51  ? 28  THR E CG2 1 
ATOM   8028  N N   . ILE E 1 22  ? 17.458  -1.959  -55.177  1.00 71.95  ? 29  ILE E N   1 
ATOM   8029  C CA  . ILE E 1 22  ? 18.490  -1.590  -54.218  1.00 69.03  ? 29  ILE E CA  1 
ATOM   8030  C C   . ILE E 1 22  ? 18.542  -0.083  -54.003  1.00 70.22  ? 29  ILE E C   1 
ATOM   8031  O O   . ILE E 1 22  ? 19.028  0.375   -52.961  1.00 85.06  ? 29  ILE E O   1 
ATOM   8032  C CB  . ILE E 1 22  ? 19.859  -2.132  -54.672  1.00 73.62  ? 29  ILE E CB  1 
ATOM   8033  C CG1 . ILE E 1 22  ? 20.835  -2.193  -53.495  1.00 78.38  ? 29  ILE E CG1 1 
ATOM   8034  C CG2 . ILE E 1 22  ? 20.429  -1.279  -55.795  1.00 77.53  ? 29  ILE E CG2 1 
ATOM   8035  C CD1 . ILE E 1 22  ? 20.456  -3.216  -52.449  1.00 77.78  ? 29  ILE E CD1 1 
ATOM   8036  N N   . MET E 1 23  ? 18.039  0.706   -54.959  1.00 88.41  ? 30  MET E N   1 
ATOM   8037  C CA  . MET E 1 23  ? 18.104  2.158   -54.886  1.00 85.13  ? 30  MET E CA  1 
ATOM   8038  C C   . MET E 1 23  ? 16.753  2.847   -54.778  1.00 87.58  ? 30  MET E C   1 
ATOM   8039  O O   . MET E 1 23  ? 16.716  4.021   -54.395  1.00 87.32  ? 30  MET E O   1 
ATOM   8040  C CB  . MET E 1 23  ? 18.846  2.729   -56.107  1.00 78.31  ? 30  MET E CB  1 
ATOM   8041  C CG  . MET E 1 23  ? 20.220  3.271   -55.758  1.00 77.51  ? 30  MET E CG  1 
ATOM   8042  S SD  . MET E 1 23  ? 21.164  3.884   -57.158  1.00 99.08  ? 30  MET E SD  1 
ATOM   8043  C CE  . MET E 1 23  ? 22.362  2.568   -57.321  1.00 82.84  ? 30  MET E CE  1 
ATOM   8044  N N   . GLU E 1 24  ? 15.655  2.166   -55.097  1.00 93.17  ? 31  GLU E N   1 
ATOM   8045  C CA  . GLU E 1 24  ? 14.326  2.756   -55.044  1.00 98.21  ? 31  GLU E CA  1 
ATOM   8046  C C   . GLU E 1 24  ? 13.380  1.816   -54.313  1.00 93.05  ? 31  GLU E C   1 
ATOM   8047  O O   . GLU E 1 24  ? 13.554  0.594   -54.329  1.00 90.97  ? 31  GLU E O   1 
ATOM   8048  C CB  . GLU E 1 24  ? 13.775  3.045   -56.449  1.00 92.99  ? 31  GLU E CB  1 
ATOM   8049  C CG  . GLU E 1 24  ? 14.831  3.370   -57.491  1.00 105.33 ? 31  GLU E CG  1 
ATOM   8050  C CD  . GLU E 1 24  ? 14.247  3.502   -58.882  1.00 114.27 ? 31  GLU E CD  1 
ATOM   8051  O OE1 . GLU E 1 24  ? 13.322  4.322   -59.063  1.00 102.68 ? 31  GLU E OE1 1 
ATOM   8052  O OE2 . GLU E 1 24  ? 14.708  2.779   -59.792  1.00 101.12 ? 31  GLU E OE2 1 
ATOM   8053  N N   . LYS E 1 25  ? 12.369  2.400   -53.675  1.00 85.03  ? 32  LYS E N   1 
ATOM   8054  C CA  . LYS E 1 25  ? 11.344  1.655   -52.964  1.00 89.49  ? 32  LYS E CA  1 
ATOM   8055  C C   . LYS E 1 25  ? 9.978   1.933   -53.577  1.00 89.12  ? 32  LYS E C   1 
ATOM   8056  O O   . LYS E 1 25  ? 9.701   3.046   -54.036  1.00 81.50  ? 32  LYS E O   1 
ATOM   8057  C CB  . LYS E 1 25  ? 11.323  2.014   -51.473  1.00 87.50  ? 32  LYS E CB  1 
ATOM   8058  C CG  . LYS E 1 25  ? 12.181  1.124   -50.588  1.00 104.99 ? 32  LYS E CG  1 
ATOM   8059  C CD  . LYS E 1 25  ? 12.142  1.609   -49.148  1.00 99.20  ? 32  LYS E CD  1 
ATOM   8060  C CE  . LYS E 1 25  ? 11.991  0.456   -48.172  1.00 107.37 ? 32  LYS E CE  1 
ATOM   8061  N NZ  . LYS E 1 25  ? 10.906  0.732   -47.190  1.00 93.76  ? 32  LYS E NZ  1 
ATOM   8062  N N   . ASN E 1 26  ? 9.128   0.904   -53.582  1.00 87.28  ? 33  ASN E N   1 
ATOM   8063  C CA  . ASN E 1 26  ? 7.752   0.999   -54.076  1.00 87.39  ? 33  ASN E CA  1 
ATOM   8064  C C   . ASN E 1 26  ? 7.713   1.494   -55.524  1.00 84.80  ? 33  ASN E C   1 
ATOM   8065  O O   . ASN E 1 26  ? 7.178   2.559   -55.837  1.00 79.84  ? 33  ASN E O   1 
ATOM   8066  C CB  . ASN E 1 26  ? 6.902   1.889   -53.161  1.00 81.23  ? 33  ASN E CB  1 
ATOM   8067  C CG  . ASN E 1 26  ? 6.528   1.201   -51.863  1.00 104.25 ? 33  ASN E CG  1 
ATOM   8068  O OD1 . ASN E 1 26  ? 7.056   0.139   -51.536  1.00 110.58 ? 33  ASN E OD1 1 
ATOM   8069  N ND2 . ASN E 1 26  ? 5.612   1.806   -51.116  1.00 94.53  ? 33  ASN E ND2 1 
ATOM   8070  N N   . VAL E 1 27  ? 8.293   0.690   -56.409  1.00 76.28  ? 34  VAL E N   1 
ATOM   8071  C CA  . VAL E 1 27  ? 8.320   0.976   -57.839  1.00 63.80  ? 34  VAL E CA  1 
ATOM   8072  C C   . VAL E 1 27  ? 7.227   0.155   -58.509  1.00 72.03  ? 34  VAL E C   1 
ATOM   8073  O O   . VAL E 1 27  ? 7.225   -1.079  -58.424  1.00 87.79  ? 34  VAL E O   1 
ATOM   8074  C CB  . VAL E 1 27  ? 9.696   0.664   -58.448  1.00 78.71  ? 34  VAL E CB  1 
ATOM   8075  C CG1 . VAL E 1 27  ? 9.620   0.674   -59.967  1.00 68.41  ? 34  VAL E CG1 1 
ATOM   8076  C CG2 . VAL E 1 27  ? 10.729  1.665   -57.960  1.00 84.35  ? 34  VAL E CG2 1 
ATOM   8077  N N   . THR E 1 28  ? 6.301   0.836   -59.180  1.00 70.91  ? 35  THR E N   1 
ATOM   8078  C CA  . THR E 1 28  ? 5.213   0.159   -59.871  1.00 66.36  ? 35  THR E CA  1 
ATOM   8079  C C   . THR E 1 28  ? 5.699   -0.405  -61.201  1.00 70.08  ? 35  THR E C   1 
ATOM   8080  O O   . THR E 1 28  ? 6.404   0.269   -61.957  1.00 77.90  ? 35  THR E O   1 
ATOM   8081  C CB  . THR E 1 28  ? 4.047   1.121   -60.105  1.00 68.09  ? 35  THR E CB  1 
ATOM   8082  O OG1 . THR E 1 28  ? 3.714   1.777   -58.875  1.00 78.29  ? 35  THR E OG1 1 
ATOM   8083  C CG2 . THR E 1 28  ? 2.826   0.367   -60.612  1.00 60.12  ? 35  THR E CG2 1 
ATOM   8084  N N   . VAL E 1 29  ? 5.320   -1.654  -61.481  1.00 68.63  ? 36  VAL E N   1 
ATOM   8085  C CA  . VAL E 1 29  ? 5.739   -2.348  -62.690  1.00 57.35  ? 36  VAL E CA  1 
ATOM   8086  C C   . VAL E 1 29  ? 4.519   -2.965  -63.362  1.00 69.82  ? 36  VAL E C   1 
ATOM   8087  O O   . VAL E 1 29  ? 3.454   -3.115  -62.760  1.00 75.17  ? 36  VAL E O   1 
ATOM   8088  C CB  . VAL E 1 29  ? 6.799   -3.436  -62.411  1.00 64.13  ? 36  VAL E CB  1 
ATOM   8089  C CG1 . VAL E 1 29  ? 8.004   -2.842  -61.693  1.00 69.89  ? 36  VAL E CG1 1 
ATOM   8090  C CG2 . VAL E 1 29  ? 6.192   -4.573  -61.605  1.00 77.44  ? 36  VAL E CG2 1 
ATOM   8091  N N   . THR E 1 30  ? 4.692   -3.322  -64.637  1.00 69.25  ? 37  THR E N   1 
ATOM   8092  C CA  . THR E 1 30  ? 3.606   -3.933  -65.395  1.00 76.28  ? 37  THR E CA  1 
ATOM   8093  C C   . THR E 1 30  ? 3.379   -5.389  -65.009  1.00 76.55  ? 37  THR E C   1 
ATOM   8094  O O   . THR E 1 30  ? 2.240   -5.867  -65.064  1.00 98.16  ? 37  THR E O   1 
ATOM   8095  C CB  . THR E 1 30  ? 3.885   -3.839  -66.897  1.00 72.05  ? 37  THR E CB  1 
ATOM   8096  O OG1 . THR E 1 30  ? 4.981   -4.697  -67.237  1.00 65.79  ? 37  THR E OG1 1 
ATOM   8097  C CG2 . THR E 1 30  ? 4.229   -2.410  -67.286  1.00 58.65  ? 37  THR E CG2 1 
ATOM   8098  N N   . HIS E 1 31  ? 4.433   -6.108  -64.631  1.00 81.47  ? 38  HIS E N   1 
ATOM   8099  C CA  . HIS E 1 31  ? 4.301   -7.506  -64.250  1.00 87.87  ? 38  HIS E CA  1 
ATOM   8100  C C   . HIS E 1 31  ? 5.376   -7.849  -63.231  1.00 89.47  ? 38  HIS E C   1 
ATOM   8101  O O   . HIS E 1 31  ? 6.499   -7.341  -63.306  1.00 78.80  ? 38  HIS E O   1 
ATOM   8102  C CB  . HIS E 1 31  ? 4.407   -8.432  -65.468  1.00 77.98  ? 38  HIS E CB  1 
ATOM   8103  C CG  . HIS E 1 31  ? 3.614   -9.695  -65.336  1.00 93.53  ? 38  HIS E CG  1 
ATOM   8104  N ND1 . HIS E 1 31  ? 3.607   -10.674 -66.306  1.00 109.30 ? 38  HIS E ND1 1 
ATOM   8105  C CD2 . HIS E 1 31  ? 2.797   -10.136 -64.351  1.00 95.73  ? 38  HIS E CD2 1 
ATOM   8106  C CE1 . HIS E 1 31  ? 2.822   -11.665 -65.923  1.00 110.38 ? 38  HIS E CE1 1 
ATOM   8107  N NE2 . HIS E 1 31  ? 2.318   -11.364 -64.740  1.00 109.21 ? 38  HIS E NE2 1 
ATOM   8108  N N   . ALA E 1 32  ? 5.025   -8.716  -62.284  1.00 92.72  ? 39  ALA E N   1 
ATOM   8109  C CA  . ALA E 1 32  ? 5.941   -9.113  -61.227  1.00 86.83  ? 39  ALA E CA  1 
ATOM   8110  C C   . ALA E 1 32  ? 5.647   -10.552 -60.830  1.00 75.69  ? 39  ALA E C   1 
ATOM   8111  O O   . ALA E 1 32  ? 4.551   -11.069 -61.062  1.00 84.08  ? 39  ALA E O   1 
ATOM   8112  C CB  . ALA E 1 32  ? 5.833   -8.179  -60.018  1.00 68.99  ? 39  ALA E CB  1 
ATOM   8113  N N   . GLN E 1 33  ? 6.644   -11.200 -60.229  1.00 72.52  ? 40  GLN E N   1 
ATOM   8114  C CA  . GLN E 1 33  ? 6.521   -12.590 -59.812  1.00 71.39  ? 40  GLN E CA  1 
ATOM   8115  C C   . GLN E 1 33  ? 7.093   -12.755 -58.414  1.00 81.90  ? 40  GLN E C   1 
ATOM   8116  O O   . GLN E 1 33  ? 8.244   -12.385 -58.161  1.00 72.60  ? 40  GLN E O   1 
ATOM   8117  C CB  . GLN E 1 33  ? 7.233   -13.530 -60.792  1.00 61.69  ? 40  GLN E CB  1 
ATOM   8118  C CG  . GLN E 1 33  ? 7.031   -15.008 -60.492  1.00 61.19  ? 40  GLN E CG  1 
ATOM   8119  C CD  . GLN E 1 33  ? 7.491   -15.902 -61.628  1.00 84.80  ? 40  GLN E CD  1 
ATOM   8120  O OE1 . GLN E 1 33  ? 7.699   -17.102 -61.444  1.00 96.37  ? 40  GLN E OE1 1 
ATOM   8121  N NE2 . GLN E 1 33  ? 7.645   -15.322 -62.813  1.00 86.62  ? 40  GLN E NE2 1 
ATOM   8122  N N   . ASP E 1 34  ? 6.287   -13.310 -57.513  1.00 72.72  ? 41  ASP E N   1 
ATOM   8123  C CA  . ASP E 1 34  ? 6.713   -13.577 -56.149  1.00 74.11  ? 41  ASP E CA  1 
ATOM   8124  C C   . ASP E 1 34  ? 7.349   -14.959 -56.071  1.00 78.89  ? 41  ASP E C   1 
ATOM   8125  O O   . ASP E 1 34  ? 6.839   -15.923 -56.648  1.00 67.20  ? 41  ASP E O   1 
ATOM   8126  C CB  . ASP E 1 34  ? 5.525   -13.483 -55.190  1.00 75.00  ? 41  ASP E CB  1 
ATOM   8127  C CG  . ASP E 1 34  ? 5.945   -13.258 -53.749  1.00 91.90  ? 41  ASP E CG  1 
ATOM   8128  O OD1 . ASP E 1 34  ? 7.077   -13.638 -53.385  1.00 93.11  ? 41  ASP E OD1 1 
ATOM   8129  O OD2 . ASP E 1 34  ? 5.138   -12.701 -52.975  1.00 92.18  ? 41  ASP E OD2 1 
ATOM   8130  N N   . ILE E 1 35  ? 8.470   -15.047 -55.361  1.00 65.03  ? 42  ILE E N   1 
ATOM   8131  C CA  . ILE E 1 35  ? 9.189   -16.303 -55.201  1.00 74.65  ? 42  ILE E CA  1 
ATOM   8132  C C   . ILE E 1 35  ? 9.156   -16.782 -53.750  1.00 67.70  ? 42  ILE E C   1 
ATOM   8133  O O   . ILE E 1 35  ? 9.958   -17.627 -53.357  1.00 66.03  ? 42  ILE E O   1 
ATOM   8134  C CB  . ILE E 1 35  ? 10.633  -16.190 -55.721  1.00 68.61  ? 42  ILE E CB  1 
ATOM   8135  C CG1 . ILE E 1 35  ? 11.400  -15.116 -54.947  1.00 61.29  ? 42  ILE E CG1 1 
ATOM   8136  C CG2 . ILE E 1 35  ? 10.638  -15.891 -57.214  1.00 59.62  ? 42  ILE E CG2 1 
ATOM   8137  C CD1 . ILE E 1 35  ? 12.821  -14.906 -55.426  1.00 54.48  ? 42  ILE E CD1 1 
ATOM   8138  N N   . LEU E 1 36  ? 8.234   -16.255 -52.949  1.00 63.36  ? 43  LEU E N   1 
ATOM   8139  C CA  . LEU E 1 36  ? 8.099   -16.621 -51.545  1.00 60.43  ? 43  LEU E CA  1 
ATOM   8140  C C   . LEU E 1 36  ? 6.791   -17.376 -51.355  1.00 70.43  ? 43  LEU E C   1 
ATOM   8141  O O   . LEU E 1 36  ? 5.721   -16.871 -51.712  1.00 74.17  ? 43  LEU E O   1 
ATOM   8142  C CB  . LEU E 1 36  ? 8.137   -15.381 -50.651  1.00 55.96  ? 43  LEU E CB  1 
ATOM   8143  C CG  . LEU E 1 36  ? 8.103   -15.632 -49.142  1.00 67.48  ? 43  LEU E CG  1 
ATOM   8144  C CD1 . LEU E 1 36  ? 9.338   -16.400 -48.704  1.00 65.07  ? 43  LEU E CD1 1 
ATOM   8145  C CD2 . LEU E 1 36  ? 7.978   -14.329 -48.365  1.00 61.66  ? 43  LEU E CD2 1 
ATOM   8146  N N   . GLU E 1 37  ? 6.879   -18.579 -50.792  1.00 62.52  ? 44  GLU E N   1 
ATOM   8147  C CA  . GLU E 1 37  ? 5.693   -19.370 -50.497  1.00 66.18  ? 44  GLU E CA  1 
ATOM   8148  C C   . GLU E 1 37  ? 5.115   -18.939 -49.155  1.00 63.28  ? 44  GLU E C   1 
ATOM   8149  O O   . GLU E 1 37  ? 5.823   -18.922 -48.143  1.00 77.41  ? 44  GLU E O   1 
ATOM   8150  C CB  . GLU E 1 37  ? 6.036   -20.859 -50.481  1.00 57.28  ? 44  GLU E CB  1 
ATOM   8151  C CG  . GLU E 1 37  ? 4.841   -21.761 -50.249  1.00 62.96  ? 44  GLU E CG  1 
ATOM   8152  C CD  . GLU E 1 37  ? 3.810   -21.656 -51.354  1.00 102.13 ? 44  GLU E CD  1 
ATOM   8153  O OE1 . GLU E 1 37  ? 4.210   -21.620 -52.537  1.00 123.39 ? 44  GLU E OE1 1 
ATOM   8154  O OE2 . GLU E 1 37  ? 2.602   -21.608 -51.040  1.00 99.56  ? 44  GLU E OE2 1 
ATOM   8155  N N   . LYS E 1 38  ? 3.826   -18.586 -49.146  1.00 64.60  ? 45  LYS E N   1 
ATOM   8156  C CA  . LYS E 1 38  ? 3.203   -18.004 -47.964  1.00 65.38  ? 45  LYS E CA  1 
ATOM   8157  C C   . LYS E 1 38  ? 1.895   -18.678 -47.563  1.00 68.34  ? 45  LYS E C   1 
ATOM   8158  O O   . LYS E 1 38  ? 1.215   -18.179 -46.659  1.00 64.36  ? 45  LYS E O   1 
ATOM   8159  C CB  . LYS E 1 38  ? 2.943   -16.506 -48.177  1.00 53.08  ? 45  LYS E CB  1 
ATOM   8160  C CG  . LYS E 1 38  ? 4.178   -15.680 -48.484  1.00 75.96  ? 45  LYS E CG  1 
ATOM   8161  C CD  . LYS E 1 38  ? 3.851   -14.194 -48.476  1.00 78.93  ? 45  LYS E CD  1 
ATOM   8162  C CE  . LYS E 1 38  ? 2.769   -13.853 -49.489  1.00 74.82  ? 45  LYS E CE  1 
ATOM   8163  N NZ  . LYS E 1 38  ? 3.213   -14.122 -50.885  1.00 76.13  ? 45  LYS E NZ  1 
ATOM   8164  N N   . THR E 1 39  ? 1.520   -19.788 -48.193  1.00 68.66  ? 46  THR E N   1 
ATOM   8165  C CA  . THR E 1 39  ? 0.215   -20.391 -47.957  1.00 75.42  ? 46  THR E CA  1 
ATOM   8166  C C   . THR E 1 39  ? 0.348   -21.878 -47.662  1.00 81.86  ? 46  THR E C   1 
ATOM   8167  O O   . THR E 1 39  ? 1.146   -22.579 -48.292  1.00 77.24  ? 46  THR E O   1 
ATOM   8168  C CB  . THR E 1 39  ? -0.719  -20.181 -49.158  1.00 70.96  ? 46  THR E CB  1 
ATOM   8169  O OG1 . THR E 1 39  ? -0.011  -20.454 -50.374  1.00 91.01  ? 46  THR E OG1 1 
ATOM   8170  C CG2 . THR E 1 39  ? -1.242  -18.751 -49.184  1.00 71.05  ? 46  THR E CG2 1 
ATOM   8171  N N   . HIS E 1 40  ? -0.444  -22.347 -46.699  1.00 74.06  ? 47  HIS E N   1 
ATOM   8172  C CA  . HIS E 1 40  ? -0.524  -23.755 -46.341  1.00 68.09  ? 47  HIS E CA  1 
ATOM   8173  C C   . HIS E 1 40  ? -1.985  -24.188 -46.359  1.00 76.94  ? 47  HIS E C   1 
ATOM   8174  O O   . HIS E 1 40  ? -2.897  -23.369 -46.215  1.00 71.04  ? 47  HIS E O   1 
ATOM   8175  C CB  . HIS E 1 40  ? 0.098   -24.024 -44.962  1.00 64.09  ? 47  HIS E CB  1 
ATOM   8176  C CG  . HIS E 1 40  ? -0.607  -23.337 -43.835  1.00 63.65  ? 47  HIS E CG  1 
ATOM   8177  N ND1 . HIS E 1 40  ? -1.663  -23.910 -43.159  1.00 78.79  ? 47  HIS E ND1 1 
ATOM   8178  C CD2 . HIS E 1 40  ? -0.411  -22.124 -43.267  1.00 65.48  ? 47  HIS E CD2 1 
ATOM   8179  C CE1 . HIS E 1 40  ? -2.086  -23.080 -42.222  1.00 86.37  ? 47  HIS E CE1 1 
ATOM   8180  N NE2 . HIS E 1 40  ? -1.343  -21.989 -42.267  1.00 66.03  ? 47  HIS E NE2 1 
ATOM   8181  N N   . ASN E 1 41  ? -2.201  -25.490 -46.544  1.00 81.17  ? 48  ASN E N   1 
ATOM   8182  C CA  . ASN E 1 41  ? -3.546  -26.033 -46.695  1.00 78.73  ? 48  ASN E CA  1 
ATOM   8183  C C   . ASN E 1 41  ? -4.204  -26.384 -45.367  1.00 81.60  ? 48  ASN E C   1 
ATOM   8184  O O   . ASN E 1 41  ? -5.358  -26.825 -45.362  1.00 93.41  ? 48  ASN E O   1 
ATOM   8185  C CB  . ASN E 1 41  ? -3.518  -27.269 -47.607  1.00 61.37  ? 48  ASN E CB  1 
ATOM   8186  C CG  . ASN E 1 41  ? -2.878  -28.477 -46.946  1.00 88.78  ? 48  ASN E CG  1 
ATOM   8187  O OD1 . ASN E 1 41  ? -2.101  -28.349 -45.999  1.00 84.59  ? 48  ASN E OD1 1 
ATOM   8188  N ND2 . ASN E 1 41  ? -3.197  -29.661 -47.454  1.00 90.15  ? 48  ASN E ND2 1 
ATOM   8189  N N   . GLY E 1 42  ? -3.501  -26.203 -44.251  1.00 77.92  ? 49  GLY E N   1 
ATOM   8190  C CA  . GLY E 1 42  ? -4.088  -26.423 -42.939  1.00 75.88  ? 49  GLY E CA  1 
ATOM   8191  C C   . GLY E 1 42  ? -4.493  -27.853 -42.661  1.00 82.30  ? 49  GLY E C   1 
ATOM   8192  O O   . GLY E 1 42  ? -5.449  -28.082 -41.914  1.00 73.69  ? 49  GLY E O   1 
ATOM   8193  N N   . LYS E 1 43  ? -3.784  -28.825 -43.234  1.00 82.14  ? 50  LYS E N   1 
ATOM   8194  C CA  . LYS E 1 43  ? -4.063  -30.235 -43.003  1.00 70.95  ? 50  LYS E CA  1 
ATOM   8195  C C   . LYS E 1 43  ? -2.752  -30.999 -42.892  1.00 77.88  ? 50  LYS E C   1 
ATOM   8196  O O   . LYS E 1 43  ? -1.711  -30.566 -43.392  1.00 80.38  ? 50  LYS E O   1 
ATOM   8197  C CB  . LYS E 1 43  ? -4.917  -30.847 -44.125  1.00 80.35  ? 50  LYS E CB  1 
ATOM   8198  C CG  . LYS E 1 43  ? -6.358  -30.382 -44.154  1.00 83.99  ? 50  LYS E CG  1 
ATOM   8199  C CD  . LYS E 1 43  ? -7.033  -30.605 -42.814  1.00 103.94 ? 50  LYS E CD  1 
ATOM   8200  C CE  . LYS E 1 43  ? -8.328  -31.383 -42.958  1.00 100.41 ? 50  LYS E CE  1 
ATOM   8201  N NZ  . LYS E 1 43  ? -9.371  -30.838 -42.042  1.00 102.03 ? 50  LYS E NZ  1 
ATOM   8202  N N   . LEU E 1 44  ? -2.817  -32.149 -42.226  1.00 69.54  ? 51  LEU E N   1 
ATOM   8203  C CA  . LEU E 1 44  ? -1.706  -33.092 -42.193  1.00 62.70  ? 51  LEU E CA  1 
ATOM   8204  C C   . LEU E 1 44  ? -1.891  -34.091 -43.328  1.00 53.79  ? 51  LEU E C   1 
ATOM   8205  O O   . LEU E 1 44  ? -2.882  -34.831 -43.352  1.00 62.26  ? 51  LEU E O   1 
ATOM   8206  C CB  . LEU E 1 44  ? -1.638  -33.809 -40.844  1.00 65.09  ? 51  LEU E CB  1 
ATOM   8207  C CG  . LEU E 1 44  ? -1.299  -32.973 -39.609  1.00 66.69  ? 51  LEU E CG  1 
ATOM   8208  C CD1 . LEU E 1 44  ? -1.261  -33.854 -38.372  1.00 55.63  ? 51  LEU E CD1 1 
ATOM   8209  C CD2 . LEU E 1 44  ? 0.026   -32.246 -39.787  1.00 71.41  ? 51  LEU E CD2 1 
ATOM   8210  N N   . CYS E 1 45  ? -0.948  -34.110 -44.264  1.00 58.60  ? 52  CYS E N   1 
ATOM   8211  C CA  . CYS E 1 45  ? -1.057  -34.935 -45.458  1.00 69.28  ? 52  CYS E CA  1 
ATOM   8212  C C   . CYS E 1 45  ? -0.046  -36.070 -45.422  1.00 64.01  ? 52  CYS E C   1 
ATOM   8213  O O   . CYS E 1 45  ? 0.784   -36.177 -44.516  1.00 63.94  ? 52  CYS E O   1 
ATOM   8214  C CB  . CYS E 1 45  ? -0.834  -34.094 -46.724  1.00 70.93  ? 52  CYS E CB  1 
ATOM   8215  S SG  . CYS E 1 45  ? -1.872  -32.629 -46.871  1.00 101.93 ? 52  CYS E SG  1 
ATOM   8216  N N   . ASP E 1 46  ? -0.139  -36.931 -46.430  1.00 66.09  ? 53  ASP E N   1 
ATOM   8217  C CA  . ASP E 1 46  ? 0.888   -37.935 -46.652  1.00 67.62  ? 53  ASP E CA  1 
ATOM   8218  C C   . ASP E 1 46  ? 2.175   -37.266 -47.121  1.00 63.03  ? 53  ASP E C   1 
ATOM   8219  O O   . ASP E 1 46  ? 2.154   -36.232 -47.794  1.00 70.76  ? 53  ASP E O   1 
ATOM   8220  C CB  . ASP E 1 46  ? 0.423   -38.960 -47.686  1.00 69.78  ? 53  ASP E CB  1 
ATOM   8221  C CG  . ASP E 1 46  ? -0.854  -39.668 -47.274  1.00 83.63  ? 53  ASP E CG  1 
ATOM   8222  O OD1 . ASP E 1 46  ? -1.332  -39.435 -46.143  1.00 83.56  ? 53  ASP E OD1 1 
ATOM   8223  O OD2 . ASP E 1 46  ? -1.379  -40.460 -48.085  1.00 88.75  ? 53  ASP E OD2 1 
ATOM   8224  N N   . LEU E 1 47  ? 3.303   -37.861 -46.754  1.00 66.06  ? 54  LEU E N   1 
ATOM   8225  C CA  . LEU E 1 47  ? 4.613   -37.359 -47.146  1.00 51.16  ? 54  LEU E CA  1 
ATOM   8226  C C   . LEU E 1 47  ? 5.170   -38.290 -48.214  1.00 63.41  ? 54  LEU E C   1 
ATOM   8227  O O   . LEU E 1 47  ? 5.584   -39.414 -47.910  1.00 59.63  ? 54  LEU E O   1 
ATOM   8228  C CB  . LEU E 1 47  ? 5.551   -37.265 -45.945  1.00 55.40  ? 54  LEU E CB  1 
ATOM   8229  C CG  . LEU E 1 47  ? 6.797   -36.404 -46.150  1.00 64.06  ? 54  LEU E CG  1 
ATOM   8230  C CD1 . LEU E 1 47  ? 6.412   -34.976 -46.514  1.00 64.28  ? 54  LEU E CD1 1 
ATOM   8231  C CD2 . LEU E 1 47  ? 7.671   -36.425 -44.907  1.00 63.83  ? 54  LEU E CD2 1 
ATOM   8232  N N   . ASN E 1 48  ? 5.175   -37.816 -49.462  1.00 74.11  ? 55  ASN E N   1 
ATOM   8233  C CA  . ASN E 1 48  ? 5.673   -38.587 -50.603  1.00 55.31  ? 55  ASN E CA  1 
ATOM   8234  C C   . ASN E 1 48  ? 4.930   -39.916 -50.743  1.00 63.64  ? 55  ASN E C   1 
ATOM   8235  O O   . ASN E 1 48  ? 5.524   -40.954 -51.041  1.00 53.14  ? 55  ASN E O   1 
ATOM   8236  C CB  . ASN E 1 48  ? 7.182   -38.816 -50.497  1.00 58.92  ? 55  ASN E CB  1 
ATOM   8237  C CG  . ASN E 1 48  ? 7.950   -37.530 -50.257  1.00 85.31  ? 55  ASN E CG  1 
ATOM   8238  O OD1 . ASN E 1 48  ? 7.616   -36.483 -50.811  1.00 81.26  ? 55  ASN E OD1 1 
ATOM   8239  N ND2 . ASN E 1 48  ? 8.984   -37.603 -49.425  1.00 87.06  ? 55  ASN E ND2 1 
ATOM   8240  N N   . GLY E 1 49  A 3.616   -39.882 -50.522  1.00 63.87  ? 55  GLY E N   1 
ATOM   8241  C CA  . GLY E 1 49  A 2.769   -41.036 -50.731  1.00 59.42  ? 55  GLY E CA  1 
ATOM   8242  C C   . GLY E 1 49  A 2.616   -41.975 -49.555  1.00 67.67  ? 55  GLY E C   1 
ATOM   8243  O O   . GLY E 1 49  A 1.982   -43.027 -49.707  1.00 72.47  ? 55  GLY E O   1 
ATOM   8244  N N   . VAL E 1 50  ? 3.163   -41.638 -48.390  1.00 70.59  ? 56  VAL E N   1 
ATOM   8245  C CA  . VAL E 1 50  ? 3.118   -42.504 -47.217  1.00 60.82  ? 56  VAL E CA  1 
ATOM   8246  C C   . VAL E 1 50  ? 2.362   -41.785 -46.110  1.00 72.95  ? 56  VAL E C   1 
ATOM   8247  O O   . VAL E 1 50  ? 2.668   -40.631 -45.788  1.00 69.07  ? 56  VAL E O   1 
ATOM   8248  C CB  . VAL E 1 50  ? 4.527   -42.905 -46.748  1.00 67.62  ? 56  VAL E CB  1 
ATOM   8249  C CG1 . VAL E 1 50  ? 4.439   -43.902 -45.612  1.00 61.44  ? 56  VAL E CG1 1 
ATOM   8250  C CG2 . VAL E 1 50  ? 5.323   -43.485 -47.910  1.00 47.10  ? 56  VAL E CG2 1 
ATOM   8251  N N   . LYS E 1 51  ? 1.374   -42.466 -45.537  1.00 63.40  ? 57  LYS E N   1 
ATOM   8252  C CA  . LYS E 1 51  ? 0.556   -41.875 -44.490  1.00 64.93  ? 57  LYS E CA  1 
ATOM   8253  C C   . LYS E 1 51  ? 1.373   -41.679 -43.215  1.00 74.26  ? 57  LYS E C   1 
ATOM   8254  O O   . LYS E 1 51  ? 2.235   -42.502 -42.895  1.00 65.71  ? 57  LYS E O   1 
ATOM   8255  C CB  . LYS E 1 51  ? -0.649  -42.764 -44.196  1.00 71.77  ? 57  LYS E CB  1 
ATOM   8256  C CG  . LYS E 1 51  ? -1.950  -42.264 -44.783  1.00 101.87 ? 57  LYS E CG  1 
ATOM   8257  C CD  . LYS E 1 51  ? -2.959  -43.390 -44.902  1.00 104.66 ? 57  LYS E CD  1 
ATOM   8258  C CE  . LYS E 1 51  ? -4.323  -42.868 -45.307  1.00 98.27  ? 57  LYS E CE  1 
ATOM   8259  N NZ  . LYS E 1 51  ? -5.398  -43.828 -44.944  1.00 97.13  ? 57  LYS E NZ  1 
ATOM   8260  N N   . PRO E 1 52  ? 1.134   -40.601 -42.475  1.00 60.60  ? 58  PRO E N   1 
ATOM   8261  C CA  . PRO E 1 52  ? 1.748   -40.466 -41.153  1.00 52.64  ? 58  PRO E CA  1 
ATOM   8262  C C   . PRO E 1 52  ? 1.083   -41.381 -40.137  1.00 59.11  ? 58  PRO E C   1 
ATOM   8263  O O   . PRO E 1 52  ? -0.050  -41.836 -40.307  1.00 63.33  ? 58  PRO E O   1 
ATOM   8264  C CB  . PRO E 1 52  ? 1.517   -38.993 -40.803  1.00 51.74  ? 58  PRO E CB  1 
ATOM   8265  C CG  . PRO E 1 52  ? 0.285   -38.628 -41.554  1.00 50.36  ? 58  PRO E CG  1 
ATOM   8266  C CD  . PRO E 1 52  ? 0.339   -39.415 -42.839  1.00 66.39  ? 58  PRO E CD  1 
ATOM   8267  N N   . LEU E 1 53  ? 1.818   -41.652 -39.062  1.00 61.90  ? 59  LEU E N   1 
ATOM   8268  C CA  . LEU E 1 53  ? 1.272   -42.355 -37.906  1.00 55.08  ? 59  LEU E CA  1 
ATOM   8269  C C   . LEU E 1 53  ? 0.780   -41.309 -36.913  1.00 50.49  ? 59  LEU E C   1 
ATOM   8270  O O   . LEU E 1 53  ? 1.581   -40.584 -36.314  1.00 61.67  ? 59  LEU E O   1 
ATOM   8271  C CB  . LEU E 1 53  ? 2.315   -43.274 -37.278  1.00 57.05  ? 59  LEU E CB  1 
ATOM   8272  C CG  . LEU E 1 53  ? 1.891   -43.966 -35.981  1.00 54.69  ? 59  LEU E CG  1 
ATOM   8273  C CD1 . LEU E 1 53  ? 0.595   -44.735 -36.180  1.00 53.26  ? 59  LEU E CD1 1 
ATOM   8274  C CD2 . LEU E 1 53  ? 2.991   -44.885 -35.476  1.00 64.75  ? 59  LEU E CD2 1 
ATOM   8275  N N   . ILE E 1 54  ? -0.534  -41.228 -36.741  1.00 54.75  ? 60  ILE E N   1 
ATOM   8276  C CA  . ILE E 1 54  ? -1.160  -40.216 -35.900  1.00 65.98  ? 60  ILE E CA  1 
ATOM   8277  C C   . ILE E 1 54  ? -1.646  -40.898 -34.631  1.00 60.36  ? 60  ILE E C   1 
ATOM   8278  O O   . ILE E 1 54  ? -2.627  -41.652 -34.651  1.00 67.59  ? 60  ILE E O   1 
ATOM   8279  C CB  . ILE E 1 54  ? -2.305  -39.502 -36.630  1.00 53.93  ? 60  ILE E CB  1 
ATOM   8280  C CG1 . ILE E 1 54  ? -1.743  -38.679 -37.792  1.00 62.32  ? 60  ILE E CG1 1 
ATOM   8281  C CG2 . ILE E 1 54  ? -3.095  -38.627 -35.662  1.00 50.18  ? 60  ILE E CG2 1 
ATOM   8282  C CD1 . ILE E 1 54  ? -2.754  -38.356 -38.865  1.00 53.68  ? 60  ILE E CD1 1 
ATOM   8283  N N   . LEU E 1 55  ? -0.954  -40.638 -33.525  1.00 66.04  ? 61  LEU E N   1 
ATOM   8284  C CA  . LEU E 1 55  ? -1.381  -41.084 -32.205  1.00 67.08  ? 61  LEU E CA  1 
ATOM   8285  C C   . LEU E 1 55  ? -2.291  -40.003 -31.633  1.00 70.57  ? 61  LEU E C   1 
ATOM   8286  O O   . LEU E 1 55  ? -1.837  -38.888 -31.357  1.00 82.71  ? 61  LEU E O   1 
ATOM   8287  C CB  . LEU E 1 55  ? -0.172  -41.332 -31.307  1.00 63.20  ? 61  LEU E CB  1 
ATOM   8288  C CG  . LEU E 1 55  ? 0.969   -42.142 -31.930  1.00 63.52  ? 61  LEU E CG  1 
ATOM   8289  C CD1 . LEU E 1 55  ? 2.248   -41.982 -31.124  1.00 70.52  ? 61  LEU E CD1 1 
ATOM   8290  C CD2 . LEU E 1 55  ? 0.588   -43.610 -32.045  1.00 54.21  ? 61  LEU E CD2 1 
ATOM   8291  N N   . LYS E 1 56  ? -3.573  -40.330 -31.458  1.00 75.79  ? 62  LYS E N   1 
ATOM   8292  C CA  . LYS E 1 56  ? -4.581  -39.322 -31.151  1.00 77.64  ? 62  LYS E CA  1 
ATOM   8293  C C   . LYS E 1 56  ? -4.279  -38.590 -29.850  1.00 80.32  ? 62  LYS E C   1 
ATOM   8294  O O   . LYS E 1 56  ? -3.937  -37.405 -29.872  1.00 87.85  ? 62  LYS E O   1 
ATOM   8295  C CB  . LYS E 1 56  ? -5.968  -39.970 -31.081  1.00 75.23  ? 62  LYS E CB  1 
ATOM   8296  C CG  . LYS E 1 56  ? -6.482  -40.497 -32.415  1.00 76.54  ? 62  LYS E CG  1 
ATOM   8297  C CD  . LYS E 1 56  ? -6.637  -39.379 -33.436  1.00 101.84 ? 62  LYS E CD  1 
ATOM   8298  C CE  . LYS E 1 56  ? -7.029  -39.930 -34.802  1.00 85.05  ? 62  LYS E CE  1 
ATOM   8299  N NZ  . LYS E 1 56  ? -8.462  -39.691 -35.137  1.00 91.22  ? 62  LYS E NZ  1 
ATOM   8300  N N   . ASP E 1 57  ? -4.357  -39.283 -28.713  1.00 81.24  ? 63  ASP E N   1 
ATOM   8301  C CA  . ASP E 1 57  ? -4.007  -38.669 -27.437  1.00 81.38  ? 63  ASP E CA  1 
ATOM   8302  C C   . ASP E 1 57  ? -3.004  -39.516 -26.665  1.00 71.97  ? 63  ASP E C   1 
ATOM   8303  O O   . ASP E 1 57  ? -2.869  -39.354 -25.449  1.00 76.59  ? 63  ASP E O   1 
ATOM   8304  C CB  . ASP E 1 57  ? -5.249  -38.415 -26.579  1.00 93.72  ? 63  ASP E CB  1 
ATOM   8305  C CG  . ASP E 1 57  ? -5.147  -37.127 -25.777  1.00 113.27 ? 63  ASP E CG  1 
ATOM   8306  O OD1 . ASP E 1 57  ? -6.188  -36.641 -25.284  1.00 121.37 ? 63  ASP E OD1 1 
ATOM   8307  O OD2 . ASP E 1 57  ? -4.025  -36.587 -25.659  1.00 107.22 ? 63  ASP E OD2 1 
ATOM   8308  N N   . CYS E 1 58  ? -2.299  -40.410 -27.348  1.00 78.36  ? 64  CYS E N   1 
ATOM   8309  C CA  . CYS E 1 58  ? -1.307  -41.270 -26.726  1.00 71.21  ? 64  CYS E CA  1 
ATOM   8310  C C   . CYS E 1 58  ? 0.093   -40.860 -27.159  1.00 58.45  ? 64  CYS E C   1 
ATOM   8311  O O   . CYS E 1 58  ? 0.286   -40.188 -28.177  1.00 64.97  ? 64  CYS E O   1 
ATOM   8312  C CB  . CYS E 1 58  ? -1.560  -42.742 -27.075  1.00 53.53  ? 64  CYS E CB  1 
ATOM   8313  S SG  . CYS E 1 58  ? -3.016  -43.406 -26.245  1.00 124.15 ? 64  CYS E SG  1 
ATOM   8314  N N   . SER E 1 59  ? 1.066   -41.263 -26.356  1.00 58.65  ? 65  SER E N   1 
ATOM   8315  C CA  . SER E 1 59  ? 2.471   -41.071 -26.671  1.00 52.05  ? 65  SER E CA  1 
ATOM   8316  C C   . SER E 1 59  ? 3.055   -42.367 -27.220  1.00 52.09  ? 65  SER E C   1 
ATOM   8317  O O   . SER E 1 59  ? 2.418   -43.423 -27.210  1.00 52.32  ? 65  SER E O   1 
ATOM   8318  C CB  . SER E 1 59  ? 3.244   -40.613 -25.433  1.00 65.95  ? 65  SER E CB  1 
ATOM   8319  O OG  . SER E 1 59  ? 3.256   -41.627 -24.445  1.00 54.60  ? 65  SER E OG  1 
ATOM   8320  N N   . VAL E 1 60  ? 4.288   -42.269 -27.715  1.00 51.36  ? 66  VAL E N   1 
ATOM   8321  C CA  . VAL E 1 60  ? 4.958   -43.441 -28.267  1.00 54.21  ? 66  VAL E CA  1 
ATOM   8322  C C   . VAL E 1 60  ? 5.109   -44.519 -27.201  1.00 56.22  ? 66  VAL E C   1 
ATOM   8323  O O   . VAL E 1 60  ? 4.921   -45.711 -27.472  1.00 58.23  ? 66  VAL E O   1 
ATOM   8324  C CB  . VAL E 1 60  ? 6.317   -43.042 -28.873  1.00 58.89  ? 66  VAL E CB  1 
ATOM   8325  C CG1 . VAL E 1 60  ? 6.990   -44.247 -29.511  1.00 52.54  ? 66  VAL E CG1 1 
ATOM   8326  C CG2 . VAL E 1 60  ? 6.133   -41.926 -29.889  1.00 54.91  ? 66  VAL E CG2 1 
ATOM   8327  N N   . ALA E 1 61  ? 5.447   -44.117 -25.973  1.00 51.91  ? 67  ALA E N   1 
ATOM   8328  C CA  . ALA E 1 61  ? 5.633   -45.083 -24.894  1.00 51.37  ? 67  ALA E CA  1 
ATOM   8329  C C   . ALA E 1 61  ? 4.333   -45.814 -24.575  1.00 60.26  ? 67  ALA E C   1 
ATOM   8330  O O   . ALA E 1 61  ? 4.298   -47.049 -24.526  1.00 60.29  ? 67  ALA E O   1 
ATOM   8331  C CB  . ALA E 1 61  ? 6.177   -44.379 -23.651  1.00 48.41  ? 67  ALA E CB  1 
ATOM   8332  N N   . GLY E 1 62  ? 3.250   -45.066 -24.356  1.00 56.98  ? 68  GLY E N   1 
ATOM   8333  C CA  . GLY E 1 62  ? 1.977   -45.700 -24.051  1.00 40.03  ? 68  GLY E CA  1 
ATOM   8334  C C   . GLY E 1 62  ? 1.458   -46.547 -25.196  1.00 56.21  ? 68  GLY E C   1 
ATOM   8335  O O   . GLY E 1 62  ? 0.891   -47.621 -24.980  1.00 63.27  ? 68  GLY E O   1 
ATOM   8336  N N   . TRP E 1 63  ? 1.639   -46.071 -26.429  1.00 56.75  ? 69  TRP E N   1 
ATOM   8337  C CA  . TRP E 1 63  ? 1.219   -46.842 -27.595  1.00 48.37  ? 69  TRP E CA  1 
ATOM   8338  C C   . TRP E 1 63  ? 1.995   -48.150 -27.707  1.00 52.88  ? 69  TRP E C   1 
ATOM   8339  O O   . TRP E 1 63  ? 1.413   -49.204 -27.990  1.00 49.50  ? 69  TRP E O   1 
ATOM   8340  C CB  . TRP E 1 63  ? 1.386   -45.994 -28.856  1.00 58.72  ? 69  TRP E CB  1 
ATOM   8341  C CG  . TRP E 1 63  ? 1.294   -46.761 -30.135  1.00 55.33  ? 69  TRP E CG  1 
ATOM   8342  C CD1 . TRP E 1 63  ? 0.201   -47.411 -30.626  1.00 80.75  ? 69  TRP E CD1 1 
ATOM   8343  C CD2 . TRP E 1 63  ? 2.336   -46.937 -31.102  1.00 64.64  ? 69  TRP E CD2 1 
ATOM   8344  N NE1 . TRP E 1 63  ? 0.502   -47.993 -31.833  1.00 80.19  ? 69  TRP E NE1 1 
ATOM   8345  C CE2 . TRP E 1 63  ? 1.805   -47.716 -32.149  1.00 62.04  ? 69  TRP E CE2 1 
ATOM   8346  C CE3 . TRP E 1 63  ? 3.667   -46.518 -31.182  1.00 67.88  ? 69  TRP E CE3 1 
ATOM   8347  C CZ2 . TRP E 1 63  ? 2.558   -48.084 -33.262  1.00 74.58  ? 69  TRP E CZ2 1 
ATOM   8348  C CZ3 . TRP E 1 63  ? 4.413   -46.884 -32.288  1.00 71.90  ? 69  TRP E CZ3 1 
ATOM   8349  C CH2 . TRP E 1 63  ? 3.857   -47.659 -33.313  1.00 70.94  ? 69  TRP E CH2 1 
ATOM   8350  N N   . LEU E 1 64  ? 3.312   -48.105 -27.488  1.00 53.17  ? 70  LEU E N   1 
ATOM   8351  C CA  . LEU E 1 64  ? 4.128   -49.310 -27.619  1.00 52.85  ? 70  LEU E CA  1 
ATOM   8352  C C   . LEU E 1 64  ? 3.791   -50.334 -26.540  1.00 55.37  ? 70  LEU E C   1 
ATOM   8353  O O   . LEU E 1 64  ? 3.564   -51.513 -26.837  1.00 57.08  ? 70  LEU E O   1 
ATOM   8354  C CB  . LEU E 1 64  ? 5.612   -48.947 -27.561  1.00 51.94  ? 70  LEU E CB  1 
ATOM   8355  C CG  . LEU E 1 64  ? 6.245   -48.364 -28.822  1.00 56.11  ? 70  LEU E CG  1 
ATOM   8356  C CD1 . LEU E 1 64  ? 7.749   -48.276 -28.640  1.00 56.41  ? 70  LEU E CD1 1 
ATOM   8357  C CD2 . LEU E 1 64  ? 5.895   -49.208 -30.037  1.00 61.05  ? 70  LEU E CD2 1 
ATOM   8358  N N   . LEU E 1 65  ? 3.757   -49.901 -25.279  1.00 49.47  ? 71  LEU E N   1 
ATOM   8359  C CA  . LEU E 1 65  ? 3.517   -50.813 -24.169  1.00 46.80  ? 71  LEU E CA  1 
ATOM   8360  C C   . LEU E 1 65  ? 2.072   -51.280 -24.083  1.00 55.49  ? 71  LEU E C   1 
ATOM   8361  O O   . LEU E 1 65  ? 1.795   -52.256 -23.377  1.00 49.62  ? 71  LEU E O   1 
ATOM   8362  C CB  . LEU E 1 65  ? 3.927   -50.155 -22.852  1.00 47.36  ? 71  LEU E CB  1 
ATOM   8363  C CG  . LEU E 1 65  ? 5.441   -50.113 -22.638  1.00 49.55  ? 71  LEU E CG  1 
ATOM   8364  C CD1 . LEU E 1 65  ? 5.785   -49.324 -21.398  1.00 43.44  ? 71  LEU E CD1 1 
ATOM   8365  C CD2 . LEU E 1 65  ? 5.989   -51.527 -22.544  1.00 44.42  ? 71  LEU E CD2 1 
ATOM   8366  N N   . GLY E 1 66  ? 1.150   -50.623 -24.780  1.00 46.10  ? 72  GLY E N   1 
ATOM   8367  C CA  . GLY E 1 66  ? -0.229  -51.070 -24.771  1.00 50.80  ? 72  GLY E CA  1 
ATOM   8368  C C   . GLY E 1 66  ? -1.035  -50.526 -23.611  1.00 53.59  ? 72  GLY E C   1 
ATOM   8369  O O   . GLY E 1 66  ? -1.749  -51.279 -22.942  1.00 47.29  ? 72  GLY E O   1 
ATOM   8370  N N   . ASN E 1 67  ? -0.920  -49.225 -23.363  1.00 54.79  ? 73  ASN E N   1 
ATOM   8371  C CA  . ASN E 1 67  ? -1.756  -48.559 -22.382  1.00 50.07  ? 73  ASN E CA  1 
ATOM   8372  C C   . ASN E 1 67  ? -3.218  -48.818 -22.734  1.00 61.99  ? 73  ASN E C   1 
ATOM   8373  O O   . ASN E 1 67  ? -3.632  -48.538 -23.868  1.00 58.95  ? 73  ASN E O   1 
ATOM   8374  C CB  . ASN E 1 67  ? -1.457  -47.057 -22.369  1.00 49.03  ? 73  ASN E CB  1 
ATOM   8375  C CG  . ASN E 1 67  ? -2.226  -46.296 -21.291  1.00 52.05  ? 73  ASN E CG  1 
ATOM   8376  O OD1 . ASN E 1 67  ? -3.413  -46.528 -21.065  1.00 67.32  ? 73  ASN E OD1 1 
ATOM   8377  N ND2 . ASN E 1 67  ? -1.544  -45.366 -20.632  1.00 47.10  ? 73  ASN E ND2 1 
ATOM   8378  N N   . PRO E 1 68  ? -4.021  -49.356 -21.810  1.00 67.60  ? 74  PRO E N   1 
ATOM   8379  C CA  . PRO E 1 68  ? -5.408  -49.712 -22.154  1.00 63.48  ? 74  PRO E CA  1 
ATOM   8380  C C   . PRO E 1 68  ? -6.259  -48.520 -22.546  1.00 63.99  ? 74  PRO E C   1 
ATOM   8381  O O   . PRO E 1 68  ? -7.346  -48.717 -23.104  1.00 69.71  ? 74  PRO E O   1 
ATOM   8382  C CB  . PRO E 1 68  ? -5.932  -50.382 -20.875  1.00 55.06  ? 74  PRO E CB  1 
ATOM   8383  C CG  . PRO E 1 68  ? -5.052  -49.870 -19.788  1.00 67.00  ? 74  PRO E CG  1 
ATOM   8384  C CD  . PRO E 1 68  ? -3.699  -49.673 -20.409  1.00 62.36  ? 74  PRO E CD  1 
ATOM   8385  N N   . MET E 1 69  ? -5.805  -47.299 -22.275  1.00 55.14  ? 75  MET E N   1 
ATOM   8386  C CA  . MET E 1 69  ? -6.470  -46.102 -22.769  1.00 70.01  ? 75  MET E CA  1 
ATOM   8387  C C   . MET E 1 69  ? -6.055  -45.747 -24.192  1.00 80.38  ? 75  MET E C   1 
ATOM   8388  O O   . MET E 1 69  ? -6.564  -44.766 -24.744  1.00 80.14  ? 75  MET E O   1 
ATOM   8389  C CB  . MET E 1 69  ? -6.190  -44.925 -21.831  1.00 61.25  ? 75  MET E CB  1 
ATOM   8390  C CG  . MET E 1 69  ? -6.918  -45.004 -20.493  1.00 84.22  ? 75  MET E CG  1 
ATOM   8391  S SD  . MET E 1 69  ? -8.705  -44.806 -20.648  1.00 91.73  ? 75  MET E SD  1 
ATOM   8392  C CE  . MET E 1 69  ? -9.280  -46.457 -20.257  1.00 72.17  ? 75  MET E CE  1 
ATOM   8393  N N   . CYS E 1 70  ? -5.150  -46.514 -24.792  1.00 90.95  ? 76  CYS E N   1 
ATOM   8394  C CA  . CYS E 1 70  ? -4.781  -46.351 -26.190  1.00 91.46  ? 76  CYS E CA  1 
ATOM   8395  C C   . CYS E 1 70  ? -5.436  -47.439 -27.028  1.00 101.57 ? 76  CYS E C   1 
ATOM   8396  O O   . CYS E 1 70  ? -5.525  -48.596 -26.605  1.00 111.27 ? 76  CYS E O   1 
ATOM   8397  C CB  . CYS E 1 70  ? -3.262  -46.403 -26.371  1.00 72.65  ? 76  CYS E CB  1 
ATOM   8398  S SG  . CYS E 1 70  ? -2.393  -45.153 -25.417  1.00 92.54  ? 76  CYS E SG  1 
ATOM   8399  N N   . ASP E 1 71  ? -5.907  -47.054 -28.212  1.00 109.29 ? 77  ASP E N   1 
ATOM   8400  C CA  . ASP E 1 71  ? -6.407  -48.026 -29.174  1.00 131.95 ? 77  ASP E CA  1 
ATOM   8401  C C   . ASP E 1 71  ? -5.313  -49.036 -29.490  1.00 137.97 ? 77  ASP E C   1 
ATOM   8402  O O   . ASP E 1 71  ? -4.247  -48.672 -29.997  1.00 119.04 ? 77  ASP E O   1 
ATOM   8403  C CB  . ASP E 1 71  ? -6.870  -47.310 -30.445  1.00 138.51 ? 77  ASP E CB  1 
ATOM   8404  C CG  . ASP E 1 71  ? -7.595  -48.233 -31.417  1.00 148.29 ? 77  ASP E CG  1 
ATOM   8405  O OD1 . ASP E 1 71  ? -7.270  -49.436 -31.472  1.00 148.81 ? 77  ASP E OD1 1 
ATOM   8406  O OD2 . ASP E 1 71  ? -8.495  -47.750 -32.137  1.00 146.08 ? 77  ASP E OD2 1 
ATOM   8407  N N   . GLU E 1 72  ? -5.572  -50.305 -29.179  1.00 146.01 ? 78  GLU E N   1 
ATOM   8408  C CA  . GLU E 1 72  ? -4.626  -51.375 -29.463  1.00 140.10 ? 78  GLU E CA  1 
ATOM   8409  C C   . GLU E 1 72  ? -4.828  -52.002 -30.835  1.00 140.47 ? 78  GLU E C   1 
ATOM   8410  O O   . GLU E 1 72  ? -3.991  -52.805 -31.259  1.00 128.04 ? 78  GLU E O   1 
ATOM   8411  C CB  . GLU E 1 72  ? -4.715  -52.460 -28.384  1.00 138.04 ? 78  GLU E CB  1 
ATOM   8412  C CG  . GLU E 1 72  ? -3.689  -52.306 -27.273  1.00 116.59 ? 78  GLU E CG  1 
ATOM   8413  C CD  . GLU E 1 72  ? -2.363  -52.964 -27.611  1.00 129.60 ? 78  GLU E CD  1 
ATOM   8414  O OE1 . GLU E 1 72  ? -2.266  -54.203 -27.487  1.00 109.18 ? 78  GLU E OE1 1 
ATOM   8415  O OE2 . GLU E 1 72  ? -1.423  -52.246 -28.017  1.00 107.16 ? 78  GLU E OE2 1 
ATOM   8416  N N   . PHE E 1 73  ? -5.909  -51.653 -31.537  1.00 159.70 ? 79  PHE E N   1 
ATOM   8417  C CA  . PHE E 1 73  ? -6.151  -52.123 -32.896  1.00 161.76 ? 79  PHE E CA  1 
ATOM   8418  C C   . PHE E 1 73  ? -5.585  -51.176 -33.945  1.00 151.53 ? 79  PHE E C   1 
ATOM   8419  O O   . PHE E 1 73  ? -6.072  -51.147 -35.084  1.00 143.81 ? 79  PHE E O   1 
ATOM   8420  C CB  . PHE E 1 73  ? -7.649  -52.330 -33.121  1.00 156.44 ? 79  PHE E CB  1 
ATOM   8421  C CG  . PHE E 1 73  ? -8.269  -53.336 -32.195  1.00 158.13 ? 79  PHE E CG  1 
ATOM   8422  C CD1 . PHE E 1 73  ? -7.526  -54.398 -31.702  1.00 145.96 ? 79  PHE E CD1 1 
ATOM   8423  C CD2 . PHE E 1 73  ? -9.596  -53.220 -31.817  1.00 155.44 ? 79  PHE E CD2 1 
ATOM   8424  C CE1 . PHE E 1 73  ? -8.096  -55.324 -30.850  1.00 132.40 ? 79  PHE E CE1 1 
ATOM   8425  C CE2 . PHE E 1 73  ? -10.173 -54.142 -30.965  1.00 138.86 ? 79  PHE E CE2 1 
ATOM   8426  C CZ  . PHE E 1 73  ? -9.422  -55.196 -30.481  1.00 132.20 ? 79  PHE E CZ  1 
ATOM   8427  N N   . ILE E 1 74  ? -4.566  -50.401 -33.588  1.00 149.38 ? 80  ILE E N   1 
ATOM   8428  C CA  . ILE E 1 74  ? -3.974  -49.425 -34.495  1.00 139.98 ? 80  ILE E CA  1 
ATOM   8429  C C   . ILE E 1 74  ? -3.074  -50.167 -35.477  1.00 123.51 ? 80  ILE E C   1 
ATOM   8430  O O   . ILE E 1 74  ? -2.074  -50.779 -35.087  1.00 127.78 ? 80  ILE E O   1 
ATOM   8431  C CB  . ILE E 1 74  ? -3.211  -48.347 -33.712  1.00 127.21 ? 80  ILE E CB  1 
ATOM   8432  C CG1 . ILE E 1 74  ? -2.354  -47.484 -34.640  1.00 114.03 ? 80  ILE E CG1 1 
ATOM   8433  C CG2 . ILE E 1 74  ? -2.397  -48.974 -32.586  1.00 120.66 ? 80  ILE E CG2 1 
ATOM   8434  C CD1 . ILE E 1 74  ? -1.840  -46.223 -33.972  1.00 82.50  ? 80  ILE E CD1 1 
ATOM   8435  N N   . ARG E 1 75  ? -3.433  -50.113 -36.759  1.00 116.85 ? 81  ARG E N   1 
ATOM   8436  C CA  . ARG E 1 75  ? -2.944  -51.025 -37.791  1.00 115.80 ? 81  ARG E CA  1 
ATOM   8437  C C   . ARG E 1 75  ? -2.354  -50.242 -38.964  1.00 109.50 ? 81  ARG E C   1 
ATOM   8438  O O   . ARG E 1 75  ? -2.715  -50.434 -40.127  1.00 111.93 ? 81  ARG E O   1 
ATOM   8439  C CB  . ARG E 1 75  ? -4.077  -51.958 -38.225  1.00 120.17 ? 81  ARG E CB  1 
ATOM   8440  C CG  . ARG E 1 75  ? -3.722  -53.056 -39.237  1.00 136.22 ? 81  ARG E CG  1 
ATOM   8441  C CD  . ARG E 1 75  ? -2.632  -54.000 -38.755  1.00 133.49 ? 81  ARG E CD  1 
ATOM   8442  N NE  . ARG E 1 75  ? -2.433  -55.092 -39.702  1.00 157.74 ? 81  ARG E NE  1 
ATOM   8443  C CZ  . ARG E 1 75  ? -1.673  -55.017 -40.787  1.00 149.11 ? 81  ARG E CZ  1 
ATOM   8444  N NH1 . ARG E 1 75  ? -0.997  -53.920 -41.082  1.00 130.49 ? 81  ARG E NH1 1 
ATOM   8445  N NH2 . ARG E 1 75  ? -1.592  -56.069 -41.598  1.00 155.15 ? 81  ARG E NH2 1 
ATOM   8446  N N   . VAL E 1 76  ? -1.457  -49.308 -38.664  1.00 95.10  ? 82  VAL E N   1 
ATOM   8447  C CA  . VAL E 1 76  ? -0.694  -48.631 -39.709  1.00 79.56  ? 82  VAL E CA  1 
ATOM   8448  C C   . VAL E 1 76  ? 0.619   -49.386 -39.890  1.00 75.75  ? 82  VAL E C   1 
ATOM   8449  O O   . VAL E 1 76  ? 1.550   -49.205 -39.093  1.00 85.85  ? 82  VAL E O   1 
ATOM   8450  C CB  . VAL E 1 76  ? -0.453  -47.154 -39.365  1.00 73.66  ? 82  VAL E CB  1 
ATOM   8451  C CG1 . VAL E 1 76  ? 0.011   -46.391 -40.597  1.00 70.98  ? 82  VAL E CG1 1 
ATOM   8452  C CG2 . VAL E 1 76  ? -1.713  -46.528 -38.785  1.00 95.48  ? 82  VAL E CG2 1 
ATOM   8453  N N   . PRO E 1 77  ? 0.742   -50.239 -40.912  1.00 67.77  ? 83  PRO E N   1 
ATOM   8454  C CA  . PRO E 1 77  ? 1.949   -51.067 -41.048  1.00 62.50  ? 83  PRO E CA  1 
ATOM   8455  C C   . PRO E 1 77  ? 3.168   -50.313 -41.549  1.00 63.93  ? 83  PRO E C   1 
ATOM   8456  O O   . PRO E 1 77  ? 4.263   -50.893 -41.579  1.00 68.16  ? 83  PRO E O   1 
ATOM   8457  C CB  . PRO E 1 77  ? 1.517   -52.134 -42.061  1.00 59.34  ? 83  PRO E CB  1 
ATOM   8458  C CG  . PRO E 1 77  ? 0.519   -51.430 -42.914  1.00 48.65  ? 83  PRO E CG  1 
ATOM   8459  C CD  . PRO E 1 77  ? -0.209  -50.461 -42.016  1.00 61.70  ? 83  PRO E CD  1 
ATOM   8460  N N   . GLU E 1 78  A 3.014   -49.052 -41.944  1.00 60.72  ? 83  GLU E N   1 
ATOM   8461  C CA  . GLU E 1 78  A 4.099   -48.271 -42.519  1.00 62.52  ? 83  GLU E CA  1 
ATOM   8462  C C   . GLU E 1 78  A 3.735   -46.801 -42.405  1.00 66.59  ? 83  GLU E C   1 
ATOM   8463  O O   . GLU E 1 78  A 2.571   -46.433 -42.586  1.00 56.14  ? 83  GLU E O   1 
ATOM   8464  C CB  . GLU E 1 78  A 4.337   -48.659 -43.984  1.00 63.97  ? 83  GLU E CB  1 
ATOM   8465  C CG  . GLU E 1 78  A 5.146   -47.654 -44.785  1.00 90.88  ? 83  GLU E CG  1 
ATOM   8466  C CD  . GLU E 1 78  A 5.318   -48.068 -46.230  1.00 98.80  ? 83  GLU E CD  1 
ATOM   8467  O OE1 . GLU E 1 78  A 4.433   -48.778 -46.753  1.00 110.07 ? 83  GLU E OE1 1 
ATOM   8468  O OE2 . GLU E 1 78  A 6.337   -47.685 -46.841  1.00 104.54 ? 83  GLU E OE2 1 
ATOM   8469  N N   . TRP E 1 79  ? 4.728   -45.966 -42.108  1.00 50.20  ? 84  TRP E N   1 
ATOM   8470  C CA  . TRP E 1 79  ? 4.482   -44.535 -42.022  1.00 51.71  ? 84  TRP E CA  1 
ATOM   8471  C C   . TRP E 1 79  ? 5.762   -43.772 -42.325  1.00 51.17  ? 84  TRP E C   1 
ATOM   8472  O O   . TRP E 1 79  ? 6.866   -44.322 -42.287  1.00 53.79  ? 84  TRP E O   1 
ATOM   8473  C CB  . TRP E 1 79  ? 3.926   -44.135 -40.649  1.00 61.41  ? 84  TRP E CB  1 
ATOM   8474  C CG  . TRP E 1 79  ? 4.821   -44.462 -39.497  1.00 58.05  ? 84  TRP E CG  1 
ATOM   8475  C CD1 . TRP E 1 79  ? 5.782   -43.662 -38.953  1.00 57.01  ? 84  TRP E CD1 1 
ATOM   8476  C CD2 . TRP E 1 79  ? 4.827   -45.673 -38.734  1.00 55.50  ? 84  TRP E CD2 1 
ATOM   8477  N NE1 . TRP E 1 79  ? 6.393   -44.304 -37.903  1.00 55.30  ? 84  TRP E NE1 1 
ATOM   8478  C CE2 . TRP E 1 79  ? 5.824   -45.540 -37.747  1.00 56.29  ? 84  TRP E CE2 1 
ATOM   8479  C CE3 . TRP E 1 79  ? 4.089   -46.859 -38.792  1.00 52.78  ? 84  TRP E CE3 1 
ATOM   8480  C CZ2 . TRP E 1 79  ? 6.099   -46.546 -36.825  1.00 54.85  ? 84  TRP E CZ2 1 
ATOM   8481  C CZ3 . TRP E 1 79  ? 4.365   -47.858 -37.876  1.00 57.78  ? 84  TRP E CZ3 1 
ATOM   8482  C CH2 . TRP E 1 79  ? 5.363   -47.696 -36.907  1.00 50.32  ? 84  TRP E CH2 1 
ATOM   8483  N N   . SER E 1 80  ? 5.590   -42.487 -42.636  1.00 56.56  ? 85  SER E N   1 
ATOM   8484  C CA  . SER E 1 80  ? 6.699   -41.598 -42.960  1.00 53.85  ? 85  SER E CA  1 
ATOM   8485  C C   . SER E 1 80  ? 7.091   -40.686 -41.808  1.00 60.50  ? 85  SER E C   1 
ATOM   8486  O O   . SER E 1 80  ? 8.266   -40.327 -41.691  1.00 74.23  ? 85  SER E O   1 
ATOM   8487  C CB  . SER E 1 80  ? 6.350   -40.744 -44.185  1.00 58.58  ? 85  SER E CB  1 
ATOM   8488  O OG  . SER E 1 80  ? 5.085   -40.125 -44.031  1.00 58.93  ? 85  SER E OG  1 
ATOM   8489  N N   . TYR E 1 81  ? 6.138   -40.301 -40.963  1.00 50.89  ? 86  TYR E N   1 
ATOM   8490  C CA  . TYR E 1 81  ? 6.435   -39.528 -39.765  1.00 58.32  ? 86  TYR E CA  1 
ATOM   8491  C C   . TYR E 1 81  ? 5.321   -39.758 -38.754  1.00 64.84  ? 86  TYR E C   1 
ATOM   8492  O O   . TYR E 1 81  ? 4.221   -40.192 -39.105  1.00 65.01  ? 86  TYR E O   1 
ATOM   8493  C CB  . TYR E 1 81  ? 6.606   -38.034 -40.079  1.00 59.62  ? 86  TYR E CB  1 
ATOM   8494  C CG  . TYR E 1 81  ? 5.362   -37.330 -40.583  1.00 59.11  ? 86  TYR E CG  1 
ATOM   8495  C CD1 . TYR E 1 81  ? 4.889   -37.543 -41.870  1.00 67.01  ? 86  TYR E CD1 1 
ATOM   8496  C CD2 . TYR E 1 81  ? 4.679   -36.427 -39.778  1.00 53.92  ? 86  TYR E CD2 1 
ATOM   8497  C CE1 . TYR E 1 81  ? 3.761   -36.892 -42.336  1.00 67.92  ? 86  TYR E CE1 1 
ATOM   8498  C CE2 . TYR E 1 81  ? 3.551   -35.772 -40.237  1.00 59.91  ? 86  TYR E CE2 1 
ATOM   8499  C CZ  . TYR E 1 81  ? 3.096   -36.009 -41.513  1.00 60.48  ? 86  TYR E CZ  1 
ATOM   8500  O OH  . TYR E 1 81  ? 1.972   -35.358 -41.969  1.00 57.12  ? 86  TYR E OH  1 
ATOM   8501  N N   . ILE E 1 82  ? 5.625   -39.466 -37.491  1.00 65.48  ? 87  ILE E N   1 
ATOM   8502  C CA  . ILE E 1 82  ? 4.708   -39.686 -36.378  1.00 59.45  ? 87  ILE E CA  1 
ATOM   8503  C C   . ILE E 1 82  ? 4.215   -38.338 -35.874  1.00 51.75  ? 87  ILE E C   1 
ATOM   8504  O O   . ILE E 1 82  ? 5.000   -37.395 -35.722  1.00 68.57  ? 87  ILE E O   1 
ATOM   8505  C CB  . ILE E 1 82  ? 5.380   -40.483 -35.241  1.00 50.53  ? 87  ILE E CB  1 
ATOM   8506  C CG1 . ILE E 1 82  ? 5.664   -41.919 -35.685  1.00 62.57  ? 87  ILE E CG1 1 
ATOM   8507  C CG2 . ILE E 1 82  ? 4.527   -40.457 -33.978  1.00 52.44  ? 87  ILE E CG2 1 
ATOM   8508  C CD1 . ILE E 1 82  ? 6.273   -42.786 -34.604  1.00 54.75  ? 87  ILE E CD1 1 
ATOM   8509  N N   . VAL E 1 83  ? 2.912   -38.249 -35.621  1.00 58.79  ? 88  VAL E N   1 
ATOM   8510  C CA  . VAL E 1 83  ? 2.287   -37.034 -35.115  1.00 69.70  ? 88  VAL E CA  1 
ATOM   8511  C C   . VAL E 1 83  ? 1.824   -37.315 -33.691  1.00 56.24  ? 88  VAL E C   1 
ATOM   8512  O O   . VAL E 1 83  ? 0.761   -37.907 -33.471  1.00 71.06  ? 88  VAL E O   1 
ATOM   8513  C CB  . VAL E 1 83  ? 1.123   -36.572 -35.997  1.00 68.41  ? 88  VAL E CB  1 
ATOM   8514  C CG1 . VAL E 1 83  ? 0.521   -35.286 -35.447  1.00 51.55  ? 88  VAL E CG1 1 
ATOM   8515  C CG2 . VAL E 1 83  ? 1.590   -36.379 -37.426  1.00 52.17  ? 88  VAL E CG2 1 
ATOM   8516  N N   . GLU E 1 84  ? 2.628   -36.895 -32.720  1.00 63.28  ? 89  GLU E N   1 
ATOM   8517  C CA  . GLU E 1 84  ? 2.169   -36.788 -31.346  1.00 55.72  ? 89  GLU E CA  1 
ATOM   8518  C C   . GLU E 1 84  ? 1.472   -35.448 -31.145  1.00 64.47  ? 89  GLU E C   1 
ATOM   8519  O O   . GLU E 1 84  ? 1.530   -34.552 -31.991  1.00 72.15  ? 89  GLU E O   1 
ATOM   8520  C CB  . GLU E 1 84  ? 3.337   -36.921 -30.370  1.00 67.00  ? 89  GLU E CB  1 
ATOM   8521  C CG  . GLU E 1 84  ? 3.513   -38.299 -29.757  1.00 66.19  ? 89  GLU E CG  1 
ATOM   8522  C CD  . GLU E 1 84  ? 4.680   -38.349 -28.786  1.00 88.73  ? 89  GLU E CD  1 
ATOM   8523  O OE1 . GLU E 1 84  ? 5.435   -37.356 -28.718  1.00 74.03  ? 89  GLU E OE1 1 
ATOM   8524  O OE2 . GLU E 1 84  ? 4.842   -39.376 -28.092  1.00 84.54  ? 89  GLU E OE2 1 
ATOM   8525  N N   . ARG E 1 85  ? 0.804   -35.312 -30.009  1.00 74.36  ? 90  ARG E N   1 
ATOM   8526  C CA  . ARG E 1 85  ? 0.237   -34.034 -29.611  1.00 77.15  ? 90  ARG E CA  1 
ATOM   8527  C C   . ARG E 1 85  ? 1.148   -33.360 -28.592  1.00 69.09  ? 90  ARG E C   1 
ATOM   8528  O O   . ARG E 1 85  ? 2.102   -33.955 -28.084  1.00 79.12  ? 90  ARG E O   1 
ATOM   8529  C CB  . ARG E 1 85  ? -1.181  -34.215 -29.066  1.00 78.64  ? 90  ARG E CB  1 
ATOM   8530  C CG  . ARG E 1 85  ? -2.237  -33.876 -30.107  1.00 70.88  ? 90  ARG E CG  1 
ATOM   8531  C CD  . ARG E 1 85  ? -3.589  -34.449 -29.767  1.00 85.76  ? 90  ARG E CD  1 
ATOM   8532  N NE  . ARG E 1 85  ? -4.070  -34.012 -28.464  1.00 101.32 ? 90  ARG E NE  1 
ATOM   8533  C CZ  . ARG E 1 85  ? -4.693  -32.864 -28.239  1.00 102.84 ? 90  ARG E CZ  1 
ATOM   8534  N NH1 . ARG E 1 85  ? -4.903  -31.988 -29.209  1.00 76.47  ? 90  ARG E NH1 1 
ATOM   8535  N NH2 . ARG E 1 85  ? -5.120  -32.589 -27.011  1.00 96.16  ? 90  ARG E NH2 1 
ATOM   8536  N N   . ALA E 1 86  ? 0.853   -32.087 -28.317  1.00 78.20  ? 91  ALA E N   1 
ATOM   8537  C CA  . ALA E 1 86  ? 1.736   -31.282 -27.476  1.00 87.81  ? 91  ALA E CA  1 
ATOM   8538  C C   . ALA E 1 86  ? 1.922   -31.919 -26.105  1.00 95.34  ? 91  ALA E C   1 
ATOM   8539  O O   . ALA E 1 86  ? 3.048   -32.032 -25.607  1.00 84.16  ? 91  ALA E O   1 
ATOM   8540  C CB  . ALA E 1 86  ? 1.182   -29.863 -27.343  1.00 94.86  ? 91  ALA E CB  1 
ATOM   8541  N N   . ASN E 1 87  ? 0.825   -32.342 -25.479  1.00 87.71  ? 92  ASN E N   1 
ATOM   8542  C CA  . ASN E 1 87  ? 0.861   -33.048 -24.200  1.00 80.37  ? 92  ASN E CA  1 
ATOM   8543  C C   . ASN E 1 87  ? -0.086  -34.235 -24.289  1.00 82.87  ? 92  ASN E C   1 
ATOM   8544  O O   . ASN E 1 87  ? -1.278  -34.118 -23.970  1.00 78.51  ? 92  ASN E O   1 
ATOM   8545  C CB  . ASN E 1 87  ? 0.495   -32.121 -23.043  1.00 67.29  ? 92  ASN E CB  1 
ATOM   8546  C CG  . ASN E 1 87  ? 1.631   -31.193 -22.660  1.00 91.07  ? 92  ASN E CG  1 
ATOM   8547  O OD1 . ASN E 1 87  ? 2.755   -31.636 -22.419  1.00 96.37  ? 92  ASN E OD1 1 
ATOM   8548  N ND2 . ASN E 1 87  ? 1.347   -29.897 -22.613  1.00 87.25  ? 92  ASN E ND2 1 
ATOM   8549  N N   . PRO E 1 88  ? 0.402   -35.390 -24.744  1.00 64.68  ? 93  PRO E N   1 
ATOM   8550  C CA  . PRO E 1 88  ? -0.464  -36.571 -24.825  1.00 70.52  ? 93  PRO E CA  1 
ATOM   8551  C C   . PRO E 1 88  ? -1.022  -36.933 -23.458  1.00 73.21  ? 93  PRO E C   1 
ATOM   8552  O O   . PRO E 1 88  ? -0.322  -36.879 -22.445  1.00 80.98  ? 93  PRO E O   1 
ATOM   8553  C CB  . PRO E 1 88  ? 0.470   -37.662 -25.362  1.00 79.74  ? 93  PRO E CB  1 
ATOM   8554  C CG  . PRO E 1 88  ? 1.586   -36.921 -26.029  1.00 72.46  ? 93  PRO E CG  1 
ATOM   8555  C CD  . PRO E 1 88  ? 1.764   -35.664 -25.232  1.00 69.43  ? 93  PRO E CD  1 
ATOM   8556  N N   . ALA E 1 89  ? -2.299  -37.305 -23.437  1.00 72.09  ? 94  ALA E N   1 
ATOM   8557  C CA  . ALA E 1 89  ? -2.985  -37.610 -22.190  1.00 71.56  ? 94  ALA E CA  1 
ATOM   8558  C C   . ALA E 1 89  ? -2.793  -39.048 -21.732  1.00 69.88  ? 94  ALA E C   1 
ATOM   8559  O O   . ALA E 1 89  ? -3.207  -39.384 -20.617  1.00 84.74  ? 94  ALA E O   1 
ATOM   8560  C CB  . ALA E 1 89  ? -4.482  -37.316 -22.327  1.00 81.72  ? 94  ALA E CB  1 
ATOM   8561  N N   . ASN E 1 90  ? -2.180  -39.906 -22.553  1.00 67.10  ? 95  ASN E N   1 
ATOM   8562  C CA  . ASN E 1 90  ? -1.987  -41.316 -22.211  1.00 70.78  ? 95  ASN E CA  1 
ATOM   8563  C C   . ASN E 1 90  ? -0.516  -41.677 -22.422  1.00 64.07  ? 95  ASN E C   1 
ATOM   8564  O O   . ASN E 1 90  ? -0.122  -42.209 -23.464  1.00 78.75  ? 95  ASN E O   1 
ATOM   8565  C CB  . ASN E 1 90  ? -2.920  -42.198 -23.026  1.00 71.77  ? 95  ASN E CB  1 
ATOM   8566  C CG  . ASN E 1 90  ? -4.380  -41.961 -22.690  1.00 75.35  ? 95  ASN E CG  1 
ATOM   8567  O OD1 . ASN E 1 90  ? -4.766  -41.954 -21.520  1.00 76.73  ? 95  ASN E OD1 1 
ATOM   8568  N ND2 . ASN E 1 90  ? -5.198  -41.755 -23.715  1.00 78.72  ? 95  ASN E ND2 1 
ATOM   8569  N N   . ASP E 1 91  ? 0.288   -41.380 -21.410  1.00 62.00  ? 96  ASP E N   1 
ATOM   8570  C CA  . ASP E 1 91  ? 1.658   -41.856 -21.292  1.00 62.17  ? 96  ASP E CA  1 
ATOM   8571  C C   . ASP E 1 91  ? 1.630   -43.161 -20.495  1.00 56.46  ? 96  ASP E C   1 
ATOM   8572  O O   . ASP E 1 91  ? 0.586   -43.812 -20.393  1.00 83.77  ? 96  ASP E O   1 
ATOM   8573  C CB  . ASP E 1 91  ? 2.539   -40.775 -20.659  1.00 68.43  ? 96  ASP E CB  1 
ATOM   8574  C CG  . ASP E 1 91  ? 3.884   -40.642 -21.346  1.00 99.00  ? 96  ASP E CG  1 
ATOM   8575  O OD1 . ASP E 1 91  ? 4.057   -41.225 -22.439  1.00 89.54  ? 96  ASP E OD1 1 
ATOM   8576  O OD2 . ASP E 1 91  ? 4.767   -39.954 -20.788  1.00 114.03 ? 96  ASP E OD2 1 
ATOM   8577  N N   . LEU E 1 92  A 2.776   -43.587 -19.966  1.00 65.49  ? 96  LEU E N   1 
ATOM   8578  C CA  . LEU E 1 92  A 2.797   -44.721 -19.049  1.00 76.96  ? 96  LEU E CA  1 
ATOM   8579  C C   . LEU E 1 92  A 1.801   -44.489 -17.918  1.00 65.52  ? 96  LEU E C   1 
ATOM   8580  O O   . LEU E 1 92  A 2.001   -43.604 -17.080  1.00 60.64  ? 96  LEU E O   1 
ATOM   8581  C CB  . LEU E 1 92  A 4.204   -44.917 -18.482  1.00 55.21  ? 96  LEU E CB  1 
ATOM   8582  C CG  . LEU E 1 92  A 5.360   -44.715 -19.461  1.00 51.46  ? 96  LEU E CG  1 
ATOM   8583  C CD1 . LEU E 1 92  A 6.648   -44.431 -18.712  1.00 57.67  ? 96  LEU E CD1 1 
ATOM   8584  C CD2 . LEU E 1 92  A 5.518   -45.932 -20.350  1.00 52.12  ? 96  LEU E CD2 1 
ATOM   8585  N N   . CYS E 1 93  ? 0.723   -45.277 -17.887  1.00 58.22  ? 97  CYS E N   1 
ATOM   8586  C CA  . CYS E 1 93  ? -0.294  -45.091 -16.857  1.00 57.24  ? 97  CYS E CA  1 
ATOM   8587  C C   . CYS E 1 93  ? 0.248   -45.435 -15.475  1.00 64.58  ? 97  CYS E C   1 
ATOM   8588  O O   . CYS E 1 93  ? -0.021  -44.723 -14.501  1.00 50.63  ? 97  CYS E O   1 
ATOM   8589  C CB  . CYS E 1 93  ? -1.530  -45.927 -17.188  1.00 47.98  ? 97  CYS E CB  1 
ATOM   8590  S SG  . CYS E 1 93  ? -1.159  -47.608 -17.729  1.00 72.88  ? 97  CYS E SG  1 
ATOM   8591  N N   . TYR E 1 94  ? 1.007   -46.517 -15.369  1.00 57.18  ? 98  TYR E N   1 
ATOM   8592  C CA  . TYR E 1 94  ? 1.720   -46.805 -14.132  1.00 47.34  ? 98  TYR E CA  1 
ATOM   8593  C C   . TYR E 1 94  ? 3.015   -46.001 -14.110  1.00 56.60  ? 98  TYR E C   1 
ATOM   8594  O O   . TYR E 1 94  ? 3.798   -46.080 -15.062  1.00 49.80  ? 98  TYR E O   1 
ATOM   8595  C CB  . TYR E 1 94  ? 2.016   -48.295 -14.007  1.00 45.56  ? 98  TYR E CB  1 
ATOM   8596  C CG  . TYR E 1 94  ? 2.352   -48.732 -12.598  1.00 51.93  ? 98  TYR E CG  1 
ATOM   8597  C CD1 . TYR E 1 94  ? 3.646   -48.631 -12.109  1.00 49.30  ? 98  TYR E CD1 1 
ATOM   8598  C CD2 . TYR E 1 94  ? 1.371   -49.244 -11.757  1.00 46.75  ? 98  TYR E CD2 1 
ATOM   8599  C CE1 . TYR E 1 94  ? 3.957   -49.027 -10.822  1.00 53.79  ? 98  TYR E CE1 1 
ATOM   8600  C CE2 . TYR E 1 94  ? 1.674   -49.643 -10.467  1.00 48.89  ? 98  TYR E CE2 1 
ATOM   8601  C CZ  . TYR E 1 94  ? 2.967   -49.533 -10.005  1.00 57.81  ? 98  TYR E CZ  1 
ATOM   8602  O OH  . TYR E 1 94  ? 3.272   -49.930 -8.722   1.00 59.54  ? 98  TYR E OH  1 
ATOM   8603  N N   . PRO E 1 95  ? 3.269   -45.217 -13.061  1.00 51.86  ? 99  PRO E N   1 
ATOM   8604  C CA  . PRO E 1 95  ? 4.399   -44.280 -13.098  1.00 49.59  ? 99  PRO E CA  1 
ATOM   8605  C C   . PRO E 1 95  ? 5.733   -44.992 -13.257  1.00 54.79  ? 99  PRO E C   1 
ATOM   8606  O O   . PRO E 1 95  ? 5.939   -46.101 -12.758  1.00 56.65  ? 99  PRO E O   1 
ATOM   8607  C CB  . PRO E 1 95  ? 4.307   -43.560 -11.748  1.00 47.80  ? 99  PRO E CB  1 
ATOM   8608  C CG  . PRO E 1 95  ? 3.581   -44.515 -10.865  1.00 54.90  ? 99  PRO E CG  1 
ATOM   8609  C CD  . PRO E 1 95  ? 2.590   -45.211 -11.755  1.00 45.37  ? 99  PRO E CD  1 
ATOM   8610  N N   . GLY E 1 96  ? 6.643   -44.331 -13.967  1.00 52.23  ? 100 GLY E N   1 
ATOM   8611  C CA  . GLY E 1 96  ? 7.959   -44.881 -14.229  1.00 51.41  ? 100 GLY E CA  1 
ATOM   8612  C C   . GLY E 1 96  ? 8.659   -44.198 -15.385  1.00 63.95  ? 100 GLY E C   1 
ATOM   8613  O O   . GLY E 1 96  ? 8.602   -42.972 -15.512  1.00 64.51  ? 100 GLY E O   1 
ATOM   8614  N N   . SER E 1 97  ? 9.327   -44.976 -16.234  1.00 61.40  ? 101 SER E N   1 
ATOM   8615  C CA  . SER E 1 97  ? 10.056  -44.402 -17.356  1.00 57.30  ? 101 SER E CA  1 
ATOM   8616  C C   . SER E 1 97  ? 10.262  -45.466 -18.422  1.00 48.93  ? 101 SER E C   1 
ATOM   8617  O O   . SER E 1 97  ? 10.156  -46.668 -18.160  1.00 46.58  ? 101 SER E O   1 
ATOM   8618  C CB  . SER E 1 97  ? 11.407  -43.830 -16.911  1.00 59.20  ? 101 SER E CB  1 
ATOM   8619  O OG  . SER E 1 97  ? 12.269  -44.862 -16.465  1.00 56.55  ? 101 SER E OG  1 
ATOM   8620  N N   . LEU E 1 98  ? 10.554  -45.002 -19.633  1.00 59.66  ? 102 LEU E N   1 
ATOM   8621  C CA  . LEU E 1 98  ? 11.027  -45.852 -20.719  1.00 46.49  ? 102 LEU E CA  1 
ATOM   8622  C C   . LEU E 1 98  ? 12.467  -45.459 -21.017  1.00 59.11  ? 102 LEU E C   1 
ATOM   8623  O O   . LEU E 1 98  ? 12.751  -44.286 -21.286  1.00 57.99  ? 102 LEU E O   1 
ATOM   8624  C CB  . LEU E 1 98  ? 10.146  -45.713 -21.960  1.00 49.24  ? 102 LEU E CB  1 
ATOM   8625  C CG  . LEU E 1 98  ? 10.501  -46.616 -23.144  1.00 59.65  ? 102 LEU E CG  1 
ATOM   8626  C CD1 . LEU E 1 98  ? 10.777  -48.038 -22.679  1.00 51.68  ? 102 LEU E CD1 1 
ATOM   8627  C CD2 . LEU E 1 98  ? 9.382   -46.603 -24.174  1.00 54.61  ? 102 LEU E CD2 1 
ATOM   8628  N N   . ASN E 1 99  ? 13.371  -46.433 -20.955  1.00 50.07  ? 103 ASN E N   1 
ATOM   8629  C CA  . ASN E 1 99  ? 14.791  -46.146 -21.095  1.00 40.84  ? 103 ASN E CA  1 
ATOM   8630  C C   . ASN E 1 99  ? 15.135  -45.809 -22.541  1.00 51.56  ? 103 ASN E C   1 
ATOM   8631  O O   . ASN E 1 99  ? 14.597  -46.405 -23.479  1.00 58.32  ? 103 ASN E O   1 
ATOM   8632  C CB  . ASN E 1 99  ? 15.617  -47.339 -20.614  1.00 49.31  ? 103 ASN E CB  1 
ATOM   8633  C CG  . ASN E 1 99  ? 17.109  -47.066 -20.634  1.00 42.46  ? 103 ASN E CG  1 
ATOM   8634  O OD1 . ASN E 1 99  ? 17.628  -46.317 -19.806  1.00 54.29  ? 103 ASN E OD1 1 
ATOM   8635  N ND2 . ASN E 1 99  ? 17.808  -47.687 -21.575  1.00 58.07  ? 103 ASN E ND2 1 
ATOM   8636  N N   . ASP E 1 100 ? 16.041  -44.844 -22.713  1.00 50.23  ? 104 ASP E N   1 
ATOM   8637  C CA  . ASP E 1 100 ? 16.464  -44.371 -24.031  1.00 54.79  ? 104 ASP E CA  1 
ATOM   8638  C C   . ASP E 1 100 ? 15.258  -43.976 -24.880  1.00 51.90  ? 104 ASP E C   1 
ATOM   8639  O O   . ASP E 1 100 ? 15.122  -44.369 -26.041  1.00 59.31  ? 104 ASP E O   1 
ATOM   8640  C CB  . ASP E 1 100 ? 17.323  -45.420 -24.743  1.00 60.54  ? 104 ASP E CB  1 
ATOM   8641  C CG  . ASP E 1 100 ? 18.702  -45.562 -24.124  1.00 65.02  ? 104 ASP E CG  1 
ATOM   8642  O OD1 . ASP E 1 100 ? 19.215  -44.563 -23.577  1.00 74.41  ? 104 ASP E OD1 1 
ATOM   8643  O OD2 . ASP E 1 100 ? 19.273  -46.672 -24.187  1.00 60.78  ? 104 ASP E OD2 1 
ATOM   8644  N N   . TYR E 1 101 ? 14.367  -43.187 -24.275  1.00 50.31  ? 105 TYR E N   1 
ATOM   8645  C CA  . TYR E 1 101 ? 13.091  -42.869 -24.911  1.00 49.90  ? 105 TYR E CA  1 
ATOM   8646  C C   . TYR E 1 101 ? 13.288  -42.066 -26.193  1.00 47.44  ? 105 TYR E C   1 
ATOM   8647  O O   . TYR E 1 101 ? 12.725  -42.403 -27.240  1.00 52.21  ? 105 TYR E O   1 
ATOM   8648  C CB  . TYR E 1 101 ? 12.199  -42.106 -23.931  1.00 39.93  ? 105 TYR E CB  1 
ATOM   8649  C CG  . TYR E 1 101 ? 10.767  -41.964 -24.390  1.00 56.53  ? 105 TYR E CG  1 
ATOM   8650  C CD1 . TYR E 1 101 ? 10.164  -42.950 -25.158  1.00 53.32  ? 105 TYR E CD1 1 
ATOM   8651  C CD2 . TYR E 1 101 ? 10.021  -40.839 -24.060  1.00 55.15  ? 105 TYR E CD2 1 
ATOM   8652  C CE1 . TYR E 1 101 ? 8.856   -42.825 -25.580  1.00 49.69  ? 105 TYR E CE1 1 
ATOM   8653  C CE2 . TYR E 1 101 ? 8.711   -40.704 -24.480  1.00 63.04  ? 105 TYR E CE2 1 
ATOM   8654  C CZ  . TYR E 1 101 ? 8.133   -41.700 -25.240  1.00 62.09  ? 105 TYR E CZ  1 
ATOM   8655  O OH  . TYR E 1 101 ? 6.829   -41.572 -25.661  1.00 60.51  ? 105 TYR E OH  1 
ATOM   8656  N N   . GLU E 1 102 ? 14.092  -41.000 -26.129  1.00 46.55  ? 106 GLU E N   1 
ATOM   8657  C CA  . GLU E 1 102 ? 14.232  -40.105 -27.275  1.00 54.94  ? 106 GLU E CA  1 
ATOM   8658  C C   . GLU E 1 102 ? 14.850  -40.817 -28.473  1.00 54.59  ? 106 GLU E C   1 
ATOM   8659  O O   . GLU E 1 102 ? 14.415  -40.617 -29.614  1.00 57.73  ? 106 GLU E O   1 
ATOM   8660  C CB  . GLU E 1 102 ? 15.063  -38.880 -26.889  1.00 65.94  ? 106 GLU E CB  1 
ATOM   8661  C CG  . GLU E 1 102 ? 14.370  -37.929 -25.915  1.00 73.81  ? 106 GLU E CG  1 
ATOM   8662  C CD  . GLU E 1 102 ? 13.281  -37.089 -26.567  1.00 77.59  ? 106 GLU E CD  1 
ATOM   8663  O OE1 . GLU E 1 102 ? 13.009  -37.278 -27.772  1.00 89.57  ? 106 GLU E OE1 1 
ATOM   8664  O OE2 . GLU E 1 102 ? 12.698  -36.232 -25.869  1.00 93.09  ? 106 GLU E OE2 1 
ATOM   8665  N N   . GLU E 1 103 ? 15.869  -41.647 -28.239  1.00 52.01  ? 107 GLU E N   1 
ATOM   8666  C CA  . GLU E 1 103 ? 16.456  -42.409 -29.335  1.00 47.40  ? 107 GLU E CA  1 
ATOM   8667  C C   . GLU E 1 103 ? 15.459  -43.406 -29.910  1.00 53.39  ? 107 GLU E C   1 
ATOM   8668  O O   . GLU E 1 103 ? 15.450  -43.652 -31.122  1.00 63.39  ? 107 GLU E O   1 
ATOM   8669  C CB  . GLU E 1 103 ? 17.724  -43.121 -28.867  1.00 44.09  ? 107 GLU E CB  1 
ATOM   8670  C CG  . GLU E 1 103 ? 18.950  -42.227 -28.855  1.00 56.10  ? 107 GLU E CG  1 
ATOM   8671  C CD  . GLU E 1 103 ? 19.316  -41.732 -30.241  1.00 72.59  ? 107 GLU E CD  1 
ATOM   8672  O OE1 . GLU E 1 103 ? 19.387  -42.565 -31.170  1.00 77.34  ? 107 GLU E OE1 1 
ATOM   8673  O OE2 . GLU E 1 103 ? 19.525  -40.511 -30.406  1.00 67.17  ? 107 GLU E OE2 1 
ATOM   8674  N N   . LEU E 1 104 ? 14.616  -43.994 -29.058  1.00 51.55  ? 108 LEU E N   1 
ATOM   8675  C CA  . LEU E 1 104 ? 13.594  -44.911 -29.553  1.00 51.24  ? 108 LEU E CA  1 
ATOM   8676  C C   . LEU E 1 104 ? 12.580  -44.188 -30.431  1.00 48.29  ? 108 LEU E C   1 
ATOM   8677  O O   . LEU E 1 104 ? 12.154  -44.717 -31.464  1.00 58.58  ? 108 LEU E O   1 
ATOM   8678  C CB  . LEU E 1 104 ? 12.895  -45.605 -28.386  1.00 45.95  ? 108 LEU E CB  1 
ATOM   8679  C CG  . LEU E 1 104 ? 11.813  -46.608 -28.788  1.00 47.96  ? 108 LEU E CG  1 
ATOM   8680  C CD1 . LEU E 1 104 ? 12.417  -47.747 -29.594  1.00 50.52  ? 108 LEU E CD1 1 
ATOM   8681  C CD2 . LEU E 1 104 ? 11.084  -47.138 -27.565  1.00 38.82  ? 108 LEU E CD2 1 
ATOM   8682  N N   . LYS E 1 105 ? 12.172  -42.979 -30.031  1.00 46.19  ? 109 LYS E N   1 
ATOM   8683  C CA  . LYS E 1 105 ? 11.218  -42.220 -30.834  1.00 49.39  ? 109 LYS E CA  1 
ATOM   8684  C C   . LYS E 1 105 ? 11.808  -41.844 -32.189  1.00 59.36  ? 109 LYS E C   1 
ATOM   8685  O O   . LYS E 1 105 ? 11.116  -41.898 -33.212  1.00 57.08  ? 109 LYS E O   1 
ATOM   8686  C CB  . LYS E 1 105 ? 10.761  -40.973 -30.074  1.00 39.08  ? 109 LYS E CB  1 
ATOM   8687  C CG  . LYS E 1 105 ? 9.789   -41.273 -28.942  1.00 50.91  ? 109 LYS E CG  1 
ATOM   8688  C CD  . LYS E 1 105 ? 9.009   -40.038 -28.509  1.00 54.12  ? 109 LYS E CD  1 
ATOM   8689  C CE  . LYS E 1 105 ? 9.852   -39.102 -27.661  1.00 64.81  ? 109 LYS E CE  1 
ATOM   8690  N NZ  . LYS E 1 105 ? 9.038   -37.976 -27.118  1.00 75.24  ? 109 LYS E NZ  1 
ATOM   8691  N N   . HIS E 1 106 ? 13.085  -41.454 -32.214  1.00 58.62  ? 110 HIS E N   1 
ATOM   8692  C CA  . HIS E 1 106 ? 13.741  -41.158 -33.484  1.00 63.40  ? 110 HIS E CA  1 
ATOM   8693  C C   . HIS E 1 106 ? 13.824  -42.400 -34.361  1.00 51.69  ? 110 HIS E C   1 
ATOM   8694  O O   . HIS E 1 106 ? 13.632  -42.326 -35.580  1.00 61.09  ? 110 HIS E O   1 
ATOM   8695  C CB  . HIS E 1 106 ? 15.137  -40.586 -33.233  1.00 54.88  ? 110 HIS E CB  1 
ATOM   8696  C CG  . HIS E 1 106 ? 15.844  -40.151 -34.478  1.00 66.67  ? 110 HIS E CG  1 
ATOM   8697  N ND1 . HIS E 1 106 ? 15.785  -38.859 -34.955  1.00 57.15  ? 110 HIS E ND1 1 
ATOM   8698  C CD2 . HIS E 1 106 ? 16.621  -40.838 -35.349  1.00 60.82  ? 110 HIS E CD2 1 
ATOM   8699  C CE1 . HIS E 1 106 ? 16.498  -38.768 -36.063  1.00 63.33  ? 110 HIS E CE1 1 
ATOM   8700  N NE2 . HIS E 1 106 ? 17.015  -39.955 -36.325  1.00 68.27  ? 110 HIS E NE2 1 
ATOM   8701  N N   . LEU E 1 107 ? 14.115  -43.554 -33.753  1.00 50.07  ? 111 LEU E N   1 
ATOM   8702  C CA  . LEU E 1 107 ? 14.195  -44.805 -34.501  1.00 48.92  ? 111 LEU E CA  1 
ATOM   8703  C C   . LEU E 1 107 ? 12.860  -45.172 -35.136  1.00 54.61  ? 111 LEU E C   1 
ATOM   8704  O O   . LEU E 1 107 ? 12.830  -45.726 -36.240  1.00 60.09  ? 111 LEU E O   1 
ATOM   8705  C CB  . LEU E 1 107 ? 14.670  -45.929 -33.578  1.00 51.15  ? 111 LEU E CB  1 
ATOM   8706  C CG  . LEU E 1 107 ? 14.610  -47.369 -34.097  1.00 46.77  ? 111 LEU E CG  1 
ATOM   8707  C CD1 . LEU E 1 107 ? 15.703  -47.642 -35.121  1.00 67.46  ? 111 LEU E CD1 1 
ATOM   8708  C CD2 . LEU E 1 107 ? 14.690  -48.358 -32.944  1.00 66.68  ? 111 LEU E CD2 1 
ATOM   8709  N N   . LEU E 1 108 ? 11.752  -44.874 -34.462  1.00 60.57  ? 112 LEU E N   1 
ATOM   8710  C CA  . LEU E 1 108 ? 10.426  -45.245 -34.936  1.00 63.18  ? 112 LEU E CA  1 
ATOM   8711  C C   . LEU E 1 108 ? 9.753   -44.157 -35.763  1.00 58.40  ? 112 LEU E C   1 
ATOM   8712  O O   . LEU E 1 108 ? 8.602   -44.342 -36.172  1.00 58.14  ? 112 LEU E O   1 
ATOM   8713  C CB  . LEU E 1 108 ? 9.526   -45.602 -33.748  1.00 48.50  ? 112 LEU E CB  1 
ATOM   8714  C CG  . LEU E 1 108 ? 9.815   -46.912 -33.019  1.00 52.11  ? 112 LEU E CG  1 
ATOM   8715  C CD1 . LEU E 1 108 ? 8.938   -47.026 -31.789  1.00 50.40  ? 112 LEU E CD1 1 
ATOM   8716  C CD2 . LEU E 1 108 ? 9.584   -48.089 -33.948  1.00 57.28  ? 112 LEU E CD2 1 
ATOM   8717  N N   . SER E 1 109 ? 10.435  -43.038 -36.020  1.00 50.59  ? 113 SER E N   1 
ATOM   8718  C CA  . SER E 1 109 ? 9.792   -41.916 -36.697  1.00 58.79  ? 113 SER E CA  1 
ATOM   8719  C C   . SER E 1 109 ? 9.338   -42.295 -38.103  1.00 54.39  ? 113 SER E C   1 
ATOM   8720  O O   . SER E 1 109 ? 8.236   -41.926 -38.526  1.00 54.84  ? 113 SER E O   1 
ATOM   8721  C CB  . SER E 1 109 ? 10.742  -40.720 -36.740  1.00 59.25  ? 113 SER E CB  1 
ATOM   8722  O OG  . SER E 1 109 ? 11.995  -41.086 -37.291  1.00 65.75  ? 113 SER E OG  1 
ATOM   8723  N N   . ARG E 1 110 ? 10.170  -43.026 -38.844  1.00 58.66  ? 114 ARG E N   1 
ATOM   8724  C CA  . ARG E 1 110 ? 9.795   -43.564 -40.146  1.00 54.74  ? 114 ARG E CA  1 
ATOM   8725  C C   . ARG E 1 110 ? 10.102  -45.052 -40.157  1.00 45.93  ? 114 ARG E C   1 
ATOM   8726  O O   . ARG E 1 110 ? 11.244  -45.453 -39.910  1.00 64.49  ? 114 ARG E O   1 
ATOM   8727  C CB  . ARG E 1 110 ? 10.537  -42.857 -41.285  1.00 60.74  ? 114 ARG E CB  1 
ATOM   8728  C CG  . ARG E 1 110 ? 10.437  -43.575 -42.623  1.00 68.66  ? 114 ARG E CG  1 
ATOM   8729  C CD  . ARG E 1 110 ? 10.152  -42.608 -43.763  1.00 81.70  ? 114 ARG E CD  1 
ATOM   8730  N NE  . ARG E 1 110 ? 11.147  -41.547 -43.856  1.00 92.80  ? 114 ARG E NE  1 
ATOM   8731  C CZ  . ARG E 1 110 ? 12.245  -41.611 -44.597  1.00 104.17 ? 114 ARG E CZ  1 
ATOM   8732  N NH1 . ARG E 1 110 ? 12.533  -42.683 -45.317  1.00 109.81 ? 114 ARG E NH1 1 
ATOM   8733  N NH2 . ARG E 1 110 ? 13.075  -40.572 -44.617  1.00 79.12  ? 114 ARG E NH2 1 
ATOM   8734  N N   . ILE E 1 111 ? 9.093   -45.867 -40.450  1.00 47.09  ? 115 ILE E N   1 
ATOM   8735  C CA  . ILE E 1 111 ? 9.213   -47.319 -40.395  1.00 54.22  ? 115 ILE E CA  1 
ATOM   8736  C C   . ILE E 1 111 ? 8.651   -47.910 -41.679  1.00 51.97  ? 115 ILE E C   1 
ATOM   8737  O O   . ILE E 1 111 ? 7.530   -47.579 -42.082  1.00 54.76  ? 115 ILE E O   1 
ATOM   8738  C CB  . ILE E 1 111 ? 8.493   -47.901 -39.164  1.00 54.12  ? 115 ILE E CB  1 
ATOM   8739  C CG1 . ILE E 1 111 ? 9.227   -47.494 -37.885  1.00 60.39  ? 115 ILE E CG1 1 
ATOM   8740  C CG2 . ILE E 1 111 ? 8.388   -49.410 -39.264  1.00 46.21  ? 115 ILE E CG2 1 
ATOM   8741  C CD1 . ILE E 1 111 ? 10.689  -47.873 -37.878  1.00 59.07  ? 115 ILE E CD1 1 
ATOM   8742  N N   . ASN E 1 112 ? 9.431   -48.786 -42.318  1.00 71.21  ? 116 ASN E N   1 
ATOM   8743  C CA  . ASN E 1 112 ? 9.007   -49.408 -43.569  1.00 62.87  ? 116 ASN E CA  1 
ATOM   8744  C C   . ASN E 1 112 ? 7.980   -50.511 -43.336  1.00 65.06  ? 116 ASN E C   1 
ATOM   8745  O O   . ASN E 1 112 ? 7.065   -50.688 -44.147  1.00 73.07  ? 116 ASN E O   1 
ATOM   8746  C CB  . ASN E 1 112 ? 10.224  -49.960 -44.314  1.00 63.59  ? 116 ASN E CB  1 
ATOM   8747  C CG  . ASN E 1 112 ? 9.884   -50.444 -45.710  1.00 89.03  ? 116 ASN E CG  1 
ATOM   8748  O OD1 . ASN E 1 112 ? 9.571   -51.617 -45.915  1.00 85.10  ? 116 ASN E OD1 1 
ATOM   8749  N ND2 . ASN E 1 112 ? 9.947   -49.540 -46.680  1.00 99.00  ? 116 ASN E ND2 1 
ATOM   8750  N N   . HIS E 1 113 ? 8.115   -51.265 -42.245  1.00 63.71  ? 117 HIS E N   1 
ATOM   8751  C CA  . HIS E 1 113 ? 7.176   -52.336 -41.931  1.00 68.16  ? 117 HIS E CA  1 
ATOM   8752  C C   . HIS E 1 113 ? 7.098   -52.501 -40.421  1.00 75.60  ? 117 HIS E C   1 
ATOM   8753  O O   . HIS E 1 113 ? 8.131   -52.556 -39.748  1.00 72.50  ? 117 HIS E O   1 
ATOM   8754  C CB  . HIS E 1 113 ? 7.593   -53.655 -42.591  1.00 72.04  ? 117 HIS E CB  1 
ATOM   8755  C CG  . HIS E 1 113 ? 6.627   -54.776 -42.363  1.00 90.04  ? 117 HIS E CG  1 
ATOM   8756  N ND1 . HIS E 1 113 ? 6.917   -55.859 -41.561  1.00 92.09  ? 117 HIS E ND1 1 
ATOM   8757  C CD2 . HIS E 1 113 ? 5.372   -54.980 -42.829  1.00 89.45  ? 117 HIS E CD2 1 
ATOM   8758  C CE1 . HIS E 1 113 ? 5.884   -56.682 -41.544  1.00 89.82  ? 117 HIS E CE1 1 
ATOM   8759  N NE2 . HIS E 1 113 ? 4.933   -56.172 -42.306  1.00 86.76  ? 117 HIS E NE2 1 
ATOM   8760  N N   . PHE E 1 114 ? 5.876   -52.594 -39.898  1.00 68.29  ? 118 PHE E N   1 
ATOM   8761  C CA  . PHE E 1 114 ? 5.644   -52.642 -38.459  1.00 62.29  ? 118 PHE E CA  1 
ATOM   8762  C C   . PHE E 1 114 ? 4.486   -53.588 -38.183  1.00 60.80  ? 118 PHE E C   1 
ATOM   8763  O O   . PHE E 1 114 ? 3.361   -53.334 -38.626  1.00 74.40  ? 118 PHE E O   1 
ATOM   8764  C CB  . PHE E 1 114 ? 5.345   -51.242 -37.914  1.00 57.19  ? 118 PHE E CB  1 
ATOM   8765  C CG  . PHE E 1 114 ? 5.550   -51.105 -36.433  1.00 50.93  ? 118 PHE E CG  1 
ATOM   8766  C CD1 . PHE E 1 114 ? 6.827   -51.027 -35.903  1.00 64.90  ? 118 PHE E CD1 1 
ATOM   8767  C CD2 . PHE E 1 114 ? 4.466   -51.033 -35.574  1.00 56.08  ? 118 PHE E CD2 1 
ATOM   8768  C CE1 . PHE E 1 114 ? 7.020   -50.893 -34.539  1.00 59.09  ? 118 PHE E CE1 1 
ATOM   8769  C CE2 . PHE E 1 114 ? 4.651   -50.897 -34.211  1.00 58.10  ? 118 PHE E CE2 1 
ATOM   8770  C CZ  . PHE E 1 114 ? 5.930   -50.827 -33.692  1.00 61.14  ? 118 PHE E CZ  1 
ATOM   8771  N N   . GLU E 1 115 ? 4.757   -54.674 -37.460  1.00 60.41  ? 119 GLU E N   1 
ATOM   8772  C CA  . GLU E 1 115 ? 3.741   -55.670 -37.147  1.00 58.70  ? 119 GLU E CA  1 
ATOM   8773  C C   . GLU E 1 115 ? 3.935   -56.172 -35.725  1.00 60.49  ? 119 GLU E C   1 
ATOM   8774  O O   . GLU E 1 115 ? 5.045   -56.556 -35.346  1.00 71.00  ? 119 GLU E O   1 
ATOM   8775  C CB  . GLU E 1 115 ? 3.796   -56.848 -38.129  1.00 48.36  ? 119 GLU E CB  1 
ATOM   8776  C CG  . GLU E 1 115 ? 2.824   -57.973 -37.800  1.00 67.34  ? 119 GLU E CG  1 
ATOM   8777  C CD  . GLU E 1 115 ? 3.004   -59.183 -38.696  1.00 90.57  ? 119 GLU E CD  1 
ATOM   8778  O OE1 . GLU E 1 115 ? 3.748   -59.080 -39.693  1.00 100.60 ? 119 GLU E OE1 1 
ATOM   8779  O OE2 . GLU E 1 115 ? 2.405   -60.239 -38.399  1.00 95.96  ? 119 GLU E OE2 1 
ATOM   8780  N N   . LYS E 1 116 ? 2.857   -56.171 -34.946  1.00 56.01  ? 120 LYS E N   1 
ATOM   8781  C CA  . LYS E 1 116 ? 2.893   -56.726 -33.601  1.00 60.49  ? 120 LYS E CA  1 
ATOM   8782  C C   . LYS E 1 116 ? 2.668   -58.231 -33.657  1.00 49.64  ? 120 LYS E C   1 
ATOM   8783  O O   . LYS E 1 116 ? 1.761   -58.707 -34.346  1.00 60.99  ? 120 LYS E O   1 
ATOM   8784  C CB  . LYS E 1 116 ? 1.836   -56.063 -32.717  1.00 35.83  ? 120 LYS E CB  1 
ATOM   8785  C CG  . LYS E 1 116 ? 1.931   -56.451 -31.249  1.00 58.08  ? 120 LYS E CG  1 
ATOM   8786  C CD  . LYS E 1 116 ? 1.033   -55.591 -30.369  1.00 49.12  ? 120 LYS E CD  1 
ATOM   8787  C CE  . LYS E 1 116 ? -0.440  -55.855 -30.633  1.00 56.22  ? 120 LYS E CE  1 
ATOM   8788  N NZ  . LYS E 1 116 ? -1.303  -55.103 -29.682  1.00 91.03  ? 120 LYS E NZ  1 
ATOM   8789  N N   . ILE E 1 117 ? 3.502   -58.983 -32.940  1.00 59.23  ? 121 ILE E N   1 
ATOM   8790  C CA  . ILE E 1 117 ? 3.409   -60.437 -32.917  1.00 46.98  ? 121 ILE E CA  1 
ATOM   8791  C C   . ILE E 1 117 ? 3.473   -60.923 -31.477  1.00 60.64  ? 121 ILE E C   1 
ATOM   8792  O O   . ILE E 1 117 ? 4.013   -60.249 -30.594  1.00 61.24  ? 121 ILE E O   1 
ATOM   8793  C CB  . ILE E 1 117 ? 4.518   -61.112 -33.758  1.00 46.19  ? 121 ILE E CB  1 
ATOM   8794  C CG1 . ILE E 1 117 ? 5.890   -60.894 -33.118  1.00 51.29  ? 121 ILE E CG1 1 
ATOM   8795  C CG2 . ILE E 1 117 ? 4.500   -60.593 -35.187  1.00 61.37  ? 121 ILE E CG2 1 
ATOM   8796  C CD1 . ILE E 1 117 ? 7.004   -61.662 -33.795  1.00 48.70  ? 121 ILE E CD1 1 
ATOM   8797  N N   . LEU E 1 118 ? 2.911   -62.107 -31.250  1.00 54.45  ? 122 LEU E N   1 
ATOM   8798  C CA  . LEU E 1 118 ? 2.920   -62.755 -29.944  1.00 53.12  ? 122 LEU E CA  1 
ATOM   8799  C C   . LEU E 1 118 ? 4.144   -63.660 -29.862  1.00 54.23  ? 122 LEU E C   1 
ATOM   8800  O O   . LEU E 1 118 ? 4.274   -64.604 -30.648  1.00 70.23  ? 122 LEU E O   1 
ATOM   8801  C CB  . LEU E 1 118 ? 1.624   -63.548 -29.750  1.00 40.21  ? 122 LEU E CB  1 
ATOM   8802  C CG  . LEU E 1 118 ? 1.238   -64.208 -28.419  1.00 61.68  ? 122 LEU E CG  1 
ATOM   8803  C CD1 . LEU E 1 118 ? 1.935   -65.551 -28.221  1.00 74.12  ? 122 LEU E CD1 1 
ATOM   8804  C CD2 . LEU E 1 118 ? 1.506   -63.280 -27.245  1.00 56.42  ? 122 LEU E CD2 1 
ATOM   8805  N N   . ILE E 1 119 ? 5.041   -63.376 -28.918  1.00 49.38  ? 123 ILE E N   1 
ATOM   8806  C CA  . ILE E 1 119 ? 6.291   -64.109 -28.787  1.00 50.97  ? 123 ILE E CA  1 
ATOM   8807  C C   . ILE E 1 119 ? 6.312   -64.978 -27.534  1.00 66.12  ? 123 ILE E C   1 
ATOM   8808  O O   . ILE E 1 119 ? 6.855   -66.085 -27.558  1.00 67.41  ? 123 ILE E O   1 
ATOM   8809  C CB  . ILE E 1 119 ? 7.507   -63.154 -28.819  1.00 53.97  ? 123 ILE E CB  1 
ATOM   8810  C CG1 . ILE E 1 119 ? 7.468   -62.164 -27.653  1.00 59.88  ? 123 ILE E CG1 1 
ATOM   8811  C CG2 . ILE E 1 119 ? 7.563   -62.409 -30.145  1.00 57.78  ? 123 ILE E CG2 1 
ATOM   8812  C CD1 . ILE E 1 119 ? 8.740   -61.356 -27.498  1.00 46.11  ? 123 ILE E CD1 1 
ATOM   8813  N N   . ILE E 1 120 ? 5.740   -64.500 -26.433  1.00 63.65  ? 124 ILE E N   1 
ATOM   8814  C CA  . ILE E 1 120 ? 5.695   -65.272 -25.193  1.00 57.75  ? 124 ILE E CA  1 
ATOM   8815  C C   . ILE E 1 120 ? 4.265   -65.273 -24.665  1.00 63.07  ? 124 ILE E C   1 
ATOM   8816  O O   . ILE E 1 120 ? 3.851   -64.313 -23.998  1.00 73.91  ? 124 ILE E O   1 
ATOM   8817  C CB  . ILE E 1 120 ? 6.674   -64.717 -24.148  1.00 70.36  ? 124 ILE E CB  1 
ATOM   8818  C CG1 . ILE E 1 120 ? 8.091   -64.667 -24.721  1.00 60.22  ? 124 ILE E CG1 1 
ATOM   8819  C CG2 . ILE E 1 120 ? 6.655   -65.578 -22.897  1.00 65.44  ? 124 ILE E CG2 1 
ATOM   8820  C CD1 . ILE E 1 120 ? 8.874   -63.434 -24.318  1.00 72.95  ? 124 ILE E CD1 1 
ATOM   8821  N N   . PRO E 1 121 ? 3.482   -66.312 -24.939  1.00 68.18  ? 125 PRO E N   1 
ATOM   8822  C CA  . PRO E 1 121 ? 2.095   -66.338 -24.467  1.00 65.25  ? 125 PRO E CA  1 
ATOM   8823  C C   . PRO E 1 121 ? 2.022   -66.476 -22.956  1.00 70.94  ? 125 PRO E C   1 
ATOM   8824  O O   . PRO E 1 121 ? 2.959   -66.928 -22.293  1.00 76.67  ? 125 PRO E O   1 
ATOM   8825  C CB  . PRO E 1 121 ? 1.504   -67.567 -25.165  1.00 67.72  ? 125 PRO E CB  1 
ATOM   8826  C CG  . PRO E 1 121 ? 2.678   -68.454 -25.400  1.00 60.22  ? 125 PRO E CG  1 
ATOM   8827  C CD  . PRO E 1 121 ? 3.843   -67.539 -25.670  1.00 54.08  ? 125 PRO E CD  1 
ATOM   8828  N N   . LYS E 1 122 A 0.870   -66.076 -22.413  1.00 71.83  ? 125 LYS E N   1 
ATOM   8829  C CA  . LYS E 1 122 A 0.658   -66.115 -20.971  1.00 72.26  ? 125 LYS E CA  1 
ATOM   8830  C C   . LYS E 1 122 A 0.605   -67.533 -20.418  1.00 64.55  ? 125 LYS E C   1 
ATOM   8831  O O   . LYS E 1 122 A 0.643   -67.699 -19.194  1.00 77.30  ? 125 LYS E O   1 
ATOM   8832  C CB  . LYS E 1 122 A -0.624  -65.360 -20.610  1.00 58.49  ? 125 LYS E CB  1 
ATOM   8833  C CG  . LYS E 1 122 A -0.532  -63.858 -20.839  1.00 76.48  ? 125 LYS E CG  1 
ATOM   8834  C CD  . LYS E 1 122 A -1.836  -63.150 -20.507  1.00 71.88  ? 125 LYS E CD  1 
ATOM   8835  C CE  . LYS E 1 122 A -2.145  -63.210 -19.020  1.00 81.72  ? 125 LYS E CE  1 
ATOM   8836  N NZ  . LYS E 1 122 A -3.398  -62.474 -18.694  1.00 84.37  ? 125 LYS E NZ  1 
ATOM   8837  N N   . SER E 1 123 B 0.526   -68.551 -21.274  1.00 69.06  ? 125 SER E N   1 
ATOM   8838  C CA  . SER E 1 123 B 0.617   -69.937 -20.831  1.00 82.72  ? 125 SER E CA  1 
ATOM   8839  C C   . SER E 1 123 B 2.057   -70.400 -20.640  1.00 78.98  ? 125 SER E C   1 
ATOM   8840  O O   . SER E 1 123 B 2.277   -71.570 -20.308  1.00 77.82  ? 125 SER E O   1 
ATOM   8841  C CB  . SER E 1 123 B -0.089  -70.861 -21.828  1.00 78.82  ? 125 SER E CB  1 
ATOM   8842  O OG  . SER E 1 123 B 0.752   -71.175 -22.925  1.00 87.52  ? 125 SER E OG  1 
ATOM   8843  N N   . SER E 1 124 ? 3.035   -69.525 -20.852  1.00 66.62  ? 126 SER E N   1 
ATOM   8844  C CA  . SER E 1 124 ? 4.440   -69.876 -20.710  1.00 66.08  ? 126 SER E CA  1 
ATOM   8845  C C   . SER E 1 124 ? 4.944   -69.750 -19.278  1.00 75.01  ? 126 SER E C   1 
ATOM   8846  O O   . SER E 1 124 ? 6.137   -69.962 -19.037  1.00 71.84  ? 126 SER E O   1 
ATOM   8847  C CB  . SER E 1 124 ? 5.297   -69.002 -21.632  1.00 59.61  ? 126 SER E CB  1 
ATOM   8848  O OG  . SER E 1 124 ? 4.897   -69.138 -22.985  1.00 79.64  ? 126 SER E OG  1 
ATOM   8849  N N   . TRP E 1 125 ? 4.074   -69.413 -18.327  1.00 64.54  ? 127 TRP E N   1 
ATOM   8850  C CA  . TRP E 1 125 ? 4.451   -69.235 -16.925  1.00 70.52  ? 127 TRP E CA  1 
ATOM   8851  C C   . TRP E 1 125 ? 3.542   -70.097 -16.056  1.00 81.41  ? 127 TRP E C   1 
ATOM   8852  O O   . TRP E 1 125 ? 2.648   -69.587 -15.369  1.00 87.40  ? 127 TRP E O   1 
ATOM   8853  C CB  . TRP E 1 125 ? 4.363   -67.763 -16.519  1.00 71.06  ? 127 TRP E CB  1 
ATOM   8854  C CG  . TRP E 1 125 ? 4.760   -66.814 -17.608  1.00 58.70  ? 127 TRP E CG  1 
ATOM   8855  C CD1 . TRP E 1 125 ? 3.940   -66.246 -18.539  1.00 55.74  ? 127 TRP E CD1 1 
ATOM   8856  C CD2 . TRP E 1 125 ? 6.077   -66.320 -17.880  1.00 66.61  ? 127 TRP E CD2 1 
ATOM   8857  N NE1 . TRP E 1 125 ? 4.663   -65.430 -19.373  1.00 62.34  ? 127 TRP E NE1 1 
ATOM   8858  C CE2 . TRP E 1 125 ? 5.978   -65.458 -18.989  1.00 52.29  ? 127 TRP E CE2 1 
ATOM   8859  C CE3 . TRP E 1 125 ? 7.329   -66.522 -17.293  1.00 61.97  ? 127 TRP E CE3 1 
ATOM   8860  C CZ2 . TRP E 1 125 ? 7.083   -64.799 -19.522  1.00 42.30  ? 127 TRP E CZ2 1 
ATOM   8861  C CZ3 . TRP E 1 125 ? 8.424   -65.868 -17.826  1.00 62.91  ? 127 TRP E CZ3 1 
ATOM   8862  C CH2 . TRP E 1 125 ? 8.294   -65.018 -18.929  1.00 54.54  ? 127 TRP E CH2 1 
ATOM   8863  N N   . PRO E 1 126 ? 3.744   -71.418 -16.066  1.00 65.48  ? 128 PRO E N   1 
ATOM   8864  C CA  . PRO E 1 126 ? 2.842   -72.302 -15.308  1.00 76.47  ? 128 PRO E CA  1 
ATOM   8865  C C   . PRO E 1 126 ? 2.966   -72.167 -13.799  1.00 86.13  ? 128 PRO E C   1 
ATOM   8866  O O   . PRO E 1 126 ? 2.023   -72.536 -13.087  1.00 77.60  ? 128 PRO E O   1 
ATOM   8867  C CB  . PRO E 1 126 ? 3.253   -73.704 -15.776  1.00 62.00  ? 128 PRO E CB  1 
ATOM   8868  C CG  . PRO E 1 126 ? 4.682   -73.554 -16.167  1.00 63.99  ? 128 PRO E CG  1 
ATOM   8869  C CD  . PRO E 1 126 ? 4.811   -72.172 -16.749  1.00 64.65  ? 128 PRO E CD  1 
ATOM   8870  N N   . ASN E 1 127 ? 4.085   -71.657 -13.286  1.00 72.21  ? 129 ASN E N   1 
ATOM   8871  C CA  . ASN E 1 127 ? 4.313   -71.563 -11.850  1.00 54.90  ? 129 ASN E CA  1 
ATOM   8872  C C   . ASN E 1 127 ? 4.314   -70.116 -11.361  1.00 58.26  ? 129 ASN E C   1 
ATOM   8873  O O   . ASN E 1 127 ? 4.927   -69.799 -10.339  1.00 53.57  ? 129 ASN E O   1 
ATOM   8874  C CB  . ASN E 1 127 ? 5.616   -72.262 -11.471  1.00 59.85  ? 129 ASN E CB  1 
ATOM   8875  C CG  . ASN E 1 127 ? 5.595   -73.745 -11.794  1.00 69.01  ? 129 ASN E CG  1 
ATOM   8876  O OD1 . ASN E 1 127 ? 4.900   -74.524 -11.142  1.00 64.84  ? 129 ASN E OD1 1 
ATOM   8877  N ND2 . ASN E 1 127 ? 6.361   -74.144 -12.805  1.00 71.95  ? 129 ASN E ND2 1 
ATOM   8878  N N   . HIS E 1 128 ? 3.638   -69.232 -12.089  1.00 70.46  ? 130 HIS E N   1 
ATOM   8879  C CA  . HIS E 1 128 ? 3.431   -67.857 -11.662  1.00 58.56  ? 130 HIS E CA  1 
ATOM   8880  C C   . HIS E 1 128 ? 2.014   -67.443 -12.029  1.00 58.18  ? 130 HIS E C   1 
ATOM   8881  O O   . HIS E 1 128 ? 1.382   -68.033 -12.908  1.00 75.28  ? 130 HIS E O   1 
ATOM   8882  C CB  . HIS E 1 128 ? 4.443   -66.892 -12.300  1.00 51.60  ? 130 HIS E CB  1 
ATOM   8883  C CG  . HIS E 1 128 ? 5.872   -67.212 -11.985  1.00 59.50  ? 130 HIS E CG  1 
ATOM   8884  N ND1 . HIS E 1 128 ? 6.566   -68.221 -12.617  1.00 60.78  ? 130 HIS E ND1 1 
ATOM   8885  C CD2 . HIS E 1 128 ? 6.739   -66.651 -11.110  1.00 50.49  ? 130 HIS E CD2 1 
ATOM   8886  C CE1 . HIS E 1 128 ? 7.798   -68.270 -12.142  1.00 65.11  ? 130 HIS E CE1 1 
ATOM   8887  N NE2 . HIS E 1 128 ? 7.929   -67.328 -11.226  1.00 55.65  ? 130 HIS E NE2 1 
ATOM   8888  N N   . GLU E 1 129 ? 1.516   -66.421 -11.341  1.00 50.31  ? 131 GLU E N   1 
ATOM   8889  C CA  . GLU E 1 129 ? 0.201   -65.869 -11.632  1.00 52.07  ? 131 GLU E CA  1 
ATOM   8890  C C   . GLU E 1 129 ? 0.335   -64.792 -12.700  1.00 60.93  ? 131 GLU E C   1 
ATOM   8891  O O   . GLU E 1 129 ? 1.135   -63.863 -12.555  1.00 58.05  ? 131 GLU E O   1 
ATOM   8892  C CB  . GLU E 1 129 ? -0.440  -65.292 -10.369  1.00 48.81  ? 131 GLU E CB  1 
ATOM   8893  C CG  . GLU E 1 129 ? -0.575  -66.281 -9.216   1.00 67.27  ? 131 GLU E CG  1 
ATOM   8894  C CD  . GLU E 1 129 ? -1.805  -67.168 -9.317   1.00 71.91  ? 131 GLU E CD  1 
ATOM   8895  O OE1 . GLU E 1 129 ? -2.114  -67.650 -10.428  1.00 85.38  ? 131 GLU E OE1 1 
ATOM   8896  O OE2 . GLU E 1 129 ? -2.466  -67.382 -8.278   1.00 87.62  ? 131 GLU E OE2 1 
ATOM   8897  N N   . THR E 1 130 ? -0.444  -64.924 -13.775  1.00 58.40  ? 132 THR E N   1 
ATOM   8898  C CA  . THR E 1 130 ? -0.374  -63.997 -14.895  1.00 64.30  ? 132 THR E CA  1 
ATOM   8899  C C   . THR E 1 130 ? -1.562  -63.053 -14.985  1.00 54.38  ? 132 THR E C   1 
ATOM   8900  O O   . THR E 1 130 ? -1.480  -62.054 -15.707  1.00 59.40  ? 132 THR E O   1 
ATOM   8901  C CB  . THR E 1 130 ? -0.264  -64.765 -16.220  1.00 64.94  ? 132 THR E CB  1 
ATOM   8902  O OG1 . THR E 1 130 ? -1.468  -65.510 -16.442  1.00 70.51  ? 132 THR E OG1 1 
ATOM   8903  C CG2 . THR E 1 130 ? 0.918   -65.720 -16.187  1.00 52.35  ? 132 THR E CG2 1 
ATOM   8904  N N   . SER E 1 131 ? -2.653  -63.336 -14.275  1.00 56.54  ? 133 SER E N   1 
ATOM   8905  C CA  . SER E 1 131 ? -3.882  -62.563 -14.384  1.00 53.12  ? 133 SER E CA  1 
ATOM   8906  C C   . SER E 1 131 ? -4.126  -61.659 -13.182  1.00 61.38  ? 133 SER E C   1 
ATOM   8907  O O   . SER E 1 131 ? -5.187  -61.031 -13.098  1.00 57.56  ? 133 SER E O   1 
ATOM   8908  C CB  . SER E 1 131 ? -5.073  -63.505 -14.577  1.00 56.15  ? 133 SER E CB  1 
ATOM   8909  O OG  . SER E 1 131 ? -4.820  -64.439 -15.613  1.00 73.44  ? 133 SER E OG  1 
ATOM   8910  N N   . LEU E 1 132 A -3.179  -61.576 -12.252  1.00 53.09  ? 133 LEU E N   1 
ATOM   8911  C CA  . LEU E 1 132 A -3.334  -60.753 -11.062  1.00 53.55  ? 133 LEU E CA  1 
ATOM   8912  C C   . LEU E 1 132 A -2.527  -59.464 -11.122  1.00 49.35  ? 133 LEU E C   1 
ATOM   8913  O O   . LEU E 1 132 A -2.501  -58.719 -10.138  1.00 60.41  ? 133 LEU E O   1 
ATOM   8914  C CB  . LEU E 1 132 A -2.943  -61.555 -9.818   1.00 53.80  ? 133 LEU E CB  1 
ATOM   8915  C CG  . LEU E 1 132 A -3.756  -62.832 -9.596   1.00 56.66  ? 133 LEU E CG  1 
ATOM   8916  C CD1 . LEU E 1 132 A -3.274  -63.580 -8.363   1.00 45.13  ? 133 LEU E CD1 1 
ATOM   8917  C CD2 . LEU E 1 132 A -5.240  -62.510 -9.490   1.00 45.53  ? 133 LEU E CD2 1 
ATOM   8918  N N   . GLY E 1 133 ? -1.870  -59.186 -12.243  1.00 60.84  ? 134 GLY E N   1 
ATOM   8919  C CA  . GLY E 1 133 ? -1.085  -57.976 -12.380  1.00 58.84  ? 134 GLY E CA  1 
ATOM   8920  C C   . GLY E 1 133 ? -1.865  -56.820 -12.972  1.00 57.95  ? 134 GLY E C   1 
ATOM   8921  O O   . GLY E 1 133 ? -1.584  -56.382 -14.090  1.00 60.82  ? 134 GLY E O   1 
ATOM   8922  N N   . VAL E 1 134 ? -2.850  -56.319 -12.228  1.00 50.46  ? 135 VAL E N   1 
ATOM   8923  C CA  . VAL E 1 134 ? -3.651  -55.181 -12.651  1.00 47.27  ? 135 VAL E CA  1 
ATOM   8924  C C   . VAL E 1 134 ? -3.560  -54.100 -11.582  1.00 48.49  ? 135 VAL E C   1 
ATOM   8925  O O   . VAL E 1 134 ? -3.306  -54.371 -10.406  1.00 54.69  ? 135 VAL E O   1 
ATOM   8926  C CB  . VAL E 1 134 ? -5.122  -55.562 -12.919  1.00 57.45  ? 135 VAL E CB  1 
ATOM   8927  C CG1 . VAL E 1 134 ? -5.221  -56.476 -14.130  1.00 47.56  ? 135 VAL E CG1 1 
ATOM   8928  C CG2 . VAL E 1 134 ? -5.733  -56.229 -11.694  1.00 42.61  ? 135 VAL E CG2 1 
ATOM   8929  N N   . SER E 1 135 ? -3.772  -52.856 -12.009  1.00 46.22  ? 136 SER E N   1 
ATOM   8930  C CA  . SER E 1 135 ? -3.627  -51.711 -11.125  1.00 40.52  ? 136 SER E CA  1 
ATOM   8931  C C   . SER E 1 135 ? -4.656  -50.649 -11.481  1.00 49.12  ? 136 SER E C   1 
ATOM   8932  O O   . SER E 1 135 ? -5.066  -50.522 -12.638  1.00 50.74  ? 136 SER E O   1 
ATOM   8933  C CB  . SER E 1 135 ? -2.215  -51.117 -11.208  1.00 39.73  ? 136 SER E CB  1 
ATOM   8934  O OG  . SER E 1 135 ? -2.206  -49.764 -10.785  1.00 52.86  ? 136 SER E OG  1 
ATOM   8935  N N   . ALA E 1 136 ? -5.064  -49.882 -10.466  1.00 42.87  ? 137 ALA E N   1 
ATOM   8936  C CA  . ALA E 1 136 ? -5.959  -48.755 -10.692  1.00 42.37  ? 137 ALA E CA  1 
ATOM   8937  C C   . ALA E 1 136 ? -5.265  -47.605 -11.409  1.00 49.97  ? 137 ALA E C   1 
ATOM   8938  O O   . ALA E 1 136 ? -5.946  -46.716 -11.932  1.00 48.65  ? 137 ALA E O   1 
ATOM   8939  C CB  . ALA E 1 136 ? -6.537  -48.270 -9.362   1.00 28.67  ? 137 ALA E CB  1 
ATOM   8940  N N   . ALA E 1 137 ? -3.929  -47.597 -11.436  1.00 49.46  ? 138 ALA E N   1 
ATOM   8941  C CA  . ALA E 1 137 ? -3.211  -46.587 -12.206  1.00 56.65  ? 138 ALA E CA  1 
ATOM   8942  C C   . ALA E 1 137 ? -3.457  -46.740 -13.700  1.00 54.06  ? 138 ALA E C   1 
ATOM   8943  O O   . ALA E 1 137 ? -3.336  -45.765 -14.451  1.00 55.36  ? 138 ALA E O   1 
ATOM   8944  C CB  . ALA E 1 137 ? -1.713  -46.662 -11.913  1.00 56.05  ? 138 ALA E CB  1 
ATOM   8945  N N   . CYS E 1 138 ? -3.815  -47.944 -14.147  1.00 48.21  ? 139 CYS E N   1 
ATOM   8946  C CA  . CYS E 1 138 ? -4.056  -48.241 -15.556  1.00 58.08  ? 139 CYS E CA  1 
ATOM   8947  C C   . CYS E 1 138 ? -5.487  -48.743 -15.717  1.00 54.21  ? 139 CYS E C   1 
ATOM   8948  O O   . CYS E 1 138 ? -5.713  -49.925 -16.006  1.00 51.30  ? 139 CYS E O   1 
ATOM   8949  C CB  . CYS E 1 138 ? -3.057  -49.272 -16.078  1.00 57.43  ? 139 CYS E CB  1 
ATOM   8950  S SG  . CYS E 1 138 ? -1.340  -48.727 -16.043  1.00 88.10  ? 139 CYS E SG  1 
ATOM   8951  N N   . PRO E 1 139 ? -6.476  -47.872 -15.530  1.00 50.11  ? 140 PRO E N   1 
ATOM   8952  C CA  . PRO E 1 139 ? -7.869  -48.319 -15.607  1.00 42.88  ? 140 PRO E CA  1 
ATOM   8953  C C   . PRO E 1 139 ? -8.281  -48.637 -17.035  1.00 52.28  ? 140 PRO E C   1 
ATOM   8954  O O   . PRO E 1 139 ? -7.728  -48.110 -18.003  1.00 56.64  ? 140 PRO E O   1 
ATOM   8955  C CB  . PRO E 1 139 ? -8.652  -47.120 -15.061  1.00 42.90  ? 140 PRO E CB  1 
ATOM   8956  C CG  . PRO E 1 139 ? -7.812  -45.951 -15.442  1.00 32.45  ? 140 PRO E CG  1 
ATOM   8957  C CD  . PRO E 1 139 ? -6.379  -46.412 -15.347  1.00 43.91  ? 140 PRO E CD  1 
ATOM   8958  N N   . TYR E 1 140 ? -9.263  -49.525 -17.154  1.00 56.81  ? 141 TYR E N   1 
ATOM   8959  C CA  . TYR E 1 140 ? -9.930  -49.791 -18.419  1.00 52.80  ? 141 TYR E CA  1 
ATOM   8960  C C   . TYR E 1 140 ? -11.396 -50.037 -18.125  1.00 53.75  ? 141 TYR E C   1 
ATOM   8961  O O   . TYR E 1 140 ? -11.724 -50.906 -17.315  1.00 52.14  ? 141 TYR E O   1 
ATOM   8962  C CB  . TYR E 1 140 ? -9.316  -50.995 -19.145  1.00 51.62  ? 141 TYR E CB  1 
ATOM   8963  C CG  . TYR E 1 140 ? -10.016 -51.340 -20.437  1.00 51.27  ? 141 TYR E CG  1 
ATOM   8964  C CD1 . TYR E 1 140 ? -9.950  -50.488 -21.533  1.00 57.48  ? 141 TYR E CD1 1 
ATOM   8965  C CD2 . TYR E 1 140 ? -10.740 -52.516 -20.564  1.00 49.02  ? 141 TYR E CD2 1 
ATOM   8966  C CE1 . TYR E 1 140 ? -10.590 -50.800 -22.719  1.00 52.61  ? 141 TYR E CE1 1 
ATOM   8967  C CE2 . TYR E 1 140 ? -11.382 -52.836 -21.744  1.00 63.11  ? 141 TYR E CE2 1 
ATOM   8968  C CZ  . TYR E 1 140 ? -11.304 -51.975 -22.819  1.00 65.93  ? 141 TYR E CZ  1 
ATOM   8969  O OH  . TYR E 1 140 ? -11.943 -52.292 -23.995  1.00 79.07  ? 141 TYR E OH  1 
ATOM   8970  N N   . GLN E 1 141 ? -12.267 -49.262 -18.769  1.00 58.54  ? 142 GLN E N   1 
ATOM   8971  C CA  . GLN E 1 141 ? -13.704 -49.274 -18.477  1.00 50.41  ? 142 GLN E CA  1 
ATOM   8972  C C   . GLN E 1 141 ? -13.973 -48.941 -17.012  1.00 57.36  ? 142 GLN E C   1 
ATOM   8973  O O   . GLN E 1 141 ? -15.004 -49.315 -16.455  1.00 54.10  ? 142 GLN E O   1 
ATOM   8974  C CB  . GLN E 1 141 ? -14.340 -50.611 -18.855  1.00 48.61  ? 142 GLN E CB  1 
ATOM   8975  C CG  . GLN E 1 141 ? -14.593 -50.786 -20.345  1.00 51.92  ? 142 GLN E CG  1 
ATOM   8976  C CD  . GLN E 1 141 ? -14.719 -52.241 -20.752  1.00 73.52  ? 142 GLN E CD  1 
ATOM   8977  O OE1 . GLN E 1 141 ? -14.246 -53.133 -20.049  1.00 52.77  ? 142 GLN E OE1 1 
ATOM   8978  N NE2 . GLN E 1 141 ? -15.362 -52.487 -21.889  1.00 85.03  ? 142 GLN E NE2 1 
ATOM   8979  N N   . GLY E 1 142 ? -13.031 -48.234 -16.383  1.00 47.16  ? 143 GLY E N   1 
ATOM   8980  C CA  . GLY E 1 142 ? -13.155 -47.783 -15.019  1.00 51.49  ? 143 GLY E CA  1 
ATOM   8981  C C   . GLY E 1 142 ? -12.437 -48.643 -13.993  1.00 50.83  ? 143 GLY E C   1 
ATOM   8982  O O   . GLY E 1 142 ? -11.986 -48.123 -12.965  1.00 63.49  ? 143 GLY E O   1 
ATOM   8983  N N   . THR E 1 143 ? -12.313 -49.938 -14.253  1.00 54.39  ? 144 THR E N   1 
ATOM   8984  C CA  . THR E 1 143 ? -11.759 -50.901 -13.313  1.00 54.29  ? 144 THR E CA  1 
ATOM   8985  C C   . THR E 1 143 ? -10.302 -51.204 -13.645  1.00 53.42  ? 144 THR E C   1 
ATOM   8986  O O   . THR E 1 143 ? -9.851  -50.976 -14.773  1.00 57.33  ? 144 THR E O   1 
ATOM   8987  C CB  . THR E 1 143 ? -12.590 -52.189 -13.333  1.00 53.50  ? 144 THR E CB  1 
ATOM   8988  O OG1 . THR E 1 143 ? -12.426 -52.860 -14.586  1.00 49.18  ? 144 THR E OG1 1 
ATOM   8989  C CG2 . THR E 1 143 ? -14.062 -51.862 -13.126  1.00 53.15  ? 144 THR E CG2 1 
ATOM   8990  N N   . PRO E 1 144 ? -9.529  -51.707 -12.676  1.00 46.35  ? 145 PRO E N   1 
ATOM   8991  C CA  . PRO E 1 144 ? -8.079  -51.847 -12.883  1.00 57.46  ? 145 PRO E CA  1 
ATOM   8992  C C   . PRO E 1 144 ? -7.728  -52.750 -14.057  1.00 46.61  ? 145 PRO E C   1 
ATOM   8993  O O   . PRO E 1 144 ? -8.400  -53.746 -14.329  1.00 50.85  ? 145 PRO E O   1 
ATOM   8994  C CB  . PRO E 1 144 ? -7.592  -52.445 -11.558  1.00 50.24  ? 145 PRO E CB  1 
ATOM   8995  C CG  . PRO E 1 144 ? -8.584  -51.995 -10.556  1.00 37.11  ? 145 PRO E CG  1 
ATOM   8996  C CD  . PRO E 1 144 ? -9.905  -51.987 -11.277  1.00 43.52  ? 145 PRO E CD  1 
ATOM   8997  N N   . SER E 1 145 ? -6.655  -52.383 -14.748  1.00 60.45  ? 146 SER E N   1 
ATOM   8998  C CA  . SER E 1 145 ? -6.102  -53.143 -15.865  1.00 55.02  ? 146 SER E CA  1 
ATOM   8999  C C   . SER E 1 145 ? -4.595  -52.896 -15.875  1.00 58.18  ? 146 SER E C   1 
ATOM   9000  O O   . SER E 1 145 ? -4.024  -52.454 -14.872  1.00 60.39  ? 146 SER E O   1 
ATOM   9001  C CB  . SER E 1 145 ? -6.800  -52.759 -17.181  1.00 57.66  ? 146 SER E CB  1 
ATOM   9002  O OG  . SER E 1 145 ? -6.423  -53.630 -18.235  1.00 52.85  ? 146 SER E OG  1 
ATOM   9003  N N   . PHE E 1 146 ? -3.942  -53.186 -16.997  1.00 51.37  ? 147 PHE E N   1 
ATOM   9004  C CA  . PHE E 1 146 ? -2.495  -53.035 -17.091  1.00 44.21  ? 147 PHE E CA  1 
ATOM   9005  C C   . PHE E 1 146 ? -2.119  -52.836 -18.555  1.00 52.99  ? 147 PHE E C   1 
ATOM   9006  O O   . PHE E 1 146 ? -2.973  -52.880 -19.446  1.00 46.77  ? 147 PHE E O   1 
ATOM   9007  C CB  . PHE E 1 146 ? -1.785  -54.245 -16.477  1.00 41.50  ? 147 PHE E CB  1 
ATOM   9008  C CG  . PHE E 1 146 ? -0.325  -54.026 -16.217  1.00 54.70  ? 147 PHE E CG  1 
ATOM   9009  C CD1 . PHE E 1 146 ? 0.093   -53.030 -15.352  1.00 49.17  ? 147 PHE E CD1 1 
ATOM   9010  C CD2 . PHE E 1 146 ? 0.629   -54.820 -16.829  1.00 54.14  ? 147 PHE E CD2 1 
ATOM   9011  C CE1 . PHE E 1 146 ? 1.438   -52.824 -15.107  1.00 51.68  ? 147 PHE E CE1 1 
ATOM   9012  C CE2 . PHE E 1 146 ? 1.976   -54.620 -16.587  1.00 54.76  ? 147 PHE E CE2 1 
ATOM   9013  C CZ  . PHE E 1 146 ? 2.380   -53.620 -15.725  1.00 49.75  ? 147 PHE E CZ  1 
ATOM   9014  N N   . PHE E 1 147 ? -0.830  -52.589 -18.794  1.00 51.89  ? 148 PHE E N   1 
ATOM   9015  C CA  . PHE E 1 147 ? -0.318  -52.527 -20.157  1.00 42.60  ? 148 PHE E CA  1 
ATOM   9016  C C   . PHE E 1 147 ? -0.599  -53.842 -20.874  1.00 53.46  ? 148 PHE E C   1 
ATOM   9017  O O   . PHE E 1 147 ? -0.357  -54.923 -20.330  1.00 61.85  ? 148 PHE E O   1 
ATOM   9018  C CB  . PHE E 1 147 ? 1.184   -52.239 -20.152  1.00 39.27  ? 148 PHE E CB  1 
ATOM   9019  C CG  . PHE E 1 147 ? 1.551   -50.898 -19.581  1.00 50.55  ? 148 PHE E CG  1 
ATOM   9020  C CD1 . PHE E 1 147 ? 1.322   -49.736 -20.299  1.00 45.82  ? 148 PHE E CD1 1 
ATOM   9021  C CD2 . PHE E 1 147 ? 2.147   -50.801 -18.334  1.00 46.88  ? 148 PHE E CD2 1 
ATOM   9022  C CE1 . PHE E 1 147 ? 1.667   -48.502 -19.779  1.00 52.65  ? 148 PHE E CE1 1 
ATOM   9023  C CE2 . PHE E 1 147 ? 2.496   -49.571 -17.808  1.00 43.56  ? 148 PHE E CE2 1 
ATOM   9024  C CZ  . PHE E 1 147 ? 2.255   -48.420 -18.532  1.00 49.06  ? 148 PHE E CZ  1 
ATOM   9025  N N   . ARG E 1 148 ? -1.114  -53.748 -22.100  1.00 52.59  ? 149 ARG E N   1 
ATOM   9026  C CA  . ARG E 1 148 ? -1.593  -54.942 -22.788  1.00 45.09  ? 149 ARG E CA  1 
ATOM   9027  C C   . ARG E 1 148 ? -0.462  -55.797 -23.350  1.00 53.46  ? 149 ARG E C   1 
ATOM   9028  O O   . ARG E 1 148 ? -0.629  -57.015 -23.487  1.00 59.21  ? 149 ARG E O   1 
ATOM   9029  C CB  . ARG E 1 148 ? -2.556  -54.554 -23.910  1.00 57.31  ? 149 ARG E CB  1 
ATOM   9030  C CG  . ARG E 1 148 ? -3.835  -53.871 -23.441  1.00 57.74  ? 149 ARG E CG  1 
ATOM   9031  C CD  . ARG E 1 148 ? -5.006  -54.253 -24.340  1.00 81.65  ? 149 ARG E CD  1 
ATOM   9032  N NE  . ARG E 1 148 ? -5.822  -53.106 -24.723  1.00 91.26  ? 149 ARG E NE  1 
ATOM   9033  C CZ  . ARG E 1 148 ? -7.015  -52.828 -24.213  1.00 94.18  ? 149 ARG E CZ  1 
ATOM   9034  N NH1 . ARG E 1 148 ? -7.567  -53.594 -23.286  1.00 88.13  ? 149 ARG E NH1 1 
ATOM   9035  N NH2 . ARG E 1 148 ? -7.672  -51.757 -24.648  1.00 96.64  ? 149 ARG E NH2 1 
ATOM   9036  N N   . ASN E 1 149 ? 0.676   -55.196 -23.690  1.00 57.79  ? 150 ASN E N   1 
ATOM   9037  C CA  . ASN E 1 149 ? 1.745   -55.907 -24.383  1.00 47.47  ? 150 ASN E CA  1 
ATOM   9038  C C   . ASN E 1 149 ? 2.772   -56.532 -23.445  1.00 55.56  ? 150 ASN E C   1 
ATOM   9039  O O   . ASN E 1 149 ? 3.673   -57.231 -23.920  1.00 59.17  ? 150 ASN E O   1 
ATOM   9040  C CB  . ASN E 1 149 ? 2.451   -54.965 -25.364  1.00 59.36  ? 150 ASN E CB  1 
ATOM   9041  C CG  . ASN E 1 149 ? 1.532   -54.484 -26.471  1.00 55.92  ? 150 ASN E CG  1 
ATOM   9042  O OD1 . ASN E 1 149 ? 0.640   -55.208 -26.915  1.00 62.10  ? 150 ASN E OD1 1 
ATOM   9043  N ND2 . ASN E 1 149 ? 1.746   -53.254 -26.922  1.00 58.79  ? 150 ASN E ND2 1 
ATOM   9044  N N   . VAL E 1 150 ? 2.664   -56.309 -22.134  1.00 51.81  ? 151 VAL E N   1 
ATOM   9045  C CA  . VAL E 1 150 ? 3.579   -56.893 -21.164  1.00 50.35  ? 151 VAL E CA  1 
ATOM   9046  C C   . VAL E 1 150 ? 2.767   -57.530 -20.044  1.00 53.20  ? 151 VAL E C   1 
ATOM   9047  O O   . VAL E 1 150 ? 1.608   -57.182 -19.809  1.00 57.74  ? 151 VAL E O   1 
ATOM   9048  C CB  . VAL E 1 150 ? 4.575   -55.857 -20.593  1.00 55.11  ? 151 VAL E CB  1 
ATOM   9049  C CG1 . VAL E 1 150 ? 5.523   -55.375 -21.684  1.00 44.15  ? 151 VAL E CG1 1 
ATOM   9050  C CG2 . VAL E 1 150 ? 3.833   -54.687 -19.969  1.00 50.53  ? 151 VAL E CG2 1 
ATOM   9051  N N   . VAL E 1 151 ? 3.393   -58.478 -19.351  1.00 48.97  ? 152 VAL E N   1 
ATOM   9052  C CA  . VAL E 1 151 ? 2.737   -59.276 -18.322  1.00 41.88  ? 152 VAL E CA  1 
ATOM   9053  C C   . VAL E 1 151 ? 3.396   -58.986 -16.981  1.00 49.73  ? 152 VAL E C   1 
ATOM   9054  O O   . VAL E 1 151 ? 4.627   -59.018 -16.866  1.00 51.83  ? 152 VAL E O   1 
ATOM   9055  C CB  . VAL E 1 151 ? 2.795   -60.781 -18.642  1.00 45.41  ? 152 VAL E CB  1 
ATOM   9056  C CG1 . VAL E 1 151 ? 1.903   -61.559 -17.687  1.00 49.76  ? 152 VAL E CG1 1 
ATOM   9057  C CG2 . VAL E 1 151 ? 2.389   -61.033 -20.082  1.00 65.05  ? 152 VAL E CG2 1 
ATOM   9058  N N   . TRP E 1 152 ? 2.574   -58.701 -15.975  1.00 47.90  ? 153 TRP E N   1 
ATOM   9059  C CA  . TRP E 1 152 ? 3.027   -58.431 -14.613  1.00 40.67  ? 153 TRP E CA  1 
ATOM   9060  C C   . TRP E 1 152 ? 2.898   -59.726 -13.816  1.00 50.18  ? 153 TRP E C   1 
ATOM   9061  O O   . TRP E 1 152 ? 1.820   -60.056 -13.314  1.00 52.50  ? 153 TRP E O   1 
ATOM   9062  C CB  . TRP E 1 152 ? 2.208   -57.298 -14.001  1.00 46.57  ? 153 TRP E CB  1 
ATOM   9063  C CG  . TRP E 1 152 ? 2.667   -56.829 -12.651  1.00 60.98  ? 153 TRP E CG  1 
ATOM   9064  C CD1 . TRP E 1 152 ? 3.705   -57.321 -11.911  1.00 49.72  ? 153 TRP E CD1 1 
ATOM   9065  C CD2 . TRP E 1 152 ? 2.096   -55.764 -11.881  1.00 55.99  ? 153 TRP E CD2 1 
ATOM   9066  N NE1 . TRP E 1 152 ? 3.813   -56.628 -10.729  1.00 49.08  ? 153 TRP E NE1 1 
ATOM   9067  C CE2 . TRP E 1 152 ? 2.837   -55.668 -10.687  1.00 45.86  ? 153 TRP E CE2 1 
ATOM   9068  C CE3 . TRP E 1 152 ? 1.029   -54.882 -12.086  1.00 56.59  ? 153 TRP E CE3 1 
ATOM   9069  C CZ2 . TRP E 1 152 ? 2.546   -54.727 -9.703   1.00 49.26  ? 153 TRP E CZ2 1 
ATOM   9070  C CZ3 . TRP E 1 152 ? 0.743   -53.949 -11.107  1.00 49.87  ? 153 TRP E CZ3 1 
ATOM   9071  C CH2 . TRP E 1 152 ? 1.498   -53.879 -9.931   1.00 47.53  ? 153 TRP E CH2 1 
ATOM   9072  N N   . LEU E 1 153 ? 4.003   -60.457 -13.700  1.00 43.33  ? 154 LEU E N   1 
ATOM   9073  C CA  . LEU E 1 153 ? 3.993   -61.755 -13.041  1.00 39.45  ? 154 LEU E CA  1 
ATOM   9074  C C   . LEU E 1 153 ? 3.956   -61.599 -11.526  1.00 53.04  ? 154 LEU E C   1 
ATOM   9075  O O   . LEU E 1 153 ? 4.579   -60.696 -10.961  1.00 58.69  ? 154 LEU E O   1 
ATOM   9076  C CB  . LEU E 1 153 ? 5.217   -62.570 -13.458  1.00 41.86  ? 154 LEU E CB  1 
ATOM   9077  C CG  . LEU E 1 153 ? 5.280   -62.904 -14.951  1.00 46.97  ? 154 LEU E CG  1 
ATOM   9078  C CD1 . LEU E 1 153 ? 6.590   -63.580 -15.311  1.00 53.54  ? 154 LEU E CD1 1 
ATOM   9079  C CD2 . LEU E 1 153 ? 4.098   -63.774 -15.356  1.00 42.50  ? 154 LEU E CD2 1 
ATOM   9080  N N   . ILE E 1 154 ? 3.219   -62.498 -10.873  1.00 55.93  ? 155 ILE E N   1 
ATOM   9081  C CA  . ILE E 1 154 ? 3.011   -62.480 -9.432   1.00 48.84  ? 155 ILE E CA  1 
ATOM   9082  C C   . ILE E 1 154 ? 3.305   -63.875 -8.893   1.00 50.12  ? 155 ILE E C   1 
ATOM   9083  O O   . ILE E 1 154 ? 3.235   -64.873 -9.613   1.00 53.71  ? 155 ILE E O   1 
ATOM   9084  C CB  . ILE E 1 154 ? 1.572   -62.034 -9.068   1.00 54.49  ? 155 ILE E CB  1 
ATOM   9085  C CG1 . ILE E 1 154 ? 1.244   -60.700 -9.740   1.00 52.04  ? 155 ILE E CG1 1 
ATOM   9086  C CG2 . ILE E 1 154 ? 1.388   -61.884 -7.565   1.00 48.18  ? 155 ILE E CG2 1 
ATOM   9087  C CD1 . ILE E 1 154 ? 2.077   -59.545 -9.236   1.00 45.67  ? 155 ILE E CD1 1 
ATOM   9088  N N   . LYS E 1 155 ? 3.650   -63.931 -7.608   1.00 54.08  ? 156 LYS E N   1 
ATOM   9089  C CA  . LYS E 1 155 ? 3.935   -65.202 -6.958   1.00 56.11  ? 156 LYS E CA  1 
ATOM   9090  C C   . LYS E 1 155 ? 2.700   -66.097 -6.966   1.00 51.66  ? 156 LYS E C   1 
ATOM   9091  O O   . LYS E 1 155 ? 1.560   -65.625 -6.962   1.00 48.30  ? 156 LYS E O   1 
ATOM   9092  C CB  . LYS E 1 155 ? 4.400   -64.970 -5.519   1.00 47.33  ? 156 LYS E CB  1 
ATOM   9093  C CG  . LYS E 1 155 ? 3.271   -64.643 -4.548   1.00 44.88  ? 156 LYS E CG  1 
ATOM   9094  C CD  . LYS E 1 155 ? 3.788   -64.337 -3.153   1.00 58.71  ? 156 LYS E CD  1 
ATOM   9095  C CE  . LYS E 1 155 ? 2.641   -64.219 -2.161   1.00 48.14  ? 156 LYS E CE  1 
ATOM   9096  N NZ  . LYS E 1 155 ? 3.073   -63.618 -0.869   1.00 56.10  ? 156 LYS E NZ  1 
ATOM   9097  N N   . LYS E 1 156 ? 2.939   -67.405 -6.987   1.00 61.43  ? 157 LYS E N   1 
ATOM   9098  C CA  . LYS E 1 156 ? 1.875   -68.400 -6.982   1.00 61.59  ? 157 LYS E CA  1 
ATOM   9099  C C   . LYS E 1 156 ? 2.110   -69.361 -5.828   1.00 55.57  ? 157 LYS E C   1 
ATOM   9100  O O   . LYS E 1 156 ? 3.216   -69.891 -5.678   1.00 68.41  ? 157 LYS E O   1 
ATOM   9101  C CB  . LYS E 1 156 ? 1.825   -69.164 -8.309   1.00 58.79  ? 157 LYS E CB  1 
ATOM   9102  C CG  . LYS E 1 156 ? 0.657   -70.126 -8.437   1.00 55.21  ? 157 LYS E CG  1 
ATOM   9103  C CD  . LYS E 1 156 ? 0.733   -70.864 -9.759   1.00 61.82  ? 157 LYS E CD  1 
ATOM   9104  C CE  . LYS E 1 156 ? -0.645  -71.237 -10.272  1.00 75.46  ? 157 LYS E CE  1 
ATOM   9105  N NZ  . LYS E 1 156 ? -0.588  -71.716 -11.682  1.00 88.41  ? 157 LYS E NZ  1 
ATOM   9106  N N   . ASN E 1 157 ? 1.069   -69.586 -5.023   1.00 70.27  ? 158 ASN E N   1 
ATOM   9107  C CA  . ASN E 1 157 ? 1.153   -70.441 -3.839   1.00 57.87  ? 158 ASN E CA  1 
ATOM   9108  C C   . ASN E 1 157 ? 2.272   -69.981 -2.906   1.00 64.43  ? 158 ASN E C   1 
ATOM   9109  O O   . ASN E 1 157 ? 3.047   -70.790 -2.390   1.00 66.42  ? 158 ASN E O   1 
ATOM   9110  C CB  . ASN E 1 157 ? 1.333   -71.908 -4.228   1.00 58.37  ? 158 ASN E CB  1 
ATOM   9111  C CG  . ASN E 1 157 ? 0.349   -72.352 -5.292   1.00 75.60  ? 158 ASN E CG  1 
ATOM   9112  O OD1 . ASN E 1 157 ? 0.726   -72.988 -6.276   1.00 77.77  ? 158 ASN E OD1 1 
ATOM   9113  N ND2 . ASN E 1 157 ? -0.920  -72.016 -5.101   1.00 83.67  ? 158 ASN E ND2 1 
ATOM   9114  N N   . ASP E 1 158 ? 2.355   -68.665 -2.700   1.00 53.54  ? 159 ASP E N   1 
ATOM   9115  C CA  . ASP E 1 158 ? 3.370   -68.050 -1.842   1.00 61.24  ? 159 ASP E CA  1 
ATOM   9116  C C   . ASP E 1 158 ? 4.780   -68.455 -2.270   1.00 62.47  ? 159 ASP E C   1 
ATOM   9117  O O   . ASP E 1 158 ? 5.662   -68.693 -1.443   1.00 61.02  ? 159 ASP E O   1 
ATOM   9118  C CB  . ASP E 1 158 ? 3.130   -68.391 -0.369   1.00 48.51  ? 159 ASP E CB  1 
ATOM   9119  C CG  . ASP E 1 158 ? 3.890   -67.474 0.576    1.00 78.58  ? 159 ASP E CG  1 
ATOM   9120  O OD1 . ASP E 1 158 ? 4.158   -66.313 0.197    1.00 75.69  ? 159 ASP E OD1 1 
ATOM   9121  O OD2 . ASP E 1 158 ? 4.230   -67.919 1.695    1.00 91.96  ? 159 ASP E OD2 1 
ATOM   9122  N N   . ALA E 1 159 ? 4.997   -68.532 -3.580   1.00 62.52  ? 160 ALA E N   1 
ATOM   9123  C CA  . ALA E 1 159 ? 6.295   -68.923 -4.108   1.00 47.86  ? 160 ALA E CA  1 
ATOM   9124  C C   . ALA E 1 159 ? 6.517   -68.247 -5.450   1.00 57.04  ? 160 ALA E C   1 
ATOM   9125  O O   . ALA E 1 159 ? 5.587   -68.124 -6.253   1.00 63.05  ? 160 ALA E O   1 
ATOM   9126  C CB  . ALA E 1 159 ? 6.404   -70.445 -4.255   1.00 48.39  ? 160 ALA E CB  1 
ATOM   9127  N N   . TYR E 1 160 ? 7.753   -67.811 -5.684   1.00 59.50  ? 161 TYR E N   1 
ATOM   9128  C CA  . TYR E 1 160 ? 8.163   -67.224 -6.958   1.00 50.00  ? 161 TYR E CA  1 
ATOM   9129  C C   . TYR E 1 160 ? 9.401   -67.976 -7.421   1.00 44.74  ? 161 TYR E C   1 
ATOM   9130  O O   . TYR E 1 160 ? 10.534  -67.554 -7.149   1.00 47.56  ? 161 TYR E O   1 
ATOM   9131  C CB  . TYR E 1 160 ? 8.438   -65.728 -6.824   1.00 49.55  ? 161 TYR E CB  1 
ATOM   9132  C CG  . TYR E 1 160 ? 8.490   -64.974 -8.139   1.00 52.87  ? 161 TYR E CG  1 
ATOM   9133  C CD1 . TYR E 1 160 ? 9.543   -65.153 -9.027   1.00 46.61  ? 161 TYR E CD1 1 
ATOM   9134  C CD2 . TYR E 1 160 ? 7.493   -64.069 -8.482   1.00 56.23  ? 161 TYR E CD2 1 
ATOM   9135  C CE1 . TYR E 1 160 ? 9.594   -64.464 -10.225  1.00 53.54  ? 161 TYR E CE1 1 
ATOM   9136  C CE2 . TYR E 1 160 ? 7.537   -63.373 -9.678   1.00 57.34  ? 161 TYR E CE2 1 
ATOM   9137  C CZ  . TYR E 1 160 ? 8.590   -63.574 -10.544  1.00 58.91  ? 161 TYR E CZ  1 
ATOM   9138  O OH  . TYR E 1 160 ? 8.637   -62.883 -11.733  1.00 46.99  ? 161 TYR E OH  1 
ATOM   9139  N N   . PRO E 1 161 ? 9.226   -69.106 -8.104   1.00 55.66  ? 162 PRO E N   1 
ATOM   9140  C CA  . PRO E 1 161 ? 10.387  -69.824 -8.638   1.00 54.62  ? 162 PRO E CA  1 
ATOM   9141  C C   . PRO E 1 161 ? 11.129  -68.973 -9.656   1.00 46.69  ? 162 PRO E C   1 
ATOM   9142  O O   . PRO E 1 161 ? 10.542  -68.130 -10.338  1.00 56.17  ? 162 PRO E O   1 
ATOM   9143  C CB  . PRO E 1 161 ? 9.771   -71.069 -9.288   1.00 46.29  ? 162 PRO E CB  1 
ATOM   9144  C CG  . PRO E 1 161 ? 8.425   -71.216 -8.648   1.00 54.29  ? 162 PRO E CG  1 
ATOM   9145  C CD  . PRO E 1 161 ? 7.964   -69.819 -8.362   1.00 52.62  ? 162 PRO E CD  1 
ATOM   9146  N N   . THR E 1 162 ? 12.439  -69.192 -9.740   1.00 55.93  ? 163 THR E N   1 
ATOM   9147  C CA  . THR E 1 162 ? 13.271  -68.403 -10.637  1.00 46.40  ? 163 THR E CA  1 
ATOM   9148  C C   . THR E 1 162 ? 12.906  -68.692 -12.087  1.00 54.58  ? 163 THR E C   1 
ATOM   9149  O O   . THR E 1 162 ? 12.733  -69.850 -12.480  1.00 64.13  ? 163 THR E O   1 
ATOM   9150  C CB  . THR E 1 162 ? 14.750  -68.699 -10.390  1.00 51.87  ? 163 THR E CB  1 
ATOM   9151  O OG1 . THR E 1 162 ? 15.091  -68.323 -9.050   1.00 74.05  ? 163 THR E OG1 1 
ATOM   9152  C CG2 . THR E 1 162 ? 15.626  -67.921 -11.362  1.00 56.40  ? 163 THR E CG2 1 
ATOM   9153  N N   . ILE E 1 163 ? 12.783  -67.632 -12.878  1.00 57.88  ? 164 ILE E N   1 
ATOM   9154  C CA  . ILE E 1 163 ? 12.399  -67.732 -14.280  1.00 53.27  ? 164 ILE E CA  1 
ATOM   9155  C C   . ILE E 1 163 ? 13.653  -67.833 -15.134  1.00 48.20  ? 164 ILE E C   1 
ATOM   9156  O O   . ILE E 1 163 ? 14.592  -67.048 -14.967  1.00 59.03  ? 164 ILE E O   1 
ATOM   9157  C CB  . ILE E 1 163 ? 11.545  -66.525 -14.697  1.00 51.82  ? 164 ILE E CB  1 
ATOM   9158  C CG1 . ILE E 1 163 ? 10.189  -66.571 -13.995  1.00 53.76  ? 164 ILE E CG1 1 
ATOM   9159  C CG2 . ILE E 1 163 ? 11.390  -66.480 -16.210  1.00 49.38  ? 164 ILE E CG2 1 
ATOM   9160  C CD1 . ILE E 1 163 ? 9.476   -65.243 -13.967  1.00 61.34  ? 164 ILE E CD1 1 
ATOM   9161  N N   . LYS E 1 164 ? 13.676  -68.809 -16.038  1.00 52.22  ? 165 LYS E N   1 
ATOM   9162  C CA  . LYS E 1 164 ? 14.749  -68.968 -17.019  1.00 50.28  ? 165 LYS E CA  1 
ATOM   9163  C C   . LYS E 1 164 ? 14.089  -69.232 -18.367  1.00 57.59  ? 165 LYS E C   1 
ATOM   9164  O O   . LYS E 1 164 ? 13.750  -70.377 -18.683  1.00 66.20  ? 165 LYS E O   1 
ATOM   9165  C CB  . LYS E 1 164 ? 15.692  -70.105 -16.638  1.00 54.07  ? 165 LYS E CB  1 
ATOM   9166  C CG  . LYS E 1 164 ? 16.491  -69.881 -15.371  1.00 62.87  ? 165 LYS E CG  1 
ATOM   9167  C CD  . LYS E 1 164 ? 16.693  -71.198 -14.646  1.00 87.88  ? 165 LYS E CD  1 
ATOM   9168  C CE  . LYS E 1 164 ? 17.868  -71.144 -13.687  1.00 78.99  ? 165 LYS E CE  1 
ATOM   9169  N NZ  . LYS E 1 164 ? 17.966  -72.400 -12.889  1.00 88.88  ? 165 LYS E NZ  1 
ATOM   9170  N N   . ILE E 1 165 ? 13.902  -68.183 -19.162  1.00 52.10  ? 166 ILE E N   1 
ATOM   9171  C CA  . ILE E 1 165 ? 13.213  -68.289 -20.440  1.00 52.64  ? 166 ILE E CA  1 
ATOM   9172  C C   . ILE E 1 165 ? 14.029  -67.569 -21.505  1.00 56.37  ? 166 ILE E C   1 
ATOM   9173  O O   . ILE E 1 165 ? 14.660  -66.542 -21.232  1.00 58.62  ? 166 ILE E O   1 
ATOM   9174  C CB  . ILE E 1 165 ? 11.776  -67.725 -20.362  1.00 51.23  ? 166 ILE E CB  1 
ATOM   9175  C CG1 . ILE E 1 165 ? 10.992  -68.068 -21.631  1.00 66.97  ? 166 ILE E CG1 1 
ATOM   9176  C CG2 . ILE E 1 165 ? 11.791  -66.219 -20.114  1.00 43.62  ? 166 ILE E CG2 1 
ATOM   9177  C CD1 . ILE E 1 165 ? 9.495   -67.922 -21.479  1.00 66.19  ? 166 ILE E CD1 1 
ATOM   9178  N N   . SER E 1 166 ? 14.040  -68.129 -22.712  1.00 57.77  ? 167 SER E N   1 
ATOM   9179  C CA  . SER E 1 166 ? 14.725  -67.522 -23.841  1.00 57.87  ? 167 SER E CA  1 
ATOM   9180  C C   . SER E 1 166 ? 13.823  -67.574 -25.064  1.00 55.67  ? 167 SER E C   1 
ATOM   9181  O O   . SER E 1 166 ? 13.052  -68.520 -25.246  1.00 68.28  ? 167 SER E O   1 
ATOM   9182  C CB  . SER E 1 166 ? 16.060  -68.220 -24.142  1.00 47.73  ? 167 SER E CB  1 
ATOM   9183  O OG  . SER E 1 166 ? 15.853  -69.541 -24.610  1.00 63.52  ? 167 SER E OG  1 
ATOM   9184  N N   . TYR E 1 167 ? 13.922  -66.544 -25.899  1.00 51.33  ? 168 TYR E N   1 
ATOM   9185  C CA  . TYR E 1 167 ? 13.187  -66.475 -27.154  1.00 53.71  ? 168 TYR E CA  1 
ATOM   9186  C C   . TYR E 1 167 ? 14.168  -66.260 -28.295  1.00 58.47  ? 168 TYR E C   1 
ATOM   9187  O O   . TYR E 1 167 ? 14.982  -65.331 -28.252  1.00 52.43  ? 168 TYR E O   1 
ATOM   9188  C CB  . TYR E 1 167 ? 12.145  -65.352 -27.134  1.00 37.56  ? 168 TYR E CB  1 
ATOM   9189  C CG  . TYR E 1 167 ? 11.509  -65.106 -28.483  1.00 59.74  ? 168 TYR E CG  1 
ATOM   9190  C CD1 . TYR E 1 167 ? 10.436  -65.873 -28.919  1.00 60.52  ? 168 TYR E CD1 1 
ATOM   9191  C CD2 . TYR E 1 167 ? 11.986  -64.109 -29.324  1.00 55.17  ? 168 TYR E CD2 1 
ATOM   9192  C CE1 . TYR E 1 167 ? 9.854   -65.652 -30.154  1.00 55.79  ? 168 TYR E CE1 1 
ATOM   9193  C CE2 . TYR E 1 167 ? 11.414  -63.885 -30.557  1.00 62.72  ? 168 TYR E CE2 1 
ATOM   9194  C CZ  . TYR E 1 167 ? 10.348  -64.655 -30.969  1.00 60.60  ? 168 TYR E CZ  1 
ATOM   9195  O OH  . TYR E 1 167 ? 9.776   -64.428 -32.199  1.00 77.46  ? 168 TYR E OH  1 
ATOM   9196  N N   . ASN E 1 168 ? 14.080  -67.110 -29.312  1.00 60.49  ? 169 ASN E N   1 
ATOM   9197  C CA  . ASN E 1 168 ? 14.930  -67.024 -30.492  1.00 60.92  ? 169 ASN E CA  1 
ATOM   9198  C C   . ASN E 1 168 ? 14.138  -66.381 -31.623  1.00 61.23  ? 169 ASN E C   1 
ATOM   9199  O O   . ASN E 1 168 ? 13.040  -66.840 -31.957  1.00 69.98  ? 169 ASN E O   1 
ATOM   9200  C CB  . ASN E 1 168 ? 15.434  -68.412 -30.896  1.00 57.01  ? 169 ASN E CB  1 
ATOM   9201  C CG  . ASN E 1 168 ? 16.366  -68.381 -32.096  1.00 74.57  ? 169 ASN E CG  1 
ATOM   9202  O OD1 . ASN E 1 168 ? 16.751  -67.317 -32.581  1.00 85.90  ? 169 ASN E OD1 1 
ATOM   9203  N ND2 . ASN E 1 168 ? 16.740  -69.564 -32.577  1.00 86.57  ? 169 ASN E ND2 1 
ATOM   9204  N N   . ASN E 1 169 ? 14.694  -65.318 -32.206  1.00 59.84  ? 170 ASN E N   1 
ATOM   9205  C CA  . ASN E 1 169 ? 14.009  -64.589 -33.265  1.00 54.39  ? 170 ASN E CA  1 
ATOM   9206  C C   . ASN E 1 169 ? 14.015  -65.404 -34.550  1.00 68.71  ? 170 ASN E C   1 
ATOM   9207  O O   . ASN E 1 169 ? 14.919  -65.267 -35.381  1.00 67.39  ? 170 ASN E O   1 
ATOM   9208  C CB  . ASN E 1 169 ? 14.661  -63.220 -33.488  1.00 53.14  ? 170 ASN E CB  1 
ATOM   9209  C CG  . ASN E 1 169 ? 13.929  -62.379 -34.524  1.00 57.55  ? 170 ASN E CG  1 
ATOM   9210  O OD1 . ASN E 1 169 ? 12.839  -62.732 -34.976  1.00 57.34  ? 170 ASN E OD1 1 
ATOM   9211  N ND2 . ASN E 1 169 ? 14.526  -61.253 -34.897  1.00 59.87  ? 170 ASN E ND2 1 
ATOM   9212  N N   . THR E 1 170 ? 13.002  -66.253 -34.720  1.00 74.68  ? 171 THR E N   1 
ATOM   9213  C CA  . THR E 1 170 ? 12.874  -67.089 -35.906  1.00 71.36  ? 171 THR E CA  1 
ATOM   9214  C C   . THR E 1 170 ? 12.278  -66.345 -37.094  1.00 62.82  ? 171 THR E C   1 
ATOM   9215  O O   . THR E 1 170 ? 12.183  -66.925 -38.181  1.00 74.23  ? 171 THR E O   1 
ATOM   9216  C CB  . THR E 1 170 ? 12.026  -68.323 -35.589  1.00 66.48  ? 171 THR E CB  1 
ATOM   9217  O OG1 . THR E 1 170 ? 10.874  -67.931 -34.831  1.00 84.25  ? 171 THR E OG1 1 
ATOM   9218  C CG2 . THR E 1 170 ? 12.834  -69.335 -34.791  1.00 61.84  ? 171 THR E CG2 1 
ATOM   9219  N N   . ASN E 1 171 ? 11.874  -65.090 -36.917  1.00 73.65  ? 172 ASN E N   1 
ATOM   9220  C CA  . ASN E 1 171 ? 11.378  -64.293 -38.026  1.00 61.35  ? 172 ASN E CA  1 
ATOM   9221  C C   . ASN E 1 171 ? 12.538  -63.842 -38.912  1.00 73.79  ? 172 ASN E C   1 
ATOM   9222  O O   . ASN E 1 171 ? 13.715  -64.037 -38.596  1.00 67.30  ? 172 ASN E O   1 
ATOM   9223  C CB  . ASN E 1 171 ? 10.600  -63.083 -37.510  1.00 52.42  ? 172 ASN E CB  1 
ATOM   9224  C CG  . ASN E 1 171 ? 9.525   -63.464 -36.508  1.00 74.97  ? 172 ASN E CG  1 
ATOM   9225  O OD1 . ASN E 1 171 ? 8.385   -63.740 -36.880  1.00 77.82  ? 172 ASN E OD1 1 
ATOM   9226  N ND2 . ASN E 1 171 ? 9.885   -63.482 -35.228  1.00 62.85  ? 172 ASN E ND2 1 
ATOM   9227  N N   . ARG E 1 172 ? 12.193  -63.227 -40.041  1.00 82.00  ? 173 ARG E N   1 
ATOM   9228  C CA  . ARG E 1 172 ? 13.182  -62.723 -40.983  1.00 83.59  ? 173 ARG E CA  1 
ATOM   9229  C C   . ARG E 1 172 ? 13.513  -61.253 -40.769  1.00 67.63  ? 173 ARG E C   1 
ATOM   9230  O O   . ARG E 1 172 ? 14.316  -60.698 -41.524  1.00 76.17  ? 173 ARG E O   1 
ATOM   9231  C CB  . ARG E 1 172 ? 12.699  -62.938 -42.421  1.00 100.60 ? 173 ARG E CB  1 
ATOM   9232  C CG  . ARG E 1 172 ? 12.436  -64.395 -42.771  1.00 105.85 ? 173 ARG E CG  1 
ATOM   9233  C CD  . ARG E 1 172 ? 12.201  -64.594 -44.263  1.00 134.47 ? 173 ARG E CD  1 
ATOM   9234  N NE  . ARG E 1 172 ? 13.335  -64.147 -45.063  1.00 152.35 ? 173 ARG E NE  1 
ATOM   9235  C CZ  . ARG E 1 172 ? 13.312  -63.100 -45.877  1.00 143.29 ? 173 ARG E CZ  1 
ATOM   9236  N NH1 . ARG E 1 172 ? 12.213  -62.384 -46.051  1.00 135.17 ? 173 ARG E NH1 1 
ATOM   9237  N NH2 . ARG E 1 172 ? 14.418  -62.767 -46.537  1.00 131.86 ? 173 ARG E NH2 1 
ATOM   9238  N N   . GLU E 1 173 ? 12.921  -60.612 -39.764  1.00 69.37  ? 174 GLU E N   1 
ATOM   9239  C CA  . GLU E 1 173 ? 13.085  -59.184 -39.537  1.00 62.82  ? 174 GLU E CA  1 
ATOM   9240  C C   . GLU E 1 173 ? 13.511  -58.935 -38.096  1.00 67.86  ? 174 GLU E C   1 
ATOM   9241  O O   . GLU E 1 173 ? 13.418  -59.813 -37.233  1.00 66.62  ? 174 GLU E O   1 
ATOM   9242  C CB  . GLU E 1 173 ? 11.788  -58.420 -39.837  1.00 57.58  ? 174 GLU E CB  1 
ATOM   9243  C CG  . GLU E 1 173 ? 11.066  -58.877 -41.093  1.00 74.77  ? 174 GLU E CG  1 
ATOM   9244  C CD  . GLU E 1 173 ? 9.677   -58.282 -41.211  1.00 86.31  ? 174 GLU E CD  1 
ATOM   9245  O OE1 . GLU E 1 173 ? 9.285   -57.500 -40.319  1.00 87.93  ? 174 GLU E OE1 1 
ATOM   9246  O OE2 . GLU E 1 173 ? 8.975   -58.600 -42.194  1.00 95.82  ? 174 GLU E OE2 1 
ATOM   9247  N N   . ASP E 1 174 ? 13.985  -57.717 -37.844  1.00 60.33  ? 175 ASP E N   1 
ATOM   9248  C CA  . ASP E 1 174 ? 14.324  -57.308 -36.487  1.00 56.38  ? 175 ASP E CA  1 
ATOM   9249  C C   . ASP E 1 174 ? 13.080  -57.280 -35.608  1.00 55.92  ? 175 ASP E C   1 
ATOM   9250  O O   . ASP E 1 174 ? 11.970  -56.995 -36.066  1.00 51.35  ? 175 ASP E O   1 
ATOM   9251  C CB  . ASP E 1 174 ? 14.983  -55.928 -36.490  1.00 55.57  ? 175 ASP E CB  1 
ATOM   9252  C CG  . ASP E 1 174 ? 16.422  -55.966 -36.958  1.00 68.40  ? 175 ASP E CG  1 
ATOM   9253  O OD1 . ASP E 1 174 ? 16.976  -57.075 -37.105  1.00 74.75  ? 175 ASP E OD1 1 
ATOM   9254  O OD2 . ASP E 1 174 ? 16.999  -54.880 -37.177  1.00 66.30  ? 175 ASP E OD2 1 
ATOM   9255  N N   . LEU E 1 175 ? 13.272  -57.584 -34.329  1.00 53.43  ? 176 LEU E N   1 
ATOM   9256  C CA  . LEU E 1 175 ? 12.199  -57.558 -33.345  1.00 49.66  ? 176 LEU E CA  1 
ATOM   9257  C C   . LEU E 1 175 ? 12.477  -56.487 -32.300  1.00 47.09  ? 176 LEU E C   1 
ATOM   9258  O O   . LEU E 1 175 ? 13.562  -56.456 -31.708  1.00 59.11  ? 176 LEU E O   1 
ATOM   9259  C CB  . LEU E 1 175 ? 12.036  -58.922 -32.673  1.00 43.68  ? 176 LEU E CB  1 
ATOM   9260  C CG  . LEU E 1 175 ? 11.005  -59.853 -33.310  1.00 65.10  ? 176 LEU E CG  1 
ATOM   9261  C CD1 . LEU E 1 175 ? 10.899  -61.142 -32.526  1.00 54.18  ? 176 LEU E CD1 1 
ATOM   9262  C CD2 . LEU E 1 175 ? 9.656   -59.163 -33.382  1.00 64.25  ? 176 LEU E CD2 1 
ATOM   9263  N N   . LEU E 1 176 ? 11.499  -55.612 -32.084  1.00 45.71  ? 177 LEU E N   1 
ATOM   9264  C CA  . LEU E 1 176 ? 11.540  -54.644 -30.996  1.00 42.32  ? 177 LEU E CA  1 
ATOM   9265  C C   . LEU E 1 176 ? 10.876  -55.269 -29.777  1.00 47.90  ? 177 LEU E C   1 
ATOM   9266  O O   . LEU E 1 176 ? 9.672   -55.544 -29.795  1.00 55.78  ? 177 LEU E O   1 
ATOM   9267  C CB  . LEU E 1 176 ? 10.833  -53.349 -31.393  1.00 45.91  ? 177 LEU E CB  1 
ATOM   9268  C CG  . LEU E 1 176 ? 10.609  -52.321 -30.280  1.00 47.78  ? 177 LEU E CG  1 
ATOM   9269  C CD1 . LEU E 1 176 ? 11.932  -51.854 -29.689  1.00 44.49  ? 177 LEU E CD1 1 
ATOM   9270  C CD2 . LEU E 1 176 ? 9.806   -51.140 -30.804  1.00 49.75  ? 177 LEU E CD2 1 
ATOM   9271  N N   . ILE E 1 177 ? 11.658  -55.490 -28.723  1.00 49.92  ? 178 ILE E N   1 
ATOM   9272  C CA  . ILE E 1 177 ? 11.212  -56.214 -27.539  1.00 60.05  ? 178 ILE E CA  1 
ATOM   9273  C C   . ILE E 1 177 ? 11.289  -55.281 -26.340  1.00 42.68  ? 178 ILE E C   1 
ATOM   9274  O O   . ILE E 1 177 ? 12.305  -54.607 -26.137  1.00 43.98  ? 178 ILE E O   1 
ATOM   9275  C CB  . ILE E 1 177 ? 12.057  -57.479 -27.300  1.00 45.23  ? 178 ILE E CB  1 
ATOM   9276  C CG1 . ILE E 1 177 ? 11.974  -58.412 -28.510  1.00 45.81  ? 178 ILE E CG1 1 
ATOM   9277  C CG2 . ILE E 1 177 ? 11.608  -58.190 -26.038  1.00 44.10  ? 178 ILE E CG2 1 
ATOM   9278  C CD1 . ILE E 1 177 ? 12.697  -59.725 -28.319  1.00 50.06  ? 178 ILE E CD1 1 
ATOM   9279  N N   . LEU E 1 178 ? 10.219  -55.243 -25.550  1.00 53.82  ? 179 LEU E N   1 
ATOM   9280  C CA  . LEU E 1 178 ? 10.154  -54.410 -24.361  1.00 49.88  ? 179 LEU E CA  1 
ATOM   9281  C C   . LEU E 1 178 ? 9.908   -55.265 -23.124  1.00 51.09  ? 179 LEU E C   1 
ATOM   9282  O O   . LEU E 1 178 ? 9.204   -56.279 -23.174  1.00 53.38  ? 179 LEU E O   1 
ATOM   9283  C CB  . LEU E 1 178 ? 9.056   -53.347 -24.479  1.00 42.36  ? 179 LEU E CB  1 
ATOM   9284  C CG  . LEU E 1 178 ? 9.254   -52.254 -25.533  1.00 46.43  ? 179 LEU E CG  1 
ATOM   9285  C CD1 . LEU E 1 178 ? 8.655   -52.650 -26.878  1.00 50.55  ? 179 LEU E CD1 1 
ATOM   9286  C CD2 . LEU E 1 178 ? 8.682   -50.927 -25.048  1.00 48.30  ? 179 LEU E CD2 1 
ATOM   9287  N N   . TRP E 1 179 ? 10.504  -54.839 -22.013  1.00 49.73  ? 180 TRP E N   1 
ATOM   9288  C CA  . TRP E 1 179 ? 10.328  -55.486 -20.721  1.00 45.07  ? 180 TRP E CA  1 
ATOM   9289  C C   . TRP E 1 179 ? 10.539  -54.436 -19.642  1.00 49.90  ? 180 TRP E C   1 
ATOM   9290  O O   . TRP E 1 179 ? 10.985  -53.318 -19.916  1.00 41.27  ? 180 TRP E O   1 
ATOM   9291  C CB  . TRP E 1 179 ? 11.290  -56.665 -20.542  1.00 43.67  ? 180 TRP E CB  1 
ATOM   9292  C CG  . TRP E 1 179 ? 12.725  -56.251 -20.451  1.00 53.26  ? 180 TRP E CG  1 
ATOM   9293  C CD1 . TRP E 1 179 ? 13.441  -56.020 -19.313  1.00 52.98  ? 180 TRP E CD1 1 
ATOM   9294  C CD2 . TRP E 1 179 ? 13.621  -56.014 -21.544  1.00 56.72  ? 180 TRP E CD2 1 
ATOM   9295  N NE1 . TRP E 1 179 ? 14.727  -55.655 -19.628  1.00 51.57  ? 180 TRP E NE1 1 
ATOM   9296  C CE2 . TRP E 1 179 ? 14.863  -55.644 -20.991  1.00 47.94  ? 180 TRP E CE2 1 
ATOM   9297  C CE3 . TRP E 1 179 ? 13.494  -56.078 -22.934  1.00 56.60  ? 180 TRP E CE3 1 
ATOM   9298  C CZ2 . TRP E 1 179 ? 15.970  -55.341 -21.780  1.00 48.64  ? 180 TRP E CZ2 1 
ATOM   9299  C CZ3 . TRP E 1 179 ? 14.595  -55.777 -23.716  1.00 54.71  ? 180 TRP E CZ3 1 
ATOM   9300  C CH2 . TRP E 1 179 ? 15.816  -55.413 -23.137  1.00 56.26  ? 180 TRP E CH2 1 
ATOM   9301  N N   . GLY E 1 180 ? 10.216  -54.801 -18.401  1.00 44.97  ? 181 GLY E N   1 
ATOM   9302  C CA  . GLY E 1 180 ? 10.289  -53.841 -17.319  1.00 43.83  ? 181 GLY E CA  1 
ATOM   9303  C C   . GLY E 1 180 ? 10.592  -54.478 -15.980  1.00 50.92  ? 181 GLY E C   1 
ATOM   9304  O O   . GLY E 1 180 ? 10.555  -55.701 -15.816  1.00 51.74  ? 181 GLY E O   1 
ATOM   9305  N N   . ILE E 1 181 ? 10.896  -53.612 -15.015  1.00 47.74  ? 182 ILE E N   1 
ATOM   9306  C CA  . ILE E 1 181 ? 11.157  -53.996 -13.633  1.00 51.42  ? 182 ILE E CA  1 
ATOM   9307  C C   . ILE E 1 181 ? 10.256  -53.161 -12.734  1.00 49.32  ? 182 ILE E C   1 
ATOM   9308  O O   . ILE E 1 181 ? 10.032  -51.974 -12.997  1.00 48.85  ? 182 ILE E O   1 
ATOM   9309  C CB  . ILE E 1 181 ? 12.644  -53.806 -13.256  1.00 49.12  ? 182 ILE E CB  1 
ATOM   9310  C CG1 . ILE E 1 181 ? 12.886  -54.189 -11.793  1.00 52.42  ? 182 ILE E CG1 1 
ATOM   9311  C CG2 . ILE E 1 181 ? 13.095  -52.375 -13.528  1.00 51.76  ? 182 ILE E CG2 1 
ATOM   9312  C CD1 . ILE E 1 181 ? 14.328  -54.057 -11.347  1.00 52.53  ? 182 ILE E CD1 1 
ATOM   9313  N N   . HIS E 1 182 ? 9.722   -53.781 -11.685  1.00 44.40  ? 183 HIS E N   1 
ATOM   9314  C CA  . HIS E 1 182 ? 8.844   -53.098 -10.744  1.00 47.68  ? 183 HIS E CA  1 
ATOM   9315  C C   . HIS E 1 182 ? 9.612   -52.778 -9.468   1.00 46.37  ? 183 HIS E C   1 
ATOM   9316  O O   . HIS E 1 182 ? 10.092  -53.687 -8.781   1.00 47.58  ? 183 HIS E O   1 
ATOM   9317  C CB  . HIS E 1 182 ? 7.612   -53.946 -10.424  1.00 48.79  ? 183 HIS E CB  1 
ATOM   9318  C CG  . HIS E 1 182 ? 6.736   -53.355 -9.363   1.00 50.99  ? 183 HIS E CG  1 
ATOM   9319  N ND1 . HIS E 1 182 ? 6.295   -54.075 -8.274   1.00 47.32  ? 183 HIS E ND1 1 
ATOM   9320  C CD2 . HIS E 1 182 ? 6.230   -52.108 -9.219   1.00 46.01  ? 183 HIS E CD2 1 
ATOM   9321  C CE1 . HIS E 1 182 ? 5.549   -53.299 -7.508   1.00 48.09  ? 183 HIS E CE1 1 
ATOM   9322  N NE2 . HIS E 1 182 ? 5.493   -52.100 -8.060   1.00 53.68  ? 183 HIS E NE2 1 
ATOM   9323  N N   . HIS E 1 183 ? 9.729   -51.489 -9.156   1.00 51.60  ? 184 HIS E N   1 
ATOM   9324  C CA  . HIS E 1 183 ? 10.282  -51.054 -7.879   1.00 51.79  ? 184 HIS E CA  1 
ATOM   9325  C C   . HIS E 1 183 ? 9.154   -51.033 -6.857   1.00 55.30  ? 184 HIS E C   1 
ATOM   9326  O O   . HIS E 1 183 ? 8.228   -50.222 -6.959   1.00 54.60  ? 184 HIS E O   1 
ATOM   9327  C CB  . HIS E 1 183 ? 10.929  -49.678 -8.007   1.00 46.30  ? 184 HIS E CB  1 
ATOM   9328  C CG  . HIS E 1 183 ? 12.029  -49.612 -9.022   1.00 59.42  ? 184 HIS E CG  1 
ATOM   9329  N ND1 . HIS E 1 183 ? 13.109  -50.467 -9.007   1.00 65.69  ? 184 HIS E ND1 1 
ATOM   9330  C CD2 . HIS E 1 183 ? 12.220  -48.782 -10.075  1.00 66.38  ? 184 HIS E CD2 1 
ATOM   9331  C CE1 . HIS E 1 183 ? 13.916  -50.172 -10.011  1.00 55.31  ? 184 HIS E CE1 1 
ATOM   9332  N NE2 . HIS E 1 183 ? 13.399  -49.153 -10.675  1.00 62.49  ? 184 HIS E NE2 1 
ATOM   9333  N N   . SER E 1 184 ? 9.220   -51.930 -5.878   1.00 47.28  ? 185 SER E N   1 
ATOM   9334  C CA  . SER E 1 184 ? 8.190   -51.991 -4.853   1.00 54.29  ? 185 SER E CA  1 
ATOM   9335  C C   . SER E 1 184 ? 8.445   -50.938 -3.774   1.00 48.52  ? 185 SER E C   1 
ATOM   9336  O O   . SER E 1 184 ? 9.498   -50.294 -3.729   1.00 59.74  ? 185 SER E O   1 
ATOM   9337  C CB  . SER E 1 184 ? 8.127   -53.392 -4.248   1.00 51.56  ? 185 SER E CB  1 
ATOM   9338  O OG  . SER E 1 184 ? 9.428   -53.904 -4.018   1.00 58.68  ? 185 SER E OG  1 
ATOM   9339  N N   . ASN E 1 185 ? 7.454   -50.766 -2.898   1.00 53.81  ? 186 ASN E N   1 
ATOM   9340  C CA  . ASN E 1 185 ? 7.487   -49.723 -1.878   1.00 66.02  ? 186 ASN E CA  1 
ATOM   9341  C C   . ASN E 1 185 ? 8.266   -50.131 -0.631   1.00 49.07  ? 186 ASN E C   1 
ATOM   9342  O O   . ASN E 1 185 ? 9.111   -49.370 -0.154   1.00 63.13  ? 186 ASN E O   1 
ATOM   9343  C CB  . ASN E 1 185 ? 6.059   -49.335 -1.485   1.00 76.03  ? 186 ASN E CB  1 
ATOM   9344  C CG  . ASN E 1 185 ? 5.247   -48.831 -2.660   1.00 74.84  ? 186 ASN E CG  1 
ATOM   9345  O OD1 . ASN E 1 185 ? 5.801   -48.313 -3.627   1.00 88.46  ? 186 ASN E OD1 1 
ATOM   9346  N ND2 . ASN E 1 185 ? 3.930   -48.978 -2.582   1.00 87.61  ? 186 ASN E ND2 1 
ATOM   9347  N N   . ASN E 1 186 ? 8.008   -51.324 -0.099   1.00 56.12  ? 187 ASN E N   1 
ATOM   9348  C CA  . ASN E 1 186 ? 8.627   -51.752 1.152    1.00 61.92  ? 187 ASN E CA  1 
ATOM   9349  C C   . ASN E 1 186 ? 8.807   -53.264 1.135    1.00 51.26  ? 187 ASN E C   1 
ATOM   9350  O O   . ASN E 1 186 ? 8.458   -53.942 0.166    1.00 59.05  ? 187 ASN E O   1 
ATOM   9351  C CB  . ASN E 1 186 ? 7.796   -51.307 2.361    1.00 64.41  ? 187 ASN E CB  1 
ATOM   9352  C CG  . ASN E 1 186 ? 6.327   -51.636 2.205    1.00 48.71  ? 187 ASN E CG  1 
ATOM   9353  O OD1 . ASN E 1 186 ? 5.946   -52.800 2.085    1.00 64.67  ? 187 ASN E OD1 1 
ATOM   9354  N ND2 . ASN E 1 186 ? 5.488   -50.605 2.203    1.00 49.74  ? 187 ASN E ND2 1 
ATOM   9355  N N   . ALA E 1 187 ? 9.360   -53.789 2.231    1.00 62.72  ? 188 ALA E N   1 
ATOM   9356  C CA  . ALA E 1 187 ? 9.616   -55.223 2.321    1.00 51.18  ? 188 ALA E CA  1 
ATOM   9357  C C   . ALA E 1 187 ? 8.320   -56.026 2.321    1.00 55.35  ? 188 ALA E C   1 
ATOM   9358  O O   . ALA E 1 187 ? 8.238   -57.085 1.687    1.00 61.79  ? 188 ALA E O   1 
ATOM   9359  C CB  . ALA E 1 187 ? 10.439  -55.539 3.570    1.00 64.01  ? 188 ALA E CB  1 
ATOM   9360  N N   . GLU E 1 188 ? 7.302   -55.551 3.042    1.00 55.18  ? 189 GLU E N   1 
ATOM   9361  C CA  . GLU E 1 188 ? 6.041   -56.285 3.103    1.00 51.57  ? 189 GLU E CA  1 
ATOM   9362  C C   . GLU E 1 188 ? 5.376   -56.358 1.733    1.00 62.32  ? 189 GLU E C   1 
ATOM   9363  O O   . GLU E 1 188 ? 4.868   -57.414 1.338    1.00 66.24  ? 189 GLU E O   1 
ATOM   9364  C CB  . GLU E 1 188 ? 5.098   -55.641 4.118    1.00 55.91  ? 189 GLU E CB  1 
ATOM   9365  C CG  . GLU E 1 188 ? 3.850   -56.470 4.367    1.00 85.80  ? 189 GLU E CG  1 
ATOM   9366  C CD  . GLU E 1 188 ? 2.735   -55.690 5.033    1.00 109.41 ? 189 GLU E CD  1 
ATOM   9367  O OE1 . GLU E 1 188 ? 3.002   -54.581 5.543    1.00 113.09 ? 189 GLU E OE1 1 
ATOM   9368  O OE2 . GLU E 1 188 ? 1.590   -56.188 5.047    1.00 112.43 ? 189 GLU E OE2 1 
ATOM   9369  N N   . GLU E 1 189 ? 5.364   -55.245 0.995    1.00 55.31  ? 190 GLU E N   1 
ATOM   9370  C CA  . GLU E 1 189 ? 4.804   -55.270 -0.352   1.00 50.71  ? 190 GLU E CA  1 
ATOM   9371  C C   . GLU E 1 189 ? 5.633   -56.156 -1.271   1.00 60.40  ? 190 GLU E C   1 
ATOM   9372  O O   . GLU E 1 189 ? 5.087   -56.853 -2.135   1.00 60.26  ? 190 GLU E O   1 
ATOM   9373  C CB  . GLU E 1 189 ? 4.710   -53.852 -0.915   1.00 60.55  ? 190 GLU E CB  1 
ATOM   9374  C CG  . GLU E 1 189 ? 3.617   -53.690 -1.963   1.00 84.68  ? 190 GLU E CG  1 
ATOM   9375  C CD  . GLU E 1 189 ? 3.993   -52.724 -3.071   1.00 103.01 ? 190 GLU E CD  1 
ATOM   9376  O OE1 . GLU E 1 189 ? 5.100   -52.147 -3.010   1.00 97.24  ? 190 GLU E OE1 1 
ATOM   9377  O OE2 . GLU E 1 189 ? 3.182   -52.548 -4.006   1.00 99.84  ? 190 GLU E OE2 1 
ATOM   9378  N N   . GLN E 1 190 ? 6.959   -56.134 -1.104   1.00 55.42  ? 191 GLN E N   1 
ATOM   9379  C CA  . GLN E 1 190 ? 7.830   -56.995 -1.900   1.00 45.45  ? 191 GLN E CA  1 
ATOM   9380  C C   . GLN E 1 190 ? 7.522   -58.467 -1.655   1.00 44.82  ? 191 GLN E C   1 
ATOM   9381  O O   . GLN E 1 190 ? 7.494   -59.269 -2.596   1.00 52.53  ? 191 GLN E O   1 
ATOM   9382  C CB  . GLN E 1 190 ? 9.295   -56.689 -1.582   1.00 45.16  ? 191 GLN E CB  1 
ATOM   9383  C CG  . GLN E 1 190 ? 10.292  -57.648 -2.213   1.00 36.94  ? 191 GLN E CG  1 
ATOM   9384  C CD  . GLN E 1 190 ? 10.411  -57.468 -3.714   1.00 46.88  ? 191 GLN E CD  1 
ATOM   9385  O OE1 . GLN E 1 190 ? 10.012  -56.440 -4.261   1.00 49.08  ? 191 GLN E OE1 1 
ATOM   9386  N NE2 . GLN E 1 190 ? 10.961  -58.472 -4.388   1.00 42.19  ? 191 GLN E NE2 1 
ATOM   9387  N N   . THR E 1 191 ? 7.284   -58.841 -0.395   1.00 58.57  ? 192 THR E N   1 
ATOM   9388  C CA  . THR E 1 191 ? 6.952   -60.226 -0.078   1.00 56.11  ? 192 THR E CA  1 
ATOM   9389  C C   . THR E 1 191 ? 5.544   -60.591 -0.540   1.00 61.44  ? 192 THR E C   1 
ATOM   9390  O O   . THR E 1 191 ? 5.311   -61.728 -0.967   1.00 59.08  ? 192 THR E O   1 
ATOM   9391  C CB  . THR E 1 191 ? 7.099   -60.471 1.427    1.00 44.07  ? 192 THR E CB  1 
ATOM   9392  O OG1 . THR E 1 191 ? 8.406   -60.072 1.855    1.00 70.76  ? 192 THR E OG1 1 
ATOM   9393  C CG2 . THR E 1 191 ? 6.898   -61.943 1.753    1.00 61.58  ? 192 THR E CG2 1 
ATOM   9394  N N   . ASN E 1 192 ? 4.598   -59.648 -0.472   1.00 57.98  ? 193 ASN E N   1 
ATOM   9395  C CA  . ASN E 1 192 ? 3.228   -59.943 -0.885   1.00 54.00  ? 193 ASN E CA  1 
ATOM   9396  C C   . ASN E 1 192 ? 3.156   -60.280 -2.366   1.00 55.83  ? 193 ASN E C   1 
ATOM   9397  O O   . ASN E 1 192 ? 2.379   -61.149 -2.773   1.00 60.82  ? 193 ASN E O   1 
ATOM   9398  C CB  . ASN E 1 192 ? 2.310   -58.761 -0.570   1.00 72.35  ? 193 ASN E CB  1 
ATOM   9399  C CG  . ASN E 1 192 ? 1.472   -58.986 0.676    1.00 92.85  ? 193 ASN E CG  1 
ATOM   9400  O OD1 . ASN E 1 192 ? 1.971   -59.458 1.696    1.00 88.99  ? 193 ASN E OD1 1 
ATOM   9401  N ND2 . ASN E 1 192 ? 0.187   -58.650 0.596    1.00 91.99  ? 193 ASN E ND2 1 
ATOM   9402  N N   . LEU E 1 193 ? 3.938   -59.586 -3.190   1.00 60.20  ? 194 LEU E N   1 
ATOM   9403  C CA  . LEU E 1 193 ? 3.877   -59.781 -4.632   1.00 52.41  ? 194 LEU E CA  1 
ATOM   9404  C C   . LEU E 1 193 ? 4.808   -60.884 -5.119   1.00 55.50  ? 194 LEU E C   1 
ATOM   9405  O O   . LEU E 1 193 ? 4.422   -61.680 -5.981   1.00 50.38  ? 194 LEU E O   1 
ATOM   9406  C CB  . LEU E 1 193 ? 4.209   -58.472 -5.353   1.00 50.60  ? 194 LEU E CB  1 
ATOM   9407  C CG  . LEU E 1 193 ? 3.206   -57.332 -5.178   1.00 55.40  ? 194 LEU E CG  1 
ATOM   9408  C CD1 . LEU E 1 193 ? 3.783   -56.029 -5.708   1.00 50.55  ? 194 LEU E CD1 1 
ATOM   9409  C CD2 . LEU E 1 193 ? 1.899   -57.663 -5.879   1.00 39.28  ? 194 LEU E CD2 1 
ATOM   9410  N N   . TYR E 1 194 ? 6.027   -60.959 -4.579   1.00 55.63  ? 195 TYR E N   1 
ATOM   9411  C CA  . TYR E 1 194 ? 7.046   -61.832 -5.141   1.00 49.54  ? 195 TYR E CA  1 
ATOM   9412  C C   . TYR E 1 194 ? 7.687   -62.796 -4.151   1.00 53.05  ? 195 TYR E C   1 
ATOM   9413  O O   . TYR E 1 194 ? 8.451   -63.663 -4.587   1.00 54.22  ? 195 TYR E O   1 
ATOM   9414  C CB  . TYR E 1 194 ? 8.154   -60.995 -5.801   1.00 48.73  ? 195 TYR E CB  1 
ATOM   9415  C CG  . TYR E 1 194 ? 7.627   -59.819 -6.596   1.00 54.46  ? 195 TYR E CG  1 
ATOM   9416  C CD1 . TYR E 1 194 ? 6.893   -60.013 -7.760   1.00 48.14  ? 195 TYR E CD1 1 
ATOM   9417  C CD2 . TYR E 1 194 ? 7.864   -58.513 -6.181   1.00 45.61  ? 195 TYR E CD2 1 
ATOM   9418  C CE1 . TYR E 1 194 ? 6.408   -58.940 -8.488   1.00 41.94  ? 195 TYR E CE1 1 
ATOM   9419  C CE2 . TYR E 1 194 ? 7.384   -57.434 -6.903   1.00 43.64  ? 195 TYR E CE2 1 
ATOM   9420  C CZ  . TYR E 1 194 ? 6.657   -57.654 -8.054   1.00 50.52  ? 195 TYR E CZ  1 
ATOM   9421  O OH  . TYR E 1 194 ? 6.178   -56.585 -8.776   1.00 44.65  ? 195 TYR E OH  1 
ATOM   9422  N N   . LYS E 1 195 ? 7.466   -62.635 -2.844   1.00 56.01  ? 196 LYS E N   1 
ATOM   9423  C CA  . LYS E 1 195 ? 7.852   -63.621 -1.835   1.00 62.61  ? 196 LYS E CA  1 
ATOM   9424  C C   . LYS E 1 195 ? 9.368   -63.683 -1.649   1.00 50.95  ? 196 LYS E C   1 
ATOM   9425  O O   . LYS E 1 195 ? 9.859   -64.253 -0.669   1.00 81.10  ? 196 LYS E O   1 
ATOM   9426  C CB  . LYS E 1 195 ? 7.277   -64.998 -2.211   1.00 66.55  ? 196 LYS E CB  1 
ATOM   9427  C CG  . LYS E 1 195 ? 7.768   -66.198 -1.402   1.00 50.86  ? 196 LYS E CG  1 
ATOM   9428  C CD  . LYS E 1 195 ? 7.379   -66.097 0.062    1.00 64.33  ? 196 LYS E CD  1 
ATOM   9429  C CE  . LYS E 1 195 ? 7.967   -67.246 0.862    1.00 54.00  ? 196 LYS E CE  1 
ATOM   9430  N NZ  . LYS E 1 195 ? 7.569   -67.188 2.294    1.00 95.11  ? 196 LYS E NZ  1 
ATOM   9431  N N   . ASN E 1 196 ? 10.121  -63.030 -2.532   1.00 58.78  ? 197 ASN E N   1 
ATOM   9432  C CA  . ASN E 1 196 ? 11.574  -63.071 -2.474   1.00 44.61  ? 197 ASN E CA  1 
ATOM   9433  C C   . ASN E 1 196 ? 12.102  -61.706 -2.068   1.00 49.55  ? 197 ASN E C   1 
ATOM   9434  O O   . ASN E 1 196 ? 11.904  -60.728 -2.805   1.00 60.49  ? 197 ASN E O   1 
ATOM   9435  C CB  . ASN E 1 196 ? 12.159  -63.496 -3.820   1.00 62.14  ? 197 ASN E CB  1 
ATOM   9436  C CG  . ASN E 1 196 ? 11.813  -64.932 -4.180   1.00 58.61  ? 197 ASN E CG  1 
ATOM   9437  O OD1 . ASN E 1 196 ? 11.708  -65.794 -3.308   1.00 50.03  ? 197 ASN E OD1 1 
ATOM   9438  N ND2 . ASN E 1 196 ? 11.636  -65.194 -5.472   1.00 53.67  ? 197 ASN E ND2 1 
ATOM   9439  N N   . PRO E 1 197 ? 12.759  -61.586 -0.911   1.00 49.28  ? 198 PRO E N   1 
ATOM   9440  C CA  . PRO E 1 197 ? 13.223  -60.257 -0.480   1.00 50.52  ? 198 PRO E CA  1 
ATOM   9441  C C   . PRO E 1 197 ? 14.274  -59.654 -1.394   1.00 57.32  ? 198 PRO E C   1 
ATOM   9442  O O   . PRO E 1 197 ? 14.260  -58.438 -1.625   1.00 46.97  ? 198 PRO E O   1 
ATOM   9443  C CB  . PRO E 1 197 ? 13.772  -60.523 0.928    1.00 44.97  ? 198 PRO E CB  1 
ATOM   9444  C CG  . PRO E 1 197 ? 14.149  -61.970 0.914    1.00 45.57  ? 198 PRO E CG  1 
ATOM   9445  C CD  . PRO E 1 197 ? 13.140  -62.647 0.037    1.00 52.10  ? 198 PRO E CD  1 
ATOM   9446  N N   . THR E 1 198 ? 15.185  -60.467 -1.925   1.00 46.87  ? 199 THR E N   1 
ATOM   9447  C CA  . THR E 1 198 ? 16.285  -59.992 -2.761   1.00 55.71  ? 199 THR E CA  1 
ATOM   9448  C C   . THR E 1 198 ? 16.103  -60.558 -4.163   1.00 61.41  ? 199 THR E C   1 
ATOM   9449  O O   . THR E 1 198 ? 16.241  -61.769 -4.372   1.00 63.67  ? 199 THR E O   1 
ATOM   9450  C CB  . THR E 1 198 ? 17.634  -60.401 -2.172   1.00 43.86  ? 199 THR E CB  1 
ATOM   9451  O OG1 . THR E 1 198 ? 17.714  -59.961 -0.810   1.00 66.44  ? 199 THR E OG1 1 
ATOM   9452  C CG2 . THR E 1 198 ? 18.772  -59.778 -2.964   1.00 53.56  ? 199 THR E CG2 1 
ATOM   9453  N N   . THR E 1 199 ? 15.806  -59.685 -5.124   1.00 54.60  ? 200 THR E N   1 
ATOM   9454  C CA  . THR E 1 199 ? 15.458  -60.102 -6.472   1.00 52.23  ? 200 THR E CA  1 
ATOM   9455  C C   . THR E 1 199 ? 16.356  -59.414 -7.492   1.00 51.11  ? 200 THR E C   1 
ATOM   9456  O O   . THR E 1 199 ? 17.017  -58.413 -7.202   1.00 44.14  ? 200 THR E O   1 
ATOM   9457  C CB  . THR E 1 199 ? 13.987  -59.803 -6.793   1.00 54.52  ? 200 THR E CB  1 
ATOM   9458  O OG1 . THR E 1 199 ? 13.716  -58.418 -6.551   1.00 48.92  ? 200 THR E OG1 1 
ATOM   9459  C CG2 . THR E 1 199 ? 13.072  -60.650 -5.926   1.00 45.17  ? 200 THR E CG2 1 
ATOM   9460  N N   . TYR E 1 200 ? 16.364  -59.974 -8.701   1.00 58.32  ? 201 TYR E N   1 
ATOM   9461  C CA  . TYR E 1 200 ? 17.188  -59.477 -9.792   1.00 52.40  ? 201 TYR E CA  1 
ATOM   9462  C C   . TYR E 1 200 ? 16.503  -59.799 -11.111  1.00 55.32  ? 201 TYR E C   1 
ATOM   9463  O O   . TYR E 1 200 ? 15.650  -60.687 -11.189  1.00 49.07  ? 201 TYR E O   1 
ATOM   9464  C CB  . TYR E 1 200 ? 18.590  -60.099 -9.770   1.00 48.87  ? 201 TYR E CB  1 
ATOM   9465  C CG  . TYR E 1 200 ? 18.586  -61.573 -10.114  1.00 55.15  ? 201 TYR E CG  1 
ATOM   9466  C CD1 . TYR E 1 200 ? 18.285  -62.528 -9.151   1.00 47.21  ? 201 TYR E CD1 1 
ATOM   9467  C CD2 . TYR E 1 200 ? 18.874  -62.009 -11.403  1.00 55.53  ? 201 TYR E CD2 1 
ATOM   9468  C CE1 . TYR E 1 200 ? 18.271  -63.874 -9.458   1.00 50.34  ? 201 TYR E CE1 1 
ATOM   9469  C CE2 . TYR E 1 200 ? 18.863  -63.354 -11.721  1.00 59.83  ? 201 TYR E CE2 1 
ATOM   9470  C CZ  . TYR E 1 200 ? 18.561  -64.282 -10.743  1.00 56.75  ? 201 TYR E CZ  1 
ATOM   9471  O OH  . TYR E 1 200 ? 18.549  -65.623 -11.048  1.00 67.24  ? 201 TYR E OH  1 
ATOM   9472  N N   . ILE E 1 201 ? 16.886  -59.064 -12.153  1.00 55.14  ? 202 ILE E N   1 
ATOM   9473  C CA  . ILE E 1 201 ? 16.479  -59.358 -13.523  1.00 47.82  ? 202 ILE E CA  1 
ATOM   9474  C C   . ILE E 1 201 ? 17.714  -59.258 -14.404  1.00 54.93  ? 202 ILE E C   1 
ATOM   9475  O O   . ILE E 1 201 ? 18.366  -58.207 -14.444  1.00 55.69  ? 202 ILE E O   1 
ATOM   9476  C CB  . ILE E 1 201 ? 15.385  -58.402 -14.028  1.00 52.21  ? 202 ILE E CB  1 
ATOM   9477  C CG1 . ILE E 1 201 ? 14.151  -58.467 -13.130  1.00 53.64  ? 202 ILE E CG1 1 
ATOM   9478  C CG2 . ILE E 1 201 ? 15.014  -58.739 -15.466  1.00 36.72  ? 202 ILE E CG2 1 
ATOM   9479  C CD1 . ILE E 1 201 ? 13.087  -57.466 -13.508  1.00 52.87  ? 202 ILE E CD1 1 
ATOM   9480  N N   . SER E 1 202 ? 18.031  -60.337 -15.114  1.00 47.12  ? 203 SER E N   1 
ATOM   9481  C CA  . SER E 1 202 ? 19.168  -60.370 -16.026  1.00 52.81  ? 203 SER E CA  1 
ATOM   9482  C C   . SER E 1 202 ? 18.672  -60.662 -17.434  1.00 56.01  ? 203 SER E C   1 
ATOM   9483  O O   . SER E 1 202 ? 17.950  -61.641 -17.652  1.00 53.73  ? 203 SER E O   1 
ATOM   9484  C CB  . SER E 1 202 ? 20.198  -61.415 -15.590  1.00 54.60  ? 203 SER E CB  1 
ATOM   9485  O OG  . SER E 1 202 ? 19.602  -62.690 -15.438  1.00 66.69  ? 203 SER E OG  1 
ATOM   9486  N N   . VAL E 1 203 ? 19.059  -59.813 -18.383  1.00 52.18  ? 204 VAL E N   1 
ATOM   9487  C CA  . VAL E 1 203 ? 18.664  -59.942 -19.780  1.00 48.23  ? 204 VAL E CA  1 
ATOM   9488  C C   . VAL E 1 203 ? 19.926  -60.079 -20.616  1.00 52.90  ? 204 VAL E C   1 
ATOM   9489  O O   . VAL E 1 203 ? 20.854  -59.273 -20.485  1.00 47.87  ? 204 VAL E O   1 
ATOM   9490  C CB  . VAL E 1 203 ? 17.824  -58.742 -20.252  1.00 49.39  ? 204 VAL E CB  1 
ATOM   9491  C CG1 . VAL E 1 203 ? 17.193  -59.043 -21.602  1.00 50.39  ? 204 VAL E CG1 1 
ATOM   9492  C CG2 . VAL E 1 203 ? 16.763  -58.400 -19.221  1.00 49.91  ? 204 VAL E CG2 1 
ATOM   9493  N N   . GLY E 1 204 ? 19.962  -61.098 -21.470  1.00 59.95  ? 205 GLY E N   1 
ATOM   9494  C CA  . GLY E 1 204 ? 21.141  -61.338 -22.275  1.00 47.45  ? 205 GLY E CA  1 
ATOM   9495  C C   . GLY E 1 204 ? 20.868  -61.684 -23.722  1.00 62.57  ? 205 GLY E C   1 
ATOM   9496  O O   . GLY E 1 204 ? 20.101  -62.607 -24.017  1.00 67.63  ? 205 GLY E O   1 
ATOM   9497  N N   . THR E 1 205 ? 21.482  -60.935 -24.635  1.00 58.50  ? 206 THR E N   1 
ATOM   9498  C CA  . THR E 1 205 ? 21.501  -61.282 -26.051  1.00 60.41  ? 206 THR E CA  1 
ATOM   9499  C C   . THR E 1 205 ? 22.948  -61.316 -26.516  1.00 57.98  ? 206 THR E C   1 
ATOM   9500  O O   . THR E 1 205 ? 23.864  -61.327 -25.690  1.00 64.15  ? 206 THR E O   1 
ATOM   9501  C CB  . THR E 1 205 ? 20.702  -60.280 -26.889  1.00 60.49  ? 206 THR E CB  1 
ATOM   9502  O OG1 . THR E 1 205 ? 21.409  -59.040 -26.955  1.00 68.11  ? 206 THR E OG1 1 
ATOM   9503  C CG2 . THR E 1 205 ? 19.329  -60.043 -26.281  1.00 57.65  ? 206 THR E CG2 1 
ATOM   9504  N N   . SER E 1 206 ? 23.167  -61.351 -27.832  1.00 62.59  ? 207 SER E N   1 
ATOM   9505  C CA  . SER E 1 206 ? 24.533  -61.314 -28.343  1.00 62.57  ? 207 SER E CA  1 
ATOM   9506  C C   . SER E 1 206 ? 25.246  -60.028 -27.949  1.00 52.45  ? 207 SER E C   1 
ATOM   9507  O O   . SER E 1 206 ? 26.467  -60.031 -27.760  1.00 68.38  ? 207 SER E O   1 
ATOM   9508  C CB  . SER E 1 206 ? 24.531  -61.473 -29.862  1.00 52.68  ? 207 SER E CB  1 
ATOM   9509  O OG  . SER E 1 206 ? 23.897  -60.373 -30.490  1.00 65.65  ? 207 SER E OG  1 
ATOM   9510  N N   . THR E 1 207 ? 24.508  -58.926 -27.815  1.00 61.32  ? 208 THR E N   1 
ATOM   9511  C CA  . THR E 1 207 ? 25.095  -57.626 -27.526  1.00 55.54  ? 208 THR E CA  1 
ATOM   9512  C C   . THR E 1 207 ? 24.542  -56.969 -26.267  1.00 63.64  ? 208 THR E C   1 
ATOM   9513  O O   . THR E 1 207 ? 24.966  -55.857 -25.934  1.00 70.97  ? 208 THR E O   1 
ATOM   9514  C CB  . THR E 1 207 ? 24.892  -56.679 -28.717  1.00 81.73  ? 208 THR E CB  1 
ATOM   9515  O OG1 . THR E 1 207 ? 23.530  -56.748 -29.158  1.00 78.82  ? 208 THR E OG1 1 
ATOM   9516  C CG2 . THR E 1 207 ? 25.815  -57.059 -29.865  1.00 84.92  ? 208 THR E CG2 1 
ATOM   9517  N N   . LEU E 1 208 ? 23.617  -57.612 -25.562  1.00 68.79  ? 209 LEU E N   1 
ATOM   9518  C CA  . LEU E 1 208 ? 23.000  -57.041 -24.372  1.00 58.56  ? 209 LEU E CA  1 
ATOM   9519  C C   . LEU E 1 208 ? 23.421  -57.836 -23.144  1.00 61.29  ? 209 LEU E C   1 
ATOM   9520  O O   . LEU E 1 208 ? 23.277  -59.063 -23.115  1.00 65.03  ? 209 LEU E O   1 
ATOM   9521  C CB  . LEU E 1 208 ? 21.475  -57.029 -24.500  1.00 60.04  ? 209 LEU E CB  1 
ATOM   9522  C CG  . LEU E 1 208 ? 20.669  -56.407 -23.357  1.00 56.76  ? 209 LEU E CG  1 
ATOM   9523  C CD1 . LEU E 1 208 ? 20.905  -54.905 -23.264  1.00 35.80  ? 209 LEU E CD1 1 
ATOM   9524  C CD2 . LEU E 1 208 ? 19.192  -56.710 -23.533  1.00 58.97  ? 209 LEU E CD2 1 
ATOM   9525  N N   . ASN E 1 209 ? 23.946  -57.137 -22.135  1.00 50.00  ? 210 ASN E N   1 
ATOM   9526  C CA  . ASN E 1 209 ? 24.380  -57.739 -20.871  1.00 41.34  ? 210 ASN E CA  1 
ATOM   9527  C C   . ASN E 1 209 ? 23.843  -56.854 -19.749  1.00 58.43  ? 210 ASN E C   1 
ATOM   9528  O O   . ASN E 1 209 ? 24.531  -55.944 -19.278  1.00 66.06  ? 210 ASN E O   1 
ATOM   9529  C CB  . ASN E 1 209 ? 25.901  -57.871 -20.821  1.00 42.92  ? 210 ASN E CB  1 
ATOM   9530  C CG  . ASN E 1 209 ? 26.380  -58.686 -19.637  1.00 63.76  ? 210 ASN E CG  1 
ATOM   9531  O OD1 . ASN E 1 209 ? 25.669  -59.553 -19.133  1.00 61.54  ? 210 ASN E OD1 1 
ATOM   9532  N ND2 . ASN E 1 209 ? 27.601  -58.411 -19.189  1.00 58.30  ? 210 ASN E ND2 1 
ATOM   9533  N N   . GLN E 1 210 ? 22.616  -57.133 -19.315  1.00 59.64  ? 211 GLN E N   1 
ATOM   9534  C CA  . GLN E 1 210 ? 21.896  -56.284 -18.377  1.00 51.82  ? 211 GLN E CA  1 
ATOM   9535  C C   . GLN E 1 210 ? 21.604  -57.036 -17.086  1.00 56.89  ? 211 GLN E C   1 
ATOM   9536  O O   . GLN E 1 210 ? 21.280  -58.227 -17.108  1.00 49.32  ? 211 GLN E O   1 
ATOM   9537  C CB  . GLN E 1 210 ? 20.583  -55.782 -18.991  1.00 50.39  ? 211 GLN E CB  1 
ATOM   9538  C CG  . GLN E 1 210 ? 19.835  -54.774 -18.133  1.00 54.49  ? 211 GLN E CG  1 
ATOM   9539  C CD  . GLN E 1 210 ? 18.489  -54.393 -18.718  1.00 62.84  ? 211 GLN E CD  1 
ATOM   9540  O OE1 . GLN E 1 210 ? 17.595  -55.230 -18.843  1.00 55.22  ? 211 GLN E OE1 1 
ATOM   9541  N NE2 . GLN E 1 210 ? 18.339  -53.125 -19.084  1.00 59.56  ? 211 GLN E NE2 1 
ATOM   9542  N N   . ARG E 1 211 ? 21.725  -56.329 -15.963  1.00 52.42  ? 212 ARG E N   1 
ATOM   9543  C CA  . ARG E 1 211 ? 21.356  -56.850 -14.651  1.00 57.26  ? 212 ARG E CA  1 
ATOM   9544  C C   . ARG E 1 211 ? 20.640  -55.743 -13.892  1.00 55.09  ? 212 ARG E C   1 
ATOM   9545  O O   . ARG E 1 211 ? 21.226  -54.686 -13.640  1.00 56.96  ? 212 ARG E O   1 
ATOM   9546  C CB  . ARG E 1 211 ? 22.584  -57.334 -13.874  1.00 50.76  ? 212 ARG E CB  1 
ATOM   9547  C CG  . ARG E 1 211 ? 22.336  -57.555 -12.389  1.00 67.29  ? 212 ARG E CG  1 
ATOM   9548  C CD  . ARG E 1 211 ? 22.394  -59.029 -12.013  1.00 64.40  ? 212 ARG E CD  1 
ATOM   9549  N NE  . ARG E 1 211 ? 22.309  -59.216 -10.569  1.00 95.68  ? 212 ARG E NE  1 
ATOM   9550  C CZ  . ARG E 1 211 ? 22.345  -60.393 -9.960   1.00 105.40 ? 212 ARG E CZ  1 
ATOM   9551  N NH1 . ARG E 1 211 ? 22.452  -61.523 -10.641  1.00 74.63  ? 212 ARG E NH1 1 
ATOM   9552  N NH2 . ARG E 1 211 ? 22.275  -60.439 -8.632   1.00 79.14  ? 212 ARG E NH2 1 
ATOM   9553  N N   . LEU E 1 212 ? 19.381  -55.984 -13.533  1.00 55.99  ? 213 LEU E N   1 
ATOM   9554  C CA  . LEU E 1 212 ? 18.535  -54.987 -12.892  1.00 48.43  ? 213 LEU E CA  1 
ATOM   9555  C C   . LEU E 1 212 ? 18.159  -55.444 -11.490  1.00 60.22  ? 213 LEU E C   1 
ATOM   9556  O O   . LEU E 1 212 ? 17.820  -56.612 -11.278  1.00 65.05  ? 213 LEU E O   1 
ATOM   9557  C CB  . LEU E 1 212 ? 17.267  -54.733 -13.715  1.00 46.12  ? 213 LEU E CB  1 
ATOM   9558  C CG  . LEU E 1 212 ? 17.471  -54.203 -15.135  1.00 52.57  ? 213 LEU E CG  1 
ATOM   9559  C CD1 . LEU E 1 212 ? 16.162  -54.241 -15.903  1.00 59.47  ? 213 LEU E CD1 1 
ATOM   9560  C CD2 . LEU E 1 212 ? 18.038  -52.791 -15.109  1.00 58.28  ? 213 LEU E CD2 1 
ATOM   9561  N N   . VAL E 1 213 ? 18.221  -54.517 -10.538  1.00 51.33  ? 214 VAL E N   1 
ATOM   9562  C CA  . VAL E 1 213 ? 17.859  -54.787 -9.147   1.00 46.14  ? 214 VAL E CA  1 
ATOM   9563  C C   . VAL E 1 213 ? 16.816  -53.766 -8.707   1.00 54.68  ? 214 VAL E C   1 
ATOM   9564  O O   . VAL E 1 213 ? 16.987  -52.563 -8.959   1.00 49.37  ? 214 VAL E O   1 
ATOM   9565  C CB  . VAL E 1 213 ? 19.094  -54.759 -8.233   1.00 45.70  ? 214 VAL E CB  1 
ATOM   9566  C CG1 . VAL E 1 213 ? 18.681  -54.713 -6.766   1.00 43.06  ? 214 VAL E CG1 1 
ATOM   9567  C CG2 . VAL E 1 213 ? 19.973  -55.972 -8.497   1.00 55.65  ? 214 VAL E CG2 1 
ATOM   9568  N N   . PRO E 1 214 ? 15.722  -54.192 -8.073   1.00 48.85  ? 215 PRO E N   1 
ATOM   9569  C CA  . PRO E 1 214 ? 14.701  -53.232 -7.635   1.00 43.08  ? 215 PRO E CA  1 
ATOM   9570  C C   . PRO E 1 214 ? 15.251  -52.262 -6.601   1.00 59.86  ? 215 PRO E C   1 
ATOM   9571  O O   . PRO E 1 214 ? 16.043  -52.632 -5.731   1.00 55.56  ? 215 PRO E O   1 
ATOM   9572  C CB  . PRO E 1 214 ? 13.606  -54.125 -7.038   1.00 41.86  ? 215 PRO E CB  1 
ATOM   9573  C CG  . PRO E 1 214 ? 13.845  -55.473 -7.627   1.00 39.90  ? 215 PRO E CG  1 
ATOM   9574  C CD  . PRO E 1 214 ? 15.328  -55.581 -7.789   1.00 39.16  ? 215 PRO E CD  1 
ATOM   9575  N N   . LYS E 1 215 ? 14.819  -51.010 -6.704   1.00 55.85  ? 216 LYS E N   1 
ATOM   9576  C CA  . LYS E 1 215 ? 15.148  -49.976 -5.727   1.00 48.10  ? 216 LYS E CA  1 
ATOM   9577  C C   . LYS E 1 215 ? 13.944  -49.816 -4.805   1.00 49.60  ? 216 LYS E C   1 
ATOM   9578  O O   . LYS E 1 215 ? 12.992  -49.099 -5.124   1.00 58.86  ? 216 LYS E O   1 
ATOM   9579  C CB  . LYS E 1 215 ? 15.517  -48.667 -6.418   1.00 34.92  ? 216 LYS E CB  1 
ATOM   9580  C CG  . LYS E 1 215 ? 16.966  -48.604 -6.884   1.00 49.04  ? 216 LYS E CG  1 
ATOM   9581  C CD  . LYS E 1 215 ? 17.253  -47.331 -7.668   1.00 47.89  ? 216 LYS E CD  1 
ATOM   9582  C CE  . LYS E 1 215 ? 16.820  -47.463 -9.119   1.00 65.81  ? 216 LYS E CE  1 
ATOM   9583  N NZ  . LYS E 1 215 ? 17.112  -46.231 -9.901   1.00 73.53  ? 216 LYS E NZ  1 
ATOM   9584  N N   . ILE E 1 216 ? 13.987  -50.496 -3.664   1.00 51.82  ? 217 ILE E N   1 
ATOM   9585  C CA  . ILE E 1 216 ? 12.891  -50.484 -2.703   1.00 53.57  ? 217 ILE E CA  1 
ATOM   9586  C C   . ILE E 1 216 ? 13.110  -49.308 -1.758   1.00 48.78  ? 217 ILE E C   1 
ATOM   9587  O O   . ILE E 1 216 ? 14.000  -49.339 -0.905   1.00 56.21  ? 217 ILE E O   1 
ATOM   9588  C CB  . ILE E 1 216 ? 12.802  -51.808 -1.936   1.00 49.73  ? 217 ILE E CB  1 
ATOM   9589  C CG1 . ILE E 1 216 ? 12.587  -52.969 -2.911   1.00 51.65  ? 217 ILE E CG1 1 
ATOM   9590  C CG2 . ILE E 1 216 ? 11.679  -51.761 -0.914   1.00 51.57  ? 217 ILE E CG2 1 
ATOM   9591  C CD1 . ILE E 1 216 ? 12.511  -54.322 -2.237   1.00 49.03  ? 217 ILE E CD1 1 
ATOM   9592  N N   . ALA E 1 217 ? 12.295  -48.268 -1.911   1.00 51.16  ? 218 ALA E N   1 
ATOM   9593  C CA  . ALA E 1 217 ? 12.409  -47.073 -1.089   1.00 46.70  ? 218 ALA E CA  1 
ATOM   9594  C C   . ALA E 1 217 ? 11.054  -46.380 -1.050   1.00 53.85  ? 218 ALA E C   1 
ATOM   9595  O O   . ALA E 1 217 ? 10.153  -46.689 -1.832   1.00 60.80  ? 218 ALA E O   1 
ATOM   9596  C CB  . ALA E 1 217 ? 13.494  -46.131 -1.619   1.00 46.72  ? 218 ALA E CB  1 
ATOM   9597  N N   . THR E 1 218 ? 10.921  -45.436 -0.121   1.00 69.99  ? 219 THR E N   1 
ATOM   9598  C CA  . THR E 1 218 ? 9.685   -44.680 0.023    1.00 55.23  ? 219 THR E CA  1 
ATOM   9599  C C   . THR E 1 218 ? 9.629   -43.566 -1.015   1.00 66.61  ? 219 THR E C   1 
ATOM   9600  O O   . THR E 1 218 ? 10.568  -42.774 -1.144   1.00 75.08  ? 219 THR E O   1 
ATOM   9601  C CB  . THR E 1 218 ? 9.569   -44.099 1.434    1.00 52.69  ? 219 THR E CB  1 
ATOM   9602  O OG1 . THR E 1 218 ? 10.860  -43.675 1.888    1.00 96.14  ? 219 THR E OG1 1 
ATOM   9603  C CG2 . THR E 1 218 ? 9.006   -45.139 2.395    1.00 39.66  ? 219 THR E CG2 1 
ATOM   9604  N N   . ARG E 1 219 ? 8.526   -43.513 -1.759   1.00 81.87  ? 220 ARG E N   1 
ATOM   9605  C CA  . ARG E 1 219 ? 8.306   -42.500 -2.778   1.00 72.76  ? 220 ARG E CA  1 
ATOM   9606  C C   . ARG E 1 219 ? 6.892   -41.952 -2.649   1.00 77.29  ? 220 ARG E C   1 
ATOM   9607  O O   . ARG E 1 219 ? 6.006   -42.587 -2.072   1.00 60.79  ? 220 ARG E O   1 
ATOM   9608  C CB  . ARG E 1 219 ? 8.522   -43.060 -4.191   1.00 63.53  ? 220 ARG E CB  1 
ATOM   9609  C CG  . ARG E 1 219 ? 9.965   -43.410 -4.520   1.00 77.44  ? 220 ARG E CG  1 
ATOM   9610  C CD  . ARG E 1 219 ? 10.028  -44.307 -5.743   1.00 63.81  ? 220 ARG E CD  1 
ATOM   9611  N NE  . ARG E 1 219 ? 9.342   -45.572 -5.504   1.00 64.05  ? 220 ARG E NE  1 
ATOM   9612  C CZ  . ARG E 1 219 ? 9.954   -46.726 -5.276   1.00 62.12  ? 220 ARG E CZ  1 
ATOM   9613  N NH1 . ARG E 1 219 ? 11.274  -46.825 -5.298   1.00 58.99  ? 220 ARG E NH1 1 
ATOM   9614  N NH2 . ARG E 1 219 ? 9.224   -47.808 -5.025   1.00 59.72  ? 220 ARG E NH2 1 
ATOM   9615  N N   . SER E 1 220 ? 6.692   -40.753 -3.188   1.00 87.35  ? 221 SER E N   1 
ATOM   9616  C CA  . SER E 1 220 ? 5.377   -40.133 -3.184   1.00 78.93  ? 221 SER E CA  1 
ATOM   9617  C C   . SER E 1 220 ? 4.481   -40.766 -4.247   1.00 75.97  ? 221 SER E C   1 
ATOM   9618  O O   . SER E 1 220 ? 4.948   -41.395 -5.200   1.00 78.62  ? 221 SER E O   1 
ATOM   9619  C CB  . SER E 1 220 ? 5.497   -38.627 -3.411   1.00 69.99  ? 221 SER E CB  1 
ATOM   9620  O OG  . SER E 1 220 ? 6.515   -38.333 -4.354   1.00 91.61  ? 221 SER E OG  1 
ATOM   9621  N N   . GLN E 1 221 ? 3.172   -40.592 -4.067   1.00 80.20  ? 222 GLN E N   1 
ATOM   9622  C CA  . GLN E 1 221 ? 2.204   -41.198 -4.972   1.00 68.08  ? 222 GLN E CA  1 
ATOM   9623  C C   . GLN E 1 221 ? 2.169   -40.464 -6.306   1.00 69.66  ? 222 GLN E C   1 
ATOM   9624  O O   . GLN E 1 221 ? 2.079   -39.233 -6.352   1.00 79.42  ? 222 GLN E O   1 
ATOM   9625  C CB  . GLN E 1 221 ? 0.810   -41.199 -4.343   1.00 61.20  ? 222 GLN E CB  1 
ATOM   9626  C CG  . GLN E 1 221 ? 0.495   -42.437 -3.523   1.00 68.42  ? 222 GLN E CG  1 
ATOM   9627  C CD  . GLN E 1 221 ? -0.916  -42.436 -2.968   1.00 71.45  ? 222 GLN E CD  1 
ATOM   9628  O OE1 . GLN E 1 221 ? -1.811  -41.793 -3.515   1.00 74.55  ? 222 GLN E OE1 1 
ATOM   9629  N NE2 . GLN E 1 221 ? -1.120  -43.159 -1.872   1.00 69.15  ? 222 GLN E NE2 1 
ATOM   9630  N N   . VAL E 1 222 ? 2.245   -41.229 -7.392   1.00 63.79  ? 223 VAL E N   1 
ATOM   9631  C CA  . VAL E 1 222 ? 1.996   -40.735 -8.741   1.00 51.93  ? 223 VAL E CA  1 
ATOM   9632  C C   . VAL E 1 222 ? 0.947   -41.638 -9.369   1.00 62.77  ? 223 VAL E C   1 
ATOM   9633  O O   . VAL E 1 222 ? 1.116   -42.863 -9.396   1.00 63.08  ? 223 VAL E O   1 
ATOM   9634  C CB  . VAL E 1 222 ? 3.277   -40.707 -9.595   1.00 52.26  ? 223 VAL E CB  1 
ATOM   9635  C CG1 . VAL E 1 222 ? 2.964   -40.207 -10.998  1.00 52.99  ? 223 VAL E CG1 1 
ATOM   9636  C CG2 . VAL E 1 222 ? 4.334   -39.836 -8.938   1.00 60.01  ? 223 VAL E CG2 1 
ATOM   9637  N N   . ASN E 1 223 ? -0.132  -41.035 -9.873   1.00 52.36  ? 224 ASN E N   1 
ATOM   9638  C CA  . ASN E 1 223 ? -1.316  -41.776 -10.316  1.00 44.27  ? 224 ASN E CA  1 
ATOM   9639  C C   . ASN E 1 223 ? -1.846  -42.678 -9.202   1.00 47.99  ? 224 ASN E C   1 
ATOM   9640  O O   . ASN E 1 223 ? -2.368  -43.767 -9.453   1.00 56.01  ? 224 ASN E O   1 
ATOM   9641  C CB  . ASN E 1 223 ? -1.030  -42.587 -11.584  1.00 57.47  ? 224 ASN E CB  1 
ATOM   9642  C CG  . ASN E 1 223 ? -0.746  -41.708 -12.787  1.00 68.36  ? 224 ASN E CG  1 
ATOM   9643  O OD1 . ASN E 1 223 ? -1.190  -40.562 -12.853  1.00 72.64  ? 224 ASN E OD1 1 
ATOM   9644  N ND2 . ASN E 1 223 ? -0.008  -42.246 -13.752  1.00 65.49  ? 224 ASN E ND2 1 
ATOM   9645  N N   . GLY E 1 224 ? -1.703  -42.226 -7.957   1.00 46.37  ? 225 GLY E N   1 
ATOM   9646  C CA  . GLY E 1 224 ? -2.185  -42.965 -6.809   1.00 46.84  ? 225 GLY E CA  1 
ATOM   9647  C C   . GLY E 1 224 ? -1.360  -44.167 -6.411   1.00 52.24  ? 225 GLY E C   1 
ATOM   9648  O O   . GLY E 1 224 ? -1.781  -44.916 -5.523   1.00 63.13  ? 225 GLY E O   1 
ATOM   9649  N N   . LEU E 1 225 ? -0.202  -44.382 -7.032   1.00 63.19  ? 226 LEU E N   1 
ATOM   9650  C CA  . LEU E 1 225 ? 0.639   -45.539 -6.750   1.00 64.69  ? 226 LEU E CA  1 
ATOM   9651  C C   . LEU E 1 225 ? 2.035   -45.069 -6.365   1.00 59.70  ? 226 LEU E C   1 
ATOM   9652  O O   . LEU E 1 225 ? 2.613   -44.214 -7.043   1.00 60.31  ? 226 LEU E O   1 
ATOM   9653  C CB  . LEU E 1 225 ? 0.712   -46.481 -7.960   1.00 58.38  ? 226 LEU E CB  1 
ATOM   9654  C CG  . LEU E 1 225 ? -0.405  -47.512 -8.174   1.00 53.10  ? 226 LEU E CG  1 
ATOM   9655  C CD1 . LEU E 1 225 ? -0.447  -48.505 -7.025   1.00 73.83  ? 226 LEU E CD1 1 
ATOM   9656  C CD2 . LEU E 1 225 ? -1.767  -46.860 -8.367   1.00 58.28  ? 226 LEU E CD2 1 
ATOM   9657  N N   . ARG E 1 226 ? 2.573   -45.624 -5.278   1.00 58.60  ? 227 ARG E N   1 
ATOM   9658  C CA  . ARG E 1 226 ? 3.903   -45.254 -4.809   1.00 65.65  ? 227 ARG E CA  1 
ATOM   9659  C C   . ARG E 1 226 ? 5.019   -46.055 -5.466   1.00 66.18  ? 227 ARG E C   1 
ATOM   9660  O O   . ARG E 1 226 ? 6.187   -45.665 -5.358   1.00 57.15  ? 227 ARG E O   1 
ATOM   9661  C CB  . ARG E 1 226 ? 3.995   -45.414 -3.288   1.00 80.24  ? 227 ARG E CB  1 
ATOM   9662  C CG  . ARG E 1 226 ? 3.120   -44.439 -2.525   1.00 75.77  ? 227 ARG E CG  1 
ATOM   9663  C CD  . ARG E 1 226 ? 3.525   -44.296 -1.067   1.00 65.32  ? 227 ARG E CD  1 
ATOM   9664  N NE  . ARG E 1 226 ? 2.883   -43.138 -0.456   1.00 79.95  ? 227 ARG E NE  1 
ATOM   9665  C CZ  . ARG E 1 226 ? 1.793   -43.193 0.297    1.00 94.02  ? 227 ARG E CZ  1 
ATOM   9666  N NH1 . ARG E 1 226 ? 1.207   -44.344 0.583    1.00 102.45 ? 227 ARG E NH1 1 
ATOM   9667  N NH2 . ARG E 1 226 ? 1.279   -42.064 0.780    1.00 85.32  ? 227 ARG E NH2 1 
ATOM   9668  N N   . GLY E 1 227 ? 4.697   -47.162 -6.129   1.00 55.93  ? 228 GLY E N   1 
ATOM   9669  C CA  . GLY E 1 227 ? 5.702   -47.914 -6.842   1.00 50.41  ? 228 GLY E CA  1 
ATOM   9670  C C   . GLY E 1 227 ? 6.033   -47.297 -8.185   1.00 61.33  ? 228 GLY E C   1 
ATOM   9671  O O   . GLY E 1 227 ? 5.380   -46.368 -8.659   1.00 53.71  ? 228 GLY E O   1 
ATOM   9672  N N   . ARG E 1 228 ? 7.084   -47.828 -8.804   1.00 50.48  ? 229 ARG E N   1 
ATOM   9673  C CA  . ARG E 1 228 ? 7.530   -47.390 -10.117  1.00 45.84  ? 229 ARG E CA  1 
ATOM   9674  C C   . ARG E 1 228 ? 7.835   -48.607 -10.977  1.00 54.24  ? 229 ARG E C   1 
ATOM   9675  O O   . ARG E 1 228 ? 8.180   -49.679 -10.468  1.00 49.79  ? 229 ARG E O   1 
ATOM   9676  C CB  . ARG E 1 228 ? 8.779   -46.498 -10.039  1.00 34.97  ? 229 ARG E CB  1 
ATOM   9677  C CG  . ARG E 1 228 ? 8.628   -45.259 -9.175   1.00 51.72  ? 229 ARG E CG  1 
ATOM   9678  C CD  . ARG E 1 228 ? 7.655   -44.256 -9.777   1.00 40.20  ? 229 ARG E CD  1 
ATOM   9679  N NE  . ARG E 1 228 ? 7.552   -43.053 -8.958   1.00 64.19  ? 229 ARG E NE  1 
ATOM   9680  C CZ  . ARG E 1 228 ? 6.666   -42.881 -7.986   1.00 62.48  ? 229 ARG E CZ  1 
ATOM   9681  N NH1 . ARG E 1 228 ? 5.772   -43.811 -7.693   1.00 61.86  ? 229 ARG E NH1 1 
ATOM   9682  N NH2 . ARG E 1 228 ? 6.679   -41.748 -7.289   1.00 59.90  ? 229 ARG E NH2 1 
ATOM   9683  N N   . MET E 1 229 ? 7.697   -48.432 -12.289  1.00 56.20  ? 230 MET E N   1 
ATOM   9684  C CA  . MET E 1 229 ? 8.058   -49.458 -13.257  1.00 43.67  ? 230 MET E CA  1 
ATOM   9685  C C   . MET E 1 229 ? 8.953   -48.832 -14.313  1.00 42.77  ? 230 MET E C   1 
ATOM   9686  O O   . MET E 1 229 ? 8.553   -47.872 -14.980  1.00 52.88  ? 230 MET E O   1 
ATOM   9687  C CB  . MET E 1 229 ? 6.812   -50.083 -13.897  1.00 39.96  ? 230 MET E CB  1 
ATOM   9688  C CG  . MET E 1 229 ? 6.131   -51.111 -13.011  1.00 51.28  ? 230 MET E CG  1 
ATOM   9689  S SD  . MET E 1 229 ? 4.547   -51.673 -13.656  1.00 60.86  ? 230 MET E SD  1 
ATOM   9690  C CE  . MET E 1 229 ? 4.105   -52.897 -12.428  1.00 52.28  ? 230 MET E CE  1 
ATOM   9691  N N   . ASP E 1 230 ? 10.159  -49.370 -14.461  1.00 49.08  ? 231 ASP E N   1 
ATOM   9692  C CA  . ASP E 1 230 ? 11.129  -48.884 -15.434  1.00 50.17  ? 231 ASP E CA  1 
ATOM   9693  C C   . ASP E 1 230 ? 11.202  -49.882 -16.578  1.00 51.88  ? 231 ASP E C   1 
ATOM   9694  O O   . ASP E 1 230 ? 11.484  -51.065 -16.356  1.00 50.82  ? 231 ASP E O   1 
ATOM   9695  C CB  . ASP E 1 230 ? 12.504  -48.686 -14.795  1.00 51.88  ? 231 ASP E CB  1 
ATOM   9696  C CG  . ASP E 1 230 ? 12.519  -47.558 -13.783  1.00 63.65  ? 231 ASP E CG  1 
ATOM   9697  O OD1 . ASP E 1 230 ? 11.827  -46.543 -14.016  1.00 76.73  ? 231 ASP E OD1 1 
ATOM   9698  O OD2 . ASP E 1 230 ? 13.215  -47.687 -12.755  1.00 90.14  ? 231 ASP E OD2 1 
ATOM   9699  N N   . PHE E 1 231 ? 10.954  -49.406 -17.794  1.00 44.58  ? 232 PHE E N   1 
ATOM   9700  C CA  . PHE E 1 231 ? 10.880  -50.260 -18.970  1.00 47.93  ? 232 PHE E CA  1 
ATOM   9701  C C   . PHE E 1 231 ? 12.109  -50.068 -19.847  1.00 49.67  ? 232 PHE E C   1 
ATOM   9702  O O   . PHE E 1 231 ? 12.640  -48.959 -19.963  1.00 49.57  ? 232 PHE E O   1 
ATOM   9703  C CB  . PHE E 1 231 ? 9.610   -49.978 -19.774  1.00 39.31  ? 232 PHE E CB  1 
ATOM   9704  C CG  . PHE E 1 231 ? 8.357   -50.473 -19.115  1.00 45.23  ? 232 PHE E CG  1 
ATOM   9705  C CD1 . PHE E 1 231 ? 7.995   -51.808 -19.205  1.00 43.21  ? 232 PHE E CD1 1 
ATOM   9706  C CD2 . PHE E 1 231 ? 7.542   -49.607 -18.403  1.00 44.31  ? 232 PHE E CD2 1 
ATOM   9707  C CE1 . PHE E 1 231 ? 6.844   -52.271 -18.599  1.00 49.93  ? 232 PHE E CE1 1 
ATOM   9708  C CE2 . PHE E 1 231 ? 6.387   -50.062 -17.796  1.00 47.24  ? 232 PHE E CE2 1 
ATOM   9709  C CZ  . PHE E 1 231 ? 6.037   -51.397 -17.893  1.00 56.14  ? 232 PHE E CZ  1 
ATOM   9710  N N   . PHE E 1 232 ? 12.553  -51.161 -20.459  1.00 51.85  ? 233 PHE E N   1 
ATOM   9711  C CA  . PHE E 1 232 ? 13.727  -51.174 -21.314  1.00 50.63  ? 233 PHE E CA  1 
ATOM   9712  C C   . PHE E 1 232 ? 13.367  -51.839 -22.634  1.00 53.57  ? 233 PHE E C   1 
ATOM   9713  O O   . PHE E 1 232 ? 12.336  -52.507 -22.753  1.00 58.42  ? 233 PHE E O   1 
ATOM   9714  C CB  . PHE E 1 232 ? 14.900  -51.903 -20.643  1.00 48.27  ? 233 PHE E CB  1 
ATOM   9715  C CG  . PHE E 1 232 ? 15.339  -51.281 -19.348  1.00 62.51  ? 233 PHE E CG  1 
ATOM   9716  C CD1 . PHE E 1 232 ? 14.662  -51.550 -18.166  1.00 50.17  ? 233 PHE E CD1 1 
ATOM   9717  C CD2 . PHE E 1 232 ? 16.431  -50.429 -19.311  1.00 44.58  ? 233 PHE E CD2 1 
ATOM   9718  C CE1 . PHE E 1 232 ? 15.062  -50.976 -16.974  1.00 43.26  ? 233 PHE E CE1 1 
ATOM   9719  C CE2 . PHE E 1 232 ? 16.839  -49.852 -18.124  1.00 50.60  ? 233 PHE E CE2 1 
ATOM   9720  C CZ  . PHE E 1 232 ? 16.154  -50.126 -16.952  1.00 47.48  ? 233 PHE E CZ  1 
ATOM   9721  N N   . TRP E 1 233 ? 14.223  -51.646 -23.634  1.00 50.24  ? 234 TRP E N   1 
ATOM   9722  C CA  . TRP E 1 233 ? 13.955  -52.201 -24.951  1.00 52.31  ? 234 TRP E CA  1 
ATOM   9723  C C   . TRP E 1 233 ? 15.261  -52.585 -25.629  1.00 53.04  ? 234 TRP E C   1 
ATOM   9724  O O   . TRP E 1 233 ? 16.338  -52.094 -25.282  1.00 53.84  ? 234 TRP E O   1 
ATOM   9725  C CB  . TRP E 1 233 ? 13.169  -51.219 -25.827  1.00 42.54  ? 234 TRP E CB  1 
ATOM   9726  C CG  . TRP E 1 233 ? 13.877  -49.920 -26.070  1.00 51.83  ? 234 TRP E CG  1 
ATOM   9727  C CD1 . TRP E 1 233 ? 13.855  -48.814 -25.272  1.00 57.81  ? 234 TRP E CD1 1 
ATOM   9728  C CD2 . TRP E 1 233 ? 14.706  -49.587 -27.193  1.00 55.86  ? 234 TRP E CD2 1 
ATOM   9729  N NE1 . TRP E 1 233 ? 14.620  -47.815 -25.824  1.00 59.33  ? 234 TRP E NE1 1 
ATOM   9730  C CE2 . TRP E 1 233 ? 15.152  -48.264 -27.004  1.00 53.35  ? 234 TRP E CE2 1 
ATOM   9731  C CE3 . TRP E 1 233 ? 15.114  -50.280 -28.337  1.00 55.37  ? 234 TRP E CE3 1 
ATOM   9732  C CZ2 . TRP E 1 233 ? 15.986  -47.619 -27.915  1.00 61.89  ? 234 TRP E CZ2 1 
ATOM   9733  C CZ3 . TRP E 1 233 ? 15.942  -49.636 -29.243  1.00 58.09  ? 234 TRP E CZ3 1 
ATOM   9734  C CH2 . TRP E 1 233 ? 16.369  -48.320 -29.025  1.00 49.31  ? 234 TRP E CH2 1 
ATOM   9735  N N   . THR E 1 234 ? 15.144  -53.485 -26.602  1.00 50.92  ? 235 THR E N   1 
ATOM   9736  C CA  . THR E 1 234 ? 16.270  -53.908 -27.416  1.00 48.68  ? 235 THR E CA  1 
ATOM   9737  C C   . THR E 1 234 ? 15.746  -54.296 -28.790  1.00 59.15  ? 235 THR E C   1 
ATOM   9738  O O   . THR E 1 234 ? 14.557  -54.578 -28.966  1.00 56.63  ? 235 THR E O   1 
ATOM   9739  C CB  . THR E 1 234 ? 17.027  -55.083 -26.782  1.00 53.00  ? 235 THR E CB  1 
ATOM   9740  O OG1 . THR E 1 234 ? 18.258  -55.294 -27.484  1.00 57.38  ? 235 THR E OG1 1 
ATOM   9741  C CG2 . THR E 1 234 ? 16.193  -56.355 -26.853  1.00 45.64  ? 235 THR E CG2 1 
ATOM   9742  N N   . ILE E 1 235 ? 16.644  -54.295 -29.769  1.00 52.55  ? 236 ILE E N   1 
ATOM   9743  C CA  . ILE E 1 235 ? 16.339  -54.763 -31.114  1.00 55.19  ? 236 ILE E CA  1 
ATOM   9744  C C   . ILE E 1 235 ? 17.005  -56.122 -31.274  1.00 54.76  ? 236 ILE E C   1 
ATOM   9745  O O   . ILE E 1 235 ? 18.238  -56.224 -31.274  1.00 63.97  ? 236 ILE E O   1 
ATOM   9746  C CB  . ILE E 1 235 ? 16.812  -53.776 -32.188  1.00 56.16  ? 236 ILE E CB  1 
ATOM   9747  C CG1 . ILE E 1 235 ? 16.102  -52.429 -32.029  1.00 46.27  ? 236 ILE E CG1 1 
ATOM   9748  C CG2 . ILE E 1 235 ? 16.571  -54.349 -33.576  1.00 42.67  ? 236 ILE E CG2 1 
ATOM   9749  C CD1 . ILE E 1 235 ? 14.618  -52.475 -32.324  1.00 55.49  ? 236 ILE E CD1 1 
ATOM   9750  N N   . LEU E 1 236 ? 16.194  -57.168 -31.403  1.00 49.56  ? 237 LEU E N   1 
ATOM   9751  C CA  . LEU E 1 236 ? 16.697  -58.534 -31.505  1.00 54.69  ? 237 LEU E CA  1 
ATOM   9752  C C   . LEU E 1 236 ? 16.831  -58.888 -32.981  1.00 52.55  ? 237 LEU E C   1 
ATOM   9753  O O   . LEU E 1 236 ? 15.828  -59.077 -33.677  1.00 60.66  ? 237 LEU E O   1 
ATOM   9754  C CB  . LEU E 1 236 ? 15.769  -59.506 -30.782  1.00 45.11  ? 237 LEU E CB  1 
ATOM   9755  C CG  . LEU E 1 236 ? 16.281  -60.939 -30.626  1.00 45.04  ? 237 LEU E CG  1 
ATOM   9756  C CD1 . LEU E 1 236 ? 17.552  -60.971 -29.788  1.00 49.48  ? 237 LEU E CD1 1 
ATOM   9757  C CD2 . LEU E 1 236 ? 15.211  -61.827 -30.014  1.00 40.11  ? 237 LEU E CD2 1 
ATOM   9758  N N   . LYS E 1 237 ? 18.070  -58.974 -33.455  1.00 60.47  ? 238 LYS E N   1 
ATOM   9759  C CA  . LYS E 1 237 ? 18.324  -59.270 -34.854  1.00 58.86  ? 238 LYS E CA  1 
ATOM   9760  C C   . LYS E 1 237 ? 17.968  -60.726 -35.163  1.00 61.60  ? 238 LYS E C   1 
ATOM   9761  O O   . LYS E 1 237 ? 17.966  -61.574 -34.267  1.00 53.53  ? 238 LYS E O   1 
ATOM   9762  C CB  . LYS E 1 237 ? 19.787  -58.982 -35.188  1.00 41.25  ? 238 LYS E CB  1 
ATOM   9763  C CG  . LYS E 1 237 ? 20.097  -57.489 -35.193  1.00 55.44  ? 238 LYS E CG  1 
ATOM   9764  C CD  . LYS E 1 237 ? 21.539  -57.185 -34.825  1.00 55.76  ? 238 LYS E CD  1 
ATOM   9765  C CE  . LYS E 1 237 ? 22.488  -57.466 -35.975  1.00 84.52  ? 238 LYS E CE  1 
ATOM   9766  N NZ  . LYS E 1 237 ? 23.485  -56.366 -36.110  1.00 84.82  ? 238 LYS E NZ  1 
ATOM   9767  N N   . PRO E 1 238 ? 17.638  -61.034 -36.420  1.00 63.62  ? 239 PRO E N   1 
ATOM   9768  C CA  . PRO E 1 238 ? 17.174  -62.389 -36.749  1.00 57.70  ? 239 PRO E CA  1 
ATOM   9769  C C   . PRO E 1 238 ? 18.213  -63.448 -36.409  1.00 61.56  ? 239 PRO E C   1 
ATOM   9770  O O   . PRO E 1 238 ? 19.420  -63.227 -36.534  1.00 66.16  ? 239 PRO E O   1 
ATOM   9771  C CB  . PRO E 1 238 ? 16.917  -62.318 -38.259  1.00 49.89  ? 239 PRO E CB  1 
ATOM   9772  C CG  . PRO E 1 238 ? 16.676  -60.875 -38.531  1.00 59.82  ? 239 PRO E CG  1 
ATOM   9773  C CD  . PRO E 1 238 ? 17.574  -60.137 -37.587  1.00 54.65  ? 239 PRO E CD  1 
ATOM   9774  N N   . ASN E 1 239 ? 17.721  -64.605 -35.962  1.00 52.45  ? 240 ASN E N   1 
ATOM   9775  C CA  . ASN E 1 239 ? 18.486  -65.769 -35.519  1.00 66.37  ? 240 ASN E CA  1 
ATOM   9776  C C   . ASN E 1 239 ? 19.231  -65.524 -34.212  1.00 74.15  ? 240 ASN E C   1 
ATOM   9777  O O   . ASN E 1 239 ? 19.893  -66.444 -33.713  1.00 70.17  ? 240 ASN E O   1 
ATOM   9778  C CB  . ASN E 1 239 ? 19.480  -66.263 -36.580  1.00 58.96  ? 240 ASN E CB  1 
ATOM   9779  C CG  . ASN E 1 239 ? 18.800  -67.010 -37.713  1.00 90.66  ? 240 ASN E CG  1 
ATOM   9780  O OD1 . ASN E 1 239 ? 18.032  -67.945 -37.481  1.00 79.71  ? 240 ASN E OD1 1 
ATOM   9781  N ND2 . ASN E 1 239 ? 19.074  -66.596 -38.944  1.00 84.87  ? 240 ASN E ND2 1 
ATOM   9782  N N   . ASP E 1 240 ? 19.151  -64.326 -33.642  1.00 56.82  ? 241 ASP E N   1 
ATOM   9783  C CA  . ASP E 1 240 ? 19.685  -64.058 -32.317  1.00 51.26  ? 241 ASP E CA  1 
ATOM   9784  C C   . ASP E 1 240 ? 18.604  -64.300 -31.272  1.00 59.42  ? 241 ASP E C   1 
ATOM   9785  O O   . ASP E 1 240 ? 17.411  -64.115 -31.528  1.00 62.54  ? 241 ASP E O   1 
ATOM   9786  C CB  . ASP E 1 240 ? 20.200  -62.621 -32.213  1.00 49.80  ? 241 ASP E CB  1 
ATOM   9787  C CG  . ASP E 1 240 ? 21.039  -62.389 -30.970  1.00 70.54  ? 241 ASP E CG  1 
ATOM   9788  O OD1 . ASP E 1 240 ? 21.586  -63.377 -30.435  1.00 66.53  ? 241 ASP E OD1 1 
ATOM   9789  O OD2 . ASP E 1 240 ? 21.147  -61.224 -30.529  1.00 70.34  ? 241 ASP E OD2 1 
ATOM   9790  N N   . ALA E 1 241 ? 19.032  -64.714 -30.086  1.00 60.48  ? 242 ALA E N   1 
ATOM   9791  C CA  . ALA E 1 241 ? 18.119  -65.055 -29.008  1.00 59.65  ? 242 ALA E CA  1 
ATOM   9792  C C   . ALA E 1 241 ? 18.294  -64.100 -27.835  1.00 55.05  ? 242 ALA E C   1 
ATOM   9793  O O   . ALA E 1 241 ? 19.386  -63.583 -27.587  1.00 63.21  ? 242 ALA E O   1 
ATOM   9794  C CB  . ALA E 1 241 ? 18.336  -66.495 -28.538  1.00 46.46  ? 242 ALA E CB  1 
ATOM   9795  N N   . ILE E 1 242 ? 17.198  -63.869 -27.119  1.00 47.53  ? 243 ILE E N   1 
ATOM   9796  C CA  . ILE E 1 242 ? 17.199  -63.076 -25.897  1.00 47.55  ? 243 ILE E CA  1 
ATOM   9797  C C   . ILE E 1 242 ? 16.968  -64.021 -24.728  1.00 53.31  ? 243 ILE E C   1 
ATOM   9798  O O   . ILE E 1 242 ? 16.131  -64.927 -24.806  1.00 55.93  ? 243 ILE E O   1 
ATOM   9799  C CB  . ILE E 1 242 ? 16.139  -61.955 -25.940  1.00 51.27  ? 243 ILE E CB  1 
ATOM   9800  C CG1 . ILE E 1 242 ? 16.229  -61.086 -24.684  1.00 47.05  ? 243 ILE E CG1 1 
ATOM   9801  C CG2 . ILE E 1 242 ? 14.734  -62.529 -26.123  1.00 41.10  ? 243 ILE E CG2 1 
ATOM   9802  C CD1 . ILE E 1 242 ? 15.508  -59.765 -24.812  1.00 41.80  ? 243 ILE E CD1 1 
ATOM   9803  N N   . HIS E 1 243 ? 17.735  -63.834 -23.658  1.00 49.46  ? 244 HIS E N   1 
ATOM   9804  C CA  . HIS E 1 243 ? 17.687  -64.712 -22.497  1.00 53.78  ? 244 HIS E CA  1 
ATOM   9805  C C   . HIS E 1 243 ? 17.279  -63.910 -21.269  1.00 54.86  ? 244 HIS E C   1 
ATOM   9806  O O   . HIS E 1 243 ? 17.892  -62.882 -20.961  1.00 47.89  ? 244 HIS E O   1 
ATOM   9807  C CB  . HIS E 1 243 ? 19.040  -65.393 -22.275  1.00 52.09  ? 244 HIS E CB  1 
ATOM   9808  C CG  . HIS E 1 243 ? 19.578  -66.075 -23.496  1.00 62.42  ? 244 HIS E CG  1 
ATOM   9809  N ND1 . HIS E 1 243 ? 19.368  -67.411 -23.757  1.00 56.30  ? 244 HIS E ND1 1 
ATOM   9810  C CD2 . HIS E 1 243 ? 20.311  -65.601 -24.531  1.00 54.64  ? 244 HIS E CD2 1 
ATOM   9811  C CE1 . HIS E 1 243 ? 19.951  -67.732 -24.898  1.00 67.79  ? 244 HIS E CE1 1 
ATOM   9812  N NE2 . HIS E 1 243 ? 20.531  -66.651 -25.389  1.00 58.40  ? 244 HIS E NE2 1 
ATOM   9813  N N   . PHE E 1 244 ? 16.247  -64.383 -20.573  1.00 46.59  ? 245 PHE E N   1 
ATOM   9814  C CA  . PHE E 1 244 ? 15.724  -63.733 -19.382  1.00 45.43  ? 245 PHE E CA  1 
ATOM   9815  C C   . PHE E 1 244 ? 15.930  -64.630 -18.171  1.00 49.26  ? 245 PHE E C   1 
ATOM   9816  O O   . PHE E 1 244 ? 15.737  -65.847 -18.247  1.00 53.74  ? 245 PHE E O   1 
ATOM   9817  C CB  . PHE E 1 244 ? 14.230  -63.414 -19.525  1.00 45.56  ? 245 PHE E CB  1 
ATOM   9818  C CG  . PHE E 1 244 ? 13.938  -62.247 -20.421  1.00 51.49  ? 245 PHE E CG  1 
ATOM   9819  C CD1 . PHE E 1 244 ? 14.093  -60.950 -19.962  1.00 55.29  ? 245 PHE E CD1 1 
ATOM   9820  C CD2 . PHE E 1 244 ? 13.492  -62.446 -21.717  1.00 39.37  ? 245 PHE E CD2 1 
ATOM   9821  C CE1 . PHE E 1 244 ? 13.818  -59.871 -20.782  1.00 57.91  ? 245 PHE E CE1 1 
ATOM   9822  C CE2 . PHE E 1 244 ? 13.214  -61.371 -22.542  1.00 40.57  ? 245 PHE E CE2 1 
ATOM   9823  C CZ  . PHE E 1 244 ? 13.378  -60.081 -22.072  1.00 46.81  ? 245 PHE E CZ  1 
ATOM   9824  N N   . GLU E 1 245 ? 16.327  -64.022 -17.055  1.00 45.05  ? 246 GLU E N   1 
ATOM   9825  C CA  . GLU E 1 245 ? 16.411  -64.717 -15.777  1.00 49.10  ? 246 GLU E CA  1 
ATOM   9826  C C   . GLU E 1 245 ? 16.038  -63.742 -14.672  1.00 57.34  ? 246 GLU E C   1 
ATOM   9827  O O   . GLU E 1 245 ? 16.638  -62.668 -14.560  1.00 57.39  ? 246 GLU E O   1 
ATOM   9828  C CB  . GLU E 1 245 ? 17.803  -65.306 -15.542  1.00 64.70  ? 246 GLU E CB  1 
ATOM   9829  C CG  . GLU E 1 245 ? 17.937  -66.039 -14.220  1.00 68.54  ? 246 GLU E CG  1 
ATOM   9830  C CD  . GLU E 1 245 ? 19.148  -66.948 -14.171  1.00 76.83  ? 246 GLU E CD  1 
ATOM   9831  O OE1 . GLU E 1 245 ? 19.452  -67.594 -15.197  1.00 92.69  ? 246 GLU E OE1 1 
ATOM   9832  O OE2 . GLU E 1 245 ? 19.797  -67.018 -13.106  1.00 79.67  ? 246 GLU E OE2 1 
ATOM   9833  N N   . SER E 1 246 ? 15.048  -64.114 -13.861  1.00 49.23  ? 247 SER E N   1 
ATOM   9834  C CA  . SER E 1 246 ? 14.551  -63.243 -12.807  1.00 52.07  ? 247 SER E CA  1 
ATOM   9835  C C   . SER E 1 246 ? 13.880  -64.085 -11.733  1.00 52.80  ? 247 SER E C   1 
ATOM   9836  O O   . SER E 1 246 ? 13.360  -65.170 -12.009  1.00 53.78  ? 247 SER E O   1 
ATOM   9837  C CB  . SER E 1 246 ? 13.564  -62.205 -13.354  1.00 48.99  ? 247 SER E CB  1 
ATOM   9838  O OG  . SER E 1 246 ? 12.969  -61.469 -12.299  1.00 53.34  ? 247 SER E OG  1 
ATOM   9839  N N   . ASN E 1 247 ? 13.898  -63.569 -10.505  1.00 53.81  ? 248 ASN E N   1 
ATOM   9840  C CA  . ASN E 1 247 ? 13.212  -64.194 -9.381   1.00 52.95  ? 248 ASN E CA  1 
ATOM   9841  C C   . ASN E 1 247 ? 12.266  -63.213 -8.696   1.00 49.89  ? 248 ASN E C   1 
ATOM   9842  O O   . ASN E 1 247 ? 11.971  -63.349 -7.507   1.00 52.24  ? 248 ASN E O   1 
ATOM   9843  C CB  . ASN E 1 247 ? 14.212  -64.770 -8.378   1.00 41.30  ? 248 ASN E CB  1 
ATOM   9844  C CG  . ASN E 1 247 ? 15.004  -63.698 -7.662   1.00 42.84  ? 248 ASN E CG  1 
ATOM   9845  O OD1 . ASN E 1 247 ? 15.348  -62.673 -8.246   1.00 59.81  ? 248 ASN E OD1 1 
ATOM   9846  N ND2 . ASN E 1 247 ? 15.294  -63.929 -6.387   1.00 51.96  ? 248 ASN E ND2 1 
ATOM   9847  N N   . GLY E 1 248 ? 11.786  -62.229 -9.433   1.00 48.34  ? 249 GLY E N   1 
ATOM   9848  C CA  . GLY E 1 248 ? 10.818  -61.286 -8.910   1.00 48.94  ? 249 GLY E CA  1 
ATOM   9849  C C   . GLY E 1 248 ? 10.922  -59.946 -9.604   1.00 44.02  ? 249 GLY E C   1 
ATOM   9850  O O   . GLY E 1 248 ? 11.902  -59.631 -10.279  1.00 47.69  ? 249 GLY E O   1 
ATOM   9851  N N   . ASN E 1 249 ? 9.867   -59.146 -9.433   1.00 45.11  ? 250 ASN E N   1 
ATOM   9852  C CA  . ASN E 1 249 ? 9.799   -57.772 -9.931   1.00 44.87  ? 250 ASN E CA  1 
ATOM   9853  C C   . ASN E 1 249 ? 9.937   -57.700 -11.448  1.00 46.59  ? 250 ASN E C   1 
ATOM   9854  O O   . ASN E 1 249 ? 10.385  -56.687 -11.988  1.00 50.85  ? 250 ASN E O   1 
ATOM   9855  C CB  . ASN E 1 249 ? 10.859  -56.891 -9.264   1.00 35.37  ? 250 ASN E CB  1 
ATOM   9856  C CG  . ASN E 1 249 ? 10.786  -56.936 -7.750   1.00 47.88  ? 250 ASN E CG  1 
ATOM   9857  O OD1 . ASN E 1 249 ? 11.143  -57.937 -7.129   1.00 49.19  ? 250 ASN E OD1 1 
ATOM   9858  N ND2 . ASN E 1 249 ? 10.332  -55.843 -7.147   1.00 42.99  ? 250 ASN E ND2 1 
ATOM   9859  N N   . PHE E 1 250 ? 9.541   -58.759 -12.149  1.00 52.56  ? 251 PHE E N   1 
ATOM   9860  C CA  . PHE E 1 250 ? 9.769   -58.882 -13.583  1.00 55.46  ? 251 PHE E CA  1 
ATOM   9861  C C   . PHE E 1 250 ? 8.477   -58.596 -14.338  1.00 51.23  ? 251 PHE E C   1 
ATOM   9862  O O   . PHE E 1 250 ? 7.466   -59.277 -14.130  1.00 59.74  ? 251 PHE E O   1 
ATOM   9863  C CB  . PHE E 1 250 ? 10.299  -60.276 -13.920  1.00 50.38  ? 251 PHE E CB  1 
ATOM   9864  C CG  . PHE E 1 250 ? 10.631  -60.468 -15.370  1.00 56.48  ? 251 PHE E CG  1 
ATOM   9865  C CD1 . PHE E 1 250 ? 11.261  -59.465 -16.091  1.00 49.29  ? 251 PHE E CD1 1 
ATOM   9866  C CD2 . PHE E 1 250 ? 10.328  -61.659 -16.010  1.00 50.83  ? 251 PHE E CD2 1 
ATOM   9867  C CE1 . PHE E 1 250 ? 11.572  -59.643 -17.429  1.00 43.42  ? 251 PHE E CE1 1 
ATOM   9868  C CE2 . PHE E 1 250 ? 10.637  -61.846 -17.345  1.00 42.64  ? 251 PHE E CE2 1 
ATOM   9869  C CZ  . PHE E 1 250 ? 11.259  -60.837 -18.056  1.00 43.23  ? 251 PHE E CZ  1 
ATOM   9870  N N   . ILE E 1 251 ? 8.513   -57.590 -15.207  1.00 50.71  ? 252 ILE E N   1 
ATOM   9871  C CA  . ILE E 1 251 ? 7.412   -57.279 -16.113  1.00 47.94  ? 252 ILE E CA  1 
ATOM   9872  C C   . ILE E 1 251 ? 7.795   -57.875 -17.463  1.00 50.17  ? 252 ILE E C   1 
ATOM   9873  O O   . ILE E 1 251 ? 8.504   -57.250 -18.257  1.00 46.28  ? 252 ILE E O   1 
ATOM   9874  C CB  . ILE E 1 251 ? 7.154   -55.774 -16.201  1.00 46.22  ? 252 ILE E CB  1 
ATOM   9875  C CG1 . ILE E 1 251 ? 7.128   -55.156 -14.801  1.00 51.36  ? 252 ILE E CG1 1 
ATOM   9876  C CG2 . ILE E 1 251 ? 5.845   -55.499 -16.921  1.00 42.53  ? 252 ILE E CG2 1 
ATOM   9877  C CD1 . ILE E 1 251 ? 6.065   -55.734 -13.895  1.00 39.13  ? 252 ILE E CD1 1 
ATOM   9878  N N   . ALA E 1 252 ? 7.323   -59.095 -17.721  1.00 51.43  ? 253 ALA E N   1 
ATOM   9879  C CA  . ALA E 1 252 ? 7.778   -59.913 -18.833  1.00 50.89  ? 253 ALA E CA  1 
ATOM   9880  C C   . ALA E 1 252 ? 7.187   -59.440 -20.161  1.00 52.20  ? 253 ALA E C   1 
ATOM   9881  O O   . ALA E 1 252 ? 6.096   -58.864 -20.198  1.00 49.52  ? 253 ALA E O   1 
ATOM   9882  C CB  . ALA E 1 252 ? 7.399   -61.371 -18.600  1.00 43.53  ? 253 ALA E CB  1 
ATOM   9883  N N   . PRO E 1 253 ? 7.897   -59.668 -21.266  1.00 54.95  ? 254 PRO E N   1 
ATOM   9884  C CA  . PRO E 1 253 ? 7.317   -59.387 -22.584  1.00 52.65  ? 254 PRO E CA  1 
ATOM   9885  C C   . PRO E 1 253 ? 6.235   -60.397 -22.936  1.00 53.84  ? 254 PRO E C   1 
ATOM   9886  O O   . PRO E 1 253 ? 6.327   -61.580 -22.598  1.00 60.29  ? 254 PRO E O   1 
ATOM   9887  C CB  . PRO E 1 253 ? 8.514   -59.505 -23.537  1.00 30.66  ? 254 PRO E CB  1 
ATOM   9888  C CG  . PRO E 1 253 ? 9.732   -59.516 -22.657  1.00 54.02  ? 254 PRO E CG  1 
ATOM   9889  C CD  . PRO E 1 253 ? 9.297   -60.109 -21.364  1.00 55.63  ? 254 PRO E CD  1 
ATOM   9890  N N   . GLU E 1 254 ? 5.197   -59.916 -23.615  1.00 54.23  ? 255 GLU E N   1 
ATOM   9891  C CA  . GLU E 1 254 ? 4.205   -60.787 -24.232  1.00 56.90  ? 255 GLU E CA  1 
ATOM   9892  C C   . GLU E 1 254 ? 4.126   -60.582 -25.735  1.00 60.12  ? 255 GLU E C   1 
ATOM   9893  O O   . GLU E 1 254 ? 4.128   -61.558 -26.493  1.00 55.25  ? 255 GLU E O   1 
ATOM   9894  C CB  . GLU E 1 254 ? 2.822   -60.563 -23.600  1.00 45.33  ? 255 GLU E CB  1 
ATOM   9895  C CG  . GLU E 1 254 ? 1.806   -61.636 -23.964  1.00 71.55  ? 255 GLU E CG  1 
ATOM   9896  C CD  . GLU E 1 254 ? 0.443   -61.390 -23.348  1.00 87.54  ? 255 GLU E CD  1 
ATOM   9897  O OE1 . GLU E 1 254 ? 0.300   -60.410 -22.588  1.00 87.99  ? 255 GLU E OE1 1 
ATOM   9898  O OE2 . GLU E 1 254 ? -0.488  -62.176 -23.627  1.00 91.05  ? 255 GLU E OE2 1 
ATOM   9899  N N   . TYR E 1 255 ? 4.066   -59.332 -26.187  1.00 55.48  ? 256 TYR E N   1 
ATOM   9900  C CA  . TYR E 1 255 ? 4.022   -59.001 -27.601  1.00 51.28  ? 256 TYR E CA  1 
ATOM   9901  C C   . TYR E 1 255 ? 5.250   -58.186 -27.977  1.00 54.32  ? 256 TYR E C   1 
ATOM   9902  O O   . TYR E 1 255 ? 5.707   -57.338 -27.203  1.00 66.70  ? 256 TYR E O   1 
ATOM   9903  C CB  . TYR E 1 255 ? 2.751   -58.220 -27.948  1.00 48.42  ? 256 TYR E CB  1 
ATOM   9904  C CG  . TYR E 1 255 ? 1.482   -59.029 -27.812  1.00 54.40  ? 256 TYR E CG  1 
ATOM   9905  C CD1 . TYR E 1 255 ? 0.823   -59.123 -26.593  1.00 65.95  ? 256 TYR E CD1 1 
ATOM   9906  C CD2 . TYR E 1 255 ? 0.943   -59.697 -28.904  1.00 49.77  ? 256 TYR E CD2 1 
ATOM   9907  C CE1 . TYR E 1 255 ? -0.337  -59.863 -26.465  1.00 51.89  ? 256 TYR E CE1 1 
ATOM   9908  C CE2 . TYR E 1 255 ? -0.217  -60.439 -28.785  1.00 49.30  ? 256 TYR E CE2 1 
ATOM   9909  C CZ  . TYR E 1 255 ? -0.853  -60.518 -27.564  1.00 60.54  ? 256 TYR E CZ  1 
ATOM   9910  O OH  . TYR E 1 255 ? -2.008  -61.256 -27.442  1.00 75.37  ? 256 TYR E OH  1 
ATOM   9911  N N   . ALA E 1 256 ? 5.780   -58.452 -29.167  1.00 53.87  ? 257 ALA E N   1 
ATOM   9912  C CA  . ALA E 1 256 ? 6.895   -57.708 -29.728  1.00 48.47  ? 257 ALA E CA  1 
ATOM   9913  C C   . ALA E 1 256 ? 6.495   -57.197 -31.103  1.00 52.22  ? 257 ALA E C   1 
ATOM   9914  O O   . ALA E 1 256 ? 5.448   -57.561 -31.645  1.00 57.96  ? 257 ALA E O   1 
ATOM   9915  C CB  . ALA E 1 256 ? 8.164   -58.567 -29.818  1.00 49.77  ? 257 ALA E CB  1 
ATOM   9916  N N   . TYR E 1 257 ? 7.338   -56.339 -31.669  1.00 51.23  ? 258 TYR E N   1 
ATOM   9917  C CA  . TYR E 1 257 ? 7.056   -55.700 -32.946  1.00 54.81  ? 258 TYR E CA  1 
ATOM   9918  C C   . TYR E 1 257 ? 8.127   -56.077 -33.957  1.00 51.06  ? 258 TYR E C   1 
ATOM   9919  O O   . TYR E 1 257 ? 9.302   -55.741 -33.775  1.00 54.21  ? 258 TYR E O   1 
ATOM   9920  C CB  . TYR E 1 257 ? 6.982   -54.180 -32.792  1.00 59.82  ? 258 TYR E CB  1 
ATOM   9921  C CG  . TYR E 1 257 ? 5.919   -53.718 -31.824  1.00 57.55  ? 258 TYR E CG  1 
ATOM   9922  C CD1 . TYR E 1 257 ? 4.585   -53.660 -32.205  1.00 50.22  ? 258 TYR E CD1 1 
ATOM   9923  C CD2 . TYR E 1 257 ? 6.249   -53.340 -30.530  1.00 58.05  ? 258 TYR E CD2 1 
ATOM   9924  C CE1 . TYR E 1 257 ? 3.609   -53.237 -31.324  1.00 52.80  ? 258 TYR E CE1 1 
ATOM   9925  C CE2 . TYR E 1 257 ? 5.280   -52.916 -29.641  1.00 57.16  ? 258 TYR E CE2 1 
ATOM   9926  C CZ  . TYR E 1 257 ? 3.962   -52.868 -30.044  1.00 47.92  ? 258 TYR E CZ  1 
ATOM   9927  O OH  . TYR E 1 257 ? 2.995   -52.446 -29.161  1.00 53.99  ? 258 TYR E OH  1 
ATOM   9928  N N   . LYS E 1 258 ? 7.721   -56.775 -35.014  1.00 65.27  ? 259 LYS E N   1 
ATOM   9929  C CA  . LYS E 1 258 ? 8.578   -56.923 -36.180  1.00 52.28  ? 259 LYS E CA  1 
ATOM   9930  C C   . LYS E 1 258 ? 8.722   -55.569 -36.859  1.00 47.68  ? 259 LYS E C   1 
ATOM   9931  O O   . LYS E 1 258 ? 7.724   -54.916 -37.179  1.00 63.71  ? 259 LYS E O   1 
ATOM   9932  C CB  . LYS E 1 258 ? 7.994   -57.953 -37.146  1.00 52.58  ? 259 LYS E CB  1 
ATOM   9933  C CG  . LYS E 1 258 ? 8.373   -59.388 -36.822  1.00 63.87  ? 259 LYS E CG  1 
ATOM   9934  C CD  . LYS E 1 258 ? 7.348   -60.377 -37.355  1.00 65.48  ? 259 LYS E CD  1 
ATOM   9935  C CE  . LYS E 1 258 ? 7.048   -60.147 -38.827  1.00 77.73  ? 259 LYS E CE  1 
ATOM   9936  N NZ  . LYS E 1 258 ? 6.004   -61.088 -39.321  1.00 86.44  ? 259 LYS E NZ  1 
ATOM   9937  N N   . ILE E 1 259 ? 9.962   -55.139 -37.069  1.00 43.83  ? 260 ILE E N   1 
ATOM   9938  C CA  . ILE E 1 259 ? 10.242  -53.780 -37.513  1.00 51.79  ? 260 ILE E CA  1 
ATOM   9939  C C   . ILE E 1 259 ? 11.260  -53.823 -38.645  1.00 61.88  ? 260 ILE E C   1 
ATOM   9940  O O   . ILE E 1 259 ? 12.229  -54.588 -38.600  1.00 58.38  ? 260 ILE E O   1 
ATOM   9941  C CB  . ILE E 1 259 ? 10.737  -52.901 -36.343  1.00 64.07  ? 260 ILE E CB  1 
ATOM   9942  C CG1 . ILE E 1 259 ? 10.941  -51.454 -36.793  1.00 70.13  ? 260 ILE E CG1 1 
ATOM   9943  C CG2 . ILE E 1 259 ? 12.014  -53.469 -35.730  1.00 60.80  ? 260 ILE E CG2 1 
ATOM   9944  C CD1 . ILE E 1 259 ? 11.595  -50.587 -35.738  1.00 76.14  ? 260 ILE E CD1 1 
ATOM   9945  N N   . VAL E 1 260 A 11.015  -53.020 -39.677  1.00 62.80  ? 260 VAL E N   1 
ATOM   9946  C CA  . VAL E 1 260 A 11.948  -52.824 -40.780  1.00 46.83  ? 260 VAL E CA  1 
ATOM   9947  C C   . VAL E 1 260 A 12.096  -51.324 -40.992  1.00 61.03  ? 260 VAL E C   1 
ATOM   9948  O O   . VAL E 1 260 A 11.105  -50.632 -41.251  1.00 59.96  ? 260 VAL E O   1 
ATOM   9949  C CB  . VAL E 1 260 A 11.477  -53.512 -42.072  1.00 64.00  ? 260 VAL E CB  1 
ATOM   9950  C CG1 . VAL E 1 260 A 12.396  -53.151 -43.228  1.00 56.13  ? 260 VAL E CG1 1 
ATOM   9951  C CG2 . VAL E 1 260 A 11.421  -55.021 -41.882  1.00 56.37  ? 260 VAL E CG2 1 
ATOM   9952  N N   . LYS E 1 261 ? 13.323  -50.823 -40.878  1.00 65.16  ? 261 LYS E N   1 
ATOM   9953  C CA  . LYS E 1 261 ? 13.603  -49.400 -41.011  1.00 75.14  ? 261 LYS E CA  1 
ATOM   9954  C C   . LYS E 1 261 ? 14.525  -49.169 -42.199  1.00 76.47  ? 261 LYS E C   1 
ATOM   9955  O O   . LYS E 1 261 ? 15.546  -49.850 -42.341  1.00 79.36  ? 261 LYS E O   1 
ATOM   9956  C CB  . LYS E 1 261 ? 14.233  -48.835 -39.737  1.00 60.16  ? 261 LYS E CB  1 
ATOM   9957  C CG  . LYS E 1 261 ? 14.273  -47.319 -39.706  1.00 70.73  ? 261 LYS E CG  1 
ATOM   9958  C CD  . LYS E 1 261 ? 15.059  -46.819 -38.516  1.00 64.98  ? 261 LYS E CD  1 
ATOM   9959  C CE  . LYS E 1 261 ? 15.078  -45.304 -38.464  1.00 74.38  ? 261 LYS E CE  1 
ATOM   9960  N NZ  . LYS E 1 261 ? 13.703  -44.738 -38.377  1.00 58.65  ? 261 LYS E NZ  1 
ATOM   9961  N N   . LYS E 1 262 ? 14.164  -48.202 -43.045  1.00 75.88  ? 262 LYS E N   1 
ATOM   9962  C CA  . LYS E 1 262 ? 14.927  -47.874 -44.244  1.00 72.70  ? 262 LYS E CA  1 
ATOM   9963  C C   . LYS E 1 262 ? 15.097  -46.367 -44.400  1.00 88.50  ? 262 LYS E C   1 
ATOM   9964  O O   . LYS E 1 262 ? 15.261  -45.868 -45.516  1.00 120.24 ? 262 LYS E O   1 
ATOM   9965  C CB  . LYS E 1 262 ? 14.266  -48.466 -45.489  1.00 80.34  ? 262 LYS E CB  1 
ATOM   9966  C CG  . LYS E 1 262 ? 14.474  -49.961 -45.655  1.00 88.39  ? 262 LYS E CG  1 
ATOM   9967  C CD  . LYS E 1 262 ? 13.563  -50.527 -46.731  1.00 91.88  ? 262 LYS E CD  1 
ATOM   9968  C CE  . LYS E 1 262 ? 13.845  -52.001 -46.973  1.00 100.37 ? 262 LYS E CE  1 
ATOM   9969  N NZ  . LYS E 1 262 ? 12.803  -52.631 -47.831  1.00 107.99 ? 262 LYS E NZ  1 
ATOM   9970  N N   . GLY E 1 263 ? 15.062  -45.633 -43.300  1.00 82.75  ? 263 GLY E N   1 
ATOM   9971  C CA  . GLY E 1 263 ? 15.222  -44.195 -43.351  1.00 88.12  ? 263 GLY E CA  1 
ATOM   9972  C C   . GLY E 1 263 ? 14.790  -43.544 -42.060  1.00 82.23  ? 263 GLY E C   1 
ATOM   9973  O O   . GLY E 1 263 ? 14.052  -44.113 -41.254  1.00 80.50  ? 263 GLY E O   1 
ATOM   9974  N N   . ASP E 1 264 ? 15.254  -42.313 -41.872  1.00 87.55  ? 264 ASP E N   1 
ATOM   9975  C CA  . ASP E 1 264 ? 15.021  -41.557 -40.651  1.00 88.19  ? 264 ASP E CA  1 
ATOM   9976  C C   . ASP E 1 264 ? 14.055  -40.406 -40.901  1.00 73.16  ? 264 ASP E C   1 
ATOM   9977  O O   . ASP E 1 264 ? 13.949  -39.884 -42.014  1.00 80.90  ? 264 ASP E O   1 
ATOM   9978  C CB  . ASP E 1 264 ? 16.338  -41.018 -40.084  1.00 103.30 ? 264 ASP E CB  1 
ATOM   9979  C CG  . ASP E 1 264 ? 17.129  -42.077 -39.341  1.00 123.12 ? 264 ASP E CG  1 
ATOM   9980  O OD1 . ASP E 1 264 ? 16.638  -42.562 -38.300  1.00 90.61  ? 264 ASP E OD1 1 
ATOM   9981  O OD2 . ASP E 1 264 ? 18.235  -42.431 -39.804  1.00 122.95 ? 264 ASP E OD2 1 
ATOM   9982  N N   . SER E 1 265 ? 13.353  -40.019 -39.844  1.00 72.04  ? 265 SER E N   1 
ATOM   9983  C CA  . SER E 1 265 ? 12.375  -38.937 -39.875  1.00 60.23  ? 265 SER E CA  1 
ATOM   9984  C C   . SER E 1 265 ? 12.374  -38.292 -38.492  1.00 67.92  ? 265 SER E C   1 
ATOM   9985  O O   . SER E 1 265 ? 13.327  -38.452 -37.722  1.00 83.36  ? 265 SER E O   1 
ATOM   9986  C CB  . SER E 1 265 ? 10.996  -39.467 -40.303  1.00 70.73  ? 265 SER E CB  1 
ATOM   9987  O OG  . SER E 1 265 ? 10.117  -38.405 -40.628  1.00 67.06  ? 265 SER E OG  1 
ATOM   9988  N N   . THR E 1 266 ? 11.316  -37.549 -38.173  1.00 56.42  ? 266 THR E N   1 
ATOM   9989  C CA  . THR E 1 266 ? 11.195  -36.939 -36.858  1.00 66.33  ? 266 THR E CA  1 
ATOM   9990  C C   . THR E 1 266 ? 9.760   -37.061 -36.365  1.00 62.84  ? 266 THR E C   1 
ATOM   9991  O O   . THR E 1 266 ? 8.859   -37.485 -37.095  1.00 74.65  ? 266 THR E O   1 
ATOM   9992  C CB  . THR E 1 266 ? 11.631  -35.466 -36.877  1.00 65.52  ? 266 THR E CB  1 
ATOM   9993  O OG1 . THR E 1 266 ? 12.023  -35.067 -35.558  1.00 71.82  ? 266 THR E OG1 1 
ATOM   9994  C CG2 . THR E 1 266 ? 10.491  -34.574 -37.354  1.00 73.64  ? 266 THR E CG2 1 
ATOM   9995  N N   . ILE E 1 267 ? 9.561   -36.694 -35.102  1.00 57.33  ? 267 ILE E N   1 
ATOM   9996  C CA  . ILE E 1 267 ? 8.241   -36.648 -34.482  1.00 59.06  ? 267 ILE E CA  1 
ATOM   9997  C C   . ILE E 1 267 ? 7.716   -35.225 -34.598  1.00 57.42  ? 267 ILE E C   1 
ATOM   9998  O O   . ILE E 1 267 ? 8.402   -34.272 -34.206  1.00 74.17  ? 267 ILE E O   1 
ATOM   9999  C CB  . ILE E 1 267 ? 8.298   -37.086 -33.008  1.00 63.25  ? 267 ILE E CB  1 
ATOM   10000 C CG1 . ILE E 1 267 ? 9.060   -38.405 -32.854  1.00 59.33  ? 267 ILE E CG1 1 
ATOM   10001 C CG2 . ILE E 1 267 ? 6.892   -37.209 -32.434  1.00 50.31  ? 267 ILE E CG2 1 
ATOM   10002 C CD1 . ILE E 1 267 ? 8.275   -39.631 -33.254  1.00 60.60  ? 267 ILE E CD1 1 
ATOM   10003 N N   . MET E 1 268 ? 6.507   -35.072 -35.135  1.00 54.08  ? 268 MET E N   1 
ATOM   10004 C CA  . MET E 1 268 ? 5.867   -33.763 -35.221  1.00 56.40  ? 268 MET E CA  1 
ATOM   10005 C C   . MET E 1 268 ? 4.814   -33.629 -34.132  1.00 51.80  ? 268 MET E C   1 
ATOM   10006 O O   . MET E 1 268 ? 3.981   -34.522 -33.950  1.00 64.93  ? 268 MET E O   1 
ATOM   10007 C CB  . MET E 1 268 ? 5.218   -33.515 -36.585  1.00 59.98  ? 268 MET E CB  1 
ATOM   10008 C CG  . MET E 1 268 ? 4.475   -32.170 -36.636  1.00 74.67  ? 268 MET E CG  1 
ATOM   10009 S SD  . MET E 1 268 ? 3.614   -31.875 -38.188  1.00 88.08  ? 268 MET E SD  1 
ATOM   10010 C CE  . MET E 1 268 ? 4.952   -31.518 -39.280  1.00 68.16  ? 268 MET E CE  1 
ATOM   10011 N N   . LYS E 1 269 ? 4.856   -32.507 -33.417  1.00 57.91  ? 269 LYS E N   1 
ATOM   10012 C CA  . LYS E 1 269 ? 3.874   -32.178 -32.391  1.00 67.82  ? 269 LYS E CA  1 
ATOM   10013 C C   . LYS E 1 269 ? 2.835   -31.255 -33.017  1.00 61.45  ? 269 LYS E C   1 
ATOM   10014 O O   . LYS E 1 269 ? 3.135   -30.100 -33.337  1.00 57.50  ? 269 LYS E O   1 
ATOM   10015 C CB  . LYS E 1 269 ? 4.545   -31.520 -31.188  1.00 69.80  ? 269 LYS E CB  1 
ATOM   10016 C CG  . LYS E 1 269 ? 5.679   -32.333 -30.589  1.00 46.71  ? 269 LYS E CG  1 
ATOM   10017 C CD  . LYS E 1 269 ? 5.150   -33.555 -29.863  1.00 78.74  ? 269 LYS E CD  1 
ATOM   10018 C CE  . LYS E 1 269 ? 5.765   -33.670 -28.480  1.00 88.01  ? 269 LYS E CE  1 
ATOM   10019 N NZ  . LYS E 1 269 ? 4.780   -34.188 -27.491  1.00 78.28  ? 269 LYS E NZ  1 
ATOM   10020 N N   . SER E 1 270 ? 1.619   -31.764 -33.202  1.00 78.38  ? 270 SER E N   1 
ATOM   10021 C CA  . SER E 1 270 ? 0.576   -30.992 -33.862  1.00 67.87  ? 270 SER E CA  1 
ATOM   10022 C C   . SER E 1 270 ? -0.788  -31.558 -33.500  1.00 69.86  ? 270 SER E C   1 
ATOM   10023 O O   . SER E 1 270 ? -0.922  -32.744 -33.187  1.00 70.47  ? 270 SER E O   1 
ATOM   10024 C CB  . SER E 1 270 ? 0.758   -30.992 -35.384  1.00 74.15  ? 270 SER E CB  1 
ATOM   10025 O OG  . SER E 1 270 ? -0.428  -30.572 -36.038  1.00 66.91  ? 270 SER E OG  1 
ATOM   10026 N N   . GLY E 1 271 ? -1.798  -30.689 -33.546  1.00 65.32  ? 271 GLY E N   1 
ATOM   10027 C CA  . GLY E 1 271 ? -3.181  -31.091 -33.397  1.00 67.77  ? 271 GLY E CA  1 
ATOM   10028 C C   . GLY E 1 271 ? -4.018  -30.955 -34.648  1.00 74.46  ? 271 GLY E C   1 
ATOM   10029 O O   . GLY E 1 271 ? -5.246  -31.089 -34.570  1.00 70.86  ? 271 GLY E O   1 
ATOM   10030 N N   . VAL E 1 272 ? -3.405  -30.690 -35.803  1.00 74.58  ? 272 VAL E N   1 
ATOM   10031 C CA  . VAL E 1 272 ? -4.159  -30.511 -37.037  1.00 65.56  ? 272 VAL E CA  1 
ATOM   10032 C C   . VAL E 1 272 ? -4.693  -31.857 -37.515  1.00 63.83  ? 272 VAL E C   1 
ATOM   10033 O O   . VAL E 1 272 ? -4.099  -32.915 -37.268  1.00 72.59  ? 272 VAL E O   1 
ATOM   10034 C CB  . VAL E 1 272 ? -3.278  -29.838 -38.106  1.00 67.87  ? 272 VAL E CB  1 
ATOM   10035 C CG1 . VAL E 1 272 ? -4.109  -29.421 -39.309  1.00 74.91  ? 272 VAL E CG1 1 
ATOM   10036 C CG2 . VAL E 1 272 ? -2.567  -28.634 -37.514  1.00 70.87  ? 272 VAL E CG2 1 
ATOM   10037 N N   . GLU E 1 273 ? -5.835  -31.819 -38.194  1.00 76.13  ? 273 GLU E N   1 
ATOM   10038 C CA  . GLU E 1 273 ? -6.504  -33.034 -38.633  1.00 73.57  ? 273 GLU E CA  1 
ATOM   10039 C C   . GLU E 1 273 ? -5.868  -33.588 -39.902  1.00 73.17  ? 273 GLU E C   1 
ATOM   10040 O O   . GLU E 1 273 ? -5.288  -32.853 -40.707  1.00 73.38  ? 273 GLU E O   1 
ATOM   10041 C CB  . GLU E 1 273 ? -7.988  -32.760 -38.875  1.00 89.83  ? 273 GLU E CB  1 
ATOM   10042 C CG  . GLU E 1 273 ? -8.540  -31.628 -38.027  1.00 122.80 ? 273 GLU E CG  1 
ATOM   10043 C CD  . GLU E 1 273 ? -10.054 -31.627 -37.958  1.00 139.34 ? 273 GLU E CD  1 
ATOM   10044 O OE1 . GLU E 1 273 ? -10.682 -32.466 -38.638  1.00 127.01 ? 273 GLU E OE1 1 
ATOM   10045 O OE2 . GLU E 1 273 ? -10.614 -30.789 -37.222  1.00 128.24 ? 273 GLU E OE2 1 
ATOM   10046 N N   . TYR E 1 274 ? -5.983  -34.903 -40.071  1.00 73.72  ? 274 TYR E N   1 
ATOM   10047 C CA  . TYR E 1 274 ? -5.562  -35.541 -41.309  1.00 63.69  ? 274 TYR E CA  1 
ATOM   10048 C C   . TYR E 1 274 ? -6.504  -35.149 -42.444  1.00 77.00  ? 274 TYR E C   1 
ATOM   10049 O O   . TYR E 1 274 ? -7.704  -34.947 -42.241  1.00 81.98  ? 274 TYR E O   1 
ATOM   10050 C CB  . TYR E 1 274 ? -5.528  -37.060 -41.140  1.00 52.77  ? 274 TYR E CB  1 
ATOM   10051 C CG  . TYR E 1 274 ? -5.048  -37.797 -42.366  1.00 71.94  ? 274 TYR E CG  1 
ATOM   10052 C CD1 . TYR E 1 274 ? -3.703  -37.815 -42.705  1.00 70.62  ? 274 TYR E CD1 1 
ATOM   10053 C CD2 . TYR E 1 274 ? -5.940  -38.476 -43.184  1.00 69.68  ? 274 TYR E CD2 1 
ATOM   10054 C CE1 . TYR E 1 274 ? -3.259  -38.485 -43.826  1.00 71.51  ? 274 TYR E CE1 1 
ATOM   10055 C CE2 . TYR E 1 274 ? -5.504  -39.152 -44.306  1.00 76.70  ? 274 TYR E CE2 1 
ATOM   10056 C CZ  . TYR E 1 274 ? -4.164  -39.151 -44.623  1.00 83.45  ? 274 TYR E CZ  1 
ATOM   10057 O OH  . TYR E 1 274 ? -3.721  -39.818 -45.741  1.00 94.63  ? 274 TYR E OH  1 
ATOM   10058 N N   . GLY E 1 275 ? -5.950  -35.035 -43.651  1.00 79.99  ? 275 GLY E N   1 
ATOM   10059 C CA  . GLY E 1 275 ? -6.705  -34.459 -44.748  1.00 79.89  ? 275 GLY E CA  1 
ATOM   10060 C C   . GLY E 1 275 ? -6.848  -35.291 -46.008  1.00 91.26  ? 275 GLY E C   1 
ATOM   10061 O O   . GLY E 1 275 ? -7.443  -34.822 -46.984  1.00 108.21 ? 275 GLY E O   1 
ATOM   10062 N N   . HIS E 1 276 ? -6.319  -36.517 -46.007  1.00 87.19  ? 276 HIS E N   1 
ATOM   10063 C CA  . HIS E 1 276 ? -6.349  -37.393 -47.185  1.00 102.00 ? 276 HIS E CA  1 
ATOM   10064 C C   . HIS E 1 276 ? -5.720  -36.712 -48.398  1.00 93.31  ? 276 HIS E C   1 
ATOM   10065 O O   . HIS E 1 276 ? -6.179  -36.867 -49.532  1.00 92.51  ? 276 HIS E O   1 
ATOM   10066 C CB  . HIS E 1 276 ? -7.772  -37.860 -47.502  1.00 93.08  ? 276 HIS E CB  1 
ATOM   10067 C CG  . HIS E 1 276 ? -8.315  -38.852 -46.521  1.00 110.89 ? 276 HIS E CG  1 
ATOM   10068 N ND1 . HIS E 1 276 ? -8.941  -38.478 -45.351  1.00 106.65 ? 276 HIS E ND1 1 
ATOM   10069 C CD2 . HIS E 1 276 ? -8.320  -40.206 -46.533  1.00 105.57 ? 276 HIS E CD2 1 
ATOM   10070 C CE1 . HIS E 1 276 ? -9.310  -39.558 -44.686  1.00 108.70 ? 276 HIS E CE1 1 
ATOM   10071 N NE2 . HIS E 1 276 ? -8.945  -40.620 -45.381  1.00 124.88 ? 276 HIS E NE2 1 
ATOM   10072 N N   . CYS E 1 277 ? -4.662  -35.949 -48.155  1.00 97.72  ? 277 CYS E N   1 
ATOM   10073 C CA  . CYS E 1 277 ? -3.929  -35.230 -49.181  1.00 67.10  ? 277 CYS E CA  1 
ATOM   10074 C C   . CYS E 1 277 ? -2.524  -35.813 -49.307  1.00 69.75  ? 277 CYS E C   1 
ATOM   10075 O O   . CYS E 1 277 ? -2.186  -36.823 -48.679  1.00 85.50  ? 277 CYS E O   1 
ATOM   10076 C CB  . CYS E 1 277 ? -3.911  -33.734 -48.850  1.00 71.04  ? 277 CYS E CB  1 
ATOM   10077 S SG  . CYS E 1 277 ? -3.752  -33.365 -47.083  1.00 140.83 ? 277 CYS E SG  1 
ATOM   10078 N N   . ASN E 1 278 ? -1.702  -35.178 -50.137  1.00 65.38  ? 278 ASN E N   1 
ATOM   10079 C CA  . ASN E 1 278 ? -0.308  -35.564 -50.288  1.00 62.45  ? 278 ASN E CA  1 
ATOM   10080 C C   . ASN E 1 278 ? 0.527   -34.310 -50.486  1.00 74.93  ? 278 ASN E C   1 
ATOM   10081 O O   . ASN E 1 278 ? 0.046   -33.304 -51.016  1.00 80.13  ? 278 ASN E O   1 
ATOM   10082 C CB  . ASN E 1 278 ? -0.111  -36.530 -51.464  1.00 47.05  ? 278 ASN E CB  1 
ATOM   10083 C CG  . ASN E 1 278 ? 1.229   -37.242 -51.418  1.00 76.77  ? 278 ASN E CG  1 
ATOM   10084 O OD1 . ASN E 1 278 ? 2.220   -36.698 -50.931  1.00 85.09  ? 278 ASN E OD1 1 
ATOM   10085 N ND2 . ASN E 1 278 ? 1.263   -38.466 -51.929  1.00 75.20  ? 278 ASN E ND2 1 
ATOM   10086 N N   . THR E 1 279 ? 1.786   -34.377 -50.059  1.00 70.46  ? 279 THR E N   1 
ATOM   10087 C CA  . THR E 1 279 ? 2.668   -33.224 -50.150  1.00 54.23  ? 279 THR E CA  1 
ATOM   10088 C C   . THR E 1 279 ? 4.112   -33.695 -50.115  1.00 66.67  ? 279 THR E C   1 
ATOM   10089 O O   . THR E 1 279 ? 4.409   -34.828 -49.726  1.00 63.18  ? 279 THR E O   1 
ATOM   10090 C CB  . THR E 1 279 ? 2.410   -32.227 -49.015  1.00 61.20  ? 279 THR E CB  1 
ATOM   10091 O OG1 . THR E 1 279 ? 3.184   -31.041 -49.233  1.00 72.57  ? 279 THR E OG1 1 
ATOM   10092 C CG2 . THR E 1 279 ? 2.798   -32.835 -47.673  1.00 65.07  ? 279 THR E CG2 1 
ATOM   10093 N N   . LYS E 1 280 ? 5.009   -32.805 -50.538  1.00 73.90  ? 280 LYS E N   1 
ATOM   10094 C CA  . LYS E 1 280 ? 6.440   -33.020 -50.396  1.00 76.59  ? 280 LYS E CA  1 
ATOM   10095 C C   . LYS E 1 280 ? 7.039   -32.241 -49.233  1.00 74.31  ? 280 LYS E C   1 
ATOM   10096 O O   . LYS E 1 280 ? 8.224   -32.420 -48.932  1.00 71.35  ? 280 LYS E O   1 
ATOM   10097 C CB  . LYS E 1 280 ? 7.166   -32.652 -51.698  1.00 76.02  ? 280 LYS E CB  1 
ATOM   10098 C CG  . LYS E 1 280 ? 6.732   -33.494 -52.892  1.00 76.34  ? 280 LYS E CG  1 
ATOM   10099 C CD  . LYS E 1 280 ? 7.649   -33.315 -54.095  1.00 75.44  ? 280 LYS E CD  1 
ATOM   10100 C CE  . LYS E 1 280 ? 7.399   -32.001 -54.817  1.00 103.83 ? 280 LYS E CE  1 
ATOM   10101 N NZ  . LYS E 1 280 ? 8.203   -31.915 -56.070  1.00 101.46 ? 280 LYS E NZ  1 
ATOM   10102 N N   . CYS E 1 281 ? 6.253   -31.392 -48.575  1.00 61.70  ? 281 CYS E N   1 
ATOM   10103 C CA  . CYS E 1 281 ? 6.725   -30.627 -47.426  1.00 60.33  ? 281 CYS E CA  1 
ATOM   10104 C C   . CYS E 1 281 ? 5.564   -30.437 -46.462  1.00 74.18  ? 281 CYS E C   1 
ATOM   10105 O O   . CYS E 1 281 ? 4.551   -29.832 -46.824  1.00 78.62  ? 281 CYS E O   1 
ATOM   10106 C CB  . CYS E 1 281 ? 7.293   -29.273 -47.857  1.00 58.68  ? 281 CYS E CB  1 
ATOM   10107 S SG  . CYS E 1 281 ? 7.902   -28.279 -46.484  1.00 87.65  ? 281 CYS E SG  1 
ATOM   10108 N N   . GLN E 1 282 ? 5.713   -30.948 -45.242  1.00 58.19  ? 282 GLN E N   1 
ATOM   10109 C CA  . GLN E 1 282 ? 4.685   -30.863 -44.215  1.00 57.78  ? 282 GLN E CA  1 
ATOM   10110 C C   . GLN E 1 282 ? 5.175   -30.006 -43.056  1.00 52.71  ? 282 GLN E C   1 
ATOM   10111 O O   . GLN E 1 282 ? 6.321   -30.140 -42.614  1.00 59.94  ? 282 GLN E O   1 
ATOM   10112 C CB  . GLN E 1 282 ? 4.300   -32.256 -43.708  1.00 56.15  ? 282 GLN E CB  1 
ATOM   10113 C CG  . GLN E 1 282 ? 3.228   -32.258 -42.628  1.00 60.28  ? 282 GLN E CG  1 
ATOM   10114 C CD  . GLN E 1 282 ? 1.857   -31.886 -43.160  1.00 69.76  ? 282 GLN E CD  1 
ATOM   10115 O OE1 . GLN E 1 282 ? 1.319   -32.555 -44.042  1.00 56.47  ? 282 GLN E OE1 1 
ATOM   10116 N NE2 . GLN E 1 282 ? 1.285   -30.813 -42.626  1.00 66.55  ? 282 GLN E NE2 1 
ATOM   10117 N N   . THR E 1 283 ? 4.306   -29.128 -42.568  1.00 47.43  ? 283 THR E N   1 
ATOM   10118 C CA  . THR E 1 283 ? 4.577   -28.248 -41.444  1.00 64.06  ? 283 THR E CA  1 
ATOM   10119 C C   . THR E 1 283 ? 3.537   -28.486 -40.354  1.00 62.82  ? 283 THR E C   1 
ATOM   10120 O O   . THR E 1 283 ? 2.454   -29.018 -40.627  1.00 58.21  ? 283 THR E O   1 
ATOM   10121 C CB  . THR E 1 283 ? 4.551   -26.772 -41.871  1.00 65.99  ? 283 THR E CB  1 
ATOM   10122 O OG1 . THR E 1 283 ? 3.199   -26.296 -41.871  1.00 65.55  ? 283 THR E OG1 1 
ATOM   10123 C CG2 . THR E 1 283 ? 5.139   -26.603 -43.263  1.00 68.17  ? 283 THR E CG2 1 
ATOM   10124 N N   . PRO E 1 284 ? 3.833   -28.114 -39.104  1.00 71.25  ? 284 PRO E N   1 
ATOM   10125 C CA  . PRO E 1 284 ? 2.867   -28.362 -38.020  1.00 64.15  ? 284 PRO E CA  1 
ATOM   10126 C C   . PRO E 1 284 ? 1.538   -27.652 -38.202  1.00 70.09  ? 284 PRO E C   1 
ATOM   10127 O O   . PRO E 1 284 ? 0.560   -28.034 -37.549  1.00 69.68  ? 284 PRO E O   1 
ATOM   10128 C CB  . PRO E 1 284 ? 3.604   -27.856 -36.771  1.00 57.62  ? 284 PRO E CB  1 
ATOM   10129 C CG  . PRO E 1 284 ? 5.043   -27.954 -37.124  1.00 53.77  ? 284 PRO E CG  1 
ATOM   10130 C CD  . PRO E 1 284 ? 5.107   -27.593 -38.578  1.00 63.97  ? 284 PRO E CD  1 
ATOM   10131 N N   . VAL E 1 285 ? 1.467   -26.628 -39.055  1.00 67.83  ? 285 VAL E N   1 
ATOM   10132 C CA  . VAL E 1 285 ? 0.209   -25.931 -39.307  1.00 62.90  ? 285 VAL E CA  1 
ATOM   10133 C C   . VAL E 1 285 ? -0.434  -26.336 -40.626  1.00 72.53  ? 285 VAL E C   1 
ATOM   10134 O O   . VAL E 1 285 ? -1.604  -25.991 -40.860  1.00 71.81  ? 285 VAL E O   1 
ATOM   10135 C CB  . VAL E 1 285 ? 0.401   -24.399 -39.270  1.00 60.49  ? 285 VAL E CB  1 
ATOM   10136 C CG1 . VAL E 1 285 ? 0.858   -23.957 -37.888  1.00 40.98  ? 285 VAL E CG1 1 
ATOM   10137 C CG2 . VAL E 1 285 ? 1.394   -23.961 -40.335  1.00 62.33  ? 285 VAL E CG2 1 
ATOM   10138 N N   . GLY E 1 286 ? 0.277   -27.049 -41.486  1.00 65.66  ? 286 GLY E N   1 
ATOM   10139 C CA  . GLY E 1 286 ? -0.291  -27.506 -42.738  1.00 61.03  ? 286 GLY E CA  1 
ATOM   10140 C C   . GLY E 1 286 ? 0.787   -27.809 -43.750  1.00 68.13  ? 286 GLY E C   1 
ATOM   10141 O O   . GLY E 1 286 ? 1.967   -27.525 -43.550  1.00 72.55  ? 286 GLY E O   1 
ATOM   10142 N N   . ALA E 1 287 ? 0.353   -28.404 -44.857  1.00 68.45  ? 287 ALA E N   1 
ATOM   10143 C CA  . ALA E 1 287 ? 1.257   -28.723 -45.952  1.00 62.13  ? 287 ALA E CA  1 
ATOM   10144 C C   . ALA E 1 287 ? 1.448   -27.510 -46.854  1.00 64.63  ? 287 ALA E C   1 
ATOM   10145 O O   . ALA E 1 287 ? 0.537   -26.698 -47.040  1.00 70.86  ? 287 ALA E O   1 
ATOM   10146 C CB  . ALA E 1 287 ? 0.722   -29.901 -46.766  1.00 55.47  ? 287 ALA E CB  1 
ATOM   10147 N N   . ILE E 1 288 ? 2.652   -27.389 -47.416  1.00 65.43  ? 288 ILE E N   1 
ATOM   10148 C CA  . ILE E 1 288 ? 2.997   -26.266 -48.278  1.00 73.88  ? 288 ILE E CA  1 
ATOM   10149 C C   . ILE E 1 288 ? 3.561   -26.797 -49.590  1.00 80.84  ? 288 ILE E C   1 
ATOM   10150 O O   . ILE E 1 288 ? 4.047   -27.927 -49.676  1.00 61.93  ? 288 ILE E O   1 
ATOM   10151 C CB  . ILE E 1 288 ? 4.005   -25.301 -47.613  1.00 59.19  ? 288 ILE E CB  1 
ATOM   10152 C CG1 . ILE E 1 288 ? 5.409   -25.908 -47.602  1.00 71.41  ? 288 ILE E CG1 1 
ATOM   10153 C CG2 . ILE E 1 288 ? 3.569   -24.963 -46.196  1.00 66.62  ? 288 ILE E CG2 1 
ATOM   10154 C CD1 . ILE E 1 288 ? 6.472   -24.969 -47.065  1.00 68.08  ? 288 ILE E CD1 1 
ATOM   10155 N N   . ASN E 1 289 ? 3.482   -25.960 -50.622  1.00 88.22  ? 289 ASN E N   1 
ATOM   10156 C CA  . ASN E 1 289 ? 4.053   -26.295 -51.918  1.00 85.69  ? 289 ASN E CA  1 
ATOM   10157 C C   . ASN E 1 289 ? 5.555   -26.036 -51.914  1.00 88.95  ? 289 ASN E C   1 
ATOM   10158 O O   . ASN E 1 289 ? 6.027   -25.045 -51.351  1.00 88.53  ? 289 ASN E O   1 
ATOM   10159 C CB  . ASN E 1 289 ? 3.377   -25.481 -53.023  1.00 89.31  ? 289 ASN E CB  1 
ATOM   10160 C CG  . ASN E 1 289 ? 2.074   -26.101 -53.497  1.00 100.88 ? 289 ASN E CG  1 
ATOM   10161 O OD1 . ASN E 1 289 ? 1.913   -27.321 -53.483  1.00 88.17  ? 289 ASN E OD1 1 
ATOM   10162 N ND2 . ASN E 1 289 ? 1.137   -25.259 -53.925  1.00 113.10 ? 289 ASN E ND2 1 
ATOM   10163 N N   . SER E 1 290 ? 6.308   -26.935 -52.550  1.00 84.36  ? 290 SER E N   1 
ATOM   10164 C CA  . SER E 1 290 ? 7.765   -26.882 -52.541  1.00 71.50  ? 290 SER E CA  1 
ATOM   10165 C C   . SER E 1 290 ? 8.339   -26.464 -53.893  1.00 84.49  ? 290 SER E C   1 
ATOM   10166 O O   . SER E 1 290 ? 9.467   -26.831 -54.231  1.00 83.01  ? 290 SER E O   1 
ATOM   10167 C CB  . SER E 1 290 ? 8.347   -28.231 -52.123  1.00 74.46  ? 290 SER E CB  1 
ATOM   10168 O OG  . SER E 1 290 ? 8.331   -29.143 -53.207  1.00 94.51  ? 290 SER E OG  1 
ATOM   10169 N N   . SER E 1 291 ? 7.576   -25.708 -54.682  1.00 98.10  ? 291 SER E N   1 
ATOM   10170 C CA  . SER E 1 291 ? 8.087   -25.239 -55.966  1.00 85.17  ? 291 SER E CA  1 
ATOM   10171 C C   . SER E 1 291 ? 8.973   -24.009 -55.799  1.00 74.62  ? 291 SER E C   1 
ATOM   10172 O O   . SER E 1 291 ? 10.050  -23.923 -56.398  1.00 77.24  ? 291 SER E O   1 
ATOM   10173 C CB  . SER E 1 291 ? 6.925   -24.939 -56.914  1.00 71.26  ? 291 SER E CB  1 
ATOM   10174 O OG  . SER E 1 291 ? 6.026   -24.013 -56.331  1.00 94.39  ? 291 SER E OG  1 
ATOM   10175 N N   . MET E 1 292 ? 8.535   -23.049 -54.991  1.00 74.69  ? 292 MET E N   1 
ATOM   10176 C CA  . MET E 1 292 ? 9.299   -21.828 -54.806  1.00 63.61  ? 292 MET E CA  1 
ATOM   10177 C C   . MET E 1 292 ? 10.542  -22.094 -53.957  1.00 69.92  ? 292 MET E C   1 
ATOM   10178 O O   . MET E 1 292 ? 10.577  -23.046 -53.173  1.00 76.65  ? 292 MET E O   1 
ATOM   10179 C CB  . MET E 1 292 ? 8.429   -20.755 -54.156  1.00 77.65  ? 292 MET E CB  1 
ATOM   10180 C CG  . MET E 1 292 ? 7.236   -20.324 -55.006  1.00 70.44  ? 292 MET E CG  1 
ATOM   10181 S SD  . MET E 1 292 ? 7.696   -19.574 -56.586  1.00 111.75 ? 292 MET E SD  1 
ATOM   10182 C CE  . MET E 1 292 ? 7.560   -20.962 -57.717  1.00 72.50  ? 292 MET E CE  1 
ATOM   10183 N N   . PRO E 1 293 ? 11.588  -21.274 -54.107  1.00 67.71  ? 293 PRO E N   1 
ATOM   10184 C CA  . PRO E 1 293 ? 12.823  -21.509 -53.346  1.00 63.01  ? 293 PRO E CA  1 
ATOM   10185 C C   . PRO E 1 293 ? 12.776  -21.038 -51.901  1.00 65.99  ? 293 PRO E C   1 
ATOM   10186 O O   . PRO E 1 293 ? 13.669  -21.409 -51.125  1.00 72.31  ? 293 PRO E O   1 
ATOM   10187 C CB  . PRO E 1 293 ? 13.870  -20.718 -54.141  1.00 65.54  ? 293 PRO E CB  1 
ATOM   10188 C CG  . PRO E 1 293 ? 13.091  -19.606 -54.753  1.00 58.51  ? 293 PRO E CG  1 
ATOM   10189 C CD  . PRO E 1 293 ? 11.738  -20.176 -55.079  1.00 66.03  ? 293 PRO E CD  1 
ATOM   10190 N N   . PHE E 1 294 ? 11.781  -20.245 -51.509  1.00 58.79  ? 294 PHE E N   1 
ATOM   10191 C CA  . PHE E 1 294 ? 11.719  -19.702 -50.160  1.00 65.78  ? 294 PHE E CA  1 
ATOM   10192 C C   . PHE E 1 294 ? 10.296  -19.785 -49.628  1.00 56.47  ? 294 PHE E C   1 
ATOM   10193 O O   . PHE E 1 294 ? 9.328   -19.790 -50.394  1.00 67.94  ? 294 PHE E O   1 
ATOM   10194 C CB  . PHE E 1 294 ? 12.209  -18.248 -50.116  1.00 62.46  ? 294 PHE E CB  1 
ATOM   10195 C CG  . PHE E 1 294 ? 13.629  -18.069 -50.577  1.00 61.20  ? 294 PHE E CG  1 
ATOM   10196 C CD1 . PHE E 1 294 ? 14.685  -18.309 -49.715  1.00 63.24  ? 294 PHE E CD1 1 
ATOM   10197 C CD2 . PHE E 1 294 ? 13.906  -17.658 -51.869  1.00 64.78  ? 294 PHE E CD2 1 
ATOM   10198 C CE1 . PHE E 1 294 ? 15.993  -18.144 -50.135  1.00 56.58  ? 294 PHE E CE1 1 
ATOM   10199 C CE2 . PHE E 1 294 ? 15.212  -17.491 -52.294  1.00 61.67  ? 294 PHE E CE2 1 
ATOM   10200 C CZ  . PHE E 1 294 ? 16.256  -17.735 -51.426  1.00 54.56  ? 294 PHE E CZ  1 
ATOM   10201 N N   . HIS E 1 295 ? 10.182  -19.849 -48.302  1.00 62.05  ? 295 HIS E N   1 
ATOM   10202 C CA  . HIS E 1 295 ? 8.889   -19.853 -47.632  1.00 64.43  ? 295 HIS E CA  1 
ATOM   10203 C C   . HIS E 1 295 ? 9.051   -19.230 -46.253  1.00 59.63  ? 295 HIS E C   1 
ATOM   10204 O O   . HIS E 1 295 ? 10.161  -19.131 -45.722  1.00 65.13  ? 295 HIS E O   1 
ATOM   10205 C CB  . HIS E 1 295 ? 8.307   -21.268 -47.521  1.00 58.44  ? 295 HIS E CB  1 
ATOM   10206 C CG  . HIS E 1 295 ? 8.778   -22.025 -46.320  1.00 62.41  ? 295 HIS E CG  1 
ATOM   10207 N ND1 . HIS E 1 295 ? 8.085   -22.035 -45.129  1.00 63.48  ? 295 HIS E ND1 1 
ATOM   10208 C CD2 . HIS E 1 295 ? 9.874   -22.795 -46.123  1.00 61.10  ? 295 HIS E CD2 1 
ATOM   10209 C CE1 . HIS E 1 295 ? 8.732   -22.780 -44.251  1.00 64.44  ? 295 HIS E CE1 1 
ATOM   10210 N NE2 . HIS E 1 295 ? 9.822   -23.253 -44.829  1.00 62.66  ? 295 HIS E NE2 1 
ATOM   10211 N N   . ASN E 1 296 ? 7.924   -18.803 -45.679  1.00 62.36  ? 296 ASN E N   1 
ATOM   10212 C CA  . ASN E 1 296 ? 7.913   -18.115 -44.391  1.00 70.72  ? 296 ASN E CA  1 
ATOM   10213 C C   . ASN E 1 296 ? 6.835   -18.674 -43.469  1.00 67.51  ? 296 ASN E C   1 
ATOM   10214 O O   . ASN E 1 296 ? 6.307   -17.955 -42.617  1.00 65.78  ? 296 ASN E O   1 
ATOM   10215 C CB  . ASN E 1 296 ? 7.721   -16.609 -44.582  1.00 66.02  ? 296 ASN E CB  1 
ATOM   10216 C CG  . ASN E 1 296 ? 6.342   -16.254 -45.121  1.00 67.36  ? 296 ASN E CG  1 
ATOM   10217 O OD1 . ASN E 1 296 ? 5.644   -17.098 -45.685  1.00 57.11  ? 296 ASN E OD1 1 
ATOM   10218 N ND2 . ASN E 1 296 ? 5.949   -14.997 -44.953  1.00 65.03  ? 296 ASN E ND2 1 
ATOM   10219 N N   . ILE E 1 297 ? 6.504   -19.956 -43.618  1.00 68.07  ? 297 ILE E N   1 
ATOM   10220 C CA  . ILE E 1 297 ? 5.355   -20.534 -42.929  1.00 70.07  ? 297 ILE E CA  1 
ATOM   10221 C C   . ILE E 1 297 ? 5.739   -21.048 -41.546  1.00 74.30  ? 297 ILE E C   1 
ATOM   10222 O O   . ILE E 1 297 ? 5.206   -20.580 -40.534  1.00 83.10  ? 297 ILE E O   1 
ATOM   10223 C CB  . ILE E 1 297 ? 4.713   -21.648 -43.776  1.00 69.26  ? 297 ILE E CB  1 
ATOM   10224 C CG1 . ILE E 1 297 ? 3.977   -21.038 -44.972  1.00 69.80  ? 297 ILE E CG1 1 
ATOM   10225 C CG2 . ILE E 1 297 ? 3.757   -22.477 -42.936  1.00 54.32  ? 297 ILE E CG2 1 
ATOM   10226 C CD1 . ILE E 1 297 ? 4.498   -21.499 -46.318  1.00 70.19  ? 297 ILE E CD1 1 
ATOM   10227 N N   . HIS E 1 298 ? 6.665   -22.011 -41.485  1.00 74.65  ? 298 HIS E N   1 
ATOM   10228 C CA  . HIS E 1 298 ? 6.973   -22.644 -40.208  1.00 70.70  ? 298 HIS E CA  1 
ATOM   10229 C C   . HIS E 1 298 ? 8.341   -23.297 -40.282  1.00 72.13  ? 298 HIS E C   1 
ATOM   10230 O O   . HIS E 1 298 ? 8.681   -23.866 -41.328  1.00 67.36  ? 298 HIS E O   1 
ATOM   10231 C CB  . HIS E 1 298 ? 5.907   -23.686 -39.846  1.00 75.45  ? 298 HIS E CB  1 
ATOM   10232 C CG  . HIS E 1 298 ? 5.835   -23.998 -38.384  1.00 74.89  ? 298 HIS E CG  1 
ATOM   10233 N ND1 . HIS E 1 298 ? 6.780   -24.765 -37.737  1.00 79.11  ? 298 HIS E ND1 1 
ATOM   10234 C CD2 . HIS E 1 298 ? 4.925   -23.652 -37.443  1.00 73.71  ? 298 HIS E CD2 1 
ATOM   10235 C CE1 . HIS E 1 298 ? 6.459   -24.872 -36.461  1.00 66.55  ? 298 HIS E CE1 1 
ATOM   10236 N NE2 . HIS E 1 298 ? 5.336   -24.208 -36.256  1.00 71.17  ? 298 HIS E NE2 1 
ATOM   10237 N N   . PRO E 1 299 ? 9.148   -23.239 -39.217  1.00 69.02  ? 299 PRO E N   1 
ATOM   10238 C CA  . PRO E 1 299 ? 10.490  -23.841 -39.281  1.00 69.98  ? 299 PRO E CA  1 
ATOM   10239 C C   . PRO E 1 299 ? 10.536  -25.344 -39.044  1.00 63.58  ? 299 PRO E C   1 
ATOM   10240 O O   . PRO E 1 299 ? 11.548  -25.967 -39.391  1.00 66.58  ? 299 PRO E O   1 
ATOM   10241 C CB  . PRO E 1 299 ? 11.256  -23.095 -38.180  1.00 50.71  ? 299 PRO E CB  1 
ATOM   10242 C CG  . PRO E 1 299 ? 10.200  -22.726 -37.193  1.00 56.96  ? 299 PRO E CG  1 
ATOM   10243 C CD  . PRO E 1 299 ? 8.970   -22.414 -38.007  1.00 68.03  ? 299 PRO E CD  1 
ATOM   10244 N N   . LEU E 1 300 ? 9.492   -25.951 -38.478  1.00 60.60  ? 300 LEU E N   1 
ATOM   10245 C CA  . LEU E 1 300 ? 9.523   -27.371 -38.114  1.00 65.01  ? 300 LEU E CA  1 
ATOM   10246 C C   . LEU E 1 300 ? 8.904   -28.224 -39.222  1.00 63.98  ? 300 LEU E C   1 
ATOM   10247 O O   . LEU E 1 300 ? 7.875   -28.879 -39.053  1.00 74.34  ? 300 LEU E O   1 
ATOM   10248 C CB  . LEU E 1 300 ? 8.811   -27.591 -36.783  1.00 55.09  ? 300 LEU E CB  1 
ATOM   10249 C CG  . LEU E 1 300 ? 9.422   -26.939 -35.541  1.00 57.81  ? 300 LEU E CG  1 
ATOM   10250 C CD1 . LEU E 1 300 ? 8.683   -27.378 -34.282  1.00 60.40  ? 300 LEU E CD1 1 
ATOM   10251 C CD2 . LEU E 1 300 ? 10.902  -27.269 -35.440  1.00 63.09  ? 300 LEU E CD2 1 
ATOM   10252 N N   . THR E 1 301 ? 9.580   -28.237 -40.364  1.00 58.64  ? 301 THR E N   1 
ATOM   10253 C CA  . THR E 1 301 ? 9.105   -28.941 -41.544  1.00 66.46  ? 301 THR E CA  1 
ATOM   10254 C C   . THR E 1 301 ? 9.736   -30.324 -41.660  1.00 55.21  ? 301 THR E C   1 
ATOM   10255 O O   . THR E 1 301 ? 10.809  -30.598 -41.116  1.00 68.14  ? 301 THR E O   1 
ATOM   10256 C CB  . THR E 1 301 ? 9.407   -28.135 -42.809  1.00 61.63  ? 301 THR E CB  1 
ATOM   10257 O OG1 . THR E 1 301 ? 10.826  -27.989 -42.956  1.00 57.18  ? 301 THR E OG1 1 
ATOM   10258 C CG2 . THR E 1 301 ? 8.773   -26.758 -42.721  1.00 71.87  ? 301 THR E CG2 1 
ATOM   10259 N N   . ILE E 1 302 ? 9.043   -31.196 -42.388  1.00 55.78  ? 302 ILE E N   1 
ATOM   10260 C CA  . ILE E 1 302 ? 9.573   -32.487 -42.804  1.00 71.73  ? 302 ILE E CA  1 
ATOM   10261 C C   . ILE E 1 302 ? 9.410   -32.600 -44.306  1.00 73.45  ? 302 ILE E C   1 
ATOM   10262 O O   . ILE E 1 302 ? 8.322   -32.346 -44.838  1.00 62.62  ? 302 ILE E O   1 
ATOM   10263 C CB  . ILE E 1 302 ? 8.845   -33.671 -42.146  1.00 51.33  ? 302 ILE E CB  1 
ATOM   10264 C CG1 . ILE E 1 302 ? 8.465   -33.348 -40.709  1.00 48.40  ? 302 ILE E CG1 1 
ATOM   10265 C CG2 . ILE E 1 302 ? 9.687   -34.948 -42.195  1.00 70.80  ? 302 ILE E CG2 1 
ATOM   10266 C CD1 . ILE E 1 302 ? 7.651   -34.528 -40.000  1.00 69.80  ? 302 ILE E CD1 1 
ATOM   10267 N N   . GLY E 1 303 ? 10.454  -33.069 -44.971  1.00 79.30  ? 303 GLY E N   1 
ATOM   10268 C CA  . GLY E 1 303 ? 10.392  -33.307 -46.392  1.00 75.46  ? 303 GLY E CA  1 
ATOM   10269 C C   . GLY E 1 303 ? 11.374  -32.458 -47.164  1.00 69.80  ? 303 GLY E C   1 
ATOM   10270 O O   . GLY E 1 303 ? 12.371  -31.980 -46.616  1.00 70.33  ? 303 GLY E O   1 
ATOM   10271 N N   . GLU E 1 304 ? 11.092  -32.271 -48.449  1.00 75.16  ? 304 GLU E N   1 
ATOM   10272 C CA  . GLU E 1 304 ? 11.891  -31.423 -49.323  1.00 77.09  ? 304 GLU E CA  1 
ATOM   10273 C C   . GLU E 1 304 ? 11.226  -30.052 -49.363  1.00 71.45  ? 304 GLU E C   1 
ATOM   10274 O O   . GLU E 1 304 ? 10.194  -29.873 -50.021  1.00 73.48  ? 304 GLU E O   1 
ATOM   10275 C CB  . GLU E 1 304 ? 12.001  -32.026 -50.722  1.00 66.14  ? 304 GLU E CB  1 
ATOM   10276 C CG  . GLU E 1 304 ? 12.515  -33.457 -50.751  1.00 71.06  ? 304 GLU E CG  1 
ATOM   10277 C CD  . GLU E 1 304 ? 11.441  -34.471 -50.409  1.00 91.97  ? 304 GLU E CD  1 
ATOM   10278 O OE1 . GLU E 1 304 ? 10.263  -34.072 -50.282  1.00 97.15  ? 304 GLU E OE1 1 
ATOM   10279 O OE2 . GLU E 1 304 ? 11.773  -35.666 -50.263  1.00 94.79  ? 304 GLU E OE2 1 
ATOM   10280 N N   . CYS E 1 305 ? 11.817  -29.086 -48.668  1.00 65.69  ? 305 CYS E N   1 
ATOM   10281 C CA  . CYS E 1 305 ? 11.135  -27.826 -48.434  1.00 69.60  ? 305 CYS E CA  1 
ATOM   10282 C C   . CYS E 1 305 ? 11.967  -26.645 -48.912  1.00 63.97  ? 305 CYS E C   1 
ATOM   10283 O O   . CYS E 1 305 ? 13.197  -26.720 -48.947  1.00 78.50  ? 305 CYS E O   1 
ATOM   10284 C CB  . CYS E 1 305 ? 10.821  -27.640 -46.944  1.00 73.35  ? 305 CYS E CB  1 
ATOM   10285 S SG  . CYS E 1 305 ? 9.804   -28.936 -46.211  1.00 102.97 ? 305 CYS E SG  1 
ATOM   10286 N N   . PRO E 1 306 ? 11.322  -25.543 -49.289  1.00 62.78  ? 306 PRO E N   1 
ATOM   10287 C CA  . PRO E 1 306 ? 12.064  -24.307 -49.553  1.00 66.74  ? 306 PRO E CA  1 
ATOM   10288 C C   . PRO E 1 306 ? 12.729  -23.790 -48.287  1.00 64.57  ? 306 PRO E C   1 
ATOM   10289 O O   . PRO E 1 306 ? 12.311  -24.088 -47.166  1.00 64.30  ? 306 PRO E O   1 
ATOM   10290 C CB  . PRO E 1 306 ? 10.983  -23.340 -50.055  1.00 57.79  ? 306 PRO E CB  1 
ATOM   10291 C CG  . PRO E 1 306 ? 9.688   -23.922 -49.591  1.00 65.30  ? 306 PRO E CG  1 
ATOM   10292 C CD  . PRO E 1 306 ? 9.889   -25.405 -49.601  1.00 64.68  ? 306 PRO E CD  1 
ATOM   10293 N N   . LYS E 1 307 ? 13.792  -23.015 -48.484  1.00 59.35  ? 307 LYS E N   1 
ATOM   10294 C CA  . LYS E 1 307 ? 14.529  -22.459 -47.358  1.00 53.50  ? 307 LYS E CA  1 
ATOM   10295 C C   . LYS E 1 307 ? 13.654  -21.482 -46.580  1.00 63.87  ? 307 LYS E C   1 
ATOM   10296 O O   . LYS E 1 307 ? 12.988  -20.621 -47.162  1.00 60.43  ? 307 LYS E O   1 
ATOM   10297 C CB  . LYS E 1 307 ? 15.800  -21.773 -47.852  1.00 48.88  ? 307 LYS E CB  1 
ATOM   10298 C CG  . LYS E 1 307 ? 16.683  -22.682 -48.694  1.00 62.55  ? 307 LYS E CG  1 
ATOM   10299 C CD  . LYS E 1 307 ? 17.256  -23.820 -47.864  1.00 61.07  ? 307 LYS E CD  1 
ATOM   10300 C CE  . LYS E 1 307 ? 17.744  -24.960 -48.746  1.00 54.85  ? 307 LYS E CE  1 
ATOM   10301 N NZ  . LYS E 1 307 ? 16.608  -25.743 -49.312  1.00 80.36  ? 307 LYS E NZ  1 
ATOM   10302 N N   . TYR E 1 308 ? 13.654  -21.626 -45.257  1.00 59.39  ? 308 TYR E N   1 
ATOM   10303 C CA  . TYR E 1 308 ? 12.796  -20.825 -44.396  1.00 57.87  ? 308 TYR E CA  1 
ATOM   10304 C C   . TYR E 1 308 ? 13.447  -19.475 -44.124  1.00 57.61  ? 308 TYR E C   1 
ATOM   10305 O O   . TYR E 1 308 ? 14.588  -19.410 -43.658  1.00 69.76  ? 308 TYR E O   1 
ATOM   10306 C CB  . TYR E 1 308 ? 12.527  -21.573 -43.089  1.00 53.51  ? 308 TYR E CB  1 
ATOM   10307 C CG  . TYR E 1 308 ? 11.744  -20.796 -42.055  1.00 64.44  ? 308 TYR E CG  1 
ATOM   10308 C CD1 . TYR E 1 308 ? 10.388  -20.544 -42.221  1.00 61.22  ? 308 TYR E CD1 1 
ATOM   10309 C CD2 . TYR E 1 308 ? 12.359  -20.332 -40.897  1.00 59.99  ? 308 TYR E CD2 1 
ATOM   10310 C CE1 . TYR E 1 308 ? 9.668   -19.837 -41.270  1.00 60.62  ? 308 TYR E CE1 1 
ATOM   10311 C CE2 . TYR E 1 308 ? 11.648  -19.626 -39.942  1.00 54.25  ? 308 TYR E CE2 1 
ATOM   10312 C CZ  . TYR E 1 308 ? 10.305  -19.382 -40.133  1.00 64.11  ? 308 TYR E CZ  1 
ATOM   10313 O OH  . TYR E 1 308 ? 9.595   -18.681 -39.186  1.00 73.54  ? 308 TYR E OH  1 
ATOM   10314 N N   . VAL E 1 309 ? 12.721  -18.395 -44.415  1.00 58.96  ? 309 VAL E N   1 
ATOM   10315 C CA  . VAL E 1 309 ? 13.233  -17.041 -44.254  1.00 57.11  ? 309 VAL E CA  1 
ATOM   10316 C C   . VAL E 1 309 ? 12.245  -16.219 -43.439  1.00 57.59  ? 309 VAL E C   1 
ATOM   10317 O O   . VAL E 1 309 ? 11.044  -16.504 -43.408  1.00 57.93  ? 309 VAL E O   1 
ATOM   10318 C CB  . VAL E 1 309 ? 13.503  -16.360 -45.616  1.00 60.44  ? 309 VAL E CB  1 
ATOM   10319 C CG1 . VAL E 1 309 ? 14.555  -17.123 -46.396  1.00 58.97  ? 309 VAL E CG1 1 
ATOM   10320 C CG2 . VAL E 1 309 ? 12.216  -16.248 -46.421  1.00 45.21  ? 309 VAL E CG2 1 
ATOM   10321 N N   . LYS E 1 310 ? 12.766  -15.184 -42.775  1.00 65.13  ? 310 LYS E N   1 
ATOM   10322 C CA  . LYS E 1 310 ? 11.941  -14.205 -42.066  1.00 60.11  ? 310 LYS E CA  1 
ATOM   10323 C C   . LYS E 1 310 ? 11.688  -13.033 -43.008  1.00 69.34  ? 310 LYS E C   1 
ATOM   10324 O O   . LYS E 1 310 ? 12.334  -11.984 -42.948  1.00 86.16  ? 310 LYS E O   1 
ATOM   10325 C CB  . LYS E 1 310 ? 12.620  -13.761 -40.775  1.00 68.51  ? 310 LYS E CB  1 
ATOM   10326 C CG  . LYS E 1 310 ? 11.904  -12.649 -40.017  1.00 91.05  ? 310 LYS E CG  1 
ATOM   10327 C CD  . LYS E 1 310 ? 12.218  -12.727 -38.527  1.00 75.22  ? 310 LYS E CD  1 
ATOM   10328 C CE  . LYS E 1 310 ? 12.194  -11.343 -37.876  1.00 85.66  ? 310 LYS E CE  1 
ATOM   10329 N NZ  . LYS E 1 310 ? 11.423  -10.360 -38.703  1.00 92.02  ? 310 LYS E NZ  1 
ATOM   10330 N N   . SER E 1 311 ? 10.728  -13.232 -43.907  1.00 70.10  ? 311 SER E N   1 
ATOM   10331 C CA  . SER E 1 311 ? 10.399  -12.244 -44.921  1.00 71.23  ? 311 SER E CA  1 
ATOM   10332 C C   . SER E 1 311 ? 8.906   -12.284 -45.207  1.00 77.41  ? 311 SER E C   1 
ATOM   10333 O O   . SER E 1 311 ? 8.255   -13.322 -45.059  1.00 66.56  ? 311 SER E O   1 
ATOM   10334 C CB  . SER E 1 311 ? 11.190  -12.487 -46.213  1.00 75.45  ? 311 SER E CB  1 
ATOM   10335 O OG  . SER E 1 311 ? 10.942  -11.464 -47.161  1.00 93.89  ? 311 SER E OG  1 
ATOM   10336 N N   . ASN E 1 312 ? 8.372   -11.138 -45.623  1.00 74.15  ? 312 ASN E N   1 
ATOM   10337 C CA  . ASN E 1 312 ? 6.965   -11.004 -45.979  1.00 71.76  ? 312 ASN E CA  1 
ATOM   10338 C C   . ASN E 1 312 ? 6.718   -11.128 -47.476  1.00 68.99  ? 312 ASN E C   1 
ATOM   10339 O O   . ASN E 1 312 ? 5.685   -11.666 -47.885  1.00 82.49  ? 312 ASN E O   1 
ATOM   10340 C CB  . ASN E 1 312 ? 6.423   -9.658  -45.486  1.00 82.59  ? 312 ASN E CB  1 
ATOM   10341 C CG  . ASN E 1 312 ? 6.433   -9.544  -43.973  1.00 87.86  ? 312 ASN E CG  1 
ATOM   10342 O OD1 . ASN E 1 312 ? 6.064   -10.482 -43.266  1.00 86.36  ? 312 ASN E OD1 1 
ATOM   10343 N ND2 . ASN E 1 312 ? 6.860   -8.391  -43.468  1.00 80.29  ? 312 ASN E ND2 1 
ATOM   10344 N N   . LYS E 1 313 ? 7.641   -10.639 -48.301  1.00 89.82  ? 313 LYS E N   1 
ATOM   10345 C CA  . LYS E 1 313 ? 7.492   -10.697 -49.747  1.00 75.40  ? 313 LYS E CA  1 
ATOM   10346 C C   . LYS E 1 313 ? 8.866   -10.726 -50.398  1.00 80.43  ? 313 LYS E C   1 
ATOM   10347 O O   . LYS E 1 313 ? 9.790   -10.039 -49.954  1.00 77.41  ? 313 LYS E O   1 
ATOM   10348 C CB  . LYS E 1 313 ? 6.687   -9.506  -50.277  1.00 75.53  ? 313 LYS E CB  1 
ATOM   10349 C CG  . LYS E 1 313 ? 7.023   -8.185  -49.603  1.00 90.13  ? 313 LYS E CG  1 
ATOM   10350 C CD  . LYS E 1 313 ? 6.560   -7.006  -50.439  1.00 102.61 ? 313 LYS E CD  1 
ATOM   10351 C CE  . LYS E 1 313 ? 7.554   -6.711  -51.549  1.00 120.24 ? 313 LYS E CE  1 
ATOM   10352 N NZ  . LYS E 1 313 ? 7.068   -5.658  -52.482  1.00 108.30 ? 313 LYS E NZ  1 
ATOM   10353 N N   . LEU E 1 314 ? 8.990   -11.534 -51.450  1.00 69.92  ? 314 LEU E N   1 
ATOM   10354 C CA  . LEU E 1 314 ? 10.180  -11.586 -52.299  1.00 69.11  ? 314 LEU E CA  1 
ATOM   10355 C C   . LEU E 1 314 ? 9.672   -11.583 -53.736  1.00 77.73  ? 314 LEU E C   1 
ATOM   10356 O O   . LEU E 1 314 ? 9.488   -12.640 -54.343  1.00 73.76  ? 314 LEU E O   1 
ATOM   10357 C CB  . LEU E 1 314 ? 11.030  -12.817 -51.994  1.00 65.18  ? 314 LEU E CB  1 
ATOM   10358 C CG  . LEU E 1 314 ? 11.672  -12.902 -50.609  1.00 62.87  ? 314 LEU E CG  1 
ATOM   10359 C CD1 . LEU E 1 314 ? 12.233  -14.295 -50.376  1.00 69.50  ? 314 LEU E CD1 1 
ATOM   10360 C CD2 . LEU E 1 314 ? 12.763  -11.853 -50.459  1.00 61.40  ? 314 LEU E CD2 1 
ATOM   10361 N N   . VAL E 1 315 ? 9.451   -10.391 -54.282  1.00 73.91  ? 315 VAL E N   1 
ATOM   10362 C CA  . VAL E 1 315 ? 8.802   -10.225 -55.578  1.00 81.61  ? 315 VAL E CA  1 
ATOM   10363 C C   . VAL E 1 315 ? 9.818   -9.676  -56.570  1.00 69.09  ? 315 VAL E C   1 
ATOM   10364 O O   . VAL E 1 315 ? 10.469  -8.656  -56.311  1.00 67.89  ? 315 VAL E O   1 
ATOM   10365 C CB  . VAL E 1 315 ? 7.557   -9.324  -55.473  1.00 67.61  ? 315 VAL E CB  1 
ATOM   10366 C CG1 . VAL E 1 315 ? 7.899   -7.978  -54.848  1.00 92.63  ? 315 VAL E CG1 1 
ATOM   10367 C CG2 . VAL E 1 315 ? 6.917   -9.143  -56.831  1.00 79.42  ? 315 VAL E CG2 1 
ATOM   10368 N N   . LEU E 1 316 ? 9.968   -10.371 -57.694  1.00 67.35  ? 316 LEU E N   1 
ATOM   10369 C CA  . LEU E 1 316 ? 10.874  -9.972  -58.759  1.00 67.25  ? 316 LEU E CA  1 
ATOM   10370 C C   . LEU E 1 316 ? 10.121  -9.194  -59.826  1.00 71.11  ? 316 LEU E C   1 
ATOM   10371 O O   . LEU E 1 316 ? 9.007   -9.562  -60.210  1.00 67.46  ? 316 LEU E O   1 
ATOM   10372 C CB  . LEU E 1 316 ? 11.546  -11.190 -59.393  1.00 41.33  ? 316 LEU E CB  1 
ATOM   10373 C CG  . LEU E 1 316 ? 12.698  -11.855 -58.642  1.00 66.06  ? 316 LEU E CG  1 
ATOM   10374 C CD1 . LEU E 1 316 ? 13.145  -13.109 -59.375  1.00 58.73  ? 316 LEU E CD1 1 
ATOM   10375 C CD2 . LEU E 1 316 ? 13.856  -10.885 -58.484  1.00 59.07  ? 316 LEU E CD2 1 
ATOM   10376 N N   . ALA E 1 317 ? 10.739  -8.121  -60.310  1.00 74.58  ? 317 ALA E N   1 
ATOM   10377 C CA  . ALA E 1 317 ? 10.182  -7.385  -61.437  1.00 66.15  ? 317 ALA E CA  1 
ATOM   10378 C C   . ALA E 1 317 ? 10.429  -8.167  -62.721  1.00 59.15  ? 317 ALA E C   1 
ATOM   10379 O O   . ALA E 1 317 ? 11.581  -8.395  -63.105  1.00 67.94  ? 317 ALA E O   1 
ATOM   10380 C CB  . ALA E 1 317 ? 10.805  -5.995  -61.523  1.00 56.38  ? 317 ALA E CB  1 
ATOM   10381 N N   . THR E 1 318 ? 9.348   -8.594  -63.375  1.00 67.57  ? 318 THR E N   1 
ATOM   10382 C CA  . THR E 1 318 ? 9.433   -9.292  -64.652  1.00 78.70  ? 318 THR E CA  1 
ATOM   10383 C C   . THR E 1 318 ? 8.770   -8.497  -65.771  1.00 77.68  ? 318 THR E C   1 
ATOM   10384 O O   . THR E 1 318 ? 8.459   -9.053  -66.829  1.00 86.62  ? 318 THR E O   1 
ATOM   10385 C CB  . THR E 1 318 ? 8.818   -10.690 -64.550  1.00 70.16  ? 318 THR E CB  1 
ATOM   10386 O OG1 . THR E 1 318 ? 8.965   -11.372 -65.802  1.00 110.97 ? 318 THR E OG1 1 
ATOM   10387 C CG2 . THR E 1 318 ? 7.343   -10.606 -64.197  1.00 84.39  ? 318 THR E CG2 1 
ATOM   10388 N N   . GLY E 1 319 ? 8.552   -7.203  -65.554  1.00 74.76  ? 319 GLY E N   1 
ATOM   10389 C CA  . GLY E 1 319 ? 7.980   -6.335  -66.564  1.00 69.43  ? 319 GLY E CA  1 
ATOM   10390 C C   . GLY E 1 319 ? 8.676   -4.991  -66.615  1.00 75.05  ? 319 GLY E C   1 
ATOM   10391 O O   . GLY E 1 319 ? 9.840   -4.877  -66.222  1.00 75.84  ? 319 GLY E O   1 
ATOM   10392 N N   . LEU E 1 320 ? 7.976   -3.965  -67.090  1.00 66.77  ? 320 LEU E N   1 
ATOM   10393 C CA  . LEU E 1 320 ? 8.539   -2.633  -67.248  1.00 74.40  ? 320 LEU E CA  1 
ATOM   10394 C C   . LEU E 1 320 ? 7.972   -1.690  -66.196  1.00 66.90  ? 320 LEU E C   1 
ATOM   10395 O O   . LEU E 1 320 ? 6.959   -1.976  -65.555  1.00 71.00  ? 320 LEU E O   1 
ATOM   10396 C CB  . LEU E 1 320 ? 8.258   -2.071  -68.647  1.00 62.57  ? 320 LEU E CB  1 
ATOM   10397 C CG  . LEU E 1 320 ? 8.915   -2.754  -69.849  1.00 75.13  ? 320 LEU E CG  1 
ATOM   10398 C CD1 . LEU E 1 320 ? 8.166   -4.014  -70.253  1.00 79.80  ? 320 LEU E CD1 1 
ATOM   10399 C CD2 . LEU E 1 320 ? 9.007   -1.793  -71.017  1.00 80.97  ? 320 LEU E CD2 1 
ATOM   10400 N N   . ARG E 1 321 ? 8.648   -0.555  -66.025  1.00 76.76  ? 321 ARG E N   1 
ATOM   10401 C CA  . ARG E 1 321 ? 8.147   0.477   -65.129  1.00 72.45  ? 321 ARG E CA  1 
ATOM   10402 C C   . ARG E 1 321 ? 6.806   1.003   -65.623  1.00 75.07  ? 321 ARG E C   1 
ATOM   10403 O O   . ARG E 1 321 ? 6.615   1.243   -66.819  1.00 91.46  ? 321 ARG E O   1 
ATOM   10404 C CB  . ARG E 1 321 ? 9.144   1.634   -65.027  1.00 67.11  ? 321 ARG E CB  1 
ATOM   10405 C CG  . ARG E 1 321 ? 10.375  1.372   -64.176  1.00 70.12  ? 321 ARG E CG  1 
ATOM   10406 C CD  . ARG E 1 321 ? 11.038  2.698   -63.816  1.00 75.51  ? 321 ARG E CD  1 
ATOM   10407 N NE  . ARG E 1 321 ? 12.488  2.666   -63.961  1.00 95.13  ? 321 ARG E NE  1 
ATOM   10408 C CZ  . ARG E 1 321 ? 13.343  2.615   -62.949  1.00 92.16  ? 321 ARG E CZ  1 
ATOM   10409 N NH1 . ARG E 1 321 ? 12.928  2.590   -61.693  1.00 92.97  ? 321 ARG E NH1 1 
ATOM   10410 N NH2 . ARG E 1 321 ? 14.648  2.594   -63.203  1.00 88.31  ? 321 ARG E NH2 1 
ATOM   10411 N N   . ASN E 1 322 ? 5.872   1.177   -64.695  1.00 81.15  ? 322 ASN E N   1 
ATOM   10412 C CA  . ASN E 1 322 ? 4.569   1.748   -64.990  1.00 71.44  ? 322 ASN E CA  1 
ATOM   10413 C C   . ASN E 1 322 ? 4.485   3.151   -64.404  1.00 88.30  ? 322 ASN E C   1 
ATOM   10414 O O   . ASN E 1 322 ? 5.144   3.466   -63.409  1.00 97.96  ? 322 ASN E O   1 
ATOM   10415 C CB  . ASN E 1 322 ? 3.441   0.874   -64.433  1.00 70.85  ? 322 ASN E CB  1 
ATOM   10416 C CG  . ASN E 1 322 ? 2.315   0.672   -65.428  1.00 78.09  ? 322 ASN E CG  1 
ATOM   10417 O OD1 . ASN E 1 322 ? 2.516   0.768   -66.638  1.00 77.44  ? 322 ASN E OD1 1 
ATOM   10418 N ND2 . ASN E 1 322 ? 1.121   0.387   -64.921  1.00 86.51  ? 322 ASN E ND2 1 
ATOM   10419 N N   . SER E 1 323 ? 3.676   3.995   -65.034  1.00 98.66  ? 323 SER E N   1 
ATOM   10420 C CA  . SER E 1 323 ? 3.537   5.378   -64.594  1.00 112.69 ? 323 SER E CA  1 
ATOM   10421 C C   . SER E 1 323 ? 2.139   5.915   -64.879  1.00 96.50  ? 323 SER E C   1 
ATOM   10422 O O   . SER E 1 323 ? 1.707   6.895   -64.272  1.00 105.02 ? 323 SER E O   1 
ATOM   10423 C CB  . SER E 1 323 ? 4.589   6.261   -65.269  1.00 117.98 ? 323 SER E CB  1 
ATOM   10424 O OG  . SER E 1 323 ? 4.571   7.574   -64.736  1.00 115.21 ? 323 SER E OG  1 
ATOM   10425 N N   . ILE F 2 6   ? 1.735   12.302  -79.493  1.00 99.32  ? 6   ILE F N   1 
ATOM   10426 C CA  . ILE F 2 6   ? 2.159   11.283  -78.541  1.00 116.40 ? 6   ILE F CA  1 
ATOM   10427 C C   . ILE F 2 6   ? 3.663   11.384  -78.308  1.00 117.46 ? 6   ILE F C   1 
ATOM   10428 O O   . ILE F 2 6   ? 4.452   11.345  -79.253  1.00 110.04 ? 6   ILE F O   1 
ATOM   10429 C CB  . ILE F 2 6   ? 1.766   9.866   -79.016  1.00 102.44 ? 6   ILE F CB  1 
ATOM   10430 C CG1 . ILE F 2 6   ? 0.266   9.620   -78.820  1.00 113.35 ? 6   ILE F CG1 1 
ATOM   10431 C CG2 . ILE F 2 6   ? 2.577   8.808   -78.283  1.00 76.67  ? 6   ILE F CG2 1 
ATOM   10432 C CD1 . ILE F 2 6   ? -0.609  10.151  -79.942  1.00 109.89 ? 6   ILE F CD1 1 
ATOM   10433 N N   . ALA F 2 7   ? 4.051   11.515  -77.043  1.00 125.30 ? 7   ALA F N   1 
ATOM   10434 C CA  . ALA F 2 7   ? 5.452   11.660  -76.673  1.00 98.66  ? 7   ALA F CA  1 
ATOM   10435 C C   . ALA F 2 7   ? 6.129   10.290  -76.676  1.00 100.58 ? 7   ALA F C   1 
ATOM   10436 O O   . ALA F 2 7   ? 5.547   9.279   -77.079  1.00 97.39  ? 7   ALA F O   1 
ATOM   10437 C CB  . ALA F 2 7   ? 5.567   12.360  -75.323  1.00 93.86  ? 7   ALA F CB  1 
ATOM   10438 N N   . GLY F 2 8   ? 7.378   10.241  -76.219  1.00 103.01 ? 8   GLY F N   1 
ATOM   10439 C CA  . GLY F 2 8   ? 8.145   9.011   -76.270  1.00 94.40  ? 8   GLY F CA  1 
ATOM   10440 C C   . GLY F 2 8   ? 8.592   8.476   -74.925  1.00 112.39 ? 8   GLY F C   1 
ATOM   10441 O O   . GLY F 2 8   ? 7.906   8.654   -73.912  1.00 115.86 ? 8   GLY F O   1 
ATOM   10442 N N   . PHE F 2 9   ? 9.755   7.819   -74.906  1.00 106.96 ? 9   PHE F N   1 
ATOM   10443 C CA  . PHE F 2 9   ? 10.183  7.097   -73.711  1.00 95.15  ? 9   PHE F CA  1 
ATOM   10444 C C   . PHE F 2 9   ? 10.640  8.031   -72.600  1.00 96.59  ? 9   PHE F C   1 
ATOM   10445 O O   . PHE F 2 9   ? 10.461  7.715   -71.419  1.00 97.97  ? 9   PHE F O   1 
ATOM   10446 C CB  . PHE F 2 9   ? 11.299  6.113   -74.061  1.00 88.29  ? 9   PHE F CB  1 
ATOM   10447 C CG  . PHE F 2 9   ? 12.614  6.766   -74.421  1.00 99.05  ? 9   PHE F CG  1 
ATOM   10448 C CD1 . PHE F 2 9   ? 13.605  6.934   -73.464  1.00 108.73 ? 9   PHE F CD1 1 
ATOM   10449 C CD2 . PHE F 2 9   ? 12.861  7.200   -75.714  1.00 103.43 ? 9   PHE F CD2 1 
ATOM   10450 C CE1 . PHE F 2 9   ? 14.806  7.527   -73.790  1.00 94.45  ? 9   PHE F CE1 1 
ATOM   10451 C CE2 . PHE F 2 9   ? 14.067  7.797   -76.044  1.00 98.33  ? 9   PHE F CE2 1 
ATOM   10452 C CZ  . PHE F 2 9   ? 15.037  7.959   -75.082  1.00 94.25  ? 9   PHE F CZ  1 
ATOM   10453 N N   . ILE F 2 10  ? 11.244  9.167   -72.952  1.00 94.68  ? 10  ILE F N   1 
ATOM   10454 C CA  . ILE F 2 10  ? 11.748  10.086  -71.933  1.00 104.31 ? 10  ILE F CA  1 
ATOM   10455 C C   . ILE F 2 10  ? 10.616  10.569  -71.036  1.00 109.03 ? 10  ILE F C   1 
ATOM   10456 O O   . ILE F 2 10  ? 10.828  10.862  -69.850  1.00 124.09 ? 10  ILE F O   1 
ATOM   10457 C CB  . ILE F 2 10  ? 12.495  11.265  -72.595  1.00 88.79  ? 10  ILE F CB  1 
ATOM   10458 C CG1 . ILE F 2 10  ? 13.674  10.741  -73.420  1.00 88.22  ? 10  ILE F CG1 1 
ATOM   10459 C CG2 . ILE F 2 10  ? 12.981  12.259  -71.556  1.00 93.59  ? 10  ILE F CG2 1 
ATOM   10460 C CD1 . ILE F 2 10  ? 14.629  11.824  -73.892  1.00 94.19  ? 10  ILE F CD1 1 
ATOM   10461 N N   . GLU F 2 11  ? 9.398   10.625  -71.567  1.00 114.83 ? 11  GLU F N   1 
ATOM   10462 C CA  . GLU F 2 11  ? 8.245   11.074  -70.798  1.00 114.06 ? 11  GLU F CA  1 
ATOM   10463 C C   . GLU F 2 11  ? 7.568   9.934   -70.045  1.00 98.95  ? 11  GLU F C   1 
ATOM   10464 O O   . GLU F 2 11  ? 7.176   10.109  -68.886  1.00 102.62 ? 11  GLU F O   1 
ATOM   10465 C CB  . GLU F 2 11  ? 7.240   11.761  -71.725  1.00 125.95 ? 11  GLU F CB  1 
ATOM   10466 C CG  . GLU F 2 11  ? 7.894   12.716  -72.710  1.00 124.73 ? 11  GLU F CG  1 
ATOM   10467 C CD  . GLU F 2 11  ? 8.608   13.865  -72.028  1.00 129.65 ? 11  GLU F CD  1 
ATOM   10468 O OE1 . GLU F 2 11  ? 7.992   14.510  -71.155  1.00 140.13 ? 11  GLU F OE1 1 
ATOM   10469 O OE2 . GLU F 2 11  ? 9.785   14.118  -72.361  1.00 126.16 ? 11  GLU F OE2 1 
ATOM   10470 N N   . GLY F 2 12  ? 7.427   8.775   -70.669  1.00 104.78 ? 12  GLY F N   1 
ATOM   10471 C CA  . GLY F 2 12  ? 6.800   7.647   -70.011  1.00 79.66  ? 12  GLY F CA  1 
ATOM   10472 C C   . GLY F 2 12  ? 6.388   6.584   -71.006  1.00 99.85  ? 12  GLY F C   1 
ATOM   10473 O O   . GLY F 2 12  ? 6.654   6.678   -72.204  1.00 111.82 ? 12  GLY F O   1 
ATOM   10474 N N   . GLY F 2 13  ? 5.725   5.556   -70.471  1.00 77.28  ? 13  GLY F N   1 
ATOM   10475 C CA  . GLY F 2 13  ? 5.271   4.452   -71.287  1.00 82.70  ? 13  GLY F CA  1 
ATOM   10476 C C   . GLY F 2 13  ? 3.981   4.750   -72.030  1.00 83.08  ? 13  GLY F C   1 
ATOM   10477 O O   . GLY F 2 13  ? 3.255   5.699   -71.732  1.00 71.80  ? 13  GLY F O   1 
ATOM   10478 N N   . TRP F 2 14  ? 3.696   3.903   -73.015  1.00 68.25  ? 14  TRP F N   1 
ATOM   10479 C CA  . TRP F 2 14  ? 2.520   4.035   -73.866  1.00 75.87  ? 14  TRP F CA  1 
ATOM   10480 C C   . TRP F 2 14  ? 1.503   2.970   -73.484  1.00 81.16  ? 14  TRP F C   1 
ATOM   10481 O O   . TRP F 2 14  ? 1.792   1.771   -73.574  1.00 82.28  ? 14  TRP F O   1 
ATOM   10482 C CB  . TRP F 2 14  ? 2.891   3.893   -75.342  1.00 68.04  ? 14  TRP F CB  1 
ATOM   10483 C CG  . TRP F 2 14  ? 3.772   4.976   -75.871  1.00 74.10  ? 14  TRP F CG  1 
ATOM   10484 C CD1 . TRP F 2 14  ? 3.909   6.242   -75.380  1.00 72.67  ? 14  TRP F CD1 1 
ATOM   10485 C CD2 . TRP F 2 14  ? 4.647   4.886   -77.001  1.00 65.88  ? 14  TRP F CD2 1 
ATOM   10486 N NE1 . TRP F 2 14  ? 4.814   6.947   -76.138  1.00 84.98  ? 14  TRP F NE1 1 
ATOM   10487 C CE2 . TRP F 2 14  ? 5.282   6.136   -77.138  1.00 71.20  ? 14  TRP F CE2 1 
ATOM   10488 C CE3 . TRP F 2 14  ? 4.956   3.869   -77.910  1.00 67.20  ? 14  TRP F CE3 1 
ATOM   10489 C CZ2 . TRP F 2 14  ? 6.207   6.396   -78.148  1.00 76.31  ? 14  TRP F CZ2 1 
ATOM   10490 C CZ3 . TRP F 2 14  ? 5.873   4.129   -78.911  1.00 65.37  ? 14  TRP F CZ3 1 
ATOM   10491 C CH2 . TRP F 2 14  ? 6.486   5.383   -79.023  1.00 72.92  ? 14  TRP F CH2 1 
ATOM   10492 N N   . GLN F 2 15  ? 0.313   3.409   -73.067  1.00 81.74  ? 15  GLN F N   1 
ATOM   10493 C CA  . GLN F 2 15  ? -0.793  2.481   -72.876  1.00 81.17  ? 15  GLN F CA  1 
ATOM   10494 C C   . GLN F 2 15  ? -1.329  1.962   -74.203  1.00 87.81  ? 15  GLN F C   1 
ATOM   10495 O O   . GLN F 2 15  ? -2.018  0.936   -74.218  1.00 90.94  ? 15  GLN F O   1 
ATOM   10496 C CB  . GLN F 2 15  ? -1.917  3.150   -72.079  1.00 70.32  ? 15  GLN F CB  1 
ATOM   10497 C CG  . GLN F 2 15  ? -1.508  3.605   -70.681  1.00 84.54  ? 15  GLN F CG  1 
ATOM   10498 C CD  . GLN F 2 15  ? -1.922  2.627   -69.595  1.00 85.39  ? 15  GLN F CD  1 
ATOM   10499 O OE1 . GLN F 2 15  ? -2.802  1.790   -69.801  1.00 90.20  ? 15  GLN F OE1 1 
ATOM   10500 N NE2 . GLN F 2 15  ? -1.289  2.729   -68.430  1.00 90.21  ? 15  GLN F NE2 1 
ATOM   10501 N N   . GLY F 2 16  ? -1.025  2.642   -75.314  1.00 88.89  ? 16  GLY F N   1 
ATOM   10502 C CA  . GLY F 2 16  ? -1.435  2.165   -76.624  1.00 82.33  ? 16  GLY F CA  1 
ATOM   10503 C C   . GLY F 2 16  ? -0.611  1.014   -77.158  1.00 83.89  ? 16  GLY F C   1 
ATOM   10504 O O   . GLY F 2 16  ? -1.088  0.276   -78.026  1.00 81.68  ? 16  GLY F O   1 
ATOM   10505 N N   . MET F 2 17  ? 0.613   0.846   -76.663  1.00 96.34  ? 17  MET F N   1 
ATOM   10506 C CA  . MET F 2 17  ? 1.451   -0.291  -77.032  1.00 96.65  ? 17  MET F CA  1 
ATOM   10507 C C   . MET F 2 17  ? 0.993   -1.495  -76.221  1.00 108.94 ? 17  MET F C   1 
ATOM   10508 O O   . MET F 2 17  ? 1.302   -1.615  -75.032  1.00 105.92 ? 17  MET F O   1 
ATOM   10509 C CB  . MET F 2 17  ? 2.925   0.019   -76.792  1.00 86.99  ? 17  MET F CB  1 
ATOM   10510 C CG  . MET F 2 17  ? 3.855   -1.151  -77.071  1.00 87.58  ? 17  MET F CG  1 
ATOM   10511 S SD  . MET F 2 17  ? 5.313   -0.663  -78.009  1.00 96.38  ? 17  MET F SD  1 
ATOM   10512 C CE  . MET F 2 17  ? 4.559   -0.116  -79.539  1.00 81.20  ? 17  MET F CE  1 
ATOM   10513 N N   . VAL F 2 18  ? 0.250   -2.392  -76.864  1.00 99.07  ? 18  VAL F N   1 
ATOM   10514 C CA  . VAL F 2 18  ? -0.354  -3.528  -76.178  1.00 101.57 ? 18  VAL F CA  1 
ATOM   10515 C C   . VAL F 2 18  ? 0.011   -4.820  -76.896  1.00 100.37 ? 18  VAL F C   1 
ATOM   10516 O O   . VAL F 2 18  ? -0.615  -5.863  -76.676  1.00 111.81 ? 18  VAL F O   1 
ATOM   10517 C CB  . VAL F 2 18  ? -1.882  -3.364  -76.082  1.00 101.66 ? 18  VAL F CB  1 
ATOM   10518 C CG1 . VAL F 2 18  ? -2.233  -2.237  -75.124  1.00 97.89  ? 18  VAL F CG1 1 
ATOM   10519 C CG2 . VAL F 2 18  ? -2.466  -3.094  -77.458  1.00 90.54  ? 18  VAL F CG2 1 
ATOM   10520 N N   . ASP F 2 19  ? 1.028   -4.763  -77.756  1.00 99.34  ? 19  ASP F N   1 
ATOM   10521 C CA  . ASP F 2 19  ? 1.471   -5.931  -78.502  1.00 113.91 ? 19  ASP F CA  1 
ATOM   10522 C C   . ASP F 2 19  ? 2.944   -6.254  -78.291  1.00 112.37 ? 19  ASP F C   1 
ATOM   10523 O O   . ASP F 2 19  ? 3.452   -7.191  -78.917  1.00 118.58 ? 19  ASP F O   1 
ATOM   10524 C CB  . ASP F 2 19  ? 1.202   -5.739  -80.002  1.00 121.54 ? 19  ASP F CB  1 
ATOM   10525 C CG  . ASP F 2 19  ? 1.087   -7.054  -80.749  1.00 134.95 ? 19  ASP F CG  1 
ATOM   10526 O OD1 . ASP F 2 19  ? 0.812   -8.083  -80.096  1.00 134.27 ? 19  ASP F OD1 1 
ATOM   10527 O OD2 . ASP F 2 19  ? 1.276   -7.059  -81.986  1.00 139.53 ? 19  ASP F OD2 1 
ATOM   10528 N N   . GLY F 2 20  ? 3.640   -5.516  -77.434  1.00 103.08 ? 20  GLY F N   1 
ATOM   10529 C CA  . GLY F 2 20  ? 5.048   -5.778  -77.202  1.00 93.61  ? 20  GLY F CA  1 
ATOM   10530 C C   . GLY F 2 20  ? 5.557   -4.954  -76.042  1.00 92.70  ? 20  GLY F C   1 
ATOM   10531 O O   . GLY F 2 20  ? 4.816   -4.190  -75.418  1.00 96.99  ? 20  GLY F O   1 
ATOM   10532 N N   . TRP F 2 21  ? 6.847   -5.128  -75.757  1.00 84.07  ? 21  TRP F N   1 
ATOM   10533 C CA  . TRP F 2 21  ? 7.514   -4.387  -74.693  1.00 80.66  ? 21  TRP F CA  1 
ATOM   10534 C C   . TRP F 2 21  ? 8.074   -3.058  -75.187  1.00 75.48  ? 21  TRP F C   1 
ATOM   10535 O O   . TRP F 2 21  ? 7.874   -2.022  -74.546  1.00 70.56  ? 21  TRP F O   1 
ATOM   10536 C CB  . TRP F 2 21  ? 8.634   -5.236  -74.084  1.00 82.04  ? 21  TRP F CB  1 
ATOM   10537 C CG  . TRP F 2 21  ? 8.183   -6.119  -72.963  1.00 93.43  ? 21  TRP F CG  1 
ATOM   10538 C CD1 . TRP F 2 21  ? 6.908   -6.273  -72.502  1.00 90.67  ? 21  TRP F CD1 1 
ATOM   10539 C CD2 . TRP F 2 21  ? 9.008   -6.963  -72.151  1.00 96.23  ? 21  TRP F CD2 1 
ATOM   10540 N NE1 . TRP F 2 21  ? 6.887   -7.163  -71.456  1.00 89.84  ? 21  TRP F NE1 1 
ATOM   10541 C CE2 . TRP F 2 21  ? 8.164   -7.602  -71.221  1.00 87.74  ? 21  TRP F CE2 1 
ATOM   10542 C CE3 . TRP F 2 21  ? 10.378  -7.243  -72.121  1.00 87.82  ? 21  TRP F CE3 1 
ATOM   10543 C CZ2 . TRP F 2 21  ? 8.644   -8.502  -70.273  1.00 85.97  ? 21  TRP F CZ2 1 
ATOM   10544 C CZ3 . TRP F 2 21  ? 10.852  -8.138  -71.180  1.00 84.48  ? 21  TRP F CZ3 1 
ATOM   10545 C CH2 . TRP F 2 21  ? 9.987   -8.756  -70.269  1.00 88.63  ? 21  TRP F CH2 1 
ATOM   10546 N N   . TYR F 2 22  ? 8.777   -3.072  -76.316  1.00 71.67  ? 22  TYR F N   1 
ATOM   10547 C CA  . TYR F 2 22  ? 9.318   -1.865  -76.922  1.00 71.17  ? 22  TYR F CA  1 
ATOM   10548 C C   . TYR F 2 22  ? 8.798   -1.742  -78.349  1.00 74.40  ? 22  TYR F C   1 
ATOM   10549 O O   . TYR F 2 22  ? 8.553   -2.747  -79.024  1.00 71.90  ? 22  TYR F O   1 
ATOM   10550 C CB  . TYR F 2 22  ? 10.852  -1.874  -76.929  1.00 68.73  ? 22  TYR F CB  1 
ATOM   10551 C CG  . TYR F 2 22  ? 11.476  -2.622  -75.772  1.00 65.89  ? 22  TYR F CG  1 
ATOM   10552 C CD1 . TYR F 2 22  ? 11.515  -2.067  -74.498  1.00 69.91  ? 22  TYR F CD1 1 
ATOM   10553 C CD2 . TYR F 2 22  ? 12.034  -3.881  -75.955  1.00 70.04  ? 22  TYR F CD2 1 
ATOM   10554 C CE1 . TYR F 2 22  ? 12.087  -2.749  -73.440  1.00 66.25  ? 22  TYR F CE1 1 
ATOM   10555 C CE2 . TYR F 2 22  ? 12.608  -4.570  -74.903  1.00 69.15  ? 22  TYR F CE2 1 
ATOM   10556 C CZ  . TYR F 2 22  ? 12.632  -3.999  -73.648  1.00 63.40  ? 22  TYR F CZ  1 
ATOM   10557 O OH  . TYR F 2 22  ? 13.203  -4.679  -72.596  1.00 71.55  ? 22  TYR F OH  1 
ATOM   10558 N N   . GLY F 2 23  ? 8.635   -0.509  -78.808  1.00 68.07  ? 23  GLY F N   1 
ATOM   10559 C CA  . GLY F 2 23  ? 8.114   -0.299  -80.139  1.00 74.08  ? 23  GLY F CA  1 
ATOM   10560 C C   . GLY F 2 23  ? 8.132   1.155   -80.547  1.00 72.66  ? 23  GLY F C   1 
ATOM   10561 O O   . GLY F 2 23  ? 8.834   1.977   -79.955  1.00 63.49  ? 23  GLY F O   1 
ATOM   10562 N N   . TYR F 2 24  ? 7.337   1.461   -81.572  1.00 75.56  ? 24  TYR F N   1 
ATOM   10563 C CA  . TYR F 2 24  ? 7.342   2.770   -82.205  1.00 67.40  ? 24  TYR F CA  1 
ATOM   10564 C C   . TYR F 2 24  ? 5.931   3.338   -82.262  1.00 66.08  ? 24  TYR F C   1 
ATOM   10565 O O   . TYR F 2 24  ? 4.937   2.608   -82.211  1.00 57.19  ? 24  TYR F O   1 
ATOM   10566 C CB  . TYR F 2 24  ? 7.912   2.709   -83.629  1.00 51.98  ? 24  TYR F CB  1 
ATOM   10567 C CG  . TYR F 2 24  ? 9.202   1.937   -83.765  1.00 58.79  ? 24  TYR F CG  1 
ATOM   10568 C CD1 . TYR F 2 24  ? 10.429  2.575   -83.659  1.00 66.01  ? 24  TYR F CD1 1 
ATOM   10569 C CD2 . TYR F 2 24  ? 9.193   0.572   -84.021  1.00 64.81  ? 24  TYR F CD2 1 
ATOM   10570 C CE1 . TYR F 2 24  ? 11.613  1.876   -83.794  1.00 60.96  ? 24  TYR F CE1 1 
ATOM   10571 C CE2 . TYR F 2 24  ? 10.371  -0.137  -84.157  1.00 68.63  ? 24  TYR F CE2 1 
ATOM   10572 C CZ  . TYR F 2 24  ? 11.579  0.521   -84.042  1.00 61.93  ? 24  TYR F CZ  1 
ATOM   10573 O OH  . TYR F 2 24  ? 12.759  -0.175  -84.176  1.00 77.11  ? 24  TYR F OH  1 
ATOM   10574 N N   . HIS F 2 25  ? 5.862   4.664   -82.359  1.00 64.29  ? 25  HIS F N   1 
ATOM   10575 C CA  . HIS F 2 25  ? 4.634   5.382   -82.668  1.00 70.44  ? 25  HIS F CA  1 
ATOM   10576 C C   . HIS F 2 25  ? 4.936   6.408   -83.748  1.00 73.17  ? 25  HIS F C   1 
ATOM   10577 O O   . HIS F 2 25  ? 5.863   7.211   -83.601  1.00 81.96  ? 25  HIS F O   1 
ATOM   10578 C CB  . HIS F 2 25  ? 4.054   6.073   -81.431  1.00 60.19  ? 25  HIS F CB  1 
ATOM   10579 C CG  . HIS F 2 25  ? 2.905   6.982   -81.735  1.00 72.54  ? 25  HIS F CG  1 
ATOM   10580 N ND1 . HIS F 2 25  ? 1.620   6.521   -81.922  1.00 66.67  ? 25  HIS F ND1 1 
ATOM   10581 C CD2 . HIS F 2 25  ? 2.850   8.325   -81.897  1.00 83.81  ? 25  HIS F CD2 1 
ATOM   10582 C CE1 . HIS F 2 25  ? 0.821   7.542   -82.178  1.00 70.51  ? 25  HIS F CE1 1 
ATOM   10583 N NE2 . HIS F 2 25  ? 1.542   8.648   -82.168  1.00 84.74  ? 25  HIS F NE2 1 
ATOM   10584 N N   . HIS F 2 26  ? 4.158   6.382   -84.826  1.00 83.03  ? 26  HIS F N   1 
ATOM   10585 C CA  . HIS F 2 26  ? 4.358   7.281   -85.951  1.00 78.62  ? 26  HIS F CA  1 
ATOM   10586 C C   . HIS F 2 26  ? 3.141   8.180   -86.124  1.00 67.67  ? 26  HIS F C   1 
ATOM   10587 O O   . HIS F 2 26  ? 2.054   7.898   -85.613  1.00 68.47  ? 26  HIS F O   1 
ATOM   10588 C CB  . HIS F 2 26  ? 4.630   6.502   -87.247  1.00 60.20  ? 26  HIS F CB  1 
ATOM   10589 C CG  . HIS F 2 26  ? 3.430   5.792   -87.793  1.00 68.92  ? 26  HIS F CG  1 
ATOM   10590 N ND1 . HIS F 2 26  ? 2.480   6.423   -88.567  1.00 80.85  ? 26  HIS F ND1 1 
ATOM   10591 C CD2 . HIS F 2 26  ? 3.027   4.505   -87.680  1.00 79.68  ? 26  HIS F CD2 1 
ATOM   10592 C CE1 . HIS F 2 26  ? 1.543   5.556   -88.905  1.00 85.75  ? 26  HIS F CE1 1 
ATOM   10593 N NE2 . HIS F 2 26  ? 1.851   4.385   -88.380  1.00 87.16  ? 26  HIS F NE2 1 
ATOM   10594 N N   . SER F 2 27  ? 3.341   9.280   -86.851  1.00 72.30  ? 27  SER F N   1 
ATOM   10595 C CA  . SER F 2 27  ? 2.271   10.247  -87.097  1.00 71.33  ? 27  SER F CA  1 
ATOM   10596 C C   . SER F 2 27  ? 2.572   10.954  -88.415  1.00 69.06  ? 27  SER F C   1 
ATOM   10597 O O   . SER F 2 27  ? 3.423   11.846  -88.460  1.00 71.32  ? 27  SER F O   1 
ATOM   10598 C CB  . SER F 2 27  ? 2.155   11.239  -85.947  1.00 71.25  ? 27  SER F CB  1 
ATOM   10599 O OG  . SER F 2 27  ? 1.364   12.356  -86.315  1.00 74.98  ? 27  SER F OG  1 
ATOM   10600 N N   . ASN F 2 28  ? 1.873   10.553  -89.476  1.00 70.93  ? 28  ASN F N   1 
ATOM   10601 C CA  . ASN F 2 28  ? 1.993   11.224  -90.765  1.00 72.46  ? 28  ASN F CA  1 
ATOM   10602 C C   . ASN F 2 28  ? 0.617   11.626  -91.281  1.00 68.17  ? 28  ASN F C   1 
ATOM   10603 O O   . ASN F 2 28  ? -0.373  11.552  -90.547  1.00 72.91  ? 28  ASN F O   1 
ATOM   10604 C CB  . ASN F 2 28  ? 2.719   10.336  -91.782  1.00 55.12  ? 28  ASN F CB  1 
ATOM   10605 C CG  . ASN F 2 28  ? 2.106   8.954   -91.906  1.00 57.00  ? 28  ASN F CG  1 
ATOM   10606 O OD1 . ASN F 2 28  ? 0.932   8.745   -91.599  1.00 66.71  ? 28  ASN F OD1 1 
ATOM   10607 N ND2 . ASN F 2 28  ? 2.905   7.998   -92.364  1.00 60.62  ? 28  ASN F ND2 1 
ATOM   10608 N N   . GLU F 2 29  ? 0.544   12.056  -92.541  1.00 84.10  ? 29  GLU F N   1 
ATOM   10609 C CA  . GLU F 2 29  ? -0.725  12.486  -93.115  1.00 76.84  ? 29  GLU F CA  1 
ATOM   10610 C C   . GLU F 2 29  ? -1.692  11.339  -93.364  1.00 77.60  ? 29  GLU F C   1 
ATOM   10611 O O   . GLU F 2 29  ? -2.862  11.596  -93.666  1.00 74.93  ? 29  GLU F O   1 
ATOM   10612 C CB  . GLU F 2 29  ? -0.473  13.251  -94.409  1.00 75.29  ? 29  GLU F CB  1 
ATOM   10613 C CG  . GLU F 2 29  ? -0.208  14.719  -94.149  1.00 101.18 ? 29  GLU F CG  1 
ATOM   10614 C CD  . GLU F 2 29  ? 0.597   15.390  -95.238  1.00 107.51 ? 29  GLU F CD  1 
ATOM   10615 O OE1 . GLU F 2 29  ? 0.607   14.884  -96.380  1.00 102.74 ? 29  GLU F OE1 1 
ATOM   10616 O OE2 . GLU F 2 29  ? 1.226   16.431  -94.949  1.00 111.68 ? 29  GLU F OE2 1 
ATOM   10617 N N   . GLN F 2 30  ? -1.241  10.094  -93.251  1.00 83.24  ? 30  GLN F N   1 
ATOM   10618 C CA  . GLN F 2 30  ? -2.122  8.938   -93.331  1.00 67.17  ? 30  GLN F CA  1 
ATOM   10619 C C   . GLN F 2 30  ? -2.689  8.537   -91.975  1.00 74.68  ? 30  GLN F C   1 
ATOM   10620 O O   . GLN F 2 30  ? -3.412  7.539   -91.893  1.00 86.23  ? 30  GLN F O   1 
ATOM   10621 C CB  . GLN F 2 30  ? -1.376  7.752   -93.946  1.00 64.08  ? 30  GLN F CB  1 
ATOM   10622 C CG  . GLN F 2 30  ? -0.984  7.950   -95.397  1.00 52.84  ? 30  GLN F CG  1 
ATOM   10623 C CD  . GLN F 2 30  ? 0.328   7.274   -95.735  1.00 72.09  ? 30  GLN F CD  1 
ATOM   10624 O OE1 . GLN F 2 30  ? 1.394   7.737   -95.333  1.00 73.59  ? 30  GLN F OE1 1 
ATOM   10625 N NE2 . GLN F 2 30  ? 0.257   6.172   -96.472  1.00 66.31  ? 30  GLN F NE2 1 
ATOM   10626 N N   . GLY F 2 31  ? -2.385  9.285   -90.923  1.00 73.20  ? 31  GLY F N   1 
ATOM   10627 C CA  . GLY F 2 31  ? -2.827  8.970   -89.580  1.00 70.09  ? 31  GLY F CA  1 
ATOM   10628 C C   . GLY F 2 31  ? -1.677  8.481   -88.717  1.00 78.88  ? 31  GLY F C   1 
ATOM   10629 O O   . GLY F 2 31  ? -0.524  8.395   -89.144  1.00 79.88  ? 31  GLY F O   1 
ATOM   10630 N N   . SER F 2 32  ? -2.022  8.159   -87.476  1.00 71.40  ? 32  SER F N   1 
ATOM   10631 C CA  . SER F 2 32  ? -1.068  7.690   -86.485  1.00 77.23  ? 32  SER F CA  1 
ATOM   10632 C C   . SER F 2 32  ? -1.287  6.208   -86.205  1.00 77.30  ? 32  SER F C   1 
ATOM   10633 O O   . SER F 2 32  ? -2.238  5.588   -86.689  1.00 84.85  ? 32  SER F O   1 
ATOM   10634 C CB  . SER F 2 32  ? -1.185  8.508   -85.194  1.00 68.09  ? 32  SER F CB  1 
ATOM   10635 O OG  . SER F 2 32  ? -2.521  8.529   -84.722  1.00 87.63  ? 32  SER F OG  1 
ATOM   10636 N N   . GLY F 2 33  ? -0.383  5.642   -85.416  1.00 78.96  ? 33  GLY F N   1 
ATOM   10637 C CA  . GLY F 2 33  ? -0.488  4.242   -85.048  1.00 73.16  ? 33  GLY F CA  1 
ATOM   10638 C C   . GLY F 2 33  ? 0.714   3.817   -84.234  1.00 76.08  ? 33  GLY F C   1 
ATOM   10639 O O   . GLY F 2 33  ? 1.695   4.556   -84.092  1.00 72.29  ? 33  GLY F O   1 
ATOM   10640 N N   . TYR F 2 34  ? 0.621   2.602   -83.701  1.00 69.34  ? 34  TYR F N   1 
ATOM   10641 C CA  . TYR F 2 34  ? 1.683   1.998   -82.912  1.00 61.69  ? 34  TYR F CA  1 
ATOM   10642 C C   . TYR F 2 34  ? 2.207   0.753   -83.615  1.00 56.57  ? 34  TYR F C   1 
ATOM   10643 O O   . TYR F 2 34  ? 1.467   0.062   -84.321  1.00 69.83  ? 34  TYR F O   1 
ATOM   10644 C CB  . TYR F 2 34  ? 1.200   1.623   -81.504  1.00 57.27  ? 34  TYR F CB  1 
ATOM   10645 C CG  . TYR F 2 34  ? 0.918   2.802   -80.599  1.00 59.91  ? 34  TYR F CG  1 
ATOM   10646 C CD1 . TYR F 2 34  ? 1.942   3.423   -79.898  1.00 64.74  ? 34  TYR F CD1 1 
ATOM   10647 C CD2 . TYR F 2 34  ? -0.373  3.284   -80.433  1.00 62.55  ? 34  TYR F CD2 1 
ATOM   10648 C CE1 . TYR F 2 34  ? 1.690   4.497   -79.066  1.00 62.49  ? 34  TYR F CE1 1 
ATOM   10649 C CE2 . TYR F 2 34  ? -0.635  4.357   -79.600  1.00 59.13  ? 34  TYR F CE2 1 
ATOM   10650 C CZ  . TYR F 2 34  ? 0.402   4.960   -78.920  1.00 62.10  ? 34  TYR F CZ  1 
ATOM   10651 O OH  . TYR F 2 34  ? 0.156   6.029   -78.090  1.00 69.79  ? 34  TYR F OH  1 
ATOM   10652 N N   . ALA F 2 35  ? 3.493   0.475   -83.414  1.00 58.98  ? 35  ALA F N   1 
ATOM   10653 C CA  . ALA F 2 35  ? 4.129   -0.706  -83.990  1.00 70.64  ? 35  ALA F CA  1 
ATOM   10654 C C   . ALA F 2 35  ? 5.262   -1.137  -83.073  1.00 82.94  ? 35  ALA F C   1 
ATOM   10655 O O   . ALA F 2 35  ? 6.168   -0.345  -82.795  1.00 80.69  ? 35  ALA F O   1 
ATOM   10656 C CB  . ALA F 2 35  ? 4.652   -0.425  -85.399  1.00 58.32  ? 35  ALA F CB  1 
ATOM   10657 N N   . ALA F 2 36  ? 5.213   -2.383  -82.610  1.00 80.57  ? 36  ALA F N   1 
ATOM   10658 C CA  . ALA F 2 36  ? 6.199   -2.898  -81.674  1.00 91.28  ? 36  ALA F CA  1 
ATOM   10659 C C   . ALA F 2 36  ? 7.360   -3.560  -82.408  1.00 86.11  ? 36  ALA F C   1 
ATOM   10660 O O   . ALA F 2 36  ? 7.204   -4.095  -83.509  1.00 86.64  ? 36  ALA F O   1 
ATOM   10661 C CB  . ALA F 2 36  ? 5.558   -3.896  -80.709  1.00 72.59  ? 36  ALA F CB  1 
ATOM   10662 N N   . ASP F 2 37  ? 8.533   -3.516  -81.780  1.00 83.31  ? 37  ASP F N   1 
ATOM   10663 C CA  . ASP F 2 37  ? 9.729   -4.172  -82.298  1.00 85.80  ? 37  ASP F CA  1 
ATOM   10664 C C   . ASP F 2 37  ? 9.750   -5.604  -81.775  1.00 83.77  ? 37  ASP F C   1 
ATOM   10665 O O   . ASP F 2 37  ? 9.999   -5.836  -80.588  1.00 81.31  ? 37  ASP F O   1 
ATOM   10666 C CB  . ASP F 2 37  ? 10.986  -3.414  -81.879  1.00 75.09  ? 37  ASP F CB  1 
ATOM   10667 C CG  . ASP F 2 37  ? 12.248  -4.005  -82.473  1.00 84.63  ? 37  ASP F CG  1 
ATOM   10668 O OD1 . ASP F 2 37  ? 12.153  -4.668  -83.527  1.00 103.54 ? 37  ASP F OD1 1 
ATOM   10669 O OD2 . ASP F 2 37  ? 13.333  -3.811  -81.884  1.00 94.44  ? 37  ASP F OD2 1 
ATOM   10670 N N   . LYS F 2 38  ? 9.489   -6.565  -82.664  1.00 81.22  ? 38  LYS F N   1 
ATOM   10671 C CA  . LYS F 2 38  ? 9.335   -7.951  -82.235  1.00 83.76  ? 38  LYS F CA  1 
ATOM   10672 C C   . LYS F 2 38  ? 10.643  -8.537  -81.716  1.00 80.84  ? 38  LYS F C   1 
ATOM   10673 O O   . LYS F 2 38  ? 10.649  -9.243  -80.701  1.00 87.36  ? 38  LYS F O   1 
ATOM   10674 C CB  . LYS F 2 38  ? 8.788   -8.797  -83.384  1.00 84.87  ? 38  LYS F CB  1 
ATOM   10675 C CG  . LYS F 2 38  ? 7.376   -8.432  -83.812  1.00 100.99 ? 38  LYS F CG  1 
ATOM   10676 C CD  . LYS F 2 38  ? 6.402   -8.554  -82.652  1.00 117.42 ? 38  LYS F CD  1 
ATOM   10677 C CE  . LYS F 2 38  ? 5.864   -7.195  -82.233  1.00 116.48 ? 38  LYS F CE  1 
ATOM   10678 N NZ  . LYS F 2 38  ? 5.174   -7.254  -80.915  1.00 129.13 ? 38  LYS F NZ  1 
ATOM   10679 N N   . GLU F 2 39  ? 11.759  -8.263  -82.396  1.00 75.15  ? 39  GLU F N   1 
ATOM   10680 C CA  . GLU F 2 39  ? 13.010  -8.939  -82.061  1.00 84.98  ? 39  GLU F CA  1 
ATOM   10681 C C   . GLU F 2 39  ? 13.509  -8.534  -80.679  1.00 86.00  ? 39  GLU F C   1 
ATOM   10682 O O   . GLU F 2 39  ? 13.847  -9.389  -79.854  1.00 80.54  ? 39  GLU F O   1 
ATOM   10683 C CB  . GLU F 2 39  ? 14.071  -8.640  -83.119  1.00 79.02  ? 39  GLU F CB  1 
ATOM   10684 C CG  . GLU F 2 39  ? 15.074  -9.768  -83.307  1.00 98.50  ? 39  GLU F CG  1 
ATOM   10685 C CD  . GLU F 2 39  ? 16.445  -9.274  -83.722  1.00 115.17 ? 39  GLU F CD  1 
ATOM   10686 O OE1 . GLU F 2 39  ? 16.972  -8.359  -83.055  1.00 108.28 ? 39  GLU F OE1 1 
ATOM   10687 O OE2 . GLU F 2 39  ? 16.995  -9.799  -84.715  1.00 116.55 ? 39  GLU F OE2 1 
ATOM   10688 N N   . SER F 2 40  ? 13.572  -7.229  -80.410  1.00 77.25  ? 40  SER F N   1 
ATOM   10689 C CA  . SER F 2 40  ? 14.079  -6.775  -79.119  1.00 73.40  ? 40  SER F CA  1 
ATOM   10690 C C   . SER F 2 40  ? 13.102  -7.082  -77.993  1.00 84.84  ? 40  SER F C   1 
ATOM   10691 O O   . SER F 2 40  ? 13.517  -7.216  -76.836  1.00 83.93  ? 40  SER F O   1 
ATOM   10692 C CB  . SER F 2 40  ? 14.395  -5.279  -79.160  1.00 65.70  ? 40  SER F CB  1 
ATOM   10693 O OG  . SER F 2 40  ? 13.219  -4.516  -79.372  1.00 86.59  ? 40  SER F OG  1 
ATOM   10694 N N   . THR F 2 41  ? 11.807  -7.180  -78.302  1.00 79.88  ? 41  THR F N   1 
ATOM   10695 C CA  . THR F 2 41  ? 10.837  -7.571  -77.286  1.00 81.69  ? 41  THR F CA  1 
ATOM   10696 C C   . THR F 2 41  ? 10.978  -9.046  -76.924  1.00 78.98  ? 41  THR F C   1 
ATOM   10697 O O   . THR F 2 41  ? 10.958  -9.407  -75.740  1.00 76.01  ? 41  THR F O   1 
ATOM   10698 C CB  . THR F 2 41  ? 9.420   -7.276  -77.774  1.00 75.35  ? 41  THR F CB  1 
ATOM   10699 O OG1 . THR F 2 41  ? 9.243   -5.860  -77.899  1.00 84.79  ? 41  THR F OG1 1 
ATOM   10700 C CG2 . THR F 2 41  ? 8.394   -7.831  -76.804  1.00 65.51  ? 41  THR F CG2 1 
ATOM   10701 N N   . GLN F 2 42  ? 11.134  -9.911  -77.927  1.00 73.58  ? 42  GLN F N   1 
ATOM   10702 C CA  . GLN F 2 42  ? 11.205  -11.343 -77.660  1.00 70.40  ? 42  GLN F CA  1 
ATOM   10703 C C   . GLN F 2 42  ? 12.512  -11.719 -76.972  1.00 77.61  ? 42  GLN F C   1 
ATOM   10704 O O   . GLN F 2 42  ? 12.522  -12.569 -76.075  1.00 88.16  ? 42  GLN F O   1 
ATOM   10705 C CB  . GLN F 2 42  ? 11.030  -12.127 -78.960  1.00 68.35  ? 42  GLN F CB  1 
ATOM   10706 C CG  . GLN F 2 42  ? 10.870  -13.629 -78.770  1.00 82.88  ? 42  GLN F CG  1 
ATOM   10707 C CD  . GLN F 2 42  ? 9.618   -14.003 -77.994  1.00 101.23 ? 42  GLN F CD  1 
ATOM   10708 O OE1 . GLN F 2 42  ? 9.555   -15.068 -77.381  1.00 111.40 ? 42  GLN F OE1 1 
ATOM   10709 N NE2 . GLN F 2 42  ? 8.612   -13.135 -78.027  1.00 94.01  ? 42  GLN F NE2 1 
ATOM   10710 N N   . LYS F 2 43  ? 13.625  -11.103 -77.380  1.00 72.79  ? 43  LYS F N   1 
ATOM   10711 C CA  . LYS F 2 43  ? 14.901  -11.396 -76.735  1.00 76.09  ? 43  LYS F CA  1 
ATOM   10712 C C   . LYS F 2 43  ? 14.924  -10.897 -75.295  1.00 73.80  ? 43  LYS F C   1 
ATOM   10713 O O   . LYS F 2 43  ? 15.489  -11.557 -74.415  1.00 69.85  ? 43  LYS F O   1 
ATOM   10714 C CB  . LYS F 2 43  ? 16.050  -10.797 -77.547  1.00 71.91  ? 43  LYS F CB  1 
ATOM   10715 C CG  . LYS F 2 43  ? 16.586  -11.758 -78.597  1.00 97.18  ? 43  LYS F CG  1 
ATOM   10716 C CD  . LYS F 2 43  ? 17.372  -11.059 -79.690  1.00 94.21  ? 43  LYS F CD  1 
ATOM   10717 C CE  . LYS F 2 43  ? 17.737  -12.047 -80.789  1.00 108.25 ? 43  LYS F CE  1 
ATOM   10718 N NZ  . LYS F 2 43  ? 18.504  -11.417 -81.897  1.00 102.27 ? 43  LYS F NZ  1 
ATOM   10719 N N   . ALA F 2 44  ? 14.318  -9.736  -75.034  1.00 62.28  ? 44  ALA F N   1 
ATOM   10720 C CA  . ALA F 2 44  ? 14.223  -9.248  -73.662  1.00 64.04  ? 44  ALA F CA  1 
ATOM   10721 C C   . ALA F 2 44  ? 13.366  -10.173 -72.806  1.00 78.04  ? 44  ALA F C   1 
ATOM   10722 O O   . ALA F 2 44  ? 13.701  -10.446 -71.647  1.00 77.42  ? 44  ALA F O   1 
ATOM   10723 C CB  . ALA F 2 44  ? 13.660  -7.827  -73.645  1.00 61.03  ? 44  ALA F CB  1 
ATOM   10724 N N   . ILE F 2 45  ? 12.257  -10.665 -73.360  1.00 76.37  ? 45  ILE F N   1 
ATOM   10725 C CA  . ILE F 2 45  ? 11.390  -11.580 -72.621  1.00 75.34  ? 45  ILE F CA  1 
ATOM   10726 C C   . ILE F 2 45  ? 12.127  -12.876 -72.304  1.00 71.43  ? 45  ILE F C   1 
ATOM   10727 O O   . ILE F 2 45  ? 11.983  -13.437 -71.210  1.00 75.10  ? 45  ILE F O   1 
ATOM   10728 C CB  . ILE F 2 45  ? 10.090  -11.827 -73.409  1.00 70.07  ? 45  ILE F CB  1 
ATOM   10729 C CG1 . ILE F 2 45  ? 9.077   -10.723 -73.097  1.00 75.84  ? 45  ILE F CG1 1 
ATOM   10730 C CG2 . ILE F 2 45  ? 9.516   -13.211 -73.114  1.00 67.32  ? 45  ILE F CG2 1 
ATOM   10731 C CD1 . ILE F 2 45  ? 8.042   -10.507 -74.178  1.00 77.13  ? 45  ILE F CD1 1 
ATOM   10732 N N   . ASP F 2 46  ? 12.933  -13.365 -73.248  1.00 61.72  ? 46  ASP F N   1 
ATOM   10733 C CA  . ASP F 2 46  ? 13.733  -14.559 -72.993  1.00 74.77  ? 46  ASP F CA  1 
ATOM   10734 C C   . ASP F 2 46  ? 14.727  -14.327 -71.861  1.00 76.06  ? 46  ASP F C   1 
ATOM   10735 O O   . ASP F 2 46  ? 14.917  -15.198 -71.003  1.00 78.88  ? 46  ASP F O   1 
ATOM   10736 C CB  . ASP F 2 46  ? 14.466  -14.982 -74.267  1.00 64.09  ? 46  ASP F CB  1 
ATOM   10737 C CG  . ASP F 2 46  ? 13.520  -15.425 -75.366  1.00 92.36  ? 46  ASP F CG  1 
ATOM   10738 O OD1 . ASP F 2 46  ? 12.303  -15.532 -75.103  1.00 94.90  ? 46  ASP F OD1 1 
ATOM   10739 O OD2 . ASP F 2 46  ? 13.996  -15.666 -76.497  1.00 96.87  ? 46  ASP F OD2 1 
ATOM   10740 N N   . GLY F 2 47  ? 15.375  -13.161 -71.845  1.00 74.32  ? 47  GLY F N   1 
ATOM   10741 C CA  . GLY F 2 47  ? 16.359  -12.885 -70.809  1.00 72.68  ? 47  GLY F CA  1 
ATOM   10742 C C   . GLY F 2 47  ? 15.750  -12.789 -69.423  1.00 77.26  ? 47  GLY F C   1 
ATOM   10743 O O   . GLY F 2 47  ? 16.292  -13.337 -68.459  1.00 75.10  ? 47  GLY F O   1 
ATOM   10744 N N   . VAL F 2 48  ? 14.619  -12.090 -69.301  1.00 78.41  ? 48  VAL F N   1 
ATOM   10745 C CA  . VAL F 2 48  ? 13.947  -11.986 -68.009  1.00 68.58  ? 48  VAL F CA  1 
ATOM   10746 C C   . VAL F 2 48  ? 13.428  -13.349 -67.566  1.00 79.83  ? 48  VAL F C   1 
ATOM   10747 O O   . VAL F 2 48  ? 13.501  -13.701 -66.382  1.00 79.32  ? 48  VAL F O   1 
ATOM   10748 C CB  . VAL F 2 48  ? 12.821  -10.939 -68.072  1.00 64.66  ? 48  VAL F CB  1 
ATOM   10749 C CG1 . VAL F 2 48  ? 12.145  -10.804 -66.716  1.00 68.17  ? 48  VAL F CG1 1 
ATOM   10750 C CG2 . VAL F 2 48  ? 13.371  -9.596  -68.530  1.00 81.95  ? 48  VAL F CG2 1 
ATOM   10751 N N   . THR F 2 49  ? 12.893  -14.134 -68.506  1.00 79.75  ? 49  THR F N   1 
ATOM   10752 C CA  . THR F 2 49  ? 12.425  -15.479 -68.179  1.00 72.64  ? 49  THR F CA  1 
ATOM   10753 C C   . THR F 2 49  ? 13.562  -16.344 -67.648  1.00 70.45  ? 49  THR F C   1 
ATOM   10754 O O   . THR F 2 49  ? 13.396  -17.058 -66.652  1.00 81.62  ? 49  THR F O   1 
ATOM   10755 C CB  . THR F 2 49  ? 11.787  -16.122 -69.413  1.00 75.01  ? 49  THR F CB  1 
ATOM   10756 O OG1 . THR F 2 49  ? 10.444  -15.644 -69.564  1.00 76.95  ? 49  THR F OG1 1 
ATOM   10757 C CG2 . THR F 2 49  ? 11.778  -17.643 -69.301  1.00 76.90  ? 49  THR F CG2 1 
ATOM   10758 N N   . ASN F 2 50  ? 14.729  -16.282 -68.293  1.00 66.99  ? 50  ASN F N   1 
ATOM   10759 C CA  . ASN F 2 50  ? 15.879  -17.047 -67.824  1.00 69.82  ? 50  ASN F CA  1 
ATOM   10760 C C   . ASN F 2 50  ? 16.332  -16.581 -66.445  1.00 71.20  ? 50  ASN F C   1 
ATOM   10761 O O   . ASN F 2 50  ? 16.692  -17.402 -65.594  1.00 67.54  ? 50  ASN F O   1 
ATOM   10762 C CB  . ASN F 2 50  ? 17.023  -16.944 -68.833  1.00 72.28  ? 50  ASN F CB  1 
ATOM   10763 C CG  . ASN F 2 50  ? 16.737  -17.699 -70.116  1.00 92.13  ? 50  ASN F CG  1 
ATOM   10764 O OD1 . ASN F 2 50  ? 15.614  -18.146 -70.350  1.00 101.72 ? 50  ASN F OD1 1 
ATOM   10765 N ND2 . ASN F 2 50  ? 17.755  -17.844 -70.957  1.00 85.71  ? 50  ASN F ND2 1 
ATOM   10766 N N   . LYS F 2 51  ? 16.326  -15.266 -66.208  1.00 68.17  ? 51  LYS F N   1 
ATOM   10767 C CA  . LYS F 2 51  ? 16.750  -14.744 -64.911  1.00 58.73  ? 51  LYS F CA  1 
ATOM   10768 C C   . LYS F 2 51  ? 15.842  -15.241 -63.792  1.00 60.13  ? 51  LYS F C   1 
ATOM   10769 O O   . LYS F 2 51  ? 16.318  -15.676 -62.737  1.00 79.56  ? 51  LYS F O   1 
ATOM   10770 C CB  . LYS F 2 51  ? 16.774  -13.215 -64.938  1.00 57.36  ? 51  LYS F CB  1 
ATOM   10771 C CG  . LYS F 2 51  ? 17.065  -12.599 -63.580  1.00 59.36  ? 51  LYS F CG  1 
ATOM   10772 C CD  . LYS F 2 51  ? 16.754  -11.112 -63.534  1.00 65.64  ? 51  LYS F CD  1 
ATOM   10773 C CE  . LYS F 2 51  ? 17.685  -10.311 -64.426  1.00 77.17  ? 51  LYS F CE  1 
ATOM   10774 N NZ  . LYS F 2 51  ? 17.755  -8.891  -63.982  1.00 70.82  ? 51  LYS F NZ  1 
ATOM   10775 N N   . VAL F 2 52  ? 14.526  -15.179 -64.005  1.00 63.30  ? 52  VAL F N   1 
ATOM   10776 C CA  . VAL F 2 52  ? 13.584  -15.660 -62.997  1.00 71.92  ? 52  VAL F CA  1 
ATOM   10777 C C   . VAL F 2 52  ? 13.750  -17.159 -62.784  1.00 73.28  ? 52  VAL F C   1 
ATOM   10778 O O   . VAL F 2 52  ? 13.768  -17.642 -61.644  1.00 75.53  ? 52  VAL F O   1 
ATOM   10779 C CB  . VAL F 2 52  ? 12.141  -15.295 -63.396  1.00 60.18  ? 52  VAL F CB  1 
ATOM   10780 C CG1 . VAL F 2 52  ? 11.146  -16.276 -62.792  1.00 69.23  ? 52  VAL F CG1 1 
ATOM   10781 C CG2 . VAL F 2 52  ? 11.814  -13.876 -62.957  1.00 58.60  ? 52  VAL F CG2 1 
ATOM   10782 N N   . ASN F 2 53  ? 13.885  -17.919 -63.874  1.00 62.29  ? 53  ASN F N   1 
ATOM   10783 C CA  . ASN F 2 53  ? 14.048  -19.363 -63.751  1.00 68.28  ? 53  ASN F CA  1 
ATOM   10784 C C   . ASN F 2 53  ? 15.360  -19.722 -63.061  1.00 70.07  ? 53  ASN F C   1 
ATOM   10785 O O   . ASN F 2 53  ? 15.416  -20.692 -62.299  1.00 76.04  ? 53  ASN F O   1 
ATOM   10786 C CB  . ASN F 2 53  ? 13.963  -20.023 -65.127  1.00 61.85  ? 53  ASN F CB  1 
ATOM   10787 C CG  . ASN F 2 53  ? 12.559  -19.984 -65.708  1.00 79.54  ? 53  ASN F CG  1 
ATOM   10788 O OD1 . ASN F 2 53  ? 11.575  -19.877 -64.974  1.00 71.82  ? 53  ASN F OD1 1 
ATOM   10789 N ND2 . ASN F 2 53  ? 12.460  -20.077 -67.029  1.00 80.11  ? 53  ASN F ND2 1 
ATOM   10790 N N   . SER F 2 54  ? 16.427  -18.959 -63.316  1.00 68.99  ? 54  SER F N   1 
ATOM   10791 C CA  . SER F 2 54  ? 17.703  -19.239 -62.665  1.00 60.90  ? 54  SER F CA  1 
ATOM   10792 C C   . SER F 2 54  ? 17.608  -19.055 -61.155  1.00 73.62  ? 54  SER F C   1 
ATOM   10793 O O   . SER F 2 54  ? 18.129  -19.872 -60.387  1.00 76.71  ? 54  SER F O   1 
ATOM   10794 C CB  . SER F 2 54  ? 18.801  -18.343 -63.241  1.00 64.10  ? 54  SER F CB  1 
ATOM   10795 O OG  . SER F 2 54  ? 19.163  -18.746 -64.550  1.00 81.04  ? 54  SER F OG  1 
ATOM   10796 N N   . ILE F 2 55  ? 16.942  -17.988 -60.709  1.00 61.89  ? 55  ILE F N   1 
ATOM   10797 C CA  . ILE F 2 55  ? 16.810  -17.729 -59.278  1.00 62.19  ? 55  ILE F CA  1 
ATOM   10798 C C   . ILE F 2 55  ? 16.040  -18.851 -58.592  1.00 67.47  ? 55  ILE F C   1 
ATOM   10799 O O   . ILE F 2 55  ? 16.311  -19.184 -57.431  1.00 79.03  ? 55  ILE F O   1 
ATOM   10800 C CB  . ILE F 2 55  ? 16.156  -16.348 -59.061  1.00 60.32  ? 55  ILE F CB  1 
ATOM   10801 C CG1 . ILE F 2 55  ? 17.219  -15.247 -59.131  1.00 67.79  ? 55  ILE F CG1 1 
ATOM   10802 C CG2 . ILE F 2 55  ? 15.387  -16.288 -57.744  1.00 53.65  ? 55  ILE F CG2 1 
ATOM   10803 C CD1 . ILE F 2 55  ? 16.718  -13.941 -59.708  1.00 66.85  ? 55  ILE F CD1 1 
ATOM   10804 N N   . ILE F 2 56  ? 15.100  -19.471 -59.297  1.00 73.77  ? 56  ILE F N   1 
ATOM   10805 C CA  . ILE F 2 56  ? 14.272  -20.523 -58.717  1.00 67.91  ? 56  ILE F CA  1 
ATOM   10806 C C   . ILE F 2 56  ? 14.918  -21.896 -58.866  1.00 69.38  ? 56  ILE F C   1 
ATOM   10807 O O   . ILE F 2 56  ? 14.988  -22.667 -57.906  1.00 77.07  ? 56  ILE F O   1 
ATOM   10808 C CB  . ILE F 2 56  ? 12.867  -20.490 -59.357  1.00 56.26  ? 56  ILE F CB  1 
ATOM   10809 C CG1 . ILE F 2 56  ? 12.198  -19.138 -59.096  1.00 60.74  ? 56  ILE F CG1 1 
ATOM   10810 C CG2 . ILE F 2 56  ? 12.009  -21.627 -58.828  1.00 57.22  ? 56  ILE F CG2 1 
ATOM   10811 C CD1 . ILE F 2 56  ? 10.835  -18.996 -59.738  1.00 64.47  ? 56  ILE F CD1 1 
ATOM   10812 N N   . ASP F 2 57  ? 15.405  -22.225 -60.066  1.00 68.91  ? 57  ASP F N   1 
ATOM   10813 C CA  . ASP F 2 57  ? 15.858  -23.582 -60.354  1.00 74.10  ? 57  ASP F CA  1 
ATOM   10814 C C   . ASP F 2 57  ? 17.216  -23.915 -59.749  1.00 71.16  ? 57  ASP F C   1 
ATOM   10815 O O   . ASP F 2 57  ? 17.498  -25.095 -59.513  1.00 87.49  ? 57  ASP F O   1 
ATOM   10816 C CB  . ASP F 2 57  ? 15.910  -23.811 -61.867  1.00 86.70  ? 57  ASP F CB  1 
ATOM   10817 C CG  . ASP F 2 57  ? 14.566  -23.600 -62.536  1.00 97.65  ? 57  ASP F CG  1 
ATOM   10818 O OD1 . ASP F 2 57  ? 13.532  -23.690 -61.840  1.00 99.53  ? 57  ASP F OD1 1 
ATOM   10819 O OD2 . ASP F 2 57  ? 14.544  -23.347 -63.760  1.00 99.40  ? 57  ASP F OD2 1 
ATOM   10820 N N   . LYS F 2 58  ? 18.061  -22.920 -59.494  1.00 68.79  ? 58  LYS F N   1 
ATOM   10821 C CA  . LYS F 2 58  ? 19.403  -23.183 -58.989  1.00 69.26  ? 58  LYS F CA  1 
ATOM   10822 C C   . LYS F 2 58  ? 19.430  -23.494 -57.498  1.00 75.09  ? 58  LYS F C   1 
ATOM   10823 O O   . LYS F 2 58  ? 20.502  -23.810 -56.968  1.00 72.73  ? 58  LYS F O   1 
ATOM   10824 C CB  . LYS F 2 58  ? 20.317  -21.996 -59.300  1.00 66.38  ? 58  LYS F CB  1 
ATOM   10825 C CG  . LYS F 2 58  ? 20.574  -21.807 -60.789  1.00 78.69  ? 58  LYS F CG  1 
ATOM   10826 C CD  . LYS F 2 58  ? 21.972  -22.258 -61.172  1.00 80.07  ? 58  LYS F CD  1 
ATOM   10827 C CE  . LYS F 2 58  ? 22.067  -22.609 -62.647  1.00 91.38  ? 58  LYS F CE  1 
ATOM   10828 N NZ  . LYS F 2 58  ? 21.742  -24.043 -62.884  1.00 91.50  ? 58  LYS F NZ  1 
ATOM   10829 N N   . MET F 2 59  ? 18.291  -23.415 -56.813  1.00 80.99  ? 59  MET F N   1 
ATOM   10830 C CA  . MET F 2 59  ? 18.215  -23.796 -55.410  1.00 67.43  ? 59  MET F CA  1 
ATOM   10831 C C   . MET F 2 59  ? 18.210  -25.314 -55.281  1.00 68.61  ? 59  MET F C   1 
ATOM   10832 O O   . MET F 2 59  ? 17.467  -26.006 -55.985  1.00 71.10  ? 59  MET F O   1 
ATOM   10833 C CB  . MET F 2 59  ? 16.962  -23.206 -54.761  1.00 63.52  ? 59  MET F CB  1 
ATOM   10834 C CG  . MET F 2 59  ? 16.752  -23.634 -53.318  1.00 61.05  ? 59  MET F CG  1 
ATOM   10835 S SD  . MET F 2 59  ? 17.932  -22.887 -52.178  1.00 74.75  ? 59  MET F SD  1 
ATOM   10836 C CE  . MET F 2 59  ? 17.392  -21.179 -52.209  1.00 66.43  ? 59  MET F CE  1 
ATOM   10837 N N   . ASN F 2 60  ? 19.041  -25.831 -54.381  1.00 77.46  ? 60  ASN F N   1 
ATOM   10838 C CA  . ASN F 2 60  ? 19.098  -27.258 -54.098  1.00 69.83  ? 60  ASN F CA  1 
ATOM   10839 C C   . ASN F 2 60  ? 18.383  -27.542 -52.784  1.00 71.70  ? 60  ASN F C   1 
ATOM   10840 O O   . ASN F 2 60  ? 18.709  -26.946 -51.751  1.00 70.64  ? 60  ASN F O   1 
ATOM   10841 C CB  . ASN F 2 60  ? 20.545  -27.748 -54.034  1.00 66.84  ? 60  ASN F CB  1 
ATOM   10842 C CG  . ASN F 2 60  ? 20.644  -29.243 -53.786  1.00 84.40  ? 60  ASN F CG  1 
ATOM   10843 O OD1 . ASN F 2 60  ? 20.342  -30.050 -54.665  1.00 90.56  ? 60  ASN F OD1 1 
ATOM   10844 N ND2 . ASN F 2 60  ? 21.080  -29.618 -52.588  1.00 87.28  ? 60  ASN F ND2 1 
ATOM   10845 N N   . THR F 2 61  ? 17.402  -28.442 -52.830  1.00 76.59  ? 61  THR F N   1 
ATOM   10846 C CA  . THR F 2 61  ? 16.649  -28.844 -51.652  1.00 88.04  ? 61  THR F CA  1 
ATOM   10847 C C   . THR F 2 61  ? 16.676  -30.360 -51.533  1.00 69.98  ? 61  THR F C   1 
ATOM   10848 O O   . THR F 2 61  ? 16.558  -31.070 -52.536  1.00 75.96  ? 61  THR F O   1 
ATOM   10849 C CB  . THR F 2 61  ? 15.190  -28.366 -51.710  1.00 86.08  ? 61  THR F CB  1 
ATOM   10850 O OG1 . THR F 2 61  ? 14.411  -29.310 -52.454  1.00 86.38  ? 61  THR F OG1 1 
ATOM   10851 C CG2 . THR F 2 61  ? 15.093  -27.004 -52.380  1.00 77.15  ? 61  THR F CG2 1 
ATOM   10852 N N   . GLN F 2 62  ? 16.840  -30.851 -50.306  1.00 73.61  ? 62  GLN F N   1 
ATOM   10853 C CA  . GLN F 2 62  ? 16.809  -32.279 -50.018  1.00 68.03  ? 62  GLN F CA  1 
ATOM   10854 C C   . GLN F 2 62  ? 15.857  -32.532 -48.856  1.00 64.24  ? 62  GLN F C   1 
ATOM   10855 O O   . GLN F 2 62  ? 15.314  -31.602 -48.249  1.00 76.38  ? 62  GLN F O   1 
ATOM   10856 C CB  . GLN F 2 62  ? 18.206  -32.836 -49.709  1.00 67.10  ? 62  GLN F CB  1 
ATOM   10857 C CG  . GLN F 2 62  ? 18.924  -32.186 -48.535  1.00 72.92  ? 62  GLN F CG  1 
ATOM   10858 C CD  . GLN F 2 62  ? 19.627  -30.904 -48.931  1.00 75.06  ? 62  GLN F CD  1 
ATOM   10859 O OE1 . GLN F 2 62  ? 18.993  -29.873 -49.156  1.00 79.92  ? 62  GLN F OE1 1 
ATOM   10860 N NE2 . GLN F 2 62  ? 20.945  -30.969 -49.042  1.00 68.12  ? 62  GLN F NE2 1 
ATOM   10861 N N   . PHE F 2 63  ? 15.646  -33.810 -48.554  1.00 56.75  ? 63  PHE F N   1 
ATOM   10862 C CA  . PHE F 2 63  ? 14.774  -34.184 -47.450  1.00 69.60  ? 63  PHE F CA  1 
ATOM   10863 C C   . PHE F 2 63  ? 15.417  -33.814 -46.120  1.00 65.91  ? 63  PHE F C   1 
ATOM   10864 O O   . PHE F 2 63  ? 16.577  -34.149 -45.862  1.00 65.28  ? 63  PHE F O   1 
ATOM   10865 C CB  . PHE F 2 63  ? 14.474  -35.684 -47.493  1.00 63.36  ? 63  PHE F CB  1 
ATOM   10866 C CG  . PHE F 2 63  ? 13.591  -36.161 -46.369  1.00 74.95  ? 63  PHE F CG  1 
ATOM   10867 C CD1 . PHE F 2 63  ? 14.137  -36.577 -45.164  1.00 57.66  ? 63  PHE F CD1 1 
ATOM   10868 C CD2 . PHE F 2 63  ? 12.215  -36.199 -46.523  1.00 74.09  ? 63  PHE F CD2 1 
ATOM   10869 C CE1 . PHE F 2 63  ? 13.328  -37.011 -44.133  1.00 64.62  ? 63  PHE F CE1 1 
ATOM   10870 C CE2 . PHE F 2 63  ? 11.402  -36.633 -45.496  1.00 70.21  ? 63  PHE F CE2 1 
ATOM   10871 C CZ  . PHE F 2 63  ? 11.958  -37.040 -44.301  1.00 73.73  ? 63  PHE F CZ  1 
ATOM   10872 N N   . GLU F 2 64  ? 14.658  -33.123 -45.273  1.00 62.04  ? 64  GLU F N   1 
ATOM   10873 C CA  . GLU F 2 64  ? 15.093  -32.816 -43.918  1.00 67.54  ? 64  GLU F CA  1 
ATOM   10874 C C   . GLU F 2 64  ? 13.917  -32.980 -42.968  1.00 76.20  ? 64  GLU F C   1 
ATOM   10875 O O   . GLU F 2 64  ? 12.807  -32.525 -43.258  1.00 59.35  ? 64  GLU F O   1 
ATOM   10876 C CB  . GLU F 2 64  ? 15.659  -31.392 -43.800  1.00 59.18  ? 64  GLU F CB  1 
ATOM   10877 C CG  . GLU F 2 64  ? 16.890  -31.116 -44.656  1.00 68.84  ? 64  GLU F CG  1 
ATOM   10878 C CD  . GLU F 2 64  ? 18.102  -31.939 -44.249  1.00 75.87  ? 64  GLU F CD  1 
ATOM   10879 O OE1 . GLU F 2 64  ? 18.094  -32.539 -43.153  1.00 87.10  ? 64  GLU F OE1 1 
ATOM   10880 O OE2 . GLU F 2 64  ? 19.072  -31.981 -45.033  1.00 75.29  ? 64  GLU F OE2 1 
ATOM   10881 N N   . ALA F 2 65  ? 14.168  -33.636 -41.839  1.00 81.72  ? 65  ALA F N   1 
ATOM   10882 C CA  . ALA F 2 65  ? 13.182  -33.793 -40.774  1.00 54.94  ? 65  ALA F CA  1 
ATOM   10883 C C   . ALA F 2 65  ? 13.614  -32.906 -39.613  1.00 59.50  ? 65  ALA F C   1 
ATOM   10884 O O   . ALA F 2 65  ? 14.602  -33.203 -38.933  1.00 74.39  ? 65  ALA F O   1 
ATOM   10885 C CB  . ALA F 2 65  ? 13.060  -35.252 -40.345  1.00 57.77  ? 65  ALA F CB  1 
ATOM   10886 N N   . VAL F 2 66  ? 12.876  -31.823 -39.390  1.00 57.43  ? 66  VAL F N   1 
ATOM   10887 C CA  . VAL F 2 66  ? 13.215  -30.823 -38.384  1.00 66.44  ? 66  VAL F CA  1 
ATOM   10888 C C   . VAL F 2 66  ? 12.257  -30.980 -37.212  1.00 69.17  ? 66  VAL F C   1 
ATOM   10889 O O   . VAL F 2 66  ? 11.044  -30.785 -37.361  1.00 71.95  ? 66  VAL F O   1 
ATOM   10890 C CB  . VAL F 2 66  ? 13.156  -29.400 -38.961  1.00 67.86  ? 66  VAL F CB  1 
ATOM   10891 C CG1 . VAL F 2 66  ? 13.413  -28.379 -37.870  1.00 61.31  ? 66  VAL F CG1 1 
ATOM   10892 C CG2 . VAL F 2 66  ? 14.164  -29.247 -40.090  1.00 55.26  ? 66  VAL F CG2 1 
ATOM   10893 N N   . GLY F 2 67  ? 12.802  -31.325 -36.048  1.00 88.46  ? 67  GLY F N   1 
ATOM   10894 C CA  . GLY F 2 67  ? 11.998  -31.512 -34.856  1.00 57.99  ? 67  GLY F CA  1 
ATOM   10895 C C   . GLY F 2 67  ? 12.694  -31.065 -33.586  1.00 75.55  ? 67  GLY F C   1 
ATOM   10896 O O   . GLY F 2 67  ? 13.623  -30.253 -33.629  1.00 81.43  ? 67  GLY F O   1 
ATOM   10897 N N   . ARG F 2 68  ? 12.246  -31.592 -32.443  1.00 63.96  ? 68  ARG F N   1 
ATOM   10898 C CA  . ARG F 2 68  ? 12.803  -31.263 -31.126  1.00 57.07  ? 68  ARG F CA  1 
ATOM   10899 C C   . ARG F 2 68  ? 12.863  -32.570 -30.336  1.00 67.50  ? 68  ARG F C   1 
ATOM   10900 O O   . ARG F 2 68  ? 11.880  -32.968 -29.704  1.00 74.06  ? 68  ARG F O   1 
ATOM   10901 C CB  . ARG F 2 68  ? 11.959  -30.212 -30.413  1.00 55.28  ? 68  ARG F CB  1 
ATOM   10902 C CG  . ARG F 2 68  ? 11.810  -28.886 -31.152  1.00 52.84  ? 68  ARG F CG  1 
ATOM   10903 C CD  . ARG F 2 68  ? 12.946  -27.929 -30.827  1.00 74.23  ? 68  ARG F CD  1 
ATOM   10904 N NE  . ARG F 2 68  ? 12.846  -26.686 -31.584  1.00 74.59  ? 68  ARG F NE  1 
ATOM   10905 C CZ  . ARG F 2 68  ? 13.436  -26.472 -32.752  1.00 84.79  ? 68  ARG F CZ  1 
ATOM   10906 N NH1 . ARG F 2 68  ? 14.183  -27.400 -33.329  1.00 82.70  ? 68  ARG F NH1 1 
ATOM   10907 N NH2 . ARG F 2 68  ? 13.275  -25.298 -33.355  1.00 91.44  ? 68  ARG F NH2 1 
ATOM   10908 N N   . GLU F 2 69  ? 14.019  -33.234 -30.370  1.00 67.09  ? 69  GLU F N   1 
ATOM   10909 C CA  . GLU F 2 69  ? 14.156  -34.573 -29.808  1.00 62.37  ? 69  GLU F CA  1 
ATOM   10910 C C   . GLU F 2 69  ? 15.159  -34.622 -28.658  1.00 67.58  ? 69  GLU F C   1 
ATOM   10911 O O   . GLU F 2 69  ? 15.790  -35.655 -28.425  1.00 59.77  ? 69  GLU F O   1 
ATOM   10912 C CB  . GLU F 2 69  ? 14.553  -35.573 -30.895  1.00 75.50  ? 69  GLU F CB  1 
ATOM   10913 C CG  . GLU F 2 69  ? 13.803  -35.407 -32.206  1.00 87.30  ? 69  GLU F CG  1 
ATOM   10914 C CD  . GLU F 2 69  ? 13.981  -36.597 -33.129  1.00 99.98  ? 69  GLU F CD  1 
ATOM   10915 O OE1 . GLU F 2 69  ? 13.561  -37.710 -32.747  1.00 91.73  ? 69  GLU F OE1 1 
ATOM   10916 O OE2 . GLU F 2 69  ? 14.547  -36.421 -34.230  1.00 84.38  ? 69  GLU F OE2 1 
ATOM   10917 N N   . PHE F 2 70  ? 15.317  -33.524 -27.926  1.00 72.75  ? 70  PHE F N   1 
ATOM   10918 C CA  . PHE F 2 70  ? 16.252  -33.461 -26.811  1.00 67.87  ? 70  PHE F CA  1 
ATOM   10919 C C   . PHE F 2 70  ? 15.504  -33.144 -25.523  1.00 56.81  ? 70  PHE F C   1 
ATOM   10920 O O   . PHE F 2 70  ? 14.646  -32.257 -25.496  1.00 70.89  ? 70  PHE F O   1 
ATOM   10921 C CB  . PHE F 2 70  ? 17.346  -32.420 -27.071  1.00 69.27  ? 70  PHE F CB  1 
ATOM   10922 C CG  . PHE F 2 70  ? 18.151  -32.692 -28.311  1.00 61.09  ? 70  PHE F CG  1 
ATOM   10923 C CD1 . PHE F 2 70  ? 19.036  -33.758 -28.358  1.00 63.19  ? 70  PHE F CD1 1 
ATOM   10924 C CD2 . PHE F 2 70  ? 18.018  -31.889 -29.430  1.00 62.68  ? 70  PHE F CD2 1 
ATOM   10925 C CE1 . PHE F 2 70  ? 19.773  -34.017 -29.500  1.00 64.45  ? 70  PHE F CE1 1 
ATOM   10926 C CE2 . PHE F 2 70  ? 18.755  -32.141 -30.573  1.00 61.94  ? 70  PHE F CE2 1 
ATOM   10927 C CZ  . PHE F 2 70  ? 19.632  -33.207 -30.608  1.00 48.06  ? 70  PHE F CZ  1 
ATOM   10928 N N   . ASN F 2 71  ? 15.838  -33.869 -24.457  1.00 63.09  ? 71  ASN F N   1 
ATOM   10929 C CA  . ASN F 2 71  ? 15.103  -33.774 -23.203  1.00 71.19  ? 71  ASN F CA  1 
ATOM   10930 C C   . ASN F 2 71  ? 15.631  -32.606 -22.369  1.00 64.40  ? 71  ASN F C   1 
ATOM   10931 O O   . ASN F 2 71  ? 16.428  -31.785 -22.832  1.00 66.51  ? 71  ASN F O   1 
ATOM   10932 C CB  . ASN F 2 71  ? 15.165  -35.104 -22.451  1.00 75.58  ? 71  ASN F CB  1 
ATOM   10933 C CG  . ASN F 2 71  ? 16.588  -35.570 -22.187  1.00 62.46  ? 71  ASN F CG  1 
ATOM   10934 O OD1 . ASN F 2 71  ? 17.487  -34.768 -21.933  1.00 68.84  ? 71  ASN F OD1 1 
ATOM   10935 N ND2 . ASN F 2 71  ? 16.794  -36.880 -22.241  1.00 65.89  ? 71  ASN F ND2 1 
ATOM   10936 N N   . ASN F 2 72  ? 15.189  -32.528 -21.111  1.00 73.09  ? 72  ASN F N   1 
ATOM   10937 C CA  . ASN F 2 72  ? 15.517  -31.398 -20.249  1.00 78.95  ? 72  ASN F CA  1 
ATOM   10938 C C   . ASN F 2 72  ? 16.951  -31.425 -19.737  1.00 64.68  ? 72  ASN F C   1 
ATOM   10939 O O   . ASN F 2 72  ? 17.406  -30.419 -19.182  1.00 64.86  ? 72  ASN F O   1 
ATOM   10940 C CB  . ASN F 2 72  ? 14.548  -31.344 -19.067  1.00 77.83  ? 72  ASN F CB  1 
ATOM   10941 C CG  . ASN F 2 72  ? 13.575  -30.186 -19.165  1.00 100.92 ? 72  ASN F CG  1 
ATOM   10942 O OD1 . ASN F 2 72  ? 13.951  -29.077 -19.545  1.00 106.15 ? 72  ASN F OD1 1 
ATOM   10943 N ND2 . ASN F 2 72  ? 12.316  -30.439 -18.828  1.00 115.65 ? 72  ASN F ND2 1 
ATOM   10944 N N   . LEU F 2 73  ? 17.671  -32.535 -19.899  1.00 52.95  ? 73  LEU F N   1 
ATOM   10945 C CA  . LEU F 2 73  ? 19.083  -32.600 -19.544  1.00 53.84  ? 73  LEU F CA  1 
ATOM   10946 C C   . LEU F 2 73  ? 19.979  -32.659 -20.775  1.00 64.88  ? 73  LEU F C   1 
ATOM   10947 O O   . LEU F 2 73  ? 21.123  -33.119 -20.690  1.00 64.28  ? 73  LEU F O   1 
ATOM   10948 C CB  . LEU F 2 73  ? 19.351  -33.788 -18.620  1.00 59.21  ? 73  LEU F CB  1 
ATOM   10949 C CG  . LEU F 2 73  ? 19.185  -33.460 -17.134  1.00 61.86  ? 73  LEU F CG  1 
ATOM   10950 C CD1 . LEU F 2 73  ? 19.299  -34.708 -16.275  1.00 50.82  ? 73  LEU F CD1 1 
ATOM   10951 C CD2 . LEU F 2 73  ? 20.214  -32.423 -16.713  1.00 49.03  ? 73  LEU F CD2 1 
ATOM   10952 N N   . GLU F 2 74  ? 19.473  -32.204 -21.921  1.00 63.39  ? 74  GLU F N   1 
ATOM   10953 C CA  . GLU F 2 74  ? 20.247  -32.068 -23.149  1.00 63.40  ? 74  GLU F CA  1 
ATOM   10954 C C   . GLU F 2 74  ? 20.081  -30.668 -23.729  1.00 65.91  ? 74  GLU F C   1 
ATOM   10955 O O   . GLU F 2 74  ? 20.087  -30.487 -24.949  1.00 77.11  ? 74  GLU F O   1 
ATOM   10956 C CB  . GLU F 2 74  ? 19.841  -33.131 -24.170  1.00 58.07  ? 74  GLU F CB  1 
ATOM   10957 C CG  . GLU F 2 74  ? 20.246  -34.546 -23.786  1.00 59.03  ? 74  GLU F CG  1 
ATOM   10958 C CD  . GLU F 2 74  ? 19.578  -35.599 -24.649  1.00 73.77  ? 74  GLU F CD  1 
ATOM   10959 O OE1 . GLU F 2 74  ? 18.385  -35.430 -24.978  1.00 67.75  ? 74  GLU F OE1 1 
ATOM   10960 O OE2 . GLU F 2 74  ? 20.246  -36.592 -25.004  1.00 78.20  ? 74  GLU F OE2 1 
ATOM   10961 N N   . ARG F 2 75  ? 19.934  -29.667 -22.853  1.00 67.73  ? 75  ARG F N   1 
ATOM   10962 C CA  . ARG F 2 75  ? 19.649  -28.305 -23.295  1.00 63.85  ? 75  ARG F CA  1 
ATOM   10963 C C   . ARG F 2 75  ? 20.825  -27.688 -24.039  1.00 66.61  ? 75  ARG F C   1 
ATOM   10964 O O   . ARG F 2 75  ? 20.625  -26.816 -24.892  1.00 63.97  ? 75  ARG F O   1 
ATOM   10965 C CB  . ARG F 2 75  ? 19.271  -27.433 -22.096  1.00 61.76  ? 75  ARG F CB  1 
ATOM   10966 C CG  . ARG F 2 75  ? 17.935  -27.776 -21.445  1.00 58.83  ? 75  ARG F CG  1 
ATOM   10967 C CD  . ARG F 2 75  ? 16.802  -26.915 -21.992  1.00 76.53  ? 75  ARG F CD  1 
ATOM   10968 N NE  . ARG F 2 75  ? 16.288  -27.401 -23.267  1.00 100.01 ? 75  ARG F NE  1 
ATOM   10969 C CZ  . ARG F 2 75  ? 15.172  -28.105 -23.406  1.00 104.36 ? 75  ARG F CZ  1 
ATOM   10970 N NH1 . ARG F 2 75  ? 14.422  -28.425 -22.364  1.00 103.25 ? 75  ARG F NH1 1 
ATOM   10971 N NH2 . ARG F 2 75  ? 14.797  -28.493 -24.621  1.00 86.45  ? 75  ARG F NH2 1 
ATOM   10972 N N   . ARG F 2 76  ? 22.053  -28.108 -23.724  1.00 68.05  ? 76  ARG F N   1 
ATOM   10973 C CA  . ARG F 2 76  ? 23.213  -27.590 -24.443  1.00 67.65  ? 76  ARG F CA  1 
ATOM   10974 C C   . ARG F 2 76  ? 23.164  -27.977 -25.916  1.00 61.34  ? 76  ARG F C   1 
ATOM   10975 O O   . ARG F 2 76  ? 23.450  -27.152 -26.792  1.00 66.43  ? 76  ARG F O   1 
ATOM   10976 C CB  . ARG F 2 76  ? 24.503  -28.095 -23.799  1.00 63.79  ? 76  ARG F CB  1 
ATOM   10977 C CG  . ARG F 2 76  ? 24.761  -27.569 -22.397  1.00 64.52  ? 76  ARG F CG  1 
ATOM   10978 C CD  . ARG F 2 76  ? 25.994  -28.231 -21.819  1.00 54.09  ? 76  ARG F CD  1 
ATOM   10979 N NE  . ARG F 2 76  ? 25.826  -29.677 -21.741  1.00 46.85  ? 76  ARG F NE  1 
ATOM   10980 C CZ  . ARG F 2 76  ? 26.823  -30.551 -21.733  1.00 47.04  ? 76  ARG F CZ  1 
ATOM   10981 N NH1 . ARG F 2 76  ? 28.083  -30.163 -21.838  1.00 57.05  ? 76  ARG F NH1 1 
ATOM   10982 N NH2 . ARG F 2 76  ? 26.548  -31.847 -21.625  1.00 44.39  ? 76  ARG F NH2 1 
ATOM   10983 N N   . ILE F 2 77  ? 22.801  -29.227 -26.206  1.00 62.49  ? 77  ILE F N   1 
ATOM   10984 C CA  . ILE F 2 77  ? 22.675  -29.661 -27.593  1.00 61.19  ? 77  ILE F CA  1 
ATOM   10985 C C   . ILE F 2 77  ? 21.500  -28.963 -28.267  1.00 68.08  ? 77  ILE F C   1 
ATOM   10986 O O   . ILE F 2 77  ? 21.581  -28.575 -29.439  1.00 67.36  ? 77  ILE F O   1 
ATOM   10987 C CB  . ILE F 2 77  ? 22.543  -31.192 -27.661  1.00 53.11  ? 77  ILE F CB  1 
ATOM   10988 C CG1 . ILE F 2 77  ? 23.767  -31.850 -27.021  1.00 62.05  ? 77  ILE F CG1 1 
ATOM   10989 C CG2 . ILE F 2 77  ? 22.363  -31.636 -29.102  1.00 66.26  ? 77  ILE F CG2 1 
ATOM   10990 C CD1 . ILE F 2 77  ? 23.664  -33.356 -26.883  1.00 75.70  ? 77  ILE F CD1 1 
ATOM   10991 N N   . GLU F 2 78  ? 20.390  -28.797 -27.542  1.00 65.42  ? 78  GLU F N   1 
ATOM   10992 C CA  . GLU F 2 78  ? 19.248  -28.072 -28.089  1.00 65.37  ? 78  GLU F CA  1 
ATOM   10993 C C   . GLU F 2 78  ? 19.635  -26.643 -28.448  1.00 67.93  ? 78  GLU F C   1 
ATOM   10994 O O   . GLU F 2 78  ? 19.207  -26.115 -29.482  1.00 73.05  ? 78  GLU F O   1 
ATOM   10995 C CB  . GLU F 2 78  ? 18.092  -28.090 -27.085  1.00 65.33  ? 78  GLU F CB  1 
ATOM   10996 C CG  . GLU F 2 78  ? 16.744  -27.615 -27.631  1.00 90.66  ? 78  GLU F CG  1 
ATOM   10997 C CD  . GLU F 2 78  ? 16.651  -26.105 -27.766  1.00 117.14 ? 78  GLU F CD  1 
ATOM   10998 O OE1 . GLU F 2 78  ? 15.971  -25.631 -28.702  1.00 120.57 ? 78  GLU F OE1 1 
ATOM   10999 O OE2 . GLU F 2 78  ? 17.261  -25.394 -26.939  1.00 110.03 ? 78  GLU F OE2 1 
ATOM   11000 N N   . ASN F 2 79  ? 20.452  -26.003 -27.608  1.00 67.15  ? 79  ASN F N   1 
ATOM   11001 C CA  . ASN F 2 79  ? 20.936  -24.663 -27.919  1.00 63.56  ? 79  ASN F CA  1 
ATOM   11002 C C   . ASN F 2 79  ? 21.793  -24.667 -29.178  1.00 75.72  ? 79  ASN F C   1 
ATOM   11003 O O   . ASN F 2 79  ? 21.733  -23.729 -29.982  1.00 75.63  ? 79  ASN F O   1 
ATOM   11004 C CB  . ASN F 2 79  ? 21.723  -24.101 -26.735  1.00 50.68  ? 79  ASN F CB  1 
ATOM   11005 C CG  . ASN F 2 79  ? 22.276  -22.717 -27.009  1.00 65.13  ? 79  ASN F CG  1 
ATOM   11006 O OD1 . ASN F 2 79  ? 23.490  -22.513 -27.037  1.00 81.05  ? 79  ASN F OD1 1 
ATOM   11007 N ND2 . ASN F 2 79  ? 21.384  -21.756 -27.221  1.00 68.78  ? 79  ASN F ND2 1 
ATOM   11008 N N   . LEU F 2 80  ? 22.604  -25.712 -29.362  1.00 73.39  ? 80  LEU F N   1 
ATOM   11009 C CA  . LEU F 2 80  ? 23.407  -25.818 -30.575  1.00 60.36  ? 80  LEU F CA  1 
ATOM   11010 C C   . LEU F 2 80  ? 22.523  -25.916 -31.811  1.00 61.93  ? 80  LEU F C   1 
ATOM   11011 O O   . LEU F 2 80  ? 22.818  -25.305 -32.844  1.00 71.68  ? 80  LEU F O   1 
ATOM   11012 C CB  . LEU F 2 80  ? 24.337  -27.027 -30.488  1.00 60.22  ? 80  LEU F CB  1 
ATOM   11013 C CG  . LEU F 2 80  ? 25.576  -26.946 -31.377  1.00 60.87  ? 80  LEU F CG  1 
ATOM   11014 C CD1 . LEU F 2 80  ? 26.546  -25.939 -30.793  1.00 86.16  ? 80  LEU F CD1 1 
ATOM   11015 C CD2 . LEU F 2 80  ? 26.235  -28.307 -31.541  1.00 66.33  ? 80  LEU F CD2 1 
ATOM   11016 N N   . ASN F 2 81  ? 21.437  -26.689 -31.724  1.00 58.06  ? 81  ASN F N   1 
ATOM   11017 C CA  . ASN F 2 81  ? 20.481  -26.754 -32.825  1.00 54.80  ? 81  ASN F CA  1 
ATOM   11018 C C   . ASN F 2 81  ? 19.838  -25.395 -33.069  1.00 62.69  ? 81  ASN F C   1 
ATOM   11019 O O   . ASN F 2 81  ? 19.606  -25.005 -34.220  1.00 71.18  ? 81  ASN F O   1 
ATOM   11020 C CB  . ASN F 2 81  ? 19.411  -27.806 -32.528  1.00 55.79  ? 81  ASN F CB  1 
ATOM   11021 C CG  . ASN F 2 81  ? 18.439  -27.993 -33.677  1.00 56.28  ? 81  ASN F CG  1 
ATOM   11022 O OD1 . ASN F 2 81  ? 18.818  -27.921 -34.845  1.00 80.62  ? 81  ASN F OD1 1 
ATOM   11023 N ND2 . ASN F 2 81  ? 17.174  -28.232 -33.348  1.00 84.09  ? 81  ASN F ND2 1 
ATOM   11024 N N   . LYS F 2 82  ? 19.534  -24.666 -31.994  1.00 63.51  ? 82  LYS F N   1 
ATOM   11025 C CA  . LYS F 2 82  ? 18.944  -23.338 -32.128  1.00 59.97  ? 82  LYS F CA  1 
ATOM   11026 C C   . LYS F 2 82  ? 19.891  -22.377 -32.836  1.00 71.16  ? 82  LYS F C   1 
ATOM   11027 O O   . LYS F 2 82  ? 19.470  -21.609 -33.709  1.00 75.01  ? 82  LYS F O   1 
ATOM   11028 C CB  . LYS F 2 82  ? 18.569  -22.798 -30.749  1.00 59.15  ? 82  LYS F CB  1 
ATOM   11029 C CG  . LYS F 2 82  ? 17.945  -21.417 -30.766  1.00 57.25  ? 82  LYS F CG  1 
ATOM   11030 C CD  . LYS F 2 82  ? 18.464  -20.573 -29.615  1.00 74.02  ? 82  LYS F CD  1 
ATOM   11031 C CE  . LYS F 2 82  ? 17.523  -19.421 -29.317  1.00 65.90  ? 82  LYS F CE  1 
ATOM   11032 N NZ  . LYS F 2 82  ? 17.080  -18.738 -30.562  1.00 75.25  ? 82  LYS F NZ  1 
ATOM   11033 N N   . LYS F 2 83  ? 21.176  -22.402 -32.468  1.00 66.57  ? 83  LYS F N   1 
ATOM   11034 C CA  . LYS F 2 83  ? 22.144  -21.499 -33.083  1.00 57.82  ? 83  LYS F CA  1 
ATOM   11035 C C   . LYS F 2 83  ? 22.304  -21.793 -34.571  1.00 67.06  ? 83  LYS F C   1 
ATOM   11036 O O   . LYS F 2 83  ? 22.444  -20.870 -35.382  1.00 68.80  ? 83  LYS F O   1 
ATOM   11037 C CB  . LYS F 2 83  ? 23.486  -21.597 -32.355  1.00 55.28  ? 83  LYS F CB  1 
ATOM   11038 C CG  . LYS F 2 83  ? 23.476  -20.944 -30.977  1.00 68.82  ? 83  LYS F CG  1 
ATOM   11039 C CD  . LYS F 2 83  ? 24.475  -21.579 -30.020  1.00 75.18  ? 83  LYS F CD  1 
ATOM   11040 C CE  . LYS F 2 83  ? 25.871  -20.998 -30.167  1.00 100.89 ? 83  LYS F CE  1 
ATOM   11041 N NZ  . LYS F 2 83  ? 26.763  -21.500 -29.083  1.00 96.84  ? 83  LYS F NZ  1 
ATOM   11042 N N   . MET F 2 84  ? 22.281  -23.074 -34.946  1.00 64.47  ? 84  MET F N   1 
ATOM   11043 C CA  . MET F 2 84  ? 22.397  -23.447 -36.352  1.00 59.99  ? 84  MET F CA  1 
ATOM   11044 C C   . MET F 2 84  ? 21.175  -23.002 -37.148  1.00 67.59  ? 84  MET F C   1 
ATOM   11045 O O   . MET F 2 84  ? 21.304  -22.433 -38.239  1.00 67.37  ? 84  MET F O   1 
ATOM   11046 C CB  . MET F 2 84  ? 22.586  -24.958 -36.477  1.00 54.00  ? 84  MET F CB  1 
ATOM   11047 C CG  . MET F 2 84  ? 22.381  -25.495 -37.886  1.00 66.60  ? 84  MET F CG  1 
ATOM   11048 S SD  . MET F 2 84  ? 22.168  -27.286 -37.896  1.00 79.20  ? 84  MET F SD  1 
ATOM   11049 C CE  . MET F 2 84  ? 20.428  -27.425 -38.299  1.00 66.87  ? 84  MET F CE  1 
ATOM   11050 N N   . GLU F 2 85  ? 19.977  -23.271 -36.625  1.00 60.02  ? 85  GLU F N   1 
ATOM   11051 C CA  . GLU F 2 85  ? 18.759  -22.939 -37.356  1.00 58.07  ? 85  GLU F CA  1 
ATOM   11052 C C   . GLU F 2 85  ? 18.614  -21.433 -37.540  1.00 60.66  ? 85  GLU F C   1 
ATOM   11053 O O   . GLU F 2 85  ? 18.233  -20.964 -38.620  1.00 73.86  ? 85  GLU F O   1 
ATOM   11054 C CB  . GLU F 2 85  ? 17.540  -23.515 -36.635  1.00 46.00  ? 85  GLU F CB  1 
ATOM   11055 C CG  . GLU F 2 85  ? 17.226  -24.952 -37.017  1.00 71.87  ? 85  GLU F CG  1 
ATOM   11056 C CD  . GLU F 2 85  ? 16.014  -25.498 -36.290  1.00 88.81  ? 85  GLU F CD  1 
ATOM   11057 O OE1 . GLU F 2 85  ? 15.353  -24.724 -35.564  1.00 70.61  ? 85  GLU F OE1 1 
ATOM   11058 O OE2 . GLU F 2 85  ? 15.726  -26.704 -36.443  1.00 92.61  ? 85  GLU F OE2 1 
ATOM   11059 N N   . ASP F 2 86  ? 18.912  -20.657 -36.497  1.00 62.47  ? 86  ASP F N   1 
ATOM   11060 C CA  . ASP F 2 86  ? 18.844  -19.208 -36.622  1.00 69.06  ? 86  ASP F CA  1 
ATOM   11061 C C   . ASP F 2 86  ? 19.935  -18.672 -37.540  1.00 65.85  ? 86  ASP F C   1 
ATOM   11062 O O   . ASP F 2 86  ? 19.710  -17.692 -38.258  1.00 69.62  ? 86  ASP F O   1 
ATOM   11063 C CB  . ASP F 2 86  ? 18.934  -18.559 -35.241  1.00 76.11  ? 86  ASP F CB  1 
ATOM   11064 C CG  . ASP F 2 86  ? 17.795  -18.973 -34.329  1.00 83.58  ? 86  ASP F CG  1 
ATOM   11065 O OD1 . ASP F 2 86  ? 16.866  -19.656 -34.812  1.00 96.29  ? 86  ASP F OD1 1 
ATOM   11066 O OD2 . ASP F 2 86  ? 17.827  -18.624 -33.132  1.00 85.21  ? 86  ASP F OD2 1 
ATOM   11067 N N   . GLY F 2 87  ? 21.115  -19.296 -37.532  1.00 61.66  ? 87  GLY F N   1 
ATOM   11068 C CA  . GLY F 2 87  ? 22.173  -18.865 -38.431  1.00 53.13  ? 87  GLY F CA  1 
ATOM   11069 C C   . GLY F 2 87  ? 21.818  -19.065 -39.892  1.00 56.27  ? 87  GLY F C   1 
ATOM   11070 O O   . GLY F 2 87  ? 22.057  -18.187 -40.724  1.00 67.41  ? 87  GLY F O   1 
ATOM   11071 N N   . PHE F 2 88  ? 21.249  -20.227 -40.226  1.00 55.79  ? 88  PHE F N   1 
ATOM   11072 C CA  . PHE F 2 88  ? 20.796  -20.459 -41.593  1.00 55.15  ? 88  PHE F CA  1 
ATOM   11073 C C   . PHE F 2 88  ? 19.628  -19.553 -41.957  1.00 60.31  ? 88  PHE F C   1 
ATOM   11074 O O   . PHE F 2 88  ? 19.492  -19.157 -43.120  1.00 68.92  ? 88  PHE F O   1 
ATOM   11075 C CB  . PHE F 2 88  ? 20.412  -21.928 -41.779  1.00 50.10  ? 88  PHE F CB  1 
ATOM   11076 C CG  . PHE F 2 88  ? 21.587  -22.837 -41.997  1.00 64.43  ? 88  PHE F CG  1 
ATOM   11077 C CD1 . PHE F 2 88  ? 22.598  -22.484 -42.875  1.00 59.68  ? 88  PHE F CD1 1 
ATOM   11078 C CD2 . PHE F 2 88  ? 21.685  -24.041 -41.319  1.00 60.45  ? 88  PHE F CD2 1 
ATOM   11079 C CE1 . PHE F 2 88  ? 23.681  -23.317 -43.077  1.00 66.64  ? 88  PHE F CE1 1 
ATOM   11080 C CE2 . PHE F 2 88  ? 22.767  -24.877 -41.517  1.00 61.48  ? 88  PHE F CE2 1 
ATOM   11081 C CZ  . PHE F 2 88  ? 23.767  -24.514 -42.396  1.00 63.10  ? 88  PHE F CZ  1 
ATOM   11082 N N   . LEU F 2 89  ? 18.775  -19.224 -40.984  1.00 58.17  ? 89  LEU F N   1 
ATOM   11083 C CA  . LEU F 2 89  ? 17.691  -18.281 -41.235  1.00 60.70  ? 89  LEU F CA  1 
ATOM   11084 C C   . LEU F 2 89  ? 18.232  -16.909 -41.616  1.00 65.11  ? 89  LEU F C   1 
ATOM   11085 O O   . LEU F 2 89  ? 17.737  -16.276 -42.556  1.00 67.73  ? 89  LEU F O   1 
ATOM   11086 C CB  . LEU F 2 89  ? 16.793  -18.171 -40.003  1.00 56.38  ? 89  LEU F CB  1 
ATOM   11087 C CG  . LEU F 2 89  ? 15.729  -17.072 -40.066  1.00 54.00  ? 89  LEU F CG  1 
ATOM   11088 C CD1 . LEU F 2 89  ? 14.498  -17.541 -40.829  1.00 59.03  ? 89  LEU F CD1 1 
ATOM   11089 C CD2 . LEU F 2 89  ? 15.357  -16.577 -38.675  1.00 55.71  ? 89  LEU F CD2 1 
ATOM   11090 N N   . ASP F 2 90  ? 19.251  -16.433 -40.897  1.00 65.21  ? 90  ASP F N   1 
ATOM   11091 C CA  . ASP F 2 90  ? 19.808  -15.114 -41.181  1.00 65.64  ? 90  ASP F CA  1 
ATOM   11092 C C   . ASP F 2 90  ? 20.514  -15.087 -42.530  1.00 60.09  ? 90  ASP F C   1 
ATOM   11093 O O   . ASP F 2 90  ? 20.461  -14.078 -43.244  1.00 63.31  ? 90  ASP F O   1 
ATOM   11094 C CB  . ASP F 2 90  ? 20.765  -14.697 -40.064  1.00 65.03  ? 90  ASP F CB  1 
ATOM   11095 C CG  . ASP F 2 90  ? 20.069  -14.550 -38.727  1.00 74.56  ? 90  ASP F CG  1 
ATOM   11096 O OD1 . ASP F 2 90  ? 18.857  -14.840 -38.652  1.00 74.43  ? 90  ASP F OD1 1 
ATOM   11097 O OD2 . ASP F 2 90  ? 20.733  -14.142 -37.750  1.00 89.43  ? 90  ASP F OD2 1 
ATOM   11098 N N   . VAL F 2 91  ? 21.187  -16.180 -42.894  1.00 63.96  ? 91  VAL F N   1 
ATOM   11099 C CA  . VAL F 2 91  ? 21.897  -16.228 -44.169  1.00 57.60  ? 91  VAL F CA  1 
ATOM   11100 C C   . VAL F 2 91  ? 20.914  -16.175 -45.333  1.00 58.34  ? 91  VAL F C   1 
ATOM   11101 O O   . VAL F 2 91  ? 21.083  -15.390 -46.273  1.00 67.00  ? 91  VAL F O   1 
ATOM   11102 C CB  . VAL F 2 91  ? 22.789  -17.480 -44.241  1.00 48.33  ? 91  VAL F CB  1 
ATOM   11103 C CG1 . VAL F 2 91  ? 23.036  -17.880 -45.688  1.00 57.37  ? 91  VAL F CG1 1 
ATOM   11104 C CG2 . VAL F 2 91  ? 24.108  -17.232 -43.532  1.00 53.49  ? 91  VAL F CG2 1 
ATOM   11105 N N   . TRP F 2 92  ? 19.873  -17.009 -45.290  1.00 61.72  ? 92  TRP F N   1 
ATOM   11106 C CA  . TRP F 2 92  ? 18.918  -17.042 -46.393  1.00 65.00  ? 92  TRP F CA  1 
ATOM   11107 C C   . TRP F 2 92  ? 18.095  -15.761 -46.459  1.00 63.89  ? 92  TRP F C   1 
ATOM   11108 O O   . TRP F 2 92  ? 17.818  -15.255 -47.553  1.00 66.23  ? 92  TRP F O   1 
ATOM   11109 C CB  . TRP F 2 92  ? 18.005  -18.262 -46.271  1.00 52.32  ? 92  TRP F CB  1 
ATOM   11110 C CG  . TRP F 2 92  ? 18.674  -19.553 -46.638  1.00 52.53  ? 92  TRP F CG  1 
ATOM   11111 C CD1 . TRP F 2 92  ? 18.815  -20.656 -45.848  1.00 53.91  ? 92  TRP F CD1 1 
ATOM   11112 C CD2 . TRP F 2 92  ? 19.303  -19.871 -47.887  1.00 55.73  ? 92  TRP F CD2 1 
ATOM   11113 N NE1 . TRP F 2 92  ? 19.486  -21.643 -46.530  1.00 59.23  ? 92  TRP F NE1 1 
ATOM   11114 C CE2 . TRP F 2 92  ? 19.797  -21.186 -47.783  1.00 62.20  ? 92  TRP F CE2 1 
ATOM   11115 C CE3 . TRP F 2 92  ? 19.492  -19.173 -49.084  1.00 69.29  ? 92  TRP F CE3 1 
ATOM   11116 C CZ2 . TRP F 2 92  ? 20.469  -21.816 -48.829  1.00 65.84  ? 92  TRP F CZ2 1 
ATOM   11117 C CZ3 . TRP F 2 92  ? 20.161  -19.800 -50.120  1.00 65.32  ? 92  TRP F CZ3 1 
ATOM   11118 C CH2 . TRP F 2 92  ? 20.641  -21.108 -49.986  1.00 62.66  ? 92  TRP F CH2 1 
ATOM   11119 N N   . THR F 2 93  ? 17.688  -15.228 -45.305  1.00 58.89  ? 93  THR F N   1 
ATOM   11120 C CA  . THR F 2 93  ? 16.895  -14.003 -45.298  1.00 62.56  ? 93  THR F CA  1 
ATOM   11121 C C   . THR F 2 93  ? 17.679  -12.837 -45.890  1.00 68.49  ? 93  THR F C   1 
ATOM   11122 O O   . THR F 2 93  ? 17.159  -12.082 -46.719  1.00 80.27  ? 93  THR F O   1 
ATOM   11123 C CB  . THR F 2 93  ? 16.441  -13.678 -43.874  1.00 62.27  ? 93  THR F CB  1 
ATOM   11124 O OG1 . THR F 2 93  ? 15.497  -14.664 -43.437  1.00 65.37  ? 93  THR F OG1 1 
ATOM   11125 C CG2 . THR F 2 93  ? 15.791  -12.300 -43.815  1.00 53.42  ? 93  THR F CG2 1 
ATOM   11126 N N   . TYR F 2 94  ? 18.940  -12.683 -45.485  1.00 65.53  ? 94  TYR F N   1 
ATOM   11127 C CA  . TYR F 2 94  ? 19.749  -11.574 -45.981  1.00 59.35  ? 94  TYR F CA  1 
ATOM   11128 C C   . TYR F 2 94  ? 20.045  -11.727 -47.469  1.00 71.53  ? 94  TYR F C   1 
ATOM   11129 O O   . TYR F 2 94  ? 19.932  -10.765 -48.238  1.00 71.95  ? 94  TYR F O   1 
ATOM   11130 C CB  . TYR F 2 94  ? 21.046  -11.475 -45.176  1.00 64.21  ? 94  TYR F CB  1 
ATOM   11131 C CG  . TYR F 2 94  ? 21.837  -10.212 -45.432  1.00 63.08  ? 94  TYR F CG  1 
ATOM   11132 C CD1 . TYR F 2 94  ? 21.399  -8.987  -44.947  1.00 66.83  ? 94  TYR F CD1 1 
ATOM   11133 C CD2 . TYR F 2 94  ? 23.028  -10.247 -46.146  1.00 68.66  ? 94  TYR F CD2 1 
ATOM   11134 C CE1 . TYR F 2 94  ? 22.120  -7.829  -45.173  1.00 61.62  ? 94  TYR F CE1 1 
ATOM   11135 C CE2 . TYR F 2 94  ? 23.757  -9.094  -46.377  1.00 68.57  ? 94  TYR F CE2 1 
ATOM   11136 C CZ  . TYR F 2 94  ? 23.297  -7.888  -45.888  1.00 69.33  ? 94  TYR F CZ  1 
ATOM   11137 O OH  . TYR F 2 94  ? 24.016  -6.735  -46.113  1.00 76.66  ? 94  TYR F OH  1 
ATOM   11138 N N   . ASN F 2 95  ? 20.424  -12.935 -47.894  1.00 72.37  ? 95  ASN F N   1 
ATOM   11139 C CA  . ASN F 2 95  ? 20.745  -13.157 -49.301  1.00 64.39  ? 95  ASN F CA  1 
ATOM   11140 C C   . ASN F 2 95  ? 19.522  -12.971 -50.191  1.00 72.20  ? 95  ASN F C   1 
ATOM   11141 O O   . ASN F 2 95  ? 19.613  -12.353 -51.257  1.00 71.57  ? 95  ASN F O   1 
ATOM   11142 C CB  . ASN F 2 95  ? 21.338  -14.554 -49.489  1.00 67.59  ? 95  ASN F CB  1 
ATOM   11143 C CG  . ASN F 2 95  ? 22.730  -14.683 -48.900  1.00 89.01  ? 95  ASN F CG  1 
ATOM   11144 O OD1 . ASN F 2 95  ? 23.238  -13.756 -48.269  1.00 81.58  ? 95  ASN F OD1 1 
ATOM   11145 N ND2 . ASN F 2 95  ? 23.353  -15.840 -49.098  1.00 91.69  ? 95  ASN F ND2 1 
ATOM   11146 N N   . ALA F 2 96  ? 18.368  -13.498 -49.773  1.00 71.62  ? 96  ALA F N   1 
ATOM   11147 C CA  . ALA F 2 96  ? 17.172  -13.413 -50.608  1.00 56.39  ? 96  ALA F CA  1 
ATOM   11148 C C   . ALA F 2 96  ? 16.700  -11.973 -50.770  1.00 61.92  ? 96  ALA F C   1 
ATOM   11149 O O   . ALA F 2 96  ? 16.327  -11.559 -51.875  1.00 75.81  ? 96  ALA F O   1 
ATOM   11150 C CB  . ALA F 2 96  ? 16.057  -14.278 -50.020  1.00 53.94  ? 96  ALA F CB  1 
ATOM   11151 N N   . GLU F 2 97  ? 16.698  -11.199 -49.682  1.00 71.04  ? 97  GLU F N   1 
ATOM   11152 C CA  . GLU F 2 97  ? 16.266  -9.806  -49.761  1.00 76.62  ? 97  GLU F CA  1 
ATOM   11153 C C   . GLU F 2 97  ? 17.191  -8.996  -50.662  1.00 81.04  ? 97  GLU F C   1 
ATOM   11154 O O   . GLU F 2 97  ? 16.731  -8.241  -51.526  1.00 91.85  ? 97  GLU F O   1 
ATOM   11155 C CB  . GLU F 2 97  ? 16.211  -9.193  -48.360  1.00 66.25  ? 97  GLU F CB  1 
ATOM   11156 C CG  . GLU F 2 97  ? 15.171  -9.810  -47.430  1.00 82.85  ? 97  GLU F CG  1 
ATOM   11157 C CD  . GLU F 2 97  ? 13.806  -9.159  -47.545  1.00 104.05 ? 97  GLU F CD  1 
ATOM   11158 O OE1 . GLU F 2 97  ? 13.640  -8.263  -48.400  1.00 108.42 ? 97  GLU F OE1 1 
ATOM   11159 O OE2 . GLU F 2 97  ? 12.900  -9.541  -46.773  1.00 97.77  ? 97  GLU F OE2 1 
ATOM   11160 N N   . LEU F 2 98  ? 18.505  -9.151  -50.478  1.00 74.58  ? 98  LEU F N   1 
ATOM   11161 C CA  . LEU F 2 98  ? 19.467  -8.378  -51.259  1.00 78.84  ? 98  LEU F CA  1 
ATOM   11162 C C   . LEU F 2 98  ? 19.476  -8.807  -52.721  1.00 76.96  ? 98  LEU F C   1 
ATOM   11163 O O   . LEU F 2 98  ? 19.568  -7.962  -53.620  1.00 83.23  ? 98  LEU F O   1 
ATOM   11164 C CB  . LEU F 2 98  ? 20.864  -8.511  -50.650  1.00 55.13  ? 98  LEU F CB  1 
ATOM   11165 C CG  . LEU F 2 98  ? 21.308  -7.463  -49.623  1.00 68.45  ? 98  LEU F CG  1 
ATOM   11166 C CD1 . LEU F 2 98  ? 21.722  -6.174  -50.314  1.00 82.16  ? 98  LEU F CD1 1 
ATOM   11167 C CD2 . LEU F 2 98  ? 20.217  -7.189  -48.599  1.00 69.11  ? 98  LEU F CD2 1 
ATOM   11168 N N   . LEU F 2 99  ? 19.386  -10.115 -52.979  1.00 72.07  ? 99  LEU F N   1 
ATOM   11169 C CA  . LEU F 2 99  ? 19.401  -10.609 -54.354  1.00 63.04  ? 99  LEU F CA  1 
ATOM   11170 C C   . LEU F 2 99  ? 18.224  -10.064 -55.153  1.00 74.50  ? 99  LEU F C   1 
ATOM   11171 O O   . LEU F 2 99  ? 18.384  -9.656  -56.309  1.00 73.89  ? 99  LEU F O   1 
ATOM   11172 C CB  . LEU F 2 99  ? 19.386  -12.137 -54.361  1.00 67.56  ? 99  LEU F CB  1 
ATOM   11173 C CG  . LEU F 2 99  ? 18.867  -12.839 -55.618  1.00 74.77  ? 99  LEU F CG  1 
ATOM   11174 C CD1 . LEU F 2 99  ? 19.854  -12.717 -56.768  1.00 70.67  ? 99  LEU F CD1 1 
ATOM   11175 C CD2 . LEU F 2 99  ? 18.559  -14.298 -55.319  1.00 64.16  ? 99  LEU F CD2 1 
ATOM   11176 N N   . VAL F 2 100 ? 17.031  -10.057 -54.554  1.00 71.55  ? 100 VAL F N   1 
ATOM   11177 C CA  . VAL F 2 100 ? 15.857  -9.520  -55.236  1.00 66.98  ? 100 VAL F CA  1 
ATOM   11178 C C   . VAL F 2 100 ? 16.033  -8.032  -55.511  1.00 75.28  ? 100 VAL F C   1 
ATOM   11179 O O   . VAL F 2 100 ? 15.716  -7.546  -56.604  1.00 74.04  ? 100 VAL F O   1 
ATOM   11180 C CB  . VAL F 2 100 ? 14.586  -9.805  -54.413  1.00 69.13  ? 100 VAL F CB  1 
ATOM   11181 C CG1 . VAL F 2 100 ? 13.497  -8.792  -54.732  1.00 75.23  ? 100 VAL F CG1 1 
ATOM   11182 C CG2 . VAL F 2 100 ? 14.091  -11.218 -54.683  1.00 69.02  ? 100 VAL F CG2 1 
ATOM   11183 N N   . LEU F 2 101 ? 16.548  -7.288  -54.528  1.00 76.37  ? 101 LEU F N   1 
ATOM   11184 C CA  . LEU F 2 101 ? 16.755  -5.855  -54.715  1.00 73.83  ? 101 LEU F CA  1 
ATOM   11185 C C   . LEU F 2 101 ? 17.759  -5.578  -55.828  1.00 72.89  ? 101 LEU F C   1 
ATOM   11186 O O   . LEU F 2 101 ? 17.553  -4.675  -56.648  1.00 66.51  ? 101 LEU F O   1 
ATOM   11187 C CB  . LEU F 2 101 ? 17.216  -5.213  -53.406  1.00 71.85  ? 101 LEU F CB  1 
ATOM   11188 C CG  . LEU F 2 101 ? 16.203  -5.178  -52.260  1.00 66.60  ? 101 LEU F CG  1 
ATOM   11189 C CD1 . LEU F 2 101 ? 16.785  -4.472  -51.043  1.00 67.12  ? 101 LEU F CD1 1 
ATOM   11190 C CD2 . LEU F 2 101 ? 14.912  -4.512  -52.702  1.00 57.59  ? 101 LEU F CD2 1 
ATOM   11191 N N   . MET F 2 102 ? 18.856  -6.340  -55.871  1.00 71.34  ? 102 MET F N   1 
ATOM   11192 C CA  . MET F 2 102 ? 19.857  -6.131  -56.914  1.00 63.79  ? 102 MET F CA  1 
ATOM   11193 C C   . MET F 2 102 ? 19.319  -6.507  -58.289  1.00 72.72  ? 102 MET F C   1 
ATOM   11194 O O   . MET F 2 102 ? 19.522  -5.771  -59.262  1.00 78.96  ? 102 MET F O   1 
ATOM   11195 C CB  . MET F 2 102 ? 21.121  -6.931  -56.606  1.00 74.44  ? 102 MET F CB  1 
ATOM   11196 C CG  . MET F 2 102 ? 21.942  -6.389  -55.452  1.00 73.26  ? 102 MET F CG  1 
ATOM   11197 S SD  . MET F 2 102 ? 23.550  -7.194  -55.337  1.00 94.27  ? 102 MET F SD  1 
ATOM   11198 C CE  . MET F 2 102 ? 23.067  -8.918  -55.315  1.00 72.99  ? 102 MET F CE  1 
ATOM   11199 N N   . GLU F 2 103 ? 18.634  -7.648  -58.392  1.00 73.70  ? 103 GLU F N   1 
ATOM   11200 C CA  . GLU F 2 103 ? 18.160  -8.101  -59.696  1.00 75.65  ? 103 GLU F CA  1 
ATOM   11201 C C   . GLU F 2 103 ? 17.000  -7.256  -60.205  1.00 68.23  ? 103 GLU F C   1 
ATOM   11202 O O   . GLU F 2 103 ? 16.830  -7.115  -61.421  1.00 68.03  ? 103 GLU F O   1 
ATOM   11203 C CB  . GLU F 2 103 ? 17.764  -9.576  -59.630  1.00 67.21  ? 103 GLU F CB  1 
ATOM   11204 C CG  . GLU F 2 103 ? 18.949  -10.519 -59.515  1.00 73.99  ? 103 GLU F CG  1 
ATOM   11205 C CD  . GLU F 2 103 ? 19.923  -10.378 -60.670  1.00 92.31  ? 103 GLU F CD  1 
ATOM   11206 O OE1 . GLU F 2 103 ? 19.464  -10.235 -61.822  1.00 100.49 ? 103 GLU F OE1 1 
ATOM   11207 O OE2 . GLU F 2 103 ? 21.147  -10.405 -60.427  1.00 100.01 ? 103 GLU F OE2 1 
ATOM   11208 N N   . ASN F 2 104 ? 16.190  -6.697  -59.303  1.00 63.83  ? 104 ASN F N   1 
ATOM   11209 C CA  . ASN F 2 104 ? 15.150  -5.771  -59.737  1.00 67.66  ? 104 ASN F CA  1 
ATOM   11210 C C   . ASN F 2 104 ? 15.756  -4.516  -60.353  1.00 73.31  ? 104 ASN F C   1 
ATOM   11211 O O   . ASN F 2 104 ? 15.277  -4.028  -61.383  1.00 78.19  ? 104 ASN F O   1 
ATOM   11212 C CB  . ASN F 2 104 ? 14.234  -5.410  -58.568  1.00 61.78  ? 104 ASN F CB  1 
ATOM   11213 C CG  . ASN F 2 104 ? 13.240  -6.508  -58.246  1.00 67.72  ? 104 ASN F CG  1 
ATOM   11214 O OD1 . ASN F 2 104 ? 13.071  -7.454  -59.016  1.00 65.61  ? 104 ASN F OD1 1 
ATOM   11215 N ND2 . ASN F 2 104 ? 12.566  -6.382  -57.109  1.00 66.33  ? 104 ASN F ND2 1 
ATOM   11216 N N   . GLU F 2 105 ? 16.816  -3.982  -59.739  1.00 74.13  ? 105 GLU F N   1 
ATOM   11217 C CA  . GLU F 2 105 ? 17.513  -2.840  -60.322  1.00 70.80  ? 105 GLU F CA  1 
ATOM   11218 C C   . GLU F 2 105 ? 18.129  -3.206  -61.667  1.00 69.21  ? 105 GLU F C   1 
ATOM   11219 O O   . GLU F 2 105 ? 18.094  -2.411  -62.613  1.00 74.68  ? 105 GLU F O   1 
ATOM   11220 C CB  . GLU F 2 105 ? 18.590  -2.333  -59.361  1.00 78.25  ? 105 GLU F CB  1 
ATOM   11221 C CG  . GLU F 2 105 ? 19.314  -1.081  -59.836  1.00 82.79  ? 105 GLU F CG  1 
ATOM   11222 C CD  . GLU F 2 105 ? 18.585  0.195   -59.462  1.00 105.92 ? 105 GLU F CD  1 
ATOM   11223 O OE1 . GLU F 2 105 ? 17.992  0.244   -58.364  1.00 96.99  ? 105 GLU F OE1 1 
ATOM   11224 O OE2 . GLU F 2 105 ? 18.601  1.151   -60.265  1.00 113.25 ? 105 GLU F OE2 1 
ATOM   11225 N N   . ARG F 2 106 ? 18.701  -4.408  -61.766  1.00 66.53  ? 106 ARG F N   1 
ATOM   11226 C CA  . ARG F 2 106 ? 19.283  -4.864  -63.024  1.00 65.19  ? 106 ARG F CA  1 
ATOM   11227 C C   . ARG F 2 106 ? 18.225  -4.972  -64.117  1.00 73.69  ? 106 ARG F C   1 
ATOM   11228 O O   . ARG F 2 106 ? 18.474  -4.603  -65.271  1.00 76.82  ? 106 ARG F O   1 
ATOM   11229 C CB  . ARG F 2 106 ? 19.977  -6.211  -62.812  1.00 76.35  ? 106 ARG F CB  1 
ATOM   11230 C CG  . ARG F 2 106 ? 21.496  -6.146  -62.770  1.00 73.13  ? 106 ARG F CG  1 
ATOM   11231 C CD  . ARG F 2 106 ? 22.076  -6.315  -64.165  1.00 115.38 ? 106 ARG F CD  1 
ATOM   11232 N NE  . ARG F 2 106 ? 23.477  -5.918  -64.243  1.00 127.48 ? 106 ARG F NE  1 
ATOM   11233 C CZ  . ARG F 2 106 ? 24.128  -5.712  -65.380  1.00 113.77 ? 106 ARG F CZ  1 
ATOM   11234 N NH1 . ARG F 2 106 ? 23.535  -5.865  -66.552  1.00 128.27 ? 106 ARG F NH1 1 
ATOM   11235 N NH2 . ARG F 2 106 ? 25.403  -5.336  -65.339  1.00 94.42  ? 106 ARG F NH2 1 
ATOM   11236 N N   . THR F 2 107 ? 17.040  -5.481  -63.773  1.00 75.09  ? 107 THR F N   1 
ATOM   11237 C CA  . THR F 2 107 ? 15.987  -5.655  -64.768  1.00 70.43  ? 107 THR F CA  1 
ATOM   11238 C C   . THR F 2 107 ? 15.493  -4.315  -65.303  1.00 71.35  ? 107 THR F C   1 
ATOM   11239 O O   . THR F 2 107 ? 15.310  -4.155  -66.516  1.00 66.22  ? 107 THR F O   1 
ATOM   11240 C CB  . THR F 2 107 ? 14.828  -6.452  -64.168  1.00 67.87  ? 107 THR F CB  1 
ATOM   11241 O OG1 . THR F 2 107 ? 15.269  -7.779  -63.856  1.00 65.63  ? 107 THR F OG1 1 
ATOM   11242 C CG2 . THR F 2 107 ? 13.662  -6.528  -65.144  1.00 55.47  ? 107 THR F CG2 1 
ATOM   11243 N N   . LEU F 2 108 ? 15.270  -3.341  -64.417  1.00 72.01  ? 108 LEU F N   1 
ATOM   11244 C CA  . LEU F 2 108 ? 14.757  -2.048  -64.861  1.00 65.30  ? 108 LEU F CA  1 
ATOM   11245 C C   . LEU F 2 108 ? 15.801  -1.288  -65.671  1.00 76.85  ? 108 LEU F C   1 
ATOM   11246 O O   . LEU F 2 108 ? 15.462  -0.609  -66.647  1.00 80.90  ? 108 LEU F O   1 
ATOM   11247 C CB  . LEU F 2 108 ? 14.292  -1.227  -63.660  1.00 62.91  ? 108 LEU F CB  1 
ATOM   11248 C CG  . LEU F 2 108 ? 13.295  -1.932  -62.733  1.00 68.17  ? 108 LEU F CG  1 
ATOM   11249 C CD1 . LEU F 2 108 ? 12.762  -0.975  -61.676  1.00 80.05  ? 108 LEU F CD1 1 
ATOM   11250 C CD2 . LEU F 2 108 ? 12.154  -2.572  -63.518  1.00 60.23  ? 108 LEU F CD2 1 
ATOM   11251 N N   . ASP F 2 109 ? 17.075  -1.386  -65.279  1.00 72.63  ? 109 ASP F N   1 
ATOM   11252 C CA  . ASP F 2 109 ? 18.143  -0.826  -66.101  1.00 72.59  ? 109 ASP F CA  1 
ATOM   11253 C C   . ASP F 2 109 ? 18.251  -1.547  -67.438  1.00 70.60  ? 109 ASP F C   1 
ATOM   11254 O O   . ASP F 2 109 ? 18.607  -0.931  -68.450  1.00 74.25  ? 109 ASP F O   1 
ATOM   11255 C CB  . ASP F 2 109 ? 19.476  -0.895  -65.353  1.00 76.22  ? 109 ASP F CB  1 
ATOM   11256 C CG  . ASP F 2 109 ? 19.477  -0.066  -64.084  1.00 101.60 ? 109 ASP F CG  1 
ATOM   11257 O OD1 . ASP F 2 109 ? 18.400  0.440   -63.699  1.00 115.93 ? 109 ASP F OD1 1 
ATOM   11258 O OD2 . ASP F 2 109 ? 20.557  0.081   -63.473  1.00 94.39  ? 109 ASP F OD2 1 
ATOM   11259 N N   . PHE F 2 110 ? 17.950  -2.847  -67.458  1.00 73.20  ? 110 PHE F N   1 
ATOM   11260 C CA  . PHE F 2 110 ? 17.993  -3.613  -68.699  1.00 55.64  ? 110 PHE F CA  1 
ATOM   11261 C C   . PHE F 2 110 ? 16.951  -3.114  -69.693  1.00 68.89  ? 110 PHE F C   1 
ATOM   11262 O O   . PHE F 2 110 ? 17.218  -3.041  -70.899  1.00 68.15  ? 110 PHE F O   1 
ATOM   11263 C CB  . PHE F 2 110 ? 17.793  -5.098  -68.388  1.00 58.89  ? 110 PHE F CB  1 
ATOM   11264 C CG  . PHE F 2 110 ? 17.615  -5.963  -69.602  1.00 46.59  ? 110 PHE F CG  1 
ATOM   11265 C CD1 . PHE F 2 110 ? 18.659  -6.159  -70.491  1.00 56.89  ? 110 PHE F CD1 1 
ATOM   11266 C CD2 . PHE F 2 110 ? 16.409  -6.602  -69.838  1.00 50.91  ? 110 PHE F CD2 1 
ATOM   11267 C CE1 . PHE F 2 110 ? 18.497  -6.963  -71.603  1.00 54.28  ? 110 PHE F CE1 1 
ATOM   11268 C CE2 . PHE F 2 110 ? 16.242  -7.409  -70.946  1.00 59.73  ? 110 PHE F CE2 1 
ATOM   11269 C CZ  . PHE F 2 110 ? 17.287  -7.590  -71.830  1.00 58.03  ? 110 PHE F CZ  1 
ATOM   11270 N N   . HIS F 2 111 ? 15.757  -2.766  -69.206  1.00 68.66  ? 111 HIS F N   1 
ATOM   11271 C CA  . HIS F 2 111 ? 14.728  -2.217  -70.085  1.00 68.63  ? 111 HIS F CA  1 
ATOM   11272 C C   . HIS F 2 111 ? 15.140  -0.861  -70.647  1.00 66.31  ? 111 HIS F C   1 
ATOM   11273 O O   . HIS F 2 111 ? 14.870  -0.561  -71.816  1.00 78.75  ? 111 HIS F O   1 
ATOM   11274 C CB  . HIS F 2 111 ? 13.402  -2.102  -69.334  1.00 52.37  ? 111 HIS F CB  1 
ATOM   11275 C CG  . HIS F 2 111 ? 12.748  -3.419  -69.059  1.00 66.56  ? 111 HIS F CG  1 
ATOM   11276 N ND1 . HIS F 2 111 ? 12.818  -4.481  -69.934  1.00 63.54  ? 111 HIS F ND1 1 
ATOM   11277 C CD2 . HIS F 2 111 ? 12.017  -3.849  -68.004  1.00 62.93  ? 111 HIS F CD2 1 
ATOM   11278 C CE1 . HIS F 2 111 ? 12.155  -5.508  -69.432  1.00 69.66  ? 111 HIS F CE1 1 
ATOM   11279 N NE2 . HIS F 2 111 ? 11.659  -5.151  -68.261  1.00 78.11  ? 111 HIS F NE2 1 
ATOM   11280 N N   . ASP F 2 112 ? 15.784  -0.026  -69.828  1.00 61.57  ? 112 ASP F N   1 
ATOM   11281 C CA  . ASP F 2 112 ? 16.186  1.300   -70.288  1.00 65.85  ? 112 ASP F CA  1 
ATOM   11282 C C   . ASP F 2 112 ? 17.190  1.216   -71.433  1.00 80.23  ? 112 ASP F C   1 
ATOM   11283 O O   . ASP F 2 112 ? 17.105  1.984   -72.399  1.00 81.58  ? 112 ASP F O   1 
ATOM   11284 C CB  . ASP F 2 112 ? 16.767  2.106   -69.125  1.00 67.68  ? 112 ASP F CB  1 
ATOM   11285 C CG  . ASP F 2 112 ? 15.704  2.572   -68.148  1.00 92.91  ? 112 ASP F CG  1 
ATOM   11286 O OD1 . ASP F 2 112 ? 14.503  2.429   -68.458  1.00 99.57  ? 112 ASP F OD1 1 
ATOM   11287 O OD2 . ASP F 2 112 ? 16.072  3.084   -67.068  1.00 111.69 ? 112 ASP F OD2 1 
ATOM   11288 N N   . SER F 2 113 ? 18.155  0.297   -71.338  1.00 72.91  ? 113 SER F N   1 
ATOM   11289 C CA  . SER F 2 113 ? 19.171  0.182   -72.381  1.00 73.17  ? 113 SER F CA  1 
ATOM   11290 C C   . SER F 2 113 ? 18.558  -0.232  -73.713  1.00 65.71  ? 113 SER F C   1 
ATOM   11291 O O   . SER F 2 113 ? 18.950  0.276   -74.770  1.00 75.01  ? 113 SER F O   1 
ATOM   11292 C CB  . SER F 2 113 ? 20.251  -0.814  -71.961  1.00 71.59  ? 113 SER F CB  1 
ATOM   11293 O OG  . SER F 2 113 ? 19.862  -2.144  -72.262  1.00 83.84  ? 113 SER F OG  1 
ATOM   11294 N N   . ASN F 2 114 ? 17.600  -1.163  -73.683  1.00 67.28  ? 114 ASN F N   1 
ATOM   11295 C CA  . ASN F 2 114 ? 16.973  -1.626  -74.918  1.00 77.00  ? 114 ASN F CA  1 
ATOM   11296 C C   . ASN F 2 114 ? 16.239  -0.493  -75.625  1.00 76.62  ? 114 ASN F C   1 
ATOM   11297 O O   . ASN F 2 114 ? 16.293  -0.382  -76.856  1.00 70.85  ? 114 ASN F O   1 
ATOM   11298 C CB  . ASN F 2 114 ? 16.015  -2.780  -74.621  1.00 62.25  ? 114 ASN F CB  1 
ATOM   11299 C CG  . ASN F 2 114 ? 16.721  -3.992  -74.050  1.00 68.93  ? 114 ASN F CG  1 
ATOM   11300 O OD1 . ASN F 2 114 ? 17.890  -4.240  -74.344  1.00 69.19  ? 114 ASN F OD1 1 
ATOM   11301 N ND2 . ASN F 2 114 ? 16.011  -4.757  -73.230  1.00 70.78  ? 114 ASN F ND2 1 
ATOM   11302 N N   . VAL F 2 115 ? 15.541  0.353   -74.864  1.00 65.08  ? 115 VAL F N   1 
ATOM   11303 C CA  . VAL F 2 115 ? 14.825  1.476   -75.461  1.00 62.37  ? 115 VAL F CA  1 
ATOM   11304 C C   . VAL F 2 115 ? 15.800  2.454   -76.105  1.00 70.01  ? 115 VAL F C   1 
ATOM   11305 O O   . VAL F 2 115 ? 15.580  2.927   -77.228  1.00 69.98  ? 115 VAL F O   1 
ATOM   11306 C CB  . VAL F 2 115 ? 13.943  2.166   -74.404  1.00 59.53  ? 115 VAL F CB  1 
ATOM   11307 C CG1 . VAL F 2 115 ? 13.590  3.565   -74.852  1.00 75.58  ? 115 VAL F CG1 1 
ATOM   11308 C CG2 . VAL F 2 115 ? 12.682  1.353   -74.155  1.00 73.24  ? 115 VAL F CG2 1 
ATOM   11309 N N   . LYS F 2 116 ? 16.894  2.770   -75.407  1.00 66.51  ? 116 LYS F N   1 
ATOM   11310 C CA  . LYS F 2 116 ? 17.882  3.701   -75.947  1.00 67.94  ? 116 LYS F CA  1 
ATOM   11311 C C   . LYS F 2 116 ? 18.528  3.151   -77.213  1.00 70.84  ? 116 LYS F C   1 
ATOM   11312 O O   . LYS F 2 116 ? 18.785  3.901   -78.163  1.00 82.02  ? 116 LYS F O   1 
ATOM   11313 C CB  . LYS F 2 116 ? 18.939  4.012   -74.887  1.00 62.88  ? 116 LYS F CB  1 
ATOM   11314 C CG  . LYS F 2 116 ? 20.215  4.633   -75.430  1.00 80.53  ? 116 LYS F CG  1 
ATOM   11315 C CD  . LYS F 2 116 ? 21.070  5.184   -74.304  1.00 101.17 ? 116 LYS F CD  1 
ATOM   11316 C CE  . LYS F 2 116 ? 22.536  5.223   -74.690  1.00 105.16 ? 116 LYS F CE  1 
ATOM   11317 N NZ  . LYS F 2 116 ? 23.374  4.607   -73.624  1.00 102.76 ? 116 LYS F NZ  1 
ATOM   11318 N N   . ASN F 2 117 ? 18.799  1.843   -77.246  1.00 58.11  ? 117 ASN F N   1 
ATOM   11319 C CA  . ASN F 2 117 ? 19.391  1.239   -78.436  1.00 60.06  ? 117 ASN F CA  1 
ATOM   11320 C C   . ASN F 2 117 ? 18.462  1.360   -79.639  1.00 66.55  ? 117 ASN F C   1 
ATOM   11321 O O   . ASN F 2 117 ? 18.919  1.604   -80.762  1.00 81.20  ? 117 ASN F O   1 
ATOM   11322 C CB  . ASN F 2 117 ? 19.740  -0.225  -78.167  1.00 66.40  ? 117 ASN F CB  1 
ATOM   11323 C CG  . ASN F 2 117 ? 20.943  -0.378  -77.254  1.00 87.50  ? 117 ASN F CG  1 
ATOM   11324 O OD1 . ASN F 2 117 ? 21.763  0.532   -77.132  1.00 79.92  ? 117 ASN F OD1 1 
ATOM   11325 N ND2 . ASN F 2 117 ? 21.056  -1.536  -76.613  1.00 93.67  ? 117 ASN F ND2 1 
ATOM   11326 N N   . LEU F 2 118 ? 17.156  1.183   -79.427  1.00 72.95  ? 118 LEU F N   1 
ATOM   11327 C CA  . LEU F 2 118 ? 16.197  1.406   -80.505  1.00 70.22  ? 118 LEU F CA  1 
ATOM   11328 C C   . LEU F 2 118 ? 16.209  2.861   -80.957  1.00 62.78  ? 118 LEU F C   1 
ATOM   11329 O O   . LEU F 2 118 ? 16.148  3.147   -82.159  1.00 69.31  ? 118 LEU F O   1 
ATOM   11330 C CB  . LEU F 2 118 ? 14.794  0.995   -80.057  1.00 70.68  ? 118 LEU F CB  1 
ATOM   11331 C CG  . LEU F 2 118 ? 14.253  -0.329  -80.599  1.00 74.73  ? 118 LEU F CG  1 
ATOM   11332 C CD1 . LEU F 2 118 ? 15.278  -1.438  -80.430  1.00 73.32  ? 118 LEU F CD1 1 
ATOM   11333 C CD2 . LEU F 2 118 ? 12.949  -0.694  -79.907  1.00 79.25  ? 118 LEU F CD2 1 
ATOM   11334 N N   . TYR F 2 119 ? 16.281  3.793   -80.004  1.00 66.26  ? 119 TYR F N   1 
ATOM   11335 C CA  . TYR F 2 119 ? 16.330  5.212   -80.345  1.00 62.47  ? 119 TYR F CA  1 
ATOM   11336 C C   . TYR F 2 119 ? 17.587  5.550   -81.137  1.00 69.72  ? 119 TYR F C   1 
ATOM   11337 O O   . TYR F 2 119 ? 17.526  6.291   -82.125  1.00 82.08  ? 119 TYR F O   1 
ATOM   11338 C CB  . TYR F 2 119 ? 16.255  6.051   -79.068  1.00 60.17  ? 119 TYR F CB  1 
ATOM   11339 C CG  . TYR F 2 119 ? 16.240  7.551   -79.285  1.00 62.49  ? 119 TYR F CG  1 
ATOM   11340 C CD1 . TYR F 2 119 ? 17.423  8.275   -79.360  1.00 62.32  ? 119 TYR F CD1 1 
ATOM   11341 C CD2 . TYR F 2 119 ? 15.041  8.245   -79.393  1.00 70.41  ? 119 TYR F CD2 1 
ATOM   11342 C CE1 . TYR F 2 119 ? 17.413  9.645   -79.551  1.00 68.98  ? 119 TYR F CE1 1 
ATOM   11343 C CE2 . TYR F 2 119 ? 15.021  9.616   -79.581  1.00 67.38  ? 119 TYR F CE2 1 
ATOM   11344 C CZ  . TYR F 2 119 ? 16.209  10.310  -79.660  1.00 67.99  ? 119 TYR F CZ  1 
ATOM   11345 O OH  . TYR F 2 119 ? 16.189  11.674  -79.849  1.00 70.60  ? 119 TYR F OH  1 
ATOM   11346 N N   . ASP F 2 120 ? 18.737  5.012   -80.722  1.00 73.91  ? 120 ASP F N   1 
ATOM   11347 C CA  . ASP F 2 120 ? 19.990  5.348   -81.392  1.00 68.48  ? 120 ASP F CA  1 
ATOM   11348 C C   . ASP F 2 120 ? 20.081  4.728   -82.783  1.00 65.84  ? 120 ASP F C   1 
ATOM   11349 O O   . ASP F 2 120 ? 20.733  5.296   -83.666  1.00 71.08  ? 120 ASP F O   1 
ATOM   11350 C CB  . ASP F 2 120 ? 21.180  4.918   -80.533  1.00 70.74  ? 120 ASP F CB  1 
ATOM   11351 C CG  . ASP F 2 120 ? 21.319  5.753   -79.271  1.00 84.11  ? 120 ASP F CG  1 
ATOM   11352 O OD1 . ASP F 2 120 ? 20.353  6.457   -78.912  1.00 89.08  ? 120 ASP F OD1 1 
ATOM   11353 O OD2 . ASP F 2 120 ? 22.398  5.711   -78.643  1.00 110.05 ? 120 ASP F OD2 1 
ATOM   11354 N N   . LYS F 2 121 ? 19.455  3.567   -82.995  1.00 65.87  ? 121 LYS F N   1 
ATOM   11355 C CA  . LYS F 2 121 ? 19.417  2.988   -84.336  1.00 71.24  ? 121 LYS F CA  1 
ATOM   11356 C C   . LYS F 2 121 ? 18.646  3.884   -85.299  1.00 72.97  ? 121 LYS F C   1 
ATOM   11357 O O   . LYS F 2 121 ? 19.046  4.056   -86.456  1.00 72.64  ? 121 LYS F O   1 
ATOM   11358 C CB  . LYS F 2 121 ? 18.806  1.586   -84.293  1.00 74.56  ? 121 LYS F CB  1 
ATOM   11359 C CG  . LYS F 2 121 ? 19.834  0.459   -84.237  1.00 79.40  ? 121 LYS F CG  1 
ATOM   11360 C CD  . LYS F 2 121 ? 19.224  -0.837  -83.710  1.00 86.70  ? 121 LYS F CD  1 
ATOM   11361 C CE  . LYS F 2 121 ? 18.599  -1.680  -84.816  1.00 87.56  ? 121 LYS F CE  1 
ATOM   11362 N NZ  . LYS F 2 121 ? 19.615  -2.496  -85.542  1.00 99.63  ? 121 LYS F NZ  1 
ATOM   11363 N N   . VAL F 2 122 ? 17.533  4.461   -84.839  1.00 69.09  ? 122 VAL F N   1 
ATOM   11364 C CA  . VAL F 2 122 ? 16.752  5.357   -85.686  1.00 66.64  ? 122 VAL F CA  1 
ATOM   11365 C C   . VAL F 2 122 ? 17.515  6.649   -85.953  1.00 64.96  ? 122 VAL F C   1 
ATOM   11366 O O   . VAL F 2 122 ? 17.552  7.140   -87.088  1.00 75.31  ? 122 VAL F O   1 
ATOM   11367 C CB  . VAL F 2 122 ? 15.379  5.631   -85.047  1.00 52.08  ? 122 VAL F CB  1 
ATOM   11368 C CG1 . VAL F 2 122 ? 14.790  6.930   -85.575  1.00 59.71  ? 122 VAL F CG1 1 
ATOM   11369 C CG2 . VAL F 2 122 ? 14.432  4.475   -85.316  1.00 53.49  ? 122 VAL F CG2 1 
ATOM   11370 N N   . ARG F 2 123 ? 18.132  7.222   -84.918  1.00 61.03  ? 123 ARG F N   1 
ATOM   11371 C CA  . ARG F 2 123 ? 18.806  8.506   -85.077  1.00 63.87  ? 123 ARG F CA  1 
ATOM   11372 C C   . ARG F 2 123 ? 19.954  8.413   -86.076  1.00 63.73  ? 123 ARG F C   1 
ATOM   11373 O O   . ARG F 2 123 ? 20.227  9.371   -86.809  1.00 69.62  ? 123 ARG F O   1 
ATOM   11374 C CB  . ARG F 2 123 ? 19.308  8.999   -83.722  1.00 64.67  ? 123 ARG F CB  1 
ATOM   11375 C CG  . ARG F 2 123 ? 19.857  10.412  -83.725  1.00 77.25  ? 123 ARG F CG  1 
ATOM   11376 C CD  . ARG F 2 123 ? 20.588  10.670  -82.426  1.00 73.19  ? 123 ARG F CD  1 
ATOM   11377 N NE  . ARG F 2 123 ? 21.709  9.752   -82.277  1.00 85.97  ? 123 ARG F NE  1 
ATOM   11378 C CZ  . ARG F 2 123 ? 22.213  9.364   -81.115  1.00 100.95 ? 123 ARG F CZ  1 
ATOM   11379 N NH1 . ARG F 2 123 ? 21.708  9.784   -79.966  1.00 87.69  ? 123 ARG F NH1 1 
ATOM   11380 N NH2 . ARG F 2 123 ? 23.246  8.526   -81.104  1.00 89.34  ? 123 ARG F NH2 1 
ATOM   11381 N N   . LEU F 2 124 ? 20.641  7.269   -86.118  1.00 64.64  ? 124 LEU F N   1 
ATOM   11382 C CA  . LEU F 2 124 ? 21.717  7.087   -87.087  1.00 60.98  ? 124 LEU F CA  1 
ATOM   11383 C C   . LEU F 2 124 ? 21.196  7.116   -88.519  1.00 65.99  ? 124 LEU F C   1 
ATOM   11384 O O   . LEU F 2 124 ? 21.839  7.682   -89.409  1.00 70.65  ? 124 LEU F O   1 
ATOM   11385 C CB  . LEU F 2 124 ? 22.448  5.774   -86.824  1.00 69.91  ? 124 LEU F CB  1 
ATOM   11386 C CG  . LEU F 2 124 ? 23.606  5.814   -85.834  1.00 75.08  ? 124 LEU F CG  1 
ATOM   11387 C CD1 . LEU F 2 124 ? 24.346  4.498   -85.902  1.00 92.81  ? 124 LEU F CD1 1 
ATOM   11388 C CD2 . LEU F 2 124 ? 24.535  6.981   -86.135  1.00 72.40  ? 124 LEU F CD2 1 
ATOM   11389 N N   . GLN F 2 125 ? 20.045  6.486   -88.766  1.00 64.37  ? 125 GLN F N   1 
ATOM   11390 C CA  . GLN F 2 125 ? 19.501  6.451   -90.120  1.00 63.28  ? 125 GLN F CA  1 
ATOM   11391 C C   . GLN F 2 125 ? 19.080  7.840   -90.584  1.00 65.85  ? 125 GLN F C   1 
ATOM   11392 O O   . GLN F 2 125 ? 19.384  8.247   -91.712  1.00 64.62  ? 125 GLN F O   1 
ATOM   11393 C CB  . GLN F 2 125 ? 18.314  5.489   -90.187  1.00 69.98  ? 125 GLN F CB  1 
ATOM   11394 C CG  . GLN F 2 125 ? 18.655  4.039   -89.904  1.00 54.93  ? 125 GLN F CG  1 
ATOM   11395 C CD  . GLN F 2 125 ? 17.498  3.108   -90.206  1.00 64.27  ? 125 GLN F CD  1 
ATOM   11396 O OE1 . GLN F 2 125 ? 17.489  2.422   -91.227  1.00 80.39  ? 125 GLN F OE1 1 
ATOM   11397 N NE2 . GLN F 2 125 ? 16.513  3.080   -89.316  1.00 63.41  ? 125 GLN F NE2 1 
ATOM   11398 N N   . LEU F 2 126 ? 18.378  8.582   -89.725  1.00 63.61  ? 126 LEU F N   1 
ATOM   11399 C CA  . LEU F 2 126 ? 17.768  9.836   -90.154  1.00 66.32  ? 126 LEU F CA  1 
ATOM   11400 C C   . LEU F 2 126 ? 18.813  10.920  -90.386  1.00 65.37  ? 126 LEU F C   1 
ATOM   11401 O O   . LEU F 2 126 ? 18.676  11.731  -91.310  1.00 70.39  ? 126 LEU F O   1 
ATOM   11402 C CB  . LEU F 2 126 ? 16.731  10.286  -89.125  1.00 51.06  ? 126 LEU F CB  1 
ATOM   11403 C CG  . LEU F 2 126 ? 15.625  9.261   -88.865  1.00 60.50  ? 126 LEU F CG  1 
ATOM   11404 C CD1 . LEU F 2 126 ? 14.549  9.836   -87.959  1.00 55.84  ? 126 LEU F CD1 1 
ATOM   11405 C CD2 . LEU F 2 126 ? 15.028  8.774   -90.179  1.00 56.44  ? 126 LEU F CD2 1 
ATOM   11406 N N   . ARG F 2 127 ? 19.869  10.937  -89.575  1.00 62.26  ? 127 ARG F N   1 
ATOM   11407 C CA  . ARG F 2 127 ? 20.949  11.934  -89.660  1.00 62.56  ? 127 ARG F CA  1 
ATOM   11408 C C   . ARG F 2 127 ? 20.306  13.315  -89.544  1.00 62.71  ? 127 ARG F C   1 
ATOM   11409 O O   . ARG F 2 127 ? 19.541  13.549  -88.594  1.00 66.19  ? 127 ARG F O   1 
ATOM   11410 C CB  . ARG F 2 127 ? 21.771  11.693  -90.924  1.00 71.26  ? 127 ARG F CB  1 
ATOM   11411 C CG  . ARG F 2 127 ? 21.948  10.225  -91.296  1.00 73.15  ? 127 ARG F CG  1 
ATOM   11412 C CD  . ARG F 2 127 ? 23.414  9.856   -91.459  1.00 82.14  ? 127 ARG F CD  1 
ATOM   11413 N NE  . ARG F 2 127 ? 24.101  10.734  -92.400  1.00 75.43  ? 127 ARG F NE  1 
ATOM   11414 C CZ  . ARG F 2 127 ? 24.293  10.456  -93.682  1.00 86.62  ? 127 ARG F CZ  1 
ATOM   11415 N NH1 . ARG F 2 127 ? 23.873  9.318   -94.214  1.00 77.91  ? 127 ARG F NH1 1 
ATOM   11416 N NH2 . ARG F 2 127 ? 24.924  11.339  -94.450  1.00 86.47  ? 127 ARG F NH2 1 
ATOM   11417 N N   . ASP F 2 128 ? 20.573  14.245  -90.459  1.00 63.67  ? 128 ASP F N   1 
ATOM   11418 C CA  . ASP F 2 128 ? 19.983  15.576  -90.409  1.00 64.40  ? 128 ASP F CA  1 
ATOM   11419 C C   . ASP F 2 128 ? 18.699  15.689  -91.225  1.00 65.45  ? 128 ASP F C   1 
ATOM   11420 O O   . ASP F 2 128 ? 18.154  16.790  -91.348  1.00 69.66  ? 128 ASP F O   1 
ATOM   11421 C CB  . ASP F 2 128 ? 20.999  16.627  -90.874  1.00 62.63  ? 128 ASP F CB  1 
ATOM   11422 C CG  . ASP F 2 128 ? 21.593  16.313  -92.234  1.00 82.46  ? 128 ASP F CG  1 
ATOM   11423 O OD1 . ASP F 2 128 ? 21.144  15.343  -92.877  1.00 82.00  ? 128 ASP F OD1 1 
ATOM   11424 O OD2 . ASP F 2 128 ? 22.516  17.040  -92.657  1.00 82.73  ? 128 ASP F OD2 1 
ATOM   11425 N N   . ASN F 2 129 ? 18.206  14.582  -91.787  1.00 58.44  ? 129 ASN F N   1 
ATOM   11426 C CA  . ASN F 2 129 ? 16.894  14.587  -92.425  1.00 60.50  ? 129 ASN F CA  1 
ATOM   11427 C C   . ASN F 2 129 ? 15.757  14.755  -91.427  1.00 60.82  ? 129 ASN F C   1 
ATOM   11428 O O   . ASN F 2 129 ? 14.618  14.989  -91.846  1.00 59.82  ? 129 ASN F O   1 
ATOM   11429 C CB  . ASN F 2 129 ? 16.679  13.296  -93.217  1.00 53.87  ? 129 ASN F CB  1 
ATOM   11430 C CG  . ASN F 2 129 ? 17.306  13.345  -94.593  1.00 67.81  ? 129 ASN F CG  1 
ATOM   11431 O OD1 . ASN F 2 129 ? 17.974  14.315  -94.949  1.00 64.49  ? 129 ASN F OD1 1 
ATOM   11432 N ND2 . ASN F 2 129 ? 17.096  12.293  -95.376  1.00 56.75  ? 129 ASN F ND2 1 
ATOM   11433 N N   . ALA F 2 130 ? 16.031  14.625  -90.131  1.00 64.14  ? 130 ALA F N   1 
ATOM   11434 C CA  . ALA F 2 130 ? 15.020  14.779  -89.099  1.00 62.29  ? 130 ALA F CA  1 
ATOM   11435 C C   . ALA F 2 130 ? 15.622  15.519  -87.915  1.00 60.67  ? 130 ALA F C   1 
ATOM   11436 O O   . ALA F 2 130 ? 16.842  15.650  -87.789  1.00 66.08  ? 130 ALA F O   1 
ATOM   11437 C CB  . ALA F 2 130 ? 14.454  13.426  -88.648  1.00 55.10  ? 130 ALA F CB  1 
ATOM   11438 N N   . LYS F 2 131 ? 14.743  16.004  -87.043  1.00 55.13  ? 131 LYS F N   1 
ATOM   11439 C CA  . LYS F 2 131 ? 15.126  16.783  -85.874  1.00 58.89  ? 131 LYS F CA  1 
ATOM   11440 C C   . LYS F 2 131 ? 14.715  16.041  -84.608  1.00 61.23  ? 131 LYS F C   1 
ATOM   11441 O O   . LYS F 2 131 ? 13.587  15.547  -84.514  1.00 67.01  ? 131 LYS F O   1 
ATOM   11442 C CB  . LYS F 2 131 ? 14.484  18.174  -85.917  1.00 56.79  ? 131 LYS F CB  1 
ATOM   11443 C CG  . LYS F 2 131 ? 14.025  18.697  -84.561  1.00 71.37  ? 131 LYS F CG  1 
ATOM   11444 C CD  . LYS F 2 131 ? 13.631  20.168  -84.610  1.00 80.43  ? 131 LYS F CD  1 
ATOM   11445 C CE  . LYS F 2 131 ? 12.526  20.456  -85.615  1.00 79.59  ? 131 LYS F CE  1 
ATOM   11446 N NZ  . LYS F 2 131 ? 12.164  21.898  -85.560  1.00 87.77  ? 131 LYS F NZ  1 
ATOM   11447 N N   . GLU F 2 132 ? 15.630  15.962  -83.642  1.00 72.91  ? 132 GLU F N   1 
ATOM   11448 C CA  . GLU F 2 132 ? 15.341  15.330  -82.361  1.00 67.15  ? 132 GLU F CA  1 
ATOM   11449 C C   . GLU F 2 132 ? 14.546  16.292  -81.489  1.00 65.42  ? 132 GLU F C   1 
ATOM   11450 O O   . GLU F 2 132 ? 14.990  17.416  -81.233  1.00 78.34  ? 132 GLU F O   1 
ATOM   11451 C CB  . GLU F 2 132 ? 16.629  14.920  -81.653  1.00 73.28  ? 132 GLU F CB  1 
ATOM   11452 C CG  . GLU F 2 132 ? 17.474  13.904  -82.391  1.00 90.54  ? 132 GLU F CG  1 
ATOM   11453 C CD  . GLU F 2 132 ? 18.666  13.453  -81.570  1.00 99.57  ? 132 GLU F CD  1 
ATOM   11454 O OE1 . GLU F 2 132 ? 18.456  12.866  -80.487  1.00 89.81  ? 132 GLU F OE1 1 
ATOM   11455 O OE2 . GLU F 2 132 ? 19.813  13.703  -81.996  1.00 91.17  ? 132 GLU F OE2 1 
ATOM   11456 N N   . LEU F 2 133 ? 13.376  15.854  -81.028  1.00 61.72  ? 133 LEU F N   1 
ATOM   11457 C CA  . LEU F 2 133 ? 12.542  16.697  -80.181  1.00 67.50  ? 133 LEU F CA  1 
ATOM   11458 C C   . LEU F 2 133 ? 12.915  16.617  -78.707  1.00 69.72  ? 133 LEU F C   1 
ATOM   11459 O O   . LEU F 2 133 ? 12.449  17.450  -77.924  1.00 71.23  ? 133 LEU F O   1 
ATOM   11460 C CB  . LEU F 2 133 ? 11.069  16.322  -80.360  1.00 69.33  ? 133 LEU F CB  1 
ATOM   11461 C CG  . LEU F 2 133 ? 10.558  16.325  -81.802  1.00 65.77  ? 133 LEU F CG  1 
ATOM   11462 C CD1 . LEU F 2 133 ? 9.071   16.021  -81.842  1.00 76.96  ? 133 LEU F CD1 1 
ATOM   11463 C CD2 . LEU F 2 133 ? 10.860  17.653  -82.479  1.00 58.00  ? 133 LEU F CD2 1 
ATOM   11464 N N   . GLY F 2 134 ? 13.741  15.649  -78.314  1.00 79.27  ? 134 GLY F N   1 
ATOM   11465 C CA  . GLY F 2 134 ? 14.149  15.505  -76.934  1.00 80.57  ? 134 GLY F CA  1 
ATOM   11466 C C   . GLY F 2 134 ? 13.180  14.758  -76.045  1.00 87.87  ? 134 GLY F C   1 
ATOM   11467 O O   . GLY F 2 134 ? 13.452  14.615  -74.846  1.00 90.92  ? 134 GLY F O   1 
ATOM   11468 N N   . ASN F 2 135 ? 12.056  14.288  -76.582  1.00 88.41  ? 135 ASN F N   1 
ATOM   11469 C CA  . ASN F 2 135 ? 11.097  13.496  -75.824  1.00 63.72  ? 135 ASN F CA  1 
ATOM   11470 C C   . ASN F 2 135 ? 11.083  12.038  -76.259  1.00 71.62  ? 135 ASN F C   1 
ATOM   11471 O O   . ASN F 2 135 ? 10.219  11.277  -75.814  1.00 80.41  ? 135 ASN F O   1 
ATOM   11472 C CB  . ASN F 2 135 ? 9.695   14.098  -75.954  1.00 83.13  ? 135 ASN F CB  1 
ATOM   11473 C CG  . ASN F 2 135 ? 9.200   14.121  -77.388  1.00 92.42  ? 135 ASN F CG  1 
ATOM   11474 O OD1 . ASN F 2 135 ? 9.978   13.963  -78.329  1.00 77.41  ? 135 ASN F OD1 1 
ATOM   11475 N ND2 . ASN F 2 135 ? 7.899   14.324  -77.562  1.00 107.44 ? 135 ASN F ND2 1 
ATOM   11476 N N   . GLY F 2 136 ? 12.025  11.630  -77.107  1.00 73.98  ? 136 GLY F N   1 
ATOM   11477 C CA  . GLY F 2 136 ? 12.028  10.307  -77.692  1.00 67.49  ? 136 GLY F CA  1 
ATOM   11478 C C   . GLY F 2 136 ? 11.464  10.239  -79.093  1.00 74.57  ? 136 GLY F C   1 
ATOM   11479 O O   . GLY F 2 136 ? 11.342  9.136   -79.640  1.00 70.65  ? 136 GLY F O   1 
ATOM   11480 N N   . CYS F 2 137 ? 11.123  11.378  -79.691  1.00 70.25  ? 137 CYS F N   1 
ATOM   11481 C CA  . CYS F 2 137 ? 10.504  11.430  -81.005  1.00 80.48  ? 137 CYS F CA  1 
ATOM   11482 C C   . CYS F 2 137 ? 11.387  12.204  -81.974  1.00 74.04  ? 137 CYS F C   1 
ATOM   11483 O O   . CYS F 2 137 ? 12.188  13.054  -81.571  1.00 63.44  ? 137 CYS F O   1 
ATOM   11484 C CB  . CYS F 2 137 ? 9.118   12.089  -80.947  1.00 85.85  ? 137 CYS F CB  1 
ATOM   11485 S SG  . CYS F 2 137 ? 7.885   11.240  -79.934  1.00 96.76  ? 137 CYS F SG  1 
ATOM   11486 N N   . PHE F 2 138 ? 11.229  11.898  -83.258  1.00 76.79  ? 138 PHE F N   1 
ATOM   11487 C CA  . PHE F 2 138 ? 11.915  12.597  -84.336  1.00 71.25  ? 138 PHE F CA  1 
ATOM   11488 C C   . PHE F 2 138 ? 10.878  13.242  -85.243  1.00 57.13  ? 138 PHE F C   1 
ATOM   11489 O O   . PHE F 2 138 ? 9.929   12.578  -85.672  1.00 60.12  ? 138 PHE F O   1 
ATOM   11490 C CB  . PHE F 2 138 ? 12.789  11.642  -85.153  1.00 60.60  ? 138 PHE F CB  1 
ATOM   11491 C CG  . PHE F 2 138 ? 13.863  10.963  -84.356  1.00 76.46  ? 138 PHE F CG  1 
ATOM   11492 C CD1 . PHE F 2 138 ? 13.588  9.814   -83.635  1.00 74.27  ? 138 PHE F CD1 1 
ATOM   11493 C CD2 . PHE F 2 138 ? 15.154  11.461  -84.347  1.00 75.49  ? 138 PHE F CD2 1 
ATOM   11494 C CE1 . PHE F 2 138 ? 14.577  9.183   -82.910  1.00 70.57  ? 138 PHE F CE1 1 
ATOM   11495 C CE2 . PHE F 2 138 ? 16.149  10.833  -83.624  1.00 64.56  ? 138 PHE F CE2 1 
ATOM   11496 C CZ  . PHE F 2 138 ? 15.860  9.692   -82.906  1.00 74.84  ? 138 PHE F CZ  1 
ATOM   11497 N N   . GLU F 2 139 ? 11.058  14.526  -85.536  1.00 65.63  ? 139 GLU F N   1 
ATOM   11498 C CA  . GLU F 2 139 ? 10.233  15.224  -86.513  1.00 64.86  ? 139 GLU F CA  1 
ATOM   11499 C C   . GLU F 2 139 ? 10.974  15.242  -87.844  1.00 64.39  ? 139 GLU F C   1 
ATOM   11500 O O   . GLU F 2 139 ? 12.104  15.736  -87.922  1.00 62.95  ? 139 GLU F O   1 
ATOM   11501 C CB  . GLU F 2 139 ? 9.913   16.648  -86.060  1.00 71.47  ? 139 GLU F CB  1 
ATOM   11502 C CG  . GLU F 2 139 ? 9.035   17.409  -87.041  1.00 69.82  ? 139 GLU F CG  1 
ATOM   11503 C CD  . GLU F 2 139 ? 8.756   18.832  -86.601  1.00 101.17 ? 139 GLU F CD  1 
ATOM   11504 O OE1 . GLU F 2 139 ? 9.056   19.167  -85.436  1.00 92.43  ? 139 GLU F OE1 1 
ATOM   11505 O OE2 . GLU F 2 139 ? 8.238   19.618  -87.423  1.00 99.37  ? 139 GLU F OE2 1 
ATOM   11506 N N   . PHE F 2 140 ? 10.341  14.702  -88.882  1.00 64.80  ? 140 PHE F N   1 
ATOM   11507 C CA  . PHE F 2 140 ? 10.974  14.606  -90.190  1.00 64.78  ? 140 PHE F CA  1 
ATOM   11508 C C   . PHE F 2 140 ? 10.993  15.963  -90.882  1.00 64.05  ? 140 PHE F C   1 
ATOM   11509 O O   . PHE F 2 140 ? 9.972   16.655  -90.943  1.00 62.74  ? 140 PHE F O   1 
ATOM   11510 C CB  . PHE F 2 140 ? 10.240  13.586  -91.060  1.00 57.78  ? 140 PHE F CB  1 
ATOM   11511 C CG  . PHE F 2 140 ? 10.493  12.160  -90.673  1.00 65.43  ? 140 PHE F CG  1 
ATOM   11512 C CD1 . PHE F 2 140 ? 11.600  11.487  -91.159  1.00 56.71  ? 140 PHE F CD1 1 
ATOM   11513 C CD2 . PHE F 2 140 ? 9.622   11.489  -89.831  1.00 60.20  ? 140 PHE F CD2 1 
ATOM   11514 C CE1 . PHE F 2 140 ? 11.837  10.173  -90.811  1.00 69.98  ? 140 PHE F CE1 1 
ATOM   11515 C CE2 . PHE F 2 140 ? 9.853   10.171  -89.479  1.00 57.63  ? 140 PHE F CE2 1 
ATOM   11516 C CZ  . PHE F 2 140 ? 10.963  9.513   -89.969  1.00 64.27  ? 140 PHE F CZ  1 
ATOM   11517 N N   . TYR F 2 141 ? 12.158  16.340  -91.412  1.00 68.65  ? 141 TYR F N   1 
ATOM   11518 C CA  . TYR F 2 141 ? 12.283  17.534  -92.251  1.00 60.48  ? 141 TYR F CA  1 
ATOM   11519 C C   . TYR F 2 141 ? 11.715  17.325  -93.662  1.00 59.05  ? 141 TYR F C   1 
ATOM   11520 O O   . TYR F 2 141 ? 11.862  18.169  -94.558  1.00 75.31  ? 141 TYR F O   1 
ATOM   11521 C CB  . TYR F 2 141 ? 13.749  17.964  -92.343  1.00 67.06  ? 141 TYR F CB  1 
ATOM   11522 C CG  . TYR F 2 141 ? 14.267  18.693  -91.126  1.00 64.31  ? 141 TYR F CG  1 
ATOM   11523 C CD1 . TYR F 2 141 ? 13.488  19.643  -90.477  1.00 53.02  ? 141 TYR F CD1 1 
ATOM   11524 C CD2 . TYR F 2 141 ? 15.535  18.429  -90.625  1.00 59.57  ? 141 TYR F CD2 1 
ATOM   11525 C CE1 . TYR F 2 141 ? 13.961  20.312  -89.363  1.00 64.80  ? 141 TYR F CE1 1 
ATOM   11526 C CE2 . TYR F 2 141 ? 16.014  19.091  -89.513  1.00 55.44  ? 141 TYR F CE2 1 
ATOM   11527 C CZ  . TYR F 2 141 ? 15.224  20.031  -88.887  1.00 60.47  ? 141 TYR F CZ  1 
ATOM   11528 O OH  . TYR F 2 141 ? 15.707  20.687  -87.780  1.00 76.34  ? 141 TYR F OH  1 
ATOM   11529 N N   . HIS F 2 142 ? 11.072  16.182  -93.878  1.00 60.84  ? 142 HIS F N   1 
ATOM   11530 C CA  . HIS F 2 142 ? 10.448  15.870  -95.152  1.00 57.32  ? 142 HIS F CA  1 
ATOM   11531 C C   . HIS F 2 142 ? 9.205   15.033  -94.890  1.00 68.98  ? 142 HIS F C   1 
ATOM   11532 O O   . HIS F 2 142 ? 8.917   14.645  -93.757  1.00 86.03  ? 142 HIS F O   1 
ATOM   11533 C CB  . HIS F 2 142 ? 11.410  15.128  -96.084  1.00 51.01  ? 142 HIS F CB  1 
ATOM   11534 C CG  . HIS F 2 142 ? 11.820  13.779  -95.580  1.00 61.83  ? 142 HIS F CG  1 
ATOM   11535 N ND1 . HIS F 2 142 ? 11.065  12.645  -95.790  1.00 61.24  ? 142 HIS F ND1 1 
ATOM   11536 C CD2 . HIS F 2 142 ? 12.904  13.381  -94.872  1.00 65.81  ? 142 HIS F CD2 1 
ATOM   11537 C CE1 . HIS F 2 142 ? 11.667  11.607  -95.238  1.00 66.77  ? 142 HIS F CE1 1 
ATOM   11538 N NE2 . HIS F 2 142 ? 12.785  12.027  -94.675  1.00 65.54  ? 142 HIS F NE2 1 
ATOM   11539 N N   . LYS F 2 143 ? 8.465   14.761  -95.959  1.00 70.72  ? 143 LYS F N   1 
ATOM   11540 C CA  . LYS F 2 143 ? 7.293   13.904  -95.867  1.00 73.50  ? 143 LYS F CA  1 
ATOM   11541 C C   . LYS F 2 143 ? 7.727   12.449  -95.764  1.00 75.82  ? 143 LYS F C   1 
ATOM   11542 O O   . LYS F 2 143 ? 8.500   11.962  -96.593  1.00 73.34  ? 143 LYS F O   1 
ATOM   11543 C CB  . LYS F 2 143 ? 6.390   14.099  -97.080  1.00 70.59  ? 143 LYS F CB  1 
ATOM   11544 C CG  . LYS F 2 143 ? 5.750   15.464  -97.149  1.00 80.80  ? 143 LYS F CG  1 
ATOM   11545 C CD  . LYS F 2 143 ? 4.751   15.669  -96.016  1.00 83.98  ? 143 LYS F CD  1 
ATOM   11546 C CE  . LYS F 2 143 ? 4.033   16.999  -96.212  1.00 76.34  ? 143 LYS F CE  1 
ATOM   11547 N NZ  . LYS F 2 143 ? 3.764   17.186  -97.680  1.00 84.06  ? 143 LYS F NZ  1 
ATOM   11548 N N   . CYS F 2 144 ? 7.231   11.756  -94.743  1.00 69.57  ? 144 CYS F N   1 
ATOM   11549 C CA  . CYS F 2 144 ? 7.538   10.346  -94.517  1.00 81.69  ? 144 CYS F CA  1 
ATOM   11550 C C   . CYS F 2 144 ? 6.210   9.605   -94.414  1.00 67.06  ? 144 CYS F C   1 
ATOM   11551 O O   . CYS F 2 144 ? 5.527   9.684   -93.389  1.00 68.13  ? 144 CYS F O   1 
ATOM   11552 C CB  . CYS F 2 144 ? 8.392   10.168  -93.266  1.00 59.27  ? 144 CYS F CB  1 
ATOM   11553 S SG  . CYS F 2 144 ? 8.968   8.488   -92.944  1.00 106.41 ? 144 CYS F SG  1 
ATOM   11554 N N   . ASP F 2 145 ? 5.841   8.895   -95.479  1.00 67.58  ? 145 ASP F N   1 
ATOM   11555 C CA  . ASP F 2 145 ? 4.574   8.177   -95.520  1.00 75.17  ? 145 ASP F CA  1 
ATOM   11556 C C   . ASP F 2 145 ? 4.712   6.858   -94.762  1.00 81.17  ? 145 ASP F C   1 
ATOM   11557 O O   . ASP F 2 145 ? 5.728   6.588   -94.115  1.00 75.42  ? 145 ASP F O   1 
ATOM   11558 C CB  . ASP F 2 145 ? 4.123   7.976   -96.966  1.00 64.25  ? 145 ASP F CB  1 
ATOM   11559 C CG  . ASP F 2 145 ? 5.025   7.033   -97.746  1.00 84.01  ? 145 ASP F CG  1 
ATOM   11560 O OD1 . ASP F 2 145 ? 6.149   6.744   -97.286  1.00 80.84  ? 145 ASP F OD1 1 
ATOM   11561 O OD2 . ASP F 2 145 ? 4.602   6.574   -98.828  1.00 96.57  ? 145 ASP F OD2 1 
ATOM   11562 N N   . ASN F 2 146 ? 3.680   6.013   -94.840  1.00 72.75  ? 146 ASN F N   1 
ATOM   11563 C CA  . ASN F 2 146 ? 3.694   4.754   -94.101  1.00 60.49  ? 146 ASN F CA  1 
ATOM   11564 C C   . ASN F 2 146 ? 4.825   3.845   -94.570  1.00 63.59  ? 146 ASN F C   1 
ATOM   11565 O O   . ASN F 2 146 ? 5.481   3.188   -93.753  1.00 81.50  ? 146 ASN F O   1 
ATOM   11566 C CB  . ASN F 2 146 ? 2.343   4.052   -94.233  1.00 54.46  ? 146 ASN F CB  1 
ATOM   11567 C CG  . ASN F 2 146 ? 1.239   4.776   -93.486  1.00 66.19  ? 146 ASN F CG  1 
ATOM   11568 O OD1 . ASN F 2 146 ? 1.501   5.560   -92.573  1.00 58.98  ? 146 ASN F OD1 1 
ATOM   11569 N ND2 . ASN F 2 146 ? -0.004  4.512   -93.868  1.00 80.76  ? 146 ASN F ND2 1 
ATOM   11570 N N   . GLU F 2 147 ? 5.068   3.792   -95.882  1.00 66.97  ? 147 GLU F N   1 
ATOM   11571 C CA  . GLU F 2 147 ? 6.183   2.997   -96.388  1.00 72.13  ? 147 GLU F CA  1 
ATOM   11572 C C   . GLU F 2 147 ? 7.520   3.571   -95.934  1.00 81.55  ? 147 GLU F C   1 
ATOM   11573 O O   . GLU F 2 147 ? 8.455   2.818   -95.636  1.00 76.90  ? 147 GLU F O   1 
ATOM   11574 C CB  . GLU F 2 147 ? 6.117   2.904   -97.912  1.00 68.23  ? 147 GLU F CB  1 
ATOM   11575 C CG  . GLU F 2 147 ? 4.984   2.024   -98.423  1.00 109.78 ? 147 GLU F CG  1 
ATOM   11576 C CD  . GLU F 2 147 ? 4.936   1.941   -99.937  1.00 133.88 ? 147 GLU F CD  1 
ATOM   11577 O OE1 . GLU F 2 147 ? 5.945   2.288   -100.586 1.00 128.25 ? 147 GLU F OE1 1 
ATOM   11578 O OE2 . GLU F 2 147 ? 3.886   1.530   -100.477 1.00 120.99 ? 147 GLU F OE2 1 
ATOM   11579 N N   . CYS F 2 148 ? 7.634   4.901   -95.886  1.00 77.23  ? 148 CYS F N   1 
ATOM   11580 C CA  . CYS F 2 148 ? 8.840   5.522   -95.348  1.00 69.42  ? 148 CYS F CA  1 
ATOM   11581 C C   . CYS F 2 148 ? 9.004   5.221   -93.863  1.00 80.56  ? 148 CYS F C   1 
ATOM   11582 O O   . CYS F 2 148 ? 10.118  4.951   -93.399  1.00 66.58  ? 148 CYS F O   1 
ATOM   11583 C CB  . CYS F 2 148 ? 8.808   7.031   -95.590  1.00 75.44  ? 148 CYS F CB  1 
ATOM   11584 S SG  . CYS F 2 148 ? 10.006  7.964   -94.612  1.00 77.64  ? 148 CYS F SG  1 
ATOM   11585 N N   . MET F 2 149 ? 7.905   5.269   -93.102  1.00 73.94  ? 149 MET F N   1 
ATOM   11586 C CA  . MET F 2 149 ? 7.969   4.959   -91.677  1.00 65.22  ? 149 MET F CA  1 
ATOM   11587 C C   . MET F 2 149 ? 8.420   3.522   -91.448  1.00 72.88  ? 149 MET F C   1 
ATOM   11588 O O   . MET F 2 149 ? 9.216   3.250   -90.541  1.00 76.17  ? 149 MET F O   1 
ATOM   11589 C CB  . MET F 2 149 ? 6.609   5.196   -91.019  1.00 58.61  ? 149 MET F CB  1 
ATOM   11590 C CG  . MET F 2 149 ? 6.146   6.642   -91.002  1.00 55.54  ? 149 MET F CG  1 
ATOM   11591 S SD  . MET F 2 149 ? 7.103   7.713   -89.913  1.00 74.67  ? 149 MET F SD  1 
ATOM   11592 C CE  . MET F 2 149 ? 6.097   9.195   -89.960  1.00 71.42  ? 149 MET F CE  1 
ATOM   11593 N N   . GLU F 2 150 ? 7.915   2.588   -92.257  1.00 63.33  ? 150 GLU F N   1 
ATOM   11594 C CA  . GLU F 2 150 ? 8.355   1.201   -92.157  1.00 69.16  ? 150 GLU F CA  1 
ATOM   11595 C C   . GLU F 2 150 ? 9.837   1.060   -92.481  1.00 64.93  ? 150 GLU F C   1 
ATOM   11596 O O   . GLU F 2 150 ? 10.525  0.221   -91.888  1.00 74.22  ? 150 GLU F O   1 
ATOM   11597 C CB  . GLU F 2 150 ? 7.510   0.318   -93.079  1.00 77.76  ? 150 GLU F CB  1 
ATOM   11598 C CG  . GLU F 2 150 ? 8.090   -1.063  -93.365  1.00 87.63  ? 150 GLU F CG  1 
ATOM   11599 C CD  . GLU F 2 150 ? 8.220   -1.930  -92.125  1.00 94.33  ? 150 GLU F CD  1 
ATOM   11600 O OE1 . GLU F 2 150 ? 7.505   -1.675  -91.132  1.00 91.53  ? 150 GLU F OE1 1 
ATOM   11601 O OE2 . GLU F 2 150 ? 9.041   -2.872  -92.148  1.00 81.96  ? 150 GLU F OE2 1 
ATOM   11602 N N   . SER F 2 151 ? 10.349  1.876   -93.406  1.00 64.92  ? 151 SER F N   1 
ATOM   11603 C CA  . SER F 2 151 ? 11.773  1.826   -93.724  1.00 76.46  ? 151 SER F CA  1 
ATOM   11604 C C   . SER F 2 151 ? 12.626  2.278   -92.546  1.00 69.27  ? 151 SER F C   1 
ATOM   11605 O O   . SER F 2 151 ? 13.796  1.893   -92.448  1.00 64.55  ? 151 SER F O   1 
ATOM   11606 C CB  . SER F 2 151 ? 12.077  2.687   -94.949  1.00 57.55  ? 151 SER F CB  1 
ATOM   11607 O OG  . SER F 2 151 ? 12.418  4.008   -94.570  1.00 68.33  ? 151 SER F OG  1 
ATOM   11608 N N   . VAL F 2 152 ? 12.071  3.108   -91.662  1.00 52.91  ? 152 VAL F N   1 
ATOM   11609 C CA  . VAL F 2 152 ? 12.784  3.487   -90.448  1.00 60.37  ? 152 VAL F CA  1 
ATOM   11610 C C   . VAL F 2 152 ? 12.683  2.386   -89.399  1.00 69.12  ? 152 VAL F C   1 
ATOM   11611 O O   . VAL F 2 152 ? 13.637  2.139   -88.652  1.00 61.88  ? 152 VAL F O   1 
ATOM   11612 C CB  . VAL F 2 152 ? 12.252  4.830   -89.911  1.00 66.42  ? 152 VAL F CB  1 
ATOM   11613 C CG1 . VAL F 2 152 ? 13.127  5.331   -88.771  1.00 61.89  ? 152 VAL F CG1 1 
ATOM   11614 C CG2 . VAL F 2 152 ? 12.179  5.859   -91.028  1.00 62.37  ? 152 VAL F CG2 1 
ATOM   11615 N N   . ARG F 2 153 ? 11.531  1.715   -89.319  1.00 70.68  ? 153 ARG F N   1 
ATOM   11616 C CA  . ARG F 2 153 ? 11.357  0.658   -88.326  1.00 63.15  ? 153 ARG F CA  1 
ATOM   11617 C C   . ARG F 2 153 ? 12.275  -0.524  -88.608  1.00 66.32  ? 153 ARG F C   1 
ATOM   11618 O O   . ARG F 2 153 ? 12.907  -1.060  -87.689  1.00 78.00  ? 153 ARG F O   1 
ATOM   11619 C CB  . ARG F 2 153 ? 9.896   0.219   -88.270  1.00 64.72  ? 153 ARG F CB  1 
ATOM   11620 C CG  . ARG F 2 153 ? 9.011   1.179   -87.494  1.00 51.39  ? 153 ARG F CG  1 
ATOM   11621 C CD  . ARG F 2 153 ? 7.639   0.589   -87.246  1.00 52.67  ? 153 ARG F CD  1 
ATOM   11622 N NE  . ARG F 2 153 ? 6.860   0.491   -88.473  1.00 61.36  ? 153 ARG F NE  1 
ATOM   11623 C CZ  . ARG F 2 153 ? 6.022   1.424   -88.902  1.00 77.40  ? 153 ARG F CZ  1 
ATOM   11624 N NH1 . ARG F 2 153 ? 5.823   2.541   -88.220  1.00 77.37  ? 153 ARG F NH1 1 
ATOM   11625 N NH2 . ARG F 2 153 ? 5.366   1.232   -90.043  1.00 87.66  ? 153 ARG F NH2 1 
ATOM   11626 N N   . ASN F 2 154 ? 12.365  -0.952  -89.866  1.00 64.75  ? 154 ASN F N   1 
ATOM   11627 C CA  . ASN F 2 154 ? 13.457  -1.837  -90.235  1.00 62.26  ? 154 ASN F CA  1 
ATOM   11628 C C   . ASN F 2 154 ? 14.656  -0.971  -90.628  1.00 73.40  ? 154 ASN F C   1 
ATOM   11629 O O   . ASN F 2 154 ? 14.624  0.256   -90.508  1.00 88.73  ? 154 ASN F O   1 
ATOM   11630 C CB  . ASN F 2 154 ? 13.028  -2.847  -91.313  1.00 63.17  ? 154 ASN F CB  1 
ATOM   11631 C CG  . ASN F 2 154 ? 12.662  -2.215  -92.663  1.00 86.73  ? 154 ASN F CG  1 
ATOM   11632 O OD1 . ASN F 2 154 ? 12.909  -1.040  -92.921  1.00 89.29  ? 154 ASN F OD1 1 
ATOM   11633 N ND2 . ASN F 2 154 ? 12.064  -3.037  -93.537  1.00 95.64  ? 154 ASN F ND2 1 
ATOM   11634 N N   . GLY F 2 155 ? 15.740  -1.598  -91.067  1.00 62.33  ? 155 GLY F N   1 
ATOM   11635 C CA  . GLY F 2 155 ? 16.968  -0.849  -91.256  1.00 78.77  ? 155 GLY F CA  1 
ATOM   11636 C C   . GLY F 2 155 ? 17.234  -0.374  -92.670  1.00 79.76  ? 155 GLY F C   1 
ATOM   11637 O O   . GLY F 2 155 ? 18.388  -0.361  -93.111  1.00 91.11  ? 155 GLY F O   1 
ATOM   11638 N N   . THR F 2 156 ? 16.189  0.037   -93.391  1.00 77.70  ? 156 THR F N   1 
ATOM   11639 C CA  . THR F 2 156 ? 16.302  0.327   -94.817  1.00 75.72  ? 156 THR F CA  1 
ATOM   11640 C C   . THR F 2 156 ? 15.903  1.762   -95.161  1.00 79.17  ? 156 THR F C   1 
ATOM   11641 O O   . THR F 2 156 ? 15.359  2.012   -96.238  1.00 85.07  ? 156 THR F O   1 
ATOM   11642 C CB  . THR F 2 156 ? 15.459  -0.653  -95.634  1.00 82.13  ? 156 THR F CB  1 
ATOM   11643 O OG1 . THR F 2 156 ? 14.120  -0.155  -95.744  1.00 84.83  ? 156 THR F OG1 1 
ATOM   11644 C CG2 . THR F 2 156 ? 15.422  -2.022  -94.967  1.00 74.97  ? 156 THR F CG2 1 
ATOM   11645 N N   . TYR F 2 157 ? 16.169  2.718   -94.272  1.00 72.38  ? 157 TYR F N   1 
ATOM   11646 C CA  . TYR F 2 157 ? 15.835  4.110   -94.551  1.00 63.32  ? 157 TYR F CA  1 
ATOM   11647 C C   . TYR F 2 157 ? 16.824  4.696   -95.554  1.00 67.57  ? 157 TYR F C   1 
ATOM   11648 O O   . TYR F 2 157 ? 18.041  4.587   -95.376  1.00 73.53  ? 157 TYR F O   1 
ATOM   11649 C CB  . TYR F 2 157 ? 15.826  4.936   -93.265  1.00 69.51  ? 157 TYR F CB  1 
ATOM   11650 C CG  . TYR F 2 157 ? 15.612  6.417   -93.494  1.00 63.55  ? 157 TYR F CG  1 
ATOM   11651 C CD1 . TYR F 2 157 ? 14.350  6.921   -93.786  1.00 54.91  ? 157 TYR F CD1 1 
ATOM   11652 C CD2 . TYR F 2 157 ? 16.672  7.311   -93.414  1.00 58.35  ? 157 TYR F CD2 1 
ATOM   11653 C CE1 . TYR F 2 157 ? 14.152  8.276   -93.996  1.00 59.12  ? 157 TYR F CE1 1 
ATOM   11654 C CE2 . TYR F 2 157 ? 16.484  8.666   -93.621  1.00 65.11  ? 157 TYR F CE2 1 
ATOM   11655 C CZ  . TYR F 2 157 ? 15.224  9.143   -93.912  1.00 57.88  ? 157 TYR F CZ  1 
ATOM   11656 O OH  . TYR F 2 157 ? 15.035  10.491  -94.118  1.00 57.99  ? 157 TYR F OH  1 
ATOM   11657 N N   . ASP F 2 158 ? 16.295  5.324   -96.604  1.00 74.47  ? 158 ASP F N   1 
ATOM   11658 C CA  . ASP F 2 158 ? 17.093  5.829   -97.723  1.00 75.70  ? 158 ASP F CA  1 
ATOM   11659 C C   . ASP F 2 158 ? 17.318  7.325   -97.515  1.00 72.60  ? 158 ASP F C   1 
ATOM   11660 O O   . ASP F 2 158 ? 16.498  8.155   -97.907  1.00 69.14  ? 158 ASP F O   1 
ATOM   11661 C CB  . ASP F 2 158 ? 16.391  5.537   -99.047  1.00 77.26  ? 158 ASP F CB  1 
ATOM   11662 C CG  . ASP F 2 158 ? 17.302  5.702   -100.253 1.00 84.90  ? 158 ASP F CG  1 
ATOM   11663 O OD1 . ASP F 2 158 ? 18.287  6.463   -100.167 1.00 86.82  ? 158 ASP F OD1 1 
ATOM   11664 O OD2 . ASP F 2 158 ? 17.026  5.071   -101.295 1.00 99.19  ? 158 ASP F OD2 1 
ATOM   11665 N N   . TYR F 2 159 ? 18.449  7.668   -96.893  1.00 65.15  ? 159 TYR F N   1 
ATOM   11666 C CA  . TYR F 2 159 ? 18.754  9.074   -96.629  1.00 67.98  ? 159 TYR F CA  1 
ATOM   11667 C C   . TYR F 2 159 ? 18.884  9.913   -97.896  1.00 72.80  ? 159 TYR F C   1 
ATOM   11668 O O   . TYR F 2 159 ? 18.219  10.960  -97.982  1.00 59.48  ? 159 TYR F O   1 
ATOM   11669 C CB  . TYR F 2 159 ? 20.017  9.174   -95.763  1.00 60.03  ? 159 TYR F CB  1 
ATOM   11670 C CG  . TYR F 2 159 ? 20.536  10.588  -95.579  1.00 70.24  ? 159 TYR F CG  1 
ATOM   11671 C CD1 . TYR F 2 159 ? 21.420  11.156  -96.492  1.00 62.34  ? 159 TYR F CD1 1 
ATOM   11672 C CD2 . TYR F 2 159 ? 20.147  11.353  -94.487  1.00 65.26  ? 159 TYR F CD2 1 
ATOM   11673 C CE1 . TYR F 2 159 ? 21.891  12.445  -96.329  1.00 55.34  ? 159 TYR F CE1 1 
ATOM   11674 C CE2 . TYR F 2 159 ? 20.617  12.642  -94.314  1.00 68.80  ? 159 TYR F CE2 1 
ATOM   11675 C CZ  . TYR F 2 159 ? 21.488  13.183  -95.238  1.00 61.83  ? 159 TYR F CZ  1 
ATOM   11676 O OH  . TYR F 2 159 ? 21.958  14.465  -95.072  1.00 67.67  ? 159 TYR F OH  1 
ATOM   11677 N N   . PRO F 2 160 ? 19.698  9.547   -98.895  1.00 73.35  ? 160 PRO F N   1 
ATOM   11678 C CA  . PRO F 2 160 ? 19.871  10.446  -100.050 1.00 76.27  ? 160 PRO F CA  1 
ATOM   11679 C C   . PRO F 2 160 ? 18.602  10.676  -100.851 1.00 67.37  ? 160 PRO F C   1 
ATOM   11680 O O   . PRO F 2 160 ? 18.537  11.654  -101.607 1.00 68.77  ? 160 PRO F O   1 
ATOM   11681 C CB  . PRO F 2 160 ? 20.944  9.742   -100.892 1.00 71.24  ? 160 PRO F CB  1 
ATOM   11682 C CG  . PRO F 2 160 ? 20.886  8.322   -100.472 1.00 66.97  ? 160 PRO F CG  1 
ATOM   11683 C CD  . PRO F 2 160 ? 20.554  8.352   -99.017  1.00 61.91  ? 160 PRO F CD  1 
ATOM   11684 N N   . GLN F 2 161 ? 17.598  9.805   -100.726 1.00 58.19  ? 161 GLN F N   1 
ATOM   11685 C CA  . GLN F 2 161 ? 16.351  10.009  -101.455 1.00 52.57  ? 161 GLN F CA  1 
ATOM   11686 C C   . GLN F 2 161 ? 15.639  11.276  -100.997 1.00 66.54  ? 161 GLN F C   1 
ATOM   11687 O O   . GLN F 2 161 ? 15.137  12.049  -101.823 1.00 68.16  ? 161 GLN F O   1 
ATOM   11688 C CB  . GLN F 2 161 ? 15.443  8.790   -101.288 1.00 61.64  ? 161 GLN F CB  1 
ATOM   11689 C CG  . GLN F 2 161 ? 14.055  8.960   -101.886 1.00 65.84  ? 161 GLN F CG  1 
ATOM   11690 C CD  . GLN F 2 161 ? 13.249  7.674   -101.870 1.00 87.76  ? 161 GLN F CD  1 
ATOM   11691 O OE1 . GLN F 2 161 ? 13.808  6.578   -101.847 1.00 104.38 ? 161 GLN F OE1 1 
ATOM   11692 N NE2 . GLN F 2 161 ? 11.927  7.803   -101.881 1.00 101.34 ? 161 GLN F NE2 1 
ATOM   11693 N N   . TYR F 2 162 ? 15.586  11.510  -99.687  1.00 55.04  ? 162 TYR F N   1 
ATOM   11694 C CA  . TYR F 2 162 ? 14.862  12.644  -99.128  1.00 47.96  ? 162 TYR F CA  1 
ATOM   11695 C C   . TYR F 2 162 ? 15.761  13.821  -98.772  1.00 49.18  ? 162 TYR F C   1 
ATOM   11696 O O   . TYR F 2 162 ? 15.261  14.823  -98.252  1.00 50.06  ? 162 TYR F O   1 
ATOM   11697 C CB  . TYR F 2 162 ? 14.085  12.214  -97.880  1.00 55.83  ? 162 TYR F CB  1 
ATOM   11698 C CG  . TYR F 2 162 ? 13.373  10.887  -98.002  1.00 68.21  ? 162 TYR F CG  1 
ATOM   11699 C CD1 . TYR F 2 162 ? 13.929  9.731   -97.472  1.00 69.34  ? 162 TYR F CD1 1 
ATOM   11700 C CD2 . TYR F 2 162 ? 12.141  10.789  -98.635  1.00 61.60  ? 162 TYR F CD2 1 
ATOM   11701 C CE1 . TYR F 2 162 ? 13.284  8.515   -97.575  1.00 75.31  ? 162 TYR F CE1 1 
ATOM   11702 C CE2 . TYR F 2 162 ? 11.487  9.575   -98.743  1.00 66.65  ? 162 TYR F CE2 1 
ATOM   11703 C CZ  . TYR F 2 162 ? 12.065  8.442   -98.211  1.00 84.80  ? 162 TYR F CZ  1 
ATOM   11704 O OH  . TYR F 2 162 ? 11.424  7.228   -98.311  1.00 97.75  ? 162 TYR F OH  1 
ATOM   11705 N N   . SER F 2 163 ? 17.069  13.727  -99.031  1.00 55.76  ? 163 SER F N   1 
ATOM   11706 C CA  . SER F 2 163 ? 17.997  14.745  -98.544  1.00 51.03  ? 163 SER F CA  1 
ATOM   11707 C C   . SER F 2 163 ? 17.712  16.110  -99.160  1.00 60.33  ? 163 SER F C   1 
ATOM   11708 O O   . SER F 2 163 ? 17.770  17.134  -98.468  1.00 58.42  ? 163 SER F O   1 
ATOM   11709 C CB  . SER F 2 163 ? 19.438  14.317  -98.825  1.00 52.85  ? 163 SER F CB  1 
ATOM   11710 O OG  . SER F 2 163 ? 19.669  14.174  -100.215 1.00 74.82  ? 163 SER F OG  1 
ATOM   11711 N N   . GLU F 2 164 ? 17.407  16.147  -100.459 1.00 60.76  ? 164 GLU F N   1 
ATOM   11712 C CA  . GLU F 2 164 ? 17.143  17.422  -101.122 1.00 58.19  ? 164 GLU F CA  1 
ATOM   11713 C C   . GLU F 2 164 ? 15.896  18.091  -100.554 1.00 65.12  ? 164 GLU F C   1 
ATOM   11714 O O   . GLU F 2 164 ? 15.895  19.297  -100.282 1.00 67.72  ? 164 GLU F O   1 
ATOM   11715 C CB  . GLU F 2 164 ? 17.003  17.209  -102.629 1.00 73.66  ? 164 GLU F CB  1 
ATOM   11716 C CG  . GLU F 2 164 ? 16.751  18.485  -103.414 1.00 67.62  ? 164 GLU F CG  1 
ATOM   11717 C CD  . GLU F 2 164 ? 16.650  18.239  -104.908 1.00 87.69  ? 164 GLU F CD  1 
ATOM   11718 O OE1 . GLU F 2 164 ? 17.207  17.227  -105.385 1.00 82.38  ? 164 GLU F OE1 1 
ATOM   11719 O OE2 . GLU F 2 164 ? 16.009  19.055  -105.605 1.00 77.05  ? 164 GLU F OE2 1 
ATOM   11720 N N   . GLU F 2 165 ? 14.818  17.322  -100.377 1.00 71.33  ? 165 GLU F N   1 
ATOM   11721 C CA  . GLU F 2 165 ? 13.614  17.873  -99.766  1.00 43.82  ? 165 GLU F CA  1 
ATOM   11722 C C   . GLU F 2 165 ? 13.860  18.257  -98.313  1.00 57.28  ? 165 GLU F C   1 
ATOM   11723 O O   . GLU F 2 165 ? 13.401  19.311  -97.855  1.00 54.63  ? 165 GLU F O   1 
ATOM   11724 C CB  . GLU F 2 165 ? 12.464  16.871  -99.866  1.00 61.78  ? 165 GLU F CB  1 
ATOM   11725 C CG  . GLU F 2 165 ? 11.188  17.328  -99.172  1.00 59.76  ? 165 GLU F CG  1 
ATOM   11726 C CD  . GLU F 2 165 ? 10.087  16.287  -99.225  1.00 74.32  ? 165 GLU F CD  1 
ATOM   11727 O OE1 . GLU F 2 165 ? 10.290  15.240  -99.876  1.00 64.66  ? 165 GLU F OE1 1 
ATOM   11728 O OE2 . GLU F 2 165 ? 9.019   16.516  -98.616  1.00 65.04  ? 165 GLU F OE2 1 
ATOM   11729 N N   . ALA F 2 166 ? 14.577  17.409  -97.571  1.00 59.50  ? 166 ALA F N   1 
ATOM   11730 C CA  . ALA F 2 166 ? 14.862  17.705  -96.170  1.00 59.30  ? 166 ALA F CA  1 
ATOM   11731 C C   . ALA F 2 166 ? 15.720  18.953  -96.034  1.00 53.31  ? 166 ALA F C   1 
ATOM   11732 O O   . ALA F 2 166 ? 15.522  19.752  -95.111  1.00 65.17  ? 166 ALA F O   1 
ATOM   11733 C CB  . ALA F 2 166 ? 15.546  16.511  -95.506  1.00 49.22  ? 166 ALA F CB  1 
ATOM   11734 N N   . ARG F 2 167 ? 16.692  19.132  -96.932  1.00 61.15  ? 167 ARG F N   1 
ATOM   11735 C CA  . ARG F 2 167 ? 17.565  20.297  -96.841  1.00 57.80  ? 167 ARG F CA  1 
ATOM   11736 C C   . ARG F 2 167 ? 16.782  21.591  -97.042  1.00 57.10  ? 167 ARG F C   1 
ATOM   11737 O O   . ARG F 2 167 ? 16.947  22.552  -96.282  1.00 64.07  ? 167 ARG F O   1 
ATOM   11738 C CB  . ARG F 2 167 ? 18.706  20.186  -97.855  1.00 68.13  ? 167 ARG F CB  1 
ATOM   11739 C CG  . ARG F 2 167 ? 19.802  21.224  -97.661  1.00 59.61  ? 167 ARG F CG  1 
ATOM   11740 C CD  . ARG F 2 167 ? 21.009  20.939  -98.544  1.00 73.40  ? 167 ARG F CD  1 
ATOM   11741 N NE  . ARG F 2 167 ? 21.149  19.521  -98.855  1.00 102.80 ? 167 ARG F NE  1 
ATOM   11742 C CZ  . ARG F 2 167 ? 21.141  19.021  -100.084 1.00 115.26 ? 167 ARG F CZ  1 
ATOM   11743 N NH1 . ARG F 2 167 ? 21.034  19.802  -101.147 1.00 113.06 ? 167 ARG F NH1 1 
ATOM   11744 N NH2 . ARG F 2 167 ? 21.252  17.706  -100.252 1.00 96.51  ? 167 ARG F NH2 1 
ATOM   11745 N N   . LEU F 2 168 ? 15.905  21.626  -98.050  1.00 62.19  ? 168 LEU F N   1 
ATOM   11746 C CA  . LEU F 2 168 ? 15.138  22.840  -98.328  1.00 60.12  ? 168 LEU F CA  1 
ATOM   11747 C C   . LEU F 2 168 ? 14.280  23.247  -97.134  1.00 61.59  ? 168 LEU F C   1 
ATOM   11748 O O   . LEU F 2 168 ? 14.246  24.425  -96.757  1.00 71.61  ? 168 LEU F O   1 
ATOM   11749 C CB  . LEU F 2 168 ? 14.259  22.632  -99.563  1.00 64.18  ? 168 LEU F CB  1 
ATOM   11750 C CG  . LEU F 2 168 ? 14.857  22.991  -100.922 1.00 58.29  ? 168 LEU F CG  1 
ATOM   11751 C CD1 . LEU F 2 168 ? 14.144  22.224  -102.022 1.00 60.36  ? 168 LEU F CD1 1 
ATOM   11752 C CD2 . LEU F 2 168 ? 14.758  24.490  -101.166 1.00 60.56  ? 168 LEU F CD2 1 
ATOM   11753 N N   . LYS F 2 169 ? 13.584  22.287  -96.521  1.00 58.74  ? 169 LYS F N   1 
ATOM   11754 C CA  . LYS F 2 169 ? 12.734  22.597  -95.380  1.00 67.85  ? 169 LYS F CA  1 
ATOM   11755 C C   . LYS F 2 169 ? 13.526  22.842  -94.104  1.00 60.56  ? 169 LYS F C   1 
ATOM   11756 O O   . LYS F 2 169 ? 13.021  23.519  -93.203  1.00 73.73  ? 169 LYS F O   1 
ATOM   11757 C CB  . LYS F 2 169 ? 11.724  21.471  -95.160  1.00 55.96  ? 169 LYS F CB  1 
ATOM   11758 C CG  . LYS F 2 169 ? 10.561  21.500  -96.139  1.00 77.56  ? 169 LYS F CG  1 
ATOM   11759 C CD  . LYS F 2 169 ? 10.314  20.142  -96.768  1.00 77.87  ? 169 LYS F CD  1 
ATOM   11760 C CE  . LYS F 2 169 ? 8.871   19.715  -96.548  1.00 67.33  ? 169 LYS F CE  1 
ATOM   11761 N NZ  . LYS F 2 169 ? 8.434   18.591  -97.426  1.00 69.63  ? 169 LYS F NZ  1 
ATOM   11762 N N   . ARG F 2 170 ? 14.750  22.313  -94.003  1.00 63.90  ? 170 ARG F N   1 
ATOM   11763 C CA  . ARG F 2 170 ? 15.560  22.566  -92.815  1.00 67.05  ? 170 ARG F CA  1 
ATOM   11764 C C   . ARG F 2 170 ? 16.021  24.016  -92.763  1.00 76.14  ? 170 ARG F C   1 
ATOM   11765 O O   . ARG F 2 170 ? 16.090  24.611  -91.683  1.00 74.31  ? 170 ARG F O   1 
ATOM   11766 C CB  . ARG F 2 170 ? 16.758  21.615  -92.778  1.00 58.55  ? 170 ARG F CB  1 
ATOM   11767 C CG  . ARG F 2 170 ? 17.574  21.697  -91.489  1.00 60.83  ? 170 ARG F CG  1 
ATOM   11768 C CD  . ARG F 2 170 ? 18.640  20.607  -91.406  1.00 55.80  ? 170 ARG F CD  1 
ATOM   11769 N NE  . ARG F 2 170 ? 19.588  20.660  -92.514  1.00 58.37  ? 170 ARG F NE  1 
ATOM   11770 C CZ  . ARG F 2 170 ? 19.723  19.713  -93.433  1.00 71.17  ? 170 ARG F CZ  1 
ATOM   11771 N NH1 . ARG F 2 170 ? 19.000  18.605  -93.396  1.00 65.81  ? 170 ARG F NH1 1 
ATOM   11772 N NH2 . ARG F 2 170 ? 20.611  19.879  -94.409  1.00 67.44  ? 170 ARG F NH2 1 
ATOM   11773 N N   . GLU F 2 171 ? 16.345  24.601  -93.920  1.00 65.34  ? 171 GLU F N   1 
ATOM   11774 C CA  . GLU F 2 171 ? 16.796  25.987  -93.939  1.00 76.61  ? 171 GLU F CA  1 
ATOM   11775 C C   . GLU F 2 171 ? 15.651  26.959  -93.682  1.00 77.06  ? 171 GLU F C   1 
ATOM   11776 O O   . GLU F 2 171 ? 15.863  28.016  -93.075  1.00 90.51  ? 171 GLU F O   1 
ATOM   11777 C CB  . GLU F 2 171 ? 17.475  26.304  -95.272  1.00 76.46  ? 171 GLU F CB  1 
ATOM   11778 C CG  . GLU F 2 171 ? 18.383  25.195  -95.773  1.00 78.19  ? 171 GLU F CG  1 
ATOM   11779 C CD  . GLU F 2 171 ? 19.369  25.663  -96.822  1.00 96.39  ? 171 GLU F CD  1 
ATOM   11780 O OE1 . GLU F 2 171 ? 20.442  26.173  -96.437  1.00 104.88 ? 171 GLU F OE1 1 
ATOM   11781 O OE2 . GLU F 2 171 ? 19.075  25.524  -98.028  1.00 103.67 ? 171 GLU F OE2 1 
ATOM   11782 N N   . GLU F 2 172 ? 14.441  26.631  -94.142  1.00 77.49  ? 172 GLU F N   1 
ATOM   11783 C CA  . GLU F 2 172 ? 13.297  27.505  -93.894  1.00 81.47  ? 172 GLU F CA  1 
ATOM   11784 C C   . GLU F 2 172 ? 12.972  27.587  -92.408  1.00 83.45  ? 172 GLU F C   1 
ATOM   11785 O O   . GLU F 2 172 ? 12.676  28.670  -91.887  1.00 88.45  ? 172 GLU F O   1 
ATOM   11786 C CB  . GLU F 2 172 ? 12.082  27.017  -94.681  1.00 71.28  ? 172 GLU F CB  1 
ATOM   11787 C CG  . GLU F 2 172 ? 12.201  27.200  -96.183  1.00 100.69 ? 172 GLU F CG  1 
ATOM   11788 C CD  . GLU F 2 172 ? 10.858  27.422  -96.850  1.00 127.43 ? 172 GLU F CD  1 
ATOM   11789 O OE1 . GLU F 2 172 ? 9.823   27.058  -96.249  1.00 112.66 ? 172 GLU F OE1 1 
ATOM   11790 O OE2 . GLU F 2 172 ? 10.839  27.969  -97.974  1.00 118.95 ? 172 GLU F OE2 1 
ATOM   11791 N N   . ILE F 2 173 ? 13.009  26.449  -91.712  1.00 72.21  ? 173 ILE F N   1 
ATOM   11792 C CA  . ILE F 2 173 ? 12.718  26.441  -90.281  1.00 89.22  ? 173 ILE F CA  1 
ATOM   11793 C C   . ILE F 2 173 ? 13.774  27.226  -89.514  1.00 93.05  ? 173 ILE F C   1 
ATOM   11794 O O   . ILE F 2 173 ? 13.455  27.993  -88.600  1.00 91.70  ? 173 ILE F O   1 
ATOM   11795 C CB  . ILE F 2 173 ? 12.605  24.993  -89.771  1.00 88.19  ? 173 ILE F CB  1 
ATOM   11796 C CG1 . ILE F 2 173 ? 11.518  24.244  -90.543  1.00 76.70  ? 173 ILE F CG1 1 
ATOM   11797 C CG2 . ILE F 2 173 ? 12.301  24.973  -88.280  1.00 77.20  ? 173 ILE F CG2 1 
ATOM   11798 C CD1 . ILE F 2 173 ? 11.483  22.756  -90.261  1.00 72.55  ? 173 ILE F CD1 1 
ATOM   11799 N N   . SER F 2 174 ? 15.046  27.050  -89.873  1.00 78.70  ? 174 SER F N   1 
ATOM   11800 C CA  . SER F 2 174 ? 16.116  27.695  -89.120  1.00 89.71  ? 174 SER F CA  1 
ATOM   11801 C C   . SER F 2 174 ? 16.185  29.192  -89.400  1.00 89.46  ? 174 SER F C   1 
ATOM   11802 O O   . SER F 2 174 ? 16.623  29.961  -88.536  1.00 96.62  ? 174 SER F O   1 
ATOM   11803 C CB  . SER F 2 174 ? 17.455  27.025  -89.432  1.00 120.36 ? 174 SER F CB  1 
ATOM   11804 O OG  . SER F 2 174 ? 18.466  27.480  -88.550  1.00 130.96 ? 174 SER F OG  1 
ATOM   11805 N N   . SER F 2 175 ? 15.771  29.626  -90.590  1.00 87.37  ? 175 SER F N   1 
ATOM   11806 C CA  . SER F 2 175 ? 15.737  31.049  -90.900  1.00 91.53  ? 175 SER F CA  1 
ATOM   11807 C C   . SER F 2 175 ? 14.534  31.763  -90.293  1.00 85.75  ? 175 SER F C   1 
ATOM   11808 O O   . SER F 2 175 ? 14.516  32.999  -90.267  1.00 87.50  ? 175 SER F O   1 
ATOM   11809 C CB  . SER F 2 175 ? 15.750  31.256  -92.418  1.00 87.28  ? 175 SER F CB  1 
ATOM   11810 O OG  . SER F 2 175 ? 14.982  30.267  -93.081  1.00 105.07 ? 175 SER F OG  1 
ATOM   11811 N N   . GLY F 2 176 ? 13.545  31.023  -89.791  1.00 87.23  ? 176 GLY F N   1 
ATOM   11812 C CA  . GLY F 2 176 ? 12.361  31.610  -89.203  1.00 75.90  ? 176 GLY F CA  1 
ATOM   11813 C C   . GLY F 2 176 ? 11.160  31.682  -90.117  1.00 92.84  ? 176 GLY F C   1 
ATOM   11814 O O   . GLY F 2 176 ? 10.102  32.154  -89.681  1.00 98.12  ? 176 GLY F O   1 
ATOM   11815 N N   . ARG F 2 177 ? 11.288  31.234  -91.364  1.00 94.03  ? 177 ARG F N   1 
ATOM   11816 C CA  . ARG F 2 177 ? 10.202  31.284  -92.338  1.00 91.86  ? 177 ARG F CA  1 
ATOM   11817 C C   . ARG F 2 177 ? 8.955   30.572  -91.821  1.00 89.22  ? 177 ARG F C   1 
ATOM   11818 O O   . ARG F 2 177 ? 7.830   30.992  -92.093  1.00 98.02  ? 177 ARG F O   1 
ATOM   11819 C CB  . ARG F 2 177 ? 10.645  30.658  -93.663  1.00 83.35  ? 177 ARG F CB  1 
ATOM   11820 C CG  . ARG F 2 177 ? 12.048  31.050  -94.111  1.00 86.59  ? 177 ARG F CG  1 
ATOM   11821 C CD  . ARG F 2 177 ? 12.135  32.518  -94.490  1.00 80.24  ? 177 ARG F CD  1 
ATOM   11822 N NE  . ARG F 2 177 ? 11.155  32.865  -95.510  1.00 59.33  ? 177 ARG F NE  1 
ATOM   11823 C CZ  . ARG F 2 177 ? 11.053  34.059  -96.077  1.00 51.56  ? 177 ARG F CZ  1 
ATOM   11824 N NH1 . ARG F 2 177 ? 11.873  35.046  -95.760  1.00 53.65  ? 177 ARG F NH1 1 
ATOM   11825 N NH2 . ARG F 2 177 ? 10.103  34.267  -96.985  1.00 56.33  ? 177 ARG F NH2 1 
HETATM 11826 C C1  . NAG G 3 .   ? 55.600  -40.095 -9.369   1.00 76.41  ? 1   NAG G C1  1 
HETATM 11827 C C2  . NAG G 3 .   ? 55.832  -39.598 -7.944   1.00 91.50  ? 1   NAG G C2  1 
HETATM 11828 C C3  . NAG G 3 .   ? 56.197  -38.124 -7.996   1.00 99.65  ? 1   NAG G C3  1 
HETATM 11829 C C4  . NAG G 3 .   ? 57.388  -37.908 -8.922   1.00 91.23  ? 1   NAG G C4  1 
HETATM 11830 C C5  . NAG G 3 .   ? 57.095  -38.529 -10.290  1.00 84.59  ? 1   NAG G C5  1 
HETATM 11831 C C6  . NAG G 3 .   ? 58.233  -38.401 -11.277  1.00 98.31  ? 1   NAG G C6  1 
HETATM 11832 C C7  . NAG G 3 .   ? 54.683  -40.526 -5.973   1.00 90.08  ? 1   NAG G C7  1 
HETATM 11833 C C8  . NAG G 3 .   ? 53.352  -40.629 -5.272   1.00 81.28  ? 1   NAG G C8  1 
HETATM 11834 N N2  . NAG G 3 .   ? 54.674  -39.819 -7.119   1.00 94.37  ? 1   NAG G N2  1 
HETATM 11835 O O3  . NAG G 3 .   ? 56.468  -37.731 -6.677   1.00 90.58  ? 1   NAG G O3  1 
HETATM 11836 O O4  . NAG G 3 .   ? 57.590  -36.518 -9.027   1.00 118.51 ? 1   NAG G O4  1 
HETATM 11837 O O5  . NAG G 3 .   ? 56.780  -39.896 -10.113  1.00 104.92 ? 1   NAG G O5  1 
HETATM 11838 O O6  . NAG G 3 .   ? 59.454  -38.626 -10.614  1.00 105.54 ? 1   NAG G O6  1 
HETATM 11839 O O7  . NAG G 3 .   ? 55.688  -41.053 -5.516   1.00 94.92  ? 1   NAG G O7  1 
HETATM 11840 C C1  . NAG G 3 .   ? 58.761  -36.141 -8.280   1.00 116.65 ? 2   NAG G C1  1 
HETATM 11841 C C2  . NAG G 3 .   ? 58.878  -34.618 -8.318   1.00 113.86 ? 2   NAG G C2  1 
HETATM 11842 C C3  . NAG G 3 .   ? 60.049  -34.114 -7.477   1.00 114.38 ? 2   NAG G C3  1 
HETATM 11843 C C4  . NAG G 3 .   ? 60.052  -34.759 -6.078   1.00 124.97 ? 2   NAG G C4  1 
HETATM 11844 C C5  . NAG G 3 .   ? 59.826  -36.274 -6.190   1.00 112.97 ? 2   NAG G C5  1 
HETATM 11845 C C6  . NAG G 3 .   ? 59.663  -36.963 -4.856   1.00 107.41 ? 2   NAG G C6  1 
HETATM 11846 C C7  . NAG G 3 .   ? 57.986  -33.457 -10.291  1.00 101.12 ? 2   NAG G C7  1 
HETATM 11847 C C8  . NAG G 3 .   ? 58.289  -33.059 -11.713  1.00 91.84  ? 2   NAG G C8  1 
HETATM 11848 N N2  . NAG G 3 .   ? 58.964  -34.142 -9.674   1.00 114.78 ? 2   NAG G N2  1 
HETATM 11849 O O3  . NAG G 3 .   ? 59.824  -32.728 -7.465   1.00 116.88 ? 2   NAG G O3  1 
HETATM 11850 O O4  . NAG G 3 .   ? 61.230  -34.544 -5.300   1.00 129.47 ? 2   NAG G O4  1 
HETATM 11851 O O5  . NAG G 3 .   ? 58.660  -36.532 -6.938   1.00 116.55 ? 2   NAG G O5  1 
HETATM 11852 O O6  . NAG G 3 .   ? 58.900  -38.136 -5.008   1.00 105.13 ? 2   NAG G O6  1 
HETATM 11853 O O7  . NAG G 3 .   ? 56.922  -33.169 -9.758   1.00 87.28  ? 2   NAG G O7  1 
HETATM 11854 C C1  . BMA G 3 .   ? 62.149  -33.515 -5.748   1.00 125.33 ? 3   BMA G C1  1 
HETATM 11855 C C2  . BMA G 3 .   ? 61.829  -32.274 -4.926   1.00 122.02 ? 3   BMA G C2  1 
HETATM 11856 C C3  . BMA G 3 .   ? 62.906  -31.185 -5.097   1.00 120.64 ? 3   BMA G C3  1 
HETATM 11857 C C4  . BMA G 3 .   ? 64.369  -31.675 -5.004   1.00 133.15 ? 3   BMA G C4  1 
HETATM 11858 C C5  . BMA G 3 .   ? 64.599  -33.066 -5.600   1.00 132.15 ? 3   BMA G C5  1 
HETATM 11859 C C6  . BMA G 3 .   ? 65.813  -33.794 -5.037   1.00 135.38 ? 3   BMA G C6  1 
HETATM 11860 O O2  . BMA G 3 .   ? 61.649  -32.656 -3.585   1.00 148.74 ? 3   BMA G O2  1 
HETATM 11861 O O3  . BMA G 3 .   ? 62.572  -30.190 -4.160   1.00 74.64  ? 3   BMA G O3  1 
HETATM 11862 O O4  . BMA G 3 .   ? 65.137  -30.706 -5.695   1.00 141.49 ? 3   BMA G O4  1 
HETATM 11863 O O5  . BMA G 3 .   ? 63.485  -33.950 -5.570   1.00 142.22 ? 3   BMA G O5  1 
HETATM 11864 O O6  . BMA G 3 .   ? 65.779  -33.700 -3.633   1.00 94.58  ? 3   BMA G O6  1 
HETATM 11865 C C1  . NAG H 3 .   ? 2.675   -30.920 -0.846   1.00 73.91  ? 1   NAG H C1  1 
HETATM 11866 C C2  . NAG H 3 .   ? 1.904   -32.210 -1.147   1.00 82.37  ? 1   NAG H C2  1 
HETATM 11867 C C3  . NAG H 3 .   ? 0.642   -31.909 -1.954   1.00 79.79  ? 1   NAG H C3  1 
HETATM 11868 C C4  . NAG H 3 .   ? -0.203  -30.817 -1.308   1.00 89.40  ? 1   NAG H C4  1 
HETATM 11869 C C5  . NAG H 3 .   ? 0.700   -29.600 -1.064   1.00 91.55  ? 1   NAG H C5  1 
HETATM 11870 C C6  . NAG H 3 .   ? 0.054   -28.424 -0.368   1.00 101.05 ? 1   NAG H C6  1 
HETATM 11871 C C7  . NAG H 3 .   ? 2.967   -34.421 -1.457   1.00 76.95  ? 1   NAG H C7  1 
HETATM 11872 C C8  . NAG H 3 .   ? 3.880   -35.215 -2.358   1.00 59.00  ? 1   NAG H C8  1 
HETATM 11873 N N2  . NAG H 3 .   ? 2.739   -33.153 -1.847   1.00 72.52  ? 1   NAG H N2  1 
HETATM 11874 O O3  . NAG H 3 .   ? -0.066  -33.115 -2.088   1.00 76.42  ? 1   NAG H O3  1 
HETATM 11875 O O4  . NAG H 3 .   ? -1.246  -30.547 -2.224   1.00 89.36  ? 1   NAG H O4  1 
HETATM 11876 O O5  . NAG H 3 .   ? 1.793   -29.992 -0.257   1.00 82.23  ? 1   NAG H O5  1 
HETATM 11877 O O6  . NAG H 3 .   ? -0.327  -28.806 0.933    1.00 96.76  ? 1   NAG H O6  1 
HETATM 11878 O O7  . NAG H 3 .   ? 2.479   -34.917 -0.451   1.00 111.01 ? 1   NAG H O7  1 
HETATM 11879 C C1  . NAG H 3 .   ? -2.538  -30.522 -1.580   1.00 75.11  ? 2   NAG H C1  1 
HETATM 11880 C C2  . NAG H 3 .   ? -3.464  -29.634 -2.422   1.00 85.53  ? 2   NAG H C2  1 
HETATM 11881 C C3  . NAG H 3 .   ? -4.870  -29.617 -1.823   1.00 86.86  ? 2   NAG H C3  1 
HETATM 11882 C C4  . NAG H 3 .   ? -5.392  -31.042 -1.664   1.00 82.93  ? 2   NAG H C4  1 
HETATM 11883 C C5  . NAG H 3 .   ? -4.368  -31.845 -0.850   1.00 86.74  ? 2   NAG H C5  1 
HETATM 11884 C C6  . NAG H 3 .   ? -4.736  -33.295 -0.644   1.00 82.30  ? 2   NAG H C6  1 
HETATM 11885 C C7  . NAG H 3 .   ? -2.160  -27.904 -3.584   1.00 88.81  ? 2   NAG H C7  1 
HETATM 11886 C C8  . NAG H 3 .   ? -1.708  -26.468 -3.526   1.00 93.56  ? 2   NAG H C8  1 
HETATM 11887 N N2  . NAG H 3 .   ? -2.930  -28.302 -2.554   1.00 91.56  ? 2   NAG H N2  1 
HETATM 11888 O O3  . NAG H 3 .   ? -5.677  -28.831 -2.659   1.00 93.16  ? 2   NAG H O3  1 
HETATM 11889 O O4  . NAG H 3 .   ? -6.646  -30.992 -1.010   1.00 93.58  ? 2   NAG H O4  1 
HETATM 11890 O O5  . NAG H 3 .   ? -3.103  -31.809 -1.484   1.00 71.72  ? 2   NAG H O5  1 
HETATM 11891 O O6  . NAG H 3 .   ? -4.291  -34.066 -1.734   1.00 89.26  ? 2   NAG H O6  1 
HETATM 11892 O O7  . NAG H 3 .   ? -1.834  -28.635 -4.510   1.00 83.69  ? 2   NAG H O7  1 
HETATM 11893 C C1  . BMA H 3 .   ? -7.707  -31.337 -1.939   1.00 98.40  ? 3   BMA H C1  1 
HETATM 11894 C C2  . BMA H 3 .   ? -8.847  -31.918 -1.107   1.00 102.32 ? 3   BMA H C2  1 
HETATM 11895 C C3  . BMA H 3 .   ? -10.138 -32.051 -1.939   1.00 113.35 ? 3   BMA H C3  1 
HETATM 11896 C C4  . BMA H 3 .   ? -10.515 -30.822 -2.788   1.00 120.10 ? 3   BMA H C4  1 
HETATM 11897 C C5  . BMA H 3 .   ? -9.306  -30.151 -3.436   1.00 118.14 ? 3   BMA H C5  1 
HETATM 11898 C C6  . BMA H 3 .   ? -9.564  -28.728 -3.914   1.00 121.71 ? 3   BMA H C6  1 
HETATM 11899 O O2  . BMA H 3 .   ? -9.028  -31.123 0.036    1.00 92.22  ? 3   BMA H O2  1 
HETATM 11900 O O3  . BMA H 3 .   ? -11.132 -32.411 -1.016   1.00 73.14  ? 3   BMA H O3  1 
HETATM 11901 O O4  . BMA H 3 .   ? -11.402 -31.306 -3.780   1.00 125.45 ? 3   BMA H O4  1 
HETATM 11902 O O5  . BMA H 3 .   ? -8.107  -30.186 -2.667   1.00 111.40 ? 3   BMA H O5  1 
HETATM 11903 O O6  . BMA H 3 .   ? -8.571  -28.445 -4.877   1.00 100.75 ? 3   BMA H O6  1 
HETATM 11904 C C1  . NAG I 4 .   ? 17.609  -69.714 -33.718  1.00 91.63  ? 1   NAG I C1  1 
HETATM 11905 C C2  . NAG I 4 .   ? 19.050  -70.064 -33.332  1.00 91.47  ? 1   NAG I C2  1 
HETATM 11906 C C3  . NAG I 4 .   ? 19.883  -70.280 -34.595  1.00 100.96 ? 1   NAG I C3  1 
HETATM 11907 C C4  . NAG I 4 .   ? 19.233  -71.283 -35.541  1.00 105.86 ? 1   NAG I C4  1 
HETATM 11908 C C5  . NAG I 4 .   ? 17.784  -70.854 -35.796  1.00 107.91 ? 1   NAG I C5  1 
HETATM 11909 C C6  . NAG I 4 .   ? 16.964  -71.799 -36.645  1.00 108.70 ? 1   NAG I C6  1 
HETATM 11910 C C7  . NAG I 4 .   ? 20.179  -69.229 -31.284  1.00 89.19  ? 1   NAG I C7  1 
HETATM 11911 C C8  . NAG I 4 .   ? 20.152  -70.647 -30.770  1.00 92.62  ? 1   NAG I C8  1 
HETATM 11912 N N2  . NAG I 4 .   ? 19.636  -69.038 -32.505  1.00 78.59  ? 1   NAG I N2  1 
HETATM 11913 O O3  . NAG I 4 .   ? 21.166  -70.685 -34.190  1.00 90.20  ? 1   NAG I O3  1 
HETATM 11914 O O4  . NAG I 4 .   ? 20.000  -71.264 -36.726  1.00 128.81 ? 1   NAG I O4  1 
HETATM 11915 O O5  . NAG I 4 .   ? 17.117  -70.733 -34.557  1.00 111.03 ? 1   NAG I O5  1 
HETATM 11916 O O6  . NAG I 4 .   ? 16.702  -72.975 -35.918  1.00 109.79 ? 1   NAG I O6  1 
HETATM 11917 O O7  . NAG I 4 .   ? 20.670  -68.326 -30.621  1.00 80.02  ? 1   NAG I O7  1 
HETATM 11918 C C1  . NAG I 4 .   ? 20.450  -72.595 -37.048  1.00 130.88 ? 2   NAG I C1  1 
HETATM 11919 C C2  . NAG I 4 .   ? 20.846  -72.609 -38.532  1.00 130.63 ? 2   NAG I C2  1 
HETATM 11920 C C3  . NAG I 4 .   ? 21.414  -73.974 -38.908  1.00 138.80 ? 2   NAG I C3  1 
HETATM 11921 C C4  . NAG I 4 .   ? 22.528  -74.362 -37.948  1.00 139.17 ? 2   NAG I C4  1 
HETATM 11922 C C5  . NAG I 4 .   ? 22.011  -74.281 -36.510  1.00 131.76 ? 2   NAG I C5  1 
HETATM 11923 C C6  . NAG I 4 .   ? 23.039  -74.650 -35.465  1.00 130.84 ? 2   NAG I C6  1 
HETATM 11924 C C7  . NAG I 4 .   ? 19.476  -71.037 -39.844  1.00 120.38 ? 2   NAG I C7  1 
HETATM 11925 C C8  . NAG I 4 .   ? 18.244  -70.925 -40.703  1.00 109.69 ? 2   NAG I C8  1 
HETATM 11926 N N2  . NAG I 4 .   ? 19.725  -72.272 -39.371  1.00 124.53 ? 2   NAG I N2  1 
HETATM 11927 O O3  . NAG I 4 .   ? 21.871  -73.901 -40.231  1.00 144.86 ? 2   NAG I O3  1 
HETATM 11928 O O4  . NAG I 4 .   ? 22.924  -75.674 -38.283  1.00 137.06 ? 2   NAG I O4  1 
HETATM 11929 O O5  . NAG I 4 .   ? 21.560  -72.965 -36.258  1.00 136.21 ? 2   NAG I O5  1 
HETATM 11930 O O6  . NAG I 4 .   ? 22.467  -74.572 -34.180  1.00 118.59 ? 2   NAG I O6  1 
HETATM 11931 O O7  . NAG I 4 .   ? 20.179  -70.064 -39.605  1.00 116.47 ? 2   NAG I O7  1 
HETATM 11932 C C1  . NAG J 3 .   ? 11.610  -2.766  -94.891  1.00 99.18  ? 1   NAG J C1  1 
HETATM 11933 C C2  . NAG J 3 .   ? 10.724  -3.918  -95.385  1.00 109.61 ? 1   NAG J C2  1 
HETATM 11934 C C3  . NAG J 3 .   ? 10.408  -3.736  -96.868  1.00 104.91 ? 1   NAG J C3  1 
HETATM 11935 C C4  . NAG J 3 .   ? 9.795   -2.369  -97.147  1.00 100.88 ? 1   NAG J C4  1 
HETATM 11936 C C5  . NAG J 3 .   ? 10.684  -1.298  -96.484  1.00 92.54  ? 1   NAG J C5  1 
HETATM 11937 C C6  . NAG J 3 .   ? 10.179  0.121   -96.609  1.00 78.51  ? 1   NAG J C6  1 
HETATM 11938 C C7  . NAG J 3 .   ? 10.935  -6.066  -94.187  1.00 102.50 ? 1   NAG J C7  1 
HETATM 11939 C C8  . NAG J 3 .   ? 11.740  -7.337  -94.098  1.00 110.12 ? 1   NAG J C8  1 
HETATM 11940 N N2  . NAG J 3 .   ? 11.342  -5.194  -95.130  1.00 106.90 ? 1   NAG J N2  1 
HETATM 11941 O O3  . NAG J 3 .   ? 9.562   -4.785  -97.262  1.00 95.77  ? 1   NAG J O3  1 
HETATM 11942 O O4  . NAG J 3 .   ? 9.754   -2.275  -98.560  1.00 100.67 ? 1   NAG J O4  1 
HETATM 11943 O O5  . NAG J 3 .   ? 10.872  -1.580  -95.101  1.00 96.92  ? 1   NAG J O5  1 
HETATM 11944 O O6  . NAG J 3 .   ? 8.787   0.137   -96.410  1.00 83.20  ? 1   NAG J O6  1 
HETATM 11945 O O7  . NAG J 3 .   ? 9.985   -5.864  -93.443  1.00 96.03  ? 1   NAG J O7  1 
HETATM 11946 C C1  . NAG J 3 .   ? 8.510   -1.740  -99.081  1.00 111.32 ? 2   NAG J C1  1 
HETATM 11947 C C2  . NAG J 3 .   ? 8.633   -1.708  -100.613 1.00 105.08 ? 2   NAG J C2  1 
HETATM 11948 C C3  . NAG J 3 .   ? 7.351   -1.142  -101.225 1.00 104.28 ? 2   NAG J C3  1 
HETATM 11949 C C4  . NAG J 3 .   ? 6.112   -1.881  -100.726 1.00 121.85 ? 2   NAG J C4  1 
HETATM 11950 C C5  . NAG J 3 .   ? 6.158   -1.918  -99.190  1.00 125.79 ? 2   NAG J C5  1 
HETATM 11951 C C6  . NAG J 3 .   ? 5.024   -2.670  -98.535  1.00 122.41 ? 2   NAG J C6  1 
HETATM 11952 C C7  . NAG J 3 .   ? 10.956  -1.471  -101.437 1.00 97.86  ? 2   NAG J C7  1 
HETATM 11953 C C8  . NAG J 3 .   ? 11.034  -2.978  -101.476 1.00 105.38 ? 2   NAG J C8  1 
HETATM 11954 N N2  . NAG J 3 .   ? 9.787   -0.945  -101.018 1.00 90.68  ? 2   NAG J N2  1 
HETATM 11955 O O3  . NAG J 3 .   ? 7.481   -1.215  -102.619 1.00 99.77  ? 2   NAG J O3  1 
HETATM 11956 O O4  . NAG J 3 .   ? 4.987   -1.179  -101.224 1.00 129.24 ? 2   NAG J O4  1 
HETATM 11957 O O5  . NAG J 3 .   ? 7.371   -2.511  -98.755  1.00 122.52 ? 2   NAG J O5  1 
HETATM 11958 O O6  . NAG J 3 .   ? 4.891   -3.945  -99.116  1.00 120.55 ? 2   NAG J O6  1 
HETATM 11959 O O7  . NAG J 3 .   ? 11.909  -0.783  -101.769 1.00 95.36  ? 2   NAG J O7  1 
HETATM 11960 C C1  . BMA J 3 .   ? 4.108   -2.071  -101.962 1.00 136.70 ? 3   BMA J C1  1 
HETATM 11961 C C2  . BMA J 3 .   ? 2.778   -1.345  -102.143 1.00 137.43 ? 3   BMA J C2  1 
HETATM 11962 C C3  . BMA J 3 .   ? 1.833   -2.149  -103.060 1.00 138.51 ? 3   BMA J C3  1 
HETATM 11963 C C4  . BMA J 3 .   ? 2.471   -2.741  -104.338 1.00 134.91 ? 3   BMA J C4  1 
HETATM 11964 C C5  . BMA J 3 .   ? 3.934   -3.155  -104.172 1.00 129.22 ? 3   BMA J C5  1 
HETATM 11965 C C6  . BMA J 3 .   ? 4.721   -3.226  -105.474 1.00 121.65 ? 3   BMA J C6  1 
HETATM 11966 O O2  . BMA J 3 .   ? 3.039   -0.058  -102.637 1.00 130.01 ? 3   BMA J O2  1 
HETATM 11967 O O3  . BMA J 3 .   ? 0.748   -1.292  -103.314 1.00 124.51 ? 3   BMA J O3  1 
HETATM 11968 O O4  . BMA J 3 .   ? 1.678   -3.866  -104.667 1.00 119.89 ? 3   BMA J O4  1 
HETATM 11969 O O5  . BMA J 3 .   ? 4.673   -2.403  -103.218 1.00 131.41 ? 3   BMA J O5  1 
HETATM 11970 O O6  . BMA J 3 .   ? 4.393   -2.106  -106.259 1.00 103.27 ? 3   BMA J O6  1 
HETATM 11971 C C1  . GAL K 5 .   ? 33.747  -84.077 -21.785  1.00 160.04 ? 1   GAL K C1  1 
HETATM 11972 C C2  . GAL K 5 .   ? 34.345  -82.761 -22.253  1.00 164.83 ? 1   GAL K C2  1 
HETATM 11973 C C3  . GAL K 5 .   ? 33.218  -81.889 -22.790  1.00 170.16 ? 1   GAL K C3  1 
HETATM 11974 C C4  . GAL K 5 .   ? 32.427  -82.630 -23.871  1.00 167.51 ? 1   GAL K C4  1 
HETATM 11975 C C5  . GAL K 5 .   ? 32.001  -84.010 -23.355  1.00 173.01 ? 1   GAL K C5  1 
HETATM 11976 C C6  . GAL K 5 .   ? 31.361  -84.859 -24.428  1.00 161.26 ? 1   GAL K C6  1 
HETATM 11977 O O1  . GAL K 5 .   ? 34.770  -84.891 -21.357  1.00 141.26 ? 1   GAL K O1  1 
HETATM 11978 O O2  . GAL K 5 .   ? 34.986  -82.177 -21.146  1.00 124.43 ? 1   GAL K O2  1 
HETATM 11979 O O3  . GAL K 5 .   ? 33.813  -80.697 -23.250  1.00 176.35 ? 1   GAL K O3  1 
HETATM 11980 O O4  . GAL K 5 .   ? 33.224  -82.702 -25.025  1.00 153.00 ? 1   GAL K O4  1 
HETATM 11981 O O5  . GAL K 5 .   ? 33.108  -84.722 -22.853  1.00 179.28 ? 1   GAL K O5  1 
HETATM 11982 O O6  . GAL K 5 .   ? 30.345  -84.095 -25.027  1.00 134.36 ? 1   GAL K O6  1 
HETATM 11983 C C1  . NAG K 5 .   ? 32.958  -79.556 -23.042  1.00 135.28 ? 2   NAG K C1  1 
HETATM 11984 C C2  . NAG K 5 .   ? 33.825  -78.308 -23.281  1.00 127.17 ? 2   NAG K C2  1 
HETATM 11985 C C3  . NAG K 5 .   ? 33.019  -77.012 -23.349  1.00 113.13 ? 2   NAG K C3  1 
HETATM 11986 C C4  . NAG K 5 .   ? 31.755  -77.180 -24.180  1.00 120.61 ? 2   NAG K C4  1 
HETATM 11987 C C5  . NAG K 5 .   ? 31.005  -78.445 -23.760  1.00 121.81 ? 2   NAG K C5  1 
HETATM 11988 C C6  . NAG K 5 .   ? 29.731  -78.673 -24.540  1.00 130.76 ? 2   NAG K C6  1 
HETATM 11989 C C7  . NAG K 5 .   ? 36.143  -77.906 -22.541  1.00 126.96 ? 2   NAG K C7  1 
HETATM 11990 C C8  . NAG K 5 .   ? 37.046  -77.849 -21.335  1.00 97.64  ? 2   NAG K C8  1 
HETATM 11991 N N2  . NAG K 5 .   ? 34.856  -78.200 -22.279  1.00 134.67 ? 2   NAG K N2  1 
HETATM 11992 O O3  . NAG K 5 .   ? 33.878  -76.069 -23.931  1.00 109.48 ? 2   NAG K O3  1 
HETATM 11993 O O4  . NAG K 5 .   ? 30.978  -76.020 -23.973  1.00 116.03 ? 2   NAG K O4  1 
HETATM 11994 O O5  . NAG K 5 .   ? 31.858  -79.560 -23.921  1.00 128.31 ? 2   NAG K O5  1 
HETATM 11995 O O6  . NAG K 5 .   ? 29.825  -78.008 -25.777  1.00 135.77 ? 2   NAG K O6  1 
HETATM 11996 O O7  . NAG K 5 .   ? 36.574  -77.693 -23.667  1.00 107.31 ? 2   NAG K O7  1 
HETATM 11997 C C1  . GAL K 5 .   ? 34.154  -74.973 -23.041  1.00 89.99  ? 3   GAL K C1  1 
HETATM 11998 C C2  . GAL K 5 .   ? 34.968  -73.991 -23.873  1.00 84.09  ? 3   GAL K C2  1 
HETATM 11999 C C3  . GAL K 5 .   ? 35.221  -72.720 -23.089  1.00 81.01  ? 3   GAL K C3  1 
HETATM 12000 C C4  . GAL K 5 .   ? 33.902  -72.136 -22.574  1.00 72.24  ? 3   GAL K C4  1 
HETATM 12001 C C5  . GAL K 5 .   ? 33.191  -73.224 -21.764  1.00 80.44  ? 3   GAL K C5  1 
HETATM 12002 C C6  . GAL K 5 .   ? 31.842  -72.784 -21.230  1.00 66.70  ? 3   GAL K C6  1 
HETATM 12003 O O2  . GAL K 5 .   ? 36.198  -74.594 -24.171  1.00 80.18  ? 3   GAL K O2  1 
HETATM 12004 O O3  . GAL K 5 .   ? 35.965  -71.942 -24.000  1.00 90.45  ? 3   GAL K O3  1 
HETATM 12005 O O4  . GAL K 5 .   ? 33.105  -71.748 -23.663  1.00 68.49  ? 3   GAL K O4  1 
HETATM 12006 O O5  . GAL K 5 .   ? 32.974  -74.354 -22.583  1.00 89.44  ? 3   GAL K O5  1 
HETATM 12007 O O6  . GAL K 5 .   ? 31.160  -73.878 -20.663  1.00 97.04  ? 3   GAL K O6  1 
HETATM 12008 C C1  . SIA K 5 .   ? 37.713  -70.372 -24.513  1.00 83.60  ? 4   SIA K C1  1 
HETATM 12009 C C2  . SIA K 5 .   ? 37.073  -71.261 -23.372  1.00 70.80  ? 4   SIA K C2  1 
HETATM 12010 C C3  . SIA K 5 .   ? 38.121  -72.204 -22.778  1.00 67.90  ? 4   SIA K C3  1 
HETATM 12011 C C4  . SIA K 5 .   ? 39.287  -71.440 -22.148  1.00 74.68  ? 4   SIA K C4  1 
HETATM 12012 C C5  . SIA K 5 .   ? 38.769  -70.596 -20.987  1.00 69.18  ? 4   SIA K C5  1 
HETATM 12013 C C6  . SIA K 5 .   ? 37.577  -69.719 -21.451  1.00 66.43  ? 4   SIA K C6  1 
HETATM 12014 C C7  . SIA K 5 .   ? 36.736  -69.230 -20.253  1.00 65.06  ? 4   SIA K C7  1 
HETATM 12015 C C8  . SIA K 5 .   ? 35.509  -68.437 -20.752  1.00 60.12  ? 4   SIA K C8  1 
HETATM 12016 C C9  . SIA K 5 .   ? 34.880  -67.655 -19.607  1.00 57.34  ? 4   SIA K C9  1 
HETATM 12017 C C10 . SIA K 5 .   ? 39.955  -69.425 -19.139  1.00 56.12  ? 4   SIA K C10 1 
HETATM 12018 C C11 . SIA K 5 .   ? 41.064  -68.433 -18.798  1.00 48.94  ? 4   SIA K C11 1 
HETATM 12019 N N5  . SIA K 5 .   ? 39.791  -69.694 -20.460  1.00 62.12  ? 4   SIA K N5  1 
HETATM 12020 O O1A . SIA K 5 .   ? 37.400  -69.150 -24.458  1.00 74.66  ? 4   SIA K O1A 1 
HETATM 12021 O O1B . SIA K 5 .   ? 38.447  -70.979 -25.325  1.00 85.87  ? 4   SIA K O1B 1 
HETATM 12022 O O4  . SIA K 5 .   ? 40.299  -72.312 -21.620  1.00 67.54  ? 4   SIA K O4  1 
HETATM 12023 O O6  . SIA K 5 .   ? 36.625  -70.404 -22.266  1.00 68.07  ? 4   SIA K O6  1 
HETATM 12024 O O7  . SIA K 5 .   ? 36.355  -70.343 -19.456  1.00 62.62  ? 4   SIA K O7  1 
HETATM 12025 O O8  . SIA K 5 .   ? 35.854  -67.600 -21.858  1.00 65.20  ? 4   SIA K O8  1 
HETATM 12026 O O9  . SIA K 5 .   ? 33.803  -66.854 -20.097  1.00 70.06  ? 4   SIA K O9  1 
HETATM 12027 O O10 . SIA K 5 .   ? 39.268  -69.926 -18.254  1.00 69.27  ? 4   SIA K O10 1 
HETATM 12028 C C1  . NAG L 6 .   ? 24.760  -25.914 -73.979  1.00 118.34 ? 401 NAG A C1  1 
HETATM 12029 C C2  . NAG L 6 .   ? 23.319  -26.426 -74.043  1.00 129.77 ? 401 NAG A C2  1 
HETATM 12030 C C3  . NAG L 6 .   ? 23.260  -27.820 -73.436  1.00 127.31 ? 401 NAG A C3  1 
HETATM 12031 C C4  . NAG L 6 .   ? 24.234  -28.736 -74.158  1.00 131.53 ? 401 NAG A C4  1 
HETATM 12032 C C5  . NAG L 6 .   ? 25.633  -28.116 -74.140  1.00 117.89 ? 401 NAG A C5  1 
HETATM 12033 C C6  . NAG L 6 .   ? 26.654  -28.925 -74.906  1.00 123.27 ? 401 NAG A C6  1 
HETATM 12034 C C7  . NAG L 6 .   ? 21.253  -25.091 -73.936  1.00 116.08 ? 401 NAG A C7  1 
HETATM 12035 C C8  . NAG L 6 .   ? 20.447  -24.164 -73.063  1.00 113.24 ? 401 NAG A C8  1 
HETATM 12036 N N2  . NAG L 6 .   ? 22.400  -25.535 -73.386  1.00 124.21 ? 401 NAG A N2  1 
HETATM 12037 O O3  . NAG L 6 .   ? 21.939  -28.279 -73.554  1.00 114.65 ? 401 NAG A O3  1 
HETATM 12038 O O4  . NAG L 6 .   ? 24.203  -29.975 -73.486  1.00 130.64 ? 401 NAG A O4  1 
HETATM 12039 O O5  . NAG L 6 .   ? 25.582  -26.813 -74.690  1.00 124.85 ? 401 NAG A O5  1 
HETATM 12040 O O6  . NAG L 6 .   ? 27.513  -28.064 -75.614  1.00 104.09 ? 401 NAG A O6  1 
HETATM 12041 O O7  . NAG L 6 .   ? 20.874  -25.405 -75.056  1.00 114.02 ? 401 NAG A O7  1 
HETATM 12042 C C1  . NAG M 6 .   ? 46.434  -30.774 -58.550  1.00 116.63 ? 402 NAG A C1  1 
HETATM 12043 C C2  . NAG M 6 .   ? 45.785  -31.488 -59.747  1.00 120.73 ? 402 NAG A C2  1 
HETATM 12044 C C3  . NAG M 6 .   ? 46.815  -32.229 -60.597  1.00 141.58 ? 402 NAG A C3  1 
HETATM 12045 C C4  . NAG M 6 .   ? 47.995  -31.328 -60.925  1.00 127.44 ? 402 NAG A C4  1 
HETATM 12046 C C5  . NAG M 6 .   ? 48.532  -30.691 -59.640  1.00 115.00 ? 402 NAG A C5  1 
HETATM 12047 C C6  . NAG M 6 .   ? 49.705  -29.765 -59.864  1.00 108.76 ? 402 NAG A C6  1 
HETATM 12048 C C7  . NAG M 6 .   ? 44.541  -33.442 -58.560  1.00 123.21 ? 402 NAG A C7  1 
HETATM 12049 C C8  . NAG M 6 .   ? 45.719  -34.087 -57.860  1.00 109.50 ? 402 NAG A C8  1 
HETATM 12050 N N2  . NAG M 6 .   ? 44.686  -32.342 -59.345  1.00 113.92 ? 402 NAG A N2  1 
HETATM 12051 O O3  . NAG M 6 .   ? 46.178  -32.705 -61.756  1.00 148.59 ? 402 NAG A O3  1 
HETATM 12052 O O4  . NAG M 6 .   ? 48.967  -32.148 -61.532  1.00 127.12 ? 402 NAG A O4  1 
HETATM 12053 O O5  . NAG M 6 .   ? 47.496  -29.964 -59.004  1.00 106.88 ? 402 NAG A O5  1 
HETATM 12054 O O6  . NAG M 6 .   ? 49.761  -28.815 -58.827  1.00 109.92 ? 402 NAG A O6  1 
HETATM 12055 O O7  . NAG M 6 .   ? 43.430  -33.925 -58.421  1.00 131.35 ? 402 NAG A O7  1 
HETATM 12056 C C1  . NAG N 6 .   ? 47.014  -0.304  -52.135  1.00 129.26 ? 401 NAG C C1  1 
HETATM 12057 C C2  . NAG N 6 .   ? 46.971  -0.063  -50.614  1.00 115.01 ? 401 NAG C C2  1 
HETATM 12058 C C3  . NAG N 6 .   ? 48.262  -0.670  -50.050  1.00 123.03 ? 401 NAG C C3  1 
HETATM 12059 C C4  . NAG N 6 .   ? 48.475  -2.117  -50.484  1.00 126.47 ? 401 NAG C C4  1 
HETATM 12060 C C5  . NAG N 6 .   ? 48.303  -2.242  -52.001  1.00 133.22 ? 401 NAG C C5  1 
HETATM 12061 C C6  . NAG N 6 .   ? 48.407  -3.651  -52.539  1.00 128.15 ? 401 NAG C C6  1 
HETATM 12062 C C7  . NAG N 6 .   ? 46.685  1.846   -49.042  1.00 116.43 ? 401 NAG C C7  1 
HETATM 12063 C C8  . NAG N 6 .   ? 46.622  3.350   -48.970  1.00 92.07  ? 401 NAG C C8  1 
HETATM 12064 N N2  . NAG N 6 .   ? 46.873  1.336   -50.279  1.00 109.69 ? 401 NAG C N2  1 
HETATM 12065 O O3  . NAG N 6 .   ? 48.242  -0.577  -48.649  1.00 121.79 ? 401 NAG C O3  1 
HETATM 12066 O O4  . NAG N 6 .   ? 49.775  -2.475  -50.067  1.00 118.29 ? 401 NAG C O4  1 
HETATM 12067 O O5  . NAG N 6 .   ? 47.047  -1.694  -52.346  1.00 126.31 ? 401 NAG C O5  1 
HETATM 12068 O O6  . NAG N 6 .   ? 49.736  -4.096  -52.391  1.00 115.74 ? 401 NAG C O6  1 
HETATM 12069 O O7  . NAG N 6 .   ? 46.574  1.159   -48.035  1.00 111.42 ? 401 NAG C O7  1 
HETATM 12070 C C1  . NAG O 6 .   ? 29.773  2.644   -29.909  1.00 139.29 ? 402 NAG C C1  1 
HETATM 12071 C C2  . NAG O 6 .   ? 31.294  2.745   -30.075  1.00 145.87 ? 402 NAG C C2  1 
HETATM 12072 C C3  . NAG O 6 .   ? 31.872  3.816   -29.155  1.00 143.33 ? 402 NAG C C3  1 
HETATM 12073 C C4  . NAG O 6 .   ? 31.117  5.126   -29.323  1.00 135.52 ? 402 NAG C C4  1 
HETATM 12074 C C5  . NAG O 6 .   ? 29.614  4.870   -29.163  1.00 133.46 ? 402 NAG C C5  1 
HETATM 12075 C C6  . NAG O 6 .   ? 28.752  6.100   -29.308  1.00 131.11 ? 402 NAG C C6  1 
HETATM 12076 C C7  . NAG O 6 .   ? 32.064  0.521   -28.958  1.00 135.44 ? 402 NAG C C7  1 
HETATM 12077 C C8  . NAG O 6 .   ? 31.451  0.710   -27.587  1.00 96.18  ? 402 NAG C C8  1 
HETATM 12078 N N2  . NAG O 6 .   ? 31.940  1.456   -29.938  1.00 143.53 ? 402 NAG C N2  1 
HETATM 12079 O O3  . NAG O 6 .   ? 33.246  3.946   -29.421  1.00 122.38 ? 402 NAG C O3  1 
HETATM 12080 O O4  . NAG O 6 .   ? 31.599  5.985   -28.316  1.00 116.86 ? 402 NAG C O4  1 
HETATM 12081 O O5  . NAG O 6 .   ? 29.198  3.914   -30.122  1.00 137.52 ? 402 NAG C O5  1 
HETATM 12082 O O6  . NAG O 6 .   ? 28.833  6.550   -30.638  1.00 131.33 ? 402 NAG C O6  1 
HETATM 12083 O O7  . NAG O 6 .   ? 32.694  -0.497  -29.191  1.00 135.16 ? 402 NAG C O7  1 
HETATM 12084 C C1  . NAG P 6 .   ? 13.968  29.408  -66.171  1.00 140.71 ? 201 NAG D C1  1 
HETATM 12085 C C2  . NAG P 6 .   ? 13.143  30.197  -65.147  1.00 137.41 ? 201 NAG D C2  1 
HETATM 12086 C C3  . NAG P 6 .   ? 12.485  31.399  -65.811  1.00 141.74 ? 201 NAG D C3  1 
HETATM 12087 C C4  . NAG P 6 .   ? 13.547  32.246  -66.490  1.00 143.04 ? 201 NAG D C4  1 
HETATM 12088 C C5  . NAG P 6 .   ? 14.377  31.363  -67.428  1.00 141.83 ? 201 NAG D C5  1 
HETATM 12089 C C6  . NAG P 6 .   ? 15.482  32.115  -68.127  1.00 129.12 ? 201 NAG D C6  1 
HETATM 12090 C C7  . NAG P 6 .   ? 12.320  28.850  -63.259  1.00 124.97 ? 201 NAG D C7  1 
HETATM 12091 C C8  . NAG P 6 .   ? 11.181  27.986  -62.784  1.00 109.08 ? 201 NAG D C8  1 
HETATM 12092 N N2  . NAG P 6 .   ? 12.173  29.352  -64.500  1.00 126.52 ? 201 NAG D N2  1 
HETATM 12093 O O3  . NAG P 6 .   ? 11.802  32.121  -64.820  1.00 120.52 ? 201 NAG D O3  1 
HETATM 12094 O O4  . NAG P 6 .   ? 12.866  33.265  -67.189  1.00 125.03 ? 201 NAG D O4  1 
HETATM 12095 O O5  . NAG P 6 .   ? 14.944  30.280  -66.707  1.00 149.35 ? 201 NAG D O5  1 
HETATM 12096 O O6  . NAG P 6 .   ? 16.308  32.727  -67.165  1.00 121.38 ? 201 NAG D O6  1 
HETATM 12097 O O7  . NAG P 6 .   ? 13.296  29.062  -62.552  1.00 118.75 ? 201 NAG D O7  1 
HETATM 12098 C C1  . NAG Q 6 .   ? -0.138  -25.708 -54.425  1.00 120.51 ? 401 NAG E C1  1 
HETATM 12099 C C2  . NAG Q 6 .   ? -1.292  -24.868 -53.858  1.00 130.94 ? 401 NAG E C2  1 
HETATM 12100 C C3  . NAG Q 6 .   ? -2.610  -25.224 -54.540  1.00 133.24 ? 401 NAG E C3  1 
HETATM 12101 C C4  . NAG Q 6 .   ? -2.465  -25.139 -56.050  1.00 132.79 ? 401 NAG E C4  1 
HETATM 12102 C C5  . NAG Q 6 .   ? -1.315  -26.051 -56.478  1.00 119.36 ? 401 NAG E C5  1 
HETATM 12103 C C6  . NAG Q 6 .   ? -1.074  -26.065 -57.971  1.00 98.62  ? 401 NAG E C6  1 
HETATM 12104 C C7  . NAG Q 6 .   ? -0.887  -24.193 -51.521  1.00 110.15 ? 401 NAG E C7  1 
HETATM 12105 C C8  . NAG Q 6 .   ? -1.142  -24.575 -50.086  1.00 91.53  ? 401 NAG E C8  1 
HETATM 12106 N N2  . NAG Q 6 .   ? -1.407  -25.035 -52.433  1.00 116.49 ? 401 NAG E N2  1 
HETATM 12107 O O3  . NAG Q 6 .   ? -3.598  -24.346 -54.063  1.00 123.76 ? 401 NAG E O3  1 
HETATM 12108 O O4  . NAG Q 6 .   ? -3.694  -25.541 -56.616  1.00 127.90 ? 401 NAG E O4  1 
HETATM 12109 O O5  . NAG Q 6 .   ? -0.129  -25.624 -55.836  1.00 127.50 ? 401 NAG E O5  1 
HETATM 12110 O O6  . NAG Q 6 .   ? 0.046   -26.863 -58.270  1.00 105.86 ? 401 NAG E O6  1 
HETATM 12111 O O7  . NAG Q 6 .   ? -0.248  -23.191 -51.813  1.00 114.30 ? 401 NAG E O7  1 
HETATM 12112 O O   . HOH R 7 .   ? 37.390  -37.147 -27.661  1.00 63.88  ? 501 HOH A O   1 
HETATM 12113 O O   . HOH R 7 .   ? 30.726  -49.752 -20.848  1.00 65.03  ? 502 HOH A O   1 
HETATM 12114 O O   . HOH R 7 .   ? 35.858  -52.200 -32.573  1.00 68.01  ? 503 HOH A O   1 
HETATM 12115 O O   . HOH R 7 .   ? 56.196  -38.806 -45.102  1.00 70.84  ? 504 HOH A O   1 
HETATM 12116 O O   . HOH R 7 .   ? 38.933  -38.720 -15.093  1.00 68.09  ? 505 HOH A O   1 
HETATM 12117 O O   . HOH R 7 .   ? 59.451  -36.195 -25.356  1.00 72.38  ? 506 HOH A O   1 
HETATM 12118 O O   . HOH R 7 .   ? 60.478  -58.522 -14.454  1.00 61.60  ? 507 HOH A O   1 
HETATM 12119 O O   . HOH R 7 .   ? 46.027  -75.522 -31.573  1.00 65.61  ? 508 HOH A O   1 
HETATM 12120 O O   . HOH R 7 .   ? 35.233  -51.572 -34.686  1.00 72.50  ? 509 HOH A O   1 
HETATM 12121 O O   . HOH R 7 .   ? 43.802  -61.817 0.550    1.00 47.35  ? 510 HOH A O   1 
HETATM 12122 O O   . HOH R 7 .   ? 31.627  -46.609 -11.619  1.00 55.43  ? 511 HOH A O   1 
HETATM 12123 O O   . HOH R 7 .   ? 32.395  -44.109 -12.631  1.00 69.76  ? 512 HOH A O   1 
HETATM 12124 O O   . HOH R 7 .   ? 35.598  -54.050 0.131    1.00 68.17  ? 513 HOH A O   1 
HETATM 12125 O O   . HOH S 7 .   ? 26.109  -36.966 -39.867  1.00 68.88  ? 201 HOH B O   1 
HETATM 12126 O O   . HOH S 7 .   ? 32.668  -34.447 -34.580  1.00 52.74  ? 202 HOH B O   1 
HETATM 12127 O O   . HOH S 7 .   ? 47.440  -4.821  -89.664  1.00 71.32  ? 203 HOH B O   1 
HETATM 12128 O O   . HOH T 7 .   ? 39.341  -42.631 11.070   1.00 55.07  ? 501 HOH C O   1 
HETATM 12129 O O   . HOH T 7 .   ? 30.007  -41.275 18.866   1.00 60.87  ? 502 HOH C O   1 
HETATM 12130 O O   . HOH T 7 .   ? 39.305  -17.754 6.256    1.00 65.35  ? 503 HOH C O   1 
HETATM 12131 O O   . HOH T 7 .   ? 29.462  -48.536 2.840    1.00 58.40  ? 504 HOH C O   1 
HETATM 12132 O O   . HOH T 7 .   ? 22.915  -35.223 -10.656  1.00 66.78  ? 505 HOH C O   1 
HETATM 12133 O O   . HOH T 7 .   ? 38.981  -34.190 6.580    1.00 49.87  ? 506 HOH C O   1 
HETATM 12134 O O   . HOH T 7 .   ? 27.901  -14.318 -36.520  1.00 62.24  ? 507 HOH C O   1 
HETATM 12135 O O   . HOH T 7 .   ? 28.924  -36.710 -8.840   1.00 63.20  ? 508 HOH C O   1 
HETATM 12136 O O   . HOH T 7 .   ? 22.051  -37.949 -14.979  1.00 64.67  ? 509 HOH C O   1 
HETATM 12137 O O   . HOH T 7 .   ? 8.107   -30.798 4.255    1.00 54.37  ? 510 HOH C O   1 
HETATM 12138 O O   . HOH T 7 .   ? 40.369  -33.184 8.233    1.00 54.79  ? 511 HOH C O   1 
HETATM 12139 O O   . HOH T 7 .   ? 20.552  -36.212 -10.045  1.00 59.00  ? 512 HOH C O   1 
HETATM 12140 O O   . HOH T 7 .   ? 34.436  -24.227 -13.941  1.00 60.88  ? 513 HOH C O   1 
HETATM 12141 O O   . HOH T 7 .   ? 28.868  -38.813 -10.429  1.00 56.69  ? 514 HOH C O   1 
HETATM 12142 O O   . HOH U 7 .   ? 30.461  -18.207 -36.555  1.00 65.23  ? 301 HOH D O   1 
HETATM 12143 O O   . HOH U 7 .   ? 30.709  -38.639 -25.314  1.00 56.08  ? 302 HOH D O   1 
HETATM 12144 O O   . HOH U 7 .   ? 30.930  -36.774 -19.558  1.00 59.88  ? 303 HOH D O   1 
HETATM 12145 O O   . HOH V 7 .   ? 11.325  -25.696 -53.371  1.00 67.71  ? 501 HOH E O   1 
HETATM 12146 O O   . HOH V 7 .   ? 16.836  -45.004 -47.191  1.00 66.63  ? 502 HOH E O   1 
HETATM 12147 O O   . HOH V 7 .   ? -1.730  -28.181 -33.437  1.00 73.80  ? 503 HOH E O   1 
HETATM 12148 O O   . HOH V 7 .   ? 20.203  -57.431 -28.581  1.00 66.05  ? 504 HOH E O   1 
HETATM 12149 O O   . HOH V 7 .   ? -12.875 -55.328 -13.907  1.00 54.67  ? 505 HOH E O   1 
HETATM 12150 O O   . HOH V 7 .   ? 16.817  -49.594 -23.070  1.00 62.13  ? 506 HOH E O   1 
HETATM 12151 O O   . HOH V 7 .   ? 1.403   -39.567 -0.215   1.00 49.60  ? 507 HOH E O   1 
HETATM 12152 O O   . HOH V 7 .   ? -0.949  -37.534 -29.156  1.00 72.36  ? 508 HOH E O   1 
HETATM 12153 O O   . HOH V 7 .   ? 18.200  -51.455 -4.438   1.00 66.49  ? 509 HOH E O   1 
HETATM 12154 O O   . HOH V 7 .   ? -0.038  -51.823 -33.465  1.00 70.15  ? 510 HOH E O   1 
HETATM 12155 O O   . HOH V 7 .   ? 8.343   -68.214 -26.358  1.00 63.01  ? 511 HOH E O   1 
HETATM 12156 O O   . HOH V 7 .   ? 1.656   -49.005 -4.407   1.00 49.54  ? 512 HOH E O   1 
HETATM 12157 O O   . HOH V 7 .   ? 22.813  -53.629 -16.634  1.00 57.49  ? 513 HOH E O   1 
HETATM 12158 O O   . HOH V 7 .   ? -3.002  -34.896 -33.155  1.00 67.37  ? 514 HOH E O   1 
HETATM 12159 O O   . HOH V 7 .   ? -1.240  -57.114 4.703    1.00 51.57  ? 515 HOH E O   1 
HETATM 12160 O O   . HOH V 7 .   ? -2.643  -42.928 -38.087  1.00 63.94  ? 516 HOH E O   1 
HETATM 12161 O O   . HOH V 7 .   ? 7.405   -12.386 -68.198  1.00 72.53  ? 517 HOH E O   1 
HETATM 12162 O O   . HOH V 7 .   ? 21.699  -57.563 -31.447  1.00 63.60  ? 518 HOH E O   1 
HETATM 12163 O O   . HOH V 7 .   ? 15.053  -66.685 -4.939   1.00 63.93  ? 519 HOH E O   1 
HETATM 12164 O O   . HOH V 7 .   ? 7.778   -40.866 -20.909  1.00 58.31  ? 520 HOH E O   1 
HETATM 12165 O O   . HOH V 7 .   ? 5.808   -41.293 -13.990  1.00 67.91  ? 521 HOH E O   1 
HETATM 12166 O O   . HOH V 7 .   ? 9.532   -7.527  -45.008  1.00 71.15  ? 522 HOH E O   1 
HETATM 12167 O O   . HOH V 7 .   ? 9.762   -41.900 -20.205  1.00 55.95  ? 523 HOH E O   1 
HETATM 12168 O O   . HOH V 7 .   ? 19.057  -51.300 -11.600  1.00 56.97  ? 524 HOH E O   1 
HETATM 12169 O O   . HOH V 7 .   ? 17.062  -49.859 -12.205  1.00 63.49  ? 525 HOH E O   1 
HETATM 12170 O O   . HOH W 7 .   ? 19.223  16.166  -95.796  1.00 66.23  ? 201 HOH F O   1 
HETATM 12171 O O   . HOH W 7 .   ? 8.850   31.924  -96.227  1.00 61.38  ? 202 HOH F O   1 
HETATM 12172 O O   . HOH W 7 .   ? 14.562  26.831  -98.654  1.00 63.70  ? 203 HOH F O   1 
HETATM 12173 O O   . HOH W 7 .   ? 17.640  -30.232 -56.314  1.00 70.82  ? 204 HOH F O   1 
# 
