data_9NR5
# 
_entry.id   9NR5 
# 
_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   9NR5         pdb_00009nr5 10.2210/pdb9nr5/pdb 
WWPDB D_1000294074 ?            ?                   
# 
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                        9NR5 
_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' 36509.453 3  ? Q226L ? ? 
2 polymer     man 'Hemagglutinin HA2' 20442.520 3  ? ?     ? ? 
3 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   3  ? ?     ? 
? 
4 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   1  
? ?     ? ? 
5 branched    man 'N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 
674.604   3  ? ?     ? ? 
6 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   6  ? ?     ? ? 
7 water       nat water 18.015    56 ? ?     ? ? 
# 
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 
;PGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGRLCDLNGVKPLILKDCSVAGWLLGNPMCDEFIRVPEWSY
IVERTNPANDLCYPGNLNDYEELKHLLSRINHFEKTLIIPKSSWPNHETSGVSAACPYQGVPSFFRNVVWLTKKNDAYPT
IKMSYNNTNGEDLLILWGIHHSNNAAEQINLYKNPTTYVSVGTSTLNQRLVPKIATRSQVNGLQGRMDFFWTILKPNDAI
HFESNGNFIAPEYAYKIVKKGDSTIMKSEMEYGHCNTKCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATGLRN
SPLR
;
;PGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGRLCDLNGVKPLILKDCSVAGWLLGNPMCDEFIRVPEWSY
IVERTNPANDLCYPGNLNDYEELKHLLSRINHFEKTLIIPKSSWPNHETSGVSAACPYQGVPSFFRNVVWLTKKNDAYPT
IKMSYNNTNGEDLLILWGIHHSNNAAEQINLYKNPTTYVSVGTSTLNQRLVPKIATRSQVNGLQGRMDFFWTILKPNDAI
HFESNGNFIAPEYAYKIVKKGDSTIMKSEMEYGHCNTKCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATGLRN
SPLR
;
A,C,E ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADRESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEARLKREEISSGR
;
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADRESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
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   PRO n 
1 2   GLY n 
1 3   ASP n 
1 4   GLN n 
1 5   ILE n 
1 6   CYS n 
1 7   ILE n 
1 8   GLY n 
1 9   TYR n 
1 10  HIS n 
1 11  ALA n 
1 12  ASN n 
1 13  ASN n 
1 14  SER n 
1 15  THR n 
1 16  GLU n 
1 17  GLN n 
1 18  VAL n 
1 19  ASP n 
1 20  THR n 
1 21  ILE n 
1 22  MET n 
1 23  GLU n 
1 24  LYS n 
1 25  ASN n 
1 26  VAL n 
1 27  THR n 
1 28  VAL n 
1 29  THR n 
1 30  HIS n 
1 31  ALA n 
1 32  GLN n 
1 33  ASP n 
1 34  ILE n 
1 35  LEU n 
1 36  GLU n 
1 37  LYS n 
1 38  THR n 
1 39  HIS n 
1 40  ASN n 
1 41  GLY n 
1 42  ARG n 
1 43  LEU n 
1 44  CYS n 
1 45  ASP n 
1 46  LEU n 
1 47  ASN n 
1 48  GLY n 
1 49  VAL n 
1 50  LYS n 
1 51  PRO n 
1 52  LEU n 
1 53  ILE n 
1 54  LEU n 
1 55  LYS n 
1 56  ASP n 
1 57  CYS n 
1 58  SER n 
1 59  VAL n 
1 60  ALA n 
1 61  GLY n 
1 62  TRP n 
1 63  LEU n 
1 64  LEU n 
1 65  GLY n 
1 66  ASN n 
1 67  PRO n 
1 68  MET n 
1 69  CYS n 
1 70  ASP n 
1 71  GLU n 
1 72  PHE n 
1 73  ILE n 
1 74  ARG n 
1 75  VAL n 
1 76  PRO n 
1 77  GLU n 
1 78  TRP n 
1 79  SER n 
1 80  TYR n 
1 81  ILE n 
1 82  VAL n 
1 83  GLU n 
1 84  ARG n 
1 85  THR n 
1 86  ASN n 
1 87  PRO n 
1 88  ALA n 
1 89  ASN n 
1 90  ASP n 
1 91  LEU n 
1 92  CYS n 
1 93  TYR n 
1 94  PRO n 
1 95  GLY n 
1 96  ASN n 
1 97  LEU n 
1 98  ASN n 
1 99  ASP n 
1 100 TYR n 
1 101 GLU n 
1 102 GLU n 
1 103 LEU n 
1 104 LYS n 
1 105 HIS n 
1 106 LEU n 
1 107 LEU n 
1 108 SER n 
1 109 ARG n 
1 110 ILE n 
1 111 ASN n 
1 112 HIS n 
1 113 PHE n 
1 114 GLU n 
1 115 LYS n 
1 116 THR n 
1 117 LEU n 
1 118 ILE n 
1 119 ILE n 
1 120 PRO n 
1 121 LYS n 
1 122 SER n 
1 123 SER n 
1 124 TRP n 
1 125 PRO n 
1 126 ASN n 
1 127 HIS n 
1 128 GLU n 
1 129 THR n 
1 130 SER n 
1 131 GLY n 
1 132 VAL n 
1 133 SER n 
1 134 ALA n 
1 135 ALA n 
1 136 CYS n 
1 137 PRO n 
1 138 TYR n 
1 139 GLN n 
1 140 GLY n 
1 141 VAL n 
1 142 PRO n 
1 143 SER n 
1 144 PHE n 
1 145 PHE n 
1 146 ARG n 
1 147 ASN n 
1 148 VAL n 
1 149 VAL n 
1 150 TRP n 
1 151 LEU n 
1 152 THR n 
1 153 LYS n 
1 154 LYS n 
1 155 ASN n 
1 156 ASP n 
1 157 ALA n 
1 158 TYR n 
1 159 PRO n 
1 160 THR n 
1 161 ILE n 
1 162 LYS n 
1 163 MET n 
1 164 SER n 
1 165 TYR n 
1 166 ASN n 
1 167 ASN n 
1 168 THR n 
1 169 ASN n 
1 170 GLY n 
1 171 GLU n 
1 172 ASP n 
1 173 LEU n 
1 174 LEU n 
1 175 ILE n 
1 176 LEU n 
1 177 TRP n 
1 178 GLY n 
1 179 ILE n 
1 180 HIS n 
1 181 HIS n 
1 182 SER n 
1 183 ASN n 
1 184 ASN n 
1 185 ALA n 
1 186 ALA n 
1 187 GLU n 
1 188 GLN n 
1 189 ILE n 
1 190 ASN n 
1 191 LEU n 
1 192 TYR n 
1 193 LYS n 
1 194 ASN n 
1 195 PRO n 
1 196 THR n 
1 197 THR n 
1 198 TYR n 
1 199 VAL n 
1 200 SER n 
1 201 VAL n 
1 202 GLY n 
1 203 THR n 
1 204 SER n 
1 205 THR n 
1 206 LEU n 
1 207 ASN n 
1 208 GLN n 
1 209 ARG n 
1 210 LEU n 
1 211 VAL n 
1 212 PRO n 
1 213 LYS n 
1 214 ILE n 
1 215 ALA n 
1 216 THR n 
1 217 ARG n 
1 218 SER n 
1 219 GLN n 
1 220 VAL n 
1 221 ASN n 
1 222 GLY n 
1 223 LEU n 
1 224 GLN n 
1 225 GLY n 
1 226 ARG n 
1 227 MET n 
1 228 ASP n 
1 229 PHE n 
1 230 PHE n 
1 231 TRP n 
1 232 THR n 
1 233 ILE n 
1 234 LEU n 
1 235 LYS n 
1 236 PRO n 
1 237 ASN n 
1 238 ASP n 
1 239 ALA n 
1 240 ILE n 
1 241 HIS n 
1 242 PHE n 
1 243 GLU n 
1 244 SER n 
1 245 ASN n 
1 246 GLY n 
1 247 ASN n 
1 248 PHE n 
1 249 ILE n 
1 250 ALA n 
1 251 PRO n 
1 252 GLU n 
1 253 TYR n 
1 254 ALA n 
1 255 TYR n 
1 256 LYS n 
1 257 ILE n 
1 258 VAL n 
1 259 LYS n 
1 260 LYS n 
1 261 GLY n 
1 262 ASP n 
1 263 SER n 
1 264 THR n 
1 265 ILE n 
1 266 MET n 
1 267 LYS n 
1 268 SER n 
1 269 GLU n 
1 270 MET n 
1 271 GLU n 
1 272 TYR n 
1 273 GLY n 
1 274 HIS n 
1 275 CYS n 
1 276 ASN n 
1 277 THR n 
1 278 LYS n 
1 279 CYS n 
1 280 GLN n 
1 281 THR n 
1 282 PRO n 
1 283 ILE n 
1 284 GLY n 
1 285 ALA n 
1 286 ILE n 
1 287 ASN n 
1 288 SER n 
1 289 SER n 
1 290 MET n 
1 291 PRO n 
1 292 PHE n 
1 293 HIS n 
1 294 ASN n 
1 295 ILE n 
1 296 HIS n 
1 297 PRO n 
1 298 LEU n 
1 299 THR n 
1 300 ILE n 
1 301 GLY n 
1 302 GLU n 
1 303 CYS n 
1 304 PRO n 
1 305 LYS n 
1 306 TYR n 
1 307 VAL n 
1 308 LYS n 
1 309 SER n 
1 310 ASN n 
1 311 LYS n 
1 312 LEU n 
1 313 VAL n 
1 314 LEU n 
1 315 ALA n 
1 316 THR n 
1 317 GLY n 
1 318 LEU n 
1 319 ARG n 
1 320 ASN n 
1 321 SER n 
1 322 PRO n 
1 323 LEU n 
1 324 ARG n 
2 1   GLY n 
2 2   LEU n 
2 3   PHE n 
2 4   GLY n 
2 5   ALA n 
2 6   ILE n 
2 7   ALA n 
2 8   GLY n 
2 9   PHE n 
2 10  ILE n 
2 11  GLU n 
2 12  GLY n 
2 13  GLY n 
2 14  TRP n 
2 15  GLN n 
2 16  GLY n 
2 17  MET n 
2 18  VAL n 
2 19  ASP n 
2 20  GLY n 
2 21  TRP n 
2 22  TYR n 
2 23  GLY n 
2 24  TYR n 
2 25  HIS n 
2 26  HIS n 
2 27  SER n 
2 28  ASN n 
2 29  GLU n 
2 30  GLN n 
2 31  GLY n 
2 32  SER n 
2 33  GLY n 
2 34  TYR n 
2 35  ALA n 
2 36  ALA n 
2 37  ASP n 
2 38  ARG 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' 1 324 ? ? HA ? ? ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? ? 
'Spodoptera aff. frugiperda 1 BOLD-2017' 2449148 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 177 ? ? HA ? ? ? ? ? ? '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 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                               
'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                                    WURCS PDB2Glycan 
1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                                                          LINUCS PDB-CARE   ? 
4 4 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                      
'Glycam Condensed Sequence' GMML       1.0   
5 4 '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 
6 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'                                       LINUCS PDB-CARE   ? 
7 5 DNeup5Aca2-6DGalpb1-4DGlcpNAcb1-ROH                                                                      
'Glycam Condensed Sequence' GMML       1.0   
8 5 'WURCS=2.0/3,3,2/[a2122h-1b_1-5_2*NCC/3=O][a2112h-1b_1-5][Aad21122h-2a_2-6_5*NCC/3=O]/1-2-3/a4-b1_b6-c2' WURCS PDB2Glycan 
1.1.0 
9 5 '[][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{[(6+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 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
3 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
4 5 2 GAL C1 O1 1 NAG O4 HO4 sing ? 
5 5 3 SIA C2 O2 2 GAL O6 HO6 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   PRO 1   9   9   PRO PRO A . n 
A 1 2   GLY 2   10  10  GLY GLY A . n 
A 1 3   ASP 3   11  11  ASP ASP A . n 
A 1 4   GLN 4   12  12  GLN GLN A . n 
A 1 5   ILE 5   13  13  ILE ILE A . n 
A 1 6   CYS 6   14  14  CYS CYS A . n 
A 1 7   ILE 7   15  15  ILE ILE A . n 
A 1 8   GLY 8   16  16  GLY GLY A . n 
A 1 9   TYR 9   17  17  TYR TYR A . n 
A 1 10  HIS 10  18  18  HIS HIS A . n 
A 1 11  ALA 11  19  19  ALA ALA A . n 
A 1 12  ASN 12  20  20  ASN ASN A . n 
A 1 13  ASN 13  21  21  ASN ASN A . n 
A 1 14  SER 14  22  22  SER SER A . n 
A 1 15  THR 15  23  23  THR THR A . n 
A 1 16  GLU 16  24  24  GLU GLU A . n 
A 1 17  GLN 17  25  25  GLN GLN A . n 
A 1 18  VAL 18  26  26  VAL VAL A . n 
A 1 19  ASP 19  27  27  ASP ASP A . n 
A 1 20  THR 20  28  28  THR THR A . n 
A 1 21  ILE 21  29  29  ILE ILE A . n 
A 1 22  MET 22  30  30  MET MET A . n 
A 1 23  GLU 23  31  31  GLU GLU A . n 
A 1 24  LYS 24  32  32  LYS LYS A . n 
A 1 25  ASN 25  33  33  ASN ASN A . n 
A 1 26  VAL 26  34  34  VAL VAL A . n 
A 1 27  THR 27  35  35  THR THR A . n 
A 1 28  VAL 28  36  36  VAL VAL A . n 
A 1 29  THR 29  37  37  THR THR A . n 
A 1 30  HIS 30  38  38  HIS HIS A . n 
A 1 31  ALA 31  39  39  ALA ALA A . n 
A 1 32  GLN 32  40  40  GLN GLN A . n 
A 1 33  ASP 33  41  41  ASP ASP A . n 
A 1 34  ILE 34  42  42  ILE ILE A . n 
A 1 35  LEU 35  43  43  LEU LEU A . n 
A 1 36  GLU 36  44  44  GLU GLU A . n 
A 1 37  LYS 37  45  45  LYS LYS A . n 
A 1 38  THR 38  46  46  THR THR A . n 
A 1 39  HIS 39  47  47  HIS HIS A . n 
A 1 40  ASN 40  48  48  ASN ASN A . n 
A 1 41  GLY 41  49  49  GLY GLY A . n 
A 1 42  ARG 42  50  50  ARG ARG A . n 
A 1 43  LEU 43  51  51  LEU LEU A . n 
A 1 44  CYS 44  52  52  CYS CYS A . n 
A 1 45  ASP 45  53  53  ASP ASP A . n 
A 1 46  LEU 46  54  54  LEU LEU A . n 
A 1 47  ASN 47  55  55  ASN ASN A . n 
A 1 48  GLY 48  55  55  GLY GLY A A n 
A 1 49  VAL 49  56  56  VAL VAL A . n 
A 1 50  LYS 50  57  57  LYS LYS A . n 
A 1 51  PRO 51  58  58  PRO PRO A . n 
A 1 52  LEU 52  59  59  LEU LEU A . n 
A 1 53  ILE 53  60  60  ILE ILE A . n 
A 1 54  LEU 54  61  61  LEU LEU A . n 
A 1 55  LYS 55  62  62  LYS LYS A . n 
A 1 56  ASP 56  63  63  ASP ASP A . n 
A 1 57  CYS 57  64  64  CYS CYS A . n 
A 1 58  SER 58  65  65  SER SER A . n 
A 1 59  VAL 59  66  66  VAL VAL A . n 
A 1 60  ALA 60  67  67  ALA ALA A . n 
A 1 61  GLY 61  68  68  GLY GLY A . n 
A 1 62  TRP 62  69  69  TRP TRP A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  LEU 64  71  71  LEU LEU A . n 
A 1 65  GLY 65  72  72  GLY GLY A . n 
A 1 66  ASN 66  73  73  ASN ASN A . n 
A 1 67  PRO 67  74  74  PRO PRO A . n 
A 1 68  MET 68  75  75  MET MET A . n 
A 1 69  CYS 69  76  76  CYS CYS A . n 
A 1 70  ASP 70  77  77  ASP ASP A . n 
A 1 71  GLU 71  78  78  GLU GLU A . n 
A 1 72  PHE 72  79  79  PHE PHE A . n 
A 1 73  ILE 73  80  80  ILE ILE A . n 
A 1 74  ARG 74  81  81  ARG ARG A . n 
A 1 75  VAL 75  82  82  VAL VAL A . n 
A 1 76  PRO 76  83  83  PRO PRO A . n 
A 1 77  GLU 77  83  83  GLU GLU A A n 
A 1 78  TRP 78  84  84  TRP TRP A . n 
A 1 79  SER 79  85  85  SER SER A . n 
A 1 80  TYR 80  86  86  TYR TYR A . n 
A 1 81  ILE 81  87  87  ILE ILE A . n 
A 1 82  VAL 82  88  88  VAL VAL A . n 
A 1 83  GLU 83  89  89  GLU GLU A . n 
A 1 84  ARG 84  90  90  ARG ARG A . n 
A 1 85  THR 85  91  91  THR THR A . n 
A 1 86  ASN 86  92  92  ASN ASN A . n 
A 1 87  PRO 87  93  93  PRO PRO A . n 
A 1 88  ALA 88  94  94  ALA ALA A . n 
A 1 89  ASN 89  95  95  ASN ASN A . n 
A 1 90  ASP 90  96  96  ASP ASP A . n 
A 1 91  LEU 91  96  96  LEU LEU A A n 
A 1 92  CYS 92  97  97  CYS CYS A . n 
A 1 93  TYR 93  98  98  TYR TYR A . n 
A 1 94  PRO 94  99  99  PRO PRO A . n 
A 1 95  GLY 95  100 100 GLY GLY A . n 
A 1 96  ASN 96  101 101 ASN ASN A . n 
A 1 97  LEU 97  102 102 LEU LEU A . n 
A 1 98  ASN 98  103 103 ASN ASN A . n 
A 1 99  ASP 99  104 104 ASP ASP A . n 
A 1 100 TYR 100 105 105 TYR TYR A . n 
A 1 101 GLU 101 106 106 GLU GLU A . n 
A 1 102 GLU 102 107 107 GLU GLU A . n 
A 1 103 LEU 103 108 108 LEU LEU A . n 
A 1 104 LYS 104 109 109 LYS LYS A . n 
A 1 105 HIS 105 110 110 HIS HIS A . n 
A 1 106 LEU 106 111 111 LEU LEU A . n 
A 1 107 LEU 107 112 112 LEU LEU A . n 
A 1 108 SER 108 113 113 SER SER A . n 
A 1 109 ARG 109 114 114 ARG ARG A . n 
A 1 110 ILE 110 115 115 ILE ILE A . n 
A 1 111 ASN 111 116 116 ASN ASN A . n 
A 1 112 HIS 112 117 117 HIS HIS A . n 
A 1 113 PHE 113 118 118 PHE PHE A . n 
A 1 114 GLU 114 119 119 GLU GLU A . n 
A 1 115 LYS 115 120 120 LYS LYS A . n 
A 1 116 THR 116 121 121 THR THR A . n 
A 1 117 LEU 117 122 122 LEU LEU A . n 
A 1 118 ILE 118 123 123 ILE ILE A . n 
A 1 119 ILE 119 124 124 ILE ILE A . n 
A 1 120 PRO 120 125 125 PRO PRO A . n 
A 1 121 LYS 121 125 125 LYS LYS A A n 
A 1 122 SER 122 125 125 SER SER A B n 
A 1 123 SER 123 126 126 SER SER A . n 
A 1 124 TRP 124 127 127 TRP TRP A . n 
A 1 125 PRO 125 128 128 PRO PRO A . n 
A 1 126 ASN 126 129 129 ASN ASN A . n 
A 1 127 HIS 127 130 130 HIS HIS A . n 
A 1 128 GLU 128 131 131 GLU GLU A . n 
A 1 129 THR 129 132 132 THR THR A . n 
A 1 130 SER 130 133 133 SER SER A . n 
A 1 131 GLY 131 134 134 GLY GLY A . n 
A 1 132 VAL 132 135 135 VAL VAL A . n 
A 1 133 SER 133 136 136 SER SER A . n 
A 1 134 ALA 134 137 137 ALA ALA A . n 
A 1 135 ALA 135 138 138 ALA ALA A . n 
A 1 136 CYS 136 139 139 CYS CYS A . n 
A 1 137 PRO 137 140 140 PRO PRO A . n 
A 1 138 TYR 138 141 141 TYR TYR A . n 
A 1 139 GLN 139 142 142 GLN GLN A . n 
A 1 140 GLY 140 143 143 GLY GLY A . n 
A 1 141 VAL 141 144 144 VAL VAL A . n 
A 1 142 PRO 142 145 145 PRO PRO A . n 
A 1 143 SER 143 146 146 SER SER A . n 
A 1 144 PHE 144 147 147 PHE PHE A . n 
A 1 145 PHE 145 148 148 PHE PHE A . n 
A 1 146 ARG 146 149 149 ARG ARG A . n 
A 1 147 ASN 147 150 150 ASN ASN A . n 
A 1 148 VAL 148 151 151 VAL VAL A . n 
A 1 149 VAL 149 152 152 VAL VAL A . n 
A 1 150 TRP 150 153 153 TRP TRP A . n 
A 1 151 LEU 151 154 154 LEU LEU A . n 
A 1 152 THR 152 155 155 THR THR A . n 
A 1 153 LYS 153 156 156 LYS LYS A . n 
A 1 154 LYS 154 157 157 LYS LYS A . n 
A 1 155 ASN 155 158 158 ASN ASN A . n 
A 1 156 ASP 156 159 159 ASP ASP A . n 
A 1 157 ALA 157 160 160 ALA ALA A . n 
A 1 158 TYR 158 161 161 TYR TYR A . n 
A 1 159 PRO 159 162 162 PRO PRO A . n 
A 1 160 THR 160 163 163 THR THR A . n 
A 1 161 ILE 161 164 164 ILE ILE A . n 
A 1 162 LYS 162 165 165 LYS LYS A . n 
A 1 163 MET 163 166 166 MET MET A . n 
A 1 164 SER 164 167 167 SER SER A . n 
A 1 165 TYR 165 168 168 TYR TYR A . n 
A 1 166 ASN 166 169 169 ASN ASN A . n 
A 1 167 ASN 167 170 170 ASN ASN A . n 
A 1 168 THR 168 171 171 THR THR A . n 
A 1 169 ASN 169 172 172 ASN ASN A . n 
A 1 170 GLY 170 173 173 GLY GLY A . n 
A 1 171 GLU 171 174 174 GLU GLU A . n 
A 1 172 ASP 172 175 175 ASP ASP A . n 
A 1 173 LEU 173 176 176 LEU LEU A . n 
A 1 174 LEU 174 177 177 LEU LEU A . n 
A 1 175 ILE 175 178 178 ILE ILE A . n 
A 1 176 LEU 176 179 179 LEU LEU A . n 
A 1 177 TRP 177 180 180 TRP TRP A . n 
A 1 178 GLY 178 181 181 GLY GLY A . n 
A 1 179 ILE 179 182 182 ILE ILE A . n 
A 1 180 HIS 180 183 183 HIS HIS A . n 
A 1 181 HIS 181 184 184 HIS HIS A . n 
A 1 182 SER 182 185 185 SER SER A . n 
A 1 183 ASN 183 186 186 ASN ASN A . n 
A 1 184 ASN 184 187 187 ASN ASN A . n 
A 1 185 ALA 185 188 188 ALA ALA A . n 
A 1 186 ALA 186 189 189 ALA ALA A . n 
A 1 187 GLU 187 190 190 GLU GLU A . n 
A 1 188 GLN 188 191 191 GLN GLN A . n 
A 1 189 ILE 189 192 192 ILE ILE A . n 
A 1 190 ASN 190 193 193 ASN ASN A . n 
A 1 191 LEU 191 194 194 LEU LEU A . n 
A 1 192 TYR 192 195 195 TYR TYR A . n 
A 1 193 LYS 193 196 196 LYS LYS A . n 
A 1 194 ASN 194 197 197 ASN ASN A . n 
A 1 195 PRO 195 198 198 PRO PRO A . n 
A 1 196 THR 196 199 199 THR THR A . n 
A 1 197 THR 197 200 200 THR THR A . n 
A 1 198 TYR 198 201 201 TYR TYR A . n 
A 1 199 VAL 199 202 202 VAL VAL A . n 
A 1 200 SER 200 203 203 SER SER A . n 
A 1 201 VAL 201 204 204 VAL VAL A . n 
A 1 202 GLY 202 205 205 GLY GLY A . n 
A 1 203 THR 203 206 206 THR THR A . n 
A 1 204 SER 204 207 207 SER SER A . n 
A 1 205 THR 205 208 208 THR THR A . n 
A 1 206 LEU 206 209 209 LEU LEU A . n 
A 1 207 ASN 207 210 210 ASN ASN A . n 
A 1 208 GLN 208 211 211 GLN GLN A . n 
A 1 209 ARG 209 212 212 ARG ARG A . n 
A 1 210 LEU 210 213 213 LEU LEU A . n 
A 1 211 VAL 211 214 214 VAL VAL A . n 
A 1 212 PRO 212 215 215 PRO PRO A . n 
A 1 213 LYS 213 216 216 LYS LYS A . n 
A 1 214 ILE 214 217 217 ILE ILE A . n 
A 1 215 ALA 215 218 218 ALA ALA A . n 
A 1 216 THR 216 219 219 THR THR A . n 
A 1 217 ARG 217 220 220 ARG ARG A . n 
A 1 218 SER 218 221 221 SER SER A . n 
A 1 219 GLN 219 222 222 GLN GLN A . n 
A 1 220 VAL 220 223 223 VAL VAL A . n 
A 1 221 ASN 221 224 224 ASN ASN A . n 
A 1 222 GLY 222 225 225 GLY GLY A . n 
A 1 223 LEU 223 226 226 LEU LEU A . n 
A 1 224 GLN 224 227 227 GLN GLN A . n 
A 1 225 GLY 225 228 228 GLY GLY A . n 
A 1 226 ARG 226 229 229 ARG ARG A . n 
A 1 227 MET 227 230 230 MET MET A . n 
A 1 228 ASP 228 231 231 ASP ASP A . n 
A 1 229 PHE 229 232 232 PHE PHE A . n 
A 1 230 PHE 230 233 233 PHE PHE A . n 
A 1 231 TRP 231 234 234 TRP TRP A . n 
A 1 232 THR 232 235 235 THR THR A . n 
A 1 233 ILE 233 236 236 ILE ILE A . n 
A 1 234 LEU 234 237 237 LEU LEU A . n 
A 1 235 LYS 235 238 238 LYS LYS A . n 
A 1 236 PRO 236 239 239 PRO PRO A . n 
A 1 237 ASN 237 240 240 ASN ASN A . n 
A 1 238 ASP 238 241 241 ASP ASP A . n 
A 1 239 ALA 239 242 242 ALA ALA A . n 
A 1 240 ILE 240 243 243 ILE ILE A . n 
A 1 241 HIS 241 244 244 HIS HIS A . n 
A 1 242 PHE 242 245 245 PHE PHE A . n 
A 1 243 GLU 243 246 246 GLU GLU A . n 
A 1 244 SER 244 247 247 SER SER A . n 
A 1 245 ASN 245 248 248 ASN ASN A . n 
A 1 246 GLY 246 249 249 GLY GLY A . n 
A 1 247 ASN 247 250 250 ASN ASN A . n 
A 1 248 PHE 248 251 251 PHE PHE A . n 
A 1 249 ILE 249 252 252 ILE ILE A . n 
A 1 250 ALA 250 253 253 ALA ALA A . n 
A 1 251 PRO 251 254 254 PRO PRO A . n 
A 1 252 GLU 252 255 255 GLU GLU A . n 
A 1 253 TYR 253 256 256 TYR TYR A . n 
A 1 254 ALA 254 257 257 ALA ALA A . n 
A 1 255 TYR 255 258 258 TYR TYR A . n 
A 1 256 LYS 256 259 259 LYS LYS A . n 
A 1 257 ILE 257 260 260 ILE ILE A . n 
A 1 258 VAL 258 260 260 VAL VAL A A n 
A 1 259 LYS 259 261 261 LYS LYS A . n 
A 1 260 LYS 260 262 262 LYS LYS A . n 
A 1 261 GLY 261 263 263 GLY GLY A . n 
A 1 262 ASP 262 264 264 ASP ASP A . n 
A 1 263 SER 263 265 265 SER SER A . n 
A 1 264 THR 264 266 266 THR THR A . n 
A 1 265 ILE 265 267 267 ILE ILE A . n 
A 1 266 MET 266 268 268 MET MET A . n 
A 1 267 LYS 267 269 269 LYS LYS A . n 
A 1 268 SER 268 270 270 SER SER A . n 
A 1 269 GLU 269 271 271 GLU GLU A . n 
A 1 270 MET 270 272 272 MET MET A . n 
A 1 271 GLU 271 273 273 GLU GLU A . n 
A 1 272 TYR 272 274 274 TYR TYR A . n 
A 1 273 GLY 273 275 275 GLY GLY A . n 
A 1 274 HIS 274 276 276 HIS HIS A . n 
A 1 275 CYS 275 277 277 CYS CYS A . n 
A 1 276 ASN 276 278 278 ASN ASN A . n 
A 1 277 THR 277 279 279 THR THR A . n 
A 1 278 LYS 278 280 280 LYS LYS A . n 
A 1 279 CYS 279 281 281 CYS CYS A . n 
A 1 280 GLN 280 282 282 GLN GLN A . n 
A 1 281 THR 281 283 283 THR THR A . n 
A 1 282 PRO 282 284 284 PRO PRO A . n 
A 1 283 ILE 283 285 285 ILE ILE A . n 
A 1 284 GLY 284 286 286 GLY GLY A . n 
A 1 285 ALA 285 287 287 ALA ALA A . n 
A 1 286 ILE 286 288 288 ILE ILE A . n 
A 1 287 ASN 287 289 289 ASN ASN A . n 
A 1 288 SER 288 290 290 SER SER A . n 
A 1 289 SER 289 291 291 SER SER A . n 
A 1 290 MET 290 292 292 MET MET A . n 
A 1 291 PRO 291 293 293 PRO PRO A . n 
A 1 292 PHE 292 294 294 PHE PHE A . n 
A 1 293 HIS 293 295 295 HIS HIS A . n 
A 1 294 ASN 294 296 296 ASN ASN A . n 
A 1 295 ILE 295 297 297 ILE ILE A . n 
A 1 296 HIS 296 298 298 HIS HIS A . n 
A 1 297 PRO 297 299 299 PRO PRO A . n 
A 1 298 LEU 298 300 300 LEU LEU A . n 
A 1 299 THR 299 301 301 THR THR A . n 
A 1 300 ILE 300 302 302 ILE ILE A . n 
A 1 301 GLY 301 303 303 GLY GLY A . n 
A 1 302 GLU 302 304 304 GLU GLU A . n 
A 1 303 CYS 303 305 305 CYS CYS A . n 
A 1 304 PRO 304 306 306 PRO PRO A . n 
A 1 305 LYS 305 307 307 LYS LYS A . n 
A 1 306 TYR 306 308 308 TYR TYR A . n 
A 1 307 VAL 307 309 309 VAL VAL A . n 
A 1 308 LYS 308 310 310 LYS LYS A . n 
A 1 309 SER 309 311 311 SER SER A . n 
A 1 310 ASN 310 312 312 ASN ASN A . n 
A 1 311 LYS 311 313 313 LYS LYS A . n 
A 1 312 LEU 312 314 314 LEU LEU A . n 
A 1 313 VAL 313 315 315 VAL VAL A . n 
A 1 314 LEU 314 316 316 LEU LEU A . n 
A 1 315 ALA 315 317 317 ALA ALA A . n 
A 1 316 THR 316 318 318 THR THR A . n 
A 1 317 GLY 317 319 319 GLY GLY A . n 
A 1 318 LEU 318 320 320 LEU LEU A . n 
A 1 319 ARG 319 321 321 ARG ARG A . n 
A 1 320 ASN 320 322 322 ASN ASN A . n 
A 1 321 SER 321 323 323 SER SER A . n 
A 1 322 PRO 322 324 ?   ?   ?   A . n 
A 1 323 LEU 323 325 ?   ?   ?   A . n 
A 1 324 ARG 324 326 ?   ?   ?   A . n 
B 2 1   GLY 1   1   1   GLY GLY B . n 
B 2 2   LEU 2   2   2   LEU LEU B . n 
B 2 3   PHE 3   3   3   PHE PHE B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   ALA 5   5   5   ALA ALA 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  ARG 38  38  38  ARG ARG 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   PRO 1   9   ?   ?   ?   C . n 
C 1 2   GLY 2   10  10  GLY GLY C . n 
C 1 3   ASP 3   11  11  ASP ASP C . n 
C 1 4   GLN 4   12  12  GLN GLN C . n 
C 1 5   ILE 5   13  13  ILE ILE C . n 
C 1 6   CYS 6   14  14  CYS CYS C . n 
C 1 7   ILE 7   15  15  ILE ILE C . n 
C 1 8   GLY 8   16  16  GLY GLY C . n 
C 1 9   TYR 9   17  17  TYR TYR C . n 
C 1 10  HIS 10  18  18  HIS HIS C . n 
C 1 11  ALA 11  19  19  ALA ALA C . n 
C 1 12  ASN 12  20  20  ASN ASN C . n 
C 1 13  ASN 13  21  21  ASN ASN C . n 
C 1 14  SER 14  22  22  SER SER C . n 
C 1 15  THR 15  23  23  THR THR C . n 
C 1 16  GLU 16  24  24  GLU GLU C . n 
C 1 17  GLN 17  25  25  GLN GLN C . n 
C 1 18  VAL 18  26  26  VAL VAL C . n 
C 1 19  ASP 19  27  27  ASP ASP C . n 
C 1 20  THR 20  28  28  THR THR C . n 
C 1 21  ILE 21  29  29  ILE ILE C . n 
C 1 22  MET 22  30  30  MET MET C . n 
C 1 23  GLU 23  31  31  GLU GLU C . n 
C 1 24  LYS 24  32  32  LYS LYS C . n 
C 1 25  ASN 25  33  33  ASN ASN C . n 
C 1 26  VAL 26  34  34  VAL VAL C . n 
C 1 27  THR 27  35  35  THR THR C . n 
C 1 28  VAL 28  36  36  VAL VAL C . n 
C 1 29  THR 29  37  37  THR THR C . n 
C 1 30  HIS 30  38  38  HIS HIS C . n 
C 1 31  ALA 31  39  39  ALA ALA C . n 
C 1 32  GLN 32  40  40  GLN GLN C . n 
C 1 33  ASP 33  41  41  ASP ASP C . n 
C 1 34  ILE 34  42  42  ILE ILE C . n 
C 1 35  LEU 35  43  43  LEU LEU C . n 
C 1 36  GLU 36  44  44  GLU GLU C . n 
C 1 37  LYS 37  45  45  LYS LYS C . n 
C 1 38  THR 38  46  46  THR THR C . n 
C 1 39  HIS 39  47  47  HIS HIS C . n 
C 1 40  ASN 40  48  48  ASN ASN C . n 
C 1 41  GLY 41  49  49  GLY GLY C . n 
C 1 42  ARG 42  50  50  ARG ARG C . n 
C 1 43  LEU 43  51  51  LEU LEU C . n 
C 1 44  CYS 44  52  52  CYS CYS C . n 
C 1 45  ASP 45  53  53  ASP ASP C . n 
C 1 46  LEU 46  54  54  LEU LEU C . n 
C 1 47  ASN 47  55  55  ASN ASN C . n 
C 1 48  GLY 48  55  55  GLY GLY C A n 
C 1 49  VAL 49  56  56  VAL VAL C . n 
C 1 50  LYS 50  57  57  LYS LYS C . n 
C 1 51  PRO 51  58  58  PRO PRO C . n 
C 1 52  LEU 52  59  59  LEU LEU C . n 
C 1 53  ILE 53  60  60  ILE ILE C . n 
C 1 54  LEU 54  61  61  LEU LEU C . n 
C 1 55  LYS 55  62  62  LYS LYS C . n 
C 1 56  ASP 56  63  63  ASP ASP C . n 
C 1 57  CYS 57  64  64  CYS CYS C . n 
C 1 58  SER 58  65  65  SER SER C . n 
C 1 59  VAL 59  66  66  VAL VAL C . n 
C 1 60  ALA 60  67  67  ALA ALA C . n 
C 1 61  GLY 61  68  68  GLY GLY C . n 
C 1 62  TRP 62  69  69  TRP TRP C . n 
C 1 63  LEU 63  70  70  LEU LEU C . n 
C 1 64  LEU 64  71  71  LEU LEU C . n 
C 1 65  GLY 65  72  72  GLY GLY C . n 
C 1 66  ASN 66  73  73  ASN ASN C . n 
C 1 67  PRO 67  74  74  PRO PRO C . n 
C 1 68  MET 68  75  75  MET MET C . n 
C 1 69  CYS 69  76  76  CYS CYS C . n 
C 1 70  ASP 70  77  77  ASP ASP C . n 
C 1 71  GLU 71  78  78  GLU GLU C . n 
C 1 72  PHE 72  79  79  PHE PHE C . n 
C 1 73  ILE 73  80  80  ILE ILE C . n 
C 1 74  ARG 74  81  81  ARG ARG C . n 
C 1 75  VAL 75  82  82  VAL VAL C . n 
C 1 76  PRO 76  83  83  PRO PRO C . n 
C 1 77  GLU 77  83  83  GLU GLU C A n 
C 1 78  TRP 78  84  84  TRP TRP C . n 
C 1 79  SER 79  85  85  SER SER C . n 
C 1 80  TYR 80  86  86  TYR TYR C . n 
C 1 81  ILE 81  87  87  ILE ILE C . n 
C 1 82  VAL 82  88  88  VAL VAL C . n 
C 1 83  GLU 83  89  89  GLU GLU C . n 
C 1 84  ARG 84  90  90  ARG ARG C . n 
C 1 85  THR 85  91  91  THR THR C . n 
C 1 86  ASN 86  92  92  ASN ASN C . n 
C 1 87  PRO 87  93  93  PRO PRO C . n 
C 1 88  ALA 88  94  94  ALA ALA C . n 
C 1 89  ASN 89  95  95  ASN ASN C . n 
C 1 90  ASP 90  96  96  ASP ASP C . n 
C 1 91  LEU 91  96  96  LEU LEU C A n 
C 1 92  CYS 92  97  97  CYS CYS C . n 
C 1 93  TYR 93  98  98  TYR TYR C . n 
C 1 94  PRO 94  99  99  PRO PRO C . n 
C 1 95  GLY 95  100 100 GLY GLY C . n 
C 1 96  ASN 96  101 101 ASN ASN C . n 
C 1 97  LEU 97  102 102 LEU LEU C . n 
C 1 98  ASN 98  103 103 ASN ASN C . n 
C 1 99  ASP 99  104 104 ASP ASP C . n 
C 1 100 TYR 100 105 105 TYR TYR C . n 
C 1 101 GLU 101 106 106 GLU GLU C . n 
C 1 102 GLU 102 107 107 GLU GLU C . n 
C 1 103 LEU 103 108 108 LEU LEU C . n 
C 1 104 LYS 104 109 109 LYS LYS C . n 
C 1 105 HIS 105 110 110 HIS HIS C . n 
C 1 106 LEU 106 111 111 LEU LEU C . n 
C 1 107 LEU 107 112 112 LEU LEU C . n 
C 1 108 SER 108 113 113 SER SER C . n 
C 1 109 ARG 109 114 114 ARG ARG C . n 
C 1 110 ILE 110 115 115 ILE ILE C . n 
C 1 111 ASN 111 116 116 ASN ASN C . n 
C 1 112 HIS 112 117 117 HIS HIS C . n 
C 1 113 PHE 113 118 118 PHE PHE C . n 
C 1 114 GLU 114 119 119 GLU GLU C . n 
C 1 115 LYS 115 120 120 LYS LYS C . n 
C 1 116 THR 116 121 121 THR THR C . n 
C 1 117 LEU 117 122 122 LEU LEU C . n 
C 1 118 ILE 118 123 123 ILE ILE C . n 
C 1 119 ILE 119 124 124 ILE ILE C . n 
C 1 120 PRO 120 125 125 PRO PRO C . n 
C 1 121 LYS 121 125 125 LYS LYS C A n 
C 1 122 SER 122 125 125 SER SER C B n 
C 1 123 SER 123 126 126 SER SER C . n 
C 1 124 TRP 124 127 127 TRP TRP C . n 
C 1 125 PRO 125 128 128 PRO PRO C . n 
C 1 126 ASN 126 129 129 ASN ASN C . n 
C 1 127 HIS 127 130 130 HIS HIS C . n 
C 1 128 GLU 128 131 131 GLU GLU C . n 
C 1 129 THR 129 132 132 THR THR C . n 
C 1 130 SER 130 133 133 SER SER C . n 
C 1 131 GLY 131 134 134 GLY GLY C . n 
C 1 132 VAL 132 135 135 VAL VAL C . n 
C 1 133 SER 133 136 136 SER SER C . n 
C 1 134 ALA 134 137 137 ALA ALA C . n 
C 1 135 ALA 135 138 138 ALA ALA C . n 
C 1 136 CYS 136 139 139 CYS CYS C . n 
C 1 137 PRO 137 140 140 PRO PRO C . n 
C 1 138 TYR 138 141 141 TYR TYR C . n 
C 1 139 GLN 139 142 142 GLN GLN C . n 
C 1 140 GLY 140 143 143 GLY GLY C . n 
C 1 141 VAL 141 144 144 VAL VAL C . n 
C 1 142 PRO 142 145 145 PRO PRO C . n 
C 1 143 SER 143 146 146 SER SER C . n 
C 1 144 PHE 144 147 147 PHE PHE C . n 
C 1 145 PHE 145 148 148 PHE PHE C . n 
C 1 146 ARG 146 149 149 ARG ARG C . n 
C 1 147 ASN 147 150 150 ASN ASN C . n 
C 1 148 VAL 148 151 151 VAL VAL C . n 
C 1 149 VAL 149 152 152 VAL VAL C . n 
C 1 150 TRP 150 153 153 TRP TRP C . n 
C 1 151 LEU 151 154 154 LEU LEU C . n 
C 1 152 THR 152 155 155 THR THR C . n 
C 1 153 LYS 153 156 156 LYS LYS C . n 
C 1 154 LYS 154 157 157 LYS LYS C . n 
C 1 155 ASN 155 158 158 ASN ASN C . n 
C 1 156 ASP 156 159 159 ASP ASP C . n 
C 1 157 ALA 157 160 160 ALA ALA C . n 
C 1 158 TYR 158 161 161 TYR TYR C . n 
C 1 159 PRO 159 162 162 PRO PRO C . n 
C 1 160 THR 160 163 163 THR THR C . n 
C 1 161 ILE 161 164 164 ILE ILE C . n 
C 1 162 LYS 162 165 165 LYS LYS C . n 
C 1 163 MET 163 166 166 MET MET C . n 
C 1 164 SER 164 167 167 SER SER C . n 
C 1 165 TYR 165 168 168 TYR TYR C . n 
C 1 166 ASN 166 169 169 ASN ASN C . n 
C 1 167 ASN 167 170 170 ASN ASN C . n 
C 1 168 THR 168 171 171 THR THR C . n 
C 1 169 ASN 169 172 172 ASN ASN C . n 
C 1 170 GLY 170 173 173 GLY GLY C . n 
C 1 171 GLU 171 174 174 GLU GLU C . n 
C 1 172 ASP 172 175 175 ASP ASP C . n 
C 1 173 LEU 173 176 176 LEU LEU C . n 
C 1 174 LEU 174 177 177 LEU LEU C . n 
C 1 175 ILE 175 178 178 ILE ILE C . n 
C 1 176 LEU 176 179 179 LEU LEU C . n 
C 1 177 TRP 177 180 180 TRP TRP C . n 
C 1 178 GLY 178 181 181 GLY GLY C . n 
C 1 179 ILE 179 182 182 ILE ILE C . n 
C 1 180 HIS 180 183 183 HIS HIS C . n 
C 1 181 HIS 181 184 184 HIS HIS C . n 
C 1 182 SER 182 185 185 SER SER C . n 
C 1 183 ASN 183 186 186 ASN ASN C . n 
C 1 184 ASN 184 187 187 ASN ASN C . n 
C 1 185 ALA 185 188 188 ALA ALA C . n 
C 1 186 ALA 186 189 189 ALA ALA C . n 
C 1 187 GLU 187 190 190 GLU GLU C . n 
C 1 188 GLN 188 191 191 GLN GLN C . n 
C 1 189 ILE 189 192 192 ILE ILE C . n 
C 1 190 ASN 190 193 193 ASN ASN C . n 
C 1 191 LEU 191 194 194 LEU LEU C . n 
C 1 192 TYR 192 195 195 TYR TYR C . n 
C 1 193 LYS 193 196 196 LYS LYS C . n 
C 1 194 ASN 194 197 197 ASN ASN C . n 
C 1 195 PRO 195 198 198 PRO PRO C . n 
C 1 196 THR 196 199 199 THR THR C . n 
C 1 197 THR 197 200 200 THR THR C . n 
C 1 198 TYR 198 201 201 TYR TYR C . n 
C 1 199 VAL 199 202 202 VAL VAL C . n 
C 1 200 SER 200 203 203 SER SER C . n 
C 1 201 VAL 201 204 204 VAL VAL C . n 
C 1 202 GLY 202 205 205 GLY GLY C . n 
C 1 203 THR 203 206 206 THR THR C . n 
C 1 204 SER 204 207 207 SER SER C . n 
C 1 205 THR 205 208 208 THR THR C . n 
C 1 206 LEU 206 209 209 LEU LEU C . n 
C 1 207 ASN 207 210 210 ASN ASN C . n 
C 1 208 GLN 208 211 211 GLN GLN C . n 
C 1 209 ARG 209 212 212 ARG ARG C . n 
C 1 210 LEU 210 213 213 LEU LEU C . n 
C 1 211 VAL 211 214 214 VAL VAL C . n 
C 1 212 PRO 212 215 215 PRO PRO C . n 
C 1 213 LYS 213 216 216 LYS LYS C . n 
C 1 214 ILE 214 217 217 ILE ILE C . n 
C 1 215 ALA 215 218 218 ALA ALA C . n 
C 1 216 THR 216 219 219 THR THR C . n 
C 1 217 ARG 217 220 220 ARG ARG C . n 
C 1 218 SER 218 221 221 SER SER C . n 
C 1 219 GLN 219 222 222 GLN GLN C . n 
C 1 220 VAL 220 223 223 VAL VAL C . n 
C 1 221 ASN 221 224 224 ASN ASN C . n 
C 1 222 GLY 222 225 225 GLY GLY C . n 
C 1 223 LEU 223 226 226 LEU LEU C . n 
C 1 224 GLN 224 227 227 GLN GLN C . n 
C 1 225 GLY 225 228 228 GLY GLY C . n 
C 1 226 ARG 226 229 229 ARG ARG C . n 
C 1 227 MET 227 230 230 MET MET C . n 
C 1 228 ASP 228 231 231 ASP ASP C . n 
C 1 229 PHE 229 232 232 PHE PHE C . n 
C 1 230 PHE 230 233 233 PHE PHE C . n 
C 1 231 TRP 231 234 234 TRP TRP C . n 
C 1 232 THR 232 235 235 THR THR C . n 
C 1 233 ILE 233 236 236 ILE ILE C . n 
C 1 234 LEU 234 237 237 LEU LEU C . n 
C 1 235 LYS 235 238 238 LYS LYS C . n 
C 1 236 PRO 236 239 239 PRO PRO C . n 
C 1 237 ASN 237 240 240 ASN ASN C . n 
C 1 238 ASP 238 241 241 ASP ASP C . n 
C 1 239 ALA 239 242 242 ALA ALA C . n 
C 1 240 ILE 240 243 243 ILE ILE C . n 
C 1 241 HIS 241 244 244 HIS HIS C . n 
C 1 242 PHE 242 245 245 PHE PHE C . n 
C 1 243 GLU 243 246 246 GLU GLU C . n 
C 1 244 SER 244 247 247 SER SER C . n 
C 1 245 ASN 245 248 248 ASN ASN C . n 
C 1 246 GLY 246 249 249 GLY GLY C . n 
C 1 247 ASN 247 250 250 ASN ASN C . n 
C 1 248 PHE 248 251 251 PHE PHE C . n 
C 1 249 ILE 249 252 252 ILE ILE C . n 
C 1 250 ALA 250 253 253 ALA ALA C . n 
C 1 251 PRO 251 254 254 PRO PRO C . n 
C 1 252 GLU 252 255 255 GLU GLU C . n 
C 1 253 TYR 253 256 256 TYR TYR C . n 
C 1 254 ALA 254 257 257 ALA ALA C . n 
C 1 255 TYR 255 258 258 TYR TYR C . n 
C 1 256 LYS 256 259 259 LYS LYS C . n 
C 1 257 ILE 257 260 260 ILE ILE C . n 
C 1 258 VAL 258 260 260 VAL VAL C A n 
C 1 259 LYS 259 261 261 LYS LYS C . n 
C 1 260 LYS 260 262 262 LYS LYS C . n 
C 1 261 GLY 261 263 263 GLY GLY C . n 
C 1 262 ASP 262 264 264 ASP ASP C . n 
C 1 263 SER 263 265 265 SER SER C . n 
C 1 264 THR 264 266 266 THR THR C . n 
C 1 265 ILE 265 267 267 ILE ILE C . n 
C 1 266 MET 266 268 268 MET MET C . n 
C 1 267 LYS 267 269 269 LYS LYS C . n 
C 1 268 SER 268 270 270 SER SER C . n 
C 1 269 GLU 269 271 271 GLU GLU C . n 
C 1 270 MET 270 272 272 MET MET C . n 
C 1 271 GLU 271 273 273 GLU GLU C . n 
C 1 272 TYR 272 274 274 TYR TYR C . n 
C 1 273 GLY 273 275 275 GLY GLY C . n 
C 1 274 HIS 274 276 276 HIS HIS C . n 
C 1 275 CYS 275 277 277 CYS CYS C . n 
C 1 276 ASN 276 278 278 ASN ASN C . n 
C 1 277 THR 277 279 279 THR THR C . n 
C 1 278 LYS 278 280 280 LYS LYS C . n 
C 1 279 CYS 279 281 281 CYS CYS C . n 
C 1 280 GLN 280 282 282 GLN GLN C . n 
C 1 281 THR 281 283 283 THR THR C . n 
C 1 282 PRO 282 284 284 PRO PRO C . n 
C 1 283 ILE 283 285 285 ILE ILE C . n 
C 1 284 GLY 284 286 286 GLY GLY C . n 
C 1 285 ALA 285 287 287 ALA ALA C . n 
C 1 286 ILE 286 288 288 ILE ILE C . n 
C 1 287 ASN 287 289 289 ASN ASN C . n 
C 1 288 SER 288 290 290 SER SER C . n 
C 1 289 SER 289 291 291 SER SER C . n 
C 1 290 MET 290 292 292 MET MET C . n 
C 1 291 PRO 291 293 293 PRO PRO C . n 
C 1 292 PHE 292 294 294 PHE PHE C . n 
C 1 293 HIS 293 295 295 HIS HIS C . n 
C 1 294 ASN 294 296 296 ASN ASN C . n 
C 1 295 ILE 295 297 297 ILE ILE C . n 
C 1 296 HIS 296 298 298 HIS HIS C . n 
C 1 297 PRO 297 299 299 PRO PRO C . n 
C 1 298 LEU 298 300 300 LEU LEU C . n 
C 1 299 THR 299 301 301 THR THR C . n 
C 1 300 ILE 300 302 302 ILE ILE C . n 
C 1 301 GLY 301 303 303 GLY GLY C . n 
C 1 302 GLU 302 304 304 GLU GLU C . n 
C 1 303 CYS 303 305 305 CYS CYS C . n 
C 1 304 PRO 304 306 306 PRO PRO C . n 
C 1 305 LYS 305 307 307 LYS LYS C . n 
C 1 306 TYR 306 308 308 TYR TYR C . n 
C 1 307 VAL 307 309 309 VAL VAL C . n 
C 1 308 LYS 308 310 310 LYS LYS C . n 
C 1 309 SER 309 311 311 SER SER C . n 
C 1 310 ASN 310 312 312 ASN ASN C . n 
C 1 311 LYS 311 313 313 LYS LYS C . n 
C 1 312 LEU 312 314 314 LEU LEU C . n 
C 1 313 VAL 313 315 315 VAL VAL C . n 
C 1 314 LEU 314 316 316 LEU LEU C . n 
C 1 315 ALA 315 317 317 ALA ALA C . n 
C 1 316 THR 316 318 318 THR THR C . n 
C 1 317 GLY 317 319 319 GLY GLY C . n 
C 1 318 LEU 318 320 320 LEU LEU C . n 
C 1 319 ARG 319 321 321 ARG ARG C . n 
C 1 320 ASN 320 322 322 ASN ASN C . n 
C 1 321 SER 321 323 323 SER SER C . n 
C 1 322 PRO 322 324 324 PRO PRO C . n 
C 1 323 LEU 323 325 325 LEU LEU C . n 
C 1 324 ARG 324 326 326 ARG ARG C . n 
D 2 1   GLY 1   1   1   GLY GLY D . n 
D 2 2   LEU 2   2   2   LEU LEU D . n 
D 2 3   PHE 3   3   3   PHE PHE D . n 
D 2 4   GLY 4   4   4   GLY GLY D . n 
D 2 5   ALA 5   5   5   ALA ALA 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  ARG 38  38  38  ARG ARG 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   PRO 1   9   9   PRO PRO E . n 
E 1 2   GLY 2   10  10  GLY GLY E . n 
E 1 3   ASP 3   11  11  ASP ASP E . n 
E 1 4   GLN 4   12  12  GLN GLN E . n 
E 1 5   ILE 5   13  13  ILE ILE E . n 
E 1 6   CYS 6   14  14  CYS CYS E . n 
E 1 7   ILE 7   15  15  ILE ILE E . n 
E 1 8   GLY 8   16  16  GLY GLY E . n 
E 1 9   TYR 9   17  17  TYR TYR E . n 
E 1 10  HIS 10  18  18  HIS HIS E . n 
E 1 11  ALA 11  19  19  ALA ALA E . n 
E 1 12  ASN 12  20  20  ASN ASN E . n 
E 1 13  ASN 13  21  21  ASN ASN E . n 
E 1 14  SER 14  22  22  SER SER E . n 
E 1 15  THR 15  23  23  THR THR E . n 
E 1 16  GLU 16  24  24  GLU GLU E . n 
E 1 17  GLN 17  25  25  GLN GLN E . n 
E 1 18  VAL 18  26  26  VAL VAL E . n 
E 1 19  ASP 19  27  27  ASP ASP E . n 
E 1 20  THR 20  28  28  THR THR E . n 
E 1 21  ILE 21  29  29  ILE ILE E . n 
E 1 22  MET 22  30  30  MET MET E . n 
E 1 23  GLU 23  31  31  GLU GLU E . n 
E 1 24  LYS 24  32  32  LYS LYS E . n 
E 1 25  ASN 25  33  33  ASN ASN E . n 
E 1 26  VAL 26  34  34  VAL VAL E . n 
E 1 27  THR 27  35  35  THR THR E . n 
E 1 28  VAL 28  36  36  VAL VAL E . n 
E 1 29  THR 29  37  37  THR THR E . n 
E 1 30  HIS 30  38  38  HIS HIS E . n 
E 1 31  ALA 31  39  39  ALA ALA E . n 
E 1 32  GLN 32  40  40  GLN GLN E . n 
E 1 33  ASP 33  41  41  ASP ASP E . n 
E 1 34  ILE 34  42  42  ILE ILE E . n 
E 1 35  LEU 35  43  43  LEU LEU E . n 
E 1 36  GLU 36  44  44  GLU GLU E . n 
E 1 37  LYS 37  45  45  LYS LYS E . n 
E 1 38  THR 38  46  46  THR THR E . n 
E 1 39  HIS 39  47  47  HIS HIS E . n 
E 1 40  ASN 40  48  48  ASN ASN E . n 
E 1 41  GLY 41  49  49  GLY GLY E . n 
E 1 42  ARG 42  50  50  ARG ARG E . n 
E 1 43  LEU 43  51  51  LEU LEU E . n 
E 1 44  CYS 44  52  52  CYS CYS E . n 
E 1 45  ASP 45  53  53  ASP ASP E . n 
E 1 46  LEU 46  54  54  LEU LEU E . n 
E 1 47  ASN 47  55  55  ASN ASN E . n 
E 1 48  GLY 48  55  55  GLY GLY E A n 
E 1 49  VAL 49  56  56  VAL VAL E . n 
E 1 50  LYS 50  57  57  LYS LYS E . n 
E 1 51  PRO 51  58  58  PRO PRO E . n 
E 1 52  LEU 52  59  59  LEU LEU E . n 
E 1 53  ILE 53  60  60  ILE ILE E . n 
E 1 54  LEU 54  61  61  LEU LEU E . n 
E 1 55  LYS 55  62  62  LYS LYS E . n 
E 1 56  ASP 56  63  63  ASP ASP E . n 
E 1 57  CYS 57  64  64  CYS CYS E . n 
E 1 58  SER 58  65  65  SER SER E . n 
E 1 59  VAL 59  66  66  VAL VAL E . n 
E 1 60  ALA 60  67  67  ALA ALA E . n 
E 1 61  GLY 61  68  68  GLY GLY E . n 
E 1 62  TRP 62  69  69  TRP TRP E . n 
E 1 63  LEU 63  70  70  LEU LEU E . n 
E 1 64  LEU 64  71  71  LEU LEU E . n 
E 1 65  GLY 65  72  72  GLY GLY E . n 
E 1 66  ASN 66  73  73  ASN ASN E . n 
E 1 67  PRO 67  74  74  PRO PRO E . n 
E 1 68  MET 68  75  75  MET MET E . n 
E 1 69  CYS 69  76  76  CYS CYS E . n 
E 1 70  ASP 70  77  77  ASP ASP E . n 
E 1 71  GLU 71  78  78  GLU GLU E . n 
E 1 72  PHE 72  79  79  PHE PHE E . n 
E 1 73  ILE 73  80  80  ILE ILE E . n 
E 1 74  ARG 74  81  81  ARG ARG E . n 
E 1 75  VAL 75  82  82  VAL VAL E . n 
E 1 76  PRO 76  83  83  PRO PRO E . n 
E 1 77  GLU 77  83  83  GLU GLU E A n 
E 1 78  TRP 78  84  84  TRP TRP E . n 
E 1 79  SER 79  85  85  SER SER E . n 
E 1 80  TYR 80  86  86  TYR TYR E . n 
E 1 81  ILE 81  87  87  ILE ILE E . n 
E 1 82  VAL 82  88  88  VAL VAL E . n 
E 1 83  GLU 83  89  89  GLU GLU E . n 
E 1 84  ARG 84  90  90  ARG ARG E . n 
E 1 85  THR 85  91  91  THR THR E . n 
E 1 86  ASN 86  92  92  ASN ASN E . n 
E 1 87  PRO 87  93  93  PRO PRO E . n 
E 1 88  ALA 88  94  94  ALA ALA E . n 
E 1 89  ASN 89  95  95  ASN ASN E . n 
E 1 90  ASP 90  96  96  ASP ASP E . n 
E 1 91  LEU 91  96  96  LEU LEU E A n 
E 1 92  CYS 92  97  97  CYS CYS E . n 
E 1 93  TYR 93  98  98  TYR TYR E . n 
E 1 94  PRO 94  99  99  PRO PRO E . n 
E 1 95  GLY 95  100 100 GLY GLY E . n 
E 1 96  ASN 96  101 101 ASN ASN E . n 
E 1 97  LEU 97  102 102 LEU LEU E . n 
E 1 98  ASN 98  103 103 ASN ASN E . n 
E 1 99  ASP 99  104 104 ASP ASP E . n 
E 1 100 TYR 100 105 105 TYR TYR E . n 
E 1 101 GLU 101 106 106 GLU GLU E . n 
E 1 102 GLU 102 107 107 GLU GLU E . n 
E 1 103 LEU 103 108 108 LEU LEU E . n 
E 1 104 LYS 104 109 109 LYS LYS E . n 
E 1 105 HIS 105 110 110 HIS HIS E . n 
E 1 106 LEU 106 111 111 LEU LEU E . n 
E 1 107 LEU 107 112 112 LEU LEU E . n 
E 1 108 SER 108 113 113 SER SER E . n 
E 1 109 ARG 109 114 114 ARG ARG E . n 
E 1 110 ILE 110 115 115 ILE ILE E . n 
E 1 111 ASN 111 116 116 ASN ASN E . n 
E 1 112 HIS 112 117 117 HIS HIS E . n 
E 1 113 PHE 113 118 118 PHE PHE E . n 
E 1 114 GLU 114 119 119 GLU GLU E . n 
E 1 115 LYS 115 120 120 LYS LYS E . n 
E 1 116 THR 116 121 121 THR THR E . n 
E 1 117 LEU 117 122 122 LEU LEU E . n 
E 1 118 ILE 118 123 123 ILE ILE E . n 
E 1 119 ILE 119 124 124 ILE ILE E . n 
E 1 120 PRO 120 125 125 PRO PRO E . n 
E 1 121 LYS 121 125 125 LYS LYS E A n 
E 1 122 SER 122 125 125 SER SER E B n 
E 1 123 SER 123 126 126 SER SER E . n 
E 1 124 TRP 124 127 127 TRP TRP E . n 
E 1 125 PRO 125 128 128 PRO PRO E . n 
E 1 126 ASN 126 129 129 ASN ASN E . n 
E 1 127 HIS 127 130 130 HIS HIS E . n 
E 1 128 GLU 128 131 131 GLU GLU E . n 
E 1 129 THR 129 132 132 THR THR E . n 
E 1 130 SER 130 133 133 SER SER E . n 
E 1 131 GLY 131 134 134 GLY GLY E . n 
E 1 132 VAL 132 135 135 VAL VAL E . n 
E 1 133 SER 133 136 136 SER SER E . n 
E 1 134 ALA 134 137 137 ALA ALA E . n 
E 1 135 ALA 135 138 138 ALA ALA E . n 
E 1 136 CYS 136 139 139 CYS CYS E . n 
E 1 137 PRO 137 140 140 PRO PRO E . n 
E 1 138 TYR 138 141 141 TYR TYR E . n 
E 1 139 GLN 139 142 142 GLN GLN E . n 
E 1 140 GLY 140 143 143 GLY GLY E . n 
E 1 141 VAL 141 144 144 VAL VAL E . n 
E 1 142 PRO 142 145 145 PRO PRO E . n 
E 1 143 SER 143 146 146 SER SER E . n 
E 1 144 PHE 144 147 147 PHE PHE E . n 
E 1 145 PHE 145 148 148 PHE PHE E . n 
E 1 146 ARG 146 149 149 ARG ARG E . n 
E 1 147 ASN 147 150 150 ASN ASN E . n 
E 1 148 VAL 148 151 151 VAL VAL E . n 
E 1 149 VAL 149 152 152 VAL VAL E . n 
E 1 150 TRP 150 153 153 TRP TRP E . n 
E 1 151 LEU 151 154 154 LEU LEU E . n 
E 1 152 THR 152 155 155 THR THR E . n 
E 1 153 LYS 153 156 156 LYS LYS E . n 
E 1 154 LYS 154 157 157 LYS LYS E . n 
E 1 155 ASN 155 158 158 ASN ASN E . n 
E 1 156 ASP 156 159 159 ASP ASP E . n 
E 1 157 ALA 157 160 160 ALA ALA E . n 
E 1 158 TYR 158 161 161 TYR TYR E . n 
E 1 159 PRO 159 162 162 PRO PRO E . n 
E 1 160 THR 160 163 163 THR THR E . n 
E 1 161 ILE 161 164 164 ILE ILE E . n 
E 1 162 LYS 162 165 165 LYS LYS E . n 
E 1 163 MET 163 166 166 MET MET E . n 
E 1 164 SER 164 167 167 SER SER E . n 
E 1 165 TYR 165 168 168 TYR TYR E . n 
E 1 166 ASN 166 169 169 ASN ASN E . n 
E 1 167 ASN 167 170 170 ASN ASN E . n 
E 1 168 THR 168 171 171 THR THR E . n 
E 1 169 ASN 169 172 172 ASN ASN E . n 
E 1 170 GLY 170 173 173 GLY GLY E . n 
E 1 171 GLU 171 174 174 GLU GLU E . n 
E 1 172 ASP 172 175 175 ASP ASP E . n 
E 1 173 LEU 173 176 176 LEU LEU E . n 
E 1 174 LEU 174 177 177 LEU LEU E . n 
E 1 175 ILE 175 178 178 ILE ILE E . n 
E 1 176 LEU 176 179 179 LEU LEU E . n 
E 1 177 TRP 177 180 180 TRP TRP E . n 
E 1 178 GLY 178 181 181 GLY GLY E . n 
E 1 179 ILE 179 182 182 ILE ILE E . n 
E 1 180 HIS 180 183 183 HIS HIS E . n 
E 1 181 HIS 181 184 184 HIS HIS E . n 
E 1 182 SER 182 185 185 SER SER E . n 
E 1 183 ASN 183 186 186 ASN ASN E . n 
E 1 184 ASN 184 187 187 ASN ASN E . n 
E 1 185 ALA 185 188 188 ALA ALA E . n 
E 1 186 ALA 186 189 189 ALA ALA E . n 
E 1 187 GLU 187 190 190 GLU GLU E . n 
E 1 188 GLN 188 191 191 GLN GLN E . n 
E 1 189 ILE 189 192 192 ILE ILE E . n 
E 1 190 ASN 190 193 193 ASN ASN E . n 
E 1 191 LEU 191 194 194 LEU LEU E . n 
E 1 192 TYR 192 195 195 TYR TYR E . n 
E 1 193 LYS 193 196 196 LYS LYS E . n 
E 1 194 ASN 194 197 197 ASN ASN E . n 
E 1 195 PRO 195 198 198 PRO PRO E . n 
E 1 196 THR 196 199 199 THR THR E . n 
E 1 197 THR 197 200 200 THR THR E . n 
E 1 198 TYR 198 201 201 TYR TYR E . n 
E 1 199 VAL 199 202 202 VAL VAL E . n 
E 1 200 SER 200 203 203 SER SER E . n 
E 1 201 VAL 201 204 204 VAL VAL E . n 
E 1 202 GLY 202 205 205 GLY GLY E . n 
E 1 203 THR 203 206 206 THR THR E . n 
E 1 204 SER 204 207 207 SER SER E . n 
E 1 205 THR 205 208 208 THR THR E . n 
E 1 206 LEU 206 209 209 LEU LEU E . n 
E 1 207 ASN 207 210 210 ASN ASN E . n 
E 1 208 GLN 208 211 211 GLN GLN E . n 
E 1 209 ARG 209 212 212 ARG ARG E . n 
E 1 210 LEU 210 213 213 LEU LEU E . n 
E 1 211 VAL 211 214 214 VAL VAL E . n 
E 1 212 PRO 212 215 215 PRO PRO E . n 
E 1 213 LYS 213 216 216 LYS LYS E . n 
E 1 214 ILE 214 217 217 ILE ILE E . n 
E 1 215 ALA 215 218 218 ALA ALA E . n 
E 1 216 THR 216 219 219 THR THR E . n 
E 1 217 ARG 217 220 220 ARG ARG E . n 
E 1 218 SER 218 221 221 SER SER E . n 
E 1 219 GLN 219 222 222 GLN GLN E . n 
E 1 220 VAL 220 223 223 VAL VAL E . n 
E 1 221 ASN 221 224 224 ASN ASN E . n 
E 1 222 GLY 222 225 225 GLY GLY E . n 
E 1 223 LEU 223 226 226 LEU LEU E . n 
E 1 224 GLN 224 227 227 GLN GLN E . n 
E 1 225 GLY 225 228 228 GLY GLY E . n 
E 1 226 ARG 226 229 229 ARG ARG E . n 
E 1 227 MET 227 230 230 MET MET E . n 
E 1 228 ASP 228 231 231 ASP ASP E . n 
E 1 229 PHE 229 232 232 PHE PHE E . n 
E 1 230 PHE 230 233 233 PHE PHE E . n 
E 1 231 TRP 231 234 234 TRP TRP E . n 
E 1 232 THR 232 235 235 THR THR E . n 
E 1 233 ILE 233 236 236 ILE ILE E . n 
E 1 234 LEU 234 237 237 LEU LEU E . n 
E 1 235 LYS 235 238 238 LYS LYS E . n 
E 1 236 PRO 236 239 239 PRO PRO E . n 
E 1 237 ASN 237 240 240 ASN ASN E . n 
E 1 238 ASP 238 241 241 ASP ASP E . n 
E 1 239 ALA 239 242 242 ALA ALA E . n 
E 1 240 ILE 240 243 243 ILE ILE E . n 
E 1 241 HIS 241 244 244 HIS HIS E . n 
E 1 242 PHE 242 245 245 PHE PHE E . n 
E 1 243 GLU 243 246 246 GLU GLU E . n 
E 1 244 SER 244 247 247 SER SER E . n 
E 1 245 ASN 245 248 248 ASN ASN E . n 
E 1 246 GLY 246 249 249 GLY GLY E . n 
E 1 247 ASN 247 250 250 ASN ASN E . n 
E 1 248 PHE 248 251 251 PHE PHE E . n 
E 1 249 ILE 249 252 252 ILE ILE E . n 
E 1 250 ALA 250 253 253 ALA ALA E . n 
E 1 251 PRO 251 254 254 PRO PRO E . n 
E 1 252 GLU 252 255 255 GLU GLU E . n 
E 1 253 TYR 253 256 256 TYR TYR E . n 
E 1 254 ALA 254 257 257 ALA ALA E . n 
E 1 255 TYR 255 258 258 TYR TYR E . n 
E 1 256 LYS 256 259 259 LYS LYS E . n 
E 1 257 ILE 257 260 260 ILE ILE E . n 
E 1 258 VAL 258 260 260 VAL VAL E A n 
E 1 259 LYS 259 261 261 LYS LYS E . n 
E 1 260 LYS 260 262 262 LYS LYS E . n 
E 1 261 GLY 261 263 263 GLY GLY E . n 
E 1 262 ASP 262 264 264 ASP ASP E . n 
E 1 263 SER 263 265 265 SER SER E . n 
E 1 264 THR 264 266 266 THR THR E . n 
E 1 265 ILE 265 267 267 ILE ILE E . n 
E 1 266 MET 266 268 268 MET MET E . n 
E 1 267 LYS 267 269 269 LYS LYS E . n 
E 1 268 SER 268 270 270 SER SER E . n 
E 1 269 GLU 269 271 271 GLU GLU E . n 
E 1 270 MET 270 272 272 MET MET E . n 
E 1 271 GLU 271 273 273 GLU GLU E . n 
E 1 272 TYR 272 274 274 TYR TYR E . n 
E 1 273 GLY 273 275 275 GLY GLY E . n 
E 1 274 HIS 274 276 276 HIS HIS E . n 
E 1 275 CYS 275 277 277 CYS CYS E . n 
E 1 276 ASN 276 278 278 ASN ASN E . n 
E 1 277 THR 277 279 279 THR THR E . n 
E 1 278 LYS 278 280 280 LYS LYS E . n 
E 1 279 CYS 279 281 281 CYS CYS E . n 
E 1 280 GLN 280 282 282 GLN GLN E . n 
E 1 281 THR 281 283 283 THR THR E . n 
E 1 282 PRO 282 284 284 PRO PRO E . n 
E 1 283 ILE 283 285 285 ILE ILE E . n 
E 1 284 GLY 284 286 286 GLY GLY E . n 
E 1 285 ALA 285 287 287 ALA ALA E . n 
E 1 286 ILE 286 288 288 ILE ILE E . n 
E 1 287 ASN 287 289 289 ASN ASN E . n 
E 1 288 SER 288 290 290 SER SER E . n 
E 1 289 SER 289 291 291 SER SER E . n 
E 1 290 MET 290 292 292 MET MET E . n 
E 1 291 PRO 291 293 293 PRO PRO E . n 
E 1 292 PHE 292 294 294 PHE PHE E . n 
E 1 293 HIS 293 295 295 HIS HIS E . n 
E 1 294 ASN 294 296 296 ASN ASN E . n 
E 1 295 ILE 295 297 297 ILE ILE E . n 
E 1 296 HIS 296 298 298 HIS HIS E . n 
E 1 297 PRO 297 299 299 PRO PRO E . n 
E 1 298 LEU 298 300 300 LEU LEU E . n 
E 1 299 THR 299 301 301 THR THR E . n 
E 1 300 ILE 300 302 302 ILE ILE E . n 
E 1 301 GLY 301 303 303 GLY GLY E . n 
E 1 302 GLU 302 304 304 GLU GLU E . n 
E 1 303 CYS 303 305 305 CYS CYS E . n 
E 1 304 PRO 304 306 306 PRO PRO E . n 
E 1 305 LYS 305 307 307 LYS LYS E . n 
E 1 306 TYR 306 308 308 TYR TYR E . n 
E 1 307 VAL 307 309 309 VAL VAL E . n 
E 1 308 LYS 308 310 310 LYS LYS E . n 
E 1 309 SER 309 311 311 SER SER E . n 
E 1 310 ASN 310 312 312 ASN ASN E . n 
E 1 311 LYS 311 313 313 LYS LYS E . n 
E 1 312 LEU 312 314 314 LEU LEU E . n 
E 1 313 VAL 313 315 315 VAL VAL E . n 
E 1 314 LEU 314 316 316 LEU LEU E . n 
E 1 315 ALA 315 317 317 ALA ALA E . n 
E 1 316 THR 316 318 318 THR THR E . n 
E 1 317 GLY 317 319 319 GLY GLY E . n 
E 1 318 LEU 318 320 320 LEU LEU E . n 
E 1 319 ARG 319 321 321 ARG ARG E . n 
E 1 320 ASN 320 322 322 ASN ASN E . n 
E 1 321 SER 321 323 323 SER SER E . n 
E 1 322 PRO 322 324 ?   ?   ?   E . n 
E 1 323 LEU 323 325 ?   ?   ?   E . n 
E 1 324 ARG 324 326 ?   ?   ?   E . n 
F 2 1   GLY 1   1   1   GLY GLY F . n 
F 2 2   LEU 2   2   2   LEU LEU F . n 
F 2 3   PHE 3   3   3   PHE PHE F . n 
F 2 4   GLY 4   4   4   GLY GLY F . n 
F 2 5   ALA 5   5   5   ALA ALA 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  ARG 38  38  38  ARG ARG 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 
H 3 NAG 1 H NAG 1 H NAG 1 n 
H 3 NAG 2 H NAG 2 H NAG 2 n 
I 4 NAG 1 I NAG 1 I NAG 1 n 
I 4 NAG 2 I NAG 2 I NAG 2 n 
I 4 BMA 3 I BMA 3 I BMA 3 n 
J 3 NAG 1 J NAG 1 J NAG 1 n 
J 3 NAG 2 J NAG 2 J NAG 2 n 
K 5 NAG 1 K NAG 1 K NAG 1 n 
K 5 GAL 2 K GAL 2 K GAL 2 n 
K 5 SIA 3 K SIA 3 K SIA 3 n 
L 5 NAG 1 L NAG 1 L NAG 1 n 
L 5 GAL 2 L GAL 2 L GAL 2 n 
L 5 SIA 3 L SIA 3 L SIA 3 n 
M 5 NAG 1 M NAG 1 M NAG 1 n 
M 5 GAL 2 M GAL 2 M GAL 2 n 
M 5 SIA 3 M SIA 3 M SIA 3 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 
N 6 NAG 1  401 324 NAG NAG A . 
O 6 NAG 1  402 327 NAG NAG A . 
P 6 NAG 1  403 328 NAG NAG A . 
Q 6 NAG 1  401 327 NAG NAG C . 
R 6 NAG 1  402 328 NAG NAG C . 
S 6 NAG 1  401 424 NAG NAG E . 
T 7 HOH 1  501 66  HOH HOH A . 
T 7 HOH 2  502 81  HOH HOH A . 
T 7 HOH 3  503 48  HOH HOH A . 
T 7 HOH 4  504 14  HOH HOH A . 
T 7 HOH 5  505 44  HOH HOH A . 
T 7 HOH 6  506 46  HOH HOH A . 
T 7 HOH 7  507 26  HOH HOH A . 
T 7 HOH 8  508 40  HOH HOH A . 
T 7 HOH 9  509 21  HOH HOH A . 
T 7 HOH 10 510 25  HOH HOH A . 
T 7 HOH 11 511 31  HOH HOH A . 
T 7 HOH 12 512 10  HOH HOH A . 
T 7 HOH 13 513 135 HOH HOH A . 
T 7 HOH 14 514 7   HOH HOH A . 
T 7 HOH 15 515 8   HOH HOH A . 
T 7 HOH 16 516 143 HOH HOH A . 
T 7 HOH 17 517 111 HOH HOH A . 
T 7 HOH 18 518 33  HOH HOH A . 
U 7 HOH 1  201 5   HOH HOH B . 
U 7 HOH 2  202 52  HOH HOH B . 
U 7 HOH 3  203 45  HOH HOH B . 
U 7 HOH 4  204 104 HOH HOH B . 
U 7 HOH 5  205 84  HOH HOH B . 
U 7 HOH 6  206 41  HOH HOH B . 
U 7 HOH 7  207 38  HOH HOH B . 
V 7 HOH 1  501 22  HOH HOH C . 
V 7 HOH 2  502 51  HOH HOH C . 
V 7 HOH 3  503 89  HOH HOH C . 
V 7 HOH 4  504 47  HOH HOH C . 
V 7 HOH 5  505 114 HOH HOH C . 
V 7 HOH 6  506 15  HOH HOH C . 
W 7 HOH 1  201 23  HOH HOH D . 
W 7 HOH 2  202 9   HOH HOH D . 
W 7 HOH 3  203 139 HOH HOH D . 
W 7 HOH 4  204 116 HOH HOH D . 
W 7 HOH 5  205 43  HOH HOH D . 
X 7 HOH 1  501 119 HOH HOH E . 
X 7 HOH 2  502 110 HOH HOH E . 
X 7 HOH 3  503 24  HOH HOH E . 
X 7 HOH 4  504 39  HOH HOH E . 
X 7 HOH 5  505 2   HOH HOH E . 
X 7 HOH 6  506 50  HOH HOH E . 
X 7 HOH 7  507 36  HOH HOH E . 
X 7 HOH 8  508 113 HOH HOH E . 
X 7 HOH 9  509 19  HOH HOH E . 
X 7 HOH 10 510 32  HOH HOH E . 
X 7 HOH 11 511 95  HOH HOH E . 
X 7 HOH 12 512 115 HOH HOH E . 
X 7 HOH 13 513 117 HOH HOH E . 
X 7 HOH 14 514 30  HOH HOH E . 
Y 7 HOH 1  201 103 HOH HOH F . 
Y 7 HOH 2  202 37  HOH HOH F . 
Y 7 HOH 3  203 35  HOH HOH F . 
Y 7 HOH 4  204 17  HOH HOH F . 
Y 7 HOH 5  205 20  HOH HOH F . 
Y 7 HOH 6  206 11  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                   126.19 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NR5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     188.080 
_cell.length_a_esd                 ? 
_cell.length_b                     99.827 
_cell.length_b_esd                 ? 
_cell.length_c                     132.059 
_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                         9NR5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9NR5 
_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             2.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.99 
_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    '0.2M ammonium format, 20% PEG3350' 
_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         2024-01-31 
_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                                       9NR5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.52 
_reflns.d_resolution_low                               39.68 
_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                                     65184 
_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                           98 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          23.8 
_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                                0.127 
_reflns.pdbx_Rpim_I_all                                0.049 
_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                                    2.52 
_reflns_shell.d_res_low                                     2.56 
_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                             6297 
_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                               0.95 
_reflns_shell.pdbx_Rpim_I_all                               0.36 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.78 
_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                                 9NR5 
_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                            2.52 
_refine.ls_d_res_low                             39.68 
_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                     65184 
_refine.ls_number_reflns_R_free                  3262 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.52 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2032 
_refine.ls_R_factor_R_free                       0.2569 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2004 
_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                          1.37 
_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                 28.72 
_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                       2.52 
_refine_hist.d_res_low                        39.68 
_refine_hist.number_atoms_solvent             56 
_refine_hist.number_atoms_total               12294 
_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        11893 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         345 
_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' ? 0.003  ? 12511 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.567  ? 16951 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.037 ? 2147  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043  ? 1877  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 2185  ? 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' 2.52 2.56  . . 125 2488 91.00 . . . . 0.3324 . . . . . . . . . . . . . . . 0.4174 
'X-RAY DIFFRACTION' 2.56 2.60  . . 125 2690 96.00 . . . . 0.2921 . . . . . . . . . . . . . . . 0.3660 
'X-RAY DIFFRACTION' 2.60 2.64  . . 149 2664 97.00 . . . . 0.2678 . . . . . . . . . . . . . . . 0.3160 
'X-RAY DIFFRACTION' 2.64 2.68  . . 141 2651 98.00 . . . . 0.2631 . . . . . . . . . . . . . . . 0.3784 
'X-RAY DIFFRACTION' 2.68 2.73  . . 132 2723 99.00 . . . . 0.2577 . . . . . . . . . . . . . . . 0.3957 
'X-RAY DIFFRACTION' 2.73 2.79  . . 110 2724 99.00 . . . . 0.2466 . . . . . . . . . . . . . . . 0.3133 
'X-RAY DIFFRACTION' 2.79 2.84  . . 161 2707 99.00 . . . . 0.2565 . . . . . . . . . . . . . . . 0.2970 
'X-RAY DIFFRACTION' 2.84 2.90  . . 148 2702 99.00 . . . . 0.2625 . . . . . . . . . . . . . . . 0.3313 
'X-RAY DIFFRACTION' 2.90 2.97  . . 147 2728 99.00 . . . . 0.2729 . . . . . . . . . . . . . . . 0.3352 
'X-RAY DIFFRACTION' 2.97 3.05  . . 139 2719 98.00 . . . . 0.2528 . . . . . . . . . . . . . . . 0.3120 
'X-RAY DIFFRACTION' 3.05 3.13  . . 137 2728 98.00 . . . . 0.2405 . . . . . . . . . . . . . . . 0.2829 
'X-RAY DIFFRACTION' 3.13 3.22  . . 157 2674 97.00 . . . . 0.2376 . . . . . . . . . . . . . . . 0.3041 
'X-RAY DIFFRACTION' 3.22 3.32  . . 127 2537 92.00 . . . . 0.2357 . . . . . . . . . . . . . . . 0.3343 
'X-RAY DIFFRACTION' 3.32 3.44  . . 167 2684 99.00 . . . . 0.2312 . . . . . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 3.44 3.58  . . 149 2725 99.00 . . . . 0.2255 . . . . . . . . . . . . . . . 0.3063 
'X-RAY DIFFRACTION' 3.58 3.74  . . 129 2727 99.00 . . . . 0.1907 . . . . . . . . . . . . . . . 0.2782 
'X-RAY DIFFRACTION' 3.74 3.94  . . 166 2719 98.00 . . . . 0.1845 . . . . . . . . . . . . . . . 0.2468 
'X-RAY DIFFRACTION' 3.94 4.19  . . 133 2721 99.00 . . . . 0.1712 . . . . . . . . . . . . . . . 0.2318 
'X-RAY DIFFRACTION' 4.19 4.51  . . 153 2737 99.00 . . . . 0.1562 . . . . . . . . . . . . . . . 0.1938 
'X-RAY DIFFRACTION' 4.51 4.96  . . 157 2585 94.00 . . . . 0.1456 . . . . . . . . . . . . . . . 0.1989 
'X-RAY DIFFRACTION' 4.96 5.68  . . 134 2779 99.00 . . . . 0.1615 . . . . . . . . . . . . . . . 0.1987 
'X-RAY DIFFRACTION' 5.68 7.15  . . 155 2770 99.00 . . . . 0.1874 . . . . . . . . . . . . . . . 0.2183 
'X-RAY DIFFRACTION' 7.15 39.68 . . 121 2740 95.00 . . . . 0.1705 . . . . . . . . . . . . . . . 0.2119 
# 
_struct.entry_id                     9NR5 
_struct.title                        
'Crystal structure of H5 hemagglutinin Q226L mutant from the influenza virus A/black swan/Akita/1/2016 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        9NR5 
_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 5 ? 
M N N 5 ? 
N N N 6 ? 
O N N 6 ? 
P N N 6 ? 
Q N N 6 ? 
R N N 6 ? 
S N N 6 ? 
T N N 7 ? 
U N N 7 ? 
V N N 7 ? 
W N N 7 ? 
X N N 7 ? 
Y 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 A0A1L7N0F8_9INFA A0A1L7N0F8 ? 1 
;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGRLCDLNGVKPLILKDCSVAGWLLGNPMCDEFIRVPEWSYIV
ERTNPANDLCYPGNLNDYEELKHLLSRINHFEKTLIIPKSSWPNHETSGVSAACPYQGVPSFFRNVVWLTKKNDAYPTIK
MSYNNTNGEDLLILWGIHHSNNAAEQINLYKNPTTYVSVGTSTLNQRLVPKIATRSQVNGQQGRMDFFWTILKPNDAIHF
ESNGNFIAPEYAYKIVKKGDSTIMKSEMEYGHCNTKCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATGLRNSP
LR
;
17  
2 UNP A0A1L7N0F8_9INFA A0A1L7N0F8 ? 2 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADRESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEARLKREEIS
;
345 
# 
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 9NR5 A 3 ? 324 ? A0A1L7N0F8 17  ? 338 ? 11 326 
2 2 9NR5 B 1 ? 174 ? A0A1L7N0F8 345 ? 518 ? 1  174 
3 1 9NR5 C 3 ? 324 ? A0A1L7N0F8 17  ? 338 ? 11 326 
4 2 9NR5 D 1 ? 174 ? A0A1L7N0F8 345 ? 518 ? 1  174 
5 1 9NR5 E 3 ? 324 ? A0A1L7N0F8 17  ? 338 ? 11 326 
6 2 9NR5 F 1 ? 174 ? A0A1L7N0F8 345 ? 518 ? 1  174 
# 
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 9NR5 PRO A 1   ? UNP A0A1L7N0F8 ?   ?   'expression tag'      9   1  
1 9NR5 GLY A 2   ? UNP A0A1L7N0F8 ?   ?   'expression tag'      10  2  
1 9NR5 LEU A 223 ? UNP A0A1L7N0F8 GLN 237 'engineered mutation' 226 3  
2 9NR5 SER B 175 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      175 4  
2 9NR5 GLY B 176 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      176 5  
2 9NR5 ARG B 177 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      177 6  
3 9NR5 PRO C 1   ? UNP A0A1L7N0F8 ?   ?   'expression tag'      9   7  
3 9NR5 GLY C 2   ? UNP A0A1L7N0F8 ?   ?   'expression tag'      10  8  
3 9NR5 LEU C 223 ? UNP A0A1L7N0F8 GLN 237 'engineered mutation' 226 9  
4 9NR5 SER D 175 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      175 10 
4 9NR5 GLY D 176 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      176 11 
4 9NR5 ARG D 177 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      177 12 
5 9NR5 PRO E 1   ? UNP A0A1L7N0F8 ?   ?   'expression tag'      9   13 
5 9NR5 GLY E 2   ? UNP A0A1L7N0F8 ?   ?   'expression tag'      10  14 
5 9NR5 LEU E 223 ? UNP A0A1L7N0F8 GLN 237 'engineered mutation' 226 15 
6 9NR5 SER F 175 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      175 16 
6 9NR5 GLY F 176 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      176 17 
6 9NR5 ARG F 177 ? UNP A0A1L7N0F8 ?   ?   'expression tag'      177 18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_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,X,Y 
# 
_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 58  ? GLY A 65  ? SER A 65  GLY A 72  1 ? 8  
HELX_P HELX_P2  AA2 ASP A 99  ? LEU A 107 ? ASP A 104 LEU A 112 1 ? 9  
HELX_P HELX_P3  AA3 PRO A 120 ? TRP A 124 ? PRO A 125 TRP A 127 5 ? 5  
HELX_P HELX_P4  AA4 ASN A 184 ? LYS A 193 ? 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 ? SER B 174 ? ASP B 158 SER B 174 1 ? 17 
HELX_P HELX_P9  AA9 SER C 58  ? GLY C 65  ? SER C 65  GLY C 72  1 ? 8  
HELX_P HELX_P10 AB1 ASP C 99  ? LEU C 107 ? ASP C 104 LEU C 112 1 ? 9  
HELX_P HELX_P11 AB2 PRO C 120 ? TRP C 124 ? PRO C 125 TRP C 127 5 ? 5  
HELX_P HELX_P12 AB3 ASN C 184 ? LYS C 193 ? ASN C 187 LYS C 196 1 ? 10 
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 TYR D 159 ? GLN D 161 ? TYR D 159 GLN D 161 5 ? 3  
HELX_P HELX_P17 AB8 TYR D 162 ? ILE D 173 ? TYR D 162 ILE D 173 1 ? 12 
HELX_P HELX_P18 AB9 SER E 58  ? GLY E 65  ? SER E 65  GLY E 72  1 ? 8  
HELX_P HELX_P19 AC1 ASP E 99  ? SER E 108 ? ASP E 104 SER E 113 1 ? 10 
HELX_P HELX_P20 AC2 PRO E 120 ? TRP E 124 ? PRO E 125 TRP E 127 5 ? 5  
HELX_P HELX_P21 AC3 ASN E 184 ? LYS E 193 ? ASN E 187 LYS E 196 1 ? 10 
HELX_P HELX_P22 AC4 ASP F 37  ? LYS F 58  ? ASP F 37  LYS F 58  1 ? 22 
HELX_P HELX_P23 AC5 GLU F 74  ? ARG F 127 ? GLU F 74  ARG F 127 1 ? 54 
HELX_P HELX_P24 AC6 ASP F 145 ? ASN F 154 ? ASP F 145 ASN F 154 1 ? 10 
HELX_P HELX_P25 AC7 ASP F 158 ? SER F 175 ? ASP F 158 SER F 175 1 ? 18 
# 
_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 6   SG  ? ? ? 1_555 B CYS 137 SG ? ? A CYS 14  B CYS 137 1_555 ? ? ? ? ? ? ? 2.037 ? ?               
disulf2  disulf ?    ? A CYS 44  SG  ? ? ? 1_555 A CYS 275 SG ? ? A CYS 52  A CYS 277 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf3  disulf ?    ? A CYS 57  SG  ? ? ? 1_555 A CYS 69  SG ? ? A CYS 64  A CYS 76  1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf4  disulf ?    ? A CYS 92  SG  ? ? ? 1_555 A CYS 136 SG ? ? A CYS 97  A CYS 139 1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf5  disulf ?    ? A CYS 279 SG  ? ? ? 1_555 A CYS 303 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf6  disulf ?    ? B CYS 144 SG  ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.042 ? ?               
disulf7  disulf ?    ? C CYS 6   SG  ? ? ? 1_555 D CYS 137 SG ? ? C CYS 14  D CYS 137 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf8  disulf ?    ? C CYS 44  SG  ? ? ? 1_555 C CYS 275 SG ? ? C CYS 52  C CYS 277 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf9  disulf ?    ? C CYS 57  SG  ? ? ? 1_555 C CYS 69  SG ? ? C CYS 64  C CYS 76  1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf10 disulf ?    ? C CYS 279 SG  ? ? ? 1_555 C CYS 303 SG ? ? C CYS 281 C CYS 305 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf11 disulf ?    ? D CYS 144 SG  ? ? ? 1_555 D CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.043 ? ?               
disulf12 disulf ?    ? E CYS 6   SG  ? ? ? 1_555 F CYS 137 SG ? ? E CYS 14  F CYS 137 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf13 disulf ?    ? E CYS 44  SG  ? ? ? 1_555 E CYS 275 SG ? ? E CYS 52  E CYS 277 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf14 disulf ?    ? E CYS 57  SG  ? ? ? 1_555 E CYS 69  SG ? ? E CYS 64  E CYS 76  1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf15 disulf ?    ? E CYS 92  SG  ? ? ? 1_555 E CYS 136 SG ? ? E CYS 97  E CYS 139 1_555 ? ? ? ? ? ? ? 2.041 ? ?               
disulf16 disulf ?    ? E CYS 279 SG  ? ? ? 1_555 E CYS 303 SG ? ? E CYS 281 E CYS 305 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf17 disulf ?    ? F CYS 144 SG  ? ? ? 1_555 F CYS 148 SG ? ? F CYS 144 F CYS 148 1_555 ? ? ? ? ? ? ? 2.044 ? ?               
covale1  covale one  ? A ASN 13  ND2 ? ? ? 1_555 O NAG .   C1 ? ? A ASN 21  A NAG 402 1_555 ? ? ? ? ? ? ? 1.447 ? N-Glycosylation 
covale2  covale one  ? A ASN 25  ND2 ? ? ? 1_555 P NAG .   C1 ? ? A ASN 33  A NAG 403 1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
covale3  covale one  ? A ASN 166 ND2 ? ? ? 1_555 N NAG .   C1 ? ? A ASN 169 A NAG 401 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale4  covale one  ? C ASN 25  ND2 ? ? ? 1_555 Q NAG .   C1 ? ? C ASN 33  C NAG 401 1_555 ? ? ? ? ? ? ? 1.444 ? N-Glycosylation 
covale5  covale one  ? C ASN 166 ND2 ? ? ? 1_555 G NAG .   C1 ? ? C ASN 169 G NAG 1   1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale6  covale one  ? C ASN 287 ND2 ? ? ? 1_555 R NAG .   C1 ? ? C ASN 289 C NAG 402 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale7  covale one  ? D ASN 154 ND2 ? ? ? 1_555 H NAG .   C1 ? ? D ASN 154 H NAG 1   1_555 ? ? ? ? ? ? ? 1.456 ? N-Glycosylation 
covale8  covale one  ? E ASN 25  ND2 ? ? ? 1_555 S NAG .   C1 ? ? E ASN 33  E NAG 401 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale9  covale one  ? E ASN 166 ND2 ? ? ? 1_555 I NAG .   C1 ? ? E ASN 169 I NAG 1   1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale10 covale one  ? F ASN 154 ND2 ? ? ? 1_555 J NAG .   C1 ? ? F ASN 154 J NAG 1   1_555 ? ? ? ? ? ? ? 1.446 ? N-Glycosylation 
covale11 covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.448 ? ?               
covale12 covale both ? H NAG .   O4  ? ? ? 1_555 H NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.446 ? ?               
covale13 covale both ? I NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? I NAG 1   I NAG 2   1_555 ? ? ? ? ? ? ? 1.449 ? ?               
covale14 covale both ? I NAG .   O4  ? ? ? 1_555 I BMA .   C1 ? ? I NAG 2   I BMA 3   1_555 ? ? ? ? ? ? ? 1.453 ? ?               
covale15 covale both ? J NAG .   O4  ? ? ? 1_555 J NAG .   C1 ? ? J NAG 1   J NAG 2   1_555 ? ? ? ? ? ? ? 1.446 ? ?               
covale16 covale both ? K NAG .   O4  ? ? ? 1_555 K GAL .   C1 ? ? K NAG 1   K GAL 2   1_555 ? ? ? ? ? ? ? 1.440 ? ?               
covale17 covale both ? K GAL .   O6  ? ? ? 1_555 K SIA .   C2 ? ? K GAL 2   K SIA 3   1_555 ? ? ? ? ? ? ? 1.445 ? ?               
covale18 covale both ? L NAG .   O4  ? ? ? 1_555 L GAL .   C1 ? ? L NAG 1   L GAL 2   1_555 ? ? ? ? ? ? ? 1.443 ? ?               
covale19 covale both ? L GAL .   O6  ? ? ? 1_555 L SIA .   C2 ? ? L GAL 2   L SIA 3   1_555 ? ? ? ? ? ? ? 1.447 ? ?               
covale20 covale both ? M NAG .   O4  ? ? ? 1_555 M GAL .   C1 ? ? M NAG 1   M GAL 2   1_555 ? ? ? ? ? ? ? 1.441 ? ?               
covale21 covale both ? M GAL .   O6  ? ? ? 1_555 M SIA .   C2 ? ? M GAL 2   M SIA 3   1_555 ? ? ? ? ? ? ? 1.446 ? ?               
# 
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 C 166 ? NAG G 1   ? 1_555 ASN C 169 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG H .   ? ASN D 154 ? NAG H 1   ? 1_555 ASN D 154 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG I .   ? ASN E 166 ? 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 N .   ? ASN A 166 ? NAG A 401 ? 1_555 ASN A 169 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG O .   ? ASN A 13  ? NAG A 402 ? 1_555 ASN A 21  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG P .   ? ASN A 25  ? NAG A 403 ? 1_555 ASN A 33  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG Q .   ? ASN C 25  ? NAG C 401 ? 1_555 ASN C 33  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG R .   ? ASN C 287 ? NAG C 402 ? 1_555 ASN C 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG S .   ? ASN E 25  ? NAG E 401 ? 1_555 ASN E 33  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 CYS A 6   ? CYS B 137 ? CYS A 14  ? 1_555 CYS B 137 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS A 44  ? CYS A 275 ? CYS A 52  ? 1_555 CYS A 277 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 57  ? CYS A 69  ? CYS A 64  ? 1_555 CYS A 76  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 92  ? CYS A 136 ? CYS A 97  ? 1_555 CYS A 139 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS A 279 ? CYS A 303 ? 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 6   ? CYS D 137 ? CYS C 14  ? 1_555 CYS D 137 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
18 CYS C 44  ? CYS C 275 ? CYS C 52  ? 1_555 CYS C 277 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
19 CYS C 57  ? CYS C 69  ? CYS C 64  ? 1_555 CYS C 76  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
20 CYS C 279 ? CYS C 303 ? CYS C 281 ? 1_555 CYS C 305 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
21 CYS D 144 ? CYS D 148 ? CYS D 144 ? 1_555 CYS D 148 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
22 CYS E 6   ? CYS F 137 ? CYS E 14  ? 1_555 CYS F 137 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
23 CYS E 44  ? CYS E 275 ? CYS E 52  ? 1_555 CYS E 277 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
24 CYS E 57  ? CYS E 69  ? CYS E 64  ? 1_555 CYS E 76  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
25 CYS E 92  ? CYS E 136 ? CYS E 97  ? 1_555 CYS E 139 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
26 CYS E 279 ? CYS E 303 ? CYS E 281 ? 1_555 CYS E 305 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
27 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 ? 5 ? 
AB4 ? 2 ? 
AB5 ? 2 ? 
AB6 ? 3 ? 
AB7 ? 2 ? 
AB8 ? 3 ? 
AB9 ? 5 ? 
AC1 ? 5 ? 
AC2 ? 2 ? 
AC3 ? 2 ? 
AC4 ? 4 ? 
AC5 ? 3 ? 
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 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB7 1 2 ? parallel      
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? 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 
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 SER B 32  ? ALA B 36  ? SER B 32  ALA B 36  
AA1 2 TYR B 22  ? SER B 27  ? TYR B 22  SER B 27  
AA1 3 GLN A 4   ? TYR A 9   ? 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 17  ? VAL A 18  ? GLN A 25  VAL A 26  
AA2 2 VAL A 26  ? THR A 27  ? VAL A 34  THR A 35  
AA3 1 ALA A 31  ? ASP A 33  ? ALA A 39  ASP A 41  
AA3 2 VAL A 313 ? ALA A 315 ? VAL A 315 ALA A 317 
AA4 1 LEU A 35  ? GLU A 36  ? LEU A 43  GLU A 44  
AA4 2 PHE A 292 ? HIS A 293 ? PHE A 294 HIS A 295 
AA4 3 LYS A 305 ? TYR A 306 ? LYS A 307 TYR A 308 
AA5 1 LEU A 43  ? LEU A 46  ? LEU A 51  LEU A 54  
AA5 2 TYR A 272 ? THR A 277 ? TYR A 274 THR A 279 
AA6 1 LEU A 52  ? ILE A 53  ? LEU A 59  ILE A 60  
AA6 2 ILE A 81  ? GLU A 83  ? ILE A 87  GLU A 89  
AA6 3 ILE A 265 ? LYS A 267 ? ILE A 267 LYS A 269 
AA7 1 GLY A 95  ? LEU A 97  ? GLY A 100 LEU A 102 
AA7 2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 
AA7 3 ASP A 172 ? HIS A 181 ? ASP A 175 HIS A 184 
AA7 4 TYR A 253 ? VAL A 258 A TYR A 256 VAL A 260 
AA7 5 HIS A 112 ? LEU A 117 ? HIS A 117 LEU A 122 
AA8 1 GLY A 95  ? LEU A 97  ? GLY A 100 LEU A 102 
AA8 2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 
AA8 3 ASP A 172 ? HIS A 181 ? ASP A 175 HIS A 184 
AA8 4 PHE A 248 ? PRO A 251 ? PHE A 251 PRO A 254 
AA8 5 VAL A 148 ? TRP A 150 ? VAL A 151 TRP A 153 
AA9 1 SER A 133 ? TYR A 138 ? SER A 136 TYR A 141 
AA9 2 VAL A 141 ? SER A 143 ? VAL A 144 SER A 146 
AB1 1 ILE A 161 ? ASN A 166 ? ILE A 164 ASN A 169 
AB1 2 ALA A 239 ? SER A 244 ? ALA A 242 SER A 247 
AB1 3 VAL A 199 ? GLY A 202 ? VAL A 202 GLY A 205 
AB1 4 ASN A 207 ? LEU A 210 ? ASN A 210 LEU A 213 
AB2 1 GLY A 284 ? ALA A 285 ? GLY A 286 ALA A 287 
AB2 2 CYS A 279 ? THR A 281 ? CYS A 281 THR A 283 
AB2 3 ILE A 300 ? GLU A 302 ? 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  ? ALA D 36  ? GLY D 31  ALA D 36  
AB3 2 TYR D 22  ? ASN D 28  ? TYR D 22  ASN D 28  
AB3 3 GLN C 4   ? TYR C 9   ? GLN C 12  TYR C 17  
AB3 4 CYS D 137 ? PHE D 140 ? CYS D 137 PHE D 140 
AB3 5 ALA D 130 ? GLU D 132 ? ALA D 130 GLU D 132 
AB4 1 GLN C 17  ? VAL C 18  ? GLN C 25  VAL C 26  
AB4 2 VAL C 26  ? THR C 27  ? VAL C 34  THR C 35  
AB5 1 ALA C 31  ? ASP C 33  ? ALA C 39  ASP C 41  
AB5 2 VAL C 313 ? ALA C 315 ? VAL C 315 ALA C 317 
AB6 1 LEU C 35  ? GLU C 36  ? LEU C 43  GLU C 44  
AB6 2 PHE C 292 ? HIS C 293 ? PHE C 294 HIS C 295 
AB6 3 LYS C 305 ? TYR C 306 ? LYS C 307 TYR C 308 
AB7 1 LEU C 43  ? LEU C 46  ? LEU C 51  LEU C 54  
AB7 2 TYR C 272 ? THR C 277 ? TYR C 274 THR C 279 
AB8 1 LEU C 52  ? ILE C 53  ? LEU C 59  ILE C 60  
AB8 2 ILE C 81  ? GLU C 83  ? ILE C 87  GLU C 89  
AB8 3 ILE C 265 ? LYS C 267 ? ILE C 267 LYS C 269 
AB9 1 GLY C 95  ? LEU C 97  ? GLY C 100 LEU C 102 
AB9 2 ARG C 226 ? LEU C 234 ? ARG C 229 LEU C 237 
AB9 3 ASP C 172 ? HIS C 181 ? ASP C 175 HIS C 184 
AB9 4 TYR C 253 ? VAL C 258 A TYR C 256 VAL C 260 
AB9 5 HIS C 112 ? LEU C 117 ? HIS C 117 LEU C 122 
AC1 1 GLY C 95  ? LEU C 97  ? GLY C 100 LEU C 102 
AC1 2 ARG C 226 ? LEU C 234 ? ARG C 229 LEU C 237 
AC1 3 ASP C 172 ? HIS C 181 ? ASP C 175 HIS C 184 
AC1 4 PHE C 248 ? PRO C 251 ? PHE C 251 PRO C 254 
AC1 5 VAL C 148 ? TRP C 150 ? VAL C 151 TRP C 153 
AC2 1 HIS C 127 ? GLU C 128 ? HIS C 130 GLU C 131 
AC2 2 THR C 152 ? LYS C 153 ? THR C 155 LYS C 156 
AC3 1 SER C 133 ? TYR C 138 ? SER C 136 TYR C 141 
AC3 2 VAL C 141 ? SER C 143 ? VAL C 144 SER C 146 
AC4 1 ILE C 161 ? ASN C 166 ? ILE C 164 ASN C 169 
AC4 2 ALA C 239 ? SER C 244 ? ALA C 242 SER C 247 
AC4 3 VAL C 199 ? GLY C 202 ? VAL C 202 GLY C 205 
AC4 4 ASN C 207 ? LEU C 210 ? ASN C 210 LEU C 213 
AC5 1 CYS C 279 ? GLN C 280 ? CYS C 281 GLN C 282 
AC5 2 ILE C 300 ? GLU C 302 ? ILE C 302 GLU C 304 
AC5 3 PHE D 63  ? ALA D 65  ? PHE D 63  ALA D 65  
AC6 1 SER F 32  ? ALA F 36  ? SER F 32  ALA F 36  
AC6 2 TYR F 22  ? SER F 27  ? TYR F 22  SER F 27  
AC6 3 GLN E 4   ? TYR E 9   ? 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 17  ? VAL E 18  ? GLN E 25  VAL E 26  
AC7 2 VAL E 26  ? THR E 27  ? VAL E 34  THR E 35  
AC8 1 ALA E 31  ? ASP E 33  ? ALA E 39  ASP E 41  
AC8 2 VAL E 313 ? ALA E 315 ? VAL E 315 ALA E 317 
AC9 1 LEU E 35  ? GLU E 36  ? LEU E 43  GLU E 44  
AC9 2 PHE E 292 ? HIS E 293 ? PHE E 294 HIS E 295 
AC9 3 LYS E 305 ? TYR E 306 ? LYS E 307 TYR E 308 
AD1 1 LEU E 43  ? LEU E 46  ? LEU E 51  LEU E 54  
AD1 2 TYR E 272 ? THR E 277 ? TYR E 274 THR E 279 
AD2 1 LEU E 52  ? LEU E 54  ? LEU E 59  LEU E 61  
AD2 2 ILE E 81  ? GLU E 83  ? ILE E 87  GLU E 89  
AD2 3 ILE E 265 ? LYS E 267 ? ILE E 267 LYS E 269 
AD3 1 GLY E 95  ? LEU E 97  ? GLY E 100 LEU E 102 
AD3 2 ARG E 226 ? LEU E 234 ? ARG E 229 LEU E 237 
AD3 3 ASP E 172 ? HIS E 181 ? ASP E 175 HIS E 184 
AD3 4 TYR E 253 ? VAL E 258 A TYR E 256 VAL E 260 
AD3 5 HIS E 112 ? LEU E 117 ? HIS E 117 LEU E 122 
AD4 1 GLY E 95  ? LEU E 97  ? GLY E 100 LEU E 102 
AD4 2 ARG E 226 ? LEU E 234 ? ARG E 229 LEU E 237 
AD4 3 ASP E 172 ? HIS E 181 ? ASP E 175 HIS E 184 
AD4 4 PHE E 248 ? PRO E 251 ? PHE E 251 PRO E 254 
AD4 5 VAL E 148 ? TRP E 150 ? VAL E 151 TRP E 153 
AD5 1 SER E 133 ? TYR E 138 ? SER E 136 TYR E 141 
AD5 2 VAL E 141 ? SER E 143 ? VAL E 144 SER E 146 
AD6 1 ILE E 161 ? ASN E 166 ? ILE E 164 ASN E 169 
AD6 2 ALA E 239 ? SER E 244 ? ALA E 242 SER E 247 
AD6 3 VAL E 199 ? GLY E 202 ? VAL E 202 GLY E 205 
AD6 4 ASN E 207 ? LEU E 210 ? ASN E 210 LEU E 213 
AD7 1 GLY E 284 ? ILE E 286 ? GLY E 286 ILE E 288 
AD7 2 CYS E 279 ? THR E 281 ? CYS E 281 THR E 283 
AD7 3 ILE E 300 ? GLU E 302 ? 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 6   ? N CYS A 14  
AA1 3 4 N ILE A 5   ? 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 18  ? N VAL A 26  O VAL A 26  ? O VAL A 34  
AA3 1 2 N GLN A 32  ? N GLN A 40  O LEU A 314 ? O LEU A 316 
AA4 1 2 N GLU A 36  ? N GLU A 44  O PHE A 292 ? O PHE A 294 
AA4 2 3 N HIS A 293 ? N HIS A 295 O LYS A 305 ? O LYS A 307 
AA5 1 2 N ASP A 45  ? N ASP A 53  O CYS A 275 ? O CYS A 277 
AA6 1 2 N LEU A 52  ? N LEU A 59  O VAL A 82  ? O VAL A 88  
AA6 2 3 N ILE A 81  ? N ILE A 87  O MET A 266 ? O MET A 268 
AA7 1 2 N ASN A 96  ? N ASN A 101 O PHE A 229 ? O PHE A 232 
AA7 2 3 O ARG A 226 ? O ARG A 229 N HIS A 181 ? N HIS A 184 
AA7 3 4 N LEU A 174 ? N LEU A 177 O TYR A 255 ? O TYR A 258 
AA7 4 5 O ALA A 254 ? O ALA A 257 N THR A 116 ? N THR A 121 
AA8 1 2 N ASN A 96  ? N ASN A 101 O PHE A 229 ? O PHE A 232 
AA8 2 3 O ARG A 226 ? O ARG A 229 N HIS A 181 ? N HIS A 184 
AA8 3 4 N GLY A 178 ? N GLY A 181 O ILE A 249 ? O ILE A 252 
AA8 4 5 O ALA A 250 ? O ALA A 253 N VAL A 149 ? N VAL A 152 
AA9 1 2 N TYR A 138 ? N TYR A 141 O VAL A 141 ? O VAL A 144 
AB1 1 2 N ILE A 161 ? N ILE A 164 O SER A 244 ? O SER A 247 
AB1 2 3 O GLU A 243 ? O GLU A 246 N SER A 200 ? N SER A 203 
AB1 3 4 N VAL A 199 ? N VAL A 202 O LEU A 210 ? O LEU A 213 
AB2 1 2 O GLY A 284 ? O GLY A 286 N THR A 281 ? N THR A 283 
AB2 2 3 N GLN A 280 ? N GLN A 282 O ILE A 300 ? O ILE A 302 
AB2 3 4 N GLY A 301 ? N GLY A 303 O GLU B 64  ? O GLU B 64  
AB3 1 2 O ALA D 35  ? O ALA D 35  N TYR D 24  ? N TYR D 24  
AB3 2 3 O HIS D 25  ? O HIS D 25  N CYS C 6   ? N CYS C 14  
AB3 3 4 N ILE C 5   ? N ILE C 13  O PHE D 138 ? O PHE D 138 
AB3 4 5 O GLU D 139 ? O GLU D 139 N LYS D 131 ? N LYS D 131 
AB4 1 2 N VAL C 18  ? N VAL C 26  O VAL C 26  ? O VAL C 34  
AB5 1 2 N GLN C 32  ? N GLN C 40  O LEU C 314 ? O LEU C 316 
AB6 1 2 N GLU C 36  ? N GLU C 44  O PHE C 292 ? O PHE C 294 
AB6 2 3 N HIS C 293 ? N HIS C 295 O LYS C 305 ? O LYS C 307 
AB7 1 2 N ASP C 45  ? N ASP C 53  O CYS C 275 ? O CYS C 277 
AB8 1 2 N LEU C 52  ? N LEU C 59  O VAL C 82  ? O VAL C 88  
AB8 2 3 N ILE C 81  ? N ILE C 87  O MET C 266 ? O MET C 268 
AB9 1 2 N ASN C 96  ? N ASN C 101 O PHE C 229 ? O PHE C 232 
AB9 2 3 O PHE C 230 ? O PHE C 233 N TRP C 177 ? N TRP C 180 
AB9 3 4 N ASP C 172 ? N ASP C 175 O ILE C 257 ? O ILE C 260 
AB9 4 5 O ALA C 254 ? O ALA C 257 N THR C 116 ? N THR C 121 
AC1 1 2 N ASN C 96  ? N ASN C 101 O PHE C 229 ? O PHE C 232 
AC1 2 3 O PHE C 230 ? O PHE C 233 N TRP C 177 ? N TRP C 180 
AC1 3 4 N GLY C 178 ? N GLY C 181 O ILE C 249 ? O ILE C 252 
AC1 4 5 O ALA C 250 ? O ALA C 253 N VAL C 149 ? N VAL C 152 
AC2 1 2 N GLU C 128 ? N GLU C 131 O THR C 152 ? O THR C 155 
AC3 1 2 N TYR C 138 ? N TYR C 141 O VAL C 141 ? O VAL C 144 
AC4 1 2 N MET C 163 ? N MET C 166 O PHE C 242 ? O PHE C 245 
AC4 2 3 O GLU C 243 ? O GLU C 246 N SER C 200 ? N SER C 203 
AC4 3 4 N VAL C 199 ? N VAL C 202 O LEU C 210 ? O LEU C 213 
AC5 1 2 N GLN C 280 ? N GLN C 282 O ILE C 300 ? O ILE C 302 
AC5 2 3 N GLY C 301 ? 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 HIS F 25  ? O HIS F 25  N CYS E 6   ? N CYS E 14  
AC6 3 4 N ILE E 5   ? 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 18  ? N VAL E 26  O VAL E 26  ? O VAL E 34  
AC8 1 2 N GLN E 32  ? N GLN E 40  O LEU E 314 ? O LEU E 316 
AC9 1 2 N GLU E 36  ? N GLU E 44  O PHE E 292 ? O PHE E 294 
AC9 2 3 N HIS E 293 ? N HIS E 295 O LYS E 305 ? O LYS E 307 
AD1 1 2 N ASP E 45  ? N ASP E 53  O CYS E 275 ? O CYS E 277 
AD2 1 2 N LEU E 52  ? N LEU E 59  O VAL E 82  ? O VAL E 88  
AD2 2 3 N ILE E 81  ? N ILE E 87  O MET E 266 ? O MET E 268 
AD3 1 2 N ASN E 96  ? N ASN E 101 O PHE E 229 ? O PHE E 232 
AD3 2 3 O ARG E 226 ? O ARG E 229 N HIS E 181 ? N HIS E 184 
AD3 3 4 N LEU E 174 ? N LEU E 177 O TYR E 255 ? O TYR E 258 
AD3 4 5 O ALA E 254 ? O ALA E 257 N THR E 116 ? N THR E 121 
AD4 1 2 N ASN E 96  ? N ASN E 101 O PHE E 229 ? O PHE E 232 
AD4 2 3 O ARG E 226 ? O ARG E 229 N HIS E 181 ? N HIS E 184 
AD4 3 4 N GLY E 178 ? N GLY E 181 O ILE E 249 ? O ILE E 252 
AD4 4 5 O ALA E 250 ? O ALA E 253 N VAL E 149 ? N VAL E 152 
AD5 1 2 N TYR E 138 ? N TYR E 141 O VAL E 141 ? O VAL E 144 
AD6 1 2 N ILE E 161 ? N ILE E 164 O SER E 244 ? O SER E 247 
AD6 2 3 O GLU E 243 ? O GLU E 246 N SER E 200 ? N SER E 203 
AD6 3 4 N VAL E 199 ? N VAL E 202 O LEU E 210 ? O LEU E 213 
AD7 1 2 O ILE E 286 ? O ILE E 288 N CYS E 279 ? N CYS E 281 
AD7 2 3 N GLN E 280 ? N GLN E 282 O ILE E 300 ? O ILE E 302 
AD7 3 4 N GLY E 301 ? N GLY E 303 O GLU F 64  ? O GLU F 64  
# 
_pdbx_entry_details.entry_id                   9NR5 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 F ASP 128 ? ? OH F TYR 159 ? ? 2.17 
2 1 O6  K GAL 2   ? ? C3 K SIA 3   ? ? 2.17 
3 1 O6  L GAL 2   ? ? C3 L SIA 3   ? ? 2.18 
# 
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 GLU A 78  ? ? 161.13  -45.73  
2  1 ILE A 80  ? ? 50.52   177.14  
3  1 ASP A 96  ? ? -147.53 -156.72 
4  1 TRP A 127 ? ? -112.60 79.52   
5  1 LYS A 196 ? ? 71.97   -10.95  
6  1 ASN A 250 ? ? 59.60   19.24   
7  1 ARG B 127 ? ? 49.30   -135.99 
8  1 ASN B 129 ? ? -69.94  1.56    
9  1 ILE C 80  ? ? 42.89   -177.55 
10 1 ASP C 96  ? ? -96.88  -64.33  
11 1 CYS C 139 ? ? -116.99 66.91   
12 1 LYS C 196 ? ? 71.79   -10.25  
13 1 THR C 206 ? ? -125.73 -167.37 
14 1 SER C 265 ? ? -148.98 -159.35 
15 1 ALA D 5   ? ? -92.17  -60.99  
16 1 ARG D 127 ? ? 54.11   -136.60 
17 1 ASP E 96  ? ? -95.79  -64.53  
18 1 SER E 133 ? ? -93.37  50.12   
19 1 CYS E 139 ? ? -118.34 61.60   
20 1 LYS E 196 ? ? 71.46   -9.47   
21 1 SER E 265 ? ? -150.17 -159.81 
22 1 ALA F 5   ? ? -92.65  -60.40  
23 1 ALA F 7   ? ? 57.72   14.75   
24 1 ARG F 127 ? ? 56.84   -131.57 
25 1 THR F 156 ? ? -95.99  30.18   
# 
_pdbx_molecule_features.prd_id    PRD_900046 
_pdbx_molecule_features.name      "6'-sialyl-N-acetyllactosamine" 
_pdbx_molecule_features.type      Oligosaccharide 
_pdbx_molecule_features.class     'Glycan component' 
_pdbx_molecule_features.details   oligosaccharide 
# 
_pdbx_molecule.instance_id   1 
_pdbx_molecule.prd_id        PRD_900046 
_pdbx_molecule.asym_id       K 
# 
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 PRO 324 ? A PRO 322 
2  1 Y 1 A LEU 325 ? A LEU 323 
3  1 Y 1 A ARG 326 ? A ARG 324 
4  1 Y 1 B SER 175 ? B SER 175 
5  1 Y 1 B GLY 176 ? B GLY 176 
6  1 Y 1 B ARG 177 ? B ARG 177 
7  1 Y 1 C PRO 9   ? C PRO 1   
8  1 Y 1 D SER 175 ? D SER 175 
9  1 Y 1 D GLY 176 ? D GLY 176 
10 1 Y 1 D ARG 177 ? D ARG 177 
11 1 Y 1 E PRO 324 ? E PRO 322 
12 1 Y 1 E LEU 325 ? E LEU 323 
13 1 Y 1 E ARG 326 ? E ARG 324 
# 
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 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
5 NAG 1 n 
5 GAL 2 n 
5 SIA 3 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                    9NR5 
_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]   0.005317 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003890 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010017 
_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]   0.009383 
_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 1   ? -55.971 37.621  -7.354  1.00 82.15  ? 9   PRO A N   1 
ATOM   2     C CA  . PRO A 1 1   ? -56.140 39.070  -7.501  1.00 82.01  ? 9   PRO A CA  1 
ATOM   3     C C   . PRO A 1 1   ? -56.335 39.786  -6.165  1.00 84.33  ? 9   PRO A C   1 
ATOM   4     O O   . PRO A 1 1   ? -56.928 40.863  -6.132  1.00 92.78  ? 9   PRO A O   1 
ATOM   5     C CB  . PRO A 1 1   ? -57.397 39.184  -8.364  1.00 76.14  ? 9   PRO A CB  1 
ATOM   6     C CG  . PRO A 1 1   ? -58.201 37.975  -8.000  1.00 85.57  ? 9   PRO A CG  1 
ATOM   7     C CD  . PRO A 1 1   ? -57.211 36.884  -7.663  1.00 86.64  ? 9   PRO A CD  1 
ATOM   8     N N   . GLY A 1 2   ? -55.848 39.194  -5.079  1.00 75.22  ? 10  GLY A N   1 
ATOM   9     C CA  . GLY A 1 2   ? -55.989 39.768  -3.755  1.00 68.73  ? 10  GLY A CA  1 
ATOM   10    C C   . GLY A 1 2   ? -54.741 40.511  -3.315  1.00 70.45  ? 10  GLY A C   1 
ATOM   11    O O   . GLY A 1 2   ? -53.629 40.189  -3.727  1.00 63.96  ? 10  GLY A O   1 
ATOM   12    N N   . ASP A 1 3   ? -54.941 41.517  -2.467  1.00 61.34  ? 11  ASP A N   1 
ATOM   13    C CA  . ASP A 1 3   ? -53.830 42.311  -1.962  1.00 52.29  ? 11  ASP A CA  1 
ATOM   14    C C   . ASP A 1 3   ? -52.929 41.472  -1.068  1.00 58.48  ? 11  ASP A C   1 
ATOM   15    O O   . ASP A 1 3   ? -53.370 40.524  -0.413  1.00 61.96  ? 11  ASP A O   1 
ATOM   16    C CB  . ASP A 1 3   ? -54.347 43.520  -1.187  1.00 61.48  ? 11  ASP A CB  1 
ATOM   17    C CG  . ASP A 1 3   ? -54.942 44.574  -2.092  1.00 63.18  ? 11  ASP A CG  1 
ATOM   18    O OD1 . ASP A 1 3   ? -54.722 44.484  -3.320  1.00 57.69  ? 11  ASP A OD1 1 
ATOM   19    O OD2 . ASP A 1 3   ? -55.638 45.479  -1.580  1.00 59.59  ? 11  ASP A OD2 1 
ATOM   20    N N   . GLN A 1 4   ? -51.648 41.832  -1.043  1.00 60.47  ? 12  GLN A N   1 
ATOM   21    C CA  . GLN A 1 4   ? -50.652 41.055  -0.326  1.00 53.81  ? 12  GLN A CA  1 
ATOM   22    C C   . GLN A 1 4   ? -49.709 41.968  0.440   1.00 57.53  ? 12  GLN A C   1 
ATOM   23    O O   . GLN A 1 4   ? -49.304 43.021  -0.061  1.00 55.57  ? 12  GLN A O   1 
ATOM   24    C CB  . GLN A 1 4   ? -49.849 40.175  -1.285  1.00 47.89  ? 12  GLN A CB  1 
ATOM   25    C CG  . GLN A 1 4   ? -50.393 38.773  -1.408  1.00 54.13  ? 12  GLN A CG  1 
ATOM   26    C CD  . GLN A 1 4   ? -49.635 37.947  -2.418  1.00 58.09  ? 12  GLN A CD  1 
ATOM   27    O OE1 . GLN A 1 4   ? -48.405 37.942  -2.432  1.00 64.17  ? 12  GLN A OE1 1 
ATOM   28    N NE2 . GLN A 1 4   ? -50.367 37.235  -3.270  1.00 80.19  ? 12  GLN A NE2 1 
ATOM   29    N N   . ILE A 1 5   ? -49.367 41.556  1.659   1.00 60.00  ? 13  ILE A N   1 
ATOM   30    C CA  . ILE A 1 5   ? -48.272 42.145  2.418   1.00 45.61  ? 13  ILE A CA  1 
ATOM   31    C C   . ILE A 1 5   ? -47.353 41.015  2.863   1.00 48.20  ? 13  ILE A C   1 
ATOM   32    O O   . ILE A 1 5   ? -47.816 39.931  3.235   1.00 46.88  ? 13  ILE A O   1 
ATOM   33    C CB  . ILE A 1 5   ? -48.768 42.979  3.622   1.00 49.41  ? 13  ILE A CB  1 
ATOM   34    C CG1 . ILE A 1 5   ? -47.608 43.768  4.233   1.00 44.82  ? 13  ILE A CG1 1 
ATOM   35    C CG2 . ILE A 1 5   ? -49.450 42.106  4.671   1.00 40.76  ? 13  ILE A CG2 1 
ATOM   36    C CD1 . ILE A 1 5   ? -48.048 44.964  5.034   1.00 51.72  ? 13  ILE A CD1 1 
ATOM   37    N N   . CYS A 1 6   ? -46.047 41.261  2.798   1.00 61.77  ? 14  CYS A N   1 
ATOM   38    C CA  . CYS A 1 6   ? -45.045 40.226  2.998   1.00 49.25  ? 14  CYS A CA  1 
ATOM   39    C C   . CYS A 1 6   ? -44.035 40.686  4.039   1.00 50.82  ? 14  CYS A C   1 
ATOM   40    O O   . CYS A 1 6   ? -43.859 41.881  4.274   1.00 52.64  ? 14  CYS A O   1 
ATOM   41    C CB  . CYS A 1 6   ? -44.331 39.897  1.683   1.00 45.53  ? 14  CYS A CB  1 
ATOM   42    S SG  . CYS A 1 6   ? -45.452 39.346  0.381   1.00 70.45  ? 14  CYS A SG  1 
ATOM   43    N N   . ILE A 1 7   ? -43.367 39.721  4.667   1.00 46.97  ? 15  ILE A N   1 
ATOM   44    C CA  . ILE A 1 7   ? -42.291 39.994  5.611   1.00 45.00  ? 15  ILE A CA  1 
ATOM   45    C C   . ILE A 1 7   ? -40.998 39.442  5.024   1.00 43.18  ? 15  ILE A C   1 
ATOM   46    O O   . ILE A 1 7   ? -40.961 38.300  4.551   1.00 45.76  ? 15  ILE A O   1 
ATOM   47    C CB  . ILE A 1 7   ? -42.580 39.397  7.003   1.00 36.93  ? 15  ILE A CB  1 
ATOM   48    C CG1 . ILE A 1 7   ? -43.666 40.204  7.721   1.00 40.12  ? 15  ILE A CG1 1 
ATOM   49    C CG2 . ILE A 1 7   ? -41.327 39.370  7.843   1.00 39.20  ? 15  ILE A CG2 1 
ATOM   50    C CD1 . ILE A 1 7   ? -45.053 39.640  7.565   1.00 58.23  ? 15  ILE A CD1 1 
ATOM   51    N N   . GLY A 1 8   ? -39.949 40.258  5.033   1.00 43.20  ? 16  GLY A N   1 
ATOM   52    C CA  . GLY A 1 8   ? -38.691 39.856  4.437   1.00 31.59  ? 16  GLY A CA  1 
ATOM   53    C C   . GLY A 1 8   ? -37.495 40.528  5.077   1.00 42.20  ? 16  GLY A C   1 
ATOM   54    O O   . GLY A 1 8   ? -37.630 41.234  6.081   1.00 39.28  ? 16  GLY A O   1 
ATOM   55    N N   . TYR A 1 9   ? -36.315 40.327  4.503   1.00 39.24  ? 17  TYR A N   1 
ATOM   56    C CA  . TYR A 1 9   ? -35.091 40.810  5.118   1.00 34.72  ? 17  TYR A CA  1 
ATOM   57    C C   . TYR A 1 9   ? -34.145 41.305  4.036   1.00 41.54  ? 17  TYR A C   1 
ATOM   58    O O   . TYR A 1 9   ? -34.275 40.965  2.857   1.00 39.65  ? 17  TYR A O   1 
ATOM   59    C CB  . TYR A 1 9   ? -34.415 39.729  5.979   1.00 37.65  ? 17  TYR A CB  1 
ATOM   60    C CG  . TYR A 1 9   ? -34.257 38.384  5.304   1.00 45.43  ? 17  TYR A CG  1 
ATOM   61    C CD1 . TYR A 1 9   ? -35.342 37.522  5.160   1.00 29.08  ? 17  TYR A CD1 1 
ATOM   62    C CD2 . TYR A 1 9   ? -33.021 37.969  4.823   1.00 43.82  ? 17  TYR A CD2 1 
ATOM   63    C CE1 . TYR A 1 9   ? -35.200 36.291  4.546   1.00 41.89  ? 17  TYR A CE1 1 
ATOM   64    C CE2 . TYR A 1 9   ? -32.868 36.730  4.207   1.00 44.42  ? 17  TYR A CE2 1 
ATOM   65    C CZ  . TYR A 1 9   ? -33.964 35.899  4.070   1.00 48.44  ? 17  TYR A CZ  1 
ATOM   66    O OH  . TYR A 1 9   ? -33.838 34.669  3.462   1.00 48.12  ? 17  TYR A OH  1 
ATOM   67    N N   . HIS A 1 10  ? -33.190 42.122  4.462   1.00 38.64  ? 18  HIS A N   1 
ATOM   68    C CA  . HIS A 1 10  ? -32.294 42.800  3.540   1.00 39.38  ? 18  HIS A CA  1 
ATOM   69    C C   . HIS A 1 10  ? -31.361 41.808  2.850   1.00 45.01  ? 18  HIS A C   1 
ATOM   70    O O   . HIS A 1 10  ? -30.990 40.774  3.410   1.00 42.58  ? 18  HIS A O   1 
ATOM   71    C CB  . HIS A 1 10  ? -31.493 43.864  4.293   1.00 43.90  ? 18  HIS A CB  1 
ATOM   72    C CG  . HIS A 1 10  ? -30.354 44.442  3.512   1.00 66.49  ? 18  HIS A CG  1 
ATOM   73    N ND1 . HIS A 1 10  ? -30.537 45.329  2.472   1.00 57.43  ? 18  HIS A ND1 1 
ATOM   74    C CD2 . HIS A 1 10  ? -29.015 44.264  3.625   1.00 55.55  ? 18  HIS A CD2 1 
ATOM   75    C CE1 . HIS A 1 10  ? -29.361 45.669  1.976   1.00 71.00  ? 18  HIS A CE1 1 
ATOM   76    N NE2 . HIS A 1 10  ? -28.421 45.035  2.656   1.00 71.54  ? 18  HIS A NE2 1 
ATOM   77    N N   . ALA A 1 11  ? -31.009 42.128  1.606   1.00 52.93  ? 19  ALA A N   1 
ATOM   78    C CA  . ALA A 1 11  ? -29.988 41.407  0.859   1.00 46.98  ? 19  ALA A CA  1 
ATOM   79    C C   . ALA A 1 11  ? -29.235 42.411  -0.006  1.00 58.20  ? 19  ALA A C   1 
ATOM   80    O O   . ALA A 1 11  ? -29.817 43.385  -0.494  1.00 67.83  ? 19  ALA A O   1 
ATOM   81    C CB  . ALA A 1 11  ? -30.596 40.292  -0.001  1.00 35.91  ? 19  ALA A CB  1 
ATOM   82    N N   . ASN A 1 12  ? -27.936 42.178  -0.187  1.00 57.90  ? 20  ASN A N   1 
ATOM   83    C CA  . ASN A 1 12  ? -27.096 43.116  -0.925  1.00 52.10  ? 20  ASN A CA  1 
ATOM   84    C C   . ASN A 1 12  ? -26.128 42.323  -1.798  1.00 51.68  ? 20  ASN A C   1 
ATOM   85    O O   . ASN A 1 12  ? -26.280 41.112  -1.986  1.00 48.94  ? 20  ASN A O   1 
ATOM   86    C CB  . ASN A 1 12  ? -26.373 44.077  0.030   1.00 47.91  ? 20  ASN A CB  1 
ATOM   87    C CG  . ASN A 1 12  ? -25.425 43.365  0.989   1.00 50.11  ? 20  ASN A CG  1 
ATOM   88    O OD1 . ASN A 1 12  ? -25.100 42.192  0.817   1.00 49.85  ? 20  ASN A OD1 1 
ATOM   89    N ND2 . ASN A 1 12  ? -24.975 44.087  2.010   1.00 45.06  ? 20  ASN A ND2 1 
ATOM   90    N N   . ASN A 1 13  ? -25.119 43.019  -2.325  1.00 54.27  ? 21  ASN A N   1 
ATOM   91    C CA  . ASN A 1 13  ? -24.160 42.446  -3.263  1.00 60.33  ? 21  ASN A CA  1 
ATOM   92    C C   . ASN A 1 13  ? -22.899 41.922  -2.585  1.00 55.66  ? 21  ASN A C   1 
ATOM   93    O O   . ASN A 1 13  ? -21.920 41.618  -3.276  1.00 66.08  ? 21  ASN A O   1 
ATOM   94    C CB  . ASN A 1 13  ? -23.782 43.481  -4.334  1.00 57.48  ? 21  ASN A CB  1 
ATOM   95    C CG  . ASN A 1 13  ? -23.142 44.740  -3.749  1.00 71.12  ? 21  ASN A CG  1 
ATOM   96    O OD1 . ASN A 1 13  ? -22.925 44.842  -2.540  1.00 53.05  ? 21  ASN A OD1 1 
ATOM   97    N ND2 . ASN A 1 13  ? -22.841 45.708  -4.617  1.00 80.81  ? 21  ASN A ND2 1 
ATOM   98    N N   . SER A 1 14  ? -22.895 41.818  -1.259  1.00 56.74  ? 22  SER A N   1 
ATOM   99    C CA  . SER A 1 14  ? -21.697 41.402  -0.541  1.00 58.76  ? 22  SER A CA  1 
ATOM   100   C C   . SER A 1 14  ? -21.349 39.950  -0.850  1.00 55.63  ? 22  SER A C   1 
ATOM   101   O O   . SER A 1 14  ? -22.226 39.087  -0.951  1.00 50.65  ? 22  SER A O   1 
ATOM   102   C CB  . SER A 1 14  ? -21.891 41.586  0.966   1.00 50.41  ? 22  SER A CB  1 
ATOM   103   O OG  . SER A 1 14  ? -20.933 40.848  1.706   1.00 53.06  ? 22  SER A OG  1 
ATOM   104   N N   . THR A 1 15  ? -20.052 39.688  -1.018  1.00 55.01  ? 23  THR A N   1 
ATOM   105   C CA  . THR A 1 15  ? -19.528 38.334  -1.140  1.00 58.50  ? 23  THR A CA  1 
ATOM   106   C C   . THR A 1 15  ? -18.699 37.937  0.077   1.00 45.86  ? 23  THR A C   1 
ATOM   107   O O   . THR A 1 15  ? -17.944 36.963  0.019   1.00 53.07  ? 23  THR A O   1 
ATOM   108   C CB  . THR A 1 15  ? -18.695 38.185  -2.416  1.00 59.38  ? 23  THR A CB  1 
ATOM   109   O OG1 . THR A 1 15  ? -17.664 39.180  -2.437  1.00 58.90  ? 23  THR A OG1 1 
ATOM   110   C CG2 . THR A 1 15  ? -19.573 38.336  -3.653  1.00 42.48  ? 23  THR A CG2 1 
ATOM   111   N N   . GLU A 1 16  ? -18.814 38.687  1.171   1.00 46.91  ? 24  GLU A N   1 
ATOM   112   C CA  . GLU A 1 16  ? -18.112 38.333  2.396   1.00 53.53  ? 24  GLU A CA  1 
ATOM   113   C C   . GLU A 1 16  ? -18.645 37.013  2.941   1.00 59.88  ? 24  GLU A C   1 
ATOM   114   O O   . GLU A 1 16  ? -19.855 36.760  2.941   1.00 46.66  ? 24  GLU A O   1 
ATOM   115   C CB  . GLU A 1 16  ? -18.263 39.444  3.436   1.00 48.82  ? 24  GLU A CB  1 
ATOM   116   C CG  . GLU A 1 16  ? -16.948 40.126  3.808   1.00 71.75  ? 24  GLU A CG  1 
ATOM   117   C CD  . GLU A 1 16  ? -17.104 41.153  4.921   1.00 85.23  ? 24  GLU A CD  1 
ATOM   118   O OE1 . GLU A 1 16  ? -18.104 41.906  4.915   1.00 76.48  ? 24  GLU A OE1 1 
ATOM   119   O OE2 . GLU A 1 16  ? -16.222 41.203  5.808   1.00 79.43  ? 24  GLU A OE2 1 
ATOM   120   N N   . GLN A 1 17  ? -17.731 36.164  3.404   1.00 55.94  ? 25  GLN A N   1 
ATOM   121   C CA  . GLN A 1 17  ? -18.062 34.823  3.860   1.00 50.16  ? 25  GLN A CA  1 
ATOM   122   C C   . GLN A 1 17  ? -17.618 34.637  5.303   1.00 44.80  ? 25  GLN A C   1 
ATOM   123   O O   . GLN A 1 17  ? -16.571 35.149  5.713   1.00 61.08  ? 25  GLN A O   1 
ATOM   124   C CB  . GLN A 1 17  ? -17.403 33.761  2.973   1.00 46.91  ? 25  GLN A CB  1 
ATOM   125   C CG  . GLN A 1 17  ? -18.156 33.487  1.683   1.00 57.59  ? 25  GLN A CG  1 
ATOM   126   C CD  . GLN A 1 17  ? -17.714 32.200  1.019   1.00 59.70  ? 25  GLN A CD  1 
ATOM   127   O OE1 . GLN A 1 17  ? -16.664 31.649  1.344   1.00 71.00  ? 25  GLN A OE1 1 
ATOM   128   N NE2 . GLN A 1 17  ? -18.513 31.713  0.080   1.00 54.83  ? 25  GLN A NE2 1 
ATOM   129   N N   . VAL A 1 18  ? -18.428 33.905  6.070   1.00 40.60  ? 26  VAL A N   1 
ATOM   130   C CA  . VAL A 1 18  ? -18.098 33.507  7.431   1.00 39.34  ? 26  VAL A CA  1 
ATOM   131   C C   . VAL A 1 18  ? -18.373 32.016  7.573   1.00 47.77  ? 26  VAL A C   1 
ATOM   132   O O   . VAL A 1 18  ? -19.094 31.410  6.775   1.00 46.99  ? 26  VAL A O   1 
ATOM   133   C CB  . VAL A 1 18  ? -18.891 34.289  8.502   1.00 42.43  ? 26  VAL A CB  1 
ATOM   134   C CG1 . VAL A 1 18  ? -18.778 35.792  8.276   1.00 42.57  ? 26  VAL A CG1 1 
ATOM   135   C CG2 . VAL A 1 18  ? -20.347 33.838  8.519   1.00 29.93  ? 26  VAL A CG2 1 
ATOM   136   N N   . ASP A 1 19  ? -17.786 31.428  8.609   1.00 40.01  ? 27  ASP A N   1 
ATOM   137   C CA  . ASP A 1 19  ? -18.024 30.039  8.968   1.00 45.55  ? 27  ASP A CA  1 
ATOM   138   C C   . ASP A 1 19  ? -18.835 29.991  10.256  1.00 41.69  ? 27  ASP A C   1 
ATOM   139   O O   . ASP A 1 19  ? -18.679 30.846  11.132  1.00 38.11  ? 27  ASP A O   1 
ATOM   140   C CB  . ASP A 1 19  ? -16.702 29.276  9.144   1.00 39.10  ? 27  ASP A CB  1 
ATOM   141   C CG  . ASP A 1 19  ? -16.118 28.787  7.820   1.00 57.13  ? 27  ASP A CG  1 
ATOM   142   O OD1 . ASP A 1 19  ? -16.627 29.189  6.751   1.00 62.30  ? 27  ASP A OD1 1 
ATOM   143   O OD2 . ASP A 1 19  ? -15.148 27.997  7.848   1.00 63.11  ? 27  ASP A OD2 1 
ATOM   144   N N   . THR A 1 20  ? -19.726 29.017  10.357  1.00 41.93  ? 28  THR A N   1 
ATOM   145   C CA  . THR A 1 20  ? -20.420 28.755  11.606  1.00 40.57  ? 28  THR A CA  1 
ATOM   146   C C   . THR A 1 20  ? -20.007 27.386  12.126  1.00 40.79  ? 28  THR A C   1 
ATOM   147   O O   . THR A 1 20  ? -19.292 26.632  11.463  1.00 39.15  ? 28  THR A O   1 
ATOM   148   C CB  . THR A 1 20  ? -21.946 28.844  11.432  1.00 49.51  ? 28  THR A CB  1 
ATOM   149   O OG1 . THR A 1 20  ? -22.436 27.676  10.759  1.00 44.69  ? 28  THR A OG1 1 
ATOM   150   C CG2 . THR A 1 20  ? -22.331 30.089  10.638  1.00 38.17  ? 28  THR A CG2 1 
ATOM   151   N N   . ILE A 1 21  ? -20.464 27.074  13.339  1.00 40.05  ? 29  ILE A N   1 
ATOM   152   C CA  . ILE A 1 21  ? -20.163 25.775  13.933  1.00 43.40  ? 29  ILE A CA  1 
ATOM   153   C C   . ILE A 1 21  ? -20.712 24.637  13.072  1.00 46.99  ? 29  ILE A C   1 
ATOM   154   O O   . ILE A 1 21  ? -20.173 23.525  13.077  1.00 42.28  ? 29  ILE A O   1 
ATOM   155   C CB  . ILE A 1 21  ? -20.727 25.723  15.365  1.00 46.53  ? 29  ILE A CB  1 
ATOM   156   C CG1 . ILE A 1 21  ? -20.296 24.442  16.081  1.00 60.55  ? 29  ILE A CG1 1 
ATOM   157   C CG2 . ILE A 1 21  ? -22.232 25.840  15.326  1.00 63.98  ? 29  ILE A CG2 1 
ATOM   158   C CD1 . ILE A 1 21  ? -18.807 24.361  16.323  1.00 47.34  ? 29  ILE A CD1 1 
ATOM   159   N N   . MET A 1 22  ? -21.776 24.890  12.312  1.00 42.32  ? 30  MET A N   1 
ATOM   160   C CA  . MET A 1 22  ? -22.401 23.842  11.524  1.00 49.85  ? 30  MET A CA  1 
ATOM   161   C C   . MET A 1 22  ? -22.321 24.055  10.022  1.00 52.36  ? 30  MET A C   1 
ATOM   162   O O   . MET A 1 22  ? -22.575 23.107  9.272   1.00 51.18  ? 30  MET A O   1 
ATOM   163   C CB  . MET A 1 22  ? -23.871 23.693  11.932  1.00 51.72  ? 30  MET A CB  1 
ATOM   164   C CG  . MET A 1 22  ? -24.014 23.236  13.366  1.00 50.31  ? 30  MET A CG  1 
ATOM   165   S SD  . MET A 1 22  ? -25.719 23.053  13.844  1.00 59.96  ? 30  MET A SD  1 
ATOM   166   C CE  . MET A 1 22  ? -25.948 21.352  13.410  1.00 45.13  ? 30  MET A CE  1 
ATOM   167   N N   . GLU A 1 23  ? -21.978 25.252  9.561   1.00 42.85  ? 31  GLU A N   1 
ATOM   168   C CA  . GLU A 1 23  ? -21.851 25.527  8.142   1.00 46.61  ? 31  GLU A CA  1 
ATOM   169   C C   . GLU A 1 23  ? -20.542 26.252  7.885   1.00 49.41  ? 31  GLU A C   1 
ATOM   170   O O   . GLU A 1 23  ? -20.040 26.987  8.740   1.00 49.34  ? 31  GLU A O   1 
ATOM   171   C CB  . GLU A 1 23  ? -23.014 26.377  7.608   1.00 45.33  ? 31  GLU A CB  1 
ATOM   172   C CG  . GLU A 1 23  ? -24.403 25.848  7.930   1.00 58.24  ? 31  GLU A CG  1 
ATOM   173   C CD  . GLU A 1 23  ? -25.461 26.935  7.847   1.00 69.97  ? 31  GLU A CD  1 
ATOM   174   O OE1 . GLU A 1 23  ? -25.885 27.265  6.718   1.00 58.20  ? 31  GLU A OE1 1 
ATOM   175   O OE2 . GLU A 1 23  ? -25.866 27.459  8.909   1.00 57.72  ? 31  GLU A OE2 1 
ATOM   176   N N   . LYS A 1 24  ? -19.999 26.045  6.691   1.00 50.04  ? 32  LYS A N   1 
ATOM   177   C CA  . LYS A 1 24  ? -18.802 26.741  6.252   1.00 58.89  ? 32  LYS A CA  1 
ATOM   178   C C   . LYS A 1 24  ? -19.128 27.568  5.017   1.00 50.78  ? 32  LYS A C   1 
ATOM   179   O O   . LYS A 1 24  ? -20.005 27.209  4.226   1.00 48.45  ? 32  LYS A O   1 
ATOM   180   C CB  . LYS A 1 24  ? -17.659 25.759  5.956   1.00 47.43  ? 32  LYS A CB  1 
ATOM   181   C CG  . LYS A 1 24  ? -17.360 24.806  7.108   1.00 62.57  ? 32  LYS A CG  1 
ATOM   182   C CD  . LYS A 1 24  ? -15.866 24.711  7.394   1.00 56.38  ? 32  LYS A CD  1 
ATOM   183   C CE  . LYS A 1 24  ? -15.171 23.793  6.403   1.00 55.91  ? 32  LYS A CE  1 
ATOM   184   N NZ  . LYS A 1 24  ? -14.243 22.837  7.073   1.00 64.05  ? 32  LYS A NZ  1 
ATOM   185   N N   . ASN A 1 25  ? -18.430 28.696  4.878   1.00 50.90  ? 33  ASN A N   1 
ATOM   186   C CA  . ASN A 1 25  ? -18.539 29.568  3.709   1.00 52.69  ? 33  ASN A CA  1 
ATOM   187   C C   . ASN A 1 25  ? -19.983 30.032  3.503   1.00 50.15  ? 33  ASN A C   1 
ATOM   188   O O   . ASN A 1 25  ? -20.611 29.770  2.476   1.00 45.23  ? 33  ASN A O   1 
ATOM   189   C CB  . ASN A 1 25  ? -17.997 28.873  2.454   1.00 53.37  ? 33  ASN A CB  1 
ATOM   190   C CG  . ASN A 1 25  ? -16.496 28.633  2.516   1.00 71.01  ? 33  ASN A CG  1 
ATOM   191   O OD1 . ASN A 1 25  ? -15.877 28.746  3.576   1.00 80.34  ? 33  ASN A OD1 1 
ATOM   192   N ND2 . ASN A 1 25  ? -15.903 28.300  1.373   1.00 85.79  ? 33  ASN A ND2 1 
ATOM   193   N N   . VAL A 1 26  ? -20.499 30.734  4.508   1.00 48.53  ? 34  VAL A N   1 
ATOM   194   C CA  . VAL A 1 26  ? -21.833 31.324  4.469   1.00 38.82  ? 34  VAL A CA  1 
ATOM   195   C C   . VAL A 1 26  ? -21.687 32.797  4.108   1.00 40.56  ? 34  VAL A C   1 
ATOM   196   O O   . VAL A 1 26  ? -21.015 33.553  4.820   1.00 47.06  ? 34  VAL A O   1 
ATOM   197   C CB  . VAL A 1 26  ? -22.559 31.159  5.813   1.00 46.88  ? 34  VAL A CB  1 
ATOM   198   C CG1 . VAL A 1 26  ? -23.843 31.984  5.830   1.00 41.22  ? 34  VAL A CG1 1 
ATOM   199   C CG2 . VAL A 1 26  ? -22.853 29.690  6.090   1.00 39.98  ? 34  VAL A CG2 1 
ATOM   200   N N   . THR A 1 27  ? -22.311 33.209  3.007   1.00 37.48  ? 35  THR A N   1 
ATOM   201   C CA  . THR A 1 27  ? -22.256 34.602  2.576   1.00 45.16  ? 35  THR A CA  1 
ATOM   202   C C   . THR A 1 27  ? -23.193 35.456  3.425   1.00 44.84  ? 35  THR A C   1 
ATOM   203   O O   . THR A 1 27  ? -24.382 35.145  3.559   1.00 40.98  ? 35  THR A O   1 
ATOM   204   C CB  . THR A 1 27  ? -22.631 34.724  1.098   1.00 38.66  ? 35  THR A CB  1 
ATOM   205   O OG1 . THR A 1 27  ? -21.803 33.855  0.315   1.00 47.45  ? 35  THR A OG1 1 
ATOM   206   C CG2 . THR A 1 27  ? -22.443 36.148  0.616   1.00 37.95  ? 35  THR A CG2 1 
ATOM   207   N N   . VAL A 1 28  ? -22.658 36.541  3.986   1.00 37.79  ? 36  VAL A N   1 
ATOM   208   C CA  . VAL A 1 28  ? -23.413 37.434  4.856   1.00 37.23  ? 36  VAL A CA  1 
ATOM   209   C C   . VAL A 1 28  ? -23.371 38.846  4.284   1.00 49.14  ? 36  VAL A C   1 
ATOM   210   O O   . VAL A 1 28  ? -22.423 39.228  3.590   1.00 46.22  ? 36  VAL A O   1 
ATOM   211   C CB  . VAL A 1 28  ? -22.874 37.417  6.302   1.00 51.13  ? 36  VAL A CB  1 
ATOM   212   C CG1 . VAL A 1 28  ? -23.151 36.068  6.952   1.00 42.72  ? 36  VAL A CG1 1 
ATOM   213   C CG2 . VAL A 1 28  ? -21.377 37.744  6.326   1.00 42.64  ? 36  VAL A CG2 1 
ATOM   214   N N   . THR A 1 29  ? -24.413 39.628  4.592   1.00 51.35  ? 37  THR A N   1 
ATOM   215   C CA  . THR A 1 29  ? -24.505 40.991  4.070   1.00 51.07  ? 37  THR A CA  1 
ATOM   216   C C   . THR A 1 29  ? -23.430 41.902  4.655   1.00 52.09  ? 37  THR A C   1 
ATOM   217   O O   . THR A 1 29  ? -23.030 42.876  4.009   1.00 55.26  ? 37  THR A O   1 
ATOM   218   C CB  . THR A 1 29  ? -25.894 41.581  4.342   1.00 41.57  ? 37  THR A CB  1 
ATOM   219   O OG1 . THR A 1 29  ? -26.166 41.561  5.747   1.00 44.00  ? 37  THR A OG1 1 
ATOM   220   C CG2 . THR A 1 29  ? -26.970 40.789  3.616   1.00 48.50  ? 37  THR A CG2 1 
ATOM   221   N N   . HIS A 1 30  ? -22.958 41.613  5.866   1.00 53.96  ? 38  HIS A N   1 
ATOM   222   C CA  . HIS A 1 30  ? -21.883 42.385  6.472   1.00 51.44  ? 38  HIS A CA  1 
ATOM   223   C C   . HIS A 1 30  ? -21.141 41.508  7.469   1.00 51.84  ? 38  HIS A C   1 
ATOM   224   O O   . HIS A 1 30  ? -21.717 40.591  8.059   1.00 50.29  ? 38  HIS A O   1 
ATOM   225   C CB  . HIS A 1 30  ? -22.406 43.650  7.164   1.00 56.19  ? 38  HIS A CB  1 
ATOM   226   C CG  . HIS A 1 30  ? -21.346 44.678  7.417   1.00 80.45  ? 38  HIS A CG  1 
ATOM   227   N ND1 . HIS A 1 30  ? -20.307 44.907  6.538   1.00 86.71  ? 38  HIS A ND1 1 
ATOM   228   C CD2 . HIS A 1 30  ? -21.160 45.535  8.449   1.00 91.71  ? 38  HIS A CD2 1 
ATOM   229   C CE1 . HIS A 1 30  ? -19.529 45.861  7.019   1.00 81.37  ? 38  HIS A CE1 1 
ATOM   230   N NE2 . HIS A 1 30  ? -20.025 46.259  8.177   1.00 86.34  ? 38  HIS A NE2 1 
ATOM   231   N N   . ALA A 1 31  ? -19.857 41.806  7.654   1.00 58.24  ? 39  ALA A N   1 
ATOM   232   C CA  . ALA A 1 31  ? -19.006 41.028  8.542   1.00 57.66  ? 39  ALA A CA  1 
ATOM   233   C C   . ALA A 1 31  ? -17.865 41.906  9.029   1.00 51.81  ? 39  ALA A C   1 
ATOM   234   O O   . ALA A 1 31  ? -17.570 42.952  8.446   1.00 65.43  ? 39  ALA A O   1 
ATOM   235   C CB  . ALA A 1 31  ? -18.459 39.774  7.847   1.00 47.00  ? 39  ALA A CB  1 
ATOM   236   N N   . GLN A 1 32  ? -17.219 41.466  10.106  1.00 45.26  ? 40  GLN A N   1 
ATOM   237   C CA  . GLN A 1 32  ? -16.151 42.243  10.725  1.00 52.12  ? 40  GLN A CA  1 
ATOM   238   C C   . GLN A 1 32  ? -15.078 41.301  11.251  1.00 47.68  ? 40  GLN A C   1 
ATOM   239   O O   . GLN A 1 32  ? -15.382 40.398  12.036  1.00 46.17  ? 40  GLN A O   1 
ATOM   240   C CB  . GLN A 1 32  ? -16.709 43.111  11.854  1.00 50.46  ? 40  GLN A CB  1 
ATOM   241   C CG  . GLN A 1 32  ? -15.657 43.681  12.782  1.00 53.48  ? 40  GLN A CG  1 
ATOM   242   C CD  . GLN A 1 32  ? -16.133 44.934  13.488  1.00 64.80  ? 40  GLN A CD  1 
ATOM   243   O OE1 . GLN A 1 32  ? -17.318 45.070  13.804  1.00 66.57  ? 40  GLN A OE1 1 
ATOM   244   N NE2 . GLN A 1 32  ? -15.211 45.853  13.748  1.00 78.59  ? 40  GLN A NE2 1 
ATOM   245   N N   . ASP A 1 33  ? -13.833 41.514  10.826  1.00 58.35  ? 41  ASP A N   1 
ATOM   246   C CA  . ASP A 1 33  ? -12.703 40.746  11.339  1.00 56.67  ? 41  ASP A CA  1 
ATOM   247   C C   . ASP A 1 33  ? -12.218 41.331  12.661  1.00 53.16  ? 41  ASP A C   1 
ATOM   248   O O   . ASP A 1 33  ? -12.160 42.552  12.832  1.00 59.77  ? 41  ASP A O   1 
ATOM   249   C CB  . ASP A 1 33  ? -11.557 40.735  10.320  1.00 44.65  ? 41  ASP A CB  1 
ATOM   250   C CG  . ASP A 1 33  ? -10.601 39.555  10.513  1.00 68.89  ? 41  ASP A CG  1 
ATOM   251   O OD1 . ASP A 1 33  ? -10.369 39.146  11.673  1.00 66.43  ? 41  ASP A OD1 1 
ATOM   252   O OD2 . ASP A 1 33  ? -10.082 39.028  9.500   1.00 55.56  ? 41  ASP A OD2 1 
ATOM   253   N N   . ILE A 1 34  ? -11.872 40.452  13.602  1.00 47.80  ? 42  ILE A N   1 
ATOM   254   C CA  . ILE A 1 34  ? -11.350 40.862  14.901  1.00 47.53  ? 42  ILE A CA  1 
ATOM   255   C C   . ILE A 1 34  ? -9.894  40.444  15.091  1.00 47.82  ? 42  ILE A C   1 
ATOM   256   O O   . ILE A 1 34  ? -9.371  40.524  16.208  1.00 48.95  ? 42  ILE A O   1 
ATOM   257   C CB  . ILE A 1 34  ? -12.223 40.330  16.048  1.00 43.75  ? 42  ILE A CB  1 
ATOM   258   C CG1 . ILE A 1 34  ? -12.301 38.804  15.994  1.00 47.28  ? 42  ILE A CG1 1 
ATOM   259   C CG2 . ILE A 1 34  ? -13.609 40.934  15.980  1.00 47.81  ? 42  ILE A CG2 1 
ATOM   260   C CD1 . ILE A 1 34  ? -12.480 38.160  17.344  1.00 38.01  ? 42  ILE A CD1 1 
ATOM   261   N N   . LEU A 1 35  ? -9.219  40.012  14.027  1.00 51.16  ? 43  LEU A N   1 
ATOM   262   C CA  . LEU A 1 35  ? -7.814  39.622  14.078  1.00 54.68  ? 43  LEU A CA  1 
ATOM   263   C C   . LEU A 1 35  ? -6.962  40.723  13.460  1.00 52.45  ? 43  LEU A C   1 
ATOM   264   O O   . LEU A 1 35  ? -7.140  41.060  12.285  1.00 43.51  ? 43  LEU A O   1 
ATOM   265   C CB  . LEU A 1 35  ? -7.585  38.306  13.337  1.00 47.21  ? 43  LEU A CB  1 
ATOM   266   C CG  . LEU A 1 35  ? -6.124  37.870  13.234  1.00 44.31  ? 43  LEU A CG  1 
ATOM   267   C CD1 . LEU A 1 35  ? -5.651  37.393  14.576  1.00 45.49  ? 43  LEU A CD1 1 
ATOM   268   C CD2 . LEU A 1 35  ? -5.952  36.778  12.201  1.00 44.20  ? 43  LEU A CD2 1 
ATOM   269   N N   . GLU A 1 36  ? -6.025  41.263  14.240  1.00 55.72  ? 44  GLU A N   1 
ATOM   270   C CA  . GLU A 1 36  ? -5.123  42.290  13.731  1.00 51.79  ? 44  GLU A CA  1 
ATOM   271   C C   . GLU A 1 36  ? -4.052  41.659  12.851  1.00 47.31  ? 44  GLU A C   1 
ATOM   272   O O   . GLU A 1 36  ? -3.380  40.705  13.257  1.00 49.66  ? 44  GLU A O   1 
ATOM   273   C CB  . GLU A 1 36  ? -4.473  43.062  14.876  1.00 46.22  ? 44  GLU A CB  1 
ATOM   274   C CG  . GLU A 1 36  ? -3.999  44.452  14.479  1.00 61.90  ? 44  GLU A CG  1 
ATOM   275   C CD  . GLU A 1 36  ? -5.090  45.277  13.815  1.00 64.15  ? 44  GLU A CD  1 
ATOM   276   O OE1 . GLU A 1 36  ? -6.064  45.653  14.501  1.00 65.70  ? 44  GLU A OE1 1 
ATOM   277   O OE2 . GLU A 1 36  ? -4.976  45.540  12.602  1.00 62.08  ? 44  GLU A OE2 1 
ATOM   278   N N   . LYS A 1 37  ? -3.896  42.194  11.642  1.00 49.76  ? 45  LYS A N   1 
ATOM   279   C CA  . LYS A 1 37  ? -2.949  41.653  10.677  1.00 50.17  ? 45  LYS A CA  1 
ATOM   280   C C   . LYS A 1 37  ? -2.071  42.735  10.064  1.00 50.63  ? 45  LYS A C   1 
ATOM   281   O O   . LYS A 1 37  ? -1.391  42.471  9.065   1.00 57.42  ? 45  LYS A O   1 
ATOM   282   C CB  . LYS A 1 37  ? -3.684  40.894  9.563   1.00 50.35  ? 45  LYS A CB  1 
ATOM   283   C CG  . LYS A 1 37  ? -4.437  39.662  10.028  1.00 63.49  ? 45  LYS A CG  1 
ATOM   284   C CD  . LYS A 1 37  ? -5.190  39.002  8.877   1.00 67.47  ? 45  LYS A CD  1 
ATOM   285   C CE  . LYS A 1 37  ? -6.451  39.772  8.525   1.00 61.90  ? 45  LYS A CE  1 
ATOM   286   N NZ  . LYS A 1 37  ? -7.534  39.536  9.519   1.00 66.22  ? 45  LYS A NZ  1 
ATOM   287   N N   . THR A 1 38  ? -2.065  43.939  10.628  1.00 52.78  ? 46  THR A N   1 
ATOM   288   C CA  . THR A 1 38  ? -1.353  45.064  10.040  1.00 65.43  ? 46  THR A CA  1 
ATOM   289   C C   . THR A 1 38  ? -0.413  45.682  11.065  1.00 58.35  ? 46  THR A C   1 
ATOM   290   O O   . THR A 1 38  ? -0.814  45.951  12.202  1.00 49.83  ? 46  THR A O   1 
ATOM   291   C CB  . THR A 1 38  ? -2.334  46.121  9.520   1.00 65.40  ? 46  THR A CB  1 
ATOM   292   O OG1 . THR A 1 38  ? -3.358  46.347  10.497  1.00 63.63  ? 46  THR A OG1 1 
ATOM   293   C CG2 . THR A 1 38  ? -2.977  45.650  8.224   1.00 60.17  ? 46  THR A CG2 1 
ATOM   294   N N   . HIS A 1 39  ? 0.830   45.905  10.654  1.00 57.17  ? 47  HIS A N   1 
ATOM   295   C CA  . HIS A 1 39  ? 1.803   46.671  11.417  1.00 68.09  ? 47  HIS A CA  1 
ATOM   296   C C   . HIS A 1 39  ? 2.286   47.839  10.563  1.00 63.23  ? 47  HIS A C   1 
ATOM   297   O O   . HIS A 1 39  ? 1.926   47.967  9.391   1.00 62.64  ? 47  HIS A O   1 
ATOM   298   C CB  . HIS A 1 39  ? 2.980   45.793  11.863  1.00 55.11  ? 47  HIS A CB  1 
ATOM   299   C CG  . HIS A 1 39  ? 3.651   45.066  10.739  1.00 54.64  ? 47  HIS A CG  1 
ATOM   300   N ND1 . HIS A 1 39  ? 4.794   45.536  10.128  1.00 51.81  ? 47  HIS A ND1 1 
ATOM   301   C CD2 . HIS A 1 39  ? 3.341   43.905  10.115  1.00 51.92  ? 47  HIS A CD2 1 
ATOM   302   C CE1 . HIS A 1 39  ? 5.158   44.695  9.176   1.00 63.42  ? 47  HIS A CE1 1 
ATOM   303   N NE2 . HIS A 1 39  ? 4.292   43.697  9.146   1.00 48.46  ? 47  HIS A NE2 1 
ATOM   304   N N   . ASN A 1 40  ? 3.101   48.707  11.163  1.00 52.00  ? 48  ASN A N   1 
ATOM   305   C CA  . ASN A 1 40  ? 3.655   49.855  10.456  1.00 53.45  ? 48  ASN A CA  1 
ATOM   306   C C   . ASN A 1 40  ? 5.065   49.612  9.930   1.00 61.38  ? 48  ASN A C   1 
ATOM   307   O O   . ASN A 1 40  ? 5.630   50.497  9.279   1.00 65.75  ? 48  ASN A O   1 
ATOM   308   C CB  . ASN A 1 40  ? 3.637   51.095  11.364  1.00 48.07  ? 48  ASN A CB  1 
ATOM   309   C CG  . ASN A 1 40  ? 4.642   51.012  12.501  1.00 55.80  ? 48  ASN A CG  1 
ATOM   310   O OD1 . ASN A 1 40  ? 5.207   49.952  12.781  1.00 55.34  ? 48  ASN A OD1 1 
ATOM   311   N ND2 . ASN A 1 40  ? 4.842   52.128  13.185  1.00 49.90  ? 48  ASN A ND2 1 
ATOM   312   N N   . GLY A 1 41  ? 5.648   48.447  10.205  1.00 58.23  ? 49  GLY A N   1 
ATOM   313   C CA  . GLY A 1 41  ? 6.975   48.133  9.703   1.00 57.08  ? 49  GLY A CA  1 
ATOM   314   C C   . GLY A 1 41  ? 8.086   49.013  10.228  1.00 60.22  ? 49  GLY A C   1 
ATOM   315   O O   . GLY A 1 41  ? 9.134   49.114  9.587   1.00 57.99  ? 49  GLY A O   1 
ATOM   316   N N   . ARG A 1 42  ? 7.900   49.641  11.388  1.00 61.03  ? 50  ARG A N   1 
ATOM   317   C CA  . ARG A 1 42  ? 8.847   50.615  11.909  1.00 61.99  ? 50  ARG A CA  1 
ATOM   318   C C   . ARG A 1 42  ? 9.118   50.351  13.384  1.00 64.65  ? 50  ARG A C   1 
ATOM   319   O O   . ARG A 1 42  ? 8.301   49.758  14.092  1.00 59.43  ? 50  ARG A O   1 
ATOM   320   C CB  . ARG A 1 42  ? 8.327   52.051  11.732  1.00 62.09  ? 50  ARG A CB  1 
ATOM   321   C CG  . ARG A 1 42  ? 8.854   52.766  10.500  1.00 67.52  ? 50  ARG A CG  1 
ATOM   322   C CD  . ARG A 1 42  ? 7.799   53.691  9.902   1.00 78.20  ? 50  ARG A CD  1 
ATOM   323   N NE  . ARG A 1 42  ? 8.280   54.359  8.697   1.00 94.55  ? 50  ARG A NE  1 
ATOM   324   C CZ  . ARG A 1 42  ? 8.568   55.651  8.619   1.00 101.25 ? 50  ARG A CZ  1 
ATOM   325   N NH1 . ARG A 1 42  ? 8.421   56.456  9.660   1.00 91.66  ? 50  ARG A NH1 1 
ATOM   326   N NH2 . ARG A 1 42  ? 9.015   56.148  7.469   1.00 97.49  ? 50  ARG A NH2 1 
ATOM   327   N N   . LEU A 1 43  ? 10.290  50.799  13.837  1.00 66.66  ? 51  LEU A N   1 
ATOM   328   C CA  . LEU A 1 43  ? 10.642  50.789  15.253  1.00 50.34  ? 51  LEU A CA  1 
ATOM   329   C C   . LEU A 1 43  ? 10.215  52.114  15.873  1.00 52.06  ? 51  LEU A C   1 
ATOM   330   O O   . LEU A 1 43  ? 10.708  53.174  15.477  1.00 60.26  ? 51  LEU A O   1 
ATOM   331   C CB  . LEU A 1 43  ? 12.141  50.569  15.446  1.00 61.41  ? 51  LEU A CB  1 
ATOM   332   C CG  . LEU A 1 43  ? 12.650  49.135  15.306  1.00 67.69  ? 51  LEU A CG  1 
ATOM   333   C CD1 . LEU A 1 43  ? 14.153  49.070  15.544  1.00 64.16  ? 51  LEU A CD1 1 
ATOM   334   C CD2 . LEU A 1 43  ? 11.913  48.211  16.261  1.00 61.57  ? 51  LEU A CD2 1 
ATOM   335   N N   . CYS A 1 44  ? 9.315   52.053  16.846  1.00 51.02  ? 52  CYS A N   1 
ATOM   336   C CA  . CYS A 1 44  ? 8.663   53.234  17.388  1.00 58.06  ? 52  CYS A CA  1 
ATOM   337   C C   . CYS A 1 44  ? 9.061   53.451  18.841  1.00 52.64  ? 52  CYS A C   1 
ATOM   338   O O   . CYS A 1 44  ? 9.722   52.617  19.467  1.00 45.71  ? 52  CYS A O   1 
ATOM   339   C CB  . CYS A 1 44  ? 7.139   53.107  17.277  1.00 51.96  ? 52  CYS A CB  1 
ATOM   340   S SG  . CYS A 1 44  ? 6.498   52.980  15.590  1.00 74.34  ? 52  CYS A SG  1 
ATOM   341   N N   . ASP A 1 45  ? 8.650   54.604  19.368  1.00 56.02  ? 53  ASP A N   1 
ATOM   342   C CA  . ASP A 1 45  ? 8.723   54.847  20.798  1.00 51.14  ? 53  ASP A CA  1 
ATOM   343   C C   . ASP A 1 45  ? 7.673   54.013  21.517  1.00 57.29  ? 53  ASP A C   1 
ATOM   344   O O   . ASP A 1 45  ? 6.652   53.621  20.944  1.00 56.47  ? 53  ASP A O   1 
ATOM   345   C CB  . ASP A 1 45  ? 8.494   56.325  21.120  1.00 56.82  ? 53  ASP A CB  1 
ATOM   346   C CG  . ASP A 1 45  ? 9.598   57.219  20.601  1.00 64.05  ? 53  ASP A CG  1 
ATOM   347   O OD1 . ASP A 1 45  ? 10.577  56.700  20.026  1.00 72.54  ? 53  ASP A OD1 1 
ATOM   348   O OD2 . ASP A 1 45  ? 9.480   58.450  20.768  1.00 70.87  ? 53  ASP A OD2 1 
ATOM   349   N N   . LEU A 1 46  ? 7.925   53.751  22.791  1.00 49.11  ? 54  LEU A N   1 
ATOM   350   C CA  . LEU A 1 46  ? 6.995   53.005  23.629  1.00 54.37  ? 54  LEU A CA  1 
ATOM   351   C C   . LEU A 1 46  ? 6.460   53.957  24.692  1.00 61.56  ? 54  LEU A C   1 
ATOM   352   O O   . LEU A 1 46  ? 7.154   54.267  25.665  1.00 61.49  ? 54  LEU A O   1 
ATOM   353   C CB  . LEU A 1 46  ? 7.671   51.787  24.250  1.00 57.35  ? 54  LEU A CB  1 
ATOM   354   C CG  . LEU A 1 46  ? 6.742   50.851  25.022  1.00 60.80  ? 54  LEU A CG  1 
ATOM   355   C CD1 . LEU A 1 46  ? 5.651   50.315  24.103  1.00 49.02  ? 54  LEU A CD1 1 
ATOM   356   C CD2 . LEU A 1 46  ? 7.532   49.717  25.657  1.00 41.56  ? 54  LEU A CD2 1 
ATOM   357   N N   . ASN A 1 47  ? 5.221   54.418  24.494  1.00 55.08  ? 55  ASN A N   1 
ATOM   358   C CA  . ASN A 1 47  ? 4.552   55.324  25.427  1.00 50.56  ? 55  ASN A CA  1 
ATOM   359   C C   . ASN A 1 47  ? 5.371   56.597  25.639  1.00 52.93  ? 55  ASN A C   1 
ATOM   360   O O   . ASN A 1 47  ? 5.611   57.032  26.767  1.00 56.32  ? 55  ASN A O   1 
ATOM   361   C CB  . ASN A 1 47  ? 4.257   54.624  26.756  1.00 49.55  ? 55  ASN A CB  1 
ATOM   362   C CG  . ASN A 1 47  ? 3.503   53.315  26.571  1.00 68.70  ? 55  ASN A CG  1 
ATOM   363   O OD1 . ASN A 1 47  ? 2.491   53.261  25.871  1.00 63.00  ? 55  ASN A OD1 1 
ATOM   364   N ND2 . ASN A 1 47  ? 3.995   52.253  27.203  1.00 74.57  ? 55  ASN A ND2 1 
ATOM   365   N N   . GLY A 1 48  A 5.813   57.189  24.530  1.00 54.16  ? 55  GLY A N   1 
ATOM   366   C CA  . GLY A 1 48  A 6.523   58.450  24.562  1.00 54.91  ? 55  GLY A CA  1 
ATOM   367   C C   . GLY A 1 48  A 7.985   58.370  24.940  1.00 64.97  ? 55  GLY A C   1 
ATOM   368   O O   . GLY A 1 48  A 8.608   59.418  25.152  1.00 56.51  ? 55  GLY A O   1 
ATOM   369   N N   . VAL A 1 49  ? 8.553   57.169  25.032  1.00 57.90  ? 56  VAL A N   1 
ATOM   370   C CA  . VAL A 1 49  ? 9.951   56.978  25.397  1.00 49.49  ? 56  VAL A CA  1 
ATOM   371   C C   . VAL A 1 49  ? 10.647  56.239  24.260  1.00 55.95  ? 56  VAL A C   1 
ATOM   372   O O   . VAL A 1 49  ? 10.204  55.161  23.847  1.00 59.72  ? 56  VAL A O   1 
ATOM   373   C CB  . VAL A 1 49  ? 10.090  56.212  26.723  1.00 53.67  ? 56  VAL A CB  1 
ATOM   374   C CG1 . VAL A 1 49  ? 11.558  56.004  27.069  1.00 56.27  ? 56  VAL A CG1 1 
ATOM   375   C CG2 . VAL A 1 49  ? 9.376   56.967  27.834  1.00 41.65  ? 56  VAL A CG2 1 
ATOM   376   N N   . LYS A 1 50  ? 11.731  56.826  23.759  1.00 56.45  ? 57  LYS A N   1 
ATOM   377   C CA  . LYS A 1 50  ? 12.442  56.267  22.618  1.00 54.51  ? 57  LYS A CA  1 
ATOM   378   C C   . LYS A 1 50  ? 13.242  55.038  23.046  1.00 49.20  ? 57  LYS A C   1 
ATOM   379   O O   . LYS A 1 50  ? 13.731  54.978  24.177  1.00 49.07  ? 57  LYS A O   1 
ATOM   380   C CB  . LYS A 1 50  ? 13.372  57.320  22.015  1.00 64.27  ? 57  LYS A CB  1 
ATOM   381   C CG  . LYS A 1 50  ? 14.122  56.890  20.762  1.00 51.14  ? 57  LYS A CG  1 
ATOM   382   C CD  . LYS A 1 50  ? 14.770  58.080  20.072  1.00 61.12  ? 57  LYS A CD  1 
ATOM   383   C CE  . LYS A 1 50  ? 15.602  57.637  18.878  1.00 68.60  ? 57  LYS A CE  1 
ATOM   384   N NZ  . LYS A 1 50  ? 17.009  57.334  19.259  1.00 72.28  ? 57  LYS A NZ  1 
ATOM   385   N N   . PRO A 1 51  ? 13.366  54.033  22.183  1.00 44.87  ? 58  PRO A N   1 
ATOM   386   C CA  . PRO A 1 51  ? 14.231  52.894  22.498  1.00 46.34  ? 58  PRO A CA  1 
ATOM   387   C C   . PRO A 1 51  ? 15.701  53.211  22.273  1.00 51.97  ? 58  PRO A C   1 
ATOM   388   O O   . PRO A 1 51  ? 16.070  54.015  21.414  1.00 51.45  ? 58  PRO A O   1 
ATOM   389   C CB  . PRO A 1 51  ? 13.756  51.813  21.521  1.00 42.91  ? 58  PRO A CB  1 
ATOM   390   C CG  . PRO A 1 51  ? 13.237  52.585  20.360  1.00 46.52  ? 58  PRO A CG  1 
ATOM   391   C CD  . PRO A 1 51  ? 12.591  53.809  20.950  1.00 50.67  ? 58  PRO A CD  1 
ATOM   392   N N   . LEU A 1 52  ? 16.544  52.546  23.059  1.00 52.19  ? 59  LEU A N   1 
ATOM   393   C CA  . LEU A 1 52  ? 17.986  52.589  22.845  1.00 51.36  ? 59  LEU A CA  1 
ATOM   394   C C   . LEU A 1 52  ? 18.327  51.617  21.723  1.00 55.62  ? 59  LEU A C   1 
ATOM   395   O O   . LEU A 1 52  ? 18.234  50.398  21.898  1.00 58.00  ? 59  LEU A O   1 
ATOM   396   C CB  . LEU A 1 52  ? 18.735  52.239  24.130  1.00 52.65  ? 59  LEU A CB  1 
ATOM   397   C CG  . LEU A 1 52  ? 20.241  51.981  23.995  1.00 57.21  ? 59  LEU A CG  1 
ATOM   398   C CD1 . LEU A 1 52  ? 20.962  53.219  23.492  1.00 61.01  ? 59  LEU A CD1 1 
ATOM   399   C CD2 . LEU A 1 52  ? 20.849  51.514  25.305  1.00 54.53  ? 59  LEU A CD2 1 
ATOM   400   N N   . ILE A 1 53  ? 18.707  52.148  20.565  1.00 57.42  ? 60  ILE A N   1 
ATOM   401   C CA  . ILE A 1 53  ? 19.031  51.336  19.397  1.00 62.18  ? 60  ILE A CA  1 
ATOM   402   C C   . ILE A 1 53  ? 20.548  51.288  19.263  1.00 60.40  ? 60  ILE A C   1 
ATOM   403   O O   . ILE A 1 53  ? 21.179  52.270  18.858  1.00 72.64  ? 60  ILE A O   1 
ATOM   404   C CB  . ILE A 1 53  ? 18.370  51.882  18.125  1.00 59.45  ? 60  ILE A CB  1 
ATOM   405   C CG1 . ILE A 1 53  ? 16.854  51.672  18.184  1.00 66.05  ? 60  ILE A CG1 1 
ATOM   406   C CG2 . ILE A 1 53  ? 18.956  51.206  16.891  1.00 52.25  ? 60  ILE A CG2 1 
ATOM   407   C CD1 . ILE A 1 53  ? 16.040  52.860  17.705  1.00 56.93  ? 60  ILE A CD1 1 
ATOM   408   N N   . LEU A 1 54  ? 21.138  50.149  19.612  1.00 64.66  ? 61  LEU A N   1 
ATOM   409   C CA  . LEU A 1 54  ? 22.566  49.927  19.411  1.00 66.11  ? 61  LEU A CA  1 
ATOM   410   C C   . LEU A 1 54  ? 22.772  49.460  17.976  1.00 69.40  ? 61  LEU A C   1 
ATOM   411   O O   . LEU A 1 54  ? 22.423  48.328  17.630  1.00 82.86  ? 61  LEU A O   1 
ATOM   412   C CB  . LEU A 1 54  ? 23.100  48.906  20.411  1.00 54.26  ? 61  LEU A CB  1 
ATOM   413   C CG  . LEU A 1 54  ? 22.666  49.130  21.861  1.00 58.66  ? 61  LEU A CG  1 
ATOM   414   C CD1 . LEU A 1 54  ? 22.975  47.913  22.714  1.00 52.07  ? 61  LEU A CD1 1 
ATOM   415   C CD2 . LEU A 1 54  ? 23.320  50.385  22.436  1.00 55.87  ? 61  LEU A CD2 1 
ATOM   416   N N   . LYS A 1 55  ? 23.328  50.338  17.141  1.00 80.18  ? 62  LYS A N   1 
ATOM   417   C CA  . LYS A 1 55  ? 23.373  50.075  15.708  1.00 81.04  ? 62  LYS A CA  1 
ATOM   418   C C   . LYS A 1 55  ? 24.136  48.793  15.409  1.00 72.13  ? 62  LYS A C   1 
ATOM   419   O O   . LYS A 1 55  ? 23.559  47.801  14.960  1.00 75.06  ? 62  LYS A O   1 
ATOM   420   C CB  . LYS A 1 55  ? 23.990  51.269  14.970  1.00 83.39  ? 62  LYS A CB  1 
ATOM   421   C CG  . LYS A 1 55  ? 23.075  51.887  13.916  1.00 81.52  ? 62  LYS A CG  1 
ATOM   422   C CD  . LYS A 1 55  ? 21.820  52.483  14.543  1.00 77.60  ? 62  LYS A CD  1 
ATOM   423   C CE  . LYS A 1 55  ? 22.093  53.865  15.119  1.00 88.94  ? 62  LYS A CE  1 
ATOM   424   N NZ  . LYS A 1 55  ? 20.933  54.374  15.901  1.00 58.65  ? 62  LYS A NZ  1 
ATOM   425   N N   . ASP A 1 56  ? 25.440  48.779  15.687  1.00 67.15  ? 63  ASP A N   1 
ATOM   426   C CA  . ASP A 1 56  ? 26.269  47.629  15.343  1.00 74.63  ? 63  ASP A CA  1 
ATOM   427   C C   . ASP A 1 56  ? 27.012  47.075  16.552  1.00 69.32  ? 63  ASP A C   1 
ATOM   428   O O   . ASP A 1 56  ? 27.940  46.277  16.388  1.00 66.59  ? 63  ASP A O   1 
ATOM   429   C CB  . ASP A 1 56  ? 27.258  47.995  14.232  1.00 79.97  ? 63  ASP A CB  1 
ATOM   430   C CG  . ASP A 1 56  ? 28.175  49.146  14.617  1.00 101.02 ? 63  ASP A CG  1 
ATOM   431   O OD1 . ASP A 1 56  ? 27.717  50.078  15.315  1.00 104.03 ? 63  ASP A OD1 1 
ATOM   432   O OD2 . ASP A 1 56  ? 29.361  49.120  14.222  1.00 102.32 ? 63  ASP A OD2 1 
ATOM   433   N N   . CYS A 1 57  ? 26.615  47.467  17.759  1.00 64.07  ? 64  CYS A N   1 
ATOM   434   C CA  . CYS A 1 57  ? 27.298  47.056  18.974  1.00 68.56  ? 64  CYS A CA  1 
ATOM   435   C C   . CYS A 1 57  ? 26.369  46.271  19.887  1.00 63.53  ? 64  CYS A C   1 
ATOM   436   O O   . CYS A 1 57  ? 25.156  46.497  19.918  1.00 64.28  ? 64  CYS A O   1 
ATOM   437   C CB  . CYS A 1 57  ? 27.859  48.262  19.734  1.00 64.18  ? 64  CYS A CB  1 
ATOM   438   S SG  . CYS A 1 57  ? 29.264  49.025  18.914  1.00 108.12 ? 64  CYS A SG  1 
ATOM   439   N N   . SER A 1 58  ? 26.961  45.332  20.618  1.00 57.10  ? 65  SER A N   1 
ATOM   440   C CA  . SER A 1 58  ? 26.274  44.615  21.676  1.00 51.32  ? 65  SER A CA  1 
ATOM   441   C C   . SER A 1 58  ? 26.228  45.470  22.936  1.00 51.28  ? 65  SER A C   1 
ATOM   442   O O   . SER A 1 58  ? 26.921  46.484  23.058  1.00 45.25  ? 65  SER A O   1 
ATOM   443   C CB  . SER A 1 58  ? 26.969  43.287  21.960  1.00 40.59  ? 65  SER A CB  1 
ATOM   444   O OG  . SER A 1 58  ? 28.113  43.481  22.777  1.00 53.35  ? 65  SER A OG  1 
ATOM   445   N N   . VAL A 1 59  ? 25.399  45.045  23.890  1.00 48.81  ? 66  VAL A N   1 
ATOM   446   C CA  . VAL A 1 59  ? 25.282  45.792  25.139  1.00 50.71  ? 66  VAL A CA  1 
ATOM   447   C C   . VAL A 1 59  ? 26.626  45.842  25.857  1.00 49.67  ? 66  VAL A C   1 
ATOM   448   O O   . VAL A 1 59  ? 27.025  46.888  26.383  1.00 42.61  ? 66  VAL A O   1 
ATOM   449   C CB  . VAL A 1 59  ? 24.176  45.186  26.021  1.00 44.92  ? 66  VAL A CB  1 
ATOM   450   C CG1 . VAL A 1 59  ? 24.129  45.889  27.373  1.00 38.68  ? 66  VAL A CG1 1 
ATOM   451   C CG2 . VAL A 1 59  ? 22.828  45.292  25.312  1.00 41.24  ? 66  VAL A CG2 1 
ATOM   452   N N   . ALA A 1 60  ? 27.355  44.724  25.872  1.00 54.80  ? 67  ALA A N   1 
ATOM   453   C CA  . ALA A 1 60  ? 28.666  44.707  26.516  1.00 47.60  ? 67  ALA A CA  1 
ATOM   454   C C   . ALA A 1 60  ? 29.621  45.686  25.844  1.00 41.96  ? 67  ALA A C   1 
ATOM   455   O O   . ALA A 1 60  ? 30.294  46.475  26.516  1.00 46.70  ? 67  ALA A O   1 
ATOM   456   C CB  . ALA A 1 60  ? 29.243  43.292  26.498  1.00 41.93  ? 67  ALA A CB  1 
ATOM   457   N N   . GLY A 1 61  ? 29.680  45.660  24.511  1.00 42.64  ? 68  GLY A N   1 
ATOM   458   C CA  . GLY A 1 61  ? 30.561  46.573  23.801  1.00 37.99  ? 68  GLY A CA  1 
ATOM   459   C C   . GLY A 1 61  ? 30.201  48.026  24.034  1.00 53.00  ? 68  GLY A C   1 
ATOM   460   O O   . GLY A 1 61  ? 31.078  48.870  24.229  1.00 50.40  ? 68  GLY A O   1 
ATOM   461   N N   . TRP A 1 62  ? 28.903  48.336  24.026  1.00 50.88  ? 69  TRP A N   1 
ATOM   462   C CA  . TRP A 1 62  ? 28.461  49.700  24.290  1.00 43.42  ? 69  TRP A CA  1 
ATOM   463   C C   . TRP A 1 62  ? 28.789  50.122  25.720  1.00 46.61  ? 69  TRP A C   1 
ATOM   464   O O   . TRP A 1 62  ? 29.220  51.258  25.955  1.00 50.42  ? 69  TRP A O   1 
ATOM   465   C CB  . TRP A 1 62  ? 26.964  49.807  23.999  1.00 50.39  ? 69  TRP A CB  1 
ATOM   466   C CG  . TRP A 1 62  ? 26.282  50.999  24.573  1.00 46.15  ? 69  TRP A CG  1 
ATOM   467   C CD1 . TRP A 1 62  ? 26.365  52.286  24.129  1.00 60.60  ? 69  TRP A CD1 1 
ATOM   468   C CD2 . TRP A 1 62  ? 25.384  51.015  25.687  1.00 57.77  ? 69  TRP A CD2 1 
ATOM   469   N NE1 . TRP A 1 62  ? 25.581  53.106  24.904  1.00 52.33  ? 69  TRP A NE1 1 
ATOM   470   C CE2 . TRP A 1 62  ? 24.969  52.350  25.869  1.00 57.34  ? 69  TRP A CE2 1 
ATOM   471   C CE3 . TRP A 1 62  ? 24.891  50.030  26.550  1.00 54.80  ? 69  TRP A CE3 1 
ATOM   472   C CZ2 . TRP A 1 62  ? 24.086  52.726  26.880  1.00 52.98  ? 69  TRP A CZ2 1 
ATOM   473   C CZ3 . TRP A 1 62  ? 24.013  50.407  27.554  1.00 51.71  ? 69  TRP A CZ3 1 
ATOM   474   C CH2 . TRP A 1 62  ? 23.620  51.743  27.709  1.00 51.08  ? 69  TRP A CH2 1 
ATOM   475   N N   . LEU A 1 63  ? 28.605  49.217  26.686  1.00 47.98  ? 70  LEU A N   1 
ATOM   476   C CA  . LEU A 1 63  ? 28.882  49.548  28.083  1.00 52.67  ? 70  LEU A CA  1 
ATOM   477   C C   . LEU A 1 63  ? 30.370  49.786  28.317  1.00 48.44  ? 70  LEU A C   1 
ATOM   478   O O   . LEU A 1 63  ? 30.759  50.763  28.966  1.00 49.97  ? 70  LEU A O   1 
ATOM   479   C CB  . LEU A 1 63  ? 28.378  48.430  28.998  1.00 54.06  ? 70  LEU A CB  1 
ATOM   480   C CG  . LEU A 1 63  ? 26.941  48.518  29.513  1.00 62.61  ? 70  LEU A CG  1 
ATOM   481   C CD1 . LEU A 1 63  ? 26.725  47.505  30.636  1.00 46.43  ? 70  LEU A CD1 1 
ATOM   482   C CD2 . LEU A 1 63  ? 26.614  49.927  29.979  1.00 55.19  ? 70  LEU A CD2 1 
ATOM   483   N N   . LEU A 1 64  ? 31.216  48.894  27.806  1.00 42.46  ? 71  LEU A N   1 
ATOM   484   C CA  . LEU A 1 64  ? 32.647  48.971  28.067  1.00 55.84  ? 71  LEU A CA  1 
ATOM   485   C C   . LEU A 1 64  ? 33.358  49.999  27.198  1.00 59.09  ? 71  LEU A C   1 
ATOM   486   O O   . LEU A 1 64  ? 34.502  50.355  27.501  1.00 51.68  ? 71  LEU A O   1 
ATOM   487   C CB  . LEU A 1 64  ? 33.290  47.599  27.866  1.00 53.86  ? 71  LEU A CB  1 
ATOM   488   C CG  . LEU A 1 64  ? 33.085  46.587  28.990  1.00 43.73  ? 71  LEU A CG  1 
ATOM   489   C CD1 . LEU A 1 64  ? 33.319  45.181  28.472  1.00 43.99  ? 71  LEU A CD1 1 
ATOM   490   C CD2 . LEU A 1 64  ? 34.018  46.899  30.146  1.00 56.53  ? 71  LEU A CD2 1 
ATOM   491   N N   . GLY A 1 65  ? 32.717  50.481  26.136  1.00 52.00  ? 72  GLY A N   1 
ATOM   492   C CA  . GLY A 1 65  ? 33.334  51.463  25.272  1.00 43.75  ? 72  GLY A CA  1 
ATOM   493   C C   . GLY A 1 65  ? 34.292  50.860  24.267  1.00 53.71  ? 72  GLY A C   1 
ATOM   494   O O   . GLY A 1 65  ? 35.455  51.268  24.178  1.00 66.58  ? 72  GLY A O   1 
ATOM   495   N N   . ASN A 1 66  ? 33.814  49.875  23.519  1.00 46.30  ? 73  ASN A N   1 
ATOM   496   C CA  . ASN A 1 66  ? 34.575  49.347  22.400  1.00 53.30  ? 73  ASN A CA  1 
ATOM   497   C C   . ASN A 1 66  ? 34.902  50.488  21.443  1.00 61.03  ? 73  ASN A C   1 
ATOM   498   O O   . ASN A 1 66  ? 33.995  51.227  21.037  1.00 62.60  ? 73  ASN A O   1 
ATOM   499   C CB  . ASN A 1 66  ? 33.760  48.260  21.695  1.00 55.17  ? 73  ASN A CB  1 
ATOM   500   C CG  . ASN A 1 66  ? 34.517  47.566  20.573  1.00 55.26  ? 73  ASN A CG  1 
ATOM   501   O OD1 . ASN A 1 66  ? 35.363  48.156  19.904  1.00 65.42  ? 73  ASN A OD1 1 
ATOM   502   N ND2 . ASN A 1 66  ? 34.184  46.304  20.344  1.00 47.16  ? 73  ASN A ND2 1 
ATOM   503   N N   . PRO A 1 67  ? 36.171  50.679  21.077  1.00 66.01  ? 74  PRO A N   1 
ATOM   504   C CA  . PRO A 1 67  ? 36.517  51.812  20.202  1.00 63.39  ? 74  PRO A CA  1 
ATOM   505   C C   . PRO A 1 67  ? 35.773  51.806  18.877  1.00 63.32  ? 74  PRO A C   1 
ATOM   506   O O   . PRO A 1 67  ? 35.484  52.881  18.336  1.00 75.53  ? 74  PRO A O   1 
ATOM   507   C CB  . PRO A 1 67  ? 38.035  51.658  20.005  1.00 65.22  ? 74  PRO A CB  1 
ATOM   508   C CG  . PRO A 1 67  ? 38.375  50.272  20.509  1.00 67.75  ? 74  PRO A CG  1 
ATOM   509   C CD  . PRO A 1 67  ? 37.361  49.958  21.557  1.00 52.34  ? 74  PRO A CD  1 
ATOM   510   N N   . MET A 1 68  ? 35.434  50.629  18.343  1.00 60.85  ? 75  MET A N   1 
ATOM   511   C CA  . MET A 1 68  ? 34.643  50.576  17.117  1.00 76.91  ? 75  MET A CA  1 
ATOM   512   C C   . MET A 1 68  ? 33.192  50.998  17.340  1.00 77.33  ? 75  MET A C   1 
ATOM   513   O O   . MET A 1 68  ? 32.487  51.289  16.368  1.00 75.67  ? 75  MET A O   1 
ATOM   514   C CB  . MET A 1 68  ? 34.704  49.168  16.512  1.00 59.23  ? 75  MET A CB  1 
ATOM   515   C CG  . MET A 1 68  ? 35.923  48.931  15.628  1.00 80.05  ? 75  MET A CG  1 
ATOM   516   S SD  . MET A 1 68  ? 36.505  50.442  14.819  1.00 105.29 ? 75  MET A SD  1 
ATOM   517   C CE  . MET A 1 68  ? 38.058  49.904  14.112  1.00 67.11  ? 75  MET A CE  1 
ATOM   518   N N   . CYS A 1 69  ? 32.731  51.040  18.589  1.00 77.27  ? 76  CYS A N   1 
ATOM   519   C CA  . CYS A 1 69  ? 31.384  51.518  18.875  1.00 80.97  ? 76  CYS A CA  1 
ATOM   520   C C   . CYS A 1 69  ? 31.326  53.033  18.732  1.00 93.14  ? 76  CYS A C   1 
ATOM   521   O O   . CYS A 1 69  ? 32.159  53.749  19.296  1.00 88.14  ? 76  CYS A O   1 
ATOM   522   C CB  . CYS A 1 69  ? 30.951  51.085  20.276  1.00 77.60  ? 76  CYS A CB  1 
ATOM   523   S SG  . CYS A 1 69  ? 30.622  49.309  20.398  1.00 80.72  ? 76  CYS A SG  1 
ATOM   524   N N   . ASP A 1 70  ? 30.342  53.517  17.970  1.00 100.21 ? 77  ASP A N   1 
ATOM   525   C CA  . ASP A 1 70  ? 30.277  54.925  17.594  1.00 105.12 ? 77  ASP A CA  1 
ATOM   526   C C   . ASP A 1 70  ? 30.228  55.832  18.816  1.00 106.03 ? 77  ASP A C   1 
ATOM   527   O O   . ASP A 1 70  ? 31.202  56.533  19.109  1.00 106.46 ? 77  ASP A O   1 
ATOM   528   C CB  . ASP A 1 70  ? 29.055  55.178  16.708  1.00 107.14 ? 77  ASP A CB  1 
ATOM   529   C CG  . ASP A 1 70  ? 28.936  54.174  15.577  1.00 110.41 ? 77  ASP A CG  1 
ATOM   530   O OD1 . ASP A 1 70  ? 29.822  53.298  15.459  1.00 102.47 ? 77  ASP A OD1 1 
ATOM   531   O OD2 . ASP A 1 70  ? 27.951  54.254  14.813  1.00 103.50 ? 77  ASP A OD2 1 
ATOM   532   N N   . GLU A 1 71  ? 29.118  55.765  19.557  1.00 112.85 ? 78  GLU A N   1 
ATOM   533   C CA  . GLU A 1 71  ? 28.829  56.578  20.736  1.00 123.17 ? 78  GLU A CA  1 
ATOM   534   C C   . GLU A 1 71  ? 27.334  56.545  21.003  1.00 118.61 ? 78  GLU A C   1 
ATOM   535   O O   . GLU A 1 71  ? 26.901  56.371  22.147  1.00 113.92 ? 78  GLU A O   1 
ATOM   536   C CB  . GLU A 1 71  ? 29.272  58.037  20.572  1.00 118.38 ? 78  GLU A CB  1 
ATOM   537   C CG  . GLU A 1 71  ? 28.996  58.911  21.790  1.00 112.67 ? 78  GLU A CG  1 
ATOM   538   C CD  . GLU A 1 71  ? 29.817  58.504  23.004  1.00 123.43 ? 78  GLU A CD  1 
ATOM   539   O OE1 . GLU A 1 71  ? 30.930  57.965  22.818  1.00 124.09 ? 78  GLU A OE1 1 
ATOM   540   O OE2 . GLU A 1 71  ? 29.352  58.726  24.143  1.00 109.62 ? 78  GLU A OE2 1 
ATOM   541   N N   . PHE A 1 72  ? 26.547  56.723  19.941  1.00 116.13 ? 79  PHE A N   1 
ATOM   542   C CA  . PHE A 1 72  ? 25.089  56.827  19.998  1.00 124.38 ? 79  PHE A CA  1 
ATOM   543   C C   . PHE A 1 72  ? 24.620  58.012  20.836  1.00 122.62 ? 79  PHE A C   1 
ATOM   544   O O   . PHE A 1 72  ? 23.460  58.040  21.260  1.00 120.02 ? 79  PHE A O   1 
ATOM   545   C CB  . PHE A 1 72  ? 24.445  55.535  20.522  1.00 119.80 ? 79  PHE A CB  1 
ATOM   546   C CG  . PHE A 1 72  ? 24.986  54.283  19.896  1.00 113.52 ? 79  PHE A CG  1 
ATOM   547   C CD1 . PHE A 1 72  ? 24.608  53.914  18.617  1.00 105.52 ? 79  PHE A CD1 1 
ATOM   548   C CD2 . PHE A 1 72  ? 25.867  53.469  20.593  1.00 110.27 ? 79  PHE A CD2 1 
ATOM   549   C CE1 . PHE A 1 72  ? 25.101  52.761  18.040  1.00 103.58 ? 79  PHE A CE1 1 
ATOM   550   C CE2 . PHE A 1 72  ? 26.364  52.312  20.021  1.00 98.14  ? 79  PHE A CE2 1 
ATOM   551   C CZ  . PHE A 1 72  ? 25.980  51.957  18.743  1.00 103.00 ? 79  PHE A CZ  1 
ATOM   552   N N   . ILE A 1 73  ? 25.513  58.985  21.075  1.00 109.29 ? 80  ILE A N   1 
ATOM   553   C CA  . ILE A 1 73  ? 25.302  60.196  21.876  1.00 98.01  ? 80  ILE A CA  1 
ATOM   554   C C   . ILE A 1 73  ? 24.713  59.861  23.247  1.00 92.95  ? 80  ILE A C   1 
ATOM   555   O O   . ILE A 1 73  ? 24.477  58.692  23.573  1.00 94.21  ? 80  ILE A O   1 
ATOM   556   C CB  . ILE A 1 73  ? 24.453  61.240  21.105  1.00 101.37 ? 80  ILE A CB  1 
ATOM   557   C CG1 . ILE A 1 73  ? 24.651  62.649  21.674  1.00 106.87 ? 80  ILE A CG1 1 
ATOM   558   C CG2 . ILE A 1 73  ? 22.964  60.949  21.168  1.00 97.99  ? 80  ILE A CG2 1 
ATOM   559   C CD1 . ILE A 1 73  ? 26.069  63.160  21.608  1.00 104.80 ? 80  ILE A CD1 1 
ATOM   560   N N   . ARG A 1 74  ? 24.531  60.876  24.089  1.00 87.99  ? 81  ARG A N   1 
ATOM   561   C CA  . ARG A 1 74  ? 23.967  60.681  25.420  1.00 76.80  ? 81  ARG A CA  1 
ATOM   562   C C   . ARG A 1 74  ? 22.460  60.508  25.293  1.00 78.96  ? 81  ARG A C   1 
ATOM   563   O O   . ARG A 1 74  ? 21.735  61.482  25.059  1.00 80.20  ? 81  ARG A O   1 
ATOM   564   C CB  . ARG A 1 74  ? 24.301  61.862  26.326  1.00 69.51  ? 81  ARG A CB  1 
ATOM   565   C CG  . ARG A 1 74  ? 25.706  61.838  26.883  1.00 71.50  ? 81  ARG A CG  1 
ATOM   566   C CD  . ARG A 1 74  ? 26.076  63.178  27.484  1.00 77.21  ? 81  ARG A CD  1 
ATOM   567   N NE  . ARG A 1 74  ? 27.505  63.261  27.754  1.00 100.92 ? 81  ARG A NE  1 
ATOM   568   C CZ  . ARG A 1 74  ? 28.079  62.857  28.879  1.00 104.16 ? 81  ARG A CZ  1 
ATOM   569   N NH1 . ARG A 1 74  ? 27.370  62.340  29.869  1.00 88.38  ? 81  ARG A NH1 1 
ATOM   570   N NH2 . ARG A 1 74  ? 29.397  62.974  29.013  1.00 100.94 ? 81  ARG A NH2 1 
ATOM   571   N N   . VAL A 1 75  ? 21.989  59.272  25.432  1.00 73.66  ? 82  VAL A N   1 
ATOM   572   C CA  . VAL A 1 75  ? 20.568  58.980  25.581  1.00 54.47  ? 82  VAL A CA  1 
ATOM   573   C C   . VAL A 1 75  ? 20.312  58.725  27.063  1.00 53.78  ? 82  VAL A C   1 
ATOM   574   O O   . VAL A 1 75  ? 20.753  57.692  27.591  1.00 49.81  ? 82  VAL A O   1 
ATOM   575   C CB  . VAL A 1 75  ? 20.137  57.791  24.710  1.00 53.79  ? 82  VAL A CB  1 
ATOM   576   C CG1 . VAL A 1 75  ? 21.112  56.630  24.839  1.00 65.97  ? 82  VAL A CG1 1 
ATOM   577   C CG2 . VAL A 1 75  ? 18.713  57.359  25.056  1.00 47.14  ? 82  VAL A CG2 1 
ATOM   578   N N   . PRO A 1 76  ? 19.643  59.632  27.772  1.00 51.88  ? 83  PRO A N   1 
ATOM   579   C CA  . PRO A 1 76  ? 19.464  59.478  29.220  1.00 49.03  ? 83  PRO A CA  1 
ATOM   580   C C   . PRO A 1 76  ? 18.293  58.600  29.640  1.00 56.59  ? 83  PRO A C   1 
ATOM   581   O O   . PRO A 1 76  ? 18.120  58.376  30.844  1.00 55.93  ? 83  PRO A O   1 
ATOM   582   C CB  . PRO A 1 76  ? 19.236  60.929  29.674  1.00 46.10  ? 83  PRO A CB  1 
ATOM   583   C CG  . PRO A 1 76  ? 18.567  61.585  28.509  1.00 45.28  ? 83  PRO A CG  1 
ATOM   584   C CD  . PRO A 1 76  ? 19.080  60.899  27.263  1.00 53.20  ? 83  PRO A CD  1 
ATOM   585   N N   . GLU A 1 77  A 17.500  58.087  28.703  1.00 47.02  ? 83  GLU A N   1 
ATOM   586   C CA  . GLU A 1 77  A 16.303  57.336  29.052  1.00 54.34  ? 83  GLU A CA  1 
ATOM   587   C C   . GLU A 1 77  A 15.867  56.516  27.848  1.00 54.87  ? 83  GLU A C   1 
ATOM   588   O O   . GLU A 1 77  A 15.907  57.006  26.716  1.00 55.54  ? 83  GLU A O   1 
ATOM   589   C CB  . GLU A 1 77  A 15.178  58.287  29.497  1.00 51.22  ? 83  GLU A CB  1 
ATOM   590   C CG  . GLU A 1 77  A 13.784  57.681  29.516  1.00 76.07  ? 83  GLU A CG  1 
ATOM   591   C CD  . GLU A 1 77  A 12.689  58.737  29.493  1.00 82.93  ? 83  GLU A CD  1 
ATOM   592   O OE1 . GLU A 1 77  A 12.909  59.815  28.899  1.00 68.94  ? 83  GLU A OE1 1 
ATOM   593   O OE2 . GLU A 1 77  A 11.608  58.488  30.072  1.00 76.87  ? 83  GLU A OE2 1 
ATOM   594   N N   . TRP A 1 78  ? 15.452  55.274  28.093  1.00 44.84  ? 84  TRP A N   1 
ATOM   595   C CA  . TRP A 1 78  ? 14.897  54.454  27.024  1.00 48.85  ? 84  TRP A CA  1 
ATOM   596   C C   . TRP A 1 78  ? 13.873  53.479  27.594  1.00 57.50  ? 84  TRP A C   1 
ATOM   597   O O   . TRP A 1 78  ? 13.882  53.156  28.785  1.00 53.89  ? 84  TRP A O   1 
ATOM   598   C CB  . TRP A 1 78  ? 15.988  53.701  26.252  1.00 41.27  ? 84  TRP A CB  1 
ATOM   599   C CG  . TRP A 1 78  ? 16.863  52.839  27.107  1.00 58.57  ? 84  TRP A CG  1 
ATOM   600   C CD1 . TRP A 1 78  ? 16.634  51.546  27.470  1.00 57.50  ? 84  TRP A CD1 1 
ATOM   601   C CD2 . TRP A 1 78  ? 18.115  53.208  27.704  1.00 60.38  ? 84  TRP A CD2 1 
ATOM   602   N NE1 . TRP A 1 78  ? 17.662  51.084  28.258  1.00 50.30  ? 84  TRP A NE1 1 
ATOM   603   C CE2 . TRP A 1 78  ? 18.584  52.085  28.417  1.00 58.81  ? 84  TRP A CE2 1 
ATOM   604   C CE3 . TRP A 1 78  ? 18.883  54.379  27.708  1.00 49.08  ? 84  TRP A CE3 1 
ATOM   605   C CZ2 . TRP A 1 78  ? 19.787  52.097  29.123  1.00 49.93  ? 84  TRP A CZ2 1 
ATOM   606   C CZ3 . TRP A 1 78  ? 20.072  54.389  28.414  1.00 48.91  ? 84  TRP A CZ3 1 
ATOM   607   C CH2 . TRP A 1 78  ? 20.512  53.255  29.111  1.00 43.23  ? 84  TRP A CH2 1 
ATOM   608   N N   . SER A 1 79  ? 12.978  53.019  26.715  1.00 42.37  ? 85  SER A N   1 
ATOM   609   C CA  . SER A 1 79  ? 11.935  52.075  27.099  1.00 48.28  ? 85  SER A CA  1 
ATOM   610   C C   . SER A 1 79  ? 12.321  50.629  26.825  1.00 51.46  ? 85  SER A C   1 
ATOM   611   O O   . SER A 1 79  ? 11.873  49.730  27.546  1.00 55.96  ? 85  SER A O   1 
ATOM   612   C CB  . SER A 1 79  ? 10.629  52.401  26.366  1.00 58.26  ? 85  SER A CB  1 
ATOM   613   O OG  . SER A 1 79  ? 10.840  52.500  24.968  1.00 50.34  ? 85  SER A OG  1 
ATOM   614   N N   . TYR A 1 80  ? 13.126  50.382  25.796  1.00 51.82  ? 86  TYR A N   1 
ATOM   615   C CA  . TYR A 1 80  ? 13.625  49.045  25.504  1.00 55.89  ? 86  TYR A CA  1 
ATOM   616   C C   . TYR A 1 80  ? 14.870  49.180  24.641  1.00 57.55  ? 86  TYR A C   1 
ATOM   617   O O   . TYR A 1 80  ? 15.171  50.254  24.116  1.00 53.62  ? 86  TYR A O   1 
ATOM   618   C CB  . TYR A 1 80  ? 12.563  48.177  24.819  1.00 34.21  ? 86  TYR A CB  1 
ATOM   619   C CG  . TYR A 1 80  ? 12.108  48.678  23.469  1.00 46.77  ? 86  TYR A CG  1 
ATOM   620   C CD1 . TYR A 1 80  ? 11.225  49.750  23.363  1.00 39.23  ? 86  TYR A CD1 1 
ATOM   621   C CD2 . TYR A 1 80  ? 12.542  48.069  22.300  1.00 42.56  ? 86  TYR A CD2 1 
ATOM   622   C CE1 . TYR A 1 80  ? 10.803  50.207  22.136  1.00 35.13  ? 86  TYR A CE1 1 
ATOM   623   C CE2 . TYR A 1 80  ? 12.116  48.518  21.062  1.00 44.96  ? 86  TYR A CE2 1 
ATOM   624   C CZ  . TYR A 1 80  ? 11.248  49.590  20.986  1.00 42.46  ? 86  TYR A CZ  1 
ATOM   625   O OH  . TYR A 1 80  ? 10.827  50.050  19.755  1.00 49.81  ? 86  TYR A OH  1 
ATOM   626   N N   . ILE A 1 81  ? 15.596  48.072  24.504  1.00 50.24  ? 87  ILE A N   1 
ATOM   627   C CA  . ILE A 1 81  ? 16.864  48.035  23.783  1.00 44.47  ? 87  ILE A CA  1 
ATOM   628   C C   . ILE A 1 81  ? 16.684  47.216  22.514  1.00 42.82  ? 87  ILE A C   1 
ATOM   629   O O   . ILE A 1 81  ? 16.135  46.108  22.558  1.00 56.16  ? 87  ILE A O   1 
ATOM   630   C CB  . ILE A 1 81  ? 17.988  47.443  24.650  1.00 45.63  ? 87  ILE A CB  1 
ATOM   631   C CG1 . ILE A 1 81  ? 18.461  48.457  25.692  1.00 46.88  ? 87  ILE A CG1 1 
ATOM   632   C CG2 . ILE A 1 81  ? 19.140  46.984  23.775  1.00 49.81  ? 87  ILE A CG2 1 
ATOM   633   C CD1 . ILE A 1 81  ? 19.341  47.846  26.768  1.00 41.88  ? 87  ILE A CD1 1 
ATOM   634   N N   . VAL A 1 82  ? 17.159  47.748  21.391  1.00 51.36  ? 88  VAL A N   1 
ATOM   635   C CA  . VAL A 1 82  ? 17.162  47.029  20.122  1.00 44.05  ? 88  VAL A CA  1 
ATOM   636   C C   . VAL A 1 82  ? 18.595  46.651  19.779  1.00 51.15  ? 88  VAL A C   1 
ATOM   637   O O   . VAL A 1 82  ? 19.456  47.525  19.618  1.00 53.49  ? 88  VAL A O   1 
ATOM   638   C CB  . VAL A 1 82  ? 16.542  47.855  18.990  1.00 48.44  ? 88  VAL A CB  1 
ATOM   639   C CG1 . VAL A 1 82  ? 16.619  47.067  17.685  1.00 39.88  ? 88  VAL A CG1 1 
ATOM   640   C CG2 . VAL A 1 82  ? 15.104  48.225  19.331  1.00 47.24  ? 88  VAL A CG2 1 
ATOM   641   N N   . GLU A 1 83  ? 18.841  45.352  19.654  1.00 51.60  ? 89  GLU A N   1 
ATOM   642   C CA  . GLU A 1 83  ? 20.097  44.816  19.155  1.00 53.23  ? 89  GLU A CA  1 
ATOM   643   C C   . GLU A 1 83  ? 19.863  44.164  17.801  1.00 51.99  ? 89  GLU A C   1 
ATOM   644   O O   . GLU A 1 83  ? 18.773  43.659  17.517  1.00 62.63  ? 89  GLU A O   1 
ATOM   645   C CB  . GLU A 1 83  ? 20.683  43.776  20.114  1.00 48.83  ? 89  GLU A CB  1 
ATOM   646   C CG  . GLU A 1 83  ? 21.626  44.303  21.170  1.00 45.41  ? 89  GLU A CG  1 
ATOM   647   C CD  . GLU A 1 83  ? 22.279  43.171  21.953  1.00 63.94  ? 89  GLU A CD  1 
ATOM   648   O OE1 . GLU A 1 83  ? 21.725  42.048  21.937  1.00 61.06  ? 89  GLU A OE1 1 
ATOM   649   O OE2 . GLU A 1 83  ? 23.341  43.394  22.576  1.00 61.47  ? 89  GLU A OE2 1 
ATOM   650   N N   . ARG A 1 84  ? 20.892  44.174  16.962  1.00 55.78  ? 90  ARG A N   1 
ATOM   651   C CA  . ARG A 1 84  ? 20.828  43.351  15.768  1.00 64.84  ? 90  ARG A CA  1 
ATOM   652   C C   . ARG A 1 84  ? 20.978  41.882  16.150  1.00 64.24  ? 90  ARG A C   1 
ATOM   653   O O   . ARG A 1 84  ? 21.440  41.540  17.242  1.00 62.76  ? 90  ARG A O   1 
ATOM   654   C CB  . ARG A 1 84  ? 21.907  43.760  14.767  1.00 65.92  ? 90  ARG A CB  1 
ATOM   655   C CG  . ARG A 1 84  ? 21.966  45.249  14.524  1.00 68.55  ? 90  ARG A CG  1 
ATOM   656   C CD  . ARG A 1 84  ? 21.881  45.586  13.046  1.00 79.39  ? 90  ARG A CD  1 
ATOM   657   N NE  . ARG A 1 84  ? 22.563  46.836  12.727  1.00 93.91  ? 90  ARG A NE  1 
ATOM   658   C CZ  . ARG A 1 84  ? 23.769  46.918  12.180  1.00 92.07  ? 90  ARG A CZ  1 
ATOM   659   N NH1 . ARG A 1 84  ? 24.464  45.836  11.873  1.00 98.01  ? 90  ARG A NH1 1 
ATOM   660   N NH2 . ARG A 1 84  ? 24.293  48.118  11.942  1.00 81.33  ? 90  ARG A NH2 1 
ATOM   661   N N   . THR A 1 85  ? 20.569  41.007  15.232  1.00 69.94  ? 91  THR A N   1 
ATOM   662   C CA  . THR A 1 85  ? 20.601  39.576  15.519  1.00 67.13  ? 91  THR A CA  1 
ATOM   663   C C   . THR A 1 85  ? 22.019  39.095  15.798  1.00 71.74  ? 91  THR A C   1 
ATOM   664   O O   . THR A 1 85  ? 22.251  38.354  16.761  1.00 75.80  ? 91  THR A O   1 
ATOM   665   C CB  . THR A 1 85  ? 19.989  38.800  14.357  1.00 66.42  ? 91  THR A CB  1 
ATOM   666   O OG1 . THR A 1 85  ? 18.677  39.310  14.085  1.00 70.90  ? 91  THR A OG1 1 
ATOM   667   C CG2 . THR A 1 85  ? 19.900  37.322  14.697  1.00 75.69  ? 91  THR A CG2 1 
ATOM   668   N N   . ASN A 1 86  ? 22.983  39.513  14.983  1.00 69.15  ? 92  ASN A N   1 
ATOM   669   C CA  . ASN A 1 86  ? 24.388  39.146  15.161  1.00 80.45  ? 92  ASN A CA  1 
ATOM   670   C C   . ASN A 1 86  ? 25.219  40.422  15.147  1.00 75.20  ? 92  ASN A C   1 
ATOM   671   O O   . ASN A 1 86  ? 25.740  40.823  14.098  1.00 77.91  ? 92  ASN A O   1 
ATOM   672   C CB  . ASN A 1 86  ? 24.853  38.168  14.081  1.00 88.32  ? 92  ASN A CB  1 
ATOM   673   C CG  . ASN A 1 86  ? 24.562  36.722  14.438  1.00 93.46  ? 92  ASN A CG  1 
ATOM   674   O OD1 . ASN A 1 86  ? 23.511  36.410  14.998  1.00 95.24  ? 92  ASN A OD1 1 
ATOM   675   N ND2 . ASN A 1 86  ? 25.495  35.832  14.117  1.00 99.23  ? 92  ASN A ND2 1 
ATOM   676   N N   . PRO A 1 87  ? 25.354  41.091  16.293  1.00 68.89  ? 93  PRO A N   1 
ATOM   677   C CA  . PRO A 1 87  ? 26.096  42.358  16.322  1.00 70.29  ? 93  PRO A CA  1 
ATOM   678   C C   . PRO A 1 87  ? 27.547  42.160  15.910  1.00 73.65  ? 93  PRO A C   1 
ATOM   679   O O   . PRO A 1 87  ? 28.171  41.144  16.226  1.00 83.64  ? 93  PRO A O   1 
ATOM   680   C CB  . PRO A 1 87  ? 25.980  42.808  17.783  1.00 62.37  ? 93  PRO A CB  1 
ATOM   681   C CG  . PRO A 1 87  ? 24.839  42.025  18.347  1.00 56.42  ? 93  PRO A CG  1 
ATOM   682   C CD  . PRO A 1 87  ? 24.850  40.717  17.623  1.00 71.51  ? 93  PRO A CD  1 
ATOM   683   N N   . ALA A 1 88  ? 28.080  43.147  15.189  1.00 75.86  ? 94  ALA A N   1 
ATOM   684   C CA  . ALA A 1 88  ? 29.451  43.055  14.701  1.00 77.22  ? 94  ALA A CA  1 
ATOM   685   C C   . ALA A 1 88  ? 30.468  43.433  15.768  1.00 72.43  ? 94  ALA A C   1 
ATOM   686   O O   . ALA A 1 88  ? 31.606  42.952  15.729  1.00 71.34  ? 94  ALA A O   1 
ATOM   687   C CB  . ALA A 1 88  ? 29.635  43.943  13.469  1.00 65.53  ? 94  ALA A CB  1 
ATOM   688   N N   . ASN A 1 89  ? 30.089  44.283  16.718  1.00 74.76  ? 95  ASN A N   1 
ATOM   689   C CA  . ASN A 1 89  ? 31.014  44.801  17.716  1.00 67.64  ? 95  ASN A CA  1 
ATOM   690   C C   . ASN A 1 89  ? 30.552  44.403  19.111  1.00 76.24  ? 95  ASN A C   1 
ATOM   691   O O   . ASN A 1 89  ? 29.410  44.669  19.498  1.00 75.19  ? 95  ASN A O   1 
ATOM   692   C CB  . ASN A 1 89  ? 31.144  46.321  17.605  1.00 76.71  ? 95  ASN A CB  1 
ATOM   693   C CG  . ASN A 1 89  ? 31.887  46.751  16.353  1.00 81.97  ? 95  ASN A CG  1 
ATOM   694   O OD1 . ASN A 1 89  ? 32.689  45.994  15.801  1.00 75.87  ? 95  ASN A OD1 1 
ATOM   695   N ND2 . ASN A 1 89  ? 31.623  47.971  15.898  1.00 85.98  ? 95  ASN A ND2 1 
ATOM   696   N N   . ASP A 1 90  ? 31.456  43.782  19.855  1.00 67.48  ? 96  ASP A N   1 
ATOM   697   C CA  . ASP A 1 90  ? 31.273  43.344  21.233  1.00 58.68  ? 96  ASP A CA  1 
ATOM   698   C C   . ASP A 1 90  ? 32.644  43.470  21.887  1.00 68.64  ? 96  ASP A C   1 
ATOM   699   O O   . ASP A 1 90  ? 33.460  44.295  21.461  1.00 86.54  ? 96  ASP A O   1 
ATOM   700   C CB  . ASP A 1 90  ? 30.661  41.932  21.291  1.00 58.18  ? 96  ASP A CB  1 
ATOM   701   C CG  . ASP A 1 90  ? 31.638  40.850  20.882  1.00 88.02  ? 96  ASP A CG  1 
ATOM   702   O OD1 . ASP A 1 90  ? 31.926  40.739  19.672  1.00 103.45 ? 96  ASP A OD1 1 
ATOM   703   O OD2 . ASP A 1 90  ? 32.113  40.109  21.769  1.00 77.71  ? 96  ASP A OD2 1 
ATOM   704   N N   . LEU A 1 91  A 32.883  42.717  22.962  1.00 68.31  ? 96  LEU A N   1 
ATOM   705   C CA  . LEU A 1 91  A 34.226  42.695  23.529  1.00 69.39  ? 96  LEU A CA  1 
ATOM   706   C C   . LEU A 1 91  A 35.258  42.482  22.427  1.00 59.62  ? 96  LEU A C   1 
ATOM   707   O O   . LEU A 1 91  A 35.357  41.391  21.856  1.00 68.32  ? 96  LEU A O   1 
ATOM   708   C CB  . LEU A 1 91  A 34.356  41.591  24.580  1.00 63.70  ? 96  LEU A CB  1 
ATOM   709   C CG  . LEU A 1 91  A 33.123  41.241  25.409  1.00 55.14  ? 96  LEU A CG  1 
ATOM   710   C CD1 . LEU A 1 91  A 33.381  39.990  26.239  1.00 56.45  ? 96  LEU A CD1 1 
ATOM   711   C CD2 . LEU A 1 91  A 32.757  42.404  26.300  1.00 57.03  ? 96  LEU A CD2 1 
ATOM   712   N N   . CYS A 1 92  ? 36.037  43.525  22.138  1.00 51.99  ? 97  CYS A N   1 
ATOM   713   C CA  . CYS A 1 92  ? 37.065  43.452  21.106  1.00 51.45  ? 97  CYS A CA  1 
ATOM   714   C C   . CYS A 1 92  ? 38.291  42.695  21.600  1.00 46.26  ? 97  CYS A C   1 
ATOM   715   O O   . CYS A 1 92  ? 38.902  41.930  20.844  1.00 45.06  ? 97  CYS A O   1 
ATOM   716   C CB  . CYS A 1 92  ? 37.426  44.864  20.646  1.00 40.14  ? 97  CYS A CB  1 
ATOM   717   S SG  . CYS A 1 92  ? 37.890  45.970  22.008  1.00 70.96  ? 97  CYS A SG  1 
ATOM   718   N N   . TYR A 1 93  ? 38.665  42.899  22.852  1.00 38.58  ? 98  TYR A N   1 
ATOM   719   C CA  . TYR A 1 93  ? 39.546  41.962  23.524  1.00 53.76  ? 98  TYR A CA  1 
ATOM   720   C C   . TYR A 1 93  ? 38.716  40.761  23.955  1.00 51.76  ? 98  TYR A C   1 
ATOM   721   O O   . TYR A 1 93  ? 37.724  40.937  24.671  1.00 47.75  ? 98  TYR A O   1 
ATOM   722   C CB  . TYR A 1 93  ? 40.210  42.612  24.729  1.00 52.55  ? 98  TYR A CB  1 
ATOM   723   C CG  . TYR A 1 93  ? 41.530  41.988  25.115  1.00 59.35  ? 98  TYR A CG  1 
ATOM   724   C CD1 . TYR A 1 93  ? 41.590  40.697  25.629  1.00 56.87  ? 98  TYR A CD1 1 
ATOM   725   C CD2 . TYR A 1 93  ? 42.718  42.690  24.972  1.00 53.08  ? 98  TYR A CD2 1 
ATOM   726   C CE1 . TYR A 1 93  ? 42.802  40.123  25.986  1.00 52.49  ? 98  TYR A CE1 1 
ATOM   727   C CE2 . TYR A 1 93  ? 43.931  42.127  25.330  1.00 58.46  ? 98  TYR A CE2 1 
ATOM   728   C CZ  . TYR A 1 93  ? 43.968  40.843  25.833  1.00 58.57  ? 98  TYR A CZ  1 
ATOM   729   O OH  . TYR A 1 93  ? 45.176  40.285  26.186  1.00 61.60  ? 98  TYR A OH  1 
ATOM   730   N N   . PRO A 1 94  ? 39.062  39.545  23.536  1.00 49.71  ? 99  PRO A N   1 
ATOM   731   C CA  . PRO A 1 94  ? 38.210  38.392  23.850  1.00 42.24  ? 99  PRO A CA  1 
ATOM   732   C C   . PRO A 1 94  ? 38.124  38.147  25.350  1.00 51.90  ? 99  PRO A C   1 
ATOM   733   O O   . PRO A 1 94  ? 39.029  38.487  26.115  1.00 51.37  ? 99  PRO A O   1 
ATOM   734   C CB  . PRO A 1 94  ? 38.897  37.226  23.124  1.00 50.75  ? 99  PRO A CB  1 
ATOM   735   C CG  . PRO A 1 94  ? 40.293  37.688  22.865  1.00 56.51  ? 99  PRO A CG  1 
ATOM   736   C CD  . PRO A 1 94  ? 40.223  39.177  22.709  1.00 54.87  ? 99  PRO A CD  1 
ATOM   737   N N   . GLY A 1 95  ? 37.004  37.573  25.765  1.00 48.71  ? 100 GLY A N   1 
ATOM   738   C CA  . GLY A 1 95  ? 36.762  37.284  27.171  1.00 47.65  ? 100 GLY A CA  1 
ATOM   739   C C   . GLY A 1 95  ? 35.279  37.060  27.412  1.00 56.46  ? 100 GLY A C   1 
ATOM   740   O O   . GLY A 1 95  ? 34.565  36.563  26.540  1.00 50.85  ? 100 GLY A O   1 
ATOM   741   N N   . ASN A 1 96  ? 34.841  37.435  28.611  1.00 56.97  ? 101 ASN A N   1 
ATOM   742   C CA  . ASN A 1 96  ? 33.442  37.315  28.993  1.00 52.85  ? 101 ASN A CA  1 
ATOM   743   C C   . ASN A 1 96  ? 33.052  38.500  29.861  1.00 57.18  ? 101 ASN A C   1 
ATOM   744   O O   . ASN A 1 96  ? 33.895  39.141  30.497  1.00 55.10  ? 101 ASN A O   1 
ATOM   745   C CB  . ASN A 1 96  ? 33.154  36.014  29.762  1.00 46.35  ? 101 ASN A CB  1 
ATOM   746   C CG  . ASN A 1 96  ? 33.653  34.778  29.035  1.00 69.93  ? 101 ASN A CG  1 
ATOM   747   O OD1 . ASN A 1 96  ? 32.955  34.211  28.190  1.00 76.61  ? 101 ASN A OD1 1 
ATOM   748   N ND2 . ASN A 1 96  ? 34.866  34.350  29.366  1.00 59.31  ? 101 ASN A ND2 1 
ATOM   749   N N   . LEU A 1 97  ? 31.755  38.779  29.882  1.00 47.78  ? 102 LEU A N   1 
ATOM   750   C CA  . LEU A 1 97  ? 31.152  39.686  30.846  1.00 39.21  ? 102 LEU A CA  1 
ATOM   751   C C   . LEU A 1 97  ? 30.283  38.849  31.782  1.00 47.75  ? 102 LEU A C   1 
ATOM   752   O O   . LEU A 1 97  ? 29.422  38.091  31.323  1.00 44.75  ? 102 LEU A O   1 
ATOM   753   C CB  . LEU A 1 97  ? 30.335  40.768  30.138  1.00 33.37  ? 102 LEU A CB  1 
ATOM   754   C CG  . LEU A 1 97  ? 29.649  41.816  31.019  1.00 44.34  ? 102 LEU A CG  1 
ATOM   755   C CD1 . LEU A 1 97  ? 30.579  42.311  32.106  1.00 47.84  ? 102 LEU A CD1 1 
ATOM   756   C CD2 . LEU A 1 97  ? 29.119  42.981  30.190  1.00 45.11  ? 102 LEU A CD2 1 
ATOM   757   N N   . ASN A 1 98  ? 30.524  38.973  33.085  1.00 50.86  ? 103 ASN A N   1 
ATOM   758   C CA  . ASN A 1 98  ? 29.826  38.158  34.073  1.00 40.83  ? 103 ASN A CA  1 
ATOM   759   C C   . ASN A 1 98  ? 28.369  38.578  34.203  1.00 40.88  ? 103 ASN A C   1 
ATOM   760   O O   . ASN A 1 98  ? 28.048  39.770  34.175  1.00 44.95  ? 103 ASN A O   1 
ATOM   761   C CB  . ASN A 1 98  ? 30.514  38.277  35.429  1.00 44.67  ? 103 ASN A CB  1 
ATOM   762   C CG  . ASN A 1 98  ? 30.243  37.092  36.329  1.00 41.61  ? 103 ASN A CG  1 
ATOM   763   O OD1 . ASN A 1 98  ? 29.512  37.198  37.314  1.00 47.66  ? 103 ASN A OD1 1 
ATOM   764   N ND2 . ASN A 1 98  ? 30.841  35.955  36.000  1.00 48.93  ? 103 ASN A ND2 1 
ATOM   765   N N   . ASP A 1 99  ? 27.488  37.587  34.367  1.00 46.25  ? 104 ASP A N   1 
ATOM   766   C CA  . ASP A 1 99  ? 26.045  37.813  34.512  1.00 44.32  ? 104 ASP A CA  1 
ATOM   767   C C   . ASP A 1 99  ? 25.522  38.709  33.396  1.00 42.72  ? 104 ASP A C   1 
ATOM   768   O O   . ASP A 1 99  ? 24.745  39.639  33.626  1.00 38.41  ? 104 ASP A O   1 
ATOM   769   C CB  . ASP A 1 99  ? 25.709  38.401  35.882  1.00 57.98  ? 104 ASP A CB  1 
ATOM   770   C CG  . ASP A 1 99  ? 25.945  37.421  37.011  1.00 55.86  ? 104 ASP A CG  1 
ATOM   771   O OD1 . ASP A 1 99  ? 25.647  36.221  36.828  1.00 60.95  ? 104 ASP A OD1 1 
ATOM   772   O OD2 . ASP A 1 99  ? 26.433  37.852  38.079  1.00 59.35  ? 104 ASP A OD2 1 
ATOM   773   N N   . TYR A 1 100 ? 25.968  38.424  32.172  1.00 43.13  ? 105 TYR A N   1 
ATOM   774   C CA  . TYR A 1 100 ? 25.675  39.302  31.044  1.00 47.54  ? 105 TYR A CA  1 
ATOM   775   C C   . TYR A 1 100 ? 24.173  39.431  30.816  1.00 42.02  ? 105 TYR A C   1 
ATOM   776   O O   . TYR A 1 100 ? 23.654  40.539  30.642  1.00 45.38  ? 105 TYR A O   1 
ATOM   777   C CB  . TYR A 1 100 ? 26.371  38.771  29.789  1.00 33.13  ? 105 TYR A CB  1 
ATOM   778   C CG  . TYR A 1 100 ? 26.302  39.697  28.596  1.00 45.57  ? 105 TYR A CG  1 
ATOM   779   C CD1 . TYR A 1 100 ? 26.260  41.077  28.762  1.00 41.89  ? 105 TYR A CD1 1 
ATOM   780   C CD2 . TYR A 1 100 ? 26.285  39.191  27.302  1.00 39.20  ? 105 TYR A CD2 1 
ATOM   781   C CE1 . TYR A 1 100 ? 26.202  41.925  27.671  1.00 41.98  ? 105 TYR A CE1 1 
ATOM   782   C CE2 . TYR A 1 100 ? 26.228  40.031  26.207  1.00 49.47  ? 105 TYR A CE2 1 
ATOM   783   C CZ  . TYR A 1 100 ? 26.188  41.398  26.397  1.00 50.22  ? 105 TYR A CZ  1 
ATOM   784   O OH  . TYR A 1 100 ? 26.132  42.236  25.308  1.00 48.77  ? 105 TYR A OH  1 
ATOM   785   N N   . GLU A 1 101 ? 23.455  38.306  30.836  1.00 40.00  ? 106 GLU A N   1 
ATOM   786   C CA  . GLU A 1 101 ? 22.029  38.329  30.526  1.00 39.84  ? 106 GLU A CA  1 
ATOM   787   C C   . GLU A 1 101 ? 21.233  39.034  31.617  1.00 38.59  ? 106 GLU A C   1 
ATOM   788   O O   . GLU A 1 101 ? 20.261  39.741  31.324  1.00 38.82  ? 106 GLU A O   1 
ATOM   789   C CB  . GLU A 1 101 ? 21.516  36.907  30.314  1.00 35.40  ? 106 GLU A CB  1 
ATOM   790   C CG  . GLU A 1 101 ? 22.131  36.197  29.113  1.00 40.95  ? 106 GLU A CG  1 
ATOM   791   C CD  . GLU A 1 101 ? 23.529  35.658  29.396  1.00 57.70  ? 106 GLU A CD  1 
ATOM   792   O OE1 . GLU A 1 101 ? 23.870  35.469  30.586  1.00 51.13  ? 106 GLU A OE1 1 
ATOM   793   O OE2 . GLU A 1 101 ? 24.284  35.423  28.426  1.00 59.81  ? 106 GLU A OE2 1 
ATOM   794   N N   . GLU A 1 102 ? 21.626  38.852  32.879  1.00 43.85  ? 107 GLU A N   1 
ATOM   795   C CA  . GLU A 1 102 ? 20.991  39.594  33.964  1.00 40.95  ? 107 GLU A CA  1 
ATOM   796   C C   . GLU A 1 102 ? 21.262  41.088  33.841  1.00 43.95  ? 107 GLU A C   1 
ATOM   797   O O   . GLU A 1 102 ? 20.372  41.909  34.090  1.00 48.99  ? 107 GLU A O   1 
ATOM   798   C CB  . GLU A 1 102 ? 21.473  39.070  35.316  1.00 37.83  ? 107 GLU A CB  1 
ATOM   799   C CG  . GLU A 1 102 ? 20.762  37.802  35.772  1.00 45.27  ? 107 GLU A CG  1 
ATOM   800   C CD  . GLU A 1 102 ? 19.255  37.993  35.937  1.00 58.68  ? 107 GLU A CD  1 
ATOM   801   O OE1 . GLU A 1 102 ? 18.834  38.989  36.572  1.00 50.94  ? 107 GLU A OE1 1 
ATOM   802   O OE2 . GLU A 1 102 ? 18.490  37.146  35.423  1.00 43.33  ? 107 GLU A OE2 1 
ATOM   803   N N   . LEU A 1 103 ? 22.489  41.459  33.465  1.00 48.96  ? 108 LEU A N   1 
ATOM   804   C CA  . LEU A 1 103 ? 22.800  42.867  33.247  1.00 40.92  ? 108 LEU A CA  1 
ATOM   805   C C   . LEU A 1 103 ? 21.985  43.440  32.096  1.00 47.58  ? 108 LEU A C   1 
ATOM   806   O O   . LEU A 1 103 ? 21.483  44.568  32.179  1.00 43.15  ? 108 LEU A O   1 
ATOM   807   C CB  . LEU A 1 103 ? 24.296  43.036  32.985  1.00 46.86  ? 108 LEU A CB  1 
ATOM   808   C CG  . LEU A 1 103 ? 24.842  44.459  32.845  1.00 43.47  ? 108 LEU A CG  1 
ATOM   809   C CD1 . LEU A 1 103 ? 24.346  45.341  33.980  1.00 40.27  ? 108 LEU A CD1 1 
ATOM   810   C CD2 . LEU A 1 103 ? 26.366  44.425  32.810  1.00 46.88  ? 108 LEU A CD2 1 
ATOM   811   N N   . LYS A 1 104 ? 21.842  42.673  31.011  1.00 46.63  ? 109 LYS A N   1 
ATOM   812   C CA  . LYS A 1 104 ? 21.054  43.130  29.872  1.00 38.60  ? 109 LYS A CA  1 
ATOM   813   C C   . LYS A 1 104 ? 19.596  43.322  30.259  1.00 47.05  ? 109 LYS A C   1 
ATOM   814   O O   . LYS A 1 104 ? 18.938  44.261  29.794  1.00 46.83  ? 109 LYS A O   1 
ATOM   815   C CB  . LYS A 1 104 ? 21.175  42.137  28.716  1.00 44.51  ? 109 LYS A CB  1 
ATOM   816   C CG  . LYS A 1 104 ? 22.432  42.300  27.875  1.00 46.52  ? 109 LYS A CG  1 
ATOM   817   C CD  . LYS A 1 104 ? 22.289  41.626  26.515  1.00 41.07  ? 109 LYS A CD  1 
ATOM   818   C CE  . LYS A 1 104 ? 22.570  40.142  26.608  1.00 34.91  ? 109 LYS A CE  1 
ATOM   819   N NZ  . LYS A 1 104 ? 22.522  39.503  25.265  1.00 52.84  ? 109 LYS A NZ  1 
ATOM   820   N N   . HIS A 1 105 ? 19.066  42.429  31.094  1.00 45.27  ? 110 HIS A N   1 
ATOM   821   C CA  . HIS A 1 105 ? 17.692  42.587  31.554  1.00 54.76  ? 110 HIS A CA  1 
ATOM   822   C C   . HIS A 1 105 ? 17.555  43.815  32.446  1.00 50.79  ? 110 HIS A C   1 
ATOM   823   O O   . HIS A 1 105 ? 16.562  44.547  32.357  1.00 45.51  ? 110 HIS A O   1 
ATOM   824   C CB  . HIS A 1 105 ? 17.239  41.322  32.285  1.00 43.61  ? 110 HIS A CB  1 
ATOM   825   C CG  . HIS A 1 105 ? 15.789  41.320  32.646  1.00 40.20  ? 110 HIS A CG  1 
ATOM   826   N ND1 . HIS A 1 105 ? 14.786  41.316  31.701  1.00 50.71  ? 110 HIS A ND1 1 
ATOM   827   C CD2 . HIS A 1 105 ? 15.171  41.322  33.851  1.00 39.85  ? 110 HIS A CD2 1 
ATOM   828   C CE1 . HIS A 1 105 ? 13.613  41.317  32.308  1.00 44.99  ? 110 HIS A CE1 1 
ATOM   829   N NE2 . HIS A 1 105 ? 13.819  41.323  33.613  1.00 47.03  ? 110 HIS A NE2 1 
ATOM   830   N N   . LEU A 1 106 ? 18.555  44.064  33.297  1.00 44.95  ? 111 LEU A N   1 
ATOM   831   C CA  . LEU A 1 106 ? 18.516  45.217  34.190  1.00 44.07  ? 111 LEU A CA  1 
ATOM   832   C C   . LEU A 1 106 ? 18.516  46.527  33.407  1.00 53.54  ? 111 LEU A C   1 
ATOM   833   O O   . LEU A 1 106 ? 17.850  47.493  33.797  1.00 43.83  ? 111 LEU A O   1 
ATOM   834   C CB  . LEU A 1 106 ? 19.701  45.162  35.155  1.00 46.24  ? 111 LEU A CB  1 
ATOM   835   C CG  . LEU A 1 106 ? 19.955  46.364  36.071  1.00 54.99  ? 111 LEU A CG  1 
ATOM   836   C CD1 . LEU A 1 106 ? 18.739  46.668  36.917  1.00 57.25  ? 111 LEU A CD1 1 
ATOM   837   C CD2 . LEU A 1 106 ? 21.154  46.111  36.959  1.00 41.12  ? 111 LEU A CD2 1 
ATOM   838   N N   . LEU A 1 107 ? 19.255  46.580  32.302  1.00 43.91  ? 112 LEU A N   1 
ATOM   839   C CA  . LEU A 1 107 ? 19.344  47.787  31.493  1.00 47.80  ? 112 LEU A CA  1 
ATOM   840   C C   . LEU A 1 107 ? 18.266  47.878  30.419  1.00 56.65  ? 112 LEU A C   1 
ATOM   841   O O   . LEU A 1 107 ? 18.286  48.827  29.628  1.00 52.38  ? 112 LEU A O   1 
ATOM   842   C CB  . LEU A 1 107 ? 20.722  47.880  30.834  1.00 44.79  ? 112 LEU A CB  1 
ATOM   843   C CG  . LEU A 1 107 ? 21.912  47.952  31.788  1.00 53.87  ? 112 LEU A CG  1 
ATOM   844   C CD1 . LEU A 1 107 ? 23.156  47.466  31.086  1.00 40.97  ? 112 LEU A CD1 1 
ATOM   845   C CD2 . LEU A 1 107 ? 22.094  49.370  32.301  1.00 60.07  ? 112 LEU A CD2 1 
ATOM   846   N N   . SER A 1 108 ? 17.328  46.925  30.371  1.00 45.30  ? 113 SER A N   1 
ATOM   847   C CA  . SER A 1 108 ? 16.351  46.914  29.285  1.00 48.30  ? 113 SER A CA  1 
ATOM   848   C C   . SER A 1 108 ? 15.496  48.177  29.297  1.00 51.92  ? 113 SER A C   1 
ATOM   849   O O   . SER A 1 108 ? 15.168  48.721  28.236  1.00 48.59  ? 113 SER A O   1 
ATOM   850   C CB  . SER A 1 108 ? 15.475  45.659  29.364  1.00 52.00  ? 113 SER A CB  1 
ATOM   851   O OG  . SER A 1 108 ? 14.867  45.506  30.637  1.00 49.91  ? 113 SER A OG  1 
ATOM   852   N N   . ARG A 1 109 ? 15.126  48.661  30.483  1.00 50.42  ? 114 ARG A N   1 
ATOM   853   C CA  . ARG A 1 109 ? 14.344  49.888  30.617  1.00 57.08  ? 114 ARG A CA  1 
ATOM   854   C C   . ARG A 1 109 ? 14.942  50.716  31.743  1.00 56.37  ? 114 ARG A C   1 
ATOM   855   O O   . ARG A 1 109 ? 15.043  50.237  32.878  1.00 48.12  ? 114 ARG A O   1 
ATOM   856   C CB  . ARG A 1 109 ? 12.869  49.581  30.892  1.00 55.37  ? 114 ARG A CB  1 
ATOM   857   C CG  . ARG A 1 109 ? 11.993  50.806  31.012  1.00 50.12  ? 114 ARG A CG  1 
ATOM   858   C CD  . ARG A 1 109 ? 10.625  50.442  31.552  1.00 49.91  ? 114 ARG A CD  1 
ATOM   859   N NE  . ARG A 1 109 ? 9.583   50.573  30.542  1.00 67.34  ? 114 ARG A NE  1 
ATOM   860   C CZ  . ARG A 1 109 ? 8.308   50.273  30.744  1.00 80.46  ? 114 ARG A CZ  1 
ATOM   861   N NH1 . ARG A 1 109 ? 7.886   49.802  31.907  1.00 71.96  ? 114 ARG A NH1 1 
ATOM   862   N NH2 . ARG A 1 109 ? 7.436   50.447  29.753  1.00 82.75  ? 114 ARG A NH2 1 
ATOM   863   N N   . ILE A 1 110 ? 15.334  51.951  31.430  1.00 54.15  ? 115 ILE A N   1 
ATOM   864   C CA  . ILE A 1 110 ? 16.078  52.808  32.347  1.00 46.59  ? 115 ILE A CA  1 
ATOM   865   C C   . ILE A 1 110 ? 15.440  54.192  32.355  1.00 54.24  ? 115 ILE A C   1 
ATOM   866   O O   . ILE A 1 110 ? 15.168  54.763  31.292  1.00 54.10  ? 115 ILE A O   1 
ATOM   867   C CB  . ILE A 1 110 ? 17.567  52.891  31.955  1.00 61.01  ? 115 ILE A CB  1 
ATOM   868   C CG1 . ILE A 1 110 ? 18.237  51.529  32.142  1.00 53.12  ? 115 ILE A CG1 1 
ATOM   869   C CG2 . ILE A 1 110 ? 18.301  53.942  32.778  1.00 48.98  ? 115 ILE A CG2 1 
ATOM   870   C CD1 . ILE A 1 110 ? 18.177  51.016  33.561  1.00 52.94  ? 115 ILE A CD1 1 
ATOM   871   N N   . ASN A 1 111 ? 15.201  54.727  33.556  1.00 51.35  ? 116 ASN A N   1 
ATOM   872   C CA  . ASN A 1 111 ? 14.595  56.047  33.687  1.00 58.98  ? 116 ASN A CA  1 
ATOM   873   C C   . ASN A 1 111 ? 15.618  57.157  33.469  1.00 60.64  ? 116 ASN A C   1 
ATOM   874   O O   . ASN A 1 111 ? 15.344  58.126  32.753  1.00 60.39  ? 116 ASN A O   1 
ATOM   875   C CB  . ASN A 1 111 ? 13.931  56.190  35.059  1.00 57.26  ? 116 ASN A CB  1 
ATOM   876   C CG  . ASN A 1 111 ? 13.036  57.409  35.146  1.00 68.63  ? 116 ASN A CG  1 
ATOM   877   O OD1 . ASN A 1 111 ? 12.764  58.064  34.141  1.00 81.39  ? 116 ASN A OD1 1 
ATOM   878   N ND2 . ASN A 1 111 ? 12.579  57.726  36.352  1.00 65.49  ? 116 ASN A ND2 1 
ATOM   879   N N   . HIS A 1 112 ? 16.795  57.044  34.090  1.00 60.83  ? 117 HIS A N   1 
ATOM   880   C CA  . HIS A 1 112 ? 17.877  57.997  33.875  1.00 54.55  ? 117 HIS A CA  1 
ATOM   881   C C   . HIS A 1 112 ? 19.208  57.264  33.782  1.00 65.51  ? 117 HIS A C   1 
ATOM   882   O O   . HIS A 1 112 ? 19.495  56.367  34.582  1.00 60.11  ? 117 HIS A O   1 
ATOM   883   C CB  . HIS A 1 112 ? 17.945  59.056  34.984  1.00 58.77  ? 117 HIS A CB  1 
ATOM   884   C CG  . HIS A 1 112 ? 19.029  60.070  34.777  1.00 71.53  ? 117 HIS A CG  1 
ATOM   885   N ND1 . HIS A 1 112 ? 20.080  60.229  35.656  1.00 77.01  ? 117 HIS A ND1 1 
ATOM   886   C CD2 . HIS A 1 112 ? 19.232  60.967  33.783  1.00 60.18  ? 117 HIS A CD2 1 
ATOM   887   C CE1 . HIS A 1 112 ? 20.880  61.183  35.214  1.00 69.39  ? 117 HIS A CE1 1 
ATOM   888   N NE2 . HIS A 1 112 ? 20.388  61.647  34.079  1.00 66.39  ? 117 HIS A NE2 1 
ATOM   889   N N   . PHE A 1 113 ? 20.026  57.673  32.812  1.00 54.79  ? 118 PHE A N   1 
ATOM   890   C CA  . PHE A 1 113 ? 21.310  57.045  32.531  1.00 54.60  ? 118 PHE A CA  1 
ATOM   891   C C   . PHE A 1 113 ? 22.320  58.122  32.160  1.00 62.04  ? 118 PHE A C   1 
ATOM   892   O O   . PHE A 1 113 ? 22.061  58.927  31.260  1.00 61.09  ? 118 PHE A O   1 
ATOM   893   C CB  . PHE A 1 113 ? 21.173  56.032  31.391  1.00 49.24  ? 118 PHE A CB  1 
ATOM   894   C CG  . PHE A 1 113 ? 22.273  55.019  31.338  1.00 44.98  ? 118 PHE A CG  1 
ATOM   895   C CD1 . PHE A 1 113 ? 22.392  54.056  32.326  1.00 44.32  ? 118 PHE A CD1 1 
ATOM   896   C CD2 . PHE A 1 113 ? 23.174  55.013  30.285  1.00 43.94  ? 118 PHE A CD2 1 
ATOM   897   C CE1 . PHE A 1 113 ? 23.397  53.112  32.276  1.00 46.42  ? 118 PHE A CE1 1 
ATOM   898   C CE2 . PHE A 1 113 ? 24.183  54.072  30.229  1.00 51.15  ? 118 PHE A CE2 1 
ATOM   899   C CZ  . PHE A 1 113 ? 24.294  53.119  31.223  1.00 51.09  ? 118 PHE A CZ  1 
ATOM   900   N N   . GLU A 1 114 ? 23.468  58.133  32.838  1.00 51.58  ? 119 GLU A N   1 
ATOM   901   C CA  . GLU A 1 114 ? 24.483  59.151  32.579  1.00 58.61  ? 119 GLU A CA  1 
ATOM   902   C C   . GLU A 1 114 ? 25.869  58.585  32.852  1.00 55.15  ? 119 GLU A C   1 
ATOM   903   O O   . GLU A 1 114 ? 26.156  58.148  33.972  1.00 48.00  ? 119 GLU A O   1 
ATOM   904   C CB  . GLU A 1 114 ? 24.233  60.398  33.433  1.00 63.97  ? 119 GLU A CB  1 
ATOM   905   C CG  . GLU A 1 114 ? 25.295  61.479  33.284  1.00 72.90  ? 119 GLU A CG  1 
ATOM   906   C CD  . GLU A 1 114 ? 24.921  62.774  33.985  1.00 80.20  ? 119 GLU A CD  1 
ATOM   907   O OE1 . GLU A 1 114 ? 24.399  62.713  35.119  1.00 80.77  ? 119 GLU A OE1 1 
ATOM   908   O OE2 . GLU A 1 114 ? 25.153  63.855  33.400  1.00 90.16  ? 119 GLU A OE2 1 
ATOM   909   N N   . LYS A 1 115 ? 26.724  58.609  31.831  1.00 49.08  ? 120 LYS A N   1 
ATOM   910   C CA  . LYS A 1 115 ? 28.117  58.211  31.989  1.00 55.86  ? 120 LYS A CA  1 
ATOM   911   C C   . LYS A 1 115 ? 28.874  59.239  32.825  1.00 52.33  ? 120 LYS A C   1 
ATOM   912   O O   . LYS A 1 115 ? 28.796  60.443  32.565  1.00 60.13  ? 120 LYS A O   1 
ATOM   913   C CB  . LYS A 1 115 ? 28.775  58.056  30.618  1.00 53.95  ? 120 LYS A CB  1 
ATOM   914   C CG  . LYS A 1 115 ? 30.175  57.469  30.653  1.00 47.40  ? 120 LYS A CG  1 
ATOM   915   C CD  . LYS A 1 115 ? 30.522  56.815  29.325  1.00 51.91  ? 120 LYS A CD  1 
ATOM   916   C CE  . LYS A 1 115 ? 30.860  57.848  28.265  1.00 52.63  ? 120 LYS A CE  1 
ATOM   917   N NZ  . LYS A 1 115 ? 32.152  57.535  27.595  1.00 75.13  ? 120 LYS A NZ  1 
ATOM   918   N N   . THR A 1 116 ? 29.612  58.757  33.828  1.00 49.43  ? 121 THR A N   1 
ATOM   919   C CA  . THR A 1 116 ? 30.338  59.598  34.773  1.00 53.77  ? 121 THR A CA  1 
ATOM   920   C C   . THR A 1 116 ? 31.782  59.127  34.872  1.00 56.95  ? 121 THR A C   1 
ATOM   921   O O   . THR A 1 116 ? 32.045  57.924  34.960  1.00 53.89  ? 121 THR A O   1 
ATOM   922   C CB  . THR A 1 116 ? 29.700  59.558  36.176  1.00 56.36  ? 121 THR A CB  1 
ATOM   923   O OG1 . THR A 1 116 ? 28.308  59.878  36.083  1.00 72.09  ? 121 THR A OG1 1 
ATOM   924   C CG2 . THR A 1 116 ? 30.377  60.556  37.111  1.00 55.70  ? 121 THR A CG2 1 
ATOM   925   N N   . LEU A 1 117 ? 32.712  60.079  34.870  1.00 61.38  ? 122 LEU A N   1 
ATOM   926   C CA  . LEU A 1 117 ? 34.121  59.783  35.105  1.00 54.20  ? 122 LEU A CA  1 
ATOM   927   C C   . LEU A 1 117 ? 34.340  59.699  36.611  1.00 55.35  ? 122 LEU A C   1 
ATOM   928   O O   . LEU A 1 117 ? 34.213  60.702  37.319  1.00 59.41  ? 122 LEU A O   1 
ATOM   929   C CB  . LEU A 1 117 ? 34.999  60.859  34.471  1.00 56.27  ? 122 LEU A CB  1 
ATOM   930   C CG  . LEU A 1 117 ? 36.518  60.792  34.662  1.00 70.34  ? 122 LEU A CG  1 
ATOM   931   C CD1 . LEU A 1 117 ? 37.042  59.373  34.503  1.00 63.01  ? 122 LEU A CD1 1 
ATOM   932   C CD2 . LEU A 1 117 ? 37.216  61.731  33.687  1.00 63.29  ? 122 LEU A CD2 1 
ATOM   933   N N   . ILE A 1 118 ? 34.655  58.503  37.110  1.00 59.17  ? 123 ILE A N   1 
ATOM   934   C CA  . ILE A 1 118 ? 34.780  58.287  38.541  1.00 61.10  ? 123 ILE A CA  1 
ATOM   935   C C   . ILE A 1 118 ? 36.224  58.067  38.983  1.00 58.82  ? 123 ILE A C   1 
ATOM   936   O O   . ILE A 1 118 ? 36.562  58.391  40.128  1.00 65.47  ? 123 ILE A O   1 
ATOM   937   C CB  . ILE A 1 118 ? 33.888  57.113  38.998  1.00 54.11  ? 123 ILE A CB  1 
ATOM   938   C CG1 . ILE A 1 118 ? 34.205  55.855  38.191  1.00 50.62  ? 123 ILE A CG1 1 
ATOM   939   C CG2 . ILE A 1 118 ? 32.423  57.470  38.859  1.00 59.89  ? 123 ILE A CG2 1 
ATOM   940   C CD1 . ILE A 1 118 ? 33.987  54.579  38.961  1.00 40.92  ? 123 ILE A CD1 1 
ATOM   941   N N   . ILE A 1 119 ? 37.078  57.516  38.127  1.00 58.43  ? 124 ILE A N   1 
ATOM   942   C CA  . ILE A 1 119 ? 38.489  57.317  38.450  1.00 57.63  ? 124 ILE A CA  1 
ATOM   943   C C   . ILE A 1 119 ? 39.326  57.748  37.252  1.00 52.78  ? 124 ILE A C   1 
ATOM   944   O O   . ILE A 1 119 ? 39.532  56.954  36.323  1.00 51.73  ? 124 ILE A O   1 
ATOM   945   C CB  . ILE A 1 119 ? 38.793  55.858  38.828  1.00 50.78  ? 124 ILE A CB  1 
ATOM   946   C CG1 . ILE A 1 119 ? 37.883  55.383  39.963  1.00 56.85  ? 124 ILE A CG1 1 
ATOM   947   C CG2 . ILE A 1 119 ? 40.250  55.713  39.235  1.00 57.17  ? 124 ILE A CG2 1 
ATOM   948   C CD1 . ILE A 1 119 ? 37.907  53.883  40.169  1.00 54.65  ? 124 ILE A CD1 1 
ATOM   949   N N   . PRO A 1 120 ? 39.823  58.980  37.226  1.00 60.70  ? 125 PRO A N   1 
ATOM   950   C CA  . PRO A 1 120 ? 40.652  59.417  36.097  1.00 54.83  ? 125 PRO A CA  1 
ATOM   951   C C   . PRO A 1 120 ? 41.998  58.711  36.097  1.00 57.11  ? 125 PRO A C   1 
ATOM   952   O O   . PRO A 1 120 ? 42.467  58.198  37.116  1.00 59.12  ? 125 PRO A O   1 
ATOM   953   C CB  . PRO A 1 120 ? 40.815  60.922  36.327  1.00 57.57  ? 125 PRO A CB  1 
ATOM   954   C CG  . PRO A 1 120 ? 40.596  61.115  37.792  1.00 55.89  ? 125 PRO A CG  1 
ATOM   955   C CD  . PRO A 1 120 ? 39.735  59.991  38.294  1.00 51.28  ? 125 PRO A CD  1 
ATOM   956   N N   . LYS A 1 121 A 42.623  58.691  34.917  1.00 56.67  ? 125 LYS A N   1 
ATOM   957   C CA  . LYS A 1 121 A 43.914  58.028  34.767  1.00 58.54  ? 125 LYS A CA  1 
ATOM   958   C C   . LYS A 1 121 A 44.997  58.656  35.636  1.00 52.88  ? 125 LYS A C   1 
ATOM   959   O O   . LYS A 1 121 A 45.990  57.988  35.950  1.00 63.57  ? 125 LYS A O   1 
ATOM   960   C CB  . LYS A 1 121 A 44.341  58.043  33.298  1.00 63.16  ? 125 LYS A CB  1 
ATOM   961   C CG  . LYS A 1 121 A 43.441  57.220  32.384  1.00 56.95  ? 125 LYS A CG  1 
ATOM   962   C CD  . LYS A 1 121 A 44.134  56.913  31.067  1.00 53.42  ? 125 LYS A CD  1 
ATOM   963   C CE  . LYS A 1 121 A 43.249  56.075  30.160  1.00 57.99  ? 125 LYS A CE  1 
ATOM   964   N NZ  . LYS A 1 121 A 43.506  56.361  28.721  1.00 71.85  ? 125 LYS A NZ  1 
ATOM   965   N N   . SER A 1 122 B 44.821  59.914  36.047  1.00 60.58  ? 125 SER A N   1 
ATOM   966   C CA  . SER A 1 122 B 45.777  60.567  36.933  1.00 63.66  ? 125 SER A CA  1 
ATOM   967   C C   . SER A 1 122 B 45.865  59.896  38.299  1.00 72.67  ? 125 SER A C   1 
ATOM   968   O O   . SER A 1 122 B 46.853  60.098  39.011  1.00 80.09  ? 125 SER A O   1 
ATOM   969   C CB  . SER A 1 122 B 45.403  62.039  37.105  1.00 71.31  ? 125 SER A CB  1 
ATOM   970   O OG  . SER A 1 122 B 44.845  62.561  35.910  1.00 76.32  ? 125 SER A OG  1 
ATOM   971   N N   . SER A 1 123 ? 44.859  59.104  38.678  1.00 68.88  ? 126 SER A N   1 
ATOM   972   C CA  . SER A 1 123 ? 44.879  58.407  39.960  1.00 70.33  ? 126 SER A CA  1 
ATOM   973   C C   . SER A 1 123 ? 45.839  57.224  39.976  1.00 63.33  ? 126 SER A C   1 
ATOM   974   O O   . SER A 1 123 ? 46.006  56.602  41.031  1.00 66.21  ? 126 SER A O   1 
ATOM   975   C CB  . SER A 1 123 ? 43.470  57.930  40.319  1.00 69.27  ? 126 SER A CB  1 
ATOM   976   O OG  . SER A 1 123 ? 42.536  58.991  40.230  1.00 71.04  ? 126 SER A OG  1 
ATOM   977   N N   . TRP A 1 124 ? 46.458  56.893  38.843  1.00 59.31  ? 127 TRP A N   1 
ATOM   978   C CA  . TRP A 1 124 ? 47.419  55.798  38.779  1.00 81.32  ? 127 TRP A CA  1 
ATOM   979   C C   . TRP A 1 124 ? 48.817  56.344  38.508  1.00 76.85  ? 127 TRP A C   1 
ATOM   980   O O   . TRP A 1 124 ? 49.294  56.298  37.366  1.00 77.27  ? 127 TRP A O   1 
ATOM   981   C CB  . TRP A 1 124 ? 47.009  54.794  37.698  1.00 66.39  ? 127 TRP A CB  1 
ATOM   982   C CG  . TRP A 1 124 ? 45.550  54.460  37.746  1.00 66.00  ? 127 TRP A CG  1 
ATOM   983   C CD1 . TRP A 1 124 ? 44.592  54.837  36.850  1.00 55.56  ? 127 TRP A CD1 1 
ATOM   984   C CD2 . TRP A 1 124 ? 44.880  53.689  38.750  1.00 59.81  ? 127 TRP A CD2 1 
ATOM   985   N NE1 . TRP A 1 124 ? 43.367  54.347  37.233  1.00 62.88  ? 127 TRP A NE1 1 
ATOM   986   C CE2 . TRP A 1 124 ? 43.517  53.638  38.396  1.00 64.06  ? 127 TRP A CE2 1 
ATOM   987   C CE3 . TRP A 1 124 ? 45.300  53.036  39.912  1.00 57.05  ? 127 TRP A CE3 1 
ATOM   988   C CZ2 . TRP A 1 124 ? 42.571  52.959  39.163  1.00 61.87  ? 127 TRP A CZ2 1 
ATOM   989   C CZ3 . TRP A 1 124 ? 44.360  52.364  40.671  1.00 74.92  ? 127 TRP A CZ3 1 
ATOM   990   C CH2 . TRP A 1 124 ? 43.011  52.331  40.294  1.00 63.54  ? 127 TRP A CH2 1 
ATOM   991   N N   . PRO A 1 125 ? 49.507  56.866  39.528  1.00 80.72  ? 128 PRO A N   1 
ATOM   992   C CA  . PRO A 1 125 ? 50.790  57.537  39.281  1.00 82.50  ? 128 PRO A CA  1 
ATOM   993   C C   . PRO A 1 125 ? 51.962  56.571  39.166  1.00 78.54  ? 128 PRO A C   1 
ATOM   994   O O   . PRO A 1 125 ? 52.935  56.850  38.458  1.00 73.59  ? 128 PRO A O   1 
ATOM   995   C CB  . PRO A 1 125 ? 50.935  58.456  40.499  1.00 77.71  ? 128 PRO A CB  1 
ATOM   996   C CG  . PRO A 1 125 ? 50.216  57.724  41.598  1.00 78.96  ? 128 PRO A CG  1 
ATOM   997   C CD  . PRO A 1 125 ? 49.150  56.859  40.959  1.00 85.15  ? 128 PRO A CD  1 
ATOM   998   N N   . ASN A 1 126 ? 51.876  55.429  39.845  1.00 67.19  ? 129 ASN A N   1 
ATOM   999   C CA  . ASN A 1 126 ? 52.946  54.443  39.856  1.00 58.98  ? 129 ASN A CA  1 
ATOM   1000  C C   . ASN A 1 126 ? 52.715  53.310  38.869  1.00 65.64  ? 129 ASN A C   1 
ATOM   1001  O O   . ASN A 1 126 ? 53.437  52.310  38.916  1.00 72.40  ? 129 ASN A O   1 
ATOM   1002  C CB  . ASN A 1 126 ? 53.125  53.871  41.262  1.00 60.65  ? 129 ASN A CB  1 
ATOM   1003  C CG  . ASN A 1 126 ? 52.783  54.872  42.340  1.00 76.06  ? 129 ASN A CG  1 
ATOM   1004  O OD1 . ASN A 1 126 ? 53.383  55.946  42.416  1.00 74.92  ? 129 ASN A OD1 1 
ATOM   1005  N ND2 . ASN A 1 126 ? 51.811  54.530  43.179  1.00 85.22  ? 129 ASN A ND2 1 
ATOM   1006  N N   . HIS A 1 127 ? 51.727  53.437  37.985  1.00 72.91  ? 130 HIS A N   1 
ATOM   1007  C CA  . HIS A 1 127 ? 51.411  52.404  37.011  1.00 65.69  ? 130 HIS A CA  1 
ATOM   1008  C C   . HIS A 1 127 ? 51.260  53.026  35.632  1.00 62.81  ? 130 HIS A C   1 
ATOM   1009  O O   . HIS A 1 127 ? 50.921  54.205  35.498  1.00 71.81  ? 130 HIS A O   1 
ATOM   1010  C CB  . HIS A 1 127 ? 50.121  51.652  37.379  1.00 65.90  ? 130 HIS A CB  1 
ATOM   1011  C CG  . HIS A 1 127 ? 50.118  51.105  38.772  1.00 65.91  ? 130 HIS A CG  1 
ATOM   1012  N ND1 . HIS A 1 127 ? 49.862  51.887  39.879  1.00 60.87  ? 130 HIS A ND1 1 
ATOM   1013  C CD2 . HIS A 1 127 ? 50.337  49.852  39.238  1.00 61.94  ? 130 HIS A CD2 1 
ATOM   1014  C CE1 . HIS A 1 127 ? 49.929  51.139  40.966  1.00 66.66  ? 130 HIS A CE1 1 
ATOM   1015  N NE2 . HIS A 1 127 ? 50.215  49.900  40.605  1.00 58.70  ? 130 HIS A NE2 1 
ATOM   1016  N N   . GLU A 1 128 ? 51.521  52.221  34.606  1.00 63.03  ? 131 GLU A N   1 
ATOM   1017  C CA  . GLU A 1 128 ? 51.311  52.632  33.225  1.00 67.06  ? 131 GLU A CA  1 
ATOM   1018  C C   . GLU A 1 128 ? 49.857  52.395  32.839  1.00 64.40  ? 131 GLU A C   1 
ATOM   1019  O O   . GLU A 1 128 ? 49.315  51.308  33.070  1.00 61.05  ? 131 GLU A O   1 
ATOM   1020  C CB  . GLU A 1 128 ? 52.244  51.867  32.286  1.00 67.76  ? 131 GLU A CB  1 
ATOM   1021  C CG  . GLU A 1 128 ? 52.682  52.652  31.058  1.00 84.35  ? 131 GLU A CG  1 
ATOM   1022  C CD  . GLU A 1 128 ? 53.112  54.068  31.391  1.00 93.95  ? 131 GLU A CD  1 
ATOM   1023  O OE1 . GLU A 1 128 ? 54.142  54.230  32.082  1.00 76.16  ? 131 GLU A OE1 1 
ATOM   1024  O OE2 . GLU A 1 128 ? 52.419  55.017  30.964  1.00 96.44  ? 131 GLU A OE2 1 
ATOM   1025  N N   . THR A 1 129 ? 49.227  53.414  32.250  1.00 74.31  ? 132 THR A N   1 
ATOM   1026  C CA  . THR A 1 129 ? 47.808  53.372  31.911  1.00 60.72  ? 132 THR A CA  1 
ATOM   1027  C C   . THR A 1 129 ? 47.562  53.476  30.410  1.00 58.63  ? 132 THR A C   1 
ATOM   1028  O O   . THR A 1 129 ? 46.429  53.727  29.990  1.00 61.52  ? 132 THR A O   1 
ATOM   1029  C CB  . THR A 1 129 ? 47.057  54.490  32.632  1.00 60.73  ? 132 THR A CB  1 
ATOM   1030  O OG1 . THR A 1 129 ? 47.365  55.742  32.007  1.00 59.36  ? 132 THR A OG1 1 
ATOM   1031  C CG2 . THR A 1 129 ? 47.461  54.544  34.100  1.00 58.62  ? 132 THR A CG2 1 
ATOM   1032  N N   . SER A 1 130 ? 48.595  53.281  29.592  1.00 69.86  ? 133 SER A N   1 
ATOM   1033  C CA  . SER A 1 130 ? 48.517  53.489  28.153  1.00 65.84  ? 133 SER A CA  1 
ATOM   1034  C C   . SER A 1 130 ? 48.320  52.196  27.370  1.00 55.57  ? 133 SER A C   1 
ATOM   1035  O O   . SER A 1 130 ? 48.495  52.196  26.147  1.00 64.49  ? 133 SER A O   1 
ATOM   1036  C CB  . SER A 1 130 ? 49.777  54.201  27.659  1.00 73.91  ? 133 SER A CB  1 
ATOM   1037  O OG  . SER A 1 130 ? 50.944  53.519  28.090  1.00 73.01  ? 133 SER A OG  1 
ATOM   1038  N N   . GLY A 1 131 ? 47.973  51.100  28.039  1.00 56.09  ? 134 GLY A N   1 
ATOM   1039  C CA  . GLY A 1 131 ? 47.820  49.823  27.372  1.00 39.64  ? 134 GLY A CA  1 
ATOM   1040  C C   . GLY A 1 131 ? 46.789  49.826  26.259  1.00 56.00  ? 134 GLY A C   1 
ATOM   1041  O O   . GLY A 1 131 ? 45.655  50.277  26.449  1.00 54.38  ? 134 GLY A O   1 
ATOM   1042  N N   . VAL A 1 132 ? 47.180  49.329  25.087  1.00 57.55  ? 135 VAL A N   1 
ATOM   1043  C CA  . VAL A 1 132 ? 46.291  49.183  23.944  1.00 53.26  ? 135 VAL A CA  1 
ATOM   1044  C C   . VAL A 1 132 ? 46.510  47.799  23.343  1.00 48.46  ? 135 VAL A C   1 
ATOM   1045  O O   . VAL A 1 132 ? 47.379  47.040  23.770  1.00 45.04  ? 135 VAL A O   1 
ATOM   1046  C CB  . VAL A 1 132 ? 46.515  50.277  22.880  1.00 50.53  ? 135 VAL A CB  1 
ATOM   1047  C CG1 . VAL A 1 132 ? 46.181  51.646  23.444  1.00 45.95  ? 135 VAL A CG1 1 
ATOM   1048  C CG2 . VAL A 1 132 ? 47.947  50.240  22.385  1.00 46.93  ? 135 VAL A CG2 1 
ATOM   1049  N N   . SER A 1 133 ? 45.696  47.472  22.341  1.00 52.45  ? 136 SER A N   1 
ATOM   1050  C CA  . SER A 1 133 ? 45.813  46.187  21.668  1.00 55.88  ? 136 SER A CA  1 
ATOM   1051  C C   . SER A 1 133 ? 45.298  46.305  20.243  1.00 57.59  ? 136 SER A C   1 
ATOM   1052  O O   . SER A 1 133 ? 44.397  47.097  19.955  1.00 58.22  ? 136 SER A O   1 
ATOM   1053  C CB  . SER A 1 133 ? 45.044  45.087  22.404  1.00 55.35  ? 136 SER A CB  1 
ATOM   1054  O OG  . SER A 1 133 ? 44.811  43.988  21.540  1.00 53.44  ? 136 SER A OG  1 
ATOM   1055  N N   . ALA A 1 134 ? 45.875  45.493  19.352  1.00 52.58  ? 137 ALA A N   1 
ATOM   1056  C CA  . ALA A 1 134 ? 45.440  45.485  17.961  1.00 53.92  ? 137 ALA A CA  1 
ATOM   1057  C C   . ALA A 1 134 ? 44.092  44.800  17.781  1.00 53.93  ? 137 ALA A C   1 
ATOM   1058  O O   . ALA A 1 134 ? 43.455  44.978  16.738  1.00 58.28  ? 137 ALA A O   1 
ATOM   1059  C CB  . ALA A 1 134 ? 46.490  44.811  17.080  1.00 43.88  ? 137 ALA A CB  1 
ATOM   1060  N N   . ALA A 1 135 ? 43.647  44.020  18.768  1.00 62.07  ? 138 ALA A N   1 
ATOM   1061  C CA  . ALA A 1 135 ? 42.312  43.439  18.724  1.00 56.47  ? 138 ALA A CA  1 
ATOM   1062  C C   . ALA A 1 135 ? 41.227  44.469  18.998  1.00 67.56  ? 138 ALA A C   1 
ATOM   1063  O O   . ALA A 1 135 ? 40.050  44.184  18.748  1.00 57.90  ? 138 ALA A O   1 
ATOM   1064  C CB  . ALA A 1 135 ? 42.204  42.290  19.729  1.00 56.35  ? 138 ALA A CB  1 
ATOM   1065  N N   . CYS A 1 136 ? 41.597  45.656  19.479  1.00 63.03  ? 139 CYS A N   1 
ATOM   1066  C CA  . CYS A 1 136 ? 40.663  46.746  19.756  1.00 49.83  ? 139 CYS A CA  1 
ATOM   1067  C C   . CYS A 1 136 ? 41.092  47.994  18.994  1.00 48.78  ? 139 CYS A C   1 
ATOM   1068  O O   . CYS A 1 136 ? 41.422  49.021  19.597  1.00 47.20  ? 139 CYS A O   1 
ATOM   1069  C CB  . CYS A 1 136 ? 40.603  47.037  21.253  1.00 52.78  ? 139 CYS A CB  1 
ATOM   1070  S SG  . CYS A 1 136 ? 39.900  45.721  22.240  1.00 79.71  ? 139 CYS A SG  1 
ATOM   1071  N N   . PRO A 1 137 ? 41.087  47.946  17.666  1.00 50.64  ? 140 PRO A N   1 
ATOM   1072  C CA  . PRO A 1 137 ? 41.584  49.087  16.895  1.00 44.80  ? 140 PRO A CA  1 
ATOM   1073  C C   . PRO A 1 137 ? 40.598  50.242  16.910  1.00 49.25  ? 140 PRO A C   1 
ATOM   1074  O O   . PRO A 1 137 ? 39.398  50.080  17.145  1.00 57.39  ? 140 PRO A O   1 
ATOM   1075  C CB  . PRO A 1 137 ? 41.749  48.517  15.485  1.00 44.83  ? 140 PRO A CB  1 
ATOM   1076  C CG  . PRO A 1 137 ? 40.709  47.446  15.402  1.00 43.84  ? 140 PRO A CG  1 
ATOM   1077  C CD  . PRO A 1 137 ? 40.503  46.907  16.797  1.00 43.62  ? 140 PRO A CD  1 
ATOM   1078  N N   . TYR A 1 138 ? 41.135  51.432  16.675  1.00 57.57  ? 141 TYR A N   1 
ATOM   1079  C CA  . TYR A 1 138 ? 40.333  52.622  16.421  1.00 45.70  ? 141 TYR A CA  1 
ATOM   1080  C C   . TYR A 1 138 ? 40.924  53.294  15.194  1.00 50.12  ? 141 TYR A C   1 
ATOM   1081  O O   . TYR A 1 138 ? 42.062  53.774  15.237  1.00 58.47  ? 141 TYR A O   1 
ATOM   1082  C CB  . TYR A 1 138 ? 40.332  53.569  17.620  1.00 53.95  ? 141 TYR A CB  1 
ATOM   1083  C CG  . TYR A 1 138 ? 39.497  54.803  17.394  1.00 55.73  ? 141 TYR A CG  1 
ATOM   1084  C CD1 . TYR A 1 138 ? 38.147  54.700  17.084  1.00 60.73  ? 141 TYR A CD1 1 
ATOM   1085  C CD2 . TYR A 1 138 ? 40.057  56.070  17.473  1.00 56.48  ? 141 TYR A CD2 1 
ATOM   1086  C CE1 . TYR A 1 138 ? 37.375  55.825  16.870  1.00 52.06  ? 141 TYR A CE1 1 
ATOM   1087  C CE2 . TYR A 1 138 ? 39.296  57.201  17.260  1.00 54.63  ? 141 TYR A CE2 1 
ATOM   1088  C CZ  . TYR A 1 138 ? 37.955  57.073  16.960  1.00 65.15  ? 141 TYR A CZ  1 
ATOM   1089  O OH  . TYR A 1 138 ? 37.191  58.195  16.747  1.00 58.58  ? 141 TYR A OH  1 
ATOM   1090  N N   . GLN A 1 139 ? 40.162  53.318  14.103  1.00 50.10  ? 142 GLN A N   1 
ATOM   1091  C CA  . GLN A 1 139 ? 40.637  53.867  12.834  1.00 51.20  ? 142 GLN A CA  1 
ATOM   1092  C C   . GLN A 1 139 ? 41.949  53.207  12.410  1.00 49.38  ? 142 GLN A C   1 
ATOM   1093  O O   . GLN A 1 139 ? 42.880  53.872  11.949  1.00 52.85  ? 142 GLN A O   1 
ATOM   1094  C CB  . GLN A 1 139 ? 40.790  55.389  12.911  1.00 50.94  ? 142 GLN A CB  1 
ATOM   1095  C CG  . GLN A 1 139 ? 39.693  56.085  13.705  1.00 59.13  ? 142 GLN A CG  1 
ATOM   1096  C CD  . GLN A 1 139 ? 38.753  56.901  12.829  1.00 53.33  ? 142 GLN A CD  1 
ATOM   1097  O OE1 . GLN A 1 139 ? 38.560  56.606  11.651  1.00 61.42  ? 142 GLN A OE1 1 
ATOM   1098  N NE2 . GLN A 1 139 ? 38.158  57.928  13.408  1.00 57.28  ? 142 GLN A NE2 1 
ATOM   1099  N N   . GLY A 1 140 ? 42.027  51.887  12.576  1.00 48.35  ? 143 GLY A N   1 
ATOM   1100  C CA  . GLY A 1 140 ? 43.190  51.126  12.165  1.00 42.13  ? 143 GLY A CA  1 
ATOM   1101  C C   . GLY A 1 140 ? 44.376  51.216  13.095  1.00 51.36  ? 143 GLY A C   1 
ATOM   1102  O O   . GLY A 1 140 ? 45.459  50.737  12.742  1.00 59.90  ? 143 GLY A O   1 
ATOM   1103  N N   . VAL A 1 141 ? 44.206  51.810  14.270  1.00 45.67  ? 144 VAL A N   1 
ATOM   1104  C CA  . VAL A 1 141 ? 45.295  52.041  15.212  1.00 42.77  ? 144 VAL A CA  1 
ATOM   1105  C C   . VAL A 1 141 ? 44.954  51.307  16.503  1.00 52.90  ? 144 VAL A C   1 
ATOM   1106  O O   . VAL A 1 141 ? 43.797  51.358  16.947  1.00 61.78  ? 144 VAL A O   1 
ATOM   1107  C CB  . VAL A 1 141 ? 45.502  53.547  15.443  1.00 46.04  ? 144 VAL A CB  1 
ATOM   1108  C CG1 . VAL A 1 141 ? 46.436  53.799  16.612  1.00 47.75  ? 144 VAL A CG1 1 
ATOM   1109  C CG2 . VAL A 1 141 ? 46.028  54.203  14.178  1.00 40.72  ? 144 VAL A CG2 1 
ATOM   1110  N N   . PRO A 1 142 ? 45.906  50.608  17.126  1.00 58.96  ? 145 PRO A N   1 
ATOM   1111  C CA  . PRO A 1 142 ? 45.600  49.885  18.368  1.00 46.67  ? 145 PRO A CA  1 
ATOM   1112  C C   . PRO A 1 142 ? 45.059  50.812  19.445  1.00 47.03  ? 145 PRO A C   1 
ATOM   1113  O O   . PRO A 1 142 ? 45.576  51.908  19.669  1.00 57.89  ? 145 PRO A O   1 
ATOM   1114  C CB  . PRO A 1 142 ? 46.952  49.288  18.771  1.00 42.17  ? 145 PRO A CB  1 
ATOM   1115  C CG  . PRO A 1 142 ? 47.687  49.149  17.483  1.00 46.78  ? 145 PRO A CG  1 
ATOM   1116  C CD  . PRO A 1 142 ? 47.273  50.327  16.649  1.00 54.14  ? 145 PRO A CD  1 
ATOM   1117  N N   . SER A 1 143 ? 44.023  50.345  20.129  1.00 44.75  ? 146 SER A N   1 
ATOM   1118  C CA  . SER A 1 143 ? 43.326  51.145  21.129  1.00 52.58  ? 146 SER A CA  1 
ATOM   1119  C C   . SER A 1 143 ? 42.824  50.197  22.214  1.00 60.66  ? 146 SER A C   1 
ATOM   1120  O O   . SER A 1 143 ? 43.281  49.053  22.316  1.00 55.95  ? 146 SER A O   1 
ATOM   1121  C CB  . SER A 1 143 ? 42.208  51.966  20.460  1.00 44.23  ? 146 SER A CB  1 
ATOM   1122  O OG  . SER A 1 143 ? 41.593  52.847  21.381  1.00 54.18  ? 146 SER A OG  1 
ATOM   1123  N N   . PHE A 1 144 ? 41.887  50.670  23.032  1.00 57.26  ? 147 PHE A N   1 
ATOM   1124  C CA  . PHE A 1 144 ? 41.354  49.878  24.130  1.00 58.05  ? 147 PHE A CA  1 
ATOM   1125  C C   . PHE A 1 144 ? 39.954  50.371  24.461  1.00 50.30  ? 147 PHE A C   1 
ATOM   1126  O O   . PHE A 1 144 ? 39.491  51.385  23.931  1.00 50.28  ? 147 PHE A O   1 
ATOM   1127  C CB  . PHE A 1 144 ? 42.263  49.955  25.363  1.00 52.36  ? 147 PHE A CB  1 
ATOM   1128  C CG  . PHE A 1 144 ? 41.978  48.899  26.392  1.00 46.93  ? 147 PHE A CG  1 
ATOM   1129  C CD1 . PHE A 1 144 ? 41.944  47.560  26.037  1.00 44.16  ? 147 PHE A CD1 1 
ATOM   1130  C CD2 . PHE A 1 144 ? 41.739  49.246  27.709  1.00 44.69  ? 147 PHE A CD2 1 
ATOM   1131  C CE1 . PHE A 1 144 ? 41.684  46.588  26.979  1.00 34.58  ? 147 PHE A CE1 1 
ATOM   1132  C CE2 . PHE A 1 144 ? 41.479  48.276  28.659  1.00 54.08  ? 147 PHE A CE2 1 
ATOM   1133  C CZ  . PHE A 1 144 ? 41.450  46.944  28.292  1.00 42.59  ? 147 PHE A CZ  1 
ATOM   1134  N N   . PHE A 1 145 ? 39.279  49.635  25.345  1.00 57.64  ? 148 PHE A N   1 
ATOM   1135  C CA  . PHE A 1 145 ? 37.979  50.060  25.851  1.00 49.42  ? 148 PHE A CA  1 
ATOM   1136  C C   . PHE A 1 145 ? 38.093  51.447  26.469  1.00 45.62  ? 148 PHE A C   1 
ATOM   1137  O O   . PHE A 1 145 ? 39.014  51.720  27.242  1.00 48.96  ? 148 PHE A O   1 
ATOM   1138  C CB  . PHE A 1 145 ? 37.462  49.073  26.896  1.00 49.55  ? 148 PHE A CB  1 
ATOM   1139  C CG  . PHE A 1 145 ? 37.260  47.674  26.384  1.00 50.32  ? 148 PHE A CG  1 
ATOM   1140  C CD1 . PHE A 1 145 ? 36.249  47.389  25.479  1.00 43.79  ? 148 PHE A CD1 1 
ATOM   1141  C CD2 . PHE A 1 145 ? 38.063  46.638  26.831  1.00 46.25  ? 148 PHE A CD2 1 
ATOM   1142  C CE1 . PHE A 1 145 ? 36.055  46.102  25.017  1.00 53.07  ? 148 PHE A CE1 1 
ATOM   1143  C CE2 . PHE A 1 145 ? 37.874  45.341  26.373  1.00 48.52  ? 148 PHE A CE2 1 
ATOM   1144  C CZ  . PHE A 1 145 ? 36.869  45.074  25.465  1.00 51.26  ? 148 PHE A CZ  1 
ATOM   1145  N N   . ARG A 1 146 ? 37.144  52.322  26.136  1.00 53.51  ? 149 ARG A N   1 
ATOM   1146  C CA  . ARG A 1 146 ? 37.223  53.715  26.558  1.00 44.80  ? 149 ARG A CA  1 
ATOM   1147  C C   . ARG A 1 146 ? 36.808  53.939  28.006  1.00 43.40  ? 149 ARG A C   1 
ATOM   1148  O O   . ARG A 1 146 ? 37.101  55.007  28.552  1.00 48.86  ? 149 ARG A O   1 
ATOM   1149  C CB  . ARG A 1 146 ? 36.364  54.586  25.637  1.00 47.28  ? 149 ARG A CB  1 
ATOM   1150  C CG  . ARG A 1 146 ? 37.082  55.016  24.368  1.00 60.06  ? 149 ARG A CG  1 
ATOM   1151  C CD  . ARG A 1 146 ? 36.225  54.821  23.123  1.00 70.00  ? 149 ARG A CD  1 
ATOM   1152  N NE  . ARG A 1 146 ? 36.361  55.923  22.176  1.00 80.59  ? 149 ARG A NE  1 
ATOM   1153  C CZ  . ARG A 1 146 ? 37.435  56.149  21.429  1.00 82.98  ? 149 ARG A CZ  1 
ATOM   1154  N NH1 . ARG A 1 146 ? 38.494  55.357  21.478  1.00 85.50  ? 149 ARG A NH1 1 
ATOM   1155  N NH2 . ARG A 1 146 ? 37.447  57.201  20.613  1.00 85.03  ? 149 ARG A NH2 1 
ATOM   1156  N N   . ASN A 1 147 ? 36.144  52.975  28.643  1.00 44.98  ? 150 ASN A N   1 
ATOM   1157  C CA  . ASN A 1 147 ? 35.617  53.167  29.987  1.00 45.56  ? 150 ASN A CA  1 
ATOM   1158  C C   . ASN A 1 147 ? 36.385  52.404  31.054  1.00 43.75  ? 150 ASN A C   1 
ATOM   1159  O O   . ASN A 1 147 ? 36.052  52.519  32.238  1.00 43.84  ? 150 ASN A O   1 
ATOM   1160  C CB  . ASN A 1 147 ? 34.138  52.775  30.030  1.00 52.69  ? 150 ASN A CB  1 
ATOM   1161  C CG  . ASN A 1 147 ? 33.310  53.549  29.029  1.00 59.96  ? 150 ASN A CG  1 
ATOM   1162  O OD1 . ASN A 1 147 ? 33.536  54.744  28.813  1.00 57.10  ? 150 ASN A OD1 1 
ATOM   1163  N ND2 . ASN A 1 147 ? 32.346  52.877  28.410  1.00 53.31  ? 150 ASN A ND2 1 
ATOM   1164  N N   . VAL A 1 148 ? 37.401  51.632  30.672  1.00 44.38  ? 151 VAL A N   1 
ATOM   1165  C CA  . VAL A 1 148 ? 38.266  50.941  31.615  1.00 40.13  ? 151 VAL A CA  1 
ATOM   1166  C C   . VAL A 1 148 ? 39.709  51.185  31.201  1.00 49.04  ? 151 VAL A C   1 
ATOM   1167  O O   . VAL A 1 148 ? 39.995  51.592  30.073  1.00 49.58  ? 151 VAL A O   1 
ATOM   1168  C CB  . VAL A 1 148 ? 37.975  49.428  31.692  1.00 50.75  ? 151 VAL A CB  1 
ATOM   1169  C CG1 . VAL A 1 148 ? 36.615  49.176  32.322  1.00 49.18  ? 151 VAL A CG1 1 
ATOM   1170  C CG2 . VAL A 1 148 ? 38.045  48.813  30.311  1.00 35.69  ? 151 VAL A CG2 1 
ATOM   1171  N N   . VAL A 1 149 ? 40.623  50.927  32.135  1.00 45.30  ? 152 VAL A N   1 
ATOM   1172  C CA  . VAL A 1 149 ? 42.040  51.228  31.968  1.00 51.96  ? 152 VAL A CA  1 
ATOM   1173  C C   . VAL A 1 149 ? 42.842  49.944  32.139  1.00 53.70  ? 152 VAL A C   1 
ATOM   1174  O O   . VAL A 1 149 ? 42.674  49.227  33.133  1.00 55.21  ? 152 VAL A O   1 
ATOM   1175  C CB  . VAL A 1 149 ? 42.511  52.297  32.971  1.00 51.51  ? 152 VAL A CB  1 
ATOM   1176  C CG1 . VAL A 1 149 ? 44.010  52.478  32.879  1.00 58.01  ? 152 VAL A CG1 1 
ATOM   1177  C CG2 . VAL A 1 149 ? 41.795  53.619  32.727  1.00 53.28  ? 152 VAL A CG2 1 
ATOM   1178  N N   . TRP A 1 150 ? 43.718  49.661  31.175  1.00 50.11  ? 153 TRP A N   1 
ATOM   1179  C CA  . TRP A 1 150 ? 44.632  48.520  31.246  1.00 50.70  ? 153 TRP A CA  1 
ATOM   1180  C C   . TRP A 1 150 ? 45.873  48.951  32.019  1.00 48.52  ? 153 TRP A C   1 
ATOM   1181  O O   . TRP A 1 150 ? 46.798  49.540  31.454  1.00 53.00  ? 153 TRP A O   1 
ATOM   1182  C CB  . TRP A 1 150 ? 44.997  48.032  29.848  1.00 48.91  ? 153 TRP A CB  1 
ATOM   1183  C CG  . TRP A 1 150 ? 45.644  46.675  29.820  1.00 46.61  ? 153 TRP A CG  1 
ATOM   1184  C CD1 . TRP A 1 150 ? 46.099  45.957  30.891  1.00 42.96  ? 153 TRP A CD1 1 
ATOM   1185  C CD2 . TRP A 1 150 ? 45.899  45.870  28.660  1.00 44.62  ? 153 TRP A CD2 1 
ATOM   1186  N NE1 . TRP A 1 150 ? 46.617  44.756  30.469  1.00 40.64  ? 153 TRP A NE1 1 
ATOM   1187  C CE2 . TRP A 1 150 ? 46.507  44.679  29.105  1.00 38.32  ? 153 TRP A CE2 1 
ATOM   1188  C CE3 . TRP A 1 150 ? 45.665  46.040  27.290  1.00 50.30  ? 153 TRP A CE3 1 
ATOM   1189  C CZ2 . TRP A 1 150 ? 46.891  43.665  28.228  1.00 51.89  ? 153 TRP A CZ2 1 
ATOM   1190  C CZ3 . TRP A 1 150 ? 46.045  45.032  26.420  1.00 50.81  ? 153 TRP A CZ3 1 
ATOM   1191  C CH2 . TRP A 1 150 ? 46.655  43.861  26.893  1.00 58.40  ? 153 TRP A CH2 1 
ATOM   1192  N N   . LEU A 1 151 ? 45.894  48.660  33.317  1.00 48.13  ? 154 LEU A N   1 
ATOM   1193  C CA  . LEU A 1 151 ? 47.030  49.015  34.156  1.00 54.92  ? 154 LEU A CA  1 
ATOM   1194  C C   . LEU A 1 151 ? 48.157  48.010  33.961  1.00 59.84  ? 154 LEU A C   1 
ATOM   1195  O O   . LEU A 1 151 ? 47.932  46.795  34.001  1.00 61.23  ? 154 LEU A O   1 
ATOM   1196  C CB  . LEU A 1 151 ? 46.618  49.064  35.626  1.00 54.45  ? 154 LEU A CB  1 
ATOM   1197  C CG  . LEU A 1 151 ? 45.612  50.150  36.010  1.00 63.09  ? 154 LEU A CG  1 
ATOM   1198  C CD1 . LEU A 1 151 ? 45.123  49.935  37.432  1.00 58.01  ? 154 LEU A CD1 1 
ATOM   1199  C CD2 . LEU A 1 151 ? 46.213  51.545  35.847  1.00 48.91  ? 154 LEU A CD2 1 
ATOM   1200  N N   . THR A 1 152 ? 49.368  48.518  33.751  1.00 61.45  ? 155 THR A N   1 
ATOM   1201  C CA  . THR A 1 152 ? 50.546  47.678  33.613  1.00 63.89  ? 155 THR A CA  1 
ATOM   1202  C C   . THR A 1 152 ? 51.695  48.301  34.397  1.00 64.54  ? 155 THR A C   1 
ATOM   1203  O O   . THR A 1 152 ? 51.590  49.413  34.923  1.00 61.12  ? 155 THR A O   1 
ATOM   1204  C CB  . THR A 1 152 ? 50.924  47.470  32.139  1.00 62.34  ? 155 THR A CB  1 
ATOM   1205  O OG1 . THR A 1 152 ? 52.246  46.926  32.057  1.00 80.41  ? 155 THR A OG1 1 
ATOM   1206  C CG2 . THR A 1 152 ? 50.860  48.778  31.370  1.00 59.48  ? 155 THR A CG2 1 
ATOM   1207  N N   . LYS A 1 153 ? 52.803  47.566  34.472  1.00 68.94  ? 156 LYS A N   1 
ATOM   1208  C CA  . LYS A 1 153 ? 53.909  47.940  35.342  1.00 69.44  ? 156 LYS A CA  1 
ATOM   1209  C C   . LYS A 1 153 ? 54.597  49.213  34.851  1.00 68.16  ? 156 LYS A C   1 
ATOM   1210  O O   . LYS A 1 153 ? 54.566  49.562  33.667  1.00 61.14  ? 156 LYS A O   1 
ATOM   1211  C CB  . LYS A 1 153 ? 54.930  46.807  35.435  1.00 63.68  ? 156 LYS A CB  1 
ATOM   1212  C CG  . LYS A 1 153 ? 55.934  46.773  34.292  1.00 54.76  ? 156 LYS A CG  1 
ATOM   1213  C CD  . LYS A 1 153 ? 56.366  45.346  33.987  1.00 68.07  ? 156 LYS A CD  1 
ATOM   1214  C CE  . LYS A 1 153 ? 57.619  45.307  33.130  1.00 64.77  ? 156 LYS A CE  1 
ATOM   1215  N NZ  . LYS A 1 153 ? 58.000  43.907  32.783  1.00 66.83  ? 156 LYS A NZ  1 
ATOM   1216  N N   . LYS A 1 154 ? 55.228  49.909  35.798  1.00 60.93  ? 157 LYS A N   1 
ATOM   1217  C CA  . LYS A 1 154 ? 55.964  51.139  35.540  1.00 68.90  ? 157 LYS A CA  1 
ATOM   1218  C C   . LYS A 1 154 ? 57.314  51.066  36.240  1.00 74.30  ? 157 LYS A C   1 
ATOM   1219  O O   . LYS A 1 154 ? 57.377  50.765  37.437  1.00 69.58  ? 157 LYS A O   1 
ATOM   1220  C CB  . LYS A 1 154 ? 55.177  52.362  36.025  1.00 56.41  ? 157 LYS A CB  1 
ATOM   1221  C CG  . LYS A 1 154 ? 55.929  53.673  35.910  1.00 70.89  ? 157 LYS A CG  1 
ATOM   1222  C CD  . LYS A 1 154 ? 55.155  54.684  35.085  1.00 71.23  ? 157 LYS A CD  1 
ATOM   1223  C CE  . LYS A 1 154 ? 55.849  56.035  35.074  1.00 65.78  ? 157 LYS A CE  1 
ATOM   1224  N NZ  . LYS A 1 154 ? 56.713  56.196  33.868  1.00 74.78  ? 157 LYS A NZ  1 
ATOM   1225  N N   . ASN A 1 155 ? 58.383  51.348  35.494  1.00 71.72  ? 158 ASN A N   1 
ATOM   1226  C CA  . ASN A 1 155 ? 59.752  51.343  36.019  1.00 77.23  ? 158 ASN A CA  1 
ATOM   1227  C C   . ASN A 1 155 ? 60.091  50.010  36.688  1.00 68.88  ? 158 ASN A C   1 
ATOM   1228  O O   . ASN A 1 155 ? 60.665  49.959  37.779  1.00 67.61  ? 158 ASN A O   1 
ATOM   1229  C CB  . ASN A 1 155 ? 59.979  52.514  36.982  1.00 63.72  ? 158 ASN A CB  1 
ATOM   1230  C CG  . ASN A 1 155 ? 59.625  53.857  36.367  1.00 71.26  ? 158 ASN A CG  1 
ATOM   1231  O OD1 . ASN A 1 155 ? 59.088  54.738  37.041  1.00 71.95  ? 158 ASN A OD1 1 
ATOM   1232  N ND2 . ASN A 1 155 ? 59.924  54.018  35.082  1.00 67.60  ? 158 ASN A ND2 1 
ATOM   1233  N N   . ASP A 1 156 ? 59.727  48.917  36.012  1.00 63.32  ? 159 ASP A N   1 
ATOM   1234  C CA  . ASP A 1 156 ? 59.969  47.561  36.508  1.00 79.04  ? 159 ASP A CA  1 
ATOM   1235  C C   . ASP A 1 156 ? 59.332  47.350  37.883  1.00 80.45  ? 159 ASP A C   1 
ATOM   1236  O O   . ASP A 1 156 ? 59.943  46.799  38.802  1.00 88.24  ? 159 ASP A O   1 
ATOM   1237  C CB  . ASP A 1 156 ? 61.469  47.252  36.544  1.00 86.83  ? 159 ASP A CB  1 
ATOM   1238  C CG  . ASP A 1 156 ? 61.761  45.764  36.522  1.00 99.43  ? 159 ASP A CG  1 
ATOM   1239  O OD1 . ASP A 1 156 ? 60.902  44.997  36.039  1.00 101.86 ? 159 ASP A OD1 1 
ATOM   1240  O OD2 . ASP A 1 156 ? 62.851  45.364  36.987  1.00 94.20  ? 159 ASP A OD2 1 
ATOM   1241  N N   . ALA A 1 157 ? 58.087  47.797  38.021  1.00 75.99  ? 160 ALA A N   1 
ATOM   1242  C CA  . ALA A 1 157 ? 57.398  47.673  39.296  1.00 78.04  ? 160 ALA A CA  1 
ATOM   1243  C C   . ALA A 1 157 ? 55.895  47.776  39.079  1.00 70.40  ? 160 ALA A C   1 
ATOM   1244  O O   . ALA A 1 157 ? 55.431  48.570  38.256  1.00 66.86  ? 160 ALA A O   1 
ATOM   1245  C CB  . ALA A 1 157 ? 57.870  48.745  40.288  1.00 51.15  ? 160 ALA A CB  1 
ATOM   1246  N N   . TYR A 1 158 ? 55.147  46.959  39.820  1.00 69.32  ? 161 TYR A N   1 
ATOM   1247  C CA  . TYR A 1 158 ? 53.693  47.071  39.934  1.00 65.67  ? 161 TYR A CA  1 
ATOM   1248  C C   . TYR A 1 158 ? 53.390  47.116  41.425  1.00 60.27  ? 161 TYR A C   1 
ATOM   1249  O O   . TYR A 1 158 ? 53.150  46.075  42.054  1.00 60.16  ? 161 TYR A O   1 
ATOM   1250  C CB  . TYR A 1 158 ? 52.974  45.912  39.241  1.00 66.74  ? 161 TYR A CB  1 
ATOM   1251  C CG  . TYR A 1 158 ? 51.475  46.110  39.020  1.00 70.04  ? 161 TYR A CG  1 
ATOM   1252  C CD1 . TYR A 1 158 ? 50.599  46.256  40.092  1.00 58.54  ? 161 TYR A CD1 1 
ATOM   1253  C CD2 . TYR A 1 158 ? 50.938  46.120  37.736  1.00 64.18  ? 161 TYR A CD2 1 
ATOM   1254  C CE1 . TYR A 1 158 ? 49.237  46.423  39.892  1.00 63.10  ? 161 TYR A CE1 1 
ATOM   1255  C CE2 . TYR A 1 158 ? 49.577  46.285  37.528  1.00 67.67  ? 161 TYR A CE2 1 
ATOM   1256  C CZ  . TYR A 1 158 ? 48.730  46.436  38.608  1.00 66.77  ? 161 TYR A CZ  1 
ATOM   1257  O OH  . TYR A 1 158 ? 47.375  46.601  38.402  1.00 59.07  ? 161 TYR A OH  1 
ATOM   1258  N N   . PRO A 1 159 ? 53.434  48.300  42.033  1.00 55.42  ? 162 PRO A N   1 
ATOM   1259  C CA  . PRO A 1 159 ? 53.074  48.410  43.450  1.00 56.67  ? 162 PRO A CA  1 
ATOM   1260  C C   . PRO A 1 159 ? 51.636  47.969  43.676  1.00 75.57  ? 162 PRO A C   1 
ATOM   1261  O O   . PRO A 1 159 ? 50.760  48.192  42.837  1.00 69.50  ? 162 PRO A O   1 
ATOM   1262  C CB  . PRO A 1 159 ? 53.258  49.902  43.755  1.00 48.55  ? 162 PRO A CB  1 
ATOM   1263  C CG  . PRO A 1 159 ? 54.062  50.453  42.623  1.00 52.38  ? 162 PRO A CG  1 
ATOM   1264  C CD  . PRO A 1 159 ? 53.785  49.598  41.435  1.00 57.05  ? 162 PRO A CD  1 
ATOM   1265  N N   . THR A 1 160 ? 51.401  47.328  44.819  1.00 75.77  ? 163 THR A N   1 
ATOM   1266  C CA  . THR A 1 160 ? 50.057  46.879  45.157  1.00 62.04  ? 163 THR A CA  1 
ATOM   1267  C C   . THR A 1 160 ? 49.112  48.072  45.241  1.00 69.57  ? 163 THR A C   1 
ATOM   1268  O O   . THR A 1 160 ? 49.430  49.092  45.860  1.00 59.25  ? 163 THR A O   1 
ATOM   1269  C CB  . THR A 1 160 ? 50.068  46.108  46.478  1.00 64.88  ? 163 THR A CB  1 
ATOM   1270  O OG1 . THR A 1 160 ? 50.750  44.860  46.299  1.00 63.62  ? 163 THR A OG1 1 
ATOM   1271  C CG2 . THR A 1 160 ? 48.647  45.832  46.957  1.00 70.34  ? 163 THR A CG2 1 
ATOM   1272  N N   . ILE A 1 161 ? 47.954  47.940  44.601  1.00 64.25  ? 164 ILE A N   1 
ATOM   1273  C CA  . ILE A 1 161 ? 46.962  49.006  44.535  1.00 57.11  ? 164 ILE A CA  1 
ATOM   1274  C C   . ILE A 1 161 ? 45.961  48.818  45.664  1.00 52.51  ? 164 ILE A C   1 
ATOM   1275  O O   . ILE A 1 161 ? 45.446  47.715  45.872  1.00 68.09  ? 164 ILE A O   1 
ATOM   1276  C CB  . ILE A 1 161 ? 46.256  49.009  43.171  1.00 57.29  ? 164 ILE A CB  1 
ATOM   1277  C CG1 . ILE A 1 161 ? 47.256  49.303  42.054  1.00 55.25  ? 164 ILE A CG1 1 
ATOM   1278  C CG2 . ILE A 1 161 ? 45.129  50.015  43.161  1.00 63.65  ? 164 ILE A CG2 1 
ATOM   1279  C CD1 . ILE A 1 161 ? 46.650  49.258  40.670  1.00 56.26  ? 164 ILE A CD1 1 
ATOM   1280  N N   . LYS A 1 162 ? 45.694  49.890  46.408  1.00 56.38  ? 165 LYS A N   1 
ATOM   1281  C CA  . LYS A 1 162 ? 44.656  49.900  47.438  1.00 61.20  ? 165 LYS A CA  1 
ATOM   1282  C C   . LYS A 1 162 ? 43.873  51.195  47.261  1.00 74.18  ? 165 LYS A C   1 
ATOM   1283  O O   . LYS A 1 162 ? 44.200  52.211  47.880  1.00 73.46  ? 165 LYS A O   1 
ATOM   1284  C CB  . LYS A 1 162 ? 45.252  49.778  48.837  1.00 70.28  ? 165 LYS A CB  1 
ATOM   1285  C CG  . LYS A 1 162 ? 45.374  48.343  49.335  1.00 67.30  ? 165 LYS A CG  1 
ATOM   1286  C CD  . LYS A 1 162 ? 44.758  48.175  50.722  1.00 83.38  ? 165 LYS A CD  1 
ATOM   1287  C CE  . LYS A 1 162 ? 45.647  47.328  51.633  1.00 90.32  ? 165 LYS A CE  1 
ATOM   1288  N NZ  . LYS A 1 162 ? 45.290  47.467  53.077  1.00 78.61  ? 165 LYS A NZ  1 
ATOM   1289  N N   . MET A 1 163 ? 42.843  51.151  46.415  1.00 72.63  ? 166 MET A N   1 
ATOM   1290  C CA  . MET A 1 163 ? 42.039  52.318  46.083  1.00 66.15  ? 166 MET A CA  1 
ATOM   1291  C C   . MET A 1 163 ? 40.594  52.097  46.505  1.00 68.78  ? 166 MET A C   1 
ATOM   1292  O O   . MET A 1 163 ? 40.117  50.961  46.591  1.00 71.46  ? 166 MET A O   1 
ATOM   1293  C CB  . MET A 1 163 ? 42.088  52.634  44.577  1.00 72.21  ? 166 MET A CB  1 
ATOM   1294  C CG  . MET A 1 163 ? 43.468  53.022  44.050  1.00 90.11  ? 166 MET A CG  1 
ATOM   1295  S SD  . MET A 1 163 ? 44.317  54.279  45.038  1.00 153.20 ? 166 MET A SD  1 
ATOM   1296  C CE  . MET A 1 163 ? 45.760  54.626  44.029  1.00 60.99  ? 166 MET A CE  1 
ATOM   1297  N N   . SER A 1 164 ? 39.903  53.198  46.775  1.00 62.46  ? 167 SER A N   1 
ATOM   1298  C CA  . SER A 1 164 ? 38.494  53.161  47.122  1.00 57.11  ? 167 SER A CA  1 
ATOM   1299  C C   . SER A 1 164 ? 37.810  54.351  46.470  1.00 57.35  ? 167 SER A C   1 
ATOM   1300  O O   . SER A 1 164 ? 38.448  55.361  46.171  1.00 49.38  ? 167 SER A O   1 
ATOM   1301  C CB  . SER A 1 164 ? 38.280  53.185  48.640  1.00 54.28  ? 167 SER A CB  1 
ATOM   1302  O OG  . SER A 1 164 ? 38.044  54.504  49.095  1.00 57.93  ? 167 SER A OG  1 
ATOM   1303  N N   . TYR A 1 165 ? 36.510  54.217  46.227  1.00 57.56  ? 168 TYR A N   1 
ATOM   1304  C CA  . TYR A 1 165 ? 35.729  55.299  45.643  1.00 50.62  ? 168 TYR A CA  1 
ATOM   1305  C C   . TYR A 1 165 ? 34.358  55.315  46.291  1.00 56.97  ? 168 TYR A C   1 
ATOM   1306  O O   . TYR A 1 165 ? 33.653  54.304  46.278  1.00 64.68  ? 168 TYR A O   1 
ATOM   1307  C CB  . TYR A 1 165 ? 35.605  55.156  44.124  1.00 47.34  ? 168 TYR A CB  1 
ATOM   1308  C CG  . TYR A 1 165 ? 34.550  56.066  43.534  1.00 70.10  ? 168 TYR A CG  1 
ATOM   1309  C CD1 . TYR A 1 165 ? 34.785  57.428  43.374  1.00 63.96  ? 168 TYR A CD1 1 
ATOM   1310  C CD2 . TYR A 1 165 ? 33.309  55.568  43.157  1.00 60.93  ? 168 TYR A CD2 1 
ATOM   1311  C CE1 . TYR A 1 165 ? 33.817  58.263  42.841  1.00 54.73  ? 168 TYR A CE1 1 
ATOM   1312  C CE2 . TYR A 1 165 ? 32.340  56.393  42.627  1.00 62.63  ? 168 TYR A CE2 1 
ATOM   1313  C CZ  . TYR A 1 165 ? 32.595  57.737  42.471  1.00 71.99  ? 168 TYR A CZ  1 
ATOM   1314  O OH  . TYR A 1 165 ? 31.616  58.551  41.940  1.00 78.24  ? 168 TYR A OH  1 
ATOM   1315  N N   . ASN A 1 166 ? 33.981  56.465  46.840  1.00 58.03  ? 169 ASN A N   1 
ATOM   1316  C CA  . ASN A 1 166 ? 32.689  56.640  47.486  1.00 69.62  ? 169 ASN A CA  1 
ATOM   1317  C C   . ASN A 1 166 ? 31.703  57.213  46.476  1.00 71.25  ? 169 ASN A C   1 
ATOM   1318  O O   . ASN A 1 166 ? 31.996  58.213  45.812  1.00 74.74  ? 169 ASN A O   1 
ATOM   1319  C CB  . ASN A 1 166 ? 32.833  57.560  48.701  1.00 63.72  ? 169 ASN A CB  1 
ATOM   1320  C CG  . ASN A 1 166 ? 31.541  57.721  49.485  1.00 78.20  ? 169 ASN A CG  1 
ATOM   1321  O OD1 . ASN A 1 166 ? 30.535  57.071  49.200  1.00 78.94  ? 169 ASN A OD1 1 
ATOM   1322  N ND2 . ASN A 1 166 ? 31.572  58.600  50.489  1.00 86.77  ? 169 ASN A ND2 1 
ATOM   1323  N N   . ASN A 1 167 ? 30.540  56.571  46.353  1.00 72.80  ? 170 ASN A N   1 
ATOM   1324  C CA  . ASN A 1 167 ? 29.516  56.999  45.400  1.00 70.40  ? 170 ASN A CA  1 
ATOM   1325  C C   . ASN A 1 167 ? 28.837  58.254  45.941  1.00 72.27  ? 170 ASN A C   1 
ATOM   1326  O O   . ASN A 1 167 ? 27.790  58.207  46.590  1.00 65.72  ? 170 ASN A O   1 
ATOM   1327  C CB  . ASN A 1 167 ? 28.511  55.884  45.146  1.00 60.93  ? 170 ASN A CB  1 
ATOM   1328  C CG  . ASN A 1 167 ? 27.502  56.248  44.072  1.00 72.27  ? 170 ASN A CG  1 
ATOM   1329  O OD1 . ASN A 1 167 ? 27.681  57.227  43.347  1.00 68.65  ? 170 ASN A OD1 1 
ATOM   1330  N ND2 . ASN A 1 167 ? 26.431  55.462  43.968  1.00 60.13  ? 170 ASN A ND2 1 
ATOM   1331  N N   . THR A 1 168 ? 29.458  59.405  45.657  1.00 74.50  ? 171 THR A N   1 
ATOM   1332  C CA  . THR A 1 168 ? 28.956  60.685  46.146  1.00 73.17  ? 171 THR A CA  1 
ATOM   1333  C C   . THR A 1 168 ? 27.756  61.191  45.358  1.00 73.37  ? 171 THR A C   1 
ATOM   1334  O O   . THR A 1 168 ? 27.039  62.071  45.849  1.00 76.12  ? 171 THR A O   1 
ATOM   1335  C CB  . THR A 1 168 ? 30.066  61.743  46.118  1.00 65.69  ? 171 THR A CB  1 
ATOM   1336  O OG1 . THR A 1 168 ? 30.563  61.892  44.782  1.00 70.56  ? 171 THR A OG1 1 
ATOM   1337  C CG2 . THR A 1 168 ? 31.209  61.337  47.034  1.00 70.77  ? 171 THR A CG2 1 
ATOM   1338  N N   . ASN A 1 169 ? 27.522  60.667  44.158  1.00 70.56  ? 172 ASN A N   1 
ATOM   1339  C CA  . ASN A 1 169 ? 26.338  61.045  43.402  1.00 72.43  ? 172 ASN A CA  1 
ATOM   1340  C C   . ASN A 1 169 ? 25.082  60.547  44.113  1.00 71.67  ? 172 ASN A C   1 
ATOM   1341  O O   . ASN A 1 169 ? 25.113  59.605  44.908  1.00 77.95  ? 172 ASN A O   1 
ATOM   1342  C CB  . ASN A 1 169 ? 26.398  60.484  41.979  1.00 74.08  ? 172 ASN A CB  1 
ATOM   1343  C CG  . ASN A 1 169 ? 27.798  60.531  41.388  1.00 79.37  ? 172 ASN A CG  1 
ATOM   1344  O OD1 . ASN A 1 169 ? 28.569  59.575  41.504  1.00 62.24  ? 172 ASN A OD1 1 
ATOM   1345  N ND2 . ASN A 1 169 ? 28.129  61.644  40.744  1.00 87.11  ? 172 ASN A ND2 1 
ATOM   1346  N N   . GLY A 1 170 ? 23.968  61.208  43.832  1.00 64.26  ? 173 GLY A N   1 
ATOM   1347  C CA  . GLY A 1 170 ? 22.721  60.845  44.474  1.00 79.38  ? 173 GLY A CA  1 
ATOM   1348  C C   . GLY A 1 170 ? 22.011  59.656  43.875  1.00 77.87  ? 173 GLY A C   1 
ATOM   1349  O O   . GLY A 1 170 ? 20.937  59.274  44.350  1.00 73.82  ? 173 GLY A O   1 
ATOM   1350  N N   . GLU A 1 171 ? 22.584  59.055  42.840  1.00 77.05  ? 174 GLU A N   1 
ATOM   1351  C CA  . GLU A 1 171 ? 21.965  57.962  42.111  1.00 68.93  ? 174 GLU A CA  1 
ATOM   1352  C C   . GLU A 1 171 ? 22.791  56.691  42.274  1.00 70.31  ? 174 GLU A C   1 
ATOM   1353  O O   . GLU A 1 171 ? 23.934  56.716  42.739  1.00 72.17  ? 174 GLU A O   1 
ATOM   1354  C CB  . GLU A 1 171 ? 21.819  58.321  40.626  1.00 64.87  ? 174 GLU A CB  1 
ATOM   1355  C CG  . GLU A 1 171 ? 20.461  58.896  40.265  1.00 83.04  ? 174 GLU A CG  1 
ATOM   1356  C CD  . GLU A 1 171 ? 20.484  59.720  38.986  1.00 85.52  ? 174 GLU A CD  1 
ATOM   1357  O OE1 . GLU A 1 171 ? 21.144  59.300  38.010  1.00 77.97  ? 174 GLU A OE1 1 
ATOM   1358  O OE2 . GLU A 1 171 ? 19.824  60.781  38.950  1.00 78.19  ? 174 GLU A OE2 1 
ATOM   1359  N N   . ASP A 1 172 ? 22.188  55.571  41.889  1.00 60.38  ? 175 ASP A N   1 
ATOM   1360  C CA  . ASP A 1 172 ? 22.907  54.306  41.835  1.00 52.47  ? 175 ASP A CA  1 
ATOM   1361  C C   . ASP A 1 172 ? 23.972  54.352  40.748  1.00 55.07  ? 175 ASP A C   1 
ATOM   1362  O O   . ASP A 1 172 ? 23.809  55.002  39.711  1.00 53.86  ? 175 ASP A O   1 
ATOM   1363  C CB  . ASP A 1 172 ? 21.941  53.151  41.566  1.00 66.62  ? 175 ASP A CB  1 
ATOM   1364  C CG  . ASP A 1 172 ? 21.345  52.575  42.834  1.00 66.78  ? 175 ASP A CG  1 
ATOM   1365  O OD1 . ASP A 1 172 ? 22.109  52.309  43.784  1.00 80.12  ? 175 ASP A OD1 1 
ATOM   1366  O OD2 . ASP A 1 172 ? 20.111  52.388  42.881  1.00 86.95  ? 175 ASP A OD2 1 
ATOM   1367  N N   . LEU A 1 173 ? 25.072  53.646  40.990  1.00 49.91  ? 176 LEU A N   1 
ATOM   1368  C CA  . LEU A 1 173 ? 26.201  53.624  40.074  1.00 45.22  ? 176 LEU A CA  1 
ATOM   1369  C C   . LEU A 1 173 ? 26.441  52.205  39.584  1.00 46.34  ? 176 LEU A C   1 
ATOM   1370  O O   . LEU A 1 173 ? 26.609  51.283  40.390  1.00 50.79  ? 176 LEU A O   1 
ATOM   1371  C CB  . LEU A 1 173 ? 27.461  54.165  40.752  1.00 60.93  ? 176 LEU A CB  1 
ATOM   1372  C CG  . LEU A 1 173 ? 28.453  54.896  39.850  1.00 55.64  ? 176 LEU A CG  1 
ATOM   1373  C CD1 . LEU A 1 173 ? 27.755  55.977  39.043  1.00 58.78  ? 176 LEU A CD1 1 
ATOM   1374  C CD2 . LEU A 1 173 ? 29.569  55.489  40.684  1.00 70.41  ? 176 LEU A CD2 1 
ATOM   1375  N N   . LEU A 1 174 ? 26.465  52.035  38.267  1.00 45.36  ? 177 LEU A N   1 
ATOM   1376  C CA  . LEU A 1 174 ? 26.877  50.781  37.650  1.00 48.42  ? 177 LEU A CA  1 
ATOM   1377  C C   . LEU A 1 174 ? 28.369  50.877  37.348  1.00 55.27  ? 177 LEU A C   1 
ATOM   1378  O O   . LEU A 1 174 ? 28.791  51.695  36.523  1.00 54.02  ? 177 LEU A O   1 
ATOM   1379  C CB  . LEU A 1 174 ? 26.065  50.512  36.386  1.00 49.14  ? 177 LEU A CB  1 
ATOM   1380  C CG  . LEU A 1 174 ? 26.554  49.377  35.484  1.00 54.37  ? 177 LEU A CG  1 
ATOM   1381  C CD1 . LEU A 1 174 ? 26.290  48.018  36.121  1.00 46.25  ? 177 LEU A CD1 1 
ATOM   1382  C CD2 . LEU A 1 174 ? 25.902  49.469  34.116  1.00 48.92  ? 177 LEU A CD2 1 
ATOM   1383  N N   . ILE A 1 175 ? 29.167  50.048  38.016  1.00 55.94  ? 178 ILE A N   1 
ATOM   1384  C CA  . ILE A 1 175 ? 30.620  50.077  37.904  1.00 48.03  ? 178 ILE A CA  1 
ATOM   1385  C C   . ILE A 1 175 ? 31.081  48.805  37.206  1.00 49.83  ? 178 ILE A C   1 
ATOM   1386  O O   . ILE A 1 175 ? 30.668  47.700  37.578  1.00 53.22  ? 178 ILE A O   1 
ATOM   1387  C CB  . ILE A 1 175 ? 31.286  50.229  39.282  1.00 54.93  ? 178 ILE A CB  1 
ATOM   1388  C CG1 . ILE A 1 175 ? 30.965  51.605  39.869  1.00 63.11  ? 178 ILE A CG1 1 
ATOM   1389  C CG2 . ILE A 1 175 ? 32.793  50.039  39.177  1.00 54.55  ? 178 ILE A CG2 1 
ATOM   1390  C CD1 . ILE A 1 175 ? 31.307  51.741  41.333  1.00 60.76  ? 178 ILE A CD1 1 
ATOM   1391  N N   . LEU A 1 176 ? 31.930  48.964  36.194  1.00 45.95  ? 179 LEU A N   1 
ATOM   1392  C CA  . LEU A 1 176 ? 32.485  47.865  35.418  1.00 41.17  ? 179 LEU A CA  1 
ATOM   1393  C C   . LEU A 1 176 ? 33.988  47.772  35.665  1.00 58.12  ? 179 LEU A C   1 
ATOM   1394  O O   . LEU A 1 176 ? 34.685  48.792  35.673  1.00 55.18  ? 179 LEU A O   1 
ATOM   1395  C CB  . LEU A 1 176 ? 32.214  48.079  33.927  1.00 49.34  ? 179 LEU A CB  1 
ATOM   1396  C CG  . LEU A 1 176 ? 30.878  47.601  33.348  1.00 49.10  ? 179 LEU A CG  1 
ATOM   1397  C CD1 . LEU A 1 176 ? 30.958  47.389  31.857  1.00 59.79  ? 179 LEU A CD1 1 
ATOM   1398  C CD2 . LEU A 1 176 ? 30.481  46.317  33.990  1.00 52.50  ? 179 LEU A CD2 1 
ATOM   1399  N N   . TRP A 1 177 ? 34.486  46.552  35.872  1.00 50.34  ? 180 TRP A N   1 
ATOM   1400  C CA  . TRP A 1 177 ? 35.922  46.302  35.969  1.00 44.26  ? 180 TRP A CA  1 
ATOM   1401  C C   . TRP A 1 177 ? 36.213  44.915  35.412  1.00 49.18  ? 180 TRP A C   1 
ATOM   1402  O O   . TRP A 1 177 ? 35.307  44.192  34.992  1.00 52.51  ? 180 TRP A O   1 
ATOM   1403  C CB  . TRP A 1 177 ? 36.422  46.430  37.409  1.00 46.05  ? 180 TRP A CB  1 
ATOM   1404  C CG  . TRP A 1 177 ? 35.975  45.312  38.295  1.00 53.39  ? 180 TRP A CG  1 
ATOM   1405  C CD1 . TRP A 1 177 ? 36.666  44.174  38.594  1.00 47.59  ? 180 TRP A CD1 1 
ATOM   1406  C CD2 . TRP A 1 177 ? 34.729  45.221  38.997  1.00 46.74  ? 180 TRP A CD2 1 
ATOM   1407  N NE1 . TRP A 1 177 ? 35.930  43.383  39.444  1.00 45.29  ? 180 TRP A NE1 1 
ATOM   1408  C CE2 . TRP A 1 177 ? 34.737  44.005  39.708  1.00 47.43  ? 180 TRP A CE2 1 
ATOM   1409  C CE3 . TRP A 1 177 ? 33.609  46.053  39.097  1.00 46.92  ? 180 TRP A CE3 1 
ATOM   1410  C CZ2 . TRP A 1 177 ? 33.669  43.598  40.505  1.00 45.29  ? 180 TRP A CZ2 1 
ATOM   1411  C CZ3 . TRP A 1 177 ? 32.551  45.648  39.890  1.00 46.40  ? 180 TRP A CZ3 1 
ATOM   1412  C CH2 . TRP A 1 177 ? 32.588  44.430  40.583  1.00 46.31  ? 180 TRP A CH2 1 
ATOM   1413  N N   . GLY A 1 178 ? 37.489  44.537  35.420  1.00 50.00  ? 181 GLY A N   1 
ATOM   1414  C CA  . GLY A 1 178 ? 37.852  43.249  34.858  1.00 46.34  ? 181 GLY A CA  1 
ATOM   1415  C C   . GLY A 1 178 ? 39.234  42.798  35.270  1.00 50.21  ? 181 GLY A C   1 
ATOM   1416  O O   . GLY A 1 178 ? 39.990  43.524  35.919  1.00 45.14  ? 181 GLY A O   1 
ATOM   1417  N N   . ILE A 1 179 ? 39.548  41.564  34.883  1.00 51.15  ? 182 ILE A N   1 
ATOM   1418  C CA  . ILE A 1 179 ? 40.853  40.961  35.114  1.00 45.08  ? 182 ILE A CA  1 
ATOM   1419  C C   . ILE A 1 179 ? 41.332  40.359  33.800  1.00 53.14  ? 182 ILE A C   1 
ATOM   1420  O O   . ILE A 1 179 ? 40.526  39.862  33.003  1.00 50.25  ? 182 ILE A O   1 
ATOM   1421  C CB  . ILE A 1 179 ? 40.808  39.894  36.232  1.00 52.25  ? 182 ILE A CB  1 
ATOM   1422  C CG1 . ILE A 1 179 ? 42.227  39.474  36.628  1.00 45.83  ? 182 ILE A CG1 1 
ATOM   1423  C CG2 . ILE A 1 179 ? 39.973  38.683  35.805  1.00 43.39  ? 182 ILE A CG2 1 
ATOM   1424  C CD1 . ILE A 1 179 ? 42.285  38.289  37.563  1.00 49.95  ? 182 ILE A CD1 1 
ATOM   1425  N N   . HIS A 1 180 ? 42.641  40.425  33.566  1.00 47.90  ? 183 HIS A N   1 
ATOM   1426  C CA  . HIS A 1 180 ? 43.255  39.959  32.329  1.00 53.13  ? 183 HIS A CA  1 
ATOM   1427  C C   . HIS A 1 180 ? 43.983  38.647  32.579  1.00 54.42  ? 183 HIS A C   1 
ATOM   1428  O O   . HIS A 1 180 ? 44.759  38.537  33.534  1.00 56.84  ? 183 HIS A O   1 
ATOM   1429  C CB  . HIS A 1 180 ? 44.233  41.003  31.782  1.00 53.71  ? 183 HIS A CB  1 
ATOM   1430  C CG  . HIS A 1 180 ? 45.089  40.499  30.662  1.00 49.34  ? 183 HIS A CG  1 
ATOM   1431  N ND1 . HIS A 1 180 ? 46.465  40.479  30.728  1.00 56.75  ? 183 HIS A ND1 1 
ATOM   1432  C CD2 . HIS A 1 180 ? 44.763  39.999  29.446  1.00 44.15  ? 183 HIS A CD2 1 
ATOM   1433  C CE1 . HIS A 1 180 ? 46.950  39.985  29.602  1.00 61.88  ? 183 HIS A CE1 1 
ATOM   1434  N NE2 . HIS A 1 180 ? 45.938  39.689  28.806  1.00 47.08  ? 183 HIS A NE2 1 
ATOM   1435  N N   . HIS A 1 181 ? 43.741  37.660  31.718  1.00 53.70  ? 184 HIS A N   1 
ATOM   1436  C CA  . HIS A 1 181 ? 44.405  36.363  31.797  1.00 48.15  ? 184 HIS A CA  1 
ATOM   1437  C C   . HIS A 1 181 ? 45.524  36.311  30.761  1.00 54.33  ? 184 HIS A C   1 
ATOM   1438  O O   . HIS A 1 181 ? 45.263  36.405  29.557  1.00 52.16  ? 184 HIS A O   1 
ATOM   1439  C CB  . HIS A 1 181 ? 43.409  35.225  31.567  1.00 50.76  ? 184 HIS A CB  1 
ATOM   1440  C CG  . HIS A 1 181 ? 42.233  35.250  32.496  1.00 57.92  ? 184 HIS A CG  1 
ATOM   1441  N ND1 . HIS A 1 181 ? 42.306  34.815  33.802  1.00 57.65  ? 184 HIS A ND1 1 
ATOM   1442  C CD2 . HIS A 1 181 ? 40.955  35.657  32.307  1.00 53.96  ? 184 HIS A CD2 1 
ATOM   1443  C CE1 . HIS A 1 181 ? 41.125  34.953  34.378  1.00 50.19  ? 184 HIS A CE1 1 
ATOM   1444  N NE2 . HIS A 1 181 ? 40.288  35.465  33.493  1.00 47.96  ? 184 HIS A NE2 1 
ATOM   1445  N N   . SER A 1 182 ? 46.764  36.157  31.229  1.00 55.02  ? 185 SER A N   1 
ATOM   1446  C CA  . SER A 1 182 ? 47.912  36.103  30.334  1.00 58.40  ? 185 SER A CA  1 
ATOM   1447  C C   . SER A 1 182 ? 48.135  34.679  29.821  1.00 60.79  ? 185 SER A C   1 
ATOM   1448  O O   . SER A 1 182 ? 47.568  33.704  30.323  1.00 60.08  ? 185 SER A O   1 
ATOM   1449  C CB  . SER A 1 182 ? 49.169  36.627  31.032  1.00 51.24  ? 185 SER A CB  1 
ATOM   1450  O OG  . SER A 1 182 ? 49.197  36.260  32.398  1.00 57.27  ? 185 SER A OG  1 
ATOM   1451  N N   . ASN A 1 183 ? 48.989  34.564  28.805  1.00 64.92  ? 186 ASN A N   1 
ATOM   1452  C CA  . ASN A 1 183 ? 49.179  33.299  28.107  1.00 63.02  ? 186 ASN A CA  1 
ATOM   1453  C C   . ASN A 1 183 ? 50.339  32.467  28.640  1.00 65.22  ? 186 ASN A C   1 
ATOM   1454  O O   . ASN A 1 183 ? 50.347  31.248  28.431  1.00 61.75  ? 186 ASN A O   1 
ATOM   1455  C CB  . ASN A 1 183 ? 49.394  33.553  26.613  1.00 65.68  ? 186 ASN A CB  1 
ATOM   1456  C CG  . ASN A 1 183 ? 48.483  34.631  26.078  1.00 55.39  ? 186 ASN A CG  1 
ATOM   1457  O OD1 . ASN A 1 183 ? 47.271  34.568  26.254  1.00 73.26  ? 186 ASN A OD1 1 
ATOM   1458  N ND2 . ASN A 1 183 ? 49.060  35.630  25.421  1.00 58.43  ? 186 ASN A ND2 1 
ATOM   1459  N N   . ASN A 1 184 ? 51.315  33.081  29.303  1.00 56.72  ? 187 ASN A N   1 
ATOM   1460  C CA  . ASN A 1 184 ? 52.467  32.340  29.801  1.00 60.26  ? 187 ASN A CA  1 
ATOM   1461  C C   . ASN A 1 184 ? 53.131  33.146  30.908  1.00 61.58  ? 187 ASN A C   1 
ATOM   1462  O O   . ASN A 1 184 ? 52.858  34.336  31.090  1.00 65.13  ? 187 ASN A O   1 
ATOM   1463  C CB  . ASN A 1 184 ? 53.460  32.031  28.682  1.00 56.14  ? 187 ASN A CB  1 
ATOM   1464  C CG  . ASN A 1 184 ? 53.865  33.265  27.909  1.00 62.49  ? 187 ASN A CG  1 
ATOM   1465  O OD1 . ASN A 1 184 ? 54.566  34.136  28.428  1.00 58.95  ? 187 ASN A OD1 1 
ATOM   1466  N ND2 . ASN A 1 184 ? 53.429  33.346  26.656  1.00 59.25  ? 187 ASN A ND2 1 
ATOM   1467  N N   . ALA A 1 185 ? 54.018  32.474  31.645  1.00 65.06  ? 188 ALA A N   1 
ATOM   1468  C CA  . ALA A 1 185 ? 54.676  33.108  32.784  1.00 64.68  ? 188 ALA A CA  1 
ATOM   1469  C C   . ALA A 1 185 ? 55.528  34.292  32.347  1.00 62.66  ? 188 ALA A C   1 
ATOM   1470  O O   . ALA A 1 185 ? 55.592  35.311  33.045  1.00 59.56  ? 188 ALA A O   1 
ATOM   1471  C CB  . ALA A 1 185 ? 55.525  32.083  33.535  1.00 65.87  ? 188 ALA A CB  1 
ATOM   1472  N N   . ALA A 1 186 ? 56.203  34.172  31.200  1.00 67.94  ? 189 ALA A N   1 
ATOM   1473  C CA  . ALA A 1 186 ? 57.058  35.255  30.723  1.00 68.56  ? 189 ALA A CA  1 
ATOM   1474  C C   . ALA A 1 186 ? 56.246  36.510  30.421  1.00 63.00  ? 189 ALA A C   1 
ATOM   1475  O O   . ALA A 1 186 ? 56.617  37.618  30.826  1.00 66.16  ? 189 ALA A O   1 
ATOM   1476  C CB  . ALA A 1 186 ? 57.835  34.803  29.487  1.00 59.88  ? 189 ALA A CB  1 
ATOM   1477  N N   . GLU A 1 187 ? 55.121  36.353  29.720  1.00 66.52  ? 190 GLU A N   1 
ATOM   1478  C CA  . GLU A 1 187 ? 54.282  37.503  29.395  1.00 59.89  ? 190 GLU A CA  1 
ATOM   1479  C C   . GLU A 1 187 ? 53.694  38.132  30.653  1.00 65.59  ? 190 GLU A C   1 
ATOM   1480  O O   . GLU A 1 187 ? 53.549  39.359  30.732  1.00 59.19  ? 190 GLU A O   1 
ATOM   1481  C CB  . GLU A 1 187 ? 53.176  37.083  28.428  1.00 65.86  ? 190 GLU A CB  1 
ATOM   1482  C CG  . GLU A 1 187 ? 51.868  37.840  28.596  1.00 79.71  ? 190 GLU A CG  1 
ATOM   1483  C CD  . GLU A 1 187 ? 50.912  37.609  27.446  1.00 78.89  ? 190 GLU A CD  1 
ATOM   1484  O OE1 . GLU A 1 187 ? 51.380  37.514  26.290  1.00 83.62  ? 190 GLU A OE1 1 
ATOM   1485  O OE2 . GLU A 1 187 ? 49.692  37.517  27.701  1.00 76.10  ? 190 GLU A OE2 1 
ATOM   1486  N N   . GLN A 1 188 ? 53.361  37.307  31.651  1.00 62.67  ? 191 GLN A N   1 
ATOM   1487  C CA  . GLN A 1 188 ? 52.855  37.836  32.914  1.00 59.02  ? 191 GLN A CA  1 
ATOM   1488  C C   . GLN A 1 188 ? 53.867  38.773  33.561  1.00 58.80  ? 191 GLN A C   1 
ATOM   1489  O O   . GLN A 1 188 ? 53.511  39.867  34.015  1.00 62.21  ? 191 GLN A O   1 
ATOM   1490  C CB  . GLN A 1 188 ? 52.503  36.685  33.859  1.00 55.79  ? 191 GLN A CB  1 
ATOM   1491  C CG  . GLN A 1 188 ? 52.134  37.119  35.271  1.00 55.75  ? 191 GLN A CG  1 
ATOM   1492  C CD  . GLN A 1 188 ? 50.814  37.870  35.325  1.00 57.65  ? 191 GLN A CD  1 
ATOM   1493  O OE1 . GLN A 1 188 ? 49.960  37.717  34.448  1.00 50.84  ? 191 GLN A OE1 1 
ATOM   1494  N NE2 . GLN A 1 188 ? 50.636  38.679  36.364  1.00 46.63  ? 191 GLN A NE2 1 
ATOM   1495  N N   . ILE A 1 189 ? 55.138  38.366  33.600  1.00 59.27  ? 192 ILE A N   1 
ATOM   1496  C CA  . ILE A 1 189 ? 56.184  39.231  34.137  1.00 64.82  ? 192 ILE A CA  1 
ATOM   1497  C C   . ILE A 1 189 ? 56.419  40.429  33.220  1.00 64.98  ? 192 ILE A C   1 
ATOM   1498  O O   . ILE A 1 189 ? 56.696  41.540  33.694  1.00 54.82  ? 192 ILE A O   1 
ATOM   1499  C CB  . ILE A 1 189 ? 57.470  38.416  34.374  1.00 66.66  ? 192 ILE A CB  1 
ATOM   1500  C CG1 . ILE A 1 189 ? 57.315  37.549  35.627  1.00 65.59  ? 192 ILE A CG1 1 
ATOM   1501  C CG2 . ILE A 1 189 ? 58.684  39.327  34.511  1.00 61.78  ? 192 ILE A CG2 1 
ATOM   1502  C CD1 . ILE A 1 189 ? 58.005  36.210  35.536  1.00 63.51  ? 192 ILE A CD1 1 
ATOM   1503  N N   . ASN A 1 190 ? 56.294  40.234  31.903  1.00 54.82  ? 193 ASN A N   1 
ATOM   1504  C CA  . ASN A 1 190 ? 56.522  41.324  30.958  1.00 68.75  ? 193 ASN A CA  1 
ATOM   1505  C C   . ASN A 1 190 ? 55.571  42.492  31.184  1.00 66.95  ? 193 ASN A C   1 
ATOM   1506  O O   . ASN A 1 190 ? 55.915  43.637  30.870  1.00 60.36  ? 193 ASN A O   1 
ATOM   1507  C CB  . ASN A 1 190 ? 56.377  40.816  29.523  1.00 60.00  ? 193 ASN A CB  1 
ATOM   1508  C CG  . ASN A 1 190 ? 57.528  39.931  29.095  1.00 84.84  ? 193 ASN A CG  1 
ATOM   1509  O OD1 . ASN A 1 190 ? 58.539  39.817  29.796  1.00 91.16  ? 193 ASN A OD1 1 
ATOM   1510  N ND2 . ASN A 1 190 ? 57.380  39.292  27.940  1.00 83.84  ? 193 ASN A ND2 1 
ATOM   1511  N N   . LEU A 1 191 ? 54.378  42.231  31.717  1.00 68.77  ? 194 LEU A N   1 
ATOM   1512  C CA  . LEU A 1 191 ? 53.356  43.258  31.888  1.00 64.83  ? 194 LEU A CA  1 
ATOM   1513  C C   . LEU A 1 191 ? 53.183  43.725  33.325  1.00 60.80  ? 194 LEU A C   1 
ATOM   1514  O O   . LEU A 1 191 ? 52.953  44.916  33.552  1.00 52.08  ? 194 LEU A O   1 
ATOM   1515  C CB  . LEU A 1 191 ? 52.008  42.750  31.361  1.00 70.08  ? 194 LEU A CB  1 
ATOM   1516  C CG  . LEU A 1 191 ? 51.709  43.063  29.894  1.00 59.48  ? 194 LEU A CG  1 
ATOM   1517  C CD1 . LEU A 1 191 ? 52.378  42.053  28.980  1.00 67.34  ? 194 LEU A CD1 1 
ATOM   1518  C CD2 . LEU A 1 191 ? 50.214  43.089  29.656  1.00 70.10  ? 194 LEU A CD2 1 
ATOM   1519  N N   . TYR A 1 192 ? 53.291  42.825  34.306  1.00 62.97  ? 195 TYR A N   1 
ATOM   1520  C CA  . TYR A 1 192 ? 53.023  43.166  35.698  1.00 60.98  ? 195 TYR A CA  1 
ATOM   1521  C C   . TYR A 1 192 ? 54.167  42.860  36.656  1.00 73.77  ? 195 TYR A C   1 
ATOM   1522  O O   . TYR A 1 192 ? 54.095  43.281  37.817  1.00 69.28  ? 195 TYR A O   1 
ATOM   1523  C CB  . TYR A 1 192 ? 51.758  42.441  36.186  1.00 64.31  ? 195 TYR A CB  1 
ATOM   1524  C CG  . TYR A 1 192 ? 50.649  42.443  35.161  1.00 59.25  ? 195 TYR A CG  1 
ATOM   1525  C CD1 . TYR A 1 192 ? 49.871  43.578  34.958  1.00 62.49  ? 195 TYR A CD1 1 
ATOM   1526  C CD2 . TYR A 1 192 ? 50.390  41.322  34.382  1.00 47.96  ? 195 TYR A CD2 1 
ATOM   1527  C CE1 . TYR A 1 192 ? 48.856  43.592  34.015  1.00 55.52  ? 195 TYR A CE1 1 
ATOM   1528  C CE2 . TYR A 1 192 ? 49.374  41.324  33.437  1.00 51.57  ? 195 TYR A CE2 1 
ATOM   1529  C CZ  . TYR A 1 192 ? 48.612  42.465  33.258  1.00 58.49  ? 195 TYR A CZ  1 
ATOM   1530  O OH  . TYR A 1 192 ? 47.608  42.484  32.317  1.00 43.23  ? 195 TYR A OH  1 
ATOM   1531  N N   . LYS A 1 193 ? 55.182  42.101  36.230  1.00 73.71  ? 196 LYS A N   1 
ATOM   1532  C CA  . LYS A 1 193 ? 56.413  41.858  36.979  1.00 69.07  ? 196 LYS A CA  1 
ATOM   1533  C C   . LYS A 1 193 ? 56.176  40.936  38.175  1.00 62.38  ? 196 LYS A C   1 
ATOM   1534  O O   . LYS A 1 193 ? 57.125  40.384  38.740  1.00 75.98  ? 196 LYS A O   1 
ATOM   1535  C CB  . LYS A 1 193 ? 57.029  43.203  37.403  1.00 71.24  ? 196 LYS A CB  1 
ATOM   1536  C CG  . LYS A 1 193 ? 57.940  43.193  38.629  1.00 82.58  ? 196 LYS A CG  1 
ATOM   1537  C CD  . LYS A 1 193 ? 59.351  42.745  38.272  1.00 82.40  ? 196 LYS A CD  1 
ATOM   1538  C CE  . LYS A 1 193 ? 59.989  41.959  39.407  1.00 73.45  ? 196 LYS A CE  1 
ATOM   1539  N NZ  . LYS A 1 193 ? 61.215  41.248  38.954  1.00 69.54  ? 196 LYS A NZ  1 
ATOM   1540  N N   . ASN A 1 194 ? 54.916  40.673  38.506  1.00 68.49  ? 197 ASN A N   1 
ATOM   1541  C CA  . ASN A 1 194 ? 54.588  39.816  39.636  1.00 61.11  ? 197 ASN A CA  1 
ATOM   1542  C C   . ASN A 1 194 ? 54.047  38.493  39.121  1.00 66.29  ? 197 ASN A C   1 
ATOM   1543  O O   . ASN A 1 194 ? 53.043  38.482  38.393  1.00 70.51  ? 197 ASN A O   1 
ATOM   1544  C CB  . ASN A 1 194 ? 53.577  40.498  40.553  1.00 53.72  ? 197 ASN A CB  1 
ATOM   1545  C CG  . ASN A 1 194 ? 54.071  41.842  41.055  1.00 62.02  ? 197 ASN A CG  1 
ATOM   1546  O OD1 . ASN A 1 194 ? 55.272  42.103  41.072  1.00 65.33  ? 197 ASN A OD1 1 
ATOM   1547  N ND2 . ASN A 1 194 ? 53.145  42.708  41.455  1.00 58.74  ? 197 ASN A ND2 1 
ATOM   1548  N N   . PRO A 1 195 ? 54.688  37.365  39.438  1.00 76.04  ? 198 PRO A N   1 
ATOM   1549  C CA  . PRO A 1 195 ? 54.237  36.088  38.862  1.00 69.82  ? 198 PRO A CA  1 
ATOM   1550  C C   . PRO A 1 195 ? 52.867  35.651  39.349  1.00 65.23  ? 198 PRO A C   1 
ATOM   1551  O O   . PRO A 1 195 ? 52.143  34.984  38.601  1.00 61.97  ? 198 PRO A O   1 
ATOM   1552  C CB  . PRO A 1 195 ? 55.332  35.099  39.287  1.00 65.27  ? 198 PRO A CB  1 
ATOM   1553  C CG  . PRO A 1 195 ? 55.988  35.714  40.473  1.00 77.99  ? 198 PRO A CG  1 
ATOM   1554  C CD  . PRO A 1 195 ? 55.725  37.193  40.471  1.00 66.02  ? 198 PRO A CD  1 
ATOM   1555  N N   . THR A 1 196 ? 52.490  35.995  40.578  1.00 69.72  ? 199 THR A N   1 
ATOM   1556  C CA  . THR A 1 196 ? 51.222  35.575  41.167  1.00 63.13  ? 199 THR A CA  1 
ATOM   1557  C C   . THR A 1 196 ? 50.461  36.824  41.587  1.00 58.98  ? 199 THR A C   1 
ATOM   1558  O O   . THR A 1 196 ? 50.867  37.521  42.524  1.00 59.70  ? 199 THR A O   1 
ATOM   1559  C CB  . THR A 1 196 ? 51.450  34.642  42.357  1.00 69.76  ? 199 THR A CB  1 
ATOM   1560  O OG1 . THR A 1 196 ? 52.096  33.444  41.908  1.00 70.26  ? 199 THR A OG1 1 
ATOM   1561  C CG2 . THR A 1 196 ? 50.125  34.281  43.021  1.00 72.13  ? 199 THR A CG2 1 
ATOM   1562  N N   . THR A 1 197 ? 49.364  37.109  40.898  1.00 67.92  ? 200 THR A N   1 
ATOM   1563  C CA  . THR A 1 197 ? 48.584  38.314  41.136  1.00 62.97  ? 200 THR A CA  1 
ATOM   1564  C C   . THR A 1 197 ? 47.143  37.944  41.464  1.00 59.18  ? 200 THR A C   1 
ATOM   1565  O O   . THR A 1 197 ? 46.770  36.769  41.502  1.00 59.43  ? 200 THR A O   1 
ATOM   1566  C CB  . THR A 1 197 ? 48.637  39.251  39.927  1.00 54.03  ? 200 THR A CB  1 
ATOM   1567  O OG1 . THR A 1 197 ? 48.129  38.567  38.778  1.00 50.31  ? 200 THR A OG1 1 
ATOM   1568  C CG2 . THR A 1 197 ? 50.067  39.695  39.654  1.00 55.51  ? 200 THR A CG2 1 
ATOM   1569  N N   . TYR A 1 198 ? 46.333  38.974  41.689  1.00 60.04  ? 201 TYR A N   1 
ATOM   1570  C CA  . TYR A 1 198 ? 44.928  38.808  42.036  1.00 55.64  ? 201 TYR A CA  1 
ATOM   1571  C C   . TYR A 1 198 ? 44.250  40.171  41.971  1.00 64.05  ? 201 TYR A C   1 
ATOM   1572  O O   . TYR A 1 198 ? 44.910  41.213  41.911  1.00 58.56  ? 201 TYR A O   1 
ATOM   1573  C CB  . TYR A 1 198 ? 44.772  38.190  43.425  1.00 60.07  ? 201 TYR A CB  1 
ATOM   1574  C CG  . TYR A 1 198 ? 45.176  39.139  44.523  1.00 61.88  ? 201 TYR A CG  1 
ATOM   1575  C CD1 . TYR A 1 198 ? 46.509  39.282  44.883  1.00 61.73  ? 201 TYR A CD1 1 
ATOM   1576  C CD2 . TYR A 1 198 ? 44.228  39.900  45.193  1.00 63.78  ? 201 TYR A CD2 1 
ATOM   1577  C CE1 . TYR A 1 198 ? 46.887  40.152  45.884  1.00 63.07  ? 201 TYR A CE1 1 
ATOM   1578  C CE2 . TYR A 1 198 ? 44.593  40.770  46.192  1.00 59.17  ? 201 TYR A CE2 1 
ATOM   1579  C CZ  . TYR A 1 198 ? 45.925  40.894  46.536  1.00 74.98  ? 201 TYR A CZ  1 
ATOM   1580  O OH  . TYR A 1 198 ? 46.298  41.765  47.534  1.00 73.22  ? 201 TYR A OH  1 
ATOM   1581  N N   . VAL A 1 199 ? 42.917  40.148  41.979  1.00 66.57  ? 202 VAL A N   1 
ATOM   1582  C CA  . VAL A 1 199 ? 42.098  41.353  42.067  1.00 62.21  ? 202 VAL A CA  1 
ATOM   1583  C C   . VAL A 1 199 ? 41.052  41.141  43.154  1.00 57.30  ? 202 VAL A C   1 
ATOM   1584  O O   . VAL A 1 199 ? 40.302  40.159  43.113  1.00 58.67  ? 202 VAL A O   1 
ATOM   1585  C CB  . VAL A 1 199 ? 41.413  41.695  40.729  1.00 55.49  ? 202 VAL A CB  1 
ATOM   1586  C CG1 . VAL A 1 199 ? 40.639  42.995  40.862  1.00 58.21  ? 202 VAL A CG1 1 
ATOM   1587  C CG2 . VAL A 1 199 ? 42.437  41.805  39.602  1.00 52.62  ? 202 VAL A CG2 1 
ATOM   1588  N N   . SER A 1 200 ? 40.999  42.060  44.118  1.00 59.90  ? 203 SER A N   1 
ATOM   1589  C CA  . SER A 1 200 ? 40.043  42.007  45.219  1.00 55.84  ? 203 SER A CA  1 
ATOM   1590  C C   . SER A 1 200 ? 39.128  43.219  45.133  1.00 61.62  ? 203 SER A C   1 
ATOM   1591  O O   . SER A 1 200 ? 39.602  44.360  45.093  1.00 55.80  ? 203 SER A O   1 
ATOM   1592  C CB  . SER A 1 200 ? 40.754  41.970  46.573  1.00 49.27  ? 203 SER A CB  1 
ATOM   1593  O OG  . SER A 1 200 ? 41.090  40.638  46.928  1.00 67.08  ? 203 SER A OG  1 
ATOM   1594  N N   . VAL A 1 201 ? 37.821  42.973  45.110  1.00 56.42  ? 204 VAL A N   1 
ATOM   1595  C CA  . VAL A 1 201 ? 36.817  44.025  45.017  1.00 56.93  ? 204 VAL A CA  1 
ATOM   1596  C C   . VAL A 1 201 ? 35.840  43.857  46.171  1.00 50.62  ? 204 VAL A C   1 
ATOM   1597  O O   . VAL A 1 201 ? 35.378  42.743  46.443  1.00 55.62  ? 204 VAL A O   1 
ATOM   1598  C CB  . VAL A 1 201 ? 36.083  43.992  43.665  1.00 59.92  ? 204 VAL A CB  1 
ATOM   1599  C CG1 . VAL A 1 201 ? 35.406  45.329  43.410  1.00 49.03  ? 204 VAL A CG1 1 
ATOM   1600  C CG2 . VAL A 1 201 ? 37.059  43.649  42.535  1.00 48.11  ? 204 VAL A CG2 1 
ATOM   1601  N N   . GLY A 1 202 ? 35.532  44.958  46.847  1.00 53.36  ? 205 GLY A N   1 
ATOM   1602  C CA  . GLY A 1 202 ? 34.653  44.896  47.995  1.00 54.44  ? 205 GLY A CA  1 
ATOM   1603  C C   . GLY A 1 202 ? 33.723  46.083  48.124  1.00 65.03  ? 205 GLY A C   1 
ATOM   1604  O O   . GLY A 1 202 ? 34.118  47.224  47.869  1.00 53.36  ? 205 GLY A O   1 
ATOM   1605  N N   . THR A 1 203 ? 32.478  45.813  48.521  1.00 63.99  ? 206 THR A N   1 
ATOM   1606  C CA  . THR A 1 203 ? 31.472  46.833  48.801  1.00 50.40  ? 206 THR A CA  1 
ATOM   1607  C C   . THR A 1 203 ? 30.750  46.430  50.079  1.00 54.41  ? 206 THR A C   1 
ATOM   1608  O O   . THR A 1 203 ? 31.220  45.579  50.837  1.00 61.50  ? 206 THR A O   1 
ATOM   1609  C CB  . THR A 1 203 ? 30.470  47.000  47.646  1.00 59.91  ? 206 THR A CB  1 
ATOM   1610  O OG1 . THR A 1 203 ? 29.609  45.853  47.583  1.00 65.50  ? 206 THR A OG1 1 
ATOM   1611  C CG2 . THR A 1 203 ? 31.184  47.171  46.316  1.00 59.63  ? 206 THR A CG2 1 
ATOM   1612  N N   . SER A 1 204 ? 29.597  47.052  50.325  1.00 65.18  ? 207 SER A N   1 
ATOM   1613  C CA  . SER A 1 204 ? 28.773  46.630  51.451  1.00 64.39  ? 207 SER A CA  1 
ATOM   1614  C C   . SER A 1 204 ? 28.184  45.239  51.245  1.00 59.12  ? 207 SER A C   1 
ATOM   1615  O O   . SER A 1 204 ? 27.836  44.575  52.229  1.00 53.61  ? 207 SER A O   1 
ATOM   1616  C CB  . SER A 1 204 ? 27.653  47.642  51.691  1.00 57.82  ? 207 SER A CB  1 
ATOM   1617  O OG  . SER A 1 204 ? 26.904  47.854  50.510  1.00 74.05  ? 207 SER A OG  1 
ATOM   1618  N N   . THR A 1 205 ? 28.072  44.783  49.996  1.00 65.46  ? 208 THR A N   1 
ATOM   1619  C CA  . THR A 1 205 ? 27.533  43.467  49.675  1.00 64.39  ? 208 THR A CA  1 
ATOM   1620  C C   . THR A 1 205 ? 28.497  42.579  48.900  1.00 55.36  ? 208 THR A C   1 
ATOM   1621  O O   . THR A 1 205 ? 28.409  41.356  49.012  1.00 62.32  ? 208 THR A O   1 
ATOM   1622  C CB  . THR A 1 205 ? 26.226  43.601  48.865  1.00 62.39  ? 208 THR A CB  1 
ATOM   1623  O OG1 . THR A 1 205 ? 26.451  44.410  47.702  1.00 59.98  ? 208 THR A OG1 1 
ATOM   1624  C CG2 . THR A 1 205 ? 25.132  44.242  49.712  1.00 39.61  ? 208 THR A CG2 1 
ATOM   1625  N N   . LEU A 1 206 ? 29.421  43.152  48.135  1.00 58.78  ? 209 LEU A N   1 
ATOM   1626  C CA  . LEU A 1 206 ? 30.265  42.376  47.237  1.00 54.58  ? 209 LEU A CA  1 
ATOM   1627  C C   . LEU A 1 206 ? 31.588  42.029  47.913  1.00 58.13  ? 209 LEU A C   1 
ATOM   1628  O O   . LEU A 1 206 ? 32.234  42.890  48.518  1.00 56.82  ? 209 LEU A O   1 
ATOM   1629  C CB  . LEU A 1 206 ? 30.509  43.153  45.944  1.00 52.95  ? 209 LEU A CB  1 
ATOM   1630  C CG  . LEU A 1 206 ? 31.579  42.637  44.984  1.00 55.09  ? 209 LEU A CG  1 
ATOM   1631  C CD1 . LEU A 1 206 ? 31.001  41.583  44.054  1.00 52.70  ? 209 LEU A CD1 1 
ATOM   1632  C CD2 . LEU A 1 206 ? 32.145  43.797  44.185  1.00 57.01  ? 209 LEU A CD2 1 
ATOM   1633  N N   . ASN A 1 207 ? 31.976  40.757  47.824  1.00 54.21  ? 210 ASN A N   1 
ATOM   1634  C CA  . ASN A 1 207 ? 33.246  40.263  48.356  1.00 47.54  ? 210 ASN A CA  1 
ATOM   1635  C C   . ASN A 1 207 ? 33.841  39.360  47.280  1.00 55.79  ? 210 ASN A C   1 
ATOM   1636  O O   . ASN A 1 207 ? 33.556  38.161  47.237  1.00 69.18  ? 210 ASN A O   1 
ATOM   1637  C CB  . ASN A 1 207 ? 33.051  39.529  49.674  1.00 47.37  ? 210 ASN A CB  1 
ATOM   1638  C CG  . ASN A 1 207 ? 34.349  39.355  50.439  1.00 59.20  ? 210 ASN A CG  1 
ATOM   1639  O OD1 . ASN A 1 207 ? 35.297  40.122  50.263  1.00 61.29  ? 210 ASN A OD1 1 
ATOM   1640  N ND2 . ASN A 1 207 ? 34.401  38.337  51.289  1.00 57.07  ? 210 ASN A ND2 1 
ATOM   1641  N N   . GLN A 1 208 ? 34.669  39.936  46.414  1.00 52.84  ? 211 GLN A N   1 
ATOM   1642  C CA  . GLN A 1 208 ? 35.155  39.260  45.221  1.00 55.68  ? 211 GLN A CA  1 
ATOM   1643  C C   . GLN A 1 208 ? 36.673  39.160  45.255  1.00 62.76  ? 211 GLN A C   1 
ATOM   1644  O O   . GLN A 1 208 ? 37.358  40.074  45.726  1.00 60.02  ? 211 GLN A O   1 
ATOM   1645  C CB  . GLN A 1 208 ? 34.705  40.003  43.954  1.00 50.99  ? 211 GLN A CB  1 
ATOM   1646  C CG  . GLN A 1 208 ? 35.000  39.270  42.654  1.00 54.24  ? 211 GLN A CG  1 
ATOM   1647  C CD  . GLN A 1 208 ? 34.599  40.073  41.428  1.00 62.05  ? 211 GLN A CD  1 
ATOM   1648  O OE1 . GLN A 1 208 ? 35.406  40.816  40.865  1.00 53.85  ? 211 GLN A OE1 1 
ATOM   1649  N NE2 . GLN A 1 208 ? 33.344  39.926  41.007  1.00 62.81  ? 211 GLN A NE2 1 
ATOM   1650  N N   . ARG A 1 209 ? 37.194  38.046  44.750  1.00 57.28  ? 212 ARG A N   1 
ATOM   1651  C CA  . ARG A 1 209 ? 38.637  37.848  44.664  1.00 53.69  ? 212 ARG A CA  1 
ATOM   1652  C C   . ARG A 1 209 ? 38.920  37.023  43.419  1.00 52.62  ? 212 ARG A C   1 
ATOM   1653  O O   . ARG A 1 209 ? 38.624  35.825  43.390  1.00 59.97  ? 212 ARG A O   1 
ATOM   1654  C CB  . ARG A 1 209 ? 39.170  37.158  45.911  1.00 50.69  ? 212 ARG A CB  1 
ATOM   1655  C CG  . ARG A 1 209 ? 40.643  37.391  46.154  1.00 56.93  ? 212 ARG A CG  1 
ATOM   1656  C CD  . ARG A 1 209 ? 41.312  36.133  46.664  1.00 58.16  ? 212 ARG A CD  1 
ATOM   1657  N NE  . ARG A 1 209 ? 42.737  36.111  46.356  1.00 71.59  ? 212 ARG A NE  1 
ATOM   1658  C CZ  . ARG A 1 209 ? 43.648  36.850  46.974  1.00 73.26  ? 212 ARG A CZ  1 
ATOM   1659  N NH1 . ARG A 1 209 ? 43.315  37.699  47.934  1.00 64.32  ? 212 ARG A NH1 1 
ATOM   1660  N NH2 . ARG A 1 209 ? 44.925  36.732  46.622  1.00 77.45  ? 212 ARG A NH2 1 
ATOM   1661  N N   . LEU A 1 210 ? 39.488  37.656  42.400  1.00 53.28  ? 213 LEU A N   1 
ATOM   1662  C CA  . LEU A 1 210 ? 39.792  36.993  41.142  1.00 56.77  ? 213 LEU A CA  1 
ATOM   1663  C C   . LEU A 1 210 ? 41.283  36.705  41.037  1.00 58.28  ? 213 LEU A C   1 
ATOM   1664  O O   . LEU A 1 210 ? 42.117  37.452  41.552  1.00 55.63  ? 213 LEU A O   1 
ATOM   1665  C CB  . LEU A 1 210 ? 39.356  37.845  39.951  1.00 49.57  ? 213 LEU A CB  1 
ATOM   1666  C CG  . LEU A 1 210 ? 38.018  38.564  40.073  1.00 51.13  ? 213 LEU A CG  1 
ATOM   1667  C CD1 . LEU A 1 210 ? 37.945  39.672  39.039  1.00 53.94  ? 213 LEU A CD1 1 
ATOM   1668  C CD2 . LEU A 1 210 ? 36.868  37.579  39.903  1.00 54.37  ? 213 LEU A CD2 1 
ATOM   1669  N N   . VAL A 1 211 ? 41.608  35.615  40.350  1.00 59.34  ? 214 VAL A N   1 
ATOM   1670  C CA  . VAL A 1 211 ? 42.993  35.213  40.127  1.00 56.96  ? 214 VAL A CA  1 
ATOM   1671  C C   . VAL A 1 211 ? 43.174  34.916  38.642  1.00 58.30  ? 214 VAL A C   1 
ATOM   1672  O O   . VAL A 1 211 ? 42.323  34.250  38.034  1.00 61.78  ? 214 VAL A O   1 
ATOM   1673  C CB  . VAL A 1 211 ? 43.367  34.001  40.997  1.00 60.34  ? 214 VAL A CB  1 
ATOM   1674  C CG1 . VAL A 1 211 ? 44.506  33.216  40.369  1.00 46.52  ? 214 VAL A CG1 1 
ATOM   1675  C CG2 . VAL A 1 211 ? 43.735  34.454  42.402  1.00 53.52  ? 214 VAL A CG2 1 
ATOM   1676  N N   . PRO A 1 212 ? 44.245  35.401  38.016  1.00 55.14  ? 215 PRO A N   1 
ATOM   1677  C CA  . PRO A 1 212 ? 44.457  35.119  36.593  1.00 50.47  ? 215 PRO A CA  1 
ATOM   1678  C C   . PRO A 1 212 ? 44.702  33.639  36.339  1.00 48.79  ? 215 PRO A C   1 
ATOM   1679  O O   . PRO A 1 212 ? 45.284  32.930  37.163  1.00 57.61  ? 215 PRO A O   1 
ATOM   1680  C CB  . PRO A 1 212 ? 45.694  35.959  36.243  1.00 49.15  ? 215 PRO A CB  1 
ATOM   1681  C CG  . PRO A 1 212 ? 45.807  36.969  37.346  1.00 44.62  ? 215 PRO A CG  1 
ATOM   1682  C CD  . PRO A 1 212 ? 45.274  36.296  38.567  1.00 49.70  ? 215 PRO A CD  1 
ATOM   1683  N N   . LYS A 1 213 ? 44.258  33.183  35.174  1.00 40.77  ? 216 LYS A N   1 
ATOM   1684  C CA  . LYS A 1 213 ? 44.430  31.804  34.730  1.00 44.24  ? 216 LYS A CA  1 
ATOM   1685  C C   . LYS A 1 213 ? 45.416  31.824  33.568  1.00 52.30  ? 216 LYS A C   1 
ATOM   1686  O O   . LYS A 1 213 ? 45.036  32.085  32.422  1.00 45.03  ? 216 LYS A O   1 
ATOM   1687  C CB  . LYS A 1 213 ? 43.088  31.188  34.337  1.00 48.13  ? 216 LYS A CB  1 
ATOM   1688  C CG  . LYS A 1 213 ? 42.115  31.074  35.509  1.00 47.53  ? 216 LYS A CG  1 
ATOM   1689  C CD  . LYS A 1 213 ? 40.848  30.354  35.122  1.00 50.71  ? 216 LYS A CD  1 
ATOM   1690  C CE  . LYS A 1 213 ? 39.719  31.338  34.881  1.00 57.70  ? 216 LYS A CE  1 
ATOM   1691  N NZ  . LYS A 1 213 ? 38.491  30.620  34.469  1.00 54.50  ? 216 LYS A NZ  1 
ATOM   1692  N N   . ILE A 1 214 ? 46.686  31.563  33.874  1.00 63.20  ? 217 ILE A N   1 
ATOM   1693  C CA  . ILE A 1 214 ? 47.767  31.664  32.899  1.00 56.05  ? 217 ILE A CA  1 
ATOM   1694  C C   . ILE A 1 214 ? 47.912  30.299  32.236  1.00 57.53  ? 217 ILE A C   1 
ATOM   1695  O O   . ILE A 1 214 ? 48.544  29.394  32.779  1.00 67.66  ? 217 ILE A O   1 
ATOM   1696  C CB  . ILE A 1 214 ? 49.073  32.121  33.548  1.00 63.89  ? 217 ILE A CB  1 
ATOM   1697  C CG1 . ILE A 1 214 ? 48.805  33.240  34.553  1.00 62.94  ? 217 ILE A CG1 1 
ATOM   1698  C CG2 . ILE A 1 214 ? 50.055  32.589  32.488  1.00 60.00  ? 217 ILE A CG2 1 
ATOM   1699  C CD1 . ILE A 1 214 ? 50.040  33.704  35.290  1.00 65.13  ? 217 ILE A CD1 1 
ATOM   1700  N N   . ALA A 1 215 ? 47.333  30.157  31.048  1.00 54.65  ? 218 ALA A N   1 
ATOM   1701  C CA  . ALA A 1 215 ? 47.344  28.886  30.342  1.00 59.08  ? 218 ALA A CA  1 
ATOM   1702  C C   . ALA A 1 215 ? 47.178  29.157  28.855  1.00 57.01  ? 218 ALA A C   1 
ATOM   1703  O O   . ALA A 1 215 ? 46.798  30.254  28.440  1.00 59.86  ? 218 ALA A O   1 
ATOM   1704  C CB  . ALA A 1 215 ? 46.248  27.949  30.860  1.00 58.40  ? 218 ALA A CB  1 
ATOM   1705  N N   . THR A 1 216 ? 47.473  28.137  28.056  1.00 54.95  ? 219 THR A N   1 
ATOM   1706  C CA  . THR A 1 216 ? 47.355  28.257  26.610  1.00 44.37  ? 219 THR A CA  1 
ATOM   1707  C C   . THR A 1 216 ? 45.890  28.264  26.187  1.00 56.71  ? 219 THR A C   1 
ATOM   1708  O O   . THR A 1 216 ? 45.068  27.515  26.721  1.00 55.05  ? 219 THR A O   1 
ATOM   1709  C CB  . THR A 1 216 ? 48.102  27.110  25.928  1.00 44.04  ? 219 THR A CB  1 
ATOM   1710  O OG1 . THR A 1 216 ? 49.443  27.046  26.434  1.00 56.42  ? 219 THR A OG1 1 
ATOM   1711  C CG2 . THR A 1 216 ? 48.145  27.314  24.426  1.00 46.76  ? 219 THR A CG2 1 
ATOM   1712  N N   . ARG A 1 217 ? 45.566  29.119  25.218  1.00 54.57  ? 220 ARG A N   1 
ATOM   1713  C CA  . ARG A 1 217 ? 44.214  29.222  24.689  1.00 54.67  ? 220 ARG A CA  1 
ATOM   1714  C C   . ARG A 1 217 ? 44.282  29.415  23.180  1.00 58.22  ? 220 ARG A C   1 
ATOM   1715  O O   . ARG A 1 217 ? 45.323  29.774  22.629  1.00 57.76  ? 220 ARG A O   1 
ATOM   1716  C CB  . ARG A 1 217 ? 43.438  30.374  25.346  1.00 50.68  ? 220 ARG A CB  1 
ATOM   1717  C CG  . ARG A 1 217 ? 42.923  30.042  26.739  1.00 54.87  ? 220 ARG A CG  1 
ATOM   1718  C CD  . ARG A 1 217 ? 42.544  31.286  27.525  1.00 44.83  ? 220 ARG A CD  1 
ATOM   1719  N NE  . ARG A 1 217 ? 43.654  32.223  27.665  1.00 48.06  ? 220 ARG A NE  1 
ATOM   1720  C CZ  . ARG A 1 217 ? 44.327  32.435  28.788  1.00 54.78  ? 220 ARG A CZ  1 
ATOM   1721  N NH1 . ARG A 1 217 ? 44.067  31.751  29.892  1.00 47.47  ? 220 ARG A NH1 1 
ATOM   1722  N NH2 . ARG A 1 217 ? 45.282  33.360  28.808  1.00 54.64  ? 220 ARG A NH2 1 
ATOM   1723  N N   . SER A 1 218 ? 43.162  29.148  22.512  1.00 44.96  ? 221 SER A N   1 
ATOM   1724  C CA  . SER A 1 218 ? 43.073  29.378  21.078  1.00 48.73  ? 221 SER A CA  1 
ATOM   1725  C C   . SER A 1 218 ? 42.916  30.866  20.789  1.00 61.35  ? 221 SER A C   1 
ATOM   1726  O O   . SER A 1 218 ? 42.368  31.622  21.597  1.00 60.15  ? 221 SER A O   1 
ATOM   1727  C CB  . SER A 1 218 ? 41.897  28.610  20.477  1.00 54.37  ? 221 SER A CB  1 
ATOM   1728  O OG  . SER A 1 218 ? 42.006  27.224  20.747  1.00 67.27  ? 221 SER A OG  1 
ATOM   1729  N N   . GLN A 1 219 ? 43.393  31.284  19.620  1.00 69.69  ? 222 GLN A N   1 
ATOM   1730  C CA  . GLN A 1 219 ? 43.385  32.698  19.271  1.00 64.38  ? 222 GLN A CA  1 
ATOM   1731  C C   . GLN A 1 219 ? 41.977  33.163  18.906  1.00 55.80  ? 222 GLN A C   1 
ATOM   1732  O O   . GLN A 1 219 ? 41.263  32.496  18.151  1.00 57.83  ? 222 GLN A O   1 
ATOM   1733  C CB  . GLN A 1 219 ? 44.367  32.975  18.128  1.00 66.27  ? 222 GLN A CB  1 
ATOM   1734  C CG  . GLN A 1 219 ? 43.933  32.508  16.743  1.00 79.72  ? 222 GLN A CG  1 
ATOM   1735  C CD  . GLN A 1 219 ? 43.589  33.662  15.819  1.00 87.22  ? 222 GLN A CD  1 
ATOM   1736  O OE1 . GLN A 1 219 ? 43.174  34.728  16.271  1.00 82.61  ? 222 GLN A OE1 1 
ATOM   1737  N NE2 . GLN A 1 219 ? 43.766  33.456  14.517  1.00 85.54  ? 222 GLN A NE2 1 
ATOM   1738  N N   . VAL A 1 220 ? 41.573  34.296  19.476  1.00 58.54  ? 223 VAL A N   1 
ATOM   1739  C CA  . VAL A 1 220 ? 40.333  34.979  19.123  1.00 58.05  ? 223 VAL A CA  1 
ATOM   1740  C C   . VAL A 1 220 ? 40.677  36.442  18.881  1.00 62.97  ? 223 VAL A C   1 
ATOM   1741  O O   . VAL A 1 220 ? 41.245  37.100  19.762  1.00 56.11  ? 223 VAL A O   1 
ATOM   1742  C CB  . VAL A 1 220 ? 39.259  34.842  20.216  1.00 59.59  ? 223 VAL A CB  1 
ATOM   1743  C CG1 . VAL A 1 220 ? 38.028  35.679  19.866  1.00 44.13  ? 223 VAL A CG1 1 
ATOM   1744  C CG2 . VAL A 1 220 ? 38.878  33.385  20.403  1.00 46.25  ? 223 VAL A CG2 1 
ATOM   1745  N N   . ASN A 1 221 ? 40.333  36.949  17.693  1.00 61.03  ? 224 ASN A N   1 
ATOM   1746  C CA  . ASN A 1 221 ? 40.741  38.289  17.257  1.00 63.70  ? 224 ASN A CA  1 
ATOM   1747  C C   . ASN A 1 221 ? 42.256  38.450  17.343  1.00 66.20  ? 224 ASN A C   1 
ATOM   1748  O O   . ASN A 1 221 ? 42.763  39.489  17.772  1.00 66.05  ? 224 ASN A O   1 
ATOM   1749  C CB  . ASN A 1 221 ? 40.037  39.388  18.058  1.00 53.33  ? 224 ASN A CB  1 
ATOM   1750  C CG  . ASN A 1 221 ? 38.530  39.279  17.998  1.00 63.64  ? 224 ASN A CG  1 
ATOM   1751  O OD1 . ASN A 1 221 ? 37.968  38.796  17.015  1.00 61.17  ? 224 ASN A OD1 1 
ATOM   1752  N ND2 . ASN A 1 221 ? 37.863  39.730  19.059  1.00 56.97  ? 224 ASN A ND2 1 
ATOM   1753  N N   . GLY A 1 222 ? 42.984  37.404  16.953  1.00 62.57  ? 225 GLY A N   1 
ATOM   1754  C CA  . GLY A 1 222 ? 44.433  37.429  16.973  1.00 63.94  ? 225 GLY A CA  1 
ATOM   1755  C C   . GLY A 1 222 ? 45.067  37.253  18.333  1.00 63.37  ? 225 GLY A C   1 
ATOM   1756  O O   . GLY A 1 222 ? 46.297  37.337  18.439  1.00 67.84  ? 225 GLY A O   1 
ATOM   1757  N N   . LEU A 1 223 ? 44.281  36.992  19.375  1.00 60.92  ? 226 LEU A N   1 
ATOM   1758  C CA  . LEU A 1 223 ? 44.771  37.016  20.744  1.00 59.06  ? 226 LEU A CA  1 
ATOM   1759  C C   . LEU A 1 223 ? 44.452  35.713  21.458  1.00 65.40  ? 226 LEU A C   1 
ATOM   1760  O O   . LEU A 1 223 ? 43.330  35.202  21.370  1.00 63.75  ? 226 LEU A O   1 
ATOM   1761  C CB  . LEU A 1 223 ? 44.151  38.177  21.516  1.00 50.24  ? 226 LEU A CB  1 
ATOM   1762  C CG  . LEU A 1 223 ? 44.658  39.568  21.149  1.00 57.53  ? 226 LEU A CG  1 
ATOM   1763  C CD1 . LEU A 1 223 ? 44.433  40.513  22.310  1.00 62.65  ? 226 LEU A CD1 1 
ATOM   1764  C CD2 . LEU A 1 223 ? 46.132  39.517  20.781  1.00 58.00  ? 226 LEU A CD2 1 
ATOM   1765  N N   . GLN A 1 224 ? 45.446  35.184  22.170  1.00 46.92  ? 227 GLN A N   1 
ATOM   1766  C CA  . GLN A 1 224 ? 45.231  34.075  23.087  1.00 46.89  ? 227 GLN A CA  1 
ATOM   1767  C C   . GLN A 1 224 ? 44.859  34.539  24.489  1.00 54.41  ? 227 GLN A C   1 
ATOM   1768  O O   . GLN A 1 224 ? 44.390  33.724  25.293  1.00 49.05  ? 227 GLN A O   1 
ATOM   1769  C CB  . GLN A 1 224 ? 46.477  33.190  23.161  1.00 49.44  ? 227 GLN A CB  1 
ATOM   1770  C CG  . GLN A 1 224 ? 46.796  32.442  21.881  1.00 55.17  ? 227 GLN A CG  1 
ATOM   1771  C CD  . GLN A 1 224 ? 48.088  31.653  21.982  1.00 54.95  ? 227 GLN A CD  1 
ATOM   1772  O OE1 . GLN A 1 224 ? 49.141  32.201  22.308  1.00 65.60  ? 227 GLN A OE1 1 
ATOM   1773  N NE2 . GLN A 1 224 ? 48.014  30.358  21.704  1.00 58.34  ? 227 GLN A NE2 1 
ATOM   1774  N N   . GLY A 1 225 ? 45.066  35.819  24.805  1.00 52.96  ? 228 GLY A N   1 
ATOM   1775  C CA  . GLY A 1 225 ? 44.671  36.333  26.095  1.00 53.80  ? 228 GLY A CA  1 
ATOM   1776  C C   . GLY A 1 225 ? 43.173  36.536  26.197  1.00 49.03  ? 228 GLY A C   1 
ATOM   1777  O O   . GLY A 1 225 ? 42.453  36.541  25.201  1.00 48.07  ? 228 GLY A O   1 
ATOM   1778  N N   . ARG A 1 226 ? 42.703  36.691  27.434  1.00 45.79  ? 229 ARG A N   1 
ATOM   1779  C CA  . ARG A 1 226 ? 41.296  36.938  27.708  1.00 48.74  ? 229 ARG A CA  1 
ATOM   1780  C C   . ARG A 1 226 ? 41.177  38.011  28.776  1.00 45.56  ? 229 ARG A C   1 
ATOM   1781  O O   . ARG A 1 226 ? 42.064  38.177  29.617  1.00 48.31  ? 229 ARG A O   1 
ATOM   1782  C CB  . ARG A 1 226 ? 40.560  35.677  28.185  1.00 36.12  ? 229 ARG A CB  1 
ATOM   1783  C CG  . ARG A 1 226 ? 40.610  34.521  27.213  1.00 36.26  ? 229 ARG A CG  1 
ATOM   1784  C CD  . ARG A 1 226 ? 39.863  34.840  25.945  1.00 47.49  ? 229 ARG A CD  1 
ATOM   1785  N NE  . ARG A 1 226 ? 39.820  33.694  25.047  1.00 53.44  ? 229 ARG A NE  1 
ATOM   1786  C CZ  . ARG A 1 226 ? 40.649  33.503  24.031  1.00 49.76  ? 229 ARG A CZ  1 
ATOM   1787  N NH1 . ARG A 1 226 ? 41.616  34.363  23.756  1.00 45.31  ? 229 ARG A NH1 1 
ATOM   1788  N NH2 . ARG A 1 226 ? 40.497  32.426  23.265  1.00 51.29  ? 229 ARG A NH2 1 
ATOM   1789  N N   . MET A 1 227 ? 40.060  38.732  28.742  1.00 51.16  ? 230 MET A N   1 
ATOM   1790  C CA  . MET A 1 227 ? 39.716  39.679  29.793  1.00 52.51  ? 230 MET A CA  1 
ATOM   1791  C C   . MET A 1 227 ? 38.315  39.357  30.286  1.00 50.95  ? 230 MET A C   1 
ATOM   1792  O O   . MET A 1 227 ? 37.356  39.398  29.507  1.00 47.98  ? 230 MET A O   1 
ATOM   1793  C CB  . MET A 1 227 ? 39.802  41.120  29.293  1.00 43.86  ? 230 MET A CB  1 
ATOM   1794  C CG  . MET A 1 227 ? 41.120  41.794  29.622  1.00 52.27  ? 230 MET A CG  1 
ATOM   1795  S SD  . MET A 1 227 ? 41.351  43.292  28.661  1.00 53.59  ? 230 MET A SD  1 
ATOM   1796  C CE  . MET A 1 227 ? 43.139  43.424  28.621  1.00 46.07  ? 230 MET A CE  1 
ATOM   1797  N N   . ASP A 1 228 ? 38.204  39.021  31.567  1.00 46.56  ? 231 ASP A N   1 
ATOM   1798  C CA  . ASP A 1 228 ? 36.926  38.711  32.194  1.00 51.53  ? 231 ASP A CA  1 
ATOM   1799  C C   . ASP A 1 228 ? 36.453  39.938  32.959  1.00 51.85  ? 231 ASP A C   1 
ATOM   1800  O O   . ASP A 1 228 ? 37.169  40.440  33.832  1.00 50.26  ? 231 ASP A O   1 
ATOM   1801  C CB  . ASP A 1 228 ? 37.048  37.509  33.131  1.00 51.83  ? 231 ASP A CB  1 
ATOM   1802  C CG  . ASP A 1 228 ? 37.153  36.192  32.383  1.00 51.27  ? 231 ASP A CG  1 
ATOM   1803  O OD1 . ASP A 1 228 ? 36.929  36.180  31.152  1.00 50.18  ? 231 ASP A OD1 1 
ATOM   1804  O OD2 . ASP A 1 228 ? 37.465  35.167  33.029  1.00 59.11  ? 231 ASP A OD2 1 
ATOM   1805  N N   . PHE A 1 229 ? 35.245  40.401  32.647  1.00 57.88  ? 232 PHE A N   1 
ATOM   1806  C CA  . PHE A 1 229 ? 34.695  41.624  33.209  1.00 45.47  ? 232 PHE A CA  1 
ATOM   1807  C C   . PHE A 1 229 ? 33.544  41.311  34.157  1.00 39.68  ? 232 PHE A C   1 
ATOM   1808  O O   . PHE A 1 229 ? 32.801  40.347  33.963  1.00 50.56  ? 232 PHE A O   1 
ATOM   1809  C CB  . PHE A 1 229 ? 34.210  42.563  32.102  1.00 51.50  ? 232 PHE A CB  1 
ATOM   1810  C CG  . PHE A 1 229 ? 35.320  43.211  31.329  1.00 41.39  ? 232 PHE A CG  1 
ATOM   1811  C CD1 . PHE A 1 229 ? 36.047  44.253  31.879  1.00 40.69  ? 232 PHE A CD1 1 
ATOM   1812  C CD2 . PHE A 1 229 ? 35.636  42.777  30.054  1.00 40.41  ? 232 PHE A CD2 1 
ATOM   1813  C CE1 . PHE A 1 229 ? 37.068  44.855  31.169  1.00 40.71  ? 232 PHE A CE1 1 
ATOM   1814  C CE2 . PHE A 1 229 ? 36.653  43.372  29.337  1.00 41.40  ? 232 PHE A CE2 1 
ATOM   1815  C CZ  . PHE A 1 229 ? 37.371  44.414  29.895  1.00 48.42  ? 232 PHE A CZ  1 
ATOM   1816  N N   . PHE A 1 230 ? 33.410  42.146  35.186  1.00 42.52  ? 233 PHE A N   1 
ATOM   1817  C CA  . PHE A 1 230 ? 32.419  41.968  36.237  1.00 43.77  ? 233 PHE A CA  1 
ATOM   1818  C C   . PHE A 1 230 ? 31.782  43.319  36.539  1.00 50.19  ? 233 PHE A C   1 
ATOM   1819  O O   . PHE A 1 230 ? 32.253  44.366  36.082  1.00 48.84  ? 233 PHE A O   1 
ATOM   1820  C CB  . PHE A 1 230 ? 33.045  41.362  37.503  1.00 44.69  ? 233 PHE A CB  1 
ATOM   1821  C CG  . PHE A 1 230 ? 33.689  40.016  37.283  1.00 50.35  ? 233 PHE A CG  1 
ATOM   1822  C CD1 . PHE A 1 230 ? 34.960  39.915  36.728  1.00 47.63  ? 233 PHE A CD1 1 
ATOM   1823  C CD2 . PHE A 1 230 ? 33.031  38.852  37.645  1.00 44.74  ? 233 PHE A CD2 1 
ATOM   1824  C CE1 . PHE A 1 230 ? 35.552  38.682  36.525  1.00 47.64  ? 233 PHE A CE1 1 
ATOM   1825  C CE2 . PHE A 1 230 ? 33.620  37.611  37.444  1.00 48.04  ? 233 PHE A CE2 1 
ATOM   1826  C CZ  . PHE A 1 230 ? 34.882  37.528  36.886  1.00 50.89  ? 233 PHE A CZ  1 
ATOM   1827  N N   . TRP A 1 231 ? 30.699  43.297  37.316  1.00 47.50  ? 234 TRP A N   1 
ATOM   1828  C CA  . TRP A 1 231 ? 29.956  44.521  37.582  1.00 45.92  ? 234 TRP A CA  1 
ATOM   1829  C C   . TRP A 1 231 ? 29.287  44.455  38.945  1.00 48.42  ? 234 TRP A C   1 
ATOM   1830  O O   . TRP A 1 231 ? 29.207  43.401  39.579  1.00 61.02  ? 234 TRP A O   1 
ATOM   1831  C CB  . TRP A 1 231 ? 28.906  44.797  36.506  1.00 44.12  ? 234 TRP A CB  1 
ATOM   1832  C CG  . TRP A 1 231 ? 27.878  43.721  36.317  1.00 50.98  ? 234 TRP A CG  1 
ATOM   1833  C CD1 . TRP A 1 231 ? 28.033  42.544  35.642  1.00 45.46  ? 234 TRP A CD1 1 
ATOM   1834  C CD2 . TRP A 1 231 ? 26.526  43.740  36.785  1.00 50.37  ? 234 TRP A CD2 1 
ATOM   1835  N NE1 . TRP A 1 231 ? 26.863  41.826  35.669  1.00 54.29  ? 234 TRP A NE1 1 
ATOM   1836  C CE2 . TRP A 1 231 ? 25.922  42.538  36.366  1.00 58.75  ? 234 TRP A CE2 1 
ATOM   1837  C CE3 . TRP A 1 231 ? 25.768  44.654  37.523  1.00 44.95  ? 234 TRP A CE3 1 
ATOM   1838  C CZ2 . TRP A 1 231 ? 24.598  42.227  36.662  1.00 43.55  ? 234 TRP A CZ2 1 
ATOM   1839  C CZ3 . TRP A 1 231 ? 24.456  44.344  37.814  1.00 51.88  ? 234 TRP A CZ3 1 
ATOM   1840  C CH2 . TRP A 1 231 ? 23.883  43.140  37.384  1.00 48.32  ? 234 TRP A CH2 1 
ATOM   1841  N N   . THR A 1 232 ? 28.820  45.619  39.388  1.00 41.98  ? 235 THR A N   1 
ATOM   1842  C CA  . THR A 1 232 ? 28.065  45.756  40.623  1.00 44.35  ? 235 THR A CA  1 
ATOM   1843  C C   . THR A 1 232 ? 27.300  47.070  40.566  1.00 52.25  ? 235 THR A C   1 
ATOM   1844  O O   . THR A 1 232 ? 27.614  47.960  39.768  1.00 48.68  ? 235 THR A O   1 
ATOM   1845  C CB  . THR A 1 232 ? 28.974  45.716  41.857  1.00 44.98  ? 235 THR A CB  1 
ATOM   1846  O OG1 . THR A 1 232 ? 28.198  45.387  43.015  1.00 62.48  ? 235 THR A OG1 1 
ATOM   1847  C CG2 . THR A 1 232 ? 29.635  47.077  42.076  1.00 53.79  ? 235 THR A CG2 1 
ATOM   1848  N N   . ILE A 1 233 ? 26.289  47.178  41.416  1.00 54.52  ? 236 ILE A N   1 
ATOM   1849  C CA  . ILE A 1 233 ? 25.515  48.403  41.563  1.00 52.13  ? 236 ILE A CA  1 
ATOM   1850  C C   . ILE A 1 233 ? 25.918  49.014  42.899  1.00 55.95  ? 236 ILE A C   1 
ATOM   1851  O O   . ILE A 1 233 ? 25.497  48.545  43.964  1.00 56.82  ? 236 ILE A O   1 
ATOM   1852  C CB  . ILE A 1 233 ? 24.007  48.147  41.492  1.00 58.04  ? 236 ILE A CB  1 
ATOM   1853  C CG1 . ILE A 1 233 ? 23.666  47.295  40.267  1.00 52.97  ? 236 ILE A CG1 1 
ATOM   1854  C CG2 . ILE A 1 233 ? 23.254  49.467  41.449  1.00 53.62  ? 236 ILE A CG2 1 
ATOM   1855  C CD1 . ILE A 1 233 ? 23.830  48.019  38.950  1.00 51.31  ? 236 ILE A CD1 1 
ATOM   1856  N N   . LEU A 1 234 ? 26.743  50.058  42.849  1.00 52.49  ? 237 LEU A N   1 
ATOM   1857  C CA  . LEU A 1 234 ? 27.174  50.757  44.055  1.00 53.33  ? 237 LEU A CA  1 
ATOM   1858  C C   . LEU A 1 234 ? 26.068  51.713  44.482  1.00 58.17  ? 237 LEU A C   1 
ATOM   1859  O O   . LEU A 1 234 ? 25.743  52.663  43.760  1.00 51.06  ? 237 LEU A O   1 
ATOM   1860  C CB  . LEU A 1 234 ? 28.481  51.503  43.808  1.00 60.94  ? 237 LEU A CB  1 
ATOM   1861  C CG  . LEU A 1 234 ? 29.191  52.017  45.061  1.00 60.46  ? 237 LEU A CG  1 
ATOM   1862  C CD1 . LEU A 1 234 ? 29.547  50.868  45.991  1.00 58.05  ? 237 LEU A CD1 1 
ATOM   1863  C CD2 . LEU A 1 234 ? 30.432  52.807  44.685  1.00 57.68  ? 237 LEU A CD2 1 
ATOM   1864  N N   . LYS A 1 235 ? 25.480  51.451  45.645  1.00 56.63  ? 238 LYS A N   1 
ATOM   1865  C CA  . LYS A 1 235 ? 24.389  52.271  46.134  1.00 60.61  ? 238 LYS A CA  1 
ATOM   1866  C C   . LYS A 1 235 ? 24.915  53.633  46.582  1.00 64.53  ? 238 LYS A C   1 
ATOM   1867  O O   . LYS A 1 235 ? 26.103  53.780  46.881  1.00 64.32  ? 238 LYS A O   1 
ATOM   1868  C CB  . LYS A 1 235 ? 23.673  51.565  47.283  1.00 60.88  ? 238 LYS A CB  1 
ATOM   1869  C CG  . LYS A 1 235 ? 22.882  50.336  46.847  1.00 68.70  ? 238 LYS A CG  1 
ATOM   1870  C CD  . LYS A 1 235 ? 21.836  49.939  47.884  1.00 80.90  ? 238 LYS A CD  1 
ATOM   1871  C CE  . LYS A 1 235 ? 20.436  50.368  47.465  1.00 75.89  ? 238 LYS A CE  1 
ATOM   1872  N NZ  . LYS A 1 235 ? 19.389  49.812  48.372  1.00 75.45  ? 238 LYS A NZ  1 
ATOM   1873  N N   . PRO A 1 236 ? 24.054  54.650  46.612  1.00 65.40  ? 239 PRO A N   1 
ATOM   1874  C CA  . PRO A 1 236 ? 24.507  55.978  47.051  1.00 62.98  ? 239 PRO A CA  1 
ATOM   1875  C C   . PRO A 1 236 ? 25.112  55.926  48.447  1.00 72.34  ? 239 PRO A C   1 
ATOM   1876  O O   . PRO A 1 236 ? 24.640  55.201  49.325  1.00 61.00  ? 239 PRO A O   1 
ATOM   1877  C CB  . PRO A 1 236 ? 23.230  56.827  47.024  1.00 64.93  ? 239 PRO A CB  1 
ATOM   1878  C CG  . PRO A 1 236 ? 22.181  56.012  46.331  1.00 62.75  ? 239 PRO A CG  1 
ATOM   1879  C CD  . PRO A 1 236 ? 22.750  54.691  45.931  1.00 52.30  ? 239 PRO A CD  1 
ATOM   1880  N N   . ASN A 1 237 ? 26.188  56.698  48.629  1.00 68.29  ? 240 ASN A N   1 
ATOM   1881  C CA  . ASN A 1 237 ? 26.950  56.789  49.875  1.00 57.39  ? 240 ASN A CA  1 
ATOM   1882  C C   . ASN A 1 237 ? 27.620  55.471  50.251  1.00 69.80  ? 240 ASN A C   1 
ATOM   1883  O O   . ASN A 1 237 ? 28.003  55.270  51.410  1.00 71.91  ? 240 ASN A O   1 
ATOM   1884  C CB  . ASN A 1 237 ? 26.076  57.298  51.026  1.00 69.02  ? 240 ASN A CB  1 
ATOM   1885  C CG  . ASN A 1 237 ? 25.652  58.743  50.831  1.00 81.06  ? 240 ASN A CG  1 
ATOM   1886  O OD1 . ASN A 1 237 ? 26.442  59.574  50.383  1.00 69.69  ? 240 ASN A OD1 1 
ATOM   1887  N ND2 . ASN A 1 237 ? 24.398  59.046  51.153  1.00 70.23  ? 240 ASN A ND2 1 
ATOM   1888  N N   . ASP A 1 238 ? 27.783  54.566  49.293  1.00 61.85  ? 241 ASP A N   1 
ATOM   1889  C CA  . ASP A 1 238 ? 28.564  53.357  49.488  1.00 68.33  ? 241 ASP A CA  1 
ATOM   1890  C C   . ASP A 1 238 ? 29.894  53.500  48.762  1.00 65.90  ? 241 ASP A C   1 
ATOM   1891  O O   . ASP A 1 238 ? 30.013  54.251  47.789  1.00 61.46  ? 241 ASP A O   1 
ATOM   1892  C CB  . ASP A 1 238 ? 27.817  52.113  48.989  1.00 58.09  ? 241 ASP A CB  1 
ATOM   1893  C CG  . ASP A 1 238 ? 28.383  50.821  49.563  1.00 74.72  ? 241 ASP A CG  1 
ATOM   1894  O OD1 . ASP A 1 238 ? 29.127  50.885  50.565  1.00 71.09  ? 241 ASP A OD1 1 
ATOM   1895  O OD2 . ASP A 1 238 ? 28.092  49.740  49.008  1.00 74.03  ? 241 ASP A OD2 1 
ATOM   1896  N N   . ALA A 1 239 ? 30.900  52.785  49.250  1.00 56.52  ? 242 ALA A N   1 
ATOM   1897  C CA  . ALA A 1 239 ? 32.239  52.848  48.687  1.00 67.25  ? 242 ALA A CA  1 
ATOM   1898  C C   . ALA A 1 239 ? 32.667  51.468  48.214  1.00 65.56  ? 242 ALA A C   1 
ATOM   1899  O O   . ALA A 1 239 ? 32.443  50.466  48.902  1.00 60.19  ? 242 ALA A O   1 
ATOM   1900  C CB  . ALA A 1 239 ? 33.249  53.388  49.705  1.00 56.60  ? 242 ALA A CB  1 
ATOM   1901  N N   . ILE A 1 240 ? 33.282  51.423  47.035  1.00 52.93  ? 243 ILE A N   1 
ATOM   1902  C CA  . ILE A 1 240 ? 33.842  50.201  46.476  1.00 53.38  ? 243 ILE A CA  1 
ATOM   1903  C C   . ILE A 1 240 ? 35.357  50.265  46.631  1.00 65.09  ? 243 ILE A C   1 
ATOM   1904  O O   . ILE A 1 240 ? 35.977  51.296  46.338  1.00 58.56  ? 243 ILE A O   1 
ATOM   1905  C CB  . ILE A 1 240 ? 33.431  50.018  45.005  1.00 52.73  ? 243 ILE A CB  1 
ATOM   1906  C CG1 . ILE A 1 240 ? 34.125  48.793  44.399  1.00 49.85  ? 243 ILE A CG1 1 
ATOM   1907  C CG2 . ILE A 1 240 ? 33.719  51.286  44.197  1.00 47.71  ? 243 ILE A CG2 1 
ATOM   1908  C CD1 . ILE A 1 240 ? 33.447  48.278  43.145  1.00 55.93  ? 243 ILE A CD1 1 
ATOM   1909  N N   . HIS A 1 241 ? 35.949  49.174  47.111  1.00 61.13  ? 244 HIS A N   1 
ATOM   1910  C CA  . HIS A 1 241 ? 37.373  49.119  47.418  1.00 47.67  ? 244 HIS A CA  1 
ATOM   1911  C C   . HIS A 1 241 ? 38.070  48.172  46.450  1.00 61.27  ? 244 HIS A C   1 
ATOM   1912  O O   . HIS A 1 241 ? 37.765  46.974  46.418  1.00 56.24  ? 244 HIS A O   1 
ATOM   1913  C CB  . HIS A 1 241 ? 37.596  48.673  48.863  1.00 51.46  ? 244 HIS A CB  1 
ATOM   1914  C CG  . HIS A 1 241 ? 36.776  49.433  49.858  1.00 67.94  ? 244 HIS A CG  1 
ATOM   1915  N ND1 . HIS A 1 241 ? 37.262  50.527  50.542  1.00 65.05  ? 244 HIS A ND1 1 
ATOM   1916  C CD2 . HIS A 1 241 ? 35.500  49.263  50.277  1.00 70.08  ? 244 HIS A CD2 1 
ATOM   1917  C CE1 . HIS A 1 241 ? 36.321  50.995  51.342  1.00 75.35  ? 244 HIS A CE1 1 
ATOM   1918  N NE2 . HIS A 1 241 ? 35.242  50.246  51.201  1.00 74.52  ? 244 HIS A NE2 1 
ATOM   1919  N N   . PHE A 1 242 ? 39.018  48.703  45.684  1.00 66.92  ? 245 PHE A N   1 
ATOM   1920  C CA  . PHE A 1 242 ? 39.799  47.911  44.746  1.00 56.99  ? 245 PHE A CA  1 
ATOM   1921  C C   . PHE A 1 242 ? 41.171  47.603  45.331  1.00 58.50  ? 245 PHE A C   1 
ATOM   1922  O O   . PHE A 1 242 ? 41.747  48.401  46.074  1.00 64.20  ? 245 PHE A O   1 
ATOM   1923  C CB  . PHE A 1 242 ? 39.942  48.633  43.405  1.00 56.29  ? 245 PHE A CB  1 
ATOM   1924  C CG  . PHE A 1 242 ? 38.668  48.672  42.608  1.00 62.39  ? 245 PHE A CG  1 
ATOM   1925  C CD1 . PHE A 1 242 ? 38.234  47.551  41.914  1.00 59.34  ? 245 PHE A CD1 1 
ATOM   1926  C CD2 . PHE A 1 242 ? 37.893  49.819  42.571  1.00 50.78  ? 245 PHE A CD2 1 
ATOM   1927  C CE1 . PHE A 1 242 ? 37.054  47.580  41.186  1.00 54.70  ? 245 PHE A CE1 1 
ATOM   1928  C CE2 . PHE A 1 242 ? 36.714  49.854  41.846  1.00 55.22  ? 245 PHE A CE2 1 
ATOM   1929  C CZ  . PHE A 1 242 ? 36.295  48.731  41.153  1.00 57.68  ? 245 PHE A CZ  1 
ATOM   1930  N N   . GLU A 1 243 ? 41.685  46.424  44.988  1.00 62.23  ? 246 GLU A N   1 
ATOM   1931  C CA  . GLU A 1 243 ? 42.918  45.920  45.584  1.00 55.70  ? 246 GLU A CA  1 
ATOM   1932  C C   . GLU A 1 243 ? 43.530  44.914  44.623  1.00 63.08  ? 246 GLU A C   1 
ATOM   1933  O O   . GLU A 1 243 ? 42.933  43.863  44.367  1.00 66.37  ? 246 GLU A O   1 
ATOM   1934  C CB  . GLU A 1 243 ? 42.631  45.283  46.948  1.00 68.28  ? 246 GLU A CB  1 
ATOM   1935  C CG  . GLU A 1 243 ? 43.715  45.477  48.005  1.00 75.62  ? 246 GLU A CG  1 
ATOM   1936  C CD  . GLU A 1 243 ? 44.774  44.395  47.967  1.00 80.68  ? 246 GLU A CD  1 
ATOM   1937  O OE1 . GLU A 1 243 ? 44.795  43.625  46.989  1.00 94.49  ? 246 GLU A OE1 1 
ATOM   1938  O OE2 . GLU A 1 243 ? 45.580  44.308  48.918  1.00 87.92  ? 246 GLU A OE2 1 
ATOM   1939  N N   . SER A 1 244 ? 44.709  45.227  44.089  1.00 58.60  ? 247 SER A N   1 
ATOM   1940  C CA  . SER A 1 244 ? 45.341  44.336  43.126  1.00 62.20  ? 247 SER A CA  1 
ATOM   1941  C C   . SER A 1 244 ? 46.840  44.589  43.092  1.00 71.32  ? 247 SER A C   1 
ATOM   1942  O O   . SER A 1 244 ? 47.316  45.684  43.399  1.00 63.68  ? 247 SER A O   1 
ATOM   1943  C CB  . SER A 1 244 ? 44.756  44.515  41.722  1.00 49.34  ? 247 SER A CB  1 
ATOM   1944  O OG  . SER A 1 244 ? 45.486  43.758  40.771  1.00 50.00  ? 247 SER A OG  1 
ATOM   1945  N N   . ASN A 1 245 ? 47.573  43.550  42.688  1.00 64.86  ? 248 ASN A N   1 
ATOM   1946  C CA  . ASN A 1 245 ? 48.997  43.648  42.386  1.00 62.03  ? 248 ASN A CA  1 
ATOM   1947  C C   . ASN A 1 245 ? 49.297  43.194  40.961  1.00 62.90  ? 248 ASN A C   1 
ATOM   1948  O O   . ASN A 1 245 ? 50.406  42.730  40.685  1.00 56.37  ? 248 ASN A O   1 
ATOM   1949  C CB  . ASN A 1 245 ? 49.819  42.834  43.387  1.00 59.90  ? 248 ASN A CB  1 
ATOM   1950  C CG  . ASN A 1 245 ? 49.572  41.346  43.264  1.00 61.31  ? 248 ASN A CG  1 
ATOM   1951  O OD1 . ASN A 1 245 ? 48.487  40.921  42.866  1.00 63.46  ? 248 ASN A OD1 1 
ATOM   1952  N ND2 . ASN A 1 245 ? 50.576  40.546  43.604  1.00 56.06  ? 248 ASN A ND2 1 
ATOM   1953  N N   . GLY A 1 246 ? 48.333  43.297  40.061  1.00 63.21  ? 249 GLY A N   1 
ATOM   1954  C CA  . GLY A 1 246 ? 48.544  42.944  38.670  1.00 55.36  ? 249 GLY A CA  1 
ATOM   1955  C C   . GLY A 1 246 ? 47.262  42.467  38.023  1.00 52.77  ? 249 GLY A C   1 
ATOM   1956  O O   . GLY A 1 246 ? 46.277  42.145  38.685  1.00 53.76  ? 249 GLY A O   1 
ATOM   1957  N N   . ASN A 1 247 ? 47.291  42.438  36.688  1.00 51.38  ? 250 ASN A N   1 
ATOM   1958  C CA  . ASN A 1 247 ? 46.221  41.896  35.845  1.00 49.43  ? 250 ASN A CA  1 
ATOM   1959  C C   . ASN A 1 247 ? 44.885  42.609  36.052  1.00 56.28  ? 250 ASN A C   1 
ATOM   1960  O O   . ASN A 1 247 ? 43.830  42.079  35.684  1.00 48.12  ? 250 ASN A O   1 
ATOM   1961  C CB  . ASN A 1 247 ? 46.048  40.388  36.066  1.00 45.53  ? 250 ASN A CB  1 
ATOM   1962  C CG  . ASN A 1 247 ? 47.303  39.595  35.731  1.00 52.51  ? 250 ASN A CG  1 
ATOM   1963  O OD1 . ASN A 1 247 ? 48.297  39.651  36.455  1.00 49.23  ? 250 ASN A OD1 1 
ATOM   1964  N ND2 . ASN A 1 247 ? 47.255  38.843  34.634  1.00 40.86  ? 250 ASN A ND2 1 
ATOM   1965  N N   . PHE A 1 248 ? 44.908  43.814  36.613  1.00 48.22  ? 251 PHE A N   1 
ATOM   1966  C CA  . PHE A 1 248 ? 43.697  44.551  36.946  1.00 42.68  ? 251 PHE A CA  1 
ATOM   1967  C C   . PHE A 1 248 ? 43.345  45.504  35.810  1.00 43.29  ? 251 PHE A C   1 
ATOM   1968  O O   . PHE A 1 248 ? 44.183  46.305  35.382  1.00 60.70  ? 251 PHE A O   1 
ATOM   1969  C CB  . PHE A 1 248 ? 43.895  45.318  38.255  1.00 51.36  ? 251 PHE A CB  1 
ATOM   1970  C CG  . PHE A 1 248 ? 42.714  46.145  38.669  1.00 45.89  ? 251 PHE A CG  1 
ATOM   1971  C CD1 . PHE A 1 248 ? 41.426  45.655  38.548  1.00 52.51  ? 251 PHE A CD1 1 
ATOM   1972  C CD2 . PHE A 1 248 ? 42.897  47.413  39.204  1.00 43.70  ? 251 PHE A CD2 1 
ATOM   1973  C CE1 . PHE A 1 248 ? 40.338  46.417  38.942  1.00 55.92  ? 251 PHE A CE1 1 
ATOM   1974  C CE2 . PHE A 1 248 ? 41.816  48.179  39.599  1.00 47.59  ? 251 PHE A CE2 1 
ATOM   1975  C CZ  . PHE A 1 248 ? 40.535  47.681  39.468  1.00 46.66  ? 251 PHE A CZ  1 
ATOM   1976  N N   . ILE A 1 249 ? 42.114  45.409  35.324  1.00 50.59  ? 252 ILE A N   1 
ATOM   1977  C CA  . ILE A 1 249 ? 41.579  46.335  34.332  1.00 49.69  ? 252 ILE A CA  1 
ATOM   1978  C C   . ILE A 1 249 ? 40.679  47.298  35.097  1.00 52.47  ? 252 ILE A C   1 
ATOM   1979  O O   . ILE A 1 249 ? 39.524  46.983  35.399  1.00 48.89  ? 252 ILE A O   1 
ATOM   1980  C CB  . ILE A 1 249 ? 40.828  45.605  33.219  1.00 37.42  ? 252 ILE A CB  1 
ATOM   1981  C CG1 . ILE A 1 249 ? 41.652  44.414  32.729  1.00 48.35  ? 252 ILE A CG1 1 
ATOM   1982  C CG2 . ILE A 1 249 ? 40.552  46.543  32.056  1.00 40.28  ? 252 ILE A CG2 1 
ATOM   1983  C CD1 . ILE A 1 249 ? 42.953  44.817  32.065  1.00 49.85  ? 252 ILE A CD1 1 
ATOM   1984  N N   . ALA A 1 250 ? 41.219  48.481  35.429  1.00 50.44  ? 253 ALA A N   1 
ATOM   1985  C CA  . ALA A 1 250 ? 40.581  49.387  36.371  1.00 54.93  ? 253 ALA A CA  1 
ATOM   1986  C C   . ALA A 1 250 ? 39.382  50.096  35.747  1.00 49.63  ? 253 ALA A C   1 
ATOM   1987  O O   . ALA A 1 250 ? 39.370  50.376  34.546  1.00 50.51  ? 253 ALA A O   1 
ATOM   1988  C CB  . ALA A 1 250 ? 41.577  50.424  36.870  1.00 43.54  ? 253 ALA A CB  1 
ATOM   1989  N N   . PRO A 1 251 ? 38.355  50.383  36.542  1.00 46.30  ? 254 PRO A N   1 
ATOM   1990  C CA  . PRO A 1 251 ? 37.271  51.237  36.048  1.00 55.67  ? 254 PRO A CA  1 
ATOM   1991  C C   . PRO A 1 251 ? 37.747  52.669  35.870  1.00 57.78  ? 254 PRO A C   1 
ATOM   1992  O O   . PRO A 1 251 ? 38.501  53.201  36.688  1.00 57.81  ? 254 PRO A O   1 
ATOM   1993  C CB  . PRO A 1 251 ? 36.200  51.132  37.142  1.00 47.51  ? 254 PRO A CB  1 
ATOM   1994  C CG  . PRO A 1 251 ? 36.927  50.678  38.358  1.00 49.11  ? 254 PRO A CG  1 
ATOM   1995  C CD  . PRO A 1 251 ? 38.085  49.855  37.892  1.00 42.25  ? 254 PRO A CD  1 
ATOM   1996  N N   . GLU A 1 252 ? 37.314  53.286  34.774  1.00 50.86  ? 255 GLU A N   1 
ATOM   1997  C CA  . GLU A 1 252 ? 37.530  54.704  34.529  1.00 45.72  ? 255 GLU A CA  1 
ATOM   1998  C C   . GLU A 1 252 ? 36.226  55.483  34.518  1.00 56.06  ? 255 GLU A C   1 
ATOM   1999  O O   . GLU A 1 252 ? 36.062  56.440  35.283  1.00 56.37  ? 255 GLU A O   1 
ATOM   2000  C CB  . GLU A 1 252 ? 38.272  54.905  33.201  1.00 55.53  ? 255 GLU A CB  1 
ATOM   2001  C CG  . GLU A 1 252 ? 38.645  56.355  32.916  1.00 60.56  ? 255 GLU A CG  1 
ATOM   2002  C CD  . GLU A 1 252 ? 39.317  56.524  31.566  1.00 67.72  ? 255 GLU A CD  1 
ATOM   2003  O OE1 . GLU A 1 252 ? 39.228  55.592  30.735  1.00 65.68  ? 255 GLU A OE1 1 
ATOM   2004  O OE2 . GLU A 1 252 ? 39.933  57.586  31.337  1.00 70.99  ? 255 GLU A OE2 1 
ATOM   2005  N N   . TYR A 1 253 ? 35.278  55.073  33.683  1.00 59.79  ? 256 TYR A N   1 
ATOM   2006  C CA  . TYR A 1 253 ? 33.938  55.632  33.663  1.00 52.55  ? 256 TYR A CA  1 
ATOM   2007  C C   . TYR A 1 253 ? 32.967  54.666  34.329  1.00 53.38  ? 256 TYR A C   1 
ATOM   2008  O O   . TYR A 1 253 ? 33.181  53.450  34.333  1.00 58.96  ? 256 TYR A O   1 
ATOM   2009  C CB  . TYR A 1 253 ? 33.485  55.919  32.230  1.00 54.45  ? 256 TYR A CB  1 
ATOM   2010  C CG  . TYR A 1 253 ? 34.226  57.061  31.577  1.00 62.92  ? 256 TYR A CG  1 
ATOM   2011  C CD1 . TYR A 1 253 ? 35.404  56.839  30.873  1.00 67.09  ? 256 TYR A CD1 1 
ATOM   2012  C CD2 . TYR A 1 253 ? 33.748  58.361  31.662  1.00 61.15  ? 256 TYR A CD2 1 
ATOM   2013  C CE1 . TYR A 1 253 ? 36.085  57.883  30.272  1.00 63.78  ? 256 TYR A CE1 1 
ATOM   2014  C CE2 . TYR A 1 253 ? 34.422  59.412  31.063  1.00 60.35  ? 256 TYR A CE2 1 
ATOM   2015  C CZ  . TYR A 1 253 ? 35.587  59.166  30.371  1.00 61.63  ? 256 TYR A CZ  1 
ATOM   2016  O OH  . TYR A 1 253 ? 36.257  60.209  29.775  1.00 62.58  ? 256 TYR A OH  1 
ATOM   2017  N N   . ALA A 1 254 ? 31.907  55.225  34.910  1.00 52.02  ? 257 ALA A N   1 
ATOM   2018  C CA  . ALA A 1 254 ? 30.805  54.455  35.470  1.00 45.33  ? 257 ALA A CA  1 
ATOM   2019  C C   . ALA A 1 254 ? 29.508  55.152  35.088  1.00 50.34  ? 257 ALA A C   1 
ATOM   2020  O O   . ALA A 1 254 ? 29.516  56.261  34.549  1.00 44.99  ? 257 ALA A O   1 
ATOM   2021  C CB  . ALA A 1 254 ? 30.924  54.306  36.992  1.00 47.12  ? 257 ALA A CB  1 
ATOM   2022  N N   . TYR A 1 255 ? 28.381  54.500  35.369  1.00 49.45  ? 258 TYR A N   1 
ATOM   2023  C CA  . TYR A 1 255 ? 27.086  54.962  34.881  1.00 46.50  ? 258 TYR A CA  1 
ATOM   2024  C C   . TYR A 1 255 ? 26.141  55.226  36.043  1.00 49.13  ? 258 TYR A C   1 
ATOM   2025  O O   . TYR A 1 255 ? 25.882  54.331  36.855  1.00 48.98  ? 258 TYR A O   1 
ATOM   2026  C CB  . TYR A 1 255 ? 26.475  53.942  33.924  1.00 46.18  ? 258 TYR A CB  1 
ATOM   2027  C CG  . TYR A 1 255 ? 27.245  53.763  32.635  1.00 50.13  ? 258 TYR A CG  1 
ATOM   2028  C CD1 . TYR A 1 255 ? 27.190  54.721  31.627  1.00 50.60  ? 258 TYR A CD1 1 
ATOM   2029  C CD2 . TYR A 1 255 ? 28.026  52.637  32.425  1.00 37.59  ? 258 TYR A CD2 1 
ATOM   2030  C CE1 . TYR A 1 255 ? 27.888  54.553  30.442  1.00 45.27  ? 258 TYR A CE1 1 
ATOM   2031  C CE2 . TYR A 1 255 ? 28.729  52.462  31.246  1.00 46.69  ? 258 TYR A CE2 1 
ATOM   2032  C CZ  . TYR A 1 255 ? 28.657  53.420  30.258  1.00 48.53  ? 258 TYR A CZ  1 
ATOM   2033  O OH  . TYR A 1 255 ? 29.360  53.239  29.088  1.00 49.71  ? 258 TYR A OH  1 
ATOM   2034  N N   . LYS A 1 256 ? 25.629  56.453  36.119  1.00 46.26  ? 259 LYS A N   1 
ATOM   2035  C CA  . LYS A 1 256 ? 24.504  56.743  36.997  1.00 57.08  ? 259 LYS A CA  1 
ATOM   2036  C C   . LYS A 1 256 ? 23.250  56.104  36.416  1.00 54.02  ? 259 LYS A C   1 
ATOM   2037  O O   . LYS A 1 256 ? 22.964  56.262  35.226  1.00 56.61  ? 259 LYS A O   1 
ATOM   2038  C CB  . LYS A 1 256 ? 24.316  58.252  37.142  1.00 65.36  ? 259 LYS A CB  1 
ATOM   2039  C CG  . LYS A 1 256 ? 25.061  58.879  38.314  1.00 78.73  ? 259 LYS A CG  1 
ATOM   2040  C CD  . LYS A 1 256 ? 25.442  60.329  38.022  1.00 75.58  ? 259 LYS A CD  1 
ATOM   2041  C CE  . LYS A 1 256 ? 24.219  61.239  38.034  1.00 74.04  ? 259 LYS A CE  1 
ATOM   2042  N NZ  . LYS A 1 256 ? 23.828  61.648  39.414  1.00 72.80  ? 259 LYS A NZ  1 
ATOM   2043  N N   . ILE A 1 257 ? 22.503  55.376  37.245  1.00 54.38  ? 260 ILE A N   1 
ATOM   2044  C CA  . ILE A 1 257 ? 21.395  54.559  36.757  1.00 62.49  ? 260 ILE A CA  1 
ATOM   2045  C C   . ILE A 1 257 ? 20.188  54.711  37.680  1.00 55.75  ? 260 ILE A C   1 
ATOM   2046  O O   . ILE A 1 257 ? 20.321  54.661  38.908  1.00 56.39  ? 260 ILE A O   1 
ATOM   2047  C CB  . ILE A 1 257 ? 21.812  53.079  36.622  1.00 56.03  ? 260 ILE A CB  1 
ATOM   2048  C CG1 . ILE A 1 257 ? 20.672  52.239  36.049  1.00 67.37  ? 260 ILE A CG1 1 
ATOM   2049  C CG2 . ILE A 1 257 ? 22.291  52.510  37.955  1.00 54.46  ? 260 ILE A CG2 1 
ATOM   2050  C CD1 . ILE A 1 257 ? 20.983  50.755  36.014  1.00 74.52  ? 260 ILE A CD1 1 
ATOM   2051  N N   . VAL A 1 258 A 19.014  54.920  37.085  1.00 54.18  ? 260 VAL A N   1 
ATOM   2052  C CA  . VAL A 1 258 A 17.739  54.912  37.797  1.00 57.16  ? 260 VAL A CA  1 
ATOM   2053  C C   . VAL A 1 258 A 16.809  53.930  37.100  1.00 62.76  ? 260 VAL A C   1 
ATOM   2054  O O   . VAL A 1 258 A 16.585  54.032  35.887  1.00 53.95  ? 260 VAL A O   1 
ATOM   2055  C CB  . VAL A 1 258 A 17.090  56.308  37.851  1.00 65.93  ? 260 VAL A CB  1 
ATOM   2056  C CG1 . VAL A 1 258 A 16.011  56.341  38.918  1.00 57.88  ? 260 VAL A CG1 1 
ATOM   2057  C CG2 . VAL A 1 258 A 18.129  57.370  38.125  1.00 70.05  ? 260 VAL A CG2 1 
ATOM   2058  N N   . LYS A 1 259 ? 16.261  52.986  37.862  1.00 52.50  ? 261 LYS A N   1 
ATOM   2059  C CA  . LYS A 1 259 ? 15.379  51.968  37.310  1.00 56.20  ? 261 LYS A CA  1 
ATOM   2060  C C   . LYS A 1 259 ? 14.063  51.959  38.071  1.00 59.67  ? 261 LYS A C   1 
ATOM   2061  O O   . LYS A 1 259 ? 14.050  51.817  39.298  1.00 55.02  ? 261 LYS A O   1 
ATOM   2062  C CB  . LYS A 1 259 ? 16.027  50.580  37.358  1.00 52.28  ? 261 LYS A CB  1 
ATOM   2063  C CG  . LYS A 1 259 ? 15.452  49.603  36.335  1.00 51.92  ? 261 LYS A CG  1 
ATOM   2064  C CD  . LYS A 1 259 ? 15.591  48.167  36.808  1.00 57.79  ? 261 LYS A CD  1 
ATOM   2065  C CE  . LYS A 1 259 ? 15.003  47.194  35.798  1.00 55.61  ? 261 LYS A CE  1 
ATOM   2066  N NZ  . LYS A 1 259 ? 15.261  47.623  34.397  1.00 64.99  ? 261 LYS A NZ  1 
ATOM   2067  N N   . LYS A 1 260 ? 12.959  52.101  37.336  1.00 65.10  ? 262 LYS A N   1 
ATOM   2068  C CA  . LYS A 1 260 ? 11.628  51.970  37.906  1.00 62.83  ? 262 LYS A CA  1 
ATOM   2069  C C   . LYS A 1 260 ? 10.712  51.084  37.073  1.00 65.47  ? 262 LYS A C   1 
ATOM   2070  O O   . LYS A 1 260 ? 9.564   50.862  37.473  1.00 77.24  ? 262 LYS A O   1 
ATOM   2071  C CB  . LYS A 1 260 ? 10.982  53.352  38.091  1.00 62.02  ? 262 LYS A CB  1 
ATOM   2072  C CG  . LYS A 1 260 ? 11.228  54.320  36.946  1.00 61.70  ? 262 LYS A CG  1 
ATOM   2073  C CD  . LYS A 1 260 ? 10.291  55.518  37.041  1.00 80.70  ? 262 LYS A CD  1 
ATOM   2074  C CE  . LYS A 1 260 ? 9.336   55.574  35.848  1.00 90.14  ? 262 LYS A CE  1 
ATOM   2075  N NZ  . LYS A 1 260 ? 8.153   56.458  36.084  1.00 59.14  ? 262 LYS A NZ  1 
ATOM   2076  N N   . GLY A 1 261 ? 11.185  50.568  35.933  1.00 60.23  ? 263 GLY A N   1 
ATOM   2077  C CA  . GLY A 1 261 ? 10.385  49.689  35.108  1.00 64.66  ? 263 GLY A CA  1 
ATOM   2078  C C   . GLY A 1 261 ? 11.243  48.614  34.471  1.00 61.32  ? 263 GLY A C   1 
ATOM   2079  O O   . GLY A 1 261 ? 12.473  48.676  34.494  1.00 61.86  ? 263 GLY A O   1 
ATOM   2080  N N   . ASP A 1 262 ? 10.568  47.625  33.892  1.00 74.14  ? 264 ASP A N   1 
ATOM   2081  C CA  . ASP A 1 262 ? 11.221  46.469  33.299  1.00 61.49  ? 264 ASP A CA  1 
ATOM   2082  C C   . ASP A 1 262 ? 10.786  46.298  31.851  1.00 43.25  ? 264 ASP A C   1 
ATOM   2083  O O   . ASP A 1 262 ? 9.699   46.723  31.450  1.00 57.60  ? 264 ASP A O   1 
ATOM   2084  C CB  . ASP A 1 262 ? 10.913  45.187  34.084  1.00 69.69  ? 264 ASP A CB  1 
ATOM   2085  C CG  . ASP A 1 262 ? 11.281  45.299  35.551  1.00 81.37  ? 264 ASP A CG  1 
ATOM   2086  O OD1 . ASP A 1 262 ? 12.476  45.136  35.879  1.00 74.04  ? 264 ASP A OD1 1 
ATOM   2087  O OD2 . ASP A 1 262 ? 10.374  45.550  36.375  1.00 85.87  ? 264 ASP A OD2 1 
ATOM   2088  N N   . SER A 1 263 ? 11.648  45.657  31.075  1.00 39.02  ? 265 SER A N   1 
ATOM   2089  C CA  . SER A 1 263 ? 11.452  45.490  29.642  1.00 44.08  ? 265 SER A CA  1 
ATOM   2090  C C   . SER A 1 263 ? 12.278  44.281  29.214  1.00 37.92  ? 265 SER A C   1 
ATOM   2091  O O   . SER A 1 263 ? 12.653  43.452  30.051  1.00 47.60  ? 265 SER A O   1 
ATOM   2092  C CB  . SER A 1 263 ? 11.828  46.779  28.894  1.00 49.27  ? 265 SER A CB  1 
ATOM   2093  O OG  . SER A 1 263 ? 11.288  46.784  27.585  1.00 62.18  ? 265 SER A OG  1 
ATOM   2094  N N   . THR A 1 264 ? 12.546  44.163  27.918  1.00 41.94  ? 266 THR A N   1 
ATOM   2095  C CA  . THR A 1 264 ? 13.438  43.125  27.427  1.00 55.77  ? 266 THR A CA  1 
ATOM   2096  C C   . THR A 1 264 ? 14.259  43.659  26.259  1.00 52.99  ? 266 THR A C   1 
ATOM   2097  O O   . THR A 1 264 ? 14.012  44.750  25.740  1.00 50.49  ? 266 THR A O   1 
ATOM   2098  C CB  . THR A 1 264 ? 12.662  41.872  27.005  1.00 50.93  ? 266 THR A CB  1 
ATOM   2099  O OG1 . THR A 1 264 ? 13.561  40.755  26.937  1.00 51.26  ? 266 THR A OG1 1 
ATOM   2100  C CG2 . THR A 1 264 ? 12.010  42.092  25.649  1.00 41.01  ? 266 THR A CG2 1 
ATOM   2101  N N   . ILE A 1 265 ? 15.259  42.872  25.866  1.00 43.37  ? 267 ILE A N   1 
ATOM   2102  C CA  . ILE A 1 265 ? 16.029  43.126  24.653  1.00 35.98  ? 267 ILE A CA  1 
ATOM   2103  C C   . ILE A 1 265 ? 15.222  42.660  23.448  1.00 46.44  ? 267 ILE A C   1 
ATOM   2104  O O   . ILE A 1 265 ? 14.674  41.551  23.445  1.00 49.36  ? 267 ILE A O   1 
ATOM   2105  C CB  . ILE A 1 265 ? 17.382  42.398  24.710  1.00 44.41  ? 267 ILE A CB  1 
ATOM   2106  C CG1 . ILE A 1 265 ? 18.104  42.700  26.027  1.00 53.25  ? 267 ILE A CG1 1 
ATOM   2107  C CG2 . ILE A 1 265 ? 18.233  42.740  23.485  1.00 44.30  ? 267 ILE A CG2 1 
ATOM   2108  C CD1 . ILE A 1 265 ? 18.549  44.132  26.164  1.00 44.41  ? 267 ILE A CD1 1 
ATOM   2109  N N   . MET A 1 266 ? 15.159  43.492  22.413  1.00 44.14  ? 268 MET A N   1 
ATOM   2110  C CA  . MET A 1 266 ? 14.494  43.133  21.169  1.00 47.37  ? 268 MET A CA  1 
ATOM   2111  C C   . MET A 1 266 ? 15.538  42.927  20.079  1.00 50.52  ? 268 MET A C   1 
ATOM   2112  O O   . MET A 1 266 ? 16.384  43.798  19.848  1.00 50.38  ? 268 MET A O   1 
ATOM   2113  C CB  . MET A 1 266 ? 13.489  44.208  20.743  1.00 39.07  ? 268 MET A CB  1 
ATOM   2114  C CG  . MET A 1 266 ? 13.226  44.240  19.239  1.00 45.67  ? 268 MET A CG  1 
ATOM   2115  S SD  . MET A 1 266 ? 11.705  45.100  18.755  1.00 57.46  ? 268 MET A SD  1 
ATOM   2116  C CE  . MET A 1 266 ? 10.483  44.289  19.780  1.00 46.95  ? 268 MET A CE  1 
ATOM   2117  N N   . LYS A 1 267 ? 15.476  41.776  19.415  1.00 40.30  ? 269 LYS A N   1 
ATOM   2118  C CA  . LYS A 1 267 ? 16.376  41.456  18.313  1.00 52.63  ? 269 LYS A CA  1 
ATOM   2119  C C   . LYS A 1 267 ? 15.726  41.913  17.011  1.00 53.76  ? 269 LYS A C   1 
ATOM   2120  O O   . LYS A 1 267 ? 14.727  41.337  16.572  1.00 57.49  ? 269 LYS A O   1 
ATOM   2121  C CB  . LYS A 1 267 ? 16.680  39.959  18.287  1.00 40.89  ? 269 LYS A CB  1 
ATOM   2122  C CG  . LYS A 1 267 ? 18.103  39.602  18.680  1.00 61.34  ? 269 LYS A CG  1 
ATOM   2123  C CD  . LYS A 1 267 ? 18.478  40.178  20.038  1.00 58.67  ? 269 LYS A CD  1 
ATOM   2124  C CE  . LYS A 1 267 ? 19.823  39.632  20.514  1.00 72.11  ? 269 LYS A CE  1 
ATOM   2125  N NZ  . LYS A 1 267 ? 20.953  39.983  19.601  1.00 68.07  ? 269 LYS A NZ  1 
ATOM   2126  N N   . SER A 1 268 ? 16.287  42.950  16.396  1.00 56.85  ? 270 SER A N   1 
ATOM   2127  C CA  . SER A 1 268 ? 15.706  43.489  15.176  1.00 56.89  ? 270 SER A CA  1 
ATOM   2128  C C   . SER A 1 268 ? 16.778  44.216  14.382  1.00 60.80  ? 270 SER A C   1 
ATOM   2129  O O   . SER A 1 268 ? 17.677  44.839  14.951  1.00 54.86  ? 270 SER A O   1 
ATOM   2130  C CB  . SER A 1 268 ? 14.542  44.438  15.479  1.00 51.30  ? 270 SER A CB  1 
ATOM   2131  O OG  . SER A 1 268 ? 13.968  44.922  14.278  1.00 59.69  ? 270 SER A OG  1 
ATOM   2132  N N   . GLU A 1 269 ? 16.668  44.131  13.059  1.00 69.09  ? 271 GLU A N   1 
ATOM   2133  C CA  . GLU A 1 269 ? 17.560  44.843  12.158  1.00 70.46  ? 271 GLU A CA  1 
ATOM   2134  C C   . GLU A 1 269 ? 16.996  46.180  11.700  1.00 68.77  ? 271 GLU A C   1 
ATOM   2135  O O   . GLU A 1 269 ? 17.698  46.936  11.025  1.00 70.33  ? 271 GLU A O   1 
ATOM   2136  C CB  . GLU A 1 269 ? 17.877  43.971  10.939  1.00 59.44  ? 271 GLU A CB  1 
ATOM   2137  C CG  . GLU A 1 269 ? 17.870  42.483  11.226  1.00 70.20  ? 271 GLU A CG  1 
ATOM   2138  C CD  . GLU A 1 269 ? 19.203  41.973  11.752  1.00 80.48  ? 271 GLU A CD  1 
ATOM   2139  O OE1 . GLU A 1 269 ? 20.082  42.799  12.086  1.00 80.29  ? 271 GLU A OE1 1 
ATOM   2140  O OE2 . GLU A 1 269 ? 19.371  40.738  11.827  1.00 85.84  ? 271 GLU A OE2 1 
ATOM   2141  N N   . MET A 1 270 ? 15.758  46.497  12.067  1.00 68.58  ? 272 MET A N   1 
ATOM   2142  C CA  . MET A 1 270 ? 15.112  47.693  11.557  1.00 60.91  ? 272 MET A CA  1 
ATOM   2143  C C   . MET A 1 270 ? 15.678  48.946  12.225  1.00 72.81  ? 272 MET A C   1 
ATOM   2144  O O   . MET A 1 270 ? 16.403  48.888  13.223  1.00 68.23  ? 272 MET A O   1 
ATOM   2145  C CB  . MET A 1 270 ? 13.604  47.609  11.760  1.00 67.16  ? 272 MET A CB  1 
ATOM   2146  C CG  . MET A 1 270 ? 12.905  46.797  10.689  1.00 63.63  ? 272 MET A CG  1 
ATOM   2147  S SD  . MET A 1 270 ? 11.119  46.825  10.852  1.00 78.19  ? 272 MET A SD  1 
ATOM   2148  C CE  . MET A 1 270 ? 10.921  47.438  12.519  1.00 63.44  ? 272 MET A CE  1 
ATOM   2149  N N   . GLU A 1 271 ? 15.341  50.092  11.644  1.00 86.61  ? 273 GLU A N   1 
ATOM   2150  C CA  . GLU A 1 271 ? 15.819  51.392  12.088  1.00 83.46  ? 273 GLU A CA  1 
ATOM   2151  C C   . GLU A 1 271 ? 14.696  52.161  12.772  1.00 77.80  ? 273 GLU A C   1 
ATOM   2152  O O   . GLU A 1 271 ? 13.515  51.810  12.679  1.00 65.05  ? 273 GLU A O   1 
ATOM   2153  C CB  . GLU A 1 271 ? 16.367  52.199  10.905  1.00 88.20  ? 273 GLU A CB  1 
ATOM   2154  C CG  . GLU A 1 271 ? 15.366  52.362  9.765   1.00 102.72 ? 273 GLU A CG  1 
ATOM   2155  C CD  . GLU A 1 271 ? 15.437  53.728  9.103   1.00 102.98 ? 273 GLU A CD  1 
ATOM   2156  O OE1 . GLU A 1 271 ? 16.449  54.435  9.296   1.00 101.52 ? 273 GLU A OE1 1 
ATOM   2157  O OE2 . GLU A 1 271 ? 14.477  54.092  8.388   1.00 99.90  ? 273 GLU A OE2 1 
ATOM   2158  N N   . TYR A 1 272 ? 15.089  53.231  13.463  1.00 60.42  ? 274 TYR A N   1 
ATOM   2159  C CA  . TYR A 1 272 ? 14.125  54.094  14.131  1.00 65.53  ? 274 TYR A CA  1 
ATOM   2160  C C   . TYR A 1 272 ? 13.152  54.688  13.116  1.00 67.54  ? 274 TYR A C   1 
ATOM   2161  O O   . TYR A 1 272 ? 13.539  55.066  12.006  1.00 69.65  ? 274 TYR A O   1 
ATOM   2162  C CB  . TYR A 1 272 ? 14.859  55.201  14.888  1.00 48.45  ? 274 TYR A CB  1 
ATOM   2163  C CG  . TYR A 1 272 ? 13.972  56.054  15.762  1.00 63.42  ? 274 TYR A CG  1 
ATOM   2164  C CD1 . TYR A 1 272 ? 13.138  55.481  16.712  1.00 63.97  ? 274 TYR A CD1 1 
ATOM   2165  C CD2 . TYR A 1 272 ? 13.971  57.438  15.637  1.00 63.44  ? 274 TYR A CD2 1 
ATOM   2166  C CE1 . TYR A 1 272 ? 12.326  56.265  17.516  1.00 73.14  ? 274 TYR A CE1 1 
ATOM   2167  C CE2 . TYR A 1 272 ? 13.165  58.229  16.435  1.00 62.70  ? 274 TYR A CE2 1 
ATOM   2168  C CZ  . TYR A 1 272 ? 12.345  57.639  17.373  1.00 73.79  ? 274 TYR A CZ  1 
ATOM   2169  O OH  . TYR A 1 272 ? 11.544  58.427  18.168  1.00 63.47  ? 274 TYR A OH  1 
ATOM   2170  N N   . GLY A 1 273 ? 11.879  54.755  13.497  1.00 57.93  ? 275 GLY A N   1 
ATOM   2171  C CA  . GLY A 1 273 ? 10.840  55.165  12.571  1.00 66.80  ? 275 GLY A CA  1 
ATOM   2172  C C   . GLY A 1 273 ? 10.135  56.462  12.915  1.00 67.52  ? 275 GLY A C   1 
ATOM   2173  O O   . GLY A 1 273 ? 9.185   56.849  12.226  1.00 68.62  ? 275 GLY A O   1 
ATOM   2174  N N   . HIS A 1 274 ? 10.582  57.134  13.979  1.00 65.26  ? 276 HIS A N   1 
ATOM   2175  C CA  . HIS A 1 274 ? 10.030  58.425  14.400  1.00 68.28  ? 276 HIS A CA  1 
ATOM   2176  C C   . HIS A 1 274 ? 8.516   58.338  14.584  1.00 64.38  ? 276 HIS A C   1 
ATOM   2177  O O   . HIS A 1 274 ? 7.741   59.106  14.010  1.00 71.80  ? 276 HIS A O   1 
ATOM   2178  C CB  . HIS A 1 274 ? 10.407  59.531  13.411  1.00 61.50  ? 276 HIS A CB  1 
ATOM   2179  C CG  . HIS A 1 274 ? 11.872  59.591  13.105  1.00 71.45  ? 276 HIS A CG  1 
ATOM   2180  N ND1 . HIS A 1 274 ? 12.775  60.249  13.913  1.00 73.52  ? 276 HIS A ND1 1 
ATOM   2181  C CD2 . HIS A 1 274 ? 12.591  59.072  12.081  1.00 69.01  ? 276 HIS A CD2 1 
ATOM   2182  C CE1 . HIS A 1 274 ? 13.987  60.135  13.399  1.00 66.66  ? 276 HIS A CE1 1 
ATOM   2183  N NE2 . HIS A 1 274 ? 13.903  59.424  12.288  1.00 72.06  ? 276 HIS A NE2 1 
ATOM   2184  N N   . CYS A 1 275 ? 8.101   57.379  15.405  1.00 72.37  ? 277 CYS A N   1 
ATOM   2185  C CA  . CYS A 1 275 ? 6.699   57.060  15.625  1.00 68.71  ? 277 CYS A CA  1 
ATOM   2186  C C   . CYS A 1 275 ? 6.502   56.672  17.083  1.00 62.16  ? 277 CYS A C   1 
ATOM   2187  O O   . CYS A 1 275 ? 7.463   56.483  17.835  1.00 67.08  ? 277 CYS A O   1 
ATOM   2188  C CB  . CYS A 1 275 ? 6.232   55.951  14.666  1.00 65.34  ? 277 CYS A CB  1 
ATOM   2189  S SG  . CYS A 1 275 ? 7.365   54.510  14.566  1.00 100.45 ? 277 CYS A SG  1 
ATOM   2190  N N   . ASN A 1 276 ? 5.241   56.576  17.488  1.00 51.42  ? 278 ASN A N   1 
ATOM   2191  C CA  . ASN A 1 276 ? 4.888   56.182  18.843  1.00 54.23  ? 278 ASN A CA  1 
ATOM   2192  C C   . ASN A 1 276 ? 3.886   55.038  18.786  1.00 56.61  ? 278 ASN A C   1 
ATOM   2193  O O   . ASN A 1 276 ? 3.094   54.930  17.845  1.00 53.45  ? 278 ASN A O   1 
ATOM   2194  C CB  . ASN A 1 276 ? 4.307   57.357  19.642  1.00 49.18  ? 278 ASN A CB  1 
ATOM   2195  C CG  . ASN A 1 276 ? 4.339   57.116  21.142  1.00 64.30  ? 278 ASN A CG  1 
ATOM   2196  O OD1 . ASN A 1 276 ? 5.031   56.219  21.624  1.00 63.77  ? 278 ASN A OD1 1 
ATOM   2197  N ND2 . ASN A 1 276 ? 3.586   57.920  21.889  1.00 60.56  ? 278 ASN A ND2 1 
ATOM   2198  N N   . THR A 1 277 ? 3.942   54.171  19.793  1.00 47.22  ? 279 THR A N   1 
ATOM   2199  C CA  . THR A 1 277 ? 3.061   53.016  19.835  1.00 36.96  ? 279 THR A CA  1 
ATOM   2200  C C   . THR A 1 277 ? 2.961   52.514  21.265  1.00 46.82  ? 279 THR A C   1 
ATOM   2201  O O   . THR A 1 277 ? 3.774   52.860  22.128  1.00 52.07  ? 279 THR A O   1 
ATOM   2202  C CB  . THR A 1 277 ? 3.547   51.892  18.915  1.00 46.63  ? 279 THR A CB  1 
ATOM   2203  O OG1 . THR A 1 277 ? 2.472   50.975  18.667  1.00 60.41  ? 279 THR A OG1 1 
ATOM   2204  C CG2 . THR A 1 277 ? 4.697   51.138  19.559  1.00 50.70  ? 279 THR A CG2 1 
ATOM   2205  N N   . LYS A 1 278 ? 1.937   51.698  21.503  1.00 49.80  ? 280 LYS A N   1 
ATOM   2206  C CA  . LYS A 1 278 ? 1.816   50.950  22.743  1.00 50.98  ? 280 LYS A CA  1 
ATOM   2207  C C   . LYS A 1 278 ? 2.262   49.505  22.592  1.00 43.83  ? 280 LYS A C   1 
ATOM   2208  O O   . LYS A 1 278 ? 2.342   48.792  23.596  1.00 45.63  ? 280 LYS A O   1 
ATOM   2209  C CB  . LYS A 1 278 ? 0.367   50.984  23.247  1.00 43.70  ? 280 LYS A CB  1 
ATOM   2210  C CG  . LYS A 1 278 ? -0.665  50.838  22.140  1.00 65.30  ? 280 LYS A CG  1 
ATOM   2211  C CD  . LYS A 1 278 ? -1.858  49.989  22.577  1.00 79.05  ? 280 LYS A CD  1 
ATOM   2212  C CE  . LYS A 1 278 ? -2.870  49.832  21.447  1.00 66.19  ? 280 LYS A CE  1 
ATOM   2213  N NZ  . LYS A 1 278 ? -2.239  49.329  20.190  1.00 65.19  ? 280 LYS A NZ  1 
ATOM   2214  N N   . CYS A 1 279 ? 2.561   49.066  21.369  1.00 42.51  ? 281 CYS A N   1 
ATOM   2215  C CA  . CYS A 1 279 ? 2.846   47.662  21.084  1.00 45.07  ? 281 CYS A CA  1 
ATOM   2216  C C   . CYS A 1 279 ? 3.874   47.583  19.969  1.00 42.03  ? 281 CYS A C   1 
ATOM   2217  O O   . CYS A 1 279 ? 3.600   48.010  18.843  1.00 56.00  ? 281 CYS A O   1 
ATOM   2218  C CB  . CYS A 1 279 ? 1.567   46.916  20.686  1.00 53.04  ? 281 CYS A CB  1 
ATOM   2219  S SG  . CYS A 1 279 ? 1.820   45.177  20.256  1.00 63.31  ? 281 CYS A SG  1 
ATOM   2220  N N   . GLN A 1 280 ? 5.039   47.018  20.270  1.00 49.40  ? 282 GLN A N   1 
ATOM   2221  C CA  . GLN A 1 280 ? 6.140   46.929  19.323  1.00 43.89  ? 282 GLN A CA  1 
ATOM   2222  C C   . GLN A 1 280 ? 6.508   45.472  19.073  1.00 44.38  ? 282 GLN A C   1 
ATOM   2223  O O   . GLN A 1 280 ? 6.603   44.675  20.011  1.00 43.11  ? 282 GLN A O   1 
ATOM   2224  C CB  . GLN A 1 280 ? 7.362   47.699  19.835  1.00 46.02  ? 282 GLN A CB  1 
ATOM   2225  C CG  . GLN A 1 280 ? 8.533   47.721  18.865  1.00 41.45  ? 282 GLN A CG  1 
ATOM   2226  C CD  . GLN A 1 280 ? 8.272   48.616  17.668  1.00 52.94  ? 282 GLN A CD  1 
ATOM   2227  O OE1 . GLN A 1 280 ? 7.957   49.800  17.819  1.00 50.01  ? 282 GLN A OE1 1 
ATOM   2228  N NE2 . GLN A 1 280 ? 8.398   48.054  16.470  1.00 49.74  ? 282 GLN A NE2 1 
ATOM   2229  N N   . THR A 1 281 ? 6.704   45.131  17.804  1.00 42.17  ? 283 THR A N   1 
ATOM   2230  C CA  . THR A 1 281 ? 7.211   43.840  17.370  1.00 39.26  ? 283 THR A CA  1 
ATOM   2231  C C   . THR A 1 281 ? 8.491   44.051  16.569  1.00 52.14  ? 283 THR A C   1 
ATOM   2232  O O   . THR A 1 281 ? 8.739   45.152  16.063  1.00 47.03  ? 283 THR A O   1 
ATOM   2233  C CB  . THR A 1 281 ? 6.183   43.083  16.512  1.00 45.82  ? 283 THR A CB  1 
ATOM   2234  O OG1 . THR A 1 281 ? 6.293   43.498  15.143  1.00 46.60  ? 283 THR A OG1 1 
ATOM   2235  C CG2 . THR A 1 281 ? 4.763   43.325  17.011  1.00 44.08  ? 283 THR A CG2 1 
ATOM   2236  N N   . PRO A 1 282 ? 9.334   43.020  16.440  1.00 49.86  ? 284 PRO A N   1 
ATOM   2237  C CA  . PRO A 1 282 ? 10.601  43.199  15.711  1.00 48.71  ? 284 PRO A CA  1 
ATOM   2238  C C   . PRO A 1 282 ? 10.436  43.592  14.248  1.00 54.96  ? 284 PRO A C   1 
ATOM   2239  O O   . PRO A 1 282 ? 11.411  44.055  13.641  1.00 57.43  ? 284 PRO A O   1 
ATOM   2240  C CB  . PRO A 1 282 ? 11.278  41.829  15.851  1.00 46.39  ? 284 PRO A CB  1 
ATOM   2241  C CG  . PRO A 1 282 ? 10.714  41.270  17.112  1.00 37.20  ? 284 PRO A CG  1 
ATOM   2242  C CD  . PRO A 1 282 ? 9.286   41.718  17.129  1.00 47.93  ? 284 PRO A CD  1 
ATOM   2243  N N   . ILE A 1 283 ? 9.252   43.421  13.659  1.00 46.61  ? 285 ILE A N   1 
ATOM   2244  C CA  . ILE A 1 283 ? 9.007   43.807  12.273  1.00 47.88  ? 285 ILE A CA  1 
ATOM   2245  C C   . ILE A 1 283 ? 8.029   44.966  12.146  1.00 55.66  ? 285 ILE A C   1 
ATOM   2246  O O   . ILE A 1 283 ? 7.693   45.351  11.016  1.00 55.29  ? 285 ILE A O   1 
ATOM   2247  C CB  . ILE A 1 283 ? 8.521   42.613  11.430  1.00 45.03  ? 285 ILE A CB  1 
ATOM   2248  C CG1 . ILE A 1 283 ? 7.133   42.162  11.893  1.00 45.06  ? 285 ILE A CG1 1 
ATOM   2249  C CG2 . ILE A 1 283 ? 9.520   41.474  11.500  1.00 42.30  ? 285 ILE A CG2 1 
ATOM   2250  C CD1 . ILE A 1 283 ? 6.501   41.119  10.999  1.00 37.38  ? 285 ILE A CD1 1 
ATOM   2251  N N   . GLY A 1 284 ? 7.559   45.532  13.249  1.00 52.01  ? 286 GLY A N   1 
ATOM   2252  C CA  . GLY A 1 284 ? 6.665   46.672  13.172  1.00 51.32  ? 286 GLY A CA  1 
ATOM   2253  C C   . GLY A 1 284 ? 5.879   46.862  14.449  1.00 53.85  ? 286 GLY A C   1 
ATOM   2254  O O   . GLY A 1 284 ? 5.854   46.009  15.334  1.00 52.06  ? 286 GLY A O   1 
ATOM   2255  N N   . ALA A 1 285 ? 5.217   48.014  14.524  1.00 59.77  ? 287 ALA A N   1 
ATOM   2256  C CA  . ALA A 1 285 ? 4.392   48.382  15.665  1.00 58.13  ? 287 ALA A CA  1 
ATOM   2257  C C   . ALA A 1 285 ? 2.915   48.164  15.346  1.00 54.02  ? 287 ALA A C   1 
ATOM   2258  O O   . ALA A 1 285 ? 2.500   48.195  14.184  1.00 46.08  ? 287 ALA A O   1 
ATOM   2259  C CB  . ALA A 1 285 ? 4.633   49.840  16.062  1.00 46.53  ? 287 ALA A CB  1 
ATOM   2260  N N   . ILE A 1 286 ? 2.125   47.935  16.394  1.00 50.80  ? 288 ILE A N   1 
ATOM   2261  C CA  . ILE A 1 286 ? 0.705   47.619  16.271  1.00 39.45  ? 288 ILE A CA  1 
ATOM   2262  C C   . ILE A 1 286 ? -0.093  48.714  16.965  1.00 46.10  ? 288 ILE A C   1 
ATOM   2263  O O   . ILE A 1 286 ? 0.099   48.966  18.161  1.00 50.65  ? 288 ILE A O   1 
ATOM   2264  C CB  . ILE A 1 286 ? 0.374   46.244  16.874  1.00 49.65  ? 288 ILE A CB  1 
ATOM   2265  C CG1 . ILE A 1 286 ? 0.969   45.120  16.025  1.00 40.38  ? 288 ILE A CG1 1 
ATOM   2266  C CG2 . ILE A 1 286 ? -1.139  46.060  17.036  1.00 49.16  ? 288 ILE A CG2 1 
ATOM   2267  C CD1 . ILE A 1 286 ? 1.052   43.802  16.769  1.00 45.98  ? 288 ILE A CD1 1 
ATOM   2268  N N   . ASN A 1 287 ? -0.985  49.359  16.218  1.00 51.15  ? 289 ASN A N   1 
ATOM   2269  C CA  . ASN A 1 287 ? -1.975  50.285  16.765  1.00 61.60  ? 289 ASN A CA  1 
ATOM   2270  C C   . ASN A 1 287 ? -3.328  49.615  16.556  1.00 60.02  ? 289 ASN A C   1 
ATOM   2271  O O   . ASN A 1 287 ? -3.857  49.600  15.441  1.00 54.81  ? 289 ASN A O   1 
ATOM   2272  C CB  . ASN A 1 287 ? -1.899  51.649  16.081  1.00 60.99  ? 289 ASN A CB  1 
ATOM   2273  C CG  . ASN A 1 287 ? -3.009  52.599  16.522  1.00 83.56  ? 289 ASN A CG  1 
ATOM   2274  O OD1 . ASN A 1 287 ? -3.400  53.502  15.777  1.00 91.14  ? 289 ASN A OD1 1 
ATOM   2275  N ND2 . ASN A 1 287 ? -3.507  52.409  17.741  1.00 76.56  ? 289 ASN A ND2 1 
ATOM   2276  N N   . SER A 1 288 ? -3.884  49.050  17.624  1.00 57.79  ? 290 SER A N   1 
ATOM   2277  C CA  . SER A 1 288 ? -5.095  48.259  17.463  1.00 60.95  ? 290 SER A CA  1 
ATOM   2278  C C   . SER A 1 288 ? -5.858  48.187  18.776  1.00 57.77  ? 290 SER A C   1 
ATOM   2279  O O   . SER A 1 288 ? -5.294  48.350  19.862  1.00 55.61  ? 290 SER A O   1 
ATOM   2280  C CB  . SER A 1 288 ? -4.762  46.850  16.966  1.00 58.47  ? 290 SER A CB  1 
ATOM   2281  O OG  . SER A 1 288 ? -5.685  45.898  17.460  1.00 68.79  ? 290 SER A OG  1 
ATOM   2282  N N   . SER A 1 289 ? -7.161  47.944  18.650  1.00 62.44  ? 291 SER A N   1 
ATOM   2283  C CA  . SER A 1 289 ? -8.006  47.569  19.772  1.00 56.57  ? 291 SER A CA  1 
ATOM   2284  C C   . SER A 1 289 ? -8.536  46.149  19.630  1.00 49.30  ? 291 SER A C   1 
ATOM   2285  O O   . SER A 1 289 ? -9.284  45.690  20.501  1.00 56.04  ? 291 SER A O   1 
ATOM   2286  C CB  . SER A 1 289 ? -9.177  48.550  19.911  1.00 62.16  ? 291 SER A CB  1 
ATOM   2287  O OG  . SER A 1 289 ? -9.947  48.580  18.721  1.00 70.96  ? 291 SER A OG  1 
ATOM   2288  N N   . MET A 1 290 ? -8.170  45.446  18.561  1.00 46.14  ? 292 MET A N   1 
ATOM   2289  C CA  . MET A 1 290 ? -8.645  44.092  18.333  1.00 50.25  ? 292 MET A CA  1 
ATOM   2290  C C   . MET A 1 290 ? -8.058  43.134  19.371  1.00 53.28  ? 292 MET A C   1 
ATOM   2291  O O   . MET A 1 290 ? -6.915  43.300  19.806  1.00 46.09  ? 292 MET A O   1 
ATOM   2292  C CB  . MET A 1 290 ? -8.270  43.640  16.924  1.00 45.68  ? 292 MET A CB  1 
ATOM   2293  C CG  . MET A 1 290 ? -9.120  44.271  15.826  1.00 54.64  ? 292 MET A CG  1 
ATOM   2294  S SD  . MET A 1 290 ? -10.880 44.317  16.232  1.00 73.94  ? 292 MET A SD  1 
ATOM   2295  C CE  . MET A 1 290 ? -11.323 45.992  15.781  1.00 55.87  ? 292 MET A CE  1 
ATOM   2296  N N   . PRO A 1 291 ? -8.823  42.121  19.790  1.00 46.30  ? 293 PRO A N   1 
ATOM   2297  C CA  . PRO A 1 291 ? -8.338  41.238  20.864  1.00 48.75  ? 293 PRO A CA  1 
ATOM   2298  C C   . PRO A 1 291 ? -7.235  40.281  20.438  1.00 42.59  ? 293 PRO A C   1 
ATOM   2299  O O   . PRO A 1 291 ? -6.516  39.780  21.311  1.00 43.67  ? 293 PRO A O   1 
ATOM   2300  C CB  . PRO A 1 291 ? -9.603  40.476  21.292  1.00 36.57  ? 293 PRO A CB  1 
ATOM   2301  C CG  . PRO A 1 291 ? -10.465 40.486  20.084  1.00 37.16  ? 293 PRO A CG  1 
ATOM   2302  C CD  . PRO A 1 291 ? -10.203 41.800  19.389  1.00 46.95  ? 293 PRO A CD  1 
ATOM   2303  N N   . PHE A 1 292 ? -7.073  40.005  19.145  1.00 45.81  ? 294 PHE A N   1 
ATOM   2304  C CA  . PHE A 1 292 ? -6.093  39.032  18.683  1.00 46.06  ? 294 PHE A CA  1 
ATOM   2305  C C   . PHE A 1 292 ? -5.294  39.591  17.516  1.00 50.03  ? 294 PHE A C   1 
ATOM   2306  O O   . PHE A 1 292 ? -5.771  40.450  16.768  1.00 49.12  ? 294 PHE A O   1 
ATOM   2307  C CB  . PHE A 1 292 ? -6.763  37.715  18.260  1.00 41.74  ? 294 PHE A CB  1 
ATOM   2308  C CG  . PHE A 1 292 ? -7.719  37.170  19.281  1.00 44.06  ? 294 PHE A CG  1 
ATOM   2309  C CD1 . PHE A 1 292 ? -7.253  36.473  20.379  1.00 43.89  ? 294 PHE A CD1 1 
ATOM   2310  C CD2 . PHE A 1 292 ? -9.087  37.364  19.145  1.00 47.70  ? 294 PHE A CD2 1 
ATOM   2311  C CE1 . PHE A 1 292 ? -8.130  35.974  21.325  1.00 39.21  ? 294 PHE A CE1 1 
ATOM   2312  C CE2 . PHE A 1 292 ? -9.967  36.866  20.086  1.00 47.05  ? 294 PHE A CE2 1 
ATOM   2313  C CZ  . PHE A 1 292 ? -9.485  36.173  21.180  1.00 40.72  ? 294 PHE A CZ  1 
ATOM   2314  N N   . HIS A 1 293 ? -4.069  39.085  17.370  1.00 42.56  ? 295 HIS A N   1 
ATOM   2315  C CA  . HIS A 1 293 ? -3.213  39.423  16.241  1.00 40.52  ? 295 HIS A CA  1 
ATOM   2316  C C   . HIS A 1 293 ? -2.399  38.194  15.855  1.00 45.59  ? 295 HIS A C   1 
ATOM   2317  O O   . HIS A 1 293 ? -2.360  37.193  16.575  1.00 45.99  ? 295 HIS A O   1 
ATOM   2318  C CB  . HIS A 1 293 ? -2.294  40.604  16.562  1.00 43.73  ? 295 HIS A CB  1 
ATOM   2319  C CG  . HIS A 1 293 ? -1.125  40.236  17.419  1.00 40.09  ? 295 HIS A CG  1 
ATOM   2320  N ND1 . HIS A 1 293 ? 0.108   39.909  16.899  1.00 40.40  ? 295 HIS A ND1 1 
ATOM   2321  C CD2 . HIS A 1 293 ? -1.007  40.133  18.764  1.00 36.52  ? 295 HIS A CD2 1 
ATOM   2322  C CE1 . HIS A 1 293 ? 0.939   39.628  17.887  1.00 45.37  ? 295 HIS A CE1 1 
ATOM   2323  N NE2 . HIS A 1 293 ? 0.287   39.754  19.029  1.00 49.66  ? 295 HIS A NE2 1 
ATOM   2324  N N   . ASN A 1 294 ? -1.745  38.280  14.693  1.00 44.11  ? 296 ASN A N   1 
ATOM   2325  C CA  . ASN A 1 294 ? -0.891  37.199  14.218  1.00 44.01  ? 296 ASN A CA  1 
ATOM   2326  C C   . ASN A 1 294 ? 0.418   37.735  13.643  1.00 47.78  ? 296 ASN A C   1 
ATOM   2327  O O   . ASN A 1 294 ? 1.024   37.100  12.775  1.00 49.46  ? 296 ASN A O   1 
ATOM   2328  C CB  . ASN A 1 294 ? -1.612  36.341  13.173  1.00 37.12  ? 296 ASN A CB  1 
ATOM   2329  C CG  . ASN A 1 294 ? -1.968  37.119  11.914  1.00 50.33  ? 296 ASN A CG  1 
ATOM   2330  O OD1 . ASN A 1 294 ? -1.818  38.343  11.856  1.00 52.06  ? 296 ASN A OD1 1 
ATOM   2331  N ND2 . ASN A 1 294 ? -2.452  36.407  10.899  1.00 46.92  ? 296 ASN A ND2 1 
ATOM   2332  N N   . ILE A 1 295 ? 0.871   38.895  14.122  1.00 45.28  ? 297 ILE A N   1 
ATOM   2333  C CA  . ILE A 1 295 ? 2.038   39.550  13.532  1.00 48.61  ? 297 ILE A CA  1 
ATOM   2334  C C   . ILE A 1 295 ? 3.318   38.806  13.897  1.00 45.35  ? 297 ILE A C   1 
ATOM   2335  O O   . ILE A 1 295 ? 4.074   38.365  13.025  1.00 48.38  ? 297 ILE A O   1 
ATOM   2336  C CB  . ILE A 1 295 ? 2.108   41.023  13.975  1.00 48.19  ? 297 ILE A CB  1 
ATOM   2337  C CG1 . ILE A 1 295 ? 0.735   41.675  13.853  1.00 43.94  ? 297 ILE A CG1 1 
ATOM   2338  C CG2 . ILE A 1 295 ? 3.137   41.788  13.149  1.00 46.68  ? 297 ILE A CG2 1 
ATOM   2339  C CD1 . ILE A 1 295 ? 0.277   41.818  12.434  1.00 49.71  ? 297 ILE A CD1 1 
ATOM   2340  N N   . HIS A 1 296 ? 3.576   38.661  15.190  1.00 41.14  ? 298 HIS A N   1 
ATOM   2341  C CA  . HIS A 1 296 ? 4.860   38.203  15.697  1.00 43.03  ? 298 HIS A CA  1 
ATOM   2342  C C   . HIS A 1 296 ? 4.696   37.833  17.165  1.00 48.43  ? 298 HIS A C   1 
ATOM   2343  O O   . HIS A 1 296 ? 3.941   38.497  17.887  1.00 40.31  ? 298 HIS A O   1 
ATOM   2344  C CB  . HIS A 1 296 ? 5.917   39.301  15.523  1.00 48.57  ? 298 HIS A CB  1 
ATOM   2345  C CG  . HIS A 1 296 ? 7.326   38.796  15.464  1.00 49.41  ? 298 HIS A CG  1 
ATOM   2346  N ND1 . HIS A 1 296 ? 8.063   38.507  16.594  1.00 55.41  ? 298 HIS A ND1 1 
ATOM   2347  C CD2 . HIS A 1 296 ? 8.140   38.547  14.411  1.00 52.23  ? 298 HIS A CD2 1 
ATOM   2348  C CE1 . HIS A 1 296 ? 9.266   38.092  16.239  1.00 44.09  ? 298 HIS A CE1 1 
ATOM   2349  N NE2 . HIS A 1 296 ? 9.339   38.107  14.920  1.00 51.34  ? 298 HIS A NE2 1 
ATOM   2350  N N   . PRO A 1 297 ? 5.377   36.788  17.646  1.00 38.27  ? 299 PRO A N   1 
ATOM   2351  C CA  . PRO A 1 297 ? 5.243   36.418  19.063  1.00 42.91  ? 299 PRO A CA  1 
ATOM   2352  C C   . PRO A 1 297 ? 6.068   37.261  20.023  1.00 47.44  ? 299 PRO A C   1 
ATOM   2353  O O   . PRO A 1 297 ? 5.696   37.359  21.200  1.00 52.94  ? 299 PRO A O   1 
ATOM   2354  C CB  . PRO A 1 297 ? 5.712   34.957  19.087  1.00 49.61  ? 299 PRO A CB  1 
ATOM   2355  C CG  . PRO A 1 297 ? 6.683   34.869  17.954  1.00 42.51  ? 299 PRO A CG  1 
ATOM   2356  C CD  . PRO A 1 297 ? 6.174   35.811  16.886  1.00 40.20  ? 299 PRO A CD  1 
ATOM   2357  N N   . LEU A 1 298 ? 7.170   37.864  19.582  1.00 46.13  ? 300 LEU A N   1 
ATOM   2358  C CA  . LEU A 1 298 ? 8.070   38.572  20.498  1.00 46.69  ? 300 LEU A CA  1 
ATOM   2359  C C   . LEU A 1 298 ? 7.691   40.054  20.568  1.00 46.80  ? 300 LEU A C   1 
ATOM   2360  O O   . LEU A 1 298 ? 8.371   40.938  20.044  1.00 54.19  ? 300 LEU A O   1 
ATOM   2361  C CB  . LEU A 1 298 ? 9.519   38.380  20.065  1.00 52.07  ? 300 LEU A CB  1 
ATOM   2362  C CG  . LEU A 1 298 ? 9.956   36.952  19.721  1.00 59.30  ? 300 LEU A CG  1 
ATOM   2363  C CD1 . LEU A 1 298 ? 11.388  36.935  19.190  1.00 34.43  ? 300 LEU A CD1 1 
ATOM   2364  C CD2 . LEU A 1 298 ? 9.820   36.034  20.930  1.00 43.27  ? 300 LEU A CD2 1 
ATOM   2365  N N   . THR A 1 299 ? 6.582   40.318  21.252  1.00 49.08  ? 301 THR A N   1 
ATOM   2366  C CA  . THR A 1 299 ? 6.029   41.662  21.337  1.00 48.01  ? 301 THR A CA  1 
ATOM   2367  C C   . THR A 1 299 ? 6.417   42.331  22.651  1.00 43.61  ? 301 THR A C   1 
ATOM   2368  O O   . THR A 1 299 ? 6.669   41.670  23.662  1.00 42.33  ? 301 THR A O   1 
ATOM   2369  C CB  . THR A 1 299 ? 4.502   41.643  21.203  1.00 37.74  ? 301 THR A CB  1 
ATOM   2370  O OG1 . THR A 1 299 ? 3.931   40.877  22.271  1.00 46.31  ? 301 THR A OG1 1 
ATOM   2371  C CG2 . THR A 1 299 ? 4.096   41.034  19.881  1.00 39.07  ? 301 THR A CG2 1 
ATOM   2372  N N   . ILE A 1 300 ? 6.472   43.660  22.621  1.00 43.23  ? 302 ILE A N   1 
ATOM   2373  C CA  . ILE A 1 300 ? 6.773   44.464  23.798  1.00 44.19  ? 302 ILE A CA  1 
ATOM   2374  C C   . ILE A 1 300 ? 5.685   45.517  23.932  1.00 44.48  ? 302 ILE A C   1 
ATOM   2375  O O   . ILE A 1 300 ? 5.440   46.280  22.991  1.00 48.37  ? 302 ILE A O   1 
ATOM   2376  C CB  . ILE A 1 300 ? 8.158   45.125  23.714  1.00 45.85  ? 302 ILE A CB  1 
ATOM   2377  C CG1 . ILE A 1 300 ? 9.256   44.064  23.694  1.00 43.14  ? 302 ILE A CG1 1 
ATOM   2378  C CG2 . ILE A 1 300 ? 8.369   46.074  24.881  1.00 41.88  ? 302 ILE A CG2 1 
ATOM   2379  C CD1 . ILE A 1 300 ? 10.612  44.629  23.330  1.00 51.58  ? 302 ILE A CD1 1 
ATOM   2380  N N   . GLY A 1 301 ? 5.036   45.559  25.094  1.00 46.83  ? 303 GLY A N   1 
ATOM   2381  C CA  . GLY A 1 301 ? 3.973   46.516  25.333  1.00 48.69  ? 303 GLY A CA  1 
ATOM   2382  C C   . GLY A 1 301 ? 2.644   45.875  25.673  1.00 47.66  ? 303 GLY A C   1 
ATOM   2383  O O   . GLY A 1 301 ? 2.597   44.738  26.151  1.00 48.40  ? 303 GLY A O   1 
ATOM   2384  N N   . GLU A 1 302 ? 1.556   46.610  25.449  1.00 58.75  ? 304 GLU A N   1 
ATOM   2385  C CA  . GLU A 1 302 ? 0.196   46.117  25.659  1.00 49.20  ? 304 GLU A CA  1 
ATOM   2386  C C   . GLU A 1 302 ? -0.358  45.715  24.299  1.00 45.66  ? 304 GLU A C   1 
ATOM   2387  O O   . GLU A 1 302 ? -0.761  46.565  23.501  1.00 48.59  ? 304 GLU A O   1 
ATOM   2388  C CB  . GLU A 1 302 ? -0.673  47.173  26.331  1.00 54.65  ? 304 GLU A CB  1 
ATOM   2389  C CG  . GLU A 1 302 ? -0.327  47.419  27.785  1.00 57.68  ? 304 GLU A CG  1 
ATOM   2390  C CD  . GLU A 1 302 ? -1.241  48.441  28.431  1.00 90.17  ? 304 GLU A CD  1 
ATOM   2391  O OE1 . GLU A 1 302 ? -2.112  48.034  29.233  1.00 81.63  ? 304 GLU A OE1 1 
ATOM   2392  O OE2 . GLU A 1 302 ? -1.084  49.648  28.141  1.00 91.73  ? 304 GLU A OE2 1 
ATOM   2393  N N   . CYS A 1 303 ? -0.394  44.418  24.047  1.00 44.97  ? 305 CYS A N   1 
ATOM   2394  C CA  . CYS A 1 303 ? -0.649  43.886  22.723  1.00 52.92  ? 305 CYS A CA  1 
ATOM   2395  C C   . CYS A 1 303 ? -1.835  42.934  22.752  1.00 44.66  ? 305 CYS A C   1 
ATOM   2396  O O   . CYS A 1 303 ? -2.212  42.429  23.816  1.00 40.75  ? 305 CYS A O   1 
ATOM   2397  C CB  . CYS A 1 303 ? 0.597   43.158  22.199  1.00 45.28  ? 305 CYS A CB  1 
ATOM   2398  S SG  . CYS A 1 303 ? 2.058   44.238  22.045  1.00 78.02  ? 305 CYS A SG  1 
ATOM   2399  N N   . PRO A 1 304 ? -2.471  42.697  21.608  1.00 48.51  ? 306 PRO A N   1 
ATOM   2400  C CA  . PRO A 1 304 ? -3.484  41.640  21.542  1.00 45.57  ? 306 PRO A CA  1 
ATOM   2401  C C   . PRO A 1 304 ? -2.845  40.277  21.766  1.00 57.17  ? 306 PRO A C   1 
ATOM   2402  O O   . PRO A 1 304 ? -1.625  40.109  21.690  1.00 43.36  ? 306 PRO A O   1 
ATOM   2403  C CB  . PRO A 1 304 ? -4.052  41.769  20.122  1.00 43.24  ? 306 PRO A CB  1 
ATOM   2404  C CG  . PRO A 1 304 ? -3.691  43.167  19.686  1.00 54.70  ? 306 PRO A CG  1 
ATOM   2405  C CD  . PRO A 1 304 ? -2.385  43.467  20.353  1.00 55.53  ? 306 PRO A CD  1 
ATOM   2406  N N   . LYS A 1 305 ? -3.688  39.297  22.078  1.00 49.89  ? 307 LYS A N   1 
ATOM   2407  C CA  . LYS A 1 305 ? -3.194  37.943  22.278  1.00 47.83  ? 307 LYS A CA  1 
ATOM   2408  C C   . LYS A 1 305 ? -2.776  37.344  20.941  1.00 49.33  ? 307 LYS A C   1 
ATOM   2409  O O   . LYS A 1 305 ? -3.518  37.416  19.955  1.00 42.92  ? 307 LYS A O   1 
ATOM   2410  C CB  . LYS A 1 305 ? -4.263  37.083  22.947  1.00 45.82  ? 307 LYS A CB  1 
ATOM   2411  C CG  . LYS A 1 305 ? -4.681  37.598  24.315  1.00 50.95  ? 307 LYS A CG  1 
ATOM   2412  C CD  . LYS A 1 305 ? -3.471  37.993  25.147  1.00 38.93  ? 307 LYS A CD  1 
ATOM   2413  C CE  . LYS A 1 305 ? -3.883  38.553  26.498  1.00 51.17  ? 307 LYS A CE  1 
ATOM   2414  N NZ  . LYS A 1 305 ? -4.414  39.940  26.393  1.00 64.34  ? 307 LYS A NZ  1 
ATOM   2415  N N   . TYR A 1 306 ? -1.574  36.775  20.905  1.00 42.04  ? 308 TYR A N   1 
ATOM   2416  C CA  . TYR A 1 306 ? -1.049  36.172  19.687  1.00 40.39  ? 308 TYR A CA  1 
ATOM   2417  C C   . TYR A 1 306 ? -1.747  34.843  19.425  1.00 35.62  ? 308 TYR A C   1 
ATOM   2418  O O   . TYR A 1 306 ? -1.909  34.031  20.341  1.00 39.69  ? 308 TYR A O   1 
ATOM   2419  C CB  . TYR A 1 306 ? 0.462   35.970  19.811  1.00 28.79  ? 308 TYR A CB  1 
ATOM   2420  C CG  . TYR A 1 306 ? 1.133   35.485  18.547  1.00 47.89  ? 308 TYR A CG  1 
ATOM   2421  C CD1 . TYR A 1 306 ? 0.955   36.153  17.341  1.00 40.84  ? 308 TYR A CD1 1 
ATOM   2422  C CD2 . TYR A 1 306 ? 1.952   34.362  18.559  1.00 50.73  ? 308 TYR A CD2 1 
ATOM   2423  C CE1 . TYR A 1 306 ? 1.573   35.713  16.181  1.00 37.81  ? 308 TYR A CE1 1 
ATOM   2424  C CE2 . TYR A 1 306 ? 2.572   33.915  17.406  1.00 48.61  ? 308 TYR A CE2 1 
ATOM   2425  C CZ  . TYR A 1 306 ? 2.378   34.593  16.219  1.00 52.17  ? 308 TYR A CZ  1 
ATOM   2426  O OH  . TYR A 1 306 ? 2.994   34.152  15.066  1.00 49.60  ? 308 TYR A OH  1 
ATOM   2427  N N   . VAL A 1 307 ? -2.167  34.624  18.177  1.00 36.54  ? 309 VAL A N   1 
ATOM   2428  C CA  . VAL A 1 307 ? -2.803  33.375  17.768  1.00 46.05  ? 309 VAL A CA  1 
ATOM   2429  C C   . VAL A 1 307 ? -2.220  32.925  16.438  1.00 44.29  ? 309 VAL A C   1 
ATOM   2430  O O   . VAL A 1 307 ? -1.610  33.705  15.703  1.00 43.11  ? 309 VAL A O   1 
ATOM   2431  C CB  . VAL A 1 307 ? -4.340  33.493  17.629  1.00 36.93  ? 309 VAL A CB  1 
ATOM   2432  C CG1 . VAL A 1 307 ? -4.994  33.829  18.967  1.00 34.40  ? 309 VAL A CG1 1 
ATOM   2433  C CG2 . VAL A 1 307 ? -4.680  34.532  16.579  1.00 29.68  ? 309 VAL A CG2 1 
ATOM   2434  N N   . LYS A 1 308 ? -2.427  31.647  16.126  1.00 40.35  ? 310 LYS A N   1 
ATOM   2435  C CA  . LYS A 1 308 ? -2.070  31.095  14.819  1.00 48.30  ? 310 LYS A CA  1 
ATOM   2436  C C   . LYS A 1 308 ? -3.360  30.998  14.009  1.00 48.88  ? 310 LYS A C   1 
ATOM   2437  O O   . LYS A 1 308 ? -4.051  29.979  14.015  1.00 53.24  ? 310 LYS A O   1 
ATOM   2438  C CB  . LYS A 1 308 ? -1.370  29.746  14.950  1.00 46.12  ? 310 LYS A CB  1 
ATOM   2439  C CG  . LYS A 1 308 ? -1.171  29.021  13.622  1.00 53.30  ? 310 LYS A CG  1 
ATOM   2440  C CD  . LYS A 1 308 ? -0.711  27.587  13.846  1.00 74.80  ? 310 LYS A CD  1 
ATOM   2441  C CE  . LYS A 1 308 ? 0.287   27.126  12.791  1.00 70.31  ? 310 LYS A CE  1 
ATOM   2442  N NZ  . LYS A 1 308 ? 1.343   26.243  13.373  1.00 76.45  ? 310 LYS A NZ  1 
ATOM   2443  N N   . SER A 1 309 ? -3.692  32.085  13.322  1.00 45.58  ? 311 SER A N   1 
ATOM   2444  C CA  . SER A 1 309 ? -4.897  32.146  12.516  1.00 41.47  ? 311 SER A CA  1 
ATOM   2445  C C   . SER A 1 309 ? -4.694  33.166  11.408  1.00 53.90  ? 311 SER A C   1 
ATOM   2446  O O   . SER A 1 309 ? -3.842  34.056  11.501  1.00 46.88  ? 311 SER A O   1 
ATOM   2447  C CB  . SER A 1 309 ? -6.120  32.509  13.363  1.00 45.04  ? 311 SER A CB  1 
ATOM   2448  O OG  . SER A 1 309 ? -7.284  32.563  12.561  1.00 53.47  ? 311 SER A OG  1 
ATOM   2449  N N   . ASN A 1 310 ? -5.497  33.034  10.353  1.00 50.84  ? 312 ASN A N   1 
ATOM   2450  C CA  . ASN A 1 310 ? -5.450  33.980  9.250   1.00 50.95  ? 312 ASN A CA  1 
ATOM   2451  C C   . ASN A 1 310 ? -6.634  34.933  9.216   1.00 56.32  ? 312 ASN A C   1 
ATOM   2452  O O   . ASN A 1 310 ? -6.529  35.996  8.596   1.00 57.35  ? 312 ASN A O   1 
ATOM   2453  C CB  . ASN A 1 310 ? -5.357  33.234  7.912   1.00 51.41  ? 312 ASN A CB  1 
ATOM   2454  C CG  . ASN A 1 310 ? -3.961  32.683  7.653   1.00 64.91  ? 312 ASN A CG  1 
ATOM   2455  O OD1 . ASN A 1 310 ? -2.969  33.206  8.167   1.00 61.78  ? 312 ASN A OD1 1 
ATOM   2456  N ND2 . ASN A 1 310 ? -3.879  31.625  6.856   1.00 70.03  ? 312 ASN A ND2 1 
ATOM   2457  N N   . LYS A 1 311 ? -7.740  34.591  9.873   1.00 55.27  ? 313 LYS A N   1 
ATOM   2458  C CA  . LYS A 1 311 ? -8.902  35.463  9.930   1.00 53.79  ? 313 LYS A CA  1 
ATOM   2459  C C   . LYS A 1 311 ? -9.793  35.017  11.079  1.00 47.48  ? 313 LYS A C   1 
ATOM   2460  O O   . LYS A 1 311 ? -9.898  33.819  11.362  1.00 49.25  ? 313 LYS A O   1 
ATOM   2461  C CB  . LYS A 1 311 ? -9.688  35.449  8.609   1.00 47.75  ? 313 LYS A CB  1 
ATOM   2462  C CG  . LYS A 1 311 ? -9.895  34.064  8.012   1.00 52.32  ? 313 LYS A CG  1 
ATOM   2463  C CD  . LYS A 1 311 ? -10.924 34.078  6.884   1.00 53.01  ? 313 LYS A CD  1 
ATOM   2464  C CE  . LYS A 1 311 ? -11.161 32.671  6.341   1.00 66.41  ? 313 LYS A CE  1 
ATOM   2465  N NZ  . LYS A 1 311 ? -12.282 31.970  7.041   1.00 71.12  ? 313 LYS A NZ  1 
ATOM   2466  N N   . LEU A 1 312 ? -10.420 35.988  11.741  1.00 44.73  ? 314 LEU A N   1 
ATOM   2467  C CA  . LEU A 1 312 ? -11.461 35.749  12.743  1.00 49.45  ? 314 LEU A CA  1 
ATOM   2468  C C   . LEU A 1 312 ? -12.627 36.664  12.380  1.00 49.74  ? 314 LEU A C   1 
ATOM   2469  O O   . LEU A 1 312 ? -12.764 37.760  12.931  1.00 53.97  ? 314 LEU A O   1 
ATOM   2470  C CB  . LEU A 1 312 ? -10.947 36.004  14.154  1.00 45.04  ? 314 LEU A CB  1 
ATOM   2471  C CG  . LEU A 1 312 ? -9.672  35.253  14.538  1.00 43.17  ? 314 LEU A CG  1 
ATOM   2472  C CD1 . LEU A 1 312 ? -9.061  35.848  15.802  1.00 39.91  ? 314 LEU A CD1 1 
ATOM   2473  C CD2 . LEU A 1 312 ? -9.964  33.765  14.716  1.00 37.23  ? 314 LEU A CD2 1 
ATOM   2474  N N   . VAL A 1 313 ? -13.476 36.209  11.466  1.00 38.21  ? 315 VAL A N   1 
ATOM   2475  C CA  . VAL A 1 313 ? -14.469 37.062  10.825  1.00 48.73  ? 315 VAL A CA  1 
ATOM   2476  C C   . VAL A 1 313 ? -15.812 36.845  11.511  1.00 48.86  ? 315 VAL A C   1 
ATOM   2477  O O   . VAL A 1 313 ? -16.446 35.797  11.349  1.00 45.00  ? 315 VAL A O   1 
ATOM   2478  C CB  . VAL A 1 313 ? -14.555 36.780  9.320   1.00 52.69  ? 315 VAL A CB  1 
ATOM   2479  C CG1 . VAL A 1 313 ? -15.634 37.639  8.681   1.00 43.53  ? 315 VAL A CG1 1 
ATOM   2480  C CG2 . VAL A 1 313 ? -13.197 37.019  8.662   1.00 38.46  ? 315 VAL A CG2 1 
ATOM   2481  N N   . LEU A 1 314 ? -16.254 37.845  12.270  1.00 43.28  ? 316 LEU A N   1 
ATOM   2482  C CA  . LEU A 1 314 ? -17.550 37.789  12.930  1.00 41.54  ? 316 LEU A CA  1 
ATOM   2483  C C   . LEU A 1 314 ? -18.639 38.245  11.974  1.00 44.05  ? 316 LEU A C   1 
ATOM   2484  O O   . LEU A 1 314 ? -18.515 39.292  11.330  1.00 45.80  ? 316 LEU A O   1 
ATOM   2485  C CB  . LEU A 1 314 ? -17.559 38.671  14.177  1.00 39.78  ? 316 LEU A CB  1 
ATOM   2486  C CG  . LEU A 1 314 ? -16.983 38.054  15.445  1.00 45.33  ? 316 LEU A CG  1 
ATOM   2487  C CD1 . LEU A 1 314 ? -16.891 39.103  16.537  1.00 49.60  ? 316 LEU A CD1 1 
ATOM   2488  C CD2 . LEU A 1 314 ? -17.835 36.882  15.886  1.00 35.31  ? 316 LEU A CD2 1 
ATOM   2489  N N   . ALA A 1 315 ? -19.704 37.459  11.877  1.00 45.15  ? 317 ALA A N   1 
ATOM   2490  C CA  . ALA A 1 315 ? -20.856 37.887  11.102  1.00 42.73  ? 317 ALA A CA  1 
ATOM   2491  C C   . ALA A 1 315 ? -21.609 38.970  11.860  1.00 38.53  ? 317 ALA A C   1 
ATOM   2492  O O   . ALA A 1 315 ? -21.844 38.850  13.066  1.00 37.67  ? 317 ALA A O   1 
ATOM   2493  C CB  . ALA A 1 315 ? -21.776 36.703  10.812  1.00 44.32  ? 317 ALA A CB  1 
ATOM   2494  N N   . THR A 1 316 ? -21.967 40.039  11.157  1.00 44.75  ? 318 THR A N   1 
ATOM   2495  C CA  . THR A 1 316 ? -22.851 41.064  11.697  1.00 53.60  ? 318 THR A CA  1 
ATOM   2496  C C   . THR A 1 316 ? -24.179 41.145  10.965  1.00 57.41  ? 318 THR A C   1 
ATOM   2497  O O   . THR A 1 316 ? -25.221 41.309  11.605  1.00 56.16  ? 318 THR A O   1 
ATOM   2498  C CB  . THR A 1 316 ? -22.166 42.436  11.663  1.00 46.24  ? 318 THR A CB  1 
ATOM   2499  O OG1 . THR A 1 316 ? -21.506 42.618  10.405  1.00 63.42  ? 318 THR A OG1 1 
ATOM   2500  C CG2 . THR A 1 316 ? -21.145 42.533  12.775  1.00 41.71  ? 318 THR A CG2 1 
ATOM   2501  N N   . GLY A 1 317 ? -24.176 41.007  9.645   1.00 56.26  ? 319 GLY A N   1 
ATOM   2502  C CA  . GLY A 1 317 ? -25.394 41.068  8.864   1.00 44.97  ? 319 GLY A CA  1 
ATOM   2503  C C   . GLY A 1 317 ? -26.112 39.735  8.813   1.00 43.92  ? 319 GLY A C   1 
ATOM   2504  O O   . GLY A 1 317 ? -25.875 38.832  9.618   1.00 56.48  ? 319 GLY A O   1 
ATOM   2505  N N   . LEU A 1 318 ? -27.008 39.620  7.842   1.00 50.94  ? 320 LEU A N   1 
ATOM   2506  C CA  . LEU A 1 318 ? -27.870 38.460  7.684   1.00 51.00  ? 320 LEU A CA  1 
ATOM   2507  C C   . LEU A 1 318 ? -27.266 37.472  6.691   1.00 44.32  ? 320 LEU A C   1 
ATOM   2508  O O   . LEU A 1 318 ? -26.321 37.780  5.963   1.00 40.20  ? 320 LEU A O   1 
ATOM   2509  C CB  . LEU A 1 318 ? -29.263 38.888  7.213   1.00 35.93  ? 320 LEU A CB  1 
ATOM   2510  C CG  . LEU A 1 318 ? -29.975 39.960  8.041   1.00 52.88  ? 320 LEU A CG  1 
ATOM   2511  C CD1 . LEU A 1 318 ? -29.659 41.357  7.523   1.00 54.66  ? 320 LEU A CD1 1 
ATOM   2512  C CD2 . LEU A 1 318 ? -31.474 39.714  8.021   1.00 48.93  ? 320 LEU A CD2 1 
ATOM   2513  N N   . ARG A 1 319 ? -27.842 36.273  6.661   1.00 38.92  ? 321 ARG A N   1 
ATOM   2514  C CA  . ARG A 1 319 ? -27.484 35.285  5.653   1.00 46.50  ? 321 ARG A CA  1 
ATOM   2515  C C   . ARG A 1 319 ? -27.898 35.810  4.284   1.00 47.54  ? 321 ARG A C   1 
ATOM   2516  O O   . ARG A 1 319 ? -29.090 35.869  3.968   1.00 61.74  ? 321 ARG A O   1 
ATOM   2517  C CB  . ARG A 1 319 ? -28.159 33.948  5.953   1.00 47.57  ? 321 ARG A CB  1 
ATOM   2518  C CG  . ARG A 1 319 ? -28.003 32.914  4.846   1.00 46.31  ? 321 ARG A CG  1 
ATOM   2519  C CD  . ARG A 1 319 ? -28.913 31.710  5.071   1.00 38.04  ? 321 ARG A CD  1 
ATOM   2520  N NE  . ARG A 1 319 ? -28.722 31.135  6.396   1.00 56.32  ? 321 ARG A NE  1 
ATOM   2521  C CZ  . ARG A 1 319 ? -27.826 30.199  6.677   1.00 49.70  ? 321 ARG A CZ  1 
ATOM   2522  N NH1 . ARG A 1 319 ? -27.035 29.699  5.742   1.00 47.52  ? 321 ARG A NH1 1 
ATOM   2523  N NH2 . ARG A 1 319 ? -27.719 29.757  7.927   1.00 38.05  ? 321 ARG A NH2 1 
ATOM   2524  N N   . ASN A 1 320 ? -26.918 36.205  3.479   1.00 51.51  ? 322 ASN A N   1 
ATOM   2525  C CA  . ASN A 1 320 ? -27.192 36.815  2.188   1.00 50.21  ? 322 ASN A CA  1 
ATOM   2526  C C   . ASN A 1 320 ? -27.602 35.765  1.164   1.00 46.94  ? 322 ASN A C   1 
ATOM   2527  O O   . ASN A 1 320 ? -27.152 34.618  1.205   1.00 58.03  ? 322 ASN A O   1 
ATOM   2528  C CB  . ASN A 1 320 ? -25.964 37.578  1.692   1.00 52.56  ? 322 ASN A CB  1 
ATOM   2529  C CG  . ASN A 1 320 ? -26.308 38.606  0.634   1.00 56.54  ? 322 ASN A CG  1 
ATOM   2530  O OD1 . ASN A 1 320 ? -27.474 38.782  0.278   1.00 60.70  ? 322 ASN A OD1 1 
ATOM   2531  N ND2 . ASN A 1 320 ? -25.291 39.297  0.129   1.00 59.22  ? 322 ASN A ND2 1 
ATOM   2532  N N   . SER A 1 321 ? -28.461 36.174  0.234   1.00 65.96  ? 323 SER A N   1 
ATOM   2533  C CA  . SER A 1 321 ? -28.921 35.281  -0.828  1.00 67.80  ? 323 SER A CA  1 
ATOM   2534  C C   . SER A 1 321 ? -28.793 35.931  -2.204  1.00 60.06  ? 323 SER A C   1 
ATOM   2535  O O   . SER A 1 321 ? -28.456 35.267  -3.184  1.00 58.56  ? 323 SER A O   1 
ATOM   2536  C CB  . SER A 1 321 ? -30.370 34.859  -0.581  1.00 75.80  ? 323 SER A CB  1 
ATOM   2537  O OG  . SER A 1 321 ? -31.105 35.902  0.039   1.00 62.21  ? 323 SER A OG  1 
ATOM   2538  N N   . GLY B 2 1   ? -32.372 27.881  9.397   1.00 48.12  ? 1   GLY B N   1 
ATOM   2539  C CA  . GLY B 2 1   ? -32.058 28.382  10.723  1.00 51.95  ? 1   GLY B CA  1 
ATOM   2540  C C   . GLY B 2 1   ? -32.919 27.757  11.803  1.00 54.26  ? 1   GLY B C   1 
ATOM   2541  O O   . GLY B 2 1   ? -33.880 27.042  11.497  1.00 43.48  ? 1   GLY B O   1 
ATOM   2542  N N   . LEU B 2 2   ? -32.578 28.033  13.066  1.00 44.11  ? 2   LEU B N   1 
ATOM   2543  C CA  . LEU B 2 2   ? -33.316 27.443  14.180  1.00 47.64  ? 2   LEU B CA  1 
ATOM   2544  C C   . LEU B 2 2   ? -34.794 27.804  14.104  1.00 52.24  ? 2   LEU B C   1 
ATOM   2545  O O   . LEU B 2 2   ? -35.667 26.949  14.294  1.00 53.26  ? 2   LEU B O   1 
ATOM   2546  C CB  . LEU B 2 2   ? -32.717 27.905  15.509  1.00 46.34  ? 2   LEU B CB  1 
ATOM   2547  C CG  . LEU B 2 2   ? -31.459 27.180  15.993  1.00 46.09  ? 2   LEU B CG  1 
ATOM   2548  C CD1 . LEU B 2 2   ? -30.924 27.836  17.258  1.00 31.68  ? 2   LEU B CD1 1 
ATOM   2549  C CD2 . LEU B 2 2   ? -31.725 25.697  16.216  1.00 40.64  ? 2   LEU B CD2 1 
ATOM   2550  N N   . PHE B 2 3   ? -35.092 29.059  13.819  1.00 58.22  ? 3   PHE B N   1 
ATOM   2551  C CA  . PHE B 2 3   ? -36.451 29.479  13.533  1.00 53.08  ? 3   PHE B CA  1 
ATOM   2552  C C   . PHE B 2 3   ? -36.706 29.318  12.036  1.00 60.30  ? 3   PHE B C   1 
ATOM   2553  O O   . PHE B 2 3   ? -35.786 29.120  11.238  1.00 75.96  ? 3   PHE B O   1 
ATOM   2554  C CB  . PHE B 2 3   ? -36.663 30.907  14.033  1.00 49.22  ? 3   PHE B CB  1 
ATOM   2555  C CG  . PHE B 2 3   ? -36.150 31.120  15.434  1.00 45.86  ? 3   PHE B CG  1 
ATOM   2556  C CD1 . PHE B 2 3   ? -34.798 31.357  15.667  1.00 43.99  ? 3   PHE B CD1 1 
ATOM   2557  C CD2 . PHE B 2 3   ? -37.005 31.045  16.521  1.00 45.15  ? 3   PHE B CD2 1 
ATOM   2558  C CE1 . PHE B 2 3   ? -34.314 31.525  16.956  1.00 46.63  ? 3   PHE B CE1 1 
ATOM   2559  C CE2 . PHE B 2 3   ? -36.529 31.219  17.815  1.00 37.70  ? 3   PHE B CE2 1 
ATOM   2560  C CZ  . PHE B 2 3   ? -35.184 31.460  18.031  1.00 48.86  ? 3   PHE B CZ  1 
ATOM   2561  N N   . GLY B 2 4   ? -37.968 29.362  11.651  1.00 47.13  ? 4   GLY B N   1 
ATOM   2562  C CA  . GLY B 2 4   ? -38.257 28.923  10.306  1.00 54.19  ? 4   GLY B CA  1 
ATOM   2563  C C   . GLY B 2 4   ? -38.137 29.939  9.195   1.00 62.81  ? 4   GLY B C   1 
ATOM   2564  O O   . GLY B 2 4   ? -38.389 29.583  8.038   1.00 53.09  ? 4   GLY B O   1 
ATOM   2565  N N   . ALA B 2 5   ? -37.738 31.180  9.487   1.00 57.34  ? 5   ALA B N   1 
ATOM   2566  C CA  . ALA B 2 5   ? -37.944 32.275  8.538   1.00 60.98  ? 5   ALA B CA  1 
ATOM   2567  C C   . ALA B 2 5   ? -36.822 32.404  7.506   1.00 55.45  ? 5   ALA B C   1 
ATOM   2568  O O   . ALA B 2 5   ? -37.051 32.217  6.307   1.00 53.67  ? 5   ALA B O   1 
ATOM   2569  C CB  . ALA B 2 5   ? -38.120 33.593  9.303   1.00 56.66  ? 5   ALA B CB  1 
ATOM   2570  N N   . ILE B 2 6   ? -35.602 32.704  7.952   1.00 55.90  ? 6   ILE B N   1 
ATOM   2571  C CA  . ILE B 2 6   ? -34.541 33.036  7.009   1.00 56.93  ? 6   ILE B CA  1 
ATOM   2572  C C   . ILE B 2 6   ? -34.074 31.774  6.298   1.00 59.69  ? 6   ILE B C   1 
ATOM   2573  O O   . ILE B 2 6   ? -33.716 30.775  6.938   1.00 56.42  ? 6   ILE B O   1 
ATOM   2574  C CB  . ILE B 2 6   ? -33.382 33.739  7.725   1.00 50.81  ? 6   ILE B CB  1 
ATOM   2575  C CG1 . ILE B 2 6   ? -33.883 35.036  8.362   1.00 51.41  ? 6   ILE B CG1 1 
ATOM   2576  C CG2 . ILE B 2 6   ? -32.255 34.009  6.744   1.00 40.33  ? 6   ILE B CG2 1 
ATOM   2577  C CD1 . ILE B 2 6   ? -32.810 36.065  8.591   1.00 38.41  ? 6   ILE B CD1 1 
ATOM   2578  N N   . ALA B 2 7   ? -34.081 31.819  4.963   1.00 57.91  ? 7   ALA B N   1 
ATOM   2579  C CA  . ALA B 2 7   ? -33.793 30.652  4.127   1.00 63.46  ? 7   ALA B CA  1 
ATOM   2580  C C   . ALA B 2 7   ? -34.704 29.488  4.493   1.00 64.56  ? 7   ALA B C   1 
ATOM   2581  O O   . ALA B 2 7   ? -34.333 28.319  4.365   1.00 69.01  ? 7   ALA B O   1 
ATOM   2582  C CB  . ALA B 2 7   ? -32.319 30.246  4.216   1.00 56.11  ? 7   ALA B CB  1 
ATOM   2583  N N   . GLY B 2 8   ? -35.900 29.817  4.977   1.00 63.85  ? 8   GLY B N   1 
ATOM   2584  C CA  . GLY B 2 8   ? -36.898 28.840  5.357   1.00 54.29  ? 8   GLY B CA  1 
ATOM   2585  C C   . GLY B 2 8   ? -38.174 29.045  4.573   1.00 55.02  ? 8   GLY B C   1 
ATOM   2586  O O   . GLY B 2 8   ? -38.174 28.911  3.346   1.00 56.60  ? 8   GLY B O   1 
ATOM   2587  N N   . PHE B 2 9   ? -39.273 29.377  5.255   1.00 48.45  ? 9   PHE B N   1 
ATOM   2588  C CA  . PHE B 2 9   ? -40.492 29.654  4.508   1.00 53.81  ? 9   PHE B CA  1 
ATOM   2589  C C   . PHE B 2 9   ? -40.411 30.981  3.763   1.00 55.77  ? 9   PHE B C   1 
ATOM   2590  O O   . PHE B 2 9   ? -41.191 31.198  2.833   1.00 63.79  ? 9   PHE B O   1 
ATOM   2591  C CB  . PHE B 2 9   ? -41.723 29.596  5.421   1.00 49.18  ? 9   PHE B CB  1 
ATOM   2592  C CG  . PHE B 2 9   ? -41.765 30.648  6.493   1.00 61.09  ? 9   PHE B CG  1 
ATOM   2593  C CD1 . PHE B 2 9   ? -42.347 31.882  6.254   1.00 58.90  ? 9   PHE B CD1 1 
ATOM   2594  C CD2 . PHE B 2 9   ? -41.271 30.383  7.760   1.00 61.45  ? 9   PHE B CD2 1 
ATOM   2595  C CE1 . PHE B 2 9   ? -42.404 32.844  7.246   1.00 55.67  ? 9   PHE B CE1 1 
ATOM   2596  C CE2 . PHE B 2 9   ? -41.327 31.339  8.756   1.00 54.62  ? 9   PHE B CE2 1 
ATOM   2597  C CZ  . PHE B 2 9   ? -41.894 32.571  8.498   1.00 57.13  ? 9   PHE B CZ  1 
ATOM   2598  N N   . ILE B 2 10  ? -39.476 31.855  4.126   1.00 54.47  ? 10  ILE B N   1 
ATOM   2599  C CA  . ILE B 2 10  ? -39.116 33.010  3.309   1.00 54.41  ? 10  ILE B CA  1 
ATOM   2600  C C   . ILE B 2 10  ? -37.822 32.645  2.588   1.00 55.12  ? 10  ILE B C   1 
ATOM   2601  O O   . ILE B 2 10  ? -36.735 32.687  3.170   1.00 65.46  ? 10  ILE B O   1 
ATOM   2602  C CB  . ILE B 2 10  ? -38.967 34.285  4.145   1.00 55.44  ? 10  ILE B CB  1 
ATOM   2603  C CG1 . ILE B 2 10  ? -40.196 34.492  5.032   1.00 49.99  ? 10  ILE B CG1 1 
ATOM   2604  C CG2 . ILE B 2 10  ? -38.762 35.485  3.241   1.00 44.38  ? 10  ILE B CG2 1 
ATOM   2605  C CD1 . ILE B 2 10  ? -39.935 35.332  6.259   1.00 53.95  ? 10  ILE B CD1 1 
ATOM   2606  N N   . GLU B 2 11  ? -37.937 32.285  1.311   1.00 60.35  ? 11  GLU B N   1 
ATOM   2607  C CA  . GLU B 2 11  ? -36.822 31.712  0.555   1.00 57.76  ? 11  GLU B CA  1 
ATOM   2608  C C   . GLU B 2 11  ? -35.972 32.822  -0.063  1.00 58.34  ? 11  GLU B C   1 
ATOM   2609  O O   . GLU B 2 11  ? -35.913 33.011  -1.279  1.00 76.24  ? 11  GLU B O   1 
ATOM   2610  C CB  . GLU B 2 11  ? -37.346 30.754  -0.507  1.00 65.22  ? 11  GLU B CB  1 
ATOM   2611  C CG  . GLU B 2 11  ? -38.307 29.696  0.026   1.00 87.65  ? 11  GLU B CG  1 
ATOM   2612  C CD  . GLU B 2 11  ? -39.730 29.881  -0.481  1.00 95.43  ? 11  GLU B CD  1 
ATOM   2613  O OE1 . GLU B 2 11  ? -40.663 29.333  0.148   1.00 91.84  ? 11  GLU B OE1 1 
ATOM   2614  O OE2 . GLU B 2 11  ? -39.915 30.571  -1.506  1.00 95.98  ? 11  GLU B OE2 1 
ATOM   2615  N N   . GLY B 2 12  ? -35.296 33.564  0.808   1.00 54.75  ? 12  GLY B N   1 
ATOM   2616  C CA  . GLY B 2 12  ? -34.348 34.558  0.342   1.00 55.03  ? 12  GLY B CA  1 
ATOM   2617  C C   . GLY B 2 12  ? -34.644 35.983  0.762   1.00 50.64  ? 12  GLY B C   1 
ATOM   2618  O O   . GLY B 2 12  ? -35.801 36.351  0.986   1.00 51.88  ? 12  GLY B O   1 
ATOM   2619  N N   . GLY B 2 13  ? -33.592 36.799  0.867   1.00 47.81  ? 13  GLY B N   1 
ATOM   2620  C CA  . GLY B 2 13  ? -33.749 38.195  1.209   1.00 41.87  ? 13  GLY B CA  1 
ATOM   2621  C C   . GLY B 2 13  ? -34.059 39.059  0.004   1.00 44.48  ? 13  GLY B C   1 
ATOM   2622  O O   . GLY B 2 13  ? -33.925 38.645  -1.147  1.00 49.18  ? 13  GLY B O   1 
ATOM   2623  N N   . TRP B 2 14  ? -34.484 40.288  0.292   1.00 49.82  ? 14  TRP B N   1 
ATOM   2624  C CA  . TRP B 2 14  ? -34.911 41.235  -0.731  1.00 45.46  ? 14  TRP B CA  1 
ATOM   2625  C C   . TRP B 2 14  ? -33.755 42.157  -1.107  1.00 42.68  ? 14  TRP B C   1 
ATOM   2626  O O   . TRP B 2 14  ? -33.309 42.967  -0.288  1.00 34.82  ? 14  TRP B O   1 
ATOM   2627  C CB  . TRP B 2 14  ? -36.093 42.066  -0.241  1.00 39.40  ? 14  TRP B CB  1 
ATOM   2628  C CG  . TRP B 2 14  ? -37.366 41.314  -0.112  1.00 36.94  ? 14  TRP B CG  1 
ATOM   2629  C CD1 . TRP B 2 14  ? -37.763 40.241  -0.856  1.00 37.06  ? 14  TRP B CD1 1 
ATOM   2630  C CD2 . TRP B 2 14  ? -38.428 41.580  0.815   1.00 35.90  ? 14  TRP B CD2 1 
ATOM   2631  N NE1 . TRP B 2 14  ? -39.009 39.818  -0.445  1.00 45.77  ? 14  TRP B NE1 1 
ATOM   2632  C CE2 . TRP B 2 14  ? -39.440 40.626  0.576   1.00 35.65  ? 14  TRP B CE2 1 
ATOM   2633  C CE3 . TRP B 2 14  ? -38.618 42.525  1.828   1.00 39.39  ? 14  TRP B CE3 1 
ATOM   2634  C CZ2 . TRP B 2 14  ? -40.625 40.592  1.310   1.00 32.08  ? 14  TRP B CZ2 1 
ATOM   2635  C CZ3 . TRP B 2 14  ? -39.798 42.494  2.553   1.00 50.50  ? 14  TRP B CZ3 1 
ATOM   2636  C CH2 . TRP B 2 14  ? -40.785 41.530  2.291   1.00 42.25  ? 14  TRP B CH2 1 
ATOM   2637  N N   . GLN B 2 15  ? -33.286 42.046  -2.348  1.00 47.27  ? 15  GLN B N   1 
ATOM   2638  C CA  . GLN B 2 15  ? -32.290 42.990  -2.835  1.00 52.54  ? 15  GLN B CA  1 
ATOM   2639  C C   . GLN B 2 15  ? -32.855 44.403  -2.918  1.00 64.14  ? 15  GLN B C   1 
ATOM   2640  O O   . GLN B 2 15  ? -32.107 45.376  -2.768  1.00 58.00  ? 15  GLN B O   1 
ATOM   2641  C CB  . GLN B 2 15  ? -31.770 42.539  -4.199  1.00 66.03  ? 15  GLN B CB  1 
ATOM   2642  C CG  . GLN B 2 15  ? -30.617 43.365  -4.727  1.00 75.30  ? 15  GLN B CG  1 
ATOM   2643  C CD  . GLN B 2 15  ? -29.272 42.820  -4.287  1.00 86.86  ? 15  GLN B CD  1 
ATOM   2644  O OE1 . GLN B 2 15  ? -29.152 41.647  -3.920  1.00 73.54  ? 15  GLN B OE1 1 
ATOM   2645  N NE2 . GLN B 2 15  ? -28.250 43.672  -4.320  1.00 67.33  ? 15  GLN B NE2 1 
ATOM   2646  N N   . GLY B 2 16  ? -34.168 44.532  -3.134  1.00 64.01  ? 16  GLY B N   1 
ATOM   2647  C CA  . GLY B 2 16  ? -34.819 45.823  -3.306  1.00 50.59  ? 16  GLY B CA  1 
ATOM   2648  C C   . GLY B 2 16  ? -35.077 46.600  -2.034  1.00 56.12  ? 16  GLY B C   1 
ATOM   2649  O O   . GLY B 2 16  ? -35.529 47.746  -2.104  1.00 58.48  ? 16  GLY B O   1 
ATOM   2650  N N   . MET B 2 17  ? -34.817 46.008  -0.874  1.00 50.30  ? 17  MET B N   1 
ATOM   2651  C CA  . MET B 2 17  ? -34.958 46.699  0.401   1.00 48.79  ? 17  MET B CA  1 
ATOM   2652  C C   . MET B 2 17  ? -33.591 47.234  0.806   1.00 65.20  ? 17  MET B C   1 
ATOM   2653  O O   . MET B 2 17  ? -32.773 46.509  1.377   1.00 66.98  ? 17  MET B O   1 
ATOM   2654  C CB  . MET B 2 17  ? -35.516 45.779  1.476   1.00 46.66  ? 17  MET B CB  1 
ATOM   2655  C CG  . MET B 2 17  ? -35.846 46.526  2.744   1.00 54.61  ? 17  MET B CG  1 
ATOM   2656  S SD  . MET B 2 17  ? -36.682 45.520  3.965   1.00 65.27  ? 17  MET B SD  1 
ATOM   2657  C CE  . MET B 2 17  ? -38.267 46.351  3.925   1.00 62.02  ? 17  MET B CE  1 
ATOM   2658  N N   . VAL B 2 18  ? -33.354 48.517  0.529   1.00 68.78  ? 18  VAL B N   1 
ATOM   2659  C CA  . VAL B 2 18  ? -32.062 49.124  0.823   1.00 55.51  ? 18  VAL B CA  1 
ATOM   2660  C C   . VAL B 2 18  ? -31.993 49.731  2.219   1.00 69.50  ? 18  VAL B C   1 
ATOM   2661  O O   . VAL B 2 18  ? -30.887 49.934  2.741   1.00 77.83  ? 18  VAL B O   1 
ATOM   2662  C CB  . VAL B 2 18  ? -31.727 50.193  -0.230  1.00 55.68  ? 18  VAL B CB  1 
ATOM   2663  C CG1 . VAL B 2 18  ? -31.585 49.547  -1.596  1.00 49.94  ? 18  VAL B CG1 1 
ATOM   2664  C CG2 . VAL B 2 18  ? -32.804 51.263  -0.253  1.00 54.15  ? 18  VAL B CG2 1 
ATOM   2665  N N   . ASP B 2 19  ? -33.132 50.031  2.835   1.00 57.23  ? 19  ASP B N   1 
ATOM   2666  C CA  . ASP B 2 19  ? -33.175 50.529  4.201   1.00 66.18  ? 19  ASP B CA  1 
ATOM   2667  C C   . ASP B 2 19  ? -33.662 49.425  5.130   1.00 68.20  ? 19  ASP B C   1 
ATOM   2668  O O   . ASP B 2 19  ? -34.575 48.670  4.784   1.00 83.49  ? 19  ASP B O   1 
ATOM   2669  C CB  . ASP B 2 19  ? -34.090 51.753  4.318   1.00 75.81  ? 19  ASP B CB  1 
ATOM   2670  C CG  . ASP B 2 19  ? -34.027 52.400  5.694   1.00 90.72  ? 19  ASP B CG  1 
ATOM   2671  O OD1 . ASP B 2 19  ? -33.160 53.274  5.911   1.00 89.73  ? 19  ASP B OD1 1 
ATOM   2672  O OD2 . ASP B 2 19  ? -34.845 52.032  6.562   1.00 96.81  ? 19  ASP B OD2 1 
ATOM   2673  N N   . GLY B 2 20  ? -33.034 49.320  6.297   1.00 54.79  ? 20  GLY B N   1 
ATOM   2674  C CA  . GLY B 2 20  ? -33.475 48.376  7.306   1.00 58.31  ? 20  GLY B CA  1 
ATOM   2675  C C   . GLY B 2 20  ? -33.034 46.943  7.083   1.00 49.40  ? 20  GLY B C   1 
ATOM   2676  O O   . GLY B 2 20  ? -32.790 46.517  5.949   1.00 42.58  ? 20  GLY B O   1 
ATOM   2677  N N   . TRP B 2 21  ? -32.924 46.188  8.177   1.00 43.22  ? 21  TRP B N   1 
ATOM   2678  C CA  . TRP B 2 21  ? -32.568 44.777  8.079   1.00 48.59  ? 21  TRP B CA  1 
ATOM   2679  C C   . TRP B 2 21  ? -33.794 43.920  7.802   1.00 53.85  ? 21  TRP B C   1 
ATOM   2680  O O   . TRP B 2 21  ? -33.721 42.945  7.042   1.00 42.04  ? 21  TRP B O   1 
ATOM   2681  C CB  . TRP B 2 21  ? -31.877 44.324  9.366   1.00 36.64  ? 21  TRP B CB  1 
ATOM   2682  C CG  . TRP B 2 21  ? -30.384 44.478  9.345   1.00 55.32  ? 21  TRP B CG  1 
ATOM   2683  C CD1 . TRP B 2 21  ? -29.606 44.791  8.268   1.00 57.31  ? 21  TRP B CD1 1 
ATOM   2684  C CD2 . TRP B 2 21  ? -29.488 44.322  10.454  1.00 45.94  ? 21  TRP B CD2 1 
ATOM   2685  N NE1 . TRP B 2 21  ? -28.283 44.836  8.637   1.00 61.60  ? 21  TRP B NE1 1 
ATOM   2686  C CE2 . TRP B 2 21  ? -28.184 44.552  9.974   1.00 48.47  ? 21  TRP B CE2 1 
ATOM   2687  C CE3 . TRP B 2 21  ? -29.663 44.006  11.804  1.00 44.60  ? 21  TRP B CE3 1 
ATOM   2688  C CZ2 . TRP B 2 21  ? -27.060 44.475  10.795  1.00 49.08  ? 21  TRP B CZ2 1 
ATOM   2689  C CZ3 . TRP B 2 21  ? -28.544 43.934  12.622  1.00 49.03  ? 21  TRP B CZ3 1 
ATOM   2690  C CH2 . TRP B 2 21  ? -27.262 44.165  12.113  1.00 42.95  ? 21  TRP B CH2 1 
ATOM   2691  N N   . TYR B 2 22  ? -34.923 44.273  8.413   1.00 41.70  ? 22  TYR B N   1 
ATOM   2692  C CA  . TYR B 2 22  ? -36.181 43.570  8.248   1.00 41.00  ? 22  TYR B CA  1 
ATOM   2693  C C   . TYR B 2 22  ? -37.279 44.571  7.933   1.00 44.40  ? 22  TYR B C   1 
ATOM   2694  O O   . TYR B 2 22  ? -37.239 45.723  8.374   1.00 50.13  ? 22  TYR B O   1 
ATOM   2695  C CB  . TYR B 2 22  ? -36.561 42.779  9.508   1.00 41.75  ? 22  TYR B CB  1 
ATOM   2696  C CG  . TYR B 2 22  ? -35.391 42.346  10.361  1.00 35.44  ? 22  TYR B CG  1 
ATOM   2697  C CD1 . TYR B 2 22  ? -34.495 41.389  9.906   1.00 39.22  ? 22  TYR B CD1 1 
ATOM   2698  C CD2 . TYR B 2 22  ? -35.196 42.876  11.630  1.00 43.10  ? 22  TYR B CD2 1 
ATOM   2699  C CE1 . TYR B 2 22  ? -33.427 40.976  10.690  1.00 36.03  ? 22  TYR B CE1 1 
ATOM   2700  C CE2 . TYR B 2 22  ? -34.129 42.469  12.422  1.00 39.06  ? 22  TYR B CE2 1 
ATOM   2701  C CZ  . TYR B 2 22  ? -33.250 41.518  11.945  1.00 34.15  ? 22  TYR B CZ  1 
ATOM   2702  O OH  . TYR B 2 22  ? -32.187 41.111  12.718  1.00 44.13  ? 22  TYR B OH  1 
ATOM   2703  N N   . GLY B 2 23  ? -38.271 44.118  7.185   1.00 45.16  ? 23  GLY B N   1 
ATOM   2704  C CA  . GLY B 2 23  ? -39.392 44.976  6.880   1.00 46.32  ? 23  GLY B CA  1 
ATOM   2705  C C   . GLY B 2 23  ? -40.404 44.271  6.014   1.00 45.72  ? 23  GLY B C   1 
ATOM   2706  O O   . GLY B 2 23  ? -40.428 43.041  5.926   1.00 48.51  ? 23  GLY B O   1 
ATOM   2707  N N   . TYR B 2 24  ? -41.236 45.074  5.366   1.00 48.76  ? 24  TYR B N   1 
ATOM   2708  C CA  . TYR B 2 24  ? -42.413 44.584  4.677   1.00 44.67  ? 24  TYR B CA  1 
ATOM   2709  C C   . TYR B 2 24  ? -42.367 44.938  3.199   1.00 44.96  ? 24  TYR B C   1 
ATOM   2710  O O   . TYR B 2 24  ? -41.700 45.894  2.788   1.00 47.39  ? 24  TYR B O   1 
ATOM   2711  C CB  . TYR B 2 24  ? -43.694 45.157  5.294   1.00 42.35  ? 24  TYR B CB  1 
ATOM   2712  C CG  . TYR B 2 24  ? -43.689 45.233  6.806   1.00 47.90  ? 24  TYR B CG  1 
ATOM   2713  C CD1 . TYR B 2 24  ? -43.122 46.316  7.466   1.00 43.08  ? 24  TYR B CD1 1 
ATOM   2714  C CD2 . TYR B 2 24  ? -44.270 44.229  7.574   1.00 48.19  ? 24  TYR B CD2 1 
ATOM   2715  C CE1 . TYR B 2 24  ? -43.123 46.394  8.846   1.00 54.05  ? 24  TYR B CE1 1 
ATOM   2716  C CE2 . TYR B 2 24  ? -44.276 44.299  8.955   1.00 54.01  ? 24  TYR B CE2 1 
ATOM   2717  C CZ  . TYR B 2 24  ? -43.700 45.385  9.586   1.00 55.35  ? 24  TYR B CZ  1 
ATOM   2718  O OH  . TYR B 2 24  ? -43.697 45.467  10.960  1.00 58.87  ? 24  TYR B OH  1 
ATOM   2719  N N   . HIS B 2 25  ? -43.073 44.140  2.405   1.00 45.90  ? 25  HIS B N   1 
ATOM   2720  C CA  . HIS B 2 25  ? -43.359 44.456  1.014   1.00 47.47  ? 25  HIS B CA  1 
ATOM   2721  C C   . HIS B 2 25  ? -44.858 44.330  0.804   1.00 49.68  ? 25  HIS B C   1 
ATOM   2722  O O   . HIS B 2 25  ? -45.455 43.315  1.176   1.00 51.71  ? 25  HIS B O   1 
ATOM   2723  C CB  . HIS B 2 25  ? -42.611 43.532  0.049   1.00 39.39  ? 25  HIS B CB  1 
ATOM   2724  C CG  . HIS B 2 25  ? -42.824 43.879  -1.390  1.00 50.82  ? 25  HIS B CG  1 
ATOM   2725  N ND1 . HIS B 2 25  ? -41.971 44.703  -2.093  1.00 59.18  ? 25  HIS B ND1 1 
ATOM   2726  C CD2 . HIS B 2 25  ? -43.805 43.529  -2.254  1.00 49.86  ? 25  HIS B CD2 1 
ATOM   2727  C CE1 . HIS B 2 25  ? -42.411 44.837  -3.330  1.00 59.52  ? 25  HIS B CE1 1 
ATOM   2728  N NE2 . HIS B 2 25  ? -43.523 44.134  -3.454  1.00 55.88  ? 25  HIS B NE2 1 
ATOM   2729  N N   . HIS B 2 26  ? -45.462 45.352  0.212   1.00 48.92  ? 26  HIS B N   1 
ATOM   2730  C CA  . HIS B 2 26  ? -46.900 45.383  0.011   1.00 45.42  ? 26  HIS B CA  1 
ATOM   2731  C C   . HIS B 2 26  ? -47.212 45.454  -1.475  1.00 41.78  ? 26  HIS B C   1 
ATOM   2732  O O   . HIS B 2 26  ? -46.423 45.966  -2.271  1.00 49.63  ? 26  HIS B O   1 
ATOM   2733  C CB  . HIS B 2 26  ? -47.550 46.569  0.741   1.00 50.29  ? 26  HIS B CB  1 
ATOM   2734  C CG  . HIS B 2 26  ? -47.413 47.872  0.015   1.00 57.05  ? 26  HIS B CG  1 
ATOM   2735  N ND1 . HIS B 2 26  ? -46.405 48.771  0.288   1.00 54.57  ? 26  HIS B ND1 1 
ATOM   2736  C CD2 . HIS B 2 26  ? -48.153 48.426  -0.975  1.00 59.46  ? 26  HIS B CD2 1 
ATOM   2737  C CE1 . HIS B 2 26  ? -46.529 49.822  -0.504  1.00 59.03  ? 26  HIS B CE1 1 
ATOM   2738  N NE2 . HIS B 2 26  ? -47.581 49.637  -1.280  1.00 70.83  ? 26  HIS B NE2 1 
ATOM   2739  N N   . SER B 2 27  ? -48.369 44.919  -1.838  1.00 45.25  ? 27  SER B N   1 
ATOM   2740  C CA  . SER B 2 27  ? -48.877 45.008  -3.197  1.00 43.55  ? 27  SER B CA  1 
ATOM   2741  C C   . SER B 2 27  ? -50.382 45.186  -3.105  1.00 44.87  ? 27  SER B C   1 
ATOM   2742  O O   . SER B 2 27  ? -51.062 44.368  -2.481  1.00 51.52  ? 27  SER B O   1 
ATOM   2743  C CB  . SER B 2 27  ? -48.520 43.759  -4.006  1.00 43.93  ? 27  SER B CB  1 
ATOM   2744  O OG  . SER B 2 27  ? -48.367 44.064  -5.378  1.00 54.22  ? 27  SER B OG  1 
ATOM   2745  N N   . ASN B 2 28  ? -50.895 46.260  -3.696  1.00 51.14  ? 28  ASN B N   1 
ATOM   2746  C CA  . ASN B 2 28  ? -52.332 46.492  -3.736  1.00 56.06  ? 28  ASN B CA  1 
ATOM   2747  C C   . ASN B 2 28  ? -52.667 47.215  -5.036  1.00 50.00  ? 28  ASN B C   1 
ATOM   2748  O O   . ASN B 2 28  ? -51.842 47.297  -5.950  1.00 55.29  ? 28  ASN B O   1 
ATOM   2749  C CB  . ASN B 2 28  ? -52.799 47.256  -2.488  1.00 52.33  ? 28  ASN B CB  1 
ATOM   2750  C CG  . ASN B 2 28  ? -52.119 48.602  -2.326  1.00 48.48  ? 28  ASN B CG  1 
ATOM   2751  O OD1 . ASN B 2 28  ? -51.593 49.174  -3.281  1.00 48.82  ? 28  ASN B OD1 1 
ATOM   2752  N ND2 . ASN B 2 28  ? -52.126 49.116  -1.102  1.00 46.55  ? 28  ASN B ND2 1 
ATOM   2753  N N   . GLU B 2 29  ? -53.894 47.738  -5.116  1.00 50.95  ? 29  GLU B N   1 
ATOM   2754  C CA  . GLU B 2 29  ? -54.329 48.444  -6.317  1.00 59.85  ? 29  GLU B CA  1 
ATOM   2755  C C   . GLU B 2 29  ? -53.530 49.724  -6.534  1.00 55.43  ? 29  GLU B C   1 
ATOM   2756  O O   . GLU B 2 29  ? -53.210 50.075  -7.677  1.00 53.25  ? 29  GLU B O   1 
ATOM   2757  C CB  . GLU B 2 29  ? -55.824 48.752  -6.227  1.00 66.37  ? 29  GLU B CB  1 
ATOM   2758  C CG  . GLU B 2 29  ? -56.707 47.733  -6.928  1.00 82.07  ? 29  GLU B CG  1 
ATOM   2759  C CD  . GLU B 2 29  ? -58.170 48.134  -6.936  1.00 92.70  ? 29  GLU B CD  1 
ATOM   2760  O OE1 . GLU B 2 29  ? -58.808 48.086  -5.861  1.00 91.88  ? 29  GLU B OE1 1 
ATOM   2761  O OE2 . GLU B 2 29  ? -58.680 48.499  -8.017  1.00 88.06  ? 29  GLU B OE2 1 
ATOM   2762  N N   . GLN B 2 30  ? -53.207 50.439  -5.452  1.00 48.62  ? 30  GLN B N   1 
ATOM   2763  C CA  . GLN B 2 30  ? -52.433 51.673  -5.574  1.00 56.12  ? 30  GLN B CA  1 
ATOM   2764  C C   . GLN B 2 30  ? -51.040 51.414  -6.138  1.00 57.80  ? 30  GLN B C   1 
ATOM   2765  O O   . GLN B 2 30  ? -50.562 52.168  -6.993  1.00 58.85  ? 30  GLN B O   1 
ATOM   2766  C CB  . GLN B 2 30  ? -52.337 52.368  -4.215  1.00 63.87  ? 30  GLN B CB  1 
ATOM   2767  C CG  . GLN B 2 30  ? -53.650 52.441  -3.446  1.00 72.97  ? 30  GLN B CG  1 
ATOM   2768  C CD  . GLN B 2 30  ? -53.751 53.699  -2.602  1.00 71.94  ? 30  GLN B CD  1 
ATOM   2769  O OE1 . GLN B 2 30  ? -54.085 53.644  -1.417  1.00 64.87  ? 30  GLN B OE1 1 
ATOM   2770  N NE2 . GLN B 2 30  ? -53.462 54.842  -3.211  1.00 75.17  ? 30  GLN B NE2 1 
ATOM   2771  N N   . GLY B 2 31  ? -50.372 50.360  -5.677  1.00 51.84  ? 31  GLY B N   1 
ATOM   2772  C CA  . GLY B 2 31  ? -49.034 50.065  -6.162  1.00 57.74  ? 31  GLY B CA  1 
ATOM   2773  C C   . GLY B 2 31  ? -48.327 49.078  -5.250  1.00 49.20  ? 31  GLY B C   1 
ATOM   2774  O O   . GLY B 2 31  ? -48.965 48.287  -4.558  1.00 53.14  ? 31  GLY B O   1 
ATOM   2775  N N   . SER B 2 32  ? -46.994 49.140  -5.269  1.00 44.73  ? 32  SER B N   1 
ATOM   2776  C CA  . SER B 2 32  ? -46.176 48.236  -4.470  1.00 49.55  ? 32  SER B CA  1 
ATOM   2777  C C   . SER B 2 32  ? -44.909 48.946  -4.016  1.00 58.11  ? 32  SER B C   1 
ATOM   2778  O O   . SER B 2 32  ? -44.510 49.968  -4.580  1.00 55.12  ? 32  SER B O   1 
ATOM   2779  C CB  . SER B 2 32  ? -45.827 46.962  -5.249  1.00 51.21  ? 32  SER B CB  1 
ATOM   2780  O OG  . SER B 2 32  ? -45.212 47.270  -6.488  1.00 46.18  ? 32  SER B OG  1 
ATOM   2781  N N   . GLY B 2 33  ? -44.278 48.390  -2.987  1.00 60.91  ? 33  GLY B N   1 
ATOM   2782  C CA  . GLY B 2 33  ? -43.045 48.959  -2.479  1.00 53.70  ? 33  GLY B CA  1 
ATOM   2783  C C   . GLY B 2 33  ? -42.595 48.274  -1.207  1.00 57.14  ? 33  GLY B C   1 
ATOM   2784  O O   . GLY B 2 33  ? -43.299 47.441  -0.630  1.00 52.81  ? 33  GLY B O   1 
ATOM   2785  N N   . TYR B 2 34  ? -41.391 48.652  -0.774  1.00 50.85  ? 34  TYR B N   1 
ATOM   2786  C CA  . TYR B 2 34  ? -40.776 48.146  0.444   1.00 45.07  ? 34  TYR B CA  1 
ATOM   2787  C C   . TYR B 2 34  ? -40.845 49.196  1.548   1.00 40.58  ? 34  TYR B C   1 
ATOM   2788  O O   . TYR B 2 34  ? -40.896 50.399  1.285   1.00 62.13  ? 34  TYR B O   1 
ATOM   2789  C CB  . TYR B 2 34  ? -39.313 47.752  0.207   1.00 47.84  ? 34  TYR B CB  1 
ATOM   2790  C CG  . TYR B 2 34  ? -39.094 46.752  -0.910  1.00 47.59  ? 34  TYR B CG  1 
ATOM   2791  C CD1 . TYR B 2 34  ? -38.987 47.170  -2.231  1.00 43.70  ? 34  TYR B CD1 1 
ATOM   2792  C CD2 . TYR B 2 34  ? -38.981 45.391  -0.643  1.00 43.81  ? 34  TYR B CD2 1 
ATOM   2793  C CE1 . TYR B 2 34  ? -38.785 46.267  -3.256  1.00 38.50  ? 34  TYR B CE1 1 
ATOM   2794  C CE2 . TYR B 2 34  ? -38.779 44.476  -1.665  1.00 46.43  ? 34  TYR B CE2 1 
ATOM   2795  C CZ  . TYR B 2 34  ? -38.681 44.923  -2.970  1.00 56.18  ? 34  TYR B CZ  1 
ATOM   2796  O OH  . TYR B 2 34  ? -38.476 44.032  -3.998  1.00 66.17  ? 34  TYR B OH  1 
ATOM   2797  N N   . ALA B 2 35  ? -40.851 48.725  2.792   1.00 41.68  ? 35  ALA B N   1 
ATOM   2798  C CA  . ALA B 2 35  ? -40.874 49.610  3.952   1.00 44.28  ? 35  ALA B CA  1 
ATOM   2799  C C   . ALA B 2 35  ? -40.249 48.874  5.125   1.00 53.09  ? 35  ALA B C   1 
ATOM   2800  O O   . ALA B 2 35  ? -40.733 47.808  5.516   1.00 56.63  ? 35  ALA B O   1 
ATOM   2801  C CB  . ALA B 2 35  ? -42.298 50.054  4.289   1.00 44.52  ? 35  ALA B CB  1 
ATOM   2802  N N   . ALA B 2 36  ? -39.187 49.438  5.684   1.00 48.89  ? 36  ALA B N   1 
ATOM   2803  C CA  . ALA B 2 36  ? -38.454 48.765  6.741   1.00 50.97  ? 36  ALA B CA  1 
ATOM   2804  C C   . ALA B 2 36  ? -39.102 49.010  8.096   1.00 60.23  ? 36  ALA B C   1 
ATOM   2805  O O   . ALA B 2 36  ? -39.705 50.059  8.342   1.00 66.81  ? 36  ALA B O   1 
ATOM   2806  C CB  . ALA B 2 36  ? -37.002 49.235  6.768   1.00 53.59  ? 36  ALA B CB  1 
ATOM   2807  N N   . ASP B 2 37  ? -38.981 48.019  8.976   1.00 59.58  ? 37  ASP B N   1 
ATOM   2808  C CA  . ASP B 2 37  ? -39.411 48.153  10.365  1.00 58.01  ? 37  ASP B CA  1 
ATOM   2809  C C   . ASP B 2 37  ? -38.227 48.691  11.155  1.00 54.66  ? 37  ASP B C   1 
ATOM   2810  O O   . ASP B 2 37  ? -37.265 47.968  11.427  1.00 56.32  ? 37  ASP B O   1 
ATOM   2811  C CB  . ASP B 2 37  ? -39.904 46.819  10.914  1.00 43.75  ? 37  ASP B CB  1 
ATOM   2812  C CG  . ASP B 2 37  ? -40.580 46.964  12.257  1.00 63.58  ? 37  ASP B CG  1 
ATOM   2813  O OD1 . ASP B 2 37  ? -41.803 47.231  12.284  1.00 69.04  ? 37  ASP B OD1 1 
ATOM   2814  O OD2 . ASP B 2 37  ? -39.885 46.813  13.285  1.00 59.49  ? 37  ASP B OD2 1 
ATOM   2815  N N   . ARG B 2 38  ? -38.290 49.976  11.515  1.00 58.06  ? 38  ARG B N   1 
ATOM   2816  C CA  . ARG B 2 38  ? -37.131 50.622  12.124  1.00 56.24  ? 38  ARG B CA  1 
ATOM   2817  C C   . ARG B 2 38  ? -36.844 50.070  13.515  1.00 49.55  ? 38  ARG B C   1 
ATOM   2818  O O   . ARG B 2 38  ? -35.679 49.919  13.896  1.00 53.49  ? 38  ARG B O   1 
ATOM   2819  C CB  . ARG B 2 38  ? -37.329 52.138  12.174  1.00 60.21  ? 38  ARG B CB  1 
ATOM   2820  C CG  . ARG B 2 38  ? -37.460 52.816  10.810  1.00 55.84  ? 38  ARG B CG  1 
ATOM   2821  C CD  . ARG B 2 38  ? -36.193 52.674  9.962   1.00 80.64  ? 38  ARG B CD  1 
ATOM   2822  N NE  . ARG B 2 38  ? -34.994 52.492  10.773  1.00 91.80  ? 38  ARG B NE  1 
ATOM   2823  C CZ  . ARG B 2 38  ? -33.925 51.805  10.393  1.00 83.39  ? 38  ARG B CZ  1 
ATOM   2824  N NH1 . ARG B 2 38  ? -33.854 51.239  9.198   1.00 79.88  ? 38  ARG B NH1 1 
ATOM   2825  N NH2 . ARG B 2 38  ? -32.903 51.678  11.235  1.00 79.35  ? 38  ARG B NH2 1 
ATOM   2826  N N   . GLU B 2 39  ? -37.886 49.770  14.287  1.00 56.94  ? 39  GLU B N   1 
ATOM   2827  C CA  . GLU B 2 39  ? -37.678 49.313  15.658  1.00 61.64  ? 39  GLU B CA  1 
ATOM   2828  C C   . GLU B 2 39  ? -36.961 47.969  15.691  1.00 55.76  ? 39  GLU B C   1 
ATOM   2829  O O   . GLU B 2 39  ? -35.995 47.786  16.443  1.00 55.94  ? 39  GLU B O   1 
ATOM   2830  C CB  . GLU B 2 39  ? -39.016 49.233  16.392  1.00 68.28  ? 39  GLU B CB  1 
ATOM   2831  C CG  . GLU B 2 39  ? -39.217 50.339  17.413  1.00 86.25  ? 39  GLU B CG  1 
ATOM   2832  C CD  . GLU B 2 39  ? -38.373 50.138  18.657  1.00 105.66 ? 39  GLU B CD  1 
ATOM   2833  O OE1 . GLU B 2 39  ? -37.194 50.557  18.656  1.00 98.03  ? 39  GLU B OE1 1 
ATOM   2834  O OE2 . GLU B 2 39  ? -38.891 49.559  19.636  1.00 100.86 ? 39  GLU B OE2 1 
ATOM   2835  N N   . SER B 2 40  ? -37.417 47.013  14.876  1.00 54.71  ? 40  SER B N   1 
ATOM   2836  C CA  . SER B 2 40  ? -36.767 45.707  14.832  1.00 50.36  ? 40  SER B CA  1 
ATOM   2837  C C   . SER B 2 40  ? -35.344 45.822  14.308  1.00 47.67  ? 40  SER B C   1 
ATOM   2838  O O   . SER B 2 40  ? -34.433 45.156  14.811  1.00 45.96  ? 40  SER B O   1 
ATOM   2839  C CB  . SER B 2 40  ? -37.573 44.742  13.966  1.00 44.89  ? 40  SER B CB  1 
ATOM   2840  O OG  . SER B 2 40  ? -38.963 44.931  14.166  1.00 79.89  ? 40  SER B OG  1 
ATOM   2841  N N   . THR B 2 41  ? -35.135 46.654  13.286  1.00 48.27  ? 41  THR B N   1 
ATOM   2842  C CA  . THR B 2 41  ? -33.793 46.843  12.752  1.00 44.13  ? 41  THR B CA  1 
ATOM   2843  C C   . THR B 2 41  ? -32.872 47.458  13.797  1.00 53.36  ? 41  THR B C   1 
ATOM   2844  O O   . THR B 2 41  ? -31.779 46.940  14.058  1.00 47.81  ? 41  THR B O   1 
ATOM   2845  C CB  . THR B 2 41  ? -33.848 47.714  11.501  1.00 42.25  ? 41  THR B CB  1 
ATOM   2846  O OG1 . THR B 2 41  ? -34.588 47.035  10.480  1.00 46.56  ? 41  THR B OG1 1 
ATOM   2847  C CG2 . THR B 2 41  ? -32.446 48.000  10.996  1.00 42.11  ? 41  THR B CG2 1 
ATOM   2848  N N   . GLN B 2 42  ? -33.313 48.549  14.431  1.00 45.27  ? 42  GLN B N   1 
ATOM   2849  C CA  . GLN B 2 42  ? -32.465 49.239  15.398  1.00 50.28  ? 42  GLN B CA  1 
ATOM   2850  C C   . GLN B 2 42  ? -32.137 48.344  16.584  1.00 54.15  ? 42  GLN B C   1 
ATOM   2851  O O   . GLN B 2 42  ? -30.997 48.333  17.065  1.00 52.58  ? 42  GLN B O   1 
ATOM   2852  C CB  . GLN B 2 42  ? -33.141 50.526  15.869  1.00 52.25  ? 42  GLN B CB  1 
ATOM   2853  C CG  . GLN B 2 42  ? -32.188 51.514  16.538  1.00 52.66  ? 42  GLN B CG  1 
ATOM   2854  C CD  . GLN B 2 42  ? -30.977 51.828  15.681  1.00 55.53  ? 42  GLN B CD  1 
ATOM   2855  O OE1 . GLN B 2 42  ? -29.847 51.492  16.036  1.00 64.22  ? 42  GLN B OE1 1 
ATOM   2856  N NE2 . GLN B 2 42  ? -31.209 52.468  14.539  1.00 58.98  ? 42  GLN B NE2 1 
ATOM   2857  N N   . LYS B 2 43  ? -33.123 47.587  17.069  1.00 46.74  ? 43  LYS B N   1 
ATOM   2858  C CA  . LYS B 2 43  ? -32.861 46.642  18.149  1.00 48.29  ? 43  LYS B CA  1 
ATOM   2859  C C   . LYS B 2 43  ? -31.831 45.607  17.721  1.00 50.23  ? 43  LYS B C   1 
ATOM   2860  O O   . LYS B 2 43  ? -30.925 45.263  18.490  1.00 49.07  ? 43  LYS B O   1 
ATOM   2861  C CB  . LYS B 2 43  ? -34.161 45.961  18.579  1.00 48.92  ? 43  LYS B CB  1 
ATOM   2862  C CG  . LYS B 2 43  ? -34.219 45.592  20.057  1.00 66.13  ? 43  LYS B CG  1 
ATOM   2863  C CD  . LYS B 2 43  ? -34.795 44.199  20.260  1.00 76.21  ? 43  LYS B CD  1 
ATOM   2864  C CE  . LYS B 2 43  ? -33.881 43.137  19.664  1.00 70.64  ? 43  LYS B CE  1 
ATOM   2865  N NZ  . LYS B 2 43  ? -34.158 41.786  20.213  1.00 67.26  ? 43  LYS B NZ  1 
ATOM   2866  N N   . ALA B 2 44  ? -31.950 45.103  16.493  1.00 42.76  ? 44  ALA B N   1 
ATOM   2867  C CA  . ALA B 2 44  ? -30.991 44.119  16.010  1.00 50.57  ? 44  ALA B CA  1 
ATOM   2868  C C   . ALA B 2 44  ? -29.610 44.738  15.823  1.00 44.43  ? 44  ALA B C   1 
ATOM   2869  O O   . ALA B 2 44  ? -28.595 44.094  16.112  1.00 49.33  ? 44  ALA B O   1 
ATOM   2870  C CB  . ALA B 2 44  ? -31.495 43.491  14.712  1.00 39.30  ? 44  ALA B CB  1 
ATOM   2871  N N   . ILE B 2 45  ? -29.547 45.982  15.340  1.00 43.03  ? 45  ILE B N   1 
ATOM   2872  C CA  . ILE B 2 45  ? -28.260 46.664  15.213  1.00 48.21  ? 45  ILE B CA  1 
ATOM   2873  C C   . ILE B 2 45  ? -27.614 46.845  16.581  1.00 47.49  ? 45  ILE B C   1 
ATOM   2874  O O   . ILE B 2 45  ? -26.415 46.595  16.757  1.00 46.27  ? 45  ILE B O   1 
ATOM   2875  C CB  . ILE B 2 45  ? -28.434 48.010  14.483  1.00 53.39  ? 45  ILE B CB  1 
ATOM   2876  C CG1 . ILE B 2 45  ? -28.935 47.782  13.054  1.00 49.02  ? 45  ILE B CG1 1 
ATOM   2877  C CG2 . ILE B 2 45  ? -27.131 48.805  14.494  1.00 36.86  ? 45  ILE B CG2 1 
ATOM   2878  C CD1 . ILE B 2 45  ? -28.991 49.038  12.207  1.00 42.17  ? 45  ILE B CD1 1 
ATOM   2879  N N   . ASP B 2 46  ? -28.397 47.273  17.572  1.00 39.32  ? 46  ASP B N   1 
ATOM   2880  C CA  . ASP B 2 46  ? -27.847 47.469  18.909  1.00 41.80  ? 46  ASP B CA  1 
ATOM   2881  C C   . ASP B 2 46  ? -27.375 46.149  19.508  1.00 50.29  ? 46  ASP B C   1 
ATOM   2882  O O   . ASP B 2 46  ? -26.324 46.094  20.161  1.00 46.98  ? 46  ASP B O   1 
ATOM   2883  C CB  . ASP B 2 46  ? -28.885 48.140  19.810  1.00 43.65  ? 46  ASP B CB  1 
ATOM   2884  C CG  . ASP B 2 46  ? -29.225 49.559  19.356  1.00 67.49  ? 46  ASP B CG  1 
ATOM   2885  O OD1 . ASP B 2 46  ? -28.412 50.171  18.628  1.00 62.37  ? 46  ASP B OD1 1 
ATOM   2886  O OD2 . ASP B 2 46  ? -30.311 50.062  19.723  1.00 64.92  ? 46  ASP B OD2 1 
ATOM   2887  N N   . GLY B 2 47  ? -28.136 45.072  19.296  1.00 46.41  ? 47  GLY B N   1 
ATOM   2888  C CA  . GLY B 2 47  ? -27.732 43.785  19.836  1.00 42.01  ? 47  GLY B CA  1 
ATOM   2889  C C   . GLY B 2 47  ? -26.435 43.287  19.230  1.00 48.04  ? 47  GLY B C   1 
ATOM   2890  O O   . GLY B 2 47  ? -25.520 42.870  19.945  1.00 39.15  ? 47  GLY B O   1 
ATOM   2891  N N   . VAL B 2 48  ? -26.327 43.353  17.903  1.00 39.69  ? 48  VAL B N   1 
ATOM   2892  C CA  . VAL B 2 48  ? -25.133 42.851  17.233  1.00 47.02  ? 48  VAL B CA  1 
ATOM   2893  C C   . VAL B 2 48  ? -23.924 43.711  17.578  1.00 45.79  ? 48  VAL B C   1 
ATOM   2894  O O   . VAL B 2 48  ? -22.814 43.199  17.774  1.00 41.43  ? 48  VAL B O   1 
ATOM   2895  C CB  . VAL B 2 48  ? -25.378 42.773  15.717  1.00 46.89  ? 48  VAL B CB  1 
ATOM   2896  C CG1 . VAL B 2 48  ? -24.098 42.431  14.984  1.00 48.67  ? 48  VAL B CG1 1 
ATOM   2897  C CG2 . VAL B 2 48  ? -26.451 41.737  15.423  1.00 38.68  ? 48  VAL B CG2 1 
ATOM   2898  N N   . THR B 2 49  ? -24.118 45.026  17.667  1.00 46.11  ? 49  THR B N   1 
ATOM   2899  C CA  . THR B 2 49  ? -23.021 45.910  18.040  1.00 41.87  ? 49  THR B CA  1 
ATOM   2900  C C   . THR B 2 49  ? -22.540 45.621  19.455  1.00 40.53  ? 49  THR B C   1 
ATOM   2901  O O   . THR B 2 49  ? -21.332 45.606  19.719  1.00 49.73  ? 49  THR B O   1 
ATOM   2902  C CB  . THR B 2 49  ? -23.462 47.364  17.906  1.00 47.20  ? 49  THR B CB  1 
ATOM   2903  O OG1 . THR B 2 49  ? -23.842 47.611  16.549  1.00 49.67  ? 49  THR B OG1 1 
ATOM   2904  C CG2 . THR B 2 49  ? -22.330 48.312  18.300  1.00 35.21  ? 49  THR B CG2 1 
ATOM   2905  N N   . ASN B 2 50  ? -23.472 45.388  20.379  1.00 36.47  ? 50  ASN B N   1 
ATOM   2906  C CA  . ASN B 2 50  ? -23.075 45.063  21.741  1.00 36.48  ? 50  ASN B CA  1 
ATOM   2907  C C   . ASN B 2 50  ? -22.296 43.756  21.794  1.00 43.02  ? 50  ASN B C   1 
ATOM   2908  O O   . ASN B 2 50  ? -21.368 43.618  22.599  1.00 49.22  ? 50  ASN B O   1 
ATOM   2909  C CB  . ASN B 2 50  ? -24.307 44.996  22.640  1.00 42.85  ? 50  ASN B CB  1 
ATOM   2910  C CG  . ASN B 2 50  ? -23.992 45.338  24.080  1.00 65.73  ? 50  ASN B CG  1 
ATOM   2911  O OD1 . ASN B 2 50  ? -23.909 46.512  24.448  1.00 73.18  ? 50  ASN B OD1 1 
ATOM   2912  N ND2 . ASN B 2 50  ? -23.805 44.310  24.905  1.00 61.33  ? 50  ASN B ND2 1 
ATOM   2913  N N   . LYS B 2 51  ? -22.645 42.796  20.935  1.00 40.65  ? 51  LYS B N   1 
ATOM   2914  C CA  . LYS B 2 51  ? -21.929 41.526  20.909  1.00 46.33  ? 51  LYS B CA  1 
ATOM   2915  C C   . LYS B 2 51  ? -20.480 41.716  20.478  1.00 44.54  ? 51  LYS B C   1 
ATOM   2916  O O   . LYS B 2 51  ? -19.559 41.206  21.125  1.00 47.13  ? 51  LYS B O   1 
ATOM   2917  C CB  . LYS B 2 51  ? -22.639 40.542  19.981  1.00 41.55  ? 51  LYS B CB  1 
ATOM   2918  C CG  . LYS B 2 51  ? -21.857 39.256  19.749  1.00 44.75  ? 51  LYS B CG  1 
ATOM   2919  C CD  . LYS B 2 51  ? -22.446 38.437  18.620  1.00 44.63  ? 51  LYS B CD  1 
ATOM   2920  C CE  . LYS B 2 51  ? -23.801 37.867  19.010  1.00 53.65  ? 51  LYS B CE  1 
ATOM   2921  N NZ  . LYS B 2 51  ? -24.106 36.626  18.252  1.00 51.89  ? 51  LYS B NZ  1 
ATOM   2922  N N   . VAL B 2 52  ? -20.260 42.448  19.385  1.00 45.56  ? 52  VAL B N   1 
ATOM   2923  C CA  . VAL B 2 52  ? -18.903 42.645  18.882  1.00 45.70  ? 52  VAL B CA  1 
ATOM   2924  C C   . VAL B 2 52  ? -18.063 43.402  19.900  1.00 47.95  ? 52  VAL B C   1 
ATOM   2925  O O   . VAL B 2 52  ? -16.907 43.049  20.160  1.00 50.21  ? 52  VAL B O   1 
ATOM   2926  C CB  . VAL B 2 52  ? -18.934 43.368  17.523  1.00 43.84  ? 52  VAL B CB  1 
ATOM   2927  C CG1 . VAL B 2 52  ? -17.539 43.799  17.126  1.00 39.97  ? 52  VAL B CG1 1 
ATOM   2928  C CG2 . VAL B 2 52  ? -19.530 42.466  16.459  1.00 39.43  ? 52  VAL B CG2 1 
ATOM   2929  N N   . ASN B 2 53  ? -18.632 44.452  20.498  1.00 49.71  ? 53  ASN B N   1 
ATOM   2930  C CA  . ASN B 2 53  ? -17.900 45.226  21.494  1.00 41.66  ? 53  ASN B CA  1 
ATOM   2931  C C   . ASN B 2 53  ? -17.601 44.398  22.738  1.00 46.67  ? 53  ASN B C   1 
ATOM   2932  O O   . ASN B 2 53  ? -16.527 44.536  23.335  1.00 48.94  ? 53  ASN B O   1 
ATOM   2933  C CB  . ASN B 2 53  ? -18.687 46.483  21.858  1.00 48.03  ? 53  ASN B CB  1 
ATOM   2934  C CG  . ASN B 2 53  ? -18.732 47.482  20.724  1.00 49.61  ? 53  ASN B CG  1 
ATOM   2935  O OD1 . ASN B 2 53  ? -17.825 47.527  19.890  1.00 48.56  ? 53  ASN B OD1 1 
ATOM   2936  N ND2 . ASN B 2 53  ? -19.786 48.292  20.685  1.00 45.60  ? 53  ASN B ND2 1 
ATOM   2937  N N   . SER B 2 54  ? -18.537 43.541  23.150  1.00 44.70  ? 54  SER B N   1 
ATOM   2938  C CA  . SER B 2 54  ? -18.284 42.682  24.303  1.00 42.92  ? 54  SER B CA  1 
ATOM   2939  C C   . SER B 2 54  ? -17.129 41.727  24.033  1.00 47.83  ? 54  SER B C   1 
ATOM   2940  O O   . SER B 2 54  ? -16.280 41.504  24.903  1.00 43.60  ? 54  SER B O   1 
ATOM   2941  C CB  . SER B 2 54  ? -19.544 41.903  24.666  1.00 38.05  ? 54  SER B CB  1 
ATOM   2942  O OG  . SER B 2 54  ? -20.450 42.725  25.373  1.00 50.08  ? 54  SER B OG  1 
ATOM   2943  N N   . ILE B 2 55  ? -17.074 41.162  22.827  1.00 37.83  ? 55  ILE B N   1 
ATOM   2944  C CA  . ILE B 2 55  ? -15.976 40.269  22.480  1.00 42.83  ? 55  ILE B CA  1 
ATOM   2945  C C   . ILE B 2 55  ? -14.657 41.026  22.481  1.00 45.99  ? 55  ILE B C   1 
ATOM   2946  O O   . ILE B 2 55  ? -13.612 40.476  22.852  1.00 46.02  ? 55  ILE B O   1 
ATOM   2947  C CB  . ILE B 2 55  ? -16.261 39.595  21.124  1.00 41.68  ? 55  ILE B CB  1 
ATOM   2948  C CG1 . ILE B 2 55  ? -17.467 38.663  21.247  1.00 38.61  ? 55  ILE B CG1 1 
ATOM   2949  C CG2 . ILE B 2 55  ? -15.047 38.832  20.622  1.00 39.99  ? 55  ILE B CG2 1 
ATOM   2950  C CD1 . ILE B 2 55  ? -18.226 38.479  19.954  1.00 45.57  ? 55  ILE B CD1 1 
ATOM   2951  N N   . ILE B 2 56  ? -14.681 42.298  22.088  1.00 41.74  ? 56  ILE B N   1 
ATOM   2952  C CA  . ILE B 2 56  ? -13.458 43.090  22.048  1.00 48.37  ? 56  ILE B CA  1 
ATOM   2953  C C   . ILE B 2 56  ? -13.129 43.661  23.425  1.00 51.57  ? 56  ILE B C   1 
ATOM   2954  O O   . ILE B 2 56  ? -12.014 43.494  23.932  1.00 49.60  ? 56  ILE B O   1 
ATOM   2955  C CB  . ILE B 2 56  ? -13.588 44.204  20.995  1.00 48.61  ? 56  ILE B CB  1 
ATOM   2956  C CG1 . ILE B 2 56  ? -13.631 43.597  19.589  1.00 44.62  ? 56  ILE B CG1 1 
ATOM   2957  C CG2 . ILE B 2 56  ? -12.448 45.197  21.138  1.00 28.51  ? 56  ILE B CG2 1 
ATOM   2958  C CD1 . ILE B 2 56  ? -13.983 44.592  18.506  1.00 37.13  ? 56  ILE B CD1 1 
ATOM   2959  N N   . ASP B 2 57  ? -14.098 44.327  24.058  1.00 48.07  ? 57  ASP B N   1 
ATOM   2960  C CA  . ASP B 2 57  ? -13.807 45.105  25.259  1.00 45.93  ? 57  ASP B CA  1 
ATOM   2961  C C   . ASP B 2 57  ? -13.580 44.244  26.496  1.00 53.94  ? 57  ASP B C   1 
ATOM   2962  O O   . ASP B 2 57  ? -13.073 44.757  27.498  1.00 57.31  ? 57  ASP B O   1 
ATOM   2963  C CB  . ASP B 2 57  ? -14.937 46.098  25.527  1.00 54.82  ? 57  ASP B CB  1 
ATOM   2964  C CG  . ASP B 2 57  ? -15.110 47.103  24.401  1.00 63.61  ? 57  ASP B CG  1 
ATOM   2965  O OD1 . ASP B 2 57  ? -14.167 47.268  23.595  1.00 65.85  ? 57  ASP B OD1 1 
ATOM   2966  O OD2 . ASP B 2 57  ? -16.190 47.725  24.322  1.00 62.45  ? 57  ASP B OD2 1 
ATOM   2967  N N   . LYS B 2 58  ? -13.946 42.963  26.467  1.00 54.69  ? 58  LYS B N   1 
ATOM   2968  C CA  . LYS B 2 58  ? -13.701 42.109  27.623  1.00 45.48  ? 58  LYS B CA  1 
ATOM   2969  C C   . LYS B 2 58  ? -12.288 41.547  27.653  1.00 47.87  ? 58  LYS B C   1 
ATOM   2970  O O   . LYS B 2 58  ? -11.905 40.933  28.655  1.00 47.01  ? 58  LYS B O   1 
ATOM   2971  C CB  . LYS B 2 58  ? -14.709 40.955  27.664  1.00 50.64  ? 58  LYS B CB  1 
ATOM   2972  C CG  . LYS B 2 58  ? -16.130 41.378  28.018  1.00 49.17  ? 58  LYS B CG  1 
ATOM   2973  C CD  . LYS B 2 58  ? -16.283 41.643  29.503  1.00 42.92  ? 58  LYS B CD  1 
ATOM   2974  C CE  . LYS B 2 58  ? -17.672 42.175  29.821  1.00 44.62  ? 58  LYS B CE  1 
ATOM   2975  N NZ  . LYS B 2 58  ? -17.801 42.547  31.258  1.00 48.03  ? 58  LYS B NZ  1 
ATOM   2976  N N   . MET B 2 59  ? -11.515 41.727  26.586  1.00 53.12  ? 59  MET B N   1 
ATOM   2977  C CA  . MET B 2 59  ? -10.131 41.277  26.586  1.00 49.89  ? 59  MET B CA  1 
ATOM   2978  C C   . MET B 2 59  ? -9.302  42.149  27.515  1.00 53.64  ? 59  MET B C   1 
ATOM   2979  O O   . MET B 2 59  ? -9.343  43.380  27.433  1.00 60.52  ? 59  MET B O   1 
ATOM   2980  C CB  . MET B 2 59  ? -9.556  41.321  25.171  1.00 49.38  ? 59  MET B CB  1 
ATOM   2981  C CG  . MET B 2 59  ? -8.165  40.720  25.043  1.00 47.30  ? 59  MET B CG  1 
ATOM   2982  S SD  . MET B 2 59  ? -8.056  39.037  25.685  1.00 56.83  ? 59  MET B SD  1 
ATOM   2983  C CE  . MET B 2 59  ? -8.575  38.106  24.242  1.00 46.22  ? 59  MET B CE  1 
ATOM   2984  N N   . ASN B 2 60  ? -8.545  41.511  28.398  1.00 60.82  ? 60  ASN B N   1 
ATOM   2985  C CA  . ASN B 2 60  ? -7.653  42.217  29.304  1.00 66.91  ? 60  ASN B CA  1 
ATOM   2986  C C   . ASN B 2 60  ? -6.249  42.182  28.724  1.00 59.39  ? 60  ASN B C   1 
ATOM   2987  O O   . ASN B 2 60  ? -5.693  41.101  28.490  1.00 55.74  ? 60  ASN B O   1 
ATOM   2988  C CB  . ASN B 2 60  ? -7.686  41.603  30.701  1.00 60.90  ? 60  ASN B CB  1 
ATOM   2989  C CG  . ASN B 2 60  ? -6.782  42.329  31.677  1.00 70.88  ? 60  ASN B CG  1 
ATOM   2990  O OD1 . ASN B 2 60  ? -6.976  43.514  31.967  1.00 70.95  ? 60  ASN B OD1 1 
ATOM   2991  N ND2 . ASN B 2 60  ? -5.791  41.616  32.201  1.00 61.61  ? 60  ASN B ND2 1 
ATOM   2992  N N   . THR B 2 61  ? -5.692  43.363  28.476  1.00 63.74  ? 61  THR B N   1 
ATOM   2993  C CA  . THR B 2 61  ? -4.354  43.489  27.921  1.00 65.31  ? 61  THR B CA  1 
ATOM   2994  C C   . THR B 2 61  ? -3.433  44.148  28.930  1.00 56.99  ? 61  THR B C   1 
ATOM   2995  O O   . THR B 2 61  ? -3.790  45.141  29.587  1.00 65.92  ? 61  THR B O   1 
ATOM   2996  C CB  . THR B 2 61  ? -4.327  44.263  26.609  1.00 59.66  ? 61  THR B CB  1 
ATOM   2997  O OG1 . THR B 2 61  ? -4.611  45.642  26.855  1.00 84.93  ? 61  THR B OG1 1 
ATOM   2998  C CG2 . THR B 2 61  ? -5.348  43.685  25.658  1.00 47.94  ? 61  THR B CG2 1 
ATOM   2999  N N   . GLN B 2 62  ? -2.236  43.593  28.991  1.00 61.66  ? 62  GLN B N   1 
ATOM   3000  C CA  . GLN B 2 62  ? -1.262  43.791  30.035  1.00 53.16  ? 62  GLN B CA  1 
ATOM   3001  C C   . GLN B 2 62  ? 0.087   44.097  29.384  1.00 51.11  ? 62  GLN B C   1 
ATOM   3002  O O   . GLN B 2 62  ? 0.371   43.636  28.277  1.00 50.54  ? 62  GLN B O   1 
ATOM   3003  C CB  . GLN B 2 62  ? -1.240  42.523  30.921  1.00 59.18  ? 62  GLN B CB  1 
ATOM   3004  C CG  . GLN B 2 62  ? -2.077  42.694  32.193  1.00 69.73  ? 62  GLN B CG  1 
ATOM   3005  C CD  . GLN B 2 62  ? -2.012  41.396  32.915  1.00 62.39  ? 62  GLN B CD  1 
ATOM   3006  O OE1 . GLN B 2 62  ? -1.785  40.403  32.256  1.00 64.38  ? 62  GLN B OE1 1 
ATOM   3007  N NE2 . GLN B 2 62  ? -2.004  41.381  34.304  1.00 71.42  ? 62  GLN B NE2 1 
ATOM   3008  N N   . PHE B 2 63  ? 0.887   44.976  29.996  1.00 56.64  ? 63  PHE B N   1 
ATOM   3009  C CA  . PHE B 2 63  ? 2.220   45.201  29.439  1.00 46.59  ? 63  PHE B CA  1 
ATOM   3010  C C   . PHE B 2 63  ? 3.036   43.938  29.655  1.00 54.19  ? 63  PHE B C   1 
ATOM   3011  O O   . PHE B 2 63  ? 3.135   43.447  30.784  1.00 42.41  ? 63  PHE B O   1 
ATOM   3012  C CB  . PHE B 2 63  ? 2.938   46.402  30.074  1.00 40.90  ? 63  PHE B CB  1 
ATOM   3013  C CG  . PHE B 2 63  ? 4.433   46.441  29.776  1.00 48.99  ? 63  PHE B CG  1 
ATOM   3014  C CD1 . PHE B 2 63  ? 4.914   47.041  28.621  1.00 54.48  ? 63  PHE B CD1 1 
ATOM   3015  C CD2 . PHE B 2 63  ? 5.349   45.869  30.651  1.00 49.57  ? 63  PHE B CD2 1 
ATOM   3016  C CE1 . PHE B 2 63  ? 6.273   47.071  28.345  1.00 55.57  ? 63  PHE B CE1 1 
ATOM   3017  C CE2 . PHE B 2 63  ? 6.707   45.898  30.379  1.00 56.45  ? 63  PHE B CE2 1 
ATOM   3018  C CZ  . PHE B 2 63  ? 7.168   46.501  29.226  1.00 47.80  ? 63  PHE B CZ  1 
ATOM   3019  N N   . GLU B 2 64  ? 3.604   43.404  28.575  1.00 42.09  ? 64  GLU B N   1 
ATOM   3020  C CA  . GLU B 2 64  ? 4.521   42.273  28.638  1.00 48.81  ? 64  GLU B CA  1 
ATOM   3021  C C   . GLU B 2 64  ? 5.754   42.579  27.797  1.00 43.39  ? 64  GLU B C   1 
ATOM   3022  O O   . GLU B 2 64  ? 5.683   43.319  26.813  1.00 41.75  ? 64  GLU B O   1 
ATOM   3023  C CB  . GLU B 2 64  ? 3.871   40.966  28.135  1.00 44.52  ? 64  GLU B CB  1 
ATOM   3024  C CG  . GLU B 2 64  ? 2.783   40.364  29.028  1.00 46.88  ? 64  GLU B CG  1 
ATOM   3025  C CD  . GLU B 2 64  ? 3.112   40.403  30.517  1.00 54.14  ? 64  GLU B CD  1 
ATOM   3026  O OE1 . GLU B 2 64  ? 4.246   40.045  30.903  1.00 59.56  ? 64  GLU B OE1 1 
ATOM   3027  O OE2 . GLU B 2 64  ? 2.218   40.769  31.309  1.00 59.31  ? 64  GLU B OE2 1 
ATOM   3028  N N   . ALA B 2 65  ? 6.890   42.008  28.185  1.00 42.93  ? 65  ALA B N   1 
ATOM   3029  C CA  . ALA B 2 65  ? 8.118   42.129  27.404  1.00 44.75  ? 65  ALA B CA  1 
ATOM   3030  C C   . ALA B 2 65  ? 8.573   40.722  27.039  1.00 30.35  ? 65  ALA B C   1 
ATOM   3031  O O   . ALA B 2 65  ? 8.990   39.954  27.911  1.00 49.43  ? 65  ALA B O   1 
ATOM   3032  C CB  . ALA B 2 65  ? 9.195   42.895  28.173  1.00 38.39  ? 65  ALA B CB  1 
ATOM   3033  N N   . VAL B 2 66  ? 8.472   40.378  25.757  1.00 43.70  ? 66  VAL B N   1 
ATOM   3034  C CA  . VAL B 2 66  ? 8.719   39.021  25.280  1.00 44.18  ? 66  VAL B CA  1 
ATOM   3035  C C   . VAL B 2 66  ? 10.001  39.024  24.463  1.00 47.19  ? 66  VAL B C   1 
ATOM   3036  O O   . VAL B 2 66  ? 10.074  39.659  23.403  1.00 45.50  ? 66  VAL B O   1 
ATOM   3037  C CB  . VAL B 2 66  ? 7.543   38.482  24.449  1.00 46.88  ? 66  VAL B CB  1 
ATOM   3038  C CG1 . VAL B 2 66  ? 7.763   37.011  24.125  1.00 46.81  ? 66  VAL B CG1 1 
ATOM   3039  C CG2 . VAL B 2 66  ? 6.216   38.676  25.191  1.00 22.53  ? 66  VAL B CG2 1 
ATOM   3040  N N   . GLY B 2 67  ? 11.005  38.299  24.948  1.00 57.61  ? 67  GLY B N   1 
ATOM   3041  C CA  . GLY B 2 67  ? 12.266  38.167  24.246  1.00 46.17  ? 67  GLY B CA  1 
ATOM   3042  C C   . GLY B 2 67  ? 12.951  36.852  24.556  1.00 51.04  ? 67  GLY B C   1 
ATOM   3043  O O   . GLY B 2 67  ? 12.372  35.986  25.219  1.00 64.70  ? 67  GLY B O   1 
ATOM   3044  N N   . ARG B 2 68  ? 14.181  36.688  24.081  1.00 53.88  ? 68  ARG B N   1 
ATOM   3045  C CA  . ARG B 2 68  ? 14.984  35.494  24.340  1.00 42.00  ? 68  ARG B CA  1 
ATOM   3046  C C   . ARG B 2 68  ? 16.207  35.919  25.141  1.00 40.19  ? 68  ARG B C   1 
ATOM   3047  O O   . ARG B 2 68  ? 17.218  36.336  24.565  1.00 59.17  ? 68  ARG B O   1 
ATOM   3048  C CB  . ARG B 2 68  ? 15.381  34.810  23.038  1.00 42.79  ? 68  ARG B CB  1 
ATOM   3049  C CG  . ARG B 2 68  ? 14.204  34.415  22.184  1.00 41.28  ? 68  ARG B CG  1 
ATOM   3050  C CD  . ARG B 2 68  ? 13.194  33.612  22.995  1.00 38.50  ? 68  ARG B CD  1 
ATOM   3051  N NE  . ARG B 2 68  ? 12.221  32.952  22.132  1.00 54.63  ? 68  ARG B NE  1 
ATOM   3052  C CZ  . ARG B 2 68  ? 10.909  32.976  22.326  1.00 38.76  ? 68  ARG B CZ  1 
ATOM   3053  N NH1 . ARG B 2 68  ? 10.375  33.614  23.353  1.00 38.99  ? 68  ARG B NH1 1 
ATOM   3054  N NH2 . ARG B 2 68  ? 10.115  32.337  21.472  1.00 46.41  ? 68  ARG B NH2 1 
ATOM   3055  N N   . GLU B 2 69  ? 16.124  35.798  26.467  1.00 47.47  ? 69  GLU B N   1 
ATOM   3056  C CA  . GLU B 2 69  ? 17.141  36.320  27.371  1.00 47.53  ? 69  GLU B CA  1 
ATOM   3057  C C   . GLU B 2 69  ? 17.983  35.226  28.025  1.00 45.30  ? 69  GLU B C   1 
ATOM   3058  O O   . GLU B 2 69  ? 18.699  35.503  28.991  1.00 52.93  ? 69  GLU B O   1 
ATOM   3059  C CB  . GLU B 2 69  ? 16.486  37.194  28.442  1.00 43.82  ? 69  GLU B CB  1 
ATOM   3060  C CG  . GLU B 2 69  ? 15.879  38.485  27.902  1.00 52.33  ? 69  GLU B CG  1 
ATOM   3061  C CD  . GLU B 2 69  ? 16.355  39.726  28.649  1.00 68.65  ? 69  GLU B CD  1 
ATOM   3062  O OE1 . GLU B 2 69  ? 17.584  39.959  28.725  1.00 67.67  ? 69  GLU B OE1 1 
ATOM   3063  O OE2 . GLU B 2 69  ? 15.491  40.472  29.159  1.00 68.35  ? 69  GLU B OE2 1 
ATOM   3064  N N   . PHE B 2 70  ? 17.931  33.997  27.517  1.00 43.95  ? 70  PHE B N   1 
ATOM   3065  C CA  . PHE B 2 70  ? 18.663  32.881  28.103  1.00 47.31  ? 70  PHE B CA  1 
ATOM   3066  C C   . PHE B 2 70  ? 19.750  32.392  27.151  1.00 47.77  ? 70  PHE B C   1 
ATOM   3067  O O   . PHE B 2 70  ? 19.553  32.360  25.932  1.00 51.39  ? 70  PHE B O   1 
ATOM   3068  C CB  . PHE B 2 70  ? 17.706  31.742  28.462  1.00 49.55  ? 70  PHE B CB  1 
ATOM   3069  C CG  . PHE B 2 70  ? 16.686  32.122  29.501  1.00 43.22  ? 70  PHE B CG  1 
ATOM   3070  C CD1 . PHE B 2 70  ? 17.053  32.271  30.831  1.00 38.71  ? 70  PHE B CD1 1 
ATOM   3071  C CD2 . PHE B 2 70  ? 15.363  32.348  29.147  1.00 49.11  ? 70  PHE B CD2 1 
ATOM   3072  C CE1 . PHE B 2 70  ? 16.118  32.633  31.792  1.00 37.46  ? 70  PHE B CE1 1 
ATOM   3073  C CE2 . PHE B 2 70  ? 14.421  32.711  30.103  1.00 36.31  ? 70  PHE B CE2 1 
ATOM   3074  C CZ  . PHE B 2 70  ? 14.800  32.853  31.426  1.00 43.46  ? 70  PHE B CZ  1 
ATOM   3075  N N   . ASN B 2 71  ? 20.898  32.012  27.717  1.00 41.38  ? 71  ASN B N   1 
ATOM   3076  C CA  . ASN B 2 71  ? 22.090  31.688  26.945  1.00 43.74  ? 71  ASN B CA  1 
ATOM   3077  C C   . ASN B 2 71  ? 22.151  30.189  26.639  1.00 58.37  ? 71  ASN B C   1 
ATOM   3078  O O   . ASN B 2 71  ? 21.203  29.437  26.885  1.00 42.96  ? 71  ASN B O   1 
ATOM   3079  C CB  . ASN B 2 71  ? 23.344  32.162  27.681  1.00 40.48  ? 71  ASN B CB  1 
ATOM   3080  C CG  . ASN B 2 71  ? 23.524  31.495  29.036  1.00 50.04  ? 71  ASN B CG  1 
ATOM   3081  O OD1 . ASN B 2 71  ? 23.514  30.266  29.151  1.00 50.35  ? 71  ASN B OD1 1 
ATOM   3082  N ND2 . ASN B 2 71  ? 23.706  32.308  30.071  1.00 47.74  ? 71  ASN B ND2 1 
ATOM   3083  N N   . ASN B 2 72  ? 23.299  29.737  26.119  1.00 49.43  ? 72  ASN B N   1 
ATOM   3084  C CA  . ASN B 2 72  ? 23.436  28.376  25.609  1.00 51.97  ? 72  ASN B CA  1 
ATOM   3085  C C   . ASN B 2 72  ? 23.527  27.326  26.708  1.00 50.18  ? 72  ASN B C   1 
ATOM   3086  O O   . ASN B 2 72  ? 23.387  26.135  26.409  1.00 56.92  ? 72  ASN B O   1 
ATOM   3087  C CB  . ASN B 2 72  ? 24.659  28.271  24.692  1.00 57.91  ? 72  ASN B CB  1 
ATOM   3088  C CG  . ASN B 2 72  ? 25.964  28.162  25.462  1.00 82.63  ? 72  ASN B CG  1 
ATOM   3089  O OD1 . ASN B 2 72  ? 26.119  28.751  26.536  1.00 75.50  ? 72  ASN B OD1 1 
ATOM   3090  N ND2 . ASN B 2 72  ? 26.909  27.398  24.920  1.00 90.78  ? 72  ASN B ND2 1 
ATOM   3091  N N   . LEU B 2 73  ? 23.761  27.721  27.959  1.00 40.25  ? 73  LEU B N   1 
ATOM   3092  C CA  . LEU B 2 73  ? 23.728  26.782  29.074  1.00 50.24  ? 73  LEU B CA  1 
ATOM   3093  C C   . LEU B 2 73  ? 22.484  26.967  29.940  1.00 52.97  ? 73  LEU B C   1 
ATOM   3094  O O   . LEU B 2 73  ? 22.461  26.537  31.099  1.00 55.48  ? 73  LEU B O   1 
ATOM   3095  C CB  . LEU B 2 73  ? 24.999  26.898  29.914  1.00 39.21  ? 73  LEU B CB  1 
ATOM   3096  C CG  . LEU B 2 73  ? 26.187  26.162  29.281  1.00 59.23  ? 73  LEU B CG  1 
ATOM   3097  C CD1 . LEU B 2 73  ? 27.453  26.360  30.095  1.00 47.41  ? 73  LEU B CD1 1 
ATOM   3098  C CD2 . LEU B 2 73  ? 25.885  24.672  29.098  1.00 47.83  ? 73  LEU B CD2 1 
ATOM   3099  N N   . GLU B 2 74  ? 21.449  27.602  29.398  1.00 48.14  ? 74  GLU B N   1 
ATOM   3100  C CA  . GLU B 2 74  ? 20.152  27.712  30.049  1.00 47.52  ? 74  GLU B CA  1 
ATOM   3101  C C   . GLU B 2 74  ? 19.056  27.217  29.119  1.00 49.92  ? 74  GLU B C   1 
ATOM   3102  O O   . GLU B 2 74  ? 17.924  27.708  29.161  1.00 51.28  ? 74  GLU B O   1 
ATOM   3103  C CB  . GLU B 2 74  ? 19.876  29.153  30.481  1.00 45.16  ? 74  GLU B CB  1 
ATOM   3104  C CG  . GLU B 2 74  ? 20.832  29.697  31.530  1.00 42.17  ? 74  GLU B CG  1 
ATOM   3105  C CD  . GLU B 2 74  ? 20.869  31.220  31.541  1.00 50.94  ? 74  GLU B CD  1 
ATOM   3106  O OE1 . GLU B 2 74  ? 20.494  31.830  30.515  1.00 51.16  ? 74  GLU B OE1 1 
ATOM   3107  O OE2 . GLU B 2 74  ? 21.261  31.806  32.574  1.00 44.07  ? 74  GLU B OE2 1 
ATOM   3108  N N   . ARG B 2 75  ? 19.382  26.253  28.258  1.00 46.19  ? 75  ARG B N   1 
ATOM   3109  C CA  . ARG B 2 75  ? 18.429  25.834  27.243  1.00 47.40  ? 75  ARG B CA  1 
ATOM   3110  C C   . ARG B 2 75  ? 17.260  25.048  27.831  1.00 55.28  ? 75  ARG B C   1 
ATOM   3111  O O   . ARG B 2 75  ? 16.220  24.930  27.178  1.00 57.00  ? 75  ARG B O   1 
ATOM   3112  C CB  . ARG B 2 75  ? 19.154  25.021  26.166  1.00 46.03  ? 75  ARG B CB  1 
ATOM   3113  C CG  . ARG B 2 75  ? 20.263  25.792  25.415  1.00 50.10  ? 75  ARG B CG  1 
ATOM   3114  C CD  . ARG B 2 75  ? 19.838  26.247  24.010  1.00 75.45  ? 75  ARG B CD  1 
ATOM   3115  N NE  . ARG B 2 75  ? 20.647  27.350  23.474  1.00 83.45  ? 75  ARG B NE  1 
ATOM   3116  C CZ  . ARG B 2 75  ? 20.383  28.653  23.572  1.00 85.32  ? 75  ARG B CZ  1 
ATOM   3117  N NH1 . ARG B 2 75  ? 19.281  29.101  24.158  1.00 78.05  ? 75  ARG B NH1 1 
ATOM   3118  N NH2 . ARG B 2 75  ? 21.241  29.532  23.043  1.00 74.92  ? 75  ARG B NH2 1 
ATOM   3119  N N   . ARG B 2 76  ? 17.399  24.513  29.048  1.00 51.05  ? 76  ARG B N   1 
ATOM   3120  C CA  . ARG B 2 76  ? 16.249  23.898  29.707  1.00 43.14  ? 76  ARG B CA  1 
ATOM   3121  C C   . ARG B 2 76  ? 15.207  24.945  30.081  1.00 47.91  ? 76  ARG B C   1 
ATOM   3122  O O   . ARG B 2 76  ? 14.000  24.696  29.979  1.00 38.04  ? 76  ARG B O   1 
ATOM   3123  C CB  . ARG B 2 76  ? 16.696  23.124  30.951  1.00 40.39  ? 76  ARG B CB  1 
ATOM   3124  C CG  . ARG B 2 76  ? 17.463  21.834  30.656  1.00 47.14  ? 76  ARG B CG  1 
ATOM   3125  C CD  . ARG B 2 76  ? 18.165  21.291  31.901  1.00 38.05  ? 76  ARG B CD  1 
ATOM   3126  N NE  . ARG B 2 76  ? 18.910  22.327  32.607  1.00 40.74  ? 76  ARG B NE  1 
ATOM   3127  C CZ  . ARG B 2 76  ? 18.947  22.455  33.926  1.00 39.98  ? 76  ARG B CZ  1 
ATOM   3128  N NH1 . ARG B 2 76  ? 18.307  21.613  34.720  1.00 44.67  ? 76  ARG B NH1 1 
ATOM   3129  N NH2 . ARG B 2 76  ? 19.635  23.459  34.463  1.00 34.49  ? 76  ARG B NH2 1 
ATOM   3130  N N   . ILE B 2 77  ? 15.653  26.124  30.515  1.00 48.23  ? 77  ILE B N   1 
ATOM   3131  C CA  . ILE B 2 77  ? 14.723  27.143  30.991  1.00 50.69  ? 77  ILE B CA  1 
ATOM   3132  C C   . ILE B 2 77  ? 13.919  27.729  29.839  1.00 50.58  ? 77  ILE B C   1 
ATOM   3133  O O   . ILE B 2 77  ? 12.720  28.000  29.974  1.00 59.79  ? 77  ILE B O   1 
ATOM   3134  C CB  . ILE B 2 77  ? 15.485  28.227  31.766  1.00 45.24  ? 77  ILE B CB  1 
ATOM   3135  C CG1 . ILE B 2 77  ? 15.898  27.669  33.124  1.00 56.31  ? 77  ILE B CG1 1 
ATOM   3136  C CG2 . ILE B 2 77  ? 14.620  29.458  31.937  1.00 44.79  ? 77  ILE B CG2 1 
ATOM   3137  C CD1 . ILE B 2 77  ? 16.603  28.655  34.005  1.00 53.48  ? 77  ILE B CD1 1 
ATOM   3138  N N   . GLU B 2 78  ? 14.555  27.944  28.692  1.00 42.81  ? 78  GLU B N   1 
ATOM   3139  C CA  . GLU B 2 78  ? 13.818  28.484  27.558  1.00 53.43  ? 78  GLU B CA  1 
ATOM   3140  C C   . GLU B 2 78  ? 12.806  27.495  27.020  1.00 41.18  ? 78  GLU B C   1 
ATOM   3141  O O   . GLU B 2 78  ? 11.755  27.903  26.518  1.00 46.67  ? 78  GLU B O   1 
ATOM   3142  C CB  . GLU B 2 78  ? 14.776  28.833  26.456  1.00 36.33  ? 78  GLU B CB  1 
ATOM   3143  C CG  . GLU B 2 78  ? 15.841  27.842  26.408  1.00 67.62  ? 78  GLU B CG  1 
ATOM   3144  C CD  . GLU B 2 78  ? 16.856  28.240  25.416  1.00 95.84  ? 78  GLU B CD  1 
ATOM   3145  O OE1 . GLU B 2 78  ? 16.868  27.652  24.324  1.00 94.16  ? 78  GLU B OE1 1 
ATOM   3146  O OE2 . GLU B 2 78  ? 17.593  29.197  25.733  1.00 87.37  ? 78  GLU B OE2 1 
ATOM   3147  N N   . ASN B 2 79  ? 13.122  26.201  27.069  1.00 43.49  ? 79  ASN B N   1 
ATOM   3148  C CA  . ASN B 2 79  ? 12.108  25.207  26.755  1.00 47.86  ? 79  ASN B CA  1 
ATOM   3149  C C   . ASN B 2 79  ? 10.901  25.383  27.658  1.00 39.86  ? 79  ASN B C   1 
ATOM   3150  O O   . ASN B 2 79  ? 9.758   25.248  27.210  1.00 44.36  ? 79  ASN B O   1 
ATOM   3151  C CB  . ASN B 2 79  ? 12.673  23.796  26.887  1.00 39.71  ? 79  ASN B CB  1 
ATOM   3152  C CG  . ASN B 2 79  ? 11.705  22.739  26.399  1.00 42.27  ? 79  ASN B CG  1 
ATOM   3153  O OD1 . ASN B 2 79  ? 11.217  22.801  25.270  1.00 49.29  ? 79  ASN B OD1 1 
ATOM   3154  N ND2 . ASN B 2 79  ? 11.407  21.769  27.257  1.00 48.65  ? 79  ASN B ND2 1 
ATOM   3155  N N   . LEU B 2 80  ? 11.136  25.712  28.931  1.00 31.80  ? 80  LEU B N   1 
ATOM   3156  C CA  . LEU B 2 80  ? 10.030  26.050  29.818  1.00 39.43  ? 80  LEU B CA  1 
ATOM   3157  C C   . LEU B 2 80  ? 9.277   27.266  29.297  1.00 47.98  ? 80  LEU B C   1 
ATOM   3158  O O   . LEU B 2 80  ? 8.042   27.293  29.312  1.00 40.36  ? 80  LEU B O   1 
ATOM   3159  C CB  . LEU B 2 80  ? 10.544  26.290  31.238  1.00 41.81  ? 80  LEU B CB  1 
ATOM   3160  C CG  . LEU B 2 80  ? 9.516   26.725  32.285  1.00 56.89  ? 80  LEU B CG  1 
ATOM   3161  C CD1 . LEU B 2 80  ? 8.515   25.618  32.557  1.00 46.33  ? 80  LEU B CD1 1 
ATOM   3162  C CD2 . LEU B 2 80  ? 10.207  27.140  33.572  1.00 53.50  ? 80  LEU B CD2 1 
ATOM   3163  N N   . ASN B 2 81  ? 10.004  28.274  28.814  1.00 34.81  ? 81  ASN B N   1 
ATOM   3164  C CA  . ASN B 2 81  ? 9.339   29.417  28.199  1.00 33.66  ? 81  ASN B CA  1 
ATOM   3165  C C   . ASN B 2 81  ? 8.686   29.039  26.874  1.00 38.15  ? 81  ASN B C   1 
ATOM   3166  O O   . ASN B 2 81  ? 7.621   29.565  26.528  1.00 43.58  ? 81  ASN B O   1 
ATOM   3167  C CB  . ASN B 2 81  ? 10.329  30.557  27.991  1.00 32.85  ? 81  ASN B CB  1 
ATOM   3168  C CG  . ASN B 2 81  ? 9.713   31.715  27.246  1.00 33.67  ? 81  ASN B CG  1 
ATOM   3169  O OD1 . ASN B 2 81  ? 9.008   32.540  27.828  1.00 36.54  ? 81  ASN B OD1 1 
ATOM   3170  N ND2 . ASN B 2 81  ? 9.956   31.774  25.946  1.00 45.47  ? 81  ASN B ND2 1 
ATOM   3171  N N   . LYS B 2 82  ? 9.327   28.155  26.106  1.00 31.40  ? 82  LYS B N   1 
ATOM   3172  C CA  . LYS B 2 82  ? 8.747   27.702  24.846  1.00 40.40  ? 82  LYS B CA  1 
ATOM   3173  C C   . LYS B 2 82  ? 7.444   26.947  25.081  1.00 42.72  ? 82  LYS B C   1 
ATOM   3174  O O   . LYS B 2 82  ? 6.453   27.165  24.375  1.00 48.03  ? 82  LYS B O   1 
ATOM   3175  C CB  . LYS B 2 82  ? 9.754   26.826  24.100  1.00 34.46  ? 82  LYS B CB  1 
ATOM   3176  C CG  . LYS B 2 82  ? 9.430   26.579  22.637  1.00 41.36  ? 82  LYS B CG  1 
ATOM   3177  C CD  . LYS B 2 82  ? 9.536   25.093  22.296  1.00 47.77  ? 82  LYS B CD  1 
ATOM   3178  C CE  . LYS B 2 82  ? 9.474   24.856  20.792  1.00 45.27  ? 82  LYS B CE  1 
ATOM   3179  N NZ  . LYS B 2 82  ? 8.068   24.710  20.308  1.00 55.69  ? 82  LYS B NZ  1 
ATOM   3180  N N   . LYS B 2 83  ? 7.424   26.062  26.080  1.00 39.09  ? 83  LYS B N   1 
ATOM   3181  C CA  . LYS B 2 83  ? 6.201   25.342  26.406  1.00 45.02  ? 83  LYS B CA  1 
ATOM   3182  C C   . LYS B 2 83  ? 5.120   26.299  26.889  1.00 45.23  ? 83  LYS B C   1 
ATOM   3183  O O   . LYS B 2 83  ? 3.940   26.132  26.562  1.00 34.51  ? 83  LYS B O   1 
ATOM   3184  C CB  . LYS B 2 83  ? 6.493   24.271  27.457  1.00 42.63  ? 83  LYS B CB  1 
ATOM   3185  C CG  . LYS B 2 83  ? 7.082   23.000  26.878  1.00 45.68  ? 83  LYS B CG  1 
ATOM   3186  C CD  . LYS B 2 83  ? 7.190   21.894  27.914  1.00 41.30  ? 83  LYS B CD  1 
ATOM   3187  C CE  . LYS B 2 83  ? 8.210   22.240  28.991  1.00 45.58  ? 83  LYS B CE  1 
ATOM   3188  N NZ  . LYS B 2 83  ? 7.984   21.426  30.222  1.00 54.76  ? 83  LYS B NZ  1 
ATOM   3189  N N   . MET B 2 84  ? 5.508   27.315  27.661  1.00 48.11  ? 84  MET B N   1 
ATOM   3190  C CA  . MET B 2 84  ? 4.539   28.289  28.149  1.00 43.94  ? 84  MET B CA  1 
ATOM   3191  C C   . MET B 2 84  ? 3.964   29.120  27.005  1.00 47.57  ? 84  MET B C   1 
ATOM   3192  O O   . MET B 2 84  ? 2.743   29.292  26.903  1.00 48.27  ? 84  MET B O   1 
ATOM   3193  C CB  . MET B 2 84  ? 5.190   29.184  29.201  1.00 31.96  ? 84  MET B CB  1 
ATOM   3194  C CG  . MET B 2 84  ? 4.218   30.132  29.872  1.00 54.26  ? 84  MET B CG  1 
ATOM   3195  S SD  . MET B 2 84  ? 4.940   31.752  30.164  1.00 59.85  ? 84  MET B SD  1 
ATOM   3196  C CE  . MET B 2 84  ? 4.871   32.440  28.512  1.00 49.26  ? 84  MET B CE  1 
ATOM   3197  N N   . GLU B 2 85  ? 4.828   29.632  26.123  1.00 46.45  ? 85  GLU B N   1 
ATOM   3198  C CA  . GLU B 2 85  ? 4.347   30.444  25.008  1.00 46.69  ? 85  GLU B CA  1 
ATOM   3199  C C   . GLU B 2 85  ? 3.464   29.631  24.070  1.00 46.33  ? 85  GLU B C   1 
ATOM   3200  O O   . GLU B 2 85  ? 2.393   30.091  23.656  1.00 48.89  ? 85  GLU B O   1 
ATOM   3201  C CB  . GLU B 2 85  ? 5.527   31.038  24.240  1.00 39.40  ? 85  GLU B CB  1 
ATOM   3202  C CG  . GLU B 2 85  ? 6.064   32.333  24.812  1.00 57.26  ? 85  GLU B CG  1 
ATOM   3203  C CD  . GLU B 2 85  ? 7.270   32.849  24.046  1.00 58.38  ? 85  GLU B CD  1 
ATOM   3204  O OE1 . GLU B 2 85  ? 7.518   32.361  22.923  1.00 56.28  ? 85  GLU B OE1 1 
ATOM   3205  O OE2 . GLU B 2 85  ? 7.971   33.742  24.567  1.00 59.73  ? 85  GLU B OE2 1 
ATOM   3206  N N   . ASP B 2 86  ? 3.894   28.415  23.731  1.00 50.74  ? 86  ASP B N   1 
ATOM   3207  C CA  . ASP B 2 86  ? 3.117   27.579  22.824  1.00 46.60  ? 86  ASP B CA  1 
ATOM   3208  C C   . ASP B 2 86  ? 1.789   27.157  23.441  1.00 47.16  ? 86  ASP B C   1 
ATOM   3209  O O   . ASP B 2 86  ? 0.778   27.079  22.731  1.00 42.38  ? 86  ASP B O   1 
ATOM   3210  C CB  . ASP B 2 86  ? 3.942   26.360  22.419  1.00 44.15  ? 86  ASP B CB  1 
ATOM   3211  C CG  . ASP B 2 86  ? 5.142   26.731  21.566  1.00 58.27  ? 86  ASP B CG  1 
ATOM   3212  O OD1 . ASP B 2 86  ? 5.290   27.932  21.239  1.00 55.80  ? 86  ASP B OD1 1 
ATOM   3213  O OD2 . ASP B 2 86  ? 5.935   25.829  21.219  1.00 58.82  ? 86  ASP B OD2 1 
ATOM   3214  N N   . GLY B 2 87  ? 1.769   26.903  24.751  1.00 39.10  ? 87  GLY B N   1 
ATOM   3215  C CA  . GLY B 2 87  ? 0.516   26.577  25.411  1.00 34.80  ? 87  GLY B CA  1 
ATOM   3216  C C   . GLY B 2 87  ? -0.508  27.696  25.331  1.00 40.98  ? 87  GLY B C   1 
ATOM   3217  O O   . GLY B 2 87  ? -1.690  27.448  25.085  1.00 49.40  ? 87  GLY B O   1 
ATOM   3218  N N   . PHE B 2 88  ? -0.076  28.942  25.546  1.00 36.82  ? 88  PHE B N   1 
ATOM   3219  C CA  . PHE B 2 88  ? -1.021  30.056  25.489  1.00 39.02  ? 88  PHE B CA  1 
ATOM   3220  C C   . PHE B 2 88  ? -1.478  30.319  24.059  1.00 39.75  ? 88  PHE B C   1 
ATOM   3221  O O   . PHE B 2 88  ? -2.638  30.682  23.830  1.00 37.41  ? 88  PHE B O   1 
ATOM   3222  C CB  . PHE B 2 88  ? -0.407  31.318  26.102  1.00 33.92  ? 88  PHE B CB  1 
ATOM   3223  C CG  . PHE B 2 88  ? -0.456  31.343  27.607  1.00 41.66  ? 88  PHE B CG  1 
ATOM   3224  C CD1 . PHE B 2 88  ? -1.668  31.280  28.277  1.00 42.54  ? 88  PHE B CD1 1 
ATOM   3225  C CD2 . PHE B 2 88  ? 0.710   31.411  28.351  1.00 35.10  ? 88  PHE B CD2 1 
ATOM   3226  C CE1 . PHE B 2 88  ? -1.714  31.290  29.668  1.00 48.69  ? 88  PHE B CE1 1 
ATOM   3227  C CE2 . PHE B 2 88  ? 0.670   31.421  29.737  1.00 39.71  ? 88  PHE B CE2 1 
ATOM   3228  C CZ  . PHE B 2 88  ? -0.541  31.358  30.396  1.00 36.33  ? 88  PHE B CZ  1 
ATOM   3229  N N   . LEU B 2 89  ? -0.586  30.146  23.081  1.00 43.79  ? 89  LEU B N   1 
ATOM   3230  C CA  . LEU B 2 89  ? -1.002  30.304  21.690  1.00 47.82  ? 89  LEU B CA  1 
ATOM   3231  C C   . LEU B 2 89  ? -2.053  29.267  21.320  1.00 41.19  ? 89  LEU B C   1 
ATOM   3232  O O   . LEU B 2 89  ? -3.028  29.577  20.626  1.00 47.13  ? 89  LEU B O   1 
ATOM   3233  C CB  . LEU B 2 89  ? 0.204   30.202  20.757  1.00 50.10  ? 89  LEU B CB  1 
ATOM   3234  C CG  . LEU B 2 89  ? -0.113  30.145  19.259  1.00 52.91  ? 89  LEU B CG  1 
ATOM   3235  C CD1 . LEU B 2 89  ? 0.777   31.098  18.488  1.00 56.42  ? 89  LEU B CD1 1 
ATOM   3236  C CD2 . LEU B 2 89  ? 0.040   28.733  18.721  1.00 55.51  ? 89  LEU B CD2 1 
ATOM   3237  N N   . ASP B 2 90  ? -1.872  28.028  21.778  1.00 45.28  ? 90  ASP B N   1 
ATOM   3238  C CA  . ASP B 2 90  ? -2.864  26.992  21.525  1.00 37.21  ? 90  ASP B CA  1 
ATOM   3239  C C   . ASP B 2 90  ? -4.188  27.319  22.205  1.00 41.83  ? 90  ASP B C   1 
ATOM   3240  O O   . ASP B 2 90  ? -5.261  27.110  21.625  1.00 44.88  ? 90  ASP B O   1 
ATOM   3241  C CB  . ASP B 2 90  ? -2.331  25.638  21.993  1.00 39.73  ? 90  ASP B CB  1 
ATOM   3242  C CG  . ASP B 2 90  ? -1.183  25.133  21.132  1.00 50.71  ? 90  ASP B CG  1 
ATOM   3243  O OD1 . ASP B 2 90  ? -0.953  25.717  20.052  1.00 56.40  ? 90  ASP B OD1 1 
ATOM   3244  O OD2 . ASP B 2 90  ? -0.511  24.155  21.532  1.00 56.14  ? 90  ASP B OD2 1 
ATOM   3245  N N   . VAL B 2 91  ? -4.136  27.830  23.439  1.00 28.85  ? 91  VAL B N   1 
ATOM   3246  C CA  . VAL B 2 91  ? -5.367  28.153  24.159  1.00 40.90  ? 91  VAL B CA  1 
ATOM   3247  C C   . VAL B 2 91  ? -6.116  29.274  23.450  1.00 37.12  ? 91  VAL B C   1 
ATOM   3248  O O   . VAL B 2 91  ? -7.310  29.157  23.147  1.00 46.90  ? 91  VAL B O   1 
ATOM   3249  C CB  . VAL B 2 91  ? -5.050  28.519  25.621  1.00 39.71  ? 91  VAL B CB  1 
ATOM   3250  C CG1 . VAL B 2 91  ? -6.184  29.335  26.237  1.00 28.39  ? 91  VAL B CG1 1 
ATOM   3251  C CG2 . VAL B 2 91  ? -4.790  27.260  26.436  1.00 30.29  ? 91  VAL B CG2 1 
ATOM   3252  N N   . TRP B 2 92  ? -5.409  30.365  23.146  1.00 33.69  ? 92  TRP B N   1 
ATOM   3253  C CA  . TRP B 2 92  ? -6.032  31.529  22.527  1.00 33.90  ? 92  TRP B CA  1 
ATOM   3254  C C   . TRP B 2 92  ? -6.533  31.223  21.121  1.00 41.58  ? 92  TRP B C   1 
ATOM   3255  O O   . TRP B 2 92  ? -7.615  31.677  20.732  1.00 37.78  ? 92  TRP B O   1 
ATOM   3256  C CB  . TRP B 2 92  ? -5.041  32.691  22.499  1.00 37.63  ? 92  TRP B CB  1 
ATOM   3257  C CG  . TRP B 2 92  ? -4.844  33.350  23.837  1.00 33.14  ? 92  TRP B CG  1 
ATOM   3258  C CD1 . TRP B 2 92  ? -3.678  33.467  24.526  1.00 32.90  ? 92  TRP B CD1 1 
ATOM   3259  C CD2 . TRP B 2 92  ? -5.850  33.981  24.643  1.00 42.16  ? 92  TRP B CD2 1 
ATOM   3260  N NE1 . TRP B 2 92  ? -3.887  34.138  25.708  1.00 43.90  ? 92  TRP B NE1 1 
ATOM   3261  C CE2 . TRP B 2 92  ? -5.214  34.461  25.805  1.00 41.52  ? 92  TRP B CE2 1 
ATOM   3262  C CE3 . TRP B 2 92  ? -7.227  34.187  24.494  1.00 40.11  ? 92  TRP B CE3 1 
ATOM   3263  C CZ2 . TRP B 2 92  ? -5.905  35.134  26.813  1.00 41.02  ? 92  TRP B CZ2 1 
ATOM   3264  C CZ3 . TRP B 2 92  ? -7.911  34.855  25.497  1.00 42.09  ? 92  TRP B CZ3 1 
ATOM   3265  C CH2 . TRP B 2 92  ? -7.249  35.320  26.641  1.00 39.53  ? 92  TRP B CH2 1 
ATOM   3266  N N   . THR B 2 93  ? -5.757  30.476  20.335  1.00 37.85  ? 93  THR B N   1 
ATOM   3267  C CA  . THR B 2 93  ? -6.206  30.123  18.992  1.00 38.36  ? 93  THR B CA  1 
ATOM   3268  C C   . THR B 2 93  ? -7.475  29.282  19.039  1.00 42.92  ? 93  THR B C   1 
ATOM   3269  O O   . THR B 2 93  ? -8.438  29.551  18.312  1.00 47.35  ? 93  THR B O   1 
ATOM   3270  C CB  . THR B 2 93  ? -5.103  29.375  18.244  1.00 44.30  ? 93  THR B CB  1 
ATOM   3271  O OG1 . THR B 2 93  ? -3.873  30.096  18.360  1.00 46.08  ? 93  THR B OG1 1 
ATOM   3272  C CG2 . THR B 2 93  ? -5.466  29.205  16.778  1.00 41.91  ? 93  THR B CG2 1 
ATOM   3273  N N   . TYR B 2 94  ? -7.497  28.257  19.896  1.00 36.38  ? 94  TYR B N   1 
ATOM   3274  C CA  . TYR B 2 94  ? -8.658  27.376  19.952  1.00 35.80  ? 94  TYR B CA  1 
ATOM   3275  C C   . TYR B 2 94  ? -9.895  28.127  20.416  1.00 40.52  ? 94  TYR B C   1 
ATOM   3276  O O   . TYR B 2 94  ? -10.979 27.963  19.844  1.00 43.86  ? 94  TYR B O   1 
ATOM   3277  C CB  . TYR B 2 94  ? -8.378  26.190  20.873  1.00 37.01  ? 94  TYR B CB  1 
ATOM   3278  C CG  . TYR B 2 94  ? -9.395  25.078  20.781  1.00 38.38  ? 94  TYR B CG  1 
ATOM   3279  C CD1 . TYR B 2 94  ? -9.538  24.334  19.616  1.00 47.66  ? 94  TYR B CD1 1 
ATOM   3280  C CD2 . TYR B 2 94  ? -10.214 24.770  21.860  1.00 46.20  ? 94  TYR B CD2 1 
ATOM   3281  C CE1 . TYR B 2 94  ? -10.469 23.310  19.528  1.00 40.23  ? 94  TYR B CE1 1 
ATOM   3282  C CE2 . TYR B 2 94  ? -11.148 23.747  21.784  1.00 40.56  ? 94  TYR B CE2 1 
ATOM   3283  C CZ  . TYR B 2 94  ? -11.268 23.019  20.617  1.00 43.44  ? 94  TYR B CZ  1 
ATOM   3284  O OH  . TYR B 2 94  ? -12.188 21.998  20.541  1.00 41.14  ? 94  TYR B OH  1 
ATOM   3285  N N   . ASN B 2 95  ? -9.754  28.953  21.457  1.00 43.68  ? 95  ASN B N   1 
ATOM   3286  C CA  . ASN B 2 95  ? -10.896 29.706  21.963  1.00 43.12  ? 95  ASN B CA  1 
ATOM   3287  C C   . ASN B 2 95  ? -11.376 30.736  20.948  1.00 45.34  ? 95  ASN B C   1 
ATOM   3288  O O   . ASN B 2 95  ? -12.584 30.877  20.727  1.00 41.17  ? 95  ASN B O   1 
ATOM   3289  C CB  . ASN B 2 95  ? -10.539 30.375  23.288  1.00 41.67  ? 95  ASN B CB  1 
ATOM   3290  C CG  . ASN B 2 95  ? -10.544 29.395  24.449  1.00 68.71  ? 95  ASN B CG  1 
ATOM   3291  O OD1 . ASN B 2 95  ? -10.881 28.218  24.282  1.00 52.42  ? 95  ASN B OD1 1 
ATOM   3292  N ND2 . ASN B 2 95  ? -10.171 29.873  25.634  1.00 68.14  ? 95  ASN B ND2 1 
ATOM   3293  N N   . ALA B 2 96  ? -10.448 31.454  20.310  1.00 41.86  ? 96  ALA B N   1 
ATOM   3294  C CA  . ALA B 2 96  ? -10.843 32.466  19.334  1.00 40.70  ? 96  ALA B CA  1 
ATOM   3295  C C   . ALA B 2 96  ? -11.552 31.834  18.143  1.00 43.91  ? 96  ALA B C   1 
ATOM   3296  O O   . ALA B 2 96  ? -12.605 32.316  17.708  1.00 37.50  ? 96  ALA B O   1 
ATOM   3297  C CB  . ALA B 2 96  ? -9.624  33.265  18.876  1.00 34.07  ? 96  ALA B CB  1 
ATOM   3298  N N   . GLU B 2 97  ? -10.997 30.742  17.610  1.00 35.56  ? 97  GLU B N   1 
ATOM   3299  C CA  . GLU B 2 97  ? -11.633 30.082  16.473  1.00 38.66  ? 97  GLU B CA  1 
ATOM   3300  C C   . GLU B 2 97  ? -13.016 29.558  16.843  1.00 42.15  ? 97  GLU B C   1 
ATOM   3301  O O   . GLU B 2 97  ? -13.974 29.726  16.080  1.00 51.93  ? 97  GLU B O   1 
ATOM   3302  C CB  . GLU B 2 97  ? -10.750 28.947  15.949  1.00 47.73  ? 97  GLU B CB  1 
ATOM   3303  C CG  . GLU B 2 97  ? -9.429  29.408  15.322  1.00 45.64  ? 97  GLU B CG  1 
ATOM   3304  C CD  . GLU B 2 97  ? -9.583  29.885  13.884  1.00 57.24  ? 97  GLU B CD  1 
ATOM   3305  O OE1 . GLU B 2 97  ? -10.706 29.816  13.338  1.00 57.83  ? 97  GLU B OE1 1 
ATOM   3306  O OE2 . GLU B 2 97  ? -8.574  30.329  13.296  1.00 51.99  ? 97  GLU B OE2 1 
ATOM   3307  N N   . LEU B 2 98  ? -13.145 28.936  18.018  1.00 38.26  ? 98  LEU B N   1 
ATOM   3308  C CA  . LEU B 2 98  ? -14.440 28.401  18.427  1.00 47.26  ? 98  LEU B CA  1 
ATOM   3309  C C   . LEU B 2 98  ? -15.421 29.511  18.778  1.00 46.89  ? 98  LEU B C   1 
ATOM   3310  O O   . LEU B 2 98  ? -16.631 29.356  18.570  1.00 47.64  ? 98  LEU B O   1 
ATOM   3311  C CB  . LEU B 2 98  ? -14.273 27.449  19.609  1.00 38.50  ? 98  LEU B CB  1 
ATOM   3312  C CG  . LEU B 2 98  ? -14.382 25.959  19.284  1.00 38.14  ? 98  LEU B CG  1 
ATOM   3313  C CD1 . LEU B 2 98  ? -15.779 25.622  18.805  1.00 57.86  ? 98  LEU B CD1 1 
ATOM   3314  C CD2 . LEU B 2 98  ? -13.365 25.568  18.235  1.00 49.71  ? 98  LEU B CD2 1 
ATOM   3315  N N   . LEU B 2 99  ? -14.924 30.624  19.319  1.00 39.01  ? 99  LEU B N   1 
ATOM   3316  C CA  . LEU B 2 99  ? -15.795 31.747  19.646  1.00 41.37  ? 99  LEU B CA  1 
ATOM   3317  C C   . LEU B 2 99  ? -16.449 32.322  18.394  1.00 48.09  ? 99  LEU B C   1 
ATOM   3318  O O   . LEU B 2 99  ? -17.649 32.621  18.391  1.00 38.98  ? 99  LEU B O   1 
ATOM   3319  C CB  . LEU B 2 99  ? -14.996 32.826  20.373  1.00 45.61  ? 99  LEU B CB  1 
ATOM   3320  C CG  . LEU B 2 99  ? -15.795 33.828  21.202  1.00 61.20  ? 99  LEU B CG  1 
ATOM   3321  C CD1 . LEU B 2 99  ? -15.160 33.965  22.570  1.00 61.51  ? 99  LEU B CD1 1 
ATOM   3322  C CD2 . LEU B 2 99  ? -15.869 35.174  20.505  1.00 58.13  ? 99  LEU B CD2 1 
ATOM   3323  N N   . VAL B 2 100 ? -15.674 32.477  17.317  1.00 39.15  ? 100 VAL B N   1 
ATOM   3324  C CA  . VAL B 2 100 ? -16.233 33.009  16.079  1.00 50.07  ? 100 VAL B CA  1 
ATOM   3325  C C   . VAL B 2 100 ? -17.276 32.055  15.514  1.00 42.88  ? 100 VAL B C   1 
ATOM   3326  O O   . VAL B 2 100 ? -18.358 32.479  15.093  1.00 46.48  ? 100 VAL B O   1 
ATOM   3327  C CB  . VAL B 2 100 ? -15.112 33.293  15.061  1.00 43.27  ? 100 VAL B CB  1 
ATOM   3328  C CG1 . VAL B 2 100 ? -15.701 33.804  13.761  1.00 42.89  ? 100 VAL B CG1 1 
ATOM   3329  C CG2 . VAL B 2 100 ? -14.131 34.295  15.622  1.00 45.87  ? 100 VAL B CG2 1 
ATOM   3330  N N   . LEU B 2 101 ? -16.976 30.753  15.506  1.00 40.17  ? 101 LEU B N   1 
ATOM   3331  C CA  . LEU B 2 101 ? -17.919 29.777  14.966  1.00 41.47  ? 101 LEU B CA  1 
ATOM   3332  C C   . LEU B 2 101 ? -19.219 29.767  15.757  1.00 45.03  ? 101 LEU B C   1 
ATOM   3333  O O   . LEU B 2 101 ? -20.309 29.704  15.176  1.00 40.75  ? 101 LEU B O   1 
ATOM   3334  C CB  . LEU B 2 101 ? -17.291 28.381  14.963  1.00 36.73  ? 101 LEU B CB  1 
ATOM   3335  C CG  . LEU B 2 101 ? -16.062 28.197  14.073  1.00 44.89  ? 101 LEU B CG  1 
ATOM   3336  C CD1 . LEU B 2 101 ? -15.584 26.752  14.088  1.00 40.60  ? 101 LEU B CD1 1 
ATOM   3337  C CD2 . LEU B 2 101 ? -16.366 28.658  12.657  1.00 35.84  ? 101 LEU B CD2 1 
ATOM   3338  N N   . MET B 2 102 ? -19.120 29.818  17.087  1.00 44.07  ? 102 MET B N   1 
ATOM   3339  C CA  . MET B 2 102 ? -20.307 29.800  17.934  1.00 34.82  ? 102 MET B CA  1 
ATOM   3340  C C   . MET B 2 102 ? -21.107 31.085  17.788  1.00 41.06  ? 102 MET B C   1 
ATOM   3341  O O   . MET B 2 102 ? -22.333 31.051  17.632  1.00 40.43  ? 102 MET B O   1 
ATOM   3342  C CB  . MET B 2 102 ? -19.893 29.591  19.386  1.00 41.51  ? 102 MET B CB  1 
ATOM   3343  C CG  . MET B 2 102 ? -19.416 28.183  19.690  1.00 56.67  ? 102 MET B CG  1 
ATOM   3344  S SD  . MET B 2 102 ? -18.655 28.087  21.318  1.00 59.57  ? 102 MET B SD  1 
ATOM   3345  C CE  . MET B 2 102 ? -18.949 26.373  21.722  1.00 50.62  ? 102 MET B CE  1 
ATOM   3346  N N   . GLU B 2 103 ? -20.427 32.231  17.839  1.00 42.51  ? 103 GLU B N   1 
ATOM   3347  C CA  . GLU B 2 103 ? -21.130 33.507  17.792  1.00 38.72  ? 103 GLU B CA  1 
ATOM   3348  C C   . GLU B 2 103 ? -21.775 33.736  16.429  1.00 41.44  ? 103 GLU B C   1 
ATOM   3349  O O   . GLU B 2 103 ? -22.877 34.289  16.343  1.00 40.25  ? 103 GLU B O   1 
ATOM   3350  C CB  . GLU B 2 103 ? -20.171 34.641  18.149  1.00 44.49  ? 103 GLU B CB  1 
ATOM   3351  C CG  . GLU B 2 103 ? -20.033 34.890  19.656  1.00 44.85  ? 103 GLU B CG  1 
ATOM   3352  C CD  . GLU B 2 103 ? -21.314 34.598  20.436  1.00 62.53  ? 103 GLU B CD  1 
ATOM   3353  O OE1 . GLU B 2 103 ? -22.339 35.283  20.205  1.00 67.89  ? 103 GLU B OE1 1 
ATOM   3354  O OE2 . GLU B 2 103 ? -21.294 33.692  21.295  1.00 69.27  ? 103 GLU B OE2 1 
ATOM   3355  N N   . ASN B 2 104 ? -21.116 33.294  15.354  1.00 30.95  ? 104 ASN B N   1 
ATOM   3356  C CA  . ASN B 2 104 ? -21.711 33.414  14.027  1.00 38.05  ? 104 ASN B CA  1 
ATOM   3357  C C   . ASN B 2 104 ? -23.003 32.609  13.925  1.00 42.26  ? 104 ASN B C   1 
ATOM   3358  O O   . ASN B 2 104 ? -23.978 33.061  13.313  1.00 40.50  ? 104 ASN B O   1 
ATOM   3359  C CB  . ASN B 2 104 ? -20.712 32.968  12.961  1.00 36.28  ? 104 ASN B CB  1 
ATOM   3360  C CG  . ASN B 2 104 ? -19.598 33.977  12.745  1.00 40.88  ? 104 ASN B CG  1 
ATOM   3361  O OD1 . ASN B 2 104 ? -19.650 35.096  13.254  1.00 36.77  ? 104 ASN B OD1 1 
ATOM   3362  N ND2 . ASN B 2 104 ? -18.576 33.579  11.991  1.00 38.81  ? 104 ASN B ND2 1 
ATOM   3363  N N   . GLU B 2 105 ? -23.030 31.406  14.505  1.00 44.93  ? 105 GLU B N   1 
ATOM   3364  C CA  . GLU B 2 105 ? -24.264 30.628  14.507  1.00 39.31  ? 105 GLU B CA  1 
ATOM   3365  C C   . GLU B 2 105 ? -25.359 31.349  15.282  1.00 44.12  ? 105 GLU B C   1 
ATOM   3366  O O   . GLU B 2 105 ? -26.503 31.439  14.818  1.00 42.38  ? 105 GLU B O   1 
ATOM   3367  C CB  . GLU B 2 105 ? -24.012 29.240  15.094  1.00 43.54  ? 105 GLU B CB  1 
ATOM   3368  C CG  . GLU B 2 105 ? -25.205 28.301  14.989  1.00 50.81  ? 105 GLU B CG  1 
ATOM   3369  C CD  . GLU B 2 105 ? -25.153 27.413  13.751  1.00 74.17  ? 105 GLU B CD  1 
ATOM   3370  O OE1 . GLU B 2 105 ? -26.208 26.859  13.377  1.00 74.33  ? 105 GLU B OE1 1 
ATOM   3371  O OE2 . GLU B 2 105 ? -24.062 27.266  13.153  1.00 71.46  ? 105 GLU B OE2 1 
ATOM   3372  N N   . ARG B 2 106 ? -25.018 31.897  16.453  1.00 36.26  ? 106 ARG B N   1 
ATOM   3373  C CA  . ARG B 2 106 ? -26.002 32.636  17.236  1.00 42.19  ? 106 ARG B CA  1 
ATOM   3374  C C   . ARG B 2 106 ? -26.470 33.878  16.493  1.00 45.20  ? 106 ARG B C   1 
ATOM   3375  O O   . ARG B 2 106 ? -27.658 34.222  16.531  1.00 36.14  ? 106 ARG B O   1 
ATOM   3376  C CB  . ARG B 2 106 ? -25.423 33.022  18.597  1.00 39.59  ? 106 ARG B CB  1 
ATOM   3377  C CG  . ARG B 2 106 ? -24.743 31.888  19.337  1.00 63.82  ? 106 ARG B CG  1 
ATOM   3378  C CD  . ARG B 2 106 ? -25.739 30.863  19.845  1.00 56.66  ? 106 ARG B CD  1 
ATOM   3379  N NE  . ARG B 2 106 ? -25.171 30.053  20.918  1.00 84.25  ? 106 ARG B NE  1 
ATOM   3380  C CZ  . ARG B 2 106 ? -25.883 29.336  21.777  1.00 86.53  ? 106 ARG B CZ  1 
ATOM   3381  N NH1 . ARG B 2 106 ? -27.203 29.278  21.702  1.00 77.86  ? 106 ARG B NH1 1 
ATOM   3382  N NH2 . ARG B 2 106 ? -25.254 28.643  22.724  1.00 81.05  ? 106 ARG B NH2 1 
ATOM   3383  N N   . THR B 2 107 ? -25.549 34.568  15.815  1.00 40.56  ? 107 THR B N   1 
ATOM   3384  C CA  . THR B 2 107 ? -25.913 35.779  15.087  1.00 39.79  ? 107 THR B CA  1 
ATOM   3385  C C   . THR B 2 107 ? -26.909 35.475  13.973  1.00 35.13  ? 107 THR B C   1 
ATOM   3386  O O   . THR B 2 107 ? -27.932 36.155  13.841  1.00 33.50  ? 107 THR B O   1 
ATOM   3387  C CB  . THR B 2 107 ? -24.657 36.446  14.533  1.00 41.23  ? 107 THR B CB  1 
ATOM   3388  O OG1 . THR B 2 107 ? -23.893 36.989  15.620  1.00 48.30  ? 107 THR B OG1 1 
ATOM   3389  C CG2 . THR B 2 107 ? -25.020 37.565  13.565  1.00 32.64  ? 107 THR B CG2 1 
ATOM   3390  N N   . LEU B 2 108 ? -26.648 34.430  13.183  1.00 36.15  ? 108 LEU B N   1 
ATOM   3391  C CA  . LEU B 2 108 ? -27.570 34.077  12.106  1.00 42.88  ? 108 LEU B CA  1 
ATOM   3392  C C   . LEU B 2 108 ? -28.940 33.693  12.654  1.00 37.19  ? 108 LEU B C   1 
ATOM   3393  O O   . LEU B 2 108 ? -29.971 34.076  12.090  1.00 42.77  ? 108 LEU B O   1 
ATOM   3394  C CB  . LEU B 2 108 ? -26.989 32.943  11.258  1.00 33.42  ? 108 LEU B CB  1 
ATOM   3395  C CG  . LEU B 2 108 ? -25.682 33.260  10.521  1.00 52.56  ? 108 LEU B CG  1 
ATOM   3396  C CD1 . LEU B 2 108 ? -25.373 32.208  9.451   1.00 45.77  ? 108 LEU B CD1 1 
ATOM   3397  C CD2 . LEU B 2 108 ? -25.701 34.674  9.917   1.00 38.67  ? 108 LEU B CD2 1 
ATOM   3398  N N   . ASP B 2 109 ? -28.973 32.946  13.760  1.00 34.21  ? 109 ASP B N   1 
ATOM   3399  C CA  . ASP B 2 109 ? -30.251 32.568  14.353  1.00 33.51  ? 109 ASP B CA  1 
ATOM   3400  C C   . ASP B 2 109 ? -30.937 33.755  15.012  1.00 33.89  ? 109 ASP B C   1 
ATOM   3401  O O   . ASP B 2 109 ? -32.169 33.782  15.111  1.00 41.85  ? 109 ASP B O   1 
ATOM   3402  C CB  . ASP B 2 109 ? -30.046 31.441  15.359  1.00 43.15  ? 109 ASP B CB  1 
ATOM   3403  C CG  . ASP B 2 109 ? -29.723 30.123  14.686  1.00 60.09  ? 109 ASP B CG  1 
ATOM   3404  O OD1 . ASP B 2 109 ? -30.356 29.818  13.649  1.00 50.52  ? 109 ASP B OD1 1 
ATOM   3405  O OD2 . ASP B 2 109 ? -28.831 29.401  15.184  1.00 63.66  ? 109 ASP B OD2 1 
ATOM   3406  N N   . PHE B 2 110 ? -30.160 34.740  15.465  1.00 30.71  ? 110 PHE B N   1 
ATOM   3407  C CA  . PHE B 2 110 ? -30.750 35.966  15.989  1.00 34.32  ? 110 PHE B CA  1 
ATOM   3408  C C   . PHE B 2 110 ? -31.554 36.687  14.911  1.00 44.84  ? 110 PHE B C   1 
ATOM   3409  O O   . PHE B 2 110 ? -32.712 37.064  15.131  1.00 36.51  ? 110 PHE B O   1 
ATOM   3410  C CB  . PHE B 2 110 ? -29.650 36.869  16.546  1.00 28.97  ? 110 PHE B CB  1 
ATOM   3411  C CG  . PHE B 2 110 ? -30.146 38.195  17.043  1.00 42.98  ? 110 PHE B CG  1 
ATOM   3412  C CD1 . PHE B 2 110 ? -31.020 38.266  18.115  1.00 39.34  ? 110 PHE B CD1 1 
ATOM   3413  C CD2 . PHE B 2 110 ? -29.727 39.375  16.444  1.00 41.31  ? 110 PHE B CD2 1 
ATOM   3414  C CE1 . PHE B 2 110 ? -31.477 39.489  18.576  1.00 43.36  ? 110 PHE B CE1 1 
ATOM   3415  C CE2 . PHE B 2 110 ? -30.174 40.601  16.905  1.00 38.90  ? 110 PHE B CE2 1 
ATOM   3416  C CZ  . PHE B 2 110 ? -31.053 40.658  17.970  1.00 46.52  ? 110 PHE B CZ  1 
ATOM   3417  N N   . HIS B 2 111 ? -30.963 36.855  13.721  1.00 37.20  ? 111 HIS B N   1 
ATOM   3418  C CA  . HIS B 2 111 ? -31.693 37.466  12.614  1.00 42.04  ? 111 HIS B CA  1 
ATOM   3419  C C   . HIS B 2 111 ? -32.911 36.636  12.244  1.00 42.68  ? 111 HIS B C   1 
ATOM   3420  O O   . HIS B 2 111 ? -33.978 37.187  11.950  1.00 48.95  ? 111 HIS B O   1 
ATOM   3421  C CB  . HIS B 2 111 ? -30.782 37.631  11.399  1.00 35.39  ? 111 HIS B CB  1 
ATOM   3422  C CG  . HIS B 2 111 ? -29.654 38.587  11.613  1.00 43.31  ? 111 HIS B CG  1 
ATOM   3423  N ND1 . HIS B 2 111 ? -29.855 39.920  11.898  1.00 42.73  ? 111 HIS B ND1 1 
ATOM   3424  C CD2 . HIS B 2 111 ? -28.312 38.404  11.586  1.00 43.89  ? 111 HIS B CD2 1 
ATOM   3425  C CE1 . HIS B 2 111 ? -28.685 40.517  12.039  1.00 44.98  ? 111 HIS B CE1 1 
ATOM   3426  N NE2 . HIS B 2 111 ? -27.733 39.620  11.855  1.00 50.14  ? 111 HIS B NE2 1 
ATOM   3427  N N   . ASP B 2 112 ? -32.769 35.308  12.260  1.00 39.66  ? 112 ASP B N   1 
ATOM   3428  C CA  . ASP B 2 112 ? -33.894 34.426  11.967  1.00 36.85  ? 112 ASP B CA  1 
ATOM   3429  C C   . ASP B 2 112 ? -35.038 34.646  12.951  1.00 39.09  ? 112 ASP B C   1 
ATOM   3430  O O   . ASP B 2 112 ? -36.203 34.740  12.548  1.00 39.44  ? 112 ASP B O   1 
ATOM   3431  C CB  . ASP B 2 112 ? -33.428 32.970  11.999  1.00 44.70  ? 112 ASP B CB  1 
ATOM   3432  C CG  . ASP B 2 112 ? -34.307 32.055  11.174  1.00 49.41  ? 112 ASP B CG  1 
ATOM   3433  O OD1 . ASP B 2 112 ? -35.409 32.477  10.777  1.00 57.52  ? 112 ASP B OD1 1 
ATOM   3434  O OD2 . ASP B 2 112 ? -33.889 30.911  10.911  1.00 59.24  ? 112 ASP B OD2 1 
ATOM   3435  N N   . SER B 2 113 ? -34.726 34.737  14.245  1.00 42.55  ? 113 SER B N   1 
ATOM   3436  C CA  . SER B 2 113 ? -35.770 34.945  15.245  1.00 35.48  ? 113 SER B CA  1 
ATOM   3437  C C   . SER B 2 113 ? -36.445 36.300  15.065  1.00 44.29  ? 113 SER B C   1 
ATOM   3438  O O   . SER B 2 113 ? -37.667 36.419  15.217  1.00 46.93  ? 113 SER B O   1 
ATOM   3439  C CB  . SER B 2 113 ? -35.181 34.822  16.650  1.00 36.47  ? 113 SER B CB  1 
ATOM   3440  O OG  . SER B 2 113 ? -35.868 35.644  17.579  1.00 50.06  ? 113 SER B OG  1 
ATOM   3441  N N   . ASN B 2 114 ? -35.663 37.331  14.744  1.00 44.34  ? 114 ASN B N   1 
ATOM   3442  C CA  . ASN B 2 114 ? -36.229 38.666  14.584  1.00 37.83  ? 114 ASN B CA  1 
ATOM   3443  C C   . ASN B 2 114 ? -37.233 38.715  13.438  1.00 40.98  ? 114 ASN B C   1 
ATOM   3444  O O   . ASN B 2 114 ? -38.299 39.328  13.565  1.00 41.11  ? 114 ASN B O   1 
ATOM   3445  C CB  . ASN B 2 114 ? -35.106 39.674  14.366  1.00 36.24  ? 114 ASN B CB  1 
ATOM   3446  C CG  . ASN B 2 114 ? -34.310 39.920  15.621  1.00 35.69  ? 114 ASN B CG  1 
ATOM   3447  O OD1 . ASN B 2 114 ? -34.851 39.876  16.726  1.00 45.92  ? 114 ASN B OD1 1 
ATOM   3448  N ND2 . ASN B 2 114 ? -33.017 40.172  15.464  1.00 41.66  ? 114 ASN B ND2 1 
ATOM   3449  N N   . VAL B 2 115 ? -36.908 38.079  12.311  1.00 39.53  ? 115 VAL B N   1 
ATOM   3450  C CA  . VAL B 2 115 ? -37.837 38.048  11.186  1.00 43.52  ? 115 VAL B CA  1 
ATOM   3451  C C   . VAL B 2 115 ? -39.100 37.285  11.561  1.00 40.62  ? 115 VAL B C   1 
ATOM   3452  O O   . VAL B 2 115 ? -40.221 37.719  11.266  1.00 48.36  ? 115 VAL B O   1 
ATOM   3453  C CB  . VAL B 2 115 ? -37.154 37.438  9.948   1.00 37.71  ? 115 VAL B CB  1 
ATOM   3454  C CG1 . VAL B 2 115 ? -38.136 37.342  8.786   1.00 35.05  ? 115 VAL B CG1 1 
ATOM   3455  C CG2 . VAL B 2 115 ? -35.959 38.268  9.556   1.00 37.11  ? 115 VAL B CG2 1 
ATOM   3456  N N   . LYS B 2 116 ? -38.937 36.137  12.221  1.00 42.52  ? 116 LYS B N   1 
ATOM   3457  C CA  . LYS B 2 116 ? -40.086 35.317  12.580  1.00 42.68  ? 116 LYS B CA  1 
ATOM   3458  C C   . LYS B 2 116 ? -41.003 36.056  13.546  1.00 44.33  ? 116 LYS B C   1 
ATOM   3459  O O   . LYS B 2 116 ? -42.229 36.023  13.397  1.00 51.76  ? 116 LYS B O   1 
ATOM   3460  C CB  . LYS B 2 116 ? -39.608 33.989  13.175  1.00 46.08  ? 116 LYS B CB  1 
ATOM   3461  C CG  . LYS B 2 116 ? -40.694 33.147  13.816  1.00 37.11  ? 116 LYS B CG  1 
ATOM   3462  C CD  . LYS B 2 116 ? -41.399 32.266  12.798  1.00 61.65  ? 116 LYS B CD  1 
ATOM   3463  C CE  . LYS B 2 116 ? -42.753 31.814  13.323  1.00 61.66  ? 116 LYS B CE  1 
ATOM   3464  N NZ  . LYS B 2 116 ? -42.622 31.100  14.624  1.00 68.65  ? 116 LYS B NZ  1 
ATOM   3465  N N   . ASN B 2 117 ? -40.425 36.746  14.531  1.00 44.00  ? 117 ASN B N   1 
ATOM   3466  C CA  . ASN B 2 117 ? -41.239 37.498  15.479  1.00 43.23  ? 117 ASN B CA  1 
ATOM   3467  C C   . ASN B 2 117 ? -41.999 38.626  14.786  1.00 51.35  ? 117 ASN B C   1 
ATOM   3468  O O   . ASN B 2 117 ? -43.129 38.949  15.168  1.00 59.58  ? 117 ASN B O   1 
ATOM   3469  C CB  . ASN B 2 117 ? -40.360 38.041  16.605  1.00 35.28  ? 117 ASN B CB  1 
ATOM   3470  C CG  . ASN B 2 117 ? -39.919 36.956  17.571  1.00 46.36  ? 117 ASN B CG  1 
ATOM   3471  O OD1 . ASN B 2 117 ? -40.458 35.849  17.569  1.00 56.31  ? 117 ASN B OD1 1 
ATOM   3472  N ND2 . ASN B 2 117 ? -38.933 37.267  18.402  1.00 50.93  ? 117 ASN B ND2 1 
ATOM   3473  N N   . LEU B 2 118 ? -41.390 39.249  13.772  1.00 48.26  ? 118 LEU B N   1 
ATOM   3474  C CA  . LEU B 2 118 ? -42.101 40.263  12.999  1.00 41.66  ? 118 LEU B CA  1 
ATOM   3475  C C   . LEU B 2 118 ? -43.242 39.647  12.197  1.00 52.10  ? 118 LEU B C   1 
ATOM   3476  O O   . LEU B 2 118 ? -44.334 40.222  12.117  1.00 43.61  ? 118 LEU B O   1 
ATOM   3477  C CB  . LEU B 2 118 ? -41.128 40.991  12.077  1.00 40.91  ? 118 LEU B CB  1 
ATOM   3478  C CG  . LEU B 2 118 ? -41.636 42.298  11.473  1.00 55.35  ? 118 LEU B CG  1 
ATOM   3479  C CD1 . LEU B 2 118 ? -41.315 43.468  12.393  1.00 53.50  ? 118 LEU B CD1 1 
ATOM   3480  C CD2 . LEU B 2 118 ? -41.036 42.508  10.095  1.00 47.28  ? 118 LEU B CD2 1 
ATOM   3481  N N   . TYR B 2 119 ? -43.010 38.474  11.603  1.00 48.98  ? 119 TYR B N   1 
ATOM   3482  C CA  . TYR B 2 119 ? -44.069 37.789  10.869  1.00 45.48  ? 119 TYR B CA  1 
ATOM   3483  C C   . TYR B 2 119 ? -45.236 37.439  11.786  1.00 54.32  ? 119 TYR B C   1 
ATOM   3484  O O   . TYR B 2 119 ? -46.401 37.641  11.424  1.00 55.89  ? 119 TYR B O   1 
ATOM   3485  C CB  . TYR B 2 119 ? -43.504 36.535  10.207  1.00 44.00  ? 119 TYR B CB  1 
ATOM   3486  C CG  . TYR B 2 119 ? -44.524 35.673  9.503   1.00 52.14  ? 119 TYR B CG  1 
ATOM   3487  C CD1 . TYR B 2 119 ? -44.875 35.919  8.182   1.00 44.46  ? 119 TYR B CD1 1 
ATOM   3488  C CD2 . TYR B 2 119 ? -45.119 34.596  10.150  1.00 56.30  ? 119 TYR B CD2 1 
ATOM   3489  C CE1 . TYR B 2 119 ? -45.798 35.126  7.530   1.00 55.20  ? 119 TYR B CE1 1 
ATOM   3490  C CE2 . TYR B 2 119 ? -46.048 33.798  9.505   1.00 52.68  ? 119 TYR B CE2 1 
ATOM   3491  C CZ  . TYR B 2 119 ? -46.383 34.069  8.196   1.00 51.22  ? 119 TYR B CZ  1 
ATOM   3492  O OH  . TYR B 2 119 ? -47.302 33.281  7.548   1.00 50.62  ? 119 TYR B OH  1 
ATOM   3493  N N   . ASP B 2 120 ? -44.941 36.926  12.983  1.00 52.34  ? 120 ASP B N   1 
ATOM   3494  C CA  . ASP B 2 120 ? -46.005 36.571  13.917  1.00 62.07  ? 120 ASP B CA  1 
ATOM   3495  C C   . ASP B 2 120 ? -46.772 37.799  14.389  1.00 59.26  ? 120 ASP B C   1 
ATOM   3496  O O   . ASP B 2 120 ? -47.975 37.710  14.658  1.00 59.63  ? 120 ASP B O   1 
ATOM   3497  C CB  . ASP B 2 120 ? -45.425 35.812  15.113  1.00 43.58  ? 120 ASP B CB  1 
ATOM   3498  C CG  . ASP B 2 120 ? -45.060 34.377  14.774  1.00 58.59  ? 120 ASP B CG  1 
ATOM   3499  O OD1 . ASP B 2 120 ? -45.346 33.935  13.641  1.00 67.77  ? 120 ASP B OD1 1 
ATOM   3500  O OD2 . ASP B 2 120 ? -44.484 33.688  15.643  1.00 70.70  ? 120 ASP B OD2 1 
ATOM   3501  N N   . LYS B 2 121 ? -46.092 38.943  14.509  1.00 49.91  ? 121 LYS B N   1 
ATOM   3502  C CA  . LYS B 2 121 ? -46.766 40.171  14.914  1.00 49.24  ? 121 LYS B CA  1 
ATOM   3503  C C   . LYS B 2 121 ? -47.821 40.577  13.892  1.00 61.76  ? 121 LYS B C   1 
ATOM   3504  O O   . LYS B 2 121 ? -48.940 40.955  14.260  1.00 63.26  ? 121 LYS B O   1 
ATOM   3505  C CB  . LYS B 2 121 ? -45.734 41.285  15.108  1.00 49.53  ? 121 LYS B CB  1 
ATOM   3506  C CG  . LYS B 2 121 ? -46.173 42.432  16.015  1.00 48.97  ? 121 LYS B CG  1 
ATOM   3507  C CD  . LYS B 2 121 ? -47.039 43.453  15.273  1.00 75.53  ? 121 LYS B CD  1 
ATOM   3508  C CE  . LYS B 2 121 ? -48.006 44.146  16.220  1.00 69.24  ? 121 LYS B CE  1 
ATOM   3509  N NZ  . LYS B 2 121 ? -49.190 43.285  16.509  1.00 75.62  ? 121 LYS B NZ  1 
ATOM   3510  N N   . VAL B 2 122 ? -47.483 40.504  12.603  1.00 52.90  ? 122 VAL B N   1 
ATOM   3511  C CA  . VAL B 2 122 ? -48.447 40.840  11.560  1.00 50.97  ? 122 VAL B CA  1 
ATOM   3512  C C   . VAL B 2 122 ? -49.612 39.862  11.574  1.00 60.53  ? 122 VAL B C   1 
ATOM   3513  O O   . VAL B 2 122 ? -50.781 40.259  11.493  1.00 63.22  ? 122 VAL B O   1 
ATOM   3514  C CB  . VAL B 2 122 ? -47.756 40.867  10.186  1.00 46.15  ? 122 VAL B CB  1 
ATOM   3515  C CG1 . VAL B 2 122 ? -48.774 41.148  9.087   1.00 49.69  ? 122 VAL B CG1 1 
ATOM   3516  C CG2 . VAL B 2 122 ? -46.651 41.903  10.182  1.00 58.25  ? 122 VAL B CG2 1 
ATOM   3517  N N   . ARG B 2 123 ? -49.310 38.566  11.683  1.00 54.92  ? 123 ARG B N   1 
ATOM   3518  C CA  . ARG B 2 123 ? -50.354 37.550  11.688  1.00 52.39  ? 123 ARG B CA  1 
ATOM   3519  C C   . ARG B 2 123 ? -51.311 37.734  12.859  1.00 67.54  ? 123 ARG B C   1 
ATOM   3520  O O   . ARG B 2 123 ? -52.500 37.415  12.743  1.00 62.27  ? 123 ARG B O   1 
ATOM   3521  C CB  . ARG B 2 123 ? -49.709 36.164  11.723  1.00 53.63  ? 123 ARG B CB  1 
ATOM   3522  C CG  . ARG B 2 123 ? -50.681 35.005  11.747  1.00 62.75  ? 123 ARG B CG  1 
ATOM   3523  C CD  . ARG B 2 123 ? -50.005 33.755  12.282  1.00 69.23  ? 123 ARG B CD  1 
ATOM   3524  N NE  . ARG B 2 123 ? -49.961 33.749  13.739  1.00 70.66  ? 123 ARG B NE  1 
ATOM   3525  C CZ  . ARG B 2 123 ? -48.999 33.187  14.455  1.00 67.59  ? 123 ARG B CZ  1 
ATOM   3526  N NH1 . ARG B 2 123 ? -47.986 32.560  13.877  1.00 84.85  ? 123 ARG B NH1 1 
ATOM   3527  N NH2 . ARG B 2 123 ? -49.053 33.256  15.782  1.00 75.73  ? 123 ARG B NH2 1 
ATOM   3528  N N   . LEU B 2 124 ? -50.818 38.258  13.986  1.00 60.56  ? 124 LEU B N   1 
ATOM   3529  C CA  . LEU B 2 124 ? -51.681 38.485  15.144  1.00 67.94  ? 124 LEU B CA  1 
ATOM   3530  C C   . LEU B 2 124 ? -52.729 39.559  14.867  1.00 69.58  ? 124 LEU B C   1 
ATOM   3531  O O   . LEU B 2 124 ? -53.886 39.424  15.282  1.00 67.73  ? 124 LEU B O   1 
ATOM   3532  C CB  . LEU B 2 124 ? -50.840 38.862  16.363  1.00 65.82  ? 124 LEU B CB  1 
ATOM   3533  C CG  . LEU B 2 124 ? -50.648 37.778  17.427  1.00 74.62  ? 124 LEU B CG  1 
ATOM   3534  C CD1 . LEU B 2 124 ? -50.279 36.443  16.785  1.00 73.54  ? 124 LEU B CD1 1 
ATOM   3535  C CD2 . LEU B 2 124 ? -49.594 38.206  18.445  1.00 67.81  ? 124 LEU B CD2 1 
ATOM   3536  N N   . GLN B 2 125 ? -52.345 40.646  14.194  1.00 60.08  ? 125 GLN B N   1 
ATOM   3537  C CA  . GLN B 2 125 ? -53.324 41.681  13.875  1.00 64.54  ? 125 GLN B CA  1 
ATOM   3538  C C   . GLN B 2 125 ? -54.301 41.204  12.809  1.00 66.44  ? 125 GLN B C   1 
ATOM   3539  O O   . GLN B 2 125 ? -55.518 41.379  12.945  1.00 78.00  ? 125 GLN B O   1 
ATOM   3540  C CB  . GLN B 2 125 ? -52.626 42.962  13.416  1.00 67.21  ? 125 GLN B CB  1 
ATOM   3541  C CG  . GLN B 2 125 ? -51.187 43.096  13.836  1.00 64.37  ? 125 GLN B CG  1 
ATOM   3542  C CD  . GLN B 2 125 ? -50.569 44.377  13.324  1.00 75.01  ? 125 GLN B CD  1 
ATOM   3543  O OE1 . GLN B 2 125 ? -51.191 45.439  13.371  1.00 76.82  ? 125 GLN B OE1 1 
ATOM   3544  N NE2 . GLN B 2 125 ? -49.347 44.281  12.806  1.00 70.87  ? 125 GLN B NE2 1 
ATOM   3545  N N   . LEU B 2 126 ? -53.785 40.599  11.736  1.00 60.03  ? 126 LEU B N   1 
ATOM   3546  C CA  . LEU B 2 126 ? -54.644 40.213  10.620  1.00 53.22  ? 126 LEU B CA  1 
ATOM   3547  C C   . LEU B 2 126 ? -55.644 39.141  11.033  1.00 66.56  ? 126 LEU B C   1 
ATOM   3548  O O   . LEU B 2 126 ? -56.826 39.218  10.675  1.00 75.76  ? 126 LEU B O   1 
ATOM   3549  C CB  . LEU B 2 126 ? -53.795 39.731  9.442   1.00 44.75  ? 126 LEU B CB  1 
ATOM   3550  C CG  . LEU B 2 126 ? -52.857 40.765  8.808   1.00 50.34  ? 126 LEU B CG  1 
ATOM   3551  C CD1 . LEU B 2 126 ? -52.558 40.409  7.367   1.00 37.97  ? 126 LEU B CD1 1 
ATOM   3552  C CD2 . LEU B 2 126 ? -53.427 42.175  8.894   1.00 58.82  ? 126 LEU B CD2 1 
ATOM   3553  N N   . ARG B 2 127 ? -55.191 38.144  11.793  1.00 67.63  ? 127 ARG B N   1 
ATOM   3554  C CA  . ARG B 2 127 ? -56.026 37.018  12.195  1.00 59.84  ? 127 ARG B CA  1 
ATOM   3555  C C   . ARG B 2 127 ? -56.745 36.437  10.985  1.00 58.45  ? 127 ARG B C   1 
ATOM   3556  O O   . ARG B 2 127 ? -56.143 36.288  9.917   1.00 68.01  ? 127 ARG B O   1 
ATOM   3557  C CB  . ARG B 2 127 ? -57.018 37.444  13.282  1.00 65.06  ? 127 ARG B CB  1 
ATOM   3558  C CG  . ARG B 2 127 ? -56.406 37.467  14.679  1.00 62.41  ? 127 ARG B CG  1 
ATOM   3559  C CD  . ARG B 2 127 ? -57.359 38.026  15.731  1.00 80.81  ? 127 ARG B CD  1 
ATOM   3560  N NE  . ARG B 2 127 ? -58.694 37.448  15.640  1.00 92.01  ? 127 ARG B NE  1 
ATOM   3561  C CZ  . ARG B 2 127 ? -59.815 38.109  15.897  1.00 90.95  ? 127 ARG B CZ  1 
ATOM   3562  N NH1 . ARG B 2 127 ? -59.798 39.376  16.277  1.00 85.05  ? 127 ARG B NH1 1 
ATOM   3563  N NH2 . ARG B 2 127 ? -60.983 37.483  15.770  1.00 81.37  ? 127 ARG B NH2 1 
ATOM   3564  N N   . ASP B 2 128 ? -58.037 36.135  11.126  1.00 67.58  ? 128 ASP B N   1 
ATOM   3565  C CA  . ASP B 2 128 ? -58.782 35.517  10.033  1.00 71.59  ? 128 ASP B CA  1 
ATOM   3566  C C   . ASP B 2 128 ? -59.076 36.480  8.884   1.00 75.79  ? 128 ASP B C   1 
ATOM   3567  O O   . ASP B 2 128 ? -59.537 36.031  7.828   1.00 69.13  ? 128 ASP B O   1 
ATOM   3568  C CB  . ASP B 2 128 ? -60.085 34.915  10.566  1.00 66.60  ? 128 ASP B CB  1 
ATOM   3569  C CG  . ASP B 2 128 ? -61.165 35.956  10.780  1.00 73.48  ? 128 ASP B CG  1 
ATOM   3570  O OD1 . ASP B 2 128 ? -60.870 37.006  11.388  1.00 70.62  ? 128 ASP B OD1 1 
ATOM   3571  O OD2 . ASP B 2 128 ? -62.312 35.719  10.342  1.00 87.97  ? 128 ASP B OD2 1 
ATOM   3572  N N   . ASN B 2 129 ? -58.809 37.778  9.049   1.00 67.51  ? 129 ASN B N   1 
ATOM   3573  C CA  . ASN B 2 129 ? -59.060 38.759  7.996   1.00 65.00  ? 129 ASN B CA  1 
ATOM   3574  C C   . ASN B 2 129 ? -58.113 38.624  6.808   1.00 64.16  ? 129 ASN B C   1 
ATOM   3575  O O   . ASN B 2 129 ? -58.202 39.426  5.872   1.00 57.23  ? 129 ASN B O   1 
ATOM   3576  C CB  . ASN B 2 129 ? -58.958 40.175  8.565   1.00 69.06  ? 129 ASN B CB  1 
ATOM   3577  C CG  . ASN B 2 129 ? -60.305 40.763  8.904   1.00 68.08  ? 129 ASN B CG  1 
ATOM   3578  O OD1 . ASN B 2 129 ? -61.335 40.103  8.762   1.00 73.87  ? 129 ASN B OD1 1 
ATOM   3579  N ND2 . ASN B 2 129 ? -60.308 42.011  9.363   1.00 62.28  ? 129 ASN B ND2 1 
ATOM   3580  N N   . ALA B 2 130 ? -57.208 37.652  6.820   1.00 64.06  ? 130 ALA B N   1 
ATOM   3581  C CA  . ALA B 2 130 ? -56.289 37.446  5.710   1.00 64.59  ? 130 ALA B CA  1 
ATOM   3582  C C   . ALA B 2 130 ? -55.809 36.005  5.752   1.00 54.78  ? 130 ALA B C   1 
ATOM   3583  O O   . ALA B 2 130 ? -55.959 35.307  6.758   1.00 57.10  ? 130 ALA B O   1 
ATOM   3584  C CB  . ALA B 2 130 ? -55.108 38.421  5.763   1.00 61.27  ? 130 ALA B CB  1 
ATOM   3585  N N   . LYS B 2 131 ? -55.219 35.573  4.645   1.00 52.58  ? 131 LYS B N   1 
ATOM   3586  C CA  . LYS B 2 131 ? -54.771 34.200  4.466   1.00 49.71  ? 131 LYS B CA  1 
ATOM   3587  C C   . LYS B 2 131 ? -53.249 34.158  4.420   1.00 63.97  ? 131 LYS B C   1 
ATOM   3588  O O   . LYS B 2 131 ? -52.628 34.905  3.656   1.00 67.67  ? 131 LYS B O   1 
ATOM   3589  C CB  . LYS B 2 131 ? -55.358 33.619  3.181   1.00 51.02  ? 131 LYS B CB  1 
ATOM   3590  C CG  . LYS B 2 131 ? -54.466 32.627  2.456   1.00 56.77  ? 131 LYS B CG  1 
ATOM   3591  C CD  . LYS B 2 131 ? -55.177 32.077  1.224   1.00 54.52  ? 131 LYS B CD  1 
ATOM   3592  C CE  . LYS B 2 131 ? -54.567 30.757  0.776   1.00 62.09  ? 131 LYS B CE  1 
ATOM   3593  N NZ  . LYS B 2 131 ? -54.248 30.723  -0.678  1.00 54.59  ? 131 LYS B NZ  1 
ATOM   3594  N N   . GLU B 2 132 ? -52.650 33.295  5.241   1.00 57.82  ? 132 GLU B N   1 
ATOM   3595  C CA  . GLU B 2 132 ? -51.210 33.073  5.173   1.00 60.21  ? 132 GLU B CA  1 
ATOM   3596  C C   . GLU B 2 132 ? -50.885 32.221  3.954   1.00 54.43  ? 132 GLU B C   1 
ATOM   3597  O O   . GLU B 2 132 ? -51.499 31.172  3.739   1.00 67.80  ? 132 GLU B O   1 
ATOM   3598  C CB  . GLU B 2 132 ? -50.699 32.388  6.440   1.00 46.14  ? 132 GLU B CB  1 
ATOM   3599  C CG  . GLU B 2 132 ? -51.055 33.095  7.729   1.00 58.89  ? 132 GLU B CG  1 
ATOM   3600  C CD  . GLU B 2 132 ? -50.552 32.351  8.951   1.00 67.10  ? 132 GLU B CD  1 
ATOM   3601  O OE1 . GLU B 2 132 ? -49.360 31.976  8.974   1.00 63.17  ? 132 GLU B OE1 1 
ATOM   3602  O OE2 . GLU B 2 132 ? -51.354 32.132  9.885   1.00 76.32  ? 132 GLU B OE2 1 
ATOM   3603  N N   . LEU B 2 133 ? -49.916 32.669  3.158   1.00 58.39  ? 133 LEU B N   1 
ATOM   3604  C CA  . LEU B 2 133 ? -49.524 31.949  1.953   1.00 57.66  ? 133 LEU B CA  1 
ATOM   3605  C C   . LEU B 2 133 ? -48.437 30.917  2.196   1.00 47.22  ? 133 LEU B C   1 
ATOM   3606  O O   . LEU B 2 133 ? -48.134 30.138  1.285   1.00 53.70  ? 133 LEU B O   1 
ATOM   3607  C CB  . LEU B 2 133 ? -49.048 32.932  0.876   1.00 53.82  ? 133 LEU B CB  1 
ATOM   3608  C CG  . LEU B 2 133 ? -50.079 33.303  -0.189  1.00 65.00  ? 133 LEU B CG  1 
ATOM   3609  C CD1 . LEU B 2 133 ? -51.403 33.668  0.458   1.00 61.55  ? 133 LEU B CD1 1 
ATOM   3610  C CD2 . LEU B 2 133 ? -49.571 34.441  -1.056  1.00 57.83  ? 133 LEU B CD2 1 
ATOM   3611  N N   . GLY B 2 134 ? -47.840 30.898  3.386   1.00 58.98  ? 134 GLY B N   1 
ATOM   3612  C CA  . GLY B 2 134 ? -46.757 29.990  3.695   1.00 43.08  ? 134 GLY B CA  1 
ATOM   3613  C C   . GLY B 2 134 ? -45.389 30.433  3.221   1.00 57.81  ? 134 GLY B C   1 
ATOM   3614  O O   . GLY B 2 134 ? -44.401 29.741  3.501   1.00 55.31  ? 134 GLY B O   1 
ATOM   3615  N N   . ASN B 2 135 ? -45.293 31.564  2.519   1.00 47.33  ? 135 ASN B N   1 
ATOM   3616  C CA  . ASN B 2 135 ? -44.016 32.065  2.024   1.00 52.98  ? 135 ASN B CA  1 
ATOM   3617  C C   . ASN B 2 135 ? -43.647 33.410  2.645   1.00 53.69  ? 135 ASN B C   1 
ATOM   3618  O O   . ASN B 2 135 ? -42.838 34.150  2.076   1.00 45.62  ? 135 ASN B O   1 
ATOM   3619  C CB  . ASN B 2 135 ? -44.037 32.170  0.498   1.00 43.44  ? 135 ASN B CB  1 
ATOM   3620  C CG  . ASN B 2 135 ? -44.995 33.232  0.005   1.00 53.29  ? 135 ASN B CG  1 
ATOM   3621  O OD1 . ASN B 2 135 ? -45.912 33.635  0.720   1.00 57.80  ? 135 ASN B OD1 1 
ATOM   3622  N ND2 . ASN B 2 135 ? -44.786 33.696  -1.221  1.00 60.97  ? 135 ASN B ND2 1 
ATOM   3623  N N   . GLY B 2 136 ? -44.214 33.736  3.804   1.00 59.19  ? 136 GLY B N   1 
ATOM   3624  C CA  . GLY B 2 136 ? -43.989 35.014  4.442   1.00 48.36  ? 136 GLY B CA  1 
ATOM   3625  C C   . GLY B 2 136 ? -44.952 36.106  4.036   1.00 53.77  ? 136 GLY B C   1 
ATOM   3626  O O   . GLY B 2 136 ? -44.820 37.238  4.519   1.00 54.93  ? 136 GLY B O   1 
ATOM   3627  N N   . CYS B 2 137 ? -45.916 35.805  3.172   1.00 53.25  ? 137 CYS B N   1 
ATOM   3628  C CA  . CYS B 2 137 ? -46.873 36.779  2.675   1.00 55.77  ? 137 CYS B CA  1 
ATOM   3629  C C   . CYS B 2 137 ? -48.266 36.484  3.216   1.00 53.04  ? 137 CYS B C   1 
ATOM   3630  O O   . CYS B 2 137 ? -48.588 35.353  3.587   1.00 59.99  ? 137 CYS B O   1 
ATOM   3631  C CB  . CYS B 2 137 ? -46.898 36.781  1.144   1.00 49.59  ? 137 CYS B CB  1 
ATOM   3632  S SG  . CYS B 2 137 ? -45.340 37.312  0.407   1.00 69.80  ? 137 CYS B SG  1 
ATOM   3633  N N   . PHE B 2 138 ? -49.085 37.532  3.270   1.00 54.42  ? 138 PHE B N   1 
ATOM   3634  C CA  . PHE B 2 138 ? -50.486 37.441  3.662   1.00 52.77  ? 138 PHE B CA  1 
ATOM   3635  C C   . PHE B 2 138 ? -51.337 37.990  2.527   1.00 56.91  ? 138 PHE B C   1 
ATOM   3636  O O   . PHE B 2 138 ? -51.187 39.157  2.148   1.00 49.41  ? 138 PHE B O   1 
ATOM   3637  C CB  . PHE B 2 138 ? -50.763 38.228  4.944   1.00 46.59  ? 138 PHE B CB  1 
ATOM   3638  C CG  . PHE B 2 138 ? -50.026 37.722  6.142   1.00 56.02  ? 138 PHE B CG  1 
ATOM   3639  C CD1 . PHE B 2 138 ? -48.734 38.144  6.406   1.00 60.57  ? 138 PHE B CD1 1 
ATOM   3640  C CD2 . PHE B 2 138 ? -50.630 36.837  7.018   1.00 52.83  ? 138 PHE B CD2 1 
ATOM   3641  C CE1 . PHE B 2 138 ? -48.055 37.686  7.512   1.00 54.91  ? 138 PHE B CE1 1 
ATOM   3642  C CE2 . PHE B 2 138 ? -49.956 36.373  8.128   1.00 54.63  ? 138 PHE B CE2 1 
ATOM   3643  C CZ  . PHE B 2 138 ? -48.666 36.797  8.376   1.00 61.40  ? 138 PHE B CZ  1 
ATOM   3644  N N   . GLU B 2 139 ? -52.234 37.161  2.000   1.00 53.21  ? 139 GLU B N   1 
ATOM   3645  C CA  . GLU B 2 139 ? -53.177 37.593  0.975   1.00 48.68  ? 139 GLU B CA  1 
ATOM   3646  C C   . GLU B 2 139 ? -54.436 38.092  1.670   1.00 59.45  ? 139 GLU B C   1 
ATOM   3647  O O   . GLU B 2 139 ? -55.150 37.317  2.315   1.00 62.80  ? 139 GLU B O   1 
ATOM   3648  C CB  . GLU B 2 139 ? -53.495 36.459  0.004   1.00 61.36  ? 139 GLU B CB  1 
ATOM   3649  C CG  . GLU B 2 139 ? -54.076 36.921  -1.327  1.00 73.94  ? 139 GLU B CG  1 
ATOM   3650  C CD  . GLU B 2 139 ? -54.652 35.778  -2.146  1.00 79.21  ? 139 GLU B CD  1 
ATOM   3651  O OE1 . GLU B 2 139 ? -55.622 35.139  -1.684  1.00 83.77  ? 139 GLU B OE1 1 
ATOM   3652  O OE2 . GLU B 2 139 ? -54.134 35.519  -3.253  1.00 87.75  ? 139 GLU B OE2 1 
ATOM   3653  N N   . PHE B 2 140 ? -54.703 39.386  1.542   1.00 58.93  ? 140 PHE B N   1 
ATOM   3654  C CA  . PHE B 2 140 ? -55.867 39.985  2.169   1.00 59.36  ? 140 PHE B CA  1 
ATOM   3655  C C   . PHE B 2 140 ? -57.154 39.502  1.504   1.00 68.45  ? 140 PHE B C   1 
ATOM   3656  O O   . PHE B 2 140 ? -57.159 38.989  0.381   1.00 71.04  ? 140 PHE B O   1 
ATOM   3657  C CB  . PHE B 2 140 ? -55.795 41.507  2.083   1.00 52.83  ? 140 PHE B CB  1 
ATOM   3658  C CG  . PHE B 2 140 ? -54.907 42.133  3.113   1.00 68.92  ? 140 PHE B CG  1 
ATOM   3659  C CD1 . PHE B 2 140 ? -55.382 42.391  4.387   1.00 55.14  ? 140 PHE B CD1 1 
ATOM   3660  C CD2 . PHE B 2 140 ? -53.598 42.476  2.805   1.00 64.04  ? 140 PHE B CD2 1 
ATOM   3661  C CE1 . PHE B 2 140 ? -54.569 42.974  5.340   1.00 60.15  ? 140 PHE B CE1 1 
ATOM   3662  C CE2 . PHE B 2 140 ? -52.781 43.061  3.753   1.00 54.61  ? 140 PHE B CE2 1 
ATOM   3663  C CZ  . PHE B 2 140 ? -53.268 43.311  5.023   1.00 46.40  ? 140 PHE B CZ  1 
ATOM   3664  N N   . TYR B 2 141 ? -58.260 39.671  2.226   1.00 65.24  ? 141 TYR B N   1 
ATOM   3665  C CA  . TYR B 2 141 ? -59.592 39.506  1.667   1.00 68.25  ? 141 TYR B CA  1 
ATOM   3666  C C   . TYR B 2 141 ? -60.358 40.816  1.552   1.00 70.73  ? 141 TYR B C   1 
ATOM   3667  O O   . TYR B 2 141 ? -61.462 40.816  0.997   1.00 79.56  ? 141 TYR B O   1 
ATOM   3668  C CB  . TYR B 2 141 ? -60.430 38.544  2.523   1.00 69.21  ? 141 TYR B CB  1 
ATOM   3669  C CG  . TYR B 2 141 ? -59.909 37.135  2.642   1.00 62.52  ? 141 TYR B CG  1 
ATOM   3670  C CD1 . TYR B 2 141 ? -59.588 36.389  1.516   1.00 69.26  ? 141 TYR B CD1 1 
ATOM   3671  C CD2 . TYR B 2 141 ? -59.768 36.538  3.887   1.00 71.85  ? 141 TYR B CD2 1 
ATOM   3672  C CE1 . TYR B 2 141 ? -59.122 35.090  1.630   1.00 58.15  ? 141 TYR B CE1 1 
ATOM   3673  C CE2 . TYR B 2 141 ? -59.302 35.243  4.013   1.00 62.52  ? 141 TYR B CE2 1 
ATOM   3674  C CZ  . TYR B 2 141 ? -58.982 34.523  2.883   1.00 54.18  ? 141 TYR B CZ  1 
ATOM   3675  O OH  . TYR B 2 141 ? -58.524 33.232  3.013   1.00 51.02  ? 141 TYR B OH  1 
ATOM   3676  N N   . HIS B 2 142 ? -59.818 41.925  2.064   1.00 75.46  ? 142 HIS B N   1 
ATOM   3677  C CA  . HIS B 2 142 ? -60.631 43.108  2.318   1.00 66.58  ? 142 HIS B CA  1 
ATOM   3678  C C   . HIS B 2 142 ? -60.031 44.378  1.729   1.00 82.66  ? 142 HIS B C   1 
ATOM   3679  O O   . HIS B 2 142 ? -60.251 45.467  2.264   1.00 94.63  ? 142 HIS B O   1 
ATOM   3680  C CB  . HIS B 2 142 ? -60.868 43.285  3.817   1.00 69.50  ? 142 HIS B CB  1 
ATOM   3681  C CG  . HIS B 2 142 ? -59.639 43.652  4.588   1.00 69.30  ? 142 HIS B CG  1 
ATOM   3682  N ND1 . HIS B 2 142 ? -59.081 44.912  4.546   1.00 72.12  ? 142 HIS B ND1 1 
ATOM   3683  C CD2 . HIS B 2 142 ? -58.866 42.927  5.429   1.00 63.77  ? 142 HIS B CD2 1 
ATOM   3684  C CE1 . HIS B 2 142 ? -58.013 44.946  5.322   1.00 66.29  ? 142 HIS B CE1 1 
ATOM   3685  N NE2 . HIS B 2 142 ? -57.863 43.755  5.873   1.00 75.35  ? 142 HIS B NE2 1 
ATOM   3686  N N   . LYS B 2 143 ? -59.276 44.265  0.633   1.00 73.32  ? 143 LYS B N   1 
ATOM   3687  C CA  . LYS B 2 143 ? -58.887 45.427  -0.171  1.00 77.69  ? 143 LYS B CA  1 
ATOM   3688  C C   . LYS B 2 143 ? -58.141 46.463  0.678   1.00 62.38  ? 143 LYS B C   1 
ATOM   3689  O O   . LYS B 2 143 ? -58.626 47.561  0.956   1.00 75.22  ? 143 LYS B O   1 
ATOM   3690  C CB  . LYS B 2 143 ? -60.115 46.056  -0.841  1.00 76.15  ? 143 LYS B CB  1 
ATOM   3691  C CG  . LYS B 2 143 ? -59.832 46.713  -2.181  1.00 83.11  ? 143 LYS B CG  1 
ATOM   3692  C CD  . LYS B 2 143 ? -59.722 45.681  -3.291  1.00 72.33  ? 143 LYS B CD  1 
ATOM   3693  C CE  . LYS B 2 143 ? -61.082 45.110  -3.644  1.00 80.39  ? 143 LYS B CE  1 
ATOM   3694  N NZ  . LYS B 2 143 ? -61.917 46.094  -4.387  1.00 86.62  ? 143 LYS B NZ  1 
ATOM   3695  N N   . CYS B 2 144 ? -56.952 46.064  1.109   1.00 63.80  ? 144 CYS B N   1 
ATOM   3696  C CA  . CYS B 2 144 ? -56.146 46.902  1.984   1.00 67.26  ? 144 CYS B CA  1 
ATOM   3697  C C   . CYS B 2 144 ? -55.467 47.992  1.156   1.00 61.29  ? 144 CYS B C   1 
ATOM   3698  O O   . CYS B 2 144 ? -54.685 47.693  0.248   1.00 66.71  ? 144 CYS B O   1 
ATOM   3699  C CB  . CYS B 2 144 ? -55.130 46.035  2.724   1.00 57.29  ? 144 CYS B CB  1 
ATOM   3700  S SG  . CYS B 2 144 ? -54.230 46.838  4.063   1.00 71.49  ? 144 CYS B SG  1 
ATOM   3701  N N   . ASP B 2 145 ? -55.778 49.254  1.456   1.00 66.25  ? 145 ASP B N   1 
ATOM   3702  C CA  . ASP B 2 145 ? -55.189 50.386  0.755   1.00 63.85  ? 145 ASP B CA  1 
ATOM   3703  C C   . ASP B 2 145 ? -53.898 50.821  1.448   1.00 58.29  ? 145 ASP B C   1 
ATOM   3704  O O   . ASP B 2 145 ? -53.438 50.200  2.408   1.00 65.50  ? 145 ASP B O   1 
ATOM   3705  C CB  . ASP B 2 145 ? -56.188 51.542  0.664   1.00 54.36  ? 145 ASP B CB  1 
ATOM   3706  C CG  . ASP B 2 145 ? -56.936 51.775  1.966   1.00 75.72  ? 145 ASP B CG  1 
ATOM   3707  O OD1 . ASP B 2 145 ? -57.831 50.964  2.298   1.00 77.05  ? 145 ASP B OD1 1 
ATOM   3708  O OD2 . ASP B 2 145 ? -56.627 52.769  2.657   1.00 79.38  ? 145 ASP B OD2 1 
ATOM   3709  N N   . ASN B 2 146 ? -53.307 51.915  0.960   1.00 61.62  ? 146 ASN B N   1 
ATOM   3710  C CA  . ASN B 2 146 ? -51.996 52.336  1.450   1.00 53.97  ? 146 ASN B CA  1 
ATOM   3711  C C   . ASN B 2 146 ? -52.038 52.712  2.926   1.00 65.98  ? 146 ASN B C   1 
ATOM   3712  O O   . ASN B 2 146 ? -51.097 52.419  3.675   1.00 68.21  ? 146 ASN B O   1 
ATOM   3713  C CB  . ASN B 2 146 ? -51.472 53.502  0.613   1.00 55.74  ? 146 ASN B CB  1 
ATOM   3714  C CG  . ASN B 2 146 ? -50.725 53.036  -0.618  1.00 56.29  ? 146 ASN B CG  1 
ATOM   3715  O OD1 . ASN B 2 146 ? -50.373 51.862  -0.733  1.00 58.71  ? 146 ASN B OD1 1 
ATOM   3716  N ND2 . ASN B 2 146 ? -50.477 53.954  -1.548  1.00 57.20  ? 146 ASN B ND2 1 
ATOM   3717  N N   . GLU B 2 147 ? -53.111 53.370  3.364   1.00 73.16  ? 147 GLU B N   1 
ATOM   3718  C CA  . GLU B 2 147 ? -53.238 53.702  4.779   1.00 76.43  ? 147 GLU B CA  1 
ATOM   3719  C C   . GLU B 2 147 ? -53.558 52.465  5.607   1.00 66.00  ? 147 GLU B C   1 
ATOM   3720  O O   . GLU B 2 147 ? -53.107 52.342  6.752   1.00 63.09  ? 147 GLU B O   1 
ATOM   3721  C CB  . GLU B 2 147 ? -54.300 54.785  4.964   1.00 74.77  ? 147 GLU B CB  1 
ATOM   3722  C CG  . GLU B 2 147 ? -54.291 55.884  3.891   1.00 83.15  ? 147 GLU B CG  1 
ATOM   3723  C CD  . GLU B 2 147 ? -53.013 56.725  3.863   1.00 108.81 ? 147 GLU B CD  1 
ATOM   3724  O OE1 . GLU B 2 147 ? -51.898 56.168  3.737   1.00 111.19 ? 147 GLU B OE1 1 
ATOM   3725  O OE2 . GLU B 2 147 ? -53.130 57.964  3.970   1.00 115.63 ? 147 GLU B OE2 1 
ATOM   3726  N N   . CYS B 2 148 ? -54.340 51.544  5.042   1.00 59.35  ? 148 CYS B N   1 
ATOM   3727  C CA  . CYS B 2 148 ? -54.539 50.242  5.667   1.00 59.69  ? 148 CYS B CA  1 
ATOM   3728  C C   . CYS B 2 148 ? -53.219 49.499  5.830   1.00 61.86  ? 148 CYS B C   1 
ATOM   3729  O O   . CYS B 2 148 ? -52.943 48.930  6.894   1.00 67.93  ? 148 CYS B O   1 
ATOM   3730  C CB  . CYS B 2 148 ? -55.528 49.424  4.832   1.00 65.60  ? 148 CYS B CB  1 
ATOM   3731  S SG  . CYS B 2 148 ? -55.662 47.674  5.254   1.00 76.52  ? 148 CYS B SG  1 
ATOM   3732  N N   . MET B 2 149 ? -52.384 49.501  4.788   1.00 62.18  ? 149 MET B N   1 
ATOM   3733  C CA  . MET B 2 149 ? -51.086 48.840  4.882   1.00 64.56  ? 149 MET B CA  1 
ATOM   3734  C C   . MET B 2 149 ? -50.218 49.491  5.949   1.00 66.31  ? 149 MET B C   1 
ATOM   3735  O O   . MET B 2 149 ? -49.523 48.798  6.704   1.00 64.99  ? 149 MET B O   1 
ATOM   3736  C CB  . MET B 2 149 ? -50.378 48.867  3.527   1.00 55.85  ? 149 MET B CB  1 
ATOM   3737  C CG  . MET B 2 149 ? -51.092 48.088  2.442   1.00 56.13  ? 149 MET B CG  1 
ATOM   3738  S SD  . MET B 2 149 ? -50.722 46.328  2.510   1.00 63.54  ? 149 MET B SD  1 
ATOM   3739  C CE  . MET B 2 149 ? -51.480 45.742  0.994   1.00 49.61  ? 149 MET B CE  1 
ATOM   3740  N N   . GLU B 2 150 ? -50.245 50.823  6.028   1.00 56.36  ? 150 GLU B N   1 
ATOM   3741  C CA  . GLU B 2 150 ? -49.483 51.518  7.060   1.00 62.69  ? 150 GLU B CA  1 
ATOM   3742  C C   . GLU B 2 150 ? -49.937 51.098  8.450   1.00 65.75  ? 150 GLU B C   1 
ATOM   3743  O O   . GLU B 2 150 ? -49.119 50.994  9.369   1.00 75.65  ? 150 GLU B O   1 
ATOM   3744  C CB  . GLU B 2 150 ? -49.615 53.030  6.886   1.00 76.41  ? 150 GLU B CB  1 
ATOM   3745  C CG  . GLU B 2 150 ? -49.000 53.848  8.013   1.00 76.98  ? 150 GLU B CG  1 
ATOM   3746  C CD  . GLU B 2 150 ? -47.489 53.935  7.914   1.00 84.95  ? 150 GLU B CD  1 
ATOM   3747  O OE1 . GLU B 2 150 ? -46.962 53.804  6.789   1.00 82.38  ? 150 GLU B OE1 1 
ATOM   3748  O OE2 . GLU B 2 150 ? -46.830 54.141  8.958   1.00 79.53  ? 150 GLU B OE2 1 
ATOM   3749  N N   . SER B 2 151 ? -51.236 50.843  8.619   1.00 64.27  ? 151 SER B N   1 
ATOM   3750  C CA  . SER B 2 151 ? -51.747 50.445  9.925   1.00 68.05  ? 151 SER B CA  1 
ATOM   3751  C C   . SER B 2 151 ? -51.199 49.090  10.352  1.00 66.80  ? 151 SER B C   1 
ATOM   3752  O O   . SER B 2 151 ? -50.989 48.856  11.547  1.00 74.93  ? 151 SER B O   1 
ATOM   3753  C CB  . SER B 2 151 ? -53.277 50.429  9.902   1.00 61.33  ? 151 SER B CB  1 
ATOM   3754  O OG  . SER B 2 151 ? -53.772 49.208  9.383   1.00 65.54  ? 151 SER B OG  1 
ATOM   3755  N N   . VAL B 2 152 ? -50.971 48.184  9.398   1.00 61.41  ? 152 VAL B N   1 
ATOM   3756  C CA  . VAL B 2 152 ? -50.397 46.881  9.725   1.00 65.59  ? 152 VAL B CA  1 
ATOM   3757  C C   . VAL B 2 152 ? -48.940 47.029  10.154  1.00 71.96  ? 152 VAL B C   1 
ATOM   3758  O O   . VAL B 2 152 ? -48.505 46.445  11.154  1.00 67.57  ? 152 VAL B O   1 
ATOM   3759  C CB  . VAL B 2 152 ? -50.536 45.920  8.532   1.00 66.47  ? 152 VAL B CB  1 
ATOM   3760  C CG1 . VAL B 2 152 ? -49.701 44.665  8.764   1.00 65.03  ? 152 VAL B CG1 1 
ATOM   3761  C CG2 . VAL B 2 152 ? -51.996 45.571  8.299   1.00 53.91  ? 152 VAL B CG2 1 
ATOM   3762  N N   . ARG B 2 153 ? -48.161 47.804  9.395   1.00 61.40  ? 153 ARG B N   1 
ATOM   3763  C CA  . ARG B 2 153 ? -46.775 48.056  9.775   1.00 60.52  ? 153 ARG B CA  1 
ATOM   3764  C C   . ARG B 2 153 ? -46.701 48.869  11.062  1.00 71.48  ? 153 ARG B C   1 
ATOM   3765  O O   . ARG B 2 153 ? -45.822 48.637  11.900  1.00 75.41  ? 153 ARG B O   1 
ATOM   3766  C CB  . ARG B 2 153 ? -46.044 48.768  8.636   1.00 52.82  ? 153 ARG B CB  1 
ATOM   3767  C CG  . ARG B 2 153 ? -46.125 48.029  7.305   1.00 52.03  ? 153 ARG B CG  1 
ATOM   3768  C CD  . ARG B 2 153 ? -45.445 48.804  6.181   1.00 46.58  ? 153 ARG B CD  1 
ATOM   3769  N NE  . ARG B 2 153 ? -45.994 50.145  6.024   1.00 50.17  ? 153 ARG B NE  1 
ATOM   3770  C CZ  . ARG B 2 153 ? -46.454 50.641  4.882   1.00 66.30  ? 153 ARG B CZ  1 
ATOM   3771  N NH1 . ARG B 2 153 ? -46.449 49.930  3.767   1.00 67.91  ? 153 ARG B NH1 1 
ATOM   3772  N NH2 . ARG B 2 153 ? -46.931 51.884  4.860   1.00 62.17  ? 153 ARG B NH2 1 
ATOM   3773  N N   . ASN B 2 154 ? -47.614 49.829  11.227  1.00 71.51  ? 154 ASN B N   1 
ATOM   3774  C CA  . ASN B 2 154 ? -47.695 50.605  12.462  1.00 65.78  ? 154 ASN B CA  1 
ATOM   3775  C C   . ASN B 2 154 ? -48.068 49.707  13.636  1.00 64.80  ? 154 ASN B C   1 
ATOM   3776  O O   . ASN B 2 154 ? -47.448 49.769  14.703  1.00 85.63  ? 154 ASN B O   1 
ATOM   3777  C CB  . ASN B 2 154 ? -48.712 51.742  12.263  1.00 83.65  ? 154 ASN B CB  1 
ATOM   3778  C CG  . ASN B 2 154 ? -49.121 52.463  13.555  1.00 95.77  ? 154 ASN B CG  1 
ATOM   3779  O OD1 . ASN B 2 154 ? -48.750 52.095  14.670  1.00 95.52  ? 154 ASN B OD1 1 
ATOM   3780  N ND2 . ASN B 2 154 ? -49.911 53.518  13.383  1.00 85.86  ? 154 ASN B ND2 1 
ATOM   3781  N N   . GLY B 2 155 ? -49.062 48.846  13.449  1.00 69.56  ? 155 GLY B N   1 
ATOM   3782  C CA  . GLY B 2 155 ? -49.649 48.100  14.540  1.00 76.65  ? 155 GLY B CA  1 
ATOM   3783  C C   . GLY B 2 155 ? -51.044 48.543  14.935  1.00 87.25  ? 155 GLY B C   1 
ATOM   3784  O O   . GLY B 2 155 ? -51.533 48.118  15.988  1.00 87.17  ? 155 GLY B O   1 
ATOM   3785  N N   . THR B 2 156 ? -51.697 49.378  14.130  1.00 77.05  ? 156 THR B N   1 
ATOM   3786  C CA  . THR B 2 156 ? -53.039 49.879  14.407  1.00 75.86  ? 156 THR B CA  1 
ATOM   3787  C C   . THR B 2 156 ? -54.045 49.357  13.386  1.00 71.63  ? 156 THR B C   1 
ATOM   3788  O O   . THR B 2 156 ? -54.904 50.095  12.899  1.00 75.24  ? 156 THR B O   1 
ATOM   3789  C CB  . THR B 2 156 ? -53.056 51.404  14.439  1.00 79.63  ? 156 THR B CB  1 
ATOM   3790  O OG1 . THR B 2 156 ? -52.808 51.919  13.123  1.00 84.98  ? 156 THR B OG1 1 
ATOM   3791  C CG2 . THR B 2 156 ? -52.006 51.929  15.403  1.00 84.73  ? 156 THR B CG2 1 
ATOM   3792  N N   . TYR B 2 157 ? -53.941 48.075  13.052  1.00 75.83  ? 157 TYR B N   1 
ATOM   3793  C CA  . TYR B 2 157 ? -54.859 47.458  12.104  1.00 77.81  ? 157 TYR B CA  1 
ATOM   3794  C C   . TYR B 2 157 ? -56.256 47.413  12.709  1.00 78.47  ? 157 TYR B C   1 
ATOM   3795  O O   . TYR B 2 157 ? -56.484 46.733  13.714  1.00 73.85  ? 157 TYR B O   1 
ATOM   3796  C CB  . TYR B 2 157 ? -54.371 46.060  11.744  1.00 64.59  ? 157 TYR B CB  1 
ATOM   3797  C CG  . TYR B 2 157 ? -55.300 45.301  10.830  1.00 63.07  ? 157 TYR B CG  1 
ATOM   3798  C CD1 . TYR B 2 157 ? -55.443 45.660  9.496   1.00 66.37  ? 157 TYR B CD1 1 
ATOM   3799  C CD2 . TYR B 2 157 ? -56.033 44.220  11.300  1.00 61.97  ? 157 TYR B CD2 1 
ATOM   3800  C CE1 . TYR B 2 157 ? -56.292 44.960  8.655   1.00 60.33  ? 157 TYR B CE1 1 
ATOM   3801  C CE2 . TYR B 2 157 ? -56.882 43.515  10.467  1.00 64.71  ? 157 TYR B CE2 1 
ATOM   3802  C CZ  . TYR B 2 157 ? -57.007 43.890  9.148   1.00 55.84  ? 157 TYR B CZ  1 
ATOM   3803  O OH  . TYR B 2 157 ? -57.853 43.192  8.322   1.00 68.92  ? 157 TYR B OH  1 
ATOM   3804  N N   . ASP B 2 158 ? -57.189 48.142  12.099  1.00 77.47  ? 158 ASP B N   1 
ATOM   3805  C CA  . ASP B 2 158 ? -58.573 48.202  12.567  1.00 88.15  ? 158 ASP B CA  1 
ATOM   3806  C C   . ASP B 2 158 ? -59.286 46.940  12.099  1.00 71.97  ? 158 ASP B C   1 
ATOM   3807  O O   . ASP B 2 158 ? -59.898 46.902  11.030  1.00 68.50  ? 158 ASP B O   1 
ATOM   3808  C CB  . ASP B 2 158 ? -59.260 49.465  12.054  1.00 95.63  ? 158 ASP B CB  1 
ATOM   3809  C CG  . ASP B 2 158 ? -60.440 49.892  12.919  1.00 94.00  ? 158 ASP B CG  1 
ATOM   3810  O OD1 . ASP B 2 158 ? -60.836 49.127  13.826  1.00 91.21  ? 158 ASP B OD1 1 
ATOM   3811  O OD2 . ASP B 2 158 ? -60.973 50.999  12.690  1.00 97.78  ? 158 ASP B OD2 1 
ATOM   3812  N N   . TYR B 2 159 ? -59.191 45.884  12.909  1.00 69.15  ? 159 TYR B N   1 
ATOM   3813  C CA  . TYR B 2 159 ? -59.826 44.616  12.553  1.00 69.10  ? 159 TYR B CA  1 
ATOM   3814  C C   . TYR B 2 159 ? -61.340 44.719  12.404  1.00 71.92  ? 159 TYR B C   1 
ATOM   3815  O O   . TYR B 2 159 ? -61.873 44.169  11.424  1.00 78.94  ? 159 TYR B O   1 
ATOM   3816  C CB  . TYR B 2 159 ? -59.444 43.538  13.574  1.00 75.46  ? 159 TYR B CB  1 
ATOM   3817  C CG  . TYR B 2 159 ? -60.100 42.201  13.302  1.00 79.00  ? 159 TYR B CG  1 
ATOM   3818  C CD1 . TYR B 2 159 ? -59.538 41.294  12.412  1.00 72.31  ? 159 TYR B CD1 1 
ATOM   3819  C CD2 . TYR B 2 159 ? -61.292 41.854  13.925  1.00 81.14  ? 159 TYR B CD2 1 
ATOM   3820  C CE1 . TYR B 2 159 ? -60.144 40.073  12.158  1.00 73.98  ? 159 TYR B CE1 1 
ATOM   3821  C CE2 . TYR B 2 159 ? -61.903 40.642  13.677  1.00 82.11  ? 159 TYR B CE2 1 
ATOM   3822  C CZ  . TYR B 2 159 ? -61.329 39.754  12.794  1.00 82.16  ? 159 TYR B CZ  1 
ATOM   3823  O OH  . TYR B 2 159 ? -61.954 38.548  12.556  1.00 54.40  ? 159 TYR B OH  1 
ATOM   3824  N N   . PRO B 2 160 ? -62.093 45.359  13.315  1.00 84.41  ? 160 PRO B N   1 
ATOM   3825  C CA  . PRO B 2 160 ? -63.555 45.430  13.118  1.00 84.91  ? 160 PRO B CA  1 
ATOM   3826  C C   . PRO B 2 160 ? -63.973 46.141  11.843  1.00 74.69  ? 160 PRO B C   1 
ATOM   3827  O O   . PRO B 2 160 ? -65.010 45.793  11.263  1.00 79.76  ? 160 PRO B O   1 
ATOM   3828  C CB  . PRO B 2 160 ? -64.043 46.185  14.364  1.00 77.01  ? 160 PRO B CB  1 
ATOM   3829  C CG  . PRO B 2 160 ? -62.982 45.970  15.378  1.00 78.98  ? 160 PRO B CG  1 
ATOM   3830  C CD  . PRO B 2 160 ? -61.697 45.946  14.610  1.00 79.93  ? 160 PRO B CD  1 
ATOM   3831  N N   . GLN B 2 161 ? -63.197 47.126  11.388  1.00 70.95  ? 161 GLN B N   1 
ATOM   3832  C CA  . GLN B 2 161 ? -63.574 47.883  10.200  1.00 71.01  ? 161 GLN B CA  1 
ATOM   3833  C C   . GLN B 2 161 ? -63.599 47.008  8.952   1.00 61.47  ? 161 GLN B C   1 
ATOM   3834  O O   . GLN B 2 161 ? -64.341 47.301  8.007   1.00 74.87  ? 161 GLN B O   1 
ATOM   3835  C CB  . GLN B 2 161 ? -62.615 49.064  10.028  1.00 74.32  ? 161 GLN B CB  1 
ATOM   3836  C CG  . GLN B 2 161 ? -62.327 49.474  8.595   1.00 73.51  ? 161 GLN B CG  1 
ATOM   3837  C CD  . GLN B 2 161 ? -61.892 50.919  8.487   1.00 86.40  ? 161 GLN B CD  1 
ATOM   3838  O OE1 . GLN B 2 161 ? -61.206 51.439  9.368   1.00 95.36  ? 161 GLN B OE1 1 
ATOM   3839  N NE2 . GLN B 2 161 ? -62.286 51.578  7.404   1.00 81.61  ? 161 GLN B NE2 1 
ATOM   3840  N N   . TYR B 2 162 ? -62.826 45.921  8.934   1.00 66.27  ? 162 TYR B N   1 
ATOM   3841  C CA  . TYR B 2 162 ? -62.731 45.064  7.760   1.00 65.05  ? 162 TYR B CA  1 
ATOM   3842  C C   . TYR B 2 162 ? -63.281 43.661  7.971   1.00 65.18  ? 162 TYR B C   1 
ATOM   3843  O O   . TYR B 2 162 ? -63.283 42.871  7.018   1.00 63.52  ? 162 TYR B O   1 
ATOM   3844  C CB  . TYR B 2 162 ? -61.270 44.963  7.294   1.00 66.29  ? 162 TYR B CB  1 
ATOM   3845  C CG  . TYR B 2 162 ? -60.611 46.303  7.049   1.00 68.53  ? 162 TYR B CG  1 
ATOM   3846  C CD1 . TYR B 2 162 ? -60.955 47.078  5.949   1.00 66.87  ? 162 TYR B CD1 1 
ATOM   3847  C CD2 . TYR B 2 162 ? -59.651 46.798  7.924   1.00 61.55  ? 162 TYR B CD2 1 
ATOM   3848  C CE1 . TYR B 2 162 ? -60.357 48.307  5.723   1.00 69.68  ? 162 TYR B CE1 1 
ATOM   3849  C CE2 . TYR B 2 162 ? -59.049 48.027  7.707   1.00 65.54  ? 162 TYR B CE2 1 
ATOM   3850  C CZ  . TYR B 2 162 ? -59.405 48.777  6.605   1.00 68.14  ? 162 TYR B CZ  1 
ATOM   3851  O OH  . TYR B 2 162 ? -58.809 49.999  6.381   1.00 77.45  ? 162 TYR B OH  1 
ATOM   3852  N N   . SER B 2 163 ? -63.756 43.327  9.174   1.00 76.10  ? 163 SER B N   1 
ATOM   3853  C CA  . SER B 2 163 ? -64.148 41.948  9.462   1.00 77.90  ? 163 SER B CA  1 
ATOM   3854  C C   . SER B 2 163 ? -65.250 41.479  8.524   1.00 76.35  ? 163 SER B C   1 
ATOM   3855  O O   . SER B 2 163 ? -65.191 40.369  7.983   1.00 77.09  ? 163 SER B O   1 
ATOM   3856  C CB  . SER B 2 163 ? -64.601 41.823  10.916  1.00 69.14  ? 163 SER B CB  1 
ATOM   3857  O OG  . SER B 2 163 ? -63.759 42.568  11.772  1.00 79.45  ? 163 SER B OG  1 
ATOM   3858  N N   . GLU B 2 164 ? -66.266 42.319  8.317   1.00 67.21  ? 164 GLU B N   1 
ATOM   3859  C CA  . GLU B 2 164 ? -67.365 41.948  7.433   1.00 81.22  ? 164 GLU B CA  1 
ATOM   3860  C C   . GLU B 2 164 ? -66.884 41.802  5.995   1.00 75.45  ? 164 GLU B C   1 
ATOM   3861  O O   . GLU B 2 164 ? -67.116 40.772  5.351   1.00 74.19  ? 164 GLU B O   1 
ATOM   3862  C CB  . GLU B 2 164 ? -68.485 42.986  7.532   1.00 83.70  ? 164 GLU B CB  1 
ATOM   3863  C CG  . GLU B 2 164 ? -69.851 42.497  7.063   1.00 91.81  ? 164 GLU B CG  1 
ATOM   3864  C CD  . GLU B 2 164 ? -70.355 41.287  7.837   1.00 97.02  ? 164 GLU B CD  1 
ATOM   3865  O OE1 . GLU B 2 164 ? -69.982 41.124  9.019   1.00 91.28  ? 164 GLU B OE1 1 
ATOM   3866  O OE2 . GLU B 2 164 ? -71.131 40.495  7.257   1.00 93.41  ? 164 GLU B OE2 1 
ATOM   3867  N N   . GLU B 2 165 ? -66.177 42.817  5.489   1.00 75.26  ? 165 GLU B N   1 
ATOM   3868  C CA  . GLU B 2 165 ? -65.734 42.811  4.098   1.00 70.21  ? 165 GLU B CA  1 
ATOM   3869  C C   . GLU B 2 165 ? -64.920 41.564  3.776   1.00 78.88  ? 165 GLU B C   1 
ATOM   3870  O O   . GLU B 2 165 ? -65.065 40.980  2.695   1.00 74.93  ? 165 GLU B O   1 
ATOM   3871  C CB  . GLU B 2 165 ? -64.922 44.073  3.810   1.00 67.29  ? 165 GLU B CB  1 
ATOM   3872  C CG  . GLU B 2 165 ? -65.004 44.534  2.372   1.00 78.93  ? 165 GLU B CG  1 
ATOM   3873  C CD  . GLU B 2 165 ? -63.795 45.339  1.950   1.00 71.69  ? 165 GLU B CD  1 
ATOM   3874  O OE1 . GLU B 2 165 ? -63.401 46.257  2.702   1.00 73.46  ? 165 GLU B OE1 1 
ATOM   3875  O OE2 . GLU B 2 165 ? -63.241 45.054  0.866   1.00 72.60  ? 165 GLU B OE2 1 
ATOM   3876  N N   . ALA B 2 166 ? -64.058 41.139  4.705   1.00 76.46  ? 166 ALA B N   1 
ATOM   3877  C CA  . ALA B 2 166 ? -63.302 39.907  4.504   1.00 74.65  ? 166 ALA B CA  1 
ATOM   3878  C C   . ALA B 2 166 ? -64.188 38.675  4.629   1.00 78.10  ? 166 ALA B C   1 
ATOM   3879  O O   . ALA B 2 166 ? -63.948 37.670  3.950   1.00 70.46  ? 166 ALA B O   1 
ATOM   3880  C CB  . ALA B 2 166 ? -62.146 39.830  5.502   1.00 75.38  ? 166 ALA B CB  1 
ATOM   3881  N N   . ARG B 2 167 ? -65.203 38.727  5.498   1.00 76.80  ? 167 ARG B N   1 
ATOM   3882  C CA  . ARG B 2 167 ? -66.086 37.578  5.667   1.00 81.68  ? 167 ARG B CA  1 
ATOM   3883  C C   . ARG B 2 167 ? -66.864 37.287  4.389   1.00 89.94  ? 167 ARG B C   1 
ATOM   3884  O O   . ARG B 2 167 ? -66.969 36.127  3.972   1.00 82.43  ? 167 ARG B O   1 
ATOM   3885  C CB  . ARG B 2 167 ? -67.039 37.815  6.839   1.00 86.92  ? 167 ARG B CB  1 
ATOM   3886  C CG  . ARG B 2 167 ? -67.513 36.534  7.512   1.00 84.16  ? 167 ARG B CG  1 
ATOM   3887  C CD  . ARG B 2 167 ? -68.895 36.698  8.129   1.00 89.72  ? 167 ARG B CD  1 
ATOM   3888  N NE  . ARG B 2 167 ? -69.702 37.692  7.429   1.00 98.44  ? 167 ARG B NE  1 
ATOM   3889  C CZ  . ARG B 2 167 ? -70.648 37.405  6.544   1.00 100.04 ? 167 ARG B CZ  1 
ATOM   3890  N NH1 . ARG B 2 167 ? -70.931 36.156  6.212   1.00 93.50  ? 167 ARG B NH1 1 
ATOM   3891  N NH2 . ARG B 2 167 ? -71.329 38.398  5.979   1.00 91.83  ? 167 ARG B NH2 1 
ATOM   3892  N N   . LEU B 2 168 ? -67.408 38.329  3.748   1.00 88.39  ? 168 LEU B N   1 
ATOM   3893  C CA  . LEU B 2 168 ? -68.128 38.132  2.491   1.00 85.99  ? 168 LEU B CA  1 
ATOM   3894  C C   . LEU B 2 168 ? -67.216 37.549  1.421   1.00 87.15  ? 168 LEU B C   1 
ATOM   3895  O O   . LEU B 2 168 ? -67.622 36.655  0.667   1.00 81.88  ? 168 LEU B O   1 
ATOM   3896  C CB  . LEU B 2 168 ? -68.735 39.448  1.998   1.00 87.13  ? 168 LEU B CB  1 
ATOM   3897  C CG  . LEU B 2 168 ? -70.043 39.982  2.602   1.00 96.94  ? 168 LEU B CG  1 
ATOM   3898  C CD1 . LEU B 2 168 ? -71.144 38.930  2.542   1.00 89.64  ? 168 LEU B CD1 1 
ATOM   3899  C CD2 . LEU B 2 168 ? -69.873 40.519  4.017   1.00 90.90  ? 168 LEU B CD2 1 
ATOM   3900  N N   . LYS B 2 169 ? -65.982 38.053  1.331   1.00 83.52  ? 169 LYS B N   1 
ATOM   3901  C CA  . LYS B 2 169 ? -65.021 37.492  0.388   1.00 88.98  ? 169 LYS B CA  1 
ATOM   3902  C C   . LYS B 2 169 ? -64.710 36.038  0.717   1.00 86.25  ? 169 LYS B C   1 
ATOM   3903  O O   . LYS B 2 169 ? -64.680 35.189  -0.179  1.00 88.94  ? 169 LYS B O   1 
ATOM   3904  C CB  . LYS B 2 169 ? -63.740 38.327  0.382   1.00 86.91  ? 169 LYS B CB  1 
ATOM   3905  C CG  . LYS B 2 169 ? -62.643 37.797  -0.535  1.00 71.62  ? 169 LYS B CG  1 
ATOM   3906  C CD  . LYS B 2 169 ? -63.144 37.589  -1.958  1.00 74.14  ? 169 LYS B CD  1 
ATOM   3907  C CE  . LYS B 2 169 ? -63.258 38.909  -2.710  1.00 82.85  ? 169 LYS B CE  1 
ATOM   3908  N NZ  . LYS B 2 169 ? -61.980 39.672  -2.714  1.00 86.18  ? 169 LYS B NZ  1 
ATOM   3909  N N   . ARG B 2 170 ? -64.499 35.729  2.002   1.00 90.55  ? 170 ARG B N   1 
ATOM   3910  C CA  . ARG B 2 170 ? -64.084 34.382  2.389   1.00 93.99  ? 170 ARG B CA  1 
ATOM   3911  C C   . ARG B 2 170 ? -65.106 33.336  1.958   1.00 94.44  ? 170 ARG B C   1 
ATOM   3912  O O   . ARG B 2 170 ? -64.737 32.228  1.552   1.00 98.34  ? 170 ARG B O   1 
ATOM   3913  C CB  . ARG B 2 170 ? -63.849 34.315  3.900   1.00 87.43  ? 170 ARG B CB  1 
ATOM   3914  C CG  . ARG B 2 170 ? -62.687 33.411  4.313   1.00 80.94  ? 170 ARG B CG  1 
ATOM   3915  C CD  . ARG B 2 170 ? -62.087 33.823  5.653   1.00 60.49  ? 170 ARG B CD  1 
ATOM   3916  N NE  . ARG B 2 170 ? -63.099 34.083  6.671   1.00 62.10  ? 170 ARG B NE  1 
ATOM   3917  C CZ  . ARG B 2 170 ? -63.178 35.203  7.380   1.00 68.36  ? 170 ARG B CZ  1 
ATOM   3918  N NH1 . ARG B 2 170 ? -62.329 36.200  7.196   1.00 66.87  ? 170 ARG B NH1 1 
ATOM   3919  N NH2 . ARG B 2 170 ? -64.135 35.326  8.295   1.00 64.94  ? 170 ARG B NH2 1 
ATOM   3920  N N   . GLU B 2 171 ? -66.397 33.671  2.028   1.00 93.19  ? 171 GLU B N   1 
ATOM   3921  C CA  . GLU B 2 171 ? -67.430 32.733  1.602   1.00 98.10  ? 171 GLU B CA  1 
ATOM   3922  C C   . GLU B 2 171 ? -67.488 32.571  0.087   1.00 95.96  ? 171 GLU B C   1 
ATOM   3923  O O   . GLU B 2 171 ? -67.983 31.544  -0.393  1.00 104.28 ? 171 GLU B O   1 
ATOM   3924  C CB  . GLU B 2 171 ? -68.796 33.177  2.127   1.00 105.37 ? 171 GLU B CB  1 
ATOM   3925  C CG  . GLU B 2 171 ? -68.787 33.632  3.577   1.00 107.99 ? 171 GLU B CG  1 
ATOM   3926  C CD  . GLU B 2 171 ? -69.358 32.593  4.521   1.00 112.52 ? 171 GLU B CD  1 
ATOM   3927  O OE1 . GLU B 2 171 ? -69.058 31.393  4.338   1.00 106.79 ? 171 GLU B OE1 1 
ATOM   3928  O OE2 . GLU B 2 171 ? -70.106 32.980  5.445   1.00 99.05  ? 171 GLU B OE2 1 
ATOM   3929  N N   . GLU B 2 172 ? -67.001 33.556  -0.674  1.00 97.24  ? 172 GLU B N   1 
ATOM   3930  C CA  . GLU B 2 172 ? -67.065 33.471  -2.132  1.00 101.60 ? 172 GLU B CA  1 
ATOM   3931  C C   . GLU B 2 172 ? -66.209 32.326  -2.666  1.00 100.55 ? 172 GLU B C   1 
ATOM   3932  O O   . GLU B 2 172 ? -66.635 31.599  -3.571  1.00 100.47 ? 172 GLU B O   1 
ATOM   3933  C CB  . GLU B 2 172 ? -66.641 34.801  -2.760  1.00 97.73  ? 172 GLU B CB  1 
ATOM   3934  C CG  . GLU B 2 172 ? -67.754 35.839  -2.864  1.00 95.07  ? 172 GLU B CG  1 
ATOM   3935  C CD  . GLU B 2 172 ? -69.083 35.243  -3.300  1.00 111.21 ? 172 GLU B CD  1 
ATOM   3936  O OE1 . GLU B 2 172 ? -69.103 34.472  -4.284  1.00 111.56 ? 172 GLU B OE1 1 
ATOM   3937  O OE2 . GLU B 2 172 ? -70.111 35.550  -2.657  1.00 101.77 ? 172 GLU B OE2 1 
ATOM   3938  N N   . ILE B 2 173 ? -64.997 32.152  -2.124  1.00 104.93 ? 173 ILE B N   1 
ATOM   3939  C CA  . ILE B 2 173 ? -64.142 31.050  -2.562  1.00 109.84 ? 173 ILE B CA  1 
ATOM   3940  C C   . ILE B 2 173 ? -64.548 29.726  -1.930  1.00 105.64 ? 173 ILE B C   1 
ATOM   3941  O O   . ILE B 2 173 ? -64.058 28.668  -2.350  1.00 99.25  ? 173 ILE B O   1 
ATOM   3942  C CB  . ILE B 2 173 ? -62.648 31.335  -2.292  1.00 104.70 ? 173 ILE B CB  1 
ATOM   3943  C CG1 . ILE B 2 173 ? -62.259 32.783  -2.620  1.00 98.97  ? 173 ILE B CG1 1 
ATOM   3944  C CG2 . ILE B 2 173 ? -61.749 30.426  -3.111  1.00 101.88 ? 173 ILE B CG2 1 
ATOM   3945  C CD1 . ILE B 2 173 ? -62.403 33.754  -1.480  1.00 83.77  ? 173 ILE B CD1 1 
ATOM   3946  N N   . SER B 2 174 ? -65.431 29.747  -0.937  1.00 101.96 ? 174 SER B N   1 
ATOM   3947  C CA  . SER B 2 174 ? -65.978 28.517  -0.376  1.00 104.51 ? 174 SER B CA  1 
ATOM   3948  C C   . SER B 2 174 ? -67.434 28.330  -0.804  1.00 90.54  ? 174 SER B C   1 
ATOM   3949  O O   . SER B 2 174 ? -67.846 28.803  -1.865  1.00 86.61  ? 174 SER B O   1 
ATOM   3950  C CB  . SER B 2 174 ? -65.874 28.520  1.152   1.00 95.44  ? 174 SER B CB  1 
ATOM   3951  O OG  . SER B 2 174 ? -66.093 29.818  1.675   1.00 97.23  ? 174 SER B OG  1 
ATOM   3952  N N   . GLY C 1 2   ? -67.001 37.862  28.330  1.00 53.36  ? 10  GLY C N   1 
ATOM   3953  C CA  . GLY C 1 2   ? -66.458 36.543  28.049  1.00 62.59  ? 10  GLY C CA  1 
ATOM   3954  C C   . GLY C 1 2   ? -65.341 36.104  28.982  1.00 52.14  ? 10  GLY C C   1 
ATOM   3955  O O   . GLY C 1 2   ? -64.427 36.876  29.280  1.00 60.96  ? 10  GLY C O   1 
ATOM   3956  N N   . ASP C 1 3   ? -65.415 34.855  29.440  1.00 50.63  ? 11  ASP C N   1 
ATOM   3957  C CA  . ASP C 1 3   ? -64.402 34.316  30.339  1.00 49.57  ? 11  ASP C CA  1 
ATOM   3958  C C   . ASP C 1 3   ? -63.046 34.253  29.639  1.00 51.98  ? 11  ASP C C   1 
ATOM   3959  O O   . ASP C 1 3   ? -62.953 34.020  28.431  1.00 53.61  ? 11  ASP C O   1 
ATOM   3960  C CB  . ASP C 1 3   ? -64.809 32.923  30.830  1.00 45.49  ? 11  ASP C CB  1 
ATOM   3961  C CG  . ASP C 1 3   ? -66.173 32.912  31.514  1.00 65.63  ? 11  ASP C CG  1 
ATOM   3962  O OD1 . ASP C 1 3   ? -66.642 33.989  31.943  1.00 63.89  ? 11  ASP C OD1 1 
ATOM   3963  O OD2 . ASP C 1 3   ? -66.775 31.819  31.625  1.00 59.43  ? 11  ASP C OD2 1 
ATOM   3964  N N   . GLN C 1 4   ? -61.983 34.480  30.408  1.00 44.36  ? 12  GLN C N   1 
ATOM   3965  C CA  . GLN C 1 4   ? -60.647 34.560  29.835  1.00 53.33  ? 12  GLN C CA  1 
ATOM   3966  C C   . GLN C 1 4   ? -59.645 33.805  30.695  1.00 42.25  ? 12  GLN C C   1 
ATOM   3967  O O   . GLN C 1 4   ? -59.754 33.772  31.923  1.00 42.22  ? 12  GLN C O   1 
ATOM   3968  C CB  . GLN C 1 4   ? -60.187 36.015  29.670  1.00 50.15  ? 12  GLN C CB  1 
ATOM   3969  C CG  . GLN C 1 4   ? -60.916 36.776  28.568  1.00 63.66  ? 12  GLN C CG  1 
ATOM   3970  C CD  . GLN C 1 4   ? -60.378 38.182  28.378  1.00 74.16  ? 12  GLN C CD  1 
ATOM   3971  O OE1 . GLN C 1 4   ? -59.192 38.442  28.601  1.00 68.69  ? 12  GLN C OE1 1 
ATOM   3972  N NE2 . GLN C 1 4   ? -61.249 39.097  27.965  1.00 64.70  ? 12  GLN C NE2 1 
ATOM   3973  N N   . ILE C 1 5   ? -58.666 33.196  30.028  1.00 43.19  ? 13  ILE C N   1 
ATOM   3974  C CA  . ILE C 1 5   ? -57.492 32.634  30.682  1.00 43.37  ? 13  ILE C CA  1 
ATOM   3975  C C   . ILE C 1 5   ? -56.256 33.212  30.001  1.00 46.57  ? 13  ILE C C   1 
ATOM   3976  O O   . ILE C 1 5   ? -56.216 33.351  28.772  1.00 42.44  ? 13  ILE C O   1 
ATOM   3977  C CB  . ILE C 1 5   ? -57.488 31.088  30.660  1.00 42.20  ? 13  ILE C CB  1 
ATOM   3978  C CG1 . ILE C 1 5   ? -56.431 30.547  31.628  1.00 46.31  ? 13  ILE C CG1 1 
ATOM   3979  C CG2 . ILE C 1 5   ? -57.269 30.544  29.256  1.00 41.35  ? 13  ILE C CG2 1 
ATOM   3980  C CD1 . ILE C 1 5   ? -56.565 29.064  31.933  1.00 39.49  ? 13  ILE C CD1 1 
ATOM   3981  N N   . CYS C 1 6   ? -55.267 33.592  30.807  1.00 46.32  ? 14  CYS C N   1 
ATOM   3982  C CA  . CYS C 1 6   ? -54.086 34.297  30.334  1.00 41.32  ? 14  CYS C CA  1 
ATOM   3983  C C   . CYS C 1 6   ? -52.823 33.558  30.750  1.00 43.21  ? 14  CYS C C   1 
ATOM   3984  O O   . CYS C 1 6   ? -52.768 32.941  31.816  1.00 39.40  ? 14  CYS C O   1 
ATOM   3985  C CB  . CYS C 1 6   ? -54.028 35.728  30.886  1.00 39.09  ? 14  CYS C CB  1 
ATOM   3986  S SG  . CYS C 1 6   ? -55.331 36.819  30.303  1.00 65.89  ? 14  CYS C SG  1 
ATOM   3987  N N   . ILE C 1 7   ? -51.808 33.640  29.899  1.00 38.41  ? 15  ILE C N   1 
ATOM   3988  C CA  . ILE C 1 7   ? -50.481 33.120  30.198  1.00 45.27  ? 15  ILE C CA  1 
ATOM   3989  C C   . ILE C 1 7   ? -49.602 34.282  30.625  1.00 46.57  ? 15  ILE C C   1 
ATOM   3990  O O   . ILE C 1 7   ? -49.736 35.409  30.134  1.00 52.16  ? 15  ILE C O   1 
ATOM   3991  C CB  . ILE C 1 7   ? -49.868 32.383  28.990  1.00 46.42  ? 15  ILE C CB  1 
ATOM   3992  C CG1 . ILE C 1 7   ? -50.895 31.448  28.357  1.00 46.50  ? 15  ILE C CG1 1 
ATOM   3993  C CG2 . ILE C 1 7   ? -48.623 31.620  29.404  1.00 45.48  ? 15  ILE C CG2 1 
ATOM   3994  C CD1 . ILE C 1 7   ? -51.137 30.203  29.155  1.00 49.79  ? 15  ILE C CD1 1 
ATOM   3995  N N   . GLY C 1 8   ? -48.699 34.014  31.557  1.00 38.34  ? 16  GLY C N   1 
ATOM   3996  C CA  . GLY C 1 8   ? -47.837 35.068  32.052  1.00 46.72  ? 16  GLY C CA  1 
ATOM   3997  C C   . GLY C 1 8   ? -46.729 34.475  32.886  1.00 39.74  ? 16  GLY C C   1 
ATOM   3998  O O   . GLY C 1 8   ? -46.657 33.262  33.092  1.00 47.69  ? 16  GLY C O   1 
ATOM   3999  N N   . TYR C 1 9   ? -45.863 35.354  33.370  1.00 46.17  ? 17  TYR C N   1 
ATOM   4000  C CA  . TYR C 1 9   ? -44.681 34.941  34.105  1.00 43.95  ? 17  TYR C CA  1 
ATOM   4001  C C   . TYR C 1 9   ? -44.549 35.784  35.365  1.00 47.99  ? 17  TYR C C   1 
ATOM   4002  O O   . TYR C 1 9   ? -45.240 36.791  35.549  1.00 52.07  ? 17  TYR C O   1 
ATOM   4003  C CB  . TYR C 1 9   ? -43.416 35.041  33.239  1.00 39.38  ? 17  TYR C CB  1 
ATOM   4004  C CG  . TYR C 1 9   ? -43.284 36.332  32.463  1.00 46.88  ? 17  TYR C CG  1 
ATOM   4005  C CD1 . TYR C 1 9   ? -44.001 36.540  31.291  1.00 38.36  ? 17  TYR C CD1 1 
ATOM   4006  C CD2 . TYR C 1 9   ? -42.426 37.338  32.892  1.00 48.17  ? 17  TYR C CD2 1 
ATOM   4007  C CE1 . TYR C 1 9   ? -43.880 37.719  30.577  1.00 45.13  ? 17  TYR C CE1 1 
ATOM   4008  C CE2 . TYR C 1 9   ? -42.297 38.517  32.182  1.00 47.28  ? 17  TYR C CE2 1 
ATOM   4009  C CZ  . TYR C 1 9   ? -43.030 38.704  31.028  1.00 52.13  ? 17  TYR C CZ  1 
ATOM   4010  O OH  . TYR C 1 9   ? -42.912 39.876  30.315  1.00 55.13  ? 17  TYR C OH  1 
ATOM   4011  N N   . HIS C 1 10  ? -43.647 35.341  36.234  1.00 44.59  ? 18  HIS C N   1 
ATOM   4012  C CA  . HIS C 1 10  ? -43.445 35.946  37.542  1.00 43.58  ? 18  HIS C CA  1 
ATOM   4013  C C   . HIS C 1 10  ? -42.681 37.259  37.434  1.00 53.42  ? 18  HIS C C   1 
ATOM   4014  O O   . HIS C 1 10  ? -41.754 37.394  36.630  1.00 54.13  ? 18  HIS C O   1 
ATOM   4015  C CB  . HIS C 1 10  ? -42.684 34.968  38.439  1.00 56.75  ? 18  HIS C CB  1 
ATOM   4016  C CG  . HIS C 1 10  ? -42.107 35.585  39.673  1.00 66.05  ? 18  HIS C CG  1 
ATOM   4017  N ND1 . HIS C 1 10  ? -40.757 35.565  39.953  1.00 64.22  ? 18  HIS C ND1 1 
ATOM   4018  C CD2 . HIS C 1 10  ? -42.698 36.219  40.713  1.00 66.54  ? 18  HIS C CD2 1 
ATOM   4019  C CE1 . HIS C 1 10  ? -40.540 36.171  41.107  1.00 65.94  ? 18  HIS C CE1 1 
ATOM   4020  N NE2 . HIS C 1 10  ? -41.702 36.576  41.589  1.00 81.01  ? 18  HIS C NE2 1 
ATOM   4021  N N   . ALA C 1 11  ? -43.083 38.232  38.251  1.00 58.78  ? 19  ALA C N   1 
ATOM   4022  C CA  . ALA C 1 11  ? -42.372 39.494  38.401  1.00 50.40  ? 19  ALA C CA  1 
ATOM   4023  C C   . ALA C 1 11  ? -42.301 39.830  39.885  1.00 59.22  ? 19  ALA C C   1 
ATOM   4024  O O   . ALA C 1 11  ? -43.200 39.476  40.652  1.00 66.10  ? 19  ALA C O   1 
ATOM   4025  C CB  . ALA C 1 11  ? -43.056 40.626  37.625  1.00 38.64  ? 19  ALA C CB  1 
ATOM   4026  N N   . ASN C 1 12  ? -41.229 40.512  40.292  1.00 49.10  ? 20  ASN C N   1 
ATOM   4027  C CA  . ASN C 1 12  ? -41.046 40.844  41.703  1.00 51.12  ? 20  ASN C CA  1 
ATOM   4028  C C   . ASN C 1 12  ? -40.375 42.214  41.817  1.00 56.88  ? 20  ASN C C   1 
ATOM   4029  O O   . ASN C 1 12  ? -40.296 42.979  40.851  1.00 55.53  ? 20  ASN C O   1 
ATOM   4030  C CB  . ASN C 1 12  ? -40.258 39.743  42.429  1.00 47.67  ? 20  ASN C CB  1 
ATOM   4031  C CG  . ASN C 1 12  ? -38.826 39.607  41.933  1.00 55.13  ? 20  ASN C CG  1 
ATOM   4032  O OD1 . ASN C 1 12  ? -38.328 40.430  41.160  1.00 51.31  ? 20  ASN C OD1 1 
ATOM   4033  N ND2 . ASN C 1 12  ? -38.155 38.554  42.383  1.00 49.24  ? 20  ASN C ND2 1 
ATOM   4034  N N   . ASN C 1 13  ? -39.885 42.520  43.018  1.00 55.16  ? 21  ASN C N   1 
ATOM   4035  C CA  . ASN C 1 13  ? -39.322 43.826  43.334  1.00 65.71  ? 21  ASN C CA  1 
ATOM   4036  C C   . ASN C 1 13  ? -37.799 43.830  43.306  1.00 63.88  ? 21  ASN C C   1 
ATOM   4037  O O   . ASN C 1 13  ? -37.176 44.735  43.871  1.00 58.15  ? 21  ASN C O   1 
ATOM   4038  C CB  . ASN C 1 13  ? -39.827 44.301  44.697  1.00 52.94  ? 21  ASN C CB  1 
ATOM   4039  C CG  . ASN C 1 13  ? -41.245 44.835  44.634  1.00 74.95  ? 21  ASN C CG  1 
ATOM   4040  O OD1 . ASN C 1 13  ? -41.711 45.256  43.575  1.00 86.11  ? 21  ASN C OD1 1 
ATOM   4041  N ND2 . ASN C 1 13  ? -41.938 44.821  45.769  1.00 89.35  ? 21  ASN C ND2 1 
ATOM   4042  N N   . SER C 1 14  ? -37.189 42.841  42.662  1.00 66.84  ? 22  SER C N   1 
ATOM   4043  C CA  . SER C 1 14  ? -35.739 42.796  42.570  1.00 52.97  ? 22  SER C CA  1 
ATOM   4044  C C   . SER C 1 14  ? -35.218 43.888  41.644  1.00 53.37  ? 22  SER C C   1 
ATOM   4045  O O   . SER C 1 14  ? -35.852 44.240  40.645  1.00 53.98  ? 22  SER C O   1 
ATOM   4046  C CB  . SER C 1 14  ? -35.278 41.432  42.068  1.00 50.43  ? 22  SER C CB  1 
ATOM   4047  O OG  . SER C 1 14  ? -33.948 41.509  41.584  1.00 56.64  ? 22  SER C OG  1 
ATOM   4048  N N   . THR C 1 15  ? -34.053 44.429  41.987  1.00 51.31  ? 23  THR C N   1 
ATOM   4049  C CA  . THR C 1 15  ? -33.361 45.385  41.135  1.00 52.54  ? 23  THR C CA  1 
ATOM   4050  C C   . THR C 1 15  ? -32.013 44.852  40.670  1.00 60.80  ? 23  THR C C   1 
ATOM   4051  O O   . THR C 1 15  ? -31.214 45.614  40.114  1.00 58.87  ? 23  THR C O   1 
ATOM   4052  C CB  . THR C 1 15  ? -33.179 46.719  41.864  1.00 61.22  ? 23  THR C CB  1 
ATOM   4053  O OG1 . THR C 1 15  ? -32.773 46.468  43.215  1.00 63.18  ? 23  THR C OG1 1 
ATOM   4054  C CG2 . THR C 1 15  ? -34.482 47.516  41.863  1.00 51.99  ? 23  THR C CG2 1 
ATOM   4055  N N   . GLU C 1 16  ? -31.742 43.565  40.890  1.00 48.83  ? 24  GLU C N   1 
ATOM   4056  C CA  . GLU C 1 16  ? -30.481 42.974  40.468  1.00 55.65  ? 24  GLU C CA  1 
ATOM   4057  C C   . GLU C 1 16  ? -30.343 43.054  38.953  1.00 53.55  ? 24  GLU C C   1 
ATOM   4058  O O   . GLU C 1 16  ? -31.282 42.747  38.213  1.00 53.50  ? 24  GLU C O   1 
ATOM   4059  C CB  . GLU C 1 16  ? -30.398 41.520  40.933  1.00 55.34  ? 24  GLU C CB  1 
ATOM   4060  C CG  . GLU C 1 16  ? -29.878 41.352  42.350  1.00 68.68  ? 24  GLU C CG  1 
ATOM   4061  C CD  . GLU C 1 16  ? -29.289 39.973  42.599  1.00 85.69  ? 24  GLU C CD  1 
ATOM   4062  O OE1 . GLU C 1 16  ? -30.057 39.041  42.930  1.00 76.91  ? 24  GLU C OE1 1 
ATOM   4063  O OE2 . GLU C 1 16  ? -28.054 39.823  42.463  1.00 90.17  ? 24  GLU C OE2 1 
ATOM   4064  N N   . GLN C 1 17  ? -29.166 43.468  38.495  1.00 56.89  ? 25  GLN C N   1 
ATOM   4065  C CA  . GLN C 1 17  ? -28.884 43.640  37.078  1.00 60.88  ? 25  GLN C CA  1 
ATOM   4066  C C   . GLN C 1 17  ? -27.803 42.659  36.648  1.00 53.39  ? 25  GLN C C   1 
ATOM   4067  O O   . GLN C 1 17  ? -26.771 42.535  37.316  1.00 61.40  ? 25  GLN C O   1 
ATOM   4068  C CB  . GLN C 1 17  ? -28.446 45.074  36.778  1.00 54.55  ? 25  GLN C CB  1 
ATOM   4069  C CG  . GLN C 1 17  ? -29.596 46.026  36.506  1.00 56.20  ? 25  GLN C CG  1 
ATOM   4070  C CD  . GLN C 1 17  ? -29.148 47.473  36.430  1.00 73.82  ? 25  GLN C CD  1 
ATOM   4071  O OE1 . GLN C 1 17  ? -27.950 47.768  36.446  1.00 72.76  ? 25  GLN C OE1 1 
ATOM   4072  N NE2 . GLN C 1 17  ? -30.110 48.384  36.340  1.00 65.78  ? 25  GLN C NE2 1 
ATOM   4073  N N   . VAL C 1 18  ? -28.051 41.958  35.542  1.00 41.41  ? 26  VAL C N   1 
ATOM   4074  C CA  . VAL C 1 18  ? -27.055 41.125  34.886  1.00 39.83  ? 26  VAL C CA  1 
ATOM   4075  C C   . VAL C 1 18  ? -26.794 41.702  33.502  1.00 47.83  ? 26  VAL C C   1 
ATOM   4076  O O   . VAL C 1 18  ? -27.505 42.587  33.025  1.00 43.26  ? 26  VAL C O   1 
ATOM   4077  C CB  . VAL C 1 18  ? -27.485 39.650  34.769  1.00 46.82  ? 26  VAL C CB  1 
ATOM   4078  C CG1 . VAL C 1 18  ? -27.927 39.099  36.112  1.00 46.55  ? 26  VAL C CG1 1 
ATOM   4079  C CG2 . VAL C 1 18  ? -28.587 39.517  33.728  1.00 42.73  ? 26  VAL C CG2 1 
ATOM   4080  N N   . ASP C 1 19  ? -25.771 41.164  32.848  1.00 51.91  ? 27  ASP C N   1 
ATOM   4081  C CA  . ASP C 1 19  ? -25.403 41.568  31.502  1.00 48.58  ? 27  ASP C CA  1 
ATOM   4082  C C   . ASP C 1 19  ? -25.397 40.353  30.585  1.00 38.26  ? 27  ASP C C   1 
ATOM   4083  O O   . ASP C 1 19  ? -24.988 39.261  30.987  1.00 43.85  ? 27  ASP C O   1 
ATOM   4084  C CB  . ASP C 1 19  ? -24.033 42.252  31.495  1.00 42.43  ? 27  ASP C CB  1 
ATOM   4085  C CG  . ASP C 1 19  ? -24.102 43.698  31.956  1.00 63.41  ? 27  ASP C CG  1 
ATOM   4086  O OD1 . ASP C 1 19  ? -24.349 43.934  33.161  1.00 71.71  ? 27  ASP C OD1 1 
ATOM   4087  O OD2 . ASP C 1 19  ? -23.905 44.599  31.113  1.00 67.26  ? 27  ASP C OD2 1 
ATOM   4088  N N   . THR C 1 20  ? -25.867 40.542  29.359  1.00 30.54  ? 28  THR C N   1 
ATOM   4089  C CA  . THR C 1 20  ? -25.804 39.511  28.336  1.00 42.61  ? 28  THR C CA  1 
ATOM   4090  C C   . THR C 1 20  ? -24.848 39.943  27.232  1.00 46.78  ? 28  THR C C   1 
ATOM   4091  O O   . THR C 1 20  ? -24.402 41.091  27.178  1.00 46.92  ? 28  THR C O   1 
ATOM   4092  C CB  . THR C 1 20  ? -27.195 39.212  27.758  1.00 45.73  ? 28  THR C CB  1 
ATOM   4093  O OG1 . THR C 1 20  ? -27.517 40.173  26.745  1.00 49.67  ? 28  THR C OG1 1 
ATOM   4094  C CG2 . THR C 1 20  ? -28.253 39.255  28.853  1.00 32.51  ? 28  THR C CG2 1 
ATOM   4095  N N   . ILE C 1 21  ? -24.537 38.999  26.341  1.00 50.95  ? 29  ILE C N   1 
ATOM   4096  C CA  . ILE C 1 21  ? -23.629 39.298  25.240  1.00 40.97  ? 29  ILE C CA  1 
ATOM   4097  C C   . ILE C 1 21  ? -24.201 40.401  24.360  1.00 48.98  ? 29  ILE C C   1 
ATOM   4098  O O   . ILE C 1 21  ? -23.453 41.136  23.703  1.00 58.65  ? 29  ILE C O   1 
ATOM   4099  C CB  . ILE C 1 21  ? -23.328 38.015  24.432  1.00 44.53  ? 29  ILE C CB  1 
ATOM   4100  C CG1 . ILE C 1 21  ? -22.239 38.274  23.395  1.00 56.32  ? 29  ILE C CG1 1 
ATOM   4101  C CG2 . ILE C 1 21  ? -24.581 37.481  23.758  1.00 60.53  ? 29  ILE C CG2 1 
ATOM   4102  C CD1 . ILE C 1 21  ? -20.858 37.898  23.871  1.00 46.90  ? 29  ILE C CD1 1 
ATOM   4103  N N   . MET C 1 22  ? -25.527 40.560  24.350  1.00 50.90  ? 30  MET C N   1 
ATOM   4104  C CA  . MET C 1 22  ? -26.178 41.519  23.472  1.00 53.37  ? 30  MET C CA  1 
ATOM   4105  C C   . MET C 1 22  ? -26.871 42.663  24.205  1.00 51.05  ? 30  MET C C   1 
ATOM   4106  O O   . MET C 1 22  ? -27.279 43.631  23.553  1.00 47.31  ? 30  MET C O   1 
ATOM   4107  C CB  . MET C 1 22  ? -27.198 40.800  22.577  1.00 49.12  ? 30  MET C CB  1 
ATOM   4108  C CG  . MET C 1 22  ? -26.572 40.171  21.347  1.00 53.09  ? 30  MET C CG  1 
ATOM   4109  S SD  . MET C 1 22  ? -27.777 39.892  20.047  1.00 69.19  ? 30  MET C SD  1 
ATOM   4110  C CE  . MET C 1 22  ? -28.747 38.587  20.783  1.00 65.10  ? 30  MET C CE  1 
ATOM   4111  N N   . GLU C 1 23  ? -27.018 42.585  25.525  1.00 46.92  ? 31  GLU C N   1 
ATOM   4112  C CA  . GLU C 1 23  ? -27.712 43.615  26.287  1.00 53.36  ? 31  GLU C CA  1 
ATOM   4113  C C   . GLU C 1 23  ? -26.965 43.878  27.583  1.00 48.05  ? 31  GLU C C   1 
ATOM   4114  O O   . GLU C 1 23  ? -26.328 42.984  28.144  1.00 51.01  ? 31  GLU C O   1 
ATOM   4115  C CB  . GLU C 1 23  ? -29.167 43.217  26.604  1.00 54.89  ? 31  GLU C CB  1 
ATOM   4116  C CG  . GLU C 1 23  ? -30.210 43.811  25.667  1.00 53.69  ? 31  GLU C CG  1 
ATOM   4117  C CD  . GLU C 1 23  ? -31.598 43.898  26.298  1.00 84.12  ? 31  GLU C CD  1 
ATOM   4118  O OE1 . GLU C 1 23  ? -31.870 44.886  27.017  1.00 74.03  ? 31  GLU C OE1 1 
ATOM   4119  O OE2 . GLU C 1 23  ? -32.422 42.983  26.067  1.00 70.38  ? 31  GLU C OE2 1 
ATOM   4120  N N   . LYS C 1 24  ? -27.077 45.109  28.073  1.00 54.43  ? 32  LYS C N   1 
ATOM   4121  C CA  . LYS C 1 24  ? -26.435 45.515  29.311  1.00 55.19  ? 32  LYS C CA  1 
ATOM   4122  C C   . LYS C 1 24  ? -27.480 46.001  30.305  1.00 52.89  ? 32  LYS C C   1 
ATOM   4123  O O   . LYS C 1 24  ? -28.551 46.481  29.919  1.00 49.65  ? 32  LYS C O   1 
ATOM   4124  C CB  . LYS C 1 24  ? -25.397 46.616  29.063  1.00 53.59  ? 32  LYS C CB  1 
ATOM   4125  C CG  . LYS C 1 24  ? -24.233 46.171  28.195  1.00 57.77  ? 32  LYS C CG  1 
ATOM   4126  C CD  . LYS C 1 24  ? -23.076 47.154  28.264  1.00 58.30  ? 32  LYS C CD  1 
ATOM   4127  C CE  . LYS C 1 24  ? -21.763 46.475  27.913  1.00 54.05  ? 32  LYS C CE  1 
ATOM   4128  N NZ  . LYS C 1 24  ? -21.653 46.233  26.444  1.00 60.43  ? 32  LYS C NZ  1 
ATOM   4129  N N   . ASN C 1 25  ? -27.157 45.850  31.590  1.00 52.16  ? 33  ASN C N   1 
ATOM   4130  C CA  . ASN C 1 25  ? -27.974 46.344  32.699  1.00 56.64  ? 33  ASN C CA  1 
ATOM   4131  C C   . ASN C 1 25  ? -29.430 45.891  32.554  1.00 51.20  ? 33  ASN C C   1 
ATOM   4132  O O   . ASN C 1 25  ? -30.360 46.693  32.452  1.00 49.73  ? 33  ASN C O   1 
ATOM   4133  C CB  . ASN C 1 25  ? -27.867 47.870  32.818  1.00 49.24  ? 33  ASN C CB  1 
ATOM   4134  C CG  . ASN C 1 25  ? -26.578 48.320  33.511  1.00 77.95  ? 33  ASN C CG  1 
ATOM   4135  O OD1 . ASN C 1 25  ? -25.519 47.712  33.346  1.00 75.12  ? 33  ASN C OD1 1 
ATOM   4136  N ND2 . ASN C 1 25  ? -26.671 49.391  34.296  1.00 98.01  ? 33  ASN C ND2 1 
ATOM   4137  N N   . VAL C 1 26  ? -29.607 44.571  32.546  1.00 56.37  ? 34  VAL C N   1 
ATOM   4138  C CA  . VAL C 1 26  ? -30.919 43.942  32.420  1.00 50.38  ? 34  VAL C CA  1 
ATOM   4139  C C   . VAL C 1 26  ? -31.366 43.497  33.805  1.00 45.58  ? 34  VAL C C   1 
ATOM   4140  O O   . VAL C 1 26  ? -30.666 42.726  34.471  1.00 48.81  ? 34  VAL C O   1 
ATOM   4141  C CB  . VAL C 1 26  ? -30.883 42.748  31.453  1.00 45.90  ? 34  VAL C CB  1 
ATOM   4142  C CG1 . VAL C 1 26  ? -32.136 41.911  31.611  1.00 43.28  ? 34  VAL C CG1 1 
ATOM   4143  C CG2 . VAL C 1 26  ? -30.736 43.218  30.017  1.00 50.35  ? 34  VAL C CG2 1 
ATOM   4144  N N   . THR C 1 27  ? -32.529 43.977  34.240  1.00 43.20  ? 35  THR C N   1 
ATOM   4145  C CA  . THR C 1 27  ? -33.038 43.632  35.561  1.00 43.96  ? 35  THR C CA  1 
ATOM   4146  C C   . THR C 1 27  ? -33.677 42.248  35.532  1.00 45.32  ? 35  THR C C   1 
ATOM   4147  O O   . THR C 1 27  ? -34.456 41.930  34.629  1.00 44.45  ? 35  THR C O   1 
ATOM   4148  C CB  . THR C 1 27  ? -34.045 44.679  36.035  1.00 47.16  ? 35  THR C CB  1 
ATOM   4149  O OG1 . THR C 1 27  ? -33.440 45.976  35.974  1.00 50.21  ? 35  THR C OG1 1 
ATOM   4150  C CG2 . THR C 1 27  ? -34.480 44.396  37.468  1.00 44.46  ? 35  THR C CG2 1 
ATOM   4151  N N   . VAL C 1 28  ? -33.341 41.424  36.525  1.00 36.62  ? 36  VAL C N   1 
ATOM   4152  C CA  . VAL C 1 28  ? -33.809 40.049  36.598  1.00 42.23  ? 36  VAL C CA  1 
ATOM   4153  C C   . VAL C 1 28  ? -34.433 39.812  37.968  1.00 46.04  ? 36  VAL C C   1 
ATOM   4154  O O   . VAL C 1 28  ? -34.197 40.556  38.922  1.00 45.64  ? 36  VAL C O   1 
ATOM   4155  C CB  . VAL C 1 28  ? -32.671 39.040  36.337  1.00 48.34  ? 36  VAL C CB  1 
ATOM   4156  C CG1 . VAL C 1 28  ? -32.270 39.063  34.868  1.00 44.24  ? 36  VAL C CG1 1 
ATOM   4157  C CG2 . VAL C 1 28  ? -31.475 39.361  37.220  1.00 49.09  ? 36  VAL C CG2 1 
ATOM   4158  N N   . THR C 1 29  ? -35.257 38.764  38.052  1.00 44.25  ? 37  THR C N   1 
ATOM   4159  C CA  . THR C 1 29  ? -35.923 38.448  39.310  1.00 49.19  ? 37  THR C CA  1 
ATOM   4160  C C   . THR C 1 29  ? -35.004 37.751  40.306  1.00 51.25  ? 37  THR C C   1 
ATOM   4161  O O   . THR C 1 29  ? -35.287 37.776  41.508  1.00 60.04  ? 37  THR C O   1 
ATOM   4162  C CB  . THR C 1 29  ? -37.163 37.584  39.060  1.00 41.55  ? 37  THR C CB  1 
ATOM   4163  O OG1 . THR C 1 29  ? -36.765 36.299  38.564  1.00 49.25  ? 37  THR C OG1 1 
ATOM   4164  C CG2 . THR C 1 29  ? -38.082 38.251  38.050  1.00 42.23  ? 37  THR C CG2 1 
ATOM   4165  N N   . HIS C 1 30  ? -33.918 37.135  39.843  1.00 47.96  ? 38  HIS C N   1 
ATOM   4166  C CA  . HIS C 1 30  ? -32.978 36.475  40.737  1.00 57.49  ? 38  HIS C CA  1 
ATOM   4167  C C   . HIS C 1 30  ? -31.647 36.313  40.017  1.00 50.39  ? 38  HIS C C   1 
ATOM   4168  O O   . HIS C 1 30  ? -31.603 36.165  38.792  1.00 46.48  ? 38  HIS C O   1 
ATOM   4169  C CB  . HIS C 1 30  ? -33.509 35.114  41.209  1.00 63.60  ? 38  HIS C CB  1 
ATOM   4170  C CG  . HIS C 1 30  ? -32.856 34.609  42.459  1.00 86.00  ? 38  HIS C CG  1 
ATOM   4171  N ND1 . HIS C 1 30  ? -32.319 35.449  43.412  1.00 81.30  ? 38  HIS C ND1 1 
ATOM   4172  C CD2 . HIS C 1 30  ? -32.657 33.348  42.914  1.00 92.94  ? 38  HIS C CD2 1 
ATOM   4173  C CE1 . HIS C 1 30  ? -31.816 34.728  44.398  1.00 81.57  ? 38  HIS C CE1 1 
ATOM   4174  N NE2 . HIS C 1 30  ? -32.008 33.451  44.121  1.00 84.91  ? 38  HIS C NE2 1 
ATOM   4175  N N   . ALA C 1 31  ? -30.564 36.337  40.790  1.00 56.46  ? 39  ALA C N   1 
ATOM   4176  C CA  . ALA C 1 31  ? -29.230 36.235  40.216  1.00 59.96  ? 39  ALA C CA  1 
ATOM   4177  C C   . ALA C 1 31  ? -28.272 35.664  41.250  1.00 45.88  ? 39  ALA C C   1 
ATOM   4178  O O   . ALA C 1 31  ? -28.522 35.713  42.457  1.00 58.31  ? 39  ALA C O   1 
ATOM   4179  C CB  . ALA C 1 31  ? -28.730 37.595  39.711  1.00 47.85  ? 39  ALA C CB  1 
ATOM   4180  N N   . GLN C 1 32  ? -27.165 35.120  40.755  1.00 49.43  ? 40  GLN C N   1 
ATOM   4181  C CA  . GLN C 1 32  ? -26.144 34.503  41.588  1.00 54.79  ? 40  GLN C CA  1 
ATOM   4182  C C   . GLN C 1 32  ? -24.771 34.982  41.140  1.00 47.45  ? 40  GLN C C   1 
ATOM   4183  O O   . GLN C 1 32  ? -24.486 35.024  39.940  1.00 49.22  ? 40  GLN C O   1 
ATOM   4184  C CB  . GLN C 1 32  ? -26.222 32.975  41.504  1.00 49.35  ? 40  GLN C CB  1 
ATOM   4185  C CG  . GLN C 1 32  ? -25.842 32.258  42.779  1.00 56.72  ? 40  GLN C CG  1 
ATOM   4186  C CD  . GLN C 1 32  ? -26.284 30.810  42.773  1.00 62.61  ? 40  GLN C CD  1 
ATOM   4187  O OE1 . GLN C 1 32  ? -25.472 29.897  42.936  1.00 68.08  ? 40  GLN C OE1 1 
ATOM   4188  N NE2 . GLN C 1 32  ? -27.581 30.591  42.580  1.00 68.82  ? 40  GLN C NE2 1 
ATOM   4189  N N   . ASP C 1 33  ? -23.923 35.340  42.103  1.00 54.44  ? 41  ASP C N   1 
ATOM   4190  C CA  . ASP C 1 33  ? -22.562 35.788  41.826  1.00 46.58  ? 41  ASP C CA  1 
ATOM   4191  C C   . ASP C 1 33  ? -21.602 34.624  42.041  1.00 41.84  ? 41  ASP C C   1 
ATOM   4192  O O   . ASP C 1 33  ? -21.580 34.024  43.121  1.00 46.94  ? 41  ASP C O   1 
ATOM   4193  C CB  . ASP C 1 33  ? -22.175 36.971  42.719  1.00 49.08  ? 41  ASP C CB  1 
ATOM   4194  C CG  . ASP C 1 33  ? -21.077 37.838  42.107  1.00 60.94  ? 41  ASP C CG  1 
ATOM   4195  O OD1 . ASP C 1 33  ? -20.247 37.303  41.340  1.00 61.12  ? 41  ASP C OD1 1 
ATOM   4196  O OD2 . ASP C 1 33  ? -21.041 39.056  42.393  1.00 58.98  ? 41  ASP C OD2 1 
ATOM   4197  N N   . ILE C 1 34  ? -20.809 34.311  41.017  1.00 45.18  ? 42  ILE C N   1 
ATOM   4198  C CA  . ILE C 1 34  ? -19.871 33.196  41.076  1.00 43.86  ? 42  ILE C CA  1 
ATOM   4199  C C   . ILE C 1 34  ? -18.443 33.667  41.347  1.00 54.09  ? 42  ILE C C   1 
ATOM   4200  O O   . ILE C 1 34  ? -17.508 32.860  41.313  1.00 47.15  ? 42  ILE C O   1 
ATOM   4201  C CB  . ILE C 1 34  ? -19.939 32.359  39.791  1.00 38.81  ? 42  ILE C CB  1 
ATOM   4202  C CG1 . ILE C 1 34  ? -19.661 33.240  38.571  1.00 49.26  ? 42  ILE C CG1 1 
ATOM   4203  C CG2 . ILE C 1 34  ? -21.295 31.703  39.667  1.00 37.09  ? 42  ILE C CG2 1 
ATOM   4204  C CD1 . ILE C 1 34  ? -19.431 32.470  37.282  1.00 44.15  ? 42  ILE C CD1 1 
ATOM   4205  N N   . LEU C 1 35  ? -18.256 34.953  41.625  1.00 61.15  ? 43  LEU C N   1 
ATOM   4206  C CA  . LEU C 1 35  ? -16.941 35.518  41.910  1.00 62.78  ? 43  LEU C CA  1 
ATOM   4207  C C   . LEU C 1 35  ? -16.802 35.696  43.417  1.00 57.27  ? 43  LEU C C   1 
ATOM   4208  O O   . LEU C 1 35  ? -17.494 36.525  44.015  1.00 51.23  ? 43  LEU C O   1 
ATOM   4209  C CB  . LEU C 1 35  ? -16.757 36.850  41.184  1.00 47.28  ? 43  LEU C CB  1 
ATOM   4210  C CG  . LEU C 1 35  ? -15.466 37.610  41.490  1.00 54.89  ? 43  LEU C CG  1 
ATOM   4211  C CD1 . LEU C 1 35  ? -14.275 36.844  40.965  1.00 45.20  ? 43  LEU C CD1 1 
ATOM   4212  C CD2 . LEU C 1 35  ? -15.507 39.007  40.895  1.00 56.99  ? 43  LEU C CD2 1 
ATOM   4213  N N   . GLU C 1 36  ? -15.909 34.920  44.029  1.00 51.89  ? 44  GLU C N   1 
ATOM   4214  C CA  . GLU C 1 36  ? -15.624 35.094  45.447  1.00 57.31  ? 44  GLU C CA  1 
ATOM   4215  C C   . GLU C 1 36  ? -14.921 36.428  45.677  1.00 61.54  ? 44  GLU C C   1 
ATOM   4216  O O   . GLU C 1 36  ? -13.957 36.761  44.982  1.00 57.68  ? 44  GLU C O   1 
ATOM   4217  C CB  . GLU C 1 36  ? -14.759 33.946  45.962  1.00 58.89  ? 44  GLU C CB  1 
ATOM   4218  C CG  . GLU C 1 36  ? -14.594 33.926  47.473  1.00 55.43  ? 44  GLU C CG  1 
ATOM   4219  C CD  . GLU C 1 36  ? -15.876 34.287  48.206  1.00 72.78  ? 44  GLU C CD  1 
ATOM   4220  O OE1 . GLU C 1 36  ? -16.879 33.551  48.058  1.00 68.12  ? 44  GLU C OE1 1 
ATOM   4221  O OE2 . GLU C 1 36  ? -15.881 35.306  48.932  1.00 62.84  ? 44  GLU C OE2 1 
ATOM   4222  N N   . LYS C 1 37  ? -15.409 37.192  46.656  1.00 63.32  ? 45  LYS C N   1 
ATOM   4223  C CA  . LYS C 1 37  ? -14.871 38.511  46.949  1.00 55.98  ? 45  LYS C CA  1 
ATOM   4224  C C   . LYS C 1 37  ? -14.544 38.728  48.419  1.00 56.41  ? 45  LYS C C   1 
ATOM   4225  O O   . LYS C 1 37  ? -14.017 39.792  48.763  1.00 65.27  ? 45  LYS C O   1 
ATOM   4226  C CB  . LYS C 1 37  ? -15.853 39.605  46.500  1.00 61.12  ? 45  LYS C CB  1 
ATOM   4227  C CG  . LYS C 1 37  ? -15.891 39.846  45.003  1.00 69.30  ? 45  LYS C CG  1 
ATOM   4228  C CD  . LYS C 1 37  ? -17.068 40.730  44.608  1.00 61.35  ? 45  LYS C CD  1 
ATOM   4229  C CE  . LYS C 1 37  ? -18.333 39.914  44.412  1.00 61.29  ? 45  LYS C CE  1 
ATOM   4230  N NZ  . LYS C 1 37  ? -18.970 39.548  45.708  1.00 82.34  ? 45  LYS C NZ  1 
ATOM   4231  N N   . THR C 1 38  ? -14.828 37.763  49.289  1.00 57.38  ? 46  THR C N   1 
ATOM   4232  C CA  . THR C 1 38  ? -14.708 37.944  50.728  1.00 59.94  ? 46  THR C CA  1 
ATOM   4233  C C   . THR C 1 38  ? -13.550 37.118  51.275  1.00 57.67  ? 46  THR C C   1 
ATOM   4234  O O   . THR C 1 38  ? -13.372 35.952  50.905  1.00 53.09  ? 46  THR C O   1 
ATOM   4235  C CB  . THR C 1 38  ? -16.011 37.559  51.447  1.00 48.27  ? 46  THR C CB  1 
ATOM   4236  O OG1 . THR C 1 38  ? -16.187 36.136  51.410  1.00 61.64  ? 46  THR C OG1 1 
ATOM   4237  C CG2 . THR C 1 38  ? -17.214 38.225  50.785  1.00 50.72  ? 46  THR C CG2 1 
ATOM   4238  N N   . HIS C 1 39  ? -12.762 37.735  52.153  1.00 62.21  ? 47  HIS C N   1 
ATOM   4239  C CA  . HIS C 1 39  ? -11.720 37.053  52.904  1.00 60.84  ? 47  HIS C CA  1 
ATOM   4240  C C   . HIS C 1 39  ? -11.852 37.427  54.372  1.00 62.98  ? 47  HIS C C   1 
ATOM   4241  O O   . HIS C 1 39  ? -12.312 38.523  54.706  1.00 59.15  ? 47  HIS C O   1 
ATOM   4242  C CB  . HIS C 1 39  ? -10.320 37.412  52.387  1.00 59.99  ? 47  HIS C CB  1 
ATOM   4243  C CG  . HIS C 1 39  ? -10.010 38.875  52.447  1.00 54.66  ? 47  HIS C CG  1 
ATOM   4244  N ND1 . HIS C 1 39  ? -9.334  39.449  53.502  1.00 49.20  ? 47  HIS C ND1 1 
ATOM   4245  C CD2 . HIS C 1 39  ? -10.280 39.881  51.582  1.00 54.51  ? 47  HIS C CD2 1 
ATOM   4246  C CE1 . HIS C 1 39  ? -9.203  40.746  53.286  1.00 54.39  ? 47  HIS C CE1 1 
ATOM   4247  N NE2 . HIS C 1 39  ? -9.769  41.034  52.128  1.00 60.66  ? 47  HIS C NE2 1 
ATOM   4248  N N   . ASN C 1 40  ? -11.447 36.508  55.253  1.00 46.73  ? 48  ASN C N   1 
ATOM   4249  C CA  . ASN C 1 40  ? -11.608 36.736  56.686  1.00 58.18  ? 48  ASN C CA  1 
ATOM   4250  C C   . ASN C 1 40  ? -10.584 37.710  57.265  1.00 63.71  ? 48  ASN C C   1 
ATOM   4251  O O   . ASN C 1 40  ? -10.724 38.106  58.427  1.00 68.62  ? 48  ASN C O   1 
ATOM   4252  C CB  . ASN C 1 40  ? -11.552 35.405  57.446  1.00 56.35  ? 48  ASN C CB  1 
ATOM   4253  C CG  . ASN C 1 40  ? -10.182 34.756  57.407  1.00 53.23  ? 48  ASN C CG  1 
ATOM   4254  O OD1 . ASN C 1 40  ? -9.263  35.241  56.748  1.00 55.70  ? 48  ASN C OD1 1 
ATOM   4255  N ND2 . ASN C 1 40  ? -10.048 33.633  58.102  1.00 50.55  ? 48  ASN C ND2 1 
ATOM   4256  N N   . GLY C 1 41  ? -9.563  38.091  56.502  1.00 59.85  ? 49  GLY C N   1 
ATOM   4257  C CA  . GLY C 1 41  ? -8.613  39.083  56.969  1.00 59.50  ? 49  GLY C CA  1 
ATOM   4258  C C   . GLY C 1 41  ? -7.621  38.620  58.016  1.00 58.67  ? 49  GLY C C   1 
ATOM   4259  O O   . GLY C 1 41  ? -7.087  39.455  58.748  1.00 60.13  ? 49  GLY C O   1 
ATOM   4260  N N   . ARG C 1 42  ? -7.347  37.318  58.108  1.00 52.25  ? 50  ARG C N   1 
ATOM   4261  C CA  . ARG C 1 42  ? -6.397  36.814  59.090  1.00 61.64  ? 50  ARG C CA  1 
ATOM   4262  C C   . ARG C 1 42  ? -5.644  35.619  58.513  1.00 69.45  ? 50  ARG C C   1 
ATOM   4263  O O   . ARG C 1 42  ? -6.050  35.030  57.508  1.00 56.53  ? 50  ARG C O   1 
ATOM   4264  C CB  . ARG C 1 42  ? -7.094  36.437  60.402  1.00 67.09  ? 50  ARG C CB  1 
ATOM   4265  C CG  . ARG C 1 42  ? -8.378  35.650  60.228  1.00 67.34  ? 50  ARG C CG  1 
ATOM   4266  C CD  . ARG C 1 42  ? -8.874  35.116  61.562  1.00 71.98  ? 50  ARG C CD  1 
ATOM   4267  N NE  . ARG C 1 42  ? -10.012 35.870  62.074  1.00 71.76  ? 50  ARG C NE  1 
ATOM   4268  C CZ  . ARG C 1 42  ? -10.498 35.747  63.301  1.00 76.74  ? 50  ARG C CZ  1 
ATOM   4269  N NH1 . ARG C 1 42  ? -9.959  34.915  64.178  1.00 63.63  ? 50  ARG C NH1 1 
ATOM   4270  N NH2 . ARG C 1 42  ? -11.551 36.477  63.659  1.00 77.39  ? 50  ARG C NH2 1 
ATOM   4271  N N   . LEU C 1 43  ? -4.523  35.281  59.155  1.00 56.94  ? 51  LEU C N   1 
ATOM   4272  C CA  . LEU C 1 43  ? -3.679  34.170  58.723  1.00 56.62  ? 51  LEU C CA  1 
ATOM   4273  C C   . LEU C 1 43  ? -4.054  32.908  59.488  1.00 55.11  ? 51  LEU C C   1 
ATOM   4274  O O   . LEU C 1 43  ? -4.138  32.923  60.720  1.00 63.23  ? 51  LEU C O   1 
ATOM   4275  C CB  . LEU C 1 43  ? -2.200  34.490  58.934  1.00 66.78  ? 51  LEU C CB  1 
ATOM   4276  C CG  . LEU C 1 43  ? -1.653  35.735  58.233  1.00 75.03  ? 51  LEU C CG  1 
ATOM   4277  C CD1 . LEU C 1 43  ? -0.253  36.048  58.728  1.00 73.43  ? 51  LEU C CD1 1 
ATOM   4278  C CD2 . LEU C 1 43  ? -1.661  35.562  56.719  1.00 73.36  ? 51  LEU C CD2 1 
ATOM   4279  N N   . CYS C 1 44  ? -4.256  31.815  58.759  1.00 60.80  ? 52  CYS C N   1 
ATOM   4280  C CA  . CYS C 1 44  ? -4.882  30.616  59.293  1.00 61.62  ? 52  CYS C CA  1 
ATOM   4281  C C   . CYS C 1 44  ? -3.965  29.416  59.131  1.00 50.84  ? 52  CYS C C   1 
ATOM   4282  O O   . CYS C 1 44  ? -2.912  29.486  58.492  1.00 53.16  ? 52  CYS C O   1 
ATOM   4283  C CB  . CYS C 1 44  ? -6.217  30.338  58.586  1.00 55.84  ? 52  CYS C CB  1 
ATOM   4284  S SG  . CYS C 1 44  ? -7.464  31.637  58.760  1.00 71.67  ? 52  CYS C SG  1 
ATOM   4285  N N   . ASP C 1 45  ? -4.383  28.302  59.729  1.00 64.07  ? 53  ASP C N   1 
ATOM   4286  C CA  . ASP C 1 45  ? -3.790  27.013  59.415  1.00 56.77  ? 53  ASP C CA  1 
ATOM   4287  C C   . ASP C 1 45  ? -4.188  26.592  58.004  1.00 53.18  ? 53  ASP C C   1 
ATOM   4288  O O   . ASP C 1 45  ? -5.210  27.023  57.464  1.00 62.20  ? 53  ASP C O   1 
ATOM   4289  C CB  . ASP C 1 45  ? -4.239  25.940  60.409  1.00 63.28  ? 53  ASP C CB  1 
ATOM   4290  C CG  . ASP C 1 45  ? -3.978  26.328  61.853  1.00 75.65  ? 53  ASP C CG  1 
ATOM   4291  O OD1 . ASP C 1 45  ? -3.325  27.366  62.088  1.00 77.05  ? 53  ASP C OD1 1 
ATOM   4292  O OD2 . ASP C 1 45  ? -4.426  25.585  62.754  1.00 74.23  ? 53  ASP C OD2 1 
ATOM   4293  N N   . LEU C 1 46  ? -3.362  25.746  57.402  1.00 57.13  ? 54  LEU C N   1 
ATOM   4294  C CA  . LEU C 1 46  ? -3.631  25.198  56.078  1.00 52.26  ? 54  LEU C CA  1 
ATOM   4295  C C   . LEU C 1 46  ? -3.836  23.699  56.228  1.00 59.21  ? 54  LEU C C   1 
ATOM   4296  O O   . LEU C 1 46  ? -2.886  22.965  56.533  1.00 54.41  ? 54  LEU C O   1 
ATOM   4297  C CB  . LEU C 1 46  ? -2.496  25.509  55.103  1.00 49.20  ? 54  LEU C CB  1 
ATOM   4298  C CG  . LEU C 1 46  ? -2.786  25.101  53.656  1.00 57.59  ? 54  LEU C CG  1 
ATOM   4299  C CD1 . LEU C 1 46  ? -3.549  26.200  52.929  1.00 51.46  ? 54  LEU C CD1 1 
ATOM   4300  C CD2 . LEU C 1 46  ? -1.499  24.751  52.923  1.00 63.63  ? 54  LEU C CD2 1 
ATOM   4301  N N   . ASN C 1 47  ? -5.078  23.254  56.014  1.00 57.47  ? 55  ASN C N   1 
ATOM   4302  C CA  . ASN C 1 47  ? -5.462  21.850  56.172  1.00 53.64  ? 55  ASN C CA  1 
ATOM   4303  C C   . ASN C 1 47  ? -5.102  21.332  57.562  1.00 61.29  ? 55  ASN C C   1 
ATOM   4304  O O   . ASN C 1 47  ? -4.577  20.227  57.717  1.00 61.34  ? 55  ASN C O   1 
ATOM   4305  C CB  . ASN C 1 47  ? -4.839  20.980  55.080  1.00 52.04  ? 55  ASN C CB  1 
ATOM   4306  C CG  . ASN C 1 47  ? -5.126  21.510  53.687  1.00 58.57  ? 55  ASN C CG  1 
ATOM   4307  O OD1 . ASN C 1 47  ? -6.277  21.756  53.327  1.00 56.46  ? 55  ASN C OD1 1 
ATOM   4308  N ND2 . ASN C 1 47  ? -4.074  21.695  52.895  1.00 55.24  ? 55  ASN C ND2 1 
ATOM   4309  N N   . GLY C 1 48  A -5.375  22.149  58.580  1.00 58.63  ? 55  GLY C N   1 
ATOM   4310  C CA  . GLY C 1 48  A -5.147  21.779  59.959  1.00 63.32  ? 55  GLY C CA  1 
ATOM   4311  C C   . GLY C 1 48  A -3.732  21.963  60.463  1.00 66.74  ? 55  GLY C C   1 
ATOM   4312  O O   . GLY C 1 48  A -3.476  21.678  61.640  1.00 66.72  ? 55  GLY C O   1 
ATOM   4313  N N   . VAL C 1 49  ? -2.807  22.429  59.625  1.00 63.98  ? 56  VAL C N   1 
ATOM   4314  C CA  . VAL C 1 49  ? -1.401  22.569  59.994  1.00 60.98  ? 56  VAL C CA  1 
ATOM   4315  C C   . VAL C 1 49  ? -1.080  24.052  60.110  1.00 59.94  ? 56  VAL C C   1 
ATOM   4316  O O   . VAL C 1 49  ? -1.261  24.814  59.151  1.00 63.19  ? 56  VAL C O   1 
ATOM   4317  C CB  . VAL C 1 49  ? -0.476  21.881  58.981  1.00 59.47  ? 56  VAL C CB  1 
ATOM   4318  C CG1 . VAL C 1 49  ? 0.951   21.838  59.512  1.00 58.69  ? 56  VAL C CG1 1 
ATOM   4319  C CG2 . VAL C 1 49  ? -0.980  20.483  58.679  1.00 50.42  ? 56  VAL C CG2 1 
ATOM   4320  N N   . LYS C 1 50  ? -0.598  24.458  61.281  1.00 62.84  ? 57  LYS C N   1 
ATOM   4321  C CA  . LYS C 1 50  ? -0.312  25.859  61.530  1.00 58.73  ? 57  LYS C CA  1 
ATOM   4322  C C   . LYS C 1 50  ? 0.888   26.310  60.696  1.00 55.04  ? 57  LYS C C   1 
ATOM   4323  O O   . LYS C 1 50  ? 1.776   25.513  60.389  1.00 58.27  ? 57  LYS C O   1 
ATOM   4324  C CB  . LYS C 1 50  ? -0.032  26.086  63.014  1.00 67.14  ? 57  LYS C CB  1 
ATOM   4325  C CG  . LYS C 1 50  ? -0.601  24.999  63.926  1.00 81.38  ? 57  LYS C CG  1 
ATOM   4326  C CD  . LYS C 1 50  ? -0.459  25.362  65.400  1.00 82.69  ? 57  LYS C CD  1 
ATOM   4327  C CE  . LYS C 1 50  ? -1.543  26.342  65.837  1.00 90.08  ? 57  LYS C CE  1 
ATOM   4328  N NZ  . LYS C 1 50  ? -2.915  25.786  65.685  1.00 78.62  ? 57  LYS C NZ  1 
ATOM   4329  N N   . PRO C 1 51  ? 0.930   27.576  60.301  1.00 44.03  ? 58  PRO C N   1 
ATOM   4330  C CA  . PRO C 1 51  ? 2.100   28.088  59.584  1.00 55.85  ? 58  PRO C CA  1 
ATOM   4331  C C   . PRO C 1 51  ? 3.248   28.393  60.539  1.00 55.10  ? 58  PRO C C   1 
ATOM   4332  O O   . PRO C 1 51  ? 3.126   28.312  61.761  1.00 58.03  ? 58  PRO C O   1 
ATOM   4333  C CB  . PRO C 1 51  ? 1.581   29.367  58.923  1.00 55.08  ? 58  PRO C CB  1 
ATOM   4334  C CG  . PRO C 1 51  ? 0.477   29.820  59.809  1.00 47.69  ? 58  PRO C CG  1 
ATOM   4335  C CD  . PRO C 1 51  ? -0.151  28.576  60.382  1.00 53.92  ? 58  PRO C CD  1 
ATOM   4336  N N   . LEU C 1 52  ? 4.383   28.743  59.947  1.00 57.12  ? 59  LEU C N   1 
ATOM   4337  C CA  . LEU C 1 52  ? 5.527   29.264  60.681  1.00 53.10  ? 59  LEU C CA  1 
ATOM   4338  C C   . LEU C 1 52  ? 5.524   30.778  60.526  1.00 63.49  ? 59  LEU C C   1 
ATOM   4339  O O   . LEU C 1 52  ? 5.567   31.287  59.400  1.00 67.33  ? 59  LEU C O   1 
ATOM   4340  C CB  . LEU C 1 52  ? 6.835   28.668  60.161  1.00 56.12  ? 59  LEU C CB  1 
ATOM   4341  C CG  . LEU C 1 52  ? 7.942   28.394  61.180  1.00 58.58  ? 59  LEU C CG  1 
ATOM   4342  C CD1 . LEU C 1 52  ? 9.149   27.763  60.507  1.00 58.04  ? 59  LEU C CD1 1 
ATOM   4343  C CD2 . LEU C 1 52  ? 8.339   29.660  61.911  1.00 63.27  ? 59  LEU C CD2 1 
ATOM   4344  N N   . ILE C 1 53  ? 5.467   31.493  61.645  1.00 58.68  ? 60  ILE C N   1 
ATOM   4345  C CA  . ILE C 1 53  ? 5.396   32.950  61.644  1.00 57.58  ? 60  ILE C CA  1 
ATOM   4346  C C   . ILE C 1 53  ? 6.636   33.492  62.341  1.00 59.11  ? 60  ILE C C   1 
ATOM   4347  O O   . ILE C 1 53  ? 6.866   33.210  63.524  1.00 60.16  ? 60  ILE C O   1 
ATOM   4348  C CB  . ILE C 1 53  ? 4.115   33.457  62.324  1.00 58.74  ? 60  ILE C CB  1 
ATOM   4349  C CG1 . ILE C 1 53  ? 2.883   32.870  61.627  1.00 59.85  ? 60  ILE C CG1 1 
ATOM   4350  C CG2 . ILE C 1 53  ? 4.083   34.979  62.327  1.00 50.94  ? 60  ILE C CG2 1 
ATOM   4351  C CD1 . ILE C 1 53  ? 1.624   33.710  61.752  1.00 57.93  ? 60  ILE C CD1 1 
ATOM   4352  N N   . LEU C 1 54  ? 7.432   34.268  61.611  1.00 64.31  ? 61  LEU C N   1 
ATOM   4353  C CA  . LEU C 1 54  ? 8.613   34.927  62.152  1.00 71.88  ? 61  LEU C CA  1 
ATOM   4354  C C   . LEU C 1 54  ? 8.307   36.412  62.288  1.00 70.87  ? 61  LEU C C   1 
ATOM   4355  O O   . LEU C 1 54  ? 8.074   37.096  61.285  1.00 82.07  ? 61  LEU C O   1 
ATOM   4356  C CB  . LEU C 1 54  ? 9.827   34.699  61.252  1.00 65.21  ? 61  LEU C CB  1 
ATOM   4357  C CG  . LEU C 1 54  ? 9.964   33.286  60.676  1.00 61.58  ? 61  LEU C CG  1 
ATOM   4358  C CD1 . LEU C 1 54  ? 10.697  33.309  59.344  1.00 58.94  ? 61  LEU C CD1 1 
ATOM   4359  C CD2 . LEU C 1 54  ? 10.671  32.367  61.662  1.00 59.68  ? 61  LEU C CD2 1 
ATOM   4360  N N   . LYS C 1 55  ? 8.304   36.908  63.525  1.00 80.18  ? 62  LYS C N   1 
ATOM   4361  C CA  . LYS C 1 55  ? 7.888   38.288  63.749  1.00 89.96  ? 62  LYS C CA  1 
ATOM   4362  C C   . LYS C 1 55  ? 8.982   39.273  63.350  1.00 93.28  ? 62  LYS C C   1 
ATOM   4363  O O   . LYS C 1 55  ? 8.796   40.083  62.443  1.00 88.10  ? 62  LYS C O   1 
ATOM   4364  C CB  . LYS C 1 55  ? 7.482   38.492  65.210  1.00 90.89  ? 62  LYS C CB  1 
ATOM   4365  C CG  . LYS C 1 55  ? 6.000   38.289  65.471  1.00 83.13  ? 62  LYS C CG  1 
ATOM   4366  C CD  . LYS C 1 55  ? 5.751   36.941  66.117  1.00 74.18  ? 62  LYS C CD  1 
ATOM   4367  C CE  . LYS C 1 55  ? 6.586   36.789  67.381  1.00 96.97  ? 62  LYS C CE  1 
ATOM   4368  N NZ  . LYS C 1 55  ? 6.618   35.384  67.876  1.00 108.93 ? 62  LYS C NZ  1 
ATOM   4369  N N   . ASP C 1 56  ? 10.133  39.229  64.009  1.00 88.42  ? 63  ASP C N   1 
ATOM   4370  C CA  . ASP C 1 56  ? 11.207  40.139  63.646  1.00 90.55  ? 63  ASP C CA  1 
ATOM   4371  C C   . ASP C 1 56  ? 12.347  39.444  62.927  1.00 82.50  ? 63  ASP C C   1 
ATOM   4372  O O   . ASP C 1 56  ? 13.358  40.086  62.625  1.00 85.83  ? 63  ASP C O   1 
ATOM   4373  C CB  . ASP C 1 56  ? 11.739  40.864  64.885  1.00 100.22 ? 63  ASP C CB  1 
ATOM   4374  C CG  . ASP C 1 56  ? 10.724  41.815  65.481  1.00 106.53 ? 63  ASP C CG  1 
ATOM   4375  O OD1 . ASP C 1 56  ? 11.142  42.817  66.101  1.00 105.64 ? 63  ASP C OD1 1 
ATOM   4376  O OD2 . ASP C 1 56  ? 9.509   41.569  65.324  1.00 108.27 ? 63  ASP C OD2 1 
ATOM   4377  N N   . CYS C 1 57  ? 12.203  38.167  62.617  1.00 72.02  ? 64  CYS C N   1 
ATOM   4378  C CA  . CYS C 1 57  ? 13.330  37.359  62.201  1.00 78.63  ? 64  CYS C CA  1 
ATOM   4379  C C   . CYS C 1 57  ? 13.157  36.950  60.743  1.00 75.19  ? 64  CYS C C   1 
ATOM   4380  O O   . CYS C 1 57  ? 12.038  36.871  60.231  1.00 63.31  ? 64  CYS C O   1 
ATOM   4381  C CB  . CYS C 1 57  ? 13.448  36.127  63.102  1.00 75.28  ? 64  CYS C CB  1 
ATOM   4382  S SG  . CYS C 1 57  ? 15.077  35.381  63.135  1.00 111.52 ? 64  CYS C SG  1 
ATOM   4383  N N   . SER C 1 58  ? 14.277  36.738  60.066  1.00 74.52  ? 65  SER C N   1 
ATOM   4384  C CA  . SER C 1 58  ? 14.278  36.144  58.740  1.00 59.35  ? 65  SER C CA  1 
ATOM   4385  C C   . SER C 1 58  ? 14.595  34.659  58.859  1.00 50.69  ? 65  SER C C   1 
ATOM   4386  O O   . SER C 1 58  ? 14.960  34.165  59.927  1.00 64.86  ? 65  SER C O   1 
ATOM   4387  C CB  . SER C 1 58  ? 15.291  36.843  57.832  1.00 59.79  ? 65  SER C CB  1 
ATOM   4388  O OG  . SER C 1 58  ? 16.595  36.335  58.062  1.00 71.68  ? 65  SER C OG  1 
ATOM   4389  N N   . VAL C 1 59  ? 14.445  33.941  57.745  1.00 59.40  ? 66  VAL C N   1 
ATOM   4390  C CA  . VAL C 1 59  ? 14.716  32.506  57.761  1.00 55.09  ? 66  VAL C CA  1 
ATOM   4391  C C   . VAL C 1 59  ? 16.176  32.248  58.118  1.00 58.19  ? 66  VAL C C   1 
ATOM   4392  O O   . VAL C 1 59  ? 16.492  31.331  58.888  1.00 54.18  ? 66  VAL C O   1 
ATOM   4393  C CB  . VAL C 1 59  ? 14.332  31.869  56.411  1.00 44.15  ? 66  VAL C CB  1 
ATOM   4394  C CG1 . VAL C 1 59  ? 14.685  30.385  56.389  1.00 40.62  ? 66  VAL C CG1 1 
ATOM   4395  C CG2 . VAL C 1 59  ? 12.851  32.060  56.141  1.00 55.54  ? 66  VAL C CG2 1 
ATOM   4396  N N   . ALA C 1 60  ? 17.085  33.066  57.583  1.00 57.81  ? 67  ALA C N   1 
ATOM   4397  C CA  . ALA C 1 60  ? 18.503  32.907  57.892  1.00 56.47  ? 67  ALA C CA  1 
ATOM   4398  C C   . ALA C 1 60  ? 18.770  33.114  59.379  1.00 59.80  ? 67  ALA C C   1 
ATOM   4399  O O   . ALA C 1 60  ? 19.447  32.301  60.019  1.00 52.77  ? 67  ALA C O   1 
ATOM   4400  C CB  . ALA C 1 60  ? 19.332  33.878  57.050  1.00 46.38  ? 67  ALA C CB  1 
ATOM   4401  N N   . GLY C 1 61  ? 18.226  34.190  59.954  1.00 58.75  ? 68  GLY C N   1 
ATOM   4402  C CA  . GLY C 1 61  ? 18.464  34.461  61.364  1.00 62.64  ? 68  GLY C CA  1 
ATOM   4403  C C   . GLY C 1 61  ? 17.871  33.405  62.277  1.00 67.06  ? 68  GLY C C   1 
ATOM   4404  O O   . GLY C 1 61  ? 18.506  32.983  63.247  1.00 68.36  ? 68  GLY C O   1 
ATOM   4405  N N   . TRP C 1 62  ? 16.648  32.963  61.979  1.00 62.05  ? 69  TRP C N   1 
ATOM   4406  C CA  . TRP C 1 62  ? 16.015  31.925  62.785  1.00 67.84  ? 69  TRP C CA  1 
ATOM   4407  C C   . TRP C 1 62  ? 16.813  30.626  62.731  1.00 58.20  ? 69  TRP C C   1 
ATOM   4408  O O   . TRP C 1 62  ? 17.004  29.962  63.756  1.00 60.92  ? 69  TRP C O   1 
ATOM   4409  C CB  . TRP C 1 62  ? 14.570  31.719  62.311  1.00 65.90  ? 69  TRP C CB  1 
ATOM   4410  C CG  . TRP C 1 62  ? 13.911  30.458  62.788  1.00 68.15  ? 69  TRP C CG  1 
ATOM   4411  C CD1 . TRP C 1 62  ? 13.546  30.152  64.069  1.00 73.58  ? 69  TRP C CD1 1 
ATOM   4412  C CD2 . TRP C 1 62  ? 13.529  29.335  61.984  1.00 71.63  ? 69  TRP C CD2 1 
ATOM   4413  N NE1 . TRP C 1 62  ? 12.966  28.905  64.111  1.00 73.27  ? 69  TRP C NE1 1 
ATOM   4414  C CE2 . TRP C 1 62  ? 12.944  28.383  62.844  1.00 68.93  ? 69  TRP C CE2 1 
ATOM   4415  C CE3 . TRP C 1 62  ? 13.626  29.042  60.619  1.00 61.64  ? 69  TRP C CE3 1 
ATOM   4416  C CZ2 . TRP C 1 62  ? 12.460  27.161  62.384  1.00 66.10  ? 69  TRP C CZ2 1 
ATOM   4417  C CZ3 . TRP C 1 62  ? 13.144  27.826  60.165  1.00 61.11  ? 69  TRP C CZ3 1 
ATOM   4418  C CH2 . TRP C 1 62  ? 12.569  26.902  61.045  1.00 62.02  ? 69  TRP C CH2 1 
ATOM   4419  N N   . LEU C 1 63  ? 17.305  30.259  61.544  1.00 63.89  ? 70  LEU C N   1 
ATOM   4420  C CA  . LEU C 1 63  ? 18.067  29.021  61.401  1.00 63.97  ? 70  LEU C CA  1 
ATOM   4421  C C   . LEU C 1 63  ? 19.395  29.092  62.145  1.00 65.31  ? 70  LEU C C   1 
ATOM   4422  O O   . LEU C 1 63  ? 19.733  28.188  62.918  1.00 69.41  ? 70  LEU C O   1 
ATOM   4423  C CB  . LEU C 1 63  ? 18.309  28.723  59.923  1.00 63.21  ? 70  LEU C CB  1 
ATOM   4424  C CG  . LEU C 1 63  ? 17.218  27.994  59.143  1.00 59.95  ? 70  LEU C CG  1 
ATOM   4425  C CD1 . LEU C 1 63  ? 17.754  27.627  57.770  1.00 56.46  ? 70  LEU C CD1 1 
ATOM   4426  C CD2 . LEU C 1 63  ? 16.740  26.760  59.895  1.00 54.25  ? 70  LEU C CD2 1 
ATOM   4427  N N   . LEU C 1 64  ? 20.169  30.155  61.915  1.00 63.08  ? 71  LEU C N   1 
ATOM   4428  C CA  . LEU C 1 64  ? 21.478  30.290  62.543  1.00 66.76  ? 71  LEU C CA  1 
ATOM   4429  C C   . LEU C 1 64  ? 21.399  30.711  64.002  1.00 73.12  ? 71  LEU C C   1 
ATOM   4430  O O   . LEU C 1 64  ? 22.411  30.634  64.707  1.00 69.02  ? 71  LEU C O   1 
ATOM   4431  C CB  . LEU C 1 64  ? 22.339  31.290  61.768  1.00 54.57  ? 71  LEU C CB  1 
ATOM   4432  C CG  . LEU C 1 64  ? 22.421  31.075  60.258  1.00 56.16  ? 71  LEU C CG  1 
ATOM   4433  C CD1 . LEU C 1 64  ? 22.887  32.341  59.576  1.00 53.37  ? 71  LEU C CD1 1 
ATOM   4434  C CD2 . LEU C 1 64  ? 23.345  29.909  59.924  1.00 59.56  ? 71  LEU C CD2 1 
ATOM   4435  N N   . GLY C 1 65  ? 20.232  31.134  64.476  1.00 71.08  ? 72  GLY C N   1 
ATOM   4436  C CA  . GLY C 1 65  ? 20.097  31.528  65.861  1.00 71.29  ? 72  GLY C CA  1 
ATOM   4437  C C   . GLY C 1 65  ? 20.582  32.937  66.121  1.00 64.09  ? 72  GLY C C   1 
ATOM   4438  O O   . GLY C 1 65  ? 21.510  33.148  66.907  1.00 76.18  ? 72  GLY C O   1 
ATOM   4439  N N   . ASN C 1 66  ? 19.970  33.906  65.458  1.00 65.14  ? 73  ASN C N   1 
ATOM   4440  C CA  . ASN C 1 66  ? 20.234  35.302  65.755  1.00 69.49  ? 73  ASN C CA  1 
ATOM   4441  C C   . ASN C 1 66  ? 19.804  35.582  67.190  1.00 77.97  ? 73  ASN C C   1 
ATOM   4442  O O   . ASN C 1 66  ? 18.645  35.315  67.544  1.00 75.43  ? 73  ASN C O   1 
ATOM   4443  C CB  . ASN C 1 66  ? 19.480  36.201  64.772  1.00 70.32  ? 73  ASN C CB  1 
ATOM   4444  C CG  . ASN C 1 66  ? 19.910  37.657  64.845  1.00 68.72  ? 73  ASN C CG  1 
ATOM   4445  O OD1 . ASN C 1 66  ? 19.986  38.243  65.923  1.00 70.80  ? 73  ASN C OD1 1 
ATOM   4446  N ND2 . ASN C 1 66  ? 20.170  38.255  63.688  1.00 67.51  ? 73  ASN C ND2 1 
ATOM   4447  N N   . PRO C 1 67  ? 20.696  36.083  68.048  1.00 87.26  ? 74  PRO C N   1 
ATOM   4448  C CA  . PRO C 1 67  ? 20.298  36.344  69.442  1.00 84.83  ? 74  PRO C CA  1 
ATOM   4449  C C   . PRO C 1 67  ? 19.147  37.327  69.567  1.00 86.43  ? 74  PRO C C   1 
ATOM   4450  O O   . PRO C 1 67  ? 18.323  37.188  70.480  1.00 91.49  ? 74  PRO C O   1 
ATOM   4451  C CB  . PRO C 1 67  ? 21.587  36.886  70.081  1.00 84.22  ? 74  PRO C CB  1 
ATOM   4452  C CG  . PRO C 1 67  ? 22.459  37.302  68.931  1.00 78.19  ? 74  PRO C CG  1 
ATOM   4453  C CD  . PRO C 1 67  ? 22.117  36.382  67.805  1.00 75.84  ? 74  PRO C CD  1 
ATOM   4454  N N   . MET C 1 68  ? 19.062  38.313  68.668  1.00 85.04  ? 75  MET C N   1 
ATOM   4455  C CA  . MET C 1 68  ? 17.931  39.235  68.677  1.00 86.15  ? 75  MET C CA  1 
ATOM   4456  C C   . MET C 1 68  ? 16.625  38.516  68.362  1.00 90.94  ? 75  MET C C   1 
ATOM   4457  O O   . MET C 1 68  ? 15.562  38.911  68.857  1.00 91.37  ? 75  MET C O   1 
ATOM   4458  C CB  . MET C 1 68  ? 18.173  40.369  67.678  1.00 87.64  ? 75  MET C CB  1 
ATOM   4459  C CG  . MET C 1 68  ? 18.612  41.678  68.313  1.00 95.34  ? 75  MET C CG  1 
ATOM   4460  S SD  . MET C 1 68  ? 17.438  42.271  69.544  1.00 122.13 ? 75  MET C SD  1 
ATOM   4461  C CE  . MET C 1 68  ? 16.213  43.061  68.501  1.00 97.73  ? 75  MET C CE  1 
ATOM   4462  N N   . CYS C 1 69  ? 16.681  37.468  67.541  1.00 94.36  ? 76  CYS C N   1 
ATOM   4463  C CA  . CYS C 1 69  ? 15.507  36.645  67.266  1.00 100.43 ? 76  CYS C CA  1 
ATOM   4464  C C   . CYS C 1 69  ? 15.169  35.842  68.512  1.00 106.27 ? 76  CYS C C   1 
ATOM   4465  O O   . CYS C 1 69  ? 15.871  34.883  68.848  1.00 103.37 ? 76  CYS C O   1 
ATOM   4466  C CB  . CYS C 1 69  ? 15.764  35.714  66.084  1.00 82.65  ? 76  CYS C CB  1 
ATOM   4467  S SG  . CYS C 1 69  ? 16.041  36.539  64.502  1.00 86.89  ? 76  CYS C SG  1 
ATOM   4468  N N   . ASP C 1 70  ? 14.101  36.234  69.202  1.00 122.28 ? 77  ASP C N   1 
ATOM   4469  C CA  . ASP C 1 70  ? 13.671  35.500  70.383  1.00 121.39 ? 77  ASP C CA  1 
ATOM   4470  C C   . ASP C 1 70  ? 13.334  34.066  70.003  1.00 121.38 ? 77  ASP C C   1 
ATOM   4471  O O   . ASP C 1 70  ? 12.483  33.826  69.140  1.00 127.26 ? 77  ASP C O   1 
ATOM   4472  C CB  . ASP C 1 70  ? 12.464  36.187  71.024  1.00 119.69 ? 77  ASP C CB  1 
ATOM   4473  C CG  . ASP C 1 70  ? 11.487  36.737  69.996  1.00 124.08 ? 77  ASP C CG  1 
ATOM   4474  O OD1 . ASP C 1 70  ? 11.707  36.528  68.784  1.00 127.70 ? 77  ASP C OD1 1 
ATOM   4475  O OD2 . ASP C 1 70  ? 10.493  37.376  70.401  1.00 120.60 ? 77  ASP C OD2 1 
ATOM   4476  N N   . GLU C 1 71  ? 14.005  33.109  70.641  1.00 115.64 ? 78  GLU C N   1 
ATOM   4477  C CA  . GLU C 1 71  ? 13.733  31.709  70.349  1.00 109.47 ? 78  GLU C CA  1 
ATOM   4478  C C   . GLU C 1 71  ? 12.396  31.326  70.962  1.00 115.91 ? 78  GLU C C   1 
ATOM   4479  O O   . GLU C 1 71  ? 12.341  30.554  71.926  1.00 121.83 ? 78  GLU C O   1 
ATOM   4480  C CB  . GLU C 1 71  ? 14.855  30.808  70.874  1.00 100.19 ? 78  GLU C CB  1 
ATOM   4481  C CG  . GLU C 1 71  ? 14.923  29.440  70.197  1.00 108.02 ? 78  GLU C CG  1 
ATOM   4482  C CD  . GLU C 1 71  ? 14.131  28.374  70.934  1.00 117.41 ? 78  GLU C CD  1 
ATOM   4483  O OE1 . GLU C 1 71  ? 14.162  28.363  72.183  1.00 126.12 ? 78  GLU C OE1 1 
ATOM   4484  O OE2 . GLU C 1 71  ? 13.468  27.552  70.265  1.00 100.97 ? 78  GLU C OE2 1 
ATOM   4485  N N   . PHE C 1 72  ? 11.313  31.879  70.419  1.00 118.31 ? 79  PHE C N   1 
ATOM   4486  C CA  . PHE C 1 72  ? 9.978   31.562  70.901  1.00 127.72 ? 79  PHE C CA  1 
ATOM   4487  C C   . PHE C 1 72  ? 9.553   30.204  70.363  1.00 127.79 ? 79  PHE C C   1 
ATOM   4488  O O   . PHE C 1 72  ? 9.623   29.964  69.155  1.00 127.69 ? 79  PHE C O   1 
ATOM   4489  C CB  . PHE C 1 72  ? 8.983   32.649  70.486  1.00 121.70 ? 79  PHE C CB  1 
ATOM   4490  C CG  . PHE C 1 72  ? 8.970   33.839  71.406  1.00 128.20 ? 79  PHE C CG  1 
ATOM   4491  C CD1 . PHE C 1 72  ? 9.873   33.931  72.455  1.00 131.84 ? 79  PHE C CD1 1 
ATOM   4492  C CD2 . PHE C 1 72  ? 8.059   34.866  71.219  1.00 127.20 ? 79  PHE C CD2 1 
ATOM   4493  C CE1 . PHE C 1 72  ? 9.866   35.022  73.301  1.00 129.88 ? 79  PHE C CE1 1 
ATOM   4494  C CE2 . PHE C 1 72  ? 8.047   35.959  72.062  1.00 132.05 ? 79  PHE C CE2 1 
ATOM   4495  C CZ  . PHE C 1 72  ? 8.952   36.038  73.104  1.00 136.23 ? 79  PHE C CZ  1 
ATOM   4496  N N   . ILE C 1 73  ? 9.139   29.320  71.277  1.00 124.40 ? 80  ILE C N   1 
ATOM   4497  C CA  . ILE C 1 73  ? 8.615   27.969  71.057  1.00 116.16 ? 80  ILE C CA  1 
ATOM   4498  C C   . ILE C 1 73  ? 9.385   27.156  70.013  1.00 113.58 ? 80  ILE C C   1 
ATOM   4499  O O   . ILE C 1 73  ? 10.430  27.580  69.504  1.00 110.83 ? 80  ILE C O   1 
ATOM   4500  C CB  . ILE C 1 73  ? 7.092   27.996  70.758  1.00 109.41 ? 80  ILE C CB  1 
ATOM   4501  C CG1 . ILE C 1 73  ? 6.627   28.924  69.610  1.00 115.20 ? 80  ILE C CG1 1 
ATOM   4502  C CG2 . ILE C 1 73  ? 6.306   28.305  72.035  1.00 105.10 ? 80  ILE C CG2 1 
ATOM   4503  C CD1 . ILE C 1 73  ? 7.173   28.635  68.233  1.00 106.06 ? 80  ILE C CD1 1 
ATOM   4504  N N   . ARG C 1 74  ? 8.905   25.943  69.752  1.00 107.53 ? 81  ARG C N   1 
ATOM   4505  C CA  . ARG C 1 74  ? 9.498   25.050  68.757  1.00 99.64  ? 81  ARG C CA  1 
ATOM   4506  C C   . ARG C 1 74  ? 8.342   24.382  68.022  1.00 100.31 ? 81  ARG C C   1 
ATOM   4507  O O   . ARG C 1 74  ? 7.694   23.484  68.567  1.00 98.63  ? 81  ARG C O   1 
ATOM   4508  C CB  . ARG C 1 74  ? 10.420  24.019  69.401  1.00 88.61  ? 81  ARG C CB  1 
ATOM   4509  C CG  . ARG C 1 74  ? 11.365  23.317  68.428  1.00 106.99 ? 81  ARG C CG  1 
ATOM   4510  C CD  . ARG C 1 74  ? 11.978  24.292  67.433  1.00 109.18 ? 81  ARG C CD  1 
ATOM   4511  N NE  . ARG C 1 74  ? 12.884  25.236  68.077  1.00 109.53 ? 81  ARG C NE  1 
ATOM   4512  C CZ  . ARG C 1 74  ? 13.675  26.081  67.428  1.00 101.18 ? 81  ARG C CZ  1 
ATOM   4513  N NH1 . ARG C 1 74  ? 13.695  26.131  66.106  1.00 87.11  ? 81  ARG C NH1 1 
ATOM   4514  N NH2 . ARG C 1 74  ? 14.462  26.898  68.122  1.00 103.58 ? 81  ARG C NH2 1 
ATOM   4515  N N   . VAL C 1 75  ? 8.084   24.821  66.793  1.00 95.90  ? 82  VAL C N   1 
ATOM   4516  C CA  . VAL C 1 75  ? 7.005   24.241  65.998  1.00 84.99  ? 82  VAL C CA  1 
ATOM   4517  C C   . VAL C 1 75  ? 7.543   22.978  65.338  1.00 79.67  ? 82  VAL C C   1 
ATOM   4518  O O   . VAL C 1 75  ? 8.408   23.066  64.455  1.00 81.50  ? 82  VAL C O   1 
ATOM   4519  C CB  . VAL C 1 75  ? 6.479   25.231  64.948  1.00 80.30  ? 82  VAL C CB  1 
ATOM   4520  C CG1 . VAL C 1 75  ? 5.074   24.850  64.522  1.00 82.07  ? 82  VAL C CG1 1 
ATOM   4521  C CG2 . VAL C 1 75  ? 6.497   26.645  65.486  1.00 93.33  ? 82  VAL C CG2 1 
ATOM   4522  N N   . PRO C 1 76  ? 7.070   21.792  65.731  1.00 70.82  ? 83  PRO C N   1 
ATOM   4523  C CA  . PRO C 1 76  ? 7.602   20.559  65.127  1.00 62.53  ? 83  PRO C CA  1 
ATOM   4524  C C   . PRO C 1 76  ? 7.270   20.414  63.653  1.00 66.23  ? 83  PRO C C   1 
ATOM   4525  O O   . PRO C 1 76  ? 7.963   19.664  62.956  1.00 60.67  ? 83  PRO C O   1 
ATOM   4526  C CB  . PRO C 1 76  ? 6.964   19.434  65.957  1.00 65.43  ? 83  PRO C CB  1 
ATOM   4527  C CG  . PRO C 1 76  ? 5.993   20.078  66.890  1.00 74.83  ? 83  PRO C CG  1 
ATOM   4528  C CD  . PRO C 1 76  ? 5.968   21.552  66.676  1.00 69.59  ? 83  PRO C CD  1 
ATOM   4529  N N   . GLU C 1 77  A 6.245   21.104  63.154  1.00 60.49  ? 83  GLU C N   1 
ATOM   4530  C CA  . GLU C 1 77  A 5.883   21.026  61.744  1.00 58.35  ? 83  GLU C CA  1 
ATOM   4531  C C   . GLU C 1 77  A 5.068   22.255  61.375  1.00 62.42  ? 83  GLU C C   1 
ATOM   4532  O O   . GLU C 1 77  A 4.473   22.907  62.235  1.00 58.64  ? 83  GLU C O   1 
ATOM   4533  C CB  . GLU C 1 77  A 5.097   19.748  61.437  1.00 67.41  ? 83  GLU C CB  1 
ATOM   4534  C CG  . GLU C 1 77  A 3.591   19.893  61.582  1.00 67.25  ? 83  GLU C CG  1 
ATOM   4535  C CD  . GLU C 1 77  A 2.858   18.574  61.405  1.00 94.74  ? 83  GLU C CD  1 
ATOM   4536  O OE1 . GLU C 1 77  A 3.045   17.923  60.353  1.00 90.12  ? 83  GLU C OE1 1 
ATOM   4537  O OE2 . GLU C 1 77  A 2.092   18.190  62.315  1.00 90.12  ? 83  GLU C OE2 1 
ATOM   4538  N N   . TRP C 1 78  ? 5.040   22.559  60.078  1.00 56.14  ? 84  TRP C N   1 
ATOM   4539  C CA  . TRP C 1 78  ? 4.245   23.678  59.588  1.00 53.13  ? 84  TRP C CA  1 
ATOM   4540  C C   . TRP C 1 78  ? 3.903   23.445  58.122  1.00 57.37  ? 84  TRP C C   1 
ATOM   4541  O O   . TRP C 1 78  ? 4.494   22.591  57.455  1.00 51.99  ? 84  TRP C O   1 
ATOM   4542  C CB  . TRP C 1 78  ? 4.974   25.013  59.774  1.00 52.44  ? 84  TRP C CB  1 
ATOM   4543  C CG  . TRP C 1 78  ? 6.309   25.062  59.110  1.00 63.52  ? 84  TRP C CG  1 
ATOM   4544  C CD1 . TRP C 1 78  ? 6.572   25.456  57.833  1.00 63.82  ? 84  TRP C CD1 1 
ATOM   4545  C CD2 . TRP C 1 78  ? 7.571   24.699  59.686  1.00 58.97  ? 84  TRP C CD2 1 
ATOM   4546  N NE1 . TRP C 1 78  ? 7.919   25.364  57.576  1.00 56.58  ? 84  TRP C NE1 1 
ATOM   4547  C CE2 . TRP C 1 78  ? 8.554   24.900  58.697  1.00 62.30  ? 84  TRP C CE2 1 
ATOM   4548  C CE3 . TRP C 1 78  ? 7.965   24.225  60.942  1.00 61.20  ? 84  TRP C CE3 1 
ATOM   4549  C CZ2 . TRP C 1 78  ? 9.906   24.647  58.925  1.00 60.90  ? 84  TRP C CZ2 1 
ATOM   4550  C CZ3 . TRP C 1 78  ? 9.305   23.971  61.163  1.00 67.68  ? 84  TRP C CZ3 1 
ATOM   4551  C CH2 . TRP C 1 78  ? 10.259  24.183  60.160  1.00 61.71  ? 84  TRP C CH2 1 
ATOM   4552  N N   . SER C 1 79  ? 2.927   24.215  57.634  1.00 54.48  ? 85  SER C N   1 
ATOM   4553  C CA  . SER C 1 79  ? 2.448   24.115  56.259  1.00 51.03  ? 85  SER C CA  1 
ATOM   4554  C C   . SER C 1 79  ? 3.050   25.166  55.336  1.00 49.81  ? 85  SER C C   1 
ATOM   4555  O O   . SER C 1 79  ? 3.330   24.869  54.172  1.00 49.85  ? 85  SER C O   1 
ATOM   4556  C CB  . SER C 1 79  ? 0.920   24.223  56.222  1.00 51.81  ? 85  SER C CB  1 
ATOM   4557  O OG  . SER C 1 79  ? 0.483   25.445  56.788  1.00 60.16  ? 85  SER C OG  1 
ATOM   4558  N N   . TYR C 1 80  ? 3.252   26.387  55.824  1.00 50.56  ? 86  TYR C N   1 
ATOM   4559  C CA  . TYR C 1 80  ? 3.948   27.420  55.066  1.00 59.38  ? 86  TYR C CA  1 
ATOM   4560  C C   . TYR C 1 80  ? 4.619   28.376  56.044  1.00 59.69  ? 86  TYR C C   1 
ATOM   4561  O O   . TYR C 1 80  ? 4.376   28.331  57.253  1.00 59.82  ? 86  TYR C O   1 
ATOM   4562  C CB  . TYR C 1 80  ? 3.003   28.165  54.121  1.00 44.16  ? 86  TYR C CB  1 
ATOM   4563  C CG  . TYR C 1 80  ? 1.904   28.930  54.815  1.00 48.94  ? 86  TYR C CG  1 
ATOM   4564  C CD1 . TYR C 1 80  ? 0.799   28.272  55.350  1.00 44.80  ? 86  TYR C CD1 1 
ATOM   4565  C CD2 . TYR C 1 80  ? 1.956   30.311  54.916  1.00 46.36  ? 86  TYR C CD2 1 
ATOM   4566  C CE1 . TYR C 1 80  ? -0.209  28.969  55.983  1.00 36.26  ? 86  TYR C CE1 1 
ATOM   4567  C CE2 . TYR C 1 80  ? 0.944   31.021  55.539  1.00 53.22  ? 86  TYR C CE2 1 
ATOM   4568  C CZ  . TYR C 1 80  ? -0.132  30.345  56.073  1.00 41.39  ? 86  TYR C CZ  1 
ATOM   4569  O OH  . TYR C 1 80  ? -1.128  31.059  56.695  1.00 50.37  ? 86  TYR C OH  1 
ATOM   4570  N N   . ILE C 1 81  ? 5.472   29.246  55.508  1.00 49.25  ? 87  ILE C N   1 
ATOM   4571  C CA  . ILE C 1 81  ? 6.252   30.191  56.302  1.00 49.44  ? 87  ILE C CA  1 
ATOM   4572  C C   . ILE C 1 81  ? 5.784   31.606  55.989  1.00 56.46  ? 87  ILE C C   1 
ATOM   4573  O O   . ILE C 1 81  ? 5.588   31.958  54.818  1.00 54.33  ? 87  ILE C O   1 
ATOM   4574  C CB  . ILE C 1 81  ? 7.759   30.044  56.034  1.00 54.17  ? 87  ILE C CB  1 
ATOM   4575  C CG1 . ILE C 1 81  ? 8.244   28.662  56.471  1.00 49.41  ? 87  ILE C CG1 1 
ATOM   4576  C CG2 . ILE C 1 81  ? 8.537   31.133  56.751  1.00 51.75  ? 87  ILE C CG2 1 
ATOM   4577  C CD1 . ILE C 1 81  ? 9.744   28.570  56.625  1.00 54.43  ? 87  ILE C CD1 1 
ATOM   4578  N N   . VAL C 1 82  ? 5.610   32.414  57.034  1.00 65.23  ? 88  VAL C N   1 
ATOM   4579  C CA  . VAL C 1 82  ? 5.235   33.819  56.908  1.00 53.80  ? 88  VAL C CA  1 
ATOM   4580  C C   . VAL C 1 82  ? 6.426   34.684  57.299  1.00 61.28  ? 88  VAL C C   1 
ATOM   4581  O O   . VAL C 1 82  ? 6.978   34.540  58.397  1.00 60.65  ? 88  VAL C O   1 
ATOM   4582  C CB  . VAL C 1 82  ? 4.011   34.162  57.772  1.00 52.50  ? 88  VAL C CB  1 
ATOM   4583  C CG1 . VAL C 1 82  ? 3.353   35.440  57.271  1.00 45.32  ? 88  VAL C CG1 1 
ATOM   4584  C CG2 . VAL C 1 82  ? 3.023   33.004  57.763  1.00 70.13  ? 88  VAL C CG2 1 
ATOM   4585  N N   . GLU C 1 83  ? 6.814   35.584  56.401  1.00 63.37  ? 89  GLU C N   1 
ATOM   4586  C CA  . GLU C 1 83  ? 7.860   36.565  56.637  1.00 61.69  ? 89  GLU C CA  1 
ATOM   4587  C C   . GLU C 1 83  ? 7.293   37.953  56.390  1.00 61.23  ? 89  GLU C C   1 
ATOM   4588  O O   . GLU C 1 83  ? 6.367   38.123  55.593  1.00 62.68  ? 89  GLU C O   1 
ATOM   4589  C CB  . GLU C 1 83  ? 9.064   36.343  55.708  1.00 58.83  ? 89  GLU C CB  1 
ATOM   4590  C CG  . GLU C 1 83  ? 10.207  35.545  56.298  1.00 66.82  ? 89  GLU C CG  1 
ATOM   4591  C CD  . GLU C 1 83  ? 11.451  35.583  55.420  1.00 72.94  ? 89  GLU C CD  1 
ATOM   4592  O OE1 . GLU C 1 83  ? 11.342  35.982  54.238  1.00 75.27  ? 89  GLU C OE1 1 
ATOM   4593  O OE2 . GLU C 1 83  ? 12.539  35.212  55.910  1.00 63.57  ? 89  GLU C OE2 1 
ATOM   4594  N N   . ARG C 1 84  ? 7.846   38.952  57.070  1.00 68.48  ? 90  ARG C N   1 
ATOM   4595  C CA  . ARG C 1 84  ? 7.508   40.308  56.672  1.00 78.85  ? 90  ARG C CA  1 
ATOM   4596  C C   . ARG C 1 84  ? 8.285   40.696  55.422  1.00 78.38  ? 90  ARG C C   1 
ATOM   4597  O O   . ARG C 1 84  ? 9.249   40.037  55.020  1.00 73.37  ? 90  ARG C O   1 
ATOM   4598  C CB  . ARG C 1 84  ? 7.799   41.314  57.780  1.00 80.15  ? 90  ARG C CB  1 
ATOM   4599  C CG  . ARG C 1 84  ? 6.792   41.326  58.889  1.00 80.72  ? 90  ARG C CG  1 
ATOM   4600  C CD  . ARG C 1 84  ? 7.542   41.201  60.163  1.00 79.02  ? 90  ARG C CD  1 
ATOM   4601  N NE  . ARG C 1 84  ? 6.700   41.125  61.352  1.00 94.40  ? 90  ARG C NE  1 
ATOM   4602  C CZ  . ARG C 1 84  ? 6.469   42.131  62.186  1.00 99.88  ? 90  ARG C CZ  1 
ATOM   4603  N NH1 . ARG C 1 84  ? 6.997   43.328  61.991  1.00 94.45  ? 90  ARG C NH1 1 
ATOM   4604  N NH2 . ARG C 1 84  ? 5.700   41.924  63.251  1.00 95.70  ? 90  ARG C NH2 1 
ATOM   4605  N N   . THR C 1 85  ? 7.845   41.793  54.803  1.00 75.62  ? 91  THR C N   1 
ATOM   4606  C CA  . THR C 1 85  ? 8.516   42.274  53.604  1.00 67.92  ? 91  THR C CA  1 
ATOM   4607  C C   . THR C 1 85  ? 9.968   42.622  53.895  1.00 70.77  ? 91  THR C C   1 
ATOM   4608  O O   . THR C 1 85  ? 10.866  42.258  53.129  1.00 69.27  ? 91  THR C O   1 
ATOM   4609  C CB  . THR C 1 85  ? 7.770   43.482  53.039  1.00 67.04  ? 91  THR C CB  1 
ATOM   4610  O OG1 . THR C 1 85  ? 6.400   43.130  52.810  1.00 65.50  ? 91  THR C OG1 1 
ATOM   4611  C CG2 . THR C 1 85  ? 8.403   43.939  51.731  1.00 66.96  ? 91  THR C CG2 1 
ATOM   4612  N N   . ASN C 1 86  ? 10.220  43.307  55.010  1.00 71.63  ? 92  ASN C N   1 
ATOM   4613  C CA  . ASN C 1 86  ? 11.571  43.684  55.424  1.00 73.57  ? 92  ASN C CA  1 
ATOM   4614  C C   . ASN C 1 86  ? 11.758  43.316  56.889  1.00 71.37  ? 92  ASN C C   1 
ATOM   4615  O O   . ASN C 1 86  ? 11.473  44.123  57.785  1.00 73.27  ? 92  ASN C O   1 
ATOM   4616  C CB  . ASN C 1 86  ? 11.825  45.171  55.192  1.00 75.04  ? 92  ASN C CB  1 
ATOM   4617  C CG  . ASN C 1 86  ? 11.487  45.605  53.779  1.00 80.22  ? 92  ASN C CG  1 
ATOM   4618  O OD1 . ASN C 1 86  ? 12.298  45.462  52.861  1.00 74.04  ? 92  ASN C OD1 1 
ATOM   4619  N ND2 . ASN C 1 86  ? 10.281  46.135  53.596  1.00 83.37  ? 92  ASN C ND2 1 
ATOM   4620  N N   . PRO C 1 87  ? 12.231  42.105  57.174  1.00 70.36  ? 93  PRO C N   1 
ATOM   4621  C CA  . PRO C 1 87  ? 12.480  41.722  58.568  1.00 72.15  ? 93  PRO C CA  1 
ATOM   4622  C C   . PRO C 1 87  ? 13.650  42.499  59.154  1.00 75.18  ? 93  PRO C C   1 
ATOM   4623  O O   . PRO C 1 87  ? 14.510  43.025  58.443  1.00 75.23  ? 93  PRO C O   1 
ATOM   4624  C CB  . PRO C 1 87  ? 12.785  40.220  58.496  1.00 58.55  ? 93  PRO C CB  1 
ATOM   4625  C CG  . PRO C 1 87  ? 12.775  39.846  57.047  1.00 72.04  ? 93  PRO C CG  1 
ATOM   4626  C CD  . PRO C 1 87  ? 12.646  41.074  56.210  1.00 69.91  ? 93  PRO C CD  1 
ATOM   4627  N N   . ALA C 1 88  ? 13.665  42.572  60.486  1.00 71.39  ? 94  ALA C N   1 
ATOM   4628  C CA  . ALA C 1 88  ? 14.616  43.421  61.196  1.00 74.24  ? 94  ALA C CA  1 
ATOM   4629  C C   . ALA C 1 88  ? 15.929  42.716  61.517  1.00 74.96  ? 94  ALA C C   1 
ATOM   4630  O O   . ALA C 1 88  ? 16.996  43.332  61.422  1.00 80.53  ? 94  ALA C O   1 
ATOM   4631  C CB  . ALA C 1 88  ? 13.986  43.943  62.489  1.00 70.49  ? 94  ALA C CB  1 
ATOM   4632  N N   . ASN C 1 89  ? 15.883  41.444  61.902  1.00 65.48  ? 95  ASN C N   1 
ATOM   4633  C CA  . ASN C 1 89  ? 17.066  40.715  62.359  1.00 70.30  ? 95  ASN C CA  1 
ATOM   4634  C C   . ASN C 1 89  ? 17.317  39.538  61.421  1.00 74.78  ? 95  ASN C C   1 
ATOM   4635  O O   . ASN C 1 89  ? 16.855  38.423  61.673  1.00 73.12  ? 95  ASN C O   1 
ATOM   4636  C CB  . ASN C 1 89  ? 16.894  40.246  63.807  1.00 76.89  ? 95  ASN C CB  1 
ATOM   4637  C CG  . ASN C 1 89  ? 16.024  41.181  64.626  1.00 87.05  ? 95  ASN C CG  1 
ATOM   4638  O OD1 . ASN C 1 89  ? 14.989  40.777  65.159  1.00 74.12  ? 95  ASN C OD1 1 
ATOM   4639  N ND2 . ASN C 1 89  ? 16.446  42.438  64.738  1.00 81.20  ? 95  ASN C ND2 1 
ATOM   4640  N N   . ASP C 1 90  ? 18.054  39.791  60.337  1.00 81.67  ? 96  ASP C N   1 
ATOM   4641  C CA  . ASP C 1 90  ? 18.396  38.753  59.370  1.00 75.50  ? 96  ASP C CA  1 
ATOM   4642  C C   . ASP C 1 90  ? 19.783  38.167  59.623  1.00 68.42  ? 96  ASP C C   1 
ATOM   4643  O O   . ASP C 1 90  ? 19.912  36.992  59.979  1.00 78.36  ? 96  ASP C O   1 
ATOM   4644  C CB  . ASP C 1 90  ? 18.283  39.329  57.947  1.00 70.51  ? 96  ASP C CB  1 
ATOM   4645  C CG  . ASP C 1 90  ? 19.061  38.527  56.916  1.00 83.09  ? 96  ASP C CG  1 
ATOM   4646  O OD1 . ASP C 1 90  ? 18.470  37.608  56.308  1.00 88.58  ? 96  ASP C OD1 1 
ATOM   4647  O OD2 . ASP C 1 90  ? 20.251  38.833  56.693  1.00 80.68  ? 96  ASP C OD2 1 
ATOM   4648  N N   . LEU C 1 91  A 20.829  38.977  59.487  1.00 76.09  ? 96  LEU C N   1 
ATOM   4649  C CA  . LEU C 1 91  A 22.208  38.509  59.667  1.00 77.58  ? 96  LEU C CA  1 
ATOM   4650  C C   . LEU C 1 91  A 22.922  39.578  60.488  1.00 71.70  ? 96  LEU C C   1 
ATOM   4651  O O   . LEU C 1 91  A 23.424  40.561  59.936  1.00 69.25  ? 96  LEU C O   1 
ATOM   4652  C CB  . LEU C 1 91  A 22.901  38.258  58.332  1.00 70.70  ? 96  LEU C CB  1 
ATOM   4653  C CG  . LEU C 1 91  A 22.686  36.900  57.654  1.00 64.86  ? 96  LEU C CG  1 
ATOM   4654  C CD1 . LEU C 1 91  A 23.760  36.626  56.611  1.00 64.39  ? 96  LEU C CD1 1 
ATOM   4655  C CD2 . LEU C 1 91  A 22.662  35.793  58.685  1.00 69.92  ? 96  LEU C CD2 1 
ATOM   4656  N N   . CYS C 1 92  ? 22.949  39.383  61.810  1.00 71.16  ? 97  CYS C N   1 
ATOM   4657  C CA  . CYS C 1 92  ? 23.553  40.375  62.694  1.00 70.68  ? 97  CYS C CA  1 
ATOM   4658  C C   . CYS C 1 92  ? 25.008  40.628  62.320  1.00 73.96  ? 97  CYS C C   1 
ATOM   4659  O O   . CYS C 1 92  ? 25.449  41.781  62.255  1.00 71.16  ? 97  CYS C O   1 
ATOM   4660  C CB  . CYS C 1 92  ? 23.425  39.918  64.147  1.00 60.24  ? 97  CYS C CB  1 
ATOM   4661  S SG  . CYS C 1 92  ? 23.569  38.131  64.370  1.00 82.19  ? 97  CYS C SG  1 
ATOM   4662  N N   . TYR C 1 93  ? 25.763  39.566  62.053  1.00 70.46  ? 98  TYR C N   1 
ATOM   4663  C CA  . TYR C 1 93  ? 27.078  39.709  61.446  1.00 78.03  ? 98  TYR C CA  1 
ATOM   4664  C C   . TYR C 1 93  ? 26.935  39.633  59.934  1.00 66.09  ? 98  TYR C C   1 
ATOM   4665  O O   . TYR C 1 93  ? 26.445  38.619  59.423  1.00 65.62  ? 98  TYR C O   1 
ATOM   4666  C CB  . TYR C 1 93  ? 28.022  38.627  61.936  1.00 66.20  ? 98  TYR C CB  1 
ATOM   4667  C CG  . TYR C 1 93  ? 29.476  39.030  61.887  1.00 76.46  ? 98  TYR C CG  1 
ATOM   4668  C CD1 . TYR C 1 93  ? 30.152  39.126  60.677  1.00 73.93  ? 98  TYR C CD1 1 
ATOM   4669  C CD2 . TYR C 1 93  ? 30.177  39.314  63.051  1.00 80.97  ? 98  TYR C CD2 1 
ATOM   4670  C CE1 . TYR C 1 93  ? 31.488  39.495  60.628  1.00 77.77  ? 98  TYR C CE1 1 
ATOM   4671  C CE2 . TYR C 1 93  ? 31.512  39.680  63.014  1.00 76.12  ? 98  TYR C CE2 1 
ATOM   4672  C CZ  . TYR C 1 93  ? 32.162  39.771  61.800  1.00 80.81  ? 98  TYR C CZ  1 
ATOM   4673  O OH  . TYR C 1 93  ? 33.489  40.138  61.757  1.00 75.89  ? 98  TYR C OH  1 
ATOM   4674  N N   . PRO C 1 94  ? 27.353  40.656  59.190  1.00 72.33  ? 99  PRO C N   1 
ATOM   4675  C CA  . PRO C 1 94  ? 27.084  40.679  57.747  1.00 62.42  ? 99  PRO C CA  1 
ATOM   4676  C C   . PRO C 1 94  ? 27.734  39.508  57.023  1.00 72.65  ? 99  PRO C C   1 
ATOM   4677  O O   . PRO C 1 94  ? 28.758  38.971  57.448  1.00 70.06  ? 99  PRO C O   1 
ATOM   4678  C CB  . PRO C 1 94  ? 27.682  42.017  57.294  1.00 66.14  ? 99  PRO C CB  1 
ATOM   4679  C CG  . PRO C 1 94  ? 28.675  42.370  58.354  1.00 62.40  ? 99  PRO C CG  1 
ATOM   4680  C CD  . PRO C 1 94  ? 28.116  41.833  59.632  1.00 64.87  ? 99  PRO C CD  1 
ATOM   4681  N N   . GLY C 1 95  ? 27.100  39.105  55.926  1.00 60.70  ? 100 GLY C N   1 
ATOM   4682  C CA  . GLY C 1 95  ? 27.585  37.974  55.152  1.00 65.39  ? 100 GLY C CA  1 
ATOM   4683  C C   . GLY C 1 95  ? 26.525  37.472  54.193  1.00 68.50  ? 100 GLY C C   1 
ATOM   4684  O O   . GLY C 1 95  ? 25.647  38.229  53.757  1.00 59.41  ? 100 GLY C O   1 
ATOM   4685  N N   . ASN C 1 96  ? 26.613  36.187  53.872  1.00 65.06  ? 101 ASN C N   1 
ATOM   4686  C CA  . ASN C 1 96  ? 25.668  35.555  52.971  1.00 60.75  ? 101 ASN C CA  1 
ATOM   4687  C C   . ASN C 1 96  ? 25.322  34.177  53.497  1.00 55.13  ? 101 ASN C C   1 
ATOM   4688  O O   . ASN C 1 96  ? 26.085  33.560  54.244  1.00 59.42  ? 101 ASN C O   1 
ATOM   4689  C CB  . ASN C 1 96  ? 26.224  35.429  51.545  1.00 61.77  ? 101 ASN C CB  1 
ATOM   4690  C CG  . ASN C 1 96  ? 26.365  36.767  50.857  1.00 65.29  ? 101 ASN C CG  1 
ATOM   4691  O OD1 . ASN C 1 96  ? 27.467  37.294  50.730  1.00 68.73  ? 101 ASN C OD1 1 
ATOM   4692  N ND2 . ASN C 1 96  ? 25.246  37.325  50.407  1.00 81.95  ? 101 ASN C ND2 1 
ATOM   4693  N N   . LEU C 1 97  ? 24.147  33.705  53.100  1.00 51.69  ? 102 LEU C N   1 
ATOM   4694  C CA  . LEU C 1 97  ? 23.764  32.309  53.247  1.00 51.41  ? 102 LEU C CA  1 
ATOM   4695  C C   . LEU C 1 97  ? 23.681  31.711  51.849  1.00 55.60  ? 102 LEU C C   1 
ATOM   4696  O O   . LEU C 1 97  ? 22.910  32.193  51.013  1.00 58.78  ? 102 LEU C O   1 
ATOM   4697  C CB  . LEU C 1 97  ? 22.432  32.175  53.988  1.00 47.29  ? 102 LEU C CB  1 
ATOM   4698  C CG  . LEU C 1 97  ? 21.955  30.754  54.306  1.00 51.86  ? 102 LEU C CG  1 
ATOM   4699  C CD1 . LEU C 1 97  ? 23.104  29.867  54.762  1.00 43.32  ? 102 LEU C CD1 1 
ATOM   4700  C CD2 . LEU C 1 97  ? 20.853  30.781  55.351  1.00 51.89  ? 102 LEU C CD2 1 
ATOM   4701  N N   . ASN C 1 98  ? 24.480  30.677  51.596  1.00 50.10  ? 103 ASN C N   1 
ATOM   4702  C CA  . ASN C 1 98  ? 24.521  30.061  50.277  1.00 53.33  ? 103 ASN C CA  1 
ATOM   4703  C C   . ASN C 1 98  ? 23.200  29.371  49.954  1.00 52.15  ? 103 ASN C C   1 
ATOM   4704  O O   . ASN C 1 98  ? 22.606  28.706  50.807  1.00 46.33  ? 103 ASN C O   1 
ATOM   4705  C CB  . ASN C 1 98  ? 25.664  29.052  50.203  1.00 50.95  ? 103 ASN C CB  1 
ATOM   4706  C CG  . ASN C 1 98  ? 26.015  28.664  48.779  1.00 47.65  ? 103 ASN C CG  1 
ATOM   4707  O OD1 . ASN C 1 98  ? 25.889  27.506  48.393  1.00 55.67  ? 103 ASN C OD1 1 
ATOM   4708  N ND2 . ASN C 1 98  ? 26.468  29.636  47.993  1.00 55.09  ? 103 ASN C ND2 1 
ATOM   4709  N N   . ASP C 1 99  ? 22.747  29.536  48.708  1.00 49.32  ? 104 ASP C N   1 
ATOM   4710  C CA  . ASP C 1 99  ? 21.513  28.921  48.216  1.00 47.21  ? 104 ASP C CA  1 
ATOM   4711  C C   . ASP C 1 99  ? 20.356  29.197  49.168  1.00 46.26  ? 104 ASP C C   1 
ATOM   4712  O O   . ASP C 1 99  ? 19.571  28.311  49.512  1.00 42.92  ? 104 ASP C O   1 
ATOM   4713  C CB  . ASP C 1 99  ? 21.693  27.420  47.997  1.00 57.93  ? 104 ASP C CB  1 
ATOM   4714  C CG  . ASP C 1 99  ? 22.586  27.112  46.817  1.00 62.82  ? 104 ASP C CG  1 
ATOM   4715  O OD1 . ASP C 1 99  ? 22.941  28.062  46.086  1.00 69.86  ? 104 ASP C OD1 1 
ATOM   4716  O OD2 . ASP C 1 99  ? 22.934  25.928  46.621  1.00 66.24  ? 104 ASP C OD2 1 
ATOM   4717  N N   . TYR C 1 100 ? 20.268  30.456  49.600  1.00 40.86  ? 105 TYR C N   1 
ATOM   4718  C CA  . TYR C 1 100 ? 19.267  30.841  50.588  1.00 46.20  ? 105 TYR C CA  1 
ATOM   4719  C C   . TYR C 1 100 ? 17.855  30.579  50.076  1.00 52.64  ? 105 TYR C C   1 
ATOM   4720  O O   . TYR C 1 100 ? 17.004  30.069  50.815  1.00 53.97  ? 105 TYR C O   1 
ATOM   4721  C CB  . TYR C 1 100 ? 19.457  32.316  50.949  1.00 37.14  ? 105 TYR C CB  1 
ATOM   4722  C CG  . TYR C 1 100 ? 18.592  32.836  52.079  1.00 44.13  ? 105 TYR C CG  1 
ATOM   4723  C CD1 . TYR C 1 100 ? 18.266  32.038  53.169  1.00 42.31  ? 105 TYR C CD1 1 
ATOM   4724  C CD2 . TYR C 1 100 ? 18.126  34.144  52.065  1.00 35.64  ? 105 TYR C CD2 1 
ATOM   4725  C CE1 . TYR C 1 100 ? 17.482  32.527  54.205  1.00 36.86  ? 105 TYR C CE1 1 
ATOM   4726  C CE2 . TYR C 1 100 ? 17.349  34.640  53.090  1.00 45.41  ? 105 TYR C CE2 1 
ATOM   4727  C CZ  . TYR C 1 100 ? 17.027  33.833  54.159  1.00 55.19  ? 105 TYR C CZ  1 
ATOM   4728  O OH  . TYR C 1 100 ? 16.243  34.345  55.175  1.00 58.22  ? 105 TYR C OH  1 
ATOM   4729  N N   . GLU C 1 101 ? 17.590  30.905  48.809  1.00 42.92  ? 106 GLU C N   1 
ATOM   4730  C CA  . GLU C 1 101 ? 16.235  30.772  48.286  1.00 53.12  ? 106 GLU C CA  1 
ATOM   4731  C C   . GLU C 1 101 ? 15.842  29.309  48.121  1.00 56.47  ? 106 GLU C C   1 
ATOM   4732  O O   . GLU C 1 101 ? 14.710  28.927  48.439  1.00 48.61  ? 106 GLU C O   1 
ATOM   4733  C CB  . GLU C 1 101 ? 16.110  31.521  46.961  1.00 59.06  ? 106 GLU C CB  1 
ATOM   4734  C CG  . GLU C 1 101 ? 16.283  33.027  47.090  1.00 45.46  ? 106 GLU C CG  1 
ATOM   4735  C CD  . GLU C 1 101 ? 17.742  33.445  47.057  1.00 63.90  ? 106 GLU C CD  1 
ATOM   4736  O OE1 . GLU C 1 101 ? 18.591  32.620  46.650  1.00 60.95  ? 106 GLU C OE1 1 
ATOM   4737  O OE2 . GLU C 1 101 ? 18.040  34.597  47.438  1.00 72.36  ? 106 GLU C OE2 1 
ATOM   4738  N N   . GLU C 1 102 ? 16.762  28.476  47.626  1.00 50.79  ? 107 GLU C N   1 
ATOM   4739  C CA  . GLU C 1 102 ? 16.479  27.047  47.521  1.00 50.93  ? 107 GLU C CA  1 
ATOM   4740  C C   . GLU C 1 102 ? 16.297  26.421  48.899  1.00 51.89  ? 107 GLU C C   1 
ATOM   4741  O O   . GLU C 1 102 ? 15.463  25.525  49.075  1.00 55.46  ? 107 GLU C O   1 
ATOM   4742  C CB  . GLU C 1 102 ? 17.593  26.344  46.745  1.00 46.23  ? 107 GLU C CB  1 
ATOM   4743  C CG  . GLU C 1 102 ? 17.413  26.387  45.228  1.00 51.06  ? 107 GLU C CG  1 
ATOM   4744  C CD  . GLU C 1 102 ? 16.299  25.474  44.734  1.00 57.82  ? 107 GLU C CD  1 
ATOM   4745  O OE1 . GLU C 1 102 ? 16.256  24.299  45.161  1.00 52.47  ? 107 GLU C OE1 1 
ATOM   4746  O OE2 . GLU C 1 102 ? 15.464  25.934  43.922  1.00 47.64  ? 107 GLU C OE2 1 
ATOM   4747  N N   . LEU C 1 103 ? 17.076  26.873  49.887  1.00 51.88  ? 108 LEU C N   1 
ATOM   4748  C CA  . LEU C 1 103 ? 16.867  26.419  51.258  1.00 53.30  ? 108 LEU C CA  1 
ATOM   4749  C C   . LEU C 1 103 ? 15.531  26.908  51.803  1.00 50.12  ? 108 LEU C C   1 
ATOM   4750  O O   . LEU C 1 103 ? 14.830  26.165  52.499  1.00 52.43  ? 108 LEU C O   1 
ATOM   4751  C CB  . LEU C 1 103 ? 18.013  26.888  52.153  1.00 52.83  ? 108 LEU C CB  1 
ATOM   4752  C CG  . LEU C 1 103 ? 17.972  26.382  53.598  1.00 51.97  ? 108 LEU C CG  1 
ATOM   4753  C CD1 . LEU C 1 103 ? 18.087  24.867  53.642  1.00 51.52  ? 108 LEU C CD1 1 
ATOM   4754  C CD2 . LEU C 1 103 ? 19.062  27.027  54.427  1.00 52.15  ? 108 LEU C CD2 1 
ATOM   4755  N N   . LYS C 1 104 ? 15.163  28.156  51.501  1.00 51.41  ? 109 LYS C N   1 
ATOM   4756  C CA  . LYS C 1 104 ? 13.872  28.671  51.943  1.00 50.48  ? 109 LYS C CA  1 
ATOM   4757  C C   . LYS C 1 104 ? 12.728  27.869  51.340  1.00 60.21  ? 109 LYS C C   1 
ATOM   4758  O O   . LYS C 1 104 ? 11.742  27.567  52.023  1.00 64.39  ? 109 LYS C O   1 
ATOM   4759  C CB  . LYS C 1 104 ? 13.735  30.144  51.565  1.00 50.43  ? 109 LYS C CB  1 
ATOM   4760  C CG  . LYS C 1 104 ? 14.263  31.106  52.597  1.00 53.83  ? 109 LYS C CG  1 
ATOM   4761  C CD  . LYS C 1 104 ? 14.699  32.405  51.946  1.00 43.57  ? 109 LYS C CD  1 
ATOM   4762  C CE  . LYS C 1 104 ? 13.706  33.514  52.206  1.00 46.91  ? 109 LYS C CE  1 
ATOM   4763  N NZ  . LYS C 1 104 ? 13.889  34.631  51.242  1.00 61.33  ? 109 LYS C NZ  1 
ATOM   4764  N N   . HIS C 1 105 ? 12.837  27.523  50.055  1.00 55.83  ? 110 HIS C N   1 
ATOM   4765  C CA  . HIS C 1 105 ? 11.805  26.715  49.418  1.00 53.51  ? 110 HIS C CA  1 
ATOM   4766  C C   . HIS C 1 105 ? 11.716  25.338  50.063  1.00 52.04  ? 110 HIS C C   1 
ATOM   4767  O O   . HIS C 1 105 ? 10.618  24.795  50.235  1.00 48.08  ? 110 HIS C O   1 
ATOM   4768  C CB  . HIS C 1 105 ? 12.082  26.600  47.919  1.00 48.13  ? 110 HIS C CB  1 
ATOM   4769  C CG  . HIS C 1 105 ? 11.008  25.887  47.158  1.00 57.56  ? 110 HIS C CG  1 
ATOM   4770  N ND1 . HIS C 1 105 ? 9.790   26.466  46.870  1.00 53.71  ? 110 HIS C ND1 1 
ATOM   4771  C CD2 . HIS C 1 105 ? 10.972  24.644  46.621  1.00 47.51  ? 110 HIS C CD2 1 
ATOM   4772  C CE1 . HIS C 1 105 ? 9.049   25.608  46.192  1.00 56.83  ? 110 HIS C CE1 1 
ATOM   4773  N NE2 . HIS C 1 105 ? 9.742   24.495  46.028  1.00 48.23  ? 110 HIS C NE2 1 
ATOM   4774  N N   . LEU C 1 106 ? 12.862  24.768  50.444  1.00 46.57  ? 111 LEU C N   1 
ATOM   4775  C CA  . LEU C 1 106 ? 12.872  23.455  51.083  1.00 54.67  ? 111 LEU C CA  1 
ATOM   4776  C C   . LEU C 1 106 ? 12.187  23.474  52.445  1.00 54.03  ? 111 LEU C C   1 
ATOM   4777  O O   . LEU C 1 106 ? 11.614  22.461  52.861  1.00 44.43  ? 111 LEU C O   1 
ATOM   4778  C CB  . LEU C 1 106 ? 14.311  22.958  51.224  1.00 53.79  ? 111 LEU C CB  1 
ATOM   4779  C CG  . LEU C 1 106 ? 14.493  21.552  51.794  1.00 55.19  ? 111 LEU C CG  1 
ATOM   4780  C CD1 . LEU C 1 106 ? 15.439  20.746  50.925  1.00 46.35  ? 111 LEU C CD1 1 
ATOM   4781  C CD2 . LEU C 1 106 ? 15.002  21.629  53.223  1.00 63.55  ? 111 LEU C CD2 1 
ATOM   4782  N N   . LEU C 1 107 ? 12.240  24.600  53.152  1.00 54.85  ? 112 LEU C N   1 
ATOM   4783  C CA  . LEU C 1 107 ? 11.696  24.714  54.500  1.00 56.27  ? 112 LEU C CA  1 
ATOM   4784  C C   . LEU C 1 107 ? 10.278  25.271  54.537  1.00 55.12  ? 112 LEU C C   1 
ATOM   4785  O O   . LEU C 1 107 ? 9.748   25.493  55.631  1.00 46.77  ? 112 LEU C O   1 
ATOM   4786  C CB  . LEU C 1 107 ? 12.604  25.601  55.357  1.00 49.42  ? 112 LEU C CB  1 
ATOM   4787  C CG  . LEU C 1 107 ? 14.056  25.149  55.509  1.00 56.79  ? 112 LEU C CG  1 
ATOM   4788  C CD1 . LEU C 1 107 ? 14.907  26.255  56.113  1.00 51.13  ? 112 LEU C CD1 1 
ATOM   4789  C CD2 . LEU C 1 107 ? 14.121  23.910  56.360  1.00 49.51  ? 112 LEU C CD2 1 
ATOM   4790  N N   . SER C 1 108 ? 9.660   25.522  53.382  1.00 56.37  ? 113 SER C N   1 
ATOM   4791  C CA  . SER C 1 108 ? 8.329   26.125  53.372  1.00 53.70  ? 113 SER C CA  1 
ATOM   4792  C C   . SER C 1 108 ? 7.305   25.213  54.039  1.00 48.58  ? 113 SER C C   1 
ATOM   4793  O O   . SER C 1 108 ? 6.482   25.669  54.839  1.00 55.87  ? 113 SER C O   1 
ATOM   4794  C CB  . SER C 1 108 ? 7.918   26.448  51.937  1.00 45.16  ? 113 SER C CB  1 
ATOM   4795  O OG  . SER C 1 108 ? 8.346   25.420  51.062  1.00 54.39  ? 113 SER C OG  1 
ATOM   4796  N N   . ARG C 1 109 ? 7.341   23.920  53.722  1.00 48.40  ? 114 ARG C N   1 
ATOM   4797  C CA  . ARG C 1 109 ? 6.478   22.927  54.351  1.00 55.49  ? 114 ARG C CA  1 
ATOM   4798  C C   . ARG C 1 109 ? 7.352   21.800  54.875  1.00 57.68  ? 114 ARG C C   1 
ATOM   4799  O O   . ARG C 1 109 ? 8.016   21.111  54.092  1.00 49.67  ? 114 ARG C O   1 
ATOM   4800  C CB  . ARG C 1 109 ? 5.433   22.385  53.369  1.00 53.15  ? 114 ARG C CB  1 
ATOM   4801  C CG  . ARG C 1 109 ? 4.324   21.581  54.032  1.00 53.11  ? 114 ARG C CG  1 
ATOM   4802  C CD  . ARG C 1 109 ? 3.756   20.512  53.102  1.00 45.09  ? 114 ARG C CD  1 
ATOM   4803  N NE  . ARG C 1 109 ? 2.429   20.872  52.617  1.00 66.24  ? 114 ARG C NE  1 
ATOM   4804  C CZ  . ARG C 1 109 ? 2.054   20.827  51.345  1.00 68.18  ? 114 ARG C CZ  1 
ATOM   4805  N NH1 . ARG C 1 109 ? 2.874   20.405  50.397  1.00 65.50  ? 114 ARG C NH1 1 
ATOM   4806  N NH2 . ARG C 1 109 ? 0.825   21.216  51.016  1.00 74.76  ? 114 ARG C NH2 1 
ATOM   4807  N N   . ILE C 1 110 ? 7.350   21.612  56.193  1.00 54.76  ? 115 ILE C N   1 
ATOM   4808  C CA  . ILE C 1 110 ? 8.201   20.635  56.861  1.00 59.34  ? 115 ILE C CA  1 
ATOM   4809  C C   . ILE C 1 110 ? 7.318   19.718  57.694  1.00 57.27  ? 115 ILE C C   1 
ATOM   4810  O O   . ILE C 1 110 ? 6.513   20.192  58.506  1.00 52.08  ? 115 ILE C O   1 
ATOM   4811  C CB  . ILE C 1 110 ? 9.271   21.321  57.733  1.00 59.91  ? 115 ILE C CB  1 
ATOM   4812  C CG1 . ILE C 1 110 ? 10.411  21.835  56.858  1.00 51.54  ? 115 ILE C CG1 1 
ATOM   4813  C CG2 . ILE C 1 110 ? 9.823   20.360  58.768  1.00 58.52  ? 115 ILE C CG2 1 
ATOM   4814  C CD1 . ILE C 1 110 ? 10.947  20.795  55.907  1.00 46.30  ? 115 ILE C CD1 1 
ATOM   4815  N N   . ASN C 1 111 ? 7.471   18.407  57.490  1.00 54.97  ? 116 ASN C N   1 
ATOM   4816  C CA  . ASN C 1 111 ? 6.685   17.429  58.232  1.00 52.43  ? 116 ASN C CA  1 
ATOM   4817  C C   . ASN C 1 111 ? 7.172   17.257  59.667  1.00 72.16  ? 116 ASN C C   1 
ATOM   4818  O O   . ASN C 1 111 ? 6.358   17.000  60.560  1.00 69.75  ? 116 ASN C O   1 
ATOM   4819  C CB  . ASN C 1 111 ? 6.708   16.081  57.505  1.00 60.21  ? 116 ASN C CB  1 
ATOM   4820  C CG  . ASN C 1 111 ? 5.671   15.113  58.038  1.00 67.53  ? 116 ASN C CG  1 
ATOM   4821  O OD1 . ASN C 1 111 ? 4.716   15.514  58.703  1.00 76.11  ? 116 ASN C OD1 1 
ATOM   4822  N ND2 . ASN C 1 111 ? 5.846   13.832  57.738  1.00 67.72  ? 116 ASN C ND2 1 
ATOM   4823  N N   . HIS C 1 112 ? 8.480   17.381  59.910  1.00 70.84  ? 117 HIS C N   1 
ATOM   4824  C CA  . HIS C 1 112 ? 9.018   17.274  61.262  1.00 70.60  ? 117 HIS C CA  1 
ATOM   4825  C C   . HIS C 1 112 ? 10.304  18.081  61.383  1.00 71.08  ? 117 HIS C C   1 
ATOM   4826  O O   . HIS C 1 112 ? 11.203  17.955  60.545  1.00 65.38  ? 117 HIS C O   1 
ATOM   4827  C CB  . HIS C 1 112 ? 9.282   15.814  61.650  1.00 75.90  ? 117 HIS C CB  1 
ATOM   4828  C CG  . HIS C 1 112 ? 9.701   15.639  63.079  1.00 88.68  ? 117 HIS C CG  1 
ATOM   4829  N ND1 . HIS C 1 112 ? 8.833   15.818  64.136  1.00 87.54  ? 117 HIS C ND1 1 
ATOM   4830  C CD2 . HIS C 1 112 ? 10.897  15.314  63.625  1.00 84.56  ? 117 HIS C CD2 1 
ATOM   4831  C CE1 . HIS C 1 112 ? 9.474   15.604  65.271  1.00 86.93  ? 117 HIS C CE1 1 
ATOM   4832  N NE2 . HIS C 1 112 ? 10.728  15.296  64.989  1.00 80.13  ? 117 HIS C NE2 1 
ATOM   4833  N N   . PHE C 1 113 ? 10.395  18.884  62.444  1.00 67.46  ? 118 PHE C N   1 
ATOM   4834  C CA  . PHE C 1 113 ? 11.550  19.741  62.689  1.00 72.66  ? 118 PHE C CA  1 
ATOM   4835  C C   . PHE C 1 113 ? 11.948  19.633  64.153  1.00 74.84  ? 118 PHE C C   1 
ATOM   4836  O O   . PHE C 1 113 ? 11.132  19.910  65.039  1.00 73.08  ? 118 PHE C O   1 
ATOM   4837  C CB  . PHE C 1 113 ? 11.238  21.193  62.327  1.00 69.16  ? 118 PHE C CB  1 
ATOM   4838  C CG  . PHE C 1 113 ? 12.418  21.950  61.817  1.00 63.50  ? 118 PHE C CG  1 
ATOM   4839  C CD1 . PHE C 1 113 ? 13.231  21.405  60.837  1.00 68.27  ? 118 PHE C CD1 1 
ATOM   4840  C CD2 . PHE C 1 113 ? 12.718  23.206  62.313  1.00 62.56  ? 118 PHE C CD2 1 
ATOM   4841  C CE1 . PHE C 1 113 ? 14.324  22.102  60.361  1.00 69.01  ? 118 PHE C CE1 1 
ATOM   4842  C CE2 . PHE C 1 113 ? 13.811  23.907  61.843  1.00 72.66  ? 118 PHE C CE2 1 
ATOM   4843  C CZ  . PHE C 1 113 ? 14.613  23.355  60.864  1.00 68.02  ? 118 PHE C CZ  1 
ATOM   4844  N N   . GLU C 1 114 ? 13.200  19.251  64.407  1.00 70.35  ? 119 GLU C N   1 
ATOM   4845  C CA  . GLU C 1 114 ? 13.701  19.059  65.767  1.00 75.19  ? 119 GLU C CA  1 
ATOM   4846  C C   . GLU C 1 114 ? 15.129  19.577  65.840  1.00 73.60  ? 119 GLU C C   1 
ATOM   4847  O O   . GLU C 1 114 ? 16.039  18.978  65.257  1.00 68.57  ? 119 GLU C O   1 
ATOM   4848  C CB  . GLU C 1 114 ? 13.641  17.586  66.178  1.00 79.63  ? 119 GLU C CB  1 
ATOM   4849  C CG  . GLU C 1 114 ? 13.264  17.352  67.636  1.00 85.75  ? 119 GLU C CG  1 
ATOM   4850  C CD  . GLU C 1 114 ? 12.380  16.130  67.817  1.00 99.64  ? 119 GLU C CD  1 
ATOM   4851  O OE1 . GLU C 1 114 ? 11.426  16.193  68.624  1.00 104.51 ? 119 GLU C OE1 1 
ATOM   4852  O OE2 . GLU C 1 114 ? 12.638  15.108  67.148  1.00 104.60 ? 119 GLU C OE2 1 
ATOM   4853  N N   . LYS C 1 115 ? 15.328  20.683  66.554  1.00 73.03  ? 120 LYS C N   1 
ATOM   4854  C CA  . LYS C 1 115 ? 16.675  21.184  66.785  1.00 65.05  ? 120 LYS C CA  1 
ATOM   4855  C C   . LYS C 1 115 ? 17.450  20.199  67.653  1.00 70.63  ? 120 LYS C C   1 
ATOM   4856  O O   . LYS C 1 115 ? 16.923  19.659  68.628  1.00 74.82  ? 120 LYS C O   1 
ATOM   4857  C CB  . LYS C 1 115 ? 16.627  22.559  67.451  1.00 63.90  ? 120 LYS C CB  1 
ATOM   4858  C CG  . LYS C 1 115 ? 17.984  23.241  67.555  1.00 66.88  ? 120 LYS C CG  1 
ATOM   4859  C CD  . LYS C 1 115 ? 17.833  24.730  67.811  1.00 74.20  ? 120 LYS C CD  1 
ATOM   4860  C CE  . LYS C 1 115 ? 17.946  25.053  69.293  1.00 77.03  ? 120 LYS C CE  1 
ATOM   4861  N NZ  . LYS C 1 115 ? 17.910  26.521  69.535  1.00 89.51  ? 120 LYS C NZ  1 
ATOM   4862  N N   . THR C 1 116 ? 18.707  19.957  67.287  1.00 72.55  ? 121 THR C N   1 
ATOM   4863  C CA  . THR C 1 116 ? 19.504  18.927  67.937  1.00 72.99  ? 121 THR C CA  1 
ATOM   4864  C C   . THR C 1 116 ? 20.926  19.418  68.140  1.00 72.65  ? 121 THR C C   1 
ATOM   4865  O O   . THR C 1 116 ? 21.513  20.029  67.244  1.00 71.75  ? 121 THR C O   1 
ATOM   4866  C CB  . THR C 1 116 ? 19.529  17.633  67.110  1.00 74.59  ? 121 THR C CB  1 
ATOM   4867  O OG1 . THR C 1 116 ? 18.187  17.206  66.845  1.00 84.19  ? 121 THR C OG1 1 
ATOM   4868  C CG2 . THR C 1 116 ? 20.273  16.530  67.853  1.00 65.61  ? 121 THR C CG2 1 
ATOM   4869  N N   . LEU C 1 117 ? 21.475  19.140  69.320  1.00 73.37  ? 122 LEU C N   1 
ATOM   4870  C CA  . LEU C 1 117 ? 22.894  19.347  69.572  1.00 75.00  ? 122 LEU C CA  1 
ATOM   4871  C C   . LEU C 1 117 ? 23.669  18.191  68.950  1.00 74.23  ? 122 LEU C C   1 
ATOM   4872  O O   . LEU C 1 117 ? 23.442  17.027  69.300  1.00 80.11  ? 122 LEU C O   1 
ATOM   4873  C CB  . LEU C 1 117 ? 23.160  19.443  71.074  1.00 80.82  ? 122 LEU C CB  1 
ATOM   4874  C CG  . LEU C 1 117 ? 24.566  19.789  71.584  1.00 83.14  ? 122 LEU C CG  1 
ATOM   4875  C CD1 . LEU C 1 117 ? 25.421  18.538  71.769  1.00 68.92  ? 122 LEU C CD1 1 
ATOM   4876  C CD2 . LEU C 1 117 ? 25.267  20.789  70.679  1.00 83.45  ? 122 LEU C CD2 1 
ATOM   4877  N N   . ILE C 1 118 ? 24.573  18.504  68.024  1.00 65.39  ? 123 ILE C N   1 
ATOM   4878  C CA  . ILE C 1 118 ? 25.380  17.496  67.353  1.00 73.44  ? 123 ILE C CA  1 
ATOM   4879  C C   . ILE C 1 118 ? 26.860  17.635  67.694  1.00 74.29  ? 123 ILE C C   1 
ATOM   4880  O O   . ILE C 1 118 ? 27.567  16.631  67.807  1.00 73.70  ? 123 ILE C O   1 
ATOM   4881  C CB  . ILE C 1 118 ? 25.161  17.530  65.824  1.00 68.66  ? 123 ILE C CB  1 
ATOM   4882  C CG1 . ILE C 1 118 ? 25.479  18.913  65.254  1.00 69.19  ? 123 ILE C CG1 1 
ATOM   4883  C CG2 . ILE C 1 118 ? 23.737  17.123  65.485  1.00 70.72  ? 123 ILE C CG2 1 
ATOM   4884  C CD1 . ILE C 1 118 ? 25.878  18.878  63.801  1.00 52.42  ? 123 ILE C CD1 1 
ATOM   4885  N N   . ILE C 1 119 ? 27.347  18.863  67.844  1.00 74.94  ? 124 ILE C N   1 
ATOM   4886  C CA  . ILE C 1 119 ? 28.734  19.106  68.235  1.00 71.91  ? 124 ILE C CA  1 
ATOM   4887  C C   . ILE C 1 119 ? 28.747  20.042  69.439  1.00 74.39  ? 124 ILE C C   1 
ATOM   4888  O O   . ILE C 1 119 ? 28.553  21.257  69.281  1.00 68.41  ? 124 ILE C O   1 
ATOM   4889  C CB  . ILE C 1 119 ? 29.553  19.685  67.070  1.00 77.50  ? 124 ILE C CB  1 
ATOM   4890  C CG1 . ILE C 1 119 ? 29.541  18.728  65.877  1.00 79.72  ? 124 ILE C CG1 1 
ATOM   4891  C CG2 . ILE C 1 119 ? 30.984  19.957  67.508  1.00 84.45  ? 124 ILE C CG2 1 
ATOM   4892  C CD1 . ILE C 1 119 ? 30.378  19.203  64.711  1.00 76.43  ? 124 ILE C CD1 1 
ATOM   4893  N N   . PRO C 1 120 ? 28.967  19.530  70.648  1.00 81.75  ? 125 PRO C N   1 
ATOM   4894  C CA  . PRO C 1 120 ? 28.981  20.399  71.829  1.00 77.66  ? 125 PRO C CA  1 
ATOM   4895  C C   . PRO C 1 120 ? 30.212  21.289  71.855  1.00 73.28  ? 125 PRO C C   1 
ATOM   4896  O O   . PRO C 1 120 ? 31.246  20.990  71.253  1.00 78.54  ? 125 PRO C O   1 
ATOM   4897  C CB  . PRO C 1 120 ? 28.993  19.409  72.997  1.00 77.16  ? 125 PRO C CB  1 
ATOM   4898  C CG  . PRO C 1 120 ? 29.659  18.192  72.438  1.00 75.48  ? 125 PRO C CG  1 
ATOM   4899  C CD  . PRO C 1 120 ? 29.289  18.130  70.978  1.00 69.92  ? 125 PRO C CD  1 
ATOM   4900  N N   . LYS C 1 121 A 30.086  22.406  72.579  1.00 78.38  ? 125 LYS C N   1 
ATOM   4901  C CA  . LYS C 1 121 A 31.214  23.322  72.726  1.00 80.58  ? 125 LYS C CA  1 
ATOM   4902  C C   . LYS C 1 121 A 32.413  22.639  73.370  1.00 73.24  ? 125 LYS C C   1 
ATOM   4903  O O   . LYS C 1 121 A 33.558  23.033  73.124  1.00 73.03  ? 125 LYS C O   1 
ATOM   4904  C CB  . LYS C 1 121 A 30.804  24.541  73.553  1.00 81.63  ? 125 LYS C CB  1 
ATOM   4905  C CG  . LYS C 1 121 A 30.555  25.807  72.749  1.00 69.23  ? 125 LYS C CG  1 
ATOM   4906  C CD  . LYS C 1 121 A 29.987  26.901  73.640  1.00 64.40  ? 125 LYS C CD  1 
ATOM   4907  C CE  . LYS C 1 121 A 29.134  27.883  72.855  1.00 85.18  ? 125 LYS C CE  1 
ATOM   4908  N NZ  . LYS C 1 121 A 29.934  29.017  72.317  1.00 79.35  ? 125 LYS C NZ  1 
ATOM   4909  N N   . SER C 1 122 B 32.172  21.610  74.185  1.00 88.56  ? 125 SER C N   1 
ATOM   4910  C CA  . SER C 1 122 B 33.240  20.906  74.883  1.00 73.00  ? 125 SER C CA  1 
ATOM   4911  C C   . SER C 1 122 B 34.136  20.102  73.951  1.00 75.00  ? 125 SER C C   1 
ATOM   4912  O O   . SER C 1 122 B 35.201  19.652  74.388  1.00 90.60  ? 125 SER C O   1 
ATOM   4913  C CB  . SER C 1 122 B 32.642  19.981  75.941  1.00 75.15  ? 125 SER C CB  1 
ATOM   4914  O OG  . SER C 1 122 B 31.864  20.712  76.872  1.00 89.25  ? 125 SER C OG  1 
ATOM   4915  N N   . SER C 1 123 ? 33.740  19.902  72.694  1.00 73.68  ? 126 SER C N   1 
ATOM   4916  C CA  . SER C 1 123 ? 34.538  19.138  71.746  1.00 79.07  ? 126 SER C CA  1 
ATOM   4917  C C   . SER C 1 123 ? 35.593  19.990  71.041  1.00 82.82  ? 126 SER C C   1 
ATOM   4918  O O   . SER C 1 123 ? 36.114  19.580  69.997  1.00 75.23  ? 126 SER C O   1 
ATOM   4919  C CB  . SER C 1 123 ? 33.629  18.449  70.722  1.00 85.31  ? 126 SER C CB  1 
ATOM   4920  O OG  . SER C 1 123 ? 32.631  19.329  70.236  1.00 80.64  ? 126 SER C OG  1 
ATOM   4921  N N   . TRP C 1 124 ? 35.931  21.152  71.601  1.00 89.54  ? 127 TRP C N   1 
ATOM   4922  C CA  . TRP C 1 124 ? 36.988  22.019  71.079  1.00 88.12  ? 127 TRP C CA  1 
ATOM   4923  C C   . TRP C 1 124 ? 37.968  22.328  72.205  1.00 88.77  ? 127 TRP C C   1 
ATOM   4924  O O   . TRP C 1 124 ? 38.025  23.456  72.712  1.00 76.62  ? 127 TRP C O   1 
ATOM   4925  C CB  . TRP C 1 124 ? 36.409  23.307  70.492  1.00 80.42  ? 127 TRP C CB  1 
ATOM   4926  C CG  . TRP C 1 124 ? 35.260  23.092  69.550  1.00 82.47  ? 127 TRP C CG  1 
ATOM   4927  C CD1 . TRP C 1 124 ? 33.967  23.488  69.733  1.00 71.19  ? 127 TRP C CD1 1 
ATOM   4928  C CD2 . TRP C 1 124 ? 35.302  22.438  68.275  1.00 75.75  ? 127 TRP C CD2 1 
ATOM   4929  N NE1 . TRP C 1 124 ? 33.202  23.119  68.655  1.00 76.52  ? 127 TRP C NE1 1 
ATOM   4930  C CE2 . TRP C 1 124 ? 33.997  22.473  67.745  1.00 67.57  ? 127 TRP C CE2 1 
ATOM   4931  C CE3 . TRP C 1 124 ? 36.316  21.827  67.530  1.00 78.69  ? 127 TRP C CE3 1 
ATOM   4932  C CZ2 . TRP C 1 124 ? 33.679  21.922  66.506  1.00 70.30  ? 127 TRP C CZ2 1 
ATOM   4933  C CZ3 . TRP C 1 124 ? 35.998  21.277  66.299  1.00 75.54  ? 127 TRP C CZ3 1 
ATOM   4934  C CH2 . TRP C 1 124 ? 34.690  21.328  65.802  1.00 79.35  ? 127 TRP C CH2 1 
ATOM   4935  N N   . PRO C 1 125 ? 38.766  21.337  72.620  1.00 87.29  ? 128 PRO C N   1 
ATOM   4936  C CA  . PRO C 1 125 ? 39.670  21.555  73.760  1.00 87.11  ? 128 PRO C CA  1 
ATOM   4937  C C   . PRO C 1 125 ? 40.909  22.363  73.418  1.00 78.76  ? 128 PRO C C   1 
ATOM   4938  O O   . PRO C 1 125 ? 41.484  22.989  74.320  1.00 78.54  ? 128 PRO C O   1 
ATOM   4939  C CB  . PRO C 1 125 ? 40.042  20.130  74.187  1.00 85.82  ? 128 PRO C CB  1 
ATOM   4940  C CG  . PRO C 1 125 ? 39.947  19.331  72.926  1.00 79.75  ? 128 PRO C CG  1 
ATOM   4941  C CD  . PRO C 1 125 ? 38.904  19.984  72.049  1.00 71.99  ? 128 PRO C CD  1 
ATOM   4942  N N   . ASN C 1 126 ? 41.339  22.367  72.159  1.00 77.08  ? 129 ASN C N   1 
ATOM   4943  C CA  . ASN C 1 126 ? 42.526  23.093  71.733  1.00 69.16  ? 129 ASN C CA  1 
ATOM   4944  C C   . ASN C 1 126 ? 42.198  24.409  71.042  1.00 75.28  ? 129 ASN C C   1 
ATOM   4945  O O   . ASN C 1 126 ? 43.098  25.041  70.479  1.00 71.95  ? 129 ASN C O   1 
ATOM   4946  C CB  . ASN C 1 126 ? 43.371  22.215  70.811  1.00 71.45  ? 129 ASN C CB  1 
ATOM   4947  C CG  . ASN C 1 126 ? 43.536  20.807  71.346  1.00 81.69  ? 129 ASN C CG  1 
ATOM   4948  O OD1 . ASN C 1 126 ? 42.697  19.939  71.108  1.00 85.53  ? 129 ASN C OD1 1 
ATOM   4949  N ND2 . ASN C 1 126 ? 44.615  20.577  72.083  1.00 77.51  ? 129 ASN C ND2 1 
ATOM   4950  N N   . HIS C 1 127 ? 40.936  24.837  71.066  1.00 71.88  ? 130 HIS C N   1 
ATOM   4951  C CA  . HIS C 1 127 ? 40.534  26.078  70.424  1.00 58.29  ? 130 HIS C CA  1 
ATOM   4952  C C   . HIS C 1 127 ? 39.599  26.849  71.342  1.00 68.23  ? 130 HIS C C   1 
ATOM   4953  O O   . HIS C 1 127 ? 38.912  26.268  72.186  1.00 78.85  ? 130 HIS C O   1 
ATOM   4954  C CB  . HIS C 1 127 ? 39.845  25.823  69.077  1.00 53.29  ? 130 HIS C CB  1 
ATOM   4955  C CG  . HIS C 1 127 ? 40.684  25.057  68.105  1.00 58.96  ? 130 HIS C CG  1 
ATOM   4956  N ND1 . HIS C 1 127 ? 40.934  23.707  68.238  1.00 63.96  ? 130 HIS C ND1 1 
ATOM   4957  C CD2 . HIS C 1 127 ? 41.327  25.450  66.979  1.00 54.59  ? 130 HIS C CD2 1 
ATOM   4958  C CE1 . HIS C 1 127 ? 41.699  23.303  67.239  1.00 50.32  ? 130 HIS C CE1 1 
ATOM   4959  N NE2 . HIS C 1 127 ? 41.952  24.341  66.462  1.00 57.54  ? 130 HIS C NE2 1 
ATOM   4960  N N   . GLU C 1 128 ? 39.579  28.165  71.166  1.00 72.36  ? 131 GLU C N   1 
ATOM   4961  C CA  . GLU C 1 128 ? 38.693  29.027  71.933  1.00 84.73  ? 131 GLU C CA  1 
ATOM   4962  C C   . GLU C 1 128 ? 37.337  29.125  71.245  1.00 80.95  ? 131 GLU C C   1 
ATOM   4963  O O   . GLU C 1 128 ? 37.261  29.323  70.028  1.00 79.38  ? 131 GLU C O   1 
ATOM   4964  C CB  . GLU C 1 128 ? 39.302  30.417  72.105  1.00 78.37  ? 131 GLU C CB  1 
ATOM   4965  C CG  . GLU C 1 128 ? 38.754  31.231  73.284  1.00 95.71  ? 131 GLU C CG  1 
ATOM   4966  C CD  . GLU C 1 128 ? 38.540  30.422  74.563  1.00 104.02 ? 131 GLU C CD  1 
ATOM   4967  O OE1 . GLU C 1 128 ? 39.372  30.562  75.486  1.00 94.47  ? 131 GLU C OE1 1 
ATOM   4968  O OE2 . GLU C 1 128 ? 37.520  29.699  74.677  1.00 91.75  ? 131 GLU C OE2 1 
ATOM   4969  N N   . THR C 1 129 ? 36.268  28.985  72.029  1.00 72.94  ? 132 THR C N   1 
ATOM   4970  C CA  . THR C 1 129 ? 34.911  28.986  71.496  1.00 70.24  ? 132 THR C CA  1 
ATOM   4971  C C   . THR C 1 129 ? 34.082  30.163  71.992  1.00 63.61  ? 132 THR C C   1 
ATOM   4972  O O   . THR C 1 129 ? 32.860  30.165  71.808  1.00 67.52  ? 132 THR C O   1 
ATOM   4973  C CB  . THR C 1 129 ? 34.197  27.676  71.847  1.00 73.43  ? 132 THR C CB  1 
ATOM   4974  O OG1 . THR C 1 129 ? 33.678  27.756  73.181  1.00 78.05  ? 132 THR C OG1 1 
ATOM   4975  C CG2 . THR C 1 129 ? 35.152  26.494  71.748  1.00 65.04  ? 132 THR C CG2 1 
ATOM   4976  N N   . SER C 1 130 ? 34.707  31.165  72.606  1.00 76.39  ? 133 SER C N   1 
ATOM   4977  C CA  . SER C 1 130 ? 33.991  32.272  73.223  1.00 73.48  ? 133 SER C CA  1 
ATOM   4978  C C   . SER C 1 130 ? 33.823  33.467  72.291  1.00 72.98  ? 133 SER C C   1 
ATOM   4979  O O   . SER C 1 130 ? 33.601  34.586  72.769  1.00 73.34  ? 133 SER C O   1 
ATOM   4980  C CB  . SER C 1 130 ? 34.704  32.702  74.508  1.00 83.29  ? 133 SER C CB  1 
ATOM   4981  O OG  . SER C 1 130 ? 34.450  34.064  74.807  1.00 93.05  ? 133 SER C OG  1 
ATOM   4982  N N   . GLY C 1 131 ? 33.920  33.259  70.979  1.00 75.96  ? 134 GLY C N   1 
ATOM   4983  C CA  . GLY C 1 131 ? 33.804  34.348  70.027  1.00 64.92  ? 134 GLY C CA  1 
ATOM   4984  C C   . GLY C 1 131 ? 32.478  35.079  70.084  1.00 68.49  ? 134 GLY C C   1 
ATOM   4985  O O   . GLY C 1 131 ? 31.416  34.457  70.003  1.00 71.48  ? 134 GLY C O   1 
ATOM   4986  N N   . VAL C 1 132 ? 32.531  36.405  70.230  1.00 71.10  ? 135 VAL C N   1 
ATOM   4987  C CA  . VAL C 1 132 ? 31.350  37.256  70.292  1.00 69.19  ? 135 VAL C CA  1 
ATOM   4988  C C   . VAL C 1 132 ? 31.560  38.451  69.371  1.00 63.97  ? 135 VAL C C   1 
ATOM   4989  O O   . VAL C 1 132 ? 32.659  38.697  68.876  1.00 70.32  ? 135 VAL C O   1 
ATOM   4990  C CB  . VAL C 1 132 ? 31.036  37.741  71.725  1.00 79.74  ? 135 VAL C CB  1 
ATOM   4991  C CG1 . VAL C 1 132 ? 31.162  36.604  72.729  1.00 80.12  ? 135 VAL C CG1 1 
ATOM   4992  C CG2 . VAL C 1 132 ? 31.961  38.889  72.104  1.00 76.44  ? 135 VAL C CG2 1 
ATOM   4993  N N   . SER C 1 133 ? 30.481  39.200  69.149  1.00 63.02  ? 136 SER C N   1 
ATOM   4994  C CA  . SER C 1 133 ? 30.542  40.400  68.329  1.00 64.79  ? 136 SER C CA  1 
ATOM   4995  C C   . SER C 1 133 ? 29.463  41.375  68.776  1.00 70.24  ? 136 SER C C   1 
ATOM   4996  O O   . SER C 1 133 ? 28.394  40.971  69.240  1.00 73.32  ? 136 SER C O   1 
ATOM   4997  C CB  . SER C 1 133 ? 30.375  40.081  66.843  1.00 58.27  ? 136 SER C CB  1 
ATOM   4998  O OG  . SER C 1 133 ? 30.386  41.272  66.079  1.00 56.42  ? 136 SER C OG  1 
ATOM   4999  N N   . ALA C 1 134 ? 29.758  42.669  68.629  1.00 75.35  ? 137 ALA C N   1 
ATOM   5000  C CA  . ALA C 1 134 ? 28.810  43.698  69.044  1.00 82.23  ? 137 ALA C CA  1 
ATOM   5001  C C   . ALA C 1 134 ? 27.649  43.822  68.068  1.00 77.25  ? 137 ALA C C   1 
ATOM   5002  O O   . ALA C 1 134 ? 26.544  44.209  68.466  1.00 92.30  ? 137 ALA C O   1 
ATOM   5003  C CB  . ALA C 1 134 ? 29.519  45.044  69.200  1.00 71.37  ? 137 ALA C CB  1 
ATOM   5004  N N   . ALA C 1 135 ? 27.877  43.513  66.791  1.00 76.46  ? 138 ALA C N   1 
ATOM   5005  C CA  . ALA C 1 135 ? 26.799  43.537  65.811  1.00 73.26  ? 138 ALA C CA  1 
ATOM   5006  C C   . ALA C 1 135 ? 25.757  42.455  66.063  1.00 76.65  ? 138 ALA C C   1 
ATOM   5007  O O   . ALA C 1 135 ? 24.681  42.507  65.459  1.00 70.29  ? 138 ALA C O   1 
ATOM   5008  C CB  . ALA C 1 135 ? 27.365  43.396  64.399  1.00 66.63  ? 138 ALA C CB  1 
ATOM   5009  N N   . CYS C 1 136 ? 26.045  41.491  66.942  1.00 72.32  ? 139 CYS C N   1 
ATOM   5010  C CA  . CYS C 1 136 ? 25.111  40.436  67.328  1.00 69.19  ? 139 CYS C CA  1 
ATOM   5011  C C   . CYS C 1 136 ? 24.804  40.565  68.817  1.00 73.77  ? 139 CYS C C   1 
ATOM   5012  O O   . CYS C 1 136 ? 25.168  39.690  69.613  1.00 78.45  ? 139 CYS C O   1 
ATOM   5013  C CB  . CYS C 1 136 ? 25.684  39.053  67.024  1.00 73.78  ? 139 CYS C CB  1 
ATOM   5014  S SG  . CYS C 1 136 ? 26.713  38.981  65.548  1.00 86.20  ? 139 CYS C SG  1 
ATOM   5015  N N   . PRO C 1 137 ? 24.124  41.640  69.227  1.00 73.41  ? 140 PRO C N   1 
ATOM   5016  C CA  . PRO C 1 137 ? 23.933  41.876  70.663  1.00 83.74  ? 140 PRO C CA  1 
ATOM   5017  C C   . PRO C 1 137 ? 22.700  41.196  71.239  1.00 83.96  ? 140 PRO C C   1 
ATOM   5018  O O   . PRO C 1 137 ? 21.598  41.312  70.693  1.00 85.31  ? 140 PRO C O   1 
ATOM   5019  C CB  . PRO C 1 137 ? 23.815  43.403  70.741  1.00 80.87  ? 140 PRO C CB  1 
ATOM   5020  C CG  . PRO C 1 137 ? 23.243  43.809  69.394  1.00 76.03  ? 140 PRO C CG  1 
ATOM   5021  C CD  . PRO C 1 137 ? 23.460  42.675  68.415  1.00 74.31  ? 140 PRO C CD  1 
ATOM   5022  N N   . TYR C 1 138 ? 22.880  40.482  72.348  1.00 79.29  ? 141 TYR C N   1 
ATOM   5023  C CA  . TYR C 1 138 ? 21.782  39.963  73.156  1.00 90.49  ? 141 TYR C CA  1 
ATOM   5024  C C   . TYR C 1 138 ? 21.762  40.735  74.467  1.00 95.68  ? 141 TYR C C   1 
ATOM   5025  O O   . TYR C 1 138 ? 22.761  40.750  75.194  1.00 94.36  ? 141 TYR C O   1 
ATOM   5026  C CB  . TYR C 1 138 ? 21.944  38.465  73.427  1.00 90.36  ? 141 TYR C CB  1 
ATOM   5027  C CG  . TYR C 1 138 ? 20.779  37.821  74.163  1.00 101.43 ? 141 TYR C CG  1 
ATOM   5028  C CD1 . TYR C 1 138 ? 19.578  38.502  74.366  1.00 103.78 ? 141 TYR C CD1 1 
ATOM   5029  C CD2 . TYR C 1 138 ? 20.893  36.538  74.683  1.00 98.68  ? 141 TYR C CD2 1 
ATOM   5030  C CE1 . TYR C 1 138 ? 18.526  37.918  75.047  1.00 106.89 ? 141 TYR C CE1 1 
ATOM   5031  C CE2 . TYR C 1 138 ? 19.845  35.946  75.370  1.00 104.24 ? 141 TYR C CE2 1 
ATOM   5032  C CZ  . TYR C 1 138 ? 18.664  36.639  75.545  1.00 104.61 ? 141 TYR C CZ  1 
ATOM   5033  O OH  . TYR C 1 138 ? 17.622  36.047  76.224  1.00 98.75  ? 141 TYR C OH  1 
ATOM   5034  N N   . GLN C 1 139 ? 20.625  41.366  74.768  1.00 95.79  ? 142 GLN C N   1 
ATOM   5035  C CA  . GLN C 1 139 ? 20.431  42.096  76.020  1.00 101.59 ? 142 GLN C CA  1 
ATOM   5036  C C   . GLN C 1 139 ? 21.455  43.218  76.183  1.00 104.37 ? 142 GLN C C   1 
ATOM   5037  O O   . GLN C 1 139 ? 21.849  43.559  77.301  1.00 112.44 ? 142 GLN C O   1 
ATOM   5038  C CB  . GLN C 1 139 ? 20.470  41.148  77.225  1.00 107.83 ? 142 GLN C CB  1 
ATOM   5039  C CG  . GLN C 1 139 ? 19.639  41.599  78.417  1.00 119.21 ? 142 GLN C CG  1 
ATOM   5040  C CD  . GLN C 1 139 ? 20.498  41.993  79.607  1.00 124.78 ? 142 GLN C CD  1 
ATOM   5041  O OE1 . GLN C 1 139 ? 21.697  41.711  79.642  1.00 116.02 ? 142 GLN C OE1 1 
ATOM   5042  N NE2 . GLN C 1 139 ? 19.888  42.653  80.587  1.00 110.01 ? 142 GLN C NE2 1 
ATOM   5043  N N   . GLY C 1 140 ? 21.896  43.798  75.069  1.00 92.79  ? 143 GLY C N   1 
ATOM   5044  C CA  . GLY C 1 140 ? 22.809  44.921  75.113  1.00 90.34  ? 143 GLY C CA  1 
ATOM   5045  C C   . GLY C 1 140 ? 24.270  44.579  75.301  1.00 93.82  ? 143 GLY C C   1 
ATOM   5046  O O   . GLY C 1 140 ? 25.080  45.496  75.473  1.00 94.43  ? 143 GLY C O   1 
ATOM   5047  N N   . VAL C 1 141 ? 24.640  43.302  75.274  1.00 91.18  ? 144 VAL C N   1 
ATOM   5048  C CA  . VAL C 1 141 ? 26.044  42.914  75.402  1.00 86.87  ? 144 VAL C CA  1 
ATOM   5049  C C   . VAL C 1 141 ? 26.415  42.017  74.226  1.00 85.88  ? 144 VAL C C   1 
ATOM   5050  O O   . VAL C 1 141 ? 25.553  41.294  73.707  1.00 80.36  ? 144 VAL C O   1 
ATOM   5051  C CB  . VAL C 1 141 ? 26.319  42.220  76.746  1.00 90.15  ? 144 VAL C CB  1 
ATOM   5052  C CG1 . VAL C 1 141 ? 26.448  43.252  77.857  1.00 84.67  ? 144 VAL C CG1 1 
ATOM   5053  C CG2 . VAL C 1 141 ? 25.224  41.217  77.070  1.00 88.42  ? 144 VAL C CG2 1 
ATOM   5054  N N   . PRO C 1 142 ? 27.669  42.040  73.770  1.00 93.69  ? 145 PRO C N   1 
ATOM   5055  C CA  . PRO C 1 142 ? 28.039  41.258  72.580  1.00 82.32  ? 145 PRO C CA  1 
ATOM   5056  C C   . PRO C 1 142 ? 27.748  39.774  72.749  1.00 78.22  ? 145 PRO C C   1 
ATOM   5057  O O   . PRO C 1 142 ? 27.987  39.187  73.806  1.00 73.61  ? 145 PRO C O   1 
ATOM   5058  C CB  . PRO C 1 142 ? 29.543  41.516  72.431  1.00 81.05  ? 145 PRO C CB  1 
ATOM   5059  C CG  . PRO C 1 142 ? 29.852  42.713  73.259  1.00 76.01  ? 145 PRO C CG  1 
ATOM   5060  C CD  . PRO C 1 142 ? 28.687  43.040  74.137  1.00 84.09  ? 145 PRO C CD  1 
ATOM   5061  N N   . SER C 1 143 ? 27.239  39.171  71.677  1.00 88.43  ? 146 SER C N   1 
ATOM   5062  C CA  . SER C 1 143 ? 26.877  37.759  71.649  1.00 92.10  ? 146 SER C CA  1 
ATOM   5063  C C   . SER C 1 143 ? 27.189  37.224  70.254  1.00 76.47  ? 146 SER C C   1 
ATOM   5064  O O   . SER C 1 143 ? 27.896  37.862  69.468  1.00 85.21  ? 146 SER C O   1 
ATOM   5065  C CB  . SER C 1 143 ? 25.403  37.566  72.034  1.00 80.03  ? 146 SER C CB  1 
ATOM   5066  O OG  . SER C 1 143 ? 25.205  36.326  72.690  1.00 76.39  ? 146 SER C OG  1 
ATOM   5067  N N   . PHE C 1 144 ? 26.662  36.042  69.944  1.00 71.24  ? 147 PHE C N   1 
ATOM   5068  C CA  . PHE C 1 144 ? 26.897  35.409  68.654  1.00 74.35  ? 147 PHE C CA  1 
ATOM   5069  C C   . PHE C 1 144 ? 25.679  34.571  68.287  1.00 76.95  ? 147 PHE C C   1 
ATOM   5070  O O   . PHE C 1 144 ? 24.714  34.471  69.050  1.00 79.58  ? 147 PHE C O   1 
ATOM   5071  C CB  . PHE C 1 144 ? 28.167  34.554  68.689  1.00 59.16  ? 147 PHE C CB  1 
ATOM   5072  C CG  . PHE C 1 144 ? 28.689  34.185  67.333  1.00 65.66  ? 147 PHE C CG  1 
ATOM   5073  C CD1 . PHE C 1 144 ? 28.916  35.159  66.374  1.00 70.37  ? 147 PHE C CD1 1 
ATOM   5074  C CD2 . PHE C 1 144 ? 28.948  32.863  67.015  1.00 65.80  ? 147 PHE C CD2 1 
ATOM   5075  C CE1 . PHE C 1 144 ? 29.396  34.821  65.125  1.00 69.23  ? 147 PHE C CE1 1 
ATOM   5076  C CE2 . PHE C 1 144 ? 29.431  32.518  65.767  1.00 65.60  ? 147 PHE C CE2 1 
ATOM   5077  C CZ  . PHE C 1 144 ? 29.654  33.497  64.821  1.00 58.47  ? 147 PHE C CZ  1 
ATOM   5078  N N   . PHE C 1 145 ? 25.729  33.976  67.097  1.00 79.72  ? 148 PHE C N   1 
ATOM   5079  C CA  . PHE C 1 145 ? 24.716  33.008  66.703  1.00 72.64  ? 148 PHE C CA  1 
ATOM   5080  C C   . PHE C 1 145 ? 24.695  31.844  67.687  1.00 74.58  ? 148 PHE C C   1 
ATOM   5081  O O   . PHE C 1 145 ? 25.741  31.349  68.116  1.00 81.35  ? 148 PHE C O   1 
ATOM   5082  C CB  . PHE C 1 145 ? 24.987  32.495  65.289  1.00 65.87  ? 148 PHE C CB  1 
ATOM   5083  C CG  . PHE C 1 145 ? 24.905  33.554  64.224  1.00 72.12  ? 148 PHE C CG  1 
ATOM   5084  C CD1 . PHE C 1 145 ? 23.680  34.062  63.822  1.00 72.20  ? 148 PHE C CD1 1 
ATOM   5085  C CD2 . PHE C 1 145 ? 26.053  34.032  63.614  1.00 71.72  ? 148 PHE C CD2 1 
ATOM   5086  C CE1 . PHE C 1 145 ? 23.602  35.031  62.838  1.00 66.11  ? 148 PHE C CE1 1 
ATOM   5087  C CE2 . PHE C 1 145 ? 25.982  35.005  62.628  1.00 77.67  ? 148 PHE C CE2 1 
ATOM   5088  C CZ  . PHE C 1 145 ? 24.754  35.505  62.241  1.00 62.93  ? 148 PHE C CZ  1 
ATOM   5089  N N   . ARG C 1 146 ? 23.490  31.411  68.048  1.00 62.77  ? 149 ARG C N   1 
ATOM   5090  C CA  . ARG C 1 146 ? 23.334  30.381  69.066  1.00 62.97  ? 149 ARG C CA  1 
ATOM   5091  C C   . ARG C 1 146 ? 23.636  28.978  68.558  1.00 64.46  ? 149 ARG C C   1 
ATOM   5092  O O   . ARG C 1 146 ? 23.957  28.100  69.366  1.00 62.50  ? 149 ARG C O   1 
ATOM   5093  C CB  . ARG C 1 146 ? 21.914  30.422  69.616  1.00 63.14  ? 149 ARG C CB  1 
ATOM   5094  C CG  . ARG C 1 146 ? 21.518  31.781  70.127  1.00 70.57  ? 149 ARG C CG  1 
ATOM   5095  C CD  . ARG C 1 146 ? 22.069  32.034  71.519  1.00 82.01  ? 149 ARG C CD  1 
ATOM   5096  N NE  . ARG C 1 146 ? 21.343  33.101  72.200  1.00 98.07  ? 149 ARG C NE  1 
ATOM   5097  C CZ  . ARG C 1 146 ? 20.026  33.157  72.361  1.00 99.33  ? 149 ARG C CZ  1 
ATOM   5098  N NH1 . ARG C 1 146 ? 19.236  32.154  72.008  1.00 104.72 ? 149 ARG C NH1 1 
ATOM   5099  N NH2 . ARG C 1 146 ? 19.488  34.245  72.899  1.00 98.84  ? 149 ARG C NH2 1 
ATOM   5100  N N   . ASN C 1 147 ? 23.532  28.742  67.252  1.00 70.24  ? 150 ASN C N   1 
ATOM   5101  C CA  . ASN C 1 147 ? 23.670  27.400  66.705  1.00 69.38  ? 150 ASN C CA  1 
ATOM   5102  C C   . ASN C 1 147 ? 25.017  27.149  66.040  1.00 62.93  ? 150 ASN C C   1 
ATOM   5103  O O   . ASN C 1 147 ? 25.280  26.014  65.629  1.00 61.32  ? 150 ASN C O   1 
ATOM   5104  C CB  . ASN C 1 147 ? 22.539  27.124  65.703  1.00 76.21  ? 150 ASN C CB  1 
ATOM   5105  C CG  . ASN C 1 147 ? 21.170  27.483  66.258  1.00 69.01  ? 150 ASN C CG  1 
ATOM   5106  O OD1 . ASN C 1 147 ? 20.883  27.250  67.431  1.00 73.61  ? 150 ASN C OD1 1 
ATOM   5107  N ND2 . ASN C 1 147 ? 20.321  28.055  65.415  1.00 66.41  ? 150 ASN C ND2 1 
ATOM   5108  N N   . VAL C 1 148 ? 25.872  28.167  65.926  1.00 67.95  ? 151 VAL C N   1 
ATOM   5109  C CA  . VAL C 1 148 ? 27.226  28.009  65.412  1.00 68.51  ? 151 VAL C CA  1 
ATOM   5110  C C   . VAL C 1 148 ? 28.197  28.672  66.384  1.00 70.94  ? 151 VAL C C   1 
ATOM   5111  O O   . VAL C 1 148 ? 27.824  29.539  67.178  1.00 69.50  ? 151 VAL C O   1 
ATOM   5112  C CB  . VAL C 1 148 ? 27.394  28.591  63.991  1.00 59.91  ? 151 VAL C CB  1 
ATOM   5113  C CG1 . VAL C 1 148 ? 26.520  27.848  63.005  1.00 58.97  ? 151 VAL C CG1 1 
ATOM   5114  C CG2 . VAL C 1 148 ? 27.068  30.069  63.976  1.00 61.63  ? 151 VAL C CG2 1 
ATOM   5115  N N   . VAL C 1 149 ? 29.459  28.247  66.315  1.00 59.41  ? 152 VAL C N   1 
ATOM   5116  C CA  . VAL C 1 149 ? 30.481  28.634  67.282  1.00 72.71  ? 152 VAL C CA  1 
ATOM   5117  C C   . VAL C 1 149 ? 31.648  29.278  66.542  1.00 70.18  ? 152 VAL C C   1 
ATOM   5118  O O   . VAL C 1 149 ? 32.148  28.722  65.557  1.00 73.13  ? 152 VAL C O   1 
ATOM   5119  C CB  . VAL C 1 149 ? 30.958  27.427  68.111  1.00 70.68  ? 152 VAL C CB  1 
ATOM   5120  C CG1 . VAL C 1 149 ? 32.388  27.631  68.583  1.00 75.60  ? 152 VAL C CG1 1 
ATOM   5121  C CG2 . VAL C 1 149 ? 30.034  27.199  69.296  1.00 70.27  ? 152 VAL C CG2 1 
ATOM   5122  N N   . TRP C 1 150 ? 32.080  30.443  67.025  1.00 65.65  ? 153 TRP C N   1 
ATOM   5123  C CA  . TRP C 1 150 ? 33.213  31.168  66.457  1.00 64.39  ? 153 TRP C CA  1 
ATOM   5124  C C   . TRP C 1 150 ? 34.501  30.621  67.070  1.00 67.68  ? 153 TRP C C   1 
ATOM   5125  O O   . TRP C 1 150 ? 34.808  30.891  68.236  1.00 67.89  ? 153 TRP C O   1 
ATOM   5126  C CB  . TRP C 1 150 ? 33.067  32.666  66.718  1.00 56.42  ? 153 TRP C CB  1 
ATOM   5127  C CG  . TRP C 1 150 ? 33.932  33.539  65.858  1.00 55.40  ? 153 TRP C CG  1 
ATOM   5128  C CD1 . TRP C 1 150 ? 34.989  33.147  65.088  1.00 59.92  ? 153 TRP C CD1 1 
ATOM   5129  C CD2 . TRP C 1 150 ? 33.814  34.957  65.687  1.00 49.52  ? 153 TRP C CD2 1 
ATOM   5130  N NE1 . TRP C 1 150 ? 35.534  34.233  64.444  1.00 52.36  ? 153 TRP C NE1 1 
ATOM   5131  C CE2 . TRP C 1 150 ? 34.832  35.356  64.797  1.00 45.22  ? 153 TRP C CE2 1 
ATOM   5132  C CE3 . TRP C 1 150 ? 32.945  35.927  66.198  1.00 61.09  ? 153 TRP C CE3 1 
ATOM   5133  C CZ2 . TRP C 1 150 ? 35.005  36.684  64.406  1.00 58.93  ? 153 TRP C CZ2 1 
ATOM   5134  C CZ3 . TRP C 1 150 ? 33.121  37.247  65.811  1.00 64.00  ? 153 TRP C CZ3 1 
ATOM   5135  C CH2 . TRP C 1 150 ? 34.142  37.612  64.923  1.00 63.13  ? 153 TRP C CH2 1 
ATOM   5136  N N   . LEU C 1 151 ? 35.257  29.860  66.280  1.00 65.26  ? 154 LEU C N   1 
ATOM   5137  C CA  . LEU C 1 151 ? 36.465  29.192  66.754  1.00 70.22  ? 154 LEU C CA  1 
ATOM   5138  C C   . LEU C 1 151 ? 37.658  30.130  66.589  1.00 69.05  ? 154 LEU C C   1 
ATOM   5139  O O   . LEU C 1 151 ? 38.102  30.386  65.466  1.00 79.17  ? 154 LEU C O   1 
ATOM   5140  C CB  . LEU C 1 151 ? 36.690  27.886  65.993  1.00 64.31  ? 154 LEU C CB  1 
ATOM   5141  C CG  . LEU C 1 151 ? 35.882  26.656  66.418  1.00 61.25  ? 154 LEU C CG  1 
ATOM   5142  C CD1 . LEU C 1 151 ? 36.470  25.389  65.817  1.00 62.34  ? 154 LEU C CD1 1 
ATOM   5143  C CD2 . LEU C 1 151 ? 35.817  26.541  67.929  1.00 65.72  ? 154 LEU C CD2 1 
ATOM   5144  N N   . THR C 1 152 ? 38.178  30.636  67.708  1.00 81.91  ? 155 THR C N   1 
ATOM   5145  C CA  . THR C 1 152 ? 39.389  31.443  67.724  1.00 79.08  ? 155 THR C CA  1 
ATOM   5146  C C   . THR C 1 152 ? 40.560  30.613  68.251  1.00 77.14  ? 155 THR C C   1 
ATOM   5147  O O   . THR C 1 152 ? 40.426  29.430  68.576  1.00 75.42  ? 155 THR C O   1 
ATOM   5148  C CB  . THR C 1 152 ? 39.198  32.707  68.567  1.00 74.60  ? 155 THR C CB  1 
ATOM   5149  O OG1 . THR C 1 152 ? 38.422  32.401  69.733  1.00 88.04  ? 155 THR C OG1 1 
ATOM   5150  C CG2 . THR C 1 152 ? 38.498  33.792  67.760  1.00 75.38  ? 155 THR C CG2 1 
ATOM   5151  N N   . LYS C 1 153 ? 41.726  31.247  68.340  1.00 79.73  ? 156 LYS C N   1 
ATOM   5152  C CA  . LYS C 1 153 ? 42.935  30.547  68.747  1.00 83.19  ? 156 LYS C CA  1 
ATOM   5153  C C   . LYS C 1 153 ? 43.025  30.437  70.266  1.00 74.80  ? 156 LYS C C   1 
ATOM   5154  O O   . LYS C 1 153 ? 42.517  31.284  71.008  1.00 62.01  ? 156 LYS C O   1 
ATOM   5155  C CB  . LYS C 1 153 ? 44.175  31.257  68.204  1.00 79.57  ? 156 LYS C CB  1 
ATOM   5156  C CG  . LYS C 1 153 ? 44.292  32.710  68.624  1.00 75.33  ? 156 LYS C CG  1 
ATOM   5157  C CD  . LYS C 1 153 ? 45.653  33.276  68.260  1.00 86.16  ? 156 LYS C CD  1 
ATOM   5158  C CE  . LYS C 1 153 ? 45.815  34.688  68.789  1.00 82.29  ? 156 LYS C CE  1 
ATOM   5159  N NZ  . LYS C 1 153 ? 46.513  35.554  67.804  1.00 87.07  ? 156 LYS C NZ  1 
ATOM   5160  N N   . LYS C 1 154 ? 43.680  29.371  70.723  1.00 79.02  ? 157 LYS C N   1 
ATOM   5161  C CA  . LYS C 1 154 ? 43.917  29.123  72.139  1.00 82.96  ? 157 LYS C CA  1 
ATOM   5162  C C   . LYS C 1 154 ? 45.413  28.989  72.379  1.00 82.48  ? 157 LYS C C   1 
ATOM   5163  O O   . LYS C 1 154 ? 46.086  28.208  71.697  1.00 92.91  ? 157 LYS C O   1 
ATOM   5164  C CB  . LYS C 1 154 ? 43.189  27.858  72.606  1.00 80.21  ? 157 LYS C CB  1 
ATOM   5165  C CG  . LYS C 1 154 ? 43.180  27.662  74.113  1.00 86.65  ? 157 LYS C CG  1 
ATOM   5166  C CD  . LYS C 1 154 ? 42.040  26.745  74.543  1.00 89.58  ? 157 LYS C CD  1 
ATOM   5167  C CE  . LYS C 1 154 ? 42.252  26.211  75.954  1.00 82.60  ? 157 LYS C CE  1 
ATOM   5168  N NZ  . LYS C 1 154 ? 42.152  24.724  76.023  1.00 77.32  ? 157 LYS C NZ  1 
ATOM   5169  N N   . ASN C 1 155 ? 45.926  29.748  73.351  1.00 87.90  ? 158 ASN C N   1 
ATOM   5170  C CA  . ASN C 1 155 ? 47.344  29.717  73.725  1.00 89.16  ? 158 ASN C CA  1 
ATOM   5171  C C   . ASN C 1 155 ? 48.248  30.031  72.533  1.00 93.93  ? 158 ASN C C   1 
ATOM   5172  O O   . ASN C 1 155 ? 49.279  29.385  72.326  1.00 84.07  ? 158 ASN C O   1 
ATOM   5173  C CB  . ASN C 1 155 ? 47.718  28.371  74.351  1.00 76.39  ? 158 ASN C CB  1 
ATOM   5174  C CG  . ASN C 1 155 ? 47.241  28.245  75.782  1.00 78.52  ? 158 ASN C CG  1 
ATOM   5175  O OD1 . ASN C 1 155 ? 47.218  29.224  76.527  1.00 87.92  ? 158 ASN C OD1 1 
ATOM   5176  N ND2 . ASN C 1 155 ? 46.849  27.037  76.174  1.00 71.26  ? 158 ASN C ND2 1 
ATOM   5177  N N   . ASP C 1 156 ? 47.856  31.038  71.746  1.00 101.53 ? 159 ASP C N   1 
ATOM   5178  C CA  . ASP C 1 156 ? 48.590  31.441  70.544  1.00 94.82  ? 159 ASP C CA  1 
ATOM   5179  C C   . ASP C 1 156 ? 48.785  30.259  69.597  1.00 95.17  ? 159 ASP C C   1 
ATOM   5180  O O   . ASP C 1 156 ? 49.835  30.104  68.970  1.00 99.34  ? 159 ASP C O   1 
ATOM   5181  C CB  . ASP C 1 156 ? 49.933  32.084  70.902  1.00 94.52  ? 159 ASP C CB  1 
ATOM   5182  C CG  . ASP C 1 156 ? 50.454  33.001  69.808  1.00 97.75  ? 159 ASP C CG  1 
ATOM   5183  O OD1 . ASP C 1 156 ? 49.633  33.697  69.173  1.00 93.53  ? 159 ASP C OD1 1 
ATOM   5184  O OD2 . ASP C 1 156 ? 51.685  33.024  69.585  1.00 98.17  ? 159 ASP C OD2 1 
ATOM   5185  N N   . ALA C 1 157 ? 47.761  29.415  69.493  1.00 88.19  ? 160 ALA C N   1 
ATOM   5186  C CA  . ALA C 1 157 ? 47.833  28.231  68.653  1.00 85.91  ? 160 ALA C CA  1 
ATOM   5187  C C   . ALA C 1 157 ? 46.466  27.953  68.047  1.00 88.29  ? 160 ALA C C   1 
ATOM   5188  O O   . ALA C 1 157 ? 45.432  28.178  68.685  1.00 79.77  ? 160 ALA C O   1 
ATOM   5189  C CB  . ALA C 1 157 ? 48.318  27.010  69.443  1.00 72.07  ? 160 ALA C CB  1 
ATOM   5190  N N   . TYR C 1 158 ? 46.475  27.481  66.805  1.00 82.34  ? 161 TYR C N   1 
ATOM   5191  C CA  . TYR C 1 158 ? 45.279  26.998  66.119  1.00 71.57  ? 161 TYR C CA  1 
ATOM   5192  C C   . TYR C 1 158 ? 45.643  25.665  65.480  1.00 59.60  ? 161 TYR C C   1 
ATOM   5193  O O   . TYR C 1 158 ? 46.044  25.612  64.309  1.00 55.62  ? 161 TYR C O   1 
ATOM   5194  C CB  . TYR C 1 158 ? 44.779  28.008  65.088  1.00 65.82  ? 161 TYR C CB  1 
ATOM   5195  C CG  . TYR C 1 158 ? 43.318  27.853  64.714  1.00 71.74  ? 161 TYR C CG  1 
ATOM   5196  C CD1 . TYR C 1 158 ? 42.869  26.737  64.013  1.00 66.98  ? 161 TYR C CD1 1 
ATOM   5197  C CD2 . TYR C 1 158 ? 42.389  28.832  65.045  1.00 74.41  ? 161 TYR C CD2 1 
ATOM   5198  C CE1 . TYR C 1 158 ? 41.537  26.599  63.661  1.00 59.96  ? 161 TYR C CE1 1 
ATOM   5199  C CE2 . TYR C 1 158 ? 41.053  28.702  64.696  1.00 68.57  ? 161 TYR C CE2 1 
ATOM   5200  C CZ  . TYR C 1 158 ? 40.634  27.584  64.004  1.00 70.28  ? 161 TYR C CZ  1 
ATOM   5201  O OH  . TYR C 1 158 ? 39.305  27.455  63.656  1.00 73.60  ? 161 TYR C OH  1 
ATOM   5202  N N   . PRO C 1 159 ? 45.558  24.572  66.237  1.00 68.04  ? 162 PRO C N   1 
ATOM   5203  C CA  . PRO C 1 159 ? 45.801  23.248  65.650  1.00 58.95  ? 162 PRO C CA  1 
ATOM   5204  C C   . PRO C 1 159 ? 44.778  22.932  64.570  1.00 72.92  ? 162 PRO C C   1 
ATOM   5205  O O   . PRO C 1 159 ? 43.620  23.354  64.634  1.00 67.02  ? 162 PRO C O   1 
ATOM   5206  C CB  . PRO C 1 159 ? 45.664  22.296  66.845  1.00 56.43  ? 162 PRO C CB  1 
ATOM   5207  C CG  . PRO C 1 159 ? 45.833  23.163  68.059  1.00 68.39  ? 162 PRO C CG  1 
ATOM   5208  C CD  . PRO C 1 159 ? 45.286  24.504  67.683  1.00 67.45  ? 162 PRO C CD  1 
ATOM   5209  N N   . THR C 1 160 ? 45.222  22.178  63.568  1.00 73.35  ? 163 THR C N   1 
ATOM   5210  C CA  . THR C 1 160 ? 44.363  21.827  62.443  1.00 68.53  ? 163 THR C CA  1 
ATOM   5211  C C   . THR C 1 160 ? 43.258  20.878  62.899  1.00 79.57  ? 163 THR C C   1 
ATOM   5212  O O   . THR C 1 160 ? 43.536  19.803  63.442  1.00 74.12  ? 163 THR C O   1 
ATOM   5213  C CB  . THR C 1 160 ? 45.192  21.195  61.326  1.00 70.91  ? 163 THR C CB  1 
ATOM   5214  O OG1 . THR C 1 160 ? 45.914  22.218  60.630  1.00 67.50  ? 163 THR C OG1 1 
ATOM   5215  C CG2 . THR C 1 160 ? 44.295  20.456  60.338  1.00 76.97  ? 163 THR C CG2 1 
ATOM   5216  N N   . ILE C 1 161 ? 42.007  21.275  62.665  1.00 72.65  ? 164 ILE C N   1 
ATOM   5217  C CA  . ILE C 1 161 ? 40.850  20.486  63.075  1.00 58.24  ? 164 ILE C CA  1 
ATOM   5218  C C   . ILE C 1 161 ? 40.612  19.380  62.058  1.00 60.51  ? 164 ILE C C   1 
ATOM   5219  O O   . ILE C 1 161 ? 40.620  19.623  60.846  1.00 61.71  ? 164 ILE C O   1 
ATOM   5220  C CB  . ILE C 1 161 ? 39.606  21.377  63.218  1.00 67.77  ? 164 ILE C CB  1 
ATOM   5221  C CG1 . ILE C 1 161 ? 39.729  22.281  64.444  1.00 59.43  ? 164 ILE C CG1 1 
ATOM   5222  C CG2 . ILE C 1 161 ? 38.340  20.531  63.297  1.00 68.83  ? 164 ILE C CG2 1 
ATOM   5223  C CD1 . ILE C 1 161 ? 39.509  23.743  64.138  1.00 62.13  ? 164 ILE C CD1 1 
ATOM   5224  N N   . LYS C 1 162 ? 40.408  18.157  62.551  1.00 65.27  ? 165 LYS C N   1 
ATOM   5225  C CA  . LYS C 1 162 ? 40.035  17.002  61.732  1.00 64.87  ? 165 LYS C CA  1 
ATOM   5226  C C   . LYS C 1 162 ? 38.906  16.292  62.475  1.00 68.35  ? 165 LYS C C   1 
ATOM   5227  O O   . LYS C 1 162 ? 39.152  15.403  63.294  1.00 63.84  ? 165 LYS C O   1 
ATOM   5228  C CB  . LYS C 1 162 ? 41.228  16.083  61.481  1.00 75.57  ? 165 LYS C CB  1 
ATOM   5229  C CG  . LYS C 1 162 ? 41.966  16.364  60.177  1.00 69.72  ? 165 LYS C CG  1 
ATOM   5230  C CD  . LYS C 1 162 ? 42.441  15.075  59.519  1.00 68.76  ? 165 LYS C CD  1 
ATOM   5231  C CE  . LYS C 1 162 ? 43.303  15.366  58.297  1.00 76.92  ? 165 LYS C CE  1 
ATOM   5232  N NZ  . LYS C 1 162 ? 43.531  14.148  57.465  1.00 70.26  ? 165 LYS C NZ  1 
ATOM   5233  N N   . MET C 1 163 ? 37.669  16.690  62.180  1.00 71.88  ? 166 MET C N   1 
ATOM   5234  C CA  . MET C 1 163 ? 36.491  16.276  62.929  1.00 66.10  ? 166 MET C CA  1 
ATOM   5235  C C   . MET C 1 163 ? 35.437  15.756  61.958  1.00 78.78  ? 166 MET C C   1 
ATOM   5236  O O   . MET C 1 163 ? 35.267  16.300  60.863  1.00 79.62  ? 166 MET C O   1 
ATOM   5237  C CB  . MET C 1 163 ? 35.959  17.464  63.772  1.00 68.04  ? 166 MET C CB  1 
ATOM   5238  C CG  . MET C 1 163 ? 34.473  17.474  64.171  1.00 70.52  ? 166 MET C CG  1 
ATOM   5239  S SD  . MET C 1 163 ? 33.700  15.903  64.634  1.00 119.00 ? 166 MET C SD  1 
ATOM   5240  C CE  . MET C 1 163 ? 34.212  15.708  66.338  1.00 98.14  ? 166 MET C CE  1 
ATOM   5241  N N   . SER C 1 164 ? 34.737  14.696  62.365  1.00 79.38  ? 167 SER C N   1 
ATOM   5242  C CA  . SER C 1 164 ? 33.701  14.068  61.553  1.00 70.83  ? 167 SER C CA  1 
ATOM   5243  C C   . SER C 1 164 ? 32.527  13.661  62.433  1.00 71.44  ? 167 SER C C   1 
ATOM   5244  O O   . SER C 1 164 ? 32.721  13.081  63.504  1.00 70.96  ? 167 SER C O   1 
ATOM   5245  C CB  . SER C 1 164 ? 34.245  12.841  60.815  1.00 64.36  ? 167 SER C CB  1 
ATOM   5246  O OG  . SER C 1 164 ? 34.227  11.700  61.655  1.00 76.81  ? 167 SER C OG  1 
ATOM   5247  N N   . TYR C 1 165 ? 31.310  13.959  61.973  1.00 79.93  ? 168 TYR C N   1 
ATOM   5248  C CA  . TYR C 1 165 ? 30.082  13.628  62.690  1.00 70.65  ? 168 TYR C CA  1 
ATOM   5249  C C   . TYR C 1 165 ? 29.219  12.711  61.835  1.00 72.89  ? 168 TYR C C   1 
ATOM   5250  O O   . TYR C 1 165 ? 28.917  13.033  60.681  1.00 70.74  ? 168 TYR C O   1 
ATOM   5251  C CB  . TYR C 1 165 ? 29.293  14.889  63.063  1.00 60.98  ? 168 TYR C CB  1 
ATOM   5252  C CG  . TYR C 1 165 ? 27.915  14.609  63.631  1.00 79.21  ? 168 TYR C CG  1 
ATOM   5253  C CD1 . TYR C 1 165 ? 27.741  14.330  64.981  1.00 73.67  ? 168 TYR C CD1 1 
ATOM   5254  C CD2 . TYR C 1 165 ? 26.786  14.630  62.817  1.00 74.64  ? 168 TYR C CD2 1 
ATOM   5255  C CE1 . TYR C 1 165 ? 26.487  14.075  65.505  1.00 71.49  ? 168 TYR C CE1 1 
ATOM   5256  C CE2 . TYR C 1 165 ? 25.529  14.374  63.332  1.00 78.97  ? 168 TYR C CE2 1 
ATOM   5257  C CZ  . TYR C 1 165 ? 25.384  14.098  64.675  1.00 81.31  ? 168 TYR C CZ  1 
ATOM   5258  O OH  . TYR C 1 165 ? 24.132  13.844  65.187  1.00 75.24  ? 168 TYR C OH  1 
ATOM   5259  N N   . ASN C 1 166 ? 28.803  11.589  62.414  1.00 75.26  ? 169 ASN C N   1 
ATOM   5260  C CA  . ASN C 1 166 ? 27.977  10.599  61.736  1.00 69.70  ? 169 ASN C CA  1 
ATOM   5261  C C   . ASN C 1 166 ? 26.521  10.814  62.131  1.00 81.45  ? 169 ASN C C   1 
ATOM   5262  O O   . ASN C 1 166 ? 26.204  10.913  63.321  1.00 86.06  ? 169 ASN C O   1 
ATOM   5263  C CB  . ASN C 1 166 ? 28.442  9.187   62.106  1.00 65.60  ? 169 ASN C CB  1 
ATOM   5264  C CG  . ASN C 1 166 ? 27.708  8.088   61.346  1.00 77.60  ? 169 ASN C CG  1 
ATOM   5265  O OD1 . ASN C 1 166 ? 26.477  8.026   61.340  1.00 68.84  ? 169 ASN C OD1 1 
ATOM   5266  N ND2 . ASN C 1 166 ? 28.475  7.198   60.711  1.00 73.70  ? 169 ASN C ND2 1 
ATOM   5267  N N   . ASN C 1 167 ? 25.639  10.896  61.134  1.00 77.29  ? 170 ASN C N   1 
ATOM   5268  C CA  . ASN C 1 167 ? 24.217  11.058  61.412  1.00 77.71  ? 170 ASN C CA  1 
ATOM   5269  C C   . ASN C 1 167 ? 23.628  9.748   61.920  1.00 82.99  ? 170 ASN C C   1 
ATOM   5270  O O   . ASN C 1 167 ? 23.217  8.895   61.126  1.00 70.48  ? 170 ASN C O   1 
ATOM   5271  C CB  . ASN C 1 167 ? 23.464  11.532  60.167  1.00 71.78  ? 170 ASN C CB  1 
ATOM   5272  C CG  . ASN C 1 167 ? 22.041  11.972  60.476  1.00 74.39  ? 170 ASN C CG  1 
ATOM   5273  O OD1 . ASN C 1 167 ? 21.680  12.180  61.634  1.00 70.66  ? 170 ASN C OD1 1 
ATOM   5274  N ND2 . ASN C 1 167 ? 21.226  12.110  59.437  1.00 75.61  ? 170 ASN C ND2 1 
ATOM   5275  N N   . THR C 1 168 ? 23.590  9.582   63.245  1.00 86.19  ? 171 THR C N   1 
ATOM   5276  C CA  . THR C 1 168 ? 23.067  8.368   63.859  1.00 91.24  ? 171 THR C CA  1 
ATOM   5277  C C   . THR C 1 168 ? 21.554  8.392   64.030  1.00 83.02  ? 171 THR C C   1 
ATOM   5278  O O   . THR C 1 168 ? 20.976  7.368   64.413  1.00 74.30  ? 171 THR C O   1 
ATOM   5279  C CB  . THR C 1 168 ? 23.723  8.134   65.221  1.00 83.02  ? 171 THR C CB  1 
ATOM   5280  O OG1 . THR C 1 168 ? 23.877  9.387   65.899  1.00 81.02  ? 171 THR C OG1 1 
ATOM   5281  C CG2 . THR C 1 168 ? 25.086  7.477   65.050  1.00 79.92  ? 171 THR C CG2 1 
ATOM   5282  N N   . ASN C 1 169 ? 20.908  9.527   63.774  1.00 78.71  ? 172 ASN C N   1 
ATOM   5283  C CA  . ASN C 1 169 ? 19.457  9.590   63.802  1.00 78.00  ? 172 ASN C CA  1 
ATOM   5284  C C   . ASN C 1 169 ? 18.875  8.914   62.562  1.00 81.22  ? 172 ASN C C   1 
ATOM   5285  O O   . ASN C 1 169 ? 19.572  8.630   61.582  1.00 87.40  ? 172 ASN C O   1 
ATOM   5286  C CB  . ASN C 1 169 ? 18.982  11.040  63.883  1.00 83.63  ? 172 ASN C CB  1 
ATOM   5287  C CG  . ASN C 1 169 ? 19.756  11.851  64.899  1.00 92.17  ? 172 ASN C CG  1 
ATOM   5288  O OD1 . ASN C 1 169 ? 20.848  12.347  64.615  1.00 86.59  ? 172 ASN C OD1 1 
ATOM   5289  N ND2 . ASN C 1 169 ? 19.190  11.998  66.092  1.00 97.82  ? 172 ASN C ND2 1 
ATOM   5290  N N   . GLY C 1 170 ? 17.577  8.650   62.615  1.00 73.63  ? 173 GLY C N   1 
ATOM   5291  C CA  . GLY C 1 170 ? 16.869  8.060   61.502  1.00 86.35  ? 173 GLY C CA  1 
ATOM   5292  C C   . GLY C 1 170 ? 16.264  9.049   60.533  1.00 77.92  ? 173 GLY C C   1 
ATOM   5293  O O   . GLY C 1 170 ? 15.516  8.642   59.639  1.00 80.96  ? 173 GLY C O   1 
ATOM   5294  N N   . GLU C 1 171 ? 16.559  10.339  60.682  1.00 73.00  ? 174 GLU C N   1 
ATOM   5295  C CA  . GLU C 1 171 ? 15.959  11.380  59.863  1.00 78.45  ? 174 GLU C CA  1 
ATOM   5296  C C   . GLU C 1 171 ? 17.044  12.287  59.295  1.00 79.19  ? 174 GLU C C   1 
ATOM   5297  O O   . GLU C 1 171 ? 18.179  12.316  59.778  1.00 77.10  ? 174 GLU C O   1 
ATOM   5298  C CB  . GLU C 1 171 ? 14.938  12.200  60.668  1.00 73.06  ? 174 GLU C CB  1 
ATOM   5299  C CG  . GLU C 1 171 ? 13.751  11.377  61.176  1.00 80.89  ? 174 GLU C CG  1 
ATOM   5300  C CD  . GLU C 1 171 ? 12.819  12.169  62.081  1.00 89.52  ? 174 GLU C CD  1 
ATOM   5301  O OE1 . GLU C 1 171 ? 13.112  13.352  62.355  1.00 92.35  ? 174 GLU C OE1 1 
ATOM   5302  O OE2 . GLU C 1 171 ? 11.789  11.609  62.516  1.00 81.28  ? 174 GLU C OE2 1 
ATOM   5303  N N   . ASP C 1 172 ? 16.680  13.023  58.247  1.00 83.64  ? 175 ASP C N   1 
ATOM   5304  C CA  . ASP C 1 172 ? 17.629  13.907  57.585  1.00 74.19  ? 175 ASP C CA  1 
ATOM   5305  C C   . ASP C 1 172 ? 18.074  15.022  58.523  1.00 76.76  ? 175 ASP C C   1 
ATOM   5306  O O   . ASP C 1 172 ? 17.302  15.518  59.349  1.00 69.87  ? 175 ASP C O   1 
ATOM   5307  C CB  . ASP C 1 172 ? 17.008  14.507  56.324  1.00 73.28  ? 175 ASP C CB  1 
ATOM   5308  C CG  . ASP C 1 172 ? 16.884  13.500  55.202  1.00 86.60  ? 175 ASP C CG  1 
ATOM   5309  O OD1 . ASP C 1 172 ? 17.582  12.465  55.255  1.00 83.30  ? 175 ASP C OD1 1 
ATOM   5310  O OD2 . ASP C 1 172 ? 16.088  13.742  54.269  1.00 88.49  ? 175 ASP C OD2 1 
ATOM   5311  N N   . LEU C 1 173 ? 19.338  15.417  58.387  1.00 59.97  ? 176 LEU C N   1 
ATOM   5312  C CA  . LEU C 1 173 ? 19.937  16.447  59.224  1.00 60.56  ? 176 LEU C CA  1 
ATOM   5313  C C   . LEU C 1 173 ? 20.346  17.629  58.356  1.00 52.62  ? 176 LEU C C   1 
ATOM   5314  O O   . LEU C 1 173 ? 21.151  17.477  57.430  1.00 52.49  ? 176 LEU C O   1 
ATOM   5315  C CB  . LEU C 1 173 ? 21.143  15.890  59.985  1.00 65.59  ? 176 LEU C CB  1 
ATOM   5316  C CG  . LEU C 1 173 ? 21.380  16.401  61.408  1.00 61.80  ? 176 LEU C CG  1 
ATOM   5317  C CD1 . LEU C 1 173 ? 20.092  16.441  62.209  1.00 59.02  ? 176 LEU C CD1 1 
ATOM   5318  C CD2 . LEU C 1 173 ? 22.413  15.536  62.105  1.00 70.71  ? 176 LEU C CD2 1 
ATOM   5319  N N   . LEU C 1 174 ? 19.790  18.800  58.654  1.00 51.72  ? 177 LEU C N   1 
ATOM   5320  C CA  . LEU C 1 174 ? 20.211  20.046  58.028  1.00 55.92  ? 177 LEU C CA  1 
ATOM   5321  C C   . LEU C 1 174 ? 21.308  20.670  58.886  1.00 59.19  ? 177 LEU C C   1 
ATOM   5322  O O   . LEU C 1 174 ? 21.060  21.053  60.034  1.00 63.84  ? 177 LEU C O   1 
ATOM   5323  C CB  . LEU C 1 174 ? 19.029  21.003  57.873  1.00 47.25  ? 177 LEU C CB  1 
ATOM   5324  C CG  . LEU C 1 174 ? 19.376  22.456  57.530  1.00 54.14  ? 177 LEU C CG  1 
ATOM   5325  C CD1 . LEU C 1 174 ? 19.829  22.573  56.083  1.00 50.91  ? 177 LEU C CD1 1 
ATOM   5326  C CD2 . LEU C 1 174 ? 18.208  23.394  57.808  1.00 48.32  ? 177 LEU C CD2 1 
ATOM   5327  N N   . ILE C 1 175 ? 22.516  20.765  58.334  1.00 57.41  ? 178 ILE C N   1 
ATOM   5328  C CA  . ILE C 1 175 ? 23.692  21.234  59.060  1.00 63.51  ? 178 ILE C CA  1 
ATOM   5329  C C   . ILE C 1 175 ? 24.177  22.521  58.411  1.00 53.01  ? 178 ILE C C   1 
ATOM   5330  O O   . ILE C 1 175 ? 24.315  22.589  57.185  1.00 50.25  ? 178 ILE C O   1 
ATOM   5331  C CB  . ILE C 1 175 ? 24.812  20.178  59.072  1.00 60.14  ? 178 ILE C CB  1 
ATOM   5332  C CG1 . ILE C 1 175 ? 24.283  18.848  59.605  1.00 59.66  ? 178 ILE C CG1 1 
ATOM   5333  C CG2 . ILE C 1 175 ? 25.999  20.657  59.902  1.00 57.91  ? 178 ILE C CG2 1 
ATOM   5334  C CD1 . ILE C 1 175 ? 25.236  17.701  59.402  1.00 54.63  ? 178 ILE C CD1 1 
ATOM   5335  N N   . LEU C 1 176 ? 24.436  23.535  59.232  1.00 51.45  ? 179 LEU C N   1 
ATOM   5336  C CA  . LEU C 1 176 ? 24.910  24.827  58.762  1.00 50.24  ? 179 LEU C CA  1 
ATOM   5337  C C   . LEU C 1 176 ? 26.284  25.129  59.344  1.00 63.35  ? 179 LEU C C   1 
ATOM   5338  O O   . LEU C 1 176 ? 26.526  24.917  60.537  1.00 65.58  ? 179 LEU C O   1 
ATOM   5339  C CB  . LEU C 1 176 ? 23.932  25.936  59.137  1.00 50.15  ? 179 LEU C CB  1 
ATOM   5340  C CG  . LEU C 1 176 ? 22.496  25.715  58.673  1.00 64.12  ? 179 LEU C CG  1 
ATOM   5341  C CD1 . LEU C 1 176 ? 21.562  25.611  59.870  1.00 70.31  ? 179 LEU C CD1 1 
ATOM   5342  C CD2 . LEU C 1 176 ? 22.073  26.836  57.746  1.00 58.15  ? 179 LEU C CD2 1 
ATOM   5343  N N   . TRP C 1 177 ? 27.181  25.620  58.491  1.00 57.05  ? 180 TRP C N   1 
ATOM   5344  C CA  . TRP C 1 177 ? 28.510  26.054  58.895  1.00 60.39  ? 180 TRP C CA  1 
ATOM   5345  C C   . TRP C 1 177 ? 28.900  27.262  58.058  1.00 60.65  ? 180 TRP C C   1 
ATOM   5346  O O   . TRP C 1 177 ? 28.230  27.608  57.081  1.00 50.46  ? 180 TRP C O   1 
ATOM   5347  C CB  . TRP C 1 177 ? 29.548  24.939  58.731  1.00 53.59  ? 180 TRP C CB  1 
ATOM   5348  C CG  . TRP C 1 177 ? 29.740  24.543  57.304  1.00 63.06  ? 180 TRP C CG  1 
ATOM   5349  C CD1 . TRP C 1 177 ? 30.717  24.977  56.457  1.00 61.06  ? 180 TRP C CD1 1 
ATOM   5350  C CD2 . TRP C 1 177 ? 28.915  23.651  56.545  1.00 62.01  ? 180 TRP C CD2 1 
ATOM   5351  N NE1 . TRP C 1 177 ? 30.560  24.399  55.219  1.00 60.09  ? 180 TRP C NE1 1 
ATOM   5352  C CE2 . TRP C 1 177 ? 29.462  23.580  55.247  1.00 64.29  ? 180 TRP C CE2 1 
ATOM   5353  C CE3 . TRP C 1 177 ? 27.773  22.900  56.838  1.00 53.52  ? 180 TRP C CE3 1 
ATOM   5354  C CZ2 . TRP C 1 177 ? 28.904  22.789  54.243  1.00 67.96  ? 180 TRP C CZ2 1 
ATOM   5355  C CZ3 . TRP C 1 177 ? 27.221  22.111  55.839  1.00 59.26  ? 180 TRP C CZ3 1 
ATOM   5356  C CH2 . TRP C 1 177 ? 27.786  22.065  54.557  1.00 59.28  ? 180 TRP C CH2 1 
ATOM   5357  N N   . GLY C 1 178 ? 30.007  27.903  58.438  1.00 60.24  ? 181 GLY C N   1 
ATOM   5358  C CA  . GLY C 1 178 ? 30.435  29.096  57.739  1.00 55.52  ? 181 GLY C CA  1 
ATOM   5359  C C   . GLY C 1 178 ? 31.928  29.335  57.814  1.00 67.23  ? 181 GLY C C   1 
ATOM   5360  O O   . GLY C 1 178 ? 32.668  28.653  58.530  1.00 63.11  ? 181 GLY C O   1 
ATOM   5361  N N   . ILE C 1 179 ? 32.363  30.328  57.046  1.00 59.96  ? 182 ILE C N   1 
ATOM   5362  C CA  . ILE C 1 179 ? 33.735  30.808  57.070  1.00 62.39  ? 182 ILE C CA  1 
ATOM   5363  C C   . ILE C 1 179 ? 33.705  32.312  57.315  1.00 68.80  ? 182 ILE C C   1 
ATOM   5364  O O   . ILE C 1 179 ? 32.803  33.013  56.840  1.00 58.11  ? 182 ILE C O   1 
ATOM   5365  C CB  . ILE C 1 179 ? 34.487  30.454  55.768  1.00 63.60  ? 182 ILE C CB  1 
ATOM   5366  C CG1 . ILE C 1 179 ? 36.001  30.598  55.967  1.00 66.76  ? 182 ILE C CG1 1 
ATOM   5367  C CG2 . ILE C 1 179 ? 33.978  31.280  54.594  1.00 54.88  ? 182 ILE C CG2 1 
ATOM   5368  C CD1 . ILE C 1 179 ? 36.800  30.564  54.685  1.00 59.13  ? 182 ILE C CD1 1 
ATOM   5369  N N   . HIS C 1 180 ? 34.669  32.800  58.093  1.00 64.14  ? 183 HIS C N   1 
ATOM   5370  C CA  . HIS C 1 180 ? 34.738  34.204  58.481  1.00 62.89  ? 183 HIS C CA  1 
ATOM   5371  C C   . HIS C 1 180 ? 35.801  34.901  57.641  1.00 63.08  ? 183 HIS C C   1 
ATOM   5372  O O   . HIS C 1 180 ? 36.960  34.472  57.618  1.00 57.63  ? 183 HIS C O   1 
ATOM   5373  C CB  . HIS C 1 180 ? 35.052  34.339  59.972  1.00 63.84  ? 183 HIS C CB  1 
ATOM   5374  C CG  . HIS C 1 180 ? 35.519  35.704  60.376  1.00 66.50  ? 183 HIS C CG  1 
ATOM   5375  N ND1 . HIS C 1 180 ? 36.753  35.932  60.947  1.00 65.50  ? 183 HIS C ND1 1 
ATOM   5376  C CD2 . HIS C 1 180 ? 34.913  36.914  60.296  1.00 59.08  ? 183 HIS C CD2 1 
ATOM   5377  C CE1 . HIS C 1 180 ? 36.889  37.222  61.198  1.00 68.40  ? 183 HIS C CE1 1 
ATOM   5378  N NE2 . HIS C 1 180 ? 35.786  37.840  60.813  1.00 64.47  ? 183 HIS C NE2 1 
ATOM   5379  N N   . HIS C 1 181 ? 35.407  35.972  56.956  1.00 59.24  ? 184 HIS C N   1 
ATOM   5380  C CA  . HIS C 1 181 ? 36.331  36.766  56.151  1.00 64.92  ? 184 HIS C CA  1 
ATOM   5381  C C   . HIS C 1 181 ? 36.881  37.894  57.016  1.00 67.53  ? 184 HIS C C   1 
ATOM   5382  O O   . HIS C 1 181 ? 36.139  38.798  57.417  1.00 65.98  ? 184 HIS C O   1 
ATOM   5383  C CB  . HIS C 1 181 ? 35.633  37.318  54.910  1.00 61.53  ? 184 HIS C CB  1 
ATOM   5384  C CG  . HIS C 1 181 ? 35.131  36.259  53.980  1.00 67.70  ? 184 HIS C CG  1 
ATOM   5385  N ND1 . HIS C 1 181 ? 35.964  35.340  53.380  1.00 68.53  ? 184 HIS C ND1 1 
ATOM   5386  C CD2 . HIS C 1 181 ? 33.880  35.972  53.548  1.00 68.27  ? 184 HIS C CD2 1 
ATOM   5387  C CE1 . HIS C 1 181 ? 35.249  34.531  52.620  1.00 70.05  ? 184 HIS C CE1 1 
ATOM   5388  N NE2 . HIS C 1 181 ? 33.981  34.894  52.703  1.00 70.78  ? 184 HIS C NE2 1 
ATOM   5389  N N   . SER C 1 182 ? 38.179  37.844  57.299  1.00 51.48  ? 185 SER C N   1 
ATOM   5390  C CA  . SER C 1 182 ? 38.820  38.831  58.154  1.00 65.90  ? 185 SER C CA  1 
ATOM   5391  C C   . SER C 1 182 ? 39.329  40.029  57.343  1.00 64.09  ? 185 SER C C   1 
ATOM   5392  O O   . SER C 1 182 ? 39.492  39.970  56.120  1.00 63.76  ? 185 SER C O   1 
ATOM   5393  C CB  . SER C 1 182 ? 39.955  38.180  58.948  1.00 68.03  ? 185 SER C CB  1 
ATOM   5394  O OG  . SER C 1 182 ? 40.792  37.406  58.117  1.00 63.82  ? 185 SER C OG  1 
ATOM   5395  N N   . ASN C 1 183 ? 39.569  41.134  58.053  1.00 59.77  ? 186 ASN C N   1 
ATOM   5396  C CA  . ASN C 1 183 ? 39.769  42.428  57.402  1.00 72.00  ? 186 ASN C CA  1 
ATOM   5397  C C   . ASN C 1 183 ? 41.189  42.621  56.869  1.00 64.05  ? 186 ASN C C   1 
ATOM   5398  O O   . ASN C 1 183 ? 41.371  43.239  55.814  1.00 56.92  ? 186 ASN C O   1 
ATOM   5399  C CB  . ASN C 1 183 ? 39.411  43.551  58.373  1.00 74.50  ? 186 ASN C CB  1 
ATOM   5400  C CG  . ASN C 1 183 ? 37.975  43.465  58.849  1.00 71.42  ? 186 ASN C CG  1 
ATOM   5401  O OD1 . ASN C 1 183 ? 37.049  43.419  58.042  1.00 73.28  ? 186 ASN C OD1 1 
ATOM   5402  N ND2 . ASN C 1 183 ? 37.781  43.438  60.161  1.00 69.60  ? 186 ASN C ND2 1 
ATOM   5403  N N   . ASN C 1 184 ? 42.204  42.131  57.577  1.00 69.21  ? 187 ASN C N   1 
ATOM   5404  C CA  . ASN C 1 184 ? 43.586  42.339  57.153  1.00 66.94  ? 187 ASN C CA  1 
ATOM   5405  C C   . ASN C 1 184 ? 44.467  41.277  57.798  1.00 64.84  ? 187 ASN C C   1 
ATOM   5406  O O   . ASN C 1 184 ? 43.999  40.431  58.565  1.00 71.80  ? 187 ASN C O   1 
ATOM   5407  C CB  . ASN C 1 184 ? 44.077  43.747  57.505  1.00 56.22  ? 187 ASN C CB  1 
ATOM   5408  C CG  . ASN C 1 184 ? 43.811  44.111  58.948  1.00 61.24  ? 187 ASN C CG  1 
ATOM   5409  O OD1 . ASN C 1 184 ? 44.350  43.491  59.865  1.00 61.18  ? 187 ASN C OD1 1 
ATOM   5410  N ND2 . ASN C 1 184 ? 42.969  45.119  59.160  1.00 56.23  ? 187 ASN C ND2 1 
ATOM   5411  N N   . ALA C 1 185 ? 45.763  41.335  57.478  1.00 66.17  ? 188 ALA C N   1 
ATOM   5412  C CA  . ALA C 1 185 ? 46.705  40.343  57.987  1.00 71.01  ? 188 ALA C CA  1 
ATOM   5413  C C   . ALA C 1 185 ? 46.848  40.430  59.502  1.00 67.13  ? 188 ALA C C   1 
ATOM   5414  O O   . ALA C 1 185 ? 46.991  39.403  60.177  1.00 63.55  ? 188 ALA C O   1 
ATOM   5415  C CB  . ALA C 1 185 ? 48.062  40.517  57.309  1.00 51.84  ? 188 ALA C CB  1 
ATOM   5416  N N   . ALA C 1 186 ? 46.823  41.648  60.050  1.00 62.04  ? 189 ALA C N   1 
ATOM   5417  C CA  . ALA C 1 186 ? 46.926  41.815  61.497  1.00 70.24  ? 189 ALA C CA  1 
ATOM   5418  C C   . ALA C 1 186 ? 45.755  41.155  62.210  1.00 74.22  ? 189 ALA C C   1 
ATOM   5419  O O   . ALA C 1 186 ? 45.937  40.466  63.221  1.00 70.23  ? 189 ALA C O   1 
ATOM   5420  C CB  . ALA C 1 186 ? 46.993  43.302  61.849  1.00 60.12  ? 189 ALA C CB  1 
ATOM   5421  N N   . GLU C 1 187 ? 44.542  41.353  61.692  1.00 69.92  ? 190 GLU C N   1 
ATOM   5422  C CA  . GLU C 1 187 ? 43.374  40.719  62.289  1.00 69.03  ? 190 GLU C CA  1 
ATOM   5423  C C   . GLU C 1 187 ? 43.429  39.204  62.124  1.00 68.16  ? 190 GLU C C   1 
ATOM   5424  O O   . GLU C 1 187 ? 43.056  38.461  63.039  1.00 64.96  ? 190 GLU C O   1 
ATOM   5425  C CB  . GLU C 1 187 ? 42.101  41.298  61.671  1.00 76.00  ? 190 GLU C CB  1 
ATOM   5426  C CG  . GLU C 1 187 ? 40.870  41.158  62.550  1.00 89.55  ? 190 GLU C CG  1 
ATOM   5427  C CD  . GLU C 1 187 ? 39.578  41.246  61.766  1.00 85.57  ? 190 GLU C CD  1 
ATOM   5428  O OE1 . GLU C 1 187 ? 39.491  40.634  60.683  1.00 88.17  ? 190 GLU C OE1 1 
ATOM   5429  O OE2 . GLU C 1 187 ? 38.647  41.932  62.235  1.00 82.30  ? 190 GLU C OE2 1 
ATOM   5430  N N   . GLN C 1 188 ? 43.910  38.728  60.972  1.00 62.55  ? 191 GLN C N   1 
ATOM   5431  C CA  . GLN C 1 188 ? 44.002  37.289  60.753  1.00 51.64  ? 191 GLN C CA  1 
ATOM   5432  C C   . GLN C 1 188 ? 44.898  36.630  61.795  1.00 66.63  ? 191 GLN C C   1 
ATOM   5433  O O   . GLN C 1 188 ? 44.544  35.587  62.357  1.00 63.81  ? 191 GLN C O   1 
ATOM   5434  C CB  . GLN C 1 188 ? 44.519  37.009  59.341  1.00 56.91  ? 191 GLN C CB  1 
ATOM   5435  C CG  . GLN C 1 188 ? 44.531  35.533  58.958  1.00 68.55  ? 191 GLN C CG  1 
ATOM   5436  C CD  . GLN C 1 188 ? 43.141  34.925  58.928  1.00 60.27  ? 191 GLN C CD  1 
ATOM   5437  O OE1 . GLN C 1 188 ? 42.154  35.613  58.653  1.00 57.74  ? 191 GLN C OE1 1 
ATOM   5438  N NE2 . GLN C 1 188 ? 43.058  33.628  59.204  1.00 51.61  ? 191 GLN C NE2 1 
ATOM   5439  N N   . ILE C 1 189 ? 46.057  37.232  62.076  1.00 75.16  ? 192 ILE C N   1 
ATOM   5440  C CA  . ILE C 1 189 ? 46.955  36.691  63.093  1.00 73.33  ? 192 ILE C CA  1 
ATOM   5441  C C   . ILE C 1 189 ? 46.333  36.813  64.479  1.00 70.97  ? 192 ILE C C   1 
ATOM   5442  O O   . ILE C 1 189 ? 46.391  35.878  65.287  1.00 67.16  ? 192 ILE C O   1 
ATOM   5443  C CB  . ILE C 1 189 ? 48.324  37.393  63.018  1.00 79.39  ? 192 ILE C CB  1 
ATOM   5444  C CG1 . ILE C 1 189 ? 49.133  36.869  61.826  1.00 89.07  ? 192 ILE C CG1 1 
ATOM   5445  C CG2 . ILE C 1 189 ? 49.103  37.216  64.323  1.00 65.32  ? 192 ILE C CG2 1 
ATOM   5446  C CD1 . ILE C 1 189 ? 48.975  35.378  61.566  1.00 79.59  ? 192 ILE C CD1 1 
ATOM   5447  N N   . ASN C 1 190 ? 45.718  37.962  64.769  1.00 67.38  ? 193 ASN C N   1 
ATOM   5448  C CA  . ASN C 1 190 ? 45.155  38.207  66.090  1.00 71.78  ? 193 ASN C CA  1 
ATOM   5449  C C   . ASN C 1 190 ? 44.040  37.234  66.441  1.00 80.01  ? 193 ASN C C   1 
ATOM   5450  O O   . ASN C 1 190 ? 43.771  37.021  67.628  1.00 82.68  ? 193 ASN C O   1 
ATOM   5451  C CB  . ASN C 1 190 ? 44.626  39.639  66.176  1.00 74.50  ? 193 ASN C CB  1 
ATOM   5452  C CG  . ASN C 1 190 ? 45.456  40.512  67.087  1.00 89.11  ? 193 ASN C CG  1 
ATOM   5453  O OD1 . ASN C 1 190 ? 46.018  40.040  68.078  1.00 104.21 ? 193 ASN C OD1 1 
ATOM   5454  N ND2 . ASN C 1 190 ? 45.541  41.797  66.759  1.00 97.56  ? 193 ASN C ND2 1 
ATOM   5455  N N   . LEU C 1 191 ? 43.384  36.640  65.443  1.00 74.66  ? 194 LEU C N   1 
ATOM   5456  C CA  . LEU C 1 191 ? 42.230  35.784  65.680  1.00 73.99  ? 194 LEU C CA  1 
ATOM   5457  C C   . LEU C 1 191 ? 42.484  34.306  65.430  1.00 66.80  ? 194 LEU C C   1 
ATOM   5458  O O   . LEU C 1 191 ? 41.863  33.474  66.093  1.00 63.26  ? 194 LEU C O   1 
ATOM   5459  C CB  . LEU C 1 191 ? 41.043  36.239  64.819  1.00 74.09  ? 194 LEU C CB  1 
ATOM   5460  C CG  . LEU C 1 191 ? 40.197  37.388  65.381  1.00 70.75  ? 194 LEU C CG  1 
ATOM   5461  C CD1 . LEU C 1 191 ? 40.873  38.739  65.213  1.00 76.05  ? 194 LEU C CD1 1 
ATOM   5462  C CD2 . LEU C 1 191 ? 38.823  37.398  64.735  1.00 73.56  ? 194 LEU C CD2 1 
ATOM   5463  N N   . TYR C 1 192 ? 43.374  33.955  64.499  1.00 70.75  ? 195 TYR C N   1 
ATOM   5464  C CA  . TYR C 1 192 ? 43.631  32.557  64.162  1.00 65.14  ? 195 TYR C CA  1 
ATOM   5465  C C   . TYR C 1 192 ? 45.104  32.179  64.104  1.00 71.96  ? 195 TYR C C   1 
ATOM   5466  O O   . TYR C 1 192 ? 45.401  30.978  64.077  1.00 70.67  ? 195 TYR C O   1 
ATOM   5467  C CB  . TYR C 1 192 ? 42.977  32.204  62.816  1.00 64.24  ? 195 TYR C CB  1 
ATOM   5468  C CG  . TYR C 1 192 ? 41.560  32.717  62.685  1.00 63.78  ? 195 TYR C CG  1 
ATOM   5469  C CD1 . TYR C 1 192 ? 40.508  32.081  63.333  1.00 64.48  ? 195 TYR C CD1 1 
ATOM   5470  C CD2 . TYR C 1 192 ? 41.274  33.843  61.923  1.00 62.58  ? 195 TYR C CD2 1 
ATOM   5471  C CE1 . TYR C 1 192 ? 39.211  32.551  63.224  1.00 63.00  ? 195 TYR C CE1 1 
ATOM   5472  C CE2 . TYR C 1 192 ? 39.980  34.320  61.809  1.00 66.82  ? 195 TYR C CE2 1 
ATOM   5473  C CZ  . TYR C 1 192 ? 38.953  33.669  62.460  1.00 64.29  ? 195 TYR C CZ  1 
ATOM   5474  O OH  . TYR C 1 192 ? 37.665  34.140  62.350  1.00 62.41  ? 195 TYR C OH  1 
ATOM   5475  N N   . LYS C 1 193 ? 46.023  33.146  64.023  1.00 74.03  ? 196 LYS C N   1 
ATOM   5476  C CA  . LYS C 1 193 ? 47.466  32.935  64.146  1.00 81.87  ? 196 LYS C CA  1 
ATOM   5477  C C   . LYS C 1 193 ? 48.043  32.226  62.920  1.00 75.37  ? 196 LYS C C   1 
ATOM   5478  O O   . LYS C 1 193 ? 49.262  32.201  62.721  1.00 86.46  ? 196 LYS C O   1 
ATOM   5479  C CB  . LYS C 1 193 ? 47.766  32.169  65.450  1.00 88.12  ? 196 LYS C CB  1 
ATOM   5480  C CG  . LYS C 1 193 ? 49.083  31.392  65.522  1.00 81.07  ? 196 LYS C CG  1 
ATOM   5481  C CD  . LYS C 1 193 ? 50.267  32.311  65.795  1.00 77.80  ? 196 LYS C CD  1 
ATOM   5482  C CE  . LYS C 1 193 ? 51.576  31.537  65.823  1.00 84.92  ? 196 LYS C CE  1 
ATOM   5483  N NZ  . LYS C 1 193 ? 51.372  30.118  66.238  1.00 83.00  ? 196 LYS C NZ  1 
ATOM   5484  N N   . ASN C 1 194 ? 47.182  31.722  62.044  1.00 67.41  ? 197 ASN C N   1 
ATOM   5485  C CA  . ASN C 1 194 ? 47.634  31.066  60.827  1.00 73.66  ? 197 ASN C CA  1 
ATOM   5486  C C   . ASN C 1 194 ? 47.340  31.970  59.642  1.00 74.77  ? 197 ASN C C   1 
ATOM   5487  O O   . ASN C 1 194 ? 46.172  32.325  59.419  1.00 83.89  ? 197 ASN C O   1 
ATOM   5488  C CB  . ASN C 1 194 ? 46.957  29.709  60.657  1.00 69.25  ? 197 ASN C CB  1 
ATOM   5489  C CG  . ASN C 1 194 ? 47.372  28.720  61.727  1.00 68.43  ? 197 ASN C CG  1 
ATOM   5490  O OD1 . ASN C 1 194 ? 48.485  28.788  62.248  1.00 63.90  ? 197 ASN C OD1 1 
ATOM   5491  N ND2 . ASN C 1 194 ? 46.473  27.803  62.072  1.00 64.99  ? 197 ASN C ND2 1 
ATOM   5492  N N   . PRO C 1 195 ? 48.351  32.381  58.873  1.00 79.31  ? 198 PRO C N   1 
ATOM   5493  C CA  . PRO C 1 195 ? 48.092  33.386  57.829  1.00 77.89  ? 198 PRO C CA  1 
ATOM   5494  C C   . PRO C 1 195 ? 47.372  32.823  56.615  1.00 69.02  ? 198 PRO C C   1 
ATOM   5495  O O   . PRO C 1 195 ? 46.545  33.524  56.018  1.00 58.62  ? 198 PRO C O   1 
ATOM   5496  C CB  . PRO C 1 195 ? 49.496  33.908  57.480  1.00 68.42  ? 198 PRO C CB  1 
ATOM   5497  C CG  . PRO C 1 195 ? 50.472  32.912  58.055  1.00 68.98  ? 198 PRO C CG  1 
ATOM   5498  C CD  . PRO C 1 195 ? 49.734  31.878  58.853  1.00 78.67  ? 198 PRO C CD  1 
ATOM   5499  N N   . THR C 1 196 ? 47.651  31.578  56.234  1.00 64.69  ? 199 THR C N   1 
ATOM   5500  C CA  . THR C 1 196 ? 47.017  30.939  55.086  1.00 63.39  ? 199 THR C CA  1 
ATOM   5501  C C   . THR C 1 196 ? 46.119  29.820  55.603  1.00 71.18  ? 199 THR C C   1 
ATOM   5502  O O   . THR C 1 196 ? 46.611  28.805  56.113  1.00 71.00  ? 199 THR C O   1 
ATOM   5503  C CB  . THR C 1 196 ? 48.065  30.408  54.111  1.00 62.98  ? 199 THR C CB  1 
ATOM   5504  O OG1 . THR C 1 196 ? 48.750  31.514  53.509  1.00 69.02  ? 199 THR C OG1 1 
ATOM   5505  C CG2 . THR C 1 196 ? 47.416  29.569  53.025  1.00 55.58  ? 199 THR C CG2 1 
ATOM   5506  N N   . THR C 1 197 ? 44.807  29.999  55.463  1.00 61.17  ? 200 THR C N   1 
ATOM   5507  C CA  . THR C 1 197 ? 43.838  29.105  56.077  1.00 64.27  ? 200 THR C CA  1 
ATOM   5508  C C   . THR C 1 197 ? 42.859  28.581  55.035  1.00 68.19  ? 200 THR C C   1 
ATOM   5509  O O   . THR C 1 197 ? 42.819  29.036  53.888  1.00 69.81  ? 200 THR C O   1 
ATOM   5510  C CB  . THR C 1 197 ? 43.079  29.805  57.209  1.00 64.75  ? 200 THR C CB  1 
ATOM   5511  O OG1 . THR C 1 197 ? 42.700  31.119  56.782  1.00 64.80  ? 200 THR C OG1 1 
ATOM   5512  C CG2 . THR C 1 197 ? 43.964  29.919  58.442  1.00 66.44  ? 200 THR C CG2 1 
ATOM   5513  N N   . TYR C 1 198 ? 42.060  27.605  55.458  1.00 69.44  ? 201 TYR C N   1 
ATOM   5514  C CA  . TYR C 1 198 ? 41.111  26.945  54.575  1.00 70.47  ? 201 TYR C CA  1 
ATOM   5515  C C   . TYR C 1 198 ? 40.044  26.268  55.423  1.00 75.67  ? 201 TYR C C   1 
ATOM   5516  O O   . TYR C 1 198 ? 40.246  26.001  56.612  1.00 73.33  ? 201 TYR C O   1 
ATOM   5517  C CB  . TYR C 1 198 ? 41.809  25.922  53.671  1.00 63.72  ? 201 TYR C CB  1 
ATOM   5518  C CG  . TYR C 1 198 ? 42.375  24.744  54.429  1.00 61.30  ? 201 TYR C CG  1 
ATOM   5519  C CD1 . TYR C 1 198 ? 43.611  24.828  55.061  1.00 68.58  ? 201 TYR C CD1 1 
ATOM   5520  C CD2 . TYR C 1 198 ? 41.670  23.551  54.525  1.00 61.39  ? 201 TYR C CD2 1 
ATOM   5521  C CE1 . TYR C 1 198 ? 44.130  23.754  55.765  1.00 61.99  ? 201 TYR C CE1 1 
ATOM   5522  C CE2 . TYR C 1 198 ? 42.181  22.473  55.224  1.00 70.94  ? 201 TYR C CE2 1 
ATOM   5523  C CZ  . TYR C 1 198 ? 43.410  22.581  55.841  1.00 63.55  ? 201 TYR C CZ  1 
ATOM   5524  O OH  . TYR C 1 198 ? 43.916  21.510  56.534  1.00 70.45  ? 201 TYR C OH  1 
ATOM   5525  N N   . VAL C 1 199 ? 38.902  25.996  54.796  1.00 69.92  ? 202 VAL C N   1 
ATOM   5526  C CA  . VAL C 1 199 ? 37.827  25.217  55.401  1.00 66.88  ? 202 VAL C CA  1 
ATOM   5527  C C   . VAL C 1 199 ? 37.410  24.145  54.403  1.00 67.77  ? 202 VAL C C   1 
ATOM   5528  O O   . VAL C 1 199 ? 36.947  24.468  53.302  1.00 68.54  ? 202 VAL C O   1 
ATOM   5529  C CB  . VAL C 1 199 ? 36.621  26.089  55.790  1.00 70.10  ? 202 VAL C CB  1 
ATOM   5530  C CG1 . VAL C 1 199 ? 35.492  25.218  56.313  1.00 57.10  ? 202 VAL C CG1 1 
ATOM   5531  C CG2 . VAL C 1 199 ? 37.025  27.129  56.832  1.00 55.76  ? 202 VAL C CG2 1 
ATOM   5532  N N   . SER C 1 200 ? 37.565  22.880  54.786  1.00 62.38  ? 203 SER C N   1 
ATOM   5533  C CA  . SER C 1 200 ? 37.221  21.746  53.937  1.00 56.31  ? 203 SER C CA  1 
ATOM   5534  C C   . SER C 1 200 ? 36.060  20.977  54.548  1.00 56.47  ? 203 SER C C   1 
ATOM   5535  O O   . SER C 1 200 ? 36.126  20.563  55.709  1.00 60.44  ? 203 SER C O   1 
ATOM   5536  C CB  . SER C 1 200 ? 38.415  20.809  53.744  1.00 50.36  ? 203 SER C CB  1 
ATOM   5537  O OG  . SER C 1 200 ? 39.181  21.182  52.613  1.00 76.12  ? 203 SER C OG  1 
ATOM   5538  N N   . VAL C 1 201 ? 35.008  20.772  53.758  1.00 55.54  ? 204 VAL C N   1 
ATOM   5539  C CA  . VAL C 1 201 ? 33.829  20.029  54.186  1.00 60.38  ? 204 VAL C CA  1 
ATOM   5540  C C   . VAL C 1 201 ? 33.572  18.906  53.191  1.00 55.46  ? 204 VAL C C   1 
ATOM   5541  O O   . VAL C 1 201 ? 33.534  19.143  51.978  1.00 61.77  ? 204 VAL C O   1 
ATOM   5542  C CB  . VAL C 1 201 ? 32.596  20.942  54.307  1.00 62.83  ? 204 VAL C CB  1 
ATOM   5543  C CG1 . VAL C 1 201 ? 31.465  20.219  55.036  1.00 53.99  ? 204 VAL C CG1 1 
ATOM   5544  C CG2 . VAL C 1 201 ? 32.977  22.245  55.015  1.00 47.04  ? 204 VAL C CG2 1 
ATOM   5545  N N   . GLY C 1 202 ? 33.399  17.690  53.700  1.00 58.07  ? 205 GLY C N   1 
ATOM   5546  C CA  . GLY C 1 202 ? 33.174  16.547  52.839  1.00 56.25  ? 205 GLY C CA  1 
ATOM   5547  C C   . GLY C 1 202 ? 32.112  15.587  53.341  1.00 68.80  ? 205 GLY C C   1 
ATOM   5548  O O   . GLY C 1 202 ? 32.119  15.185  54.508  1.00 68.08  ? 205 GLY C O   1 
ATOM   5549  N N   . THR C 1 203 ? 31.180  15.220  52.462  1.00 58.28  ? 206 THR C N   1 
ATOM   5550  C CA  . THR C 1 203 ? 30.218  14.161  52.743  1.00 62.43  ? 206 THR C CA  1 
ATOM   5551  C C   . THR C 1 203 ? 30.286  13.129  51.627  1.00 62.98  ? 206 THR C C   1 
ATOM   5552  O O   . THR C 1 203 ? 31.231  13.134  50.829  1.00 56.96  ? 206 THR C O   1 
ATOM   5553  C CB  . THR C 1 203 ? 28.789  14.709  52.883  1.00 60.05  ? 206 THR C CB  1 
ATOM   5554  O OG1 . THR C 1 203 ? 28.257  15.028  51.589  1.00 61.04  ? 206 THR C OG1 1 
ATOM   5555  C CG2 . THR C 1 203 ? 28.762  15.949  53.769  1.00 53.04  ? 206 THR C CG2 1 
ATOM   5556  N N   . SER C 1 204 ? 29.306  12.224  51.573  1.00 60.72  ? 207 SER C N   1 
ATOM   5557  C CA  . SER C 1 204 ? 29.242  11.280  50.464  1.00 59.60  ? 207 SER C CA  1 
ATOM   5558  C C   . SER C 1 204 ? 29.009  11.983  49.132  1.00 58.25  ? 207 SER C C   1 
ATOM   5559  O O   . SER C 1 204 ? 29.357  11.433  48.081  1.00 54.18  ? 207 SER C O   1 
ATOM   5560  C CB  . SER C 1 204 ? 28.151  10.234  50.722  1.00 61.11  ? 207 SER C CB  1 
ATOM   5561  O OG  . SER C 1 204 ? 26.861  10.747  50.436  1.00 68.91  ? 207 SER C OG  1 
ATOM   5562  N N   . THR C 1 205 ? 28.438  13.186  49.149  1.00 59.80  ? 208 THR C N   1 
ATOM   5563  C CA  . THR C 1 205 ? 28.216  13.959  47.935  1.00 65.60  ? 208 THR C CA  1 
ATOM   5564  C C   . THR C 1 205 ? 28.878  15.330  47.952  1.00 64.32  ? 208 THR C C   1 
ATOM   5565  O O   . THR C 1 205 ? 29.327  15.793  46.901  1.00 61.71  ? 208 THR C O   1 
ATOM   5566  C CB  . THR C 1 205 ? 26.709  14.137  47.679  1.00 57.74  ? 208 THR C CB  1 
ATOM   5567  O OG1 . THR C 1 205 ? 26.131  14.903  48.742  1.00 56.46  ? 208 THR C OG1 1 
ATOM   5568  C CG2 . THR C 1 205 ? 26.017  12.785  47.605  1.00 46.74  ? 208 THR C CG2 1 
ATOM   5569  N N   . LEU C 1 206 ? 28.956  15.986  49.107  1.00 56.60  ? 209 LEU C N   1 
ATOM   5570  C CA  . LEU C 1 206 ? 29.561  17.307  49.198  1.00 53.96  ? 209 LEU C CA  1 
ATOM   5571  C C   . LEU C 1 206 ? 31.080  17.197  49.228  1.00 57.94  ? 209 LEU C C   1 
ATOM   5572  O O   . LEU C 1 206 ? 31.638  16.358  49.941  1.00 61.37  ? 209 LEU C O   1 
ATOM   5573  C CB  . LEU C 1 206 ? 29.065  18.032  50.447  1.00 58.92  ? 209 LEU C CB  1 
ATOM   5574  C CG  . LEU C 1 206 ? 29.290  19.540  50.489  1.00 58.45  ? 209 LEU C CG  1 
ATOM   5575  C CD1 . LEU C 1 206 ? 28.213  20.248  49.681  1.00 50.23  ? 209 LEU C CD1 1 
ATOM   5576  C CD2 . LEU C 1 206 ? 29.290  20.021  51.929  1.00 57.35  ? 209 LEU C CD2 1 
ATOM   5577  N N   . ASN C 1 207 ? 31.747  18.045  48.447  1.00 55.80  ? 210 ASN C N   1 
ATOM   5578  C CA  . ASN C 1 207 ? 33.211  18.089  48.397  1.00 54.99  ? 210 ASN C CA  1 
ATOM   5579  C C   . ASN C 1 207 ? 33.611  19.555  48.235  1.00 51.48  ? 210 ASN C C   1 
ATOM   5580  O O   . ASN C 1 207 ? 33.747  20.050  47.114  1.00 50.15  ? 210 ASN C O   1 
ATOM   5581  C CB  . ASN C 1 207 ? 33.748  17.222  47.267  1.00 47.80  ? 210 ASN C CB  1 
ATOM   5582  C CG  . ASN C 1 207 ? 35.258  17.221  47.211  1.00 58.52  ? 210 ASN C CG  1 
ATOM   5583  O OD1 . ASN C 1 207 ? 35.922  17.505  48.209  1.00 53.10  ? 210 ASN C OD1 1 
ATOM   5584  N ND2 . ASN C 1 207 ? 35.812  16.903  46.046  1.00 55.61  ? 210 ASN C ND2 1 
ATOM   5585  N N   . GLN C 1 208 ? 33.823  20.236  49.361  1.00 43.62  ? 211 GLN C N   1 
ATOM   5586  C CA  . GLN C 1 208 ? 33.930  21.688  49.385  1.00 46.00  ? 211 GLN C CA  1 
ATOM   5587  C C   . GLN C 1 208 ? 35.231  22.129  50.039  1.00 56.72  ? 211 GLN C C   1 
ATOM   5588  O O   . GLN C 1 208 ? 35.647  21.565  51.055  1.00 59.07  ? 211 GLN C O   1 
ATOM   5589  C CB  . GLN C 1 208 ? 32.740  22.300  50.134  1.00 39.61  ? 211 GLN C CB  1 
ATOM   5590  C CG  . GLN C 1 208 ? 32.834  23.802  50.348  1.00 51.40  ? 211 GLN C CG  1 
ATOM   5591  C CD  . GLN C 1 208 ? 31.586  24.378  50.987  1.00 58.53  ? 211 GLN C CD  1 
ATOM   5592  O OE1 . GLN C 1 208 ? 31.506  24.513  52.209  1.00 57.83  ? 211 GLN C OE1 1 
ATOM   5593  N NE2 . GLN C 1 208 ? 30.603  24.721  50.162  1.00 62.57  ? 211 GLN C NE2 1 
ATOM   5594  N N   . ARG C 1 209 ? 35.867  23.140  49.447  1.00 58.25  ? 212 ARG C N   1 
ATOM   5595  C CA  . ARG C 1 209 ? 37.010  23.817  50.045  1.00 57.29  ? 212 ARG C CA  1 
ATOM   5596  C C   . ARG C 1 209 ? 36.766  25.319  50.010  1.00 59.02  ? 212 ARG C C   1 
ATOM   5597  O O   . ARG C 1 209 ? 36.492  25.885  48.947  1.00 60.38  ? 212 ARG C O   1 
ATOM   5598  C CB  . ARG C 1 209 ? 38.317  23.483  49.326  1.00 59.67  ? 212 ARG C CB  1 
ATOM   5599  C CG  . ARG C 1 209 ? 39.556  23.959  50.077  1.00 54.91  ? 212 ARG C CG  1 
ATOM   5600  C CD  . ARG C 1 209 ? 40.826  23.294  49.567  1.00 70.34  ? 212 ARG C CD  1 
ATOM   5601  N NE  . ARG C 1 209 ? 41.992  23.663  50.364  1.00 66.93  ? 212 ARG C NE  1 
ATOM   5602  C CZ  . ARG C 1 209 ? 42.668  24.795  50.225  1.00 62.21  ? 212 ARG C CZ  1 
ATOM   5603  N NH1 . ARG C 1 209 ? 42.320  25.701  49.326  1.00 74.32  ? 212 ARG C NH1 1 
ATOM   5604  N NH2 . ARG C 1 209 ? 43.720  25.024  51.004  1.00 70.27  ? 212 ARG C NH2 1 
ATOM   5605  N N   . LEU C 1 210 ? 36.877  25.959  51.168  1.00 56.14  ? 213 LEU C N   1 
ATOM   5606  C CA  . LEU C 1 210 ? 36.646  27.387  51.308  1.00 60.65  ? 213 LEU C CA  1 
ATOM   5607  C C   . LEU C 1 210 ? 37.913  28.064  51.804  1.00 71.47  ? 213 LEU C C   1 
ATOM   5608  O O   . LEU C 1 210 ? 38.570  27.567  52.719  1.00 69.61  ? 213 LEU C O   1 
ATOM   5609  C CB  . LEU C 1 210 ? 35.489  27.661  52.280  1.00 58.10  ? 213 LEU C CB  1 
ATOM   5610  C CG  . LEU C 1 210 ? 34.131  27.070  51.908  1.00 64.39  ? 213 LEU C CG  1 
ATOM   5611  C CD1 . LEU C 1 210 ? 33.176  27.187  53.090  1.00 60.93  ? 213 LEU C CD1 1 
ATOM   5612  C CD2 . LEU C 1 210 ? 33.564  27.760  50.676  1.00 55.78  ? 213 LEU C CD2 1 
ATOM   5613  N N   . VAL C 1 211 ? 38.248  29.197  51.197  1.00 66.48  ? 214 VAL C N   1 
ATOM   5614  C CA  . VAL C 1 211 ? 39.446  29.961  51.524  1.00 60.47  ? 214 VAL C CA  1 
ATOM   5615  C C   . VAL C 1 211 ? 39.017  31.372  51.885  1.00 61.08  ? 214 VAL C C   1 
ATOM   5616  O O   . VAL C 1 211 ? 38.198  31.962  51.175  1.00 59.38  ? 214 VAL C O   1 
ATOM   5617  C CB  . VAL C 1 211 ? 40.455  29.989  50.360  1.00 60.44  ? 214 VAL C CB  1 
ATOM   5618  C CG1 . VAL C 1 211 ? 41.530  31.032  50.608  1.00 58.15  ? 214 VAL C CG1 1 
ATOM   5619  C CG2 . VAL C 1 211 ? 41.083  28.611  50.169  1.00 51.88  ? 214 VAL C CG2 1 
ATOM   5620  N N   . PRO C 1 212 ? 39.542  31.958  52.962  1.00 65.49  ? 215 PRO C N   1 
ATOM   5621  C CA  . PRO C 1 212 ? 39.169  33.331  53.323  1.00 55.97  ? 215 PRO C CA  1 
ATOM   5622  C C   . PRO C 1 212 ? 39.653  34.346  52.298  1.00 58.18  ? 215 PRO C C   1 
ATOM   5623  O O   . PRO C 1 212 ? 40.648  34.139  51.597  1.00 64.40  ? 215 PRO C O   1 
ATOM   5624  C CB  . PRO C 1 212 ? 39.860  33.541  54.676  1.00 60.86  ? 215 PRO C CB  1 
ATOM   5625  C CG  . PRO C 1 212 ? 40.156  32.166  55.182  1.00 60.68  ? 215 PRO C CG  1 
ATOM   5626  C CD  . PRO C 1 212 ? 40.415  31.333  53.972  1.00 66.39  ? 215 PRO C CD  1 
ATOM   5627  N N   . LYS C 1 213 ? 38.935  35.461  52.227  1.00 58.15  ? 216 LYS C N   1 
ATOM   5628  C CA  . LYS C 1 213 ? 39.246  36.549  51.304  1.00 60.52  ? 216 LYS C CA  1 
ATOM   5629  C C   . LYS C 1 213 ? 39.648  37.775  52.121  1.00 63.61  ? 216 LYS C C   1 
ATOM   5630  O O   . LYS C 1 213 ? 38.794  38.456  52.695  1.00 56.47  ? 216 LYS C O   1 
ATOM   5631  C CB  . LYS C 1 213 ? 38.056  36.838  50.394  1.00 63.97  ? 216 LYS C CB  1 
ATOM   5632  C CG  . LYS C 1 213 ? 37.687  35.668  49.488  1.00 58.14  ? 216 LYS C CG  1 
ATOM   5633  C CD  . LYS C 1 213 ? 36.767  36.107  48.362  1.00 58.20  ? 216 LYS C CD  1 
ATOM   5634  C CE  . LYS C 1 213 ? 35.308  36.018  48.784  1.00 70.38  ? 216 LYS C CE  1 
ATOM   5635  N NZ  . LYS C 1 213 ? 34.564  35.028  47.964  1.00 60.22  ? 216 LYS C NZ  1 
ATOM   5636  N N   . ILE C 1 214 ? 40.951  38.049  52.160  1.00 71.28  ? 217 ILE C N   1 
ATOM   5637  C CA  . ILE C 1 214 ? 41.516  39.134  52.955  1.00 60.73  ? 217 ILE C CA  1 
ATOM   5638  C C   . ILE C 1 214 ? 41.523  40.398  52.101  1.00 64.86  ? 217 ILE C C   1 
ATOM   5639  O O   . ILE C 1 214 ? 42.356  40.545  51.203  1.00 68.20  ? 217 ILE C O   1 
ATOM   5640  C CB  . ILE C 1 214 ? 42.934  38.794  53.430  1.00 74.28  ? 217 ILE C CB  1 
ATOM   5641  C CG1 . ILE C 1 214 ? 42.907  37.669  54.461  1.00 62.39  ? 217 ILE C CG1 1 
ATOM   5642  C CG2 . ILE C 1 214 ? 43.612  40.036  54.011  1.00 73.40  ? 217 ILE C CG2 1 
ATOM   5643  C CD1 . ILE C 1 214 ? 42.642  38.149  55.850  1.00 72.93  ? 217 ILE C CD1 1 
ATOM   5644  N N   . ALA C 1 215 ? 40.609  41.317  52.391  1.00 55.82  ? 218 ALA C N   1 
ATOM   5645  C CA  . ALA C 1 215 ? 40.544  42.596  51.692  1.00 55.23  ? 218 ALA C CA  1 
ATOM   5646  C C   . ALA C 1 215 ? 39.625  43.514  52.482  1.00 59.81  ? 218 ALA C C   1 
ATOM   5647  O O   . ALA C 1 215 ? 38.914  43.078  53.391  1.00 66.53  ? 218 ALA C O   1 
ATOM   5648  C CB  . ALA C 1 215 ? 40.056  42.440  50.249  1.00 50.32  ? 218 ALA C CB  1 
ATOM   5649  N N   . THR C 1 216 ? 39.643  44.795  52.122  1.00 56.66  ? 219 THR C N   1 
ATOM   5650  C CA  . THR C 1 216 ? 38.842  45.799  52.811  1.00 63.66  ? 219 THR C CA  1 
ATOM   5651  C C   . THR C 1 216 ? 37.482  45.942  52.134  1.00 72.57  ? 219 THR C C   1 
ATOM   5652  O O   . THR C 1 216 ? 37.399  46.073  50.907  1.00 64.60  ? 219 THR C O   1 
ATOM   5653  C CB  . THR C 1 216 ? 39.567  47.148  52.845  1.00 60.80  ? 219 THR C CB  1 
ATOM   5654  O OG1 . THR C 1 216 ? 39.571  47.731  51.537  1.00 62.49  ? 219 THR C OG1 1 
ATOM   5655  C CG2 . THR C 1 216 ? 41.010  46.976  53.327  1.00 61.14  ? 219 THR C CG2 1 
ATOM   5656  N N   . ARG C 1 217 ? 36.422  45.908  52.934  1.00 65.36  ? 220 ARG C N   1 
ATOM   5657  C CA  . ARG C 1 217 ? 35.057  46.074  52.460  1.00 65.22  ? 220 ARG C CA  1 
ATOM   5658  C C   . ARG C 1 217 ? 34.462  47.351  53.039  1.00 64.97  ? 220 ARG C C   1 
ATOM   5659  O O   . ARG C 1 217 ? 35.133  48.124  53.726  1.00 75.58  ? 220 ARG C O   1 
ATOM   5660  C CB  . ARG C 1 217 ? 34.202  44.863  52.833  1.00 60.01  ? 220 ARG C CB  1 
ATOM   5661  C CG  . ARG C 1 217 ? 34.636  43.572  52.180  1.00 60.26  ? 220 ARG C CG  1 
ATOM   5662  C CD  . ARG C 1 217 ? 34.317  42.394  53.071  1.00 54.07  ? 220 ARG C CD  1 
ATOM   5663  N NE  . ARG C 1 217 ? 35.323  41.347  52.970  1.00 59.42  ? 220 ARG C NE  1 
ATOM   5664  C CZ  . ARG C 1 217 ? 36.207  41.058  53.914  1.00 61.11  ? 220 ARG C CZ  1 
ATOM   5665  N NH1 . ARG C 1 217 ? 36.236  41.720  55.060  1.00 67.02  ? 220 ARG C NH1 1 
ATOM   5666  N NH2 . ARG C 1 217 ? 37.083  40.078  53.705  1.00 57.79  ? 220 ARG C NH2 1 
ATOM   5667  N N   . SER C 1 218 ? 33.185  47.572  52.747  1.00 63.51  ? 221 SER C N   1 
ATOM   5668  C CA  . SER C 1 218 ? 32.438  48.662  53.352  1.00 49.80  ? 221 SER C CA  1 
ATOM   5669  C C   . SER C 1 218 ? 31.809  48.200  54.663  1.00 57.10  ? 221 SER C C   1 
ATOM   5670  O O   . SER C 1 218 ? 31.568  47.010  54.881  1.00 70.64  ? 221 SER C O   1 
ATOM   5671  C CB  . SER C 1 218 ? 31.360  49.178  52.398  1.00 65.15  ? 221 SER C CB  1 
ATOM   5672  O OG  . SER C 1 218 ? 31.885  50.139  51.498  1.00 65.39  ? 221 SER C OG  1 
ATOM   5673  N N   . GLN C 1 219 ? 31.548  49.160  55.543  1.00 60.19  ? 222 GLN C N   1 
ATOM   5674  C CA  . GLN C 1 219 ? 31.037  48.846  56.870  1.00 71.16  ? 222 GLN C CA  1 
ATOM   5675  C C   . GLN C 1 219 ? 29.564  48.466  56.794  1.00 68.92  ? 222 GLN C C   1 
ATOM   5676  O O   . GLN C 1 219 ? 28.759  49.186  56.195  1.00 63.26  ? 222 GLN C O   1 
ATOM   5677  C CB  . GLN C 1 219 ? 31.221  50.041  57.801  1.00 72.55  ? 222 GLN C CB  1 
ATOM   5678  C CG  . GLN C 1 219 ? 32.421  49.941  58.724  1.00 78.87  ? 222 GLN C CG  1 
ATOM   5679  C CD  . GLN C 1 219 ? 32.111  50.430  60.122  1.00 88.78  ? 222 GLN C CD  1 
ATOM   5680  O OE1 . GLN C 1 219 ? 31.489  51.478  60.298  1.00 86.62  ? 222 GLN C OE1 1 
ATOM   5681  N NE2 . GLN C 1 219 ? 32.586  49.701  61.125  1.00 88.99  ? 222 GLN C NE2 1 
ATOM   5682  N N   . VAL C 1 220 ? 29.214  47.333  57.396  1.00 66.98  ? 223 VAL C N   1 
ATOM   5683  C CA  . VAL C 1 220 ? 27.826  46.906  57.542  1.00 67.27  ? 223 VAL C CA  1 
ATOM   5684  C C   . VAL C 1 220 ? 27.619  46.476  58.986  1.00 68.66  ? 223 VAL C C   1 
ATOM   5685  O O   . VAL C 1 220 ? 28.398  45.674  59.513  1.00 62.74  ? 223 VAL C O   1 
ATOM   5686  C CB  . VAL C 1 220 ? 27.466  45.759  56.576  1.00 61.25  ? 223 VAL C CB  1 
ATOM   5687  C CG1 . VAL C 1 220 ? 26.087  45.215  56.901  1.00 62.61  ? 223 VAL C CG1 1 
ATOM   5688  C CG2 . VAL C 1 220 ? 27.516  46.241  55.133  1.00 57.53  ? 223 VAL C CG2 1 
ATOM   5689  N N   . ASN C 1 221 ? 26.576  47.013  59.626  1.00 60.78  ? 224 ASN C N   1 
ATOM   5690  C CA  . ASN C 1 221 ? 26.323  46.781  61.049  1.00 61.70  ? 224 ASN C CA  1 
ATOM   5691  C C   . ASN C 1 221 ? 27.543  47.133  61.896  1.00 75.06  ? 224 ASN C C   1 
ATOM   5692  O O   . ASN C 1 221 ? 27.824  46.475  62.901  1.00 81.38  ? 224 ASN C O   1 
ATOM   5693  C CB  . ASN C 1 221 ? 25.887  45.337  61.320  1.00 70.58  ? 224 ASN C CB  1 
ATOM   5694  C CG  . ASN C 1 221 ? 24.611  44.966  60.586  1.00 77.37  ? 224 ASN C CG  1 
ATOM   5695  O OD1 . ASN C 1 221 ? 23.850  45.837  60.158  1.00 77.56  ? 224 ASN C OD1 1 
ATOM   5696  N ND2 . ASN C 1 221 ? 24.372  43.667  60.433  1.00 60.52  ? 224 ASN C ND2 1 
ATOM   5697  N N   . GLY C 1 222 ? 28.286  48.160  61.487  1.00 65.99  ? 225 GLY C N   1 
ATOM   5698  C CA  . GLY C 1 222 ? 29.474  48.556  62.210  1.00 75.88  ? 225 GLY C CA  1 
ATOM   5699  C C   . GLY C 1 222 ? 30.677  47.666  62.013  1.00 77.31  ? 225 GLY C C   1 
ATOM   5700  O O   . GLY C 1 222 ? 31.676  47.837  62.719  1.00 83.79  ? 225 GLY C O   1 
ATOM   5701  N N   . LEU C 1 223 ? 30.635  46.742  61.057  1.00 73.40  ? 226 LEU C N   1 
ATOM   5702  C CA  . LEU C 1 223 ? 31.719  45.796  60.848  1.00 59.04  ? 226 LEU C CA  1 
ATOM   5703  C C   . LEU C 1 223 ? 32.097  45.738  59.377  1.00 64.22  ? 226 LEU C C   1 
ATOM   5704  O O   . LEU C 1 223 ? 31.263  45.950  58.492  1.00 63.95  ? 226 LEU C O   1 
ATOM   5705  C CB  . LEU C 1 223 ? 31.341  44.400  61.343  1.00 65.74  ? 226 LEU C CB  1 
ATOM   5706  C CG  . LEU C 1 223 ? 31.149  44.351  62.856  1.00 78.81  ? 226 LEU C CG  1 
ATOM   5707  C CD1 . LEU C 1 223 ? 30.765  42.964  63.303  1.00 69.43  ? 226 LEU C CD1 1 
ATOM   5708  C CD2 . LEU C 1 223 ? 32.419  44.815  63.554  1.00 76.62  ? 226 LEU C CD2 1 
ATOM   5709  N N   . GLN C 1 224 ? 33.378  45.457  59.133  1.00 70.24  ? 227 GLN C N   1 
ATOM   5710  C CA  . GLN C 1 224 ? 33.905  45.294  57.787  1.00 64.79  ? 227 GLN C CA  1 
ATOM   5711  C C   . GLN C 1 224 ? 34.113  43.836  57.396  1.00 64.29  ? 227 GLN C C   1 
ATOM   5712  O O   . GLN C 1 224 ? 34.241  43.544  56.201  1.00 59.93  ? 227 GLN C O   1 
ATOM   5713  C CB  . GLN C 1 224 ? 35.233  46.045  57.645  1.00 63.13  ? 227 GLN C CB  1 
ATOM   5714  C CG  . GLN C 1 224 ? 35.160  47.277  56.769  1.00 68.91  ? 227 GLN C CG  1 
ATOM   5715  C CD  . GLN C 1 224 ? 36.455  48.068  56.774  1.00 74.74  ? 227 GLN C CD  1 
ATOM   5716  O OE1 . GLN C 1 224 ? 37.546  47.495  56.781  1.00 62.68  ? 227 GLN C OE1 1 
ATOM   5717  N NE2 . GLN C 1 224 ? 36.340  49.391  56.770  1.00 82.01  ? 227 GLN C NE2 1 
ATOM   5718  N N   . GLY C 1 225 ? 34.164  42.922  58.367  1.00 62.94  ? 228 GLY C N   1 
ATOM   5719  C CA  . GLY C 1 225 ? 34.277  41.512  58.060  1.00 65.89  ? 228 GLY C CA  1 
ATOM   5720  C C   . GLY C 1 225 ? 32.950  40.900  57.651  1.00 62.91  ? 228 GLY C C   1 
ATOM   5721  O O   . GLY C 1 225 ? 31.884  41.499  57.796  1.00 59.77  ? 228 GLY C O   1 
ATOM   5722  N N   . ARG C 1 226 ? 33.032  39.681  57.118  1.00 59.77  ? 229 ARG C N   1 
ATOM   5723  C CA  . ARG C 1 226 ? 31.864  38.952  56.646  1.00 63.66  ? 229 ARG C CA  1 
ATOM   5724  C C   . ARG C 1 226 ? 31.938  37.506  57.109  1.00 64.49  ? 229 ARG C C   1 
ATOM   5725  O O   . ARG C 1 226 ? 33.020  36.962  57.340  1.00 60.31  ? 229 ARG C O   1 
ATOM   5726  C CB  . ARG C 1 226 ? 31.737  38.978  55.110  1.00 56.10  ? 229 ARG C CB  1 
ATOM   5727  C CG  . ARG C 1 226 ? 31.686  40.368  54.495  1.00 59.44  ? 229 ARG C CG  1 
ATOM   5728  C CD  . ARG C 1 226 ? 30.435  41.114  54.906  1.00 56.39  ? 229 ARG C CD  1 
ATOM   5729  N NE  . ARG C 1 226 ? 30.358  42.422  54.269  1.00 62.45  ? 229 ARG C NE  1 
ATOM   5730  C CZ  . ARG C 1 226 ? 30.628  43.568  54.878  1.00 58.47  ? 229 ARG C CZ  1 
ATOM   5731  N NH1 . ARG C 1 226 ? 31.003  43.605  56.146  1.00 63.38  ? 229 ARG C NH1 1 
ATOM   5732  N NH2 . ARG C 1 226 ? 30.516  44.707  54.198  1.00 56.10  ? 229 ARG C NH2 1 
ATOM   5733  N N   . MET C 1 227 ? 30.770  36.885  57.231  1.00 62.39  ? 230 MET C N   1 
ATOM   5734  C CA  . MET C 1 227 ? 30.672  35.463  57.531  1.00 67.81  ? 230 MET C CA  1 
ATOM   5735  C C   . MET C 1 227 ? 29.754  34.819  56.501  1.00 60.37  ? 230 MET C C   1 
ATOM   5736  O O   . MET C 1 227 ? 28.539  35.040  56.522  1.00 64.03  ? 230 MET C O   1 
ATOM   5737  C CB  . MET C 1 227 ? 30.161  35.227  58.952  1.00 70.85  ? 230 MET C CB  1 
ATOM   5738  C CG  . MET C 1 227 ? 31.249  34.781  59.917  1.00 65.85  ? 230 MET C CG  1 
ATOM   5739  S SD  . MET C 1 227 ? 30.768  34.881  61.650  1.00 77.85  ? 230 MET C SD  1 
ATOM   5740  C CE  . MET C 1 227 ? 31.723  36.287  62.201  1.00 69.44  ? 230 MET C CE  1 
ATOM   5741  N N   . ASP C 1 228 ? 30.339  34.033  55.600  1.00 60.46  ? 231 ASP C N   1 
ATOM   5742  C CA  . ASP C 1 228 ? 29.587  33.329  54.570  1.00 61.32  ? 231 ASP C CA  1 
ATOM   5743  C C   . ASP C 1 228 ? 29.177  31.963  55.104  1.00 62.64  ? 231 ASP C C   1 
ATOM   5744  O O   . ASP C 1 228 ? 30.038  31.150  55.457  1.00 52.32  ? 231 ASP C O   1 
ATOM   5745  C CB  . ASP C 1 228 ? 30.419  33.170  53.299  1.00 57.30  ? 231 ASP C CB  1 
ATOM   5746  C CG  . ASP C 1 228 ? 30.417  34.417  52.437  1.00 58.57  ? 231 ASP C CG  1 
ATOM   5747  O OD1 . ASP C 1 228 ? 29.574  35.308  52.670  1.00 63.73  ? 231 ASP C OD1 1 
ATOM   5748  O OD2 . ASP C 1 228 ? 31.265  34.503  51.522  1.00 67.16  ? 231 ASP C OD2 1 
ATOM   5749  N N   . PHE C 1 229 ? 27.874  31.706  55.144  1.00 56.27  ? 232 PHE C N   1 
ATOM   5750  C CA  . PHE C 1 229 ? 27.347  30.464  55.687  1.00 55.63  ? 232 PHE C CA  1 
ATOM   5751  C C   . PHE C 1 229 ? 26.911  29.520  54.572  1.00 52.43  ? 232 PHE C C   1 
ATOM   5752  O O   . PHE C 1 229 ? 26.437  29.947  53.516  1.00 57.43  ? 232 PHE C O   1 
ATOM   5753  C CB  . PHE C 1 229 ? 26.173  30.738  56.626  1.00 61.19  ? 232 PHE C CB  1 
ATOM   5754  C CG  . PHE C 1 229 ? 26.578  31.346  57.934  1.00 48.30  ? 232 PHE C CG  1 
ATOM   5755  C CD1 . PHE C 1 229 ? 27.123  30.564  58.937  1.00 55.93  ? 232 PHE C CD1 1 
ATOM   5756  C CD2 . PHE C 1 229 ? 26.404  32.702  58.165  1.00 60.70  ? 232 PHE C CD2 1 
ATOM   5757  C CE1 . PHE C 1 229 ? 27.494  31.119  60.145  1.00 64.87  ? 232 PHE C CE1 1 
ATOM   5758  C CE2 . PHE C 1 229 ? 26.772  33.266  59.373  1.00 72.18  ? 232 PHE C CE2 1 
ATOM   5759  C CZ  . PHE C 1 229 ? 27.318  32.472  60.365  1.00 68.88  ? 232 PHE C CZ  1 
ATOM   5760  N N   . PHE C 1 230 ? 27.080  28.223  54.825  1.00 54.60  ? 233 PHE C N   1 
ATOM   5761  C CA  . PHE C 1 230 ? 26.735  27.164  53.889  1.00 50.01  ? 233 PHE C CA  1 
ATOM   5762  C C   . PHE C 1 230 ? 25.912  26.109  54.617  1.00 62.08  ? 233 PHE C C   1 
ATOM   5763  O O   . PHE C 1 230 ? 25.792  26.121  55.844  1.00 56.66  ? 233 PHE C O   1 
ATOM   5764  C CB  . PHE C 1 230 ? 27.990  26.540  53.262  1.00 51.03  ? 233 PHE C CB  1 
ATOM   5765  C CG  . PHE C 1 230 ? 28.784  27.500  52.420  1.00 65.04  ? 233 PHE C CG  1 
ATOM   5766  C CD1 . PHE C 1 230 ? 29.689  28.376  53.005  1.00 55.23  ? 233 PHE C CD1 1 
ATOM   5767  C CD2 . PHE C 1 230 ? 28.615  27.539  51.046  1.00 53.85  ? 233 PHE C CD2 1 
ATOM   5768  C CE1 . PHE C 1 230 ? 30.411  29.266  52.232  1.00 54.69  ? 233 PHE C CE1 1 
ATOM   5769  C CE2 . PHE C 1 230 ? 29.333  28.430  50.268  1.00 58.11  ? 233 PHE C CE2 1 
ATOM   5770  C CZ  . PHE C 1 230 ? 30.234  29.291  50.861  1.00 59.74  ? 233 PHE C CZ  1 
ATOM   5771  N N   . TRP C 1 231 ? 25.329  25.189  53.851  1.00 57.65  ? 234 TRP C N   1 
ATOM   5772  C CA  . TRP C 1 231 ? 24.495  24.155  54.443  1.00 53.36  ? 234 TRP C CA  1 
ATOM   5773  C C   . TRP C 1 231 ? 24.533  22.906  53.578  1.00 53.58  ? 234 TRP C C   1 
ATOM   5774  O O   . TRP C 1 231 ? 25.008  22.921  52.441  1.00 63.46  ? 234 TRP C O   1 
ATOM   5775  C CB  . TRP C 1 231 ? 23.053  24.639  54.641  1.00 61.33  ? 234 TRP C CB  1 
ATOM   5776  C CG  . TRP C 1 231 ? 22.361  25.051  53.378  1.00 58.23  ? 234 TRP C CG  1 
ATOM   5777  C CD1 . TRP C 1 231 ? 22.439  26.264  52.759  1.00 63.61  ? 234 TRP C CD1 1 
ATOM   5778  C CD2 . TRP C 1 231 ? 21.478  24.251  52.583  1.00 49.21  ? 234 TRP C CD2 1 
ATOM   5779  N NE1 . TRP C 1 231 ? 21.659  26.269  51.626  1.00 47.43  ? 234 TRP C NE1 1 
ATOM   5780  C CE2 . TRP C 1 231 ? 21.061  25.044  51.494  1.00 49.21  ? 234 TRP C CE2 1 
ATOM   5781  C CE3 . TRP C 1 231 ? 20.999  22.942  52.685  1.00 56.46  ? 234 TRP C CE3 1 
ATOM   5782  C CZ2 . TRP C 1 231 ? 20.187  24.571  50.515  1.00 54.13  ? 234 TRP C CZ2 1 
ATOM   5783  C CZ3 . TRP C 1 231 ? 20.130  22.473  51.712  1.00 50.39  ? 234 TRP C CZ3 1 
ATOM   5784  C CH2 . TRP C 1 231 ? 19.734  23.285  50.642  1.00 43.85  ? 234 TRP C CH2 1 
ATOM   5785  N N   . THR C 1 232 ? 24.043  21.809  54.151  1.00 49.59  ? 235 THR C N   1 
ATOM   5786  C CA  . THR C 1 232 ? 23.881  20.557  53.428  1.00 54.34  ? 235 THR C CA  1 
ATOM   5787  C C   . THR C 1 232 ? 22.805  19.735  54.122  1.00 52.98  ? 235 THR C C   1 
ATOM   5788  O O   . THR C 1 232 ? 22.402  20.033  55.250  1.00 52.62  ? 235 THR C O   1 
ATOM   5789  C CB  . THR C 1 232 ? 25.192  19.767  53.343  1.00 51.87  ? 235 THR C CB  1 
ATOM   5790  O OG1 . THR C 1 232 ? 25.158  18.900  52.203  1.00 56.26  ? 235 THR C OG1 1 
ATOM   5791  C CG2 . THR C 1 232 ? 25.398  18.925  54.594  1.00 55.07  ? 235 THR C CG2 1 
ATOM   5792  N N   . ILE C 1 233 ? 22.330  18.712  53.424  1.00 50.64  ? 236 ILE C N   1 
ATOM   5793  C CA  . ILE C 1 233 ? 21.377  17.755  53.972  1.00 45.99  ? 236 ILE C CA  1 
ATOM   5794  C C   . ILE C 1 233 ? 22.133  16.450  54.170  1.00 44.31  ? 236 ILE C C   1 
ATOM   5795  O O   . ILE C 1 233 ? 22.446  15.749  53.199  1.00 50.41  ? 236 ILE C O   1 
ATOM   5796  C CB  . ILE C 1 233 ? 20.160  17.567  53.055  1.00 53.33  ? 236 ILE C CB  1 
ATOM   5797  C CG1 . ILE C 1 233 ? 19.370  18.874  52.928  1.00 44.74  ? 236 ILE C CG1 1 
ATOM   5798  C CG2 . ILE C 1 233 ? 19.266  16.458  53.578  1.00 50.03  ? 236 ILE C CG2 1 
ATOM   5799  C CD1 . ILE C 1 233 ? 18.875  19.426  54.249  1.00 45.02  ? 236 ILE C CD1 1 
ATOM   5800  N N   . LEU C 1 234 ? 22.447  16.127  55.422  1.00 49.93  ? 237 LEU C N   1 
ATOM   5801  C CA  . LEU C 1 234 ? 23.161  14.892  55.722  1.00 58.57  ? 237 LEU C CA  1 
ATOM   5802  C C   . LEU C 1 234 ? 22.157  13.754  55.845  1.00 65.82  ? 237 LEU C C   1 
ATOM   5803  O O   . LEU C 1 234 ? 21.291  13.772  56.728  1.00 57.61  ? 237 LEU C O   1 
ATOM   5804  C CB  . LEU C 1 234 ? 23.983  15.031  57.002  1.00 54.10  ? 237 LEU C CB  1 
ATOM   5805  C CG  . LEU C 1 234 ? 25.043  13.945  57.240  1.00 52.80  ? 237 LEU C CG  1 
ATOM   5806  C CD1 . LEU C 1 234 ? 25.915  13.704  56.012  1.00 48.41  ? 237 LEU C CD1 1 
ATOM   5807  C CD2 . LEU C 1 234 ? 25.909  14.280  58.436  1.00 58.40  ? 237 LEU C CD2 1 
ATOM   5808  N N   . LYS C 1 235 ? 22.268  12.774  54.952  1.00 65.33  ? 238 LYS C N   1 
ATOM   5809  C CA  . LYS C 1 235 ? 21.376  11.632  54.967  1.00 71.05  ? 238 LYS C CA  1 
ATOM   5810  C C   . LYS C 1 235 ? 21.700  10.733  56.158  1.00 71.94  ? 238 LYS C C   1 
ATOM   5811  O O   . LYS C 1 235 ? 22.796  10.804  56.719  1.00 69.07  ? 238 LYS C O   1 
ATOM   5812  C CB  . LYS C 1 235 ? 21.494  10.854  53.656  1.00 62.00  ? 238 LYS C CB  1 
ATOM   5813  C CG  . LYS C 1 235 ? 21.178  11.674  52.414  1.00 63.70  ? 238 LYS C CG  1 
ATOM   5814  C CD  . LYS C 1 235 ? 19.793  11.344  51.875  1.00 83.01  ? 238 LYS C CD  1 
ATOM   5815  C CE  . LYS C 1 235 ? 18.793  12.436  52.216  1.00 74.25  ? 238 LYS C CE  1 
ATOM   5816  N NZ  . LYS C 1 235 ? 17.389  11.979  52.031  1.00 80.30  ? 238 LYS C NZ  1 
ATOM   5817  N N   . PRO C 1 236 ? 20.752  9.893   56.580  1.00 80.75  ? 239 PRO C N   1 
ATOM   5818  C CA  . PRO C 1 236 ? 21.034  8.973   57.690  1.00 68.14  ? 239 PRO C CA  1 
ATOM   5819  C C   . PRO C 1 236 ? 22.199  8.047   57.365  1.00 78.18  ? 239 PRO C C   1 
ATOM   5820  O O   . PRO C 1 236 ? 22.392  7.641   56.217  1.00 80.16  ? 239 PRO C O   1 
ATOM   5821  C CB  . PRO C 1 236 ? 19.722  8.195   57.847  1.00 83.76  ? 239 PRO C CB  1 
ATOM   5822  C CG  . PRO C 1 236 ? 18.676  9.097   57.275  1.00 80.05  ? 239 PRO C CG  1 
ATOM   5823  C CD  . PRO C 1 236 ? 19.343  9.823   56.148  1.00 69.83  ? 239 PRO C CD  1 
ATOM   5824  N N   . ASN C 1 237 ? 22.991  7.737   58.394  1.00 75.40  ? 240 ASN C N   1 
ATOM   5825  C CA  . ASN C 1 237 ? 24.131  6.824   58.309  1.00 72.70  ? 240 ASN C CA  1 
ATOM   5826  C C   . ASN C 1 237 ? 25.241  7.346   57.399  1.00 77.17  ? 240 ASN C C   1 
ATOM   5827  O O   . ASN C 1 237 ? 26.089  6.572   56.943  1.00 73.47  ? 240 ASN C O   1 
ATOM   5828  C CB  . ASN C 1 237 ? 23.694  5.424   57.861  1.00 76.11  ? 240 ASN C CB  1 
ATOM   5829  C CG  . ASN C 1 237 ? 22.922  4.688   58.935  1.00 90.69  ? 240 ASN C CG  1 
ATOM   5830  O OD1 . ASN C 1 237 ? 23.457  4.388   60.002  1.00 91.00  ? 240 ASN C OD1 1 
ATOM   5831  N ND2 . ASN C 1 237 ? 21.653  4.398   58.662  1.00 94.95  ? 240 ASN C ND2 1 
ATOM   5832  N N   . ASP C 1 238 ? 25.262  8.647   57.129  1.00 78.64  ? 241 ASP C N   1 
ATOM   5833  C CA  . ASP C 1 238 ? 26.346  9.276   56.393  1.00 74.17  ? 241 ASP C CA  1 
ATOM   5834  C C   . ASP C 1 238 ? 27.096  10.225  57.317  1.00 69.54  ? 241 ASP C C   1 
ATOM   5835  O O   . ASP C 1 238 ? 26.537  10.751  58.285  1.00 65.53  ? 241 ASP C O   1 
ATOM   5836  C CB  . ASP C 1 238 ? 25.831  10.036  55.162  1.00 67.70  ? 241 ASP C CB  1 
ATOM   5837  C CG  . ASP C 1 238 ? 26.945  10.389  54.178  1.00 66.76  ? 241 ASP C CG  1 
ATOM   5838  O OD1 . ASP C 1 238 ? 27.884  9.583   54.012  1.00 69.96  ? 241 ASP C OD1 1 
ATOM   5839  O OD2 . ASP C 1 238 ? 26.887  11.478  53.572  1.00 58.55  ? 241 ASP C OD2 1 
ATOM   5840  N N   . ALA C 1 239 ? 28.371  10.432  57.016  1.00 64.71  ? 242 ALA C N   1 
ATOM   5841  C CA  . ALA C 1 239 ? 29.249  11.238  57.848  1.00 69.35  ? 242 ALA C CA  1 
ATOM   5842  C C   . ALA C 1 239 ? 29.660  12.504  57.109  1.00 59.95  ? 242 ALA C C   1 
ATOM   5843  O O   . ALA C 1 239 ? 29.964  12.467  55.912  1.00 53.31  ? 242 ALA C O   1 
ATOM   5844  C CB  . ALA C 1 239 ? 30.490  10.440  58.260  1.00 55.09  ? 242 ALA C CB  1 
ATOM   5845  N N   . ILE C 1 240 ? 29.657  13.625  57.826  1.00 52.45  ? 243 ILE C N   1 
ATOM   5846  C CA  . ILE C 1 240 ? 30.188  14.886  57.323  1.00 68.42  ? 243 ILE C CA  1 
ATOM   5847  C C   . ILE C 1 240 ? 31.560  15.104  57.950  1.00 72.35  ? 243 ILE C C   1 
ATOM   5848  O O   . ILE C 1 240 ? 31.730  14.942  59.165  1.00 68.84  ? 243 ILE C O   1 
ATOM   5849  C CB  . ILE C 1 240 ? 29.231  16.055  57.619  1.00 59.68  ? 243 ILE C CB  1 
ATOM   5850  C CG1 . ILE C 1 240 ? 29.769  17.355  57.019  1.00 56.48  ? 243 ILE C CG1 1 
ATOM   5851  C CG2 . ILE C 1 240 ? 28.980  16.202  59.116  1.00 54.61  ? 243 ILE C CG2 1 
ATOM   5852  C CD1 . ILE C 1 240 ? 28.803  18.503  57.123  1.00 61.06  ? 243 ILE C CD1 1 
ATOM   5853  N N   . HIS C 1 241 ? 32.549  15.435  57.123  1.00 68.56  ? 244 HIS C N   1 
ATOM   5854  C CA  . HIS C 1 241 ? 33.939  15.530  57.556  1.00 65.16  ? 244 HIS C CA  1 
ATOM   5855  C C   . HIS C 1 241 ? 34.407  16.975  57.448  1.00 75.90  ? 244 HIS C C   1 
ATOM   5856  O O   . HIS C 1 241 ? 34.353  17.573  56.367  1.00 65.25  ? 244 HIS C O   1 
ATOM   5857  C CB  . HIS C 1 241 ? 34.836  14.615  56.724  1.00 67.09  ? 244 HIS C CB  1 
ATOM   5858  C CG  . HIS C 1 241 ? 34.373  13.193  56.684  1.00 71.39  ? 244 HIS C CG  1 
ATOM   5859  N ND1 . HIS C 1 241 ? 34.731  12.266  57.639  1.00 67.87  ? 244 HIS C ND1 1 
ATOM   5860  C CD2 . HIS C 1 241 ? 33.575  12.540  55.806  1.00 66.27  ? 244 HIS C CD2 1 
ATOM   5861  C CE1 . HIS C 1 241 ? 34.176  11.102  57.350  1.00 70.48  ? 244 HIS C CE1 1 
ATOM   5862  N NE2 . HIS C 1 241 ? 33.471  11.241  56.242  1.00 73.30  ? 244 HIS C NE2 1 
ATOM   5863  N N   . PHE C 1 242 ? 34.888  17.518  58.562  1.00 67.82  ? 245 PHE C N   1 
ATOM   5864  C CA  . PHE C 1 242 ? 35.362  18.889  58.638  1.00 54.47  ? 245 PHE C CA  1 
ATOM   5865  C C   . PHE C 1 242 ? 36.879  18.919  58.795  1.00 70.33  ? 245 PHE C C   1 
ATOM   5866  O O   . PHE C 1 242 ? 37.476  18.048  59.436  1.00 63.42  ? 245 PHE C O   1 
ATOM   5867  C CB  . PHE C 1 242 ? 34.707  19.631  59.804  1.00 58.16  ? 245 PHE C CB  1 
ATOM   5868  C CG  . PHE C 1 242 ? 33.319  20.121  59.509  1.00 63.51  ? 245 PHE C CG  1 
ATOM   5869  C CD1 . PHE C 1 242 ? 33.120  21.375  58.963  1.00 67.84  ? 245 PHE C CD1 1 
ATOM   5870  C CD2 . PHE C 1 242 ? 32.212  19.338  59.798  1.00 62.80  ? 245 PHE C CD2 1 
ATOM   5871  C CE1 . PHE C 1 242 ? 31.848  21.844  58.697  1.00 73.03  ? 245 PHE C CE1 1 
ATOM   5872  C CE2 . PHE C 1 242 ? 30.932  19.798  59.534  1.00 70.77  ? 245 PHE C CE2 1 
ATOM   5873  C CZ  . PHE C 1 242 ? 30.749  21.054  58.982  1.00 69.63  ? 245 PHE C CZ  1 
ATOM   5874  N N   . GLU C 1 243 ? 37.496  19.940  58.205  1.00 60.30  ? 246 GLU C N   1 
ATOM   5875  C CA  . GLU C 1 243 ? 38.943  20.112  58.274  1.00 65.55  ? 246 GLU C CA  1 
ATOM   5876  C C   . GLU C 1 243 ? 39.251  21.583  58.056  1.00 67.85  ? 246 GLU C C   1 
ATOM   5877  O O   . GLU C 1 243 ? 38.934  22.126  56.992  1.00 65.32  ? 246 GLU C O   1 
ATOM   5878  C CB  . GLU C 1 243 ? 39.644  19.246  57.232  1.00 70.78  ? 246 GLU C CB  1 
ATOM   5879  C CG  . GLU C 1 243 ? 41.156  19.396  57.194  1.00 65.20  ? 246 GLU C CG  1 
ATOM   5880  C CD  . GLU C 1 243 ? 41.803  18.360  56.293  1.00 76.35  ? 246 GLU C CD  1 
ATOM   5881  O OE1 . GLU C 1 243 ? 41.070  17.487  55.779  1.00 78.75  ? 246 GLU C OE1 1 
ATOM   5882  O OE2 . GLU C 1 243 ? 43.037  18.415  56.098  1.00 65.75  ? 246 GLU C OE2 1 
ATOM   5883  N N   . SER C 1 244 ? 39.847  22.228  59.056  1.00 61.58  ? 247 SER C N   1 
ATOM   5884  C CA  . SER C 1 244 ? 40.157  23.647  58.950  1.00 60.35  ? 247 SER C CA  1 
ATOM   5885  C C   . SER C 1 244 ? 41.289  24.002  59.902  1.00 73.07  ? 247 SER C C   1 
ATOM   5886  O O   . SER C 1 244 ? 41.463  23.372  60.949  1.00 68.29  ? 247 SER C O   1 
ATOM   5887  C CB  . SER C 1 244 ? 38.933  24.512  59.251  1.00 51.23  ? 247 SER C CB  1 
ATOM   5888  O OG  . SER C 1 244 ? 39.292  25.879  59.338  1.00 51.33  ? 247 SER C OG  1 
ATOM   5889  N N   . ASN C 1 245 ? 42.050  25.033  59.525  1.00 68.87  ? 248 ASN C N   1 
ATOM   5890  C CA  . ASN C 1 245 ? 43.106  25.584  60.367  1.00 69.02  ? 248 ASN C CA  1 
ATOM   5891  C C   . ASN C 1 245 ? 42.892  27.067  60.647  1.00 73.59  ? 248 ASN C C   1 
ATOM   5892  O O   . ASN C 1 245 ? 43.851  27.776  60.969  1.00 74.50  ? 248 ASN C O   1 
ATOM   5893  C CB  . ASN C 1 245 ? 44.480  25.356  59.730  1.00 62.63  ? 248 ASN C CB  1 
ATOM   5894  C CG  . ASN C 1 245 ? 44.680  26.167  58.465  1.00 70.23  ? 248 ASN C CG  1 
ATOM   5895  O OD1 . ASN C 1 245 ? 43.732  26.420  57.722  1.00 68.95  ? 248 ASN C OD1 1 
ATOM   5896  N ND2 . ASN C 1 245 ? 45.917  26.583  58.216  1.00 58.44  ? 248 ASN C ND2 1 
ATOM   5897  N N   . GLY C 1 246 ? 41.666  27.547  60.532  1.00 62.31  ? 249 GLY C N   1 
ATOM   5898  C CA  . GLY C 1 246 ? 41.346  28.932  60.823  1.00 63.32  ? 249 GLY C CA  1 
ATOM   5899  C C   . GLY C 1 246 ? 40.120  29.394  60.060  1.00 61.01  ? 249 GLY C C   1 
ATOM   5900  O O   . GLY C 1 246 ? 39.746  28.848  59.025  1.00 57.68  ? 249 GLY C O   1 
ATOM   5901  N N   . ASN C 1 247 ? 39.480  30.433  60.600  1.00 62.01  ? 250 ASN C N   1 
ATOM   5902  C CA  . ASN C 1 247 ? 38.327  31.099  59.993  1.00 65.90  ? 250 ASN C CA  1 
ATOM   5903  C C   . ASN C 1 247 ? 37.098  30.198  59.912  1.00 67.41  ? 250 ASN C C   1 
ATOM   5904  O O   . ASN C 1 247 ? 36.151  30.501  59.177  1.00 55.74  ? 250 ASN C O   1 
ATOM   5905  C CB  . ASN C 1 247 ? 38.668  31.649  58.601  1.00 54.29  ? 250 ASN C CB  1 
ATOM   5906  C CG  . ASN C 1 247 ? 39.917  32.507  58.602  1.00 59.57  ? 250 ASN C CG  1 
ATOM   5907  O OD1 . ASN C 1 247 ? 41.038  31.997  58.549  1.00 55.52  ? 250 ASN C OD1 1 
ATOM   5908  N ND2 . ASN C 1 247 ? 39.730  33.820  58.659  1.00 57.26  ? 250 ASN C ND2 1 
ATOM   5909  N N   . PHE C 1 248 ? 37.080  29.106  60.670  1.00 67.01  ? 251 PHE C N   1 
ATOM   5910  C CA  . PHE C 1 248 ? 36.013  28.117  60.586  1.00 59.04  ? 251 PHE C CA  1 
ATOM   5911  C C   . PHE C 1 248 ? 34.934  28.430  61.616  1.00 61.71  ? 251 PHE C C   1 
ATOM   5912  O O   . PHE C 1 248 ? 35.212  28.500  62.817  1.00 66.76  ? 251 PHE C O   1 
ATOM   5913  C CB  . PHE C 1 248 ? 36.578  26.714  60.799  1.00 63.12  ? 251 PHE C CB  1 
ATOM   5914  C CG  . PHE C 1 248 ? 35.532  25.646  60.921  1.00 66.66  ? 251 PHE C CG  1 
ATOM   5915  C CD1 . PHE C 1 248 ? 34.407  25.652  60.106  1.00 71.62  ? 251 PHE C CD1 1 
ATOM   5916  C CD2 . PHE C 1 248 ? 35.680  24.623  61.844  1.00 59.83  ? 251 PHE C CD2 1 
ATOM   5917  C CE1 . PHE C 1 248 ? 33.448  24.664  60.220  1.00 55.13  ? 251 PHE C CE1 1 
ATOM   5918  C CE2 . PHE C 1 248 ? 34.724  23.633  61.959  1.00 62.68  ? 251 PHE C CE2 1 
ATOM   5919  C CZ  . PHE C 1 248 ? 33.609  23.656  61.149  1.00 56.52  ? 251 PHE C CZ  1 
ATOM   5920  N N   . ILE C 1 249 ? 33.706  28.612  61.144  1.00 61.82  ? 252 ILE C N   1 
ATOM   5921  C CA  . ILE C 1 249 ? 32.551  28.832  62.006  1.00 68.20  ? 252 ILE C CA  1 
ATOM   5922  C C   . ILE C 1 249 ? 31.852  27.483  62.139  1.00 64.71  ? 252 ILE C C   1 
ATOM   5923  O O   . ILE C 1 249 ? 31.083  27.078  61.263  1.00 64.67  ? 252 ILE C O   1 
ATOM   5924  C CB  . ILE C 1 249 ? 31.619  29.909  61.445  1.00 67.54  ? 252 ILE C CB  1 
ATOM   5925  C CG1 . ILE C 1 249 ? 32.361  31.230  61.197  1.00 65.00  ? 252 ILE C CG1 1 
ATOM   5926  C CG2 . ILE C 1 249 ? 30.464  30.145  62.398  1.00 70.32  ? 252 ILE C CG2 1 
ATOM   5927  C CD1 . ILE C 1 249 ? 33.460  31.559  62.205  1.00 65.44  ? 252 ILE C CD1 1 
ATOM   5928  N N   . ALA C 1 250 ? 32.120  26.781  63.243  1.00 66.16  ? 253 ALA C N   1 
ATOM   5929  C CA  . ALA C 1 250 ? 31.716  25.393  63.409  1.00 62.18  ? 253 ALA C CA  1 
ATOM   5930  C C   . ALA C 1 250 ? 30.224  25.275  63.726  1.00 63.14  ? 253 ALA C C   1 
ATOM   5931  O O   . ALA C 1 250 ? 29.625  26.195  64.290  1.00 62.86  ? 253 ALA C O   1 
ATOM   5932  C CB  . ALA C 1 250 ? 32.530  24.736  64.519  1.00 64.96  ? 253 ALA C CB  1 
ATOM   5933  N N   . PRO C 1 251 ? 29.604  24.147  63.372  1.00 70.39  ? 254 PRO C N   1 
ATOM   5934  C CA  . PRO C 1 251 ? 28.203  23.927  63.749  1.00 77.54  ? 254 PRO C CA  1 
ATOM   5935  C C   . PRO C 1 251 ? 28.085  23.390  65.167  1.00 80.35  ? 254 PRO C C   1 
ATOM   5936  O O   . PRO C 1 251 ? 28.858  22.530  65.596  1.00 77.82  ? 254 PRO C O   1 
ATOM   5937  C CB  . PRO C 1 251 ? 27.716  22.884  62.729  1.00 67.35  ? 254 PRO C CB  1 
ATOM   5938  C CG  . PRO C 1 251 ? 28.915  22.544  61.854  1.00 62.27  ? 254 PRO C CG  1 
ATOM   5939  C CD  . PRO C 1 251 ? 30.132  23.037  62.562  1.00 59.43  ? 254 PRO C CD  1 
ATOM   5940  N N   . GLU C 1 252 ? 27.098  23.905  65.899  1.00 78.09  ? 255 GLU C N   1 
ATOM   5941  C CA  . GLU C 1 252 ? 26.762  23.381  67.217  1.00 76.58  ? 255 GLU C CA  1 
ATOM   5942  C C   . GLU C 1 252 ? 25.406  22.687  67.207  1.00 80.09  ? 255 GLU C C   1 
ATOM   5943  O O   . GLU C 1 252 ? 25.309  21.503  67.546  1.00 68.35  ? 255 GLU C O   1 
ATOM   5944  C CB  . GLU C 1 252 ? 26.789  24.509  68.261  1.00 75.57  ? 255 GLU C CB  1 
ATOM   5945  C CG  . GLU C 1 252 ? 26.767  24.025  69.709  1.00 79.16  ? 255 GLU C CG  1 
ATOM   5946  C CD  . GLU C 1 252 ? 26.675  25.166  70.710  1.00 85.26  ? 255 GLU C CD  1 
ATOM   5947  O OE1 . GLU C 1 252 ? 26.840  26.337  70.303  1.00 88.61  ? 255 GLU C OE1 1 
ATOM   5948  O OE2 . GLU C 1 252 ? 26.437  24.893  71.906  1.00 91.47  ? 255 GLU C OE2 1 
ATOM   5949  N N   . TYR C 1 253 ? 24.357  23.388  66.791  1.00 72.75  ? 256 TYR C N   1 
ATOM   5950  C CA  . TYR C 1 253 ? 23.010  22.840  66.728  1.00 69.57  ? 256 TYR C CA  1 
ATOM   5951  C C   . TYR C 1 253 ? 22.657  22.538  65.276  1.00 69.65  ? 256 TYR C C   1 
ATOM   5952  O O   . TYR C 1 253 ? 22.847  23.385  64.397  1.00 68.30  ? 256 TYR C O   1 
ATOM   5953  C CB  . TYR C 1 253 ? 21.991  23.814  67.333  1.00 67.91  ? 256 TYR C CB  1 
ATOM   5954  C CG  . TYR C 1 253 ? 22.045  23.937  68.845  1.00 85.07  ? 256 TYR C CG  1 
ATOM   5955  C CD1 . TYR C 1 253 ? 22.541  22.906  69.633  1.00 87.83  ? 256 TYR C CD1 1 
ATOM   5956  C CD2 . TYR C 1 253 ? 21.591  25.087  69.484  1.00 87.87  ? 256 TYR C CD2 1 
ATOM   5957  C CE1 . TYR C 1 253 ? 22.588  23.020  71.018  1.00 89.44  ? 256 TYR C CE1 1 
ATOM   5958  C CE2 . TYR C 1 253 ? 21.634  25.210  70.866  1.00 80.48  ? 256 TYR C CE2 1 
ATOM   5959  C CZ  . TYR C 1 253 ? 22.133  24.174  71.626  1.00 82.58  ? 256 TYR C CZ  1 
ATOM   5960  O OH  . TYR C 1 253 ? 22.176  24.294  72.997  1.00 75.39  ? 256 TYR C OH  1 
ATOM   5961  N N   . ALA C 1 254 ? 22.156  21.334  65.028  1.00 70.94  ? 257 ALA C N   1 
ATOM   5962  C CA  . ALA C 1 254 ? 21.620  20.944  63.733  1.00 58.68  ? 257 ALA C CA  1 
ATOM   5963  C C   . ALA C 1 254 ? 20.106  20.779  63.844  1.00 68.30  ? 257 ALA C C   1 
ATOM   5964  O O   . ALA C 1 254 ? 19.504  21.029  64.892  1.00 73.82  ? 257 ALA C O   1 
ATOM   5965  C CB  . ALA C 1 254 ? 22.290  19.664  63.231  1.00 62.05  ? 257 ALA C CB  1 
ATOM   5966  N N   . TYR C 1 255 ? 19.486  20.353  62.745  1.00 72.87  ? 258 TYR C N   1 
ATOM   5967  C CA  . TYR C 1 255 ? 18.029  20.259  62.669  1.00 62.77  ? 258 TYR C CA  1 
ATOM   5968  C C   . TYR C 1 255 ? 17.644  18.937  62.021  1.00 61.91  ? 258 TYR C C   1 
ATOM   5969  O O   . TYR C 1 255 ? 17.925  18.719  60.838  1.00 61.70  ? 258 TYR C O   1 
ATOM   5970  C CB  . TYR C 1 255 ? 17.445  21.427  61.878  1.00 58.43  ? 258 TYR C CB  1 
ATOM   5971  C CG  . TYR C 1 255 ? 17.590  22.778  62.535  1.00 54.20  ? 258 TYR C CG  1 
ATOM   5972  C CD1 . TYR C 1 255 ? 16.765  23.153  63.587  1.00 56.18  ? 258 TYR C CD1 1 
ATOM   5973  C CD2 . TYR C 1 255 ? 18.537  23.689  62.087  1.00 53.65  ? 258 TYR C CD2 1 
ATOM   5974  C CE1 . TYR C 1 255 ? 16.888  24.394  64.186  1.00 66.28  ? 258 TYR C CE1 1 
ATOM   5975  C CE2 . TYR C 1 255 ? 18.666  24.937  62.679  1.00 61.23  ? 258 TYR C CE2 1 
ATOM   5976  C CZ  . TYR C 1 255 ? 17.840  25.283  63.728  1.00 65.24  ? 258 TYR C CZ  1 
ATOM   5977  O OH  . TYR C 1 255 ? 17.964  26.519  64.320  1.00 58.63  ? 258 TYR C OH  1 
ATOM   5978  N N   . LYS C 1 256 ? 17.002  18.057  62.786  1.00 64.50  ? 259 LYS C N   1 
ATOM   5979  C CA  . LYS C 1 256 ? 16.379  16.882  62.192  1.00 66.50  ? 259 LYS C CA  1 
ATOM   5980  C C   . LYS C 1 256 ? 15.202  17.326  61.332  1.00 69.30  ? 259 LYS C C   1 
ATOM   5981  O O   . LYS C 1 256 ? 14.404  18.175  61.743  1.00 56.34  ? 259 LYS C O   1 
ATOM   5982  C CB  . LYS C 1 256 ? 15.915  15.912  63.276  1.00 64.62  ? 259 LYS C CB  1 
ATOM   5983  C CG  . LYS C 1 256 ? 17.045  15.229  64.035  1.00 87.62  ? 259 LYS C CG  1 
ATOM   5984  C CD  . LYS C 1 256 ? 16.616  14.851  65.447  1.00 95.27  ? 259 LYS C CD  1 
ATOM   5985  C CE  . LYS C 1 256 ? 15.818  13.555  65.466  1.00 82.71  ? 259 LYS C CE  1 
ATOM   5986  N NZ  . LYS C 1 256 ? 14.653  13.647  66.390  1.00 86.47  ? 259 LYS C NZ  1 
ATOM   5987  N N   . ILE C 1 257 ? 15.096  16.767  60.130  1.00 72.47  ? 260 ILE C N   1 
ATOM   5988  C CA  . ILE C 1 257 ? 14.116  17.238  59.161  1.00 67.28  ? 260 ILE C CA  1 
ATOM   5989  C C   . ILE C 1 257 ? 13.475  16.047  58.459  1.00 68.51  ? 260 ILE C C   1 
ATOM   5990  O O   . ILE C 1 257 ? 14.130  15.034  58.188  1.00 65.05  ? 260 ILE C O   1 
ATOM   5991  C CB  . ILE C 1 257 ? 14.755  18.220  58.153  1.00 64.59  ? 260 ILE C CB  1 
ATOM   5992  C CG1 . ILE C 1 257 ? 13.798  19.371  57.865  1.00 72.59  ? 260 ILE C CG1 1 
ATOM   5993  C CG2 . ILE C 1 257 ? 15.145  17.540  56.850  1.00 65.11  ? 260 ILE C CG2 1 
ATOM   5994  C CD1 . ILE C 1 257 ? 14.468  20.534  57.204  1.00 73.43  ? 260 ILE C CD1 1 
ATOM   5995  N N   . VAL C 1 258 A 12.169  16.155  58.219  1.00 68.85  ? 260 VAL C N   1 
ATOM   5996  C CA  . VAL C 1 258 A 11.423  15.230  57.375  1.00 65.93  ? 260 VAL C CA  1 
ATOM   5997  C C   . VAL C 1 258 A 10.565  16.060  56.432  1.00 64.54  ? 260 VAL C C   1 
ATOM   5998  O O   . VAL C 1 258 A 9.795   16.917  56.881  1.00 53.19  ? 260 VAL C O   1 
ATOM   5999  C CB  . VAL C 1 258 A 10.540  14.263  58.190  1.00 77.77  ? 260 VAL C CB  1 
ATOM   6000  C CG1 . VAL C 1 258 A 9.999   13.165  57.287  1.00 66.87  ? 260 VAL C CG1 1 
ATOM   6001  C CG2 . VAL C 1 258 A 11.317  13.660  59.354  1.00 72.01  ? 260 VAL C CG2 1 
ATOM   6002  N N   . LYS C 1 259 ? 10.699  15.813  55.132  1.00 64.46  ? 261 LYS C N   1 
ATOM   6003  C CA  . LYS C 1 259 ? 9.967   16.559  54.121  1.00 55.97  ? 261 LYS C CA  1 
ATOM   6004  C C   . LYS C 1 259 ? 9.040   15.621  53.366  1.00 67.09  ? 261 LYS C C   1 
ATOM   6005  O O   . LYS C 1 259 ? 9.484   14.603  52.824  1.00 68.09  ? 261 LYS C O   1 
ATOM   6006  C CB  . LYS C 1 259 ? 10.915  17.263  53.147  1.00 52.57  ? 261 LYS C CB  1 
ATOM   6007  C CG  . LYS C 1 259 ? 10.214  18.329  52.306  1.00 57.96  ? 261 LYS C CG  1 
ATOM   6008  C CD  . LYS C 1 259 ? 11.189  19.145  51.484  1.00 55.69  ? 261 LYS C CD  1 
ATOM   6009  C CE  . LYS C 1 259 ? 10.458  20.182  50.648  1.00 62.47  ? 261 LYS C CE  1 
ATOM   6010  N NZ  . LYS C 1 259 ? 9.717   21.173  51.485  1.00 58.42  ? 261 LYS C NZ  1 
ATOM   6011  N N   . LYS C 1 260 ? 7.755   15.974  53.324  1.00 65.70  ? 262 LYS C N   1 
ATOM   6012  C CA  . LYS C 1 260 ? 6.751   15.191  52.625  1.00 68.27  ? 262 LYS C CA  1 
ATOM   6013  C C   . LYS C 1 260 ? 6.031   15.965  51.531  1.00 65.13  ? 262 LYS C C   1 
ATOM   6014  O O   . LYS C 1 260 ? 5.375   15.341  50.688  1.00 78.97  ? 262 LYS C O   1 
ATOM   6015  C CB  . LYS C 1 260 ? 5.714   14.643  53.622  1.00 55.69  ? 262 LYS C CB  1 
ATOM   6016  C CG  . LYS C 1 260 ? 5.873   13.166  53.966  1.00 62.83  ? 262 LYS C CG  1 
ATOM   6017  C CD  . LYS C 1 260 ? 7.281   12.668  53.692  1.00 76.65  ? 262 LYS C CD  1 
ATOM   6018  C CE  . LYS C 1 260 ? 7.524   11.296  54.295  1.00 80.72  ? 262 LYS C CE  1 
ATOM   6019  N NZ  . LYS C 1 260 ? 8.894   10.810  53.971  1.00 84.54  ? 262 LYS C NZ  1 
ATOM   6020  N N   . GLY C 1 261 ? 6.136   17.291  51.511  1.00 67.52  ? 263 GLY C N   1 
ATOM   6021  C CA  . GLY C 1 261 ? 5.465   18.103  50.515  1.00 62.97  ? 263 GLY C CA  1 
ATOM   6022  C C   . GLY C 1 261 ? 6.136   19.455  50.408  1.00 67.73  ? 263 GLY C C   1 
ATOM   6023  O O   . GLY C 1 261 ? 7.054   19.781  51.164  1.00 58.26  ? 263 GLY C O   1 
ATOM   6024  N N   . ASP C 1 262 ? 5.656   20.252  49.455  1.00 68.67  ? 264 ASP C N   1 
ATOM   6025  C CA  . ASP C 1 262 ? 6.264   21.534  49.136  1.00 59.65  ? 264 ASP C CA  1 
ATOM   6026  C C   . ASP C 1 262 ? 5.260   22.670  49.288  1.00 50.91  ? 264 ASP C C   1 
ATOM   6027  O O   . ASP C 1 262 ? 4.044   22.481  49.199  1.00 60.49  ? 264 ASP C O   1 
ATOM   6028  C CB  . ASP C 1 262 ? 6.850   21.532  47.716  1.00 61.34  ? 264 ASP C CB  1 
ATOM   6029  C CG  . ASP C 1 262 ? 8.368   21.388  47.714  1.00 86.29  ? 264 ASP C CG  1 
ATOM   6030  O OD1 . ASP C 1 262 ? 8.900   20.547  46.953  1.00 98.27  ? 264 ASP C OD1 1 
ATOM   6031  O OD2 . ASP C 1 262 ? 9.031   22.119  48.483  1.00 86.00  ? 264 ASP C OD2 1 
ATOM   6032  N N   . SER C 1 263 ? 5.794   23.860  49.525  1.00 49.46  ? 265 SER C N   1 
ATOM   6033  C CA  . SER C 1 263 ? 4.993   25.056  49.749  1.00 49.30  ? 265 SER C CA  1 
ATOM   6034  C C   . SER C 1 263 ? 5.797   26.244  49.222  1.00 46.18  ? 265 SER C C   1 
ATOM   6035  O O   . SER C 1 263 ? 6.672   26.077  48.366  1.00 46.93  ? 265 SER C O   1 
ATOM   6036  C CB  . SER C 1 263 ? 4.610   25.158  51.235  1.00 50.45  ? 265 SER C CB  1 
ATOM   6037  O OG  . SER C 1 263 ? 3.674   26.192  51.458  1.00 59.37  ? 265 SER C OG  1 
ATOM   6038  N N   . THR C 1 264 ? 5.473   27.450  49.686  1.00 47.26  ? 266 THR C N   1 
ATOM   6039  C CA  . THR C 1 264 ? 6.250   28.642  49.348  1.00 56.88  ? 266 THR C CA  1 
ATOM   6040  C C   . THR C 1 264 ? 6.356   29.521  50.592  1.00 59.19  ? 266 THR C C   1 
ATOM   6041  O O   . THR C 1 264 ? 5.964   29.124  51.695  1.00 53.83  ? 266 THR C O   1 
ATOM   6042  C CB  . THR C 1 264 ? 5.631   29.398  48.161  1.00 58.31  ? 266 THR C CB  1 
ATOM   6043  O OG1 . THR C 1 264 ? 6.582   30.336  47.637  1.00 57.14  ? 266 THR C OG1 1 
ATOM   6044  C CG2 . THR C 1 264 ? 4.381   30.154  48.590  1.00 48.81  ? 266 THR C CG2 1 
ATOM   6045  N N   . ILE C 1 265 ? 6.903   30.723  50.412  1.00 54.86  ? 267 ILE C N   1 
ATOM   6046  C CA  . ILE C 1 265 ? 7.046   31.713  51.473  1.00 43.56  ? 267 ILE C CA  1 
ATOM   6047  C C   . ILE C 1 265 ? 6.074   32.850  51.199  1.00 52.94  ? 267 ILE C C   1 
ATOM   6048  O O   . ILE C 1 265 ? 6.036   33.387  50.085  1.00 53.17  ? 267 ILE C O   1 
ATOM   6049  C CB  . ILE C 1 265 ? 8.488   32.241  51.563  1.00 54.50  ? 267 ILE C CB  1 
ATOM   6050  C CG1 . ILE C 1 265 ? 9.483   31.077  51.587  1.00 52.82  ? 267 ILE C CG1 1 
ATOM   6051  C CG2 . ILE C 1 265 ? 8.649   33.153  52.773  1.00 48.85  ? 267 ILE C CG2 1 
ATOM   6052  C CD1 . ILE C 1 265 ? 9.731   30.509  52.964  1.00 48.80  ? 267 ILE C CD1 1 
ATOM   6053  N N   . MET C 1 266 ? 5.301   33.226  52.214  1.00 50.59  ? 268 MET C N   1 
ATOM   6054  C CA  . MET C 1 266 ? 4.314   34.291  52.097  1.00 49.31  ? 268 MET C CA  1 
ATOM   6055  C C   . MET C 1 266 ? 4.831   35.544  52.789  1.00 53.05  ? 268 MET C C   1 
ATOM   6056  O O   . MET C 1 266 ? 5.277   35.485  53.939  1.00 54.56  ? 268 MET C O   1 
ATOM   6057  C CB  . MET C 1 266 ? 2.974   33.865  52.701  1.00 44.41  ? 268 MET C CB  1 
ATOM   6058  C CG  . MET C 1 266 ? 1.938   34.976  52.754  1.00 48.35  ? 268 MET C CG  1 
ATOM   6059  S SD  . MET C 1 266 ? 0.316   34.366  53.272  1.00 56.32  ? 268 MET C SD  1 
ATOM   6060  C CE  . MET C 1 266 ? -0.264  33.676  51.723  1.00 42.60  ? 268 MET C CE  1 
ATOM   6061  N N   . LYS C 1 267 ? 4.770   36.671  52.084  1.00 46.85  ? 269 LYS C N   1 
ATOM   6062  C CA  . LYS C 1 267 ? 5.200   37.962  52.613  1.00 59.58  ? 269 LYS C CA  1 
ATOM   6063  C C   . LYS C 1 267 ? 3.967   38.694  53.135  1.00 56.24  ? 269 LYS C C   1 
ATOM   6064  O O   . LYS C 1 267 ? 3.229   39.315  52.366  1.00 62.85  ? 269 LYS C O   1 
ATOM   6065  C CB  . LYS C 1 267 ? 5.927   38.769  51.543  1.00 46.71  ? 269 LYS C CB  1 
ATOM   6066  C CG  . LYS C 1 267 ? 7.246   38.162  51.119  1.00 52.12  ? 269 LYS C CG  1 
ATOM   6067  C CD  . LYS C 1 267 ? 8.088   37.783  52.333  1.00 67.14  ? 269 LYS C CD  1 
ATOM   6068  C CE  . LYS C 1 267 ? 9.561   38.064  52.094  1.00 65.07  ? 269 LYS C CE  1 
ATOM   6069  N NZ  . LYS C 1 267 ? 9.952   37.713  50.700  1.00 63.16  ? 269 LYS C NZ  1 
ATOM   6070  N N   . SER C 1 268 ? 3.751   38.623  54.449  1.00 54.91  ? 270 SER C N   1 
ATOM   6071  C CA  . SER C 1 268 ? 2.626   39.284  55.095  1.00 69.82  ? 270 SER C CA  1 
ATOM   6072  C C   . SER C 1 268 ? 3.090   39.934  56.392  1.00 68.19  ? 270 SER C C   1 
ATOM   6073  O O   . SER C 1 268 ? 4.015   39.454  57.051  1.00 57.67  ? 270 SER C O   1 
ATOM   6074  C CB  . SER C 1 268 ? 1.482   38.299  55.388  1.00 55.12  ? 270 SER C CB  1 
ATOM   6075  O OG  . SER C 1 268 ? 0.305   38.988  55.770  1.00 59.29  ? 270 SER C OG  1 
ATOM   6076  N N   . GLU C 1 269 ? 2.426   41.028  56.758  1.00 72.92  ? 271 GLU C N   1 
ATOM   6077  C CA  . GLU C 1 269 ? 2.714   41.735  57.998  1.00 79.38  ? 271 GLU C CA  1 
ATOM   6078  C C   . GLU C 1 269 ? 1.696   41.429  59.090  1.00 75.68  ? 271 GLU C C   1 
ATOM   6079  O O   . GLU C 1 269 ? 1.667   42.122  60.112  1.00 78.05  ? 271 GLU C O   1 
ATOM   6080  C CB  . GLU C 1 269 ? 2.785   43.243  57.738  1.00 67.91  ? 271 GLU C CB  1 
ATOM   6081  C CG  . GLU C 1 269 ? 4.206   43.801  57.714  1.00 84.54  ? 271 GLU C CG  1 
ATOM   6082  C CD  . GLU C 1 269 ? 4.880   43.662  56.356  1.00 89.41  ? 271 GLU C CD  1 
ATOM   6083  O OE1 . GLU C 1 269 ? 4.298   43.021  55.453  1.00 89.40  ? 271 GLU C OE1 1 
ATOM   6084  O OE2 . GLU C 1 269 ? 6.001   44.190  56.193  1.00 91.53  ? 271 GLU C OE2 1 
ATOM   6085  N N   . MET C 1 270 ? 0.870   40.405  58.901  1.00 69.30  ? 272 MET C N   1 
ATOM   6086  C CA  . MET C 1 270 ? -0.151  40.027  59.863  1.00 69.15  ? 272 MET C CA  1 
ATOM   6087  C C   . MET C 1 270 ? 0.346   38.873  60.732  1.00 64.73  ? 272 MET C C   1 
ATOM   6088  O O   . MET C 1 270 ? 1.441   38.341  60.541  1.00 70.01  ? 272 MET C O   1 
ATOM   6089  C CB  . MET C 1 270 ? -1.452  39.667  59.142  1.00 63.03  ? 272 MET C CB  1 
ATOM   6090  C CG  . MET C 1 270 ? -2.291  40.876  58.747  1.00 58.25  ? 272 MET C CG  1 
ATOM   6091  S SD  . MET C 1 270 ? -3.763  40.481  57.776  1.00 79.11  ? 272 MET C SD  1 
ATOM   6092  C CE  . MET C 1 270 ? -3.684  38.688  57.730  1.00 62.45  ? 272 MET C CE  1 
ATOM   6093  N N   . GLU C 1 271 ? -0.480  38.482  61.704  1.00 77.80  ? 273 GLU C N   1 
ATOM   6094  C CA  . GLU C 1 271 ? -0.113  37.424  62.638  1.00 78.19  ? 273 GLU C CA  1 
ATOM   6095  C C   . GLU C 1 271 ? -1.160  36.319  62.675  1.00 77.23  ? 273 GLU C C   1 
ATOM   6096  O O   . GLU C 1 271 ? -2.087  36.300  61.857  1.00 77.88  ? 273 GLU C O   1 
ATOM   6097  C CB  . GLU C 1 271 ? 0.094   37.997  64.041  1.00 82.37  ? 273 GLU C CB  1 
ATOM   6098  C CG  . GLU C 1 271 ? 1.546   38.282  64.375  1.00 93.28  ? 273 GLU C CG  1 
ATOM   6099  C CD  . GLU C 1 271 ? 1.701   39.343  65.446  1.00 106.54 ? 273 GLU C CD  1 
ATOM   6100  O OE1 . GLU C 1 271 ? 0.757   40.141  65.635  1.00 104.88 ? 273 GLU C OE1 1 
ATOM   6101  O OE2 . GLU C 1 271 ? 2.769   39.378  66.095  1.00 83.37  ? 273 GLU C OE2 1 
ATOM   6102  N N   . TYR C 1 272 ? -1.016  35.397  63.626  1.00 60.14  ? 274 TYR C N   1 
ATOM   6103  C CA  . TYR C 1 272 ? -1.913  34.253  63.706  1.00 65.20  ? 274 TYR C CA  1 
ATOM   6104  C C   . TYR C 1 272 ? -3.351  34.700  63.955  1.00 67.98  ? 274 TYR C C   1 
ATOM   6105  O O   . TYR C 1 272 ? -3.610  35.617  64.739  1.00 67.51  ? 274 TYR C O   1 
ATOM   6106  C CB  . TYR C 1 272 ? -1.460  33.310  64.817  1.00 54.77  ? 274 TYR C CB  1 
ATOM   6107  C CG  . TYR C 1 272 ? -2.036  31.925  64.705  1.00 67.33  ? 274 TYR C CG  1 
ATOM   6108  C CD1 . TYR C 1 272 ? -2.456  31.427  63.482  1.00 68.51  ? 274 TYR C CD1 1 
ATOM   6109  C CD2 . TYR C 1 272 ? -2.153  31.110  65.821  1.00 73.94  ? 274 TYR C CD2 1 
ATOM   6110  C CE1 . TYR C 1 272 ? -2.984  30.160  63.375  1.00 79.95  ? 274 TYR C CE1 1 
ATOM   6111  C CE2 . TYR C 1 272 ? -2.676  29.840  65.725  1.00 67.68  ? 274 TYR C CE2 1 
ATOM   6112  C CZ  . TYR C 1 272 ? -3.091  29.370  64.500  1.00 78.02  ? 274 TYR C CZ  1 
ATOM   6113  O OH  . TYR C 1 272 ? -3.613  28.105  64.402  1.00 88.18  ? 274 TYR C OH  1 
ATOM   6114  N N   . GLY C 1 273 ? -4.288  34.043  63.273  1.00 66.99  ? 275 GLY C N   1 
ATOM   6115  C CA  . GLY C 1 273 ? -5.698  34.345  63.420  1.00 61.79  ? 275 GLY C CA  1 
ATOM   6116  C C   . GLY C 1 273 ? -6.507  33.245  64.079  1.00 63.31  ? 275 GLY C C   1 
ATOM   6117  O O   . GLY C 1 273 ? -7.729  33.376  64.208  1.00 73.72  ? 275 GLY C O   1 
ATOM   6118  N N   . HIS C 1 274 ? -5.848  32.160  64.488  1.00 69.97  ? 276 HIS C N   1 
ATOM   6119  C CA  . HIS C 1 274 ? -6.488  31.033  65.171  1.00 72.85  ? 276 HIS C CA  1 
ATOM   6120  C C   . HIS C 1 274 ? -7.655  30.485  64.349  1.00 75.97  ? 276 HIS C C   1 
ATOM   6121  O O   . HIS C 1 274 ? -8.807  30.462  64.783  1.00 79.08  ? 276 HIS C O   1 
ATOM   6122  C CB  . HIS C 1 274 ? -6.944  31.433  66.575  1.00 66.06  ? 276 HIS C CB  1 
ATOM   6123  C CG  . HIS C 1 274 ? -5.846  31.991  67.424  1.00 76.80  ? 276 HIS C CG  1 
ATOM   6124  N ND1 . HIS C 1 274 ? -5.700  33.342  67.658  1.00 71.82  ? 276 HIS C ND1 1 
ATOM   6125  C CD2 . HIS C 1 274 ? -4.835  31.381  68.088  1.00 67.05  ? 276 HIS C CD2 1 
ATOM   6126  C CE1 . HIS C 1 274 ? -4.649  33.540  68.433  1.00 62.40  ? 276 HIS C CE1 1 
ATOM   6127  N NE2 . HIS C 1 274 ? -4.107  32.367  68.709  1.00 71.94  ? 276 HIS C NE2 1 
ATOM   6128  N N   . CYS C 1 275 ? -7.331  30.040  63.139  1.00 77.67  ? 277 CYS C N   1 
ATOM   6129  C CA  . CYS C 1 275 ? -8.340  29.628  62.174  1.00 77.74  ? 277 CYS C CA  1 
ATOM   6130  C C   . CYS C 1 275 ? -7.752  28.574  61.244  1.00 70.27  ? 277 CYS C C   1 
ATOM   6131  O O   . CYS C 1 275 ? -6.542  28.340  61.219  1.00 74.63  ? 277 CYS C O   1 
ATOM   6132  C CB  . CYS C 1 275 ? -8.878  30.843  61.406  1.00 76.27  ? 277 CYS C CB  1 
ATOM   6133  S SG  . CYS C 1 275 ? -7.579  31.953  60.764  1.00 98.03  ? 277 CYS C SG  1 
ATOM   6134  N N   . ASN C 1 276 ? -8.638  27.921  60.492  1.00 75.58  ? 278 ASN C N   1 
ATOM   6135  C CA  . ASN C 1 276 ? -8.274  26.881  59.539  1.00 61.65  ? 278 ASN C CA  1 
ATOM   6136  C C   . ASN C 1 276 ? -8.849  27.246  58.180  1.00 62.44  ? 278 ASN C C   1 
ATOM   6137  O O   . ASN C 1 276 ? -9.955  27.786  58.093  1.00 64.11  ? 278 ASN C O   1 
ATOM   6138  C CB  . ASN C 1 276 ? -8.801  25.509  59.982  1.00 60.13  ? 278 ASN C CB  1 
ATOM   6139  C CG  . ASN C 1 276 ? -8.049  24.353  59.340  1.00 69.07  ? 278 ASN C CG  1 
ATOM   6140  O OD1 . ASN C 1 276 ? -7.084  24.553  58.607  1.00 68.65  ? 278 ASN C OD1 1 
ATOM   6141  N ND2 . ASN C 1 276 ? -8.493  23.132  59.620  1.00 76.30  ? 278 ASN C ND2 1 
ATOM   6142  N N   . THR C 1 277 ? -8.097  26.956  57.120  1.00 57.07  ? 279 THR C N   1 
ATOM   6143  C CA  . THR C 1 277 ? -8.527  27.328  55.780  1.00 51.06  ? 279 THR C CA  1 
ATOM   6144  C C   . THR C 1 277 ? -7.960  26.359  54.757  1.00 52.97  ? 279 THR C C   1 
ATOM   6145  O O   . THR C 1 277 ? -7.030  25.596  55.031  1.00 51.83  ? 279 THR C O   1 
ATOM   6146  C CB  . THR C 1 277 ? -8.102  28.750  55.412  1.00 56.49  ? 279 THR C CB  1 
ATOM   6147  O OG1 . THR C 1 277 ? -8.735  29.134  54.184  1.00 60.66  ? 279 THR C OG1 1 
ATOM   6148  C CG2 . THR C 1 277 ? -6.591  28.823  55.235  1.00 59.31  ? 279 THR C CG2 1 
ATOM   6149  N N   . LYS C 1 278 ? -8.557  26.397  53.567  1.00 59.17  ? 280 LYS C N   1 
ATOM   6150  C CA  . LYS C 1 278 ? -8.074  25.656  52.412  1.00 61.43  ? 280 LYS C CA  1 
ATOM   6151  C C   . LYS C 1 278 ? -7.272  26.527  51.456  1.00 52.11  ? 280 LYS C C   1 
ATOM   6152  O O   . LYS C 1 278 ? -6.519  25.993  50.633  1.00 45.42  ? 280 LYS C O   1 
ATOM   6153  C CB  . LYS C 1 278 ? -9.263  25.031  51.665  1.00 53.38  ? 280 LYS C CB  1 
ATOM   6154  C CG  . LYS C 1 278 ? -8.926  23.809  50.831  1.00 68.19  ? 280 LYS C CG  1 
ATOM   6155  C CD  . LYS C 1 278 ? -10.194 23.078  50.401  1.00 76.00  ? 280 LYS C CD  1 
ATOM   6156  C CE  . LYS C 1 278 ? -10.940 23.846  49.317  1.00 70.10  ? 280 LYS C CE  1 
ATOM   6157  N NZ  . LYS C 1 278 ? -11.553 22.936  48.308  1.00 72.58  ? 280 LYS C NZ  1 
ATOM   6158  N N   . CYS C 1 279 ? -7.414  27.849  51.552  1.00 52.19  ? 281 CYS C N   1 
ATOM   6159  C CA  . CYS C 1 279 ? -6.798  28.793  50.626  1.00 50.73  ? 281 CYS C CA  1 
ATOM   6160  C C   . CYS C 1 279 ? -6.414  30.051  51.389  1.00 59.59  ? 281 CYS C C   1 
ATOM   6161  O O   . CYS C 1 279 ? -7.288  30.749  51.915  1.00 57.97  ? 281 CYS C O   1 
ATOM   6162  C CB  . CYS C 1 279 ? -7.750  29.138  49.478  1.00 56.60  ? 281 CYS C CB  1 
ATOM   6163  S SG  . CYS C 1 279 ? -7.110  30.386  48.361  1.00 63.81  ? 281 CYS C SG  1 
ATOM   6164  N N   . GLN C 1 280 ? -5.119  30.349  51.427  1.00 57.18  ? 282 GLN C N   1 
ATOM   6165  C CA  . GLN C 1 280 ? -4.586  31.457  52.204  1.00 47.78  ? 282 GLN C CA  1 
ATOM   6166  C C   . GLN C 1 280 ? -4.006  32.522  51.281  1.00 46.53  ? 282 GLN C C   1 
ATOM   6167  O O   . GLN C 1 280 ? -3.342  32.208  50.289  1.00 50.48  ? 282 GLN C O   1 
ATOM   6168  C CB  . GLN C 1 280 ? -3.510  30.966  53.183  1.00 52.90  ? 282 GLN C CB  1 
ATOM   6169  C CG  . GLN C 1 280 ? -2.899  32.063  54.045  1.00 45.26  ? 282 GLN C CG  1 
ATOM   6170  C CD  . GLN C 1 280 ? -3.888  32.637  55.041  1.00 60.12  ? 282 GLN C CD  1 
ATOM   6171  O OE1 . GLN C 1 280 ? -4.444  31.915  55.867  1.00 56.30  ? 282 GLN C OE1 1 
ATOM   6172  N NE2 . GLN C 1 280 ? -4.118  33.945  54.962  1.00 59.25  ? 282 GLN C NE2 1 
ATOM   6173  N N   . THR C 1 281 ? -4.272  33.777  51.609  1.00 55.49  ? 283 THR C N   1 
ATOM   6174  C CA  . THR C 1 281 ? -3.724  34.940  50.936  1.00 51.79  ? 283 THR C CA  1 
ATOM   6175  C C   . THR C 1 281 ? -3.010  35.810  51.963  1.00 56.24  ? 283 THR C C   1 
ATOM   6176  O O   . THR C 1 281 ? -3.247  35.675  53.169  1.00 55.89  ? 283 THR C O   1 
ATOM   6177  C CB  . THR C 1 281 ? -4.828  35.752  50.245  1.00 47.24  ? 283 THR C CB  1 
ATOM   6178  O OG1 . THR C 1 281 ? -5.410  36.654  51.192  1.00 54.47  ? 283 THR C OG1 1 
ATOM   6179  C CG2 . THR C 1 281 ? -5.903  34.831  49.681  1.00 53.36  ? 283 THR C CG2 1 
ATOM   6180  N N   . PRO C 1 282 ? -2.110  36.696  51.528  1.00 51.38  ? 284 PRO C N   1 
ATOM   6181  C CA  . PRO C 1 282 ? -1.388  37.530  52.504  1.00 58.39  ? 284 PRO C CA  1 
ATOM   6182  C C   . PRO C 1 282 ? -2.289  38.461  53.296  1.00 61.03  ? 284 PRO C C   1 
ATOM   6183  O O   . PRO C 1 282 ? -1.877  38.928  54.367  1.00 63.80  ? 284 PRO C O   1 
ATOM   6184  C CB  . PRO C 1 282 ? -0.396  38.318  51.634  1.00 57.91  ? 284 PRO C CB  1 
ATOM   6185  C CG  . PRO C 1 282 ? -0.287  37.544  50.360  1.00 58.32  ? 284 PRO C CG  1 
ATOM   6186  C CD  . PRO C 1 282 ? -1.629  36.917  50.153  1.00 58.07  ? 284 PRO C CD  1 
ATOM   6187  N N   . ILE C 1 283 ? -3.498  38.745  52.813  1.00 52.95  ? 285 ILE C N   1 
ATOM   6188  C CA  . ILE C 1 283 ? -4.412  39.678  53.463  1.00 47.48  ? 285 ILE C CA  1 
ATOM   6189  C C   . ILE C 1 283 ? -5.625  38.971  54.057  1.00 61.55  ? 285 ILE C C   1 
ATOM   6190  O O   . ILE C 1 283 ? -6.562  39.636  54.515  1.00 59.77  ? 285 ILE C O   1 
ATOM   6191  C CB  . ILE C 1 283 ? -4.854  40.789  52.499  1.00 53.23  ? 285 ILE C CB  1 
ATOM   6192  C CG1 . ILE C 1 283 ? -5.669  40.201  51.342  1.00 55.25  ? 285 ILE C CG1 1 
ATOM   6193  C CG2 . ILE C 1 283 ? -3.646  41.553  51.991  1.00 34.00  ? 285 ILE C CG2 1 
ATOM   6194  C CD1 . ILE C 1 283 ? -6.320  41.245  50.447  1.00 57.18  ? 285 ILE C CD1 1 
ATOM   6195  N N   . GLY C 1 284 ? -5.643  37.647  54.054  1.00 60.54  ? 286 GLY C N   1 
ATOM   6196  C CA  . GLY C 1 284 ? -6.728  36.888  54.652  1.00 53.79  ? 286 GLY C CA  1 
ATOM   6197  C C   . GLY C 1 284 ? -7.103  35.660  53.846  1.00 54.15  ? 286 GLY C C   1 
ATOM   6198  O O   . GLY C 1 284 ? -6.957  35.610  52.625  1.00 56.93  ? 286 GLY C O   1 
ATOM   6199  N N   . ALA C 1 285 ? -7.601  34.644  54.542  1.00 45.95  ? 287 ALA C N   1 
ATOM   6200  C CA  . ALA C 1 285 ? -7.992  33.406  53.895  1.00 52.88  ? 287 ALA C CA  1 
ATOM   6201  C C   . ALA C 1 285 ? -9.385  33.534  53.284  1.00 59.63  ? 287 ALA C C   1 
ATOM   6202  O O   . ALA C 1 285 ? -10.177 34.409  53.648  1.00 49.01  ? 287 ALA C O   1 
ATOM   6203  C CB  . ALA C 1 285 ? -7.947  32.250  54.890  1.00 41.64  ? 287 ALA C CB  1 
ATOM   6204  N N   . ILE C 1 286 ? -9.675  32.653  52.329  1.00 56.90  ? 288 ILE C N   1 
ATOM   6205  C CA  . ILE C 1 286 ? -10.972 32.617  51.665  1.00 57.03  ? 288 ILE C CA  1 
ATOM   6206  C C   . ILE C 1 286 ? -11.519 31.200  51.739  1.00 55.72  ? 288 ILE C C   1 
ATOM   6207  O O   . ILE C 1 286 ? -10.776 30.223  51.588  1.00 55.65  ? 288 ILE C O   1 
ATOM   6208  C CB  . ILE C 1 286 ? -10.898 33.110  50.202  1.00 54.23  ? 288 ILE C CB  1 
ATOM   6209  C CG1 . ILE C 1 286 ? -9.984  32.223  49.361  1.00 58.52  ? 288 ILE C CG1 1 
ATOM   6210  C CG2 . ILE C 1 286 ? -10.428 34.560  50.149  1.00 58.70  ? 288 ILE C CG2 1 
ATOM   6211  C CD1 . ILE C 1 286 ? -9.488  32.901  48.088  1.00 58.57  ? 288 ILE C CD1 1 
ATOM   6212  N N   . ASN C 1 287 ? -12.819 31.094  52.006  1.00 55.64  ? 289 ASN C N   1 
ATOM   6213  C CA  . ASN C 1 287 ? -13.517 29.818  52.137  1.00 60.27  ? 289 ASN C CA  1 
ATOM   6214  C C   . ASN C 1 287 ? -14.747 29.884  51.238  1.00 57.61  ? 289 ASN C C   1 
ATOM   6215  O O   . ASN C 1 287 ? -15.740 30.528  51.588  1.00 62.03  ? 289 ASN C O   1 
ATOM   6216  C CB  . ASN C 1 287 ? -13.897 29.546  53.593  1.00 52.83  ? 289 ASN C CB  1 
ATOM   6217  C CG  . ASN C 1 287 ? -14.915 28.430  53.736  1.00 67.39  ? 289 ASN C CG  1 
ATOM   6218  O OD1 . ASN C 1 287 ? -14.887 27.449  52.993  1.00 69.84  ? 289 ASN C OD1 1 
ATOM   6219  N ND2 . ASN C 1 287 ? -15.820 28.573  54.703  1.00 80.06  ? 289 ASN C ND2 1 
ATOM   6220  N N   . SER C 1 288 ? -14.676 29.237  50.078  1.00 57.66  ? 290 SER C N   1 
ATOM   6221  C CA  . SER C 1 288 ? -15.805 29.215  49.158  1.00 65.94  ? 290 SER C CA  1 
ATOM   6222  C C   . SER C 1 288 ? -15.595 28.113  48.131  1.00 59.01  ? 290 SER C C   1 
ATOM   6223  O O   . SER C 1 288 ? -14.493 27.578  47.978  1.00 47.47  ? 290 SER C O   1 
ATOM   6224  C CB  . SER C 1 288 ? -15.998 30.570  48.465  1.00 59.76  ? 290 SER C CB  1 
ATOM   6225  O OG  . SER C 1 288 ? -15.221 30.667  47.286  1.00 54.28  ? 290 SER C OG  1 
ATOM   6226  N N   . SER C 1 289 ? -16.680 27.775  47.437  1.00 59.63  ? 291 SER C N   1 
ATOM   6227  C CA  . SER C 1 289 ? -16.644 26.815  46.342  1.00 63.07  ? 291 SER C CA  1 
ATOM   6228  C C   . SER C 1 289 ? -16.784 27.488  44.983  1.00 49.68  ? 291 SER C C   1 
ATOM   6229  O O   . SER C 1 289 ? -16.927 26.795  43.969  1.00 51.58  ? 291 SER C O   1 
ATOM   6230  C CB  . SER C 1 289 ? -17.736 25.761  46.524  1.00 49.77  ? 291 SER C CB  1 
ATOM   6231  O OG  . SER C 1 289 ? -19.002 26.375  46.687  1.00 71.82  ? 291 SER C OG  1 
ATOM   6232  N N   . MET C 1 290 ? -16.740 28.818  44.938  1.00 46.10  ? 292 MET C N   1 
ATOM   6233  C CA  . MET C 1 290 ? -16.877 29.531  43.680  1.00 50.85  ? 292 MET C CA  1 
ATOM   6234  C C   . MET C 1 290 ? -15.657 29.287  42.793  1.00 48.48  ? 292 MET C C   1 
ATOM   6235  O O   . MET C 1 290 ? -14.542 29.102  43.289  1.00 51.86  ? 292 MET C O   1 
ATOM   6236  C CB  . MET C 1 290 ? -17.061 31.026  43.931  1.00 37.57  ? 292 MET C CB  1 
ATOM   6237  C CG  . MET C 1 290 ? -18.365 31.376  44.630  1.00 42.83  ? 292 MET C CG  1 
ATOM   6238  S SD  . MET C 1 290 ? -19.823 30.701  43.788  1.00 67.49  ? 292 MET C SD  1 
ATOM   6239  C CE  . MET C 1 290 ? -20.281 29.346  44.875  1.00 49.19  ? 292 MET C CE  1 
ATOM   6240  N N   . PRO C 1 291 ? -15.846 29.260  41.472  1.00 45.16  ? 293 PRO C N   1 
ATOM   6241  C CA  . PRO C 1 291 ? -14.713 28.973  40.581  1.00 45.45  ? 293 PRO C CA  1 
ATOM   6242  C C   . PRO C 1 291 ? -13.727 30.120  40.447  1.00 44.24  ? 293 PRO C C   1 
ATOM   6243  O O   . PRO C 1 291 ? -12.583 29.877  40.044  1.00 43.87  ? 293 PRO C O   1 
ATOM   6244  C CB  . PRO C 1 291 ? -15.390 28.662  39.240  1.00 40.51  ? 293 PRO C CB  1 
ATOM   6245  C CG  . PRO C 1 291 ? -16.683 29.395  39.297  1.00 44.16  ? 293 PRO C CG  1 
ATOM   6246  C CD  . PRO C 1 291 ? -17.117 29.382  40.738  1.00 46.60  ? 293 PRO C CD  1 
ATOM   6247  N N   . PHE C 1 292 ? -14.114 31.351  40.779  1.00 44.36  ? 294 PHE C N   1 
ATOM   6248  C CA  . PHE C 1 292 ? -13.251 32.504  40.570  1.00 53.39  ? 294 PHE C CA  1 
ATOM   6249  C C   . PHE C 1 292 ? -13.217 33.385  41.810  1.00 57.27  ? 294 PHE C C   1 
ATOM   6250  O O   . PHE C 1 292 ? -14.163 33.409  42.604  1.00 53.89  ? 294 PHE C O   1 
ATOM   6251  C CB  . PHE C 1 292 ? -13.712 33.327  39.357  1.00 39.79  ? 294 PHE C CB  1 
ATOM   6252  C CG  . PHE C 1 292 ? -13.935 32.502  38.128  1.00 42.93  ? 294 PHE C CG  1 
ATOM   6253  C CD1 . PHE C 1 292 ? -12.866 31.940  37.453  1.00 44.70  ? 294 PHE C CD1 1 
ATOM   6254  C CD2 . PHE C 1 292 ? -15.215 32.269  37.658  1.00 48.65  ? 294 PHE C CD2 1 
ATOM   6255  C CE1 . PHE C 1 292 ? -13.069 31.169  36.325  1.00 39.38  ? 294 PHE C CE1 1 
ATOM   6256  C CE2 . PHE C 1 292 ? -15.425 31.500  36.534  1.00 41.18  ? 294 PHE C CE2 1 
ATOM   6257  C CZ  . PHE C 1 292 ? -14.351 30.948  35.866  1.00 33.25  ? 294 PHE C CZ  1 
ATOM   6258  N N   . HIS C 1 293 ? -12.105 34.105  41.965  1.00 55.30  ? 295 HIS C N   1 
ATOM   6259  C CA  . HIS C 1 293 ? -11.939 35.092  43.024  1.00 53.46  ? 295 HIS C CA  1 
ATOM   6260  C C   . HIS C 1 293 ? -11.088 36.240  42.497  1.00 50.40  ? 295 HIS C C   1 
ATOM   6261  O O   . HIS C 1 293 ? -10.347 36.093  41.521  1.00 49.42  ? 295 HIS C O   1 
ATOM   6262  C CB  . HIS C 1 293 ? -11.310 34.475  44.281  1.00 49.36  ? 295 HIS C CB  1 
ATOM   6263  C CG  . HIS C 1 293 ? -9.823  34.301  44.199  1.00 54.28  ? 295 HIS C CG  1 
ATOM   6264  N ND1 . HIS C 1 293 ? -8.934  35.289  44.566  1.00 48.02  ? 295 HIS C ND1 1 
ATOM   6265  C CD2 . HIS C 1 293 ? -9.069  33.245  43.808  1.00 51.00  ? 295 HIS C CD2 1 
ATOM   6266  C CE1 . HIS C 1 293 ? -7.698  34.851  44.399  1.00 50.86  ? 295 HIS C CE1 1 
ATOM   6267  N NE2 . HIS C 1 293 ? -7.753  33.613  43.940  1.00 52.10  ? 295 HIS C NE2 1 
ATOM   6268  N N   . ASN C 1 294 ? -11.204 37.393  43.155  1.00 41.78  ? 296 ASN C N   1 
ATOM   6269  C CA  . ASN C 1 294 ? -10.406 38.572  42.826  1.00 53.73  ? 296 ASN C CA  1 
ATOM   6270  C C   . ASN C 1 294 ? -9.723  39.132  44.071  1.00 48.45  ? 296 ASN C C   1 
ATOM   6271  O O   . ASN C 1 294 ? -9.572  40.347  44.226  1.00 41.82  ? 296 ASN C O   1 
ATOM   6272  C CB  . ASN C 1 294 ? -11.264 39.641  42.153  1.00 41.71  ? 296 ASN C CB  1 
ATOM   6273  C CG  . ASN C 1 294 ? -12.296 40.240  43.091  1.00 46.20  ? 296 ASN C CG  1 
ATOM   6274  O OD1 . ASN C 1 294 ? -12.537 39.723  44.184  1.00 40.63  ? 296 ASN C OD1 1 
ATOM   6275  N ND2 . ASN C 1 294 ? -12.918 41.333  42.663  1.00 43.66  ? 296 ASN C ND2 1 
ATOM   6276  N N   . ILE C 1 295 ? -9.292  38.251  44.974  1.00 45.08  ? 297 ILE C N   1 
ATOM   6277  C CA  . ILE C 1 295 ? -8.746  38.692  46.256  1.00 46.24  ? 297 ILE C CA  1 
ATOM   6278  C C   . ILE C 1 295 ? -7.300  39.142  46.106  1.00 48.72  ? 297 ILE C C   1 
ATOM   6279  O O   . ILE C 1 295 ? -6.957  40.300  46.371  1.00 62.80  ? 297 ILE C O   1 
ATOM   6280  C CB  . ILE C 1 295 ? -8.865  37.571  47.307  1.00 52.86  ? 297 ILE C CB  1 
ATOM   6281  C CG1 . ILE C 1 295 ? -10.299 37.047  47.383  1.00 54.93  ? 297 ILE C CG1 1 
ATOM   6282  C CG2 . ILE C 1 295 ? -8.410  38.069  48.667  1.00 44.28  ? 297 ILE C CG2 1 
ATOM   6283  C CD1 . ILE C 1 295 ? -11.280 38.057  47.910  1.00 49.11  ? 297 ILE C CD1 1 
ATOM   6284  N N   . HIS C 1 296 ? -6.431  38.228  45.684  1.00 47.78  ? 298 HIS C N   1 
ATOM   6285  C CA  . HIS C 1 296 ? -4.992  38.441  45.722  1.00 52.24  ? 298 HIS C CA  1 
ATOM   6286  C C   . HIS C 1 296 ? -4.312  37.352  44.905  1.00 51.84  ? 298 HIS C C   1 
ATOM   6287  O O   . HIS C 1 296 ? -4.692  36.179  45.001  1.00 55.57  ? 298 HIS C O   1 
ATOM   6288  C CB  . HIS C 1 296 ? -4.493  38.427  47.169  1.00 53.83  ? 298 HIS C CB  1 
ATOM   6289  C CG  . HIS C 1 296 ? -3.180  39.115  47.370  1.00 59.68  ? 298 HIS C CG  1 
ATOM   6290  N ND1 . HIS C 1 296 ? -1.978  38.552  46.993  1.00 58.17  ? 298 HIS C ND1 1 
ATOM   6291  C CD2 . HIS C 1 296 ? -2.877  40.310  47.929  1.00 53.44  ? 298 HIS C CD2 1 
ATOM   6292  C CE1 . HIS C 1 296 ? -0.993  39.377  47.299  1.00 45.78  ? 298 HIS C CE1 1 
ATOM   6293  N NE2 . HIS C 1 296 ? -1.511  40.450  47.869  1.00 48.63  ? 298 HIS C NE2 1 
ATOM   6294  N N   . PRO C 1 297 ? -3.309  37.694  44.093  1.00 49.45  ? 299 PRO C N   1 
ATOM   6295  C CA  . PRO C 1 297 ? -2.658  36.659  43.272  1.00 48.44  ? 299 PRO C CA  1 
ATOM   6296  C C   . PRO C 1 297 ? -1.785  35.699  44.062  1.00 44.45  ? 299 PRO C C   1 
ATOM   6297  O O   . PRO C 1 297 ? -1.590  34.559  43.625  1.00 45.32  ? 299 PRO C O   1 
ATOM   6298  C CB  . PRO C 1 297 ? -1.827  37.476  42.273  1.00 45.66  ? 299 PRO C CB  1 
ATOM   6299  C CG  . PRO C 1 297 ? -1.586  38.785  42.967  1.00 44.75  ? 299 PRO C CG  1 
ATOM   6300  C CD  . PRO C 1 297 ? -2.809  39.048  43.797  1.00 40.45  ? 299 PRO C CD  1 
ATOM   6301  N N   . LEU C 1 298 ? -1.241  36.117  45.204  1.00 52.36  ? 300 LEU C N   1 
ATOM   6302  C CA  . LEU C 1 298 ? -0.239  35.312  45.906  1.00 56.13  ? 300 LEU C CA  1 
ATOM   6303  C C   . LEU C 1 298 ? -0.944  34.383  46.890  1.00 48.91  ? 300 LEU C C   1 
ATOM   6304  O O   . LEU C 1 298 ? -0.953  34.588  48.105  1.00 54.29  ? 300 LEU C O   1 
ATOM   6305  C CB  . LEU C 1 298 ? 0.783   36.211  46.589  1.00 41.74  ? 300 LEU C CB  1 
ATOM   6306  C CG  . LEU C 1 298 ? 1.466   37.204  45.642  1.00 62.11  ? 300 LEU C CG  1 
ATOM   6307  C CD1 . LEU C 1 298 ? 2.455   38.104  46.383  1.00 48.14  ? 300 LEU C CD1 1 
ATOM   6308  C CD2 . LEU C 1 298 ? 2.153   36.461  44.507  1.00 49.18  ? 300 LEU C CD2 1 
ATOM   6309  N N   . THR C 1 299 ? -1.533  33.327  46.342  1.00 47.79  ? 301 THR C N   1 
ATOM   6310  C CA  . THR C 1 299 ? -2.315  32.380  47.119  1.00 49.83  ? 301 THR C CA  1 
ATOM   6311  C C   . THR C 1 299 ? -1.510  31.119  47.404  1.00 44.81  ? 301 THR C C   1 
ATOM   6312  O O   . THR C 1 299 ? -0.620  30.738  46.640  1.00 46.35  ? 301 THR C O   1 
ATOM   6313  C CB  . THR C 1 299 ? -3.607  32.013  46.384  1.00 49.03  ? 301 THR C CB  1 
ATOM   6314  O OG1 . THR C 1 299 ? -3.291  31.560  45.062  1.00 52.86  ? 301 THR C OG1 1 
ATOM   6315  C CG2 . THR C 1 299 ? -4.531  33.219  46.294  1.00 43.58  ? 301 THR C CG2 1 
ATOM   6316  N N   . ILE C 1 300 ? -1.823  30.483  48.530  1.00 40.40  ? 302 ILE C N   1 
ATOM   6317  C CA  . ILE C 1 300 ? -1.272  29.181  48.883  1.00 44.45  ? 302 ILE C CA  1 
ATOM   6318  C C   . ILE C 1 300 ? -2.428  28.277  49.273  1.00 57.94  ? 302 ILE C C   1 
ATOM   6319  O O   . ILE C 1 300 ? -3.163  28.581  50.222  1.00 62.85  ? 302 ILE C O   1 
ATOM   6320  C CB  . ILE C 1 300 ? -0.260  29.263  50.034  1.00 55.89  ? 302 ILE C CB  1 
ATOM   6321  C CG1 . ILE C 1 300 ? 0.903   30.186  49.675  1.00 49.52  ? 302 ILE C CG1 1 
ATOM   6322  C CG2 . ILE C 1 300 ? 0.241   27.876  50.378  1.00 39.77  ? 302 ILE C CG2 1 
ATOM   6323  C CD1 . ILE C 1 300 ? 1.682   30.642  50.884  1.00 52.11  ? 302 ILE C CD1 1 
ATOM   6324  N N   . GLY C 1 301 ? -2.582  27.165  48.560  1.00 55.71  ? 303 GLY C N   1 
ATOM   6325  C CA  . GLY C 1 301 ? -3.617  26.202  48.849  1.00 49.73  ? 303 GLY C CA  1 
ATOM   6326  C C   . GLY C 1 301 ? -4.434  25.900  47.614  1.00 51.30  ? 303 GLY C C   1 
ATOM   6327  O O   . GLY C 1 301 ? -4.019  26.176  46.483  1.00 54.10  ? 303 GLY C O   1 
ATOM   6328  N N   . GLU C 1 302 ? -5.604  25.308  47.846  1.00 61.21  ? 304 GLU C N   1 
ATOM   6329  C CA  . GLU C 1 302 ? -6.572  25.020  46.794  1.00 52.70  ? 304 GLU C CA  1 
ATOM   6330  C C   . GLU C 1 302 ? -7.499  26.223  46.680  1.00 52.73  ? 304 GLU C C   1 
ATOM   6331  O O   . GLU C 1 302 ? -8.314  26.474  47.573  1.00 65.55  ? 304 GLU C O   1 
ATOM   6332  C CB  . GLU C 1 302 ? -7.347  23.743  47.110  1.00 60.60  ? 304 GLU C CB  1 
ATOM   6333  C CG  . GLU C 1 302 ? -7.832  22.985  45.887  1.00 63.03  ? 304 GLU C CG  1 
ATOM   6334  C CD  . GLU C 1 302 ? -7.929  21.486  46.121  1.00 78.17  ? 304 GLU C CD  1 
ATOM   6335  O OE1 . GLU C 1 302 ? -7.141  20.956  46.934  1.00 87.26  ? 304 GLU C OE1 1 
ATOM   6336  O OE2 . GLU C 1 302 ? -8.793  20.838  45.488  1.00 75.57  ? 304 GLU C OE2 1 
ATOM   6337  N N   . CYS C 1 303 ? -7.380  26.963  45.589  1.00 46.61  ? 305 CYS C N   1 
ATOM   6338  C CA  . CYS C 1 303 ? -7.992  28.274  45.465  1.00 49.49  ? 305 CYS C CA  1 
ATOM   6339  C C   . CYS C 1 303 ? -8.784  28.371  44.172  1.00 43.54  ? 305 CYS C C   1 
ATOM   6340  O O   . CYS C 1 303 ? -8.540  27.619  43.223  1.00 48.23  ? 305 CYS C O   1 
ATOM   6341  C CB  . CYS C 1 303 ? -6.913  29.365  45.505  1.00 51.66  ? 305 CYS C CB  1 
ATOM   6342  S SG  . CYS C 1 303 ? -5.950  29.367  47.044  1.00 72.43  ? 305 CYS C SG  1 
ATOM   6343  N N   . PRO C 1 304 ? -9.759  29.273  44.110  1.00 52.07  ? 306 PRO C N   1 
ATOM   6344  C CA  . PRO C 1 304 ? -10.412 29.568  42.831  1.00 46.63  ? 306 PRO C CA  1 
ATOM   6345  C C   . PRO C 1 304 ? -9.442  30.259  41.886  1.00 51.41  ? 306 PRO C C   1 
ATOM   6346  O O   . PRO C 1 304 ? -8.351  30.682  42.266  1.00 47.67  ? 306 PRO C O   1 
ATOM   6347  C CB  . PRO C 1 304 ? -11.572 30.492  43.215  1.00 46.87  ? 306 PRO C CB  1 
ATOM   6348  C CG  . PRO C 1 304 ? -11.750 30.313  44.699  1.00 50.27  ? 306 PRO C CG  1 
ATOM   6349  C CD  . PRO C 1 304 ? -10.385 29.995  45.231  1.00 57.04  ? 306 PRO C CD  1 
ATOM   6350  N N   . LYS C 1 305 ? -9.858  30.368  40.629  1.00 48.02  ? 307 LYS C N   1 
ATOM   6351  C CA  . LYS C 1 305 ? -9.020  30.985  39.612  1.00 38.30  ? 307 LYS C CA  1 
ATOM   6352  C C   . LYS C 1 305 ? -9.025  32.499  39.779  1.00 47.75  ? 307 LYS C C   1 
ATOM   6353  O O   . LYS C 1 305 ? -10.089 33.124  39.832  1.00 46.50  ? 307 LYS C O   1 
ATOM   6354  C CB  . LYS C 1 305 ? -9.503  30.592  38.217  1.00 43.44  ? 307 LYS C CB  1 
ATOM   6355  C CG  . LYS C 1 305 ? -9.363  29.102  37.918  1.00 42.40  ? 307 LYS C CG  1 
ATOM   6356  C CD  . LYS C 1 305 ? -7.986  28.581  38.329  1.00 42.13  ? 307 LYS C CD  1 
ATOM   6357  C CE  . LYS C 1 305 ? -7.967  27.058  38.440  1.00 47.95  ? 307 LYS C CE  1 
ATOM   6358  N NZ  . LYS C 1 305 ? -7.770  26.589  39.844  1.00 60.19  ? 307 LYS C NZ  1 
ATOM   6359  N N   . TYR C 1 306 ? -7.832  33.084  39.867  1.00 45.99  ? 308 TYR C N   1 
ATOM   6360  C CA  . TYR C 1 306 ? -7.712  34.521  40.072  1.00 46.02  ? 308 TYR C CA  1 
ATOM   6361  C C   . TYR C 1 306 ? -8.038  35.263  38.782  1.00 43.43  ? 308 TYR C C   1 
ATOM   6362  O O   . TYR C 1 306 ? -7.489  34.952  37.721  1.00 45.27  ? 308 TYR C O   1 
ATOM   6363  C CB  . TYR C 1 306 ? -6.302  34.873  40.553  1.00 41.14  ? 308 TYR C CB  1 
ATOM   6364  C CG  . TYR C 1 306 ? -6.137  36.333  40.909  1.00 52.27  ? 308 TYR C CG  1 
ATOM   6365  C CD1 . TYR C 1 306 ? -7.024  36.960  41.775  1.00 55.77  ? 308 TYR C CD1 1 
ATOM   6366  C CD2 . TYR C 1 306 ? -5.107  37.089  40.370  1.00 62.11  ? 308 TYR C CD2 1 
ATOM   6367  C CE1 . TYR C 1 306 ? -6.882  38.298  42.099  1.00 53.58  ? 308 TYR C CE1 1 
ATOM   6368  C CE2 . TYR C 1 306 ? -4.959  38.430  40.687  1.00 56.95  ? 308 TYR C CE2 1 
ATOM   6369  C CZ  . TYR C 1 306 ? -5.851  39.028  41.550  1.00 53.24  ? 308 TYR C CZ  1 
ATOM   6370  O OH  . TYR C 1 306 ? -5.711  40.359  41.869  1.00 57.78  ? 308 TYR C OH  1 
ATOM   6371  N N   . VAL C 1 307 ? -8.931  36.248  38.874  1.00 45.15  ? 309 VAL C N   1 
ATOM   6372  C CA  . VAL C 1 307 ? -9.374  37.017  37.717  1.00 47.04  ? 309 VAL C CA  1 
ATOM   6373  C C   . VAL C 1 307 ? -9.388  38.496  38.065  1.00 49.26  ? 309 VAL C C   1 
ATOM   6374  O O   . VAL C 1 307 ? -9.531  38.880  39.230  1.00 52.35  ? 309 VAL C O   1 
ATOM   6375  C CB  . VAL C 1 307 ? -10.774 36.585  37.228  1.00 40.15  ? 309 VAL C CB  1 
ATOM   6376  C CG1 . VAL C 1 307 ? -10.744 35.162  36.669  1.00 37.19  ? 309 VAL C CG1 1 
ATOM   6377  C CG2 . VAL C 1 307 ? -11.783 36.715  38.355  1.00 35.37  ? 309 VAL C CG2 1 
ATOM   6378  N N   . LYS C 1 308 ? -9.254  39.333  37.033  1.00 53.12  ? 310 LYS C N   1 
ATOM   6379  C CA  . LYS C 1 308 ? -9.338  40.785  37.189  1.00 50.84  ? 310 LYS C CA  1 
ATOM   6380  C C   . LYS C 1 308 ? -10.765 41.193  36.849  1.00 48.99  ? 310 LYS C C   1 
ATOM   6381  O O   . LYS C 1 308 ? -11.089 41.590  35.729  1.00 64.25  ? 310 LYS C O   1 
ATOM   6382  C CB  . LYS C 1 308 ? -8.312  41.495  36.313  1.00 57.31  ? 310 LYS C CB  1 
ATOM   6383  C CG  . LYS C 1 308 ? -8.404  43.016  36.353  1.00 55.70  ? 310 LYS C CG  1 
ATOM   6384  C CD  . LYS C 1 308 ? -7.576  43.660  35.244  1.00 64.75  ? 310 LYS C CD  1 
ATOM   6385  C CE  . LYS C 1 308 ? -8.019  45.095  34.975  1.00 79.40  ? 310 LYS C CE  1 
ATOM   6386  N NZ  . LYS C 1 308 ? -9.444  45.174  34.526  1.00 87.08  ? 310 LYS C NZ  1 
ATOM   6387  N N   . SER C 1 309 ? -11.638 41.072  37.843  1.00 46.92  ? 311 SER C N   1 
ATOM   6388  C CA  . SER C 1 309 ? -13.051 41.314  37.623  1.00 48.38  ? 311 SER C CA  1 
ATOM   6389  C C   . SER C 1 309 ? -13.690 41.735  38.936  1.00 61.23  ? 311 SER C C   1 
ATOM   6390  O O   . SER C 1 309 ? -13.282 41.294  40.015  1.00 56.27  ? 311 SER C O   1 
ATOM   6391  C CB  . SER C 1 309 ? -13.746 40.067  37.057  1.00 49.32  ? 311 SER C CB  1 
ATOM   6392  O OG  . SER C 1 309 ? -15.154 40.196  37.124  1.00 57.97  ? 311 SER C OG  1 
ATOM   6393  N N   . ASN C 1 310 ? -14.697 42.597  38.833  1.00 50.37  ? 312 ASN C N   1 
ATOM   6394  C CA  . ASN C 1 310 ? -15.425 43.051  40.008  1.00 56.86  ? 312 ASN C CA  1 
ATOM   6395  C C   . ASN C 1 310 ? -16.688 42.247  40.272  1.00 61.51  ? 312 ASN C C   1 
ATOM   6396  O O   . ASN C 1 310 ? -17.051 42.056  41.437  1.00 67.84  ? 312 ASN C O   1 
ATOM   6397  C CB  . ASN C 1 310 ? -15.776 44.536  39.868  1.00 76.55  ? 312 ASN C CB  1 
ATOM   6398  C CG  . ASN C 1 310 ? -14.559 45.439  40.014  1.00 72.63  ? 312 ASN C CG  1 
ATOM   6399  O OD1 . ASN C 1 310 ? -14.258 46.243  39.132  1.00 71.26  ? 312 ASN C OD1 1 
ATOM   6400  N ND2 . ASN C 1 310 ? -13.853 45.306  41.133  1.00 68.75  ? 312 ASN C ND2 1 
ATOM   6401  N N   . LYS C 1 311 ? -17.357 41.757  39.229  1.00 60.40  ? 313 LYS C N   1 
ATOM   6402  C CA  . LYS C 1 311 ? -18.569 40.969  39.401  1.00 62.91  ? 313 LYS C CA  1 
ATOM   6403  C C   . LYS C 1 311 ? -18.692 39.969  38.260  1.00 62.68  ? 313 LYS C C   1 
ATOM   6404  O O   . LYS C 1 311 ? -18.363 40.280  37.112  1.00 62.22  ? 313 LYS C O   1 
ATOM   6405  C CB  . LYS C 1 311 ? -19.821 41.860  39.462  1.00 48.36  ? 313 LYS C CB  1 
ATOM   6406  C CG  . LYS C 1 311 ? -19.915 42.914  38.361  1.00 50.33  ? 313 LYS C CG  1 
ATOM   6407  C CD  . LYS C 1 311 ? -21.066 43.893  38.614  1.00 52.53  ? 313 LYS C CD  1 
ATOM   6408  C CE  . LYS C 1 311 ? -22.325 43.480  37.864  1.00 73.87  ? 313 LYS C CE  1 
ATOM   6409  N NZ  . LYS C 1 311 ? -23.572 43.938  38.546  1.00 82.22  ? 313 LYS C NZ  1 
ATOM   6410  N N   . LEU C 1 312 ? -19.161 38.764  38.591  1.00 52.25  ? 314 LEU C N   1 
ATOM   6411  C CA  . LEU C 1 312 ? -19.519 37.735  37.614  1.00 52.97  ? 314 LEU C CA  1 
ATOM   6412  C C   . LEU C 1 312 ? -20.904 37.228  38.009  1.00 55.19  ? 314 LEU C C   1 
ATOM   6413  O O   . LEU C 1 312 ? -21.026 36.223  38.716  1.00 47.37  ? 314 LEU C O   1 
ATOM   6414  C CB  . LEU C 1 312 ? -18.494 36.614  37.585  1.00 48.26  ? 314 LEU C CB  1 
ATOM   6415  C CG  . LEU C 1 312 ? -17.121 36.978  37.025  1.00 41.49  ? 314 LEU C CG  1 
ATOM   6416  C CD1 . LEU C 1 312 ? -16.161 35.837  37.282  1.00 45.66  ? 314 LEU C CD1 1 
ATOM   6417  C CD2 . LEU C 1 312 ? -17.213 37.289  35.538  1.00 40.74  ? 314 LEU C CD2 1 
ATOM   6418  N N   . VAL C 1 313 ? -21.944 37.918  37.547  1.00 45.21  ? 315 VAL C N   1 
ATOM   6419  C CA  . VAL C 1 313 ? -23.308 37.681  38.005  1.00 49.87  ? 315 VAL C CA  1 
ATOM   6420  C C   . VAL C 1 313 ? -24.052 36.874  36.950  1.00 43.03  ? 315 VAL C C   1 
ATOM   6421  O O   . VAL C 1 313 ? -24.209 37.322  35.807  1.00 39.84  ? 315 VAL C O   1 
ATOM   6422  C CB  . VAL C 1 313 ? -24.035 39.000  38.305  1.00 48.61  ? 315 VAL C CB  1 
ATOM   6423  C CG1 . VAL C 1 313 ? -25.445 38.721  38.789  1.00 41.89  ? 315 VAL C CG1 1 
ATOM   6424  C CG2 . VAL C 1 313 ? -23.266 39.804  39.337  1.00 43.87  ? 315 VAL C CG2 1 
ATOM   6425  N N   . LEU C 1 314 ? -24.513 35.689  37.336  1.00 38.47  ? 316 LEU C N   1 
ATOM   6426  C CA  . LEU C 1 314 ? -25.265 34.801  36.460  1.00 40.67  ? 316 LEU C CA  1 
ATOM   6427  C C   . LEU C 1 314 ? -26.752 34.976  36.722  1.00 45.89  ? 316 LEU C C   1 
ATOM   6428  O O   . LEU C 1 314 ? -27.204 34.858  37.867  1.00 47.55  ? 316 LEU C O   1 
ATOM   6429  C CB  . LEU C 1 314 ? -24.874 33.342  36.691  1.00 36.41  ? 316 LEU C CB  1 
ATOM   6430  C CG  . LEU C 1 314 ? -23.600 32.832  36.033  1.00 38.90  ? 316 LEU C CG  1 
ATOM   6431  C CD1 . LEU C 1 314 ? -23.334 31.409  36.488  1.00 41.18  ? 316 LEU C CD1 1 
ATOM   6432  C CD2 . LEU C 1 314 ? -23.734 32.908  34.520  1.00 38.00  ? 316 LEU C CD2 1 
ATOM   6433  N N   . ALA C 1 315 ? -27.510 35.259  35.670  1.00 42.66  ? 317 ALA C N   1 
ATOM   6434  C CA  . ALA C 1 315 ? -28.950 35.374  35.830  1.00 40.01  ? 317 ALA C CA  1 
ATOM   6435  C C   . ALA C 1 315 ? -29.548 33.996  36.085  1.00 47.62  ? 317 ALA C C   1 
ATOM   6436  O O   . ALA C 1 315 ? -29.193 33.019  35.421  1.00 41.39  ? 317 ALA C O   1 
ATOM   6437  C CB  . ALA C 1 315 ? -29.577 36.013  34.593  1.00 45.62  ? 317 ALA C CB  1 
ATOM   6438  N N   . THR C 1 316 ? -30.436 33.914  37.069  1.00 47.27  ? 318 THR C N   1 
ATOM   6439  C CA  . THR C 1 316 ? -31.176 32.690  37.330  1.00 43.83  ? 318 THR C CA  1 
ATOM   6440  C C   . THR C 1 316 ? -32.676 32.837  37.127  1.00 53.21  ? 318 THR C C   1 
ATOM   6441  O O   . THR C 1 316 ? -33.317 31.888  36.671  1.00 50.97  ? 318 THR C O   1 
ATOM   6442  C CB  . THR C 1 316 ? -30.903 32.186  38.757  1.00 54.00  ? 318 THR C CB  1 
ATOM   6443  O OG1 . THR C 1 316 ? -31.073 33.260  39.689  1.00 63.84  ? 318 THR C OG1 1 
ATOM   6444  C CG2 . THR C 1 316 ? -29.480 31.651  38.869  1.00 48.66  ? 318 THR C CG2 1 
ATOM   6445  N N   . GLY C 1 317 ? -33.247 33.999  37.423  1.00 44.91  ? 319 GLY C N   1 
ATOM   6446  C CA  . GLY C 1 317 ? -34.655 34.253  37.201  1.00 39.11  ? 319 GLY C CA  1 
ATOM   6447  C C   . GLY C 1 317 ? -34.934 34.838  35.832  1.00 42.41  ? 319 GLY C C   1 
ATOM   6448  O O   . GLY C 1 317 ? -34.158 34.683  34.886  1.00 50.35  ? 319 GLY C O   1 
ATOM   6449  N N   . LEU C 1 318 ? -36.064 35.532  35.737  1.00 45.72  ? 320 LEU C N   1 
ATOM   6450  C CA  . LEU C 1 318 ? -36.586 36.060  34.485  1.00 44.12  ? 320 LEU C CA  1 
ATOM   6451  C C   . LEU C 1 318 ? -36.321 37.559  34.383  1.00 47.93  ? 320 LEU C C   1 
ATOM   6452  O O   . LEU C 1 318 ? -36.076 38.241  35.380  1.00 44.77  ? 320 LEU C O   1 
ATOM   6453  C CB  . LEU C 1 318 ? -38.094 35.792  34.376  1.00 42.78  ? 320 LEU C CB  1 
ATOM   6454  C CG  . LEU C 1 318 ? -38.605 34.345  34.344  1.00 49.87  ? 320 LEU C CG  1 
ATOM   6455  C CD1 . LEU C 1 318 ? -38.713 33.738  35.738  1.00 54.89  ? 320 LEU C CD1 1 
ATOM   6456  C CD2 . LEU C 1 318 ? -39.951 34.274  33.646  1.00 46.15  ? 320 LEU C CD2 1 
ATOM   6457  N N   . ARG C 1 319 ? -36.376 38.068  33.154  1.00 35.62  ? 321 ARG C N   1 
ATOM   6458  C CA  . ARG C 1 319 ? -36.318 39.508  32.940  1.00 42.96  ? 321 ARG C CA  1 
ATOM   6459  C C   . ARG C 1 319 ? -37.497 40.179  33.637  1.00 46.05  ? 321 ARG C C   1 
ATOM   6460  O O   . ARG C 1 319 ? -38.656 39.851  33.366  1.00 59.95  ? 321 ARG C O   1 
ATOM   6461  C CB  . ARG C 1 319 ? -36.326 39.815  31.444  1.00 40.67  ? 321 ARG C CB  1 
ATOM   6462  C CG  . ARG C 1 319 ? -36.596 41.276  31.105  1.00 57.11  ? 321 ARG C CG  1 
ATOM   6463  C CD  . ARG C 1 319 ? -36.136 41.617  29.689  1.00 59.10  ? 321 ARG C CD  1 
ATOM   6464  N NE  . ARG C 1 319 ? -35.757 40.433  28.927  1.00 56.42  ? 321 ARG C NE  1 
ATOM   6465  C CZ  . ARG C 1 319 ? -34.790 40.401  28.018  1.00 60.86  ? 321 ARG C CZ  1 
ATOM   6466  N NH1 . ARG C 1 319 ? -34.071 41.476  27.737  1.00 46.94  ? 321 ARG C NH1 1 
ATOM   6467  N NH2 . ARG C 1 319 ? -34.543 39.264  27.370  1.00 65.66  ? 321 ARG C NH2 1 
ATOM   6468  N N   . ASN C 1 320 ? -37.200 41.112  34.538  1.00 40.24  ? 322 ASN C N   1 
ATOM   6469  C CA  . ASN C 1 320 ? -38.206 41.695  35.414  1.00 52.67  ? 322 ASN C CA  1 
ATOM   6470  C C   . ASN C 1 320 ? -38.880 42.909  34.776  1.00 56.26  ? 322 ASN C C   1 
ATOM   6471  O O   . ASN C 1 320 ? -38.340 43.553  33.874  1.00 66.45  ? 322 ASN C O   1 
ATOM   6472  C CB  . ASN C 1 320 ? -37.585 42.091  36.753  1.00 51.74  ? 322 ASN C CB  1 
ATOM   6473  C CG  . ASN C 1 320 ? -38.622 42.257  37.848  1.00 50.00  ? 322 ASN C CG  1 
ATOM   6474  O OD1 . ASN C 1 320 ? -39.798 41.944  37.659  1.00 57.49  ? 322 ASN C OD1 1 
ATOM   6475  N ND2 . ASN C 1 320 ? -38.189 42.750  39.001  1.00 52.46  ? 322 ASN C ND2 1 
ATOM   6476  N N   . SER C 1 321 ? -40.066 43.221  35.278  1.00 66.16  ? 323 SER C N   1 
ATOM   6477  C CA  . SER C 1 321 ? -40.955 44.258  34.783  1.00 80.74  ? 323 SER C CA  1 
ATOM   6478  C C   . SER C 1 321 ? -40.938 45.490  35.688  1.00 81.37  ? 323 SER C C   1 
ATOM   6479  O O   . SER C 1 321 ? -40.459 45.434  36.826  1.00 69.86  ? 323 SER C O   1 
ATOM   6480  C CB  . SER C 1 321 ? -42.379 43.692  34.678  1.00 68.98  ? 323 SER C CB  1 
ATOM   6481  O OG  . SER C 1 321 ? -42.402 42.574  33.814  1.00 60.21  ? 323 SER C OG  1 
ATOM   6482  N N   . PRO C 1 322 ? -41.460 46.647  35.202  1.00 94.74  ? 324 PRO C N   1 
ATOM   6483  C CA  . PRO C 1 322 ? -41.475 47.853  36.044  1.00 94.85  ? 324 PRO C CA  1 
ATOM   6484  C C   . PRO C 1 322 ? -42.463 47.784  37.202  1.00 100.83 ? 324 PRO C C   1 
ATOM   6485  O O   . PRO C 1 322 ? -43.144 46.772  37.399  1.00 91.49  ? 324 PRO C O   1 
ATOM   6486  C CB  . PRO C 1 322 ? -41.867 48.959  35.056  1.00 99.15  ? 324 PRO C CB  1 
ATOM   6487  C CG  . PRO C 1 322 ? -42.667 48.245  34.011  1.00 86.84  ? 324 PRO C CG  1 
ATOM   6488  C CD  . PRO C 1 322 ? -41.943 46.938  33.841  1.00 94.36  ? 324 PRO C CD  1 
ATOM   6489  N N   . LEU C 1 323 ? -42.545 48.866  37.979  1.00 105.85 ? 325 LEU C N   1 
ATOM   6490  C CA  . LEU C 1 323 ? -43.584 48.996  38.993  1.00 97.72  ? 325 LEU C CA  1 
ATOM   6491  C C   . LEU C 1 323 ? -44.879 49.457  38.334  1.00 99.16  ? 325 LEU C C   1 
ATOM   6492  O O   . LEU C 1 323 ? -44.874 50.370  37.501  1.00 98.92  ? 325 LEU C O   1 
ATOM   6493  C CB  . LEU C 1 323 ? -43.156 49.975  40.088  1.00 104.15 ? 325 LEU C CB  1 
ATOM   6494  C CG  . LEU C 1 323 ? -42.747 51.400  39.699  1.00 110.81 ? 325 LEU C CG  1 
ATOM   6495  C CD1 . LEU C 1 323 ? -43.868 52.399  39.988  1.00 106.81 ? 325 LEU C CD1 1 
ATOM   6496  C CD2 . LEU C 1 323 ? -41.466 51.802  40.415  1.00 95.48  ? 325 LEU C CD2 1 
ATOM   6497  N N   . ARG C 1 324 ? -45.984 48.819  38.700  1.00 100.08 ? 326 ARG C N   1 
ATOM   6498  C CA  . ARG C 1 324 ? -47.270 49.105  38.078  1.00 82.63  ? 326 ARG C CA  1 
ATOM   6499  C C   . ARG C 1 324 ? -48.327 49.465  39.120  1.00 91.20  ? 326 ARG C C   1 
ATOM   6500  O O   . ARG C 1 324 ? -48.005 49.845  40.246  1.00 90.53  ? 326 ARG C O   1 
ATOM   6501  C CB  . ARG C 1 324 ? -47.733 47.906  37.247  1.00 90.14  ? 326 ARG C CB  1 
ATOM   6502  C CG  . ARG C 1 324 ? -46.810 47.561  36.088  1.00 89.87  ? 326 ARG C CG  1 
ATOM   6503  C CD  . ARG C 1 324 ? -47.343 46.386  35.280  1.00 85.51  ? 326 ARG C CD  1 
ATOM   6504  N NE  . ARG C 1 324 ? -48.461 46.770  34.426  1.00 103.51 ? 326 ARG C NE  1 
ATOM   6505  C CZ  . ARG C 1 324 ? -49.575 46.064  34.285  1.00 108.13 ? 326 ARG C CZ  1 
ATOM   6506  N NH1 . ARG C 1 324 ? -49.763 44.930  34.940  1.00 98.00  ? 326 ARG C NH1 1 
ATOM   6507  N NH2 . ARG C 1 324 ? -50.525 46.509  33.467  1.00 110.96 ? 326 ARG C NH2 1 
ATOM   6508  N N   . GLY D 2 1   ? -32.703 34.932  19.072  1.00 48.34  ? 1   GLY D N   1 
ATOM   6509  C CA  . GLY D 2 1   ? -32.836 33.870  20.053  1.00 48.21  ? 1   GLY D CA  1 
ATOM   6510  C C   . GLY D 2 1   ? -34.148 33.962  20.799  1.00 66.09  ? 1   GLY D C   1 
ATOM   6511  O O   . GLY D 2 1   ? -34.628 32.974  21.355  1.00 76.34  ? 1   GLY D O   1 
ATOM   6512  N N   . LEU D 2 2   ? -34.737 35.156  20.797  1.00 62.80  ? 2   LEU D N   1 
ATOM   6513  C CA  . LEU D 2 2   ? -35.998 35.369  21.490  1.00 47.07  ? 2   LEU D CA  1 
ATOM   6514  C C   . LEU D 2 2   ? -37.087 34.489  20.891  1.00 60.04  ? 2   LEU D C   1 
ATOM   6515  O O   . LEU D 2 2   ? -37.088 34.190  19.691  1.00 44.25  ? 2   LEU D O   1 
ATOM   6516  C CB  . LEU D 2 2   ? -36.410 36.840  21.411  1.00 46.29  ? 2   LEU D CB  1 
ATOM   6517  C CG  . LEU D 2 2   ? -36.803 37.524  22.722  1.00 55.67  ? 2   LEU D CG  1 
ATOM   6518  C CD1 . LEU D 2 2   ? -35.742 37.285  23.791  1.00 52.78  ? 2   LEU D CD1 1 
ATOM   6519  C CD2 . LEU D 2 2   ? -37.025 39.018  22.506  1.00 42.19  ? 2   LEU D CD2 1 
ATOM   6520  N N   . PHE D 2 3   ? -38.000 34.048  21.746  1.00 50.85  ? 3   PHE D N   1 
ATOM   6521  C CA  . PHE D 2 3   ? -39.149 33.272  21.323  1.00 52.25  ? 3   PHE D CA  1 
ATOM   6522  C C   . PHE D 2 3   ? -40.420 34.101  21.291  1.00 54.52  ? 3   PHE D C   1 
ATOM   6523  O O   . PHE D 2 3   ? -41.494 33.560  21.004  1.00 54.47  ? 3   PHE D O   1 
ATOM   6524  C CB  . PHE D 2 3   ? -39.306 32.051  22.232  1.00 45.13  ? 3   PHE D CB  1 
ATOM   6525  C CG  . PHE D 2 3   ? -38.218 31.037  22.044  1.00 48.75  ? 3   PHE D CG  1 
ATOM   6526  C CD1 . PHE D 2 3   ? -37.003 31.168  22.706  1.00 46.21  ? 3   PHE D CD1 1 
ATOM   6527  C CD2 . PHE D 2 3   ? -38.390 29.975  21.172  1.00 37.31  ? 3   PHE D CD2 1 
ATOM   6528  C CE1 . PHE D 2 3   ? -35.991 30.241  22.517  1.00 44.19  ? 3   PHE D CE1 1 
ATOM   6529  C CE2 . PHE D 2 3   ? -37.389 29.044  20.980  1.00 42.01  ? 3   PHE D CE2 1 
ATOM   6530  C CZ  . PHE D 2 3   ? -36.186 29.177  21.653  1.00 55.47  ? 3   PHE D CZ  1 
ATOM   6531  N N   . GLY D 2 4   ? -40.316 35.400  21.570  1.00 53.54  ? 4   GLY D N   1 
ATOM   6532  C CA  . GLY D 2 4   ? -41.383 36.346  21.328  1.00 53.05  ? 4   GLY D CA  1 
ATOM   6533  C C   . GLY D 2 4   ? -42.388 36.520  22.445  1.00 53.88  ? 4   GLY D C   1 
ATOM   6534  O O   . GLY D 2 4   ? -43.268 37.383  22.326  1.00 53.53  ? 4   GLY D O   1 
ATOM   6535  N N   . ALA D 2 5   ? -42.285 35.749  23.527  1.00 52.74  ? 5   ALA D N   1 
ATOM   6536  C CA  . ALA D 2 5   ? -43.299 35.797  24.579  1.00 58.23  ? 5   ALA D CA  1 
ATOM   6537  C C   . ALA D 2 5   ? -42.936 36.800  25.675  1.00 51.44  ? 5   ALA D C   1 
ATOM   6538  O O   . ALA D 2 5   ? -43.671 37.765  25.906  1.00 50.23  ? 5   ALA D O   1 
ATOM   6539  C CB  . ALA D 2 5   ? -43.513 34.395  25.169  1.00 47.04  ? 5   ALA D CB  1 
ATOM   6540  N N   . ILE D 2 6   ? -41.805 36.587  26.351  1.00 45.42  ? 6   ILE D N   1 
ATOM   6541  C CA  . ILE D 2 6   ? -41.392 37.488  27.419  1.00 53.19  ? 6   ILE D CA  1 
ATOM   6542  C C   . ILE D 2 6   ? -40.969 38.817  26.811  1.00 53.60  ? 6   ILE D C   1 
ATOM   6543  O O   . ILE D 2 6   ? -40.119 38.861  25.912  1.00 62.51  ? 6   ILE D O   1 
ATOM   6544  C CB  . ILE D 2 6   ? -40.257 36.861  28.243  1.00 54.94  ? 6   ILE D CB  1 
ATOM   6545  C CG1 . ILE D 2 6   ? -40.800 35.711  29.093  1.00 53.64  ? 6   ILE D CG1 1 
ATOM   6546  C CG2 . ILE D 2 6   ? -39.581 37.914  29.122  1.00 50.34  ? 6   ILE D CG2 1 
ATOM   6547  C CD1 . ILE D 2 6   ? -39.801 35.149  30.073  1.00 35.27  ? 6   ILE D CD1 1 
ATOM   6548  N N   . ALA D 2 7   ? -41.570 39.906  27.297  1.00 56.96  ? 7   ALA D N   1 
ATOM   6549  C CA  . ALA D 2 7   ? -41.355 41.246  26.739  1.00 62.04  ? 7   ALA D CA  1 
ATOM   6550  C C   . ALA D 2 7   ? -41.656 41.259  25.245  1.00 57.45  ? 7   ALA D C   1 
ATOM   6551  O O   . ALA D 2 7   ? -41.003 41.947  24.457  1.00 67.01  ? 7   ALA D O   1 
ATOM   6552  C CB  . ALA D 2 7   ? -39.936 41.747  27.021  1.00 53.56  ? 7   ALA D CB  1 
ATOM   6553  N N   . GLY D 2 8   ? -42.653 40.470  24.855  1.00 61.57  ? 8   GLY D N   1 
ATOM   6554  C CA  . GLY D 2 8   ? -43.077 40.346  23.476  1.00 45.19  ? 8   GLY D CA  1 
ATOM   6555  C C   . GLY D 2 8   ? -44.582 40.453  23.386  1.00 59.48  ? 8   GLY D C   1 
ATOM   6556  O O   . GLY D 2 8   ? -45.152 41.469  23.796  1.00 59.54  ? 8   GLY D O   1 
ATOM   6557  N N   . PHE D 2 9   ? -45.248 39.420  22.861  1.00 63.14  ? 9   PHE D N   1 
ATOM   6558  C CA  . PHE D 2 9   ? -46.704 39.453  22.856  1.00 49.76  ? 9   PHE D CA  1 
ATOM   6559  C C   . PHE D 2 9   ? -47.278 39.359  24.266  1.00 55.73  ? 9   PHE D C   1 
ATOM   6560  O O   . PHE D 2 9   ? -48.451 39.688  24.462  1.00 58.29  ? 9   PHE D O   1 
ATOM   6561  C CB  . PHE D 2 9   ? -47.272 38.359  21.934  1.00 54.12  ? 9   PHE D CB  1 
ATOM   6562  C CG  . PHE D 2 9   ? -47.223 36.967  22.502  1.00 57.91  ? 9   PHE D CG  1 
ATOM   6563  C CD1 . PHE D 2 9   ? -48.252 36.483  23.303  1.00 56.11  ? 9   PHE D CD1 1 
ATOM   6564  C CD2 . PHE D 2 9   ? -46.172 36.122  22.191  1.00 52.39  ? 9   PHE D CD2 1 
ATOM   6565  C CE1 . PHE D 2 9   ? -48.209 35.198  23.812  1.00 63.33  ? 9   PHE D CE1 1 
ATOM   6566  C CE2 . PHE D 2 9   ? -46.125 34.833  22.694  1.00 53.84  ? 9   PHE D CE2 1 
ATOM   6567  C CZ  . PHE D 2 9   ? -47.143 34.371  23.505  1.00 51.35  ? 9   PHE D CZ  1 
ATOM   6568  N N   . ILE D 2 10  ? -46.489 38.932  25.249  1.00 51.36  ? 10  ILE D N   1 
ATOM   6569  C CA  . ILE D 2 10  ? -46.841 39.090  26.657  1.00 53.20  ? 10  ILE D CA  1 
ATOM   6570  C C   . ILE D 2 10  ? -46.022 40.267  27.172  1.00 53.16  ? 10  ILE D C   1 
ATOM   6571  O O   . ILE D 2 10  ? -44.791 40.192  27.253  1.00 54.06  ? 10  ILE D O   1 
ATOM   6572  C CB  . ILE D 2 10  ? -46.573 37.819  27.474  1.00 53.43  ? 10  ILE D CB  1 
ATOM   6573  C CG1 . ILE D 2 10  ? -47.461 36.671  26.999  1.00 54.86  ? 10  ILE D CG1 1 
ATOM   6574  C CG2 . ILE D 2 10  ? -46.846 38.085  28.952  1.00 45.26  ? 10  ILE D CG2 1 
ATOM   6575  C CD1 . ILE D 2 10  ? -47.476 35.471  27.929  1.00 56.16  ? 10  ILE D CD1 1 
ATOM   6576  N N   . GLU D 2 11  ? -46.697 41.359  27.513  1.00 64.97  ? 11  GLU D N   1 
ATOM   6577  C CA  . GLU D 2 11  ? -46.040 42.626  27.829  1.00 70.48  ? 11  GLU D CA  1 
ATOM   6578  C C   . GLU D 2 11  ? -45.945 42.766  29.346  1.00 69.66  ? 11  GLU D C   1 
ATOM   6579  O O   . GLU D 2 11  ? -46.801 43.378  29.987  1.00 91.26  ? 11  GLU D O   1 
ATOM   6580  C CB  . GLU D 2 11  ? -46.796 43.787  27.190  1.00 79.97  ? 11  GLU D CB  1 
ATOM   6581  C CG  . GLU D 2 11  ? -46.046 45.105  27.201  1.00 110.01 ? 11  GLU D CG  1 
ATOM   6582  C CD  . GLU D 2 11  ? -46.969 46.304  27.080  1.00 111.06 ? 11  GLU D CD  1 
ATOM   6583  O OE1 . GLU D 2 11  ? -48.206 46.124  27.150  1.00 92.90  ? 11  GLU D OE1 1 
ATOM   6584  O OE2 . GLU D 2 11  ? -46.453 47.430  26.913  1.00 102.66 ? 11  GLU D OE2 1 
ATOM   6585  N N   . GLY D 2 12  ? -44.902 42.197  29.920  1.00 60.34  ? 12  GLY D N   1 
ATOM   6586  C CA  . GLY D 2 12  ? -44.666 42.344  31.343  1.00 53.88  ? 12  GLY D CA  1 
ATOM   6587  C C   . GLY D 2 12  ? -45.159 41.155  32.147  1.00 56.80  ? 12  GLY D C   1 
ATOM   6588  O O   . GLY D 2 12  ? -46.120 40.467  31.777  1.00 50.81  ? 12  GLY D O   1 
ATOM   6589  N N   . GLY D 2 13  ? -44.493 40.914  33.279  1.00 49.35  ? 13  GLY D N   1 
ATOM   6590  C CA  . GLY D 2 13  ? -44.863 39.844  34.180  1.00 51.39  ? 13  GLY D CA  1 
ATOM   6591  C C   . GLY D 2 13  ? -45.882 40.288  35.218  1.00 55.84  ? 13  GLY D C   1 
ATOM   6592  O O   . GLY D 2 13  ? -46.320 41.436  35.257  1.00 50.35  ? 13  GLY D O   1 
ATOM   6593  N N   . TRP D 2 14  ? -46.251 39.345  36.082  1.00 56.98  ? 14  TRP D N   1 
ATOM   6594  C CA  . TRP D 2 14  ? -47.276 39.554  37.097  1.00 48.36  ? 14  TRP D CA  1 
ATOM   6595  C C   . TRP D 2 14  ? -46.648 39.577  38.482  1.00 52.43  ? 14  TRP D C   1 
ATOM   6596  O O   . TRP D 2 14  ? -45.913 38.654  38.847  1.00 56.08  ? 14  TRP D O   1 
ATOM   6597  C CB  . TRP D 2 14  ? -48.332 38.450  37.048  1.00 53.87  ? 14  TRP D CB  1 
ATOM   6598  C CG  . TRP D 2 14  ? -49.186 38.454  35.832  1.00 52.17  ? 14  TRP D CG  1 
ATOM   6599  C CD1 . TRP D 2 14  ? -49.643 39.543  35.147  1.00 56.66  ? 14  TRP D CD1 1 
ATOM   6600  C CD2 . TRP D 2 14  ? -49.706 37.306  35.157  1.00 49.81  ? 14  TRP D CD2 1 
ATOM   6601  N NE1 . TRP D 2 14  ? -50.419 39.141  34.084  1.00 52.64  ? 14  TRP D NE1 1 
ATOM   6602  C CE2 . TRP D 2 14  ? -50.470 37.771  34.069  1.00 49.77  ? 14  TRP D CE2 1 
ATOM   6603  C CE3 . TRP D 2 14  ? -49.598 35.928  35.368  1.00 48.22  ? 14  TRP D CE3 1 
ATOM   6604  C CZ2 . TRP D 2 14  ? -51.120 36.907  33.192  1.00 51.83  ? 14  TRP D CZ2 1 
ATOM   6605  C CZ3 . TRP D 2 14  ? -50.248 35.072  34.502  1.00 52.12  ? 14  TRP D CZ3 1 
ATOM   6606  C CH2 . TRP D 2 14  ? -50.999 35.565  33.426  1.00 51.51  ? 14  TRP D CH2 1 
ATOM   6607  N N   . GLN D 2 15  ? -46.950 40.621  39.260  1.00 59.13  ? 15  GLN D N   1 
ATOM   6608  C CA  . GLN D 2 15  ? -46.567 40.604  40.668  1.00 56.65  ? 15  GLN D CA  1 
ATOM   6609  C C   . GLN D 2 15  ? -47.426 39.624  41.457  1.00 61.46  ? 15  GLN D C   1 
ATOM   6610  O O   . GLN D 2 15  ? -46.986 39.106  42.490  1.00 54.71  ? 15  GLN D O   1 
ATOM   6611  C CB  . GLN D 2 15  ? -46.673 42.005  41.272  1.00 50.19  ? 15  GLN D CB  1 
ATOM   6612  C CG  . GLN D 2 15  ? -45.777 43.042  40.623  1.00 51.34  ? 15  GLN D CG  1 
ATOM   6613  C CD  . GLN D 2 15  ? -44.348 42.989  41.131  1.00 64.43  ? 15  GLN D CD  1 
ATOM   6614  O OE1 . GLN D 2 15  ? -44.094 42.591  42.270  1.00 63.64  ? 15  GLN D OE1 1 
ATOM   6615  N NE2 . GLN D 2 15  ? -43.406 43.397  40.287  1.00 55.56  ? 15  GLN D NE2 1 
ATOM   6616  N N   . GLY D 2 16  ? -48.641 39.343  40.975  1.00 55.04  ? 16  GLY D N   1 
ATOM   6617  C CA  . GLY D 2 16  ? -49.552 38.454  41.677  1.00 51.00  ? 16  GLY D CA  1 
ATOM   6618  C C   . GLY D 2 16  ? -49.183 36.988  41.589  1.00 69.09  ? 16  GLY D C   1 
ATOM   6619  O O   . GLY D 2 16  ? -49.690 36.185  42.381  1.00 78.66  ? 16  GLY D O   1 
ATOM   6620  N N   . MET D 2 17  ? -48.323 36.617  40.642  1.00 61.52  ? 17  MET D N   1 
ATOM   6621  C CA  . MET D 2 17  ? -47.836 35.242  40.512  1.00 65.47  ? 17  MET D CA  1 
ATOM   6622  C C   . MET D 2 17  ? -46.659 35.058  41.462  1.00 68.39  ? 17  MET D C   1 
ATOM   6623  O O   . MET D 2 17  ? -45.507 35.334  41.124  1.00 68.62  ? 17  MET D O   1 
ATOM   6624  C CB  . MET D 2 17  ? -47.445 34.949  39.067  1.00 65.55  ? 17  MET D CB  1 
ATOM   6625  C CG  . MET D 2 17  ? -46.880 33.556  38.827  1.00 61.73  ? 17  MET D CG  1 
ATOM   6626  S SD  . MET D 2 17  ? -48.151 32.328  38.507  1.00 71.78  ? 17  MET D SD  1 
ATOM   6627  C CE  . MET D 2 17  ? -49.309 33.274  37.522  1.00 58.13  ? 17  MET D CE  1 
ATOM   6628  N N   . VAL D 2 18  ? -46.946 34.569  42.668  1.00 69.15  ? 18  VAL D N   1 
ATOM   6629  C CA  . VAL D 2 18  ? -45.958 34.497  43.739  1.00 61.32  ? 18  VAL D CA  1 
ATOM   6630  C C   . VAL D 2 18  ? -45.536 33.073  44.056  1.00 67.68  ? 18  VAL D C   1 
ATOM   6631  O O   . VAL D 2 18  ? -44.627 32.882  44.876  1.00 77.97  ? 18  VAL D O   1 
ATOM   6632  C CB  . VAL D 2 18  ? -46.471 35.195  45.011  1.00 61.04  ? 18  VAL D CB  1 
ATOM   6633  C CG1 . VAL D 2 18  ? -46.554 36.701  44.793  1.00 56.80  ? 18  VAL D CG1 1 
ATOM   6634  C CG2 . VAL D 2 18  ? -47.823 34.633  45.410  1.00 66.02  ? 18  VAL D CG2 1 
ATOM   6635  N N   . ASP D 2 19  ? -46.155 32.065  43.439  1.00 59.38  ? 19  ASP D N   1 
ATOM   6636  C CA  . ASP D 2 19  ? -45.858 30.671  43.753  1.00 67.62  ? 19  ASP D CA  1 
ATOM   6637  C C   . ASP D 2 19  ? -45.183 29.924  42.606  1.00 62.93  ? 19  ASP D C   1 
ATOM   6638  O O   . ASP D 2 19  ? -45.092 28.690  42.650  1.00 62.79  ? 19  ASP D O   1 
ATOM   6639  C CB  . ASP D 2 19  ? -47.133 29.934  44.178  1.00 71.66  ? 19  ASP D CB  1 
ATOM   6640  C CG  . ASP D 2 19  ? -48.354 30.347  43.368  1.00 87.33  ? 19  ASP D CG  1 
ATOM   6641  O OD1 . ASP D 2 19  ? -49.370 29.618  43.414  1.00 87.54  ? 19  ASP D OD1 1 
ATOM   6642  O OD2 . ASP D 2 19  ? -48.308 31.400  42.697  1.00 88.62  ? 19  ASP D OD2 1 
ATOM   6643  N N   . GLY D 2 20  ? -44.704 30.628  41.591  1.00 50.84  ? 20  GLY D N   1 
ATOM   6644  C CA  . GLY D 2 20  ? -44.045 29.961  40.483  1.00 49.42  ? 20  GLY D CA  1 
ATOM   6645  C C   . GLY D 2 20  ? -43.526 30.973  39.487  1.00 52.37  ? 20  GLY D C   1 
ATOM   6646  O O   . GLY D 2 20  ? -43.802 32.173  39.579  1.00 61.03  ? 20  GLY D O   1 
ATOM   6647  N N   . TRP D 2 21  ? -42.762 30.460  38.523  1.00 54.19  ? 21  TRP D N   1 
ATOM   6648  C CA  . TRP D 2 21  ? -42.143 31.306  37.510  1.00 52.89  ? 21  TRP D CA  1 
ATOM   6649  C C   . TRP D 2 21  ? -43.096 31.576  36.352  1.00 48.89  ? 21  TRP D C   1 
ATOM   6650  O O   . TRP D 2 21  ? -43.225 32.715  35.890  1.00 52.47  ? 21  TRP D O   1 
ATOM   6651  C CB  . TRP D 2 21  ? -40.858 30.649  37.004  1.00 51.64  ? 21  TRP D CB  1 
ATOM   6652  C CG  . TRP D 2 21  ? -39.639 31.010  37.785  1.00 53.20  ? 21  TRP D CG  1 
ATOM   6653  C CD1 . TRP D 2 21  ? -39.526 31.986  38.733  1.00 67.20  ? 21  TRP D CD1 1 
ATOM   6654  C CD2 . TRP D 2 21  ? -38.345 30.407  37.674  1.00 49.33  ? 21  TRP D CD2 1 
ATOM   6655  N NE1 . TRP D 2 21  ? -38.240 32.024  39.222  1.00 75.23  ? 21  TRP D NE1 1 
ATOM   6656  C CE2 . TRP D 2 21  ? -37.497 31.064  38.588  1.00 50.35  ? 21  TRP D CE2 1 
ATOM   6657  C CE3 . TRP D 2 21  ? -37.822 29.376  36.889  1.00 46.89  ? 21  TRP D CE3 1 
ATOM   6658  C CZ2 . TRP D 2 21  ? -36.156 30.722  38.740  1.00 49.22  ? 21  TRP D CZ2 1 
ATOM   6659  C CZ3 . TRP D 2 21  ? -36.490 29.037  37.043  1.00 58.17  ? 21  TRP D CZ3 1 
ATOM   6660  C CH2 . TRP D 2 21  ? -35.673 29.708  37.960  1.00 55.07  ? 21  TRP D CH2 1 
ATOM   6661  N N   . TYR D 2 22  ? -43.768 30.536  35.871  1.00 46.65  ? 22  TYR D N   1 
ATOM   6662  C CA  . TYR D 2 22  ? -44.744 30.646  34.800  1.00 36.93  ? 22  TYR D CA  1 
ATOM   6663  C C   . TYR D 2 22  ? -46.098 30.192  35.320  1.00 44.74  ? 22  TYR D C   1 
ATOM   6664  O O   . TYR D 2 22  ? -46.183 29.312  36.180  1.00 46.19  ? 22  TYR D O   1 
ATOM   6665  C CB  . TYR D 2 22  ? -44.329 29.810  33.584  1.00 36.63  ? 22  TYR D CB  1 
ATOM   6666  C CG  . TYR D 2 22  ? -42.831 29.701  33.395  1.00 38.71  ? 22  TYR D CG  1 
ATOM   6667  C CD1 . TYR D 2 22  ? -42.062 30.829  33.127  1.00 42.83  ? 22  TYR D CD1 1 
ATOM   6668  C CD2 . TYR D 2 22  ? -42.183 28.474  33.486  1.00 45.20  ? 22  TYR D CD2 1 
ATOM   6669  C CE1 . TYR D 2 22  ? -40.694 30.739  32.948  1.00 40.93  ? 22  TYR D CE1 1 
ATOM   6670  C CE2 . TYR D 2 22  ? -40.808 28.374  33.310  1.00 40.11  ? 22  TYR D CE2 1 
ATOM   6671  C CZ  . TYR D 2 22  ? -40.072 29.512  33.043  1.00 43.32  ? 22  TYR D CZ  1 
ATOM   6672  O OH  . TYR D 2 22  ? -38.710 29.434  32.867  1.00 46.40  ? 22  TYR D OH  1 
ATOM   6673  N N   . GLY D 2 23  ? -47.161 30.799  34.810  1.00 39.29  ? 23  GLY D N   1 
ATOM   6674  C CA  . GLY D 2 23  ? -48.466 30.442  35.318  1.00 38.38  ? 23  GLY D CA  1 
ATOM   6675  C C   . GLY D 2 23  ? -49.588 31.040  34.505  1.00 44.41  ? 23  GLY D C   1 
ATOM   6676  O O   . GLY D 2 23  ? -49.384 31.587  33.418  1.00 43.96  ? 23  GLY D O   1 
ATOM   6677  N N   . TYR D 2 24  ? -50.786 30.930  35.064  1.00 48.29  ? 24  TYR D N   1 
ATOM   6678  C CA  . TYR D 2 24  ? -52.009 31.344  34.403  1.00 44.21  ? 24  TYR D CA  1 
ATOM   6679  C C   . TYR D 2 24  ? -52.741 32.367  35.257  1.00 37.20  ? 24  TYR D C   1 
ATOM   6680  O O   . TYR D 2 24  ? -52.573 32.420  36.481  1.00 37.24  ? 24  TYR D O   1 
ATOM   6681  C CB  . TYR D 2 24  ? -52.933 30.145  34.131  1.00 45.92  ? 24  TYR D CB  1 
ATOM   6682  C CG  . TYR D 2 24  ? -52.249 28.924  33.538  1.00 44.58  ? 24  TYR D CG  1 
ATOM   6683  C CD1 . TYR D 2 24  ? -51.685 27.950  34.356  1.00 56.78  ? 24  TYR D CD1 1 
ATOM   6684  C CD2 . TYR D 2 24  ? -52.174 28.743  32.164  1.00 44.02  ? 24  TYR D CD2 1 
ATOM   6685  C CE1 . TYR D 2 24  ? -51.069 26.826  33.819  1.00 46.61  ? 24  TYR D CE1 1 
ATOM   6686  C CE2 . TYR D 2 24  ? -51.554 27.626  31.618  1.00 51.77  ? 24  TYR D CE2 1 
ATOM   6687  C CZ  . TYR D 2 24  ? -51.006 26.670  32.452  1.00 45.49  ? 24  TYR D CZ  1 
ATOM   6688  O OH  . TYR D 2 24  ? -50.394 25.557  31.918  1.00 56.82  ? 24  TYR D OH  1 
ATOM   6689  N N   . HIS D 2 25  ? -53.535 33.200  34.592  1.00 40.16  ? 25  HIS D N   1 
ATOM   6690  C CA  . HIS D 2 25  ? -54.527 34.035  35.253  1.00 41.30  ? 25  HIS D CA  1 
ATOM   6691  C C   . HIS D 2 25  ? -55.857 33.828  34.548  1.00 43.64  ? 25  HIS D C   1 
ATOM   6692  O O   . HIS D 2 25  ? -55.913 33.807  33.314  1.00 43.13  ? 25  HIS D O   1 
ATOM   6693  C CB  . HIS D 2 25  ? -54.150 35.520  35.238  1.00 46.28  ? 25  HIS D CB  1 
ATOM   6694  C CG  . HIS D 2 25  ? -55.099 36.380  36.013  1.00 40.72  ? 25  HIS D CG  1 
ATOM   6695  N ND1 . HIS D 2 25  ? -56.313 36.795  35.504  1.00 45.12  ? 25  HIS D ND1 1 
ATOM   6696  C CD2 . HIS D 2 25  ? -55.028 36.877  37.271  1.00 36.50  ? 25  HIS D CD2 1 
ATOM   6697  C CE1 . HIS D 2 25  ? -56.940 37.523  36.411  1.00 45.37  ? 25  HIS D CE1 1 
ATOM   6698  N NE2 . HIS D 2 25  ? -56.182 37.589  37.491  1.00 51.54  ? 25  HIS D NE2 1 
ATOM   6699  N N   . HIS D 2 26  ? -56.919 33.668  35.327  1.00 38.21  ? 26  HIS D N   1 
ATOM   6700  C CA  . HIS D 2 26  ? -58.229 33.368  34.780  1.00 40.68  ? 26  HIS D CA  1 
ATOM   6701  C C   . HIS D 2 26  ? -59.243 34.345  35.345  1.00 46.32  ? 26  HIS D C   1 
ATOM   6702  O O   . HIS D 2 26  ? -59.072 34.881  36.443  1.00 48.74  ? 26  HIS D O   1 
ATOM   6703  C CB  . HIS D 2 26  ? -58.661 31.925  35.090  1.00 31.70  ? 26  HIS D CB  1 
ATOM   6704  C CG  . HIS D 2 26  ? -58.943 31.681  36.538  1.00 37.08  ? 26  HIS D CG  1 
ATOM   6705  N ND1 . HIS D 2 26  ? -60.187 31.882  37.096  1.00 47.99  ? 26  HIS D ND1 1 
ATOM   6706  C CD2 . HIS D 2 26  ? -58.141 31.262  37.546  1.00 43.79  ? 26  HIS D CD2 1 
ATOM   6707  C CE1 . HIS D 2 26  ? -60.138 31.597  38.386  1.00 60.18  ? 26  HIS D CE1 1 
ATOM   6708  N NE2 . HIS D 2 26  ? -58.908 31.220  38.684  1.00 48.95  ? 26  HIS D NE2 1 
ATOM   6709  N N   . SER D 2 27  ? -60.298 34.575  34.573  1.00 39.62  ? 27  SER D N   1 
ATOM   6710  C CA  . SER D 2 27  ? -61.396 35.430  35.005  1.00 49.34  ? 27  SER D CA  1 
ATOM   6711  C C   . SER D 2 27  ? -62.683 34.847  34.443  1.00 44.52  ? 27  SER D C   1 
ATOM   6712  O O   . SER D 2 27  ? -62.813 34.704  33.222  1.00 45.10  ? 27  SER D O   1 
ATOM   6713  C CB  . SER D 2 27  ? -61.180 36.871  34.535  1.00 47.14  ? 27  SER D CB  1 
ATOM   6714  O OG  . SER D 2 27  ? -62.386 37.613  34.558  1.00 67.60  ? 27  SER D OG  1 
ATOM   6715  N N   . ASN D 2 28  ? -63.613 34.489  35.322  1.00 45.71  ? 28  ASN D N   1 
ATOM   6716  C CA  . ASN D 2 28  ? -64.888 33.901  34.908  1.00 53.02  ? 28  ASN D CA  1 
ATOM   6717  C C   . ASN D 2 28  ? -65.976 34.394  35.857  1.00 53.16  ? 28  ASN D C   1 
ATOM   6718  O O   . ASN D 2 28  ? -65.798 35.366  36.600  1.00 55.41  ? 28  ASN D O   1 
ATOM   6719  C CB  . ASN D 2 28  ? -64.795 32.366  34.838  1.00 38.97  ? 28  ASN D CB  1 
ATOM   6720  C CG  . ASN D 2 28  ? -64.398 31.733  36.165  1.00 48.58  ? 28  ASN D CG  1 
ATOM   6721  O OD1 . ASN D 2 28  ? -64.342 32.390  37.203  1.00 56.84  ? 28  ASN D OD1 1 
ATOM   6722  N ND2 . ASN D 2 28  ? -64.096 30.441  36.124  1.00 48.63  ? 28  ASN D ND2 1 
ATOM   6723  N N   . GLU D 2 29  ? -67.129 33.716  35.823  1.00 61.31  ? 29  GLU D N   1 
ATOM   6724  C CA  . GLU D 2 29  ? -68.256 34.099  36.666  1.00 66.01  ? 29  GLU D CA  1 
ATOM   6725  C C   . GLU D 2 29  ? -67.913 33.986  38.145  1.00 61.73  ? 29  GLU D C   1 
ATOM   6726  O O   . GLU D 2 29  ? -68.300 34.844  38.947  1.00 63.85  ? 29  GLU D O   1 
ATOM   6727  C CB  . GLU D 2 29  ? -69.468 33.228  36.338  1.00 64.78  ? 29  GLU D CB  1 
ATOM   6728  C CG  . GLU D 2 29  ? -70.559 33.948  35.570  1.00 80.09  ? 29  GLU D CG  1 
ATOM   6729  C CD  . GLU D 2 29  ? -71.509 32.994  34.874  1.00 90.74  ? 29  GLU D CD  1 
ATOM   6730  O OE1 . GLU D 2 29  ? -71.273 31.766  34.923  1.00 91.90  ? 29  GLU D OE1 1 
ATOM   6731  O OE2 . GLU D 2 29  ? -72.491 33.476  34.273  1.00 80.47  ? 29  GLU D OE2 1 
ATOM   6732  N N   . GLN D 2 30  ? -67.191 32.934  38.526  1.00 57.69  ? 30  GLN D N   1 
ATOM   6733  C CA  . GLN D 2 30  ? -66.872 32.697  39.928  1.00 62.52  ? 30  GLN D CA  1 
ATOM   6734  C C   . GLN D 2 30  ? -65.781 33.615  40.464  1.00 47.70  ? 30  GLN D C   1 
ATOM   6735  O O   . GLN D 2 30  ? -65.513 33.589  41.669  1.00 48.11  ? 30  GLN D O   1 
ATOM   6736  C CB  . GLN D 2 30  ? -66.457 31.239  40.132  1.00 54.05  ? 30  GLN D CB  1 
ATOM   6737  C CG  . GLN D 2 30  ? -67.097 30.268  39.159  1.00 56.02  ? 30  GLN D CG  1 
ATOM   6738  C CD  . GLN D 2 30  ? -67.097 28.847  39.683  1.00 64.83  ? 30  GLN D CD  1 
ATOM   6739  O OE1 . GLN D 2 30  ? -67.187 28.615  40.888  1.00 68.84  ? 30  GLN D OE1 1 
ATOM   6740  N NE2 . GLN D 2 30  ? -66.990 27.886  38.778  1.00 61.96  ? 30  GLN D NE2 1 
ATOM   6741  N N   . GLY D 2 31  ? -65.145 34.414  39.614  1.00 49.07  ? 31  GLY D N   1 
ATOM   6742  C CA  . GLY D 2 31  ? -64.104 35.306  40.079  1.00 55.25  ? 31  GLY D CA  1 
ATOM   6743  C C   . GLY D 2 31  ? -62.843 35.254  39.242  1.00 54.44  ? 31  GLY D C   1 
ATOM   6744  O O   . GLY D 2 31  ? -62.886 34.938  38.049  1.00 57.28  ? 31  GLY D O   1 
ATOM   6745  N N   . SER D 2 32  ? -61.710 35.565  39.863  1.00 47.42  ? 32  SER D N   1 
ATOM   6746  C CA  . SER D 2 32  ? -60.441 35.603  39.156  1.00 42.03  ? 32  SER D CA  1 
ATOM   6747  C C   . SER D 2 32  ? -59.327 35.266  40.130  1.00 50.98  ? 32  SER D C   1 
ATOM   6748  O O   . SER D 2 32  ? -59.491 35.373  41.348  1.00 54.63  ? 32  SER D O   1 
ATOM   6749  C CB  . SER D 2 32  ? -60.193 36.973  38.521  1.00 50.23  ? 32  SER D CB  1 
ATOM   6750  O OG  . SER D 2 32  ? -59.811 37.916  39.507  1.00 55.42  ? 32  SER D OG  1 
ATOM   6751  N N   . GLY D 2 33  ? -58.188 34.863  39.578  1.00 52.88  ? 33  GLY D N   1 
ATOM   6752  C CA  . GLY D 2 33  ? -57.026 34.565  40.399  1.00 43.73  ? 33  GLY D CA  1 
ATOM   6753  C C   . GLY D 2 33  ? -55.891 34.034  39.549  1.00 51.13  ? 33  GLY D C   1 
ATOM   6754  O O   . GLY D 2 33  ? -56.049 33.751  38.356  1.00 45.89  ? 33  GLY D O   1 
ATOM   6755  N N   . TYR D 2 34  ? -54.735 33.900  40.193  1.00 53.23  ? 34  TYR D N   1 
ATOM   6756  C CA  . TYR D 2 34  ? -53.520 33.388  39.579  1.00 44.64  ? 34  TYR D CA  1 
ATOM   6757  C C   . TYR D 2 34  ? -53.328 31.916  39.934  1.00 50.07  ? 34  TYR D C   1 
ATOM   6758  O O   . TYR D 2 34  ? -53.852 31.423  40.935  1.00 52.48  ? 34  TYR D O   1 
ATOM   6759  C CB  . TYR D 2 34  ? -52.305 34.197  40.036  1.00 42.24  ? 34  TYR D CB  1 
ATOM   6760  C CG  . TYR D 2 34  ? -52.349 35.660  39.646  1.00 50.84  ? 34  TYR D CG  1 
ATOM   6761  C CD1 . TYR D 2 34  ? -51.807 36.090  38.442  1.00 48.16  ? 34  TYR D CD1 1 
ATOM   6762  C CD2 . TYR D 2 34  ? -52.920 36.612  40.484  1.00 49.50  ? 34  TYR D CD2 1 
ATOM   6763  C CE1 . TYR D 2 34  ? -51.839 37.423  38.076  1.00 48.86  ? 34  TYR D CE1 1 
ATOM   6764  C CE2 . TYR D 2 34  ? -52.958 37.953  40.124  1.00 40.36  ? 34  TYR D CE2 1 
ATOM   6765  C CZ  . TYR D 2 34  ? -52.414 38.349  38.918  1.00 46.32  ? 34  TYR D CZ  1 
ATOM   6766  O OH  . TYR D 2 34  ? -52.438 39.673  38.545  1.00 51.94  ? 34  TYR D OH  1 
ATOM   6767  N N   . ALA D 2 35  ? -52.565 31.214  39.095  1.00 38.06  ? 35  ALA D N   1 
ATOM   6768  C CA  . ALA D 2 35  ? -52.271 29.802  39.335  1.00 43.95  ? 35  ALA D CA  1 
ATOM   6769  C C   . ALA D 2 35  ? -50.947 29.441  38.681  1.00 43.21  ? 35  ALA D C   1 
ATOM   6770  O O   . ALA D 2 35  ? -50.821 29.503  37.454  1.00 47.86  ? 35  ALA D O   1 
ATOM   6771  C CB  . ALA D 2 35  ? -53.387 28.906  38.801  1.00 39.67  ? 35  ALA D CB  1 
ATOM   6772  N N   . ALA D 2 36  ? -49.972 29.047  39.492  1.00 50.45  ? 36  ALA D N   1 
ATOM   6773  C CA  . ALA D 2 36  ? -48.656 28.700  38.977  1.00 60.78  ? 36  ALA D CA  1 
ATOM   6774  C C   . ALA D 2 36  ? -48.664 27.307  38.358  1.00 54.96  ? 36  ALA D C   1 
ATOM   6775  O O   . ALA D 2 36  ? -49.278 26.377  38.889  1.00 54.57  ? 36  ALA D O   1 
ATOM   6776  C CB  . ALA D 2 36  ? -47.610 28.774  40.089  1.00 48.12  ? 36  ALA D CB  1 
ATOM   6777  N N   . ASP D 2 37  ? -47.983 27.172  37.222  1.00 49.48  ? 37  ASP D N   1 
ATOM   6778  C CA  . ASP D 2 37  ? -47.803 25.884  36.560  1.00 55.98  ? 37  ASP D CA  1 
ATOM   6779  C C   . ASP D 2 37  ? -46.590 25.200  37.180  1.00 58.41  ? 37  ASP D C   1 
ATOM   6780  O O   . ASP D 2 37  ? -45.448 25.590  36.918  1.00 50.36  ? 37  ASP D O   1 
ATOM   6781  C CB  . ASP D 2 37  ? -47.630 26.068  35.055  1.00 49.48  ? 37  ASP D CB  1 
ATOM   6782  C CG  . ASP D 2 37  ? -47.569 24.749  34.309  1.00 51.59  ? 37  ASP D CG  1 
ATOM   6783  O OD1 . ASP D 2 37  ? -46.469 24.159  34.230  1.00 59.60  ? 37  ASP D OD1 1 
ATOM   6784  O OD2 . ASP D 2 37  ? -48.624 24.297  33.811  1.00 65.34  ? 37  ASP D OD2 1 
ATOM   6785  N N   . ARG D 2 38  ? -46.842 24.185  38.008  1.00 57.78  ? 38  ARG D N   1 
ATOM   6786  C CA  . ARG D 2 38  ? -45.769 23.591  38.800  1.00 57.03  ? 38  ARG D CA  1 
ATOM   6787  C C   . ARG D 2 38  ? -44.784 22.822  37.928  1.00 56.43  ? 38  ARG D C   1 
ATOM   6788  O O   . ARG D 2 38  ? -43.577 22.828  38.198  1.00 56.50  ? 38  ARG D O   1 
ATOM   6789  C CB  . ARG D 2 38  ? -46.362 22.684  39.880  1.00 56.86  ? 38  ARG D CB  1 
ATOM   6790  C CG  . ARG D 2 38  ? -45.352 21.775  40.571  1.00 75.54  ? 38  ARG D CG  1 
ATOM   6791  C CD  . ARG D 2 38  ? -44.844 22.383  41.871  1.00 93.23  ? 38  ARG D CD  1 
ATOM   6792  N NE  . ARG D 2 38  ? -43.800 23.376  41.639  1.00 97.25  ? 38  ARG D NE  1 
ATOM   6793  C CZ  . ARG D 2 38  ? -43.120 23.989  42.599  1.00 100.66 ? 38  ARG D CZ  1 
ATOM   6794  N NH1 . ARG D 2 38  ? -43.343 23.730  43.878  1.00 102.65 ? 38  ARG D NH1 1 
ATOM   6795  N NH2 . ARG D 2 38  ? -42.195 24.886  42.268  1.00 88.48  ? 38  ARG D NH2 1 
ATOM   6796  N N   . GLU D 2 39  ? -45.274 22.153  36.881  1.00 52.07  ? 39  GLU D N   1 
ATOM   6797  C CA  . GLU D 2 39  ? -44.418 21.256  36.107  1.00 55.66  ? 39  GLU D CA  1 
ATOM   6798  C C   . GLU D 2 39  ? -43.342 22.025  35.349  1.00 57.99  ? 39  GLU D C   1 
ATOM   6799  O O   . GLU D 2 39  ? -42.152 21.698  35.437  1.00 60.58  ? 39  GLU D O   1 
ATOM   6800  C CB  . GLU D 2 39  ? -45.266 20.426  35.143  1.00 62.73  ? 39  GLU D CB  1 
ATOM   6801  C CG  . GLU D 2 39  ? -44.509 19.912  33.926  1.00 75.25  ? 39  GLU D CG  1 
ATOM   6802  C CD  . GLU D 2 39  ? -45.428 19.307  32.880  1.00 100.13 ? 39  GLU D CD  1 
ATOM   6803  O OE1 . GLU D 2 39  ? -46.265 20.050  32.323  1.00 100.02 ? 39  GLU D OE1 1 
ATOM   6804  O OE2 . GLU D 2 39  ? -45.312 18.091  32.614  1.00 110.51 ? 39  GLU D OE2 1 
ATOM   6805  N N   . SER D 2 40  ? -43.738 23.057  34.603  1.00 55.08  ? 40  SER D N   1 
ATOM   6806  C CA  . SER D 2 40  ? -42.759 23.819  33.837  1.00 55.49  ? 40  SER D CA  1 
ATOM   6807  C C   . SER D 2 40  ? -41.867 24.661  34.741  1.00 54.16  ? 40  SER D C   1 
ATOM   6808  O O   . SER D 2 40  ? -40.688 24.862  34.429  1.00 48.04  ? 40  SER D O   1 
ATOM   6809  C CB  . SER D 2 40  ? -43.466 24.704  32.817  1.00 52.22  ? 40  SER D CB  1 
ATOM   6810  O OG  . SER D 2 40  ? -44.555 25.368  33.422  1.00 62.14  ? 40  SER D OG  1 
ATOM   6811  N N   . THR D 2 41  ? -42.407 25.171  35.852  1.00 39.84  ? 41  THR D N   1 
ATOM   6812  C CA  . THR D 2 41  ? -41.579 25.919  36.792  1.00 41.65  ? 41  THR D CA  1 
ATOM   6813  C C   . THR D 2 41  ? -40.505 25.028  37.403  1.00 48.03  ? 41  THR D C   1 
ATOM   6814  O O   . THR D 2 41  ? -39.343 25.434  37.515  1.00 47.11  ? 41  THR D O   1 
ATOM   6815  C CB  . THR D 2 41  ? -42.446 26.543  37.888  1.00 44.84  ? 41  THR D CB  1 
ATOM   6816  O OG1 . THR D 2 41  ? -43.286 27.559  37.326  1.00 43.75  ? 41  THR D OG1 1 
ATOM   6817  C CG2 . THR D 2 41  ? -41.580 27.172  38.961  1.00 42.79  ? 41  THR D CG2 1 
ATOM   6818  N N   . GLN D 2 42  ? -40.873 23.805  37.793  1.00 55.98  ? 42  GLN D N   1 
ATOM   6819  C CA  . GLN D 2 42  ? -39.898 22.891  38.378  1.00 49.45  ? 42  GLN D CA  1 
ATOM   6820  C C   . GLN D 2 42  ? -38.848 22.472  37.357  1.00 55.41  ? 42  GLN D C   1 
ATOM   6821  O O   . GLN D 2 42  ? -37.659 22.383  37.686  1.00 52.34  ? 42  GLN D O   1 
ATOM   6822  C CB  . GLN D 2 42  ? -40.601 21.666  38.958  1.00 49.58  ? 42  GLN D CB  1 
ATOM   6823  C CG  . GLN D 2 42  ? -39.768 20.933  40.006  1.00 50.20  ? 42  GLN D CG  1 
ATOM   6824  C CD  . GLN D 2 42  ? -39.151 21.883  41.020  1.00 62.47  ? 42  GLN D CD  1 
ATOM   6825  O OE1 . GLN D 2 42  ? -39.860 22.617  41.716  1.00 58.27  ? 42  GLN D OE1 1 
ATOM   6826  N NE2 . GLN D 2 42  ? -37.826 21.875  41.107  1.00 47.43  ? 42  GLN D NE2 1 
ATOM   6827  N N   . LYS D 2 43  ? -39.265 22.207  36.115  1.00 45.06  ? 43  LYS D N   1 
ATOM   6828  C CA  . LYS D 2 43  ? -38.299 21.895  35.066  1.00 46.55  ? 43  LYS D CA  1 
ATOM   6829  C C   . LYS D 2 43  ? -37.329 23.048  34.863  1.00 54.47  ? 43  LYS D C   1 
ATOM   6830  O O   . LYS D 2 43  ? -36.119 22.837  34.708  1.00 47.61  ? 43  LYS D O   1 
ATOM   6831  C CB  . LYS D 2 43  ? -39.019 21.583  33.755  1.00 54.61  ? 43  LYS D CB  1 
ATOM   6832  C CG  . LYS D 2 43  ? -39.403 20.125  33.566  1.00 62.84  ? 43  LYS D CG  1 
ATOM   6833  C CD  . LYS D 2 43  ? -40.562 19.964  32.577  1.00 72.17  ? 43  LYS D CD  1 
ATOM   6834  C CE  . LYS D 2 43  ? -40.866 21.262  31.826  1.00 84.48  ? 43  LYS D CE  1 
ATOM   6835  N NZ  . LYS D 2 43  ? -42.165 21.219  31.093  1.00 77.28  ? 43  LYS D NZ  1 
ATOM   6836  N N   . ALA D 2 44  ? -37.847 24.280  34.857  1.00 47.10  ? 44  ALA D N   1 
ATOM   6837  C CA  . ALA D 2 44  ? -36.988 25.448  34.727  1.00 53.70  ? 44  ALA D CA  1 
ATOM   6838  C C   . ALA D 2 44  ? -36.054 25.586  35.926  1.00 44.66  ? 44  ALA D C   1 
ATOM   6839  O O   . ALA D 2 44  ? -34.878 25.923  35.763  1.00 45.44  ? 44  ALA D O   1 
ATOM   6840  C CB  . ALA D 2 44  ? -37.839 26.706  34.552  1.00 33.34  ? 44  ALA D CB  1 
ATOM   6841  N N   . ILE D 2 45  ? -36.560 25.341  37.136  1.00 47.40  ? 45  ILE D N   1 
ATOM   6842  C CA  . ILE D 2 45  ? -35.720 25.469  38.323  1.00 46.40  ? 45  ILE D CA  1 
ATOM   6843  C C   . ILE D 2 45  ? -34.621 24.416  38.307  1.00 46.78  ? 45  ILE D C   1 
ATOM   6844  O O   . ILE D 2 45  ? -33.450 24.709  38.573  1.00 53.17  ? 45  ILE D O   1 
ATOM   6845  C CB  . ILE D 2 45  ? -36.566 25.375  39.604  1.00 48.60  ? 45  ILE D CB  1 
ATOM   6846  C CG1 . ILE D 2 45  ? -37.325 26.677  39.832  1.00 45.89  ? 45  ILE D CG1 1 
ATOM   6847  C CG2 . ILE D 2 45  ? -35.675 25.098  40.807  1.00 42.59  ? 45  ILE D CG2 1 
ATOM   6848  C CD1 . ILE D 2 45  ? -38.541 26.510  40.704  1.00 46.16  ? 45  ILE D CD1 1 
ATOM   6849  N N   . ASP D 2 46  ? -34.982 23.174  37.989  1.00 45.69  ? 46  ASP D N   1 
ATOM   6850  C CA  . ASP D 2 46  ? -33.984 22.115  37.944  1.00 47.27  ? 46  ASP D CA  1 
ATOM   6851  C C   . ASP D 2 46  ? -32.913 22.417  36.902  1.00 54.78  ? 46  ASP D C   1 
ATOM   6852  O O   . ASP D 2 46  ? -31.718 22.202  37.147  1.00 51.66  ? 46  ASP D O   1 
ATOM   6853  C CB  . ASP D 2 46  ? -34.658 20.773  37.655  1.00 50.37  ? 46  ASP D CB  1 
ATOM   6854  C CG  . ASP D 2 46  ? -35.632 20.355  38.750  1.00 52.84  ? 46  ASP D CG  1 
ATOM   6855  O OD1 . ASP D 2 46  ? -35.663 21.015  39.813  1.00 47.30  ? 46  ASP D OD1 1 
ATOM   6856  O OD2 . ASP D 2 46  ? -36.368 19.365  38.541  1.00 54.63  ? 46  ASP D OD2 1 
ATOM   6857  N N   . GLY D 2 47  ? -33.325 22.914  35.732  1.00 50.47  ? 47  GLY D N   1 
ATOM   6858  C CA  . GLY D 2 47  ? -32.363 23.200  34.678  1.00 43.01  ? 47  GLY D CA  1 
ATOM   6859  C C   . GLY D 2 47  ? -31.431 24.346  35.023  1.00 51.30  ? 47  GLY D C   1 
ATOM   6860  O O   . GLY D 2 47  ? -30.221 24.272  34.785  1.00 50.79  ? 47  GLY D O   1 
ATOM   6861  N N   . VAL D 2 48  ? -31.986 25.430  35.569  1.00 43.46  ? 48  VAL D N   1 
ATOM   6862  C CA  . VAL D 2 48  ? -31.177 26.600  35.895  1.00 45.19  ? 48  VAL D CA  1 
ATOM   6863  C C   . VAL D 2 48  ? -30.203 26.276  37.020  1.00 46.94  ? 48  VAL D C   1 
ATOM   6864  O O   . VAL D 2 48  ? -29.056 26.742  37.025  1.00 46.61  ? 48  VAL D O   1 
ATOM   6865  C CB  . VAL D 2 48  ? -32.096 27.787  36.237  1.00 45.26  ? 48  VAL D CB  1 
ATOM   6866  C CG1 . VAL D 2 48  ? -31.415 28.755  37.191  1.00 52.28  ? 48  VAL D CG1 1 
ATOM   6867  C CG2 . VAL D 2 48  ? -32.512 28.500  34.962  1.00 34.39  ? 48  VAL D CG2 1 
ATOM   6868  N N   . THR D 2 49  ? -30.642 25.463  37.985  1.00 44.61  ? 49  THR D N   1 
ATOM   6869  C CA  . THR D 2 49  ? -29.742 24.985  39.027  1.00 39.66  ? 49  THR D CA  1 
ATOM   6870  C C   . THR D 2 49  ? -28.624 24.139  38.438  1.00 42.62  ? 49  THR D C   1 
ATOM   6871  O O   . THR D 2 49  ? -27.464 24.255  38.850  1.00 54.03  ? 49  THR D O   1 
ATOM   6872  C CB  . THR D 2 49  ? -30.528 24.187  40.066  1.00 41.88  ? 49  THR D CB  1 
ATOM   6873  O OG1 . THR D 2 49  ? -31.580 25.007  40.595  1.00 47.46  ? 49  THR D OG1 1 
ATOM   6874  C CG2 . THR D 2 49  ? -29.612 23.729  41.200  1.00 28.95  ? 49  THR D CG2 1 
ATOM   6875  N N   . ASN D 2 50  ? -28.953 23.284  37.469  1.00 46.29  ? 50  ASN D N   1 
ATOM   6876  C CA  . ASN D 2 50  ? -27.934 22.463  36.828  1.00 33.42  ? 50  ASN D CA  1 
ATOM   6877  C C   . ASN D 2 50  ? -26.911 23.324  36.100  1.00 45.42  ? 50  ASN D C   1 
ATOM   6878  O O   . ASN D 2 50  ? -25.714 23.013  36.104  1.00 44.52  ? 50  ASN D O   1 
ATOM   6879  C CB  . ASN D 2 50  ? -28.583 21.479  35.860  1.00 42.42  ? 50  ASN D CB  1 
ATOM   6880  C CG  . ASN D 2 50  ? -28.599 20.063  36.398  1.00 67.16  ? 50  ASN D CG  1 
ATOM   6881  O OD1 . ASN D 2 50  ? -27.689 19.277  36.130  1.00 67.53  ? 50  ASN D OD1 1 
ATOM   6882  N ND2 . ASN D 2 50  ? -29.637 19.728  37.160  1.00 67.55  ? 50  ASN D ND2 1 
ATOM   6883  N N   . LYS D 2 51  ? -27.364 24.404  35.458  1.00 35.94  ? 51  LYS D N   1 
ATOM   6884  C CA  . LYS D 2 51  ? -26.437 25.284  34.756  1.00 41.94  ? 51  LYS D CA  1 
ATOM   6885  C C   . LYS D 2 51  ? -25.452 25.921  35.726  1.00 47.74  ? 51  LYS D C   1 
ATOM   6886  O O   . LYS D 2 51  ? -24.238 25.908  35.497  1.00 44.59  ? 51  LYS D O   1 
ATOM   6887  C CB  . LYS D 2 51  ? -27.203 26.365  33.995  1.00 44.48  ? 51  LYS D CB  1 
ATOM   6888  C CG  . LYS D 2 51  ? -26.326 27.531  33.580  1.00 45.53  ? 51  LYS D CG  1 
ATOM   6889  C CD  . LYS D 2 51  ? -27.122 28.636  32.917  1.00 49.04  ? 51  LYS D CD  1 
ATOM   6890  C CE  . LYS D 2 51  ? -28.008 28.096  31.817  1.00 52.98  ? 51  LYS D CE  1 
ATOM   6891  N NZ  . LYS D 2 51  ? -28.048 29.055  30.687  1.00 46.90  ? 51  LYS D NZ  1 
ATOM   6892  N N   . VAL D 2 52  ? -25.959 26.477  36.827  1.00 41.42  ? 52  VAL D N   1 
ATOM   6893  C CA  . VAL D 2 52  ? -25.080 27.086  37.816  1.00 37.14  ? 52  VAL D CA  1 
ATOM   6894  C C   . VAL D 2 52  ? -24.135 26.044  38.401  1.00 43.84  ? 52  VAL D C   1 
ATOM   6895  O O   . VAL D 2 52  ? -22.929 26.285  38.544  1.00 38.49  ? 52  VAL D O   1 
ATOM   6896  C CB  . VAL D 2 52  ? -25.917 27.770  38.912  1.00 40.23  ? 52  VAL D CB  1 
ATOM   6897  C CG1 . VAL D 2 52  ? -25.017 28.203  40.067  1.00 41.35  ? 52  VAL D CG1 1 
ATOM   6898  C CG2 . VAL D 2 52  ? -26.686 28.949  38.329  1.00 39.32  ? 52  VAL D CG2 1 
ATOM   6899  N N   . ASN D 2 53  ? -24.661 24.870  38.744  1.00 39.68  ? 53  ASN D N   1 
ATOM   6900  C CA  . ASN D 2 53  ? -23.816 23.849  39.349  1.00 42.67  ? 53  ASN D CA  1 
ATOM   6901  C C   . ASN D 2 53  ? -22.806 23.307  38.349  1.00 43.34  ? 53  ASN D C   1 
ATOM   6902  O O   . ASN D 2 53  ? -21.681 22.966  38.724  1.00 50.72  ? 53  ASN D O   1 
ATOM   6903  C CB  . ASN D 2 53  ? -24.674 22.725  39.924  1.00 41.69  ? 53  ASN D CB  1 
ATOM   6904  C CG  . ASN D 2 53  ? -25.443 23.163  41.150  1.00 43.35  ? 53  ASN D CG  1 
ATOM   6905  O OD1 . ASN D 2 53  ? -25.104 24.160  41.788  1.00 53.86  ? 53  ASN D OD1 1 
ATOM   6906  N ND2 . ASN D 2 53  ? -26.489 22.428  41.480  1.00 37.90  ? 53  ASN D ND2 1 
ATOM   6907  N N   . SER D 2 54  ? -23.186 23.212  37.072  1.00 42.94  ? 54  SER D N   1 
ATOM   6908  C CA  . SER D 2 54  ? -22.223 22.785  36.063  1.00 39.46  ? 54  SER D CA  1 
ATOM   6909  C C   . SER D 2 54  ? -21.087 23.792  35.930  1.00 49.12  ? 54  SER D C   1 
ATOM   6910  O O   . SER D 2 54  ? -19.913 23.410  35.842  1.00 43.18  ? 54  SER D O   1 
ATOM   6911  C CB  . SER D 2 54  ? -22.924 22.575  34.721  1.00 40.25  ? 54  SER D CB  1 
ATOM   6912  O OG  . SER D 2 54  ? -24.032 21.702  34.865  1.00 48.42  ? 54  SER D OG  1 
ATOM   6913  N N   . ILE D 2 55  ? -21.414 25.087  35.927  1.00 46.93  ? 55  ILE D N   1 
ATOM   6914  C CA  . ILE D 2 55  ? -20.386 26.117  35.823  1.00 44.22  ? 55  ILE D CA  1 
ATOM   6915  C C   . ILE D 2 55  ? -19.477 26.095  37.046  1.00 47.95  ? 55  ILE D C   1 
ATOM   6916  O O   . ILE D 2 55  ? -18.269 26.345  36.940  1.00 52.91  ? 55  ILE D O   1 
ATOM   6917  C CB  . ILE D 2 55  ? -21.048 27.493  35.608  1.00 36.22  ? 55  ILE D CB  1 
ATOM   6918  C CG1 . ILE D 2 55  ? -21.755 27.522  34.253  1.00 40.76  ? 55  ILE D CG1 1 
ATOM   6919  C CG2 . ILE D 2 55  ? -20.024 28.622  35.663  1.00 39.86  ? 55  ILE D CG2 1 
ATOM   6920  C CD1 . ILE D 2 55  ? -22.716 28.679  34.089  1.00 46.19  ? 55  ILE D CD1 1 
ATOM   6921  N N   . ILE D 2 56  ? -20.028 25.777  38.216  1.00 47.18  ? 56  ILE D N   1 
ATOM   6922  C CA  . ILE D 2 56  ? -19.228 25.723  39.434  1.00 46.78  ? 56  ILE D CA  1 
ATOM   6923  C C   . ILE D 2 56  ? -18.479 24.398  39.539  1.00 51.22  ? 56  ILE D C   1 
ATOM   6924  O O   . ILE D 2 56  ? -17.263 24.372  39.762  1.00 50.96  ? 56  ILE D O   1 
ATOM   6925  C CB  . ILE D 2 56  ? -20.125 25.964  40.662  1.00 53.61  ? 56  ILE D CB  1 
ATOM   6926  C CG1 . ILE D 2 56  ? -20.683 27.389  40.644  1.00 46.94  ? 56  ILE D CG1 1 
ATOM   6927  C CG2 . ILE D 2 56  ? -19.353 25.695  41.951  1.00 42.96  ? 56  ILE D CG2 1 
ATOM   6928  C CD1 . ILE D 2 56  ? -21.743 27.650  41.701  1.00 39.03  ? 56  ILE D CD1 1 
ATOM   6929  N N   . ASP D 2 57  ? -19.186 23.276  39.374  1.00 52.90  ? 57  ASP D N   1 
ATOM   6930  C CA  . ASP D 2 57  ? -18.601 21.974  39.690  1.00 42.34  ? 57  ASP D CA  1 
ATOM   6931  C C   . ASP D 2 57  ? -17.584 21.503  38.656  1.00 45.24  ? 57  ASP D C   1 
ATOM   6932  O O   . ASP D 2 57  ? -16.750 20.648  38.974  1.00 49.65  ? 57  ASP D O   1 
ATOM   6933  C CB  . ASP D 2 57  ? -19.699 20.919  39.843  1.00 43.79  ? 57  ASP D CB  1 
ATOM   6934  C CG  . ASP D 2 57  ? -20.601 21.180  41.044  1.00 57.31  ? 57  ASP D CG  1 
ATOM   6935  O OD1 . ASP D 2 57  ? -20.213 21.972  41.929  1.00 56.97  ? 57  ASP D OD1 1 
ATOM   6936  O OD2 . ASP D 2 57  ? -21.700 20.587  41.102  1.00 66.06  ? 57  ASP D OD2 1 
ATOM   6937  N N   . LYS D 2 58  ? -17.629 22.018  37.430  1.00 41.65  ? 58  LYS D N   1 
ATOM   6938  C CA  . LYS D 2 58  ? -16.681 21.563  36.423  1.00 45.56  ? 58  LYS D CA  1 
ATOM   6939  C C   . LYS D 2 58  ? -15.286 22.143  36.617  1.00 49.46  ? 58  LYS D C   1 
ATOM   6940  O O   . LYS D 2 58  ? -14.344 21.685  35.961  1.00 39.59  ? 58  LYS D O   1 
ATOM   6941  C CB  . LYS D 2 58  ? -17.192 21.907  35.024  1.00 45.80  ? 58  LYS D CB  1 
ATOM   6942  C CG  . LYS D 2 58  ? -18.330 21.017  34.545  1.00 48.17  ? 58  LYS D CG  1 
ATOM   6943  C CD  . LYS D 2 58  ? -17.906 19.566  34.463  1.00 52.35  ? 58  LYS D CD  1 
ATOM   6944  C CE  . LYS D 2 58  ? -19.015 18.693  33.891  1.00 53.71  ? 58  LYS D CE  1 
ATOM   6945  N NZ  . LYS D 2 58  ? -18.620 17.256  33.878  1.00 54.41  ? 58  LYS D NZ  1 
ATOM   6946  N N   . MET D 2 59  ? -15.130 23.131  37.493  1.00 48.63  ? 59  MET D N   1 
ATOM   6947  C CA  . MET D 2 59  ? -13.817 23.707  37.733  1.00 41.65  ? 59  MET D CA  1 
ATOM   6948  C C   . MET D 2 59  ? -12.956 22.735  38.526  1.00 42.03  ? 59  MET D C   1 
ATOM   6949  O O   . MET D 2 59  ? -13.370 22.237  39.577  1.00 58.65  ? 59  MET D O   1 
ATOM   6950  C CB  . MET D 2 59  ? -13.945 25.028  38.487  1.00 35.69  ? 59  MET D CB  1 
ATOM   6951  C CG  . MET D 2 59  ? -12.614 25.648  38.842  1.00 38.97  ? 59  MET D CG  1 
ATOM   6952  S SD  . MET D 2 59  ? -11.650 26.065  37.373  1.00 53.08  ? 59  MET D SD  1 
ATOM   6953  C CE  . MET D 2 59  ? -12.488 27.552  36.823  1.00 34.04  ? 59  MET D CE  1 
ATOM   6954  N N   . ASN D 2 60  ? -11.755 22.472  38.027  1.00 44.46  ? 60  ASN D N   1 
ATOM   6955  C CA  . ASN D 2 60  ? -10.780 21.656  38.736  1.00 48.61  ? 60  ASN D CA  1 
ATOM   6956  C C   . ASN D 2 60  ? -9.803  22.575  39.455  1.00 47.41  ? 60  ASN D C   1 
ATOM   6957  O O   . ASN D 2 60  ? -9.169  23.428  38.826  1.00 54.99  ? 60  ASN D O   1 
ATOM   6958  C CB  . ASN D 2 60  ? -10.030 20.730  37.783  1.00 53.85  ? 60  ASN D CB  1 
ATOM   6959  C CG  . ASN D 2 60  ? -9.007  19.876  38.500  1.00 61.77  ? 60  ASN D CG  1 
ATOM   6960  O OD1 . ASN D 2 60  ? -9.360  19.026  39.321  1.00 66.44  ? 60  ASN D OD1 1 
ATOM   6961  N ND2 . ASN D 2 60  ? -7.732  20.104  38.207  1.00 53.58  ? 60  ASN D ND2 1 
ATOM   6962  N N   . THR D 2 61  ? -9.693  22.409  40.767  1.00 48.56  ? 61  THR D N   1 
ATOM   6963  C CA  . THR D 2 61  ? -8.741  23.157  41.573  1.00 53.73  ? 61  THR D CA  1 
ATOM   6964  C C   . THR D 2 61  ? -7.729  22.194  42.178  1.00 55.38  ? 61  THR D C   1 
ATOM   6965  O O   . THR D 2 61  ? -8.064  21.056  42.520  1.00 62.80  ? 61  THR D O   1 
ATOM   6966  C CB  . THR D 2 61  ? -9.445  23.958  42.679  1.00 51.62  ? 61  THR D CB  1 
ATOM   6967  O OG1 . THR D 2 61  ? -10.004 23.061  43.644  1.00 63.01  ? 61  THR D OG1 1 
ATOM   6968  C CG2 . THR D 2 61  ? -10.548 24.830  42.096  1.00 44.32  ? 61  THR D CG2 1 
ATOM   6969  N N   . GLN D 2 62  ? -6.484  22.647  42.282  1.00 53.40  ? 62  GLN D N   1 
ATOM   6970  C CA  . GLN D 2 62  ? -5.428  21.857  42.896  1.00 55.21  ? 62  GLN D CA  1 
ATOM   6971  C C   . GLN D 2 62  ? -4.580  22.763  43.774  1.00 53.14  ? 62  GLN D C   1 
ATOM   6972  O O   . GLN D 2 62  ? -4.623  23.990  43.659  1.00 44.42  ? 62  GLN D O   1 
ATOM   6973  C CB  . GLN D 2 62  ? -4.559  21.153  41.845  1.00 52.46  ? 62  GLN D CB  1 
ATOM   6974  C CG  . GLN D 2 62  ? -4.569  21.807  40.477  1.00 52.09  ? 62  GLN D CG  1 
ATOM   6975  C CD  . GLN D 2 62  ? -3.874  20.955  39.429  1.00 56.90  ? 62  GLN D CD  1 
ATOM   6976  O OE1 . GLN D 2 62  ? -3.065  20.088  39.759  1.00 52.77  ? 62  GLN D OE1 1 
ATOM   6977  N NE2 . GLN D 2 62  ? -4.182  21.203  38.160  1.00 53.58  ? 62  GLN D NE2 1 
ATOM   6978  N N   . PHE D 2 63  ? -3.820  22.140  44.671  1.00 54.33  ? 63  PHE D N   1 
ATOM   6979  C CA  . PHE D 2 63  ? -2.964  22.894  45.575  1.00 50.97  ? 63  PHE D CA  1 
ATOM   6980  C C   . PHE D 2 63  ? -1.849  23.581  44.798  1.00 51.37  ? 63  PHE D C   1 
ATOM   6981  O O   . PHE D 2 63  ? -1.129  22.940  44.027  1.00 53.25  ? 63  PHE D O   1 
ATOM   6982  C CB  . PHE D 2 63  ? -2.368  21.968  46.635  1.00 47.12  ? 63  PHE D CB  1 
ATOM   6983  C CG  . PHE D 2 63  ? -1.328  22.627  47.494  1.00 57.45  ? 63  PHE D CG  1 
ATOM   6984  C CD1 . PHE D 2 63  ? -1.699  23.336  48.626  1.00 55.39  ? 63  PHE D CD1 1 
ATOM   6985  C CD2 . PHE D 2 63  ? 0.020   22.546  47.169  1.00 49.50  ? 63  PHE D CD2 1 
ATOM   6986  C CE1 . PHE D 2 63  ? -0.747  23.949  49.419  1.00 59.63  ? 63  PHE D CE1 1 
ATOM   6987  C CE2 . PHE D 2 63  ? 0.976   23.159  47.959  1.00 55.24  ? 63  PHE D CE2 1 
ATOM   6988  C CZ  . PHE D 2 63  ? 0.592   23.860  49.085  1.00 55.51  ? 63  PHE D CZ  1 
ATOM   6989  N N   . GLU D 2 64  ? -1.696  24.884  45.016  1.00 51.75  ? 64  GLU D N   1 
ATOM   6990  C CA  . GLU D 2 64  ? -0.581  25.631  44.456  1.00 54.93  ? 64  GLU D CA  1 
ATOM   6991  C C   . GLU D 2 64  ? -0.026  26.559  45.524  1.00 50.29  ? 64  GLU D C   1 
ATOM   6992  O O   . GLU D 2 64  ? -0.762  27.052  46.380  1.00 52.06  ? 64  GLU D O   1 
ATOM   6993  C CB  . GLU D 2 64  ? -0.989  26.444  43.215  1.00 46.06  ? 64  GLU D CB  1 
ATOM   6994  C CG  . GLU D 2 64  ? -1.419  25.607  42.009  1.00 45.34  ? 64  GLU D CG  1 
ATOM   6995  C CD  . GLU D 2 64  ? -0.371  24.597  41.573  1.00 48.37  ? 64  GLU D CD  1 
ATOM   6996  O OE1 . GLU D 2 64  ? 0.835   24.854  41.762  1.00 71.23  ? 64  GLU D OE1 1 
ATOM   6997  O OE2 . GLU D 2 64  ? -0.755  23.546  41.027  1.00 52.05  ? 64  GLU D OE2 1 
ATOM   6998  N N   . ALA D 2 65  ? 1.285   26.786  45.469  1.00 52.67  ? 65  ALA D N   1 
ATOM   6999  C CA  . ALA D 2 65  ? 1.962   27.730  46.353  1.00 52.37  ? 65  ALA D CA  1 
ATOM   7000  C C   . ALA D 2 65  ? 2.562   28.827  45.485  1.00 50.35  ? 65  ALA D C   1 
ATOM   7001  O O   . ALA D 2 65  ? 3.509   28.580  44.732  1.00 52.97  ? 65  ALA D O   1 
ATOM   7002  C CB  . ALA D 2 65  ? 3.030   27.034  47.195  1.00 39.92  ? 65  ALA D CB  1 
ATOM   7003  N N   . VAL D 2 66  ? 2.010   30.031  45.583  1.00 51.27  ? 66  VAL D N   1 
ATOM   7004  C CA  . VAL D 2 66  ? 2.405   31.153  44.741  1.00 45.88  ? 66  VAL D CA  1 
ATOM   7005  C C   . VAL D 2 66  ? 3.121   32.172  45.616  1.00 58.12  ? 66  VAL D C   1 
ATOM   7006  O O   . VAL D 2 66  ? 2.510   32.785  46.500  1.00 54.53  ? 66  VAL D O   1 
ATOM   7007  C CB  . VAL D 2 66  ? 1.201   31.787  44.037  1.00 51.10  ? 66  VAL D CB  1 
ATOM   7008  C CG1 . VAL D 2 66  ? 1.638   33.016  43.253  1.00 43.69  ? 66  VAL D CG1 1 
ATOM   7009  C CG2 . VAL D 2 66  ? 0.518   30.766  43.135  1.00 37.76  ? 66  VAL D CG2 1 
ATOM   7010  N N   . GLY D 2 67  ? 4.411   32.370  45.356  1.00 55.12  ? 67  GLY D N   1 
ATOM   7011  C CA  . GLY D 2 67  ? 5.184   33.376  46.057  1.00 52.68  ? 67  GLY D CA  1 
ATOM   7012  C C   . GLY D 2 67  ? 6.144   34.122  45.150  1.00 55.69  ? 67  GLY D C   1 
ATOM   7013  O O   . GLY D 2 67  ? 5.984   34.120  43.927  1.00 58.03  ? 67  GLY D O   1 
ATOM   7014  N N   . ARG D 2 68  ? 7.144   34.775  45.743  1.00 56.60  ? 68  ARG D N   1 
ATOM   7015  C CA  . ARG D 2 68  ? 8.190   35.493  45.012  1.00 51.76  ? 68  ARG D CA  1 
ATOM   7016  C C   . ARG D 2 68  ? 9.524   35.010  45.576  1.00 49.01  ? 68  ARG D C   1 
ATOM   7017  O O   . ARG D 2 68  ? 10.053  35.592  46.526  1.00 57.71  ? 68  ARG D O   1 
ATOM   7018  C CB  . ARG D 2 68  ? 8.019   37.002  45.150  1.00 43.09  ? 68  ARG D CB  1 
ATOM   7019  C CG  . ARG D 2 68  ? 6.731   37.529  44.545  1.00 42.46  ? 68  ARG D CG  1 
ATOM   7020  C CD  . ARG D 2 68  ? 6.646   37.183  43.072  1.00 46.64  ? 68  ARG D CD  1 
ATOM   7021  N NE  . ARG D 2 68  ? 5.573   37.906  42.398  1.00 49.16  ? 68  ARG D NE  1 
ATOM   7022  C CZ  . ARG D 2 68  ? 4.561   37.323  41.771  1.00 50.11  ? 68  ARG D CZ  1 
ATOM   7023  N NH1 . ARG D 2 68  ? 4.438   36.007  41.734  1.00 36.83  ? 68  ARG D NH1 1 
ATOM   7024  N NH2 . ARG D 2 68  ? 3.655   38.080  41.158  1.00 51.46  ? 68  ARG D NH2 1 
ATOM   7025  N N   . GLU D 2 69  ? 10.067  33.944  44.984  1.00 48.43  ? 69  GLU D N   1 
ATOM   7026  C CA  . GLU D 2 69  ? 11.196  33.218  45.553  1.00 56.31  ? 69  GLU D CA  1 
ATOM   7027  C C   . GLU D 2 69  ? 12.492  33.414  44.770  1.00 52.84  ? 69  GLU D C   1 
ATOM   7028  O O   . GLU D 2 69  ? 13.443  32.650  44.961  1.00 49.41  ? 69  GLU D O   1 
ATOM   7029  C CB  . GLU D 2 69  ? 10.862  31.727  45.646  1.00 56.83  ? 69  GLU D CB  1 
ATOM   7030  C CG  . GLU D 2 69  ? 9.554   31.415  46.366  1.00 68.92  ? 69  GLU D CG  1 
ATOM   7031  C CD  . GLU D 2 69  ? 9.499   29.985  46.897  1.00 84.26  ? 69  GLU D CD  1 
ATOM   7032  O OE1 . GLU D 2 69  ? 10.273  29.659  47.826  1.00 71.28  ? 69  GLU D OE1 1 
ATOM   7033  O OE2 . GLU D 2 69  ? 8.676   29.189  46.385  1.00 75.24  ? 69  GLU D OE2 1 
ATOM   7034  N N   . PHE D 2 70  ? 12.561  34.421  43.903  1.00 53.54  ? 70  PHE D N   1 
ATOM   7035  C CA  . PHE D 2 70  ? 13.738  34.651  43.074  1.00 51.41  ? 70  PHE D CA  1 
ATOM   7036  C C   . PHE D 2 70  ? 14.400  35.969  43.459  1.00 49.49  ? 70  PHE D C   1 
ATOM   7037  O O   . PHE D 2 70  ? 13.718  36.971  43.690  1.00 50.62  ? 70  PHE D O   1 
ATOM   7038  C CB  . PHE D 2 70  ? 13.362  34.637  41.586  1.00 56.94  ? 70  PHE D CB  1 
ATOM   7039  C CG  . PHE D 2 70  ? 12.811  33.316  41.122  1.00 43.83  ? 70  PHE D CG  1 
ATOM   7040  C CD1 . PHE D 2 70  ? 13.636  32.208  41.009  1.00 46.56  ? 70  PHE D CD1 1 
ATOM   7041  C CD2 . PHE D 2 70  ? 11.464  33.173  40.824  1.00 51.71  ? 70  PHE D CD2 1 
ATOM   7042  C CE1 . PHE D 2 70  ? 13.132  30.981  40.596  1.00 44.84  ? 70  PHE D CE1 1 
ATOM   7043  C CE2 . PHE D 2 70  ? 10.953  31.949  40.412  1.00 46.93  ? 70  PHE D CE2 1 
ATOM   7044  C CZ  . PHE D 2 70  ? 11.791  30.851  40.299  1.00 37.66  ? 70  PHE D CZ  1 
ATOM   7045  N N   . ASN D 2 71  ? 15.733  35.959  43.536  1.00 53.72  ? 71  ASN D N   1 
ATOM   7046  C CA  . ASN D 2 71  ? 16.489  37.101  44.027  1.00 52.26  ? 71  ASN D CA  1 
ATOM   7047  C C   . ASN D 2 71  ? 16.852  38.057  42.889  1.00 51.62  ? 71  ASN D C   1 
ATOM   7048  O O   . ASN D 2 71  ? 16.514  37.839  41.722  1.00 39.37  ? 71  ASN D O   1 
ATOM   7049  C CB  . ASN D 2 71  ? 17.739  36.633  44.769  1.00 52.18  ? 71  ASN D CB  1 
ATOM   7050  C CG  . ASN D 2 71  ? 18.670  35.813  43.897  1.00 57.58  ? 71  ASN D CG  1 
ATOM   7051  O OD1 . ASN D 2 71  ? 18.972  36.187  42.762  1.00 48.57  ? 71  ASN D OD1 1 
ATOM   7052  N ND2 . ASN D 2 71  ? 19.145  34.691  44.434  1.00 52.70  ? 71  ASN D ND2 1 
ATOM   7053  N N   . ASN D 2 72  ? 17.590  39.120  43.235  1.00 56.29  ? 72  ASN D N   1 
ATOM   7054  C CA  . ASN D 2 72  ? 17.834  40.232  42.319  1.00 49.69  ? 72  ASN D CA  1 
ATOM   7055  C C   . ASN D 2 72  ? 18.710  39.857  41.127  1.00 48.22  ? 72  ASN D C   1 
ATOM   7056  O O   . ASN D 2 72  ? 18.788  40.639  40.173  1.00 56.39  ? 72  ASN D O   1 
ATOM   7057  C CB  . ASN D 2 72  ? 18.459  41.411  43.074  1.00 54.05  ? 72  ASN D CB  1 
ATOM   7058  C CG  . ASN D 2 72  ? 19.938  41.209  43.362  1.00 77.25  ? 72  ASN D CG  1 
ATOM   7059  O OD1 . ASN D 2 72  ? 20.347  40.171  43.886  1.00 69.64  ? 72  ASN D OD1 1 
ATOM   7060  N ND2 . ASN D 2 72  ? 20.749  42.208  43.021  1.00 82.52  ? 72  ASN D ND2 1 
ATOM   7061  N N   . LEU D 2 73  ? 19.370  38.700  41.152  1.00 47.68  ? 73  LEU D N   1 
ATOM   7062  C CA  . LEU D 2 73  ? 20.113  38.206  40.000  1.00 46.98  ? 73  LEU D CA  1 
ATOM   7063  C C   . LEU D 2 73  ? 19.373  37.083  39.284  1.00 48.86  ? 73  LEU D C   1 
ATOM   7064  O O   . LEU D 2 73  ? 19.988  36.320  38.533  1.00 51.92  ? 73  LEU D O   1 
ATOM   7065  C CB  . LEU D 2 73  ? 21.509  37.748  40.423  1.00 43.60  ? 73  LEU D CB  1 
ATOM   7066  C CG  . LEU D 2 73  ? 22.542  38.882  40.429  1.00 56.01  ? 73  LEU D CG  1 
ATOM   7067  C CD1 . LEU D 2 73  ? 23.814  38.470  41.149  1.00 50.98  ? 73  LEU D CD1 1 
ATOM   7068  C CD2 . LEU D 2 73  ? 22.855  39.351  39.012  1.00 51.44  ? 73  LEU D CD2 1 
ATOM   7069  N N   . GLU D 2 74  ? 18.066  36.963  39.518  1.00 47.63  ? 74  GLU D N   1 
ATOM   7070  C CA  . GLU D 2 74  ? 17.211  36.001  38.836  1.00 49.69  ? 74  GLU D CA  1 
ATOM   7071  C C   . GLU D 2 74  ? 15.974  36.689  38.272  1.00 47.28  ? 74  GLU D C   1 
ATOM   7072  O O   . GLU D 2 74  ? 14.903  36.081  38.196  1.00 51.25  ? 74  GLU D O   1 
ATOM   7073  C CB  . GLU D 2 74  ? 16.803  34.866  39.776  1.00 43.90  ? 74  GLU D CB  1 
ATOM   7074  C CG  . GLU D 2 74  ? 17.936  33.947  40.185  1.00 36.37  ? 74  GLU D CG  1 
ATOM   7075  C CD  . GLU D 2 74  ? 17.580  33.076  41.381  1.00 49.67  ? 74  GLU D CD  1 
ATOM   7076  O OE1 . GLU D 2 74  ? 16.774  33.522  42.228  1.00 44.55  ? 74  GLU D OE1 1 
ATOM   7077  O OE2 . GLU D 2 74  ? 18.109  31.946  41.474  1.00 47.15  ? 74  GLU D OE2 1 
ATOM   7078  N N   . ARG D 2 75  ? 16.105  37.962  37.879  1.00 42.68  ? 75  ARG D N   1 
ATOM   7079  C CA  . ARG D 2 75  ? 14.946  38.714  37.403  1.00 45.10  ? 75  ARG D CA  1 
ATOM   7080  C C   . ARG D 2 75  ? 14.392  38.138  36.108  1.00 45.22  ? 75  ARG D C   1 
ATOM   7081  O O   . ARG D 2 75  ? 13.193  38.276  35.839  1.00 47.13  ? 75  ARG D O   1 
ATOM   7082  C CB  . ARG D 2 75  ? 15.305  40.188  37.206  1.00 34.75  ? 75  ARG D CB  1 
ATOM   7083  C CG  . ARG D 2 75  ? 15.734  40.907  38.479  1.00 38.50  ? 75  ARG D CG  1 
ATOM   7084  C CD  . ARG D 2 75  ? 14.693  40.777  39.569  1.00 62.56  ? 75  ARG D CD  1 
ATOM   7085  N NE  . ARG D 2 75  ? 14.731  41.906  40.491  1.00 73.24  ? 75  ARG D NE  1 
ATOM   7086  C CZ  . ARG D 2 75  ? 14.441  41.830  41.783  1.00 71.77  ? 75  ARG D CZ  1 
ATOM   7087  N NH1 . ARG D 2 75  ? 14.074  40.690  42.345  1.00 74.48  ? 75  ARG D NH1 1 
ATOM   7088  N NH2 . ARG D 2 75  ? 14.522  42.927  42.532  1.00 85.41  ? 75  ARG D NH2 1 
ATOM   7089  N N   . ARG D 2 76  ? 15.240  37.507  35.292  1.00 42.23  ? 76  ARG D N   1 
ATOM   7090  C CA  . ARG D 2 76  ? 14.756  36.883  34.064  1.00 37.44  ? 76  ARG D CA  1 
ATOM   7091  C C   . ARG D 2 76  ? 13.783  35.751  34.368  1.00 39.91  ? 76  ARG D C   1 
ATOM   7092  O O   . ARG D 2 76  ? 12.782  35.575  33.663  1.00 48.89  ? 76  ARG D O   1 
ATOM   7093  C CB  . ARG D 2 76  ? 15.929  36.364  33.236  1.00 45.07  ? 76  ARG D CB  1 
ATOM   7094  C CG  . ARG D 2 76  ? 16.670  37.425  32.453  1.00 40.21  ? 76  ARG D CG  1 
ATOM   7095  C CD  . ARG D 2 76  ? 17.973  36.865  31.885  1.00 47.12  ? 76  ARG D CD  1 
ATOM   7096  N NE  . ARG D 2 76  ? 18.731  36.098  32.869  1.00 33.93  ? 76  ARG D NE  1 
ATOM   7097  C CZ  . ARG D 2 76  ? 19.390  34.978  32.598  1.00 42.95  ? 76  ARG D CZ  1 
ATOM   7098  N NH1 . ARG D 2 76  ? 19.411  34.466  31.378  1.00 33.59  ? 76  ARG D NH1 1 
ATOM   7099  N NH2 . ARG D 2 76  ? 20.045  34.356  33.577  1.00 30.44  ? 76  ARG D NH2 1 
ATOM   7100  N N   . ILE D 2 77  ? 14.069  34.959  35.405  1.00 47.66  ? 77  ILE D N   1 
ATOM   7101  C CA  . ILE D 2 77  ? 13.157  33.885  35.785  1.00 48.41  ? 77  ILE D CA  1 
ATOM   7102  C C   . ILE D 2 77  ? 11.862  34.457  36.342  1.00 49.24  ? 77  ILE D C   1 
ATOM   7103  O O   . ILE D 2 77  ? 10.771  33.953  36.047  1.00 42.41  ? 77  ILE D O   1 
ATOM   7104  C CB  . ILE D 2 77  ? 13.824  32.935  36.791  1.00 48.17  ? 77  ILE D CB  1 
ATOM   7105  C CG1 . ILE D 2 77  ? 15.081  32.329  36.184  1.00 44.23  ? 77  ILE D CG1 1 
ATOM   7106  C CG2 . ILE D 2 77  ? 12.869  31.820  37.161  1.00 44.00  ? 77  ILE D CG2 1 
ATOM   7107  C CD1 . ILE D 2 77  ? 14.797  31.544  34.942  1.00 58.30  ? 77  ILE D CD1 1 
ATOM   7108  N N   . GLU D 2 78  ? 11.958  35.506  37.165  1.00 43.32  ? 78  GLU D N   1 
ATOM   7109  C CA  . GLU D 2 78  ? 10.746  36.110  37.709  1.00 45.89  ? 78  GLU D CA  1 
ATOM   7110  C C   . GLU D 2 78  ? 9.885   36.701  36.603  1.00 45.33  ? 78  GLU D C   1 
ATOM   7111  O O   . GLU D 2 78  ? 8.652   36.663  36.688  1.00 52.66  ? 78  GLU D O   1 
ATOM   7112  C CB  . GLU D 2 78  ? 11.095  37.176  38.751  1.00 42.38  ? 78  GLU D CB  1 
ATOM   7113  C CG  . GLU D 2 78  ? 9.903   37.693  39.553  1.00 49.66  ? 78  GLU D CG  1 
ATOM   7114  C CD  . GLU D 2 78  ? 8.844   36.618  39.831  1.00 74.82  ? 78  GLU D CD  1 
ATOM   7115  O OE1 . GLU D 2 78  ? 7.673   36.802  39.413  1.00 54.96  ? 78  GLU D OE1 1 
ATOM   7116  O OE2 . GLU D 2 78  ? 9.177   35.599  40.482  1.00 59.26  ? 78  GLU D OE2 1 
ATOM   7117  N N   . ASN D 2 79  ? 10.510  37.243  35.557  1.00 38.84  ? 79  ASN D N   1 
ATOM   7118  C CA  . ASN D 2 79  ? 9.734   37.723  34.423  1.00 48.88  ? 79  ASN D CA  1 
ATOM   7119  C C   . ASN D 2 79  ? 9.043   36.577  33.699  1.00 50.78  ? 79  ASN D C   1 
ATOM   7120  O O   . ASN D 2 79  ? 7.956   36.763  33.139  1.00 41.87  ? 79  ASN D O   1 
ATOM   7121  C CB  . ASN D 2 79  ? 10.621  38.494  33.454  1.00 42.58  ? 79  ASN D CB  1 
ATOM   7122  C CG  . ASN D 2 79  ? 9.820   39.194  32.393  1.00 38.81  ? 79  ASN D CG  1 
ATOM   7123  O OD1 . ASN D 2 79  ? 10.007  38.966  31.198  1.00 52.24  ? 79  ASN D OD1 1 
ATOM   7124  N ND2 . ASN D 2 79  ? 8.890   40.030  32.823  1.00 40.41  ? 79  ASN D ND2 1 
ATOM   7125  N N   . LEU D 2 80  ? 9.663   35.396  33.683  1.00 40.99  ? 80  LEU D N   1 
ATOM   7126  C CA  . LEU D 2 80  ? 9.001   34.227  33.117  1.00 45.85  ? 80  LEU D CA  1 
ATOM   7127  C C   . LEU D 2 80  ? 7.762   33.858  33.926  1.00 47.22  ? 80  LEU D C   1 
ATOM   7128  O O   . LEU D 2 80  ? 6.710   33.545  33.356  1.00 35.91  ? 80  LEU D O   1 
ATOM   7129  C CB  . LEU D 2 80  ? 9.985   33.057  33.042  1.00 38.36  ? 80  LEU D CB  1 
ATOM   7130  C CG  . LEU D 2 80  ? 9.448   31.700  32.576  1.00 52.22  ? 80  LEU D CG  1 
ATOM   7131  C CD1 . LEU D 2 80  ? 8.708   31.817  31.248  1.00 47.19  ? 80  LEU D CD1 1 
ATOM   7132  C CD2 . LEU D 2 80  ? 10.575  30.683  32.467  1.00 42.77  ? 80  LEU D CD2 1 
ATOM   7133  N N   . ASN D 2 81  ? 7.863   33.906  35.259  1.00 37.49  ? 81  ASN D N   1 
ATOM   7134  C CA  . ASN D 2 81  ? 6.710   33.611  36.107  1.00 39.41  ? 81  ASN D CA  1 
ATOM   7135  C C   . ASN D 2 81  ? 5.634   34.681  35.971  1.00 46.36  ? 81  ASN D C   1 
ATOM   7136  O O   . ASN D 2 81  ? 4.434   34.374  35.998  1.00 42.21  ? 81  ASN D O   1 
ATOM   7137  C CB  . ASN D 2 81  ? 7.152   33.476  37.563  1.00 37.77  ? 81  ASN D CB  1 
ATOM   7138  C CG  . ASN D 2 81  ? 5.981   33.431  38.526  1.00 38.42  ? 81  ASN D CG  1 
ATOM   7139  O OD1 . ASN D 2 81  ? 5.271   32.429  38.613  1.00 56.97  ? 81  ASN D OD1 1 
ATOM   7140  N ND2 . ASN D 2 81  ? 5.772   34.522  39.254  1.00 46.79  ? 81  ASN D ND2 1 
ATOM   7141  N N   . LYS D 2 82  ? 6.045   35.943  35.833  1.00 45.27  ? 82  LYS D N   1 
ATOM   7142  C CA  . LYS D 2 82  ? 5.085   37.022  35.632  1.00 40.64  ? 82  LYS D CA  1 
ATOM   7143  C C   . LYS D 2 82  ? 4.307   36.833  34.337  1.00 42.14  ? 82  LYS D C   1 
ATOM   7144  O O   . LYS D 2 82  ? 3.084   37.009  34.307  1.00 39.07  ? 82  LYS D O   1 
ATOM   7145  C CB  . LYS D 2 82  ? 5.812   38.367  35.632  1.00 42.02  ? 82  LYS D CB  1 
ATOM   7146  C CG  . LYS D 2 82  ? 5.081   39.486  34.896  1.00 44.64  ? 82  LYS D CG  1 
ATOM   7147  C CD  . LYS D 2 82  ? 5.370   40.829  35.540  1.00 41.42  ? 82  LYS D CD  1 
ATOM   7148  C CE  . LYS D 2 82  ? 4.330   41.873  35.152  1.00 44.05  ? 82  LYS D CE  1 
ATOM   7149  N NZ  . LYS D 2 82  ? 4.485   42.274  33.732  1.00 48.26  ? 82  LYS D NZ  1 
ATOM   7150  N N   . LYS D 2 83  ? 4.999   36.467  33.256  1.00 43.79  ? 83  LYS D N   1 
ATOM   7151  C CA  . LYS D 2 83  ? 4.318   36.248  31.986  1.00 44.94  ? 83  LYS D CA  1 
ATOM   7152  C C   . LYS D 2 83  ? 3.352   35.076  32.079  1.00 44.35  ? 83  LYS D C   1 
ATOM   7153  O O   . LYS D 2 83  ? 2.283   35.091  31.459  1.00 50.33  ? 83  LYS D O   1 
ATOM   7154  C CB  . LYS D 2 83  ? 5.338   36.016  30.872  1.00 38.56  ? 83  LYS D CB  1 
ATOM   7155  C CG  . LYS D 2 83  ? 6.040   37.281  30.417  1.00 38.00  ? 83  LYS D CG  1 
ATOM   7156  C CD  . LYS D 2 83  ? 6.916   37.019  29.198  1.00 30.19  ? 83  LYS D CD  1 
ATOM   7157  C CE  . LYS D 2 83  ? 8.210   36.330  29.587  1.00 35.22  ? 83  LYS D CE  1 
ATOM   7158  N NZ  . LYS D 2 83  ? 8.890   35.729  28.406  1.00 47.92  ? 83  LYS D NZ  1 
ATOM   7159  N N   . MET D 2 84  ? 3.706   34.048  32.852  1.00 45.64  ? 84  MET D N   1 
ATOM   7160  C CA  . MET D 2 84  ? 2.788   32.932  33.028  1.00 37.51  ? 84  MET D CA  1 
ATOM   7161  C C   . MET D 2 84  ? 1.600   33.327  33.899  1.00 45.23  ? 84  MET D C   1 
ATOM   7162  O O   . MET D 2 84  ? 0.453   33.001  33.573  1.00 52.58  ? 84  MET D O   1 
ATOM   7163  C CB  . MET D 2 84  ? 3.525   31.733  33.618  1.00 44.34  ? 84  MET D CB  1 
ATOM   7164  C CG  . MET D 2 84  ? 2.593   30.635  34.096  1.00 49.59  ? 84  MET D CG  1 
ATOM   7165  S SD  . MET D 2 84  ? 3.268   29.706  35.478  1.00 57.57  ? 84  MET D SD  1 
ATOM   7166  C CE  . MET D 2 84  ? 2.451   30.535  36.849  1.00 48.96  ? 84  MET D CE  1 
ATOM   7167  N N   . GLU D 2 85  ? 1.850   34.042  35.002  1.00 51.07  ? 85  GLU D N   1 
ATOM   7168  C CA  . GLU D 2 85  ? 0.759   34.474  35.875  1.00 43.41  ? 85  GLU D CA  1 
ATOM   7169  C C   . GLU D 2 85  ? -0.213  35.375  35.129  1.00 41.78  ? 85  GLU D C   1 
ATOM   7170  O O   . GLU D 2 85  ? -1.437  35.211  35.219  1.00 47.58  ? 85  GLU D O   1 
ATOM   7171  C CB  . GLU D 2 85  ? 1.319   35.209  37.093  1.00 41.61  ? 85  GLU D CB  1 
ATOM   7172  C CG  . GLU D 2 85  ? 1.561   34.346  38.315  1.00 51.15  ? 85  GLU D CG  1 
ATOM   7173  C CD  . GLU D 2 85  ? 1.979   35.166  39.524  1.00 52.94  ? 85  GLU D CD  1 
ATOM   7174  O OE1 . GLU D 2 85  ? 1.694   36.384  39.546  1.00 62.91  ? 85  GLU D OE1 1 
ATOM   7175  O OE2 . GLU D 2 85  ? 2.593   34.599  40.451  1.00 43.36  ? 85  GLU D OE2 1 
ATOM   7176  N N   . ASP D 2 86  ? 0.324   36.337  34.385  1.00 40.24  ? 86  ASP D N   1 
ATOM   7177  C CA  . ASP D 2 86  ? -0.512  37.265  33.638  1.00 44.09  ? 86  ASP D CA  1 
ATOM   7178  C C   . ASP D 2 86  ? -1.259  36.559  32.517  1.00 43.68  ? 86  ASP D C   1 
ATOM   7179  O O   . ASP D 2 86  ? -2.410  36.899  32.219  1.00 47.53  ? 86  ASP D O   1 
ATOM   7180  C CB  . ASP D 2 86  ? 0.354   38.398  33.096  1.00 52.08  ? 86  ASP D CB  1 
ATOM   7181  C CG  . ASP D 2 86  ? 0.941   39.252  34.200  1.00 53.20  ? 86  ASP D CG  1 
ATOM   7182  O OD1 . ASP D 2 86  ? 0.518   39.086  35.366  1.00 57.44  ? 86  ASP D OD1 1 
ATOM   7183  O OD2 . ASP D 2 86  ? 1.811   40.096  33.907  1.00 47.52  ? 86  ASP D OD2 1 
ATOM   7184  N N   . GLY D 2 87  ? -0.625  35.571  31.885  1.00 43.84  ? 87  GLY D N   1 
ATOM   7185  C CA  . GLY D 2 87  ? -1.304  34.823  30.842  1.00 42.49  ? 87  GLY D CA  1 
ATOM   7186  C C   . GLY D 2 87  ? -2.520  34.080  31.361  1.00 47.04  ? 87  GLY D C   1 
ATOM   7187  O O   . GLY D 2 87  ? -3.590  34.116  30.748  1.00 42.64  ? 87  GLY D O   1 
ATOM   7188  N N   . PHE D 2 88  ? -2.379  33.411  32.507  1.00 43.13  ? 88  PHE D N   1 
ATOM   7189  C CA  . PHE D 2 88  ? -3.506  32.674  33.069  1.00 43.33  ? 88  PHE D CA  1 
ATOM   7190  C C   . PHE D 2 88  ? -4.597  33.619  33.558  1.00 46.15  ? 88  PHE D C   1 
ATOM   7191  O O   . PHE D 2 88  ? -5.789  33.315  33.431  1.00 42.78  ? 88  PHE D O   1 
ATOM   7192  C CB  . PHE D 2 88  ? -3.030  31.766  34.200  1.00 36.11  ? 88  PHE D CB  1 
ATOM   7193  C CG  . PHE D 2 88  ? -2.354  30.524  33.721  1.00 41.76  ? 88  PHE D CG  1 
ATOM   7194  C CD1 . PHE D 2 88  ? -2.969  29.704  32.789  1.00 41.21  ? 88  PHE D CD1 1 
ATOM   7195  C CD2 . PHE D 2 88  ? -1.099  30.179  34.187  1.00 38.89  ? 88  PHE D CD2 1 
ATOM   7196  C CE1 . PHE D 2 88  ? -2.346  28.555  32.334  1.00 41.87  ? 88  PHE D CE1 1 
ATOM   7197  C CE2 . PHE D 2 88  ? -0.472  29.030  33.738  1.00 43.54  ? 88  PHE D CE2 1 
ATOM   7198  C CZ  . PHE D 2 88  ? -1.094  28.219  32.812  1.00 46.95  ? 88  PHE D CZ  1 
ATOM   7199  N N   . LEU D 2 89  ? -4.216  34.767  34.123  1.00 41.86  ? 89  LEU D N   1 
ATOM   7200  C CA  . LEU D 2 89  ? -5.225  35.743  34.518  1.00 46.28  ? 89  LEU D CA  1 
ATOM   7201  C C   . LEU D 2 89  ? -5.995  36.252  33.305  1.00 41.62  ? 89  LEU D C   1 
ATOM   7202  O O   . LEU D 2 89  ? -7.220  36.407  33.355  1.00 47.11  ? 89  LEU D O   1 
ATOM   7203  C CB  . LEU D 2 89  ? -4.577  36.906  35.271  1.00 36.97  ? 89  LEU D CB  1 
ATOM   7204  C CG  . LEU D 2 89  ? -5.550  38.015  35.690  1.00 50.54  ? 89  LEU D CG  1 
ATOM   7205  C CD1 . LEU D 2 89  ? -5.443  38.293  37.172  1.00 48.03  ? 89  LEU D CD1 1 
ATOM   7206  C CD2 . LEU D 2 89  ? -5.322  39.294  34.889  1.00 47.16  ? 89  LEU D CD2 1 
ATOM   7207  N N   . ASP D 2 90  ? -5.288  36.513  32.203  1.00 42.57  ? 90  ASP D N   1 
ATOM   7208  C CA  . ASP D 2 90  ? -5.949  36.973  30.987  1.00 42.01  ? 90  ASP D CA  1 
ATOM   7209  C C   . ASP D 2 90  ? -6.878  35.906  30.420  1.00 40.67  ? 90  ASP D C   1 
ATOM   7210  O O   . ASP D 2 90  ? -7.979  36.221  29.952  1.00 43.28  ? 90  ASP D O   1 
ATOM   7211  C CB  . ASP D 2 90  ? -4.905  37.380  29.947  1.00 46.92  ? 90  ASP D CB  1 
ATOM   7212  C CG  . ASP D 2 90  ? -4.181  38.661  30.318  1.00 61.41  ? 90  ASP D CG  1 
ATOM   7213  O OD1 . ASP D 2 90  ? -4.683  39.394  31.198  1.00 60.72  ? 90  ASP D OD1 1 
ATOM   7214  O OD2 . ASP D 2 90  ? -3.114  38.936  29.727  1.00 60.78  ? 90  ASP D OD2 1 
ATOM   7215  N N   . VAL D 2 91  ? -6.445  34.641  30.434  1.00 34.39  ? 91  VAL D N   1 
ATOM   7216  C CA  . VAL D 2 91  ? -7.289  33.563  29.920  1.00 37.85  ? 91  VAL D CA  1 
ATOM   7217  C C   . VAL D 2 91  ? -8.550  33.432  30.762  1.00 42.07  ? 91  VAL D C   1 
ATOM   7218  O O   . VAL D 2 91  ? -9.672  33.456  30.241  1.00 40.86  ? 91  VAL D O   1 
ATOM   7219  C CB  . VAL D 2 91  ? -6.511  32.236  29.884  1.00 39.76  ? 91  VAL D CB  1 
ATOM   7220  C CG1 . VAL D 2 91  ? -7.473  31.069  29.667  1.00 28.42  ? 91  VAL D CG1 1 
ATOM   7221  C CG2 . VAL D 2 91  ? -5.433  32.263  28.808  1.00 30.31  ? 91  VAL D CG2 1 
ATOM   7222  N N   . TRP D 2 92  ? -8.383  33.323  32.082  1.00 38.39  ? 92  TRP D N   1 
ATOM   7223  C CA  . TRP D 2 92  ? -9.522  33.079  32.960  1.00 38.92  ? 92  TRP D CA  1 
ATOM   7224  C C   . TRP D 2 92  ? -10.491 34.255  32.969  1.00 39.85  ? 92  TRP D C   1 
ATOM   7225  O O   . TRP D 2 92  ? -11.711 34.055  32.956  1.00 38.59  ? 92  TRP D O   1 
ATOM   7226  C CB  . TRP D 2 92  ? -9.038  32.770  34.376  1.00 36.96  ? 92  TRP D CB  1 
ATOM   7227  C CG  . TRP D 2 92  ? -8.499  31.379  34.541  1.00 40.58  ? 92  TRP D CG  1 
ATOM   7228  C CD1 . TRP D 2 92  ? -7.248  31.034  34.957  1.00 34.21  ? 92  TRP D CD1 1 
ATOM   7229  C CD2 . TRP D 2 92  ? -9.194  30.143  34.295  1.00 38.44  ? 92  TRP D CD2 1 
ATOM   7230  N NE1 . TRP D 2 92  ? -7.118  29.667  34.990  1.00 45.75  ? 92  TRP D NE1 1 
ATOM   7231  C CE2 . TRP D 2 92  ? -8.296  29.096  34.586  1.00 39.78  ? 92  TRP D CE2 1 
ATOM   7232  C CE3 . TRP D 2 92  ? -10.486 29.822  33.858  1.00 43.74  ? 92  TRP D CE3 1 
ATOM   7233  C CZ2 . TRP D 2 92  ? -8.647  27.749  34.455  1.00 42.16  ? 92  TRP D CZ2 1 
ATOM   7234  C CZ3 . TRP D 2 92  ? -10.835 28.482  33.729  1.00 31.76  ? 92  TRP D CZ3 1 
ATOM   7235  C CH2 . TRP D 2 92  ? -9.917  27.464  34.025  1.00 36.89  ? 92  TRP D CH2 1 
ATOM   7236  N N   . THR D 2 93  ? -9.972  35.484  32.995  1.00 41.94  ? 93  THR D N   1 
ATOM   7237  C CA  . THR D 2 93  ? -10.845 36.655  33.035  1.00 35.61  ? 93  THR D CA  1 
ATOM   7238  C C   . THR D 2 93  ? -11.696 36.754  31.776  1.00 41.03  ? 93  THR D C   1 
ATOM   7239  O O   . THR D 2 93  ? -12.906 36.999  31.850  1.00 46.84  ? 93  THR D O   1 
ATOM   7240  C CB  . THR D 2 93  ? -10.022 37.933  33.225  1.00 36.75  ? 93  THR D CB  1 
ATOM   7241  O OG1 . THR D 2 93  ? -8.945  37.687  34.136  1.00 33.18  ? 93  THR D OG1 1 
ATOM   7242  C CG2 . THR D 2 93  ? -10.881 39.056  33.749  1.00 47.45  ? 93  THR D CG2 1 
ATOM   7243  N N   . TYR D 2 94  ? -11.076 36.574  30.607  1.00 44.50  ? 94  TYR D N   1 
ATOM   7244  C CA  . TYR D 2 94  ? -11.818 36.664  29.352  1.00 44.24  ? 94  TYR D CA  1 
ATOM   7245  C C   . TYR D 2 94  ? -12.866 35.562  29.259  1.00 40.10  ? 94  TYR D C   1 
ATOM   7246  O O   . TYR D 2 94  ? -14.018 35.812  28.885  1.00 47.98  ? 94  TYR D O   1 
ATOM   7247  C CB  . TYR D 2 94  ? -10.850 36.589  28.173  1.00 41.48  ? 94  TYR D CB  1 
ATOM   7248  C CG  . TYR D 2 94  ? -11.448 36.943  26.833  1.00 43.52  ? 94  TYR D CG  1 
ATOM   7249  C CD1 . TYR D 2 94  ? -11.867 38.240  26.553  1.00 46.07  ? 94  TYR D CD1 1 
ATOM   7250  C CD2 . TYR D 2 94  ? -11.580 35.983  25.838  1.00 40.44  ? 94  TYR D CD2 1 
ATOM   7251  C CE1 . TYR D 2 94  ? -12.409 38.568  25.315  1.00 42.47  ? 94  TYR D CE1 1 
ATOM   7252  C CE2 . TYR D 2 94  ? -12.118 36.299  24.602  1.00 43.15  ? 94  TYR D CE2 1 
ATOM   7253  C CZ  . TYR D 2 94  ? -12.531 37.590  24.345  1.00 50.30  ? 94  TYR D CZ  1 
ATOM   7254  O OH  . TYR D 2 94  ? -13.066 37.894  23.114  1.00 48.72  ? 94  TYR D OH  1 
ATOM   7255  N N   . ASN D 2 95  ? -12.480 34.332  29.608  1.00 35.29  ? 95  ASN D N   1 
ATOM   7256  C CA  . ASN D 2 95  ? -13.404 33.209  29.512  1.00 46.21  ? 95  ASN D CA  1 
ATOM   7257  C C   . ASN D 2 95  ? -14.560 33.357  30.494  1.00 47.39  ? 95  ASN D C   1 
ATOM   7258  O O   . ASN D 2 95  ? -15.718 33.122  30.135  1.00 45.85  ? 95  ASN D O   1 
ATOM   7259  C CB  . ASN D 2 95  ? -12.653 31.900  29.749  1.00 50.10  ? 95  ASN D CB  1 
ATOM   7260  C CG  . ASN D 2 95  ? -11.868 31.450  28.525  1.00 73.13  ? 95  ASN D CG  1 
ATOM   7261  O OD1 . ASN D 2 95  ? -11.850 32.135  27.497  1.00 48.35  ? 95  ASN D OD1 1 
ATOM   7262  N ND2 . ASN D 2 95  ? -11.218 30.290  28.628  1.00 68.67  ? 95  ASN D ND2 1 
ATOM   7263  N N   . ALA D 2 96  ? -14.269 33.764  31.731  1.00 45.88  ? 96  ALA D N   1 
ATOM   7264  C CA  . ALA D 2 96  ? -15.323 33.898  32.732  1.00 41.74  ? 96  ALA D CA  1 
ATOM   7265  C C   . ALA D 2 96  ? -16.286 35.028  32.388  1.00 48.18  ? 96  ALA D C   1 
ATOM   7266  O O   . ALA D 2 96  ? -17.502 34.889  32.565  1.00 47.79  ? 96  ALA D O   1 
ATOM   7267  C CB  . ALA D 2 96  ? -14.707 34.113  34.114  1.00 34.50  ? 96  ALA D CB  1 
ATOM   7268  N N   . GLU D 2 97  ? -15.767 36.161  31.909  1.00 45.65  ? 97  GLU D N   1 
ATOM   7269  C CA  . GLU D 2 97  ? -16.649 37.270  31.560  1.00 40.34  ? 97  GLU D CA  1 
ATOM   7270  C C   . GLU D 2 97  ? -17.553 36.906  30.393  1.00 35.36  ? 97  GLU D C   1 
ATOM   7271  O O   . GLU D 2 97  ? -18.743 37.237  30.393  1.00 50.58  ? 97  GLU D O   1 
ATOM   7272  C CB  . GLU D 2 97  ? -15.833 38.522  31.234  1.00 38.39  ? 97  GLU D CB  1 
ATOM   7273  C CG  . GLU D 2 97  ? -15.209 39.198  32.454  1.00 53.83  ? 97  GLU D CG  1 
ATOM   7274  C CD  . GLU D 2 97  ? -16.203 40.020  33.265  1.00 59.56  ? 97  GLU D CD  1 
ATOM   7275  O OE1 . GLU D 2 97  ? -17.362 40.190  32.825  1.00 61.07  ? 97  GLU D OE1 1 
ATOM   7276  O OE2 . GLU D 2 97  ? -15.816 40.498  34.353  1.00 69.06  ? 97  GLU D OE2 1 
ATOM   7277  N N   . LEU D 2 98  ? -17.006 36.224  29.386  1.00 43.73  ? 98  LEU D N   1 
ATOM   7278  C CA  . LEU D 2 98  ? -17.806 35.864  28.222  1.00 46.67  ? 98  LEU D CA  1 
ATOM   7279  C C   . LEU D 2 98  ? -18.743 34.697  28.509  1.00 42.27  ? 98  LEU D C   1 
ATOM   7280  O O   . LEU D 2 98  ? -19.864 34.666  27.982  1.00 44.15  ? 98  LEU D O   1 
ATOM   7281  C CB  . LEU D 2 98  ? -16.893 35.545  27.039  1.00 40.28  ? 98  LEU D CB  1 
ATOM   7282  C CG  . LEU D 2 98  ? -16.348 36.790  26.335  1.00 41.05  ? 98  LEU D CG  1 
ATOM   7283  C CD1 . LEU D 2 98  ? -15.832 36.435  24.965  1.00 43.60  ? 98  LEU D CD1 1 
ATOM   7284  C CD2 . LEU D 2 98  ? -17.407 37.873  26.232  1.00 39.61  ? 98  LEU D CD2 1 
ATOM   7285  N N   . LEU D 2 99  ? -18.321 33.750  29.349  1.00 27.89  ? 99  LEU D N   1 
ATOM   7286  C CA  . LEU D 2 99  ? -19.210 32.661  29.735  1.00 36.90  ? 99  LEU D CA  1 
ATOM   7287  C C   . LEU D 2 99  ? -20.440 33.195  30.458  1.00 50.12  ? 99  LEU D C   1 
ATOM   7288  O O   . LEU D 2 99  ? -21.565 32.761  30.185  1.00 39.39  ? 99  LEU D O   1 
ATOM   7289  C CB  . LEU D 2 99  ? -18.461 31.655  30.608  1.00 39.71  ? 99  LEU D CB  1 
ATOM   7290  C CG  . LEU D 2 99  ? -19.292 30.585  31.312  1.00 47.90  ? 99  LEU D CG  1 
ATOM   7291  C CD1 . LEU D 2 99  ? -19.709 29.505  30.331  1.00 42.68  ? 99  LEU D CD1 1 
ATOM   7292  C CD2 . LEU D 2 99  ? -18.492 29.984  32.456  1.00 44.25  ? 99  LEU D CD2 1 
ATOM   7293  N N   . VAL D 2 100 ? -20.246 34.159  31.364  1.00 41.92  ? 100 VAL D N   1 
ATOM   7294  C CA  . VAL D 2 100 ? -21.378 34.787  32.043  1.00 44.80  ? 100 VAL D CA  1 
ATOM   7295  C C   . VAL D 2 100 ? -22.264 35.504  31.032  1.00 37.85  ? 100 VAL D C   1 
ATOM   7296  O O   . VAL D 2 100 ? -23.493 35.382  31.061  1.00 45.45  ? 100 VAL D O   1 
ATOM   7297  C CB  . VAL D 2 100 ? -20.881 35.750  33.139  1.00 45.54  ? 100 VAL D CB  1 
ATOM   7298  C CG1 . VAL D 2 100 ? -21.967 36.751  33.523  1.00 31.80  ? 100 VAL D CG1 1 
ATOM   7299  C CG2 . VAL D 2 100 ? -20.405 34.977  34.358  1.00 39.67  ? 100 VAL D CG2 1 
ATOM   7300  N N   . LEU D 2 101 ? -21.651 36.257  30.114  1.00 40.71  ? 101 LEU D N   1 
ATOM   7301  C CA  . LEU D 2 101 ? -22.430 36.980  29.113  1.00 44.12  ? 101 LEU D CA  1 
ATOM   7302  C C   . LEU D 2 101 ? -23.207 36.022  28.216  1.00 45.49  ? 101 LEU D C   1 
ATOM   7303  O O   . LEU D 2 101 ? -24.379 36.264  27.905  1.00 43.91  ? 101 LEU D O   1 
ATOM   7304  C CB  . LEU D 2 101 ? -21.513 37.871  28.274  1.00 41.91  ? 101 LEU D CB  1 
ATOM   7305  C CG  . LEU D 2 101 ? -20.931 39.132  28.918  1.00 52.06  ? 101 LEU D CG  1 
ATOM   7306  C CD1 . LEU D 2 101 ? -20.415 40.069  27.839  1.00 38.29  ? 101 LEU D CD1 1 
ATOM   7307  C CD2 . LEU D 2 101 ? -21.958 39.832  29.795  1.00 36.43  ? 101 LEU D CD2 1 
ATOM   7308  N N   . MET D 2 102 ? -22.565 34.934  27.784  1.00 47.98  ? 102 MET D N   1 
ATOM   7309  C CA  . MET D 2 102 ? -23.221 33.993  26.881  1.00 38.51  ? 102 MET D CA  1 
ATOM   7310  C C   . MET D 2 102 ? -24.314 33.210  27.595  1.00 37.49  ? 102 MET D C   1 
ATOM   7311  O O   . MET D 2 102 ? -25.411 33.028  27.055  1.00 46.98  ? 102 MET D O   1 
ATOM   7312  C CB  . MET D 2 102 ? -22.186 33.042  26.283  1.00 44.65  ? 102 MET D CB  1 
ATOM   7313  C CG  . MET D 2 102 ? -21.661 33.453  24.914  1.00 49.22  ? 102 MET D CG  1 
ATOM   7314  S SD  . MET D 2 102 ? -19.915 33.028  24.732  1.00 60.20  ? 102 MET D SD  1 
ATOM   7315  C CE  . MET D 2 102 ? -20.008 31.247  24.812  1.00 49.38  ? 102 MET D CE  1 
ATOM   7316  N N   . GLU D 2 103 ? -24.036 32.738  28.813  1.00 38.75  ? 103 GLU D N   1 
ATOM   7317  C CA  . GLU D 2 103 ? -25.029 31.964  29.544  1.00 38.33  ? 103 GLU D CA  1 
ATOM   7318  C C   . GLU D 2 103 ? -26.173 32.828  30.056  1.00 47.79  ? 103 GLU D C   1 
ATOM   7319  O O   . GLU D 2 103 ? -27.275 32.312  30.264  1.00 45.86  ? 103 GLU D O   1 
ATOM   7320  C CB  . GLU D 2 103 ? -24.368 31.211  30.700  1.00 44.00  ? 103 GLU D CB  1 
ATOM   7321  C CG  . GLU D 2 103 ? -23.620 29.937  30.268  1.00 46.61  ? 103 GLU D CG  1 
ATOM   7322  C CD  . GLU D 2 103 ? -24.503 28.939  29.516  1.00 65.90  ? 103 GLU D CD  1 
ATOM   7323  O OE1 . GLU D 2 103 ? -25.711 28.831  29.831  1.00 60.31  ? 103 GLU D OE1 1 
ATOM   7324  O OE2 . GLU D 2 103 ? -23.986 28.253  28.607  1.00 63.72  ? 103 GLU D OE2 1 
ATOM   7325  N N   . ASN D 2 104 ? -25.947 34.128  30.261  1.00 44.62  ? 104 ASN D N   1 
ATOM   7326  C CA  . ASN D 2 104 ? -27.057 35.006  30.615  1.00 38.14  ? 104 ASN D CA  1 
ATOM   7327  C C   . ASN D 2 104 ? -28.022 35.157  29.447  1.00 43.45  ? 104 ASN D C   1 
ATOM   7328  O O   . ASN D 2 104 ? -29.243 35.163  29.640  1.00 40.76  ? 104 ASN D O   1 
ATOM   7329  C CB  . ASN D 2 104 ? -26.531 36.365  31.067  1.00 32.49  ? 104 ASN D CB  1 
ATOM   7330  C CG  . ASN D 2 104 ? -26.051 36.354  32.516  1.00 44.88  ? 104 ASN D CG  1 
ATOM   7331  O OD1 . ASN D 2 104 ? -26.187 35.354  33.222  1.00 40.64  ? 104 ASN D OD1 1 
ATOM   7332  N ND2 . ASN D 2 104 ? -25.473 37.465  32.957  1.00 44.60  ? 104 ASN D ND2 1 
ATOM   7333  N N   . GLU D 2 105 ? -27.495 35.269  28.226  1.00 43.46  ? 105 GLU D N   1 
ATOM   7334  C CA  . GLU D 2 105 ? -28.366 35.309  27.056  1.00 46.96  ? 105 GLU D CA  1 
ATOM   7335  C C   . GLU D 2 105 ? -29.180 34.026  26.940  1.00 47.13  ? 105 GLU D C   1 
ATOM   7336  O O   . GLU D 2 105 ? -30.391 34.069  26.694  1.00 56.69  ? 105 GLU D O   1 
ATOM   7337  C CB  . GLU D 2 105 ? -27.537 35.537  25.793  1.00 46.35  ? 105 GLU D CB  1 
ATOM   7338  C CG  . GLU D 2 105 ? -28.325 36.100  24.623  1.00 54.55  ? 105 GLU D CG  1 
ATOM   7339  C CD  . GLU D 2 105 ? -28.563 37.594  24.750  1.00 75.04  ? 105 GLU D CD  1 
ATOM   7340  O OE1 . GLU D 2 105 ? -27.577 38.357  24.658  1.00 74.47  ? 105 GLU D OE1 1 
ATOM   7341  O OE2 . GLU D 2 105 ? -29.733 38.004  24.934  1.00 71.18  ? 105 GLU D OE2 1 
ATOM   7342  N N   . ARG D 2 106 ? -28.532 32.874  27.138  1.00 44.31  ? 106 ARG D N   1 
ATOM   7343  C CA  . ARG D 2 106 ? -29.223 31.593  27.029  1.00 41.98  ? 106 ARG D CA  1 
ATOM   7344  C C   . ARG D 2 106 ? -30.312 31.449  28.085  1.00 40.54  ? 106 ARG D C   1 
ATOM   7345  O O   . ARG D 2 106 ? -31.416 30.977  27.787  1.00 37.05  ? 106 ARG D O   1 
ATOM   7346  C CB  . ARG D 2 106 ? -28.217 30.448  27.144  1.00 46.62  ? 106 ARG D CB  1 
ATOM   7347  C CG  . ARG D 2 106 ? -27.095 30.505  26.120  1.00 55.68  ? 106 ARG D CG  1 
ATOM   7348  C CD  . ARG D 2 106 ? -27.574 30.032  24.767  1.00 61.69  ? 106 ARG D CD  1 
ATOM   7349  N NE  . ARG D 2 106 ? -27.899 28.610  24.767  1.00 80.76  ? 106 ARG D NE  1 
ATOM   7350  C CZ  . ARG D 2 106 ? -28.924 28.074  24.117  1.00 78.57  ? 106 ARG D CZ  1 
ATOM   7351  N NH1 . ARG D 2 106 ? -29.752 28.816  23.397  1.00 79.59  ? 106 ARG D NH1 1 
ATOM   7352  N NH2 . ARG D 2 106 ? -29.122 26.760  24.189  1.00 56.03  ? 106 ARG D NH2 1 
ATOM   7353  N N   . THR D 2 107 ? -30.020 31.844  29.325  1.00 31.73  ? 107 THR D N   1 
ATOM   7354  C CA  . THR D 2 107 ? -31.005 31.693  30.390  1.00 40.10  ? 107 THR D CA  1 
ATOM   7355  C C   . THR D 2 107 ? -32.258 32.516  30.108  1.00 44.10  ? 107 THR D C   1 
ATOM   7356  O O   . THR D 2 107 ? -33.380 32.032  30.297  1.00 42.22  ? 107 THR D O   1 
ATOM   7357  C CB  . THR D 2 107 ? -30.390 32.086  31.730  1.00 40.54  ? 107 THR D CB  1 
ATOM   7358  O OG1 . THR D 2 107 ? -29.422 31.100  32.113  1.00 40.81  ? 107 THR D OG1 1 
ATOM   7359  C CG2 . THR D 2 107 ? -31.463 32.173  32.802  1.00 37.97  ? 107 THR D CG2 1 
ATOM   7360  N N   . LEU D 2 108 ? -32.092 33.754  29.640  1.00 31.50  ? 108 LEU D N   1 
ATOM   7361  C CA  . LEU D 2 108 ? -33.262 34.587  29.379  1.00 40.27  ? 108 LEU D CA  1 
ATOM   7362  C C   . LEU D 2 108 ? -34.082 34.041  28.214  1.00 42.23  ? 108 LEU D C   1 
ATOM   7363  O O   . LEU D 2 108 ? -35.317 34.126  28.222  1.00 37.69  ? 108 LEU D O   1 
ATOM   7364  C CB  . LEU D 2 108 ? -32.832 36.031  29.122  1.00 34.13  ? 108 LEU D CB  1 
ATOM   7365  C CG  . LEU D 2 108 ? -32.125 36.700  30.304  1.00 46.64  ? 108 LEU D CG  1 
ATOM   7366  C CD1 . LEU D 2 108 ? -31.972 38.198  30.063  1.00 43.76  ? 108 LEU D CD1 1 
ATOM   7367  C CD2 . LEU D 2 108 ? -32.879 36.424  31.603  1.00 43.11  ? 108 LEU D CD2 1 
ATOM   7368  N N   . ASP D 2 109 ? -33.417 33.477  27.202  1.00 31.81  ? 109 ASP D N   1 
ATOM   7369  C CA  . ASP D 2 109 ? -34.138 32.834  26.108  1.00 48.55  ? 109 ASP D CA  1 
ATOM   7370  C C   . ASP D 2 109 ? -34.795 31.525  26.543  1.00 39.37  ? 109 ASP D C   1 
ATOM   7371  O O   . ASP D 2 109 ? -35.865 31.170  26.033  1.00 39.71  ? 109 ASP D O   1 
ATOM   7372  C CB  . ASP D 2 109 ? -33.191 32.599  24.936  1.00 41.93  ? 109 ASP D CB  1 
ATOM   7373  C CG  . ASP D 2 109 ? -32.816 33.885  24.235  1.00 63.97  ? 109 ASP D CG  1 
ATOM   7374  O OD1 . ASP D 2 109 ? -33.695 34.768  24.115  1.00 60.70  ? 109 ASP D OD1 1 
ATOM   7375  O OD2 . ASP D 2 109 ? -31.646 34.019  23.816  1.00 69.38  ? 109 ASP D OD2 1 
ATOM   7376  N N   . PHE D 2 110 ? -34.178 30.809  27.486  1.00 34.54  ? 110 PHE D N   1 
ATOM   7377  C CA  . PHE D 2 110 ? -34.793 29.610  28.047  1.00 32.92  ? 110 PHE D CA  1 
ATOM   7378  C C   . PHE D 2 110 ? -36.119 29.938  28.721  1.00 39.99  ? 110 PHE D C   1 
ATOM   7379  O O   . PHE D 2 110 ? -37.120 29.240  28.511  1.00 35.52  ? 110 PHE D O   1 
ATOM   7380  C CB  . PHE D 2 110 ? -33.824 28.963  29.038  1.00 33.24  ? 110 PHE D CB  1 
ATOM   7381  C CG  . PHE D 2 110 ? -34.365 27.745  29.733  1.00 40.95  ? 110 PHE D CG  1 
ATOM   7382  C CD1 . PHE D 2 110 ? -34.655 26.590  29.022  1.00 44.14  ? 110 PHE D CD1 1 
ATOM   7383  C CD2 . PHE D 2 110 ? -34.541 27.739  31.110  1.00 34.76  ? 110 PHE D CD2 1 
ATOM   7384  C CE1 . PHE D 2 110 ? -35.131 25.460  29.668  1.00 35.31  ? 110 PHE D CE1 1 
ATOM   7385  C CE2 . PHE D 2 110 ? -35.016 26.609  31.759  1.00 39.82  ? 110 PHE D CE2 1 
ATOM   7386  C CZ  . PHE D 2 110 ? -35.312 25.470  31.035  1.00 26.59  ? 110 PHE D CZ  1 
ATOM   7387  N N   . HIS D 2 111 ? -36.150 31.008  29.522  1.00 35.88  ? 111 HIS D N   1 
ATOM   7388  C CA  . HIS D 2 111 ? -37.404 31.433  30.139  1.00 37.53  ? 111 HIS D CA  1 
ATOM   7389  C C   . HIS D 2 111 ? -38.425 31.827  29.083  1.00 37.92  ? 111 HIS D C   1 
ATOM   7390  O O   . HIS D 2 111 ? -39.603 31.465  29.182  1.00 38.51  ? 111 HIS D O   1 
ATOM   7391  C CB  . HIS D 2 111 ? -37.158 32.601  31.093  1.00 34.59  ? 111 HIS D CB  1 
ATOM   7392  C CG  . HIS D 2 111 ? -36.448 32.216  32.352  1.00 39.47  ? 111 HIS D CG  1 
ATOM   7393  N ND1 . HIS D 2 111 ? -36.932 31.259  33.216  1.00 38.45  ? 111 HIS D ND1 1 
ATOM   7394  C CD2 . HIS D 2 111 ? -35.290 32.664  32.896  1.00 37.93  ? 111 HIS D CD2 1 
ATOM   7395  C CE1 . HIS D 2 111 ? -36.103 31.131  34.237  1.00 41.51  ? 111 HIS D CE1 1 
ATOM   7396  N NE2 . HIS D 2 111 ? -35.100 31.973  34.068  1.00 49.00  ? 111 HIS D NE2 1 
ATOM   7397  N N   . ASP D 2 112 ? -37.988 32.564  28.061  1.00 36.10  ? 112 ASP D N   1 
ATOM   7398  C CA  . ASP D 2 112 ? -38.893 32.970  26.991  1.00 37.20  ? 112 ASP D CA  1 
ATOM   7399  C C   . ASP D 2 112 ? -39.474 31.756  26.278  1.00 41.14  ? 112 ASP D C   1 
ATOM   7400  O O   . ASP D 2 112 ? -40.670 31.719  25.964  1.00 47.16  ? 112 ASP D O   1 
ATOM   7401  C CB  . ASP D 2 112 ? -38.148 33.874  26.006  1.00 44.70  ? 112 ASP D CB  1 
ATOM   7402  C CG  . ASP D 2 112 ? -39.077 34.628  25.074  1.00 53.32  ? 112 ASP D CG  1 
ATOM   7403  O OD1 . ASP D 2 112 ? -40.306 34.598  25.287  1.00 55.70  ? 112 ASP D OD1 1 
ATOM   7404  O OD2 . ASP D 2 112 ? -38.570 35.254  24.120  1.00 50.26  ? 112 ASP D OD2 1 
ATOM   7405  N N   . SER D 2 113 ? -38.642 30.747  26.021  1.00 37.94  ? 113 SER D N   1 
ATOM   7406  C CA  . SER D 2 113 ? -39.122 29.539  25.364  1.00 42.71  ? 113 SER D CA  1 
ATOM   7407  C C   . SER D 2 113 ? -40.157 28.819  26.220  1.00 38.65  ? 113 SER D C   1 
ATOM   7408  O O   . SER D 2 113 ? -41.158 28.310  25.701  1.00 42.73  ? 113 SER D O   1 
ATOM   7409  C CB  . SER D 2 113 ? -37.942 28.621  25.048  1.00 37.90  ? 113 SER D CB  1 
ATOM   7410  O OG  . SER D 2 113 ? -38.371 27.304  24.759  1.00 51.68  ? 113 SER D OG  1 
ATOM   7411  N N   . ASN D 2 114 ? -39.932 28.760  27.534  1.00 37.19  ? 114 ASN D N   1 
ATOM   7412  C CA  . ASN D 2 114 ? -40.868 28.055  28.401  1.00 31.50  ? 114 ASN D CA  1 
ATOM   7413  C C   . ASN D 2 114 ? -42.231 28.731  28.408  1.00 36.74  ? 114 ASN D C   1 
ATOM   7414  O O   . ASN D 2 114 ? -43.265 28.058  28.333  1.00 45.75  ? 114 ASN D O   1 
ATOM   7415  C CB  . ASN D 2 114 ? -40.303 27.957  29.816  1.00 32.02  ? 114 ASN D CB  1 
ATOM   7416  C CG  . ASN D 2 114 ? -39.105 27.040  29.893  1.00 40.40  ? 114 ASN D CG  1 
ATOM   7417  O OD1 . ASN D 2 114 ? -38.994 26.078  29.126  1.00 46.19  ? 114 ASN D OD1 1 
ATOM   7418  N ND2 . ASN D 2 114 ? -38.194 27.335  30.814  1.00 42.00  ? 114 ASN D ND2 1 
ATOM   7419  N N   . VAL D 2 115 ? -42.251 30.064  28.484  1.00 41.02  ? 115 VAL D N   1 
ATOM   7420  C CA  . VAL D 2 115 ? -43.517 30.788  28.463  1.00 41.64  ? 115 VAL D CA  1 
ATOM   7421  C C   . VAL D 2 115 ? -44.235 30.556  27.141  1.00 38.78  ? 115 VAL D C   1 
ATOM   7422  O O   . VAL D 2 115 ? -45.443 30.292  27.111  1.00 44.10  ? 115 VAL D O   1 
ATOM   7423  C CB  . VAL D 2 115 ? -43.277 32.286  28.736  1.00 45.88  ? 115 VAL D CB  1 
ATOM   7424  C CG1 . VAL D 2 115 ? -44.571 33.087  28.581  1.00 39.91  ? 115 VAL D CG1 1 
ATOM   7425  C CG2 . VAL D 2 115 ? -42.700 32.479  30.127  1.00 30.04  ? 115 VAL D CG2 1 
ATOM   7426  N N   . LYS D 2 116 ? -43.497 30.622  26.029  1.00 39.67  ? 116 LYS D N   1 
ATOM   7427  C CA  . LYS D 2 116 ? -44.108 30.407  24.720  1.00 43.17  ? 116 LYS D CA  1 
ATOM   7428  C C   . LYS D 2 116 ? -44.662 28.994  24.597  1.00 47.31  ? 116 LYS D C   1 
ATOM   7429  O O   . LYS D 2 116 ? -45.768 28.795  24.081  1.00 50.69  ? 116 LYS D O   1 
ATOM   7430  C CB  . LYS D 2 116 ? -43.089 30.684  23.614  1.00 41.66  ? 116 LYS D CB  1 
ATOM   7431  C CG  . LYS D 2 116 ? -43.621 30.491  22.204  1.00 37.72  ? 116 LYS D CG  1 
ATOM   7432  C CD  . LYS D 2 116 ? -42.530 29.995  21.269  1.00 53.78  ? 116 LYS D CD  1 
ATOM   7433  C CE  . LYS D 2 116 ? -42.710 30.543  19.860  1.00 57.24  ? 116 LYS D CE  1 
ATOM   7434  N NZ  . LYS D 2 116 ? -44.134 30.500  19.439  1.00 51.37  ? 116 LYS D NZ  1 
ATOM   7435  N N   . ASN D 2 117 ? -43.911 27.999  25.071  1.00 43.57  ? 117 ASN D N   1 
ATOM   7436  C CA  . ASN D 2 117 ? -44.402 26.627  25.022  1.00 46.27  ? 117 ASN D CA  1 
ATOM   7437  C C   . ASN D 2 117 ? -45.661 26.467  25.865  1.00 43.11  ? 117 ASN D C   1 
ATOM   7438  O O   . ASN D 2 117 ? -46.599 25.768  25.464  1.00 47.45  ? 117 ASN D O   1 
ATOM   7439  C CB  . ASN D 2 117 ? -43.302 25.663  25.469  1.00 35.41  ? 117 ASN D CB  1 
ATOM   7440  C CG  . ASN D 2 117 ? -42.182 25.553  24.440  1.00 53.10  ? 117 ASN D CG  1 
ATOM   7441  O OD1 . ASN D 2 117 ? -42.330 26.003  23.300  1.00 42.82  ? 117 ASN D OD1 1 
ATOM   7442  N ND2 . ASN D 2 117 ? -41.053 24.971  24.841  1.00 41.04  ? 117 ASN D ND2 1 
ATOM   7443  N N   . LEU D 2 118 ? -45.709 27.121  27.029  1.00 41.30  ? 118 LEU D N   1 
ATOM   7444  C CA  . LEU D 2 118 ? -46.914 27.073  27.850  1.00 41.04  ? 118 LEU D CA  1 
ATOM   7445  C C   . LEU D 2 118 ? -48.093 27.711  27.128  1.00 51.93  ? 118 LEU D C   1 
ATOM   7446  O O   . LEU D 2 118 ? -49.221 27.212  27.206  1.00 48.40  ? 118 LEU D O   1 
ATOM   7447  C CB  . LEU D 2 118 ? -46.668 27.763  29.190  1.00 37.72  ? 118 LEU D CB  1 
ATOM   7448  C CG  . LEU D 2 118 ? -47.366 27.146  30.400  1.00 49.61  ? 118 LEU D CG  1 
ATOM   7449  C CD1 . LEU D 2 118 ? -46.598 25.933  30.899  1.00 52.78  ? 118 LEU D CD1 1 
ATOM   7450  C CD2 . LEU D 2 118 ? -47.522 28.180  31.505  1.00 54.77  ? 118 LEU D CD2 1 
ATOM   7451  N N   . TYR D 2 119 ? -47.850 28.816  26.419  1.00 48.61  ? 119 TYR D N   1 
ATOM   7452  C CA  . TYR D 2 119 ? -48.908 29.437  25.629  1.00 47.24  ? 119 TYR D CA  1 
ATOM   7453  C C   . TYR D 2 119 ? -49.404 28.497  24.534  1.00 46.10  ? 119 TYR D C   1 
ATOM   7454  O O   . TYR D 2 119 ? -50.614 28.373  24.313  1.00 45.51  ? 119 TYR D O   1 
ATOM   7455  C CB  . TYR D 2 119 ? -48.404 30.752  25.029  1.00 32.31  ? 119 TYR D CB  1 
ATOM   7456  C CG  . TYR D 2 119 ? -49.421 31.477  24.181  1.00 48.96  ? 119 TYR D CG  1 
ATOM   7457  C CD1 . TYR D 2 119 ? -50.317 32.373  24.752  1.00 46.51  ? 119 TYR D CD1 1 
ATOM   7458  C CD2 . TYR D 2 119 ? -49.484 31.272  22.806  1.00 43.90  ? 119 TYR D CD2 1 
ATOM   7459  C CE1 . TYR D 2 119 ? -51.246 33.042  23.979  1.00 45.42  ? 119 TYR D CE1 1 
ATOM   7460  C CE2 . TYR D 2 119 ? -50.414 31.934  22.028  1.00 46.04  ? 119 TYR D CE2 1 
ATOM   7461  C CZ  . TYR D 2 119 ? -51.290 32.818  22.620  1.00 44.91  ? 119 TYR D CZ  1 
ATOM   7462  O OH  . TYR D 2 119 ? -52.217 33.481  21.851  1.00 67.23  ? 119 TYR D OH  1 
ATOM   7463  N N   . ASP D 2 120 ? -48.484 27.821  23.841  1.00 48.21  ? 120 ASP D N   1 
ATOM   7464  C CA  . ASP D 2 120 ? -48.885 26.966  22.727  1.00 53.46  ? 120 ASP D CA  1 
ATOM   7465  C C   . ASP D 2 120 ? -49.685 25.762  23.207  1.00 53.92  ? 120 ASP D C   1 
ATOM   7466  O O   . ASP D 2 120 ? -50.665 25.369  22.563  1.00 56.95  ? 120 ASP D O   1 
ATOM   7467  C CB  . ASP D 2 120 ? -47.653 26.523  21.938  1.00 46.50  ? 120 ASP D CB  1 
ATOM   7468  C CG  . ASP D 2 120 ? -47.194 27.576  20.936  1.00 61.18  ? 120 ASP D CG  1 
ATOM   7469  O OD1 . ASP D 2 120 ? -47.958 28.535  20.682  1.00 65.03  ? 120 ASP D OD1 1 
ATOM   7470  O OD2 . ASP D 2 120 ? -46.065 27.453  20.413  1.00 60.20  ? 120 ASP D OD2 1 
ATOM   7471  N N   . LYS D 2 121 ? -49.292 25.171  24.339  1.00 44.86  ? 121 LYS D N   1 
ATOM   7472  C CA  . LYS D 2 121 ? -50.010 24.011  24.856  1.00 48.90  ? 121 LYS D CA  1 
ATOM   7473  C C   . LYS D 2 121 ? -51.464 24.358  25.159  1.00 61.53  ? 121 LYS D C   1 
ATOM   7474  O O   . LYS D 2 121 ? -52.374 23.566  24.881  1.00 60.75  ? 121 LYS D O   1 
ATOM   7475  C CB  . LYS D 2 121 ? -49.301 23.470  26.102  1.00 45.61  ? 121 LYS D CB  1 
ATOM   7476  C CG  . LYS D 2 121 ? -50.095 22.426  26.871  1.00 62.85  ? 121 LYS D CG  1 
ATOM   7477  C CD  . LYS D 2 121 ? -49.575 22.257  28.295  1.00 74.22  ? 121 LYS D CD  1 
ATOM   7478  C CE  . LYS D 2 121 ? -50.363 21.191  29.057  1.00 71.60  ? 121 LYS D CE  1 
ATOM   7479  N NZ  . LYS D 2 121 ? -51.231 20.359  28.164  1.00 61.96  ? 121 LYS D NZ  1 
ATOM   7480  N N   . VAL D 2 122 ? -51.703 25.547  25.716  1.00 51.08  ? 122 VAL D N   1 
ATOM   7481  C CA  . VAL D 2 122 ? -53.071 25.995  25.954  1.00 52.24  ? 122 VAL D CA  1 
ATOM   7482  C C   . VAL D 2 122 ? -53.803 26.217  24.632  1.00 53.92  ? 122 VAL D C   1 
ATOM   7483  O O   . VAL D 2 122 ? -54.980 25.860  24.490  1.00 44.90  ? 122 VAL D O   1 
ATOM   7484  C CB  . VAL D 2 122 ? -53.063 27.264  26.824  1.00 44.71  ? 122 VAL D CB  1 
ATOM   7485  C CG1 . VAL D 2 122 ? -54.362 28.045  26.650  1.00 44.83  ? 122 VAL D CG1 1 
ATOM   7486  C CG2 . VAL D 2 122 ? -52.842 26.902  28.280  1.00 42.54  ? 122 VAL D CG2 1 
ATOM   7487  N N   . ARG D 2 123 ? -53.124 26.811  23.647  1.00 44.42  ? 123 ARG D N   1 
ATOM   7488  C CA  . ARG D 2 123 ? -53.773 27.100  22.371  1.00 42.34  ? 123 ARG D CA  1 
ATOM   7489  C C   . ARG D 2 123 ? -54.214 25.822  21.667  1.00 57.99  ? 123 ARG D C   1 
ATOM   7490  O O   . ARG D 2 123 ? -55.316 25.762  21.105  1.00 50.15  ? 123 ARG D O   1 
ATOM   7491  C CB  . ARG D 2 123 ? -52.832 27.903  21.477  1.00 41.88  ? 123 ARG D CB  1 
ATOM   7492  C CG  . ARG D 2 123 ? -53.536 28.742  20.422  1.00 52.05  ? 123 ARG D CG  1 
ATOM   7493  C CD  . ARG D 2 123 ? -53.043 28.405  19.024  1.00 59.12  ? 123 ARG D CD  1 
ATOM   7494  N NE  . ARG D 2 123 ? -51.594 28.244  18.974  1.00 63.41  ? 123 ARG D NE  1 
ATOM   7495  C CZ  . ARG D 2 123 ? -50.969 27.310  18.269  1.00 70.62  ? 123 ARG D CZ  1 
ATOM   7496  N NH1 . ARG D 2 123 ? -51.639 26.432  17.538  1.00 65.26  ? 123 ARG D NH1 1 
ATOM   7497  N NH2 . ARG D 2 123 ? -49.641 27.252  18.299  1.00 53.02  ? 123 ARG D NH2 1 
ATOM   7498  N N   . LEU D 2 124 ? -53.369 24.787  21.689  1.00 51.38  ? 124 LEU D N   1 
ATOM   7499  C CA  . LEU D 2 124 ? -53.714 23.530  21.030  1.00 61.83  ? 124 LEU D CA  1 
ATOM   7500  C C   . LEU D 2 124 ? -54.915 22.863  21.694  1.00 62.79  ? 124 LEU D C   1 
ATOM   7501  O O   . LEU D 2 124 ? -55.782 22.307  21.008  1.00 53.51  ? 124 LEU D O   1 
ATOM   7502  C CB  . LEU D 2 124 ? -52.505 22.593  21.027  1.00 51.38  ? 124 LEU D CB  1 
ATOM   7503  C CG  . LEU D 2 124 ? -51.319 23.111  20.211  1.00 58.94  ? 124 LEU D CG  1 
ATOM   7504  C CD1 . LEU D 2 124 ? -50.001 22.471  20.664  1.00 55.73  ? 124 LEU D CD1 1 
ATOM   7505  C CD2 . LEU D 2 124 ? -51.567 22.896  18.722  1.00 53.63  ? 124 LEU D CD2 1 
ATOM   7506  N N   . GLN D 2 125 ? -54.981 22.904  23.028  1.00 54.35  ? 125 GLN D N   1 
ATOM   7507  C CA  . GLN D 2 125 ? -56.144 22.369  23.728  1.00 40.48  ? 125 GLN D CA  1 
ATOM   7508  C C   . GLN D 2 125 ? -57.416 23.106  23.330  1.00 47.73  ? 125 GLN D C   1 
ATOM   7509  O O   . GLN D 2 125 ? -58.442 22.482  23.035  1.00 58.50  ? 125 GLN D O   1 
ATOM   7510  C CB  . GLN D 2 125 ? -55.938 22.472  25.236  1.00 41.66  ? 125 GLN D CB  1 
ATOM   7511  C CG  . GLN D 2 125 ? -54.961 21.494  25.817  1.00 41.50  ? 125 GLN D CG  1 
ATOM   7512  C CD  . GLN D 2 125 ? -55.069 21.444  27.325  1.00 62.86  ? 125 GLN D CD  1 
ATOM   7513  O OE1 . GLN D 2 125 ? -55.624 20.499  27.889  1.00 71.40  ? 125 GLN D OE1 1 
ATOM   7514  N NE2 . GLN D 2 125 ? -54.562 22.477  27.987  1.00 55.94  ? 125 GLN D NE2 1 
ATOM   7515  N N   . LEU D 2 126 ? -57.367 24.441  23.315  1.00 44.74  ? 126 LEU D N   1 
ATOM   7516  C CA  . LEU D 2 126 ? -58.589 25.229  23.188  1.00 42.97  ? 126 LEU D CA  1 
ATOM   7517  C C   . LEU D 2 126 ? -59.144 25.187  21.771  1.00 56.79  ? 126 LEU D C   1 
ATOM   7518  O O   . LEU D 2 126 ? -60.364 25.100  21.582  1.00 63.49  ? 126 LEU D O   1 
ATOM   7519  C CB  . LEU D 2 126 ? -58.329 26.671  23.613  1.00 41.61  ? 126 LEU D CB  1 
ATOM   7520  C CG  . LEU D 2 126 ? -58.126 26.895  25.112  1.00 51.12  ? 126 LEU D CG  1 
ATOM   7521  C CD1 . LEU D 2 126 ? -58.452 28.330  25.488  1.00 41.61  ? 126 LEU D CD1 1 
ATOM   7522  C CD2 . LEU D 2 126 ? -58.965 25.919  25.931  1.00 50.87  ? 126 LEU D CD2 1 
ATOM   7523  N N   . ARG D 2 127 ? -58.269 25.252  20.769  1.00 60.87  ? 127 ARG D N   1 
ATOM   7524  C CA  . ARG D 2 127 ? -58.691 25.346  19.376  1.00 61.10  ? 127 ARG D CA  1 
ATOM   7525  C C   . ARG D 2 127 ? -59.644 26.521  19.188  1.00 62.49  ? 127 ARG D C   1 
ATOM   7526  O O   . ARG D 2 127 ? -59.420 27.602  19.744  1.00 50.89  ? 127 ARG D O   1 
ATOM   7527  C CB  . ARG D 2 127 ? -59.337 24.037  18.917  1.00 68.91  ? 127 ARG D CB  1 
ATOM   7528  C CG  . ARG D 2 127 ? -58.460 22.810  19.124  1.00 78.50  ? 127 ARG D CG  1 
ATOM   7529  C CD  . ARG D 2 127 ? -58.621 21.822  17.981  1.00 79.81  ? 127 ARG D CD  1 
ATOM   7530  N NE  . ARG D 2 127 ? -57.689 22.091  16.891  1.00 95.12  ? 127 ARG D NE  1 
ATOM   7531  C CZ  . ARG D 2 127 ? -58.050 22.387  15.649  1.00 88.52  ? 127 ARG D CZ  1 
ATOM   7532  N NH1 . ARG D 2 127 ? -59.324 22.454  15.297  1.00 84.60  ? 127 ARG D NH1 1 
ATOM   7533  N NH2 . ARG D 2 127 ? -57.110 22.622  14.736  1.00 78.07  ? 127 ARG D NH2 1 
ATOM   7534  N N   . ASP D 2 128 ? -60.723 26.316  18.434  1.00 67.03  ? 128 ASP D N   1 
ATOM   7535  C CA  . ASP D 2 128 ? -61.647 27.392  18.104  1.00 68.10  ? 128 ASP D CA  1 
ATOM   7536  C C   . ASP D 2 128 ? -62.710 27.618  19.172  1.00 72.98  ? 128 ASP D C   1 
ATOM   7537  O O   . ASP D 2 128 ? -63.555 28.506  19.003  1.00 67.46  ? 128 ASP D O   1 
ATOM   7538  C CB  . ASP D 2 128 ? -62.320 27.123  16.754  1.00 77.54  ? 128 ASP D CB  1 
ATOM   7539  C CG  . ASP D 2 128 ? -62.956 25.747  16.675  1.00 86.87  ? 128 ASP D CG  1 
ATOM   7540  O OD1 . ASP D 2 128 ? -62.683 24.907  17.559  1.00 84.46  ? 128 ASP D OD1 1 
ATOM   7541  O OD2 . ASP D 2 128 ? -63.732 25.508  15.725  1.00 87.22  ? 128 ASP D OD2 1 
ATOM   7542  N N   . ASN D 2 129 ? -62.687 26.849  20.266  1.00 70.04  ? 129 ASN D N   1 
ATOM   7543  C CA  . ASN D 2 129 ? -63.581 27.108  21.391  1.00 64.40  ? 129 ASN D CA  1 
ATOM   7544  C C   . ASN D 2 129 ? -63.263 28.427  22.086  1.00 64.27  ? 129 ASN D C   1 
ATOM   7545  O O   . ASN D 2 129 ? -64.053 28.884  22.919  1.00 58.24  ? 129 ASN D O   1 
ATOM   7546  C CB  . ASN D 2 129 ? -63.512 25.956  22.400  1.00 55.47  ? 129 ASN D CB  1 
ATOM   7547  C CG  . ASN D 2 129 ? -64.359 24.762  21.985  1.00 68.21  ? 129 ASN D CG  1 
ATOM   7548  O OD1 . ASN D 2 129 ? -65.011 24.783  20.940  1.00 71.09  ? 129 ASN D OD1 1 
ATOM   7549  N ND2 . ASN D 2 129 ? -64.350 23.713  22.804  1.00 61.67  ? 129 ASN D ND2 1 
ATOM   7550  N N   . ALA D 2 130 ? -62.120 29.033  21.775  1.00 50.58  ? 130 ALA D N   1 
ATOM   7551  C CA  . ALA D 2 130 ? -61.788 30.370  22.235  1.00 67.01  ? 130 ALA D CA  1 
ATOM   7552  C C   . ALA D 2 130 ? -60.994 31.062  21.140  1.00 63.71  ? 130 ALA D C   1 
ATOM   7553  O O   . ALA D 2 130 ? -60.444 30.417  20.244  1.00 64.43  ? 130 ALA D O   1 
ATOM   7554  C CB  . ALA D 2 130 ? -60.986 30.346  23.542  1.00 59.01  ? 130 ALA D CB  1 
ATOM   7555  N N   . LYS D 2 131 ? -60.944 32.385  21.212  1.00 55.65  ? 131 LYS D N   1 
ATOM   7556  C CA  . LYS D 2 131 ? -60.106 33.168  20.320  1.00 65.35  ? 131 LYS D CA  1 
ATOM   7557  C C   . LYS D 2 131 ? -58.954 33.769  21.112  1.00 66.07  ? 131 LYS D C   1 
ATOM   7558  O O   . LYS D 2 131 ? -59.129 34.188  22.261  1.00 59.33  ? 131 LYS D O   1 
ATOM   7559  C CB  . LYS D 2 131 ? -60.910 34.266  19.620  1.00 60.84  ? 131 LYS D CB  1 
ATOM   7560  C CG  . LYS D 2 131 ? -61.341 35.418  20.509  1.00 62.70  ? 131 LYS D CG  1 
ATOM   7561  C CD  . LYS D 2 131 ? -61.265 36.737  19.753  1.00 65.17  ? 131 LYS D CD  1 
ATOM   7562  C CE  . LYS D 2 131 ? -62.369 37.691  20.177  1.00 65.86  ? 131 LYS D CE  1 
ATOM   7563  N NZ  . LYS D 2 131 ? -62.087 39.100  19.771  1.00 66.59  ? 131 LYS D NZ  1 
ATOM   7564  N N   . GLU D 2 132 ? -57.765 33.771  20.513  1.00 59.33  ? 132 GLU D N   1 
ATOM   7565  C CA  . GLU D 2 132 ? -56.619 34.399  21.151  1.00 60.23  ? 132 GLU D CA  1 
ATOM   7566  C C   . GLU D 2 132 ? -56.638 35.894  20.868  1.00 51.38  ? 132 GLU D C   1 
ATOM   7567  O O   . GLU D 2 132 ? -56.803 36.317  19.720  1.00 58.71  ? 132 GLU D O   1 
ATOM   7568  C CB  . GLU D 2 132 ? -55.305 33.777  20.672  1.00 63.59  ? 132 GLU D CB  1 
ATOM   7569  C CG  . GLU D 2 132 ? -55.310 33.231  19.258  1.00 69.74  ? 132 GLU D CG  1 
ATOM   7570  C CD  . GLU D 2 132 ? -53.932 32.748  18.821  1.00 75.95  ? 132 GLU D CD  1 
ATOM   7571  O OE1 . GLU D 2 132 ? -53.015 33.589  18.707  1.00 84.19  ? 132 GLU D OE1 1 
ATOM   7572  O OE2 . GLU D 2 132 ? -53.762 31.531  18.592  1.00 66.63  ? 132 GLU D OE2 1 
ATOM   7573  N N   . LEU D 2 133 ? -56.473 36.692  21.924  1.00 56.71  ? 133 LEU D N   1 
ATOM   7574  C CA  . LEU D 2 133 ? -56.484 38.145  21.821  1.00 59.45  ? 133 LEU D CA  1 
ATOM   7575  C C   . LEU D 2 133 ? -55.141 38.731  21.401  1.00 58.53  ? 133 LEU D C   1 
ATOM   7576  O O   . LEU D 2 133 ? -55.081 39.925  21.085  1.00 57.84  ? 133 LEU D O   1 
ATOM   7577  C CB  . LEU D 2 133 ? -56.918 38.756  23.158  1.00 54.30  ? 133 LEU D CB  1 
ATOM   7578  C CG  . LEU D 2 133 ? -58.127 38.085  23.816  1.00 59.57  ? 133 LEU D CG  1 
ATOM   7579  C CD1 . LEU D 2 133 ? -58.476 38.735  25.151  1.00 55.67  ? 133 LEU D CD1 1 
ATOM   7580  C CD2 . LEU D 2 133 ? -59.319 38.113  22.872  1.00 69.07  ? 133 LEU D CD2 1 
ATOM   7581  N N   . GLY D 2 134 ? -54.069 37.935  21.396  1.00 50.24  ? 134 GLY D N   1 
ATOM   7582  C CA  . GLY D 2 134 ? -52.763 38.394  20.971  1.00 47.13  ? 134 GLY D CA  1 
ATOM   7583  C C   . GLY D 2 134 ? -51.867 38.929  22.069  1.00 45.79  ? 134 GLY D C   1 
ATOM   7584  O O   . GLY D 2 134 ? -50.686 39.195  21.808  1.00 57.20  ? 134 GLY D O   1 
ATOM   7585  N N   . ASN D 2 135 ? -52.383 39.103  23.282  1.00 47.60  ? 135 ASN D N   1 
ATOM   7586  C CA  . ASN D 2 135 ? -51.590 39.579  24.405  1.00 49.35  ? 135 ASN D CA  1 
ATOM   7587  C C   . ASN D 2 135 ? -51.185 38.451  25.341  1.00 53.72  ? 135 ASN D C   1 
ATOM   7588  O O   . ASN D 2 135 ? -50.717 38.717  26.453  1.00 56.77  ? 135 ASN D O   1 
ATOM   7589  C CB  . ASN D 2 135 ? -52.358 40.653  25.178  1.00 44.17  ? 135 ASN D CB  1 
ATOM   7590  C CG  . ASN D 2 135 ? -53.790 40.249  25.459  1.00 63.24  ? 135 ASN D CG  1 
ATOM   7591  O OD1 . ASN D 2 135 ? -54.151 39.078  25.329  1.00 64.55  ? 135 ASN D OD1 1 
ATOM   7592  N ND2 . ASN D 2 135 ? -54.617 41.214  25.843  1.00 61.09  ? 135 ASN D ND2 1 
ATOM   7593  N N   . GLY D 2 136 ? -51.336 37.203  24.911  1.00 56.30  ? 136 GLY D N   1 
ATOM   7594  C CA  . GLY D 2 136 ? -51.106 36.064  25.771  1.00 50.89  ? 136 GLY D CA  1 
ATOM   7595  C C   . GLY D 2 136 ? -52.345 35.557  26.462  1.00 52.18  ? 136 GLY D C   1 
ATOM   7596  O O   . GLY D 2 136 ? -52.237 34.708  27.357  1.00 51.60  ? 136 GLY D O   1 
ATOM   7597  N N   . CYS D 2 137 ? -53.517 36.049  26.074  1.00 57.19  ? 137 CYS D N   1 
ATOM   7598  C CA  . CYS D 2 137 ? -54.784 35.703  26.691  1.00 45.93  ? 137 CYS D CA  1 
ATOM   7599  C C   . CYS D 2 137 ? -55.698 35.052  25.663  1.00 46.08  ? 137 CYS D C   1 
ATOM   7600  O O   . CYS D 2 137 ? -55.549 35.246  24.454  1.00 47.09  ? 137 CYS D O   1 
ATOM   7601  C CB  . CYS D 2 137 ? -55.465 36.944  27.282  1.00 44.80  ? 137 CYS D CB  1 
ATOM   7602  S SG  . CYS D 2 137 ? -54.564 37.713  28.644  1.00 64.18  ? 137 CYS D SG  1 
ATOM   7603  N N   . PHE D 2 138 ? -56.646 34.264  26.165  1.00 46.26  ? 138 PHE D N   1 
ATOM   7604  C CA  . PHE D 2 138 ? -57.668 33.623  25.350  1.00 50.94  ? 138 PHE D CA  1 
ATOM   7605  C C   . PHE D 2 138 ? -59.035 34.020  25.882  1.00 51.90  ? 138 PHE D C   1 
ATOM   7606  O O   . PHE D 2 138 ? -59.278 33.940  27.090  1.00 45.07  ? 138 PHE D O   1 
ATOM   7607  C CB  . PHE D 2 138 ? -57.526 32.100  25.369  1.00 44.54  ? 138 PHE D CB  1 
ATOM   7608  C CG  . PHE D 2 138 ? -56.238 31.606  24.783  1.00 59.66  ? 138 PHE D CG  1 
ATOM   7609  C CD1 . PHE D 2 138 ? -55.090 31.538  25.558  1.00 53.52  ? 138 PHE D CD1 1 
ATOM   7610  C CD2 . PHE D 2 138 ? -56.171 31.214  23.459  1.00 56.71  ? 138 PHE D CD2 1 
ATOM   7611  C CE1 . PHE D 2 138 ? -53.905 31.089  25.020  1.00 50.79  ? 138 PHE D CE1 1 
ATOM   7612  C CE2 . PHE D 2 138 ? -54.984 30.761  22.917  1.00 48.69  ? 138 PHE D CE2 1 
ATOM   7613  C CZ  . PHE D 2 138 ? -53.852 30.696  23.699  1.00 56.04  ? 138 PHE D CZ  1 
ATOM   7614  N N   . GLU D 2 139 ? -59.919 34.448  24.987  1.00 56.50  ? 139 GLU D N   1 
ATOM   7615  C CA  . GLU D 2 139 ? -61.293 34.774  25.344  1.00 57.10  ? 139 GLU D CA  1 
ATOM   7616  C C   . GLU D 2 139 ? -62.174 33.587  24.978  1.00 57.40  ? 139 GLU D C   1 
ATOM   7617  O O   . GLU D 2 139 ? -62.279 33.225  23.801  1.00 63.32  ? 139 GLU D O   1 
ATOM   7618  C CB  . GLU D 2 139 ? -61.766 36.046  24.640  1.00 56.50  ? 139 GLU D CB  1 
ATOM   7619  C CG  . GLU D 2 139 ? -62.809 36.844  25.427  1.00 76.29  ? 139 GLU D CG  1 
ATOM   7620  C CD  . GLU D 2 139 ? -63.764 37.624  24.532  1.00 85.88  ? 139 GLU D CD  1 
ATOM   7621  O OE1 . GLU D 2 139 ? -63.430 38.768  24.153  1.00 78.90  ? 139 GLU D OE1 1 
ATOM   7622  O OE2 . GLU D 2 139 ? -64.850 37.093  24.210  1.00 83.92  ? 139 GLU D OE2 1 
ATOM   7623  N N   . PHE D 2 140 ? -62.785 32.976  25.987  1.00 54.24  ? 140 PHE D N   1 
ATOM   7624  C CA  . PHE D 2 140 ? -63.621 31.806  25.764  1.00 57.14  ? 140 PHE D CA  1 
ATOM   7625  C C   . PHE D 2 140 ? -64.953 32.202  25.138  1.00 67.97  ? 140 PHE D C   1 
ATOM   7626  O O   . PHE D 2 140 ? -65.527 33.245  25.460  1.00 71.00  ? 140 PHE D O   1 
ATOM   7627  C CB  . PHE D 2 140 ? -63.865 31.070  27.080  1.00 55.99  ? 140 PHE D CB  1 
ATOM   7628  C CG  . PHE D 2 140 ? -62.702 30.236  27.536  1.00 59.59  ? 140 PHE D CG  1 
ATOM   7629  C CD1 . PHE D 2 140 ? -62.527 28.948  27.058  1.00 42.93  ? 140 PHE D CD1 1 
ATOM   7630  C CD2 . PHE D 2 140 ? -61.785 30.739  28.449  1.00 52.41  ? 140 PHE D CD2 1 
ATOM   7631  C CE1 . PHE D 2 140 ? -61.459 28.174  27.479  1.00 50.61  ? 140 PHE D CE1 1 
ATOM   7632  C CE2 . PHE D 2 140 ? -60.715 29.970  28.874  1.00 46.38  ? 140 PHE D CE2 1 
ATOM   7633  C CZ  . PHE D 2 140 ? -60.552 28.685  28.388  1.00 48.11  ? 140 PHE D CZ  1 
ATOM   7634  N N   . TYR D 2 141 ? -65.439 31.361  24.225  1.00 71.37  ? 141 TYR D N   1 
ATOM   7635  C CA  . TYR D 2 141 ? -66.789 31.529  23.705  1.00 68.63  ? 141 TYR D CA  1 
ATOM   7636  C C   . TYR D 2 141 ? -67.810 30.862  24.618  1.00 74.58  ? 141 TYR D C   1 
ATOM   7637  O O   . TYR D 2 141 ? -68.879 31.427  24.880  1.00 81.50  ? 141 TYR D O   1 
ATOM   7638  C CB  . TYR D 2 141 ? -66.881 30.962  22.288  1.00 68.80  ? 141 TYR D CB  1 
ATOM   7639  C CG  . TYR D 2 141 ? -66.071 31.733  21.274  1.00 69.10  ? 141 TYR D CG  1 
ATOM   7640  C CD1 . TYR D 2 141 ? -66.116 33.119  21.229  1.00 56.23  ? 141 TYR D CD1 1 
ATOM   7641  C CD2 . TYR D 2 141 ? -65.250 31.073  20.370  1.00 68.95  ? 141 TYR D CD2 1 
ATOM   7642  C CE1 . TYR D 2 141 ? -65.377 33.828  20.305  1.00 55.88  ? 141 TYR D CE1 1 
ATOM   7643  C CE2 . TYR D 2 141 ? -64.503 31.771  19.443  1.00 61.20  ? 141 TYR D CE2 1 
ATOM   7644  C CZ  . TYR D 2 141 ? -64.572 33.149  19.414  1.00 65.48  ? 141 TYR D CZ  1 
ATOM   7645  O OH  . TYR D 2 141 ? -63.833 33.852  18.492  1.00 59.77  ? 141 TYR D OH  1 
ATOM   7646  N N   . HIS D 2 142 ? -67.497 29.667  25.107  1.00 72.86  ? 142 HIS D N   1 
ATOM   7647  C CA  . HIS D 2 142 ? -68.342 28.967  26.058  1.00 65.82  ? 142 HIS D CA  1 
ATOM   7648  C C   . HIS D 2 142 ? -68.032 29.418  27.481  1.00 65.36  ? 142 HIS D C   1 
ATOM   7649  O O   . HIS D 2 142 ? -67.025 30.076  27.752  1.00 65.91  ? 142 HIS D O   1 
ATOM   7650  C CB  . HIS D 2 142 ? -68.159 27.456  25.928  1.00 69.87  ? 142 HIS D CB  1 
ATOM   7651  C CG  . HIS D 2 142 ? -66.778 26.980  26.261  1.00 70.98  ? 142 HIS D CG  1 
ATOM   7652  N ND1 . HIS D 2 142 ? -66.450 26.451  27.491  1.00 71.45  ? 142 HIS D ND1 1 
ATOM   7653  C CD2 . HIS D 2 142 ? -65.643 26.943  25.521  1.00 61.80  ? 142 HIS D CD2 1 
ATOM   7654  C CE1 . HIS D 2 142 ? -65.174 26.109  27.495  1.00 54.67  ? 142 HIS D CE1 1 
ATOM   7655  N NE2 . HIS D 2 142 ? -64.662 26.396  26.312  1.00 59.59  ? 142 HIS D NE2 1 
ATOM   7656  N N   . LYS D 2 143 ? -68.922 29.055  28.399  1.00 66.91  ? 143 LYS D N   1 
ATOM   7657  C CA  . LYS D 2 143 ? -68.738 29.379  29.805  1.00 64.45  ? 143 LYS D CA  1 
ATOM   7658  C C   . LYS D 2 143 ? -67.730 28.410  30.408  1.00 68.92  ? 143 LYS D C   1 
ATOM   7659  O O   . LYS D 2 143 ? -67.941 27.193  30.381  1.00 62.04  ? 143 LYS D O   1 
ATOM   7660  C CB  . LYS D 2 143 ? -70.070 29.313  30.546  1.00 52.85  ? 143 LYS D CB  1 
ATOM   7661  C CG  . LYS D 2 143 ? -70.983 30.485  30.252  1.00 70.52  ? 143 LYS D CG  1 
ATOM   7662  C CD  . LYS D 2 143 ? -71.321 31.244  31.525  1.00 84.65  ? 143 LYS D CD  1 
ATOM   7663  C CE  . LYS D 2 143 ? -72.141 32.489  31.225  1.00 84.85  ? 143 LYS D CE  1 
ATOM   7664  N NZ  . LYS D 2 143 ? -71.434 33.731  31.650  1.00 83.79  ? 143 LYS D NZ  1 
ATOM   7665  N N   . CYS D 2 144 ? -66.633 28.944  30.941  1.00 54.88  ? 144 CYS D N   1 
ATOM   7666  C CA  . CYS D 2 144 ? -65.555 28.128  31.494  1.00 62.04  ? 144 CYS D CA  1 
ATOM   7667  C C   . CYS D 2 144 ? -65.466 28.422  32.988  1.00 56.87  ? 144 CYS D C   1 
ATOM   7668  O O   . CYS D 2 144 ? -64.899 29.439  33.400  1.00 55.81  ? 144 CYS D O   1 
ATOM   7669  C CB  . CYS D 2 144 ? -64.233 28.403  30.777  1.00 46.31  ? 144 CYS D CB  1 
ATOM   7670  S SG  . CYS D 2 144 ? -62.871 27.300  31.237  1.00 66.85  ? 144 CYS D SG  1 
ATOM   7671  N N   . ASP D 2 145 ? -66.021 27.520  33.793  1.00 56.31  ? 145 ASP D N   1 
ATOM   7672  C CA  . ASP D 2 145 ? -66.013 27.662  35.242  1.00 53.15  ? 145 ASP D CA  1 
ATOM   7673  C C   . ASP D 2 145 ? -64.624 27.310  35.781  1.00 56.20  ? 145 ASP D C   1 
ATOM   7674  O O   . ASP D 2 145 ? -63.675 27.078  35.025  1.00 46.75  ? 145 ASP D O   1 
ATOM   7675  C CB  . ASP D 2 145 ? -67.127 26.811  35.854  1.00 46.84  ? 145 ASP D CB  1 
ATOM   7676  C CG  . ASP D 2 145 ? -66.866 25.313  35.745  1.00 63.35  ? 145 ASP D CG  1 
ATOM   7677  O OD1 . ASP D 2 145 ? -66.100 24.890  34.854  1.00 66.01  ? 145 ASP D OD1 1 
ATOM   7678  O OD2 . ASP D 2 145 ? -67.438 24.554  36.555  1.00 71.20  ? 145 ASP D OD2 1 
ATOM   7679  N N   . ASN D 2 146 ? -64.486 27.281  37.109  1.00 50.28  ? 146 ASN D N   1 
ATOM   7680  C CA  . ASN D 2 146 ? -63.187 26.999  37.711  1.00 50.06  ? 146 ASN D CA  1 
ATOM   7681  C C   . ASN D 2 146 ? -62.705 25.596  37.361  1.00 61.54  ? 146 ASN D C   1 
ATOM   7682  O O   . ASN D 2 146 ? -61.516 25.391  37.087  1.00 57.36  ? 146 ASN D O   1 
ATOM   7683  C CB  . ASN D 2 146 ? -63.258 27.181  39.227  1.00 47.20  ? 146 ASN D CB  1 
ATOM   7684  C CG  . ASN D 2 146 ? -63.242 28.642  39.642  1.00 52.12  ? 146 ASN D CG  1 
ATOM   7685  O OD1 . ASN D 2 146 ? -63.141 29.538  38.805  1.00 53.80  ? 146 ASN D OD1 1 
ATOM   7686  N ND2 . ASN D 2 146 ? -63.337 28.887  40.943  1.00 55.70  ? 146 ASN D ND2 1 
ATOM   7687  N N   . GLU D 2 147 ? -63.613 24.614  37.374  1.00 64.69  ? 147 GLU D N   1 
ATOM   7688  C CA  . GLU D 2 147 ? -63.241 23.252  37.000  1.00 63.86  ? 147 GLU D CA  1 
ATOM   7689  C C   . GLU D 2 147 ? -62.794 23.184  35.546  1.00 55.08  ? 147 GLU D C   1 
ATOM   7690  O O   . GLU D 2 147 ? -61.829 22.487  35.214  1.00 57.68  ? 147 GLU D O   1 
ATOM   7691  C CB  . GLU D 2 147 ? -64.415 22.304  37.250  1.00 57.00  ? 147 GLU D CB  1 
ATOM   7692  C CG  . GLU D 2 147 ? -64.529 21.821  38.689  1.00 76.43  ? 147 GLU D CG  1 
ATOM   7693  C CD  . GLU D 2 147 ? -65.415 20.594  38.822  1.00 106.45 ? 147 GLU D CD  1 
ATOM   7694  O OE1 . GLU D 2 147 ? -65.392 19.738  37.909  1.00 105.61 ? 147 GLU D OE1 1 
ATOM   7695  O OE2 . GLU D 2 147 ? -66.133 20.483  39.839  1.00 102.03 ? 147 GLU D OE2 1 
ATOM   7696  N N   . CYS D 2 148 ? -63.494 23.899  34.663  1.00 55.11  ? 148 CYS D N   1 
ATOM   7697  C CA  . CYS D 2 148 ? -63.043 24.039  33.283  1.00 58.28  ? 148 CYS D CA  1 
ATOM   7698  C C   . CYS D 2 148 ? -61.667 24.690  33.211  1.00 53.76  ? 148 CYS D C   1 
ATOM   7699  O O   . CYS D 2 148 ? -60.795 24.230  32.463  1.00 55.17  ? 148 CYS D O   1 
ATOM   7700  C CB  . CYS D 2 148 ? -64.073 24.847  32.492  1.00 54.90  ? 148 CYS D CB  1 
ATOM   7701  S SG  . CYS D 2 148 ? -63.553 25.410  30.865  1.00 77.59  ? 148 CYS D SG  1 
ATOM   7702  N N   . MET D 2 149 ? -61.446 25.753  33.990  1.00 46.34  ? 149 MET D N   1 
ATOM   7703  C CA  . MET D 2 149 ? -60.141 26.408  33.985  1.00 51.53  ? 149 MET D CA  1 
ATOM   7704  C C   . MET D 2 149 ? -59.052 25.461  34.470  1.00 53.54  ? 149 MET D C   1 
ATOM   7705  O O   . MET D 2 149 ? -57.955 25.420  33.899  1.00 44.09  ? 149 MET D O   1 
ATOM   7706  C CB  . MET D 2 149 ? -60.173 27.667  34.851  1.00 58.49  ? 149 MET D CB  1 
ATOM   7707  C CG  . MET D 2 149 ? -61.070 28.772  34.322  1.00 57.07  ? 149 MET D CG  1 
ATOM   7708  S SD  . MET D 2 149 ? -60.423 29.542  32.831  1.00 50.57  ? 149 MET D SD  1 
ATOM   7709  C CE  . MET D 2 149 ? -61.630 30.839  32.558  1.00 40.96  ? 149 MET D CE  1 
ATOM   7710  N N   . GLU D 2 150 ? -59.339 24.690  35.522  1.00 53.22  ? 150 GLU D N   1 
ATOM   7711  C CA  . GLU D 2 150 ? -58.357 23.736  36.028  1.00 55.82  ? 150 GLU D CA  1 
ATOM   7712  C C   . GLU D 2 150 ? -58.035 22.679  34.980  1.00 50.44  ? 150 GLU D C   1 
ATOM   7713  O O   . GLU D 2 150 ? -56.880 22.259  34.847  1.00 49.57  ? 150 GLU D O   1 
ATOM   7714  C CB  . GLU D 2 150 ? -58.867 23.092  37.318  1.00 61.06  ? 150 GLU D CB  1 
ATOM   7715  C CG  . GLU D 2 150 ? -58.078 21.874  37.782  1.00 67.04  ? 150 GLU D CG  1 
ATOM   7716  C CD  . GLU D 2 150 ? -56.674 22.215  38.256  1.00 73.19  ? 150 GLU D CD  1 
ATOM   7717  O OE1 . GLU D 2 150 ? -56.514 23.195  39.016  1.00 77.82  ? 150 GLU D OE1 1 
ATOM   7718  O OE2 . GLU D 2 150 ? -55.730 21.493  37.872  1.00 80.12  ? 150 GLU D OE2 1 
ATOM   7719  N N   . SER D 2 151 ? -59.042 22.251  34.214  1.00 50.77  ? 151 SER D N   1 
ATOM   7720  C CA  . SER D 2 151 ? -58.804 21.288  33.145  1.00 56.96  ? 151 SER D CA  1 
ATOM   7721  C C   . SER D 2 151 ? -57.886 21.859  32.071  1.00 54.89  ? 151 SER D C   1 
ATOM   7722  O O   . SER D 2 151 ? -57.119 21.113  31.456  1.00 58.24  ? 151 SER D O   1 
ATOM   7723  C CB  . SER D 2 151 ? -60.133 20.833  32.531  1.00 53.81  ? 151 SER D CB  1 
ATOM   7724  O OG  . SER D 2 151 ? -60.578 21.710  31.506  1.00 51.90  ? 151 SER D OG  1 
ATOM   7725  N N   . VAL D 2 152 ? -57.958 23.168  31.818  1.00 47.50  ? 152 VAL D N   1 
ATOM   7726  C CA  . VAL D 2 152 ? -57.033 23.777  30.866  1.00 50.86  ? 152 VAL D CA  1 
ATOM   7727  C C   . VAL D 2 152 ? -55.625 23.828  31.446  1.00 51.71  ? 152 VAL D C   1 
ATOM   7728  O O   . VAL D 2 152 ? -54.641 23.570  30.743  1.00 55.49  ? 152 VAL D O   1 
ATOM   7729  C CB  . VAL D 2 152 ? -57.526 25.175  30.452  1.00 51.84  ? 152 VAL D CB  1 
ATOM   7730  C CG1 . VAL D 2 152 ? -56.478 25.872  29.599  1.00 43.86  ? 152 VAL D CG1 1 
ATOM   7731  C CG2 . VAL D 2 152 ? -58.836 25.070  29.692  1.00 44.37  ? 152 VAL D CG2 1 
ATOM   7732  N N   . ARG D 2 153 ? -55.507 24.160  32.736  1.00 54.38  ? 153 ARG D N   1 
ATOM   7733  C CA  . ARG D 2 153 ? -54.194 24.286  33.365  1.00 51.57  ? 153 ARG D CA  1 
ATOM   7734  C C   . ARG D 2 153 ? -53.471 22.946  33.432  1.00 58.91  ? 153 ARG D C   1 
ATOM   7735  O O   . ARG D 2 153 ? -52.271 22.872  33.142  1.00 59.91  ? 153 ARG D O   1 
ATOM   7736  C CB  . ARG D 2 153 ? -54.336 24.899  34.758  1.00 47.33  ? 153 ARG D CB  1 
ATOM   7737  C CG  . ARG D 2 153 ? -54.789 26.347  34.722  1.00 43.06  ? 153 ARG D CG  1 
ATOM   7738  C CD  . ARG D 2 153 ? -54.567 27.049  36.041  1.00 50.96  ? 153 ARG D CD  1 
ATOM   7739  N NE  . ARG D 2 153 ? -55.270 26.407  37.143  1.00 53.08  ? 153 ARG D NE  1 
ATOM   7740  C CZ  . ARG D 2 153 ? -56.477 26.758  37.564  1.00 56.61  ? 153 ARG D CZ  1 
ATOM   7741  N NH1 . ARG D 2 153 ? -57.159 27.729  36.978  1.00 52.63  ? 153 ARG D NH1 1 
ATOM   7742  N NH2 . ARG D 2 153 ? -57.016 26.116  38.596  1.00 53.92  ? 153 ARG D NH2 1 
ATOM   7743  N N   . ASN D 2 154 ? -54.167 21.879  33.819  1.00 60.97  ? 154 ASN D N   1 
ATOM   7744  C CA  . ASN D 2 154 ? -53.605 20.552  33.628  1.00 55.87  ? 154 ASN D CA  1 
ATOM   7745  C C   . ASN D 2 154 ? -53.971 20.108  32.211  1.00 53.54  ? 154 ASN D C   1 
ATOM   7746  O O   . ASN D 2 154 ? -54.449 20.903  31.401  1.00 67.61  ? 154 ASN D O   1 
ATOM   7747  C CB  . ASN D 2 154 ? -54.013 19.605  34.770  1.00 57.48  ? 154 ASN D CB  1 
ATOM   7748  C CG  . ASN D 2 154 ? -55.501 19.232  34.792  1.00 67.11  ? 154 ASN D CG  1 
ATOM   7749  O OD1 . ASN D 2 154 ? -56.226 19.359  33.805  1.00 65.33  ? 154 ASN D OD1 1 
ATOM   7750  N ND2 . ASN D 2 154 ? -55.947 18.750  35.963  1.00 74.34  ? 154 ASN D ND2 1 
ATOM   7751  N N   . GLY D 2 155 ? -53.715 18.860  31.866  1.00 53.65  ? 155 GLY D N   1 
ATOM   7752  C CA  . GLY D 2 155 ? -53.868 18.515  30.469  1.00 70.49  ? 155 GLY D CA  1 
ATOM   7753  C C   . GLY D 2 155 ? -55.231 18.018  30.044  1.00 59.44  ? 155 GLY D C   1 
ATOM   7754  O O   . GLY D 2 155 ? -55.365 17.515  28.924  1.00 67.02  ? 155 GLY D O   1 
ATOM   7755  N N   . THR D 2 156 ? -56.252 18.147  30.887  1.00 58.17  ? 156 THR D N   1 
ATOM   7756  C CA  . THR D 2 156 ? -57.500 17.402  30.722  1.00 66.59  ? 156 THR D CA  1 
ATOM   7757  C C   . THR D 2 156 ? -58.645 18.261  30.197  1.00 73.62  ? 156 THR D C   1 
ATOM   7758  O O   . THR D 2 156 ? -59.799 18.066  30.590  1.00 76.31  ? 156 THR D O   1 
ATOM   7759  C CB  . THR D 2 156 ? -57.888 16.747  32.044  1.00 69.79  ? 156 THR D CB  1 
ATOM   7760  O OG1 . THR D 2 156 ? -58.209 17.762  33.004  1.00 65.86  ? 156 THR D OG1 1 
ATOM   7761  C CG2 . THR D 2 156 ? -56.740 15.895  32.575  1.00 63.71  ? 156 THR D CG2 1 
ATOM   7762  N N   . TYR D 2 157 ? -58.372 19.207  29.305  1.00 63.61  ? 157 TYR D N   1 
ATOM   7763  C CA  . TYR D 2 157 ? -59.452 20.014  28.757  1.00 62.25  ? 157 TYR D CA  1 
ATOM   7764  C C   . TYR D 2 157 ? -60.280 19.186  27.783  1.00 62.91  ? 157 TYR D C   1 
ATOM   7765  O O   . TYR D 2 157 ? -59.746 18.604  26.835  1.00 66.38  ? 157 TYR D O   1 
ATOM   7766  C CB  . TYR D 2 157 ? -58.902 21.255  28.058  1.00 61.74  ? 157 TYR D CB  1 
ATOM   7767  C CG  . TYR D 2 157 ? -59.961 22.062  27.339  1.00 49.66  ? 157 TYR D CG  1 
ATOM   7768  C CD1 . TYR D 2 157 ? -60.978 22.698  28.042  1.00 56.21  ? 157 TYR D CD1 1 
ATOM   7769  C CD2 . TYR D 2 157 ? -59.946 22.185  25.956  1.00 57.98  ? 157 TYR D CD2 1 
ATOM   7770  C CE1 . TYR D 2 157 ? -61.951 23.437  27.383  1.00 49.98  ? 157 TYR D CE1 1 
ATOM   7771  C CE2 . TYR D 2 157 ? -60.911 22.922  25.289  1.00 54.81  ? 157 TYR D CE2 1 
ATOM   7772  C CZ  . TYR D 2 157 ? -61.912 23.544  26.006  1.00 53.28  ? 157 TYR D CZ  1 
ATOM   7773  O OH  . TYR D 2 157 ? -62.870 24.279  25.344  1.00 49.22  ? 157 TYR D OH  1 
ATOM   7774  N N   . ASP D 2 158 ? -61.590 19.140  28.017  1.00 70.72  ? 158 ASP D N   1 
ATOM   7775  C CA  . ASP D 2 158 ? -62.505 18.351  27.193  1.00 68.72  ? 158 ASP D CA  1 
ATOM   7776  C C   . ASP D 2 158 ? -63.051 19.248  26.091  1.00 69.07  ? 158 ASP D C   1 
ATOM   7777  O O   . ASP D 2 158 ? -64.067 19.926  26.256  1.00 69.86  ? 158 ASP D O   1 
ATOM   7778  C CB  . ASP D 2 158 ? -63.619 17.758  28.049  1.00 78.63  ? 158 ASP D CB  1 
ATOM   7779  C CG  . ASP D 2 158 ? -64.344 16.616  27.360  1.00 77.77  ? 158 ASP D CG  1 
ATOM   7780  O OD1 . ASP D 2 158 ? -64.752 16.784  26.192  1.00 83.47  ? 158 ASP D OD1 1 
ATOM   7781  O OD2 . ASP D 2 158 ? -64.512 15.551  27.990  1.00 74.34  ? 158 ASP D OD2 1 
ATOM   7782  N N   . TYR D 2 159 ? -62.366 19.254  24.947  1.00 68.88  ? 159 TYR D N   1 
ATOM   7783  C CA  . TYR D 2 159 ? -62.823 20.061  23.816  1.00 69.66  ? 159 TYR D CA  1 
ATOM   7784  C C   . TYR D 2 159 ? -64.209 19.663  23.316  1.00 70.35  ? 159 TYR D C   1 
ATOM   7785  O O   . TYR D 2 159 ? -65.036 20.565  23.093  1.00 71.02  ? 159 TYR D O   1 
ATOM   7786  C CB  . TYR D 2 159 ? -61.786 20.005  22.688  1.00 73.04  ? 159 TYR D CB  1 
ATOM   7787  C CG  . TYR D 2 159 ? -62.233 20.691  21.414  1.00 73.13  ? 159 TYR D CG  1 
ATOM   7788  C CD1 . TYR D 2 159 ? -62.081 22.061  21.253  1.00 71.19  ? 159 TYR D CD1 1 
ATOM   7789  C CD2 . TYR D 2 159 ? -62.806 19.969  20.373  1.00 80.10  ? 159 TYR D CD2 1 
ATOM   7790  C CE1 . TYR D 2 159 ? -62.487 22.693  20.095  1.00 77.91  ? 159 TYR D CE1 1 
ATOM   7791  C CE2 . TYR D 2 159 ? -63.216 20.595  19.209  1.00 73.19  ? 159 TYR D CE2 1 
ATOM   7792  C CZ  . TYR D 2 159 ? -63.054 21.957  19.078  1.00 81.60  ? 159 TYR D CZ  1 
ATOM   7793  O OH  . TYR D 2 159 ? -63.455 22.593  17.926  1.00 85.72  ? 159 TYR D OH  1 
ATOM   7794  N N   . PRO D 2 160 ? -64.531 18.379  23.102  1.00 68.78  ? 160 PRO D N   1 
ATOM   7795  C CA  . PRO D 2 160 ? -65.883 18.048  22.611  1.00 71.62  ? 160 PRO D CA  1 
ATOM   7796  C C   . PRO D 2 160 ? -67.009 18.464  23.546  1.00 71.32  ? 160 PRO D C   1 
ATOM   7797  O O   . PRO D 2 160 ? -68.127 18.707  23.074  1.00 63.77  ? 160 PRO D O   1 
ATOM   7798  C CB  . PRO D 2 160 ? -65.829 16.523  22.444  1.00 65.34  ? 160 PRO D CB  1 
ATOM   7799  C CG  . PRO D 2 160 ? -64.386 16.215  22.254  1.00 71.57  ? 160 PRO D CG  1 
ATOM   7800  C CD  . PRO D 2 160 ? -63.664 17.185  23.132  1.00 71.17  ? 160 PRO D CD  1 
ATOM   7801  N N   . GLN D 2 161 ? -66.752 18.562  24.853  1.00 67.76  ? 161 GLN D N   1 
ATOM   7802  C CA  . GLN D 2 161 ? -67.823 18.865  25.799  1.00 65.80  ? 161 GLN D CA  1 
ATOM   7803  C C   . GLN D 2 161 ? -68.460 20.222  25.513  1.00 62.87  ? 161 GLN D C   1 
ATOM   7804  O O   . GLN D 2 161 ? -69.685 20.368  25.588  1.00 77.21  ? 161 GLN D O   1 
ATOM   7805  C CB  . GLN D 2 161 ? -67.287 18.815  27.230  1.00 72.89  ? 161 GLN D CB  1 
ATOM   7806  C CG  . GLN D 2 161 ? -68.178 18.068  28.212  1.00 78.38  ? 161 GLN D CG  1 
ATOM   7807  C CD  . GLN D 2 161 ? -67.534 17.917  29.579  1.00 96.75  ? 161 GLN D CD  1 
ATOM   7808  O OE1 . GLN D 2 161 ? -67.296 16.801  30.049  1.00 91.23  ? 161 GLN D OE1 1 
ATOM   7809  N NE2 . GLN D 2 161 ? -67.247 19.045  30.227  1.00 77.48  ? 161 GLN D NE2 1 
ATOM   7810  N N   . TYR D 2 162 ? -67.649 21.225  25.184  1.00 68.13  ? 162 TYR D N   1 
ATOM   7811  C CA  . TYR D 2 162 ? -68.141 22.569  24.914  1.00 66.29  ? 162 TYR D CA  1 
ATOM   7812  C C   . TYR D 2 162 ? -68.159 22.905  23.427  1.00 57.20  ? 162 TYR D C   1 
ATOM   7813  O O   . TYR D 2 162 ? -68.340 24.074  23.072  1.00 61.92  ? 162 TYR D O   1 
ATOM   7814  C CB  . TYR D 2 162 ? -67.297 23.603  25.669  1.00 67.20  ? 162 TYR D CB  1 
ATOM   7815  C CG  . TYR D 2 162 ? -66.914 23.183  27.071  1.00 59.26  ? 162 TYR D CG  1 
ATOM   7816  C CD1 . TYR D 2 162 ? -65.729 22.501  27.315  1.00 55.03  ? 162 TYR D CD1 1 
ATOM   7817  C CD2 . TYR D 2 162 ? -67.743 23.466  28.151  1.00 62.71  ? 162 TYR D CD2 1 
ATOM   7818  C CE1 . TYR D 2 162 ? -65.378 22.111  28.595  1.00 59.21  ? 162 TYR D CE1 1 
ATOM   7819  C CE2 . TYR D 2 162 ? -67.399 23.079  29.438  1.00 61.45  ? 162 TYR D CE2 1 
ATOM   7820  C CZ  . TYR D 2 162 ? -66.217 22.402  29.652  1.00 65.54  ? 162 TYR D CZ  1 
ATOM   7821  O OH  . TYR D 2 162 ? -65.873 22.017  30.928  1.00 72.22  ? 162 TYR D OH  1 
ATOM   7822  N N   . SER D 2 163 ? -67.981 21.909  22.555  1.00 67.01  ? 163 SER D N   1 
ATOM   7823  C CA  . SER D 2 163 ? -67.831 22.179  21.127  1.00 72.13  ? 163 SER D CA  1 
ATOM   7824  C C   . SER D 2 163 ? -69.060 22.878  20.558  1.00 83.29  ? 163 SER D C   1 
ATOM   7825  O O   . SER D 2 163 ? -68.946 23.917  19.897  1.00 78.18  ? 163 SER D O   1 
ATOM   7826  C CB  . SER D 2 163 ? -67.563 20.873  20.378  1.00 69.93  ? 163 SER D CB  1 
ATOM   7827  O OG  . SER D 2 163 ? -66.173 20.620  20.274  1.00 83.78  ? 163 SER D OG  1 
ATOM   7828  N N   . GLU D 2 164 ? -70.250 22.323  20.808  1.00 81.42  ? 164 GLU D N   1 
ATOM   7829  C CA  . GLU D 2 164 ? -71.467 22.926  20.275  1.00 84.91  ? 164 GLU D CA  1 
ATOM   7830  C C   . GLU D 2 164 ? -71.807 24.223  21.000  1.00 77.84  ? 164 GLU D C   1 
ATOM   7831  O O   . GLU D 2 164 ? -72.258 25.188  20.372  1.00 91.01  ? 164 GLU D O   1 
ATOM   7832  C CB  . GLU D 2 164 ? -72.632 21.939  20.359  1.00 96.95  ? 164 GLU D CB  1 
ATOM   7833  C CG  . GLU D 2 164 ? -73.458 21.853  19.079  1.00 105.56 ? 164 GLU D CG  1 
ATOM   7834  C CD  . GLU D 2 164 ? -74.786 21.141  19.279  1.00 128.18 ? 164 GLU D CD  1 
ATOM   7835  O OE1 . GLU D 2 164 ? -75.657 21.692  19.985  1.00 127.68 ? 164 GLU D OE1 1 
ATOM   7836  O OE2 . GLU D 2 164 ? -74.960 20.031  18.727  1.00 127.21 ? 164 GLU D OE2 1 
ATOM   7837  N N   . GLU D 2 165 ? -71.600 24.264  22.318  1.00 68.37  ? 165 GLU D N   1 
ATOM   7838  C CA  . GLU D 2 165 ? -71.891 25.478  23.075  1.00 73.90  ? 165 GLU D CA  1 
ATOM   7839  C C   . GLU D 2 165 ? -71.042 26.648  22.590  1.00 80.47  ? 165 GLU D C   1 
ATOM   7840  O O   . GLU D 2 165 ? -71.542 27.769  22.440  1.00 78.79  ? 165 GLU D O   1 
ATOM   7841  C CB  . GLU D 2 165 ? -71.670 25.229  24.568  1.00 77.59  ? 165 GLU D CB  1 
ATOM   7842  C CG  . GLU D 2 165 ? -71.877 26.453  25.454  1.00 69.15  ? 165 GLU D CG  1 
ATOM   7843  C CD  . GLU D 2 165 ? -71.613 26.157  26.924  1.00 83.34  ? 165 GLU D CD  1 
ATOM   7844  O OE1 . GLU D 2 165 ? -71.398 24.971  27.265  1.00 83.60  ? 165 GLU D OE1 1 
ATOM   7845  O OE2 . GLU D 2 165 ? -71.615 27.110  27.735  1.00 65.13  ? 165 GLU D OE2 1 
ATOM   7846  N N   . ALA D 2 166 ? -69.752 26.406  22.336  1.00 83.09  ? 166 ALA D N   1 
ATOM   7847  C CA  . ALA D 2 166 ? -68.905 27.446  21.762  1.00 86.21  ? 166 ALA D CA  1 
ATOM   7848  C C   . ALA D 2 166 ? -69.275 27.730  20.313  1.00 84.45  ? 166 ALA D C   1 
ATOM   7849  O O   . ALA D 2 166 ? -69.188 28.879  19.865  1.00 80.98  ? 166 ALA D O   1 
ATOM   7850  C CB  . ALA D 2 166 ? -67.432 27.048  21.859  1.00 67.82  ? 166 ALA D CB  1 
ATOM   7851  N N   . ARG D 2 167 ? -69.675 26.698  19.566  1.00 84.90  ? 167 ARG D N   1 
ATOM   7852  C CA  . ARG D 2 167 ? -70.046 26.892  18.169  1.00 88.26  ? 167 ARG D CA  1 
ATOM   7853  C C   . ARG D 2 167 ? -71.259 27.807  18.040  1.00 94.45  ? 167 ARG D C   1 
ATOM   7854  O O   . ARG D 2 167 ? -71.288 28.691  17.176  1.00 97.68  ? 167 ARG D O   1 
ATOM   7855  C CB  . ARG D 2 167 ? -70.318 25.540  17.508  1.00 97.75  ? 167 ARG D CB  1 
ATOM   7856  C CG  . ARG D 2 167 ? -70.653 25.620  16.025  1.00 107.30 ? 167 ARG D CG  1 
ATOM   7857  C CD  . ARG D 2 167 ? -71.776 24.656  15.653  1.00 103.41 ? 167 ARG D CD  1 
ATOM   7858  N NE  . ARG D 2 167 ? -73.088 25.283  15.745  1.00 98.42  ? 167 ARG D NE  1 
ATOM   7859  C CZ  . ARG D 2 167 ? -73.579 26.130  14.849  1.00 115.84 ? 167 ARG D CZ  1 
ATOM   7860  N NH1 . ARG D 2 167 ? -72.891 26.471  13.771  1.00 116.48 ? 167 ARG D NH1 1 
ATOM   7861  N NH2 . ARG D 2 167 ? -74.789 26.648  15.039  1.00 112.15 ? 167 ARG D NH2 1 
ATOM   7862  N N   . LEU D 2 168 ? -72.271 27.610  18.889  1.00 89.72  ? 168 LEU D N   1 
ATOM   7863  C CA  . LEU D 2 168 ? -73.465 28.447  18.812  1.00 100.28 ? 168 LEU D CA  1 
ATOM   7864  C C   . LEU D 2 168 ? -73.147 29.898  19.152  1.00 97.19  ? 168 LEU D C   1 
ATOM   7865  O O   . LEU D 2 168 ? -73.620 30.821  18.477  1.00 100.19 ? 168 LEU D O   1 
ATOM   7866  C CB  . LEU D 2 168 ? -74.553 27.898  19.738  1.00 99.92  ? 168 LEU D CB  1 
ATOM   7867  C CG  . LEU D 2 168 ? -75.730 27.179  19.069  1.00 107.82 ? 168 LEU D CG  1 
ATOM   7868  C CD1 . LEU D 2 168 ? -76.517 28.138  18.184  1.00 90.81  ? 168 LEU D CD1 1 
ATOM   7869  C CD2 . LEU D 2 168 ? -75.262 25.959  18.274  1.00 95.46  ? 168 LEU D CD2 1 
ATOM   7870  N N   . LYS D 2 169 ? -72.344 30.120  20.196  1.00 100.27 ? 169 LYS D N   1 
ATOM   7871  C CA  . LYS D 2 169 ? -71.938 31.477  20.547  1.00 95.69  ? 169 LYS D CA  1 
ATOM   7872  C C   . LYS D 2 169 ? -71.057 32.088  19.464  1.00 97.14  ? 169 LYS D C   1 
ATOM   7873  O O   . LYS D 2 169 ? -71.155 33.287  19.175  1.00 89.03  ? 169 LYS D O   1 
ATOM   7874  C CB  . LYS D 2 169 ? -71.209 31.471  21.891  1.00 87.87  ? 169 LYS D CB  1 
ATOM   7875  C CG  . LYS D 2 169 ? -70.697 32.830  22.331  1.00 77.71  ? 169 LYS D CG  1 
ATOM   7876  C CD  . LYS D 2 169 ? -71.795 33.632  23.005  1.00 85.48  ? 169 LYS D CD  1 
ATOM   7877  C CE  . LYS D 2 169 ? -71.242 34.474  24.141  1.00 78.00  ? 169 LYS D CE  1 
ATOM   7878  N NZ  . LYS D 2 169 ? -69.972 35.146  23.756  1.00 81.43  ? 169 LYS D NZ  1 
ATOM   7879  N N   . ARG D 2 170 ? -70.185 31.278  18.859  1.00 98.76  ? 170 ARG D N   1 
ATOM   7880  C CA  . ARG D 2 170 ? -69.323 31.775  17.793  1.00 99.35  ? 170 ARG D CA  1 
ATOM   7881  C C   . ARG D 2 170 ? -70.122 32.197  16.566  1.00 107.36 ? 170 ARG D C   1 
ATOM   7882  O O   . ARG D 2 170 ? -69.642 33.006  15.766  1.00 104.96 ? 170 ARG D O   1 
ATOM   7883  C CB  . ARG D 2 170 ? -68.291 30.715  17.412  1.00 91.40  ? 170 ARG D CB  1 
ATOM   7884  C CG  . ARG D 2 170 ? -66.953 31.284  16.982  1.00 80.12  ? 170 ARG D CG  1 
ATOM   7885  C CD  . ARG D 2 170 ? -66.031 30.181  16.505  1.00 79.40  ? 170 ARG D CD  1 
ATOM   7886  N NE  . ARG D 2 170 ? -66.775 29.058  15.947  1.00 83.69  ? 170 ARG D NE  1 
ATOM   7887  C CZ  . ARG D 2 170 ? -66.614 27.796  16.319  1.00 86.69  ? 170 ARG D CZ  1 
ATOM   7888  N NH1 . ARG D 2 170 ? -65.744 27.458  17.257  1.00 81.98  ? 170 ARG D NH1 1 
ATOM   7889  N NH2 . ARG D 2 170 ? -67.343 26.849  15.734  1.00 84.93  ? 170 ARG D NH2 1 
ATOM   7890  N N   . GLU D 2 171 ? -71.326 31.649  16.383  1.00 110.19 ? 171 GLU D N   1 
ATOM   7891  C CA  . GLU D 2 171 ? -72.187 32.132  15.309  1.00 112.71 ? 171 GLU D CA  1 
ATOM   7892  C C   . GLU D 2 171 ? -72.975 33.365  15.732  1.00 114.71 ? 171 GLU D C   1 
ATOM   7893  O O   . GLU D 2 171 ? -73.256 34.233  14.896  1.00 117.53 ? 171 GLU D O   1 
ATOM   7894  C CB  . GLU D 2 171 ? -73.136 31.021  14.845  1.00 123.29 ? 171 GLU D CB  1 
ATOM   7895  C CG  . GLU D 2 171 ? -72.436 29.779  14.288  1.00 122.94 ? 171 GLU D CG  1 
ATOM   7896  C CD  . GLU D 2 171 ? -71.486 30.097  13.142  1.00 127.60 ? 171 GLU D CD  1 
ATOM   7897  O OE1 . GLU D 2 171 ? -71.963 30.495  12.056  1.00 120.33 ? 171 GLU D OE1 1 
ATOM   7898  O OE2 . GLU D 2 171 ? -70.259 29.951  13.333  1.00 118.73 ? 171 GLU D OE2 1 
ATOM   7899  N N   . GLU D 2 172 ? -73.319 33.473  17.017  1.00 111.33 ? 172 GLU D N   1 
ATOM   7900  C CA  . GLU D 2 172 ? -74.046 34.630  17.531  1.00 110.10 ? 172 GLU D CA  1 
ATOM   7901  C C   . GLU D 2 172 ? -73.177 35.877  17.655  1.00 109.13 ? 172 GLU D C   1 
ATOM   7902  O O   . GLU D 2 172 ? -73.713 36.961  17.903  1.00 94.54  ? 172 GLU D O   1 
ATOM   7903  C CB  . GLU D 2 172 ? -74.671 34.300  18.893  1.00 96.30  ? 172 GLU D CB  1 
ATOM   7904  C CG  . GLU D 2 172 ? -75.794 35.246  19.389  1.00 111.53 ? 172 GLU D CG  1 
ATOM   7905  C CD  . GLU D 2 172 ? -76.624 35.906  18.281  1.00 123.38 ? 172 GLU D CD  1 
ATOM   7906  O OE1 . GLU D 2 172 ? -76.208 36.951  17.731  1.00 125.45 ? 172 GLU D OE1 1 
ATOM   7907  O OE2 . GLU D 2 172 ? -77.713 35.383  17.965  1.00 113.92 ? 172 GLU D OE2 1 
ATOM   7908  N N   . ILE D 2 173 ? -71.859 35.778  17.496  1.00 114.35 ? 173 ILE D N   1 
ATOM   7909  C CA  . ILE D 2 173 ? -71.098 37.019  17.379  1.00 110.28 ? 173 ILE D CA  1 
ATOM   7910  C C   . ILE D 2 173 ? -71.397 37.599  15.996  1.00 116.11 ? 173 ILE D C   1 
ATOM   7911  O O   . ILE D 2 173 ? -70.956 37.079  14.966  1.00 110.02 ? 173 ILE D O   1 
ATOM   7912  C CB  . ILE D 2 173 ? -69.594 36.820  17.627  1.00 99.57  ? 173 ILE D CB  1 
ATOM   7913  C CG1 . ILE D 2 173 ? -68.867 38.165  17.570  1.00 99.83  ? 173 ILE D CG1 1 
ATOM   7914  C CG2 . ILE D 2 173 ? -68.962 35.815  16.676  1.00 92.25  ? 173 ILE D CG2 1 
ATOM   7915  C CD1 . ILE D 2 173 ? -68.865 38.918  18.888  1.00 94.49  ? 173 ILE D CD1 1 
ATOM   7916  N N   . SER D 2 174 ? -72.206 38.652  15.974  1.00 118.73 ? 174 SER D N   1 
ATOM   7917  C CA  . SER D 2 174 ? -72.749 39.184  14.734  1.00 119.61 ? 174 SER D CA  1 
ATOM   7918  C C   . SER D 2 174 ? -72.269 40.610  14.505  1.00 112.05 ? 174 SER D C   1 
ATOM   7919  O O   . SER D 2 174 ? -71.370 41.087  15.198  1.00 106.59 ? 174 SER D O   1 
ATOM   7920  C CB  . SER D 2 174 ? -74.281 39.132  14.762  1.00 107.91 ? 174 SER D CB  1 
ATOM   7921  O OG  . SER D 2 174 ? -74.841 39.709  13.595  1.00 103.22 ? 174 SER D OG  1 
ATOM   7922  N N   . PRO E 1 1   ? -63.215 6.706   11.924  1.00 96.98  ? 9   PRO E N   1 
ATOM   7923  C CA  . PRO E 1 1   ? -62.030 7.524   12.209  1.00 94.26  ? 9   PRO E CA  1 
ATOM   7924  C C   . PRO E 1 1   ? -61.816 8.624   11.173  1.00 92.91  ? 9   PRO E C   1 
ATOM   7925  O O   . PRO E 1 1   ? -62.783 9.124   10.596  1.00 113.37 ? 9   PRO E O   1 
ATOM   7926  C CB  . PRO E 1 1   ? -60.884 6.508   12.170  1.00 88.50  ? 9   PRO E CB  1 
ATOM   7927  C CG  . PRO E 1 1   ? -61.376 5.420   11.278  1.00 87.87  ? 9   PRO E CG  1 
ATOM   7928  C CD  . PRO E 1 1   ? -62.862 5.344   11.486  1.00 99.12  ? 9   PRO E CD  1 
ATOM   7929  N N   . GLY E 1 2   ? -60.560 8.991   10.947  1.00 74.94  ? 10  GLY E N   1 
ATOM   7930  C CA  . GLY E 1 2   ? -60.230 10.003  9.962   1.00 60.58  ? 10  GLY E CA  1 
ATOM   7931  C C   . GLY E 1 2   ? -58.782 9.881   9.553   1.00 64.65  ? 10  GLY E C   1 
ATOM   7932  O O   . GLY E 1 2   ? -57.933 9.449   10.339  1.00 58.21  ? 10  GLY E O   1 
ATOM   7933  N N   . ASP E 1 3   ? -58.498 10.259  8.307   1.00 54.73  ? 11  ASP E N   1 
ATOM   7934  C CA  . ASP E 1 3   ? -57.136 10.166  7.798   1.00 47.54  ? 11  ASP E CA  1 
ATOM   7935  C C   . ASP E 1 3   ? -56.208 11.075  8.594   1.00 50.08  ? 11  ASP E C   1 
ATOM   7936  O O   . ASP E 1 3   ? -56.579 12.187  8.978   1.00 49.78  ? 11  ASP E O   1 
ATOM   7937  C CB  . ASP E 1 3   ? -57.099 10.536  6.317   1.00 53.96  ? 11  ASP E CB  1 
ATOM   7938  C CG  . ASP E 1 3   ? -57.792 9.511   5.443   1.00 56.46  ? 11  ASP E CG  1 
ATOM   7939  O OD1 . ASP E 1 3   ? -58.097 8.405   5.944   1.00 54.96  ? 11  ASP E OD1 1 
ATOM   7940  O OD2 . ASP E 1 3   ? -58.033 9.813   4.257   1.00 57.60  ? 11  ASP E OD2 1 
ATOM   7941  N N   . GLN E 1 4   ? -54.994 10.590  8.846   1.00 42.79  ? 12  GLN E N   1 
ATOM   7942  C CA  . GLN E 1 4   ? -54.040 11.282  9.699   1.00 45.11  ? 12  GLN E CA  1 
ATOM   7943  C C   . GLN E 1 4   ? -52.661 11.304  9.059   1.00 41.18  ? 12  GLN E C   1 
ATOM   7944  O O   . GLN E 1 4   ? -52.263 10.364  8.367   1.00 44.14  ? 12  GLN E O   1 
ATOM   7945  C CB  . GLN E 1 4   ? -53.932 10.617  11.074  1.00 51.54  ? 12  GLN E CB  1 
ATOM   7946  C CG  . GLN E 1 4   ? -54.934 11.106  12.102  1.00 46.90  ? 12  GLN E CG  1 
ATOM   7947  C CD  . GLN E 1 4   ? -54.498 10.785  13.515  1.00 58.84  ? 12  GLN E CD  1 
ATOM   7948  O OE1 . GLN E 1 4   ? -53.303 10.626  13.787  1.00 53.44  ? 12  GLN E OE1 1 
ATOM   7949  N NE2 . GLN E 1 4   ? -55.464 10.666  14.422  1.00 46.19  ? 12  GLN E NE2 1 
ATOM   7950  N N   . ILE E 1 5   ? -51.938 12.395  9.305   1.00 46.08  ? 13  ILE E N   1 
ATOM   7951  C CA  . ILE E 1 5   ? -50.511 12.499  9.027   1.00 36.99  ? 13  ILE E CA  1 
ATOM   7952  C C   . ILE E 1 5   ? -49.849 13.089  10.266  1.00 44.86  ? 13  ILE E C   1 
ATOM   7953  O O   . ILE E 1 5   ? -50.417 13.966  10.927  1.00 47.84  ? 13  ILE E O   1 
ATOM   7954  C CB  . ILE E 1 5   ? -50.215 13.343  7.765   1.00 37.89  ? 13  ILE E CB  1 
ATOM   7955  C CG1 . ILE E 1 5   ? -48.766 13.161  7.324   1.00 40.19  ? 13  ILE E CG1 1 
ATOM   7956  C CG2 . ILE E 1 5   ? -50.512 14.822  7.983   1.00 41.14  ? 13  ILE E CG2 1 
ATOM   7957  C CD1 . ILE E 1 5   ? -48.484 13.730  5.959   1.00 41.30  ? 13  ILE E CD1 1 
ATOM   7958  N N   . CYS E 1 6   ? -48.671 12.573  10.609  1.00 48.90  ? 14  CYS E N   1 
ATOM   7959  C CA  . CYS E 1 6   ? -47.991 12.947  11.840  1.00 38.22  ? 14  CYS E CA  1 
ATOM   7960  C C   . CYS E 1 6   ? -46.554 13.334  11.527  1.00 42.00  ? 14  CYS E C   1 
ATOM   7961  O O   . CYS E 1 6   ? -45.974 12.890  10.534  1.00 40.56  ? 14  CYS E O   1 
ATOM   7962  C CB  . CYS E 1 6   ? -47.993 11.803  12.872  1.00 42.65  ? 14  CYS E CB  1 
ATOM   7963  S SG  . CYS E 1 6   ? -49.637 11.198  13.348  1.00 66.82  ? 14  CYS E SG  1 
ATOM   7964  N N   . ILE E 1 7   ? -45.989 14.171  12.389  1.00 42.11  ? 15  ILE E N   1 
ATOM   7965  C CA  . ILE E 1 7   ? -44.590 14.567  12.319  1.00 36.88  ? 15  ILE E CA  1 
ATOM   7966  C C   . ILE E 1 7   ? -43.868 13.896  13.476  1.00 39.49  ? 15  ILE E C   1 
ATOM   7967  O O   . ILE E 1 7   ? -44.392 13.834  14.594  1.00 36.96  ? 15  ILE E O   1 
ATOM   7968  C CB  . ILE E 1 7   ? -44.430 16.100  12.373  1.00 36.36  ? 15  ILE E CB  1 
ATOM   7969  C CG1 . ILE E 1 7   ? -45.328 16.764  11.325  1.00 43.25  ? 15  ILE E CG1 1 
ATOM   7970  C CG2 . ILE E 1 7   ? -42.982 16.503  12.176  1.00 32.22  ? 15  ILE E CG2 1 
ATOM   7971  C CD1 . ILE E 1 7   ? -44.683 16.891  9.967   1.00 36.49  ? 15  ILE E CD1 1 
ATOM   7972  N N   . GLY E 1 8   ? -42.683 13.361  13.204  1.00 32.79  ? 16  GLY E N   1 
ATOM   7973  C CA  . GLY E 1 8   ? -41.981 12.654  14.255  1.00 35.85  ? 16  GLY E CA  1 
ATOM   7974  C C   . GLY E 1 8   ? -40.512 12.529  13.934  1.00 39.38  ? 16  GLY E C   1 
ATOM   7975  O O   . GLY E 1 8   ? -40.023 13.038  12.922  1.00 40.35  ? 16  GLY E O   1 
ATOM   7976  N N   . TYR E 1 9   ? -39.811 11.819  14.812  1.00 37.23  ? 17  TYR E N   1 
ATOM   7977  C CA  . TYR E 1 9   ? -38.365 11.763  14.752  1.00 39.75  ? 17  TYR E CA  1 
ATOM   7978  C C   . TYR E 1 9   ? -37.892 10.359  15.115  1.00 50.18  ? 17  TYR E C   1 
ATOM   7979  O O   . TYR E 1 9   ? -38.641 9.539   15.658  1.00 45.25  ? 17  TYR E O   1 
ATOM   7980  C CB  . TYR E 1 9   ? -37.742 12.827  15.664  1.00 43.46  ? 17  TYR E CB  1 
ATOM   7981  C CG  . TYR E 1 9   ? -38.283 12.840  17.080  1.00 46.43  ? 17  TYR E CG  1 
ATOM   7982  C CD1 . TYR E 1 9   ? -39.465 13.496  17.389  1.00 35.24  ? 17  TYR E CD1 1 
ATOM   7983  C CD2 . TYR E 1 9   ? -37.600 12.202  18.110  1.00 48.05  ? 17  TYR E CD2 1 
ATOM   7984  C CE1 . TYR E 1 9   ? -39.964 13.506  18.682  1.00 49.70  ? 17  TYR E CE1 1 
ATOM   7985  C CE2 . TYR E 1 9   ? -38.087 12.213  19.406  1.00 43.29  ? 17  TYR E CE2 1 
ATOM   7986  C CZ  . TYR E 1 9   ? -39.272 12.862  19.686  1.00 47.99  ? 17  TYR E CZ  1 
ATOM   7987  O OH  . TYR E 1 9   ? -39.763 12.877  20.977  1.00 49.72  ? 17  TYR E OH  1 
ATOM   7988  N N   . HIS E 1 10  ? -36.624 10.102  14.802  1.00 51.35  ? 18  HIS E N   1 
ATOM   7989  C CA  . HIS E 1 10  ? -36.033 8.773   14.891  1.00 46.64  ? 18  HIS E CA  1 
ATOM   7990  C C   . HIS E 1 10  ? -35.859 8.329   16.342  1.00 44.59  ? 18  HIS E C   1 
ATOM   7991  O O   . HIS E 1 10  ? -35.679 9.143   17.251  1.00 50.82  ? 18  HIS E O   1 
ATOM   7992  C CB  . HIS E 1 10  ? -34.682 8.775   14.172  1.00 48.82  ? 18  HIS E CB  1 
ATOM   7993  C CG  . HIS E 1 10  ? -33.928 7.488   14.278  1.00 62.49  ? 18  HIS E CG  1 
ATOM   7994  N ND1 . HIS E 1 10  ? -34.490 6.268   13.972  1.00 62.14  ? 18  HIS E ND1 1 
ATOM   7995  C CD2 . HIS E 1 10  ? -32.650 7.233   14.645  1.00 56.50  ? 18  HIS E CD2 1 
ATOM   7996  C CE1 . HIS E 1 10  ? -33.593 5.315   14.149  1.00 55.06  ? 18  HIS E CE1 1 
ATOM   7997  N NE2 . HIS E 1 10  ? -32.468 5.874   14.559  1.00 67.43  ? 18  HIS E NE2 1 
ATOM   7998  N N   . ALA E 1 11  ? -35.924 7.016   16.552  1.00 49.94  ? 19  ALA E N   1 
ATOM   7999  C CA  . ALA E 1 11  ? -35.600 6.416   17.839  1.00 45.16  ? 19  ALA E CA  1 
ATOM   8000  C C   . ALA E 1 11  ? -35.026 5.030   17.591  1.00 51.25  ? 19  ALA E C   1 
ATOM   8001  O O   . ALA E 1 11  ? -35.461 4.329   16.674  1.00 57.29  ? 19  ALA E O   1 
ATOM   8002  C CB  . ALA E 1 11  ? -36.821 6.335   18.759  1.00 36.44  ? 19  ALA E CB  1 
ATOM   8003  N N   . ASN E 1 12  ? -34.041 4.646   18.402  1.00 47.27  ? 20  ASN E N   1 
ATOM   8004  C CA  . ASN E 1 12  ? -33.403 3.341   18.283  1.00 44.58  ? 20  ASN E CA  1 
ATOM   8005  C C   . ASN E 1 12  ? -33.223 2.768   19.686  1.00 49.29  ? 20  ASN E C   1 
ATOM   8006  O O   . ASN E 1 12  ? -33.789 3.272   20.662  1.00 48.13  ? 20  ASN E O   1 
ATOM   8007  C CB  . ASN E 1 12  ? -32.082 3.442   17.504  1.00 48.27  ? 20  ASN E CB  1 
ATOM   8008  C CG  . ASN E 1 12  ? -31.083 4.387   18.150  1.00 47.27  ? 20  ASN E CG  1 
ATOM   8009  O OD1 . ASN E 1 12  ? -31.304 4.895   19.248  1.00 42.46  ? 20  ASN E OD1 1 
ATOM   8010  N ND2 . ASN E 1 12  ? -29.969 4.621   17.466  1.00 43.11  ? 20  ASN E ND2 1 
ATOM   8011  N N   . ASN E 1 13  ? -32.433 1.699   19.787  1.00 55.65  ? 21  ASN E N   1 
ATOM   8012  C CA  . ASN E 1 13  ? -32.224 0.985   21.041  1.00 63.37  ? 21  ASN E CA  1 
ATOM   8013  C C   . ASN E 1 13  ? -30.967 1.437   21.778  1.00 61.72  ? 21  ASN E C   1 
ATOM   8014  O O   . ASN E 1 13  ? -30.575 0.802   22.762  1.00 60.34  ? 21  ASN E O   1 
ATOM   8015  C CB  . ASN E 1 13  ? -32.164 -0.525  20.784  1.00 62.94  ? 21  ASN E CB  1 
ATOM   8016  C CG  . ASN E 1 13  ? -31.088 -0.903  19.782  1.00 70.95  ? 21  ASN E CG  1 
ATOM   8017  O OD1 . ASN E 1 13  ? -30.568 -0.048  19.065  1.00 74.25  ? 21  ASN E OD1 1 
ATOM   8018  N ND2 . ASN E 1 13  ? -30.746 -2.189  19.730  1.00 73.33  ? 21  ASN E ND2 1 
ATOM   8019  N N   . SER E 1 14  ? -30.330 2.514   21.326  1.00 61.88  ? 22  SER E N   1 
ATOM   8020  C CA  . SER E 1 14  ? -29.084 2.964   21.931  1.00 56.76  ? 22  SER E CA  1 
ATOM   8021  C C   . SER E 1 14  ? -29.298 3.403   23.376  1.00 56.74  ? 22  SER E C   1 
ATOM   8022  O O   . SER E 1 14  ? -30.338 3.968   23.726  1.00 51.64  ? 22  SER E O   1 
ATOM   8023  C CB  . SER E 1 14  ? -28.491 4.117   21.123  1.00 68.73  ? 22  SER E CB  1 
ATOM   8024  O OG  . SER E 1 14  ? -27.642 4.920   21.927  1.00 57.15  ? 22  SER E OG  1 
ATOM   8025  N N   . THR E 1 15  ? -28.301 3.128   24.218  1.00 56.41  ? 23  THR E N   1 
ATOM   8026  C CA  . THR E 1 15  ? -28.306 3.549   25.614  1.00 52.32  ? 23  THR E CA  1 
ATOM   8027  C C   . THR E 1 15  ? -27.222 4.576   25.911  1.00 46.57  ? 23  THR E C   1 
ATOM   8028  O O   . THR E 1 15  ? -26.984 4.885   27.083  1.00 40.75  ? 23  THR E O   1 
ATOM   8029  C CB  . THR E 1 15  ? -28.145 2.340   26.542  1.00 57.63  ? 23  THR E CB  1 
ATOM   8030  O OG1 . THR E 1 15  ? -27.095 1.495   26.051  1.00 55.09  ? 23  THR E OG1 1 
ATOM   8031  C CG2 . THR E 1 15  ? -29.450 1.546   26.635  1.00 45.93  ? 23  THR E CG2 1 
ATOM   8032  N N   . GLU E 1 16  ? -26.563 5.106   24.880  1.00 46.10  ? 24  GLU E N   1 
ATOM   8033  C CA  . GLU E 1 16  ? -25.568 6.151   25.078  1.00 41.60  ? 24  GLU E CA  1 
ATOM   8034  C C   . GLU E 1 16  ? -26.193 7.352   25.772  1.00 53.82  ? 24  GLU E C   1 
ATOM   8035  O O   . GLU E 1 16  ? -27.308 7.772   25.448  1.00 56.42  ? 24  GLU E O   1 
ATOM   8036  C CB  . GLU E 1 16  ? -24.964 6.581   23.742  1.00 49.52  ? 24  GLU E CB  1 
ATOM   8037  C CG  . GLU E 1 16  ? -24.290 5.462   22.962  1.00 72.39  ? 24  GLU E CG  1 
ATOM   8038  C CD  . GLU E 1 16  ? -24.491 5.592   21.456  1.00 95.72  ? 24  GLU E CD  1 
ATOM   8039  O OE1 . GLU E 1 16  ? -23.632 6.217   20.792  1.00 85.35  ? 24  GLU E OE1 1 
ATOM   8040  O OE2 . GLU E 1 16  ? -25.505 5.072   20.939  1.00 81.12  ? 24  GLU E OE2 1 
ATOM   8041  N N   . GLN E 1 17  ? -25.466 7.904   26.737  1.00 52.90  ? 25  GLN E N   1 
ATOM   8042  C CA  . GLN E 1 17  ? -25.928 9.032   27.527  1.00 43.70  ? 25  GLN E CA  1 
ATOM   8043  C C   . GLN E 1 17  ? -24.946 10.186  27.397  1.00 45.37  ? 25  GLN E C   1 
ATOM   8044  O O   . GLN E 1 17  ? -23.728 9.979   27.358  1.00 49.89  ? 25  GLN E O   1 
ATOM   8045  C CB  . GLN E 1 17  ? -26.088 8.639   28.998  1.00 37.93  ? 25  GLN E CB  1 
ATOM   8046  C CG  . GLN E 1 17  ? -27.375 7.902   29.290  1.00 46.92  ? 25  GLN E CG  1 
ATOM   8047  C CD  . GLN E 1 17  ? -27.519 7.557   30.755  1.00 52.70  ? 25  GLN E CD  1 
ATOM   8048  O OE1 . GLN E 1 17  ? -26.713 7.979   31.583  1.00 63.08  ? 25  GLN E OE1 1 
ATOM   8049  N NE2 . GLN E 1 17  ? -28.550 6.790   31.086  1.00 51.40  ? 25  GLN E NE2 1 
ATOM   8050  N N   . VAL E 1 18  ? -25.486 11.403  27.326  1.00 42.96  ? 26  VAL E N   1 
ATOM   8051  C CA  . VAL E 1 18  ? -24.695 12.623  27.296  1.00 32.63  ? 26  VAL E CA  1 
ATOM   8052  C C   . VAL E 1 18  ? -25.224 13.575  28.357  1.00 43.13  ? 26  VAL E C   1 
ATOM   8053  O O   . VAL E 1 18  ? -26.364 13.468  28.816  1.00 44.36  ? 26  VAL E O   1 
ATOM   8054  C CB  . VAL E 1 18  ? -24.717 13.322  25.920  1.00 40.84  ? 26  VAL E CB  1 
ATOM   8055  C CG1 . VAL E 1 18  ? -24.156 12.408  24.840  1.00 40.54  ? 26  VAL E CG1 1 
ATOM   8056  C CG2 . VAL E 1 18  ? -26.132 13.791  25.588  1.00 33.33  ? 26  VAL E CG2 1 
ATOM   8057  N N   . ASP E 1 19  ? -24.378 14.524  28.732  1.00 44.32  ? 27  ASP E N   1 
ATOM   8058  C CA  . ASP E 1 19  ? -24.750 15.571  29.664  1.00 44.01  ? 27  ASP E CA  1 
ATOM   8059  C C   . ASP E 1 19  ? -24.853 16.899  28.925  1.00 43.64  ? 27  ASP E C   1 
ATOM   8060  O O   . ASP E 1 19  ? -24.153 17.135  27.935  1.00 44.22  ? 27  ASP E O   1 
ATOM   8061  C CB  . ASP E 1 19  ? -23.736 15.675  30.809  1.00 41.82  ? 27  ASP E CB  1 
ATOM   8062  C CG  . ASP E 1 19  ? -24.049 14.729  31.958  1.00 58.13  ? 27  ASP E CG  1 
ATOM   8063  O OD1 . ASP E 1 19  ? -24.832 13.775  31.755  1.00 72.93  ? 27  ASP E OD1 1 
ATOM   8064  O OD2 . ASP E 1 19  ? -23.517 14.941  33.068  1.00 67.77  ? 27  ASP E OD2 1 
ATOM   8065  N N   . THR E 1 20  ? -25.759 17.750  29.391  1.00 35.94  ? 28  THR E N   1 
ATOM   8066  C CA  . THR E 1 20  ? -25.893 19.114  28.899  1.00 40.83  ? 28  THR E CA  1 
ATOM   8067  C C   . THR E 1 20  ? -25.771 20.082  30.072  1.00 41.74  ? 28  THR E C   1 
ATOM   8068  O O   . THR E 1 20  ? -25.727 19.683  31.237  1.00 49.56  ? 28  THR E O   1 
ATOM   8069  C CB  . THR E 1 20  ? -27.226 19.324  28.164  1.00 43.13  ? 28  THR E CB  1 
ATOM   8070  O OG1 . THR E 1 20  ? -28.279 19.509  29.117  1.00 37.18  ? 28  THR E OG1 1 
ATOM   8071  C CG2 . THR E 1 20  ? -27.557 18.137  27.258  1.00 40.73  ? 28  THR E CG2 1 
ATOM   8072  N N   . ILE E 1 21  ? -25.734 21.376  29.748  1.00 41.17  ? 29  ILE E N   1 
ATOM   8073  C CA  . ILE E 1 21  ? -25.643 22.408  30.777  1.00 38.73  ? 29  ILE E CA  1 
ATOM   8074  C C   . ILE E 1 21  ? -26.841 22.334  31.720  1.00 44.56  ? 29  ILE E C   1 
ATOM   8075  O O   . ILE E 1 21  ? -26.703 22.516  32.935  1.00 50.24  ? 29  ILE E O   1 
ATOM   8076  C CB  . ILE E 1 21  ? -25.511 23.794  30.113  1.00 42.30  ? 29  ILE E CB  1 
ATOM   8077  C CG1 . ILE E 1 21  ? -24.045 24.137  29.867  1.00 58.17  ? 29  ILE E CG1 1 
ATOM   8078  C CG2 . ILE E 1 21  ? -26.134 24.870  30.969  1.00 62.46  ? 29  ILE E CG2 1 
ATOM   8079  C CD1 . ILE E 1 21  ? -23.301 24.523  31.123  1.00 42.65  ? 29  ILE E CD1 1 
ATOM   8080  N N   . MET E 1 22  ? -28.028 22.040  31.186  1.00 43.25  ? 30  MET E N   1 
ATOM   8081  C CA  . MET E 1 22  ? -29.243 22.026  31.993  1.00 49.95  ? 30  MET E CA  1 
ATOM   8082  C C   . MET E 1 22  ? -29.704 20.626  32.391  1.00 47.31  ? 30  MET E C   1 
ATOM   8083  O O   . MET E 1 22  ? -30.510 20.499  33.320  1.00 42.25  ? 30  MET E O   1 
ATOM   8084  C CB  . MET E 1 22  ? -30.382 22.723  31.237  1.00 51.02  ? 30  MET E CB  1 
ATOM   8085  C CG  . MET E 1 22  ? -29.954 24.004  30.524  1.00 52.26  ? 30  MET E CG  1 
ATOM   8086  S SD  . MET E 1 22  ? -31.173 25.328  30.404  1.00 61.01  ? 30  MET E SD  1 
ATOM   8087  C CE  . MET E 1 22  ? -31.702 25.578  32.086  1.00 53.71  ? 30  MET E CE  1 
ATOM   8088  N N   . GLU E 1 23  ? -29.239 19.577  31.711  1.00 39.15  ? 31  GLU E N   1 
ATOM   8089  C CA  . GLU E 1 23  ? -29.696 18.222  31.981  1.00 50.62  ? 31  GLU E CA  1 
ATOM   8090  C C   . GLU E 1 23  ? -28.514 17.272  32.108  1.00 54.44  ? 31  GLU E C   1 
ATOM   8091  O O   . GLU E 1 23  ? -27.482 17.440  31.452  1.00 55.54  ? 31  GLU E O   1 
ATOM   8092  C CB  . GLU E 1 23  ? -30.627 17.701  30.880  1.00 52.60  ? 31  GLU E CB  1 
ATOM   8093  C CG  . GLU E 1 23  ? -31.910 18.479  30.709  1.00 62.53  ? 31  GLU E CG  1 
ATOM   8094  C CD  . GLU E 1 23  ? -32.808 17.863  29.657  1.00 70.83  ? 31  GLU E CD  1 
ATOM   8095  O OE1 . GLU E 1 23  ? -33.350 16.767  29.916  1.00 71.35  ? 31  GLU E OE1 1 
ATOM   8096  O OE2 . GLU E 1 23  ? -32.966 18.468  28.573  1.00 59.48  ? 31  GLU E OE2 1 
ATOM   8097  N N   . LYS E 1 24  ? -28.690 16.252  32.942  1.00 50.46  ? 32  LYS E N   1 
ATOM   8098  C CA  . LYS E 1 24  ? -27.692 15.213  33.131  1.00 58.68  ? 32  LYS E CA  1 
ATOM   8099  C C   . LYS E 1 24  ? -28.279 13.869  32.727  1.00 48.47  ? 32  LYS E C   1 
ATOM   8100  O O   . LYS E 1 24  ? -29.477 13.626  32.891  1.00 47.88  ? 32  LYS E O   1 
ATOM   8101  C CB  . LYS E 1 24  ? -27.207 15.154  34.588  1.00 56.04  ? 32  LYS E CB  1 
ATOM   8102  C CG  . LYS E 1 24  ? -26.267 16.283  34.986  1.00 63.80  ? 32  LYS E CG  1 
ATOM   8103  C CD  . LYS E 1 24  ? -25.254 15.816  36.024  1.00 61.53  ? 32  LYS E CD  1 
ATOM   8104  C CE  . LYS E 1 24  ? -25.024 16.868  37.104  1.00 72.15  ? 32  LYS E CE  1 
ATOM   8105  N NZ  . LYS E 1 24  ? -26.014 16.773  38.214  1.00 70.05  ? 32  LYS E NZ  1 
ATOM   8106  N N   . ASN E 1 25  ? -27.423 13.005  32.178  1.00 52.79  ? 33  ASN E N   1 
ATOM   8107  C CA  . ASN E 1 25  ? -27.786 11.629  31.837  1.00 54.78  ? 33  ASN E CA  1 
ATOM   8108  C C   . ASN E 1 25  ? -28.978 11.590  30.873  1.00 50.12  ? 33  ASN E C   1 
ATOM   8109  O O   . ASN E 1 25  ? -30.053 11.069  31.181  1.00 46.95  ? 33  ASN E O   1 
ATOM   8110  C CB  . ASN E 1 25  ? -28.068 10.814  33.107  1.00 54.97  ? 33  ASN E CB  1 
ATOM   8111  C CG  . ASN E 1 25  ? -26.831 10.625  33.967  1.00 56.88  ? 33  ASN E CG  1 
ATOM   8112  O OD1 . ASN E 1 25  ? -25.716 10.926  33.540  1.00 64.72  ? 33  ASN E OD1 1 
ATOM   8113  N ND2 . ASN E 1 25  ? -27.022 10.121  35.184  1.00 64.10  ? 33  ASN E ND2 1 
ATOM   8114  N N   . VAL E 1 26  ? -28.763 12.152  29.688  1.00 47.82  ? 34  VAL E N   1 
ATOM   8115  C CA  . VAL E 1 26  ? -29.773 12.197  28.635  1.00 38.94  ? 34  VAL E CA  1 
ATOM   8116  C C   . VAL E 1 26  ? -29.418 11.151  27.589  1.00 39.44  ? 34  VAL E C   1 
ATOM   8117  O O   . VAL E 1 26  ? -28.315 11.173  27.027  1.00 45.41  ? 34  VAL E O   1 
ATOM   8118  C CB  . VAL E 1 26  ? -29.860 13.593  27.998  1.00 45.99  ? 34  VAL E CB  1 
ATOM   8119  C CG1 . VAL E 1 26  ? -30.833 13.582  26.824  1.00 42.14  ? 34  VAL E CG1 1 
ATOM   8120  C CG2 . VAL E 1 26  ? -30.259 14.630  29.038  1.00 43.06  ? 34  VAL E CG2 1 
ATOM   8121  N N   . THR E 1 27  ? -30.350 10.242  27.316  1.00 36.59  ? 35  THR E N   1 
ATOM   8122  C CA  . THR E 1 27  ? -30.118 9.191   26.334  1.00 41.12  ? 35  THR E CA  1 
ATOM   8123  C C   . THR E 1 27  ? -30.281 9.746   24.923  1.00 41.35  ? 35  THR E C   1 
ATOM   8124  O O   . THR E 1 27  ? -31.243 10.466  24.637  1.00 46.20  ? 35  THR E O   1 
ATOM   8125  C CB  . THR E 1 27  ? -31.078 8.025   26.570  1.00 45.50  ? 35  THR E CB  1 
ATOM   8126  O OG1 . THR E 1 27  ? -31.016 7.634   27.946  1.00 48.84  ? 35  THR E OG1 1 
ATOM   8127  C CG2 . THR E 1 27  ? -30.701 6.834   25.697  1.00 38.10  ? 35  THR E CG2 1 
ATOM   8128  N N   . VAL E 1 28  ? -29.336 9.406   24.041  1.00 34.90  ? 36  VAL E N   1 
ATOM   8129  C CA  . VAL E 1 28  ? -29.316 9.899   22.671  1.00 42.61  ? 36  VAL E CA  1 
ATOM   8130  C C   . VAL E 1 28  ? -29.134 8.728   21.711  1.00 47.32  ? 36  VAL E C   1 
ATOM   8131  O O   . VAL E 1 28  ? -28.588 7.681   22.066  1.00 49.31  ? 36  VAL E O   1 
ATOM   8132  C CB  . VAL E 1 28  ? -28.207 10.952  22.446  1.00 44.85  ? 36  VAL E CB  1 
ATOM   8133  C CG1 . VAL E 1 28  ? -28.543 12.239  23.180  1.00 44.54  ? 36  VAL E CG1 1 
ATOM   8134  C CG2 . VAL E 1 28  ? -26.852 10.412  22.892  1.00 38.53  ? 36  VAL E CG2 1 
ATOM   8135  N N   . THR E 1 29  ? -29.601 8.923   20.471  1.00 48.92  ? 37  THR E N   1 
ATOM   8136  C CA  . THR E 1 29  ? -29.523 7.856   19.476  1.00 50.42  ? 37  THR E CA  1 
ATOM   8137  C C   . THR E 1 29  ? -28.090 7.597   19.030  1.00 51.11  ? 37  THR E C   1 
ATOM   8138  O O   . THR E 1 29  ? -27.747 6.459   18.690  1.00 56.64  ? 37  THR E O   1 
ATOM   8139  C CB  . THR E 1 29  ? -30.400 8.181   18.261  1.00 45.25  ? 37  THR E CB  1 
ATOM   8140  O OG1 . THR E 1 29  ? -29.738 9.128   17.411  1.00 42.21  ? 37  THR E OG1 1 
ATOM   8141  C CG2 . THR E 1 29  ? -31.732 8.744   18.703  1.00 42.38  ? 37  THR E CG2 1 
ATOM   8142  N N   . HIS E 1 30  ? -27.246 8.626   19.022  1.00 47.38  ? 38  HIS E N   1 
ATOM   8143  C CA  . HIS E 1 30  ? -25.854 8.469   18.626  1.00 56.11  ? 38  HIS E CA  1 
ATOM   8144  C C   . HIS E 1 30  ? -25.009 9.501   19.360  1.00 58.58  ? 38  HIS E C   1 
ATOM   8145  O O   . HIS E 1 30  ? -25.487 10.589  19.694  1.00 51.51  ? 38  HIS E O   1 
ATOM   8146  C CB  . HIS E 1 30  ? -25.685 8.612   17.109  1.00 52.68  ? 38  HIS E CB  1 
ATOM   8147  C CG  . HIS E 1 30  ? -24.457 7.943   16.570  1.00 77.17  ? 38  HIS E CG  1 
ATOM   8148  N ND1 . HIS E 1 30  ? -23.816 6.916   17.230  1.00 74.49  ? 38  HIS E ND1 1 
ATOM   8149  C CD2 . HIS E 1 30  ? -23.753 8.157   15.433  1.00 85.07  ? 38  HIS E CD2 1 
ATOM   8150  C CE1 . HIS E 1 30  ? -22.771 6.525   16.523  1.00 73.87  ? 38  HIS E CE1 1 
ATOM   8151  N NE2 . HIS E 1 30  ? -22.710 7.262   15.428  1.00 94.58  ? 38  HIS E NE2 1 
ATOM   8152  N N   . ALA E 1 31  ? -23.751 9.142   19.614  1.00 53.29  ? 39  ALA E N   1 
ATOM   8153  C CA  . ALA E 1 31  ? -22.820 10.017  20.312  1.00 46.88  ? 39  ALA E CA  1 
ATOM   8154  C C   . ALA E 1 31  ? -21.396 9.672   19.902  1.00 50.61  ? 39  ALA E C   1 
ATOM   8155  O O   . ALA E 1 31  ? -21.115 8.571   19.423  1.00 58.08  ? 39  ALA E O   1 
ATOM   8156  C CB  . ALA E 1 31  ? -22.973 9.908   21.833  1.00 46.35  ? 39  ALA E CB  1 
ATOM   8157  N N   . GLN E 1 32  ? -20.498 10.633  20.099  1.00 53.75  ? 40  GLN E N   1 
ATOM   8158  C CA  . GLN E 1 32  ? -19.096 10.472  19.750  1.00 43.40  ? 40  GLN E CA  1 
ATOM   8159  C C   . GLN E 1 32  ? -18.231 11.042  20.865  1.00 48.66  ? 40  GLN E C   1 
ATOM   8160  O O   . GLN E 1 32  ? -18.519 12.121  21.394  1.00 47.33  ? 40  GLN E O   1 
ATOM   8161  C CB  . GLN E 1 32  ? -18.772 11.169  18.424  1.00 45.57  ? 40  GLN E CB  1 
ATOM   8162  C CG  . GLN E 1 32  ? -17.293 11.169  18.077  1.00 53.81  ? 40  GLN E CG  1 
ATOM   8163  C CD  . GLN E 1 32  ? -17.051 11.229  16.588  1.00 66.29  ? 40  GLN E CD  1 
ATOM   8164  O OE1 . GLN E 1 32  ? -17.993 11.339  15.799  1.00 65.13  ? 40  GLN E OE1 1 
ATOM   8165  N NE2 . GLN E 1 32  ? -15.783 11.163  16.190  1.00 75.40  ? 40  GLN E NE2 1 
ATOM   8166  N N   . ASP E 1 33  ? -17.171 10.319  21.212  1.00 46.43  ? 41  ASP E N   1 
ATOM   8167  C CA  . ASP E 1 33  ? -16.246 10.734  22.259  1.00 45.85  ? 41  ASP E CA  1 
ATOM   8168  C C   . ASP E 1 33  ? -15.048 11.433  21.626  1.00 47.11  ? 41  ASP E C   1 
ATOM   8169  O O   . ASP E 1 33  ? -14.451 10.916  20.676  1.00 42.74  ? 41  ASP E O   1 
ATOM   8170  C CB  . ASP E 1 33  ? -15.786 9.531   23.088  1.00 46.52  ? 41  ASP E CB  1 
ATOM   8171  C CG  . ASP E 1 33  ? -15.223 9.932   24.450  1.00 61.26  ? 41  ASP E CG  1 
ATOM   8172  O OD1 . ASP E 1 33  ? -14.451 10.913  24.516  1.00 60.55  ? 41  ASP E OD1 1 
ATOM   8173  O OD2 . ASP E 1 33  ? -15.542 9.260   25.456  1.00 62.48  ? 41  ASP E OD2 1 
ATOM   8174  N N   . ILE E 1 34  ? -14.710 12.613  22.148  1.00 39.96  ? 42  ILE E N   1 
ATOM   8175  C CA  . ILE E 1 34  ? -13.576 13.386  21.653  1.00 43.06  ? 42  ILE E CA  1 
ATOM   8176  C C   . ILE E 1 34  ? -12.375 13.301  22.593  1.00 46.96  ? 42  ILE E C   1 
ATOM   8177  O O   . ILE E 1 34  ? -11.390 14.020  22.401  1.00 48.76  ? 42  ILE E O   1 
ATOM   8178  C CB  . ILE E 1 34  ? -13.969 14.852  21.400  1.00 46.86  ? 42  ILE E CB  1 
ATOM   8179  C CG1 . ILE E 1 34  ? -14.518 15.492  22.675  1.00 43.20  ? 42  ILE E CG1 1 
ATOM   8180  C CG2 . ILE E 1 34  ? -14.991 14.949  20.283  1.00 39.51  ? 42  ILE E CG2 1 
ATOM   8181  C CD1 . ILE E 1 34  ? -14.698 16.985  22.568  1.00 42.76  ? 42  ILE E CD1 1 
ATOM   8182  N N   . LEU E 1 35  ? -12.435 12.442  23.607  1.00 42.02  ? 43  LEU E N   1 
ATOM   8183  C CA  . LEU E 1 35  ? -11.309 12.192  24.495  1.00 50.92  ? 43  LEU E CA  1 
ATOM   8184  C C   . LEU E 1 35  ? -10.625 10.887  24.108  1.00 53.89  ? 43  LEU E C   1 
ATOM   8185  O O   . LEU E 1 35  ? -11.290 9.880   23.854  1.00 49.63  ? 43  LEU E O   1 
ATOM   8186  C CB  . LEU E 1 35  ? -11.765 12.125  25.953  1.00 47.01  ? 43  LEU E CB  1 
ATOM   8187  C CG  . LEU E 1 35  ? -10.633 11.897  26.956  1.00 44.71  ? 43  LEU E CG  1 
ATOM   8188  C CD1 . LEU E 1 35  ? -9.880  13.192  27.177  1.00 42.64  ? 43  LEU E CD1 1 
ATOM   8189  C CD2 . LEU E 1 35  ? -11.171 11.363  28.271  1.00 48.57  ? 43  LEU E CD2 1 
ATOM   8190  N N   . GLU E 1 36  ? -9.295  10.909  24.062  1.00 49.58  ? 44  GLU E N   1 
ATOM   8191  C CA  . GLU E 1 36  ? -8.509  9.730   23.717  1.00 53.49  ? 44  GLU E CA  1 
ATOM   8192  C C   . GLU E 1 36  ? -8.015  9.066   24.995  1.00 50.84  ? 44  GLU E C   1 
ATOM   8193  O O   . GLU E 1 36  ? -7.351  9.707   25.816  1.00 49.82  ? 44  GLU E O   1 
ATOM   8194  C CB  . GLU E 1 36  ? -7.332  10.095  22.812  1.00 47.03  ? 44  GLU E CB  1 
ATOM   8195  C CG  . GLU E 1 36  ? -6.558  8.888   22.315  1.00 48.77  ? 44  GLU E CG  1 
ATOM   8196  C CD  . GLU E 1 36  ? -7.440  7.875   21.605  1.00 68.47  ? 44  GLU E CD  1 
ATOM   8197  O OE1 . GLU E 1 36  ? -7.733  8.066   20.404  1.00 62.23  ? 44  GLU E OE1 1 
ATOM   8198  O OE2 . GLU E 1 36  ? -7.844  6.887   22.256  1.00 80.56  ? 44  GLU E OE2 1 
ATOM   8199  N N   . LYS E 1 37  ? -8.336  7.782   25.159  1.00 53.99  ? 45  LYS E N   1 
ATOM   8200  C CA  . LYS E 1 37  ? -7.960  7.038   26.351  1.00 51.78  ? 45  LYS E CA  1 
ATOM   8201  C C   . LYS E 1 37  ? -7.096  5.822   26.060  1.00 51.01  ? 45  LYS E C   1 
ATOM   8202  O O   . LYS E 1 37  ? -6.785  5.071   26.992  1.00 53.03  ? 45  LYS E O   1 
ATOM   8203  C CB  . LYS E 1 37  ? -9.207  6.580   27.122  1.00 57.81  ? 45  LYS E CB  1 
ATOM   8204  C CG  . LYS E 1 37  ? -10.362 7.559   27.124  1.00 61.25  ? 45  LYS E CG  1 
ATOM   8205  C CD  . LYS E 1 37  ? -11.602 6.917   27.730  1.00 59.77  ? 45  LYS E CD  1 
ATOM   8206  C CE  . LYS E 1 37  ? -12.863 7.624   27.274  1.00 61.47  ? 45  LYS E CE  1 
ATOM   8207  N NZ  . LYS E 1 37  ? -12.942 7.719   25.790  1.00 60.86  ? 45  LYS E NZ  1 
ATOM   8208  N N   . THR E 1 38  ? -6.699  5.601   24.811  1.00 60.49  ? 46  THR E N   1 
ATOM   8209  C CA  . THR E 1 38  ? -6.036  4.370   24.409  1.00 70.54  ? 46  THR E CA  1 
ATOM   8210  C C   . THR E 1 38  ? -4.612  4.646   23.944  1.00 59.46  ? 46  THR E C   1 
ATOM   8211  O O   . THR E 1 38  ? -4.358  5.613   23.217  1.00 53.64  ? 46  THR E O   1 
ATOM   8212  C CB  . THR E 1 38  ? -6.820  3.666   23.295  1.00 63.46  ? 46  THR E CB  1 
ATOM   8213  O OG1 . THR E 1 38  ? -7.076  4.594   22.234  1.00 60.15  ? 46  THR E OG1 1 
ATOM   8214  C CG2 . THR E 1 38  ? -8.143  3.142   23.831  1.00 62.55  ? 46  THR E CG2 1 
ATOM   8215  N N   . HIS E 1 39  ? -3.690  3.787   24.373  1.00 52.69  ? 47  HIS E N   1 
ATOM   8216  C CA  . HIS E 1 39  ? -2.308  3.813   23.918  1.00 61.70  ? 47  HIS E CA  1 
ATOM   8217  C C   . HIS E 1 39  ? -1.865  2.388   23.620  1.00 63.28  ? 47  HIS E C   1 
ATOM   8218  O O   . HIS E 1 39  ? -2.393  1.431   24.191  1.00 68.22  ? 47  HIS E O   1 
ATOM   8219  C CB  . HIS E 1 39  ? -1.376  4.455   24.957  1.00 52.93  ? 47  HIS E CB  1 
ATOM   8220  C CG  . HIS E 1 39  ? -1.423  3.798   26.303  1.00 53.06  ? 47  HIS E CG  1 
ATOM   8221  N ND1 . HIS E 1 39  ? -0.720  2.649   26.596  1.00 57.43  ? 47  HIS E ND1 1 
ATOM   8222  C CD2 . HIS E 1 39  ? -2.083  4.134   27.437  1.00 49.79  ? 47  HIS E CD2 1 
ATOM   8223  C CE1 . HIS E 1 39  ? -0.948  2.304   27.851  1.00 55.50  ? 47  HIS E CE1 1 
ATOM   8224  N NE2 . HIS E 1 39  ? -1.772  3.189   28.384  1.00 44.58  ? 47  HIS E NE2 1 
ATOM   8225  N N   . ASN E 1 40  ? -0.892  2.248   22.717  1.00 52.90  ? 48  ASN E N   1 
ATOM   8226  C CA  . ASN E 1 40  ? -0.427  0.915   22.352  1.00 58.95  ? 48  ASN E CA  1 
ATOM   8227  C C   . ASN E 1 40  ? 0.459   0.281   23.420  1.00 60.40  ? 48  ASN E C   1 
ATOM   8228  O O   . ASN E 1 40  ? 0.789   -0.904  23.302  1.00 74.81  ? 48  ASN E O   1 
ATOM   8229  C CB  . ASN E 1 40  ? 0.306   0.942   20.998  1.00 50.24  ? 48  ASN E CB  1 
ATOM   8230  C CG  . ASN E 1 40  ? 1.585   1.781   21.014  1.00 67.02  ? 48  ASN E CG  1 
ATOM   8231  O OD1 . ASN E 1 40  ? 2.092   2.175   22.067  1.00 54.85  ? 48  ASN E OD1 1 
ATOM   8232  N ND2 . ASN E 1 40  ? 2.113   2.053   19.824  1.00 52.54  ? 48  ASN E ND2 1 
ATOM   8233  N N   . GLY E 1 41  ? 0.850   1.031   24.447  1.00 55.63  ? 49  GLY E N   1 
ATOM   8234  C CA  . GLY E 1 41  ? 1.659   0.480   25.520  1.00 62.91  ? 49  GLY E CA  1 
ATOM   8235  C C   . GLY E 1 41  ? 3.077   0.104   25.145  1.00 55.94  ? 49  GLY E C   1 
ATOM   8236  O O   . GLY E 1 41  ? 3.659   -0.779  25.780  1.00 56.49  ? 49  GLY E O   1 
ATOM   8237  N N   . ARG E 1 42  ? 3.648   0.738   24.122  1.00 52.14  ? 50  ARG E N   1 
ATOM   8238  C CA  . ARG E 1 42  ? 4.999   0.429   23.675  1.00 54.59  ? 50  ARG E CA  1 
ATOM   8239  C C   . ARG E 1 42  ? 5.756   1.719   23.392  1.00 66.20  ? 50  ARG E C   1 
ATOM   8240  O O   . ARG E 1 42  ? 5.159   2.750   23.071  1.00 58.66  ? 50  ARG E O   1 
ATOM   8241  C CB  . ARG E 1 42  ? 4.995   -0.466  22.423  1.00 55.85  ? 50  ARG E CB  1 
ATOM   8242  C CG  . ARG E 1 42  ? 3.852   -1.461  22.384  1.00 67.22  ? 50  ARG E CG  1 
ATOM   8243  C CD  . ARG E 1 42  ? 3.936   -2.427  21.203  1.00 72.23  ? 50  ARG E CD  1 
ATOM   8244  N NE  . ARG E 1 42  ? 2.629   -2.722  20.615  1.00 99.72  ? 50  ARG E NE  1 
ATOM   8245  C CZ  . ARG E 1 42  ? 1.550   -3.126  21.278  1.00 99.17  ? 50  ARG E CZ  1 
ATOM   8246  N NH1 . ARG E 1 42  ? 1.578   -3.373  22.578  1.00 92.42  ? 50  ARG E NH1 1 
ATOM   8247  N NH2 . ARG E 1 42  ? 0.408   -3.288  20.615  1.00 88.80  ? 50  ARG E NH2 1 
ATOM   8248  N N   . LEU E 1 43  ? 7.079   1.653   23.528  1.00 52.82  ? 51  LEU E N   1 
ATOM   8249  C CA  . LEU E 1 43  ? 7.939   2.754   23.119  1.00 41.87  ? 51  LEU E CA  1 
ATOM   8250  C C   . LEU E 1 43  ? 8.208   2.644   21.625  1.00 53.65  ? 51  LEU E C   1 
ATOM   8251  O O   . LEU E 1 43  ? 8.616   1.585   21.139  1.00 58.88  ? 51  LEU E O   1 
ATOM   8252  C CB  . LEU E 1 43  ? 9.252   2.738   23.900  1.00 55.39  ? 51  LEU E CB  1 
ATOM   8253  C CG  . LEU E 1 43  ? 9.186   3.047   25.397  1.00 55.15  ? 51  LEU E CG  1 
ATOM   8254  C CD1 . LEU E 1 43  ? 10.539  2.816   26.060  1.00 63.06  ? 51  LEU E CD1 1 
ATOM   8255  C CD2 . LEU E 1 43  ? 8.723   4.469   25.625  1.00 57.88  ? 51  LEU E CD2 1 
ATOM   8256  N N   . CYS E 1 44  ? 7.988   3.736   20.902  1.00 49.81  ? 52  CYS E N   1 
ATOM   8257  C CA  . CYS E 1 44  ? 7.986   3.736   19.447  1.00 58.41  ? 52  CYS E CA  1 
ATOM   8258  C C   . CYS E 1 44  ? 8.998   4.742   18.921  1.00 55.83  ? 52  CYS E C   1 
ATOM   8259  O O   . CYS E 1 44  ? 9.519   5.581   19.659  1.00 57.17  ? 52  CYS E O   1 
ATOM   8260  C CB  . CYS E 1 44  ? 6.592   4.080   18.897  1.00 56.79  ? 52  CYS E CB  1 
ATOM   8261  S SG  . CYS E 1 44  ? 5.263   2.935   19.333  1.00 72.89  ? 52  CYS E SG  1 
ATOM   8262  N N   . ASP E 1 45  ? 9.274   4.646   17.622  1.00 57.88  ? 53  ASP E N   1 
ATOM   8263  C CA  . ASP E 1 45  ? 10.027  5.691   16.946  1.00 52.94  ? 53  ASP E CA  1 
ATOM   8264  C C   . ASP E 1 45  ? 9.213   6.977   16.930  1.00 66.88  ? 53  ASP E C   1 
ATOM   8265  O O   . ASP E 1 45  ? 7.984   6.953   16.811  1.00 67.23  ? 53  ASP E O   1 
ATOM   8266  C CB  . ASP E 1 45  ? 10.368  5.283   15.509  1.00 67.14  ? 53  ASP E CB  1 
ATOM   8267  C CG  . ASP E 1 45  ? 11.071  3.938   15.423  1.00 71.53  ? 53  ASP E CG  1 
ATOM   8268  O OD1 . ASP E 1 45  ? 11.876  3.619   16.323  1.00 72.23  ? 53  ASP E OD1 1 
ATOM   8269  O OD2 . ASP E 1 45  ? 10.815  3.200   14.448  1.00 72.55  ? 53  ASP E OD2 1 
ATOM   8270  N N   . LEU E 1 46  ? 9.901   8.106   17.051  1.00 57.77  ? 54  LEU E N   1 
ATOM   8271  C CA  . LEU E 1 46  ? 9.273   9.417   16.933  1.00 51.56  ? 54  LEU E CA  1 
ATOM   8272  C C   . LEU E 1 46  ? 9.526   9.909   15.514  1.00 57.73  ? 54  LEU E C   1 
ATOM   8273  O O   . LEU E 1 46  ? 10.632  10.347  15.186  1.00 59.44  ? 54  LEU E O   1 
ATOM   8274  C CB  . LEU E 1 46  ? 9.817   10.385  17.977  1.00 48.76  ? 54  LEU E CB  1 
ATOM   8275  C CG  . LEU E 1 46  ? 8.909   11.570  18.297  1.00 49.28  ? 54  LEU E CG  1 
ATOM   8276  C CD1 . LEU E 1 46  ? 7.524   11.084  18.719  1.00 48.99  ? 54  LEU E CD1 1 
ATOM   8277  C CD2 . LEU E 1 46  ? 9.532   12.428  19.383  1.00 54.85  ? 54  LEU E CD2 1 
ATOM   8278  N N   . ASN E 1 47  ? 8.491   9.828   14.674  1.00 58.38  ? 55  ASN E N   1 
ATOM   8279  C CA  . ASN E 1 47  ? 8.585   10.197  13.261  1.00 61.11  ? 55  ASN E CA  1 
ATOM   8280  C C   . ASN E 1 47  ? 9.697   9.415   12.566  1.00 60.92  ? 55  ASN E C   1 
ATOM   8281  O O   . ASN E 1 47  ? 10.576  9.979   11.910  1.00 55.61  ? 55  ASN E O   1 
ATOM   8282  C CB  . ASN E 1 47  ? 8.779   11.706  13.095  1.00 57.16  ? 55  ASN E CB  1 
ATOM   8283  C CG  . ASN E 1 47  ? 7.655   12.503  13.718  1.00 64.21  ? 55  ASN E CG  1 
ATOM   8284  O OD1 . ASN E 1 47  ? 6.514   12.451  13.259  1.00 61.61  ? 55  ASN E OD1 1 
ATOM   8285  N ND2 . ASN E 1 47  ? 7.970   13.242  14.776  1.00 67.13  ? 55  ASN E ND2 1 
ATOM   8286  N N   . GLY E 1 48  A 9.672   8.097   12.750  1.00 60.41  ? 55  GLY E N   1 
ATOM   8287  C CA  . GLY E 1 48  A 10.590  7.207   12.076  1.00 68.11  ? 55  GLY E CA  1 
ATOM   8288  C C   . GLY E 1 48  A 12.008  7.203   12.604  1.00 67.68  ? 55  GLY E C   1 
ATOM   8289  O O   . GLY E 1 48  A 12.865  6.537   12.007  1.00 67.48  ? 55  GLY E O   1 
ATOM   8290  N N   . VAL E 1 49  ? 12.291  7.914   13.693  1.00 64.33  ? 56  VAL E N   1 
ATOM   8291  C CA  . VAL E 1 49  ? 13.628  7.969   14.276  1.00 46.77  ? 56  VAL E CA  1 
ATOM   8292  C C   . VAL E 1 49  ? 13.596  7.220   15.601  1.00 60.70  ? 56  VAL E C   1 
ATOM   8293  O O   . VAL E 1 49  ? 12.806  7.551   16.495  1.00 57.82  ? 56  VAL E O   1 
ATOM   8294  C CB  . VAL E 1 49  ? 14.112  9.415   14.462  1.00 47.48  ? 56  VAL E CB  1 
ATOM   8295  C CG1 . VAL E 1 49  ? 15.498  9.436   15.076  1.00 50.00  ? 56  VAL E CG1 1 
ATOM   8296  C CG2 . VAL E 1 49  ? 14.120  10.142  13.131  1.00 46.72  ? 56  VAL E CG2 1 
ATOM   8297  N N   . LYS E 1 50  ? 14.452  6.208   15.721  1.00 65.40  ? 57  LYS E N   1 
ATOM   8298  C CA  . LYS E 1 50  ? 14.474  5.369   16.910  1.00 59.04  ? 57  LYS E CA  1 
ATOM   8299  C C   . LYS E 1 50  ? 14.991  6.159   18.112  1.00 58.55  ? 57  LYS E C   1 
ATOM   8300  O O   . LYS E 1 50  ? 15.916  6.965   17.976  1.00 51.52  ? 57  LYS E O   1 
ATOM   8301  C CB  . LYS E 1 50  ? 15.351  4.138   16.664  1.00 59.49  ? 57  LYS E CB  1 
ATOM   8302  C CG  . LYS E 1 50  ? 15.707  3.340   17.906  1.00 62.96  ? 57  LYS E CG  1 
ATOM   8303  C CD  . LYS E 1 50  ? 15.388  1.864   17.732  1.00 66.77  ? 57  LYS E CD  1 
ATOM   8304  C CE  . LYS E 1 50  ? 15.665  1.079   19.009  1.00 60.16  ? 57  LYS E CE  1 
ATOM   8305  N NZ  . LYS E 1 50  ? 17.048  0.533   19.044  1.00 67.59  ? 57  LYS E NZ  1 
ATOM   8306  N N   . PRO E 1 51  ? 14.401  5.973   19.291  1.00 48.83  ? 58  PRO E N   1 
ATOM   8307  C CA  . PRO E 1 51  ? 14.962  6.581   20.500  1.00 45.52  ? 58  PRO E CA  1 
ATOM   8308  C C   . PRO E 1 51  ? 16.219  5.861   20.959  1.00 51.45  ? 58  PRO E C   1 
ATOM   8309  O O   . PRO E 1 51  ? 16.464  4.700   20.627  1.00 59.64  ? 58  PRO E O   1 
ATOM   8310  C CB  . PRO E 1 51  ? 13.843  6.424   21.533  1.00 48.98  ? 58  PRO E CB  1 
ATOM   8311  C CG  . PRO E 1 51  ? 13.045  5.263   21.055  1.00 41.17  ? 58  PRO E CG  1 
ATOM   8312  C CD  . PRO E 1 51  ? 13.140  5.259   19.556  1.00 48.00  ? 58  PRO E CD  1 
ATOM   8313  N N   . LEU E 1 52  ? 17.016  6.574   21.751  1.00 56.68  ? 59  LEU E N   1 
ATOM   8314  C CA  . LEU E 1 52  ? 18.181  6.000   22.413  1.00 50.90  ? 59  LEU E CA  1 
ATOM   8315  C C   . LEU E 1 52  ? 17.733  5.445   23.758  1.00 53.83  ? 59  LEU E C   1 
ATOM   8316  O O   . LEU E 1 52  ? 17.303  6.200   24.636  1.00 60.15  ? 59  LEU E O   1 
ATOM   8317  C CB  . LEU E 1 52  ? 19.281  7.045   22.591  1.00 50.09  ? 59  LEU E CB  1 
ATOM   8318  C CG  . LEU E 1 52  ? 20.632  6.519   23.079  1.00 56.38  ? 59  LEU E CG  1 
ATOM   8319  C CD1 . LEU E 1 52  ? 21.292  5.669   22.003  1.00 47.69  ? 59  LEU E CD1 1 
ATOM   8320  C CD2 . LEU E 1 52  ? 21.546  7.662   23.485  1.00 57.86  ? 59  LEU E CD2 1 
ATOM   8321  N N   . ILE E 1 53  ? 17.827  4.130   23.921  1.00 56.40  ? 60  ILE E N   1 
ATOM   8322  C CA  . ILE E 1 53  ? 17.401  3.459   25.143  1.00 50.64  ? 60  ILE E CA  1 
ATOM   8323  C C   . ILE E 1 53  ? 18.651  3.064   25.916  1.00 55.93  ? 60  ILE E C   1 
ATOM   8324  O O   . ILE E 1 53  ? 19.454  2.249   25.445  1.00 70.59  ? 60  ILE E O   1 
ATOM   8325  C CB  . ILE E 1 53  ? 16.509  2.246   24.845  1.00 51.18  ? 60  ILE E CB  1 
ATOM   8326  C CG1 . ILE E 1 53  ? 15.193  2.705   24.216  1.00 56.90  ? 60  ILE E CG1 1 
ATOM   8327  C CG2 . ILE E 1 53  ? 16.226  1.466   26.115  1.00 49.76  ? 60  ILE E CG2 1 
ATOM   8328  C CD1 . ILE E 1 53  ? 14.695  1.809   23.104  1.00 58.81  ? 60  ILE E CD1 1 
ATOM   8329  N N   . LEU E 1 54  ? 18.826  3.652   27.099  1.00 66.27  ? 61  LEU E N   1 
ATOM   8330  C CA  . LEU E 1 54  ? 19.947  3.343   27.989  1.00 60.01  ? 61  LEU E CA  1 
ATOM   8331  C C   . LEU E 1 54  ? 19.416  2.406   29.067  1.00 67.04  ? 61  LEU E C   1 
ATOM   8332  O O   . LEU E 1 54  ? 18.898  2.843   30.096  1.00 77.52  ? 61  LEU E O   1 
ATOM   8333  C CB  . LEU E 1 54  ? 20.536  4.616   28.583  1.00 61.93  ? 61  LEU E CB  1 
ATOM   8334  C CG  . LEU E 1 54  ? 21.013  5.665   27.581  1.00 62.55  ? 61  LEU E CG  1 
ATOM   8335  C CD1 . LEU E 1 54  ? 21.268  6.980   28.287  1.00 56.66  ? 61  LEU E CD1 1 
ATOM   8336  C CD2 . LEU E 1 54  ? 22.261  5.193   26.846  1.00 67.95  ? 61  LEU E CD2 1 
ATOM   8337  N N   . LYS E 1 55  ? 19.553  1.103   28.825  1.00 76.46  ? 62  LYS E N   1 
ATOM   8338  C CA  . LYS E 1 55  ? 18.855  0.092   29.611  1.00 77.70  ? 62  LYS E CA  1 
ATOM   8339  C C   . LYS E 1 55  ? 19.174  0.192   31.098  1.00 79.20  ? 62  LYS E C   1 
ATOM   8340  O O   . LYS E 1 55  ? 18.302  0.544   31.898  1.00 83.53  ? 62  LYS E O   1 
ATOM   8341  C CB  . LYS E 1 55  ? 19.195  -1.304  29.084  1.00 75.70  ? 62  LYS E CB  1 
ATOM   8342  C CG  . LYS E 1 55  ? 18.832  -1.519  27.616  1.00 70.30  ? 62  LYS E CG  1 
ATOM   8343  C CD  . LYS E 1 55  ? 18.335  -2.939  27.365  1.00 85.06  ? 62  LYS E CD  1 
ATOM   8344  C CE  . LYS E 1 55  ? 18.122  -3.207  25.880  1.00 76.50  ? 62  LYS E CE  1 
ATOM   8345  N NZ  . LYS E 1 55  ? 18.227  -4.659  25.553  1.00 67.74  ? 62  LYS E NZ  1 
ATOM   8346  N N   . ASP E 1 56  ? 20.422  -0.078  31.481  1.00 75.18  ? 63  ASP E N   1 
ATOM   8347  C CA  . ASP E 1 56  ? 20.818  -0.046  32.884  1.00 73.12  ? 63  ASP E CA  1 
ATOM   8348  C C   . ASP E 1 56  ? 21.847  1.042   33.164  1.00 78.68  ? 63  ASP E C   1 
ATOM   8349  O O   . ASP E 1 56  ? 22.509  1.019   34.207  1.00 72.94  ? 63  ASP E O   1 
ATOM   8350  C CB  . ASP E 1 56  ? 21.350  -1.412  33.320  1.00 66.53  ? 63  ASP E CB  1 
ATOM   8351  C CG  . ASP E 1 56  ? 20.687  -1.916  34.593  1.00 91.21  ? 63  ASP E CG  1 
ATOM   8352  O OD1 . ASP E 1 56  ? 21.034  -3.026  35.054  1.00 102.42 ? 63  ASP E OD1 1 
ATOM   8353  O OD2 . ASP E 1 56  ? 19.816  -1.199  35.132  1.00 90.54  ? 63  ASP E OD2 1 
ATOM   8354  N N   . CYS E 1 57  ? 21.989  2.002   32.258  1.00 75.17  ? 64  CYS E N   1 
ATOM   8355  C CA  . CYS E 1 57  ? 22.966  3.067   32.401  1.00 76.84  ? 64  CYS E CA  1 
ATOM   8356  C C   . CYS E 1 57  ? 22.296  4.429   32.392  1.00 66.20  ? 64  CYS E C   1 
ATOM   8357  O O   . CYS E 1 57  ? 21.256  4.633   31.758  1.00 59.41  ? 64  CYS E O   1 
ATOM   8358  C CB  . CYS E 1 57  ? 24.005  3.034   31.287  1.00 77.97  ? 64  CYS E CB  1 
ATOM   8359  S SG  . CYS E 1 57  ? 25.179  1.698   31.395  1.00 112.57 ? 64  CYS E SG  1 
ATOM   8360  N N   . SER E 1 58  ? 22.914  5.358   33.107  1.00 65.03  ? 65  SER E N   1 
ATOM   8361  C CA  . SER E 1 58  ? 22.565  6.756   32.977  1.00 65.77  ? 65  SER E CA  1 
ATOM   8362  C C   . SER E 1 58  ? 23.315  7.364   31.794  1.00 62.77  ? 65  SER E C   1 
ATOM   8363  O O   . SER E 1 58  ? 24.152  6.721   31.153  1.00 53.50  ? 65  SER E O   1 
ATOM   8364  C CB  . SER E 1 58  ? 22.884  7.507   34.265  1.00 61.35  ? 65  SER E CB  1 
ATOM   8365  O OG  . SER E 1 58  ? 24.274  7.761   34.356  1.00 69.28  ? 65  SER E OG  1 
ATOM   8366  N N   . VAL E 1 59  ? 22.997  8.626   31.500  1.00 60.61  ? 66  VAL E N   1 
ATOM   8367  C CA  . VAL E 1 59  ? 23.672  9.315   30.405  1.00 53.71  ? 66  VAL E CA  1 
ATOM   8368  C C   . VAL E 1 59  ? 25.162  9.451   30.702  1.00 52.47  ? 66  VAL E C   1 
ATOM   8369  O O   . VAL E 1 59  ? 26.008  9.232   29.826  1.00 42.76  ? 66  VAL E O   1 
ATOM   8370  C CB  . VAL E 1 59  ? 23.001  10.677  30.145  1.00 45.56  ? 66  VAL E CB  1 
ATOM   8371  C CG1 . VAL E 1 59  ? 23.937  11.621  29.402  1.00 39.33  ? 66  VAL E CG1 1 
ATOM   8372  C CG2 . VAL E 1 59  ? 21.698  10.480  29.368  1.00 45.97  ? 66  VAL E CG2 1 
ATOM   8373  N N   . ALA E 1 60  ? 25.506  9.799   31.946  1.00 48.97  ? 67  ALA E N   1 
ATOM   8374  C CA  . ALA E 1 60  ? 26.908  10.010  32.293  1.00 48.67  ? 67  ALA E CA  1 
ATOM   8375  C C   . ALA E 1 60  ? 27.722  8.729   32.134  1.00 56.70  ? 67  ALA E C   1 
ATOM   8376  O O   . ALA E 1 60  ? 28.833  8.754   31.587  1.00 46.06  ? 67  ALA E O   1 
ATOM   8377  C CB  . ALA E 1 60  ? 27.018  10.552  33.719  1.00 41.21  ? 67  ALA E CB  1 
ATOM   8378  N N   . GLY E 1 61  ? 27.186  7.598   32.599  1.00 57.88  ? 68  GLY E N   1 
ATOM   8379  C CA  . GLY E 1 61  ? 27.889  6.337   32.430  1.00 51.46  ? 68  GLY E CA  1 
ATOM   8380  C C   . GLY E 1 61  ? 28.047  5.948   30.974  1.00 53.50  ? 68  GLY E C   1 
ATOM   8381  O O   . GLY E 1 61  ? 29.113  5.486   30.558  1.00 54.37  ? 68  GLY E O   1 
ATOM   8382  N N   . TRP E 1 62  ? 26.994  6.137   30.180  1.00 50.16  ? 69  TRP E N   1 
ATOM   8383  C CA  . TRP E 1 62  ? 27.069  5.823   28.758  1.00 49.22  ? 69  TRP E CA  1 
ATOM   8384  C C   . TRP E 1 62  ? 28.108  6.693   28.052  1.00 60.97  ? 69  TRP E C   1 
ATOM   8385  O O   . TRP E 1 62  ? 28.878  6.198   27.219  1.00 59.45  ? 69  TRP E O   1 
ATOM   8386  C CB  . TRP E 1 62  ? 25.685  5.991   28.133  1.00 55.86  ? 69  TRP E CB  1 
ATOM   8387  C CG  . TRP E 1 62  ? 25.675  6.070   26.649  1.00 59.25  ? 69  TRP E CG  1 
ATOM   8388  C CD1 . TRP E 1 62  ? 25.917  5.055   25.772  1.00 56.36  ? 69  TRP E CD1 1 
ATOM   8389  C CD2 . TRP E 1 62  ? 25.377  7.224   25.858  1.00 56.21  ? 69  TRP E CD2 1 
ATOM   8390  N NE1 . TRP E 1 62  ? 25.803  5.510   24.481  1.00 60.47  ? 69  TRP E NE1 1 
ATOM   8391  C CE2 . TRP E 1 62  ? 25.472  6.839   24.507  1.00 54.52  ? 69  TRP E CE2 1 
ATOM   8392  C CE3 . TRP E 1 62  ? 25.043  8.547   26.162  1.00 56.71  ? 69  TRP E CE3 1 
ATOM   8393  C CZ2 . TRP E 1 62  ? 25.248  7.729   23.461  1.00 52.36  ? 69  TRP E CZ2 1 
ATOM   8394  C CZ3 . TRP E 1 62  ? 24.822  9.430   25.121  1.00 55.49  ? 69  TRP E CZ3 1 
ATOM   8395  C CH2 . TRP E 1 62  ? 24.926  9.018   23.788  1.00 62.12  ? 69  TRP E CH2 1 
ATOM   8396  N N   . LEU E 1 63  ? 28.156  7.988   28.384  1.00 58.31  ? 70  LEU E N   1 
ATOM   8397  C CA  . LEU E 1 63  ? 29.108  8.893   27.742  1.00 56.92  ? 70  LEU E CA  1 
ATOM   8398  C C   . LEU E 1 63  ? 30.547  8.557   28.122  1.00 60.43  ? 70  LEU E C   1 
ATOM   8399  O O   . LEU E 1 63  ? 31.412  8.407   27.250  1.00 56.54  ? 70  LEU E O   1 
ATOM   8400  C CB  . LEU E 1 63  ? 28.789  10.339  28.117  1.00 53.37  ? 70  LEU E CB  1 
ATOM   8401  C CG  . LEU E 1 63  ? 27.660  11.029  27.354  1.00 59.98  ? 70  LEU E CG  1 
ATOM   8402  C CD1 . LEU E 1 63  ? 27.359  12.378  27.985  1.00 49.88  ? 70  LEU E CD1 1 
ATOM   8403  C CD2 . LEU E 1 63  ? 28.019  11.184  25.887  1.00 52.49  ? 70  LEU E CD2 1 
ATOM   8404  N N   . LEU E 1 64  ? 30.825  8.435   29.421  1.00 55.51  ? 71  LEU E N   1 
ATOM   8405  C CA  . LEU E 1 64  ? 32.188  8.191   29.880  1.00 50.13  ? 71  LEU E CA  1 
ATOM   8406  C C   . LEU E 1 64  ? 32.647  6.759   29.638  1.00 53.12  ? 71  LEU E C   1 
ATOM   8407  O O   . LEU E 1 64  ? 33.850  6.489   29.723  1.00 57.69  ? 71  LEU E O   1 
ATOM   8408  C CB  . LEU E 1 64  ? 32.305  8.530   31.366  1.00 42.55  ? 71  LEU E CB  1 
ATOM   8409  C CG  . LEU E 1 64  ? 32.203  10.021  31.687  1.00 49.89  ? 71  LEU E CG  1 
ATOM   8410  C CD1 . LEU E 1 64  ? 31.936  10.248  33.163  1.00 53.26  ? 71  LEU E CD1 1 
ATOM   8411  C CD2 . LEU E 1 64  ? 33.467  10.735  31.250  1.00 47.47  ? 71  LEU E CD2 1 
ATOM   8412  N N   . GLY E 1 65  ? 31.732  5.845   29.337  1.00 54.62  ? 72  GLY E N   1 
ATOM   8413  C CA  . GLY E 1 65  ? 32.108  4.468   29.102  1.00 60.22  ? 72  GLY E CA  1 
ATOM   8414  C C   . GLY E 1 65  ? 32.355  3.696   30.380  1.00 56.33  ? 72  GLY E C   1 
ATOM   8415  O O   . GLY E 1 65  ? 33.459  3.190   30.604  1.00 69.21  ? 72  GLY E O   1 
ATOM   8416  N N   . ASN E 1 66  ? 31.337  3.610   31.226  1.00 48.82  ? 73  ASN E N   1 
ATOM   8417  C CA  . ASN E 1 66  ? 31.416  2.756   32.400  1.00 61.35  ? 73  ASN E CA  1 
ATOM   8418  C C   . ASN E 1 66  ? 31.698  1.321   31.959  1.00 72.96  ? 73  ASN E C   1 
ATOM   8419  O O   . ASN E 1 66  ? 31.109  0.845   30.981  1.00 76.08  ? 73  ASN E O   1 
ATOM   8420  C CB  . ASN E 1 66  ? 30.107  2.833   33.191  1.00 60.28  ? 73  ASN E CB  1 
ATOM   8421  C CG  . ASN E 1 66  ? 30.110  1.975   34.443  1.00 61.40  ? 73  ASN E CG  1 
ATOM   8422  O OD1 . ASN E 1 66  ? 30.277  0.756   34.383  1.00 71.28  ? 73  ASN E OD1 1 
ATOM   8423  N ND2 . ASN E 1 66  ? 29.887  2.609   35.589  1.00 59.81  ? 73  ASN E ND2 1 
ATOM   8424  N N   . PRO E 1 67  ? 32.613  0.618   32.629  1.00 75.62  ? 74  PRO E N   1 
ATOM   8425  C CA  . PRO E 1 67  ? 32.914  -0.764  32.215  1.00 81.61  ? 74  PRO E CA  1 
ATOM   8426  C C   . PRO E 1 67  ? 31.702  -1.683  32.234  1.00 79.29  ? 74  PRO E C   1 
ATOM   8427  O O   . PRO E 1 67  ? 31.613  -2.593  31.399  1.00 79.50  ? 74  PRO E O   1 
ATOM   8428  C CB  . PRO E 1 67  ? 33.987  -1.212  33.223  1.00 73.60  ? 74  PRO E CB  1 
ATOM   8429  C CG  . PRO E 1 67  ? 34.015  -0.152  34.297  1.00 71.95  ? 74  PRO E CG  1 
ATOM   8430  C CD  . PRO E 1 67  ? 33.531  1.106   33.670  1.00 61.12  ? 74  PRO E CD  1 
ATOM   8431  N N   . MET E 1 68  ? 30.755  -1.470  33.146  1.00 69.77  ? 75  MET E N   1 
ATOM   8432  C CA  . MET E 1 68  ? 29.538  -2.267  33.207  1.00 78.71  ? 75  MET E CA  1 
ATOM   8433  C C   . MET E 1 68  ? 28.421  -1.699  32.349  1.00 84.88  ? 75  MET E C   1 
ATOM   8434  O O   . MET E 1 68  ? 27.244  -1.949  32.633  1.00 79.37  ? 75  MET E O   1 
ATOM   8435  C CB  . MET E 1 68  ? 29.069  -2.389  34.657  1.00 77.31  ? 75  MET E CB  1 
ATOM   8436  C CG  . MET E 1 68  ? 30.144  -2.880  35.599  1.00 81.02  ? 75  MET E CG  1 
ATOM   8437  S SD  . MET E 1 68  ? 30.096  -4.673  35.828  1.00 93.35  ? 75  MET E SD  1 
ATOM   8438  C CE  . MET E 1 68  ? 31.005  -5.267  34.401  1.00 67.20  ? 75  MET E CE  1 
ATOM   8439  N N   . CYS E 1 69  ? 28.757  -0.940  31.312  1.00 91.19  ? 76  CYS E N   1 
ATOM   8440  C CA  . CYS E 1 69  ? 27.756  -0.137  30.626  1.00 94.09  ? 76  CYS E CA  1 
ATOM   8441  C C   . CYS E 1 69  ? 27.638  -0.462  29.145  1.00 107.72 ? 76  CYS E C   1 
ATOM   8442  O O   . CYS E 1 69  ? 26.521  -0.646  28.647  1.00 117.69 ? 76  CYS E O   1 
ATOM   8443  C CB  . CYS E 1 69  ? 28.079  1.348   30.826  1.00 81.36  ? 76  CYS E CB  1 
ATOM   8444  S SG  . CYS E 1 69  ? 26.761  2.447   30.371  1.00 121.55 ? 76  CYS E SG  1 
ATOM   8445  N N   . ASP E 1 70  ? 28.756  -0.553  28.421  1.00 99.69  ? 77  ASP E N   1 
ATOM   8446  C CA  . ASP E 1 70  ? 28.716  -0.633  26.959  1.00 113.13 ? 77  ASP E CA  1 
ATOM   8447  C C   . ASP E 1 70  ? 28.379  -2.045  26.472  1.00 113.43 ? 77  ASP E C   1 
ATOM   8448  O O   . ASP E 1 70  ? 29.144  -2.700  25.763  1.00 109.41 ? 77  ASP E O   1 
ATOM   8449  C CB  . ASP E 1 70  ? 30.030  -0.149  26.359  1.00 111.29 ? 77  ASP E CB  1 
ATOM   8450  C CG  . ASP E 1 70  ? 29.934  0.088   24.861  1.00 123.34 ? 77  ASP E CG  1 
ATOM   8451  O OD1 . ASP E 1 70  ? 28.806  0.040   24.320  1.00 125.55 ? 77  ASP E OD1 1 
ATOM   8452  O OD2 . ASP E 1 70  ? 30.982  0.324   24.225  1.00 115.44 ? 77  ASP E OD2 1 
ATOM   8453  N N   . GLU E 1 71  ? 27.191  -2.506  26.860  1.00 117.55 ? 78  GLU E N   1 
ATOM   8454  C CA  . GLU E 1 71  ? 26.525  -3.562  26.112  1.00 116.64 ? 78  GLU E CA  1 
ATOM   8455  C C   . GLU E 1 71  ? 25.891  -3.023  24.838  1.00 121.11 ? 78  GLU E C   1 
ATOM   8456  O O   . GLU E 1 71  ? 25.367  -3.809  24.039  1.00 119.43 ? 78  GLU E O   1 
ATOM   8457  C CB  . GLU E 1 71  ? 25.460  -4.249  26.975  1.00 106.99 ? 78  GLU E CB  1 
ATOM   8458  C CG  . GLU E 1 71  ? 25.966  -4.758  28.318  1.00 114.06 ? 78  GLU E CG  1 
ATOM   8459  C CD  . GLU E 1 71  ? 25.821  -3.726  29.420  1.00 119.00 ? 78  GLU E CD  1 
ATOM   8460  O OE1 . GLU E 1 71  ? 24.895  -2.892  29.336  1.00 116.24 ? 78  GLU E OE1 1 
ATOM   8461  O OE2 . GLU E 1 71  ? 26.635  -3.745  30.368  1.00 114.98 ? 78  GLU E OE2 1 
ATOM   8462  N N   . PHE E 1 72  ? 25.943  -1.704  24.640  1.00 114.22 ? 79  PHE E N   1 
ATOM   8463  C CA  . PHE E 1 72  ? 25.348  -1.021  23.505  1.00 114.69 ? 79  PHE E CA  1 
ATOM   8464  C C   . PHE E 1 72  ? 26.203  -1.194  22.250  1.00 112.05 ? 79  PHE E C   1 
ATOM   8465  O O   . PHE E 1 72  ? 27.322  -1.715  22.279  1.00 96.24  ? 79  PHE E O   1 
ATOM   8466  C CB  . PHE E 1 72  ? 25.171  0.473   23.803  1.00 111.34 ? 79  PHE E CB  1 
ATOM   8467  C CG  . PHE E 1 72  ? 24.510  0.770   25.126  1.00 114.36 ? 79  PHE E CG  1 
ATOM   8468  C CD1 . PHE E 1 72  ? 23.152  0.550   25.312  1.00 106.25 ? 79  PHE E CD1 1 
ATOM   8469  C CD2 . PHE E 1 72  ? 25.251  1.283   26.180  1.00 107.20 ? 79  PHE E CD2 1 
ATOM   8470  C CE1 . PHE E 1 72  ? 22.548  0.830   26.532  1.00 88.46  ? 79  PHE E CE1 1 
ATOM   8471  C CE2 . PHE E 1 72  ? 24.652  1.564   27.399  1.00 102.03 ? 79  PHE E CE2 1 
ATOM   8472  C CZ  . PHE E 1 72  ? 23.301  1.337   27.574  1.00 97.02  ? 79  PHE E CZ  1 
ATOM   8473  N N   . ILE E 1 73  ? 25.651  -0.716  21.138  1.00 108.95 ? 80  ILE E N   1 
ATOM   8474  C CA  . ILE E 1 73  ? 26.288  -0.718  19.827  1.00 92.21  ? 80  ILE E CA  1 
ATOM   8475  C C   . ILE E 1 73  ? 26.212  0.733   19.364  1.00 85.97  ? 80  ILE E C   1 
ATOM   8476  O O   . ILE E 1 73  ? 25.779  1.607   20.124  1.00 82.88  ? 80  ILE E O   1 
ATOM   8477  C CB  . ILE E 1 73  ? 25.594  -1.710  18.864  1.00 92.42  ? 80  ILE E CB  1 
ATOM   8478  C CG1 . ILE E 1 73  ? 25.582  -3.126  19.447  1.00 106.10 ? 80  ILE E CG1 1 
ATOM   8479  C CG2 . ILE E 1 73  ? 26.317  -1.857  17.530  1.00 93.47  ? 80  ILE E CG2 1 
ATOM   8480  C CD1 . ILE E 1 73  ? 24.308  -3.519  20.164  1.00 109.74 ? 80  ILE E CD1 1 
ATOM   8481  N N   . ARG E 1 74  ? 26.655  1.012   18.147  1.00 82.90  ? 81  ARG E N   1 
ATOM   8482  C CA  . ARG E 1 74  ? 26.656  2.370   17.628  1.00 81.62  ? 81  ARG E CA  1 
ATOM   8483  C C   . ARG E 1 74  ? 25.241  2.775   17.244  1.00 80.19  ? 81  ARG E C   1 
ATOM   8484  O O   . ARG E 1 74  ? 24.629  2.160   16.362  1.00 74.06  ? 81  ARG E O   1 
ATOM   8485  C CB  . ARG E 1 74  ? 27.584  2.468   16.423  1.00 68.04  ? 81  ARG E CB  1 
ATOM   8486  C CG  . ARG E 1 74  ? 29.035  2.588   16.814  1.00 85.96  ? 81  ARG E CG  1 
ATOM   8487  C CD  . ARG E 1 74  ? 29.956  2.624   15.618  1.00 97.70  ? 81  ARG E CD  1 
ATOM   8488  N NE  . ARG E 1 74  ? 30.903  3.717   15.774  1.00 98.12  ? 81  ARG E NE  1 
ATOM   8489  C CZ  . ARG E 1 74  ? 32.167  3.573   16.144  1.00 100.93 ? 81  ARG E CZ  1 
ATOM   8490  N NH1 . ARG E 1 74  ? 32.700  2.377   16.344  1.00 102.40 ? 81  ARG E NH1 1 
ATOM   8491  N NH2 . ARG E 1 74  ? 32.920  4.658   16.305  1.00 94.43  ? 81  ARG E NH2 1 
ATOM   8492  N N   . VAL E 1 75  ? 24.715  3.796   17.912  1.00 77.97  ? 82  VAL E N   1 
ATOM   8493  C CA  . VAL E 1 75  ? 23.474  4.444   17.507  1.00 66.00  ? 82  VAL E CA  1 
ATOM   8494  C C   . VAL E 1 75  ? 23.848  5.820   16.959  1.00 58.90  ? 82  VAL E C   1 
ATOM   8495  O O   . VAL E 1 75  ? 24.260  6.704   17.730  1.00 51.99  ? 82  VAL E O   1 
ATOM   8496  C CB  . VAL E 1 75  ? 22.475  4.547   18.669  1.00 64.15  ? 82  VAL E CB  1 
ATOM   8497  C CG1 . VAL E 1 75  ? 21.362  5.530   18.331  1.00 64.22  ? 82  VAL E CG1 1 
ATOM   8498  C CG2 . VAL E 1 75  ? 21.898  3.181   18.986  1.00 68.37  ? 82  VAL E CG2 1 
ATOM   8499  N N   . PRO E 1 76  ? 23.760  6.038   15.644  1.00 51.28  ? 83  PRO E N   1 
ATOM   8500  C CA  . PRO E 1 76  ? 24.204  7.312   15.071  1.00 55.66  ? 83  PRO E CA  1 
ATOM   8501  C C   . PRO E 1 76  ? 23.160  8.422   15.109  1.00 67.34  ? 83  PRO E C   1 
ATOM   8502  O O   . PRO E 1 76  ? 23.501  9.579   14.817  1.00 63.11  ? 83  PRO E O   1 
ATOM   8503  C CB  . PRO E 1 76  ? 24.543  6.927   13.631  1.00 58.84  ? 83  PRO E CB  1 
ATOM   8504  C CG  . PRO E 1 76  ? 23.486  5.902   13.318  1.00 61.90  ? 83  PRO E CG  1 
ATOM   8505  C CD  . PRO E 1 76  ? 23.343  5.092   14.597  1.00 58.35  ? 83  PRO E CD  1 
ATOM   8506  N N   . GLU E 1 77  A 21.910  8.123   15.453  1.00 63.28  ? 83  GLU E N   1 
ATOM   8507  C CA  . GLU E 1 77  A 20.853  9.123   15.415  1.00 56.32  ? 83  GLU E CA  1 
ATOM   8508  C C   . GLU E 1 77  A 19.729  8.669   16.334  1.00 59.35  ? 83  GLU E C   1 
ATOM   8509  O O   . GLU E 1 77  A 19.424  7.477   16.393  1.00 62.84  ? 83  GLU E O   1 
ATOM   8510  C CB  . GLU E 1 77  A 20.340  9.317   13.982  1.00 58.89  ? 83  GLU E CB  1 
ATOM   8511  C CG  . GLU E 1 77  A 19.147  10.248  13.850  1.00 83.72  ? 83  GLU E CG  1 
ATOM   8512  C CD  . GLU E 1 77  A 18.965  10.775  12.436  1.00 91.69  ? 83  GLU E CD  1 
ATOM   8513  O OE1 . GLU E 1 77  A 19.206  10.006  11.480  1.00 97.12  ? 83  GLU E OE1 1 
ATOM   8514  O OE2 . GLU E 1 77  A 18.573  11.953  12.282  1.00 91.62  ? 83  GLU E OE2 1 
ATOM   8515  N N   . TRP E 1 78  ? 19.125  9.615   17.052  1.00 60.32  ? 84  TRP E N   1 
ATOM   8516  C CA  . TRP E 1 78  ? 17.962  9.294   17.868  1.00 57.30  ? 84  TRP E CA  1 
ATOM   8517  C C   . TRP E 1 78  ? 17.083  10.529  18.023  1.00 57.94  ? 84  TRP E C   1 
ATOM   8518  O O   . TRP E 1 78  ? 17.524  11.664  17.820  1.00 60.84  ? 84  TRP E O   1 
ATOM   8519  C CB  . TRP E 1 78  ? 18.367  8.727   19.237  1.00 51.10  ? 84  TRP E CB  1 
ATOM   8520  C CG  . TRP E 1 78  ? 19.197  9.650   20.065  1.00 54.34  ? 84  TRP E CG  1 
ATOM   8521  C CD1 . TRP E 1 78  ? 18.746  10.625  20.904  1.00 55.46  ? 84  TRP E CD1 1 
ATOM   8522  C CD2 . TRP E 1 78  ? 20.626  9.679   20.148  1.00 50.44  ? 84  TRP E CD2 1 
ATOM   8523  N NE1 . TRP E 1 78  ? 19.805  11.265  21.499  1.00 49.30  ? 84  TRP E NE1 1 
ATOM   8524  C CE2 . TRP E 1 78  ? 20.971  10.705  21.050  1.00 49.44  ? 84  TRP E CE2 1 
ATOM   8525  C CE3 . TRP E 1 78  ? 21.647  8.941   19.542  1.00 52.26  ? 84  TRP E CE3 1 
ATOM   8526  C CZ2 . TRP E 1 78  ? 22.295  11.010  21.365  1.00 46.25  ? 84  TRP E CZ2 1 
ATOM   8527  C CZ3 . TRP E 1 78  ? 22.960  9.248   19.853  1.00 60.87  ? 84  TRP E CZ3 1 
ATOM   8528  C CH2 . TRP E 1 78  ? 23.273  10.274  20.757  1.00 48.55  ? 84  TRP E CH2 1 
ATOM   8529  N N   . SER E 1 79  ? 15.819  10.287  18.375  1.00 51.22  ? 85  SER E N   1 
ATOM   8530  C CA  . SER E 1 79  ? 14.831  11.347  18.538  1.00 55.26  ? 85  SER E CA  1 
ATOM   8531  C C   . SER E 1 79  ? 14.619  11.760  19.988  1.00 51.38  ? 85  SER E C   1 
ATOM   8532  O O   . SER E 1 79  ? 14.323  12.930  20.251  1.00 48.65  ? 85  SER E O   1 
ATOM   8533  C CB  . SER E 1 79  ? 13.486  10.912  17.947  1.00 51.21  ? 85  SER E CB  1 
ATOM   8534  O OG  . SER E 1 79  ? 13.137  9.614   18.393  1.00 48.28  ? 85  SER E OG  1 
ATOM   8535  N N   . TYR E 1 80  ? 14.746  10.830  20.928  1.00 49.03  ? 86  TYR E N   1 
ATOM   8536  C CA  . TYR E 1 80  ? 14.688  11.144  22.349  1.00 50.34  ? 86  TYR E CA  1 
ATOM   8537  C C   . TYR E 1 80  ? 15.459  10.056  23.082  1.00 47.85  ? 86  TYR E C   1 
ATOM   8538  O O   . TYR E 1 80  ? 15.915  9.083   22.477  1.00 49.01  ? 86  TYR E O   1 
ATOM   8539  C CB  . TYR E 1 80  ? 13.242  11.270  22.850  1.00 37.72  ? 86  TYR E CB  1 
ATOM   8540  C CG  . TYR E 1 80  ? 12.411  10.019  22.684  1.00 45.43  ? 86  TYR E CG  1 
ATOM   8541  C CD1 . TYR E 1 80  ? 11.919  9.648   21.436  1.00 48.02  ? 86  TYR E CD1 1 
ATOM   8542  C CD2 . TYR E 1 80  ? 12.109  9.214   23.773  1.00 36.55  ? 86  TYR E CD2 1 
ATOM   8543  C CE1 . TYR E 1 80  ? 11.157  8.503   21.277  1.00 45.06  ? 86  TYR E CE1 1 
ATOM   8544  C CE2 . TYR E 1 80  ? 11.346  8.069   23.625  1.00 48.89  ? 86  TYR E CE2 1 
ATOM   8545  C CZ  . TYR E 1 80  ? 10.873  7.719   22.375  1.00 44.13  ? 86  TYR E CZ  1 
ATOM   8546  O OH  . TYR E 1 80  ? 10.122  6.577   22.228  1.00 46.21  ? 86  TYR E OH  1 
ATOM   8547  N N   . ILE E 1 81  ? 15.618  10.237  24.389  1.00 42.66  ? 87  ILE E N   1 
ATOM   8548  C CA  . ILE E 1 81  ? 16.391  9.321   25.220  1.00 49.67  ? 87  ILE E CA  1 
ATOM   8549  C C   . ILE E 1 81  ? 15.479  8.743   26.292  1.00 57.81  ? 87  ILE E C   1 
ATOM   8550  O O   . ILE E 1 81  ? 14.787  9.492   26.992  1.00 54.74  ? 87  ILE E O   1 
ATOM   8551  C CB  . ILE E 1 81  ? 17.601  10.019  25.864  1.00 46.63  ? 87  ILE E CB  1 
ATOM   8552  C CG1 . ILE E 1 81  ? 18.595  10.459  24.789  1.00 50.53  ? 87  ILE E CG1 1 
ATOM   8553  C CG2 . ILE E 1 81  ? 18.259  9.093   26.877  1.00 48.51  ? 87  ILE E CG2 1 
ATOM   8554  C CD1 . ILE E 1 81  ? 19.805  11.173  25.342  1.00 30.75  ? 87  ILE E CD1 1 
ATOM   8555  N N   . VAL E 1 82  ? 15.488  7.418   26.422  1.00 53.22  ? 88  VAL E N   1 
ATOM   8556  C CA  . VAL E 1 82  ? 14.755  6.719   27.470  1.00 44.40  ? 88  VAL E CA  1 
ATOM   8557  C C   . VAL E 1 82  ? 15.753  6.304   28.544  1.00 49.81  ? 88  VAL E C   1 
ATOM   8558  O O   . VAL E 1 82  ? 16.645  5.483   28.301  1.00 50.40  ? 88  VAL E O   1 
ATOM   8559  C CB  . VAL E 1 82  ? 13.994  5.506   26.922  1.00 50.40  ? 88  VAL E CB  1 
ATOM   8560  C CG1 . VAL E 1 82  ? 13.443  4.676   28.066  1.00 35.48  ? 88  VAL E CG1 1 
ATOM   8561  C CG2 . VAL E 1 82  ? 12.867  5.961   26.003  1.00 55.53  ? 88  VAL E CG2 1 
ATOM   8562  N N   . GLU E 1 83  ? 15.605  6.875   29.733  1.00 47.45  ? 89  GLU E N   1 
ATOM   8563  C CA  . GLU E 1 83  ? 16.378  6.491   30.903  1.00 49.06  ? 89  GLU E CA  1 
ATOM   8564  C C   . GLU E 1 83  ? 15.447  5.823   31.902  1.00 59.00  ? 89  GLU E C   1 
ATOM   8565  O O   . GLU E 1 83  ? 14.297  6.243   32.070  1.00 59.68  ? 89  GLU E O   1 
ATOM   8566  C CB  . GLU E 1 83  ? 17.044  7.708   31.554  1.00 56.93  ? 89  GLU E CB  1 
ATOM   8567  C CG  . GLU E 1 83  ? 18.555  7.737   31.491  1.00 56.00  ? 89  GLU E CG  1 
ATOM   8568  C CD  . GLU E 1 83  ? 19.137  8.826   32.377  1.00 74.81  ? 89  GLU E CD  1 
ATOM   8569  O OE1 . GLU E 1 83  ? 18.344  9.482   33.086  1.00 74.87  ? 89  GLU E OE1 1 
ATOM   8570  O OE2 . GLU E 1 83  ? 20.374  9.031   32.363  1.00 66.07  ? 89  GLU E OE2 1 
ATOM   8571  N N   . ARG E 1 84  ? 15.936  4.778   32.556  1.00 66.52  ? 90  ARG E N   1 
ATOM   8572  C CA  . ARG E 1 84  ? 15.155  4.199   33.633  1.00 64.46  ? 90  ARG E CA  1 
ATOM   8573  C C   . ARG E 1 84  ? 15.145  5.153   34.822  1.00 63.05  ? 90  ARG E C   1 
ATOM   8574  O O   . ARG E 1 84  ? 16.012  6.019   34.959  1.00 60.15  ? 90  ARG E O   1 
ATOM   8575  C CB  . ARG E 1 84  ? 15.710  2.830   34.016  1.00 57.87  ? 90  ARG E CB  1 
ATOM   8576  C CG  . ARG E 1 84  ? 15.555  1.810   32.901  1.00 62.51  ? 90  ARG E CG  1 
ATOM   8577  C CD  . ARG E 1 84  ? 15.180  0.441   33.430  1.00 69.48  ? 90  ARG E CD  1 
ATOM   8578  N NE  . ARG E 1 84  ? 15.712  -0.625  32.589  1.00 79.44  ? 90  ARG E NE  1 
ATOM   8579  C CZ  . ARG E 1 84  ? 16.527  -1.581  33.012  1.00 81.66  ? 90  ARG E CZ  1 
ATOM   8580  N NH1 . ARG E 1 84  ? 16.926  -1.641  34.272  1.00 72.44  ? 90  ARG E NH1 1 
ATOM   8581  N NH2 . ARG E 1 84  ? 16.956  -2.496  32.148  1.00 73.17  ? 90  ARG E NH2 1 
ATOM   8582  N N   . THR E 1 85  ? 14.125  5.008   35.672  1.00 66.89  ? 91  THR E N   1 
ATOM   8583  C CA  . THR E 1 85  ? 13.911  5.979   36.742  1.00 60.29  ? 91  THR E CA  1 
ATOM   8584  C C   . THR E 1 85  ? 15.127  6.069   37.655  1.00 68.89  ? 91  THR E C   1 
ATOM   8585  O O   . THR E 1 85  ? 15.574  7.166   38.011  1.00 69.29  ? 91  THR E O   1 
ATOM   8586  C CB  . THR E 1 85  ? 12.655  5.615   37.533  1.00 67.28  ? 91  THR E CB  1 
ATOM   8587  O OG1 . THR E 1 85  ? 11.518  5.676   36.663  1.00 71.55  ? 91  THR E OG1 1 
ATOM   8588  C CG2 . THR E 1 85  ? 12.449  6.579   38.697  1.00 69.56  ? 91  THR E CG2 1 
ATOM   8589  N N   . ASN E 1 86  ? 15.687  4.921   38.033  1.00 77.11  ? 92  ASN E N   1 
ATOM   8590  C CA  . ASN E 1 86  ? 16.932  4.860   38.794  1.00 72.54  ? 92  ASN E CA  1 
ATOM   8591  C C   . ASN E 1 86  ? 17.879  3.922   38.060  1.00 71.66  ? 92  ASN E C   1 
ATOM   8592  O O   . ASN E 1 86  ? 17.842  2.701   38.261  1.00 71.58  ? 92  ASN E O   1 
ATOM   8593  C CB  . ASN E 1 86  ? 16.691  4.399   40.230  1.00 70.90  ? 92  ASN E CB  1 
ATOM   8594  C CG  . ASN E 1 86  ? 15.380  4.913   40.792  1.00 87.56  ? 92  ASN E CG  1 
ATOM   8595  O OD1 . ASN E 1 86  ? 15.192  6.119   40.955  1.00 88.42  ? 92  ASN E OD1 1 
ATOM   8596  N ND2 . ASN E 1 86  ? 14.462  3.999   41.086  1.00 87.96  ? 92  ASN E ND2 1 
ATOM   8597  N N   . PRO E 1 87  ? 18.727  4.453   37.182  1.00 70.29  ? 93  PRO E N   1 
ATOM   8598  C CA  . PRO E 1 87  ? 19.732  3.609   36.531  1.00 68.21  ? 93  PRO E CA  1 
ATOM   8599  C C   . PRO E 1 87  ? 20.737  3.083   37.545  1.00 70.76  ? 93  PRO E C   1 
ATOM   8600  O O   . PRO E 1 87  ? 20.962  3.678   38.603  1.00 64.17  ? 93  PRO E O   1 
ATOM   8601  C CB  . PRO E 1 87  ? 20.398  4.556   35.524  1.00 62.63  ? 93  PRO E CB  1 
ATOM   8602  C CG  . PRO E 1 87  ? 19.415  5.686   35.352  1.00 67.31  ? 93  PRO E CG  1 
ATOM   8603  C CD  . PRO E 1 87  ? 18.782  5.841   36.699  1.00 64.09  ? 93  PRO E CD  1 
ATOM   8604  N N   . ALA E 1 88  ? 21.330  1.937   37.215  1.00 73.78  ? 94  ALA E N   1 
ATOM   8605  C CA  . ALA E 1 88  ? 22.257  1.268   38.120  1.00 77.40  ? 94  ALA E CA  1 
ATOM   8606  C C   . ALA E 1 88  ? 23.699  1.726   37.924  1.00 69.10  ? 94  ALA E C   1 
ATOM   8607  O O   . ALA E 1 88  ? 24.382  2.065   38.895  1.00 74.42  ? 94  ALA E O   1 
ATOM   8608  C CB  . ALA E 1 88  ? 22.158  -0.251  37.941  1.00 62.02  ? 94  ALA E CB  1 
ATOM   8609  N N   . ASN E 1 89  ? 24.176  1.745   36.684  1.00 71.87  ? 95  ASN E N   1 
ATOM   8610  C CA  . ASN E 1 89  ? 25.568  2.076   36.386  1.00 66.84  ? 95  ASN E CA  1 
ATOM   8611  C C   . ASN E 1 89  ? 25.630  3.527   35.918  1.00 78.69  ? 95  ASN E C   1 
ATOM   8612  O O   . ASN E 1 89  ? 25.557  3.818   34.723  1.00 80.64  ? 95  ASN E O   1 
ATOM   8613  C CB  . ASN E 1 89  ? 26.134  1.120   35.343  1.00 73.05  ? 95  ASN E CB  1 
ATOM   8614  C CG  . ASN E 1 89  ? 25.773  -0.326  35.622  1.00 80.08  ? 95  ASN E CG  1 
ATOM   8615  O OD1 . ASN E 1 89  ? 25.293  -1.038  34.740  1.00 82.31  ? 95  ASN E OD1 1 
ATOM   8616  N ND2 . ASN E 1 89  ? 25.995  -0.765  36.857  1.00 64.50  ? 95  ASN E ND2 1 
ATOM   8617  N N   . ASP E 1 90  ? 25.760  4.449   36.873  1.00 70.64  ? 96  ASP E N   1 
ATOM   8618  C CA  . ASP E 1 90  ? 25.903  5.866   36.556  1.00 65.02  ? 96  ASP E CA  1 
ATOM   8619  C C   . ASP E 1 90  ? 27.362  6.311   36.524  1.00 66.59  ? 96  ASP E C   1 
ATOM   8620  O O   . ASP E 1 90  ? 27.879  6.675   35.465  1.00 71.85  ? 96  ASP E O   1 
ATOM   8621  C CB  . ASP E 1 90  ? 25.114  6.709   37.568  1.00 62.17  ? 96  ASP E CB  1 
ATOM   8622  C CG  . ASP E 1 90  ? 25.335  8.202   37.389  1.00 80.64  ? 96  ASP E CG  1 
ATOM   8623  O OD1 . ASP E 1 90  ? 24.934  8.755   36.340  1.00 77.26  ? 96  ASP E OD1 1 
ATOM   8624  O OD2 . ASP E 1 90  ? 25.921  8.822   38.301  1.00 88.22  ? 96  ASP E OD2 1 
ATOM   8625  N N   . LEU E 1 91  A 28.048  6.256   37.662  1.00 63.71  ? 96  LEU E N   1 
ATOM   8626  C CA  . LEU E 1 91  A 29.425  6.747   37.771  1.00 69.05  ? 96  LEU E CA  1 
ATOM   8627  C C   . LEU E 1 91  A 30.177  5.774   38.671  1.00 60.24  ? 96  LEU E C   1 
ATOM   8628  O O   . LEU E 1 91  A 30.118  5.892   39.899  1.00 53.52  ? 96  LEU E O   1 
ATOM   8629  C CB  . LEU E 1 91  A 29.476  8.170   38.323  1.00 51.57  ? 96  LEU E CB  1 
ATOM   8630  C CG  . LEU E 1 91  A 29.221  9.327   37.351  1.00 58.26  ? 96  LEU E CG  1 
ATOM   8631  C CD1 . LEU E 1 91  A 29.569  10.674  37.981  1.00 45.98  ? 96  LEU E CD1 1 
ATOM   8632  C CD2 . LEU E 1 91  A 29.999  9.125   36.056  1.00 53.57  ? 96  LEU E CD2 1 
ATOM   8633  N N   . CYS E 1 92  ? 30.876  4.817   38.055  1.00 62.84  ? 97  CYS E N   1 
ATOM   8634  C CA  . CYS E 1 92  ? 31.554  3.783   38.831  1.00 62.68  ? 97  CYS E CA  1 
ATOM   8635  C C   . CYS E 1 92  ? 32.503  4.405   39.848  1.00 51.88  ? 97  CYS E C   1 
ATOM   8636  O O   . CYS E 1 92  ? 32.435  4.099   41.045  1.00 47.00  ? 97  CYS E O   1 
ATOM   8637  C CB  . CYS E 1 92  ? 32.291  2.819   37.896  1.00 52.93  ? 97  CYS E CB  1 
ATOM   8638  S SG  . CYS E 1 92  ? 33.638  3.538   36.918  1.00 85.98  ? 97  CYS E SG  1 
ATOM   8639  N N   . TYR E 1 93  ? 33.366  5.307   39.401  1.00 54.45  ? 98  TYR E N   1 
ATOM   8640  C CA  . TYR E 1 93  ? 34.158  6.101   40.331  1.00 62.73  ? 98  TYR E CA  1 
ATOM   8641  C C   . TYR E 1 93  ? 33.326  7.285   40.810  1.00 60.02  ? 98  TYR E C   1 
ATOM   8642  O O   . TYR E 1 93  ? 32.852  8.068   39.980  1.00 53.09  ? 98  TYR E O   1 
ATOM   8643  C CB  . TYR E 1 93  ? 35.443  6.585   39.673  1.00 53.16  ? 98  TYR E CB  1 
ATOM   8644  C CG  . TYR E 1 93  ? 36.547  6.885   40.661  1.00 64.87  ? 98  TYR E CG  1 
ATOM   8645  C CD1 . TYR E 1 93  ? 36.554  8.072   41.380  1.00 60.45  ? 98  TYR E CD1 1 
ATOM   8646  C CD2 . TYR E 1 93  ? 37.579  5.979   40.880  1.00 55.37  ? 98  TYR E CD2 1 
ATOM   8647  C CE1 . TYR E 1 93  ? 37.560  8.354   42.289  1.00 62.20  ? 98  TYR E CE1 1 
ATOM   8648  C CE2 . TYR E 1 93  ? 38.588  6.253   41.784  1.00 57.71  ? 98  TYR E CE2 1 
ATOM   8649  C CZ  . TYR E 1 93  ? 38.572  7.442   42.489  1.00 65.80  ? 98  TYR E CZ  1 
ATOM   8650  O OH  . TYR E 1 93  ? 39.568  7.725   43.396  1.00 56.66  ? 98  TYR E OH  1 
ATOM   8651  N N   . PRO E 1 94  ? 33.117  7.449   42.116  1.00 56.78  ? 99  PRO E N   1 
ATOM   8652  C CA  . PRO E 1 94  ? 32.239  8.525   42.591  1.00 53.83  ? 99  PRO E CA  1 
ATOM   8653  C C   . PRO E 1 94  ? 32.761  9.899   42.197  1.00 56.91  ? 99  PRO E C   1 
ATOM   8654  O O   . PRO E 1 94  ? 33.968  10.125  42.083  1.00 56.15  ? 99  PRO E O   1 
ATOM   8655  C CB  . PRO E 1 94  ? 32.236  8.340   44.114  1.00 53.24  ? 99  PRO E CB  1 
ATOM   8656  C CG  . PRO E 1 94  ? 33.475  7.566   44.409  1.00 54.91  ? 99  PRO E CG  1 
ATOM   8657  C CD  . PRO E 1 94  ? 33.690  6.669   43.225  1.00 51.53  ? 99  PRO E CD  1 
ATOM   8658  N N   . GLY E 1 95  ? 31.828  10.814  41.976  1.00 52.35  ? 100 GLY E N   1 
ATOM   8659  C CA  . GLY E 1 95  ? 32.152  12.170  41.562  1.00 54.81  ? 100 GLY E CA  1 
ATOM   8660  C C   . GLY E 1 95  ? 30.932  12.834  40.944  1.00 59.27  ? 100 GLY E C   1 
ATOM   8661  O O   . GLY E 1 95  ? 29.793  12.491  41.266  1.00 60.90  ? 100 GLY E O   1 
ATOM   8662  N N   . ASN E 1 96  ? 31.196  13.787  40.055  1.00 56.50  ? 101 ASN E N   1 
ATOM   8663  C CA  . ASN E 1 96  ? 30.131  14.504  39.371  1.00 55.60  ? 101 ASN E CA  1 
ATOM   8664  C C   . ASN E 1 96  ? 30.515  14.727  37.918  1.00 51.11  ? 101 ASN E C   1 
ATOM   8665  O O   . ASN E 1 96  ? 31.688  14.669  37.539  1.00 51.81  ? 101 ASN E O   1 
ATOM   8666  C CB  . ASN E 1 96  ? 29.819  15.862  40.029  1.00 47.67  ? 101 ASN E CB  1 
ATOM   8667  C CG  . ASN E 1 96  ? 30.088  15.869  41.524  1.00 74.82  ? 101 ASN E CG  1 
ATOM   8668  O OD1 . ASN E 1 96  ? 31.185  16.212  41.970  1.00 81.09  ? 101 ASN E OD1 1 
ATOM   8669  N ND2 . ASN E 1 96  ? 29.077  15.501  42.308  1.00 72.10  ? 101 ASN E ND2 1 
ATOM   8670  N N   . LEU E 1 97  ? 29.496  14.960  37.101  1.00 49.39  ? 102 LEU E N   1 
ATOM   8671  C CA  . LEU E 1 97  ? 29.662  15.491  35.757  1.00 47.62  ? 102 LEU E CA  1 
ATOM   8672  C C   . LEU E 1 97  ? 29.091  16.902  35.758  1.00 46.38  ? 102 LEU E C   1 
ATOM   8673  O O   . LEU E 1 97  ? 27.915  17.097  36.084  1.00 53.69  ? 102 LEU E O   1 
ATOM   8674  C CB  . LEU E 1 97  ? 28.960  14.606  34.727  1.00 38.11  ? 102 LEU E CB  1 
ATOM   8675  C CG  . LEU E 1 97  ? 29.055  15.071  33.275  1.00 42.97  ? 102 LEU E CG  1 
ATOM   8676  C CD1 . LEU E 1 97  ? 30.497  15.326  32.884  1.00 46.49  ? 102 LEU E CD1 1 
ATOM   8677  C CD2 . LEU E 1 97  ? 28.416  14.061  32.343  1.00 43.50  ? 102 LEU E CD2 1 
ATOM   8678  N N   . ASN E 1 98  ? 29.925  17.883  35.426  1.00 49.89  ? 103 ASN E N   1 
ATOM   8679  C CA  . ASN E 1 98  ? 29.509  19.277  35.501  1.00 41.08  ? 103 ASN E CA  1 
ATOM   8680  C C   . ASN E 1 98  ? 28.474  19.593  34.430  1.00 47.91  ? 103 ASN E C   1 
ATOM   8681  O O   . ASN E 1 98  ? 28.571  19.121  33.293  1.00 47.46  ? 103 ASN E O   1 
ATOM   8682  C CB  . ASN E 1 98  ? 30.719  20.193  35.348  1.00 40.93  ? 103 ASN E CB  1 
ATOM   8683  C CG  . ASN E 1 98  ? 30.373  21.659  35.538  1.00 47.98  ? 103 ASN E CG  1 
ATOM   8684  O OD1 . ASN E 1 98  ? 30.022  22.090  36.638  1.00 44.16  ? 103 ASN E OD1 1 
ATOM   8685  N ND2 . ASN E 1 98  ? 30.481  22.435  34.466  1.00 54.80  ? 103 ASN E ND2 1 
ATOM   8686  N N   . ASP E 1 99  ? 27.483  20.408  34.802  1.00 53.77  ? 104 ASP E N   1 
ATOM   8687  C CA  . ASP E 1 99  ? 26.386  20.793  33.910  1.00 47.86  ? 104 ASP E CA  1 
ATOM   8688  C C   . ASP E 1 99  ? 25.709  19.560  33.320  1.00 45.62  ? 104 ASP E C   1 
ATOM   8689  O O   . ASP E 1 99  ? 25.418  19.491  32.123  1.00 51.22  ? 104 ASP E O   1 
ATOM   8690  C CB  . ASP E 1 99  ? 26.873  21.729  32.803  1.00 53.32  ? 104 ASP E CB  1 
ATOM   8691  C CG  . ASP E 1 99  ? 27.261  23.095  33.327  1.00 64.78  ? 104 ASP E CG  1 
ATOM   8692  O OD1 . ASP E 1 99  ? 26.798  23.462  34.428  1.00 72.95  ? 104 ASP E OD1 1 
ATOM   8693  O OD2 . ASP E 1 99  ? 28.032  23.801  32.638  1.00 66.02  ? 104 ASP E OD2 1 
ATOM   8694  N N   . TYR E 1 100 ? 25.457  18.574  34.186  1.00 49.35  ? 105 TYR E N   1 
ATOM   8695  C CA  . TYR E 1 100 ? 24.897  17.304  33.734  1.00 53.35  ? 105 TYR E CA  1 
ATOM   8696  C C   . TYR E 1 100 ? 23.545  17.499  33.061  1.00 42.89  ? 105 TYR E C   1 
ATOM   8697  O O   . TYR E 1 100 ? 23.286  16.928  31.996  1.00 48.31  ? 105 TYR E O   1 
ATOM   8698  C CB  . TYR E 1 100 ? 24.766  16.343  34.916  1.00 51.00  ? 105 TYR E CB  1 
ATOM   8699  C CG  . TYR E 1 100 ? 24.400  14.924  34.537  1.00 44.10  ? 105 TYR E CG  1 
ATOM   8700  C CD1 . TYR E 1 100 ? 24.735  14.407  33.293  1.00 46.79  ? 105 TYR E CD1 1 
ATOM   8701  C CD2 . TYR E 1 100 ? 23.734  14.096  35.431  1.00 46.54  ? 105 TYR E CD2 1 
ATOM   8702  C CE1 . TYR E 1 100 ? 24.409  13.112  32.944  1.00 50.67  ? 105 TYR E CE1 1 
ATOM   8703  C CE2 . TYR E 1 100 ? 23.401  12.796  35.091  1.00 41.55  ? 105 TYR E CE2 1 
ATOM   8704  C CZ  . TYR E 1 100 ? 23.743  12.309  33.845  1.00 54.06  ? 105 TYR E CZ  1 
ATOM   8705  O OH  . TYR E 1 100 ? 23.425  11.016  33.493  1.00 56.17  ? 105 TYR E OH  1 
ATOM   8706  N N   . GLU E 1 101 ? 22.677  18.314  33.664  1.00 48.13  ? 106 GLU E N   1 
ATOM   8707  C CA  . GLU E 1 101 ? 21.309  18.449  33.171  1.00 53.21  ? 106 GLU E CA  1 
ATOM   8708  C C   . GLU E 1 101 ? 21.265  19.148  31.818  1.00 45.23  ? 106 GLU E C   1 
ATOM   8709  O O   . GLU E 1 101 ? 20.524  18.727  30.921  1.00 53.39  ? 106 GLU E O   1 
ATOM   8710  C CB  . GLU E 1 101 ? 20.455  19.199  34.194  1.00 48.31  ? 106 GLU E CB  1 
ATOM   8711  C CG  . GLU E 1 101 ? 20.343  18.507  35.549  1.00 51.33  ? 106 GLU E CG  1 
ATOM   8712  C CD  . GLU E 1 101 ? 21.589  18.681  36.402  1.00 67.49  ? 106 GLU E CD  1 
ATOM   8713  O OE1 . GLU E 1 101 ? 22.396  19.588  36.099  1.00 69.70  ? 106 GLU E OE1 1 
ATOM   8714  O OE2 . GLU E 1 101 ? 21.767  17.906  37.366  1.00 71.58  ? 106 GLU E OE2 1 
ATOM   8715  N N   . GLU E 1 102 ? 22.049  20.215  31.650  1.00 47.41  ? 107 GLU E N   1 
ATOM   8716  C CA  . GLU E 1 102 ? 22.115  20.880  30.353  1.00 39.37  ? 107 GLU E CA  1 
ATOM   8717  C C   . GLU E 1 102 ? 22.708  19.957  29.295  1.00 47.73  ? 107 GLU E C   1 
ATOM   8718  O O   . GLU E 1 102 ? 22.266  19.963  28.139  1.00 41.81  ? 107 GLU E O   1 
ATOM   8719  C CB  . GLU E 1 102 ? 22.926  22.170  30.468  1.00 32.91  ? 107 GLU E CB  1 
ATOM   8720  C CG  . GLU E 1 102 ? 22.130  23.355  31.011  1.00 45.54  ? 107 GLU E CG  1 
ATOM   8721  C CD  . GLU E 1 102 ? 21.071  23.860  30.036  1.00 55.06  ? 107 GLU E CD  1 
ATOM   8722  O OE1 . GLU E 1 102 ? 21.401  24.051  28.842  1.00 45.83  ? 107 GLU E OE1 1 
ATOM   8723  O OE2 . GLU E 1 102 ? 19.911  24.065  30.466  1.00 40.85  ? 107 GLU E OE2 1 
ATOM   8724  N N   . LEU E 1 103 ? 23.708  19.154  29.671  1.00 45.95  ? 108 LEU E N   1 
ATOM   8725  C CA  . LEU E 1 103 ? 24.280  18.195  28.730  1.00 41.96  ? 108 LEU E CA  1 
ATOM   8726  C C   . LEU E 1 103 ? 23.250  17.154  28.310  1.00 44.82  ? 108 LEU E C   1 
ATOM   8727  O O   . LEU E 1 103 ? 23.191  16.765  27.138  1.00 40.55  ? 108 LEU E O   1 
ATOM   8728  C CB  . LEU E 1 103 ? 25.505  17.522  29.346  1.00 40.08  ? 108 LEU E CB  1 
ATOM   8729  C CG  . LEU E 1 103 ? 26.186  16.426  28.524  1.00 49.15  ? 108 LEU E CG  1 
ATOM   8730  C CD1 . LEU E 1 103 ? 26.696  16.967  27.195  1.00 40.04  ? 108 LEU E CD1 1 
ATOM   8731  C CD2 . LEU E 1 103 ? 27.321  15.805  29.330  1.00 44.48  ? 108 LEU E CD2 1 
ATOM   8732  N N   . LYS E 1 104 ? 22.434  16.687  29.258  1.00 44.83  ? 109 LYS E N   1 
ATOM   8733  C CA  . LYS E 1 104 ? 21.377  15.740  28.918  1.00 45.82  ? 109 LYS E CA  1 
ATOM   8734  C C   . LYS E 1 104 ? 20.366  16.371  27.966  1.00 44.60  ? 109 LYS E C   1 
ATOM   8735  O O   . LYS E 1 104 ? 19.907  15.726  27.016  1.00 41.49  ? 109 LYS E O   1 
ATOM   8736  C CB  . LYS E 1 104 ? 20.696  15.240  30.194  1.00 46.66  ? 109 LYS E CB  1 
ATOM   8737  C CG  . LYS E 1 104 ? 21.553  14.286  31.015  1.00 46.08  ? 109 LYS E CG  1 
ATOM   8738  C CD  . LYS E 1 104 ? 20.707  13.285  31.784  1.00 44.39  ? 109 LYS E CD  1 
ATOM   8739  C CE  . LYS E 1 104 ? 20.478  13.737  33.213  1.00 42.34  ? 109 LYS E CE  1 
ATOM   8740  N NZ  . LYS E 1 104 ? 19.414  12.918  33.863  1.00 60.41  ? 109 LYS E NZ  1 
ATOM   8741  N N   . HIS E 1 105 ? 20.018  17.638  28.195  1.00 41.05  ? 110 HIS E N   1 
ATOM   8742  C CA  . HIS E 1 105 ? 19.108  18.320  27.281  1.00 46.28  ? 110 HIS E CA  1 
ATOM   8743  C C   . HIS E 1 105 ? 19.706  18.409  25.884  1.00 47.07  ? 110 HIS E C   1 
ATOM   8744  O O   . HIS E 1 105 ? 19.010  18.190  24.885  1.00 48.30  ? 110 HIS E O   1 
ATOM   8745  C CB  . HIS E 1 105 ? 18.772  19.711  27.818  1.00 40.60  ? 110 HIS E CB  1 
ATOM   8746  C CG  . HIS E 1 105 ? 17.629  20.369  27.114  1.00 43.24  ? 110 HIS E CG  1 
ATOM   8747  N ND1 . HIS E 1 105 ? 16.317  19.996  27.314  1.00 49.40  ? 110 HIS E ND1 1 
ATOM   8748  C CD2 . HIS E 1 105 ? 17.600  21.378  26.211  1.00 45.86  ? 110 HIS E CD2 1 
ATOM   8749  C CE1 . HIS E 1 105 ? 15.529  20.746  26.565  1.00 49.05  ? 110 HIS E CE1 1 
ATOM   8750  N NE2 . HIS E 1 105 ? 16.283  21.593  25.887  1.00 49.87  ? 110 HIS E NE2 1 
ATOM   8751  N N   . LEU E 1 106 ? 21.005  18.707  25.797  1.00 45.88  ? 111 LEU E N   1 
ATOM   8752  C CA  . LEU E 1 106 ? 21.660  18.834  24.500  1.00 45.85  ? 111 LEU E CA  1 
ATOM   8753  C C   . LEU E 1 106 ? 21.630  17.517  23.728  1.00 46.40  ? 111 LEU E C   1 
ATOM   8754  O O   . LEU E 1 106 ? 21.474  17.509  22.501  1.00 47.81  ? 111 LEU E O   1 
ATOM   8755  C CB  . LEU E 1 106 ? 23.097  19.322  24.697  1.00 39.74  ? 111 LEU E CB  1 
ATOM   8756  C CG  . LEU E 1 106 ? 24.072  19.207  23.526  1.00 45.85  ? 111 LEU E CG  1 
ATOM   8757  C CD1 . LEU E 1 106 ? 23.794  20.285  22.505  1.00 50.66  ? 111 LEU E CD1 1 
ATOM   8758  C CD2 . LEU E 1 106 ? 25.504  19.304  24.023  1.00 51.15  ? 111 LEU E CD2 1 
ATOM   8759  N N   . LEU E 1 107 ? 21.764  16.395  24.427  1.00 42.82  ? 112 LEU E N   1 
ATOM   8760  C CA  . LEU E 1 107 ? 21.829  15.094  23.779  1.00 42.03  ? 112 LEU E CA  1 
ATOM   8761  C C   . LEU E 1 107 ? 20.465  14.440  23.597  1.00 47.01  ? 112 LEU E C   1 
ATOM   8762  O O   . LEU E 1 107 ? 20.400  13.328  23.065  1.00 43.35  ? 112 LEU E O   1 
ATOM   8763  C CB  . LEU E 1 107 ? 22.741  14.161  24.581  1.00 45.70  ? 112 LEU E CB  1 
ATOM   8764  C CG  . LEU E 1 107 ? 24.216  14.553  24.625  1.00 45.25  ? 112 LEU E CG  1 
ATOM   8765  C CD1 . LEU E 1 107 ? 24.883  13.901  25.823  1.00 41.46  ? 112 LEU E CD1 1 
ATOM   8766  C CD2 . LEU E 1 107 ? 24.916  14.165  23.328  1.00 42.98  ? 112 LEU E CD2 1 
ATOM   8767  N N   . SER E 1 108 ? 19.379  15.098  24.011  1.00 46.07  ? 113 SER E N   1 
ATOM   8768  C CA  . SER E 1 108 ? 18.059  14.476  23.923  1.00 45.06  ? 113 SER E CA  1 
ATOM   8769  C C   . SER E 1 108 ? 17.708  14.116  22.484  1.00 44.87  ? 113 SER E C   1 
ATOM   8770  O O   . SER E 1 108 ? 17.147  13.047  22.223  1.00 47.28  ? 113 SER E O   1 
ATOM   8771  C CB  . SER E 1 108 ? 16.999  15.405  24.514  1.00 49.04  ? 113 SER E CB  1 
ATOM   8772  O OG  . SER E 1 108 ? 17.059  16.691  23.921  1.00 47.81  ? 113 SER E OG  1 
ATOM   8773  N N   . ARG E 1 109 ? 18.027  14.993  21.536  1.00 52.12  ? 114 ARG E N   1 
ATOM   8774  C CA  . ARG E 1 109 ? 17.805  14.736  20.118  1.00 52.40  ? 114 ARG E CA  1 
ATOM   8775  C C   . ARG E 1 109 ? 19.082  15.093  19.372  1.00 47.89  ? 114 ARG E C   1 
ATOM   8776  O O   . ARG E 1 109 ? 19.520  16.248  19.411  1.00 47.25  ? 114 ARG E O   1 
ATOM   8777  C CB  . ARG E 1 109 ? 16.612  15.543  19.591  1.00 41.05  ? 114 ARG E CB  1 
ATOM   8778  C CG  . ARG E 1 109 ? 16.184  15.172  18.190  1.00 48.33  ? 114 ARG E CG  1 
ATOM   8779  C CD  . ARG E 1 109 ? 14.729  15.523  17.942  1.00 58.52  ? 114 ARG E CD  1 
ATOM   8780  N NE  . ARG E 1 109 ? 14.589  16.588  16.958  1.00 59.70  ? 114 ARG E NE  1 
ATOM   8781  C CZ  . ARG E 1 109 ? 13.491  17.313  16.791  1.00 73.67  ? 114 ARG E CZ  1 
ATOM   8782  N NH1 . ARG E 1 109 ? 12.416  17.123  17.540  1.00 70.62  ? 114 ARG E NH1 1 
ATOM   8783  N NH2 . ARG E 1 109 ? 13.471  18.254  15.850  1.00 74.62  ? 114 ARG E NH2 1 
ATOM   8784  N N   . ILE E 1 110 ? 19.677  14.107  18.700  1.00 42.91  ? 115 ILE E N   1 
ATOM   8785  C CA  . ILE E 1 110 ? 20.945  14.278  18.000  1.00 46.50  ? 115 ILE E CA  1 
ATOM   8786  C C   . ILE E 1 110 ? 20.781  13.778  16.570  1.00 45.46  ? 115 ILE E C   1 
ATOM   8787  O O   . ILE E 1 110 ? 20.274  12.673  16.350  1.00 47.12  ? 115 ILE E O   1 
ATOM   8788  C CB  . ILE E 1 110 ? 22.095  13.535  18.711  1.00 53.94  ? 115 ILE E CB  1 
ATOM   8789  C CG1 . ILE E 1 110 ? 22.384  14.184  20.065  1.00 46.03  ? 115 ILE E CG1 1 
ATOM   8790  C CG2 . ILE E 1 110 ? 23.357  13.538  17.860  1.00 46.90  ? 115 ILE E CG2 1 
ATOM   8791  C CD1 . ILE E 1 110 ? 22.669  15.661  19.973  1.00 51.07  ? 115 ILE E CD1 1 
ATOM   8792  N N   . ASN E 1 111 ? 21.193  14.602  15.600  1.00 50.25  ? 116 ASN E N   1 
ATOM   8793  C CA  . ASN E 1 111 ? 21.093  14.218  14.194  1.00 53.90  ? 116 ASN E CA  1 
ATOM   8794  C C   . ASN E 1 111 ? 22.195  13.246  13.784  1.00 54.54  ? 116 ASN E C   1 
ATOM   8795  O O   . ASN E 1 111 ? 21.972  12.386  12.927  1.00 51.04  ? 116 ASN E O   1 
ATOM   8796  C CB  . ASN E 1 111 ? 21.129  15.457  13.296  1.00 57.90  ? 116 ASN E CB  1 
ATOM   8797  C CG  . ASN E 1 111 ? 20.676  15.159  11.875  1.00 63.36  ? 116 ASN E CG  1 
ATOM   8798  O OD1 . ASN E 1 111 ? 21.233  15.685  10.911  1.00 69.54  ? 116 ASN E OD1 1 
ATOM   8799  N ND2 . ASN E 1 111 ? 19.665  14.309  11.740  1.00 60.36  ? 116 ASN E ND2 1 
ATOM   8800  N N   . HIS E 1 112 ? 23.393  13.391  14.351  1.00 62.28  ? 117 HIS E N   1 
ATOM   8801  C CA  . HIS E 1 112 ? 24.495  12.486  14.049  1.00 55.24  ? 117 HIS E CA  1 
ATOM   8802  C C   . HIS E 1 112 ? 25.414  12.377  15.257  1.00 62.62  ? 117 HIS E C   1 
ATOM   8803  O O   . HIS E 1 112 ? 25.843  13.393  15.811  1.00 53.75  ? 117 HIS E O   1 
ATOM   8804  C CB  . HIS E 1 112 ? 25.290  12.951  12.826  1.00 62.05  ? 117 HIS E CB  1 
ATOM   8805  C CG  . HIS E 1 112 ? 26.415  12.032  12.465  1.00 68.23  ? 117 HIS E CG  1 
ATOM   8806  N ND1 . HIS E 1 112 ? 27.738  12.357  12.670  1.00 73.57  ? 117 HIS E ND1 1 
ATOM   8807  C CD2 . HIS E 1 112 ? 26.412  10.789  11.927  1.00 66.23  ? 117 HIS E CD2 1 
ATOM   8808  C CE1 . HIS E 1 112 ? 28.502  11.357  12.266  1.00 78.59  ? 117 HIS E CE1 1 
ATOM   8809  N NE2 . HIS E 1 112 ? 27.722  10.393  11.812  1.00 71.94  ? 117 HIS E NE2 1 
ATOM   8810  N N   . PHE E 1 113 ? 25.722  11.140  15.642  1.00 60.87  ? 118 PHE E N   1 
ATOM   8811  C CA  . PHE E 1 113 ? 26.547  10.837  16.804  1.00 59.47  ? 118 PHE E CA  1 
ATOM   8812  C C   . PHE E 1 113 ? 27.510  9.722   16.425  1.00 62.23  ? 118 PHE E C   1 
ATOM   8813  O O   . PHE E 1 113 ? 27.087  8.703   15.870  1.00 62.38  ? 118 PHE E O   1 
ATOM   8814  C CB  . PHE E 1 113 ? 25.672  10.413  17.988  1.00 52.08  ? 118 PHE E CB  1 
ATOM   8815  C CG  . PHE E 1 113 ? 26.309  10.619  19.330  1.00 59.69  ? 118 PHE E CG  1 
ATOM   8816  C CD1 . PHE E 1 113 ? 26.506  11.895  19.831  1.00 60.63  ? 118 PHE E CD1 1 
ATOM   8817  C CD2 . PHE E 1 113 ? 26.693  9.533   20.102  1.00 57.12  ? 118 PHE E CD2 1 
ATOM   8818  C CE1 . PHE E 1 113 ? 27.084  12.086  21.076  1.00 57.48  ? 118 PHE E CE1 1 
ATOM   8819  C CE2 . PHE E 1 113 ? 27.268  9.716   21.344  1.00 56.79  ? 118 PHE E CE2 1 
ATOM   8820  C CZ  . PHE E 1 113 ? 27.465  10.997  21.833  1.00 52.14  ? 118 PHE E CZ  1 
ATOM   8821  N N   . GLU E 1 114 ? 28.795  9.906   16.724  1.00 49.32  ? 119 GLU E N   1 
ATOM   8822  C CA  . GLU E 1 114 ? 29.802  8.930   16.307  1.00 55.97  ? 119 GLU E CA  1 
ATOM   8823  C C   . GLU E 1 114 ? 31.012  9.055   17.220  1.00 58.42  ? 119 GLU E C   1 
ATOM   8824  O O   . GLU E 1 114 ? 31.710  10.073  17.185  1.00 59.38  ? 119 GLU E O   1 
ATOM   8825  C CB  . GLU E 1 114 ? 30.188  9.145   14.848  1.00 65.85  ? 119 GLU E CB  1 
ATOM   8826  C CG  . GLU E 1 114 ? 31.491  8.475   14.434  1.00 57.24  ? 119 GLU E CG  1 
ATOM   8827  C CD  . GLU E 1 114 ? 31.815  8.686   12.965  1.00 65.16  ? 119 GLU E CD  1 
ATOM   8828  O OE1 . GLU E 1 114 ? 30.876  8.681   12.141  1.00 83.81  ? 119 GLU E OE1 1 
ATOM   8829  O OE2 . GLU E 1 114 ? 33.007  8.860   12.633  1.00 88.35  ? 119 GLU E OE2 1 
ATOM   8830  N N   . LYS E 1 115 ? 31.255  8.023   18.026  1.00 66.93  ? 120 LYS E N   1 
ATOM   8831  C CA  . LYS E 1 115 ? 32.447  7.987   18.861  1.00 64.35  ? 120 LYS E CA  1 
ATOM   8832  C C   . LYS E 1 115 ? 33.694  7.961   17.986  1.00 58.40  ? 120 LYS E C   1 
ATOM   8833  O O   . LYS E 1 115 ? 33.758  7.224   16.998  1.00 66.96  ? 120 LYS E O   1 
ATOM   8834  C CB  . LYS E 1 115 ? 32.405  6.763   19.780  1.00 54.28  ? 120 LYS E CB  1 
ATOM   8835  C CG  . LYS E 1 115 ? 33.566  6.663   20.762  1.00 55.31  ? 120 LYS E CG  1 
ATOM   8836  C CD  . LYS E 1 115 ? 33.199  5.810   21.975  1.00 52.87  ? 120 LYS E CD  1 
ATOM   8837  C CE  . LYS E 1 115 ? 33.484  4.334   21.735  1.00 57.31  ? 120 LYS E CE  1 
ATOM   8838  N NZ  . LYS E 1 115 ? 33.825  3.613   22.995  1.00 58.90  ? 120 LYS E NZ  1 
ATOM   8839  N N   . THR E 1 116 ? 34.681  8.777   18.343  1.00 55.45  ? 121 THR E N   1 
ATOM   8840  C CA  . THR E 1 116 ? 35.916  8.862   17.578  1.00 58.10  ? 121 THR E CA  1 
ATOM   8841  C C   . THR E 1 116 ? 37.108  8.969   18.518  1.00 64.22  ? 121 THR E C   1 
ATOM   8842  O O   . THR E 1 116 ? 37.056  9.670   19.534  1.00 59.59  ? 121 THR E O   1 
ATOM   8843  C CB  . THR E 1 116 ? 35.902  10.055  16.610  1.00 60.85  ? 121 THR E CB  1 
ATOM   8844  O OG1 . THR E 1 116 ? 37.148  10.116  15.904  1.00 65.90  ? 121 THR E OG1 1 
ATOM   8845  C CG2 . THR E 1 116 ? 35.676  11.361  17.356  1.00 61.69  ? 121 THR E CG2 1 
ATOM   8846  N N   . LEU E 1 117 ? 38.178  8.259   18.170  1.00 69.41  ? 122 LEU E N   1 
ATOM   8847  C CA  . LEU E 1 117 ? 39.423  8.328   18.919  1.00 61.88  ? 122 LEU E CA  1 
ATOM   8848  C C   . LEU E 1 117 ? 40.146  9.623   18.578  1.00 60.13  ? 122 LEU E C   1 
ATOM   8849  O O   . LEU E 1 117 ? 40.373  9.926   17.402  1.00 66.15  ? 122 LEU E O   1 
ATOM   8850  C CB  . LEU E 1 117 ? 40.298  7.116   18.593  1.00 69.80  ? 122 LEU E CB  1 
ATOM   8851  C CG  . LEU E 1 117 ? 41.712  6.999   19.172  1.00 67.68  ? 122 LEU E CG  1 
ATOM   8852  C CD1 . LEU E 1 117 ? 41.753  7.319   20.657  1.00 62.28  ? 122 LEU E CD1 1 
ATOM   8853  C CD2 . LEU E 1 117 ? 42.258  5.603   18.915  1.00 56.94  ? 122 LEU E CD2 1 
ATOM   8854  N N   . ILE E 1 118 ? 40.505  10.392  19.605  1.00 58.42  ? 123 ILE E N   1 
ATOM   8855  C CA  . ILE E 1 118 ? 41.151  11.682  19.424  1.00 54.11  ? 123 ILE E CA  1 
ATOM   8856  C C   . ILE E 1 118 ? 42.545  11.712  20.035  1.00 57.50  ? 123 ILE E C   1 
ATOM   8857  O O   . ILE E 1 118 ? 43.482  12.237  19.423  1.00 62.16  ? 123 ILE E O   1 
ATOM   8858  C CB  . ILE E 1 118 ? 40.281  12.825  19.987  1.00 60.13  ? 123 ILE E CB  1 
ATOM   8859  C CG1 . ILE E 1 118 ? 39.781  12.481  21.390  1.00 58.10  ? 123 ILE E CG1 1 
ATOM   8860  C CG2 . ILE E 1 118 ? 39.097  13.070  19.066  1.00 53.17  ? 123 ILE E CG2 1 
ATOM   8861  C CD1 . ILE E 1 118 ? 39.776  13.654  22.338  1.00 54.04  ? 123 ILE E CD1 1 
ATOM   8862  N N   . ILE E 1 119 ? 42.712  11.155  21.231  1.00 58.49  ? 124 ILE E N   1 
ATOM   8863  C CA  . ILE E 1 119 ? 44.027  11.091  21.868  1.00 56.77  ? 124 ILE E CA  1 
ATOM   8864  C C   . ILE E 1 119 ? 44.336  9.650   22.265  1.00 60.67  ? 124 ILE E C   1 
ATOM   8865  O O   . ILE E 1 119 ? 43.928  9.206   23.349  1.00 51.78  ? 124 ILE E O   1 
ATOM   8866  C CB  . ILE E 1 119 ? 44.105  12.016  23.091  1.00 51.96  ? 124 ILE E CB  1 
ATOM   8867  C CG1 . ILE E 1 119 ? 43.690  13.439  22.713  1.00 61.98  ? 124 ILE E CG1 1 
ATOM   8868  C CG2 . ILE E 1 119 ? 45.512  12.006  23.665  1.00 58.72  ? 124 ILE E CG2 1 
ATOM   8869  C CD1 . ILE E 1 119 ? 43.304  14.294  23.898  1.00 54.21  ? 124 ILE E CD1 1 
ATOM   8870  N N   . PRO E 1 120 ? 45.053  8.892   21.439  1.00 66.27  ? 125 PRO E N   1 
ATOM   8871  C CA  . PRO E 1 120 ? 45.392  7.516   21.814  1.00 58.61  ? 125 PRO E CA  1 
ATOM   8872  C C   . PRO E 1 120 ? 46.367  7.487   22.982  1.00 67.28  ? 125 PRO E C   1 
ATOM   8873  O O   . PRO E 1 120 ? 47.075  8.456   23.267  1.00 71.22  ? 125 PRO E O   1 
ATOM   8874  C CB  . PRO E 1 120 ? 46.023  6.941   20.542  1.00 50.24  ? 125 PRO E CB  1 
ATOM   8875  C CG  . PRO E 1 120 ? 46.548  8.130   19.816  1.00 64.31  ? 125 PRO E CG  1 
ATOM   8876  C CD  . PRO E 1 120 ? 45.617  9.269   20.131  1.00 59.53  ? 125 PRO E CD  1 
ATOM   8877  N N   . LYS E 1 121 A 46.382  6.344   23.674  1.00 66.67  ? 125 LYS E N   1 
ATOM   8878  C CA  . LYS E 1 121 A 47.217  6.202   24.863  1.00 66.95  ? 125 LYS E CA  1 
ATOM   8879  C C   . LYS E 1 121 A 48.703  6.298   24.548  1.00 62.93  ? 125 LYS E C   1 
ATOM   8880  O O   . LYS E 1 121 A 49.495  6.603   25.446  1.00 65.51  ? 125 LYS E O   1 
ATOM   8881  C CB  . LYS E 1 121 A 46.916  4.876   25.562  1.00 66.68  ? 125 LYS E CB  1 
ATOM   8882  C CG  . LYS E 1 121 A 45.808  4.963   26.594  1.00 63.55  ? 125 LYS E CG  1 
ATOM   8883  C CD  . LYS E 1 121 A 45.044  3.658   26.697  1.00 54.64  ? 125 LYS E CD  1 
ATOM   8884  C CE  . LYS E 1 121 A 44.231  3.597   27.981  1.00 73.76  ? 125 LYS E CE  1 
ATOM   8885  N NZ  . LYS E 1 121 A 43.140  2.585   27.899  1.00 85.46  ? 125 LYS E NZ  1 
ATOM   8886  N N   . SER E 1 122 B 49.098  6.058   23.296  1.00 64.07  ? 125 SER E N   1 
ATOM   8887  C CA  . SER E 1 122 B 50.499  6.210   22.922  1.00 64.85  ? 125 SER E CA  1 
ATOM   8888  C C   . SER E 1 122 B 50.967  7.657   23.007  1.00 66.20  ? 125 SER E C   1 
ATOM   8889  O O   . SER E 1 122 B 52.177  7.904   23.004  1.00 68.68  ? 125 SER E O   1 
ATOM   8890  C CB  . SER E 1 122 B 50.730  5.659   21.513  1.00 59.24  ? 125 SER E CB  1 
ATOM   8891  O OG  . SER E 1 122 B 49.917  6.317   20.557  1.00 65.25  ? 125 SER E OG  1 
ATOM   8892  N N   . SER E 1 123 ? 50.043  8.613   23.101  1.00 68.79  ? 126 SER E N   1 
ATOM   8893  C CA  . SER E 1 123 ? 50.376  10.027  23.216  1.00 63.74  ? 126 SER E CA  1 
ATOM   8894  C C   . SER E 1 123 ? 50.831  10.422  24.617  1.00 68.79  ? 126 SER E C   1 
ATOM   8895  O O   . SER E 1 123 ? 50.992  11.616  24.887  1.00 68.11  ? 126 SER E O   1 
ATOM   8896  C CB  . SER E 1 123 ? 49.177  10.880  22.800  1.00 72.19  ? 126 SER E CB  1 
ATOM   8897  O OG  . SER E 1 123 ? 48.738  10.532  21.497  1.00 75.41  ? 126 SER E OG  1 
ATOM   8898  N N   . TRP E 1 124 ? 51.045  9.457   25.509  1.00 69.72  ? 127 TRP E N   1 
ATOM   8899  C CA  . TRP E 1 124 ? 51.549  9.716   26.858  1.00 76.25  ? 127 TRP E CA  1 
ATOM   8900  C C   . TRP E 1 124 ? 52.767  8.837   27.105  1.00 72.73  ? 127 TRP E C   1 
ATOM   8901  O O   . TRP E 1 124 ? 52.749  7.950   27.966  1.00 66.72  ? 127 TRP E O   1 
ATOM   8902  C CB  . TRP E 1 124 ? 50.466  9.461   27.905  1.00 72.03  ? 127 TRP E CB  1 
ATOM   8903  C CG  . TRP E 1 124 ? 49.119  9.952   27.501  1.00 74.45  ? 127 TRP E CG  1 
ATOM   8904  C CD1 . TRP E 1 124 ? 48.077  9.203   27.032  1.00 70.80  ? 127 TRP E CD1 1 
ATOM   8905  C CD2 . TRP E 1 124 ? 48.661  11.309  27.524  1.00 79.51  ? 127 TRP E CD2 1 
ATOM   8906  N NE1 . TRP E 1 124 ? 46.997  10.011  26.764  1.00 64.38  ? 127 TRP E NE1 1 
ATOM   8907  C CE2 . TRP E 1 124 ? 47.329  11.308  27.057  1.00 69.86  ? 127 TRP E CE2 1 
ATOM   8908  C CE3 . TRP E 1 124 ? 49.246  12.524  27.894  1.00 65.21  ? 127 TRP E CE3 1 
ATOM   8909  C CZ2 . TRP E 1 124 ? 46.574  12.475  26.952  1.00 54.17  ? 127 TRP E CZ2 1 
ATOM   8910  C CZ3 . TRP E 1 124 ? 48.495  13.682  27.789  1.00 64.50  ? 127 TRP E CZ3 1 
ATOM   8911  C CH2 . TRP E 1 124 ? 47.173  13.648  27.320  1.00 67.56  ? 127 TRP E CH2 1 
ATOM   8912  N N   . PRO E 1 125 ? 53.856  9.066   26.366  1.00 75.52  ? 128 PRO E N   1 
ATOM   8913  C CA  . PRO E 1 125 ? 55.024  8.183   26.497  1.00 69.67  ? 128 PRO E CA  1 
ATOM   8914  C C   . PRO E 1 125 ? 55.695  8.260   27.856  1.00 68.81  ? 128 PRO E C   1 
ATOM   8915  O O   . PRO E 1 125 ? 56.355  7.292   28.253  1.00 62.33  ? 128 PRO E O   1 
ATOM   8916  C CB  . PRO E 1 125 ? 55.955  8.672   25.381  1.00 72.09  ? 128 PRO E CB  1 
ATOM   8917  C CG  . PRO E 1 125 ? 55.605  10.108  25.213  1.00 68.35  ? 128 PRO E CG  1 
ATOM   8918  C CD  . PRO E 1 125 ? 54.132  10.225  25.496  1.00 74.59  ? 128 PRO E CD  1 
ATOM   8919  N N   . ASN E 1 126 ? 55.540  9.367   28.584  1.00 66.87  ? 129 ASN E N   1 
ATOM   8920  C CA  . ASN E 1 126 ? 56.193  9.565   29.871  1.00 58.86  ? 129 ASN E CA  1 
ATOM   8921  C C   . ASN E 1 126 ? 55.208  9.551   31.031  1.00 60.39  ? 129 ASN E C   1 
ATOM   8922  O O   . ASN E 1 126 ? 55.488  10.126  32.088  1.00 61.74  ? 129 ASN E O   1 
ATOM   8923  C CB  . ASN E 1 126 ? 56.985  10.871  29.859  1.00 63.30  ? 129 ASN E CB  1 
ATOM   8924  C CG  . ASN E 1 126 ? 57.983  10.928  28.721  1.00 78.61  ? 129 ASN E CG  1 
ATOM   8925  O OD1 . ASN E 1 126 ? 57.623  11.216  27.579  1.00 77.80  ? 129 ASN E OD1 1 
ATOM   8926  N ND2 . ASN E 1 126 ? 59.244  10.636  29.025  1.00 78.57  ? 129 ASN E ND2 1 
ATOM   8927  N N   . HIS E 1 127 ? 54.055  8.912   30.851  1.00 64.51  ? 130 HIS E N   1 
ATOM   8928  C CA  . HIS E 1 127 ? 53.050  8.804   31.896  1.00 56.97  ? 130 HIS E CA  1 
ATOM   8929  C C   . HIS E 1 127 ? 52.432  7.417   31.843  1.00 67.51  ? 130 HIS E C   1 
ATOM   8930  O O   . HIS E 1 127 ? 52.332  6.806   30.775  1.00 67.69  ? 130 HIS E O   1 
ATOM   8931  C CB  . HIS E 1 127 ? 51.953  9.874   31.747  1.00 59.06  ? 130 HIS E CB  1 
ATOM   8932  C CG  . HIS E 1 127 ? 52.475  11.278  31.734  1.00 61.30  ? 130 HIS E CG  1 
ATOM   8933  N ND1 . HIS E 1 127 ? 53.000  11.867  30.604  1.00 57.25  ? 130 HIS E ND1 1 
ATOM   8934  C CD2 . HIS E 1 127 ? 52.562  12.206  32.718  1.00 55.54  ? 130 HIS E CD2 1 
ATOM   8935  C CE1 . HIS E 1 127 ? 53.383  13.099  30.891  1.00 66.18  ? 130 HIS E CE1 1 
ATOM   8936  N NE2 . HIS E 1 127 ? 53.127  13.329  32.166  1.00 58.59  ? 130 HIS E NE2 1 
ATOM   8937  N N   . GLU E 1 128 ? 52.024  6.922   33.006  1.00 62.71  ? 131 GLU E N   1 
ATOM   8938  C CA  . GLU E 1 128 ? 51.316  5.654   33.077  1.00 64.02  ? 131 GLU E CA  1 
ATOM   8939  C C   . GLU E 1 128 ? 49.869  5.858   32.651  1.00 66.35  ? 131 GLU E C   1 
ATOM   8940  O O   . GLU E 1 128 ? 49.212  6.807   33.090  1.00 62.53  ? 131 GLU E O   1 
ATOM   8941  C CB  . GLU E 1 128 ? 51.385  5.080   34.492  1.00 69.66  ? 131 GLU E CB  1 
ATOM   8942  C CG  . GLU E 1 128 ? 51.553  3.568   34.546  1.00 71.38  ? 131 GLU E CG  1 
ATOM   8943  C CD  . GLU E 1 128 ? 52.807  3.098   33.838  1.00 82.62  ? 131 GLU E CD  1 
ATOM   8944  O OE1 . GLU E 1 128 ? 53.877  3.708   34.048  1.00 83.24  ? 131 GLU E OE1 1 
ATOM   8945  O OE2 . GLU E 1 128 ? 52.723  2.117   33.070  1.00 90.09  ? 131 GLU E OE2 1 
ATOM   8946  N N   . THR E 1 129 ? 49.375  4.975   31.786  1.00 56.08  ? 132 THR E N   1 
ATOM   8947  C CA  . THR E 1 129 ? 48.013  5.069   31.286  1.00 60.12  ? 132 THR E CA  1 
ATOM   8948  C C   . THR E 1 129 ? 47.117  3.943   31.780  1.00 68.52  ? 132 THR E C   1 
ATOM   8949  O O   . THR E 1 129 ? 45.924  3.936   31.458  1.00 55.66  ? 132 THR E O   1 
ATOM   8950  C CB  . THR E 1 129 ? 48.010  5.095   29.753  1.00 64.67  ? 132 THR E CB  1 
ATOM   8951  O OG1 . THR E 1 129 ? 48.275  3.781   29.249  1.00 69.07  ? 132 THR E OG1 1 
ATOM   8952  C CG2 . THR E 1 129 ? 49.071  6.062   29.235  1.00 68.35  ? 132 THR E CG2 1 
ATOM   8953  N N   . SER E 1 130 ? 47.650  2.996   32.548  1.00 75.49  ? 133 SER E N   1 
ATOM   8954  C CA  . SER E 1 130 ? 46.863  1.870   33.051  1.00 76.08  ? 133 SER E CA  1 
ATOM   8955  C C   . SER E 1 130 ? 46.292  2.151   34.438  1.00 75.00  ? 133 SER E C   1 
ATOM   8956  O O   . SER E 1 130 ? 46.413  1.345   35.359  1.00 86.52  ? 133 SER E O   1 
ATOM   8957  C CB  . SER E 1 130 ? 47.719  0.610   33.062  1.00 69.36  ? 133 SER E CB  1 
ATOM   8958  O OG  . SER E 1 130 ? 48.900  0.814   33.818  1.00 84.54  ? 133 SER E OG  1 
ATOM   8959  N N   . GLY E 1 131 ? 45.647  3.304   34.592  1.00 75.67  ? 134 GLY E N   1 
ATOM   8960  C CA  . GLY E 1 131 ? 44.968  3.622   35.831  1.00 71.99  ? 134 GLY E CA  1 
ATOM   8961  C C   . GLY E 1 131 ? 43.698  2.811   35.974  1.00 75.48  ? 134 GLY E C   1 
ATOM   8962  O O   . GLY E 1 131 ? 42.811  2.874   35.114  1.00 66.19  ? 134 GLY E O   1 
ATOM   8963  N N   . VAL E 1 132 ? 43.605  2.028   37.042  1.00 68.09  ? 135 VAL E N   1 
ATOM   8964  C CA  . VAL E 1 132 ? 42.549  1.036   37.197  1.00 70.56  ? 135 VAL E CA  1 
ATOM   8965  C C   . VAL E 1 132 ? 42.032  1.079   38.629  1.00 68.44  ? 135 VAL E C   1 
ATOM   8966  O O   . VAL E 1 132 ? 42.811  1.238   39.574  1.00 76.28  ? 135 VAL E O   1 
ATOM   8967  C CB  . VAL E 1 132 ? 43.062  -0.369  36.822  1.00 77.25  ? 135 VAL E CB  1 
ATOM   8968  C CG1 . VAL E 1 132 ? 41.966  -1.356  36.932  1.00 73.92  ? 135 VAL E CG1 1 
ATOM   8969  C CG2 . VAL E 1 132 ? 43.617  -0.388  35.400  1.00 81.35  ? 135 VAL E CG2 1 
ATOM   8970  N N   . SER E 1 133 ? 40.715  0.939   38.790  1.00 54.11  ? 136 SER E N   1 
ATOM   8971  C CA  . SER E 1 133 ? 40.079  0.991   40.100  1.00 66.25  ? 136 SER E CA  1 
ATOM   8972  C C   . SER E 1 133 ? 39.100  -0.164  40.263  1.00 65.80  ? 136 SER E C   1 
ATOM   8973  O O   . SER E 1 133 ? 38.483  -0.615  39.294  1.00 65.18  ? 136 SER E O   1 
ATOM   8974  C CB  . SER E 1 133 ? 39.335  2.316   40.312  1.00 62.75  ? 136 SER E CB  1 
ATOM   8975  O OG  . SER E 1 133 ? 38.429  2.218   41.399  1.00 51.31  ? 136 SER E OG  1 
ATOM   8976  N N   . ALA E 1 134 ? 38.953  -0.632  41.510  1.00 63.83  ? 137 ALA E N   1 
ATOM   8977  C CA  . ALA E 1 134 ? 38.002  -1.699  41.814  1.00 53.86  ? 137 ALA E CA  1 
ATOM   8978  C C   . ALA E 1 134 ? 36.555  -1.224  41.804  1.00 63.98  ? 137 ALA E C   1 
ATOM   8979  O O   . ALA E 1 134 ? 35.653  -2.039  41.579  1.00 63.29  ? 137 ALA E O   1 
ATOM   8980  C CB  . ALA E 1 134 ? 38.311  -2.325  43.174  1.00 45.44  ? 137 ALA E CB  1 
ATOM   8981  N N   . ALA E 1 135 ? 36.313  0.067   42.039  1.00 63.61  ? 138 ALA E N   1 
ATOM   8982  C CA  . ALA E 1 135 ? 34.962  0.600   41.940  1.00 56.38  ? 138 ALA E CA  1 
ATOM   8983  C C   . ALA E 1 135 ? 34.437  0.579   40.513  1.00 59.47  ? 138 ALA E C   1 
ATOM   8984  O O   . ALA E 1 135 ? 33.235  0.773   40.312  1.00 52.72  ? 138 ALA E O   1 
ATOM   8985  C CB  . ALA E 1 135 ? 34.915  2.027   42.490  1.00 59.43  ? 138 ALA E CB  1 
ATOM   8986  N N   . CYS E 1 136 ? 35.299  0.326   39.529  1.00 60.04  ? 139 CYS E N   1 
ATOM   8987  C CA  . CYS E 1 136 ? 34.914  0.256   38.121  1.00 60.00  ? 139 CYS E CA  1 
ATOM   8988  C C   . CYS E 1 136 ? 35.194  -1.134  37.558  1.00 59.61  ? 139 CYS E C   1 
ATOM   8989  O O   . CYS E 1 136 ? 35.982  -1.284  36.617  1.00 53.78  ? 139 CYS E O   1 
ATOM   8990  C CB  . CYS E 1 136 ? 35.666  1.313   37.320  1.00 53.17  ? 139 CYS E CB  1 
ATOM   8991  S SG  . CYS E 1 136 ? 35.359  2.990   37.869  1.00 70.79  ? 139 CYS E SG  1 
ATOM   8992  N N   . PRO E 1 137 ? 34.560  -2.173  38.093  1.00 63.67  ? 140 PRO E N   1 
ATOM   8993  C CA  . PRO E 1 137 ? 34.892  -3.530  37.654  1.00 61.91  ? 140 PRO E CA  1 
ATOM   8994  C C   . PRO E 1 137 ? 34.332  -3.848  36.279  1.00 60.68  ? 140 PRO E C   1 
ATOM   8995  O O   . PRO E 1 137 ? 33.262  -3.381  35.887  1.00 65.99  ? 140 PRO E O   1 
ATOM   8996  C CB  . PRO E 1 137 ? 34.236  -4.409  38.722  1.00 61.18  ? 140 PRO E CB  1 
ATOM   8997  C CG  . PRO E 1 137 ? 33.042  -3.627  39.142  1.00 47.51  ? 140 PRO E CG  1 
ATOM   8998  C CD  . PRO E 1 137 ? 33.412  -2.168  39.019  1.00 60.53  ? 140 PRO E CD  1 
ATOM   8999  N N   . TYR E 1 138 ? 35.085  -4.656  35.541  1.00 60.09  ? 141 TYR E N   1 
ATOM   9000  C CA  . TYR E 1 138 ? 34.589  -5.301  34.333  1.00 52.80  ? 141 TYR E CA  1 
ATOM   9001  C C   . TYR E 1 138 ? 34.717  -6.803  34.542  1.00 57.28  ? 141 TYR E C   1 
ATOM   9002  O O   . TYR E 1 138 ? 35.833  -7.332  34.607  1.00 63.76  ? 141 TYR E O   1 
ATOM   9003  C CB  . TYR E 1 138 ? 35.345  -4.846  33.087  1.00 50.66  ? 141 TYR E CB  1 
ATOM   9004  C CG  . TYR E 1 138 ? 34.802  -5.478  31.830  1.00 57.85  ? 141 TYR E CG  1 
ATOM   9005  C CD1 . TYR E 1 138 ? 33.445  -5.426  31.542  1.00 65.53  ? 141 TYR E CD1 1 
ATOM   9006  C CD2 . TYR E 1 138 ? 35.634  -6.147  30.945  1.00 60.00  ? 141 TYR E CD2 1 
ATOM   9007  C CE1 . TYR E 1 138 ? 32.930  -6.013  30.401  1.00 66.42  ? 141 TYR E CE1 1 
ATOM   9008  C CE2 . TYR E 1 138 ? 35.129  -6.739  29.797  1.00 64.91  ? 141 TYR E CE2 1 
ATOM   9009  C CZ  . TYR E 1 138 ? 33.775  -6.668  29.532  1.00 71.17  ? 141 TYR E CZ  1 
ATOM   9010  O OH  . TYR E 1 138 ? 33.259  -7.252  28.397  1.00 75.05  ? 141 TYR E OH  1 
ATOM   9011  N N   . GLN E 1 139 ? 33.574  -7.481  34.667  1.00 55.23  ? 142 GLN E N   1 
ATOM   9012  C CA  . GLN E 1 139 ? 33.527  -8.920  34.936  1.00 53.91  ? 142 GLN E CA  1 
ATOM   9013  C C   . GLN E 1 139 ? 34.287  -9.276  36.213  1.00 51.30  ? 142 GLN E C   1 
ATOM   9014  O O   . GLN E 1 139 ? 34.932  -10.321 36.301  1.00 55.36  ? 142 GLN E O   1 
ATOM   9015  C CB  . GLN E 1 139 ? 34.060  -9.725  33.746  1.00 62.70  ? 142 GLN E CB  1 
ATOM   9016  C CG  . GLN E 1 139 ? 33.618  -9.195  32.391  1.00 65.81  ? 142 GLN E CG  1 
ATOM   9017  C CD  . GLN E 1 139 ? 32.427  -9.950  31.836  1.00 67.08  ? 142 GLN E CD  1 
ATOM   9018  O OE1 . GLN E 1 139 ? 31.767  -10.701 32.552  1.00 80.18  ? 142 GLN E OE1 1 
ATOM   9019  N NE2 . GLN E 1 139 ? 32.139  -9.747  30.558  1.00 75.83  ? 142 GLN E NE2 1 
ATOM   9020  N N   . GLY E 1 140 ? 34.217  -8.398  37.213  1.00 53.64  ? 143 GLY E N   1 
ATOM   9021  C CA  . GLY E 1 140 ? 34.898  -8.601  38.473  1.00 52.53  ? 143 GLY E CA  1 
ATOM   9022  C C   . GLY E 1 140 ? 36.319  -8.070  38.522  1.00 49.79  ? 143 GLY E C   1 
ATOM   9023  O O   . GLY E 1 140 ? 36.780  -7.657  39.592  1.00 55.57  ? 143 GLY E O   1 
ATOM   9024  N N   . VAL E 1 141 ? 37.026  -8.086  37.399  1.00 49.64  ? 144 VAL E N   1 
ATOM   9025  C CA  . VAL E 1 141 ? 38.384  -7.534  37.347  1.00 57.27  ? 144 VAL E CA  1 
ATOM   9026  C C   . VAL E 1 141 ? 38.305  -6.011  37.372  1.00 60.35  ? 144 VAL E C   1 
ATOM   9027  O O   . VAL E 1 141 ? 37.492  -5.427  36.636  1.00 60.97  ? 144 VAL E O   1 
ATOM   9028  C CB  . VAL E 1 141 ? 39.111  -8.027  36.095  1.00 49.81  ? 144 VAL E CB  1 
ATOM   9029  C CG1 . VAL E 1 141 ? 40.520  -7.455  36.036  1.00 55.87  ? 144 VAL E CG1 1 
ATOM   9030  C CG2 . VAL E 1 141 ? 39.150  -9.544  36.073  1.00 50.02  ? 144 VAL E CG2 1 
ATOM   9031  N N   . PRO E 1 142 ? 39.109  -5.331  38.190  1.00 68.72  ? 145 PRO E N   1 
ATOM   9032  C CA  . PRO E 1 142 ? 39.070  -3.863  38.204  1.00 62.87  ? 145 PRO E CA  1 
ATOM   9033  C C   . PRO E 1 142 ? 39.397  -3.280  36.836  1.00 61.92  ? 145 PRO E C   1 
ATOM   9034  O O   . PRO E 1 142 ? 40.261  -3.782  36.111  1.00 54.10  ? 145 PRO E O   1 
ATOM   9035  C CB  . PRO E 1 142 ? 40.132  -3.489  39.245  1.00 54.98  ? 145 PRO E CB  1 
ATOM   9036  C CG  . PRO E 1 142 ? 40.218  -4.687  40.134  1.00 57.58  ? 145 PRO E CG  1 
ATOM   9037  C CD  . PRO E 1 142 ? 40.009  -5.869  39.227  1.00 60.76  ? 145 PRO E CD  1 
ATOM   9038  N N   . SER E 1 143 ? 38.704  -2.199  36.497  1.00 65.79  ? 146 SER E N   1 
ATOM   9039  C CA  . SER E 1 143 ? 38.821  -1.562  35.191  1.00 57.75  ? 146 SER E CA  1 
ATOM   9040  C C   . SER E 1 143 ? 38.600  -0.063  35.378  1.00 63.48  ? 146 SER E C   1 
ATOM   9041  O O   . SER E 1 143 ? 38.679  0.452   36.499  1.00 65.21  ? 146 SER E O   1 
ATOM   9042  C CB  . SER E 1 143 ? 37.833  -2.194  34.195  1.00 54.39  ? 146 SER E CB  1 
ATOM   9043  O OG  . SER E 1 143 ? 38.071  -1.714  32.886  1.00 58.86  ? 146 SER E OG  1 
ATOM   9044  N N   . PHE E 1 144 ? 38.329  0.639   34.281  1.00 59.53  ? 147 PHE E N   1 
ATOM   9045  C CA  . PHE E 1 144 ? 38.136  2.083   34.314  1.00 72.38  ? 147 PHE E CA  1 
ATOM   9046  C C   . PHE E 1 144 ? 37.190  2.486   33.188  1.00 61.19  ? 147 PHE E C   1 
ATOM   9047  O O   . PHE E 1 144 ? 36.781  1.659   32.368  1.00 47.25  ? 147 PHE E O   1 
ATOM   9048  C CB  . PHE E 1 144 ? 39.479  2.815   34.201  1.00 52.60  ? 147 PHE E CB  1 
ATOM   9049  C CG  . PHE E 1 144 ? 39.422  4.252   34.624  1.00 60.53  ? 147 PHE E CG  1 
ATOM   9050  C CD1 . PHE E 1 144 ? 38.946  4.599   35.878  1.00 57.99  ? 147 PHE E CD1 1 
ATOM   9051  C CD2 . PHE E 1 144 ? 39.837  5.258   33.767  1.00 56.55  ? 147 PHE E CD2 1 
ATOM   9052  C CE1 . PHE E 1 144 ? 38.894  5.922   36.273  1.00 57.86  ? 147 PHE E CE1 1 
ATOM   9053  C CE2 . PHE E 1 144 ? 39.787  6.580   34.155  1.00 59.07  ? 147 PHE E CE2 1 
ATOM   9054  C CZ  . PHE E 1 144 ? 39.316  6.914   35.410  1.00 59.21  ? 147 PHE E CZ  1 
ATOM   9055  N N   . PHE E 1 145 ? 36.841  3.775   33.159  1.00 57.97  ? 148 PHE E N   1 
ATOM   9056  C CA  . PHE E 1 145 ? 36.056  4.319   32.057  1.00 56.35  ? 148 PHE E CA  1 
ATOM   9057  C C   . PHE E 1 145 ? 36.773  4.073   30.738  1.00 55.35  ? 148 PHE E C   1 
ATOM   9058  O O   . PHE E 1 145 ? 37.979  4.306   30.620  1.00 62.95  ? 148 PHE E O   1 
ATOM   9059  C CB  . PHE E 1 145 ? 35.829  5.819   32.239  1.00 52.11  ? 148 PHE E CB  1 
ATOM   9060  C CG  . PHE E 1 145 ? 35.067  6.191   33.479  1.00 49.60  ? 148 PHE E CG  1 
ATOM   9061  C CD1 . PHE E 1 145 ? 33.714  5.923   33.585  1.00 46.78  ? 148 PHE E CD1 1 
ATOM   9062  C CD2 . PHE E 1 145 ? 35.699  6.843   34.524  1.00 53.94  ? 148 PHE E CD2 1 
ATOM   9063  C CE1 . PHE E 1 145 ? 33.012  6.282   34.716  1.00 46.07  ? 148 PHE E CE1 1 
ATOM   9064  C CE2 . PHE E 1 145 ? 35.001  7.202   35.662  1.00 53.42  ? 148 PHE E CE2 1 
ATOM   9065  C CZ  . PHE E 1 145 ? 33.655  6.922   35.757  1.00 46.83  ? 148 PHE E CZ  1 
ATOM   9066  N N   . ARG E 1 146 ? 36.026  3.612   29.737  1.00 56.57  ? 149 ARG E N   1 
ATOM   9067  C CA  . ARG E 1 146 ? 36.645  3.234   28.474  1.00 62.84  ? 149 ARG E CA  1 
ATOM   9068  C C   . ARG E 1 146 ? 37.065  4.432   27.629  1.00 65.50  ? 149 ARG E C   1 
ATOM   9069  O O   . ARG E 1 146 ? 37.961  4.296   26.788  1.00 62.37  ? 149 ARG E O   1 
ATOM   9070  C CB  . ARG E 1 146 ? 35.692  2.342   27.674  1.00 49.86  ? 149 ARG E CB  1 
ATOM   9071  C CG  . ARG E 1 146 ? 35.735  0.873   28.074  1.00 52.64  ? 149 ARG E CG  1 
ATOM   9072  C CD  . ARG E 1 146 ? 34.714  0.069   27.291  1.00 73.99  ? 149 ARG E CD  1 
ATOM   9073  N NE  . ARG E 1 146 ? 34.269  -1.114  28.016  1.00 92.45  ? 149 ARG E NE  1 
ATOM   9074  C CZ  . ARG E 1 146 ? 33.095  -1.219  28.623  1.00 97.26  ? 149 ARG E CZ  1 
ATOM   9075  N NH1 . ARG E 1 146 ? 32.232  -0.215  28.637  1.00 90.07  ? 149 ARG E NH1 1 
ATOM   9076  N NH2 . ARG E 1 146 ? 32.780  -2.356  29.237  1.00 91.00  ? 149 ARG E NH2 1 
ATOM   9077  N N   . ASN E 1 147 ? 36.455  5.599   27.835  1.00 65.91  ? 150 ASN E N   1 
ATOM   9078  C CA  . ASN E 1 147 ? 36.679  6.742   26.961  1.00 59.83  ? 150 ASN E CA  1 
ATOM   9079  C C   . ASN E 1 147 ? 37.654  7.769   27.524  1.00 54.07  ? 150 ASN E C   1 
ATOM   9080  O O   . ASN E 1 147 ? 38.026  8.702   26.806  1.00 49.82  ? 150 ASN E O   1 
ATOM   9081  C CB  . ASN E 1 147 ? 35.340  7.416   26.642  1.00 53.54  ? 150 ASN E CB  1 
ATOM   9082  C CG  . ASN E 1 147 ? 34.359  6.462   25.988  1.00 62.26  ? 150 ASN E CG  1 
ATOM   9083  O OD1 . ASN E 1 147 ? 34.730  5.684   25.109  1.00 62.56  ? 150 ASN E OD1 1 
ATOM   9084  N ND2 . ASN E 1 147 ? 33.102  6.512   26.417  1.00 60.76  ? 150 ASN E ND2 1 
ATOM   9085  N N   . VAL E 1 148 ? 38.096  7.617   28.770  1.00 53.87  ? 151 VAL E N   1 
ATOM   9086  C CA  . VAL E 1 148 ? 39.068  8.526   29.358  1.00 58.25  ? 151 VAL E CA  1 
ATOM   9087  C C   . VAL E 1 148 ? 40.187  7.701   29.980  1.00 57.61  ? 151 VAL E C   1 
ATOM   9088  O O   . VAL E 1 148 ? 40.034  6.508   30.251  1.00 57.22  ? 151 VAL E O   1 
ATOM   9089  C CB  . VAL E 1 148 ? 38.426  9.472   30.395  1.00 49.15  ? 151 VAL E CB  1 
ATOM   9090  C CG1 . VAL E 1 148 ? 37.625  10.545  29.692  1.00 42.73  ? 151 VAL E CG1 1 
ATOM   9091  C CG2 . VAL E 1 148 ? 37.532  8.701   31.326  1.00 39.36  ? 151 VAL E CG2 1 
ATOM   9092  N N   . VAL E 1 149 ? 41.330  8.351   30.190  1.00 61.42  ? 152 VAL E N   1 
ATOM   9093  C CA  . VAL E 1 149 ? 42.553  7.687   30.629  1.00 49.26  ? 152 VAL E CA  1 
ATOM   9094  C C   . VAL E 1 149 ? 42.992  8.279   31.961  1.00 54.99  ? 152 VAL E C   1 
ATOM   9095  O O   . VAL E 1 149 ? 43.121  9.502   32.091  1.00 61.55  ? 152 VAL E O   1 
ATOM   9096  C CB  . VAL E 1 149 ? 43.678  7.821   29.586  1.00 49.31  ? 152 VAL E CB  1 
ATOM   9097  C CG1 . VAL E 1 149 ? 44.880  6.991   29.997  1.00 67.09  ? 152 VAL E CG1 1 
ATOM   9098  C CG2 . VAL E 1 149 ? 43.187  7.404   28.211  1.00 60.12  ? 152 VAL E CG2 1 
ATOM   9099  N N   . TRP E 1 150 ? 43.231  7.411   32.941  1.00 61.31  ? 153 TRP E N   1 
ATOM   9100  C CA  . TRP E 1 150 ? 43.801  7.825   34.217  1.00 56.99  ? 153 TRP E CA  1 
ATOM   9101  C C   . TRP E 1 150 ? 45.315  7.916   34.078  1.00 53.82  ? 153 TRP E C   1 
ATOM   9102  O O   . TRP E 1 150 ? 45.980  6.906   33.823  1.00 57.23  ? 153 TRP E O   1 
ATOM   9103  C CB  . TRP E 1 150 ? 43.423  6.835   35.316  1.00 52.41  ? 153 TRP E CB  1 
ATOM   9104  C CG  . TRP E 1 150 ? 43.635  7.353   36.704  1.00 47.07  ? 153 TRP E CG  1 
ATOM   9105  C CD1 . TRP E 1 150 ? 44.359  8.452   37.073  1.00 47.98  ? 153 TRP E CD1 1 
ATOM   9106  C CD2 . TRP E 1 150 ? 43.105  6.798   37.912  1.00 50.41  ? 153 TRP E CD2 1 
ATOM   9107  N NE1 . TRP E 1 150 ? 44.310  8.615   38.439  1.00 47.69  ? 153 TRP E NE1 1 
ATOM   9108  C CE2 . TRP E 1 150 ? 43.546  7.612   38.977  1.00 45.44  ? 153 TRP E CE2 1 
ATOM   9109  C CE3 . TRP E 1 150 ? 42.296  5.693   38.197  1.00 56.75  ? 153 TRP E CE3 1 
ATOM   9110  C CZ2 . TRP E 1 150 ? 43.208  7.353   40.303  1.00 54.79  ? 153 TRP E CZ2 1 
ATOM   9111  C CZ3 . TRP E 1 150 ? 41.963  5.439   39.515  1.00 65.88  ? 153 TRP E CZ3 1 
ATOM   9112  C CH2 . TRP E 1 150 ? 42.417  6.266   40.551  1.00 59.99  ? 153 TRP E CH2 1 
ATOM   9113  N N   . LEU E 1 151 ? 45.861  9.116   34.252  1.00 56.80  ? 154 LEU E N   1 
ATOM   9114  C CA  . LEU E 1 151 ? 47.291  9.335   34.090  1.00 55.82  ? 154 LEU E CA  1 
ATOM   9115  C C   . LEU E 1 151 ? 47.998  9.219   35.435  1.00 59.46  ? 154 LEU E C   1 
ATOM   9116  O O   . LEU E 1 151 ? 47.610  9.874   36.409  1.00 61.65  ? 154 LEU E O   1 
ATOM   9117  C CB  . LEU E 1 151 ? 47.563  10.699  33.457  1.00 48.31  ? 154 LEU E CB  1 
ATOM   9118  C CG  . LEU E 1 151 ? 47.176  10.810  31.980  1.00 50.92  ? 154 LEU E CG  1 
ATOM   9119  C CD1 . LEU E 1 151 ? 47.206  12.260  31.535  1.00 64.42  ? 154 LEU E CD1 1 
ATOM   9120  C CD2 . LEU E 1 151 ? 48.080  9.958   31.101  1.00 53.56  ? 154 LEU E CD2 1 
ATOM   9121  N N   . THR E 1 152 ? 49.035  8.383   35.481  1.00 51.37  ? 155 THR E N   1 
ATOM   9122  C CA  . THR E 1 152 ? 49.769  8.096   36.704  1.00 63.08  ? 155 THR E CA  1 
ATOM   9123  C C   . THR E 1 152 ? 51.253  8.370   36.478  1.00 61.90  ? 155 THR E C   1 
ATOM   9124  O O   . THR E 1 152 ? 51.743  8.356   35.345  1.00 55.40  ? 155 THR E O   1 
ATOM   9125  C CB  . THR E 1 152 ? 49.556  6.637   37.153  1.00 57.76  ? 155 THR E CB  1 
ATOM   9126  O OG1 . THR E 1 152 ? 48.226  6.222   36.816  1.00 65.10  ? 155 THR E OG1 1 
ATOM   9127  C CG2 . THR E 1 152 ? 49.748  6.494   38.654  1.00 68.00  ? 155 THR E CG2 1 
ATOM   9128  N N   . LYS E 1 153 ? 51.966  8.624   37.575  1.00 54.73  ? 156 LYS E N   1 
ATOM   9129  C CA  . LYS E 1 153 ? 53.401  8.879   37.502  1.00 67.71  ? 156 LYS E CA  1 
ATOM   9130  C C   . LYS E 1 153 ? 54.147  7.664   36.954  1.00 61.54  ? 156 LYS E C   1 
ATOM   9131  O O   . LYS E 1 153 ? 53.743  6.515   37.152  1.00 68.95  ? 156 LYS E O   1 
ATOM   9132  C CB  . LYS E 1 153 ? 53.949  9.250   38.882  1.00 62.87  ? 156 LYS E CB  1 
ATOM   9133  C CG  . LYS E 1 153 ? 54.078  8.078   39.843  1.00 60.83  ? 156 LYS E CG  1 
ATOM   9134  C CD  . LYS E 1 153 ? 54.376  8.553   41.258  1.00 68.23  ? 156 LYS E CD  1 
ATOM   9135  C CE  . LYS E 1 153 ? 55.005  7.448   42.093  1.00 71.39  ? 156 LYS E CE  1 
ATOM   9136  N NZ  . LYS E 1 153 ? 55.282  7.896   43.487  1.00 76.50  ? 156 LYS E NZ  1 
ATOM   9137  N N   . LYS E 1 154 ? 55.237  7.935   36.234  1.00 57.57  ? 157 LYS E N   1 
ATOM   9138  C CA  . LYS E 1 154 ? 56.069  6.905   35.623  1.00 61.17  ? 157 LYS E CA  1 
ATOM   9139  C C   . LYS E 1 154 ? 57.531  7.194   35.926  1.00 71.16  ? 157 LYS E C   1 
ATOM   9140  O O   . LYS E 1 154 ? 57.985  8.333   35.769  1.00 73.21  ? 157 LYS E O   1 
ATOM   9141  C CB  . LYS E 1 154 ? 55.851  6.838   34.108  1.00 64.20  ? 157 LYS E CB  1 
ATOM   9142  C CG  . LYS E 1 154 ? 56.444  5.601   33.463  1.00 67.64  ? 157 LYS E CG  1 
ATOM   9143  C CD  . LYS E 1 154 ? 55.944  5.423   32.041  1.00 65.53  ? 157 LYS E CD  1 
ATOM   9144  C CE  . LYS E 1 154 ? 56.987  5.873   31.036  1.00 68.28  ? 157 LYS E CE  1 
ATOM   9145  N NZ  . LYS E 1 154 ? 57.130  4.915   29.902  1.00 65.11  ? 157 LYS E NZ  1 
ATOM   9146  N N   . ASN E 1 155 ? 58.261  6.159   36.346  1.00 76.08  ? 158 ASN E N   1 
ATOM   9147  C CA  . ASN E 1 155 ? 59.662  6.285   36.757  1.00 72.36  ? 158 ASN E CA  1 
ATOM   9148  C C   . ASN E 1 155 ? 59.829  7.365   37.823  1.00 66.15  ? 158 ASN E C   1 
ATOM   9149  O O   . ASN E 1 155 ? 60.794  8.133   37.815  1.00 70.92  ? 158 ASN E O   1 
ATOM   9150  C CB  . ASN E 1 155 ? 60.571  6.560   35.556  1.00 64.91  ? 158 ASN E CB  1 
ATOM   9151  C CG  . ASN E 1 155 ? 60.452  5.499   34.482  1.00 72.54  ? 158 ASN E CG  1 
ATOM   9152  O OD1 . ASN E 1 155 ? 60.685  4.316   34.734  1.00 74.25  ? 158 ASN E OD1 1 
ATOM   9153  N ND2 . ASN E 1 155 ? 60.085  5.918   33.275  1.00 67.58  ? 158 ASN E ND2 1 
ATOM   9154  N N   . ASP E 1 156 ? 58.875  7.411   38.756  1.00 72.54  ? 159 ASP E N   1 
ATOM   9155  C CA  . ASP E 1 156 ? 58.847  8.417   39.821  1.00 88.01  ? 159 ASP E CA  1 
ATOM   9156  C C   . ASP E 1 156 ? 58.857  9.836   39.254  1.00 82.91  ? 159 ASP E C   1 
ATOM   9157  O O   . ASP E 1 156 ? 59.545  10.722  39.763  1.00 92.36  ? 159 ASP E O   1 
ATOM   9158  C CB  . ASP E 1 156 ? 60.006  8.217   40.802  1.00 89.47  ? 159 ASP E CB  1 
ATOM   9159  C CG  . ASP E 1 156 ? 59.723  7.135   41.823  1.00 109.96 ? 159 ASP E CG  1 
ATOM   9160  O OD1 . ASP E 1 156 ? 58.532  6.884   42.108  1.00 111.22 ? 159 ASP E OD1 1 
ATOM   9161  O OD2 . ASP E 1 156 ? 60.690  6.532   42.338  1.00 128.73 ? 159 ASP E OD2 1 
ATOM   9162  N N   . ALA E 1 157 ? 58.084  10.057  38.193  1.00 73.15  ? 160 ALA E N   1 
ATOM   9163  C CA  . ALA E 1 157 ? 58.071  11.357  37.541  1.00 76.95  ? 160 ALA E CA  1 
ATOM   9164  C C   . ALA E 1 157 ? 56.716  11.601  36.894  1.00 71.35  ? 160 ALA E C   1 
ATOM   9165  O O   . ALA E 1 157 ? 56.123  10.689  36.311  1.00 74.62  ? 160 ALA E O   1 
ATOM   9166  C CB  . ALA E 1 157 ? 59.183  11.459  36.489  1.00 69.66  ? 160 ALA E CB  1 
ATOM   9167  N N   . TYR E 1 158 ? 56.238  12.841  37.000  1.00 67.64  ? 161 TYR E N   1 
ATOM   9168  C CA  . TYR E 1 158 ? 55.030  13.296  36.311  1.00 71.40  ? 161 TYR E CA  1 
ATOM   9169  C C   . TYR E 1 158 ? 55.388  14.570  35.557  1.00 69.95  ? 161 TYR E C   1 
ATOM   9170  O O   . TYR E 1 158 ? 55.207  15.683  36.075  1.00 54.93  ? 161 TYR E O   1 
ATOM   9171  C CB  . TYR E 1 158 ? 53.874  13.529  37.285  1.00 63.24  ? 161 TYR E CB  1 
ATOM   9172  C CG  . TYR E 1 158 ? 52.503  13.570  36.630  1.00 66.34  ? 161 TYR E CG  1 
ATOM   9173  C CD1 . TYR E 1 158 ? 52.143  14.612  35.778  1.00 63.36  ? 161 TYR E CD1 1 
ATOM   9174  C CD2 . TYR E 1 158 ? 51.566  12.573  36.870  1.00 60.64  ? 161 TYR E CD2 1 
ATOM   9175  C CE1 . TYR E 1 158 ? 50.892  14.652  35.178  1.00 65.90  ? 161 TYR E CE1 1 
ATOM   9176  C CE2 . TYR E 1 158 ? 50.312  12.605  36.277  1.00 65.20  ? 161 TYR E CE2 1 
ATOM   9177  C CZ  . TYR E 1 158 ? 49.978  13.647  35.433  1.00 73.51  ? 161 TYR E CZ  1 
ATOM   9178  O OH  . TYR E 1 158 ? 48.729  13.682  34.845  1.00 63.98  ? 161 TYR E OH  1 
ATOM   9179  N N   . PRO E 1 159 ? 55.917  14.446  34.338  1.00 70.07  ? 162 PRO E N   1 
ATOM   9180  C CA  . PRO E 1 159 ? 56.249  15.642  33.554  1.00 67.93  ? 162 PRO E CA  1 
ATOM   9181  C C   . PRO E 1 159 ? 55.005  16.473  33.275  1.00 66.47  ? 162 PRO E C   1 
ATOM   9182  O O   . PRO E 1 159 ? 53.915  15.939  33.062  1.00 65.48  ? 162 PRO E O   1 
ATOM   9183  C CB  . PRO E 1 159 ? 56.845  15.072  32.260  1.00 65.37  ? 162 PRO E CB  1 
ATOM   9184  C CG  . PRO E 1 159 ? 57.116  13.625  32.532  1.00 57.91  ? 162 PRO E CG  1 
ATOM   9185  C CD  . PRO E 1 159 ? 56.164  13.200  33.595  1.00 67.74  ? 162 PRO E CD  1 
ATOM   9186  N N   . THR E 1 160 ? 55.179  17.792  33.276  1.00 63.68  ? 163 THR E N   1 
ATOM   9187  C CA  . THR E 1 160 ? 54.066  18.691  33.001  1.00 55.29  ? 163 THR E CA  1 
ATOM   9188  C C   . THR E 1 160 ? 53.552  18.470  31.584  1.00 65.30  ? 163 THR E C   1 
ATOM   9189  O O   . THR E 1 160 ? 54.311  18.571  30.616  1.00 69.21  ? 163 THR E O   1 
ATOM   9190  C CB  . THR E 1 160 ? 54.498  20.143  33.196  1.00 56.13  ? 163 THR E CB  1 
ATOM   9191  O OG1 . THR E 1 160 ? 54.964  20.331  34.539  1.00 57.08  ? 163 THR E OG1 1 
ATOM   9192  C CG2 . THR E 1 160 ? 53.328  21.079  32.940  1.00 71.93  ? 163 THR E CG2 1 
ATOM   9193  N N   . ILE E 1 161 ? 52.262  18.167  31.467  1.00 53.79  ? 164 ILE E N   1 
ATOM   9194  C CA  . ILE E 1 161 ? 51.660  17.854  30.175  1.00 68.75  ? 164 ILE E CA  1 
ATOM   9195  C C   . ILE E 1 161 ? 51.254  19.152  29.492  1.00 66.98  ? 164 ILE E C   1 
ATOM   9196  O O   . ILE E 1 161 ? 50.482  19.941  30.045  1.00 66.35  ? 164 ILE E O   1 
ATOM   9197  C CB  . ILE E 1 161 ? 50.452  16.922  30.334  1.00 63.02  ? 164 ILE E CB  1 
ATOM   9198  C CG1 . ILE E 1 161 ? 50.905  15.507  30.691  1.00 66.69  ? 164 ILE E CG1 1 
ATOM   9199  C CG2 . ILE E 1 161 ? 49.633  16.906  29.057  1.00 65.14  ? 164 ILE E CG2 1 
ATOM   9200  C CD1 . ILE E 1 161 ? 49.906  14.744  31.534  1.00 65.94  ? 164 ILE E CD1 1 
ATOM   9201  N N   . LYS E 1 162 ? 51.773  19.377  28.286  1.00 65.31  ? 165 LYS E N   1 
ATOM   9202  C CA  . LYS E 1 162 ? 51.411  20.529  27.461  1.00 65.62  ? 165 LYS E CA  1 
ATOM   9203  C C   . LYS E 1 162 ? 51.077  19.974  26.083  1.00 66.86  ? 165 LYS E C   1 
ATOM   9204  O O   . LYS E 1 162 ? 51.940  19.905  25.204  1.00 70.12  ? 165 LYS E O   1 
ATOM   9205  C CB  . LYS E 1 162 ? 52.535  21.561  27.404  1.00 69.69  ? 165 LYS E CB  1 
ATOM   9206  C CG  . LYS E 1 162 ? 52.397  22.695  28.408  1.00 79.83  ? 165 LYS E CG  1 
ATOM   9207  C CD  . LYS E 1 162 ? 53.450  23.776  28.179  1.00 86.59  ? 165 LYS E CD  1 
ATOM   9208  C CE  . LYS E 1 162 ? 53.010  24.758  27.100  1.00 91.22  ? 165 LYS E CE  1 
ATOM   9209  N NZ  . LYS E 1 162 ? 53.875  25.974  27.056  1.00 83.10  ? 165 LYS E NZ  1 
ATOM   9210  N N   . MET E 1 163 ? 49.824  19.572  25.898  1.00 62.73  ? 166 MET E N   1 
ATOM   9211  C CA  . MET E 1 163 ? 49.386  18.964  24.654  1.00 63.01  ? 166 MET E CA  1 
ATOM   9212  C C   . MET E 1 163 ? 48.101  19.630  24.188  1.00 67.95  ? 166 MET E C   1 
ATOM   9213  O O   . MET E 1 163 ? 47.417  20.317  24.951  1.00 70.44  ? 166 MET E O   1 
ATOM   9214  C CB  . MET E 1 163 ? 49.184  17.450  24.814  1.00 57.63  ? 166 MET E CB  1 
ATOM   9215  C CG  . MET E 1 163 ? 47.983  17.062  25.662  1.00 69.63  ? 166 MET E CG  1 
ATOM   9216  S SD  . MET E 1 163 ? 46.473  16.846  24.703  1.00 86.69  ? 166 MET E SD  1 
ATOM   9217  C CE  . MET E 1 163 ? 47.109  16.057  23.224  1.00 69.23  ? 166 MET E CE  1 
ATOM   9218  N N   . SER E 1 164 ? 47.780  19.420  22.914  1.00 59.59  ? 167 SER E N   1 
ATOM   9219  C CA  . SER E 1 164 ? 46.572  19.991  22.345  1.00 54.96  ? 167 SER E CA  1 
ATOM   9220  C C   . SER E 1 164 ? 46.020  19.049  21.286  1.00 63.08  ? 167 SER E C   1 
ATOM   9221  O O   . SER E 1 164 ? 46.736  18.208  20.737  1.00 60.50  ? 167 SER E O   1 
ATOM   9222  C CB  . SER E 1 164 ? 46.832  21.379  21.747  1.00 51.23  ? 167 SER E CB  1 
ATOM   9223  O OG  . SER E 1 164 ? 47.468  21.280  20.486  1.00 64.80  ? 167 SER E OG  1 
ATOM   9224  N N   . TYR E 1 165 ? 44.724  19.194  21.018  1.00 55.76  ? 168 TYR E N   1 
ATOM   9225  C CA  . TYR E 1 165 ? 44.062  18.500  19.925  1.00 53.24  ? 168 TYR E CA  1 
ATOM   9226  C C   . TYR E 1 165 ? 43.294  19.515  19.093  1.00 60.88  ? 168 TYR E C   1 
ATOM   9227  O O   . TYR E 1 165 ? 42.634  20.405  19.636  1.00 64.10  ? 168 TYR E O   1 
ATOM   9228  C CB  . TYR E 1 165 ? 43.106  17.408  20.425  1.00 50.42  ? 168 TYR E CB  1 
ATOM   9229  C CG  . TYR E 1 165 ? 42.297  16.771  19.314  1.00 61.77  ? 168 TYR E CG  1 
ATOM   9230  C CD1 . TYR E 1 165 ? 42.841  15.769  18.517  1.00 64.49  ? 168 TYR E CD1 1 
ATOM   9231  C CD2 . TYR E 1 165 ? 40.993  17.175  19.056  1.00 55.89  ? 168 TYR E CD2 1 
ATOM   9232  C CE1 . TYR E 1 165 ? 42.107  15.186  17.496  1.00 64.56  ? 168 TYR E CE1 1 
ATOM   9233  C CE2 . TYR E 1 165 ? 40.252  16.597  18.038  1.00 59.67  ? 168 TYR E CE2 1 
ATOM   9234  C CZ  . TYR E 1 165 ? 40.813  15.605  17.262  1.00 64.41  ? 168 TYR E CZ  1 
ATOM   9235  O OH  . TYR E 1 165 ? 40.076  15.032  16.250  1.00 61.81  ? 168 TYR E OH  1 
ATOM   9236  N N   . ASN E 1 166 ? 43.383  19.370  17.777  1.00 61.72  ? 169 ASN E N   1 
ATOM   9237  C CA  . ASN E 1 166 ? 42.760  20.276  16.824  1.00 59.50  ? 169 ASN E CA  1 
ATOM   9238  C C   . ASN E 1 166 ? 41.645  19.528  16.107  1.00 63.87  ? 169 ASN E C   1 
ATOM   9239  O O   . ASN E 1 166 ? 41.881  18.462  15.528  1.00 70.82  ? 169 ASN E O   1 
ATOM   9240  C CB  . ASN E 1 166 ? 43.811  20.796  15.837  1.00 67.61  ? 169 ASN E CB  1 
ATOM   9241  C CG  . ASN E 1 166 ? 43.243  21.727  14.772  1.00 66.59  ? 169 ASN E CG  1 
ATOM   9242  O OD1 . ASN E 1 166 ? 42.302  21.382  14.057  1.00 61.27  ? 169 ASN E OD1 1 
ATOM   9243  N ND2 . ASN E 1 166 ? 43.843  22.915  14.649  1.00 63.96  ? 169 ASN E ND2 1 
ATOM   9244  N N   . ASN E 1 167 ? 40.434  20.084  16.149  1.00 64.37  ? 170 ASN E N   1 
ATOM   9245  C CA  . ASN E 1 167 ? 39.292  19.435  15.518  1.00 63.12  ? 170 ASN E CA  1 
ATOM   9246  C C   . ASN E 1 167 ? 39.376  19.562  14.003  1.00 67.00  ? 170 ASN E C   1 
ATOM   9247  O O   . ASN E 1 167 ? 38.885  20.537  13.423  1.00 69.00  ? 170 ASN E O   1 
ATOM   9248  C CB  . ASN E 1 167 ? 37.976  20.025  16.028  1.00 52.87  ? 170 ASN E CB  1 
ATOM   9249  C CG  . ASN E 1 167 ? 36.765  19.235  15.561  1.00 59.50  ? 170 ASN E CG  1 
ATOM   9250  O OD1 . ASN E 1 167 ? 36.899  18.235  14.859  1.00 55.63  ? 170 ASN E OD1 1 
ATOM   9251  N ND2 . ASN E 1 167 ? 35.575  19.682  15.950  1.00 58.64  ? 170 ASN E ND2 1 
ATOM   9252  N N   . THR E 1 168 ? 39.997  18.574  13.357  1.00 62.77  ? 171 THR E N   1 
ATOM   9253  C CA  . THR E 1 168 ? 40.127  18.559  11.907  1.00 71.79  ? 171 THR E CA  1 
ATOM   9254  C C   . THR E 1 168 ? 38.875  18.051  11.201  1.00 70.85  ? 171 THR E C   1 
ATOM   9255  O O   . THR E 1 168 ? 38.761  18.224  9.983   1.00 79.05  ? 171 THR E O   1 
ATOM   9256  C CB  . THR E 1 168 ? 41.332  17.703  11.502  1.00 70.86  ? 171 THR E CB  1 
ATOM   9257  O OG1 . THR E 1 168 ? 41.185  16.383  12.039  1.00 73.74  ? 171 THR E OG1 1 
ATOM   9258  C CG2 . THR E 1 168 ? 42.620  18.314  12.034  1.00 53.75  ? 171 THR E CG2 1 
ATOM   9259  N N   . ASN E 1 169 ? 37.938  17.441  11.927  1.00 71.22  ? 172 ASN E N   1 
ATOM   9260  C CA  . ASN E 1 169 ? 36.705  16.960  11.318  1.00 78.44  ? 172 ASN E CA  1 
ATOM   9261  C C   . ASN E 1 169 ? 35.773  18.129  10.998  1.00 79.15  ? 172 ASN E C   1 
ATOM   9262  O O   . ASN E 1 169 ? 35.972  19.267  11.436  1.00 78.20  ? 172 ASN E O   1 
ATOM   9263  C CB  . ASN E 1 169 ? 35.999  15.963  12.237  1.00 67.57  ? 172 ASN E CB  1 
ATOM   9264  C CG  . ASN E 1 169 ? 36.953  14.957  12.852  1.00 80.91  ? 172 ASN E CG  1 
ATOM   9265  O OD1 . ASN E 1 169 ? 37.353  13.989  12.205  1.00 95.51  ? 172 ASN E OD1 1 
ATOM   9266  N ND2 . ASN E 1 169 ? 37.322  15.181  14.112  1.00 66.54  ? 172 ASN E ND2 1 
ATOM   9267  N N   . GLY E 1 170 ? 34.746  17.838  10.210  1.00 70.17  ? 173 GLY E N   1 
ATOM   9268  C CA  . GLY E 1 170 ? 33.790  18.841  9.801   1.00 71.88  ? 173 GLY E CA  1 
ATOM   9269  C C   . GLY E 1 170 ? 32.610  19.020  10.728  1.00 70.67  ? 173 GLY E C   1 
ATOM   9270  O O   . GLY E 1 170 ? 31.678  19.755  10.387  1.00 75.89  ? 173 GLY E O   1 
ATOM   9271  N N   . GLU E 1 171 ? 32.613  18.374  11.891  1.00 66.02  ? 174 GLU E N   1 
ATOM   9272  C CA  . GLU E 1 171 ? 31.492  18.431  12.815  1.00 65.04  ? 174 GLU E CA  1 
ATOM   9273  C C   . GLU E 1 171 ? 31.976  18.867  14.191  1.00 59.35  ? 174 GLU E C   1 
ATOM   9274  O O   . GLU E 1 171 ? 33.174  18.855  14.485  1.00 63.93  ? 174 GLU E O   1 
ATOM   9275  C CB  . GLU E 1 171 ? 30.772  17.074  12.916  1.00 57.95  ? 174 GLU E CB  1 
ATOM   9276  C CG  . GLU E 1 171 ? 30.777  16.264  11.622  1.00 73.81  ? 174 GLU E CG  1 
ATOM   9277  C CD  . GLU E 1 171 ? 29.644  15.252  11.544  1.00 78.25  ? 174 GLU E CD  1 
ATOM   9278  O OE1 . GLU E 1 171 ? 29.347  14.596  12.566  1.00 81.60  ? 174 GLU E OE1 1 
ATOM   9279  O OE2 . GLU E 1 171 ? 29.052  15.108  10.454  1.00 73.66  ? 174 GLU E OE2 1 
ATOM   9280  N N   . ASP E 1 172 ? 31.022  19.263  15.028  1.00 63.31  ? 175 ASP E N   1 
ATOM   9281  C CA  . ASP E 1 172 ? 31.321  19.599  16.412  1.00 61.03  ? 175 ASP E CA  1 
ATOM   9282  C C   . ASP E 1 172 ? 31.762  18.356  17.174  1.00 60.10  ? 175 ASP E C   1 
ATOM   9283  O O   . ASP E 1 172 ? 31.313  17.239  16.900  1.00 64.18  ? 175 ASP E O   1 
ATOM   9284  C CB  . ASP E 1 172 ? 30.098  20.212  17.098  1.00 78.95  ? 175 ASP E CB  1 
ATOM   9285  C CG  . ASP E 1 172 ? 29.692  21.548  16.504  1.00 80.30  ? 175 ASP E CG  1 
ATOM   9286  O OD1 . ASP E 1 172 ? 30.493  22.137  15.750  1.00 85.58  ? 175 ASP E OD1 1 
ATOM   9287  O OD2 . ASP E 1 172 ? 28.568  22.011  16.795  1.00 78.07  ? 175 ASP E OD2 1 
ATOM   9288  N N   . LEU E 1 173 ? 32.648  18.557  18.143  1.00 56.26  ? 176 LEU E N   1 
ATOM   9289  C CA  . LEU E 1 173 ? 33.160  17.473  18.970  1.00 54.36  ? 176 LEU E CA  1 
ATOM   9290  C C   . LEU E 1 173 ? 32.759  17.719  20.416  1.00 49.44  ? 176 LEU E C   1 
ATOM   9291  O O   . LEU E 1 173 ? 33.087  18.765  20.986  1.00 55.91  ? 176 LEU E O   1 
ATOM   9292  C CB  . LEU E 1 173 ? 34.682  17.359  18.846  1.00 44.54  ? 176 LEU E CB  1 
ATOM   9293  C CG  . LEU E 1 173 ? 35.222  16.431  17.755  1.00 56.02  ? 176 LEU E CG  1 
ATOM   9294  C CD1 . LEU E 1 173 ? 36.737  16.328  17.843  1.00 72.13  ? 176 LEU E CD1 1 
ATOM   9295  C CD2 . LEU E 1 173 ? 34.591  15.048  17.839  1.00 52.98  ? 176 LEU E CD2 1 
ATOM   9296  N N   . LEU E 1 174 ? 32.060  16.756  21.008  1.00 50.04  ? 177 LEU E N   1 
ATOM   9297  C CA  . LEU E 1 174 ? 31.826  16.744  22.445  1.00 52.33  ? 177 LEU E CA  1 
ATOM   9298  C C   . LEU E 1 174 ? 32.995  16.026  23.114  1.00 48.74  ? 177 LEU E C   1 
ATOM   9299  O O   . LEU E 1 174 ? 33.253  14.852  22.826  1.00 45.27  ? 177 LEU E O   1 
ATOM   9300  C CB  . LEU E 1 174 ? 30.500  16.060  22.773  1.00 52.88  ? 177 LEU E CB  1 
ATOM   9301  C CG  . LEU E 1 174 ? 30.246  15.651  24.225  1.00 58.92  ? 177 LEU E CG  1 
ATOM   9302  C CD1 . LEU E 1 174 ? 30.245  16.863  25.152  1.00 44.14  ? 177 LEU E CD1 1 
ATOM   9303  C CD2 . LEU E 1 174 ? 28.931  14.884  24.324  1.00 51.03  ? 177 LEU E CD2 1 
ATOM   9304  N N   . ILE E 1 175 ? 33.706  16.739  23.987  1.00 49.22  ? 178 ILE E N   1 
ATOM   9305  C CA  . ILE E 1 175 ? 34.927  16.254  24.622  1.00 47.38  ? 178 ILE E CA  1 
ATOM   9306  C C   . ILE E 1 175 ? 34.728  16.289  26.131  1.00 46.78  ? 178 ILE E C   1 
ATOM   9307  O O   . ILE E 1 175 ? 34.232  17.283  26.673  1.00 49.83  ? 178 ILE E O   1 
ATOM   9308  C CB  . ILE E 1 175 ? 36.151  17.096  24.215  1.00 50.69  ? 178 ILE E CB  1 
ATOM   9309  C CG1 . ILE E 1 175 ? 36.350  17.056  22.699  1.00 57.45  ? 178 ILE E CG1 1 
ATOM   9310  C CG2 . ILE E 1 175 ? 37.414  16.605  24.928  1.00 45.86  ? 178 ILE E CG2 1 
ATOM   9311  C CD1 . ILE E 1 175 ? 37.693  17.600  22.247  1.00 46.23  ? 178 ILE E CD1 1 
ATOM   9312  N N   . LEU E 1 176 ? 35.115  15.209  26.805  1.00 45.48  ? 179 LEU E N   1 
ATOM   9313  C CA  . LEU E 1 176 ? 34.996  15.099  28.251  1.00 46.26  ? 179 LEU E CA  1 
ATOM   9314  C C   . LEU E 1 176 ? 36.359  14.811  28.861  1.00 48.17  ? 179 LEU E C   1 
ATOM   9315  O O   . LEU E 1 176 ? 37.166  14.075  28.286  1.00 43.08  ? 179 LEU E O   1 
ATOM   9316  C CB  . LEU E 1 176 ? 34.011  14.001  28.647  1.00 45.36  ? 179 LEU E CB  1 
ATOM   9317  C CG  . LEU E 1 176 ? 32.566  14.204  28.196  1.00 55.12  ? 179 LEU E CG  1 
ATOM   9318  C CD1 . LEU E 1 176 ? 32.301  13.406  26.931  1.00 50.71  ? 179 LEU E CD1 1 
ATOM   9319  C CD2 . LEU E 1 176 ? 31.595  13.808  29.302  1.00 44.78  ? 179 LEU E CD2 1 
ATOM   9320  N N   . TRP E 1 177 ? 36.607  15.409  30.023  1.00 37.45  ? 180 TRP E N   1 
ATOM   9321  C CA  . TRP E 1 177 ? 37.844  15.225  30.765  1.00 40.40  ? 180 TRP E CA  1 
ATOM   9322  C C   . TRP E 1 177 ? 37.516  15.385  32.240  1.00 49.77  ? 180 TRP E C   1 
ATOM   9323  O O   . TRP E 1 177 ? 36.391  15.730  32.608  1.00 47.86  ? 180 TRP E O   1 
ATOM   9324  C CB  . TRP E 1 177 ? 38.919  16.230  30.336  1.00 45.02  ? 180 TRP E CB  1 
ATOM   9325  C CG  . TRP E 1 177 ? 38.567  17.649  30.699  1.00 52.44  ? 180 TRP E CG  1 
ATOM   9326  C CD1 . TRP E 1 177 ? 38.935  18.326  31.827  1.00 41.51  ? 180 TRP E CD1 1 
ATOM   9327  C CD2 . TRP E 1 177 ? 37.760  18.556  29.932  1.00 51.97  ? 180 TRP E CD2 1 
ATOM   9328  N NE1 . TRP E 1 177 ? 38.413  19.599  31.806  1.00 47.01  ? 180 TRP E NE1 1 
ATOM   9329  C CE2 . TRP E 1 177 ? 37.690  19.766  30.653  1.00 54.39  ? 180 TRP E CE2 1 
ATOM   9330  C CE3 . TRP E 1 177 ? 37.095  18.463  28.703  1.00 44.89  ? 180 TRP E CE3 1 
ATOM   9331  C CZ2 . TRP E 1 177 ? 36.979  20.873  30.188  1.00 50.82  ? 180 TRP E CZ2 1 
ATOM   9332  C CZ3 . TRP E 1 177 ? 36.393  19.562  28.241  1.00 50.06  ? 180 TRP E CZ3 1 
ATOM   9333  C CH2 . TRP E 1 177 ? 36.337  20.750  28.983  1.00 50.97  ? 180 TRP E CH2 1 
ATOM   9334  N N   . GLY E 1 178 ? 38.510  15.151  33.091  1.00 49.11  ? 181 GLY E N   1 
ATOM   9335  C CA  . GLY E 1 178 ? 38.221  15.213  34.511  1.00 41.46  ? 181 GLY E CA  1 
ATOM   9336  C C   . GLY E 1 178 ? 39.452  15.447  35.353  1.00 45.03  ? 181 GLY E C   1 
ATOM   9337  O O   . GLY E 1 178 ? 40.587  15.411  34.874  1.00 50.71  ? 181 GLY E O   1 
ATOM   9338  N N   . ILE E 1 179 ? 39.198  15.689  36.637  1.00 43.68  ? 182 ILE E N   1 
ATOM   9339  C CA  . ILE E 1 179 ? 40.232  15.879  37.642  1.00 42.49  ? 182 ILE E CA  1 
ATOM   9340  C C   . ILE E 1 179 ? 39.950  14.934  38.804  1.00 55.86  ? 182 ILE E C   1 
ATOM   9341  O O   . ILE E 1 179 ? 38.802  14.798  39.243  1.00 47.48  ? 182 ILE E O   1 
ATOM   9342  C CB  . ILE E 1 179 ? 40.297  17.346  38.120  1.00 48.18  ? 182 ILE E CB  1 
ATOM   9343  C CG1 . ILE E 1 179 ? 41.399  17.534  39.161  1.00 46.71  ? 182 ILE E CG1 1 
ATOM   9344  C CG2 . ILE E 1 179 ? 38.957  17.801  38.674  1.00 43.29  ? 182 ILE E CG2 1 
ATOM   9345  C CD1 . ILE E 1 179 ? 41.871  18.968  39.282  1.00 47.35  ? 182 ILE E CD1 1 
ATOM   9346  N N   . HIS E 1 180 ? 40.994  14.272  39.294  1.00 55.27  ? 183 HIS E N   1 
ATOM   9347  C CA  . HIS E 1 180 ? 40.869  13.319  40.389  1.00 52.10  ? 183 HIS E CA  1 
ATOM   9348  C C   . HIS E 1 180 ? 41.204  13.998  41.708  1.00 56.07  ? 183 HIS E C   1 
ATOM   9349  O O   . HIS E 1 180 ? 42.277  14.593  41.849  1.00 57.05  ? 183 HIS E O   1 
ATOM   9350  C CB  . HIS E 1 180 ? 41.788  12.116  40.174  1.00 50.43  ? 183 HIS E CB  1 
ATOM   9351  C CG  . HIS E 1 180 ? 41.916  11.236  41.378  1.00 61.53  ? 183 HIS E CG  1 
ATOM   9352  N ND1 . HIS E 1 180 ? 43.123  10.717  41.797  1.00 62.17  ? 183 HIS E ND1 1 
ATOM   9353  C CD2 . HIS E 1 180 ? 40.988  10.785  42.257  1.00 63.34  ? 183 HIS E CD2 1 
ATOM   9354  C CE1 . HIS E 1 180 ? 42.932  9.984   42.879  1.00 67.64  ? 183 HIS E CE1 1 
ATOM   9355  N NE2 . HIS E 1 180 ? 41.646  10.010  43.180  1.00 61.82  ? 183 HIS E NE2 1 
ATOM   9356  N N   . HIS E 1 181 ? 40.295  13.894  42.674  1.00 51.54  ? 184 HIS E N   1 
ATOM   9357  C CA  . HIS E 1 181 ? 40.515  14.444  44.005  1.00 51.09  ? 184 HIS E CA  1 
ATOM   9358  C C   . HIS E 1 181 ? 41.092  13.356  44.907  1.00 64.66  ? 184 HIS E C   1 
ATOM   9359  O O   . HIS E 1 181 ? 40.468  12.306  45.101  1.00 60.04  ? 184 HIS E O   1 
ATOM   9360  C CB  . HIS E 1 181 ? 39.211  14.996  44.582  1.00 51.58  ? 184 HIS E CB  1 
ATOM   9361  C CG  . HIS E 1 181 ? 38.653  16.160  43.818  1.00 69.45  ? 184 HIS E CG  1 
ATOM   9362  N ND1 . HIS E 1 181 ? 37.609  16.036  42.926  1.00 73.58  ? 184 HIS E ND1 1 
ATOM   9363  C CD2 . HIS E 1 181 ? 38.988  17.473  43.820  1.00 68.10  ? 184 HIS E CD2 1 
ATOM   9364  C CE1 . HIS E 1 181 ? 37.331  17.218  42.407  1.00 53.74  ? 184 HIS E CE1 1 
ATOM   9365  N NE2 . HIS E 1 181 ? 38.152  18.108  42.934  1.00 52.72  ? 184 HIS E NE2 1 
ATOM   9366  N N   . SER E 1 182 ? 42.283  13.607  45.451  1.00 64.48  ? 185 SER E N   1 
ATOM   9367  C CA  . SER E 1 182 ? 42.949  12.668  46.341  1.00 51.67  ? 185 SER E CA  1 
ATOM   9368  C C   . SER E 1 182 ? 42.457  12.843  47.777  1.00 59.60  ? 185 SER E C   1 
ATOM   9369  O O   . SER E 1 182 ? 41.734  13.785  48.110  1.00 64.57  ? 185 SER E O   1 
ATOM   9370  C CB  . SER E 1 182 ? 44.463  12.854  46.280  1.00 62.88  ? 185 SER E CB  1 
ATOM   9371  O OG  . SER E 1 182 ? 44.942  12.627  44.968  1.00 76.85  ? 185 SER E OG  1 
ATOM   9372  N N   . ASN E 1 183 ? 42.878  11.923  48.644  1.00 61.57  ? 186 ASN E N   1 
ATOM   9373  C CA  . ASN E 1 183 ? 42.410  11.897  50.023  1.00 56.58  ? 186 ASN E CA  1 
ATOM   9374  C C   . ASN E 1 183 ? 43.423  12.421  51.028  1.00 65.15  ? 186 ASN E C   1 
ATOM   9375  O O   . ASN E 1 183 ? 43.023  12.963  52.064  1.00 66.41  ? 186 ASN E O   1 
ATOM   9376  C CB  . ASN E 1 183 ? 42.009  10.471  50.411  1.00 62.50  ? 186 ASN E CB  1 
ATOM   9377  C CG  . ASN E 1 183 ? 41.092  9.836   49.390  1.00 64.98  ? 186 ASN E CG  1 
ATOM   9378  O OD1 . ASN E 1 183 ? 40.001  10.343  49.125  1.00 64.43  ? 186 ASN E OD1 1 
ATOM   9379  N ND2 . ASN E 1 183 ? 41.529  8.727   48.805  1.00 53.61  ? 186 ASN E ND2 1 
ATOM   9380  N N   . ASN E 1 184 ? 44.718  12.273  50.753  1.00 69.20  ? 187 ASN E N   1 
ATOM   9381  C CA  . ASN E 1 184 ? 45.761  12.729  51.662  1.00 62.07  ? 187 ASN E CA  1 
ATOM   9382  C C   . ASN E 1 184 ? 47.035  12.975  50.866  1.00 56.73  ? 187 ASN E C   1 
ATOM   9383  O O   . ASN E 1 184 ? 47.172  12.539  49.719  1.00 61.31  ? 187 ASN E O   1 
ATOM   9384  C CB  . ASN E 1 184 ? 46.012  11.720  52.787  1.00 46.50  ? 187 ASN E CB  1 
ATOM   9385  C CG  . ASN E 1 184 ? 46.173  10.304  52.274  1.00 65.70  ? 187 ASN E CG  1 
ATOM   9386  O OD1 . ASN E 1 184 ? 47.052  10.018  51.459  1.00 61.61  ? 187 ASN E OD1 1 
ATOM   9387  N ND2 . ASN E 1 184 ? 45.318  9.406   52.751  1.00 66.16  ? 187 ASN E ND2 1 
ATOM   9388  N N   . ALA E 1 185 ? 47.979  13.674  51.499  1.00 57.04  ? 188 ALA E N   1 
ATOM   9389  C CA  . ALA E 1 185 ? 49.224  14.022  50.823  1.00 53.64  ? 188 ALA E CA  1 
ATOM   9390  C C   . ALA E 1 185 ? 49.992  12.780  50.395  1.00 59.07  ? 188 ALA E C   1 
ATOM   9391  O O   . ALA E 1 185 ? 50.629  12.773  49.335  1.00 62.72  ? 188 ALA E O   1 
ATOM   9392  C CB  . ALA E 1 185 ? 50.084  14.897  51.730  1.00 43.82  ? 188 ALA E CB  1 
ATOM   9393  N N   . ALA E 1 186 ? 49.935  11.716  51.201  1.00 64.67  ? 189 ALA E N   1 
ATOM   9394  C CA  . ALA E 1 186 ? 50.642  10.481  50.868  1.00 60.20  ? 189 ALA E CA  1 
ATOM   9395  C C   . ALA E 1 186 ? 50.109  9.869   49.578  1.00 61.72  ? 189 ALA E C   1 
ATOM   9396  O O   . ALA E 1 186 ? 50.880  9.515   48.676  1.00 52.33  ? 189 ALA E O   1 
ATOM   9397  C CB  . ALA E 1 186 ? 50.524  9.486   52.023  1.00 64.23  ? 189 ALA E CB  1 
ATOM   9398  N N   . GLU E 1 187 ? 48.785  9.737   49.473  1.00 67.59  ? 190 GLU E N   1 
ATOM   9399  C CA  . GLU E 1 187 ? 48.188  9.197   48.256  1.00 63.27  ? 190 GLU E CA  1 
ATOM   9400  C C   . GLU E 1 187 ? 48.485  10.092  47.058  1.00 66.30  ? 190 GLU E C   1 
ATOM   9401  O O   . GLU E 1 187 ? 48.706  9.601   45.944  1.00 56.55  ? 190 GLU E O   1 
ATOM   9402  C CB  . GLU E 1 187 ? 46.681  9.028   48.452  1.00 61.94  ? 190 GLU E CB  1 
ATOM   9403  C CG  . GLU E 1 187 ? 45.983  8.214   47.375  1.00 75.58  ? 190 GLU E CG  1 
ATOM   9404  C CD  . GLU E 1 187 ? 44.602  8.757   47.034  1.00 78.07  ? 190 GLU E CD  1 
ATOM   9405  O OE1 . GLU E 1 187 ? 43.943  9.345   47.922  1.00 76.17  ? 190 GLU E OE1 1 
ATOM   9406  O OE2 . GLU E 1 187 ? 44.176  8.601   45.872  1.00 81.05  ? 190 GLU E OE2 1 
ATOM   9407  N N   . GLN E 1 188 ? 48.503  11.411  47.272  1.00 60.30  ? 191 GLN E N   1 
ATOM   9408  C CA  . GLN E 1 188 ? 48.795  12.337  46.183  1.00 60.25  ? 191 GLN E CA  1 
ATOM   9409  C C   . GLN E 1 188 ? 50.193  12.101  45.620  1.00 64.46  ? 191 GLN E C   1 
ATOM   9410  O O   . GLN E 1 188 ? 50.382  12.039  44.398  1.00 56.80  ? 191 GLN E O   1 
ATOM   9411  C CB  . GLN E 1 188 ? 48.643  13.778  46.674  1.00 59.66  ? 191 GLN E CB  1 
ATOM   9412  C CG  . GLN E 1 188 ? 49.133  14.830  45.692  1.00 70.01  ? 191 GLN E CG  1 
ATOM   9413  C CD  . GLN E 1 188 ? 48.249  14.949  44.462  1.00 61.65  ? 191 GLN E CD  1 
ATOM   9414  O OE1 . GLN E 1 188 ? 47.136  14.425  44.425  1.00 65.10  ? 191 GLN E OE1 1 
ATOM   9415  N NE2 . GLN E 1 188 ? 48.747  15.635  43.443  1.00 63.74  ? 191 GLN E NE2 1 
ATOM   9416  N N   . ILE E 1 189 ? 51.185  11.951  46.502  1.00 58.53  ? 192 ILE E N   1 
ATOM   9417  C CA  . ILE E 1 189 ? 52.550  11.693  46.054  1.00 51.36  ? 192 ILE E CA  1 
ATOM   9418  C C   . ILE E 1 189 ? 52.654  10.311  45.426  1.00 58.58  ? 192 ILE E C   1 
ATOM   9419  O O   . ILE E 1 189 ? 53.344  10.123  44.416  1.00 54.82  ? 192 ILE E O   1 
ATOM   9420  C CB  . ILE E 1 189 ? 53.533  11.855  47.228  1.00 66.07  ? 192 ILE E CB  1 
ATOM   9421  C CG1 . ILE E 1 189 ? 53.387  13.240  47.862  1.00 54.40  ? 192 ILE E CG1 1 
ATOM   9422  C CG2 . ILE E 1 189 ? 54.967  11.608  46.773  1.00 48.98  ? 192 ILE E CG2 1 
ATOM   9423  C CD1 . ILE E 1 189 ? 53.974  13.328  49.253  1.00 58.52  ? 192 ILE E CD1 1 
ATOM   9424  N N   . ASN E 1 190 ? 51.967  9.323   46.007  1.00 52.75  ? 193 ASN E N   1 
ATOM   9425  C CA  . ASN E 1 190 ? 52.068  7.956   45.506  1.00 61.97  ? 193 ASN E CA  1 
ATOM   9426  C C   . ASN E 1 190 ? 51.520  7.825   44.090  1.00 65.84  ? 193 ASN E C   1 
ATOM   9427  O O   . ASN E 1 190 ? 51.971  6.958   43.331  1.00 62.33  ? 193 ASN E O   1 
ATOM   9428  C CB  . ASN E 1 190 ? 51.340  6.997   46.449  1.00 59.30  ? 193 ASN E CB  1 
ATOM   9429  C CG  . ASN E 1 190 ? 51.459  5.553   46.009  1.00 76.05  ? 193 ASN E CG  1 
ATOM   9430  O OD1 . ASN E 1 190 ? 50.461  4.842   45.895  1.00 91.71  ? 193 ASN E OD1 1 
ATOM   9431  N ND2 . ASN E 1 190 ? 52.686  5.115   45.747  1.00 83.05  ? 193 ASN E ND2 1 
ATOM   9432  N N   . LEU E 1 191 ? 50.563  8.674   43.711  1.00 66.54  ? 194 LEU E N   1 
ATOM   9433  C CA  . LEU E 1 191 ? 49.959  8.632   42.383  1.00 64.02  ? 194 LEU E CA  1 
ATOM   9434  C C   . LEU E 1 191 ? 50.611  9.582   41.387  1.00 62.49  ? 194 LEU E C   1 
ATOM   9435  O O   . LEU E 1 191 ? 50.796  9.215   40.220  1.00 47.98  ? 194 LEU E O   1 
ATOM   9436  C CB  . LEU E 1 191 ? 48.466  8.958   42.465  1.00 64.50  ? 194 LEU E CB  1 
ATOM   9437  C CG  . LEU E 1 191 ? 47.600  8.040   43.321  1.00 68.60  ? 194 LEU E CG  1 
ATOM   9438  C CD1 . LEU E 1 191 ? 46.171  8.555   43.350  1.00 60.01  ? 194 LEU E CD1 1 
ATOM   9439  C CD2 . LEU E 1 191 ? 47.661  6.605   42.813  1.00 72.39  ? 194 LEU E CD2 1 
ATOM   9440  N N   . TYR E 1 192 ? 50.961  10.797  41.812  1.00 53.57  ? 195 TYR E N   1 
ATOM   9441  C CA  . TYR E 1 192 ? 51.437  11.820  40.888  1.00 64.83  ? 195 TYR E CA  1 
ATOM   9442  C C   . TYR E 1 192 ? 52.770  12.453  41.268  1.00 66.92  ? 195 TYR E C   1 
ATOM   9443  O O   . TYR E 1 192 ? 53.346  13.156  40.428  1.00 61.51  ? 195 TYR E O   1 
ATOM   9444  C CB  . TYR E 1 192 ? 50.383  12.931  40.742  1.00 65.88  ? 195 TYR E CB  1 
ATOM   9445  C CG  . TYR E 1 192 ? 48.973  12.399  40.596  1.00 53.56  ? 195 TYR E CG  1 
ATOM   9446  C CD1 . TYR E 1 192 ? 48.547  11.840  39.398  1.00 49.71  ? 195 TYR E CD1 1 
ATOM   9447  C CD2 . TYR E 1 192 ? 48.077  12.440  41.657  1.00 49.38  ? 195 TYR E CD2 1 
ATOM   9448  C CE1 . TYR E 1 192 ? 47.268  11.342  39.255  1.00 56.85  ? 195 TYR E CE1 1 
ATOM   9449  C CE2 . TYR E 1 192 ? 46.789  11.943  41.525  1.00 53.18  ? 195 TYR E CE2 1 
ATOM   9450  C CZ  . TYR E 1 192 ? 46.391  11.395  40.317  1.00 62.40  ? 195 TYR E CZ  1 
ATOM   9451  O OH  . TYR E 1 192 ? 45.116  10.897  40.159  1.00 52.25  ? 195 TYR E OH  1 
ATOM   9452  N N   . LYS E 1 193 ? 53.249  12.274  42.504  1.00 64.13  ? 196 LYS E N   1 
ATOM   9453  C CA  . LYS E 1 193 ? 54.559  12.733  42.965  1.00 72.57  ? 196 LYS E CA  1 
ATOM   9454  C C   . LYS E 1 193 ? 54.609  14.253  43.116  1.00 67.36  ? 196 LYS E C   1 
ATOM   9455  O O   . LYS E 1 193 ? 55.546  14.791  43.713  1.00 72.47  ? 196 LYS E O   1 
ATOM   9456  C CB  . LYS E 1 193 ? 55.663  12.235  42.017  1.00 72.13  ? 196 LYS E CB  1 
ATOM   9457  C CG  . LYS E 1 193 ? 57.092  12.593  42.419  1.00 73.25  ? 196 LYS E CG  1 
ATOM   9458  C CD  . LYS E 1 193 ? 57.612  11.675  43.517  1.00 90.59  ? 196 LYS E CD  1 
ATOM   9459  C CE  . LYS E 1 193 ? 58.600  10.652  42.973  1.00 93.53  ? 196 LYS E CE  1 
ATOM   9460  N NZ  . LYS E 1 193 ? 58.475  9.333   43.659  1.00 85.19  ? 196 LYS E NZ  1 
ATOM   9461  N N   . ASN E 1 194 ? 53.583  14.954  42.645  1.00 73.41  ? 197 ASN E N   1 
ATOM   9462  C CA  . ASN E 1 194 ? 53.568  16.410  42.720  1.00 63.02  ? 197 ASN E CA  1 
ATOM   9463  C C   . ASN E 1 194 ? 52.524  16.853  43.736  1.00 67.45  ? 197 ASN E C   1 
ATOM   9464  O O   . ASN E 1 194 ? 51.318  16.712  43.480  1.00 78.78  ? 197 ASN E O   1 
ATOM   9465  C CB  . ASN E 1 194 ? 53.282  17.014  41.345  1.00 58.05  ? 197 ASN E CB  1 
ATOM   9466  C CG  . ASN E 1 194 ? 54.402  16.749  40.351  1.00 63.03  ? 197 ASN E CG  1 
ATOM   9467  O OD1 . ASN E 1 194 ? 55.579  16.806  40.704  1.00 72.59  ? 197 ASN E OD1 1 
ATOM   9468  N ND2 . ASN E 1 194 ? 54.041  16.456  39.107  1.00 58.19  ? 197 ASN E ND2 1 
ATOM   9469  N N   . PRO E 1 195 ? 52.929  17.370  44.900  1.00 67.55  ? 198 PRO E N   1 
ATOM   9470  C CA  . PRO E 1 195 ? 51.930  17.716  45.930  1.00 65.48  ? 198 PRO E CA  1 
ATOM   9471  C C   . PRO E 1 195 ? 50.966  18.813  45.504  1.00 68.79  ? 198 PRO E C   1 
ATOM   9472  O O   . PRO E 1 195 ? 49.762  18.715  45.776  1.00 58.91  ? 198 PRO E O   1 
ATOM   9473  C CB  . PRO E 1 195 ? 52.797  18.145  47.124  1.00 65.67  ? 198 PRO E CB  1 
ATOM   9474  C CG  . PRO E 1 195 ? 54.113  18.553  46.520  1.00 51.37  ? 198 PRO E CG  1 
ATOM   9475  C CD  . PRO E 1 195 ? 54.308  17.668  45.326  1.00 56.46  ? 198 PRO E CD  1 
ATOM   9476  N N   . THR E 1 196 ? 51.461  19.853  44.837  1.00 71.44  ? 199 THR E N   1 
ATOM   9477  C CA  . THR E 1 196 ? 50.639  20.968  44.384  1.00 74.05  ? 199 THR E CA  1 
ATOM   9478  C C   . THR E 1 196 ? 50.423  20.837  42.882  1.00 64.93  ? 199 THR E C   1 
ATOM   9479  O O   . THR E 1 196 ? 51.382  20.896  42.104  1.00 75.34  ? 199 THR E O   1 
ATOM   9480  C CB  . THR E 1 196 ? 51.296  22.304  44.727  1.00 74.98  ? 199 THR E CB  1 
ATOM   9481  O OG1 . THR E 1 196 ? 51.491  22.381  46.145  1.00 62.41  ? 199 THR E OG1 1 
ATOM   9482  C CG2 . THR E 1 196 ? 50.421  23.464  44.274  1.00 64.58  ? 199 THR E CG2 1 
ATOM   9483  N N   . THR E 1 197 ? 49.167  20.674  42.479  1.00 58.31  ? 200 THR E N   1 
ATOM   9484  C CA  . THR E 1 197 ? 48.843  20.242  41.129  1.00 58.03  ? 200 THR E CA  1 
ATOM   9485  C C   . THR E 1 197 ? 47.663  21.042  40.597  1.00 55.82  ? 200 THR E C   1 
ATOM   9486  O O   . THR E 1 197 ? 46.927  21.685  41.353  1.00 57.12  ? 200 THR E O   1 
ATOM   9487  C CB  . THR E 1 197 ? 48.529  18.742  41.104  1.00 64.98  ? 200 THR E CB  1 
ATOM   9488  O OG1 . THR E 1 197 ? 47.969  18.381  39.835  1.00 64.80  ? 200 THR E OG1 1 
ATOM   9489  C CG2 . THR E 1 197 ? 47.543  18.401  42.212  1.00 40.68  ? 200 THR E CG2 1 
ATOM   9490  N N   . TYR E 1 198 ? 47.498  20.997  39.275  1.00 54.46  ? 201 TYR E N   1 
ATOM   9491  C CA  . TYR E 1 198 ? 46.461  21.760  38.593  1.00 53.90  ? 201 TYR E CA  1 
ATOM   9492  C C   . TYR E 1 198 ? 46.124  21.083  37.271  1.00 61.45  ? 201 TYR E C   1 
ATOM   9493  O O   . TYR E 1 198 ? 46.911  20.293  36.734  1.00 51.82  ? 201 TYR E O   1 
ATOM   9494  C CB  . TYR E 1 198 ? 46.903  23.206  38.346  1.00 53.81  ? 201 TYR E CB  1 
ATOM   9495  C CG  . TYR E 1 198 ? 48.038  23.310  37.354  1.00 53.74  ? 201 TYR E CG  1 
ATOM   9496  C CD1 . TYR E 1 198 ? 49.357  23.189  37.769  1.00 50.73  ? 201 TYR E CD1 1 
ATOM   9497  C CD2 . TYR E 1 198 ? 47.790  23.517  36.003  1.00 57.91  ? 201 TYR E CD2 1 
ATOM   9498  C CE1 . TYR E 1 198 ? 50.401  23.272  36.863  1.00 54.35  ? 201 TYR E CE1 1 
ATOM   9499  C CE2 . TYR E 1 198 ? 48.827  23.601  35.091  1.00 64.90  ? 201 TYR E CE2 1 
ATOM   9500  C CZ  . TYR E 1 198 ? 50.129  23.480  35.526  1.00 56.06  ? 201 TYR E CZ  1 
ATOM   9501  O OH  . TYR E 1 198 ? 51.157  23.567  34.618  1.00 68.07  ? 201 TYR E OH  1 
ATOM   9502  N N   . VAL E 1 199 ? 44.943  21.417  36.749  1.00 59.00  ? 202 VAL E N   1 
ATOM   9503  C CA  . VAL E 1 199 ? 44.492  20.994  35.424  1.00 52.98  ? 202 VAL E CA  1 
ATOM   9504  C C   . VAL E 1 199 ? 43.892  22.215  34.742  1.00 61.34  ? 202 VAL E C   1 
ATOM   9505  O O   . VAL E 1 199 ? 42.872  22.748  35.202  1.00 68.28  ? 202 VAL E O   1 
ATOM   9506  C CB  . VAL E 1 199 ? 43.458  19.862  35.490  1.00 58.83  ? 202 VAL E CB  1 
ATOM   9507  C CG1 . VAL E 1 199 ? 42.891  19.605  34.102  1.00 57.99  ? 202 VAL E CG1 1 
ATOM   9508  C CG2 . VAL E 1 199 ? 44.074  18.603  36.063  1.00 55.84  ? 202 VAL E CG2 1 
ATOM   9509  N N   . SER E 1 200 ? 44.511  22.662  33.653  1.00 50.92  ? 203 SER E N   1 
ATOM   9510  C CA  . SER E 1 200 ? 44.036  23.823  32.912  1.00 55.70  ? 203 SER E CA  1 
ATOM   9511  C C   . SER E 1 200 ? 43.601  23.385  31.524  1.00 54.96  ? 203 SER E C   1 
ATOM   9512  O O   . SER E 1 200 ? 44.303  22.619  30.859  1.00 51.88  ? 203 SER E O   1 
ATOM   9513  C CB  . SER E 1 200 ? 45.111  24.910  32.800  1.00 53.39  ? 203 SER E CB  1 
ATOM   9514  O OG  . SER E 1 200 ? 46.072  24.585  31.812  1.00 73.40  ? 203 SER E OG  1 
ATOM   9515  N N   . VAL E 1 201 ? 42.431  23.860  31.105  1.00 47.31  ? 204 VAL E N   1 
ATOM   9516  C CA  . VAL E 1 201 ? 41.839  23.521  29.817  1.00 47.67  ? 204 VAL E CA  1 
ATOM   9517  C C   . VAL E 1 201 ? 41.417  24.813  29.134  1.00 53.95  ? 204 VAL E C   1 
ATOM   9518  O O   . VAL E 1 201 ? 40.730  25.640  29.741  1.00 56.96  ? 204 VAL E O   1 
ATOM   9519  C CB  . VAL E 1 201 ? 40.627  22.577  29.967  1.00 51.11  ? 204 VAL E CB  1 
ATOM   9520  C CG1 . VAL E 1 201 ? 40.185  22.062  28.604  1.00 47.51  ? 204 VAL E CG1 1 
ATOM   9521  C CG2 . VAL E 1 201 ? 40.948  21.422  30.909  1.00 46.86  ? 204 VAL E CG2 1 
ATOM   9522  N N   . GLY E 1 202 ? 41.816  24.978  27.876  1.00 51.85  ? 205 GLY E N   1 
ATOM   9523  C CA  . GLY E 1 202 ? 41.487  26.174  27.131  1.00 50.32  ? 205 GLY E CA  1 
ATOM   9524  C C   . GLY E 1 202 ? 41.091  25.910  25.692  1.00 57.89  ? 205 GLY E C   1 
ATOM   9525  O O   . GLY E 1 202 ? 41.658  25.034  25.030  1.00 56.80  ? 205 GLY E O   1 
ATOM   9526  N N   . THR E 1 203 ? 40.102  26.659  25.206  1.00 48.26  ? 206 THR E N   1 
ATOM   9527  C CA  . THR E 1 203 ? 39.674  26.627  23.810  1.00 50.06  ? 206 THR E CA  1 
ATOM   9528  C C   . THR E 1 203 ? 39.490  28.070  23.353  1.00 55.71  ? 206 THR E C   1 
ATOM   9529  O O   . THR E 1 203 ? 39.933  29.011  24.019  1.00 57.61  ? 206 THR E O   1 
ATOM   9530  C CB  . THR E 1 203 ? 38.382  25.816  23.615  1.00 57.83  ? 206 THR E CB  1 
ATOM   9531  O OG1 . THR E 1 203 ? 37.275  26.513  24.199  1.00 60.41  ? 206 THR E OG1 1 
ATOM   9532  C CG2 . THR E 1 203 ? 38.496  24.434  24.242  1.00 54.12  ? 206 THR E CG2 1 
ATOM   9533  N N   . SER E 1 204 ? 38.842  28.252  22.200  1.00 49.41  ? 207 SER E N   1 
ATOM   9534  C CA  . SER E 1 204 ? 38.525  29.605  21.756  1.00 51.17  ? 207 SER E CA  1 
ATOM   9535  C C   . SER E 1 204 ? 37.592  30.312  22.735  1.00 52.95  ? 207 SER E C   1 
ATOM   9536  O O   . SER E 1 204 ? 37.627  31.543  22.846  1.00 56.11  ? 207 SER E O   1 
ATOM   9537  C CB  . SER E 1 204 ? 37.912  29.574  20.356  1.00 44.74  ? 207 SER E CB  1 
ATOM   9538  O OG  . SER E 1 204 ? 36.612  29.015  20.377  1.00 65.46  ? 207 SER E OG  1 
ATOM   9539  N N   . THR E 1 205 ? 36.773  29.555  23.469  1.00 55.55  ? 208 THR E N   1 
ATOM   9540  C CA  . THR E 1 205 ? 35.846  30.115  24.445  1.00 52.24  ? 208 THR E CA  1 
ATOM   9541  C C   . THR E 1 205 ? 36.060  29.617  25.867  1.00 48.99  ? 208 THR E C   1 
ATOM   9542  O O   . THR E 1 205 ? 35.740  30.343  26.811  1.00 50.45  ? 208 THR E O   1 
ATOM   9543  C CB  . THR E 1 205 ? 34.395  29.812  24.043  1.00 59.96  ? 208 THR E CB  1 
ATOM   9544  O OG1 . THR E 1 205 ? 34.176  28.396  24.099  1.00 55.74  ? 208 THR E OG1 1 
ATOM   9545  C CG2 . THR E 1 205 ? 34.109  30.316  22.629  1.00 51.41  ? 208 THR E CG2 1 
ATOM   9546  N N   . LEU E 1 206 ? 36.581  28.405  26.048  1.00 53.53  ? 209 LEU E N   1 
ATOM   9547  C CA  . LEU E 1 206 ? 36.760  27.842  27.379  1.00 41.20  ? 209 LEU E CA  1 
ATOM   9548  C C   . LEU E 1 206 ? 38.061  28.324  28.003  1.00 52.22  ? 209 LEU E C   1 
ATOM   9549  O O   . LEU E 1 206 ? 39.091  28.431  27.332  1.00 54.73  ? 209 LEU E O   1 
ATOM   9550  C CB  . LEU E 1 206 ? 36.746  26.313  27.322  1.00 51.37  ? 209 LEU E CB  1 
ATOM   9551  C CG  . LEU E 1 206 ? 36.893  25.560  28.649  1.00 53.17  ? 209 LEU E CG  1 
ATOM   9552  C CD1 . LEU E 1 206 ? 35.674  25.775  29.535  1.00 45.57  ? 209 LEU E CD1 1 
ATOM   9553  C CD2 . LEU E 1 206 ? 37.109  24.079  28.396  1.00 41.58  ? 209 LEU E CD2 1 
ATOM   9554  N N   . ASN E 1 207 ? 38.008  28.616  29.299  1.00 52.73  ? 210 ASN E N   1 
ATOM   9555  C CA  . ASN E 1 207 ? 39.178  29.083  30.041  1.00 42.85  ? 210 ASN E CA  1 
ATOM   9556  C C   . ASN E 1 207 ? 39.019  28.560  31.471  1.00 55.05  ? 210 ASN E C   1 
ATOM   9557  O O   . ASN E 1 207 ? 38.408  29.214  32.319  1.00 58.76  ? 210 ASN E O   1 
ATOM   9558  C CB  . ASN E 1 207 ? 39.281  30.601  29.990  1.00 43.61  ? 210 ASN E CB  1 
ATOM   9559  C CG  . ASN E 1 207 ? 40.525  31.130  30.669  1.00 56.48  ? 210 ASN E CG  1 
ATOM   9560  O OD1 . ASN E 1 207 ? 41.582  30.496  30.647  1.00 50.83  ? 210 ASN E OD1 1 
ATOM   9561  N ND2 . ASN E 1 207 ? 40.404  32.304  31.280  1.00 56.26  ? 210 ASN E ND2 1 
ATOM   9562  N N   . GLN E 1 208 ? 39.586  27.381  31.727  1.00 41.15  ? 211 GLN E N   1 
ATOM   9563  C CA  . GLN E 1 208 ? 39.297  26.629  32.940  1.00 41.17  ? 211 GLN E CA  1 
ATOM   9564  C C   . GLN E 1 208 ? 40.585  26.245  33.649  1.00 50.75  ? 211 GLN E C   1 
ATOM   9565  O O   . GLN E 1 208 ? 41.563  25.847  33.012  1.00 55.01  ? 211 GLN E O   1 
ATOM   9566  C CB  . GLN E 1 208 ? 38.484  25.371  32.608  1.00 45.44  ? 211 GLN E CB  1 
ATOM   9567  C CG  . GLN E 1 208 ? 38.278  24.404  33.756  1.00 44.60  ? 211 GLN E CG  1 
ATOM   9568  C CD  . GLN E 1 208 ? 37.397  23.233  33.354  1.00 58.80  ? 211 GLN E CD  1 
ATOM   9569  O OE1 . GLN E 1 208 ? 37.886  22.192  32.916  1.00 58.85  ? 211 GLN E OE1 1 
ATOM   9570  N NE2 . GLN E 1 208 ? 36.087  23.406  33.488  1.00 57.24  ? 211 GLN E NE2 1 
ATOM   9571  N N   . ARG E 1 209 ? 40.575  26.360  34.974  1.00 51.95  ? 212 ARG E N   1 
ATOM   9572  C CA  . ARG E 1 209 ? 41.712  25.978  35.806  1.00 55.87  ? 212 ARG E CA  1 
ATOM   9573  C C   . ARG E 1 209 ? 41.172  25.226  37.015  1.00 60.74  ? 212 ARG E C   1 
ATOM   9574  O O   . ARG E 1 209 ? 40.465  25.812  37.839  1.00 52.71  ? 212 ARG E O   1 
ATOM   9575  C CB  . ARG E 1 209 ? 42.513  27.203  36.237  1.00 59.59  ? 212 ARG E CB  1 
ATOM   9576  C CG  . ARG E 1 209 ? 43.494  26.932  37.356  1.00 61.73  ? 212 ARG E CG  1 
ATOM   9577  C CD  . ARG E 1 209 ? 44.920  27.110  36.886  1.00 64.97  ? 212 ARG E CD  1 
ATOM   9578  N NE  . ARG E 1 209 ? 45.859  27.100  38.000  1.00 68.69  ? 212 ARG E NE  1 
ATOM   9579  C CZ  . ARG E 1 209 ? 47.172  26.976  37.869  1.00 77.34  ? 212 ARG E CZ  1 
ATOM   9580  N NH1 . ARG E 1 209 ? 47.737  26.819  36.682  1.00 66.23  ? 212 ARG E NH1 1 
ATOM   9581  N NH2 . ARG E 1 209 ? 47.939  27.015  38.956  1.00 70.23  ? 212 ARG E NH2 1 
ATOM   9582  N N   . LEU E 1 210 ? 41.509  23.943  37.126  1.00 63.74  ? 213 LEU E N   1 
ATOM   9583  C CA  . LEU E 1 210 ? 41.012  23.083  38.192  1.00 55.28  ? 213 LEU E CA  1 
ATOM   9584  C C   . LEU E 1 210 ? 42.155  22.642  39.097  1.00 58.43  ? 213 LEU E C   1 
ATOM   9585  O O   . LEU E 1 210 ? 43.228  22.258  38.617  1.00 58.01  ? 213 LEU E O   1 
ATOM   9586  C CB  . LEU E 1 210 ? 40.310  21.848  37.621  1.00 57.98  ? 213 LEU E CB  1 
ATOM   9587  C CG  . LEU E 1 210 ? 39.187  22.097  36.616  1.00 53.14  ? 213 LEU E CG  1 
ATOM   9588  C CD1 . LEU E 1 210 ? 38.980  20.872  35.750  1.00 52.78  ? 213 LEU E CD1 1 
ATOM   9589  C CD2 . LEU E 1 210 ? 37.911  22.467  37.336  1.00 49.38  ? 213 LEU E CD2 1 
ATOM   9590  N N   . VAL E 1 211 ? 41.913  22.682  40.404  1.00 55.52  ? 214 VAL E N   1 
ATOM   9591  C CA  . VAL E 1 211 ? 42.878  22.261  41.412  1.00 53.81  ? 214 VAL E CA  1 
ATOM   9592  C C   . VAL E 1 211 ? 42.209  21.217  42.295  1.00 63.12  ? 214 VAL E C   1 
ATOM   9593  O O   . VAL E 1 211 ? 41.077  21.429  42.737  1.00 60.70  ? 214 VAL E O   1 
ATOM   9594  C CB  . VAL E 1 211 ? 43.386  23.443  42.258  1.00 54.73  ? 214 VAL E CB  1 
ATOM   9595  C CG1 . VAL E 1 211 ? 44.237  22.947  43.422  1.00 68.03  ? 214 VAL E CG1 1 
ATOM   9596  C CG2 . VAL E 1 211 ? 44.178  24.413  41.391  1.00 55.97  ? 214 VAL E CG2 1 
ATOM   9597  N N   . PRO E 1 212 ? 42.849  20.077  42.563  1.00 67.35  ? 215 PRO E N   1 
ATOM   9598  C CA  . PRO E 1 212 ? 42.208  19.049  43.390  1.00 57.98  ? 215 PRO E CA  1 
ATOM   9599  C C   . PRO E 1 212 ? 42.019  19.505  44.828  1.00 51.97  ? 215 PRO E C   1 
ATOM   9600  O O   . PRO E 1 212 ? 42.833  20.245  45.385  1.00 61.93  ? 215 PRO E O   1 
ATOM   9601  C CB  . PRO E 1 212 ? 43.182  17.867  43.312  1.00 58.67  ? 215 PRO E CB  1 
ATOM   9602  C CG  . PRO E 1 212 ? 44.033  18.142  42.116  1.00 51.22  ? 215 PRO E CG  1 
ATOM   9603  C CD  . PRO E 1 212 ? 44.155  19.632  42.054  1.00 52.01  ? 215 PRO E CD  1 
ATOM   9604  N N   . LYS E 1 213 ? 40.925  19.039  45.429  1.00 50.94  ? 216 LYS E N   1 
ATOM   9605  C CA  . LYS E 1 213 ? 40.625  19.264  46.839  1.00 50.43  ? 216 LYS E CA  1 
ATOM   9606  C C   . LYS E 1 213 ? 40.987  17.988  47.587  1.00 57.98  ? 216 LYS E C   1 
ATOM   9607  O O   . LYS E 1 213 ? 40.275  16.984  47.508  1.00 57.29  ? 216 LYS E O   1 
ATOM   9608  C CB  . LYS E 1 213 ? 39.156  19.632  47.037  1.00 57.80  ? 216 LYS E CB  1 
ATOM   9609  C CG  . LYS E 1 213 ? 38.602  20.587  45.993  1.00 59.57  ? 216 LYS E CG  1 
ATOM   9610  C CD  . LYS E 1 213 ? 37.129  20.889  46.239  1.00 62.30  ? 216 LYS E CD  1 
ATOM   9611  C CE  . LYS E 1 213 ? 36.365  21.035  44.927  1.00 41.24  ? 216 LYS E CE  1 
ATOM   9612  N NZ  . LYS E 1 213 ? 35.007  20.427  45.004  1.00 70.24  ? 216 LYS E NZ  1 
ATOM   9613  N N   . ILE E 1 214 ? 42.104  18.026  48.308  1.00 75.18  ? 217 ILE E N   1 
ATOM   9614  C CA  . ILE E 1 214 ? 42.608  16.868  49.037  1.00 58.54  ? 217 ILE E CA  1 
ATOM   9615  C C   . ILE E 1 214 ? 42.030  16.941  50.447  1.00 53.35  ? 217 ILE E C   1 
ATOM   9616  O O   . ILE E 1 214 ? 42.498  17.710  51.289  1.00 57.92  ? 217 ILE E O   1 
ATOM   9617  C CB  . ILE E 1 214 ? 44.137  16.821  49.047  1.00 59.99  ? 217 ILE E CB  1 
ATOM   9618  C CG1 . ILE E 1 214 ? 44.685  16.790  47.616  1.00 59.46  ? 217 ILE E CG1 1 
ATOM   9619  C CG2 . ILE E 1 214 ? 44.633  15.618  49.831  1.00 51.71  ? 217 ILE E CG2 1 
ATOM   9620  C CD1 . ILE E 1 214 ? 45.180  18.130  47.117  1.00 68.49  ? 217 ILE E CD1 1 
ATOM   9621  N N   . ALA E 1 215 ? 40.997  16.145  50.700  1.00 65.84  ? 218 ALA E N   1 
ATOM   9622  C CA  . ALA E 1 215 ? 40.353  16.119  52.004  1.00 65.22  ? 218 ALA E CA  1 
ATOM   9623  C C   . ALA E 1 215 ? 39.675  14.770  52.176  1.00 64.20  ? 218 ALA E C   1 
ATOM   9624  O O   . ALA E 1 215 ? 39.490  14.019  51.215  1.00 65.21  ? 218 ALA E O   1 
ATOM   9625  C CB  . ALA E 1 215 ? 39.349  17.263  52.166  1.00 48.28  ? 218 ALA E CB  1 
ATOM   9626  N N   . THR E 1 216 ? 39.313  14.472  53.419  1.00 69.08  ? 219 THR E N   1 
ATOM   9627  C CA  . THR E 1 216 ? 38.651  13.215  53.733  1.00 74.66  ? 219 THR E CA  1 
ATOM   9628  C C   . THR E 1 216 ? 37.164  13.314  53.412  1.00 70.42  ? 219 THR E C   1 
ATOM   9629  O O   . THR E 1 216 ? 36.500  14.284  53.793  1.00 59.54  ? 219 THR E O   1 
ATOM   9630  C CB  . THR E 1 216 ? 38.864  12.858  55.202  1.00 71.03  ? 219 THR E CB  1 
ATOM   9631  O OG1 . THR E 1 216 ? 38.680  14.029  56.006  1.00 85.36  ? 219 THR E OG1 1 
ATOM   9632  C CG2 . THR E 1 216 ? 40.277  12.323  55.416  1.00 75.02  ? 219 THR E CG2 1 
ATOM   9633  N N   . ARG E 1 217 ? 36.649  12.311  52.704  1.00 68.93  ? 220 ARG E N   1 
ATOM   9634  C CA  . ARG E 1 217 ? 35.252  12.265  52.300  1.00 71.22  ? 220 ARG E CA  1 
ATOM   9635  C C   . ARG E 1 217 ? 34.654  10.919  52.682  1.00 71.12  ? 220 ARG E C   1 
ATOM   9636  O O   . ARG E 1 217 ? 35.367  9.933   52.884  1.00 74.30  ? 220 ARG E O   1 
ATOM   9637  C CB  . ARG E 1 217 ? 35.089  12.494  50.790  1.00 59.10  ? 220 ARG E CB  1 
ATOM   9638  C CG  . ARG E 1 217 ? 35.105  13.957  50.390  1.00 65.08  ? 220 ARG E CG  1 
ATOM   9639  C CD  . ARG E 1 217 ? 35.594  14.130  48.967  1.00 57.59  ? 220 ARG E CD  1 
ATOM   9640  N NE  . ARG E 1 217 ? 36.942  13.604  48.791  1.00 62.26  ? 220 ARG E NE  1 
ATOM   9641  C CZ  . ARG E 1 217 ? 37.955  14.288  48.277  1.00 61.98  ? 220 ARG E CZ  1 
ATOM   9642  N NH1 . ARG E 1 217 ? 37.820  15.551  47.902  1.00 48.84  ? 220 ARG E NH1 1 
ATOM   9643  N NH2 . ARG E 1 217 ? 39.134  13.689  48.138  1.00 65.47  ? 220 ARG E NH2 1 
ATOM   9644  N N   . SER E 1 218 ? 33.327  10.894  52.782  1.00 73.72  ? 221 SER E N   1 
ATOM   9645  C CA  . SER E 1 218 ? 32.616  9.656   53.062  1.00 61.11  ? 221 SER E CA  1 
ATOM   9646  C C   . SER E 1 218 ? 32.763  8.681   51.900  1.00 57.54  ? 221 SER E C   1 
ATOM   9647  O O   . SER E 1 218 ? 32.810  9.072   50.731  1.00 71.70  ? 221 SER E O   1 
ATOM   9648  C CB  . SER E 1 218 ? 31.138  9.935   53.323  1.00 58.41  ? 221 SER E CB  1 
ATOM   9649  O OG  . SER E 1 218 ? 30.946  10.463  54.622  1.00 64.73  ? 221 SER E OG  1 
ATOM   9650  N N   . GLN E 1 219 ? 32.836  7.398   52.235  1.00 62.84  ? 222 GLN E N   1 
ATOM   9651  C CA  . GLN E 1 219 ? 33.043  6.372   51.224  1.00 60.97  ? 222 GLN E CA  1 
ATOM   9652  C C   . GLN E 1 219 ? 31.811  6.250   50.329  1.00 72.27  ? 222 GLN E C   1 
ATOM   9653  O O   . GLN E 1 219 ? 30.674  6.260   50.812  1.00 62.53  ? 222 GLN E O   1 
ATOM   9654  C CB  . GLN E 1 219 ? 33.368  5.037   51.905  1.00 57.50  ? 222 GLN E CB  1 
ATOM   9655  C CG  . GLN E 1 219 ? 32.817  3.790   51.224  1.00 72.73  ? 222 GLN E CG  1 
ATOM   9656  C CD  . GLN E 1 219 ? 31.385  3.468   51.622  1.00 79.24  ? 222 GLN E CD  1 
ATOM   9657  O OE1 . GLN E 1 219 ? 30.970  3.710   52.758  1.00 88.69  ? 222 GLN E OE1 1 
ATOM   9658  N NE2 . GLN E 1 219 ? 30.617  2.933   50.677  1.00 74.38  ? 222 GLN E NE2 1 
ATOM   9659  N N   . VAL E 1 220 ? 32.040  6.166   49.019  1.00 62.32  ? 223 VAL E N   1 
ATOM   9660  C CA  . VAL E 1 220 ? 31.009  5.847   48.037  1.00 48.24  ? 223 VAL E CA  1 
ATOM   9661  C C   . VAL E 1 220 ? 31.595  4.830   47.068  1.00 56.25  ? 223 VAL E C   1 
ATOM   9662  O O   . VAL E 1 220 ? 32.694  5.037   46.541  1.00 58.08  ? 223 VAL E O   1 
ATOM   9663  C CB  . VAL E 1 220 ? 30.513  7.096   47.279  1.00 54.65  ? 223 VAL E CB  1 
ATOM   9664  C CG1 . VAL E 1 220 ? 29.484  6.704   46.222  1.00 49.26  ? 223 VAL E CG1 1 
ATOM   9665  C CG2 . VAL E 1 220 ? 29.922  8.112   48.238  1.00 42.08  ? 223 VAL E CG2 1 
ATOM   9666  N N   . ASN E 1 221 ? 30.866  3.735   46.834  1.00 61.54  ? 224 ASN E N   1 
ATOM   9667  C CA  . ASN E 1 221 ? 31.376  2.600   46.057  1.00 59.27  ? 224 ASN E CA  1 
ATOM   9668  C C   . ASN E 1 221 ? 32.691  2.099   46.641  1.00 55.27  ? 224 ASN E C   1 
ATOM   9669  O O   . ASN E 1 221 ? 33.610  1.709   45.918  1.00 65.84  ? 224 ASN E O   1 
ATOM   9670  C CB  . ASN E 1 221 ? 31.545  2.953   44.577  1.00 54.33  ? 224 ASN E CB  1 
ATOM   9671  C CG  . ASN E 1 221 ? 30.242  3.347   43.920  1.00 59.19  ? 224 ASN E CG  1 
ATOM   9672  O OD1 . ASN E 1 221 ? 29.180  3.289   44.536  1.00 64.71  ? 224 ASN E OD1 1 
ATOM   9673  N ND2 . ASN E 1 221 ? 30.319  3.765   42.659  1.00 51.27  ? 224 ASN E ND2 1 
ATOM   9674  N N   . GLY E 1 222 ? 32.784  2.129   47.969  1.00 61.80  ? 225 GLY E N   1 
ATOM   9675  C CA  . GLY E 1 222 ? 34.002  1.739   48.652  1.00 67.04  ? 225 GLY E CA  1 
ATOM   9676  C C   . GLY E 1 222 ? 35.174  2.675   48.467  1.00 63.36  ? 225 GLY E C   1 
ATOM   9677  O O   . GLY E 1 222 ? 36.319  2.258   48.661  1.00 72.59  ? 225 GLY E O   1 
ATOM   9678  N N   . LEU E 1 223 ? 34.930  3.934   48.104  1.00 57.93  ? 226 LEU E N   1 
ATOM   9679  C CA  . LEU E 1 223 ? 36.011  4.849   47.765  1.00 58.62  ? 226 LEU E CA  1 
ATOM   9680  C C   . LEU E 1 223 ? 35.769  6.219   48.374  1.00 62.38  ? 226 LEU E C   1 
ATOM   9681  O O   . LEU E 1 223 ? 34.644  6.727   48.354  1.00 68.59  ? 226 LEU E O   1 
ATOM   9682  C CB  . LEU E 1 223 ? 36.157  4.989   46.249  1.00 56.11  ? 226 LEU E CB  1 
ATOM   9683  C CG  . LEU E 1 223 ? 36.936  3.863   45.585  1.00 52.27  ? 226 LEU E CG  1 
ATOM   9684  C CD1 . LEU E 1 223 ? 37.208  4.215   44.143  1.00 60.24  ? 226 LEU E CD1 1 
ATOM   9685  C CD2 . LEU E 1 223 ? 38.227  3.624   46.336  1.00 68.68  ? 226 LEU E CD2 1 
ATOM   9686  N N   . GLN E 1 224 ? 36.838  6.817   48.903  1.00 57.79  ? 227 GLN E N   1 
ATOM   9687  C CA  . GLN E 1 224 ? 36.793  8.178   49.421  1.00 59.93  ? 227 GLN E CA  1 
ATOM   9688  C C   . GLN E 1 224 ? 37.253  9.221   48.413  1.00 63.92  ? 227 GLN E C   1 
ATOM   9689  O O   . GLN E 1 224 ? 37.005  10.415  48.623  1.00 59.71  ? 227 GLN E O   1 
ATOM   9690  C CB  . GLN E 1 224 ? 37.651  8.298   50.684  1.00 62.55  ? 227 GLN E CB  1 
ATOM   9691  C CG  . GLN E 1 224 ? 37.140  7.489   51.857  1.00 70.16  ? 227 GLN E CG  1 
ATOM   9692  C CD  . GLN E 1 224 ? 38.101  7.503   53.024  1.00 74.08  ? 227 GLN E CD  1 
ATOM   9693  O OE1 . GLN E 1 224 ? 39.158  8.134   52.966  1.00 77.14  ? 227 GLN E OE1 1 
ATOM   9694  N NE2 . GLN E 1 224 ? 37.743  6.802   54.094  1.00 84.41  ? 227 GLN E NE2 1 
ATOM   9695  N N   . GLY E 1 225 ? 37.921  8.802   47.334  1.00 57.56  ? 228 GLY E N   1 
ATOM   9696  C CA  . GLY E 1 225 ? 38.291  9.731   46.289  1.00 61.39  ? 228 GLY E CA  1 
ATOM   9697  C C   . GLY E 1 225 ? 37.109  10.125  45.419  1.00 63.73  ? 228 GLY E C   1 
ATOM   9698  O O   . GLY E 1 225 ? 36.057  9.487   45.415  1.00 64.69  ? 228 GLY E O   1 
ATOM   9699  N N   . ARG E 1 226 ? 37.292  11.212  44.673  1.00 62.37  ? 229 ARG E N   1 
ATOM   9700  C CA  . ARG E 1 226 ? 36.262  11.719  43.779  1.00 55.84  ? 229 ARG E CA  1 
ATOM   9701  C C   . ARG E 1 226 ? 36.894  12.117  42.456  1.00 53.60  ? 229 ARG E C   1 
ATOM   9702  O O   . ARG E 1 226 ? 38.047  12.550  42.405  1.00 59.41  ? 229 ARG E O   1 
ATOM   9703  C CB  . ARG E 1 226 ? 35.522  12.928  44.370  1.00 49.45  ? 229 ARG E CB  1 
ATOM   9704  C CG  . ARG E 1 226 ? 34.782  12.643  45.658  1.00 49.97  ? 229 ARG E CG  1 
ATOM   9705  C CD  . ARG E 1 226 ? 33.536  11.808  45.409  1.00 57.77  ? 229 ARG E CD  1 
ATOM   9706  N NE  . ARG E 1 226 ? 32.833  11.541  46.656  1.00 56.14  ? 229 ARG E NE  1 
ATOM   9707  C CZ  . ARG E 1 226 ? 33.065  10.493  47.434  1.00 58.68  ? 229 ARG E CZ  1 
ATOM   9708  N NH1 . ARG E 1 226 ? 33.948  9.566   47.098  1.00 59.44  ? 229 ARG E NH1 1 
ATOM   9709  N NH2 . ARG E 1 226 ? 32.400  10.376  48.579  1.00 56.77  ? 229 ARG E NH2 1 
ATOM   9710  N N   . MET E 1 227 ? 36.118  11.983  41.387  1.00 49.22  ? 230 MET E N   1 
ATOM   9711  C CA  . MET E 1 227 ? 36.538  12.421  40.063  1.00 50.70  ? 230 MET E CA  1 
ATOM   9712  C C   . MET E 1 227 ? 35.481  13.368  39.506  1.00 60.40  ? 230 MET E C   1 
ATOM   9713  O O   . MET E 1 227 ? 34.341  12.960  39.258  1.00 57.33  ? 230 MET E O   1 
ATOM   9714  C CB  . MET E 1 227 ? 36.759  11.223  39.148  1.00 46.72  ? 230 MET E CB  1 
ATOM   9715  C CG  . MET E 1 227 ? 38.144  10.625  39.282  1.00 52.88  ? 230 MET E CG  1 
ATOM   9716  S SD  . MET E 1 227 ? 38.457  9.384   38.029  1.00 58.28  ? 230 MET E SD  1 
ATOM   9717  C CE  . MET E 1 227 ? 39.442  8.210   38.950  1.00 64.05  ? 230 MET E CE  1 
ATOM   9718  N N   . ASP E 1 228 ? 35.854  14.635  39.333  1.00 55.17  ? 231 ASP E N   1 
ATOM   9719  C CA  . ASP E 1 228 ? 34.971  15.645  38.762  1.00 47.39  ? 231 ASP E CA  1 
ATOM   9720  C C   . ASP E 1 228 ? 35.230  15.728  37.264  1.00 45.35  ? 231 ASP E C   1 
ATOM   9721  O O   . ASP E 1 228 ? 36.357  16.004  36.841  1.00 48.01  ? 231 ASP E O   1 
ATOM   9722  C CB  . ASP E 1 228 ? 35.201  17.006  39.419  1.00 47.30  ? 231 ASP E CB  1 
ATOM   9723  C CG  . ASP E 1 228 ? 34.500  17.134  40.758  1.00 59.72  ? 231 ASP E CG  1 
ATOM   9724  O OD1 . ASP E 1 228 ? 33.771  16.191  41.134  1.00 60.26  ? 231 ASP E OD1 1 
ATOM   9725  O OD2 . ASP E 1 228 ? 34.678  18.173  41.436  1.00 57.59  ? 231 ASP E OD2 1 
ATOM   9726  N N   . PHE E 1 229 ? 34.191  15.495  36.470  1.00 42.21  ? 232 PHE E N   1 
ATOM   9727  C CA  . PHE E 1 229 ? 34.294  15.498  35.020  1.00 49.08  ? 232 PHE E CA  1 
ATOM   9728  C C   . PHE E 1 229 ? 33.654  16.754  34.442  1.00 46.31  ? 232 PHE E C   1 
ATOM   9729  O O   . PHE E 1 229 ? 32.704  17.306  35.005  1.00 47.72  ? 232 PHE E O   1 
ATOM   9730  C CB  . PHE E 1 229 ? 33.636  14.252  34.418  1.00 54.04  ? 232 PHE E CB  1 
ATOM   9731  C CG  . PHE E 1 229 ? 34.458  13.015  34.569  1.00 52.35  ? 232 PHE E CG  1 
ATOM   9732  C CD1 . PHE E 1 229 ? 35.563  12.804  33.764  1.00 52.54  ? 232 PHE E CD1 1 
ATOM   9733  C CD2 . PHE E 1 229 ? 34.138  12.067  35.525  1.00 52.72  ? 232 PHE E CD2 1 
ATOM   9734  C CE1 . PHE E 1 229 ? 36.332  11.673  33.906  1.00 45.57  ? 232 PHE E CE1 1 
ATOM   9735  C CE2 . PHE E 1 229 ? 34.906  10.930  35.672  1.00 61.46  ? 232 PHE E CE2 1 
ATOM   9736  C CZ  . PHE E 1 229 ? 36.004  10.734  34.862  1.00 52.47  ? 232 PHE E CZ  1 
ATOM   9737  N N   . PHE E 1 230 ? 34.202  17.209  33.317  1.00 48.62  ? 233 PHE E N   1 
ATOM   9738  C CA  . PHE E 1 230 ? 33.737  18.411  32.644  1.00 45.58  ? 233 PHE E CA  1 
ATOM   9739  C C   . PHE E 1 230 ? 33.700  18.147  31.147  1.00 49.35  ? 233 PHE E C   1 
ATOM   9740  O O   . PHE E 1 230 ? 34.338  17.217  30.644  1.00 49.66  ? 233 PHE E O   1 
ATOM   9741  C CB  . PHE E 1 230 ? 34.635  19.619  32.943  1.00 40.63  ? 233 PHE E CB  1 
ATOM   9742  C CG  . PHE E 1 230 ? 34.658  20.020  34.390  1.00 49.48  ? 233 PHE E CG  1 
ATOM   9743  C CD1 . PHE E 1 230 ? 35.451  19.339  35.305  1.00 49.52  ? 233 PHE E CD1 1 
ATOM   9744  C CD2 . PHE E 1 230 ? 33.906  21.092  34.834  1.00 42.31  ? 233 PHE E CD2 1 
ATOM   9745  C CE1 . PHE E 1 230 ? 35.476  19.712  36.639  1.00 45.54  ? 233 PHE E CE1 1 
ATOM   9746  C CE2 . PHE E 1 230 ? 33.926  21.469  36.169  1.00 47.73  ? 233 PHE E CE2 1 
ATOM   9747  C CZ  . PHE E 1 230 ? 34.714  20.777  37.070  1.00 51.07  ? 233 PHE E CZ  1 
ATOM   9748  N N   . TRP E 1 231 ? 32.949  18.980  30.434  1.00 40.88  ? 234 TRP E N   1 
ATOM   9749  C CA  . TRP E 1 231 ? 32.779  18.795  29.003  1.00 46.22  ? 234 TRP E CA  1 
ATOM   9750  C C   . TRP E 1 231 ? 32.776  20.143  28.298  1.00 43.03  ? 234 TRP E C   1 
ATOM   9751  O O   . TRP E 1 231 ? 32.646  21.199  28.920  1.00 49.00  ? 234 TRP E O   1 
ATOM   9752  C CB  . TRP E 1 231 ? 31.489  18.027  28.689  1.00 55.31  ? 234 TRP E CB  1 
ATOM   9753  C CG  . TRP E 1 231 ? 30.248  18.703  29.174  1.00 44.06  ? 234 TRP E CG  1 
ATOM   9754  C CD1 . TRP E 1 231 ? 29.752  18.701  30.448  1.00 48.56  ? 234 TRP E CD1 1 
ATOM   9755  C CD2 . TRP E 1 231 ? 29.339  19.480  28.391  1.00 47.23  ? 234 TRP E CD2 1 
ATOM   9756  N NE1 . TRP E 1 231 ? 28.587  19.430  30.504  1.00 46.11  ? 234 TRP E NE1 1 
ATOM   9757  C CE2 . TRP E 1 231 ? 28.314  19.921  29.254  1.00 48.16  ? 234 TRP E CE2 1 
ATOM   9758  C CE3 . TRP E 1 231 ? 29.291  19.847  27.042  1.00 50.75  ? 234 TRP E CE3 1 
ATOM   9759  C CZ2 . TRP E 1 231 ? 27.255  20.710  28.810  1.00 51.73  ? 234 TRP E CZ2 1 
ATOM   9760  C CZ3 . TRP E 1 231 ? 28.240  20.628  26.605  1.00 51.35  ? 234 TRP E CZ3 1 
ATOM   9761  C CH2 . TRP E 1 231 ? 27.236  21.051  27.486  1.00 49.02  ? 234 TRP E CH2 1 
ATOM   9762  N N   . THR E 1 232 ? 32.943  20.086  26.981  1.00 39.00  ? 235 THR E N   1 
ATOM   9763  C CA  . THR E 1 232 ? 32.873  21.265  26.132  1.00 47.86  ? 235 THR E CA  1 
ATOM   9764  C C   . THR E 1 232 ? 32.491  20.815  24.732  1.00 48.10  ? 235 THR E C   1 
ATOM   9765  O O   . THR E 1 232 ? 32.545  19.627  24.408  1.00 46.08  ? 235 THR E O   1 
ATOM   9766  C CB  . THR E 1 232 ? 34.194  22.039  26.108  1.00 47.77  ? 235 THR E CB  1 
ATOM   9767  O OG1 . THR E 1 232 ? 33.955  23.381  25.661  1.00 59.83  ? 235 THR E OG1 1 
ATOM   9768  C CG2 . THR E 1 232 ? 35.176  21.380  25.160  1.00 40.82  ? 235 THR E CG2 1 
ATOM   9769  N N   . ILE E 1 233 ? 32.083  21.780  23.917  1.00 51.80  ? 236 ILE E N   1 
ATOM   9770  C CA  . ILE E 1 233 ? 31.763  21.555  22.512  1.00 53.91  ? 236 ILE E CA  1 
ATOM   9771  C C   . ILE E 1 233 ? 32.830  22.274  21.700  1.00 53.37  ? 236 ILE E C   1 
ATOM   9772  O O   . ILE E 1 233 ? 32.881  23.510  21.681  1.00 56.34  ? 236 ILE E O   1 
ATOM   9773  C CB  . ILE E 1 233 ? 30.356  22.056  22.157  1.00 53.10  ? 236 ILE E CB  1 
ATOM   9774  C CG1 . ILE E 1 233 ? 29.312  21.389  23.051  1.00 42.07  ? 236 ILE E CG1 1 
ATOM   9775  C CG2 . ILE E 1 233 ? 30.043  21.798  20.687  1.00 53.17  ? 236 ILE E CG2 1 
ATOM   9776  C CD1 . ILE E 1 233 ? 29.090  19.932  22.734  1.00 48.22  ? 236 ILE E CD1 1 
ATOM   9777  N N   . LEU E 1 234 ? 33.687  21.508  21.034  1.00 54.42  ? 237 LEU E N   1 
ATOM   9778  C CA  . LEU E 1 234 ? 34.798  22.071  20.273  1.00 54.42  ? 237 LEU E CA  1 
ATOM   9779  C C   . LEU E 1 234 ? 34.363  22.234  18.821  1.00 64.15  ? 237 LEU E C   1 
ATOM   9780  O O   . LEU E 1 234 ? 34.116  21.244  18.124  1.00 61.54  ? 237 LEU E O   1 
ATOM   9781  C CB  . LEU E 1 234 ? 36.031  21.181  20.385  1.00 55.77  ? 237 LEU E CB  1 
ATOM   9782  C CG  . LEU E 1 234 ? 37.348  21.770  19.879  1.00 48.04  ? 237 LEU E CG  1 
ATOM   9783  C CD1 . LEU E 1 234 ? 37.853  22.868  20.800  1.00 51.83  ? 237 LEU E CD1 1 
ATOM   9784  C CD2 . LEU E 1 234 ? 38.375  20.676  19.731  1.00 46.48  ? 237 LEU E CD2 1 
ATOM   9785  N N   . LYS E 1 235 ? 34.272  23.485  18.368  1.00 62.59  ? 238 LYS E N   1 
ATOM   9786  C CA  . LYS E 1 235 ? 33.833  23.780  17.015  1.00 58.54  ? 238 LYS E CA  1 
ATOM   9787  C C   . LYS E 1 235 ? 34.880  23.309  16.006  1.00 61.05  ? 238 LYS E C   1 
ATOM   9788  O O   . LYS E 1 235 ? 36.049  23.121  16.352  1.00 51.86  ? 238 LYS E O   1 
ATOM   9789  C CB  . LYS E 1 235 ? 33.577  25.279  16.859  1.00 66.26  ? 238 LYS E CB  1 
ATOM   9790  C CG  . LYS E 1 235 ? 32.542  25.842  17.827  1.00 65.27  ? 238 LYS E CG  1 
ATOM   9791  C CD  . LYS E 1 235 ? 31.118  25.580  17.344  1.00 72.10  ? 238 LYS E CD  1 
ATOM   9792  C CE  . LYS E 1 235 ? 30.295  26.865  17.292  1.00 87.60  ? 238 LYS E CE  1 
ATOM   9793  N NZ  . LYS E 1 235 ? 29.181  26.787  16.300  1.00 80.70  ? 238 LYS E NZ  1 
ATOM   9794  N N   . PRO E 1 236 ? 34.478  23.080  14.754  1.00 63.07  ? 239 PRO E N   1 
ATOM   9795  C CA  . PRO E 1 236 ? 35.448  22.632  13.747  1.00 57.12  ? 239 PRO E CA  1 
ATOM   9796  C C   . PRO E 1 236 ? 36.571  23.642  13.562  1.00 60.30  ? 239 PRO E C   1 
ATOM   9797  O O   . PRO E 1 236 ? 36.362  24.854  13.634  1.00 61.13  ? 239 PRO E O   1 
ATOM   9798  C CB  . PRO E 1 236 ? 34.601  22.485  12.478  1.00 61.41  ? 239 PRO E CB  1 
ATOM   9799  C CG  . PRO E 1 236 ? 33.215  22.266  12.976  1.00 62.71  ? 239 PRO E CG  1 
ATOM   9800  C CD  . PRO E 1 236 ? 33.106  23.099  14.222  1.00 62.05  ? 239 PRO E CD  1 
ATOM   9801  N N   . ASN E 1 237 ? 37.774  23.118  13.336  1.00 67.37  ? 240 ASN E N   1 
ATOM   9802  C CA  . ASN E 1 237 ? 39.008  23.882  13.183  1.00 65.83  ? 240 ASN E CA  1 
ATOM   9803  C C   . ASN E 1 237 ? 39.419  24.610  14.456  1.00 59.03  ? 240 ASN E C   1 
ATOM   9804  O O   . ASN E 1 237 ? 40.384  25.382  14.435  1.00 57.55  ? 240 ASN E O   1 
ATOM   9805  C CB  . ASN E 1 237 ? 38.920  24.875  12.013  1.00 73.74  ? 240 ASN E CB  1 
ATOM   9806  C CG  . ASN E 1 237 ? 39.185  24.216  10.674  1.00 96.60  ? 240 ASN E CG  1 
ATOM   9807  O OD1 . ASN E 1 237 ? 38.748  23.089  10.422  1.00 90.84  ? 240 ASN E OD1 1 
ATOM   9808  N ND2 . ASN E 1 237 ? 39.923  24.908  9.813   1.00 99.87  ? 240 ASN E ND2 1 
ATOM   9809  N N   . ASP E 1 238 ? 38.725  24.382  15.565  1.00 57.17  ? 241 ASP E N   1 
ATOM   9810  C CA  . ASP E 1 238 ? 39.180  24.864  16.858  1.00 53.53  ? 241 ASP E CA  1 
ATOM   9811  C C   . ASP E 1 238 ? 40.030  23.796  17.533  1.00 58.63  ? 241 ASP E C   1 
ATOM   9812  O O   . ASP E 1 238 ? 39.949  22.608  17.213  1.00 55.09  ? 241 ASP E O   1 
ATOM   9813  C CB  . ASP E 1 238 ? 37.998  25.239  17.756  1.00 53.00  ? 241 ASP E CB  1 
ATOM   9814  C CG  . ASP E 1 238 ? 38.420  26.049  18.976  1.00 62.71  ? 241 ASP E CG  1 
ATOM   9815  O OD1 . ASP E 1 238 ? 39.531  26.626  18.962  1.00 63.39  ? 241 ASP E OD1 1 
ATOM   9816  O OD2 . ASP E 1 238 ? 37.642  26.106  19.954  1.00 54.88  ? 241 ASP E OD2 1 
ATOM   9817  N N   . ALA E 1 239 ? 40.861  24.236  18.476  1.00 51.53  ? 242 ALA E N   1 
ATOM   9818  C CA  . ALA E 1 239 ? 41.741  23.335  19.201  1.00 59.77  ? 242 ALA E CA  1 
ATOM   9819  C C   . ALA E 1 239 ? 41.538  23.503  20.699  1.00 56.37  ? 242 ALA E C   1 
ATOM   9820  O O   . ALA E 1 239 ? 41.313  24.615  21.186  1.00 55.67  ? 242 ALA E O   1 
ATOM   9821  C CB  . ALA E 1 239 ? 43.212  23.578  18.838  1.00 55.97  ? 242 ALA E CB  1 
ATOM   9822  N N   . ILE E 1 240 ? 41.613  22.390  21.422  1.00 49.41  ? 243 ILE E N   1 
ATOM   9823  C CA  . ILE E 1 240 ? 41.551  22.383  22.880  1.00 53.49  ? 243 ILE E CA  1 
ATOM   9824  C C   . ILE E 1 240 ? 42.964  22.181  23.405  1.00 51.04  ? 243 ILE E C   1 
ATOM   9825  O O   . ILE E 1 240 ? 43.752  21.428  22.821  1.00 50.79  ? 243 ILE E O   1 
ATOM   9826  C CB  . ILE E 1 240 ? 40.580  21.296  23.389  1.00 53.76  ? 243 ILE E CB  1 
ATOM   9827  C CG1 . ILE E 1 240 ? 40.421  21.358  24.911  1.00 53.52  ? 243 ILE E CG1 1 
ATOM   9828  C CG2 . ILE E 1 240 ? 41.015  19.904  22.935  1.00 50.21  ? 243 ILE E CG2 1 
ATOM   9829  C CD1 . ILE E 1 240 ? 39.107  20.767  25.400  1.00 44.76  ? 243 ILE E CD1 1 
ATOM   9830  N N   . HIS E 1 241 ? 43.304  22.882  24.485  1.00 53.58  ? 244 HIS E N   1 
ATOM   9831  C CA  . HIS E 1 241 ? 44.655  22.881  25.032  1.00 47.52  ? 244 HIS E CA  1 
ATOM   9832  C C   . HIS E 1 241 ? 44.624  22.413  26.478  1.00 50.36  ? 244 HIS E C   1 
ATOM   9833  O O   . HIS E 1 241 ? 43.904  22.984  27.303  1.00 54.80  ? 244 HIS E O   1 
ATOM   9834  C CB  . HIS E 1 241 ? 45.282  24.274  24.930  1.00 51.06  ? 244 HIS E CB  1 
ATOM   9835  C CG  . HIS E 1 241 ? 45.213  24.858  23.553  1.00 58.69  ? 244 HIS E CG  1 
ATOM   9836  N ND1 . HIS E 1 241 ? 46.321  24.994  22.745  1.00 59.50  ? 244 HIS E ND1 1 
ATOM   9837  C CD2 . HIS E 1 241 ? 44.163  25.320  22.833  1.00 56.37  ? 244 HIS E CD2 1 
ATOM   9838  C CE1 . HIS E 1 241 ? 45.958  25.526  21.591  1.00 64.33  ? 244 HIS E CE1 1 
ATOM   9839  N NE2 . HIS E 1 241 ? 44.653  25.730  21.617  1.00 56.75  ? 244 HIS E NE2 1 
ATOM   9840  N N   . PHE E 1 242 ? 45.415  21.386  26.781  1.00 53.29  ? 245 PHE E N   1 
ATOM   9841  C CA  . PHE E 1 242 ? 45.466  20.776  28.103  1.00 51.68  ? 245 PHE E CA  1 
ATOM   9842  C C   . PHE E 1 242 ? 46.836  21.007  28.727  1.00 56.57  ? 245 PHE E C   1 
ATOM   9843  O O   . PHE E 1 242 ? 47.865  20.725  28.101  1.00 54.60  ? 245 PHE E O   1 
ATOM   9844  C CB  . PHE E 1 242 ? 45.186  19.271  28.031  1.00 52.45  ? 245 PHE E CB  1 
ATOM   9845  C CG  . PHE E 1 242 ? 43.776  18.923  27.647  1.00 56.83  ? 245 PHE E CG  1 
ATOM   9846  C CD1 . PHE E 1 242 ? 42.727  19.133  28.530  1.00 61.98  ? 245 PHE E CD1 1 
ATOM   9847  C CD2 . PHE E 1 242 ? 43.500  18.367  26.408  1.00 48.55  ? 245 PHE E CD2 1 
ATOM   9848  C CE1 . PHE E 1 242 ? 41.426  18.800  28.178  1.00 53.49  ? 245 PHE E CE1 1 
ATOM   9849  C CE2 . PHE E 1 242 ? 42.208  18.033  26.049  1.00 47.55  ? 245 PHE E CE2 1 
ATOM   9850  C CZ  . PHE E 1 242 ? 41.167  18.250  26.936  1.00 53.86  ? 245 PHE E CZ  1 
ATOM   9851  N N   . GLU E 1 243 ? 46.845  21.511  29.958  1.00 57.33  ? 246 GLU E N   1 
ATOM   9852  C CA  . GLU E 1 243 ? 48.057  21.622  30.757  1.00 58.42  ? 246 GLU E CA  1 
ATOM   9853  C C   . GLU E 1 243 ? 47.772  21.056  32.138  1.00 56.47  ? 246 GLU E C   1 
ATOM   9854  O O   . GLU E 1 243 ? 46.813  21.473  32.796  1.00 59.73  ? 246 GLU E O   1 
ATOM   9855  C CB  . GLU E 1 243 ? 48.540  23.074  30.861  1.00 63.46  ? 246 GLU E CB  1 
ATOM   9856  C CG  . GLU E 1 243 ? 49.947  23.238  31.423  1.00 66.92  ? 246 GLU E CG  1 
ATOM   9857  C CD  . GLU E 1 243 ? 50.385  24.695  31.482  1.00 83.36  ? 246 GLU E CD  1 
ATOM   9858  O OE1 . GLU E 1 243 ? 50.361  25.369  30.429  1.00 85.84  ? 246 GLU E OE1 1 
ATOM   9859  O OE2 . GLU E 1 243 ? 50.754  25.168  32.579  1.00 80.85  ? 246 GLU E OE2 1 
ATOM   9860  N N   . SER E 1 244 ? 48.598  20.109  32.573  1.00 57.11  ? 247 SER E N   1 
ATOM   9861  C CA  . SER E 1 244 ? 48.400  19.476  33.867  1.00 61.11  ? 247 SER E CA  1 
ATOM   9862  C C   . SER E 1 244 ? 49.714  18.879  34.346  1.00 62.66  ? 247 SER E C   1 
ATOM   9863  O O   . SER E 1 244 ? 50.502  18.370  33.544  1.00 57.67  ? 247 SER E O   1 
ATOM   9864  C CB  . SER E 1 244 ? 47.326  18.386  33.795  1.00 49.46  ? 247 SER E CB  1 
ATOM   9865  O OG  . SER E 1 244 ? 47.214  17.715  35.035  1.00 44.59  ? 247 SER E OG  1 
ATOM   9866  N N   . ASN E 1 245 ? 49.933  18.936  35.658  1.00 53.39  ? 248 ASN E N   1 
ATOM   9867  C CA  . ASN E 1 245 ? 51.066  18.284  36.300  1.00 55.02  ? 248 ASN E CA  1 
ATOM   9868  C C   . ASN E 1 245 ? 50.595  17.270  37.338  1.00 62.67  ? 248 ASN E C   1 
ATOM   9869  O O   . ASN E 1 245 ? 51.291  17.013  38.322  1.00 63.51  ? 248 ASN E O   1 
ATOM   9870  C CB  . ASN E 1 245 ? 51.999  19.312  36.937  1.00 46.64  ? 248 ASN E CB  1 
ATOM   9871  C CG  . ASN E 1 245 ? 51.372  20.001  38.126  1.00 56.00  ? 248 ASN E CG  1 
ATOM   9872  O OD1 . ASN E 1 245 ? 50.148  20.066  38.240  1.00 55.35  ? 248 ASN E OD1 1 
ATOM   9873  N ND2 . ASN E 1 245 ? 52.206  20.515  39.025  1.00 48.11  ? 248 ASN E ND2 1 
ATOM   9874  N N   . GLY E 1 246 ? 49.414  16.705  37.141  1.00 61.11  ? 249 GLY E N   1 
ATOM   9875  C CA  . GLY E 1 246 ? 48.893  15.671  38.015  1.00 57.93  ? 249 GLY E CA  1 
ATOM   9876  C C   . GLY E 1 246 ? 47.381  15.717  38.105  1.00 64.32  ? 249 GLY E C   1 
ATOM   9877  O O   . GLY E 1 246 ? 46.738  16.730  37.834  1.00 60.46  ? 249 GLY E O   1 
ATOM   9878  N N   . ASN E 1 247 ? 46.805  14.576  38.495  1.00 55.85  ? 250 ASN E N   1 
ATOM   9879  C CA  . ASN E 1 247 ? 45.370  14.409  38.740  1.00 55.59  ? 250 ASN E CA  1 
ATOM   9880  C C   . ASN E 1 247 ? 44.523  14.625  37.491  1.00 56.42  ? 250 ASN E C   1 
ATOM   9881  O O   . ASN E 1 247 ? 43.325  14.899  37.594  1.00 53.84  ? 250 ASN E O   1 
ATOM   9882  C CB  . ASN E 1 247 ? 44.883  15.335  39.859  1.00 47.28  ? 250 ASN E CB  1 
ATOM   9883  C CG  . ASN E 1 247 ? 45.722  15.222  41.102  1.00 49.62  ? 250 ASN E CG  1 
ATOM   9884  O OD1 . ASN E 1 247 ? 46.900  15.567  41.095  1.00 52.01  ? 250 ASN E OD1 1 
ATOM   9885  N ND2 . ASN E 1 247 ? 45.127  14.723  42.176  1.00 51.26  ? 250 ASN E ND2 1 
ATOM   9886  N N   . PHE E 1 248 ? 45.115  14.487  36.310  1.00 57.25  ? 251 PHE E N   1 
ATOM   9887  C CA  . PHE E 1 248 ? 44.403  14.699  35.058  1.00 41.00  ? 251 PHE E CA  1 
ATOM   9888  C C   . PHE E 1 248 ? 43.752  13.400  34.598  1.00 50.74  ? 251 PHE E C   1 
ATOM   9889  O O   . PHE E 1 248 ? 44.409  12.355  34.535  1.00 51.28  ? 251 PHE E O   1 
ATOM   9890  C CB  . PHE E 1 248 ? 45.366  15.217  33.988  1.00 42.00  ? 251 PHE E CB  1 
ATOM   9891  C CG  . PHE E 1 248 ? 44.703  15.590  32.695  1.00 48.52  ? 251 PHE E CG  1 
ATOM   9892  C CD1 . PHE E 1 248 ? 43.417  16.103  32.682  1.00 56.02  ? 251 PHE E CD1 1 
ATOM   9893  C CD2 . PHE E 1 248 ? 45.368  15.428  31.489  1.00 43.75  ? 251 PHE E CD2 1 
ATOM   9894  C CE1 . PHE E 1 248 ? 42.805  16.449  31.490  1.00 51.38  ? 251 PHE E CE1 1 
ATOM   9895  C CE2 . PHE E 1 248 ? 44.765  15.774  30.298  1.00 50.87  ? 251 PHE E CE2 1 
ATOM   9896  C CZ  . PHE E 1 248 ? 43.481  16.286  30.297  1.00 48.85  ? 251 PHE E CZ  1 
ATOM   9897  N N   . ILE E 1 249 ? 42.464  13.468  34.283  1.00 49.45  ? 252 ILE E N   1 
ATOM   9898  C CA  . ILE E 1 249 ? 41.756  12.366  33.638  1.00 44.27  ? 252 ILE E CA  1 
ATOM   9899  C C   . ILE E 1 249 ? 41.598  12.781  32.179  1.00 54.40  ? 252 ILE E C   1 
ATOM   9900  O O   . ILE E 1 249 ? 40.669  13.508  31.813  1.00 61.61  ? 252 ILE E O   1 
ATOM   9901  C CB  . ILE E 1 249 ? 40.418  12.068  34.315  1.00 50.95  ? 252 ILE E CB  1 
ATOM   9902  C CG1 . ILE E 1 249 ? 40.564  12.190  35.830  1.00 50.17  ? 252 ILE E CG1 1 
ATOM   9903  C CG2 . ILE E 1 249 ? 39.907  10.680  33.918  1.00 44.48  ? 252 ILE E CG2 1 
ATOM   9904  C CD1 . ILE E 1 249 ? 41.498  11.161  36.428  1.00 51.74  ? 252 ILE E CD1 1 
ATOM   9905  N N   . ALA E 1 250 ? 42.531  12.328  31.339  1.00 42.50  ? 253 ALA E N   1 
ATOM   9906  C CA  . ALA E 1 250 ? 42.620  12.816  29.974  1.00 49.20  ? 253 ALA E CA  1 
ATOM   9907  C C   . ALA E 1 250 ? 41.537  12.200  29.091  1.00 51.28  ? 253 ALA E C   1 
ATOM   9908  O O   . ALA E 1 250 ? 41.089  11.077  29.334  1.00 59.31  ? 253 ALA E O   1 
ATOM   9909  C CB  . ALA E 1 250 ? 43.994  12.509  29.386  1.00 43.82  ? 253 ALA E CB  1 
ATOM   9910  N N   . PRO E 1 251 ? 41.103  12.919  28.058  1.00 45.33  ? 254 PRO E N   1 
ATOM   9911  C CA  . PRO E 1 251 ? 40.196  12.317  27.076  1.00 42.35  ? 254 PRO E CA  1 
ATOM   9912  C C   . PRO E 1 251 ? 40.939  11.351  26.171  1.00 49.13  ? 254 PRO E C   1 
ATOM   9913  O O   . PRO E 1 251 ? 42.096  11.574  25.810  1.00 48.75  ? 254 PRO E O   1 
ATOM   9914  C CB  . PRO E 1 251 ? 39.670  13.519  26.281  1.00 45.12  ? 254 PRO E CB  1 
ATOM   9915  C CG  . PRO E 1 251 ? 40.253  14.747  26.932  1.00 54.94  ? 254 PRO E CG  1 
ATOM   9916  C CD  . PRO E 1 251 ? 41.434  14.312  27.726  1.00 39.84  ? 254 PRO E CD  1 
ATOM   9917  N N   . GLU E 1 252 ? 40.260  10.267  25.809  1.00 54.81  ? 255 GLU E N   1 
ATOM   9918  C CA  . GLU E 1 252 ? 40.738  9.339   24.793  1.00 46.70  ? 255 GLU E CA  1 
ATOM   9919  C C   . GLU E 1 252 ? 39.800  9.279   23.599  1.00 55.66  ? 255 GLU E C   1 
ATOM   9920  O O   . GLU E 1 252 ? 40.240  9.457   22.457  1.00 56.78  ? 255 GLU E O   1 
ATOM   9921  C CB  . GLU E 1 252 ? 40.916  7.936   25.398  1.00 52.57  ? 255 GLU E CB  1 
ATOM   9922  C CG  . GLU E 1 252 ? 41.428  6.885   24.415  1.00 57.91  ? 255 GLU E CG  1 
ATOM   9923  C CD  . GLU E 1 252 ? 41.615  5.517   25.060  1.00 74.30  ? 255 GLU E CD  1 
ATOM   9924  O OE1 . GLU E 1 252 ? 41.188  5.334   26.222  1.00 67.31  ? 255 GLU E OE1 1 
ATOM   9925  O OE2 . GLU E 1 252 ? 42.191  4.622   24.403  1.00 73.48  ? 255 GLU E OE2 1 
ATOM   9926  N N   . TYR E 1 253 ? 38.513  9.050   23.832  1.00 47.29  ? 256 TYR E N   1 
ATOM   9927  C CA  . TYR E 1 253 ? 37.505  9.062   22.786  1.00 61.82  ? 256 TYR E CA  1 
ATOM   9928  C C   . TYR E 1 253 ? 36.636  10.304  22.930  1.00 58.57  ? 256 TYR E C   1 
ATOM   9929  O O   . TYR E 1 253 ? 36.373  10.764  24.047  1.00 47.53  ? 256 TYR E O   1 
ATOM   9930  C CB  . TYR E 1 253 ? 36.632  7.800   22.841  1.00 58.33  ? 256 TYR E CB  1 
ATOM   9931  C CG  . TYR E 1 253 ? 37.354  6.534   22.438  1.00 60.34  ? 256 TYR E CG  1 
ATOM   9932  C CD1 . TYR E 1 253 ? 37.973  5.734   23.388  1.00 69.80  ? 256 TYR E CD1 1 
ATOM   9933  C CD2 . TYR E 1 253 ? 37.419  6.140   21.107  1.00 67.26  ? 256 TYR E CD2 1 
ATOM   9934  C CE1 . TYR E 1 253 ? 38.638  4.574   23.025  1.00 71.17  ? 256 TYR E CE1 1 
ATOM   9935  C CE2 . TYR E 1 253 ? 38.081  4.982   20.734  1.00 68.23  ? 256 TYR E CE2 1 
ATOM   9936  C CZ  . TYR E 1 253 ? 38.689  4.205   21.698  1.00 71.51  ? 256 TYR E CZ  1 
ATOM   9937  O OH  . TYR E 1 253 ? 39.348  3.053   21.333  1.00 87.48  ? 256 TYR E OH  1 
ATOM   9938  N N   . ALA E 1 254 ? 36.217  10.857  21.799  1.00 58.79  ? 257 ALA E N   1 
ATOM   9939  C CA  . ALA E 1 254 ? 35.288  11.976  21.745  1.00 44.10  ? 257 ALA E CA  1 
ATOM   9940  C C   . ALA E 1 254 ? 34.107  11.590  20.862  1.00 49.94  ? 257 ALA E C   1 
ATOM   9941  O O   . ALA E 1 254 ? 34.009  10.462  20.373  1.00 61.13  ? 257 ALA E O   1 
ATOM   9942  C CB  . ALA E 1 254 ? 35.979  13.242  21.232  1.00 42.12  ? 257 ALA E CB  1 
ATOM   9943  N N   . TYR E 1 255 ? 33.196  12.537  20.658  1.00 53.81  ? 258 TYR E N   1 
ATOM   9944  C CA  . TYR E 1 255 ? 31.985  12.280  19.889  1.00 53.49  ? 258 TYR E CA  1 
ATOM   9945  C C   . TYR E 1 255 ? 31.784  13.394  18.878  1.00 52.57  ? 258 TYR E C   1 
ATOM   9946  O O   . TYR E 1 255 ? 31.698  14.568  19.255  1.00 57.52  ? 258 TYR E O   1 
ATOM   9947  C CB  . TYR E 1 255 ? 30.763  12.171  20.804  1.00 52.31  ? 258 TYR E CB  1 
ATOM   9948  C CG  . TYR E 1 255 ? 30.858  11.085  21.851  1.00 47.81  ? 258 TYR E CG  1 
ATOM   9949  C CD1 . TYR E 1 255 ? 30.610  9.757   21.528  1.00 44.19  ? 258 TYR E CD1 1 
ATOM   9950  C CD2 . TYR E 1 255 ? 31.194  11.390  23.162  1.00 42.33  ? 258 TYR E CD2 1 
ATOM   9951  C CE1 . TYR E 1 255 ? 30.689  8.765   22.486  1.00 45.63  ? 258 TYR E CE1 1 
ATOM   9952  C CE2 . TYR E 1 255 ? 31.275  10.405  24.125  1.00 48.79  ? 258 TYR E CE2 1 
ATOM   9953  C CZ  . TYR E 1 255 ? 31.024  9.095   23.782  1.00 46.47  ? 258 TYR E CZ  1 
ATOM   9954  O OH  . TYR E 1 255 ? 31.109  8.116   24.744  1.00 54.35  ? 258 TYR E OH  1 
ATOM   9955  N N   . LYS E 1 256 ? 31.722  13.030  17.600  1.00 55.20  ? 259 LYS E N   1 
ATOM   9956  C CA  . LYS E 1 256 ? 31.197  13.942  16.594  1.00 56.81  ? 259 LYS E CA  1 
ATOM   9957  C C   . LYS E 1 256 ? 29.703  14.112  16.827  1.00 56.93  ? 259 LYS E C   1 
ATOM   9958  O O   . LYS E 1 256 ? 28.979  13.126  16.998  1.00 62.52  ? 259 LYS E O   1 
ATOM   9959  C CB  . LYS E 1 256 ? 31.455  13.405  15.188  1.00 62.88  ? 259 LYS E CB  1 
ATOM   9960  C CG  . LYS E 1 256 ? 32.908  13.087  14.880  1.00 66.97  ? 259 LYS E CG  1 
ATOM   9961  C CD  . LYS E 1 256 ? 33.009  11.941  13.878  1.00 73.31  ? 259 LYS E CD  1 
ATOM   9962  C CE  . LYS E 1 256 ? 33.479  12.426  12.516  1.00 73.16  ? 259 LYS E CE  1 
ATOM   9963  N NZ  . LYS E 1 256 ? 34.967  12.504  12.434  1.00 84.14  ? 259 LYS E NZ  1 
ATOM   9964  N N   . ILE E 1 257 ? 29.239  15.357  16.845  1.00 53.12  ? 260 ILE E N   1 
ATOM   9965  C CA  . ILE E 1 257 ? 27.858  15.655  17.204  1.00 58.45  ? 260 ILE E CA  1 
ATOM   9966  C C   . ILE E 1 257 ? 27.283  16.666  16.219  1.00 59.84  ? 260 ILE E C   1 
ATOM   9967  O O   . ILE E 1 257 ? 27.950  17.633  15.835  1.00 58.14  ? 260 ILE E O   1 
ATOM   9968  C CB  . ILE E 1 257 ? 27.764  16.151  18.664  1.00 62.10  ? 260 ILE E CB  1 
ATOM   9969  C CG1 . ILE E 1 257 ? 26.310  16.238  19.121  1.00 64.18  ? 260 ILE E CG1 1 
ATOM   9970  C CG2 . ILE E 1 257 ? 28.478  17.485  18.846  1.00 61.97  ? 260 ILE E CG2 1 
ATOM   9971  C CD1 . ILE E 1 257 ? 26.154  16.849  20.495  1.00 71.00  ? 260 ILE E CD1 1 
ATOM   9972  N N   . VAL E 1 258 A 26.054  16.411  15.776  1.00 55.65  ? 260 VAL E N   1 
ATOM   9973  C CA  . VAL E 1 258 A 25.294  17.333  14.939  1.00 55.21  ? 260 VAL E CA  1 
ATOM   9974  C C   . VAL E 1 258 A 23.892  17.436  15.525  1.00 57.76  ? 260 VAL E C   1 
ATOM   9975  O O   . VAL E 1 258 A 23.188  16.426  15.636  1.00 57.45  ? 260 VAL E O   1 
ATOM   9976  C CB  . VAL E 1 258 A 25.235  16.871  13.473  1.00 64.38  ? 260 VAL E CB  1 
ATOM   9977  C CG1 . VAL E 1 258 A 24.240  17.725  12.683  1.00 56.36  ? 260 VAL E CG1 1 
ATOM   9978  C CG2 . VAL E 1 258 A 26.620  16.919  12.843  1.00 53.64  ? 260 VAL E CG2 1 
ATOM   9979  N N   . LYS E 1 259 ? 23.483  18.649  15.889  1.00 62.84  ? 261 LYS E N   1 
ATOM   9980  C CA  . LYS E 1 259 ? 22.181  18.884  16.496  1.00 62.57  ? 261 LYS E CA  1 
ATOM   9981  C C   . LYS E 1 259 ? 21.339  19.766  15.586  1.00 56.68  ? 261 LYS E C   1 
ATOM   9982  O O   . LYS E 1 259 ? 21.787  20.837  15.165  1.00 62.76  ? 261 LYS E O   1 
ATOM   9983  C CB  . LYS E 1 259 ? 22.321  19.529  17.878  1.00 56.93  ? 261 LYS E CB  1 
ATOM   9984  C CG  . LYS E 1 259 ? 21.032  19.499  18.688  1.00 63.12  ? 261 LYS E CG  1 
ATOM   9985  C CD  . LYS E 1 259 ? 21.242  20.049  20.085  1.00 57.12  ? 261 LYS E CD  1 
ATOM   9986  C CE  . LYS E 1 259 ? 19.948  20.043  20.881  1.00 51.20  ? 261 LYS E CE  1 
ATOM   9987  N NZ  . LYS E 1 259 ? 19.421  18.668  21.083  1.00 59.70  ? 261 LYS E NZ  1 
ATOM   9988  N N   . LYS E 1 260 ? 20.119  19.309  15.288  1.00 65.37  ? 262 LYS E N   1 
ATOM   9989  C CA  . LYS E 1 260 ? 19.176  20.060  14.473  1.00 51.96  ? 262 LYS E CA  1 
ATOM   9990  C C   . LYS E 1 260 ? 17.817  20.234  15.135  1.00 58.31  ? 262 LYS E C   1 
ATOM   9991  O O   . LYS E 1 260 ? 16.962  20.933  14.579  1.00 68.16  ? 262 LYS E O   1 
ATOM   9992  C CB  . LYS E 1 260 ? 18.983  19.382  13.106  1.00 57.38  ? 262 LYS E CB  1 
ATOM   9993  C CG  . LYS E 1 260 ? 20.239  19.338  12.248  1.00 63.25  ? 262 LYS E CG  1 
ATOM   9994  C CD  . LYS E 1 260 ? 19.961  18.720  10.885  1.00 74.57  ? 262 LYS E CD  1 
ATOM   9995  C CE  . LYS E 1 260 ? 21.189  18.785  9.981   1.00 77.68  ? 262 LYS E CE  1 
ATOM   9996  N NZ  . LYS E 1 260 ? 21.980  20.033  10.184  1.00 73.17  ? 262 LYS E NZ  1 
ATOM   9997  N N   . GLY E 1 261 ? 17.591  19.625  16.296  1.00 67.16  ? 263 GLY E N   1 
ATOM   9998  C CA  . GLY E 1 261 ? 16.310  19.705  16.969  1.00 60.07  ? 263 GLY E CA  1 
ATOM   9999  C C   . GLY E 1 261 ? 16.481  19.420  18.444  1.00 58.48  ? 263 GLY E C   1 
ATOM   10000 O O   . GLY E 1 261 ? 17.567  19.068  18.911  1.00 55.16  ? 263 GLY E O   1 
ATOM   10001 N N   . ASP E 1 262 ? 15.386  19.569  19.182  1.00 62.06  ? 264 ASP E N   1 
ATOM   10002 C CA  . ASP E 1 262 ? 15.431  19.442  20.628  1.00 56.02  ? 264 ASP E CA  1 
ATOM   10003 C C   . ASP E 1 262 ? 14.332  18.516  21.119  1.00 56.09  ? 264 ASP E C   1 
ATOM   10004 O O   . ASP E 1 262 ? 13.278  18.378  20.493  1.00 63.27  ? 264 ASP E O   1 
ATOM   10005 C CB  . ASP E 1 262 ? 15.317  20.804  21.308  1.00 56.86  ? 264 ASP E CB  1 
ATOM   10006 C CG  . ASP E 1 262 ? 16.669  21.353  21.726  1.00 80.33  ? 264 ASP E CG  1 
ATOM   10007 O OD1 . ASP E 1 262 ? 17.314  20.749  22.615  1.00 66.80  ? 264 ASP E OD1 1 
ATOM   10008 O OD2 . ASP E 1 262 ? 17.091  22.382  21.157  1.00 84.38  ? 264 ASP E OD2 1 
ATOM   10009 N N   . SER E 1 263 ? 14.607  17.873  22.245  1.00 55.75  ? 265 SER E N   1 
ATOM   10010 C CA  . SER E 1 263 ? 13.711  16.907  22.860  1.00 48.07  ? 265 SER E CA  1 
ATOM   10011 C C   . SER E 1 263 ? 13.956  16.964  24.365  1.00 46.54  ? 265 SER E C   1 
ATOM   10012 O O   . SER E 1 263 ? 14.476  17.959  24.881  1.00 51.48  ? 265 SER E O   1 
ATOM   10013 C CB  . SER E 1 263 ? 13.932  15.513  22.247  1.00 53.70  ? 265 SER E CB  1 
ATOM   10014 O OG  . SER E 1 263 ? 13.389  14.503  23.072  1.00 59.16  ? 265 SER E OG  1 
ATOM   10015 N N   . THR E 1 264 ? 13.568  15.911  25.080  1.00 45.39  ? 266 THR E N   1 
ATOM   10016 C CA  . THR E 1 264 ? 13.851  15.826  26.508  1.00 55.70  ? 266 THR E CA  1 
ATOM   10017 C C   . THR E 1 264 ? 14.259  14.393  26.841  1.00 46.90  ? 266 THR E C   1 
ATOM   10018 O O   . THR E 1 264 ? 14.470  13.561  25.953  1.00 44.68  ? 266 THR E O   1 
ATOM   10019 C CB  . THR E 1 264 ? 12.644  16.295  27.332  1.00 57.03  ? 266 THR E CB  1 
ATOM   10020 O OG1 . THR E 1 264 ? 13.025  16.435  28.707  1.00 53.46  ? 266 THR E OG1 1 
ATOM   10021 C CG2 . THR E 1 264 ? 11.510  15.298  27.223  1.00 52.27  ? 266 THR E CG2 1 
ATOM   10022 N N   . ILE E 1 265 ? 14.385  14.112  28.138  1.00 44.91  ? 267 ILE E N   1 
ATOM   10023 C CA  . ILE E 1 265 ? 14.698  12.781  28.647  1.00 40.85  ? 267 ILE E CA  1 
ATOM   10024 C C   . ILE E 1 265 ? 13.419  12.164  29.192  1.00 51.19  ? 267 ILE E C   1 
ATOM   10025 O O   . ILE E 1 265 ? 12.737  12.771  30.029  1.00 56.78  ? 267 ILE E O   1 
ATOM   10026 C CB  . ILE E 1 265 ? 15.778  12.841  29.742  1.00 50.67  ? 267 ILE E CB  1 
ATOM   10027 C CG1 . ILE E 1 265 ? 17.016  13.593  29.244  1.00 47.15  ? 267 ILE E CG1 1 
ATOM   10028 C CG2 . ILE E 1 265 ? 16.127  11.440  30.225  1.00 55.95  ? 267 ILE E CG2 1 
ATOM   10029 C CD1 . ILE E 1 265 ? 17.892  12.779  28.326  1.00 42.35  ? 267 ILE E CD1 1 
ATOM   10030 N N   . MET E 1 266 ? 13.094  10.960  28.730  1.00 53.11  ? 268 MET E N   1 
ATOM   10031 C CA  . MET E 1 266 ? 11.896  10.255  29.166  1.00 42.46  ? 268 MET E CA  1 
ATOM   10032 C C   . MET E 1 266 ? 12.257  9.193   30.195  1.00 49.77  ? 268 MET E C   1 
ATOM   10033 O O   . MET E 1 266 ? 13.110  8.336   29.939  1.00 60.49  ? 268 MET E O   1 
ATOM   10034 C CB  . MET E 1 266 ? 11.179  9.602   27.986  1.00 38.73  ? 268 MET E CB  1 
ATOM   10035 C CG  . MET E 1 266 ? 10.004  8.734   28.415  1.00 45.77  ? 268 MET E CG  1 
ATOM   10036 S SD  . MET E 1 266 ? 9.053   8.109   27.025  1.00 60.05  ? 268 MET E SD  1 
ATOM   10037 C CE  . MET E 1 266 ? 8.026   9.528   26.651  1.00 49.08  ? 268 MET E CE  1 
ATOM   10038 N N   . LYS E 1 267 ? 11.607  9.252   31.353  1.00 42.65  ? 269 LYS E N   1 
ATOM   10039 C CA  . LYS E 1 267 ? 11.805  8.266   32.409  1.00 51.39  ? 269 LYS E CA  1 
ATOM   10040 C C   . LYS E 1 267 ? 10.777  7.156   32.226  1.00 54.08  ? 269 LYS E C   1 
ATOM   10041 O O   . LYS E 1 267 ? 9.575   7.379   32.395  1.00 62.53  ? 269 LYS E O   1 
ATOM   10042 C CB  . LYS E 1 267 ? 11.683  8.913   33.786  1.00 45.03  ? 269 LYS E CB  1 
ATOM   10043 C CG  . LYS E 1 267 ? 12.682  10.029  34.039  1.00 48.19  ? 269 LYS E CG  1 
ATOM   10044 C CD  . LYS E 1 267 ? 14.113  9.530   33.900  1.00 71.56  ? 269 LYS E CD  1 
ATOM   10045 C CE  . LYS E 1 267 ? 15.036  10.169  34.933  1.00 66.52  ? 269 LYS E CE  1 
ATOM   10046 N NZ  . LYS E 1 267 ? 16.131  9.236   35.339  1.00 62.10  ? 269 LYS E NZ  1 
ATOM   10047 N N   . SER E 1 268 ? 11.250  5.963   31.876  1.00 56.60  ? 270 SER E N   1 
ATOM   10048 C CA  . SER E 1 268 ? 10.366  4.829   31.662  1.00 61.88  ? 270 SER E CA  1 
ATOM   10049 C C   . SER E 1 268 ? 11.170  3.546   31.796  1.00 67.13  ? 270 SER E C   1 
ATOM   10050 O O   . SER E 1 268 ? 12.370  3.519   31.505  1.00 62.62  ? 270 SER E O   1 
ATOM   10051 C CB  . SER E 1 268 ? 9.694   4.891   30.287  1.00 58.57  ? 270 SER E CB  1 
ATOM   10052 O OG  . SER E 1 268 ? 9.357   3.591   29.837  1.00 57.37  ? 270 SER E OG  1 
ATOM   10053 N N   . GLU E 1 269 ? 10.492  2.486   32.229  1.00 63.08  ? 271 GLU E N   1 
ATOM   10054 C CA  . GLU E 1 269 ? 11.111  1.181   32.412  1.00 72.53  ? 271 GLU E CA  1 
ATOM   10055 C C   . GLU E 1 269 ? 10.821  0.219   31.270  1.00 73.35  ? 271 GLU E C   1 
ATOM   10056 O O   . GLU E 1 269 ? 11.218  -0.946  31.347  1.00 79.48  ? 271 GLU E O   1 
ATOM   10057 C CB  . GLU E 1 269 ? 10.648  0.559   33.736  1.00 64.25  ? 271 GLU E CB  1 
ATOM   10058 C CG  . GLU E 1 269 ? 10.641  1.532   34.904  1.00 79.57  ? 271 GLU E CG  1 
ATOM   10059 C CD  . GLU E 1 269 ? 12.042  1.921   35.340  1.00 85.84  ? 271 GLU E CD  1 
ATOM   10060 O OE1 . GLU E 1 269 ? 12.865  1.014   35.587  1.00 77.53  ? 271 GLU E OE1 1 
ATOM   10061 O OE2 . GLU E 1 269 ? 12.325  3.136   35.425  1.00 80.10  ? 271 GLU E OE2 1 
ATOM   10062 N N   . MET E 1 270 ? 10.149  0.672   30.216  1.00 69.31  ? 272 MET E N   1 
ATOM   10063 C CA  . MET E 1 270 ? 9.729   -0.208  29.139  1.00 69.45  ? 272 MET E CA  1 
ATOM   10064 C C   . MET E 1 270 ? 10.848  -0.383  28.115  1.00 72.72  ? 272 MET E C   1 
ATOM   10065 O O   . MET E 1 270 ? 11.920  0.219   28.212  1.00 59.39  ? 272 MET E O   1 
ATOM   10066 C CB  . MET E 1 270 ? 8.455   0.331   28.491  1.00 59.86  ? 272 MET E CB  1 
ATOM   10067 C CG  . MET E 1 270 ? 7.327   0.583   29.483  1.00 77.88  ? 272 MET E CG  1 
ATOM   10068 S SD  . MET E 1 270 ? 5.823   1.205   28.706  1.00 81.04  ? 272 MET E SD  1 
ATOM   10069 C CE  . MET E 1 270 ? 6.081   0.651   27.031  1.00 60.30  ? 272 MET E CE  1 
ATOM   10070 N N   . GLU E 1 271 ? 10.592  -1.222  27.115  1.00 70.24  ? 273 GLU E N   1 
ATOM   10071 C CA  . GLU E 1 271 ? 11.571  -1.558  26.094  1.00 67.79  ? 273 GLU E CA  1 
ATOM   10072 C C   . GLU E 1 271 ? 11.040  -1.183  24.715  1.00 65.66  ? 273 GLU E C   1 
ATOM   10073 O O   . GLU E 1 271 ? 9.856   -0.887  24.535  1.00 64.18  ? 273 GLU E O   1 
ATOM   10074 C CB  . GLU E 1 271 ? 11.925  -3.051  26.143  1.00 76.48  ? 273 GLU E CB  1 
ATOM   10075 C CG  . GLU E 1 271 ? 12.000  -3.628  27.551  1.00 81.02  ? 273 GLU E CG  1 
ATOM   10076 C CD  . GLU E 1 271 ? 13.421  -3.957  27.975  1.00 102.21 ? 273 GLU E CD  1 
ATOM   10077 O OE1 . GLU E 1 271 ? 13.620  -4.359  29.142  1.00 96.88  ? 273 GLU E OE1 1 
ATOM   10078 O OE2 . GLU E 1 271 ? 14.340  -3.813  27.140  1.00 98.42  ? 273 GLU E OE2 1 
ATOM   10079 N N   . TYR E 1 272 ? 11.944  -1.212  23.735  1.00 65.21  ? 274 TYR E N   1 
ATOM   10080 C CA  . TYR E 1 272 ? 11.608  -0.827  22.370  1.00 68.35  ? 274 TYR E CA  1 
ATOM   10081 C C   . TYR E 1 272 ? 10.499  -1.711  21.806  1.00 65.71  ? 274 TYR E C   1 
ATOM   10082 O O   . TYR E 1 272 ? 10.475  -2.924  22.026  1.00 76.35  ? 274 TYR E O   1 
ATOM   10083 C CB  . TYR E 1 272 ? 12.855  -0.912  21.491  1.00 58.87  ? 274 TYR E CB  1 
ATOM   10084 C CG  . TYR E 1 272 ? 12.654  -0.402  20.086  1.00 70.57  ? 274 TYR E CG  1 
ATOM   10085 C CD1 . TYR E 1 272 ? 12.157  0.874   19.853  1.00 65.10  ? 274 TYR E CD1 1 
ATOM   10086 C CD2 . TYR E 1 272 ? 12.960  -1.197  18.990  1.00 66.01  ? 274 TYR E CD2 1 
ATOM   10087 C CE1 . TYR E 1 272 ? 11.972  1.343   18.565  1.00 64.49  ? 274 TYR E CE1 1 
ATOM   10088 C CE2 . TYR E 1 272 ? 12.780  -0.736  17.700  1.00 62.83  ? 274 TYR E CE2 1 
ATOM   10089 C CZ  . TYR E 1 272 ? 12.285  0.533   17.493  1.00 64.04  ? 274 TYR E CZ  1 
ATOM   10090 O OH  . TYR E 1 272 ? 12.107  0.989   16.208  1.00 75.80  ? 274 TYR E OH  1 
ATOM   10091 N N   . GLY E 1 273 ? 9.575   -1.092  21.070  1.00 64.35  ? 275 GLY E N   1 
ATOM   10092 C CA  . GLY E 1 273 ? 8.392   -1.785  20.592  1.00 61.03  ? 275 GLY E CA  1 
ATOM   10093 C C   . GLY E 1 273 ? 8.279   -1.940  19.087  1.00 64.14  ? 275 GLY E C   1 
ATOM   10094 O O   . GLY E 1 273 ? 7.264   -2.442  18.595  1.00 65.34  ? 275 GLY E O   1 
ATOM   10095 N N   . HIS E 1 274 ? 9.305   -1.508  18.348  1.00 68.20  ? 276 HIS E N   1 
ATOM   10096 C CA  . HIS E 1 274 ? 9.369   -1.678  16.892  1.00 76.24  ? 276 HIS E CA  1 
ATOM   10097 C C   . HIS E 1 274 ? 8.134   -1.088  16.212  1.00 74.83  ? 276 HIS E C   1 
ATOM   10098 O O   . HIS E 1 274 ? 7.482   -1.725  15.381  1.00 79.59  ? 276 HIS E O   1 
ATOM   10099 C CB  . HIS E 1 274 ? 9.554   -3.151  16.519  1.00 72.32  ? 276 HIS E CB  1 
ATOM   10100 C CG  . HIS E 1 274 ? 10.649  -3.830  17.284  1.00 74.70  ? 276 HIS E CG  1 
ATOM   10101 N ND1 . HIS E 1 274 ? 11.926  -3.977  16.783  1.00 72.82  ? 276 HIS E ND1 1 
ATOM   10102 C CD2 . HIS E 1 274 ? 10.660  -4.398  18.514  1.00 66.07  ? 276 HIS E CD2 1 
ATOM   10103 C CE1 . HIS E 1 274 ? 12.675  -4.607  17.670  1.00 66.95  ? 276 HIS E CE1 1 
ATOM   10104 N NE2 . HIS E 1 274 ? 11.932  -4.873  18.730  1.00 65.24  ? 276 HIS E NE2 1 
ATOM   10105 N N   . CYS E 1 275 ? 7.818   0.150   16.578  1.00 75.87  ? 277 CYS E N   1 
ATOM   10106 C CA  . CYS E 1 275 ? 6.631   0.846   16.106  1.00 68.75  ? 277 CYS E CA  1 
ATOM   10107 C C   . CYS E 1 275 ? 6.984   2.299   15.814  1.00 74.84  ? 277 CYS E C   1 
ATOM   10108 O O   . CYS E 1 275 ? 8.058   2.790   16.175  1.00 70.69  ? 277 CYS E O   1 
ATOM   10109 C CB  . CYS E 1 275 ? 5.489   0.730   17.129  1.00 60.88  ? 277 CYS E CB  1 
ATOM   10110 S SG  . CYS E 1 275 ? 5.975   1.084   18.863  1.00 91.44  ? 277 CYS E SG  1 
ATOM   10111 N N   . ASN E 1 276 ? 6.071   2.984   15.130  1.00 62.26  ? 278 ASN E N   1 
ATOM   10112 C CA  . ASN E 1 276 ? 6.217   4.397   14.822  1.00 61.29  ? 278 ASN E CA  1 
ATOM   10113 C C   . ASN E 1 276 ? 5.084   5.167   15.482  1.00 61.23  ? 278 ASN E C   1 
ATOM   10114 O O   . ASN E 1 276 ? 3.971   4.654   15.638  1.00 59.30  ? 278 ASN E O   1 
ATOM   10115 C CB  . ASN E 1 276 ? 6.216   4.654   13.307  1.00 51.31  ? 278 ASN E CB  1 
ATOM   10116 C CG  . ASN E 1 276 ? 6.880   5.973   12.934  1.00 60.42  ? 278 ASN E CG  1 
ATOM   10117 O OD1 . ASN E 1 276 ? 7.703   6.503   13.680  1.00 60.53  ? 278 ASN E OD1 1 
ATOM   10118 N ND2 . ASN E 1 276 ? 6.530   6.501   11.768  1.00 59.08  ? 278 ASN E ND2 1 
ATOM   10119 N N   . THR E 1 277 ? 5.380   6.398   15.889  1.00 56.98  ? 279 THR E N   1 
ATOM   10120 C CA  . THR E 1 277 ? 4.371   7.220   16.536  1.00 59.79  ? 279 THR E CA  1 
ATOM   10121 C C   . THR E 1 277 ? 4.653   8.687   16.264  1.00 49.33  ? 279 THR E C   1 
ATOM   10122 O O   . THR E 1 277 ? 5.762   9.075   15.890  1.00 55.13  ? 279 THR E O   1 
ATOM   10123 C CB  . THR E 1 277 ? 4.308   6.976   18.050  1.00 55.17  ? 279 THR E CB  1 
ATOM   10124 O OG1 . THR E 1 277 ? 3.062   7.466   18.560  1.00 47.46  ? 279 THR E OG1 1 
ATOM   10125 C CG2 . THR E 1 277 ? 5.450   7.691   18.759  1.00 57.52  ? 279 THR E CG2 1 
ATOM   10126 N N   . LYS E 1 278 ? 3.607   9.491   16.437  1.00 55.98  ? 280 LYS E N   1 
ATOM   10127 C CA  . LYS E 1 278 ? 3.692   10.941  16.434  1.00 50.66  ? 280 LYS E CA  1 
ATOM   10128 C C   . LYS E 1 278 ? 3.771   11.514  17.839  1.00 50.21  ? 280 LYS E C   1 
ATOM   10129 O O   . LYS E 1 278 ? 4.199   12.661  18.007  1.00 56.38  ? 280 LYS E O   1 
ATOM   10130 C CB  . LYS E 1 278 ? 2.468   11.527  15.717  1.00 58.72  ? 280 LYS E CB  1 
ATOM   10131 C CG  . LYS E 1 278 ? 2.743   12.737  14.857  1.00 69.23  ? 280 LYS E CG  1 
ATOM   10132 C CD  . LYS E 1 278 ? 1.457   13.282  14.234  1.00 78.85  ? 280 LYS E CD  1 
ATOM   10133 C CE  . LYS E 1 278 ? 0.269   13.179  15.192  1.00 68.49  ? 280 LYS E CE  1 
ATOM   10134 N NZ  . LYS E 1 278 ? -0.861  14.054  14.774  1.00 71.87  ? 280 LYS E NZ  1 
ATOM   10135 N N   . CYS E 1 279 ? 3.370   10.733  18.842  1.00 48.82  ? 281 CYS E N   1 
ATOM   10136 C CA  . CYS E 1 279 ? 3.254   11.180  20.223  1.00 47.80  ? 281 CYS E CA  1 
ATOM   10137 C C   . CYS E 1 279 ? 3.578   10.006  21.135  1.00 59.01  ? 281 CYS E C   1 
ATOM   10138 O O   . CYS E 1 279 ? 2.971   8.937   21.008  1.00 55.68  ? 281 CYS E O   1 
ATOM   10139 C CB  . CYS E 1 279 ? 1.841   11.714  20.508  1.00 49.00  ? 281 CYS E CB  1 
ATOM   10140 S SG  . CYS E 1 279 ? 1.523   12.217  22.221  1.00 60.04  ? 281 CYS E SG  1 
ATOM   10141 N N   . GLN E 1 280 ? 4.521   10.211  22.053  1.00 55.65  ? 282 GLN E N   1 
ATOM   10142 C CA  . GLN E 1 280 ? 4.996   9.168   22.952  1.00 43.19  ? 282 GLN E CA  1 
ATOM   10143 C C   . GLN E 1 280 ? 4.763   9.581   24.399  1.00 44.50  ? 282 GLN E C   1 
ATOM   10144 O O   . GLN E 1 280 ? 4.895   10.759  24.748  1.00 52.70  ? 282 GLN E O   1 
ATOM   10145 C CB  . GLN E 1 280 ? 6.489   8.882   22.721  1.00 43.15  ? 282 GLN E CB  1 
ATOM   10146 C CG  . GLN E 1 280 ? 7.063   7.787   23.606  1.00 49.90  ? 282 GLN E CG  1 
ATOM   10147 C CD  . GLN E 1 280 ? 6.606   6.402   23.179  1.00 54.57  ? 282 GLN E CD  1 
ATOM   10148 O OE1 . GLN E 1 280 ? 6.902   5.951   22.072  1.00 47.58  ? 282 GLN E OE1 1 
ATOM   10149 N NE2 . GLN E 1 280 ? 5.877   5.723   24.057  1.00 52.41  ? 282 GLN E NE2 1 
ATOM   10150 N N   . THR E 1 281 ? 4.407   8.611   25.232  1.00 44.53  ? 283 THR E N   1 
ATOM   10151 C CA  . THR E 1 281 ? 4.272   8.770   26.671  1.00 50.77  ? 283 THR E CA  1 
ATOM   10152 C C   . THR E 1 281 ? 5.101   7.693   27.352  1.00 49.53  ? 283 THR E C   1 
ATOM   10153 O O   . THR E 1 281 ? 5.449   6.684   26.730  1.00 46.90  ? 283 THR E O   1 
ATOM   10154 C CB  . THR E 1 281 ? 2.809   8.664   27.135  1.00 49.05  ? 283 THR E CB  1 
ATOM   10155 O OG1 . THR E 1 281 ? 2.425   7.285   27.206  1.00 54.43  ? 283 THR E OG1 1 
ATOM   10156 C CG2 . THR E 1 281 ? 1.877   9.408   26.184  1.00 48.58  ? 283 THR E CG2 1 
ATOM   10157 N N   . PRO E 1 282 ? 5.448   7.881   28.629  1.00 55.24  ? 284 PRO E N   1 
ATOM   10158 C CA  . PRO E 1 282 ? 6.250   6.859   29.321  1.00 52.26  ? 284 PRO E CA  1 
ATOM   10159 C C   . PRO E 1 282 ? 5.584   5.499   29.396  1.00 61.13  ? 284 PRO E C   1 
ATOM   10160 O O   . PRO E 1 282 ? 6.287   4.497   29.584  1.00 65.76  ? 284 PRO E O   1 
ATOM   10161 C CB  . PRO E 1 282 ? 6.444   7.456   30.721  1.00 59.73  ? 284 PRO E CB  1 
ATOM   10162 C CG  . PRO E 1 282 ? 6.300   8.927   30.524  1.00 45.07  ? 284 PRO E CG  1 
ATOM   10163 C CD  . PRO E 1 282 ? 5.270   9.087   29.459  1.00 45.36  ? 284 PRO E CD  1 
ATOM   10164 N N   . ILE E 1 283 ? 4.261   5.421   29.255  1.00 55.72  ? 285 ILE E N   1 
ATOM   10165 C CA  . ILE E 1 283 ? 3.546   4.157   29.380  1.00 49.37  ? 285 ILE E CA  1 
ATOM   10166 C C   . ILE E 1 283 ? 3.000   3.656   28.054  1.00 57.68  ? 285 ILE E C   1 
ATOM   10167 O O   . ILE E 1 283 ? 2.414   2.563   28.015  1.00 58.37  ? 285 ILE E O   1 
ATOM   10168 C CB  . ILE E 1 283 ? 2.418   4.250   30.425  1.00 48.41  ? 285 ILE E CB  1 
ATOM   10169 C CG1 . ILE E 1 283 ? 1.205   4.990   29.862  1.00 46.36  ? 285 ILE E CG1 1 
ATOM   10170 C CG2 . ILE E 1 283 ? 2.919   4.921   31.689  1.00 42.45  ? 285 ILE E CG2 1 
ATOM   10171 C CD1 . ILE E 1 283 ? 0.083   5.114   30.859  1.00 40.50  ? 285 ILE E CD1 1 
ATOM   10172 N N   . GLY E 1 284 ? 3.169   4.401   26.973  1.00 53.19  ? 286 GLY E N   1 
ATOM   10173 C CA  . GLY E 1 284 ? 2.719   3.937   25.676  1.00 47.80  ? 286 GLY E CA  1 
ATOM   10174 C C   . GLY E 1 284 ? 2.540   5.078   24.703  1.00 55.03  ? 286 GLY E C   1 
ATOM   10175 O O   . GLY E 1 284 ? 2.423   6.245   25.074  1.00 47.99  ? 286 GLY E O   1 
ATOM   10176 N N   . ALA E 1 285 ? 2.516   4.720   23.423  1.00 54.05  ? 287 ALA E N   1 
ATOM   10177 C CA  . ALA E 1 285 ? 2.349   5.679   22.343  1.00 43.43  ? 287 ALA E CA  1 
ATOM   10178 C C   . ALA E 1 285 ? 0.876   5.820   21.976  1.00 58.47  ? 287 ALA E C   1 
ATOM   10179 O O   . ALA E 1 285 ? 0.071   4.911   22.184  1.00 54.76  ? 287 ALA E O   1 
ATOM   10180 C CB  . ALA E 1 285 ? 3.158   5.254   21.119  1.00 44.99  ? 287 ALA E CB  1 
ATOM   10181 N N   . ILE E 1 286 ? 0.525   6.972   21.416  1.00 55.64  ? 288 ILE E N   1 
ATOM   10182 C CA  . ILE E 1 286 ? -0.865  7.299   21.124  1.00 56.44  ? 288 ILE E CA  1 
ATOM   10183 C C   . ILE E 1 286 ? -0.987  7.714   19.665  1.00 53.62  ? 288 ILE E C   1 
ATOM   10184 O O   . ILE E 1 286 ? -0.195  8.529   19.178  1.00 52.68  ? 288 ILE E O   1 
ATOM   10185 C CB  . ILE E 1 286 ? -1.387  8.405   22.063  1.00 51.55  ? 288 ILE E CB  1 
ATOM   10186 C CG1 . ILE E 1 286 ? -2.676  9.026   21.526  1.00 65.46  ? 288 ILE E CG1 1 
ATOM   10187 C CG2 . ILE E 1 286 ? -0.346  9.455   22.271  1.00 56.64  ? 288 ILE E CG2 1 
ATOM   10188 C CD1 . ILE E 1 286 ? -3.319  9.982   22.504  1.00 76.16  ? 288 ILE E CD1 1 
ATOM   10189 N N   . ASN E 1 287 ? -1.963  7.133   18.966  1.00 48.65  ? 289 ASN E N   1 
ATOM   10190 C CA  . ASN E 1 287 ? -2.286  7.482   17.583  1.00 59.22  ? 289 ASN E CA  1 
ATOM   10191 C C   . ASN E 1 287 ? -3.714  8.015   17.576  1.00 57.70  ? 289 ASN E C   1 
ATOM   10192 O O   . ASN E 1 287 ? -4.674  7.240   17.625  1.00 57.31  ? 289 ASN E O   1 
ATOM   10193 C CB  . ASN E 1 287 ? -2.138  6.283   16.647  1.00 49.43  ? 289 ASN E CB  1 
ATOM   10194 C CG  . ASN E 1 287 ? -2.326  6.658   15.188  1.00 59.03  ? 289 ASN E CG  1 
ATOM   10195 O OD1 . ASN E 1 287 ? -1.876  7.716   14.748  1.00 66.56  ? 289 ASN E OD1 1 
ATOM   10196 N ND2 . ASN E 1 287 ? -2.986  5.788   14.428  1.00 64.37  ? 289 ASN E ND2 1 
ATOM   10197 N N   . SER E 1 288 ? -3.857  9.336   17.523  1.00 56.53  ? 290 SER E N   1 
ATOM   10198 C CA  . SER E 1 288 ? -5.171  9.940   17.654  1.00 57.92  ? 290 SER E CA  1 
ATOM   10199 C C   . SER E 1 288 ? -5.203  11.279  16.939  1.00 55.92  ? 290 SER E C   1 
ATOM   10200 O O   . SER E 1 288 ? -4.200  11.995  16.876  1.00 55.12  ? 290 SER E O   1 
ATOM   10201 C CB  . SER E 1 288 ? -5.551  10.129  19.126  1.00 56.58  ? 290 SER E CB  1 
ATOM   10202 O OG  . SER E 1 288 ? -6.918  10.474  19.260  1.00 63.93  ? 290 SER E OG  1 
ATOM   10203 N N   . SER E 1 289 ? -6.372  11.605  16.397  1.00 52.78  ? 291 SER E N   1 
ATOM   10204 C CA  . SER E 1 289 ? -6.662  12.950  15.928  1.00 49.06  ? 291 SER E CA  1 
ATOM   10205 C C   . SER E 1 289 ? -7.564  13.705  16.892  1.00 49.26  ? 291 SER E C   1 
ATOM   10206 O O   . SER E 1 289 ? -7.943  14.844  16.605  1.00 53.68  ? 291 SER E O   1 
ATOM   10207 C CB  . SER E 1 289 ? -7.303  12.900  14.536  1.00 47.06  ? 291 SER E CB  1 
ATOM   10208 O OG  . SER E 1 289 ? -8.285  11.882  14.471  1.00 63.46  ? 291 SER E OG  1 
ATOM   10209 N N   . MET E 1 290 ? -7.919  13.090  18.019  1.00 48.76  ? 292 MET E N   1 
ATOM   10210 C CA  . MET E 1 290 ? -8.809  13.714  18.983  1.00 50.30  ? 292 MET E CA  1 
ATOM   10211 C C   . MET E 1 290 ? -8.120  14.902  19.658  1.00 52.42  ? 292 MET E C   1 
ATOM   10212 O O   . MET E 1 290 ? -6.906  14.885  19.881  1.00 55.04  ? 292 MET E O   1 
ATOM   10213 C CB  . MET E 1 290 ? -9.244  12.690  20.027  1.00 45.12  ? 292 MET E CB  1 
ATOM   10214 C CG  . MET E 1 290 ? -10.336 11.722  19.557  1.00 43.62  ? 292 MET E CG  1 
ATOM   10215 S SD  . MET E 1 290 ? -11.551 12.417  18.403  1.00 62.49  ? 292 MET E SD  1 
ATOM   10216 C CE  . MET E 1 290 ? -10.971 11.810  16.819  1.00 56.44  ? 292 MET E CE  1 
ATOM   10217 N N   . PRO E 1 291 ? -8.872  15.956  19.989  1.00 46.40  ? 293 PRO E N   1 
ATOM   10218 C CA  . PRO E 1 291 ? -8.232  17.151  20.560  1.00 46.88  ? 293 PRO E CA  1 
ATOM   10219 C C   . PRO E 1 291 ? -7.753  16.969  21.991  1.00 48.46  ? 293 PRO E C   1 
ATOM   10220 O O   . PRO E 1 291 ? -6.842  17.694  22.410  1.00 49.21  ? 293 PRO E O   1 
ATOM   10221 C CB  . PRO E 1 291 ? -9.336  18.213  20.471  1.00 42.93  ? 293 PRO E CB  1 
ATOM   10222 C CG  . PRO E 1 291 ? -10.595 17.435  20.548  1.00 37.63  ? 293 PRO E CG  1 
ATOM   10223 C CD  . PRO E 1 291 ? -10.325 16.133  19.828  1.00 44.86  ? 293 PRO E CD  1 
ATOM   10224 N N   . PHE E 1 292 ? -8.315  16.025  22.748  1.00 49.27  ? 294 PHE E N   1 
ATOM   10225 C CA  . PHE E 1 292 ? -7.987  15.870  24.159  1.00 50.41  ? 294 PHE E CA  1 
ATOM   10226 C C   . PHE E 1 292 ? -7.654  14.420  24.487  1.00 46.87  ? 294 PHE E C   1 
ATOM   10227 O O   . PHE E 1 292 ? -8.138  13.487  23.838  1.00 54.93  ? 294 PHE E O   1 
ATOM   10228 C CB  . PHE E 1 292 ? -9.144  16.346  25.052  1.00 44.60  ? 294 PHE E CB  1 
ATOM   10229 C CG  . PHE E 1 292 ? -9.613  17.740  24.746  1.00 50.51  ? 294 PHE E CG  1 
ATOM   10230 C CD1 . PHE E 1 292 ? -8.842  18.837  25.093  1.00 47.49  ? 294 PHE E CD1 1 
ATOM   10231 C CD2 . PHE E 1 292 ? -10.829 17.954  24.115  1.00 52.94  ? 294 PHE E CD2 1 
ATOM   10232 C CE1 . PHE E 1 292 ? -9.270  20.121  24.814  1.00 41.86  ? 294 PHE E CE1 1 
ATOM   10233 C CE2 . PHE E 1 292 ? -11.267 19.235  23.834  1.00 40.28  ? 294 PHE E CE2 1 
ATOM   10234 C CZ  . PHE E 1 292 ? -10.489 20.320  24.182  1.00 41.63  ? 294 PHE E CZ  1 
ATOM   10235 N N   . HIS E 1 293 ? -6.823  14.243  25.515  1.00 43.81  ? 295 HIS E N   1 
ATOM   10236 C CA  . HIS E 1 293 ? -6.478  12.924  26.030  1.00 41.47  ? 295 HIS E CA  1 
ATOM   10237 C C   . HIS E 1 293 ? -6.257  13.028  27.532  1.00 44.29  ? 295 HIS E C   1 
ATOM   10238 O O   . HIS E 1 293 ? -6.054  14.119  28.074  1.00 42.75  ? 295 HIS E O   1 
ATOM   10239 C CB  . HIS E 1 293 ? -5.238  12.344  25.340  1.00 39.72  ? 295 HIS E CB  1 
ATOM   10240 C CG  . HIS E 1 293 ? -3.942  12.873  25.872  1.00 45.73  ? 295 HIS E CG  1 
ATOM   10241 N ND1 . HIS E 1 293 ? -3.262  12.272  26.910  1.00 44.51  ? 295 HIS E ND1 1 
ATOM   10242 C CD2 . HIS E 1 293 ? -3.196  13.941  25.503  1.00 42.13  ? 295 HIS E CD2 1 
ATOM   10243 C CE1 . HIS E 1 293 ? -2.155  12.949  27.159  1.00 36.94  ? 295 HIS E CE1 1 
ATOM   10244 N NE2 . HIS E 1 293 ? -2.090  13.966  26.319  1.00 45.30  ? 295 HIS E NE2 1 
ATOM   10245 N N   . ASN E 1 294 ? -6.303  11.877  28.206  1.00 37.83  ? 296 ASN E N   1 
ATOM   10246 C CA  . ASN E 1 294 ? -6.096  11.828  29.650  1.00 48.97  ? 296 ASN E CA  1 
ATOM   10247 C C   . ASN E 1 294 ? -5.075  10.762  30.037  1.00 39.87  ? 296 ASN E C   1 
ATOM   10248 O O   . ASN E 1 294 ? -5.113  10.235  31.151  1.00 42.68  ? 296 ASN E O   1 
ATOM   10249 C CB  . ASN E 1 294 ? -7.419  11.595  30.383  1.00 33.95  ? 296 ASN E CB  1 
ATOM   10250 C CG  . ASN E 1 294 ? -7.973  10.188  30.180  1.00 47.01  ? 296 ASN E CG  1 
ATOM   10251 O OD1 . ASN E 1 294 ? -7.548  9.457   29.282  1.00 45.87  ? 296 ASN E OD1 1 
ATOM   10252 N ND2 . ASN E 1 294 ? -8.935  9.810   31.012  1.00 41.78  ? 296 ASN E ND2 1 
ATOM   10253 N N   . ILE E 1 295 ? -4.144  10.448  29.138  1.00 46.10  ? 297 ILE E N   1 
ATOM   10254 C CA  . ILE E 1 295 ? -3.296  9.276   29.333  1.00 45.96  ? 297 ILE E CA  1 
ATOM   10255 C C   . ILE E 1 295 ? -2.130  9.587   30.263  1.00 48.27  ? 297 ILE E C   1 
ATOM   10256 O O   . ILE E 1 295 ? -1.918  8.890   31.262  1.00 63.37  ? 297 ILE E O   1 
ATOM   10257 C CB  . ILE E 1 295 ? -2.815  8.738   27.972  1.00 51.43  ? 297 ILE E CB  1 
ATOM   10258 C CG1 . ILE E 1 295 ? -3.986  8.078   27.230  1.00 44.26  ? 297 ILE E CG1 1 
ATOM   10259 C CG2 . ILE E 1 295 ? -1.656  7.768   28.159  1.00 42.63  ? 297 ILE E CG2 1 
ATOM   10260 C CD1 . ILE E 1 295 ? -3.856  8.093   25.721  1.00 49.81  ? 297 ILE E CD1 1 
ATOM   10261 N N   . HIS E 1 296 ? -1.354  10.629  29.955  1.00 52.97  ? 298 HIS E N   1 
ATOM   10262 C CA  . HIS E 1 296 ? -0.139  10.924  30.708  1.00 45.83  ? 298 HIS E CA  1 
ATOM   10263 C C   . HIS E 1 296 ? 0.357   12.333  30.390  1.00 51.57  ? 298 HIS E C   1 
ATOM   10264 O O   . HIS E 1 296 ? 0.306   12.762  29.230  1.00 50.68  ? 298 HIS E O   1 
ATOM   10265 C CB  . HIS E 1 296 ? 0.945   9.892   30.391  1.00 49.79  ? 298 HIS E CB  1 
ATOM   10266 C CG  . HIS E 1 296 ? 1.950   9.709   31.485  1.00 54.22  ? 298 HIS E CG  1 
ATOM   10267 N ND1 . HIS E 1 296 ? 3.064   10.511  31.613  1.00 52.54  ? 298 HIS E ND1 1 
ATOM   10268 C CD2 . HIS E 1 296 ? 2.015   8.811   32.495  1.00 55.15  ? 298 HIS E CD2 1 
ATOM   10269 C CE1 . HIS E 1 296 ? 3.769   10.117  32.658  1.00 57.32  ? 298 HIS E CE1 1 
ATOM   10270 N NE2 . HIS E 1 296 ? 3.154   9.087   33.211  1.00 51.61  ? 298 HIS E NE2 1 
ATOM   10271 N N   . PRO E 1 297 ? 0.848   13.079  31.386  1.00 46.20  ? 299 PRO E N   1 
ATOM   10272 C CA  . PRO E 1 297 ? 1.280   14.461  31.133  1.00 46.36  ? 299 PRO E CA  1 
ATOM   10273 C C   . PRO E 1 297 ? 2.673   14.594  30.528  1.00 48.79  ? 299 PRO E C   1 
ATOM   10274 O O   . PRO E 1 297 ? 2.959   15.602  29.873  1.00 46.82  ? 299 PRO E O   1 
ATOM   10275 C CB  . PRO E 1 297 ? 1.226   15.101  32.526  1.00 48.12  ? 299 PRO E CB  1 
ATOM   10276 C CG  . PRO E 1 297 ? 1.445   13.960  33.469  1.00 39.80  ? 299 PRO E CG  1 
ATOM   10277 C CD  . PRO E 1 297 ? 0.844   12.744  32.822  1.00 43.70  ? 299 PRO E CD  1 
ATOM   10278 N N   . LEU E 1 298 ? 3.553   13.612  30.733  1.00 52.07  ? 300 LEU E N   1 
ATOM   10279 C CA  . LEU E 1 298 ? 4.949   13.737  30.299  1.00 53.75  ? 300 LEU E CA  1 
ATOM   10280 C C   . LEU E 1 298 ? 5.092   13.198  28.877  1.00 49.84  ? 300 LEU E C   1 
ATOM   10281 O O   . LEU E 1 298 ? 5.618   12.113  28.635  1.00 49.69  ? 300 LEU E O   1 
ATOM   10282 C CB  . LEU E 1 298 ? 5.882   13.019  31.269  1.00 46.47  ? 300 LEU E CB  1 
ATOM   10283 C CG  . LEU E 1 298 ? 5.747   13.382  32.751  1.00 56.16  ? 300 LEU E CG  1 
ATOM   10284 C CD1 . LEU E 1 298 ? 6.802   12.654  33.573  1.00 37.35  ? 300 LEU E CD1 1 
ATOM   10285 C CD2 . LEU E 1 298 ? 5.840   14.892  32.968  1.00 50.72  ? 300 LEU E CD2 1 
ATOM   10286 N N   . THR E 1 299 ? 4.638   13.997  27.915  1.00 49.92  ? 301 THR E N   1 
ATOM   10287 C CA  . THR E 1 299 ? 4.568   13.566  26.525  1.00 48.76  ? 301 THR E CA  1 
ATOM   10288 C C   . THR E 1 299 ? 5.700   14.167  25.701  1.00 43.45  ? 301 THR E C   1 
ATOM   10289 O O   . THR E 1 299 ? 6.231   15.235  26.020  1.00 42.86  ? 301 THR E O   1 
ATOM   10290 C CB  . THR E 1 299 ? 3.227   13.953  25.901  1.00 52.98  ? 301 THR E CB  1 
ATOM   10291 O OG1 . THR E 1 299 ? 2.964   15.339  26.161  1.00 52.43  ? 301 THR E OG1 1 
ATOM   10292 C CG2 . THR E 1 299 ? 2.105   13.106  26.480  1.00 41.72  ? 301 THR E CG2 1 
ATOM   10293 N N   . ILE E 1 300 ? 6.077   13.453  24.643  1.00 40.59  ? 302 ILE E N   1 
ATOM   10294 C CA  . ILE E 1 300 ? 7.014   13.943  23.640  1.00 43.10  ? 302 ILE E CA  1 
ATOM   10295 C C   . ILE E 1 300 ? 6.383   13.715  22.275  1.00 44.20  ? 302 ILE E C   1 
ATOM   10296 O O   . ILE E 1 300 ? 6.070   12.574  21.917  1.00 51.42  ? 302 ILE E O   1 
ATOM   10297 C CB  . ILE E 1 300 ? 8.383   13.244  23.721  1.00 47.14  ? 302 ILE E CB  1 
ATOM   10298 C CG1 . ILE E 1 300 ? 8.930   13.257  25.147  1.00 37.07  ? 302 ILE E CG1 1 
ATOM   10299 C CG2 . ILE E 1 300 ? 9.380   13.905  22.780  1.00 43.73  ? 302 ILE E CG2 1 
ATOM   10300 C CD1 . ILE E 1 300 ? 10.259  12.542  25.262  1.00 41.82  ? 302 ILE E CD1 1 
ATOM   10301 N N   . GLY E 1 301 ? 6.201   14.790  21.516  1.00 44.82  ? 303 GLY E N   1 
ATOM   10302 C CA  . GLY E 1 301 ? 5.634   14.742  20.189  1.00 51.63  ? 303 GLY E CA  1 
ATOM   10303 C C   . GLY E 1 301 ? 4.460   15.686  20.062  1.00 51.86  ? 303 GLY E C   1 
ATOM   10304 O O   . GLY E 1 301 ? 4.154   16.469  20.968  1.00 49.50  ? 303 GLY E O   1 
ATOM   10305 N N   . GLU E 1 302 ? 3.792   15.611  18.912  1.00 58.17  ? 304 GLU E N   1 
ATOM   10306 C CA  . GLU E 1 302 ? 2.573   16.373  18.657  1.00 59.34  ? 304 GLU E CA  1 
ATOM   10307 C C   . GLU E 1 302 ? 1.402   15.610  19.263  1.00 51.17  ? 304 GLU E C   1 
ATOM   10308 O O   . GLU E 1 302 ? 1.015   14.549  18.760  1.00 53.07  ? 304 GLU E O   1 
ATOM   10309 C CB  . GLU E 1 302 ? 2.386   16.594  17.159  1.00 56.20  ? 304 GLU E CB  1 
ATOM   10310 C CG  . GLU E 1 302 ? 3.681   16.935  16.422  1.00 71.00  ? 304 GLU E CG  1 
ATOM   10311 C CD  . GLU E 1 302 ? 4.248   15.765  15.616  1.00 83.63  ? 304 GLU E CD  1 
ATOM   10312 O OE1 . GLU E 1 302 ? 5.061   14.991  16.174  1.00 79.89  ? 304 GLU E OE1 1 
ATOM   10313 O OE2 . GLU E 1 302 ? 3.899   15.633  14.421  1.00 77.83  ? 304 GLU E OE2 1 
ATOM   10314 N N   . CYS E 1 303 ? 0.835   16.146  20.333  1.00 47.94  ? 305 CYS E N   1 
ATOM   10315 C CA  . CYS E 1 303 ? -0.075  15.411  21.193  1.00 37.53  ? 305 CYS E CA  1 
ATOM   10316 C C   . CYS E 1 303 ? -1.350  16.209  21.411  1.00 40.76  ? 305 CYS E C   1 
ATOM   10317 O O   . CYS E 1 303 ? -1.351  17.438  21.299  1.00 51.04  ? 305 CYS E O   1 
ATOM   10318 C CB  . CYS E 1 303 ? 0.609   15.123  22.539  1.00 39.19  ? 305 CYS E CB  1 
ATOM   10319 S SG  . CYS E 1 303 ? 2.145   14.150  22.371  1.00 82.05  ? 305 CYS E SG  1 
ATOM   10320 N N   . PRO E 1 304 ? -2.458  15.537  21.704  1.00 45.12  ? 306 PRO E N   1 
ATOM   10321 C CA  . PRO E 1 304 ? -3.659  16.253  22.147  1.00 47.80  ? 306 PRO E CA  1 
ATOM   10322 C C   . PRO E 1 304 ? -3.422  16.893  23.506  1.00 46.34  ? 306 PRO E C   1 
ATOM   10323 O O   . PRO E 1 304 ? -2.445  16.609  24.197  1.00 41.50  ? 306 PRO E O   1 
ATOM   10324 C CB  . PRO E 1 304 ? -4.737  15.164  22.217  1.00 44.25  ? 306 PRO E CB  1 
ATOM   10325 C CG  . PRO E 1 304 ? -3.997  13.861  22.200  1.00 44.94  ? 306 PRO E CG  1 
ATOM   10326 C CD  . PRO E 1 304 ? -2.701  14.098  21.495  1.00 45.65  ? 306 PRO E CD  1 
ATOM   10327 N N   . LYS E 1 305 ? -4.328  17.790  23.878  1.00 45.80  ? 307 LYS E N   1 
ATOM   10328 C CA  . LYS E 1 305 ? -4.187  18.491  25.146  1.00 38.40  ? 307 LYS E CA  1 
ATOM   10329 C C   . LYS E 1 305 ? -4.544  17.567  26.305  1.00 42.73  ? 307 LYS E C   1 
ATOM   10330 O O   . LYS E 1 305 ? -5.554  16.855  26.259  1.00 46.33  ? 307 LYS E O   1 
ATOM   10331 C CB  . LYS E 1 305 ? -5.069  19.738  25.161  1.00 42.05  ? 307 LYS E CB  1 
ATOM   10332 C CG  . LYS E 1 305 ? -4.712  20.760  24.084  1.00 40.23  ? 307 LYS E CG  1 
ATOM   10333 C CD  . LYS E 1 305 ? -3.211  20.948  23.967  1.00 35.57  ? 307 LYS E CD  1 
ATOM   10334 C CE  . LYS E 1 305 ? -2.862  22.109  23.053  1.00 45.39  ? 307 LYS E CE  1 
ATOM   10335 N NZ  . LYS E 1 305 ? -2.535  21.658  21.678  1.00 61.70  ? 307 LYS E NZ  1 
ATOM   10336 N N   . TYR E 1 306 ? -3.704  17.575  27.341  1.00 38.51  ? 308 TYR E N   1 
ATOM   10337 C CA  . TYR E 1 306 ? -3.921  16.761  28.531  1.00 42.66  ? 308 TYR E CA  1 
ATOM   10338 C C   . TYR E 1 306 ? -5.007  17.378  29.407  1.00 35.20  ? 308 TYR E C   1 
ATOM   10339 O O   . TYR E 1 306 ? -4.986  18.580  29.682  1.00 44.36  ? 308 TYR E O   1 
ATOM   10340 C CB  . TYR E 1 306 ? -2.614  16.632  29.317  1.00 34.44  ? 308 TYR E CB  1 
ATOM   10341 C CG  . TYR E 1 306 ? -2.668  15.679  30.489  1.00 49.67  ? 308 TYR E CG  1 
ATOM   10342 C CD1 . TYR E 1 306 ? -3.141  14.380  30.336  1.00 48.56  ? 308 TYR E CD1 1 
ATOM   10343 C CD2 . TYR E 1 306 ? -2.217  16.068  31.745  1.00 51.65  ? 308 TYR E CD2 1 
ATOM   10344 C CE1 . TYR E 1 306 ? -3.179  13.499  31.406  1.00 47.63  ? 308 TYR E CE1 1 
ATOM   10345 C CE2 . TYR E 1 306 ? -2.251  15.196  32.822  1.00 50.10  ? 308 TYR E CE2 1 
ATOM   10346 C CZ  . TYR E 1 306 ? -2.734  13.915  32.648  1.00 53.96  ? 308 TYR E CZ  1 
ATOM   10347 O OH  . TYR E 1 306 ? -2.768  13.055  33.723  1.00 53.56  ? 308 TYR E OH  1 
ATOM   10348 N N   . VAL E 1 307 ? -5.963  16.554  29.840  1.00 45.51  ? 309 VAL E N   1 
ATOM   10349 C CA  . VAL E 1 307 ? -7.050  17.003  30.702  1.00 48.22  ? 309 VAL E CA  1 
ATOM   10350 C C   . VAL E 1 307 ? -7.291  15.959  31.782  1.00 49.65  ? 309 VAL E C   1 
ATOM   10351 O O   . VAL E 1 307 ? -6.951  14.783  31.632  1.00 51.51  ? 309 VAL E O   1 
ATOM   10352 C CB  . VAL E 1 307 ? -8.362  17.258  29.922  1.00 39.33  ? 309 VAL E CB  1 
ATOM   10353 C CG1 . VAL E 1 307 ? -8.212  18.440  28.963  1.00 38.75  ? 309 VAL E CG1 1 
ATOM   10354 C CG2 . VAL E 1 307 ? -8.773  16.009  29.171  1.00 39.61  ? 309 VAL E CG2 1 
ATOM   10355 N N   . LYS E 1 308 ? -7.894  16.406  32.881  1.00 41.34  ? 310 LYS E N   1 
ATOM   10356 C CA  . LYS E 1 308 ? -8.344  15.515  33.950  1.00 43.51  ? 310 LYS E CA  1 
ATOM   10357 C C   . LYS E 1 308 ? -9.815  15.215  33.690  1.00 51.66  ? 310 LYS E C   1 
ATOM   10358 O O   . LYS E 1 308 ? -10.707 15.904  34.186  1.00 57.41  ? 310 LYS E O   1 
ATOM   10359 C CB  . LYS E 1 308 ? -8.129  16.141  35.322  1.00 47.26  ? 310 LYS E CB  1 
ATOM   10360 C CG  . LYS E 1 308 ? -8.184  15.129  36.458  1.00 59.34  ? 310 LYS E CG  1 
ATOM   10361 C CD  . LYS E 1 308 ? -7.869  15.775  37.797  1.00 65.23  ? 310 LYS E CD  1 
ATOM   10362 C CE  . LYS E 1 308 ? -9.116  15.877  38.657  1.00 61.39  ? 310 LYS E CE  1 
ATOM   10363 N NZ  . LYS E 1 308 ? -8.808  15.968  40.110  1.00 58.58  ? 310 LYS E NZ  1 
ATOM   10364 N N   . SER E 1 309 ? -10.068 14.178  32.897  1.00 49.18  ? 311 SER E N   1 
ATOM   10365 C CA  . SER E 1 309 ? -11.427 13.859  32.493  1.00 42.81  ? 311 SER E CA  1 
ATOM   10366 C C   . SER E 1 309 ? -11.525 12.379  32.160  1.00 51.62  ? 311 SER E C   1 
ATOM   10367 O O   . SER E 1 309 ? -10.577 11.775  31.649  1.00 58.43  ? 311 SER E O   1 
ATOM   10368 C CB  . SER E 1 309 ? -11.854 14.703  31.288  1.00 41.73  ? 311 SER E CB  1 
ATOM   10369 O OG  . SER E 1 309 ? -13.237 14.551  31.031  1.00 51.69  ? 311 SER E OG  1 
ATOM   10370 N N   . ASN E 1 310 ? -12.687 11.800  32.449  1.00 50.27  ? 312 ASN E N   1 
ATOM   10371 C CA  . ASN E 1 310 ? -12.954 10.413  32.096  1.00 56.81  ? 312 ASN E CA  1 
ATOM   10372 C C   . ASN E 1 310 ? -13.695 10.268  30.780  1.00 53.80  ? 312 ASN E C   1 
ATOM   10373 O O   . ASN E 1 310 ? -13.524 9.251   30.100  1.00 52.37  ? 312 ASN E O   1 
ATOM   10374 C CB  . ASN E 1 310 ? -13.765 9.728   33.197  1.00 62.88  ? 312 ASN E CB  1 
ATOM   10375 C CG  . ASN E 1 310 ? -13.017 9.654   34.505  1.00 73.71  ? 312 ASN E CG  1 
ATOM   10376 O OD1 . ASN E 1 310 ? -11.795 9.475   34.528  1.00 59.47  ? 312 ASN E OD1 1 
ATOM   10377 N ND2 . ASN E 1 310 ? -13.744 9.801   35.609  1.00 69.64  ? 312 ASN E ND2 1 
ATOM   10378 N N   . LYS E 1 311 ? -14.507 11.255  30.407  1.00 52.98  ? 313 LYS E N   1 
ATOM   10379 C CA  . LYS E 1 311 ? -15.295 11.176  29.185  1.00 55.96  ? 313 LYS E CA  1 
ATOM   10380 C C   . LYS E 1 311 ? -15.626 12.575  28.691  1.00 43.88  ? 313 LYS E C   1 
ATOM   10381 O O   . LYS E 1 311 ? -15.961 13.464  29.480  1.00 51.72  ? 313 LYS E O   1 
ATOM   10382 C CB  . LYS E 1 311 ? -16.590 10.377  29.401  1.00 48.57  ? 313 LYS E CB  1 
ATOM   10383 C CG  . LYS E 1 311 ? -17.451 10.865  30.563  1.00 50.52  ? 313 LYS E CG  1 
ATOM   10384 C CD  . LYS E 1 311 ? -18.647 11.679  30.068  1.00 79.14  ? 313 LYS E CD  1 
ATOM   10385 C CE  . LYS E 1 311 ? -19.717 11.823  31.146  1.00 79.16  ? 313 LYS E CE  1 
ATOM   10386 N NZ  . LYS E 1 311 ? -21.060 12.096  30.556  1.00 56.52  ? 313 LYS E NZ  1 
ATOM   10387 N N   . LEU E 1 312 ? -15.532 12.758  27.377  1.00 43.46  ? 314 LEU E N   1 
ATOM   10388 C CA  . LEU E 1 312 ? -15.978 13.971  26.696  1.00 47.13  ? 314 LEU E CA  1 
ATOM   10389 C C   . LEU E 1 312 ? -16.865 13.491  25.552  1.00 51.90  ? 314 LEU E C   1 
ATOM   10390 O O   . LEU E 1 312 ? -16.395 13.305  24.427  1.00 49.15  ? 314 LEU E O   1 
ATOM   10391 C CB  . LEU E 1 312 ? -14.800 14.803  26.203  1.00 41.94  ? 314 LEU E CB  1 
ATOM   10392 C CG  . LEU E 1 312 ? -13.925 15.437  27.288  1.00 42.79  ? 314 LEU E CG  1 
ATOM   10393 C CD1 . LEU E 1 312 ? -12.701 16.089  26.672  1.00 31.46  ? 314 LEU E CD1 1 
ATOM   10394 C CD2 . LEU E 1 312 ? -14.721 16.434  28.114  1.00 27.27  ? 314 LEU E CD2 1 
ATOM   10395 N N   . VAL E 1 313 ? -18.144 13.284  25.842  1.00 44.58  ? 315 VAL E N   1 
ATOM   10396 C CA  . VAL E 1 313 ? -19.061 12.642  24.908  1.00 40.25  ? 315 VAL E CA  1 
ATOM   10397 C C   . VAL E 1 313 ? -19.964 13.706  24.301  1.00 39.26  ? 315 VAL E C   1 
ATOM   10398 O O   . VAL E 1 313 ? -20.762 14.334  25.008  1.00 39.27  ? 315 VAL E O   1 
ATOM   10399 C CB  . VAL E 1 313 ? -19.880 11.543  25.603  1.00 52.73  ? 315 VAL E CB  1 
ATOM   10400 C CG1 . VAL E 1 313 ? -20.636 10.719  24.578  1.00 38.48  ? 315 VAL E CG1 1 
ATOM   10401 C CG2 . VAL E 1 313 ? -18.967 10.655  26.452  1.00 32.71  ? 315 VAL E CG2 1 
ATOM   10402 N N   . LEU E 1 314 ? -19.842 13.902  22.988  1.00 39.24  ? 316 LEU E N   1 
ATOM   10403 C CA  . LEU E 1 314 ? -20.691 14.832  22.252  1.00 37.94  ? 316 LEU E CA  1 
ATOM   10404 C C   . LEU E 1 314 ? -21.910 14.102  21.714  1.00 34.07  ? 316 LEU E C   1 
ATOM   10405 O O   . LEU E 1 314 ? -21.780 13.058  21.067  1.00 42.62  ? 316 LEU E O   1 
ATOM   10406 C CB  . LEU E 1 314 ? -19.937 15.467  21.086  1.00 35.18  ? 316 LEU E CB  1 
ATOM   10407 C CG  . LEU E 1 314 ? -18.989 16.615  21.405  1.00 38.12  ? 316 LEU E CG  1 
ATOM   10408 C CD1 . LEU E 1 314 ? -18.263 17.011  20.140  1.00 35.90  ? 316 LEU E CD1 1 
ATOM   10409 C CD2 . LEU E 1 314 ? -19.746 17.789  22.003  1.00 33.61  ? 316 LEU E CD2 1 
ATOM   10410 N N   . ALA E 1 315 ? -23.089 14.656  21.967  1.00 39.44  ? 317 ALA E N   1 
ATOM   10411 C CA  . ALA E 1 315 ? -24.294 14.123  21.350  1.00 40.12  ? 317 ALA E CA  1 
ATOM   10412 C C   . ALA E 1 315 ? -24.272 14.441  19.862  1.00 39.26  ? 317 ALA E C   1 
ATOM   10413 O O   . ALA E 1 315 ? -24.132 15.605  19.474  1.00 43.96  ? 317 ALA E O   1 
ATOM   10414 C CB  . ALA E 1 315 ? -25.537 14.710  22.013  1.00 41.24  ? 317 ALA E CB  1 
ATOM   10415 N N   . THR E 1 316 ? -24.376 13.409  19.027  1.00 42.76  ? 318 THR E N   1 
ATOM   10416 C CA  . THR E 1 316 ? -24.492 13.595  17.589  1.00 47.64  ? 318 THR E CA  1 
ATOM   10417 C C   . THR E 1 316 ? -25.841 13.166  17.035  1.00 54.48  ? 318 THR E C   1 
ATOM   10418 O O   . THR E 1 316 ? -26.150 13.498  15.886  1.00 65.56  ? 318 THR E O   1 
ATOM   10419 C CB  . THR E 1 316 ? -23.384 12.831  16.854  1.00 49.10  ? 318 THR E CB  1 
ATOM   10420 O OG1 . THR E 1 316 ? -23.528 11.426  17.099  1.00 64.51  ? 318 THR E OG1 1 
ATOM   10421 C CG2 . THR E 1 316 ? -22.028 13.292  17.339  1.00 51.02  ? 318 THR E CG2 1 
ATOM   10422 N N   . GLY E 1 317 ? -26.650 12.445  17.814  1.00 54.38  ? 319 GLY E N   1 
ATOM   10423 C CA  . GLY E 1 317 ? -27.976 12.051  17.414  1.00 42.67  ? 319 GLY E CA  1 
ATOM   10424 C C   . GLY E 1 317 ? -29.059 12.776  18.186  1.00 45.91  ? 319 GLY E C   1 
ATOM   10425 O O   . GLY E 1 317 ? -28.838 13.838  18.783  1.00 45.53  ? 319 GLY E O   1 
ATOM   10426 N N   . LEU E 1 318 ? -30.246 12.181  18.192  1.00 45.44  ? 320 LEU E N   1 
ATOM   10427 C CA  . LEU E 1 318 ? -31.426 12.787  18.790  1.00 46.87  ? 320 LEU E CA  1 
ATOM   10428 C C   . LEU E 1 318 ? -31.631 12.284  20.213  1.00 41.79  ? 320 LEU E C   1 
ATOM   10429 O O   . LEU E 1 318 ? -31.083 11.258  20.620  1.00 38.18  ? 320 LEU E O   1 
ATOM   10430 C CB  . LEU E 1 318 ? -32.673 12.476  17.959  1.00 46.93  ? 320 LEU E CB  1 
ATOM   10431 C CG  . LEU E 1 318 ? -32.930 13.374  16.752  1.00 52.91  ? 320 LEU E CG  1 
ATOM   10432 C CD1 . LEU E 1 318 ? -31.967 13.049  15.621  1.00 62.03  ? 320 LEU E CD1 1 
ATOM   10433 C CD2 . LEU E 1 318 ? -34.355 13.207  16.290  1.00 58.18  ? 320 LEU E CD2 1 
ATOM   10434 N N   . ARG E 1 319 ? -32.433 13.028  20.970  1.00 31.53  ? 321 ARG E N   1 
ATOM   10435 C CA  . ARG E 1 319 ? -32.890 12.544  22.265  1.00 38.90  ? 321 ARG E CA  1 
ATOM   10436 C C   . ARG E 1 319 ? -33.728 11.285  22.076  1.00 51.72  ? 321 ARG E C   1 
ATOM   10437 O O   . ARG E 1 319 ? -34.639 11.249  21.243  1.00 50.88  ? 321 ARG E O   1 
ATOM   10438 C CB  . ARG E 1 319 ? -33.704 13.624  22.971  1.00 40.38  ? 321 ARG E CB  1 
ATOM   10439 C CG  . ARG E 1 319 ? -34.019 13.316  24.419  1.00 58.57  ? 321 ARG E CG  1 
ATOM   10440 C CD  . ARG E 1 319 ? -35.081 14.260  24.953  1.00 42.52  ? 321 ARG E CD  1 
ATOM   10441 N NE  . ARG E 1 319 ? -34.587 15.629  25.046  1.00 48.91  ? 321 ARG E NE  1 
ATOM   10442 C CZ  . ARG E 1 319 ? -34.101 16.176  26.151  1.00 54.18  ? 321 ARG E CZ  1 
ATOM   10443 N NH1 . ARG E 1 319 ? -34.024 15.495  27.283  1.00 50.50  ? 321 ARG E NH1 1 
ATOM   10444 N NH2 . ARG E 1 319 ? -33.680 17.439  26.120  1.00 50.97  ? 321 ARG E NH2 1 
ATOM   10445 N N   . ASN E 1 320 ? -33.420 10.251  22.850  1.00 55.58  ? 322 ASN E N   1 
ATOM   10446 C CA  . ASN E 1 320 ? -34.060 8.953   22.700  1.00 55.19  ? 322 ASN E CA  1 
ATOM   10447 C C   . ASN E 1 320 ? -35.141 8.750   23.756  1.00 54.59  ? 322 ASN E C   1 
ATOM   10448 O O   . ASN E 1 320 ? -35.197 9.447   24.772  1.00 65.79  ? 322 ASN E O   1 
ATOM   10449 C CB  . ASN E 1 320 ? -33.024 7.827   22.785  1.00 49.91  ? 322 ASN E CB  1 
ATOM   10450 C CG  . ASN E 1 320 ? -33.324 6.682   21.828  1.00 51.81  ? 322 ASN E CG  1 
ATOM   10451 O OD1 . ASN E 1 320 ? -34.430 6.568   21.306  1.00 55.24  ? 322 ASN E OD1 1 
ATOM   10452 N ND2 . ASN E 1 320 ? -32.339 5.822   21.608  1.00 66.87  ? 322 ASN E ND2 1 
ATOM   10453 N N   . SER E 1 321 ? -36.006 7.777   23.500  1.00 69.25  ? 323 SER E N   1 
ATOM   10454 C CA  . SER E 1 321 ? -37.082 7.453   24.428  1.00 77.36  ? 323 SER E CA  1 
ATOM   10455 C C   . SER E 1 321 ? -37.253 5.942   24.581  1.00 64.38  ? 323 SER E C   1 
ATOM   10456 O O   . SER E 1 321 ? -37.521 5.442   25.676  1.00 73.19  ? 323 SER E O   1 
ATOM   10457 C CB  . SER E 1 321 ? -38.387 8.103   23.962  1.00 80.68  ? 323 SER E CB  1 
ATOM   10458 O OG  . SER E 1 321 ? -38.456 8.141   22.545  1.00 68.48  ? 323 SER E OG  1 
ATOM   10459 N N   . GLY F 2 1   ? -38.058 20.753  24.948  1.00 56.11  ? 1   GLY F N   1 
ATOM   10460 C CA  . GLY F 2 1   ? -36.880 21.499  24.548  1.00 49.87  ? 1   GLY F CA  1 
ATOM   10461 C C   . GLY F 2 1   ? -37.193 22.957  24.280  1.00 56.29  ? 1   GLY F C   1 
ATOM   10462 O O   . GLY F 2 1   ? -38.282 23.428  24.605  1.00 53.19  ? 1   GLY F O   1 
ATOM   10463 N N   . LEU F 2 2   ? -36.235 23.669  23.681  1.00 49.81  ? 2   LEU F N   1 
ATOM   10464 C CA  . LEU F 2 2   ? -36.425 25.091  23.414  1.00 42.79  ? 2   LEU F CA  1 
ATOM   10465 C C   . LEU F 2 2   ? -37.602 25.328  22.475  1.00 50.30  ? 2   LEU F C   1 
ATOM   10466 O O   . LEU F 2 2   ? -38.395 26.255  22.681  1.00 53.28  ? 2   LEU F O   1 
ATOM   10467 C CB  . LEU F 2 2   ? -35.149 25.689  22.824  1.00 52.55  ? 2   LEU F CB  1 
ATOM   10468 C CG  . LEU F 2 2   ? -34.098 26.231  23.793  1.00 56.09  ? 2   LEU F CG  1 
ATOM   10469 C CD1 . LEU F 2 2   ? -33.031 26.996  23.027  1.00 42.24  ? 2   LEU F CD1 1 
ATOM   10470 C CD2 . LEU F 2 2   ? -34.736 27.109  24.862  1.00 32.84  ? 2   LEU F CD2 1 
ATOM   10471 N N   . PHE F 2 3   ? -37.735 24.505  21.441  1.00 51.62  ? 3   PHE F N   1 
ATOM   10472 C CA  . PHE F 2 3   ? -38.769 24.696  20.436  1.00 50.12  ? 3   PHE F CA  1 
ATOM   10473 C C   . PHE F 2 3   ? -40.015 23.862  20.694  1.00 50.29  ? 3   PHE F C   1 
ATOM   10474 O O   . PHE F 2 3   ? -40.960 23.926  19.903  1.00 51.41  ? 3   PHE F O   1 
ATOM   10475 C CB  . PHE F 2 3   ? -38.192 24.414  19.048  1.00 39.78  ? 3   PHE F CB  1 
ATOM   10476 C CG  . PHE F 2 3   ? -37.020 25.290  18.724  1.00 53.58  ? 3   PHE F CG  1 
ATOM   10477 C CD1 . PHE F 2 3   ? -35.733 24.920  19.096  1.00 45.33  ? 3   PHE F CD1 1 
ATOM   10478 C CD2 . PHE F 2 3   ? -37.209 26.518  18.110  1.00 47.18  ? 3   PHE F CD2 1 
ATOM   10479 C CE1 . PHE F 2 3   ? -34.658 25.743  18.827  1.00 36.85  ? 3   PHE F CE1 1 
ATOM   10480 C CE2 . PHE F 2 3   ? -36.132 27.347  17.840  1.00 47.29  ? 3   PHE F CE2 1 
ATOM   10481 C CZ  . PHE F 2 3   ? -34.857 26.956  18.198  1.00 48.22  ? 3   PHE F CZ  1 
ATOM   10482 N N   . GLY F 2 4   ? -40.045 23.098  21.784  1.00 56.10  ? 4   GLY F N   1 
ATOM   10483 C CA  . GLY F 2 4   ? -41.275 22.511  22.271  1.00 46.79  ? 4   GLY F CA  1 
ATOM   10484 C C   . GLY F 2 4   ? -41.803 21.326  21.498  1.00 45.09  ? 4   GLY F C   1 
ATOM   10485 O O   . GLY F 2 4   ? -42.888 20.840  21.824  1.00 48.65  ? 4   GLY F O   1 
ATOM   10486 N N   . ALA F 2 5   ? -41.075 20.827  20.499  1.00 51.97  ? 5   ALA F N   1 
ATOM   10487 C CA  . ALA F 2 5   ? -41.577 19.714  19.696  1.00 51.78  ? 5   ALA F CA  1 
ATOM   10488 C C   . ALA F 2 5   ? -41.119 18.361  20.240  1.00 52.88  ? 5   ALA F C   1 
ATOM   10489 O O   . ALA F 2 5   ? -41.949 17.526  20.615  1.00 53.66  ? 5   ALA F O   1 
ATOM   10490 C CB  . ALA F 2 5   ? -41.149 19.882  18.233  1.00 41.20  ? 5   ALA F CB  1 
ATOM   10491 N N   . ILE F 2 6   ? -39.805 18.134  20.299  1.00 47.96  ? 6   ILE F N   1 
ATOM   10492 C CA  . ILE F 2 6   ? -39.292 16.859  20.785  1.00 48.84  ? 6   ILE F CA  1 
ATOM   10493 C C   . ILE F 2 6   ? -39.496 16.780  22.291  1.00 57.03  ? 6   ILE F C   1 
ATOM   10494 O O   . ILE F 2 6   ? -39.080 17.677  23.038  1.00 61.78  ? 6   ILE F O   1 
ATOM   10495 C CB  . ILE F 2 6   ? -37.815 16.690  20.402  1.00 52.93  ? 6   ILE F CB  1 
ATOM   10496 C CG1 . ILE F 2 6   ? -37.700 16.320  18.919  1.00 49.59  ? 6   ILE F CG1 1 
ATOM   10497 C CG2 . ILE F 2 6   ? -37.153 15.637  21.283  1.00 36.04  ? 6   ILE F CG2 1 
ATOM   10498 C CD1 . ILE F 2 6   ? -36.285 16.259  18.386  1.00 36.03  ? 6   ILE F CD1 1 
ATOM   10499 N N   . ALA F 2 7   ? -40.153 15.712  22.742  1.00 63.04  ? 7   ALA F N   1 
ATOM   10500 C CA  . ALA F 2 7   ? -40.621 15.546  24.116  1.00 64.40  ? 7   ALA F CA  1 
ATOM   10501 C C   . ALA F 2 7   ? -41.558 16.666  24.554  1.00 63.37  ? 7   ALA F C   1 
ATOM   10502 O O   . ALA F 2 7   ? -41.811 16.822  25.753  1.00 88.84  ? 7   ALA F O   1 
ATOM   10503 C CB  . ALA F 2 7   ? -39.454 15.423  25.106  1.00 60.07  ? 7   ALA F CB  1 
ATOM   10504 N N   . GLY F 2 8   ? -42.072 17.454  23.611  1.00 64.35  ? 8   GLY F N   1 
ATOM   10505 C CA  . GLY F 2 8   ? -43.059 18.474  23.903  1.00 50.89  ? 8   GLY F CA  1 
ATOM   10506 C C   . GLY F 2 8   ? -44.445 17.998  23.528  1.00 65.18  ? 8   GLY F C   1 
ATOM   10507 O O   . GLY F 2 8   ? -44.972 17.079  24.163  1.00 73.98  ? 8   GLY F O   1 
ATOM   10508 N N   . PHE F 2 9   ? -45.049 18.591  22.495  1.00 55.89  ? 9   PHE F N   1 
ATOM   10509 C CA  . PHE F 2 9   ? -46.329 18.066  22.038  1.00 59.64  ? 9   PHE F CA  1 
ATOM   10510 C C   . PHE F 2 9   ? -46.150 16.743  21.302  1.00 62.45  ? 9   PHE F C   1 
ATOM   10511 O O   . PHE F 2 9   ? -47.068 15.916  21.290  1.00 60.50  ? 9   PHE F O   1 
ATOM   10512 C CB  . PHE F 2 9   ? -47.072 19.088  21.169  1.00 63.63  ? 9   PHE F CB  1 
ATOM   10513 C CG  . PHE F 2 9   ? -46.264 19.652  20.033  1.00 62.35  ? 9   PHE F CG  1 
ATOM   10514 C CD1 . PHE F 2 9   ? -45.484 20.780  20.214  1.00 57.14  ? 9   PHE F CD1 1 
ATOM   10515 C CD2 . PHE F 2 9   ? -46.319 19.077  18.773  1.00 60.62  ? 9   PHE F CD2 1 
ATOM   10516 C CE1 . PHE F 2 9   ? -44.750 21.309  19.168  1.00 65.14  ? 9   PHE F CE1 1 
ATOM   10517 C CE2 . PHE F 2 9   ? -45.590 19.601  17.721  1.00 60.04  ? 9   PHE F CE2 1 
ATOM   10518 C CZ  . PHE F 2 9   ? -44.805 20.718  17.917  1.00 64.82  ? 9   PHE F CZ  1 
ATOM   10519 N N   . ILE F 2 10  ? -44.980 16.509  20.707  1.00 57.01  ? 10  ILE F N   1 
ATOM   10520 C CA  . ILE F 2 10  ? -44.667 15.220  20.099  1.00 54.50  ? 10  ILE F CA  1 
ATOM   10521 C C   . ILE F 2 10  ? -44.043 14.355  21.187  1.00 53.80  ? 10  ILE F C   1 
ATOM   10522 O O   . ILE F 2 10  ? -42.872 14.514  21.537  1.00 64.33  ? 10  ILE F O   1 
ATOM   10523 C CB  . ILE F 2 10  ? -43.750 15.359  18.885  1.00 59.07  ? 10  ILE F CB  1 
ATOM   10524 C CG1 . ILE F 2 10  ? -44.413 16.228  17.820  1.00 59.66  ? 10  ILE F CG1 1 
ATOM   10525 C CG2 . ILE F 2 10  ? -43.425 13.984  18.307  1.00 51.07  ? 10  ILE F CG2 1 
ATOM   10526 C CD1 . ILE F 2 10  ? -43.435 16.813  16.843  1.00 51.56  ? 10  ILE F CD1 1 
ATOM   10527 N N   . GLU F 2 11  ? -44.835 13.433  21.722  1.00 59.58  ? 11  GLU F N   1 
ATOM   10528 C CA  . GLU F 2 11  ? -44.406 12.586  22.829  1.00 62.31  ? 11  GLU F CA  1 
ATOM   10529 C C   . GLU F 2 11  ? -43.640 11.392  22.269  1.00 77.59  ? 11  GLU F C   1 
ATOM   10530 O O   . GLU F 2 11  ? -44.225 10.517  21.619  1.00 92.36  ? 11  GLU F O   1 
ATOM   10531 C CB  . GLU F 2 11  ? -45.625 12.144  23.640  1.00 68.79  ? 11  GLU F CB  1 
ATOM   10532 C CG  . GLU F 2 11  ? -45.312 11.234  24.820  1.00 91.13  ? 11  GLU F CG  1 
ATOM   10533 C CD  . GLU F 2 11  ? -44.067 11.656  25.575  1.00 105.42 ? 11  GLU F CD  1 
ATOM   10534 O OE1 . GLU F 2 11  ? -44.024 12.806  26.068  1.00 113.83 ? 11  GLU F OE1 1 
ATOM   10535 O OE2 . GLU F 2 11  ? -43.135 10.832  25.682  1.00 96.76  ? 11  GLU F OE2 1 
ATOM   10536 N N   . GLY F 2 12  ? -42.335 11.365  22.499  1.00 52.60  ? 12  GLY F N   1 
ATOM   10537 C CA  . GLY F 2 12  ? -41.516 10.213  22.172  1.00 59.06  ? 12  GLY F CA  1 
ATOM   10538 C C   . GLY F 2 12  ? -41.242 10.089  20.679  1.00 57.35  ? 12  GLY F C   1 
ATOM   10539 O O   . GLY F 2 12  ? -41.978 10.555  19.817  1.00 54.22  ? 12  GLY F O   1 
ATOM   10540 N N   . GLY F 2 13  ? -40.125 9.406   20.383  1.00 57.98  ? 13  GLY F N   1 
ATOM   10541 C CA  . GLY F 2 13  ? -39.718 9.136   19.019  1.00 44.62  ? 13  GLY F CA  1 
ATOM   10542 C C   . GLY F 2 13  ? -40.348 7.864   18.466  1.00 49.61  ? 13  GLY F C   1 
ATOM   10543 O O   . GLY F 2 13  ? -41.135 7.182   19.123  1.00 47.46  ? 13  GLY F O   1 
ATOM   10544 N N   . TRP F 2 14  ? -39.977 7.547   17.226  1.00 48.66  ? 14  TRP F N   1 
ATOM   10545 C CA  . TRP F 2 14  ? -40.544 6.421   16.486  1.00 37.66  ? 14  TRP F CA  1 
ATOM   10546 C C   . TRP F 2 14  ? -39.471 5.366   16.257  1.00 50.32  ? 14  TRP F C   1 
ATOM   10547 O O   . TRP F 2 14  ? -38.568 5.564   15.437  1.00 41.09  ? 14  TRP F O   1 
ATOM   10548 C CB  . TRP F 2 14  ? -41.107 6.874   15.141  1.00 52.87  ? 14  TRP F CB  1 
ATOM   10549 C CG  . TRP F 2 14  ? -42.367 7.647   15.222  1.00 48.41  ? 14  TRP F CG  1 
ATOM   10550 C CD1 . TRP F 2 14  ? -43.311 7.585   16.206  1.00 42.46  ? 14  TRP F CD1 1 
ATOM   10551 C CD2 . TRP F 2 14  ? -42.843 8.596   14.264  1.00 43.18  ? 14  TRP F CD2 1 
ATOM   10552 N NE1 . TRP F 2 14  ? -44.342 8.445   15.920  1.00 39.46  ? 14  TRP F NE1 1 
ATOM   10553 C CE2 . TRP F 2 14  ? -44.078 9.076   14.732  1.00 35.13  ? 14  TRP F CE2 1 
ATOM   10554 C CE3 . TRP F 2 14  ? -42.340 9.088   13.056  1.00 43.48  ? 14  TRP F CE3 1 
ATOM   10555 C CZ2 . TRP F 2 14  ? -44.819 10.025  14.035  1.00 42.24  ? 14  TRP F CZ2 1 
ATOM   10556 C CZ3 . TRP F 2 14  ? -43.080 10.027  12.363  1.00 32.58  ? 14  TRP F CZ3 1 
ATOM   10557 C CH2 . TRP F 2 14  ? -44.303 10.488  12.856  1.00 36.44  ? 14  TRP F CH2 1 
ATOM   10558 N N   . GLN F 2 15  ? -39.591 4.229   16.949  1.00 55.12  ? 15  GLN F N   1 
ATOM   10559 C CA  . GLN F 2 15  ? -38.712 3.105   16.645  1.00 56.68  ? 15  GLN F CA  1 
ATOM   10560 C C   . GLN F 2 15  ? -38.945 2.593   15.230  1.00 59.35  ? 15  GLN F C   1 
ATOM   10561 O O   . GLN F 2 15  ? -38.017 2.074   14.598  1.00 44.69  ? 15  GLN F O   1 
ATOM   10562 C CB  . GLN F 2 15  ? -38.919 1.978   17.658  1.00 53.99  ? 15  GLN F CB  1 
ATOM   10563 C CG  . GLN F 2 15  ? -38.491 2.325   19.079  1.00 69.81  ? 15  GLN F CG  1 
ATOM   10564 C CD  . GLN F 2 15  ? -36.987 2.174   19.296  1.00 71.49  ? 15  GLN F CD  1 
ATOM   10565 O OE1 . GLN F 2 15  ? -36.339 1.314   18.693  1.00 59.88  ? 15  GLN F OE1 1 
ATOM   10566 N NE2 . GLN F 2 15  ? -36.430 3.013   20.163  1.00 65.74  ? 15  GLN F NE2 1 
ATOM   10567 N N   . GLY F 2 16  ? -40.167 2.754   14.711  1.00 52.77  ? 16  GLY F N   1 
ATOM   10568 C CA  . GLY F 2 16  ? -40.523 2.228   13.406  1.00 49.62  ? 16  GLY F CA  1 
ATOM   10569 C C   . GLY F 2 16  ? -39.962 3.006   12.235  1.00 56.28  ? 16  GLY F C   1 
ATOM   10570 O O   . GLY F 2 16  ? -39.931 2.479   11.117  1.00 66.13  ? 16  GLY F O   1 
ATOM   10571 N N   . MET F 2 17  ? -39.527 4.244   12.453  1.00 62.80  ? 17  MET F N   1 
ATOM   10572 C CA  . MET F 2 17  ? -38.863 5.016   11.409  1.00 69.81  ? 17  MET F CA  1 
ATOM   10573 C C   . MET F 2 17  ? -37.362 4.758   11.468  1.00 66.99  ? 17  MET F C   1 
ATOM   10574 O O   . MET F 2 17  ? -36.716 5.061   12.476  1.00 66.87  ? 17  MET F O   1 
ATOM   10575 C CB  . MET F 2 17  ? -39.144 6.507   11.558  1.00 63.81  ? 17  MET F CB  1 
ATOM   10576 C CG  . MET F 2 17  ? -38.449 7.333   10.498  1.00 69.98  ? 17  MET F CG  1 
ATOM   10577 S SD  . MET F 2 17  ? -38.657 9.084   10.789  1.00 66.08  ? 17  MET F SD  1 
ATOM   10578 C CE  . MET F 2 17  ? -40.189 9.300   9.907   1.00 60.85  ? 17  MET F CE  1 
ATOM   10579 N N   . VAL F 2 18  ? -36.807 4.218   10.382  1.00 67.31  ? 18  VAL F N   1 
ATOM   10580 C CA  . VAL F 2 18  ? -35.415 3.779   10.365  1.00 61.12  ? 18  VAL F CA  1 
ATOM   10581 C C   . VAL F 2 18  ? -34.635 4.444   9.236   1.00 58.54  ? 18  VAL F C   1 
ATOM   10582 O O   . VAL F 2 18  ? -33.401 4.384   9.210   1.00 76.55  ? 18  VAL F O   1 
ATOM   10583 C CB  . VAL F 2 18  ? -35.328 2.245   10.248  1.00 71.42  ? 18  VAL F CB  1 
ATOM   10584 C CG1 . VAL F 2 18  ? -36.340 1.577   11.170  1.00 55.38  ? 18  VAL F CG1 1 
ATOM   10585 C CG2 . VAL F 2 18  ? -35.548 1.806   8.806   1.00 57.23  ? 18  VAL F CG2 1 
ATOM   10586 N N   . ASP F 2 19  ? -35.340 5.083   8.301   1.00 65.00  ? 19  ASP F N   1 
ATOM   10587 C CA  . ASP F 2 19  ? -34.724 5.619   7.091   1.00 68.01  ? 19  ASP F CA  1 
ATOM   10588 C C   . ASP F 2 19  ? -34.256 7.068   7.225   1.00 70.18  ? 19  ASP F C   1 
ATOM   10589 O O   . ASP F 2 19  ? -33.688 7.604   6.266   1.00 71.61  ? 19  ASP F O   1 
ATOM   10590 C CB  . ASP F 2 19  ? -35.692 5.495   5.897   1.00 65.37  ? 19  ASP F CB  1 
ATOM   10591 C CG  . ASP F 2 19  ? -37.148 5.798   6.269   1.00 89.36  ? 19  ASP F CG  1 
ATOM   10592 O OD1 . ASP F 2 19  ? -37.548 5.543   7.426   1.00 88.15  ? 19  ASP F OD1 1 
ATOM   10593 O OD2 . ASP F 2 19  ? -37.902 6.281   5.393   1.00 82.22  ? 19  ASP F OD2 1 
ATOM   10594 N N   . GLY F 2 20  ? -34.461 7.710   8.372   1.00 65.74  ? 20  GLY F N   1 
ATOM   10595 C CA  . GLY F 2 20  ? -34.057 9.099   8.515   1.00 49.96  ? 20  GLY F CA  1 
ATOM   10596 C C   . GLY F 2 20  ? -34.199 9.579   9.945   1.00 49.19  ? 20  GLY F C   1 
ATOM   10597 O O   . GLY F 2 20  ? -34.652 8.849   10.830  1.00 58.44  ? 20  GLY F O   1 
ATOM   10598 N N   . TRP F 2 21  ? -33.796 10.833  10.162  1.00 50.70  ? 21  TRP F N   1 
ATOM   10599 C CA  . TRP F 2 21  ? -33.860 11.412  11.501  1.00 49.55  ? 21  TRP F CA  1 
ATOM   10600 C C   . TRP F 2 21  ? -35.237 11.999  11.790  1.00 41.93  ? 21  TRP F C   1 
ATOM   10601 O O   . TRP F 2 21  ? -35.748 11.865  12.908  1.00 41.04  ? 21  TRP F O   1 
ATOM   10602 C CB  . TRP F 2 21  ? -32.778 12.482  11.672  1.00 42.27  ? 21  TRP F CB  1 
ATOM   10603 C CG  . TRP F 2 21  ? -31.477 11.945  12.169  1.00 56.36  ? 21  TRP F CG  1 
ATOM   10604 C CD1 . TRP F 2 21  ? -31.209 10.660  12.551  1.00 63.57  ? 21  TRP F CD1 1 
ATOM   10605 C CD2 . TRP F 2 21  ? -30.256 12.675  12.336  1.00 56.35  ? 21  TRP F CD2 1 
ATOM   10606 N NE1 . TRP F 2 21  ? -29.897 10.548  12.948  1.00 65.14  ? 21  TRP F NE1 1 
ATOM   10607 C CE2 . TRP F 2 21  ? -29.291 11.772  12.825  1.00 50.70  ? 21  TRP F CE2 1 
ATOM   10608 C CE3 . TRP F 2 21  ? -29.886 14.006  12.121  1.00 51.10  ? 21  TRP F CE3 1 
ATOM   10609 C CZ2 . TRP F 2 21  ? -27.980 12.157  13.101  1.00 45.83  ? 21  TRP F CZ2 1 
ATOM   10610 C CZ3 . TRP F 2 21  ? -28.582 14.386  12.398  1.00 51.33  ? 21  TRP F CZ3 1 
ATOM   10611 C CH2 . TRP F 2 21  ? -27.647 13.466  12.882  1.00 49.16  ? 21  TRP F CH2 1 
ATOM   10612 N N   . TYR F 2 22  ? -35.842 12.656  10.806  1.00 35.47  ? 22  TYR F N   1 
ATOM   10613 C CA  . TYR F 2 22  ? -37.170 13.233  10.949  1.00 38.85  ? 22  TYR F CA  1 
ATOM   10614 C C   . TYR F 2 22  ? -38.021 12.841  9.752   1.00 41.82  ? 22  TYR F C   1 
ATOM   10615 O O   . TYR F 2 22  ? -37.515 12.585  8.658   1.00 53.08  ? 22  TYR F O   1 
ATOM   10616 C CB  . TYR F 2 22  ? -37.126 14.762  11.059  1.00 36.01  ? 22  TYR F CB  1 
ATOM   10617 C CG  . TYR F 2 22  ? -35.843 15.326  11.636  1.00 38.90  ? 22  TYR F CG  1 
ATOM   10618 C CD1 . TYR F 2 22  ? -35.521 15.140  12.973  1.00 31.16  ? 22  TYR F CD1 1 
ATOM   10619 C CD2 . TYR F 2 22  ? -34.968 16.061  10.848  1.00 41.51  ? 22  TYR F CD2 1 
ATOM   10620 C CE1 . TYR F 2 22  ? -34.362 15.657  13.506  1.00 43.62  ? 22  TYR F CE1 1 
ATOM   10621 C CE2 . TYR F 2 22  ? -33.799 16.587  11.378  1.00 44.33  ? 22  TYR F CE2 1 
ATOM   10622 C CZ  . TYR F 2 22  ? -33.505 16.382  12.709  1.00 39.92  ? 22  TYR F CZ  1 
ATOM   10623 O OH  . TYR F 2 22  ? -32.347 16.896  13.250  1.00 50.66  ? 22  TYR F OH  1 
ATOM   10624 N N   . GLY F 2 23  ? -39.329 12.808  9.965   1.00 33.61  ? 23  GLY F N   1 
ATOM   10625 C CA  . GLY F 2 23  ? -40.217 12.553  8.844   1.00 41.39  ? 23  GLY F CA  1 
ATOM   10626 C C   . GLY F 2 23  ? -41.652 12.398  9.288   1.00 43.77  ? 23  GLY F C   1 
ATOM   10627 O O   . GLY F 2 23  ? -42.069 12.953  10.313  1.00 39.51  ? 23  GLY F O   1 
ATOM   10628 N N   . TYR F 2 24  ? -42.398 11.619  8.509   1.00 42.70  ? 24  TYR F N   1 
ATOM   10629 C CA  . TYR F 2 24  ? -43.846 11.569  8.618   1.00 42.88  ? 24  TYR F CA  1 
ATOM   10630 C C   . TYR F 2 24  ? -44.327 10.136  8.788   1.00 48.87  ? 24  TYR F C   1 
ATOM   10631 O O   . TYR F 2 24  ? -43.697 9.184   8.315   1.00 46.80  ? 24  TYR F O   1 
ATOM   10632 C CB  . TYR F 2 24  ? -44.523 12.182  7.381   1.00 33.93  ? 24  TYR F CB  1 
ATOM   10633 C CG  . TYR F 2 24  ? -43.863 13.444  6.856   1.00 39.76  ? 24  TYR F CG  1 
ATOM   10634 C CD1 . TYR F 2 24  ? -42.785 13.378  5.982   1.00 43.01  ? 24  TYR F CD1 1 
ATOM   10635 C CD2 . TYR F 2 24  ? -44.327 14.701  7.226   1.00 38.22  ? 24  TYR F CD2 1 
ATOM   10636 C CE1 . TYR F 2 24  ? -42.180 14.525  5.499   1.00 43.43  ? 24  TYR F CE1 1 
ATOM   10637 C CE2 . TYR F 2 24  ? -43.731 15.857  6.741   1.00 41.65  ? 24  TYR F CE2 1 
ATOM   10638 C CZ  . TYR F 2 24  ? -42.656 15.760  5.879   1.00 50.41  ? 24  TYR F CZ  1 
ATOM   10639 O OH  . TYR F 2 24  ? -42.049 16.897  5.390   1.00 58.17  ? 24  TYR F OH  1 
ATOM   10640 N N   . HIS F 2 25  ? -45.449 10.001  9.487   1.00 39.10  ? 25  HIS F N   1 
ATOM   10641 C CA  . HIS F 2 25  ? -46.247 8.786   9.484   1.00 47.44  ? 25  HIS F CA  1 
ATOM   10642 C C   . HIS F 2 25  ? -47.652 9.136   9.011   1.00 47.10  ? 25  HIS F C   1 
ATOM   10643 O O   . HIS F 2 25  ? -48.200 10.179  9.385   1.00 41.11  ? 25  HIS F O   1 
ATOM   10644 C CB  . HIS F 2 25  ? -46.304 8.130   10.866  1.00 38.99  ? 25  HIS F CB  1 
ATOM   10645 C CG  . HIS F 2 25  ? -47.177 6.915   10.911  1.00 48.65  ? 25  HIS F CG  1 
ATOM   10646 N ND1 . HIS F 2 25  ? -46.753 5.677   10.477  1.00 52.52  ? 25  HIS F ND1 1 
ATOM   10647 C CD2 . HIS F 2 25  ? -48.459 6.752   11.314  1.00 50.46  ? 25  HIS F CD2 1 
ATOM   10648 C CE1 . HIS F 2 25  ? -47.731 4.802   10.621  1.00 49.99  ? 25  HIS F CE1 1 
ATOM   10649 N NE2 . HIS F 2 25  ? -48.778 5.429   11.126  1.00 48.14  ? 25  HIS F NE2 1 
ATOM   10650 N N   . HIS F 2 26  ? -48.223 8.279   8.170   1.00 37.47  ? 26  HIS F N   1 
ATOM   10651 C CA  . HIS F 2 26  ? -49.533 8.524   7.583   1.00 44.29  ? 26  HIS F CA  1 
ATOM   10652 C C   . HIS F 2 26  ? -50.432 7.322   7.815   1.00 39.90  ? 26  HIS F C   1 
ATOM   10653 O O   . HIS F 2 26  ? -49.966 6.196   7.990   1.00 49.95  ? 26  HIS F O   1 
ATOM   10654 C CB  . HIS F 2 26  ? -49.443 8.809   6.074   1.00 45.34  ? 26  HIS F CB  1 
ATOM   10655 C CG  . HIS F 2 26  ? -49.310 7.574   5.235   1.00 57.04  ? 26  HIS F CG  1 
ATOM   10656 N ND1 . HIS F 2 26  ? -48.101 6.950   5.014   1.00 54.81  ? 26  HIS F ND1 1 
ATOM   10657 C CD2 . HIS F 2 26  ? -50.236 6.848   4.564   1.00 56.80  ? 26  HIS F CD2 1 
ATOM   10658 C CE1 . HIS F 2 26  ? -48.288 5.892   4.245   1.00 53.17  ? 26  HIS F CE1 1 
ATOM   10659 N NE2 . HIS F 2 26  ? -49.575 5.808   3.957   1.00 66.91  ? 26  HIS F NE2 1 
ATOM   10660 N N   . SER F 2 27  ? -51.734 7.577   7.807   1.00 44.80  ? 27  SER F N   1 
ATOM   10661 C CA  . SER F 2 27  ? -52.714 6.510   7.957   1.00 45.90  ? 27  SER F CA  1 
ATOM   10662 C C   . SER F 2 27  ? -53.975 6.909   7.210   1.00 42.05  ? 27  SER F C   1 
ATOM   10663 O O   . SER F 2 27  ? -54.557 7.959   7.494   1.00 49.87  ? 27  SER F O   1 
ATOM   10664 C CB  . SER F 2 27  ? -53.014 6.247   9.434   1.00 45.84  ? 27  SER F CB  1 
ATOM   10665 O OG  . SER F 2 27  ? -54.006 5.246   9.585   1.00 55.22  ? 27  SER F OG  1 
ATOM   10666 N N   . ASN F 2 28  ? -54.379 6.088   6.246   1.00 49.99  ? 28  ASN F N   1 
ATOM   10667 C CA  . ASN F 2 28  ? -55.627 6.289   5.522   1.00 52.93  ? 28  ASN F CA  1 
ATOM   10668 C C   . ASN F 2 28  ? -56.249 4.915   5.293   1.00 45.68  ? 28  ASN F C   1 
ATOM   10669 O O   . ASN F 2 28  ? -55.845 3.923   5.907   1.00 48.43  ? 28  ASN F O   1 
ATOM   10670 C CB  . ASN F 2 28  ? -55.389 7.071   4.221   1.00 36.12  ? 28  ASN F CB  1 
ATOM   10671 C CG  . ASN F 2 28  ? -54.333 6.435   3.338   1.00 47.42  ? 28  ASN F CG  1 
ATOM   10672 O OD1 . ASN F 2 28  ? -54.111 5.223   3.386   1.00 46.18  ? 28  ASN F OD1 1 
ATOM   10673 N ND2 . ASN F 2 28  ? -53.677 7.252   2.521   1.00 42.02  ? 28  ASN F ND2 1 
ATOM   10674 N N   . GLU F 2 29  ? -57.240 4.849   4.399   1.00 46.42  ? 29  GLU F N   1 
ATOM   10675 C CA  . GLU F 2 29  ? -57.914 3.580   4.144   1.00 51.56  ? 29  GLU F CA  1 
ATOM   10676 C C   . GLU F 2 29  ? -57.041 2.606   3.362   1.00 54.49  ? 29  GLU F C   1 
ATOM   10677 O O   . GLU F 2 29  ? -57.254 1.393   3.461   1.00 57.12  ? 29  GLU F O   1 
ATOM   10678 C CB  . GLU F 2 29  ? -59.235 3.816   3.408   1.00 55.88  ? 29  GLU F CB  1 
ATOM   10679 C CG  . GLU F 2 29  ? -59.099 4.370   1.997   1.00 67.82  ? 29  GLU F CG  1 
ATOM   10680 C CD  . GLU F 2 29  ? -60.396 4.987   1.488   1.00 82.45  ? 29  GLU F CD  1 
ATOM   10681 O OE1 . GLU F 2 29  ? -61.481 4.579   1.961   1.00 72.04  ? 29  GLU F OE1 1 
ATOM   10682 O OE2 . GLU F 2 29  ? -60.330 5.888   0.623   1.00 82.85  ? 29  GLU F OE2 1 
ATOM   10683 N N   . GLN F 2 30  ? -56.059 3.099   2.602   1.00 49.23  ? 30  GLN F N   1 
ATOM   10684 C CA  . GLN F 2 30  ? -55.168 2.193   1.885   1.00 50.52  ? 30  GLN F CA  1 
ATOM   10685 C C   . GLN F 2 30  ? -54.167 1.529   2.825   1.00 47.92  ? 30  GLN F C   1 
ATOM   10686 O O   . GLN F 2 30  ? -53.842 0.349   2.656   1.00 54.24  ? 30  GLN F O   1 
ATOM   10687 C CB  . GLN F 2 30  ? -54.438 2.933   0.767   1.00 46.32  ? 30  GLN F CB  1 
ATOM   10688 C CG  . GLN F 2 30  ? -55.260 4.000   0.086   1.00 56.06  ? 30  GLN F CG  1 
ATOM   10689 C CD  . GLN F 2 30  ? -54.484 4.697   -1.011  1.00 74.11  ? 30  GLN F CD  1 
ATOM   10690 O OE1 . GLN F 2 30  ? -54.441 5.927   -1.076  1.00 71.95  ? 30  GLN F OE1 1 
ATOM   10691 N NE2 . GLN F 2 30  ? -53.857 3.911   -1.880  1.00 65.85  ? 30  GLN F NE2 1 
ATOM   10692 N N   . GLY F 2 31  ? -53.663 2.260   3.812   1.00 51.13  ? 31  GLY F N   1 
ATOM   10693 C CA  . GLY F 2 31  ? -52.687 1.684   4.719   1.00 49.23  ? 31  GLY F CA  1 
ATOM   10694 C C   . GLY F 2 31  ? -51.987 2.758   5.528   1.00 44.64  ? 31  GLY F C   1 
ATOM   10695 O O   . GLY F 2 31  ? -52.446 3.898   5.600   1.00 48.57  ? 31  GLY F O   1 
ATOM   10696 N N   . SER F 2 32  ? -50.869 2.368   6.136   1.00 51.39  ? 32  SER F N   1 
ATOM   10697 C CA  . SER F 2 32  ? -50.088 3.268   6.968   1.00 49.42  ? 32  SER F CA  1 
ATOM   10698 C C   . SER F 2 32  ? -48.607 2.981   6.767   1.00 49.49  ? 32  SER F C   1 
ATOM   10699 O O   . SER F 2 32  ? -48.225 1.900   6.316   1.00 51.40  ? 32  SER F O   1 
ATOM   10700 C CB  . SER F 2 32  ? -50.472 3.131   8.450   1.00 45.88  ? 32  SER F CB  1 
ATOM   10701 O OG  . SER F 2 32  ? -50.079 1.877   8.964   1.00 39.80  ? 32  SER F OG  1 
ATOM   10702 N N   . GLY F 2 33  ? -47.775 3.966   7.097   1.00 55.71  ? 33  GLY F N   1 
ATOM   10703 C CA  . GLY F 2 33  ? -46.337 3.790   6.978   1.00 51.61  ? 33  GLY F CA  1 
ATOM   10704 C C   . GLY F 2 33  ? -45.583 5.065   7.290   1.00 53.61  ? 33  GLY F C   1 
ATOM   10705 O O   . GLY F 2 33  ? -46.149 6.160   7.350   1.00 54.42  ? 33  GLY F O   1 
ATOM   10706 N N   . TYR F 2 34  ? -44.273 4.901   7.474   1.00 55.14  ? 34  TYR F N   1 
ATOM   10707 C CA  . TYR F 2 34  ? -43.356 5.999   7.746   1.00 36.72  ? 34  TYR F CA  1 
ATOM   10708 C C   . TYR F 2 34  ? -42.650 6.438   6.467   1.00 45.21  ? 34  TYR F C   1 
ATOM   10709 O O   . TYR F 2 34  ? -42.326 5.619   5.603   1.00 46.08  ? 34  TYR F O   1 
ATOM   10710 C CB  . TYR F 2 34  ? -42.301 5.598   8.781   1.00 39.59  ? 34  TYR F CB  1 
ATOM   10711 C CG  . TYR F 2 34  ? -42.846 5.114   10.104  1.00 41.62  ? 34  TYR F CG  1 
ATOM   10712 C CD1 . TYR F 2 34  ? -43.177 6.009   11.111  1.00 38.70  ? 34  TYR F CD1 1 
ATOM   10713 C CD2 . TYR F 2 34  ? -43.011 3.756   10.353  1.00 43.84  ? 34  TYR F CD2 1 
ATOM   10714 C CE1 . TYR F 2 34  ? -43.674 5.568   12.326  1.00 42.26  ? 34  TYR F CE1 1 
ATOM   10715 C CE2 . TYR F 2 34  ? -43.505 3.304   11.563  1.00 34.82  ? 34  TYR F CE2 1 
ATOM   10716 C CZ  . TYR F 2 34  ? -43.835 4.213   12.544  1.00 47.06  ? 34  TYR F CZ  1 
ATOM   10717 O OH  . TYR F 2 34  ? -44.324 3.765   13.747  1.00 57.15  ? 34  TYR F OH  1 
ATOM   10718 N N   . ALA F 2 35  ? -42.402 7.743   6.357   1.00 41.35  ? 35  ALA F N   1 
ATOM   10719 C CA  . ALA F 2 35  ? -41.598 8.288   5.269   1.00 49.50  ? 35  ALA F CA  1 
ATOM   10720 C C   . ALA F 2 35  ? -40.647 9.327   5.837   1.00 53.87  ? 35  ALA F C   1 
ATOM   10721 O O   . ALA F 2 35  ? -41.075 10.245  6.543   1.00 44.76  ? 35  ALA F O   1 
ATOM   10722 C CB  . ALA F 2 35  ? -42.466 8.916   4.174   1.00 41.36  ? 35  ALA F CB  1 
ATOM   10723 N N   . ALA F 2 36  ? -39.365 9.192   5.515   1.00 49.70  ? 36  ALA F N   1 
ATOM   10724 C CA  . ALA F 2 36  ? -38.349 10.096  6.031   1.00 53.98  ? 36  ALA F CA  1 
ATOM   10725 C C   . ALA F 2 36  ? -38.204 11.315  5.130   1.00 57.10  ? 36  ALA F C   1 
ATOM   10726 O O   . ALA F 2 36  ? -38.201 11.201  3.901   1.00 58.75  ? 36  ALA F O   1 
ATOM   10727 C CB  . ALA F 2 36  ? -37.004 9.381   6.156   1.00 50.54  ? 36  ALA F CB  1 
ATOM   10728 N N   . ASP F 2 37  ? -38.097 12.487  5.755   1.00 54.03  ? 37  ASP F N   1 
ATOM   10729 C CA  . ASP F 2 37  ? -37.797 13.725  5.044   1.00 51.31  ? 37  ASP F CA  1 
ATOM   10730 C C   . ASP F 2 37  ? -36.292 13.792  4.812   1.00 60.72  ? 37  ASP F C   1 
ATOM   10731 O O   . ASP F 2 37  ? -35.524 14.055  5.743   1.00 58.75  ? 37  ASP F O   1 
ATOM   10732 C CB  . ASP F 2 37  ? -38.289 14.931  5.839   1.00 45.60  ? 37  ASP F CB  1 
ATOM   10733 C CG  . ASP F 2 37  ? -38.263 16.211  5.030   1.00 57.23  ? 37  ASP F CG  1 
ATOM   10734 O OD1 . ASP F 2 37  ? -37.157 16.710  4.735   1.00 67.16  ? 37  ASP F OD1 1 
ATOM   10735 O OD2 . ASP F 2 37  ? -39.351 16.716  4.683   1.00 73.58  ? 37  ASP F OD2 1 
ATOM   10736 N N   . ARG F 2 38  ? -35.868 13.552  3.569   1.00 62.41  ? 38  ARG F N   1 
ATOM   10737 C CA  . ARG F 2 38  ? -34.440 13.461  3.287   1.00 62.72  ? 38  ARG F CA  1 
ATOM   10738 C C   . ARG F 2 38  ? -33.750 14.816  3.373   1.00 54.09  ? 38  ARG F C   1 
ATOM   10739 O O   . ARG F 2 38  ? -32.578 14.884  3.757   1.00 61.99  ? 38  ARG F O   1 
ATOM   10740 C CB  . ARG F 2 38  ? -34.214 12.840  1.909   1.00 68.09  ? 38  ARG F CB  1 
ATOM   10741 C CG  . ARG F 2 38  ? -35.134 11.672  1.597   1.00 79.89  ? 38  ARG F CG  1 
ATOM   10742 C CD  . ARG F 2 38  ? -34.662 10.388  2.271   1.00 75.63  ? 38  ARG F CD  1 
ATOM   10743 N NE  . ARG F 2 38  ? -34.069 9.450   1.324   1.00 84.58  ? 38  ARG F NE  1 
ATOM   10744 C CZ  . ARG F 2 38  ? -34.744 8.789   0.392   1.00 101.36 ? 38  ARG F CZ  1 
ATOM   10745 N NH1 . ARG F 2 38  ? -36.052 8.937   0.246   1.00 87.34  ? 38  ARG F NH1 1 
ATOM   10746 N NH2 . ARG F 2 38  ? -34.091 7.958   -0.416  1.00 93.09  ? 38  ARG F NH2 1 
ATOM   10747 N N   . GLU F 2 39  ? -34.447 15.896  3.014   1.00 60.26  ? 39  GLU F N   1 
ATOM   10748 C CA  . GLU F 2 39  ? -33.808 17.209  2.973   1.00 64.66  ? 39  GLU F CA  1 
ATOM   10749 C C   . GLU F 2 39  ? -33.361 17.651  4.361   1.00 55.08  ? 39  GLU F C   1 
ATOM   10750 O O   . GLU F 2 39  ? -32.196 18.008  4.568   1.00 57.14  ? 39  GLU F O   1 
ATOM   10751 C CB  . GLU F 2 39  ? -34.765 18.237  2.364   1.00 58.83  ? 39  GLU F CB  1 
ATOM   10752 C CG  . GLU F 2 39  ? -34.772 18.256  0.846   1.00 78.16  ? 39  GLU F CG  1 
ATOM   10753 C CD  . GLU F 2 39  ? -35.687 17.198  0.252   1.00 90.69  ? 39  GLU F CD  1 
ATOM   10754 O OE1 . GLU F 2 39  ? -36.622 16.751  0.954   1.00 78.31  ? 39  GLU F OE1 1 
ATOM   10755 O OE2 . GLU F 2 39  ? -35.471 16.815  -0.917  1.00 92.25  ? 39  GLU F OE2 1 
ATOM   10756 N N   . SER F 2 40  ? -34.277 17.626  5.330   1.00 55.27  ? 40  SER F N   1 
ATOM   10757 C CA  . SER F 2 40  ? -33.921 18.059  6.676   1.00 50.09  ? 40  SER F CA  1 
ATOM   10758 C C   . SER F 2 40  ? -32.964 17.075  7.336   1.00 46.15  ? 40  SER F C   1 
ATOM   10759 O O   . SER F 2 40  ? -32.052 17.484  8.062   1.00 50.71  ? 40  SER F O   1 
ATOM   10760 C CB  . SER F 2 40  ? -35.180 18.245  7.521   1.00 44.50  ? 40  SER F CB  1 
ATOM   10761 O OG  . SER F 2 40  ? -36.168 17.300  7.161   1.00 66.50  ? 40  SER F OG  1 
ATOM   10762 N N   . THR F 2 41  ? -33.148 15.776  7.089   1.00 47.48  ? 41  THR F N   1 
ATOM   10763 C CA  . THR F 2 41  ? -32.238 14.788  7.661   1.00 43.24  ? 41  THR F CA  1 
ATOM   10764 C C   . THR F 2 41  ? -30.812 14.999  7.167   1.00 43.66  ? 41  THR F C   1 
ATOM   10765 O O   . THR F 2 41  ? -29.864 14.976  7.962   1.00 45.31  ? 41  THR F O   1 
ATOM   10766 C CB  . THR F 2 41  ? -32.712 13.371  7.332   1.00 47.06  ? 41  THR F CB  1 
ATOM   10767 O OG1 . THR F 2 41  ? -33.981 13.125  7.953   1.00 43.13  ? 41  THR F OG1 1 
ATOM   10768 C CG2 . THR F 2 41  ? -31.709 12.346  7.841   1.00 47.67  ? 41  THR F CG2 1 
ATOM   10769 N N   . GLN F 2 42  ? -30.639 15.220  5.861   1.00 43.82  ? 42  GLN F N   1 
ATOM   10770 C CA  . GLN F 2 42  ? -29.297 15.405  5.316   1.00 48.57  ? 42  GLN F CA  1 
ATOM   10771 C C   . GLN F 2 42  ? -28.666 16.698  5.815   1.00 53.30  ? 42  GLN F C   1 
ATOM   10772 O O   . GLN F 2 42  ? -27.469 16.731  6.121   1.00 47.90  ? 42  GLN F O   1 
ATOM   10773 C CB  . GLN F 2 42  ? -29.332 15.390  3.788   1.00 53.64  ? 42  GLN F CB  1 
ATOM   10774 C CG  . GLN F 2 42  ? -28.007 14.999  3.144   1.00 39.42  ? 42  GLN F CG  1 
ATOM   10775 C CD  . GLN F 2 42  ? -27.292 13.911  3.920   1.00 55.54  ? 42  GLN F CD  1 
ATOM   10776 O OE1 . GLN F 2 42  ? -26.251 14.151  4.536   1.00 59.51  ? 42  GLN F OE1 1 
ATOM   10777 N NE2 . GLN F 2 42  ? -27.854 12.707  3.903   1.00 47.72  ? 42  GLN F NE2 1 
ATOM   10778 N N   . LYS F 2 43  ? -29.448 17.776  5.887   1.00 46.46  ? 43  LYS F N   1 
ATOM   10779 C CA  . LYS F 2 43  ? -28.912 19.033  6.395   1.00 50.42  ? 43  LYS F CA  1 
ATOM   10780 C C   . LYS F 2 43  ? -28.471 18.886  7.843   1.00 48.96  ? 43  LYS F C   1 
ATOM   10781 O O   . LYS F 2 43  ? -27.393 19.357  8.224   1.00 47.05  ? 43  LYS F O   1 
ATOM   10782 C CB  . LYS F 2 43  ? -29.953 20.143  6.260   1.00 47.92  ? 43  LYS F CB  1 
ATOM   10783 C CG  . LYS F 2 43  ? -29.954 20.833  4.907   1.00 64.36  ? 43  LYS F CG  1 
ATOM   10784 C CD  . LYS F 2 43  ? -31.369 21.175  4.457   1.00 83.06  ? 43  LYS F CD  1 
ATOM   10785 C CE  . LYS F 2 43  ? -31.781 22.570  4.912   1.00 74.61  ? 43  LYS F CE  1 
ATOM   10786 N NZ  . LYS F 2 43  ? -30.787 23.606  4.511   1.00 81.30  ? 43  LYS F NZ  1 
ATOM   10787 N N   . ALA F 2 44  ? -29.288 18.220  8.662   1.00 43.23  ? 44  ALA F N   1 
ATOM   10788 C CA  . ALA F 2 44  ? -28.946 18.044  10.068  1.00 47.43  ? 44  ALA F CA  1 
ATOM   10789 C C   . ALA F 2 44  ? -27.704 17.171  10.231  1.00 45.78  ? 44  ALA F C   1 
ATOM   10790 O O   . ALA F 2 44  ? -26.850 17.451  11.081  1.00 41.47  ? 44  ALA F O   1 
ATOM   10791 C CB  . ALA F 2 44  ? -30.138 17.456  10.824  1.00 39.92  ? 44  ALA F CB  1 
ATOM   10792 N N   . ILE F 2 45  ? -27.585 16.110  9.428   1.00 37.30  ? 45  ILE F N   1 
ATOM   10793 C CA  . ILE F 2 45  ? -26.399 15.261  9.492   1.00 48.26  ? 45  ILE F CA  1 
ATOM   10794 C C   . ILE F 2 45  ? -25.156 16.054  9.106   1.00 45.35  ? 45  ILE F C   1 
ATOM   10795 O O   . ILE F 2 45  ? -24.104 15.941  9.747   1.00 37.12  ? 45  ILE F O   1 
ATOM   10796 C CB  . ILE F 2 45  ? -26.581 14.022  8.597   1.00 46.24  ? 45  ILE F CB  1 
ATOM   10797 C CG1 . ILE F 2 45  ? -27.503 13.012  9.279   1.00 47.91  ? 45  ILE F CG1 1 
ATOM   10798 C CG2 . ILE F 2 45  ? -25.232 13.381  8.298   1.00 31.33  ? 45  ILE F CG2 1 
ATOM   10799 C CD1 . ILE F 2 45  ? -28.070 11.974  8.337   1.00 41.51  ? 45  ILE F CD1 1 
ATOM   10800 N N   . ASP F 2 46  ? -25.255 16.864  8.051   1.00 43.47  ? 46  ASP F N   1 
ATOM   10801 C CA  . ASP F 2 46  ? -24.117 17.673  7.631   1.00 46.01  ? 46  ASP F CA  1 
ATOM   10802 C C   . ASP F 2 46  ? -23.758 18.713  8.684   1.00 49.42  ? 46  ASP F C   1 
ATOM   10803 O O   . ASP F 2 46  ? -22.574 18.951  8.953   1.00 42.00  ? 46  ASP F O   1 
ATOM   10804 C CB  . ASP F 2 46  ? -24.417 18.340  6.291   1.00 46.04  ? 46  ASP F CB  1 
ATOM   10805 C CG  . ASP F 2 46  ? -24.657 17.332  5.182   1.00 50.59  ? 46  ASP F CG  1 
ATOM   10806 O OD1 . ASP F 2 46  ? -24.212 16.173  5.329   1.00 56.53  ? 46  ASP F OD1 1 
ATOM   10807 O OD2 . ASP F 2 46  ? -25.292 17.696  4.170   1.00 57.40  ? 46  ASP F OD2 1 
ATOM   10808 N N   . GLY F 2 47  ? -24.763 19.345  9.292   1.00 37.53  ? 47  GLY F N   1 
ATOM   10809 C CA  . GLY F 2 47  ? -24.475 20.326  10.326  1.00 44.55  ? 47  GLY F CA  1 
ATOM   10810 C C   . GLY F 2 47  ? -23.806 19.705  11.537  1.00 48.05  ? 47  GLY F C   1 
ATOM   10811 O O   . GLY F 2 47  ? -22.812 20.227  12.052  1.00 37.35  ? 47  GLY F O   1 
ATOM   10812 N N   . VAL F 2 48  ? -24.346 18.578  12.004  1.00 36.55  ? 48  VAL F N   1 
ATOM   10813 C CA  . VAL F 2 48  ? -23.790 17.892  13.165  1.00 36.71  ? 48  VAL F CA  1 
ATOM   10814 C C   . VAL F 2 48  ? -22.392 17.366  12.858  1.00 47.78  ? 48  VAL F C   1 
ATOM   10815 O O   . VAL F 2 48  ? -21.493 17.405  13.708  1.00 38.90  ? 48  VAL F O   1 
ATOM   10816 C CB  . VAL F 2 48  ? -24.743 16.763  13.603  1.00 43.67  ? 48  VAL F CB  1 
ATOM   10817 C CG1 . VAL F 2 48  ? -24.010 15.722  14.437  1.00 42.58  ? 48  VAL F CG1 1 
ATOM   10818 C CG2 . VAL F 2 48  ? -25.922 17.339  14.376  1.00 36.11  ? 48  VAL F CG2 1 
ATOM   10819 N N   . THR F 2 49  ? -22.188 16.857  11.641  1.00 46.07  ? 49  THR F N   1 
ATOM   10820 C CA  . THR F 2 49  ? -20.860 16.414  11.239  1.00 36.35  ? 49  THR F CA  1 
ATOM   10821 C C   . THR F 2 49  ? -19.878 17.576  11.220  1.00 41.36  ? 49  THR F C   1 
ATOM   10822 O O   . THR F 2 49  ? -18.733 17.441  11.670  1.00 46.33  ? 49  THR F O   1 
ATOM   10823 C CB  . THR F 2 49  ? -20.928 15.754  9.867   1.00 34.69  ? 49  THR F CB  1 
ATOM   10824 O OG1 . THR F 2 49  ? -21.887 14.688  9.905   1.00 40.81  ? 49  THR F OG1 1 
ATOM   10825 C CG2 . THR F 2 49  ? -19.556 15.205  9.472   1.00 33.25  ? 49  THR F CG2 1 
ATOM   10826 N N   . ASN F 2 50  ? -20.311 18.725  10.703  1.00 40.51  ? 50  ASN F N   1 
ATOM   10827 C CA  . ASN F 2 50  ? -19.464 19.910  10.723  1.00 37.23  ? 50  ASN F CA  1 
ATOM   10828 C C   . ASN F 2 50  ? -19.139 20.322  12.151  1.00 48.51  ? 50  ASN F C   1 
ATOM   10829 O O   . ASN F 2 50  ? -18.011 20.738  12.443  1.00 45.42  ? 50  ASN F O   1 
ATOM   10830 C CB  . ASN F 2 50  ? -20.149 21.055  9.983   1.00 40.81  ? 50  ASN F CB  1 
ATOM   10831 C CG  . ASN F 2 50  ? -19.526 21.327  8.635   1.00 64.74  ? 50  ASN F CG  1 
ATOM   10832 O OD1 . ASN F 2 50  ? -18.402 21.823  8.547   1.00 55.17  ? 50  ASN F OD1 1 
ATOM   10833 N ND2 . ASN F 2 50  ? -20.255 21.004  7.569   1.00 70.44  ? 50  ASN F ND2 1 
ATOM   10834 N N   . LYS F 2 51  ? -20.115 20.209  13.056  1.00 36.16  ? 51  LYS F N   1 
ATOM   10835 C CA  . LYS F 2 51  ? -19.888 20.608  14.441  1.00 44.35  ? 51  LYS F CA  1 
ATOM   10836 C C   . LYS F 2 51  ? -18.788 19.768  15.076  1.00 43.45  ? 51  LYS F C   1 
ATOM   10837 O O   . LYS F 2 51  ? -17.838 20.305  15.660  1.00 36.39  ? 51  LYS F O   1 
ATOM   10838 C CB  . LYS F 2 51  ? -21.182 20.492  15.245  1.00 38.73  ? 51  LYS F CB  1 
ATOM   10839 C CG  . LYS F 2 51  ? -20.972 20.668  16.741  1.00 48.62  ? 51  LYS F CG  1 
ATOM   10840 C CD  . LYS F 2 51  ? -22.217 20.310  17.527  1.00 46.27  ? 51  LYS F CD  1 
ATOM   10841 C CE  . LYS F 2 51  ? -23.343 21.282  17.247  1.00 36.98  ? 51  LYS F CE  1 
ATOM   10842 N NZ  . LYS F 2 51  ? -24.055 21.610  18.506  1.00 46.30  ? 51  LYS F NZ  1 
ATOM   10843 N N   . VAL F 2 52  ? -18.891 18.443  14.960  1.00 37.82  ? 52  VAL F N   1 
ATOM   10844 C CA  . VAL F 2 52  ? -17.855 17.579  15.513  1.00 34.50  ? 52  VAL F CA  1 
ATOM   10845 C C   . VAL F 2 52  ? -16.517 17.870  14.843  1.00 49.33  ? 52  VAL F C   1 
ATOM   10846 O O   . VAL F 2 52  ? -15.489 18.020  15.514  1.00 43.91  ? 52  VAL F O   1 
ATOM   10847 C CB  . VAL F 2 52  ? -18.254 16.101  15.367  1.00 43.70  ? 52  VAL F CB  1 
ATOM   10848 C CG1 . VAL F 2 52  ? -17.063 15.198  15.684  1.00 46.06  ? 52  VAL F CG1 1 
ATOM   10849 C CG2 . VAL F 2 52  ? -19.429 15.781  16.271  1.00 44.45  ? 52  VAL F CG2 1 
ATOM   10850 N N   . ASN F 2 53  ? -16.515 17.996  13.513  1.00 43.26  ? 53  ASN F N   1 
ATOM   10851 C CA  . ASN F 2 53  ? -15.269 18.266  12.802  1.00 44.04  ? 53  ASN F CA  1 
ATOM   10852 C C   . ASN F 2 53  ? -14.676 19.608  13.212  1.00 49.49  ? 53  ASN F C   1 
ATOM   10853 O O   . ASN F 2 53  ? -13.458 19.729  13.368  1.00 51.58  ? 53  ASN F O   1 
ATOM   10854 C CB  . ASN F 2 53  ? -15.502 18.220  11.294  1.00 53.34  ? 53  ASN F CB  1 
ATOM   10855 C CG  . ASN F 2 53  ? -15.681 16.809  10.775  1.00 48.45  ? 53  ASN F CG  1 
ATOM   10856 O OD1 . ASN F 2 53  ? -15.141 15.855  11.335  1.00 48.59  ? 53  ASN F OD1 1 
ATOM   10857 N ND2 . ASN F 2 53  ? -16.445 16.668  9.701   1.00 53.23  ? 53  ASN F ND2 1 
ATOM   10858 N N   . SER F 2 54  ? -15.518 20.632  13.387  1.00 50.20  ? 54  SER F N   1 
ATOM   10859 C CA  . SER F 2 54  ? -15.008 21.929  13.823  1.00 44.26  ? 54  SER F CA  1 
ATOM   10860 C C   . SER F 2 54  ? -14.376 21.833  15.206  1.00 46.56  ? 54  SER F C   1 
ATOM   10861 O O   . SER F 2 54  ? -13.307 22.405  15.452  1.00 47.50  ? 54  SER F O   1 
ATOM   10862 C CB  . SER F 2 54  ? -16.126 22.975  13.821  1.00 48.53  ? 54  SER F CB  1 
ATOM   10863 O OG  . SER F 2 54  ? -16.755 23.076  12.554  1.00 44.42  ? 54  SER F OG  1 
ATOM   10864 N N   . ILE F 2 55  ? -15.024 21.111  16.123  1.00 44.14  ? 55  ILE F N   1 
ATOM   10865 C CA  . ILE F 2 55  ? -14.496 20.975  17.477  1.00 43.74  ? 55  ILE F CA  1 
ATOM   10866 C C   . ILE F 2 55  ? -13.165 20.236  17.461  1.00 43.41  ? 55  ILE F C   1 
ATOM   10867 O O   . ILE F 2 55  ? -12.304 20.461  18.321  1.00 52.44  ? 55  ILE F O   1 
ATOM   10868 C CB  . ILE F 2 55  ? -15.545 20.282  18.373  1.00 43.51  ? 55  ILE F CB  1 
ATOM   10869 C CG1 . ILE F 2 55  ? -16.721 21.228  18.628  1.00 34.31  ? 55  ILE F CG1 1 
ATOM   10870 C CG2 . ILE F 2 55  ? -14.945 19.831  19.691  1.00 39.20  ? 55  ILE F CG2 1 
ATOM   10871 C CD1 . ILE F 2 55  ? -17.837 20.607  19.443  1.00 34.64  ? 55  ILE F CD1 1 
ATOM   10872 N N   . ILE F 2 56  ? -12.956 19.378  16.470  1.00 44.31  ? 56  ILE F N   1 
ATOM   10873 C CA  . ILE F 2 56  ? -11.714 18.625  16.361  1.00 44.73  ? 56  ILE F CA  1 
ATOM   10874 C C   . ILE F 2 56  ? -10.680 19.365  15.518  1.00 55.38  ? 56  ILE F C   1 
ATOM   10875 O O   . ILE F 2 56  ? -9.518  19.491  15.916  1.00 57.45  ? 56  ILE F O   1 
ATOM   10876 C CB  . ILE F 2 56  ? -12.015 17.227  15.789  1.00 46.05  ? 56  ILE F CB  1 
ATOM   10877 C CG1 . ILE F 2 56  ? -12.945 16.468  16.741  1.00 37.09  ? 56  ILE F CG1 1 
ATOM   10878 C CG2 . ILE F 2 56  ? -10.721 16.469  15.546  1.00 44.54  ? 56  ILE F CG2 1 
ATOM   10879 C CD1 . ILE F 2 56  ? -13.347 15.102  16.239  1.00 34.50  ? 56  ILE F CD1 1 
ATOM   10880 N N   . ASP F 2 57  ? -11.085 19.872  14.348  1.00 50.85  ? 57  ASP F N   1 
ATOM   10881 C CA  . ASP F 2 57  ? -10.124 20.438  13.403  1.00 47.15  ? 57  ASP F CA  1 
ATOM   10882 C C   . ASP F 2 57  ? -9.520  21.747  13.898  1.00 51.28  ? 57  ASP F C   1 
ATOM   10883 O O   . ASP F 2 57  ? -8.375  22.064  13.558  1.00 52.16  ? 57  ASP F O   1 
ATOM   10884 C CB  . ASP F 2 57  ? -10.782 20.655  12.038  1.00 50.32  ? 57  ASP F CB  1 
ATOM   10885 C CG  . ASP F 2 57  ? -11.239 19.357  11.392  1.00 64.49  ? 57  ASP F CG  1 
ATOM   10886 O OD1 . ASP F 2 57  ? -10.831 18.273  11.866  1.00 62.95  ? 57  ASP F OD1 1 
ATOM   10887 O OD2 . ASP F 2 57  ? -12.015 19.423  10.414  1.00 68.06  ? 57  ASP F OD2 1 
ATOM   10888 N N   . LYS F 2 58  ? -10.266 22.527  14.677  1.00 48.44  ? 58  LYS F N   1 
ATOM   10889 C CA  . LYS F 2 58  ? -9.753  23.815  15.122  1.00 41.40  ? 58  LYS F CA  1 
ATOM   10890 C C   . LYS F 2 58  ? -8.661  23.689  16.177  1.00 51.95  ? 58  LYS F C   1 
ATOM   10891 O O   . LYS F 2 58  ? -8.001  24.691  16.475  1.00 46.08  ? 58  LYS F O   1 
ATOM   10892 C CB  . LYS F 2 58  ? -10.895 24.676  15.659  1.00 54.73  ? 58  LYS F CB  1 
ATOM   10893 C CG  . LYS F 2 58  ? -11.867 25.153  14.593  1.00 50.63  ? 58  LYS F CG  1 
ATOM   10894 C CD  . LYS F 2 58  ? -11.185 26.054  13.576  1.00 47.19  ? 58  LYS F CD  1 
ATOM   10895 C CE  . LYS F 2 58  ? -12.206 26.638  12.606  1.00 56.23  ? 58  LYS F CE  1 
ATOM   10896 N NZ  . LYS F 2 58  ? -11.635 27.715  11.755  1.00 51.48  ? 58  LYS F NZ  1 
ATOM   10897 N N   . MET F 2 59  ? -8.462  22.505  16.753  1.00 49.41  ? 59  MET F N   1 
ATOM   10898 C CA  . MET F 2 59  ? -7.387  22.320  17.717  1.00 55.10  ? 59  MET F CA  1 
ATOM   10899 C C   . MET F 2 59  ? -6.033  22.440  17.032  1.00 48.42  ? 59  MET F C   1 
ATOM   10900 O O   . MET F 2 59  ? -5.834  21.944  15.920  1.00 58.97  ? 59  MET F O   1 
ATOM   10901 C CB  . MET F 2 59  ? -7.504  20.956  18.399  1.00 56.18  ? 59  MET F CB  1 
ATOM   10902 C CG  . MET F 2 59  ? -6.443  20.688  19.462  1.00 45.96  ? 59  MET F CG  1 
ATOM   10903 S SD  . MET F 2 59  ? -6.336  22.004  20.691  1.00 49.17  ? 59  MET F SD  1 
ATOM   10904 C CE  . MET F 2 59  ? -7.462  21.377  21.934  1.00 42.24  ? 59  MET F CE  1 
ATOM   10905 N N   . ASN F 2 60  ? -5.098  23.102  17.701  1.00 51.53  ? 60  ASN F N   1 
ATOM   10906 C CA  . ASN F 2 60  ? -3.752  23.284  17.179  1.00 58.06  ? 60  ASN F CA  1 
ATOM   10907 C C   . ASN F 2 60  ? -2.774  22.493  18.032  1.00 55.08  ? 60  ASN F C   1 
ATOM   10908 O O   . ASN F 2 60  ? -2.684  22.711  19.244  1.00 57.44  ? 60  ASN F O   1 
ATOM   10909 C CB  . ASN F 2 60  ? -3.366  24.758  17.152  1.00 56.44  ? 60  ASN F CB  1 
ATOM   10910 C CG  . ASN F 2 60  ? -2.144  25.012  16.307  1.00 66.01  ? 60  ASN F CG  1 
ATOM   10911 O OD1 . ASN F 2 60  ? -1.016  24.981  16.800  1.00 61.54  ? 60  ASN F OD1 1 
ATOM   10912 N ND2 . ASN F 2 60  ? -2.357  25.227  15.018  1.00 77.54  ? 60  ASN F ND2 1 
ATOM   10913 N N   . THR F 2 61  ? -2.042  21.582  17.399  1.00 55.08  ? 61  THR F N   1 
ATOM   10914 C CA  . THR F 2 61  ? -1.069  20.746  18.087  1.00 65.82  ? 61  THR F CA  1 
ATOM   10915 C C   . THR F 2 61  ? 0.319   21.032  17.536  1.00 54.96  ? 61  THR F C   1 
ATOM   10916 O O   . THR F 2 61  ? 0.509   21.095  16.317  1.00 67.05  ? 61  THR F O   1 
ATOM   10917 C CB  . THR F 2 61  ? -1.407  19.261  17.935  1.00 55.40  ? 61  THR F CB  1 
ATOM   10918 O OG1 . THR F 2 61  ? -0.939  18.794  16.665  1.00 77.31  ? 61  THR F OG1 1 
ATOM   10919 C CG2 . THR F 2 61  ? -2.905  19.050  18.029  1.00 50.20  ? 61  THR F CG2 1 
ATOM   10920 N N   . GLN F 2 62  ? 1.279   21.213  18.434  1.00 56.50  ? 62  GLN F N   1 
ATOM   10921 C CA  . GLN F 2 62  ? 2.666   21.433  18.063  1.00 51.36  ? 62  GLN F CA  1 
ATOM   10922 C C   . GLN F 2 62  ? 3.551   20.535  18.911  1.00 52.13  ? 62  GLN F C   1 
ATOM   10923 O O   . GLN F 2 62  ? 3.161   20.075  19.988  1.00 36.53  ? 62  GLN F O   1 
ATOM   10924 C CB  . GLN F 2 62  ? 3.081   22.898  18.234  1.00 51.94  ? 62  GLN F CB  1 
ATOM   10925 C CG  . GLN F 2 62  ? 2.265   23.667  19.257  1.00 52.49  ? 62  GLN F CG  1 
ATOM   10926 C CD  . GLN F 2 62  ? 2.586   25.152  19.252  1.00 65.89  ? 62  GLN F CD  1 
ATOM   10927 O OE1 . GLN F 2 62  ? 3.638   25.573  18.761  1.00 69.25  ? 62  GLN F OE1 1 
ATOM   10928 N NE2 . GLN F 2 62  ? 1.683   25.953  19.806  1.00 52.41  ? 62  GLN F NE2 1 
ATOM   10929 N N   . PHE F 2 63  ? 4.750   20.280  18.397  1.00 45.07  ? 63  PHE F N   1 
ATOM   10930 C CA  . PHE F 2 63  ? 5.678   19.388  19.071  1.00 42.44  ? 63  PHE F CA  1 
ATOM   10931 C C   . PHE F 2 63  ? 6.113   19.986  20.401  1.00 45.45  ? 63  PHE F C   1 
ATOM   10932 O O   . PHE F 2 63  ? 6.519   21.149  20.465  1.00 47.58  ? 63  PHE F O   1 
ATOM   10933 C CB  . PHE F 2 63  ? 6.893   19.126  18.184  1.00 41.15  ? 63  PHE F CB  1 
ATOM   10934 C CG  . PHE F 2 63  ? 7.970   18.326  18.852  1.00 44.94  ? 63  PHE F CG  1 
ATOM   10935 C CD1 . PHE F 2 63  ? 7.931   16.941  18.833  1.00 48.47  ? 63  PHE F CD1 1 
ATOM   10936 C CD2 . PHE F 2 63  ? 9.028   18.954  19.489  1.00 43.88  ? 63  PHE F CD2 1 
ATOM   10937 C CE1 . PHE F 2 63  ? 8.921   16.199  19.447  1.00 46.12  ? 63  PHE F CE1 1 
ATOM   10938 C CE2 . PHE F 2 63  ? 10.022  18.216  20.101  1.00 47.75  ? 63  PHE F CE2 1 
ATOM   10939 C CZ  . PHE F 2 63  ? 9.968   16.838  20.079  1.00 47.81  ? 63  PHE F CZ  1 
ATOM   10940 N N   . GLU F 2 64  ? 6.036   19.185  21.461  1.00 40.12  ? 64  GLU F N   1 
ATOM   10941 C CA  . GLU F 2 64  ? 6.572   19.566  22.758  1.00 46.61  ? 64  GLU F CA  1 
ATOM   10942 C C   . GLU F 2 64  ? 7.299   18.378  23.366  1.00 44.94  ? 64  GLU F C   1 
ATOM   10943 O O   . GLU F 2 64  ? 7.005   17.223  23.048  1.00 50.22  ? 64  GLU F O   1 
ATOM   10944 C CB  . GLU F 2 64  ? 5.477   20.053  23.715  1.00 42.48  ? 64  GLU F CB  1 
ATOM   10945 C CG  . GLU F 2 64  ? 4.784   21.340  23.285  1.00 52.86  ? 64  GLU F CG  1 
ATOM   10946 C CD  . GLU F 2 64  ? 5.739   22.508  23.107  1.00 49.66  ? 64  GLU F CD  1 
ATOM   10947 O OE1 . GLU F 2 64  ? 6.812   22.522  23.744  1.00 54.95  ? 64  GLU F OE1 1 
ATOM   10948 O OE2 . GLU F 2 64  ? 5.406   23.428  22.338  1.00 48.33  ? 64  GLU F OE2 1 
ATOM   10949 N N   . ALA F 2 65  ? 8.260   18.671  24.239  1.00 46.40  ? 65  ALA F N   1 
ATOM   10950 C CA  . ALA F 2 65  ? 9.033   17.648  24.941  1.00 39.93  ? 65  ALA F CA  1 
ATOM   10951 C C   . ALA F 2 65  ? 8.919   17.922  26.437  1.00 40.34  ? 65  ALA F C   1 
ATOM   10952 O O   . ALA F 2 65  ? 9.631   18.777  26.975  1.00 43.05  ? 65  ALA F O   1 
ATOM   10953 C CB  . ALA F 2 65  ? 10.482  17.636  24.472  1.00 46.63  ? 65  ALA F CB  1 
ATOM   10954 N N   . VAL F 2 66  ? 8.024   17.195  27.102  1.00 48.64  ? 66  VAL F N   1 
ATOM   10955 C CA  . VAL F 2 66  ? 7.711   17.404  28.511  1.00 43.54  ? 66  VAL F CA  1 
ATOM   10956 C C   . VAL F 2 66  ? 8.483   16.378  29.329  1.00 51.61  ? 66  VAL F C   1 
ATOM   10957 O O   . VAL F 2 66  ? 8.304   15.168  29.151  1.00 50.66  ? 66  VAL F O   1 
ATOM   10958 C CB  . VAL F 2 66  ? 6.199   17.292  28.771  1.00 45.31  ? 66  VAL F CB  1 
ATOM   10959 C CG1 . VAL F 2 66  ? 5.868   17.716  30.192  1.00 39.46  ? 66  VAL F CG1 1 
ATOM   10960 C CG2 . VAL F 2 66  ? 5.409   18.123  27.758  1.00 32.62  ? 66  VAL F CG2 1 
ATOM   10961 N N   . GLY F 2 67  ? 9.334   16.861  30.234  1.00 49.97  ? 67  GLY F N   1 
ATOM   10962 C CA  . GLY F 2 67  ? 10.105  15.996  31.109  1.00 41.64  ? 67  GLY F CA  1 
ATOM   10963 C C   . GLY F 2 67  ? 10.361  16.630  32.465  1.00 54.77  ? 67  GLY F C   1 
ATOM   10964 O O   . GLY F 2 67  ? 9.743   17.643  32.804  1.00 59.35  ? 67  GLY F O   1 
ATOM   10965 N N   . ARG F 2 68  ? 11.259  16.040  33.254  1.00 50.39  ? 68  ARG F N   1 
ATOM   10966 C CA  . ARG F 2 68  ? 11.646  16.563  34.567  1.00 44.78  ? 68  ARG F CA  1 
ATOM   10967 C C   . ARG F 2 68  ? 13.164  16.716  34.559  1.00 48.62  ? 68  ARG F C   1 
ATOM   10968 O O   . ARG F 2 68  ? 13.894  15.811  34.974  1.00 57.45  ? 68  ARG F O   1 
ATOM   10969 C CB  . ARG F 2 68  ? 11.170  15.647  35.687  1.00 39.17  ? 68  ARG F CB  1 
ATOM   10970 C CG  . ARG F 2 68  ? 9.660   15.497  35.758  1.00 42.00  ? 68  ARG F CG  1 
ATOM   10971 C CD  . ARG F 2 68  ? 8.991   16.845  35.929  1.00 44.13  ? 68  ARG F CD  1 
ATOM   10972 N NE  . ARG F 2 68  ? 7.564   16.719  36.196  1.00 53.96  ? 68  ARG F NE  1 
ATOM   10973 C CZ  . ARG F 2 68  ? 6.614   17.303  35.478  1.00 49.42  ? 68  ARG F CZ  1 
ATOM   10974 N NH1 . ARG F 2 68  ? 6.903   18.039  34.416  1.00 41.31  ? 68  ARG F NH1 1 
ATOM   10975 N NH2 . ARG F 2 68  ? 5.344   17.151  35.840  1.00 44.09  ? 68  ARG F NH2 1 
ATOM   10976 N N   . GLU F 2 69  ? 13.637  17.871  34.091  1.00 52.29  ? 69  GLU F N   1 
ATOM   10977 C CA  . GLU F 2 69  ? 15.048  18.075  33.788  1.00 48.06  ? 69  GLU F CA  1 
ATOM   10978 C C   . GLU F 2 69  ? 15.762  18.963  34.801  1.00 52.33  ? 69  GLU F C   1 
ATOM   10979 O O   . GLU F 2 69  ? 16.899  19.376  34.551  1.00 51.52  ? 69  GLU F O   1 
ATOM   10980 C CB  . GLU F 2 69  ? 15.197  18.662  32.381  1.00 51.84  ? 69  GLU F CB  1 
ATOM   10981 C CG  . GLU F 2 69  ? 15.058  17.641  31.257  1.00 49.23  ? 69  GLU F CG  1 
ATOM   10982 C CD  . GLU F 2 69  ? 16.317  17.526  30.406  1.00 74.84  ? 69  GLU F CD  1 
ATOM   10983 O OE1 . GLU F 2 69  ? 17.434  17.477  30.981  1.00 72.31  ? 69  GLU F OE1 1 
ATOM   10984 O OE2 . GLU F 2 69  ? 16.186  17.493  29.161  1.00 55.98  ? 69  GLU F OE2 1 
ATOM   10985 N N   . PHE F 2 70  ? 15.140  19.264  35.936  1.00 46.66  ? 70  PHE F N   1 
ATOM   10986 C CA  . PHE F 2 70  ? 15.758  20.103  36.952  1.00 50.35  ? 70  PHE F CA  1 
ATOM   10987 C C   . PHE F 2 70  ? 16.147  19.264  38.166  1.00 50.39  ? 70  PHE F C   1 
ATOM   10988 O O   . PHE F 2 70  ? 15.481  18.280  38.503  1.00 48.10  ? 70  PHE F O   1 
ATOM   10989 C CB  . PHE F 2 70  ? 14.819  21.244  37.352  1.00 46.00  ? 70  PHE F CB  1 
ATOM   10990 C CG  . PHE F 2 70  ? 14.426  22.125  36.201  1.00 48.31  ? 70  PHE F CG  1 
ATOM   10991 C CD1 . PHE F 2 70  ? 15.309  23.071  35.702  1.00 46.27  ? 70  PHE F CD1 1 
ATOM   10992 C CD2 . PHE F 2 70  ? 13.180  21.998  35.606  1.00 44.41  ? 70  PHE F CD2 1 
ATOM   10993 C CE1 . PHE F 2 70  ? 14.954  23.881  34.633  1.00 41.25  ? 70  PHE F CE1 1 
ATOM   10994 C CE2 . PHE F 2 70  ? 12.820  22.802  34.538  1.00 40.04  ? 70  PHE F CE2 1 
ATOM   10995 C CZ  . PHE F 2 70  ? 13.709  23.743  34.051  1.00 44.79  ? 70  PHE F CZ  1 
ATOM   10996 N N   . ASN F 2 71  ? 17.244  19.658  38.814  1.00 46.84  ? 71  ASN F N   1 
ATOM   10997 C CA  . ASN F 2 71  ? 17.855  18.856  39.865  1.00 50.79  ? 71  ASN F CA  1 
ATOM   10998 C C   . ASN F 2 71  ? 17.365  19.303  41.242  1.00 49.89  ? 71  ASN F C   1 
ATOM   10999 O O   . ASN F 2 71  ? 16.456  20.128  41.370  1.00 57.41  ? 71  ASN F O   1 
ATOM   11000 C CB  . ASN F 2 71  ? 19.380  18.913  39.758  1.00 50.82  ? 71  ASN F CB  1 
ATOM   11001 C CG  . ASN F 2 71  ? 19.932  20.327  39.854  1.00 53.22  ? 71  ASN F CG  1 
ATOM   11002 O OD1 . ASN F 2 71  ? 19.499  21.128  40.681  1.00 48.79  ? 71  ASN F OD1 1 
ATOM   11003 N ND2 . ASN F 2 71  ? 20.906  20.635  39.003  1.00 61.92  ? 71  ASN F ND2 1 
ATOM   11004 N N   . ASN F 2 72  ? 17.989  18.760  42.292  1.00 55.36  ? 72  ASN F N   1 
ATOM   11005 C CA  . ASN F 2 72  ? 17.524  19.003  43.655  1.00 60.63  ? 72  ASN F CA  1 
ATOM   11006 C C   . ASN F 2 72  ? 17.708  20.455  44.079  1.00 54.02  ? 72  ASN F C   1 
ATOM   11007 O O   . ASN F 2 72  ? 16.995  20.931  44.969  1.00 58.83  ? 72  ASN F O   1 
ATOM   11008 C CB  . ASN F 2 72  ? 18.251  18.074  44.629  1.00 65.42  ? 72  ASN F CB  1 
ATOM   11009 C CG  . ASN F 2 72  ? 17.502  17.897  45.936  1.00 65.59  ? 72  ASN F CG  1 
ATOM   11010 O OD1 . ASN F 2 72  ? 16.325  17.536  45.948  1.00 82.13  ? 72  ASN F OD1 1 
ATOM   11011 N ND2 . ASN F 2 72  ? 18.180  18.159  47.046  1.00 82.48  ? 72  ASN F ND2 1 
ATOM   11012 N N   . LEU F 2 73  ? 18.651  21.171  43.468  1.00 53.52  ? 73  LEU F N   1 
ATOM   11013 C CA  . LEU F 2 73  ? 18.890  22.573  43.783  1.00 62.70  ? 73  LEU F CA  1 
ATOM   11014 C C   . LEU F 2 73  ? 18.195  23.511  42.803  1.00 57.49  ? 73  LEU F C   1 
ATOM   11015 O O   . LEU F 2 73  ? 18.590  24.675  42.676  1.00 55.52  ? 73  LEU F O   1 
ATOM   11016 C CB  . LEU F 2 73  ? 20.393  22.858  43.829  1.00 50.01  ? 73  LEU F CB  1 
ATOM   11017 C CG  . LEU F 2 73  ? 21.078  22.473  45.144  1.00 56.33  ? 73  LEU F CG  1 
ATOM   11018 C CD1 . LEU F 2 73  ? 22.540  22.930  45.184  1.00 46.67  ? 73  LEU F CD1 1 
ATOM   11019 C CD2 . LEU F 2 73  ? 20.300  23.025  46.340  1.00 50.66  ? 73  LEU F CD2 1 
ATOM   11020 N N   . GLU F 2 74  ? 17.171  23.027  42.108  1.00 51.94  ? 74  GLU F N   1 
ATOM   11021 C CA  . GLU F 2 74  ? 16.396  23.834  41.180  1.00 55.37  ? 74  GLU F CA  1 
ATOM   11022 C C   . GLU F 2 74  ? 14.904  23.605  41.396  1.00 48.22  ? 74  GLU F C   1 
ATOM   11023 O O   . GLU F 2 74  ? 14.109  23.619  40.452  1.00 43.89  ? 74  GLU F O   1 
ATOM   11024 C CB  . GLU F 2 74  ? 16.794  23.534  39.735  1.00 53.35  ? 74  GLU F CB  1 
ATOM   11025 C CG  . GLU F 2 74  ? 18.226  23.917  39.394  1.00 43.61  ? 74  GLU F CG  1 
ATOM   11026 C CD  . GLU F 2 74  ? 18.736  23.269  38.113  1.00 51.47  ? 74  GLU F CD  1 
ATOM   11027 O OE1 . GLU F 2 74  ? 18.278  22.156  37.778  1.00 52.32  ? 74  GLU F OE1 1 
ATOM   11028 O OE2 . GLU F 2 74  ? 19.596  23.879  37.439  1.00 51.73  ? 74  GLU F OE2 1 
ATOM   11029 N N   . ARG F 2 75  ? 14.501  23.395  42.656  1.00 48.85  ? 75  ARG F N   1 
ATOM   11030 C CA  . ARG F 2 75  ? 13.100  23.113  42.950  1.00 50.38  ? 75  ARG F CA  1 
ATOM   11031 C C   . ARG F 2 75  ? 12.206  24.301  42.624  1.00 47.95  ? 75  ARG F C   1 
ATOM   11032 O O   . ARG F 2 75  ? 11.063  24.115  42.192  1.00 52.79  ? 75  ARG F O   1 
ATOM   11033 C CB  . ARG F 2 75  ? 12.938  22.713  44.415  1.00 41.43  ? 75  ARG F CB  1 
ATOM   11034 C CG  . ARG F 2 75  ? 13.812  21.539  44.836  1.00 57.95  ? 75  ARG F CG  1 
ATOM   11035 C CD  . ARG F 2 75  ? 13.006  20.260  44.956  1.00 68.54  ? 75  ARG F CD  1 
ATOM   11036 N NE  . ARG F 2 75  ? 13.768  19.086  44.551  1.00 85.39  ? 75  ARG F NE  1 
ATOM   11037 C CZ  . ARG F 2 75  ? 13.671  18.508  43.360  1.00 89.91  ? 75  ARG F CZ  1 
ATOM   11038 N NH1 . ARG F 2 75  ? 12.861  18.982  42.426  1.00 71.64  ? 75  ARG F NH1 1 
ATOM   11039 N NH2 . ARG F 2 75  ? 14.404  17.427  43.102  1.00 71.72  ? 75  ARG F NH2 1 
ATOM   11040 N N   . ARG F 2 76  ? 12.706  25.524  42.817  1.00 44.91  ? 76  ARG F N   1 
ATOM   11041 C CA  . ARG F 2 76  ? 11.900  26.705  42.529  1.00 46.55  ? 76  ARG F CA  1 
ATOM   11042 C C   . ARG F 2 76  ? 11.497  26.753  41.060  1.00 50.19  ? 76  ARG F C   1 
ATOM   11043 O O   . ARG F 2 76  ? 10.350  27.086  40.733  1.00 50.90  ? 76  ARG F O   1 
ATOM   11044 C CB  . ARG F 2 76  ? 12.663  27.970  42.920  1.00 41.94  ? 76  ARG F CB  1 
ATOM   11045 C CG  . ARG F 2 76  ? 12.731  28.213  44.421  1.00 48.98  ? 76  ARG F CG  1 
ATOM   11046 C CD  . ARG F 2 76  ? 13.819  29.220  44.775  1.00 49.78  ? 76  ARG F CD  1 
ATOM   11047 N NE  . ARG F 2 76  ? 15.058  28.981  44.042  1.00 51.72  ? 76  ARG F NE  1 
ATOM   11048 C CZ  . ARG F 2 76  ? 15.837  29.937  43.555  1.00 48.08  ? 76  ARG F CZ  1 
ATOM   11049 N NH1 . ARG F 2 76  ? 15.541  31.216  43.714  1.00 48.74  ? 76  ARG F NH1 1 
ATOM   11050 N NH2 . ARG F 2 76  ? 16.938  29.602  42.888  1.00 42.43  ? 76  ARG F NH2 1 
ATOM   11051 N N   . ILE F 2 77  ? 12.423  26.416  40.159  1.00 48.90  ? 77  ILE F N   1 
ATOM   11052 C CA  . ILE F 2 77  ? 12.103  26.399  38.735  1.00 51.87  ? 77  ILE F CA  1 
ATOM   11053 C C   . ILE F 2 77  ? 11.121  25.276  38.416  1.00 49.54  ? 77  ILE F C   1 
ATOM   11054 O O   . ILE F 2 77  ? 10.181  25.462  37.632  1.00 45.35  ? 77  ILE F O   1 
ATOM   11055 C CB  . ILE F 2 77  ? 13.388  26.289  37.897  1.00 38.74  ? 77  ILE F CB  1 
ATOM   11056 C CG1 . ILE F 2 77  ? 14.202  27.574  38.014  1.00 51.48  ? 77  ILE F CG1 1 
ATOM   11057 C CG2 . ILE F 2 77  ? 13.056  26.073  36.445  1.00 39.24  ? 77  ILE F CG2 1 
ATOM   11058 C CD1 . ILE F 2 77  ? 15.620  27.449  37.501  1.00 43.68  ? 77  ILE F CD1 1 
ATOM   11059 N N   . GLU F 2 78  ? 11.312  24.097  39.021  1.00 46.78  ? 78  GLU F N   1 
ATOM   11060 C CA  . GLU F 2 78  ? 10.363  23.004  38.819  1.00 45.75  ? 78  GLU F CA  1 
ATOM   11061 C C   . GLU F 2 78  ? 8.976   23.381  39.329  1.00 48.91  ? 78  GLU F C   1 
ATOM   11062 O O   . GLU F 2 78  ? 7.963   22.985  38.740  1.00 47.49  ? 78  GLU F O   1 
ATOM   11063 C CB  . GLU F 2 78  ? 10.860  21.731  39.506  1.00 39.25  ? 78  GLU F CB  1 
ATOM   11064 C CG  . GLU F 2 78  ? 10.044  20.465  39.218  1.00 56.85  ? 78  GLU F CG  1 
ATOM   11065 C CD  . GLU F 2 78  ? 9.602   20.336  37.753  1.00 83.82  ? 78  GLU F CD  1 
ATOM   11066 O OE1 . GLU F 2 78  ? 10.465  20.018  36.901  1.00 76.94  ? 78  GLU F OE1 1 
ATOM   11067 O OE2 . GLU F 2 78  ? 8.390   20.500  37.461  1.00 53.86  ? 78  GLU F OE2 1 
ATOM   11068 N N   . ASN F 2 79  ? 8.907   24.151  40.420  1.00 35.09  ? 79  ASN F N   1 
ATOM   11069 C CA  . ASN F 2 79  ? 7.610   24.634  40.882  1.00 42.66  ? 79  ASN F CA  1 
ATOM   11070 C C   . ASN F 2 79  ? 6.965   25.531  39.836  1.00 44.65  ? 79  ASN F C   1 
ATOM   11071 O O   . ASN F 2 79  ? 5.746   25.486  39.637  1.00 42.25  ? 79  ASN F O   1 
ATOM   11072 C CB  . ASN F 2 79  ? 7.754   25.375  42.212  1.00 47.53  ? 79  ASN F CB  1 
ATOM   11073 C CG  . ASN F 2 79  ? 6.413   25.795  42.792  1.00 50.01  ? 79  ASN F CG  1 
ATOM   11074 O OD1 . ASN F 2 79  ? 5.452   25.024  42.787  1.00 63.12  ? 79  ASN F OD1 1 
ATOM   11075 N ND2 . ASN F 2 79  ? 6.342   27.023  43.295  1.00 60.54  ? 79  ASN F ND2 1 
ATOM   11076 N N   . LEU F 2 80  ? 7.771   26.347  39.149  1.00 44.14  ? 80  LEU F N   1 
ATOM   11077 C CA  . LEU F 2 80  ? 7.236   27.156  38.060  1.00 45.82  ? 80  LEU F CA  1 
ATOM   11078 C C   . LEU F 2 80  ? 6.653   26.274  36.968  1.00 37.71  ? 80  LEU F C   1 
ATOM   11079 O O   . LEU F 2 80  ? 5.565   26.552  36.449  1.00 37.35  ? 80  LEU F O   1 
ATOM   11080 C CB  . LEU F 2 80  ? 8.327   28.062  37.489  1.00 43.72  ? 80  LEU F CB  1 
ATOM   11081 C CG  . LEU F 2 80  ? 7.900   29.437  36.968  1.00 46.57  ? 80  LEU F CG  1 
ATOM   11082 C CD1 . LEU F 2 80  ? 9.102   30.365  36.903  1.00 57.84  ? 80  LEU F CD1 1 
ATOM   11083 C CD2 . LEU F 2 80  ? 7.245   29.342  35.605  1.00 52.41  ? 80  LEU F CD2 1 
ATOM   11084 N N   . ASN F 2 81  ? 7.363   25.201  36.611  1.00 34.83  ? 81  ASN F N   1 
ATOM   11085 C CA  . ASN F 2 81  ? 6.860   24.273  35.606  1.00 40.44  ? 81  ASN F CA  1 
ATOM   11086 C C   . ASN F 2 81  ? 5.603   23.559  36.089  1.00 43.01  ? 81  ASN F C   1 
ATOM   11087 O O   . ASN F 2 81  ? 4.677   23.327  35.305  1.00 51.53  ? 81  ASN F O   1 
ATOM   11088 C CB  . ASN F 2 81  ? 7.942   23.262  35.239  1.00 45.35  ? 81  ASN F CB  1 
ATOM   11089 C CG  . ASN F 2 81  ? 7.503   22.322  34.140  1.00 44.16  ? 81  ASN F CG  1 
ATOM   11090 O OD1 . ASN F 2 81  ? 7.240   22.746  33.016  1.00 46.07  ? 81  ASN F OD1 1 
ATOM   11091 N ND2 . ASN F 2 81  ? 7.411   21.038  34.460  1.00 54.43  ? 81  ASN F ND2 1 
ATOM   11092 N N   . LYS F 2 82  ? 5.559   23.192  37.372  1.00 37.55  ? 82  LYS F N   1 
ATOM   11093 C CA  . LYS F 2 82  ? 4.354   22.579  37.924  1.00 42.72  ? 82  LYS F CA  1 
ATOM   11094 C C   . LYS F 2 82  ? 3.176   23.546  37.891  1.00 47.29  ? 82  LYS F C   1 
ATOM   11095 O O   . LYS F 2 82  ? 2.065   23.167  37.503  1.00 45.72  ? 82  LYS F O   1 
ATOM   11096 C CB  . LYS F 2 82  ? 4.613   22.099  39.352  1.00 41.01  ? 82  LYS F CB  1 
ATOM   11097 C CG  . LYS F 2 82  ? 3.365   21.633  40.092  1.00 47.78  ? 82  LYS F CG  1 
ATOM   11098 C CD  . LYS F 2 82  ? 3.640   21.438  41.576  1.00 40.27  ? 82  LYS F CD  1 
ATOM   11099 C CE  . LYS F 2 82  ? 2.357   21.483  42.391  1.00 54.14  ? 82  LYS F CE  1 
ATOM   11100 N NZ  . LYS F 2 82  ? 1.319   20.580  41.827  1.00 67.50  ? 82  LYS F NZ  1 
ATOM   11101 N N   . LYS F 2 83  ? 3.396   24.803  38.284  1.00 38.98  ? 83  LYS F N   1 
ATOM   11102 C CA  . LYS F 2 83  ? 2.304   25.768  38.237  1.00 41.63  ? 83  LYS F CA  1 
ATOM   11103 C C   . LYS F 2 83  ? 1.852   26.013  36.807  1.00 39.95  ? 83  LYS F C   1 
ATOM   11104 O O   . LYS F 2 83  ? 0.661   26.224  36.559  1.00 42.89  ? 83  LYS F O   1 
ATOM   11105 C CB  . LYS F 2 83  ? 2.721   27.075  38.906  1.00 41.37  ? 83  LYS F CB  1 
ATOM   11106 C CG  . LYS F 2 83  ? 2.867   26.960  40.419  1.00 43.29  ? 83  LYS F CG  1 
ATOM   11107 C CD  . LYS F 2 83  ? 3.055   28.327  41.068  1.00 59.80  ? 83  LYS F CD  1 
ATOM   11108 C CE  . LYS F 2 83  ? 4.246   29.075  40.475  1.00 46.75  ? 83  LYS F CE  1 
ATOM   11109 N NZ  . LYS F 2 83  ? 4.072   30.553  40.582  1.00 59.69  ? 83  LYS F NZ  1 
ATOM   11110 N N   . MET F 2 84  ? 2.779   25.959  35.852  1.00 45.92  ? 84  MET F N   1 
ATOM   11111 C CA  . MET F 2 84  ? 2.404   26.108  34.452  1.00 46.01  ? 84  MET F CA  1 
ATOM   11112 C C   . MET F 2 84  ? 1.649   24.883  33.943  1.00 47.14  ? 84  MET F C   1 
ATOM   11113 O O   . MET F 2 84  ? 0.618   25.012  33.272  1.00 50.16  ? 84  MET F O   1 
ATOM   11114 C CB  . MET F 2 84  ? 3.648   26.361  33.608  1.00 38.57  ? 84  MET F CB  1 
ATOM   11115 C CG  . MET F 2 84  ? 3.338   26.792  32.191  1.00 42.37  ? 84  MET F CG  1 
ATOM   11116 S SD  . MET F 2 84  ? 4.562   26.165  31.031  1.00 58.35  ? 84  MET F SD  1 
ATOM   11117 C CE  . MET F 2 84  ? 4.203   24.407  31.058  1.00 44.25  ? 84  MET F CE  1 
ATOM   11118 N N   . GLU F 2 85  ? 2.155   23.682  34.241  1.00 42.64  ? 85  GLU F N   1 
ATOM   11119 C CA  . GLU F 2 85  ? 1.517   22.469  33.730  1.00 50.32  ? 85  GLU F CA  1 
ATOM   11120 C C   . GLU F 2 85  ? 0.121   22.292  34.311  1.00 40.12  ? 85  GLU F C   1 
ATOM   11121 O O   . GLU F 2 85  ? -0.817  21.929  33.593  1.00 40.04  ? 85  GLU F O   1 
ATOM   11122 C CB  . GLU F 2 85  ? 2.386   21.245  34.028  1.00 42.65  ? 85  GLU F CB  1 
ATOM   11123 C CG  . GLU F 2 85  ? 3.520   21.051  33.029  1.00 54.20  ? 85  GLU F CG  1 
ATOM   11124 C CD  . GLU F 2 85  ? 4.301   19.765  33.251  1.00 60.80  ? 85  GLU F CD  1 
ATOM   11125 O OE1 . GLU F 2 85  ? 3.780   18.848  33.924  1.00 58.66  ? 85  GLU F OE1 1 
ATOM   11126 O OE2 . GLU F 2 85  ? 5.438   19.671  32.740  1.00 61.91  ? 85  GLU F OE2 1 
ATOM   11127 N N   . ASP F 2 86  ? -0.033  22.546  35.609  1.00 48.60  ? 86  ASP F N   1 
ATOM   11128 C CA  . ASP F 2 86  ? -1.348  22.474  36.234  1.00 41.85  ? 86  ASP F CA  1 
ATOM   11129 C C   . ASP F 2 86  ? -2.263  23.592  35.748  1.00 45.70  ? 86  ASP F C   1 
ATOM   11130 O O   . ASP F 2 86  ? -3.482  23.399  35.654  1.00 46.12  ? 86  ASP F O   1 
ATOM   11131 C CB  . ASP F 2 86  ? -1.198  22.521  37.755  1.00 57.17  ? 86  ASP F CB  1 
ATOM   11132 C CG  . ASP F 2 86  ? -0.317  21.403  38.290  1.00 53.61  ? 86  ASP F CG  1 
ATOM   11133 O OD1 . ASP F 2 86  ? 0.083   20.523  37.499  1.00 52.01  ? 86  ASP F OD1 1 
ATOM   11134 O OD2 . ASP F 2 86  ? -0.022  21.407  39.504  1.00 49.80  ? 86  ASP F OD2 1 
ATOM   11135 N N   . GLY F 2 87  ? -1.703  24.763  35.440  1.00 41.28  ? 87  GLY F N   1 
ATOM   11136 C CA  . GLY F 2 87  ? -2.520  25.837  34.899  1.00 31.62  ? 87  GLY F CA  1 
ATOM   11137 C C   . GLY F 2 87  ? -3.155  25.480  33.568  1.00 40.36  ? 87  GLY F C   1 
ATOM   11138 O O   . GLY F 2 87  ? -4.338  25.744  33.342  1.00 38.53  ? 87  GLY F O   1 
ATOM   11139 N N   . PHE F 2 88  ? -2.384  24.865  32.670  1.00 41.93  ? 88  PHE F N   1 
ATOM   11140 C CA  . PHE F 2 88  ? -2.950  24.492  31.379  1.00 39.64  ? 88  PHE F CA  1 
ATOM   11141 C C   . PHE F 2 88  ? -3.916  23.328  31.512  1.00 40.48  ? 88  PHE F C   1 
ATOM   11142 O O   . PHE F 2 88  ? -4.907  23.261  30.774  1.00 43.32  ? 88  PHE F O   1 
ATOM   11143 C CB  . PHE F 2 88  ? -1.840  24.164  30.384  1.00 29.44  ? 88  PHE F CB  1 
ATOM   11144 C CG  . PHE F 2 88  ? -1.101  25.375  29.888  1.00 42.99  ? 88  PHE F CG  1 
ATOM   11145 C CD1 . PHE F 2 88  ? -1.782  26.417  29.283  1.00 34.89  ? 88  PHE F CD1 1 
ATOM   11146 C CD2 . PHE F 2 88  ? 0.274   25.480  30.047  1.00 45.33  ? 88  PHE F CD2 1 
ATOM   11147 C CE1 . PHE F 2 88  ? -1.106  27.542  28.832  1.00 45.37  ? 88  PHE F CE1 1 
ATOM   11148 C CE2 . PHE F 2 88  ? 0.954   26.598  29.598  1.00 43.04  ? 88  PHE F CE2 1 
ATOM   11149 C CZ  . PHE F 2 88  ? 0.265   27.630  28.992  1.00 45.96  ? 88  PHE F CZ  1 
ATOM   11150 N N   . LEU F 2 89  ? -3.653  22.404  32.437  1.00 35.13  ? 89  LEU F N   1 
ATOM   11151 C CA  . LEU F 2 89  ? -4.589  21.308  32.658  1.00 36.50  ? 89  LEU F CA  1 
ATOM   11152 C C   . LEU F 2 89  ? -5.929  21.827  33.163  1.00 40.04  ? 89  LEU F C   1 
ATOM   11153 O O   . LEU F 2 89  ? -6.987  21.339  32.753  1.00 44.86  ? 89  LEU F O   1 
ATOM   11154 C CB  . LEU F 2 89  ? -4.004  20.297  33.640  1.00 34.38  ? 89  LEU F CB  1 
ATOM   11155 C CG  . LEU F 2 89  ? -4.982  19.201  34.069  1.00 38.30  ? 89  LEU F CG  1 
ATOM   11156 C CD1 . LEU F 2 89  ? -4.385  17.828  33.817  1.00 42.13  ? 89  LEU F CD1 1 
ATOM   11157 C CD2 . LEU F 2 89  ? -5.358  19.364  35.534  1.00 34.40  ? 89  LEU F CD2 1 
ATOM   11158 N N   . ASP F 2 90  ? -5.903  22.805  34.068  1.00 44.36  ? 90  ASP F N   1 
ATOM   11159 C CA  . ASP F 2 90  ? -7.147  23.396  34.543  1.00 33.40  ? 90  ASP F CA  1 
ATOM   11160 C C   . ASP F 2 90  ? -7.872  24.125  33.419  1.00 37.39  ? 90  ASP F C   1 
ATOM   11161 O O   . ASP F 2 90  ? -9.097  24.015  33.289  1.00 43.30  ? 90  ASP F O   1 
ATOM   11162 C CB  . ASP F 2 90  ? -6.866  24.347  35.705  1.00 38.49  ? 90  ASP F CB  1 
ATOM   11163 C CG  . ASP F 2 90  ? -6.457  23.617  36.975  1.00 55.94  ? 90  ASP F CG  1 
ATOM   11164 O OD1 . ASP F 2 90  ? -6.480  22.368  36.979  1.00 51.58  ? 90  ASP F OD1 1 
ATOM   11165 O OD2 . ASP F 2 90  ? -6.115  24.295  37.972  1.00 55.16  ? 90  ASP F OD2 1 
ATOM   11166 N N   . VAL F 2 91  ? -7.133  24.879  32.597  1.00 33.22  ? 91  VAL F N   1 
ATOM   11167 C CA  . VAL F 2 91  ? -7.765  25.646  31.524  1.00 38.79  ? 91  VAL F CA  1 
ATOM   11168 C C   . VAL F 2 91  ? -8.412  24.705  30.515  1.00 41.33  ? 91  VAL F C   1 
ATOM   11169 O O   . VAL F 2 91  ? -9.592  24.848  30.168  1.00 38.37  ? 91  VAL F O   1 
ATOM   11170 C CB  . VAL F 2 91  ? -6.742  26.581  30.848  1.00 31.88  ? 91  VAL F CB  1 
ATOM   11171 C CG1 . VAL F 2 91  ? -7.290  27.087  29.520  1.00 30.65  ? 91  VAL F CG1 1 
ATOM   11172 C CG2 . VAL F 2 91  ? -6.394  27.762  31.755  1.00 31.23  ? 91  VAL F CG2 1 
ATOM   11173 N N   . TRP F 2 92  ? -7.654  23.710  30.052  1.00 31.43  ? 92  TRP F N   1 
ATOM   11174 C CA  . TRP F 2 92  ? -8.156  22.798  29.030  1.00 34.72  ? 92  TRP F CA  1 
ATOM   11175 C C   . TRP F 2 92  ? -9.311  21.952  29.549  1.00 42.06  ? 92  TRP F C   1 
ATOM   11176 O O   . TRP F 2 92  ? -10.277 21.701  28.821  1.00 41.14  ? 92  TRP F O   1 
ATOM   11177 C CB  . TRP F 2 92  ? -7.018  21.915  28.518  1.00 30.86  ? 92  TRP F CB  1 
ATOM   11178 C CG  . TRP F 2 92  ? -6.115  22.636  27.562  1.00 39.16  ? 92  TRP F CG  1 
ATOM   11179 C CD1 . TRP F 2 92  ? -4.778  22.869  27.716  1.00 30.18  ? 92  TRP F CD1 1 
ATOM   11180 C CD2 . TRP F 2 92  ? -6.486  23.239  26.311  1.00 30.31  ? 92  TRP F CD2 1 
ATOM   11181 N NE1 . TRP F 2 92  ? -4.292  23.562  26.632  1.00 43.09  ? 92  TRP F NE1 1 
ATOM   11182 C CE2 . TRP F 2 92  ? -5.320  23.805  25.758  1.00 46.39  ? 92  TRP F CE2 1 
ATOM   11183 C CE3 . TRP F 2 92  ? -7.687  23.343  25.602  1.00 35.90  ? 92  TRP F CE3 1 
ATOM   11184 C CZ2 . TRP F 2 92  ? -5.321  24.469  24.530  1.00 42.11  ? 92  TRP F CZ2 1 
ATOM   11185 C CZ3 . TRP F 2 92  ? -7.685  24.001  24.383  1.00 29.86  ? 92  TRP F CZ3 1 
ATOM   11186 C CH2 . TRP F 2 92  ? -6.512  24.559  23.863  1.00 35.19  ? 92  TRP F CH2 1 
ATOM   11187 N N   . THR F 2 93  ? -9.230  21.502  30.800  1.00 36.77  ? 93  THR F N   1 
ATOM   11188 C CA  . THR F 2 93  ? -10.295 20.677  31.361  1.00 35.14  ? 93  THR F CA  1 
ATOM   11189 C C   . THR F 2 93  ? -11.610 21.444  31.430  1.00 41.06  ? 93  THR F C   1 
ATOM   11190 O O   . THR F 2 93  ? -12.643 20.967  30.951  1.00 48.28  ? 93  THR F O   1 
ATOM   11191 C CB  . THR F 2 93  ? -9.878  20.179  32.743  1.00 36.66  ? 93  THR F CB  1 
ATOM   11192 O OG1 . THR F 2 93  ? -8.725  19.343  32.606  1.00 33.36  ? 93  THR F OG1 1 
ATOM   11193 C CG2 . THR F 2 93  ? -10.995 19.400  33.413  1.00 38.46  ? 93  THR F CG2 1 
ATOM   11194 N N   . TYR F 2 94  ? -11.582 22.647  32.006  1.00 40.22  ? 94  TYR F N   1 
ATOM   11195 C CA  . TYR F 2 94  ? -12.797 23.446  32.149  1.00 37.49  ? 94  TYR F CA  1 
ATOM   11196 C C   . TYR F 2 94  ? -13.407 23.765  30.790  1.00 46.75  ? 94  TYR F C   1 
ATOM   11197 O O   . TYR F 2 94  ? -14.621 23.626  30.590  1.00 50.62  ? 94  TYR F O   1 
ATOM   11198 C CB  . TYR F 2 94  ? -12.474 24.737  32.904  1.00 41.18  ? 94  TYR F CB  1 
ATOM   11199 C CG  . TYR F 2 94  ? -13.661 25.476  33.475  1.00 43.21  ? 94  TYR F CG  1 
ATOM   11200 C CD1 . TYR F 2 94  ? -14.442 24.915  34.479  1.00 47.59  ? 94  TYR F CD1 1 
ATOM   11201 C CD2 . TYR F 2 94  ? -13.989 26.749  33.027  1.00 45.20  ? 94  TYR F CD2 1 
ATOM   11202 C CE1 . TYR F 2 94  ? -15.526 25.597  35.011  1.00 37.68  ? 94  TYR F CE1 1 
ATOM   11203 C CE2 . TYR F 2 94  ? -15.068 27.439  33.553  1.00 40.99  ? 94  TYR F CE2 1 
ATOM   11204 C CZ  . TYR F 2 94  ? -15.831 26.861  34.548  1.00 43.95  ? 94  TYR F CZ  1 
ATOM   11205 O OH  . TYR F 2 94  ? -16.900 27.552  35.075  1.00 40.66  ? 94  TYR F OH  1 
ATOM   11206 N N   . ASN F 2 95  ? -12.574 24.197  29.840  1.00 44.07  ? 95  ASN F N   1 
ATOM   11207 C CA  . ASN F 2 95  ? -13.075 24.527  28.513  1.00 43.54  ? 95  ASN F CA  1 
ATOM   11208 C C   . ASN F 2 95  ? -13.622 23.291  27.808  1.00 49.73  ? 95  ASN F C   1 
ATOM   11209 O O   . ASN F 2 95  ? -14.679 23.354  27.172  1.00 47.12  ? 95  ASN F O   1 
ATOM   11210 C CB  . ASN F 2 95  ? -11.971 25.190  27.685  1.00 50.40  ? 95  ASN F CB  1 
ATOM   11211 C CG  . ASN F 2 95  ? -11.647 26.605  28.165  1.00 71.79  ? 95  ASN F CG  1 
ATOM   11212 O OD1 . ASN F 2 95  ? -12.271 27.119  29.096  1.00 59.90  ? 95  ASN F OD1 1 
ATOM   11213 N ND2 . ASN F 2 95  ? -10.668 27.237  27.526  1.00 71.09  ? 95  ASN F ND2 1 
ATOM   11214 N N   . ALA F 2 96  ? -12.925 22.155  27.916  1.00 39.85  ? 96  ALA F N   1 
ATOM   11215 C CA  . ALA F 2 96  ? -13.400 20.942  27.258  1.00 41.93  ? 96  ALA F CA  1 
ATOM   11216 C C   . ALA F 2 96  ? -14.716 20.469  27.854  1.00 45.67  ? 96  ALA F C   1 
ATOM   11217 O O   . ALA F 2 96  ? -15.638 20.099  27.117  1.00 43.30  ? 96  ALA F O   1 
ATOM   11218 C CB  . ALA F 2 96  ? -12.348 19.839  27.348  1.00 40.49  ? 96  ALA F CB  1 
ATOM   11219 N N   . GLU F 2 97  ? -14.831 20.483  29.183  1.00 43.22  ? 97  GLU F N   1 
ATOM   11220 C CA  . GLU F 2 97  ? -16.072 20.048  29.813  1.00 44.56  ? 97  GLU F CA  1 
ATOM   11221 C C   . GLU F 2 97  ? -17.230 20.965  29.437  1.00 47.46  ? 97  GLU F C   1 
ATOM   11222 O O   . GLU F 2 97  ? -18.291 20.495  29.014  1.00 56.07  ? 97  GLU F O   1 
ATOM   11223 C CB  . GLU F 2 97  ? -15.900 19.987  31.331  1.00 42.60  ? 97  GLU F CB  1 
ATOM   11224 C CG  . GLU F 2 97  ? -14.842 18.992  31.797  1.00 48.76  ? 97  GLU F CG  1 
ATOM   11225 C CD  . GLU F 2 97  ? -15.308 17.544  31.751  1.00 56.21  ? 97  GLU F CD  1 
ATOM   11226 O OE1 . GLU F 2 97  ? -16.518 17.295  31.554  1.00 56.09  ? 97  GLU F OE1 1 
ATOM   11227 O OE2 . GLU F 2 97  ? -14.451 16.649  31.917  1.00 52.91  ? 97  GLU F OE2 1 
ATOM   11228 N N   . LEU F 2 98  ? -17.038 22.281  29.564  1.00 42.52  ? 98  LEU F N   1 
ATOM   11229 C CA  . LEU F 2 98  ? -18.137 23.207  29.305  1.00 42.28  ? 98  LEU F CA  1 
ATOM   11230 C C   . LEU F 2 98  ? -18.493 23.260  27.827  1.00 46.28  ? 98  LEU F C   1 
ATOM   11231 O O   . LEU F 2 98  ? -19.659 23.481  27.479  1.00 43.97  ? 98  LEU F O   1 
ATOM   11232 C CB  . LEU F 2 98  ? -17.783 24.604  29.813  1.00 40.42  ? 98  LEU F CB  1 
ATOM   11233 C CG  . LEU F 2 98  ? -17.893 24.832  31.321  1.00 48.24  ? 98  LEU F CG  1 
ATOM   11234 C CD1 . LEU F 2 98  ? -18.090 26.309  31.617  1.00 55.39  ? 98  LEU F CD1 1 
ATOM   11235 C CD2 . LEU F 2 98  ? -19.016 24.006  31.926  1.00 41.14  ? 98  LEU F CD2 1 
ATOM   11236 N N   . LEU F 2 99  ? -17.507 23.086  26.946  1.00 33.53  ? 99  LEU F N   1 
ATOM   11237 C CA  . LEU F 2 99  ? -17.803 23.045  25.520  1.00 40.55  ? 99  LEU F CA  1 
ATOM   11238 C C   . LEU F 2 99  ? -18.707 21.863  25.193  1.00 47.57  ? 99  LEU F C   1 
ATOM   11239 O O   . LEU F 2 99  ? -19.684 22.003  24.448  1.00 39.37  ? 99  LEU F O   1 
ATOM   11240 C CB  . LEU F 2 99  ? -16.500 22.980  24.724  1.00 47.19  ? 99  LEU F CB  1 
ATOM   11241 C CG  . LEU F 2 99  ? -16.557 22.514  23.270  1.00 58.24  ? 99  LEU F CG  1 
ATOM   11242 C CD1 . LEU F 2 99  ? -16.827 23.681  22.350  1.00 56.12  ? 99  LEU F CD1 1 
ATOM   11243 C CD2 . LEU F 2 99  ? -15.257 21.826  22.889  1.00 55.62  ? 99  LEU F CD2 1 
ATOM   11244 N N   . VAL F 2 100 ? -18.412 20.697  25.769  1.00 41.59  ? 100 VAL F N   1 
ATOM   11245 C CA  . VAL F 2 100 ? -19.256 19.526  25.553  1.00 48.19  ? 100 VAL F CA  1 
ATOM   11246 C C   . VAL F 2 100 ? -20.656 19.774  26.099  1.00 44.02  ? 100 VAL F C   1 
ATOM   11247 O O   . VAL F 2 100 ? -21.658 19.484  25.434  1.00 38.55  ? 100 VAL F O   1 
ATOM   11248 C CB  . VAL F 2 100 ? -18.600 18.283  26.183  1.00 42.76  ? 100 VAL F CB  1 
ATOM   11249 C CG1 . VAL F 2 100 ? -19.592 17.153  26.293  1.00 29.09  ? 100 VAL F CG1 1 
ATOM   11250 C CG2 . VAL F 2 100 ? -17.389 17.853  25.362  1.00 38.79  ? 100 VAL F CG2 1 
ATOM   11251 N N   . LEU F 2 101 ? -20.749 20.340  27.305  1.00 35.93  ? 101 LEU F N   1 
ATOM   11252 C CA  . LEU F 2 101 ? -22.056 20.615  27.895  1.00 37.19  ? 101 LEU F CA  1 
ATOM   11253 C C   . LEU F 2 101 ? -22.857 21.595  27.046  1.00 42.29  ? 101 LEU F C   1 
ATOM   11254 O O   . LEU F 2 101 ? -24.053 21.388  26.806  1.00 46.71  ? 101 LEU F O   1 
ATOM   11255 C CB  . LEU F 2 101 ? -21.885 21.154  29.316  1.00 37.50  ? 101 LEU F CB  1 
ATOM   11256 C CG  . LEU F 2 101 ? -21.458 20.162  30.401  1.00 42.07  ? 101 LEU F CG  1 
ATOM   11257 C CD1 . LEU F 2 101 ? -21.491 20.833  31.765  1.00 44.08  ? 101 LEU F CD1 1 
ATOM   11258 C CD2 . LEU F 2 101 ? -22.335 18.922  30.393  1.00 31.08  ? 101 LEU F CD2 1 
ATOM   11259 N N   . MET F 2 102 ? -22.217 22.671  26.585  1.00 45.79  ? 102 MET F N   1 
ATOM   11260 C CA  . MET F 2 102 ? -22.930 23.685  25.816  1.00 36.79  ? 102 MET F CA  1 
ATOM   11261 C C   . MET F 2 102 ? -23.297 23.177  24.427  1.00 35.94  ? 102 MET F C   1 
ATOM   11262 O O   . MET F 2 102 ? -24.380 23.483  23.912  1.00 37.92  ? 102 MET F O   1 
ATOM   11263 C CB  . MET F 2 102 ? -22.084 24.952  25.710  1.00 36.54  ? 102 MET F CB  1 
ATOM   11264 C CG  . MET F 2 102 ? -22.169 25.876  26.914  1.00 50.90  ? 102 MET F CG  1 
ATOM   11265 S SD  . MET F 2 102 ? -20.635 26.807  27.126  1.00 59.57  ? 102 MET F SD  1 
ATOM   11266 C CE  . MET F 2 102 ? -20.611 27.751  25.606  1.00 43.52  ? 102 MET F CE  1 
ATOM   11267 N N   . GLU F 2 103 ? -22.405 22.413  23.798  1.00 34.84  ? 103 GLU F N   1 
ATOM   11268 C CA  . GLU F 2 103 ? -22.675 21.944  22.444  1.00 37.68  ? 103 GLU F CA  1 
ATOM   11269 C C   . GLU F 2 103 ? -23.772 20.889  22.429  1.00 39.00  ? 103 GLU F C   1 
ATOM   11270 O O   . GLU F 2 103 ? -24.572 20.835  21.488  1.00 33.69  ? 103 GLU F O   1 
ATOM   11271 C CB  . GLU F 2 103 ? -21.392 21.412  21.812  1.00 45.08  ? 103 GLU F CB  1 
ATOM   11272 C CG  . GLU F 2 103 ? -20.596 22.490  21.084  1.00 49.54  ? 103 GLU F CG  1 
ATOM   11273 C CD  . GLU F 2 103 ? -21.487 23.570  20.490  1.00 68.22  ? 103 GLU F CD  1 
ATOM   11274 O OE1 . GLU F 2 103 ? -22.181 23.289  19.486  1.00 77.39  ? 103 GLU F OE1 1 
ATOM   11275 O OE2 . GLU F 2 103 ? -21.499 24.699  21.024  1.00 71.25  ? 103 GLU F OE2 1 
ATOM   11276 N N   . ASN F 2 104 ? -23.831 20.042  23.461  1.00 37.45  ? 104 ASN F N   1 
ATOM   11277 C CA  . ASN F 2 104 ? -24.897 19.047  23.534  1.00 35.42  ? 104 ASN F CA  1 
ATOM   11278 C C   . ASN F 2 104 ? -26.256 19.711  23.704  1.00 41.94  ? 104 ASN F C   1 
ATOM   11279 O O   . ASN F 2 104 ? -27.243 19.283  23.093  1.00 41.99  ? 104 ASN F O   1 
ATOM   11280 C CB  . ASN F 2 104 ? -24.626 18.068  24.671  1.00 35.47  ? 104 ASN F CB  1 
ATOM   11281 C CG  . ASN F 2 104 ? -23.501 17.107  24.346  1.00 42.97  ? 104 ASN F CG  1 
ATOM   11282 O OD1 . ASN F 2 104 ? -23.077 17.008  23.194  1.00 35.65  ? 104 ASN F OD1 1 
ATOM   11283 N ND2 . ASN F 2 104 ? -23.002 16.403  25.359  1.00 34.85  ? 104 ASN F ND2 1 
ATOM   11284 N N   . GLU F 2 105 ? -26.327 20.766  24.519  1.00 47.86  ? 105 GLU F N   1 
ATOM   11285 C CA  . GLU F 2 105 ? -27.588 21.484  24.662  1.00 43.44  ? 105 GLU F CA  1 
ATOM   11286 C C   . GLU F 2 105 ? -28.034 22.060  23.324  1.00 43.58  ? 105 GLU F C   1 
ATOM   11287 O O   . GLU F 2 105 ? -29.210 21.956  22.955  1.00 46.84  ? 105 GLU F O   1 
ATOM   11288 C CB  . GLU F 2 105 ? -27.449 22.582  25.716  1.00 44.72  ? 105 GLU F CB  1 
ATOM   11289 C CG  . GLU F 2 105 ? -28.413 23.747  25.550  1.00 54.90  ? 105 GLU F CG  1 
ATOM   11290 C CD  . GLU F 2 105 ? -29.630 23.632  26.455  1.00 81.30  ? 105 GLU F CD  1 
ATOM   11291 O OE1 . GLU F 2 105 ? -29.566 22.869  27.445  1.00 75.89  ? 105 GLU F OE1 1 
ATOM   11292 O OE2 . GLU F 2 105 ? -30.650 24.304  26.177  1.00 83.41  ? 105 GLU F OE2 1 
ATOM   11293 N N   . ARG F 2 106 ? -27.098 22.643  22.569  1.00 35.38  ? 106 ARG F N   1 
ATOM   11294 C CA  . ARG F 2 106 ? -27.440 23.207  21.267  1.00 42.86  ? 106 ARG F CA  1 
ATOM   11295 C C   . ARG F 2 106 ? -27.821 22.122  20.268  1.00 36.72  ? 106 ARG F C   1 
ATOM   11296 O O   . ARG F 2 106 ? -28.751 22.304  19.473  1.00 36.68  ? 106 ARG F O   1 
ATOM   11297 C CB  . ARG F 2 106 ? -26.278 24.044  20.740  1.00 38.61  ? 106 ARG F CB  1 
ATOM   11298 C CG  . ARG F 2 106 ? -26.253 25.469  21.277  1.00 59.74  ? 106 ARG F CG  1 
ATOM   11299 C CD  . ARG F 2 106 ? -25.788 26.426  20.197  1.00 72.99  ? 106 ARG F CD  1 
ATOM   11300 N NE  . ARG F 2 106 ? -24.791 25.797  19.339  1.00 96.49  ? 106 ARG F NE  1 
ATOM   11301 C CZ  . ARG F 2 106 ? -23.547 26.232  19.181  1.00 88.05  ? 106 ARG F CZ  1 
ATOM   11302 N NH1 . ARG F 2 106 ? -23.118 27.339  19.767  1.00 74.87  ? 106 ARG F NH1 1 
ATOM   11303 N NH2 . ARG F 2 106 ? -22.712 25.537  18.416  1.00 79.33  ? 106 ARG F NH2 1 
ATOM   11304 N N   . THR F 2 107 ? -27.112 20.990  20.288  1.00 33.70  ? 107 THR F N   1 
ATOM   11305 C CA  . THR F 2 107 ? -27.419 19.899  19.367  1.00 34.73  ? 107 THR F CA  1 
ATOM   11306 C C   . THR F 2 107 ? -28.832 19.366  19.586  1.00 43.02  ? 107 THR F C   1 
ATOM   11307 O O   . THR F 2 107 ? -29.580 19.156  18.624  1.00 34.46  ? 107 THR F O   1 
ATOM   11308 C CB  . THR F 2 107 ? -26.391 18.780  19.530  1.00 34.46  ? 107 THR F CB  1 
ATOM   11309 O OG1 . THR F 2 107 ? -25.142 19.188  18.964  1.00 45.52  ? 107 THR F OG1 1 
ATOM   11310 C CG2 . THR F 2 107 ? -26.860 17.497  18.840  1.00 33.02  ? 107 THR F CG2 1 
ATOM   11311 N N   . LEU F 2 108 ? -29.221 19.153  20.845  1.00 38.76  ? 108 LEU F N   1 
ATOM   11312 C CA  . LEU F 2 108 ? -30.579 18.694  21.126  1.00 46.31  ? 108 LEU F CA  1 
ATOM   11313 C C   . LEU F 2 108 ? -31.609 19.743  20.725  1.00 45.46  ? 108 LEU F C   1 
ATOM   11314 O O   . LEU F 2 108 ? -32.680 19.405  20.206  1.00 43.45  ? 108 LEU F O   1 
ATOM   11315 C CB  . LEU F 2 108 ? -30.721 18.338  22.605  1.00 41.65  ? 108 LEU F CB  1 
ATOM   11316 C CG  . LEU F 2 108 ? -29.933 17.117  23.088  1.00 49.87  ? 108 LEU F CG  1 
ATOM   11317 C CD1 . LEU F 2 108 ? -30.373 16.726  24.489  1.00 53.39  ? 108 LEU F CD1 1 
ATOM   11318 C CD2 . LEU F 2 108 ? -30.084 15.940  22.125  1.00 42.54  ? 108 LEU F CD2 1 
ATOM   11319 N N   . ASP F 2 109 ? -31.308 21.022  20.959  1.00 36.54  ? 109 ASP F N   1 
ATOM   11320 C CA  . ASP F 2 109 ? -32.228 22.069  20.532  1.00 44.35  ? 109 ASP F CA  1 
ATOM   11321 C C   . ASP F 2 109 ? -32.266 22.187  19.014  1.00 39.86  ? 109 ASP F C   1 
ATOM   11322 O O   . ASP F 2 109 ? -33.294 22.576  18.447  1.00 39.30  ? 109 ASP F O   1 
ATOM   11323 C CB  . ASP F 2 109 ? -31.839 23.401  21.173  1.00 44.35  ? 109 ASP F CB  1 
ATOM   11324 C CG  . ASP F 2 109 ? -32.123 23.428  22.663  1.00 55.09  ? 109 ASP F CG  1 
ATOM   11325 O OD1 . ASP F 2 109 ? -33.084 22.750  23.095  1.00 62.28  ? 109 ASP F OD1 1 
ATOM   11326 O OD2 . ASP F 2 109 ? -31.386 24.114  23.401  1.00 54.17  ? 109 ASP F OD2 1 
ATOM   11327 N N   . PHE F 2 110 ? -31.163 21.847  18.343  1.00 27.99  ? 110 PHE F N   1 
ATOM   11328 C CA  . PHE F 2 110 ? -31.151 21.849  16.885  1.00 30.25  ? 110 PHE F CA  1 
ATOM   11329 C C   . PHE F 2 110 ? -32.124 20.812  16.328  1.00 46.98  ? 110 PHE F C   1 
ATOM   11330 O O   . PHE F 2 110 ? -32.912 21.107  15.420  1.00 43.38  ? 110 PHE F O   1 
ATOM   11331 C CB  . PHE F 2 110 ? -29.729 21.597  16.387  1.00 31.13  ? 110 PHE F CB  1 
ATOM   11332 C CG  . PHE F 2 110 ? -29.612 21.504  14.898  1.00 37.83  ? 110 PHE F CG  1 
ATOM   11333 C CD1 . PHE F 2 110 ? -29.980 22.569  14.093  1.00 39.97  ? 110 PHE F CD1 1 
ATOM   11334 C CD2 . PHE F 2 110 ? -29.105 20.361  14.303  1.00 34.16  ? 110 PHE F CD2 1 
ATOM   11335 C CE1 . PHE F 2 110 ? -29.861 22.487  12.716  1.00 36.37  ? 110 PHE F CE1 1 
ATOM   11336 C CE2 . PHE F 2 110 ? -28.991 20.272  12.927  1.00 36.92  ? 110 PHE F CE2 1 
ATOM   11337 C CZ  . PHE F 2 110 ? -29.361 21.340  12.134  1.00 29.24  ? 110 PHE F CZ  1 
ATOM   11338 N N   . HIS F 2 111 ? -32.106 19.596  16.885  1.00 30.37  ? 111 HIS F N   1 
ATOM   11339 C CA  . HIS F 2 111 ? -33.056 18.574  16.455  1.00 42.67  ? 111 HIS F CA  1 
ATOM   11340 C C   . HIS F 2 111 ? -34.486 18.997  16.752  1.00 39.69  ? 111 HIS F C   1 
ATOM   11341 O O   . HIS F 2 111 ? -35.390 18.778  15.935  1.00 30.97  ? 111 HIS F O   1 
ATOM   11342 C CB  . HIS F 2 111 ? -32.753 17.242  17.138  1.00 38.06  ? 111 HIS F CB  1 
ATOM   11343 C CG  . HIS F 2 111 ? -31.462 16.622  16.710  1.00 42.66  ? 111 HIS F CG  1 
ATOM   11344 N ND1 . HIS F 2 111 ? -31.160 16.375  15.389  1.00 44.18  ? 111 HIS F ND1 1 
ATOM   11345 C CD2 . HIS F 2 111 ? -30.396 16.196  17.427  1.00 39.59  ? 111 HIS F CD2 1 
ATOM   11346 C CE1 . HIS F 2 111 ? -29.960 15.827  15.311  1.00 46.04  ? 111 HIS F CE1 1 
ATOM   11347 N NE2 . HIS F 2 111 ? -29.475 15.707  16.534  1.00 42.10  ? 111 HIS F NE2 1 
ATOM   11348 N N   . ASP F 2 112 ? -34.709 19.598  17.922  1.00 43.35  ? 112 ASP F N   1 
ATOM   11349 C CA  . ASP F 2 112 ? -36.035 20.094  18.265  1.00 35.41  ? 112 ASP F CA  1 
ATOM   11350 C C   . ASP F 2 112 ? -36.496 21.139  17.259  1.00 38.51  ? 112 ASP F C   1 
ATOM   11351 O O   . ASP F 2 112 ? -37.652 21.122  16.820  1.00 44.62  ? 112 ASP F O   1 
ATOM   11352 C CB  . ASP F 2 112 ? -36.012 20.674  19.680  1.00 39.92  ? 112 ASP F CB  1 
ATOM   11353 C CG  . ASP F 2 112 ? -37.397 20.897  20.253  1.00 48.52  ? 112 ASP F CG  1 
ATOM   11354 O OD1 . ASP F 2 112 ? -38.377 20.361  19.699  1.00 53.75  ? 112 ASP F OD1 1 
ATOM   11355 O OD2 . ASP F 2 112 ? -37.500 21.612  21.272  1.00 52.39  ? 112 ASP F OD2 1 
ATOM   11356 N N   . SER F 2 113 ? -35.598 22.045  16.874  1.00 38.55  ? 113 SER F N   1 
ATOM   11357 C CA  . SER F 2 113 ? -35.925 23.054  15.871  1.00 38.82  ? 113 SER F CA  1 
ATOM   11358 C C   . SER F 2 113 ? -36.314 22.425  14.539  1.00 44.81  ? 113 SER F C   1 
ATOM   11359 O O   . SER F 2 113 ? -37.315 22.812  13.923  1.00 34.91  ? 113 SER F O   1 
ATOM   11360 C CB  . SER F 2 113 ? -34.735 23.992  15.684  1.00 36.54  ? 113 SER F CB  1 
ATOM   11361 O OG  . SER F 2 113 ? -34.938 24.830  14.569  1.00 45.10  ? 113 SER F OG  1 
ATOM   11362 N N   . ASN F 2 114 ? -35.526 21.452  14.074  1.00 40.56  ? 114 ASN F N   1 
ATOM   11363 C CA  . ASN F 2 114 ? -35.785 20.855  12.770  1.00 35.29  ? 114 ASN F CA  1 
ATOM   11364 C C   . ASN F 2 114 ? -37.160 20.195  12.736  1.00 38.99  ? 114 ASN F C   1 
ATOM   11365 O O   . ASN F 2 114 ? -37.872 20.271  11.727  1.00 45.75  ? 114 ASN F O   1 
ATOM   11366 C CB  . ASN F 2 114 ? -34.688 19.842  12.439  1.00 38.88  ? 114 ASN F CB  1 
ATOM   11367 C CG  . ASN F 2 114 ? -33.334 20.492  12.218  1.00 42.12  ? 114 ASN F CG  1 
ATOM   11368 O OD1 . ASN F 2 114 ? -33.245 21.656  11.838  1.00 46.14  ? 114 ASN F OD1 1 
ATOM   11369 N ND2 . ASN F 2 114 ? -32.268 19.739  12.471  1.00 44.94  ? 114 ASN F ND2 1 
ATOM   11370 N N   . VAL F 2 115 ? -37.555 19.550  13.835  1.00 28.31  ? 115 VAL F N   1 
ATOM   11371 C CA  . VAL F 2 115 ? -38.853 18.886  13.873  1.00 35.99  ? 115 VAL F CA  1 
ATOM   11372 C C   . VAL F 2 115 ? -39.978 19.913  13.825  1.00 40.88  ? 115 VAL F C   1 
ATOM   11373 O O   . VAL F 2 115 ? -40.959 19.746  13.089  1.00 39.55  ? 115 VAL F O   1 
ATOM   11374 C CB  . VAL F 2 115 ? -38.942 17.983  15.119  1.00 32.06  ? 115 VAL F CB  1 
ATOM   11375 C CG1 . VAL F 2 115 ? -40.339 17.426  15.292  1.00 30.97  ? 115 VAL F CG1 1 
ATOM   11376 C CG2 . VAL F 2 115 ? -37.934 16.853  15.013  1.00 38.39  ? 115 VAL F CG2 1 
ATOM   11377 N N   . LYS F 2 116 ? -39.845 21.003  14.588  1.00 37.70  ? 116 LYS F N   1 
ATOM   11378 C CA  . LYS F 2 116 ? -40.890 22.020  14.612  1.00 46.69  ? 116 LYS F CA  1 
ATOM   11379 C C   . LYS F 2 116 ? -41.070 22.665  13.245  1.00 47.34  ? 116 LYS F C   1 
ATOM   11380 O O   . LYS F 2 116 ? -42.200 22.944  12.827  1.00 36.83  ? 116 LYS F O   1 
ATOM   11381 C CB  . LYS F 2 116 ? -40.577 23.086  15.662  1.00 45.99  ? 116 LYS F CB  1 
ATOM   11382 C CG  . LYS F 2 116 ? -41.668 24.135  15.785  1.00 44.98  ? 116 LYS F CG  1 
ATOM   11383 C CD  . LYS F 2 116 ? -41.533 24.957  17.052  1.00 68.70  ? 116 LYS F CD  1 
ATOM   11384 C CE  . LYS F 2 116 ? -42.844 25.653  17.397  1.00 73.82  ? 116 LYS F CE  1 
ATOM   11385 N NZ  . LYS F 2 116 ? -44.015 24.958  16.797  1.00 64.09  ? 116 LYS F NZ  1 
ATOM   11386 N N   . ASN F 2 117 ? -39.968 22.923  12.536  1.00 41.27  ? 117 ASN F N   1 
ATOM   11387 C CA  . ASN F 2 117 ? -40.085 23.506  11.204  1.00 44.88  ? 117 ASN F CA  1 
ATOM   11388 C C   . ASN F 2 117 ? -40.869 22.588  10.274  1.00 46.90  ? 117 ASN F C   1 
ATOM   11389 O O   . ASN F 2 117 ? -41.724 23.053  9.511   1.00 49.90  ? 117 ASN F O   1 
ATOM   11390 C CB  . ASN F 2 117 ? -38.700 23.806  10.634  1.00 35.66  ? 117 ASN F CB  1 
ATOM   11391 C CG  . ASN F 2 117 ? -37.971 24.890  11.411  1.00 56.88  ? 117 ASN F CG  1 
ATOM   11392 O OD1 . ASN F 2 117 ? -38.596 25.741  12.048  1.00 48.75  ? 117 ASN F OD1 1 
ATOM   11393 N ND2 . ASN F 2 117 ? -36.641 24.861  11.366  1.00 49.44  ? 117 ASN F ND2 1 
ATOM   11394 N N   . LEU F 2 118 ? -40.599 21.279  10.334  1.00 37.95  ? 118 LEU F N   1 
ATOM   11395 C CA  . LEU F 2 118 ? -41.348 20.322  9.522   1.00 45.88  ? 118 LEU F CA  1 
ATOM   11396 C C   . LEU F 2 118 ? -42.826 20.322  9.890   1.00 42.30  ? 118 LEU F C   1 
ATOM   11397 O O   . LEU F 2 118 ? -43.693 20.272  9.010   1.00 40.35  ? 118 LEU F O   1 
ATOM   11398 C CB  . LEU F 2 118 ? -40.768 18.919  9.692   1.00 40.28  ? 118 LEU F CB  1 
ATOM   11399 C CG  . LEU F 2 118 ? -39.609 18.529  8.777   1.00 55.60  ? 118 LEU F CG  1 
ATOM   11400 C CD1 . LEU F 2 118 ? -39.217 17.082  9.026   1.00 63.41  ? 118 LEU F CD1 1 
ATOM   11401 C CD2 . LEU F 2 118 ? -39.977 18.739  7.323   1.00 54.16  ? 118 LEU F CD2 1 
ATOM   11402 N N   . TYR F 2 119 ? -43.128 20.379  11.189  1.00 29.71  ? 119 TYR F N   1 
ATOM   11403 C CA  . TYR F 2 119 ? -44.514 20.446  11.634  1.00 33.75  ? 119 TYR F CA  1 
ATOM   11404 C C   . TYR F 2 119 ? -45.202 21.706  11.119  1.00 43.58  ? 119 TYR F C   1 
ATOM   11405 O O   . TYR F 2 119 ? -46.327 21.641  10.610  1.00 52.34  ? 119 TYR F O   1 
ATOM   11406 C CB  . TYR F 2 119 ? -44.561 20.390  13.160  1.00 32.16  ? 119 TYR F CB  1 
ATOM   11407 C CG  . TYR F 2 119 ? -45.950 20.460  13.746  1.00 46.94  ? 119 TYR F CG  1 
ATOM   11408 C CD1 . TYR F 2 119 ? -46.706 19.308  13.923  1.00 36.57  ? 119 TYR F CD1 1 
ATOM   11409 C CD2 . TYR F 2 119 ? -46.505 21.675  14.128  1.00 41.92  ? 119 TYR F CD2 1 
ATOM   11410 C CE1 . TYR F 2 119 ? -47.973 19.362  14.464  1.00 43.60  ? 119 TYR F CE1 1 
ATOM   11411 C CE2 . TYR F 2 119 ? -47.781 21.741  14.666  1.00 50.80  ? 119 TYR F CE2 1 
ATOM   11412 C CZ  . TYR F 2 119 ? -48.507 20.579  14.831  1.00 49.36  ? 119 TYR F CZ  1 
ATOM   11413 O OH  . TYR F 2 119 ? -49.770 20.631  15.366  1.00 54.16  ? 119 TYR F OH  1 
ATOM   11414 N N   . ASP F 2 120 ? -44.537 22.858  11.226  1.00 49.57  ? 120 ASP F N   1 
ATOM   11415 C CA  . ASP F 2 120 ? -45.177 24.117  10.853  1.00 51.51  ? 120 ASP F CA  1 
ATOM   11416 C C   . ASP F 2 120 ? -45.487 24.169  9.363   1.00 49.37  ? 120 ASP F C   1 
ATOM   11417 O O   . ASP F 2 120 ? -46.533 24.694  8.965   1.00 47.53  ? 120 ASP F O   1 
ATOM   11418 C CB  . ASP F 2 120 ? -44.302 25.297  11.267  1.00 34.34  ? 120 ASP F CB  1 
ATOM   11419 C CG  . ASP F 2 120 ? -44.473 25.654  12.732  1.00 47.24  ? 120 ASP F CG  1 
ATOM   11420 O OD1 . ASP F 2 120 ? -45.591 25.471  13.261  1.00 59.75  ? 120 ASP F OD1 1 
ATOM   11421 O OD2 . ASP F 2 120 ? -43.495 26.114  13.358  1.00 55.65  ? 120 ASP F OD2 1 
ATOM   11422 N N   . LYS F 2 121 ? -44.597 23.624  8.525   1.00 41.75  ? 121 LYS F N   1 
ATOM   11423 C CA  . LYS F 2 121 ? -44.848 23.607  7.085   1.00 48.90  ? 121 LYS F CA  1 
ATOM   11424 C C   . LYS F 2 121 ? -46.126 22.844  6.753   1.00 59.03  ? 121 LYS F C   1 
ATOM   11425 O O   . LYS F 2 121 ? -46.896 23.256  5.876   1.00 58.66  ? 121 LYS F O   1 
ATOM   11426 C CB  . LYS F 2 121 ? -43.662 22.989  6.348   1.00 41.31  ? 121 LYS F CB  1 
ATOM   11427 C CG  . LYS F 2 121 ? -42.388 23.787  6.431   1.00 49.24  ? 121 LYS F CG  1 
ATOM   11428 C CD  . LYS F 2 121 ? -41.684 23.824  5.088   1.00 69.97  ? 121 LYS F CD  1 
ATOM   11429 C CE  . LYS F 2 121 ? -41.103 22.464  4.728   1.00 76.95  ? 121 LYS F CE  1 
ATOM   11430 N NZ  . LYS F 2 121 ? -40.562 21.749  5.918   1.00 69.51  ? 121 LYS F NZ  1 
ATOM   11431 N N   . VAL F 2 122 ? -46.359 21.720  7.434   1.00 55.75  ? 122 VAL F N   1 
ATOM   11432 C CA  . VAL F 2 122 ? -47.579 20.951  7.214   1.00 51.98  ? 122 VAL F CA  1 
ATOM   11433 C C   . VAL F 2 122 ? -48.799 21.737  7.674   1.00 42.76  ? 122 VAL F C   1 
ATOM   11434 O O   . VAL F 2 122 ? -49.838 21.739  7.006   1.00 59.68  ? 122 VAL F O   1 
ATOM   11435 C CB  . VAL F 2 122 ? -47.476 19.587  7.921   1.00 47.94  ? 122 VAL F CB  1 
ATOM   11436 C CG1 . VAL F 2 122 ? -48.804 18.847  7.880   1.00 37.16  ? 122 VAL F CG1 1 
ATOM   11437 C CG2 . VAL F 2 122 ? -46.379 18.753  7.285   1.00 38.54  ? 122 VAL F CG2 1 
ATOM   11438 N N   . ARG F 2 123 ? -48.695 22.417  8.819   1.00 42.19  ? 123 ARG F N   1 
ATOM   11439 C CA  . ARG F 2 123 ? -49.851 23.121  9.367   1.00 39.80  ? 123 ARG F CA  1 
ATOM   11440 C C   . ARG F 2 123 ? -50.313 24.250  8.450   1.00 59.08  ? 123 ARG F C   1 
ATOM   11441 O O   . ARG F 2 123 ? -51.520 24.453  8.270   1.00 70.35  ? 123 ARG F O   1 
ATOM   11442 C CB  . ARG F 2 123 ? -49.526 23.660  10.757  1.00 36.51  ? 123 ARG F CB  1 
ATOM   11443 C CG  . ARG F 2 123 ? -50.605 24.571  11.319  1.00 38.11  ? 123 ARG F CG  1 
ATOM   11444 C CD  . ARG F 2 123 ? -50.177 25.198  12.638  1.00 53.18  ? 123 ARG F CD  1 
ATOM   11445 N NE  . ARG F 2 123 ? -48.902 25.903  12.538  1.00 70.32  ? 123 ARG F NE  1 
ATOM   11446 C CZ  . ARG F 2 123 ? -48.683 26.997  11.816  1.00 67.47  ? 123 ARG F CZ  1 
ATOM   11447 N NH1 . ARG F 2 123 ? -49.649 27.579  11.122  1.00 61.55  ? 123 ARG F NH1 1 
ATOM   11448 N NH2 . ARG F 2 123 ? -47.462 27.523  11.792  1.00 67.66  ? 123 ARG F NH2 1 
ATOM   11449 N N   . LEU F 2 124 ? -49.370 24.999  7.866   1.00 51.02  ? 124 LEU F N   1 
ATOM   11450 C CA  . LEU F 2 124 ? -49.744 26.089  6.966   1.00 56.04  ? 124 LEU F CA  1 
ATOM   11451 C C   . LEU F 2 124 ? -50.447 25.566  5.720   1.00 66.11  ? 124 LEU F C   1 
ATOM   11452 O O   . LEU F 2 124 ? -51.406 26.181  5.237   1.00 72.37  ? 124 LEU F O   1 
ATOM   11453 C CB  . LEU F 2 124 ? -48.515 26.913  6.577   1.00 59.50  ? 124 LEU F CB  1 
ATOM   11454 C CG  . LEU F 2 124 ? -47.669 27.478  7.721   1.00 67.13  ? 124 LEU F CG  1 
ATOM   11455 C CD1 . LEU F 2 124 ? -46.184 27.500  7.354   1.00 68.85  ? 124 LEU F CD1 1 
ATOM   11456 C CD2 . LEU F 2 124 ? -48.155 28.863  8.114   1.00 70.97  ? 124 LEU F CD2 1 
ATOM   11457 N N   . GLN F 2 125 ? -49.981 24.438  5.179   1.00 52.69  ? 125 GLN F N   1 
ATOM   11458 C CA  . GLN F 2 125 ? -50.636 23.844  4.016   1.00 58.16  ? 125 GLN F CA  1 
ATOM   11459 C C   . GLN F 2 125 ? -52.063 23.418  4.338   1.00 66.90  ? 125 GLN F C   1 
ATOM   11460 O O   . GLN F 2 125 ? -53.006 23.761  3.614   1.00 71.37  ? 125 GLN F O   1 
ATOM   11461 C CB  . GLN F 2 125 ? -49.838 22.642  3.523   1.00 56.34  ? 125 GLN F CB  1 
ATOM   11462 C CG  . GLN F 2 125 ? -48.502 22.970  2.911   1.00 41.26  ? 125 GLN F CG  1 
ATOM   11463 C CD  . GLN F 2 125 ? -47.869 21.743  2.296   1.00 56.07  ? 125 GLN F CD  1 
ATOM   11464 O OE1 . GLN F 2 125 ? -48.166 21.387  1.158   1.00 62.70  ? 125 GLN F OE1 1 
ATOM   11465 N NE2 . GLN F 2 125 ? -47.006 21.076  3.053   1.00 61.36  ? 125 GLN F NE2 1 
ATOM   11466 N N   . LEU F 2 126 ? -52.239 22.663  5.424   1.00 55.36  ? 126 LEU F N   1 
ATOM   11467 C CA  . LEU F 2 126 ? -53.528 22.030  5.687   1.00 62.76  ? 126 LEU F CA  1 
ATOM   11468 C C   . LEU F 2 126 ? -54.588 23.048  6.089   1.00 64.09  ? 126 LEU F C   1 
ATOM   11469 O O   . LEU F 2 126 ? -55.752 22.923  5.689   1.00 60.67  ? 126 LEU F O   1 
ATOM   11470 C CB  . LEU F 2 126 ? -53.373 20.957  6.764   1.00 43.81  ? 126 LEU F CB  1 
ATOM   11471 C CG  . LEU F 2 126 ? -52.394 19.831  6.422   1.00 57.22  ? 126 LEU F CG  1 
ATOM   11472 C CD1 . LEU F 2 126 ? -52.526 18.687  7.415   1.00 52.92  ? 126 LEU F CD1 1 
ATOM   11473 C CD2 . LEU F 2 126 ? -52.597 19.338  4.992   1.00 55.43  ? 126 LEU F CD2 1 
ATOM   11474 N N   . ARG F 2 127 ? -54.211 24.046  6.886   1.00 60.47  ? 127 ARG F N   1 
ATOM   11475 C CA  . ARG F 2 127 ? -55.130 25.088  7.373   1.00 68.90  ? 127 ARG F CA  1 
ATOM   11476 C C   . ARG F 2 127 ? -56.274 24.389  8.105   1.00 63.15  ? 127 ARG F C   1 
ATOM   11477 O O   . ARG F 2 127 ? -56.010 23.511  8.943   1.00 64.22  ? 127 ARG F O   1 
ATOM   11478 C CB  . ARG F 2 127 ? -55.551 25.990  6.216   1.00 70.61  ? 127 ARG F CB  1 
ATOM   11479 C CG  . ARG F 2 127 ? -54.587 27.121  5.899   1.00 63.90  ? 127 ARG F CG  1 
ATOM   11480 C CD  . ARG F 2 127 ? -54.543 27.361  4.399   1.00 70.28  ? 127 ARG F CD  1 
ATOM   11481 N NE  . ARG F 2 127 ? -53.183 27.527  3.904   1.00 77.65  ? 127 ARG F NE  1 
ATOM   11482 C CZ  . ARG F 2 127 ? -52.867 27.732  2.633   1.00 82.49  ? 127 ARG F CZ  1 
ATOM   11483 N NH1 . ARG F 2 127 ? -53.793 27.777  1.689   1.00 86.72  ? 127 ARG F NH1 1 
ATOM   11484 N NH2 . ARG F 2 127 ? -51.589 27.892  2.299   1.00 72.51  ? 127 ARG F NH2 1 
ATOM   11485 N N   . ASP F 2 128 ? -57.533 24.724  7.828   1.00 62.21  ? 128 ASP F N   1 
ATOM   11486 C CA  . ASP F 2 128 ? -58.671 24.106  8.494   1.00 59.40  ? 128 ASP F CA  1 
ATOM   11487 C C   . ASP F 2 128 ? -59.181 22.866  7.768   1.00 61.99  ? 128 ASP F C   1 
ATOM   11488 O O   . ASP F 2 128 ? -60.166 22.266  8.212   1.00 65.87  ? 128 ASP F O   1 
ATOM   11489 C CB  . ASP F 2 128 ? -59.809 25.124  8.660   1.00 66.34  ? 128 ASP F CB  1 
ATOM   11490 C CG  . ASP F 2 128 ? -60.260 25.732  7.342   1.00 58.65  ? 128 ASP F CG  1 
ATOM   11491 O OD1 . ASP F 2 128 ? -59.546 25.593  6.328   1.00 62.55  ? 128 ASP F OD1 1 
ATOM   11492 O OD2 . ASP F 2 128 ? -61.343 26.350  7.324   1.00 64.69  ? 128 ASP F OD2 1 
ATOM   11493 N N   . ASN F 2 129 ? -58.535 22.465  6.670   1.00 65.74  ? 129 ASN F N   1 
ATOM   11494 C CA  . ASN F 2 129 ? -58.861 21.191  6.043   1.00 56.72  ? 129 ASN F CA  1 
ATOM   11495 C C   . ASN F 2 129 ? -58.523 20.008  6.940   1.00 61.90  ? 129 ASN F C   1 
ATOM   11496 O O   . ASN F 2 129 ? -59.014 18.901  6.698   1.00 60.13  ? 129 ASN F O   1 
ATOM   11497 C CB  . ASN F 2 129 ? -58.127 21.053  4.710   1.00 54.49  ? 129 ASN F CB  1 
ATOM   11498 C CG  . ASN F 2 129 ? -58.869 21.710  3.571   1.00 58.86  ? 129 ASN F CG  1 
ATOM   11499 O OD1 . ASN F 2 129 ? -59.904 22.343  3.779   1.00 69.80  ? 129 ASN F OD1 1 
ATOM   11500 N ND2 . ASN F 2 129 ? -58.351 21.558  2.356   1.00 50.78  ? 129 ASN F ND2 1 
ATOM   11501 N N   . ALA F 2 130 ? -57.688 20.211  7.957   1.00 57.48  ? 130 ALA F N   1 
ATOM   11502 C CA  . ALA F 2 130 ? -57.364 19.169  8.917   1.00 59.84  ? 130 ALA F CA  1 
ATOM   11503 C C   . ALA F 2 130 ? -57.328 19.770  10.312  1.00 61.79  ? 130 ALA F C   1 
ATOM   11504 O O   . ALA F 2 130 ? -57.084 20.967  10.485  1.00 62.47  ? 130 ALA F O   1 
ATOM   11505 C CB  . ALA F 2 130 ? -56.024 18.494  8.599   1.00 53.58  ? 130 ALA F CB  1 
ATOM   11506 N N   . LYS F 2 131 ? -57.564 18.922  11.305  1.00 62.45  ? 131 LYS F N   1 
ATOM   11507 C CA  . LYS F 2 131 ? -57.592 19.328  12.702  1.00 58.62  ? 131 LYS F CA  1 
ATOM   11508 C C   . LYS F 2 131 ? -56.233 19.070  13.342  1.00 58.61  ? 131 LYS F C   1 
ATOM   11509 O O   . LYS F 2 131 ? -55.688 17.968  13.223  1.00 60.96  ? 131 LYS F O   1 
ATOM   11510 C CB  . LYS F 2 131 ? -58.687 18.570  13.454  1.00 60.74  ? 131 LYS F CB  1 
ATOM   11511 C CG  . LYS F 2 131 ? -58.611 18.691  14.968  1.00 73.20  ? 131 LYS F CG  1 
ATOM   11512 C CD  . LYS F 2 131 ? -59.834 18.080  15.642  1.00 87.24  ? 131 LYS F CD  1 
ATOM   11513 C CE  . LYS F 2 131 ? -60.081 18.711  17.011  1.00 93.67  ? 131 LYS F CE  1 
ATOM   11514 N NZ  . LYS F 2 131 ? -60.226 17.708  18.102  1.00 88.20  ? 131 LYS F NZ  1 
ATOM   11515 N N   . GLU F 2 132 ? -55.686 20.089  14.007  1.00 61.76  ? 132 GLU F N   1 
ATOM   11516 C CA  . GLU F 2 132 ? -54.482 19.913  14.812  1.00 54.20  ? 132 GLU F CA  1 
ATOM   11517 C C   . GLU F 2 132 ? -54.828 19.130  16.070  1.00 52.57  ? 132 GLU F C   1 
ATOM   11518 O O   . GLU F 2 132 ? -55.673 19.559  16.862  1.00 71.38  ? 132 GLU F O   1 
ATOM   11519 C CB  . GLU F 2 132 ? -53.888 21.265  15.194  1.00 57.69  ? 132 GLU F CB  1 
ATOM   11520 C CG  . GLU F 2 132 ? -52.855 21.814  14.242  1.00 59.55  ? 132 GLU F CG  1 
ATOM   11521 C CD  . GLU F 2 132 ? -52.121 23.011  14.822  1.00 63.88  ? 132 GLU F CD  1 
ATOM   11522 O OE1 . GLU F 2 132 ? -52.728 24.100  14.894  1.00 67.22  ? 132 GLU F OE1 1 
ATOM   11523 O OE2 . GLU F 2 132 ? -50.940 22.869  15.202  1.00 58.91  ? 132 GLU F OE2 1 
ATOM   11524 N N   . LEU F 2 133 ? -54.177 17.988  16.262  1.00 54.61  ? 133 LEU F N   1 
ATOM   11525 C CA  . LEU F 2 133 ? -54.454 17.171  17.434  1.00 58.43  ? 133 LEU F CA  1 
ATOM   11526 C C   . LEU F 2 133 ? -53.697 17.630  18.672  1.00 59.39  ? 133 LEU F C   1 
ATOM   11527 O O   . LEU F 2 133 ? -54.045 17.208  19.781  1.00 59.88  ? 133 LEU F O   1 
ATOM   11528 C CB  . LEU F 2 133 ? -54.118 15.702  17.148  1.00 63.49  ? 133 LEU F CB  1 
ATOM   11529 C CG  . LEU F 2 133 ? -55.196 14.856  16.462  1.00 55.70  ? 133 LEU F CG  1 
ATOM   11530 C CD1 . LEU F 2 133 ? -56.514 14.999  17.196  1.00 53.54  ? 133 LEU F CD1 1 
ATOM   11531 C CD2 . LEU F 2 133 ? -55.354 15.224  15.002  1.00 55.61  ? 133 LEU F CD2 1 
ATOM   11532 N N   . GLY F 2 134 ? -52.682 18.476  18.514  1.00 54.50  ? 134 GLY F N   1 
ATOM   11533 C CA  . GLY F 2 134 ? -51.857 18.871  19.635  1.00 59.37  ? 134 GLY F CA  1 
ATOM   11534 C C   . GLY F 2 134 ? -50.806 17.863  20.040  1.00 56.85  ? 134 GLY F C   1 
ATOM   11535 O O   . GLY F 2 134 ? -50.148 18.059  21.067  1.00 65.21  ? 134 GLY F O   1 
ATOM   11536 N N   . ASN F 2 135 ? -50.631 16.786  19.272  1.00 50.23  ? 135 ASN F N   1 
ATOM   11537 C CA  . ASN F 2 135 ? -49.610 15.782  19.554  1.00 52.37  ? 135 ASN F CA  1 
ATOM   11538 C C   . ASN F 2 135 ? -48.649 15.590  18.390  1.00 49.32  ? 135 ASN F C   1 
ATOM   11539 O O   . ASN F 2 135 ? -47.860 14.636  18.397  1.00 43.60  ? 135 ASN F O   1 
ATOM   11540 C CB  . ASN F 2 135 ? -50.255 14.442  19.915  1.00 46.26  ? 135 ASN F CB  1 
ATOM   11541 C CG  . ASN F 2 135 ? -51.284 13.998  18.896  1.00 61.30  ? 135 ASN F CG  1 
ATOM   11542 O OD1 . ASN F 2 135 ? -51.233 14.397  17.730  1.00 55.92  ? 135 ASN F OD1 1 
ATOM   11543 N ND2 . ASN F 2 135 ? -52.224 13.166  19.329  1.00 57.62  ? 135 ASN F ND2 1 
ATOM   11544 N N   . GLY F 2 136 ? -48.686 16.470  17.395  1.00 46.54  ? 136 GLY F N   1 
ATOM   11545 C CA  . GLY F 2 136 ? -47.877 16.312  16.207  1.00 48.10  ? 136 GLY F CA  1 
ATOM   11546 C C   . GLY F 2 136 ? -48.586 15.649  15.051  1.00 41.28  ? 136 GLY F C   1 
ATOM   11547 O O   . GLY F 2 136 ? -47.960 15.435  14.006  1.00 45.56  ? 136 GLY F O   1 
ATOM   11548 N N   . CYS F 2 137 ? -49.867 15.326  15.201  1.00 43.40  ? 137 CYS F N   1 
ATOM   11549 C CA  . CYS F 2 137 ? -50.656 14.682  14.164  1.00 46.92  ? 137 CYS F CA  1 
ATOM   11550 C C   . CYS F 2 137 ? -51.743 15.625  13.667  1.00 44.11  ? 137 CYS F C   1 
ATOM   11551 O O   . CYS F 2 137 ? -52.180 16.530  14.383  1.00 47.42  ? 137 CYS F O   1 
ATOM   11552 C CB  . CYS F 2 137 ? -51.288 13.387  14.683  1.00 47.39  ? 137 CYS F CB  1 
ATOM   11553 S SG  . CYS F 2 137 ? -50.084 12.097  15.121  1.00 68.17  ? 137 CYS F SG  1 
ATOM   11554 N N   . PHE F 2 138 ? -52.165 15.407  12.424  1.00 45.02  ? 138 PHE F N   1 
ATOM   11555 C CA  . PHE F 2 138 ? -53.261 16.145  11.808  1.00 45.29  ? 138 PHE F CA  1 
ATOM   11556 C C   . PHE F 2 138 ? -54.307 15.148  11.332  1.00 50.34  ? 138 PHE F C   1 
ATOM   11557 O O   . PHE F 2 138 ? -53.986 14.233  10.570  1.00 48.48  ? 138 PHE F O   1 
ATOM   11558 C CB  . PHE F 2 138 ? -52.774 16.987  10.626  1.00 38.65  ? 138 PHE F CB  1 
ATOM   11559 C CG  . PHE F 2 138 ? -51.842 18.096  11.008  1.00 54.57  ? 138 PHE F CG  1 
ATOM   11560 C CD1 . PHE F 2 138 ? -50.495 17.843  11.228  1.00 49.14  ? 138 PHE F CD1 1 
ATOM   11561 C CD2 . PHE F 2 138 ? -52.305 19.397  11.131  1.00 46.18  ? 138 PHE F CD2 1 
ATOM   11562 C CE1 . PHE F 2 138 ? -49.632 18.865  11.572  1.00 46.63  ? 138 PHE F CE1 1 
ATOM   11563 C CE2 . PHE F 2 138 ? -51.443 20.424  11.474  1.00 41.74  ? 138 PHE F CE2 1 
ATOM   11564 C CZ  . PHE F 2 138 ? -50.108 20.156  11.699  1.00 42.31  ? 138 PHE F CZ  1 
ATOM   11565 N N   . GLU F 2 139 ? -55.553 15.332  11.766  1.00 61.24  ? 139 GLU F N   1 
ATOM   11566 C CA  . GLU F 2 139 ? -56.666 14.507  11.304  1.00 54.22  ? 139 GLU F CA  1 
ATOM   11567 C C   . GLU F 2 139 ? -57.353 15.225  10.151  1.00 46.65  ? 139 GLU F C   1 
ATOM   11568 O O   . GLU F 2 139 ? -57.971 16.275  10.346  1.00 57.37  ? 139 GLU F O   1 
ATOM   11569 C CB  . GLU F 2 139 ? -57.656 14.221  12.431  1.00 51.40  ? 139 GLU F CB  1 
ATOM   11570 C CG  . GLU F 2 139 ? -58.681 13.146  12.083  1.00 57.54  ? 139 GLU F CG  1 
ATOM   11571 C CD  . GLU F 2 139 ? -59.938 13.220  12.932  1.00 81.51  ? 139 GLU F CD  1 
ATOM   11572 O OE1 . GLU F 2 139 ? -59.862 12.907  14.140  1.00 87.95  ? 139 GLU F OE1 1 
ATOM   11573 O OE2 . GLU F 2 139 ? -61.003 13.585  12.387  1.00 82.92  ? 139 GLU F OE2 1 
ATOM   11574 N N   . PHE F 2 140 ? -57.249 14.658  8.955   1.00 49.50  ? 140 PHE F N   1 
ATOM   11575 C CA  . PHE F 2 140 ? -57.879 15.259  7.790   1.00 54.35  ? 140 PHE F CA  1 
ATOM   11576 C C   . PHE F 2 140 ? -59.396 15.209  7.908   1.00 63.90  ? 140 PHE F C   1 
ATOM   11577 O O   . PHE F 2 140 ? -59.972 14.208  8.347   1.00 60.20  ? 140 PHE F O   1 
ATOM   11578 C CB  . PHE F 2 140 ? -57.443 14.536  6.520   1.00 58.33  ? 140 PHE F CB  1 
ATOM   11579 C CG  . PHE F 2 140 ? -56.060 14.875  6.079   1.00 56.45  ? 140 PHE F CG  1 
ATOM   11580 C CD1 . PHE F 2 140 ? -54.965 14.269  6.672   1.00 48.35  ? 140 PHE F CD1 1 
ATOM   11581 C CD2 . PHE F 2 140 ? -55.852 15.792  5.063   1.00 43.24  ? 140 PHE F CD2 1 
ATOM   11582 C CE1 . PHE F 2 140 ? -53.681 14.575  6.263   1.00 52.37  ? 140 PHE F CE1 1 
ATOM   11583 C CE2 . PHE F 2 140 ? -54.573 16.102  4.646   1.00 53.10  ? 140 PHE F CE2 1 
ATOM   11584 C CZ  . PHE F 2 140 ? -53.484 15.493  5.249   1.00 54.55  ? 140 PHE F CZ  1 
ATOM   11585 N N   . TYR F 2 141 ? -60.041 16.304  7.511   1.00 63.89  ? 141 TYR F N   1 
ATOM   11586 C CA  . TYR F 2 141 ? -61.490 16.362  7.393   1.00 58.19  ? 141 TYR F CA  1 
ATOM   11587 C C   . TYR F 2 141 ? -61.985 15.812  6.064   1.00 61.69  ? 141 TYR F C   1 
ATOM   11588 O O   . TYR F 2 141 ? -63.200 15.733  5.856   1.00 70.63  ? 141 TYR F O   1 
ATOM   11589 C CB  . TYR F 2 141 ? -61.971 17.804  7.567   1.00 64.59  ? 141 TYR F CB  1 
ATOM   11590 C CG  . TYR F 2 141 ? -62.008 18.271  9.003   1.00 67.21  ? 141 TYR F CG  1 
ATOM   11591 C CD1 . TYR F 2 141 ? -62.664 17.530  9.975   1.00 71.16  ? 141 TYR F CD1 1 
ATOM   11592 C CD2 . TYR F 2 141 ? -61.389 19.456  9.387   1.00 64.44  ? 141 TYR F CD2 1 
ATOM   11593 C CE1 . TYR F 2 141 ? -62.706 17.952  11.289  1.00 75.07  ? 141 TYR F CE1 1 
ATOM   11594 C CE2 . TYR F 2 141 ? -61.425 19.889  10.700  1.00 57.36  ? 141 TYR F CE2 1 
ATOM   11595 C CZ  . TYR F 2 141 ? -62.085 19.131  11.646  1.00 70.73  ? 141 TYR F CZ  1 
ATOM   11596 O OH  . TYR F 2 141 ? -62.128 19.550  12.956  1.00 74.55  ? 141 TYR F OH  1 
ATOM   11597 N N   . HIS F 2 142 ? -61.077 15.446  5.163   1.00 54.86  ? 142 HIS F N   1 
ATOM   11598 C CA  . HIS F 2 142 ? -61.414 14.875  3.869   1.00 57.70  ? 142 HIS F CA  1 
ATOM   11599 C C   . HIS F 2 142 ? -60.605 13.602  3.660   1.00 54.82  ? 142 HIS F C   1 
ATOM   11600 O O   . HIS F 2 142 ? -59.690 13.288  4.429   1.00 61.54  ? 142 HIS F O   1 
ATOM   11601 C CB  . HIS F 2 142 ? -61.145 15.870  2.732   1.00 55.57  ? 142 HIS F CB  1 
ATOM   11602 C CG  . HIS F 2 142 ? -59.703 16.251  2.595   1.00 62.06  ? 142 HIS F CG  1 
ATOM   11603 N ND1 . HIS F 2 142 ? -58.834 15.585  1.757   1.00 61.75  ? 142 HIS F ND1 1 
ATOM   11604 C CD2 . HIS F 2 142 ? -58.977 17.224  3.196   1.00 55.15  ? 142 HIS F CD2 1 
ATOM   11605 C CE1 . HIS F 2 142 ? -57.636 16.134  1.845   1.00 63.71  ? 142 HIS F CE1 1 
ATOM   11606 N NE2 . HIS F 2 142 ? -57.696 17.132  2.710   1.00 56.50  ? 142 HIS F NE2 1 
ATOM   11607 N N   . LYS F 2 143 ? -60.950 12.861  2.609   1.00 58.03  ? 143 LYS F N   1 
ATOM   11608 C CA  . LYS F 2 143 ? -60.209 11.656  2.261   1.00 60.57  ? 143 LYS F CA  1 
ATOM   11609 C C   . LYS F 2 143 ? -58.884 12.052  1.622   1.00 63.85  ? 143 LYS F C   1 
ATOM   11610 O O   . LYS F 2 143 ? -58.861 12.771  0.616   1.00 60.43  ? 143 LYS F O   1 
ATOM   11611 C CB  . LYS F 2 143 ? -61.021 10.768  1.320   1.00 53.95  ? 143 LYS F CB  1 
ATOM   11612 C CG  . LYS F 2 143 ? -62.091 9.934   2.014   1.00 74.69  ? 143 LYS F CG  1 
ATOM   11613 C CD  . LYS F 2 143 ? -61.585 9.346   3.328   1.00 84.56  ? 143 LYS F CD  1 
ATOM   11614 C CE  . LYS F 2 143 ? -62.729 9.080   4.303   1.00 88.21  ? 143 LYS F CE  1 
ATOM   11615 N NZ  . LYS F 2 143 ? -62.762 10.053  5.435   1.00 81.34  ? 143 LYS F NZ  1 
ATOM   11616 N N   . CYS F 2 144 ? -57.783 11.593  2.206   1.00 59.63  ? 144 CYS F N   1 
ATOM   11617 C CA  . CYS F 2 144 ? -56.445 11.909  1.710   1.00 56.69  ? 144 CYS F CA  1 
ATOM   11618 C C   . CYS F 2 144 ? -55.775 10.584  1.364   1.00 57.84  ? 144 CYS F C   1 
ATOM   11619 O O   . CYS F 2 144 ? -55.352 9.837   2.253   1.00 58.89  ? 144 CYS F O   1 
ATOM   11620 C CB  . CYS F 2 144 ? -55.657 12.713  2.741   1.00 49.59  ? 144 CYS F CB  1 
ATOM   11621 S SG  . CYS F 2 144 ? -54.062 13.361  2.178   1.00 64.12  ? 144 CYS F SG  1 
ATOM   11622 N N   . ASP F 2 145 ? -55.700 10.287  0.070   1.00 56.52  ? 145 ASP F N   1 
ATOM   11623 C CA  . ASP F 2 145 ? -55.160 9.020   -0.398  1.00 59.40  ? 145 ASP F CA  1 
ATOM   11624 C C   . ASP F 2 145 ? -53.633 9.096   -0.431  1.00 58.14  ? 145 ASP F C   1 
ATOM   11625 O O   . ASP F 2 145 ? -53.023 10.081  -0.004  1.00 56.84  ? 145 ASP F O   1 
ATOM   11626 C CB  . ASP F 2 145 ? -55.775 8.657   -1.751  1.00 57.81  ? 145 ASP F CB  1 
ATOM   11627 C CG  . ASP F 2 145 ? -55.203 9.469   -2.903  1.00 70.64  ? 145 ASP F CG  1 
ATOM   11628 O OD1 . ASP F 2 145 ? -54.816 10.638  -2.692  1.00 70.70  ? 145 ASP F OD1 1 
ATOM   11629 O OD2 . ASP F 2 145 ? -55.152 8.932   -4.030  1.00 72.21  ? 145 ASP F OD2 1 
ATOM   11630 N N   . ASN F 2 146 ? -52.993 8.041   -0.942  1.00 51.71  ? 146 ASN F N   1 
ATOM   11631 C CA  . ASN F 2 146 ? -51.535 7.984   -0.924  1.00 49.21  ? 146 ASN F CA  1 
ATOM   11632 C C   . ASN F 2 146 ? -50.909 9.103   -1.747  1.00 64.76  ? 146 ASN F C   1 
ATOM   11633 O O   . ASN F 2 146 ? -49.804 9.556   -1.431  1.00 67.49  ? 146 ASN F O   1 
ATOM   11634 C CB  . ASN F 2 146 ? -51.061 6.624   -1.426  1.00 42.28  ? 146 ASN F CB  1 
ATOM   11635 C CG  . ASN F 2 146 ? -51.005 5.590   -0.323  1.00 53.99  ? 146 ASN F CG  1 
ATOM   11636 O OD1 . ASN F 2 146 ? -51.125 5.919   0.858   1.00 63.06  ? 146 ASN F OD1 1 
ATOM   11637 N ND2 . ASN F 2 146 ? -50.829 4.331   -0.702  1.00 57.58  ? 146 ASN F ND2 1 
ATOM   11638 N N   . GLU F 2 147 ? -51.589 9.560   -2.800  1.00 63.30  ? 147 GLU F N   1 
ATOM   11639 C CA  . GLU F 2 147 ? -51.072 10.676  -3.587  1.00 57.34  ? 147 GLU F CA  1 
ATOM   11640 C C   . GLU F 2 147 ? -51.284 12.006  -2.876  1.00 56.26  ? 147 GLU F C   1 
ATOM   11641 O O   . GLU F 2 147 ? -50.434 12.899  -2.955  1.00 66.78  ? 147 GLU F O   1 
ATOM   11642 C CB  . GLU F 2 147 ? -51.729 10.692  -4.966  1.00 64.94  ? 147 GLU F CB  1 
ATOM   11643 C CG  . GLU F 2 147 ? -50.970 9.896   -6.015  1.00 81.84  ? 147 GLU F CG  1 
ATOM   11644 C CD  . GLU F 2 147 ? -51.561 8.515   -6.240  1.00 95.27  ? 147 GLU F CD  1 
ATOM   11645 O OE1 . GLU F 2 147 ? -52.437 8.104   -5.449  1.00 94.68  ? 147 GLU F OE1 1 
ATOM   11646 O OE2 . GLU F 2 147 ? -51.146 7.840   -7.206  1.00 96.74  ? 147 GLU F OE2 1 
ATOM   11647 N N   . CYS F 2 148 ? -52.417 12.155  -2.189  1.00 60.04  ? 148 CYS F N   1 
ATOM   11648 C CA  . CYS F 2 148 ? -52.649 13.340  -1.371  1.00 44.22  ? 148 CYS F CA  1 
ATOM   11649 C C   . CYS F 2 148 ? -51.617 13.455  -0.253  1.00 57.01  ? 148 CYS F C   1 
ATOM   11650 O O   . CYS F 2 148 ? -51.135 14.554  0.047   1.00 57.57  ? 148 CYS F O   1 
ATOM   11651 C CB  . CYS F 2 148 ? -54.070 13.295  -0.811  1.00 50.42  ? 148 CYS F CB  1 
ATOM   11652 S SG  . CYS F 2 148 ? -54.443 14.470  0.504   1.00 67.45  ? 148 CYS F SG  1 
ATOM   11653 N N   . MET F 2 149 ? -51.257 12.328  0.367   1.00 53.69  ? 149 MET F N   1 
ATOM   11654 C CA  . MET F 2 149 ? -50.260 12.354  1.432   1.00 63.83  ? 149 MET F CA  1 
ATOM   11655 C C   . MET F 2 149 ? -48.903 12.828  0.918   1.00 61.35  ? 149 MET F C   1 
ATOM   11656 O O   . MET F 2 149 ? -48.218 13.614  1.584   1.00 54.32  ? 149 MET F O   1 
ATOM   11657 C CB  . MET F 2 149 ? -50.141 10.969  2.068   1.00 60.73  ? 149 MET F CB  1 
ATOM   11658 C CG  . MET F 2 149 ? -51.383 10.536  2.823   1.00 55.68  ? 149 MET F CG  1 
ATOM   11659 S SD  . MET F 2 149 ? -51.506 11.355  4.423   1.00 58.82  ? 149 MET F SD  1 
ATOM   11660 C CE  . MET F 2 149 ? -53.034 10.661  5.067   1.00 50.49  ? 149 MET F CE  1 
ATOM   11661 N N   . GLU F 2 150 ? -48.499 12.363  -0.268  1.00 56.00  ? 150 GLU F N   1 
ATOM   11662 C CA  . GLU F 2 150 ? -47.229 12.803  -0.837  1.00 62.13  ? 150 GLU F CA  1 
ATOM   11663 C C   . GLU F 2 150 ? -47.248 14.296  -1.140  1.00 62.23  ? 150 GLU F C   1 
ATOM   11664 O O   . GLU F 2 150 ? -46.230 14.980  -0.988  1.00 68.85  ? 150 GLU F O   1 
ATOM   11665 C CB  . GLU F 2 150 ? -46.912 12.003  -2.099  1.00 65.58  ? 150 GLU F CB  1 
ATOM   11666 C CG  . GLU F 2 150 ? -45.670 12.470  -2.840  1.00 78.30  ? 150 GLU F CG  1 
ATOM   11667 C CD  . GLU F 2 150 ? -44.398 12.306  -2.023  1.00 90.06  ? 150 GLU F CD  1 
ATOM   11668 O OE1 . GLU F 2 150 ? -44.191 11.211  -1.455  1.00 86.14  ? 150 GLU F OE1 1 
ATOM   11669 O OE2 . GLU F 2 150 ? -43.602 13.269  -1.955  1.00 89.67  ? 150 GLU F OE2 1 
ATOM   11670 N N   . SER F 2 151 ? -48.400 14.822  -1.564  1.00 63.90  ? 151 SER F N   1 
ATOM   11671 C CA  . SER F 2 151 ? -48.511 16.258  -1.799  1.00 68.69  ? 151 SER F CA  1 
ATOM   11672 C C   . SER F 2 151 ? -48.247 17.043  -0.520  1.00 55.98  ? 151 SER F C   1 
ATOM   11673 O O   . SER F 2 151 ? -47.583 18.085  -0.548  1.00 60.08  ? 151 SER F O   1 
ATOM   11674 C CB  . SER F 2 151 ? -49.890 16.598  -2.372  1.00 60.83  ? 151 SER F CB  1 
ATOM   11675 O OG  . SER F 2 151 ? -50.866 16.733  -1.351  1.00 55.13  ? 151 SER F OG  1 
ATOM   11676 N N   . VAL F 2 152 ? -48.760 16.553  0.611   1.00 52.78  ? 152 VAL F N   1 
ATOM   11677 C CA  . VAL F 2 152 ? -48.474 17.185  1.896   1.00 57.24  ? 152 VAL F CA  1 
ATOM   11678 C C   . VAL F 2 152 ? -46.990 17.073  2.221   1.00 54.72  ? 152 VAL F C   1 
ATOM   11679 O O   . VAL F 2 152 ? -46.380 18.016  2.737   1.00 57.03  ? 152 VAL F O   1 
ATOM   11680 C CB  . VAL F 2 152 ? -49.345 16.561  3.002   1.00 55.59  ? 152 VAL F CB  1 
ATOM   11681 C CG1 . VAL F 2 152 ? -48.948 17.100  4.370   1.00 46.64  ? 152 VAL F CG1 1 
ATOM   11682 C CG2 . VAL F 2 152 ? -50.815 16.816  2.725   1.00 49.79  ? 152 VAL F CG2 1 
ATOM   11683 N N   . ARG F 2 153 ? -46.384 15.924  1.907   1.00 50.10  ? 153 ARG F N   1 
ATOM   11684 C CA  . ARG F 2 153 ? -44.981 15.699  2.242   1.00 58.79  ? 153 ARG F CA  1 
ATOM   11685 C C   . ARG F 2 153 ? -44.052 16.594  1.428   1.00 69.50  ? 153 ARG F C   1 
ATOM   11686 O O   . ARG F 2 153 ? -43.023 17.052  1.940   1.00 61.56  ? 153 ARG F O   1 
ATOM   11687 C CB  . ARG F 2 153 ? -44.618 14.227  2.032   1.00 49.01  ? 153 ARG F CB  1 
ATOM   11688 C CG  . ARG F 2 153 ? -44.989 13.332  3.194   1.00 41.15  ? 153 ARG F CG  1 
ATOM   11689 C CD  . ARG F 2 153 ? -44.272 11.991  3.124   1.00 46.92  ? 153 ARG F CD  1 
ATOM   11690 N NE  . ARG F 2 153 ? -44.696 11.202  1.975   1.00 64.94  ? 153 ARG F NE  1 
ATOM   11691 C CZ  . ARG F 2 153 ? -45.780 10.437  1.949   1.00 67.01  ? 153 ARG F CZ  1 
ATOM   11692 N NH1 . ARG F 2 153 ? -46.575 10.326  3.002   1.00 52.69  ? 153 ARG F NH1 1 
ATOM   11693 N NH2 . ARG F 2 153 ? -46.076 9.770   0.836   1.00 63.14  ? 153 ARG F NH2 1 
ATOM   11694 N N   . ASN F 2 154 ? -44.380 16.844  0.157   1.00 69.13  ? 154 ASN F N   1 
ATOM   11695 C CA  . ASN F 2 154 ? -43.492 17.585  -0.732  1.00 60.95  ? 154 ASN F CA  1 
ATOM   11696 C C   . ASN F 2 154 ? -43.982 19.000  -1.033  1.00 59.41  ? 154 ASN F C   1 
ATOM   11697 O O   . ASN F 2 154 ? -43.449 19.650  -1.937  1.00 69.75  ? 154 ASN F O   1 
ATOM   11698 C CB  . ASN F 2 154 ? -43.254 16.797  -2.030  1.00 67.71  ? 154 ASN F CB  1 
ATOM   11699 C CG  . ASN F 2 154 ? -44.468 16.770  -2.966  1.00 78.63  ? 154 ASN F CG  1 
ATOM   11700 O OD1 . ASN F 2 154 ? -45.533 17.316  -2.674  1.00 68.16  ? 154 ASN F OD1 1 
ATOM   11701 N ND2 . ASN F 2 154 ? -44.291 16.107  -4.110  1.00 84.41  ? 154 ASN F ND2 1 
ATOM   11702 N N   . GLY F 2 155 ? -44.986 19.488  -0.304  1.00 63.63  ? 155 GLY F N   1 
ATOM   11703 C CA  . GLY F 2 155 ? -45.383 20.878  -0.363  1.00 61.25  ? 155 GLY F CA  1 
ATOM   11704 C C   . GLY F 2 155 ? -46.482 21.230  -1.349  1.00 66.96  ? 155 GLY F C   1 
ATOM   11705 O O   . GLY F 2 155 ? -46.994 22.357  -1.299  1.00 69.69  ? 155 GLY F O   1 
ATOM   11706 N N   . THR F 2 156 ? -46.884 20.312  -2.227  1.00 64.84  ? 156 THR F N   1 
ATOM   11707 C CA  . THR F 2 156 ? -47.835 20.623  -3.289  1.00 70.30  ? 156 THR F CA  1 
ATOM   11708 C C   . THR F 2 156 ? -49.274 20.265  -2.923  1.00 63.89  ? 156 THR F C   1 
ATOM   11709 O O   . THR F 2 156 ? -50.072 19.941  -3.808  1.00 64.58  ? 156 THR F O   1 
ATOM   11710 C CB  . THR F 2 156 ? -47.431 19.918  -4.583  1.00 66.34  ? 156 THR F CB  1 
ATOM   11711 O OG1 . THR F 2 156 ? -48.015 18.612  -4.617  1.00 80.41  ? 156 THR F OG1 1 
ATOM   11712 C CG2 . THR F 2 156 ? -45.920 19.793  -4.670  1.00 74.94  ? 156 THR F CG2 1 
ATOM   11713 N N   . TYR F 2 157 ? -49.624 20.323  -1.641  1.00 57.63  ? 157 TYR F N   1 
ATOM   11714 C CA  . TYR F 2 157 ? -50.983 20.004  -1.220  1.00 59.55  ? 157 TYR F CA  1 
ATOM   11715 C C   . TYR F 2 157 ? -51.941 21.098  -1.676  1.00 63.56  ? 157 TYR F C   1 
ATOM   11716 O O   . TYR F 2 157 ? -51.692 22.286  -1.456  1.00 58.91  ? 157 TYR F O   1 
ATOM   11717 C CB  . TYR F 2 157 ? -51.041 19.838  0.297   1.00 58.59  ? 157 TYR F CB  1 
ATOM   11718 C CG  . TYR F 2 157 ? -52.442 19.800  0.876   1.00 63.59  ? 157 TYR F CG  1 
ATOM   11719 C CD1 . TYR F 2 157 ? -53.240 18.672  0.744   1.00 59.56  ? 157 TYR F CD1 1 
ATOM   11720 C CD2 . TYR F 2 157 ? -52.964 20.892  1.559   1.00 50.99  ? 157 TYR F CD2 1 
ATOM   11721 C CE1 . TYR F 2 157 ? -54.518 18.633  1.273   1.00 53.29  ? 157 TYR F CE1 1 
ATOM   11722 C CE2 . TYR F 2 157 ? -54.237 20.861  2.093   1.00 55.27  ? 157 TYR F CE2 1 
ATOM   11723 C CZ  . TYR F 2 157 ? -55.012 19.731  1.945   1.00 58.56  ? 157 TYR F CZ  1 
ATOM   11724 O OH  . TYR F 2 157 ? -56.285 19.695  2.476   1.00 51.83  ? 157 TYR F OH  1 
ATOM   11725 N N   . ASP F 2 158 ? -53.045 20.690  -2.300  1.00 69.52  ? 158 ASP F N   1 
ATOM   11726 C CA  . ASP F 2 158 ? -53.997 21.609  -2.926  1.00 73.39  ? 158 ASP F CA  1 
ATOM   11727 C C   . ASP F 2 158 ? -55.171 21.840  -1.980  1.00 66.04  ? 158 ASP F C   1 
ATOM   11728 O O   . ASP F 2 158 ? -56.098 21.029  -1.913  1.00 70.59  ? 158 ASP F O   1 
ATOM   11729 C CB  . ASP F 2 158 ? -54.466 21.052  -4.266  1.00 76.95  ? 158 ASP F CB  1 
ATOM   11730 C CG  . ASP F 2 158 ? -55.183 22.087  -5.107  1.00 78.81  ? 158 ASP F CG  1 
ATOM   11731 O OD1 . ASP F 2 158 ? -54.903 23.292  -4.938  1.00 81.55  ? 158 ASP F OD1 1 
ATOM   11732 O OD2 . ASP F 2 158 ? -56.024 21.694  -5.941  1.00 86.58  ? 158 ASP F OD2 1 
ATOM   11733 N N   . TYR F 2 159 ? -55.136 22.959  -1.259  1.00 61.86  ? 159 TYR F N   1 
ATOM   11734 C CA  . TYR F 2 159 ? -56.226 23.288  -0.340  1.00 66.94  ? 159 TYR F CA  1 
ATOM   11735 C C   . TYR F 2 159 ? -57.579 23.449  -1.026  1.00 73.82  ? 159 TYR F C   1 
ATOM   11736 O O   . TYR F 2 159 ? -58.565 22.878  -0.527  1.00 76.82  ? 159 TYR F O   1 
ATOM   11737 C CB  . TYR F 2 159 ? -55.862 24.547  0.450   1.00 65.65  ? 159 TYR F CB  1 
ATOM   11738 C CG  . TYR F 2 159 ? -56.907 24.980  1.455   1.00 64.08  ? 159 TYR F CG  1 
ATOM   11739 C CD1 . TYR F 2 159 ? -57.937 25.846  1.096   1.00 62.63  ? 159 TYR F CD1 1 
ATOM   11740 C CD2 . TYR F 2 159 ? -56.854 24.537  2.767   1.00 52.72  ? 159 TYR F CD2 1 
ATOM   11741 C CE1 . TYR F 2 159 ? -58.886 26.249  2.019   1.00 54.20  ? 159 TYR F CE1 1 
ATOM   11742 C CE2 . TYR F 2 159 ? -57.797 24.933  3.695   1.00 62.33  ? 159 TYR F CE2 1 
ATOM   11743 C CZ  . TYR F 2 159 ? -58.810 25.788  3.318   1.00 64.49  ? 159 TYR F CZ  1 
ATOM   11744 O OH  . TYR F 2 159 ? -59.744 26.177  4.251   1.00 55.21  ? 159 TYR F OH  1 
ATOM   11745 N N   . PRO F 2 160 ? -57.722 24.213  -2.119  1.00 77.53  ? 160 PRO F N   1 
ATOM   11746 C CA  . PRO F 2 160 ? -59.070 24.412  -2.682  1.00 81.34  ? 160 PRO F CA  1 
ATOM   11747 C C   . PRO F 2 160 ? -59.736 23.131  -3.152  1.00 78.05  ? 160 PRO F C   1 
ATOM   11748 O O   . PRO F 2 160 ? -60.967 23.025  -3.084  1.00 79.86  ? 160 PRO F O   1 
ATOM   11749 C CB  . PRO F 2 160 ? -58.822 25.381  -3.849  1.00 77.61  ? 160 PRO F CB  1 
ATOM   11750 C CG  . PRO F 2 160 ? -57.389 25.189  -4.200  1.00 74.35  ? 160 PRO F CG  1 
ATOM   11751 C CD  . PRO F 2 160 ? -56.708 24.956  -2.891  1.00 72.12  ? 160 PRO F CD  1 
ATOM   11752 N N   . GLN F 2 161 ? -58.956 22.151  -3.615  1.00 77.11  ? 161 GLN F N   1 
ATOM   11753 C CA  . GLN F 2 161 ? -59.537 20.925  -4.151  1.00 71.40  ? 161 GLN F CA  1 
ATOM   11754 C C   . GLN F 2 161 ? -60.380 20.207  -3.105  1.00 66.71  ? 161 GLN F C   1 
ATOM   11755 O O   . GLN F 2 161 ? -61.456 19.683  -3.416  1.00 78.44  ? 161 GLN F O   1 
ATOM   11756 C CB  . GLN F 2 161 ? -58.424 20.015  -4.667  1.00 56.84  ? 161 GLN F CB  1 
ATOM   11757 C CG  . GLN F 2 161 ? -58.902 18.708  -5.250  1.00 68.75  ? 161 GLN F CG  1 
ATOM   11758 C CD  . GLN F 2 161 ? -57.762 17.876  -5.801  1.00 77.81  ? 161 GLN F CD  1 
ATOM   11759 O OE1 . GLN F 2 161 ? -56.778 18.412  -6.312  1.00 82.84  ? 161 GLN F OE1 1 
ATOM   11760 N NE2 . GLN F 2 161 ? -57.886 16.559  -5.695  1.00 87.77  ? 161 GLN F NE2 1 
ATOM   11761 N N   . TYR F 2 162 ? -59.914 20.185  -1.859  1.00 63.97  ? 162 TYR F N   1 
ATOM   11762 C CA  . TYR F 2 162 ? -60.602 19.507  -0.770  1.00 60.60  ? 162 TYR F CA  1 
ATOM   11763 C C   . TYR F 2 162 ? -61.360 20.457  0.148   1.00 64.53  ? 162 TYR F C   1 
ATOM   11764 O O   . TYR F 2 162 ? -61.954 20.002  1.131   1.00 67.15  ? 162 TYR F O   1 
ATOM   11765 C CB  . TYR F 2 162 ? -59.595 18.696  0.052   1.00 52.99  ? 162 TYR F CB  1 
ATOM   11766 C CG  . TYR F 2 162 ? -58.716 17.798  -0.785  1.00 59.32  ? 162 TYR F CG  1 
ATOM   11767 C CD1 . TYR F 2 162 ? -59.207 16.609  -1.310  1.00 59.05  ? 162 TYR F CD1 1 
ATOM   11768 C CD2 . TYR F 2 162 ? -57.399 18.142  -1.061  1.00 49.41  ? 162 TYR F CD2 1 
ATOM   11769 C CE1 . TYR F 2 162 ? -58.410 15.784  -2.081  1.00 50.42  ? 162 TYR F CE1 1 
ATOM   11770 C CE2 . TYR F 2 162 ? -56.594 17.322  -1.835  1.00 58.30  ? 162 TYR F CE2 1 
ATOM   11771 C CZ  . TYR F 2 162 ? -57.108 16.143  -2.342  1.00 56.70  ? 162 TYR F CZ  1 
ATOM   11772 O OH  . TYR F 2 162 ? -56.321 15.316  -3.110  1.00 58.18  ? 162 TYR F OH  1 
ATOM   11773 N N   . SER F 2 163 ? -61.363 21.760  -0.149  1.00 66.70  ? 163 SER F N   1 
ATOM   11774 C CA  . SER F 2 163 ? -61.981 22.723  0.759   1.00 67.06  ? 163 SER F CA  1 
ATOM   11775 C C   . SER F 2 163 ? -63.460 22.430  0.949   1.00 75.84  ? 163 SER F C   1 
ATOM   11776 O O   . SER F 2 163 ? -63.972 22.483  2.075   1.00 70.91  ? 163 SER F O   1 
ATOM   11777 C CB  . SER F 2 163 ? -61.791 24.143  0.231   1.00 72.29  ? 163 SER F CB  1 
ATOM   11778 O OG  . SER F 2 163 ? -61.885 24.167  -1.181  1.00 78.67  ? 163 SER F OG  1 
ATOM   11779 N N   . GLU F 2 164 ? -64.163 22.123  -0.141  1.00 75.82  ? 164 GLU F N   1 
ATOM   11780 C CA  . GLU F 2 164 ? -65.573 21.766  -0.037  1.00 80.12  ? 164 GLU F CA  1 
ATOM   11781 C C   . GLU F 2 164 ? -65.750 20.525  0.828   1.00 87.61  ? 164 GLU F C   1 
ATOM   11782 O O   . GLU F 2 164 ? -66.343 20.588  1.912   1.00 82.00  ? 164 GLU F O   1 
ATOM   11783 C CB  . GLU F 2 164 ? -66.162 21.546  -1.432  1.00 85.25  ? 164 GLU F CB  1 
ATOM   11784 C CG  . GLU F 2 164 ? -67.679 21.655  -1.501  1.00 93.76  ? 164 GLU F CG  1 
ATOM   11785 C CD  . GLU F 2 164 ? -68.207 22.907  -0.826  1.00 94.90  ? 164 GLU F CD  1 
ATOM   11786 O OE1 . GLU F 2 164 ? -67.798 24.021  -1.219  1.00 98.83  ? 164 GLU F OE1 1 
ATOM   11787 O OE2 . GLU F 2 164 ? -69.034 22.775  0.099   1.00 94.54  ? 164 GLU F OE2 1 
ATOM   11788 N N   . GLU F 2 165 ? -65.190 19.395  0.380   1.00 79.53  ? 165 GLU F N   1 
ATOM   11789 C CA  . GLU F 2 165 ? -65.362 18.131  1.092   1.00 74.29  ? 165 GLU F CA  1 
ATOM   11790 C C   . GLU F 2 165 ? -65.014 18.273  2.567   1.00 74.64  ? 165 GLU F C   1 
ATOM   11791 O O   . GLU F 2 165 ? -65.706 17.724  3.432   1.00 72.37  ? 165 GLU F O   1 
ATOM   11792 C CB  . GLU F 2 165 ? -64.504 17.044  0.440   1.00 61.87  ? 165 GLU F CB  1 
ATOM   11793 C CG  . GLU F 2 165 ? -64.798 15.638  0.949   1.00 62.54  ? 165 GLU F CG  1 
ATOM   11794 C CD  . GLU F 2 165 ? -63.671 14.654  0.663   1.00 62.34  ? 165 GLU F CD  1 
ATOM   11795 O OE1 . GLU F 2 165 ? -62.837 14.924  -0.229  1.00 61.20  ? 165 GLU F OE1 1 
ATOM   11796 O OE2 . GLU F 2 165 ? -63.614 13.609  1.343   1.00 64.03  ? 165 GLU F OE2 1 
ATOM   11797 N N   . ALA F 2 166 ? -63.953 19.022  2.876   1.00 73.11  ? 166 ALA F N   1 
ATOM   11798 C CA  . ALA F 2 166 ? -63.625 19.282  4.273   1.00 72.21  ? 166 ALA F CA  1 
ATOM   11799 C C   . ALA F 2 166 ? -64.742 20.050  4.965   1.00 74.13  ? 166 ALA F C   1 
ATOM   11800 O O   . ALA F 2 166 ? -65.138 19.705  6.083   1.00 72.18  ? 166 ALA F O   1 
ATOM   11801 C CB  . ALA F 2 166 ? -62.307 20.046  4.374   1.00 61.74  ? 166 ALA F CB  1 
ATOM   11802 N N   . ARG F 2 167 ? -65.286 21.073  4.297   1.00 84.94  ? 167 ARG F N   1 
ATOM   11803 C CA  . ARG F 2 167 ? -66.282 21.934  4.930   1.00 86.97  ? 167 ARG F CA  1 
ATOM   11804 C C   . ARG F 2 167 ? -67.525 21.150  5.339   1.00 75.67  ? 167 ARG F C   1 
ATOM   11805 O O   . ARG F 2 167 ? -68.051 21.346  6.442   1.00 73.73  ? 167 ARG F O   1 
ATOM   11806 C CB  . ARG F 2 167 ? -66.661 23.078  3.990   1.00 89.54  ? 167 ARG F CB  1 
ATOM   11807 C CG  . ARG F 2 167 ? -67.830 23.910  4.487   1.00 89.91  ? 167 ARG F CG  1 
ATOM   11808 C CD  . ARG F 2 167 ? -68.268 24.946  3.455   1.00 97.56  ? 167 ARG F CD  1 
ATOM   11809 N NE  . ARG F 2 167 ? -69.157 24.424  2.417   1.00 93.49  ? 167 ARG F NE  1 
ATOM   11810 C CZ  . ARG F 2 167 ? -70.287 23.752  2.617   1.00 89.91  ? 167 ARG F CZ  1 
ATOM   11811 N NH1 . ARG F 2 167 ? -70.744 23.496  3.833   1.00 80.93  ? 167 ARG F NH1 1 
ATOM   11812 N NH2 . ARG F 2 167 ? -70.983 23.333  1.563   1.00 94.77  ? 167 ARG F NH2 1 
ATOM   11813 N N   . LEU F 2 168 ? -68.009 20.255  4.468   1.00 79.22  ? 168 LEU F N   1 
ATOM   11814 C CA  . LEU F 2 168 ? -69.190 19.464  4.804   1.00 75.21  ? 168 LEU F CA  1 
ATOM   11815 C C   . LEU F 2 168 ? -68.949 18.610  6.044   1.00 87.02  ? 168 LEU F C   1 
ATOM   11816 O O   . LEU F 2 168 ? -69.841 18.464  6.889   1.00 92.97  ? 168 LEU F O   1 
ATOM   11817 C CB  . LEU F 2 168 ? -69.609 18.572  3.631   1.00 78.57  ? 168 LEU F CB  1 
ATOM   11818 C CG  . LEU F 2 168 ? -70.249 19.142  2.353   1.00 86.78  ? 168 LEU F CG  1 
ATOM   11819 C CD1 . LEU F 2 168 ? -71.455 20.018  2.677   1.00 76.59  ? 168 LEU F CD1 1 
ATOM   11820 C CD2 . LEU F 2 168 ? -69.265 19.875  1.453   1.00 82.58  ? 168 LEU F CD2 1 
ATOM   11821 N N   . LYS F 2 169 ? -67.751 18.028  6.166   1.00 77.46  ? 169 LYS F N   1 
ATOM   11822 C CA  . LYS F 2 169 ? -67.434 17.204  7.330   1.00 72.43  ? 169 LYS F CA  1 
ATOM   11823 C C   . LYS F 2 169 ? -67.400 18.031  8.610   1.00 82.13  ? 169 LYS F C   1 
ATOM   11824 O O   . LYS F 2 169 ? -67.780 17.540  9.679   1.00 91.80  ? 169 LYS F O   1 
ATOM   11825 C CB  . LYS F 2 169 ? -66.101 16.487  7.113   1.00 74.54  ? 169 LYS F CB  1 
ATOM   11826 C CG  . LYS F 2 169 ? -65.704 15.535  8.238   1.00 75.45  ? 169 LYS F CG  1 
ATOM   11827 C CD  . LYS F 2 169 ? -66.797 14.519  8.526   1.00 76.04  ? 169 LYS F CD  1 
ATOM   11828 C CE  . LYS F 2 169 ? -66.490 13.178  7.884   1.00 68.68  ? 169 LYS F CE  1 
ATOM   11829 N NZ  . LYS F 2 169 ? -67.682 12.279  7.875   1.00 92.43  ? 169 LYS F NZ  1 
ATOM   11830 N N   . ARG F 2 170 ? -66.938 19.285  8.527   1.00 86.54  ? 170 ARG F N   1 
ATOM   11831 C CA  . ARG F 2 170 ? -66.889 20.133  9.716   1.00 89.44  ? 170 ARG F CA  1 
ATOM   11832 C C   . ARG F 2 170 ? -68.277 20.330  10.311  1.00 101.97 ? 170 ARG F C   1 
ATOM   11833 O O   . ARG F 2 170 ? -68.436 20.368  11.537  1.00 110.28 ? 170 ARG F O   1 
ATOM   11834 C CB  . ARG F 2 170 ? -66.253 21.485  9.385   1.00 83.00  ? 170 ARG F CB  1 
ATOM   11835 C CG  . ARG F 2 170 ? -64.964 21.406  8.579   1.00 84.64  ? 170 ARG F CG  1 
ATOM   11836 C CD  . ARG F 2 170 ? -63.998 22.536  8.920   1.00 81.61  ? 170 ARG F CD  1 
ATOM   11837 N NE  . ARG F 2 170 ? -64.458 23.824  8.414   1.00 85.20  ? 170 ARG F NE  1 
ATOM   11838 C CZ  . ARG F 2 170 ? -64.169 24.308  7.213   1.00 86.74  ? 170 ARG F CZ  1 
ATOM   11839 N NH1 . ARG F 2 170 ? -63.418 23.634  6.357   1.00 83.93  ? 170 ARG F NH1 1 
ATOM   11840 N NH2 . ARG F 2 170 ? -64.648 25.499  6.861   1.00 85.13  ? 170 ARG F NH2 1 
ATOM   11841 N N   . GLU F 2 171 ? -69.295 20.462  9.457   1.00 100.90 ? 171 GLU F N   1 
ATOM   11842 C CA  . GLU F 2 171 ? -70.659 20.641  9.944   1.00 113.04 ? 171 GLU F CA  1 
ATOM   11843 C C   . GLU F 2 171 ? -71.170 19.394  10.660  1.00 118.14 ? 171 GLU F C   1 
ATOM   11844 O O   . GLU F 2 171 ? -71.844 19.499  11.693  1.00 119.43 ? 171 GLU F O   1 
ATOM   11845 C CB  . GLU F 2 171 ? -71.580 21.012  8.779   1.00 114.71 ? 171 GLU F CB  1 
ATOM   11846 C CG  . GLU F 2 171 ? -73.068 20.864  9.073   1.00 124.10 ? 171 GLU F CG  1 
ATOM   11847 C CD  . GLU F 2 171 ? -73.622 19.521  8.629   1.00 128.71 ? 171 GLU F CD  1 
ATOM   11848 O OE1 . GLU F 2 171 ? -72.864 18.738  8.017   1.00 125.68 ? 171 GLU F OE1 1 
ATOM   11849 O OE2 . GLU F 2 171 ? -74.811 19.248  8.898   1.00 127.50 ? 171 GLU F OE2 1 
ATOM   11850 N N   . GLU F 2 172 ? -70.863 18.207  10.127  1.00 107.39 ? 172 GLU F N   1 
ATOM   11851 C CA  . GLU F 2 172 ? -71.410 16.971  10.684  1.00 105.58 ? 172 GLU F CA  1 
ATOM   11852 C C   . GLU F 2 172 ? -70.984 16.781  12.134  1.00 115.85 ? 172 GLU F C   1 
ATOM   11853 O O   . GLU F 2 172 ? -71.802 16.435  12.994  1.00 121.08 ? 172 GLU F O   1 
ATOM   11854 C CB  . GLU F 2 172 ? -70.971 15.777  9.836   1.00 103.14 ? 172 GLU F CB  1 
ATOM   11855 C CG  . GLU F 2 172 ? -71.411 15.840  8.386   1.00 102.99 ? 172 GLU F CG  1 
ATOM   11856 C CD  . GLU F 2 172 ? -71.926 14.505  7.880   1.00 113.87 ? 172 GLU F CD  1 
ATOM   11857 O OE1 . GLU F 2 172 ? -71.100 13.675  7.442   1.00 111.28 ? 172 GLU F OE1 1 
ATOM   11858 O OE2 . GLU F 2 172 ? -73.155 14.285  7.927   1.00 103.72 ? 172 GLU F OE2 1 
ATOM   11859 N N   . ILE F 2 173 ? -69.699 16.997  12.424  1.00 118.18 ? 173 ILE F N   1 
ATOM   11860 C CA  . ILE F 2 173 ? -69.228 16.923  13.803  1.00 118.41 ? 173 ILE F CA  1 
ATOM   11861 C C   . ILE F 2 173 ? -69.769 18.090  14.622  1.00 125.61 ? 173 ILE F C   1 
ATOM   11862 O O   . ILE F 2 173 ? -70.047 17.943  15.819  1.00 121.26 ? 173 ILE F O   1 
ATOM   11863 C CB  . ILE F 2 173 ? -67.690 16.865  13.834  1.00 111.64 ? 173 ILE F CB  1 
ATOM   11864 C CG1 . ILE F 2 173 ? -67.180 15.819  12.840  1.00 92.18  ? 173 ILE F CG1 1 
ATOM   11865 C CG2 . ILE F 2 173 ? -67.192 16.556  15.240  1.00 111.61 ? 173 ILE F CG2 1 
ATOM   11866 C CD1 . ILE F 2 173 ? -65.699 15.916  12.547  1.00 89.84  ? 173 ILE F CD1 1 
ATOM   11867 N N   . SER F 2 174 ? -69.925 19.262  13.998  1.00 132.46 ? 174 SER F N   1 
ATOM   11868 C CA  . SER F 2 174 ? -70.422 20.435  14.715  1.00 133.26 ? 174 SER F CA  1 
ATOM   11869 C C   . SER F 2 174 ? -71.853 20.234  15.197  1.00 128.07 ? 174 SER F C   1 
ATOM   11870 O O   . SER F 2 174 ? -72.200 20.630  16.316  1.00 126.58 ? 174 SER F O   1 
ATOM   11871 C CB  . SER F 2 174 ? -70.334 21.673  13.821  1.00 122.90 ? 174 SER F CB  1 
ATOM   11872 O OG  . SER F 2 174 ? -69.052 21.789  13.230  1.00 127.89 ? 174 SER F OG  1 
ATOM   11873 N N   . SER F 2 175 ? -72.699 19.630  14.367  1.00 124.93 ? 175 SER F N   1 
ATOM   11874 C CA  . SER F 2 175 ? -74.109 19.450  14.681  1.00 121.99 ? 175 SER F CA  1 
ATOM   11875 C C   . SER F 2 175 ? -74.379 18.207  15.520  1.00 120.82 ? 175 SER F C   1 
ATOM   11876 O O   . SER F 2 175 ? -75.540 17.806  15.651  1.00 126.90 ? 175 SER F O   1 
ATOM   11877 C CB  . SER F 2 175 ? -74.931 19.393  13.390  1.00 116.52 ? 175 SER F CB  1 
ATOM   11878 O OG  . SER F 2 175 ? -74.878 18.104  12.804  1.00 110.49 ? 175 SER F OG  1 
ATOM   11879 N N   . GLY F 2 176 ? -73.345 17.596  16.091  1.00 120.34 ? 176 GLY F N   1 
ATOM   11880 C CA  . GLY F 2 176 ? -73.538 16.375  16.858  1.00 121.94 ? 176 GLY F CA  1 
ATOM   11881 C C   . GLY F 2 176 ? -74.076 15.228  16.030  1.00 132.26 ? 176 GLY F C   1 
ATOM   11882 O O   . GLY F 2 176 ? -74.947 14.482  16.495  1.00 135.34 ? 176 GLY F O   1 
ATOM   11883 N N   . ARG F 2 177 ? -73.576 15.072  14.807  1.00 135.34 ? 177 ARG F N   1 
ATOM   11884 C CA  . ARG F 2 177 ? -74.058 14.039  13.895  1.00 132.42 ? 177 ARG F CA  1 
ATOM   11885 C C   . ARG F 2 177 ? -72.914 13.137  13.437  1.00 119.41 ? 177 ARG F C   1 
ATOM   11886 O O   . ARG F 2 177 ? -72.966 11.916  13.598  1.00 112.68 ? 177 ARG F O   1 
ATOM   11887 C CB  . ARG F 2 177 ? -74.745 14.677  12.684  1.00 128.12 ? 177 ARG F CB  1 
ATOM   11888 C CG  . ARG F 2 177 ? -76.056 14.021  12.279  1.00 123.80 ? 177 ARG F CG  1 
ATOM   11889 C CD  . ARG F 2 177 ? -76.731 14.804  11.165  1.00 130.13 ? 177 ARG F CD  1 
ATOM   11890 N NE  . ARG F 2 177 ? -76.541 16.242  11.320  1.00 136.85 ? 177 ARG F NE  1 
ATOM   11891 C CZ  . ARG F 2 177 ? -76.591 17.117  10.325  1.00 129.48 ? 177 ARG F CZ  1 
ATOM   11892 N NH1 . ARG F 2 177 ? -76.820 16.734  9.079   1.00 120.80 ? 177 ARG F NH1 1 
ATOM   11893 N NH2 . ARG F 2 177 ? -76.407 18.408  10.585  1.00 123.13 ? 177 ARG F NH2 1 
HETATM 11894 C C1  . NAG G 3 .   ? 27.902  6.095   59.982  1.00 78.18  ? 1   NAG G C1  1 
HETATM 11895 C C2  . NAG G 3 .   ? 28.869  5.460   58.972  1.00 75.11  ? 1   NAG G C2  1 
HETATM 11896 C C3  . NAG G 3 .   ? 28.219  4.220   58.349  1.00 89.51  ? 1   NAG G C3  1 
HETATM 11897 C C4  . NAG G 3 .   ? 27.683  3.254   59.404  1.00 94.61  ? 1   NAG G C4  1 
HETATM 11898 C C5  . NAG G 3 .   ? 26.773  4.040   60.359  1.00 91.18  ? 1   NAG G C5  1 
HETATM 11899 C C6  . NAG G 3 .   ? 26.212  3.239   61.515  1.00 96.30  ? 1   NAG G C6  1 
HETATM 11900 C C7  . NAG G 3 .   ? 30.212  6.276   57.046  1.00 91.70  ? 1   NAG G C7  1 
HETATM 11901 C C8  . NAG G 3 .   ? 30.347  7.428   56.080  1.00 74.37  ? 1   NAG G C8  1 
HETATM 11902 N N2  . NAG G 3 .   ? 29.217  6.409   57.947  1.00 83.09  ? 1   NAG G N2  1 
HETATM 11903 O O3  . NAG G 3 .   ? 29.145  3.606   57.489  1.00 80.28  ? 1   NAG G O3  1 
HETATM 11904 O O4  . NAG G 3 .   ? 26.986  2.249   58.697  1.00 102.50 ? 1   NAG G O4  1 
HETATM 11905 O O5  . NAG G 3 .   ? 27.509  5.113   60.907  1.00 85.22  ? 1   NAG G O5  1 
HETATM 11906 O O6  . NAG G 3 .   ? 27.247  2.476   62.090  1.00 103.45 ? 1   NAG G O6  1 
HETATM 11907 O O7  . NAG G 3 .   ? 30.958  5.306   56.991  1.00 88.76  ? 1   NAG G O7  1 
HETATM 11908 C C1  . NAG G 3 .   ? 27.324  0.923   59.172  1.00 106.47 ? 2   NAG G C1  1 
HETATM 11909 C C2  . NAG G 3 .   ? 26.458  -0.080  58.386  1.00 98.13  ? 2   NAG G C2  1 
HETATM 11910 C C3  . NAG G 3 .   ? 26.808  -1.523  58.752  1.00 110.43 ? 2   NAG G C3  1 
HETATM 11911 C C4  . NAG G 3 .   ? 28.322  -1.750  58.699  1.00 108.09 ? 2   NAG G C4  1 
HETATM 11912 C C5  . NAG G 3 .   ? 29.048  -0.655  59.494  1.00 87.55  ? 2   NAG G C5  1 
HETATM 11913 C C6  . NAG G 3 .   ? 30.555  -0.777  59.463  1.00 85.50  ? 2   NAG G C6  1 
HETATM 11914 C C7  . NAG G 3 .   ? 24.372  0.165   59.745  1.00 106.54 ? 2   NAG G C7  1 
HETATM 11915 C C8  . NAG G 3 .   ? 22.902  0.490   59.624  1.00 98.83  ? 2   NAG G C8  1 
HETATM 11916 N N2  . NAG G 3 .   ? 25.052  0.184   58.578  1.00 94.90  ? 2   NAG G N2  1 
HETATM 11917 O O3  . NAG G 3 .   ? 26.089  -2.358  57.876  1.00 86.66  ? 2   NAG G O3  1 
HETATM 11918 O O4  . NAG G 3 .   ? 28.590  -3.030  59.229  1.00 91.70  ? 2   NAG G O4  1 
HETATM 11919 O O5  . NAG G 3 .   ? 28.689  0.615   58.982  1.00 101.90 ? 2   NAG G O5  1 
HETATM 11920 O O6  . NAG G 3 .   ? 31.015  -0.562  58.152  1.00 80.50  ? 2   NAG G O6  1 
HETATM 11921 O O7  . NAG G 3 .   ? 24.867  -0.092  60.833  1.00 111.66 ? 2   NAG G O7  1 
HETATM 11922 C C1  . NAG H 3 .   ? -57.273 18.270  36.326  1.00 88.02  ? 1   NAG H C1  1 
HETATM 11923 C C2  . NAG H 3 .   ? -57.308 17.871  37.813  1.00 90.86  ? 1   NAG H C2  1 
HETATM 11924 C C3  . NAG H 3 .   ? -58.616 17.150  38.135  1.00 89.60  ? 1   NAG H C3  1 
HETATM 11925 C C4  . NAG H 3 .   ? -59.825 17.976  37.700  1.00 89.12  ? 1   NAG H C4  1 
HETATM 11926 C C5  . NAG H 3 .   ? -59.625 18.474  36.254  1.00 77.31  ? 1   NAG H C5  1 
HETATM 11927 C C6  . NAG H 3 .   ? -60.744 19.373  35.767  1.00 73.84  ? 1   NAG H C6  1 
HETATM 11928 C C7  . NAG H 3 .   ? -55.253 17.416  39.091  1.00 91.05  ? 1   NAG H C7  1 
HETATM 11929 C C8  . NAG H 3 .   ? -54.143 16.416  39.309  1.00 85.84  ? 1   NAG H C8  1 
HETATM 11930 N N2  . NAG H 3 .   ? -56.173 17.060  38.173  1.00 83.32  ? 1   NAG H N2  1 
HETATM 11931 O O3  . NAG H 3 .   ? -58.636 16.870  39.512  1.00 76.67  ? 1   NAG H O3  1 
HETATM 11932 O O4  . NAG H 3 .   ? -60.939 17.113  37.818  1.00 94.79  ? 1   NAG H O4  1 
HETATM 11933 O O5  . NAG H 3 .   ? -58.370 19.133  36.097  1.00 81.21  ? 1   NAG H O5  1 
HETATM 11934 O O6  . NAG H 3 .   ? -61.171 20.212  36.815  1.00 66.68  ? 1   NAG H O6  1 
HETATM 11935 O O7  . NAG H 3 .   ? -55.298 18.468  39.713  1.00 93.22  ? 1   NAG H O7  1 
HETATM 11936 C C1  . NAG H 3 .   ? -61.930 17.623  38.740  1.00 91.18  ? 2   NAG H C1  1 
HETATM 11937 C C2  . NAG H 3 .   ? -63.207 16.782  38.571  1.00 98.32  ? 2   NAG H C2  1 
HETATM 11938 C C3  . NAG H 3 .   ? -64.287 17.264  39.537  1.00 92.78  ? 2   NAG H C3  1 
HETATM 11939 C C4  . NAG H 3 .   ? -63.755 17.278  40.966  1.00 94.50  ? 2   NAG H C4  1 
HETATM 11940 C C5  . NAG H 3 .   ? -62.434 18.060  41.021  1.00 95.76  ? 2   NAG H C5  1 
HETATM 11941 C C6  . NAG H 3 .   ? -61.787 18.059  42.389  1.00 87.98  ? 2   NAG H C6  1 
HETATM 11942 C C7  . NAG H 3 .   ? -63.632 15.775  36.349  1.00 85.07  ? 2   NAG H C7  1 
HETATM 11943 C C8  . NAG H 3 .   ? -63.024 14.502  36.890  1.00 79.27  ? 2   NAG H C8  1 
HETATM 11944 N N2  . NAG H 3 .   ? -63.681 16.812  37.210  1.00 93.12  ? 2   NAG H N2  1 
HETATM 11945 O O3  . NAG H 3 .   ? -65.406 16.431  39.390  1.00 82.07  ? 2   NAG H O3  1 
HETATM 11946 O O4  . NAG H 3 .   ? -64.753 17.871  41.766  1.00 85.94  ? 2   NAG H O4  1 
HETATM 11947 O O5  . NAG H 3 .   ? -61.507 17.536  40.084  1.00 88.97  ? 2   NAG H O5  1 
HETATM 11948 O O6  . NAG H 3 .   ? -62.703 18.549  43.338  1.00 95.14  ? 2   NAG H O6  1 
HETATM 11949 O O7  . NAG H 3 .   ? -64.046 15.842  35.201  1.00 80.70  ? 2   NAG H O7  1 
HETATM 11950 C C1  . NAG I 4 .   ? 43.439  23.879  13.656  1.00 65.40  ? 1   NAG I C1  1 
HETATM 11951 C C2  . NAG I 4 .   ? 43.857  25.317  14.002  1.00 67.01  ? 1   NAG I C2  1 
HETATM 11952 C C3  . NAG I 4 .   ? 43.605  26.254  12.816  1.00 76.33  ? 1   NAG I C3  1 
HETATM 11953 C C4  . NAG I 4 .   ? 44.235  25.728  11.528  1.00 75.52  ? 1   NAG I C4  1 
HETATM 11954 C C5  . NAG I 4 .   ? 43.727  24.293  11.319  1.00 74.84  ? 1   NAG I C5  1 
HETATM 11955 C C6  . NAG I 4 .   ? 44.289  23.559  10.121  1.00 72.15  ? 1   NAG I C6  1 
HETATM 11956 C C7  . NAG I 4 .   ? 43.737  26.294  16.261  1.00 71.42  ? 1   NAG I C7  1 
HETATM 11957 C C8  . NAG I 4 .   ? 42.780  26.773  17.324  1.00 67.37  ? 1   NAG I C8  1 
HETATM 11958 N N2  . NAG I 4 .   ? 43.149  25.818  15.149  1.00 59.69  ? 1   NAG I N2  1 
HETATM 11959 O O3  . NAG I 4 .   ? 44.053  27.542  13.164  1.00 73.66  ? 1   NAG I O3  1 
HETATM 11960 O O4  . NAG I 4 .   ? 43.812  26.610  10.510  1.00 80.09  ? 1   NAG I O4  1 
HETATM 11961 O O5  . NAG I 4 .   ? 44.060  23.514  12.448  1.00 58.62  ? 1   NAG I O5  1 
HETATM 11962 O O6  . NAG I 4 .   ? 45.687  23.468  10.260  1.00 82.44  ? 1   NAG I O6  1 
HETATM 11963 O O7  . NAG I 4 .   ? 44.947  26.342  16.420  1.00 67.15  ? 1   NAG I O7  1 
HETATM 11964 C C1  . NAG I 4 .   ? 44.878  26.942  9.587   1.00 87.83  ? 2   NAG I C1  1 
HETATM 11965 C C2  . NAG I 4 .   ? 44.321  27.948  8.569   1.00 93.56  ? 2   NAG I C2  1 
HETATM 11966 C C3  . NAG I 4 .   ? 45.399  28.297  7.541   1.00 87.24  ? 2   NAG I C3  1 
HETATM 11967 C C4  . NAG I 4 .   ? 46.673  28.787  8.230   1.00 102.56 ? 2   NAG I C4  1 
HETATM 11968 C C5  . NAG I 4 .   ? 47.073  27.782  9.324   1.00 102.07 ? 2   NAG I C5  1 
HETATM 11969 C C6  . NAG I 4 .   ? 48.282  28.206  10.132  1.00 105.79 ? 2   NAG I C6  1 
HETATM 11970 C C7  . NAG I 4 .   ? 42.953  26.347  7.220   1.00 94.48  ? 2   NAG I C7  1 
HETATM 11971 C C8  . NAG I 4 .   ? 41.545  26.119  6.725   1.00 78.99  ? 2   NAG I C8  1 
HETATM 11972 N N2  . NAG I 4 .   ? 43.107  27.465  7.957   1.00 89.70  ? 2   NAG I N2  1 
HETATM 11973 O O3  . NAG I 4 .   ? 44.862  29.257  6.673   1.00 93.83  ? 2   NAG I O3  1 
HETATM 11974 O O4  . NAG I 4 .   ? 47.674  28.912  7.236   1.00 108.47 ? 2   NAG I O4  1 
HETATM 11975 O O5  . NAG I 4 .   ? 45.991  27.545  10.210  1.00 92.76  ? 2   NAG I O5  1 
HETATM 11976 O O6  . NAG I 4 .   ? 48.497  27.300  11.189  1.00 97.11  ? 2   NAG I O6  1 
HETATM 11977 O O7  . NAG I 4 .   ? 43.853  25.564  6.950   1.00 103.07 ? 2   NAG I O7  1 
HETATM 11978 C C1  . BMA I 4 .   ? 48.135  30.286  7.133   1.00 115.56 ? 3   BMA I C1  1 
HETATM 11979 C C2  . BMA I 4 .   ? 49.312  30.306  6.155   1.00 106.78 ? 3   BMA I C2  1 
HETATM 11980 C C3  . BMA I 4 .   ? 49.713  31.757  5.790   1.00 101.68 ? 3   BMA I C3  1 
HETATM 11981 C C4  . BMA I 4 .   ? 48.522  32.645  5.369   1.00 116.53 ? 3   BMA I C4  1 
HETATM 11982 C C5  . BMA I 4 .   ? 47.294  32.462  6.267   1.00 120.04 ? 3   BMA I C5  1 
HETATM 11983 C C6  . BMA I 4 .   ? 45.994  33.043  5.707   1.00 107.97 ? 3   BMA I C6  1 
HETATM 11984 O O2  . BMA I 4 .   ? 48.973  29.545  5.026   1.00 98.86  ? 3   BMA I O2  1 
HETATM 11985 O O3  . BMA I 4 .   ? 50.723  31.667  4.816   1.00 82.77  ? 3   BMA I O3  1 
HETATM 11986 O O4  . BMA I 4 .   ? 49.000  33.976  5.430   1.00 111.14 ? 3   BMA I O4  1 
HETATM 11987 O O5  . BMA I 4 .   ? 47.072  31.123  6.700   1.00 125.10 ? 3   BMA I O5  1 
HETATM 11988 O O6  . BMA I 4 .   ? 45.123  33.260  6.800   1.00 102.12 ? 3   BMA I O6  1 
HETATM 11989 C C1  . NAG J 3 .   ? -45.276 15.949  -5.157  1.00 95.83  ? 1   NAG J C1  1 
HETATM 11990 C C2  . NAG J 3 .   ? -44.648 15.207  -6.345  1.00 102.64 ? 1   NAG J C2  1 
HETATM 11991 C C3  . NAG J 3 .   ? -45.641 15.130  -7.503  1.00 110.16 ? 1   NAG J C3  1 
HETATM 11992 C C4  . NAG J 3 .   ? -46.963 14.517  -7.041  1.00 112.76 ? 1   NAG J C4  1 
HETATM 11993 C C5  . NAG J 3 .   ? -47.449 15.216  -5.755  1.00 95.95  ? 1   NAG J C5  1 
HETATM 11994 C C6  . NAG J 3 .   ? -48.681 14.584  -5.141  1.00 91.77  ? 1   NAG J C6  1 
HETATM 11995 C C7  . NAG J 3 .   ? -42.197 15.372  -6.402  1.00 96.92  ? 1   NAG J C7  1 
HETATM 11996 C C8  . NAG J 3 .   ? -41.034 16.184  -6.918  1.00 89.76  ? 1   NAG J C8  1 
HETATM 11997 N N2  . NAG J 3 .   ? -43.415 15.835  -6.742  1.00 95.17  ? 1   NAG J N2  1 
HETATM 11998 O O3  . NAG J 3 .   ? -45.040 14.396  -8.540  1.00 106.02 ? 1   NAG J O3  1 
HETATM 11999 O O4  . NAG J 3 .   ? -47.868 14.685  -8.115  1.00 119.56 ? 1   NAG J O4  1 
HETATM 12000 O O5  . NAG J 3 .   ? -46.431 15.242  -4.765  1.00 97.85  ? 1   NAG J O5  1 
HETATM 12001 O O6  . NAG J 3 .   ? -48.462 13.205  -4.957  1.00 83.66  ? 1   NAG J O6  1 
HETATM 12002 O O7  . NAG J 3 .   ? -42.028 14.368  -5.723  1.00 92.68  ? 1   NAG J O7  1 
HETATM 12003 C C1  . NAG J 3 .   ? -48.462 13.431  -8.522  1.00 114.23 ? 2   NAG J C1  1 
HETATM 12004 C C2  . NAG J 3 .   ? -49.500 13.738  -9.611  1.00 109.25 ? 2   NAG J C2  1 
HETATM 12005 C C3  . NAG J 3 .   ? -50.150 12.443  -10.092 1.00 110.90 ? 2   NAG J C3  1 
HETATM 12006 C C4  . NAG J 3 .   ? -49.080 11.456  -10.543 1.00 117.00 ? 2   NAG J C4  1 
HETATM 12007 C C5  . NAG J 3 .   ? -48.048 11.275  -9.420  1.00 113.84 ? 2   NAG J C5  1 
HETATM 12008 C C6  . NAG J 3 .   ? -46.907 10.352  -9.787  1.00 111.22 ? 2   NAG J C6  1 
HETATM 12009 C C7  . NAG J 3 .   ? -50.588 15.964  -9.534  1.00 114.25 ? 2   NAG J C7  1 
HETATM 12010 C C8  . NAG J 3 .   ? -49.570 16.421  -10.553 1.00 96.09  ? 2   NAG J C8  1 
HETATM 12011 N N2  . NAG J 3 .   ? -50.485 14.678  -9.140  1.00 117.29 ? 2   NAG J N2  1 
HETATM 12012 O O3  . NAG J 3 .   ? -51.031 12.756  -11.137 1.00 108.42 ? 2   NAG J O3  1 
HETATM 12013 O O4  . NAG J 3 .   ? -49.743 10.255  -10.872 1.00 109.27 ? 2   NAG J O4  1 
HETATM 12014 O O5  . NAG J 3 .   ? -47.512 12.532  -9.045  1.00 115.15 ? 2   NAG J O5  1 
HETATM 12015 O O6  . NAG J 3 .   ? -47.425 9.098   -10.161 1.00 112.34 ? 2   NAG J O6  1 
HETATM 12016 O O7  . NAG J 3 .   ? -51.441 16.730  -9.109  1.00 117.94 ? 2   NAG J O7  1 
HETATM 12017 C C1  . NAG K 5 .   ? 41.266  44.073  69.478  1.00 92.34  ? 1   NAG K C1  1 
HETATM 12018 C C2  . NAG K 5 .   ? 39.750  43.910  69.595  1.00 90.10  ? 1   NAG K C2  1 
HETATM 12019 C C3  . NAG K 5 .   ? 39.079  44.547  68.379  1.00 85.43  ? 1   NAG K C3  1 
HETATM 12020 C C4  . NAG K 5 .   ? 39.546  45.988  68.169  1.00 86.50  ? 1   NAG K C4  1 
HETATM 12021 C C5  . NAG K 5 .   ? 41.078  46.047  68.213  1.00 92.97  ? 1   NAG K C5  1 
HETATM 12022 C C6  . NAG K 5 .   ? 41.611  47.459  68.133  1.00 88.87  ? 1   NAG K C6  1 
HETATM 12023 C C7  . NAG K 5 .   ? 39.225  41.897  70.907  1.00 93.33  ? 1   NAG K C7  1 
HETATM 12024 C C8  . NAG K 5 .   ? 38.843  40.438  70.827  1.00 89.81  ? 1   NAG K C8  1 
HETATM 12025 N N2  . NAG K 5 .   ? 39.387  42.523  69.726  1.00 88.89  ? 1   NAG K N2  1 
HETATM 12026 O O1  . NAG K 5 .   ? 41.862  43.557  70.605  1.00 104.81 ? 1   NAG K O1  1 
HETATM 12027 O O3  . NAG K 5 .   ? 37.698  44.462  68.598  1.00 84.90  ? 1   NAG K O3  1 
HETATM 12028 O O4  . NAG K 5 .   ? 39.101  46.430  66.904  1.00 89.83  ? 1   NAG K O4  1 
HETATM 12029 O O5  . NAG K 5 .   ? 41.562  45.443  69.396  1.00 98.70  ? 1   NAG K O5  1 
HETATM 12030 O O6  . NAG K 5 .   ? 40.746  48.322  68.834  1.00 96.46  ? 1   NAG K O6  1 
HETATM 12031 O O7  . NAG K 5 .   ? 39.379  42.457  71.983  1.00 100.70 ? 1   NAG K O7  1 
HETATM 12032 C C1  . GAL K 5 .   ? 37.847  47.131  67.001  1.00 82.98  ? 2   GAL K C1  1 
HETATM 12033 C C2  . GAL K 5 .   ? 37.760  48.168  65.887  1.00 93.24  ? 2   GAL K C2  1 
HETATM 12034 C C3  . GAL K 5 .   ? 36.376  48.820  65.910  1.00 93.56  ? 2   GAL K C3  1 
HETATM 12035 C C4  . GAL K 5 .   ? 35.242  47.798  65.845  1.00 85.27  ? 2   GAL K C4  1 
HETATM 12036 C C5  . GAL K 5 .   ? 35.489  46.781  66.957  1.00 86.53  ? 2   GAL K C5  1 
HETATM 12037 C C6  . GAL K 5 .   ? 34.543  45.607  66.906  1.00 79.79  ? 2   GAL K C6  1 
HETATM 12038 O O2  . GAL K 5 .   ? 38.775  49.118  66.098  1.00 97.52  ? 2   GAL K O2  1 
HETATM 12039 O O3  . GAL K 5 .   ? 36.327  49.730  64.842  1.00 93.02  ? 2   GAL K O3  1 
HETATM 12040 O O4  . GAL K 5 .   ? 35.234  47.210  64.566  1.00 83.57  ? 2   GAL K O4  1 
HETATM 12041 O O5  . GAL K 5 .   ? 36.782  46.230  66.845  1.00 90.11  ? 2   GAL K O5  1 
HETATM 12042 O O6  . GAL K 5 .   ? 35.206  44.578  67.605  1.00 86.78  ? 2   GAL K O6  1 
HETATM 12043 C C1  . SIA K 5 .   ? 33.038  43.360  67.171  1.00 79.37  ? 3   SIA K C1  1 
HETATM 12044 C C2  . SIA K 5 .   ? 34.586  43.277  67.496  1.00 79.79  ? 3   SIA K C2  1 
HETATM 12045 C C3  . SIA K 5 .   ? 34.926  42.890  68.938  1.00 66.45  ? 3   SIA K C3  1 
HETATM 12046 C C4  . SIA K 5 .   ? 34.788  41.401  69.235  1.00 65.18  ? 3   SIA K C4  1 
HETATM 12047 C C5  . SIA K 5 .   ? 35.657  40.600  68.269  1.00 72.12  ? 3   SIA K C5  1 
HETATM 12048 C C6  . SIA K 5 .   ? 35.293  40.966  66.808  1.00 72.45  ? 3   SIA K C6  1 
HETATM 12049 C C7  . SIA K 5 .   ? 36.367  40.467  65.816  1.00 75.91  ? 3   SIA K C7  1 
HETATM 12050 C C8  . SIA K 5 .   ? 36.081  40.996  64.391  1.00 77.53  ? 3   SIA K C8  1 
HETATM 12051 C C9  . SIA K 5 .   ? 36.459  39.967  63.332  1.00 78.31  ? 3   SIA K C9  1 
HETATM 12052 C C10 . SIA K 5 .   ? 36.474  38.246  68.352  1.00 75.83  ? 3   SIA K C10 1 
HETATM 12053 C C11 . SIA K 5 .   ? 36.042  36.802  68.600  1.00 70.36  ? 3   SIA K C11 1 
HETATM 12054 N N5  . SIA K 5 .   ? 35.481  39.164  68.466  1.00 73.74  ? 3   SIA K N5  1 
HETATM 12055 O O1A . SIA K 5 .   ? 32.749  42.873  66.042  1.00 77.66  ? 3   SIA K O1A 1 
HETATM 12056 O O1B . SIA K 5 .   ? 32.294  43.869  68.045  1.00 82.20  ? 3   SIA K O1B 1 
HETATM 12057 O O4  . SIA K 5 .   ? 35.229  41.085  70.564  1.00 79.08  ? 3   SIA K O4  1 
HETATM 12058 O O6  . SIA K 5 .   ? 35.298  42.372  66.580  1.00 68.29  ? 3   SIA K O6  1 
HETATM 12059 O O7  . SIA K 5 .   ? 37.657  40.844  66.281  1.00 81.47  ? 3   SIA K O7  1 
HETATM 12060 O O8  . SIA K 5 .   ? 34.715  41.396  64.271  1.00 71.31  ? 3   SIA K O8  1 
HETATM 12061 O O9  . SIA K 5 .   ? 36.466  40.593  62.048  1.00 73.26  ? 3   SIA K O9  1 
HETATM 12062 O O10 . SIA K 5 .   ? 37.637  38.526  68.064  1.00 76.27  ? 3   SIA K O10 1 
HETATM 12063 C C1  . NAG L 5 .   ? 48.846  1.521   48.444  1.00 136.41 ? 1   NAG L C1  1 
HETATM 12064 C C2  . NAG L 5 .   ? 47.723  1.030   47.526  1.00 138.34 ? 1   NAG L C2  1 
HETATM 12065 C C3  . NAG L 5 .   ? 46.375  1.530   48.049  1.00 136.49 ? 1   NAG L C3  1 
HETATM 12066 C C4  . NAG L 5 .   ? 46.181  1.179   49.527  1.00 136.83 ? 1   NAG L C4  1 
HETATM 12067 C C5  . NAG L 5 .   ? 47.423  1.598   50.325  1.00 135.67 ? 1   NAG L C5  1 
HETATM 12068 C C6  . NAG L 5 .   ? 47.368  1.189   51.781  1.00 136.45 ? 1   NAG L C6  1 
HETATM 12069 C C7  . NAG L 5 .   ? 48.390  0.643   45.181  1.00 140.99 ? 1   NAG L C7  1 
HETATM 12070 C C8  . NAG L 5 .   ? 48.532  1.296   43.826  1.00 115.04 ? 1   NAG L C8  1 
HETATM 12071 N N2  . NAG L 5 .   ? 47.934  1.446   46.162  1.00 143.98 ? 1   NAG L N2  1 
HETATM 12072 O O1  . NAG L 5 .   ? 50.044  0.999   48.011  1.00 133.54 ? 1   NAG L O1  1 
HETATM 12073 O O3  . NAG L 5 .   ? 45.391  0.980   47.212  1.00 124.19 ? 1   NAG L O3  1 
HETATM 12074 O O4  . NAG L 5 .   ? 45.051  1.873   50.018  1.00 136.59 ? 1   NAG L O4  1 
HETATM 12075 O O5  . NAG L 5 .   ? 48.595  1.057   49.746  1.00 144.16 ? 1   NAG L O5  1 
HETATM 12076 O O6  . NAG L 5 .   ? 47.209  -0.207  51.876  1.00 130.62 ? 1   NAG L O6  1 
HETATM 12077 O O7  . NAG L 5 .   ? 48.680  -0.532  45.354  1.00 145.02 ? 1   NAG L O7  1 
HETATM 12078 C C1  . GAL L 5 .   ? 43.866  1.054   49.940  1.00 135.93 ? 2   GAL L C1  1 
HETATM 12079 C C2  . GAL L 5 .   ? 42.931  1.410   51.093  1.00 137.02 ? 2   GAL L C2  1 
HETATM 12080 C C3  . GAL L 5 .   ? 41.651  0.584   50.963  1.00 132.54 ? 2   GAL L C3  1 
HETATM 12081 C C4  . GAL L 5 .   ? 40.978  0.761   49.603  1.00 121.04 ? 2   GAL L C4  1 
HETATM 12082 C C5  . GAL L 5 .   ? 42.031  0.504   48.521  1.00 125.38 ? 2   GAL L C5  1 
HETATM 12083 C C6  . GAL L 5 .   ? 41.523  0.833   47.136  1.00 114.03 ? 2   GAL L C6  1 
HETATM 12084 O O2  . GAL L 5 .   ? 43.595  1.125   52.297  1.00 140.83 ? 2   GAL L O2  1 
HETATM 12085 O O3  . GAL L 5 .   ? 40.809  0.944   52.027  1.00 127.76 ? 2   GAL L O3  1 
HETATM 12086 O O4  . GAL L 5 .   ? 40.425  2.055   49.530  1.00 108.97 ? 2   GAL L O4  1 
HETATM 12087 O O5  . GAL L 5 .   ? 43.186  1.289   48.731  1.00 126.29 ? 2   GAL L O5  1 
HETATM 12088 O O6  . GAL L 5 .   ? 42.622  0.712   46.261  1.00 114.37 ? 2   GAL L O6  1 
HETATM 12089 C C1  . SIA L 5 .   ? 40.868  1.071   44.489  1.00 99.52  ? 3   SIA L C1  1 
HETATM 12090 C C2  . SIA L 5 .   ? 42.374  1.271   44.950  1.00 110.28 ? 3   SIA L C2  1 
HETATM 12091 C C3  . SIA L 5 .   ? 43.420  0.385   44.259  1.00 112.39 ? 3   SIA L C3  1 
HETATM 12092 C C4  . SIA L 5 .   ? 43.756  0.807   42.827  1.00 101.09 ? 3   SIA L C4  1 
HETATM 12093 C C5  . SIA L 5 .   ? 44.231  2.258   42.805  1.00 97.69  ? 3   SIA L C5  1 
HETATM 12094 C C6  . SIA L 5 .   ? 43.242  3.192   43.556  1.00 103.11 ? 3   SIA L C6  1 
HETATM 12095 C C7  . SIA L 5 .   ? 43.938  4.513   43.964  1.00 100.95 ? 3   SIA L C7  1 
HETATM 12096 C C8  . SIA L 5 .   ? 42.990  5.417   44.793  1.00 99.12  ? 3   SIA L C8  1 
HETATM 12097 C C9  . SIA L 5 .   ? 42.531  6.638   44.003  1.00 95.71  ? 3   SIA L C9  1 
HETATM 12098 C C10 . SIA L 5 .   ? 45.487  3.327   40.928  1.00 95.47  ? 3   SIA L C10 1 
HETATM 12099 C C11 . SIA L 5 .   ? 45.387  3.730   39.457  1.00 77.52  ? 3   SIA L C11 1 
HETATM 12100 N N5  . SIA L 5 .   ? 44.378  2.726   41.429  1.00 91.40  ? 3   SIA L N5  1 
HETATM 12101 O O1A . SIA L 5 .   ? 40.266  2.165   44.297  1.00 93.95  ? 3   SIA L O1A 1 
HETATM 12102 O O1B . SIA L 5 .   ? 40.449  -0.103  44.361  1.00 97.26  ? 3   SIA L O1B 1 
HETATM 12103 O O4  . SIA L 5 .   ? 44.817  0.022   42.252  1.00 92.88  ? 3   SIA L O4  1 
HETATM 12104 O O6  . SIA L 5 .   ? 42.800  2.675   44.813  1.00 114.62 ? 3   SIA L O6  1 
HETATM 12105 O O7  . SIA L 5 .   ? 45.146  4.230   44.664  1.00 109.29 ? 3   SIA L O7  1 
HETATM 12106 O O8  . SIA L 5 .   ? 41.878  4.672   45.294  1.00 105.34 ? 3   SIA L O8  1 
HETATM 12107 O O9  . SIA L 5 .   ? 41.632  7.409   44.805  1.00 91.33  ? 3   SIA L O9  1 
HETATM 12108 O O10 . SIA L 5 .   ? 46.509  3.546   41.578  1.00 107.52 ? 3   SIA L O10 1 
HETATM 12109 C C1  . NAG M 5 .   ? 56.173  40.600  22.634  1.00 133.67 ? 1   NAG M C1  1 
HETATM 12110 C C2  . NAG M 5 .   ? 55.043  41.481  22.097  1.00 140.88 ? 1   NAG M C2  1 
HETATM 12111 C C3  . NAG M 5 .   ? 53.868  40.603  21.659  1.00 137.01 ? 1   NAG M C3  1 
HETATM 12112 C C4  . NAG M 5 .   ? 54.305  39.460  20.730  1.00 138.82 ? 1   NAG M C4  1 
HETATM 12113 C C5  . NAG M 5 .   ? 55.546  38.761  21.305  1.00 136.89 ? 1   NAG M C5  1 
HETATM 12114 C C6  . NAG M 5 .   ? 56.129  37.703  20.391  1.00 129.14 ? 1   NAG M C6  1 
HETATM 12115 C C7  . NAG M 5 .   ? 55.207  43.641  23.287  1.00 132.00 ? 1   NAG M C7  1 
HETATM 12116 C C8  . NAG M 5 .   ? 54.583  44.486  24.371  1.00 99.33  ? 1   NAG M C8  1 
HETATM 12117 N N2  . NAG M 5 .   ? 54.619  42.447  23.080  1.00 138.02 ? 1   NAG M N2  1 
HETATM 12118 O O1  . NAG M 5 .   ? 57.252  41.392  22.956  1.00 129.39 ? 1   NAG M O1  1 
HETATM 12119 O O3  . NAG M 5 .   ? 52.921  41.467  21.080  1.00 123.52 ? 1   NAG M O3  1 
HETATM 12120 O O4  . NAG M 5 .   ? 53.263  38.507  20.631  1.00 130.53 ? 1   NAG M O4  1 
HETATM 12121 O O5  . NAG M 5 .   ? 56.553  39.703  21.622  1.00 139.31 ? 1   NAG M O5  1 
HETATM 12122 O O6  . NAG M 5 .   ? 56.396  38.251  19.121  1.00 124.52 ? 1   NAG M O6  1 
HETATM 12123 O O7  . NAG M 5 .   ? 56.181  44.025  22.655  1.00 143.46 ? 1   NAG M O7  1 
HETATM 12124 C C1  . GAL M 5 .   ? 52.340  38.816  19.568  1.00 125.34 ? 2   GAL M C1  1 
HETATM 12125 C C2  . GAL M 5 .   ? 51.744  37.514  19.035  1.00 120.75 ? 2   GAL M C2  1 
HETATM 12126 C C3  . GAL M 5 .   ? 50.622  37.829  18.046  1.00 109.29 ? 2   GAL M C3  1 
HETATM 12127 C C4  . GAL M 5 .   ? 49.568  38.745  18.662  1.00 107.72 ? 2   GAL M C4  1 
HETATM 12128 C C5  . GAL M 5 .   ? 50.302  39.994  19.152  1.00 110.13 ? 2   GAL M C5  1 
HETATM 12129 C C6  . GAL M 5 .   ? 49.394  40.962  19.876  1.00 97.85  ? 2   GAL M C6  1 
HETATM 12130 O O2  . GAL M 5 .   ? 52.774  36.785  18.416  1.00 118.47 ? 2   GAL M O2  1 
HETATM 12131 O O3  . GAL M 5 .   ? 50.093  36.602  17.616  1.00 116.92 ? 2   GAL M O3  1 
HETATM 12132 O O4  . GAL M 5 .   ? 48.920  38.053  19.704  1.00 95.69  ? 2   GAL M O4  1 
HETATM 12133 O O5  . GAL M 5 .   ? 51.310  39.634  20.067  1.00 120.99 ? 2   GAL M O5  1 
HETATM 12134 O O6  . GAL M 5 .   ? 50.199  41.959  20.465  1.00 94.92  ? 2   GAL M O6  1 
HETATM 12135 C C1  . SIA M 5 .   ? 47.981  43.033  20.854  1.00 88.66  ? 3   SIA M C1  1 
HETATM 12136 C C2  . SIA M 5 .   ? 49.450  42.770  21.399  1.00 98.95  ? 3   SIA M C2  1 
HETATM 12137 C C3  . SIA M 5 .   ? 50.346  44.016  21.443  1.00 96.01  ? 3   SIA M C3  1 
HETATM 12138 C C4  . SIA M 5 .   ? 49.979  45.010  22.547  1.00 76.72  ? 3   SIA M C4  1 
HETATM 12139 C C5  . SIA M 5 .   ? 50.033  44.308  23.902  1.00 73.40  ? 3   SIA M C5  1 
HETATM 12140 C C6  . SIA M 5 .   ? 49.166  43.020  23.883  1.00 85.06  ? 3   SIA M C6  1 
HETATM 12141 C C7  . SIA M 5 .   ? 49.479  42.097  25.084  1.00 88.75  ? 3   SIA M C7  1 
HETATM 12142 C C8  . SIA M 5 .   ? 48.595  40.824  25.034  1.00 75.49  ? 3   SIA M C8  1 
HETATM 12143 C C9  . SIA M 5 .   ? 48.537  40.138  26.395  1.00 82.70  ? 3   SIA M C9  1 
HETATM 12144 C C10 . SIA M 5 .   ? 50.255  45.480  26.096  1.00 70.58  ? 3   SIA M C10 1 
HETATM 12145 C C11 . SIA M 5 .   ? 49.569  46.467  27.039  1.00 68.32  ? 3   SIA M C11 1 
HETATM 12146 N N5  . SIA M 5 .   ? 49.575  45.214  24.951  1.00 64.25  ? 3   SIA M N5  1 
HETATM 12147 O O1A . SIA M 5 .   ? 47.079  42.517  21.572  1.00 88.22  ? 3   SIA M O1A 1 
HETATM 12148 O O1B . SIA M 5 .   ? 47.874  43.707  19.803  1.00 86.83  ? 3   SIA M O1B 1 
HETATM 12149 O O4  . SIA M 5 .   ? 50.883  46.127  22.633  1.00 73.91  ? 3   SIA M O4  1 
HETATM 12150 O O6  . SIA M 5 .   ? 49.421  42.187  22.752  1.00 95.14  ? 3   SIA M O6  1 
HETATM 12151 O O7  . SIA M 5 .   ? 50.871  41.793  25.115  1.00 91.48  ? 3   SIA M O7  1 
HETATM 12152 O O8  . SIA M 5 .   ? 47.286  41.126  24.542  1.00 66.06  ? 3   SIA M O8  1 
HETATM 12153 O O9  . SIA M 5 .   ? 47.809  38.911  26.292  1.00 72.84  ? 3   SIA M O9  1 
HETATM 12154 O O10 . SIA M 5 .   ? 51.341  44.981  26.385  1.00 89.04  ? 3   SIA M O10 1 
HETATM 12155 C C1  . NAG N 6 .   ? 30.450  58.910  51.345  1.00 92.05  ? 401 NAG A C1  1 
HETATM 12156 C C2  . NAG N 6 .   ? 30.543  58.231  52.722  1.00 80.30  ? 401 NAG A C2  1 
HETATM 12157 C C3  . NAG N 6 .   ? 29.383  58.683  53.613  1.00 81.84  ? 401 NAG A C3  1 
HETATM 12158 C C4  . NAG N 6 .   ? 29.325  60.206  53.695  1.00 92.25  ? 401 NAG A C4  1 
HETATM 12159 C C5  . NAG N 6 .   ? 29.265  60.775  52.272  1.00 87.98  ? 401 NAG A C5  1 
HETATM 12160 C C6  . NAG N 6 .   ? 29.272  62.287  52.206  1.00 77.94  ? 401 NAG A C6  1 
HETATM 12161 C C7  . NAG N 6 .   ? 31.578  56.005  52.928  1.00 74.38  ? 401 NAG A C7  1 
HETATM 12162 C C8  . NAG N 6 .   ? 31.358  54.530  52.710  1.00 62.08  ? 401 NAG A C8  1 
HETATM 12163 N N2  . NAG N 6 .   ? 30.546  56.798  52.593  1.00 80.43  ? 401 NAG A N2  1 
HETATM 12164 O O3  . NAG N 6 .   ? 29.547  58.089  54.873  1.00 84.39  ? 401 NAG A O3  1 
HETATM 12165 O O4  . NAG N 6 .   ? 28.188  60.557  54.454  1.00 82.06  ? 401 NAG A O4  1 
HETATM 12166 O O5  . NAG N 6 .   ? 30.373  60.309  51.524  1.00 94.92  ? 401 NAG A O5  1 
HETATM 12167 O O6  . NAG N 6 .   ? 30.589  62.764  52.361  1.00 78.13  ? 401 NAG A O6  1 
HETATM 12168 O O7  . NAG N 6 .   ? 32.626  56.432  53.380  1.00 80.68  ? 401 NAG A O7  1 
HETATM 12169 C C1  . NAG O 6 .   ? -22.238 46.960  -4.214  1.00 85.31  ? 402 NAG A C1  1 
HETATM 12170 C C2  . NAG O 6 .   ? -21.102 47.369  -5.160  1.00 93.18  ? 402 NAG A C2  1 
HETATM 12171 C C3  . NAG O 6 .   ? -20.502 48.703  -4.713  1.00 101.79 ? 402 NAG A C3  1 
HETATM 12172 C C4  . NAG O 6 .   ? -21.594 49.761  -4.593  1.00 100.23 ? 402 NAG A C4  1 
HETATM 12173 C C5  . NAG O 6 .   ? -22.707 49.233  -3.682  1.00 99.56  ? 402 NAG A C5  1 
HETATM 12174 C C6  . NAG O 6 .   ? -23.878 50.181  -3.539  1.00 106.14 ? 402 NAG A C6  1 
HETATM 12175 C C7  . NAG O 6 .   ? -20.002 45.442  -6.225  1.00 98.40  ? 402 NAG A C7  1 
HETATM 12176 C C8  . NAG O 6 .   ? -18.883 44.438  -6.079  1.00 91.38  ? 402 NAG A C8  1 
HETATM 12177 N N2  . NAG O 6 .   ? -20.106 46.333  -5.220  1.00 98.28  ? 402 NAG A N2  1 
HETATM 12178 O O3  . NAG O 6 .   ? -19.514 49.071  -5.639  1.00 97.16  ? 402 NAG A O3  1 
HETATM 12179 O O4  . NAG O 6 .   ? -21.003 50.927  -4.066  1.00 98.69  ? 402 NAG A O4  1 
HETATM 12180 O O5  . NAG O 6 .   ? -23.188 48.001  -4.186  1.00 91.57  ? 402 NAG A O5  1 
HETATM 12181 O O6  . NAG O 6 .   ? -24.626 50.194  -4.732  1.00 109.27 ? 402 NAG A O6  1 
HETATM 12182 O O7  . NAG O 6 .   ? -20.750 45.429  -7.193  1.00 93.13  ? 402 NAG A O7  1 
HETATM 12183 C C1  . NAG P 6 .   ? -14.484 28.052  1.297   1.00 93.29  ? 403 NAG A C1  1 
HETATM 12184 C C2  . NAG P 6 .   ? -14.184 26.684  0.664   1.00 98.19  ? 403 NAG A C2  1 
HETATM 12185 C C3  . NAG P 6 .   ? -12.677 26.472  0.539   1.00 89.14  ? 403 NAG A C3  1 
HETATM 12186 C C4  . NAG P 6 .   ? -12.051 27.645  -0.209  1.00 92.83  ? 403 NAG A C4  1 
HETATM 12187 C C5  . NAG P 6 .   ? -12.431 28.953  0.497   1.00 98.34  ? 403 NAG A C5  1 
HETATM 12188 C C6  . NAG P 6 .   ? -11.883 30.200  -0.166  1.00 96.31  ? 403 NAG A C6  1 
HETATM 12189 C C7  . NAG P 6 .   ? -15.841 24.881  1.001   1.00 93.79  ? 403 NAG A C7  1 
HETATM 12190 C C8  . NAG P 6 .   ? -16.374 25.215  -0.373  1.00 90.37  ? 403 NAG A C8  1 
HETATM 12191 N N2  . NAG P 6 .   ? -14.797 25.624  1.421   1.00 94.84  ? 403 NAG A N2  1 
HETATM 12192 O O3  . NAG P 6 .   ? -12.476 25.246  -0.115  1.00 77.76  ? 403 NAG A O3  1 
HETATM 12193 O O4  . NAG P 6 .   ? -10.657 27.448  -0.220  1.00 97.84  ? 403 NAG A O4  1 
HETATM 12194 O O5  . NAG P 6 .   ? -13.841 29.065  0.555   1.00 100.39 ? 403 NAG A O5  1 
HETATM 12195 O O6  . NAG P 6 .   ? -12.850 30.751  -1.033  1.00 83.70  ? 403 NAG A O6  1 
HETATM 12196 O O7  . NAG P 6 .   ? -16.338 23.991  1.673   1.00 87.48  ? 403 NAG A O7  1 
HETATM 12197 C C1  . NAG Q 6 .   ? -25.534 49.919  35.013  1.00 94.41  ? 401 NAG C C1  1 
HETATM 12198 C C2  . NAG Q 6 .   ? -24.833 51.030  34.219  1.00 96.23  ? 401 NAG C C2  1 
HETATM 12199 C C3  . NAG Q 6 .   ? -23.654 51.579  35.022  1.00 100.00 ? 401 NAG C C3  1 
HETATM 12200 C C4  . NAG Q 6 .   ? -24.117 52.020  36.409  1.00 104.64 ? 401 NAG C C4  1 
HETATM 12201 C C5  . NAG Q 6 .   ? -24.848 50.857  37.094  1.00 99.62  ? 401 NAG C C5  1 
HETATM 12202 C C6  . NAG Q 6 .   ? -25.395 51.207  38.462  1.00 98.79  ? 401 NAG C C6  1 
HETATM 12203 C C7  . NAG Q 6 .   ? -24.898 51.002  31.751  1.00 87.69  ? 401 NAG C C7  1 
HETATM 12204 C C8  . NAG Q 6 .   ? -24.307 50.366  30.517  1.00 65.02  ? 401 NAG C C8  1 
HETATM 12205 N N2  . NAG Q 6 .   ? -24.408 50.558  32.925  1.00 99.29  ? 401 NAG C N2  1 
HETATM 12206 O O3  . NAG Q 6 .   ? -23.104 52.639  34.287  1.00 93.81  ? 401 NAG C O3  1 
HETATM 12207 O O4  . NAG Q 6 .   ? -22.983 52.443  37.137  1.00 90.82  ? 401 NAG C O4  1 
HETATM 12208 O O5  . NAG Q 6 .   ? -25.919 50.427  36.273  1.00 101.62 ? 401 NAG C O5  1 
HETATM 12209 O O6  . NAG Q 6 .   ? -26.443 50.330  38.807  1.00 90.01  ? 401 NAG C O6  1 
HETATM 12210 O O7  . NAG Q 6 .   ? -25.761 51.861  31.665  1.00 89.72  ? 401 NAG C O7  1 
HETATM 12211 C C1  . NAG R 6 .   ? -16.838 27.575  54.938  1.00 85.73  ? 402 NAG C C1  1 
HETATM 12212 C C2  . NAG R 6 .   ? -16.571 26.761  56.214  1.00 99.04  ? 402 NAG C C2  1 
HETATM 12213 C C3  . NAG R 6 .   ? -17.635 25.671  56.347  1.00 97.46  ? 402 NAG C C3  1 
HETATM 12214 C C4  . NAG R 6 .   ? -19.028 26.297  56.319  1.00 100.83 ? 402 NAG C C4  1 
HETATM 12215 C C5  . NAG R 6 .   ? -19.176 27.209  55.087  1.00 102.33 ? 402 NAG C C5  1 
HETATM 12216 C C6  . NAG R 6 .   ? -20.487 27.966  55.022  1.00 88.17  ? 402 NAG C C6  1 
HETATM 12217 C C7  . NAG R 6 .   ? -14.298 26.538  57.151  1.00 101.62 ? 402 NAG C C7  1 
HETATM 12218 C C8  . NAG R 6 .   ? -12.964 25.850  56.974  1.00 79.20  ? 402 NAG C C8  1 
HETATM 12219 N N2  . NAG R 6 .   ? -15.235 26.218  56.235  1.00 98.43  ? 402 NAG C N2  1 
HETATM 12220 O O3  . NAG R 6 .   ? -17.397 24.970  57.540  1.00 94.50  ? 402 NAG C O3  1 
HETATM 12221 O O4  . NAG R 6 .   ? -19.957 25.234  56.324  1.00 91.08  ? 402 NAG C O4  1 
HETATM 12222 O O5  . NAG R 6 .   ? -18.120 28.153  55.042  1.00 95.14  ? 402 NAG C O5  1 
HETATM 12223 O O6  . NAG R 6 .   ? -21.424 27.233  54.270  1.00 88.21  ? 402 NAG C O6  1 
HETATM 12224 O O7  . NAG R 6 .   ? -14.494 27.327  58.067  1.00 92.76  ? 402 NAG C O7  1 
HETATM 12225 C C1  . NAG S 6 .   ? -25.906 9.891   36.072  1.00 89.46  ? 401 NAG E C1  1 
HETATM 12226 C C2  . NAG S 6 .   ? -26.322 9.984   37.548  1.00 85.11  ? 401 NAG E C2  1 
HETATM 12227 C C3  . NAG S 6 .   ? -25.119 9.707   38.449  1.00 86.35  ? 401 NAG E C3  1 
HETATM 12228 C C4  . NAG S 6 .   ? -24.476 8.375   38.076  1.00 90.60  ? 401 NAG E C4  1 
HETATM 12229 C C5  . NAG S 6 .   ? -24.139 8.375   36.579  1.00 88.39  ? 401 NAG E C5  1 
HETATM 12230 C C6  . NAG S 6 .   ? -23.528 7.081   36.080  1.00 91.33  ? 401 NAG E C6  1 
HETATM 12231 C C7  . NAG S 6 .   ? -28.219 11.539  37.753  1.00 77.05  ? 401 NAG E C7  1 
HETATM 12232 C C8  . NAG S 6 .   ? -28.609 12.955  38.102  1.00 66.91  ? 401 NAG E C8  1 
HETATM 12233 N N2  . NAG S 6 .   ? -26.902 11.270  37.837  1.00 70.43  ? 401 NAG E N2  1 
HETATM 12234 O O3  . NAG S 6 .   ? -25.548 9.732   39.785  1.00 82.86  ? 401 NAG E O3  1 
HETATM 12235 O O4  . NAG S 6 .   ? -23.321 8.233   38.872  1.00 97.68  ? 401 NAG E O4  1 
HETATM 12236 O O5  . NAG S 6 .   ? -25.314 8.632   35.830  1.00 89.11  ? 401 NAG E O5  1 
HETATM 12237 O O6  . NAG S 6 .   ? -24.526 6.094   35.953  1.00 92.97  ? 401 NAG E O6  1 
HETATM 12238 O O7  . NAG S 6 .   ? -29.053 10.710  37.416  1.00 79.28  ? 401 NAG E O7  1 
HETATM 12239 O O   . HOH T 7 .   ? 40.855  54.956  35.740  1.00 42.20  ? 501 HOH A O   1 
HETATM 12240 O O   . HOH T 7 .   ? 7.699   53.662  28.000  1.00 58.58  ? 502 HOH A O   1 
HETATM 12241 O O   . HOH T 7 .   ? 18.507  54.522  14.770  1.00 55.22  ? 503 HOH A O   1 
HETATM 12242 O O   . HOH T 7 .   ? -7.387  31.091  9.937   1.00 53.69  ? 504 HOH A O   1 
HETATM 12243 O O   . HOH T 7 .   ? -1.942  41.196  26.669  1.00 56.09  ? 505 HOH A O   1 
HETATM 12244 O O   . HOH T 7 .   ? 13.265  40.134  19.901  1.00 45.83  ? 506 HOH A O   1 
HETATM 12245 O O   . HOH T 7 .   ? 12.278  54.441  30.718  1.00 54.13  ? 507 HOH A O   1 
HETATM 12246 O O   . HOH T 7 .   ? 27.837  46.866  45.395  1.00 55.18  ? 508 HOH A O   1 
HETATM 12247 O O   . HOH T 7 .   ? 35.837  58.648  46.776  1.00 50.44  ? 509 HOH A O   1 
HETATM 12248 O O   . HOH T 7 .   ? 23.671  36.468  25.821  1.00 46.64  ? 510 HOH A O   1 
HETATM 12249 O O   . HOH T 7 .   ? -12.538 33.101  10.442  1.00 46.41  ? 511 HOH A O   1 
HETATM 12250 O O   . HOH T 7 .   ? -13.433 43.652  8.898   1.00 53.35  ? 512 HOH A O   1 
HETATM 12251 O O   . HOH T 7 .   ? -14.921 36.205  2.488   1.00 50.68  ? 513 HOH A O   1 
HETATM 12252 O O   . HOH T 7 .   ? 23.081  36.302  33.477  1.00 42.56  ? 514 HOH A O   1 
HETATM 12253 O O   . HOH T 7 .   ? -15.790 33.161  10.029  1.00 45.91  ? 515 HOH A O   1 
HETATM 12254 O O   . HOH T 7 .   ? -8.404  48.547  15.970  1.00 62.90  ? 516 HOH A O   1 
HETATM 12255 O O   . HOH T 7 .   ? 4.914   49.021  32.430  1.00 48.21  ? 517 HOH A O   1 
HETATM 12256 O O   . HOH T 7 .   ? -14.545 31.392  11.070  1.00 44.85  ? 518 HOH A O   1 
HETATM 12257 O O   . HOH U 7 .   ? -13.343 30.610  13.290  1.00 40.62  ? 201 HOH B O   1 
HETATM 12258 O O   . HOH U 7 .   ? -33.887 26.499  7.544   1.00 57.12  ? 202 HOH B O   1 
HETATM 12259 O O   . HOH U 7 .   ? -6.408  28.545  13.132  1.00 44.51  ? 203 HOH B O   1 
HETATM 12260 O O   . HOH U 7 .   ? 29.767  27.882  24.682  1.00 54.56  ? 204 HOH B O   1 
HETATM 12261 O O   . HOH U 7 .   ? -64.025 47.903  5.029   1.00 56.78  ? 205 HOH B O   1 
HETATM 12262 O O   . HOH U 7 .   ? 14.327  38.105  21.143  1.00 49.56  ? 206 HOH B O   1 
HETATM 12263 O O   . HOH U 7 .   ? 15.134  36.530  19.024  1.00 48.44  ? 207 HOH B O   1 
HETATM 12264 O O   . HOH V 7 .   ? 10.066  19.112  45.338  1.00 57.31  ? 501 HOH C O   1 
HETATM 12265 O O   . HOH V 7 .   ? 8.802   22.391  44.799  1.00 49.96  ? 502 HOH C O   1 
HETATM 12266 O O   . HOH V 7 .   ? 7.826   34.710  48.700  1.00 54.32  ? 503 HOH C O   1 
HETATM 12267 O O   . HOH V 7 .   ? 23.971  27.880  72.124  1.00 57.36  ? 504 HOH C O   1 
HETATM 12268 O O   . HOH V 7 .   ? -19.685 33.822  48.461  1.00 64.42  ? 505 HOH C O   1 
HETATM 12269 O O   . HOH V 7 .   ? -15.674 43.520  36.289  1.00 46.29  ? 506 HOH C O   1 
HETATM 12270 O O   . HOH W 7 .   ? 5.649   29.937  43.730  1.00 49.94  ? 201 HOH D O   1 
HETATM 12271 O O   . HOH W 7 .   ? -54.966 34.893  42.828  1.00 54.70  ? 202 HOH D O   1 
HETATM 12272 O O   . HOH W 7 .   ? -25.285 20.138  37.590  1.00 54.62  ? 203 HOH D O   1 
HETATM 12273 O O   . HOH W 7 .   ? -34.661 20.615  33.383  1.00 44.89  ? 204 HOH D O   1 
HETATM 12274 O O   . HOH W 7 .   ? -36.680 36.161  30.283  1.00 44.69  ? 205 HOH D O   1 
HETATM 12275 O O   . HOH X 7 .   ? 35.447  -4.681  42.308  1.00 52.60  ? 501 HOH E O   1 
HETATM 12276 O O   . HOH X 7 .   ? 43.282  27.911  32.389  1.00 51.58  ? 502 HOH E O   1 
HETATM 12277 O O   . HOH X 7 .   ? -14.675 12.248  13.865  1.00 61.13  ? 503 HOH E O   1 
HETATM 12278 O O   . HOH X 7 .   ? 35.154  24.923  23.290  1.00 54.67  ? 504 HOH E O   1 
HETATM 12279 O O   . HOH X 7 .   ? -36.147 9.178   20.083  1.00 42.38  ? 505 HOH E O   1 
HETATM 12280 O O   . HOH X 7 .   ? 30.614  24.083  24.778  1.00 54.42  ? 506 HOH E O   1 
HETATM 12281 O O   . HOH X 7 .   ? 17.202  13.348  15.522  1.00 54.66  ? 507 HOH E O   1 
HETATM 12282 O O   . HOH X 7 .   ? 1.327   5.388   17.458  1.00 51.96  ? 508 HOH E O   1 
HETATM 12283 O O   . HOH X 7 .   ? -3.499  6.558   32.170  1.00 45.84  ? 509 HOH E O   1 
HETATM 12284 O O   . HOH X 7 .   ? -37.221 11.866  22.752  1.00 46.09  ? 510 HOH E O   1 
HETATM 12285 O O   . HOH X 7 .   ? 25.556  18.678  37.258  1.00 54.66  ? 511 HOH E O   1 
HETATM 12286 O O   . HOH X 7 .   ? -32.879 19.077  34.670  1.00 53.18  ? 512 HOH E O   1 
HETATM 12287 O O   . HOH X 7 .   ? -31.536 16.362  34.677  1.00 58.85  ? 513 HOH E O   1 
HETATM 12288 O O   . HOH X 7 .   ? 2.551   19.319  25.955  1.00 37.33  ? 514 HOH E O   1 
HETATM 12289 O O   . HOH Y 7 .   ? -18.721 17.702  29.955  1.00 47.69  ? 201 HOH F O   1 
HETATM 12290 O O   . HOH Y 7 .   ? -41.528 11.538  -0.812  1.00 67.87  ? 202 HOH F O   1 
HETATM 12291 O O   . HOH Y 7 .   ? -16.979 25.097  10.556  1.00 48.44  ? 203 HOH F O   1 
HETATM 12292 O O   . HOH Y 7 .   ? -45.639 8.913   5.397   1.00 50.98  ? 204 HOH F O   1 
HETATM 12293 O O   . HOH Y 7 .   ? -21.657 20.558  4.879   1.00 57.83  ? 205 HOH F O   1 
HETATM 12294 O O   . HOH Y 7 .   ? 3.914   21.255  27.131  1.00 38.32  ? 206 HOH F O   1 
# 
