data_8SCV
# 
_entry.id   8SCV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8SCV         pdb_00008scv 10.2210/pdb8scv/pdb 
WWPDB D_1000273557 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8SCV 
_pdbx_database_status.recvd_initial_deposition_date   2023-04-05 
_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                 2 
_pdbx_contact_author.email              jodi.muckelbauer@bms.com 
_pdbx_contact_author.name_first         Jodi 
_pdbx_contact_author.name_last          Muckelbauer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7848-3178 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Muckelbauer, J.K.' 1 0000-0001-7848-3178 
'Ghosh, K.'         2 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'The Discovery of IRAK4 Inhibitor Clinical Candidates BMS-986126 and BMS-986147 for the Treatment of Autoimmune Diseases' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kumar, S.R.'        1  ? 
primary 'Dudhgoankar, S.'    2  ? 
primary 'Santella, J.B.'     3  ? 
primary 'Paidi, V.R.R.'      4  ? 
primary 'Nair, S.'           5  ? 
primary 'Sistla, R.'         6  ? 
primary 'Wu, H.'             7  ? 
primary 'Gardner, D.S.'      8  ? 
primary 'Stachura, S.'       9  ? 
primary 'Cavallaro, C.L.'    10 ? 
primary 'Brown, G.D.'        11 ? 
primary 'Pitts, W.J.'        12 ? 
primary 'Kempson, J.'        13 ? 
primary 'Tebben, A.J.'       14 ? 
primary 'Tokarski, J.S.'     15 ? 
primary 'Zhu, X.'            16 ? 
primary 'Carman, J.A.'       17 ? 
primary 'Foster, K.'         18 ? 
primary 'Caceres Cortes, J.' 19 ? 
primary 'Everlof, G.'        20 ? 
primary 'Galella, M.A.'      21 ? 
primary 'Sarjeant, A.'       22 ? 
primary 'Holloway, D.A.'     23 ? 
primary 'Fan, L.'            24 ? 
primary 'Li, X.'             25 ? 
primary 'Chaudhry, C.'       26 ? 
primary 'Locke, G.'          27 ? 
primary 'Chimalakondra, A.'  28 ? 
primary 'Mariappan, T.T.'    29 ? 
primary 'Ruepp, S.'          30 ? 
primary 'Elzinga, P.A.'      31 ? 
primary 'Saxena, A.'         32 ? 
primary 'Xie, D.'            33 ? 
primary 'Kiefer, S.E.'       34 ? 
primary 'Yan, C.'            35 ? 
primary 'Newitt, J.A.'       36 ? 
primary 'Ghosh, K.'          37 ? 
primary 'Anumula, R.K.'      38 ? 
primary 'Sack, J.S.'         39 ? 
primary 'Tino, J.A.'         40 ? 
primary 'Carter, P.H.'       41 ? 
primary 'Hynes, J.'          42 ? 
primary 'Duncia, J.V.'       43 ? 
# 
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 'Interleukin-1 receptor-associated kinase 4' 34272.566 1  2.7.11.1 ? ? ? 
2 polymer     man 'Interleukin-1 receptor-associated kinase 4' 34192.586 1  2.7.11.1 ? ? ? 
3 non-polymer syn 
'6-[(5-cyanopyrimidin-2-yl)amino]-N-[(2R)-2-fluoro-3-hydroxy-3-methylbutyl]-4-[(propan-2-yl)amino]pyridine-3-carboxamide' 401.438 
2  ?        ? ? ? 
4 non-polymer syn 'SULFATE ION' 96.063    2  ?        ? ? ? 
5 water       nat water 18.015    64 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'IRAK-4,Renal carcinoma antigen NY-REN-64' 
2 'IRAK-4,Renal carcinoma antigen NY-REN-64' 
# 
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 yes 
;GAMGVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIK
VMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPL(SEP)WHMRCKIAQGAANGINFLHENHHIHRD
IKSANILLDEAFTAKISDFGLARASEKFAQTVM(TPO)(SEP)RIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITG
LPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
;GAMGVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIK
VMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSA
NILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQL
LLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
A ? 
2 'polypeptide(L)' no yes 
;GAMGVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIK
VMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSA
NILLDEAFTAKISDFGLARASEKFAQTVM(TPO)(SEP)RIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAV
DEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
;GAMGVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIK
VMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSA
NILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQL
LLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '6-[(5-cyanopyrimidin-2-yl)amino]-N-[(2R)-2-fluoro-3-hydroxy-3-methylbutyl]-4-[(propan-2-yl)amino]pyridine-3-carboxamide' ZVG 
4 'SULFATE ION'                                                                                                             SO4 
5 water                                                                                                                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   VAL n 
1 6   SER n 
1 7   ASP n 
1 8   THR n 
1 9   ARG n 
1 10  PHE n 
1 11  HIS n 
1 12  SER n 
1 13  PHE n 
1 14  SER n 
1 15  PHE n 
1 16  TYR n 
1 17  GLU n 
1 18  LEU n 
1 19  LYS n 
1 20  ASN n 
1 21  VAL n 
1 22  THR n 
1 23  ASN n 
1 24  ASN n 
1 25  PHE n 
1 26  ASP n 
1 27  GLU n 
1 28  ARG n 
1 29  PRO n 
1 30  ILE n 
1 31  SER n 
1 32  VAL n 
1 33  GLY n 
1 34  GLY n 
1 35  ASN n 
1 36  LYS n 
1 37  MET n 
1 38  GLY n 
1 39  GLU n 
1 40  GLY n 
1 41  GLY n 
1 42  PHE n 
1 43  GLY n 
1 44  VAL n 
1 45  VAL n 
1 46  TYR n 
1 47  LYS n 
1 48  GLY n 
1 49  TYR n 
1 50  VAL n 
1 51  ASN n 
1 52  ASN n 
1 53  THR n 
1 54  THR n 
1 55  VAL n 
1 56  ALA n 
1 57  VAL n 
1 58  LYS n 
1 59  LYS n 
1 60  LEU n 
1 61  ALA n 
1 62  ALA n 
1 63  MET n 
1 64  VAL n 
1 65  ASP n 
1 66  ILE n 
1 67  THR n 
1 68  THR n 
1 69  GLU n 
1 70  GLU n 
1 71  LEU n 
1 72  LYS n 
1 73  GLN n 
1 74  GLN n 
1 75  PHE n 
1 76  ASP n 
1 77  GLN n 
1 78  GLU n 
1 79  ILE n 
1 80  LYS n 
1 81  VAL n 
1 82  MET n 
1 83  ALA n 
1 84  LYS n 
1 85  CYS n 
1 86  GLN n 
1 87  HIS n 
1 88  GLU n 
1 89  ASN n 
1 90  LEU n 
1 91  VAL n 
1 92  GLU n 
1 93  LEU n 
1 94  LEU n 
1 95  GLY n 
1 96  PHE n 
1 97  SER n 
1 98  SER n 
1 99  ASP n 
1 100 GLY n 
1 101 ASP n 
1 102 ASP n 
1 103 LEU n 
1 104 CYS n 
1 105 LEU n 
1 106 VAL n 
1 107 TYR n 
1 108 VAL n 
1 109 TYR n 
1 110 MET n 
1 111 PRO n 
1 112 ASN n 
1 113 GLY n 
1 114 SER n 
1 115 LEU n 
1 116 LEU n 
1 117 ASP n 
1 118 ARG n 
1 119 LEU n 
1 120 SER n 
1 121 CYS n 
1 122 LEU n 
1 123 ASP n 
1 124 GLY n 
1 125 THR n 
1 126 PRO n 
1 127 PRO n 
1 128 LEU n 
1 129 SEP n 
1 130 TRP n 
1 131 HIS n 
1 132 MET n 
1 133 ARG n 
1 134 CYS n 
1 135 LYS n 
1 136 ILE n 
1 137 ALA n 
1 138 GLN n 
1 139 GLY n 
1 140 ALA n 
1 141 ALA n 
1 142 ASN n 
1 143 GLY n 
1 144 ILE n 
1 145 ASN n 
1 146 PHE n 
1 147 LEU n 
1 148 HIS n 
1 149 GLU n 
1 150 ASN n 
1 151 HIS n 
1 152 HIS n 
1 153 ILE n 
1 154 HIS n 
1 155 ARG n 
1 156 ASP n 
1 157 ILE n 
1 158 LYS n 
1 159 SER n 
1 160 ALA n 
1 161 ASN n 
1 162 ILE n 
1 163 LEU n 
1 164 LEU n 
1 165 ASP n 
1 166 GLU n 
1 167 ALA n 
1 168 PHE n 
1 169 THR n 
1 170 ALA n 
1 171 LYS n 
1 172 ILE n 
1 173 SER n 
1 174 ASP n 
1 175 PHE n 
1 176 GLY n 
1 177 LEU n 
1 178 ALA n 
1 179 ARG n 
1 180 ALA n 
1 181 SER n 
1 182 GLU n 
1 183 LYS n 
1 184 PHE n 
1 185 ALA n 
1 186 GLN n 
1 187 THR n 
1 188 VAL n 
1 189 MET n 
1 190 TPO n 
1 191 SEP n 
1 192 ARG n 
1 193 ILE n 
1 194 VAL n 
1 195 GLY n 
1 196 THR n 
1 197 THR n 
1 198 ALA n 
1 199 TYR n 
1 200 MET n 
1 201 ALA n 
1 202 PRO n 
1 203 GLU n 
1 204 ALA n 
1 205 LEU n 
1 206 ARG n 
1 207 GLY n 
1 208 GLU n 
1 209 ILE n 
1 210 THR n 
1 211 PRO n 
1 212 LYS n 
1 213 SER n 
1 214 ASP n 
1 215 ILE n 
1 216 TYR n 
1 217 SER n 
1 218 PHE n 
1 219 GLY n 
1 220 VAL n 
1 221 VAL n 
1 222 LEU n 
1 223 LEU n 
1 224 GLU n 
1 225 ILE n 
1 226 ILE n 
1 227 THR n 
1 228 GLY n 
1 229 LEU n 
1 230 PRO n 
1 231 ALA n 
1 232 VAL n 
1 233 ASP n 
1 234 GLU n 
1 235 HIS n 
1 236 ARG n 
1 237 GLU n 
1 238 PRO n 
1 239 GLN n 
1 240 LEU n 
1 241 LEU n 
1 242 LEU n 
1 243 ASP n 
1 244 ILE n 
1 245 LYS n 
1 246 GLU n 
1 247 GLU n 
1 248 ILE n 
1 249 GLU n 
1 250 ASP n 
1 251 GLU n 
1 252 GLU n 
1 253 LYS n 
1 254 THR n 
1 255 ILE n 
1 256 GLU n 
1 257 ASP n 
1 258 TYR n 
1 259 ILE n 
1 260 ASP n 
1 261 LYS n 
1 262 LYS n 
1 263 MET n 
1 264 ASN n 
1 265 ASP n 
1 266 ALA n 
1 267 ASP n 
1 268 SER n 
1 269 THR n 
1 270 SER n 
1 271 VAL n 
1 272 GLU n 
1 273 ALA n 
1 274 MET n 
1 275 TYR n 
1 276 SER n 
1 277 VAL n 
1 278 ALA n 
1 279 SER n 
1 280 GLN n 
1 281 CYS n 
1 282 LEU n 
1 283 HIS n 
1 284 GLU n 
1 285 LYS n 
1 286 LYS n 
1 287 ASN n 
1 288 LYS n 
1 289 ARG n 
1 290 PRO n 
1 291 ASP n 
1 292 ILE n 
1 293 LYS n 
1 294 LYS n 
1 295 VAL n 
1 296 GLN n 
1 297 GLN n 
1 298 LEU n 
1 299 LEU n 
1 300 GLN n 
1 301 GLU n 
1 302 MET n 
1 303 THR n 
1 304 ALA n 
1 305 SER n 
2 1   GLY n 
2 2   ALA n 
2 3   MET n 
2 4   GLY n 
2 5   VAL n 
2 6   SER n 
2 7   ASP n 
2 8   THR n 
2 9   ARG n 
2 10  PHE n 
2 11  HIS n 
2 12  SER n 
2 13  PHE n 
2 14  SER n 
2 15  PHE n 
2 16  TYR n 
2 17  GLU n 
2 18  LEU n 
2 19  LYS n 
2 20  ASN n 
2 21  VAL n 
2 22  THR n 
2 23  ASN n 
2 24  ASN n 
2 25  PHE n 
2 26  ASP n 
2 27  GLU n 
2 28  ARG n 
2 29  PRO n 
2 30  ILE n 
2 31  SER n 
2 32  VAL n 
2 33  GLY n 
2 34  GLY n 
2 35  ASN n 
2 36  LYS n 
2 37  MET n 
2 38  GLY n 
2 39  GLU n 
2 40  GLY n 
2 41  GLY n 
2 42  PHE n 
2 43  GLY n 
2 44  VAL n 
2 45  VAL n 
2 46  TYR n 
2 47  LYS n 
2 48  GLY n 
2 49  TYR n 
2 50  VAL n 
2 51  ASN n 
2 52  ASN n 
2 53  THR n 
2 54  THR n 
2 55  VAL n 
2 56  ALA n 
2 57  VAL n 
2 58  LYS n 
2 59  LYS n 
2 60  LEU n 
2 61  ALA n 
2 62  ALA n 
2 63  MET n 
2 64  VAL n 
2 65  ASP n 
2 66  ILE n 
2 67  THR n 
2 68  THR n 
2 69  GLU n 
2 70  GLU n 
2 71  LEU n 
2 72  LYS n 
2 73  GLN n 
2 74  GLN n 
2 75  PHE n 
2 76  ASP n 
2 77  GLN n 
2 78  GLU n 
2 79  ILE n 
2 80  LYS n 
2 81  VAL n 
2 82  MET n 
2 83  ALA n 
2 84  LYS n 
2 85  CYS n 
2 86  GLN n 
2 87  HIS n 
2 88  GLU n 
2 89  ASN n 
2 90  LEU n 
2 91  VAL n 
2 92  GLU n 
2 93  LEU n 
2 94  LEU n 
2 95  GLY n 
2 96  PHE n 
2 97  SER n 
2 98  SER n 
2 99  ASP n 
2 100 GLY n 
2 101 ASP n 
2 102 ASP n 
2 103 LEU n 
2 104 CYS n 
2 105 LEU n 
2 106 VAL n 
2 107 TYR n 
2 108 VAL n 
2 109 TYR n 
2 110 MET n 
2 111 PRO n 
2 112 ASN n 
2 113 GLY n 
2 114 SER n 
2 115 LEU n 
2 116 LEU n 
2 117 ASP n 
2 118 ARG n 
2 119 LEU n 
2 120 SER n 
2 121 CYS n 
2 122 LEU n 
2 123 ASP n 
2 124 GLY n 
2 125 THR n 
2 126 PRO n 
2 127 PRO n 
2 128 LEU n 
2 129 SER n 
2 130 TRP n 
2 131 HIS n 
2 132 MET n 
2 133 ARG n 
2 134 CYS n 
2 135 LYS n 
2 136 ILE n 
2 137 ALA n 
2 138 GLN n 
2 139 GLY n 
2 140 ALA n 
2 141 ALA n 
2 142 ASN n 
2 143 GLY n 
2 144 ILE n 
2 145 ASN n 
2 146 PHE n 
2 147 LEU n 
2 148 HIS n 
2 149 GLU n 
2 150 ASN n 
2 151 HIS n 
2 152 HIS n 
2 153 ILE n 
2 154 HIS n 
2 155 ARG n 
2 156 ASP n 
2 157 ILE n 
2 158 LYS n 
2 159 SER n 
2 160 ALA n 
2 161 ASN n 
2 162 ILE n 
2 163 LEU n 
2 164 LEU n 
2 165 ASP n 
2 166 GLU n 
2 167 ALA n 
2 168 PHE n 
2 169 THR n 
2 170 ALA n 
2 171 LYS n 
2 172 ILE n 
2 173 SER n 
2 174 ASP n 
2 175 PHE n 
2 176 GLY n 
2 177 LEU n 
2 178 ALA n 
2 179 ARG n 
2 180 ALA n 
2 181 SER n 
2 182 GLU n 
2 183 LYS n 
2 184 PHE n 
2 185 ALA n 
2 186 GLN n 
2 187 THR n 
2 188 VAL n 
2 189 MET n 
2 190 TPO n 
2 191 SEP n 
2 192 ARG n 
2 193 ILE n 
2 194 VAL n 
2 195 GLY n 
2 196 THR n 
2 197 THR n 
2 198 ALA n 
2 199 TYR n 
2 200 MET n 
2 201 ALA n 
2 202 PRO n 
2 203 GLU n 
2 204 ALA n 
2 205 LEU n 
2 206 ARG n 
2 207 GLY n 
2 208 GLU n 
2 209 ILE n 
2 210 THR n 
2 211 PRO n 
2 212 LYS n 
2 213 SER n 
2 214 ASP n 
2 215 ILE n 
2 216 TYR n 
2 217 SER n 
2 218 PHE n 
2 219 GLY n 
2 220 VAL n 
2 221 VAL n 
2 222 LEU n 
2 223 LEU n 
2 224 GLU n 
2 225 ILE n 
2 226 ILE n 
2 227 THR n 
2 228 GLY n 
2 229 LEU n 
2 230 PRO n 
2 231 ALA n 
2 232 VAL n 
2 233 ASP n 
2 234 GLU n 
2 235 HIS n 
2 236 ARG n 
2 237 GLU n 
2 238 PRO n 
2 239 GLN n 
2 240 LEU n 
2 241 LEU n 
2 242 LEU n 
2 243 ASP n 
2 244 ILE n 
2 245 LYS n 
2 246 GLU n 
2 247 GLU n 
2 248 ILE n 
2 249 GLU n 
2 250 ASP n 
2 251 GLU n 
2 252 GLU n 
2 253 LYS n 
2 254 THR n 
2 255 ILE n 
2 256 GLU n 
2 257 ASP n 
2 258 TYR n 
2 259 ILE n 
2 260 ASP n 
2 261 LYS n 
2 262 LYS n 
2 263 MET n 
2 264 ASN n 
2 265 ASP n 
2 266 ALA n 
2 267 ASP n 
2 268 SER n 
2 269 THR n 
2 270 SER n 
2 271 VAL n 
2 272 GLU n 
2 273 ALA n 
2 274 MET n 
2 275 TYR n 
2 276 SER n 
2 277 VAL n 
2 278 ALA n 
2 279 SER n 
2 280 GLN n 
2 281 CYS n 
2 282 LEU n 
2 283 HIS n 
2 284 GLU n 
2 285 LYS n 
2 286 LYS n 
2 287 ASN n 
2 288 LYS n 
2 289 ARG n 
2 290 PRO n 
2 291 ASP n 
2 292 ILE n 
2 293 LYS n 
2 294 LYS n 
2 295 VAL n 
2 296 GLN n 
2 297 GLN n 
2 298 LEU n 
2 299 LEU n 
2 300 GLN n 
2 301 GLU n 
2 302 MET n 
2 303 THR n 
2 304 ALA n 
2 305 SER 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' 1 305 human ? IRAK4 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 305 human ? IRAK4 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                  'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE ?                  'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                  'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                  'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE ?                  'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                  'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                  'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE ?                  'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE ?                  'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER ?                  'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                  'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE ?                  'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE ?                  'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE ?                  'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                  'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE ?                  'C5 H9 N O2'      115.130 
SEP 'L-peptide linking' n PHOSPHOSERINE PHOSPHONOSERINE    'C3 H8 N O6 P'    185.072 
SER 'L-peptide linking' y SERINE ?                  'C3 H7 N O3'      105.093 
SO4 non-polymer         . 'SULFATE ION' ?                  'O4 S -2'         96.063  
THR 'L-peptide linking' y THREONINE ?                  'C4 H9 N O3'      119.119 
TPO 'L-peptide linking' n PHOSPHOTHREONINE PHOSPHONOTHREONINE 'C4 H10 N O6 P'   199.099 
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 
ZVG non-polymer         . 
'6-[(5-cyanopyrimidin-2-yl)amino]-N-[(2R)-2-fluoro-3-hydroxy-3-methylbutyl]-4-[(propan-2-yl)amino]pyridine-3-carboxamide' ? 
'C19 H24 F N7 O2' 401.438 
# 
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   GLY 1   156 ?   ?   ?   A . n 
A 1 2   ALA 2   157 ?   ?   ?   A . n 
A 1 3   MET 3   158 ?   ?   ?   A . n 
A 1 4   GLY 4   159 ?   ?   ?   A . n 
A 1 5   VAL 5   160 ?   ?   ?   A . n 
A 1 6   SER 6   161 ?   ?   ?   A . n 
A 1 7   ASP 7   162 ?   ?   ?   A . n 
A 1 8   THR 8   163 163 THR THR A . n 
A 1 9   ARG 9   164 164 ARG ARG A . n 
A 1 10  PHE 10  165 165 PHE PHE A . n 
A 1 11  HIS 11  166 166 HIS HIS A . n 
A 1 12  SER 12  167 167 SER SER A . n 
A 1 13  PHE 13  168 168 PHE PHE A . n 
A 1 14  SER 14  169 169 SER SER A . n 
A 1 15  PHE 15  170 170 PHE PHE A . n 
A 1 16  TYR 16  171 171 TYR TYR A . n 
A 1 17  GLU 17  172 172 GLU GLU A . n 
A 1 18  LEU 18  173 173 LEU LEU A . n 
A 1 19  LYS 19  174 174 LYS LYS A . n 
A 1 20  ASN 20  175 175 ASN ASN A . n 
A 1 21  VAL 21  176 176 VAL VAL A . n 
A 1 22  THR 22  177 177 THR THR A . n 
A 1 23  ASN 23  178 178 ASN ASN A . n 
A 1 24  ASN 24  179 179 ASN ASN A . n 
A 1 25  PHE 25  180 180 PHE PHE A . n 
A 1 26  ASP 26  181 181 ASP ASP A . n 
A 1 27  GLU 27  182 182 GLU GLU A . n 
A 1 28  ARG 28  183 183 ARG ARG A . n 
A 1 29  PRO 29  184 184 PRO PRO A . n 
A 1 30  ILE 30  185 185 ILE ILE A . n 
A 1 31  SER 31  186 186 SER SER A . n 
A 1 32  VAL 32  187 187 VAL VAL A . n 
A 1 33  GLY 33  188 188 GLY GLY A . n 
A 1 34  GLY 34  189 189 GLY GLY A . n 
A 1 35  ASN 35  190 190 ASN ASN A . n 
A 1 36  LYS 36  191 191 LYS LYS A . n 
A 1 37  MET 37  192 192 MET MET A . n 
A 1 38  GLY 38  193 193 GLY GLY A . n 
A 1 39  GLU 39  194 194 GLU GLU A . n 
A 1 40  GLY 40  195 195 GLY GLY A . n 
A 1 41  GLY 41  196 196 GLY GLY A . n 
A 1 42  PHE 42  197 197 PHE PHE A . n 
A 1 43  GLY 43  198 198 GLY GLY A . n 
A 1 44  VAL 44  199 199 VAL VAL A . n 
A 1 45  VAL 45  200 200 VAL VAL A . n 
A 1 46  TYR 46  201 201 TYR TYR A . n 
A 1 47  LYS 47  202 202 LYS LYS A . n 
A 1 48  GLY 48  203 203 GLY GLY A . n 
A 1 49  TYR 49  204 204 TYR TYR A . n 
A 1 50  VAL 50  205 205 VAL VAL A . n 
A 1 51  ASN 51  206 206 ASN ASN A . n 
A 1 52  ASN 52  207 207 ASN ASN A . n 
A 1 53  THR 53  208 208 THR THR A . n 
A 1 54  THR 54  209 209 THR THR A . n 
A 1 55  VAL 55  210 210 VAL VAL A . n 
A 1 56  ALA 56  211 211 ALA ALA A . n 
A 1 57  VAL 57  212 212 VAL VAL A . n 
A 1 58  LYS 58  213 213 LYS LYS A . n 
A 1 59  LYS 59  214 214 LYS LYS A . n 
A 1 60  LEU 60  215 215 LEU LEU A . n 
A 1 61  ALA 61  216 216 ALA ALA A . n 
A 1 62  ALA 62  217 217 ALA ALA A . n 
A 1 63  MET 63  218 218 MET MET A . n 
A 1 64  VAL 64  219 ?   ?   ?   A . n 
A 1 65  ASP 65  220 ?   ?   ?   A . n 
A 1 66  ILE 66  221 221 ILE ILE A . n 
A 1 67  THR 67  222 222 THR THR A . n 
A 1 68  THR 68  223 223 THR THR A . n 
A 1 69  GLU 69  224 224 GLU GLU A . n 
A 1 70  GLU 70  225 225 GLU GLU A . n 
A 1 71  LEU 71  226 226 LEU LEU A . n 
A 1 72  LYS 72  227 227 LYS LYS A . n 
A 1 73  GLN 73  228 228 GLN GLN A . n 
A 1 74  GLN 74  229 229 GLN GLN A . n 
A 1 75  PHE 75  230 230 PHE PHE A . n 
A 1 76  ASP 76  231 231 ASP ASP A . n 
A 1 77  GLN 77  232 232 GLN GLN A . n 
A 1 78  GLU 78  233 233 GLU GLU A . n 
A 1 79  ILE 79  234 234 ILE ILE A . n 
A 1 80  LYS 80  235 235 LYS LYS A . n 
A 1 81  VAL 81  236 236 VAL VAL A . n 
A 1 82  MET 82  237 237 MET MET A . n 
A 1 83  ALA 83  238 238 ALA ALA A . n 
A 1 84  LYS 84  239 239 LYS LYS A . n 
A 1 85  CYS 85  240 240 CYS CYS A . n 
A 1 86  GLN 86  241 241 GLN GLN A . n 
A 1 87  HIS 87  242 242 HIS HIS A . n 
A 1 88  GLU 88  243 243 GLU GLU A . n 
A 1 89  ASN 89  244 244 ASN ASN A . n 
A 1 90  LEU 90  245 245 LEU LEU A . n 
A 1 91  VAL 91  246 246 VAL VAL A . n 
A 1 92  GLU 92  247 247 GLU GLU A . n 
A 1 93  LEU 93  248 248 LEU LEU A . n 
A 1 94  LEU 94  249 249 LEU LEU A . n 
A 1 95  GLY 95  250 250 GLY GLY A . n 
A 1 96  PHE 96  251 251 PHE PHE A . n 
A 1 97  SER 97  252 252 SER SER A . n 
A 1 98  SER 98  253 253 SER SER A . n 
A 1 99  ASP 99  254 254 ASP ASP A . n 
A 1 100 GLY 100 255 255 GLY GLY A . n 
A 1 101 ASP 101 256 256 ASP ASP A . n 
A 1 102 ASP 102 257 257 ASP ASP A . n 
A 1 103 LEU 103 258 258 LEU LEU A . n 
A 1 104 CYS 104 259 259 CYS CYS A . n 
A 1 105 LEU 105 260 260 LEU LEU A . n 
A 1 106 VAL 106 261 261 VAL VAL A . n 
A 1 107 TYR 107 262 262 TYR TYR A . n 
A 1 108 VAL 108 263 263 VAL VAL A . n 
A 1 109 TYR 109 264 264 TYR TYR A . n 
A 1 110 MET 110 265 265 MET MET A . n 
A 1 111 PRO 111 266 266 PRO PRO A . n 
A 1 112 ASN 112 267 267 ASN ASN A . n 
A 1 113 GLY 113 268 268 GLY GLY A . n 
A 1 114 SER 114 269 269 SER SER A . n 
A 1 115 LEU 115 270 270 LEU LEU A . n 
A 1 116 LEU 116 271 271 LEU LEU A . n 
A 1 117 ASP 117 272 272 ASP ASP A . n 
A 1 118 ARG 118 273 273 ARG ARG A . n 
A 1 119 LEU 119 274 274 LEU LEU A . n 
A 1 120 SER 120 275 275 SER SER A . n 
A 1 121 CYS 121 276 276 CYS CYS A . n 
A 1 122 LEU 122 277 277 LEU LEU A . n 
A 1 123 ASP 123 278 278 ASP ASP A . n 
A 1 124 GLY 124 279 279 GLY GLY A . n 
A 1 125 THR 125 280 280 THR THR A . n 
A 1 126 PRO 126 281 281 PRO PRO A . n 
A 1 127 PRO 127 282 282 PRO PRO A . n 
A 1 128 LEU 128 283 283 LEU LEU A . n 
A 1 129 SEP 129 284 284 SEP SEP A . n 
A 1 130 TRP 130 285 285 TRP TRP A . n 
A 1 131 HIS 131 286 286 HIS HIS A . n 
A 1 132 MET 132 287 287 MET MET A . n 
A 1 133 ARG 133 288 288 ARG ARG A . n 
A 1 134 CYS 134 289 289 CYS CYS A . n 
A 1 135 LYS 135 290 290 LYS LYS A . n 
A 1 136 ILE 136 291 291 ILE ILE A . n 
A 1 137 ALA 137 292 292 ALA ALA A . n 
A 1 138 GLN 138 293 293 GLN GLN A . n 
A 1 139 GLY 139 294 294 GLY GLY A . n 
A 1 140 ALA 140 295 295 ALA ALA A . n 
A 1 141 ALA 141 296 296 ALA ALA A . n 
A 1 142 ASN 142 297 297 ASN ASN A . n 
A 1 143 GLY 143 298 298 GLY GLY A . n 
A 1 144 ILE 144 299 299 ILE ILE A . n 
A 1 145 ASN 145 300 300 ASN ASN A . n 
A 1 146 PHE 146 301 301 PHE PHE A . n 
A 1 147 LEU 147 302 302 LEU LEU A . n 
A 1 148 HIS 148 303 303 HIS HIS A . n 
A 1 149 GLU 149 304 304 GLU GLU A . n 
A 1 150 ASN 150 305 305 ASN ASN A . n 
A 1 151 HIS 151 306 306 HIS HIS A . n 
A 1 152 HIS 152 307 307 HIS HIS A . n 
A 1 153 ILE 153 308 308 ILE ILE A . n 
A 1 154 HIS 154 309 309 HIS HIS A . n 
A 1 155 ARG 155 310 310 ARG ARG A . n 
A 1 156 ASP 156 311 311 ASP ASP A . n 
A 1 157 ILE 157 312 312 ILE ILE A . n 
A 1 158 LYS 158 313 313 LYS LYS A . n 
A 1 159 SER 159 314 314 SER SER A . n 
A 1 160 ALA 160 315 315 ALA ALA A . n 
A 1 161 ASN 161 316 316 ASN ASN A . n 
A 1 162 ILE 162 317 317 ILE ILE A . n 
A 1 163 LEU 163 318 318 LEU LEU A . n 
A 1 164 LEU 164 319 319 LEU LEU A . n 
A 1 165 ASP 165 320 320 ASP ASP A . n 
A 1 166 GLU 166 321 321 GLU GLU A . n 
A 1 167 ALA 167 322 322 ALA ALA A . n 
A 1 168 PHE 168 323 323 PHE PHE A . n 
A 1 169 THR 169 324 324 THR THR A . n 
A 1 170 ALA 170 325 325 ALA ALA A . n 
A 1 171 LYS 171 326 326 LYS LYS A . n 
A 1 172 ILE 172 327 327 ILE ILE A . n 
A 1 173 SER 173 328 328 SER SER A . n 
A 1 174 ASP 174 329 329 ASP ASP A . n 
A 1 175 PHE 175 330 330 PHE PHE A . n 
A 1 176 GLY 176 331 331 GLY GLY A . n 
A 1 177 LEU 177 332 332 LEU LEU A . n 
A 1 178 ALA 178 333 333 ALA ALA A . n 
A 1 179 ARG 179 334 334 ARG ARG A . n 
A 1 180 ALA 180 335 335 ALA ALA A . n 
A 1 181 SER 181 336 336 SER SER A . n 
A 1 182 GLU 182 337 ?   ?   ?   A . n 
A 1 183 LYS 183 338 ?   ?   ?   A . n 
A 1 184 PHE 184 339 ?   ?   ?   A . n 
A 1 185 ALA 185 340 ?   ?   ?   A . n 
A 1 186 GLN 186 341 341 GLN GLN A . n 
A 1 187 THR 187 342 342 THR THR A . n 
A 1 188 VAL 188 343 343 VAL VAL A . n 
A 1 189 MET 189 344 344 MET MET A . n 
A 1 190 TPO 190 345 345 TPO TPO A . n 
A 1 191 SEP 191 346 346 SEP SEP A . n 
A 1 192 ARG 192 347 347 ARG ARG A . n 
A 1 193 ILE 193 348 348 ILE ILE A . n 
A 1 194 VAL 194 349 349 VAL VAL A . n 
A 1 195 GLY 195 350 350 GLY GLY A . n 
A 1 196 THR 196 351 351 THR THR A . n 
A 1 197 THR 197 352 352 THR THR A . n 
A 1 198 ALA 198 353 353 ALA ALA A . n 
A 1 199 TYR 199 354 354 TYR TYR A . n 
A 1 200 MET 200 355 355 MET MET A . n 
A 1 201 ALA 201 356 356 ALA ALA A . n 
A 1 202 PRO 202 357 357 PRO PRO A . n 
A 1 203 GLU 203 358 358 GLU GLU A . n 
A 1 204 ALA 204 359 359 ALA ALA A . n 
A 1 205 LEU 205 360 360 LEU LEU A . n 
A 1 206 ARG 206 361 361 ARG ARG A . n 
A 1 207 GLY 207 362 362 GLY GLY A . n 
A 1 208 GLU 208 363 363 GLU GLU A . n 
A 1 209 ILE 209 364 364 ILE ILE A . n 
A 1 210 THR 210 365 365 THR THR A . n 
A 1 211 PRO 211 366 366 PRO PRO A . n 
A 1 212 LYS 212 367 367 LYS LYS A . n 
A 1 213 SER 213 368 368 SER SER A . n 
A 1 214 ASP 214 369 369 ASP ASP A . n 
A 1 215 ILE 215 370 370 ILE ILE A . n 
A 1 216 TYR 216 371 371 TYR TYR A . n 
A 1 217 SER 217 372 372 SER SER A . n 
A 1 218 PHE 218 373 373 PHE PHE A . n 
A 1 219 GLY 219 374 374 GLY GLY A . n 
A 1 220 VAL 220 375 375 VAL VAL A . n 
A 1 221 VAL 221 376 376 VAL VAL A . n 
A 1 222 LEU 222 377 377 LEU LEU A . n 
A 1 223 LEU 223 378 378 LEU LEU A . n 
A 1 224 GLU 224 379 379 GLU GLU A . n 
A 1 225 ILE 225 380 380 ILE ILE A . n 
A 1 226 ILE 226 381 381 ILE ILE A . n 
A 1 227 THR 227 382 382 THR THR A . n 
A 1 228 GLY 228 383 383 GLY GLY A . n 
A 1 229 LEU 229 384 384 LEU LEU A . n 
A 1 230 PRO 230 385 385 PRO PRO A . n 
A 1 231 ALA 231 386 386 ALA ALA A . n 
A 1 232 VAL 232 387 387 VAL VAL A . n 
A 1 233 ASP 233 388 388 ASP ASP A . n 
A 1 234 GLU 234 389 389 GLU GLU A . n 
A 1 235 HIS 235 390 390 HIS HIS A . n 
A 1 236 ARG 236 391 391 ARG ARG A . n 
A 1 237 GLU 237 392 392 GLU GLU A . n 
A 1 238 PRO 238 393 393 PRO PRO A . n 
A 1 239 GLN 239 394 394 GLN GLN A . n 
A 1 240 LEU 240 395 395 LEU LEU A . n 
A 1 241 LEU 241 396 396 LEU LEU A . n 
A 1 242 LEU 242 397 397 LEU LEU A . n 
A 1 243 ASP 243 398 398 ASP ASP A . n 
A 1 244 ILE 244 399 399 ILE ILE A . n 
A 1 245 LYS 245 400 400 LYS LYS A . n 
A 1 246 GLU 246 401 401 GLU GLU A . n 
A 1 247 GLU 247 402 402 GLU GLU A . n 
A 1 248 ILE 248 403 403 ILE ILE A . n 
A 1 249 GLU 249 404 404 GLU GLU A . n 
A 1 250 ASP 250 405 405 ASP ASP A . n 
A 1 251 GLU 251 406 406 GLU GLU A . n 
A 1 252 GLU 252 407 407 GLU GLU A . n 
A 1 253 LYS 253 408 408 LYS LYS A . n 
A 1 254 THR 254 409 409 THR THR A . n 
A 1 255 ILE 255 410 410 ILE ILE A . n 
A 1 256 GLU 256 411 411 GLU GLU A . n 
A 1 257 ASP 257 412 412 ASP ASP A . n 
A 1 258 TYR 258 413 413 TYR TYR A . n 
A 1 259 ILE 259 414 414 ILE ILE A . n 
A 1 260 ASP 260 415 415 ASP ASP A . n 
A 1 261 LYS 261 416 416 LYS LYS A . n 
A 1 262 LYS 262 417 417 LYS LYS A . n 
A 1 263 MET 263 418 418 MET MET A . n 
A 1 264 ASN 264 419 419 ASN ASN A . n 
A 1 265 ASP 265 420 420 ASP ASP A . n 
A 1 266 ALA 266 421 421 ALA ALA A . n 
A 1 267 ASP 267 422 422 ASP ASP A . n 
A 1 268 SER 268 423 423 SER SER A . n 
A 1 269 THR 269 424 424 THR THR A . n 
A 1 270 SER 270 425 425 SER SER A . n 
A 1 271 VAL 271 426 426 VAL VAL A . n 
A 1 272 GLU 272 427 427 GLU GLU A . n 
A 1 273 ALA 273 428 428 ALA ALA A . n 
A 1 274 MET 274 429 429 MET MET A . n 
A 1 275 TYR 275 430 430 TYR TYR A . n 
A 1 276 SER 276 431 431 SER SER A . n 
A 1 277 VAL 277 432 432 VAL VAL A . n 
A 1 278 ALA 278 433 433 ALA ALA A . n 
A 1 279 SER 279 434 434 SER SER A . n 
A 1 280 GLN 280 435 435 GLN GLN A . n 
A 1 281 CYS 281 436 436 CYS CYS A . n 
A 1 282 LEU 282 437 437 LEU LEU A . n 
A 1 283 HIS 283 438 438 HIS HIS A . n 
A 1 284 GLU 284 439 439 GLU GLU A . n 
A 1 285 LYS 285 440 440 LYS LYS A . n 
A 1 286 LYS 286 441 441 LYS LYS A . n 
A 1 287 ASN 287 442 442 ASN ASN A . n 
A 1 288 LYS 288 443 443 LYS LYS A . n 
A 1 289 ARG 289 444 444 ARG ARG A . n 
A 1 290 PRO 290 445 445 PRO PRO A . n 
A 1 291 ASP 291 446 446 ASP ASP A . n 
A 1 292 ILE 292 447 447 ILE ILE A . n 
A 1 293 LYS 293 448 448 LYS LYS A . n 
A 1 294 LYS 294 449 449 LYS LYS A . n 
A 1 295 VAL 295 450 450 VAL VAL A . n 
A 1 296 GLN 296 451 451 GLN GLN A . n 
A 1 297 GLN 297 452 452 GLN GLN A . n 
A 1 298 LEU 298 453 453 LEU LEU A . n 
A 1 299 LEU 299 454 454 LEU LEU A . n 
A 1 300 GLN 300 455 455 GLN GLN A . n 
A 1 301 GLU 301 456 456 GLU GLU A . n 
A 1 302 MET 302 457 457 MET MET A . n 
A 1 303 THR 303 458 458 THR THR A . n 
A 1 304 ALA 304 459 ?   ?   ?   A . n 
A 1 305 SER 305 460 ?   ?   ?   A . n 
B 2 1   GLY 1   156 ?   ?   ?   B . n 
B 2 2   ALA 2   157 ?   ?   ?   B . n 
B 2 3   MET 3   158 ?   ?   ?   B . n 
B 2 4   GLY 4   159 ?   ?   ?   B . n 
B 2 5   VAL 5   160 ?   ?   ?   B . n 
B 2 6   SER 6   161 ?   ?   ?   B . n 
B 2 7   ASP 7   162 ?   ?   ?   B . n 
B 2 8   THR 8   163 ?   ?   ?   B . n 
B 2 9   ARG 9   164 ?   ?   ?   B . n 
B 2 10  PHE 10  165 165 PHE PHE B . n 
B 2 11  HIS 11  166 166 HIS HIS B . n 
B 2 12  SER 12  167 167 SER SER B . n 
B 2 13  PHE 13  168 168 PHE PHE B . n 
B 2 14  SER 14  169 169 SER SER B . n 
B 2 15  PHE 15  170 170 PHE PHE B . n 
B 2 16  TYR 16  171 171 TYR TYR B . n 
B 2 17  GLU 17  172 172 GLU GLU B . n 
B 2 18  LEU 18  173 173 LEU LEU B . n 
B 2 19  LYS 19  174 174 LYS LYS B . n 
B 2 20  ASN 20  175 175 ASN ASN B . n 
B 2 21  VAL 21  176 176 VAL VAL B . n 
B 2 22  THR 22  177 177 THR THR B . n 
B 2 23  ASN 23  178 178 ASN ASN B . n 
B 2 24  ASN 24  179 179 ASN ASN B . n 
B 2 25  PHE 25  180 180 PHE PHE B . n 
B 2 26  ASP 26  181 181 ASP ASP B . n 
B 2 27  GLU 27  182 182 GLU GLU B . n 
B 2 28  ARG 28  183 183 ARG ARG B . n 
B 2 29  PRO 29  184 184 PRO PRO B . n 
B 2 30  ILE 30  185 185 ILE ILE B . n 
B 2 31  SER 31  186 ?   ?   ?   B . n 
B 2 32  VAL 32  187 ?   ?   ?   B . n 
B 2 33  GLY 33  188 ?   ?   ?   B . n 
B 2 34  GLY 34  189 189 GLY GLY B . n 
B 2 35  ASN 35  190 190 ASN ASN B . n 
B 2 36  LYS 36  191 191 LYS LYS B . n 
B 2 37  MET 37  192 192 MET MET B . n 
B 2 38  GLY 38  193 193 GLY GLY B . n 
B 2 39  GLU 39  194 194 GLU GLU B . n 
B 2 40  GLY 40  195 195 GLY GLY B . n 
B 2 41  GLY 41  196 196 GLY GLY B . n 
B 2 42  PHE 42  197 197 PHE PHE B . n 
B 2 43  GLY 43  198 198 GLY GLY B . n 
B 2 44  VAL 44  199 199 VAL VAL B . n 
B 2 45  VAL 45  200 200 VAL VAL B . n 
B 2 46  TYR 46  201 201 TYR TYR B . n 
B 2 47  LYS 47  202 202 LYS LYS B . n 
B 2 48  GLY 48  203 203 GLY GLY B . n 
B 2 49  TYR 49  204 204 TYR TYR B . n 
B 2 50  VAL 50  205 205 VAL VAL B . n 
B 2 51  ASN 51  206 ?   ?   ?   B . n 
B 2 52  ASN 52  207 ?   ?   ?   B . n 
B 2 53  THR 53  208 208 THR THR B . n 
B 2 54  THR 54  209 209 THR THR B . n 
B 2 55  VAL 55  210 210 VAL VAL B . n 
B 2 56  ALA 56  211 211 ALA ALA B . n 
B 2 57  VAL 57  212 212 VAL VAL B . n 
B 2 58  LYS 58  213 213 LYS LYS B . n 
B 2 59  LYS 59  214 214 LYS LYS B . n 
B 2 60  LEU 60  215 215 LEU LEU B . n 
B 2 61  ALA 61  216 ?   ?   ?   B . n 
B 2 62  ALA 62  217 ?   ?   ?   B . n 
B 2 63  MET 63  218 ?   ?   ?   B . n 
B 2 64  VAL 64  219 ?   ?   ?   B . n 
B 2 65  ASP 65  220 ?   ?   ?   B . n 
B 2 66  ILE 66  221 ?   ?   ?   B . n 
B 2 67  THR 67  222 ?   ?   ?   B . n 
B 2 68  THR 68  223 ?   ?   ?   B . n 
B 2 69  GLU 69  224 224 GLU GLU B . n 
B 2 70  GLU 70  225 225 GLU GLU B . n 
B 2 71  LEU 71  226 226 LEU LEU B . n 
B 2 72  LYS 72  227 227 LYS LYS B . n 
B 2 73  GLN 73  228 228 GLN GLN B . n 
B 2 74  GLN 74  229 229 GLN GLN B . n 
B 2 75  PHE 75  230 230 PHE PHE B . n 
B 2 76  ASP 76  231 231 ASP ASP B . n 
B 2 77  GLN 77  232 232 GLN GLN B . n 
B 2 78  GLU 78  233 233 GLU GLU B . n 
B 2 79  ILE 79  234 234 ILE ILE B . n 
B 2 80  LYS 80  235 235 LYS LYS B . n 
B 2 81  VAL 81  236 236 VAL VAL B . n 
B 2 82  MET 82  237 237 MET MET B . n 
B 2 83  ALA 83  238 238 ALA ALA B . n 
B 2 84  LYS 84  239 239 LYS LYS B . n 
B 2 85  CYS 85  240 240 CYS CYS B . n 
B 2 86  GLN 86  241 241 GLN GLN B . n 
B 2 87  HIS 87  242 242 HIS HIS B . n 
B 2 88  GLU 88  243 243 GLU GLU B . n 
B 2 89  ASN 89  244 244 ASN ASN B . n 
B 2 90  LEU 90  245 245 LEU LEU B . n 
B 2 91  VAL 91  246 246 VAL VAL B . n 
B 2 92  GLU 92  247 247 GLU GLU B . n 
B 2 93  LEU 93  248 248 LEU LEU B . n 
B 2 94  LEU 94  249 ?   ?   ?   B . n 
B 2 95  GLY 95  250 ?   ?   ?   B . n 
B 2 96  PHE 96  251 ?   ?   ?   B . n 
B 2 97  SER 97  252 ?   ?   ?   B . n 
B 2 98  SER 98  253 ?   ?   ?   B . n 
B 2 99  ASP 99  254 ?   ?   ?   B . n 
B 2 100 GLY 100 255 ?   ?   ?   B . n 
B 2 101 ASP 101 256 ?   ?   ?   B . n 
B 2 102 ASP 102 257 257 ASP ASP B . n 
B 2 103 LEU 103 258 258 LEU LEU B . n 
B 2 104 CYS 104 259 259 CYS CYS B . n 
B 2 105 LEU 105 260 260 LEU LEU B . n 
B 2 106 VAL 106 261 261 VAL VAL B . n 
B 2 107 TYR 107 262 262 TYR TYR B . n 
B 2 108 VAL 108 263 263 VAL VAL B . n 
B 2 109 TYR 109 264 264 TYR TYR B . n 
B 2 110 MET 110 265 265 MET MET B . n 
B 2 111 PRO 111 266 266 PRO PRO B . n 
B 2 112 ASN 112 267 267 ASN ASN B . n 
B 2 113 GLY 113 268 268 GLY GLY B . n 
B 2 114 SER 114 269 269 SER SER B . n 
B 2 115 LEU 115 270 270 LEU LEU B . n 
B 2 116 LEU 116 271 271 LEU LEU B . n 
B 2 117 ASP 117 272 272 ASP ASP B . n 
B 2 118 ARG 118 273 273 ARG ARG B . n 
B 2 119 LEU 119 274 274 LEU LEU B . n 
B 2 120 SER 120 275 275 SER SER B . n 
B 2 121 CYS 121 276 276 CYS CYS B . n 
B 2 122 LEU 122 277 277 LEU LEU B . n 
B 2 123 ASP 123 278 278 ASP ASP B . n 
B 2 124 GLY 124 279 279 GLY GLY B . n 
B 2 125 THR 125 280 280 THR THR B . n 
B 2 126 PRO 126 281 281 PRO PRO B . n 
B 2 127 PRO 127 282 282 PRO PRO B . n 
B 2 128 LEU 128 283 283 LEU LEU B . n 
B 2 129 SER 129 284 284 SER SER B . n 
B 2 130 TRP 130 285 285 TRP TRP B . n 
B 2 131 HIS 131 286 286 HIS HIS B . n 
B 2 132 MET 132 287 287 MET MET B . n 
B 2 133 ARG 133 288 288 ARG ARG B . n 
B 2 134 CYS 134 289 289 CYS CYS B . n 
B 2 135 LYS 135 290 290 LYS LYS B . n 
B 2 136 ILE 136 291 291 ILE ILE B . n 
B 2 137 ALA 137 292 292 ALA ALA B . n 
B 2 138 GLN 138 293 293 GLN GLN B . n 
B 2 139 GLY 139 294 294 GLY GLY B . n 
B 2 140 ALA 140 295 295 ALA ALA B . n 
B 2 141 ALA 141 296 296 ALA ALA B . n 
B 2 142 ASN 142 297 297 ASN ASN B . n 
B 2 143 GLY 143 298 298 GLY GLY B . n 
B 2 144 ILE 144 299 299 ILE ILE B . n 
B 2 145 ASN 145 300 300 ASN ASN B . n 
B 2 146 PHE 146 301 301 PHE PHE B . n 
B 2 147 LEU 147 302 302 LEU LEU B . n 
B 2 148 HIS 148 303 303 HIS HIS B . n 
B 2 149 GLU 149 304 304 GLU GLU B . n 
B 2 150 ASN 150 305 305 ASN ASN B . n 
B 2 151 HIS 151 306 306 HIS HIS B . n 
B 2 152 HIS 152 307 307 HIS HIS B . n 
B 2 153 ILE 153 308 308 ILE ILE B . n 
B 2 154 HIS 154 309 309 HIS HIS B . n 
B 2 155 ARG 155 310 310 ARG ARG B . n 
B 2 156 ASP 156 311 311 ASP ASP B . n 
B 2 157 ILE 157 312 312 ILE ILE B . n 
B 2 158 LYS 158 313 313 LYS LYS B . n 
B 2 159 SER 159 314 314 SER SER B . n 
B 2 160 ALA 160 315 315 ALA ALA B . n 
B 2 161 ASN 161 316 316 ASN ASN B . n 
B 2 162 ILE 162 317 317 ILE ILE B . n 
B 2 163 LEU 163 318 318 LEU LEU B . n 
B 2 164 LEU 164 319 319 LEU LEU B . n 
B 2 165 ASP 165 320 320 ASP ASP B . n 
B 2 166 GLU 166 321 321 GLU GLU B . n 
B 2 167 ALA 167 322 322 ALA ALA B . n 
B 2 168 PHE 168 323 323 PHE PHE B . n 
B 2 169 THR 169 324 324 THR THR B . n 
B 2 170 ALA 170 325 325 ALA ALA B . n 
B 2 171 LYS 171 326 326 LYS LYS B . n 
B 2 172 ILE 172 327 327 ILE ILE B . n 
B 2 173 SER 173 328 328 SER SER B . n 
B 2 174 ASP 174 329 329 ASP ASP B . n 
B 2 175 PHE 175 330 330 PHE PHE B . n 
B 2 176 GLY 176 331 331 GLY GLY B . n 
B 2 177 LEU 177 332 332 LEU LEU B . n 
B 2 178 ALA 178 333 ?   ?   ?   B . n 
B 2 179 ARG 179 334 ?   ?   ?   B . n 
B 2 180 ALA 180 335 ?   ?   ?   B . n 
B 2 181 SER 181 336 ?   ?   ?   B . n 
B 2 182 GLU 182 337 ?   ?   ?   B . n 
B 2 183 LYS 183 338 ?   ?   ?   B . n 
B 2 184 PHE 184 339 ?   ?   ?   B . n 
B 2 185 ALA 185 340 ?   ?   ?   B . n 
B 2 186 GLN 186 341 ?   ?   ?   B . n 
B 2 187 THR 187 342 342 THR THR B . n 
B 2 188 VAL 188 343 343 VAL VAL B . n 
B 2 189 MET 189 344 344 MET MET B . n 
B 2 190 TPO 190 345 345 TPO TPO B . n 
B 2 191 SEP 191 346 346 SEP SEP B . n 
B 2 192 ARG 192 347 347 ARG ARG B . n 
B 2 193 ILE 193 348 348 ILE ILE B . n 
B 2 194 VAL 194 349 349 VAL VAL B . n 
B 2 195 GLY 195 350 ?   ?   ?   B . n 
B 2 196 THR 196 351 ?   ?   ?   B . n 
B 2 197 THR 197 352 352 THR THR B . n 
B 2 198 ALA 198 353 353 ALA ALA B . n 
B 2 199 TYR 199 354 354 TYR TYR B . n 
B 2 200 MET 200 355 355 MET MET B . n 
B 2 201 ALA 201 356 356 ALA ALA B . n 
B 2 202 PRO 202 357 357 PRO PRO B . n 
B 2 203 GLU 203 358 358 GLU GLU B . n 
B 2 204 ALA 204 359 359 ALA ALA B . n 
B 2 205 LEU 205 360 360 LEU LEU B . n 
B 2 206 ARG 206 361 361 ARG ARG B . n 
B 2 207 GLY 207 362 362 GLY GLY B . n 
B 2 208 GLU 208 363 363 GLU GLU B . n 
B 2 209 ILE 209 364 364 ILE ILE B . n 
B 2 210 THR 210 365 365 THR THR B . n 
B 2 211 PRO 211 366 366 PRO PRO B . n 
B 2 212 LYS 212 367 367 LYS LYS B . n 
B 2 213 SER 213 368 368 SER SER B . n 
B 2 214 ASP 214 369 369 ASP ASP B . n 
B 2 215 ILE 215 370 370 ILE ILE B . n 
B 2 216 TYR 216 371 371 TYR TYR B . n 
B 2 217 SER 217 372 372 SER SER B . n 
B 2 218 PHE 218 373 373 PHE PHE B . n 
B 2 219 GLY 219 374 374 GLY GLY B . n 
B 2 220 VAL 220 375 375 VAL VAL B . n 
B 2 221 VAL 221 376 376 VAL VAL B . n 
B 2 222 LEU 222 377 377 LEU LEU B . n 
B 2 223 LEU 223 378 378 LEU LEU B . n 
B 2 224 GLU 224 379 379 GLU GLU B . n 
B 2 225 ILE 225 380 380 ILE ILE B . n 
B 2 226 ILE 226 381 381 ILE ILE B . n 
B 2 227 THR 227 382 382 THR THR B . n 
B 2 228 GLY 228 383 383 GLY GLY B . n 
B 2 229 LEU 229 384 384 LEU LEU B . n 
B 2 230 PRO 230 385 385 PRO PRO B . n 
B 2 231 ALA 231 386 386 ALA ALA B . n 
B 2 232 VAL 232 387 387 VAL VAL B . n 
B 2 233 ASP 233 388 388 ASP ASP B . n 
B 2 234 GLU 234 389 389 GLU GLU B . n 
B 2 235 HIS 235 390 390 HIS HIS B . n 
B 2 236 ARG 236 391 391 ARG ARG B . n 
B 2 237 GLU 237 392 392 GLU GLU B . n 
B 2 238 PRO 238 393 393 PRO PRO B . n 
B 2 239 GLN 239 394 394 GLN GLN B . n 
B 2 240 LEU 240 395 395 LEU LEU B . n 
B 2 241 LEU 241 396 396 LEU LEU B . n 
B 2 242 LEU 242 397 397 LEU LEU B . n 
B 2 243 ASP 243 398 398 ASP ASP B . n 
B 2 244 ILE 244 399 399 ILE ILE B . n 
B 2 245 LYS 245 400 400 LYS LYS B . n 
B 2 246 GLU 246 401 401 GLU GLU B . n 
B 2 247 GLU 247 402 402 GLU GLU B . n 
B 2 248 ILE 248 403 403 ILE ILE B . n 
B 2 249 GLU 249 404 404 GLU GLU B . n 
B 2 250 ASP 250 405 405 ASP ASP B . n 
B 2 251 GLU 251 406 406 GLU GLU B . n 
B 2 252 GLU 252 407 407 GLU GLU B . n 
B 2 253 LYS 253 408 408 LYS LYS B . n 
B 2 254 THR 254 409 409 THR THR B . n 
B 2 255 ILE 255 410 410 ILE ILE B . n 
B 2 256 GLU 256 411 411 GLU GLU B . n 
B 2 257 ASP 257 412 412 ASP ASP B . n 
B 2 258 TYR 258 413 413 TYR TYR B . n 
B 2 259 ILE 259 414 414 ILE ILE B . n 
B 2 260 ASP 260 415 415 ASP ASP B . n 
B 2 261 LYS 261 416 416 LYS LYS B . n 
B 2 262 LYS 262 417 417 LYS LYS B . n 
B 2 263 MET 263 418 418 MET MET B . n 
B 2 264 ASN 264 419 419 ASN ASN B . n 
B 2 265 ASP 265 420 420 ASP ASP B . n 
B 2 266 ALA 266 421 421 ALA ALA B . n 
B 2 267 ASP 267 422 422 ASP ASP B . n 
B 2 268 SER 268 423 423 SER SER B . n 
B 2 269 THR 269 424 424 THR THR B . n 
B 2 270 SER 270 425 425 SER SER B . n 
B 2 271 VAL 271 426 426 VAL VAL B . n 
B 2 272 GLU 272 427 427 GLU GLU B . n 
B 2 273 ALA 273 428 428 ALA ALA B . n 
B 2 274 MET 274 429 429 MET MET B . n 
B 2 275 TYR 275 430 430 TYR TYR B . n 
B 2 276 SER 276 431 431 SER SER B . n 
B 2 277 VAL 277 432 432 VAL VAL B . n 
B 2 278 ALA 278 433 433 ALA ALA B . n 
B 2 279 SER 279 434 434 SER SER B . n 
B 2 280 GLN 280 435 435 GLN GLN B . n 
B 2 281 CYS 281 436 436 CYS CYS B . n 
B 2 282 LEU 282 437 437 LEU LEU B . n 
B 2 283 HIS 283 438 438 HIS HIS B . n 
B 2 284 GLU 284 439 439 GLU GLU B . n 
B 2 285 LYS 285 440 440 LYS LYS B . n 
B 2 286 LYS 286 441 441 LYS LYS B . n 
B 2 287 ASN 287 442 442 ASN ASN B . n 
B 2 288 LYS 288 443 443 LYS LYS B . n 
B 2 289 ARG 289 444 444 ARG ARG B . n 
B 2 290 PRO 290 445 445 PRO PRO B . n 
B 2 291 ASP 291 446 446 ASP ASP B . n 
B 2 292 ILE 292 447 447 ILE ILE B . n 
B 2 293 LYS 293 448 448 LYS LYS B . n 
B 2 294 LYS 294 449 449 LYS LYS B . n 
B 2 295 VAL 295 450 450 VAL VAL B . n 
B 2 296 GLN 296 451 451 GLN GLN B . n 
B 2 297 GLN 297 452 452 GLN GLN B . n 
B 2 298 LEU 298 453 453 LEU LEU B . n 
B 2 299 LEU 299 454 454 LEU LEU B . n 
B 2 300 GLN 300 455 455 GLN GLN B . n 
B 2 301 GLU 301 456 456 GLU GLU B . n 
B 2 302 MET 302 457 457 MET MET B . n 
B 2 303 THR 303 458 458 THR THR B . n 
B 2 304 ALA 304 459 459 ALA ALA B . n 
B 2 305 SER 305 460 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZVG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZVG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
C 3 ZVG 1  501 501 ZVG LG1 A . 
D 4 SO4 1  502 502 SO4 SO4 A . 
E 3 ZVG 1  501 501 ZVG LG1 B . 
F 4 SO4 1  502 502 SO4 SO4 B . 
G 5 HOH 1  601 601 HOH HOH A . 
G 5 HOH 2  602 602 HOH HOH A . 
G 5 HOH 3  603 603 HOH HOH A . 
G 5 HOH 4  604 605 HOH HOH A . 
G 5 HOH 5  605 604 HOH HOH A . 
G 5 HOH 6  606 606 HOH HOH A . 
G 5 HOH 7  607 607 HOH HOH A . 
G 5 HOH 8  608 608 HOH HOH A . 
G 5 HOH 9  609 609 HOH HOH A . 
G 5 HOH 10 610 610 HOH HOH A . 
G 5 HOH 11 611 611 HOH HOH A . 
G 5 HOH 12 612 612 HOH HOH A . 
G 5 HOH 13 613 613 HOH HOH A . 
G 5 HOH 14 614 614 HOH HOH A . 
G 5 HOH 15 615 615 HOH HOH A . 
G 5 HOH 16 616 616 HOH HOH A . 
G 5 HOH 17 617 617 HOH HOH A . 
G 5 HOH 18 618 618 HOH HOH A . 
G 5 HOH 19 619 619 HOH HOH A . 
G 5 HOH 20 620 620 HOH HOH A . 
G 5 HOH 21 621 621 HOH HOH A . 
G 5 HOH 22 622 622 HOH HOH A . 
G 5 HOH 23 623 623 HOH HOH A . 
G 5 HOH 24 624 624 HOH HOH A . 
G 5 HOH 25 625 625 HOH HOH A . 
G 5 HOH 26 626 627 HOH HOH A . 
G 5 HOH 27 627 626 HOH HOH A . 
G 5 HOH 28 628 628 HOH HOH A . 
G 5 HOH 29 629 629 HOH HOH A . 
G 5 HOH 30 630 630 HOH HOH A . 
G 5 HOH 31 631 631 HOH HOH A . 
G 5 HOH 32 632 632 HOH HOH A . 
G 5 HOH 33 633 633 HOH HOH A . 
G 5 HOH 34 634 634 HOH HOH A . 
G 5 HOH 35 635 635 HOH HOH A . 
G 5 HOH 36 636 636 HOH HOH A . 
G 5 HOH 37 637 637 HOH HOH A . 
G 5 HOH 38 638 638 HOH HOH A . 
H 5 HOH 1  601 601 HOH HOH B . 
H 5 HOH 2  602 602 HOH HOH B . 
H 5 HOH 3  603 603 HOH HOH B . 
H 5 HOH 4  604 604 HOH HOH B . 
H 5 HOH 5  605 605 HOH HOH B . 
H 5 HOH 6  606 606 HOH HOH B . 
H 5 HOH 7  607 607 HOH HOH B . 
H 5 HOH 8  608 608 HOH HOH B . 
H 5 HOH 9  609 609 HOH HOH B . 
H 5 HOH 10 610 610 HOH HOH B . 
H 5 HOH 11 611 611 HOH HOH B . 
H 5 HOH 12 612 612 HOH HOH B . 
H 5 HOH 13 613 613 HOH HOH B . 
H 5 HOH 14 614 614 HOH HOH B . 
H 5 HOH 15 615 615 HOH HOH B . 
H 5 HOH 16 616 616 HOH HOH B . 
H 5 HOH 17 617 617 HOH HOH B . 
H 5 HOH 18 618 618 HOH HOH B . 
H 5 HOH 19 619 619 HOH HOH B . 
H 5 HOH 20 620 620 HOH HOH B . 
H 5 HOH 21 621 621 HOH HOH B . 
H 5 HOH 22 622 622 HOH HOH B . 
H 5 HOH 23 623 623 HOH HOH B . 
H 5 HOH 24 624 624 HOH HOH B . 
H 5 HOH 25 625 625 HOH HOH B . 
H 5 HOH 26 626 626 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ILE 221 ? CG1 ? A ILE 66  CG1 
2   1 Y 1 A ILE 221 ? CG2 ? A ILE 66  CG2 
3   1 Y 1 A ILE 221 ? CD1 ? A ILE 66  CD1 
4   1 Y 1 A GLU 225 ? CG  ? A GLU 70  CG  
5   1 Y 1 A GLU 225 ? CD  ? A GLU 70  CD  
6   1 Y 1 A GLU 225 ? OE1 ? A GLU 70  OE1 
7   1 Y 1 A GLU 225 ? OE2 ? A GLU 70  OE2 
8   1 Y 1 A LYS 227 ? CG  ? A LYS 72  CG  
9   1 Y 1 A LYS 227 ? CD  ? A LYS 72  CD  
10  1 Y 1 A LYS 227 ? CE  ? A LYS 72  CE  
11  1 Y 1 A LYS 227 ? NZ  ? A LYS 72  NZ  
12  1 Y 1 A GLN 228 ? CG  ? A GLN 73  CG  
13  1 Y 1 A GLN 228 ? CD  ? A GLN 73  CD  
14  1 Y 1 A GLN 228 ? OE1 ? A GLN 73  OE1 
15  1 Y 1 A GLN 228 ? NE2 ? A GLN 73  NE2 
16  1 Y 1 A LYS 235 ? CG  ? A LYS 80  CG  
17  1 Y 1 A LYS 235 ? CD  ? A LYS 80  CD  
18  1 Y 1 A LYS 235 ? CE  ? A LYS 80  CE  
19  1 Y 1 A LYS 235 ? NZ  ? A LYS 80  NZ  
20  1 Y 1 A LYS 239 ? CG  ? A LYS 84  CG  
21  1 Y 1 A LYS 239 ? CD  ? A LYS 84  CD  
22  1 Y 1 A LYS 239 ? CE  ? A LYS 84  CE  
23  1 Y 1 A LYS 239 ? NZ  ? A LYS 84  NZ  
24  1 Y 1 A ASP 254 ? CG  ? A ASP 99  CG  
25  1 Y 1 A ASP 254 ? OD1 ? A ASP 99  OD1 
26  1 Y 1 A ASP 254 ? OD2 ? A ASP 99  OD2 
27  1 Y 1 A ASP 256 ? CG  ? A ASP 101 CG  
28  1 Y 1 A ASP 256 ? OD1 ? A ASP 101 OD1 
29  1 Y 1 A ASP 256 ? OD2 ? A ASP 101 OD2 
30  1 Y 1 A ASP 257 ? CG  ? A ASP 102 CG  
31  1 Y 1 A ASP 257 ? OD1 ? A ASP 102 OD1 
32  1 Y 1 A ASP 257 ? OD2 ? A ASP 102 OD2 
33  1 Y 1 A SER 336 ? OG  ? A SER 181 OG  
34  1 Y 1 A GLN 341 ? CG  ? A GLN 186 CG  
35  1 Y 1 A GLN 341 ? CD  ? A GLN 186 CD  
36  1 Y 1 A GLN 341 ? OE1 ? A GLN 186 OE1 
37  1 Y 1 A GLN 341 ? NE2 ? A GLN 186 NE2 
38  1 Y 1 A ARG 347 ? CG  ? A ARG 192 CG  
39  1 Y 1 A ARG 347 ? CD  ? A ARG 192 CD  
40  1 Y 1 A ARG 347 ? NE  ? A ARG 192 NE  
41  1 Y 1 A ARG 347 ? CZ  ? A ARG 192 CZ  
42  1 Y 1 A ARG 347 ? NH1 ? A ARG 192 NH1 
43  1 Y 1 A ARG 347 ? NH2 ? A ARG 192 NH2 
44  1 Y 1 A LYS 367 ? CG  ? A LYS 212 CG  
45  1 Y 1 A LYS 367 ? CD  ? A LYS 212 CD  
46  1 Y 1 A LYS 367 ? CE  ? A LYS 212 CE  
47  1 Y 1 A LYS 367 ? NZ  ? A LYS 212 NZ  
48  1 Y 1 A GLU 389 ? CG  ? A GLU 234 CG  
49  1 Y 1 A GLU 389 ? CD  ? A GLU 234 CD  
50  1 Y 1 A GLU 389 ? OE1 ? A GLU 234 OE1 
51  1 Y 1 A GLU 389 ? OE2 ? A GLU 234 OE2 
52  1 Y 1 A LYS 400 ? CG  ? A LYS 245 CG  
53  1 Y 1 A LYS 400 ? CD  ? A LYS 245 CD  
54  1 Y 1 A LYS 400 ? CE  ? A LYS 245 CE  
55  1 Y 1 A LYS 400 ? NZ  ? A LYS 245 NZ  
56  1 Y 1 A GLU 401 ? CG  ? A GLU 246 CG  
57  1 Y 1 A GLU 401 ? CD  ? A GLU 246 CD  
58  1 Y 1 A GLU 401 ? OE1 ? A GLU 246 OE1 
59  1 Y 1 A GLU 401 ? OE2 ? A GLU 246 OE2 
60  1 Y 1 A GLU 406 ? CG  ? A GLU 251 CG  
61  1 Y 1 A GLU 406 ? CD  ? A GLU 251 CD  
62  1 Y 1 A GLU 406 ? OE1 ? A GLU 251 OE1 
63  1 Y 1 A GLU 406 ? OE2 ? A GLU 251 OE2 
64  1 Y 1 A GLU 407 ? CG  ? A GLU 252 CG  
65  1 Y 1 A GLU 407 ? CD  ? A GLU 252 CD  
66  1 Y 1 A GLU 407 ? OE1 ? A GLU 252 OE1 
67  1 Y 1 A GLU 407 ? OE2 ? A GLU 252 OE2 
68  1 Y 1 A LYS 408 ? CE  ? A LYS 253 CE  
69  1 Y 1 A LYS 408 ? NZ  ? A LYS 253 NZ  
70  1 Y 1 A GLU 411 ? CG  ? A GLU 256 CG  
71  1 Y 1 A GLU 411 ? CD  ? A GLU 256 CD  
72  1 Y 1 A GLU 411 ? OE1 ? A GLU 256 OE1 
73  1 Y 1 A GLU 411 ? OE2 ? A GLU 256 OE2 
74  1 Y 1 A LYS 416 ? CG  ? A LYS 261 CG  
75  1 Y 1 A LYS 416 ? CD  ? A LYS 261 CD  
76  1 Y 1 A LYS 416 ? CE  ? A LYS 261 CE  
77  1 Y 1 A LYS 416 ? NZ  ? A LYS 261 NZ  
78  1 Y 1 A GLU 427 ? CG  ? A GLU 272 CG  
79  1 Y 1 A GLU 427 ? CD  ? A GLU 272 CD  
80  1 Y 1 A GLU 427 ? OE1 ? A GLU 272 OE1 
81  1 Y 1 A GLU 427 ? OE2 ? A GLU 272 OE2 
82  1 Y 1 A LYS 440 ? CG  ? A LYS 285 CG  
83  1 Y 1 A LYS 440 ? CD  ? A LYS 285 CD  
84  1 Y 1 A LYS 440 ? CE  ? A LYS 285 CE  
85  1 Y 1 A LYS 440 ? NZ  ? A LYS 285 NZ  
86  1 Y 1 A LYS 443 ? CG  ? A LYS 288 CG  
87  1 Y 1 A LYS 443 ? CD  ? A LYS 288 CD  
88  1 Y 1 A LYS 443 ? CE  ? A LYS 288 CE  
89  1 Y 1 A LYS 443 ? NZ  ? A LYS 288 NZ  
90  1 Y 1 A LYS 448 ? CG  ? A LYS 293 CG  
91  1 Y 1 A LYS 448 ? CD  ? A LYS 293 CD  
92  1 Y 1 A LYS 448 ? CE  ? A LYS 293 CE  
93  1 Y 1 A LYS 448 ? NZ  ? A LYS 293 NZ  
94  1 Y 1 A GLN 455 ? CG  ? A GLN 300 CG  
95  1 Y 1 A GLN 455 ? CD  ? A GLN 300 CD  
96  1 Y 1 A GLN 455 ? OE1 ? A GLN 300 OE1 
97  1 Y 1 A GLN 455 ? NE2 ? A GLN 300 NE2 
98  1 Y 1 B PHE 165 ? CG  ? B PHE 10  CG  
99  1 Y 1 B PHE 165 ? CD1 ? B PHE 10  CD1 
100 1 Y 1 B PHE 165 ? CD2 ? B PHE 10  CD2 
101 1 Y 1 B PHE 165 ? CE1 ? B PHE 10  CE1 
102 1 Y 1 B PHE 165 ? CE2 ? B PHE 10  CE2 
103 1 Y 1 B PHE 165 ? CZ  ? B PHE 10  CZ  
104 1 Y 1 B HIS 166 ? CG  ? B HIS 11  CG  
105 1 Y 1 B HIS 166 ? ND1 ? B HIS 11  ND1 
106 1 Y 1 B HIS 166 ? CD2 ? B HIS 11  CD2 
107 1 Y 1 B HIS 166 ? CE1 ? B HIS 11  CE1 
108 1 Y 1 B HIS 166 ? NE2 ? B HIS 11  NE2 
109 1 Y 1 B PHE 168 ? CG  ? B PHE 13  CG  
110 1 Y 1 B PHE 168 ? CD1 ? B PHE 13  CD1 
111 1 Y 1 B PHE 168 ? CD2 ? B PHE 13  CD2 
112 1 Y 1 B PHE 168 ? CE1 ? B PHE 13  CE1 
113 1 Y 1 B PHE 168 ? CE2 ? B PHE 13  CE2 
114 1 Y 1 B PHE 168 ? CZ  ? B PHE 13  CZ  
115 1 Y 1 B PHE 170 ? CG  ? B PHE 15  CG  
116 1 Y 1 B PHE 170 ? CD1 ? B PHE 15  CD1 
117 1 Y 1 B PHE 170 ? CD2 ? B PHE 15  CD2 
118 1 Y 1 B PHE 170 ? CE1 ? B PHE 15  CE1 
119 1 Y 1 B PHE 170 ? CE2 ? B PHE 15  CE2 
120 1 Y 1 B PHE 170 ? CZ  ? B PHE 15  CZ  
121 1 Y 1 B LYS 174 ? CG  ? B LYS 19  CG  
122 1 Y 1 B LYS 174 ? CD  ? B LYS 19  CD  
123 1 Y 1 B LYS 174 ? CE  ? B LYS 19  CE  
124 1 Y 1 B LYS 174 ? NZ  ? B LYS 19  NZ  
125 1 Y 1 B ASN 178 ? CG  ? B ASN 23  CG  
126 1 Y 1 B ASN 178 ? OD1 ? B ASN 23  OD1 
127 1 Y 1 B ASN 178 ? ND2 ? B ASN 23  ND2 
128 1 Y 1 B ASN 179 ? CG  ? B ASN 24  CG  
129 1 Y 1 B ASN 179 ? OD1 ? B ASN 24  OD1 
130 1 Y 1 B ASN 179 ? ND2 ? B ASN 24  ND2 
131 1 Y 1 B PHE 180 ? CG  ? B PHE 25  CG  
132 1 Y 1 B PHE 180 ? CD1 ? B PHE 25  CD1 
133 1 Y 1 B PHE 180 ? CD2 ? B PHE 25  CD2 
134 1 Y 1 B PHE 180 ? CE1 ? B PHE 25  CE1 
135 1 Y 1 B PHE 180 ? CE2 ? B PHE 25  CE2 
136 1 Y 1 B PHE 180 ? CZ  ? B PHE 25  CZ  
137 1 Y 1 B ASP 181 ? CG  ? B ASP 26  CG  
138 1 Y 1 B ASP 181 ? OD1 ? B ASP 26  OD1 
139 1 Y 1 B ASP 181 ? OD2 ? B ASP 26  OD2 
140 1 Y 1 B GLU 182 ? CG  ? B GLU 27  CG  
141 1 Y 1 B GLU 182 ? CD  ? B GLU 27  CD  
142 1 Y 1 B GLU 182 ? OE1 ? B GLU 27  OE1 
143 1 Y 1 B GLU 182 ? OE2 ? B GLU 27  OE2 
144 1 Y 1 B ARG 183 ? CG  ? B ARG 28  CG  
145 1 Y 1 B ARG 183 ? CD  ? B ARG 28  CD  
146 1 Y 1 B ARG 183 ? NE  ? B ARG 28  NE  
147 1 Y 1 B ARG 183 ? CZ  ? B ARG 28  CZ  
148 1 Y 1 B ARG 183 ? NH1 ? B ARG 28  NH1 
149 1 Y 1 B ARG 183 ? NH2 ? B ARG 28  NH2 
150 1 Y 1 B LYS 191 ? CG  ? B LYS 36  CG  
151 1 Y 1 B LYS 191 ? CD  ? B LYS 36  CD  
152 1 Y 1 B LYS 191 ? CE  ? B LYS 36  CE  
153 1 Y 1 B LYS 191 ? NZ  ? B LYS 36  NZ  
154 1 Y 1 B GLU 194 ? CG  ? B GLU 39  CG  
155 1 Y 1 B GLU 194 ? CD  ? B GLU 39  CD  
156 1 Y 1 B GLU 194 ? OE1 ? B GLU 39  OE1 
157 1 Y 1 B GLU 194 ? OE2 ? B GLU 39  OE2 
158 1 Y 1 B LYS 202 ? CG  ? B LYS 47  CG  
159 1 Y 1 B LYS 202 ? CD  ? B LYS 47  CD  
160 1 Y 1 B LYS 202 ? CE  ? B LYS 47  CE  
161 1 Y 1 B LYS 202 ? NZ  ? B LYS 47  NZ  
162 1 Y 1 B TYR 204 ? CG  ? B TYR 49  CG  
163 1 Y 1 B TYR 204 ? CD1 ? B TYR 49  CD1 
164 1 Y 1 B TYR 204 ? CD2 ? B TYR 49  CD2 
165 1 Y 1 B TYR 204 ? CE1 ? B TYR 49  CE1 
166 1 Y 1 B TYR 204 ? CE2 ? B TYR 49  CE2 
167 1 Y 1 B TYR 204 ? CZ  ? B TYR 49  CZ  
168 1 Y 1 B TYR 204 ? OH  ? B TYR 49  OH  
169 1 Y 1 B LYS 213 ? CG  ? B LYS 58  CG  
170 1 Y 1 B LYS 213 ? CD  ? B LYS 58  CD  
171 1 Y 1 B LYS 213 ? CE  ? B LYS 58  CE  
172 1 Y 1 B LYS 213 ? NZ  ? B LYS 58  NZ  
173 1 Y 1 B LYS 214 ? CG  ? B LYS 59  CG  
174 1 Y 1 B LYS 214 ? CD  ? B LYS 59  CD  
175 1 Y 1 B LYS 214 ? CE  ? B LYS 59  CE  
176 1 Y 1 B LYS 214 ? NZ  ? B LYS 59  NZ  
177 1 Y 1 B GLU 224 ? CG  ? B GLU 69  CG  
178 1 Y 1 B GLU 224 ? CD  ? B GLU 69  CD  
179 1 Y 1 B GLU 224 ? OE1 ? B GLU 69  OE1 
180 1 Y 1 B GLU 224 ? OE2 ? B GLU 69  OE2 
181 1 Y 1 B GLU 225 ? CG  ? B GLU 70  CG  
182 1 Y 1 B GLU 225 ? CD  ? B GLU 70  CD  
183 1 Y 1 B GLU 225 ? OE1 ? B GLU 70  OE1 
184 1 Y 1 B GLU 225 ? OE2 ? B GLU 70  OE2 
185 1 Y 1 B LEU 226 ? CG  ? B LEU 71  CG  
186 1 Y 1 B LEU 226 ? CD1 ? B LEU 71  CD1 
187 1 Y 1 B LEU 226 ? CD2 ? B LEU 71  CD2 
188 1 Y 1 B LYS 227 ? CG  ? B LYS 72  CG  
189 1 Y 1 B LYS 227 ? CD  ? B LYS 72  CD  
190 1 Y 1 B LYS 227 ? CE  ? B LYS 72  CE  
191 1 Y 1 B LYS 227 ? NZ  ? B LYS 72  NZ  
192 1 Y 1 B GLN 228 ? CG  ? B GLN 73  CG  
193 1 Y 1 B GLN 228 ? CD  ? B GLN 73  CD  
194 1 Y 1 B GLN 228 ? OE1 ? B GLN 73  OE1 
195 1 Y 1 B GLN 228 ? NE2 ? B GLN 73  NE2 
196 1 Y 1 B GLN 229 ? CG  ? B GLN 74  CG  
197 1 Y 1 B GLN 229 ? CD  ? B GLN 74  CD  
198 1 Y 1 B GLN 229 ? OE1 ? B GLN 74  OE1 
199 1 Y 1 B GLN 229 ? NE2 ? B GLN 74  NE2 
200 1 Y 1 B PHE 230 ? CG  ? B PHE 75  CG  
201 1 Y 1 B PHE 230 ? CD1 ? B PHE 75  CD1 
202 1 Y 1 B PHE 230 ? CD2 ? B PHE 75  CD2 
203 1 Y 1 B PHE 230 ? CE1 ? B PHE 75  CE1 
204 1 Y 1 B PHE 230 ? CE2 ? B PHE 75  CE2 
205 1 Y 1 B PHE 230 ? CZ  ? B PHE 75  CZ  
206 1 Y 1 B ASP 231 ? CG  ? B ASP 76  CG  
207 1 Y 1 B ASP 231 ? OD1 ? B ASP 76  OD1 
208 1 Y 1 B ASP 231 ? OD2 ? B ASP 76  OD2 
209 1 Y 1 B GLN 232 ? CG  ? B GLN 77  CG  
210 1 Y 1 B GLN 232 ? CD  ? B GLN 77  CD  
211 1 Y 1 B GLN 232 ? OE1 ? B GLN 77  OE1 
212 1 Y 1 B GLN 232 ? NE2 ? B GLN 77  NE2 
213 1 Y 1 B GLU 233 ? CG  ? B GLU 78  CG  
214 1 Y 1 B GLU 233 ? CD  ? B GLU 78  CD  
215 1 Y 1 B GLU 233 ? OE1 ? B GLU 78  OE1 
216 1 Y 1 B GLU 233 ? OE2 ? B GLU 78  OE2 
217 1 Y 1 B LYS 235 ? CG  ? B LYS 80  CG  
218 1 Y 1 B LYS 235 ? CD  ? B LYS 80  CD  
219 1 Y 1 B LYS 235 ? CE  ? B LYS 80  CE  
220 1 Y 1 B LYS 235 ? NZ  ? B LYS 80  NZ  
221 1 Y 1 B VAL 236 ? CG1 ? B VAL 81  CG1 
222 1 Y 1 B VAL 236 ? CG2 ? B VAL 81  CG2 
223 1 Y 1 B MET 237 ? CG  ? B MET 82  CG  
224 1 Y 1 B MET 237 ? SD  ? B MET 82  SD  
225 1 Y 1 B MET 237 ? CE  ? B MET 82  CE  
226 1 Y 1 B LYS 239 ? CG  ? B LYS 84  CG  
227 1 Y 1 B LYS 239 ? CD  ? B LYS 84  CD  
228 1 Y 1 B LYS 239 ? CE  ? B LYS 84  CE  
229 1 Y 1 B LYS 239 ? NZ  ? B LYS 84  NZ  
230 1 Y 1 B GLN 241 ? CG  ? B GLN 86  CG  
231 1 Y 1 B GLN 241 ? CD  ? B GLN 86  CD  
232 1 Y 1 B GLN 241 ? OE1 ? B GLN 86  OE1 
233 1 Y 1 B GLN 241 ? NE2 ? B GLN 86  NE2 
234 1 Y 1 B GLU 247 ? CG  ? B GLU 92  CG  
235 1 Y 1 B GLU 247 ? CD  ? B GLU 92  CD  
236 1 Y 1 B GLU 247 ? OE1 ? B GLU 92  OE1 
237 1 Y 1 B GLU 247 ? OE2 ? B GLU 92  OE2 
238 1 Y 1 B ASP 257 ? CG  ? B ASP 102 CG  
239 1 Y 1 B ASP 257 ? OD1 ? B ASP 102 OD1 
240 1 Y 1 B ASP 257 ? OD2 ? B ASP 102 OD2 
241 1 Y 1 B VAL 261 ? CG1 ? B VAL 106 CG1 
242 1 Y 1 B VAL 261 ? CG2 ? B VAL 106 CG2 
243 1 Y 1 B ARG 310 ? CG  ? B ARG 155 CG  
244 1 Y 1 B ARG 310 ? CD  ? B ARG 155 CD  
245 1 Y 1 B ARG 310 ? NE  ? B ARG 155 NE  
246 1 Y 1 B ARG 310 ? CZ  ? B ARG 155 CZ  
247 1 Y 1 B ARG 310 ? NH1 ? B ARG 155 NH1 
248 1 Y 1 B ARG 310 ? NH2 ? B ARG 155 NH2 
249 1 Y 1 B LYS 326 ? CG  ? B LYS 171 CG  
250 1 Y 1 B LYS 326 ? CD  ? B LYS 171 CD  
251 1 Y 1 B LYS 326 ? CE  ? B LYS 171 CE  
252 1 Y 1 B LYS 326 ? NZ  ? B LYS 171 NZ  
253 1 Y 1 B ARG 347 ? CZ  ? B ARG 192 CZ  
254 1 Y 1 B ARG 347 ? NH1 ? B ARG 192 NH1 
255 1 Y 1 B ARG 347 ? NH2 ? B ARG 192 NH2 
256 1 Y 1 B ILE 364 ? CG1 ? B ILE 209 CG1 
257 1 Y 1 B ILE 364 ? CG2 ? B ILE 209 CG2 
258 1 Y 1 B ILE 364 ? CD1 ? B ILE 209 CD1 
259 1 Y 1 B LYS 367 ? CG  ? B LYS 212 CG  
260 1 Y 1 B LYS 367 ? CD  ? B LYS 212 CD  
261 1 Y 1 B LYS 367 ? CE  ? B LYS 212 CE  
262 1 Y 1 B LYS 367 ? NZ  ? B LYS 212 NZ  
263 1 Y 1 B GLU 389 ? CG  ? B GLU 234 CG  
264 1 Y 1 B GLU 389 ? CD  ? B GLU 234 CD  
265 1 Y 1 B GLU 389 ? OE1 ? B GLU 234 OE1 
266 1 Y 1 B GLU 389 ? OE2 ? B GLU 234 OE2 
267 1 Y 1 B GLU 392 ? CG  ? B GLU 237 CG  
268 1 Y 1 B GLU 392 ? CD  ? B GLU 237 CD  
269 1 Y 1 B GLU 392 ? OE1 ? B GLU 237 OE1 
270 1 Y 1 B GLU 392 ? OE2 ? B GLU 237 OE2 
271 1 Y 1 B LYS 400 ? CG  ? B LYS 245 CG  
272 1 Y 1 B LYS 400 ? CD  ? B LYS 245 CD  
273 1 Y 1 B LYS 400 ? CE  ? B LYS 245 CE  
274 1 Y 1 B LYS 400 ? NZ  ? B LYS 245 NZ  
275 1 Y 1 B GLU 401 ? CG  ? B GLU 246 CG  
276 1 Y 1 B GLU 401 ? CD  ? B GLU 246 CD  
277 1 Y 1 B GLU 401 ? OE1 ? B GLU 246 OE1 
278 1 Y 1 B GLU 401 ? OE2 ? B GLU 246 OE2 
279 1 Y 1 B GLU 402 ? CG  ? B GLU 247 CG  
280 1 Y 1 B GLU 402 ? CD  ? B GLU 247 CD  
281 1 Y 1 B GLU 402 ? OE1 ? B GLU 247 OE1 
282 1 Y 1 B GLU 402 ? OE2 ? B GLU 247 OE2 
283 1 Y 1 B GLU 404 ? CG  ? B GLU 249 CG  
284 1 Y 1 B GLU 404 ? CD  ? B GLU 249 CD  
285 1 Y 1 B GLU 404 ? OE1 ? B GLU 249 OE1 
286 1 Y 1 B GLU 404 ? OE2 ? B GLU 249 OE2 
287 1 Y 1 B GLU 407 ? CG  ? B GLU 252 CG  
288 1 Y 1 B GLU 407 ? CD  ? B GLU 252 CD  
289 1 Y 1 B GLU 407 ? OE1 ? B GLU 252 OE1 
290 1 Y 1 B GLU 407 ? OE2 ? B GLU 252 OE2 
291 1 Y 1 B LYS 408 ? CG  ? B LYS 253 CG  
292 1 Y 1 B LYS 408 ? CD  ? B LYS 253 CD  
293 1 Y 1 B LYS 408 ? CE  ? B LYS 253 CE  
294 1 Y 1 B LYS 408 ? NZ  ? B LYS 253 NZ  
295 1 Y 1 B GLU 411 ? CG  ? B GLU 256 CG  
296 1 Y 1 B GLU 411 ? CD  ? B GLU 256 CD  
297 1 Y 1 B GLU 411 ? OE1 ? B GLU 256 OE1 
298 1 Y 1 B GLU 411 ? OE2 ? B GLU 256 OE2 
299 1 Y 1 B LYS 443 ? CG  ? B LYS 288 CG  
300 1 Y 1 B LYS 443 ? CD  ? B LYS 288 CD  
301 1 Y 1 B LYS 443 ? CE  ? B LYS 288 CE  
302 1 Y 1 B LYS 443 ? NZ  ? B LYS 288 NZ  
303 1 Y 1 B LYS 448 ? CG  ? B LYS 293 CG  
304 1 Y 1 B LYS 448 ? CD  ? B LYS 293 CD  
305 1 Y 1 B LYS 448 ? CE  ? B LYS 293 CE  
306 1 Y 1 B LYS 448 ? NZ  ? B LYS 293 NZ  
307 1 Y 1 B LYS 449 ? CD  ? B LYS 294 CD  
308 1 Y 1 B LYS 449 ? CE  ? B LYS 294 CE  
309 1 Y 1 B LYS 449 ? NZ  ? B LYS 294 NZ  
310 1 Y 1 B GLN 452 ? CG  ? B GLN 297 CG  
311 1 Y 1 B GLN 452 ? CD  ? B GLN 297 CD  
312 1 Y 1 B GLN 452 ? OE1 ? B GLN 297 OE1 
313 1 Y 1 B GLN 452 ? NE2 ? B GLN 297 NE2 
314 1 Y 1 B GLN 455 ? CG  ? B GLN 300 CG  
315 1 Y 1 B GLN 455 ? CD  ? B GLN 300 CD  
316 1 Y 1 B GLN 455 ? OE1 ? B GLN 300 OE1 
317 1 Y 1 B GLN 455 ? NE2 ? B GLN 300 NE2 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000  ? ? ? .      1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .      2 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? 2.11.1 3 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8SCV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     86.289 
_cell.length_a_esd                 ? 
_cell.length_b                     103.754 
_cell.length_b_esd                 ? 
_cell.length_c                     139.753 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8SCV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   8SCV 
_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             2.28 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.16 
_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, SITTING 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    '2.6 to 2.9 M ammonium sulphate in 25 mM HEPES pH 6.4 to 7.5 at 293K' 
_exptl_crystal_grow.pdbx_pH_range   6.4-7.5 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX-300' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-03-03 
_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   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 22-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8SCV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.69 
_reflns.d_resolution_low                               50.00 
_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                                     17703 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.7 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.086 
_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                                    2.69 
_reflns_shell.d_res_low                                     2.79 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1736 
_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                               6.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.632 
_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]                            -2.38160 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            -18.94720 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            21.32880 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               69.88 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.906 
_refine.correlation_coeff_Fo_to_Fc_free          0.903 
_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                                 8SCV 
_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                            2.69 
_refine.ls_d_res_low                             48.11 
_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                     17700 
_refine.ls_number_reflns_R_free                  899 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.5 
_refine.ls_percent_reflns_R_free                 5.080 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.222 
_refine.ls_R_factor_R_free                       0.261 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.220 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.335 
_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                            ? 
_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_analyze.entry_id                        8SCV 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.380 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.69 
_refine_hist.d_res_low                        48.11 
_refine_hist.number_atoms_solvent             64 
_refine_hist.number_atoms_total               4205 
_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        4073 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_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' ? 0.010 ? 4214 ? t_bond_d                  2.000  HARMONIC     
'X-RAY DIFFRACTION' ? 1.23  ? 5739 ? t_angle_deg               2.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1371 ? t_dihedral_angle_d        2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 94   ? t_trig_c_planes           2.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 657  ? t_gen_planes              5.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4214 ? t_it                      20.000 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?      ?            
'X-RAY DIFFRACTION' ? 2.56  ? ?    ? t_omega_torsion           ?      ?            
'X-RAY DIFFRACTION' ? 19.87 ? ?    ? t_other_torsion           ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 590  ? t_chiral_improper_torsion 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 4918 ? t_ideal_dist_contact      4.000  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.69 
_refine_ls_shell.d_res_low                        2.85 
_refine_ls_shell.number_reflns_all                2761 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             141 
_refine_ls_shell.number_reflns_R_work             2620 
_refine_ls_shell.percent_reflns_obs               99.47 
_refine_ls_shell.percent_reflns_R_free            5.11 
_refine_ls_shell.R_factor_all                     0.2530 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2497 
_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.pdbx_total_number_of_bins_used   9 
_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                  0.3140 
# 
_struct.entry_id                     8SCV 
_struct.title                        
;Crystal structure of IRAK4-HSA complexed with BMS-986126; 6-((5-CYANO-2-PYRIMIDINYL)AMINO)-N-((2R)-2-FLUORO-3-HYDROXHYLBUTYL)-4-(ISOPROPYLAMINO)NICOTINAMIDE
;
_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        8SCV 
_struct_keywords.text            'kinase, IRAK4, ligand, TRANSFERASE-TRANSFERASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'TRANSFERASE/TRANSFERASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
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 IRAK4_HUMAN Q9NWZ3 Q9NWZ3-2 1 
;VSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAK
CQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILL
DEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDI
KEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
36 
2 UNP IRAK4_HUMAN Q9NWZ3 Q9NWZ3-2 2 
;VSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAK
CQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILL
DEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDI
KEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
;
36 
# 
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 8SCV A 5 ? 305 ? Q9NWZ3 36 ? 336 ? 160 460 
2 2 8SCV B 5 ? 305 ? Q9NWZ3 36 ? 336 ? 160 460 
# 
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 8SCV GLY A 1 ? UNP Q9NWZ3 ? ? 'expression tag' 156 1 
1 8SCV ALA A 2 ? UNP Q9NWZ3 ? ? 'expression tag' 157 2 
1 8SCV MET A 3 ? UNP Q9NWZ3 ? ? 'expression tag' 158 3 
1 8SCV GLY A 4 ? UNP Q9NWZ3 ? ? 'expression tag' 159 4 
2 8SCV GLY B 1 ? UNP Q9NWZ3 ? ? 'expression tag' 156 5 
2 8SCV ALA B 2 ? UNP Q9NWZ3 ? ? 'expression tag' 157 6 
2 8SCV MET B 3 ? UNP Q9NWZ3 ? ? 'expression tag' 158 7 
2 8SCV GLY B 4 ? UNP Q9NWZ3 ? ? 'expression tag' 159 8 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 14  ? THR A 22  ? SER A 169 THR A 177 1 ? 9  
HELX_P HELX_P2  AA2 PRO A 29  ? GLY A 33  ? PRO A 184 GLY A 188 5 ? 5  
HELX_P HELX_P3  AA3 GLU A 70  ? CYS A 85  ? GLU A 225 CYS A 240 1 ? 16 
HELX_P HELX_P4  AA4 SER A 114 ? SER A 120 ? SER A 269 SER A 275 1 ? 7  
HELX_P HELX_P5  AA5 CYS A 121 ? THR A 125 ? CYS A 276 THR A 280 5 ? 5  
HELX_P HELX_P6  AA6 SEP A 129 ? ASN A 150 ? SEP A 284 ASN A 305 1 ? 22 
HELX_P HELX_P7  AA7 LYS A 158 ? ALA A 160 ? LYS A 313 ALA A 315 5 ? 3  
HELX_P HELX_P8  AA8 PRO A 202 ? ARG A 206 ? PRO A 357 ARG A 361 5 ? 5  
HELX_P HELX_P9  AA9 THR A 210 ? GLY A 228 ? THR A 365 GLY A 383 1 ? 19 
HELX_P HELX_P10 AB1 LEU A 240 ? ASP A 250 ? LEU A 395 ASP A 405 1 ? 11 
HELX_P HELX_P11 AB2 ASP A 267 ? LEU A 282 ? ASP A 422 LEU A 437 1 ? 16 
HELX_P HELX_P12 AB3 LYS A 285 ? ARG A 289 ? LYS A 440 ARG A 444 5 ? 5  
HELX_P HELX_P13 AB4 ASP A 291 ? THR A 303 ? ASP A 446 THR A 458 1 ? 13 
HELX_P HELX_P14 AB5 TYR B 16  ? THR B 22  ? TYR B 171 THR B 177 1 ? 7  
HELX_P HELX_P15 AB6 GLU B 70  ? CYS B 85  ? GLU B 225 CYS B 240 1 ? 16 
HELX_P HELX_P16 AB7 SER B 114 ? SER B 120 ? SER B 269 SER B 275 1 ? 7  
HELX_P HELX_P17 AB8 CYS B 121 ? THR B 125 ? CYS B 276 THR B 280 5 ? 5  
HELX_P HELX_P18 AB9 SER B 129 ? ASN B 150 ? SER B 284 ASN B 305 1 ? 22 
HELX_P HELX_P19 AC1 LYS B 158 ? ALA B 160 ? LYS B 313 ALA B 315 5 ? 3  
HELX_P HELX_P20 AC2 ALA B 201 ? ARG B 206 ? ALA B 356 ARG B 361 1 ? 6  
HELX_P HELX_P21 AC3 THR B 210 ? GLY B 228 ? THR B 365 GLY B 383 1 ? 19 
HELX_P HELX_P22 AC4 LEU B 240 ? ASP B 250 ? LEU B 395 ASP B 405 1 ? 11 
HELX_P HELX_P23 AC5 ASP B 267 ? LEU B 282 ? ASP B 422 LEU B 437 1 ? 16 
HELX_P HELX_P24 AC6 LYS B 285 ? ARG B 289 ? LYS B 440 ARG B 444 5 ? 5  
HELX_P HELX_P25 AC7 ASP B 291 ? THR B 303 ? ASP B 446 THR B 458 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A LEU 128 C ? ? ? 1_555 A SEP 129 N ? ? A LEU 283 A SEP 284 1_555 ? ? ? ? ? ? ? 1.353 ? ? 
covale2 covale both ? A SEP 129 C ? ? ? 1_555 A TRP 130 N ? ? A SEP 284 A TRP 285 1_555 ? ? ? ? ? ? ? 1.367 ? ? 
covale3 covale both ? A MET 189 C ? ? ? 1_555 A TPO 190 N ? ? A MET 344 A TPO 345 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale4 covale both ? A TPO 190 C ? ? ? 1_555 A SEP 191 N ? ? A TPO 345 A SEP 346 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale5 covale both ? A SEP 191 C ? ? ? 1_555 A ARG 192 N ? ? A SEP 346 A ARG 347 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale6 covale both ? B MET 189 C ? ? ? 1_555 B TPO 190 N ? ? B MET 344 B TPO 345 1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale7 covale both ? B TPO 190 C ? ? ? 1_555 B SEP 191 N ? ? B TPO 345 B SEP 346 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale8 covale both ? B SEP 191 C ? ? ? 1_555 B ARG 192 N ? ? B SEP 346 B ARG 347 1_555 ? ? ? ? ? ? ? 1.343 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 SEP A 129 ? . . . . SEP A 284 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
2 TPO A 190 ? . . . . TPO A 345 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
3 SEP A 191 ? . . . . SEP A 346 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
4 TPO B 190 ? . . . . TPO B 345 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
5 SEP B 191 ? . . . . SEP B 346 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 69  A . ? GLU 224 A GLU 70  A ? GLU 225 A 1 10.75 
2 GLU 237 A . ? GLU 392 A PRO 238 A ? PRO 393 A 1 -0.40 
3 GLU 237 B . ? GLU 392 B PRO 238 B ? PRO 393 B 1 1.31  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 11  ? SER A 12  ? HIS A 166 SER A 167 
AA1 2 LEU A 93  ? SER A 97  ? LEU A 248 SER A 252 
AA1 3 CYS A 104 ? VAL A 108 ? CYS A 259 VAL A 263 
AA1 4 THR A 53  ? LEU A 60  ? THR A 208 LEU A 215 
AA1 5 GLY A 43  ? VAL A 50  ? GLY A 198 VAL A 205 
AA1 6 LYS A 36  ? GLU A 39  ? LYS A 191 GLU A 194 
AA2 1 HIS A 152 ? ILE A 153 ? HIS A 307 ILE A 308 
AA2 2 ARG A 179 ? ALA A 180 ? ARG A 334 ALA A 335 
AA3 1 ILE A 162 ? LEU A 164 ? ILE A 317 LEU A 319 
AA3 2 ALA A 170 ? ILE A 172 ? ALA A 325 ILE A 327 
AA4 1 VAL A 188 ? MET A 189 ? VAL A 343 MET A 344 
AA4 2 GLU A 208 ? ILE A 209 ? GLU A 363 ILE A 364 
AA5 1 LYS B 36  ? GLY B 38  ? LYS B 191 GLY B 193 
AA5 2 VAL B 44  ? GLY B 48  ? VAL B 199 GLY B 203 
AA5 3 VAL B 55  ? LYS B 59  ? VAL B 210 LYS B 214 
AA5 4 CYS B 104 ? VAL B 108 ? CYS B 259 VAL B 263 
AA6 1 ILE B 162 ? LEU B 164 ? ILE B 317 LEU B 319 
AA6 2 ALA B 170 ? ILE B 172 ? ALA B 325 ILE B 327 
# 
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 N HIS A 11  ? N HIS A 166 O PHE A 96  ? O PHE A 251 
AA1 2 3 N LEU A 94  ? N LEU A 249 O VAL A 106 ? O VAL A 261 
AA1 3 4 O TYR A 107 ? O TYR A 262 N ALA A 56  ? N ALA A 211 
AA1 4 5 O VAL A 57  ? O VAL A 212 N TYR A 46  ? N TYR A 201 
AA1 5 6 O VAL A 45  ? O VAL A 200 N GLY A 38  ? N GLY A 193 
AA2 1 2 N ILE A 153 ? N ILE A 308 O ARG A 179 ? O ARG A 334 
AA3 1 2 N LEU A 163 ? N LEU A 318 O LYS A 171 ? O LYS A 326 
AA4 1 2 N VAL A 188 ? N VAL A 343 O ILE A 209 ? O ILE A 364 
AA5 1 2 N GLY B 38  ? N GLY B 193 O VAL B 45  ? O VAL B 200 
AA5 2 3 N GLY B 48  ? N GLY B 203 O VAL B 55  ? O VAL B 210 
AA5 3 4 N LYS B 58  ? N LYS B 213 O LEU B 105 ? O LEU B 260 
AA6 1 2 N LEU B 163 ? N LEU B 318 O LYS B 171 ? O LYS B 326 
# 
_pdbx_entry_details.entry_id                   8SCV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 181 ? ? -66.89  99.38   
2  1 ASN A 206 ? ? 35.25   69.79   
3  1 ASN A 207 ? ? 65.74   -0.21   
4  1 THR A 223 ? ? -95.05  -65.74  
5  1 GLU A 224 ? ? 146.73  57.31   
6  1 GLU A 225 ? ? 57.82   -54.97  
7  1 ASP A 254 ? ? 4.12    95.60   
8  1 ARG A 310 ? ? 74.49   -10.35  
9  1 ASP A 329 ? ? 59.49   87.11   
10 1 THR A 342 ? ? -161.19 89.71   
11 1 TPO A 345 ? ? -120.23 -78.70  
12 1 SEP A 346 ? ? 93.07   143.83  
13 1 ARG A 347 ? ? 56.12   102.05  
14 1 HIS A 390 ? ? -97.19  35.26   
15 1 GLU A 406 ? ? 45.95   6.33    
16 1 ASP B 181 ? ? -65.83  90.92   
17 1 GLU B 182 ? ? -57.09  -4.63   
18 1 ASN B 190 ? ? -132.17 -32.08  
19 1 GLU B 194 ? ? -161.07 -158.12 
20 1 ARG B 310 ? ? 73.66   -10.79  
21 1 ASP B 329 ? ? 59.41   86.09   
22 1 HIS B 390 ? ? -97.53  35.71   
23 1 GLU B 406 ? ? 45.56   6.93    
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   TPO 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    345 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SEP 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    346 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.95 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A SEP 129 A SEP 284 ? SER 'modified residue' 
2 A TPO 190 A TPO 345 ? THR 'modified residue' 
3 A SEP 191 A SEP 346 ? SER 'modified residue' 
4 B TPO 190 B TPO 345 ? THR 'modified residue' 
5 B SEP 191 B SEP 346 ? SER 'modified residue' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     602 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   G 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 GLY 156 ? A GLY 1   
2  1 Y 1 A ALA 157 ? A ALA 2   
3  1 Y 1 A MET 158 ? A MET 3   
4  1 Y 1 A GLY 159 ? A GLY 4   
5  1 Y 1 A VAL 160 ? A VAL 5   
6  1 Y 1 A SER 161 ? A SER 6   
7  1 Y 1 A ASP 162 ? A ASP 7   
8  1 Y 1 A VAL 219 ? A VAL 64  
9  1 Y 1 A ASP 220 ? A ASP 65  
10 1 Y 1 A GLU 337 ? A GLU 182 
11 1 Y 1 A LYS 338 ? A LYS 183 
12 1 Y 1 A PHE 339 ? A PHE 184 
13 1 Y 1 A ALA 340 ? A ALA 185 
14 1 Y 1 A ALA 459 ? A ALA 304 
15 1 Y 1 A SER 460 ? A SER 305 
16 1 Y 1 B GLY 156 ? B GLY 1   
17 1 Y 1 B ALA 157 ? B ALA 2   
18 1 Y 1 B MET 158 ? B MET 3   
19 1 Y 1 B GLY 159 ? B GLY 4   
20 1 Y 1 B VAL 160 ? B VAL 5   
21 1 Y 1 B SER 161 ? B SER 6   
22 1 Y 1 B ASP 162 ? B ASP 7   
23 1 Y 1 B THR 163 ? B THR 8   
24 1 Y 1 B ARG 164 ? B ARG 9   
25 1 Y 1 B SER 186 ? B SER 31  
26 1 Y 1 B VAL 187 ? B VAL 32  
27 1 Y 1 B GLY 188 ? B GLY 33  
28 1 Y 1 B ASN 206 ? B ASN 51  
29 1 Y 1 B ASN 207 ? B ASN 52  
30 1 Y 1 B ALA 216 ? B ALA 61  
31 1 Y 1 B ALA 217 ? B ALA 62  
32 1 Y 1 B MET 218 ? B MET 63  
33 1 Y 1 B VAL 219 ? B VAL 64  
34 1 Y 1 B ASP 220 ? B ASP 65  
35 1 Y 1 B ILE 221 ? B ILE 66  
36 1 Y 1 B THR 222 ? B THR 67  
37 1 Y 1 B THR 223 ? B THR 68  
38 1 Y 1 B LEU 249 ? B LEU 94  
39 1 Y 1 B GLY 250 ? B GLY 95  
40 1 Y 1 B PHE 251 ? B PHE 96  
41 1 Y 1 B SER 252 ? B SER 97  
42 1 Y 1 B SER 253 ? B SER 98  
43 1 Y 1 B ASP 254 ? B ASP 99  
44 1 Y 1 B GLY 255 ? B GLY 100 
45 1 Y 1 B ASP 256 ? B ASP 101 
46 1 Y 1 B ALA 333 ? B ALA 178 
47 1 Y 1 B ARG 334 ? B ARG 179 
48 1 Y 1 B ALA 335 ? B ALA 180 
49 1 Y 1 B SER 336 ? B SER 181 
50 1 Y 1 B GLU 337 ? B GLU 182 
51 1 Y 1 B LYS 338 ? B LYS 183 
52 1 Y 1 B PHE 339 ? B PHE 184 
53 1 Y 1 B ALA 340 ? B ALA 185 
54 1 Y 1 B GLN 341 ? B GLN 186 
55 1 Y 1 B GLY 350 ? B GLY 195 
56 1 Y 1 B THR 351 ? B THR 196 
57 1 Y 1 B SER 460 ? B SER 305 
# 
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  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SEP N    N N N 290 
SEP CA   C N S 291 
SEP CB   C N N 292 
SEP OG   O N N 293 
SEP C    C N N 294 
SEP O    O N N 295 
SEP OXT  O N N 296 
SEP P    P N N 297 
SEP O1P  O N N 298 
SEP O2P  O N N 299 
SEP O3P  O N N 300 
SEP H    H N N 301 
SEP H2   H N N 302 
SEP HA   H N N 303 
SEP HB2  H N N 304 
SEP HB3  H N N 305 
SEP HXT  H N N 306 
SEP HOP2 H N N 307 
SEP HOP3 H N N 308 
SER N    N N N 309 
SER CA   C N S 310 
SER C    C N N 311 
SER O    O N N 312 
SER CB   C N N 313 
SER OG   O N N 314 
SER OXT  O N N 315 
SER H    H N N 316 
SER H2   H N N 317 
SER HA   H N N 318 
SER HB2  H N N 319 
SER HB3  H N N 320 
SER HG   H N N 321 
SER HXT  H N N 322 
SO4 S    S N N 323 
SO4 O1   O N N 324 
SO4 O2   O N N 325 
SO4 O3   O N N 326 
SO4 O4   O N N 327 
THR N    N N N 328 
THR CA   C N S 329 
THR C    C N N 330 
THR O    O N N 331 
THR CB   C N R 332 
THR OG1  O N N 333 
THR CG2  C N N 334 
THR OXT  O N N 335 
THR H    H N N 336 
THR H2   H N N 337 
THR HA   H N N 338 
THR HB   H N N 339 
THR HG1  H N N 340 
THR HG21 H N N 341 
THR HG22 H N N 342 
THR HG23 H N N 343 
THR HXT  H N N 344 
TPO N    N N N 345 
TPO CA   C N S 346 
TPO CB   C N R 347 
TPO CG2  C N N 348 
TPO OG1  O N N 349 
TPO P    P N N 350 
TPO O1P  O N N 351 
TPO O2P  O N N 352 
TPO O3P  O N N 353 
TPO C    C N N 354 
TPO O    O N N 355 
TPO OXT  O N N 356 
TPO H    H N N 357 
TPO H2   H N N 358 
TPO HA   H N N 359 
TPO HB   H N N 360 
TPO HG21 H N N 361 
TPO HG22 H N N 362 
TPO HG23 H N N 363 
TPO HOP2 H N N 364 
TPO HOP3 H N N 365 
TPO HXT  H N N 366 
TRP N    N N N 367 
TRP CA   C N S 368 
TRP C    C N N 369 
TRP O    O N N 370 
TRP CB   C N N 371 
TRP CG   C Y N 372 
TRP CD1  C Y N 373 
TRP CD2  C Y N 374 
TRP NE1  N Y N 375 
TRP CE2  C Y N 376 
TRP CE3  C Y N 377 
TRP CZ2  C Y N 378 
TRP CZ3  C Y N 379 
TRP CH2  C Y N 380 
TRP OXT  O N N 381 
TRP H    H N N 382 
TRP H2   H N N 383 
TRP HA   H N N 384 
TRP HB2  H N N 385 
TRP HB3  H N N 386 
TRP HD1  H N N 387 
TRP HE1  H N N 388 
TRP HE3  H N N 389 
TRP HZ2  H N N 390 
TRP HZ3  H N N 391 
TRP HH2  H N N 392 
TRP HXT  H N N 393 
TYR N    N N N 394 
TYR CA   C N S 395 
TYR C    C N N 396 
TYR O    O N N 397 
TYR CB   C N N 398 
TYR CG   C Y N 399 
TYR CD1  C Y N 400 
TYR CD2  C Y N 401 
TYR CE1  C Y N 402 
TYR CE2  C Y N 403 
TYR CZ   C Y N 404 
TYR OH   O N N 405 
TYR OXT  O N N 406 
TYR H    H N N 407 
TYR H2   H N N 408 
TYR HA   H N N 409 
TYR HB2  H N N 410 
TYR HB3  H N N 411 
TYR HD1  H N N 412 
TYR HD2  H N N 413 
TYR HE1  H N N 414 
TYR HE2  H N N 415 
TYR HH   H N N 416 
TYR HXT  H N N 417 
VAL N    N N N 418 
VAL CA   C N S 419 
VAL C    C N N 420 
VAL O    O N N 421 
VAL CB   C N N 422 
VAL CG1  C N N 423 
VAL CG2  C N N 424 
VAL OXT  O N N 425 
VAL H    H N N 426 
VAL H2   H N N 427 
VAL HA   H N N 428 
VAL HB   H N N 429 
VAL HG11 H N N 430 
VAL HG12 H N N 431 
VAL HG13 H N N 432 
VAL HG21 H N N 433 
VAL HG22 H N N 434 
VAL HG23 H N N 435 
VAL HXT  H N N 436 
ZVG C13  C N N 437 
ZVG C18  C N N 438 
ZVG C17  C Y N 439 
ZVG C16  C Y N 440 
ZVG C15  C Y N 441 
ZVG C11  C N N 442 
ZVG C12  C N N 443 
ZVG N6   N N N 444 
ZVG N4   N Y N 445 
ZVG N5   N Y N 446 
ZVG C14  C Y N 447 
ZVG N3   N N N 448 
ZVG C8   C Y N 449 
ZVG N1   N Y N 450 
ZVG C7   C Y N 451 
ZVG C9   C Y N 452 
ZVG C10  C Y N 453 
ZVG N2   N N N 454 
ZVG C6   C Y N 455 
ZVG C5   C N N 456 
ZVG O1   O N N 457 
ZVG N    N N N 458 
ZVG C4   C N N 459 
ZVG C3   C N R 460 
ZVG F    F N N 461 
ZVG C    C N N 462 
ZVG C2   C N N 463 
ZVG C1   C N N 464 
ZVG O    O N N 465 
ZVG H1   H N N 466 
ZVG H2   H N N 467 
ZVG H3   H N N 468 
ZVG H4   H N N 469 
ZVG H5   H N N 470 
ZVG H6   H N N 471 
ZVG H7   H N N 472 
ZVG H8   H N N 473 
ZVG H9   H N N 474 
ZVG H10  H N N 475 
ZVG H11  H N N 476 
ZVG H12  H N N 477 
ZVG H13  H N N 478 
ZVG H14  H N N 479 
ZVG H15  H N N 480 
ZVG H16  H N N 481 
ZVG H17  H N N 482 
ZVG H18  H N N 483 
ZVG H19  H N N 484 
ZVG H20  H N N 485 
ZVG H21  H N N 486 
ZVG H22  H N N 487 
ZVG H23  H N N 488 
ZVG H24  H N N 489 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SEP N   CA   sing N N 277 
SEP N   H    sing N N 278 
SEP N   H2   sing N N 279 
SEP CA  CB   sing N N 280 
SEP CA  C    sing N N 281 
SEP CA  HA   sing N N 282 
SEP CB  OG   sing N N 283 
SEP CB  HB2  sing N N 284 
SEP CB  HB3  sing N N 285 
SEP OG  P    sing N N 286 
SEP C   O    doub N N 287 
SEP C   OXT  sing N N 288 
SEP OXT HXT  sing N N 289 
SEP P   O1P  doub N N 290 
SEP P   O2P  sing N N 291 
SEP P   O3P  sing N N 292 
SEP O2P HOP2 sing N N 293 
SEP O3P HOP3 sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
SO4 S   O1   doub N N 308 
SO4 S   O2   doub N N 309 
SO4 S   O3   sing N N 310 
SO4 S   O4   sing N N 311 
THR N   CA   sing N N 312 
THR N   H    sing N N 313 
THR N   H2   sing N N 314 
THR CA  C    sing N N 315 
THR CA  CB   sing N N 316 
THR CA  HA   sing N N 317 
THR C   O    doub N N 318 
THR C   OXT  sing N N 319 
THR CB  OG1  sing N N 320 
THR CB  CG2  sing N N 321 
THR CB  HB   sing N N 322 
THR OG1 HG1  sing N N 323 
THR CG2 HG21 sing N N 324 
THR CG2 HG22 sing N N 325 
THR CG2 HG23 sing N N 326 
THR OXT HXT  sing N N 327 
TPO N   CA   sing N N 328 
TPO N   H    sing N N 329 
TPO N   H2   sing N N 330 
TPO CA  CB   sing N N 331 
TPO CA  C    sing N N 332 
TPO CA  HA   sing N N 333 
TPO CB  CG2  sing N N 334 
TPO CB  OG1  sing N N 335 
TPO CB  HB   sing N N 336 
TPO CG2 HG21 sing N N 337 
TPO CG2 HG22 sing N N 338 
TPO CG2 HG23 sing N N 339 
TPO OG1 P    sing N N 340 
TPO P   O1P  doub N N 341 
TPO P   O2P  sing N N 342 
TPO P   O3P  sing N N 343 
TPO O2P HOP2 sing N N 344 
TPO O3P HOP3 sing N N 345 
TPO C   O    doub N N 346 
TPO C   OXT  sing N N 347 
TPO OXT HXT  sing N N 348 
TRP N   CA   sing N N 349 
TRP N   H    sing N N 350 
TRP N   H2   sing N N 351 
TRP CA  C    sing N N 352 
TRP CA  CB   sing N N 353 
TRP CA  HA   sing N N 354 
TRP C   O    doub N N 355 
TRP C   OXT  sing N N 356 
TRP CB  CG   sing N N 357 
TRP CB  HB2  sing N N 358 
TRP CB  HB3  sing N N 359 
TRP CG  CD1  doub Y N 360 
TRP CG  CD2  sing Y N 361 
TRP CD1 NE1  sing Y N 362 
TRP CD1 HD1  sing N N 363 
TRP CD2 CE2  doub Y N 364 
TRP CD2 CE3  sing Y N 365 
TRP NE1 CE2  sing Y N 366 
TRP NE1 HE1  sing N N 367 
TRP CE2 CZ2  sing Y N 368 
TRP CE3 CZ3  doub Y N 369 
TRP CE3 HE3  sing N N 370 
TRP CZ2 CH2  doub Y N 371 
TRP CZ2 HZ2  sing N N 372 
TRP CZ3 CH2  sing Y N 373 
TRP CZ3 HZ3  sing N N 374 
TRP CH2 HH2  sing N N 375 
TRP OXT HXT  sing N N 376 
TYR N   CA   sing N N 377 
TYR N   H    sing N N 378 
TYR N   H2   sing N N 379 
TYR CA  C    sing N N 380 
TYR CA  CB   sing N N 381 
TYR CA  HA   sing N N 382 
TYR C   O    doub N N 383 
TYR C   OXT  sing N N 384 
TYR CB  CG   sing N N 385 
TYR CB  HB2  sing N N 386 
TYR CB  HB3  sing N N 387 
TYR CG  CD1  doub Y N 388 
TYR CG  CD2  sing Y N 389 
TYR CD1 CE1  sing Y N 390 
TYR CD1 HD1  sing N N 391 
TYR CD2 CE2  doub Y N 392 
TYR CD2 HD2  sing N N 393 
TYR CE1 CZ   doub Y N 394 
TYR CE1 HE1  sing N N 395 
TYR CE2 CZ   sing Y N 396 
TYR CE2 HE2  sing N N 397 
TYR CZ  OH   sing N N 398 
TYR OH  HH   sing N N 399 
TYR OXT HXT  sing N N 400 
VAL N   CA   sing N N 401 
VAL N   H    sing N N 402 
VAL N   H2   sing N N 403 
VAL CA  C    sing N N 404 
VAL CA  CB   sing N N 405 
VAL CA  HA   sing N N 406 
VAL C   O    doub N N 407 
VAL C   OXT  sing N N 408 
VAL CB  CG1  sing N N 409 
VAL CB  CG2  sing N N 410 
VAL CB  HB   sing N N 411 
VAL CG1 HG11 sing N N 412 
VAL CG1 HG12 sing N N 413 
VAL CG1 HG13 sing N N 414 
VAL CG2 HG21 sing N N 415 
VAL CG2 HG22 sing N N 416 
VAL CG2 HG23 sing N N 417 
VAL OXT HXT  sing N N 418 
ZVG N1  C7   doub Y N 419 
ZVG N1  C8   sing Y N 420 
ZVG C7  C6   sing Y N 421 
ZVG N4  C14  doub Y N 422 
ZVG N4  C15  sing Y N 423 
ZVG N3  C14  sing N N 424 
ZVG N3  C8   sing N N 425 
ZVG C14 N5   sing Y N 426 
ZVG C8  C9   doub Y N 427 
ZVG C15 C17  doub Y N 428 
ZVG C4  N    sing N N 429 
ZVG C4  C3   sing N N 430 
ZVG N   C5   sing N N 431 
ZVG C6  C5   sing N N 432 
ZVG C6  C10  doub Y N 433 
ZVG C5  O1   doub N N 434 
ZVG N5  C16  doub Y N 435 
ZVG C13 C11  sing N N 436 
ZVG C17 C16  sing Y N 437 
ZVG C17 C18  sing N N 438 
ZVG C1  C    sing N N 439 
ZVG C9  C10  sing Y N 440 
ZVG C18 N6   trip N N 441 
ZVG C10 N2   sing N N 442 
ZVG O   C    sing N N 443 
ZVG N2  C11  sing N N 444 
ZVG C   C3   sing N N 445 
ZVG C   C2   sing N N 446 
ZVG C3  F    sing N N 447 
ZVG C11 C12  sing N N 448 
ZVG C13 H1   sing N N 449 
ZVG C13 H2   sing N N 450 
ZVG C13 H3   sing N N 451 
ZVG C16 H4   sing N N 452 
ZVG C15 H5   sing N N 453 
ZVG C11 H6   sing N N 454 
ZVG C12 H7   sing N N 455 
ZVG C12 H8   sing N N 456 
ZVG C12 H9   sing N N 457 
ZVG N3  H10  sing N N 458 
ZVG C7  H11  sing N N 459 
ZVG C9  H12  sing N N 460 
ZVG N2  H13  sing N N 461 
ZVG N   H14  sing N N 462 
ZVG C4  H15  sing N N 463 
ZVG C4  H16  sing N N 464 
ZVG C3  H17  sing N N 465 
ZVG C2  H18  sing N N 466 
ZVG C2  H19  sing N N 467 
ZVG C2  H20  sing N N 468 
ZVG C1  H21  sing N N 469 
ZVG C1  H22  sing N N 470 
ZVG C1  H23  sing N N 471 
ZVG O   H24  sing N N 472 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Unpublished IRAK4 structure' 
# 
_atom_sites.entry_id                    8SCV 
_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.fract_transf_matrix[1][1]   -0.001167 
_atom_sites.fract_transf_matrix[1][2]   -0.011446 
_atom_sites.fract_transf_matrix[1][3]   -0.001389 
_atom_sites.fract_transf_matrix[2][1]   -0.002558 
_atom_sites.fract_transf_matrix[2][2]   -0.000862 
_atom_sites.fract_transf_matrix[2][3]   0.009252 
_atom_sites.fract_transf_matrix[3][1]   -0.006861 
_atom_sites.fract_transf_matrix[3][2]   0.000919 
_atom_sites.fract_transf_matrix[3][3]   -0.001811 
_atom_sites.fract_transf_vector[1]      0.51859 
_atom_sites.fract_transf_vector[2]      0.11304 
_atom_sites.fract_transf_vector[3]      0.05144 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
F 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . THR A 1 8   ? 7.436  16.414 10.808 1.00 85.81  ?  163 THR A N   1 
ATOM   2    C CA  . THR A 1 8   ? 8.343  15.276 10.661 1.00 85.82  ?  163 THR A CA  1 
ATOM   3    C C   . THR A 1 8   ? 9.104  15.285 9.315  1.00 88.34  ?  163 THR A C   1 
ATOM   4    O O   . THR A 1 8   ? 10.320 15.487 9.334  1.00 88.39  ?  163 THR A O   1 
ATOM   5    C CB  . THR A 1 8   ? 7.705  13.931 11.134 1.00 96.70  ?  163 THR A CB  1 
ATOM   6    O OG1 . THR A 1 8   ? 8.700  12.904 11.187 1.00 94.17  ?  163 THR A OG1 1 
ATOM   7    C CG2 . THR A 1 8   ? 6.504  13.477 10.272 1.00 96.94  ?  163 THR A CG2 1 
ATOM   8    N N   . ARG A 1 9   ? 8.411  15.100 8.157  1.00 82.21  ?  164 ARG A N   1 
ATOM   9    C CA  . ARG A 1 9   ? 9.102  15.140 6.860  1.00 80.63  ?  164 ARG A CA  1 
ATOM   10   C C   . ARG A 1 9   ? 9.230  16.557 6.309  1.00 78.98  ?  164 ARG A C   1 
ATOM   11   O O   . ARG A 1 9   ? 8.233  17.262 6.093  1.00 78.52  ?  164 ARG A O   1 
ATOM   12   C CB  . ARG A 1 9   ? 8.550  14.147 5.835  1.00 83.55  ?  164 ARG A CB  1 
ATOM   13   C CG  . ARG A 1 9   ? 9.549  13.798 4.723  1.00 98.48  ?  164 ARG A CG  1 
ATOM   14   C CD  . ARG A 1 9   ? 10.697 12.912 5.190  1.00 108.80 ?  164 ARG A CD  1 
ATOM   15   N NE  . ARG A 1 9   ? 11.998 13.529 4.920  1.00 116.84 ?  164 ARG A NE  1 
ATOM   16   C CZ  . ARG A 1 9   ? 12.746 14.155 5.826  1.00 127.05 ?  164 ARG A CZ  1 
ATOM   17   N NH1 . ARG A 1 9   ? 13.913 14.680 5.482  1.00 110.98 ?  164 ARG A NH1 1 
ATOM   18   N NH2 . ARG A 1 9   ? 12.339 14.246 7.087  1.00 111.79 1  164 ARG A NH2 1 
ATOM   19   N N   . PHE A 1 10  ? 10.484 16.976 6.112  1.00 70.00  ?  165 PHE A N   1 
ATOM   20   C CA  . PHE A 1 10  ? 10.809 18.326 5.691  1.00 66.49  ?  165 PHE A CA  1 
ATOM   21   C C   . PHE A 1 10  ? 10.824 18.569 4.197  1.00 67.37  ?  165 PHE A C   1 
ATOM   22   O O   . PHE A 1 10  ? 11.168 17.679 3.409  1.00 66.31  ?  165 PHE A O   1 
ATOM   23   C CB  . PHE A 1 10  ? 12.115 18.792 6.358  1.00 66.62  ?  165 PHE A CB  1 
ATOM   24   C CG  . PHE A 1 10  ? 12.092 18.644 7.859  1.00 66.00  ?  165 PHE A CG  1 
ATOM   25   C CD1 . PHE A 1 10  ? 11.314 19.489 8.646  1.00 66.78  ?  165 PHE A CD1 1 
ATOM   26   C CD2 . PHE A 1 10  ? 12.828 17.644 8.485  1.00 66.62  ?  165 PHE A CD2 1 
ATOM   27   C CE1 . PHE A 1 10  ? 11.282 19.340 10.029 1.00 67.26  ?  165 PHE A CE1 1 
ATOM   28   C CE2 . PHE A 1 10  ? 12.805 17.502 9.873  1.00 68.30  ?  165 PHE A CE2 1 
ATOM   29   C CZ  . PHE A 1 10  ? 12.024 18.342 10.634 1.00 66.41  ?  165 PHE A CZ  1 
ATOM   30   N N   . HIS A 1 11  ? 10.466 19.806 3.823  1.00 62.42  ?  166 HIS A N   1 
ATOM   31   C CA  . HIS A 1 11  ? 10.470 20.286 2.453  1.00 61.86  ?  166 HIS A CA  1 
ATOM   32   C C   . HIS A 1 11  ? 11.912 20.424 1.938  1.00 63.92  ?  166 HIS A C   1 
ATOM   33   O O   . HIS A 1 11  ? 12.772 20.977 2.629  1.00 64.00  ?  166 HIS A O   1 
ATOM   34   C CB  . HIS A 1 11  ? 9.719  21.618 2.342  1.00 62.97  ?  166 HIS A CB  1 
ATOM   35   C CG  . HIS A 1 11  ? 9.691  22.130 0.944  1.00 67.59  ?  166 HIS A CG  1 
ATOM   36   N ND1 . HIS A 1 11  ? 10.558 22.946 0.304  1.00 70.32  ?  166 HIS A ND1 1 
ATOM   37   C CD2 . HIS A 1 11  ? 8.727  21.709 0.044  1.00 70.14  ?  166 HIS A CD2 1 
ATOM   38   C CE1 . HIS A 1 11  ? 10.110 23.061 -0.993 1.00 69.97  ?  166 HIS A CE1 1 
ATOM   39   N NE2 . HIS A 1 11  ? 9.012  22.312 -1.099 1.00 70.36  ?  166 HIS A NE2 1 
ATOM   40   N N   . SER A 1 12  ? 12.180 19.918 0.730  1.00 58.26  ?  167 SER A N   1 
ATOM   41   C CA  . SER A 1 12  ? 13.513 20.040 0.147  1.00 56.97  ?  167 SER A CA  1 
ATOM   42   C C   . SER A 1 12  ? 13.531 21.229 -0.811 1.00 60.22  ?  167 SER A C   1 
ATOM   43   O O   . SER A 1 12  ? 12.831 21.234 -1.838 1.00 60.95  ?  167 SER A O   1 
ATOM   44   C CB  . SER A 1 12  ? 13.931 18.756 -0.565 1.00 58.82  ?  167 SER A CB  1 
ATOM   45   O OG  . SER A 1 12  ? 15.215 18.898 -1.148 1.00 67.26  ?  167 SER A OG  1 
ATOM   46   N N   . PHE A 1 13  ? 14.300 22.256 -0.448 1.00 54.28  ?  168 PHE A N   1 
ATOM   47   C CA  . PHE A 1 13  ? 14.452 23.441 -1.290 1.00 52.46  ?  168 PHE A CA  1 
ATOM   48   C C   . PHE A 1 13  ? 15.646 23.206 -2.171 1.00 57.25  ?  168 PHE A C   1 
ATOM   49   O O   . PHE A 1 13  ? 16.497 22.377 -1.848 1.00 55.29  ?  168 PHE A O   1 
ATOM   50   C CB  . PHE A 1 13  ? 14.678 24.699 -0.440 1.00 52.51  ?  168 PHE A CB  1 
ATOM   51   C CG  . PHE A 1 13  ? 13.504 25.106 0.411  1.00 52.58  ?  168 PHE A CG  1 
ATOM   52   C CD1 . PHE A 1 13  ? 13.411 24.698 1.736  1.00 54.31  ?  168 PHE A CD1 1 
ATOM   53   C CD2 . PHE A 1 13  ? 12.498 25.913 -0.105 1.00 54.02  ?  168 PHE A CD2 1 
ATOM   54   C CE1 . PHE A 1 13  ? 12.335 25.096 2.531  1.00 54.84  ?  168 PHE A CE1 1 
ATOM   55   C CE2 . PHE A 1 13  ? 11.422 26.315 0.692  1.00 56.28  ?  168 PHE A CE2 1 
ATOM   56   C CZ  . PHE A 1 13  ? 11.349 25.905 2.006  1.00 54.22  ?  168 PHE A CZ  1 
ATOM   57   N N   . SER A 1 14  ? 15.715 23.909 -3.292 1.00 57.23  ?  169 SER A N   1 
ATOM   58   C CA  . SER A 1 14  ? 16.898 23.806 -4.157 1.00 58.06  ?  169 SER A CA  1 
ATOM   59   C C   . SER A 1 14  ? 17.799 24.993 -3.830 1.00 58.81  ?  169 SER A C   1 
ATOM   60   O O   . SER A 1 14  ? 17.300 26.093 -3.590 1.00 57.68  ?  169 SER A O   1 
ATOM   61   C CB  . SER A 1 14  ? 16.505 23.812 -5.630 1.00 63.42  ?  169 SER A CB  1 
ATOM   62   O OG  . SER A 1 14  ? 16.770 22.548 -6.219 1.00 76.24  ?  169 SER A OG  1 
ATOM   63   N N   . PHE A 1 15  ? 19.108 24.776 -3.805 1.00 54.50  ?  170 PHE A N   1 
ATOM   64   C CA  . PHE A 1 15  ? 20.058 25.850 -3.517 1.00 54.53  ?  170 PHE A CA  1 
ATOM   65   C C   . PHE A 1 15  ? 19.736 27.178 -4.220 1.00 59.04  ?  170 PHE A C   1 
ATOM   66   O O   . PHE A 1 15  ? 19.720 28.220 -3.555 1.00 59.55  ?  170 PHE A O   1 
ATOM   67   C CB  . PHE A 1 15  ? 21.506 25.429 -3.801 1.00 55.94  ?  170 PHE A CB  1 
ATOM   68   C CG  . PHE A 1 15  ? 22.512 26.403 -3.227 1.00 57.32  ?  170 PHE A CG  1 
ATOM   69   C CD1 . PHE A 1 15  ? 22.556 26.659 -1.859 1.00 59.23  ?  170 PHE A CD1 1 
ATOM   70   C CD2 . PHE A 1 15  ? 23.403 27.078 -4.056 1.00 58.77  ?  170 PHE A CD2 1 
ATOM   71   C CE1 . PHE A 1 15  ? 23.463 27.578 -1.333 1.00 59.51  ?  170 PHE A CE1 1 
ATOM   72   C CE2 . PHE A 1 15  ? 24.322 27.986 -3.526 1.00 60.81  ?  170 PHE A CE2 1 
ATOM   73   C CZ  . PHE A 1 15  ? 24.347 28.228 -2.171 1.00 58.71  ?  170 PHE A CZ  1 
ATOM   74   N N   . TYR A 1 16  ? 19.404 27.119 -5.534 1.00 53.59  ?  171 TYR A N   1 
ATOM   75   C CA  . TYR A 1 16  ? 19.113 28.286 -6.343 1.00 52.96  ?  171 TYR A CA  1 
ATOM   76   C C   . TYR A 1 16  ? 17.883 29.050 -5.912 1.00 56.45  ?  171 TYR A C   1 
ATOM   77   O O   . TYR A 1 16  ? 17.802 30.240 -6.199 1.00 57.34  ?  171 TYR A O   1 
ATOM   78   C CB  . TYR A 1 16  ? 19.141 27.977 -7.846 1.00 54.82  ?  171 TYR A CB  1 
ATOM   79   C CG  . TYR A 1 16  ? 17.885 27.326 -8.382 1.00 58.34  ?  171 TYR A CG  1 
ATOM   80   C CD1 . TYR A 1 16  ? 16.833 28.094 -8.887 1.00 60.54  ?  171 TYR A CD1 1 
ATOM   81   C CD2 . TYR A 1 16  ? 17.742 25.939 -8.390 1.00 58.35  ?  171 TYR A CD2 1 
ATOM   82   C CE1 . TYR A 1 16  ? 15.662 27.499 -9.349 1.00 60.05  ?  171 TYR A CE1 1 
ATOM   83   C CE2 . TYR A 1 16  ? 16.586 25.336 -8.880 1.00 58.57  ?  171 TYR A CE2 1 
ATOM   84   C CZ  . TYR A 1 16  ? 15.551 26.118 -9.364 1.00 62.86  ?  171 TYR A CZ  1 
ATOM   85   O OH  . TYR A 1 16  ? 14.405 25.516 -9.828 1.00 63.35  ?  171 TYR A OH  1 
ATOM   86   N N   . GLU A 1 17  ? 16.928 28.391 -5.240 1.00 51.88  ?  172 GLU A N   1 
ATOM   87   C CA  . GLU A 1 17  ? 15.735 29.072 -4.730 1.00 51.41  ?  172 GLU A CA  1 
ATOM   88   C C   . GLU A 1 17  ? 16.201 29.963 -3.557 1.00 52.88  ?  172 GLU A C   1 
ATOM   89   O O   . GLU A 1 17  ? 15.842 31.139 -3.482 1.00 52.07  ?  172 GLU A O   1 
ATOM   90   C CB  . GLU A 1 17  ? 14.672 28.072 -4.221 1.00 53.27  ?  172 GLU A CB  1 
ATOM   91   C CG  . GLU A 1 17  ? 14.387 26.864 -5.118 1.00 71.10  ?  172 GLU A CG  1 
ATOM   92   C CD  . GLU A 1 17  ? 13.524 25.750 -4.531 1.00 98.15  ?  172 GLU A CD  1 
ATOM   93   O OE1 . GLU A 1 17  ? 13.090 25.860 -3.361 1.00 88.61  ?  172 GLU A OE1 1 
ATOM   94   O OE2 . GLU A 1 17  ? 13.327 24.733 -5.230 1.00 98.56  -1 172 GLU A OE2 1 
ATOM   95   N N   . LEU A 1 18  ? 17.067 29.401 -2.694 1.00 47.36  ?  173 LEU A N   1 
ATOM   96   C CA  . LEU A 1 18  ? 17.607 30.051 -1.508 1.00 46.53  ?  173 LEU A CA  1 
ATOM   97   C C   . LEU A 1 18  ? 18.520 31.253 -1.780 1.00 52.02  ?  173 LEU A C   1 
ATOM   98   O O   . LEU A 1 18  ? 18.409 32.272 -1.088 1.00 51.93  ?  173 LEU A O   1 
ATOM   99   C CB  . LEU A 1 18  ? 18.172 29.018 -0.517 1.00 46.00  ?  173 LEU A CB  1 
ATOM   100  C CG  . LEU A 1 18  ? 17.140 27.943 -0.048 1.00 49.01  ?  173 LEU A CG  1 
ATOM   101  C CD1 . LEU A 1 18  ? 17.758 26.930 0.857  1.00 47.58  ?  173 LEU A CD1 1 
ATOM   102  C CD2 . LEU A 1 18  ? 15.921 28.569 0.629  1.00 49.64  ?  173 LEU A CD2 1 
ATOM   103  N N   . LYS A 1 19  ? 19.336 31.175 -2.847 1.00 48.77  ?  174 LYS A N   1 
ATOM   104  C CA  . LYS A 1 19  ? 20.195 32.250 -3.324 1.00 48.87  ?  174 LYS A CA  1 
ATOM   105  C C   . LYS A 1 19  ? 19.358 33.523 -3.617 1.00 53.60  ?  174 LYS A C   1 
ATOM   106  O O   . LYS A 1 19  ? 19.641 34.602 -3.083 1.00 53.97  ?  174 LYS A O   1 
ATOM   107  C CB  . LYS A 1 19  ? 20.847 31.815 -4.636 1.00 52.11  ?  174 LYS A CB  1 
ATOM   108  C CG  . LYS A 1 19  ? 22.134 31.027 -4.518 1.00 64.71  ?  174 LYS A CG  1 
ATOM   109  C CD  . LYS A 1 19  ? 22.660 30.633 -5.914 1.00 72.74  ?  174 LYS A CD  1 
ATOM   110  C CE  . LYS A 1 19  ? 23.024 31.798 -6.820 1.00 70.76  ?  174 LYS A CE  1 
ATOM   111  N NZ  . LYS A 1 19  ? 24.425 31.695 -7.297 1.00 73.79  1  174 LYS A NZ  1 
ATOM   112  N N   . ASN A 1 20  ? 18.268 33.344 -4.398 1.00 49.58  ?  175 ASN A N   1 
ATOM   113  C CA  . ASN A 1 20  ? 17.339 34.380 -4.842 1.00 48.86  ?  175 ASN A CA  1 
ATOM   114  C C   . ASN A 1 20  ? 16.606 35.089 -3.686 1.00 53.48  ?  175 ASN A C   1 
ATOM   115  O O   . ASN A 1 20  ? 16.534 36.326 -3.630 1.00 54.99  ?  175 ASN A O   1 
ATOM   116  C CB  . ASN A 1 20  ? 16.358 33.776 -5.838 1.00 46.02  ?  175 ASN A CB  1 
ATOM   117  C CG  . ASN A 1 20  ? 16.994 33.185 -7.098 1.00 82.07  ?  175 ASN A CG  1 
ATOM   118  O OD1 . ASN A 1 20  ? 16.543 32.160 -7.639 1.00 68.96  ?  175 ASN A OD1 1 
ATOM   119  N ND2 . ASN A 1 20  ? 18.038 33.827 -7.627 1.00 82.24  ?  175 ASN A ND2 1 
ATOM   120  N N   . VAL A 1 21  ? 16.148 34.291 -2.734 1.00 47.46  ?  176 VAL A N   1 
ATOM   121  C CA  . VAL A 1 21  ? 15.383 34.659 -1.557 1.00 45.88  ?  176 VAL A CA  1 
ATOM   122  C C   . VAL A 1 21  ? 16.240 35.405 -0.519 1.00 48.13  ?  176 VAL A C   1 
ATOM   123  O O   . VAL A 1 21  ? 15.689 36.118 0.335  1.00 47.46  ?  176 VAL A O   1 
ATOM   124  C CB  . VAL A 1 21  ? 14.780 33.324 -1.066 1.00 50.07  ?  176 VAL A CB  1 
ATOM   125  C CG1 . VAL A 1 21  ? 15.038 33.020 0.403  1.00 49.50  ?  176 VAL A CG1 1 
ATOM   126  C CG2 . VAL A 1 21  ? 13.316 33.204 -1.449 1.00 50.14  ?  176 VAL A CG2 1 
ATOM   127  N N   . THR A 1 22  ? 17.589 35.251 -0.608 1.00 41.35  ?  177 THR A N   1 
ATOM   128  C CA  . THR A 1 22  ? 18.540 35.883 0.300  1.00 39.33  ?  177 THR A CA  1 
ATOM   129  C C   . THR A 1 22  ? 19.407 36.955 -0.380 1.00 42.34  ?  177 THR A C   1 
ATOM   130  O O   . THR A 1 22  ? 20.424 37.358 0.196  1.00 40.82  ?  177 THR A O   1 
ATOM   131  C CB  . THR A 1 22  ? 19.428 34.811 0.940  1.00 45.06  ?  177 THR A CB  1 
ATOM   132  O OG1 . THR A 1 22  ? 20.188 34.139 -0.067 1.00 41.77  ?  177 THR A OG1 1 
ATOM   133  C CG2 . THR A 1 22  ? 18.653 33.836 1.787  1.00 41.18  ?  177 THR A CG2 1 
ATOM   134  N N   . ASN A 1 23  ? 19.015 37.410 -1.604 1.00 39.55  ?  178 ASN A N   1 
ATOM   135  C CA  . ASN A 1 23  ? 19.742 38.383 -2.430 1.00 39.14  ?  178 ASN A CA  1 
ATOM   136  C C   . ASN A 1 23  ? 21.189 37.905 -2.652 1.00 42.34  ?  178 ASN A C   1 
ATOM   137  O O   . ASN A 1 23  ? 22.171 38.612 -2.365 1.00 41.03  ?  178 ASN A O   1 
ATOM   138  C CB  . ASN A 1 23  ? 19.634 39.828 -1.877 1.00 45.59  ?  178 ASN A CB  1 
ATOM   139  C CG  . ASN A 1 23  ? 18.200 40.313 -1.674 1.00 87.04  ?  178 ASN A CG  1 
ATOM   140  O OD1 . ASN A 1 23  ? 17.483 40.548 -2.776 1.00 79.68  ?  178 ASN A OD1 1 
ATOM   141  N ND2 . ASN A 1 23  ? 17.714 40.480 -0.535 1.00 82.02  ?  178 ASN A ND2 1 
ATOM   142  N N   . ASN A 1 24  ? 21.293 36.662 -3.162 1.00 39.18  ?  179 ASN A N   1 
ATOM   143  C CA  . ASN A 1 24  ? 22.529 35.917 -3.432 1.00 39.33  ?  179 ASN A CA  1 
ATOM   144  C C   . ASN A 1 24  ? 23.402 35.837 -2.173 1.00 42.27  ?  179 ASN A C   1 
ATOM   145  O O   . ASN A 1 24  ? 24.579 36.189 -2.195 1.00 42.84  ?  179 ASN A O   1 
ATOM   146  C CB  . ASN A 1 24  ? 23.279 36.407 -4.699 1.00 41.06  ?  179 ASN A CB  1 
ATOM   147  C CG  . ASN A 1 24  ? 24.415 35.463 -5.105 1.00 69.15  ?  179 ASN A CG  1 
ATOM   148  O OD1 . ASN A 1 24  ? 24.352 34.223 -4.939 1.00 54.10  ?  179 ASN A OD1 1 
ATOM   149  N ND2 . ASN A 1 24  ? 25.537 36.044 -5.508 1.00 62.20  ?  179 ASN A ND2 1 
ATOM   150  N N   . PHE A 1 25  ? 22.787 35.396 -1.061 1.00 37.39  ?  180 PHE A N   1 
ATOM   151  C CA  . PHE A 1 25  ? 23.409 35.300 0.264  1.00 35.65  ?  180 PHE A CA  1 
ATOM   152  C C   . PHE A 1 25  ? 24.190 36.563 0.578  1.00 36.61  ?  180 PHE A C   1 
ATOM   153  O O   . PHE A 1 25  ? 25.404 36.521 0.722  1.00 36.86  ?  180 PHE A O   1 
ATOM   154  C CB  . PHE A 1 25  ? 24.257 34.011 0.410  1.00 36.65  ?  180 PHE A CB  1 
ATOM   155  C CG  . PHE A 1 25  ? 23.442 32.737 0.354  1.00 37.44  ?  180 PHE A CG  1 
ATOM   156  C CD1 . PHE A 1 25  ? 22.683 32.325 1.451  1.00 38.81  ?  180 PHE A CD1 1 
ATOM   157  C CD2 . PHE A 1 25  ? 23.387 31.979 -0.804 1.00 38.06  ?  180 PHE A CD2 1 
ATOM   158  C CE1 . PHE A 1 25  ? 21.920 31.156 1.402  1.00 38.12  ?  180 PHE A CE1 1 
ATOM   159  C CE2 . PHE A 1 25  ? 22.585 30.837 -0.863 1.00 40.40  ?  180 PHE A CE2 1 
ATOM   160  C CZ  . PHE A 1 25  ? 21.897 30.404 0.260  1.00 37.28  ?  180 PHE A CZ  1 
ATOM   161  N N   . ASP A 1 26  ? 23.495 37.702 0.573  1.00 32.78  ?  181 ASP A N   1 
ATOM   162  C CA  . ASP A 1 26  ? 24.088 39.020 0.842  1.00 33.21  ?  181 ASP A CA  1 
ATOM   163  C C   . ASP A 1 26  ? 24.548 39.067 2.331  1.00 39.96  ?  181 ASP A C   1 
ATOM   164  O O   . ASP A 1 26  ? 23.743 39.217 3.263  1.00 38.52  ?  181 ASP A O   1 
ATOM   165  C CB  . ASP A 1 26  ? 23.089 40.146 0.455  1.00 34.08  ?  181 ASP A CB  1 
ATOM   166  C CG  . ASP A 1 26  ? 23.553 41.581 0.631  1.00 40.09  ?  181 ASP A CG  1 
ATOM   167  O OD1 . ASP A 1 26  ? 24.702 41.786 1.042  1.00 43.27  ?  181 ASP A OD1 1 
ATOM   168  O OD2 . ASP A 1 26  ? 22.762 42.496 0.352  1.00 43.13  -1 181 ASP A OD2 1 
ATOM   169  N N   . GLU A 1 27  ? 25.857 38.849 2.514  1.00 39.15  ?  182 GLU A N   1 
ATOM   170  C CA  . GLU A 1 27  ? 26.559 38.787 3.791  1.00 40.23  ?  182 GLU A CA  1 
ATOM   171  C C   . GLU A 1 27  ? 26.626 40.071 4.634  1.00 43.60  ?  182 GLU A C   1 
ATOM   172  O O   . GLU A 1 27  ? 27.022 39.997 5.806  1.00 44.99  ?  182 GLU A O   1 
ATOM   173  C CB  . GLU A 1 27  ? 27.946 38.156 3.613  1.00 42.26  ?  182 GLU A CB  1 
ATOM   174  C CG  . GLU A 1 27  ? 27.958 36.767 4.233  1.00 60.69  ?  182 GLU A CG  1 
ATOM   175  C CD  . GLU A 1 27  ? 29.081 35.816 3.857  1.00 94.15  ?  182 GLU A CD  1 
ATOM   176  O OE1 . GLU A 1 27  ? 29.401 35.697 2.649  1.00 90.40  ?  182 GLU A OE1 1 
ATOM   177  O OE2 . GLU A 1 27  ? 29.579 35.123 4.775  1.00 88.73  -1 182 GLU A OE2 1 
ATOM   178  N N   . ARG A 1 28  ? 26.280 41.236 4.055  1.00 35.96  ?  183 ARG A N   1 
ATOM   179  C CA  . ARG A 1 28  ? 26.257 42.482 4.808  1.00 35.78  ?  183 ARG A CA  1 
ATOM   180  C C   . ARG A 1 28  ? 25.133 42.408 5.881  1.00 43.06  ?  183 ARG A C   1 
ATOM   181  O O   . ARG A 1 28  ? 24.096 41.775 5.628  1.00 44.08  ?  183 ARG A O   1 
ATOM   182  C CB  . ARG A 1 28  ? 26.003 43.672 3.866  1.00 33.93  ?  183 ARG A CB  1 
ATOM   183  C CG  . ARG A 1 28  ? 27.062 43.816 2.736  1.00 37.45  ?  183 ARG A CG  1 
ATOM   184  C CD  . ARG A 1 28  ? 26.715 44.942 1.764  1.00 40.25  ?  183 ARG A CD  1 
ATOM   185  N NE  . ARG A 1 28  ? 25.460 44.686 1.044  1.00 40.70  ?  183 ARG A NE  1 
ATOM   186  C CZ  . ARG A 1 28  ? 24.846 45.563 0.264  1.00 50.35  ?  183 ARG A CZ  1 
ATOM   187  N NH1 . ARG A 1 28  ? 23.699 45.250 -0.323 1.00 23.94  ?  183 ARG A NH1 1 
ATOM   188  N NH2 . ARG A 1 28  ? 25.360 46.772 0.081  1.00 51.69  1  183 ARG A NH2 1 
ATOM   189  N N   . PRO A 1 29  ? 25.293 43.002 7.085  1.00 39.74  ?  184 PRO A N   1 
ATOM   190  C CA  . PRO A 1 29  ? 24.201 42.939 8.072  1.00 39.05  ?  184 PRO A CA  1 
ATOM   191  C C   . PRO A 1 29  ? 22.938 43.622 7.586  1.00 43.17  ?  184 PRO A C   1 
ATOM   192  O O   . PRO A 1 29  ? 22.995 44.550 6.777  1.00 43.07  ?  184 PRO A O   1 
ATOM   193  C CB  . PRO A 1 29  ? 24.774 43.669 9.287  1.00 40.34  ?  184 PRO A CB  1 
ATOM   194  C CG  . PRO A 1 29  ? 26.247 43.647 9.093  1.00 44.27  ?  184 PRO A CG  1 
ATOM   195  C CD  . PRO A 1 29  ? 26.453 43.740 7.626  1.00 40.60  ?  184 PRO A CD  1 
ATOM   196  N N   . ILE A 1 30  ? 21.794 43.108 8.046  1.00 39.92  ?  185 ILE A N   1 
ATOM   197  C CA  . ILE A 1 30  ? 20.479 43.670 7.760  1.00 40.71  ?  185 ILE A CA  1 
ATOM   198  C C   . ILE A 1 30  ? 20.482 45.185 8.122  1.00 47.44  ?  185 ILE A C   1 
ATOM   199  O O   . ILE A 1 30  ? 19.837 45.965 7.458  1.00 49.42  ?  185 ILE A O   1 
ATOM   200  C CB  . ILE A 1 30  ? 19.318 42.830 8.423  1.00 44.23  ?  185 ILE A CB  1 
ATOM   201  C CG1 . ILE A 1 30  ? 19.616 42.443 9.913  1.00 45.61  ?  185 ILE A CG1 1 
ATOM   202  C CG2 . ILE A 1 30  ? 19.006 41.562 7.598  1.00 42.64  ?  185 ILE A CG2 1 
ATOM   203  C CD1 . ILE A 1 30  ? 18.349 42.264 10.847 1.00 58.37  ?  185 ILE A CD1 1 
ATOM   204  N N   . SER A 1 31  ? 21.337 45.597 9.079  1.00 45.47  ?  186 SER A N   1 
ATOM   205  C CA  . SER A 1 31  ? 21.570 46.965 9.562  1.00 45.56  ?  186 SER A CA  1 
ATOM   206  C C   . SER A 1 31  ? 22.153 47.901 8.477  1.00 53.23  ?  186 SER A C   1 
ATOM   207  O O   . SER A 1 31  ? 22.024 49.128 8.590  1.00 56.35  ?  186 SER A O   1 
ATOM   208  C CB  . SER A 1 31  ? 22.537 46.943 10.744 1.00 49.18  ?  186 SER A CB  1 
ATOM   209  O OG  . SER A 1 31  ? 22.547 45.697 11.428 1.00 66.21  ?  186 SER A OG  1 
ATOM   210  N N   . VAL A 1 32  ? 22.864 47.338 7.482  1.00 47.41  ?  187 VAL A N   1 
ATOM   211  C CA  . VAL A 1 32  ? 23.494 48.095 6.404  1.00 45.61  ?  187 VAL A CA  1 
ATOM   212  C C   . VAL A 1 32  ? 22.916 47.668 5.062  1.00 50.47  ?  187 VAL A C   1 
ATOM   213  O O   . VAL A 1 32  ? 23.557 47.857 4.035  1.00 51.48  ?  187 VAL A O   1 
ATOM   214  C CB  . VAL A 1 32  ? 25.056 48.096 6.429  1.00 48.81  ?  187 VAL A CB  1 
ATOM   215  C CG1 . VAL A 1 32  ? 25.611 48.521 7.786  1.00 47.90  ?  187 VAL A CG1 1 
ATOM   216  C CG2 . VAL A 1 32  ? 25.646 46.761 5.989  1.00 48.52  ?  187 VAL A CG2 1 
ATOM   217  N N   . GLY A 1 33  ? 21.707 47.106 5.086  1.00 46.13  ?  188 GLY A N   1 
ATOM   218  C CA  . GLY A 1 33  ? 20.983 46.688 3.896  1.00 45.17  ?  188 GLY A CA  1 
ATOM   219  C C   . GLY A 1 33  ? 21.354 45.355 3.272  1.00 48.46  ?  188 GLY A C   1 
ATOM   220  O O   . GLY A 1 33  ? 21.097 45.148 2.084  1.00 48.84  ?  188 GLY A O   1 
ATOM   221  N N   . GLY A 1 34  ? 21.900 44.438 4.071  1.00 42.46  ?  189 GLY A N   1 
ATOM   222  C CA  . GLY A 1 34  ? 22.237 43.089 3.636  1.00 40.28  ?  189 GLY A CA  1 
ATOM   223  C C   . GLY A 1 34  ? 21.194 42.095 4.106  1.00 41.95  ?  189 GLY A C   1 
ATOM   224  O O   . GLY A 1 34  ? 20.079 42.493 4.445  1.00 41.67  ?  189 GLY A O   1 
ATOM   225  N N   . ASN A 1 35  ? 21.538 40.792 4.141  1.00 37.41  ?  190 ASN A N   1 
ATOM   226  C CA  . ASN A 1 35  ? 20.608 39.751 4.607  1.00 36.15  ?  190 ASN A CA  1 
ATOM   227  C C   . ASN A 1 35  ? 21.108 39.019 5.849  1.00 37.46  ?  190 ASN A C   1 
ATOM   228  O O   . ASN A 1 35  ? 20.416 38.162 6.389  1.00 35.49  ?  190 ASN A O   1 
ATOM   229  C CB  . ASN A 1 35  ? 20.273 38.781 3.479  1.00 36.38  ?  190 ASN A CB  1 
ATOM   230  C CG  . ASN A 1 35  ? 19.258 39.364 2.537  1.00 48.79  ?  190 ASN A CG  1 
ATOM   231  O OD1 . ASN A 1 35  ? 19.511 40.377 1.850  1.00 31.32  ?  190 ASN A OD1 1 
ATOM   232  N ND2 . ASN A 1 35  ? 18.047 38.802 2.580  1.00 36.38  ?  190 ASN A ND2 1 
ATOM   233  N N   . LYS A 1 36  ? 22.307 39.378 6.311  1.00 34.35  ?  191 LYS A N   1 
ATOM   234  C CA  . LYS A 1 36  ? 22.901 38.738 7.465  1.00 35.65  ?  191 LYS A CA  1 
ATOM   235  C C   . LYS A 1 36  ? 22.259 39.127 8.801  1.00 41.23  ?  191 LYS A C   1 
ATOM   236  O O   . LYS A 1 36  ? 22.302 40.291 9.198  1.00 41.55  ?  191 LYS A O   1 
ATOM   237  C CB  . LYS A 1 36  ? 24.417 38.939 7.504  1.00 38.43  ?  191 LYS A CB  1 
ATOM   238  C CG  . LYS A 1 36  ? 25.099 37.806 8.248  1.00 42.60  ?  191 LYS A CG  1 
ATOM   239  C CD  . LYS A 1 36  ? 26.103 38.281 9.231  1.00 45.98  ?  191 LYS A CD  1 
ATOM   240  C CE  . LYS A 1 36  ? 27.440 38.585 8.637  1.00 46.04  ?  191 LYS A CE  1 
ATOM   241  N NZ  . LYS A 1 36  ? 28.180 39.590 9.454  1.00 62.83  1  191 LYS A NZ  1 
ATOM   242  N N   . MET A 1 37  ? 21.722 38.119 9.500  1.00 36.62  ?  192 MET A N   1 
ATOM   243  C CA  . MET A 1 37  ? 21.113 38.244 10.814 1.00 36.29  ?  192 MET A CA  1 
ATOM   244  C C   . MET A 1 37  ? 22.059 37.770 11.943 1.00 42.33  ?  192 MET A C   1 
ATOM   245  O O   . MET A 1 37  ? 21.897 38.155 13.094 1.00 41.63  ?  192 MET A O   1 
ATOM   246  C CB  . MET A 1 37  ? 19.796 37.465 10.856 1.00 38.16  ?  192 MET A CB  1 
ATOM   247  C CG  . MET A 1 37  ? 18.778 37.992 9.876  1.00 40.86  ?  192 MET A CG  1 
ATOM   248  S SD  . MET A 1 37  ? 17.121 37.375 10.195 1.00 44.35  ?  192 MET A SD  1 
ATOM   249  C CE  . MET A 1 37  ? 17.345 35.661 9.860  1.00 40.43  ?  192 MET A CE  1 
ATOM   250  N N   . GLY A 1 38  ? 23.040 36.942 11.600 1.00 39.87  ?  193 GLY A N   1 
ATOM   251  C CA  . GLY A 1 38  ? 24.003 36.442 12.568 1.00 39.24  ?  193 GLY A CA  1 
ATOM   252  C C   . GLY A 1 38  ? 24.864 35.339 12.019 1.00 45.76  ?  193 GLY A C   1 
ATOM   253  O O   . GLY A 1 38  ? 24.651 34.863 10.900 1.00 44.79  ?  193 GLY A O   1 
ATOM   254  N N   . GLU A 1 39  ? 25.844 34.921 12.823 1.00 45.79  ?  194 GLU A N   1 
ATOM   255  C CA  . GLU A 1 39  ? 26.779 33.861 12.478 1.00 46.10  ?  194 GLU A CA  1 
ATOM   256  C C   . GLU A 1 39  ? 27.292 33.172 13.716 1.00 52.43  ?  194 GLU A C   1 
ATOM   257  O O   . GLU A 1 39  ? 27.252 33.725 14.802 1.00 52.94  ?  194 GLU A O   1 
ATOM   258  C CB  . GLU A 1 39  ? 27.912 34.376 11.572 1.00 47.21  ?  194 GLU A CB  1 
ATOM   259  C CG  . GLU A 1 39  ? 28.821 35.426 12.177 1.00 56.19  ?  194 GLU A CG  1 
ATOM   260  C CD  . GLU A 1 39  ? 29.913 35.812 11.203 1.00 88.06  ?  194 GLU A CD  1 
ATOM   261  O OE1 . GLU A 1 39  ? 30.912 35.063 11.097 1.00 89.72  ?  194 GLU A OE1 1 
ATOM   262  O OE2 . GLU A 1 39  ? 29.725 36.815 10.478 1.00 88.89  -1 194 GLU A OE2 1 
ATOM   263  N N   . GLY A 1 40  ? 27.680 31.933 13.522 1.00 50.01  ?  195 GLY A N   1 
ATOM   264  C CA  . GLY A 1 40  ? 28.278 31.076 14.525 1.00 50.10  ?  195 GLY A CA  1 
ATOM   265  C C   . GLY A 1 40  ? 29.522 30.497 13.903 1.00 56.58  ?  195 GLY A C   1 
ATOM   266  O O   . GLY A 1 40  ? 29.923 30.910 12.800 1.00 55.74  ?  195 GLY A O   1 
ATOM   267  N N   . GLY A 1 41  ? 30.107 29.519 14.583 1.00 55.22  ?  196 GLY A N   1 
ATOM   268  C CA  . GLY A 1 41  ? 31.312 28.866 14.095 1.00 55.76  ?  196 GLY A CA  1 
ATOM   269  C C   . GLY A 1 41  ? 31.092 27.959 12.906 1.00 61.20  ?  196 GLY A C   1 
ATOM   270  O O   . GLY A 1 41  ? 32.005 27.794 12.091 1.00 61.16  ?  196 GLY A O   1 
ATOM   271  N N   . PHE A 1 42  ? 29.869 27.377 12.794 1.00 58.05  ?  197 PHE A N   1 
ATOM   272  C CA  . PHE A 1 42  ? 29.517 26.413 11.754 1.00 57.69  ?  197 PHE A CA  1 
ATOM   273  C C   . PHE A 1 42  ? 28.591 26.931 10.659 1.00 58.94  ?  197 PHE A C   1 
ATOM   274  O O   . PHE A 1 42  ? 28.175 26.126 9.819  1.00 58.78  ?  197 PHE A O   1 
ATOM   275  C CB  . PHE A 1 42  ? 28.979 25.096 12.377 1.00 60.03  ?  197 PHE A CB  1 
ATOM   276  C CG  . PHE A 1 42  ? 29.815 24.560 13.517 1.00 62.14  ?  197 PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 42  ? 29.324 24.552 14.813 1.00 65.84  ?  197 PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 42  ? 31.112 24.108 13.298 1.00 64.50  ?  197 PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 42  ? 30.113 24.092 15.870 1.00 67.19  ?  197 PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 42  ? 31.898 23.649 14.354 1.00 67.31  ?  197 PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 42  ? 31.393 23.636 15.630 1.00 65.46  ?  197 PHE A CZ  1 
ATOM   282  N N   . GLY A 1 43  ? 28.303 28.243 10.648 1.00 52.28  ?  198 GLY A N   1 
ATOM   283  C CA  . GLY A 1 43  ? 27.418 28.818 9.640  1.00 50.78  ?  198 GLY A CA  1 
ATOM   284  C C   . GLY A 1 43  ? 26.985 30.253 9.830  1.00 51.67  ?  198 GLY A C   1 
ATOM   285  O O   . GLY A 1 43  ? 27.236 30.868 10.869 1.00 51.77  ?  198 GLY A O   1 
ATOM   286  N N   . VAL A 1 44  ? 26.350 30.804 8.789  1.00 45.36  ?  199 VAL A N   1 
ATOM   287  C CA  . VAL A 1 44  ? 25.832 32.175 8.747  1.00 43.28  ?  199 VAL A CA  1 
ATOM   288  C C   . VAL A 1 44  ? 24.326 32.099 8.502  1.00 44.48  ?  199 VAL A C   1 
ATOM   289  O O   . VAL A 1 44  ? 23.885 31.306 7.670  1.00 44.99  ?  199 VAL A O   1 
ATOM   290  C CB  . VAL A 1 44  ? 26.576 33.068 7.702  1.00 46.20  ?  199 VAL A CB  1 
ATOM   291  C CG1 . VAL A 1 44  ? 25.999 34.475 7.645  1.00 45.28  ?  199 VAL A CG1 1 
ATOM   292  C CG2 . VAL A 1 44  ? 28.072 33.134 7.992  1.00 45.58  ?  199 VAL A CG2 1 
ATOM   293  N N   . VAL A 1 45  ? 23.545 32.895 9.259  1.00 38.08  ?  200 VAL A N   1 
ATOM   294  C CA  . VAL A 1 45  ? 22.085 32.966 9.167  1.00 35.50  ?  200 VAL A CA  1 
ATOM   295  C C   . VAL A 1 45  ? 21.654 34.205 8.362  1.00 37.16  ?  200 VAL A C   1 
ATOM   296  O O   . VAL A 1 45  ? 22.072 35.321 8.670  1.00 35.94  ?  200 VAL A O   1 
ATOM   297  C CB  . VAL A 1 45  ? 21.405 32.896 10.565 1.00 37.29  ?  200 VAL A CB  1 
ATOM   298  C CG1 . VAL A 1 45  ? 19.874 32.803 10.431 1.00 36.93  ?  200 VAL A CG1 1 
ATOM   299  C CG2 . VAL A 1 45  ? 21.941 31.719 11.358 1.00 36.34  ?  200 VAL A CG2 1 
ATOM   300  N N   . TYR A 1 46  ? 20.769 34.001 7.379  1.00 33.89  ?  201 TYR A N   1 
ATOM   301  C CA  . TYR A 1 46  ? 20.256 35.048 6.490  1.00 33.04  ?  201 TYR A CA  1 
ATOM   302  C C   . TYR A 1 46  ? 18.746 35.209 6.572  1.00 39.12  ?  201 TYR A C   1 
ATOM   303  O O   . TYR A 1 46  ? 18.022 34.233 6.789  1.00 41.70  ?  201 TYR A O   1 
ATOM   304  C CB  . TYR A 1 46  ? 20.603 34.711 5.025  1.00 33.14  ?  201 TYR A CB  1 
ATOM   305  C CG  . TYR A 1 46  ? 22.076 34.505 4.762  1.00 33.65  ?  201 TYR A CG  1 
ATOM   306  C CD1 . TYR A 1 46  ? 22.697 33.297 5.071  1.00 35.38  ?  201 TYR A CD1 1 
ATOM   307  C CD2 . TYR A 1 46  ? 22.847 35.505 4.173  1.00 33.44  ?  201 TYR A CD2 1 
ATOM   308  C CE1 . TYR A 1 46  ? 24.060 33.103 4.838  1.00 38.45  ?  201 TYR A CE1 1 
ATOM   309  C CE2 . TYR A 1 46  ? 24.206 35.314 3.921  1.00 33.81  ?  201 TYR A CE2 1 
ATOM   310  C CZ  . TYR A 1 46  ? 24.807 34.109 4.252  1.00 41.26  ?  201 TYR A CZ  1 
ATOM   311  O OH  . TYR A 1 46  ? 26.145 33.903 4.035  1.00 41.37  ?  201 TYR A OH  1 
ATOM   312  N N   . LYS A 1 47  ? 18.267 36.434 6.338  1.00 34.04  ?  202 LYS A N   1 
ATOM   313  C CA  . LYS A 1 47  ? 16.856 36.720 6.214  1.00 33.61  ?  202 LYS A CA  1 
ATOM   314  C C   . LYS A 1 47  ? 16.431 36.297 4.791  1.00 40.53  ?  202 LYS A C   1 
ATOM   315  O O   . LYS A 1 47  ? 17.172 36.446 3.824  1.00 39.54  ?  202 LYS A O   1 
ATOM   316  C CB  . LYS A 1 47  ? 16.584 38.199 6.446  1.00 34.83  ?  202 LYS A CB  1 
ATOM   317  C CG  . LYS A 1 47  ? 15.121 38.511 6.702  1.00 36.98  ?  202 LYS A CG  1 
ATOM   318  C CD  . LYS A 1 47  ? 14.956 39.904 7.234  1.00 33.32  ?  202 LYS A CD  1 
ATOM   319  C CE  . LYS A 1 47  ? 13.513 40.235 7.448  1.00 37.66  ?  202 LYS A CE  1 
ATOM   320  N NZ  . LYS A 1 47  ? 13.344 41.696 7.667  1.00 58.80  1  202 LYS A NZ  1 
ATOM   321  N N   . GLY A 1 48  ? 15.265 35.702 4.706  1.00 40.68  ?  203 GLY A N   1 
ATOM   322  C CA  . GLY A 1 48  ? 14.714 35.195 3.463  1.00 40.77  ?  203 GLY A CA  1 
ATOM   323  C C   . GLY A 1 48  ? 13.224 35.423 3.373  1.00 45.72  ?  203 GLY A C   1 
ATOM   324  O O   . GLY A 1 48  ? 12.553 35.592 4.397  1.00 40.55  ?  203 GLY A O   1 
ATOM   325  N N   . TYR A 1 49  ? 12.724 35.463 2.117  1.00 48.12  ?  204 TYR A N   1 
ATOM   326  C CA  A TYR A 1 49  ? 11.324 35.652 1.798  0.50 48.86  ?  204 TYR A CA  1 
ATOM   327  C CA  B TYR A 1 49  ? 11.303 35.622 1.833  0.50 48.92  ?  204 TYR A CA  1 
ATOM   328  C C   . TYR A 1 49  ? 10.867 34.556 0.837  1.00 55.55  ?  204 TYR A C   1 
ATOM   329  O O   . TYR A 1 49  ? 10.888 34.773 -0.375 1.00 57.17  ?  204 TYR A O   1 
ATOM   330  C CB  A TYR A 1 49  ? 11.126 37.051 1.200  0.50 49.82  ?  204 TYR A CB  1 
ATOM   331  C CB  B TYR A 1 49  ? 10.939 37.063 1.403  0.50 49.96  ?  204 TYR A CB  1 
ATOM   332  C CG  A TYR A 1 49  ? 11.228 38.161 2.220  0.50 51.35  ?  204 TYR A CG  1 
ATOM   333  C CG  B TYR A 1 49  ? 9.463  37.259 1.108  0.50 51.49  ?  204 TYR A CG  1 
ATOM   334  C CD1 A TYR A 1 49  ? 12.452 38.766 2.503  0.50 53.33  ?  204 TYR A CD1 1 
ATOM   335  C CD1 B TYR A 1 49  ? 8.534  37.382 2.139  0.50 53.40  ?  204 TYR A CD1 1 
ATOM   336  C CD2 A TYR A 1 49  ? 10.099 38.632 2.881  0.50 51.61  ?  204 TYR A CD2 1 
ATOM   337  C CD2 B TYR A 1 49  ? 8.996  37.332 -0.202 0.50 52.05  ?  204 TYR A CD2 1 
ATOM   338  C CE1 A TYR A 1 49  ? 12.551 39.789 3.446  0.50 53.93  ?  204 TYR A CE1 1 
ATOM   339  C CE1 B TYR A 1 49  ? 7.171  37.531 1.871  0.50 54.23  ?  204 TYR A CE1 1 
ATOM   340  C CE2 A TYR A 1 49  ? 10.184 39.665 3.810  0.50 52.23  ?  204 TYR A CE2 1 
ATOM   341  C CE2 B TYR A 1 49  ? 7.639  37.485 -0.481 0.50 52.68  ?  204 TYR A CE2 1 
ATOM   342  C CZ  A TYR A 1 49  ? 11.410 40.242 4.090  0.50 60.81  ?  204 TYR A CZ  1 
ATOM   343  C CZ  B TYR A 1 49  ? 6.730  37.582 0.557  0.50 59.68  ?  204 TYR A CZ  1 
ATOM   344  O OH  A TYR A 1 49  ? 11.480 41.273 4.999  0.50 64.82  ?  204 TYR A OH  1 
ATOM   345  O OH  B TYR A 1 49  ? 5.395  37.745 0.268  0.50 59.66  ?  204 TYR A OH  1 
ATOM   346  N N   . VAL A 1 50  ? 10.505 33.367 1.368  1.00 54.67  ?  205 VAL A N   1 
ATOM   347  C CA  . VAL A 1 50  ? 10.043 32.193 0.609  1.00 55.94  ?  205 VAL A CA  1 
ATOM   348  C C   . VAL A 1 50  ? 8.510  32.116 0.639  1.00 64.81  ?  205 VAL A C   1 
ATOM   349  O O   . VAL A 1 50  ? 7.946  31.963 1.725  1.00 64.60  ?  205 VAL A O   1 
ATOM   350  C CB  . VAL A 1 50  ? 10.608 30.863 1.179  1.00 60.15  ?  205 VAL A CB  1 
ATOM   351  C CG1 . VAL A 1 50  ? 10.092 29.664 0.393  1.00 60.39  ?  205 VAL A CG1 1 
ATOM   352  C CG2 . VAL A 1 50  ? 12.119 30.855 1.217  1.00 60.19  ?  205 VAL A CG2 1 
ATOM   353  N N   . ASN A 1 51  ? 7.850  32.125 -0.554 1.00 64.35  ?  206 ASN A N   1 
ATOM   354  C CA  . ASN A 1 51  ? 6.407  31.941 -0.762 1.00 64.80  ?  206 ASN A CA  1 
ATOM   355  C C   . ASN A 1 51  ? 5.561  32.545 0.345  1.00 70.90  ?  206 ASN A C   1 
ATOM   356  O O   . ASN A 1 51  ? 4.994  31.817 1.170  1.00 72.77  ?  206 ASN A O   1 
ATOM   357  C CB  . ASN A 1 51  ? 6.091  30.440 -0.907 1.00 67.22  ?  206 ASN A CB  1 
ATOM   358  C CG  . ASN A 1 51  ? 4.704  30.109 -1.439 1.00 96.51  ?  206 ASN A CG  1 
ATOM   359  O OD1 . ASN A 1 51  ? 3.913  30.980 -1.854 1.00 88.78  ?  206 ASN A OD1 1 
ATOM   360  N ND2 . ASN A 1 51  ? 4.394  28.820 -1.467 1.00 88.22  ?  206 ASN A ND2 1 
ATOM   361  N N   . ASN A 1 52  ? 5.536  33.878 0.401  1.00 66.46  ?  207 ASN A N   1 
ATOM   362  C CA  . ASN A 1 52  ? 4.812  34.677 1.391  1.00 65.28  ?  207 ASN A CA  1 
ATOM   363  C C   . ASN A 1 52  ? 5.280  34.577 2.852  1.00 66.79  ?  207 ASN A C   1 
ATOM   364  O O   . ASN A 1 52  ? 4.781  35.320 3.695  1.00 68.97  ?  207 ASN A O   1 
ATOM   365  C CB  . ASN A 1 52  ? 3.298  34.560 1.210  1.00 67.90  ?  207 ASN A CB  1 
ATOM   366  C CG  . ASN A 1 52  ? 2.811  35.011 -0.162 1.00 84.48  ?  207 ASN A CG  1 
ATOM   367  O OD1 . ASN A 1 52  ? 1.817  34.306 -0.693 1.00 74.39  ?  207 ASN A OD1 1 
ATOM   368  N ND2 . ASN A 1 52  ? 3.297  36.001 -0.745 1.00 71.67  ?  207 ASN A ND2 1 
ATOM   369  N N   . THR A 1 53  ? 6.315  33.764 3.127  1.00 59.17  ?  208 THR A N   1 
ATOM   370  C CA  . THR A 1 53  ? 6.874  33.543 4.461  1.00 56.91  ?  208 THR A CA  1 
ATOM   371  C C   . THR A 1 53  ? 8.272  34.154 4.672  1.00 55.81  ?  208 THR A C   1 
ATOM   372  O O   . THR A 1 53  ? 9.206  33.762 3.960  1.00 54.61  ?  208 THR A O   1 
ATOM   373  C CB  . THR A 1 53  ? 6.988  32.018 4.729  1.00 68.72  ?  208 THR A CB  1 
ATOM   374  O OG1 . THR A 1 53  ? 6.051  31.264 3.952  1.00 72.55  ?  208 THR A OG1 1 
ATOM   375  C CG2 . THR A 1 53  ? 6.901  31.653 6.198  1.00 67.84  ?  208 THR A CG2 1 
ATOM   376  N N   . THR A 1 54  ? 8.448  35.051 5.698  1.00 48.63  ?  209 THR A N   1 
ATOM   377  C CA  . THR A 1 54  ? 9.800  35.481 6.093  1.00 46.10  ?  209 THR A CA  1 
ATOM   378  C C   . THR A 1 54  ? 10.442 34.266 6.800  1.00 47.88  ?  209 THR A C   1 
ATOM   379  O O   . THR A 1 54  ? 9.812  33.620 7.658  1.00 48.28  ?  209 THR A O   1 
ATOM   380  C CB  . THR A 1 54  ? 9.838  36.752 6.959  1.00 47.64  ?  209 THR A CB  1 
ATOM   381  O OG1 . THR A 1 54  ? 9.090  37.781 6.301  1.00 56.03  ?  209 THR A OG1 1 
ATOM   382  C CG2 . THR A 1 54  ? 11.260 37.245 7.192  1.00 37.99  ?  209 THR A CG2 1 
ATOM   383  N N   . VAL A 1 55  ? 11.675 33.929 6.395  1.00 42.30  ?  210 VAL A N   1 
ATOM   384  C CA  . VAL A 1 55  ? 12.415 32.783 6.915  1.00 41.21  ?  210 VAL A CA  1 
ATOM   385  C C   . VAL A 1 55  ? 13.831 33.109 7.323  1.00 44.49  ?  210 VAL A C   1 
ATOM   386  O O   . VAL A 1 55  ? 14.389 34.126 6.898  1.00 44.01  ?  210 VAL A O   1 
ATOM   387  C CB  . VAL A 1 55  ? 12.401 31.564 5.949  1.00 44.58  ?  210 VAL A CB  1 
ATOM   388  C CG1 . VAL A 1 55  ? 11.022 30.915 5.871  1.00 43.92  ?  210 VAL A CG1 1 
ATOM   389  C CG2 . VAL A 1 55  ? 12.932 31.935 4.564  1.00 44.21  ?  210 VAL A CG2 1 
ATOM   390  N N   . ALA A 1 56  ? 14.432 32.198 8.128  1.00 39.85  ?  211 ALA A N   1 
ATOM   391  C CA  . ALA A 1 56  ? 15.830 32.262 8.550  1.00 37.59  ?  211 ALA A CA  1 
ATOM   392  C C   . ALA A 1 56  ? 16.564 31.112 7.843  1.00 41.45  ?  211 ALA A C   1 
ATOM   393  O O   . ALA A 1 56  ? 16.189 29.945 8.006  1.00 42.78  ?  211 ALA A O   1 
ATOM   394  C CB  . ALA A 1 56  ? 15.939 32.140 10.053 1.00 37.39  ?  211 ALA A CB  1 
ATOM   395  N N   . VAL A 1 57  ? 17.542 31.451 6.987  1.00 35.37  ?  212 VAL A N   1 
ATOM   396  C CA  . VAL A 1 57  ? 18.291 30.468 6.219  1.00 34.37  ?  212 VAL A CA  1 
ATOM   397  C C   . VAL A 1 57  ? 19.685 30.347 6.824  1.00 39.50  ?  212 VAL A C   1 
ATOM   398  O O   . VAL A 1 57  ? 20.471 31.287 6.757  1.00 39.57  ?  212 VAL A O   1 
ATOM   399  C CB  . VAL A 1 57  ? 18.352 30.794 4.689  1.00 37.84  ?  212 VAL A CB  1 
ATOM   400  C CG1 . VAL A 1 57  ? 18.982 29.651 3.892  1.00 36.99  ?  212 VAL A CG1 1 
ATOM   401  C CG2 . VAL A 1 57  ? 16.982 31.153 4.115  1.00 37.06  ?  212 VAL A CG2 1 
ATOM   402  N N   . LYS A 1 58  ? 19.995 29.192 7.425  1.00 37.44  ?  213 LYS A N   1 
ATOM   403  C CA  . LYS A 1 58  ? 21.326 28.958 7.966  1.00 36.69  ?  213 LYS A CA  1 
ATOM   404  C C   . LYS A 1 58  ? 22.143 28.185 6.909  1.00 40.47  ?  213 LYS A C   1 
ATOM   405  O O   . LYS A 1 58  ? 21.808 27.045 6.577  1.00 36.41  ?  213 LYS A O   1 
ATOM   406  C CB  . LYS A 1 58  ? 21.293 28.225 9.326  1.00 37.64  ?  213 LYS A CB  1 
ATOM   407  C CG  . LYS A 1 58  ? 22.728 28.008 9.871  1.00 36.01  ?  213 LYS A CG  1 
ATOM   408  C CD  . LYS A 1 58  ? 22.815 27.445 11.287 1.00 48.02  ?  213 LYS A CD  1 
ATOM   409  C CE  . LYS A 1 58  ? 22.178 26.078 11.419 1.00 72.99  ?  213 LYS A CE  1 
ATOM   410  N NZ  . LYS A 1 58  ? 22.220 25.565 12.817 1.00 84.95  1  213 LYS A NZ  1 
ATOM   411  N N   . LYS A 1 59  ? 23.178 28.841 6.351  1.00 39.74  ?  214 LYS A N   1 
ATOM   412  C CA  . LYS A 1 59  ? 24.064 28.235 5.373  1.00 40.57  ?  214 LYS A CA  1 
ATOM   413  C C   . LYS A 1 59  ? 25.358 27.825 6.091  1.00 48.69  ?  214 LYS A C   1 
ATOM   414  O O   . LYS A 1 59  ? 26.186 28.683 6.446  1.00 47.64  ?  214 LYS A O   1 
ATOM   415  C CB  . LYS A 1 59  ? 24.317 29.178 4.185  1.00 41.87  ?  214 LYS A CB  1 
ATOM   416  C CG  . LYS A 1 59  ? 25.282 28.628 3.129  1.00 38.02  ?  214 LYS A CG  1 
ATOM   417  C CD  . LYS A 1 59  ? 25.225 29.404 1.832  1.00 39.57  ?  214 LYS A CD  1 
ATOM   418  C CE  . LYS A 1 59  ? 26.278 30.471 1.755  1.00 58.49  ?  214 LYS A CE  1 
ATOM   419  N NZ  . LYS A 1 59  ? 27.529 29.963 1.135  1.00 70.00  1  214 LYS A NZ  1 
ATOM   420  N N   . LEU A 1 60  ? 25.504 26.496 6.320  1.00 47.96  ?  215 LEU A N   1 
ATOM   421  C CA  . LEU A 1 60  ? 26.649 25.843 6.975  1.00 48.83  ?  215 LEU A CA  1 
ATOM   422  C C   . LEU A 1 60  ? 27.972 26.276 6.330  1.00 55.60  ?  215 LEU A C   1 
ATOM   423  O O   . LEU A 1 60  ? 28.025 26.427 5.109  1.00 54.87  ?  215 LEU A O   1 
ATOM   424  C CB  . LEU A 1 60  ? 26.505 24.309 6.851  1.00 49.08  ?  215 LEU A CB  1 
ATOM   425  C CG  . LEU A 1 60  ? 25.657 23.483 7.875  1.00 52.93  ?  215 LEU A CG  1 
ATOM   426  C CD1 . LEU A 1 60  ? 26.501 22.934 8.986  1.00 53.14  ?  215 LEU A CD1 1 
ATOM   427  C CD2 . LEU A 1 60  ? 24.393 24.192 8.360  1.00 53.81  ?  215 LEU A CD2 1 
ATOM   428  N N   . ALA A 1 61  ? 29.014 26.543 7.143  1.00 55.59  ?  216 ALA A N   1 
ATOM   429  C CA  . ALA A 1 61  ? 30.331 26.959 6.639  1.00 57.90  ?  216 ALA A CA  1 
ATOM   430  C C   . ALA A 1 61  ? 31.417 26.915 7.697  1.00 69.46  ?  216 ALA A C   1 
ATOM   431  O O   . ALA A 1 61  ? 31.163 27.211 8.874  1.00 70.29  ?  216 ALA A O   1 
ATOM   432  C CB  . ALA A 1 61  ? 30.275 28.353 6.028  1.00 58.45  ?  216 ALA A CB  1 
ATOM   433  N N   . ALA A 1 62  ? 32.648 26.603 7.257  1.00 69.30  ?  217 ALA A N   1 
ATOM   434  C CA  . ALA A 1 62  ? 33.819 26.543 8.119  1.00 70.27  ?  217 ALA A CA  1 
ATOM   435  C C   . ALA A 1 62  ? 34.269 27.954 8.495  1.00 77.03  ?  217 ALA A C   1 
ATOM   436  O O   . ALA A 1 62  ? 34.741 28.717 7.636  1.00 77.69  ?  217 ALA A O   1 
ATOM   437  C CB  . ALA A 1 62  ? 34.936 25.776 7.435  1.00 70.95  ?  217 ALA A CB  1 
ATOM   438  N N   . MET A 1 63  ? 34.045 28.322 9.776  1.00 73.65  ?  218 MET A N   1 
ATOM   439  C CA  . MET A 1 63  ? 34.419 29.632 10.335 1.00 72.89  ?  218 MET A CA  1 
ATOM   440  C C   . MET A 1 63  ? 35.387 29.452 11.523 1.00 100.85 ?  218 MET A C   1 
ATOM   441  O O   . MET A 1 63  ? 35.694 28.325 11.933 1.00 64.22  ?  218 MET A O   1 
ATOM   442  C CB  . MET A 1 63  ? 33.180 30.448 10.766 1.00 74.63  ?  218 MET A CB  1 
ATOM   443  C CG  . MET A 1 63  ? 32.007 30.391 9.796  1.00 77.20  ?  218 MET A CG  1 
ATOM   444  S SD  . MET A 1 63  ? 31.506 31.996 9.140  1.00 80.11  ?  218 MET A SD  1 
ATOM   445  C CE  . MET A 1 63  ? 31.617 31.672 7.400  1.00 76.58  ?  218 MET A CE  1 
ATOM   446  N N   . ILE A 1 66  ? 37.601 26.519 11.408 1.00 71.07  ?  221 ILE A N   1 
ATOM   447  C CA  . ILE A 1 66  ? 38.272 25.281 11.013 1.00 70.96  ?  221 ILE A CA  1 
ATOM   448  C C   . ILE A 1 66  ? 37.504 24.029 11.444 1.00 73.69  ?  221 ILE A C   1 
ATOM   449  O O   . ILE A 1 66  ? 37.541 23.614 12.608 1.00 72.36  ?  221 ILE A O   1 
ATOM   450  C CB  . ILE A 1 66  ? 39.785 25.244 11.370 1.00 74.28  ?  221 ILE A CB  1 
ATOM   451  N N   . THR A 1 67  ? 36.761 23.479 10.472 1.00 70.31  ?  222 THR A N   1 
ATOM   452  C CA  . THR A 1 67  ? 35.920 22.281 10.510 1.00 70.38  ?  222 THR A CA  1 
ATOM   453  C C   . THR A 1 67  ? 35.980 21.711 9.068  1.00 74.73  ?  222 THR A C   1 
ATOM   454  O O   . THR A 1 67  ? 36.057 22.500 8.103  1.00 73.74  ?  222 THR A O   1 
ATOM   455  C CB  . THR A 1 67  ? 34.477 22.618 11.054 1.00 77.80  ?  222 THR A CB  1 
ATOM   456  O OG1 . THR A 1 67  ? 33.734 21.433 11.397 1.00 72.12  ?  222 THR A OG1 1 
ATOM   457  C CG2 . THR A 1 67  ? 33.653 23.492 10.102 1.00 77.12  ?  222 THR A CG2 1 
ATOM   458  N N   . THR A 1 68  ? 35.885 20.398 8.907  1.00 71.35  ?  223 THR A N   1 
ATOM   459  C CA  . THR A 1 68  ? 35.960 19.792 7.590  1.00 71.81  ?  223 THR A CA  1 
ATOM   460  C C   . THR A 1 68  ? 34.643 19.515 6.899  1.00 76.87  ?  223 THR A C   1 
ATOM   461  O O   . THR A 1 68  ? 34.362 20.062 5.849  1.00 76.19  ?  223 THR A O   1 
ATOM   462  C CB  . THR A 1 68  ? 36.698 18.458 7.654  1.00 81.75  ?  223 THR A CB  1 
ATOM   463  O OG1 . THR A 1 68  ? 35.770 17.407 7.922  1.00 80.81  ?  223 THR A OG1 1 
ATOM   464  C CG2 . THR A 1 68  ? 37.693 18.486 8.744  1.00 80.65  ?  223 THR A CG2 1 
ATOM   465  N N   . GLU A 1 69  ? 33.865 18.607 7.467  1.00 74.24  ?  224 GLU A N   1 
ATOM   466  C CA  . GLU A 1 69  ? 32.670 18.125 6.816  1.00 73.24  ?  224 GLU A CA  1 
ATOM   467  C C   . GLU A 1 69  ? 32.391 16.701 7.126  1.00 75.75  ?  224 GLU A C   1 
ATOM   468  O O   . GLU A 1 69  ? 32.343 15.930 6.198  1.00 76.60  ?  224 GLU A O   1 
ATOM   469  C CB  . GLU A 1 69  ? 32.900 18.123 5.328  1.00 74.30  ?  224 GLU A CB  1 
ATOM   470  C CG  . GLU A 1 69  ? 32.511 19.400 4.663  1.00 82.52  ?  224 GLU A CG  1 
ATOM   471  C CD  . GLU A 1 69  ? 33.498 19.783 3.619  1.00 102.09 ?  224 GLU A CD  1 
ATOM   472  O OE1 . GLU A 1 69  ? 33.692 18.979 2.705  1.00 75.60  ?  224 GLU A OE1 1 
ATOM   473  O OE2 . GLU A 1 69  ? 34.070 20.870 3.717  1.00 103.73 -1 224 GLU A OE2 1 
ATOM   474  N N   . GLU A 1 70  ? 32.243 16.280 8.371  1.00 69.51  ?  225 GLU A N   1 
ATOM   475  C CA  . GLU A 1 70  ? 32.097 17.038 9.634  1.00 68.39  ?  225 GLU A CA  1 
ATOM   476  C C   . GLU A 1 70  ? 30.924 18.014 9.702  1.00 70.50  ?  225 GLU A C   1 
ATOM   477  O O   . GLU A 1 70  ? 30.097 17.921 10.608 1.00 69.97  ?  225 GLU A O   1 
ATOM   478  C CB  . GLU A 1 70  ? 33.404 17.629 10.165 1.00 69.69  ?  225 GLU A CB  1 
ATOM   479  N N   . LEU A 1 71  ? 30.853 18.931 8.728  1.00 65.28  ?  226 LEU A N   1 
ATOM   480  C CA  . LEU A 1 71  ? 29.768 19.882 8.536  1.00 64.30  ?  226 LEU A CA  1 
ATOM   481  C C   . LEU A 1 71  ? 28.506 19.122 8.129  1.00 66.17  ?  226 LEU A C   1 
ATOM   482  O O   . LEU A 1 71  ? 27.450 19.356 8.719  1.00 66.97  ?  226 LEU A O   1 
ATOM   483  C CB  . LEU A 1 71  ? 30.152 20.917 7.456  1.00 64.49  ?  226 LEU A CB  1 
ATOM   484  C CG  . LEU A 1 71  ? 30.080 22.419 7.814  1.00 69.19  ?  226 LEU A CG  1 
ATOM   485  C CD1 . LEU A 1 71  ? 30.182 22.682 9.327  1.00 69.81  ?  226 LEU A CD1 1 
ATOM   486  C CD2 . LEU A 1 71  ? 31.114 23.213 7.057  1.00 70.29  ?  226 LEU A CD2 1 
ATOM   487  N N   . LYS A 1 72  ? 28.632 18.166 7.169  1.00 60.16  ?  227 LYS A N   1 
ATOM   488  C CA  . LYS A 1 72  ? 27.535 17.305 6.701  1.00 57.99  ?  227 LYS A CA  1 
ATOM   489  C C   . LYS A 1 72  ? 27.011 16.403 7.822  1.00 60.64  ?  227 LYS A C   1 
ATOM   490  O O   . LYS A 1 72  ? 25.823 16.097 7.839  1.00 60.13  ?  227 LYS A O   1 
ATOM   491  C CB  . LYS A 1 72  ? 27.947 16.491 5.470  1.00 58.48  ?  227 LYS A CB  1 
ATOM   492  N N   . GLN A 1 73  ? 27.886 16.013 8.775  1.00 57.66  ?  228 GLN A N   1 
ATOM   493  C CA  . GLN A 1 73  ? 27.529 15.191 9.944  1.00 58.82  ?  228 GLN A CA  1 
ATOM   494  C C   . GLN A 1 73  ? 26.552 15.963 10.831 1.00 63.65  ?  228 GLN A C   1 
ATOM   495  O O   . GLN A 1 73  ? 25.575 15.389 11.312 1.00 62.44  ?  228 GLN A O   1 
ATOM   496  C CB  . GLN A 1 73  ? 28.777 14.805 10.768 1.00 60.54  ?  228 GLN A CB  1 
ATOM   497  N N   . GLN A 1 74  ? 26.813 17.281 11.016 1.00 60.68  ?  229 GLN A N   1 
ATOM   498  C CA  . GLN A 1 74  ? 25.983 18.205 11.790 1.00 59.40  ?  229 GLN A CA  1 
ATOM   499  C C   . GLN A 1 74  ? 24.655 18.467 11.064 1.00 62.88  ?  229 GLN A C   1 
ATOM   500  O O   . GLN A 1 74  ? 23.628 18.684 11.721 1.00 63.25  ?  229 GLN A O   1 
ATOM   501  C CB  . GLN A 1 74  ? 26.720 19.527 11.992 1.00 60.09  ?  229 GLN A CB  1 
ATOM   502  C CG  . GLN A 1 74  ? 27.824 19.507 13.033 1.00 59.38  ?  229 GLN A CG  1 
ATOM   503  C CD  . GLN A 1 74  ? 28.490 20.858 13.102 1.00 69.42  ?  229 GLN A CD  1 
ATOM   504  O OE1 . GLN A 1 74  ? 27.744 21.935 12.817 1.00 55.72  ?  229 GLN A OE1 1 
ATOM   505  N NE2 . GLN A 1 74  ? 29.674 20.960 13.400 1.00 68.46  ?  229 GLN A NE2 1 
ATOM   506  N N   . PHE A 1 75  ? 24.686 18.470 9.705  1.00 57.48  ?  230 PHE A N   1 
ATOM   507  C CA  . PHE A 1 75  ? 23.516 18.687 8.858  1.00 56.94  ?  230 PHE A CA  1 
ATOM   508  C C   . PHE A 1 75  ? 22.509 17.550 9.041  1.00 60.13  ?  230 PHE A C   1 
ATOM   509  O O   . PHE A 1 75  ? 21.334 17.809 9.315  1.00 59.81  ?  230 PHE A O   1 
ATOM   510  C CB  . PHE A 1 75  ? 23.935 18.836 7.395  1.00 58.80  ?  230 PHE A CB  1 
ATOM   511  C CG  . PHE A 1 75  ? 22.822 19.144 6.420  1.00 60.59  ?  230 PHE A CG  1 
ATOM   512  C CD1 . PHE A 1 75  ? 22.330 20.440 6.287  1.00 63.54  ?  230 PHE A CD1 1 
ATOM   513  C CD2 . PHE A 1 75  ? 22.313 18.153 5.587  1.00 62.67  ?  230 PHE A CD2 1 
ATOM   514  C CE1 . PHE A 1 75  ? 21.317 20.728 5.374  1.00 64.67  ?  230 PHE A CE1 1 
ATOM   515  C CE2 . PHE A 1 75  ? 21.318 18.449 4.652  1.00 65.59  ?  230 PHE A CE2 1 
ATOM   516  C CZ  . PHE A 1 75  ? 20.822 19.732 4.557  1.00 64.00  ?  230 PHE A CZ  1 
ATOM   517  N N   . ASP A 1 76  ? 22.990 16.297 8.957  1.00 55.66  ?  231 ASP A N   1 
ATOM   518  C CA  . ASP A 1 76  ? 22.200 15.076 9.148  1.00 54.53  ?  231 ASP A CA  1 
ATOM   519  C C   . ASP A 1 76  ? 21.673 14.987 10.572 1.00 56.65  ?  231 ASP A C   1 
ATOM   520  O O   . ASP A 1 76  ? 20.549 14.535 10.788 1.00 56.39  ?  231 ASP A O   1 
ATOM   521  C CB  . ASP A 1 76  ? 23.051 13.842 8.795  1.00 56.10  ?  231 ASP A CB  1 
ATOM   522  C CG  . ASP A 1 76  ? 23.606 13.863 7.376  1.00 68.10  ?  231 ASP A CG  1 
ATOM   523  O OD1 . ASP A 1 76  ? 23.291 14.815 6.624  1.00 67.78  ?  231 ASP A OD1 1 
ATOM   524  O OD2 . ASP A 1 76  ? 24.388 12.960 7.035  1.00 80.94  -1 231 ASP A OD2 1 
ATOM   525  N N   . GLN A 1 77  ? 22.469 15.470 11.532 1.00 52.67  ?  232 GLN A N   1 
ATOM   526  C CA  . GLN A 1 77  ? 22.133 15.493 12.949 1.00 52.42  ?  232 GLN A CA  1 
ATOM   527  C C   . GLN A 1 77  ? 21.061 16.535 13.242 1.00 57.71  ?  232 GLN A C   1 
ATOM   528  O O   . GLN A 1 77  ? 20.124 16.237 13.986 1.00 58.32  ?  232 GLN A O   1 
ATOM   529  C CB  . GLN A 1 77  ? 23.393 15.707 13.810 1.00 53.21  ?  232 GLN A CB  1 
ATOM   530  C CG  . GLN A 1 77  ? 23.217 15.440 15.311 1.00 59.18  ?  232 GLN A CG  1 
ATOM   531  C CD  . GLN A 1 77  ? 22.753 14.055 15.710 1.00 72.05  ?  232 GLN A CD  1 
ATOM   532  O OE1 . GLN A 1 77  ? 22.983 13.036 14.880 1.00 63.95  ?  232 GLN A OE1 1 
ATOM   533  N NE2 . GLN A 1 77  ? 22.191 13.874 16.787 1.00 69.89  ?  232 GLN A NE2 1 
ATOM   534  N N   . GLU A 1 78  ? 21.175 17.742 12.643 1.00 53.89  ?  233 GLU A N   1 
ATOM   535  C CA  . GLU A 1 78  ? 20.181 18.808 12.833 1.00 53.45  ?  233 GLU A CA  1 
ATOM   536  C C   . GLU A 1 78  ? 18.800 18.331 12.364 1.00 56.10  ?  233 GLU A C   1 
ATOM   537  O O   . GLU A 1 78  ? 17.848 18.425 13.135 1.00 55.15  ?  233 GLU A O   1 
ATOM   538  C CB  . GLU A 1 78  ? 20.609 20.129 12.154 1.00 54.69  ?  233 GLU A CB  1 
ATOM   539  C CG  . GLU A 1 78  ? 19.744 21.342 12.478 1.00 60.94  ?  233 GLU A CG  1 
ATOM   540  C CD  . GLU A 1 78  ? 20.229 22.337 13.521 1.00 84.89  ?  233 GLU A CD  1 
ATOM   541  O OE1 . GLU A 1 78  ? 21.281 22.988 13.306 1.00 64.22  ?  233 GLU A OE1 1 
ATOM   542  O OE2 . GLU A 1 78  ? 19.468 22.567 14.487 1.00 89.52  -1 233 GLU A OE2 1 
ATOM   543  N N   . ILE A 1 79  ? 18.719 17.729 11.155 1.00 52.57  ?  234 ILE A N   1 
ATOM   544  C CA  . ILE A 1 79  ? 17.468 17.199 10.595 1.00 52.27  ?  234 ILE A CA  1 
ATOM   545  C C   . ILE A 1 79  ? 16.900 16.050 11.448 1.00 57.59  ?  234 ILE A C   1 
ATOM   546  O O   . ILE A 1 79  ? 15.703 16.061 11.742 1.00 55.85  ?  234 ILE A O   1 
ATOM   547  C CB  . ILE A 1 79  ? 17.602 16.831 9.091  1.00 54.72  ?  234 ILE A CB  1 
ATOM   548  C CG1 . ILE A 1 79  ? 18.060 18.057 8.263  1.00 54.14  ?  234 ILE A CG1 1 
ATOM   549  C CG2 . ILE A 1 79  ? 16.271 16.258 8.549  1.00 55.79  ?  234 ILE A CG2 1 
ATOM   550  C CD1 . ILE A 1 79  ? 18.626 17.748 6.921  1.00 52.88  ?  234 ILE A CD1 1 
ATOM   551  N N   . LYS A 1 80  ? 17.772 15.081 11.855 1.00 56.22  ?  235 LYS A N   1 
ATOM   552  C CA  . LYS A 1 80  ? 17.421 13.921 12.683 1.00 55.94  ?  235 LYS A CA  1 
ATOM   553  C C   . LYS A 1 80  ? 16.791 14.324 14.022 1.00 58.95  ?  235 LYS A C   1 
ATOM   554  O O   . LYS A 1 80  ? 15.798 13.710 14.432 1.00 60.90  ?  235 LYS A O   1 
ATOM   555  C CB  . LYS A 1 80  ? 18.647 13.024 12.916 1.00 58.95  ?  235 LYS A CB  1 
ATOM   556  N N   . VAL A 1 81  ? 17.338 15.356 14.683 1.00 52.32  ?  236 VAL A N   1 
ATOM   557  C CA  . VAL A 1 81  ? 16.802 15.824 15.965 1.00 52.41  ?  236 VAL A CA  1 
ATOM   558  C C   . VAL A 1 81  ? 15.514 16.637 15.747 1.00 58.13  ?  236 VAL A C   1 
ATOM   559  O O   . VAL A 1 81  ? 14.582 16.546 16.550 1.00 56.27  ?  236 VAL A O   1 
ATOM   560  C CB  . VAL A 1 81  ? 17.843 16.601 16.816 1.00 55.79  ?  236 VAL A CB  1 
ATOM   561  C CG1 . VAL A 1 81  ? 17.320 16.835 18.233 1.00 55.30  ?  236 VAL A CG1 1 
ATOM   562  C CG2 . VAL A 1 81  ? 19.188 15.869 16.872 1.00 55.40  ?  236 VAL A CG2 1 
ATOM   563  N N   . MET A 1 82  ? 15.478 17.429 14.652 1.00 56.86  ?  237 MET A N   1 
ATOM   564  C CA  . MET A 1 82  ? 14.356 18.279 14.255 1.00 57.03  ?  237 MET A CA  1 
ATOM   565  C C   . MET A 1 82  ? 13.115 17.469 13.924 1.00 60.61  ?  237 MET A C   1 
ATOM   566  O O   . MET A 1 82  ? 12.003 17.930 14.191 1.00 61.04  ?  237 MET A O   1 
ATOM   567  C CB  . MET A 1 82  ? 14.750 19.105 13.037 1.00 59.98  ?  237 MET A CB  1 
ATOM   568  C CG  . MET A 1 82  ? 14.632 20.557 13.230 1.00 64.38  ?  237 MET A CG  1 
ATOM   569  S SD  . MET A 1 82  ? 15.741 21.270 14.442 1.00 68.59  ?  237 MET A SD  1 
ATOM   570  C CE  . MET A 1 82  ? 14.494 21.838 15.642 1.00 64.45  ?  237 MET A CE  1 
ATOM   571  N N   . ALA A 1 83  ? 13.306 16.268 13.337 1.00 56.59  ?  238 ALA A N   1 
ATOM   572  C CA  . ALA A 1 83  ? 12.239 15.349 12.958 1.00 56.40  ?  238 ALA A CA  1 
ATOM   573  C C   . ALA A 1 83  ? 11.565 14.742 14.188 1.00 63.58  ?  238 ALA A C   1 
ATOM   574  O O   . ALA A 1 83  ? 10.349 14.542 14.177 1.00 64.67  ?  238 ALA A O   1 
ATOM   575  C CB  . ALA A 1 83  ? 12.793 14.251 12.081 1.00 56.74  ?  238 ALA A CB  1 
ATOM   576  N N   . LYS A 1 84  ? 12.346 14.458 15.241 1.00 60.26  ?  239 LYS A N   1 
ATOM   577  C CA  . LYS A 1 84  ? 11.845 13.859 16.470 1.00 60.16  ?  239 LYS A CA  1 
ATOM   578  C C   . LYS A 1 84  ? 11.464 14.883 17.536 1.00 66.36  ?  239 LYS A C   1 
ATOM   579  O O   . LYS A 1 84  ? 10.559 14.607 18.329 1.00 67.44  ?  239 LYS A O   1 
ATOM   580  C CB  . LYS A 1 84  ? 12.847 12.831 17.020 1.00 61.95  ?  239 LYS A CB  1 
ATOM   581  N N   . CYS A 1 85  ? 12.135 16.054 17.566 1.00 63.24  ?  240 CYS A N   1 
ATOM   582  C CA  . CYS A 1 85  ? 11.877 17.090 18.575 1.00 63.24  ?  240 CYS A CA  1 
ATOM   583  C C   . CYS A 1 85  ? 11.202 18.368 18.052 1.00 63.87  ?  240 CYS A C   1 
ATOM   584  O O   . CYS A 1 85  ? 11.878 19.259 17.518 1.00 64.17  ?  240 CYS A O   1 
ATOM   585  C CB  . CYS A 1 85  ? 13.136 17.413 19.376 1.00 64.29  ?  240 CYS A CB  1 
ATOM   586  S SG  . CYS A 1 85  ? 13.844 16.000 20.261 1.00 68.46  ?  240 CYS A SG  1 
ATOM   587  N N   . GLN A 1 86  ? 9.864  18.448 18.214 1.00 55.84  ?  241 GLN A N   1 
ATOM   588  C CA  . GLN A 1 86  ? 9.050  19.612 17.862 1.00 53.41  ?  241 GLN A CA  1 
ATOM   589  C C   . GLN A 1 86  ? 8.337  20.007 19.143 1.00 53.22  ?  241 GLN A C   1 
ATOM   590  O O   . GLN A 1 86  ? 7.752  19.148 19.793 1.00 52.78  ?  241 GLN A O   1 
ATOM   591  C CB  . GLN A 1 86  ? 8.051  19.291 16.755 1.00 55.00  ?  241 GLN A CB  1 
ATOM   592  C CG  . GLN A 1 86  ? 8.661  19.186 15.362 1.00 75.08  ?  241 GLN A CG  1 
ATOM   593  C CD  . GLN A 1 86  ? 8.817  17.763 14.893 1.00 96.55  ?  241 GLN A CD  1 
ATOM   594  O OE1 . GLN A 1 86  ? 8.974  16.820 15.684 1.00 97.70  ?  241 GLN A OE1 1 
ATOM   595  N NE2 . GLN A 1 86  ? 8.794  17.580 13.584 1.00 82.58  ?  241 GLN A NE2 1 
ATOM   596  N N   . HIS A 1 87  ? 8.453  21.282 19.556 1.00 46.99  ?  242 HIS A N   1 
ATOM   597  C CA  . HIS A 1 87  ? 7.906  21.789 20.818 1.00 44.87  ?  242 HIS A CA  1 
ATOM   598  C C   . HIS A 1 87  ? 7.792  23.308 20.808 1.00 46.80  ?  242 HIS A C   1 
ATOM   599  O O   . HIS A 1 87  ? 8.513  23.966 20.075 1.00 47.26  ?  242 HIS A O   1 
ATOM   600  C CB  . HIS A 1 87  ? 8.821  21.325 21.971 1.00 45.16  ?  242 HIS A CB  1 
ATOM   601  C CG  . HIS A 1 87  ? 8.333  21.647 23.349 1.00 47.96  ?  242 HIS A CG  1 
ATOM   602  N ND1 . HIS A 1 87  ? 8.754  22.794 24.019 1.00 49.67  ?  242 HIS A ND1 1 
ATOM   603  C CD2 . HIS A 1 87  ? 7.512  20.948 24.157 1.00 48.40  ?  242 HIS A CD2 1 
ATOM   604  C CE1 . HIS A 1 87  ? 8.164  22.755 25.200 1.00 48.42  ?  242 HIS A CE1 1 
ATOM   605  N NE2 . HIS A 1 87  ? 7.408  21.663 25.329 1.00 48.33  ?  242 HIS A NE2 1 
ATOM   606  N N   . GLU A 1 88  ? 6.911  23.853 21.656 1.00 43.43  ?  243 GLU A N   1 
ATOM   607  C CA  . GLU A 1 88  ? 6.607  25.281 21.872 1.00 44.14  ?  243 GLU A CA  1 
ATOM   608  C C   . GLU A 1 88  ? 7.885  26.111 22.198 1.00 48.69  ?  243 GLU A C   1 
ATOM   609  O O   . GLU A 1 88  ? 7.950  27.305 21.861 1.00 48.14  ?  243 GLU A O   1 
ATOM   610  C CB  . GLU A 1 88  ? 5.599  25.378 23.048 1.00 45.69  ?  243 GLU A CB  1 
ATOM   611  C CG  . GLU A 1 88  ? 5.103  26.768 23.429 1.00 54.87  ?  243 GLU A CG  1 
ATOM   612  C CD  . GLU A 1 88  ? 4.454  26.857 24.801 1.00 83.67  ?  243 GLU A CD  1 
ATOM   613  O OE1 . GLU A 1 88  ? 4.605  25.907 25.610 1.00 67.38  ?  243 GLU A OE1 1 
ATOM   614  O OE2 . GLU A 1 88  ? 3.818  27.901 25.078 1.00 83.61  -1 243 GLU A OE2 1 
ATOM   615  N N   . ASN A 1 89  ? 8.873  25.481 22.883 1.00 43.46  ?  244 ASN A N   1 
ATOM   616  C CA  . ASN A 1 89  ? 10.100 26.161 23.253 1.00 43.16  ?  244 ASN A CA  1 
ATOM   617  C C   . ASN A 1 89  ? 11.322 25.704 22.467 1.00 46.61  ?  244 ASN A C   1 
ATOM   618  O O   . ASN A 1 89  ? 12.452 25.785 22.960 1.00 44.96  ?  244 ASN A O   1 
ATOM   619  C CB  . ASN A 1 89  ? 10.320 26.180 24.761 1.00 43.48  ?  244 ASN A CB  1 
ATOM   620  C CG  . ASN A 1 89  ? 9.224  26.868 25.548 1.00 56.68  ?  244 ASN A CG  1 
ATOM   621  O OD1 . ASN A 1 89  ? 8.563  26.266 26.382 1.00 56.85  ?  244 ASN A OD1 1 
ATOM   622  N ND2 . ASN A 1 89  ? 9.021  28.144 25.330 1.00 49.59  ?  244 ASN A ND2 1 
ATOM   623  N N   . LEU A 1 90  ? 11.088 25.270 21.215 1.00 42.41  ?  245 LEU A N   1 
ATOM   624  C CA  . LEU A 1 90  ? 12.158 24.906 20.293 1.00 43.01  ?  245 LEU A CA  1 
ATOM   625  C C   . LEU A 1 90  ? 11.844 25.537 18.955 1.00 47.04  ?  245 LEU A C   1 
ATOM   626  O O   . LEU A 1 90  ? 10.680 25.624 18.598 1.00 48.12  ?  245 LEU A O   1 
ATOM   627  C CB  . LEU A 1 90  ? 12.294 23.369 20.084 1.00 43.22  ?  245 LEU A CB  1 
ATOM   628  C CG  . LEU A 1 90  ? 12.398 22.406 21.272 1.00 46.75  ?  245 LEU A CG  1 
ATOM   629  C CD1 . LEU A 1 90  ? 12.509 20.990 20.779 1.00 47.05  ?  245 LEU A CD1 1 
ATOM   630  C CD2 . LEU A 1 90  ? 13.594 22.699 22.126 1.00 46.79  ?  245 LEU A CD2 1 
ATOM   631  N N   . VAL A 1 91  ? 12.865 25.918 18.189 1.00 43.61  ?  246 VAL A N   1 
ATOM   632  C CA  . VAL A 1 91  ? 12.713 26.445 16.826 1.00 43.22  ?  246 VAL A CA  1 
ATOM   633  C C   . VAL A 1 91  ? 12.079 25.364 15.943 1.00 45.61  ?  246 VAL A C   1 
ATOM   634  O O   . VAL A 1 91  ? 12.154 24.169 16.260 1.00 44.32  ?  246 VAL A O   1 
ATOM   635  C CB  . VAL A 1 91  ? 14.034 26.956 16.167 1.00 46.96  ?  246 VAL A CB  1 
ATOM   636  C CG1 . VAL A 1 91  ? 14.485 28.283 16.752 1.00 46.85  ?  246 VAL A CG1 1 
ATOM   637  C CG2 . VAL A 1 91  ? 15.149 25.913 16.210 1.00 46.15  ?  246 VAL A CG2 1 
ATOM   638  N N   . GLU A 1 92  ? 11.472 25.800 14.835 1.00 41.24  ?  247 GLU A N   1 
ATOM   639  C CA  . GLU A 1 92  ? 10.819 24.919 13.891 1.00 40.54  ?  247 GLU A CA  1 
ATOM   640  C C   . GLU A 1 92  ? 11.537 25.001 12.535 1.00 46.44  ?  247 GLU A C   1 
ATOM   641  O O   . GLU A 1 92  ? 11.714 26.097 11.999 1.00 49.20  ?  247 GLU A O   1 
ATOM   642  C CB  . GLU A 1 92  ? 9.351  25.327 13.799 1.00 41.23  ?  247 GLU A CB  1 
ATOM   643  C CG  . GLU A 1 92  ? 8.511  24.538 12.823 1.00 48.91  ?  247 GLU A CG  1 
ATOM   644  C CD  . GLU A 1 92  ? 7.173  25.196 12.580 1.00 71.29  ?  247 GLU A CD  1 
ATOM   645  O OE1 . GLU A 1 92  ? 6.467  24.767 11.639 1.00 85.06  ?  247 GLU A OE1 1 
ATOM   646  O OE2 . GLU A 1 92  ? 6.848  26.170 13.299 1.00 61.02  -1 247 GLU A OE2 1 
ATOM   647  N N   . LEU A 1 93  ? 11.992 23.850 12.025 1.00 40.74  ?  248 LEU A N   1 
ATOM   648  C CA  . LEU A 1 93  ? 12.649 23.700 10.722 1.00 40.16  ?  248 LEU A CA  1 
ATOM   649  C C   . LEU A 1 93  ? 11.572 23.528 9.639  1.00 43.02  ?  248 LEU A C   1 
ATOM   650  O O   . LEU A 1 93  ? 10.638 22.743 9.785  1.00 43.63  ?  248 LEU A O   1 
ATOM   651  C CB  . LEU A 1 93  ? 13.569 22.474 10.741 1.00 40.15  ?  248 LEU A CB  1 
ATOM   652  C CG  . LEU A 1 93  ? 14.490 22.212 9.550  1.00 43.62  ?  248 LEU A CG  1 
ATOM   653  C CD1 . LEU A 1 93  ? 15.681 23.153 9.559  1.00 42.52  ?  248 LEU A CD1 1 
ATOM   654  C CD2 . LEU A 1 93  ? 14.997 20.793 9.609  1.00 44.66  ?  248 LEU A CD2 1 
ATOM   655  N N   . LEU A 1 94  ? 11.675 24.298 8.582  1.00 37.79  ?  249 LEU A N   1 
ATOM   656  C CA  . LEU A 1 94  ? 10.686 24.223 7.527  1.00 36.40  ?  249 LEU A CA  1 
ATOM   657  C C   . LEU A 1 94  ? 11.240 23.399 6.383  1.00 43.15  ?  249 LEU A C   1 
ATOM   658  O O   . LEU A 1 94  ? 10.481 22.672 5.745  1.00 43.67  ?  249 LEU A O   1 
ATOM   659  C CB  . LEU A 1 94  ? 10.226 25.633 7.077  1.00 35.38  ?  249 LEU A CB  1 
ATOM   660  C CG  . LEU A 1 94  ? 9.613  26.510 8.184  1.00 39.14  ?  249 LEU A CG  1 
ATOM   661  C CD1 . LEU A 1 94  ? 9.670  27.974 7.832  1.00 38.60  ?  249 LEU A CD1 1 
ATOM   662  C CD2 . LEU A 1 94  ? 8.187  26.079 8.533  1.00 40.49  ?  249 LEU A CD2 1 
ATOM   663  N N   . GLY A 1 95  ? 12.559 23.475 6.184  1.00 41.01  ?  250 GLY A N   1 
ATOM   664  C CA  . GLY A 1 95  ? 13.243 22.773 5.113  1.00 41.79  ?  250 GLY A CA  1 
ATOM   665  C C   . GLY A 1 95  ? 14.763 22.804 5.116  1.00 46.87  ?  250 GLY A C   1 
ATOM   666  O O   . GLY A 1 95  ? 15.398 23.309 6.048  1.00 44.58  ?  250 GLY A O   1 
ATOM   667  N N   . PHE A 1 96  ? 15.343 22.203 4.056  1.00 45.64  ?  251 PHE A N   1 
ATOM   668  C CA  . PHE A 1 96  ? 16.778 22.034 3.861  1.00 46.00  ?  251 PHE A CA  1 
ATOM   669  C C   . PHE A 1 96  ? 17.168 22.054 2.389  1.00 50.25  ?  251 PHE A C   1 
ATOM   670  O O   . PHE A 1 96  ? 16.302 22.058 1.525  1.00 49.36  ?  251 PHE A O   1 
ATOM   671  C CB  . PHE A 1 96  ? 17.269 20.737 4.550  1.00 48.17  ?  251 PHE A CB  1 
ATOM   672  C CG  . PHE A 1 96  ? 16.650 19.479 3.990  1.00 50.11  ?  251 PHE A CG  1 
ATOM   673  C CD1 . PHE A 1 96  ? 17.233 18.817 2.911  1.00 52.58  ?  251 PHE A CD1 1 
ATOM   674  C CD2 . PHE A 1 96  ? 15.469 18.971 4.517  1.00 51.65  ?  251 PHE A CD2 1 
ATOM   675  C CE1 . PHE A 1 96  ? 16.621 17.698 2.345  1.00 52.72  ?  251 PHE A CE1 1 
ATOM   676  C CE2 . PHE A 1 96  ? 14.871 17.836 3.960  1.00 53.85  ?  251 PHE A CE2 1 
ATOM   677  C CZ  . PHE A 1 96  ? 15.441 17.221 2.869  1.00 51.41  ?  251 PHE A CZ  1 
ATOM   678  N N   . SER A 1 97  ? 18.478 22.071 2.126  1.00 50.09  ?  252 SER A N   1 
ATOM   679  C CA  . SER A 1 97  ? 19.134 22.089 0.818  1.00 51.23  ?  252 SER A CA  1 
ATOM   680  C C   . SER A 1 97  ? 20.485 21.402 0.955  1.00 62.48  ?  252 SER A C   1 
ATOM   681  O O   . SER A 1 97  ? 21.282 21.783 1.830  1.00 61.59  ?  252 SER A O   1 
ATOM   682  C CB  . SER A 1 97  ? 19.365 23.521 0.357  1.00 52.44  ?  252 SER A CB  1 
ATOM   683  O OG  . SER A 1 97  ? 18.696 23.763 -0.864 1.00 63.06  ?  252 SER A OG  1 
ATOM   684  N N   . SER A 1 98  ? 20.750 20.392 0.091  1.00 64.78  ?  253 SER A N   1 
ATOM   685  C CA  . SER A 1 98  ? 22.021 19.663 0.080  1.00 66.63  ?  253 SER A CA  1 
ATOM   686  C C   . SER A 1 98  ? 23.023 20.130 -0.980 1.00 76.44  ?  253 SER A C   1 
ATOM   687  O O   . SER A 1 98  ? 24.176 20.409 -0.621 1.00 77.93  ?  253 SER A O   1 
ATOM   688  C CB  . SER A 1 98  ? 21.805 18.162 0.030  1.00 69.27  ?  253 SER A CB  1 
ATOM   689  O OG  . SER A 1 98  ? 21.692 17.682 1.358  1.00 76.94  ?  253 SER A OG  1 
ATOM   690  N N   . ASP A 1 99  ? 22.585 20.232 -2.265 1.00 74.14  ?  254 ASP A N   1 
ATOM   691  C CA  . ASP A 1 99  ? 23.366 20.678 -3.440 1.00 74.43  ?  254 ASP A CA  1 
ATOM   692  C C   . ASP A 1 99  ? 24.868 20.982 -3.221 1.00 79.20  ?  254 ASP A C   1 
ATOM   693  O O   . ASP A 1 99  ? 25.246 22.070 -2.775 1.00 78.68  ?  254 ASP A O   1 
ATOM   694  C CB  . ASP A 1 99  ? 22.645 21.808 -4.203 1.00 76.26  ?  254 ASP A CB  1 
ATOM   695  N N   . GLY A 1 100 ? 25.695 19.982 -3.509 1.00 77.09  ?  255 GLY A N   1 
ATOM   696  C CA  . GLY A 1 100 ? 27.144 20.047 -3.360 1.00 77.30  ?  255 GLY A CA  1 
ATOM   697  C C   . GLY A 1 100 ? 27.598 20.223 -1.924 1.00 81.17  ?  255 GLY A C   1 
ATOM   698  O O   . GLY A 1 100 ? 27.054 19.599 -1.005 1.00 80.69  ?  255 GLY A O   1 
ATOM   699  N N   . ASP A 1 101 ? 28.605 21.092 -1.735 1.00 76.84  ?  256 ASP A N   1 
ATOM   700  C CA  . ASP A 1 101 ? 29.168 21.429 -0.428 1.00 75.99  ?  256 ASP A CA  1 
ATOM   701  C C   . ASP A 1 101 ? 28.337 22.541 0.234  1.00 77.54  ?  256 ASP A C   1 
ATOM   702  O O   . ASP A 1 101 ? 28.542 22.845 1.413  1.00 77.79  ?  256 ASP A O   1 
ATOM   703  C CB  . ASP A 1 101 ? 30.644 21.855 -0.581 1.00 78.06  ?  256 ASP A CB  1 
ATOM   704  N N   . ASP A 1 102 ? 27.394 23.141 -0.526 1.00 71.29  ?  257 ASP A N   1 
ATOM   705  C CA  . ASP A 1 102 ? 26.524 24.213 -0.051 1.00 69.31  ?  257 ASP A CA  1 
ATOM   706  C C   . ASP A 1 102 ? 25.279 23.659 0.691  1.00 69.05  ?  257 ASP A C   1 
ATOM   707  O O   . ASP A 1 102 ? 24.295 23.251 0.056  1.00 68.92  ?  257 ASP A O   1 
ATOM   708  C CB  . ASP A 1 102 ? 26.179 25.157 -1.213 1.00 70.71  ?  257 ASP A CB  1 
ATOM   709  N N   . LEU A 1 103 ? 25.354 23.600 2.040  1.00 61.69  ?  258 LEU A N   1 
ATOM   710  C CA  . LEU A 1 103 ? 24.281 23.056 2.874  1.00 59.77  ?  258 LEU A CA  1 
ATOM   711  C C   . LEU A 1 103 ? 23.496 24.138 3.602  1.00 59.79  ?  258 LEU A C   1 
ATOM   712  O O   . LEU A 1 103 ? 24.079 24.921 4.357  1.00 59.52  ?  258 LEU A O   1 
ATOM   713  C CB  . LEU A 1 103 ? 24.833 22.043 3.890  1.00 59.89  ?  258 LEU A CB  1 
ATOM   714  C CG  . LEU A 1 103 ? 25.672 20.866 3.358  1.00 64.36  ?  258 LEU A CG  1 
ATOM   715  C CD1 . LEU A 1 103 ? 26.469 20.236 4.485  1.00 63.87  ?  258 LEU A CD1 1 
ATOM   716  C CD2 . LEU A 1 103 ? 24.786 19.799 2.699  1.00 67.24  ?  258 LEU A CD2 1 
ATOM   717  N N   . CYS A 1 104 ? 22.166 24.161 3.399  1.00 53.24  ?  259 CYS A N   1 
ATOM   718  C CA  . CYS A 1 104 ? 21.259 25.140 4.007  1.00 51.62  ?  259 CYS A CA  1 
ATOM   719  C C   . CYS A 1 104 ? 20.141 24.520 4.818  1.00 51.04  ?  259 CYS A C   1 
ATOM   720  O O   . CYS A 1 104 ? 19.641 23.471 4.446  1.00 50.14  ?  259 CYS A O   1 
ATOM   721  C CB  . CYS A 1 104 ? 20.696 26.078 2.947  1.00 52.01  ?  259 CYS A CB  1 
ATOM   722  S SG  . CYS A 1 104 ? 21.947 27.045 2.081  1.00 56.40  ?  259 CYS A SG  1 
ATOM   723  N N   . LEU A 1 105 ? 19.722 25.202 5.904  1.00 45.12  ?  260 LEU A N   1 
ATOM   724  C CA  . LEU A 1 105 ? 18.585 24.829 6.756  1.00 43.08  ?  260 LEU A CA  1 
ATOM   725  C C   . LEU A 1 105 ? 17.649 26.049 6.857  1.00 45.09  ?  260 LEU A C   1 
ATOM   726  O O   . LEU A 1 105 ? 18.122 27.155 7.089  1.00 44.33  ?  260 LEU A O   1 
ATOM   727  C CB  . LEU A 1 105 ? 19.021 24.352 8.139  1.00 42.61  ?  260 LEU A CB  1 
ATOM   728  C CG  . LEU A 1 105 ? 19.860 23.080 8.200  1.00 47.68  ?  260 LEU A CG  1 
ATOM   729  C CD1 . LEU A 1 105 ? 20.784 23.111 9.388  1.00 47.58  ?  260 LEU A CD1 1 
ATOM   730  C CD2 . LEU A 1 105 ? 18.997 21.811 8.199  1.00 49.84  ?  260 LEU A CD2 1 
ATOM   731  N N   . VAL A 1 106 ? 16.354 25.865 6.574  1.00 40.60  ?  261 VAL A N   1 
ATOM   732  C CA  . VAL A 1 106 ? 15.353 26.921 6.566  1.00 39.75  ?  261 VAL A CA  1 
ATOM   733  C C   . VAL A 1 106 ? 14.500 26.826 7.826  1.00 44.06  ?  261 VAL A C   1 
ATOM   734  O O   . VAL A 1 106 ? 13.869 25.795 8.074  1.00 43.44  ?  261 VAL A O   1 
ATOM   735  C CB  . VAL A 1 106 ? 14.508 26.889 5.257  1.00 42.85  ?  261 VAL A CB  1 
ATOM   736  C CG1 . VAL A 1 106 ? 13.455 28.001 5.233  1.00 41.86  ?  261 VAL A CG1 1 
ATOM   737  C CG2 . VAL A 1 106 ? 15.409 26.983 4.026  1.00 42.77  ?  261 VAL A CG2 1 
ATOM   738  N N   . TYR A 1 107 ? 14.458 27.916 8.601  1.00 40.38  ?  262 TYR A N   1 
ATOM   739  C CA  . TYR A 1 107 ? 13.696 27.953 9.850  1.00 39.80  ?  262 TYR A CA  1 
ATOM   740  C C   . TYR A 1 107 ? 12.637 29.002 9.851  1.00 43.27  ?  262 TYR A C   1 
ATOM   741  O O   . TYR A 1 107 ? 12.561 29.852 8.960  1.00 43.56  ?  262 TYR A O   1 
ATOM   742  C CB  . TYR A 1 107 ? 14.616 28.251 11.043 1.00 40.34  ?  262 TYR A CB  1 
ATOM   743  C CG  . TYR A 1 107 ? 15.737 27.265 11.234 1.00 42.73  ?  262 TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 107 ? 15.639 26.241 12.179 1.00 44.82  ?  262 TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 107 ? 16.936 27.401 10.539 1.00 43.11  ?  262 TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 107 ? 16.703 25.372 12.417 1.00 44.16  ?  262 TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 107 ? 18.011 26.552 10.782 1.00 43.98  ?  262 TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 107 ? 17.879 25.519 11.695 1.00 52.26  ?  262 TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 107 ? 18.935 24.667 11.890 1.00 57.36  ?  262 TYR A OH  1 
ATOM   750  N N   . VAL A 1 108 ? 11.880 29.008 10.929 1.00 38.44  ?  263 VAL A N   1 
ATOM   751  C CA  . VAL A 1 108 ? 10.894 30.044 11.141 1.00 37.71  ?  263 VAL A CA  1 
ATOM   752  C C   . VAL A 1 108 ? 11.652 31.303 11.606 1.00 41.10  ?  263 VAL A C   1 
ATOM   753  O O   . VAL A 1 108 ? 12.554 31.223 12.461 1.00 40.82  ?  263 VAL A O   1 
ATOM   754  C CB  . VAL A 1 108 ? 9.795  29.588 12.125 1.00 40.79  ?  263 VAL A CB  1 
ATOM   755  C CG1 . VAL A 1 108 ? 8.828  30.716 12.433 1.00 39.56  ?  263 VAL A CG1 1 
ATOM   756  C CG2 . VAL A 1 108 ? 9.043  28.373 11.562 1.00 40.74  ?  263 VAL A CG2 1 
ATOM   757  N N   . TYR A 1 109 ? 11.324 32.450 10.973 1.00 36.48  ?  264 TYR A N   1 
ATOM   758  C CA  . TYR A 1 109 ? 11.894 33.753 11.271 1.00 34.73  ?  264 TYR A CA  1 
ATOM   759  C C   . TYR A 1 109 ? 11.478 34.230 12.664 1.00 37.82  ?  264 TYR A C   1 
ATOM   760  O O   . TYR A 1 109 ? 10.295 34.370 12.929 1.00 36.82  ?  264 TYR A O   1 
ATOM   761  C CB  . TYR A 1 109 ? 11.501 34.769 10.196 1.00 33.72  ?  264 TYR A CB  1 
ATOM   762  C CG  . TYR A 1 109 ? 11.869 36.199 10.544 1.00 33.12  ?  264 TYR A CG  1 
ATOM   763  C CD1 . TYR A 1 109 ? 10.901 37.106 10.974 1.00 33.56  ?  264 TYR A CD1 1 
ATOM   764  C CD2 . TYR A 1 109 ? 13.178 36.658 10.400 1.00 33.50  ?  264 TYR A CD2 1 
ATOM   765  C CE1 . TYR A 1 109 ? 11.231 38.425 11.280 1.00 31.59  ?  264 TYR A CE1 1 
ATOM   766  C CE2 . TYR A 1 109 ? 13.516 37.976 10.695 1.00 34.29  ?  264 TYR A CE2 1 
ATOM   767  C CZ  . TYR A 1 109 ? 12.537 38.857 11.127 1.00 38.90  ?  264 TYR A CZ  1 
ATOM   768  O OH  . TYR A 1 109 ? 12.867 40.149 11.425 1.00 44.00  ?  264 TYR A OH  1 
ATOM   769  N N   . MET A 1 110 ? 12.457 34.493 13.530 1.00 35.93  ?  265 MET A N   1 
ATOM   770  C CA  . MET A 1 110 ? 12.237 34.972 14.895 1.00 36.28  ?  265 MET A CA  1 
ATOM   771  C C   . MET A 1 110 ? 12.335 36.516 14.935 1.00 39.38  ?  265 MET A C   1 
ATOM   772  O O   . MET A 1 110 ? 13.422 37.086 14.776 1.00 37.58  ?  265 MET A O   1 
ATOM   773  C CB  . MET A 1 110 ? 13.197 34.289 15.874 1.00 38.68  ?  265 MET A CB  1 
ATOM   774  C CG  . MET A 1 110 ? 13.008 32.785 15.951 1.00 42.55  ?  265 MET A CG  1 
ATOM   775  S SD  . MET A 1 110 ? 11.433 32.336 16.727 1.00 47.96  ?  265 MET A SD  1 
ATOM   776  C CE  . MET A 1 110 ? 10.825 31.330 15.533 1.00 45.97  ?  265 MET A CE  1 
ATOM   777  N N   . PRO A 1 111 ? 11.176 37.203 15.086 1.00 36.05  ?  266 PRO A N   1 
ATOM   778  C CA  . PRO A 1 111 ? 11.167 38.673 15.064 1.00 34.84  ?  266 PRO A CA  1 
ATOM   779  C C   . PRO A 1 111 ? 11.995 39.343 16.162 1.00 38.04  ?  266 PRO A C   1 
ATOM   780  O O   . PRO A 1 111 ? 12.417 40.494 15.995 1.00 38.49  ?  266 PRO A O   1 
ATOM   781  C CB  . PRO A 1 111 ? 9.670  39.004 15.164 1.00 36.62  ?  266 PRO A CB  1 
ATOM   782  C CG  . PRO A 1 111 ? 8.969  37.783 14.716 1.00 40.55  ?  266 PRO A CG  1 
ATOM   783  C CD  . PRO A 1 111 ? 9.803  36.679 15.251 1.00 37.73  ?  266 PRO A CD  1 
ATOM   784  N N   . ASN A 1 112 ? 12.242 38.642 17.282 1.00 32.82  ?  267 ASN A N   1 
ATOM   785  C CA  . ASN A 1 112 ? 13.083 39.215 18.330 1.00 31.98  ?  267 ASN A CA  1 
ATOM   786  C C   . ASN A 1 112 ? 14.505 38.658 18.424 1.00 36.57  ?  267 ASN A C   1 
ATOM   787  O O   . ASN A 1 112 ? 15.175 38.888 19.425 1.00 37.33  ?  267 ASN A O   1 
ATOM   788  C CB  . ASN A 1 112 ? 12.362 39.284 19.673 1.00 30.69  ?  267 ASN A CB  1 
ATOM   789  C CG  . ASN A 1 112 ? 11.385 40.407 19.741 1.00 40.54  ?  267 ASN A CG  1 
ATOM   790  O OD1 . ASN A 1 112 ? 11.734 41.557 19.503 1.00 44.34  ?  267 ASN A OD1 1 
ATOM   791  N ND2 . ASN A 1 112 ? 10.125 40.095 19.983 1.00 32.02  ?  267 ASN A ND2 1 
ATOM   792  N N   . GLY A 1 113 ? 14.967 37.993 17.361 1.00 33.77  ?  268 GLY A N   1 
ATOM   793  C CA  . GLY A 1 113 ? 16.302 37.409 17.256 1.00 34.23  ?  268 GLY A CA  1 
ATOM   794  C C   . GLY A 1 113 ? 16.715 36.542 18.439 1.00 38.79  ?  268 GLY A C   1 
ATOM   795  O O   . GLY A 1 113 ? 15.909 35.763 18.955 1.00 39.10  ?  268 GLY A O   1 
ATOM   796  N N   . SER A 1 114 ? 17.966 36.690 18.883 1.00 33.96  ?  269 SER A N   1 
ATOM   797  C CA  . SER A 1 114 ? 18.505 35.943 20.015 1.00 34.04  ?  269 SER A CA  1 
ATOM   798  C C   . SER A 1 114 ? 18.480 36.717 21.328 1.00 37.18  ?  269 SER A C   1 
ATOM   799  O O   . SER A 1 114 ? 18.525 37.962 21.339 1.00 36.08  ?  269 SER A O   1 
ATOM   800  C CB  . SER A 1 114 ? 19.930 35.474 19.720 1.00 39.08  ?  269 SER A CB  1 
ATOM   801  O OG  . SER A 1 114 ? 20.824 36.547 19.473 1.00 47.42  ?  269 SER A OG  1 
ATOM   802  N N   . LEU A 1 115 ? 18.448 35.958 22.448 1.00 31.61  ?  270 LEU A N   1 
ATOM   803  C CA  . LEU A 1 115 ? 18.491 36.492 23.810 1.00 30.20  ?  270 LEU A CA  1 
ATOM   804  C C   . LEU A 1 115 ? 19.769 37.308 23.983 1.00 36.89  ?  270 LEU A C   1 
ATOM   805  O O   . LEU A 1 115 ? 19.711 38.421 24.510 1.00 38.50  ?  270 LEU A O   1 
ATOM   806  C CB  . LEU A 1 115 ? 18.424 35.337 24.818 1.00 29.32  ?  270 LEU A CB  1 
ATOM   807  C CG  . LEU A 1 115 ? 18.497 35.643 26.311 1.00 32.18  ?  270 LEU A CG  1 
ATOM   808  C CD1 . LEU A 1 115 ? 17.455 36.675 26.733 1.00 32.36  ?  270 LEU A CD1 1 
ATOM   809  C CD2 . LEU A 1 115 ? 18.305 34.378 27.113 1.00 30.59  ?  270 LEU A CD2 1 
ATOM   810  N N   . LEU A 1 116 ? 20.912 36.788 23.469 1.00 34.49  ?  271 LEU A N   1 
ATOM   811  C CA  . LEU A 1 116 ? 22.207 37.480 23.509 1.00 33.62  ?  271 LEU A CA  1 
ATOM   812  C C   . LEU A 1 116 ? 22.082 38.868 22.901 1.00 37.83  ?  271 LEU A C   1 
ATOM   813  O O   . LEU A 1 116 ? 22.480 39.840 23.538 1.00 37.76  ?  271 LEU A O   1 
ATOM   814  C CB  . LEU A 1 116 ? 23.298 36.671 22.788 1.00 32.85  ?  271 LEU A CB  1 
ATOM   815  C CG  . LEU A 1 116 ? 24.748 37.239 22.897 1.00 34.56  ?  271 LEU A CG  1 
ATOM   816  C CD1 . LEU A 1 116 ? 25.482 36.685 24.095 1.00 32.93  ?  271 LEU A CD1 1 
ATOM   817  C CD2 . LEU A 1 116 ? 25.537 36.991 21.629 1.00 26.73  ?  271 LEU A CD2 1 
ATOM   818  N N   . ASP A 1 117 ? 21.474 38.968 21.710 1.00 34.47  ?  272 ASP A N   1 
ATOM   819  C CA  . ASP A 1 117 ? 21.324 40.250 21.030 1.00 34.59  ?  272 ASP A CA  1 
ATOM   820  C C   . ASP A 1 117 ? 20.329 41.206 21.721 1.00 38.21  ?  272 ASP A C   1 
ATOM   821  O O   . ASP A 1 117 ? 20.550 42.409 21.702 1.00 39.32  ?  272 ASP A O   1 
ATOM   822  C CB  . ASP A 1 117 ? 21.044 40.050 19.528 1.00 37.04  ?  272 ASP A CB  1 
ATOM   823  C CG  . ASP A 1 117 ? 22.174 39.382 18.756 1.00 49.25  ?  272 ASP A CG  1 
ATOM   824  O OD1 . ASP A 1 117 ? 23.254 39.165 19.351 1.00 50.16  ?  272 ASP A OD1 1 
ATOM   825  O OD2 . ASP A 1 117 ? 21.986 39.097 17.538 1.00 55.72  -1 272 ASP A OD2 1 
ATOM   826  N N   . ARG A 1 118 ? 19.282 40.675 22.371 1.00 33.38  ?  273 ARG A N   1 
ATOM   827  C CA  . ARG A 1 118 ? 18.330 41.490 23.109 1.00 33.09  ?  273 ARG A CA  1 
ATOM   828  C C   . ARG A 1 118 ? 18.887 41.987 24.441 1.00 39.42  ?  273 ARG A C   1 
ATOM   829  O O   . ARG A 1 118 ? 18.591 43.112 24.832 1.00 40.10  ?  273 ARG A O   1 
ATOM   830  C CB  . ARG A 1 118 ? 16.962 40.807 23.277 1.00 31.68  ?  273 ARG A CB  1 
ATOM   831  C CG  . ARG A 1 118 ? 16.217 40.501 21.964 1.00 32.08  ?  273 ARG A CG  1 
ATOM   832  C CD  . ARG A 1 118 ? 15.803 41.697 21.100 1.00 28.75  ?  273 ARG A CD  1 
ATOM   833  N NE  . ARG A 1 118 ? 16.912 42.374 20.423 1.00 34.61  ?  273 ARG A NE  1 
ATOM   834  C CZ  . ARG A 1 118 ? 17.561 41.912 19.354 1.00 50.64  ?  273 ARG A CZ  1 
ATOM   835  N NH1 . ARG A 1 118 ? 17.245 40.731 18.830 1.00 35.25  ?  273 ARG A NH1 1 
ATOM   836  N NH2 . ARG A 1 118 ? 18.539 42.621 18.809 1.00 33.76  1  273 ARG A NH2 1 
ATOM   837  N N   . LEU A 1 119 ? 19.713 41.183 25.119 1.00 36.53  ?  274 LEU A N   1 
ATOM   838  C CA  . LEU A 1 119 ? 20.360 41.612 26.362 1.00 37.31  ?  274 LEU A CA  1 
ATOM   839  C C   . LEU A 1 119 ? 21.407 42.746 26.104 1.00 40.55  ?  274 LEU A C   1 
ATOM   840  O O   . LEU A 1 119 ? 21.681 43.565 26.991 1.00 41.03  ?  274 LEU A O   1 
ATOM   841  C CB  . LEU A 1 119 ? 20.997 40.408 27.111 1.00 37.57  ?  274 LEU A CB  1 
ATOM   842  C CG  . LEU A 1 119 ? 20.027 39.348 27.699 1.00 42.83  ?  274 LEU A CG  1 
ATOM   843  C CD1 . LEU A 1 119 ? 20.793 38.149 28.189 1.00 44.64  ?  274 LEU A CD1 1 
ATOM   844  C CD2 . LEU A 1 119 ? 19.193 39.893 28.855 1.00 42.22  ?  274 LEU A CD2 1 
ATOM   845  N N   . SER A 1 120 ? 21.967 42.801 24.881 1.00 34.99  ?  275 SER A N   1 
ATOM   846  C CA  . SER A 1 120 ? 22.919 43.838 24.520 1.00 35.20  ?  275 SER A CA  1 
ATOM   847  C C   . SER A 1 120 ? 22.236 44.970 23.748 1.00 43.22  ?  275 SER A C   1 
ATOM   848  O O   . SER A 1 120 ? 22.908 45.946 23.382 1.00 43.35  ?  275 SER A O   1 
ATOM   849  C CB  . SER A 1 120 ? 24.091 43.264 23.733 1.00 37.52  ?  275 SER A CB  1 
ATOM   850  O OG  . SER A 1 120 ? 23.663 42.680 22.517 1.00 50.88  ?  275 SER A OG  1 
ATOM   851  N N   . CYS A 1 121 ? 20.899 44.849 23.515 1.00 40.10  ?  276 CYS A N   1 
ATOM   852  C CA  . CYS A 1 121 ? 20.075 45.857 22.836 1.00 40.46  ?  276 CYS A CA  1 
ATOM   853  C C   . CYS A 1 121 ? 20.569 46.117 21.433 1.00 43.86  ?  276 CYS A C   1 
ATOM   854  O O   . CYS A 1 121 ? 20.505 47.246 20.949 1.00 43.70  ?  276 CYS A O   1 
ATOM   855  C CB  . CYS A 1 121 ? 19.981 47.149 23.651 1.00 41.14  ?  276 CYS A CB  1 
ATOM   856  S SG  . CYS A 1 121 ? 19.252 46.938 25.295 1.00 45.61  ?  276 CYS A SG  1 
ATOM   857  N N   . LEU A 1 122 ? 21.055 45.062 20.772 1.00 40.20  ?  277 LEU A N   1 
ATOM   858  C CA  . LEU A 1 122 ? 21.549 45.136 19.404 1.00 40.19  ?  277 LEU A CA  1 
ATOM   859  C C   . LEU A 1 122 ? 20.480 45.693 18.483 1.00 43.61  ?  277 LEU A C   1 
ATOM   860  O O   . LEU A 1 122 ? 19.313 45.292 18.569 1.00 43.06  ?  277 LEU A O   1 
ATOM   861  C CB  . LEU A 1 122 ? 22.055 43.761 18.926 1.00 40.64  ?  277 LEU A CB  1 
ATOM   862  C CG  . LEU A 1 122 ? 22.786 43.731 17.568 1.00 47.37  ?  277 LEU A CG  1 
ATOM   863  C CD1 . LEU A 1 122 ? 24.059 44.617 17.560 1.00 48.02  ?  277 LEU A CD1 1 
ATOM   864  C CD2 . LEU A 1 122 ? 23.138 42.332 17.183 1.00 48.97  ?  277 LEU A CD2 1 
ATOM   865  N N   . ASP A 1 123 ? 20.872 46.684 17.674 1.00 41.32  ?  278 ASP A N   1 
ATOM   866  C CA  . ASP A 1 123 ? 20.014 47.370 16.693 1.00 41.44  ?  278 ASP A CA  1 
ATOM   867  C C   . ASP A 1 123 ? 18.921 48.277 17.262 1.00 47.60  ?  278 ASP A C   1 
ATOM   868  O O   . ASP A 1 123 ? 17.905 48.485 16.610 1.00 48.14  ?  278 ASP A O   1 
ATOM   869  C CB  . ASP A 1 123 ? 19.485 46.397 15.619 1.00 42.24  ?  278 ASP A CB  1 
ATOM   870  C CG  . ASP A 1 123 ? 20.586 45.612 14.924 1.00 50.77  ?  278 ASP A CG  1 
ATOM   871  O OD1 . ASP A 1 123 ? 20.467 44.373 14.844 1.00 52.17  ?  278 ASP A OD1 1 
ATOM   872  O OD2 . ASP A 1 123 ? 21.585 46.235 14.493 1.00 54.71  -1 278 ASP A OD2 1 
ATOM   873  N N   . GLY A 1 124 ? 19.154 48.851 18.445 1.00 44.56  ?  279 GLY A N   1 
ATOM   874  C CA  . GLY A 1 124 ? 18.198 49.768 19.056 1.00 43.48  ?  279 GLY A CA  1 
ATOM   875  C C   . GLY A 1 124 ? 17.001 49.138 19.733 1.00 46.25  ?  279 GLY A C   1 
ATOM   876  O O   . GLY A 1 124 ? 16.037 49.841 20.041 1.00 47.89  ?  279 GLY A O   1 
ATOM   877  N N   . THR A 1 125 ? 17.030 47.838 19.998 1.00 40.73  ?  280 THR A N   1 
ATOM   878  C CA  . THR A 1 125 ? 15.893 47.235 20.689 1.00 40.90  ?  280 THR A CA  1 
ATOM   879  C C   . THR A 1 125 ? 15.840 47.691 22.159 1.00 44.32  ?  280 THR A C   1 
ATOM   880  O O   . THR A 1 125 ? 16.871 47.721 22.808 1.00 43.95  ?  280 THR A O   1 
ATOM   881  C CB  . THR A 1 125 ? 15.820 45.705 20.478 1.00 45.79  ?  280 THR A CB  1 
ATOM   882  O OG1 . THR A 1 125 ? 17.054 45.072 20.866 1.00 47.13  ?  280 THR A OG1 1 
ATOM   883  C CG2 . THR A 1 125 ? 15.458 45.337 19.032 1.00 36.32  ?  280 THR A CG2 1 
ATOM   884  N N   . PRO A 1 126 ? 14.679 48.098 22.704 1.00 41.55  ?  281 PRO A N   1 
ATOM   885  C CA  . PRO A 1 126 ? 14.642 48.503 24.123 1.00 41.07  ?  281 PRO A CA  1 
ATOM   886  C C   . PRO A 1 126 ? 15.057 47.378 25.077 1.00 47.42  ?  281 PRO A C   1 
ATOM   887  O O   . PRO A 1 126 ? 14.818 46.219 24.738 1.00 46.90  ?  281 PRO A O   1 
ATOM   888  C CB  . PRO A 1 126 ? 13.183 48.910 24.337 1.00 41.92  ?  281 PRO A CB  1 
ATOM   889  C CG  . PRO A 1 126 ? 12.439 48.250 23.292 1.00 46.54  ?  281 PRO A CG  1 
ATOM   890  C CD  . PRO A 1 126 ? 13.331 48.156 22.099 1.00 42.82  ?  281 PRO A CD  1 
ATOM   891  N N   . PRO A 1 127 ? 15.678 47.667 26.254 1.00 46.41  ?  282 PRO A N   1 
ATOM   892  C CA  . PRO A 1 127 ? 16.066 46.565 27.170 1.00 45.88  ?  282 PRO A CA  1 
ATOM   893  C C   . PRO A 1 127 ? 14.901 45.689 27.595 1.00 46.98  ?  282 PRO A C   1 
ATOM   894  O O   . PRO A 1 127 ? 13.813 46.201 27.707 1.00 46.38  ?  282 PRO A O   1 
ATOM   895  C CB  . PRO A 1 127 ? 16.671 47.291 28.385 1.00 47.73  ?  282 PRO A CB  1 
ATOM   896  C CG  . PRO A 1 127 ? 17.004 48.665 27.919 1.00 51.76  ?  282 PRO A CG  1 
ATOM   897  C CD  . PRO A 1 127 ? 16.048 48.992 26.809 1.00 47.94  ?  282 PRO A CD  1 
ATOM   898  N N   . LEU A 1 128 ? 15.128 44.383 27.812 1.00 44.92  ?  283 LEU A N   1 
ATOM   899  C CA  . LEU A 1 128 ? 14.094 43.437 28.258 1.00 46.09  ?  283 LEU A CA  1 
ATOM   900  C C   . LEU A 1 128 ? 13.732 43.675 29.726 1.00 55.82  ?  283 LEU A C   1 
ATOM   901  O O   . LEU A 1 128 ? 14.618 43.714 30.581 1.00 55.27  ?  283 LEU A O   1 
ATOM   902  C CB  . LEU A 1 128 ? 14.540 41.957 28.104 1.00 45.78  ?  283 LEU A CB  1 
ATOM   903  C CG  . LEU A 1 128 ? 15.114 41.471 26.775 1.00 48.80  ?  283 LEU A CG  1 
ATOM   904  C CD1 . LEU A 1 128 ? 15.764 40.108 26.953 1.00 47.45  ?  283 LEU A CD1 1 
ATOM   905  C CD2 . LEU A 1 128 ? 14.037 41.418 25.678 1.00 50.06  ?  283 LEU A CD2 1 
HETATM 906  N N   . SEP A 1 129 ? 12.416 43.794 30.017 1.00 57.54  ?  284 SEP A N   1 
HETATM 907  C CA  . SEP A 1 129 ? 11.864 43.947 31.370 1.00 59.30  ?  284 SEP A CA  1 
HETATM 908  C CB  . SEP A 1 129 ? 10.268 44.228 31.419 1.00 62.74  ?  284 SEP A CB  1 
HETATM 909  O OG  . SEP A 1 129 ? 9.126  43.377 30.845 1.00 67.42  ?  284 SEP A OG  1 
HETATM 910  C C   . SEP A 1 129 ? 12.198 42.691 32.186 1.00 63.82  ?  284 SEP A C   1 
HETATM 911  O O   . SEP A 1 129 ? 12.277 41.605 31.595 1.00 64.23  ?  284 SEP A O   1 
HETATM 912  P P   . SEP A 1 129 ? 7.504  43.997 30.579 1.00 71.54  ?  284 SEP A P   1 
HETATM 913  O O1P . SEP A 1 129 ? 7.309  44.533 29.136 1.00 70.72  -1 284 SEP A O1P 1 
HETATM 914  O O2P . SEP A 1 129 ? 6.912  45.074 31.556 1.00 71.10  -1 284 SEP A O2P 1 
HETATM 915  O O3P . SEP A 1 129 ? 6.439  42.860 30.658 1.00 73.17  ?  284 SEP A O3P 1 
ATOM   916  N N   . TRP A 1 130 ? 12.408 42.819 33.531 1.00 59.95  ?  285 TRP A N   1 
ATOM   917  C CA  . TRP A 1 130 ? 12.661 41.661 34.402 1.00 59.24  ?  285 TRP A CA  1 
ATOM   918  C C   . TRP A 1 130 ? 11.515 40.661 34.253 1.00 61.61  ?  285 TRP A C   1 
ATOM   919  O O   . TRP A 1 130 ? 11.734 39.447 34.324 1.00 61.88  ?  285 TRP A O   1 
ATOM   920  C CB  . TRP A 1 130 ? 12.826 42.088 35.862 1.00 57.90  ?  285 TRP A CB  1 
ATOM   921  C CG  . TRP A 1 130 ? 12.936 40.933 36.820 1.00 58.94  ?  285 TRP A CG  1 
ATOM   922  C CD1 . TRP A 1 130 ? 11.983 40.506 37.698 1.00 61.82  ?  285 TRP A CD1 1 
ATOM   923  C CD2 . TRP A 1 130 ? 14.021 40.001 36.924 1.00 58.77  ?  285 TRP A CD2 1 
ATOM   924  N NE1 . TRP A 1 130 ? 12.427 39.398 38.377 1.00 61.06  ?  285 TRP A NE1 1 
ATOM   925  C CE2 . TRP A 1 130 ? 13.688 39.084 37.945 1.00 62.07  ?  285 TRP A CE2 1 
ATOM   926  C CE3 . TRP A 1 130 ? 15.259 39.862 36.263 1.00 60.04  ?  285 TRP A CE3 1 
ATOM   927  C CZ2 . TRP A 1 130 ? 14.526 38.023 38.299 1.00 60.99  ?  285 TRP A CZ2 1 
ATOM   928  C CZ3 . TRP A 1 130 ? 16.102 38.826 36.636 1.00 60.98  ?  285 TRP A CZ3 1 
ATOM   929  C CH2 . TRP A 1 130 ? 15.746 37.939 37.665 1.00 61.48  ?  285 TRP A CH2 1 
ATOM   930  N N   . HIS A 1 131 ? 10.316 41.180 33.984 1.00 57.89  ?  286 HIS A N   1 
ATOM   931  C CA  . HIS A 1 131 ? 9.123  40.381 33.734 1.00 58.32  ?  286 HIS A CA  1 
ATOM   932  C C   . HIS A 1 131 ? 9.321  39.449 32.522 1.00 59.38  ?  286 HIS A C   1 
ATOM   933  O O   . HIS A 1 131 ? 9.030  38.255 32.628 1.00 59.29  ?  286 HIS A O   1 
ATOM   934  C CB  . HIS A 1 131 ? 7.874  41.269 33.552 1.00 59.66  ?  286 HIS A CB  1 
ATOM   935  C CG  . HIS A 1 131 ? 6.622  40.459 33.408 1.00 63.42  ?  286 HIS A CG  1 
ATOM   936  N ND1 . HIS A 1 131 ? 6.117  40.114 32.168 1.00 65.50  ?  286 HIS A ND1 1 
ATOM   937  C CD2 . HIS A 1 131 ? 5.841  39.906 34.366 1.00 65.29  ?  286 HIS A CD2 1 
ATOM   938  C CE1 . HIS A 1 131 ? 5.052  39.366 32.411 1.00 65.00  ?  286 HIS A CE1 1 
ATOM   939  N NE2 . HIS A 1 131 ? 4.837  39.231 33.717 1.00 65.35  ?  286 HIS A NE2 1 
ATOM   940  N N   . MET A 1 132 ? 9.842  39.983 31.393 1.00 53.15  ?  287 MET A N   1 
ATOM   941  C CA  . MET A 1 132 ? 10.109 39.169 30.209 1.00 52.73  ?  287 MET A CA  1 
ATOM   942  C C   . MET A 1 132 ? 11.266 38.198 30.399 1.00 50.58  ?  287 MET A C   1 
ATOM   943  O O   . MET A 1 132 ? 11.205 37.058 29.925 1.00 48.17  ?  287 MET A O   1 
ATOM   944  C CB  . MET A 1 132 ? 10.291 40.007 28.960 1.00 56.36  ?  287 MET A CB  1 
ATOM   945  C CG  . MET A 1 132 ? 9.473  39.470 27.847 1.00 61.76  ?  287 MET A CG  1 
ATOM   946  S SD  . MET A 1 132 ? 7.799  40.140 27.629 1.00 67.59  ?  287 MET A SD  1 
ATOM   947  C CE  . MET A 1 132 ? 6.906  39.169 28.848 1.00 65.00  ?  287 MET A CE  1 
ATOM   948  N N   . ARG A 1 133 ? 12.274 38.626 31.166 1.00 45.36  ?  288 ARG A N   1 
ATOM   949  C CA  . ARG A 1 133 ? 13.444 37.839 31.508 1.00 45.53  ?  288 ARG A CA  1 
ATOM   950  C C   . ARG A 1 133 ? 13.069 36.555 32.256 1.00 56.05  ?  288 ARG A C   1 
ATOM   951  O O   . ARG A 1 133 ? 13.595 35.486 31.927 1.00 56.20  ?  288 ARG A O   1 
ATOM   952  C CB  . ARG A 1 133 ? 14.435 38.693 32.286 1.00 43.32  ?  288 ARG A CB  1 
ATOM   953  C CG  . ARG A 1 133 ? 15.177 39.642 31.367 1.00 42.44  ?  288 ARG A CG  1 
ATOM   954  C CD  . ARG A 1 133 ? 16.312 40.375 32.028 1.00 38.16  ?  288 ARG A CD  1 
ATOM   955  N NE  . ARG A 1 133 ? 16.446 41.728 31.476 1.00 32.20  ?  288 ARG A NE  1 
ATOM   956  C CZ  . ARG A 1 133 ? 17.573 42.428 31.467 1.00 47.41  ?  288 ARG A CZ  1 
ATOM   957  N NH1 . ARG A 1 133 ? 18.701 41.893 31.930 1.00 36.67  ?  288 ARG A NH1 1 
ATOM   958  N NH2 . ARG A 1 133 ? 17.588 43.662 30.985 1.00 41.96  1  288 ARG A NH2 1 
ATOM   959  N N   . CYS A 1 134 ? 12.099 36.643 33.199 1.00 56.07  ?  289 CYS A N   1 
ATOM   960  C CA  . CYS A 1 134 ? 11.576 35.484 33.932 1.00 56.85  ?  289 CYS A CA  1 
ATOM   961  C C   . CYS A 1 134 ? 10.788 34.571 33.010 1.00 58.04  ?  289 CYS A C   1 
ATOM   962  O O   . CYS A 1 134 ? 10.866 33.350 33.153 1.00 57.06  ?  289 CYS A O   1 
ATOM   963  C CB  . CYS A 1 134 ? 10.739 35.924 35.126 1.00 58.41  ?  289 CYS A CB  1 
ATOM   964  S SG  . CYS A 1 134 ? 11.658 36.895 36.343 1.00 63.28  ?  289 CYS A SG  1 
ATOM   965  N N   . LYS A 1 135 ? 10.038 35.154 32.056 1.00 54.20  ?  290 LYS A N   1 
ATOM   966  C CA  . LYS A 1 135 ? 9.260  34.389 31.072 1.00 53.76  ?  290 LYS A CA  1 
ATOM   967  C C   . LYS A 1 135 ? 10.230 33.592 30.184 1.00 54.71  ?  290 LYS A C   1 
ATOM   968  O O   . LYS A 1 135 ? 9.993  32.415 29.925 1.00 55.63  ?  290 LYS A O   1 
ATOM   969  C CB  . LYS A 1 135 ? 8.356  35.315 30.213 1.00 57.22  ?  290 LYS A CB  1 
ATOM   970  C CG  . LYS A 1 135 ? 7.589  34.545 29.111 1.00 74.09  ?  290 LYS A CG  1 
ATOM   971  C CD  . LYS A 1 135 ? 7.038  35.380 27.955 1.00 71.61  ?  290 LYS A CD  1 
ATOM   972  C CE  . LYS A 1 135 ? 6.092  34.502 27.156 1.00 59.70  ?  290 LYS A CE  1 
ATOM   973  N NZ  . LYS A 1 135 ? 5.420  35.218 26.029 1.00 54.85  1  290 LYS A NZ  1 
ATOM   974  N N   . ILE A 1 136 ? 11.324 34.247 29.734 1.00 47.66  ?  291 ILE A N   1 
ATOM   975  C CA  . ILE A 1 136 ? 12.358 33.647 28.888 1.00 45.54  ?  291 ILE A CA  1 
ATOM   976  C C   . ILE A 1 136 ? 13.036 32.502 29.621 1.00 47.37  ?  291 ILE A C   1 
ATOM   977  O O   . ILE A 1 136 ? 13.041 31.384 29.108 1.00 46.46  ?  291 ILE A O   1 
ATOM   978  C CB  . ILE A 1 136 ? 13.349 34.716 28.350 1.00 47.35  ?  291 ILE A CB  1 
ATOM   979  C CG1 . ILE A 1 136 ? 12.632 35.611 27.313 1.00 45.28  ?  291 ILE A CG1 1 
ATOM   980  C CG2 . ILE A 1 136 ? 14.604 34.049 27.748 1.00 47.90  ?  291 ILE A CG2 1 
ATOM   981  C CD1 . ILE A 1 136 ? 13.141 36.971 27.182 1.00 34.48  ?  291 ILE A CD1 1 
ATOM   982  N N   . ALA A 1 137 ? 13.533 32.763 30.841 1.00 43.39  ?  292 ALA A N   1 
ATOM   983  C CA  . ALA A 1 137 ? 14.170 31.747 31.666 1.00 43.75  ?  292 ALA A CA  1 
ATOM   984  C C   . ALA A 1 137 ? 13.306 30.501 31.805 1.00 48.15  ?  292 ALA A C   1 
ATOM   985  O O   . ALA A 1 137 ? 13.831 29.395 31.670 1.00 48.75  ?  292 ALA A O   1 
ATOM   986  C CB  . ALA A 1 137 ? 14.511 32.316 33.031 1.00 44.89  ?  292 ALA A CB  1 
ATOM   987  N N   . GLN A 1 138 ? 11.973 30.679 32.008 1.00 44.53  ?  293 GLN A N   1 
ATOM   988  C CA  . GLN A 1 138 ? 10.994 29.586 32.133 1.00 44.23  ?  293 GLN A CA  1 
ATOM   989  C C   . GLN A 1 138 ? 10.883 28.798 30.837 1.00 48.44  ?  293 GLN A C   1 
ATOM   990  O O   . GLN A 1 138 ? 11.087 27.584 30.836 1.00 49.58  ?  293 GLN A O   1 
ATOM   991  C CB  . GLN A 1 138 ? 9.621  30.109 32.589 1.00 45.36  ?  293 GLN A CB  1 
ATOM   992  C CG  . GLN A 1 138 ? 9.508  30.272 34.117 1.00 66.11  ?  293 GLN A CG  1 
ATOM   993  C CD  . GLN A 1 138 ? 8.465  31.270 34.602 1.00 81.04  ?  293 GLN A CD  1 
ATOM   994  O OE1 . GLN A 1 138 ? 7.523  31.676 33.885 1.00 68.33  ?  293 GLN A OE1 1 
ATOM   995  N NE2 . GLN A 1 138 ? 8.614  31.684 35.859 1.00 77.01  ?  293 GLN A NE2 1 
ATOM   996  N N   . GLY A 1 139 ? 10.630 29.502 29.745 1.00 43.58  ?  294 GLY A N   1 
ATOM   997  C CA  . GLY A 1 139 ? 10.499 28.921 28.418 1.00 42.96  ?  294 GLY A CA  1 
ATOM   998  C C   . GLY A 1 139 ? 11.739 28.179 27.990 1.00 46.06  ?  294 GLY A C   1 
ATOM   999  O O   . GLY A 1 139 ? 11.636 27.059 27.489 1.00 45.18  ?  294 GLY A O   1 
ATOM   1000 N N   . ALA A 1 140 ? 12.923 28.785 28.214 1.00 41.95  ?  295 ALA A N   1 
ATOM   1001 C CA  . ALA A 1 140 ? 14.203 28.159 27.889 1.00 41.83  ?  295 ALA A CA  1 
ATOM   1002 C C   . ALA A 1 140 ? 14.382 26.865 28.683 1.00 44.36  ?  295 ALA A C   1 
ATOM   1003 O O   . ALA A 1 140 ? 14.720 25.853 28.093 1.00 43.18  ?  295 ALA A O   1 
ATOM   1004 C CB  . ALA A 1 140 ? 15.347 29.123 28.147 1.00 42.79  ?  295 ALA A CB  1 
ATOM   1005 N N   . ALA A 1 141 ? 14.049 26.876 29.987 1.00 43.44  ?  296 ALA A N   1 
ATOM   1006 C CA  . ALA A 1 141 ? 14.112 25.684 30.840 1.00 44.63  ?  296 ALA A CA  1 
ATOM   1007 C C   . ALA A 1 141 ? 13.162 24.572 30.371 1.00 51.66  ?  296 ALA A C   1 
ATOM   1008 O O   . ALA A 1 141 ? 13.554 23.402 30.405 1.00 54.03  ?  296 ALA A O   1 
ATOM   1009 C CB  . ALA A 1 141 ? 13.830 26.044 32.290 1.00 45.44  ?  296 ALA A CB  1 
ATOM   1010 N N   . ASN A 1 142 ? 11.942 24.930 29.892 1.00 48.00  ?  297 ASN A N   1 
ATOM   1011 C CA  . ASN A 1 142 ? 10.944 23.975 29.380 1.00 48.50  ?  297 ASN A CA  1 
ATOM   1012 C C   . ASN A 1 142 ? 11.411 23.251 28.127 1.00 54.28  ?  297 ASN A C   1 
ATOM   1013 O O   . ASN A 1 142 ? 11.135 22.057 27.970 1.00 56.05  ?  297 ASN A O   1 
ATOM   1014 C CB  . ASN A 1 142 ? 9.590  24.644 29.129 1.00 50.69  ?  297 ASN A CB  1 
ATOM   1015 C CG  . ASN A 1 142 ? 8.916  25.221 30.358 1.00 84.13  ?  297 ASN A CG  1 
ATOM   1016 O OD1 . ASN A 1 142 ? 9.364  25.062 31.512 1.00 69.50  ?  297 ASN A OD1 1 
ATOM   1017 N ND2 . ASN A 1 142 ? 7.815  25.930 30.123 1.00 83.70  ?  297 ASN A ND2 1 
ATOM   1018 N N   . GLY A 1 143 ? 12.107 23.983 27.256 1.00 50.68  ?  298 GLY A N   1 
ATOM   1019 C CA  . GLY A 1 143 ? 12.682 23.468 26.022 1.00 50.39  ?  298 GLY A CA  1 
ATOM   1020 C C   . GLY A 1 143 ? 13.754 22.440 26.307 1.00 54.08  ?  298 GLY A C   1 
ATOM   1021 O O   . GLY A 1 143 ? 13.816 21.407 25.629 1.00 53.00  ?  298 GLY A O   1 
ATOM   1022 N N   . ILE A 1 144 ? 14.589 22.710 27.338 1.00 51.36  ?  299 ILE A N   1 
ATOM   1023 C CA  . ILE A 1 144 ? 15.663 21.798 27.766 1.00 52.53  ?  299 ILE A CA  1 
ATOM   1024 C C   . ILE A 1 144 ? 15.034 20.532 28.376 1.00 56.36  ?  299 ILE A C   1 
ATOM   1025 O O   . ILE A 1 144 ? 15.521 19.426 28.127 1.00 55.52  ?  299 ILE A O   1 
ATOM   1026 C CB  . ILE A 1 144 ? 16.744 22.478 28.685 1.00 55.57  ?  299 ILE A CB  1 
ATOM   1027 C CG1 . ILE A 1 144 ? 17.433 23.667 27.974 1.00 55.60  ?  299 ILE A CG1 1 
ATOM   1028 C CG2 . ILE A 1 144 ? 17.803 21.460 29.133 1.00 56.26  ?  299 ILE A CG2 1 
ATOM   1029 C CD1 . ILE A 1 144 ? 18.230 24.583 28.866 1.00 63.14  ?  299 ILE A CD1 1 
ATOM   1030 N N   . ASN A 1 145 ? 13.911 20.703 29.113 1.00 52.63  ?  300 ASN A N   1 
ATOM   1031 C CA  . ASN A 1 145 ? 13.168 19.595 29.709 1.00 51.81  ?  300 ASN A CA  1 
ATOM   1032 C C   . ASN A 1 145 ? 12.635 18.668 28.650 1.00 53.93  ?  300 ASN A C   1 
ATOM   1033 O O   . ASN A 1 145 ? 12.821 17.456 28.762 1.00 54.98  ?  300 ASN A O   1 
ATOM   1034 C CB  . ASN A 1 145 ? 12.049 20.079 30.615 1.00 53.37  ?  300 ASN A CB  1 
ATOM   1035 C CG  . ASN A 1 145 ? 11.283 18.939 31.228 1.00 74.84  ?  300 ASN A CG  1 
ATOM   1036 O OD1 . ASN A 1 145 ? 11.791 18.185 32.062 1.00 74.26  ?  300 ASN A OD1 1 
ATOM   1037 N ND2 . ASN A 1 145 ? 10.061 18.751 30.780 1.00 67.04  ?  300 ASN A ND2 1 
ATOM   1038 N N   . PHE A 1 146 ? 12.016 19.231 27.602 1.00 47.26  ?  301 PHE A N   1 
ATOM   1039 C CA  . PHE A 1 146 ? 11.498 18.435 26.503 1.00 46.37  ?  301 PHE A CA  1 
ATOM   1040 C C   . PHE A 1 146 ? 12.610 17.621 25.808 1.00 53.49  ?  301 PHE A C   1 
ATOM   1041 O O   . PHE A 1 146 ? 12.381 16.460 25.470 1.00 53.44  ?  301 PHE A O   1 
ATOM   1042 C CB  . PHE A 1 146 ? 10.739 19.318 25.514 1.00 47.07  ?  301 PHE A CB  1 
ATOM   1043 C CG  . PHE A 1 146 ? 10.253 18.587 24.285 1.00 46.94  ?  301 PHE A CG  1 
ATOM   1044 C CD1 . PHE A 1 146 ? 9.067  17.863 24.309 1.00 46.95  ?  301 PHE A CD1 1 
ATOM   1045 C CD2 . PHE A 1 146 ? 10.987 18.621 23.097 1.00 48.34  ?  301 PHE A CD2 1 
ATOM   1046 C CE1 . PHE A 1 146 ? 8.622  17.186 23.169 1.00 47.69  ?  301 PHE A CE1 1 
ATOM   1047 C CE2 . PHE A 1 146 ? 10.540 17.946 21.957 1.00 50.66  ?  301 PHE A CE2 1 
ATOM   1048 C CZ  . PHE A 1 146 ? 9.364  17.227 22.001 1.00 47.96  ?  301 PHE A CZ  1 
ATOM   1049 N N   . LEU A 1 147 ? 13.800 18.228 25.606 1.00 52.02  ?  302 LEU A N   1 
ATOM   1050 C CA  . LEU A 1 147 ? 14.949 17.581 24.968 1.00 52.12  ?  302 LEU A CA  1 
ATOM   1051 C C   . LEU A 1 147 ? 15.461 16.441 25.806 1.00 56.47  ?  302 LEU A C   1 
ATOM   1052 O O   . LEU A 1 147 ? 15.744 15.385 25.259 1.00 55.97  ?  302 LEU A O   1 
ATOM   1053 C CB  . LEU A 1 147 ? 16.082 18.575 24.699 1.00 52.14  ?  302 LEU A CB  1 
ATOM   1054 C CG  . LEU A 1 147 ? 15.899 19.509 23.521 1.00 57.38  ?  302 LEU A CG  1 
ATOM   1055 C CD1 . LEU A 1 147 ? 16.894 20.643 23.580 1.00 58.00  ?  302 LEU A CD1 1 
ATOM   1056 C CD2 . LEU A 1 147 ? 16.041 18.766 22.195 1.00 58.69  ?  302 LEU A CD2 1 
ATOM   1057 N N   . HIS A 1 148 ? 15.556 16.646 27.132 1.00 53.12  ?  303 HIS A N   1 
ATOM   1058 C CA  . HIS A 1 148 ? 16.030 15.649 28.086 1.00 53.17  ?  303 HIS A CA  1 
ATOM   1059 C C   . HIS A 1 148 ? 15.036 14.491 28.243 1.00 60.35  ?  303 HIS A C   1 
ATOM   1060 O O   . HIS A 1 148 ? 15.448 13.329 28.170 1.00 61.11  ?  303 HIS A O   1 
ATOM   1061 C CB  . HIS A 1 148 ? 16.385 16.308 29.430 1.00 53.24  ?  303 HIS A CB  1 
ATOM   1062 C CG  . HIS A 1 148 ? 17.631 17.149 29.391 1.00 55.89  ?  303 HIS A CG  1 
ATOM   1063 N ND1 . HIS A 1 148 ? 18.255 17.552 30.558 1.00 57.82  ?  303 HIS A ND1 1 
ATOM   1064 C CD2 . HIS A 1 148 ? 18.333 17.622 28.335 1.00 56.73  ?  303 HIS A CD2 1 
ATOM   1065 C CE1 . HIS A 1 148 ? 19.299 18.274 30.176 1.00 56.95  ?  303 HIS A CE1 1 
ATOM   1066 N NE2 . HIS A 1 148 ? 19.387 18.337 28.845 1.00 56.88  ?  303 HIS A NE2 1 
ATOM   1067 N N   . GLU A 1 149 ? 13.725 14.804 28.368 1.00 57.99  ?  304 GLU A N   1 
ATOM   1068 C CA  . GLU A 1 149 ? 12.635 13.820 28.436 1.00 58.03  ?  304 GLU A CA  1 
ATOM   1069 C C   . GLU A 1 149 ? 12.650 12.900 27.207 1.00 62.99  ?  304 GLU A C   1 
ATOM   1070 O O   . GLU A 1 149 ? 12.186 11.760 27.284 1.00 64.26  ?  304 GLU A O   1 
ATOM   1071 C CB  . GLU A 1 149 ? 11.277 14.529 28.494 1.00 59.40  ?  304 GLU A CB  1 
ATOM   1072 C CG  . GLU A 1 149 ? 10.832 14.920 29.894 1.00 74.61  ?  304 GLU A CG  1 
ATOM   1073 C CD  . GLU A 1 149 ? 9.458  15.568 29.977 1.00 101.02 ?  304 GLU A CD  1 
ATOM   1074 O OE1 . GLU A 1 149 ? 8.974  16.088 28.944 1.00 88.24  ?  304 GLU A OE1 1 
ATOM   1075 O OE2 . GLU A 1 149 ? 8.879  15.584 31.090 1.00 101.25 -1 304 GLU A OE2 1 
ATOM   1076 N N   . ASN A 1 150 ? 13.172 13.410 26.079 1.00 58.84  ?  305 ASN A N   1 
ATOM   1077 C CA  . ASN A 1 150 ? 13.284 12.699 24.812 1.00 58.74  ?  305 ASN A CA  1 
ATOM   1078 C C   . ASN A 1 150 ? 14.683 12.145 24.582 1.00 62.93  ?  305 ASN A C   1 
ATOM   1079 O O   . ASN A 1 150 ? 15.045 11.833 23.443 1.00 62.11  ?  305 ASN A O   1 
ATOM   1080 C CB  . ASN A 1 150 ? 12.823 13.576 23.654 1.00 58.87  ?  305 ASN A CB  1 
ATOM   1081 C CG  . ASN A 1 150 ? 11.333 13.737 23.604 1.00 78.27  ?  305 ASN A CG  1 
ATOM   1082 O OD1 . ASN A 1 150 ? 10.693 14.240 24.545 1.00 60.31  ?  305 ASN A OD1 1 
ATOM   1083 N ND2 . ASN A 1 150 ? 10.748 13.327 22.486 1.00 76.53  ?  305 ASN A ND2 1 
ATOM   1084 N N   . HIS A 1 151 ? 15.449 11.976 25.681 1.00 61.27  ?  306 HIS A N   1 
ATOM   1085 C CA  . HIS A 1 151 ? 16.796 11.401 25.715 1.00 62.46  ?  306 HIS A CA  1 
ATOM   1086 C C   . HIS A 1 151 ? 17.744 12.076 24.735 1.00 64.04  ?  306 HIS A C   1 
ATOM   1087 O O   . HIS A 1 151 ? 18.375 11.406 23.907 1.00 62.74  ?  306 HIS A O   1 
ATOM   1088 C CB  . HIS A 1 151 ? 16.757 9.873  25.496 1.00 64.97  ?  306 HIS A CB  1 
ATOM   1089 C CG  . HIS A 1 151 ? 15.789 9.167  26.386 1.00 69.98  ?  306 HIS A CG  1 
ATOM   1090 N ND1 . HIS A 1 151 ? 16.152 8.744  27.652 1.00 72.65  ?  306 HIS A ND1 1 
ATOM   1091 C CD2 . HIS A 1 151 ? 14.487 8.861  26.172 1.00 72.85  ?  306 HIS A CD2 1 
ATOM   1092 C CE1 . HIS A 1 151 ? 15.072 8.174  28.159 1.00 72.67  ?  306 HIS A CE1 1 
ATOM   1093 N NE2 . HIS A 1 151 ? 14.042 8.224  27.305 1.00 73.01  ?  306 HIS A NE2 1 
ATOM   1094 N N   . HIS A 1 152 ? 17.797 13.423 24.810 1.00 60.13  ?  307 HIS A N   1 
ATOM   1095 C CA  . HIS A 1 152 ? 18.641 14.294 23.980 1.00 58.91  ?  307 HIS A CA  1 
ATOM   1096 C C   . HIS A 1 152 ? 19.401 15.316 24.806 1.00 60.45  ?  307 HIS A C   1 
ATOM   1097 O O   . HIS A 1 152 ? 18.845 15.924 25.721 1.00 58.55  ?  307 HIS A O   1 
ATOM   1098 C CB  . HIS A 1 152 ? 17.817 15.031 22.917 1.00 59.62  ?  307 HIS A CB  1 
ATOM   1099 C CG  . HIS A 1 152 ? 17.568 14.238 21.685 1.00 63.12  ?  307 HIS A CG  1 
ATOM   1100 N ND1 . HIS A 1 152 ? 16.296 13.825 21.346 1.00 65.23  ?  307 HIS A ND1 1 
ATOM   1101 C CD2 . HIS A 1 152 ? 18.438 13.817 20.740 1.00 65.17  ?  307 HIS A CD2 1 
ATOM   1102 C CE1 . HIS A 1 152 ? 16.429 13.152 20.214 1.00 64.79  ?  307 HIS A CE1 1 
ATOM   1103 N NE2 . HIS A 1 152 ? 17.702 13.124 19.806 1.00 65.03  ?  307 HIS A NE2 1 
ATOM   1104 N N   . ILE A 1 153 ? 20.681 15.512 24.458 1.00 58.27  ?  308 ILE A N   1 
ATOM   1105 C CA  . ILE A 1 153 ? 21.598 16.486 25.078 1.00 57.04  ?  308 ILE A CA  1 
ATOM   1106 C C   . ILE A 1 153 ? 21.856 17.530 23.996 1.00 59.35  ?  308 ILE A C   1 
ATOM   1107 O O   . ILE A 1 153 ? 22.166 17.161 22.854 1.00 58.78  ?  308 ILE A O   1 
ATOM   1108 C CB  . ILE A 1 153 ? 22.901 15.826 25.608 1.00 58.62  ?  308 ILE A CB  1 
ATOM   1109 C CG1 . ILE A 1 153 ? 22.559 14.667 26.585 1.00 59.16  ?  308 ILE A CG1 1 
ATOM   1110 C CG2 . ILE A 1 153 ? 23.802 16.865 26.282 1.00 55.89  ?  308 ILE A CG2 1 
ATOM   1111 C CD1 . ILE A 1 153 ? 23.432 13.496 26.469 1.00 67.75  ?  308 ILE A CD1 1 
ATOM   1112 N N   . HIS A 1 154 ? 21.654 18.820 24.336 1.00 53.34  ?  309 HIS A N   1 
ATOM   1113 C CA  . HIS A 1 154 ? 21.821 19.907 23.379 1.00 51.66  ?  309 HIS A CA  1 
ATOM   1114 C C   . HIS A 1 154 ? 23.282 20.135 23.016 1.00 53.11  ?  309 HIS A C   1 
ATOM   1115 O O   . HIS A 1 154 ? 23.594 20.300 21.831 1.00 51.25  ?  309 HIS A O   1 
ATOM   1116 C CB  . HIS A 1 154 ? 21.157 21.191 23.889 1.00 51.89  ?  309 HIS A CB  1 
ATOM   1117 C CG  . HIS A 1 154 ? 21.111 22.277 22.861 1.00 54.43  ?  309 HIS A CG  1 
ATOM   1118 N ND1 . HIS A 1 154 ? 22.205 23.074 22.607 1.00 55.69  ?  309 HIS A ND1 1 
ATOM   1119 C CD2 . HIS A 1 154 ? 20.097 22.665 22.065 1.00 55.23  ?  309 HIS A CD2 1 
ATOM   1120 C CE1 . HIS A 1 154 ? 21.824 23.918 21.669 1.00 54.51  ?  309 HIS A CE1 1 
ATOM   1121 N NE2 . HIS A 1 154 ? 20.565 23.711 21.313 1.00 54.72  ?  309 HIS A NE2 1 
ATOM   1122 N N   . ARG A 1 155 ? 24.170 20.167 24.043 1.00 49.20  ?  310 ARG A N   1 
ATOM   1123 C CA  . ARG A 1 155 ? 25.630 20.354 23.908 1.00 48.68  ?  310 ARG A CA  1 
ATOM   1124 C C   . ARG A 1 155 ? 26.095 21.817 23.569 1.00 51.02  ?  310 ARG A C   1 
ATOM   1125 O O   . ARG A 1 155 ? 27.295 22.097 23.610 1.00 50.22  ?  310 ARG A O   1 
ATOM   1126 C CB  . ARG A 1 155 ? 26.253 19.315 22.931 1.00 48.94  ?  310 ARG A CB  1 
ATOM   1127 C CG  . ARG A 1 155 ? 26.062 17.838 23.323 1.00 58.79  ?  310 ARG A CG  1 
ATOM   1128 C CD  . ARG A 1 155 ? 26.842 16.865 22.437 1.00 61.72  ?  310 ARG A CD  1 
ATOM   1129 N NE  . ARG A 1 155 ? 28.291 17.091 22.464 1.00 70.46  ?  310 ARG A NE  1 
ATOM   1130 C CZ  . ARG A 1 155 ? 29.117 16.829 21.452 1.00 86.39  ?  310 ARG A CZ  1 
ATOM   1131 N NH1 . ARG A 1 155 ? 28.645 16.344 20.308 1.00 62.69  ?  310 ARG A NH1 1 
ATOM   1132 N NH2 . ARG A 1 155 ? 30.420 17.055 21.574 1.00 78.28  1  310 ARG A NH2 1 
ATOM   1133 N N   . ASP A 1 156 ? 25.160 22.727 23.220 1.00 46.54  ?  311 ASP A N   1 
ATOM   1134 C CA  . ASP A 1 156 ? 25.504 24.107 22.851 1.00 45.62  ?  311 ASP A CA  1 
ATOM   1135 C C   . ASP A 1 156 ? 24.539 25.165 23.448 1.00 45.00  ?  311 ASP A C   1 
ATOM   1136 O O   . ASP A 1 156 ? 24.226 26.166 22.812 1.00 44.78  ?  311 ASP A O   1 
ATOM   1137 C CB  . ASP A 1 156 ? 25.681 24.233 21.315 1.00 47.50  ?  311 ASP A CB  1 
ATOM   1138 C CG  . ASP A 1 156 ? 26.547 25.395 20.829 1.00 59.42  ?  311 ASP A CG  1 
ATOM   1139 O OD1 . ASP A 1 156 ? 27.290 25.992 21.666 1.00 60.84  ?  311 ASP A OD1 1 
ATOM   1140 O OD2 . ASP A 1 156 ? 26.482 25.713 19.623 1.00 62.92  -1 311 ASP A OD2 1 
ATOM   1141 N N   . ILE A 1 157 ? 24.091 24.938 24.682 1.00 39.31  ?  312 ILE A N   1 
ATOM   1142 C CA  . ILE A 1 157 ? 23.232 25.861 25.399 1.00 38.99  ?  312 ILE A CA  1 
ATOM   1143 C C   . ILE A 1 157 ? 23.980 27.160 25.692 1.00 44.82  ?  312 ILE A C   1 
ATOM   1144 O O   . ILE A 1 157 ? 25.001 27.166 26.388 1.00 46.08  ?  312 ILE A O   1 
ATOM   1145 C CB  . ILE A 1 157 ? 22.584 25.231 26.666 1.00 41.72  ?  312 ILE A CB  1 
ATOM   1146 C CG1 . ILE A 1 157 ? 21.610 24.068 26.299 1.00 41.80  ?  312 ILE A CG1 1 
ATOM   1147 C CG2 . ILE A 1 157 ? 21.910 26.307 27.568 1.00 41.78  ?  312 ILE A CG2 1 
ATOM   1148 C CD1 . ILE A 1 157 ? 20.289 24.471 25.472 1.00 52.40  ?  312 ILE A CD1 1 
ATOM   1149 N N   . LYS A 1 158 ? 23.500 28.252 25.085 1.00 38.77  ?  313 LYS A N   1 
ATOM   1150 C CA  . LYS A 1 158 ? 24.043 29.587 25.263 1.00 36.59  ?  313 LYS A CA  1 
ATOM   1151 C C   . LYS A 1 158 ? 22.962 30.562 24.895 1.00 42.09  ?  313 LYS A C   1 
ATOM   1152 O O   . LYS A 1 158 ? 21.969 30.146 24.280 1.00 43.22  ?  313 LYS A O   1 
ATOM   1153 C CB  . LYS A 1 158 ? 25.326 29.792 24.454 1.00 37.74  ?  313 LYS A CB  1 
ATOM   1154 C CG  . LYS A 1 158 ? 25.274 29.440 22.973 1.00 39.22  ?  313 LYS A CG  1 
ATOM   1155 C CD  . LYS A 1 158 ? 26.463 30.094 22.311 1.00 32.92  ?  313 LYS A CD  1 
ATOM   1156 C CE  . LYS A 1 158 ? 26.865 29.417 21.048 1.00 32.14  ?  313 LYS A CE  1 
ATOM   1157 N NZ  . LYS A 1 158 ? 28.112 30.029 20.548 1.00 40.72  1  313 LYS A NZ  1 
ATOM   1158 N N   . SER A 1 159 ? 23.117 31.852 25.272 1.00 37.85  ?  314 SER A N   1 
ATOM   1159 C CA  . SER A 1 159 ? 22.101 32.864 24.969 1.00 37.66  ?  314 SER A CA  1 
ATOM   1160 C C   . SER A 1 159 ? 21.937 33.164 23.466 1.00 40.52  ?  314 SER A C   1 
ATOM   1161 O O   . SER A 1 159 ? 20.870 33.594 23.058 1.00 40.75  ?  314 SER A O   1 
ATOM   1162 C CB  . SER A 1 159 ? 22.312 34.125 25.795 1.00 40.98  ?  314 SER A CB  1 
ATOM   1163 O OG  . SER A 1 159 ? 23.625 34.610 25.602 1.00 49.55  ?  314 SER A OG  1 
ATOM   1164 N N   . ALA A 1 160 ? 22.950 32.881 22.643 1.00 36.60  ?  315 ALA A N   1 
ATOM   1165 C CA  . ALA A 1 160 ? 22.824 33.066 21.196 1.00 36.57  ?  315 ALA A CA  1 
ATOM   1166 C C   . ALA A 1 160 ? 21.896 31.977 20.608 1.00 42.04  ?  315 ALA A C   1 
ATOM   1167 O O   . ALA A 1 160 ? 21.280 32.183 19.562 1.00 42.60  ?  315 ALA A O   1 
ATOM   1168 C CB  . ALA A 1 160 ? 24.180 32.993 20.540 1.00 36.72  ?  315 ALA A CB  1 
ATOM   1169 N N   . ASN A 1 161 ? 21.793 30.831 21.298 1.00 37.18  ?  316 ASN A N   1 
ATOM   1170 C CA  . ASN A 1 161 ? 20.972 29.689 20.900 1.00 36.39  ?  316 ASN A CA  1 
ATOM   1171 C C   . ASN A 1 161 ? 19.599 29.647 21.576 1.00 39.47  ?  316 ASN A C   1 
ATOM   1172 O O   . ASN A 1 161 ? 18.974 28.597 21.634 1.00 39.91  ?  316 ASN A O   1 
ATOM   1173 C CB  . ASN A 1 161 ? 21.759 28.377 21.063 1.00 33.80  ?  316 ASN A CB  1 
ATOM   1174 C CG  . ASN A 1 161 ? 22.823 28.202 19.997 1.00 52.31  ?  316 ASN A CG  1 
ATOM   1175 O OD1 . ASN A 1 161 ? 22.823 28.867 18.943 1.00 39.29  ?  316 ASN A OD1 1 
ATOM   1176 N ND2 . ASN A 1 161 ? 23.757 27.294 20.239 1.00 41.45  ?  316 ASN A ND2 1 
ATOM   1177 N N   . ILE A 1 162 ? 19.158 30.783 22.127 1.00 36.14  ?  317 ILE A N   1 
ATOM   1178 C CA  . ILE A 1 162 ? 17.827 30.956 22.708 1.00 35.83  ?  317 ILE A CA  1 
ATOM   1179 C C   . ILE A 1 162 ? 17.216 32.094 21.907 1.00 38.15  ?  317 ILE A C   1 
ATOM   1180 O O   . ILE A 1 162 ? 17.614 33.257 22.025 1.00 35.80  ?  317 ILE A O   1 
ATOM   1181 C CB  . ILE A 1 162 ? 17.791 31.201 24.231 1.00 39.37  ?  317 ILE A CB  1 
ATOM   1182 C CG1 . ILE A 1 162 ? 18.400 29.992 24.980 1.00 41.11  ?  317 ILE A CG1 1 
ATOM   1183 C CG2 . ILE A 1 162 ? 16.344 31.461 24.673 1.00 38.02  ?  317 ILE A CG2 1 
ATOM   1184 C CD1 . ILE A 1 162 ? 18.848 30.270 26.393 1.00 48.85  ?  317 ILE A CD1 1 
ATOM   1185 N N   . LEU A 1 163 ? 16.342 31.716 20.997 1.00 35.64  ?  318 LEU A N   1 
ATOM   1186 C CA  . LEU A 1 163 ? 15.684 32.630 20.081 1.00 36.03  ?  318 LEU A CA  1 
ATOM   1187 C C   . LEU A 1 163 ? 14.312 33.088 20.600 1.00 39.90  ?  318 LEU A C   1 
ATOM   1188 O O   . LEU A 1 163 ? 13.732 32.456 21.493 1.00 39.29  ?  318 LEU A O   1 
ATOM   1189 C CB  . LEU A 1 163 ? 15.652 32.002 18.681 1.00 36.23  ?  318 LEU A CB  1 
ATOM   1190 C CG  . LEU A 1 163 ? 16.840 32.332 17.726 1.00 40.20  ?  318 LEU A CG  1 
ATOM   1191 C CD1 . LEU A 1 163 ? 18.175 32.436 18.435 1.00 39.62  ?  318 LEU A CD1 1 
ATOM   1192 C CD2 . LEU A 1 163 ? 16.956 31.316 16.672 1.00 38.98  ?  318 LEU A CD2 1 
ATOM   1193 N N   . LEU A 1 164 ? 13.848 34.238 20.118 1.00 36.59  ?  319 LEU A N   1 
ATOM   1194 C CA  . LEU A 1 164 ? 12.622 34.862 20.628 1.00 36.55  ?  319 LEU A CA  1 
ATOM   1195 C C   . LEU A 1 164 ? 11.638 35.294 19.544 1.00 42.70  ?  319 LEU A C   1 
ATOM   1196 O O   . LEU A 1 164 ? 12.041 35.953 18.568 1.00 44.38  ?  319 LEU A O   1 
ATOM   1197 C CB  . LEU A 1 164 ? 12.988 36.096 21.504 1.00 35.90  ?  319 LEU A CB  1 
ATOM   1198 C CG  . LEU A 1 164 ? 14.017 35.920 22.634 1.00 38.90  ?  319 LEU A CG  1 
ATOM   1199 C CD1 . LEU A 1 164 ? 14.591 37.232 23.050 1.00 38.81  ?  319 LEU A CD1 1 
ATOM   1200 C CD2 . LEU A 1 164 ? 13.429 35.217 23.826 1.00 38.38  ?  319 LEU A CD2 1 
ATOM   1201 N N   . ASP A 1 165 ? 10.338 34.985 19.752 1.00 37.97  ?  320 ASP A N   1 
ATOM   1202 C CA  . ASP A 1 165 ? 9.263  35.395 18.839 1.00 37.29  ?  320 ASP A CA  1 
ATOM   1203 C C   . ASP A 1 165 ? 8.736  36.781 19.232 1.00 43.22  ?  320 ASP A C   1 
ATOM   1204 O O   . ASP A 1 165 ? 9.298  37.408 20.142 1.00 42.30  ?  320 ASP A O   1 
ATOM   1205 C CB  . ASP A 1 165 ? 8.143  34.331 18.762 1.00 38.52  ?  320 ASP A CB  1 
ATOM   1206 C CG  . ASP A 1 165 ? 7.248  34.147 19.985 1.00 52.14  ?  320 ASP A CG  1 
ATOM   1207 O OD1 . ASP A 1 165 ? 7.362  34.943 20.935 1.00 55.46  ?  320 ASP A OD1 1 
ATOM   1208 O OD2 . ASP A 1 165 ? 6.405  33.229 19.970 1.00 57.95  -1 320 ASP A OD2 1 
ATOM   1209 N N   . GLU A 1 166 ? 7.640  37.247 18.565 1.00 41.67  ?  321 GLU A N   1 
ATOM   1210 C CA  . GLU A 1 166 ? 6.962  38.537 18.806 1.00 41.22  ?  321 GLU A CA  1 
ATOM   1211 C C   . GLU A 1 166 ? 6.589  38.685 20.289 1.00 41.84  ?  321 GLU A C   1 
ATOM   1212 O O   . GLU A 1 166 ? 6.746  39.762 20.849 1.00 41.58  ?  321 GLU A O   1 
ATOM   1213 C CB  . GLU A 1 166 ? 5.667  38.669 17.964 1.00 42.83  ?  321 GLU A CB  1 
ATOM   1214 C CG  . GLU A 1 166 ? 5.831  38.531 16.452 1.00 62.38  ?  321 GLU A CG  1 
ATOM   1215 C CD  . GLU A 1 166 ? 5.649  37.138 15.853 1.00 86.62  ?  321 GLU A CD  1 
ATOM   1216 O OE1 . GLU A 1 166 ? 6.243  36.166 16.386 1.00 64.22  ?  321 GLU A OE1 1 
ATOM   1217 O OE2 . GLU A 1 166 ? 4.961  37.029 14.809 1.00 76.81  -1 321 GLU A OE2 1 
ATOM   1218 N N   . ALA A 1 167 ? 6.087  37.605 20.906 1.00 35.73  ?  322 ALA A N   1 
ATOM   1219 C CA  . ALA A 1 167 ? 5.655  37.579 22.302 1.00 35.36  ?  322 ALA A CA  1 
ATOM   1220 C C   . ALA A 1 167 ? 6.800  37.275 23.295 1.00 41.55  ?  322 ALA A C   1 
ATOM   1221 O O   . ALA A 1 167 ? 6.533  37.093 24.486 1.00 44.26  ?  322 ALA A O   1 
ATOM   1222 C CB  . ALA A 1 167 ? 4.532  36.559 22.465 1.00 35.62  ?  322 ALA A CB  1 
ATOM   1223 N N   . PHE A 1 168 ? 8.056  37.213 22.821 1.00 35.14  ?  323 PHE A N   1 
ATOM   1224 C CA  . PHE A 1 168 ? 9.219  36.904 23.665 1.00 35.62  ?  323 PHE A CA  1 
ATOM   1225 C C   . PHE A 1 168 ? 9.180  35.487 24.268 1.00 40.41  ?  323 PHE A C   1 
ATOM   1226 O O   . PHE A 1 168 ? 9.641  35.263 25.388 1.00 39.75  ?  323 PHE A O   1 
ATOM   1227 C CB  . PHE A 1 168 ? 9.481  37.988 24.738 1.00 36.48  ?  323 PHE A CB  1 
ATOM   1228 C CG  . PHE A 1 168 ? 9.669  39.386 24.195 1.00 35.43  ?  323 PHE A CG  1 
ATOM   1229 C CD1 . PHE A 1 168 ? 8.597  40.266 24.116 1.00 35.56  ?  323 PHE A CD1 1 
ATOM   1230 C CD2 . PHE A 1 168 ? 10.914 39.810 23.744 1.00 35.11  ?  323 PHE A CD2 1 
ATOM   1231 C CE1 . PHE A 1 168 ? 8.768  41.552 23.614 1.00 36.16  ?  323 PHE A CE1 1 
ATOM   1232 C CE2 . PHE A 1 168 ? 11.083 41.091 23.225 1.00 37.46  ?  323 PHE A CE2 1 
ATOM   1233 C CZ  . PHE A 1 168 ? 10.012 41.959 23.173 1.00 35.58  ?  323 PHE A CZ  1 
ATOM   1234 N N   . THR A 1 169 ? 8.594  34.541 23.524 1.00 36.87  ?  324 THR A N   1 
ATOM   1235 C CA  . THR A 1 169 ? 8.568  33.137 23.903 1.00 37.25  ?  324 THR A CA  1 
ATOM   1236 C C   . THR A 1 169 ? 9.968  32.610 23.532 1.00 44.42  ?  324 THR A C   1 
ATOM   1237 O O   . THR A 1 169 ? 10.440 32.833 22.411 1.00 44.92  ?  324 THR A O   1 
ATOM   1238 C CB  . THR A 1 169 ? 7.404  32.398 23.181 1.00 45.06  ?  324 THR A CB  1 
ATOM   1239 O OG1 . THR A 1 169 ? 6.166  32.828 23.728 1.00 44.17  ?  324 THR A OG1 1 
ATOM   1240 C CG2 . THR A 1 169 ? 7.495  30.869 23.273 1.00 39.80  ?  324 THR A CG2 1 
ATOM   1241 N N   . ALA A 1 170 ? 10.650 31.967 24.500 1.00 41.40  ?  325 ALA A N   1 
ATOM   1242 C CA  . ALA A 1 170 ? 11.976 31.384 24.320 1.00 39.12  ?  325 ALA A CA  1 
ATOM   1243 C C   . ALA A 1 170 ? 11.862 30.173 23.411 1.00 41.73  ?  325 ALA A C   1 
ATOM   1244 O O   . ALA A 1 170 ? 10.922 29.377 23.506 1.00 39.46  ?  325 ALA A O   1 
ATOM   1245 C CB  . ALA A 1 170 ? 12.549 30.975 25.653 1.00 39.54  ?  325 ALA A CB  1 
ATOM   1246 N N   . LYS A 1 171 ? 12.798 30.091 22.481 1.00 39.16  ?  326 LYS A N   1 
ATOM   1247 C CA  . LYS A 1 171 ? 12.867 29.019 21.518 1.00 39.27  ?  326 LYS A CA  1 
ATOM   1248 C C   . LYS A 1 171 ? 14.335 28.567 21.315 1.00 42.73  ?  326 LYS A C   1 
ATOM   1249 O O   . LYS A 1 171 ? 15.126 29.298 20.713 1.00 42.11  ?  326 LYS A O   1 
ATOM   1250 C CB  . LYS A 1 171 ? 12.172 29.449 20.210 1.00 41.87  ?  326 LYS A CB  1 
ATOM   1251 C CG  . LYS A 1 171 ? 10.723 29.006 20.171 1.00 38.15  ?  326 LYS A CG  1 
ATOM   1252 C CD  . LYS A 1 171 ? 9.859  29.968 19.401 1.00 40.78  ?  326 LYS A CD  1 
ATOM   1253 C CE  . LYS A 1 171 ? 8.389  29.766 19.699 1.00 40.60  ?  326 LYS A CE  1 
ATOM   1254 N NZ  . LYS A 1 171 ? 7.897  28.424 19.242 1.00 56.58  1  326 LYS A NZ  1 
ATOM   1255 N N   . ILE A 1 172 ? 14.690 27.376 21.862 1.00 37.79  ?  327 ILE A N   1 
ATOM   1256 C CA  . ILE A 1 172 ? 16.019 26.764 21.764 1.00 36.74  ?  327 ILE A CA  1 
ATOM   1257 C C   . ILE A 1 172 ? 16.312 26.457 20.276 1.00 40.22  ?  327 ILE A C   1 
ATOM   1258 O O   . ILE A 1 172 ? 15.478 25.867 19.595 1.00 38.75  ?  327 ILE A O   1 
ATOM   1259 C CB  . ILE A 1 172 ? 16.080 25.449 22.604 1.00 40.28  ?  327 ILE A CB  1 
ATOM   1260 C CG1 . ILE A 1 172 ? 15.575 25.578 24.080 1.00 40.61  ?  327 ILE A CG1 1 
ATOM   1261 C CG2 . ILE A 1 172 ? 17.412 24.726 22.471 1.00 42.27  ?  327 ILE A CG2 1 
ATOM   1262 C CD1 . ILE A 1 172 ? 16.538 26.210 25.162 1.00 43.30  ?  327 ILE A CD1 1 
ATOM   1263 N N   . SER A 1 173 ? 17.494 26.850 19.794 1.00 38.20  ?  328 SER A N   1 
ATOM   1264 C CA  . SER A 1 173 ? 17.943 26.593 18.433 1.00 39.53  ?  328 SER A CA  1 
ATOM   1265 C C   . SER A 1 173 ? 19.296 25.858 18.439 1.00 48.95  ?  328 SER A C   1 
ATOM   1266 O O   . SER A 1 173 ? 19.842 25.582 19.517 1.00 48.59  ?  328 SER A O   1 
ATOM   1267 C CB  . SER A 1 173 ? 18.063 27.893 17.650 1.00 39.91  ?  328 SER A CB  1 
ATOM   1268 O OG  . SER A 1 173 ? 19.165 28.641 18.124 1.00 48.46  ?  328 SER A OG  1 
ATOM   1269 N N   . ASP A 1 174 ? 19.828 25.563 17.221 1.00 47.41  ?  329 ASP A N   1 
ATOM   1270 C CA  . ASP A 1 174 ? 21.122 24.935 16.944 1.00 47.47  ?  329 ASP A CA  1 
ATOM   1271 C C   . ASP A 1 174 ? 21.292 23.545 17.554 1.00 52.18  ?  329 ASP A C   1 
ATOM   1272 O O   . ASP A 1 174 ? 21.837 23.399 18.652 1.00 50.79  ?  329 ASP A O   1 
ATOM   1273 C CB  . ASP A 1 174 ? 22.292 25.895 17.259 1.00 49.57  ?  329 ASP A CB  1 
ATOM   1274 C CG  . ASP A 1 174 ? 23.506 25.777 16.354 1.00 67.85  ?  329 ASP A CG  1 
ATOM   1275 O OD1 . ASP A 1 174 ? 24.598 26.237 16.762 1.00 69.17  ?  329 ASP A OD1 1 
ATOM   1276 O OD2 . ASP A 1 174 ? 23.363 25.248 15.225 1.00 78.54  -1 329 ASP A OD2 1 
ATOM   1277 N N   . PHE A 1 175 ? 20.849 22.522 16.815 1.00 51.29  ?  330 PHE A N   1 
ATOM   1278 C CA  . PHE A 1 175 ? 20.915 21.122 17.235 1.00 53.02  ?  330 PHE A CA  1 
ATOM   1279 C C   . PHE A 1 175 ? 21.945 20.299 16.444 1.00 57.71  ?  330 PHE A C   1 
ATOM   1280 O O   . PHE A 1 175 ? 21.916 19.071 16.487 1.00 57.16  ?  330 PHE A O   1 
ATOM   1281 C CB  . PHE A 1 175 ? 19.510 20.488 17.204 1.00 55.74  ?  330 PHE A CB  1 
ATOM   1282 C CG  . PHE A 1 175 ? 18.471 21.239 18.008 1.00 58.19  ?  330 PHE A CG  1 
ATOM   1283 C CD1 . PHE A 1 175 ? 17.632 22.168 17.401 1.00 62.14  ?  330 PHE A CD1 1 
ATOM   1284 C CD2 . PHE A 1 175 ? 18.343 21.031 19.375 1.00 59.92  ?  330 PHE A CD2 1 
ATOM   1285 C CE1 . PHE A 1 175 ? 16.684 22.874 18.151 1.00 63.29  ?  330 PHE A CE1 1 
ATOM   1286 C CE2 . PHE A 1 175 ? 17.392 21.732 20.121 1.00 63.19  ?  330 PHE A CE2 1 
ATOM   1287 C CZ  . PHE A 1 175 ? 16.570 22.651 19.508 1.00 61.78  ?  330 PHE A CZ  1 
ATOM   1288 N N   . GLY A 1 176 ? 22.867 20.986 15.764 1.00 55.44  ?  331 GLY A N   1 
ATOM   1289 C CA  . GLY A 1 176 ? 23.932 20.371 14.970 1.00 56.11  ?  331 GLY A CA  1 
ATOM   1290 C C   . GLY A 1 176 ? 24.888 19.499 15.768 1.00 61.61  ?  331 GLY A C   1 
ATOM   1291 O O   . GLY A 1 176 ? 25.416 18.521 15.237 1.00 61.74  ?  331 GLY A O   1 
ATOM   1292 N N   . LEU A 1 177 ? 25.053 19.821 17.072 1.00 59.12  ?  332 LEU A N   1 
ATOM   1293 C CA  . LEU A 1 177 ? 25.891 19.099 18.038 1.00 59.03  ?  332 LEU A CA  1 
ATOM   1294 C C   . LEU A 1 177 ? 25.063 18.176 18.944 1.00 65.20  ?  332 LEU A C   1 
ATOM   1295 O O   . LEU A 1 177 ? 25.649 17.442 19.738 1.00 64.43  ?  332 LEU A O   1 
ATOM   1296 C CB  . LEU A 1 177 ? 26.730 20.064 18.913 1.00 58.19  ?  332 LEU A CB  1 
ATOM   1297 C CG  . LEU A 1 177 ? 27.652 21.091 18.233 1.00 62.17  ?  332 LEU A CG  1 
ATOM   1298 C CD1 . LEU A 1 177 ? 28.412 21.916 19.284 1.00 62.29  ?  332 LEU A CD1 1 
ATOM   1299 C CD2 . LEU A 1 177 ? 28.640 20.440 17.257 1.00 62.39  ?  332 LEU A CD2 1 
ATOM   1300 N N   . ALA A 1 178 ? 23.712 18.210 18.827 1.00 63.60  ?  333 ALA A N   1 
ATOM   1301 C CA  . ALA A 1 178 ? 22.798 17.422 19.665 1.00 64.18  ?  333 ALA A CA  1 
ATOM   1302 C C   . ALA A 1 178 ? 23.032 15.911 19.623 1.00 71.52  ?  333 ALA A C   1 
ATOM   1303 O O   . ALA A 1 178 ? 23.394 15.367 18.577 1.00 71.84  ?  333 ALA A O   1 
ATOM   1304 C CB  . ALA A 1 178 ? 21.358 17.751 19.343 1.00 64.57  ?  333 ALA A CB  1 
ATOM   1305 N N   . ARG A 1 179 ? 22.889 15.243 20.781 1.00 69.36  ?  334 ARG A N   1 
ATOM   1306 C CA  . ARG A 1 179 ? 23.099 13.797 20.875 1.00 69.47  ?  334 ARG A CA  1 
ATOM   1307 C C   . ARG A 1 179 ? 22.030 13.112 21.688 1.00 73.44  ?  334 ARG A C   1 
ATOM   1308 O O   . ARG A 1 179 ? 21.614 13.630 22.726 1.00 71.63  ?  334 ARG A O   1 
ATOM   1309 C CB  . ARG A 1 179 ? 24.482 13.465 21.483 1.00 69.03  ?  334 ARG A CB  1 
ATOM   1310 C CG  . ARG A 1 179 ? 25.658 13.698 20.544 1.00 77.71  ?  334 ARG A CG  1 
ATOM   1311 C CD  . ARG A 1 179 ? 26.007 12.475 19.726 1.00 78.65  ?  334 ARG A CD  1 
ATOM   1312 N NE  . ARG A 1 179 ? 27.012 12.771 18.702 1.00 84.52  ?  334 ARG A NE  1 
ATOM   1313 C CZ  . ARG A 1 179 ? 28.330 12.753 18.899 1.00 97.08  ?  334 ARG A CZ  1 
ATOM   1314 N NH1 . ARG A 1 179 ? 28.827 12.469 20.099 1.00 82.15  ?  334 ARG A NH1 1 
ATOM   1315 N NH2 . ARG A 1 179 ? 29.160 13.030 17.900 1.00 81.78  1  334 ARG A NH2 1 
ATOM   1316 N N   . ALA A 1 180 ? 21.635 11.911 21.239 1.00 71.74  ?  335 ALA A N   1 
ATOM   1317 C CA  . ALA A 1 180 ? 20.683 11.051 21.939 1.00 71.78  ?  335 ALA A CA  1 
ATOM   1318 C C   . ALA A 1 180 ? 21.408 10.353 23.099 1.00 76.74  ?  335 ALA A C   1 
ATOM   1319 O O   . ALA A 1 180 ? 22.572 9.966  22.948 1.00 76.62  ?  335 ALA A O   1 
ATOM   1320 C CB  . ALA A 1 180 ? 20.092 10.027 20.986 1.00 72.33  ?  335 ALA A CB  1 
ATOM   1321 N N   . SER A 1 181 ? 20.741 10.248 24.268 1.00 73.65  ?  336 SER A N   1 
ATOM   1322 C CA  . SER A 1 181 ? 21.279 9.619  25.484 1.00 88.08  ?  336 SER A CA  1 
ATOM   1323 C C   . SER A 1 181 ? 20.644 8.248  25.727 1.00 128.64 ?  336 SER A C   1 
ATOM   1324 O O   . SER A 1 181 ? 20.254 7.560  24.783 1.00 95.82  ?  336 SER A O   1 
ATOM   1325 C CB  . SER A 1 181 ? 21.053 10.516 26.696 1.00 90.25  ?  336 SER A CB  1 
ATOM   1326 N N   . GLN A 1 186 ? 24.649 9.443  33.529 1.00 100.77 ?  341 GLN A N   1 
ATOM   1327 C CA  . GLN A 1 186 ? 25.169 10.802 33.397 1.00 99.95  ?  341 GLN A CA  1 
ATOM   1328 C C   . GLN A 1 186 ? 26.677 10.797 33.102 1.00 103.11 ?  341 GLN A C   1 
ATOM   1329 O O   . GLN A 1 186 ? 27.397 11.644 33.634 1.00 102.77 ?  341 GLN A O   1 
ATOM   1330 C CB  . GLN A 1 186 ? 24.884 11.608 34.665 1.00 20.00  ?  341 GLN A CB  1 
ATOM   1331 N N   . THR A 1 187 ? 27.156 9.842  32.246 1.00 99.06  ?  342 THR A N   1 
ATOM   1332 C CA  . THR A 1 187 ? 28.578 9.693  31.866 1.00 98.22  ?  342 THR A CA  1 
ATOM   1333 C C   . THR A 1 187 ? 28.870 8.877  30.574 1.00 99.30  ?  342 THR A C   1 
ATOM   1334 O O   . THR A 1 187 ? 29.097 7.662  30.631 1.00 99.28  ?  342 THR A O   1 
ATOM   1335 C CB  . THR A 1 187 ? 29.518 9.372  33.089 1.00 108.06 ?  342 THR A CB  1 
ATOM   1336 O OG1 . THR A 1 187 ? 30.852 9.105  32.636 1.00 109.21 ?  342 THR A OG1 1 
ATOM   1337 C CG2 . THR A 1 187 ? 29.005 8.225  33.978 1.00 106.04 ?  342 THR A CG2 1 
ATOM   1338 N N   . VAL A 1 188 ? 28.907 9.575  29.423 1.00 92.61  ?  343 VAL A N   1 
ATOM   1339 C CA  . VAL A 1 188 ? 29.276 9.031  28.102 1.00 90.96  ?  343 VAL A CA  1 
ATOM   1340 C C   . VAL A 1 188 ? 30.607 9.739  27.713 1.00 92.67  ?  343 VAL A C   1 
ATOM   1341 O O   . VAL A 1 188 ? 30.969 10.718 28.368 1.00 92.69  ?  343 VAL A O   1 
ATOM   1342 C CB  . VAL A 1 188 ? 28.166 9.232  27.030 1.00 94.35  ?  343 VAL A CB  1 
ATOM   1343 C CG1 . VAL A 1 188 ? 28.437 8.391  25.785 1.00 93.76  ?  343 VAL A CG1 1 
ATOM   1344 C CG2 . VAL A 1 188 ? 26.782 8.921  27.593 1.00 94.21  ?  343 VAL A CG2 1 
ATOM   1345 N N   . MET A 1 189 ? 31.347 9.253  26.698 1.00 86.97  ?  344 MET A N   1 
ATOM   1346 C CA  . MET A 1 189 ? 32.617 9.891  26.328 1.00 85.48  ?  344 MET A CA  1 
ATOM   1347 C C   . MET A 1 189 ? 32.808 10.114 24.842 1.00 85.17  ?  344 MET A C   1 
ATOM   1348 O O   . MET A 1 189 ? 32.259 9.384  24.018 1.00 83.49  ?  344 MET A O   1 
ATOM   1349 C CB  . MET A 1 189 ? 33.823 9.152  26.927 1.00 88.09  ?  344 MET A CB  1 
ATOM   1350 C CG  . MET A 1 189 ? 34.723 10.053 27.730 1.00 92.30  ?  344 MET A CG  1 
ATOM   1351 S SD  . MET A 1 189 ? 34.132 10.259 29.426 1.00 97.29  ?  344 MET A SD  1 
ATOM   1352 C CE  . MET A 1 189 ? 35.052 8.939  30.248 1.00 94.06  ?  344 MET A CE  1 
HETATM 1353 N N   . TPO A 1 190 ? 33.590 11.119 24.465 1.00 80.36  ?  345 TPO A N   1 
HETATM 1354 C CA  . TPO A 1 190 ? 33.743 11.417 23.049 1.00 93.10  ?  345 TPO A CA  1 
HETATM 1355 C CB  . TPO A 1 190 ? 33.112 12.760 22.698 1.00 92.92  ?  345 TPO A CB  1 
HETATM 1356 C CG2 . TPO A 1 190 ? 33.783 13.898 23.451 1.00 92.24  ?  345 TPO A CG2 1 
HETATM 1357 O OG1 . TPO A 1 190 ? 33.213 12.986 21.295 1.00 93.79  ?  345 TPO A OG1 1 
HETATM 1358 P P   . TPO A 1 190 ? 32.692 11.896 20.237 1.00 94.60  ?  345 TPO A P   1 
HETATM 1359 O O1P . TPO A 1 190 ? 31.856 12.692 19.277 1.00 94.44  -1 345 TPO A O1P 1 
HETATM 1360 O O2P . TPO A 1 190 ? 31.922 10.926 21.088 1.00 94.95  -1 345 TPO A O2P 1 
HETATM 1361 O O3P . TPO A 1 190 ? 33.949 11.344 19.632 1.00 95.25  ?  345 TPO A O3P 1 
HETATM 1362 C C   . TPO A 1 190 ? 35.178 11.308 22.606 1.00 113.53 ?  345 TPO A C   1 
HETATM 1363 O O   . TPO A 1 190 ? 35.524 10.267 22.016 1.00 79.19  ?  345 TPO A O   1 
HETATM 1364 N N   . SEP A 1 191 ? 36.005 12.314 22.884 1.00 96.44  ?  346 SEP A N   1 
HETATM 1365 C CA  . SEP A 1 191 ? 37.157 12.677 22.051 1.00 96.11  ?  346 SEP A CA  1 
HETATM 1366 C CB  . SEP A 1 191 ? 37.844 11.484 21.367 1.00 97.95  ?  346 SEP A CB  1 
HETATM 1367 O OG  . SEP A 1 191 ? 37.832 11.529 19.936 1.00 99.83  ?  346 SEP A OG  1 
HETATM 1368 C C   . SEP A 1 191 ? 36.760 13.735 21.064 1.00 96.37  ?  346 SEP A C   1 
HETATM 1369 O O   . SEP A 1 191 ? 35.627 13.709 20.546 1.00 95.55  ?  346 SEP A O   1 
HETATM 1370 P P   . SEP A 1 191 ? 37.527 10.219 19.055 1.00 101.62 ?  346 SEP A P   1 
HETATM 1371 O O1P . SEP A 1 191 ? 37.346 10.738 17.653 1.00 101.30 -1 346 SEP A O1P 1 
HETATM 1372 O O2P . SEP A 1 191 ? 36.278 9.641  19.659 1.00 101.48 ?  346 SEP A O2P 1 
HETATM 1373 O O3P . SEP A 1 191 ? 38.750 9.363  19.238 1.00 102.13 -1 346 SEP A O3P 1 
ATOM   1374 N N   . ARG A 1 192 ? 37.668 14.660 20.781 1.00 90.60  ?  347 ARG A N   1 
ATOM   1375 C CA  . ARG A 1 192 ? 37.313 15.875 20.060 1.00 88.42  ?  347 ARG A CA  1 
ATOM   1376 C C   . ARG A 1 192 ? 36.198 16.619 20.777 1.00 86.45  ?  347 ARG A C   1 
ATOM   1377 O O   . ARG A 1 192 ? 35.034 16.246 20.688 1.00 86.32  ?  347 ARG A O   1 
ATOM   1378 C CB  . ARG A 1 192 ? 36.883 15.545 18.630 1.00 87.94  ?  347 ARG A CB  1 
ATOM   1379 N N   . ILE A 1 193 ? 36.565 17.676 21.490 1.00 77.20  ?  348 ILE A N   1 
ATOM   1380 C CA  . ILE A 1 193 ? 35.602 18.449 22.253 1.00 74.10  ?  348 ILE A CA  1 
ATOM   1381 C C   . ILE A 1 193 ? 34.924 19.494 21.377 1.00 72.49  ?  348 ILE A C   1 
ATOM   1382 O O   . ILE A 1 193 ? 35.592 20.290 20.726 1.00 69.65  ?  348 ILE A O   1 
ATOM   1383 C CB  . ILE A 1 193 ? 36.278 19.143 23.443 1.00 76.52  ?  348 ILE A CB  1 
ATOM   1384 C CG1 . ILE A 1 193 ? 37.167 18.153 24.193 1.00 76.33  ?  348 ILE A CG1 1 
ATOM   1385 C CG2 . ILE A 1 193 ? 35.238 19.742 24.372 1.00 77.04  ?  348 ILE A CG2 1 
ATOM   1386 C CD1 . ILE A 1 193 ? 36.538 16.792 24.381 1.00 75.77  ?  348 ILE A CD1 1 
ATOM   1387 N N   . VAL A 1 194 ? 33.593 19.484 21.368 1.00 66.80  ?  349 VAL A N   1 
ATOM   1388 C CA  . VAL A 1 194 ? 32.824 20.481 20.606 1.00 65.02  ?  349 VAL A CA  1 
ATOM   1389 C C   . VAL A 1 194 ? 31.843 21.289 21.462 1.00 65.67  ?  349 VAL A C   1 
ATOM   1390 O O   . VAL A 1 194 ? 31.179 20.741 22.362 1.00 65.62  ?  349 VAL A O   1 
ATOM   1391 C CB  . VAL A 1 194 ? 32.213 20.016 19.250 1.00 68.20  ?  349 VAL A CB  1 
ATOM   1392 C CG1 . VAL A 1 194 ? 32.273 21.137 18.221 1.00 67.74  ?  349 VAL A CG1 1 
ATOM   1393 C CG2 . VAL A 1 194 ? 32.907 18.780 18.701 1.00 67.91  ?  349 VAL A CG2 1 
ATOM   1394 N N   . GLY A 1 195 ? 31.795 22.592 21.170 1.00 58.85  ?  350 GLY A N   1 
ATOM   1395 C CA  . GLY A 1 195 ? 30.930 23.567 21.819 1.00 57.18  ?  350 GLY A CA  1 
ATOM   1396 C C   . GLY A 1 195 ? 31.543 24.946 21.962 1.00 59.44  ?  350 GLY A C   1 
ATOM   1397 O O   . GLY A 1 195 ? 32.556 25.257 21.323 1.00 58.68  ?  350 GLY A O   1 
ATOM   1398 N N   . THR A 1 196 ? 30.930 25.774 22.842 1.00 54.46  ?  351 THR A N   1 
ATOM   1399 C CA  . THR A 1 196 ? 31.339 27.145 23.174 1.00 52.47  ?  351 THR A CA  1 
ATOM   1400 C C   . THR A 1 196 ? 31.894 27.140 24.601 1.00 55.53  ?  351 THR A C   1 
ATOM   1401 O O   . THR A 1 196 ? 31.131 26.989 25.568 1.00 53.64  ?  351 THR A O   1 
ATOM   1402 C CB  . THR A 1 196 ? 30.156 28.115 23.005 1.00 47.66  ?  351 THR A CB  1 
ATOM   1403 O OG1 . THR A 1 196 ? 29.469 27.820 21.792 1.00 42.12  ?  351 THR A OG1 1 
ATOM   1404 C CG2 . THR A 1 196 ? 30.583 29.568 23.033 1.00 39.65  ?  351 THR A CG2 1 
ATOM   1405 N N   . THR A 1 197 ? 33.233 27.316 24.714 1.00 52.44  ?  352 THR A N   1 
ATOM   1406 C CA  . THR A 1 197 ? 34.011 27.270 25.958 1.00 51.43  ?  352 THR A CA  1 
ATOM   1407 C C   . THR A 1 197 ? 33.520 28.173 27.090 1.00 52.67  ?  352 THR A C   1 
ATOM   1408 O O   . THR A 1 197 ? 33.470 27.707 28.231 1.00 51.75  ?  352 THR A O   1 
ATOM   1409 C CB  . THR A 1 197 ? 35.536 27.262 25.727 1.00 58.95  ?  352 THR A CB  1 
ATOM   1410 O OG1 . THR A 1 197 ? 36.029 28.589 25.723 1.00 67.08  ?  352 THR A OG1 1 
ATOM   1411 C CG2 . THR A 1 197 ? 35.962 26.547 24.457 1.00 53.82  ?  352 THR A CG2 1 
ATOM   1412 N N   . ALA A 1 198 ? 33.098 29.423 26.774 1.00 48.04  ?  353 ALA A N   1 
ATOM   1413 C CA  . ALA A 1 198 ? 32.570 30.378 27.777 1.00 47.72  ?  353 ALA A CA  1 
ATOM   1414 C C   . ALA A 1 198 ? 31.387 29.831 28.586 1.00 52.73  ?  353 ALA A C   1 
ATOM   1415 O O   . ALA A 1 198 ? 31.171 30.219 29.739 1.00 53.80  ?  353 ALA A O   1 
ATOM   1416 C CB  . ALA A 1 198 ? 32.178 31.688 27.120 1.00 47.85  ?  353 ALA A CB  1 
ATOM   1417 N N   . TYR A 1 199 ? 30.671 28.894 28.000 1.00 48.68  ?  354 TYR A N   1 
ATOM   1418 C CA  . TYR A 1 199 ? 29.469 28.277 28.544 1.00 49.04  ?  354 TYR A CA  1 
ATOM   1419 C C   . TYR A 1 199 ? 29.670 26.851 29.014 1.00 55.17  ?  354 TYR A C   1 
ATOM   1420 O O   . TYR A 1 199 ? 28.879 26.371 29.824 1.00 54.14  ?  354 TYR A O   1 
ATOM   1421 C CB  . TYR A 1 199 ? 28.368 28.322 27.466 1.00 48.77  ?  354 TYR A CB  1 
ATOM   1422 C CG  . TYR A 1 199 ? 27.944 29.728 27.092 1.00 48.54  ?  354 TYR A CG  1 
ATOM   1423 C CD1 . TYR A 1 199 ? 28.608 30.436 26.095 1.00 50.03  ?  354 TYR A CD1 1 
ATOM   1424 C CD2 . TYR A 1 199 ? 26.884 30.353 27.742 1.00 48.29  ?  354 TYR A CD2 1 
ATOM   1425 C CE1 . TYR A 1 199 ? 28.227 31.729 25.750 1.00 49.77  ?  354 TYR A CE1 1 
ATOM   1426 C CE2 . TYR A 1 199 ? 26.488 31.643 27.400 1.00 48.50  ?  354 TYR A CE2 1 
ATOM   1427 C CZ  . TYR A 1 199 ? 27.150 32.321 26.389 1.00 54.27  ?  354 TYR A CZ  1 
ATOM   1428 O OH  . TYR A 1 199 ? 26.801 33.603 26.046 1.00 51.24  ?  354 TYR A OH  1 
ATOM   1429 N N   . MET A 1 200 ? 30.712 26.179 28.501 1.00 53.84  ?  355 MET A N   1 
ATOM   1430 C CA  . MET A 1 200 ? 30.993 24.773 28.768 1.00 55.24  ?  355 MET A CA  1 
ATOM   1431 C C   . MET A 1 200 ? 31.279 24.387 30.207 1.00 62.56  ?  355 MET A C   1 
ATOM   1432 O O   . MET A 1 200 ? 32.071 25.030 30.898 1.00 62.57  ?  355 MET A O   1 
ATOM   1433 C CB  . MET A 1 200 ? 32.076 24.227 27.823 1.00 57.55  ?  355 MET A CB  1 
ATOM   1434 C CG  . MET A 1 200 ? 31.609 24.079 26.412 1.00 60.85  ?  355 MET A CG  1 
ATOM   1435 S SD  . MET A 1 200 ? 32.559 22.888 25.467 1.00 65.44  ?  355 MET A SD  1 
ATOM   1436 C CE  . MET A 1 200 ? 33.622 23.910 24.577 1.00 61.39  ?  355 MET A CE  1 
ATOM   1437 N N   . ALA A 1 201 ? 30.645 23.289 30.631 1.00 61.18  ?  356 ALA A N   1 
ATOM   1438 C CA  . ALA A 1 201 ? 30.796 22.667 31.946 1.00 61.52  ?  356 ALA A CA  1 
ATOM   1439 C C   . ALA A 1 201 ? 32.192 22.036 32.074 1.00 66.47  ?  356 ALA A C   1 
ATOM   1440 O O   . ALA A 1 201 ? 32.742 21.607 31.048 1.00 66.67  ?  356 ALA A O   1 
ATOM   1441 C CB  . ALA A 1 201 ? 29.722 21.606 32.137 1.00 61.97  ?  356 ALA A CB  1 
ATOM   1442 N N   . PRO A 1 202 ? 32.793 21.975 33.294 1.00 62.87  ?  357 PRO A N   1 
ATOM   1443 C CA  . PRO A 1 202 ? 34.141 21.376 33.425 1.00 62.66  ?  357 PRO A CA  1 
ATOM   1444 C C   . PRO A 1 202 ? 34.293 20.001 32.762 1.00 66.90  ?  357 PRO A C   1 
ATOM   1445 O O   . PRO A 1 202 ? 35.203 19.820 31.944 1.00 65.40  ?  357 PRO A O   1 
ATOM   1446 C CB  . PRO A 1 202 ? 34.371 21.332 34.945 1.00 64.29  ?  357 PRO A CB  1 
ATOM   1447 C CG  . PRO A 1 202 ? 33.046 21.607 35.571 1.00 68.48  ?  357 PRO A CG  1 
ATOM   1448 C CD  . PRO A 1 202 ? 32.292 22.445 34.603 1.00 64.41  ?  357 PRO A CD  1 
ATOM   1449 N N   . GLU A 1 203 ? 33.339 19.075 33.039 1.00 64.57  ?  358 GLU A N   1 
ATOM   1450 C CA  . GLU A 1 203 ? 33.319 17.733 32.452 1.00 65.17  ?  358 GLU A CA  1 
ATOM   1451 C C   . GLU A 1 203 ? 33.231 17.721 30.918 1.00 71.38  ?  358 GLU A C   1 
ATOM   1452 O O   . GLU A 1 203 ? 33.846 16.858 30.285 1.00 71.65  ?  358 GLU A O   1 
ATOM   1453 C CB  . GLU A 1 203 ? 32.232 16.850 33.084 1.00 66.60  ?  358 GLU A CB  1 
ATOM   1454 C CG  . GLU A 1 203 ? 30.798 17.124 32.645 1.00 76.00  ?  358 GLU A CG  1 
ATOM   1455 C CD  . GLU A 1 203 ? 30.045 18.247 33.336 1.00 91.11  ?  358 GLU A CD  1 
ATOM   1456 O OE1 . GLU A 1 203 ? 30.590 18.871 34.275 1.00 75.22  ?  358 GLU A OE1 1 
ATOM   1457 O OE2 . GLU A 1 203 ? 28.888 18.494 32.936 1.00 88.50  -1 358 GLU A OE2 1 
ATOM   1458 N N   . ALA A 1 204 ? 32.472 18.681 30.331 1.00 68.39  ?  359 ALA A N   1 
ATOM   1459 C CA  . ALA A 1 204 ? 32.262 18.843 28.885 1.00 67.85  ?  359 ALA A CA  1 
ATOM   1460 C C   . ALA A 1 204 ? 33.561 19.192 28.168 1.00 69.59  ?  359 ALA A C   1 
ATOM   1461 O O   . ALA A 1 204 ? 33.772 18.754 27.034 1.00 68.06  ?  359 ALA A O   1 
ATOM   1462 C CB  . ALA A 1 204 ? 31.210 19.916 28.618 1.00 68.56  ?  359 ALA A CB  1 
ATOM   1463 N N   . LEU A 1 205 ? 34.431 19.968 28.843 1.00 65.69  ?  360 LEU A N   1 
ATOM   1464 C CA  . LEU A 1 205 ? 35.739 20.367 28.320 1.00 65.47  ?  360 LEU A CA  1 
ATOM   1465 C C   . LEU A 1 205 ? 36.697 19.169 28.360 1.00 71.19  ?  360 LEU A C   1 
ATOM   1466 O O   . LEU A 1 205 ? 37.730 19.182 27.697 1.00 70.77  ?  360 LEU A O   1 
ATOM   1467 C CB  . LEU A 1 205 ? 36.296 21.570 29.112 1.00 64.90  ?  360 LEU A CB  1 
ATOM   1468 C CG  . LEU A 1 205 ? 35.577 22.906 28.903 1.00 68.30  ?  360 LEU A CG  1 
ATOM   1469 C CD1 . LEU A 1 205 ? 35.716 23.793 30.120 1.00 68.23  ?  360 LEU A CD1 1 
ATOM   1470 C CD2 . LEU A 1 205 ? 36.081 23.628 27.655 1.00 69.88  ?  360 LEU A CD2 1 
ATOM   1471 N N   . ARG A 1 206 ? 36.312 18.107 29.093 1.00 69.68  ?  361 ARG A N   1 
ATOM   1472 C CA  . ARG A 1 206 ? 37.097 16.885 29.245 1.00 70.31  ?  361 ARG A CA  1 
ATOM   1473 C C   . ARG A 1 206 ? 36.562 15.654 28.465 1.00 76.46  ?  361 ARG A C   1 
ATOM   1474 O O   . ARG A 1 206 ? 37.159 14.577 28.533 1.00 77.73  ?  361 ARG A O   1 
ATOM   1475 C CB  . ARG A 1 206 ? 37.390 16.564 30.734 1.00 69.05  ?  361 ARG A CB  1 
ATOM   1476 C CG  . ARG A 1 206 ? 37.858 17.745 31.607 1.00 73.91  ?  361 ARG A CG  1 
ATOM   1477 C CD  . ARG A 1 206 ? 39.039 18.551 31.070 1.00 77.86  ?  361 ARG A CD  1 
ATOM   1478 N NE  . ARG A 1 206 ? 39.256 19.765 31.868 1.00 80.40  ?  361 ARG A NE  1 
ATOM   1479 C CZ  . ARG A 1 206 ? 40.272 20.614 31.712 1.00 86.79  ?  361 ARG A CZ  1 
ATOM   1480 N NH1 . ARG A 1 206 ? 41.192 20.401 30.776 1.00 56.70  ?  361 ARG A NH1 1 
ATOM   1481 N NH2 . ARG A 1 206 ? 40.376 21.681 32.489 1.00 76.89  1  361 ARG A NH2 1 
ATOM   1482 N N   . GLY A 1 207 ? 35.483 15.828 27.709 1.00 72.08  ?  362 GLY A N   1 
ATOM   1483 C CA  . GLY A 1 207 ? 34.947 14.763 26.869 1.00 71.29  ?  362 GLY A CA  1 
ATOM   1484 C C   . GLY A 1 207 ? 33.636 14.145 27.286 1.00 74.03  ?  362 GLY A C   1 
ATOM   1485 O O   . GLY A 1 207 ? 32.996 13.482 26.468 1.00 74.11  ?  362 GLY A O   1 
ATOM   1486 N N   . GLU A 1 208 ? 33.233 14.342 28.553 1.00 69.38  ?  363 GLU A N   1 
ATOM   1487 C CA  . GLU A 1 208 ? 31.984 13.797 29.076 1.00 68.94  ?  363 GLU A CA  1 
ATOM   1488 C C   . GLU A 1 208 ? 30.757 14.382 28.391 1.00 72.67  ?  363 GLU A C   1 
ATOM   1489 O O   . GLU A 1 208 ? 30.587 15.605 28.324 1.00 71.89  ?  363 GLU A O   1 
ATOM   1490 C CB  . GLU A 1 208 ? 31.871 14.009 30.583 1.00 70.42  ?  363 GLU A CB  1 
ATOM   1491 C CG  . GLU A 1 208 ? 32.555 12.954 31.431 1.00 79.30  ?  363 GLU A CG  1 
ATOM   1492 C CD  . GLU A 1 208 ? 32.262 13.117 32.908 1.00 95.24  ?  363 GLU A CD  1 
ATOM   1493 O OE1 . GLU A 1 208 ? 33.226 13.099 33.707 1.00 97.60  ?  363 GLU A OE1 1 
ATOM   1494 O OE2 . GLU A 1 208 ? 31.077 13.316 33.262 1.00 82.45  -1 363 GLU A OE2 1 
ATOM   1495 N N   . ILE A 1 209 ? 29.913 13.485 27.865 1.00 68.80  ?  364 ILE A N   1 
ATOM   1496 C CA  . ILE A 1 209 ? 28.646 13.825 27.235 1.00 67.51  ?  364 ILE A CA  1 
ATOM   1497 C C   . ILE A 1 209 ? 27.566 13.461 28.252 1.00 70.09  ?  364 ILE A C   1 
ATOM   1498 O O   . ILE A 1 209 ? 27.242 12.287 28.425 1.00 68.98  ?  364 ILE A O   1 
ATOM   1499 C CB  . ILE A 1 209 ? 28.448 13.158 25.832 1.00 70.11  ?  364 ILE A CB  1 
ATOM   1500 C CG1 . ILE A 1 209 ? 29.564 13.591 24.840 1.00 69.95  ?  364 ILE A CG1 1 
ATOM   1501 C CG2 . ILE A 1 209 ? 27.051 13.476 25.267 1.00 70.90  ?  364 ILE A CG2 1 
ATOM   1502 C CD1 . ILE A 1 209 ? 29.443 13.042 23.412 1.00 73.16  ?  364 ILE A CD1 1 
ATOM   1503 N N   . THR A 1 210 ? 27.073 14.469 28.985 1.00 67.26  ?  365 THR A N   1 
ATOM   1504 C CA  . THR A 1 210 ? 26.016 14.255 29.971 1.00 66.84  ?  365 THR A CA  1 
ATOM   1505 C C   . THR A 1 210 ? 24.955 15.376 29.934 1.00 69.89  ?  365 THR A C   1 
ATOM   1506 O O   . THR A 1 210 ? 25.323 16.548 29.811 1.00 68.61  ?  365 THR A O   1 
ATOM   1507 C CB  . THR A 1 210 ? 26.589 14.018 31.393 1.00 72.93  ?  365 THR A CB  1 
ATOM   1508 O OG1 . THR A 1 210 ? 25.534 14.129 32.359 1.00 75.82  ?  365 THR A OG1 1 
ATOM   1509 C CG2 . THR A 1 210 ? 27.716 14.984 31.766 1.00 67.28  ?  365 THR A CG2 1 
ATOM   1510 N N   . PRO A 1 211 ? 23.647 15.053 30.117 1.00 66.02  ?  366 PRO A N   1 
ATOM   1511 C CA  . PRO A 1 211 ? 22.630 16.116 30.177 1.00 64.59  ?  366 PRO A CA  1 
ATOM   1512 C C   . PRO A 1 211 ? 22.907 17.127 31.288 1.00 65.80  ?  366 PRO A C   1 
ATOM   1513 O O   . PRO A 1 211 ? 22.436 18.258 31.201 1.00 66.53  ?  366 PRO A O   1 
ATOM   1514 C CB  . PRO A 1 211 ? 21.340 15.348 30.468 1.00 66.53  ?  366 PRO A CB  1 
ATOM   1515 C CG  . PRO A 1 211 ? 21.786 14.048 31.078 1.00 71.49  ?  366 PRO A CG  1 
ATOM   1516 C CD  . PRO A 1 211 ? 23.025 13.726 30.308 1.00 67.69  ?  366 PRO A CD  1 
ATOM   1517 N N   . LYS A 1 212 ? 23.685 16.736 32.314 1.00 59.17  ?  367 LYS A N   1 
ATOM   1518 C CA  . LYS A 1 212 ? 24.059 17.625 33.421 1.00 58.14  ?  367 LYS A CA  1 
ATOM   1519 C C   . LYS A 1 212 ? 24.918 18.813 32.942 1.00 60.21  ?  367 LYS A C   1 
ATOM   1520 O O   . LYS A 1 212 ? 24.880 19.874 33.571 1.00 60.43  ?  367 LYS A O   1 
ATOM   1521 C CB  . LYS A 1 212 ? 24.744 16.840 34.560 1.00 60.66  ?  367 LYS A CB  1 
ATOM   1522 N N   . SER A 1 213 ? 25.670 18.648 31.818 1.00 54.02  ?  368 SER A N   1 
ATOM   1523 C CA  . SER A 1 213 ? 26.472 19.721 31.216 1.00 52.63  ?  368 SER A CA  1 
ATOM   1524 C C   . SER A 1 213 ? 25.552 20.856 30.723 1.00 54.46  ?  368 SER A C   1 
ATOM   1525 O O   . SER A 1 213 ? 25.891 22.028 30.909 1.00 53.75  ?  368 SER A O   1 
ATOM   1526 C CB  . SER A 1 213 ? 27.304 19.198 30.046 1.00 55.55  ?  368 SER A CB  1 
ATOM   1527 O OG  . SER A 1 213 ? 28.115 18.086 30.374 1.00 60.93  ?  368 SER A OG  1 
ATOM   1528 N N   . ASP A 1 214 ? 24.382 20.497 30.113 1.00 49.43  ?  369 ASP A N   1 
ATOM   1529 C CA  . ASP A 1 214 ? 23.348 21.423 29.610 1.00 48.55  ?  369 ASP A CA  1 
ATOM   1530 C C   . ASP A 1 214 ? 22.862 22.364 30.721 1.00 53.59  ?  369 ASP A C   1 
ATOM   1531 O O   . ASP A 1 214 ? 22.714 23.560 30.474 1.00 54.05  ?  369 ASP A O   1 
ATOM   1532 C CB  . ASP A 1 214 ? 22.148 20.668 28.989 1.00 49.24  ?  369 ASP A CB  1 
ATOM   1533 C CG  . ASP A 1 214 ? 22.266 20.199 27.537 1.00 57.31  ?  369 ASP A CG  1 
ATOM   1534 O OD1 . ASP A 1 214 ? 23.308 20.491 26.889 1.00 58.17  ?  369 ASP A OD1 1 
ATOM   1535 O OD2 . ASP A 1 214 ? 21.305 19.558 27.038 1.00 60.75  -1 369 ASP A OD2 1 
ATOM   1536 N N   . ILE A 1 215 ? 22.653 21.828 31.943 1.00 49.79  ?  370 ILE A N   1 
ATOM   1537 C CA  . ILE A 1 215 ? 22.231 22.554 33.154 1.00 49.43  ?  370 ILE A CA  1 
ATOM   1538 C C   . ILE A 1 215 ? 23.287 23.606 33.532 1.00 54.63  ?  370 ILE A C   1 
ATOM   1539 O O   . ILE A 1 215 ? 22.933 24.758 33.786 1.00 54.80  ?  370 ILE A O   1 
ATOM   1540 C CB  . ILE A 1 215 ? 21.967 21.547 34.321 1.00 52.23  ?  370 ILE A CB  1 
ATOM   1541 C CG1 . ILE A 1 215 ? 20.859 20.513 33.995 1.00 51.94  ?  370 ILE A CG1 1 
ATOM   1542 C CG2 . ILE A 1 215 ? 21.806 22.214 35.724 1.00 53.44  ?  370 ILE A CG2 1 
ATOM   1543 C CD1 . ILE A 1 215 ? 19.486 21.047 33.774 1.00 56.94  ?  370 ILE A CD1 1 
ATOM   1544 N N   . TYR A 1 216 ? 24.579 23.204 33.569 1.00 51.69  ?  371 TYR A N   1 
ATOM   1545 C CA  . TYR A 1 216 ? 25.674 24.117 33.886 1.00 51.88  ?  371 TYR A CA  1 
ATOM   1546 C C   . TYR A 1 216 ? 25.582 25.332 32.964 1.00 57.04  ?  371 TYR A C   1 
ATOM   1547 O O   . TYR A 1 216 ? 25.512 26.464 33.451 1.00 57.99  ?  371 TYR A O   1 
ATOM   1548 C CB  . TYR A 1 216 ? 27.039 23.415 33.746 1.00 52.53  ?  371 TYR A CB  1 
ATOM   1549 C CG  . TYR A 1 216 ? 28.223 24.247 34.190 1.00 54.00  ?  371 TYR A CG  1 
ATOM   1550 C CD1 . TYR A 1 216 ? 28.863 25.118 33.306 1.00 55.89  ?  371 TYR A CD1 1 
ATOM   1551 C CD2 . TYR A 1 216 ? 28.711 24.160 35.493 1.00 54.97  ?  371 TYR A CD2 1 
ATOM   1552 C CE1 . TYR A 1 216 ? 29.957 25.890 33.709 1.00 57.28  ?  371 TYR A CE1 1 
ATOM   1553 C CE2 . TYR A 1 216 ? 29.794 24.935 35.913 1.00 56.35  ?  371 TYR A CE2 1 
ATOM   1554 C CZ  . TYR A 1 216 ? 30.422 25.789 35.012 1.00 66.35  ?  371 TYR A CZ  1 
ATOM   1555 O OH  . TYR A 1 216 ? 31.492 26.549 35.397 1.00 69.86  ?  371 TYR A OH  1 
ATOM   1556 N N   . SER A 1 217 ? 25.515 25.079 31.644 1.00 52.04  ?  372 SER A N   1 
ATOM   1557 C CA  . SER A 1 217 ? 25.418 26.090 30.603 1.00 51.20  ?  372 SER A CA  1 
ATOM   1558 C C   . SER A 1 217 ? 24.237 27.028 30.818 1.00 54.41  ?  372 SER A C   1 
ATOM   1559 O O   . SER A 1 217 ? 24.400 28.240 30.670 1.00 51.60  ?  372 SER A O   1 
ATOM   1560 C CB  . SER A 1 217 ? 25.350 25.430 29.236 1.00 54.24  ?  372 SER A CB  1 
ATOM   1561 O OG  . SER A 1 217 ? 26.587 24.812 28.940 1.00 61.60  ?  372 SER A OG  1 
ATOM   1562 N N   . PHE A 1 218 ? 23.080 26.475 31.230 1.00 53.80  ?  373 PHE A N   1 
ATOM   1563 C CA  . PHE A 1 218 ? 21.870 27.231 31.546 1.00 55.18  ?  373 PHE A CA  1 
ATOM   1564 C C   . PHE A 1 218 ? 22.082 28.195 32.719 1.00 57.78  ?  373 PHE A C   1 
ATOM   1565 O O   . PHE A 1 218 ? 21.490 29.276 32.722 1.00 59.10  ?  373 PHE A O   1 
ATOM   1566 C CB  . PHE A 1 218 ? 20.680 26.303 31.793 1.00 58.66  ?  373 PHE A CB  1 
ATOM   1567 C CG  . PHE A 1 218 ? 19.353 27.013 31.944 1.00 62.53  ?  373 PHE A CG  1 
ATOM   1568 C CD1 . PHE A 1 218 ? 18.758 27.652 30.859 1.00 67.30  ?  373 PHE A CD1 1 
ATOM   1569 C CD2 . PHE A 1 218 ? 18.692 27.035 33.166 1.00 66.61  ?  373 PHE A CD2 1 
ATOM   1570 C CE1 . PHE A 1 218 ? 17.532 28.317 31.002 1.00 69.16  ?  373 PHE A CE1 1 
ATOM   1571 C CE2 . PHE A 1 218 ? 17.462 27.691 33.305 1.00 70.34  ?  373 PHE A CE2 1 
ATOM   1572 C CZ  . PHE A 1 218 ? 16.890 28.327 32.221 1.00 68.80  ?  373 PHE A CZ  1 
ATOM   1573 N N   . GLY A 1 219 ? 22.974 27.844 33.650 1.00 51.11  ?  374 GLY A N   1 
ATOM   1574 C CA  . GLY A 1 219 ? 23.331 28.710 34.769 1.00 49.81  ?  374 GLY A CA  1 
ATOM   1575 C C   . GLY A 1 219 ? 24.079 29.937 34.291 1.00 52.29  ?  374 GLY A C   1 
ATOM   1576 O O   . GLY A 1 219 ? 23.878 31.050 34.802 1.00 52.97  ?  374 GLY A O   1 
ATOM   1577 N N   . VAL A 1 220 ? 24.934 29.747 33.275 1.00 47.14  ?  375 VAL A N   1 
ATOM   1578 C CA  . VAL A 1 220 ? 25.703 30.836 32.658 1.00 46.51  ?  375 VAL A CA  1 
ATOM   1579 C C   . VAL A 1 220 ? 24.699 31.795 32.013 1.00 47.15  ?  375 VAL A C   1 
ATOM   1580 O O   . VAL A 1 220 ? 24.792 33.005 32.222 1.00 47.33  ?  375 VAL A O   1 
ATOM   1581 C CB  . VAL A 1 220 ? 26.775 30.315 31.654 1.00 51.00  ?  375 VAL A CB  1 
ATOM   1582 C CG1 . VAL A 1 220 ? 27.602 31.456 31.085 1.00 50.83  ?  375 VAL A CG1 1 
ATOM   1583 C CG2 . VAL A 1 220 ? 27.695 29.282 32.307 1.00 50.78  ?  375 VAL A CG2 1 
ATOM   1584 N N   . VAL A 1 221 ? 23.688 31.229 31.307 1.00 40.77  ?  376 VAL A N   1 
ATOM   1585 C CA  . VAL A 1 221 ? 22.594 31.956 30.675 1.00 38.80  ?  376 VAL A CA  1 
ATOM   1586 C C   . VAL A 1 221 ? 21.852 32.746 31.740 1.00 42.67  ?  376 VAL A C   1 
ATOM   1587 O O   . VAL A 1 221 ? 21.656 33.949 31.560 1.00 42.15  ?  376 VAL A O   1 
ATOM   1588 C CB  . VAL A 1 221 ? 21.652 31.044 29.816 1.00 40.70  ?  376 VAL A CB  1 
ATOM   1589 C CG1 . VAL A 1 221 ? 20.354 31.775 29.419 1.00 39.41  ?  376 VAL A CG1 1 
ATOM   1590 C CG2 . VAL A 1 221 ? 22.378 30.512 28.575 1.00 39.37  ?  376 VAL A CG2 1 
ATOM   1591 N N   . LEU A 1 222 ? 21.504 32.105 32.876 1.00 40.90  ?  377 LEU A N   1 
ATOM   1592 C CA  . LEU A 1 222 ? 20.807 32.805 33.977 1.00 41.43  ?  377 LEU A CA  1 
ATOM   1593 C C   . LEU A 1 222 ? 21.594 33.996 34.518 1.00 45.00  ?  377 LEU A C   1 
ATOM   1594 O O   . LEU A 1 222 ? 20.989 35.013 34.844 1.00 44.84  ?  377 LEU A O   1 
ATOM   1595 C CB  . LEU A 1 222 ? 20.392 31.867 35.111 1.00 41.58  ?  377 LEU A CB  1 
ATOM   1596 C CG  . LEU A 1 222 ? 19.341 30.809 34.778 1.00 45.63  ?  377 LEU A CG  1 
ATOM   1597 C CD1 . LEU A 1 222 ? 19.137 29.874 35.943 1.00 45.21  ?  377 LEU A CD1 1 
ATOM   1598 C CD2 . LEU A 1 222 ? 18.026 31.427 34.350 1.00 47.65  ?  377 LEU A CD2 1 
ATOM   1599 N N   . LEU A 1 223 ? 22.933 33.906 34.561 1.00 43.33  ?  378 LEU A N   1 
ATOM   1600 C CA  . LEU A 1 223 ? 23.746 35.037 35.011 1.00 44.64  ?  378 LEU A CA  1 
ATOM   1601 C C   . LEU A 1 223 ? 23.726 36.156 33.984 1.00 51.64  ?  378 LEU A C   1 
ATOM   1602 O O   . LEU A 1 223 ? 23.705 37.332 34.374 1.00 54.16  ?  378 LEU A O   1 
ATOM   1603 C CB  . LEU A 1 223 ? 25.192 34.645 35.330 1.00 45.42  ?  378 LEU A CB  1 
ATOM   1604 C CG  . LEU A 1 223 ? 25.444 33.596 36.423 1.00 51.07  ?  378 LEU A CG  1 
ATOM   1605 C CD1 . LEU A 1 223 ? 26.952 33.388 36.617 1.00 50.46  ?  378 LEU A CD1 1 
ATOM   1606 C CD2 . LEU A 1 223 ? 24.785 33.996 37.753 1.00 53.58  ?  378 LEU A CD2 1 
ATOM   1607 N N   . GLU A 1 224 ? 23.709 35.806 32.671 1.00 46.22  ?  379 GLU A N   1 
ATOM   1608 C CA  . GLU A 1 224 ? 23.636 36.806 31.601 1.00 45.17  ?  379 GLU A CA  1 
ATOM   1609 C C   . GLU A 1 224 ? 22.296 37.523 31.705 1.00 47.74  ?  379 GLU A C   1 
ATOM   1610 O O   . GLU A 1 224 ? 22.255 38.739 31.551 1.00 47.35  ?  379 GLU A O   1 
ATOM   1611 C CB  . GLU A 1 224 ? 23.780 36.177 30.210 1.00 46.06  ?  379 GLU A CB  1 
ATOM   1612 C CG  . GLU A 1 224 ? 25.088 35.457 29.957 1.00 53.10  ?  379 GLU A CG  1 
ATOM   1613 C CD  . GLU A 1 224 ? 25.128 34.824 28.584 1.00 70.75  ?  379 GLU A CD  1 
ATOM   1614 O OE1 . GLU A 1 224 ? 25.831 35.361 27.698 1.00 68.78  ?  379 GLU A OE1 1 
ATOM   1615 O OE2 . GLU A 1 224 ? 24.390 33.836 28.372 1.00 66.80  -1 379 GLU A OE2 1 
ATOM   1616 N N   . ILE A 1 225 ? 21.206 36.772 32.004 1.00 43.15  ?  380 ILE A N   1 
ATOM   1617 C CA  . ILE A 1 225 ? 19.868 37.337 32.166 1.00 43.14  ?  380 ILE A CA  1 
ATOM   1618 C C   . ILE A 1 225 ? 19.840 38.341 33.340 1.00 51.14  ?  380 ILE A C   1 
ATOM   1619 O O   . ILE A 1 225 ? 19.315 39.457 33.179 1.00 53.16  ?  380 ILE A O   1 
ATOM   1620 C CB  . ILE A 1 225 ? 18.784 36.233 32.267 1.00 45.45  ?  380 ILE A CB  1 
ATOM   1621 C CG1 . ILE A 1 225 ? 18.536 35.543 30.888 1.00 44.92  ?  380 ILE A CG1 1 
ATOM   1622 C CG2 . ILE A 1 225 ? 17.473 36.784 32.859 1.00 44.30  ?  380 ILE A CG2 1 
ATOM   1623 C CD1 . ILE A 1 225 ? 17.471 34.315 30.904 1.00 38.56  ?  380 ILE A CD1 1 
ATOM   1624 N N   . ILE A 1 226 ? 20.447 37.972 34.492 1.00 47.08  ?  381 ILE A N   1 
ATOM   1625 C CA  . ILE A 1 226 ? 20.487 38.832 35.682 1.00 47.14  ?  381 ILE A CA  1 
ATOM   1626 C C   . ILE A 1 226 ? 21.272 40.127 35.443 1.00 50.96  ?  381 ILE A C   1 
ATOM   1627 O O   . ILE A 1 226 ? 20.818 41.206 35.829 1.00 51.70  ?  381 ILE A O   1 
ATOM   1628 C CB  . ILE A 1 226 ? 21.025 38.043 36.928 1.00 50.29  ?  381 ILE A CB  1 
ATOM   1629 C CG1 . ILE A 1 226 ? 20.025 36.948 37.371 1.00 50.24  ?  381 ILE A CG1 1 
ATOM   1630 C CG2 . ILE A 1 226 ? 21.355 38.991 38.101 1.00 51.03  ?  381 ILE A CG2 1 
ATOM   1631 C CD1 . ILE A 1 226 ? 20.601 35.856 38.190 1.00 45.54  ?  381 ILE A CD1 1 
ATOM   1632 N N   . THR A 1 227 ? 22.454 40.001 34.836 1.00 46.83  ?  382 THR A N   1 
ATOM   1633 C CA  . THR A 1 227 ? 23.425 41.075 34.657 1.00 46.68  ?  382 THR A CA  1 
ATOM   1634 C C   . THR A 1 227 ? 23.346 41.841 33.367 1.00 48.50  ?  382 THR A C   1 
ATOM   1635 O O   . THR A 1 227 ? 23.870 42.957 33.304 1.00 48.67  ?  382 THR A O   1 
ATOM   1636 C CB  . THR A 1 227 ? 24.858 40.509 34.822 1.00 60.88  ?  382 THR A CB  1 
ATOM   1637 O OG1 . THR A 1 227 ? 25.128 39.581 33.766 1.00 64.19  ?  382 THR A OG1 1 
ATOM   1638 C CG2 . THR A 1 227 ? 25.069 39.830 36.170 1.00 59.43  ?  382 THR A CG2 1 
ATOM   1639 N N   . GLY A 1 228 ? 22.787 41.223 32.332 1.00 43.23  ?  383 GLY A N   1 
ATOM   1640 C CA  . GLY A 1 228 ? 22.751 41.799 30.994 1.00 42.97  ?  383 GLY A CA  1 
ATOM   1641 C C   . GLY A 1 228 ? 24.131 41.773 30.363 1.00 46.74  ?  383 GLY A C   1 
ATOM   1642 O O   . GLY A 1 228 ? 24.375 42.447 29.359 1.00 47.88  ?  383 GLY A O   1 
ATOM   1643 N N   . LEU A 1 229 ? 25.054 41.014 30.972 1.00 43.51  ?  384 LEU A N   1 
ATOM   1644 C CA  . LEU A 1 229 ? 26.452 40.910 30.548 1.00 43.20  ?  384 LEU A CA  1 
ATOM   1645 C C   . LEU A 1 229 ? 26.718 39.626 29.774 1.00 43.57  ?  384 LEU A C   1 
ATOM   1646 O O   . LEU A 1 229 ? 26.264 38.556 30.206 1.00 40.97  ?  384 LEU A O   1 
ATOM   1647 C CB  . LEU A 1 229 ? 27.401 40.948 31.767 1.00 43.62  ?  384 LEU A CB  1 
ATOM   1648 C CG  . LEU A 1 229 ? 27.501 42.234 32.573 1.00 48.63  ?  384 LEU A CG  1 
ATOM   1649 C CD1 . LEU A 1 229 ? 28.279 42.012 33.849 1.00 48.91  ?  384 LEU A CD1 1 
ATOM   1650 C CD2 . LEU A 1 229 ? 28.136 43.333 31.777 1.00 51.87  ?  384 LEU A CD2 1 
ATOM   1651 N N   . PRO A 1 230 ? 27.497 39.701 28.665 1.00 40.39  ?  385 PRO A N   1 
ATOM   1652 C CA  . PRO A 1 230 ? 27.852 38.464 27.935 1.00 41.53  ?  385 PRO A CA  1 
ATOM   1653 C C   . PRO A 1 230 ? 28.795 37.583 28.779 1.00 49.60  ?  385 PRO A C   1 
ATOM   1654 O O   . PRO A 1 230 ? 29.595 38.118 29.557 1.00 49.09  ?  385 PRO A O   1 
ATOM   1655 C CB  . PRO A 1 230 ? 28.532 38.980 26.661 1.00 42.65  ?  385 PRO A CB  1 
ATOM   1656 C CG  . PRO A 1 230 ? 29.017 40.338 26.996 1.00 45.60  ?  385 PRO A CG  1 
ATOM   1657 C CD  . PRO A 1 230 ? 28.134 40.896 28.060 1.00 41.05  ?  385 PRO A CD  1 
ATOM   1658 N N   . ALA A 1 231 ? 28.671 36.245 28.652 1.00 48.73  ?  386 ALA A N   1 
ATOM   1659 C CA  . ALA A 1 231 ? 29.464 35.258 29.401 1.00 49.95  ?  386 ALA A CA  1 
ATOM   1660 C C   . ALA A 1 231 ? 30.990 35.606 29.440 1.00 55.58  ?  386 ALA A C   1 
ATOM   1661 O O   . ALA A 1 231 ? 31.642 35.521 30.486 1.00 53.85  ?  386 ALA A O   1 
ATOM   1662 C CB  . ALA A 1 231 ? 29.238 33.864 28.820 1.00 50.66  ?  386 ALA A CB  1 
ATOM   1663 N N   . VAL A 1 232 ? 31.513 36.036 28.297 1.00 54.64  ?  387 VAL A N   1 
ATOM   1664 C CA  . VAL A 1 232 ? 32.896 36.451 28.167 1.00 55.85  ?  387 VAL A CA  1 
ATOM   1665 C C   . VAL A 1 232 ? 32.947 37.762 27.366 1.00 60.01  ?  387 VAL A C   1 
ATOM   1666 O O   . VAL A 1 232 ? 32.170 37.948 26.432 1.00 59.32  ?  387 VAL A O   1 
ATOM   1667 C CB  . VAL A 1 232 ? 33.849 35.322 27.648 1.00 61.04  ?  387 VAL A CB  1 
ATOM   1668 C CG1 . VAL A 1 232 ? 33.666 35.047 26.168 1.00 61.41  ?  387 VAL A CG1 1 
ATOM   1669 C CG2 . VAL A 1 232 ? 35.311 35.651 27.924 1.00 61.23  ?  387 VAL A CG2 1 
ATOM   1670 N N   . ASP A 1 233 ? 33.812 38.683 27.790 1.00 58.18  ?  388 ASP A N   1 
ATOM   1671 C CA  . ASP A 1 233 ? 34.036 39.974 27.149 1.00 59.84  ?  388 ASP A CA  1 
ATOM   1672 C C   . ASP A 1 233 ? 35.524 40.341 27.295 1.00 66.49  ?  388 ASP A C   1 
ATOM   1673 O O   . ASP A 1 233 ? 35.998 40.573 28.406 1.00 66.47  ?  388 ASP A O   1 
ATOM   1674 C CB  . ASP A 1 233 ? 33.101 41.055 27.739 1.00 62.24  ?  388 ASP A CB  1 
ATOM   1675 C CG  . ASP A 1 233 ? 33.198 42.428 27.089 1.00 78.30  ?  388 ASP A CG  1 
ATOM   1676 O OD1 . ASP A 1 233 ? 34.075 42.614 26.191 1.00 79.81  ?  388 ASP A OD1 1 
ATOM   1677 O OD2 . ASP A 1 233 ? 32.403 43.324 27.472 1.00 84.76  -1 388 ASP A OD2 1 
ATOM   1678 N N   . GLU A 1 234 ? 36.262 40.348 26.173 1.00 65.59  ?  389 GLU A N   1 
ATOM   1679 C CA  . GLU A 1 234 ? 37.705 40.633 26.143 1.00 66.74  ?  389 GLU A CA  1 
ATOM   1680 C C   . GLU A 1 234 ? 38.056 42.016 26.710 1.00 74.20  ?  389 GLU A C   1 
ATOM   1681 O O   . GLU A 1 234 ? 39.070 42.162 27.387 1.00 73.77  ?  389 GLU A O   1 
ATOM   1682 C CB  . GLU A 1 234 ? 38.282 40.463 24.727 1.00 67.89  ?  389 GLU A CB  1 
ATOM   1683 N N   . HIS A 1 235 ? 37.189 43.012 26.475 1.00 72.85  ?  390 HIS A N   1 
ATOM   1684 C CA  . HIS A 1 235 ? 37.389 44.385 26.928 1.00 73.04  ?  390 HIS A CA  1 
ATOM   1685 C C   . HIS A 1 235 ? 36.653 44.713 28.242 1.00 74.05  ?  390 HIS A C   1 
ATOM   1686 O O   . HIS A 1 235 ? 36.212 45.849 28.443 1.00 73.98  ?  390 HIS A O   1 
ATOM   1687 C CB  . HIS A 1 235 ? 37.030 45.347 25.788 1.00 74.79  ?  390 HIS A CB  1 
ATOM   1688 C CG  . HIS A 1 235 ? 37.771 45.036 24.527 1.00 79.21  ?  390 HIS A CG  1 
ATOM   1689 N ND1 . HIS A 1 235 ? 39.132 45.305 24.397 1.00 81.46  ?  390 HIS A ND1 1 
ATOM   1690 C CD2 . HIS A 1 235 ? 37.333 44.433 23.398 1.00 81.73  ?  390 HIS A CD2 1 
ATOM   1691 C CE1 . HIS A 1 235 ? 39.466 44.881 23.190 1.00 81.23  ?  390 HIS A CE1 1 
ATOM   1692 N NE2 . HIS A 1 235 ? 38.418 44.354 22.547 1.00 81.68  ?  390 HIS A NE2 1 
ATOM   1693 N N   . ARG A 1 236 ? 36.569 43.722 29.157 1.00 67.17  ?  391 ARG A N   1 
ATOM   1694 C CA  . ARG A 1 236 ? 35.883 43.851 30.441 1.00 65.11  ?  391 ARG A CA  1 
ATOM   1695 C C   . ARG A 1 236 ? 36.713 43.293 31.594 1.00 69.16  ?  391 ARG A C   1 
ATOM   1696 O O   . ARG A 1 236 ? 37.515 42.371 31.396 1.00 70.66  ?  391 ARG A O   1 
ATOM   1697 C CB  . ARG A 1 236 ? 34.529 43.129 30.363 1.00 61.15  ?  391 ARG A CB  1 
ATOM   1698 C CG  . ARG A 1 236 ? 33.589 43.343 31.548 1.00 61.30  ?  391 ARG A CG  1 
ATOM   1699 C CD  . ARG A 1 236 ? 32.316 42.542 31.429 1.00 60.02  ?  391 ARG A CD  1 
ATOM   1700 N NE  . ARG A 1 236 ? 32.541 41.096 31.506 1.00 58.78  ?  391 ARG A NE  1 
ATOM   1701 C CZ  . ARG A 1 236 ? 31.709 40.192 31.009 1.00 69.01  ?  391 ARG A CZ  1 
ATOM   1702 N NH1 . ARG A 1 236 ? 31.980 38.901 31.125 1.00 55.30  ?  391 ARG A NH1 1 
ATOM   1703 N NH2 . ARG A 1 236 ? 30.598 40.571 30.392 1.00 59.55  1  391 ARG A NH2 1 
ATOM   1704 N N   . GLU A 1 237 ? 36.495 43.846 32.802 1.00 63.58  ?  392 GLU A N   1 
ATOM   1705 C CA  . GLU A 1 237 ? 37.147 43.432 34.028 1.00 63.43  ?  392 GLU A CA  1 
ATOM   1706 C C   . GLU A 1 237 ? 36.075 43.005 35.059 1.00 65.47  ?  392 GLU A C   1 
ATOM   1707 O O   . GLU A 1 237 ? 35.338 43.854 35.563 1.00 63.99  ?  392 GLU A O   1 
ATOM   1708 C CB  . GLU A 1 237 ? 38.080 44.551 34.544 1.00 65.58  ?  392 GLU A CB  1 
ATOM   1709 C CG  . GLU A 1 237 ? 38.548 44.459 35.994 1.00 80.69  ?  392 GLU A CG  1 
ATOM   1710 C CD  . GLU A 1 237 ? 38.847 45.805 36.630 1.00 108.11 ?  392 GLU A CD  1 
ATOM   1711 O OE1 . GLU A 1 237 ? 39.747 46.524 36.131 1.00 92.81  ?  392 GLU A OE1 1 
ATOM   1712 O OE2 . GLU A 1 237 ? 38.178 46.144 37.633 1.00 110.04 -1 392 GLU A OE2 1 
ATOM   1713 N N   . PRO A 1 238 ? 35.935 41.688 35.350 1.00 62.22  ?  393 PRO A N   1 
ATOM   1714 C CA  . PRO A 1 238 ? 36.680 40.529 34.803 1.00 62.03  ?  393 PRO A CA  1 
ATOM   1715 C C   . PRO A 1 238 ? 36.158 40.115 33.433 1.00 64.08  ?  393 PRO A C   1 
ATOM   1716 O O   . PRO A 1 238 ? 34.983 40.345 33.142 1.00 65.18  ?  393 PRO A O   1 
ATOM   1717 C CB  . PRO A 1 238 ? 36.401 39.404 35.825 1.00 63.83  ?  393 PRO A CB  1 
ATOM   1718 C CG  . PRO A 1 238 ? 35.596 40.028 36.940 1.00 68.27  ?  393 PRO A CG  1 
ATOM   1719 C CD  . PRO A 1 238 ? 34.943 41.239 36.330 1.00 63.73  ?  393 PRO A CD  1 
ATOM   1720 N N   . GLN A 1 239 ? 37.010 39.487 32.616 1.00 57.68  ?  394 GLN A N   1 
ATOM   1721 C CA  . GLN A 1 239 ? 36.643 39.007 31.281 1.00 57.21  ?  394 GLN A CA  1 
ATOM   1722 C C   . GLN A 1 239 ? 35.458 38.028 31.325 1.00 60.99  ?  394 GLN A C   1 
ATOM   1723 O O   . GLN A 1 239 ? 34.546 38.128 30.514 1.00 62.21  ?  394 GLN A O   1 
ATOM   1724 C CB  . GLN A 1 239 ? 37.825 38.284 30.601 1.00 58.65  ?  394 GLN A CB  1 
ATOM   1725 C CG  . GLN A 1 239 ? 39.140 39.057 30.543 1.00 75.82  ?  394 GLN A CG  1 
ATOM   1726 C CD  . GLN A 1 239 ? 39.811 38.965 29.194 1.00 100.01 ?  394 GLN A CD  1 
ATOM   1727 O OE1 . GLN A 1 239 ? 40.145 39.984 28.605 1.00 101.12 ?  394 GLN A OE1 1 
ATOM   1728 N NE2 . GLN A 1 239 ? 40.051 37.752 28.674 1.00 87.00  ?  394 GLN A NE2 1 
ATOM   1729 N N   . LEU A 1 240 ? 35.483 37.106 32.278 1.00 56.40  ?  395 LEU A N   1 
ATOM   1730 C CA  . LEU A 1 240 ? 34.519 36.039 32.447 1.00 56.53  ?  395 LEU A CA  1 
ATOM   1731 C C   . LEU A 1 240 ? 33.496 36.345 33.507 1.00 59.57  ?  395 LEU A C   1 
ATOM   1732 O O   . LEU A 1 240 ? 33.844 36.710 34.628 1.00 58.24  ?  395 LEU A O   1 
ATOM   1733 C CB  . LEU A 1 240 ? 35.256 34.737 32.824 1.00 57.02  ?  395 LEU A CB  1 
ATOM   1734 C CG  . LEU A 1 240 ? 35.692 33.778 31.719 1.00 62.06  ?  395 LEU A CG  1 
ATOM   1735 C CD1 . LEU A 1 240 ? 36.783 34.366 30.866 1.00 62.01  ?  395 LEU A CD1 1 
ATOM   1736 C CD2 . LEU A 1 240 ? 36.252 32.508 32.335 1.00 63.65  ?  395 LEU A CD2 1 
ATOM   1737 N N   . LEU A 1 241 ? 32.226 36.115 33.159 1.00 56.48  ?  396 LEU A N   1 
ATOM   1738 C CA  . LEU A 1 241 ? 31.068 36.304 34.023 1.00 55.95  ?  396 LEU A CA  1 
ATOM   1739 C C   . LEU A 1 241 ? 31.101 35.291 35.200 1.00 59.25  ?  396 LEU A C   1 
ATOM   1740 O O   . LEU A 1 241 ? 30.514 35.546 36.254 1.00 56.52  ?  396 LEU A O   1 
ATOM   1741 C CB  . LEU A 1 241 ? 29.792 36.148 33.162 1.00 55.60  ?  396 LEU A CB  1 
ATOM   1742 C CG  . LEU A 1 241 ? 28.461 36.580 33.749 1.00 59.85  ?  396 LEU A CG  1 
ATOM   1743 C CD1 . LEU A 1 241 ? 28.443 38.072 34.076 1.00 60.10  ?  396 LEU A CD1 1 
ATOM   1744 C CD2 . LEU A 1 241 ? 27.359 36.263 32.800 1.00 62.30  ?  396 LEU A CD2 1 
ATOM   1745 N N   . LEU A 1 242 ? 31.806 34.153 35.018 1.00 57.08  ?  397 LEU A N   1 
ATOM   1746 C CA  . LEU A 1 242 ? 31.937 33.147 36.077 1.00 57.02  ?  397 LEU A CA  1 
ATOM   1747 C C   . LEU A 1 242 ? 32.812 33.652 37.234 1.00 62.46  ?  397 LEU A C   1 
ATOM   1748 O O   . LEU A 1 242 ? 32.542 33.296 38.374 1.00 61.41  ?  397 LEU A O   1 
ATOM   1749 C CB  . LEU A 1 242 ? 32.397 31.784 35.534 1.00 56.19  ?  397 LEU A CB  1 
ATOM   1750 C CG  . LEU A 1 242 ? 31.330 30.961 34.780 1.00 59.04  ?  397 LEU A CG  1 
ATOM   1751 C CD1 . LEU A 1 242 ? 31.963 29.870 33.944 1.00 58.18  ?  397 LEU A CD1 1 
ATOM   1752 C CD2 . LEU A 1 242 ? 30.341 30.349 35.732 1.00 60.65  ?  397 LEU A CD2 1 
ATOM   1753 N N   . ASP A 1 243 ? 33.794 34.548 36.944 1.00 61.72  ?  398 ASP A N   1 
ATOM   1754 C CA  . ASP A 1 243 ? 34.666 35.193 37.946 1.00 62.84  ?  398 ASP A CA  1 
ATOM   1755 C C   . ASP A 1 243 ? 33.846 36.085 38.869 1.00 71.35  ?  398 ASP A C   1 
ATOM   1756 O O   . ASP A 1 243 ? 34.209 36.234 40.030 1.00 72.03  ?  398 ASP A O   1 
ATOM   1757 C CB  . ASP A 1 243 ? 35.746 36.065 37.297 1.00 64.42  ?  398 ASP A CB  1 
ATOM   1758 C CG  . ASP A 1 243 ? 36.641 35.388 36.293 1.00 74.67  ?  398 ASP A CG  1 
ATOM   1759 O OD1 . ASP A 1 243 ? 36.942 34.182 36.481 1.00 77.10  ?  398 ASP A OD1 1 
ATOM   1760 O OD2 . ASP A 1 243 ? 37.102 36.077 35.352 1.00 76.67  -1 398 ASP A OD2 1 
ATOM   1761 N N   . ILE A 1 244 ? 32.755 36.694 38.356 1.00 70.36  ?  399 ILE A N   1 
ATOM   1762 C CA  . ILE A 1 244 ? 31.884 37.536 39.176 1.00 71.30  ?  399 ILE A CA  1 
ATOM   1763 C C   . ILE A 1 244 ? 31.047 36.654 40.112 1.00 79.98  ?  399 ILE A C   1 
ATOM   1764 O O   . ILE A 1 244 ? 30.657 37.120 41.179 1.00 79.96  ?  399 ILE A O   1 
ATOM   1765 C CB  . ILE A 1 244 ? 31.079 38.659 38.421 1.00 73.97  ?  399 ILE A CB  1 
ATOM   1766 C CG1 . ILE A 1 244 ? 29.735 38.189 37.849 1.00 75.04  ?  399 ILE A CG1 1 
ATOM   1767 C CG2 . ILE A 1 244 ? 31.902 39.367 37.358 1.00 73.33  ?  399 ILE A CG2 1 
ATOM   1768 C CD1 . ILE A 1 244 ? 28.534 38.587 38.641 1.00 85.50  ?  399 ILE A CD1 1 
ATOM   1769 N N   . LYS A 1 245 ? 30.794 35.378 39.722 1.00 80.20  ?  400 LYS A N   1 
ATOM   1770 C CA  . LYS A 1 245 ? 30.060 34.420 40.554 1.00 81.81  ?  400 LYS A CA  1 
ATOM   1771 C C   . LYS A 1 245 ? 30.924 34.067 41.767 1.00 89.76  ?  400 LYS A C   1 
ATOM   1772 O O   . LYS A 1 245 ? 30.395 33.948 42.872 1.00 90.61  ?  400 LYS A O   1 
ATOM   1773 C CB  . LYS A 1 245 ? 29.662 33.153 39.762 1.00 84.31  ?  400 LYS A CB  1 
ATOM   1774 N N   . GLU A 1 246 ? 32.261 33.954 41.558 1.00 87.73  ?  401 GLU A N   1 
ATOM   1775 C CA  . GLU A 1 246 ? 33.266 33.683 42.597 1.00 88.09  ?  401 GLU A CA  1 
ATOM   1776 C C   . GLU A 1 246 ? 33.276 34.829 43.626 1.00 93.65  ?  401 GLU A C   1 
ATOM   1777 O O   . GLU A 1 246 ? 33.177 34.571 44.826 1.00 93.32  ?  401 GLU A O   1 
ATOM   1778 C CB  . GLU A 1 246 ? 34.659 33.502 41.970 1.00 89.26  ?  401 GLU A CB  1 
ATOM   1779 N N   . GLU A 1 247 ? 33.316 36.092 43.135 1.00 90.83  ?  402 GLU A N   1 
ATOM   1780 C CA  . GLU A 1 247 ? 33.290 37.333 43.914 1.00 90.72  ?  402 GLU A CA  1 
ATOM   1781 C C   . GLU A 1 247 ? 32.055 37.445 44.811 1.00 96.51  ?  402 GLU A C   1 
ATOM   1782 O O   . GLU A 1 247 ? 32.143 38.040 45.880 1.00 96.24  ?  402 GLU A O   1 
ATOM   1783 C CB  . GLU A 1 247 ? 33.389 38.549 42.985 1.00 91.89  ?  402 GLU A CB  1 
ATOM   1784 C CG  . GLU A 1 247 ? 34.790 38.792 42.454 1.00 100.12 ?  402 GLU A CG  1 
ATOM   1785 C CD  . GLU A 1 247 ? 34.868 39.589 41.167 1.00 119.11 ?  402 GLU A CD  1 
ATOM   1786 O OE1 . GLU A 1 247 ? 34.428 40.761 41.154 1.00 101.17 ?  402 GLU A OE1 1 
ATOM   1787 O OE2 . GLU A 1 247 ? 35.410 39.048 40.176 1.00 119.43 -1 402 GLU A OE2 1 
ATOM   1788 N N   . ILE A 1 248 ? 30.911 36.878 44.387 1.00 95.20  ?  403 ILE A N   1 
ATOM   1789 C CA  . ILE A 1 248 ? 29.672 36.895 45.177 1.00 96.13  ?  403 ILE A CA  1 
ATOM   1790 C C   . ILE A 1 248 ? 29.770 35.853 46.298 1.00 102.24 ?  403 ILE A C   1 
ATOM   1791 O O   . ILE A 1 248 ? 29.498 36.172 47.460 1.00 101.83 ?  403 ILE A O   1 
ATOM   1792 C CB  . ILE A 1 248 ? 28.394 36.740 44.301 1.00 99.35  ?  403 ILE A CB  1 
ATOM   1793 C CG1 . ILE A 1 248 ? 28.245 37.940 43.330 1.00 100.10 ?  403 ILE A CG1 1 
ATOM   1794 C CG2 . ILE A 1 248 ? 27.127 36.579 45.169 1.00 99.86  ?  403 ILE A CG2 1 
ATOM   1795 C CD1 . ILE A 1 248 ? 27.400 37.684 42.091 1.00 107.72 ?  403 ILE A CD1 1 
ATOM   1796 N N   . GLU A 1 249 ? 30.197 34.623 45.939 1.00 100.21 ?  404 GLU A N   1 
ATOM   1797 C CA  . GLU A 1 249 ? 30.372 33.489 46.854 1.00 100.73 ?  404 GLU A CA  1 
ATOM   1798 C C   . GLU A 1 249 ? 31.559 33.698 47.837 1.00 106.75 ?  404 GLU A C   1 
ATOM   1799 O O   . GLU A 1 249 ? 31.654 32.971 48.829 1.00 107.33 ?  404 GLU A O   1 
ATOM   1800 C CB  . GLU A 1 249 ? 30.503 32.148 46.080 1.00 101.93 ?  404 GLU A CB  1 
ATOM   1801 C CG  . GLU A 1 249 ? 29.364 31.801 45.118 1.00 109.10 ?  404 GLU A CG  1 
ATOM   1802 C CD  . GLU A 1 249 ? 27.965 31.631 45.689 1.00 118.68 ?  404 GLU A CD  1 
ATOM   1803 O OE1 . GLU A 1 249 ? 27.678 30.564 46.278 1.00 105.04 ?  404 GLU A OE1 1 
ATOM   1804 O OE2 . GLU A 1 249 ? 27.136 32.545 45.491 1.00 106.04 -1 404 GLU A OE2 1 
ATOM   1805 N N   . ASP A 1 250 ? 32.457 34.682 47.555 1.00 103.24 ?  405 ASP A N   1 
ATOM   1806 C CA  . ASP A 1 250 ? 33.607 35.061 48.390 1.00 102.93 ?  405 ASP A CA  1 
ATOM   1807 C C   . ASP A 1 250 ? 33.483 36.483 48.990 1.00 105.36 ?  405 ASP A C   1 
ATOM   1808 O O   . ASP A 1 250 ? 34.499 37.146 49.238 1.00 104.99 ?  405 ASP A O   1 
ATOM   1809 C CB  . ASP A 1 250 ? 34.929 34.876 47.630 1.00 105.18 ?  405 ASP A CB  1 
ATOM   1810 C CG  . ASP A 1 250 ? 35.308 33.422 47.376 1.00 120.43 ?  405 ASP A CG  1 
ATOM   1811 O OD1 . ASP A 1 250 ? 34.569 32.514 47.846 1.00 120.77 ?  405 ASP A OD1 1 
ATOM   1812 O OD2 . ASP A 1 250 ? 36.353 33.186 46.724 1.00 128.49 -1 405 ASP A OD2 1 
ATOM   1813 N N   . GLU A 1 251 ? 32.219 36.933 49.218 1.00 99.71  ?  406 GLU A N   1 
ATOM   1814 C CA  . GLU A 1 251 ? 31.807 38.209 49.820 1.00 98.11  ?  406 GLU A CA  1 
ATOM   1815 C C   . GLU A 1 251 ? 32.495 39.503 49.338 1.00 98.46  ?  406 GLU A C   1 
ATOM   1816 O O   . GLU A 1 251 ? 32.218 40.567 49.899 1.00 97.88  ?  406 GLU A O   1 
ATOM   1817 C CB  . GLU A 1 251 ? 31.794 38.105 51.358 1.00 99.51  ?  406 GLU A CB  1 
ATOM   1818 N N   . GLU A 1 252 ? 33.353 39.426 48.293 1.00 92.81  ?  407 GLU A N   1 
ATOM   1819 C CA  . GLU A 1 252 ? 34.072 40.577 47.717 1.00 91.99  ?  407 GLU A CA  1 
ATOM   1820 C C   . GLU A 1 252 ? 33.123 41.549 46.986 1.00 96.21  ?  407 GLU A C   1 
ATOM   1821 O O   . GLU A 1 252 ? 33.471 42.717 46.782 1.00 95.41  ?  407 GLU A O   1 
ATOM   1822 C CB  . GLU A 1 252 ? 35.211 40.107 46.793 1.00 93.10  ?  407 GLU A CB  1 
ATOM   1823 N N   . LYS A 1 253 ? 31.916 41.050 46.617 1.00 92.76  ?  408 LYS A N   1 
ATOM   1824 C CA  . LYS A 1 253 ? 30.812 41.745 45.945 1.00 91.95  ?  408 LYS A CA  1 
ATOM   1825 C C   . LYS A 1 253 ? 29.504 40.961 46.194 1.00 95.62  ?  408 LYS A C   1 
ATOM   1826 O O   . LYS A 1 253 ? 29.551 39.825 46.684 1.00 95.30  ?  408 LYS A O   1 
ATOM   1827 C CB  . LYS A 1 253 ? 31.092 41.862 44.433 1.00 93.78  ?  408 LYS A CB  1 
ATOM   1828 C CG  . LYS A 1 253 ? 31.571 43.243 43.996 1.00 101.22 ?  408 LYS A CG  1 
ATOM   1829 C CD  . LYS A 1 253 ? 32.982 43.209 43.430 1.00 105.92 ?  408 LYS A CD  1 
ATOM   1830 N N   . THR A 1 254 ? 28.342 41.572 45.888 1.00 91.59  ?  409 THR A N   1 
ATOM   1831 C CA  . THR A 1 254 ? 27.032 40.917 46.029 1.00 91.11  ?  409 THR A CA  1 
ATOM   1832 C C   . THR A 1 254 ? 26.292 40.844 44.673 1.00 93.19  ?  409 THR A C   1 
ATOM   1833 O O   . THR A 1 254 ? 26.793 41.387 43.683 1.00 92.83  ?  409 THR A O   1 
ATOM   1834 C CB  . THR A 1 254 ? 26.200 41.503 47.193 1.00 100.45 ?  409 THR A CB  1 
ATOM   1835 O OG1 . THR A 1 254 ? 24.990 40.746 47.312 1.00 99.63  ?  409 THR A OG1 1 
ATOM   1836 C CG2 . THR A 1 254 ? 25.870 42.992 47.012 1.00 99.54  ?  409 THR A CG2 1 
ATOM   1837 N N   . ILE A 1 255 ? 25.122 40.165 44.621 1.00 87.42  ?  410 ILE A N   1 
ATOM   1838 C CA  . ILE A 1 255 ? 24.363 40.077 43.378 1.00 86.01  ?  410 ILE A CA  1 
ATOM   1839 C C   . ILE A 1 255 ? 23.804 41.435 42.961 1.00 86.85  ?  410 ILE A C   1 
ATOM   1840 O O   . ILE A 1 255 ? 23.841 41.760 41.776 1.00 86.71  ?  410 ILE A O   1 
ATOM   1841 C CB  . ILE A 1 255 ? 23.366 38.880 43.295 1.00 89.31  ?  410 ILE A CB  1 
ATOM   1842 C CG1 . ILE A 1 255 ? 22.840 38.636 41.852 1.00 89.93  ?  410 ILE A CG1 1 
ATOM   1843 C CG2 . ILE A 1 255 ? 22.240 38.999 44.300 1.00 90.05  ?  410 ILE A CG2 1 
ATOM   1844 C CD1 . ILE A 1 255 ? 23.932 38.394 40.727 1.00 94.33  ?  410 ILE A CD1 1 
ATOM   1845 N N   . GLU A 1 256 ? 23.394 42.260 43.949 1.00 80.97  ?  411 GLU A N   1 
ATOM   1846 C CA  . GLU A 1 256 ? 22.875 43.615 43.753 1.00 79.55  ?  411 GLU A CA  1 
ATOM   1847 C C   . GLU A 1 256 ? 23.895 44.512 43.073 1.00 83.01  ?  411 GLU A C   1 
ATOM   1848 O O   . GLU A 1 256 ? 23.509 45.396 42.316 1.00 83.71  ?  411 GLU A O   1 
ATOM   1849 C CB  . GLU A 1 256 ? 22.403 44.226 45.077 1.00 80.65  ?  411 GLU A CB  1 
ATOM   1850 N N   . ASP A 1 257 ? 25.197 44.248 43.292 1.00 78.64  ?  412 ASP A N   1 
ATOM   1851 C CA  . ASP A 1 257 ? 26.309 44.984 42.677 1.00 77.99  ?  412 ASP A CA  1 
ATOM   1852 C C   . ASP A 1 257 ? 26.406 44.663 41.182 1.00 78.70  ?  412 ASP A C   1 
ATOM   1853 O O   . ASP A 1 257 ? 27.173 45.305 40.463 1.00 79.01  ?  412 ASP A O   1 
ATOM   1854 C CB  . ASP A 1 257 ? 27.654 44.624 43.361 1.00 80.46  ?  412 ASP A CB  1 
ATOM   1855 C CG  . ASP A 1 257 ? 27.801 45.014 44.822 1.00 97.71  ?  412 ASP A CG  1 
ATOM   1856 O OD1 . ASP A 1 257 ? 27.111 45.968 45.262 1.00 100.03 ?  412 ASP A OD1 1 
ATOM   1857 O OD2 . ASP A 1 257 ? 28.626 44.384 45.524 1.00 104.41 -1 412 ASP A OD2 1 
ATOM   1858 N N   . TYR A 1 258 ? 25.647 43.655 40.719 1.00 71.55  ?  413 TYR A N   1 
ATOM   1859 C CA  . TYR A 1 258 ? 25.680 43.227 39.329 1.00 69.52  ?  413 TYR A CA  1 
ATOM   1860 C C   . TYR A 1 258 ? 24.338 43.157 38.594 1.00 69.00  ?  413 TYR A C   1 
ATOM   1861 O O   . TYR A 1 258 ? 24.341 42.961 37.378 1.00 67.74  ?  413 TYR A O   1 
ATOM   1862 C CB  . TYR A 1 258 ? 26.485 41.936 39.195 1.00 70.70  ?  413 TYR A CB  1 
ATOM   1863 C CG  . TYR A 1 258 ? 27.970 42.167 39.334 1.00 73.01  ?  413 TYR A CG  1 
ATOM   1864 C CD1 . TYR A 1 258 ? 28.700 42.772 38.313 1.00 75.16  ?  413 TYR A CD1 1 
ATOM   1865 C CD2 . TYR A 1 258 ? 28.652 41.772 40.485 1.00 73.84  ?  413 TYR A CD2 1 
ATOM   1866 C CE1 . TYR A 1 258 ? 30.073 42.985 38.435 1.00 76.66  ?  413 TYR A CE1 1 
ATOM   1867 C CE2 . TYR A 1 258 ? 30.026 41.972 40.615 1.00 74.58  ?  413 TYR A CE2 1 
ATOM   1868 C CZ  . TYR A 1 258 ? 30.731 42.575 39.586 1.00 84.51  ?  413 TYR A CZ  1 
ATOM   1869 O OH  . TYR A 1 258 ? 32.080 42.767 39.718 1.00 88.64  ?  413 TYR A OH  1 
ATOM   1870 N N   . ILE A 1 259 ? 23.200 43.361 39.308 1.00 63.19  ?  414 ILE A N   1 
ATOM   1871 C CA  . ILE A 1 259 ? 21.862 43.355 38.683 1.00 61.57  ?  414 ILE A CA  1 
ATOM   1872 C C   . ILE A 1 259 ? 21.863 44.380 37.558 1.00 62.40  ?  414 ILE A C   1 
ATOM   1873 O O   . ILE A 1 259 ? 22.316 45.508 37.774 1.00 62.46  ?  414 ILE A O   1 
ATOM   1874 C CB  . ILE A 1 259 ? 20.675 43.601 39.659 1.00 63.83  ?  414 ILE A CB  1 
ATOM   1875 C CG1 . ILE A 1 259 ? 20.713 42.664 40.875 1.00 64.04  ?  414 ILE A CG1 1 
ATOM   1876 C CG2 . ILE A 1 259 ? 19.348 43.458 38.922 1.00 63.83  ?  414 ILE A CG2 1 
ATOM   1877 C CD1 . ILE A 1 259 ? 19.658 43.002 42.024 1.00 70.71  ?  414 ILE A CD1 1 
ATOM   1878 N N   . ASP A 1 260 ? 21.410 43.967 36.358 1.00 54.94  ?  415 ASP A N   1 
ATOM   1879 C CA  . ASP A 1 260 ? 21.369 44.819 35.179 1.00 52.78  ?  415 ASP A CA  1 
ATOM   1880 C C   . ASP A 1 260 ? 20.709 46.162 35.486 1.00 55.44  ?  415 ASP A C   1 
ATOM   1881 O O   . ASP A 1 260 ? 19.547 46.221 35.878 1.00 54.39  ?  415 ASP A O   1 
ATOM   1882 C CB  . ASP A 1 260 ? 20.681 44.093 34.010 1.00 53.46  ?  415 ASP A CB  1 
ATOM   1883 C CG  . ASP A 1 260 ? 20.784 44.754 32.643 1.00 56.83  ?  415 ASP A CG  1 
ATOM   1884 O OD1 . ASP A 1 260 ? 21.395 45.847 32.543 1.00 55.53  ?  415 ASP A OD1 1 
ATOM   1885 O OD2 . ASP A 1 260 ? 20.250 44.188 31.681 1.00 64.03  -1 415 ASP A OD2 1 
ATOM   1886 N N   . LYS A 1 261 ? 21.488 47.236 35.328 1.00 52.24  ?  416 LYS A N   1 
ATOM   1887 C CA  . LYS A 1 261 ? 21.050 48.607 35.565 1.00 51.95  ?  416 LYS A CA  1 
ATOM   1888 C C   . LYS A 1 261 ? 20.010 49.070 34.530 1.00 56.33  ?  416 LYS A C   1 
ATOM   1889 O O   . LYS A 1 261 ? 19.277 50.022 34.801 1.00 57.05  ?  416 LYS A O   1 
ATOM   1890 C CB  . LYS A 1 261 ? 22.254 49.557 35.684 1.00 53.90  ?  416 LYS A CB  1 
ATOM   1891 N N   . LYS A 1 262 ? 19.895 48.349 33.387 1.00 52.65  ?  417 LYS A N   1 
ATOM   1892 C CA  . LYS A 1 262 ? 18.927 48.635 32.314 1.00 52.19  ?  417 LYS A CA  1 
ATOM   1893 C C   . LYS A 1 262 ? 17.503 48.077 32.598 1.00 56.65  ?  417 LYS A C   1 
ATOM   1894 O O   . LYS A 1 262 ? 16.726 47.882 31.672 1.00 55.89  ?  417 LYS A O   1 
ATOM   1895 C CB  . LYS A 1 262 ? 19.459 48.163 30.944 1.00 53.66  ?  417 LYS A CB  1 
ATOM   1896 C CG  . LYS A 1 262 ? 20.720 48.878 30.462 1.00 56.62  ?  417 LYS A CG  1 
ATOM   1897 C CD  . LYS A 1 262 ? 21.257 48.353 29.110 1.00 51.93  ?  417 LYS A CD  1 
ATOM   1898 C CE  . LYS A 1 262 ? 21.864 46.973 29.171 1.00 62.07  ?  417 LYS A CE  1 
ATOM   1899 N NZ  . LYS A 1 262 ? 23.136 46.927 29.947 1.00 73.71  1  417 LYS A NZ  1 
ATOM   1900 N N   . MET A 1 263 ? 17.155 47.836 33.866 1.00 55.81  ?  418 MET A N   1 
ATOM   1901 C CA  . MET A 1 263 ? 15.814 47.337 34.245 1.00 56.56  ?  418 MET A CA  1 
ATOM   1902 C C   . MET A 1 263 ? 15.207 48.272 35.271 1.00 68.83  ?  418 MET A C   1 
ATOM   1903 O O   . MET A 1 263 ? 15.949 48.884 36.026 1.00 69.58  ?  418 MET A O   1 
ATOM   1904 C CB  . MET A 1 263 ? 15.902 45.940 34.898 1.00 57.31  ?  418 MET A CB  1 
ATOM   1905 C CG  . MET A 1 263 ? 16.347 44.848 33.987 1.00 59.25  ?  418 MET A CG  1 
ATOM   1906 S SD  . MET A 1 263 ? 16.134 43.209 34.703 1.00 62.34  ?  418 MET A SD  1 
ATOM   1907 C CE  . MET A 1 263 ? 17.511 43.119 35.755 1.00 59.30  ?  418 MET A CE  1 
ATOM   1908 N N   . ASN A 1 264 ? 13.885 48.337 35.383 1.00 71.66  ?  419 ASN A N   1 
ATOM   1909 C CA  . ASN A 1 264 ? 13.295 49.125 36.474 1.00 74.06  ?  419 ASN A CA  1 
ATOM   1910 C C   . ASN A 1 264 ? 12.355 48.268 37.310 1.00 83.45  ?  419 ASN A C   1 
ATOM   1911 O O   . ASN A 1 264 ? 12.228 48.485 38.517 1.00 84.00  ?  419 ASN A O   1 
ATOM   1912 C CB  . ASN A 1 264 ? 12.657 50.443 36.012 1.00 76.36  ?  419 ASN A CB  1 
ATOM   1913 C CG  . ASN A 1 264 ? 11.457 50.357 35.092 1.00 108.53 ?  419 ASN A CG  1 
ATOM   1914 O OD1 . ASN A 1 264 ? 10.677 49.392 35.089 1.00 108.88 ?  419 ASN A OD1 1 
ATOM   1915 N ND2 . ASN A 1 264 ? 11.245 51.422 34.328 1.00 98.08  ?  419 ASN A ND2 1 
ATOM   1916 N N   . ASP A 1 265 ? 11.762 47.237 36.667 1.00 82.89  ?  420 ASP A N   1 
ATOM   1917 C CA  . ASP A 1 265 ? 10.800 46.324 37.287 1.00 83.43  ?  420 ASP A CA  1 
ATOM   1918 C C   . ASP A 1 265 ? 11.463 45.195 38.066 1.00 89.18  ?  420 ASP A C   1 
ATOM   1919 O O   . ASP A 1 265 ? 10.756 44.312 38.564 1.00 89.50  ?  420 ASP A O   1 
ATOM   1920 C CB  . ASP A 1 265 ? 9.828  45.757 36.224 1.00 85.47  ?  420 ASP A CB  1 
ATOM   1921 C CG  . ASP A 1 265 ? 10.477 44.927 35.127 1.00 94.47  ?  420 ASP A CG  1 
ATOM   1922 O OD1 . ASP A 1 265 ? 11.534 45.363 34.592 1.00 92.66  ?  420 ASP A OD1 1 
ATOM   1923 O OD2 . ASP A 1 265 ? 9.909  43.864 34.772 1.00 102.36 -1 420 ASP A OD2 1 
ATOM   1924 N N   . ALA A 1 266 ? 12.806 45.222 38.193 1.00 86.60  ?  421 ALA A N   1 
ATOM   1925 C CA  . ALA A 1 266 ? 13.576 44.184 38.877 1.00 87.08  ?  421 ALA A CA  1 
ATOM   1926 C C   . ALA A 1 266 ? 13.564 44.328 40.390 1.00 93.71  ?  421 ALA A C   1 
ATOM   1927 O O   . ALA A 1 266 ? 14.027 45.339 40.920 1.00 94.93  ?  421 ALA A O   1 
ATOM   1928 C CB  . ALA A 1 266 ? 15.002 44.163 38.357 1.00 87.65  ?  421 ALA A CB  1 
ATOM   1929 N N   . ASP A 1 267 ? 13.039 43.318 41.087 1.00 90.78  ?  422 ASP A N   1 
ATOM   1930 C CA  . ASP A 1 267 ? 12.967 43.300 42.546 1.00 91.01  ?  422 ASP A CA  1 
ATOM   1931 C C   . ASP A 1 267 ? 13.988 42.307 43.053 1.00 94.59  ?  422 ASP A C   1 
ATOM   1932 O O   . ASP A 1 267 ? 13.995 41.150 42.613 1.00 94.59  ?  422 ASP A O   1 
ATOM   1933 C CB  . ASP A 1 267 ? 11.543 42.969 43.046 1.00 93.20  ?  422 ASP A CB  1 
ATOM   1934 C CG  . ASP A 1 267 ? 10.927 41.698 42.482 1.00 104.61 ?  422 ASP A CG  1 
ATOM   1935 O OD1 . ASP A 1 267 ? 10.705 40.748 43.266 1.00 105.17 ?  422 ASP A OD1 1 
ATOM   1936 O OD2 . ASP A 1 267 ? 10.645 41.664 41.261 1.00 111.72 -1 422 ASP A OD2 1 
ATOM   1937 N N   . SER A 1 268 ? 14.868 42.760 43.963 1.00 90.02  ?  423 SER A N   1 
ATOM   1938 C CA  . SER A 1 268 ? 15.943 41.948 44.536 1.00 89.28  ?  423 SER A CA  1 
ATOM   1939 C C   . SER A 1 268 ? 15.501 40.582 45.038 1.00 91.62  ?  423 SER A C   1 
ATOM   1940 O O   . SER A 1 268 ? 16.293 39.639 44.979 1.00 92.03  ?  423 SER A O   1 
ATOM   1941 C CB  . SER A 1 268 ? 16.710 42.722 45.598 1.00 93.66  ?  423 SER A CB  1 
ATOM   1942 O OG  . SER A 1 268 ? 17.289 43.863 44.991 1.00 104.29 ?  423 SER A OG  1 
ATOM   1943 N N   . THR A 1 269 ? 14.215 40.463 45.454 1.00 85.92  ?  424 THR A N   1 
ATOM   1944 C CA  . THR A 1 269 ? 13.581 39.223 45.914 1.00 84.81  ?  424 THR A CA  1 
ATOM   1945 C C   . THR A 1 269 ? 13.722 38.138 44.841 1.00 85.46  ?  424 THR A C   1 
ATOM   1946 O O   . THR A 1 269 ? 14.508 37.206 45.041 1.00 83.79  ?  424 THR A O   1 
ATOM   1947 C CB  . THR A 1 269 ? 12.112 39.491 46.313 1.00 92.30  ?  424 THR A CB  1 
ATOM   1948 O OG1 . THR A 1 269 ? 12.083 40.403 47.414 1.00 93.85  ?  424 THR A OG1 1 
ATOM   1949 C CG2 . THR A 1 269 ? 11.342 38.213 46.653 1.00 88.84  ?  424 THR A CG2 1 
ATOM   1950 N N   . SER A 1 270 ? 13.005 38.296 43.687 1.00 80.36  ?  425 SER A N   1 
ATOM   1951 C CA  . SER A 1 270 ? 13.024 37.349 42.567 1.00 78.82  ?  425 SER A CA  1 
ATOM   1952 C C   . SER A 1 270 ? 14.373 37.287 41.855 1.00 80.06  ?  425 SER A C   1 
ATOM   1953 O O   . SER A 1 270 ? 14.702 36.240 41.297 1.00 78.89  ?  425 SER A O   1 
ATOM   1954 C CB  . SER A 1 270 ? 11.882 37.608 41.590 1.00 80.95  ?  425 SER A CB  1 
ATOM   1955 O OG  . SER A 1 270 ? 11.947 38.916 41.056 1.00 87.56  ?  425 SER A OG  1 
ATOM   1956 N N   . VAL A 1 271 ? 15.166 38.380 41.906 1.00 75.13  ?  426 VAL A N   1 
ATOM   1957 C CA  . VAL A 1 271 ? 16.506 38.398 41.322 1.00 74.75  ?  426 VAL A CA  1 
ATOM   1958 C C   . VAL A 1 271 ? 17.410 37.444 42.108 1.00 78.73  ?  426 VAL A C   1 
ATOM   1959 O O   . VAL A 1 271 ? 18.095 36.635 41.488 1.00 79.61  ?  426 VAL A O   1 
ATOM   1960 C CB  . VAL A 1 271 ? 17.111 39.815 41.141 1.00 78.69  ?  426 VAL A CB  1 
ATOM   1961 C CG1 . VAL A 1 271 ? 18.531 39.732 40.597 1.00 78.33  ?  426 VAL A CG1 1 
ATOM   1962 C CG2 . VAL A 1 271 ? 16.253 40.673 40.213 1.00 78.68  ?  426 VAL A CG2 1 
ATOM   1963 N N   . GLU A 1 272 ? 17.363 37.490 43.465 1.00 74.47  ?  427 GLU A N   1 
ATOM   1964 C CA  . GLU A 1 272 ? 18.149 36.591 44.334 1.00 72.97  ?  427 GLU A CA  1 
ATOM   1965 C C   . GLU A 1 272 ? 17.718 35.128 44.151 1.00 73.47  ?  427 GLU A C   1 
ATOM   1966 O O   . GLU A 1 272 ? 18.556 34.228 44.245 1.00 72.83  ?  427 GLU A O   1 
ATOM   1967 C CB  . GLU A 1 272 ? 18.064 37.012 45.808 1.00 74.24  ?  427 GLU A CB  1 
ATOM   1968 N N   . ALA A 1 273 ? 16.418 34.905 43.850 1.00 68.01  ?  428 ALA A N   1 
ATOM   1969 C CA  . ALA A 1 273 ? 15.839 33.587 43.589 1.00 66.94  ?  428 ALA A CA  1 
ATOM   1970 C C   . ALA A 1 273 ? 16.428 32.989 42.291 1.00 69.46  ?  428 ALA A C   1 
ATOM   1971 O O   . ALA A 1 273 ? 16.858 31.832 42.305 1.00 69.15  ?  428 ALA A O   1 
ATOM   1972 C CB  . ALA A 1 273 ? 14.327 33.693 43.497 1.00 67.48  ?  428 ALA A CB  1 
ATOM   1973 N N   . MET A 1 274 ? 16.495 33.796 41.188 1.00 64.22  ?  429 MET A N   1 
ATOM   1974 C CA  . MET A 1 274 ? 17.086 33.365 39.918 1.00 62.75  ?  429 MET A CA  1 
ATOM   1975 C C   . MET A 1 274 ? 18.578 33.090 40.124 1.00 65.61  ?  429 MET A C   1 
ATOM   1976 O O   . MET A 1 274 ? 19.075 32.096 39.596 1.00 64.23  ?  429 MET A O   1 
ATOM   1977 C CB  . MET A 1 274 ? 16.856 34.386 38.784 1.00 64.51  ?  429 MET A CB  1 
ATOM   1978 C CG  . MET A 1 274 ? 16.953 33.753 37.390 1.00 66.95  ?  429 MET A CG  1 
ATOM   1979 S SD  . MET A 1 274 ? 16.969 34.946 36.019 1.00 69.63  ?  429 MET A SD  1 
ATOM   1980 C CE  . MET A 1 274 ? 15.243 35.015 35.650 1.00 66.28  ?  429 MET A CE  1 
ATOM   1981 N N   . TYR A 1 275 ? 19.272 33.928 40.939 1.00 62.52  ?  430 TYR A N   1 
ATOM   1982 C CA  . TYR A 1 275 ? 20.678 33.710 41.275 1.00 62.91  ?  430 TYR A CA  1 
ATOM   1983 C C   . TYR A 1 275 ? 20.881 32.414 42.070 1.00 67.26  ?  430 TYR A C   1 
ATOM   1984 O O   . TYR A 1 275 ? 21.880 31.730 41.841 1.00 67.49  ?  430 TYR A O   1 
ATOM   1985 C CB  . TYR A 1 275 ? 21.322 34.911 41.983 1.00 65.39  ?  430 TYR A CB  1 
ATOM   1986 C CG  . TYR A 1 275 ? 22.794 34.684 42.240 1.00 70.01  ?  430 TYR A CG  1 
ATOM   1987 C CD1 . TYR A 1 275 ? 23.732 34.866 41.229 1.00 72.71  ?  430 TYR A CD1 1 
ATOM   1988 C CD2 . TYR A 1 275 ? 23.239 34.181 43.462 1.00 71.19  ?  430 TYR A CD2 1 
ATOM   1989 C CE1 . TYR A 1 275 ? 25.079 34.598 41.440 1.00 73.96  ?  430 TYR A CE1 1 
ATOM   1990 C CE2 . TYR A 1 275 ? 24.581 33.883 43.675 1.00 72.17  ?  430 TYR A CE2 1 
ATOM   1991 C CZ  . TYR A 1 275 ? 25.497 34.110 42.668 1.00 79.54  ?  430 TYR A CZ  1 
ATOM   1992 O OH  . TYR A 1 275 ? 26.815 33.844 42.900 1.00 81.52  ?  430 TYR A OH  1 
ATOM   1993 N N   . SER A 1 276 ? 19.944 32.073 42.984 1.00 63.44  ?  431 SER A N   1 
ATOM   1994 C CA  . SER A 1 276 ? 19.999 30.835 43.757 1.00 62.99  ?  431 SER A CA  1 
ATOM   1995 C C   . SER A 1 276 ? 19.964 29.636 42.783 1.00 64.89  ?  431 SER A C   1 
ATOM   1996 O O   . SER A 1 276 ? 20.836 28.776 42.856 1.00 64.06  ?  431 SER A O   1 
ATOM   1997 C CB  . SER A 1 276 ? 18.856 30.783 44.772 1.00 67.38  ?  431 SER A CB  1 
ATOM   1998 O OG  . SER A 1 276 ? 18.681 29.493 45.346 1.00 72.32  ?  431 SER A OG  1 
ATOM   1999 N N   . VAL A 1 277 ? 19.009 29.636 41.827 1.00 61.45  ?  432 VAL A N   1 
ATOM   2000 C CA  . VAL A 1 277 ? 18.870 28.608 40.788 1.00 61.71  ?  432 VAL A CA  1 
ATOM   2001 C C   . VAL A 1 277 ? 20.190 28.514 39.988 1.00 67.47  ?  432 VAL A C   1 
ATOM   2002 O O   . VAL A 1 277 ? 20.758 27.424 39.891 1.00 67.55  ?  432 VAL A O   1 
ATOM   2003 C CB  . VAL A 1 277 ? 17.653 28.891 39.864 1.00 65.58  ?  432 VAL A CB  1 
ATOM   2004 C CG1 . VAL A 1 277 ? 17.558 27.879 38.732 1.00 65.41  ?  432 VAL A CG1 1 
ATOM   2005 C CG2 . VAL A 1 277 ? 16.355 28.932 40.654 1.00 65.26  ?  432 VAL A CG2 1 
ATOM   2006 N N   . ALA A 1 278 ? 20.697 29.666 39.477 1.00 63.81  ?  433 ALA A N   1 
ATOM   2007 C CA  . ALA A 1 278 ? 21.945 29.757 38.718 1.00 63.50  ?  433 ALA A CA  1 
ATOM   2008 C C   . ALA A 1 278 ? 23.103 29.121 39.476 1.00 68.65  ?  433 ALA A C   1 
ATOM   2009 O O   . ALA A 1 278 ? 23.832 28.302 38.910 1.00 67.54  ?  433 ALA A O   1 
ATOM   2010 C CB  . ALA A 1 278 ? 22.263 31.211 38.405 1.00 64.10  ?  433 ALA A CB  1 
ATOM   2011 N N   . SER A 1 279 ? 23.240 29.472 40.776 1.00 67.15  ?  434 SER A N   1 
ATOM   2012 C CA  . SER A 1 279 ? 24.276 28.958 41.673 1.00 66.62  ?  434 SER A CA  1 
ATOM   2013 C C   . SER A 1 279 ? 24.274 27.427 41.746 1.00 68.94  ?  434 SER A C   1 
ATOM   2014 O O   . SER A 1 279 ? 25.347 26.823 41.674 1.00 69.20  ?  434 SER A O   1 
ATOM   2015 C CB  . SER A 1 279 ? 24.128 29.568 43.058 1.00 70.08  ?  434 SER A CB  1 
ATOM   2016 O OG  . SER A 1 279 ? 25.345 30.188 43.433 1.00 82.66  ?  434 SER A OG  1 
ATOM   2017 N N   . GLN A 1 280 ? 23.076 26.811 41.837 1.00 63.76  ?  435 GLN A N   1 
ATOM   2018 C CA  . GLN A 1 280 ? 22.894 25.354 41.878 1.00 63.83  ?  435 GLN A CA  1 
ATOM   2019 C C   . GLN A 1 280 ? 23.256 24.714 40.542 1.00 68.89  ?  435 GLN A C   1 
ATOM   2020 O O   . GLN A 1 280 ? 23.898 23.656 40.526 1.00 68.71  ?  435 GLN A O   1 
ATOM   2021 C CB  . GLN A 1 280 ? 21.457 24.984 42.267 1.00 65.38  ?  435 GLN A CB  1 
ATOM   2022 C CG  . GLN A 1 280 ? 21.205 25.050 43.764 1.00 78.11  ?  435 GLN A CG  1 
ATOM   2023 C CD  . GLN A 1 280 ? 19.785 25.438 44.055 1.00 92.01  ?  435 GLN A CD  1 
ATOM   2024 O OE1 . GLN A 1 280 ? 19.483 26.608 44.302 1.00 86.29  ?  435 GLN A OE1 1 
ATOM   2025 N NE2 . GLN A 1 280 ? 18.876 24.473 44.023 1.00 84.22  ?  435 GLN A NE2 1 
ATOM   2026 N N   . CYS A 1 281 ? 22.862 25.381 39.419 1.00 65.54  ?  436 CYS A N   1 
ATOM   2027 C CA  . CYS A 1 281 ? 23.153 24.969 38.040 1.00 64.66  ?  436 CYS A CA  1 
ATOM   2028 C C   . CYS A 1 281 ? 24.653 24.950 37.864 1.00 66.31  ?  436 CYS A C   1 
ATOM   2029 O O   . CYS A 1 281 ? 25.148 24.120 37.114 1.00 64.63  ?  436 CYS A O   1 
ATOM   2030 C CB  . CYS A 1 281 ? 22.520 25.921 37.020 1.00 65.07  ?  436 CYS A CB  1 
ATOM   2031 S SG  . CYS A 1 281 ? 20.712 25.890 36.942 1.00 68.95  ?  436 CYS A SG  1 
ATOM   2032 N N   . LEU A 1 282 ? 25.368 25.898 38.521 1.00 63.59  ?  437 LEU A N   1 
ATOM   2033 C CA  . LEU A 1 282 ? 26.815 26.087 38.388 1.00 64.21  ?  437 LEU A CA  1 
ATOM   2034 C C   . LEU A 1 282 ? 27.717 25.309 39.340 1.00 71.27  ?  437 LEU A C   1 
ATOM   2035 O O   . LEU A 1 282 ? 28.912 25.610 39.436 1.00 71.24  ?  437 LEU A O   1 
ATOM   2036 C CB  . LEU A 1 282 ? 27.196 27.575 38.310 1.00 63.91  ?  437 LEU A CB  1 
ATOM   2037 C CG  . LEU A 1 282 ? 26.755 28.331 37.069 1.00 67.44  ?  437 LEU A CG  1 
ATOM   2038 C CD1 . LEU A 1 282 ? 26.964 29.800 37.258 1.00 66.76  ?  437 LEU A CD1 1 
ATOM   2039 C CD2 . LEU A 1 282 ? 27.490 27.852 35.839 1.00 70.45  ?  437 LEU A CD2 1 
ATOM   2040 N N   . HIS A 1 283 ? 27.168 24.265 39.988 1.00 70.44  ?  438 HIS A N   1 
ATOM   2041 C CA  . HIS A 1 283 ? 27.944 23.383 40.850 1.00 71.48  ?  438 HIS A CA  1 
ATOM   2042 C C   . HIS A 1 283 ? 28.962 22.665 40.002 1.00 75.59  ?  438 HIS A C   1 
ATOM   2043 O O   . HIS A 1 283 ? 28.632 22.096 38.955 1.00 75.30  ?  438 HIS A O   1 
ATOM   2044 C CB  . HIS A 1 283 ? 27.056 22.369 41.594 1.00 73.04  ?  438 HIS A CB  1 
ATOM   2045 C CG  . HIS A 1 283 ? 26.522 22.879 42.895 1.00 76.96  ?  438 HIS A CG  1 
ATOM   2046 N ND1 . HIS A 1 283 ? 27.355 23.464 43.844 1.00 78.95  ?  438 HIS A ND1 1 
ATOM   2047 C CD2 . HIS A 1 283 ? 25.259 22.846 43.379 1.00 79.19  ?  438 HIS A CD2 1 
ATOM   2048 C CE1 . HIS A 1 283 ? 26.566 23.798 44.852 1.00 78.75  ?  438 HIS A CE1 1 
ATOM   2049 N NE2 . HIS A 1 283 ? 25.295 23.443 44.621 1.00 79.19  ?  438 HIS A NE2 1 
ATOM   2050 N N   . GLU A 1 284 ? 30.209 22.811 40.426 1.00 72.25  ?  439 GLU A N   1 
ATOM   2051 C CA  . GLU A 1 284 ? 31.454 22.275 39.885 1.00 71.85  ?  439 GLU A CA  1 
ATOM   2052 C C   . GLU A 1 284 ? 31.338 20.750 39.618 1.00 75.45  ?  439 GLU A C   1 
ATOM   2053 O O   . GLU A 1 284 ? 31.726 20.278 38.549 1.00 74.10  ?  439 GLU A O   1 
ATOM   2054 C CB  . GLU A 1 284 ? 32.605 22.603 40.874 1.00 73.27  ?  439 GLU A CB  1 
ATOM   2055 C CG  . GLU A 1 284 ? 32.276 23.618 41.990 1.00 84.85  ?  439 GLU A CG  1 
ATOM   2056 C CD  . GLU A 1 284 ? 31.417 23.227 43.199 1.00 96.85  ?  439 GLU A CD  1 
ATOM   2057 O OE1 . GLU A 1 284 ? 30.848 24.146 43.840 1.00 68.83  ?  439 GLU A OE1 1 
ATOM   2058 O OE2 . GLU A 1 284 ? 31.310 22.015 43.510 1.00 83.64  -1 439 GLU A OE2 1 
ATOM   2059 N N   . LYS A 1 285 ? 30.739 20.010 40.575 1.00 73.15  ?  440 LYS A N   1 
ATOM   2060 C CA  . LYS A 1 285 ? 30.510 18.566 40.540 1.00 73.49  ?  440 LYS A CA  1 
ATOM   2061 C C   . LYS A 1 285 ? 29.102 18.270 39.982 1.00 77.35  ?  440 LYS A C   1 
ATOM   2062 O O   . LYS A 1 285 ? 28.090 18.542 40.636 1.00 77.55  ?  440 LYS A O   1 
ATOM   2063 C CB  . LYS A 1 285 ? 30.727 17.952 41.942 1.00 76.34  ?  440 LYS A CB  1 
ATOM   2064 N N   . LYS A 1 286 ? 29.059 17.750 38.745 1.00 72.87  ?  441 LYS A N   1 
ATOM   2065 C CA  . LYS A 1 286 ? 27.852 17.429 37.974 1.00 72.64  ?  441 LYS A CA  1 
ATOM   2066 C C   . LYS A 1 286 ? 26.684 16.769 38.710 1.00 78.33  ?  441 LYS A C   1 
ATOM   2067 O O   . LYS A 1 286 ? 25.526 17.052 38.392 1.00 78.75  ?  441 LYS A O   1 
ATOM   2068 C CB  . LYS A 1 286 ? 28.197 16.656 36.687 1.00 74.74  ?  441 LYS A CB  1 
ATOM   2069 C CG  . LYS A 1 286 ? 28.953 15.368 36.916 1.00 86.85  ?  441 LYS A CG  1 
ATOM   2070 C CD  . LYS A 1 286 ? 28.910 14.469 35.717 1.00 95.80  ?  441 LYS A CD  1 
ATOM   2071 C CE  . LYS A 1 286 ? 29.102 13.056 36.168 1.00 103.67 ?  441 LYS A CE  1 
ATOM   2072 N NZ  . LYS A 1 286 ? 29.584 12.214 35.069 1.00 109.29 1  441 LYS A NZ  1 
ATOM   2073 N N   . ASN A 1 287 ? 26.973 15.887 39.672 1.00 74.99  ?  442 ASN A N   1 
ATOM   2074 C CA  . ASN A 1 287 ? 25.914 15.192 40.408 1.00 74.82  ?  442 ASN A CA  1 
ATOM   2075 C C   . ASN A 1 287 ? 25.298 16.062 41.490 1.00 77.75  ?  442 ASN A C   1 
ATOM   2076 O O   . ASN A 1 287 ? 24.181 15.772 41.929 1.00 77.70  ?  442 ASN A O   1 
ATOM   2077 C CB  . ASN A 1 287 ? 26.381 13.824 40.929 1.00 77.20  ?  442 ASN A CB  1 
ATOM   2078 C CG  . ASN A 1 287 ? 27.029 12.964 39.862 1.00 101.22 ?  442 ASN A CG  1 
ATOM   2079 O OD1 . ASN A 1 287 ? 28.227 12.660 39.920 1.00 97.76  ?  442 ASN A OD1 1 
ATOM   2080 N ND2 . ASN A 1 287 ? 26.263 12.599 38.838 1.00 90.60  ?  442 ASN A ND2 1 
ATOM   2081 N N   . LYS A 1 288 ? 25.998 17.156 41.889 1.00 72.77  ?  443 LYS A N   1 
ATOM   2082 C CA  . LYS A 1 288 ? 25.502 18.116 42.882 1.00 71.67  ?  443 LYS A CA  1 
ATOM   2083 C C   . LYS A 1 288 ? 24.541 19.134 42.235 1.00 73.94  ?  443 LYS A C   1 
ATOM   2084 O O   . LYS A 1 288 ? 23.827 19.840 42.953 1.00 73.24  ?  443 LYS A O   1 
ATOM   2085 C CB  . LYS A 1 288 ? 26.662 18.807 43.624 1.00 73.90  ?  443 LYS A CB  1 
ATOM   2086 N N   . ARG A 1 289 ? 24.511 19.180 40.873 1.00 69.47  ?  444 ARG A N   1 
ATOM   2087 C CA  . ARG A 1 289 ? 23.644 20.060 40.069 1.00 67.97  ?  444 ARG A CA  1 
ATOM   2088 C C   . ARG A 1 289 ? 22.196 19.536 40.020 1.00 70.33  ?  444 ARG A C   1 
ATOM   2089 O O   . ARG A 1 289 ? 22.018 18.317 39.957 1.00 69.97  ?  444 ARG A O   1 
ATOM   2090 C CB  . ARG A 1 289 ? 24.172 20.167 38.631 1.00 64.48  ?  444 ARG A CB  1 
ATOM   2091 C CG  . ARG A 1 289 ? 25.402 21.036 38.458 1.00 63.71  ?  444 ARG A CG  1 
ATOM   2092 C CD  . ARG A 1 289 ? 25.871 20.984 37.022 1.00 52.98  ?  444 ARG A CD  1 
ATOM   2093 N NE  . ARG A 1 289 ? 27.330 20.989 36.923 1.00 45.55  ?  444 ARG A NE  1 
ATOM   2094 C CZ  . ARG A 1 289 ? 28.012 20.420 35.930 1.00 62.45  ?  444 ARG A CZ  1 
ATOM   2095 N NH1 . ARG A 1 289 ? 27.370 19.803 34.940 1.00 51.84  ?  444 ARG A NH1 1 
ATOM   2096 N NH2 . ARG A 1 289 ? 29.342 20.447 35.927 1.00 38.20  1  444 ARG A NH2 1 
ATOM   2097 N N   . PRO A 1 290 ? 21.153 20.414 39.987 1.00 67.13  ?  445 PRO A N   1 
ATOM   2098 C CA  . PRO A 1 290 ? 19.772 19.903 39.891 1.00 67.04  ?  445 PRO A CA  1 
ATOM   2099 C C   . PRO A 1 290 ? 19.431 19.428 38.485 1.00 71.71  ?  445 PRO A C   1 
ATOM   2100 O O   . PRO A 1 290 ? 20.063 19.879 37.524 1.00 72.10  ?  445 PRO A O   1 
ATOM   2101 C CB  . PRO A 1 290 ? 18.917 21.115 40.271 1.00 68.31  ?  445 PRO A CB  1 
ATOM   2102 C CG  . PRO A 1 290 ? 19.728 22.287 39.949 1.00 72.56  ?  445 PRO A CG  1 
ATOM   2103 C CD  . PRO A 1 290 ? 21.173 21.893 40.026 1.00 68.69  ?  445 PRO A CD  1 
ATOM   2104 N N   . ASP A 1 291 ? 18.433 18.534 38.352 1.00 67.55  ?  446 ASP A N   1 
ATOM   2105 C CA  . ASP A 1 291 ? 18.004 18.067 37.029 1.00 67.40  ?  446 ASP A CA  1 
ATOM   2106 C C   . ASP A 1 291 ? 17.111 19.157 36.416 1.00 71.69  ?  446 ASP A C   1 
ATOM   2107 O O   . ASP A 1 291 ? 16.741 20.105 37.129 1.00 72.86  ?  446 ASP A O   1 
ATOM   2108 C CB  . ASP A 1 291 ? 17.289 16.701 37.099 1.00 69.43  ?  446 ASP A CB  1 
ATOM   2109 C CG  . ASP A 1 291 ? 16.150 16.593 38.106 1.00 85.64  ?  446 ASP A CG  1 
ATOM   2110 O OD1 . ASP A 1 291 ? 15.167 17.362 37.985 1.00 86.50  ?  446 ASP A OD1 1 
ATOM   2111 O OD2 . ASP A 1 291 ? 16.206 15.693 38.969 1.00 95.95  -1 446 ASP A OD2 1 
ATOM   2112 N N   . ILE A 1 292 ? 16.766 19.041 35.121 1.00 65.25  ?  447 ILE A N   1 
ATOM   2113 C CA  . ILE A 1 292 ? 15.926 20.051 34.477 1.00 63.92  ?  447 ILE A CA  1 
ATOM   2114 C C   . ILE A 1 292 ? 14.551 20.280 35.131 1.00 67.53  ?  447 ILE A C   1 
ATOM   2115 O O   . ILE A 1 292 ? 14.180 21.441 35.346 1.00 66.58  ?  447 ILE A O   1 
ATOM   2116 C CB  . ILE A 1 292 ? 15.935 19.978 32.931 1.00 66.17  ?  447 ILE A CB  1 
ATOM   2117 C CG1 . ILE A 1 292 ? 15.429 21.287 32.267 1.00 65.82  ?  447 ILE A CG1 1 
ATOM   2118 C CG2 . ILE A 1 292 ? 15.221 18.741 32.414 1.00 66.48  ?  447 ILE A CG2 1 
ATOM   2119 C CD1 . ILE A 1 292 ? 16.354 22.543 32.432 1.00 66.42  ?  447 ILE A CD1 1 
ATOM   2120 N N   . LYS A 1 293 ? 13.844 19.181 35.523 1.00 64.32  ?  448 LYS A N   1 
ATOM   2121 C CA  . LYS A 1 293 ? 12.541 19.243 36.208 1.00 63.87  ?  448 LYS A CA  1 
ATOM   2122 C C   . LYS A 1 293 ? 12.617 20.039 37.536 1.00 69.07  ?  448 LYS A C   1 
ATOM   2123 O O   . LYS A 1 293 ? 11.686 20.780 37.850 1.00 69.06  ?  448 LYS A O   1 
ATOM   2124 C CB  . LYS A 1 293 ? 11.960 17.844 36.418 1.00 65.25  ?  448 LYS A CB  1 
ATOM   2125 N N   . LYS A 1 294 ? 13.748 19.938 38.272 1.00 65.51  ?  449 LYS A N   1 
ATOM   2126 C CA  . LYS A 1 294 ? 13.950 20.703 39.502 1.00 65.80  ?  449 LYS A CA  1 
ATOM   2127 C C   . LYS A 1 294 ? 14.174 22.186 39.166 1.00 70.78  ?  449 LYS A C   1 
ATOM   2128 O O   . LYS A 1 294 ? 13.600 23.050 39.839 1.00 71.62  ?  449 LYS A O   1 
ATOM   2129 C CB  . LYS A 1 294 ? 15.105 20.119 40.352 1.00 67.76  ?  449 LYS A CB  1 
ATOM   2130 C CG  . LYS A 1 294 ? 15.459 20.900 41.628 1.00 70.17  ?  449 LYS A CG  1 
ATOM   2131 C CD  . LYS A 1 294 ? 14.435 20.862 42.758 1.00 80.36  ?  449 LYS A CD  1 
ATOM   2132 C CE  . LYS A 1 294 ? 15.000 21.573 43.973 1.00 90.70  ?  449 LYS A CE  1 
ATOM   2133 N NZ  . LYS A 1 294 ? 14.011 21.713 45.078 1.00 94.18  1  449 LYS A NZ  1 
ATOM   2134 N N   . VAL A 1 295 ? 14.983 22.472 38.115 1.00 66.12  ?  450 VAL A N   1 
ATOM   2135 C CA  . VAL A 1 295 ? 15.273 23.835 37.640 1.00 65.58  ?  450 VAL A CA  1 
ATOM   2136 C C   . VAL A 1 295 ? 13.931 24.510 37.266 1.00 70.00  ?  450 VAL A C   1 
ATOM   2137 O O   . VAL A 1 295 ? 13.673 25.644 37.684 1.00 68.62  ?  450 VAL A O   1 
ATOM   2138 C CB  . VAL A 1 295 ? 16.327 23.850 36.484 1.00 68.90  ?  450 VAL A CB  1 
ATOM   2139 C CG1 . VAL A 1 295 ? 16.456 25.228 35.847 1.00 68.53  ?  450 VAL A CG1 1 
ATOM   2140 C CG2 . VAL A 1 295 ? 17.693 23.362 36.969 1.00 68.57  ?  450 VAL A CG2 1 
ATOM   2141 N N   . GLN A 1 296 ? 13.053 23.763 36.550 1.00 67.60  ?  451 GLN A N   1 
ATOM   2142 C CA  . GLN A 1 296 ? 11.711 24.195 36.165 1.00 67.99  ?  451 GLN A CA  1 
ATOM   2143 C C   . GLN A 1 296 ? 10.917 24.583 37.413 1.00 75.09  ?  451 GLN A C   1 
ATOM   2144 O O   . GLN A 1 296 ? 10.359 25.680 37.441 1.00 75.28  ?  451 GLN A O   1 
ATOM   2145 C CB  . GLN A 1 296 ? 10.973 23.071 35.429 1.00 69.02  ?  451 GLN A CB  1 
ATOM   2146 C CG  . GLN A 1 296 ? 11.399 22.854 33.992 1.00 74.02  ?  451 GLN A CG  1 
ATOM   2147 C CD  . GLN A 1 296 ? 10.420 21.940 33.301 1.00 84.41  ?  451 GLN A CD  1 
ATOM   2148 O OE1 . GLN A 1 296 ? 10.267 20.758 33.649 1.00 75.10  ?  451 GLN A OE1 1 
ATOM   2149 N NE2 . GLN A 1 296 ? 9.707  22.485 32.327 1.00 73.41  ?  451 GLN A NE2 1 
ATOM   2150 N N   . GLN A 1 297 ? 10.908 23.704 38.459 1.00 73.12  ?  452 GLN A N   1 
ATOM   2151 C CA  . GLN A 1 297 ? 10.207 23.904 39.738 1.00 73.52  ?  452 GLN A CA  1 
ATOM   2152 C C   . GLN A 1 297 ? 10.622 25.208 40.412 1.00 78.33  ?  452 GLN A C   1 
ATOM   2153 O O   . GLN A 1 297 ? 9.759  26.006 40.789 1.00 77.99  ?  452 GLN A O   1 
ATOM   2154 C CB  . GLN A 1 297 ? 10.460 22.732 40.714 1.00 75.09  ?  452 GLN A CB  1 
ATOM   2155 C CG  . GLN A 1 297 ? 9.818  21.391 40.371 1.00 95.42  ?  452 GLN A CG  1 
ATOM   2156 C CD  . GLN A 1 297 ? 10.294 20.305 41.318 1.00 112.54 ?  452 GLN A CD  1 
ATOM   2157 O OE1 . GLN A 1 297 ? 10.085 20.372 42.537 1.00 111.39 ?  452 GLN A OE1 1 
ATOM   2158 N NE2 . GLN A 1 297 ? 10.948 19.282 40.781 1.00 96.56  ?  452 GLN A NE2 1 
ATOM   2159 N N   . LEU A 1 298 ? 11.942 25.429 40.546 1.00 75.37  ?  453 LEU A N   1 
ATOM   2160 C CA  . LEU A 1 298 ? 12.521 26.621 41.178 1.00 75.49  ?  453 LEU A CA  1 
ATOM   2161 C C   . LEU A 1 298 ? 12.230 27.927 40.424 1.00 77.92  ?  453 LEU A C   1 
ATOM   2162 O O   . LEU A 1 298 ? 12.138 28.981 41.054 1.00 77.62  ?  453 LEU A O   1 
ATOM   2163 C CB  . LEU A 1 298 ? 14.034 26.444 41.389 1.00 75.85  ?  453 LEU A CB  1 
ATOM   2164 C CG  . LEU A 1 298 ? 14.514 25.202 42.145 1.00 80.87  ?  453 LEU A CG  1 
ATOM   2165 C CD1 . LEU A 1 298 ? 16.024 25.094 42.087 1.00 80.90  ?  453 LEU A CD1 1 
ATOM   2166 C CD2 . LEU A 1 298 ? 14.023 25.198 43.593 1.00 85.05  ?  453 LEU A CD2 1 
ATOM   2167 N N   . LEU A 1 299 ? 12.078 27.853 39.091 1.00 72.74  ?  454 LEU A N   1 
ATOM   2168 C CA  . LEU A 1 299 ? 11.764 29.015 38.264 1.00 71.60  ?  454 LEU A CA  1 
ATOM   2169 C C   . LEU A 1 299 ? 10.269 29.358 38.312 1.00 76.64  ?  454 LEU A C   1 
ATOM   2170 O O   . LEU A 1 299 ? 9.915  30.539 38.272 1.00 76.56  ?  454 LEU A O   1 
ATOM   2171 C CB  . LEU A 1 299 ? 12.266 28.832 36.823 1.00 71.03  ?  454 LEU A CB  1 
ATOM   2172 C CG  . LEU A 1 299 ? 13.784 28.876 36.610 1.00 74.04  ?  454 LEU A CG  1 
ATOM   2173 C CD1 . LEU A 1 299 ? 14.135 28.416 35.220 1.00 73.65  ?  454 LEU A CD1 1 
ATOM   2174 C CD2 . LEU A 1 299 ? 14.355 30.264 36.860 1.00 74.61  ?  454 LEU A CD2 1 
ATOM   2175 N N   . GLN A 1 300 ? 9.399  28.336 38.422 1.00 74.49  ?  455 GLN A N   1 
ATOM   2176 C CA  . GLN A 1 300 ? 7.949  28.523 38.552 1.00 74.98  ?  455 GLN A CA  1 
ATOM   2177 C C   . GLN A 1 300 ? 7.628  29.021 39.981 1.00 81.22  ?  455 GLN A C   1 
ATOM   2178 O O   . GLN A 1 300 ? 6.638  29.729 40.177 1.00 81.19  ?  455 GLN A O   1 
ATOM   2179 C CB  . GLN A 1 300 ? 7.192  27.229 38.222 1.00 75.90  ?  455 GLN A CB  1 
ATOM   2180 N N   . GLU A 1 301 ? 8.501  28.671 40.958 1.00 78.59  ?  456 GLU A N   1 
ATOM   2181 C CA  . GLU A 1 301 ? 8.434  29.080 42.368 1.00 78.91  ?  456 GLU A CA  1 
ATOM   2182 C C   . GLU A 1 301 ? 8.818  30.552 42.513 1.00 83.16  ?  456 GLU A C   1 
ATOM   2183 O O   . GLU A 1 301 ? 8.277  31.262 43.360 1.00 82.42  ?  456 GLU A O   1 
ATOM   2184 C CB  . GLU A 1 301 ? 9.391  28.214 43.214 1.00 80.44  ?  456 GLU A CB  1 
ATOM   2185 C CG  . GLU A 1 301 ? 8.701  27.076 43.950 1.00 90.25  ?  456 GLU A CG  1 
ATOM   2186 C CD  . GLU A 1 301 ? 9.390  25.725 44.011 1.00 100.41 ?  456 GLU A CD  1 
ATOM   2187 O OE1 . GLU A 1 301 ? 10.584 25.662 44.388 1.00 94.07  ?  456 GLU A OE1 1 
ATOM   2188 O OE2 . GLU A 1 301 ? 8.754  24.731 43.599 1.00 80.51  -1 456 GLU A OE2 1 
ATOM   2189 N N   . MET A 1 302 ? 9.767  30.998 41.681 1.00 80.70  ?  457 MET A N   1 
ATOM   2190 C CA  . MET A 1 302 ? 10.319 32.350 41.604 1.00 80.77  ?  457 MET A CA  1 
ATOM   2191 C C   . MET A 1 302 ? 9.236  33.399 41.250 1.00 84.63  ?  457 MET A C   1 
ATOM   2192 O O   . MET A 1 302 ? 9.296  34.528 41.745 1.00 83.95  ?  457 MET A O   1 
ATOM   2193 C CB  . MET A 1 302 ? 11.481 32.338 40.584 1.00 83.13  ?  457 MET A CB  1 
ATOM   2194 C CG  . MET A 1 302 ? 12.127 33.680 40.301 1.00 86.89  ?  457 MET A CG  1 
ATOM   2195 S SD  . MET A 1 302 ? 13.240 33.643 38.866 1.00 90.98  ?  457 MET A SD  1 
ATOM   2196 C CE  . MET A 1 302 ? 12.077 33.321 37.536 1.00 87.66  ?  457 MET A CE  1 
ATOM   2197 N N   . THR A 1 303 ? 8.242  33.014 40.420 1.00 81.08  ?  458 THR A N   1 
ATOM   2198 C CA  . THR A 1 303 ? 7.159  33.904 39.982 1.00 112.84 ?  458 THR A CA  1 
ATOM   2199 C C   . THR A 1 303 ? 5.819  33.575 40.655 1.00 133.24 ?  458 THR A C   1 
ATOM   2200 O O   . THR A 1 303 ? 4.834  34.291 40.473 1.00 88.71  ?  458 THR A O   1 
ATOM   2201 C CB  . THR A 1 303 ? 7.069  33.947 38.441 1.00 120.82 ?  458 THR A CB  1 
ATOM   2202 O OG1 . THR A 1 303 ? 7.003  32.615 37.929 1.00 123.38 ?  458 THR A OG1 1 
ATOM   2203 C CG2 . THR A 1 303 ? 8.233  34.692 37.802 1.00 116.91 ?  458 THR A CG2 1 
ATOM   2204 N N   . PHE B 2 10  ? 11.771 87.250 38.509 1.00 120.10 ?  165 PHE B N   1 
ATOM   2205 C CA  . PHE B 2 10  ? 12.578 86.391 39.372 1.00 120.02 ?  165 PHE B CA  1 
ATOM   2206 C C   . PHE B 2 10  ? 11.707 85.659 40.401 1.00 124.78 ?  165 PHE B C   1 
ATOM   2207 O O   . PHE B 2 10  ? 10.759 86.250 40.932 1.00 124.46 ?  165 PHE B O   1 
ATOM   2208 C CB  . PHE B 2 10  ? 13.672 87.212 40.073 1.00 121.66 ?  165 PHE B CB  1 
ATOM   2209 N N   . HIS B 2 11  ? 12.031 84.372 40.684 1.00 121.32 ?  166 HIS B N   1 
ATOM   2210 C CA  . HIS B 2 11  ? 11.293 83.534 41.639 1.00 120.93 ?  166 HIS B CA  1 
ATOM   2211 C C   . HIS B 2 11  ? 12.176 82.541 42.411 1.00 124.63 ?  166 HIS B C   1 
ATOM   2212 O O   . HIS B 2 11  ? 13.217 82.122 41.900 1.00 124.22 ?  166 HIS B O   1 
ATOM   2213 C CB  . HIS B 2 11  ? 10.157 82.786 40.924 1.00 121.57 ?  166 HIS B CB  1 
ATOM   2214 N N   . SER B 2 12  ? 11.742 82.166 43.643 1.00 121.15 ?  167 SER B N   1 
ATOM   2215 C CA  . SER B 2 12  ? 12.394 81.189 44.543 1.00 120.90 ?  167 SER B CA  1 
ATOM   2216 C C   . SER B 2 12  ? 11.392 80.606 45.573 1.00 124.38 ?  167 SER B C   1 
ATOM   2217 O O   . SER B 2 12  ? 10.279 81.127 45.695 1.00 123.85 ?  167 SER B O   1 
ATOM   2218 C CB  . SER B 2 12  ? 13.612 81.795 45.238 1.00 124.17 ?  167 SER B CB  1 
ATOM   2219 O OG  . SER B 2 12  ? 14.521 80.783 45.648 1.00 131.58 ?  167 SER B OG  1 
ATOM   2220 N N   . PHE B 2 13  ? 11.776 79.522 46.295 1.00 120.62 ?  168 PHE B N   1 
ATOM   2221 C CA  . PHE B 2 13  ? 10.904 78.859 47.279 1.00 120.26 ?  168 PHE B CA  1 
ATOM   2222 C C   . PHE B 2 13  ? 11.589 78.448 48.610 1.00 123.07 ?  168 PHE B C   1 
ATOM   2223 O O   . PHE B 2 13  ? 12.818 78.508 48.723 1.00 122.74 ?  168 PHE B O   1 
ATOM   2224 C CB  . PHE B 2 13  ? 10.181 77.661 46.632 1.00 122.09 ?  168 PHE B CB  1 
ATOM   2225 N N   . SER B 2 14  ? 10.767 78.036 49.612 1.00 118.42 ?  169 SER B N   1 
ATOM   2226 C CA  . SER B 2 14  ? 11.171 77.589 50.957 1.00 117.84 ?  169 SER B CA  1 
ATOM   2227 C C   . SER B 2 14  ? 11.660 76.133 50.956 1.00 120.23 ?  169 SER B C   1 
ATOM   2228 O O   . SER B 2 14  ? 11.550 75.463 49.930 1.00 120.30 ?  169 SER B O   1 
ATOM   2229 C CB  . SER B 2 14  ? 10.012 77.759 51.940 1.00 122.04 ?  169 SER B CB  1 
ATOM   2230 O OG  . SER B 2 14  ? 10.349 77.335 53.252 1.00 131.46 ?  169 SER B OG  1 
ATOM   2231 N N   . PHE B 2 15  ? 12.181 75.641 52.108 1.00 115.14 ?  170 PHE B N   1 
ATOM   2232 C CA  . PHE B 2 15  ? 12.720 74.282 52.246 1.00 114.17 ?  170 PHE B CA  1 
ATOM   2233 C C   . PHE B 2 15  ? 11.989 73.379 53.260 1.00 115.85 ?  170 PHE B C   1 
ATOM   2234 O O   . PHE B 2 15  ? 12.516 72.318 53.612 1.00 115.04 ?  170 PHE B O   1 
ATOM   2235 C CB  . PHE B 2 15  ? 14.235 74.338 52.533 1.00 115.97 ?  170 PHE B CB  1 
ATOM   2236 N N   . TYR B 2 16  ? 10.780 73.779 53.716 1.00 111.41 ?  171 TYR B N   1 
ATOM   2237 C CA  . TYR B 2 16  ? 10.012 72.983 54.688 1.00 110.72 ?  171 TYR B CA  1 
ATOM   2238 C C   . TYR B 2 16  ? 9.059  71.982 54.009 1.00 111.17 ?  171 TYR B C   1 
ATOM   2239 O O   . TYR B 2 16  ? 9.041  70.801 54.363 1.00 109.87 ?  171 TYR B O   1 
ATOM   2240 C CB  . TYR B 2 16  ? 9.301  73.878 55.743 1.00 112.50 ?  171 TYR B CB  1 
ATOM   2241 C CG  . TYR B 2 16  ? 7.986  74.494 55.302 1.00 115.36 ?  171 TYR B CG  1 
ATOM   2242 C CD1 . TYR B 2 16  ? 6.767  73.927 55.673 1.00 117.23 ?  171 TYR B CD1 1 
ATOM   2243 C CD2 . TYR B 2 16  ? 7.960  75.641 54.512 1.00 116.59 ?  171 TYR B CD2 1 
ATOM   2244 C CE1 . TYR B 2 16  ? 5.554  74.478 55.256 1.00 117.88 ?  171 TYR B CE1 1 
ATOM   2245 C CE2 . TYR B 2 16  ? 6.753  76.206 54.096 1.00 117.66 ?  171 TYR B CE2 1 
ATOM   2246 C CZ  . TYR B 2 16  ? 5.553  75.619 54.469 1.00 125.72 ?  171 TYR B CZ  1 
ATOM   2247 O OH  . TYR B 2 16  ? 4.364  76.171 54.056 1.00 128.04 ?  171 TYR B OH  1 
ATOM   2248 N N   . GLU B 2 17  ? 8.284  72.475 53.026 1.00 106.08 ?  172 GLU B N   1 
ATOM   2249 C CA  . GLU B 2 17  ? 7.307  71.735 52.222 1.00 105.15 ?  172 GLU B CA  1 
ATOM   2250 C C   . GLU B 2 17  ? 8.012  70.771 51.269 1.00 107.24 ?  172 GLU B C   1 
ATOM   2251 O O   . GLU B 2 17  ? 7.385  69.837 50.771 1.00 106.24 ?  172 GLU B O   1 
ATOM   2252 C CB  . GLU B 2 17  ? 6.386  72.707 51.444 1.00 106.40 ?  172 GLU B CB  1 
ATOM   2253 C CG  . GLU B 2 17  ? 7.078  73.584 50.402 1.00 115.88 ?  172 GLU B CG  1 
ATOM   2254 C CD  . GLU B 2 17  ? 7.874  74.767 50.925 1.00 131.79 ?  172 GLU B CD  1 
ATOM   2255 O OE1 . GLU B 2 17  ? 7.431  75.918 50.707 1.00 121.86 ?  172 GLU B OE1 1 
ATOM   2256 O OE2 . GLU B 2 17  ? 8.946  74.549 51.537 1.00 121.00 -1 172 GLU B OE2 1 
ATOM   2257 N N   . LEU B 2 18  ? 9.312  71.018 51.011 1.00 102.91 ?  173 LEU B N   1 
ATOM   2258 C CA  . LEU B 2 18  ? 10.149 70.204 50.143 1.00 101.96 ?  173 LEU B CA  1 
ATOM   2259 C C   . LEU B 2 18  ? 10.348 68.829 50.727 1.00 105.48 ?  173 LEU B C   1 
ATOM   2260 O O   . LEU B 2 18  ? 10.217 67.859 49.981 1.00 105.28 ?  173 LEU B O   1 
ATOM   2261 C CB  . LEU B 2 18  ? 11.503 70.869 49.869 1.00 101.63 ?  173 LEU B CB  1 
ATOM   2262 C CG  . LEU B 2 18  ? 11.508 72.050 48.911 1.00 105.52 ?  173 LEU B CG  1 
ATOM   2263 C CD1 . LEU B 2 18  ? 12.922 72.559 48.718 1.00 105.46 ?  173 LEU B CD1 1 
ATOM   2264 C CD2 . LEU B 2 18  ? 10.895 71.685 47.567 1.00 106.67 ?  173 LEU B CD2 1 
ATOM   2265 N N   . LYS B 2 19  ? 10.634 68.734 52.055 1.00 101.76 ?  174 LYS B N   1 
ATOM   2266 C CA  . LYS B 2 19  ? 10.808 67.449 52.750 1.00 101.71 ?  174 LYS B CA  1 
ATOM   2267 C C   . LYS B 2 19  ? 9.641  66.510 52.409 1.00 106.07 ?  174 LYS B C   1 
ATOM   2268 O O   . LYS B 2 19  ? 9.883  65.441 51.867 1.00 105.48 ?  174 LYS B O   1 
ATOM   2269 C CB  . LYS B 2 19  ? 10.937 67.650 54.270 1.00 104.02 ?  174 LYS B CB  1 
ATOM   2270 N N   . ASN B 2 20  ? 8.384  66.923 52.648 1.00 103.12 ?  175 ASN B N   1 
ATOM   2271 C CA  . ASN B 2 20  ? 7.224  66.088 52.313 1.00 103.18 ?  175 ASN B CA  1 
ATOM   2272 C C   . ASN B 2 20  ? 7.031  65.877 50.791 1.00 107.64 ?  175 ASN B C   1 
ATOM   2273 O O   . ASN B 2 20  ? 6.631  64.779 50.383 1.00 107.93 ?  175 ASN B O   1 
ATOM   2274 C CB  . ASN B 2 20  ? 5.938  66.542 53.030 1.00 103.61 ?  175 ASN B CB  1 
ATOM   2275 C CG  . ASN B 2 20  ? 5.584  68.004 52.872 1.00 128.66 ?  175 ASN B CG  1 
ATOM   2276 O OD1 . ASN B 2 20  ? 6.039  68.866 53.628 1.00 126.98 ?  175 ASN B OD1 1 
ATOM   2277 N ND2 . ASN B 2 20  ? 4.667  68.303 51.964 1.00 118.53 ?  175 ASN B ND2 1 
ATOM   2278 N N   . VAL B 2 21  ? 7.373  66.900 49.961 1.00 103.46 ?  176 VAL B N   1 
ATOM   2279 C CA  . VAL B 2 21  ? 7.299  66.872 48.487 1.00 102.93 ?  176 VAL B CA  1 
ATOM   2280 C C   . VAL B 2 21  ? 8.252  65.809 47.895 1.00 106.78 ?  176 VAL B C   1 
ATOM   2281 O O   . VAL B 2 21  ? 7.965  65.256 46.832 1.00 106.31 ?  176 VAL B O   1 
ATOM   2282 C CB  . VAL B 2 21  ? 7.479  68.300 47.872 1.00 106.39 ?  176 VAL B CB  1 
ATOM   2283 C CG1 . VAL B 2 21  ? 8.629  68.394 46.868 1.00 106.07 ?  176 VAL B CG1 1 
ATOM   2284 C CG2 . VAL B 2 21  ? 6.181  68.812 47.270 1.00 106.00 ?  176 VAL B CG2 1 
ATOM   2285 N N   . THR B 2 22  ? 9.353  65.510 48.615 1.00 103.20 ?  177 THR B N   1 
ATOM   2286 C CA  . THR B 2 22  ? 10.385 64.548 48.234 1.00 103.13 ?  177 THR B CA  1 
ATOM   2287 C C   . THR B 2 22  ? 10.342 63.260 49.080 1.00 107.46 ?  177 THR B C   1 
ATOM   2288 O O   . THR B 2 22  ? 11.309 62.488 49.054 1.00 106.84 ?  177 THR B O   1 
ATOM   2289 C CB  . THR B 2 22  ? 11.774 65.216 48.330 1.00 112.31 ?  177 THR B CB  1 
ATOM   2290 O OG1 . THR B 2 22  ? 12.036 65.577 49.688 1.00 110.72 ?  177 THR B OG1 1 
ATOM   2291 C CG2 . THR B 2 22  ? 11.943 66.424 47.380 1.00 112.15 ?  177 THR B CG2 1 
ATOM   2292 N N   . ASN B 2 23  ? 9.227  63.029 49.821 1.00 104.57 ?  178 ASN B N   1 
ATOM   2293 C CA  . ASN B 2 23  ? 9.022  61.894 50.742 1.00 104.81 ?  178 ASN B CA  1 
ATOM   2294 C C   . ASN B 2 23  ? 10.197 61.794 51.746 1.00 109.79 ?  178 ASN B C   1 
ATOM   2295 O O   . ASN B 2 23  ? 10.879 60.766 51.859 1.00 109.55 ?  178 ASN B O   1 
ATOM   2296 C CB  . ASN B 2 23  ? 8.720  60.582 50.006 1.00 104.76 ?  178 ASN B CB  1 
ATOM   2297 N N   . ASN B 2 24  ? 10.426 62.925 52.451 1.00 106.48 ?  179 ASN B N   1 
ATOM   2298 C CA  . ASN B 2 24  ? 11.491 63.171 53.429 1.00 106.24 ?  179 ASN B CA  1 
ATOM   2299 C C   . ASN B 2 24  ? 12.864 62.877 52.814 1.00 109.99 ?  179 ASN B C   1 
ATOM   2300 O O   . ASN B 2 24  ? 13.645 62.093 53.372 1.00 109.35 ?  179 ASN B O   1 
ATOM   2301 C CB  . ASN B 2 24  ? 11.236 62.450 54.768 1.00 106.54 ?  179 ASN B CB  1 
ATOM   2302 N N   . PHE B 2 25  ? 13.129 63.505 51.626 1.00 105.98 ?  180 PHE B N   1 
ATOM   2303 C CA  . PHE B 2 25  ? 14.346 63.345 50.816 1.00 105.03 ?  180 PHE B CA  1 
ATOM   2304 C C   . PHE B 2 25  ? 14.718 61.855 50.745 1.00 107.80 ?  180 PHE B C   1 
ATOM   2305 O O   . PHE B 2 25  ? 15.773 61.452 51.251 1.00 107.47 ?  180 PHE B O   1 
ATOM   2306 C CB  . PHE B 2 25  ? 15.500 64.226 51.341 1.00 106.58 ?  180 PHE B CB  1 
ATOM   2307 N N   . ASP B 2 26  ? 13.780 61.028 50.209 1.00 103.02 ?  181 ASP B N   1 
ATOM   2308 C CA  . ASP B 2 26  ? 13.918 59.571 50.080 1.00 102.09 ?  181 ASP B CA  1 
ATOM   2309 C C   . ASP B 2 26  ? 15.033 59.224 49.102 1.00 104.13 ?  181 ASP B C   1 
ATOM   2310 O O   . ASP B 2 26  ? 14.802 59.130 47.893 1.00 103.81 ?  181 ASP B O   1 
ATOM   2311 C CB  . ASP B 2 26  ? 12.584 58.915 49.673 1.00 103.81 ?  181 ASP B CB  1 
ATOM   2312 N N   . GLU B 2 27  ? 16.258 59.066 49.639 1.00 99.34  ?  182 GLU B N   1 
ATOM   2313 C CA  . GLU B 2 27  ? 17.469 58.766 48.879 1.00 98.70  ?  182 GLU B CA  1 
ATOM   2314 C C   . GLU B 2 27  ? 17.356 57.466 48.033 1.00 101.49 ?  182 GLU B C   1 
ATOM   2315 O O   . GLU B 2 27  ? 18.242 57.169 47.226 1.00 101.37 ?  182 GLU B O   1 
ATOM   2316 C CB  . GLU B 2 27  ? 18.707 58.800 49.789 1.00 100.03 ?  182 GLU B CB  1 
ATOM   2317 N N   . ARG B 2 28  ? 16.225 56.744 48.177 1.00 96.39  ?  183 ARG B N   1 
ATOM   2318 C CA  . ARG B 2 28  ? 15.897 55.546 47.412 1.00 95.28  ?  183 ARG B CA  1 
ATOM   2319 C C   . ARG B 2 28  ? 15.582 55.973 45.963 1.00 96.75  ?  183 ARG B C   1 
ATOM   2320 O O   . ARG B 2 28  ? 15.009 57.054 45.767 1.00 96.09  ?  183 ARG B O   1 
ATOM   2321 C CB  . ARG B 2 28  ? 14.694 54.826 48.037 1.00 95.72  ?  183 ARG B CB  1 
ATOM   2322 N N   . PRO B 2 29  ? 15.980 55.177 44.938 1.00 91.54  ?  184 PRO B N   1 
ATOM   2323 C CA  . PRO B 2 29  ? 15.731 55.592 43.540 1.00 90.18  ?  184 PRO B CA  1 
ATOM   2324 C C   . PRO B 2 29  ? 14.255 55.577 43.123 1.00 89.54  ?  184 PRO B C   1 
ATOM   2325 O O   . PRO B 2 29  ? 13.457 54.875 43.742 1.00 88.15  ?  184 PRO B O   1 
ATOM   2326 C CB  . PRO B 2 29  ? 16.535 54.573 42.711 1.00 92.28  ?  184 PRO B CB  1 
ATOM   2327 C CG  . PRO B 2 29  ? 17.418 53.857 43.680 1.00 97.38  ?  184 PRO B CG  1 
ATOM   2328 C CD  . PRO B 2 29  ? 16.701 53.890 44.988 1.00 93.18  ?  184 PRO B CD  1 
ATOM   2329 N N   . ILE B 2 30  ? 13.926 56.279 42.015 1.00 83.57  ?  185 ILE B N   1 
ATOM   2330 C CA  . ILE B 2 30  ? 12.620 56.433 41.359 1.00 89.34  ?  185 ILE B CA  1 
ATOM   2331 C C   . ILE B 2 30  ? 12.072 57.846 41.525 1.00 116.85 ?  185 ILE B C   1 
ATOM   2332 O O   . ILE B 2 30  ? 12.653 58.792 40.994 1.00 80.16  ?  185 ILE B O   1 
ATOM   2333 C CB  . ILE B 2 30  ? 11.584 55.278 41.580 1.00 92.29  ?  185 ILE B CB  1 
ATOM   2334 C CG1 . ILE B 2 30  ? 12.015 53.996 40.828 1.00 92.50  ?  185 ILE B CG1 1 
ATOM   2335 C CG2 . ILE B 2 30  ? 10.165 55.687 41.181 1.00 92.87  ?  185 ILE B CG2 1 
ATOM   2336 C CD1 . ILE B 2 30  ? 11.942 52.740 41.634 1.00 98.29  ?  185 ILE B CD1 1 
ATOM   2337 N N   . GLY B 2 34  ? 11.723 56.496 46.538 1.00 98.83  ?  189 GLY B N   1 
ATOM   2338 C CA  . GLY B 2 34  ? 11.049 56.721 45.261 1.00 98.40  ?  189 GLY B CA  1 
ATOM   2339 C C   . GLY B 2 34  ? 11.211 58.188 44.833 1.00 100.74 ?  189 GLY B C   1 
ATOM   2340 O O   . GLY B 2 34  ? 10.318 58.766 44.194 1.00 100.31 ?  189 GLY B O   1 
ATOM   2341 N N   . ASN B 2 35  ? 12.369 58.792 45.189 1.00 95.44  ?  190 ASN B N   1 
ATOM   2342 C CA  . ASN B 2 35  ? 12.644 60.191 44.868 1.00 94.26  ?  190 ASN B CA  1 
ATOM   2343 C C   . ASN B 2 35  ? 14.011 60.498 44.249 1.00 95.55  ?  190 ASN B C   1 
ATOM   2344 O O   . ASN B 2 35  ? 14.070 61.418 43.434 1.00 95.35  ?  190 ASN B O   1 
ATOM   2345 C CB  . ASN B 2 35  ? 12.295 61.116 46.040 1.00 94.05  ?  190 ASN B CB  1 
ATOM   2346 C CG  . ASN B 2 35  ? 10.823 61.077 46.390 1.00 105.65 ?  190 ASN B CG  1 
ATOM   2347 O OD1 . ASN B 2 35  ? 10.448 60.167 47.272 1.00 96.07  ?  190 ASN B OD1 1 
ATOM   2348 N ND2 . ASN B 2 35  ? 10.003 61.814 45.838 1.00 94.97  ?  190 ASN B ND2 1 
ATOM   2349 N N   . LYS B 2 36  ? 15.093 59.739 44.598 1.00 89.63  ?  191 LYS B N   1 
ATOM   2350 C CA  . LYS B 2 36  ? 16.433 59.966 44.028 1.00 88.46  ?  191 LYS B CA  1 
ATOM   2351 C C   . LYS B 2 36  ? 16.501 59.752 42.522 1.00 91.57  ?  191 LYS B C   1 
ATOM   2352 O O   . LYS B 2 36  ? 16.253 58.643 42.025 1.00 91.44  ?  191 LYS B O   1 
ATOM   2353 C CB  . LYS B 2 36  ? 17.504 59.112 44.705 1.00 90.10  ?  191 LYS B CB  1 
ATOM   2354 N N   . MET B 2 37  ? 16.860 60.828 41.806 1.00 86.14  ?  192 MET B N   1 
ATOM   2355 C CA  . MET B 2 37  ? 17.024 60.836 40.357 1.00 85.26  ?  192 MET B CA  1 
ATOM   2356 C C   . MET B 2 37  ? 18.502 60.834 39.943 1.00 90.98  ?  192 MET B C   1 
ATOM   2357 O O   . MET B 2 37  ? 18.819 60.494 38.803 1.00 91.55  ?  192 MET B O   1 
ATOM   2358 C CB  . MET B 2 37  ? 16.296 62.027 39.748 1.00 86.94  ?  192 MET B CB  1 
ATOM   2359 C CG  . MET B 2 37  ? 14.819 61.996 40.003 1.00 89.93  ?  192 MET B CG  1 
ATOM   2360 S SD  . MET B 2 37  ? 13.923 63.142 38.969 1.00 93.64  ?  192 MET B SD  1 
ATOM   2361 C CE  . MET B 2 37  ? 14.546 64.683 39.565 1.00 90.44  ?  192 MET B CE  1 
ATOM   2362 N N   . GLY B 2 38  ? 19.384 61.219 40.858 1.00 87.98  ?  193 GLY B N   1 
ATOM   2363 C CA  . GLY B 2 38  ? 20.816 61.247 40.602 1.00 88.51  ?  193 GLY B CA  1 
ATOM   2364 C C   . GLY B 2 38  ? 21.597 62.006 41.646 1.00 95.20  ?  193 GLY B C   1 
ATOM   2365 O O   . GLY B 2 38  ? 21.010 62.625 42.539 1.00 95.04  ?  193 GLY B O   1 
ATOM   2366 N N   . GLU B 2 39  ? 22.933 61.944 41.547 1.00 93.71  ?  194 GLU B N   1 
ATOM   2367 C CA  . GLU B 2 39  ? 23.882 62.595 42.461 1.00 94.48  ?  194 GLU B CA  1 
ATOM   2368 C C   . GLU B 2 39  ? 25.253 62.702 41.791 1.00 102.50 ?  194 GLU B C   1 
ATOM   2369 O O   . GLU B 2 39  ? 25.347 62.596 40.567 1.00 101.63 ?  194 GLU B O   1 
ATOM   2370 C CB  . GLU B 2 39  ? 24.023 61.761 43.745 1.00 95.65  ?  194 GLU B CB  1 
ATOM   2371 N N   . GLY B 2 40  ? 26.319 62.841 42.586 1.00 102.90 ?  195 GLY B N   1 
ATOM   2372 C CA  . GLY B 2 40  ? 27.684 62.833 42.065 1.00 104.14 ?  195 GLY B CA  1 
ATOM   2373 C C   . GLY B 2 40  ? 28.514 64.085 42.229 1.00 110.44 ?  195 GLY B C   1 
ATOM   2374 O O   . GLY B 2 40  ? 29.636 64.015 42.741 1.00 110.18 ?  195 GLY B O   1 
ATOM   2375 N N   . GLY B 2 41  ? 27.992 65.209 41.737 1.00 108.41 ?  196 GLY B N   1 
ATOM   2376 C CA  . GLY B 2 41  ? 28.671 66.497 41.798 1.00 108.70 ?  196 GLY B CA  1 
ATOM   2377 C C   . GLY B 2 41  ? 28.744 67.039 43.209 1.00 113.43 ?  196 GLY B C   1 
ATOM   2378 O O   . GLY B 2 41  ? 29.345 66.427 44.102 1.00 113.02 ?  196 GLY B O   1 
ATOM   2379 N N   . PHE B 2 42  ? 28.126 68.194 43.423 1.00 110.02 ?  197 PHE B N   1 
ATOM   2380 C CA  . PHE B 2 42  ? 28.109 68.783 44.756 1.00 109.61 ?  197 PHE B CA  1 
ATOM   2381 C C   . PHE B 2 42  ? 26.718 68.698 45.408 1.00 111.28 ?  197 PHE B C   1 
ATOM   2382 O O   . PHE B 2 42  ? 26.310 69.605 46.146 1.00 111.33 ?  197 PHE B O   1 
ATOM   2383 C CB  . PHE B 2 42  ? 28.698 70.201 44.732 1.00 111.75 ?  197 PHE B CB  1 
ATOM   2384 C CG  . PHE B 2 42  ? 30.023 70.304 44.006 1.00 113.74 ?  197 PHE B CG  1 
ATOM   2385 C CD1 . PHE B 2 42  ? 30.141 71.055 42.842 1.00 116.96 ?  197 PHE B CD1 1 
ATOM   2386 C CD2 . PHE B 2 42  ? 31.146 69.621 44.468 1.00 116.12 ?  197 PHE B CD2 1 
ATOM   2387 C CE1 . PHE B 2 42  ? 31.358 71.128 42.154 1.00 117.73 ?  197 PHE B CE1 1 
ATOM   2388 C CE2 . PHE B 2 42  ? 32.363 69.692 43.778 1.00 118.80 ?  197 PHE B CE2 1 
ATOM   2389 C CZ  . PHE B 2 42  ? 32.460 70.450 42.629 1.00 116.78 ?  197 PHE B CZ  1 
ATOM   2390 N N   . GLY B 2 43  ? 26.019 67.592 45.146 1.00 105.18 ?  198 GLY B N   1 
ATOM   2391 C CA  . GLY B 2 43  ? 24.686 67.347 45.694 1.00 103.81 ?  198 GLY B CA  1 
ATOM   2392 C C   . GLY B 2 43  ? 23.933 66.133 45.176 1.00 103.90 ?  198 GLY B C   1 
ATOM   2393 O O   . GLY B 2 43  ? 24.450 65.356 44.369 1.00 103.67 ?  198 GLY B O   1 
ATOM   2394 N N   . VAL B 2 44  ? 22.703 65.958 45.678 1.00 97.20  ?  199 VAL B N   1 
ATOM   2395 C CA  . VAL B 2 44  ? 21.789 64.877 45.300 1.00 95.80  ?  199 VAL B CA  1 
ATOM   2396 C C   . VAL B 2 44  ? 20.506 65.519 44.743 1.00 97.78  ?  199 VAL B C   1 
ATOM   2397 O O   . VAL B 2 44  ? 20.008 66.487 45.322 1.00 97.72  ?  199 VAL B O   1 
ATOM   2398 C CB  . VAL B 2 44  ? 21.505 63.887 46.465 1.00 99.45  ?  199 VAL B CB  1 
ATOM   2399 C CG1 . VAL B 2 44  ? 20.530 62.780 46.042 1.00 99.53  ?  199 VAL B CG1 1 
ATOM   2400 C CG2 . VAL B 2 44  ? 22.799 63.274 46.993 1.00 99.14  ?  199 VAL B CG2 1 
ATOM   2401 N N   . VAL B 2 45  ? 20.004 64.996 43.605 1.00 91.97  ?  200 VAL B N   1 
ATOM   2402 C CA  . VAL B 2 45  ? 18.799 65.479 42.924 1.00 90.57  ?  200 VAL B CA  1 
ATOM   2403 C C   . VAL B 2 45  ? 17.609 64.561 43.229 1.00 94.26  ?  200 VAL B C   1 
ATOM   2404 O O   . VAL B 2 45  ? 17.705 63.338 43.060 1.00 94.05  ?  200 VAL B O   1 
ATOM   2405 C CB  . VAL B 2 45  ? 19.022 65.678 41.400 1.00 93.51  ?  200 VAL B CB  1 
ATOM   2406 C CG1 . VAL B 2 45  ? 17.812 66.336 40.738 1.00 92.73  ?  200 VAL B CG1 1 
ATOM   2407 C CG2 . VAL B 2 45  ? 20.281 66.494 41.136 1.00 93.31  ?  200 VAL B CG2 1 
ATOM   2408 N N   . TYR B 2 46  ? 16.477 65.167 43.639 1.00 90.32  ?  201 TYR B N   1 
ATOM   2409 C CA  . TYR B 2 46  ? 15.241 64.469 44.009 1.00 89.62  ?  201 TYR B CA  1 
ATOM   2410 C C   . TYR B 2 46  ? 14.052 64.869 43.135 1.00 93.19  ?  201 TYR B C   1 
ATOM   2411 O O   . TYR B 2 46  ? 13.973 66.011 42.675 1.00 90.79  ?  201 TYR B O   1 
ATOM   2412 C CB  . TYR B 2 46  ? 14.882 64.759 45.482 1.00 90.22  ?  201 TYR B CB  1 
ATOM   2413 C CG  . TYR B 2 46  ? 15.973 64.415 46.475 1.00 90.93  ?  201 TYR B CG  1 
ATOM   2414 C CD1 . TYR B 2 46  ? 17.035 65.288 46.706 1.00 92.46  ?  201 TYR B CD1 1 
ATOM   2415 C CD2 . TYR B 2 46  ? 15.924 63.230 47.212 1.00 91.46  ?  201 TYR B CD2 1 
ATOM   2416 C CE1 . TYR B 2 46  ? 18.040 64.975 47.619 1.00 92.40  ?  201 TYR B CE1 1 
ATOM   2417 C CE2 . TYR B 2 46  ? 16.921 62.909 48.132 1.00 92.19  ?  201 TYR B CE2 1 
ATOM   2418 C CZ  . TYR B 2 46  ? 17.970 63.792 48.344 1.00 98.41  ?  201 TYR B CZ  1 
ATOM   2419 O OH  . TYR B 2 46  ? 18.967 63.475 49.238 1.00 98.42  ?  201 TYR B OH  1 
ATOM   2420 N N   . LYS B 2 47  ? 13.091 63.933 42.975 1.00 91.73  ?  202 LYS B N   1 
ATOM   2421 C CA  . LYS B 2 47  ? 11.851 64.139 42.228 1.00 92.26  ?  202 LYS B CA  1 
ATOM   2422 C C   . LYS B 2 47  ? 10.819 64.745 43.174 1.00 97.94  ?  202 LYS B C   1 
ATOM   2423 O O   . LYS B 2 47  ? 10.532 64.176 44.229 1.00 96.79  ?  202 LYS B O   1 
ATOM   2424 C CB  . LYS B 2 47  ? 11.330 62.808 41.658 1.00 94.77  ?  202 LYS B CB  1 
ATOM   2425 N N   . GLY B 2 48  ? 10.292 65.901 42.799 1.00 96.73  ?  203 GLY B N   1 
ATOM   2426 C CA  . GLY B 2 48  ? 9.279  66.594 43.585 1.00 97.86  ?  203 GLY B CA  1 
ATOM   2427 C C   . GLY B 2 48  ? 8.044  66.972 42.789 1.00 103.88 ?  203 GLY B C   1 
ATOM   2428 O O   . GLY B 2 48  ? 8.152  67.335 41.614 1.00 103.85 ?  203 GLY B O   1 
ATOM   2429 N N   . TYR B 2 49  ? 6.859  66.892 43.423 1.00 100.61 ?  204 TYR B N   1 
ATOM   2430 C CA  . TYR B 2 49  ? 5.601  67.261 42.765 1.00 100.44 ?  204 TYR B CA  1 
ATOM   2431 C C   . TYR B 2 49  ? 4.992  68.485 43.458 1.00 105.14 ?  204 TYR B C   1 
ATOM   2432 O O   . TYR B 2 49  ? 4.411  68.341 44.536 1.00 105.80 ?  204 TYR B O   1 
ATOM   2433 C CB  . TYR B 2 49  ? 4.620  66.077 42.736 1.00 101.31 ?  204 TYR B CB  1 
ATOM   2434 N N   . VAL B 2 50  ? 5.148  69.687 42.847 1.00 100.67 ?  205 VAL B N   1 
ATOM   2435 C CA  . VAL B 2 50  ? 4.628  70.956 43.388 1.00 112.61 ?  205 VAL B CA  1 
ATOM   2436 C C   . VAL B 2 50  ? 3.397  71.465 42.621 1.00 135.04 ?  205 VAL B C   1 
ATOM   2437 O O   . VAL B 2 50  ? 2.722  72.395 43.066 1.00 92.45  ?  205 VAL B O   1 
ATOM   2438 C CB  . VAL B 2 50  ? 5.706  72.065 43.575 1.00 116.10 ?  205 VAL B CB  1 
ATOM   2439 C CG1 . VAL B 2 50  ? 6.767  71.648 44.586 1.00 115.81 ?  205 VAL B CG1 1 
ATOM   2440 C CG2 . VAL B 2 50  ? 6.338  72.474 42.250 1.00 115.88 ?  205 VAL B CG2 1 
ATOM   2441 N N   . THR B 2 53  ? 2.530  69.917 38.383 1.00 99.25  ?  208 THR B N   1 
ATOM   2442 C CA  . THR B 2 53  ? 3.840  70.231 37.814 1.00 99.38  ?  208 THR B CA  1 
ATOM   2443 C C   . THR B 2 53  ? 5.011  69.699 38.671 1.00 103.82 ?  208 THR B C   1 
ATOM   2444 O O   . THR B 2 53  ? 5.265  70.184 39.784 1.00 103.92 ?  208 THR B O   1 
ATOM   2445 C CB  . THR B 2 53  ? 3.915  71.700 37.351 1.00 107.83 ?  208 THR B CB  1 
ATOM   2446 O OG1 . THR B 2 53  ? 2.896  71.925 36.371 1.00 106.12 ?  208 THR B OG1 1 
ATOM   2447 C CG2 . THR B 2 53  ? 5.273  72.064 36.756 1.00 106.97 ?  208 THR B CG2 1 
ATOM   2448 N N   . THR B 2 54  ? 5.719  68.702 38.106 1.00 99.40  ?  209 THR B N   1 
ATOM   2449 C CA  . THR B 2 54  ? 6.838  67.935 38.657 1.00 98.19  ?  209 THR B CA  1 
ATOM   2450 C C   . THR B 2 54  ? 8.121  68.759 38.597 1.00 99.71  ?  209 THR B C   1 
ATOM   2451 O O   . THR B 2 54  ? 8.335  69.484 37.623 1.00 98.06  ?  209 THR B O   1 
ATOM   2452 C CB  . THR B 2 54  ? 6.898  66.552 37.953 1.00 104.17 ?  209 THR B CB  1 
ATOM   2453 O OG1 . THR B 2 54  ? 5.660  65.875 38.141 1.00 103.30 ?  209 THR B OG1 1 
ATOM   2454 C CG2 . THR B 2 54  ? 7.982  65.635 38.484 1.00 101.83 ?  209 THR B CG2 1 
ATOM   2455 N N   . VAL B 2 55  ? 8.950  68.671 39.656 1.00 95.73  ?  210 VAL B N   1 
ATOM   2456 C CA  . VAL B 2 55  ? 10.212 69.415 39.776 1.00 95.09  ?  210 VAL B CA  1 
ATOM   2457 C C   . VAL B 2 55  ? 11.408 68.555 40.169 1.00 96.16  ?  210 VAL B C   1 
ATOM   2458 O O   . VAL B 2 55  ? 11.245 67.456 40.712 1.00 95.08  ?  210 VAL B O   1 
ATOM   2459 C CB  . VAL B 2 55  ? 10.097 70.630 40.731 1.00 99.10  ?  210 VAL B CB  1 
ATOM   2460 C CG1 . VAL B 2 55  ? 9.248  71.739 40.119 1.00 98.76  ?  210 VAL B CG1 1 
ATOM   2461 C CG2 . VAL B 2 55  ? 9.597  70.219 42.123 1.00 98.97  ?  210 VAL B CG2 1 
ATOM   2462 N N   . ALA B 2 56  ? 12.615 69.100 39.925 1.00 90.95  ?  211 ALA B N   1 
ATOM   2463 C CA  . ALA B 2 56  ? 13.885 68.491 40.308 1.00 89.68  ?  211 ALA B CA  1 
ATOM   2464 C C   . ALA B 2 56  ? 14.476 69.345 41.441 1.00 89.92  ?  211 ALA B C   1 
ATOM   2465 O O   . ALA B 2 56  ? 14.699 70.548 41.264 1.00 88.82  ?  211 ALA B O   1 
ATOM   2466 C CB  . ALA B 2 56  ? 14.834 68.442 39.113 1.00 90.41  ?  211 ALA B CB  1 
ATOM   2467 N N   . VAL B 2 57  ? 14.660 68.738 42.616 1.00 84.37  ?  212 VAL B N   1 
ATOM   2468 C CA  . VAL B 2 57  ? 15.198 69.434 43.782 1.00 83.34  ?  212 VAL B CA  1 
ATOM   2469 C C   . VAL B 2 57  ? 16.645 68.983 44.000 1.00 85.90  ?  212 VAL B C   1 
ATOM   2470 O O   . VAL B 2 57  ? 16.880 67.826 44.373 1.00 85.50  ?  212 VAL B O   1 
ATOM   2471 C CB  . VAL B 2 57  ? 14.335 69.234 45.078 1.00 86.75  ?  212 VAL B CB  1 
ATOM   2472 C CG1 . VAL B 2 57  ? 14.819 70.149 46.214 1.00 86.48  ?  212 VAL B CG1 1 
ATOM   2473 C CG2 . VAL B 2 57  ? 12.835 69.423 44.814 1.00 86.19  ?  212 VAL B CG2 1 
ATOM   2474 N N   . LYS B 2 58  ? 17.608 69.885 43.769 1.00 81.23  ?  213 LYS B N   1 
ATOM   2475 C CA  . LYS B 2 58  ? 19.011 69.567 44.013 1.00 80.59  ?  213 LYS B CA  1 
ATOM   2476 C C   . LYS B 2 58  ? 19.389 70.083 45.403 1.00 84.62  ?  213 LYS B C   1 
ATOM   2477 O O   . LYS B 2 58  ? 19.370 71.295 45.632 1.00 85.71  ?  213 LYS B O   1 
ATOM   2478 C CB  . LYS B 2 58  ? 19.935 70.135 42.913 1.00 82.16  ?  213 LYS B CB  1 
ATOM   2479 N N   . LYS B 2 59  ? 19.674 69.163 46.338 1.00 79.22  ?  214 LYS B N   1 
ATOM   2480 C CA  . LYS B 2 59  ? 20.088 69.499 47.693 1.00 78.63  ?  214 LYS B CA  1 
ATOM   2481 C C   . LYS B 2 59  ? 21.614 69.353 47.786 1.00 83.31  ?  214 LYS B C   1 
ATOM   2482 O O   . LYS B 2 59  ? 22.142 68.226 47.803 1.00 82.38  ?  214 LYS B O   1 
ATOM   2483 C CB  . LYS B 2 59  ? 19.362 68.630 48.733 1.00 81.25  ?  214 LYS B CB  1 
ATOM   2484 N N   . LEU B 2 60  ? 22.318 70.516 47.807 1.00 80.16  ?  215 LEU B N   1 
ATOM   2485 C CA  . LEU B 2 60  ? 23.783 70.668 47.889 1.00 93.82  ?  215 LEU B CA  1 
ATOM   2486 C C   . LEU B 2 60  ? 24.365 69.840 49.040 1.00 128.64 ?  215 LEU B C   1 
ATOM   2487 O O   . LEU B 2 60  ? 23.744 69.745 50.101 1.00 97.66  ?  215 LEU B O   1 
ATOM   2488 C CB  . LEU B 2 60  ? 24.144 72.159 48.101 1.00 93.59  ?  215 LEU B CB  1 
ATOM   2489 C CG  . LEU B 2 60  ? 24.295 73.140 46.899 1.00 97.64  ?  215 LEU B CG  1 
ATOM   2490 C CD1 . LEU B 2 60  ? 25.726 73.264 46.444 1.00 97.51  ?  215 LEU B CD1 1 
ATOM   2491 C CD2 . LEU B 2 60  ? 23.308 72.881 45.760 1.00 99.85  ?  215 LEU B CD2 1 
ATOM   2492 N N   . GLU B 2 69  ? 30.838 77.672 53.349 1.00 156.52 ?  224 GLU B N   1 
ATOM   2493 C CA  . GLU B 2 69  ? 31.079 78.852 52.522 1.00 156.28 ?  224 GLU B CA  1 
ATOM   2494 C C   . GLU B 2 69  ? 31.286 78.475 51.053 1.00 159.92 ?  224 GLU B C   1 
ATOM   2495 O O   . GLU B 2 69  ? 30.713 79.119 50.182 1.00 159.50 ?  224 GLU B O   1 
ATOM   2496 C CB  . GLU B 2 69  ? 32.269 79.664 53.057 1.00 157.63 ?  224 GLU B CB  1 
ATOM   2497 N N   . GLU B 2 70  ? 32.105 77.439 50.794 1.00 156.41 ?  225 GLU B N   1 
ATOM   2498 C CA  . GLU B 2 70  ? 32.449 76.868 49.484 1.00 156.28 ?  225 GLU B CA  1 
ATOM   2499 C C   . GLU B 2 70  ? 31.229 76.330 48.724 1.00 160.11 ?  225 GLU B C   1 
ATOM   2500 O O   . GLU B 2 70  ? 31.100 76.598 47.527 1.00 159.67 ?  225 GLU B O   1 
ATOM   2501 C CB  . GLU B 2 70  ? 33.524 75.779 49.636 1.00 157.66 ?  225 GLU B CB  1 
ATOM   2502 N N   . LEU B 2 71  ? 30.335 75.586 49.419 1.00 156.50 ?  226 LEU B N   1 
ATOM   2503 C CA  . LEU B 2 71  ? 29.080 75.063 48.869 1.00 156.15 ?  226 LEU B CA  1 
ATOM   2504 C C   . LEU B 2 71  ? 28.133 76.245 48.625 1.00 159.80 ?  226 LEU B C   1 
ATOM   2505 O O   . LEU B 2 71  ? 27.538 76.327 47.551 1.00 159.38 ?  226 LEU B O   1 
ATOM   2506 C CB  . LEU B 2 71  ? 28.447 74.054 49.834 1.00 156.17 ?  226 LEU B CB  1 
ATOM   2507 N N   . LYS B 2 72  ? 28.047 77.191 49.597 1.00 156.13 ?  227 LYS B N   1 
ATOM   2508 C CA  . LYS B 2 72  ? 27.234 78.411 49.507 1.00 155.77 ?  227 LYS B CA  1 
ATOM   2509 C C   . LYS B 2 72  ? 27.725 79.330 48.381 1.00 159.58 ?  227 LYS B C   1 
ATOM   2510 O O   . LYS B 2 72  ? 26.909 80.022 47.772 1.00 158.86 ?  227 LYS B O   1 
ATOM   2511 C CB  . LYS B 2 72  ? 27.200 79.158 50.851 1.00 158.10 ?  227 LYS B CB  1 
ATOM   2512 N N   . GLN B 2 73  ? 29.047 79.310 48.089 1.00 156.52 ?  228 GLN B N   1 
ATOM   2513 C CA  . GLN B 2 73  ? 29.668 80.088 47.012 1.00 156.45 ?  228 GLN B CA  1 
ATOM   2514 C C   . GLN B 2 73  ? 29.129 79.613 45.665 1.00 160.66 ?  228 GLN B C   1 
ATOM   2515 O O   . GLN B 2 73  ? 28.817 80.438 44.806 1.00 160.22 ?  228 GLN B O   1 
ATOM   2516 C CB  . GLN B 2 73  ? 31.199 79.958 47.050 1.00 157.77 ?  228 GLN B CB  1 
ATOM   2517 N N   . GLN B 2 74  ? 28.989 78.279 45.506 1.00 157.56 ?  229 GLN B N   1 
ATOM   2518 C CA  . GLN B 2 74  ? 28.451 77.616 44.315 1.00 157.47 ?  229 GLN B CA  1 
ATOM   2519 C C   . GLN B 2 74  ? 26.946 77.882 44.179 1.00 161.24 ?  229 GLN B C   1 
ATOM   2520 O O   . GLN B 2 74  ? 26.440 77.967 43.055 1.00 160.91 ?  229 GLN B O   1 
ATOM   2521 C CB  . GLN B 2 74  ? 28.705 76.103 44.393 1.00 158.82 ?  229 GLN B CB  1 
ATOM   2522 N N   . PHE B 2 75  ? 26.238 77.992 45.329 1.00 157.36 ?  230 PHE B N   1 
ATOM   2523 C CA  . PHE B 2 75  ? 24.801 78.261 45.400 1.00 156.77 ?  230 PHE B CA  1 
ATOM   2524 C C   . PHE B 2 75  ? 24.497 79.647 44.827 1.00 160.13 ?  230 PHE B C   1 
ATOM   2525 O O   . PHE B 2 75  ? 23.649 79.773 43.940 1.00 159.89 ?  230 PHE B O   1 
ATOM   2526 C CB  . PHE B 2 75  ? 24.292 78.129 46.848 1.00 158.45 ?  230 PHE B CB  1 
ATOM   2527 N N   . ASP B 2 76  ? 25.240 80.672 45.297 1.00 156.02 ?  231 ASP B N   1 
ATOM   2528 C CA  . ASP B 2 76  ? 25.131 82.064 44.857 1.00 155.36 ?  231 ASP B CA  1 
ATOM   2529 C C   . ASP B 2 76  ? 25.518 82.189 43.389 1.00 157.90 ?  231 ASP B C   1 
ATOM   2530 O O   . ASP B 2 76  ? 24.909 82.973 42.664 1.00 157.24 ?  231 ASP B O   1 
ATOM   2531 C CB  . ASP B 2 76  ? 26.019 82.970 45.726 1.00 157.17 ?  231 ASP B CB  1 
ATOM   2532 N N   . GLN B 2 77  ? 26.509 81.387 42.952 1.00 153.68 ?  232 GLN B N   1 
ATOM   2533 C CA  . GLN B 2 77  ? 27.002 81.352 41.580 1.00 153.08 ?  232 GLN B CA  1 
ATOM   2534 C C   . GLN B 2 77  ? 25.984 80.711 40.642 1.00 155.75 ?  232 GLN B C   1 
ATOM   2535 O O   . GLN B 2 77  ? 25.761 81.249 39.557 1.00 155.35 ?  232 GLN B O   1 
ATOM   2536 C CB  . GLN B 2 77  ? 28.361 80.637 41.502 1.00 154.40 ?  232 GLN B CB  1 
ATOM   2537 N N   . GLU B 2 78  ? 25.347 79.588 41.061 1.00 151.21 ?  233 GLU B N   1 
ATOM   2538 C CA  . GLU B 2 78  ? 24.332 78.909 40.246 1.00 150.34 ?  233 GLU B CA  1 
ATOM   2539 C C   . GLU B 2 78  ? 23.163 79.863 39.958 1.00 152.94 ?  233 GLU B C   1 
ATOM   2540 O O   . GLU B 2 78  ? 22.806 80.030 38.792 1.00 152.56 ?  233 GLU B O   1 
ATOM   2541 C CB  . GLU B 2 78  ? 23.861 77.590 40.894 1.00 151.61 ?  233 GLU B CB  1 
ATOM   2542 N N   . ILE B 2 79  ? 22.646 80.563 40.999 1.00 148.41 ?  234 ILE B N   1 
ATOM   2543 C CA  . ILE B 2 79  ? 21.547 81.535 40.867 1.00 147.69 ?  234 ILE B CA  1 
ATOM   2544 C C   . ILE B 2 79  ? 21.949 82.739 39.994 1.00 151.07 ?  234 ILE B C   1 
ATOM   2545 O O   . ILE B 2 79  ? 21.180 83.127 39.110 1.00 150.35 ?  234 ILE B O   1 
ATOM   2546 C CB  . ILE B 2 79  ? 20.955 81.962 42.239 1.00 150.47 ?  234 ILE B CB  1 
ATOM   2547 C CG1 . ILE B 2 79  ? 20.466 80.735 43.034 1.00 150.72 ?  234 ILE B CG1 1 
ATOM   2548 C CG2 . ILE B 2 79  ? 19.813 82.978 42.058 1.00 150.89 ?  234 ILE B CG2 1 
ATOM   2549 C CD1 . ILE B 2 79  ? 20.283 80.956 44.530 1.00 157.01 ?  234 ILE B CD1 1 
ATOM   2550 N N   . LYS B 2 80  ? 23.157 83.305 40.236 1.00 147.44 ?  235 LYS B N   1 
ATOM   2551 C CA  . LYS B 2 80  ? 23.718 84.447 39.500 1.00 147.10 ?  235 LYS B CA  1 
ATOM   2552 C C   . LYS B 2 80  ? 23.817 84.185 37.998 1.00 149.90 ?  235 LYS B C   1 
ATOM   2553 O O   . LYS B 2 80  ? 23.478 85.071 37.214 1.00 149.51 ?  235 LYS B O   1 
ATOM   2554 C CB  . LYS B 2 80  ? 25.093 84.850 40.058 1.00 149.77 ?  235 LYS B CB  1 
ATOM   2555 N N   . VAL B 2 81  ? 24.265 82.975 37.599 1.00 145.36 ?  236 VAL B N   1 
ATOM   2556 C CA  . VAL B 2 81  ? 24.381 82.602 36.186 1.00 144.57 ?  236 VAL B CA  1 
ATOM   2557 C C   . VAL B 2 81  ? 23.001 82.315 35.595 1.00 147.21 ?  236 VAL B C   1 
ATOM   2558 O O   . VAL B 2 81  ? 22.747 82.668 34.446 1.00 146.60 ?  236 VAL B O   1 
ATOM   2559 C CB  . VAL B 2 81  ? 25.368 81.435 35.946 1.00 148.45 ?  236 VAL B CB  1 
ATOM   2560 N N   . MET B 2 82  ? 22.113 81.686 36.392 1.00 143.09 ?  237 MET B N   1 
ATOM   2561 C CA  . MET B 2 82  ? 20.743 81.323 36.024 1.00 142.66 ?  237 MET B CA  1 
ATOM   2562 C C   . MET B 2 82  ? 19.883 82.548 35.735 1.00 145.93 ?  237 MET B C   1 
ATOM   2563 O O   . MET B 2 82  ? 19.018 82.496 34.861 1.00 145.53 ?  237 MET B O   1 
ATOM   2564 C CB  . MET B 2 82  ? 20.102 80.498 37.145 1.00 144.97 ?  237 MET B CB  1 
ATOM   2565 N N   . ALA B 2 83  ? 20.116 83.642 36.478 1.00 141.74 ?  238 ALA B N   1 
ATOM   2566 C CA  . ALA B 2 83  ? 19.394 84.903 36.332 1.00 140.91 ?  238 ALA B CA  1 
ATOM   2567 C C   . ALA B 2 83  ? 19.748 85.606 35.019 1.00 142.62 ?  238 ALA B C   1 
ATOM   2568 O O   . ALA B 2 83  ? 18.870 86.198 34.385 1.00 141.96 ?  238 ALA B O   1 
ATOM   2569 C CB  . ALA B 2 83  ? 19.710 85.810 37.508 1.00 141.74 ?  238 ALA B CB  1 
ATOM   2570 N N   . LYS B 2 84  ? 21.031 85.528 34.611 1.00 137.56 ?  239 LYS B N   1 
ATOM   2571 C CA  . LYS B 2 84  ? 21.535 86.162 33.394 1.00 136.42 ?  239 LYS B CA  1 
ATOM   2572 C C   . LYS B 2 84  ? 21.488 85.256 32.161 1.00 137.39 ?  239 LYS B C   1 
ATOM   2573 O O   . LYS B 2 84  ? 21.352 85.770 31.047 1.00 136.97 ?  239 LYS B O   1 
ATOM   2574 C CB  . LYS B 2 84  ? 22.953 86.707 33.611 1.00 138.96 ?  239 LYS B CB  1 
ATOM   2575 N N   . CYS B 2 85  ? 21.616 83.924 32.347 1.00 131.32 ?  240 CYS B N   1 
ATOM   2576 C CA  . CYS B 2 85  ? 21.610 82.965 31.235 1.00 129.65 ?  240 CYS B CA  1 
ATOM   2577 C C   . CYS B 2 85  ? 20.348 82.080 31.167 1.00 129.44 ?  240 CYS B C   1 
ATOM   2578 O O   . CYS B 2 85  ? 20.253 81.063 31.861 1.00 129.30 ?  240 CYS B O   1 
ATOM   2579 C CB  . CYS B 2 85  ? 22.895 82.133 31.202 1.00 129.97 ?  240 CYS B CB  1 
ATOM   2580 S SG  . CYS B 2 85  ? 24.417 83.101 31.004 1.00 133.84 ?  240 CYS B SG  1 
ATOM   2581 N N   . GLN B 2 86  ? 19.385 82.483 30.321 1.00 122.13 ?  241 GLN B N   1 
ATOM   2582 C CA  . GLN B 2 86  ? 18.142 81.755 30.057 1.00 119.93 ?  241 GLN B CA  1 
ATOM   2583 C C   . GLN B 2 86  ? 18.146 81.494 28.565 1.00 118.70 ?  241 GLN B C   1 
ATOM   2584 O O   . GLN B 2 86  ? 18.333 82.433 27.782 1.00 118.50 ?  241 GLN B O   1 
ATOM   2585 C CB  . GLN B 2 86  ? 16.908 82.577 30.472 1.00 121.20 ?  241 GLN B CB  1 
ATOM   2586 N N   . HIS B 2 87  ? 18.023 80.212 28.171 1.00 110.66 ?  242 HIS B N   1 
ATOM   2587 C CA  . HIS B 2 87  ? 18.094 79.801 26.772 1.00 108.11 ?  242 HIS B CA  1 
ATOM   2588 C C   . HIS B 2 87  ? 17.454 78.436 26.578 1.00 107.74 ?  242 HIS B C   1 
ATOM   2589 O O   . HIS B 2 87  ? 17.375 77.649 27.522 1.00 106.98 ?  242 HIS B O   1 
ATOM   2590 C CB  . HIS B 2 87  ? 19.572 79.777 26.328 1.00 108.44 ?  242 HIS B CB  1 
ATOM   2591 C CG  . HIS B 2 87  ? 19.796 79.517 24.877 1.00 111.59 ?  242 HIS B CG  1 
ATOM   2592 N ND1 . HIS B 2 87  ? 20.050 78.243 24.410 1.00 113.24 ?  242 HIS B ND1 1 
ATOM   2593 C CD2 . HIS B 2 87  ? 19.835 80.380 23.839 1.00 113.34 ?  242 HIS B CD2 1 
ATOM   2594 C CE1 . HIS B 2 87  ? 20.222 78.368 23.106 1.00 112.63 ?  242 HIS B CE1 1 
ATOM   2595 N NE2 . HIS B 2 87  ? 20.104 79.637 22.717 1.00 113.05 ?  242 HIS B NE2 1 
ATOM   2596 N N   . GLU B 2 88  ? 17.013 78.163 25.335 1.00 101.82 ?  243 GLU B N   1 
ATOM   2597 C CA  . GLU B 2 88  ? 16.387 76.928 24.841 1.00 100.21 ?  243 GLU B CA  1 
ATOM   2598 C C   . GLU B 2 88  ? 17.241 75.670 25.156 1.00 99.45  ?  243 GLU B C   1 
ATOM   2599 O O   . GLU B 2 88  ? 16.682 74.588 25.381 1.00 99.34  ?  243 GLU B O   1 
ATOM   2600 C CB  . GLU B 2 88  ? 16.178 77.079 23.317 1.00 101.67 ?  243 GLU B CB  1 
ATOM   2601 C CG  . GLU B 2 88  ? 15.489 75.927 22.598 1.00 115.05 ?  243 GLU B CG  1 
ATOM   2602 C CD  . GLU B 2 88  ? 15.661 75.912 21.088 1.00 140.71 ?  243 GLU B CD  1 
ATOM   2603 O OE1 . GLU B 2 88  ? 16.533 76.649 20.568 1.00 138.04 ?  243 GLU B OE1 1 
ATOM   2604 O OE2 . GLU B 2 88  ? 14.936 75.138 20.422 1.00 135.31 -1 243 GLU B OE2 1 
ATOM   2605 N N   . ASN B 2 89  ? 18.584 75.820 25.154 1.00 90.86  ?  244 ASN B N   1 
ATOM   2606 C CA  . ASN B 2 89  ? 19.494 74.721 25.418 1.00 88.37  ?  244 ASN B CA  1 
ATOM   2607 C C   . ASN B 2 89  ? 20.199 74.790 26.764 1.00 89.36  ?  244 ASN B C   1 
ATOM   2608 O O   . ASN B 2 89  ? 21.304 74.268 26.918 1.00 88.22  ?  244 ASN B O   1 
ATOM   2609 C CB  . ASN B 2 89  ? 20.444 74.482 24.248 1.00 85.44  ?  244 ASN B CB  1 
ATOM   2610 C CG  . ASN B 2 89  ? 19.748 74.144 22.944 1.00 91.39  ?  244 ASN B CG  1 
ATOM   2611 O OD1 . ASN B 2 89  ? 19.885 74.857 21.951 1.00 82.80  ?  244 ASN B OD1 1 
ATOM   2612 N ND2 . ASN B 2 89  ? 19.005 73.043 22.899 1.00 79.37  ?  244 ASN B ND2 1 
ATOM   2613 N N   . LEU B 2 90  ? 19.532 75.398 27.756 1.00 84.85  ?  245 LEU B N   1 
ATOM   2614 C CA  . LEU B 2 90  ? 20.009 75.459 29.136 1.00 84.17  ?  245 LEU B CA  1 
ATOM   2615 C C   . LEU B 2 90  ? 18.841 75.121 30.045 1.00 87.17  ?  245 LEU B C   1 
ATOM   2616 O O   . LEU B 2 90  ? 17.704 75.475 29.725 1.00 85.82  ?  245 LEU B O   1 
ATOM   2617 C CB  . LEU B 2 90  ? 20.547 76.849 29.540 1.00 84.31  ?  245 LEU B CB  1 
ATOM   2618 C CG  . LEU B 2 90  ? 21.590 77.576 28.687 1.00 89.67  ?  245 LEU B CG  1 
ATOM   2619 C CD1 . LEU B 2 90  ? 21.920 78.910 29.312 1.00 89.86  ?  245 LEU B CD1 1 
ATOM   2620 C CD2 . LEU B 2 90  ? 22.882 76.787 28.550 1.00 94.14  ?  245 LEU B CD2 1 
ATOM   2621 N N   . VAL B 2 91  ? 19.120 74.488 31.198 1.00 85.05  ?  246 VAL B N   1 
ATOM   2622 C CA  . VAL B 2 91  ? 18.104 74.181 32.216 1.00 86.01  ?  246 VAL B CA  1 
ATOM   2623 C C   . VAL B 2 91  ? 17.521 75.488 32.755 1.00 90.10  ?  246 VAL B C   1 
ATOM   2624 O O   . VAL B 2 91  ? 18.156 76.546 32.646 1.00 89.58  ?  246 VAL B O   1 
ATOM   2625 C CB  . VAL B 2 91  ? 18.602 73.289 33.392 1.00 90.89  ?  246 VAL B CB  1 
ATOM   2626 C CG1 . VAL B 2 91  ? 18.771 71.835 32.969 1.00 90.76  ?  246 VAL B CG1 1 
ATOM   2627 C CG2 . VAL B 2 91  ? 19.869 73.850 34.043 1.00 91.07  ?  246 VAL B CG2 1 
ATOM   2628 N N   . GLU B 2 92  ? 16.325 75.401 33.345 1.00 86.45  ?  247 GLU B N   1 
ATOM   2629 C CA  . GLU B 2 92  ? 15.638 76.545 33.913 1.00 86.16  ?  247 GLU B CA  1 
ATOM   2630 C C   . GLU B 2 92  ? 15.457 76.354 35.419 1.00 90.53  ?  247 GLU B C   1 
ATOM   2631 O O   . GLU B 2 92  ? 14.934 75.317 35.859 1.00 89.86  ?  247 GLU B O   1 
ATOM   2632 C CB  . GLU B 2 92  ? 14.295 76.760 33.205 1.00 87.27  ?  247 GLU B CB  1 
ATOM   2633 N N   . LEU B 2 93  ? 15.915 77.359 36.204 1.00 86.69  ?  248 LEU B N   1 
ATOM   2634 C CA  . LEU B 2 93  ? 15.807 77.380 37.665 1.00 106.54 ?  248 LEU B CA  1 
ATOM   2635 C C   . LEU B 2 93  ? 14.624 78.252 38.101 1.00 119.80 ?  248 LEU B C   1 
ATOM   2636 O O   . LEU B 2 93  ? 13.466 77.863 37.956 1.00 75.14  ?  248 LEU B O   1 
ATOM   2637 C CB  . LEU B 2 93  ? 17.116 77.896 38.284 1.00 106.58 ?  248 LEU B CB  1 
ATOM   2638 C CG  . LEU B 2 93  ? 17.212 77.914 39.820 1.00 111.28 ?  248 LEU B CG  1 
ATOM   2639 C CD1 . LEU B 2 93  ? 17.283 76.501 40.401 1.00 111.19 ?  248 LEU B CD1 1 
ATOM   2640 C CD2 . LEU B 2 93  ? 18.411 78.720 40.271 1.00 113.62 ?  248 LEU B CD2 1 
ATOM   2641 N N   . ASP B 2 102 ? 21.625 73.525 54.906 1.00 113.32 ?  257 ASP B N   1 
ATOM   2642 C CA  . ASP B 2 102 ? 20.855 72.760 53.927 1.00 112.83 ?  257 ASP B CA  1 
ATOM   2643 C C   . ASP B 2 102 ? 20.353 73.674 52.784 1.00 115.50 ?  257 ASP B C   1 
ATOM   2644 O O   . ASP B 2 102 ? 19.363 74.392 52.932 1.00 114.74 ?  257 ASP B O   1 
ATOM   2645 C CB  . ASP B 2 102 ? 19.717 71.975 54.605 1.00 114.75 ?  257 ASP B CB  1 
ATOM   2646 N N   . LEU B 2 103 ? 21.083 73.662 51.659 1.00 111.57 ?  258 LEU B N   1 
ATOM   2647 C CA  . LEU B 2 103 ? 20.804 74.487 50.478 1.00 111.01 ?  258 LEU B CA  1 
ATOM   2648 C C   . LEU B 2 103 ? 20.184 73.678 49.341 1.00 114.05 ?  258 LEU B C   1 
ATOM   2649 O O   . LEU B 2 103 ? 20.755 72.667 48.912 1.00 113.90 ?  258 LEU B O   1 
ATOM   2650 C CB  . LEU B 2 103 ? 22.084 75.182 49.985 1.00 111.05 ?  258 LEU B CB  1 
ATOM   2651 C CG  . LEU B 2 103 ? 22.848 76.041 50.984 1.00 115.95 ?  258 LEU B CG  1 
ATOM   2652 C CD1 . LEU B 2 103 ? 24.272 76.252 50.519 1.00 116.27 ?  258 LEU B CD1 1 
ATOM   2653 C CD2 . LEU B 2 103 ? 22.162 77.377 51.214 1.00 118.47 ?  258 LEU B CD2 1 
ATOM   2654 N N   . CYS B 2 104 ? 19.035 74.154 48.831 1.00 109.17 ?  259 CYS B N   1 
ATOM   2655 C CA  . CYS B 2 104 ? 18.294 73.511 47.749 1.00 107.93 ?  259 CYS B CA  1 
ATOM   2656 C C   . CYS B 2 104 ? 18.065 74.417 46.543 1.00 110.28 ?  259 CYS B C   1 
ATOM   2657 O O   . CYS B 2 104 ? 17.885 75.626 46.705 1.00 110.48 ?  259 CYS B O   1 
ATOM   2658 C CB  . CYS B 2 104 ? 16.979 72.942 48.269 1.00 108.10 ?  259 CYS B CB  1 
ATOM   2659 S SG  . CYS B 2 104 ? 17.175 71.663 49.537 1.00 112.00 ?  259 CYS B SG  1 
ATOM   2660 N N   . LEU B 2 105 ? 18.047 73.819 45.337 1.00 104.64 ?  260 LEU B N   1 
ATOM   2661 C CA  . LEU B 2 105 ? 17.745 74.493 44.070 1.00 103.12 ?  260 LEU B CA  1 
ATOM   2662 C C   . LEU B 2 105 ? 16.617 73.720 43.381 1.00 103.78 ?  260 LEU B C   1 
ATOM   2663 O O   . LEU B 2 105 ? 16.662 72.488 43.321 1.00 103.40 ?  260 LEU B O   1 
ATOM   2664 C CB  . LEU B 2 105 ? 18.972 74.609 43.154 1.00 103.06 ?  260 LEU B CB  1 
ATOM   2665 C CG  . LEU B 2 105 ? 20.112 75.491 43.638 1.00 107.78 ?  260 LEU B CG  1 
ATOM   2666 C CD1 . LEU B 2 105 ? 21.424 75.011 43.092 1.00 108.06 ?  260 LEU B CD1 1 
ATOM   2667 C CD2 . LEU B 2 105 ? 19.910 76.923 43.219 1.00 110.05 ?  260 LEU B CD2 1 
ATOM   2668 N N   . VAL B 2 106 ? 15.592 74.464 42.903 1.00 97.57  ?  261 VAL B N   1 
ATOM   2669 C CA  . VAL B 2 106 ? 14.393 73.941 42.245 1.00 95.87  ?  261 VAL B CA  1 
ATOM   2670 C C   . VAL B 2 106 ? 14.418 74.174 40.732 1.00 96.18  ?  261 VAL B C   1 
ATOM   2671 O O   . VAL B 2 106 ? 14.123 75.277 40.254 1.00 96.07  ?  261 VAL B O   1 
ATOM   2672 C CB  . VAL B 2 106 ? 13.094 74.474 42.897 1.00 99.53  ?  261 VAL B CB  1 
ATOM   2673 N N   . TYR B 2 107 ? 14.773 73.112 39.983 1.00 88.81  ?  262 TYR B N   1 
ATOM   2674 C CA  . TYR B 2 107 ? 14.858 73.120 38.523 1.00 85.99  ?  262 TYR B CA  1 
ATOM   2675 C C   . TYR B 2 107 ? 13.653 72.424 37.879 1.00 86.65  ?  262 TYR B C   1 
ATOM   2676 O O   . TYR B 2 107 ? 12.989 71.602 38.531 1.00 84.79  ?  262 TYR B O   1 
ATOM   2677 C CB  . TYR B 2 107 ? 16.130 72.392 38.081 1.00 85.55  ?  262 TYR B CB  1 
ATOM   2678 C CG  . TYR B 2 107 ? 17.429 73.099 38.388 1.00 85.16  ?  262 TYR B CG  1 
ATOM   2679 C CD1 . TYR B 2 107 ? 17.986 73.999 37.484 1.00 86.50  ?  262 TYR B CD1 1 
ATOM   2680 C CD2 . TYR B 2 107 ? 18.172 72.771 39.521 1.00 85.45  ?  262 TYR B CD2 1 
ATOM   2681 C CE1 . TYR B 2 107 ? 19.218 74.603 37.728 1.00 87.00  ?  262 TYR B CE1 1 
ATOM   2682 C CE2 . TYR B 2 107 ? 19.408 73.365 39.774 1.00 86.01  ?  262 TYR B CE2 1 
ATOM   2683 C CZ  . TYR B 2 107 ? 19.925 74.288 38.879 1.00 93.62  ?  262 TYR B CZ  1 
ATOM   2684 O OH  . TYR B 2 107 ? 21.143 74.879 39.121 1.00 94.54  ?  262 TYR B OH  1 
ATOM   2685 N N   . VAL B 2 108 ? 13.411 72.721 36.576 1.00 82.03  ?  263 VAL B N   1 
ATOM   2686 C CA  . VAL B 2 108 ? 12.366 72.092 35.763 1.00 81.73  ?  263 VAL B CA  1 
ATOM   2687 C C   . VAL B 2 108 ? 12.715 70.587 35.613 1.00 85.01  ?  263 VAL B C   1 
ATOM   2688 O O   . VAL B 2 108 ? 13.875 70.249 35.353 1.00 84.28  ?  263 VAL B O   1 
ATOM   2689 C CB  . VAL B 2 108 ? 12.202 72.798 34.384 1.00 85.50  ?  263 VAL B CB  1 
ATOM   2690 C CG1 . VAL B 2 108 ? 11.167 72.087 33.515 1.00 85.23  ?  263 VAL B CG1 1 
ATOM   2691 C CG2 . VAL B 2 108 ? 11.822 74.258 34.557 1.00 85.29  ?  263 VAL B CG2 1 
ATOM   2692 N N   . TYR B 2 109 ? 11.720 69.705 35.845 1.00 80.86  ?  264 TYR B N   1 
ATOM   2693 C CA  . TYR B 2 109 ? 11.858 68.253 35.752 1.00 79.81  ?  264 TYR B CA  1 
ATOM   2694 C C   . TYR B 2 109 ? 12.089 67.825 34.308 1.00 83.25  ?  264 TYR B C   1 
ATOM   2695 O O   . TYR B 2 109 ? 11.257 68.109 33.433 1.00 82.95  ?  264 TYR B O   1 
ATOM   2696 C CB  . TYR B 2 109 ? 10.619 67.557 36.322 1.00 80.52  ?  264 TYR B CB  1 
ATOM   2697 C CG  . TYR B 2 109 ? 10.571 66.068 36.067 1.00 82.68  ?  264 TYR B CG  1 
ATOM   2698 C CD1 . TYR B 2 109 ? 9.732  65.533 35.095 1.00 84.81  ?  264 TYR B CD1 1 
ATOM   2699 C CD2 . TYR B 2 109 ? 11.330 65.185 36.827 1.00 83.35  ?  264 TYR B CD2 1 
ATOM   2700 C CE1 . TYR B 2 109 ? 9.671  64.159 34.869 1.00 85.08  ?  264 TYR B CE1 1 
ATOM   2701 C CE2 . TYR B 2 109 ? 11.276 63.810 36.607 1.00 84.19  ?  264 TYR B CE2 1 
ATOM   2702 C CZ  . TYR B 2 109 ? 10.440 63.299 35.630 1.00 90.06  ?  264 TYR B CZ  1 
ATOM   2703 O OH  . TYR B 2 109 ? 10.384 61.942 35.415 1.00 90.32  ?  264 TYR B OH  1 
ATOM   2704 N N   . MET B 2 110 ? 13.220 67.130 34.069 1.00 77.89  ?  265 MET B N   1 
ATOM   2705 C CA  . MET B 2 110 ? 13.605 66.623 32.750 1.00 76.08  ?  265 MET B CA  1 
ATOM   2706 C C   . MET B 2 110 ? 13.134 65.160 32.587 1.00 76.68  ?  265 MET B C   1 
ATOM   2707 O O   . MET B 2 110 ? 13.686 64.248 33.219 1.00 75.65  ?  265 MET B O   1 
ATOM   2708 C CB  . MET B 2 110 ? 15.107 66.803 32.505 1.00 78.09  ?  265 MET B CB  1 
ATOM   2709 C CG  . MET B 2 110 ? 15.551 68.248 32.507 1.00 81.45  ?  265 MET B CG  1 
ATOM   2710 S SD  . MET B 2 110 ? 14.882 69.156 31.107 1.00 85.91  ?  265 MET B SD  1 
ATOM   2711 C CE  . MET B 2 110 ? 16.316 69.486 30.203 1.00 82.40  ?  265 MET B CE  1 
ATOM   2712 N N   . PRO B 2 111 ? 12.065 64.935 31.782 1.00 70.69  ?  266 PRO B N   1 
ATOM   2713 C CA  . PRO B 2 111 ? 11.521 63.571 31.633 1.00 69.72  ?  266 PRO B CA  1 
ATOM   2714 C C   . PRO B 2 111 ? 12.495 62.535 31.065 1.00 68.75  ?  266 PRO B C   1 
ATOM   2715 O O   . PRO B 2 111 ? 12.334 61.341 31.321 1.00 66.95  ?  266 PRO B O   1 
ATOM   2716 C CB  . PRO B 2 111 ? 10.286 63.779 30.743 1.00 71.90  ?  266 PRO B CB  1 
ATOM   2717 C CG  . PRO B 2 111 ? 9.960  65.232 30.886 1.00 76.31  ?  266 PRO B CG  1 
ATOM   2718 C CD  . PRO B 2 111 ? 11.282 65.900 30.987 1.00 71.57  ?  266 PRO B CD  1 
ATOM   2719 N N   . ASN B 2 112 ? 13.513 62.984 30.319 1.00 63.14  ?  267 ASN B N   1 
ATOM   2720 C CA  . ASN B 2 112 ? 14.499 62.047 29.799 1.00 61.67  ?  267 ASN B CA  1 
ATOM   2721 C C   . ASN B 2 112 ? 15.856 62.038 30.518 1.00 61.96  ?  267 ASN B C   1 
ATOM   2722 O O   . ASN B 2 112 ? 16.803 61.484 29.984 1.00 61.01  ?  267 ASN B O   1 
ATOM   2723 C CB  . ASN B 2 112 ? 14.607 62.122 28.283 1.00 60.02  ?  267 ASN B CB  1 
ATOM   2724 C CG  . ASN B 2 112 ? 13.460 61.431 27.610 1.00 67.34  ?  267 ASN B CG  1 
ATOM   2725 O OD1 . ASN B 2 112 ? 13.179 60.253 27.869 1.00 63.98  ?  267 ASN B OD1 1 
ATOM   2726 N ND2 . ASN B 2 112 ? 12.741 62.164 26.781 1.00 54.74  ?  267 ASN B ND2 1 
ATOM   2727 N N   . GLY B 2 113 ? 15.914 62.595 31.733 1.00 56.52  ?  268 GLY B N   1 
ATOM   2728 C CA  . GLY B 2 113 ? 17.113 62.665 32.572 1.00 54.17  ?  268 GLY B CA  1 
ATOM   2729 C C   . GLY B 2 113 ? 18.341 63.209 31.877 1.00 54.07  ?  268 GLY B C   1 
ATOM   2730 O O   . GLY B 2 113 ? 18.254 64.165 31.096 1.00 52.55  ?  268 GLY B O   1 
ATOM   2731 N N   . SER B 2 114 ? 19.494 62.561 32.126 1.00 49.12  ?  269 SER B N   1 
ATOM   2732 C CA  . SER B 2 114 ? 20.772 62.948 31.516 1.00 47.20  ?  269 SER B CA  1 
ATOM   2733 C C   . SER B 2 114 ? 21.141 62.107 30.297 1.00 47.34  ?  269 SER B C   1 
ATOM   2734 O O   . SER B 2 114 ? 20.724 60.953 30.176 1.00 45.83  ?  269 SER B O   1 
ATOM   2735 C CB  . SER B 2 114 ? 21.897 62.906 32.546 1.00 49.90  ?  269 SER B CB  1 
ATOM   2736 O OG  . SER B 2 114 ? 22.066 61.615 33.106 1.00 59.01  ?  269 SER B OG  1 
ATOM   2737 N N   . LEU B 2 115 ? 21.962 62.694 29.409 1.00 43.14  ?  270 LEU B N   1 
ATOM   2738 C CA  . LEU B 2 115 ? 22.493 62.044 28.212 1.00 41.72  ?  270 LEU B CA  1 
ATOM   2739 C C   . LEU B 2 115 ? 23.282 60.801 28.639 1.00 49.96  ?  270 LEU B C   1 
ATOM   2740 O O   . LEU B 2 115 ? 23.098 59.734 28.045 1.00 50.48  ?  270 LEU B O   1 
ATOM   2741 C CB  . LEU B 2 115 ? 23.384 63.031 27.433 1.00 40.13  ?  270 LEU B CB  1 
ATOM   2742 C CG  . LEU B 2 115 ? 24.097 62.556 26.169 1.00 42.47  ?  270 LEU B CG  1 
ATOM   2743 C CD1 . LEU B 2 115 ? 23.128 61.938 25.175 1.00 42.12  ?  270 LEU B CD1 1 
ATOM   2744 C CD2 . LEU B 2 115 ? 24.832 63.711 25.512 1.00 42.15  ?  270 LEU B CD2 1 
ATOM   2745 N N   . LEU B 2 116 ? 24.105 60.925 29.712 1.00 47.06  ?  271 LEU B N   1 
ATOM   2746 C CA  . LEU B 2 116 ? 24.880 59.818 30.264 1.00 46.60  ?  271 LEU B CA  1 
ATOM   2747 C C   . LEU B 2 116 ? 23.958 58.639 30.589 1.00 52.73  ?  271 LEU B C   1 
ATOM   2748 O O   . LEU B 2 116 ? 24.239 57.517 30.168 1.00 54.16  ?  271 LEU B O   1 
ATOM   2749 C CB  . LEU B 2 116 ? 25.653 60.260 31.523 1.00 46.08  ?  271 LEU B CB  1 
ATOM   2750 C CG  . LEU B 2 116 ? 26.609 59.212 32.118 1.00 49.22  ?  271 LEU B CG  1 
ATOM   2751 C CD1 . LEU B 2 116 ? 28.003 59.345 31.545 1.00 48.61  ?  271 LEU B CD1 1 
ATOM   2752 C CD2 . LEU B 2 116 ? 26.649 59.286 33.616 1.00 49.84  ?  271 LEU B CD2 1 
ATOM   2753 N N   . ASP B 2 117 ? 22.836 58.898 31.279 1.00 49.88  ?  272 ASP B N   1 
ATOM   2754 C CA  . ASP B 2 117 ? 21.897 57.842 31.651 1.00 50.85  ?  272 ASP B CA  1 
ATOM   2755 C C   . ASP B 2 117 ? 21.135 57.235 30.466 1.00 53.22  ?  272 ASP B C   1 
ATOM   2756 O O   . ASP B 2 117 ? 20.868 56.031 30.476 1.00 53.40  ?  272 ASP B O   1 
ATOM   2757 C CB  . ASP B 2 117 ? 20.987 58.274 32.807 1.00 53.61  ?  272 ASP B CB  1 
ATOM   2758 C CG  . ASP B 2 117 ? 21.726 58.561 34.120 1.00 72.75  ?  272 ASP B CG  1 
ATOM   2759 O OD1 . ASP B 2 117 ? 22.962 58.306 34.184 1.00 73.42  ?  272 ASP B OD1 1 
ATOM   2760 O OD2 . ASP B 2 117 ? 21.062 59.017 35.097 1.00 80.44  -1 272 ASP B OD2 1 
ATOM   2761 N N   . ARG B 2 118 ? 20.853 58.042 29.423 1.00 46.14  ?  273 ARG B N   1 
ATOM   2762 C CA  . ARG B 2 118 ? 20.181 57.551 28.231 1.00 43.87  ?  273 ARG B CA  1 
ATOM   2763 C C   . ARG B 2 118 ? 21.103 56.762 27.329 1.00 46.85  ?  273 ARG B C   1 
ATOM   2764 O O   . ARG B 2 118 ? 20.648 55.790 26.725 1.00 47.05  ?  273 ARG B O   1 
ATOM   2765 C CB  . ARG B 2 118 ? 19.452 58.654 27.467 1.00 42.96  ?  273 ARG B CB  1 
ATOM   2766 C CG  . ARG B 2 118 ? 18.317 59.341 28.244 1.00 44.20  ?  273 ARG B CG  1 
ATOM   2767 C CD  . ARG B 2 118 ? 17.130 58.486 28.635 1.00 43.46  ?  273 ARG B CD  1 
ATOM   2768 N NE  . ARG B 2 118 ? 17.397 57.525 29.717 1.00 50.44  ?  273 ARG B NE  1 
ATOM   2769 C CZ  . ARG B 2 118 ? 17.509 57.832 31.008 1.00 58.76  ?  273 ARG B CZ  1 
ATOM   2770 N NH1 . ARG B 2 118 ? 17.438 59.093 31.407 1.00 51.75  ?  273 ARG B NH1 1 
ATOM   2771 N NH2 . ARG B 2 118 ? 17.723 56.879 31.907 1.00 40.56  1  273 ARG B NH2 1 
ATOM   2772 N N   . LEU B 2 119 ? 22.400 57.125 27.265 1.00 42.17  ?  274 LEU B N   1 
ATOM   2773 C CA  . LEU B 2 119 ? 23.378 56.365 26.472 1.00 41.48  ?  274 LEU B CA  1 
ATOM   2774 C C   . LEU B 2 119 ? 23.647 54.969 27.090 1.00 44.36  ?  274 LEU B C   1 
ATOM   2775 O O   . LEU B 2 119 ? 23.987 54.018 26.370 1.00 41.41  ?  274 LEU B O   1 
ATOM   2776 C CB  . LEU B 2 119 ? 24.676 57.150 26.259 1.00 41.62  ?  274 LEU B CB  1 
ATOM   2777 C CG  . LEU B 2 119 ? 24.604 58.420 25.380 1.00 45.68  ?  274 LEU B CG  1 
ATOM   2778 C CD1 . LEU B 2 119 ? 25.893 59.202 25.474 1.00 45.41  ?  274 LEU B CD1 1 
ATOM   2779 C CD2 . LEU B 2 119 ? 24.345 58.090 23.920 1.00 45.97  ?  274 LEU B CD2 1 
ATOM   2780 N N   . SER B 2 120 ? 23.429 54.834 28.409 1.00 43.57  ?  275 SER B N   1 
ATOM   2781 C CA  . SER B 2 120 ? 23.609 53.553 29.091 1.00 43.86  ?  275 SER B CA  1 
ATOM   2782 C C   . SER B 2 120 ? 22.280 52.847 29.274 1.00 48.99  ?  275 SER B C   1 
ATOM   2783 O O   . SER B 2 120 ? 22.256 51.752 29.827 1.00 49.63  ?  275 SER B O   1 
ATOM   2784 C CB  . SER B 2 120 ? 24.333 53.738 30.421 1.00 48.66  ?  275 SER B CB  1 
ATOM   2785 O OG  . SER B 2 120 ? 23.589 54.573 31.297 1.00 65.25  ?  275 SER B OG  1 
ATOM   2786 N N   . CYS B 2 121 ? 21.168 53.464 28.800 1.00 47.01  ?  276 CYS B N   1 
ATOM   2787 C CA  . CYS B 2 121 ? 19.809 52.913 28.871 1.00 48.15  ?  276 CYS B CA  1 
ATOM   2788 C C   . CYS B 2 121 ? 19.395 52.629 30.300 1.00 53.44  ?  276 CYS B C   1 
ATOM   2789 O O   . CYS B 2 121 ? 18.708 51.642 30.561 1.00 53.87  ?  276 CYS B O   1 
ATOM   2790 C CB  . CYS B 2 121 ? 19.664 51.675 27.986 1.00 49.21  ?  276 CYS B CB  1 
ATOM   2791 S SG  . CYS B 2 121 ? 19.988 51.979 26.233 1.00 53.72  ?  276 CYS B SG  1 
ATOM   2792 N N   . LEU B 2 122 ? 19.812 53.502 31.229 1.00 50.36  ?  277 LEU B N   1 
ATOM   2793 C CA  . LEU B 2 122 ? 19.490 53.376 32.642 1.00 49.92  ?  277 LEU B CA  1 
ATOM   2794 C C   . LEU B 2 122 ? 17.987 53.349 32.833 1.00 55.14  ?  277 LEU B C   1 
ATOM   2795 O O   . LEU B 2 122 ? 17.269 54.146 32.216 1.00 54.64  ?  277 LEU B O   1 
ATOM   2796 C CB  . LEU B 2 122 ? 20.141 54.507 33.456 1.00 49.74  ?  277 LEU B CB  1 
ATOM   2797 C CG  . LEU B 2 122 ? 20.037 54.416 35.000 1.00 52.73  ?  277 LEU B CG  1 
ATOM   2798 C CD1 . LEU B 2 122 ? 20.709 53.187 35.552 1.00 51.96  ?  277 LEU B CD1 1 
ATOM   2799 C CD2 . LEU B 2 122 ? 20.625 55.621 35.636 1.00 54.81  ?  277 LEU B CD2 1 
ATOM   2800 N N   . ASP B 2 123 ? 17.521 52.358 33.616 1.00 52.16  ?  278 ASP B N   1 
ATOM   2801 C CA  . ASP B 2 123 ? 16.114 52.123 33.953 1.00 52.81  ?  278 ASP B CA  1 
ATOM   2802 C C   . ASP B 2 123 ? 15.210 51.642 32.809 1.00 58.84  ?  278 ASP B C   1 
ATOM   2803 O O   . ASP B 2 123 ? 13.996 51.897 32.831 1.00 59.75  ?  278 ASP B O   1 
ATOM   2804 C CB  . ASP B 2 123 ? 15.511 53.315 34.717 1.00 55.19  ?  278 ASP B CB  1 
ATOM   2805 C CG  . ASP B 2 123 ? 16.314 53.728 35.941 1.00 67.45  ?  278 ASP B CG  1 
ATOM   2806 O OD1 . ASP B 2 123 ? 16.606 54.937 36.077 1.00 68.27  ?  278 ASP B OD1 1 
ATOM   2807 O OD2 . ASP B 2 123 ? 16.679 52.835 36.748 1.00 71.45  -1 278 ASP B OD2 1 
ATOM   2808 N N   . GLY B 2 124 ? 15.796 50.910 31.850 1.00 54.25  ?  279 GLY B N   1 
ATOM   2809 C CA  . GLY B 2 124 ? 15.083 50.325 30.719 1.00 52.82  ?  279 GLY B CA  1 
ATOM   2810 C C   . GLY B 2 124 ? 14.690 51.273 29.610 1.00 55.48  ?  279 GLY B C   1 
ATOM   2811 O O   . GLY B 2 124 ? 13.859 50.928 28.769 1.00 56.28  ?  279 GLY B O   1 
ATOM   2812 N N   . THR B 2 125 ? 15.287 52.450 29.558 1.00 50.83  ?  280 THR B N   1 
ATOM   2813 C CA  . THR B 2 125 ? 14.951 53.369 28.471 1.00 50.34  ?  280 THR B CA  1 
ATOM   2814 C C   . THR B 2 125 ? 15.484 52.846 27.128 1.00 53.06  ?  280 THR B C   1 
ATOM   2815 O O   . THR B 2 125 ? 16.611 52.371 27.079 1.00 53.28  ?  280 THR B O   1 
ATOM   2816 C CB  . THR B 2 125 ? 15.346 54.840 28.792 1.00 54.25  ?  280 THR B CB  1 
ATOM   2817 O OG1 . THR B 2 125 ? 16.738 54.943 29.142 1.00 49.98  ?  280 THR B OG1 1 
ATOM   2818 C CG2 . THR B 2 125 ? 14.480 55.445 29.875 1.00 47.19  ?  280 THR B CG2 1 
ATOM   2819 N N   . PRO B 2 126 ? 14.695 52.867 26.037 1.00 49.25  ?  281 PRO B N   1 
ATOM   2820 C CA  . PRO B 2 126 ? 15.218 52.377 24.749 1.00 48.46  ?  281 PRO B CA  1 
ATOM   2821 C C   . PRO B 2 126 ? 16.458 53.143 24.279 1.00 51.27  ?  281 PRO B C   1 
ATOM   2822 O O   . PRO B 2 126 ? 16.559 54.323 24.596 1.00 51.39  ?  281 PRO B O   1 
ATOM   2823 C CB  . PRO B 2 126 ? 14.034 52.583 23.789 1.00 49.48  ?  281 PRO B CB  1 
ATOM   2824 C CG  . PRO B 2 126 ? 13.211 53.619 24.413 1.00 53.23  ?  281 PRO B CG  1 
ATOM   2825 C CD  . PRO B 2 126 ? 13.313 53.363 25.885 1.00 49.77  ?  281 PRO B CD  1 
ATOM   2826 N N   . PRO B 2 127 ? 17.406 52.528 23.532 1.00 47.80  ?  282 PRO B N   1 
ATOM   2827 C CA  . PRO B 2 127 ? 18.583 53.295 23.076 1.00 47.35  ?  282 PRO B CA  1 
ATOM   2828 C C   . PRO B 2 127 ? 18.211 54.511 22.216 1.00 50.22  ?  282 PRO B C   1 
ATOM   2829 O O   . PRO B 2 127 ? 17.216 54.459 21.507 1.00 50.12  ?  282 PRO B O   1 
ATOM   2830 C CB  . PRO B 2 127 ? 19.400 52.271 22.271 1.00 48.54  ?  282 PRO B CB  1 
ATOM   2831 C CG  . PRO B 2 127 ? 18.896 50.944 22.661 1.00 52.94  ?  282 PRO B CG  1 
ATOM   2832 C CD  . PRO B 2 127 ? 17.458 51.130 23.047 1.00 49.01  ?  282 PRO B CD  1 
ATOM   2833 N N   . LEU B 2 128 ? 18.997 55.594 22.296 1.00 46.02  ?  283 LEU B N   1 
ATOM   2834 C CA  . LEU B 2 128 ? 18.796 56.800 21.490 1.00 45.76  ?  283 LEU B CA  1 
ATOM   2835 C C   . LEU B 2 128 ? 19.205 56.530 20.055 1.00 50.22  ?  283 LEU B C   1 
ATOM   2836 O O   . LEU B 2 128 ? 20.311 56.063 19.799 1.00 47.69  ?  283 LEU B O   1 
ATOM   2837 C CB  . LEU B 2 128 ? 19.611 58.017 21.997 1.00 45.34  ?  283 LEU B CB  1 
ATOM   2838 C CG  . LEU B 2 128 ? 19.546 58.398 23.477 1.00 49.27  ?  283 LEU B CG  1 
ATOM   2839 C CD1 . LEU B 2 128 ? 20.630 59.380 23.810 1.00 48.80  ?  283 LEU B CD1 1 
ATOM   2840 C CD2 . LEU B 2 128 ? 18.165 58.942 23.865 1.00 49.99  ?  283 LEU B CD2 1 
ATOM   2841 N N   . SER B 2 129 ? 18.332 56.868 19.117 1.00 50.02  ?  284 SER B N   1 
ATOM   2842 C CA  . SER B 2 129 ? 18.623 56.716 17.696 1.00 50.26  ?  284 SER B CA  1 
ATOM   2843 C C   . SER B 2 129 ? 19.764 57.651 17.332 1.00 54.76  ?  284 SER B C   1 
ATOM   2844 O O   . SER B 2 129 ? 20.034 58.598 18.055 1.00 53.25  ?  284 SER B O   1 
ATOM   2845 C CB  . SER B 2 129 ? 17.388 57.085 16.880 1.00 52.78  ?  284 SER B CB  1 
ATOM   2846 O OG  . SER B 2 129 ? 16.970 58.406 17.185 1.00 59.74  ?  284 SER B OG  1 
ATOM   2847 N N   . TRP B 2 130 ? 20.409 57.407 16.206 1.00 54.75  ?  285 TRP B N   1 
ATOM   2848 C CA  . TRP B 2 130 ? 21.460 58.277 15.704 1.00 56.01  ?  285 TRP B CA  1 
ATOM   2849 C C   . TRP B 2 130 ? 20.854 59.643 15.336 1.00 65.60  ?  285 TRP B C   1 
ATOM   2850 O O   . TRP B 2 130 ? 21.511 60.679 15.499 1.00 66.92  ?  285 TRP B O   1 
ATOM   2851 C CB  . TRP B 2 130 ? 22.153 57.650 14.496 1.00 54.64  ?  285 TRP B CB  1 
ATOM   2852 C CG  . TRP B 2 130 ? 23.154 58.554 13.847 1.00 56.10  ?  285 TRP B CG  1 
ATOM   2853 C CD1 . TRP B 2 130 ? 23.014 59.195 12.655 1.00 59.05  ?  285 TRP B CD1 1 
ATOM   2854 C CD2 . TRP B 2 130 ? 24.402 59.005 14.402 1.00 56.06  ?  285 TRP B CD2 1 
ATOM   2855 N NE1 . TRP B 2 130 ? 24.119 59.973 12.402 1.00 58.66  ?  285 TRP B NE1 1 
ATOM   2856 C CE2 . TRP B 2 130 ? 24.996 59.862 13.448 1.00 60.14  ?  285 TRP B CE2 1 
ATOM   2857 C CE3 . TRP B 2 130 ? 25.082 58.755 15.606 1.00 57.00  ?  285 TRP B CE3 1 
ATOM   2858 C CZ2 . TRP B 2 130 ? 26.220 60.503 13.675 1.00 59.36  ?  285 TRP B CZ2 1 
ATOM   2859 C CZ3 . TRP B 2 130 ? 26.302 59.373 15.822 1.00 58.82  ?  285 TRP B CZ3 1 
ATOM   2860 C CH2 . TRP B 2 130 ? 26.875 60.210 14.850 1.00 59.70  ?  285 TRP B CH2 1 
ATOM   2861 N N   . HIS B 2 131 ? 19.582 59.642 14.896 1.00 63.11  ?  286 HIS B N   1 
ATOM   2862 C CA  . HIS B 2 131 ? 18.843 60.849 14.566 1.00 64.28  ?  286 HIS B CA  1 
ATOM   2863 C C   . HIS B 2 131 ? 18.739 61.775 15.793 1.00 66.88  ?  286 HIS B C   1 
ATOM   2864 O O   . HIS B 2 131 ? 19.004 62.964 15.659 1.00 65.79  ?  286 HIS B O   1 
ATOM   2865 C CB  . HIS B 2 131 ? 17.467 60.469 13.969 1.00 66.51  ?  286 HIS B CB  1 
ATOM   2866 C CG  . HIS B 2 131 ? 16.415 61.530 14.010 1.00 71.02  ?  286 HIS B CG  1 
ATOM   2867 N ND1 . HIS B 2 131 ? 16.544 62.724 13.316 1.00 73.62  ?  286 HIS B ND1 1 
ATOM   2868 C CD2 . HIS B 2 131 ? 15.258 61.546 14.701 1.00 73.65  ?  286 HIS B CD2 1 
ATOM   2869 C CE1 . HIS B 2 131 ? 15.461 63.427 13.619 1.00 73.50  ?  286 HIS B CE1 1 
ATOM   2870 N NE2 . HIS B 2 131 ? 14.648 62.750 14.429 1.00 73.79  ?  286 HIS B NE2 1 
ATOM   2871 N N   . MET B 2 132 ? 18.363 61.227 16.978 1.00 63.02  ?  287 MET B N   1 
ATOM   2872 C CA  . MET B 2 132 ? 18.249 62.004 18.211 1.00 62.92  ?  287 MET B CA  1 
ATOM   2873 C C   . MET B 2 132 ? 19.619 62.442 18.723 1.00 63.56  ?  287 MET B C   1 
ATOM   2874 O O   . MET B 2 132 ? 19.764 63.564 19.220 1.00 64.32  ?  287 MET B O   1 
ATOM   2875 C CB  . MET B 2 132 ? 17.476 61.255 19.297 1.00 66.53  ?  287 MET B CB  1 
ATOM   2876 C CG  . MET B 2 132 ? 16.024 60.941 18.970 1.00 72.73  ?  287 MET B CG  1 
ATOM   2877 S SD  . MET B 2 132 ? 14.785 62.264 19.130 1.00 79.73  ?  287 MET B SD  1 
ATOM   2878 C CE  . MET B 2 132 ? 15.111 63.322 17.706 1.00 76.43  ?  287 MET B CE  1 
ATOM   2879 N N   . ARG B 2 133 ? 20.630 61.585 18.542 1.00 55.27  ?  288 ARG B N   1 
ATOM   2880 C CA  . ARG B 2 133 ? 22.009 61.840 18.924 1.00 53.57  ?  288 ARG B CA  1 
ATOM   2881 C C   . ARG B 2 133 ? 22.582 63.081 18.227 1.00 55.79  ?  288 ARG B C   1 
ATOM   2882 O O   . ARG B 2 133 ? 23.222 63.907 18.881 1.00 54.63  ?  288 ARG B O   1 
ATOM   2883 C CB  . ARG B 2 133 ? 22.856 60.588 18.685 1.00 50.88  ?  288 ARG B CB  1 
ATOM   2884 C CG  . ARG B 2 133 ? 22.613 59.542 19.757 1.00 51.08  ?  288 ARG B CG  1 
ATOM   2885 C CD  . ARG B 2 133 ? 23.565 58.374 19.695 1.00 44.62  ?  288 ARG B CD  1 
ATOM   2886 N NE  . ARG B 2 133 ? 22.892 57.137 20.110 1.00 49.44  ?  288 ARG B NE  1 
ATOM   2887 C CZ  . ARG B 2 133 ? 23.503 56.071 20.624 1.00 59.80  ?  288 ARG B CZ  1 
ATOM   2888 N NH1 . ARG B 2 133 ? 24.814 56.085 20.842 1.00 41.09  ?  288 ARG B NH1 1 
ATOM   2889 N NH2 . ARG B 2 133 ? 22.804 54.992 20.947 1.00 42.06  1  288 ARG B NH2 1 
ATOM   2890 N N   . CYS B 2 134 ? 22.271 63.254 16.929 1.00 52.05  ?  289 CYS B N   1 
ATOM   2891 C CA  . CYS B 2 134 ? 22.678 64.433 16.150 1.00 51.19  ?  289 CYS B CA  1 
ATOM   2892 C C   . CYS B 2 134 ? 21.937 65.671 16.622 1.00 56.60  ?  289 CYS B C   1 
ATOM   2893 O O   . CYS B 2 134 ? 22.530 66.745 16.669 1.00 55.42  ?  289 CYS B O   1 
ATOM   2894 C CB  . CYS B 2 134 ? 22.476 64.200 14.659 1.00 50.55  ?  289 CYS B CB  1 
ATOM   2895 S SG  . CYS B 2 134 ? 23.431 62.812 13.998 1.00 53.80  ?  289 CYS B SG  1 
ATOM   2896 N N   . LYS B 2 135 ? 20.647 65.519 16.985 1.00 56.56  ?  290 LYS B N   1 
ATOM   2897 C CA  . LYS B 2 135 ? 19.828 66.617 17.511 1.00 58.23  ?  290 LYS B CA  1 
ATOM   2898 C C   . LYS B 2 135 ? 20.431 67.097 18.859 1.00 62.53  ?  290 LYS B C   1 
ATOM   2899 O O   . LYS B 2 135 ? 20.543 68.304 19.088 1.00 61.72  ?  290 LYS B O   1 
ATOM   2900 C CB  . LYS B 2 135 ? 18.347 66.196 17.695 1.00 61.03  ?  290 LYS B CB  1 
ATOM   2901 C CG  . LYS B 2 135 ? 17.483 67.314 18.305 1.00 74.75  ?  290 LYS B CG  1 
ATOM   2902 C CD  . LYS B 2 135 ? 16.167 66.867 18.943 1.00 84.52  ?  290 LYS B CD  1 
ATOM   2903 C CE  . LYS B 2 135 ? 15.341 68.099 19.238 1.00 95.66  ?  290 LYS B CE  1 
ATOM   2904 N NZ  . LYS B 2 135 ? 13.982 67.781 19.749 1.00 104.65 1  290 LYS B NZ  1 
ATOM   2905 N N   . ILE B 2 136 ? 20.809 66.134 19.729 1.00 58.22  ?  291 ILE B N   1 
ATOM   2906 C CA  . ILE B 2 136 ? 21.401 66.394 21.039 1.00 56.86  ?  291 ILE B CA  1 
ATOM   2907 C C   . ILE B 2 136 ? 22.728 67.127 20.872 1.00 60.40  ?  291 ILE B C   1 
ATOM   2908 O O   . ILE B 2 136 ? 22.890 68.212 21.430 1.00 61.04  ?  291 ILE B O   1 
ATOM   2909 C CB  . ILE B 2 136 ? 21.497 65.098 21.890 1.00 58.80  ?  291 ILE B CB  1 
ATOM   2910 C CG1 . ILE B 2 136 ? 20.092 64.659 22.321 1.00 58.18  ?  291 ILE B CG1 1 
ATOM   2911 C CG2 . ILE B 2 136 ? 22.401 65.312 23.116 1.00 59.42  ?  291 ILE B CG2 1 
ATOM   2912 C CD1 . ILE B 2 136 ? 19.915 63.211 22.561 1.00 67.29  ?  291 ILE B CD1 1 
ATOM   2913 N N   . ALA B 2 137 ? 23.636 66.576 20.057 1.00 54.98  ?  292 ALA B N   1 
ATOM   2914 C CA  . ALA B 2 137 ? 24.923 67.193 19.778 1.00 54.54  ?  292 ALA B CA  1 
ATOM   2915 C C   . ALA B 2 137 ? 24.773 68.657 19.350 1.00 60.27  ?  292 ALA B C   1 
ATOM   2916 O O   . ALA B 2 137 ? 25.520 69.501 19.842 1.00 60.74  ?  292 ALA B O   1 
ATOM   2917 C CB  . ALA B 2 137 ? 25.667 66.401 18.713 1.00 55.03  ?  292 ALA B CB  1 
ATOM   2918 N N   . GLN B 2 138 ? 23.774 68.961 18.481 1.00 57.72  ?  293 GLN B N   1 
ATOM   2919 C CA  . GLN B 2 138 ? 23.492 70.309 17.978 1.00 57.17  ?  293 GLN B CA  1 
ATOM   2920 C C   . GLN B 2 138 ? 23.038 71.215 19.106 1.00 60.20  ?  293 GLN B C   1 
ATOM   2921 O O   . GLN B 2 138 ? 23.641 72.261 19.331 1.00 60.10  ?  293 GLN B O   1 
ATOM   2922 C CB  . GLN B 2 138 ? 22.460 70.274 16.834 1.00 58.50  ?  293 GLN B CB  1 
ATOM   2923 C CG  . GLN B 2 138 ? 23.080 69.993 15.463 1.00 72.43  ?  293 GLN B CG  1 
ATOM   2924 C CD  . GLN B 2 138 ? 22.132 69.404 14.423 1.00 93.12  ?  293 GLN B CD  1 
ATOM   2925 O OE1 . GLN B 2 138 ? 20.893 69.472 14.518 1.00 90.46  ?  293 GLN B OE1 1 
ATOM   2926 N NE2 . GLN B 2 138 ? 22.711 68.826 13.379 1.00 78.31  ?  293 GLN B NE2 1 
ATOM   2927 N N   . GLY B 2 139 ? 22.022 70.776 19.828 1.00 57.34  ?  294 GLY B N   1 
ATOM   2928 C CA  . GLY B 2 139 ? 21.460 71.497 20.957 1.00 58.52  ?  294 GLY B CA  1 
ATOM   2929 C C   . GLY B 2 139 ? 22.478 71.780 22.036 1.00 65.58  ?  294 GLY B C   1 
ATOM   2930 O O   . GLY B 2 139 ? 22.559 72.909 22.514 1.00 66.51  ?  294 GLY B O   1 
ATOM   2931 N N   . ALA B 2 140 ? 23.291 70.770 22.391 1.00 62.71  ?  295 ALA B N   1 
ATOM   2932 C CA  . ALA B 2 140 ? 24.342 70.919 23.388 1.00 62.27  ?  295 ALA B CA  1 
ATOM   2933 C C   . ALA B 2 140 ? 25.364 71.974 22.926 1.00 66.15  ?  295 ALA B C   1 
ATOM   2934 O O   . ALA B 2 140 ? 25.713 72.852 23.708 1.00 64.57  ?  295 ALA B O   1 
ATOM   2935 C CB  . ALA B 2 140 ? 25.014 69.584 23.653 1.00 62.89  ?  295 ALA B CB  1 
ATOM   2936 N N   . ALA B 2 141 ? 25.762 71.945 21.640 1.00 64.34  ?  296 ALA B N   1 
ATOM   2937 C CA  . ALA B 2 141 ? 26.686 72.930 21.067 1.00 65.23  ?  296 ALA B CA  1 
ATOM   2938 C C   . ALA B 2 141 ? 26.112 74.363 21.100 1.00 72.45  ?  296 ALA B C   1 
ATOM   2939 O O   . ALA B 2 141 ? 26.861 75.301 21.389 1.00 73.01  ?  296 ALA B O   1 
ATOM   2940 C CB  . ALA B 2 141 ? 27.067 72.540 19.650 1.00 65.72  ?  296 ALA B CB  1 
ATOM   2941 N N   . ASN B 2 142 ? 24.791 74.522 20.848 1.00 69.26  ?  297 ASN B N   1 
ATOM   2942 C CA  . ASN B 2 142 ? 24.106 75.821 20.872 1.00 69.49  ?  297 ASN B CA  1 
ATOM   2943 C C   . ASN B 2 142 ? 24.092 76.447 22.268 1.00 73.91  ?  297 ASN B C   1 
ATOM   2944 O O   . ASN B 2 142 ? 24.233 77.664 22.391 1.00 73.23  ?  297 ASN B O   1 
ATOM   2945 C CB  . ASN B 2 142 ? 22.671 75.713 20.323 1.00 70.61  ?  297 ASN B CB  1 
ATOM   2946 C CG  . ASN B 2 142 ? 22.557 75.301 18.873 1.00 98.71  ?  297 ASN B CG  1 
ATOM   2947 O OD1 . ASN B 2 142 ? 23.544 75.167 18.135 1.00 91.10  ?  297 ASN B OD1 1 
ATOM   2948 N ND2 . ASN B 2 142 ? 21.332 75.070 18.433 1.00 93.96  ?  297 ASN B ND2 1 
ATOM   2949 N N   . GLY B 2 143 ? 23.914 75.606 23.288 1.00 70.97  ?  298 GLY B N   1 
ATOM   2950 C CA  . GLY B 2 143 ? 23.913 76.001 24.690 1.00 70.95  ?  298 GLY B CA  1 
ATOM   2951 C C   . GLY B 2 143 ? 25.273 76.530 25.110 1.00 76.12  ?  298 GLY B C   1 
ATOM   2952 O O   . GLY B 2 143 ? 25.350 77.527 25.836 1.00 76.29  ?  298 GLY B O   1 
ATOM   2953 N N   . ILE B 2 144 ? 26.361 75.882 24.625 1.00 72.62  ?  299 ILE B N   1 
ATOM   2954 C CA  . ILE B 2 144 ? 27.744 76.293 24.905 1.00 72.51  ?  299 ILE B CA  1 
ATOM   2955 C C   . ILE B 2 144 ? 28.023 77.625 24.192 1.00 78.42  ?  299 ILE B C   1 
ATOM   2956 O O   . ILE B 2 144 ? 28.683 78.496 24.766 1.00 78.16  ?  299 ILE B O   1 
ATOM   2957 C CB  . ILE B 2 144 ? 28.805 75.181 24.600 1.00 75.14  ?  299 ILE B CB  1 
ATOM   2958 C CG1 . ILE B 2 144 ? 28.537 73.895 25.423 1.00 74.83  ?  299 ILE B CG1 1 
ATOM   2959 C CG2 . ILE B 2 144 ? 30.237 75.686 24.847 1.00 75.71  ?  299 ILE B CG2 1 
ATOM   2960 C CD1 . ILE B 2 144 ? 29.282 72.655 24.958 1.00 76.15  ?  299 ILE B CD1 1 
ATOM   2961 N N   . ASN B 2 145 ? 27.464 77.798 22.971 1.00 76.19  ?  300 ASN B N   1 
ATOM   2962 C CA  . ASN B 2 145 ? 27.597 79.032 22.197 1.00 76.09  ?  300 ASN B CA  1 
ATOM   2963 C C   . ASN B 2 145 ? 26.969 80.193 22.927 1.00 79.88  ?  300 ASN B C   1 
ATOM   2964 O O   . ASN B 2 145 ? 27.600 81.237 23.049 1.00 78.55  ?  300 ASN B O   1 
ATOM   2965 C CB  . ASN B 2 145 ? 27.012 78.899 20.801 1.00 77.17  ?  300 ASN B CB  1 
ATOM   2966 C CG  . ASN B 2 145 ? 27.140 80.174 20.003 1.00 96.63  ?  300 ASN B CG  1 
ATOM   2967 O OD1 . ASN B 2 145 ? 28.241 80.605 19.619 1.00 87.74  ?  300 ASN B OD1 1 
ATOM   2968 N ND2 . ASN B 2 145 ? 26.013 80.831 19.789 1.00 86.37  ?  300 ASN B ND2 1 
ATOM   2969 N N   . PHE B 2 146 ? 25.754 79.999 23.454 1.00 78.15  ?  301 PHE B N   1 
ATOM   2970 C CA  . PHE B 2 146 ? 25.062 81.028 24.214 1.00 79.12  ?  301 PHE B CA  1 
ATOM   2971 C C   . PHE B 2 146 ? 25.862 81.451 25.460 1.00 84.00  ?  301 PHE B C   1 
ATOM   2972 O O   . PHE B 2 146 ? 25.926 82.645 25.751 1.00 84.59  ?  301 PHE B O   1 
ATOM   2973 C CB  . PHE B 2 146 ? 23.642 80.576 24.577 1.00 81.14  ?  301 PHE B CB  1 
ATOM   2974 C CG  . PHE B 2 146 ? 22.887 81.557 25.434 1.00 83.38  ?  301 PHE B CG  1 
ATOM   2975 C CD1 . PHE B 2 146 ? 22.250 82.656 24.868 1.00 87.19  ?  301 PHE B CD1 1 
ATOM   2976 C CD2 . PHE B 2 146 ? 22.817 81.388 26.810 1.00 85.97  ?  301 PHE B CD2 1 
ATOM   2977 C CE1 . PHE B 2 146 ? 21.547 83.564 25.663 1.00 88.20  ?  301 PHE B CE1 1 
ATOM   2978 C CE2 . PHE B 2 146 ? 22.109 82.293 27.605 1.00 89.13  ?  301 PHE B CE2 1 
ATOM   2979 C CZ  . PHE B 2 146 ? 21.483 83.379 27.026 1.00 87.32  ?  301 PHE B CZ  1 
ATOM   2980 N N   . LEU B 2 147 ? 26.475 80.481 26.173 1.00 79.53  ?  302 LEU B N   1 
ATOM   2981 C CA  . LEU B 2 147 ? 27.281 80.735 27.368 1.00 78.89  ?  302 LEU B CA  1 
ATOM   2982 C C   . LEU B 2 147 ? 28.536 81.518 27.034 1.00 83.43  ?  302 LEU B C   1 
ATOM   2983 O O   . LEU B 2 147 ? 28.874 82.447 27.760 1.00 83.34  ?  302 LEU B O   1 
ATOM   2984 C CB  . LEU B 2 147 ? 27.663 79.433 28.080 1.00 78.61  ?  302 LEU B CB  1 
ATOM   2985 C CG  . LEU B 2 147 ? 26.565 78.770 28.891 1.00 83.17  ?  302 LEU B CG  1 
ATOM   2986 C CD1 . LEU B 2 147 ? 26.949 77.348 29.223 1.00 83.23  ?  302 LEU B CD1 1 
ATOM   2987 C CD2 . LEU B 2 147 ? 26.228 79.567 30.168 1.00 85.76  ?  302 LEU B CD2 1 
ATOM   2988 N N   . HIS B 2 148 ? 29.204 81.157 25.932 1.00 80.60  ?  303 HIS B N   1 
ATOM   2989 C CA  . HIS B 2 148 ? 30.419 81.812 25.459 1.00 81.46  ?  303 HIS B CA  1 
ATOM   2990 C C   . HIS B 2 148 ? 30.125 83.231 24.942 1.00 89.74  ?  303 HIS B C   1 
ATOM   2991 O O   . HIS B 2 148 ? 30.837 84.163 25.313 1.00 90.14  ?  303 HIS B O   1 
ATOM   2992 C CB  . HIS B 2 148 ? 31.150 80.939 24.414 1.00 81.77  ?  303 HIS B CB  1 
ATOM   2993 C CG  . HIS B 2 148 ? 31.807 79.708 24.982 1.00 84.76  ?  303 HIS B CG  1 
ATOM   2994 N ND1 . HIS B 2 148 ? 32.757 78.996 24.260 1.00 85.99  ?  303 HIS B ND1 1 
ATOM   2995 C CD2 . HIS B 2 148 ? 31.646 79.110 26.190 1.00 86.17  ?  303 HIS B CD2 1 
ATOM   2996 C CE1 . HIS B 2 148 ? 33.114 77.984 25.035 1.00 85.14  ?  303 HIS B CE1 1 
ATOM   2997 N NE2 . HIS B 2 148 ? 32.483 78.016 26.210 1.00 85.55  ?  303 HIS B NE2 1 
ATOM   2998 N N   . GLU B 2 149 ? 29.042 83.405 24.145 1.00 88.55  ?  304 GLU B N   1 
ATOM   2999 C CA  . GLU B 2 149 ? 28.573 84.707 23.635 1.00 88.84  ?  304 GLU B CA  1 
ATOM   3000 C C   . GLU B 2 149 ? 28.284 85.672 24.792 1.00 93.21  ?  304 GLU B C   1 
ATOM   3001 O O   . GLU B 2 149 ? 28.356 86.887 24.608 1.00 93.44  ?  304 GLU B O   1 
ATOM   3002 C CB  . GLU B 2 149 ? 27.286 84.533 22.820 1.00 90.20  ?  304 GLU B CB  1 
ATOM   3003 C CG  . GLU B 2 149 ? 27.515 84.201 21.355 1.00 99.83  ?  304 GLU B CG  1 
ATOM   3004 C CD  . GLU B 2 149 ? 26.255 84.082 20.513 1.00 113.40 ?  304 GLU B CD  1 
ATOM   3005 O OE1 . GLU B 2 149 ? 25.163 83.877 21.093 1.00 97.40  ?  304 GLU B OE1 1 
ATOM   3006 O OE2 . GLU B 2 149 ? 26.365 84.177 19.268 1.00 101.82 -1 304 GLU B OE2 1 
ATOM   3007 N N   . ASN B 2 150 ? 27.951 85.122 25.973 1.00 89.40  ?  305 ASN B N   1 
ATOM   3008 C CA  . ASN B 2 150 ? 27.666 85.864 27.195 1.00 89.27  ?  305 ASN B CA  1 
ATOM   3009 C C   . ASN B 2 150 ? 28.872 85.912 28.135 1.00 94.20  ?  305 ASN B C   1 
ATOM   3010 O O   . ASN B 2 150 ? 28.715 86.184 29.324 1.00 92.78  ?  305 ASN B O   1 
ATOM   3011 C CB  . ASN B 2 150 ? 26.411 85.314 27.875 1.00 89.34  ?  305 ASN B CB  1 
ATOM   3012 C CG  . ASN B 2 150 ? 25.142 85.702 27.152 1.00 121.92 ?  305 ASN B CG  1 
ATOM   3013 O OD1 . ASN B 2 150 ? 24.938 85.398 25.966 1.00 118.75 ?  305 ASN B OD1 1 
ATOM   3014 N ND2 . ASN B 2 150 ? 24.257 86.386 27.855 1.00 115.77 ?  305 ASN B ND2 1 
ATOM   3015 N N   . HIS B 2 151 ? 30.079 85.698 27.573 1.00 92.82  ?  306 HIS B N   1 
ATOM   3016 C CA  . HIS B 2 151 ? 31.380 85.745 28.255 1.00 93.72  ?  306 HIS B CA  1 
ATOM   3017 C C   . HIS B 2 151 ? 31.449 84.866 29.495 1.00 98.24  ?  306 HIS B C   1 
ATOM   3018 O O   . HIS B 2 151 ? 31.844 85.325 30.571 1.00 99.08  ?  306 HIS B O   1 
ATOM   3019 C CB  . HIS B 2 151 ? 31.808 87.191 28.558 1.00 94.85  ?  306 HIS B CB  1 
ATOM   3020 C CG  . HIS B 2 151 ? 31.723 88.092 27.374 1.00 98.55  ?  306 HIS B CG  1 
ATOM   3021 N ND1 . HIS B 2 151 ? 32.783 88.228 26.498 1.00 100.47 ?  306 HIS B ND1 1 
ATOM   3022 C CD2 . HIS B 2 151 ? 30.695 88.865 26.950 1.00 100.44 ?  306 HIS B CD2 1 
ATOM   3023 C CE1 . HIS B 2 151 ? 32.374 89.088 25.577 1.00 100.07 ?  306 HIS B CE1 1 
ATOM   3024 N NE2 . HIS B 2 151 ? 31.123 89.498 25.808 1.00 100.39 ?  306 HIS B NE2 1 
ATOM   3025 N N   . HIS B 2 152 ? 31.065 83.601 29.338 1.00 92.72  ?  307 HIS B N   1 
ATOM   3026 C CA  . HIS B 2 152 ? 31.115 82.630 30.412 1.00 91.24  ?  307 HIS B CA  1 
ATOM   3027 C C   . HIS B 2 152 ? 31.864 81.386 29.942 1.00 88.68  ?  307 HIS B C   1 
ATOM   3028 O O   . HIS B 2 152 ? 32.111 81.206 28.740 1.00 87.85  ?  307 HIS B O   1 
ATOM   3029 C CB  . HIS B 2 152 ? 29.705 82.276 30.893 1.00 92.94  ?  307 HIS B CB  1 
ATOM   3030 C CG  . HIS B 2 152 ? 29.013 83.382 31.627 1.00 97.23  ?  307 HIS B CG  1 
ATOM   3031 N ND1 . HIS B 2 152 ? 28.190 84.284 30.971 1.00 99.39  ?  307 HIS B ND1 1 
ATOM   3032 C CD2 . HIS B 2 152 ? 28.994 83.661 32.951 1.00 99.56  ?  307 HIS B CD2 1 
ATOM   3033 C CE1 . HIS B 2 152 ? 27.717 85.089 31.910 1.00 98.92  ?  307 HIS B CE1 1 
ATOM   3034 N NE2 . HIS B 2 152 ? 28.173 84.755 33.117 1.00 99.34  ?  307 HIS B NE2 1 
ATOM   3035 N N   . ILE B 2 153 ? 32.294 80.579 30.917 1.00 79.76  ?  308 ILE B N   1 
ATOM   3036 C CA  . ILE B 2 153 ? 32.964 79.287 30.750 1.00 76.51  ?  308 ILE B CA  1 
ATOM   3037 C C   . ILE B 2 153 ? 32.202 78.332 31.683 1.00 77.09  ?  308 ILE B C   1 
ATOM   3038 O O   . ILE B 2 153 ? 31.976 78.671 32.847 1.00 76.33  ?  308 ILE B O   1 
ATOM   3039 C CB  . ILE B 2 153 ? 34.494 79.345 31.040 1.00 78.24  ?  308 ILE B CB  1 
ATOM   3040 C CG1 . ILE B 2 153 ? 35.186 80.416 30.190 1.00 77.94  ?  308 ILE B CG1 1 
ATOM   3041 C CG2 . ILE B 2 153 ? 35.153 77.981 30.802 1.00 78.43  ?  308 ILE B CG2 1 
ATOM   3042 C CD1 . ILE B 2 153 ? 36.258 81.136 30.891 1.00 79.91  ?  308 ILE B CD1 1 
ATOM   3043 N N   . HIS B 2 154 ? 31.748 77.184 31.157 1.00 71.04  ?  309 HIS B N   1 
ATOM   3044 C CA  . HIS B 2 154 ? 30.980 76.227 31.942 1.00 69.86  ?  309 HIS B CA  1 
ATOM   3045 C C   . HIS B 2 154 ? 31.847 75.511 32.977 1.00 71.05  ?  309 HIS B C   1 
ATOM   3046 O O   . HIS B 2 154 ? 31.410 75.359 34.127 1.00 70.20  ?  309 HIS B O   1 
ATOM   3047 C CB  . HIS B 2 154 ? 30.239 75.231 31.037 1.00 70.58  ?  309 HIS B CB  1 
ATOM   3048 C CG  . HIS B 2 154 ? 29.277 74.349 31.782 1.00 73.67  ?  309 HIS B CG  1 
ATOM   3049 N ND1 . HIS B 2 154 ? 29.707 73.235 32.475 1.00 75.32  ?  309 HIS B ND1 1 
ATOM   3050 C CD2 . HIS B 2 154 ? 27.937 74.453 31.920 1.00 75.16  ?  309 HIS B CD2 1 
ATOM   3051 C CE1 . HIS B 2 154 ? 28.623 72.698 33.005 1.00 74.62  ?  309 HIS B CE1 1 
ATOM   3052 N NE2 . HIS B 2 154 ? 27.533 73.393 32.691 1.00 74.96  ?  309 HIS B NE2 1 
ATOM   3053 N N   . ARG B 2 155 ? 33.056 75.051 32.559 1.00 65.24  ?  310 ARG B N   1 
ATOM   3054 C CA  . ARG B 2 155 ? 34.041 74.349 33.395 1.00 64.15  ?  310 ARG B CA  1 
ATOM   3055 C C   . ARG B 2 155 ? 33.700 72.873 33.769 1.00 65.08  ?  310 ARG B C   1 
ATOM   3056 O O   . ARG B 2 155 ? 34.571 72.157 34.281 1.00 65.38  ?  310 ARG B O   1 
ATOM   3057 C CB  . ARG B 2 155 ? 34.426 75.183 34.643 1.00 64.92  ?  310 ARG B CB  1 
ATOM   3058 N N   . ASP B 2 156 ? 32.463 72.413 33.506 1.00 58.07  ?  311 ASP B N   1 
ATOM   3059 C CA  . ASP B 2 156 ? 32.050 71.046 33.846 1.00 56.30  ?  311 ASP B CA  1 
ATOM   3060 C C   . ASP B 2 156 ? 31.198 70.365 32.736 1.00 55.77  ?  311 ASP B C   1 
ATOM   3061 O O   . ASP B 2 156 ? 30.245 69.634 33.016 1.00 53.49  ?  311 ASP B O   1 
ATOM   3062 C CB  . ASP B 2 156 ? 31.351 71.032 35.225 1.00 58.50  ?  311 ASP B CB  1 
ATOM   3063 C CG  . ASP B 2 156 ? 31.352 69.714 35.983 1.00 70.22  ?  311 ASP B CG  1 
ATOM   3064 O OD1 . ASP B 2 156 ? 32.125 68.800 35.596 1.00 72.27  ?  311 ASP B OD1 1 
ATOM   3065 O OD2 . ASP B 2 156 ? 30.560 69.586 36.954 1.00 72.59  -1 311 ASP B OD2 1 
ATOM   3066 N N   . ILE B 2 157 ? 31.571 70.605 31.470 1.00 51.23  ?  312 ILE B N   1 
ATOM   3067 C CA  . ILE B 2 157 ? 30.907 69.998 30.325 1.00 50.31  ?  312 ILE B CA  1 
ATOM   3068 C C   . ILE B 2 157 ? 31.173 68.491 30.330 1.00 53.61  ?  312 ILE B C   1 
ATOM   3069 O O   . ILE B 2 157 ? 32.320 68.034 30.247 1.00 53.82  ?  312 ILE B O   1 
ATOM   3070 C CB  . ILE B 2 157 ? 31.289 70.687 28.981 1.00 53.53  ?  312 ILE B CB  1 
ATOM   3071 C CG1 . ILE B 2 157 ? 30.768 72.146 28.914 1.00 53.24  ?  312 ILE B CG1 1 
ATOM   3072 C CG2 . ILE B 2 157 ? 30.848 69.849 27.755 1.00 55.08  ?  312 ILE B CG2 1 
ATOM   3073 C CD1 . ILE B 2 157 ? 29.175 72.345 28.901 1.00 57.93  ?  312 ILE B CD1 1 
ATOM   3074 N N   . LYS B 2 158 ? 30.098 67.735 30.485 1.00 49.57  ?  313 LYS B N   1 
ATOM   3075 C CA  . LYS B 2 158 ? 30.103 66.284 30.488 1.00 49.07  ?  313 LYS B CA  1 
ATOM   3076 C C   . LYS B 2 158 ? 28.696 65.823 30.157 1.00 53.53  ?  313 LYS B C   1 
ATOM   3077 O O   . LYS B 2 158 ? 27.766 66.632 30.226 1.00 50.93  ?  313 LYS B O   1 
ATOM   3078 C CB  . LYS B 2 158 ? 30.625 65.714 31.823 1.00 51.15  ?  313 LYS B CB  1 
ATOM   3079 C CG  . LYS B 2 158 ? 29.960 66.215 33.092 1.00 55.32  ?  313 LYS B CG  1 
ATOM   3080 C CD  . LYS B 2 158 ? 30.309 65.246 34.190 1.00 68.14  ?  313 LYS B CD  1 
ATOM   3081 C CE  . LYS B 2 158 ? 30.229 65.864 35.556 1.00 83.72  ?  313 LYS B CE  1 
ATOM   3082 N NZ  . LYS B 2 158 ? 30.674 64.913 36.608 1.00 92.14  1  313 LYS B NZ  1 
ATOM   3083 N N   . SER B 2 159 ? 28.530 64.540 29.779 1.00 52.21  ?  314 SER B N   1 
ATOM   3084 C CA  . SER B 2 159 ? 27.217 63.999 29.421 1.00 51.98  ?  314 SER B CA  1 
ATOM   3085 C C   . SER B 2 159 ? 26.221 63.935 30.595 1.00 56.09  ?  314 SER B C   1 
ATOM   3086 O O   . SER B 2 159 ? 25.011 63.952 30.355 1.00 56.65  ?  314 SER B O   1 
ATOM   3087 C CB  . SER B 2 159 ? 27.339 62.663 28.702 1.00 54.25  ?  314 SER B CB  1 
ATOM   3088 O OG  . SER B 2 159 ? 28.079 61.762 29.503 1.00 61.56  ?  314 SER B OG  1 
ATOM   3089 N N   . ALA B 2 160 ? 26.703 63.930 31.848 1.00 50.96  ?  315 ALA B N   1 
ATOM   3090 C CA  . ALA B 2 160 ? 25.797 63.952 33.005 1.00 50.85  ?  315 ALA B CA  1 
ATOM   3091 C C   . ALA B 2 160 ? 25.169 65.344 33.139 1.00 57.25  ?  315 ALA B C   1 
ATOM   3092 O O   . ALA B 2 160 ? 24.082 65.478 33.702 1.00 57.57  ?  315 ALA B O   1 
ATOM   3093 C CB  . ALA B 2 160 ? 26.555 63.609 34.268 1.00 51.16  ?  315 ALA B CB  1 
ATOM   3094 N N   . ASN B 2 161 ? 25.855 66.372 32.601 1.00 53.80  ?  316 ASN B N   1 
ATOM   3095 C CA  . ASN B 2 161 ? 25.437 67.767 32.638 1.00 53.29  ?  316 ASN B CA  1 
ATOM   3096 C C   . ASN B 2 161 ? 24.732 68.230 31.358 1.00 57.01  ?  316 ASN B C   1 
ATOM   3097 O O   . ASN B 2 161 ? 24.664 69.428 31.083 1.00 56.61  ?  316 ASN B O   1 
ATOM   3098 C CB  . ASN B 2 161 ? 26.623 68.673 33.033 1.00 53.83  ?  316 ASN B CB  1 
ATOM   3099 C CG  . ASN B 2 161 ? 26.987 68.565 34.494 1.00 69.31  ?  316 ASN B CG  1 
ATOM   3100 O OD1 . ASN B 2 161 ? 26.219 68.060 35.328 1.00 69.84  ?  316 ASN B OD1 1 
ATOM   3101 N ND2 . ASN B 2 161 ? 28.166 69.042 34.841 1.00 55.47  ?  316 ASN B ND2 1 
ATOM   3102 N N   . ILE B 2 162 ? 24.248 67.273 30.552 1.00 52.66  ?  317 ILE B N   1 
ATOM   3103 C CA  . ILE B 2 162 ? 23.443 67.528 29.357 1.00 50.91  ?  317 ILE B CA  1 
ATOM   3104 C C   . ILE B 2 162 ? 22.144 66.794 29.621 1.00 54.91  ?  317 ILE B C   1 
ATOM   3105 O O   . ILE B 2 162 ? 22.091 65.553 29.603 1.00 54.99  ?  317 ILE B O   1 
ATOM   3106 C CB  . ILE B 2 162 ? 24.107 67.157 28.018 1.00 52.68  ?  317 ILE B CB  1 
ATOM   3107 C CG1 . ILE B 2 162 ? 25.386 67.977 27.809 1.00 52.46  ?  317 ILE B CG1 1 
ATOM   3108 C CG2 . ILE B 2 162 ? 23.117 67.393 26.879 1.00 52.95  ?  317 ILE B CG2 1 
ATOM   3109 C CD1 . ILE B 2 162 ? 26.365 67.427 26.809 1.00 58.22  ?  317 ILE B CD1 1 
ATOM   3110 N N   . LEU B 2 163 ? 21.135 67.565 29.996 1.00 51.18  ?  318 LEU B N   1 
ATOM   3111 C CA  . LEU B 2 163 ? 19.826 67.039 30.347 1.00 51.51  ?  318 LEU B CA  1 
ATOM   3112 C C   . LEU B 2 163 ? 18.857 67.057 29.155 1.00 56.17  ?  318 LEU B C   1 
ATOM   3113 O O   . LEU B 2 163 ? 19.096 67.768 28.162 1.00 54.15  ?  318 LEU B O   1 
ATOM   3114 C CB  . LEU B 2 163 ? 19.303 67.756 31.600 1.00 51.31  ?  318 LEU B CB  1 
ATOM   3115 C CG  . LEU B 2 163 ? 19.624 67.122 32.974 1.00 55.00  ?  318 LEU B CG  1 
ATOM   3116 C CD1 . LEU B 2 163 ? 20.989 66.484 33.034 1.00 54.47  ?  318 LEU B CD1 1 
ATOM   3117 C CD2 . LEU B 2 163 ? 19.543 68.132 34.039 1.00 56.49  ?  318 LEU B CD2 1 
ATOM   3118 N N   . LEU B 2 164 ? 17.822 66.199 29.212 1.00 54.77  ?  319 LEU B N   1 
ATOM   3119 C CA  . LEU B 2 164 ? 16.900 66.021 28.090 1.00 55.50  ?  319 LEU B CA  1 
ATOM   3120 C C   . LEU B 2 164 ? 15.423 66.087 28.463 1.00 64.77  ?  319 LEU B C   1 
ATOM   3121 O O   . LEU B 2 164 ? 14.995 65.428 29.420 1.00 63.05  ?  319 LEU B O   1 
ATOM   3122 C CB  . LEU B 2 164 ? 17.188 64.660 27.391 1.00 54.73  ?  319 LEU B CB  1 
ATOM   3123 C CG  . LEU B 2 164 ? 18.631 64.328 26.974 1.00 57.24  ?  319 LEU B CG  1 
ATOM   3124 C CD1 . LEU B 2 164 ? 18.812 62.853 26.789 1.00 56.17  ?  319 LEU B CD1 1 
ATOM   3125 C CD2 . LEU B 2 164 ? 19.040 65.080 25.732 1.00 56.00  ?  319 LEU B CD2 1 
ATOM   3126 N N   . ASP B 2 165 ? 14.631 66.829 27.656 1.00 67.28  ?  320 ASP B N   1 
ATOM   3127 C CA  . ASP B 2 165 ? 13.176 66.934 27.834 1.00 69.09  ?  320 ASP B CA  1 
ATOM   3128 C C   . ASP B 2 165 ? 12.467 65.804 27.064 1.00 77.67  ?  320 ASP B C   1 
ATOM   3129 O O   . ASP B 2 165 ? 13.144 64.933 26.507 1.00 77.37  ?  320 ASP B O   1 
ATOM   3130 C CB  . ASP B 2 165 ? 12.647 68.335 27.443 1.00 71.05  ?  320 ASP B CB  1 
ATOM   3131 C CG  . ASP B 2 165 ? 12.666 68.711 25.964 1.00 86.79  ?  320 ASP B CG  1 
ATOM   3132 O OD1 . ASP B 2 165 ? 12.957 67.832 25.123 1.00 87.91  ?  320 ASP B OD1 1 
ATOM   3133 O OD2 . ASP B 2 165 ? 12.366 69.884 25.646 1.00 94.46  -1 320 ASP B OD2 1 
ATOM   3134 N N   . GLU B 2 166 ? 11.103 65.842 27.011 1.00 77.03  ?  321 GLU B N   1 
ATOM   3135 C CA  . GLU B 2 166 ? 10.238 64.867 26.307 1.00 76.32  ?  321 GLU B CA  1 
ATOM   3136 C C   . GLU B 2 166 ? 10.654 64.730 24.843 1.00 75.62  ?  321 GLU B C   1 
ATOM   3137 O O   . GLU B 2 166 ? 10.667 63.615 24.323 1.00 75.85  ?  321 GLU B O   1 
ATOM   3138 C CB  . GLU B 2 166 ? 8.745  65.280 26.352 1.00 77.83  ?  321 GLU B CB  1 
ATOM   3139 C CG  . GLU B 2 166 ? 8.135  65.452 27.731 1.00 90.17  ?  321 GLU B CG  1 
ATOM   3140 C CD  . GLU B 2 166 ? 8.155  66.861 28.306 1.00 124.80 ?  321 GLU B CD  1 
ATOM   3141 O OE1 . GLU B 2 166 ? 7.442  67.088 29.312 1.00 120.57 ?  321 GLU B OE1 1 
ATOM   3142 O OE2 . GLU B 2 166 ? 8.868  67.735 27.763 1.00 126.94 -1 321 GLU B OE2 1 
ATOM   3143 N N   . ALA B 2 167 ? 10.985 65.863 24.192 1.00 67.64  ?  322 ALA B N   1 
ATOM   3144 C CA  . ALA B 2 167 ? 11.387 65.919 22.788 1.00 66.24  ?  322 ALA B CA  1 
ATOM   3145 C C   . ALA B 2 167 ? 12.880 65.681 22.567 1.00 68.21  ?  322 ALA B C   1 
ATOM   3146 O O   . ALA B 2 167 ? 13.344 65.830 21.437 1.00 67.79  ?  322 ALA B O   1 
ATOM   3147 C CB  . ALA B 2 167 ? 10.978 67.256 22.189 1.00 66.98  ?  322 ALA B CB  1 
ATOM   3148 N N   . PHE B 2 168 ? 13.637 65.307 23.621 1.00 63.58  ?  323 PHE B N   1 
ATOM   3149 C CA  . PHE B 2 168 ? 15.091 65.071 23.536 1.00 62.75  ?  323 PHE B CA  1 
ATOM   3150 C C   . PHE B 2 168 ? 15.882 66.322 23.149 1.00 66.08  ?  323 PHE B C   1 
ATOM   3151 O O   . PHE B 2 168 ? 16.893 66.242 22.447 1.00 63.91  ?  323 PHE B O   1 
ATOM   3152 C CB  . PHE B 2 168 ? 15.453 63.861 22.639 1.00 64.03  ?  323 PHE B CB  1 
ATOM   3153 C CG  . PHE B 2 168 ? 14.801 62.564 23.052 1.00 65.10  ?  323 PHE B CG  1 
ATOM   3154 C CD1 . PHE B 2 168 ? 13.607 62.149 22.467 1.00 67.24  ?  323 PHE B CD1 1 
ATOM   3155 C CD2 . PHE B 2 168 ? 15.363 61.769 24.048 1.00 65.91  ?  323 PHE B CD2 1 
ATOM   3156 C CE1 . PHE B 2 168 ? 13.006 60.947 22.844 1.00 67.20  ?  323 PHE B CE1 1 
ATOM   3157 C CE2 . PHE B 2 168 ? 14.754 60.566 24.430 1.00 68.04  ?  323 PHE B CE2 1 
ATOM   3158 C CZ  . PHE B 2 168 ? 13.579 60.166 23.826 1.00 65.42  ?  323 PHE B CZ  1 
ATOM   3159 N N   . THR B 2 169 ? 15.398 67.488 23.605 1.00 64.86  ?  324 THR B N   1 
ATOM   3160 C CA  . THR B 2 169 ? 16.079 68.764 23.422 1.00 65.34  ?  324 THR B CA  1 
ATOM   3161 C C   . THR B 2 169 ? 17.174 68.774 24.501 1.00 68.78  ?  324 THR B C   1 
ATOM   3162 O O   . THR B 2 169 ? 16.885 68.516 25.687 1.00 66.62  ?  324 THR B O   1 
ATOM   3163 C CB  . THR B 2 169 ? 15.076 69.946 23.526 1.00 74.43  ?  324 THR B CB  1 
ATOM   3164 O OG1 . THR B 2 169 ? 14.245 69.948 22.367 1.00 79.25  ?  324 THR B OG1 1 
ATOM   3165 C CG2 . THR B 2 169 ? 15.757 71.307 23.647 1.00 69.84  ?  324 THR B CG2 1 
ATOM   3166 N N   . ALA B 2 170 ? 18.433 69.019 24.065 1.00 66.11  ?  325 ALA B N   1 
ATOM   3167 C CA  . ALA B 2 170 ? 19.591 69.100 24.955 1.00 66.62  ?  325 ALA B CA  1 
ATOM   3168 C C   . ALA B 2 170 ? 19.483 70.371 25.788 1.00 70.82  ?  325 ALA B C   1 
ATOM   3169 O O   . ALA B 2 170 ? 19.106 71.418 25.264 1.00 69.44  ?  325 ALA B O   1 
ATOM   3170 C CB  . ALA B 2 170 ? 20.871 69.131 24.139 1.00 67.41  ?  325 ALA B CB  1 
ATOM   3171 N N   . LYS B 2 171 ? 19.770 70.282 27.087 1.00 68.30  ?  326 LYS B N   1 
ATOM   3172 C CA  . LYS B 2 171 ? 19.727 71.438 27.977 1.00 67.42  ?  326 LYS B CA  1 
ATOM   3173 C C   . LYS B 2 171 ? 20.820 71.312 29.030 1.00 70.46  ?  326 LYS B C   1 
ATOM   3174 O O   . LYS B 2 171 ? 20.739 70.466 29.918 1.00 69.54  ?  326 LYS B O   1 
ATOM   3175 C CB  . LYS B 2 171 ? 18.321 71.665 28.561 1.00 68.99  ?  326 LYS B CB  1 
ATOM   3176 N N   . ILE B 2 172 ? 21.895 72.093 28.839 1.00 67.58  ?  327 ILE B N   1 
ATOM   3177 C CA  . ILE B 2 172 ? 23.090 72.181 29.675 1.00 67.58  ?  327 ILE B CA  1 
ATOM   3178 C C   . ILE B 2 172 ? 22.668 72.508 31.119 1.00 76.80  ?  327 ILE B C   1 
ATOM   3179 O O   . ILE B 2 172 ? 21.867 73.414 31.331 1.00 76.23  ?  327 ILE B O   1 
ATOM   3180 C CB  . ILE B 2 172 ? 24.052 73.283 29.127 1.00 69.72  ?  327 ILE B CB  1 
ATOM   3181 C CG1 . ILE B 2 172 ? 24.375 73.192 27.599 1.00 69.47  ?  327 ILE B CG1 1 
ATOM   3182 C CG2 . ILE B 2 172 ? 25.293 73.466 29.999 1.00 70.68  ?  327 ILE B CG2 1 
ATOM   3183 C CD1 . ILE B 2 172 ? 25.450 72.154 27.098 1.00 74.46  ?  327 ILE B CD1 1 
ATOM   3184 N N   . SER B 2 173 ? 23.207 71.769 32.096 1.00 78.26  ?  328 SER B N   1 
ATOM   3185 C CA  . SER B 2 173 ? 22.954 71.982 33.521 1.00 79.85  ?  328 SER B CA  1 
ATOM   3186 C C   . SER B 2 173 ? 24.281 72.167 34.278 1.00 88.28  ?  328 SER B C   1 
ATOM   3187 O O   . SER B 2 173 ? 25.356 72.113 33.669 1.00 87.04  ?  328 SER B O   1 
ATOM   3188 C CB  . SER B 2 173 ? 22.175 70.809 34.105 1.00 82.96  ?  328 SER B CB  1 
ATOM   3189 O OG  . SER B 2 173 ? 22.993 69.655 34.205 1.00 90.52  ?  328 SER B OG  1 
ATOM   3190 N N   . ASP B 2 174 ? 24.184 72.368 35.610 1.00 89.15  ?  329 ASP B N   1 
ATOM   3191 C CA  . ASP B 2 174 ? 25.284 72.515 36.571 1.00 91.03  ?  329 ASP B CA  1 
ATOM   3192 C C   . ASP B 2 174 ? 26.235 73.684 36.292 1.00 99.09  ?  329 ASP B C   1 
ATOM   3193 O O   . ASP B 2 174 ? 27.280 73.518 35.657 1.00 98.00  ?  329 ASP B O   1 
ATOM   3194 C CB  . ASP B 2 174 ? 26.017 71.173 36.800 1.00 92.91  ?  329 ASP B CB  1 
ATOM   3195 C CG  . ASP B 2 174 ? 26.540 70.930 38.203 1.00 101.99 ?  329 ASP B CG  1 
ATOM   3196 O OD1 . ASP B 2 174 ? 27.416 70.054 38.363 1.00 102.22 ?  329 ASP B OD1 1 
ATOM   3197 O OD2 . ASP B 2 174 ? 26.038 71.577 39.147 1.00 109.14 -1 329 ASP B OD2 1 
ATOM   3198 N N   . PHE B 2 175 ? 25.857 74.870 36.801 1.00 99.52  ?  330 PHE B N   1 
ATOM   3199 C CA  . PHE B 2 175 ? 26.615 76.115 36.648 1.00 100.92 ?  330 PHE B CA  1 
ATOM   3200 C C   . PHE B 2 175 ? 27.209 76.606 37.987 1.00 107.09 ?  330 PHE B C   1 
ATOM   3201 O O   . PHE B 2 175 ? 27.597 77.773 38.095 1.00 107.38 ?  330 PHE B O   1 
ATOM   3202 C CB  . PHE B 2 175 ? 25.737 77.202 36.000 1.00 103.01 ?  330 PHE B CB  1 
ATOM   3203 C CG  . PHE B 2 175 ? 25.089 76.783 34.702 1.00 104.97 ?  330 PHE B CG  1 
ATOM   3204 C CD1 . PHE B 2 175 ? 23.786 76.291 34.683 1.00 108.55 ?  330 PHE B CD1 1 
ATOM   3205 C CD2 . PHE B 2 175 ? 25.777 76.879 33.498 1.00 107.34 ?  330 PHE B CD2 1 
ATOM   3206 C CE1 . PHE B 2 175 ? 23.179 75.905 33.486 1.00 109.59 ?  330 PHE B CE1 1 
ATOM   3207 C CE2 . PHE B 2 175 ? 25.163 76.503 32.295 1.00 110.40 ?  330 PHE B CE2 1 
ATOM   3208 C CZ  . PHE B 2 175 ? 23.871 76.017 32.299 1.00 108.60 ?  330 PHE B CZ  1 
ATOM   3209 N N   . GLY B 2 176 ? 27.305 75.702 38.968 1.00 104.25 ?  331 GLY B N   1 
ATOM   3210 C CA  . GLY B 2 176 ? 27.858 75.988 40.289 1.00 104.11 ?  331 GLY B CA  1 
ATOM   3211 C C   . GLY B 2 176 ? 29.336 76.340 40.314 1.00 107.90 ?  331 GLY B C   1 
ATOM   3212 O O   . GLY B 2 176 ? 29.748 77.214 41.085 1.00 107.83 ?  331 GLY B O   1 
ATOM   3213 N N   . LEU B 2 177 ? 30.166 75.631 39.517 1.00 103.79 ?  332 LEU B N   1 
ATOM   3214 C CA  . LEU B 2 177 ? 31.621 75.848 39.485 1.00 122.29 ?  332 LEU B CA  1 
ATOM   3215 C C   . LEU B 2 177 ? 32.089 76.911 38.472 1.00 136.16 ?  332 LEU B C   1 
ATOM   3216 O O   . LEU B 2 177 ? 32.045 78.108 38.756 1.00 92.31  ?  332 LEU B O   1 
ATOM   3217 C CB  . LEU B 2 177 ? 32.382 74.504 39.338 1.00 122.21 ?  332 LEU B CB  1 
ATOM   3218 C CG  . LEU B 2 177 ? 32.707 73.943 37.934 1.00 126.59 ?  332 LEU B CG  1 
ATOM   3219 C CD1 . LEU B 2 177 ? 33.398 72.591 38.041 1.00 128.31 ?  332 LEU B CD1 1 
ATOM   3220 C CD2 . LEU B 2 177 ? 31.470 73.823 37.063 1.00 126.55 ?  332 LEU B CD2 1 
ATOM   3221 N N   . THR B 2 187 ? 48.219 72.069 44.516 1.00 82.44  ?  342 THR B N   1 
ATOM   3222 C CA  . THR B 2 187 ? 48.400 72.765 43.242 1.00 81.49  ?  342 THR B CA  1 
ATOM   3223 C C   . THR B 2 187 ? 48.980 71.858 42.151 1.00 81.42  ?  342 THR B C   1 
ATOM   3224 O O   . THR B 2 187 ? 49.312 70.703 42.403 1.00 80.34  ?  342 THR B O   1 
ATOM   3225 C CB  . THR B 2 187 ? 49.211 74.082 43.399 1.00 94.49  ?  342 THR B CB  1 
ATOM   3226 O OG1 . THR B 2 187 ? 49.671 74.258 44.745 1.00 95.28  ?  342 THR B OG1 1 
ATOM   3227 C CG2 . THR B 2 187 ? 48.451 75.308 42.901 1.00 94.18  ?  342 THR B CG2 1 
ATOM   3228 N N   . VAL B 2 188 ? 49.107 72.419 40.942 1.00 76.48  ?  343 VAL B N   1 
ATOM   3229 C CA  . VAL B 2 188 ? 49.604 71.802 39.707 1.00 75.12  ?  343 VAL B CA  1 
ATOM   3230 C C   . VAL B 2 188 ? 51.147 71.713 39.620 1.00 78.08  ?  343 VAL B C   1 
ATOM   3231 O O   . VAL B 2 188 ? 51.673 71.007 38.752 1.00 76.94  ?  343 VAL B O   1 
ATOM   3232 C CB  . VAL B 2 188 ? 48.930 72.407 38.439 1.00 77.59  ?  343 VAL B CB  1 
ATOM   3233 C CG1 . VAL B 2 188 ? 47.447 72.081 38.419 1.00 77.17  ?  343 VAL B CG1 1 
ATOM   3234 C CG2 . VAL B 2 188 ? 49.125 73.912 38.359 1.00 77.07  ?  343 VAL B CG2 1 
ATOM   3235 N N   . MET B 2 189 ? 51.855 72.412 40.539 1.00 74.54  ?  344 MET B N   1 
ATOM   3236 C CA  . MET B 2 189 ? 53.321 72.393 40.648 1.00 73.98  ?  344 MET B CA  1 
ATOM   3237 C C   . MET B 2 189 ? 53.780 71.310 41.639 1.00 77.15  ?  344 MET B C   1 
ATOM   3238 O O   . MET B 2 189 ? 54.973 71.191 41.909 1.00 76.55  ?  344 MET B O   1 
ATOM   3239 C CB  . MET B 2 189 ? 53.870 73.766 41.095 1.00 75.99  ?  344 MET B CB  1 
ATOM   3240 C CG  . MET B 2 189 ? 54.068 74.767 39.961 1.00 78.92  ?  344 MET B CG  1 
ATOM   3241 S SD  . MET B 2 189 ? 55.233 74.322 38.638 1.00 81.72  ?  344 MET B SD  1 
ATOM   3242 C CE  . MET B 2 189 ? 56.729 74.975 39.293 1.00 77.98  ?  344 MET B CE  1 
HETATM 3243 N N   . TPO B 2 190 ? 52.846 70.509 42.163 1.00 73.77  ?  345 TPO B N   1 
HETATM 3244 C CA  . TPO B 2 190 ? 53.180 69.474 43.127 1.00 74.16  ?  345 TPO B CA  1 
HETATM 3245 C CB  . TPO B 2 190 ? 52.668 70.030 44.474 1.00 77.07  ?  345 TPO B CB  1 
HETATM 3246 C CG2 . TPO B 2 190 ? 52.556 68.969 45.565 1.00 75.87  ?  345 TPO B CG2 1 
HETATM 3247 O OG1 . TPO B 2 190 ? 53.635 71.012 44.909 1.00 82.19  ?  345 TPO B OG1 1 
HETATM 3248 P P   . TPO B 2 190 ? 53.063 72.447 45.188 1.00 86.86  ?  345 TPO B P   1 
HETATM 3249 O O1P . TPO B 2 190 ? 51.916 72.858 44.224 1.00 86.45  ?  345 TPO B O1P 1 
HETATM 3250 O O2P . TPO B 2 190 ? 54.234 73.478 45.040 1.00 87.26  -1 345 TPO B O2P 1 
HETATM 3251 O O3P . TPO B 2 190 ? 52.517 72.525 46.632 1.00 87.76  -1 345 TPO B O3P 1 
HETATM 3252 C C   . TPO B 2 190 ? 52.654 68.107 42.698 1.00 75.89  ?  345 TPO B C   1 
HETATM 3253 O O   . TPO B 2 190 ? 51.548 68.008 42.164 1.00 75.84  ?  345 TPO B O   1 
HETATM 3254 N N   . SEP B 2 191 ? 53.454 67.059 42.925 1.00 70.55  ?  346 SEP B N   1 
HETATM 3255 C CA  . SEP B 2 191 ? 53.087 65.674 42.620 1.00 69.98  ?  346 SEP B CA  1 
HETATM 3256 C CB  . SEP B 2 191 ? 54.193 64.685 43.038 1.00 71.13  ?  346 SEP B CB  1 
HETATM 3257 O OG  . SEP B 2 191 ? 55.554 65.152 42.803 1.00 72.06  ?  346 SEP B OG  1 
HETATM 3258 C C   . SEP B 2 191 ? 51.817 65.309 43.388 1.00 71.56  ?  346 SEP B C   1 
HETATM 3259 O O   . SEP B 2 191 ? 51.684 65.665 44.563 1.00 70.28  ?  346 SEP B O   1 
HETATM 3260 P P   . SEP B 2 191 ? 56.207 65.533 44.135 1.00 73.24  ?  346 SEP B P   1 
HETATM 3261 O O1P . SEP B 2 191 ? 57.637 65.881 43.901 1.00 74.38  ?  346 SEP B O1P 1 
HETATM 3262 O O2P . SEP B 2 191 ? 55.420 66.646 44.821 1.00 72.92  -1 346 SEP B O2P 1 
HETATM 3263 O O3P . SEP B 2 191 ? 56.410 64.362 45.040 1.00 74.53  -1 346 SEP B O3P 1 
ATOM   3264 N N   . ARG B 2 192 ? 50.858 64.662 42.705 1.00 67.18  ?  347 ARG B N   1 
ATOM   3265 C CA  . ARG B 2 192 ? 49.567 64.303 43.289 1.00 66.76  ?  347 ARG B CA  1 
ATOM   3266 C C   . ARG B 2 192 ? 48.871 63.168 42.548 1.00 72.31  ?  347 ARG B C   1 
ATOM   3267 O O   . ARG B 2 192 ? 49.120 62.967 41.354 1.00 72.61  ?  347 ARG B O   1 
ATOM   3268 C CB  . ARG B 2 192 ? 48.626 65.546 43.370 1.00 65.31  ?  347 ARG B CB  1 
ATOM   3269 C CG  . ARG B 2 192 ? 48.189 66.155 42.032 1.00 68.71  ?  347 ARG B CG  1 
ATOM   3270 C CD  . ARG B 2 192 ? 47.044 67.134 42.193 1.00 73.72  ?  347 ARG B CD  1 
ATOM   3271 N NE  . ARG B 2 192 ? 46.395 67.432 40.915 1.00 75.37  1  347 ARG B NE  1 
ATOM   3272 N N   . ILE B 2 193 ? 47.957 62.464 43.248 1.00 68.95  ?  348 ILE B N   1 
ATOM   3273 C CA  . ILE B 2 193 ? 47.115 61.423 42.661 1.00 68.56  ?  348 ILE B CA  1 
ATOM   3274 C C   . ILE B 2 193 ? 45.993 62.156 41.912 1.00 70.85  ?  348 ILE B C   1 
ATOM   3275 O O   . ILE B 2 193 ? 45.860 61.973 40.708 1.00 69.95  ?  348 ILE B O   1 
ATOM   3276 C CB  . ILE B 2 193 ? 46.565 60.422 43.730 1.00 71.57  ?  348 ILE B CB  1 
ATOM   3277 C CG1 . ILE B 2 193 ? 47.699 59.527 44.300 1.00 72.03  ?  348 ILE B CG1 1 
ATOM   3278 C CG2 . ILE B 2 193 ? 45.402 59.575 43.166 1.00 71.22  ?  348 ILE B CG2 1 
ATOM   3279 C CD1 . ILE B 2 193 ? 47.409 58.896 45.716 1.00 80.44  ?  348 ILE B CD1 1 
ATOM   3280 N N   . VAL B 2 194 ? 45.232 63.016 42.625 1.00 67.35  ?  349 VAL B N   1 
ATOM   3281 C CA  . VAL B 2 194 ? 44.093 63.830 42.135 1.00 114.92 ?  349 VAL B CA  1 
ATOM   3282 C C   . VAL B 2 194 ? 44.023 63.981 40.590 1.00 126.22 ?  349 VAL B C   1 
ATOM   3283 O O   . VAL B 2 194 ? 43.611 63.056 39.881 1.00 68.42  ?  349 VAL B O   1 
ATOM   3284 C CB  . VAL B 2 194 ? 43.964 65.212 42.860 1.00 118.86 ?  349 VAL B CB  1 
ATOM   3285 C CG1 . VAL B 2 194 ? 42.577 65.830 42.650 1.00 118.61 ?  349 VAL B CG1 1 
ATOM   3286 C CG2 . VAL B 2 194 ? 44.280 65.104 44.351 1.00 118.65 ?  349 VAL B CG2 1 
ATOM   3287 N N   . THR B 2 197 ? 42.012 63.387 33.990 1.00 70.54  ?  352 THR B N   1 
ATOM   3288 C CA  . THR B 2 197 ? 40.650 62.862 34.096 1.00 70.21  ?  352 THR B CA  1 
ATOM   3289 C C   . THR B 2 197 ? 39.974 62.718 32.728 1.00 73.88  ?  352 THR B C   1 
ATOM   3290 O O   . THR B 2 197 ? 40.512 63.170 31.709 1.00 74.51  ?  352 THR B O   1 
ATOM   3291 C CB  . THR B 2 197 ? 39.760 63.602 35.133 1.00 73.01  ?  352 THR B CB  1 
ATOM   3292 O OG1 . THR B 2 197 ? 39.341 64.865 34.620 1.00 72.89  ?  352 THR B OG1 1 
ATOM   3293 C CG2 . THR B 2 197 ? 40.384 63.706 36.516 1.00 68.80  ?  352 THR B CG2 1 
ATOM   3294 N N   . ALA B 2 198 ? 38.783 62.082 32.733 1.00 67.78  ?  353 ALA B N   1 
ATOM   3295 C CA  . ALA B 2 198 ? 37.962 61.760 31.582 1.00 66.15  ?  353 ALA B CA  1 
ATOM   3296 C C   . ALA B 2 198 ? 37.484 62.950 30.750 1.00 68.03  ?  353 ALA B C   1 
ATOM   3297 O O   . ALA B 2 198 ? 37.554 62.864 29.519 1.00 66.64  ?  353 ALA B O   1 
ATOM   3298 C CB  . ALA B 2 198 ? 36.786 60.911 32.020 1.00 66.61  ?  353 ALA B CB  1 
ATOM   3299 N N   . TYR B 2 199 ? 36.993 64.052 31.378 1.00 63.49  ?  354 TYR B N   1 
ATOM   3300 C CA  . TYR B 2 199 ? 36.497 65.128 30.512 1.00 62.46  ?  354 TYR B CA  1 
ATOM   3301 C C   . TYR B 2 199 ? 37.427 66.303 30.347 1.00 65.48  ?  354 TYR B C   1 
ATOM   3302 O O   . TYR B 2 199 ? 37.398 66.955 29.305 1.00 64.83  ?  354 TYR B O   1 
ATOM   3303 C CB  . TYR B 2 199 ? 35.090 65.602 30.910 1.00 63.25  ?  354 TYR B CB  1 
ATOM   3304 C CG  . TYR B 2 199 ? 34.042 64.513 30.874 1.00 64.34  ?  354 TYR B CG  1 
ATOM   3305 C CD1 . TYR B 2 199 ? 33.791 63.725 31.993 1.00 66.29  ?  354 TYR B CD1 1 
ATOM   3306 C CD2 . TYR B 2 199 ? 33.288 64.277 29.722 1.00 64.69  ?  354 TYR B CD2 1 
ATOM   3307 C CE1 . TYR B 2 199 ? 32.821 62.726 31.970 1.00 67.59  ?  354 TYR B CE1 1 
ATOM   3308 C CE2 . TYR B 2 199 ? 32.313 63.280 29.688 1.00 65.18  ?  354 TYR B CE2 1 
ATOM   3309 C CZ  . TYR B 2 199 ? 32.070 62.520 30.822 1.00 74.26  ?  354 TYR B CZ  1 
ATOM   3310 O OH  . TYR B 2 199 ? 31.135 61.510 30.802 1.00 77.13  ?  354 TYR B OH  1 
ATOM   3311 N N   . MET B 2 200 ? 38.252 66.569 31.369 1.00 61.78  ?  355 MET B N   1 
ATOM   3312 C CA  . MET B 2 200 ? 39.158 67.712 31.439 1.00 60.90  ?  355 MET B CA  1 
ATOM   3313 C C   . MET B 2 200 ? 40.218 67.841 30.367 1.00 59.89  ?  355 MET B C   1 
ATOM   3314 O O   . MET B 2 200 ? 40.930 66.887 30.079 1.00 57.90  ?  355 MET B O   1 
ATOM   3315 C CB  . MET B 2 200 ? 39.757 67.857 32.839 1.00 64.07  ?  355 MET B CB  1 
ATOM   3316 C CG  . MET B 2 200 ? 38.745 68.305 33.856 1.00 69.71  ?  355 MET B CG  1 
ATOM   3317 S SD  . MET B 2 200 ? 39.500 69.172 35.246 1.00 76.48  ?  355 MET B SD  1 
ATOM   3318 C CE  . MET B 2 200 ? 39.550 67.827 36.462 1.00 73.42  ?  355 MET B CE  1 
ATOM   3319 N N   . ALA B 2 201 ? 40.335 69.052 29.810 1.00 56.36  ?  356 ALA B N   1 
ATOM   3320 C CA  . ALA B 2 201 ? 41.337 69.441 28.817 1.00 56.25  ?  356 ALA B CA  1 
ATOM   3321 C C   . ALA B 2 201 ? 42.744 69.481 29.452 1.00 60.80  ?  356 ALA B C   1 
ATOM   3322 O O   . ALA B 2 201 ? 42.840 69.753 30.650 1.00 58.89  ?  356 ALA B O   1 
ATOM   3323 C CB  . ALA B 2 201 ? 40.987 70.798 28.238 1.00 56.63  ?  356 ALA B CB  1 
ATOM   3324 N N   . PRO B 2 202 ? 43.838 69.195 28.689 1.00 60.57  ?  357 PRO B N   1 
ATOM   3325 C CA  . PRO B 2 202 ? 45.189 69.210 29.290 1.00 61.60  ?  357 PRO B CA  1 
ATOM   3326 C C   . PRO B 2 202 ? 45.498 70.481 30.090 1.00 68.20  ?  357 PRO B C   1 
ATOM   3327 O O   . PRO B 2 202 ? 45.869 70.372 31.262 1.00 68.69  ?  357 PRO B O   1 
ATOM   3328 C CB  . PRO B 2 202 ? 46.131 69.023 28.089 1.00 62.87  ?  357 PRO B CB  1 
ATOM   3329 C CG  . PRO B 2 202 ? 45.302 69.242 26.883 1.00 66.74  ?  357 PRO B CG  1 
ATOM   3330 C CD  . PRO B 2 202 ? 43.912 68.836 27.259 1.00 62.17  ?  357 PRO B CD  1 
ATOM   3331 N N   . GLU B 2 203 ? 45.241 71.668 29.497 1.00 64.43  ?  358 GLU B N   1 
ATOM   3332 C CA  . GLU B 2 203 ? 45.443 72.962 30.137 1.00 64.20  ?  358 GLU B CA  1 
ATOM   3333 C C   . GLU B 2 203 ? 44.637 73.133 31.428 1.00 68.90  ?  358 GLU B C   1 
ATOM   3334 O O   . GLU B 2 203 ? 45.146 73.730 32.377 1.00 68.65  ?  358 GLU B O   1 
ATOM   3335 C CB  . GLU B 2 203 ? 45.222 74.132 29.144 1.00 65.47  ?  358 GLU B CB  1 
ATOM   3336 C CG  . GLU B 2 203 ? 43.771 74.475 28.803 1.00 70.64  ?  358 GLU B CG  1 
ATOM   3337 C CD  . GLU B 2 203 ? 43.093 73.659 27.719 1.00 71.90  ?  358 GLU B CD  1 
ATOM   3338 O OE1 . GLU B 2 203 ? 43.755 72.795 27.099 1.00 48.94  ?  358 GLU B OE1 1 
ATOM   3339 O OE2 . GLU B 2 203 ? 41.888 73.900 27.483 1.00 53.83  -1 358 GLU B OE2 1 
ATOM   3340 N N   . ALA B 2 204 ? 43.397 72.593 31.467 1.00 65.88  ?  359 ALA B N   1 
ATOM   3341 C CA  . ALA B 2 204 ? 42.520 72.691 32.644 1.00 65.30  ?  359 ALA B CA  1 
ATOM   3342 C C   . ALA B 2 204 ? 43.118 71.950 33.831 1.00 68.47  ?  359 ALA B C   1 
ATOM   3343 O O   . ALA B 2 204 ? 43.056 72.456 34.952 1.00 68.61  ?  359 ALA B O   1 
ATOM   3344 C CB  . ALA B 2 204 ? 41.137 72.154 32.329 1.00 65.74  ?  359 ALA B CB  1 
ATOM   3345 N N   . LEU B 2 205 ? 43.736 70.780 33.570 1.00 63.59  ?  360 LEU B N   1 
ATOM   3346 C CA  . LEU B 2 205 ? 44.378 69.946 34.585 1.00 63.15  ?  360 LEU B CA  1 
ATOM   3347 C C   . LEU B 2 205 ? 45.628 70.632 35.120 1.00 68.11  ?  360 LEU B C   1 
ATOM   3348 O O   . LEU B 2 205 ? 45.999 70.392 36.260 1.00 67.36  ?  360 LEU B O   1 
ATOM   3349 C CB  . LEU B 2 205 ? 44.724 68.555 34.024 1.00 62.81  ?  360 LEU B CB  1 
ATOM   3350 C CG  . LEU B 2 205 ? 43.541 67.620 33.726 1.00 66.56  ?  360 LEU B CG  1 
ATOM   3351 C CD1 . LEU B 2 205 ? 43.885 66.639 32.620 1.00 66.25  ?  360 LEU B CD1 1 
ATOM   3352 C CD2 . LEU B 2 205 ? 43.074 66.888 34.977 1.00 66.95  ?  360 LEU B CD2 1 
ATOM   3353 N N   . ARG B 2 206 ? 46.259 71.482 34.279 1.00 65.81  ?  361 ARG B N   1 
ATOM   3354 C CA  . ARG B 2 206 ? 47.436 72.309 34.575 1.00 65.51  ?  361 ARG B CA  1 
ATOM   3355 C C   . ARG B 2 206 ? 46.999 73.716 35.116 1.00 73.90  ?  361 ARG B C   1 
ATOM   3356 O O   . ARG B 2 206 ? 47.799 74.653 35.141 1.00 73.71  ?  361 ARG B O   1 
ATOM   3357 C CB  . ARG B 2 206 ? 48.334 72.437 33.330 1.00 60.74  ?  361 ARG B CB  1 
ATOM   3358 C CG  . ARG B 2 206 ? 48.795 71.106 32.729 1.00 60.27  ?  361 ARG B CG  1 
ATOM   3359 C CD  . ARG B 2 206 ? 49.494 71.318 31.399 1.00 51.83  ?  361 ARG B CD  1 
ATOM   3360 N NE  . ARG B 2 206 ? 50.033 70.082 30.825 1.00 50.87  ?  361 ARG B NE  1 
ATOM   3361 C CZ  . ARG B 2 206 ? 50.076 69.828 29.519 1.00 75.34  ?  361 ARG B CZ  1 
ATOM   3362 N NH1 . ARG B 2 206 ? 49.599 70.707 28.648 1.00 78.53  ?  361 ARG B NH1 1 
ATOM   3363 N NH2 . ARG B 2 206 ? 50.569 68.681 29.076 1.00 62.73  1  361 ARG B NH2 1 
ATOM   3364 N N   . GLY B 2 207 ? 45.738 73.833 35.543 1.00 73.52  ?  362 GLY B N   1 
ATOM   3365 C CA  . GLY B 2 207 ? 45.189 75.045 36.151 1.00 74.62  ?  362 GLY B CA  1 
ATOM   3366 C C   . GLY B 2 207 ? 44.529 76.092 35.269 1.00 80.52  ?  362 GLY B C   1 
ATOM   3367 O O   . GLY B 2 207 ? 43.842 76.969 35.798 1.00 79.56  ?  362 GLY B O   1 
ATOM   3368 N N   . GLU B 2 208 ? 44.739 76.039 33.935 1.00 78.57  ?  363 GLU B N   1 
ATOM   3369 C CA  . GLU B 2 208 ? 44.147 77.006 33.007 1.00 78.90  ?  363 GLU B CA  1 
ATOM   3370 C C   . GLU B 2 208 ? 42.626 76.930 32.915 1.00 86.19  ?  363 GLU B C   1 
ATOM   3371 O O   . GLU B 2 208 ? 42.055 75.845 32.949 1.00 86.76  ?  363 GLU B O   1 
ATOM   3372 C CB  . GLU B 2 208 ? 44.762 76.900 31.625 1.00 79.85  ?  363 GLU B CB  1 
ATOM   3373 C CG  . GLU B 2 208 ? 45.717 78.032 31.328 1.00 87.17  ?  363 GLU B CG  1 
ATOM   3374 C CD  . GLU B 2 208 ? 46.238 77.970 29.909 1.00 104.40 ?  363 GLU B CD  1 
ATOM   3375 O OE1 . GLU B 2 208 ? 47.253 77.275 29.684 1.00 100.73 ?  363 GLU B OE1 1 
ATOM   3376 O OE2 . GLU B 2 208 ? 45.595 78.565 29.014 1.00 94.47  -1 363 GLU B OE2 1 
ATOM   3377 N N   . ILE B 2 209 ? 41.980 78.102 32.815 1.00 83.98  ?  364 ILE B N   1 
ATOM   3378 C CA  . ILE B 2 209 ? 40.529 78.273 32.725 1.00 83.93  ?  364 ILE B CA  1 
ATOM   3379 C C   . ILE B 2 209 ? 40.224 79.189 31.535 1.00 86.35  ?  364 ILE B C   1 
ATOM   3380 O O   . ILE B 2 209 ? 40.214 80.419 31.658 1.00 85.97  ?  364 ILE B O   1 
ATOM   3381 C CB  . ILE B 2 209 ? 39.938 78.800 34.067 1.00 87.08  ?  364 ILE B CB  1 
ATOM   3382 N N   . THR B 2 210 ? 40.017 78.558 30.376 1.00 81.17  ?  365 THR B N   1 
ATOM   3383 C CA  . THR B 2 210 ? 39.741 79.151 29.061 1.00 80.07  ?  365 THR B CA  1 
ATOM   3384 C C   . THR B 2 210 ? 38.479 78.540 28.422 1.00 82.69  ?  365 THR B C   1 
ATOM   3385 O O   . THR B 2 210 ? 38.254 77.338 28.583 1.00 82.16  ?  365 THR B O   1 
ATOM   3386 C CB  . THR B 2 210 ? 40.987 79.036 28.134 1.00 84.72  ?  365 THR B CB  1 
ATOM   3387 O OG1 . THR B 2 210 ? 40.602 79.242 26.774 1.00 82.82  ?  365 THR B OG1 1 
ATOM   3388 C CG2 . THR B 2 210 ? 41.701 77.699 28.248 1.00 83.67  ?  365 THR B CG2 1 
ATOM   3389 N N   . PRO B 2 211 ? 37.673 79.316 27.647 1.00 77.64  ?  366 PRO B N   1 
ATOM   3390 C CA  . PRO B 2 211 ? 36.505 78.720 26.968 1.00 75.99  ?  366 PRO B CA  1 
ATOM   3391 C C   . PRO B 2 211 ? 36.901 77.569 26.036 1.00 74.37  ?  366 PRO B C   1 
ATOM   3392 O O   . PRO B 2 211 ? 36.076 76.703 25.773 1.00 74.12  ?  366 PRO B O   1 
ATOM   3393 C CB  . PRO B 2 211 ? 35.922 79.896 26.176 1.00 77.90  ?  366 PRO B CB  1 
ATOM   3394 C CG  . PRO B 2 211 ? 37.066 80.851 26.022 1.00 82.79  ?  366 PRO B CG  1 
ATOM   3395 C CD  . PRO B 2 211 ? 37.787 80.752 27.322 1.00 78.69  ?  366 PRO B CD  1 
ATOM   3396 N N   . LYS B 2 212 ? 38.166 77.542 25.571 1.00 66.95  ?  367 LYS B N   1 
ATOM   3397 C CA  . LYS B 2 212 ? 38.682 76.467 24.721 1.00 65.87  ?  367 LYS B CA  1 
ATOM   3398 C C   . LYS B 2 212 ? 38.674 75.089 25.437 1.00 67.27  ?  367 LYS B C   1 
ATOM   3399 O O   . LYS B 2 212 ? 38.568 74.066 24.765 1.00 67.26  ?  367 LYS B O   1 
ATOM   3400 C CB  . LYS B 2 212 ? 40.068 76.818 24.151 1.00 68.21  ?  367 LYS B CB  1 
ATOM   3401 N N   . SER B 2 213 ? 38.763 75.070 26.788 1.00 61.44  ?  368 SER B N   1 
ATOM   3402 C CA  . SER B 2 213 ? 38.687 73.847 27.594 1.00 60.00  ?  368 SER B CA  1 
ATOM   3403 C C   . SER B 2 213 ? 37.306 73.199 27.438 1.00 62.20  ?  368 SER B C   1 
ATOM   3404 O O   . SER B 2 213 ? 37.229 71.969 27.335 1.00 61.80  ?  368 SER B O   1 
ATOM   3405 C CB  . SER B 2 213 ? 38.943 74.140 29.073 1.00 62.60  ?  368 SER B CB  1 
ATOM   3406 O OG  . SER B 2 213 ? 40.167 74.821 29.300 1.00 67.58  ?  368 SER B OG  1 
ATOM   3407 N N   . ASP B 2 214 ? 36.216 74.033 27.419 1.00 57.39  ?  369 ASP B N   1 
ATOM   3408 C CA  . ASP B 2 214 ? 34.809 73.612 27.241 1.00 55.78  ?  369 ASP B CA  1 
ATOM   3409 C C   . ASP B 2 214 ? 34.640 72.807 25.943 1.00 54.63  ?  369 ASP B C   1 
ATOM   3410 O O   . ASP B 2 214 ? 33.960 71.793 25.962 1.00 55.44  ?  369 ASP B O   1 
ATOM   3411 C CB  . ASP B 2 214 ? 33.844 74.824 27.249 1.00 57.71  ?  369 ASP B CB  1 
ATOM   3412 C CG  . ASP B 2 214 ? 33.362 75.353 28.600 1.00 68.73  ?  369 ASP B CG  1 
ATOM   3413 O OD1 . ASP B 2 214 ? 33.729 74.762 29.647 1.00 68.12  ?  369 ASP B OD1 1 
ATOM   3414 O OD2 . ASP B 2 214 ? 32.601 76.350 28.610 1.00 76.46  -1 369 ASP B OD2 1 
ATOM   3415 N N   . ILE B 2 215 ? 35.295 73.240 24.847 1.00 47.75  ?  370 ILE B N   1 
ATOM   3416 C CA  . ILE B 2 215 ? 35.303 72.607 23.522 1.00 47.16  ?  370 ILE B CA  1 
ATOM   3417 C C   . ILE B 2 215 ? 35.916 71.209 23.611 1.00 51.88  ?  370 ILE B C   1 
ATOM   3418 O O   . ILE B 2 215 ? 35.333 70.248 23.098 1.00 50.70  ?  370 ILE B O   1 
ATOM   3419 C CB  . ILE B 2 215 ? 36.061 73.521 22.485 1.00 49.67  ?  370 ILE B CB  1 
ATOM   3420 C CG1 . ILE B 2 215 ? 35.408 74.930 22.320 1.00 49.55  ?  370 ILE B CG1 1 
ATOM   3421 C CG2 . ILE B 2 215 ? 36.414 72.827 21.132 1.00 47.42  ?  370 ILE B CG2 1 
ATOM   3422 C CD1 . ILE B 2 215 ? 34.058 74.979 21.765 1.00 55.23  ?  370 ILE B CD1 1 
ATOM   3423 N N   . TYR B 2 216 ? 37.097 71.093 24.254 1.00 50.48  ?  371 TYR B N   1 
ATOM   3424 C CA  . TYR B 2 216 ? 37.770 69.805 24.441 1.00 50.51  ?  371 TYR B CA  1 
ATOM   3425 C C   . TYR B 2 216 ? 36.779 68.813 25.081 1.00 56.87  ?  371 TYR B C   1 
ATOM   3426 O O   . TYR B 2 216 ? 36.551 67.741 24.522 1.00 57.69  ?  371 TYR B O   1 
ATOM   3427 C CB  . TYR B 2 216 ? 39.018 69.957 25.319 1.00 50.33  ?  371 TYR B CB  1 
ATOM   3428 C CG  . TYR B 2 216 ? 39.856 68.697 25.438 1.00 50.15  ?  371 TYR B CG  1 
ATOM   3429 C CD1 . TYR B 2 216 ? 39.592 67.751 26.425 1.00 51.08  ?  371 TYR B CD1 1 
ATOM   3430 C CD2 . TYR B 2 216 ? 40.924 68.462 24.574 1.00 50.28  ?  371 TYR B CD2 1 
ATOM   3431 C CE1 . TYR B 2 216 ? 40.371 66.602 26.548 1.00 50.83  ?  371 TYR B CE1 1 
ATOM   3432 C CE2 . TYR B 2 216 ? 41.700 67.314 24.681 1.00 51.00  ?  371 TYR B CE2 1 
ATOM   3433 C CZ  . TYR B 2 216 ? 41.431 66.390 25.678 1.00 59.96  ?  371 TYR B CZ  1 
ATOM   3434 O OH  . TYR B 2 216 ? 42.223 65.260 25.785 1.00 62.08  ?  371 TYR B OH  1 
ATOM   3435 N N   . SER B 2 217 ? 36.162 69.215 26.209 1.00 52.88  ?  372 SER B N   1 
ATOM   3436 C CA  . SER B 2 217 ? 35.188 68.437 26.950 1.00 53.39  ?  372 SER B CA  1 
ATOM   3437 C C   . SER B 2 217 ? 34.029 67.987 26.075 1.00 57.77  ?  372 SER B C   1 
ATOM   3438 O O   . SER B 2 217 ? 33.618 66.827 26.165 1.00 59.57  ?  372 SER B O   1 
ATOM   3439 C CB  . SER B 2 217 ? 34.694 69.221 28.162 1.00 58.07  ?  372 SER B CB  1 
ATOM   3440 O OG  . SER B 2 217 ? 35.748 69.368 29.099 1.00 66.84  ?  372 SER B OG  1 
ATOM   3441 N N   . PHE B 2 218 ? 33.547 68.882 25.194 1.00 51.86  ?  373 PHE B N   1 
ATOM   3442 C CA  . PHE B 2 218 ? 32.477 68.591 24.240 1.00 50.64  ?  373 PHE B CA  1 
ATOM   3443 C C   . PHE B 2 218 ? 32.875 67.482 23.242 1.00 53.45  ?  373 PHE B C   1 
ATOM   3444 O O   . PHE B 2 218 ? 32.021 66.695 22.836 1.00 53.78  ?  373 PHE B O   1 
ATOM   3445 C CB  . PHE B 2 218 ? 32.018 69.865 23.522 1.00 51.40  ?  373 PHE B CB  1 
ATOM   3446 C CG  . PHE B 2 218 ? 30.806 69.668 22.648 1.00 52.05  ?  373 PHE B CG  1 
ATOM   3447 C CD1 . PHE B 2 218 ? 29.563 69.404 23.207 1.00 54.40  ?  373 PHE B CD1 1 
ATOM   3448 C CD2 . PHE B 2 218 ? 30.907 69.754 21.263 1.00 53.54  ?  373 PHE B CD2 1 
ATOM   3449 C CE1 . PHE B 2 218 ? 28.444 69.222 22.395 1.00 55.48  ?  373 PHE B CE1 1 
ATOM   3450 C CE2 . PHE B 2 218 ? 29.785 69.583 20.451 1.00 55.61  ?  373 PHE B CE2 1 
ATOM   3451 C CZ  . PHE B 2 218 ? 28.562 69.320 21.022 1.00 53.78  ?  373 PHE B CZ  1 
ATOM   3452 N N   . GLY B 2 219 ? 34.156 67.428 22.880 1.00 48.43  ?  374 GLY B N   1 
ATOM   3453 C CA  . GLY B 2 219 ? 34.694 66.369 22.032 1.00 48.40  ?  374 GLY B CA  1 
ATOM   3454 C C   . GLY B 2 219 ? 34.576 65.001 22.698 1.00 51.70  ?  374 GLY B C   1 
ATOM   3455 O O   . GLY B 2 219 ? 34.254 64.012 22.027 1.00 52.75  ?  374 GLY B O   1 
ATOM   3456 N N   . VAL B 2 220 ? 34.784 64.944 24.041 1.00 45.11  ?  375 VAL B N   1 
ATOM   3457 C CA  . VAL B 2 220 ? 34.662 63.727 24.855 1.00 43.73  ?  375 VAL B CA  1 
ATOM   3458 C C   . VAL B 2 220 ? 33.195 63.279 24.811 1.00 46.95  ?  375 VAL B C   1 
ATOM   3459 O O   . VAL B 2 220 ? 32.926 62.096 24.565 1.00 45.98  ?  375 VAL B O   1 
ATOM   3460 C CB  . VAL B 2 220 ? 35.172 63.919 26.302 1.00 46.70  ?  375 VAL B CB  1 
ATOM   3461 C CG1 . VAL B 2 220 ? 35.091 62.622 27.099 1.00 45.79  ?  375 VAL B CG1 1 
ATOM   3462 C CG2 . VAL B 2 220 ? 36.592 64.461 26.301 1.00 46.89  ?  375 VAL B CG2 1 
ATOM   3463 N N   . VAL B 2 221 ? 32.259 64.255 24.962 1.00 43.18  ?  376 VAL B N   1 
ATOM   3464 C CA  . VAL B 2 221 ? 30.816 64.049 24.883 1.00 42.67  ?  376 VAL B CA  1 
ATOM   3465 C C   . VAL B 2 221 ? 30.474 63.462 23.511 1.00 45.79  ?  376 VAL B C   1 
ATOM   3466 O O   . VAL B 2 221 ? 29.788 62.443 23.452 1.00 44.84  ?  376 VAL B O   1 
ATOM   3467 C CB  . VAL B 2 221 ? 30.003 65.329 25.226 1.00 47.11  ?  376 VAL B CB  1 
ATOM   3468 C CG1 . VAL B 2 221 ? 28.522 65.165 24.839 1.00 47.66  ?  376 VAL B CG1 1 
ATOM   3469 C CG2 . VAL B 2 221 ? 30.136 65.690 26.708 1.00 46.40  ?  376 VAL B CG2 1 
ATOM   3470 N N   . LEU B 2 222 ? 31.032 64.039 22.425 1.00 43.77  ?  377 LEU B N   1 
ATOM   3471 C CA  . LEU B 2 222 ? 30.797 63.528 21.076 1.00 45.08  ?  377 LEU B CA  1 
ATOM   3472 C C   . LEU B 2 222 ? 31.243 62.072 20.909 1.00 51.18  ?  377 LEU B C   1 
ATOM   3473 O O   . LEU B 2 222 ? 30.558 61.315 20.228 1.00 50.95  ?  377 LEU B O   1 
ATOM   3474 C CB  . LEU B 2 222 ? 31.409 64.428 19.985 1.00 45.44  ?  377 LEU B CB  1 
ATOM   3475 C CG  . LEU B 2 222 ? 30.828 65.830 19.844 1.00 50.07  ?  377 LEU B CG  1 
ATOM   3476 C CD1 . LEU B 2 222 ? 31.615 66.637 18.839 1.00 50.96  ?  377 LEU B CD1 1 
ATOM   3477 C CD2 . LEU B 2 222 ? 29.374 65.801 19.462 1.00 49.93  ?  377 LEU B CD2 1 
ATOM   3478 N N   . LEU B 2 223 ? 32.349 61.668 21.560 1.00 48.40  ?  378 LEU B N   1 
ATOM   3479 C CA  . LEU B 2 223 ? 32.804 60.276 21.490 1.00 47.92  ?  378 LEU B CA  1 
ATOM   3480 C C   . LEU B 2 223 ? 31.847 59.354 22.244 1.00 52.54  ?  378 LEU B C   1 
ATOM   3481 O O   . LEU B 2 223 ? 31.613 58.229 21.789 1.00 52.66  ?  378 LEU B O   1 
ATOM   3482 C CB  . LEU B 2 223 ? 34.235 60.076 22.003 1.00 47.26  ?  378 LEU B CB  1 
ATOM   3483 C CG  . LEU B 2 223 ? 35.378 60.828 21.325 1.00 51.70  ?  378 LEU B CG  1 
ATOM   3484 C CD1 . LEU B 2 223 ? 36.707 60.450 21.962 1.00 52.17  ?  378 LEU B CD1 1 
ATOM   3485 C CD2 . LEU B 2 223 ? 35.409 60.602 19.827 1.00 52.58  ?  378 LEU B CD2 1 
ATOM   3486 N N   . GLU B 2 224 ? 31.285 59.827 23.378 1.00 48.49  ?  379 GLU B N   1 
ATOM   3487 C CA  . GLU B 2 224 ? 30.313 59.045 24.156 1.00 47.32  ?  379 GLU B CA  1 
ATOM   3488 C C   . GLU B 2 224 ? 29.067 58.855 23.315 1.00 52.01  ?  379 GLU B C   1 
ATOM   3489 O O   . GLU B 2 224 ? 28.514 57.762 23.290 1.00 51.31  ?  379 GLU B O   1 
ATOM   3490 C CB  . GLU B 2 224 ? 29.945 59.736 25.469 1.00 48.27  ?  379 GLU B CB  1 
ATOM   3491 C CG  . GLU B 2 224 ? 31.106 59.975 26.420 1.00 53.97  ?  379 GLU B CG  1 
ATOM   3492 C CD  . GLU B 2 224 ? 30.663 60.700 27.672 1.00 76.40  ?  379 GLU B CD  1 
ATOM   3493 O OE1 . GLU B 2 224 ? 30.538 60.048 28.735 1.00 74.94  ?  379 GLU B OE1 1 
ATOM   3494 O OE2 . GLU B 2 224 ? 30.365 61.910 27.570 1.00 71.20  -1 379 GLU B OE2 1 
ATOM   3495 N N   . ILE B 2 225 ? 28.650 59.909 22.581 1.00 49.40  ?  380 ILE B N   1 
ATOM   3496 C CA  . ILE B 2 225 ? 27.491 59.856 21.691 1.00 48.59  ?  380 ILE B CA  1 
ATOM   3497 C C   . ILE B 2 225 ? 27.712 58.798 20.577 1.00 54.15  ?  380 ILE B C   1 
ATOM   3498 O O   . ILE B 2 225 ? 26.820 57.978 20.332 1.00 56.68  ?  380 ILE B O   1 
ATOM   3499 C CB  . ILE B 2 225 ? 27.112 61.271 21.156 1.00 51.04  ?  380 ILE B CB  1 
ATOM   3500 C CG1 . ILE B 2 225 ? 26.458 62.148 22.263 1.00 50.14  ?  380 ILE B CG1 1 
ATOM   3501 C CG2 . ILE B 2 225 ? 26.210 61.179 19.934 1.00 53.39  ?  380 ILE B CG2 1 
ATOM   3502 C CD1 . ILE B 2 225 ? 26.127 63.671 21.836 1.00 41.14  ?  380 ILE B CD1 1 
ATOM   3503 N N   . ILE B 2 226 ? 28.898 58.793 19.945 1.00 47.86  ?  381 ILE B N   1 
ATOM   3504 C CA  . ILE B 2 226 ? 29.226 57.857 18.866 1.00 46.80  ?  381 ILE B CA  1 
ATOM   3505 C C   . ILE B 2 226 ? 29.252 56.398 19.344 1.00 50.87  ?  381 ILE B C   1 
ATOM   3506 O O   . ILE B 2 226 ? 28.696 55.518 18.677 1.00 51.37  ?  381 ILE B O   1 
ATOM   3507 C CB  . ILE B 2 226 ? 30.565 58.259 18.159 1.00 49.45  ?  381 ILE B CB  1 
ATOM   3508 C CG1 . ILE B 2 226 ? 30.415 59.603 17.382 1.00 50.13  ?  381 ILE B CG1 1 
ATOM   3509 C CG2 . ILE B 2 226 ? 31.084 57.134 17.237 1.00 47.70  ?  381 ILE B CG2 1 
ATOM   3510 C CD1 . ILE B 2 226 ? 31.691 60.318 17.087 1.00 59.24  ?  381 ILE B CD1 1 
ATOM   3511 N N   . THR B 2 227 ? 29.921 56.152 20.478 1.00 45.22  ?  382 THR B N   1 
ATOM   3512 C CA  . THR B 2 227 ? 30.195 54.826 21.032 1.00 43.39  ?  382 THR B CA  1 
ATOM   3513 C C   . THR B 2 227 ? 29.178 54.275 22.006 1.00 46.95  ?  382 THR B C   1 
ATOM   3514 O O   . THR B 2 227 ? 29.140 53.061 22.215 1.00 46.25  ?  382 THR B O   1 
ATOM   3515 C CB  . THR B 2 227 ? 31.580 54.822 21.685 1.00 44.01  ?  382 THR B CB  1 
ATOM   3516 O OG1 . THR B 2 227 ? 31.574 55.699 22.815 1.00 43.35  ?  382 THR B OG1 1 
ATOM   3517 C CG2 . THR B 2 227 ? 32.680 55.227 20.729 1.00 42.67  ?  382 THR B CG2 1 
ATOM   3518 N N   . GLY B 2 228 ? 28.434 55.162 22.657 1.00 43.29  ?  383 GLY B N   1 
ATOM   3519 C CA  . GLY B 2 228 ? 27.498 54.789 23.707 1.00 42.44  ?  383 GLY B CA  1 
ATOM   3520 C C   . GLY B 2 228 ? 28.256 54.376 24.949 1.00 47.59  ?  383 GLY B C   1 
ATOM   3521 O O   . GLY B 2 228 ? 27.681 53.769 25.860 1.00 48.44  ?  383 GLY B O   1 
ATOM   3522 N N   . LEU B 2 229 ? 29.573 54.684 24.980 1.00 43.91  ?  384 LEU B N   1 
ATOM   3523 C CA  . LEU B 2 229 ? 30.462 54.336 26.083 1.00 44.49  ?  384 LEU B CA  1 
ATOM   3524 C C   . LEU B 2 229 ? 30.706 55.517 27.009 1.00 48.97  ?  384 LEU B C   1 
ATOM   3525 O O   . LEU B 2 229 ? 30.950 56.622 26.520 1.00 49.67  ?  384 LEU B O   1 
ATOM   3526 C CB  . LEU B 2 229 ? 31.825 53.833 25.564 1.00 44.87  ?  384 LEU B CB  1 
ATOM   3527 C CG  . LEU B 2 229 ? 31.874 52.518 24.802 1.00 48.93  ?  384 LEU B CG  1 
ATOM   3528 C CD1 . LEU B 2 229 ? 33.216 52.329 24.169 1.00 47.54  ?  384 LEU B CD1 1 
ATOM   3529 C CD2 . LEU B 2 229 ? 31.559 51.354 25.709 1.00 52.91  ?  384 LEU B CD2 1 
ATOM   3530 N N   . PRO B 2 230 ? 30.700 55.297 28.345 1.00 45.19  ?  385 PRO B N   1 
ATOM   3531 C CA  . PRO B 2 230 ? 31.025 56.399 29.263 1.00 44.96  ?  385 PRO B CA  1 
ATOM   3532 C C   . PRO B 2 230 ? 32.509 56.785 29.135 1.00 50.77  ?  385 PRO B C   1 
ATOM   3533 O O   . PRO B 2 230 ? 33.335 55.915 28.842 1.00 49.92  ?  385 PRO B O   1 
ATOM   3534 C CB  . PRO B 2 230 ? 30.695 55.822 30.638 1.00 46.17  ?  385 PRO B CB  1 
ATOM   3535 C CG  . PRO B 2 230 ? 30.743 54.360 30.479 1.00 50.13  ?  385 PRO B CG  1 
ATOM   3536 C CD  . PRO B 2 230 ? 30.438 54.035 29.071 1.00 46.10  ?  385 PRO B CD  1 
ATOM   3537 N N   . ALA B 2 231 ? 32.843 58.092 29.293 1.00 48.94  ?  386 ALA B N   1 
ATOM   3538 C CA  . ALA B 2 231 ? 34.217 58.618 29.189 1.00 49.41  ?  386 ALA B CA  1 
ATOM   3539 C C   . ALA B 2 231 ? 35.231 57.789 29.969 1.00 53.61  ?  386 ALA B C   1 
ATOM   3540 O O   . ALA B 2 231 ? 36.312 57.504 29.455 1.00 52.97  ?  386 ALA B O   1 
ATOM   3541 C CB  . ALA B 2 231 ? 34.276 60.066 29.636 1.00 50.02  ?  386 ALA B CB  1 
ATOM   3542 N N   . VAL B 2 232 ? 34.854 57.354 31.176 1.00 50.06  ?  387 VAL B N   1 
ATOM   3543 C CA  . VAL B 2 232 ? 35.686 56.489 31.984 1.00 50.17  ?  387 VAL B CA  1 
ATOM   3544 C C   . VAL B 2 232 ? 34.830 55.336 32.531 1.00 56.49  ?  387 VAL B C   1 
ATOM   3545 O O   . VAL B 2 232 ? 33.669 55.546 32.882 1.00 55.12  ?  387 VAL B O   1 
ATOM   3546 C CB  . VAL B 2 232 ? 36.501 57.265 33.070 1.00 52.93  ?  387 VAL B CB  1 
ATOM   3547 C CG1 . VAL B 2 232 ? 35.619 57.747 34.233 1.00 51.71  ?  387 VAL B CG1 1 
ATOM   3548 C CG2 . VAL B 2 232 ? 37.665 56.428 33.586 1.00 52.70  ?  387 VAL B CG2 1 
ATOM   3549 N N   . ASP B 2 233 ? 35.391 54.123 32.541 1.00 56.14  ?  388 ASP B N   1 
ATOM   3550 C CA  . ASP B 2 233 ? 34.741 52.919 33.060 1.00 57.58  ?  388 ASP B CA  1 
ATOM   3551 C C   . ASP B 2 233 ? 35.816 52.051 33.721 1.00 65.17  ?  388 ASP B C   1 
ATOM   3552 O O   . ASP B 2 233 ? 36.713 51.554 33.037 1.00 64.05  ?  388 ASP B O   1 
ATOM   3553 C CB  . ASP B 2 233 ? 33.992 52.163 31.945 1.00 59.15  ?  388 ASP B CB  1 
ATOM   3554 C CG  . ASP B 2 233 ? 33.228 50.916 32.388 1.00 69.32  ?  388 ASP B CG  1 
ATOM   3555 O OD1 . ASP B 2 233 ? 33.323 50.550 33.587 1.00 69.71  ?  388 ASP B OD1 1 
ATOM   3556 O OD2 . ASP B 2 233 ? 32.536 50.299 31.530 1.00 71.80  -1 388 ASP B OD2 1 
ATOM   3557 N N   . GLU B 2 234 ? 35.741 51.918 35.061 1.00 64.48  ?  389 GLU B N   1 
ATOM   3558 C CA  . GLU B 2 234 ? 36.711 51.167 35.865 1.00 65.38  ?  389 GLU B CA  1 
ATOM   3559 C C   . GLU B 2 234 ? 36.815 49.694 35.457 1.00 70.94  ?  389 GLU B C   1 
ATOM   3560 O O   . GLU B 2 234 ? 37.909 49.138 35.463 1.00 72.41  ?  389 GLU B O   1 
ATOM   3561 C CB  . GLU B 2 234 ? 36.395 51.299 37.362 1.00 66.82  ?  389 GLU B CB  1 
ATOM   3562 N N   . HIS B 2 235 ? 35.692 49.086 35.056 1.00 66.26  ?  390 HIS B N   1 
ATOM   3563 C CA  . HIS B 2 235 ? 35.639 47.687 34.654 1.00 65.49  ?  390 HIS B CA  1 
ATOM   3564 C C   . HIS B 2 235 ? 35.708 47.489 33.123 1.00 66.52  ?  390 HIS B C   1 
ATOM   3565 O O   . HIS B 2 235 ? 35.096 46.554 32.595 1.00 67.13  ?  390 HIS B O   1 
ATOM   3566 C CB  . HIS B 2 235 ? 34.395 47.036 35.279 1.00 66.81  ?  390 HIS B CB  1 
ATOM   3567 C CG  . HIS B 2 235 ? 34.326 47.230 36.762 1.00 70.74  ?  390 HIS B CG  1 
ATOM   3568 N ND1 . HIS B 2 235 ? 35.156 46.531 37.619 1.00 72.74  ?  390 HIS B ND1 1 
ATOM   3569 C CD2 . HIS B 2 235 ? 33.563 48.081 37.489 1.00 72.86  ?  390 HIS B CD2 1 
ATOM   3570 C CE1 . HIS B 2 235 ? 34.856 46.956 38.834 1.00 72.31  ?  390 HIS B CE1 1 
ATOM   3571 N NE2 . HIS B 2 235 ? 33.900 47.888 38.806 1.00 72.57  ?  390 HIS B NE2 1 
ATOM   3572 N N   . ARG B 2 236 ? 36.493 48.340 32.425 1.00 59.86  ?  391 ARG B N   1 
ATOM   3573 C CA  . ARG B 2 236 ? 36.650 48.309 30.971 1.00 59.12  ?  391 ARG B CA  1 
ATOM   3574 C C   . ARG B 2 236 ? 38.106 48.426 30.542 1.00 63.40  ?  391 ARG B C   1 
ATOM   3575 O O   . ARG B 2 236 ? 38.911 49.034 31.244 1.00 62.11  ?  391 ARG B O   1 
ATOM   3576 C CB  . ARG B 2 236 ? 35.825 49.447 30.352 1.00 60.24  ?  391 ARG B CB  1 
ATOM   3577 C CG  . ARG B 2 236 ? 35.680 49.430 28.823 1.00 71.06  ?  391 ARG B CG  1 
ATOM   3578 C CD  . ARG B 2 236 ? 34.907 50.629 28.293 1.00 74.45  ?  391 ARG B CD  1 
ATOM   3579 N NE  . ARG B 2 236 ? 35.606 51.898 28.509 1.00 79.36  ?  391 ARG B NE  1 
ATOM   3580 C CZ  . ARG B 2 236 ? 35.011 53.087 28.570 1.00 89.59  ?  391 ARG B CZ  1 
ATOM   3581 N NH1 . ARG B 2 236 ? 35.729 54.185 28.762 1.00 68.44  ?  391 ARG B NH1 1 
ATOM   3582 N NH2 . ARG B 2 236 ? 33.693 53.188 28.442 1.00 83.67  1  391 ARG B NH2 1 
ATOM   3583 N N   . GLU B 2 237 ? 38.439 47.842 29.377 1.00 61.16  ?  392 GLU B N   1 
ATOM   3584 C CA  . GLU B 2 237 ? 39.769 47.891 28.778 1.00 61.09  ?  392 GLU B CA  1 
ATOM   3585 C C   . GLU B 2 237 ? 39.647 48.501 27.357 1.00 66.68  ?  392 GLU B C   1 
ATOM   3586 O O   . GLU B 2 237 ? 39.082 47.866 26.447 1.00 65.36  ?  392 GLU B O   1 
ATOM   3587 C CB  . GLU B 2 237 ? 40.435 46.504 28.762 1.00 62.48  ?  392 GLU B CB  1 
ATOM   3588 N N   . PRO B 2 238 ? 40.110 49.761 27.145 1.00 64.53  ?  393 PRO B N   1 
ATOM   3589 C CA  . PRO B 2 238 ? 40.766 50.671 28.105 1.00 63.95  ?  393 PRO B CA  1 
ATOM   3590 C C   . PRO B 2 238 ? 39.766 51.377 29.003 1.00 66.33  ?  393 PRO B C   1 
ATOM   3591 O O   . PRO B 2 238 ? 38.628 51.581 28.584 1.00 66.17  ?  393 PRO B O   1 
ATOM   3592 C CB  . PRO B 2 238 ? 41.469 51.696 27.196 1.00 66.04  ?  393 PRO B CB  1 
ATOM   3593 C CG  . PRO B 2 238 ? 41.198 51.264 25.746 1.00 71.18  ?  393 PRO B CG  1 
ATOM   3594 C CD  . PRO B 2 238 ? 39.997 50.388 25.812 1.00 66.85  ?  393 PRO B CD  1 
ATOM   3595 N N   . GLN B 2 239 ? 40.196 51.779 30.217 1.00 61.69  ?  394 GLN B N   1 
ATOM   3596 C CA  . GLN B 2 239 ? 39.344 52.490 31.173 1.00 61.21  ?  394 GLN B CA  1 
ATOM   3597 C C   . GLN B 2 239 ? 38.796 53.794 30.578 1.00 65.24  ?  394 GLN B C   1 
ATOM   3598 O O   . GLN B 2 239 ? 37.617 54.100 30.745 1.00 66.65  ?  394 GLN B O   1 
ATOM   3599 C CB  . GLN B 2 239 ? 40.098 52.833 32.468 1.00 62.44  ?  394 GLN B CB  1 
ATOM   3600 C CG  . GLN B 2 239 ? 40.775 51.670 33.175 1.00 82.72  ?  394 GLN B CG  1 
ATOM   3601 C CD  . GLN B 2 239 ? 40.563 51.630 34.682 1.00 106.41 ?  394 GLN B CD  1 
ATOM   3602 O OE1 . GLN B 2 239 ? 40.095 52.585 35.342 1.00 97.09  ?  394 GLN B OE1 1 
ATOM   3603 N NE2 . GLN B 2 239 ? 40.885 50.481 35.264 1.00 101.75 ?  394 GLN B NE2 1 
ATOM   3604 N N   . LEU B 2 240 ? 39.657 54.547 29.885 1.00 59.56  ?  395 LEU B N   1 
ATOM   3605 C CA  . LEU B 2 240 ? 39.371 55.850 29.309 1.00 58.81  ?  395 LEU B CA  1 
ATOM   3606 C C   . LEU B 2 240 ? 39.054 55.788 27.837 1.00 60.28  ?  395 LEU B C   1 
ATOM   3607 O O   . LEU B 2 240 ? 39.798 55.195 27.049 1.00 58.96  ?  395 LEU B O   1 
ATOM   3608 C CB  . LEU B 2 240 ? 40.584 56.768 29.519 1.00 59.65  ?  395 LEU B CB  1 
ATOM   3609 C CG  . LEU B 2 240 ? 40.615 57.655 30.770 1.00 65.42  ?  395 LEU B CG  1 
ATOM   3610 C CD1 . LEU B 2 240 ? 40.786 56.845 32.026 1.00 66.76  ?  395 LEU B CD1 1 
ATOM   3611 C CD2 . LEU B 2 240 ? 41.771 58.608 30.692 1.00 68.91  ?  395 LEU B CD2 1 
ATOM   3612 N N   . LEU B 2 241 ? 37.972 56.476 27.463 1.00 56.20  ?  396 LEU B N   1 
ATOM   3613 C CA  . LEU B 2 241 ? 37.487 56.601 26.095 1.00 56.01  ?  396 LEU B CA  1 
ATOM   3614 C C   . LEU B 2 241 ? 38.487 57.388 25.227 1.00 61.14  ?  396 LEU B C   1 
ATOM   3615 O O   . LEU B 2 241 ? 38.504 57.220 24.013 1.00 59.08  ?  396 LEU B O   1 
ATOM   3616 C CB  . LEU B 2 241 ? 36.101 57.286 26.135 1.00 55.85  ?  396 LEU B CB  1 
ATOM   3617 C CG  . LEU B 2 241 ? 35.238 57.292 24.880 1.00 59.23  ?  396 LEU B CG  1 
ATOM   3618 C CD1 . LEU B 2 241 ? 34.859 55.886 24.455 1.00 59.20  ?  396 LEU B CD1 1 
ATOM   3619 C CD2 . LEU B 2 241 ? 34.007 58.067 25.121 1.00 60.75  ?  396 LEU B CD2 1 
ATOM   3620 N N   . LEU B 2 242 ? 39.331 58.233 25.851 1.00 61.39  ?  397 LEU B N   1 
ATOM   3621 C CA  . LEU B 2 242 ? 40.346 58.994 25.119 1.00 62.42  ?  397 LEU B CA  1 
ATOM   3622 C C   . LEU B 2 242 ? 41.456 58.087 24.569 1.00 72.44  ?  397 LEU B C   1 
ATOM   3623 O O   . LEU B 2 242 ? 41.995 58.388 23.502 1.00 72.28  ?  397 LEU B O   1 
ATOM   3624 C CB  . LEU B 2 242 ? 40.908 60.154 25.947 1.00 61.69  ?  397 LEU B CB  1 
ATOM   3625 C CG  . LEU B 2 242 ? 40.028 61.391 26.032 1.00 64.37  ?  397 LEU B CG  1 
ATOM   3626 C CD1 . LEU B 2 242 ? 40.464 62.290 27.160 1.00 63.52  ?  397 LEU B CD1 1 
ATOM   3627 C CD2 . LEU B 2 242 ? 40.014 62.160 24.728 1.00 64.62  ?  397 LEU B CD2 1 
ATOM   3628 N N   . ASP B 2 243 ? 41.743 56.943 25.257 1.00 73.08  ?  398 ASP B N   1 
ATOM   3629 C CA  . ASP B 2 243 ? 42.716 55.925 24.821 1.00 73.91  ?  398 ASP B CA  1 
ATOM   3630 C C   . ASP B 2 243 ? 42.255 55.274 23.516 1.00 79.89  ?  398 ASP B C   1 
ATOM   3631 O O   . ASP B 2 243 ? 43.092 54.888 22.706 1.00 80.14  ?  398 ASP B O   1 
ATOM   3632 C CB  . ASP B 2 243 ? 42.899 54.833 25.882 1.00 75.79  ?  398 ASP B CB  1 
ATOM   3633 C CG  . ASP B 2 243 ? 43.287 55.301 27.277 1.00 88.44  ?  398 ASP B CG  1 
ATOM   3634 O OD1 . ASP B 2 243 ? 44.039 56.295 27.385 1.00 89.57  ?  398 ASP B OD1 1 
ATOM   3635 O OD2 . ASP B 2 243 ? 42.894 54.627 28.262 1.00 95.49  -1 398 ASP B OD2 1 
ATOM   3636 N N   . ILE B 2 244 ? 40.928 55.153 23.312 1.00 78.21  ?  399 ILE B N   1 
ATOM   3637 C CA  . ILE B 2 244 ? 40.382 54.595 22.070 1.00 78.75  ?  399 ILE B CA  1 
ATOM   3638 C C   . ILE B 2 244 ? 40.539 55.607 20.920 1.00 84.90  ?  399 ILE B C   1 
ATOM   3639 O O   . ILE B 2 244 ? 40.624 55.196 19.763 1.00 84.93  ?  399 ILE B O   1 
ATOM   3640 C CB  . ILE B 2 244 ? 38.963 53.915 22.174 1.00 81.34  ?  399 ILE B CB  1 
ATOM   3641 C CG1 . ILE B 2 244 ? 37.787 54.900 21.976 1.00 81.83  ?  399 ILE B CG1 1 
ATOM   3642 C CG2 . ILE B 2 244 ? 38.797 53.073 23.448 1.00 80.85  ?  399 ILE B CG2 1 
ATOM   3643 C CD1 . ILE B 2 244 ? 37.133 54.877 20.631 1.00 86.56  ?  399 ILE B CD1 1 
ATOM   3644 N N   . LYS B 2 245 ? 40.596 56.924 21.242 1.00 83.23  ?  400 LYS B N   1 
ATOM   3645 C CA  . LYS B 2 245 ? 40.804 57.981 20.243 1.00 84.08  ?  400 LYS B CA  1 
ATOM   3646 C C   . LYS B 2 245 ? 42.226 57.876 19.714 1.00 91.11  ?  400 LYS B C   1 
ATOM   3647 O O   . LYS B 2 245 ? 42.435 58.063 18.511 1.00 91.39  ?  400 LYS B O   1 
ATOM   3648 C CB  . LYS B 2 245 ? 40.540 59.379 20.815 1.00 85.90  ?  400 LYS B CB  1 
ATOM   3649 N N   . GLU B 2 246 ? 43.193 57.519 20.606 1.00 89.31  ?  401 GLU B N   1 
ATOM   3650 C CA  . GLU B 2 246 ? 44.611 57.295 20.287 1.00 90.00  ?  401 GLU B CA  1 
ATOM   3651 C C   . GLU B 2 246 ? 44.745 56.117 19.306 1.00 95.25  ?  401 GLU B C   1 
ATOM   3652 O O   . GLU B 2 246 ? 45.392 56.262 18.266 1.00 94.70  ?  401 GLU B O   1 
ATOM   3653 C CB  . GLU B 2 246 ? 45.424 57.038 21.569 1.00 91.44  ?  401 GLU B CB  1 
ATOM   3654 N N   . GLU B 2 247 ? 44.062 54.983 19.614 1.00 92.74  ?  402 GLU B N   1 
ATOM   3655 C CA  . GLU B 2 247 ? 44.003 53.765 18.804 1.00 92.97  ?  402 GLU B CA  1 
ATOM   3656 C C   . GLU B 2 247 ? 43.475 54.016 17.381 1.00 98.96  ?  402 GLU B C   1 
ATOM   3657 O O   . GLU B 2 247 ? 43.894 53.324 16.458 1.00 99.11  ?  402 GLU B O   1 
ATOM   3658 C CB  . GLU B 2 247 ? 43.154 52.704 19.513 1.00 94.29  ?  402 GLU B CB  1 
ATOM   3659 N N   . ILE B 2 248 ? 42.571 54.999 17.202 1.00 97.00  ?  403 ILE B N   1 
ATOM   3660 C CA  . ILE B 2 248 ? 42.025 55.347 15.888 1.00 98.01  ?  403 ILE B CA  1 
ATOM   3661 C C   . ILE B 2 248 ? 43.066 56.144 15.096 1.00 104.15 ?  403 ILE B C   1 
ATOM   3662 O O   . ILE B 2 248 ? 43.339 55.811 13.939 1.00 103.75 ?  403 ILE B O   1 
ATOM   3663 C CB  . ILE B 2 248 ? 40.628 56.048 15.973 1.00 101.36 ?  403 ILE B CB  1 
ATOM   3664 C CG1 . ILE B 2 248 ? 39.570 55.095 16.586 1.00 102.08 ?  403 ILE B CG1 1 
ATOM   3665 C CG2 . ILE B 2 248 ? 40.157 56.558 14.590 1.00 101.64 ?  403 ILE B CG2 1 
ATOM   3666 C CD1 . ILE B 2 248 ? 38.353 55.779 17.217 1.00 110.83 ?  403 ILE B CD1 1 
ATOM   3667 N N   . GLU B 2 249 ? 43.666 57.173 15.731 1.00 102.13 ?  404 GLU B N   1 
ATOM   3668 C CA  . GLU B 2 249 ? 44.702 58.006 15.113 1.00 102.40 ?  404 GLU B CA  1 
ATOM   3669 C C   . GLU B 2 249 ? 45.955 57.171 14.758 1.00 106.43 ?  404 GLU B C   1 
ATOM   3670 O O   . GLU B 2 249 ? 46.591 57.423 13.729 1.00 106.38 ?  404 GLU B O   1 
ATOM   3671 C CB  . GLU B 2 249 ? 45.066 59.188 16.034 1.00 103.77 ?  404 GLU B CB  1 
ATOM   3672 N N   . ASP B 2 250 ? 46.259 56.140 15.588 1.00 102.09 ?  405 ASP B N   1 
ATOM   3673 C CA  . ASP B 2 250 ? 47.421 55.258 15.428 1.00 101.20 ?  405 ASP B CA  1 
ATOM   3674 C C   . ASP B 2 250 ? 47.116 53.944 14.683 1.00 103.50 ?  405 ASP B C   1 
ATOM   3675 O O   . ASP B 2 250 ? 47.791 52.935 14.909 1.00 102.67 ?  405 ASP B O   1 
ATOM   3676 C CB  . ASP B 2 250 ? 48.107 55.003 16.789 1.00 102.93 ?  405 ASP B CB  1 
ATOM   3677 C CG  . ASP B 2 250 ? 48.807 56.204 17.399 1.00 115.01 ?  405 ASP B CG  1 
ATOM   3678 O OD1 . ASP B 2 250 ? 48.837 57.278 16.744 1.00 115.45 ?  405 ASP B OD1 1 
ATOM   3679 O OD2 . ASP B 2 250 ? 49.340 56.070 18.525 1.00 122.03 -1 405 ASP B OD2 1 
ATOM   3680 N N   . GLU B 2 251 ? 46.097 53.970 13.787 1.00 98.98  ?  406 GLU B N   1 
ATOM   3681 C CA  . GLU B 2 251 ? 45.629 52.866 12.930 1.00 97.95  ?  406 GLU B CA  1 
ATOM   3682 C C   . GLU B 2 251 ? 45.444 51.463 13.562 1.00 98.88  ?  406 GLU B C   1 
ATOM   3683 O O   . GLU B 2 251 ? 45.141 50.513 12.836 1.00 98.55  ?  406 GLU B O   1 
ATOM   3684 C CB  . GLU B 2 251 ? 46.433 52.808 11.618 1.00 99.54  ?  406 GLU B CB  1 
ATOM   3685 C CG  . GLU B 2 251 ? 45.588 52.961 10.358 1.00 113.67 ?  406 GLU B CG  1 
ATOM   3686 C CD  . GLU B 2 251 ? 44.776 51.752 9.916  1.00 139.01 ?  406 GLU B CD  1 
ATOM   3687 O OE1 . GLU B 2 251 ? 45.227 51.036 8.991  1.00 130.21 ?  406 GLU B OE1 1 
ATOM   3688 O OE2 . GLU B 2 251 ? 43.666 51.548 10.461 1.00 134.03 -1 406 GLU B OE2 1 
ATOM   3689 N N   . GLU B 2 252 ? 45.582 51.340 14.903 1.00 93.44  ?  407 GLU B N   1 
ATOM   3690 C CA  . GLU B 2 252 ? 45.420 50.082 15.645 1.00 92.63  ?  407 GLU B CA  1 
ATOM   3691 C C   . GLU B 2 252 ? 43.952 49.608 15.676 1.00 95.70  ?  407 GLU B C   1 
ATOM   3692 O O   . GLU B 2 252 ? 43.687 48.435 15.948 1.00 95.60  ?  407 GLU B O   1 
ATOM   3693 C CB  . GLU B 2 252 ? 45.993 50.207 17.065 1.00 93.91  ?  407 GLU B CB  1 
ATOM   3694 N N   . LYS B 2 253 ? 43.010 50.539 15.392 1.00 91.02  ?  408 LYS B N   1 
ATOM   3695 C CA  . LYS B 2 253 ? 41.552 50.367 15.311 1.00 89.76  ?  408 LYS B CA  1 
ATOM   3696 C C   . LYS B 2 253 ? 40.956 51.535 14.491 1.00 90.96  ?  408 LYS B C   1 
ATOM   3697 O O   . LYS B 2 253 ? 41.658 52.514 14.225 1.00 91.27  ?  408 LYS B O   1 
ATOM   3698 C CB  . LYS B 2 253 ? 40.932 50.317 16.724 1.00 92.29  ?  408 LYS B CB  1 
ATOM   3699 N N   . THR B 2 254 ? 39.680 51.429 14.077 1.00 85.01  ?  409 THR B N   1 
ATOM   3700 C CA  . THR B 2 254 ? 38.968 52.495 13.346 1.00 83.60  ?  409 THR B CA  1 
ATOM   3701 C C   . THR B 2 254 ? 37.712 52.970 14.115 1.00 84.22  ?  409 THR B C   1 
ATOM   3702 O O   . THR B 2 254 ? 37.388 52.394 15.162 1.00 84.21  ?  409 THR B O   1 
ATOM   3703 C CB  . THR B 2 254 ? 38.723 52.125 11.869 1.00 92.16  ?  409 THR B CB  1 
ATOM   3704 O OG1 . THR B 2 254 ? 38.120 53.244 11.211 1.00 94.08  ?  409 THR B OG1 1 
ATOM   3705 C CG2 . THR B 2 254 ? 37.840 50.887 11.695 1.00 89.62  ?  409 THR B CG2 1 
ATOM   3706 N N   . ILE B 2 255 ? 37.021 54.022 13.618 1.00 77.48  ?  410 ILE B N   1 
ATOM   3707 C CA  . ILE B 2 255 ? 35.814 54.505 14.280 1.00 76.14  ?  410 ILE B CA  1 
ATOM   3708 C C   . ILE B 2 255 ? 34.677 53.487 14.208 1.00 79.97  ?  410 ILE B C   1 
ATOM   3709 O O   . ILE B 2 255 ? 33.965 53.300 15.201 1.00 79.93  ?  410 ILE B O   1 
ATOM   3710 C CB  . ILE B 2 255 ? 35.414 55.966 13.932 1.00 78.84  ?  410 ILE B CB  1 
ATOM   3711 C CG1 . ILE B 2 255 ? 34.333 56.539 14.903 1.00 79.17  ?  410 ILE B CG1 1 
ATOM   3712 C CG2 . ILE B 2 255 ? 35.002 56.141 12.472 1.00 78.96  ?  410 ILE B CG2 1 
ATOM   3713 C CD1 . ILE B 2 255 ? 34.684 56.500 16.464 1.00 83.50  ?  410 ILE B CD1 1 
ATOM   3714 N N   . GLU B 2 256 ? 34.580 52.758 13.067 1.00 75.45  ?  411 GLU B N   1 
ATOM   3715 C CA  . GLU B 2 256 ? 33.591 51.705 12.820 1.00 74.14  ?  411 GLU B CA  1 
ATOM   3716 C C   . GLU B 2 256 ? 33.710 50.582 13.839 1.00 75.40  ?  411 GLU B C   1 
ATOM   3717 O O   . GLU B 2 256 ? 32.700 49.980 14.198 1.00 75.22  ?  411 GLU B O   1 
ATOM   3718 C CB  . GLU B 2 256 ? 33.710 51.169 11.391 1.00 75.65  ?  411 GLU B CB  1 
ATOM   3719 N N   . ASP B 2 257 ? 34.931 50.344 14.354 1.00 70.50  ?  412 ASP B N   1 
ATOM   3720 C CA  . ASP B 2 257 ? 35.211 49.336 15.378 1.00 70.44  ?  412 ASP B CA  1 
ATOM   3721 C C   . ASP B 2 257 ? 34.615 49.744 16.728 1.00 72.09  ?  412 ASP B C   1 
ATOM   3722 O O   . ASP B 2 257 ? 34.623 48.940 17.671 1.00 71.75  ?  412 ASP B O   1 
ATOM   3723 C CB  . ASP B 2 257 ? 36.738 49.123 15.536 1.00 73.07  ?  412 ASP B CB  1 
ATOM   3724 C CG  . ASP B 2 257 ? 37.473 48.545 14.333 1.00 91.39  ?  412 ASP B CG  1 
ATOM   3725 O OD1 . ASP B 2 257 ? 36.827 47.857 13.506 1.00 93.05  ?  412 ASP B OD1 1 
ATOM   3726 O OD2 . ASP B 2 257 ? 38.700 48.754 14.233 1.00 100.98 -1 412 ASP B OD2 1 
ATOM   3727 N N   . TYR B 2 258 ? 34.130 50.999 16.830 1.00 66.23  ?  413 TYR B N   1 
ATOM   3728 C CA  . TYR B 2 258 ? 33.584 51.532 18.061 1.00 64.78  ?  413 TYR B CA  1 
ATOM   3729 C C   . TYR B 2 258 ? 32.175 52.140 17.981 1.00 64.16  ?  413 TYR B C   1 
ATOM   3730 O O   . TYR B 2 258 ? 31.602 52.425 19.034 1.00 63.87  ?  413 TYR B O   1 
ATOM   3731 C CB  . TYR B 2 258 ? 34.609 52.460 18.725 1.00 66.72  ?  413 TYR B CB  1 
ATOM   3732 C CG  . TYR B 2 258 ? 35.752 51.707 19.373 1.00 69.50  ?  413 TYR B CG  1 
ATOM   3733 C CD1 . TYR B 2 258 ? 35.563 50.992 20.553 1.00 71.73  ?  413 TYR B CD1 1 
ATOM   3734 C CD2 . TYR B 2 258 ? 37.023 51.706 18.806 1.00 70.58  ?  413 TYR B CD2 1 
ATOM   3735 C CE1 . TYR B 2 258 ? 36.608 50.294 21.154 1.00 73.55  ?  413 TYR B CE1 1 
ATOM   3736 C CE2 . TYR B 2 258 ? 38.079 51.009 19.399 1.00 71.86  ?  413 TYR B CE2 1 
ATOM   3737 C CZ  . TYR B 2 258 ? 37.868 50.307 20.578 1.00 81.58  ?  413 TYR B CZ  1 
ATOM   3738 O OH  . TYR B 2 258 ? 38.900 49.642 21.213 1.00 84.05  ?  413 TYR B OH  1 
ATOM   3739 N N   . ILE B 2 259 ? 31.596 52.294 16.766 1.00 57.29  ?  414 ILE B N   1 
ATOM   3740 C CA  . ILE B 2 259 ? 30.230 52.829 16.599 1.00 56.00  ?  414 ILE B CA  1 
ATOM   3741 C C   . ILE B 2 259 ? 29.261 52.000 17.441 1.00 58.24  ?  414 ILE B C   1 
ATOM   3742 O O   . ILE B 2 259 ? 29.301 50.774 17.375 1.00 58.59  ?  414 ILE B O   1 
ATOM   3743 C CB  . ILE B 2 259 ? 29.735 52.940 15.125 1.00 58.37  ?  414 ILE B CB  1 
ATOM   3744 C CG1 . ILE B 2 259 ? 30.746 53.664 14.214 1.00 59.57  ?  414 ILE B CG1 1 
ATOM   3745 C CG2 . ILE B 2 259 ? 28.360 53.621 15.067 1.00 56.75  ?  414 ILE B CG2 1 
ATOM   3746 C CD1 . ILE B 2 259 ? 30.402 53.608 12.678 1.00 74.19  ?  414 ILE B CD1 1 
ATOM   3747 N N   . ASP B 2 260 ? 28.431 52.677 18.254 1.00 52.21  ?  415 ASP B N   1 
ATOM   3748 C CA  . ASP B 2 260 ? 27.462 52.043 19.132 1.00 50.80  ?  415 ASP B CA  1 
ATOM   3749 C C   . ASP B 2 260 ? 26.591 51.034 18.374 1.00 53.28  ?  415 ASP B C   1 
ATOM   3750 O O   . ASP B 2 260 ? 25.858 51.389 17.448 1.00 53.19  ?  415 ASP B O   1 
ATOM   3751 C CB  . ASP B 2 260 ? 26.603 53.106 19.849 1.00 51.72  ?  415 ASP B CB  1 
ATOM   3752 C CG  . ASP B 2 260 ? 25.733 52.606 20.985 1.00 49.64  ?  415 ASP B CG  1 
ATOM   3753 O OD1 . ASP B 2 260 ? 25.750 51.368 21.264 1.00 47.64  ?  415 ASP B OD1 1 
ATOM   3754 O OD2 . ASP B 2 260 ? 25.037 53.437 21.598 1.00 49.95  -1 415 ASP B OD2 1 
ATOM   3755 N N   . LYS B 2 261 ? 26.688 49.774 18.781 1.00 48.86  ?  416 LYS B N   1 
ATOM   3756 C CA  . LYS B 2 261 ? 25.937 48.668 18.188 1.00 48.37  ?  416 LYS B CA  1 
ATOM   3757 C C   . LYS B 2 261 ? 24.426 48.740 18.497 1.00 51.86  ?  416 LYS B C   1 
ATOM   3758 O O   . LYS B 2 261 ? 23.617 48.124 17.784 1.00 50.62  ?  416 LYS B O   1 
ATOM   3759 C CB  . LYS B 2 261 ? 26.556 47.317 18.598 1.00 50.40  ?  416 LYS B CB  1 
ATOM   3760 C CG  . LYS B 2 261 ? 27.867 47.033 17.885 1.00 54.64  ?  416 LYS B CG  1 
ATOM   3761 C CD  . LYS B 2 261 ? 28.512 45.745 18.352 1.00 59.95  ?  416 LYS B CD  1 
ATOM   3762 C CE  . LYS B 2 261 ? 29.697 45.375 17.484 1.00 73.42  ?  416 LYS B CE  1 
ATOM   3763 N NZ  . LYS B 2 261 ? 29.285 45.027 16.090 1.00 87.12  1  416 LYS B NZ  1 
ATOM   3764 N N   . LYS B 2 262 ? 24.047 49.543 19.521 1.00 48.87  ?  417 LYS B N   1 
ATOM   3765 C CA  . LYS B 2 262 ? 22.653 49.759 19.933 1.00 49.18  ?  417 LYS B CA  1 
ATOM   3766 C C   . LYS B 2 262 ? 21.895 50.790 19.037 1.00 56.43  ?  417 LYS B C   1 
ATOM   3767 O O   . LYS B 2 262 ? 20.902 51.363 19.465 1.00 56.94  ?  417 LYS B O   1 
ATOM   3768 C CB  . LYS B 2 262 ? 22.558 50.153 21.426 1.00 50.01  ?  417 LYS B CB  1 
ATOM   3769 C CG  . LYS B 2 262 ? 23.017 49.078 22.393 1.00 52.91  ?  417 LYS B CG  1 
ATOM   3770 C CD  . LYS B 2 262 ? 22.946 49.514 23.871 1.00 55.93  ?  417 LYS B CD  1 
ATOM   3771 C CE  . LYS B 2 262 ? 23.971 50.553 24.274 1.00 63.16  ?  417 LYS B CE  1 
ATOM   3772 N NZ  . LYS B 2 262 ? 25.367 50.036 24.255 1.00 64.51  1  417 LYS B NZ  1 
ATOM   3773 N N   . MET B 2 263 ? 22.353 51.019 17.804 1.00 54.48  ?  418 MET B N   1 
ATOM   3774 C CA  . MET B 2 263 ? 21.690 51.945 16.886 1.00 53.65  ?  418 MET B CA  1 
ATOM   3775 C C   . MET B 2 263 ? 21.176 51.188 15.684 1.00 62.33  ?  418 MET B C   1 
ATOM   3776 O O   . MET B 2 263 ? 21.803 50.211 15.265 1.00 62.89  ?  418 MET B O   1 
ATOM   3777 C CB  . MET B 2 263 ? 22.623 53.083 16.473 1.00 54.81  ?  418 MET B CB  1 
ATOM   3778 C CG  . MET B 2 263 ? 22.923 54.030 17.595 1.00 57.25  ?  418 MET B CG  1 
ATOM   3779 S SD  . MET B 2 263 ? 23.762 55.538 17.056 1.00 60.39  ?  418 MET B SD  1 
ATOM   3780 C CE  . MET B 2 263 ? 25.394 54.964 16.838 1.00 56.01  ?  418 MET B CE  1 
ATOM   3781 N N   . ASN B 2 264 ? 20.015 51.652 15.149 1.00 62.49  ?  419 ASN B N   1 
ATOM   3782 C CA  . ASN B 2 264 ? 19.229 51.115 14.020 1.00 64.10  ?  419 ASN B CA  1 
ATOM   3783 C C   . ASN B 2 264 ? 19.049 52.126 12.852 1.00 70.91  ?  419 ASN B C   1 
ATOM   3784 O O   . ASN B 2 264 ? 18.232 51.880 11.956 1.00 71.89  ?  419 ASN B O   1 
ATOM   3785 C CB  . ASN B 2 264 ? 17.815 50.755 14.536 1.00 66.59  ?  419 ASN B CB  1 
ATOM   3786 C CG  . ASN B 2 264 ? 17.020 51.955 15.063 1.00 89.30  ?  419 ASN B CG  1 
ATOM   3787 O OD1 . ASN B 2 264 ? 17.497 52.751 15.894 1.00 89.31  ?  419 ASN B OD1 1 
ATOM   3788 N ND2 . ASN B 2 264 ? 15.791 52.124 14.584 1.00 70.71  ?  419 ASN B ND2 1 
ATOM   3789 N N   . ASP B 2 265 ? 19.752 53.266 12.881 1.00 67.51  ?  420 ASP B N   1 
ATOM   3790 C CA  . ASP B 2 265 ? 19.627 54.342 11.891 1.00 67.18  ?  420 ASP B CA  1 
ATOM   3791 C C   . ASP B 2 265 ? 20.963 55.031 11.643 1.00 70.98  ?  420 ASP B C   1 
ATOM   3792 O O   . ASP B 2 265 ? 21.026 56.048 10.929 1.00 69.63  ?  420 ASP B O   1 
ATOM   3793 C CB  . ASP B 2 265 ? 18.562 55.351 12.360 1.00 68.72  ?  420 ASP B CB  1 
ATOM   3794 C CG  . ASP B 2 265 ? 18.846 56.009 13.700 1.00 74.90  ?  420 ASP B CG  1 
ATOM   3795 O OD1 . ASP B 2 265 ? 19.242 55.296 14.643 1.00 76.64  ?  420 ASP B OD1 1 
ATOM   3796 O OD2 . ASP B 2 265 ? 18.644 57.228 13.811 1.00 77.02  -1 420 ASP B OD2 1 
ATOM   3797 N N   . ALA B 2 266 ? 22.031 54.461 12.235 1.00 68.05  ?  421 ALA B N   1 
ATOM   3798 C CA  . ALA B 2 266 ? 23.379 54.983 12.095 1.00 68.30  ?  421 ALA B CA  1 
ATOM   3799 C C   . ALA B 2 266 ? 23.885 54.742 10.679 1.00 74.53  ?  421 ALA B C   1 
ATOM   3800 O O   . ALA B 2 266 ? 23.586 53.697 10.085 1.00 75.16  ?  421 ALA B O   1 
ATOM   3801 C CB  . ALA B 2 266 ? 24.300 54.314 13.101 1.00 68.89  ?  421 ALA B CB  1 
ATOM   3802 N N   . ASP B 2 267 ? 24.572 55.744 10.116 1.00 71.01  ?  422 ASP B N   1 
ATOM   3803 C CA  . ASP B 2 267 ? 25.229 55.646 8.814  1.00 71.01  ?  422 ASP B CA  1 
ATOM   3804 C C   . ASP B 2 267 ? 26.651 56.140 8.978  1.00 76.50  ?  422 ASP B C   1 
ATOM   3805 O O   . ASP B 2 267 ? 26.855 57.262 9.456  1.00 77.28  ?  422 ASP B O   1 
ATOM   3806 C CB  . ASP B 2 267 ? 24.489 56.390 7.690  1.00 72.62  ?  422 ASP B CB  1 
ATOM   3807 C CG  . ASP B 2 267 ? 24.198 57.852 7.959  1.00 85.52  ?  422 ASP B CG  1 
ATOM   3808 O OD1 . ASP B 2 267 ? 24.769 58.716 7.246  1.00 85.17  ?  422 ASP B OD1 1 
ATOM   3809 O OD2 . ASP B 2 267 ? 23.376 58.138 8.858  1.00 94.71  -1 422 ASP B OD2 1 
ATOM   3810 N N   . SER B 2 268 ? 27.638 55.297 8.609  1.00 72.40  ?  423 SER B N   1 
ATOM   3811 C CA  . SER B 2 268 ? 29.065 55.599 8.733  1.00 72.08  ?  423 SER B CA  1 
ATOM   3812 C C   . SER B 2 268 ? 29.471 56.979 8.207  1.00 76.87  ?  423 SER B C   1 
ATOM   3813 O O   . SER B 2 268 ? 30.395 57.595 8.748  1.00 75.47  ?  423 SER B O   1 
ATOM   3814 C CB  . SER B 2 268 ? 29.927 54.477 8.158  1.00 74.81  ?  423 SER B CB  1 
ATOM   3815 O OG  . SER B 2 268 ? 29.485 54.000 6.899  1.00 84.01  ?  423 SER B OG  1 
ATOM   3816 N N   . THR B 2 269 ? 28.719 57.491 7.209  1.00 75.02  ?  424 THR B N   1 
ATOM   3817 C CA  . THR B 2 269 ? 28.901 58.812 6.595  1.00 74.78  ?  424 THR B CA  1 
ATOM   3818 C C   . THR B 2 269 ? 28.860 59.895 7.674  1.00 76.12  ?  424 THR B C   1 
ATOM   3819 O O   . THR B 2 269 ? 29.913 60.458 7.991  1.00 74.92  ?  424 THR B O   1 
ATOM   3820 C CB  . THR B 2 269 ? 27.853 59.023 5.469  1.00 84.97  ?  424 THR B CB  1 
ATOM   3821 O OG1 . THR B 2 269 ? 28.042 58.039 4.446  1.00 84.01  ?  424 THR B OG1 1 
ATOM   3822 C CG2 . THR B 2 269 ? 27.893 60.433 4.872  1.00 81.99  ?  424 THR B CG2 1 
ATOM   3823 N N   . SER B 2 270 ? 27.659 60.137 8.275  1.00 72.03  ?  425 SER B N   1 
ATOM   3824 C CA  . SER B 2 270 ? 27.454 61.150 9.323  1.00 71.51  ?  425 SER B CA  1 
ATOM   3825 C C   . SER B 2 270 ? 28.165 60.811 10.633 1.00 73.62  ?  425 SER B C   1 
ATOM   3826 O O   . SER B 2 270 ? 28.513 61.729 11.372 1.00 74.39  ?  425 SER B O   1 
ATOM   3827 C CB  . SER B 2 270 ? 25.975 61.449 9.542  1.00 74.80  ?  425 SER B CB  1 
ATOM   3828 O OG  . SER B 2 270 ? 25.280 60.273 9.919  1.00 84.57  ?  425 SER B OG  1 
ATOM   3829 N N   . VAL B 2 271 ? 28.420 59.509 10.900 1.00 67.78  ?  426 VAL B N   1 
ATOM   3830 C CA  . VAL B 2 271 ? 29.161 59.079 12.085 1.00 67.08  ?  426 VAL B CA  1 
ATOM   3831 C C   . VAL B 2 271 ? 30.616 59.547 11.962 1.00 72.58  ?  426 VAL B C   1 
ATOM   3832 O O   . VAL B 2 271 ? 31.136 60.113 12.922 1.00 72.03  ?  426 VAL B O   1 
ATOM   3833 C CB  . VAL B 2 271 ? 29.031 57.570 12.420 1.00 70.10  ?  426 VAL B CB  1 
ATOM   3834 C CG1 . VAL B 2 271 ? 29.901 57.194 13.607 1.00 69.52  ?  426 VAL B CG1 1 
ATOM   3835 C CG2 . VAL B 2 271 ? 27.585 57.194 12.708 1.00 70.07  ?  426 VAL B CG2 1 
ATOM   3836 N N   . GLU B 2 272 ? 31.251 59.367 10.775 1.00 70.51  ?  427 GLU B N   1 
ATOM   3837 C CA  . GLU B 2 272 ? 32.628 59.822 10.521 1.00 70.95  ?  427 GLU B CA  1 
ATOM   3838 C C   . GLU B 2 272 ? 32.728 61.357 10.588 1.00 75.61  ?  427 GLU B C   1 
ATOM   3839 O O   . GLU B 2 272 ? 33.760 61.884 11.021 1.00 76.50  ?  427 GLU B O   1 
ATOM   3840 C CB  . GLU B 2 272 ? 33.163 59.306 9.180  1.00 72.36  ?  427 GLU B CB  1 
ATOM   3841 C CG  . GLU B 2 272 ? 33.977 58.028 9.306  1.00 83.61  ?  427 GLU B CG  1 
ATOM   3842 C CD  . GLU B 2 272 ? 33.711 56.980 8.239  1.00 109.26 ?  427 GLU B CD  1 
ATOM   3843 O OE1 . GLU B 2 272 ? 33.813 57.307 7.033  1.00 108.98 ?  427 GLU B OE1 1 
ATOM   3844 O OE2 . GLU B 2 272 ? 33.429 55.818 8.613  1.00 103.48 -1 427 GLU B OE2 1 
ATOM   3845 N N   . ALA B 2 273 ? 31.635 62.061 10.200 1.00 69.98  ?  428 ALA B N   1 
ATOM   3846 C CA  . ALA B 2 273 ? 31.529 63.518 10.248 1.00 68.67  ?  428 ALA B CA  1 
ATOM   3847 C C   . ALA B 2 273 ? 31.553 64.011 11.714 1.00 70.54  ?  428 ALA B C   1 
ATOM   3848 O O   . ALA B 2 273 ? 32.317 64.933 12.025 1.00 70.25  ?  428 ALA B O   1 
ATOM   3849 C CB  . ALA B 2 273 ? 30.255 63.974 9.550  1.00 69.17  ?  428 ALA B CB  1 
ATOM   3850 N N   . MET B 2 274 ? 30.752 63.365 12.615 1.00 64.09  ?  429 MET B N   1 
ATOM   3851 C CA  . MET B 2 274 ? 30.731 63.694 14.043 1.00 62.27  ?  429 MET B CA  1 
ATOM   3852 C C   . MET B 2 274 ? 32.101 63.389 14.652 1.00 64.35  ?  429 MET B C   1 
ATOM   3853 O O   . MET B 2 274 ? 32.581 64.191 15.448 1.00 64.50  ?  429 MET B O   1 
ATOM   3854 C CB  . MET B 2 274 ? 29.609 62.969 14.800 1.00 64.04  ?  429 MET B CB  1 
ATOM   3855 C CG  . MET B 2 274 ? 29.221 63.672 16.091 1.00 67.30  ?  429 MET B CG  1 
ATOM   3856 S SD  . MET B 2 274 ? 28.104 62.727 17.159 1.00 72.11  ?  429 MET B SD  1 
ATOM   3857 C CE  . MET B 2 274 ? 26.556 63.338 16.593 1.00 68.70  ?  429 MET B CE  1 
ATOM   3858 N N   . TYR B 2 275 ? 32.758 62.278 14.229 1.00 59.68  ?  430 TYR B N   1 
ATOM   3859 C CA  . TYR B 2 275 ? 34.111 61.935 14.681 1.00 59.24  ?  430 TYR B CA  1 
ATOM   3860 C C   . TYR B 2 275 ? 35.136 62.973 14.222 1.00 64.04  ?  430 TYR B C   1 
ATOM   3861 O O   . TYR B 2 275 ? 36.045 63.282 14.983 1.00 63.96  ?  430 TYR B O   1 
ATOM   3862 C CB  . TYR B 2 275 ? 34.551 60.509 14.304 1.00 59.71  ?  430 TYR B CB  1 
ATOM   3863 C CG  . TYR B 2 275 ? 35.911 60.169 14.893 1.00 60.81  ?  430 TYR B CG  1 
ATOM   3864 C CD1 . TYR B 2 275 ? 36.043 59.803 16.230 1.00 62.56  ?  430 TYR B CD1 1 
ATOM   3865 C CD2 . TYR B 2 275 ? 37.075 60.337 14.151 1.00 61.45  ?  430 TYR B CD2 1 
ATOM   3866 C CE1 . TYR B 2 275 ? 37.298 59.545 16.793 1.00 63.95  ?  430 TYR B CE1 1 
ATOM   3867 C CE2 . TYR B 2 275 ? 38.335 60.112 14.713 1.00 62.22  ?  430 TYR B CE2 1 
ATOM   3868 C CZ  . TYR B 2 275 ? 38.443 59.707 16.033 1.00 70.04  ?  430 TYR B CZ  1 
ATOM   3869 O OH  . TYR B 2 275 ? 39.684 59.455 16.589 1.00 71.17  ?  430 TYR B OH  1 
ATOM   3870 N N   . SER B 2 276 ? 34.983 63.520 13.004 1.00 62.19  ?  431 SER B N   1 
ATOM   3871 C CA  . SER B 2 276 ? 35.863 64.565 12.476 1.00 62.74  ?  431 SER B CA  1 
ATOM   3872 C C   . SER B 2 276 ? 35.783 65.803 13.397 1.00 67.38  ?  431 SER B C   1 
ATOM   3873 O O   . SER B 2 276 ? 36.825 66.283 13.855 1.00 66.70  ?  431 SER B O   1 
ATOM   3874 C CB  . SER B 2 276 ? 35.498 64.903 11.032 1.00 66.06  ?  431 SER B CB  1 
ATOM   3875 O OG  . SER B 2 276 ? 36.131 66.082 10.559 1.00 78.26  ?  431 SER B OG  1 
ATOM   3876 N N   . VAL B 2 277 ? 34.546 66.254 13.730 1.00 63.89  ?  432 VAL B N   1 
ATOM   3877 C CA  . VAL B 2 277 ? 34.288 67.373 14.652 1.00 63.37  ?  432 VAL B CA  1 
ATOM   3878 C C   . VAL B 2 277 ? 34.949 67.075 16.020 1.00 68.60  ?  432 VAL B C   1 
ATOM   3879 O O   . VAL B 2 277 ? 35.746 67.891 16.494 1.00 68.01  ?  432 VAL B O   1 
ATOM   3880 C CB  . VAL B 2 277 ? 32.775 67.653 14.796 1.00 66.05  ?  432 VAL B CB  1 
ATOM   3881 C CG1 . VAL B 2 277 ? 32.505 68.749 15.824 1.00 65.30  ?  432 VAL B CG1 1 
ATOM   3882 C CG2 . VAL B 2 277 ? 32.152 68.003 13.452 1.00 65.71  ?  432 VAL B CG2 1 
ATOM   3883 N N   . ALA B 2 278 ? 34.666 65.878 16.604 1.00 65.53  ?  433 ALA B N   1 
ATOM   3884 C CA  . ALA B 2 278 ? 35.229 65.426 17.882 1.00 66.45  ?  433 ALA B CA  1 
ATOM   3885 C C   . ALA B 2 278 ? 36.751 65.506 17.878 1.00 72.15  ?  433 ALA B C   1 
ATOM   3886 O O   . ALA B 2 278 ? 37.329 66.059 18.815 1.00 72.64  ?  433 ALA B O   1 
ATOM   3887 C CB  . ALA B 2 278 ? 34.779 64.006 18.194 1.00 67.37  ?  433 ALA B CB  1 
ATOM   3888 N N   . SER B 2 279 ? 37.386 65.007 16.800 1.00 68.60  ?  434 SER B N   1 
ATOM   3889 C CA  . SER B 2 279 ? 38.833 65.001 16.615 1.00 68.31  ?  434 SER B CA  1 
ATOM   3890 C C   . SER B 2 279 ? 39.425 66.404 16.693 1.00 72.58  ?  434 SER B C   1 
ATOM   3891 O O   . SER B 2 279 ? 40.455 66.577 17.345 1.00 72.83  ?  434 SER B O   1 
ATOM   3892 C CB  . SER B 2 279 ? 39.200 64.340 15.296 1.00 71.99  ?  434 SER B CB  1 
ATOM   3893 O OG  . SER B 2 279 ? 40.132 63.299 15.524 1.00 85.74  ?  434 SER B OG  1 
ATOM   3894 N N   . GLN B 2 280 ? 38.754 67.402 16.071 1.00 68.37  ?  435 GLN B N   1 
ATOM   3895 C CA  . GLN B 2 280 ? 39.172 68.807 16.081 1.00 68.22  ?  435 GLN B CA  1 
ATOM   3896 C C   . GLN B 2 280 ? 39.030 69.413 17.479 1.00 70.46  ?  435 GLN B C   1 
ATOM   3897 O O   . GLN B 2 280 ? 39.924 70.145 17.914 1.00 70.76  ?  435 GLN B O   1 
ATOM   3898 C CB  . GLN B 2 280 ? 38.383 69.627 15.052 1.00 69.82  ?  435 GLN B CB  1 
ATOM   3899 C CG  . GLN B 2 280 ? 38.923 69.489 13.638 1.00 95.28  ?  435 GLN B CG  1 
ATOM   3900 C CD  . GLN B 2 280 ? 37.820 69.615 12.623 1.00 126.21 ?  435 GLN B CD  1 
ATOM   3901 O OE1 . GLN B 2 280 ? 37.269 68.620 12.138 1.00 125.10 ?  435 GLN B OE1 1 
ATOM   3902 N NE2 . GLN B 2 280 ? 37.460 70.846 12.288 1.00 119.56 ?  435 GLN B NE2 1 
ATOM   3903 N N   . CYS B 2 281 ? 37.923 69.098 18.191 1.00 64.13  ?  436 CYS B N   1 
ATOM   3904 C CA  . CYS B 2 281 ? 37.685 69.557 19.565 1.00 62.01  ?  436 CYS B CA  1 
ATOM   3905 C C   . CYS B 2 281 ? 38.737 68.962 20.487 1.00 65.19  ?  436 CYS B C   1 
ATOM   3906 O O   . CYS B 2 281 ? 39.040 69.552 21.523 1.00 64.80  ?  436 CYS B O   1 
ATOM   3907 C CB  . CYS B 2 281 ? 36.289 69.169 20.039 1.00 61.35  ?  436 CYS B CB  1 
ATOM   3908 S SG  . CYS B 2 281 ? 34.940 69.934 19.117 1.00 64.76  ?  436 CYS B SG  1 
ATOM   3909 N N   . LEU B 2 282 ? 39.241 67.758 20.148 1.00 61.19  ?  437 LEU B N   1 
ATOM   3910 C CA  . LEU B 2 282 ? 40.224 67.056 20.979 1.00 60.58  ?  437 LEU B CA  1 
ATOM   3911 C C   . LEU B 2 282 ? 41.697 67.347 20.690 1.00 67.68  ?  437 LEU B C   1 
ATOM   3912 O O   . LEU B 2 282 ? 42.564 66.612 21.167 1.00 66.40  ?  437 LEU B O   1 
ATOM   3913 C CB  . LEU B 2 282 ? 39.928 65.548 21.093 1.00 59.43  ?  437 LEU B CB  1 
ATOM   3914 C CG  . LEU B 2 282 ? 38.668 65.152 21.858 1.00 61.48  ?  437 LEU B CG  1 
ATOM   3915 C CD1 . LEU B 2 282 ? 38.395 63.712 21.686 1.00 60.98  ?  437 LEU B CD1 1 
ATOM   3916 C CD2 . LEU B 2 282 ? 38.785 65.458 23.323 1.00 60.97  ?  437 LEU B CD2 1 
ATOM   3917 N N   . HIS B 2 283 ? 41.985 68.450 19.961 1.00 67.99  ?  438 HIS B N   1 
ATOM   3918 C CA  . HIS B 2 283 ? 43.360 68.887 19.707 1.00 69.36  ?  438 HIS B CA  1 
ATOM   3919 C C   . HIS B 2 283 ? 43.986 69.279 21.043 1.00 73.73  ?  438 HIS B C   1 
ATOM   3920 O O   . HIS B 2 283 ? 43.383 70.046 21.797 1.00 73.25  ?  438 HIS B O   1 
ATOM   3921 C CB  . HIS B 2 283 ? 43.404 70.068 18.725 1.00 71.06  ?  438 HIS B CB  1 
ATOM   3922 C CG  . HIS B 2 283 ? 43.448 69.653 17.288 1.00 75.06  ?  438 HIS B CG  1 
ATOM   3923 N ND1 . HIS B 2 283 ? 44.360 68.717 16.834 1.00 77.16  ?  438 HIS B ND1 1 
ATOM   3924 C CD2 . HIS B 2 283 ? 42.710 70.087 16.242 1.00 77.27  ?  438 HIS B CD2 1 
ATOM   3925 C CE1 . HIS B 2 283 ? 44.128 68.589 15.541 1.00 76.80  ?  438 HIS B CE1 1 
ATOM   3926 N NE2 . HIS B 2 283 ? 43.144 69.393 15.140 1.00 77.23  ?  438 HIS B NE2 1 
ATOM   3927 N N   . GLU B 2 284 ? 45.153 68.694 21.379 1.00 70.67  ?  439 GLU B N   1 
ATOM   3928 C CA  . GLU B 2 284 ? 45.811 68.957 22.666 1.00 70.41  ?  439 GLU B CA  1 
ATOM   3929 C C   . GLU B 2 284 ? 46.195 70.424 22.857 1.00 74.20  ?  439 GLU B C   1 
ATOM   3930 O O   . GLU B 2 284 ? 46.068 70.971 23.959 1.00 74.17  ?  439 GLU B O   1 
ATOM   3931 C CB  . GLU B 2 284 ? 47.001 68.026 22.875 1.00 71.65  ?  439 GLU B CB  1 
ATOM   3932 C CG  . GLU B 2 284 ? 46.902 67.272 24.192 1.00 82.95  ?  439 GLU B CG  1 
ATOM   3933 C CD  . GLU B 2 284 ? 45.964 66.078 24.244 1.00 105.04 ?  439 GLU B CD  1 
ATOM   3934 O OE1 . GLU B 2 284 ? 45.869 65.337 23.239 1.00 102.75 ?  439 GLU B OE1 1 
ATOM   3935 O OE2 . GLU B 2 284 ? 45.368 65.848 25.321 1.00 100.37 -1 439 GLU B OE2 1 
ATOM   3936 N N   . LYS B 2 285 ? 46.604 71.069 21.760 1.00 69.48  ?  440 LYS B N   1 
ATOM   3937 C CA  . LYS B 2 285 ? 46.955 72.479 21.728 1.00 68.82  ?  440 LYS B CA  1 
ATOM   3938 C C   . LYS B 2 285 ? 45.681 73.317 21.530 1.00 72.83  ?  440 LYS B C   1 
ATOM   3939 O O   . LYS B 2 285 ? 45.122 73.356 20.435 1.00 73.15  ?  440 LYS B O   1 
ATOM   3940 C CB  . LYS B 2 285 ? 48.060 72.755 20.675 1.00 71.00  ?  440 LYS B CB  1 
ATOM   3941 C CG  . LYS B 2 285 ? 47.955 71.967 19.336 1.00 84.21  ?  440 LYS B CG  1 
ATOM   3942 C CD  . LYS B 2 285 ? 48.243 70.424 19.373 1.00 81.85  ?  440 LYS B CD  1 
ATOM   3943 C CE  . LYS B 2 285 ? 47.222 69.638 18.569 1.00 67.03  ?  440 LYS B CE  1 
ATOM   3944 N NZ  . LYS B 2 285 ? 47.431 68.166 18.649 1.00 65.43  1  440 LYS B NZ  1 
ATOM   3945 N N   . LYS B 2 286 ? 45.204 73.943 22.621 1.00 69.32  ?  441 LYS B N   1 
ATOM   3946 C CA  . LYS B 2 286 ? 43.981 74.753 22.709 1.00 69.43  ?  441 LYS B CA  1 
ATOM   3947 C C   . LYS B 2 286 ? 43.678 75.709 21.550 1.00 77.06  ?  441 LYS B C   1 
ATOM   3948 O O   . LYS B 2 286 ? 42.505 75.894 21.204 1.00 76.88  ?  441 LYS B O   1 
ATOM   3949 C CB  . LYS B 2 286 ? 43.876 75.471 24.064 1.00 70.25  ?  441 LYS B CB  1 
ATOM   3950 C CG  . LYS B 2 286 ? 45.064 76.361 24.374 1.00 78.44  ?  441 LYS B CG  1 
ATOM   3951 C CD  . LYS B 2 286 ? 44.780 77.332 25.488 1.00 86.47  ?  441 LYS B CD  1 
ATOM   3952 C CE  . LYS B 2 286 ? 45.651 78.556 25.326 1.00 97.20  ?  441 LYS B CE  1 
ATOM   3953 N NZ  . LYS B 2 286 ? 46.947 78.437 26.044 1.00 106.00 1  441 LYS B NZ  1 
ATOM   3954 N N   . ASN B 2 287 ? 44.712 76.326 20.963 1.00 75.81  ?  442 ASN B N   1 
ATOM   3955 C CA  . ASN B 2 287 ? 44.495 77.269 19.862 1.00 76.37  ?  442 ASN B CA  1 
ATOM   3956 C C   . ASN B 2 287 ? 44.271 76.566 18.530 1.00 80.31  ?  442 ASN B C   1 
ATOM   3957 O O   . ASN B 2 287 ? 43.725 77.188 17.611 1.00 80.67  ?  442 ASN B O   1 
ATOM   3958 C CB  . ASN B 2 287 ? 45.583 78.342 19.794 1.00 78.85  ?  442 ASN B CB  1 
ATOM   3959 C CG  . ASN B 2 287 ? 45.825 79.035 21.120 1.00 104.25 ?  442 ASN B CG  1 
ATOM   3960 O OD1 . ASN B 2 287 ? 46.908 78.915 21.710 1.00 103.10 ?  442 ASN B OD1 1 
ATOM   3961 N ND2 . ASN B 2 287 ? 44.808 79.719 21.654 1.00 89.54  ?  442 ASN B ND2 1 
ATOM   3962 N N   . LYS B 2 288 ? 44.634 75.255 18.443 1.00 75.19  ?  443 LYS B N   1 
ATOM   3963 C CA  . LYS B 2 288 ? 44.402 74.432 17.248 1.00 74.15  ?  443 LYS B CA  1 
ATOM   3964 C C   . LYS B 2 288 ? 42.946 73.900 17.214 1.00 76.80  ?  443 LYS B C   1 
ATOM   3965 O O   . LYS B 2 288 ? 42.498 73.420 16.175 1.00 76.25  ?  443 LYS B O   1 
ATOM   3966 C CB  . LYS B 2 288 ? 45.425 73.293 17.132 1.00 75.81  ?  443 LYS B CB  1 
ATOM   3967 N N   . ARG B 2 289 ? 42.214 74.018 18.346 1.00 72.19  ?  444 ARG B N   1 
ATOM   3968 C CA  . ARG B 2 289 ? 40.813 73.609 18.504 1.00 71.27  ?  444 ARG B CA  1 
ATOM   3969 C C   . ARG B 2 289 ? 39.856 74.637 17.858 1.00 77.53  ?  444 ARG B C   1 
ATOM   3970 O O   . ARG B 2 289 ? 40.143 75.839 17.916 1.00 77.88  ?  444 ARG B O   1 
ATOM   3971 C CB  . ARG B 2 289 ? 40.453 73.480 19.997 1.00 66.08  ?  444 ARG B CB  1 
ATOM   3972 C CG  . ARG B 2 289 ? 40.999 72.247 20.688 1.00 62.87  ?  444 ARG B CG  1 
ATOM   3973 C CD  . ARG B 2 289 ? 40.649 72.288 22.162 1.00 57.45  ?  444 ARG B CD  1 
ATOM   3974 N NE  . ARG B 2 289 ? 41.733 71.768 22.983 1.00 60.98  ?  444 ARG B NE  1 
ATOM   3975 C CZ  . ARG B 2 289 ? 41.969 72.143 24.232 1.00 71.31  ?  444 ARG B CZ  1 
ATOM   3976 N NH1 . ARG B 2 289 ? 41.195 73.045 24.818 1.00 59.64  ?  444 ARG B NH1 1 
ATOM   3977 N NH2 . ARG B 2 289 ? 42.986 71.628 24.903 1.00 57.44  1  444 ARG B NH2 1 
ATOM   3978 N N   . PRO B 2 290 ? 38.694 74.213 17.290 1.00 74.09  ?  445 PRO B N   1 
ATOM   3979 C CA  . PRO B 2 290 ? 37.758 75.206 16.734 1.00 73.58  ?  445 PRO B CA  1 
ATOM   3980 C C   . PRO B 2 290 ? 36.969 75.929 17.824 1.00 78.45  ?  445 PRO B C   1 
ATOM   3981 O O   . PRO B 2 290 ? 36.824 75.398 18.931 1.00 78.12  ?  445 PRO B O   1 
ATOM   3982 C CB  . PRO B 2 290 ? 36.831 74.361 15.857 1.00 75.15  ?  445 PRO B CB  1 
ATOM   3983 C CG  . PRO B 2 290 ? 36.867 73.009 16.434 1.00 79.59  ?  445 PRO B CG  1 
ATOM   3984 C CD  . PRO B 2 290 ? 38.179 72.834 17.132 1.00 75.43  ?  445 PRO B CD  1 
ATOM   3985 N N   . ASP B 2 291 ? 36.452 77.135 17.520 1.00 75.93  ?  446 ASP B N   1 
ATOM   3986 C CA  . ASP B 2 291 ? 35.624 77.866 18.487 1.00 76.18  ?  446 ASP B CA  1 
ATOM   3987 C C   . ASP B 2 291 ? 34.217 77.257 18.452 1.00 79.26  ?  446 ASP B C   1 
ATOM   3988 O O   . ASP B 2 291 ? 33.936 76.443 17.563 1.00 78.54  ?  446 ASP B O   1 
ATOM   3989 C CB  . ASP B 2 291 ? 35.607 79.390 18.211 1.00 78.74  ?  446 ASP B CB  1 
ATOM   3990 C CG  . ASP B 2 291 ? 35.258 79.806 16.786 1.00 93.59  ?  446 ASP B CG  1 
ATOM   3991 O OD1 . ASP B 2 291 ? 34.134 79.481 16.322 1.00 95.27  ?  446 ASP B OD1 1 
ATOM   3992 O OD2 . ASP B 2 291 ? 36.081 80.506 16.156 1.00 98.51  -1 446 ASP B OD2 1 
ATOM   3993 N N   . ILE B 2 292 ? 33.337 77.636 19.398 1.00 75.51  ?  447 ILE B N   1 
ATOM   3994 C CA  . ILE B 2 292 ? 31.985 77.081 19.435 1.00 75.07  ?  447 ILE B CA  1 
ATOM   3995 C C   . ILE B 2 292 ? 31.155 77.295 18.151 1.00 78.12  ?  447 ILE B C   1 
ATOM   3996 O O   . ILE B 2 292 ? 30.546 76.338 17.666 1.00 77.29  ?  447 ILE B O   1 
ATOM   3997 C CB  . ILE B 2 292 ? 31.242 77.327 20.782 1.00 78.17  ?  447 ILE B CB  1 
ATOM   3998 C CG1 . ILE B 2 292 ? 30.032 76.370 20.972 1.00 78.61  ?  447 ILE B CG1 1 
ATOM   3999 C CG2 . ILE B 2 292 ? 30.887 78.790 20.994 1.00 78.55  ?  447 ILE B CG2 1 
ATOM   4000 C CD1 . ILE B 2 292 ? 30.380 74.850 21.165 1.00 81.49  ?  447 ILE B CD1 1 
ATOM   4001 N N   . LYS B 2 293 ? 31.207 78.515 17.566 1.00 74.28  ?  448 LYS B N   1 
ATOM   4002 C CA  . LYS B 2 293 ? 30.507 78.861 16.320 1.00 73.65  ?  448 LYS B CA  1 
ATOM   4003 C C   . LYS B 2 293 ? 30.940 77.957 15.141 1.00 76.09  ?  448 LYS B C   1 
ATOM   4004 O O   . LYS B 2 293 ? 30.095 77.587 14.322 1.00 75.77  ?  448 LYS B O   1 
ATOM   4005 C CB  . LYS B 2 293 ? 30.675 80.355 15.981 1.00 76.23  ?  448 LYS B CB  1 
ATOM   4006 N N   . LYS B 2 294 ? 32.232 77.565 15.085 1.00 71.42  ?  449 LYS B N   1 
ATOM   4007 C CA  . LYS B 2 294 ? 32.733 76.652 14.050 1.00 71.12  ?  449 LYS B CA  1 
ATOM   4008 C C   . LYS B 2 294 ? 32.194 75.231 14.308 1.00 76.33  ?  449 LYS B C   1 
ATOM   4009 O O   . LYS B 2 294 ? 31.775 74.566 13.360 1.00 76.70  ?  449 LYS B O   1 
ATOM   4010 C CB  . LYS B 2 294 ? 34.274 76.672 13.974 1.00 72.26  ?  449 LYS B CB  1 
ATOM   4011 C CG  . LYS B 2 294 ? 34.892 75.707 12.958 1.00 71.38  ?  449 LYS B CG  1 
ATOM   4012 N N   . VAL B 2 295 ? 32.187 74.784 15.588 1.00 72.49  ?  450 VAL B N   1 
ATOM   4013 C CA  . VAL B 2 295 ? 31.674 73.471 16.011 1.00 71.87  ?  450 VAL B CA  1 
ATOM   4014 C C   . VAL B 2 295 ? 30.198 73.375 15.581 1.00 76.99  ?  450 VAL B C   1 
ATOM   4015 O O   . VAL B 2 295 ? 29.802 72.371 14.970 1.00 76.69  ?  450 VAL B O   1 
ATOM   4016 C CB  . VAL B 2 295 ? 31.909 73.199 17.536 1.00 74.54  ?  450 VAL B CB  1 
ATOM   4017 C CG1 . VAL B 2 295 ? 31.184 71.942 18.013 1.00 73.44  ?  450 VAL B CG1 1 
ATOM   4018 C CG2 . VAL B 2 295 ? 33.402 73.100 17.861 1.00 74.17  ?  450 VAL B CG2 1 
ATOM   4019 N N   . GLN B 2 296 ? 29.421 74.461 15.833 1.00 74.22  ?  451 GLN B N   1 
ATOM   4020 C CA  . GLN B 2 296 ? 28.015 74.597 15.436 1.00 74.10  ?  451 GLN B CA  1 
ATOM   4021 C C   . GLN B 2 296 ? 27.878 74.390 13.923 1.00 78.05  ?  451 GLN B C   1 
ATOM   4022 O O   . GLN B 2 296 ? 27.064 73.573 13.504 1.00 77.91  ?  451 GLN B O   1 
ATOM   4023 C CB  . GLN B 2 296 ? 27.481 75.987 15.804 1.00 75.38  ?  451 GLN B CB  1 
ATOM   4024 C CG  . GLN B 2 296 ? 27.184 76.203 17.279 1.00 89.55  ?  451 GLN B CG  1 
ATOM   4025 C CD  . GLN B 2 296 ? 26.407 77.483 17.472 1.00 105.91 ?  451 GLN B CD  1 
ATOM   4026 O OE1 . GLN B 2 296 ? 26.896 78.592 17.215 1.00 103.69 ?  451 GLN B OE1 1 
ATOM   4027 N NE2 . GLN B 2 296 ? 25.160 77.360 17.894 1.00 91.23  ?  451 GLN B NE2 1 
ATOM   4028 N N   . GLN B 2 297 ? 28.714 75.090 13.120 1.00 75.25  ?  452 GLN B N   1 
ATOM   4029 C CA  . GLN B 2 297 ? 28.740 75.022 11.650 1.00 75.89  ?  452 GLN B CA  1 
ATOM   4030 C C   . GLN B 2 297 ? 28.933 73.599 11.138 1.00 79.76  ?  452 GLN B C   1 
ATOM   4031 O O   . GLN B 2 297 ? 28.161 73.141 10.289 1.00 80.04  ?  452 GLN B O   1 
ATOM   4032 C CB  . GLN B 2 297 ? 29.835 75.944 11.062 1.00 77.48  ?  452 GLN B CB  1 
ATOM   4033 N N   . LEU B 2 298 ? 29.949 72.899 11.669 1.00 75.68  ?  453 LEU B N   1 
ATOM   4034 C CA  . LEU B 2 298 ? 30.288 71.526 11.291 1.00 75.31  ?  453 LEU B CA  1 
ATOM   4035 C C   . LEU B 2 298 ? 29.200 70.502 11.658 1.00 79.49  ?  453 LEU B C   1 
ATOM   4036 O O   . LEU B 2 298 ? 29.061 69.484 10.975 1.00 78.98  ?  453 LEU B O   1 
ATOM   4037 C CB  . LEU B 2 298 ? 31.635 71.109 11.894 1.00 75.10  ?  453 LEU B CB  1 
ATOM   4038 C CG  . LEU B 2 298 ? 32.848 71.993 11.628 1.00 79.26  ?  453 LEU B CG  1 
ATOM   4039 C CD1 . LEU B 2 298 ? 34.032 71.534 12.460 1.00 79.20  ?  453 LEU B CD1 1 
ATOM   4040 C CD2 . LEU B 2 298 ? 33.211 72.015 10.157 1.00 81.13  ?  453 LEU B CD2 1 
ATOM   4041 N N   . LEU B 2 299 ? 28.436 70.771 12.731 1.00 76.39  ?  454 LEU B N   1 
ATOM   4042 C CA  . LEU B 2 299 ? 27.359 69.885 13.168 1.00 76.42  ?  454 LEU B CA  1 
ATOM   4043 C C   . LEU B 2 299 ? 26.085 70.098 12.339 1.00 83.18  ?  454 LEU B C   1 
ATOM   4044 O O   . LEU B 2 299 ? 25.353 69.136 12.079 1.00 82.68  ?  454 LEU B O   1 
ATOM   4045 C CB  . LEU B 2 299 ? 27.094 70.028 14.677 1.00 75.94  ?  454 LEU B CB  1 
ATOM   4046 C CG  . LEU B 2 299 ? 28.159 69.456 15.625 1.00 79.28  ?  454 LEU B CG  1 
ATOM   4047 C CD1 . LEU B 2 299 ? 27.909 69.899 17.038 1.00 78.56  ?  454 LEU B CD1 1 
ATOM   4048 C CD2 . LEU B 2 299 ? 28.209 67.927 15.562 1.00 81.26  ?  454 LEU B CD2 1 
ATOM   4049 N N   . GLN B 2 300 ? 25.831 71.353 11.903 1.00 81.37  ?  455 GLN B N   1 
ATOM   4050 C CA  . GLN B 2 300 ? 24.693 71.688 11.042 1.00 81.42  ?  455 GLN B CA  1 
ATOM   4051 C C   . GLN B 2 300 ? 24.980 71.184 9.610  1.00 86.90  ?  455 GLN B C   1 
ATOM   4052 O O   . GLN B 2 300 ? 24.042 70.861 8.876  1.00 86.45  ?  455 GLN B O   1 
ATOM   4053 C CB  . GLN B 2 300 ? 24.401 73.194 11.070 1.00 82.40  ?  455 GLN B CB  1 
ATOM   4054 N N   . GLU B 2 301 ? 26.287 71.094 9.241  1.00 84.36  ?  456 GLU B N   1 
ATOM   4055 C CA  . GLU B 2 301 ? 26.793 70.588 7.960  1.00 84.76  ?  456 GLU B CA  1 
ATOM   4056 C C   . GLU B 2 301 ? 26.600 69.069 7.894  1.00 90.51  ?  456 GLU B C   1 
ATOM   4057 O O   . GLU B 2 301 ? 26.313 68.527 6.824  1.00 90.72  ?  456 GLU B O   1 
ATOM   4058 C CB  . GLU B 2 301 ? 28.285 70.918 7.812  1.00 86.08  ?  456 GLU B CB  1 
ATOM   4059 C CG  . GLU B 2 301 ? 28.582 72.146 6.976  1.00 97.67  ?  456 GLU B CG  1 
ATOM   4060 C CD  . GLU B 2 301 ? 30.071 72.346 6.768  1.00 122.78 ?  456 GLU B CD  1 
ATOM   4061 O OE1 . GLU B 2 301 ? 30.745 72.836 7.699  1.00 120.50 ?  456 GLU B OE1 1 
ATOM   4062 O OE2 . GLU B 2 301 ? 30.565 72.022 5.661  1.00 120.62 -1 456 GLU B OE2 1 
ATOM   4063 N N   . MET B 2 302 ? 26.781 68.397 9.049  1.00 87.86  ?  457 MET B N   1 
ATOM   4064 C CA  . MET B 2 302 ? 26.677 66.953 9.259  1.00 88.19  ?  457 MET B CA  1 
ATOM   4065 C C   . MET B 2 302 ? 25.267 66.406 8.908  1.00 93.31  ?  457 MET B C   1 
ATOM   4066 O O   . MET B 2 302 ? 25.151 65.287 8.396  1.00 92.78  ?  457 MET B O   1 
ATOM   4067 C CB  . MET B 2 302 ? 27.089 66.642 10.715 1.00 90.49  ?  457 MET B CB  1 
ATOM   4068 C CG  . MET B 2 302 ? 26.950 65.183 11.146 1.00 94.26  ?  457 MET B CG  1 
ATOM   4069 S SD  . MET B 2 302 ? 27.115 64.972 12.943 1.00 98.53  ?  457 MET B SD  1 
ATOM   4070 C CE  . MET B 2 302 ? 25.664 65.852 13.529 1.00 95.13  ?  457 MET B CE  1 
ATOM   4071 N N   . THR B 2 303 ? 24.215 67.205 9.168  1.00 91.02  ?  458 THR B N   1 
ATOM   4072 C CA  . THR B 2 303 ? 22.819 66.836 8.905  1.00 91.33  ?  458 THR B CA  1 
ATOM   4073 C C   . THR B 2 303 ? 22.224 67.524 7.651  1.00 97.05  ?  458 THR B C   1 
ATOM   4074 O O   . THR B 2 303 ? 21.070 67.265 7.303  1.00 97.13  ?  458 THR B O   1 
ATOM   4075 C CB  . THR B 2 303 ? 21.961 66.999 10.171 1.00 98.40  ?  458 THR B CB  1 
ATOM   4076 O OG1 . THR B 2 303 ? 22.140 68.314 10.700 1.00 101.19 ?  458 THR B OG1 1 
ATOM   4077 C CG2 . THR B 2 303 ? 22.275 65.957 11.232 1.00 95.20  ?  458 THR B CG2 1 
ATOM   4078 N N   . ALA B 2 304 ? 23.019 68.357 6.952  1.00 94.10  ?  459 ALA B N   1 
ATOM   4079 C CA  . ALA B 2 304 ? 22.583 69.050 5.738  1.00 127.44 ?  459 ALA B CA  1 
ATOM   4080 C C   . ALA B 2 304 ? 23.642 68.963 4.641  1.00 168.93 ?  459 ALA B C   1 
ATOM   4081 O O   . ALA B 2 304 ? 23.311 68.754 3.474  1.00 134.40 ?  459 ALA B O   1 
ATOM   4082 C CB  . ALA B 2 304 ? 22.268 70.503 6.051  1.00 128.15 ?  459 ALA B CB  1 
HETATM 4083 C C13 . ZVG C 3 .   ? 20.983 34.770 13.833 1.00 33.63  ?  501 ZVG A C13 1 
HETATM 4084 C C18 . ZVG C 3 .   ? 19.241 27.633 14.089 1.00 50.64  ?  501 ZVG A C18 1 
HETATM 4085 C C17 . ZVG C 3 .   ? 18.500 28.788 13.883 1.00 44.56  ?  501 ZVG A C17 1 
HETATM 4086 C C16 . ZVG C 3 .   ? 17.097 28.771 13.958 1.00 40.54  ?  501 ZVG A C16 1 
HETATM 4087 C C15 . ZVG C 3 .   ? 19.119 30.003 13.542 1.00 41.47  ?  501 ZVG A C15 1 
HETATM 4088 C C11 . ZVG C 3 .   ? 20.243 35.262 15.052 1.00 32.14  ?  501 ZVG A C11 1 
HETATM 4089 C C12 . ZVG C 3 .   ? 21.085 36.214 15.871 1.00 31.65  ?  501 ZVG A C12 1 
HETATM 4090 N N6  . ZVG C 3 .   ? 19.829 26.672 14.254 1.00 55.77  ?  501 ZVG A N6  1 
HETATM 4091 N N4  . ZVG C 3 .   ? 18.418 31.121 13.287 1.00 36.62  ?  501 ZVG A N4  1 
HETATM 4092 N N5  . ZVG C 3 .   ? 16.358 29.857 13.702 1.00 38.89  ?  501 ZVG A N5  1 
HETATM 4093 C C14 . ZVG C 3 .   ? 17.058 31.021 13.378 1.00 34.34  ?  501 ZVG A C14 1 
HETATM 4094 N N3  . ZVG C 3 .   ? 16.220 32.113 13.332 1.00 33.57  ?  501 ZVG A N3  1 
HETATM 4095 C C8  . ZVG C 3 .   ? 16.413 33.517 13.491 1.00 31.75  ?  501 ZVG A C8  1 
HETATM 4096 N N1  . ZVG C 3 .   ? 15.407 34.346 13.033 1.00 30.92  ?  501 ZVG A N1  1 
HETATM 4097 C C7  . ZVG C 3 .   ? 15.623 35.666 13.122 1.00 30.78  ?  501 ZVG A C7  1 
HETATM 4098 C C9  . ZVG C 3 .   ? 17.633 33.992 14.037 1.00 29.32  ?  501 ZVG A C9  1 
HETATM 4099 C C10 . ZVG C 3 .   ? 17.844 35.412 14.119 1.00 31.53  ?  501 ZVG A C10 1 
HETATM 4100 N N2  . ZVG C 3 .   ? 19.042 35.989 14.584 1.00 32.12  ?  501 ZVG A N2  1 
HETATM 4101 C C6  . ZVG C 3 .   ? 16.787 36.266 13.653 1.00 30.03  ?  501 ZVG A C6  1 
HETATM 4102 C C5  . ZVG C 3 .   ? 16.902 37.728 13.693 1.00 30.37  ?  501 ZVG A C5  1 
HETATM 4103 O O1  . ZVG C 3 .   ? 18.005 38.291 13.808 1.00 37.03  ?  501 ZVG A O1  1 
HETATM 4104 N N   . ZVG C 3 .   ? 15.689 38.440 13.635 1.00 28.21  ?  501 ZVG A N   1 
HETATM 4105 C C4  . ZVG C 3 .   ? 15.640 39.895 13.597 1.00 27.67  ?  501 ZVG A C4  1 
HETATM 4106 C C3  . ZVG C 3 .   ? 15.534 40.578 14.969 1.00 30.74  ?  501 ZVG A C3  1 
HETATM 4107 F F   . ZVG C 3 .   ? 16.656 40.166 15.700 1.00 35.45  ?  501 ZVG A F   1 
HETATM 4108 C C   . ZVG C 3 .   ? 15.523 42.176 14.884 1.00 30.74  ?  501 ZVG A C   1 
HETATM 4109 C C2  . ZVG C 3 .   ? 15.443 42.848 16.246 1.00 26.54  ?  501 ZVG A C2  1 
HETATM 4110 C C1  . ZVG C 3 .   ? 14.449 42.740 13.958 1.00 24.03  ?  501 ZVG A C1  1 
HETATM 4111 O O   . ZVG C 3 .   ? 16.819 42.473 14.306 1.00 35.20  ?  501 ZVG A O   1 
HETATM 4112 S S   . SO4 D 4 .   ? 37.985 19.920 4.061  1.00 144.01 ?  502 SO4 A S   1 
HETATM 4113 O O1  . SO4 D 4 .   ? 38.276 20.320 2.680  1.00 150.00 -1 502 SO4 A O1  1 
HETATM 4114 O O2  . SO4 D 4 .   ? 36.540 19.983 4.279  1.00 149.32 -1 502 SO4 A O2  1 
HETATM 4115 O O3  . SO4 D 4 .   ? 38.460 18.545 4.287  1.00 148.10 ?  502 SO4 A O3  1 
HETATM 4116 O O4  . SO4 D 4 .   ? 38.660 20.835 4.989  1.00 148.48 ?  502 SO4 A O4  1 
HETATM 4117 C C13 . ZVG E 3 .   ? 19.968 63.930 38.070 1.00 69.57  ?  501 ZVG B C13 1 
HETATM 4118 C C18 . ZVG E 3 .   ? 21.296 71.056 37.576 1.00 78.70  ?  501 ZVG B C18 1 
HETATM 4119 C C17 . ZVG E 3 .   ? 20.148 70.312 37.253 1.00 76.16  ?  501 ZVG B C17 1 
HETATM 4120 C C16 . ZVG E 3 .   ? 19.083 70.855 36.501 1.00 73.86  ?  501 ZVG B C16 1 
HETATM 4121 C C15 . ZVG E 3 .   ? 19.998 68.987 37.728 1.00 76.52  ?  501 ZVG B C15 1 
HETATM 4122 C C11 . ZVG E 3 .   ? 19.743 63.568 36.617 1.00 69.54  ?  501 ZVG B C11 1 
HETATM 4123 C C12 . ZVG E 3 .   ? 20.392 62.252 36.262 1.00 70.38  ?  501 ZVG B C12 1 
HETATM 4124 N N6  . ZVG E 3 .   ? 22.242 71.653 37.863 1.00 80.12  ?  501 ZVG B N6  1 
HETATM 4125 N N4  . ZVG E 3 .   ? 18.903 68.230 37.499 1.00 75.55  ?  501 ZVG B N4  1 
HETATM 4126 N N5  . ZVG E 3 .   ? 17.937 70.168 36.242 1.00 73.61  ?  501 ZVG B N5  1 
HETATM 4127 C C14 . ZVG E 3 .   ? 17.888 68.845 36.750 1.00 74.55  ?  501 ZVG B C14 1 
HETATM 4128 N N3  . ZVG E 3 .   ? 16.792 68.142 36.272 1.00 72.58  ?  501 ZVG B N3  1 
HETATM 4129 C C8  . ZVG E 3 .   ? 16.538 66.762 36.141 1.00 70.54  ?  501 ZVG B C8  1 
HETATM 4130 N N1  . ZVG E 3 .   ? 15.228 66.381 35.927 1.00 70.26  ?  501 ZVG B N1  1 
HETATM 4131 C C7  . ZVG E 3 .   ? 14.980 65.042 35.854 1.00 67.63  ?  501 ZVG B C7  1 
HETATM 4132 C C9  . ZVG E 3 .   ? 17.607 65.826 36.283 1.00 68.95  ?  501 ZVG B C9  1 
HETATM 4133 C C10 . ZVG E 3 .   ? 17.321 64.406 36.191 1.00 67.59  ?  501 ZVG B C10 1 
HETATM 4134 N N2  . ZVG E 3 .   ? 18.285 63.417 36.348 1.00 68.34  ?  501 ZVG B N2  1 
HETATM 4135 C C6  . ZVG E 3 .   ? 15.946 64.018 35.960 1.00 64.03  ?  501 ZVG B C6  1 
HETATM 4136 C C5  . ZVG E 3 .   ? 15.521 62.608 35.854 1.00 57.31  ?  501 ZVG B C5  1 
HETATM 4137 O O1  . ZVG E 3 .   ? 16.208 61.675 36.253 1.00 55.69  ?  501 ZVG B O1  1 
HETATM 4138 N N   . ZVG E 3 .   ? 14.292 62.389 35.256 1.00 56.89  ?  501 ZVG B N   1 
HETATM 4139 C C4  . ZVG E 3 .   ? 13.717 61.036 35.136 1.00 60.37  ?  501 ZVG B C4  1 
HETATM 4140 C C3  . ZVG E 3 .   ? 14.072 60.325 33.772 1.00 62.79  ?  501 ZVG B C3  1 
HETATM 4141 F F   . ZVG E 3 .   ? 15.468 60.183 33.621 1.00 63.34  ?  501 ZVG B F   1 
HETATM 4142 C C   . ZVG E 3 .   ? 13.349 58.927 33.586 1.00 60.53  ?  501 ZVG B C   1 
HETATM 4143 C C2  . ZVG E 3 .   ? 13.776 58.178 32.332 1.00 57.94  ?  501 ZVG B C2  1 
HETATM 4144 C C1  . ZVG E 3 .   ? 11.837 59.066 33.631 1.00 59.16  ?  501 ZVG B C1  1 
HETATM 4145 O O   . ZVG E 3 .   ? 13.736 58.126 34.719 1.00 60.61  ?  501 ZVG B O   1 
HETATM 4146 S S   . SO4 F 4 .   ? 26.798 52.367 5.874  1.00 66.31  ?  502 SO4 B S   1 
HETATM 4147 O O1  . SO4 F 4 .   ? 25.816 51.798 4.965  1.00 72.65  -1 502 SO4 B O1  1 
HETATM 4148 O O2  . SO4 F 4 .   ? 27.388 53.564 5.232  1.00 70.50  ?  502 SO4 B O2  1 
HETATM 4149 O O3  . SO4 F 4 .   ? 27.831 51.362 6.143  1.00 71.00  ?  502 SO4 B O3  1 
HETATM 4150 O O4  . SO4 F 4 .   ? 26.142 52.731 7.166  1.00 71.77  -1 502 SO4 B O4  1 
HETATM 4151 O O   . HOH G 5 .   ? 23.201 36.365 18.714 1.00 42.77  ?  601 HOH A O   1 
HETATM 4152 O O   . HOH G 5 .   ? 7.539  42.100 20.247 0.50 29.13  ?  602 HOH A O   1 
HETATM 4153 O O   . HOH G 5 .   ? 9.242  23.356 17.687 1.00 41.16  ?  603 HOH A O   1 
HETATM 4154 O O   . HOH G 5 .   ? 11.062 42.674 16.322 1.00 48.64  ?  604 HOH A O   1 
HETATM 4155 O O   . HOH G 5 .   ? 19.179 42.407 15.927 1.00 34.53  ?  605 HOH A O   1 
HETATM 4156 O O   . HOH G 5 .   ? 16.466 44.188 23.817 1.00 34.43  ?  606 HOH A O   1 
HETATM 4157 O O   . HOH G 5 .   ? 26.997 37.152 -2.289 1.00 41.42  ?  607 HOH A O   1 
HETATM 4158 O O   . HOH G 5 .   ? 29.418 31.641 0.342  1.00 69.06  ?  608 HOH A O   1 
HETATM 4159 O O   . HOH G 5 .   ? 20.960 29.442 16.348 1.00 50.46  ?  609 HOH A O   1 
HETATM 4160 O O   . HOH G 5 .   ? 27.153 41.547 -0.061 1.00 34.54  ?  610 HOH A O   1 
HETATM 4161 O O   . HOH G 5 .   ? 29.364 15.825 17.758 1.00 57.48  ?  611 HOH A O   1 
HETATM 4162 O O   . HOH G 5 .   ? 27.113 25.859 2.596  1.00 55.98  ?  612 HOH A O   1 
HETATM 4163 O O   . HOH G 5 .   ? 19.722 44.165 28.999 1.00 44.65  ?  613 HOH A O   1 
HETATM 4164 O O   . HOH G 5 .   ? 29.186 23.950 24.308 1.00 50.30  ?  614 HOH A O   1 
HETATM 4165 O O   . HOH G 5 .   ? 25.700 44.262 35.356 1.00 48.24  ?  615 HOH A O   1 
HETATM 4166 O O   . HOH G 5 .   ? 24.559 45.169 31.789 1.00 53.00  ?  616 HOH A O   1 
HETATM 4167 O O   . HOH G 5 .   ? 12.492 43.685 21.121 1.00 53.15  ?  617 HOH A O   1 
HETATM 4168 O O   . HOH G 5 .   ? 25.781 33.122 23.497 1.00 38.39  ?  618 HOH A O   1 
HETATM 4169 O O   . HOH G 5 .   ? 30.082 43.340 29.036 1.00 53.68  ?  619 HOH A O   1 
HETATM 4170 O O   . HOH G 5 .   ? 4.190  32.543 21.763 1.00 50.44  ?  620 HOH A O   1 
HETATM 4171 O O   . HOH G 5 .   ? 14.769 42.311 9.999  1.00 58.48  ?  621 HOH A O   1 
HETATM 4172 O O   . HOH G 5 .   ? 7.938  21.883 9.990  1.00 59.09  ?  622 HOH A O   1 
HETATM 4173 O O   . HOH G 5 .   ? 9.235  31.862 26.968 1.00 62.62  ?  623 HOH A O   1 
HETATM 4174 O O   . HOH G 5 .   ? 17.863 43.353 27.581 1.00 43.98  ?  624 HOH A O   1 
HETATM 4175 O O   . HOH G 5 .   ? 25.317 25.605 13.139 1.00 43.14  ?  625 HOH A O   1 
HETATM 4176 O O   . HOH G 5 .   ? 9.784  26.705 33.860 1.00 53.12  ?  626 HOH A O   1 
HETATM 4177 O O   . HOH G 5 .   ? 19.413 43.178 0.791  1.00 45.35  ?  627 HOH A O   1 
HETATM 4178 O O   . HOH G 5 .   ? 31.880 15.589 19.353 1.00 51.23  ?  628 HOH A O   1 
HETATM 4179 O O   . HOH G 5 .   ? 9.980  28.227 15.531 1.00 62.36  ?  629 HOH A O   1 
HETATM 4180 O O   . HOH G 5 .   ? 19.060 39.062 17.072 1.00 34.81  ?  630 HOH A O   1 
HETATM 4181 O O   . HOH G 5 .   ? 27.611 38.882 0.084  1.00 47.80  ?  631 HOH A O   1 
HETATM 4182 O O   . HOH G 5 .   ? 10.372 41.693 8.348  1.00 49.14  ?  632 HOH A O   1 
HETATM 4183 O O   . HOH G 5 .   ? 23.557 41.449 11.819 1.00 54.06  ?  633 HOH A O   1 
HETATM 4184 O O   . HOH G 5 .   ? 36.233 18.455 11.375 1.00 57.52  ?  634 HOH A O   1 
HETATM 4185 O O   . HOH G 5 .   ? 22.264 14.608 0.561  1.00 63.40  ?  635 HOH A O   1 
HETATM 4186 O O   . HOH G 5 .   ? 8.678  41.939 17.610 0.50 38.71  ?  636 HOH A O   1 
HETATM 4187 O O   . HOH G 5 .   ? 21.028 36.039 -6.621 1.00 49.49  ?  637 HOH A O   1 
HETATM 4188 O O   . HOH G 5 .   ? 21.820 10.190 18.020 1.00 66.40  ?  638 HOH A O   1 
HETATM 4189 O O   . HOH H 5 .   ? 57.261 64.207 47.307 1.00 51.66  ?  601 HOH B O   1 
HETATM 4190 O O   . HOH H 5 .   ? 15.828 51.579 11.205 1.00 49.64  ?  602 HOH B O   1 
HETATM 4191 O O   . HOH H 5 .   ? 19.252 65.546 7.840  1.00 69.98  ?  603 HOH B O   1 
HETATM 4192 O O   . HOH H 5 .   ? 59.765 67.136 44.646 1.00 31.55  ?  604 HOH B O   1 
HETATM 4193 O O   . HOH H 5 .   ? 16.529 57.220 34.704 1.00 55.29  ?  605 HOH B O   1 
HETATM 4194 O O   . HOH H 5 .   ? 24.183 48.033 15.164 1.00 68.08  ?  606 HOH B O   1 
HETATM 4195 O O   . HOH H 5 .   ? 31.669 50.876 29.026 1.00 54.76  ?  607 HOH B O   1 
HETATM 4196 O O   . HOH H 5 .   ? 17.943 55.557 26.766 1.00 45.33  ?  608 HOH B O   1 
HETATM 4197 O O   . HOH H 5 .   ? 14.613 58.721 15.848 1.00 63.03  ?  609 HOH B O   1 
HETATM 4198 O O   . HOH H 5 .   ? 10.075 61.133 25.338 1.00 51.70  ?  610 HOH B O   1 
HETATM 4199 O O   . HOH H 5 .   ? 34.480 79.268 22.091 1.00 72.26  ?  611 HOH B O   1 
HETATM 4200 O O   . HOH H 5 .   ? 23.325 54.290 23.627 1.00 52.15  ?  612 HOH B O   1 
HETATM 4201 O O   . HOH H 5 .   ? 32.906 66.831 10.042 1.00 59.36  ?  613 HOH B O   1 
HETATM 4202 O O   . HOH H 5 .   ? 35.036 47.757 20.223 1.00 73.67  ?  614 HOH B O   1 
HETATM 4203 O O   . HOH H 5 .   ? 24.915 55.614 33.635 1.00 45.13  ?  615 HOH B O   1 
HETATM 4204 O O   . HOH H 5 .   ? 40.170 77.576 20.233 1.00 62.85  ?  616 HOH B O   1 
HETATM 4205 O O   . HOH H 5 .   ? 22.386 51.587 12.741 1.00 53.45  ?  617 HOH B O   1 
HETATM 4206 O O   . HOH H 5 .   ? 31.583 65.304 40.960 1.00 74.71  ?  618 HOH B O   1 
HETATM 4207 O O   . HOH H 5 .   ? 28.056 48.893 21.247 1.00 53.54  ?  619 HOH B O   1 
HETATM 4208 O O   . HOH H 5 .   ? 28.241 50.442 23.593 1.00 52.95  ?  620 HOH B O   1 
HETATM 4209 O O   . HOH H 5 .   ? 30.373 67.243 38.921 1.00 73.78  ?  621 HOH B O   1 
HETATM 4210 O O   . HOH H 5 .   ? 32.291 58.721 32.383 1.00 62.11  ?  622 HOH B O   1 
HETATM 4211 O O   . HOH H 5 .   ? 18.923 61.786 11.371 1.00 71.75  ?  623 HOH B O   1 
HETATM 4212 O O   . HOH H 5 .   ? 30.928 62.836 39.993 1.00 72.02  ?  624 HOH B O   1 
HETATM 4213 O O   . HOH H 5 .   ? 15.232 58.132 20.728 1.00 68.89  ?  625 HOH B O   1 
HETATM 4214 O O   . HOH H 5 .   ? 29.169 50.812 28.126 1.00 46.18  ?  626 HOH B O   1 
# 
