data_8ZLR
# 
_entry.id   8ZLR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZLR         pdb_00008zlr 10.2210/pdb8zlr/pdb 
WWPDB D_1300047773 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-14 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_DOI'    
5 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
6 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZLR 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'The same protein in the dark-adapted form'                           8Z1J unspecified 
PDB 'The same protein 10 ns after illumination of the dark-adapted form'  8Z24 unspecified 
PDB 'The same protein 30 ns after illumination of the dark-adapted form'  8Z26 unspecified 
PDB 'The same protein 100 ns after illumination of the dark-adapted form' 8Z2D unspecified 
PDB 'The same protein 300 ns after illumination of the dark-adapted form' 8Z44 unspecified 
PDB 'The same protein 1 us after illumination of the dark-adapted form'   8Z3D unspecified 
PDB 'The same protein 3 us after illumination of the dark-adapted form'   8Z3G unspecified 
PDB 'The same protein 10 us after illumination of the dark-adapted form'  8Z3L unspecified 
PDB 'The same protein 30 us after illumination of the dark-adapted form'  8Z3X unspecified 
PDB 'The same protein 100 us after illumination of the dark-adapted form' 8Z41 unspecified 
PDB 'The same protein 300 us after illumination of the dark-adapted form' 8Z45 unspecified 
PDB 'The same protein 1 ms after illumination of the dark-adapted form'   8Z4K unspecified 
PDB 'The same protein 7 ms after illumination of the dark-adapted form'   8Z4M unspecified 
PDB 'The same protein 33 ms after illumination of the dark-adapted form'  8Z4P unspecified 
PDB 'The same protein 66 ms after illumination of the dark-adapted form'  8Z4U unspecified 
PDB 'The same protein 100 ms after illumination of the dark-adapted form' 8Z6I unspecified 
PDB 'The same protein 133 ms after illumination of the dark-adapted form' 8Z6J unspecified 
PDB 'The same protein 166 ms after illumination of the dark-adapted form' 8Z6K unspecified 
PDB 'The same protein 200 ms after illumination of the dark-adapted form' 8Z8F unspecified 
PDB 'The same protein 233 ms after illumination of the dark-adapted form' 8Z8K unspecified 
PDB 'The same protein in the fully reduced form'                          8ZA8 unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 mmaestre@ntu.edu.tw              Manuel      Maestre-Reyna ? 'principal investigator/group leader' 0000-0002-9566-7216 
3 mdtsai@gate.sinica.edu.tw        Ming-Daw    Tsai          ? 'principal investigator/group leader' 0000-0003-1374-0414 
4 yamamoto.junpei.es@osaka-u.ac.jp Junpei      Yamamoto      ? 'principal investigator/group leader' 0000-0002-5036-991X 
5 essen@chemie.uni-marburg.de      Lars-Oliver Essen         ? 'principal investigator/group leader' 0000-0003-4272-4026 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Maestre-Reyna, M.'  1  ? 
'Hosokawa, Y.'       2  ? 
'Wang, P.-H.'        3  ? 
'Saft, M.'           4  ? 
'Caramello, N.'      5  ? 
'Engilberge, S.'     6  ? 
'Franz-Badur, S.'    7  ? 
'Ngura Putu, E.P.G.' 8  ? 
'Nakamura, M.'       9  ? 
'Wu, W.-J.'          10 ? 
'Wu, H.-Y.'          11 ? 
'Lee, C.-C.'         12 ? 
'Huang, W.-C.'       13 ? 
'Huang, K.-F.'       14 ? 
'Chang, Y.-K.'       15 ? 
'Yang, C.-H.'        16 ? 
'Lin, W.-T.'         17 ? 
'Yang, K.-C.'        18 ? 
'Ban, Y.'            19 ? 
'Imura, T.'          20 ? 
'Kazuoka, A.'        21 ? 
'Tanida, E.'         22 ? 
'Owada, S.'          23 ? 
'Joti, Y.'           24 ? 
'Tanaka, R.'         25 ? 
'Tanaka, T.'         26 ? 
'Luo, F.'            27 ? 
'Tono, K.'           28 ? 
'Kiontke, S.'        29 ? 
'Korf, L.'           30 ? 
'Umena, Y.'          31 ? 
'Tosha, T.'          32 ? 
'Bessho, Y.'         33 ? 
'Nango, E.'          34 ? 
'Iwata, S.'          35 ? 
'Royant, A.'         36 ? 
'Tsai, M.-D.'        37 ? 
'Yamamoto, J.'       38 ? 
'Essen, L.-O.'       39 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                eadu7247 
_citation.page_last                 eadu7247 
_citation.title                     
'Capturing structural intermediates in an animal-like cryptochrome photoreceptor by time-resolved crystallography.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/sciadv.adu7247 
_citation.pdbx_database_id_PubMed   40378212 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Maestre-Reyna, M.'       1  0000-0002-9566-7216 
primary 'Hosokawa, Y.'            2  0000-0001-9559-8567 
primary 'Wang, P.H.'              3  0000-0001-7359-934X 
primary 'Saft, M.'                4  0000-0003-3943-2786 
primary 'Caramello, N.'           5  0000-0003-0025-0213 
primary 'Engilberge, S.'          6  0000-0001-8680-6790 
primary 'Franz-Badur, S.'         7  ?                   
primary 'Gusti Ngurah Putu, E.P.' 8  0000-0003-1658-4015 
primary 'Nakamura, M.'            9  0009-0001-3017-1981 
primary 'Wu, W.J.'                10 0000-0002-7253-5384 
primary 'Wu, H.Y.'                11 0000-0001-5449-8295 
primary 'Lee, C.C.'               12 0000-0002-8259-4388 
primary 'Huang, W.C.'             13 0000-0003-4437-3530 
primary 'Huang, K.F.'             14 0000-0001-5235-7421 
primary 'Chang, Y.K.'             15 0000-0003-0314-3165 
primary 'Yang, C.H.'              16 0000-0001-7517-3799 
primary 'Fong, M.I.'              17 0009-0002-4710-1039 
primary 'Lin, W.T.'               18 0009-0004-3149-205X 
primary 'Yang, K.C.'              19 0009-0006-9790-1244 
primary 'Ban, Y.'                 20 ?                   
primary 'Imura, T.'               21 ?                   
primary 'Kazuoka, A.'             22 ?                   
primary 'Tanida, E.'              23 ?                   
primary 'Owada, S.'               24 0000-0002-1451-7612 
primary 'Joti, Y.'                25 0000-0002-4040-5972 
primary 'Tanaka, R.'              26 0000-0003-1062-4792 
primary 'Tanaka, T.'              27 ?                   
primary 'Kang, J.'                28 0000-0002-3506-6400 
primary 'Luo, F.'                 29 0000-0003-0631-6236 
primary 'Tono, K.'                30 0000-0003-1218-3759 
primary 'Kiontke, S.'             31 0000-0001-5822-913X 
primary 'Korf, L.'                32 0000-0003-4882-1177 
primary 'Umena, Y.'               33 ?                   
primary 'Tosha, T.'               34 0000-0002-8971-0759 
primary 'Bessho, Y.'              35 0000-0001-9297-7473 
primary 'Nango, E.'               36 0000-0001-9851-7355 
primary 'Iwata, S.'               37 0000-0003-1735-2937 
primary 'Royant, A.'              38 0000-0002-1919-8649 
primary 'Tsai, M.D.'              39 0000-0003-1374-0414 
primary 'Yamamoto, J.'            40 0000-0002-5036-991X 
primary 'Essen, L.O.'             41 0000-0003-4272-4026 
# 
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 'Cryptochrome photoreceptor'          57807.066 1   ? ? ? ? 
2 non-polymer syn 'DIHYDROFLAVINE-ADENINE DINUCLEOTIDE' 787.566   1   ? ? ? ? 
3 water       nat water                                 18.015    159 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGEKLAAALEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGEKLAAALEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIHYDROFLAVINE-ADENINE DINUCLEOTIDE' FDA 
3 water                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   GLY n 
1 4   VAL n 
1 5   LYS n 
1 6   ASN n 
1 7   SER n 
1 8   ILE n 
1 9   ILE n 
1 10  TRP n 
1 11  PHE n 
1 12  ARG n 
1 13  LYS n 
1 14  GLY n 
1 15  LEU n 
1 16  ARG n 
1 17  LEU n 
1 18  HIS n 
1 19  ASP n 
1 20  ASN n 
1 21  PRO n 
1 22  ALA n 
1 23  LEU n 
1 24  LEU n 
1 25  GLU n 
1 26  ALA n 
1 27  CYS n 
1 28  LYS n 
1 29  ASP n 
1 30  ALA n 
1 31  LYS n 
1 32  HIS n 
1 33  VAL n 
1 34  TYR n 
1 35  PRO n 
1 36  VAL n 
1 37  PHE n 
1 38  VAL n 
1 39  LEU n 
1 40  ASP n 
1 41  PRO n 
1 42  HIS n 
1 43  PHE n 
1 44  LEU n 
1 45  GLN n 
1 46  GLN n 
1 47  SER n 
1 48  SER n 
1 49  TYR n 
1 50  LYS n 
1 51  VAL n 
1 52  SER n 
1 53  VAL n 
1 54  ASN n 
1 55  ARG n 
1 56  TYR n 
1 57  ASN n 
1 58  PHE n 
1 59  LEU n 
1 60  LEU n 
1 61  GLU n 
1 62  SER n 
1 63  LEU n 
1 64  GLU n 
1 65  ASP n 
1 66  LEU n 
1 67  GLN n 
1 68  ARG n 
1 69  SER n 
1 70  PHE n 
1 71  GLN n 
1 72  ALA n 
1 73  ARG n 
1 74  GLY n 
1 75  SER n 
1 76  ARG n 
1 77  LEU n 
1 78  LEU n 
1 79  VAL n 
1 80  LEU n 
1 81  ARG n 
1 82  GLY n 
1 83  LYS n 
1 84  PRO n 
1 85  GLU n 
1 86  GLU n 
1 87  VAL n 
1 88  PHE n 
1 89  PRO n 
1 90  ARG n 
1 91  VAL n 
1 92  PHE n 
1 93  ARG n 
1 94  GLU n 
1 95  TRP n 
1 96  GLY n 
1 97  VAL n 
1 98  THR n 
1 99  GLN n 
1 100 LEU n 
1 101 CYS n 
1 102 PHE n 
1 103 GLU n 
1 104 HIS n 
1 105 ASP n 
1 106 THR n 
1 107 GLU n 
1 108 PRO n 
1 109 TYR n 
1 110 ALA n 
1 111 LYS n 
1 112 VAL n 
1 113 ARG n 
1 114 ASP n 
1 115 ALA n 
1 116 ALA n 
1 117 VAL n 
1 118 ARG n 
1 119 ARG n 
1 120 LEU n 
1 121 ALA n 
1 122 ALA n 
1 123 GLU n 
1 124 ALA n 
1 125 GLY n 
1 126 VAL n 
1 127 GLU n 
1 128 VAL n 
1 129 VAL n 
1 130 THR n 
1 131 PRO n 
1 132 ILE n 
1 133 SER n 
1 134 HIS n 
1 135 THR n 
1 136 LEU n 
1 137 TYR n 
1 138 ASP n 
1 139 THR n 
1 140 ASP n 
1 141 MET n 
1 142 LEU n 
1 143 VAL n 
1 144 ALA n 
1 145 ARG n 
1 146 ASN n 
1 147 GLY n 
1 148 GLY n 
1 149 ALA n 
1 150 ALA n 
1 151 PRO n 
1 152 LEU n 
1 153 THR n 
1 154 MET n 
1 155 GLN n 
1 156 SER n 
1 157 PHE n 
1 158 THR n 
1 159 LYS n 
1 160 LEU n 
1 161 VAL n 
1 162 ASP n 
1 163 ARG n 
1 164 VAL n 
1 165 GLY n 
1 166 ASP n 
1 167 PRO n 
1 168 PRO n 
1 169 ALA n 
1 170 PRO n 
1 171 ALA n 
1 172 PRO n 
1 173 ASP n 
1 174 PRO n 
1 175 PRO n 
1 176 ALA n 
1 177 ALA n 
1 178 MET n 
1 179 PRO n 
1 180 PRO n 
1 181 PRO n 
1 182 ALA n 
1 183 GLU n 
1 184 ASP n 
1 185 MET n 
1 186 PRO n 
1 187 SER n 
1 188 ALA n 
1 189 ALA n 
1 190 PRO n 
1 191 ALA n 
1 192 ALA n 
1 193 THR n 
1 194 GLY n 
1 195 VAL n 
1 196 PRO n 
1 197 THR n 
1 198 TRP n 
1 199 GLN n 
1 200 GLU n 
1 201 VAL n 
1 202 GLY n 
1 203 PHE n 
1 204 LYS n 
1 205 GLU n 
1 206 PRO n 
1 207 PRO n 
1 208 LEU n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 LYS n 
1 213 GLY n 
1 214 GLY n 
1 215 GLU n 
1 216 THR n 
1 217 GLU n 
1 218 ALA n 
1 219 LEU n 
1 220 ALA n 
1 221 ARG n 
1 222 LEU n 
1 223 GLU n 
1 224 ALA n 
1 225 ALA n 
1 226 PHE n 
1 227 GLN n 
1 228 ASP n 
1 229 PRO n 
1 230 LYS n 
1 231 TRP n 
1 232 VAL n 
1 233 ALA n 
1 234 GLY n 
1 235 PHE n 
1 236 GLN n 
1 237 LYS n 
1 238 PRO n 
1 239 ASP n 
1 240 THR n 
1 241 ASP n 
1 242 PRO n 
1 243 SER n 
1 244 ALA n 
1 245 TRP n 
1 246 GLU n 
1 247 LYS n 
1 248 PRO n 
1 249 ALA n 
1 250 THR n 
1 251 THR n 
1 252 VAL n 
1 253 LEU n 
1 254 SER n 
1 255 PRO n 
1 256 TYR n 
1 257 LEU n 
1 258 LYS n 
1 259 PHE n 
1 260 GLY n 
1 261 CYS n 
1 262 LEU n 
1 263 SER n 
1 264 ALA n 
1 265 ARG n 
1 266 LEU n 
1 267 PHE n 
1 268 HIS n 
1 269 ALA n 
1 270 ARG n 
1 271 LEU n 
1 272 LEU n 
1 273 GLU n 
1 274 VAL n 
1 275 TYR n 
1 276 ARG n 
1 277 ARG n 
1 278 HIS n 
1 279 PRO n 
1 280 ALA n 
1 281 HIS n 
1 282 SER n 
1 283 GLN n 
1 284 PRO n 
1 285 PRO n 
1 286 VAL n 
1 287 SER n 
1 288 LEU n 
1 289 ARG n 
1 290 GLY n 
1 291 GLN n 
1 292 LEU n 
1 293 LEU n 
1 294 TRP n 
1 295 ARG n 
1 296 GLU n 
1 297 PHE n 
1 298 PHE n 
1 299 TYR n 
1 300 THR n 
1 301 VAL n 
1 302 GLY n 
1 303 SER n 
1 304 THR n 
1 305 THR n 
1 306 PRO n 
1 307 ASN n 
1 308 PHE n 
1 309 HIS n 
1 310 ARG n 
1 311 MET n 
1 312 ALA n 
1 313 GLY n 
1 314 ASN n 
1 315 PRO n 
1 316 VAL n 
1 317 CYS n 
1 318 LYS n 
1 319 GLN n 
1 320 ILE n 
1 321 ASP n 
1 322 TRP n 
1 323 ASP n 
1 324 ASP n 
1 325 ASN n 
1 326 PRO n 
1 327 GLU n 
1 328 PHE n 
1 329 LEU n 
1 330 ALA n 
1 331 ALA n 
1 332 TRP n 
1 333 ARG n 
1 334 GLU n 
1 335 ALA n 
1 336 ARG n 
1 337 THR n 
1 338 GLY n 
1 339 PHE n 
1 340 PRO n 
1 341 TRP n 
1 342 ILE n 
1 343 ASP n 
1 344 ALA n 
1 345 ILE n 
1 346 MET n 
1 347 THR n 
1 348 GLN n 
1 349 LEU n 
1 350 VAL n 
1 351 THR n 
1 352 TRP n 
1 353 GLY n 
1 354 TRP n 
1 355 MET n 
1 356 HIS n 
1 357 HIS n 
1 358 LEU n 
1 359 ALA n 
1 360 ARG n 
1 361 HIS n 
1 362 SER n 
1 363 VAL n 
1 364 ALA n 
1 365 CYS n 
1 366 PHE n 
1 367 LEU n 
1 368 THR n 
1 369 ARG n 
1 370 GLY n 
1 371 ASP n 
1 372 LEU n 
1 373 TYR n 
1 374 VAL n 
1 375 SER n 
1 376 TRP n 
1 377 GLU n 
1 378 ARG n 
1 379 GLY n 
1 380 MET n 
1 381 GLU n 
1 382 VAL n 
1 383 PHE n 
1 384 GLU n 
1 385 GLU n 
1 386 HIS n 
1 387 LEU n 
1 388 ILE n 
1 389 ASP n 
1 390 GLN n 
1 391 ASP n 
1 392 HIS n 
1 393 TYR n 
1 394 LEU n 
1 395 ASN n 
1 396 ALA n 
1 397 ALA n 
1 398 ASN n 
1 399 TRP n 
1 400 MET n 
1 401 TRP n 
1 402 LEU n 
1 403 SER n 
1 404 ALA n 
1 405 SER n 
1 406 ALA n 
1 407 PHE n 
1 408 PHE n 
1 409 SER n 
1 410 GLN n 
1 411 TYR n 
1 412 PHE n 
1 413 ARG n 
1 414 VAL n 
1 415 TYR n 
1 416 SER n 
1 417 PRO n 
1 418 VAL n 
1 419 VAL n 
1 420 PHE n 
1 421 GLY n 
1 422 LYS n 
1 423 LYS n 
1 424 TYR n 
1 425 ASP n 
1 426 PRO n 
1 427 GLU n 
1 428 GLY n 
1 429 ARG n 
1 430 PHE n 
1 431 ILE n 
1 432 ARG n 
1 433 LYS n 
1 434 PHE n 
1 435 LEU n 
1 436 PRO n 
1 437 VAL n 
1 438 LEU n 
1 439 LYS n 
1 440 ASP n 
1 441 MET n 
1 442 PRO n 
1 443 ALA n 
1 444 LYS n 
1 445 TYR n 
1 446 ILE n 
1 447 TYR n 
1 448 GLU n 
1 449 PRO n 
1 450 TRP n 
1 451 THR n 
1 452 ALA n 
1 453 PRO n 
1 454 LEU n 
1 455 GLU n 
1 456 VAL n 
1 457 GLN n 
1 458 ARG n 
1 459 LYS n 
1 460 ALA n 
1 461 GLY n 
1 462 CYS n 
1 463 VAL n 
1 464 VAL n 
1 465 GLY n 
1 466 ARG n 
1 467 ASP n 
1 468 TYR n 
1 469 PRO n 
1 470 ALA n 
1 471 PRO n 
1 472 ILE n 
1 473 VAL n 
1 474 ASP n 
1 475 HIS n 
1 476 ALA n 
1 477 VAL n 
1 478 ALA n 
1 479 SER n 
1 480 LYS n 
1 481 ALA n 
1 482 CYS n 
1 483 ILE n 
1 484 ALA n 
1 485 ARG n 
1 486 MET n 
1 487 ALA n 
1 488 ALA n 
1 489 ALA n 
1 490 TYR n 
1 491 ARG n 
1 492 ARG n 
1 493 SER n 
1 494 LYS n 
1 495 GLY n 
1 496 GLU n 
1 497 LYS n 
1 498 LEU n 
1 499 ALA n 
1 500 ALA n 
1 501 ALA n 
1 502 LEU n 
1 503 GLU n 
1 504 HIS n 
1 505 HIS n 
1 506 HIS n 
1 507 HIS n 
1 508 HIS n 
1 509 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   509 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'UVR3, CHLRE_06g278251v5, CHLREDRAFT_206002' 
_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      'Chlamydomonas reinhardtii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3055 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                   ? 
# 
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 
FDA non-polymer         . 'DIHYDROFLAVINE-ADENINE DINUCLEOTIDE' ? 'C27 H35 N9 O15 P2' 787.566 
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 
SER 'L-peptide linking' y SERINE                                ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                             ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                            ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                              ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                ? 'C5 H11 N O2'       117.146 
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  CYS 27  27  27  CYS CYS A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  HIS 32  32  32  HIS HIS A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  HIS 42  42  42  HIS HIS A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  GLN 46  46  ?   ?   ?   A . n 
A 1 47  SER 47  47  ?   ?   ?   A . n 
A 1 48  SER 48  48  ?   ?   ?   A . n 
A 1 49  TYR 49  49  ?   ?   ?   A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  TYR 56  56  56  TYR TYR A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  GLN 71  71  71  GLN GLN A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  TRP 95  95  95  TRP TRP A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 MET 141 141 141 MET MET A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 MET 178 178 178 MET MET A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 TRP 198 198 198 TRP TRP A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 GLN 236 236 236 GLN GLN A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 ASP 241 241 241 ASP ASP A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 TRP 245 245 245 TRP TRP A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 CYS 261 261 261 CYS CYS A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 HIS 268 268 268 HIS HIS A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ARG 270 270 270 ARG ARG A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 HIS 278 278 278 HIS HIS A . n 
A 1 279 PRO 279 279 279 PRO PRO A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 HIS 281 281 281 HIS HIS A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 GLN 283 283 283 GLN GLN A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ARG 289 289 289 ARG ARG A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 TRP 294 294 294 TRP TRP A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 PRO 306 306 306 PRO PRO A . n 
A 1 307 ASN 307 307 307 ASN ASN A . n 
A 1 308 PHE 308 308 308 PHE PHE A . n 
A 1 309 HIS 309 309 309 HIS HIS A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 MET 311 311 311 MET MET A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 ASN 314 314 ?   ?   ?   A . n 
A 1 315 PRO 315 315 ?   ?   ?   A . n 
A 1 316 VAL 316 316 ?   ?   ?   A . n 
A 1 317 CYS 317 317 ?   ?   ?   A . n 
A 1 318 LYS 318 318 ?   ?   ?   A . n 
A 1 319 GLN 319 319 ?   ?   ?   A . n 
A 1 320 ILE 320 320 ?   ?   ?   A . n 
A 1 321 ASP 321 321 ?   ?   ?   A . n 
A 1 322 TRP 322 322 ?   ?   ?   A . n 
A 1 323 ASP 323 323 ?   ?   ?   A . n 
A 1 324 ASP 324 324 ?   ?   ?   A . n 
A 1 325 ASN 325 325 325 ASN ASN A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 ARG 336 336 336 ARG ARG A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 PRO 340 340 340 PRO PRO A . n 
A 1 341 TRP 341 341 341 TRP TRP A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 MET 346 346 346 MET MET A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 GLN 348 348 348 GLN GLN A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 TRP 352 352 352 TRP TRP A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 TRP 354 354 354 TRP TRP A . n 
A 1 355 MET 355 355 355 MET MET A . n 
A 1 356 HIS 356 356 356 HIS HIS A . n 
A 1 357 HIS 357 357 357 HIS HIS A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 ARG 360 360 360 ARG ARG A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 SER 362 362 362 SER SER A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 CYS 365 365 365 CYS CYS A . n 
A 1 366 PHE 366 366 366 PHE PHE A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 THR 368 368 368 THR THR A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 ASP 371 371 371 ASP ASP A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 TRP 376 376 376 TRP TRP A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 MET 380 380 380 MET MET A . n 
A 1 381 GLU 381 381 381 GLU GLU A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 PHE 383 383 383 PHE PHE A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 ILE 388 388 388 ILE ILE A . n 
A 1 389 ASP 389 389 389 ASP ASP A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 ASP 391 391 391 ASP ASP A . n 
A 1 392 HIS 392 392 392 HIS HIS A . n 
A 1 393 TYR 393 393 393 TYR TYR A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 ASN 398 398 398 ASN ASN A . n 
A 1 399 TRP 399 399 399 TRP TRP A . n 
A 1 400 MET 400 400 400 MET MET A . n 
A 1 401 TRP 401 401 401 TRP TRP A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 SER 403 403 403 SER SER A . n 
A 1 404 ALA 404 404 ?   ?   ?   A . n 
A 1 405 SER 405 405 ?   ?   ?   A . n 
A 1 406 ALA 406 406 ?   ?   ?   A . n 
A 1 407 PHE 407 407 ?   ?   ?   A . n 
A 1 408 PHE 408 408 ?   ?   ?   A . n 
A 1 409 SER 409 409 ?   ?   ?   A . n 
A 1 410 GLN 410 410 ?   ?   ?   A . n 
A 1 411 TYR 411 411 411 TYR TYR A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 VAL 414 414 414 VAL VAL A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 SER 416 416 416 SER SER A . n 
A 1 417 PRO 417 417 417 PRO PRO A . n 
A 1 418 VAL 418 418 418 VAL VAL A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 PHE 420 420 420 PHE PHE A . n 
A 1 421 GLY 421 421 421 GLY GLY A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 TYR 424 424 424 TYR TYR A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 PRO 426 426 426 PRO PRO A . n 
A 1 427 GLU 427 427 427 GLU GLU A . n 
A 1 428 GLY 428 428 428 GLY GLY A . n 
A 1 429 ARG 429 429 429 ARG ARG A . n 
A 1 430 PHE 430 430 430 PHE PHE A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ARG 432 432 432 ARG ARG A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 PHE 434 434 434 PHE PHE A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 PRO 436 436 436 PRO PRO A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 LEU 438 438 438 LEU LEU A . n 
A 1 439 LYS 439 439 439 LYS LYS A . n 
A 1 440 ASP 440 440 440 ASP ASP A . n 
A 1 441 MET 441 441 441 MET MET A . n 
A 1 442 PRO 442 442 442 PRO PRO A . n 
A 1 443 ALA 443 443 443 ALA ALA A . n 
A 1 444 LYS 444 444 444 LYS LYS A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 ILE 446 446 446 ILE ILE A . n 
A 1 447 TYR 447 447 447 TYR TYR A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 TRP 450 450 450 TRP TRP A . n 
A 1 451 THR 451 451 451 THR THR A . n 
A 1 452 ALA 452 452 452 ALA ALA A . n 
A 1 453 PRO 453 453 453 PRO PRO A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 GLN 457 457 457 GLN GLN A . n 
A 1 458 ARG 458 458 458 ARG ARG A . n 
A 1 459 LYS 459 459 459 LYS LYS A . n 
A 1 460 ALA 460 460 460 ALA ALA A . n 
A 1 461 GLY 461 461 461 GLY GLY A . n 
A 1 462 CYS 462 462 462 CYS CYS A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 VAL 464 464 464 VAL VAL A . n 
A 1 465 GLY 465 465 465 GLY GLY A . n 
A 1 466 ARG 466 466 466 ARG ARG A . n 
A 1 467 ASP 467 467 467 ASP ASP A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 PRO 469 469 469 PRO PRO A . n 
A 1 470 ALA 470 470 470 ALA ALA A . n 
A 1 471 PRO 471 471 471 PRO PRO A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 VAL 473 473 473 VAL VAL A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 HIS 475 475 475 HIS HIS A . n 
A 1 476 ALA 476 476 ?   ?   ?   A . n 
A 1 477 VAL 477 477 ?   ?   ?   A . n 
A 1 478 ALA 478 478 ?   ?   ?   A . n 
A 1 479 SER 479 479 ?   ?   ?   A . n 
A 1 480 LYS 480 480 ?   ?   ?   A . n 
A 1 481 ALA 481 481 ?   ?   ?   A . n 
A 1 482 CYS 482 482 ?   ?   ?   A . n 
A 1 483 ILE 483 483 ?   ?   ?   A . n 
A 1 484 ALA 484 484 ?   ?   ?   A . n 
A 1 485 ARG 485 485 ?   ?   ?   A . n 
A 1 486 MET 486 486 ?   ?   ?   A . n 
A 1 487 ALA 487 487 ?   ?   ?   A . n 
A 1 488 ALA 488 488 ?   ?   ?   A . n 
A 1 489 ALA 489 489 ?   ?   ?   A . n 
A 1 490 TYR 490 490 ?   ?   ?   A . n 
A 1 491 ARG 491 491 ?   ?   ?   A . n 
A 1 492 ARG 492 492 ?   ?   ?   A . n 
A 1 493 SER 493 493 ?   ?   ?   A . n 
A 1 494 LYS 494 494 ?   ?   ?   A . n 
A 1 495 GLY 495 495 ?   ?   ?   A . n 
A 1 496 GLU 496 496 ?   ?   ?   A . n 
A 1 497 LYS 497 497 ?   ?   ?   A . n 
A 1 498 LEU 498 498 ?   ?   ?   A . n 
A 1 499 ALA 499 499 ?   ?   ?   A . n 
A 1 500 ALA 500 500 ?   ?   ?   A . n 
A 1 501 ALA 501 501 ?   ?   ?   A . n 
A 1 502 LEU 502 502 ?   ?   ?   A . n 
A 1 503 GLU 503 503 ?   ?   ?   A . n 
A 1 504 HIS 504 504 ?   ?   ?   A . n 
A 1 505 HIS 505 505 ?   ?   ?   A . n 
A 1 506 HIS 506 506 ?   ?   ?   A . n 
A 1 507 HIS 507 507 ?   ?   ?   A . n 
A 1 508 HIS 508 508 ?   ?   ?   A . n 
A 1 509 HIS 509 509 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FDA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FDA 
_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 
B 2 FDA 1   601 601 FDA FDA A . 
C 3 HOH 1   701 45  HOH HOH A . 
C 3 HOH 2   702 19  HOH HOH A . 
C 3 HOH 3   703 14  HOH HOH A . 
C 3 HOH 4   704 108 HOH HOH A . 
C 3 HOH 5   705 81  HOH HOH A . 
C 3 HOH 6   706 139 HOH HOH A . 
C 3 HOH 7   707 123 HOH HOH A . 
C 3 HOH 8   708 154 HOH HOH A . 
C 3 HOH 9   709 140 HOH HOH A . 
C 3 HOH 10  710 12  HOH HOH A . 
C 3 HOH 11  711 95  HOH HOH A . 
C 3 HOH 12  712 80  HOH HOH A . 
C 3 HOH 13  713 134 HOH HOH A . 
C 3 HOH 14  714 165 HOH HOH A . 
C 3 HOH 15  715 27  HOH HOH A . 
C 3 HOH 16  716 20  HOH HOH A . 
C 3 HOH 17  717 5   HOH HOH A . 
C 3 HOH 18  718 36  HOH HOH A . 
C 3 HOH 19  719 131 HOH HOH A . 
C 3 HOH 20  720 55  HOH HOH A . 
C 3 HOH 21  721 127 HOH HOH A . 
C 3 HOH 22  722 44  HOH HOH A . 
C 3 HOH 23  723 128 HOH HOH A . 
C 3 HOH 24  724 153 HOH HOH A . 
C 3 HOH 25  725 23  HOH HOH A . 
C 3 HOH 26  726 48  HOH HOH A . 
C 3 HOH 27  727 157 HOH HOH A . 
C 3 HOH 28  728 116 HOH HOH A . 
C 3 HOH 29  729 11  HOH HOH A . 
C 3 HOH 30  730 43  HOH HOH A . 
C 3 HOH 31  731 49  HOH HOH A . 
C 3 HOH 32  732 69  HOH HOH A . 
C 3 HOH 33  733 166 HOH HOH A . 
C 3 HOH 34  734 84  HOH HOH A . 
C 3 HOH 35  735 74  HOH HOH A . 
C 3 HOH 36  736 103 HOH HOH A . 
C 3 HOH 37  737 64  HOH HOH A . 
C 3 HOH 38  738 102 HOH HOH A . 
C 3 HOH 39  739 122 HOH HOH A . 
C 3 HOH 40  740 3   HOH HOH A . 
C 3 HOH 41  741 88  HOH HOH A . 
C 3 HOH 42  742 28  HOH HOH A . 
C 3 HOH 43  743 29  HOH HOH A . 
C 3 HOH 44  744 1   HOH HOH A . 
C 3 HOH 45  745 66  HOH HOH A . 
C 3 HOH 46  746 67  HOH HOH A . 
C 3 HOH 47  747 70  HOH HOH A . 
C 3 HOH 48  748 92  HOH HOH A . 
C 3 HOH 49  749 39  HOH HOH A . 
C 3 HOH 50  750 71  HOH HOH A . 
C 3 HOH 51  751 54  HOH HOH A . 
C 3 HOH 52  752 68  HOH HOH A . 
C 3 HOH 53  753 75  HOH HOH A . 
C 3 HOH 54  754 21  HOH HOH A . 
C 3 HOH 55  755 34  HOH HOH A . 
C 3 HOH 56  756 126 HOH HOH A . 
C 3 HOH 57  757 152 HOH HOH A . 
C 3 HOH 58  758 25  HOH HOH A . 
C 3 HOH 59  759 72  HOH HOH A . 
C 3 HOH 60  760 98  HOH HOH A . 
C 3 HOH 61  761 2   HOH HOH A . 
C 3 HOH 62  762 7   HOH HOH A . 
C 3 HOH 63  763 99  HOH HOH A . 
C 3 HOH 64  764 63  HOH HOH A . 
C 3 HOH 65  765 9   HOH HOH A . 
C 3 HOH 66  766 90  HOH HOH A . 
C 3 HOH 67  767 78  HOH HOH A . 
C 3 HOH 68  768 65  HOH HOH A . 
C 3 HOH 69  769 161 HOH HOH A . 
C 3 HOH 70  770 40  HOH HOH A . 
C 3 HOH 71  771 132 HOH HOH A . 
C 3 HOH 72  772 37  HOH HOH A . 
C 3 HOH 73  773 105 HOH HOH A . 
C 3 HOH 74  774 47  HOH HOH A . 
C 3 HOH 75  775 26  HOH HOH A . 
C 3 HOH 76  776 6   HOH HOH A . 
C 3 HOH 77  777 79  HOH HOH A . 
C 3 HOH 78  778 156 HOH HOH A . 
C 3 HOH 79  779 94  HOH HOH A . 
C 3 HOH 80  780 58  HOH HOH A . 
C 3 HOH 81  781 93  HOH HOH A . 
C 3 HOH 82  782 155 HOH HOH A . 
C 3 HOH 83  783 82  HOH HOH A . 
C 3 HOH 84  784 129 HOH HOH A . 
C 3 HOH 85  785 4   HOH HOH A . 
C 3 HOH 86  786 18  HOH HOH A . 
C 3 HOH 87  787 142 HOH HOH A . 
C 3 HOH 88  788 163 HOH HOH A . 
C 3 HOH 89  789 117 HOH HOH A . 
C 3 HOH 90  790 59  HOH HOH A . 
C 3 HOH 91  791 150 HOH HOH A . 
C 3 HOH 92  792 42  HOH HOH A . 
C 3 HOH 93  793 91  HOH HOH A . 
C 3 HOH 94  794 46  HOH HOH A . 
C 3 HOH 95  795 17  HOH HOH A . 
C 3 HOH 96  796 113 HOH HOH A . 
C 3 HOH 97  797 111 HOH HOH A . 
C 3 HOH 98  798 13  HOH HOH A . 
C 3 HOH 99  799 31  HOH HOH A . 
C 3 HOH 100 800 10  HOH HOH A . 
C 3 HOH 101 801 53  HOH HOH A . 
C 3 HOH 102 802 32  HOH HOH A . 
C 3 HOH 103 803 135 HOH HOH A . 
C 3 HOH 104 804 8   HOH HOH A . 
C 3 HOH 105 805 87  HOH HOH A . 
C 3 HOH 106 806 120 HOH HOH A . 
C 3 HOH 107 807 158 HOH HOH A . 
C 3 HOH 108 808 125 HOH HOH A . 
C 3 HOH 109 809 133 HOH HOH A . 
C 3 HOH 110 810 76  HOH HOH A . 
C 3 HOH 111 811 119 HOH HOH A . 
C 3 HOH 112 812 22  HOH HOH A . 
C 3 HOH 113 813 137 HOH HOH A . 
C 3 HOH 114 814 57  HOH HOH A . 
C 3 HOH 115 815 148 HOH HOH A . 
C 3 HOH 116 816 77  HOH HOH A . 
C 3 HOH 117 817 38  HOH HOH A . 
C 3 HOH 118 818 73  HOH HOH A . 
C 3 HOH 119 819 112 HOH HOH A . 
C 3 HOH 120 820 145 HOH HOH A . 
C 3 HOH 121 821 106 HOH HOH A . 
C 3 HOH 122 822 167 HOH HOH A . 
C 3 HOH 123 823 141 HOH HOH A . 
C 3 HOH 124 824 104 HOH HOH A . 
C 3 HOH 125 825 96  HOH HOH A . 
C 3 HOH 126 826 51  HOH HOH A . 
C 3 HOH 127 827 143 HOH HOH A . 
C 3 HOH 128 828 110 HOH HOH A . 
C 3 HOH 129 829 107 HOH HOH A . 
C 3 HOH 130 830 86  HOH HOH A . 
C 3 HOH 131 831 159 HOH HOH A . 
C 3 HOH 132 832 138 HOH HOH A . 
C 3 HOH 133 833 114 HOH HOH A . 
C 3 HOH 134 834 35  HOH HOH A . 
C 3 HOH 135 835 83  HOH HOH A . 
C 3 HOH 136 836 61  HOH HOH A . 
C 3 HOH 137 837 89  HOH HOH A . 
C 3 HOH 138 838 101 HOH HOH A . 
C 3 HOH 139 839 52  HOH HOH A . 
C 3 HOH 140 840 115 HOH HOH A . 
C 3 HOH 141 841 30  HOH HOH A . 
C 3 HOH 142 842 146 HOH HOH A . 
C 3 HOH 143 843 109 HOH HOH A . 
C 3 HOH 144 844 33  HOH HOH A . 
C 3 HOH 145 845 60  HOH HOH A . 
C 3 HOH 146 846 15  HOH HOH A . 
C 3 HOH 147 847 41  HOH HOH A . 
C 3 HOH 148 848 121 HOH HOH A . 
C 3 HOH 149 849 147 HOH HOH A . 
C 3 HOH 150 850 56  HOH HOH A . 
C 3 HOH 151 851 124 HOH HOH A . 
C 3 HOH 152 852 97  HOH HOH A . 
C 3 HOH 153 853 50  HOH HOH A . 
C 3 HOH 154 854 136 HOH HOH A . 
C 3 HOH 155 855 62  HOH HOH A . 
C 3 HOH 156 856 130 HOH HOH A . 
C 3 HOH 157 857 144 HOH HOH A . 
C 3 HOH 158 858 85  HOH HOH A . 
C 3 HOH 159 859 16  HOH HOH A . 
# 
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 0 A LYS 28  ? NZ  ? A LYS 28  NZ  
2  1 Y 0 A PHE 43  ? N   ? A PHE 43  N   
3  1 Y 1 A LYS 50  ? CG  ? A LYS 50  CG  
4  1 Y 1 A LYS 50  ? CD  ? A LYS 50  CD  
5  1 Y 1 A LYS 50  ? CE  ? A LYS 50  CE  
6  1 Y 1 A LYS 50  ? NZ  ? A LYS 50  NZ  
7  1 Y 0 A GLU 85  ? CD  ? A GLU 85  CD  
8  1 Y 0 A GLN 155 ? CD  ? A GLN 155 CD  
9  1 Y 0 A LYS 230 ? CG  ? A LYS 230 CG  
10 1 Y 0 A LYS 230 ? CD  ? A LYS 230 CD  
11 1 Y 0 A LYS 230 ? CE  ? A LYS 230 CE  
12 1 Y 0 A LYS 230 ? NZ  ? A LYS 230 NZ  
13 1 Y 0 A ARG 277 ? CG  ? A ARG 277 CG  
14 1 Y 0 A ARG 277 ? CD  ? A ARG 277 CD  
15 1 Y 0 A ARG 277 ? NE  ? A ARG 277 NE  
16 1 Y 0 A ARG 277 ? CZ  ? A ARG 277 CZ  
17 1 Y 0 A ARG 277 ? NH1 ? A ARG 277 NH1 
18 1 Y 0 A ARG 277 ? NH2 ? A ARG 277 NH2 
19 1 Y 1 A HIS 475 ? CA  ? A HIS 475 CA  
20 1 Y 1 A HIS 475 ? C   ? A HIS 475 C   
21 1 Y 1 A HIS 475 ? O   ? A HIS 475 O   
22 1 Y 1 A HIS 475 ? CB  ? A HIS 475 CB  
23 1 Y 1 A HIS 475 ? CG  ? A HIS 475 CG  
24 1 Y 1 A HIS 475 ? ND1 ? A HIS 475 ND1 
25 1 Y 1 A HIS 475 ? CD2 ? A HIS 475 CD2 
26 1 Y 1 A HIS 475 ? CE1 ? A HIS 475 CE1 
27 1 Y 1 A HIS 475 ? NE2 ? A HIS 475 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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZLR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.590 
_cell.length_a_esd                 ? 
_cell.length_b                     65.980 
_cell.length_b_esd                 ? 
_cell.length_c                     148.720 
_cell.length_c_esd                 ? 
_cell.volume                       496416.682 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZLR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZLR 
_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             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.71 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 5.6 (w/v) PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         MPCCD 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-10-25 
_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   1.24 
_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                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SACLA BEAMLINE BL2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.24 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL2 
_diffrn_source.pdbx_synchrotron_site       SACLA 
# 
_reflns.B_iso_Wilson_estimate                          46.96 
_reflns.entry_id                                       8ZLR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.13 
_reflns.d_resolution_low                               41.83 
_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                                     29512 
_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                           99.89 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                450 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.911 
_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                                   0.9981 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.13 
_reflns_shell.d_res_low                                     2.17 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.58 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1688 
_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                               70 
_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                                  0.5348 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               57.39 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZLR 
_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                            2.15 
_refine.ls_d_res_low                             41.83 
_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                     27882 
_refine.ls_number_reflns_R_free                  1414 
_refine.ls_number_reflns_R_work                  26468 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1823 
_refine.ls_R_factor_R_free                       0.2197 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1802 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      6FN3 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 21.7377 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2470 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        41.83 
_refine_hist.number_atoms_solvent             159 
_refine_hist.number_atoms_total               3830 
_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        3618 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_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' ? 0.0055  ? 3915 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6289  ? 5370 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0407  ? 566  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0069  ? 689  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.5326 ? 1431 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.15 2.23  . . 131 2602 99.89  . . . . 0.2624 . . . . . . . . . . . 0.3659 
'X-RAY DIFFRACTION' 2.23 2.32  . . 139 2619 100.00 . . . . 0.2200 . . . . . . . . . . . 0.2576 
'X-RAY DIFFRACTION' 2.32 2.42  . . 138 2597 99.96  . . . . 0.2025 . . . . . . . . . . . 0.2542 
'X-RAY DIFFRACTION' 2.42 2.55  . . 143 2608 100.00 . . . . 0.1952 . . . . . . . . . . . 0.2305 
'X-RAY DIFFRACTION' 2.55 2.71  . . 119 2625 100.00 . . . . 0.1958 . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 2.71 2.92  . . 157 2599 100.00 . . . . 0.1966 . . . . . . . . . . . 0.3176 
'X-RAY DIFFRACTION' 2.92 3.21  . . 141 2655 100.00 . . . . 0.1955 . . . . . . . . . . . 0.2714 
'X-RAY DIFFRACTION' 3.21 3.68  . . 137 2663 100.00 . . . . 0.1763 . . . . . . . . . . . 0.2058 
'X-RAY DIFFRACTION' 3.68 4.63  . . 144 2697 100.00 . . . . 0.1500 . . . . . . . . . . . 0.1763 
'X-RAY DIFFRACTION' 4.63 41.83 . . 165 2803 100.00 . . . . 0.1778 . . . . . . . . . . . 0.2042 
# 
_struct.entry_id                     8ZLR 
_struct.title                        'SFX structure of CraCRY in the semiquinone state' 
_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        8ZLR 
_struct_keywords.text            'photoreceptor, FLAVOPROTEIN, time-resolved crystallography, semiquinone state' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A8J8W0_CHLRE 
_struct_ref.pdbx_db_accession          A8J8W0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZLR 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 496 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A8J8W0 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  496 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       496 
# 
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 8ZLR LYS A 497 ? UNP A8J8W0 ? ? 'expression tag' 497 1  
1 8ZLR LEU A 498 ? UNP A8J8W0 ? ? 'expression tag' 498 2  
1 8ZLR ALA A 499 ? UNP A8J8W0 ? ? 'expression tag' 499 3  
1 8ZLR ALA A 500 ? UNP A8J8W0 ? ? 'expression tag' 500 4  
1 8ZLR ALA A 501 ? UNP A8J8W0 ? ? 'expression tag' 501 5  
1 8ZLR LEU A 502 ? UNP A8J8W0 ? ? 'expression tag' 502 6  
1 8ZLR GLU A 503 ? UNP A8J8W0 ? ? 'expression tag' 503 7  
1 8ZLR HIS A 504 ? UNP A8J8W0 ? ? 'expression tag' 504 8  
1 8ZLR HIS A 505 ? UNP A8J8W0 ? ? 'expression tag' 505 9  
1 8ZLR HIS A 506 ? UNP A8J8W0 ? ? 'expression tag' 506 10 
1 8ZLR HIS A 507 ? UNP A8J8W0 ? ? 'expression tag' 507 11 
1 8ZLR HIS A 508 ? UNP A8J8W0 ? ? 'expression tag' 508 12 
1 8ZLR HIS A 509 ? UNP A8J8W0 ? ? 'expression tag' 509 13 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1250  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  19740 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 20  ? LYS A 28  ? ASN A 20  LYS A 28  1 ? 9  
HELX_P HELX_P2  AA2 SER A 52  ? ARG A 73  ? SER A 52  ARG A 73  1 ? 22 
HELX_P HELX_P3  AA3 LYS A 83  ? GLY A 96  ? LYS A 83  GLY A 96  1 ? 14 
HELX_P HELX_P4  AA4 GLU A 107 ? ALA A 124 ? GLU A 107 ALA A 124 1 ? 18 
HELX_P HELX_P5  AA5 ASP A 138 ? ASN A 146 ? ASP A 138 ASN A 146 1 ? 9  
HELX_P HELX_P6  AA6 THR A 153 ? GLY A 165 ? THR A 153 GLY A 165 1 ? 13 
HELX_P HELX_P7  AA7 MET A 185 ? THR A 193 ? MET A 185 THR A 193 5 ? 9  
HELX_P HELX_P8  AA8 GLY A 214 ? PHE A 226 ? GLY A 214 PHE A 226 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 228 ? PHE A 235 ? ASP A 228 PHE A 235 1 ? 8  
HELX_P HELX_P10 AB1 GLN A 236 ? THR A 240 ? GLN A 236 THR A 240 5 ? 5  
HELX_P HELX_P11 AB2 LEU A 253 ? PHE A 259 ? LEU A 253 PHE A 259 1 ? 7  
HELX_P HELX_P12 AB3 SER A 263 ? HIS A 278 ? SER A 263 HIS A 278 1 ? 16 
HELX_P HELX_P13 AB4 SER A 287 ? THR A 305 ? SER A 287 THR A 305 1 ? 19 
HELX_P HELX_P14 AB5 ASN A 307 ? MET A 311 ? ASN A 307 MET A 311 5 ? 5  
HELX_P HELX_P15 AB6 PRO A 326 ? GLU A 334 ? PRO A 326 GLU A 334 1 ? 9  
HELX_P HELX_P16 AB7 PHE A 339 ? GLY A 353 ? PHE A 339 GLY A 353 1 ? 15 
HELX_P HELX_P17 AB8 HIS A 356 ? THR A 368 ? HIS A 356 THR A 368 1 ? 13 
HELX_P HELX_P18 AB9 SER A 375 ? LEU A 387 ? SER A 375 LEU A 387 1 ? 13 
HELX_P HELX_P19 AC1 ASP A 391 ? SER A 403 ? ASP A 391 SER A 403 1 ? 13 
HELX_P HELX_P20 AC2 SER A 416 ? TYR A 424 ? SER A 416 TYR A 424 5 ? 9  
HELX_P HELX_P21 AC3 GLY A 428 ? LEU A 435 ? GLY A 428 LEU A 435 1 ? 8  
HELX_P HELX_P22 AC4 PRO A 436 ? LYS A 439 ? PRO A 436 LYS A 439 5 ? 4  
HELX_P HELX_P23 AC5 PRO A 442 ? ILE A 446 ? PRO A 442 ILE A 446 5 ? 5  
HELX_P HELX_P24 AC6 GLU A 448 ? ALA A 452 ? GLU A 448 ALA A 452 5 ? 5  
HELX_P HELX_P25 AC7 PRO A 453 ? GLY A 461 ? PRO A 453 GLY A 461 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           284 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            284 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    285 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     285 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.93 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
# 
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 LEU A 78  ? ARG A 81  ? LEU A 78  ARG A 81  
AA1 2 HIS A 32  ? LEU A 39  ? HIS A 32  LEU A 39  
AA1 3 ASN A 6   ? PHE A 11  ? ASN A 6   PHE A 11  
AA1 4 GLN A 99  ? PHE A 102 ? GLN A 99  PHE A 102 
AA1 5 GLU A 127 ? VAL A 129 ? GLU A 127 VAL A 129 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 80  ? O LEU A 80  N LEU A 39  ? N LEU A 39  
AA1 2 3 O VAL A 36  ? O VAL A 36  N PHE A 11  ? N PHE A 11  
AA1 3 4 N ILE A 8   ? N ILE A 8   O CYS A 101 ? O CYS A 101 
AA1 4 5 N LEU A 100 ? N LEU A 100 O GLU A 127 ? O GLU A 127 
# 
_pdbx_entry_details.entry_id                   8ZLR 
_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   N 
# 
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 ARG A 12  ? ? -120.75 -65.47  
2 1 HIS A 42  ? ? -94.66  58.38   
3 1 SER A 75  ? ? -125.98 -166.64 
4 1 ARG A 369 ? ? -67.28  5.04    
5 1 TYR A 373 ? B 57.52   -95.19  
6 1 VAL A 374 ? B 44.51   -171.28 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 16.5586906121  -11.4942292732 12.4275818055 0.376816235188 ? -0.0596516140139 ? 0.0143316083659  ? 
0.34958998041  ? -0.0269714945437 ? 0.263086438222 ? 6.47674141218  ? -3.17872659523 ? 0.842613306959  ? 7.70752988671 ? 
0.432217034494  ? 2.8407932143   ? -0.000307870448861 ? -0.1822841761   ? -0.329743005929  ? 0.230825697258  ? -0.0198950595781 ? 
0.277106457796   ? 0.0780596147453   ? 0.134003586359   ? 0.0684673941559   ? 
2 'X-RAY DIFFRACTION' ? refined 18.8939923182  0.156560653941 16.753668181  0.354529870424 ? 0.00438897715832 ? 0.00582512443892 ? 
0.427584831529 ? -0.0172635019461 ? 0.361168108202 ? 0.918946997943 ? 0.426927223496 ? -0.122886627794 ? 2.67333838015 ? 
0.201138526233  ? 0.330089022802 ? 0.0599369815066    ? -0.07713786791  ? -0.0338159733193 ? 0.0323400134718 ? -0.0561927810149 ? 
-0.0798179497333 ? -0.00596566689714 ? -0.0106157049336 ? -0.00332320367414 ? 
3 'X-RAY DIFFRACTION' ? refined 2.0384386412   15.5591475102  28.4838573679 0.367387765686 ? -0.0316549286405 ? 0.0595439480382  ? 
0.423316369791 ? 0.0129232778511  ? 0.396960071641 ? 3.92403457073  ? -1.3355718339  ? 0.599825215495  ? 5.12984461057 ? 
-0.844418746044 ? 0.807461780323 ? -0.20471279016     ? -0.603234030326 ? -0.534335634397  ? 0.615171513645  ? 0.0477224252827  ? 
0.490938084979   ? 0.089729362777    ? -0.209386654845  ? 0.239560190499    ? 
4 'X-RAY DIFFRACTION' ? refined 0.935294108552 27.5792319295  21.9870868694 0.355130444271 ? -0.0473519412909 ? 0.0373788491952  ? 
0.432802409232 ? -0.0300619197517 ? 0.387092932825 ? 4.34678326998  ? -3.72255662639 ? 0.929599496589  ? 6.62696711732 ? 
-1.00675720614  ? 0.787453982009 ? -0.228562054576    ? -0.182494803075 ? 0.288694866751   ? 0.383979996023  ? 0.179110092328   ? 
0.0195278874175  ? -0.206394585106   ? -0.0375444598262 ? 0.017005325378    ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 3   ? A 46  A 52  ? ? 
;chain 'A' and (resid 3 through 52 )
;
2 'X-RAY DIFFRACTION' 2 A 47  A 53  ? A 298 A 304 ? ? 
;chain 'A' and (resid 53 through 304 )
;
3 'X-RAY DIFFRACTION' 3 A 299 A 305 ? A 369 A 386 ? ? 
;chain 'A' and (resid 305 through 386 )
;
4 'X-RAY DIFFRACTION' 4 A 370 A 387 ? A 451 A 475 ? ? 
;chain 'A' and (resid 387 through 475 )
;
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A GLN 46  ? A GLN 46  
4  1 Y 1 A SER 47  ? A SER 47  
5  1 Y 1 A SER 48  ? A SER 48  
6  1 Y 1 A TYR 49  ? A TYR 49  
7  1 Y 1 A ASN 314 ? A ASN 314 
8  1 Y 1 A PRO 315 ? A PRO 315 
9  1 Y 1 A VAL 316 ? A VAL 316 
10 1 Y 1 A CYS 317 ? A CYS 317 
11 1 Y 1 A LYS 318 ? A LYS 318 
12 1 Y 1 A GLN 319 ? A GLN 319 
13 1 Y 1 A ILE 320 ? A ILE 320 
14 1 Y 1 A ASP 321 ? A ASP 321 
15 1 Y 1 A TRP 322 ? A TRP 322 
16 1 Y 1 A ASP 323 ? A ASP 323 
17 1 Y 1 A ASP 324 ? A ASP 324 
18 1 Y 1 A ALA 404 ? A ALA 404 
19 1 Y 1 A SER 405 ? A SER 405 
20 1 Y 1 A ALA 406 ? A ALA 406 
21 1 Y 1 A PHE 407 ? A PHE 407 
22 1 Y 1 A PHE 408 ? A PHE 408 
23 1 Y 1 A SER 409 ? A SER 409 
24 1 Y 1 A GLN 410 ? A GLN 410 
25 1 Y 1 A ALA 476 ? A ALA 476 
26 1 Y 1 A VAL 477 ? A VAL 477 
27 1 Y 1 A ALA 478 ? A ALA 478 
28 1 Y 1 A SER 479 ? A SER 479 
29 1 Y 1 A LYS 480 ? A LYS 480 
30 1 Y 1 A ALA 481 ? A ALA 481 
31 1 Y 1 A CYS 482 ? A CYS 482 
32 1 Y 1 A ILE 483 ? A ILE 483 
33 1 Y 1 A ALA 484 ? A ALA 484 
34 1 Y 1 A ARG 485 ? A ARG 485 
35 1 Y 1 A MET 486 ? A MET 486 
36 1 Y 1 A ALA 487 ? A ALA 487 
37 1 Y 1 A ALA 488 ? A ALA 488 
38 1 Y 1 A ALA 489 ? A ALA 489 
39 1 Y 1 A TYR 490 ? A TYR 490 
40 1 Y 1 A ARG 491 ? A ARG 491 
41 1 Y 1 A ARG 492 ? A ARG 492 
42 1 Y 1 A SER 493 ? A SER 493 
43 1 Y 1 A LYS 494 ? A LYS 494 
44 1 Y 1 A GLY 495 ? A GLY 495 
45 1 Y 1 A GLU 496 ? A GLU 496 
46 1 Y 1 A LYS 497 ? A LYS 497 
47 1 Y 1 A LEU 498 ? A LEU 498 
48 1 Y 1 A ALA 499 ? A ALA 499 
49 1 Y 1 A ALA 500 ? A ALA 500 
50 1 Y 1 A ALA 501 ? A ALA 501 
51 1 Y 1 A LEU 502 ? A LEU 502 
52 1 Y 1 A GLU 503 ? A GLU 503 
53 1 Y 1 A HIS 504 ? A HIS 504 
54 1 Y 1 A HIS 505 ? A HIS 505 
55 1 Y 1 A HIS 506 ? A HIS 506 
56 1 Y 1 A HIS 507 ? A HIS 507 
57 1 Y 1 A HIS 508 ? A HIS 508 
58 1 Y 1 A HIS 509 ? A HIS 509 
# 
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  
FDA PA     P N S 88  
FDA O1A    O N N 89  
FDA O2A    O N N 90  
FDA O5B    O N N 91  
FDA C5B    C N N 92  
FDA C4B    C N R 93  
FDA O4B    O N N 94  
FDA C3B    C N S 95  
FDA O3B    O N N 96  
FDA C2B    C N R 97  
FDA O2B    O N N 98  
FDA C1B    C N R 99  
FDA N9A    N Y N 100 
FDA C8A    C Y N 101 
FDA N7A    N Y N 102 
FDA C5A    C Y N 103 
FDA C6A    C Y N 104 
FDA N6A    N N N 105 
FDA N1A    N Y N 106 
FDA C2A    C Y N 107 
FDA N3A    N Y N 108 
FDA C4A    C Y N 109 
FDA N1     N N N 110 
FDA C2     C N N 111 
FDA O2     O N N 112 
FDA N3     N N N 113 
FDA C4     C N N 114 
FDA O4     O N N 115 
FDA C4X    C N N 116 
FDA N5     N N N 117 
FDA C5X    C Y N 118 
FDA C6     C Y N 119 
FDA C7     C Y N 120 
FDA C7M    C N N 121 
FDA C8     C Y N 122 
FDA C8M    C N N 123 
FDA C9     C Y N 124 
FDA C9A    C Y N 125 
FDA N10    N N N 126 
FDA C10    C N N 127 
FDA "C1'"  C N N 128 
FDA "C2'"  C N S 129 
FDA "O2'"  O N N 130 
FDA "C3'"  C N S 131 
FDA "O3'"  O N N 132 
FDA "C4'"  C N R 133 
FDA "O4'"  O N N 134 
FDA "C5'"  C N N 135 
FDA "O5'"  O N N 136 
FDA P      P N R 137 
FDA O1P    O N N 138 
FDA O2P    O N N 139 
FDA O3P    O N N 140 
FDA HOA2   H N N 141 
FDA H51A   H N N 142 
FDA H52A   H N N 143 
FDA H4B    H N N 144 
FDA H3B    H N N 145 
FDA HO3A   H N N 146 
FDA H2B    H N N 147 
FDA HO2A   H N N 148 
FDA H1B    H N N 149 
FDA H8A    H N N 150 
FDA H61A   H N N 151 
FDA H62A   H N N 152 
FDA H2A    H N N 153 
FDA HN1    H N N 154 
FDA HN3    H N N 155 
FDA HN5    H N N 156 
FDA H6     H N N 157 
FDA HM71   H N N 158 
FDA HM72   H N N 159 
FDA HM73   H N N 160 
FDA HM81   H N N 161 
FDA HM82   H N N 162 
FDA HM83   H N N 163 
FDA H9     H N N 164 
FDA "H1'1" H N N 165 
FDA "H1'2" H N N 166 
FDA "H2'"  H N N 167 
FDA "HO2'" H N N 168 
FDA "H3'"  H N N 169 
FDA "HO3'" H N N 170 
FDA "H4'"  H N N 171 
FDA "HO4'" H N N 172 
FDA "H5'1" H N N 173 
FDA "H5'2" H N N 174 
FDA HOP2   H N N 175 
GLN N      N N N 176 
GLN CA     C N S 177 
GLN C      C N N 178 
GLN O      O N N 179 
GLN CB     C N N 180 
GLN CG     C N N 181 
GLN CD     C N N 182 
GLN OE1    O N N 183 
GLN NE2    N N N 184 
GLN OXT    O N N 185 
GLN H      H N N 186 
GLN H2     H N N 187 
GLN HA     H N N 188 
GLN HB2    H N N 189 
GLN HB3    H N N 190 
GLN HG2    H N N 191 
GLN HG3    H N N 192 
GLN HE21   H N N 193 
GLN HE22   H N N 194 
GLN HXT    H N N 195 
GLU N      N N N 196 
GLU CA     C N S 197 
GLU C      C N N 198 
GLU O      O N N 199 
GLU CB     C N N 200 
GLU CG     C N N 201 
GLU CD     C N N 202 
GLU OE1    O N N 203 
GLU OE2    O N N 204 
GLU OXT    O N N 205 
GLU H      H N N 206 
GLU H2     H N N 207 
GLU HA     H N N 208 
GLU HB2    H N N 209 
GLU HB3    H N N 210 
GLU HG2    H N N 211 
GLU HG3    H N N 212 
GLU HE2    H N N 213 
GLU HXT    H N N 214 
GLY N      N N N 215 
GLY CA     C N N 216 
GLY C      C N N 217 
GLY O      O N N 218 
GLY OXT    O N N 219 
GLY H      H N N 220 
GLY H2     H N N 221 
GLY HA2    H N N 222 
GLY HA3    H N N 223 
GLY HXT    H N N 224 
HIS N      N N N 225 
HIS CA     C N S 226 
HIS C      C N N 227 
HIS O      O N N 228 
HIS CB     C N N 229 
HIS CG     C Y N 230 
HIS ND1    N Y N 231 
HIS CD2    C Y N 232 
HIS CE1    C Y N 233 
HIS NE2    N Y N 234 
HIS OXT    O N N 235 
HIS H      H N N 236 
HIS H2     H N N 237 
HIS HA     H N N 238 
HIS HB2    H N N 239 
HIS HB3    H N N 240 
HIS HD1    H N N 241 
HIS HD2    H N N 242 
HIS HE1    H N N 243 
HIS HE2    H N N 244 
HIS HXT    H N N 245 
HOH O      O N N 246 
HOH H1     H N N 247 
HOH H2     H N N 248 
ILE N      N N N 249 
ILE CA     C N S 250 
ILE C      C N N 251 
ILE O      O N N 252 
ILE CB     C N S 253 
ILE CG1    C N N 254 
ILE CG2    C N N 255 
ILE CD1    C N N 256 
ILE OXT    O N N 257 
ILE H      H N N 258 
ILE H2     H N N 259 
ILE HA     H N N 260 
ILE HB     H N N 261 
ILE HG12   H N N 262 
ILE HG13   H N N 263 
ILE HG21   H N N 264 
ILE HG22   H N N 265 
ILE HG23   H N N 266 
ILE HD11   H N N 267 
ILE HD12   H N N 268 
ILE HD13   H N N 269 
ILE HXT    H N N 270 
LEU N      N N N 271 
LEU CA     C N S 272 
LEU C      C N N 273 
LEU O      O N N 274 
LEU CB     C N N 275 
LEU CG     C N N 276 
LEU CD1    C N N 277 
LEU CD2    C N N 278 
LEU OXT    O N N 279 
LEU H      H N N 280 
LEU H2     H N N 281 
LEU HA     H N N 282 
LEU HB2    H N N 283 
LEU HB3    H N N 284 
LEU HG     H N N 285 
LEU HD11   H N N 286 
LEU HD12   H N N 287 
LEU HD13   H N N 288 
LEU HD21   H N N 289 
LEU HD22   H N N 290 
LEU HD23   H N N 291 
LEU HXT    H N N 292 
LYS N      N N N 293 
LYS CA     C N S 294 
LYS C      C N N 295 
LYS O      O N N 296 
LYS CB     C N N 297 
LYS CG     C N N 298 
LYS CD     C N N 299 
LYS CE     C N N 300 
LYS NZ     N N N 301 
LYS OXT    O N N 302 
LYS H      H N N 303 
LYS H2     H N N 304 
LYS HA     H N N 305 
LYS HB2    H N N 306 
LYS HB3    H N N 307 
LYS HG2    H N N 308 
LYS HG3    H N N 309 
LYS HD2    H N N 310 
LYS HD3    H N N 311 
LYS HE2    H N N 312 
LYS HE3    H N N 313 
LYS HZ1    H N N 314 
LYS HZ2    H N N 315 
LYS HZ3    H N N 316 
LYS HXT    H N N 317 
MET N      N N N 318 
MET CA     C N S 319 
MET C      C N N 320 
MET O      O N N 321 
MET CB     C N N 322 
MET CG     C N N 323 
MET SD     S N N 324 
MET CE     C N N 325 
MET OXT    O N N 326 
MET H      H N N 327 
MET H2     H N N 328 
MET HA     H N N 329 
MET HB2    H N N 330 
MET HB3    H N N 331 
MET HG2    H N N 332 
MET HG3    H N N 333 
MET HE1    H N N 334 
MET HE2    H N N 335 
MET HE3    H N N 336 
MET HXT    H N N 337 
PHE N      N N N 338 
PHE CA     C N S 339 
PHE C      C N N 340 
PHE O      O N N 341 
PHE CB     C N N 342 
PHE CG     C Y N 343 
PHE CD1    C Y N 344 
PHE CD2    C Y N 345 
PHE CE1    C Y N 346 
PHE CE2    C Y N 347 
PHE CZ     C Y N 348 
PHE OXT    O N N 349 
PHE H      H N N 350 
PHE H2     H N N 351 
PHE HA     H N N 352 
PHE HB2    H N N 353 
PHE HB3    H N N 354 
PHE HD1    H N N 355 
PHE HD2    H N N 356 
PHE HE1    H N N 357 
PHE HE2    H N N 358 
PHE HZ     H N N 359 
PHE HXT    H N N 360 
PRO N      N N N 361 
PRO CA     C N S 362 
PRO C      C N N 363 
PRO O      O N N 364 
PRO CB     C N N 365 
PRO CG     C N N 366 
PRO CD     C N N 367 
PRO OXT    O N N 368 
PRO H      H N N 369 
PRO HA     H N N 370 
PRO HB2    H N N 371 
PRO HB3    H N N 372 
PRO HG2    H N N 373 
PRO HG3    H N N 374 
PRO HD2    H N N 375 
PRO HD3    H N N 376 
PRO HXT    H N N 377 
SER N      N N N 378 
SER CA     C N S 379 
SER C      C N N 380 
SER O      O N N 381 
SER CB     C N N 382 
SER OG     O N N 383 
SER OXT    O N N 384 
SER H      H N N 385 
SER H2     H N N 386 
SER HA     H N N 387 
SER HB2    H N N 388 
SER HB3    H N N 389 
SER HG     H N N 390 
SER HXT    H N N 391 
THR N      N N N 392 
THR CA     C N S 393 
THR C      C N N 394 
THR O      O N N 395 
THR CB     C N R 396 
THR OG1    O N N 397 
THR CG2    C N N 398 
THR OXT    O N N 399 
THR H      H N N 400 
THR H2     H N N 401 
THR HA     H N N 402 
THR HB     H N N 403 
THR HG1    H N N 404 
THR HG21   H N N 405 
THR HG22   H N N 406 
THR HG23   H N N 407 
THR HXT    H N N 408 
TRP N      N N N 409 
TRP CA     C N S 410 
TRP C      C N N 411 
TRP O      O N N 412 
TRP CB     C N N 413 
TRP CG     C Y N 414 
TRP CD1    C Y N 415 
TRP CD2    C Y N 416 
TRP NE1    N Y N 417 
TRP CE2    C Y N 418 
TRP CE3    C Y N 419 
TRP CZ2    C Y N 420 
TRP CZ3    C Y N 421 
TRP CH2    C Y N 422 
TRP OXT    O N N 423 
TRP H      H N N 424 
TRP H2     H N N 425 
TRP HA     H N N 426 
TRP HB2    H N N 427 
TRP HB3    H N N 428 
TRP HD1    H N N 429 
TRP HE1    H N N 430 
TRP HE3    H N N 431 
TRP HZ2    H N N 432 
TRP HZ3    H N N 433 
TRP HH2    H N N 434 
TRP HXT    H N N 435 
TYR N      N N N 436 
TYR CA     C N S 437 
TYR C      C N N 438 
TYR O      O N N 439 
TYR CB     C N N 440 
TYR CG     C Y N 441 
TYR CD1    C Y N 442 
TYR CD2    C Y N 443 
TYR CE1    C Y N 444 
TYR CE2    C Y N 445 
TYR CZ     C Y N 446 
TYR OH     O N N 447 
TYR OXT    O N N 448 
TYR H      H N N 449 
TYR H2     H N N 450 
TYR HA     H N N 451 
TYR HB2    H N N 452 
TYR HB3    H N N 453 
TYR HD1    H N N 454 
TYR HD2    H N N 455 
TYR HE1    H N N 456 
TYR HE2    H N N 457 
TYR HH     H N N 458 
TYR HXT    H N N 459 
VAL N      N N N 460 
VAL CA     C N S 461 
VAL C      C N N 462 
VAL O      O N N 463 
VAL CB     C N N 464 
VAL CG1    C N N 465 
VAL CG2    C N N 466 
VAL OXT    O N N 467 
VAL H      H N N 468 
VAL H2     H N N 469 
VAL HA     H N N 470 
VAL HB     H N N 471 
VAL HG11   H N N 472 
VAL HG12   H N N 473 
VAL HG13   H N N 474 
VAL HG21   H N N 475 
VAL HG22   H N N 476 
VAL HG23   H N N 477 
VAL HXT    H N N 478 
# 
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  
FDA PA    O1A    doub N N 83  
FDA PA    O2A    sing N N 84  
FDA PA    O5B    sing N N 85  
FDA PA    O3P    sing N N 86  
FDA O2A   HOA2   sing N N 87  
FDA O5B   C5B    sing N N 88  
FDA C5B   C4B    sing N N 89  
FDA C5B   H51A   sing N N 90  
FDA C5B   H52A   sing N N 91  
FDA C4B   O4B    sing N N 92  
FDA C4B   C3B    sing N N 93  
FDA C4B   H4B    sing N N 94  
FDA O4B   C1B    sing N N 95  
FDA C3B   O3B    sing N N 96  
FDA C3B   C2B    sing N N 97  
FDA C3B   H3B    sing N N 98  
FDA O3B   HO3A   sing N N 99  
FDA C2B   O2B    sing N N 100 
FDA C2B   C1B    sing N N 101 
FDA C2B   H2B    sing N N 102 
FDA O2B   HO2A   sing N N 103 
FDA C1B   N9A    sing N N 104 
FDA C1B   H1B    sing N N 105 
FDA N9A   C8A    sing Y N 106 
FDA N9A   C4A    sing Y N 107 
FDA C8A   N7A    doub Y N 108 
FDA C8A   H8A    sing N N 109 
FDA N7A   C5A    sing Y N 110 
FDA C5A   C6A    sing Y N 111 
FDA C5A   C4A    doub Y N 112 
FDA C6A   N6A    sing N N 113 
FDA C6A   N1A    doub Y N 114 
FDA N6A   H61A   sing N N 115 
FDA N6A   H62A   sing N N 116 
FDA N1A   C2A    sing Y N 117 
FDA C2A   N3A    doub Y N 118 
FDA C2A   H2A    sing N N 119 
FDA N3A   C4A    sing Y N 120 
FDA N1    C2     sing N N 121 
FDA N1    C10    sing N N 122 
FDA N1    HN1    sing N N 123 
FDA C2    O2     doub N N 124 
FDA C2    N3     sing N N 125 
FDA N3    C4     sing N N 126 
FDA N3    HN3    sing N N 127 
FDA C4    O4     doub N N 128 
FDA C4    C4X    sing N N 129 
FDA C4X   N5     sing N N 130 
FDA C4X   C10    doub N N 131 
FDA N5    C5X    sing N N 132 
FDA N5    HN5    sing N N 133 
FDA C5X   C6     doub Y N 134 
FDA C5X   C9A    sing Y N 135 
FDA C6    C7     sing Y N 136 
FDA C6    H6     sing N N 137 
FDA C7    C7M    sing N N 138 
FDA C7    C8     doub Y N 139 
FDA C7M   HM71   sing N N 140 
FDA C7M   HM72   sing N N 141 
FDA C7M   HM73   sing N N 142 
FDA C8    C8M    sing N N 143 
FDA C8    C9     sing Y N 144 
FDA C8M   HM81   sing N N 145 
FDA C8M   HM82   sing N N 146 
FDA C8M   HM83   sing N N 147 
FDA C9    C9A    doub Y N 148 
FDA C9    H9     sing N N 149 
FDA C9A   N10    sing N N 150 
FDA N10   C10    sing N N 151 
FDA N10   "C1'"  sing N N 152 
FDA "C1'" "C2'"  sing N N 153 
FDA "C1'" "H1'1" sing N N 154 
FDA "C1'" "H1'2" sing N N 155 
FDA "C2'" "O2'"  sing N N 156 
FDA "C2'" "C3'"  sing N N 157 
FDA "C2'" "H2'"  sing N N 158 
FDA "O2'" "HO2'" sing N N 159 
FDA "C3'" "O3'"  sing N N 160 
FDA "C3'" "C4'"  sing N N 161 
FDA "C3'" "H3'"  sing N N 162 
FDA "O3'" "HO3'" sing N N 163 
FDA "C4'" "O4'"  sing N N 164 
FDA "C4'" "C5'"  sing N N 165 
FDA "C4'" "H4'"  sing N N 166 
FDA "O4'" "HO4'" sing N N 167 
FDA "C5'" "O5'"  sing N N 168 
FDA "C5'" "H5'1" sing N N 169 
FDA "C5'" "H5'2" sing N N 170 
FDA "O5'" P      sing N N 171 
FDA P     O1P    doub N N 172 
FDA P     O2P    sing N N 173 
FDA P     O3P    sing N N 174 
FDA O2P   HOP2   sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
HOH O     H1     sing N N 243 
HOH O     H2     sing N N 244 
ILE N     CA     sing N N 245 
ILE N     H      sing N N 246 
ILE N     H2     sing N N 247 
ILE CA    C      sing N N 248 
ILE CA    CB     sing N N 249 
ILE CA    HA     sing N N 250 
ILE C     O      doub N N 251 
ILE C     OXT    sing N N 252 
ILE CB    CG1    sing N N 253 
ILE CB    CG2    sing N N 254 
ILE CB    HB     sing N N 255 
ILE CG1   CD1    sing N N 256 
ILE CG1   HG12   sing N N 257 
ILE CG1   HG13   sing N N 258 
ILE CG2   HG21   sing N N 259 
ILE CG2   HG22   sing N N 260 
ILE CG2   HG23   sing N N 261 
ILE CD1   HD11   sing N N 262 
ILE CD1   HD12   sing N N 263 
ILE CD1   HD13   sing N N 264 
ILE OXT   HXT    sing N N 265 
LEU N     CA     sing N N 266 
LEU N     H      sing N N 267 
LEU N     H2     sing N N 268 
LEU CA    C      sing N N 269 
LEU CA    CB     sing N N 270 
LEU CA    HA     sing N N 271 
LEU C     O      doub N N 272 
LEU C     OXT    sing N N 273 
LEU CB    CG     sing N N 274 
LEU CB    HB2    sing N N 275 
LEU CB    HB3    sing N N 276 
LEU CG    CD1    sing N N 277 
LEU CG    CD2    sing N N 278 
LEU CG    HG     sing N N 279 
LEU CD1   HD11   sing N N 280 
LEU CD1   HD12   sing N N 281 
LEU CD1   HD13   sing N N 282 
LEU CD2   HD21   sing N N 283 
LEU CD2   HD22   sing N N 284 
LEU CD2   HD23   sing N N 285 
LEU OXT   HXT    sing N N 286 
LYS N     CA     sing N N 287 
LYS N     H      sing N N 288 
LYS N     H2     sing N N 289 
LYS CA    C      sing N N 290 
LYS CA    CB     sing N N 291 
LYS CA    HA     sing N N 292 
LYS C     O      doub N N 293 
LYS C     OXT    sing N N 294 
LYS CB    CG     sing N N 295 
LYS CB    HB2    sing N N 296 
LYS CB    HB3    sing N N 297 
LYS CG    CD     sing N N 298 
LYS CG    HG2    sing N N 299 
LYS CG    HG3    sing N N 300 
LYS CD    CE     sing N N 301 
LYS CD    HD2    sing N N 302 
LYS CD    HD3    sing N N 303 
LYS CE    NZ     sing N N 304 
LYS CE    HE2    sing N N 305 
LYS CE    HE3    sing N N 306 
LYS NZ    HZ1    sing N N 307 
LYS NZ    HZ2    sing N N 308 
LYS NZ    HZ3    sing N N 309 
LYS OXT   HXT    sing N N 310 
MET N     CA     sing N N 311 
MET N     H      sing N N 312 
MET N     H2     sing N N 313 
MET CA    C      sing N N 314 
MET CA    CB     sing N N 315 
MET CA    HA     sing N N 316 
MET C     O      doub N N 317 
MET C     OXT    sing N N 318 
MET CB    CG     sing N N 319 
MET CB    HB2    sing N N 320 
MET CB    HB3    sing N N 321 
MET CG    SD     sing N N 322 
MET CG    HG2    sing N N 323 
MET CG    HG3    sing N N 324 
MET SD    CE     sing N N 325 
MET CE    HE1    sing N N 326 
MET CE    HE2    sing N N 327 
MET CE    HE3    sing N N 328 
MET OXT   HXT    sing N N 329 
PHE N     CA     sing N N 330 
PHE N     H      sing N N 331 
PHE N     H2     sing N N 332 
PHE CA    C      sing N N 333 
PHE CA    CB     sing N N 334 
PHE CA    HA     sing N N 335 
PHE C     O      doub N N 336 
PHE C     OXT    sing N N 337 
PHE CB    CG     sing N N 338 
PHE CB    HB2    sing N N 339 
PHE CB    HB3    sing N N 340 
PHE CG    CD1    doub Y N 341 
PHE CG    CD2    sing Y N 342 
PHE CD1   CE1    sing Y N 343 
PHE CD1   HD1    sing N N 344 
PHE CD2   CE2    doub Y N 345 
PHE CD2   HD2    sing N N 346 
PHE CE1   CZ     doub Y N 347 
PHE CE1   HE1    sing N N 348 
PHE CE2   CZ     sing Y N 349 
PHE CE2   HE2    sing N N 350 
PHE CZ    HZ     sing N N 351 
PHE OXT   HXT    sing N N 352 
PRO N     CA     sing N N 353 
PRO N     CD     sing N N 354 
PRO N     H      sing N N 355 
PRO CA    C      sing N N 356 
PRO CA    CB     sing N N 357 
PRO CA    HA     sing N N 358 
PRO C     O      doub N N 359 
PRO C     OXT    sing N N 360 
PRO CB    CG     sing N N 361 
PRO CB    HB2    sing N N 362 
PRO CB    HB3    sing N N 363 
PRO CG    CD     sing N N 364 
PRO CG    HG2    sing N N 365 
PRO CG    HG3    sing N N 366 
PRO CD    HD2    sing N N 367 
PRO CD    HD3    sing N N 368 
PRO OXT   HXT    sing N N 369 
SER N     CA     sing N N 370 
SER N     H      sing N N 371 
SER N     H2     sing N N 372 
SER CA    C      sing N N 373 
SER CA    CB     sing N N 374 
SER CA    HA     sing N N 375 
SER C     O      doub N N 376 
SER C     OXT    sing N N 377 
SER CB    OG     sing N N 378 
SER CB    HB2    sing N N 379 
SER CB    HB3    sing N N 380 
SER OG    HG     sing N N 381 
SER OXT   HXT    sing N N 382 
THR N     CA     sing N N 383 
THR N     H      sing N N 384 
THR N     H2     sing N N 385 
THR CA    C      sing N N 386 
THR CA    CB     sing N N 387 
THR CA    HA     sing N N 388 
THR C     O      doub N N 389 
THR C     OXT    sing N N 390 
THR CB    OG1    sing N N 391 
THR CB    CG2    sing N N 392 
THR CB    HB     sing N N 393 
THR OG1   HG1    sing N N 394 
THR CG2   HG21   sing N N 395 
THR CG2   HG22   sing N N 396 
THR CG2   HG23   sing N N 397 
THR OXT   HXT    sing N N 398 
TRP N     CA     sing N N 399 
TRP N     H      sing N N 400 
TRP N     H2     sing N N 401 
TRP CA    C      sing N N 402 
TRP CA    CB     sing N N 403 
TRP CA    HA     sing N N 404 
TRP C     O      doub N N 405 
TRP C     OXT    sing N N 406 
TRP CB    CG     sing N N 407 
TRP CB    HB2    sing N N 408 
TRP CB    HB3    sing N N 409 
TRP CG    CD1    doub Y N 410 
TRP CG    CD2    sing Y N 411 
TRP CD1   NE1    sing Y N 412 
TRP CD1   HD1    sing N N 413 
TRP CD2   CE2    doub Y N 414 
TRP CD2   CE3    sing Y N 415 
TRP NE1   CE2    sing Y N 416 
TRP NE1   HE1    sing N N 417 
TRP CE2   CZ2    sing Y N 418 
TRP CE3   CZ3    doub Y N 419 
TRP CE3   HE3    sing N N 420 
TRP CZ2   CH2    doub Y N 421 
TRP CZ2   HZ2    sing N N 422 
TRP CZ3   CH2    sing Y N 423 
TRP CZ3   HZ3    sing N N 424 
TRP CH2   HH2    sing N N 425 
TRP OXT   HXT    sing N N 426 
TYR N     CA     sing N N 427 
TYR N     H      sing N N 428 
TYR N     H2     sing N N 429 
TYR CA    C      sing N N 430 
TYR CA    CB     sing N N 431 
TYR CA    HA     sing N N 432 
TYR C     O      doub N N 433 
TYR C     OXT    sing N N 434 
TYR CB    CG     sing N N 435 
TYR CB    HB2    sing N N 436 
TYR CB    HB3    sing N N 437 
TYR CG    CD1    doub Y N 438 
TYR CG    CD2    sing Y N 439 
TYR CD1   CE1    sing Y N 440 
TYR CD1   HD1    sing N N 441 
TYR CD2   CE2    doub Y N 442 
TYR CD2   HD2    sing N N 443 
TYR CE1   CZ     doub Y N 444 
TYR CE1   HE1    sing N N 445 
TYR CE2   CZ     sing Y N 446 
TYR CE2   HE2    sing N N 447 
TYR CZ    OH     sing N N 448 
TYR OH    HH     sing N N 449 
TYR OXT   HXT    sing N N 450 
VAL N     CA     sing N N 451 
VAL N     H      sing N N 452 
VAL N     H2     sing N N 453 
VAL CA    C      sing N N 454 
VAL CA    CB     sing N N 455 
VAL CA    HA     sing N N 456 
VAL C     O      doub N N 457 
VAL C     OXT    sing N N 458 
VAL CB    CG1    sing N N 459 
VAL CB    CG2    sing N N 460 
VAL CB    HB     sing N N 461 
VAL CG1   HG11   sing N N 462 
VAL CG1   HG12   sing N N 463 
VAL CG1   HG13   sing N N 464 
VAL CG2   HG21   sing N N 465 
VAL CG2   HG22   sing N N 466 
VAL CG2   HG23   sing N N 467 
VAL OXT   HXT    sing N N 468 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Science and Technology (MoST, Taiwan)'                      Taiwan AS-KPQ-105-TPP         1 
'Ministry of Science and Technology (MoST, Taiwan)'                      Taiwan AS-KPQ-109-TPP2        2 
'Ministry of Education, Culture, Sports, Science and Technology (Japan)' Japan  JP20H05442             3 
'Ministry of Education, Culture, Sports, Science and Technology (Japan)' Japan  JP22H04751             4 
'Japan Science and Technology'                                           Japan  JPMJFR2057             5 
'Japan Society for the Promotion of Science (JSPS)'                      Japan  JP19H05776             6 
'National Science Council (NSC, Taiwan)'                                 Taiwan 111-2113-M-002-029-MY3 7 
'Japan Society for the Promotion of Science (JSPS)'                      Japan  JP21J13329             8 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6FN3 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.pulse_energy                 ? 
_pdbx_serial_crystallography_measurement.pulse_duration               10 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   30 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          10 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.source_size                  ? 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.focal_spot_size              1.77 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.collection_time_total        ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_pdbx_serial_crystallography_sample_delivery_injection.diffrn_id               1 
_pdbx_serial_crystallography_sample_delivery_injection.description             'High viscosity injector' 
_pdbx_serial_crystallography_sample_delivery_injection.injector_diameter       75 
_pdbx_serial_crystallography_sample_delivery_injection.injector_temperature    293 
_pdbx_serial_crystallography_sample_delivery_injection.injector_pressure       ? 
_pdbx_serial_crystallography_sample_delivery_injection.flow_rate               1 
_pdbx_serial_crystallography_sample_delivery_injection.carrier_solvent         grease 
_pdbx_serial_crystallography_sample_delivery_injection.crystal_concentration   ? 
_pdbx_serial_crystallography_sample_delivery_injection.preparation             ? 
_pdbx_serial_crystallography_sample_delivery_injection.power_by                ? 
_pdbx_serial_crystallography_sample_delivery_injection.injector_nozzle         ? 
_pdbx_serial_crystallography_sample_delivery_injection.jet_diameter            ? 
_pdbx_serial_crystallography_sample_delivery_injection.filter_size             50 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZLR 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.019767 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015156 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006724 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H   ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P   ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N      . GLY A 1 3   ? 26.07800  -31.54600 9.79600  1.000 103.50731 ?  3   GLY A N      1 
ATOM   2    C CA     . GLY A 1 3   ? 27.30300  -31.47000 8.95000  1.000 102.58092 ?  3   GLY A CA     1 
ATOM   3    C C      . GLY A 1 3   ? 27.48600  -30.12000 8.28100  1.000 92.89128  ?  3   GLY A C      1 
ATOM   4    O O      . GLY A 1 3   ? 28.58100  -29.78800 7.82500  1.000 93.27920  ?  3   GLY A O      1 
ATOM   5    H H      . GLY A 1 3   ? 26.03500  -32.34400 10.18700 1.000 124.32654 ?  3   GLY A H      1 
ATOM   6    H HA2    . GLY A 1 3   ? 28.08200  -31.64200 9.50200  1.000 123.21488 ?  3   GLY A HA2    1 
ATOM   7    H HA3    . GLY A 1 3   ? 27.25300  -32.14700 8.25700  1.000 123.21488 ?  3   GLY A HA3    1 
ATOM   8    N N      . VAL A 1 4   ? 26.40800  -29.34200 8.22300  1.000 78.64551  ?  4   VAL A N      1 
ATOM   9    C CA     . VAL A 1 4   ? 26.42400  -28.01800 7.61800  1.000 82.78736  ?  4   VAL A CA     1 
ATOM   10   C C      . VAL A 1 4   ? 25.95400  -27.00700 8.65300  1.000 67.00577  ?  4   VAL A C      1 
ATOM   11   O O      . VAL A 1 4   ? 25.32500  -27.35500 9.65700  1.000 69.29248  ?  4   VAL A O      1 
ATOM   12   C CB     . VAL A 1 4   ? 25.54500  -27.93500 6.35100  1.000 79.44386  ?  4   VAL A CB     1 
ATOM   13   C CG1    . VAL A 1 4   ? 26.21400  -28.66000 5.19500  1.000 90.44467  ?  4   VAL A CG1    1 
ATOM   14   C CG2    . VAL A 1 4   ? 24.15200  -28.50400 6.62900  1.000 89.25455  ?  4   VAL A CG2    1 
ATOM   15   H H      . VAL A 1 4   ? 25.63900  -29.56600 8.53600  1.000 94.49238  ?  4   VAL A H      1 
ATOM   16   H HA     . VAL A 1 4   ? 27.33600  -27.80100 7.36700  1.000 99.46260  ?  4   VAL A HA     1 
ATOM   17   H HB     . VAL A 1 4   ? 25.43800  -27.00500 6.09700  1.000 95.45040  ?  4   VAL A HB     1 
ATOM   18   H HG11   . VAL A 1 4   ? 25.64600  -28.59700 4.41200  1.000 108.65137 ?  4   VAL A HG11   1 
ATOM   19   H HG12   . VAL A 1 4   ? 27.07200  -28.24300 5.01500  1.000 108.65137 ?  4   VAL A HG12   1 
ATOM   20   H HG13   . VAL A 1 4   ? 26.34300  -29.59000 5.43700  1.000 108.65137 ?  4   VAL A HG13   1 
ATOM   21   H HG21   . VAL A 1 4   ? 23.61500  -28.43000 5.82500  1.000 107.22323 ?  4   VAL A HG21   1 
ATOM   22   H HG22   . VAL A 1 4   ? 24.23700  -29.43600 6.88500  1.000 107.22323 ?  4   VAL A HG22   1 
ATOM   23   H HG23   . VAL A 1 4   ? 23.74300  -28.00000 7.34900  1.000 107.22323 ?  4   VAL A HG23   1 
ATOM   24   N N      . LYS A 1 5   ? 26.25800  -25.73900 8.39000  1.000 59.18432  ?  5   LYS A N      1 
ATOM   25   C CA     . LYS A 1 5   ? 25.81200  -24.64000 9.23800  1.000 51.46989  ?  5   LYS A CA     1 
ATOM   26   C C      . LYS A 1 5   ? 24.59900  -23.97300 8.59600  1.000 52.74410  ?  5   LYS A C      1 
ATOM   27   O O      . LYS A 1 5   ? 24.69500  -23.41400 7.49700  1.000 48.45274  ?  5   LYS A O      1 
ATOM   28   C CB     . LYS A 1 5   ? 26.92500  -23.61600 9.46300  1.000 52.32688  ?  5   LYS A CB     1 
ATOM   29   C CG     . LYS A 1 5   ? 26.56400  -22.56000 10.50600 1.000 49.91766  ?  5   LYS A CG     1 
ATOM   30   C CD     . LYS A 1 5   ? 27.43900  -21.32400 10.42100 1.000 50.19933  ?  5   LYS A CD     1 
ATOM   31   C CE     . LYS A 1 5   ? 26.79300  -20.14800 11.14900 1.000 50.39557  ?  5   LYS A CE     1 
ATOM   32   N NZ     . LYS A 1 5   ? 27.79300  -19.12200 11.58000 1.000 43.18090  ?  5   LYS A NZ     1 
ATOM   33   H H      . LYS A 1 5   ? 26.73000  -25.48700 7.71600  1.000 71.13895  ?  5   LYS A H      1 
ATOM   34   H HA     . LYS A 1 5   ? 25.55300  -24.99800 10.10100 1.000 61.88164  ?  5   LYS A HA     1 
ATOM   35   H HB2    . LYS A 1 5   ? 27.72100  -24.07800 9.76900  1.000 62.91002  ?  5   LYS A HB2    1 
ATOM   36   H HB3    . LYS A 1 5   ? 27.10700  -23.16000 8.62600  1.000 62.91002  ?  5   LYS A HB3    1 
ATOM   37   H HG2    . LYS A 1 5   ? 25.64400  -22.28500 10.37200 1.000 60.01896  ?  5   LYS A HG2    1 
ATOM   38   H HG3    . LYS A 1 5   ? 26.67100  -22.94100 11.39100 1.000 60.01896  ?  5   LYS A HG3    1 
ATOM   39   H HD2    . LYS A 1 5   ? 28.29800  -21.50700 10.83300 1.000 60.35697  ?  5   LYS A HD2    1 
ATOM   40   H HD3    . LYS A 1 5   ? 27.56300  -21.07900 9.49000  1.000 60.35697  ?  5   LYS A HD3    1 
ATOM   41   H HE2    . LYS A 1 5   ? 26.15800  -19.71700 10.55600 1.000 60.59245  ?  5   LYS A HE2    1 
ATOM   42   H HE3    . LYS A 1 5   ? 26.33900  -20.47600 11.94100 1.000 60.59245  ?  5   LYS A HE3    1 
ATOM   43   H HZ1    . LYS A 1 5   ? 27.38700  -18.47300 12.03400 1.000 51.93485  ?  5   LYS A HZ1    1 
ATOM   44   H HZ2    . LYS A 1 5   ? 28.40900  -19.49800 12.10200 1.000 51.93485  ?  5   LYS A HZ2    1 
ATOM   45   H HZ3    . LYS A 1 5   ? 28.19400  -18.77000 10.86800 1.000 51.93485  ?  5   LYS A HZ3    1 
ATOM   46   N N      . ASN A 1 6   ? 23.46600  -24.04000 9.28200  1.000 45.97213  ?  6   ASN A N      1 
ATOM   47   C CA     . ASN A 1 6   ? 22.26700  -23.29200 8.93000  1.000 47.16635  ?  6   ASN A CA     1 
ATOM   48   C C      . ASN A 1 6   ? 21.95200  -22.37700 10.10600 1.000 44.99601  ?  6   ASN A C      1 
ATOM   49   O O      . ASN A 1 6   ? 21.79200  -22.85400 11.23400 1.000 50.27188  ?  6   ASN A O      1 
ATOM   50   C CB     . ASN A 1 6   ? 21.09100  -24.22300 8.61900  1.000 46.47505  ?  6   ASN A CB     1 
ATOM   51   C CG     . ASN A 1 6   ? 21.40800  -25.20800 7.50100  1.000 48.90958  ?  6   ASN A CG     1 
ATOM   52   O OD1    . ASN A 1 6   ? 21.87100  -24.82300 6.42500  1.000 50.07000  ?  6   ASN A OD1    1 
ATOM   53   N ND2    . ASN A 1 6   ? 21.15600  -26.49500 7.75200  1.000 51.17084  ?  6   ASN A ND2    1 
ATOM   54   H H      . ASN A 1 6   ? 23.36400  -24.53000 9.98200  1.000 55.28432  ?  6   ASN A H      1 
ATOM   55   H HA     . ASN A 1 6   ? 22.42100  -22.75600 8.13600  1.000 56.71739  ?  6   ASN A HA     1 
ATOM   56   H HB2    . ASN A 1 6   ? 20.87000  -24.73200 9.41500  1.000 55.88783  ?  6   ASN A HB2    1 
ATOM   57   H HB3    . ASN A 1 6   ? 20.32900  -23.69000 8.34400  1.000 55.88783  ?  6   ASN A HB3    1 
ATOM   58   H HD21   . ASN A 1 6   ? 20.83200  -26.72900 8.51300  1.000 61.52278  ?  6   ASN A HD21   1 
ATOM   59   H HD22   . ASN A 1 6   ? 21.31800  -27.08900 7.15200  1.000 61.52278  ?  6   ASN A HD22   1 
ATOM   60   N N      . SER A 1 7   ? 21.87500  -21.07900 9.84700  1.000 41.98469  ?  7   SER A N      1 
ATOM   61   C CA     . SER A 1 7   ? 21.78100  -20.08900 10.90600 1.000 46.26453  ?  7   SER A CA     1 
ATOM   62   C C      . SER A 1 7   ? 20.58600  -19.16700 10.68800 1.000 39.31645  ?  7   SER A C      1 
ATOM   63   O O      . SER A 1 7   ? 20.13600  -18.94500 9.56700  1.000 39.70153  ?  7   SER A O      1 
ATOM   64   C CB     . SER A 1 7   ? 23.06900  -19.25300 10.99300 1.000 42.45408  ?  7   SER A CB     1 
ATOM   65   O OG     . SER A 1 7   ? 23.21500  -18.44400 9.84200  1.000 46.92081  ?  7   SER A OG     1 
ATOM   66   H H      . SER A 1 7   ? 21.87500  -20.74400 9.05500  1.000 50.49940  ?  7   SER A H      1 
ATOM   67   H HA     . SER A 1 7   ? 21.64000  -20.54600 11.75100 1.000 55.63520  ?  7   SER A HA     1 
ATOM   68   H HB2    . SER A 1 7   ? 23.02500  -18.68300 11.77700 1.000 51.06266  ?  7   SER A HB2    1 
ATOM   69   H HB3    . SER A 1 7   ? 23.83100  -19.85000 11.05900 1.000 51.06266  ?  7   SER A HB3    1 
ATOM   70   H HG     . SER A 1 7   ? 23.92200  -17.99400 9.89400  1.000 56.42274  ?  7   SER A HG     1 
ATOM   71   N N      . ILE A 1 8   ? 20.07000  -18.64600 11.79100 1.000 41.13166  ?  8   ILE A N      1 
ATOM   72   C CA     . ILE A 1 8   ? 19.01200  -17.62600 11.76900 1.000 39.03467  ?  8   ILE A CA     1 
ATOM   73   C C      . ILE A 1 8   ? 19.58900  -16.34100 12.34200 1.000 37.81939  ?  8   ILE A C      1 
ATOM   74   O O      . ILE A 1 8   ? 20.25400  -16.36300 13.39100 1.000 41.07358  ?  8   ILE A O      1 
ATOM   75   C CB     . ILE A 1 8   ? 17.77800  -18.07000 12.56700 1.000 46.53904  ?  8   ILE A CB     1 
ATOM   76   C CG1    . ILE A 1 8   ? 17.07900  -19.24900 11.88200 1.000 41.73490  ?  8   ILE A CG1    1 
ATOM   77   C CG2    . ILE A 1 8   ? 16.79700  -16.89800 12.72400 1.000 40.82518  ?  8   ILE A CG2    1 
ATOM   78   C CD1    . ILE A 1 8   ? 16.08300  -19.96300 12.77000 1.000 44.98993  ?  8   ILE A CD1    1 
ATOM   79   H H      . ILE A 1 8   ? 20.31700  -18.86700 12.58500 1.000 49.47576  ?  8   ILE A H      1 
ATOM   80   H HA     . ILE A 1 8   ? 18.73900  -17.46700 10.85200 1.000 46.95937  ?  8   ILE A HA     1 
ATOM   81   H HB     . ILE A 1 8   ? 18.07500  -18.35700 13.44400 1.000 55.96462  ?  8   ILE A HB     1 
ATOM   82   H HG12   . ILE A 1 8   ? 16.60100  -18.92000 11.10500 1.000 50.19965  ?  8   ILE A HG12   1 
ATOM   83   H HG13   . ILE A 1 8   ? 17.75000  -19.89400 11.61000 1.000 50.19965  ?  8   ILE A HG13   1 
ATOM   84   H HG21   . ILE A 1 8   ? 15.95300  -17.23600 13.06300 1.000 49.10799  ?  8   ILE A HG21   1 
ATOM   85   H HG22   . ILE A 1 8   ? 17.17100  -16.25500 13.34700 1.000 49.10799  ?  8   ILE A HG22   1 
ATOM   86   H HG23   . ILE A 1 8   ? 16.66300  -16.48100 11.85900 1.000 49.10799  ?  8   ILE A HG23   1 
ATOM   87   H HD11   . ILE A 1 8   ? 15.70700  -20.71300 12.28400 1.000 54.10568  ?  8   ILE A HD11   1 
ATOM   88   H HD12   . ILE A 1 8   ? 16.54000  -20.27900 13.56500 1.000 54.10568  ?  8   ILE A HD12   1 
ATOM   89   H HD13   . ILE A 1 8   ? 15.38000  -19.34300 13.01800 1.000 54.10568  ?  8   ILE A HD13   1 
ATOM   90   N N      . ILE A 1 9   ? 19.37400  -15.23600 11.64500 1.000 34.58024  ?  9   ILE A N      1 
ATOM   91   C CA     . ILE A 1 9   ? 19.56300  -13.89500 12.20000 1.000 40.63425  ?  9   ILE A CA     1 
ATOM   92   C C      . ILE A 1 9   ? 18.17000  -13.34100 12.45400 1.000 40.59966  ?  9   ILE A C      1 
ATOM   93   O O      . ILE A 1 9   ? 17.36500  -13.20500 11.51600 1.000 37.45372  ?  9   ILE A O      1 
ATOM   94   C CB     . ILE A 1 9   ? 20.38900  -12.99200 11.28800 1.000 35.89822  ?  9   ILE A CB     1 
ATOM   95   C CG1    . ILE A 1 9   ? 20.39700  -11.55400 11.81700 1.000 43.90421  ?  9   ILE A CG1    1 
ATOM   96   C CG2    . ILE A 1 9   ? 19.86200  -12.98300 9.86400  1.000 43.52134  ?  9   ILE A CG2    1 
ATOM   97   C CD1    . ILE A 1 9   ? 20.81900  -11.41300 13.26300 1.000 43.99114  ?  9   ILE A CD1    1 
ATOM   98   H H      . ILE A 1 9   ? 19.11200  -15.23300 10.82500 1.000 41.61406  ?  9   ILE A H      1 
ATOM   99   H HA     . ILE A 1 9   ? 20.04200  -13.94400 13.04200 1.000 48.87886  ?  9   ILE A HA     1 
ATOM   100  H HB     . ILE A 1 9   ? 21.28900  -13.35300 11.28500 1.000 43.19563  ?  9   ILE A HB     1 
ATOM   101  H HG12   . ILE A 1 9   ? 21.01300  -11.03200 11.28000 1.000 52.80282  ?  9   ILE A HG12   1 
ATOM   102  H HG13   . ILE A 1 9   ? 19.50000  -11.19200 11.73800 1.000 52.80282  ?  9   ILE A HG13   1 
ATOM   103  H HG21   . ILE A 1 9   ? 20.50700  -12.54100 9.29100  1.000 52.34338  ?  9   ILE A HG21   1 
ATOM   104  H HG22   . ILE A 1 9   ? 19.73100  -13.89800 9.57000  1.000 52.34338  ?  9   ILE A HG22   1 
ATOM   105  H HG23   . ILE A 1 9   ? 19.01800  -12.50500 9.84300  1.000 52.34338  ?  9   ILE A HG23   1 
ATOM   106  H HD11   . ILE A 1 9   ? 20.94300  -10.47200 13.46600 1.000 52.90714  ?  9   ILE A HD11   1 
ATOM   107  H HD12   . ILE A 1 9   ? 20.12800  -11.78500 13.83200 1.000 52.90714  ?  9   ILE A HD12   1 
ATOM   108  H HD13   . ILE A 1 9   ? 21.65200  -11.89300 13.39700 1.000 52.90714  ?  9   ILE A HD13   1 
ATOM   109  N N      . TRP A 1 10  ? 17.87600  -13.05000 13.71900 1.000 40.79899  ?  10  TRP A N      1 
ATOM   110  C CA     . TRP A 1 10  ? 16.55700  -12.64500 14.17500 1.000 39.21326  ?  10  TRP A CA     1 
ATOM   111  C C      . TRP A 1 10  ? 16.58200  -11.15100 14.49400 1.000 41.67156  ?  10  TRP A C      1 
ATOM   112  O O      . TRP A 1 10  ? 17.28700  -10.71500 15.40400 1.000 39.43197  ?  10  TRP A O      1 
ATOM   113  C CB     . TRP A 1 10  ? 16.15100  -13.46700 15.38700 1.000 40.92595  ?  10  TRP A CB     1 
ATOM   114  C CG     . TRP A 1 10  ? 14.84000  -13.10700 16.03200 1.000 39.75092  ?  10  TRP A CG     1 
ATOM   115  C CD1    . TRP A 1 10  ? 13.78600  -12.47800 15.45700 1.000 41.21100  ?  10  TRP A CD1    1 
ATOM   116  C CD2    . TRP A 1 10  ? 14.45800  -13.38600 17.38200 1.000 36.83184  ?  10  TRP A CD2    1 
ATOM   117  N NE1    . TRP A 1 10  ? 12.75600  -12.33900 16.36800 1.000 40.47237  ?  10  TRP A NE1    1 
ATOM   118  C CE2    . TRP A 1 10  ? 13.14700  -12.89100 17.55600 1.000 38.79858  ?  10  TRP A CE2    1 
ATOM   119  C CE3    . TRP A 1 10  ? 15.09300  -14.00600 18.46400 1.000 40.71483  ?  10  TRP A CE3    1 
ATOM   120  C CZ2    . TRP A 1 10  ? 12.46600  -12.99300 18.76700 1.000 44.98856  ?  10  TRP A CZ2    1 
ATOM   121  C CZ3    . TRP A 1 10  ? 14.41200  -14.10900 19.66600 1.000 42.38779  ?  10  TRP A CZ3    1 
ATOM   122  C CH2    . TRP A 1 10  ? 13.11100  -13.60800 19.80500 1.000 44.96129  ?  10  TRP A CH2    1 
ATOM   123  H H      . TRP A 1 10  ? 18.45300  -13.08300 14.35700 1.000 49.07655  ?  10  TRP A H      1 
ATOM   124  H HA     . TRP A 1 10  ? 15.90000  -12.78400 13.47500 1.000 47.17368  ?  10  TRP A HA     1 
ATOM   125  H HB2    . TRP A 1 10  ? 16.08900  -14.39600 15.11500 1.000 49.22891  ?  10  TRP A HB2    1 
ATOM   126  H HB3    . TRP A 1 10  ? 16.83900  -13.36500 16.06400 1.000 49.22891  ?  10  TRP A HB3    1 
ATOM   127  H HD1    . TRP A 1 10  ? 13.75900  -12.18300 14.57500 1.000 49.57097  ?  10  TRP A HD1    1 
ATOM   128  H HE1    . TRP A 1 10  ? 11.99600  -11.96800 16.21300 1.000 48.68461  ?  10  TRP A HE1    1 
ATOM   129  H HE3    . TRP A 1 10  ? 15.95600  -14.34200 18.37800 1.000 48.97556  ?  10  TRP A HE3    1 
ATOM   130  H HZ2    . TRP A 1 10  ? 11.60500  -12.65500 18.86600 1.000 54.10404  ?  10  TRP A HZ2    1 
ATOM   131  H HZ3    . TRP A 1 10  ? 14.82400  -14.51900 20.39200 1.000 50.98312  ?  10  TRP A HZ3    1 
ATOM   132  H HH2    . TRP A 1 10  ? 12.67500  -13.69500 20.62200 1.000 54.07132  ?  10  TRP A HH2    1 
ATOM   133  N N      . PHE A 1 11  ? 15.79600  -10.37900 13.74500 1.000 44.42008  ?  11  PHE A N      1 
ATOM   134  C CA     . PHE A 1 11  ? 15.70200  -8.93600  13.93100 1.000 36.34124  ?  11  PHE A CA     1 
ATOM   135  C C      . PHE A 1 11  ? 14.56400  -8.62800  14.90300 1.000 41.30413  ?  11  PHE A C      1 
ATOM   136  O O      . PHE A 1 11  ? 13.43600  -9.09300  14.70100 1.000 44.31535  ?  11  PHE A O      1 
ATOM   137  C CB     . PHE A 1 11  ? 15.44000  -8.25200  12.60100 1.000 34.80143  ?  11  PHE A CB     1 
ATOM   138  C CG     . PHE A 1 11  ? 16.59100  -8.29100  11.64700 1.000 36.54550  ?  11  PHE A CG     1 
ATOM   139  C CD1    . PHE A 1 11  ? 17.58000  -7.32800  11.70500 1.000 37.47792  ?  11  PHE A CD1    1 
ATOM   140  C CD2    . PHE A 1 11  ? 16.68000  -9.28800  10.69800 1.000 39.56326  ?  11  PHE A CD2    1 
ATOM   141  C CE1    . PHE A 1 11  ? 18.64400  -7.35700  10.83300 1.000 42.31516  ?  11  PHE A CE1    1 
ATOM   142  C CE2    . PHE A 1 11  ? 17.73300  -9.32600  9.82000  1.000 43.08612  ?  11  PHE A CE2    1 
ATOM   143  C CZ     . PHE A 1 11  ? 18.72300  -8.35800  9.88600  1.000 44.47581  ?  11  PHE A CZ     1 
ATOM   144  H H      . PHE A 1 11  ? 15.29800  -10.67600 13.11000 1.000 53.42186  ?  11  PHE A H      1 
ATOM   145  H HA     . PHE A 1 11  ? 16.53400  -8.60200  14.30300 1.000 43.72725  ?  11  PHE A HA     1 
ATOM   146  H HB2    . PHE A 1 11  ? 14.68800  -8.68900  12.17100 1.000 41.87949  ?  11  PHE A HB2    1 
ATOM   147  H HB3    . PHE A 1 11  ? 15.23000  -7.32000  12.76800 1.000 41.87949  ?  11  PHE A HB3    1 
ATOM   148  H HD1    . PHE A 1 11  ? 17.52600  -6.65200  12.34200 1.000 45.09128  ?  11  PHE A HD1    1 
ATOM   149  H HD2    . PHE A 1 11  ? 16.02000  -9.94100  10.65400 1.000 47.59368  ?  11  PHE A HD2    1 
ATOM   150  H HE1    . PHE A 1 11  ? 19.30600  -6.70500  10.88100 1.000 50.89596  ?  11  PHE A HE1    1 
ATOM   151  H HE2    . PHE A 1 11  ? 17.78200  -10.00100 9.18100  1.000 51.82111  ?  11  PHE A HE2    1 
ATOM   152  H HZ     . PHE A 1 11  ? 19.43900  -8.38300  9.29300  1.000 53.48874  ?  11  PHE A HZ     1 
ATOM   153  N N      . ARG A 1 12  ? 14.86700  -7.89100  15.97400 1.000 40.24633  ?  12  ARG A N      1 
ATOM   154  C CA     . ARG A 1 12  ? 13.82800  -7.27500  16.79700 1.000 38.30312  ?  12  ARG A CA     1 
ATOM   155  C C      . ARG A 1 12  ? 14.01000  -5.76000  16.82300 1.000 43.26488  ?  12  ARG A C      1 
ATOM   156  O O      . ARG A 1 12  ? 13.17400  -5.02900  16.27400 1.000 35.54115  ?  12  ARG A O      1 
ATOM   157  C CB     . ARG A 1 12  ? 13.86600  -7.87700  18.19900 1.000 44.47870  ?  12  ARG A CB     1 
ATOM   158  C CG     . ARG A 1 12  ? 13.88100  -9.42400  18.21800 1.000 45.81918  ?  12  ARG A CG     1 
ATOM   159  C CD     . ARG A 1 12  ? 15.31100  -9.99500  18.18800 1.000 41.29795  ?  12  ARG A CD     1 
ATOM   160  N NE     . ARG A 1 12  ? 16.11600  -9.54700  19.32400 1.000 37.42304  ?  12  ARG A NE     1 
ATOM   161  C CZ     . ARG A 1 12  ? 16.09000  -10.10500 20.51900 1.000 44.29233  ?  12  ARG A CZ     1 
ATOM   162  N NH1    . ARG A 1 12  ? 15.32400  -11.15800 20.77500 1.000 47.76326  ?  12  ARG A NH1    1 
ATOM   163  N NH2    . ARG A 1 12  ? 16.84700  -9.59700  21.49400 1.000 47.82554  ?  12  ARG A NH2    1 
ATOM   164  H H      . ARG A 1 12  ? 15.66800  -7.73300  16.24400 1.000 48.41336  ?  12  ARG A H      1 
ATOM   165  H HA     . ARG A 1 12  ? 12.95600  -7.45800  16.41400 1.000 46.08151  ?  12  ARG A HA     1 
ATOM   166  H HB2    . ARG A 1 12  ? 14.66800  -7.56800  18.64900 1.000 53.49221  ?  12  ARG A HB2    1 
ATOM   167  H HB3    . ARG A 1 12  ? 13.07900  -7.58300  18.68500 1.000 53.49221  ?  12  ARG A HB3    1 
ATOM   168  H HG2    . ARG A 1 12  ? 13.44800  -9.73700  19.02900 1.000 55.10079  ?  12  ARG A HG2    1 
ATOM   169  H HG3    . ARG A 1 12  ? 13.40700  -9.75700  17.44000 1.000 55.10079  ?  12  ARG A HG3    1 
ATOM   170  H HD2    . ARG A 1 12  ? 15.26700  -10.96300 18.21300 1.000 49.67531  ?  12  ARG A HD2    1 
ATOM   171  H HD3    . ARG A 1 12  ? 15.75200  -9.70400  17.37400 1.000 49.67531  ?  12  ARG A HD3    1 
ATOM   172  H HE     . ARG A 1 12  ? 16.64200  -8.87700  19.20500 1.000 45.02542  ?  12  ARG A HE     1 
ATOM   173  H HH11   . ARG A 1 12  ? 14.83100  -11.49200 20.15400 1.000 57.43368  ?  12  ARG A HH11   1 
ATOM   174  H HH12   . ARG A 1 12  ? 15.32100  -11.50700 21.56100 1.000 57.43368  ?  12  ARG A HH12   1 
ATOM   175  H HH21   . ARG A 1 12  ? 17.34500  -8.91400  21.34000 1.000 57.50842  ?  12  ARG A HH21   1 
ATOM   176  H HH22   . ARG A 1 12  ? 16.83600  -9.95400  22.27600 1.000 57.50842  ?  12  ARG A HH22   1 
ATOM   177  N N      . LYS A 1 13  ? 15.09500  -5.26900  17.40000 1.000 39.28993  ?  13  LYS A N      1 
ATOM   178  C CA     . LYS A 1 13  ? 15.70200  -3.97900  17.11900 1.000 42.52323  ?  13  LYS A CA     1 
ATOM   179  C C      . LYS A 1 13  ? 16.83200  -4.22300  16.11000 1.000 41.11182  ?  13  LYS A C      1 
ATOM   180  O O      . LYS A 1 13  ? 16.85800  -5.24700  15.42300 1.000 37.25576  ?  13  LYS A O      1 
ATOM   181  C CB     . LYS A 1 13  ? 16.16300  -3.32000  18.41500 1.000 39.42109  ?  13  LYS A CB     1 
ATOM   182  C CG     . LYS A 1 13  ? 15.00300  -2.84900  19.30300 1.000 43.15674  ?  13  LYS A CG     1 
ATOM   183  C CD     . LYS A 1 13  ? 15.49900  -2.23100  20.58400 1.000 47.07006  ?  13  LYS A CD     1 
ATOM   184  C CE     . LYS A 1 13  ? 14.40300  -2.16700  21.63800 1.000 50.93425  ?  13  LYS A CE     1 
ATOM   185  N NZ     . LYS A 1 13  ? 14.83500  -1.39800  22.83100 1.000 51.12707  ?  13  LYS A NZ     1 
ATOM   186  H H      . LYS A 1 13  ? 15.53200  -5.69700  18.00500 1.000 47.26568  ?  13  LYS A H      1 
ATOM   187  H HA     . LYS A 1 13  ? 15.04400  -3.38000  16.73400 1.000 51.14565  ?  13  LYS A HA     1 
ATOM   188  H HB2    . LYS A 1 13  ? 16.68700  -3.95900  18.92300 1.000 47.42308  ?  13  LYS A HB2    1 
ATOM   189  H HB3    . LYS A 1 13  ? 16.70400  -2.54500  18.19700 1.000 47.42308  ?  13  LYS A HB3    1 
ATOM   190  H HG2    . LYS A 1 13  ? 14.48400  -2.18400  18.82500 1.000 51.90585  ?  13  LYS A HG2    1 
ATOM   191  H HG3    . LYS A 1 13  ? 14.44400  -3.60900  19.52800 1.000 51.90585  ?  13  LYS A HG3    1 
ATOM   192  H HD2    . LYS A 1 13  ? 16.22900  -2.76500  20.93600 1.000 56.60184  ?  13  LYS A HD2    1 
ATOM   193  H HD3    . LYS A 1 13  ? 15.80500  -1.32800  20.40700 1.000 56.60184  ?  13  LYS A HD3    1 
ATOM   194  H HE2    . LYS A 1 13  ? 13.62200  -1.73200  21.26200 1.000 61.23887  ?  13  LYS A HE2    1 
ATOM   195  H HE3    . LYS A 1 13  ? 14.17700  -3.06700  21.92100 1.000 61.23887  ?  13  LYS A HE3    1 
ATOM   196  H HZ1    . LYS A 1 13  ? 14.17800  -1.37300  23.43100 1.000 61.47025  ?  13  LYS A HZ1    1 
ATOM   197  H HZ2    . LYS A 1 13  ? 15.54800  -1.78300  23.19900 1.000 61.47025  ?  13  LYS A HZ2    1 
ATOM   198  H HZ3    . LYS A 1 13  ? 15.04400  -0.56500  22.59700 1.000 61.47025  ?  13  LYS A HZ3    1 
ATOM   199  N N      . GLY A 1 14  ? 17.74600  -3.26600  15.99000 1.000 45.59167  ?  14  GLY A N      1 
ATOM   200  C CA     . GLY A 1 14  ? 18.89000  -3.45800  15.10700 1.000 37.36923  ?  14  GLY A CA     1 
ATOM   201  C C      . GLY A 1 14  ? 18.46200  -3.74100  13.69200 1.000 38.75803  ?  14  GLY A C      1 
ATOM   202  O O      . GLY A 1 14  ? 18.97400  -4.66900  13.04700 1.000 36.73449  ?  14  GLY A O      1 
ATOM   203  H H      . GLY A 1 14  ? 17.72700  -2.51100  16.40100 1.000 54.82778  ?  14  GLY A H      1 
ATOM   204  H HA2    . GLY A 1 14  ? 19.43800  -2.65800  15.11000 1.000 44.96084  ?  14  GLY A HA2    1 
ATOM   205  H HA3    . GLY A 1 14  ? 19.42100  -4.20600  15.42400 1.000 44.96084  ?  14  GLY A HA3    1 
ATOM   206  N N      . LEU A 1 15  ? 17.50300  -2.95500  13.19600 1.000 44.16149  ?  15  LEU A N      1 
ATOM   207  C CA     . LEU A 1 15  ? 16.95800  -3.11700  11.85500 1.000 36.60721  ?  15  LEU A CA     1 
ATOM   208  C C      . LEU A 1 15  ? 17.89000  -2.45100  10.83400 1.000 41.38288  ?  15  LEU A C      1 
ATOM   209  O O      . LEU A 1 15  ? 17.58400  -1.41800  10.21800 1.000 40.36733  ?  15  LEU A O      1 
ATOM   210  C CB     . LEU A 1 15  ? 15.56000  -2.53300  11.78200 1.000 38.67662  ?  15  LEU A CB     1 
ATOM   211  C CG     . LEU A 1 15  ? 14.53500  -3.06500  12.79600 1.000 38.63433  ?  15  LEU A CG     1 
ATOM   212  C CD1    . LEU A 1 15  ? 13.14000  -2.60300  12.38800 1.000 45.89437  ?  15  LEU A CD1    1 
ATOM   213  C CD2    . LEU A 1 15  ? 14.57700  -4.57700  12.90500 1.000 41.81344  ?  15  LEU A CD2    1 
ATOM   214  H H      . LEU A 1 15  ? 17.14400  -2.30600  13.63200 1.000 53.11155  ?  15  LEU A H      1 
ATOM   215  H HA     . LEU A 1 15  ? 16.91300  -4.06400  11.65100 1.000 44.04642  ?  15  LEU A HA     1 
ATOM   216  H HB2    . LEU A 1 15  ? 15.62800  -1.57500  11.92300 1.000 46.52971  ?  15  LEU A HB2    1 
ATOM   217  H HB3    . LEU A 1 15  ? 15.20600  -2.71300  10.89800 1.000 46.52971  ?  15  LEU A HB3    1 
ATOM   218  H HG     . LEU A 1 15  ? 14.75200  -2.71400  13.67400 1.000 46.47896  ?  15  LEU A HG     1 
ATOM   219  H HD11   . LEU A 1 15  ? 12.49600  -2.93700  13.03300 1.000 55.19102  ?  15  LEU A HD11   1 
ATOM   220  H HD12   . LEU A 1 15  ? 13.12000  -1.63400  12.37200 1.000 55.19102  ?  15  LEU A HD12   1 
ATOM   221  H HD13   . LEU A 1 15  ? 12.93700  -2.95300  11.50700 1.000 55.19102  ?  15  LEU A HD13   1 
ATOM   222  H HD21   . LEU A 1 15  ? 13.90800  -4.86600  13.54600 1.000 50.29389  ?  15  LEU A HD21   1 
ATOM   223  H HD22   . LEU A 1 15  ? 14.38900  -4.96200  12.03500 1.000 50.29389  ?  15  LEU A HD22   1 
ATOM   224  H HD23   . LEU A 1 15  ? 15.45900  -4.84700  13.20300 1.000 50.29389  ?  15  LEU A HD23   1 
ATOM   225  N N      . ARG A 1 16  ? 19.05100  -3.07200  10.65600 1.000 40.86087  ?  16  ARG A N      1 
ATOM   226  C CA     . ARG A 1 16  ? 20.08500  -2.50100  9.79800  1.000 39.88953  ?  16  ARG A CA     1 
ATOM   227  C C      . ARG A 1 16  ? 21.03400  -3.61600  9.36500  1.000 37.82926  ?  16  ARG A C      1 
ATOM   228  O O      . ARG A 1 16  ? 21.13000  -4.65800  10.01500 1.000 37.13928  ?  16  ARG A O      1 
ATOM   229  C CB     . ARG A 1 16  ? 20.85100  -1.39600  10.51100 1.000 35.44969  ?  16  ARG A CB     1 
ATOM   230  C CG     . ARG A 1 16  ? 21.54200  -1.84800  11.80100 1.000 39.10308  ?  16  ARG A CG     1 
ATOM   231  C CD     . ARG A 1 16  ? 22.40600  -0.75800  12.38600 1.000 42.37897  ?  16  ARG A CD     1 
ATOM   232  N NE     . ARG A 1 16  ? 23.15000  -1.20800  13.55800 1.000 46.67888  ?  16  ARG A NE     1 
ATOM   233  C CZ     . ARG A 1 16  ? 22.67000  -1.21300  14.79700 1.000 42.89925  ?  16  ARG A CZ     1 
ATOM   234  N NH1    . ARG A 1 16  ? 21.43000  -0.82400  15.06900 1.000 40.34005  ?  16  ARG A NH1    1 
ATOM   235  N NH2    . ARG A 1 16  ? 23.45500  -1.60900  15.79100 1.000 47.32095  ?  16  ARG A NH2    1 
ATOM   236  H H      . ARG A 1 16  ? 19.26500  -3.82200  11.01900 1.000 49.15081  ?  16  ARG A H      1 
ATOM   237  H HA     . ARG A 1 16  ? 19.67300  -2.12600  9.00400  1.000 47.98521  ?  16  ARG A HA     1 
ATOM   238  H HB2    . ARG A 1 16  ? 21.53600  -1.05700  9.91300  1.000 42.65740  ?  16  ARG A HB2    1 
ATOM   239  H HB3    . ARG A 1 16  ? 20.23100  -0.68700  10.74200 1.000 42.65740  ?  16  ARG A HB3    1 
ATOM   240  H HG2    . ARG A 1 16  ? 20.86900  -2.08800  12.45700 1.000 47.04147  ?  16  ARG A HG2    1 
ATOM   241  H HG3    . ARG A 1 16  ? 22.10600  -2.61400  11.61000 1.000 47.04147  ?  16  ARG A HG3    1 
ATOM   242  H HD2    . ARG A 1 16  ? 23.04500  -0.46600  11.71700 1.000 50.97253  ?  16  ARG A HD2    1 
ATOM   243  H HD3    . ARG A 1 16  ? 21.84200  -0.01500  12.65400 1.000 50.97253  ?  16  ARG A HD3    1 
ATOM   244  H HE     . ARG A 1 16  ? 23.95400  -1.48900  13.43900 1.000 56.13242  ?  16  ARG A HE     1 
ATOM   245  H HH11   . ARG A 1 16  ? 20.91300  -0.56000  14.43400 1.000 48.52583  ?  16  ARG A HH11   1 
ATOM   246  H HH12   . ARG A 1 16  ? 21.14300  -0.83700  15.88000 1.000 48.52583  ?  16  ARG A HH12   1 
ATOM   247  H HH21   . ARG A 1 16  ? 24.26200  -1.85800  15.62900 1.000 56.90290  ?  16  ARG A HH21   1 
ATOM   248  H HH22   . ARG A 1 16  ? 23.15600  -1.61700  16.59800 1.000 56.90290  ?  16  ARG A HH22   1 
ATOM   249  N N      . LEU A 1 17  ? 21.76500  -3.34600  8.28100  1.000 37.10054  ?  17  LEU A N      1 
ATOM   250  C CA     . LEU A 1 17  ? 22.87600  -4.16500  7.85700  1.000 45.09035  ?  17  LEU A CA     1 
ATOM   251  C C      . LEU A 1 17  ? 24.19700  -3.66800  8.42700  1.000 48.27583  ?  17  LEU A C      1 
ATOM   252  O O      . LEU A 1 17  ? 25.07100  -4.47800  8.77000  1.000 46.54991  ?  17  LEU A O      1 
ATOM   253  C CB     . LEU A 1 17  ? 22.95300  -4.20800  6.32500  1.000 45.44987  ?  17  LEU A CB     1 
ATOM   254  C CG     . LEU A 1 17  ? 22.20900  -5.39400  5.67500  1.000 49.83253  ?  17  LEU A CG     1 
ATOM   255  C CD1    . LEU A 1 17  ? 20.77900  -5.45200  6.14300  1.000 48.13573  ?  17  LEU A CD1    1 
ATOM   256  C CD2    . LEU A 1 17  ? 22.28000  -5.28400  4.16000  1.000 55.69745  ?  17  LEU A CD2    1 
ATOM   257  H H      . LEU A 1 17  ? 21.62500  -2.67200  7.76600  1.000 44.63842  ?  17  LEU A H      1 
ATOM   258  H HA     . LEU A 1 17  ? 22.73200  -5.07300  8.16800  1.000 54.22619  ?  17  LEU A HA     1 
ATOM   259  H HB2    . LEU A 1 17  ? 22.56500  -3.39100  5.97500  1.000 54.65762  ?  17  LEU A HB2    1 
ATOM   260  H HB3    . LEU A 1 17  ? 23.88600  -4.26900  6.06600  1.000 54.65762  ?  17  LEU A HB3    1 
ATOM   261  H HG     . LEU A 1 17  ? 22.63500  -6.22300  5.94100  1.000 59.91681  ?  17  LEU A HG     1 
ATOM   262  H HD11   . LEU A 1 17  ? 20.30500  -6.12300  5.62800  1.000 57.88065  ?  17  LEU A HD11   1 
ATOM   263  H HD12   . LEU A 1 17  ? 20.76500  -5.68600  7.08400  1.000 57.88065  ?  17  LEU A HD12   1 
ATOM   264  H HD13   . LEU A 1 17  ? 20.36800  -4.58300  6.01200  1.000 57.88065  ?  17  LEU A HD13   1 
ATOM   265  H HD21   . LEU A 1 17  ? 21.67000  -5.92800  3.76800  1.000 66.95471  ?  17  LEU A HD21   1 
ATOM   266  H HD22   . LEU A 1 17  ? 22.02800  -4.38600  3.89600  1.000 66.95471  ?  17  LEU A HD22   1 
ATOM   267  H HD23   . LEU A 1 17  ? 23.18800  -5.47100  3.87200  1.000 66.95471  ?  17  LEU A HD23   1 
ATOM   268  N N      . HIS A 1 18  ? 24.36200  -2.35300  8.54500  1.000 44.55227  ?  18  HIS A N      1 
ATOM   269  C CA     . HIS A 1 18  ? 25.60100  -1.79700  9.05700  1.000 46.13069  ?  18  HIS A CA     1 
ATOM   270  C C      . HIS A 1 18  ? 25.69800  -2.01300  10.56500 1.000 44.29033  ?  18  HIS A C      1 
ATOM   271  O O      . HIS A 1 18  ? 24.69200  -2.12600  11.26400 1.000 43.00013  ?  18  HIS A O      1 
ATOM   272  C CB     . HIS A 1 18  ? 25.71600  -0.31500  8.68100  1.000 50.34864  ?  18  HIS A CB     1 
ATOM   273  C CG     . HIS A 1 18  ? 24.94100  0.62000   9.56400  1.000 50.11437  ?  18  HIS A CG     1 
ATOM   274  N ND1    . HIS A 1 18  ? 23.64100  1.00800   9.28800  1.000 42.84336  ?  18  HIS A ND1    1 
ATOM   275  C CD2    . HIS A 1 18  ? 25.30600  1.29800   10.68300 1.000 51.24586  ?  18  HIS A CD2    1 
ATOM   276  C CE1    . HIS A 1 18  ? 23.23000  1.85900   10.21600 1.000 44.43956  ?  18  HIS A CE1    1 
ATOM   277  N NE2    . HIS A 1 18  ? 24.22300  2.05400   11.07100 1.000 48.80410  ?  18  HIS A NE2    1 
ATOM   278  H H      . HIS A 1 18  ? 23.77100  -1.76500  8.33400  1.000 53.58050  ?  18  HIS A H      1 
ATOM   279  H HA     . HIS A 1 18  ? 26.36400  -2.24400  8.65700  1.000 55.47459  ?  18  HIS A HA     1 
ATOM   280  H HB2    . HIS A 1 18  ? 26.64900  -0.05700  8.73000  1.000 60.53614  ?  18  HIS A HB2    1 
ATOM   281  H HB3    . HIS A 1 18  ? 25.38700  -0.20100  7.77600  1.000 60.53614  ?  18  HIS A HB3    1 
ATOM   282  H HD1    . HIS A 1 18  ? 23.17300  0.73800   8.61800  1.000 51.52980  ?  18  HIS A HD1    1 
ATOM   283  H HD2    . HIS A 1 18  ? 26.13300  1.26000   11.10700 1.000 61.61281  ?  18  HIS A HD2    1 
ATOM   284  H HE1    . HIS A 1 18  ? 22.38800  2.25200   10.25900 1.000 53.44524  ?  18  HIS A HE1    1 
ATOM   285  N N      . ASP A 1 19  ? 26.93500  -2.13600  11.04400 1.000 41.97460  ?  19  ASP A N      1 
ATOM   286  C CA     . ASP A 1 19  ? 27.23500  -2.39100  12.45600 1.000 44.25724  ?  19  ASP A CA     1 
ATOM   287  C C      . ASP A 1 19  ? 26.25300  -3.40200  13.07100 1.000 45.08619  ?  19  ASP A C      1 
ATOM   288  O O      . ASP A 1 19  ? 25.54500  -3.12900  14.04100 1.000 40.47312  ?  19  ASP A O      1 
ATOM   289  C CB     . ASP A 1 19  ? 27.22600  -1.08900  13.25100 1.000 46.61786  ?  19  ASP A CB     1 
ATOM   290  C CG     . ASP A 1 19  ? 27.66300  -1.28400  14.68100 1.000 51.02458  ?  19  ASP A CG     1 
ATOM   291  O OD1    . ASP A 1 19  ? 28.40100  -2.26800  14.95700 1.000 53.57057  ?  19  ASP A OD1    1 
ATOM   292  O OD2    . ASP A 1 19  ? 27.29200  -0.45100  15.53300 1.000 54.22417  -1 19  ASP A OD2    1 
ATOM   293  H H      . ASP A 1 19  ? 27.64100  -2.07300  10.55600 1.000 50.48729  ?  19  ASP A H      1 
ATOM   294  H HA     . ASP A 1 19  ? 28.12100  -2.78300  12.50200 1.000 53.22645  ?  19  ASP A HA     1 
ATOM   295  H HB2    . ASP A 1 19  ? 27.83400  -0.45800  12.83300 1.000 56.05920  ?  19  ASP A HB2    1 
ATOM   296  H HB3    . ASP A 1 19  ? 26.32600  -0.72800  13.25700 1.000 56.05920  ?  19  ASP A HB3    1 
ATOM   297  N N      . ASN A 1 20  ? 26.24000  -4.59500  12.49300 1.000 38.67128  ?  20  ASN A N      1 
ATOM   298  C CA     . ASN A 1 20  ? 25.38600  -5.68700  12.94700 1.000 37.60021  ?  20  ASN A CA     1 
ATOM   299  C C      . ASN A 1 20  ? 26.23500  -6.92700  13.17900 1.000 36.70131  ?  20  ASN A C      1 
ATOM   300  O O      . ASN A 1 20  ? 26.31400  -7.80900  12.31700 1.000 36.72074  ?  20  ASN A O      1 
ATOM   301  C CB     . ASN A 1 20  ? 24.26400  -5.96500  11.93900 1.000 40.43815  ?  20  ASN A CB     1 
ATOM   302  C CG     . ASN A 1 20  ? 23.17500  -6.81900  12.51800 1.000 34.75939  ?  20  ASN A CG     1 
ATOM   303  O OD1    . ASN A 1 20  ? 23.39000  -7.51700  13.51400 1.000 43.08257  ?  20  ASN A OD1    1 
ATOM   304  N ND2    . ASN A 1 20  ? 21.98100  -6.76900  11.91900 1.000 40.46207  ?  20  ASN A ND2    1 
ATOM   305  H H      . ASN A 1 20  ? 26.72900  -4.80300  11.81700 1.000 46.52331  ?  20  ASN A H      1 
ATOM   306  H HA     . ASN A 1 20  ? 24.99000  -5.43900  13.79700 1.000 45.23802  ?  20  ASN A HA     1 
ATOM   307  H HB2    . ASN A 1 20  ? 23.87100  -5.12300  11.66100 1.000 48.64355  ?  20  ASN A HB2    1 
ATOM   308  H HB3    . ASN A 1 20  ? 24.63400  -6.42800  11.17100 1.000 48.64355  ?  20  ASN A HB3    1 
ATOM   309  H HD21   . ASN A 1 20  ? 21.86500  -6.26300  11.23300 1.000 48.67225  ?  20  ASN A HD21   1 
ATOM   310  H HD22   . ASN A 1 20  ? 21.32900  -7.24200  12.21900 1.000 48.67225  ?  20  ASN A HD22   1 
ATOM   311  N N      . PRO A 1 21  ? 26.90400  -7.01400  14.32900 1.000 41.01877  ?  21  PRO A N      1 
ATOM   312  C CA     . PRO A 1 21  ? 27.74700  -8.19800  14.59700 1.000 42.02118  ?  21  PRO A CA     1 
ATOM   313  C C      . PRO A 1 21  ? 26.96500  -9.50600  14.63000 1.000 44.63015  ?  21  PRO A C      1 
ATOM   314  O O      . PRO A 1 21  ? 27.51600  -10.54500 14.28500 1.000 39.56191  ?  21  PRO A O      1 
ATOM   315  C CB     . PRO A 1 21  ? 28.38100  -7.88800  15.95700 1.000 45.21496  ?  21  PRO A CB     1 
ATOM   316  C CG     . PRO A 1 21  ? 27.57200  -6.77700  16.54600 1.000 46.20588  ?  21  PRO A CG     1 
ATOM   317  C CD     . PRO A 1 21  ? 27.03300  -5.99300  15.38400 1.000 41.51390  ?  21  PRO A CD     1 
ATOM   318  H HA     . PRO A 1 21  ? 28.44500  -8.25700  13.92600 1.000 50.54319  ?  21  PRO A HA     1 
ATOM   319  H HB2    . PRO A 1 21  ? 28.34400  -8.67600  16.52100 1.000 54.37572  ?  21  PRO A HB2    1 
ATOM   320  H HB3    . PRO A 1 21  ? 29.30300  -7.61300  15.83200 1.000 54.37572  ?  21  PRO A HB3    1 
ATOM   321  H HG2    . PRO A 1 21  ? 26.84900  -7.14600  17.07600 1.000 55.56483  ?  21  PRO A HG2    1 
ATOM   322  H HG3    . PRO A 1 21  ? 28.14000  -6.21900  17.10100 1.000 55.56483  ?  21  PRO A HG3    1 
ATOM   323  H HD2    . PRO A 1 21  ? 26.17000  -5.60500  15.59800 1.000 49.93445  ?  21  PRO A HD2    1 
ATOM   324  H HD3    . PRO A 1 21  ? 27.65300  -5.29600  15.11700 1.000 49.93445  ?  21  PRO A HD3    1 
ATOM   325  N N      . ALA A 1 22  ? 25.69400  -9.48000  15.04100 1.000 41.06920  ?  22  ALA A N      1 
ATOM   326  C CA     . ALA A 1 22  ? 24.90200  -10.70300 15.02600 1.000 43.23987  ?  22  ALA A CA     1 
ATOM   327  C C      . ALA A 1 22  ? 24.74800  -11.23000 13.61000 1.000 42.57258  ?  22  ALA A C      1 
ATOM   328  O O      . ALA A 1 22  ? 24.81000  -12.44600 13.37600 1.000 41.86338  ?  22  ALA A O      1 
ATOM   329  C CB     . ALA A 1 22  ? 23.53200  -10.44400 15.65800 1.000 43.21118  ?  22  ALA A CB     1 
ATOM   330  H H      . ALA A 1 22  ? 25.28000  -8.78300  15.32700 1.000 49.40081  ?  22  ALA A H      1 
ATOM   331  H HA     . ALA A 1 22  ? 25.35100  -11.38100 15.55400 1.000 52.00562  ?  22  ALA A HA     1 
ATOM   332  H HB1    . ALA A 1 22  ? 23.01800  -11.26600 15.64600 1.000 51.97119  ?  22  ALA A HB1    1 
ATOM   333  H HB2    . ALA A 1 22  ? 23.65700  -10.14500 16.57200 1.000 51.97119  ?  22  ALA A HB2    1 
ATOM   334  H HB3    . ALA A 1 22  ? 23.07300  -9.75900  15.14600 1.000 51.97119  ?  22  ALA A HB3    1 
ATOM   335  N N      . LEU A 1 23  ? 24.54900  -10.32600 12.64500 1.000 39.67615  ?  23  LEU A N      1 
ATOM   336  C CA     . LEU A 1 23  ? 24.44000  -10.72600 11.24600 1.000 42.63880  ?  23  LEU A CA     1 
ATOM   337  C C      . LEU A 1 23  ? 25.76100  -11.26600 10.70900 1.000 45.18223  ?  23  LEU A C      1 
ATOM   338  O O      . LEU A 1 23  ? 25.77700  -12.25500 9.96000  1.000 39.68457  ?  23  LEU A O      1 
ATOM   339  C CB     . LEU A 1 23  ? 23.96400  -9.53200  10.41700 1.000 41.14203  ?  23  LEU A CB     1 
ATOM   340  C CG     . LEU A 1 23  ? 23.96200  -9.66500  8.89900  1.000 46.96920  ?  23  LEU A CG     1 
ATOM   341  C CD1    . LEU A 1 23  ? 23.07700  -10.82600 8.46200  1.000 50.97035  ?  23  LEU A CD1    1 
ATOM   342  C CD2    . LEU A 1 23  ? 23.49200  -8.35100  8.28500  1.000 45.00270  ?  23  LEU A CD2    1 
ATOM   343  H H      . LEU A 1 23  ? 24.47400  -9.47900  12.77700 1.000 47.72915  ?  23  LEU A H      1 
ATOM   344  H HA     . LEU A 1 23  ? 23.78600  -11.43800 11.16800 1.000 51.28434  ?  23  LEU A HA     1 
ATOM   345  H HB2    . LEU A 1 23  ? 23.05100  -9.33700  10.68000 1.000 49.48820  ?  23  LEU A HB2    1 
ATOM   346  H HB3    . LEU A 1 23  ? 24.53900  -8.78000  10.62800 1.000 49.48820  ?  23  LEU A HB3    1 
ATOM   347  H HG     . LEU A 1 23  ? 24.85700  -9.85600  8.57900  1.000 56.48081  ?  23  LEU A HG     1 
ATOM   348  H HD11   . LEU A 1 23  ? 23.09300  -10.88800 7.49500  1.000 61.28219  ?  23  LEU A HD11   1 
ATOM   349  H HD12   . LEU A 1 23  ? 23.41800  -11.64700 8.85200  1.000 61.28219  ?  23  LEU A HD12   1 
ATOM   350  H HD13   . LEU A 1 23  ? 22.17100  -10.66500 8.76900  1.000 61.28219  ?  23  LEU A HD13   1 
ATOM   351  H HD21   . LEU A 1 23  ? 23.34100  -8.48100  7.33600  1.000 54.12101  ?  23  LEU A HD21   1 
ATOM   352  H HD22   . LEU A 1 23  ? 22.66700  -8.07800  8.71700  1.000 54.12101  ?  23  LEU A HD22   1 
ATOM   353  H HD23   . LEU A 1 23  ? 24.17500  -7.67600  8.42200  1.000 54.12101  ?  23  LEU A HD23   1 
ATOM   354  N N      . LEU A 1 24  ? 26.88300  -10.63700 11.07500 1.000 39.50227  ?  24  LEU A N      1 
ATOM   355  C CA     . LEU A 1 24  ? 28.16700  -11.12400 10.61000 1.000 40.84438  ?  24  LEU A CA     1 
ATOM   356  C C      . LEU A 1 24  ? 28.43700  -12.54100 11.11600 1.000 45.56131  ?  24  LEU A C      1 
ATOM   357  O O      . LEU A 1 24  ? 28.95400  -13.39000 10.38400 1.000 42.79304  ?  24  LEU A O      1 
ATOM   358  C CB     . LEU A 1 24  ? 29.29200  -10.17400 11.05900 1.000 41.96721  ?  24  LEU A CB     1 
ATOM   359  C CG     . LEU A 1 24  ? 29.22000  -8.72700  10.56300 1.000 42.50340  ?  24  LEU A CG     1 
ATOM   360  C CD1    . LEU A 1 24  ? 30.33200  -7.88000  11.18900 1.000 45.31680  ?  24  LEU A CD1    1 
ATOM   361  C CD2    . LEU A 1 24  ? 29.29100  -8.65500  9.04500  1.000 49.36881  ?  24  LEU A CD2    1 
ATOM   362  H H      . LEU A 1 24  ? 26.91900  -9.94300  11.58100 1.000 47.52050  ?  24  LEU A H      1 
ATOM   363  H HA     . LEU A 1 24  ? 28.15900  -11.14200 9.64000  1.000 49.13102  ?  24  LEU A HA     1 
ATOM   364  H HB2    . LEU A 1 24  ? 29.28500  -10.14200 12.02800 1.000 50.47842  ?  24  LEU A HB2    1 
ATOM   365  H HB3    . LEU A 1 24  ? 30.13400  -10.54000 10.74500 1.000 50.47842  ?  24  LEU A HB3    1 
ATOM   366  H HG     . LEU A 1 24  ? 28.36500  -8.35800  10.83600 1.000 51.12185  ?  24  LEU A HG     1 
ATOM   367  H HD11   . LEU A 1 24  ? 30.25700  -6.96900  10.86200 1.000 54.49793  ?  24  LEU A HD11   1 
ATOM   368  H HD12   . LEU A 1 24  ? 30.23400  -7.89400  12.15400 1.000 54.49793  ?  24  LEU A HD12   1 
ATOM   369  H HD13   . LEU A 1 24  ? 31.19200  -8.25100  10.93700 1.000 54.49793  ?  24  LEU A HD13   1 
ATOM   370  H HD21   . LEU A 1 24  ? 29.29700  -7.72400  8.77200  1.000 59.36035  ?  24  LEU A HD21   1 
ATOM   371  H HD22   . LEU A 1 24  ? 30.10400  -9.09300  8.74500  1.000 59.36035  ?  24  LEU A HD22   1 
ATOM   372  H HD23   . LEU A 1 24  ? 28.51700  -9.10500  8.67100  1.000 59.36035  ?  24  LEU A HD23   1 
ATOM   373  N N      . GLU A 1 25  ? 28.09400  -12.81500 12.37800 1.000 47.70288  ?  25  GLU A N      1 
ATOM   374  C CA     . GLU A 1 25  ? 28.29400  -14.16000 12.91500 1.000 45.52010  ?  25  GLU A CA     1 
ATOM   375  C C      . GLU A 1 25  ? 27.45100  -15.18600 12.16100 1.000 45.27222  ?  25  GLU A C      1 
ATOM   376  O O      . GLU A 1 25  ? 27.94800  -16.26200 11.79400 1.000 45.19753  ?  25  GLU A O      1 
ATOM   377  C CB     . GLU A 1 25  ? 27.95700  -14.17000 14.40400 1.000 43.53037  ?  25  GLU A CB     1 
ATOM   378  C CG     . GLU A 1 25  ? 28.15400  -15.51100 15.08700 1.000 54.10211  ?  25  GLU A CG     1 
ATOM   379  C CD     . GLU A 1 25  ? 29.53900  -16.09200 14.84400 1.000 58.51091  ?  25  GLU A CD     1 
ATOM   380  O OE1    . GLU A 1 25  ? 30.54000  -15.34200 14.97000 1.000 59.67503  ?  25  GLU A OE1    1 
ATOM   381  O OE2    . GLU A 1 25  ? 29.63100  -17.29900 14.51800 1.000 57.20822  -1 25  GLU A OE2    1 
ATOM   382  H H      . GLU A 1 25  ? 27.75100  -12.25200 12.93000 1.000 57.36123  ?  25  GLU A H      1 
ATOM   383  H HA     . GLU A 1 25  ? 29.22600  -14.41000 12.81300 1.000 54.74189  ?  25  GLU A HA     1 
ATOM   384  H HB2    . GLU A 1 25  ? 28.52500  -13.52600 14.85400 1.000 52.35421  ?  25  GLU A HB2    1 
ATOM   385  H HB3    . GLU A 1 25  ? 27.02500  -13.92200 14.51100 1.000 52.35421  ?  25  GLU A HB3    1 
ATOM   386  H HG2    . GLU A 1 25  ? 28.03800  -15.39900 16.04300 1.000 65.04030  ?  25  GLU A HG2    1 
ATOM   387  H HG3    . GLU A 1 25  ? 27.50000  -16.14000 14.74500 1.000 65.04030  ?  25  GLU A HG3    1 
ATOM   388  N N      . ALA A 1 26  ? 26.19000  -14.86600 11.89300 1.000 42.57918  ?  26  ALA A N      1 
ATOM   389  C CA     . ALA A 1 26  ? 25.29800  -15.83900 11.26300 1.000 42.32882  ?  26  ALA A CA     1 
ATOM   390  C C      . ALA A 1 26  ? 25.73700  -16.18700 9.84700  1.000 47.92104  ?  26  ALA A C      1 
ATOM   391  O O      . ALA A 1 26  ? 25.51600  -17.32100 9.38900  1.000 43.83611  ?  26  ALA A O      1 
ATOM   392  C CB     . ALA A 1 26  ? 23.86600  -15.30400 11.25900 1.000 38.86710  ?  26  ALA A CB     1 
ATOM   393  H H      . ALA A 1 26  ? 25.82900  -14.10400 12.06200 1.000 51.21278  ?  26  ALA A H      1 
ATOM   394  H HA     . ALA A 1 26  ? 25.31500  -16.65700 11.78400 1.000 50.91236  ?  26  ALA A HA     1 
ATOM   395  H HB1    . ALA A 1 26  ? 23.28200  -15.96800 10.86100 1.000 46.75829  ?  26  ALA A HB1    1 
ATOM   396  H HB2    . ALA A 1 26  ? 23.59200  -15.12700 12.17200 1.000 46.75829  ?  26  ALA A HB2    1 
ATOM   397  H HB3    . ALA A 1 26  ? 23.83600  -14.48500 10.74000 1.000 46.75829  ?  26  ALA A HB3    1 
ATOM   398  N N      . CYS A 1 27  ? 26.34100  -15.23600 9.12700  1.000 43.03266  ?  27  CYS A N      1 
ATOM   399  C CA     . CYS A 1 27  ? 26.77500  -15.50600 7.76500  1.000 43.39465  ?  27  CYS A CA     1 
ATOM   400  C C      . CYS A 1 27  ? 28.05200  -16.32800 7.71100  1.000 48.15754  ?  27  CYS A C      1 
ATOM   401  O O      . CYS A 1 27  ? 28.26300  -17.07500 6.74500  1.000 44.74986  ?  27  CYS A O      1 
ATOM   402  C CB     . CYS A 1 27  ? 27.00700  -14.18200 7.01300  1.000 48.43360  ?  27  CYS A CB     1 
ATOM   403  S SG     . CYS A 1 27  ? 25.49900  -13.26900 6.71200  1.000 58.66738  ?  27  CYS A SG     1 
ATOM   404  H H      . CYS A 1 27  ? 26.50700  -14.44000 9.40500  1.000 51.75696  ?  27  CYS A H      1 
ATOM   405  H HA     . CYS A 1 27  ? 26.07100  -16.00400 7.32100  1.000 52.19134  ?  27  CYS A HA     1 
ATOM   406  H HB2    . CYS A 1 27  ? 27.59600  -13.62000 7.54100  1.000 58.23808  ?  27  CYS A HB2    1 
ATOM   407  H HB3    . CYS A 1 27  ? 27.41500  -14.37600 6.15500  1.000 58.23808  ?  27  CYS A HB3    1 
ATOM   408  H HG     . CYS A 1 27  ? 25.76600  -12.25600 6.12600  1.000 70.51863  ?  27  CYS A HG     1 
ATOM   409  N N      . LYS A 1 28  ? 28.91100  -16.19300 8.71600  1.000 42.95096  ?  28  LYS A N      1 
ATOM   410  C CA     . LYS A 1 28  ? 30.22700  -16.82800 8.68200  1.000 51.99076  ?  28  LYS A CA     1 
ATOM   411  C C      . LYS A 1 28  ? 30.10000  -18.33800 8.52800  1.000 48.74433  ?  28  LYS A C      1 
ATOM   412  O O      . LYS A 1 28  ? 29.46900  -19.00400 9.35400  1.000 49.84175  ?  28  LYS A O      1 
ATOM   413  C CB     . LYS A 1 28  ? 30.98700  -16.47000 9.95600  1.000 53.00801  ?  28  LYS A CB     1 
ATOM   414  C CG     . LYS A 1 28  ? 32.19200  -17.35200 10.25000 1.000 64.16118  ?  28  LYS A CG     1 
ATOM   415  C CD     . LYS A 1 28  ? 33.19400  -16.65400 11.17400 1.000 67.23578  ?  28  LYS A CD     1 
ATOM   416  C CE     . LYS A 1 28  ? 32.56600  -16.24800 12.51000 1.000 72.15376  ?  28  LYS A CE     1 
ATOM   417  N NZ     . LYS A 1 28  ? 32.71400  -17.30500 13.55300 0.000 64.21145  ?  28  LYS A NZ     1 
ATOM   418  H H      . LYS A 1 28  ? 28.75800  -15.73900 9.43000  1.000 51.65892  ?  28  LYS A H      1 
ATOM   419  H HA     . LYS A 1 28  ? 30.72700  -16.50200 7.91700  1.000 62.50669  ?  28  LYS A HA     1 
ATOM   420  H HB2    . LYS A 1 28  ? 31.30600  -15.55800 9.87900  1.000 63.72739  ?  28  LYS A HB2    1 
ATOM   421  H HB3    . LYS A 1 28  ? 30.38000  -16.54700 10.70900 1.000 63.72739  ?  28  LYS A HB3    1 
ATOM   422  H HG2    . LYS A 1 28  ? 31.89400  -18.16700 10.68400 1.000 77.11118  ?  28  LYS A HG2    1 
ATOM   423  H HG3    . LYS A 1 28  ? 32.64300  -17.56500 9.41800  1.000 77.11118  ?  28  LYS A HG3    1 
ATOM   424  H HD2    . LYS A 1 28  ? 33.93000  -17.25800 11.35800 1.000 80.80071  ?  28  LYS A HD2    1 
ATOM   425  H HD3    . LYS A 1 28  ? 33.52300  -15.85200 10.73900 1.000 80.80071  ?  28  LYS A HD3    1 
ATOM   426  H HE2    . LYS A 1 28  ? 32.99900  -15.44300 12.83300 1.000 86.70228  ?  28  LYS A HE2    1 
ATOM   427  H HE3    . LYS A 1 28  ? 31.61800  -16.08500 12.37900 1.000 86.70228  ?  28  LYS A HE3    1 
ATOM   428  H HZ1    . LYS A 1 28  ? 32.35100  -17.03100 14.31800 1.000 77.17152  ?  28  LYS A HZ1    1 
ATOM   429  H HZ2    . LYS A 1 28  ? 32.30600  -18.05100 13.29100 1.000 77.17152  ?  28  LYS A HZ2    1 
ATOM   430  H HZ3    . LYS A 1 28  ? 33.57600  -17.48000 13.68900 1.000 77.17152  ?  28  LYS A HZ3    1 
ATOM   431  N N      . ASP A 1 29  ? 30.67600  -18.86600 7.45600  1.000 50.05158  ?  29  ASP A N      1 
ATOM   432  C CA     . ASP A 1 29  ? 30.74700  -20.30000 7.19100  1.000 51.65086  ?  29  ASP A CA     1 
ATOM   433  C C      . ASP A 1 29  ? 29.36900  -20.93800 7.07100  1.000 56.14716  ?  29  ASP A C      1 
ATOM   434  O O      . ASP A 1 29  ? 29.22700  -22.14100 7.28700  1.000 53.62838  ?  29  ASP A O      1 
ATOM   435  C CB     . ASP A 1 29  ? 31.54800  -21.02200 8.28100  1.000 63.07047  ?  29  ASP A CB     1 
ATOM   436  C CG     . ASP A 1 29  ? 32.99100  -20.57900 8.32600  1.000 65.29065  ?  29  ASP A CG     1 
ATOM   437  O OD1    . ASP A 1 29  ? 33.55800  -20.30300 7.24400  1.000 66.50964  ?  29  ASP A OD1    1 
ATOM   438  O OD2    . ASP A 1 29  ? 33.55700  -20.50700 9.44200  1.000 67.34331  -1 29  ASP A OD2    1 
ATOM   439  H H      . ASP A 1 29  ? 31.05000  -18.39500 6.84100  1.000 60.17966  ?  29  ASP A H      1 
ATOM   440  H HA     . ASP A 1 29  ? 31.20100  -20.42100 6.34200  1.000 62.09880  ?  29  ASP A HA     1 
ATOM   441  H HB2    . ASP A 1 29  ? 31.14800  -20.83400 9.14500  1.000 75.80233  ?  29  ASP A HB2    1 
ATOM   442  H HB3    . ASP A 1 29  ? 31.53100  -21.97600 8.10800  1.000 75.80233  ?  29  ASP A HB3    1 
ATOM   443  N N      . ALA A 1 30  ? 28.35200  -20.15600 6.71600  1.000 47.77693  ?  30  ALA A N      1 
ATOM   444  C CA     . ALA A 1 30  ? 26.98100  -20.62200 6.68600  1.000 45.85154  ?  30  ALA A CA     1 
ATOM   445  C C      . ALA A 1 30  ? 26.59400  -21.06200 5.28100  1.000 49.35690  ?  30  ALA A C      1 
ATOM   446  O O      . ALA A 1 30  ? 26.83800  -20.34400 4.30400  1.000 54.04991  ?  30  ALA A O      1 
ATOM   447  C CB     . ALA A 1 30  ? 26.03400  -19.51700 7.16400  1.000 47.90741  ?  30  ALA A CB     1 
ATOM   448  H H      . ALA A 1 30  ? 28.44000  -19.33200 6.48400  1.000 57.45008  ?  30  ALA A H      1 
ATOM   449  H HA     . ALA A 1 30  ? 26.89700  -21.39100 7.27100  1.000 55.13962  ?  30  ALA A HA     1 
ATOM   450  H HB1    . ALA A 1 30  ? 25.12100  -19.84100 7.11800  1.000 57.60666  ?  30  ALA A HB1    1 
ATOM   451  H HB2    . ALA A 1 30  ? 26.25600  -19.28400 8.07900  1.000 57.60666  ?  30  ALA A HB2    1 
ATOM   452  H HB3    . ALA A 1 30  ? 26.13900  -18.74100 6.59100  1.000 57.60666  ?  30  ALA A HB3    1 
ATOM   453  N N      . LYS A 1 31  ? 26.00600  -22.25300 5.17800  1.000 51.87416  ?  31  LYS A N      1 
ATOM   454  C CA     . LYS A 1 31  ? 25.44600  -22.71000 3.91000  1.000 53.46429  ?  31  LYS A CA     1 
ATOM   455  C C      . LYS A 1 31  ? 24.11400  -22.03300 3.62000  1.000 51.01886  ?  31  LYS A C      1 
ATOM   456  O O      . LYS A 1 31  ? 23.82900  -21.67700 2.47400  1.000 53.46801  ?  31  LYS A O      1 
ATOM   457  C CB     . LYS A 1 31  ? 25.28400  -24.23400 3.93700  1.000 61.02145  ?  31  LYS A CB     1 
ATOM   458  C CG     . LYS A 1 31  ? 24.80900  -24.84100 2.62200  1.000 71.68208  ?  31  LYS A CG     1 
ATOM   459  C CD     . LYS A 1 31  ? 25.89500  -24.78600 1.54800  1.000 79.26063  ?  31  LYS A CD     1 
ATOM   460  C CE     . LYS A 1 31  ? 25.40300  -25.39100 0.24300  1.000 82.37613  ?  31  LYS A CE     1 
ATOM   461  N NZ     . LYS A 1 31  ? 26.10800  -24.81800 -0.94600 1.000 95.70881  ?  31  LYS A NZ     1 
ATOM   462  H H      . LYS A 1 31  ? 25.91800  -22.81200 5.82500  1.000 62.36676  ?  31  LYS A H      1 
ATOM   463  H HA     . LYS A 1 31  ? 26.05600  -22.48800 3.19000  1.000 64.27491  ?  31  LYS A HA     1 
ATOM   464  H HB2    . LYS A 1 31  ? 26.14200  -24.63300 4.15100  1.000 73.34350  ?  31  LYS A HB2    1 
ATOM   465  H HB3    . LYS A 1 31  ? 24.63300  -24.46400 4.61800  1.000 73.34350  ?  31  LYS A HB3    1 
ATOM   466  H HG2    . LYS A 1 31  ? 24.57000  -25.77000 2.76500  1.000 86.13626  ?  31  LYS A HG2    1 
ATOM   467  H HG3    . LYS A 1 31  ? 24.03900  -24.34600 2.30100  1.000 86.13626  ?  31  LYS A HG3    1 
ATOM   468  H HD2    . LYS A 1 31  ? 26.14100  -23.86200 1.38400  1.000 95.23052  ?  31  LYS A HD2    1 
ATOM   469  H HD3    . LYS A 1 31  ? 26.66900  -25.28800 1.84600  1.000 95.23052  ?  31  LYS A HD3    1 
ATOM   470  H HE2    . LYS A 1 31  ? 25.56200  -26.34800 0.25600  1.000 98.96913  ?  31  LYS A HE2    1 
ATOM   471  H HE3    . LYS A 1 31  ? 24.45500  -25.21300 0.14600  1.000 98.96913  ?  31  LYS A HE3    1 
ATOM   472  H HZ1    . LYS A 1 31  ? 25.79100  -25.18400 -1.69300 1.000 114.96834 ?  31  LYS A HZ1    1 
ATOM   473  H HZ2    . LYS A 1 31  ? 25.98100  -23.93800 -0.98000 1.000 114.96834 ?  31  LYS A HZ2    1 
ATOM   474  H HZ3    . LYS A 1 31  ? 26.98100  -24.98200 -0.89100 1.000 114.96834 ?  31  LYS A HZ3    1 
ATOM   475  N N      . HIS A 1 32  ? 23.28600  -21.84700 4.65100  1.000 52.75868  ?  32  HIS A N      1 
ATOM   476  C CA     . HIS A 1 32  ? 22.01900  -21.14800 4.53700  1.000 47.77003  ?  32  HIS A CA     1 
ATOM   477  C C      . HIS A 1 32  ? 21.88500  -20.19200 5.70800  1.000 44.90368  ?  32  HIS A C      1 
ATOM   478  O O      . HIS A 1 32  ? 22.25900  -20.52500 6.83600  1.000 43.97515  ?  32  HIS A O      1 
ATOM   479  C CB     . HIS A 1 32  ? 20.83000  -22.12400 4.53000  1.000 52.63220  ?  32  HIS A CB     1 
ATOM   480  C CG     . HIS A 1 32  ? 20.77900  -23.00700 3.32100  1.000 47.16256  ?  32  HIS A CG     1 
ATOM   481  N ND1    . HIS A 1 32  ? 21.16400  -24.33100 3.35100  1.000 56.79151  ?  32  HIS A ND1    1 
ATOM   482  C CD2    . HIS A 1 32  ? 20.38600  -22.75400 2.05100  1.000 51.85220  ?  32  HIS A CD2    1 
ATOM   483  C CE1    . HIS A 1 32  ? 21.01500  -24.86300 2.14600  1.000 52.81278  ?  32  HIS A CE1    1 
ATOM   484  N NE2    . HIS A 1 32  ? 20.54000  -23.92500 1.33900  1.000 59.03223  ?  32  HIS A NE2    1 
ATOM   485  H H      . HIS A 1 32  ? 23.44700  -22.12800 5.44700  1.000 63.42818  ?  32  HIS A H      1 
ATOM   486  H HA     . HIS A 1 32  ? 21.99900  -20.64100 3.71100  1.000 57.44181  ?  32  HIS A HA     1 
ATOM   487  H HB2    . HIS A 1 32  ? 20.89200  -22.69600 5.31100  1.000 63.27640  ?  32  HIS A HB2    1 
ATOM   488  H HB3    . HIS A 1 32  ? 20.00700  -21.61200 4.55800  1.000 63.27640  ?  32  HIS A HB3    1 
ATOM   489  H HD1    . HIS A 1 32  ? 21.45600  -24.74700 4.04400  1.000 68.26758  ?  32  HIS A HD1    1 
ATOM   490  H HD2    . HIS A 1 32  ? 20.07200  -21.94400 1.72000  1.000 62.34041  ?  32  HIS A HD2    1 
ATOM   491  H HE1    . HIS A 1 32  ? 21.20900  -25.74100 1.90900  1.000 63.49311  ?  32  HIS A HE1    1 
ATOM   492  N N      . VAL A 1 33  ? 21.35900  -18.99100 5.43400  1.000 44.90757  ?  33  VAL A N      1 
ATOM   493  C CA     . VAL A 1 33  ? 21.06700  -18.00600 6.46000  1.000 45.83165  ?  33  VAL A CA     1 
ATOM   494  C C      . VAL A 1 33  ? 19.61600  -17.58400 6.29700  1.000 44.71562  ?  33  VAL A C      1 
ATOM   495  O O      . VAL A 1 33  ? 19.18800  -17.25400 5.18800  1.000 48.48076  ?  33  VAL A O      1 
ATOM   496  C CB     . VAL A 1 33  ? 21.99500  -16.77600 6.36500  1.000 48.05060  ?  33  VAL A CB     1 
ATOM   497  C CG1    . VAL A 1 33  ? 21.56200  -15.71400 7.36200  1.000 48.40342  ?  33  VAL A CG1    1 
ATOM   498  C CG2    . VAL A 1 33  ? 23.43900  -17.17400 6.61000  1.000 46.65350  ?  33  VAL A CG2    1 
ATOM   499  H H      . VAL A 1 33  ? 21.16200  -18.72600 4.64000  1.000 54.00686  ?  33  VAL A H      1 
ATOM   500  H HA     . VAL A 1 33  ? 21.18500  -18.40700 7.33600  1.000 55.11575  ?  33  VAL A HA     1 
ATOM   501  H HB     . VAL A 1 33  ? 21.93300  -16.40400 5.47100  1.000 57.77848  ?  33  VAL A HB     1 
ATOM   502  H HG11   . VAL A 1 33  ? 22.27800  -15.06800 7.46600  1.000 58.20187  ?  33  VAL A HG11   1 
ATOM   503  H HG12   . VAL A 1 33  ? 20.76500  -15.27400 7.02800  1.000 58.20187  ?  33  VAL A HG12   1 
ATOM   504  H HG13   . VAL A 1 33  ? 21.37300  -16.13900 8.21300  1.000 58.20187  ?  33  VAL A HG13   1 
ATOM   505  H HG21   . VAL A 1 33  ? 24.00400  -16.39300 6.50100  1.000 56.10197  ?  33  VAL A HG21   1 
ATOM   506  H HG22   . VAL A 1 33  ? 23.52200  -17.51900 7.51200  1.000 56.10197  ?  33  VAL A HG22   1 
ATOM   507  H HG23   . VAL A 1 33  ? 23.69100  -17.85700 5.96900  1.000 56.10197  ?  33  VAL A HG23   1 
ATOM   508  N N      . TYR A 1 34  ? 18.87200  -17.58100 7.40500  1.000 46.55418  ?  34  TYR A N      1 
ATOM   509  C CA     . TYR A 1 34  ? 17.44900  -17.21200 7.39800  1.000 44.78569  ?  34  TYR A CA     1 
ATOM   510  C C      . TYR A 1 34  ? 17.25100  -15.91200 8.14100  1.000 39.62702  ?  34  TYR A C      1 
ATOM   511  O O      . TYR A 1 34  ? 17.22700  -15.90600 9.38800  1.000 42.49655  ?  34  TYR A O      1 
ATOM   512  C CB     . TYR A 1 34  ? 16.60700  -18.33200 8.03400  1.000 41.68332  ?  34  TYR A CB     1 
ATOM   513  C CG     . TYR A 1 34  ? 16.60500  -19.62800 7.24900  1.000 42.48602  ?  34  TYR A CG     1 
ATOM   514  C CD1    . TYR A 1 34  ? 17.65200  -20.53300 7.35900  1.000 45.82163  ?  34  TYR A CD1    1 
ATOM   515  C CD2    . TYR A 1 34  ? 15.54900  -19.94600 6.39900  1.000 44.52348  ?  34  TYR A CD2    1 
ATOM   516  C CE1    . TYR A 1 34  ? 17.65500  -21.72600 6.64400  1.000 44.80765  ?  34  TYR A CE1    1 
ATOM   517  C CE2    . TYR A 1 34  ? 15.54100  -21.13400 5.67000  1.000 47.50305  ?  34  TYR A CE2    1 
ATOM   518  C CZ     . TYR A 1 34  ? 16.59600  -22.01600 5.79900  1.000 43.69400  ?  34  TYR A CZ     1 
ATOM   519  O OH     . TYR A 1 34  ? 16.59600  -23.18100 5.09100  1.000 49.34375  ?  34  TYR A OH     1 
ATOM   520  H H      . TYR A 1 34  ? 19.16900  -17.79100 8.18400  1.000 55.98278  ?  34  TYR A H      1 
ATOM   521  H HA     . TYR A 1 34  ? 17.15700  -17.08100 6.48300  1.000 53.86060  ?  34  TYR A HA     1 
ATOM   522  H HB2    . TYR A 1 34  ? 16.96100  -18.52300 8.91700  1.000 50.13776  ?  34  TYR A HB2    1 
ATOM   523  H HB3    . TYR A 1 34  ? 15.68900  -18.02800 8.10300  1.000 50.13776  ?  34  TYR A HB3    1 
ATOM   524  H HD1    . TYR A 1 34  ? 18.36500  -20.33800 7.92300  1.000 55.10372  ?  34  TYR A HD1    1 
ATOM   525  H HD2    . TYR A 1 34  ? 14.83500  -19.35500 6.31700  1.000 53.54595  ?  34  TYR A HD2    1 
ATOM   526  H HE1    . TYR A 1 34  ? 18.36200  -22.32400 6.73200  1.000 53.88695  ?  34  TYR A HE1    1 
ATOM   527  H HE2    . TYR A 1 34  ? 14.83200  -21.33100 5.10200  1.000 57.12143  ?  34  TYR A HE2    1 
ATOM   528  H HH     . TYR A 1 34  ? 15.87500  -23.26000 4.66800  1.000 59.33027  ?  34  TYR A HH     1 
ATOM   529  N N      . PRO A 1 35  ? 17.08600  -14.78000 7.45200  1.000 44.86382  ?  35  PRO A N      1 
ATOM   530  C CA     . PRO A 1 35  ? 16.80400  -13.50700 8.16600  1.000 39.78271  ?  35  PRO A CA     1 
ATOM   531  C C      . PRO A 1 35  ? 15.33500  -13.44000 8.55300  1.000 40.06122  ?  35  PRO A C      1 
ATOM   532  O O      . PRO A 1 35  ? 14.44800  -13.50600 7.69400  1.000 43.75299  ?  35  PRO A O      1 
ATOM   533  C CB     . PRO A 1 35  ? 17.16900  -12.43100 7.13700  1.000 43.70921  ?  35  PRO A CB     1 
ATOM   534  C CG     . PRO A 1 35  ? 17.68100  -13.15300 5.91100  1.000 47.02269  ?  35  PRO A CG     1 
ATOM   535  C CD     . PRO A 1 35  ? 17.20400  -14.57300 6.00200  1.000 44.38231  ?  35  PRO A CD     1 
ATOM   536  H HA     . PRO A 1 35  ? 17.36300  -13.41200 8.95300  1.000 47.85702  ?  35  PRO A HA     1 
ATOM   537  H HB2    . PRO A 1 35  ? 16.37900  -11.91100 6.92100  1.000 52.56882  ?  35  PRO A HB2    1 
ATOM   538  H HB3    . PRO A 1 35  ? 17.85600  -11.85400 7.50400  1.000 52.56882  ?  35  PRO A HB3    1 
ATOM   539  H HG2    . PRO A 1 35  ? 17.32700  -12.72700 5.11500  1.000 56.54500  ?  35  PRO A HG2    1 
ATOM   540  H HG3    . PRO A 1 35  ? 18.65100  -13.12100 5.90100  1.000 56.54500  ?  35  PRO A HG3    1 
ATOM   541  H HD2    . PRO A 1 35  ? 16.34500  -14.68000 5.56500  1.000 53.37654  ?  35  PRO A HD2    1 
ATOM   542  H HD3    . PRO A 1 35  ? 17.85100  -15.18300 5.61500  1.000 53.37654  ?  35  PRO A HD3    1 
ATOM   543  N N      . VAL A 1 36  ? 15.07500  -13.30100 9.85300  1.000 36.97388  ?  36  VAL A N      1 
ATOM   544  C CA     . VAL A 1 36  ? 13.73900  -13.48700 10.40400 1.000 40.96392  ?  36  VAL A CA     1 
ATOM   545  C C      . VAL A 1 36  ? 13.34600  -12.26800 11.23900 1.000 42.04837  ?  36  VAL A C      1 
ATOM   546  O O      . VAL A 1 36  ? 14.15400  -11.75700 12.03800 1.000 39.33719  ?  36  VAL A O      1 
ATOM   547  C CB     . VAL A 1 36  ? 13.66800  -14.77000 11.25500 1.000 44.29082  ?  36  VAL A CB     1 
ATOM   548  C CG1    . VAL A 1 36  ? 12.52900  -14.69700 12.25900 1.000 49.80934  ?  36  VAL A CG1    1 
ATOM   549  C CG2    . VAL A 1 36  ? 13.51100  -15.99400 10.33800 1.000 45.24804  ?  36  VAL A CG2    1 
ATOM   550  H H      . VAL A 1 36  ? 15.66800  -13.09600 10.44100 1.000 44.48643  ?  36  VAL A H      1 
ATOM   551  H HA     . VAL A 1 36  ? 13.10500  -13.54700 9.67300  1.000 49.27448  ?  36  VAL A HA     1 
ATOM   552  H HB     . VAL A 1 36  ? 14.49200  -14.86300 11.75900 1.000 53.26676  ?  36  VAL A HB     1 
ATOM   553  H HG11   . VAL A 1 36  ? 12.33800  -15.59000 12.58600 1.000 59.88898  ?  36  VAL A HG11   1 
ATOM   554  H HG12   . VAL A 1 36  ? 12.79400  -14.12400 12.99600 1.000 59.88898  ?  36  VAL A HG12   1 
ATOM   555  H HG13   . VAL A 1 36  ? 11.74500  -14.33000 11.82100 1.000 59.88898  ?  36  VAL A HG13   1 
ATOM   556  H HG21   . VAL A 1 36  ? 13.52400  -16.79900 10.88000 1.000 54.41541  ?  36  VAL A HG21   1 
ATOM   557  H HG22   . VAL A 1 36  ? 12.66600  -15.92800 9.86500  1.000 54.41541  ?  36  VAL A HG22   1 
ATOM   558  H HG23   . VAL A 1 36  ? 14.24500  -16.01100 9.70400  1.000 54.41541  ?  36  VAL A HG23   1 
ATOM   559  N N      . PHE A 1 37  ? 12.13200  -11.79000 11.02200 1.000 42.16379  ?  37  PHE A N      1 
ATOM   560  C CA     . PHE A 1 37  ? 11.42200  -10.90900 11.95400 1.000 40.61408  ?  37  PHE A CA     1 
ATOM   561  C C      . PHE A 1 37  ? 10.11800  -11.60200 12.31900 1.000 37.41199  ?  37  PHE A C      1 
ATOM   562  O O      . PHE A 1 37  ? 9.41700   -12.10200 11.43200 1.000 42.37265  ?  37  PHE A O      1 
ATOM   563  C CB     . PHE A 1 37  ? 11.14400  -9.53800  11.33700 1.000 39.46300  ?  37  PHE A CB     1 
ATOM   564  C CG     . PHE A 1 37  ? 10.52800  -8.56100  12.29700 1.000 38.44568  ?  37  PHE A CG     1 
ATOM   565  C CD1    . PHE A 1 37  ? 9.14600   -8.50100  12.45900 1.000 37.62664  ?  37  PHE A CD1    1 
ATOM   566  C CD2    . PHE A 1 37  ? 11.31900  -7.70500  13.04500 1.000 38.86431  ?  37  PHE A CD2    1 
ATOM   567  C CE1    . PHE A 1 37  ? 8.57500   -7.59900  13.34600 1.000 40.44395  ?  37  PHE A CE1    1 
ATOM   568  C CE2    . PHE A 1 37  ? 10.75300  -6.79500  13.93200 1.000 41.27285  ?  37  PHE A CE2    1 
ATOM   569  C CZ     . PHE A 1 37  ? 9.37500   -6.75000  14.07900 1.000 43.58890  ?  37  PHE A CZ     1 
ATOM   570  H H      . PHE A 1 37  ? 11.67500  -11.96400 10.31400 1.000 50.71431  ?  37  PHE A H      1 
ATOM   571  H HA     . PHE A 1 37  ? 11.95200  -10.76000 12.75200 1.000 48.85467  ?  37  PHE A HA     1 
ATOM   572  H HB2    . PHE A 1 37  ? 11.98100  -9.15900  11.02600 1.000 47.47337  ?  37  PHE A HB2    1 
ATOM   573  H HB3    . PHE A 1 37  ? 10.53200  -9.64800  10.59300 1.000 47.47337  ?  37  PHE A HB3    1 
ATOM   574  H HD1    . PHE A 1 37  ? 8.60000   -9.07100  11.96700 1.000 45.26974  ?  37  PHE A HD1    1 
ATOM   575  H HD2    . PHE A 1 37  ? 12.24400  -7.74000  12.95300 1.000 46.75495  ?  37  PHE A HD2    1 
ATOM   576  H HE1    . PHE A 1 37  ? 7.65100   -7.56700  13.44500 1.000 48.65051  ?  37  PHE A HE1    1 
ATOM   577  H HE2    . PHE A 1 37  ? 11.29600  -6.22100  14.42200 1.000 49.64519  ?  37  PHE A HE2    1 
ATOM   578  H HZ     . PHE A 1 37  ? 8.99100   -6.14700  14.67400 1.000 52.42445  ?  37  PHE A HZ     1 
ATOM   579  N N      . VAL A 1 38  ? 9.80800   -11.65300 13.60600 1.000 39.18421  ?  38  VAL A N      1 
ATOM   580  C CA     . VAL A 1 38  ? 8.60100   -12.33100 14.08200 1.000 45.73646  ?  38  VAL A CA     1 
ATOM   581  C C      . VAL A 1 38  ? 7.57300   -11.25700 14.41900 1.000 48.28638  ?  38  VAL A C      1 
ATOM   582  O O      . VAL A 1 38  ? 7.80000   -10.41500 15.29300 1.000 48.78337  ?  38  VAL A O      1 
ATOM   583  C CB     . VAL A 1 38  ? 8.88700   -13.23300 15.29000 1.000 45.53589  ?  38  VAL A CB     1 
ATOM   584  C CG1    . VAL A 1 38  ? 7.58800   -13.85000 15.81200 1.000 48.29359  ?  38  VAL A CG1    1 
ATOM   585  C CG2    . VAL A 1 38  ? 9.87600   -14.32400 14.91900 1.000 45.00986  ?  38  VAL A CG2    1 
ATOM   586  H H      . VAL A 1 38  ? 10.28200  -11.30100 14.23100 1.000 47.13882  ?  38  VAL A H      1 
ATOM   587  H HA     . VAL A 1 38  ? 8.24700   -12.89400 13.37600 1.000 55.00153  ?  38  VAL A HA     1 
ATOM   588  H HB     . VAL A 1 38  ? 9.27700   -12.69500 15.99700 1.000 54.76084  ?  38  VAL A HB     1 
ATOM   589  H HG11   . VAL A 1 38  ? 7.80500   -14.56200 16.43400 1.000 58.07008  ?  38  VAL A HG11   1 
ATOM   590  H HG12   . VAL A 1 38  ? 7.07100   -13.16400 16.26100 1.000 58.07008  ?  38  VAL A HG12   1 
ATOM   591  H HG13   . VAL A 1 38  ? 7.08500   -14.20600 15.06300 1.000 58.07008  ?  38  VAL A HG13   1 
ATOM   592  H HG21   . VAL A 1 38  ? 9.99500   -14.91500 15.67900 1.000 54.12960  ?  38  VAL A HG21   1 
ATOM   593  H HG22   . VAL A 1 38  ? 9.52800   -14.82200 14.16300 1.000 54.12960  ?  38  VAL A HG22   1 
ATOM   594  H HG23   . VAL A 1 38  ? 10.72400  -13.91500 14.68300 1.000 54.12960  ?  38  VAL A HG23   1 
ATOM   595  N N      . LEU A 1 39  ? 6.44800   -11.29600 13.72200 1.000 52.10604  ?  39  LEU A N      1 
ATOM   596  C CA     . LEU A 1 39  ? 5.40300   -10.28200 13.82600 1.000 54.92512  ?  39  LEU A CA     1 
ATOM   597  C C      . LEU A 1 39  ? 4.17500   -10.92000 14.45300 1.000 58.47808  ?  39  LEU A C      1 
ATOM   598  O O      . LEU A 1 39  ? 3.67500   -11.93800 13.95500 1.000 59.87937  ?  39  LEU A O      1 
ATOM   599  C CB     . LEU A 1 39  ? 5.07700   -9.70500  12.44900 1.000 58.42910  ?  39  LEU A CB     1 
ATOM   600  C CG     . LEU A 1 39  ? 3.91200   -8.72900  12.34300 1.000 67.64770  ?  39  LEU A CG     1 
ATOM   601  C CD1    . LEU A 1 39  ? 4.27800   -7.60200  11.39300 1.000 77.15917  ?  39  LEU A CD1    1 
ATOM   602  C CD2    . LEU A 1 39  ? 2.65400   -9.42900  11.87700 1.000 75.45801  ?  39  LEU A CD2    1 
ATOM   603  H H      . LEU A 1 39  ? 6.25700   -11.92000 13.16200 1.000 62.64502  ?  39  LEU A H      1 
ATOM   604  H HA     . LEU A 1 39  ? 5.69700   -9.55700  14.39900 1.000 66.02792  ?  39  LEU A HA     1 
ATOM   605  H HB2    . LEU A 1 39  ? 5.86400   -9.23500  12.13200 1.000 70.23269  ?  39  LEU A HB2    1 
ATOM   606  H HB3    . LEU A 1 39  ? 4.87300   -10.44700 11.85900 1.000 70.23269  ?  39  LEU A HB3    1 
ATOM   607  H HG     . LEU A 1 39  ? 3.72700   -8.35500  13.21900 1.000 81.29501  ?  39  LEU A HG     1 
ATOM   608  H HD11   . LEU A 1 39  ? 3.52100   -7.00100  11.30900 1.000 92.70877  ?  39  LEU A HD11   1 
ATOM   609  H HD12   . LEU A 1 39  ? 5.04200   -7.12300  11.75000 1.000 92.70877  ?  39  LEU A HD12   1 
ATOM   610  H HD13   . LEU A 1 39  ? 4.49900   -7.97800  10.52600 1.000 92.70877  ?  39  LEU A HD13   1 
ATOM   611  H HD21   . LEU A 1 39  ? 1.93500   -8.78000  11.81500 1.000 90.66738  ?  39  LEU A HD21   1 
ATOM   612  H HD22   . LEU A 1 39  ? 2.81700   -9.82600  11.00700 1.000 90.66738  ?  39  LEU A HD22   1 
ATOM   613  H HD23   . LEU A 1 39  ? 2.42100   -10.12000 12.51700 1.000 90.66738  ?  39  LEU A HD23   1 
ATOM   614  N N      . ASP A 1 40  ? 3.70200   -10.33800 15.53800 1.000 68.90391  ?  40  ASP A N      1 
ATOM   615  C CA     . ASP A 1 40  ? 2.49100   -10.81200 16.20100 1.000 70.62321  ?  40  ASP A CA     1 
ATOM   616  C C      . ASP A 1 40  ? 1.28000   -10.27400 15.44600 1.000 80.72932  ?  40  ASP A C      1 
ATOM   617  O O      . ASP A 1 40  ? 0.92700   -9.09700  15.60300 1.000 81.19409  ?  40  ASP A O      1 
ATOM   618  C CB     . ASP A 1 40  ? 2.47600   -10.35800 17.66400 1.000 86.40173  ?  40  ASP A CB     1 
ATOM   619  C CG     . ASP A 1 40  ? 1.49300   -11.14400 18.50600 1.000 99.66294  ?  40  ASP A CG     1 
ATOM   620  O OD1    . ASP A 1 40  ? 0.57400   -11.76600 17.93000 1.000 94.98058  ?  40  ASP A OD1    1 
ATOM   621  O OD2    . ASP A 1 40  ? 1.63900   -11.13500 19.74600 1.000 113.53807 -1 40  ASP A OD2    1 
ATOM   622  H H      . ASP A 1 40  ? 4.06500   -9.65800  15.92000 1.000 82.80246  ?  40  ASP A H      1 
ATOM   623  H HA     . ASP A 1 40  ? 2.45400   -11.78100 16.19500 1.000 84.86563  ?  40  ASP A HA     1 
ATOM   624  H HB2    . ASP A 1 40  ? 3.36100   -10.48000 18.04300 1.000 103.79985 ?  40  ASP A HB2    1 
ATOM   625  H HB3    . ASP A 1 40  ? 2.22500   -9.42200  17.70300 1.000 103.79985 ?  40  ASP A HB3    1 
ATOM   626  N N      . PRO A 1 41  ? 0.61900   -11.08800 14.61800 1.000 82.25841  ?  41  PRO A N      1 
ATOM   627  C CA     . PRO A 1 41  ? -0.49200  -10.55000 13.81300 1.000 80.69482  ?  41  PRO A CA     1 
ATOM   628  C C      . PRO A 1 41  ? -1.64800  -10.03000 14.65100 1.000 101.49417 ?  41  PRO A C      1 
ATOM   629  O O      . PRO A 1 41  ? -2.35100  -9.10500  14.22100 1.000 92.54477  ?  41  PRO A O      1 
ATOM   630  C CB     . PRO A 1 41  ? -0.91300  -11.74800 12.95000 1.000 93.44311  ?  41  PRO A CB     1 
ATOM   631  C CG     . PRO A 1 41  ? -0.54500  -12.94200 13.77000 1.000 89.61041  ?  41  PRO A CG     1 
ATOM   632  C CD     . PRO A 1 41  ? 0.72400   -12.55800 14.49700 1.000 83.02481  ?  41  PRO A CD     1 
ATOM   633  H HA     . PRO A 1 41  ? -0.16800  -9.83900  13.23800 1.000 96.95156  ?  41  PRO A HA     1 
ATOM   634  H HB2    . PRO A 1 41  ? -1.86800  -11.71900 12.78300 1.000 112.24950 ?  41  PRO A HB2    1 
ATOM   635  H HB3    . PRO A 1 41  ? -0.42900  -11.73900 12.10900 1.000 112.24950 ?  41  PRO A HB3    1 
ATOM   636  H HG2    . PRO A 1 41  ? -1.25600  -13.14000 14.39900 1.000 107.65026 ?  41  PRO A HG2    1 
ATOM   637  H HG3    . PRO A 1 41  ? -0.39300  -13.70500 13.19000 1.000 107.65026 ?  41  PRO A HG3    1 
ATOM   638  H HD2    . PRO A 1 41  ? 0.76000   -12.97400 15.37300 1.000 99.74755  ?  41  PRO A HD2    1 
ATOM   639  H HD3    . PRO A 1 41  ? 1.50700   -12.80600 13.98000 1.000 99.74755  ?  41  PRO A HD3    1 
ATOM   640  N N      . HIS A 1 42  ? -1.86900  -10.59900 15.83400 1.000 97.43246  ?  42  HIS A N      1 
ATOM   641  C CA     . HIS A 1 42  ? -2.96800  -10.18300 16.70000 1.000 99.64495  ?  42  HIS A CA     1 
ATOM   642  C C      . HIS A 1 42  ? -2.48800  -9.14800  17.72000 1.000 101.00493 ?  42  HIS A C      1 
ATOM   643  O O      . HIS A 1 42  ? -2.58400  -9.32800  18.93300 1.000 110.11834 ?  42  HIS A O      1 
ATOM   644  C CB     . HIS A 1 42  ? -3.57700  -11.39900 17.38800 1.000 107.97259 ?  42  HIS A CB     1 
ATOM   645  C CG     . HIS A 1 42  ? -3.94000  -12.50700 16.44900 1.000 117.38517 ?  42  HIS A CG     1 
ATOM   646  N ND1    . HIS A 1 42  ? -4.42800  -12.27700 15.18000 1.000 123.27088 ?  42  HIS A ND1    1 
ATOM   647  C CD2    . HIS A 1 42  ? -3.88600  -13.85300 16.59300 1.000 118.73193 ?  42  HIS A CD2    1 
ATOM   648  C CE1    . HIS A 1 42  ? -4.65900  -13.43300 14.58300 1.000 109.31987 ?  42  HIS A CE1    1 
ATOM   649  N NE2    . HIS A 1 42  ? -4.33800  -14.40500 15.41900 1.000 120.11953 ?  42  HIS A NE2    1 
ATOM   650  H H      . HIS A 1 42  ? -1.39200  -11.23600 16.16100 1.000 117.03673 ?  42  HIS A H      1 
ATOM   651  H HA     . HIS A 1 42  ? -3.65400  -9.76600  16.15500 1.000 119.69171 ?  42  HIS A HA     1 
ATOM   652  H HB2    . HIS A 1 42  ? -2.93600  -11.75000 18.02600 1.000 129.68487 ?  42  HIS A HB2    1 
ATOM   653  H HB3    . HIS A 1 42  ? -4.38600  -11.12500 17.84800 1.000 129.68487 ?  42  HIS A HB3    1 
ATOM   654  H HD1    . HIS A 1 42  ? -4.56000  -11.50200 14.83100 1.000 148.04283 ?  42  HIS A HD1    1 
ATOM   655  H HD2    . HIS A 1 42  ? -3.59800  -14.31700 17.34600 1.000 142.59609 ?  42  HIS A HD2    1 
ATOM   656  H HE1    . HIS A 1 42  ? -4.99100  -13.54400 13.72100 1.000 131.30161 ?  42  HIS A HE1    1 
ATOM   657  N N      . PHE A 1 43  ? -1.95800  -8.04000  17.20000 0.000 96.86500  ?  43  PHE A N      1 
ATOM   658  C CA     . PHE A 1 43  ? -1.53900  -6.94200  18.06300 1.000 100.27320 ?  43  PHE A CA     1 
ATOM   659  C C      . PHE A 1 43  ? -2.72000  -6.19500  18.66600 1.000 108.84175 ?  43  PHE A C      1 
ATOM   660  O O      . PHE A 1 43  ? -2.51100  -5.34900  19.54200 1.000 113.30872 ?  43  PHE A O      1 
ATOM   661  C CB     . PHE A 1 43  ? -0.65400  -5.96400  17.29000 1.000 99.53682  ?  43  PHE A CB     1 
ATOM   662  C CG     . PHE A 1 43  ? 0.54300   -5.48800  18.06400 1.000 95.04357  ?  43  PHE A CG     1 
ATOM   663  C CD1    . PHE A 1 43  ? 1.54100   -6.37400  18.44200 1.000 101.59944 ?  43  PHE A CD1    1 
ATOM   664  C CD2    . PHE A 1 43  ? 0.67300   -4.15500  18.41500 1.000 104.09952 ?  43  PHE A CD2    1 
ATOM   665  C CE1    . PHE A 1 43  ? 2.64300   -5.93800  19.15400 1.000 109.62290 ?  43  PHE A CE1    1 
ATOM   666  C CE2    . PHE A 1 43  ? 1.77300   -3.71400  19.12800 1.000 93.91387  ?  43  PHE A CE2    1 
ATOM   667  C CZ     . PHE A 1 43  ? 2.75900   -4.60800  19.49700 1.000 106.76908 ?  43  PHE A CZ     1 
ATOM   668  H H      . PHE A 1 43  ? -1.83300  -7.90400  16.36000 1.000 116.35577 ?  43  PHE A H      1 
ATOM   669  H HA     . PHE A 1 43  ? -1.00800  -7.30700  18.78800 1.000 120.44561 ?  43  PHE A HA     1 
ATOM   670  H HB2    . PHE A 1 43  ? -0.33200  -6.40300  16.48700 1.000 119.56195 ?  43  PHE A HB2    1 
ATOM   671  H HB3    . PHE A 1 43  ? -1.18300  -5.18600  17.05300 1.000 119.56195 ?  43  PHE A HB3    1 
ATOM   672  H HD1    . PHE A 1 43  ? 1.46700   -7.27200  18.21300 1.000 122.03710 ?  43  PHE A HD1    1 
ATOM   673  H HD2    . PHE A 1 43  ? 0.01200   -3.54900  18.16900 1.000 125.03719 ?  43  PHE A HD2    1 
ATOM   674  H HE1    . PHE A 1 43  ? 3.30500   -6.54200  19.40200 1.000 131.66525 ?  43  PHE A HE1    1 
ATOM   675  H HE2    . PHE A 1 43  ? 1.84900   -2.81600  19.35800 1.000 112.81441 ?  43  PHE A HE2    1 
ATOM   676  H HZ     . PHE A 1 43  ? 3.50000   -4.31300  19.97700 1.000 128.24067 ?  43  PHE A HZ     1 
ATOM   677  N N      . LEU A 1 44  ? -3.94100  -6.47600  18.21400 1.000 114.58172 ?  44  LEU A N      1 
ATOM   678  C CA     . LEU A 1 44  ? -5.12400  -5.86500  18.80800 1.000 109.57859 ?  44  LEU A CA     1 
ATOM   679  C C      . LEU A 1 44  ? -5.20200  -6.20100  20.29300 1.000 126.24602 ?  44  LEU A C      1 
ATOM   680  O O      . LEU A 1 44  ? -5.10200  -7.36900  20.68600 1.000 134.33615 ?  44  LEU A O      1 
ATOM   681  C CB     . LEU A 1 44  ? -6.37900  -6.35700  18.08800 1.000 109.53912 ?  44  LEU A CB     1 
ATOM   682  C CG     . LEU A 1 44  ? -6.67900  -7.84900  18.24600 1.000 109.28680 ?  44  LEU A CG     1 
ATOM   683  C CD1    . LEU A 1 44  ? -7.75700  -8.07800  19.29900 1.000 114.30476 ?  44  LEU A CD1    1 
ATOM   684  C CD2    . LEU A 1 44  ? -7.08400  -8.46500  16.91400 1.000 109.59134 ?  44  LEU A CD2    1 
ATOM   685  H H      . LEU A 1 44  ? -4.11000  -7.01700  17.56700 1.000 137.61583 ?  44  LEU A H      1 
ATOM   686  H HA     . LEU A 1 44  ? -5.07400  -4.90100  18.71400 1.000 131.61208 ?  44  LEU A HA     1 
ATOM   687  H HB2    . LEU A 1 44  ? -7.14200  -5.86900  18.43600 1.000 131.56472 ?  44  LEU A HB2    1 
ATOM   688  H HB3    . LEU A 1 44  ? -6.27600  -6.18000  17.14000 1.000 131.56472 ?  44  LEU A HB3    1 
ATOM   689  H HG     . LEU A 1 44  ? -5.87100  -8.29500  18.54500 1.000 131.26192 ?  44  LEU A HG     1 
ATOM   690  H HD11   . LEU A 1 44  ? -7.86600  -9.03200  19.43700 1.000 137.28348 ?  44  LEU A HD11   1 
ATOM   691  H HD12   . LEU A 1 44  ? -7.48500  -7.65300  20.12800 1.000 137.28348 ?  44  LEU A HD12   1 
ATOM   692  H HD13   . LEU A 1 44  ? -8.59000  -7.69200  18.98800 1.000 137.28348 ?  44  LEU A HD13   1 
ATOM   693  H HD21   . LEU A 1 44  ? -7.26500  -9.40900  17.04500 1.000 131.62738 ?  44  LEU A HD21   1 
ATOM   694  H HD22   . LEU A 1 44  ? -7.88100  -8.01800  16.58900 1.000 131.62738 ?  44  LEU A HD22   1 
ATOM   695  H HD23   . LEU A 1 44  ? -6.35900  -8.35200  16.28000 1.000 131.62738 ?  44  LEU A HD23   1 
ATOM   696  N N      . GLN A 1 45  ? -5.39500  -5.17600  21.11800 1.000 117.09520 ?  45  GLN A N      1 
ATOM   697  C CA     . GLN A 1 45  ? -5.46000  -5.36100  22.56400 1.000 116.86026 ?  45  GLN A CA     1 
ATOM   698  C C      . GLN A 1 45  ? -6.14600  -4.17400  23.23100 1.000 112.75050 ?  45  GLN A C      1 
ATOM   699  O O      . GLN A 1 45  ? -7.25300  -4.29700  23.75300 1.000 106.07426 ?  45  GLN A O      1 
ATOM   700  C CB     . GLN A 1 45  ? -4.05500  -5.55000  23.14200 1.000 116.57556 ?  45  GLN A CB     1 
ATOM   701  C CG     . GLN A 1 45  ? -3.64500  -7.00400  23.31500 1.000 116.10099 ?  45  GLN A CG     1 
ATOM   702  C CD     . GLN A 1 45  ? -2.30500  -7.15300  24.00900 1.000 116.13731 ?  45  GLN A CD     1 
ATOM   703  O OE1    . GLN A 1 45  ? -1.72100  -6.17300  24.47300 1.000 108.97187 ?  45  GLN A OE1    1 
ATOM   704  N NE2    . GLN A 1 45  ? -1.81000  -8.38300  24.08200 1.000 126.83598 ?  45  GLN A NE2    1 
ATOM   705  H H      . GLN A 1 45  ? -5.49100  -4.36100  20.86300 1.000 140.63201 ?  45  GLN A H      1 
ATOM   706  H HA     . GLN A 1 45  ? -5.97600  -6.15800  22.76000 1.000 140.35009 ?  45  GLN A HA     1 
ATOM   707  H HB2    . GLN A 1 45  ? -3.41500  -5.13200  22.54500 1.000 140.00844 ?  45  GLN A HB2    1 
ATOM   708  H HB3    . GLN A 1 45  ? -4.01900  -5.12800  24.01500 1.000 140.00844 ?  45  GLN A HB3    1 
ATOM   709  H HG2    . GLN A 1 45  ? -4.31300  -7.46000  23.85100 1.000 139.43896 ?  45  GLN A HG2    1 
ATOM   710  H HG3    . GLN A 1 45  ? -3.57900  -7.42100  22.44200 1.000 139.43896 ?  45  GLN A HG3    1 
ATOM   711  H HE21   . GLN A 1 45  ? -2.24600  -9.04300  23.74400 1.000 152.32095 ?  45  GLN A HE21   1 
ATOM   712  H HE22   . GLN A 1 45  ? -1.05200  -8.52000  24.46600 1.000 152.32095 ?  45  GLN A HE22   1 
ATOM   713  N N      . LYS A 1 50  ? -3.76300  2.12500   21.24200 1.000 85.96732  ?  50  LYS A N      1 
ATOM   714  C CA     . LYS A 1 50  ? -2.59300  1.87100   22.07100 1.000 87.71557  ?  50  LYS A CA     1 
ATOM   715  C C      . LYS A 1 50  ? -1.29900  2.13600   21.30200 1.000 84.01530  ?  50  LYS A C      1 
ATOM   716  O O      . LYS A 1 50  ? -0.29800  2.56000   21.88300 1.000 82.81351  ?  50  LYS A O      1 
ATOM   717  C CB     . LYS A 1 50  ? -2.60800  0.42900   22.59100 1.000 100.89095 ?  50  LYS A CB     1 
ATOM   718  H H      . LYS A 1 50  ? -3.66200  2.77000   20.68300 1.000 103.27855 ?  50  LYS A H      1 
ATOM   719  H HA     . LYS A 1 50  ? -2.61500  2.47000   22.83400 1.000 105.37645 ?  50  LYS A HA     1 
ATOM   720  N N      . VAL A 1 51  ? -1.32300  1.87700   19.99500 1.000 88.90032  ?  51  VAL A N      1 
ATOM   721  C CA     . VAL A 1 51  ? -0.17400  2.09800   19.11800 1.000 71.35040  ?  51  VAL A CA     1 
ATOM   722  C C      . VAL A 1 51  ? -0.65300  2.87900   17.90400 1.000 69.74694  ?  51  VAL A C      1 
ATOM   723  O O      . VAL A 1 51  ? -1.55900  2.43600   17.19300 1.000 72.11309  ?  51  VAL A O      1 
ATOM   724  C CB     . VAL A 1 51  ? 0.48900   0.78200   18.68900 1.000 75.09449  ?  51  VAL A CB     1 
ATOM   725  C CG1    . VAL A 1 51  ? 1.61500   1.05000   17.70200 1.000 70.81696  ?  51  VAL A CG1    1 
ATOM   726  C CG2    . VAL A 1 51  ? 1.00500   0.03300   19.91000 1.000 89.42760  ?  51  VAL A CG2    1 
ATOM   727  H H      . VAL A 1 51  ? -2.01100  1.56600   19.58400 1.000 106.79816 ?  51  VAL A H      1 
ATOM   728  H HA     . VAL A 1 51  ? 0.48700   2.63300   19.58400 1.000 85.73825  ?  51  VAL A HA     1 
ATOM   729  H HB     . VAL A 1 51  ? -0.16900  0.22400   18.24600 1.000 90.23116  ?  51  VAL A HB     1 
ATOM   730  H HG11   . VAL A 1 51  ? 2.13900   0.24100   17.59300 1.000 85.09812  ?  51  VAL A HG11   1 
ATOM   731  H HG12   . VAL A 1 51  ? 1.23300   1.31400   16.85000 1.000 85.09812  ?  51  VAL A HG12   1 
ATOM   732  H HG13   . VAL A 1 51  ? 2.17600   1.76300   18.04700 1.000 85.09812  ?  51  VAL A HG13   1 
ATOM   733  H HG21   . VAL A 1 51  ? 1.50600   -0.74400  19.61500 1.000 107.43089 ?  51  VAL A HG21   1 
ATOM   734  H HG22   . VAL A 1 51  ? 1.58000   0.62200   20.42200 1.000 107.43089 ?  51  VAL A HG22   1 
ATOM   735  H HG23   . VAL A 1 51  ? 0.25100   -0.24700  20.45200 1.000 107.43089 ?  51  VAL A HG23   1 
ATOM   736  N N      . SER A 1 52  ? -0.05000  4.03900   17.66600 1.000 64.09325  ?  52  SER A N      1 
ATOM   737  C CA     A SER A 1 52  ? -0.43800  4.86600   16.53600 0.790 60.24603  ?  52  SER A CA     1 
ATOM   738  C CA     B SER A 1 52  ? -0.43700  4.86800   16.53600 0.210 59.97593  ?  52  SER A CA     1 
ATOM   739  C C      . SER A 1 52  ? 0.06000   4.25500   15.22800 1.000 54.02112  ?  52  SER A C      1 
ATOM   740  O O      . SER A 1 52  ? 1.07900   3.57200   15.18200 1.000 51.90251  ?  52  SER A O      1 
ATOM   741  C CB     A SER A 1 52  ? 0.11200   6.28900   16.69300 0.790 57.24368  ?  52  SER A CB     1 
ATOM   742  C CB     B SER A 1 52  ? 0.12200   6.28300   16.69400 0.210 57.21600  ?  52  SER A CB     1 
ATOM   743  O OG     A SER A 1 52  ? 1.47600   6.33000   16.31900 0.790 59.61286  ?  52  SER A OG     1 
ATOM   744  O OG     B SER A 1 52  ? 1.48500   6.33300   16.31200 0.210 59.54189  ?  52  SER A OG     1 
ATOM   745  H H      A SER A 1 52  ? 0.58600   4.36700   18.14400 0.790 77.02967  ?  52  SER A H      1 
ATOM   746  H H      B SER A 1 52  ? 0.58600   4.36700   18.14400 0.210 77.02967  ?  52  SER A H      1 
ATOM   747  H HA     A SER A 1 52  ? -1.40600  4.92200   16.49900 0.790 72.41300  ?  52  SER A HA     1 
ATOM   748  H HA     B SER A 1 52  ? -1.40400  4.92900   16.49600 0.210 72.08888  ?  52  SER A HA     1 
ATOM   749  H HB2    A SER A 1 52  ? -0.39200  6.89000   16.12200 0.790 68.10356  ?  52  SER A HB2    1 
ATOM   750  H HB2    B SER A 1 52  ? -0.38600  6.88800   16.13100 0.210 68.07036  ?  52  SER A HB2    1 
ATOM   751  H HB3    A SER A 1 52  ? 0.02800   6.56300   17.61900 0.790 68.10356  ?  52  SER A HB3    1 
ATOM   752  H HB3    B SER A 1 52  ? 0.04400   6.55100   17.62300 0.210 68.07036  ?  52  SER A HB3    1 
ATOM   753  H HG     A SER A 1 52  ? 1.76900   7.11500   16.38500 0.790 71.65321  ?  52  SER A HG     1 
ATOM   754  H HG     B SER A 1 52  ? 1.77800   7.11600   16.39400 0.210 71.56804  ?  52  SER A HG     1 
ATOM   755  N N      . VAL A 1 53  ? -0.68600  4.51600   14.15200 1.000 50.30748  ?  53  VAL A N      1 
ATOM   756  C CA     . VAL A 1 53  ? -0.28100  4.04400   12.83700 1.000 50.68062  ?  53  VAL A CA     1 
ATOM   757  C C      . VAL A 1 53  ? 1.05800   4.64600   12.44800 1.000 48.61252  ?  53  VAL A C      1 
ATOM   758  O O      . VAL A 1 53  ? 1.83600   4.02300   11.71100 1.000 47.56456  ?  53  VAL A O      1 
ATOM   759  C CB     . VAL A 1 53  ? -1.37700  4.36600   11.79200 1.000 57.20100  ?  53  VAL A CB     1 
ATOM   760  C CG1    . VAL A 1 53  ? -1.58800  5.88500   11.67600 1.000 50.75225  ?  53  VAL A CG1    1 
ATOM   761  C CG2    . VAL A 1 53  ? -1.01800  3.76800   10.44100 1.000 54.31602  ?  53  VAL A CG2    1 
ATOM   762  H H      . VAL A 1 53  ? -1.42200  4.96100   14.16100 1.000 60.48675  ?  53  VAL A H      1 
ATOM   763  H HA     . VAL A 1 53  ? -0.17900  3.08000   12.86900 1.000 60.93452  ?  53  VAL A HA     1 
ATOM   764  H HB     . VAL A 1 53  ? -2.21200  3.96900   12.08400 1.000 68.75897  ?  53  VAL A HB     1 
ATOM   765  H HG11   . VAL A 1 53  ? -2.27900  6.05900   11.01800 1.000 61.02047  ?  53  VAL A HG11   1 
ATOM   766  H HG12   . VAL A 1 53  ? -1.85800  6.23300   12.54000 1.000 61.02047  ?  53  VAL A HG12   1 
ATOM   767  H HG13   . VAL A 1 53  ? -0.75500  6.29900   11.39900 1.000 61.02047  ?  53  VAL A HG13   1 
ATOM   768  H HG21   . VAL A 1 53  ? -1.77000  3.87700   9.83700  1.000 65.29700  ?  53  VAL A HG21   1 
ATOM   769  H HG22   . VAL A 1 53  ? -0.24100  4.22800   10.08800 1.000 65.29700  ?  53  VAL A HG22   1 
ATOM   770  H HG23   . VAL A 1 53  ? -0.82100  2.82500   10.55500 1.000 65.29700  ?  53  VAL A HG23   1 
ATOM   771  N N      . ASN A 1 54  ? 1.35800   5.85200   12.93600 1.000 47.11727  ?  54  ASN A N      1 
ATOM   772  C CA     . ASN A 1 54  ? 2.61600   6.50100   12.58800 1.000 47.55913  ?  54  ASN A CA     1 
ATOM   773  C C      . ASN A 1 54  ? 3.81900   5.63800   12.99000 1.000 47.77445  ?  54  ASN A C      1 
ATOM   774  O O      . ASN A 1 54  ? 4.75000   5.44600   12.20000 1.000 40.56955  ?  54  ASN A O      1 
ATOM   775  C CB     . ASN A 1 54  ? 2.70300   7.88600   13.25700 1.000 44.35922  ?  54  ASN A CB     1 
ATOM   776  C CG     . ASN A 1 54  ? 1.95600   8.96300   12.47400 1.000 45.05412  ?  54  ASN A CG     1 
ATOM   777  O OD1    . ASN A 1 54  ? 1.76000   8.86000   11.26300 1.000 45.99700  ?  54  ASN A OD1    1 
ATOM   778  N ND2    . ASN A 1 54  ? 1.53800   10.02200  13.17400 1.000 50.96233  ?  54  ASN A ND2    1 
ATOM   779  H H      . ASN A 1 54  ? 0.85500   6.30900   13.46300 1.000 56.65850  ?  54  ASN A H      1 
ATOM   780  H HA     . ASN A 1 54  ? 2.64000   6.62400   11.62600 1.000 57.18873  ?  54  ASN A HA     1 
ATOM   781  H HB2    . ASN A 1 54  ? 2.31400   7.83400   14.14400 1.000 53.34883  ?  54  ASN A HB2    1 
ATOM   782  H HB3    . ASN A 1 54  ? 3.63500   8.15000   13.31800 1.000 53.34883  ?  54  ASN A HB3    1 
ATOM   783  H HD21   . ASN A 1 54  ? 1.69500   10.06900  14.01800 1.000 61.27257  ?  54  ASN A HD21   1 
ATOM   784  H HD22   . ASN A 1 54  ? 1.11200   10.65700  12.78000 1.000 61.27257  ?  54  ASN A HD22   1 
ATOM   785  N N      . ARG A 1 55  ? 3.81600   5.11500   14.21900 1.000 48.63194  ?  55  ARG A N      1 
ATOM   786  C CA     . ARG A 1 55  ? 4.96100   4.32600   14.66100 1.000 46.44531  ?  55  ARG A CA     1 
ATOM   787  C C      . ARG A 1 55  ? 4.96500   2.93700   14.02000 1.000 48.28249  ?  55  ARG A C      1 
ATOM   788  O O      . ARG A 1 55  ? 6.02100   2.44300   13.60300 1.000 45.74868  ?  55  ARG A O      1 
ATOM   789  C CB     . ARG A 1 55  ? 4.98000   4.19000   16.18000 1.000 50.89167  ?  55  ARG A CB     1 
ATOM   790  C CG     . ARG A 1 55  ? 6.16900   3.32700   16.66100 1.000 50.76786  ?  55  ARG A CG     1 
ATOM   791  C CD     . ARG A 1 55  ? 6.52200   3.55700   18.11500 1.000 53.54767  ?  55  ARG A CD     1 
ATOM   792  N NE     . ARG A 1 55  ? 5.65200   2.80400   19.01800 1.000 64.93797  ?  55  ARG A NE     1 
ATOM   793  C CZ     . ARG A 1 55  ? 4.67400   3.33000   19.74500 1.000 63.04212  ?  55  ARG A CZ     1 
ATOM   794  N NH1    . ARG A 1 55  ? 4.38900   4.63300   19.68600 1.000 56.65144  ?  55  ARG A NH1    1 
ATOM   795  N NH2    . ARG A 1 55  ? 3.96900   2.54000   20.55000 1.000 58.28490  ?  55  ARG A NH2    1 
ATOM   796  H H      . ARG A 1 55  ? 3.18400   5.20100   14.79600 1.000 58.47610  ?  55  ARG A H      1 
ATOM   797  H HA     . ARG A 1 55  ? 5.76500   4.79900   14.39200 1.000 55.85214  ?  55  ARG A HA     1 
ATOM   798  H HB2    . ARG A 1 55  ? 5.06200   5.07000   16.57900 1.000 61.18778  ?  55  ARG A HB2    1 
ATOM   799  H HB3    . ARG A 1 55  ? 4.15800   3.76700   16.47300 1.000 61.18778  ?  55  ARG A HB3    1 
ATOM   800  H HG2    . ARG A 1 55  ? 5.94100   2.39000   16.55400 1.000 61.03921  ?  55  ARG A HG2    1 
ATOM   801  H HG3    . ARG A 1 55  ? 6.95000   3.54100   16.12700 1.000 61.03921  ?  55  ARG A HG3    1 
ATOM   802  H HD2    . ARG A 1 55  ? 7.43700   3.27400   18.27000 1.000 64.37497  ?  55  ARG A HD2    1 
ATOM   803  H HD3    . ARG A 1 55  ? 6.42700   4.50000   18.32000 1.000 64.37497  ?  55  ARG A HD3    1 
ATOM   804  H HE     . ARG A 1 55  ? 5.78400   1.95600   19.08300 1.000 78.04334  ?  55  ARG A HE     1 
ATOM   805  H HH11   . ARG A 1 55  ? 4.84200   5.15000   19.17000 1.000 68.09950  ?  55  ARG A HH11   1 
ATOM   806  H HH12   . ARG A 1 55  ? 3.75100   4.95500   20.16500 1.000 68.09950  ?  55  ARG A HH12   1 
ATOM   807  H HH21   . ARG A 1 55  ? 4.14900   1.70000   20.59400 1.000 70.05965  ?  55  ARG A HH21   1 
ATOM   808  H HH22   . ARG A 1 55  ? 3.33300   2.86900   21.02600 1.000 70.05965  ?  55  ARG A HH22   1 
ATOM   809  N N      . TYR A 1 56  ? 3.80500   2.28300   13.94300 1.000 44.41287  ?  56  TYR A N      1 
ATOM   810  C CA     . TYR A 1 56  ? 3.76700   0.95900   13.34400 1.000 46.62331  ?  56  TYR A CA     1 
ATOM   811  C C      . TYR A 1 56  ? 4.15800   1.00600   11.87200 1.000 46.22388  ?  56  TYR A C      1 
ATOM   812  O O      . TYR A 1 56  ? 4.89200   0.13600   11.39000 1.000 44.03788  ?  56  TYR A O      1 
ATOM   813  C CB     . TYR A 1 56  ? 2.38200   0.33200   13.50600 1.000 55.59288  ?  56  TYR A CB     1 
ATOM   814  C CG     . TYR A 1 56  ? 2.43800   -1.17800  13.48700 1.000 61.52561  ?  56  TYR A CG     1 
ATOM   815  C CD1    . TYR A 1 56  ? 2.64000   -1.86800  12.29800 1.000 61.14321  ?  56  TYR A CD1    1 
ATOM   816  C CD2    . TYR A 1 56  ? 2.32000   -1.91200  14.65900 1.000 73.47771  ?  56  TYR A CD2    1 
ATOM   817  C CE1    . TYR A 1 56  ? 2.70100   -3.24600  12.27300 1.000 68.03865  ?  56  TYR A CE1    1 
ATOM   818  C CE2    . TYR A 1 56  ? 2.38500   -3.29800  14.64400 1.000 83.09261  ?  56  TYR A CE2    1 
ATOM   819  C CZ     . TYR A 1 56  ? 2.57600   -3.95500  13.44700 1.000 80.56241  ?  56  TYR A CZ     1 
ATOM   820  O OH     . TYR A 1 56  ? 2.64000   -5.32900  13.41600 1.000 87.23314  ?  56  TYR A OH     1 
ATOM   821  H H      . TYR A 1 56  ? 3.04800   2.57900   14.22300 1.000 53.41321  ?  56  TYR A H      1 
ATOM   822  H HA     . TYR A 1 56  ? 4.40400   0.39700   13.81200 1.000 56.06574  ?  56  TYR A HA     1 
ATOM   823  H HB2    . TYR A 1 56  ? 2.00400   0.61100   14.35400 1.000 66.82923  ?  56  TYR A HB2    1 
ATOM   824  H HB3    . TYR A 1 56  ? 1.81300   0.62400   12.77700 1.000 66.82923  ?  56  TYR A HB3    1 
ATOM   825  H HD1    . TYR A 1 56  ? 2.73600   -1.39200  11.50500 1.000 73.48963  ?  56  TYR A HD1    1 
ATOM   826  H HD2    . TYR A 1 56  ? 2.19500   -1.46900  15.46700 1.000 88.29102  ?  56  TYR A HD2    1 
ATOM   827  H HE1    . TYR A 1 56  ? 2.82500   -3.69400  11.46800 1.000 81.76416  ?  56  TYR A HE1    1 
ATOM   828  H HE2    . TYR A 1 56  ? 2.30100   -3.78000  15.43500 1.000 99.82890  ?  56  TYR A HE2    1 
ATOM   829  H HH     . TYR A 1 56  ? 2.55800   -5.63800  14.19300 1.000 104.79754 ?  56  TYR A HH     1 
ATOM   830  N N      . ASN A 1 57  ? 3.68600   2.02000   11.14000 1.000 46.08628  ?  57  ASN A N      1 
ATOM   831  C CA     . ASN A 1 57  ? 4.08700   2.15200   9.74500  1.000 45.76001  ?  57  ASN A CA     1 
ATOM   832  C C      . ASN A 1 57  ? 5.57100   2.45400   9.61500  1.000 44.20396  ?  57  ASN A C      1 
ATOM   833  O O      . ASN A 1 57  ? 6.20700   2.02700   8.64100  1.000 44.82117  ?  57  ASN A O      1 
ATOM   834  C CB     . ASN A 1 57  ? 3.26600   3.24300   9.06000  1.000 44.93730  ?  57  ASN A CB     1 
ATOM   835  C CG     . ASN A 1 57  ? 3.55300   3.33300   7.56900  1.000 46.74911  ?  57  ASN A CG     1 
ATOM   836  O OD1    . ASN A 1 57  ? 3.31400   2.38400   6.82800  1.000 50.52654  ?  57  ASN A OD1    1 
ATOM   837  N ND2    . ASN A 1 57  ? 4.07100   4.47900   7.13100  1.000 45.80724  ?  57  ASN A ND2    1 
ATOM   838  H H      . ASN A 1 57  ? 3.14700   2.62700   11.42300 1.000 55.42130  ?  57  ASN A H      1 
ATOM   839  H HA     . ASN A 1 57  ? 3.90800   1.31400   9.29200  1.000 55.02979  ?  57  ASN A HA     1 
ATOM   840  H HB2    . ASN A 1 57  ? 2.32200   3.04900   9.17400  1.000 54.04253  ?  57  ASN A HB2    1 
ATOM   841  H HB3    . ASN A 1 57  ? 3.47900   4.10000   9.46100  1.000 54.04253  ?  57  ASN A HB3    1 
ATOM   842  H HD21   . ASN A 1 57  ? 4.22500   5.12000   7.68400  1.000 55.08645  ?  57  ASN A HD21   1 
ATOM   843  H HD22   . ASN A 1 57  ? 4.25100   4.57800   6.29600  1.000 55.08645  ?  57  ASN A HD22   1 
ATOM   844  N N      . PHE A 1 58  ? 6.13800   3.19400   10.56900 1.000 40.81251  ?  58  PHE A N      1 
ATOM   845  C CA     . PHE A 1 58  ? 7.57300   3.41400   10.57600 1.000 38.25384  ?  58  PHE A CA     1 
ATOM   846  C C      . PHE A 1 58  ? 8.33100   2.09400   10.66000 1.000 40.71257  ?  58  PHE A C      1 
ATOM   847  O O      . PHE A 1 58  ? 9.33300   1.89500   9.96900  1.000 39.49831  ?  58  PHE A O      1 
ATOM   848  C CB     . PHE A 1 58  ? 7.93700   4.34200   11.74700 1.000 43.20425  ?  58  PHE A CB     1 
ATOM   849  C CG     . PHE A 1 58  ? 9.35400   4.85500   11.70500 1.000 41.93340  ?  58  PHE A CG     1 
ATOM   850  C CD1    . PHE A 1 58  ? 10.39900  4.07100   12.15400 1.000 41.00018  ?  58  PHE A CD1    1 
ATOM   851  C CD2    . PHE A 1 58  ? 9.62200   6.12400   11.23400 1.000 46.25506  ?  58  PHE A CD2    1 
ATOM   852  C CE1    . PHE A 1 58  ? 11.70300  4.54700   12.11900 1.000 46.66413  ?  58  PHE A CE1    1 
ATOM   853  C CE2    . PHE A 1 58  ? 10.92800  6.60700   11.20400 1.000 42.50427  ?  58  PHE A CE2    1 
ATOM   854  C CZ     . PHE A 1 58  ? 11.95900  5.81700   11.65000 1.000 38.42715  ?  58  PHE A CZ     1 
ATOM   855  H H      . PHE A 1 58  ? 5.71500   3.57300   11.21400 1.000 49.09279  ?  58  PHE A H      1 
ATOM   856  H HA     . PHE A 1 58  ? 7.84100   3.85000   9.75200  1.000 46.02238  ?  58  PHE A HA     1 
ATOM   857  H HB2    . PHE A 1 58  ? 7.34400   5.11000   11.73100 1.000 51.96287  ?  58  PHE A HB2    1 
ATOM   858  H HB3    . PHE A 1 58  ? 7.82400   3.85400   12.57800 1.000 51.96287  ?  58  PHE A HB3    1 
ATOM   859  H HD1    . PHE A 1 58  ? 10.22800  3.21700   12.48100 1.000 49.31798  ?  58  PHE A HD1    1 
ATOM   860  H HD2    . PHE A 1 58  ? 8.92400   6.66100   10.93500 1.000 55.62384  ?  58  PHE A HD2    1 
ATOM   861  H HE1    . PHE A 1 58  ? 12.40300  4.00900   12.41300 1.000 56.11472  ?  58  PHE A HE1    1 
ATOM   862  H HE2    . PHE A 1 58  ? 11.10100  7.46200   10.88200 1.000 51.12289  ?  58  PHE A HE2    1 
ATOM   863  H HZ     . PHE A 1 58  ? 12.83100  6.13900   11.63500 1.000 46.23035  ?  58  PHE A HZ     1 
ATOM   864  N N      . LEU A 1 59  ? 7.86000   1.17400   11.50900 1.000 44.35907  ?  59  LEU A N      1 
ATOM   865  C CA     . LEU A 1 59  ? 8.48100   -0.14900  11.58700 1.000 43.17075  ?  59  LEU A CA     1 
ATOM   866  C C      . LEU A 1 59  ? 8.34200   -0.89800  10.26900 1.000 39.14481  ?  59  LEU A C      1 
ATOM   867  O O      . LEU A 1 59  ? 9.31400   -1.45200  9.74600  1.000 40.68881  ?  59  LEU A O      1 
ATOM   868  C CB     . LEU A 1 59  ? 7.85000   -0.94200  12.73100 1.000 36.01238  ?  59  LEU A CB     1 
ATOM   869  C CG     . LEU A 1 59  ? 8.19400   -2.42900  12.82000 1.000 49.23903  ?  59  LEU A CG     1 
ATOM   870  C CD1    . LEU A 1 59  ? 9.59800   -2.60600  13.39900 1.000 43.88424  ?  59  LEU A CD1    1 
ATOM   871  C CD2    . LEU A 1 59  ? 7.16200   -3.15900  13.66100 1.000 44.14468  ?  59  LEU A CD2    1 
ATOM   872  H H      . LEU A 1 59  ? 7.19500   1.29000   12.04100 1.000 53.34865  ?  59  LEU A H      1 
ATOM   873  H HA     . LEU A 1 59  ? 9.42800   -0.04800  11.77200 1.000 51.92267  ?  59  LEU A HA     1 
ATOM   874  H HB2    . LEU A 1 59  ? 8.13200   -0.53600  13.56500 1.000 43.33263  ?  59  LEU A HB2    1 
ATOM   875  H HB3    . LEU A 1 59  ? 6.88700   -0.88000  12.64000 1.000 43.33263  ?  59  LEU A HB3    1 
ATOM   876  H HG     . LEU A 1 59  ? 8.18200   -2.82200  11.93300 1.000 59.20461  ?  59  LEU A HG     1 
ATOM   877  H HD11   . LEU A 1 59  ? 9.82300   -3.55000  13.39800 1.000 52.77886  ?  59  LEU A HD11   1 
ATOM   878  H HD12   . LEU A 1 59  ? 10.23000  -2.11400  12.85200 1.000 52.77886  ?  59  LEU A HD12   1 
ATOM   879  H HD13   . LEU A 1 59  ? 9.61100   -2.26400  14.30700 1.000 52.77886  ?  59  LEU A HD13   1 
ATOM   880  H HD21   . LEU A 1 59  ? 7.39300   -4.10000  13.69700 1.000 53.09139  ?  59  LEU A HD21   1 
ATOM   881  H HD22   . LEU A 1 59  ? 7.16000   -2.78400  14.55500 1.000 53.09139  ?  59  LEU A HD22   1 
ATOM   882  H HD23   . LEU A 1 59  ? 6.28800   -3.04800  13.25400 1.000 53.09139  ?  59  LEU A HD23   1 
ATOM   883  N N      . LEU A 1 60  ? 7.13400   -0.90900  9.69800  1.000 45.40322  ?  60  LEU A N      1 
ATOM   884  C CA     . LEU A 1 60  ? 6.92400   -1.61100  8.43200  1.000 44.42051  ?  60  LEU A CA     1 
ATOM   885  C C      . LEU A 1 60  ? 7.82300   -1.04600  7.34200  1.000 46.14443  ?  60  LEU A C      1 
ATOM   886  O O      . LEU A 1 60  ? 8.42000   -1.80600  6.56900  1.000 44.15944  ?  60  LEU A O      1 
ATOM   887  C CB     . LEU A 1 60  ? 5.45600   -1.51500  8.01100  1.000 44.62363  ?  60  LEU A CB     1 
ATOM   888  C CG     . LEU A 1 60  ? 4.43200   -2.13600  8.96400  1.000 49.65921  ?  60  LEU A CG     1 
ATOM   889  C CD1    . LEU A 1 60  ? 3.02800   -1.91800  8.42300  1.000 52.65473  ?  60  LEU A CD1    1 
ATOM   890  C CD2    . LEU A 1 60  ? 4.70500   -3.61500  9.16800  1.000 54.63850  ?  60  LEU A CD2    1 
ATOM   891  H H      . LEU A 1 60  ? 6.43300   -0.52600  10.01700 1.000 54.60163  ?  60  LEU A H      1 
ATOM   892  H HA     . LEU A 1 60  ? 7.14100   -2.54900  8.55500  1.000 53.42238  ?  60  LEU A HA     1 
ATOM   893  H HB2    . LEU A 1 60  ? 5.23000   -0.57700  7.92000  1.000 53.66613  ?  60  LEU A HB2    1 
ATOM   894  H HB3    . LEU A 1 60  ? 5.35800   -1.96400  7.15600  1.000 53.66613  ?  60  LEU A HB3    1 
ATOM   895  H HG     . LEU A 1 60  ? 4.50000   -1.70600  9.83100  1.000 59.70882  ?  60  LEU A HG     1 
ATOM   896  H HD11   . LEU A 1 60  ? 2.38700   -2.29000  9.04900  1.000 63.30344  ?  60  LEU A HD11   1 
ATOM   897  H HD12   . LEU A 1 60  ? 2.87400   -0.96600  8.31800  1.000 63.30344  ?  60  LEU A HD12   1 
ATOM   898  H HD13   . LEU A 1 60  ? 2.94800   -2.36300  7.56500  1.000 63.30344  ?  60  LEU A HD13   1 
ATOM   899  H HD21   . LEU A 1 60  ? 3.96900   -4.00700  9.66300  1.000 65.68397  ?  60  LEU A HD21   1 
ATOM   900  H HD22   . LEU A 1 60  ? 4.78600   -4.04300  8.30200  1.000 65.68397  ?  60  LEU A HD22   1 
ATOM   901  H HD23   . LEU A 1 60  ? 5.53100   -3.71800  9.66600  1.000 65.68397  ?  60  LEU A HD23   1 
ATOM   902  N N      . GLU A 1 61  ? 7.93200   0.28300   7.26400  1.000 38.19733  ?  61  GLU A N      1 
ATOM   903  C CA     . GLU A 1 61  ? 8.86300   0.89000   6.31800  1.000 44.90365  ?  61  GLU A CA     1 
ATOM   904  C C      . GLU A 1 61  ? 10.29100  0.41800   6.58100  1.000 40.88232  ?  61  GLU A C      1 
ATOM   905  O O      . GLU A 1 61  ? 11.04600  0.14400   5.64200  1.000 41.32798  ?  61  GLU A O      1 
ATOM   906  C CB     . GLU A 1 61  ? 8.78200   2.42100   6.40600  1.000 45.25929  ?  61  GLU A CB     1 
ATOM   907  C CG     . GLU A 1 61  ? 7.55500   3.00600   5.70100  1.000 43.92560  ?  61  GLU A CG     1 
ATOM   908  C CD     . GLU A 1 61  ? 7.38500   4.52100   5.93000  1.000 49.03794  ?  61  GLU A CD     1 
ATOM   909  O OE1    . GLU A 1 61  ? 8.08300   5.10900   6.79600  1.000 44.22165  ?  61  GLU A OE1    1 
ATOM   910  O OE2    . GLU A 1 61  ? 6.53300   5.11900   5.24500  1.000 52.62412  -1 61  GLU A OE2    1 
ATOM   911  H H      . GLU A 1 61  ? 7.48600   0.84400   7.74000  1.000 45.95456  ?  61  GLU A H      1 
ATOM   912  H HA     . GLU A 1 61  ? 8.61200   0.62600   5.41800  1.000 54.00215  ?  61  GLU A HA     1 
ATOM   913  H HB2    . GLU A 1 61  ? 8.74100   2.67900   7.34000  1.000 54.42892  ?  61  GLU A HB2    1 
ATOM   914  H HB3    . GLU A 1 61  ? 9.57300   2.80000   5.99100  1.000 54.42892  ?  61  GLU A HB3    1 
ATOM   915  H HG2    . GLU A 1 61  ? 7.64100   2.85700   4.74600  1.000 52.82849  ?  61  GLU A HG2    1 
ATOM   916  H HG3    . GLU A 1 61  ? 6.76000   2.56400   6.03600  1.000 52.82849  ?  61  GLU A HG3    1 
ATOM   917  N N      . SER A 1 62  ? 10.67100  0.29800   7.85500  1.000 36.76613  ?  62  SER A N      1 
ATOM   918  C CA     . SER A 1 62  ? 12.02000  -0.16800  8.17400  1.000 41.85778  ?  62  SER A CA     1 
ATOM   919  C C      . SER A 1 62  ? 12.23900  -1.60800  7.71600  1.000 42.31950  ?  62  SER A C      1 
ATOM   920  O O      . SER A 1 62  ? 13.33400  -1.96200  7.26900  1.000 41.83782  ?  62  SER A O      1 
ATOM   921  C CB     . SER A 1 62  ? 12.27100  -0.03500  9.67000  1.000 41.70914  ?  62  SER A CB     1 
ATOM   922  O OG     . SER A 1 62  ? 12.02200  1.30200   10.11000 1.000 44.56352  ?  62  SER A OG     1 
ATOM   923  H H      . SER A 1 62  ? 10.17800  0.47600   8.53700  1.000 44.23713  ?  62  SER A H      1 
ATOM   924  H HA     . SER A 1 62  ? 12.66300  0.38900   7.70800  1.000 50.34711  ?  62  SER A HA     1 
ATOM   925  H HB2    . SER A 1 62  ? 11.67800  -0.63900  10.14500 1.000 50.16873  ?  62  SER A HB2    1 
ATOM   926  H HB3    . SER A 1 62  ? 13.19500  -0.26200  9.85700  1.000 50.16873  ?  62  SER A HB3    1 
ATOM   927  H HG     . SER A 1 62  ? 12.12000  1.35400   10.94300 1.000 53.59400  ?  62  SER A HG     1 
ATOM   928  N N      . LEU A 1 63  ? 11.21400  -2.45400  7.83100  1.000 42.15882  ?  63  LEU A N      1 
ATOM   929  C CA     . LEU A 1 63  ? 11.33100  -3.82900  7.34900  1.000 44.06007  ?  63  LEU A CA     1 
ATOM   930  C C      . LEU A 1 63  ? 11.36300  -3.87800  5.83000  1.000 45.45647  ?  63  LEU A C      1 
ATOM   931  O O      . LEU A 1 63  ? 12.06600  -4.71400  5.24600  1.000 41.08878  ?  63  LEU A O      1 
ATOM   932  C CB     . LEU A 1 63  ? 10.16100  -4.67900  7.87400  1.000 43.62708  ?  63  LEU A CB     1 
ATOM   933  C CG     . LEU A 1 63  ? 10.05500  -4.74100  9.40600  1.000 47.68130  ?  63  LEU A CG     1 
ATOM   934  C CD1    . LEU A 1 63  ? 8.70800   -5.28400  9.82100  1.000 46.22986  ?  63  LEU A CD1    1 
ATOM   935  C CD2    . LEU A 1 63  ? 11.18600  -5.58700  9.97700  1.000 45.52671  ?  63  LEU A CD2    1 
ATOM   936  H H      . LEU A 1 63  ? 10.45100  -2.26000  8.17800  1.000 50.70835  ?  63  LEU A H      1 
ATOM   937  H HA     . LEU A 1 63  ? 12.15900  -4.20300  7.68900  1.000 52.98985  ?  63  LEU A HA     1 
ATOM   938  H HB2    . LEU A 1 63  ? 9.33200   -4.30400  7.53800  1.000 52.47026  ?  63  LEU A HB2    1 
ATOM   939  H HB3    . LEU A 1 63  ? 10.27000  -5.58700  7.55000  1.000 52.47026  ?  63  LEU A HB3    1 
ATOM   940  H HG     . LEU A 1 63  ? 10.13700  -3.84700  9.77200  1.000 57.33533  ?  63  LEU A HG     1 
ATOM   941  H HD11   . LEU A 1 63  ? 8.66300   -5.31200  10.78900 1.000 55.59361  ?  63  LEU A HD11   1 
ATOM   942  H HD12   . LEU A 1 63  ? 8.01300   -4.70200  9.47400  1.000 55.59361  ?  63  LEU A HD12   1 
ATOM   943  H HD13   . LEU A 1 63  ? 8.60200   -6.17800  9.45800  1.000 55.59361  ?  63  LEU A HD13   1 
ATOM   944  H HD21   . LEU A 1 63  ? 11.10400  -5.61300  10.94400 1.000 54.74982  ?  63  LEU A HD21   1 
ATOM   945  H HD22   . LEU A 1 63  ? 11.12300  -6.48500  9.61600  1.000 54.74982  ?  63  LEU A HD22   1 
ATOM   946  H HD23   . LEU A 1 63  ? 12.03500  -5.18900  9.72800  1.000 54.74982  ?  63  LEU A HD23   1 
ATOM   947  N N      . GLU A 1 64  ? 10.57600  -3.01000  5.17000  1.000 44.12604  ?  64  GLU A N      1 
ATOM   948  C CA     . GLU A 1 64  ? 10.62600  -2.93700  3.71700  1.000 54.67606  ?  64  GLU A CA     1 
ATOM   949  C C      . GLU A 1 64  ? 12.02800  -2.56300  3.23800  1.000 50.48340  ?  64  GLU A C      1 
ATOM   950  O O      . GLU A 1 64  ? 12.52100  -3.10800  2.24100  1.000 43.52590  ?  64  GLU A O      1 
ATOM   951  C CB     . GLU A 1 64  ? 9.60300   -1.91700  3.21400  1.000 53.78878  ?  64  GLU A CB     1 
ATOM   952  C CG     . GLU A 1 64  ? 8.39000   -2.52900  2.54900  1.000 77.84417  ?  64  GLU A CG     1 
ATOM   953  C CD     . GLU A 1 64  ? 7.20100   -1.59900  2.57500  1.000 86.98865  ?  64  GLU A CD     1 
ATOM   954  O OE1    . GLU A 1 64  ? 7.35300   -0.44100  2.12500  1.000 92.87589  ?  64  GLU A OE1    1 
ATOM   955  O OE2    . GLU A 1 64  ? 6.12100   -2.01700  3.06300  1.000 82.03371  -1 64  GLU A OE2    1 
ATOM   956  H H      . GLU A 1 64  ? 10.02000  -2.46800  5.53900  1.000 53.06901  ?  64  GLU A H      1 
ATOM   957  H HA     . GLU A 1 64  ? 10.39800  -3.80500  3.34800  1.000 65.72904  ?  64  GLU A HA     1 
ATOM   958  H HB2    . GLU A 1 64  ? 9.29200   -1.39200  3.96800  1.000 64.66430  ?  64  GLU A HB2    1 
ATOM   959  H HB3    . GLU A 1 64  ? 10.03500  -1.34000  2.56400  1.000 64.66430  ?  64  GLU A HB3    1 
ATOM   960  H HG2    . GLU A 1 64  ? 8.59900   -2.72800  1.62300  1.000 93.53078  ?  64  GLU A HG2    1 
ATOM   961  H HG3    . GLU A 1 64  ? 8.14700   -3.34300  3.01700  1.000 93.53078  ?  64  GLU A HG3    1 
ATOM   962  N N      . ASP A 1 65  ? 12.67100  -1.62900  3.93700  1.000 40.80988  ?  65  ASP A N      1 
ATOM   963  C CA     . ASP A 1 65  ? 14.05200  -1.27500  3.60700  1.000 47.18373  ?  65  ASP A CA     1 
ATOM   964  C C      . ASP A 1 65  ? 14.98300  -2.46700  3.76800  1.000 40.80458  ?  65  ASP A C      1 
ATOM   965  O O      . ASP A 1 65  ? 15.86400  -2.69200  2.93800  1.000 42.24942  ?  65  ASP A O      1 
ATOM   966  C CB     . ASP A 1 65  ? 14.51000  -0.10800  4.48800  1.000 44.85520  ?  65  ASP A CB     1 
ATOM   967  C CG     . ASP A 1 65  ? 15.81600  0.49400   4.01100  1.000 45.76947  ?  65  ASP A CG     1 
ATOM   968  O OD1    . ASP A 1 65  ? 15.85100  0.96300   2.85400  1.000 52.57851  ?  65  ASP A OD1    1 
ATOM   969  O OD2    . ASP A 1 65  ? 16.80200  0.47500   4.78400  1.000 42.87989  -1 65  ASP A OD2    1 
ATOM   970  H H      . ASP A 1 65  ? 12.33800  -1.19000  4.59700  1.000 49.08962  ?  65  ASP A H      1 
ATOM   971  H HA     . ASP A 1 65  ? 14.09200  -0.99200  2.68000  1.000 56.73824  ?  65  ASP A HA     1 
ATOM   972  H HB2    . ASP A 1 65  ? 13.83400  0.58700   4.47200  1.000 53.94401  ?  65  ASP A HB2    1 
ATOM   973  H HB3    . ASP A 1 65  ? 14.63800  -0.42600  5.39500  1.000 53.94401  ?  65  ASP A HB3    1 
ATOM   974  N N      . LEU A 1 66  ? 14.81100  -3.24200  4.85200  1.000 40.23139  ?  66  LEU A N      1 
ATOM   975  C CA     A LEU A 1 66  ? 15.64100  -4.42200  5.04900  0.140 47.33192  ?  66  LEU A CA     1 
ATOM   976  C CA     B LEU A 1 66  ? 15.64300  -4.41500  5.04700  0.860 45.69097  ?  66  LEU A CA     1 
ATOM   977  C C      . LEU A 1 66  ? 15.41900  -5.43700  3.93300  1.000 44.23406  ?  66  LEU A C      1 
ATOM   978  O O      . LEU A 1 66  ? 16.37800  -6.03600  3.42800  1.000 47.22801  ?  66  LEU A O      1 
ATOM   979  C CB     A LEU A 1 66  ? 15.33900  -5.03700  6.41200  0.140 39.36101  ?  66  LEU A CB     1 
ATOM   980  C CB     B LEU A 1 66  ? 15.35300  -5.04100  6.40400  0.860 42.55920  ?  66  LEU A CB     1 
ATOM   981  C CG     A LEU A 1 66  ? 16.50900  -5.50400  7.28100  0.140 43.63815  ?  66  LEU A CG     1 
ATOM   982  C CG     B LEU A 1 66  ? 16.06400  -4.46900  7.62100  0.860 40.36298  ?  66  LEU A CG     1 
ATOM   983  C CD1    A LEU A 1 66  ? 17.61400  -4.46300  7.37900  0.140 44.05745  ?  66  LEU A CD1    1 
ATOM   984  C CD1    B LEU A 1 66  ? 15.55300  -5.14200  8.88000  0.860 43.83462  ?  66  LEU A CD1    1 
ATOM   985  C CD2    A LEU A 1 66  ? 15.99700  -5.86900  8.67100  0.140 44.88316  ?  66  LEU A CD2    1 
ATOM   986  C CD2    B LEU A 1 66  ? 17.58300  -4.62400  7.50600  0.860 44.03272  ?  66  LEU A CD2    1 
ATOM   987  H H      A LEU A 1 66  ? 14.23000  -3.10300  5.47100  0.140 48.39544  ?  66  LEU A H      1 
ATOM   988  H H      B LEU A 1 66  ? 14.22900  -3.10400  5.47000  0.860 48.39544  ?  66  LEU A H      1 
ATOM   989  H HA     A LEU A 1 66  ? 16.57600  -4.16400  5.03500  0.140 56.91607  ?  66  LEU A HA     1 
ATOM   990  H HA     B LEU A 1 66  ? 16.57400  -4.14600  5.03100  0.860 54.94693  ?  66  LEU A HA     1 
ATOM   991  H HB2    A LEU A 1 66  ? 14.85700  -4.37400  6.93100  0.140 47.35098  ?  66  LEU A HB2    1 
ATOM   992  H HB2    B LEU A 1 66  ? 14.40200  -4.95400  6.57200  0.860 51.18881  ?  66  LEU A HB2    1 
ATOM   993  H HB3    A LEU A 1 66  ? 14.77700  -5.81400  6.26400  0.140 47.35098  ?  66  LEU A HB3    1 
ATOM   994  H HB3    B LEU A 1 66  ? 15.59700  -5.97900  6.35400  0.860 51.18881  ?  66  LEU A HB3    1 
ATOM   995  H HG     A LEU A 1 66  ? 16.90400  -6.28600  6.86400  0.140 52.48355  ?  66  LEU A HG     1 
ATOM   996  H HG     B LEU A 1 66  ? 15.87700  -3.51900  7.67400  0.860 48.55335  ?  66  LEU A HG     1 
ATOM   997  H HD11   A LEU A 1 66  ? 18.19000  -4.68400  8.12700  0.140 52.98672  ?  66  LEU A HD11   1 
ATOM   998  H HD11   B LEU A 1 66  ? 15.99500  -4.75000  9.65000  0.860 52.71932  ?  66  LEU A HD11   1 
ATOM   999  H HD12   A LEU A 1 66  ? 18.12500  -4.46700  6.55500  0.140 52.98672  ?  66  LEU A HD12   1 
ATOM   1000 H HD12   B LEU A 1 66  ? 14.59500  -5.00700  8.94400  0.860 52.71932  ?  66  LEU A HD12   1 
ATOM   1001 H HD13   A LEU A 1 66  ? 17.21400  -3.59000  7.51600  0.140 52.98672  ?  66  LEU A HD13   1 
ATOM   1002 H HD13   B LEU A 1 66  ? 15.75100  -6.09100  8.83400  0.860 52.71932  ?  66  LEU A HD13   1 
ATOM   1003 H HD21   A LEU A 1 66  ? 16.73700  -6.19800  9.20400  0.140 53.97756  ?  66  LEU A HD21   1 
ATOM   1004 H HD21   B LEU A 1 66  ? 17.99100  -4.36800  8.34800  0.860 52.95704  ?  66  LEU A HD21   1 
ATOM   1005 H HD22   A LEU A 1 66  ? 15.61700  -5.07800  9.08500  0.140 53.97756  ?  66  LEU A HD22   1 
ATOM   1006 H HD22   B LEU A 1 66  ? 17.79200  -5.55000  7.30600  0.860 52.95704  ?  66  LEU A HD22   1 
ATOM   1007 H HD23   A LEU A 1 66  ? 15.31800  -6.55700  8.58700  0.140 53.97756  ?  66  LEU A HD23   1 
ATOM   1008 H HD23   B LEU A 1 66  ? 17.90700  -4.05000  6.79400  0.860 52.95704  ?  66  LEU A HD23   1 
ATOM   1009 N N      . GLN A 1 67  ? 14.15400  -5.65700  3.54400  1.000 46.60953  ?  67  GLN A N      1 
ATOM   1010 C CA     . GLN A 1 67  ? 13.84600  -6.56300  2.45000  1.000 45.38023  ?  67  GLN A CA     1 
ATOM   1011 C C      . GLN A 1 67  ? 14.61200  -6.17000  1.18700  1.000 51.09655  ?  67  GLN A C      1 
ATOM   1012 O O      . GLN A 1 67  ? 15.24400  -7.01400  0.54000  1.000 48.27329  ?  67  GLN A O      1 
ATOM   1013 C CB     . GLN A 1 67  ? 12.34200  -6.56000  2.18600  1.000 46.56523  ?  67  GLN A CB     1 
ATOM   1014 C CG     . GLN A 1 67  ? 11.86400  -7.56500  1.14400  1.000 54.06786  ?  67  GLN A CG     1 
ATOM   1015 C CD     . GLN A 1 67  ? 12.07900  -9.01900  1.56800  1.000 55.40378  ?  67  GLN A CD     1 
ATOM   1016 O OE1    . GLN A 1 67  ? 13.16600  -9.56200  1.43300  1.000 51.43835  ?  67  GLN A OE1    1 
ATOM   1017 N NE2    . GLN A 1 67  ? 11.02400  -9.64800  2.08800  1.000 64.56471  ?  67  GLN A NE2    1 
ATOM   1018 H H      . GLN A 1 67  ? 13.46200  -5.29100  3.90100  1.000 56.04921  ?  67  GLN A H      1 
ATOM   1019 H HA     . GLN A 1 67  ? 14.10900  -7.46300  2.70000  1.000 54.57405  ?  67  GLN A HA     1 
ATOM   1020 H HB2    . GLN A 1 67  ? 11.88500  -6.76400  3.01600  1.000 55.99604  ?  67  GLN A HB2    1 
ATOM   1021 H HB3    . GLN A 1 67  ? 12.08800  -5.67700  1.87500  1.000 55.99604  ?  67  GLN A HB3    1 
ATOM   1022 H HG2    . GLN A 1 67  ? 10.91400  -7.43500  0.99400  1.000 64.99920  ?  67  GLN A HG2    1 
ATOM   1023 H HG3    . GLN A 1 67  ? 12.35300  -7.42000  0.31900  1.000 64.99920  ?  67  GLN A HG3    1 
ATOM   1024 H HE21   . GLN A 1 67  ? 10.27400  -9.23500  2.16800  1.000 77.59542  ?  67  GLN A HE21   1 
ATOM   1025 H HE22   . GLN A 1 67  ? 11.09400  -10.46600 2.34200  1.000 77.59542  ?  67  GLN A HE22   1 
ATOM   1026 N N      . ARG A 1 68  ? 14.58600  -4.87800  0.84100  1.000 49.02611  ?  68  ARG A N      1 
ATOM   1027 C CA     . ARG A 1 68  ? 15.30500  -4.41600  -0.33600 1.000 53.14654  ?  68  ARG A CA     1 
ATOM   1028 C C      . ARG A 1 68  ? 16.80500  -4.67700  -0.20500 1.000 46.30743  ?  68  ARG A C      1 
ATOM   1029 O O      . ARG A 1 68  ? 17.45200  -5.11400  -1.16500 1.000 52.20016  ?  68  ARG A O      1 
ATOM   1030 C CB     . ARG A 1 68  ? 15.05300  -2.92300  -0.55300 1.000 53.21091  ?  68  ARG A CB     1 
ATOM   1031 C CG     . ARG A 1 68  ? 13.63300  -2.58100  -0.97900 1.000 58.70421  ?  68  ARG A CG     1 
ATOM   1032 C CD     . ARG A 1 68  ? 13.57800  -1.21200  -1.64900 1.000 72.92403  ?  68  ARG A CD     1 
ATOM   1033 N NE     . ARG A 1 68  ? 14.01100  -0.16100  -0.73500 1.000 74.88986  ?  68  ARG A NE     1 
ATOM   1034 C CZ     . ARG A 1 68  ? 13.24700  0.37600   0.21000  1.000 73.18759  ?  68  ARG A CZ     1 
ATOM   1035 N NH1    . ARG A 1 68  ? 11.97300  0.03200   0.35100  1.000 68.22720  ?  68  ARG A NH1    1 
ATOM   1036 N NH2    . ARG A 1 68  ? 13.77500  1.27700   1.04100  1.000 73.05720  ?  68  ARG A NH2    1 
ATOM   1037 H H      . ARG A 1 68  ? 14.16400  -4.26200  1.26800  1.000 58.94910  ?  68  ARG A H      1 
ATOM   1038 H HA     . ARG A 1 68  ? 14.97500  -4.90000  -1.10900 1.000 63.89362  ?  68  ARG A HA     1 
ATOM   1039 H HB2    . ARG A 1 68  ? 15.23200  -2.45500  0.27700  1.000 63.97086  ?  68  ARG A HB2    1 
ATOM   1040 H HB3    . ARG A 1 68  ? 15.65200  -2.60600  -1.24800 1.000 63.97086  ?  68  ARG A HB3    1 
ATOM   1041 H HG2    . ARG A 1 68  ? 13.31600  -3.24500  -1.61100 1.000 70.56282  ?  68  ARG A HG2    1 
ATOM   1042 H HG3    . ARG A 1 68  ? 13.05600  -2.56500  -0.19900 1.000 70.56282  ?  68  ARG A HG3    1 
ATOM   1043 H HD2    . ARG A 1 68  ? 14.16400  -1.20700  -2.42100 1.000 87.62660  ?  68  ARG A HD2    1 
ATOM   1044 H HD3    . ARG A 1 68  ? 12.66600  -1.02300  -1.92300 1.000 87.62660  ?  68  ARG A HD3    1 
ATOM   1045 H HE     . ARG A 1 68  ? 14.81600  0.13100   -0.81300 1.000 89.98560  ?  68  ARG A HE     1 
ATOM   1046 H HH11   . ARG A 1 68  ? 11.62400  -0.55000  -0.17600 1.000 81.99041  ?  68  ARG A HH11   1 
ATOM   1047 H HH12   . ARG A 1 68  ? 11.49700  0.39200   0.97000  1.000 81.99041  ?  68  ARG A HH12   1 
ATOM   1048 H HH21   . ARG A 1 68  ? 14.60100  1.50400   0.96100  1.000 87.78641  ?  68  ARG A HH21   1 
ATOM   1049 H HH22   . ARG A 1 68  ? 13.29000  1.63100   1.65700  1.000 87.78641  ?  68  ARG A HH22   1 
ATOM   1050 N N      . SER A 1 69  ? 17.36500  -4.42500  0.97000  1.000 44.22441  ?  69  SER A N      1 
ATOM   1051 C CA     . SER A 1 69  ? 18.79300  -4.63000  1.17400  1.000 47.84206  ?  69  SER A CA     1 
ATOM   1052 C C      . SER A 1 69  ? 19.17800  -6.10300  1.04900  1.000 45.79060  ?  69  SER A C      1 
ATOM   1053 O O      . SER A 1 69  ? 20.21500  -6.42500  0.46900  1.000 45.98795  ?  69  SER A O      1 
ATOM   1054 C CB     . SER A 1 69  ? 19.21200  -4.08500  2.53800  1.000 46.62339  ?  69  SER A CB     1 
ATOM   1055 O OG     . SER A 1 69  ? 19.02200  -2.67600  2.58800  1.000 48.72294  ?  69  SER A OG     1 
ATOM   1056 H H      . SER A 1 69  ? 16.94500  -4.13500  1.66300  1.000 53.18706  ?  69  SER A H      1 
ATOM   1057 H HA     . SER A 1 69  ? 19.27200  -4.13900  0.48800  1.000 57.52825  ?  69  SER A HA     1 
ATOM   1058 H HB2    . SER A 1 69  ? 18.67200  -4.50300  3.22700  1.000 56.06583  ?  69  SER A HB2    1 
ATOM   1059 H HB3    . SER A 1 69  ? 20.15000  -4.28400  2.68500  1.000 56.06583  ?  69  SER A HB3    1 
ATOM   1060 H HG     . SER A 1 69  ? 19.25400  -2.38100  3.33900  1.000 58.58530  ?  69  SER A HG     1 
ATOM   1061 N N      . PHE A 1 70  ? 18.36500  -7.00400  1.60300  1.000 41.81462  ?  70  PHE A N      1 
ATOM   1062 C CA     . PHE A 1 70  ? 18.70400  -8.42400  1.52700  1.000 46.75777  ?  70  PHE A CA     1 
ATOM   1063 C C      . PHE A 1 70  ? 18.54800  -8.96000  0.11200  1.000 45.98431  ?  70  PHE A C      1 
ATOM   1064 O O      . PHE A 1 70  ? 19.32200  -9.81100  -0.32300 1.000 47.46655  ?  70  PHE A O      1 
ATOM   1065 C CB     . PHE A 1 70  ? 17.83900  -9.23600  2.49200  1.000 47.83990  ?  70  PHE A CB     1 
ATOM   1066 C CG     . PHE A 1 70  ? 18.34500  -9.23400  3.90900  1.000 49.28827  ?  70  PHE A CG     1 
ATOM   1067 C CD1    . PHE A 1 70  ? 19.58700  -9.76100  4.21300  1.000 49.24658  ?  70  PHE A CD1    1 
ATOM   1068 C CD2    . PHE A 1 70  ? 17.57400  -8.71000  4.93400  1.000 43.66262  ?  70  PHE A CD2    1 
ATOM   1069 C CE1    . PHE A 1 70  ? 20.05400  -9.76200  5.51900  1.000 50.50505  ?  70  PHE A CE1    1 
ATOM   1070 C CE2    . PHE A 1 70  ? 18.02500  -8.71200  6.22900  1.000 44.45268  ?  70  PHE A CE2    1 
ATOM   1071 C CZ     . PHE A 1 70  ? 19.27700  -9.23900  6.52300  1.000 49.81192  ?  70  PHE A CZ     1 
ATOM   1072 H H      . PHE A 1 70  ? 17.63300  -6.82500  2.01600  1.000 50.29531  ?  70  PHE A H      1 
ATOM   1073 H HA     . PHE A 1 70  ? 19.63100  -8.52700  1.79400  1.000 56.22710  ?  70  PHE A HA     1 
ATOM   1074 H HB2    . PHE A 1 70  ? 16.94400  -8.86300  2.49700  1.000 57.52565  ?  70  PHE A HB2    1 
ATOM   1075 H HB3    . PHE A 1 70  ? 17.81400  -10.15600 2.18800  1.000 57.52565  ?  70  PHE A HB3    1 
ATOM   1076 H HD1    . PHE A 1 70  ? 20.11400  -10.11900 3.53500  1.000 59.21367  ?  70  PHE A HD1    1 
ATOM   1077 H HD2    . PHE A 1 70  ? 16.73700  -8.35200  4.74100  1.000 52.51291  ?  70  PHE A HD2    1 
ATOM   1078 H HE1    . PHE A 1 70  ? 20.89200  -10.11600 5.71400  1.000 60.72383  ?  70  PHE A HE1    1 
ATOM   1079 H HE2    . PHE A 1 70  ? 17.49500  -8.36100  6.90900  1.000 53.46098  ?  70  PHE A HE2    1 
ATOM   1080 H HZ     . PHE A 1 70  ? 19.58900  -9.23700  7.39900  1.000 59.89207  ?  70  PHE A HZ     1 
ATOM   1081 N N      . GLN A 1 71  ? 17.53700  -8.47400  -0.62000 1.000 49.50668  ?  71  GLN A N      1 
ATOM   1082 C CA     . GLN A 1 71  ? 17.33100  -8.94300  -1.99000 1.000 53.25566  ?  71  GLN A CA     1 
ATOM   1083 C C      . GLN A 1 71  ? 18.50100  -8.53800  -2.88200 1.000 53.78459  ?  71  GLN A C      1 
ATOM   1084 O O      . GLN A 1 71  ? 18.92000  -9.30500  -3.76300 1.000 49.87211  ?  71  GLN A O      1 
ATOM   1085 C CB     . GLN A 1 71  ? 16.01900  -8.40100  -2.53800 1.000 56.23514  ?  71  GLN A CB     1 
ATOM   1086 C CG     . GLN A 1 71  ? 14.80000  -9.15600  -2.02500 1.000 75.61501  ?  71  GLN A CG     1 
ATOM   1087 C CD     . GLN A 1 71  ? 13.48100  -8.52100  -2.45300 1.000 95.21409  ?  71  GLN A CD     1 
ATOM   1088 O OE1    . GLN A 1 71  ? 13.46100  -7.45700  -3.08600 1.000 82.94236  ?  71  GLN A OE1    1 
ATOM   1089 N NE2    . GLN A 1 71  ? 12.37300  -9.16800  -2.10300 1.000 75.20173  ?  71  GLN A NE2    1 
ATOM   1090 H H      . GLN A 1 71  ? 16.97100  -7.88500  -0.35100 1.000 59.52579  ?  71  GLN A H      1 
ATOM   1091 H HA     . GLN A 1 71  ? 17.27200  -9.91100  -1.98900 1.000 64.02456  ?  71  GLN A HA     1 
ATOM   1092 H HB2    . GLN A 1 71  ? 15.92800  -7.47200  -2.27500 1.000 67.59994  ?  71  GLN A HB2    1 
ATOM   1093 H HB3    . GLN A 1 71  ? 16.02900  -8.47200  -3.50500 1.000 67.59994  ?  71  GLN A HB3    1 
ATOM   1094 H HG2    . GLN A 1 71  ? 14.82100  -10.06200 -2.37200 1.000 90.85578  ?  71  GLN A HG2    1 
ATOM   1095 H HG3    . GLN A 1 71  ? 14.82300  -9.17200  -1.05600 1.000 90.85578  ?  71  GLN A HG3    1 
ATOM   1096 H HE21   . GLN A 1 71  ? 12.42600  -9.90300  -1.66000 1.000 90.35985  ?  71  GLN A HE21   1 
ATOM   1097 H HE22   . GLN A 1 71  ? 11.60300  -8.85100  -2.32000 1.000 90.35985  ?  71  GLN A HE22   1 
ATOM   1098 N N      . ALA A 1 72  ? 19.05800  -7.34200  -2.65100 1.000 48.83655  ?  72  ALA A N      1 
ATOM   1099 C CA     . ALA A 1 72  ? 20.24200  -6.93200  -3.39100 1.000 51.78524  ?  72  ALA A CA     1 
ATOM   1100 C C      . ALA A 1 72  ? 21.41900  -7.88300  -3.17300 1.000 53.03803  ?  72  ALA A C      1 
ATOM   1101 O O      . ALA A 1 72  ? 22.32300  -7.92700  -4.01200 1.000 59.18094  ?  72  ALA A O      1 
ATOM   1102 C CB     . ALA A 1 72  ? 20.63100  -5.51600  -2.98400 1.000 52.86227  ?  72  ALA A CB     1 
ATOM   1103 H H      . ALA A 1 72  ? 18.77100  -6.76600  -2.08000 1.000 58.72163  ?  72  ALA A H      1 
ATOM   1104 H HA     . ALA A 1 72  ? 20.03700  -6.93200  -4.33900 1.000 62.26006  ?  72  ALA A HA     1 
ATOM   1105 H HB1    . ALA A 1 72  ? 21.41300  -5.24600  -3.49100 1.000 63.55250  ?  72  ALA A HB1    1 
ATOM   1106 H HB2    . ALA A 1 72  ? 19.89200  -4.91800  -3.17500 1.000 63.55250  ?  72  ALA A HB2    1 
ATOM   1107 H HB3    . ALA A 1 72  ? 20.83100  -5.50300  -2.03500 1.000 63.55250  ?  72  ALA A HB3    1 
ATOM   1108 N N      . ARG A 1 73  ? 21.42700  -8.64900  -2.07900 1.000 52.67303  ?  73  ARG A N      1 
ATOM   1109 C CA     . ARG A 1 73  ? 22.53400  -9.53900  -1.75500 1.000 50.50939  ?  73  ARG A CA     1 
ATOM   1110 C C      . ARG A 1 73  ? 22.16600  -11.00800 -1.91800 1.000 53.38031  ?  73  ARG A C      1 
ATOM   1111 O O      . ARG A 1 73  ? 22.81700  -11.87800 -1.31900 1.000 49.26018  ?  73  ARG A O      1 
ATOM   1112 C CB     . ARG A 1 73  ? 23.02500  -9.27700  -0.32900 1.000 51.48843  ?  73  ARG A CB     1 
ATOM   1113 C CG     . ARG A 1 73  ? 23.55600  -7.86900  -0.11500 1.000 59.08599  ?  73  ARG A CG     1 
ATOM   1114 C CD     . ARG A 1 73  ? 23.82800  -7.58100  1.35500  1.000 57.42266  ?  73  ARG A CD     1 
ATOM   1115 N NE     . ARG A 1 73  ? 24.70800  -6.42900  1.52500  1.000 60.77638  ?  73  ARG A NE     1 
ATOM   1116 C CZ     . ARG A 1 73  ? 24.34900  -5.17400  1.30800  1.000 65.39050  ?  73  ARG A CZ     1 
ATOM   1117 N NH1    . ARG A 1 73  ? 23.11200  -4.85800  0.91400  1.000 59.84986  ?  73  ARG A NH1    1 
ATOM   1118 N NH2    . ARG A 1 73  ? 25.23900  -4.20500  1.48900  1.000 65.35732  ?  73  ARG A NH2    1 
ATOM   1119 H H      . ARG A 1 73  ? 20.78900  -8.66800  -1.50300 1.000 63.32540  ?  73  ARG A H      1 
ATOM   1120 H HA     . ARG A 1 73  ? 23.26200  -9.34800  -2.36700 1.000 60.72904  ?  73  ARG A HA     1 
ATOM   1121 H HB2    . ARG A 1 73  ? 22.28700  -9.41200  0.28600  1.000 61.90389  ?  73  ARG A HB2    1 
ATOM   1122 H HB3    . ARG A 1 73  ? 23.74300  -9.89800  -0.12700 1.000 61.90389  ?  73  ARG A HB3    1 
ATOM   1123 H HG2    . ARG A 1 73  ? 24.38700  -7.76300  -0.60300 1.000 71.02095  ?  73  ARG A HG2    1 
ATOM   1124 H HG3    . ARG A 1 73  ? 22.90000  -7.22900  -0.43300 1.000 71.02095  ?  73  ARG A HG3    1 
ATOM   1125 H HD2    . ARG A 1 73  ? 22.98900  -7.39300  1.80500  1.000 69.02496  ?  73  ARG A HD2    1 
ATOM   1126 H HD3    . ARG A 1 73  ? 24.25500  -8.35300  1.75900  1.000 69.02496  ?  73  ARG A HD3    1 
ATOM   1127 H HE     . ARG A 1 73  ? 25.51500  -6.57600  1.78500  1.000 73.04943  ?  73  ARG A HE     1 
ATOM   1128 H HH11   . ARG A 1 73  ? 22.52800  -5.47800  0.79600  1.000 71.93760  ?  73  ARG A HH11   1 
ATOM   1129 H HH12   . ARG A 1 73  ? 22.90100  -4.03600  0.77800  1.000 71.93760  ?  73  ARG A HH12   1 
ATOM   1130 H HH21   . ARG A 1 73  ? 26.03800  -4.39700  1.74500  1.000 78.54655  ?  73  ARG A HH21   1 
ATOM   1131 H HH22   . ARG A 1 73  ? 25.01800  -3.38500  1.35100  1.000 78.54655  ?  73  ARG A HH22   1 
ATOM   1132 N N      . GLY A 1 74  ? 21.13800  -11.31000 -2.71600 1.000 51.73848  ?  74  GLY A N      1 
ATOM   1133 C CA     . GLY A 1 74  ? 20.78500  -12.68300 -3.02000 1.000 47.86570  ?  74  GLY A CA     1 
ATOM   1134 C C      . GLY A 1 74  ? 19.94100  -13.37400 -1.98400 1.000 51.64731  ?  74  GLY A C      1 
ATOM   1135 O O      . GLY A 1 74  ? 19.77100  -14.60400 -2.05800 1.000 47.93856  ?  74  GLY A O      1 
ATOM   1136 H H      . GLY A 1 74  ? 20.63000  -10.72800 -3.09300 1.000 62.20395  ?  74  GLY A H      1 
ATOM   1137 H HA2    . GLY A 1 74  ? 20.29400  -12.69800 -3.85700 1.000 57.55661  ?  74  GLY A HA2    1 
ATOM   1138 H HA3    . GLY A 1 74  ? 21.60100  -13.19600 -3.12400 1.000 57.55661  ?  74  GLY A HA3    1 
ATOM   1139 N N      . SER A 1 75  ? 19.40100  -12.63000 -1.01700 1.000 48.95398  ?  75  SER A N      1 
ATOM   1140 C CA     . SER A 1 75  ? 18.60100  -13.21900 0.05100  1.000 48.78149  ?  75  SER A CA     1 
ATOM   1141 C C      . SER A 1 75  ? 17.23700  -12.53600 0.14000  1.000 49.93561  ?  75  SER A C      1 
ATOM   1142 O O      . SER A 1 75  ? 16.82300  -11.82500 -0.78200 1.000 45.94109  ?  75  SER A O      1 
ATOM   1143 C CB     . SER A 1 75  ? 19.33400  -13.10300 1.38300  1.000 47.49380  ?  75  SER A CB     1 
ATOM   1144 O OG     . SER A 1 75  ? 18.70900  -13.89400 2.37000  1.000 54.03621  ?  75  SER A OG     1 
ATOM   1145 H H      . SER A 1 75  ? 19.48500  -11.77600 -0.95800 1.000 58.86255  ?  75  SER A H      1 
ATOM   1146 H HA     . SER A 1 75  ? 18.45800  -14.16000 -0.13900 1.000 58.65555  ?  75  SER A HA     1 
ATOM   1147 H HB2    . SER A 1 75  ? 20.24900  -13.40600 1.26800  1.000 57.11033  ?  75  SER A HB2    1 
ATOM   1148 H HB3    . SER A 1 75  ? 19.32500  -12.17600 1.66900  1.000 57.11033  ?  75  SER A HB3    1 
ATOM   1149 H HG     . SER A 1 75  ? 19.09100  -13.78700 3.11000  1.000 64.96122  ?  75  SER A HG     1 
ATOM   1150 N N      . ARG A 1 76  ? 16.51700  -12.77700 1.22700  1.000 50.06288  ?  76  ARG A N      1 
ATOM   1151 C CA     . ARG A 1 76  ? 15.27800  -12.06400 1.47600  1.000 50.28861  ?  76  ARG A CA     1 
ATOM   1152 C C      . ARG A 1 76  ? 14.96100  -12.14600 2.95700  1.000 49.84859  ?  76  ARG A C      1 
ATOM   1153 O O      . ARG A 1 76  ? 15.41800  -13.05500 3.66300  1.000 49.22442  ?  76  ARG A O      1 
ATOM   1154 C CB     . ARG A 1 76  ? 14.11600  -12.63500 0.63900  1.000 57.14128  ?  76  ARG A CB     1 
ATOM   1155 C CG     . ARG A 1 76  ? 13.66500  -14.01600 1.06600  1.000 52.39830  ?  76  ARG A CG     1 
ATOM   1156 C CD     . ARG A 1 76  ? 12.45700  -14.48900 0.25900  1.000 58.08578  ?  76  ARG A CD     1 
ATOM   1157 N NE     . ARG A 1 76  ? 12.45600  -15.93800 0.11100  1.000 58.34026  ?  76  ARG A NE     1 
ATOM   1158 C CZ     . ARG A 1 76  ? 11.57800  -16.76100 0.68000  1.000 56.49757  ?  76  ARG A CZ     1 
ATOM   1159 N NH1    . ARG A 1 76  ? 10.58900  -16.30800 1.43000  1.000 50.62202  ?  76  ARG A NH1    1 
ATOM   1160 N NH2    . ARG A 1 76  ? 11.69800  -18.07000 0.47800  1.000 57.59055  ?  76  ARG A NH2    1 
ATOM   1161 H H      . ARG A 1 76  ? 16.72600  -13.34900 1.83500  1.000 60.19322  ?  76  ARG A H      1 
ATOM   1162 H HA     . ARG A 1 76  ? 15.39100  -11.13000 1.23900  1.000 60.46410  ?  76  ARG A HA     1 
ATOM   1163 H HB2    . ARG A 1 76  ? 13.35500  -12.04000 0.71700  1.000 68.68731  ?  76  ARG A HB2    1 
ATOM   1164 H HB3    . ARG A 1 76  ? 14.39900  -12.69200 -0.28700 1.000 68.68731  ?  76  ARG A HB3    1 
ATOM   1165 H HG2    . ARG A 1 76  ? 14.38900  -14.64700 0.92800  1.000 62.99573  ?  76  ARG A HG2    1 
ATOM   1166 H HG3    . ARG A 1 76  ? 13.41600  -13.99700 2.00400  1.000 62.99573  ?  76  ARG A HG3    1 
ATOM   1167 H HD2    . ARG A 1 76  ? 11.64200  -14.22700 0.71500  1.000 69.82071  ?  76  ARG A HD2    1 
ATOM   1168 H HD3    . ARG A 1 76  ? 12.48500  -14.09100 -0.62500 1.000 69.82071  ?  76  ARG A HD3    1 
ATOM   1169 H HE     . ARG A 1 76  ? 13.06800  -16.28900 -0.38100 1.000 70.12608  ?  76  ARG A HE     1 
ATOM   1170 H HH11   . ARG A 1 76  ? 10.50000  -15.46300 1.56100  1.000 60.86419  ?  76  ARG A HH11   1 
ATOM   1171 H HH12   . ARG A 1 76  ? 10.03400  -16.85900 1.78800  1.000 60.86419  ?  76  ARG A HH12   1 
ATOM   1172 H HH21   . ARG A 1 76  ? 12.33500  -18.37300 -0.01400 1.000 69.22642  ?  76  ARG A HH21   1 
ATOM   1173 H HH22   . ARG A 1 76  ? 11.13800  -18.61400 0.83900  1.000 69.22642  ?  76  ARG A HH22   1 
ATOM   1174 N N      . LEU A 1 77  ? 14.16800  -11.17900 3.41800  1.000 47.30364  ?  77  LEU A N      1 
ATOM   1175 C CA     . LEU A 1 77  ? 13.70300  -11.17500 4.80100  1.000 48.71361  ?  77  LEU A CA     1 
ATOM   1176 C C      . LEU A 1 77  ? 12.44900  -12.03700 4.91500  1.000 44.95473  ?  77  LEU A C      1 
ATOM   1177 O O      . LEU A 1 77  ? 11.56900  -11.98800 4.06000  1.000 40.27611  ?  77  LEU A O      1 
ATOM   1178 C CB     . LEU A 1 77  ? 13.41700  -9.74300  5.26200  1.000 44.46300  ?  77  LEU A CB     1 
ATOM   1179 C CG     . LEU A 1 77  ? 12.83500  -9.56200  6.66800  1.000 45.75563  ?  77  LEU A CG     1 
ATOM   1180 C CD1    . LEU A 1 77  ? 13.87000  -9.85800  7.74100  1.000 46.20700  ?  77  LEU A CD1    1 
ATOM   1181 C CD2    . LEU A 1 77  ? 12.30000  -8.13500  6.82800  1.000 47.48142  ?  77  LEU A CD2    1 
ATOM   1182 H H      . LEU A 1 77  ? 13.88600  -10.51500 2.94900  1.000 56.88214  ?  77  LEU A H      1 
ATOM   1183 H HA     . LEU A 1 77  ? 14.38400  -11.54000 5.38800  1.000 58.57410  ?  77  LEU A HA     1 
ATOM   1184 H HB2    . LEU A 1 77  ? 14.25200  -9.25000  5.23800  1.000 53.47337  ?  77  LEU A HB2    1 
ATOM   1185 H HB3    . LEU A 1 77  ? 12.78300  -9.35200  4.64200  1.000 53.47337  ?  77  LEU A HB3    1 
ATOM   1186 H HG     . LEU A 1 77  ? 12.10700  -10.19100 6.78700  1.000 55.02453  ?  77  LEU A HG     1 
ATOM   1187 H HD11   . LEU A 1 77  ? 13.45400  -9.77400  8.61300  1.000 55.56617  ?  77  LEU A HD11   1 
ATOM   1188 H HD12   . LEU A 1 77  ? 14.20300  -10.76100 7.61900  1.000 55.56617  ?  77  LEU A HD12   1 
ATOM   1189 H HD13   . LEU A 1 77  ? 14.59900  -9.22300  7.66000  1.000 55.56617  ?  77  LEU A HD13   1 
ATOM   1190 H HD21   . LEU A 1 77  ? 11.98200  -8.01700  7.73600  1.000 57.09547  ?  77  LEU A HD21   1 
ATOM   1191 H HD22   . LEU A 1 77  ? 13.01600  -7.50700  6.64400  1.000 57.09547  ?  77  LEU A HD22   1 
ATOM   1192 H HD23   . LEU A 1 77  ? 11.57200  -7.99800  6.20100  1.000 57.09547  ?  77  LEU A HD23   1 
ATOM   1193 N N      . LEU A 1 78  ? 12.38600  -12.83600 5.97900  1.000 43.60559  ?  78  LEU A N      1 
ATOM   1194 C CA     . LEU A 1 78  ? 11.23100  -13.66800 6.27900  1.000 45.09249  ?  78  LEU A CA     1 
ATOM   1195 C C      . LEU A 1 78  ? 10.50900  -13.04600 7.46800  1.000 42.10996  ?  78  LEU A C      1 
ATOM   1196 O O      . LEU A 1 78  ? 11.04500  -13.01300 8.58400  1.000 41.87918  ?  78  LEU A O      1 
ATOM   1197 C CB     . LEU A 1 78  ? 11.64900  -15.10700 6.57700  1.000 43.73874  ?  78  LEU A CB     1 
ATOM   1198 C CG     . LEU A 1 78  ? 12.46300  -15.83700 5.49800  1.000 50.71632  ?  78  LEU A CG     1 
ATOM   1199 C CD1    . LEU A 1 78  ? 12.80100  -17.24300 5.95800  1.000 49.07098  ?  78  LEU A CD1    1 
ATOM   1200 C CD2    . LEU A 1 78  ? 11.71500  -15.87700 4.17600  1.000 46.71720  ?  78  LEU A CD2    1 
ATOM   1201 H H      . LEU A 1 78  ? 13.02000  -12.91300 6.55500  1.000 52.44448  ?  78  LEU A H      1 
ATOM   1202 H HA     . LEU A 1 78  ? 10.63200  -13.68200 5.51700  1.000 54.22876  ?  78  LEU A HA     1 
ATOM   1203 H HB2    . LEU A 1 78  ? 12.18900  -15.10000 7.38200  1.000 52.60426  ?  78  LEU A HB2    1 
ATOM   1204 H HB3    . LEU A 1 78  ? 10.84300  -15.62600 6.72200  1.000 52.60426  ?  78  LEU A HB3    1 
ATOM   1205 H HG     . LEU A 1 78  ? 13.29000  -15.35100 5.35300  1.000 60.97735  ?  78  LEU A HG     1 
ATOM   1206 H HD11   . LEU A 1 78  ? 13.29000  -17.69600 5.25300  1.000 59.00294  ?  78  LEU A HD11   1 
ATOM   1207 H HD12   . LEU A 1 78  ? 13.34500  -17.19100 6.75900  1.000 59.00294  ?  78  LEU A HD12   1 
ATOM   1208 H HD13   . LEU A 1 78  ? 11.97700  -17.71900 6.14800  1.000 59.00294  ?  78  LEU A HD13   1 
ATOM   1209 H HD21   . LEU A 1 78  ? 12.23300  -16.38800 3.53500  1.000 56.17841  ?  78  LEU A HD21   1 
ATOM   1210 H HD22   . LEU A 1 78  ? 10.85200  -16.29800 4.31400  1.000 56.17841  ?  78  LEU A HD22   1 
ATOM   1211 H HD23   . LEU A 1 78  ? 11.59300  -14.97000 3.85400  1.000 56.17841  ?  78  LEU A HD23   1 
ATOM   1212 N N      . VAL A 1 79  ? 9.30800   -12.54100 7.23300  1.000 43.72588  ?  79  VAL A N      1 
ATOM   1213 C CA     . VAL A 1 79  ? 8.46600   -11.99300 8.29800  1.000 45.10232  ?  79  VAL A CA     1 
ATOM   1214 C C      . VAL A 1 79  ? 7.53000   -13.11400 8.73700  1.000 46.77639  ?  79  VAL A C      1 
ATOM   1215 O O      . VAL A 1 79  ? 6.47800   -13.34700 8.12600  1.000 45.16346  ?  79  VAL A O      1 
ATOM   1216 C CB     . VAL A 1 79  ? 7.70300   -10.75300 7.84000  1.000 50.32630  ?  79  VAL A CB     1 
ATOM   1217 C CG1    . VAL A 1 79  ? 6.76800   -10.27400 8.94100  1.000 57.23759  ?  79  VAL A CG1    1 
ATOM   1218 C CG2    . VAL A 1 79  ? 8.68000   -9.64300  7.44600  1.000 51.10268  ?  79  VAL A CG2    1 
ATOM   1219 H H      . VAL A 1 79  ? 8.94900   -12.50100 6.45300  1.000 52.58882  ?  79  VAL A H      1 
ATOM   1220 H HA     . VAL A 1 79  ? 9.02000   -11.74100 9.05300  1.000 54.24055  ?  79  VAL A HA     1 
ATOM   1221 H HB     . VAL A 1 79  ? 7.16900   -10.97700 7.06200  1.000 60.50933  ?  79  VAL A HB     1 
ATOM   1222 H HG11   . VAL A 1 79  ? 6.43200   -9.39400  8.71000  1.000 68.80288  ?  79  VAL A HG11   1 
ATOM   1223 H HG12   . VAL A 1 79  ? 6.03000   -10.89900 9.02300  1.000 68.80288  ?  79  VAL A HG12   1 
ATOM   1224 H HG13   . VAL A 1 79  ? 7.25900   -10.23200 9.77700  1.000 68.80288  ?  79  VAL A HG13   1 
ATOM   1225 H HG21   . VAL A 1 79  ? 8.17500   -8.85300  7.19500  1.000 61.44099  ?  79  VAL A HG21   1 
ATOM   1226 H HG22   . VAL A 1 79  ? 9.25300   -9.44400  8.20200  1.000 61.44099  ?  79  VAL A HG22   1 
ATOM   1227 H HG23   . VAL A 1 79  ? 9.21500   -9.94600  6.69500  1.000 61.44099  ?  79  VAL A HG23   1 
ATOM   1228 N N      . LEU A 1 80  ? 7.92000   -13.81800 9.80100  1.000 42.44891  ?  80  LEU A N      1 
ATOM   1229 C CA     . LEU A 1 80  ? 7.12700   -14.92800 10.31100 1.000 45.93635  ?  80  LEU A CA     1 
ATOM   1230 C C      . LEU A 1 80  ? 6.01300   -14.41400 11.21400 1.000 45.86880  ?  80  LEU A C      1 
ATOM   1231 O O      . LEU A 1 80  ? 6.21100   -13.49000 12.00900 1.000 48.83669  ?  80  LEU A O      1 
ATOM   1232 C CB     . LEU A 1 80  ? 8.02200   -15.90500 11.07600 1.000 45.90348  ?  80  LEU A CB     1 
ATOM   1233 C CG     . LEU A 1 80  ? 9.17600   -16.52000 10.28600 1.000 50.17891  ?  80  LEU A CG     1 
ATOM   1234 C CD1    . LEU A 1 80  ? 10.05400  -17.36700 11.20600 1.000 48.37430  ?  80  LEU A CD1    1 
ATOM   1235 C CD2    . LEU A 1 80  ? 8.66500   -17.37600 9.12700  1.000 54.33251  ?  80  LEU A CD2    1 
ATOM   1236 H H      . LEU A 1 80  ? 8.64100   -13.66900 10.24400 1.000 51.05646  ?  80  LEU A H      1 
ATOM   1237 H HA     . LEU A 1 80  ? 6.71800   -15.40700 9.57300  1.000 55.24139  ?  80  LEU A HA     1 
ATOM   1238 H HB2    . LEU A 1 80  ? 8.40900   -15.43200 11.82900 1.000 55.20195  ?  80  LEU A HB2    1 
ATOM   1239 H HB3    . LEU A 1 80  ? 7.46900   -16.63600 11.39200 1.000 55.20195  ?  80  LEU A HB3    1 
ATOM   1240 H HG     . LEU A 1 80  ? 9.70900   -15.80100 9.91300  1.000 60.33246  ?  80  LEU A HG     1 
ATOM   1241 H HD11   . LEU A 1 80  ? 10.84700  -17.64300 10.72000 1.000 58.16693  ?  80  LEU A HD11   1 
ATOM   1242 H HD12   . LEU A 1 80  ? 10.30700  -16.83600 11.97700 1.000 58.16693  ?  80  LEU A HD12   1 
ATOM   1243 H HD13   . LEU A 1 80  ? 9.55300   -18.14600 11.49200 1.000 58.16693  ?  80  LEU A HD13   1 
ATOM   1244 H HD21   . LEU A 1 80  ? 9.42000   -17.79700 8.68700  1.000 65.31678  ?  80  LEU A HD21   1 
ATOM   1245 H HD22   . LEU A 1 80  ? 8.06500   -18.05400 9.47600  1.000 65.31678  ?  80  LEU A HD22   1 
ATOM   1246 H HD23   . LEU A 1 80  ? 8.19200   -16.80700 8.49900  1.000 65.31678  ?  80  LEU A HD23   1 
ATOM   1247 N N      . ARG A 1 81  ? 4.83700   -15.00600 11.07600 1.000 47.20057  ?  81  ARG A N      1 
ATOM   1248 C CA     . ARG A 1 81  ? 3.67300   -14.64100 11.87700 1.000 50.63943  ?  81  ARG A CA     1 
ATOM   1249 C C      . ARG A 1 81  ? 3.53400   -15.60400 13.04200 1.000 46.90197  ?  81  ARG A C      1 
ATOM   1250 O O      . ARG A 1 81  ? 3.59400   -16.82200 12.85100 1.000 51.70520  ?  81  ARG A O      1 
ATOM   1251 C CB     . ARG A 1 81  ? 2.39800   -14.66200 11.03500 1.000 53.54819  ?  81  ARG A CB     1 
ATOM   1252 C CG     . ARG A 1 81  ? 2.10300   -13.36100 10.33400 1.000 52.95115  ?  81  ARG A CG     1 
ATOM   1253 C CD     . ARG A 1 81  ? 2.90800   -13.21600 9.05900  1.000 57.42178  ?  81  ARG A CD     1 
ATOM   1254 N NE     . ARG A 1 81  ? 2.34400   -12.19100 8.18600  1.000 53.61304  ?  81  ARG A NE     1 
ATOM   1255 C CZ     . ARG A 1 81  ? 3.01700   -11.55600 7.23900  1.000 53.67247  ?  81  ARG A CZ     1 
ATOM   1256 N NH1    . ARG A 1 81  ? 4.29700   -11.81900 7.00100  1.000 47.08231  ?  81  ARG A NH1    1 
ATOM   1257 N NH2    . ARG A 1 81  ? 2.39000   -10.63000 6.50700  1.000 52.61863  ?  81  ARG A NH2    1 
ATOM   1258 H H      . ARG A 1 81  ? 4.68200   -15.63700 10.51300 1.000 56.75845  ?  81  ARG A H      1 
ATOM   1259 H HA     . ARG A 1 81  ? 3.79700   -13.74500 12.22600 1.000 60.88508  ?  81  ARG A HA     1 
ATOM   1260 H HB2    . ARG A 1 81  ? 2.48500   -15.35000 10.35600 1.000 64.37559  ?  81  ARG A HB2    1 
ATOM   1261 H HB3    . ARG A 1 81  ? 1.64600   -14.86200 11.61400 1.000 64.37559  ?  81  ARG A HB3    1 
ATOM   1262 H HG2    . ARG A 1 81  ? 1.16100   -13.32700 10.10300 1.000 63.65915  ?  81  ARG A HG2    1 
ATOM   1263 H HG3    . ARG A 1 81  ? 2.32800   -12.62200 10.92100 1.000 63.65915  ?  81  ARG A HG3    1 
ATOM   1264 H HD2    . ARG A 1 81  ? 3.81800   -12.96200 9.28100  1.000 69.02390  ?  81  ARG A HD2    1 
ATOM   1265 H HD3    . ARG A 1 81  ? 2.90700   -14.06000 8.58100  1.000 69.02390  ?  81  ARG A HD3    1 
ATOM   1266 H HE     . ARG A 1 81  ? 1.51700   -11.98500 8.29400  1.000 64.45342  ?  81  ARG A HE     1 
ATOM   1267 H HH11   . ARG A 1 81  ? 4.70800   -12.41400 7.46800  1.000 56.61655  ?  81  ARG A HH11   1 
ATOM   1268 H HH12   . ARG A 1 81  ? 4.71600   -11.39500 6.38100  1.000 56.61655  ?  81  ARG A HH12   1 
ATOM   1269 H HH21   . ARG A 1 81  ? 1.56100   -10.45400 6.65400  1.000 63.26012  ?  81  ARG A HH21   1 
ATOM   1270 H HH22   . ARG A 1 81  ? 2.81500   -10.21000 5.88900  1.000 63.26012  ?  81  ARG A HH22   1 
ATOM   1271 N N      . GLY A 1 82  ? 3.35200   -15.05800 14.23800 1.000 51.92528  ?  82  GLY A N      1 
ATOM   1272 C CA     . GLY A 1 82  ? 3.10800   -15.83200 15.43200 1.000 52.73975  ?  82  GLY A CA     1 
ATOM   1273 C C      . GLY A 1 82  ? 3.95500   -15.33100 16.57900 1.000 52.18519  ?  82  GLY A C      1 
ATOM   1274 O O      . GLY A 1 82  ? 4.42800   -14.18900 16.57500 1.000 53.88941  ?  82  GLY A O      1 
ATOM   1275 H H      . GLY A 1 82  ? 3.36600   -14.21000 14.38000 1.000 62.42810  ?  82  GLY A H      1 
ATOM   1276 H HA2    . GLY A 1 82  ? 2.17300   -15.76300 15.68100 1.000 63.40547  ?  82  GLY A HA2    1 
ATOM   1277 H HA3    . GLY A 1 82  ? 3.32400   -16.76300 15.26800 1.000 63.40547  ?  82  GLY A HA3    1 
ATOM   1278 N N      . LYS A 1 83  ? 4.13500   -16.19400 17.56500 1.000 52.30624  ?  83  LYS A N      1 
ATOM   1279 C CA     . LYS A 1 83  ? 4.94700   -15.91600 18.73900 1.000 54.29785  ?  83  LYS A CA     1 
ATOM   1280 C C      . LYS A 1 83  ? 6.31400   -16.57800 18.59900 1.000 53.66586  ?  83  LYS A C      1 
ATOM   1281 O O      . LYS A 1 83  ? 6.41500   -17.68500 18.04900 1.000 53.92450  ?  83  LYS A O      1 
ATOM   1282 C CB     . LYS A 1 83  ? 4.26300   -16.43800 20.00700 1.000 60.89498  ?  83  LYS A CB     1 
ATOM   1283 C CG     . LYS A 1 83  ? 2.81200   -16.00800 20.16900 1.000 70.15898  ?  83  LYS A CG     1 
ATOM   1284 C CD     . LYS A 1 83  ? 2.70600   -14.68200 20.91200 1.000 88.98341  ?  83  LYS A CD     1 
ATOM   1285 C CE     . LYS A 1 83  ? 2.68400   -14.88700 22.42300 1.000 94.14697  ?  83  LYS A CE     1 
ATOM   1286 N NZ     . LYS A 1 83  ? 3.64600   -13.96700 23.11800 1.000 100.81227 ?  83  LYS A NZ     1 
ATOM   1287 H H      . LYS A 1 83  ? 3.78400   -16.97900 17.58200 1.000 62.88526  ?  83  LYS A H      1 
ATOM   1288 H HA     . LYS A 1 83  ? 5.07000   -14.95900 18.83500 1.000 65.27519  ?  83  LYS A HA     1 
ATOM   1289 H HB2    . LYS A 1 83  ? 4.28000   -17.40800 19.98900 1.000 73.19174  ?  83  LYS A HB2    1 
ATOM   1290 H HB3    . LYS A 1 83  ? 4.75300   -16.11200 20.77800 1.000 73.19174  ?  83  LYS A HB3    1 
ATOM   1291 H HG2    . LYS A 1 83  ? 2.40900   -15.90000 19.29300 1.000 84.30855  ?  83  LYS A HG2    1 
ATOM   1292 H HG3    . LYS A 1 83  ? 2.33200   -16.68100 20.67500 1.000 84.30855  ?  83  LYS A HG3    1 
ATOM   1293 H HD2    . LYS A 1 83  ? 3.47100   -14.12700 20.69100 1.000 106.89787 ?  83  LYS A HD2    1 
ATOM   1294 H HD3    . LYS A 1 83  ? 1.88600   -14.23300 20.65300 1.000 106.89787 ?  83  LYS A HD3    1 
ATOM   1295 H HE2    . LYS A 1 83  ? 1.79200   -14.70500 22.75800 1.000 113.09413 ?  83  LYS A HE2    1 
ATOM   1296 H HE3    . LYS A 1 83  ? 2.93500   -15.80100 22.62600 1.000 113.09413 ?  83  LYS A HE3    1 
ATOM   1297 H HZ1    . LYS A 1 83  ? 3.60700   -14.09500 23.99800 1.000 121.09249 ?  83  LYS A HZ1    1 
ATOM   1298 H HZ2    . LYS A 1 83  ? 4.47600   -14.12700 22.83900 1.000 121.09249 ?  83  LYS A HZ2    1 
ATOM   1299 H HZ3    . LYS A 1 83  ? 3.43900   -13.12000 22.94000 1.000 121.09249 ?  83  LYS A HZ3    1 
ATOM   1300 N N      . PRO A 1 84  ? 7.39300   -15.94300 19.06200 1.000 50.09826  ?  84  PRO A N      1 
ATOM   1301 C CA     . PRO A 1 84  ? 8.71200   -16.57900 18.90800 1.000 48.65153  ?  84  PRO A CA     1 
ATOM   1302 C C      . PRO A 1 84  ? 8.79300   -17.95200 19.55500 1.000 45.82343  ?  84  PRO A C      1 
ATOM   1303 O O      . PRO A 1 84  ? 9.38400   -18.86900 18.97800 1.000 52.77240  ?  84  PRO A O      1 
ATOM   1304 C CB     . PRO A 1 84  ? 9.66700   -15.57400 19.58000 1.000 47.94759  ?  84  PRO A CB     1 
ATOM   1305 C CG     . PRO A 1 84  ? 8.94900   -14.28000 19.56700 1.000 51.78859  ?  84  PRO A CG     1 
ATOM   1306 C CD     . PRO A 1 84  ? 7.48500   -14.60600 19.67700 1.000 49.52962  ?  84  PRO A CD     1 
ATOM   1307 H HA     . PRO A 1 84  ? 8.93400   -16.65200 17.96700 1.000 58.49960  ?  84  PRO A HA     1 
ATOM   1308 H HB2    . PRO A 1 84  ? 9.85500   -15.85600 20.48800 1.000 57.65488  ?  84  PRO A HB2    1 
ATOM   1309 H HB3    . PRO A 1 84  ? 10.49200  -15.51600 19.07300 1.000 57.65488  ?  84  PRO A HB3    1 
ATOM   1310 H HG2    . PRO A 1 84  ? 9.23700   -13.74200 20.32100 1.000 62.26408  ?  84  PRO A HG2    1 
ATOM   1311 H HG3    . PRO A 1 84  ? 9.13400   -13.81400 18.73700 1.000 62.26408  ?  84  PRO A HG3    1 
ATOM   1312 H HD2    . PRO A 1 84  ? 7.20500   -14.63300 20.60500 1.000 59.55332  ?  84  PRO A HD2    1 
ATOM   1313 H HD3    . PRO A 1 84  ? 6.94900   -13.96200 19.18700 1.000 59.55332  ?  84  PRO A HD3    1 
ATOM   1314 N N      . GLU A 1 85  ? 8.19200   -18.12800 20.73200 1.000 49.54945  ?  85  GLU A N      1 
ATOM   1315 C CA     . GLU A 1 85  ? 8.31000   -19.38000 21.45800 1.000 48.42705  ?  85  GLU A CA     1 
ATOM   1316 C C      . GLU A 1 85  ? 7.62200   -20.53700 20.74400 1.000 55.04878  ?  85  GLU A C      1 
ATOM   1317 O O      . GLU A 1 85  ? 7.97500   -21.69800 20.98600 1.000 52.07486  ?  85  GLU A O      1 
ATOM   1318 C CB     . GLU A 1 85  ? 7.72400   -19.25500 22.87400 1.000 63.20243  ?  85  GLU A CB     1 
ATOM   1319 C CG     . GLU A 1 85  ? 7.85700   -17.87100 23.51700 1.000 74.34438  ?  85  GLU A CG     1 
ATOM   1320 C CD     . GLU A 1 85  ? 6.72100   -16.93800 23.14100 0.000 65.11560  ?  85  GLU A CD     1 
ATOM   1321 O OE1    . GLU A 1 85  ? 5.54700   -17.34600 23.25800 0.940 66.41706  ?  85  GLU A OE1    1 
ATOM   1322 O OE2    . GLU A 1 85  ? 7.01400   -15.80200 22.71500 0.950 63.08892  -1 85  GLU A OE2    1 
ATOM   1323 H H      . GLU A 1 85  ? 7.71100   -17.53500 21.12800 1.000 59.57711  ?  85  GLU A H      1 
ATOM   1324 H HA     . GLU A 1 85  ? 9.25500   -19.58000 21.54000 1.000 58.23023  ?  85  GLU A HA     1 
ATOM   1325 H HB2    . GLU A 1 85  ? 6.77800   -19.46600 22.83400 1.000 75.96069  ?  85  GLU A HB2    1 
ATOM   1326 H HB3    . GLU A 1 85  ? 8.18000   -19.88700 23.45100 1.000 75.96069  ?  85  GLU A HB3    1 
ATOM   1327 H HG2    . GLU A 1 85  ? 7.85800   -17.96900 24.48200 1.000 89.33102  ?  85  GLU A HG2    1 
ATOM   1328 H HG3    . GLU A 1 85  ? 8.68700   -17.46500 23.22400 1.000 89.33102  ?  85  GLU A HG3    1 
ATOM   1329 N N      . GLU A 1 86  ? 6.65300   -20.25100 19.88000 1.000 52.16899  ?  86  GLU A N      1 
ATOM   1330 C CA     A GLU A 1 86  ? 5.97000   -21.28900 19.11400 0.510 58.52382  ?  86  GLU A CA     1 
ATOM   1331 C CA     B GLU A 1 86  ? 5.96100   -21.28100 19.10900 0.490 58.51799  ?  86  GLU A CA     1 
ATOM   1332 C C      . GLU A 1 86  ? 6.56100   -21.48300 17.72200 1.000 56.65153  ?  86  GLU A C      1 
ATOM   1333 O O      . GLU A 1 86  ? 6.66800   -22.62300 17.25800 1.000 53.44464  ?  86  GLU A O      1 
ATOM   1334 C CB     A GLU A 1 86  ? 4.47700   -20.95300 19.00900 0.510 60.16984  ?  86  GLU A CB     1 
ATOM   1335 C CB     B GLU A 1 86  ? 4.47100   -20.93100 18.98000 0.490 60.17813  ?  86  GLU A CB     1 
ATOM   1336 C CG     A GLU A 1 86  ? 3.79200   -20.82500 20.36900 0.510 65.33025  ?  86  GLU A CG     1 
ATOM   1337 C CG     B GLU A 1 86  ? 4.08000   -20.26500 17.66400 0.490 63.23211  ?  86  GLU A CG     1 
ATOM   1338 C CD     A GLU A 1 86  ? 2.45100   -20.10700 20.30400 0.510 68.37346  ?  86  GLU A CD     1 
ATOM   1339 C CD     B GLU A 1 86  ? 2.72300   -19.58700 17.72200 0.490 65.38694  ?  86  GLU A CD     1 
ATOM   1340 O OE1    A GLU A 1 86  ? 2.29900   -19.19200 19.47100 0.510 66.65165  ?  86  GLU A OE1    1 
ATOM   1341 O OE1    B GLU A 1 86  ? 1.89900   -19.96900 18.58500 0.490 68.81166  ?  86  GLU A OE1    1 
ATOM   1342 O OE2    A GLU A 1 86  ? 1.54900   -20.46000 21.09300 0.510 60.25880  -1 86  GLU A OE2    1 
ATOM   1343 O OE2    B GLU A 1 86  ? 2.48000   -18.67500 16.90500 0.490 57.15611  -1 86  GLU A OE2    1 
ATOM   1344 H H      A GLU A 1 86  ? 6.36900   -19.45500 19.71900 0.510 62.72055  ?  86  GLU A H      1 
ATOM   1345 H H      B GLU A 1 86  ? 6.37200   -19.45400 19.72000 0.490 62.72055  ?  86  GLU A H      1 
ATOM   1346 H HA     A GLU A 1 86  ? 6.05000   -22.13700 19.58000 0.510 70.34635  ?  86  GLU A HA     1 
ATOM   1347 H HA     B GLU A 1 86  ? 6.02600   -22.12600 19.58300 0.490 70.33936  ?  86  GLU A HA     1 
ATOM   1348 H HB2    A GLU A 1 86  ? 4.37700   -20.10800 18.54300 0.510 72.32158  ?  86  GLU A HB2    1 
ATOM   1349 H HB2    B GLU A 1 86  ? 3.95500   -21.74800 19.05800 0.490 72.33152  ?  86  GLU A HB2    1 
ATOM   1350 H HB3    A GLU A 1 86  ? 4.03100   -21.65900 18.51500 0.510 72.32158  ?  86  GLU A HB3    1 
ATOM   1351 H HB3    B GLU A 1 86  ? 4.23500   -20.32000 19.69600 0.490 72.33152  ?  86  GLU A HB3    1 
ATOM   1352 H HG2    A GLU A 1 86  ? 3.63600   -21.71300 20.72700 0.510 78.51406  ?  86  GLU A HG2    1 
ATOM   1353 H HG2    B GLU A 1 86  ? 4.74200   -19.59100 17.44300 0.490 75.99630  ?  86  GLU A HG2    1 
ATOM   1354 H HG3    A GLU A 1 86  ? 4.36900   -20.32300 20.96500 0.510 78.51406  ?  86  GLU A HG3    1 
ATOM   1355 H HG3    B GLU A 1 86  ? 4.04800   -20.94000 16.96800 0.490 75.99630  ?  86  GLU A HG3    1 
ATOM   1356 N N      . VAL A 1 87  ? 6.97400   -20.39800 17.06700 1.000 51.78162  ?  87  VAL A N      1 
ATOM   1357 C CA     . VAL A 1 87  ? 7.49500   -20.48800 15.70800 1.000 52.26648  ?  87  VAL A CA     1 
ATOM   1358 C C      . VAL A 1 87  ? 8.86400   -21.15200 15.68700 1.000 46.76473  ?  87  VAL A C      1 
ATOM   1359 O O      . VAL A 1 87  ? 9.14400   -22.00300 14.83300 1.000 44.53593  ?  87  VAL A O      1 
ATOM   1360 C CB     . VAL A 1 87  ? 7.54400   -19.07400 15.07900 1.000 59.41253  ?  87  VAL A CB     1 
ATOM   1361 C CG1    . VAL A 1 87  ? 8.42900   -19.04700 13.83400 1.000 60.65397  ?  87  VAL A CG1    1 
ATOM   1362 C CG2    . VAL A 1 87  ? 6.12500   -18.59600 14.75300 1.000 58.38191  ?  87  VAL A CG2    1 
ATOM   1363 H H      . VAL A 1 87  ? 6.96300   -19.60000 17.38800 1.000 62.25572  ?  87  VAL A H      1 
ATOM   1364 H HA     . VAL A 1 87  ? 6.89700   -21.04500 15.18500 1.000 62.83755  ?  87  VAL A HA     1 
ATOM   1365 H HB     . VAL A 1 87  ? 7.93600   -18.46200 15.72100 1.000 71.41280  ?  87  VAL A HB     1 
ATOM   1366 H HG11   . VAL A 1 87  ? 8.41200   -18.15600 13.45200 1.000 72.90254  ?  87  VAL A HG11   1 
ATOM   1367 H HG12   . VAL A 1 87  ? 9.33600   -19.28100 14.08600 1.000 72.90254  ?  87  VAL A HG12   1 
ATOM   1368 H HG13   . VAL A 1 87  ? 8.08900   -19.68900 13.19000 1.000 72.90254  ?  87  VAL A HG13   1 
ATOM   1369 H HG21   . VAL A 1 87  ? 6.17200   -17.70900 14.36200 1.000 70.17607  ?  87  VAL A HG21   1 
ATOM   1370 H HG22   . VAL A 1 87  ? 5.72000   -19.21400 14.12400 1.000 70.17607  ?  87  VAL A HG22   1 
ATOM   1371 H HG23   . VAL A 1 87  ? 5.60400   -18.56900 15.57100 1.000 70.17607  ?  87  VAL A HG23   1 
ATOM   1372 N N      . PHE A 1 88  ? 9.74900   -20.75100 16.60300 1.000 47.24263  ?  88  PHE A N      1 
ATOM   1373 C CA     . PHE A 1 88  ? 11.15200  -21.14700 16.49800 1.000 42.02328  ?  88  PHE A CA     1 
ATOM   1374 C C      . PHE A 1 88  ? 11.36300  -22.64900 16.62400 1.000 43.61494  ?  88  PHE A C      1 
ATOM   1375 O O      . PHE A 1 88  ? 12.12700  -23.21500 15.81700 1.000 43.14834  ?  88  PHE A O      1 
ATOM   1376 C CB     . PHE A 1 88  ? 11.97800  -20.37700 17.53400 1.000 43.59409  ?  88  PHE A CB     1 
ATOM   1377 C CG     . PHE A 1 88  ? 12.45300  -19.02000 17.04700 1.000 45.64103  ?  88  PHE A CG     1 
ATOM   1378 C CD1    . PHE A 1 88  ? 13.09900  -18.89100 15.82700 1.000 44.68362  ?  88  PHE A CD1    1 
ATOM   1379 C CD2    . PHE A 1 88  ? 12.24000  -17.88100 17.81200 1.000 51.66243  ?  88  PHE A CD2    1 
ATOM   1380 C CE1    . PHE A 1 88  ? 13.52600  -17.64900 15.36900 1.000 52.05004  ?  88  PHE A CE1    1 
ATOM   1381 C CE2    . PHE A 1 88  ? 12.65800  -16.63600 17.36800 1.000 48.40180  ?  88  PHE A CE2    1 
ATOM   1382 C CZ     . PHE A 1 88  ? 13.30700  -16.51700 16.14700 1.000 48.16392  ?  88  PHE A CZ     1 
ATOM   1383 H H      . PHE A 1 88  ? 9.56600   -20.25700 17.28300 1.000 56.80893  ?  88  PHE A H      1 
ATOM   1384 H HA     . PHE A 1 88  ? 11.45800  -20.89300 15.61300 1.000 50.54570  ?  88  PHE A HA     1 
ATOM   1385 H HB2    . PHE A 1 88  ? 11.43300  -20.23500 18.32400 1.000 52.43068  ?  88  PHE A HB2    1 
ATOM   1386 H HB3    . PHE A 1 88  ? 12.76100  -20.90200 17.76200 1.000 52.43068  ?  88  PHE A HB3    1 
ATOM   1387 H HD1    . PHE A 1 88  ? 13.24800  -19.64700 15.30700 1.000 53.73812  ?  88  PHE A HD1    1 
ATOM   1388 H HD2    . PHE A 1 88  ? 11.81100  -17.95500 18.63400 1.000 62.11269  ?  88  PHE A HD2    1 
ATOM   1389 H HE1    . PHE A 1 88  ? 13.95700  -17.57700 14.54800 1.000 62.57782  ?  88  PHE A HE1    1 
ATOM   1390 H HE2    . PHE A 1 88  ? 12.50300  -15.88100 17.88900 1.000 58.19993  ?  88  PHE A HE2    1 
ATOM   1391 H HZ     . PHE A 1 88  ? 13.59400  -15.68300 15.85000 1.000 57.91447  ?  88  PHE A HZ     1 
ATOM   1392 N N      . PRO A 1 89  ? 10.75600  -23.35500 17.58200 1.000 44.48167  ?  89  PRO A N      1 
ATOM   1393 C CA     . PRO A 1 89  ? 10.95300  -24.82100 17.62600 1.000 46.04373  ?  89  PRO A CA     1 
ATOM   1394 C C      . PRO A 1 89  ? 10.60700  -25.50000 16.31700 1.000 46.47041  ?  89  PRO A C      1 
ATOM   1395 O O      . PRO A 1 89  ? 11.29400  -26.45100 15.90200 1.000 46.26424  ?  89  PRO A O      1 
ATOM   1396 C CB     . PRO A 1 89  ? 10.02000  -25.27400 18.76400 1.000 48.05049  ?  89  PRO A CB     1 
ATOM   1397 C CG     . PRO A 1 89  ? 9.83700   -24.06400 19.62100 1.000 48.84540  ?  89  PRO A CG     1 
ATOM   1398 C CD     . PRO A 1 89  ? 9.90900   -22.87000 18.68600 1.000 47.55519  ?  89  PRO A CD     1 
ATOM   1399 H HA     . PRO A 1 89  ? 11.87000  -25.02300 17.87100 1.000 55.37024  ?  89  PRO A HA     1 
ATOM   1400 H HB2    . PRO A 1 89  ? 9.17300   -25.57000 18.39600 1.000 57.77836  ?  89  PRO A HB2    1 
ATOM   1401 H HB3    . PRO A 1 89  ? 10.43500  -25.99400 19.26400 1.000 57.77836  ?  89  PRO A HB3    1 
ATOM   1402 H HG2    . PRO A 1 89  ? 8.97300   -24.10300 20.06000 1.000 58.73225  ?  89  PRO A HG2    1 
ATOM   1403 H HG3    . PRO A 1 89  ? 10.54500  -24.02400 20.28300 1.000 58.73225  ?  89  PRO A HG3    1 
ATOM   1404 H HD2    . PRO A 1 89  ? 9.02600   -22.63000 18.36400 1.000 57.18400  ?  89  PRO A HD2    1 
ATOM   1405 H HD3    . PRO A 1 89  ? 10.32000  -22.11000 19.12800 1.000 57.18400  ?  89  PRO A HD3    1 
ATOM   1406 N N      . ARG A 1 90  ? 9.56400   -25.02700 15.63300 1.000 46.36098  ?  90  ARG A N      1 
ATOM   1407 C CA     A ARG A 1 90  ? 9.19700   -25.61200 14.34700 0.470 50.27043  ?  90  ARG A CA     1 
ATOM   1408 C CA     B ARG A 1 90  ? 9.19600   -25.60900 14.34700 0.530 50.20126  ?  90  ARG A CA     1 
ATOM   1409 C C      . ARG A 1 90  ? 10.28400  -25.37400 13.30100 1.000 49.76140  ?  90  ARG A C      1 
ATOM   1410 O O      . ARG A 1 90  ? 10.72300  -26.31300 12.62700 1.000 47.08682  ?  90  ARG A O      1 
ATOM   1411 C CB     A ARG A 1 90  ? 7.85700   -25.03800 13.88000 0.470 55.93595  ?  90  ARG A CB     1 
ATOM   1412 C CB     B ARG A 1 90  ? 7.86200   -25.02600 13.87500 0.530 56.04167  ?  90  ARG A CB     1 
ATOM   1413 C CG     A ARG A 1 90  ? 7.74700   -24.83800 12.37300 0.470 61.12384  ?  90  ARG A CG     1 
ATOM   1414 C CG     B ARG A 1 90  ? 7.37800   -25.56800 12.53400 0.530 60.82049  ?  90  ARG A CG     1 
ATOM   1415 C CD     A ARG A 1 90  ? 6.28900   -24.66100 11.93200 0.470 65.22967  ?  90  ARG A CD     1 
ATOM   1416 C CD     B ARG A 1 90  ? 7.08300   -24.44200 11.54100 0.530 64.25727  ?  90  ARG A CD     1 
ATOM   1417 N NE     A ARG A 1 90  ? 5.60900   -23.59500 12.66000 0.470 66.73365  ?  90  ARG A NE     1 
ATOM   1418 N NE     B ARG A 1 90  ? 6.06400   -23.52200 12.03900 0.530 64.44219  ?  90  ARG A NE     1 
ATOM   1419 C CZ     A ARG A 1 90  ? 4.87700   -23.77200 13.75300 0.470 64.79725  ?  90  ARG A CZ     1 
ATOM   1420 C CZ     B ARG A 1 90  ? 5.83000   -22.31700 11.54300 0.530 62.33511  ?  90  ARG A CZ     1 
ATOM   1421 N NH1    A ARG A 1 90  ? 4.70700   -24.96600 14.28700 0.470 64.66460  ?  90  ARG A NH1    1 
ATOM   1422 N NH1    B ARG A 1 90  ? 6.51100   -21.85200 10.51000 0.530 62.61416  ?  90  ARG A NH1    1 
ATOM   1423 N NH2    A ARG A 1 90  ? 4.30600   -22.71500 14.32600 0.470 66.79470  ?  90  ARG A NH2    1 
ATOM   1424 N NH2    B ARG A 1 90  ? 4.89200   -21.55800 12.10200 0.530 55.41518  ?  90  ARG A NH2    1 
ATOM   1425 H H      A ARG A 1 90  ? 9.06000   -24.37900 15.88900 0.470 55.75094  ?  90  ARG A H      1 
ATOM   1426 H H      B ARG A 1 90  ? 9.06000   -24.37900 15.89000 0.530 55.75094  ?  90  ARG A H      1 
ATOM   1427 H HA     A ARG A 1 90  ? 9.09500   -26.57000 14.45600 0.470 60.44229  ?  90  ARG A HA     1 
ATOM   1428 H HA     B ARG A 1 90  ? 9.08900   -26.56700 14.45700 0.530 60.35928  ?  90  ARG A HA     1 
ATOM   1429 H HB2    A ARG A 1 90  ? 7.15100   -25.64700 14.14600 0.470 67.24091  ?  90  ARG A HB2    1 
ATOM   1430 H HB2    B ARG A 1 90  ? 7.18300   -25.23200 14.53600 0.530 67.36778  ?  90  ARG A HB2    1 
ATOM   1431 H HB3    A ARG A 1 90  ? 7.72700   -24.17400 14.30000 0.470 67.24091  ?  90  ARG A HB3    1 
ATOM   1432 H HB3    B ARG A 1 90  ? 7.95800   -24.06500 13.78500 0.530 67.36778  ?  90  ARG A HB3    1 
ATOM   1433 H HG2    A ARG A 1 90  ? 8.24100   -24.04200 12.11800 0.470 73.46638  ?  90  ARG A HG2    1 
ATOM   1434 H HG2    B ARG A 1 90  ? 8.06500   -26.13700 12.15200 0.530 73.10235  ?  90  ARG A HG2    1 
ATOM   1435 H HG3    A ARG A 1 90  ? 8.11100   -25.61400 11.91900 0.470 73.46638  ?  90  ARG A HG3    1 
ATOM   1436 H HG3    B ARG A 1 90  ? 6.56300   -26.07600 12.66800 0.530 73.10235  ?  90  ARG A HG3    1 
ATOM   1437 H HD2    A ARG A 1 90  ? 6.26700   -24.44100 10.98800 0.470 78.39337  ?  90  ARG A HD2    1 
ATOM   1438 H HD2    B ARG A 1 90  ? 7.89500   -23.93600 11.38200 0.530 77.22650  ?  90  ARG A HD2    1 
ATOM   1439 H HD3    A ARG A 1 90  ? 5.80700   -25.48800 12.09100 0.470 78.39337  ?  90  ARG A HD3    1 
ATOM   1440 H HD3    B ARG A 1 90  ? 6.76300   -24.82600 10.70900 0.530 77.22650  ?  90  ARG A HD3    1 
ATOM   1441 H HE     A ARG A 1 90  ? 5.68800   -22.79400 12.35900 0.470 80.19815  ?  90  ARG A HE     1 
ATOM   1442 H HE     B ARG A 1 90  ? 5.58100   -23.78200 12.70200 0.530 77.44840  ?  90  ARG A HE     1 
ATOM   1443 H HH11   A ARG A 1 90  ? 5.07600   -25.65500 13.92700 0.470 77.71529  ?  90  ARG A HH11   1 
ATOM   1444 H HH11   B ARG A 1 90  ? 7.12200   -22.33600 10.14500 0.530 75.25476  ?  90  ARG A HH11   1 
ATOM   1445 H HH12   A ARG A 1 90  ? 4.22900   -25.05600 14.99600 0.470 77.71529  ?  90  ARG A HH12   1 
ATOM   1446 H HH12   B ARG A 1 90  ? 6.34400   -21.06700 10.20200 0.530 75.25476  ?  90  ARG A HH12   1 
ATOM   1447 H HH21   A ARG A 1 90  ? 4.41400   -21.93200 13.98700 0.470 80.27141  ?  90  ARG A HH21   1 
ATOM   1448 H HH21   B ARG A 1 90  ? 4.44700   -21.85200 12.77600 0.530 66.61599  ?  90  ARG A HH21   1 
ATOM   1449 H HH22   A ARG A 1 90  ? 3.83000   -22.81500 15.03400 0.470 80.27141  ?  90  ARG A HH22   1 
ATOM   1450 H HH22   B ARG A 1 90  ? 4.73100   -20.77400 11.78800 0.530 66.61599  ?  90  ARG A HH22   1 
ATOM   1451 N N      . VAL A 1 91  ? 10.73500  -24.12200 13.15500 1.000 43.21798  ?  91  VAL A N      1 
ATOM   1452 C CA     . VAL A 1 91  ? 11.67100  -23.82900 12.08200 1.000 47.17752  ?  91  VAL A CA     1 
ATOM   1453 C C      . VAL A 1 91  ? 13.08000  -24.34300 12.40000 1.000 42.53196  ?  91  VAL A C      1 
ATOM   1454 O O      . VAL A 1 91  ? 13.85300  -24.62500 11.48100 1.000 44.90959  ?  91  VAL A O      1 
ATOM   1455 C CB     . VAL A 1 91  ? 11.68500  -22.31700 11.76000 1.000 46.49795  ?  91  VAL A CB     1 
ATOM   1456 C CG1    . VAL A 1 91  ? 10.33700  -21.89300 11.16600 1.000 48.77606  ?  91  VAL A CG1    1 
ATOM   1457 C CG2    . VAL A 1 91  ? 12.01200  -21.49200 12.98900 1.000 43.91778  ?  91  VAL A CG2    1 
ATOM   1458 H H      . VAL A 1 91  ? 10.51900  -23.45200 13.64900 1.000 51.97935  ?  91  VAL A H      1 
ATOM   1459 H HA     . VAL A 1 91  ? 11.36300  -24.29800 11.29200 1.000 56.73079  ?  91  VAL A HA     1 
ATOM   1460 H HB     . VAL A 1 91  ? 12.38000  -22.14700 11.10600 1.000 55.91531  ?  91  VAL A HB     1 
ATOM   1461 H HG11   . VAL A 1 91  ? 10.39100  -20.96400 10.89200 1.000 58.64904  ?  91  VAL A HG11   1 
ATOM   1462 H HG12   . VAL A 1 91  ? 10.14000  -22.45300 10.39900 1.000 58.64904  ?  91  VAL A HG12   1 
ATOM   1463 H HG13   . VAL A 1 91  ? 9.64700   -22.00000 11.83900 1.000 58.64904  ?  91  VAL A HG13   1 
ATOM   1464 H HG21   . VAL A 1 91  ? 12.13200  -20.56700 12.72600 1.000 52.81910  ?  91  VAL A HG21   1 
ATOM   1465 H HG22   . VAL A 1 91  ? 11.28000  -21.56400 13.62200 1.000 52.81910  ?  91  VAL A HG22   1 
ATOM   1466 H HG23   . VAL A 1 91  ? 12.82800  -21.83100 13.38900 1.000 52.81910  ?  91  VAL A HG23   1 
ATOM   1467 N N      . PHE A 1 92  ? 13.44100  -24.46100 13.68200 1.000 44.00192  ?  92  PHE A N      1 
ATOM   1468 C CA     . PHE A 1 92  ? 14.72400  -25.08700 14.02200 1.000 43.90547  ?  92  PHE A CA     1 
ATOM   1469 C C      . PHE A 1 92  ? 14.83800  -26.45200 13.34300 1.000 46.05266  ?  92  PHE A C      1 
ATOM   1470 O O      . PHE A 1 92  ? 15.84500  -26.76000 12.68100 1.000 43.65674  ?  92  PHE A O      1 
ATOM   1471 C CB     . PHE A 1 92  ? 14.87500  -25.25800 15.53500 1.000 42.64166  ?  92  PHE A CB     1 
ATOM   1472 C CG     . PHE A 1 92  ? 15.13900  -23.97600 16.28500 1.000 46.44507  ?  92  PHE A CG     1 
ATOM   1473 C CD1    . PHE A 1 92  ? 15.60700  -22.83900 15.64100 1.000 42.28922  ?  92  PHE A CD1    1 
ATOM   1474 C CD2    . PHE A 1 92  ? 14.91700  -23.91900 17.65800 1.000 46.34469  ?  92  PHE A CD2    1 
ATOM   1475 C CE1    . PHE A 1 92  ? 15.84400  -21.66300 16.34700 1.000 43.63743  ?  92  PHE A CE1    1 
ATOM   1476 C CE2    . PHE A 1 92  ? 15.15300  -22.74900 18.36900 1.000 44.99078  ?  92  PHE A CE2    1 
ATOM   1477 C CZ     . PHE A 1 92  ? 15.62500  -21.61800 17.71000 1.000 44.66663  ?  92  PHE A CZ     1 
ATOM   1478 H H      . PHE A 1 92  ? 12.97600  -24.19600 14.35500 1.000 52.92007  ?  92  PHE A H      1 
ATOM   1479 H HA     . PHE A 1 92  ? 15.43700  -24.50300 13.71800 1.000 52.80433  ?  92  PHE A HA     1 
ATOM   1480 H HB2    . PHE A 1 92  ? 14.05500  -25.64000 15.88600 1.000 51.28776  ?  92  PHE A HB2    1 
ATOM   1481 H HB3    . PHE A 1 92  ? 15.61900  -25.85600 15.70600 1.000 51.28776  ?  92  PHE A HB3    1 
ATOM   1482 H HD1    . PHE A 1 92  ? 15.76500  -22.86400 14.72500 1.000 50.86484  ?  92  PHE A HD1    1 
ATOM   1483 H HD2    . PHE A 1 92  ? 14.60800  -24.67300 18.10500 1.000 55.73140  ?  92  PHE A HD2    1 
ATOM   1484 H HE1    . PHE A 1 92  ? 16.15100  -20.90700 15.90100 1.000 52.48269  ?  92  PHE A HE1    1 
ATOM   1485 H HE2    . PHE A 1 92  ? 14.99600  -22.72100 19.28500 1.000 54.10670  ?  92  PHE A HE2    1 
ATOM   1486 H HZ     . PHE A 1 92  ? 15.79100  -20.83600 18.18500 1.000 53.71772  ?  92  PHE A HZ     1 
ATOM   1487 N N      . ARG A 1 93  ? 13.80800  -27.28600 13.50300 1.000 46.99190  ?  93  ARG A N      1 
ATOM   1488 C CA     . ARG A 1 93  ? 13.84700  -28.63900 12.94000 1.000 51.07135  ?  93  ARG A CA     1 
ATOM   1489 C C      . ARG A 1 93  ? 13.60900  -28.62800 11.43700 1.000 49.16539  ?  93  ARG A C      1 
ATOM   1490 O O      . ARG A 1 93  ? 14.25000  -29.37600 10.70600 1.000 47.20386  ?  93  ARG A O      1 
ATOM   1491 C CB     . ARG A 1 93  ? 12.81400  -29.52300 13.63200 1.000 47.92029  ?  93  ARG A CB     1 
ATOM   1492 C CG     . ARG A 1 93  ? 13.30300  -30.12400 14.94400 1.000 58.30022  ?  93  ARG A CG     1 
ATOM   1493 C CD     . ARG A 1 93  ? 12.54400  -29.55000 16.10900 1.000 67.80846  ?  93  ARG A CD     1 
ATOM   1494 N NE     . ARG A 1 93  ? 13.11900  -29.93800 17.39500 1.000 63.77936  ?  93  ARG A NE     1 
ATOM   1495 C CZ     . ARG A 1 93  ? 13.11600  -29.16600 18.47800 1.000 68.76433  ?  93  ARG A CZ     1 
ATOM   1496 N NH1    . ARG A 1 93  ? 12.60300  -27.93500 18.45300 1.000 57.93128  ?  93  ARG A NH1    1 
ATOM   1497 N NH2    . ARG A 1 93  ? 13.63500  -29.64200 19.61200 1.000 63.61119  ?  93  ARG A NH2    1 
ATOM   1498 H H      . ARG A 1 93  ? 13.08300  -27.09700 13.92600 1.000 56.50805  ?  93  ARG A H      1 
ATOM   1499 H HA     . ARG A 1 93  ? 14.72500  -29.01800 13.10300 1.000 61.40339  ?  93  ARG A HA     1 
ATOM   1500 H HB2    . ARG A 1 93  ? 12.02700  -28.99100 13.82600 1.000 57.62212  ?  93  ARG A HB2    1 
ATOM   1501 H HB3    . ARG A 1 93  ? 12.58200  -30.25500 13.03900 1.000 57.62212  ?  93  ARG A HB3    1 
ATOM   1502 H HG2    . ARG A 1 93  ? 13.16800  -31.08500 14.93000 1.000 70.07803  ?  93  ARG A HG2    1 
ATOM   1503 H HG3    . ARG A 1 93  ? 14.24500  -29.92400 15.06000 1.000 70.07803  ?  93  ARG A HG3    1 
ATOM   1504 H HD2    . ARG A 1 93  ? 12.56000  -28.58200 16.05200 1.000 81.48792  ?  93  ARG A HD2    1 
ATOM   1505 H HD3    . ARG A 1 93  ? 11.62900  -29.87000 16.08000 1.000 81.48792  ?  93  ARG A HD3    1 
ATOM   1506 H HE     . ARG A 1 93  ? 13.48200  -30.71500 17.45500 1.000 76.65301  ?  93  ARG A HE     1 
ATOM   1507 H HH11   . ARG A 1 93  ? 12.26500  -27.62500 17.72600 1.000 69.63530  ?  93  ARG A HH11   1 
ATOM   1508 H HH12   . ARG A 1 93  ? 12.61100  -27.45200 19.16400 1.000 69.63530  ?  93  ARG A HH12   1 
ATOM   1509 H HH21   . ARG A 1 93  ? 13.96400  -30.43600 19.63400 1.000 76.45120  ?  93  ARG A HH21   1 
ATOM   1510 H HH22   . ARG A 1 93  ? 13.64000  -29.15500 20.32000 1.000 76.45120  ?  93  ARG A HH22   1 
ATOM   1511 N N      . GLU A 1 94  ? 12.69800  -27.76900 10.95900 1.000 47.26759  ?  94  GLU A N      1 
ATOM   1512 C CA     . GLU A 1 94  ? 12.41100  -27.73200 9.53200  1.000 50.22769  ?  94  GLU A CA     1 
ATOM   1513 C C      . GLU A 1 94  ? 13.63300  -27.32300 8.73000  1.000 48.33958  ?  94  GLU A C      1 
ATOM   1514 O O      . GLU A 1 94  ? 13.92600  -27.92200 7.68800  1.000 42.26550  ?  94  GLU A O      1 
ATOM   1515 C CB     . GLU A 1 94  ? 11.24900  -26.77300 9.26000  1.000 54.07931  ?  94  GLU A CB     1 
ATOM   1516 C CG     . GLU A 1 94  ? 10.81900  -26.71300 7.80200  1.000 48.79612  ?  94  GLU A CG     1 
ATOM   1517 C CD     . GLU A 1 94  ? 9.72400   -25.69500 7.56300  1.000 45.63593  ?  94  GLU A CD     1 
ATOM   1518 O OE1    . GLU A 1 94  ? 8.73100   -25.71200 8.31100  1.000 49.97538  ?  94  GLU A OE1    1 
ATOM   1519 O OE2    . GLU A 1 94  ? 9.86000   -24.87500 6.62900  1.000 50.23152  -1 94  GLU A OE2    1 
ATOM   1520 H H      . GLU A 1 94  ? 12.24600  -27.21200 11.43400 1.000 56.83887  ?  94  GLU A H      1 
ATOM   1521 H HA     . GLU A 1 94  ? 12.14900  -28.62000 9.24500  1.000 60.39099  ?  94  GLU A HA     1 
ATOM   1522 H HB2    . GLU A 1 94  ? 10.48300  -27.05900 9.78100  1.000 65.01294  ?  94  GLU A HB2    1 
ATOM   1523 H HB3    . GLU A 1 94  ? 11.51600  -25.87900 9.52500  1.000 65.01294  ?  94  GLU A HB3    1 
ATOM   1524 H HG2    . GLU A 1 94  ? 11.58300  -26.46800 7.25600  1.000 58.67311  ?  94  GLU A HG2    1 
ATOM   1525 H HG3    . GLU A 1 94  ? 10.48500  -27.58300 7.53400  1.000 58.67311  ?  94  GLU A HG3    1 
ATOM   1526 N N      . TRP A 1 95  ? 14.35500  -26.28800 9.19000  1.000 46.55863  ?  95  TRP A N      1 
ATOM   1527 C CA     . TRP A 1 95  ? 15.49400  -25.75500 8.46000  1.000 45.41473  ?  95  TRP A CA     1 
ATOM   1528 C C      . TRP A 1 95  ? 16.82500  -26.38400 8.87500  1.000 43.34222  ?  95  TRP A C      1 
ATOM   1529 O O      . TRP A 1 95  ? 17.86500  -26.02500 8.30400  1.000 49.36576  ?  95  TRP A O      1 
ATOM   1530 C CB     . TRP A 1 95  ? 15.56600  -24.22600 8.64000  1.000 44.87349  ?  95  TRP A CB     1 
ATOM   1531 C CG     . TRP A 1 95  ? 14.32500  -23.50200 8.19400  1.000 45.14406  ?  95  TRP A CG     1 
ATOM   1532 C CD1    . TRP A 1 95  ? 13.35400  -23.97500 7.34200  1.000 47.10499  ?  95  TRP A CD1    1 
ATOM   1533 C CD2    . TRP A 1 95  ? 13.90900  -22.18300 8.57300  1.000 42.06974  ?  95  TRP A CD2    1 
ATOM   1534 N NE1    . TRP A 1 95  ? 12.37200  -23.03000 7.17100  1.000 42.86059  ?  95  TRP A NE1    1 
ATOM   1535 C CE2    . TRP A 1 95  ? 12.68500  -21.92200 7.91900  1.000 42.95701  ?  95  TRP A CE2    1 
ATOM   1536 C CE3    . TRP A 1 95  ? 14.45500  -21.19300 9.40200  1.000 44.57957  ?  95  TRP A CE3    1 
ATOM   1537 C CZ2    . TRP A 1 95  ? 11.99700  -20.71400 8.06800  1.000 42.95477  ?  95  TRP A CZ2    1 
ATOM   1538 C CZ3    . TRP A 1 95  ? 13.77100  -19.99400 9.55100  1.000 42.76263  ?  95  TRP A CZ3    1 
ATOM   1539 C CH2    . TRP A 1 95  ? 12.54800  -19.76600 8.88800  1.000 44.42831  ?  95  TRP A CH2    1 
ATOM   1540 H H      . TRP A 1 95  ? 14.19600  -25.88000 9.93000  1.000 55.98812  ?  95  TRP A H      1 
ATOM   1541 H HA     . TRP A 1 95  ? 15.36700  -25.94100 7.51600  1.000 54.61544  ?  95  TRP A HA     1 
ATOM   1542 H HB2    . TRP A 1 95  ? 15.70100  -24.03000 9.58100  1.000 53.96596  ?  95  TRP A HB2    1 
ATOM   1543 H HB3    . TRP A 1 95  ? 16.31000  -23.88600 8.12000  1.000 53.96596  ?  95  TRP A HB3    1 
ATOM   1544 H HD1    . TRP A 1 95  ? 13.36200  -24.81400 6.94000  1.000 56.64376  ?  95  TRP A HD1    1 
ATOM   1545 H HE1    . TRP A 1 95  ? 11.67500  -23.11800 6.67600  1.000 51.55047  ?  95  TRP A HE1    1 
ATOM   1546 H HE3    . TRP A 1 95  ? 15.26000  -21.33700 9.84400  1.000 53.61325  ?  95  TRP A HE3    1 
ATOM   1547 H HZ2    . TRP A 1 95  ? 11.19400  -20.56000 7.62500  1.000 51.66350  ?  95  TRP A HZ2    1 
ATOM   1548 H HZ3    . TRP A 1 95  ? 14.12500  -19.33000 10.09800 1.000 51.43292  ?  95  TRP A HZ3    1 
ATOM   1549 H HH2    . TRP A 1 95  ? 12.10700  -18.95600 9.01000  1.000 53.43174  ?  95  TRP A HH2    1 
ATOM   1550 N N      . GLY A 1 96  ? 16.82600  -27.31400 9.82200  1.000 42.46205  ?  96  GLY A N      1 
ATOM   1551 C CA     . GLY A 1 96  ? 18.06600  -27.92100 10.26300 1.000 43.71092  ?  96  GLY A CA     1 
ATOM   1552 C C      . GLY A 1 96  ? 19.03700  -26.88400 10.81500 1.000 45.51600  ?  96  GLY A C      1 
ATOM   1553 O O      . GLY A 1 96  ? 20.21800  -26.87800 10.46200 1.000 45.58130  ?  96  GLY A O      1 
ATOM   1554 H H      . GLY A 1 96  ? 16.12400  -27.60800 10.22100 1.000 51.07223  ?  96  GLY A H      1 
ATOM   1555 H HA2    . GLY A 1 96  ? 17.87900  -28.57000 10.95800 1.000 52.57087  ?  96  GLY A HA2    1 
ATOM   1556 H HA3    . GLY A 1 96  ? 18.48900  -28.37200 9.51500  1.000 52.57087  ?  96  GLY A HA3    1 
ATOM   1557 N N      . VAL A 1 97  ? 18.53000  -26.00300 11.68900 1.000 44.52994  ?  97  VAL A N      1 
ATOM   1558 C CA     . VAL A 1 97  ? 19.30800  -24.87900 12.17400 1.000 42.55793  ?  97  VAL A CA     1 
ATOM   1559 C C      . VAL A 1 97  ? 20.34900  -25.34500 13.17900 1.000 45.76363  ?  97  VAL A C      1 
ATOM   1560 O O      . VAL A 1 97  ? 20.09400  -26.22000 14.01000 1.000 46.04732  ?  97  VAL A O      1 
ATOM   1561 C CB     . VAL A 1 97  ? 18.38000  -23.82300 12.80400 1.000 45.51646  ?  97  VAL A CB     1 
ATOM   1562 C CG1    . VAL A 1 97  ? 19.18500  -22.64900 13.31900 1.000 41.79437  ?  97  VAL A CG1    1 
ATOM   1563 C CG2    . VAL A 1 97  ? 17.33400  -23.36200 11.79400 1.000 45.02918  ?  97  VAL A CG2    1 
ATOM   1564 H H      . VAL A 1 97  ? 17.73400  -26.04200 12.01100 1.000 53.55369  ?  97  VAL A H      1 
ATOM   1565 H HA     . VAL A 1 97  ? 19.77400  -24.48200 11.42200 1.000 51.18729  ?  97  VAL A HA     1 
ATOM   1566 H HB     . VAL A 1 97  ? 17.91500  -24.22000 13.55700 1.000 54.73753  ?  97  VAL A HB     1 
ATOM   1567 H HG11   . VAL A 1 97  ? 18.57700  -21.94300 13.58900 1.000 50.27101  ?  97  VAL A HG11   1 
ATOM   1568 H HG12   . VAL A 1 97  ? 19.71300  -22.93900 14.08000 1.000 50.27101  ?  97  VAL A HG12   1 
ATOM   1569 H HG13   . VAL A 1 97  ? 19.76800  -22.33200 12.61300 1.000 50.27101  ?  97  VAL A HG13   1 
ATOM   1570 H HG21   . VAL A 1 97  ? 16.80600  -22.65100 12.18800 1.000 54.15279  ?  97  VAL A HG21   1 
ATOM   1571 H HG22   . VAL A 1 97  ? 17.78500  -23.03800 10.99900 1.000 54.15279  ?  97  VAL A HG22   1 
ATOM   1572 H HG23   . VAL A 1 97  ? 16.76300  -24.11200 11.56700 1.000 54.15279  ?  97  VAL A HG23   1 
ATOM   1573 N N      . THR A 1 98  ? 21.54200  -24.75300 13.10000 1.000 47.44686  ?  98  THR A N      1 
ATOM   1574 C CA     . THR A 1 98  ? 22.61400  -25.00400 14.05100 1.000 44.95419  ?  98  THR A CA     1 
ATOM   1575 C C      . THR A 1 98  ? 23.00800  -23.77800 14.86700 1.000 47.59967  ?  98  THR A C      1 
ATOM   1576 O O      . THR A 1 98  ? 23.67600  -23.93400 15.89000 1.000 47.91857  ?  98  THR A O      1 
ATOM   1577 C CB     . THR A 1 98  ? 23.86600  -25.51500 13.32500 1.000 47.06545  ?  98  THR A CB     1 
ATOM   1578 O OG1    . THR A 1 98  ? 24.24400  -24.57300 12.31700 1.000 50.74433  ?  98  THR A OG1    1 
ATOM   1579 C CG2    . THR A 1 98  ? 23.60500  -26.87100 12.68200 1.000 54.39548  ?  98  THR A CG2    1 
ATOM   1580 H H      . THR A 1 98  ? 21.75500  -24.18800 12.48700 1.000 57.05401  ?  98  THR A H      1 
ATOM   1581 H HA     . THR A 1 98  ? 22.32300  -25.69500 14.66600 1.000 54.06280  ?  98  THR A HA     1 
ATOM   1582 H HB     . THR A 1 98  ? 24.58900  -25.62100 13.96300 1.000 56.59631  ?  98  THR A HB     1 
ATOM   1583 H HG1    . THR A 1 98  ? 25.03300  -24.71700 12.07000 1.000 61.01096  ?  98  THR A HG1    1 
ATOM   1584 H HG21   . THR A 1 98  ? 24.39600  -27.17000 12.20600 1.000 65.39235  ?  98  THR A HG21   1 
ATOM   1585 H HG22   . THR A 1 98  ? 23.38200  -27.52400 13.36300 1.000 65.39235  ?  98  THR A HG22   1 
ATOM   1586 H HG23   . THR A 1 98  ? 22.86800  -26.80500 12.05500 1.000 65.39235  ?  98  THR A HG23   1 
ATOM   1587 N N      . GLN A 1 99  ? 22.61700  -22.57600 14.45400 1.000 44.62405  ?  99  GLN A N      1 
ATOM   1588 C CA     . GLN A 1 99  ? 22.99500  -21.36000 15.16600 1.000 45.97298  ?  99  GLN A CA     1 
ATOM   1589 C C      . GLN A 1 99  ? 21.88600  -20.32600 15.04900 1.000 47.00482  ?  99  GLN A C      1 
ATOM   1590 O O      . GLN A 1 99  ? 21.29700  -20.14300 13.97300 1.000 44.40903  ?  99  GLN A O      1 
ATOM   1591 C CB     . GLN A 1 99  ? 24.31100  -20.79000 14.60200 1.000 45.61030  ?  99  GLN A CB     1 
ATOM   1592 C CG     . GLN A 1 99  ? 24.85300  -19.59700 15.38200 1.000 46.50886  ?  99  GLN A CG     1 
ATOM   1593 C CD     . GLN A 1 99  ? 26.03900  -18.96400 14.70400 1.000 47.78181  ?  99  GLN A CD     1 
ATOM   1594 O OE1    . GLN A 1 99  ? 25.90600  -18.33600 13.64800 1.000 44.38469  ?  99  GLN A OE1    1 
ATOM   1595 N NE2    . GLN A 1 99  ? 27.22100  -19.12900 15.29600 1.000 46.52289  ?  99  GLN A NE2    1 
ATOM   1596 H H      . GLN A 1 99  ? 22.12900  -22.43800 13.76000 1.000 53.66663  ?  99  GLN A H      1 
ATOM   1597 H HA     . GLN A 1 99  ? 23.11000  -21.55800 16.10900 1.000 55.28534  ?  99  GLN A HA     1 
ATOM   1598 H HB2    . GLN A 1 99  ? 24.98500  -21.48700 14.62200 1.000 54.85013  ?  99  GLN A HB2    1 
ATOM   1599 H HB3    . GLN A 1 99  ? 24.15800  -20.50100 13.68900 1.000 54.85013  ?  99  GLN A HB3    1 
ATOM   1600 H HG2    . GLN A 1 99  ? 24.15700  -18.92600 15.46100 1.000 55.92841  ?  99  GLN A HG2    1 
ATOM   1601 H HG3    . GLN A 1 99  ? 25.13100  -19.89200 16.26300 1.000 55.92841  ?  99  GLN A HG3    1 
ATOM   1602 H HE21   . GLN A 1 99  ? 27.27700  -19.57700 16.02700 1.000 55.94523  ?  99  GLN A HE21   1 
ATOM   1603 H HE22   . GLN A 1 99  ? 27.92800  -18.78600 14.94600 1.000 55.94523  ?  99  GLN A HE22   1 
ATOM   1604 N N      . LEU A 1 100 ? 21.60100  -19.65200 16.15700 1.000 48.68125  ?  100 LEU A N      1 
ATOM   1605 C CA     . LEU A 1 100 ? 20.63600  -18.56300 16.20400 1.000 42.01930  ?  100 LEU A CA     1 
ATOM   1606 C C      . LEU A 1 100 ? 21.33500  -17.31800 16.73700 1.000 48.25508  ?  100 LEU A C      1 
ATOM   1607 O O      . LEU A 1 100 ? 21.94200  -17.35500 17.81800 1.000 50.01730  ?  100 LEU A O      1 
ATOM   1608 C CB     . LEU A 1 100 ? 19.44900  -18.92900 17.09100 1.000 45.42542  ?  100 LEU A CB     1 
ATOM   1609 C CG     . LEU A 1 100 ? 18.53300  -17.78900 17.53900 1.000 44.91542  ?  100 LEU A CG     1 
ATOM   1610 C CD1    . LEU A 1 100 ? 17.87000  -17.12700 16.34400 1.000 43.64387  ?  100 LEU A CD1    1 
ATOM   1611 C CD2    . LEU A 1 100 ? 17.48000  -18.29700 18.52100 1.000 43.50275  ?  100 LEU A CD2    1 
ATOM   1612 H H      . LEU A 1 100 ? 21.96700  -19.81300 16.91800 1.000 58.53527  ?  100 LEU A H      1 
ATOM   1613 H HA     . LEU A 1 100 ? 20.30200  -18.37300 15.31400 1.000 50.54093  ?  100 LEU A HA     1 
ATOM   1614 H HB2    . LEU A 1 100 ? 18.89600  -19.56000 16.60400 1.000 54.62827  ?  100 LEU A HB2    1 
ATOM   1615 H HB3    . LEU A 1 100 ? 19.79500  -19.34500 17.89600 1.000 54.62827  ?  100 LEU A HB3    1 
ATOM   1616 H HG     . LEU A 1 100 ? 19.06900  -17.11900 17.99100 1.000 54.01628  ?  100 LEU A HG     1 
ATOM   1617 H HD11   . LEU A 1 100 ? 17.35900  -16.36200 16.65000 1.000 52.49041  ?  100 LEU A HD11   1 
ATOM   1618 H HD12   . LEU A 1 100 ? 18.55600  -16.83900 15.72200 1.000 52.49041  ?  100 LEU A HD12   1 
ATOM   1619 H HD13   . LEU A 1 100 ? 17.28200  -17.76800 15.91400 1.000 52.49041  ?  100 LEU A HD13   1 
ATOM   1620 H HD21   . LEU A 1 100 ? 16.93300  -17.55000 18.81300 1.000 52.32107  ?  100 LEU A HD21   1 
ATOM   1621 H HD22   . LEU A 1 100 ? 16.92600  -18.95800 18.07700 1.000 52.32107  ?  100 LEU A HD22   1 
ATOM   1622 H HD23   . LEU A 1 100 ? 17.92600  -18.69700 19.28400 1.000 52.32107  ?  100 LEU A HD23   1 
ATOM   1623 N N      . CYS A 1 101 ? 21.25600  -16.22600 15.99000 1.000 44.00707  ?  101 CYS A N      1 
ATOM   1624 C CA     . CYS A 1 101 ? 21.95000  -14.98900 16.32500 1.000 42.89697  ?  101 CYS A CA     1 
ATOM   1625 C C      . CYS A 1 101 ? 20.94100  -13.84000 16.41600 1.000 42.60328  ?  101 CYS A C      1 
ATOM   1626 O O      . CYS A 1 101 ? 20.02000  -13.74800 15.59500 1.000 40.15121  ?  101 CYS A O      1 
ATOM   1627 C CB     . CYS A 1 101 ? 23.01700  -14.65300 15.27300 1.000 36.41652  ?  101 CYS A CB     1 
ATOM   1628 S SG     . CYS A 1 101 ? 24.33700  -15.86400 15.13300 1.000 46.87370  ?  101 CYS A SG     1 
ATOM   1629 H H      . CYS A 1 101 ? 20.79400  -16.17500 15.26600 1.000 52.92625  ?  101 CYS A H      1 
ATOM   1630 H HA     . CYS A 1 101 ? 22.38600  -15.08600 17.18600 1.000 51.59413  ?  101 CYS A HA     1 
ATOM   1631 H HB2    . CYS A 1 101 ? 22.58600  -14.58900 14.40600 1.000 43.81759  ?  101 CYS A HB2    1 
ATOM   1632 H HB3    . CYS A 1 101 ? 23.42200  -13.80300 15.50500 1.000 43.81759  ?  101 CYS A HB3    1 
ATOM   1633 H HG     . CYS A 1 101 ? 25.09500  -15.51900 14.26800 1.000 56.36621  ?  101 CYS A HG     1 
ATOM   1634 N N      . PHE A 1 102 ? 21.13300  -12.96400 17.39700 1.000 39.04069  ?  102 PHE A N      1 
ATOM   1635 C CA     . PHE A 1 102 ? 20.30300  -11.76700 17.50200 1.000 41.39398  ?  102 PHE A CA     1 
ATOM   1636 C C      . PHE A 1 102 ? 20.93400  -10.76700 18.45900 1.000 43.12379  ?  102 PHE A C      1 
ATOM   1637 O O      . PHE A 1 102 ? 21.67600  -11.13500 19.37900 1.000 43.67981  ?  102 PHE A O      1 
ATOM   1638 C CB     . PHE A 1 102 ? 18.87200  -12.09700 17.95300 1.000 39.95431  ?  102 PHE A CB     1 
ATOM   1639 C CG     . PHE A 1 102 ? 18.78000  -12.82600 19.25800 1.000 40.01356  ?  102 PHE A CG     1 
ATOM   1640 C CD1    . PHE A 1 102 ? 18.79000  -12.12700 20.46600 1.000 43.75821  ?  102 PHE A CD1    1 
ATOM   1641 C CD2    . PHE A 1 102 ? 18.64400  -14.20400 19.29500 1.000 42.83482  ?  102 PHE A CD2    1 
ATOM   1642 C CE1    . PHE A 1 102 ? 18.69500  -12.80000 21.68100 1.000 42.89449  ?  102 PHE A CE1    1 
ATOM   1643 C CE2    . PHE A 1 102 ? 18.54400  -14.88100 20.50900 1.000 44.17899  ?  102 PHE A CE2    1 
ATOM   1644 C CZ     . PHE A 1 102 ? 18.56600  -14.17800 21.69900 1.000 47.09657  ?  102 PHE A CZ     1 
ATOM   1645 H H      . PHE A 1 102 ? 21.73200  -13.03800 18.00900 1.000 46.96659  ?  102 PHE A H      1 
ATOM   1646 H HA     . PHE A 1 102 ? 20.26600  -11.35200 16.62600 1.000 49.79054  ?  102 PHE A HA     1 
ATOM   1647 H HB2    . PHE A 1 102 ? 18.37900  -11.26700 18.04700 1.000 48.06294  ?  102 PHE A HB2    1 
ATOM   1648 H HB3    . PHE A 1 102 ? 18.45600  -12.65400 17.27700 1.000 48.06294  ?  102 PHE A HB3    1 
ATOM   1649 H HD1    . PHE A 1 102 ? 18.86100  -11.20000 20.45800 1.000 52.62763  ?  102 PHE A HD1    1 
ATOM   1650 H HD2    . PHE A 1 102 ? 18.62000  -14.68300 18.49800 1.000 51.51955  ?  102 PHE A HD2    1 
ATOM   1651 H HE1    . PHE A 1 102 ? 18.71800  -12.32300 22.48000 1.000 51.59115  ?  102 PHE A HE1    1 
ATOM   1652 H HE2    . PHE A 1 102 ? 18.46200  -15.80700 20.51800 1.000 53.13255  ?  102 PHE A HE2    1 
ATOM   1653 H HZ     . PHE A 1 102 ? 18.49500  -14.62900 22.50900 1.000 56.63365  ?  102 PHE A HZ     1 
ATOM   1654 N N      . GLU A 1 103 ? 20.61100  -9.48900  18.23800 1.000 43.78650  ?  103 GLU A N      1 
ATOM   1655 C CA     . GLU A 1 103 ? 21.12900  -8.41300  19.06600 1.000 43.07306  ?  103 GLU A CA     1 
ATOM   1656 C C      . GLU A 1 103 ? 20.54600  -8.47100  20.47000 1.000 41.26679  ?  103 GLU A C      1 
ATOM   1657 O O      . GLU A 1 103 ? 19.34800  -8.69900  20.65000 1.000 45.68092  ?  103 GLU A O      1 
ATOM   1658 C CB     . GLU A 1 103 ? 20.81000  -7.06500  18.41200 1.000 41.67767  ?  103 GLU A CB     1 
ATOM   1659 C CG     . GLU A 1 103 ? 21.50100  -5.88200  19.04200 1.000 40.01723  ?  103 GLU A CG     1 
ATOM   1660 C CD     . GLU A 1 103 ? 21.17600  -4.57600  18.31900 1.000 43.54162  ?  103 GLU A CD     1 
ATOM   1661 O OE1    . GLU A 1 103 ? 20.05600  -4.05600  18.51100 1.000 41.33668  ?  103 GLU A OE1    1 
ATOM   1662 O OE2    . GLU A 1 103 ? 22.03400  -4.07600  17.55600 1.000 47.07881  -1 103 GLU A OE2    1 
ATOM   1663 H H      . GLU A 1 103 ? 20.08900  -9.22200  17.60800 1.000 52.66157  ?  103 GLU A H      1 
ATOM   1664 H HA     . GLU A 1 103 ? 22.09200  -8.50000  19.14900 1.000 51.80544  ?  103 GLU A HA     1 
ATOM   1665 H HB2    . GLU A 1 103 ? 21.08100  -7.10200  17.48200 1.000 50.13097  ?  103 GLU A HB2    1 
ATOM   1666 H HB3    . GLU A 1 103 ? 19.85400  -6.91200  18.47300 1.000 50.13097  ?  103 GLU A HB3    1 
ATOM   1667 H HG2    . GLU A 1 103 ? 21.21300  -5.79800  19.96500 1.000 48.13844  ?  103 GLU A HG2    1 
ATOM   1668 H HG3    . GLU A 1 103 ? 22.46100  -6.01800  19.00600 1.000 48.13844  ?  103 GLU A HG3    1 
ATOM   1669 N N      . HIS A 1 104 ? 21.40300  -8.25400  21.46900 1.000 41.70868  ?  104 HIS A N      1 
ATOM   1670 C CA     . HIS A 1 104 ? 20.96200  -8.21900  22.85700 1.000 41.40850  ?  104 HIS A CA     1 
ATOM   1671 C C      . HIS A 1 104 ? 20.01900  -7.04200  23.10900 1.000 45.06627  ?  104 HIS A C      1 
ATOM   1672 O O      . HIS A 1 104 ? 20.18900  -5.95700  22.55600 1.000 36.38840  ?  104 HIS A O      1 
ATOM   1673 C CB     . HIS A 1 104 ? 22.16400  -8.12400  23.79000 1.000 44.15384  ?  104 HIS A CB     1 
ATOM   1674 C CG     . HIS A 1 104 ? 21.81000  -8.15500  25.24700 1.000 50.84182  ?  104 HIS A CG     1 
ATOM   1675 N ND1    . HIS A 1 104 ? 21.22400  -9.25000  25.84800 1.000 53.60497  ?  104 HIS A ND1    1 
ATOM   1676 C CD2    . HIS A 1 104 ? 21.97100  -7.22500  26.22400 1.000 51.69394  ?  104 HIS A CD2    1 
ATOM   1677 C CE1    . HIS A 1 104 ? 21.04200  -8.99800  27.13400 1.000 55.65820  ?  104 HIS A CE1    1 
ATOM   1678 N NE2    . HIS A 1 104 ? 21.48400  -7.77700  27.39000 1.000 54.77545  ?  104 HIS A NE2    1 
ATOM   1679 H H      . HIS A 1 104 ? 22.24700  -8.12500  21.36700 1.000 50.16819  ?  104 HIS A H      1 
ATOM   1680 H HA     . HIS A 1 104 ? 20.47900  -9.03700  23.05200 1.000 49.80797  ?  104 HIS A HA     1 
ATOM   1681 H HB2    . HIS A 1 104 ? 22.75400  -8.87300  23.61300 1.000 53.10238  ?  104 HIS A HB2    1 
ATOM   1682 H HB3    . HIS A 1 104 ? 22.62600  -7.28900  23.61600 1.000 53.10238  ?  104 HIS A HB3    1 
ATOM   1683 H HD2    . HIS A 1 104 ? 22.34000  -6.37700  26.12600 1.000 62.15050  ?  104 HIS A HD2    1 
ATOM   1684 H HE1    . HIS A 1 104 ? 20.66700  -9.58100  27.75400 1.000 66.90761  ?  104 HIS A HE1    1 
ATOM   1685 H HE2    . HIS A 1 104 ? 21.47000  -7.39100  28.15900 1.000 65.84831  ?  104 HIS A HE2    1 
ATOM   1686 N N      . ASP A 1 105 ? 19.01100  -7.27700  23.95200 1.000 49.75275  ?  105 ASP A N      1 
ATOM   1687 C CA     . ASP A 1 105 ? 18.01600  -6.28400  24.32200 1.000 53.02187  ?  105 ASP A CA     1 
ATOM   1688 C C      . ASP A 1 105 ? 17.81500  -6.33700  25.83100 1.000 54.41475  ?  105 ASP A C      1 
ATOM   1689 O O      . ASP A 1 105 ? 17.65600  -7.41800  26.39900 1.000 52.22213  ?  105 ASP A O      1 
ATOM   1690 C CB     . ASP A 1 105 ? 16.70000  -6.53500  23.58500 1.000 54.04314  ?  105 ASP A CB     1 
ATOM   1691 C CG     . ASP A 1 105 ? 15.69400  -5.42200  23.77700 1.000 55.07690  ?  105 ASP A CG     1 
ATOM   1692 O OD1    . ASP A 1 105 ? 16.04300  -4.39500  24.38700 1.000 59.74244  ?  105 ASP A OD1    1 
ATOM   1693 O OD2    . ASP A 1 105 ? 14.55400  -5.57400  23.30300 1.000 58.09556  -1 105 ASP A OD2    1 
ATOM   1694 H H      . ASP A 1 105 ? 18.88200  -8.03600  24.33500 1.000 59.82107  ?  105 ASP A H      1 
ATOM   1695 H HA     . ASP A 1 105 ? 18.32300  -5.39400  24.09000 1.000 63.74401  ?  105 ASP A HA     1 
ATOM   1696 H HB2    . ASP A 1 105 ? 16.88000  -6.61500  22.63600 1.000 64.96953  ?  105 ASP A HB2    1 
ATOM   1697 H HB3    . ASP A 1 105 ? 16.30400  -7.35600  23.91700 1.000 64.96953  ?  105 ASP A HB3    1 
ATOM   1698 N N      . THR A 1 106 ? 17.83100  -5.16800  26.47900 1.000 54.22236  ?  106 THR A N      1 
ATOM   1699 C CA     . THR A 1 106 ? 17.78400  -5.08800  27.93600 1.000 58.83327  ?  106 THR A CA     1 
ATOM   1700 C C      . THR A 1 106 ? 16.42000  -4.66900  28.47700 1.000 57.83211  ?  106 THR A C      1 
ATOM   1701 O O      . THR A 1 106 ? 16.28900  -4.46100  29.68700 1.000 57.54716  ?  106 THR A O      1 
ATOM   1702 C CB     . THR A 1 106 ? 18.84600  -4.11300  28.45000 1.000 58.10871  ?  106 THR A CB     1 
ATOM   1703 O OG1    . THR A 1 106 ? 18.54800  -2.78200  27.98500 1.000 51.52091  ?  106 THR A OG1    1 
ATOM   1704 C CG2    . THR A 1 106 ? 20.23900  -4.52800  27.97000 1.000 55.56130  ?  106 THR A CG2    1 
ATOM   1705 H H      . THR A 1 106 ? 17.87000  -4.40200  26.09000 1.000 65.18460  ?  106 THR A H      1 
ATOM   1706 H HA     . THR A 1 106 ? 17.98200  -5.97300  28.28100 1.000 70.71769  ?  106 THR A HA     1 
ATOM   1707 H HB     . THR A 1 106 ? 18.84900  -4.11900  29.42000 1.000 69.84822  ?  106 THR A HB     1 
ATOM   1708 H HG1    . THR A 1 106 ? 19.08500  -2.23300  28.32400 1.000 61.94286  ?  106 THR A HG1    1 
ATOM   1709 H HG21   . THR A 1 106 ? 20.91200  -3.95200  28.36600 1.000 66.79133  ?  106 THR A HG21   1 
ATOM   1710 H HG22   . THR A 1 106 ? 20.41900  -5.44500  28.22800 1.000 66.79133  ?  106 THR A HG22   1 
ATOM   1711 H HG23   . THR A 1 106 ? 20.29200  -4.45600  27.00400 1.000 66.79133  ?  106 THR A HG23   1 
ATOM   1712 N N      . GLU A 1 107 ? 15.40500  -4.53500  27.61700 1.000 57.67142  ?  107 GLU A N      1 
ATOM   1713 C CA     . GLU A 1 107 ? 14.07700  -4.18100  28.08900 1.000 60.05775  ?  107 GLU A CA     1 
ATOM   1714 C C      . GLU A 1 107 ? 13.49500  -5.32200  28.91900 1.000 61.91113  ?  107 GLU A C      1 
ATOM   1715 O O      . GLU A 1 107 ? 13.92900  -6.46800  28.80400 1.000 57.21370  ?  107 GLU A O      1 
ATOM   1716 C CB     . GLU A 1 107 ? 13.16200  -3.86000  26.92100 1.000 62.46009  ?  107 GLU A CB     1 
ATOM   1717 C CG     . GLU A 1 107 ? 13.37500  -2.47300  26.33400 1.000 64.03219  ?  107 GLU A CG     1 
ATOM   1718 C CD     . GLU A 1 107 ? 12.31300  -2.10200  25.30700 1.000 70.85309  ?  107 GLU A CD     1 
ATOM   1719 O OE1    . GLU A 1 107 ? 11.18600  -2.64000  25.39200 1.000 72.40050  ?  107 GLU A OE1    1 
ATOM   1720 O OE2    . GLU A 1 107 ? 12.60200  -1.26100  24.42100 1.000 64.93514  -1 107 GLU A OE2    1 
ATOM   1721 H H      . GLU A 1 107 ? 15.46600  -4.64400  26.76600 1.000 69.32348  ?  107 GLU A H      1 
ATOM   1722 H HA     . GLU A 1 107 ? 14.13000  -3.39000  28.64800 1.000 72.18707  ?  107 GLU A HA     1 
ATOM   1723 H HB2    . GLU A 1 107 ? 13.31900  -4.50700  26.21500 1.000 75.06988  ?  107 GLU A HB2    1 
ATOM   1724 H HB3    . GLU A 1 107 ? 12.24200  -3.91500  27.22300 1.000 75.06988  ?  107 GLU A HB3    1 
ATOM   1725 H HG2    . GLU A 1 107 ? 13.34300  -1.81800  27.04900 1.000 76.95639  ?  107 GLU A HG2    1 
ATOM   1726 H HG3    . GLU A 1 107 ? 14.24000  -2.44400  25.89600 1.000 76.95639  ?  107 GLU A HG3    1 
ATOM   1727 N N      . PRO A 1 108 ? 12.50800  -5.02600  29.77200 1.000 62.76722  ?  108 PRO A N      1 
ATOM   1728 C CA     . PRO A 1 108 ? 11.99300  -6.08000  30.66900 1.000 64.75310  ?  108 PRO A CA     1 
ATOM   1729 C C      . PRO A 1 108 ? 11.40500  -7.27600  29.94200 1.000 63.44920  ?  108 PRO A C      1 
ATOM   1730 O O      . PRO A 1 108 ? 11.79900  -8.42600  30.22200 1.000 61.17747  ?  108 PRO A O      1 
ATOM   1731 C CB     . PRO A 1 108 ? 10.93200  -5.34100  31.51000 1.000 73.17979  ?  108 PRO A CB     1 
ATOM   1732 C CG     . PRO A 1 108 ? 11.25000  -3.88000  31.36700 1.000 67.74360  ?  108 PRO A CG     1 
ATOM   1733 C CD     . PRO A 1 108 ? 11.85600  -3.72200  30.00100 1.000 63.08953  ?  108 PRO A CD     1 
ATOM   1734 H HA     . PRO A 1 108 ? 12.71400  -6.38200  31.24300 1.000 77.82149  ?  108 PRO A HA     1 
ATOM   1735 H HB2    . PRO A 1 108 ? 10.04600  -5.53600  31.16600 1.000 87.93352  ?  108 PRO A HB2    1 
ATOM   1736 H HB3    . PRO A 1 108 ? 10.99600  -5.61900  32.43700 1.000 87.93352  ?  108 PRO A HB3    1 
ATOM   1737 H HG2    . PRO A 1 108 ? 10.43500  -3.35900  31.44300 1.000 81.41009  ?  108 PRO A HG2    1 
ATOM   1738 H HG3    . PRO A 1 108 ? 11.88000  -3.61400  32.05500 1.000 81.41009  ?  108 PRO A HG3    1 
ATOM   1739 H HD2    . PRO A 1 108 ? 11.17100  -3.55600  29.33500 1.000 75.82521  ?  108 PRO A HD2    1 
ATOM   1740 H HD3    . PRO A 1 108 ? 12.50700  -3.00300  29.99200 1.000 75.82521  ?  108 PRO A HD3    1 
ATOM   1741 N N      . TYR A 1 109 ? 10.47300  -7.05200  29.01200 1.000 65.10090  ?  109 TYR A N      1 
ATOM   1742 C CA     . TYR A 1 109 ? 9.84900   -8.16900  28.31200 1.000 66.45761  ?  109 TYR A CA     1 
ATOM   1743 C C      . TYR A 1 109 ? 10.87400  -8.95600  27.50200 1.000 64.77223  ?  109 TYR A C      1 
ATOM   1744 O O      . TYR A 1 109 ? 10.77800  -10.18500 27.38700 1.000 59.25202  ?  109 TYR A O      1 
ATOM   1745 C CB     . TYR A 1 109 ? 8.72800   -7.66600  27.39500 1.000 69.16599  ?  109 TYR A CB     1 
ATOM   1746 C CG     . TYR A 1 109 ? 8.37100   -8.63800  26.29000 0.690 72.41926  ?  109 TYR A CG     1 
ATOM   1747 C CD1    . TYR A 1 109 ? 7.49300   -9.68800  26.52000 1.000 83.75217  ?  109 TYR A CD1    1 
ATOM   1748 C CD2    . TYR A 1 109 ? 8.91900   -8.51200  25.01900 1.000 71.32442  ?  109 TYR A CD2    1 
ATOM   1749 C CE1    . TYR A 1 109 ? 7.16600   -10.58700 25.51200 1.000 79.78672  ?  109 TYR A CE1    1 
ATOM   1750 C CE2    . TYR A 1 109 ? 8.60200   -9.40800  24.00700 0.660 74.72244  ?  109 TYR A CE2    1 
ATOM   1751 C CZ     . TYR A 1 109 ? 7.72300   -10.44400 24.26300 0.510 73.04376  ?  109 TYR A CZ     1 
ATOM   1752 O OH     . TYR A 1 109 ? 7.39600   -11.34500 23.26800 1.000 76.13050  ?  109 TYR A OH     1 
ATOM   1753 H H      . TYR A 1 109 ? 10.19100  -6.27600  28.77400 1.000 78.23885  ?  109 TYR A H      1 
ATOM   1754 H HA     . TYR A 1 109 ? 9.45700   -8.76300  28.97100 1.000 79.86691  ?  109 TYR A HA     1 
ATOM   1755 H HB2    . TYR A 1 109 ? 7.93200   -7.51600  27.92800 1.000 83.11696  ?  109 TYR A HB2    1 
ATOM   1756 H HB3    . TYR A 1 109 ? 9.01100   -6.83500  26.98200 1.000 83.11696  ?  109 TYR A HB3    1 
ATOM   1757 H HD1    . TYR A 1 109 ? 7.11800   -9.79300  27.36400 1.000 100.62038 ?  109 TYR A HD1    1 
ATOM   1758 H HD2    . TYR A 1 109 ? 9.51000   -7.81500  24.84400 1.000 85.70708  ?  109 TYR A HD2    1 
ATOM   1759 H HE1    . TYR A 1 109 ? 6.57200   -11.28200 25.68100 1.000 95.86183  ?  109 TYR A HE1    1 
ATOM   1760 H HE2    . TYR A 1 109 ? 8.97900   -9.31200  23.16200 1.000 89.78470  ?  109 TYR A HE2    1 
ATOM   1761 H HH     . TYR A 1 109 ? 7.84200   -11.18300 22.57500 1.000 91.47437  ?  109 TYR A HH     1 
ATOM   1762 N N      . ALA A 1 110 ? 11.85900  -8.26300  26.92500 1.000 63.98067  ?  110 ALA A N      1 
ATOM   1763 C CA     . ALA A 1 110 ? 12.83900  -8.93600  26.07800 1.000 65.58783  ?  110 ALA A CA     1 
ATOM   1764 C C      . ALA A 1 110 ? 13.60500  -9.99400  26.86300 1.000 58.78268  ?  110 ALA A C      1 
ATOM   1765 O O      . ALA A 1 110 ? 13.89800  -11.07400 26.33600 1.000 54.52898  ?  110 ALA A O      1 
ATOM   1766 C CB     . ALA A 1 110 ? 13.79900  -7.90800  25.47200 1.000 61.74969  ?  110 ALA A CB     1 
ATOM   1767 H H      . ALA A 1 110 ? 11.97800  -7.41500  27.00700 1.000 76.89457  ?  110 ALA A H      1 
ATOM   1768 H HA     . ALA A 1 110 ? 12.37800  -9.37900  25.35000 1.000 78.82317  ?  110 ALA A HA     1 
ATOM   1769 H HB1    . ALA A 1 110 ? 14.44000  -8.36900  24.90800 1.000 74.21740  ?  110 ALA A HB1    1 
ATOM   1770 H HB2    . ALA A 1 110 ? 13.29000  -7.27400  24.94300 1.000 74.21740  ?  110 ALA A HB2    1 
ATOM   1771 H HB3    . ALA A 1 110 ? 14.26100  -7.44500  26.18800 1.000 74.21740  ?  110 ALA A HB3    1 
ATOM   1772 N N      . LYS A 1 111 ? 13.93200  -9.70500  28.12400 1.000 58.91785  ?  111 LYS A N      1 
ATOM   1773 C CA     . LYS A 1 111 ? 14.67500  -10.67600 28.92500 1.000 68.28426  ?  111 LYS A CA     1 
ATOM   1774 C C      . LYS A 1 111 ? 13.87300  -11.96000 29.12300 1.000 65.22467  ?  111 LYS A C      1 
ATOM   1775 O O      . LYS A 1 111 ? 14.42100  -13.06800 29.02200 1.000 58.83519  ?  111 LYS A O      1 
ATOM   1776 C CB     . LYS A 1 111 ? 15.05200  -10.07100 30.28300 1.000 75.10361  ?  111 LYS A CB     1 
ATOM   1777 C CG     . LYS A 1 111 ? 15.51500  -8.60900  30.23700 1.000 77.64388  ?  111 LYS A CG     1 
ATOM   1778 C CD     . LYS A 1 111 ? 17.01500  -8.45600  30.49600 1.000 87.27050  ?  111 LYS A CD     1 
ATOM   1779 C CE     . LYS A 1 111 ? 17.31500  -8.23000  31.96600 1.000 86.60462  ?  111 LYS A CE     1 
ATOM   1780 N NZ     . LYS A 1 111 ? 18.76700  -8.39200  32.25700 1.000 104.55051 ?  111 LYS A NZ     1 
ATOM   1781 H H      . LYS A 1 111 ? 13.74000  -8.97100  28.53000 1.000 70.81919  ?  111 LYS A H      1 
ATOM   1782 H HA     . LYS A 1 111 ? 15.49400  -10.89800 28.45600 1.000 82.05888  ?  111 LYS A HA     1 
ATOM   1783 H HB2    . LYS A 1 111 ? 14.27500  -10.11100 30.86300 1.000 90.24210  ?  111 LYS A HB2    1 
ATOM   1784 H HB3    . LYS A 1 111 ? 15.77600  -10.59300 30.66100 1.000 90.24210  ?  111 LYS A HB3    1 
ATOM   1785 H HG2    . LYS A 1 111 ? 15.32400  -8.24300  29.35900 1.000 93.29042  ?  111 LYS A HG2    1 
ATOM   1786 H HG3    . LYS A 1 111 ? 15.04100  -8.10400  30.91600 1.000 93.29042  ?  111 LYS A HG3    1 
ATOM   1787 H HD2    . LYS A 1 111 ? 17.47200  -9.26300  30.21300 1.000 104.84237 ?  111 LYS A HD2    1 
ATOM   1788 H HD3    . LYS A 1 111 ? 17.34900  -7.69300  29.99800 1.000 104.84237 ?  111 LYS A HD3    1 
ATOM   1789 H HE2    . LYS A 1 111 ? 17.05300  -7.33000  32.21300 1.000 104.04332 ?  111 LYS A HE2    1 
ATOM   1790 H HE3    . LYS A 1 111 ? 16.82400  -8.87600  32.49700 1.000 104.04332 ?  111 LYS A HE3    1 
ATOM   1791 H HZ1    . LYS A 1 111 ? 18.91900  -8.27400  33.12600 1.000 125.57839 ?  111 LYS A HZ1    1 
ATOM   1792 H HZ2    . LYS A 1 111 ? 19.03500  -9.20900  32.02600 1.000 125.57839 ?  111 LYS A HZ2    1 
ATOM   1793 H HZ3    . LYS A 1 111 ? 19.23900  -7.79300  31.79800 1.000 125.57839 ?  111 LYS A HZ3    1 
ATOM   1794 N N      . VAL A 1 112 ? 12.57400  -11.83400 29.40600 1.000 60.83843  ?  112 VAL A N      1 
ATOM   1795 C CA     . VAL A 1 112 ? 11.72500  -13.01600 29.56300 1.000 60.78094  ?  112 VAL A CA     1 
ATOM   1796 C C      . VAL A 1 112 ? 11.62200  -13.77200 28.24300 1.000 56.74138  ?  112 VAL A C      1 
ATOM   1797 O O      . VAL A 1 112 ? 11.73300  -15.00300 28.19900 1.000 57.14837  ?  112 VAL A O      1 
ATOM   1798 C CB     . VAL A 1 112 ? 10.33600  -12.60700 30.08600 1.000 68.57286  ?  112 VAL A CB     1 
ATOM   1799 C CG1    . VAL A 1 112 ? 9.33600   -13.76000 29.95900 1.000 67.28186  ?  112 VAL A CG1    1 
ATOM   1800 C CG2    . VAL A 1 112 ? 10.43300  -12.13700 31.53000 1.000 65.59503  ?  112 VAL A CG2    1 
ATOM   1801 H H      . VAL A 1 112 ? 12.16500  -11.08400 29.51000 1.000 73.12389  ?  112 VAL A H      1 
ATOM   1802 H HA     . VAL A 1 112 ? 12.13300  -13.60700 30.21500 1.000 73.05490  ?  112 VAL A HA     1 
ATOM   1803 H HB     . VAL A 1 112 ? 10.00600  -11.87200 29.54500 1.000 82.40521  ?  112 VAL A HB     1 
ATOM   1804 H HG11   . VAL A 1 112 ? 8.48000   -13.47600 30.31600 1.000 80.85600  ?  112 VAL A HG11   1 
ATOM   1805 H HG12   . VAL A 1 112 ? 9.24200   -13.99500 29.02300 1.000 80.85600  ?  112 VAL A HG12   1 
ATOM   1806 H HG13   . VAL A 1 112 ? 9.66700   -14.52100 30.46000 1.000 80.85600  ?  112 VAL A HG13   1 
ATOM   1807 H HG21   . VAL A 1 112 ? 9.55000   -11.88400 31.84100 1.000 78.83180  ?  112 VAL A HG21   1 
ATOM   1808 H HG22   . VAL A 1 112 ? 10.78100  -12.86000 32.07500 1.000 78.83180  ?  112 VAL A HG22   1 
ATOM   1809 H HG23   . VAL A 1 112 ? 11.03000  -11.37300 31.57400 1.000 78.83180  ?  112 VAL A HG23   1 
ATOM   1810 N N      . ARG A 1 113 ? 11.39400  -13.04300 27.15000 1.000 54.77446  ?  113 ARG A N      1 
ATOM   1811 C CA     . ARG A 1 113 ? 11.23600  -13.67600 25.84300 1.000 54.77201  ?  113 ARG A CA     1 
ATOM   1812 C C      . ARG A 1 113 ? 12.52200  -14.38400 25.41500 1.000 56.46121  ?  113 ARG A C      1 
ATOM   1813 O O      . ARG A 1 113 ? 12.48800  -15.53000 24.93900 1.000 52.09933  ?  113 ARG A O      1 
ATOM   1814 C CB     . ARG A 1 113 ? 10.83000  -12.61400 24.81500 1.000 56.39698  ?  113 ARG A CB     1 
ATOM   1815 C CG     . ARG A 1 113 ? 10.77200  -13.08500 23.36800 1.000 57.61509  ?  113 ARG A CG     1 
ATOM   1816 C CD     . ARG A 1 113 ? 10.92900  -11.91300 22.40000 1.000 56.09858  ?  113 ARG A CD     1 
ATOM   1817 N NE     . ARG A 1 113 ? 12.18100  -11.18900 22.60100 1.000 53.87634  ?  113 ARG A NE     1 
ATOM   1818 C CZ     . ARG A 1 113 ? 12.37800  -9.91800  22.27300 1.000 55.80328  ?  113 ARG A CZ     1 
ATOM   1819 N NH1    . ARG A 1 113 ? 11.42100  -9.18900  21.72300 1.000 63.34298  ?  113 ARG A NH1    1 
ATOM   1820 N NH2    . ARG A 1 113 ? 13.56600  -9.36400  22.49400 1.000 55.75769  ?  113 ARG A NH2    1 
ATOM   1821 H H      . ARG A 1 113 ? 11.32700  -12.18600 27.13800 1.000 65.84712  ?  113 ARG A H      1 
ATOM   1822 H HA     . ARG A 1 113 ? 10.53400  -14.34400 25.89200 1.000 65.84419  ?  113 ARG A HA     1 
ATOM   1823 H HB2    . ARG A 1 113 ? 9.94700   -12.28700 25.04700 1.000 67.79415  ?  113 ARG A HB2    1 
ATOM   1824 H HB3    . ARG A 1 113 ? 11.47400  -11.88900 24.85600 1.000 67.79415  ?  113 ARG A HB3    1 
ATOM   1825 H HG2    . ARG A 1 113 ? 11.49100  -13.71600 23.20500 1.000 69.25588  ?  113 ARG A HG2    1 
ATOM   1826 H HG3    . ARG A 1 113 ? 9.91500   -13.50900 23.20100 1.000 69.25588  ?  113 ARG A HG3    1 
ATOM   1827 H HD2    . ARG A 1 113 ? 10.91700  -12.24900 21.49000 1.000 67.43606  ?  113 ARG A HD2    1 
ATOM   1828 H HD3    . ARG A 1 113 ? 10.19700  -11.29100 22.53300 1.000 67.43606  ?  113 ARG A HD3    1 
ATOM   1829 H HE     . ARG A 1 113 ? 12.83800  -11.61600 22.95700 1.000 64.76937  ?  113 ARG A HE     1 
ATOM   1830 H HH11   . ARG A 1 113 ? 10.65000  -9.53700  21.56900 1.000 76.12934  ?  113 ARG A HH11   1 
ATOM   1831 H HH12   . ARG A 1 113 ? 11.57100  -8.36700  21.51900 1.000 76.12934  ?  113 ARG A HH12   1 
ATOM   1832 H HH21   . ARG A 1 113 ? 14.19900  -9.82900  22.84600 1.000 67.02700  ?  113 ARG A HH21   1 
ATOM   1833 H HH22   . ARG A 1 113 ? 13.70300  -8.54100  22.28500 1.000 67.02700  ?  113 ARG A HH22   1 
ATOM   1834 N N      . ASP A 1 114 ? 13.66500  -13.71500 25.57300 1.000 48.61082  ?  114 ASP A N      1 
ATOM   1835 C CA     . ASP A 1 114 ? 14.92000  -14.26600 25.08000 1.000 49.18308  ?  114 ASP A CA     1 
ATOM   1836 C C      . ASP A 1 114 ? 15.38400  -15.46000 25.91500 1.000 52.05281  ?  114 ASP A C      1 
ATOM   1837 O O      . ASP A 1 114 ? 15.97100  -16.40100 25.37300 1.000 53.63743  ?  114 ASP A O      1 
ATOM   1838 C CB     . ASP A 1 114 ? 15.99200  -13.17600 25.05200 1.000 48.78591  ?  114 ASP A CB     1 
ATOM   1839 C CG     . ASP A 1 114 ? 15.68200  -12.08200 24.03000 1.000 48.58593  ?  114 ASP A CG     1 
ATOM   1840 O OD1    . ASP A 1 114 ? 14.83200  -12.30700 23.14100 1.000 49.49182  ?  114 ASP A OD1    1 
ATOM   1841 O OD2    . ASP A 1 114 ? 16.28900  -11.00000 24.11100 1.000 47.35337  -1 114 ASP A OD2    1 
ATOM   1842 H H      . ASP A 1 114 ? 13.73800  -12.94900 25.95800 1.000 58.45075  ?  114 ASP A H      1 
ATOM   1843 H HA     . ASP A 1 114 ? 14.78900  -14.57900 24.17200 1.000 59.13746  ?  114 ASP A HA     1 
ATOM   1844 H HB2    . ASP A 1 114 ? 16.04800  -12.76300 25.92800 1.000 58.66086  ?  114 ASP A HB2    1 
ATOM   1845 H HB3    . ASP A 1 114 ? 16.84400  -13.57500 24.81800 1.000 58.66086  ?  114 ASP A HB3    1 
ATOM   1846 N N      . ALA A 1 115 ? 15.12300  -15.44800 27.22400 1.000 56.47712  ?  115 ALA A N      1 
ATOM   1847 C CA     . ALA A 1 115 ? 15.44900  -16.60900 28.04600 1.000 59.72988  ?  115 ALA A CA     1 
ATOM   1848 C C      . ALA A 1 115 ? 14.67400  -17.84300 27.58500 1.000 58.27526  ?  115 ALA A C      1 
ATOM   1849 O O      . ALA A 1 115 ? 15.23200  -18.94800 27.50000 1.000 56.86331  ?  115 ALA A O      1 
ATOM   1850 C CB     . ALA A 1 115 ? 15.16400  -16.31200 29.51400 1.000 65.34927  ?  115 ALA A CB     1 
ATOM   1851 H H      . ALA A 1 115 ? 14.76500  -14.79200 27.65100 1.000 67.89031  ?  115 ALA A H      1 
ATOM   1852 H HA     . ALA A 1 115 ? 16.39600  -16.79900 27.96100 1.000 71.79363  ?  115 ALA A HA     1 
ATOM   1853 H HB1    . ALA A 1 115 ? 15.38000  -17.09500 30.04300 1.000 78.53689  ?  115 ALA A HB1    1 
ATOM   1854 H HB2    . ALA A 1 115 ? 15.71000  -15.56100 29.79600 1.000 78.53689  ?  115 ALA A HB2    1 
ATOM   1855 H HB3    . ALA A 1 115 ? 14.22400  -16.09300 29.61500 1.000 78.53689  ?  115 ALA A HB3    1 
ATOM   1856 N N      . ALA A 1 116 ? 13.39000  -17.67100 27.27300 1.000 56.42130  ?  116 ALA A N      1 
ATOM   1857 C CA     . ALA A 1 116 ? 12.59700  -18.80300 26.79700 1.000 61.33502  ?  116 ALA A CA     1 
ATOM   1858 C C      . ALA A 1 116 ? 13.13300  -19.33400 25.46600 1.000 59.87612  ?  116 ALA A C      1 
ATOM   1859 O O      . ALA A 1 116 ? 13.24400  -20.55200 25.27400 1.000 56.64933  ?  116 ALA A O      1 
ATOM   1860 C CB     . ALA A 1 116 ? 11.13400  -18.38500 26.65500 1.000 64.88719  ?  116 ALA A CB     1 
ATOM   1861 H H      . ALA A 1 116 ? 12.96300  -16.92700 27.32600 1.000 67.82333  ?  116 ALA A H      1 
ATOM   1862 H HA     . ALA A 1 116 ? 12.64800  -19.52000 27.44800 1.000 73.71980  ?  116 ALA A HA     1 
ATOM   1863 H HB1    . ALA A 1 116 ? 10.61700  -19.14500 26.34600 1.000 77.98239  ?  116 ALA A HB1    1 
ATOM   1864 H HB2    . ALA A 1 116 ? 10.80500  -18.09000 27.51800 1.000 77.98239  ?  116 ALA A HB2    1 
ATOM   1865 H HB3    . ALA A 1 116 ? 11.07400  -17.66100 26.01200 1.000 77.98239  ?  116 ALA A HB3    1 
ATOM   1866 N N      . VAL A 1 117 ? 13.48000  -18.43300 24.53700 1.000 49.19195  ?  117 VAL A N      1 
ATOM   1867 C CA     . VAL A 1 117 ? 14.02500  -18.87200 23.26100 1.000 48.49239  ?  117 VAL A CA     1 
ATOM   1868 C C      . VAL A 1 117 ? 15.36400  -19.57400 23.46700 1.000 48.24312  ?  117 VAL A C      1 
ATOM   1869 O O      . VAL A 1 117 ? 15.68400  -20.55200 22.77200 1.000 48.31925  ?  117 VAL A O      1 
ATOM   1870 C CB     . VAL A 1 117 ? 14.15200  -17.68500 22.28600 1.000 50.84205  ?  117 VAL A CB     1 
ATOM   1871 C CG1    . VAL A 1 117 ? 14.96400  -18.08300 21.05500 1.000 47.16288  ?  117 VAL A CG1    1 
ATOM   1872 C CG2    . VAL A 1 117 ? 12.78600  -17.19500 21.87600 1.000 50.31693  ?  117 VAL A CG2    1 
ATOM   1873 H H      . VAL A 1 117 ? 13.40800  -17.58100 24.62500 1.000 59.14811  ?  117 VAL A H      1 
ATOM   1874 H HA     . VAL A 1 117 ? 13.40800  -19.51000 22.87000 1.000 58.30863  ?  117 VAL A HA     1 
ATOM   1875 H HB     . VAL A 1 117 ? 14.61700  -16.96200 22.73600 1.000 61.12823  ?  117 VAL A HB     1 
ATOM   1876 H HG11   . VAL A 1 117 ? 14.81700  -17.42700 20.35500 1.000 56.71323  ?  117 VAL A HG11   1 
ATOM   1877 H HG12   . VAL A 1 117 ? 15.90400  -18.10900 21.29200 1.000 56.71323  ?  117 VAL A HG12   1 
ATOM   1878 H HG13   . VAL A 1 117 ? 14.67400  -18.95800 20.75400 1.000 56.71323  ?  117 VAL A HG13   1 
ATOM   1879 H HG21   . VAL A 1 117 ? 12.88800  -16.46100 21.25000 1.000 60.49808  ?  117 VAL A HG21   1 
ATOM   1880 H HG22   . VAL A 1 117 ? 12.30100  -17.92300 21.45700 1.000 60.49808  ?  117 VAL A HG22   1 
ATOM   1881 H HG23   . VAL A 1 117 ? 12.30900  -16.89200 22.66500 1.000 60.49808  ?  117 VAL A HG23   1 
ATOM   1882 N N      . ARG A 1 118 ? 16.16500  -19.08900 24.42100 1.000 52.21982  ?  118 ARG A N      1 
ATOM   1883 C CA     A ARG A 1 118 ? 17.44300  -19.73200 24.71200 0.490 51.02755  ?  118 ARG A CA     1 
ATOM   1884 C CA     B ARG A 1 118 ? 17.44400  -19.73500 24.69600 0.510 51.01288  ?  118 ARG A CA     1 
ATOM   1885 C C      . ARG A 1 118 ? 17.24700  -21.18400 25.13700 1.000 54.66021  ?  118 ARG A C      1 
ATOM   1886 O O      . ARG A 1 118 ? 18.03300  -22.06800 24.76100 1.000 53.60440  ?  118 ARG A O      1 
ATOM   1887 C CB     A ARG A 1 118 ? 18.17900  -18.96100 25.80900 0.490 54.66941  ?  118 ARG A CB     1 
ATOM   1888 C CB     B ARG A 1 118 ? 18.21100  -18.94100 25.75400 0.510 54.70405  ?  118 ARG A CB     1 
ATOM   1889 C CG     A ARG A 1 118 ? 18.93700  -17.73400 25.32600 0.490 57.69235  ?  118 ARG A CG     1 
ATOM   1890 C CG     B ARG A 1 118 ? 18.89300  -17.69000 25.19900 0.510 57.61412  ?  118 ARG A CG     1 
ATOM   1891 C CD     A ARG A 1 118 ? 19.68000  -17.07600 26.48900 0.490 60.99810  ?  118 ARG A CD     1 
ATOM   1892 C CD     B ARG A 1 118 ? 19.58400  -16.88600 26.29900 0.510 61.30952  ?  118 ARG A CD     1 
ATOM   1893 N NE     A ARG A 1 118 ? 20.02800  -15.68700 26.21600 0.490 62.64563  ?  118 ARG A NE     1 
ATOM   1894 N NE     B ARG A 1 118 ? 19.99200  -15.56200 25.83800 0.510 62.31613  ?  118 ARG A NE     1 
ATOM   1895 C CZ     A ARG A 1 118 ? 21.10700  -15.29700 25.54900 0.490 63.14561  ?  118 ARG A CZ     1 
ATOM   1896 C CZ     B ARG A 1 118 ? 19.39300  -14.42100 26.17200 0.510 61.04251  ?  118 ARG A CZ     1 
ATOM   1897 N NH1    A ARG A 1 118 ? 21.96400  -16.17200 25.05000 0.490 60.46049  ?  118 ARG A NH1    1 
ATOM   1898 N NH1    B ARG A 1 118 ? 18.33400  -14.40100 26.96500 0.510 64.23138  ?  118 ARG A NH1    1 
ATOM   1899 N NH2    A ARG A 1 118 ? 21.33200  -13.99600 25.38200 0.490 62.10777  ?  118 ARG A NH2    1 
ATOM   1900 N NH2    B ARG A 1 118 ? 19.87300  -13.27400 25.69700 0.510 55.76494  ?  118 ARG A NH2    1 
ATOM   1901 H H      A ARG A 1 118 ? 15.99200  -18.40000 24.90500 0.490 62.78155  ?  118 ARG A H      1 
ATOM   1902 H H      B ARG A 1 118 ? 15.99300  -18.40300 24.91000 0.510 62.78155  ?  118 ARG A H      1 
ATOM   1903 H HA     A ARG A 1 118 ? 17.98600  -19.71800 23.90900 0.490 61.35083  ?  118 ARG A HA     1 
ATOM   1904 H HA     B ARG A 1 118 ? 17.97600  -19.74300 23.88500 0.510 61.33322  ?  118 ARG A HA     1 
ATOM   1905 H HB2    A ARG A 1 118 ? 17.52900  -18.66300 26.46500 0.490 65.72106  ?  118 ARG A HB2    1 
ATOM   1906 H HB2    B ARG A 1 118 ? 17.59100  -18.66000 26.44500 0.510 65.76263  ?  118 ARG A HB2    1 
ATOM   1907 H HB3    A ARG A 1 118 ? 18.82200  -19.55600 26.22500 0.490 65.72106  ?  118 ARG A HB3    1 
ATOM   1908 H HB3    B ARG A 1 118 ? 18.89700  -19.51000 26.13600 0.510 65.76263  ?  118 ARG A HB3    1 
ATOM   1909 H HG2    A ARG A 1 118 ? 19.58400  -17.99500 24.65300 0.490 69.34858  ?  118 ARG A HG2    1 
ATOM   1910 H HG2    B ARG A 1 118 ? 19.56300  -17.95300 24.54900 0.510 69.25472  ?  118 ARG A HG2    1 
ATOM   1911 H HG3    A ARG A 1 118 ? 18.31200  -17.09100 24.95500 0.490 69.34858  ?  118 ARG A HG3    1 
ATOM   1912 H HG3    B ARG A 1 118 ? 18.22800  -17.12200 24.77900 0.510 69.25472  ?  118 ARG A HG3    1 
ATOM   1913 H HD2    A ARG A 1 118 ? 19.11600  -17.09600 27.27800 0.490 73.31549  ?  118 ARG A HD2    1 
ATOM   1914 H HD2    B ARG A 1 118 ? 18.97100  -16.77100 27.04300 0.510 73.68919  ?  118 ARG A HD2    1 
ATOM   1915 H HD3    A ARG A 1 118 ? 20.50200  -17.56500 26.65600 0.490 73.31549  ?  118 ARG A HD3    1 
ATOM   1916 H HD3    B ARG A 1 118 ? 20.37600  -17.36200 26.59300 0.510 73.68919  ?  118 ARG A HD3    1 
ATOM   1917 H HE     A ARG A 1 118 ? 19.49600  -15.07700 26.50700 0.490 75.29252  ?  118 ARG A HE     1 
ATOM   1918 H HE     B ARG A 1 118 ? 20.67000  -15.51700 25.31100 0.510 74.89713  ?  118 ARG A HE     1 
ATOM   1919 H HH11   A ARG A 1 118 ? 21.82700  -17.01500 25.15500 0.490 72.67035  ?  118 ARG A HH11   1 
ATOM   1920 H HH11   B ARG A 1 118 ? 18.01700  -15.13600 27.27700 0.510 77.19542  ?  118 ARG A HH11   1 
ATOM   1921 H HH12   A ARG A 1 118 ? 22.65700  -15.89900 24.62100 0.490 72.67035  ?  118 ARG A HH12   1 
ATOM   1922 H HH12   B ARG A 1 118 ? 17.96300  -13.65200 27.16800 0.510 77.19542  ?  118 ARG A HH12   1 
ATOM   1923 H HH21   A ARG A 1 118 ? 20.78100  -13.42000 25.70400 0.490 74.64709  ?  118 ARG A HH21   1 
ATOM   1924 H HH21   B ARG A 1 118 ? 20.56100  -13.27700 25.18100 0.510 67.03570  ?  118 ARG A HH21   1 
ATOM   1925 H HH22   A ARG A 1 118 ? 22.02800  -13.73200 24.95200 0.490 74.64709  ?  118 ARG A HH22   1 
ATOM   1926 H HH22   B ARG A 1 118 ? 19.49500  -12.53000 25.90500 0.510 67.03570  ?  118 ARG A HH22   1 
ATOM   1927 N N      . ARG A 1 119 ? 16.20500  -21.45200 25.93600 1.000 53.04370  ?  119 ARG A N      1 
ATOM   1928 C CA     . ARG A 1 119 ? 15.92500  -22.82700 26.34700 1.000 53.97176  ?  119 ARG A CA     1 
ATOM   1929 C C      . ARG A 1 119 ? 15.54800  -23.68900 25.14900 1.000 51.83370  ?  119 ARG A C      1 
ATOM   1930 O O      . ARG A 1 119 ? 16.03300  -24.81800 25.00600 1.000 54.93921  ?  119 ARG A O      1 
ATOM   1931 C CB     . ARG A 1 119 ? 14.80600  -22.84900 27.39300 1.000 59.26991  ?  119 ARG A CB     1 
ATOM   1932 C CG     . ARG A 1 119 ? 14.21000  -24.24400 27.65500 1.000 77.60807  ?  119 ARG A CG     1 
ATOM   1933 C CD     . ARG A 1 119 ? 12.91600  -24.21000 28.48700 1.000 79.33375  ?  119 ARG A CD     1 
ATOM   1934 N NE     . ARG A 1 119 ? 12.05000  -23.08200 28.15400 1.000 92.31837  ?  119 ARG A NE     1 
ATOM   1935 C CZ     . ARG A 1 119 ? 10.97300  -22.73400 28.84700 1.000 95.80785  ?  119 ARG A CZ     1 
ATOM   1936 N NH1    . ARG A 1 119 ? 10.56900  -23.43800 29.89300 1.000 79.65295  ?  119 ARG A NH1    1 
ATOM   1937 N NH2    . ARG A 1 119 ? 10.28700  -21.65400 28.48300 1.000 85.18395  ?  119 ARG A NH2    1 
ATOM   1938 H H      . ARG A 1 119 ? 15.65800  -20.86600 26.24600 1.000 63.77021  ?  119 ARG A H      1 
ATOM   1939 H HA     . ARG A 1 119 ? 16.72400  -23.19800 26.75200 1.000 64.88388  ?  119 ARG A HA     1 
ATOM   1940 H HB2    . ARG A 1 119 ? 15.16100  -22.51900 28.23300 1.000 71.24166  ?  119 ARG A HB2    1 
ATOM   1941 H HB3    . ARG A 1 119 ? 14.08600  -22.27500 27.08900 1.000 71.24166  ?  119 ARG A HB3    1 
ATOM   1942 H HG2    . ARG A 1 119 ? 14.00600  -24.66200 26.80400 1.000 93.24745  ?  119 ARG A HG2    1 
ATOM   1943 H HG3    . ARG A 1 119 ? 14.86100  -24.77700 28.13900 1.000 93.24745  ?  119 ARG A HG3    1 
ATOM   1944 H HD2    . ARG A 1 119 ? 12.41700  -25.02700 28.32600 1.000 95.31827  ?  119 ARG A HD2    1 
ATOM   1945 H HD3    . ARG A 1 119 ? 13.14600  -24.14200 29.42600 1.000 95.31827  ?  119 ARG A HD3    1 
ATOM   1946 H HE     . ARG A 1 119 ? 12.25200  -22.61100 27.46300 1.000 110.89981 ?  119 ARG A HE     1 
ATOM   1947 H HH11   . ARG A 1 119 ? 11.00700  -24.13700 30.13600 1.000 95.70131  ?  119 ARG A HH11   1 
ATOM   1948 H HH12   . ARG A 1 119 ? 9.86800   -23.19600 30.32900 1.000 95.70131  ?  119 ARG A HH12   1 
ATOM   1949 H HH21   . ARG A 1 119 ? 10.54200  -21.19000 27.80500 1.000 102.33851 ?  119 ARG A HH21   1 
ATOM   1950 H HH22   . ARG A 1 119 ? 9.58700   -21.41900 28.92500 1.000 102.33851 ?  119 ARG A HH22   1 
ATOM   1951 N N      . LEU A 1 120 ? 14.67300  -23.17800 24.28000 1.000 51.31672  ?  120 LEU A N      1 
ATOM   1952 C CA     . LEU A 1 120 ? 14.21700  -23.96500 23.13900 1.000 50.89301  ?  120 LEU A CA     1 
ATOM   1953 C C      . LEU A 1 120 ? 15.37000  -24.26000 22.17900 1.000 51.17236  ?  120 LEU A C      1 
ATOM   1954 O O      . LEU A 1 120 ? 15.44100  -25.34500 21.59700 1.000 49.59537  ?  120 LEU A O      1 
ATOM   1955 C CB     . LEU A 1 120 ? 13.08700  -23.23900 22.41800 1.000 52.56880  ?  120 LEU A CB     1 
ATOM   1956 C CG     . LEU A 1 120 ? 11.84900  -22.92900 23.27300 1.000 55.18442  ?  120 LEU A CG     1 
ATOM   1957 C CD1    . LEU A 1 120 ? 10.99600  -21.83900 22.63300 1.000 61.43706  ?  120 LEU A CD1    1 
ATOM   1958 C CD2    . LEU A 1 120 ? 11.01600  -24.18600 23.50500 1.000 58.69323  ?  120 LEU A CD2    1 
ATOM   1959 H H      . LEU A 1 120 ? 14.33400  -22.38900 24.32900 1.000 61.69783  ?  120 LEU A H      1 
ATOM   1960 H HA     . LEU A 1 120 ? 13.86900  -24.81100 23.46100 1.000 61.18939  ?  120 LEU A HA     1 
ATOM   1961 H HB2    . LEU A 1 120 ? 13.43000  -22.39400 22.08700 1.000 63.20033  ?  120 LEU A HB2    1 
ATOM   1962 H HB3    . LEU A 1 120 ? 12.79500  -23.79200 21.67600 1.000 63.20033  ?  120 LEU A HB3    1 
ATOM   1963 H HG     . LEU A 1 120 ? 12.15100  -22.60400 24.13600 1.000 66.33907  ?  120 LEU A HG     1 
ATOM   1964 H HD11   . LEU A 1 120 ? 10.26300  -21.62100 23.22900 1.000 73.84224  ?  120 LEU A HD11   1 
ATOM   1965 H HD12   . LEU A 1 120 ? 11.54700  -21.05400 22.48500 1.000 73.84224  ?  120 LEU A HD12   1 
ATOM   1966 H HD13   . LEU A 1 120 ? 10.65000  -22.16400 21.78700 1.000 73.84224  ?  120 LEU A HD13   1 
ATOM   1967 H HD21   . LEU A 1 120 ? 10.23000  -23.95300 24.02400 1.000 70.54964  ?  120 LEU A HD21   1 
ATOM   1968 H HD22   . LEU A 1 120 ? 10.74900  -24.55100 22.64700 1.000 70.54964  ?  120 LEU A HD22   1 
ATOM   1969 H HD23   . LEU A 1 120 ? 11.55100  -24.83500 23.98900 1.000 70.54964  ?  120 LEU A HD23   1 
ATOM   1970 N N      . ALA A 1 121 ? 16.28200  -23.30500 22.01000 1.000 52.70576  ?  121 ALA A N      1 
ATOM   1971 C CA     . ALA A 1 121 ? 17.45700  -23.54400 21.19100 1.000 50.53333  ?  121 ALA A CA     1 
ATOM   1972 C C      . ALA A 1 121 ? 18.28000  -24.69900 21.74100 1.000 46.07491  ?  121 ALA A C      1 
ATOM   1973 O O      . ALA A 1 121 ? 18.70600  -25.58100 20.98500 1.000 52.45597  ?  121 ALA A O      1 
ATOM   1974 C CB     . ALA A 1 121 ? 18.31500  -22.26800 21.10600 1.000 47.95282  ?  121 ALA A CB     1 
ATOM   1975 H H      . ALA A 1 121 ? 16.24200  -22.51900 22.35700 1.000 63.36469  ?  121 ALA A H      1 
ATOM   1976 H HA     . ALA A 1 121 ? 17.17100  -23.77300 20.29300 1.000 60.75777  ?  121 ALA A HA     1 
ATOM   1977 H HB1    . ALA A 1 121 ? 19.10900  -22.45600 20.58100 1.000 57.66115  ?  121 ALA A HB1    1 
ATOM   1978 H HB2    . ALA A 1 121 ? 17.79600  -21.56700 20.68200 1.000 57.66115  ?  121 ALA A HB2    1 
ATOM   1979 H HB3    . ALA A 1 121 ? 18.56700  -21.99700 22.00200 1.000 57.66115  ?  121 ALA A HB3    1 
ATOM   1980 N N      . ALA A 1 122 ? 18.48300  -24.73100 23.05700 1.000 48.53502  ?  122 ALA A N      1 
ATOM   1981 C CA     . ALA A 1 122 ? 19.30600  -25.79400 23.64100 1.000 52.57972  ?  122 ALA A CA     1 
ATOM   1982 C C      . ALA A 1 122 ? 18.67700  -27.16300 23.42000 1.000 57.75077  ?  122 ALA A C      1 
ATOM   1983 O O      . ALA A 1 122 ? 19.38900  -28.14900 23.16900 1.000 54.42818  ?  122 ALA A O      1 
ATOM   1984 C CB     . ALA A 1 122 ? 19.51300  -25.53900 25.13400 1.000 50.62915  ?  122 ALA A CB     1 
ATOM   1985 H H      . ALA A 1 122 ? 18.16600  -24.16500 23.62100 1.000 58.35980  ?  122 ALA A H      1 
ATOM   1986 H HA     . ALA A 1 122 ? 20.17500  -25.78600 23.21000 1.000 63.21343  ?  122 ALA A HA     1 
ATOM   1987 H HB1    . ALA A 1 122 ? 20.06500  -26.24700 25.50100 1.000 60.87275  ?  122 ALA A HB1    1 
ATOM   1988 H HB2    . ALA A 1 122 ? 19.95200  -24.68200 25.25000 1.000 60.87275  ?  122 ALA A HB2    1 
ATOM   1989 H HB3    . ALA A 1 122 ? 18.64900  -25.53000 25.57500 1.000 60.87275  ?  122 ALA A HB3    1 
ATOM   1990 N N      . GLU A 1 123 ? 17.34500  -27.25000 23.52200 1.000 54.95467  ?  123 GLU A N      1 
ATOM   1991 C CA     . GLU A 1 123 ? 16.66900  -28.52400 23.32500 1.000 56.90880  ?  123 GLU A CA     1 
ATOM   1992 C C      . GLU A 1 123 ? 16.86200  -29.04200 21.90300 1.000 53.94014  ?  123 GLU A C      1 
ATOM   1993 O O      . GLU A 1 123 ? 16.84700  -30.25700 21.68000 1.000 59.47957  ?  123 GLU A O      1 
ATOM   1994 C CB     . GLU A 1 123 ? 15.17500  -28.37900 23.62600 1.000 59.08211  ?  123 GLU A CB     1 
ATOM   1995 C CG     . GLU A 1 123 ? 14.82700  -28.45900 25.09500 1.000 71.65991  ?  123 GLU A CG     1 
ATOM   1996 C CD     . GLU A 1 123 ? 13.35200  -28.22100 25.34500 1.000 70.89577  ?  123 GLU A CD     1 
ATOM   1997 O OE1    . GLU A 1 123 ? 12.56900  -28.27200 24.37200 1.000 66.26314  ?  123 GLU A OE1    1 
ATOM   1998 O OE2    . GLU A 1 123 ? 12.97800  -27.97900 26.51200 1.000 85.54497  -1 123 GLU A OE2    1 
ATOM   1999 H H      . GLU A 1 123 ? 16.82200  -26.59200 23.70300 1.000 66.06337  ?  123 GLU A H      1 
ATOM   2000 H HA     . GLU A 1 123 ? 17.04200  -29.17300 23.94100 1.000 68.40834  ?  123 GLU A HA     1 
ATOM   2001 H HB2    . GLU A 1 123 ? 14.87500  -27.51600 23.30000 1.000 71.01630  ?  123 GLU A HB2    1 
ATOM   2002 H HB3    . GLU A 1 123 ? 14.69700  -29.09000 23.17100 1.000 71.01630  ?  123 GLU A HB3    1 
ATOM   2003 H HG2    . GLU A 1 123 ? 15.05200  -29.34200 25.42800 1.000 86.10966  ?  123 GLU A HG2    1 
ATOM   2004 H HG3    . GLU A 1 123 ? 15.32900  -27.78500 25.57900 1.000 86.10966  ?  123 GLU A HG3    1 
ATOM   2005 N N      . ALA A 1 124 ? 17.03100  -28.14400 20.93800 1.000 52.21461  ?  124 ALA A N      1 
ATOM   2006 C CA     . ALA A 1 124 ? 17.22100  -28.51800 19.54700 1.000 47.27163  ?  124 ALA A CA     1 
ATOM   2007 C C      . ALA A 1 124 ? 18.67600  -28.54700 19.13300 1.000 45.53422  ?  124 ALA A C      1 
ATOM   2008 O O      . ALA A 1 124 ? 18.96300  -28.75200 17.95300 1.000 50.01241  ?  124 ALA A O      1 
ATOM   2009 C CB     . ALA A 1 124 ? 16.45300  -27.55100 18.62900 1.000 52.35223  ?  124 ALA A CB     1 
ATOM   2010 H H      . ALA A 1 124 ? 17.03900  -27.29400 21.07100 1.000 62.77531  ?  124 ALA A H      1 
ATOM   2011 H HA     . ALA A 1 124 ? 16.85700  -29.40900 19.42000 1.000 56.84373  ?  124 ALA A HA     1 
ATOM   2012 H HB1    . ALA A 1 124 ? 16.59900  -27.81000 17.70500 1.000 62.94044  ?  124 ALA A HB1    1 
ATOM   2013 H HB2    . ALA A 1 124 ? 15.50800  -27.59800 18.84000 1.000 62.94044  ?  124 ALA A HB2    1 
ATOM   2014 H HB3    . ALA A 1 124 ? 16.78000  -26.65000 18.77500 1.000 62.94044  ?  124 ALA A HB3    1 
ATOM   2015 N N      . GLY A 1 125 ? 19.60200  -28.33900 20.07200 1.000 50.93464  ?  125 GLY A N      1 
ATOM   2016 C CA     . GLY A 1 125 ? 21.01800  -28.31800 19.74500 1.000 49.71613  ?  125 GLY A CA     1 
ATOM   2017 C C      . GLY A 1 125 ? 21.47800  -27.08100 19.00300 1.000 47.34945  ?  125 GLY A C      1 
ATOM   2018 O O      . GLY A 1 125 ? 22.45200  -27.15000 18.25300 1.000 48.14650  ?  125 GLY A O      1 
ATOM   2019 H H      . GLY A 1 125 ? 19.43100  -28.20900 20.90500 1.000 61.23933  ?  125 GLY A H      1 
ATOM   2020 H HA2    . GLY A 1 125 ? 21.52800  -28.37700 20.56800 1.000 59.77713  ?  125 GLY A HA2    1 
ATOM   2021 H HA3    . GLY A 1 125 ? 21.22100  -29.08800 19.19100 1.000 59.77713  ?  125 GLY A HA3    1 
ATOM   2022 N N      . VAL A 1 126 ? 20.81400  -25.93700 19.21300 1.000 47.66809  ?  126 VAL A N      1 
ATOM   2023 C CA     . VAL A 1 126 ? 21.09900  -24.71300 18.47600 1.000 44.43828  ?  126 VAL A CA     1 
ATOM   2024 C C      . VAL A 1 126 ? 21.94700  -23.79000 19.34400 1.000 48.17199  ?  126 VAL A C      1 
ATOM   2025 O O      . VAL A 1 126 ? 21.57900  -23.47000 20.48300 1.000 47.37262  ?  126 VAL A O      1 
ATOM   2026 C CB     . VAL A 1 126 ? 19.80100  -24.01200 18.04100 1.000 46.35204  ?  126 VAL A CB     1 
ATOM   2027 C CG1    . VAL A 1 126 ? 20.11700  -22.69100 17.32900 1.000 47.33367  ?  126 VAL A CG1    1 
ATOM   2028 C CG2    . VAL A 1 126 ? 18.97600  -24.91700 17.14400 1.000 45.40012  ?  126 VAL A CG2    1 
ATOM   2029 H H      . VAL A 1 126 ? 20.18300  -25.85000 19.79000 1.000 57.31948  ?  126 VAL A H      1 
ATOM   2030 H HA     . VAL A 1 126 ? 21.61200  -24.93600 17.68400 1.000 53.44371  ?  126 VAL A HA     1 
ATOM   2031 H HB     . VAL A 1 126 ? 19.27600  -23.81300 18.83200 1.000 55.74022  ?  126 VAL A HB     1 
ATOM   2032 H HG11   . VAL A 1 126 ? 19.31000  -22.36000 16.90400 1.000 56.91817  ?  126 VAL A HG11   1 
ATOM   2033 H HG12   . VAL A 1 126 ? 20.43400  -22.04700 17.98300 1.000 56.91817  ?  126 VAL A HG12   1 
ATOM   2034 H HG13   . VAL A 1 126 ? 20.80200  -22.84800 16.66100 1.000 56.91817  ?  126 VAL A HG13   1 
ATOM   2035 H HG21   . VAL A 1 126 ? 18.17500  -24.44400 16.86900 1.000 54.59791  ?  126 VAL A HG21   1 
ATOM   2036 H HG22   . VAL A 1 126 ? 19.50300  -25.15500 16.36500 1.000 54.59791  ?  126 VAL A HG22   1 
ATOM   2037 H HG23   . VAL A 1 126 ? 18.73500  -25.71700 17.63700 1.000 54.59791  ?  126 VAL A HG23   1 
ATOM   2038 N N      . GLU A 1 127 ? 23.08900  -23.36100 18.80100 1.000 49.02041  ?  127 GLU A N      1 
ATOM   2039 C CA     . GLU A 1 127 ? 23.91800  -22.36200 19.46400 1.000 52.61318  ?  127 GLU A CA     1 
ATOM   2040 C C      . GLU A 1 127 ? 23.28400  -20.97900 19.35200 1.000 42.05792  ?  127 GLU A C      1 
ATOM   2041 O O      . GLU A 1 127 ? 22.74600  -20.61600 18.31600 1.000 46.30526  ?  127 GLU A O      1 
ATOM   2042 C CB     . GLU A 1 127 ? 25.31500  -22.35100 18.83900 1.000 58.05325  ?  127 GLU A CB     1 
ATOM   2043 C CG     . GLU A 1 127 ? 26.18600  -21.17700 19.27000 1.000 63.65886  ?  127 GLU A CG     1 
ATOM   2044 C CD     . GLU A 1 127 ? 27.59700  -21.26000 18.70000 1.000 72.08493  ?  127 GLU A CD     1 
ATOM   2045 O OE1    . GLU A 1 127 ? 27.85600  -22.15600 17.86300 1.000 74.30991  ?  127 GLU A OE1    1 
ATOM   2046 O OE2    . GLU A 1 127 ? 28.43600  -20.42700 19.08800 1.000 87.73927  -1 127 GLU A OE2    1 
ATOM   2047 H H      . GLU A 1 127 ? 23.40300  -23.63400 18.04900 1.000 58.94226  ?  127 GLU A H      1 
ATOM   2048 H HA     . GLU A 1 127 ? 24.00300  -22.58000 20.40500 1.000 63.25359  ?  127 GLU A HA     1 
ATOM   2049 H HB2    . GLU A 1 127 ? 25.77500  -23.16600 19.09400 1.000 69.78167  ?  127 GLU A HB2    1 
ATOM   2050 H HB3    . GLU A 1 127 ? 25.22300  -22.31000 17.87500 1.000 69.78167  ?  127 GLU A HB3    1 
ATOM   2051 H HG2    . GLU A 1 127 ? 25.78300  -20.35200 18.95900 1.000 76.50840  ?  127 GLU A HG2    1 
ATOM   2052 H HG3    . GLU A 1 127 ? 26.25200  -21.17000 20.23800 1.000 76.50840  ?  127 GLU A HG3    1 
ATOM   2053 N N      . VAL A 1 128 ? 23.35900  -20.21000 20.43400 1.000 46.45109  ?  128 VAL A N      1 
ATOM   2054 C CA     . VAL A 1 128 ? 22.82400  -18.85900 20.48700 1.000 48.95698  ?  128 VAL A CA     1 
ATOM   2055 C C      . VAL A 1 128 ? 23.97600  -17.88800 20.70400 1.000 45.22871  ?  128 VAL A C      1 
ATOM   2056 O O      . VAL A 1 128 ? 24.79800  -18.08800 21.60100 1.000 47.87254  ?  128 VAL A O      1 
ATOM   2057 C CB     . VAL A 1 128 ? 21.76600  -18.70600 21.59400 1.000 51.33116  ?  128 VAL A CB     1 
ATOM   2058 C CG1    . VAL A 1 128 ? 21.12000  -17.32600 21.53700 1.000 53.14357  ?  128 VAL A CG1    1 
ATOM   2059 C CG2    . VAL A 1 128 ? 20.70100  -19.79000 21.46100 1.000 49.87120  ?  128 VAL A CG2    1 
ATOM   2060 H H      . VAL A 1 128 ? 23.72600  -20.45900 21.17000 1.000 55.85908  ?  128 VAL A H      1 
ATOM   2061 H HA     . VAL A 1 128 ? 22.40800  -18.65200 19.63600 1.000 58.86615  ?  128 VAL A HA     1 
ATOM   2062 H HB     . VAL A 1 128 ? 22.20100  -18.80200 22.45600 1.000 61.71516  ?  128 VAL A HB     1 
ATOM   2063 H HG11   . VAL A 1 128 ? 20.42700  -17.27300 22.21300 1.000 63.89005  ?  128 VAL A HG11   1 
ATOM   2064 H HG12   . VAL A 1 128 ? 21.79900  -16.65300 21.70500 1.000 63.89005  ?  128 VAL A HG12   1 
ATOM   2065 H HG13   . VAL A 1 128 ? 20.73500  -17.19400 20.65600 1.000 63.89005  ?  128 VAL A HG13   1 
ATOM   2066 H HG21   . VAL A 1 128 ? 20.00200  -19.62700 22.11300 1.000 59.96321  ?  128 VAL A HG21   1 
ATOM   2067 H HG22   . VAL A 1 128 ? 20.33100  -19.76100 20.56500 1.000 59.96321  ?  128 VAL A HG22   1 
ATOM   2068 H HG23   . VAL A 1 128 ? 21.10900  -20.65500 21.62300 1.000 59.96321  ?  128 VAL A HG23   1 
ATOM   2069 N N      . VAL A 1 129 ? 24.03700  -16.84800 19.86400 1.000 48.28367  ?  129 VAL A N      1 
ATOM   2070 C CA     . VAL A 1 129 ? 25.03800  -15.79000 19.95600 1.000 47.09182  ?  129 VAL A CA     1 
ATOM   2071 C C      . VAL A 1 129 ? 24.30300  -14.45400 20.00500 1.000 41.91867  ?  129 VAL A C      1 
ATOM   2072 O O      . VAL A 1 129 ? 23.52100  -14.15000 19.10700 1.000 45.82779  ?  129 VAL A O      1 
ATOM   2073 C CB     . VAL A 1 129 ? 26.01700  -15.82300 18.76800 1.000 45.63823  ?  129 VAL A CB     1 
ATOM   2074 C CG1    . VAL A 1 129 ? 27.00900  -14.66000 18.85800 1.000 45.43276  ?  129 VAL A CG1    1 
ATOM   2075 C CG2    . VAL A 1 129 ? 26.75300  -17.14700 18.71500 1.000 47.60713  ?  129 VAL A CG2    1 
ATOM   2076 H H      . VAL A 1 129 ? 23.48800  -16.73400 19.21200 1.000 58.05817  ?  129 VAL A H      1 
ATOM   2077 H HA     . VAL A 1 129 ? 25.54500  -15.89300 20.77700 1.000 56.62795  ?  129 VAL A HA     1 
ATOM   2078 H HB     . VAL A 1 129 ? 25.51000  -15.72800 17.94600 1.000 54.88365  ?  129 VAL A HB     1 
ATOM   2079 H HG11   . VAL A 1 129 ? 27.73300  -14.81400 18.23100 1.000 54.63708  ?  129 VAL A HG11   1 
ATOM   2080 H HG12   . VAL A 1 129 ? 26.55000  -13.83500 18.63800 1.000 54.63708  ?  129 VAL A HG12   1 
ATOM   2081 H HG13   . VAL A 1 129 ? 27.35900  -14.61300 19.76200 1.000 54.63708  ?  129 VAL A HG13   1 
ATOM   2082 H HG21   . VAL A 1 129 ? 27.34400  -17.14900 17.94600 1.000 57.24632  ?  129 VAL A HG21   1 
ATOM   2083 H HG22   . VAL A 1 129 ? 27.27000  -17.25300 19.52900 1.000 57.24632  ?  129 VAL A HG22   1 
ATOM   2084 H HG23   . VAL A 1 129 ? 26.10600  -17.86500 18.63700 1.000 57.24632  ?  129 VAL A HG23   1 
ATOM   2085 N N      . THR A 1 130 ? 24.55600  -13.66300 21.05300 1.000 46.26624  ?  130 THR A N      1 
ATOM   2086 C CA     . THR A 1 130 ? 23.85500  -12.39900 21.27800 1.000 45.20274  ?  130 THR A CA     1 
ATOM   2087 C C      . THR A 1 130 ? 24.82900  -11.26400 21.58500 1.000 48.29949  ?  130 THR A C      1 
ATOM   2088 O O      . THR A 1 130 ? 25.11500  -10.97200 22.75400 1.000 52.33371  ?  130 THR A O      1 
ATOM   2089 C CB     . THR A 1 130 ? 22.84000  -12.53900 22.42000 1.000 47.51462  ?  130 THR A CB     1 
ATOM   2090 O OG1    . THR A 1 130 ? 23.52200  -12.84100 23.63100 1.000 53.26166  ?  130 THR A OG1    1 
ATOM   2091 C CG2    . THR A 1 130 ? 21.84900  -13.64400 22.12800 1.000 48.63445  ?  130 THR A CG2    1 
ATOM   2092 H H      . THR A 1 130 ? 25.14100  -13.84300 21.65700 1.000 55.63725  ?  130 THR A H      1 
ATOM   2093 H HA     . THR A 1 130 ? 23.40800  -12.16900 20.44900 1.000 54.36105  ?  130 THR A HA     1 
ATOM   2094 H HB     . THR A 1 130 ? 22.35200  -11.70600 22.51500 1.000 57.13531  ?  130 THR A HB     1 
ATOM   2095 H HG1    . THR A 1 130 ? 23.18100  -12.41100 24.26700 1.000 64.03177  ?  130 THR A HG1    1 
ATOM   2096 H HG21   . THR A 1 130 ? 21.15100  -13.65000 22.80100 1.000 58.47911  ?  130 THR A HG21   1 
ATOM   2097 H HG22   . THR A 1 130 ? 21.44500  -13.50500 21.25700 1.000 58.47911  ?  130 THR A HG22   1 
ATOM   2098 H HG23   . THR A 1 130 ? 22.29900  -14.50300 22.13300 1.000 58.47911  ?  130 THR A HG23   1 
ATOM   2099 N N      . PRO A 1 131 ? 25.34500  -10.59000 20.56400 1.000 45.73581  ?  131 PRO A N      1 
ATOM   2100 C CA     . PRO A 1 131 ? 26.24800  -9.45800  20.80100 1.000 52.69649  ?  131 PRO A CA     1 
ATOM   2101 C C      . PRO A 1 131 ? 25.51200  -8.18300  21.20700 1.000 47.68440  ?  131 PRO A C      1 
ATOM   2102 O O      . PRO A 1 131 ? 24.31900  -8.00500  20.94300 1.000 45.37316  ?  131 PRO A O      1 
ATOM   2103 C CB     . PRO A 1 131 ? 26.96200  -9.26300  19.45300 1.000 55.95576  ?  131 PRO A CB     1 
ATOM   2104 C CG     . PRO A 1 131 ? 26.45000  -10.37700 18.53700 1.000 55.00584  ?  131 PRO A CG     1 
ATOM   2105 C CD     . PRO A 1 131 ? 25.16100  -10.86100 19.12000 1.000 46.77395  ?  131 PRO A CD     1 
ATOM   2106 H HA     . PRO A 1 131 ? 26.89100  -9.69300  21.48800 1.000 63.35356  ?  131 PRO A HA     1 
ATOM   2107 H HB2    . PRO A 1 131 ? 26.74000  -8.39100  19.09000 1.000 67.26469  ?  131 PRO A HB2    1 
ATOM   2108 H HB3    . PRO A 1 131 ? 27.92100  -9.33500  19.57800 1.000 67.26469  ?  131 PRO A HB3    1 
ATOM   2109 H HG2    . PRO A 1 131 ? 26.30700  -10.02200 17.64500 1.000 66.12478  ?  131 PRO A HG2    1 
ATOM   2110 H HG3    . PRO A 1 131 ? 27.10000  -11.09600 18.50700 1.000 66.12478  ?  131 PRO A HG3    1 
ATOM   2111 H HD2    . PRO A 1 131 ? 24.40900  -10.36300 18.76500 1.000 56.24651  ?  131 PRO A HD2    1 
ATOM   2112 H HD3    . PRO A 1 131 ? 25.03800  -11.80900 18.95600 1.000 56.24651  ?  131 PRO A HD3    1 
ATOM   2113 N N      . ILE A 1 132 ? 26.25800  -7.29100  21.84700 1.000 41.97156  ?  132 ILE A N      1 
ATOM   2114 C CA     . ILE A 1 132 ? 25.77700  -5.96900  22.23100 1.000 47.27714  ?  132 ILE A CA     1 
ATOM   2115 C C      . ILE A 1 132 ? 26.03700  -5.00000  21.08200 1.000 44.88393  ?  132 ILE A C      1 
ATOM   2116 O O      . ILE A 1 132 ? 27.19000  -4.77200  20.71400 1.000 47.53477  ?  132 ILE A O      1 
ATOM   2117 C CB     . ILE A 1 132 ? 26.47100  -5.47000  23.50800 1.000 56.25204  ?  132 ILE A CB     1 
ATOM   2118 C CG1    . ILE A 1 132 ? 26.36600  -6.49000  24.65400 1.000 54.72993  ?  132 ILE A CG1    1 
ATOM   2119 C CG2    . ILE A 1 132 ? 25.90800  -4.09700  23.91700 1.000 49.97007  ?  132 ILE A CG2    1 
ATOM   2120 C CD1    . ILE A 1 132 ? 24.98100  -6.99200  24.90700 1.000 63.47409  ?  132 ILE A CD1    1 
ATOM   2121 H H      . ILE A 1 132 ? 27.07400  -7.43200  22.07800 1.000 50.48364  ?  132 ILE A H      1 
ATOM   2122 H HA     . ILE A 1 132 ? 24.82100  -6.02200  22.38900 1.000 56.85034  ?  132 ILE A HA     1 
ATOM   2123 H HB     . ILE A 1 132 ? 27.41600  -5.36900  23.31200 1.000 67.62022  ?  132 ILE A HB     1 
ATOM   2124 H HG12   . ILE A 1 132 ? 26.92100  -7.25600  24.43800 1.000 65.79368  ?  132 ILE A HG12   1 
ATOM   2125 H HG13   . ILE A 1 132 ? 26.68100  -6.07200  25.47000 1.000 65.79368  ?  132 ILE A HG13   1 
ATOM   2126 H HG21   . ILE A 1 132 ? 26.24500  -3.86700  24.79700 1.000 60.08185  ?  132 ILE A HG21   1 
ATOM   2127 H HG22   . ILE A 1 132 ? 26.19300  -3.43300  23.27000 1.000 60.08185  ?  132 ILE A HG22   1 
ATOM   2128 H HG23   . ILE A 1 132 ? 24.93900  -4.14600  23.93600 1.000 60.08185  ?  132 ILE A HG23   1 
ATOM   2129 H HD11   . ILE A 1 132 ? 24.94700  -7.39500  25.78900 1.000 76.28668  ?  132 ILE A HD11   1 
ATOM   2130 H HD12   . ILE A 1 132 ? 24.36100  -6.24700  24.86000 1.000 76.28668  ?  132 ILE A HD12   1 
ATOM   2131 H HD13   . ILE A 1 132 ? 24.75600  -7.65300  24.23300 1.000 76.28668  ?  132 ILE A HD13   1 
ATOM   2132 N N      . SER A 1 133 ? 24.96700  -4.46400  20.48700 1.000 45.25011  ?  133 SER A N      1 
ATOM   2133 C CA     . SER A 1 133 ? 25.14000  -3.35100  19.54000 1.000 42.61257  ?  133 SER A CA     1 
ATOM   2134 C C      . SER A 1 133 ? 24.00400  -2.32500  19.56600 1.000 41.77730  ?  133 SER A C      1 
ATOM   2135 O O      . SER A 1 133 ? 24.02100  -1.41900  18.73400 1.000 38.58740  ?  133 SER A O      1 
ATOM   2136 C CB     . SER A 1 133 ? 25.30200  -3.90500  18.10700 1.000 39.91624  ?  133 SER A CB     1 
ATOM   2137 O OG     . SER A 1 133 ? 24.28800  -4.86500  17.80900 1.000 47.99228  ?  133 SER A OG     1 
ATOM   2138 H H      . SER A 1 133 ? 24.15400  -4.71600  20.60900 1.000 54.41791  ?  133 SER A H      1 
ATOM   2139 H HA     . SER A 1 133 ? 25.95400  -2.87900  19.77600 1.000 51.25285  ?  133 SER A HA     1 
ATOM   2140 H HB2    . SER A 1 133 ? 25.23500  -3.17000  17.47700 1.000 48.01726  ?  133 SER A HB2    1 
ATOM   2141 H HB3    . SER A 1 133 ? 26.17000  -4.33000  18.03000 1.000 48.01726  ?  133 SER A HB3    1 
ATOM   2142 H HG     . SER A 1 133 ? 24.41300  -5.18600  17.04300 1.000 57.70850  ?  133 SER A HG     1 
ATOM   2143 N N      . HIS A 1 134 ? 23.01400  -2.42900  20.45500 1.000 39.52013  ?  134 HIS A N      1 
ATOM   2144 C CA     . HIS A 1 134 ? 21.97400  -1.40100  20.50700 1.000 41.71044  ?  134 HIS A CA     1 
ATOM   2145 C C      . HIS A 1 134 ? 22.43500  -0.18800  21.31300 1.000 43.59127  ?  134 HIS A C      1 
ATOM   2146 O O      . HIS A 1 134 ? 22.03100  0.94300   21.01800 1.000 43.97776  ?  134 HIS A O      1 
ATOM   2147 C CB     . HIS A 1 134 ? 20.68200  -1.95900  21.11000 1.000 37.49637  ?  134 HIS A CB     1 
ATOM   2148 C CG     . HIS A 1 134 ? 19.54600  -0.97800  21.12800 1.000 37.96189  ?  134 HIS A CG     1 
ATOM   2149 N ND1    . HIS A 1 134 ? 18.96900  -0.47600  19.97700 1.000 40.73130  ?  134 HIS A ND1    1 
ATOM   2150 C CD2    . HIS A 1 134 ? 18.85800  -0.42600  22.15700 1.000 42.01552  ?  134 HIS A CD2    1 
ATOM   2151 C CE1    . HIS A 1 134 ? 17.99500  0.35300   20.29600 1.000 37.69958  ?  134 HIS A CE1    1 
ATOM   2152 N NE2    . HIS A 1 134 ? 17.90300  0.40200   21.61100 1.000 40.06512  ?  134 HIS A NE2    1 
ATOM   2153 H H      . HIS A 1 134 ? 22.92400  -3.06700  21.02300 1.000 47.54192  ?  134 HIS A H      1 
ATOM   2154 H HA     . HIS A 1 134 ? 21.77200  -1.12100  19.60100 1.000 50.17030  ?  134 HIS A HA     1 
ATOM   2155 H HB2    . HIS A 1 134 ? 20.40100  -2.72700  20.58900 1.000 45.11341  ?  134 HIS A HB2    1 
ATOM   2156 H HB3    . HIS A 1 134 ? 20.85600  -2.22700  22.02700 1.000 45.11341  ?  134 HIS A HB3    1 
ATOM   2157 H HD1    . HIS A 1 134 ? 19.20800  -0.67500  19.17500 1.000 48.99532  ?  134 HIS A HD1    1 
ATOM   2158 H HD2    . HIS A 1 134 ? 19.00400  -0.57800  23.06200 1.000 50.53640  ?  134 HIS A HD2    1 
ATOM   2159 H HE1    . HIS A 1 134 ? 17.46300  0.82400   19.69500 1.000 45.35726  ?  134 HIS A HE1    1 
ATOM   2160 N N      . THR A 1 135 ? 23.25000  -0.40800  22.32800 1.000 42.14124  ?  135 THR A N      1 
ATOM   2161 C CA     . THR A 1 135 ? 23.83100  0.66500   23.12600 1.000 44.40263  ?  135 THR A CA     1 
ATOM   2162 C C      . THR A 1 135 ? 25.28900  0.86900   22.72400 1.000 45.12929  ?  135 THR A C      1 
ATOM   2163 O O      . THR A 1 135 ? 25.89800  0.02500   22.05500 1.000 45.38032  ?  135 THR A O      1 
ATOM   2164 C CB     . THR A 1 135 ? 23.73000  0.33100   24.62000 1.000 42.26689  ?  135 THR A CB     1 
ATOM   2165 O OG1    . THR A 1 135 ? 24.27000  -0.98300  24.84500 1.000 44.43602  ?  135 THR A OG1    1 
ATOM   2166 C CG2    . THR A 1 135 ? 22.29000  0.37300   25.06800 1.000 49.33327  ?  135 THR A CG2    1 
ATOM   2167 H H      . THR A 1 135 ? 23.49200  -1.19200  22.58400 1.000 50.68726  ?  135 THR A H      1 
ATOM   2168 H HA     . THR A 1 135 ? 23.34700  1.49100   22.97000 1.000 53.40093  ?  135 THR A HA     1 
ATOM   2169 H HB     . THR A 1 135 ? 24.22800  0.97900   25.14200 1.000 50.83804  ?  135 THR A HB     1 
ATOM   2170 H HG1    . THR A 1 135 ? 24.19300  -1.19000  25.65600 1.000 53.44099  ?  135 THR A HG1    1 
ATOM   2171 H HG21   . THR A 1 135 ? 22.23000  0.16200   26.01300 1.000 59.31769  ?  135 THR A HG21   1 
ATOM   2172 H HG22   . THR A 1 135 ? 21.92300  1.25900   24.91900 1.000 59.31769  ?  135 THR A HG22   1 
ATOM   2173 H HG23   . THR A 1 135 ? 21.76800  -0.27300  24.56800 1.000 59.31769  ?  135 THR A HG23   1 
ATOM   2174 N N      . LEU A 1 136 ? 25.84300  2.00500   23.15300 1.000 41.82170  ?  136 LEU A N      1 
ATOM   2175 C CA     . LEU A 1 136 ? 27.26900  2.24900   22.91100 1.000 43.30421  ?  136 LEU A CA     1 
ATOM   2176 C C      . LEU A 1 136 ? 28.13600  1.21500   23.62200 1.000 46.83457  ?  136 LEU A C      1 
ATOM   2177 O O      . LEU A 1 136 ? 29.14000  0.74300   23.07100 1.000 46.03303  ?  136 LEU A O      1 
ATOM   2178 C CB     . LEU A 1 136 ? 27.64200  3.65200   23.37700 1.000 41.16776  ?  136 LEU A CB     1 
ATOM   2179 C CG     . LEU A 1 136 ? 27.08600  4.83700   22.59000 1.000 40.96813  ?  136 LEU A CG     1 
ATOM   2180 C CD1    . LEU A 1 136 ? 27.39400  6.11800   23.33500 1.000 41.86384  ?  136 LEU A CD1    1 
ATOM   2181 C CD2    . LEU A 1 136 ? 27.65200  4.87200   21.18200 1.000 40.92855  ?  136 LEU A CD2    1 
ATOM   2182 H H      . LEU A 1 136 ? 25.43100  2.63200   23.57300 1.000 50.30381  ?  136 LEU A H      1 
ATOM   2183 H HA     . LEU A 1 136 ? 27.43700  2.18600   21.95800 1.000 52.08283  ?  136 LEU A HA     1 
ATOM   2184 H HB2    . LEU A 1 136 ? 27.33100  3.75300   24.29000 1.000 49.51908  ?  136 LEU A HB2    1 
ATOM   2185 H HB3    . LEU A 1 136 ? 28.60900  3.72600   23.34500 1.000 49.51908  ?  136 LEU A HB3    1 
ATOM   2186 H HG     . LEU A 1 136 ? 26.12400  4.74900   22.50400 1.000 49.27953  ?  136 LEU A HG     1 
ATOM   2187 H HD11   . LEU A 1 136 ? 27.05000  6.87000   22.82800 1.000 50.35437  ?  136 LEU A HD11   1 
ATOM   2188 H HD12   . LEU A 1 136 ? 26.97000  6.08600   24.20700 1.000 50.35437  ?  136 LEU A HD12   1 
ATOM   2189 H HD13   . LEU A 1 136 ? 28.35500  6.20100   23.43800 1.000 50.35437  ?  136 LEU A HD13   1 
ATOM   2190 H HD21   . LEU A 1 136 ? 27.29600  5.64500   20.71700 1.000 49.23203  ?  136 LEU A HD21   1 
ATOM   2191 H HD22   . LEU A 1 136 ? 28.61900  4.93300   21.23200 1.000 49.23203  ?  136 LEU A HD22   1 
ATOM   2192 H HD23   . LEU A 1 136 ? 27.39600  4.05900   20.71800 1.000 49.23203  ?  136 LEU A HD23   1 
ATOM   2193 N N      . TYR A 1 137 ? 27.77800  0.87100   24.86300 1.000 45.71391  ?  137 TYR A N      1 
ATOM   2194 C CA     . TYR A 1 137 ? 28.60000  0.02800   25.70300 1.000 43.67770  ?  137 TYR A CA     1 
ATOM   2195 C C      . TYR A 1 137 ? 27.81300  -1.18900  26.17000 1.000 47.76409  ?  137 TYR A C      1 
ATOM   2196 O O      . TYR A 1 137 ? 26.57700  -1.20900  26.14000 1.000 44.69182  ?  137 TYR A O      1 
ATOM   2197 C CB     . TYR A 1 137 ? 29.10400  0.79200   26.94800 1.000 46.15489  ?  137 TYR A CB     1 
ATOM   2198 C CG     . TYR A 1 137 ? 30.01000  1.96700   26.66500 1.000 45.48229  ?  137 TYR A CG     1 
ATOM   2199 C CD1    . TYR A 1 137 ? 31.38400  1.79300   26.52700 1.000 47.82266  ?  137 TYR A CD1    1 
ATOM   2200 C CD2    . TYR A 1 137 ? 29.49600  3.26400   26.56200 1.000 44.66396  ?  137 TYR A CD2    1 
ATOM   2201 C CE1    . TYR A 1 137 ? 32.22100  2.86600   26.27900 1.000 43.91064  ?  137 TYR A CE1    1 
ATOM   2202 C CE2    . TYR A 1 137 ? 30.31600  4.34200   26.31000 1.000 42.28740  ?  137 TYR A CE2    1 
ATOM   2203 C CZ     . TYR A 1 137 ? 31.68400  4.14100   26.17000 1.000 46.02656  ?  137 TYR A CZ     1 
ATOM   2204 O OH     . TYR A 1 137 ? 32.51200  5.20300   25.93000 1.000 48.26582  ?  137 TYR A OH     1 
ATOM   2205 H H      . TYR A 1 137 ? 27.04700  1.12500   25.23900 1.000 54.97446  ?  137 TYR A H      1 
ATOM   2206 H HA     . TYR A 1 137 ? 29.36100  -0.27300  25.18300 1.000 52.53101  ?  137 TYR A HA     1 
ATOM   2207 H HB2    . TYR A 1 137 ? 28.33400  1.13000   27.43100 1.000 55.50364  ?  137 TYR A HB2    1 
ATOM   2208 H HB3    . TYR A 1 137 ? 29.59900  0.17200   27.50600 1.000 55.50364  ?  137 TYR A HB3    1 
ATOM   2209 H HD1    . TYR A 1 137 ? 31.74600  0.94000   26.60300 1.000 57.50496  ?  137 TYR A HD1    1 
ATOM   2210 H HD2    . TYR A 1 137 ? 28.58200  3.40200   26.66500 1.000 53.71452  ?  137 TYR A HD2    1 
ATOM   2211 H HE1    . TYR A 1 137 ? 33.13700  2.73400   26.18600 1.000 52.81054  ?  137 TYR A HE1    1 
ATOM   2212 H HE2    . TYR A 1 137 ? 29.95700  5.19700   26.23500 1.000 50.86265  ?  137 TYR A HE2    1 
ATOM   2213 H HH     . TYR A 1 137 ? 32.06700  5.91600   25.90900 1.000 58.03675  ?  137 TYR A HH     1 
ATOM   2214 N N      . ASP A 1 138 ? 28.54500  -2.19600  26.62000 1.000 46.22512  ?  138 ASP A N      1 
ATOM   2215 C CA     . ASP A 1 138 ? 27.96400  -3.29900  27.39400 1.000 57.00337  ?  138 ASP A CA     1 
ATOM   2216 C C      . ASP A 1 138 ? 27.53900  -2.72300  28.74300 1.000 55.59470  ?  138 ASP A C      1 
ATOM   2217 O O      . ASP A 1 138 ? 28.37500  -2.46100  29.61400 1.000 55.41460  ?  138 ASP A O      1 
ATOM   2218 C CB     . ASP A 1 138 ? 28.98000  -4.42700  27.55500 1.000 54.36444  ?  138 ASP A CB     1 
ATOM   2219 C CG     . ASP A 1 138 ? 28.41300  -5.63400  28.30800 1.000 55.15389  ?  138 ASP A CG     1 
ATOM   2220 O OD1    . ASP A 1 138 ? 27.41700  -5.49200  29.04900 1.000 53.75483  ?  138 ASP A OD1    1 
ATOM   2221 O OD2    . ASP A 1 138 ? 28.98700  -6.73900  28.16600 1.000 51.23777  -1 138 ASP A OD2    1 
ATOM   2222 H H      . ASP A 1 138 ? 29.39300  -2.27100  26.49200 1.000 55.58791  ?  138 ASP A H      1 
ATOM   2223 H HA     . ASP A 1 138 ? 27.18900  -3.66900  26.94300 1.000 68.52181  ?  138 ASP A HA     1 
ATOM   2224 H HB2    . ASP A 1 138 ? 29.26100  -4.72600  26.67600 1.000 65.35510  ?  138 ASP A HB2    1 
ATOM   2225 H HB3    . ASP A 1 138 ? 29.74400  -4.09500  28.05200 1.000 65.35510  ?  138 ASP A HB3    1 
ATOM   2226 N N      . THR A 1 139 ? 26.23500  -2.50900  28.91600 1.000 55.63512  ?  139 THR A N      1 
ATOM   2227 C CA     . THR A 1 139 ? 25.76200  -1.79300  30.09900 1.000 65.75905  ?  139 THR A CA     1 
ATOM   2228 C C      . THR A 1 139 ? 26.11300  -2.54400  31.37400 1.000 65.68043  ?  139 THR A C      1 
ATOM   2229 O O      . THR A 1 139 ? 26.44200  -1.93000  32.40100 1.000 56.86964  ?  139 THR A O      1 
ATOM   2230 C CB     . THR A 1 139 ? 24.24900  -1.56400  30.00400 1.000 75.92055  ?  139 THR A CB     1 
ATOM   2231 O OG1    . THR A 1 139 ? 23.57200  -2.82100  29.94100 1.000 81.38536  ?  139 THR A OG1    1 
ATOM   2232 C CG2    . THR A 1 139 ? 23.91200  -0.75800  28.75900 1.000 75.27245  ?  139 THR A CG2    1 
ATOM   2233 H H      . THR A 1 139 ? 25.61700  -2.76300  28.37500 1.000 66.87992  ?  139 THR A H      1 
ATOM   2234 H HA     . THR A 1 139 ? 26.19300  -0.92500  30.13400 1.000 79.02862  ?  139 THR A HA     1 
ATOM   2235 H HB     . THR A 1 139 ? 23.94900  -1.07400  30.78600 1.000 91.22243  ?  139 THR A HB     1 
ATOM   2236 H HG1    . THR A 1 139 ? 22.74300  -2.69800  29.89100 1.000 97.78020  ?  139 THR A HG1    1 
ATOM   2237 H HG21   . THR A 1 139 ? 22.95500  -0.60500  28.71200 1.000 90.44470  ?  139 THR A HG21   1 
ATOM   2238 H HG22   . THR A 1 139 ? 24.36600  0.09900   28.78500 1.000 90.44470  ?  139 THR A HG22   1 
ATOM   2239 H HG23   . THR A 1 139 ? 24.19300  -1.24000  27.96600 1.000 90.44470  ?  139 THR A HG23   1 
ATOM   2240 N N      . ASP A 1 140 ? 26.06500  -3.87700  31.32800 1.000 64.69888  ?  140 ASP A N      1 
ATOM   2241 C CA     . ASP A 1 140 ? 26.47400  -4.66900  32.48900 1.000 71.52820  ?  140 ASP A CA     1 
ATOM   2242 C C      . ASP A 1 140 ? 27.93700  -4.40900  32.84000 1.000 67.80387  ?  140 ASP A C      1 
ATOM   2243 O O      . ASP A 1 140 ? 28.29400  -4.31300  34.01900 1.000 63.56139  ?  140 ASP A O      1 
ATOM   2244 C CB     . ASP A 1 140 ? 26.23900  -6.15500  32.21100 1.000 70.88688  ?  140 ASP A CB     1 
ATOM   2245 C CG     . ASP A 1 140 ? 24.78700  -6.56400  32.41200 1.000 82.50903  ?  140 ASP A CG     1 
ATOM   2246 O OD1    . ASP A 1 140 ? 24.01200  -5.78500  33.01000 1.000 69.46016  ?  140 ASP A OD1    1 
ATOM   2247 O OD2    . ASP A 1 140 ? 24.41300  -7.66600  31.95900 1.000 86.50593  -1 140 ASP A OD2    1 
ATOM   2248 H H      . ASP A 1 140 ? 25.80500  -4.33900  30.65100 1.000 77.75642  ?  140 ASP A H      1 
ATOM   2249 H HA     . ASP A 1 140 ? 25.93300  -4.41600  33.25300 1.000 85.95160  ?  140 ASP A HA     1 
ATOM   2250 H HB2    . ASP A 1 140 ? 26.48200  -6.34800  31.29200 1.000 85.18203  ?  140 ASP A HB2    1 
ATOM   2251 H HB3    . ASP A 1 140 ? 26.78600  -6.68000  32.81700 1.000 85.18203  ?  140 ASP A HB3    1 
ATOM   2252 N N      . MET A 1 141 ? 28.79800  -4.29500  31.82600 1.000 59.15474  ?  141 MET A N      1 
ATOM   2253 C CA     . MET A 1 141 ? 30.20200  -3.99900  32.07100 1.000 64.26758  ?  141 MET A CA     1 
ATOM   2254 C C      . MET A 1 141 ? 30.36800  -2.63900  32.74200 1.000 65.28628  ?  141 MET A C      1 
ATOM   2255 O O      . MET A 1 141 ? 31.18600  -2.48000  33.66200 1.000 63.61954  ?  141 MET A O      1 
ATOM   2256 C CB     . MET A 1 141 ? 30.97900  -4.04700  30.75400 1.000 63.66513  ?  141 MET A CB     1 
ATOM   2257 C CG     . MET A 1 141 ? 32.46700  -3.79200  30.89200 1.000 84.47336  ?  141 MET A CG     1 
ATOM   2258 S SD     . MET A 1 141 ? 32.93800  -2.08900  30.49600 1.000 72.50969  ?  141 MET A SD     1 
ATOM   2259 C CE     . MET A 1 141 ? 32.74000  -2.08500  28.71300 1.000 88.15100  ?  141 MET A CE     1 
ATOM   2260 H H      . MET A 1 141 ? 28.59300  -4.38400  30.99500 1.000 71.10345  ?  141 MET A H      1 
ATOM   2261 H HA     . MET A 1 141 ? 30.56600  -4.68000  32.65800 1.000 77.23886  ?  141 MET A HA     1 
ATOM   2262 H HB2    . MET A 1 141 ? 30.86800  -4.92800  30.36200 1.000 76.51592  ?  141 MET A HB2    1 
ATOM   2263 H HB3    . MET A 1 141 ? 30.62000  -3.37100  30.15800 1.000 76.51592  ?  141 MET A HB3    1 
ATOM   2264 H HG2    . MET A 1 141 ? 32.73300  -3.96900  31.80800 1.000 101.48580 ?  141 MET A HG2    1 
ATOM   2265 H HG3    . MET A 1 141 ? 32.94500  -4.38100  30.28800 1.000 101.48580 ?  141 MET A HG3    1 
ATOM   2266 H HE1    . MET A 1 141 ? 32.98400  -1.21100  28.37000 1.000 105.89897 ?  141 MET A HE1    1 
ATOM   2267 H HE2    . MET A 1 141 ? 33.31700  -2.76400  28.33000 1.000 105.89897 ?  141 MET A HE2    1 
ATOM   2268 H HE3    . MET A 1 141 ? 31.81400  -2.27800  28.49800 1.000 105.89897 ?  141 MET A HE3    1 
ATOM   2269 N N      . LEU A 1 142 ? 29.60600  -1.63800  32.29400 1.000 64.20892  ?  142 LEU A N      1 
ATOM   2270 C CA     . LEU A 1 142 ? 29.69600  -0.31900  32.91400 1.000 64.03068  ?  142 LEU A CA     1 
ATOM   2271 C C      . LEU A 1 142 ? 29.35300  -0.39100  34.40300 1.000 66.09057  ?  142 LEU A C      1 
ATOM   2272 O O      . LEU A 1 142 ? 30.04300  0.20900   35.23800 1.000 62.66991  ?  142 LEU A O      1 
ATOM   2273 C CB     . LEU A 1 142 ? 28.76300  0.66100   32.20500 1.000 61.68950  ?  142 LEU A CB     1 
ATOM   2274 C CG     . LEU A 1 142 ? 29.14100  1.12500   30.80000 1.000 63.86787  ?  142 LEU A CG     1 
ATOM   2275 C CD1    . LEU A 1 142 ? 28.11000  2.14800   30.30800 1.000 53.14412  ?  142 LEU A CD1    1 
ATOM   2276 C CD2    . LEU A 1 142 ? 30.54000  1.71300   30.75200 1.000 63.37673  ?  142 LEU A CD2    1 
ATOM   2277 H H      . LEU A 1 142 ? 29.04100  -1.69600  31.64800 1.000 77.16848  ?  142 LEU A H      1 
ATOM   2278 H HA     . LEU A 1 142 ? 30.60400  0.00800   32.82300 1.000 76.95458  ?  142 LEU A HA     1 
ATOM   2279 H HB2    . LEU A 1 142 ? 27.89200  0.23800   32.13300 1.000 74.14517  ?  142 LEU A HB2    1 
ATOM   2280 H HB3    . LEU A 1 142 ? 28.70100  1.45800   32.75400 1.000 74.14517  ?  142 LEU A HB3    1 
ATOM   2281 H HG     . LEU A 1 142 ? 29.14200  0.35800   30.20600 1.000 76.75921  ?  142 LEU A HG     1 
ATOM   2282 H HD11   . LEU A 1 142 ? 28.37700  2.47000   29.43300 1.000 63.89071  ?  142 LEU A HD11   1 
ATOM   2283 H HD12   . LEU A 1 142 ? 27.24200  1.71900   30.25200 1.000 63.89071  ?  142 LEU A HD12   1 
ATOM   2284 H HD13   . LEU A 1 142 ? 28.07400  2.88700   30.93600 1.000 63.89071  ?  142 LEU A HD13   1 
ATOM   2285 H HD21   . LEU A 1 142 ? 30.68600  2.11000   29.87900 1.000 76.16985  ?  142 LEU A HD21   1 
ATOM   2286 H HD22   . LEU A 1 142 ? 30.62100  2.39100   31.44100 1.000 76.16985  ?  142 LEU A HD22   1 
ATOM   2287 H HD23   . LEU A 1 142 ? 31.18500  1.00600   30.90700 1.000 76.16985  ?  142 LEU A HD23   1 
ATOM   2288 N N      . VAL A 1 143 ? 28.28600  -1.11800  34.74600 1.000 59.72968  ?  143 VAL A N      1 
ATOM   2289 C CA     . VAL A 1 143 ? 27.86500  -1.22100  36.13900 1.000 65.51221  ?  143 VAL A CA     1 
ATOM   2290 C C      . VAL A 1 143 ? 28.93800  -1.91100  36.97300 1.000 65.92429  ?  143 VAL A C      1 
ATOM   2291 O O      . VAL A 1 143 ? 29.21100  -1.51300  38.10900 1.000 68.35268  ?  143 VAL A O      1 
ATOM   2292 C CB     . VAL A 1 143 ? 26.51400  -1.95800  36.22600 1.000 62.99722  ?  143 VAL A CB     1 
ATOM   2293 C CG1    . VAL A 1 143 ? 26.25600  -2.43200  37.64800 1.000 71.16500  ?  143 VAL A CG1    1 
ATOM   2294 C CG2    . VAL A 1 143 ? 25.39500  -1.05300  35.74700 1.000 62.28548  ?  143 VAL A CG2    1 
ATOM   2295 H H      . VAL A 1 143 ? 27.79500  -1.55800  34.19300 1.000 71.79338  ?  143 VAL A H      1 
ATOM   2296 H HA     . VAL A 1 143 ? 27.74700  -0.32700  36.49500 1.000 78.73242  ?  143 VAL A HA     1 
ATOM   2297 H HB     . VAL A 1 143 ? 26.53900  -2.73900  35.65200 1.000 75.71444  ?  143 VAL A HB     1 
ATOM   2298 H HG11   . VAL A 1 143 ? 25.31700  -2.66000  37.73900 1.000 85.51577  ?  143 VAL A HG11   1 
ATOM   2299 H HG12   . VAL A 1 143 ? 26.80400  -3.21300  37.82400 1.000 85.51577  ?  143 VAL A HG12   1 
ATOM   2300 H HG13   . VAL A 1 143 ? 26.48600  -1.72000  38.26500 1.000 85.51577  ?  143 VAL A HG13   1 
ATOM   2301 H HG21   . VAL A 1 143 ? 24.55200  -1.38300  36.09400 1.000 74.86035  ?  143 VAL A HG21   1 
ATOM   2302 H HG22   . VAL A 1 143 ? 25.55700  -0.15300  36.07100 1.000 74.86035  ?  143 VAL A HG22   1 
ATOM   2303 H HG23   . VAL A 1 143 ? 25.37900  -1.05700  34.77700 1.000 74.86035  ?  143 VAL A HG23   1 
ATOM   2304 N N      . ALA A 1 144 ? 29.54800  -2.96600  36.43000 1.000 63.68711  ?  144 ALA A N      1 
ATOM   2305 C CA     . ALA A 1 144 ? 30.60100  -3.66900  37.15200 1.000 58.35051  ?  144 ALA A CA     1 
ATOM   2306 C C      . ALA A 1 144 ? 31.79500  -2.75700  37.41900 1.000 67.50493  ?  144 ALA A C      1 
ATOM   2307 O O      . ALA A 1 144 ? 32.35100  -2.75700  38.52400 1.000 67.78395  ?  144 ALA A O      1 
ATOM   2308 C CB     . ALA A 1 144 ? 31.03600  -4.90100  36.36500 1.000 61.65584  ?  144 ALA A CB     1 
ATOM   2309 H H      . ALA A 1 144 ? 29.37100  -3.29100  35.65400 1.000 76.54230  ?  144 ALA A H      1 
ATOM   2310 H HA     . ALA A 1 144 ? 30.25100  -3.96200  38.00800 1.000 70.13838  ?  144 ALA A HA     1 
ATOM   2311 H HB1    . ALA A 1 144 ? 31.73500  -5.36000  36.85700 1.000 74.10478  ?  144 ALA A HB1    1 
ATOM   2312 H HB2    . ALA A 1 144 ? 30.27300  -5.48700  36.24800 1.000 74.10478  ?  144 ALA A HB2    1 
ATOM   2313 H HB3    . ALA A 1 144 ? 31.37200  -4.61900  35.49900 1.000 74.10478  ?  144 ALA A HB3    1 
ATOM   2314 N N      . ARG A 1 145 ? 32.19900  -1.96900  36.42200 1.000 69.52321  ?  145 ARG A N      1 
ATOM   2315 C CA     . ARG A 1 145 ? 33.33600  -1.07100  36.60300 1.000 76.10355  ?  145 ARG A CA     1 
ATOM   2316 C C      . ARG A 1 145 ? 33.01000  0.09500   37.52600 1.000 75.40090  ?  145 ARG A C      1 
ATOM   2317 O O      . ARG A 1 145 ? 33.92800  0.73600   38.03700 1.000 76.83404  ?  145 ARG A O      1 
ATOM   2318 C CB     . ARG A 1 145 ? 33.81900  -0.54300  35.25200 1.000 77.75054  ?  145 ARG A CB     1 
ATOM   2319 C CG     . ARG A 1 145 ? 35.19000  -1.07000  34.86200 1.000 95.58593  ?  145 ARG A CG     1 
ATOM   2320 C CD     . ARG A 1 145 ? 35.36800  -1.12100  33.35500 1.000 93.01381  ?  145 ARG A CD     1 
ATOM   2321 N NE     . ARG A 1 145 ? 36.72900  -1.50000  32.99000 1.000 111.63609 ?  145 ARG A NE     1 
ATOM   2322 C CZ     . ARG A 1 145 ? 37.74400  -0.65000  32.88000 1.000 103.49973 ?  145 ARG A CZ     1 
ATOM   2323 N NH1    . ARG A 1 145 ? 37.58700  0.64500   33.09800 1.000 93.05584  ?  145 ARG A NH1    1 
ATOM   2324 N NH2    . ARG A 1 145 ? 38.94900  -1.11500  32.54700 1.000 104.27869 ?  145 ARG A NH2    1 
ATOM   2325 H H      . ARG A 1 145 ? 31.83700  -1.93600  35.64300 1.000 83.54563  ?  145 ARG A H      1 
ATOM   2326 H HA     . ARG A 1 145 ? 34.06300  -1.57400  37.00100 1.000 91.44203  ?  145 ARG A HA     1 
ATOM   2327 H HB2    . ARG A 1 145 ? 33.18800  -0.81300  34.56500 1.000 93.41842  ?  145 ARG A HB2    1 
ATOM   2328 H HB3    . ARG A 1 145 ? 33.87000  0.42500   35.29200 1.000 93.41842  ?  145 ARG A HB3    1 
ATOM   2329 H HG2    . ARG A 1 145 ? 35.87300  -0.48600  35.22900 1.000 114.82089 ?  145 ARG A HG2    1 
ATOM   2330 H HG3    . ARG A 1 145 ? 35.29900  -1.96800  35.21200 1.000 114.82089 ?  145 ARG A HG3    1 
ATOM   2331 H HD2    . ARG A 1 145 ? 34.75800  -1.77700  32.98200 1.000 111.73434 ?  145 ARG A HD2    1 
ATOM   2332 H HD3    . ARG A 1 145 ? 35.18400  -0.24600  32.98000 1.000 111.73434 ?  145 ARG A HD3    1 
ATOM   2333 H HE     . ARG A 1 145 ? 36.88500  -2.33200  32.83500 1.000 134.08107 ?  145 ARG A HE     1 
ATOM   2334 H HH11   . ARG A 1 145 ? 36.81400  0.95400   33.31600 1.000 111.78477 ?  145 ARG A HH11   1 
ATOM   2335 H HH12   . ARG A 1 145 ? 38.25700  1.17900   33.02200 1.000 111.78477 ?  145 ARG A HH12   1 
ATOM   2336 H HH21   . ARG A 1 145 ? 39.06100  -1.95500  32.40700 1.000 125.25220 ?  145 ARG A HH21   1 
ATOM   2337 H HH22   . ARG A 1 145 ? 39.61300  -0.57400  32.47400 1.000 125.25220 ?  145 ARG A HH22   1 
ATOM   2338 N N      . ASN A 1 146 ? 31.72700  0.38200   37.74600 1.000 74.71838  ?  146 ASN A N      1 
ATOM   2339 C CA     . ASN A 1 146 ? 31.30200  1.35200   38.74100 1.000 77.09821  ?  146 ASN A CA     1 
ATOM   2340 C C      . ASN A 1 146 ? 31.08200  0.71800   40.11100 1.000 79.87859  ?  146 ASN A C      1 
ATOM   2341 O O      . ASN A 1 146 ? 30.35900  1.28400   40.93700 1.000 80.57064  ?  146 ASN A O      1 
ATOM   2342 C CB     . ASN A 1 146 ? 30.02300  2.05700   38.28100 1.000 74.48787  ?  146 ASN A CB     1 
ATOM   2343 C CG     . ASN A 1 146 ? 29.82400  3.40500   38.95600 1.000 76.03377  ?  146 ASN A CG     1 
ATOM   2344 O OD1    . ASN A 1 146 ? 30.69600  4.27400   38.90700 1.000 78.53406  ?  146 ASN A OD1    1 
ATOM   2345 N ND2    . ASN A 1 146 ? 28.67400  3.58400   39.59600 1.000 69.44961  ?  146 ASN A ND2    1 
ATOM   2346 H H      . ASN A 1 146 ? 31.07500  0.01700   37.32100 1.000 89.77983  ?  146 ASN A H      1 
ATOM   2347 H HA     . ASN A 1 146 ? 31.99600  2.02400   38.82800 1.000 92.63562  ?  146 ASN A HA     1 
ATOM   2348 H HB2    . ASN A 1 146 ? 30.07000  2.20400   37.32300 1.000 89.50322  ?  146 ASN A HB2    1 
ATOM   2349 H HB3    . ASN A 1 146 ? 29.25900  1.49800   38.49400 1.000 89.50322  ?  146 ASN A HB3    1 
ATOM   2350 H HD21   . ASN A 1 146 ? 28.08800  2.95400   39.61300 1.000 83.45730  ?  146 ASN A HD21   1 
ATOM   2351 H HD22   . ASN A 1 146 ? 28.51400  4.32900   39.99400 1.000 83.45730  ?  146 ASN A HD22   1 
ATOM   2352 N N      . GLY A 1 147 ? 31.67900  -0.44600  40.36200 1.000 78.96430  ?  147 GLY A N      1 
ATOM   2353 C CA     . GLY A 1 147 ? 31.55600  -1.11100  41.63900 1.000 80.02782  ?  147 GLY A CA     1 
ATOM   2354 C C      . GLY A 1 147 ? 30.31900  -1.95900  41.81500 1.000 76.97550  ?  147 GLY A C      1 
ATOM   2355 O O      . GLY A 1 147 ? 30.13800  -2.53800  42.89300 1.000 81.64021  ?  147 GLY A O      1 
ATOM   2356 H H      . GLY A 1 147 ? 32.16600  -0.87100  39.79400 1.000 94.87493  ?  147 GLY A H      1 
ATOM   2357 H HA2    . GLY A 1 147 ? 32.32600  -1.68700  41.76100 1.000 96.15116  ?  147 GLY A HA2    1 
ATOM   2358 H HA3    . GLY A 1 147 ? 31.55100  -0.43700  42.33700 1.000 96.15116  ?  147 GLY A HA3    1 
ATOM   2359 N N      . GLY A 1 148 ? 29.46100  -2.05400  40.79900 1.000 78.86371  ?  148 GLY A N      1 
ATOM   2360 C CA     . GLY A 1 148 ? 28.25900  -2.86200  40.87400 1.000 78.19669  ?  148 GLY A CA     1 
ATOM   2361 C C      . GLY A 1 148 ? 26.97000  -2.08000  40.95800 1.000 76.84559  ?  148 GLY A C      1 
ATOM   2362 O O      . GLY A 1 148 ? 25.90100  -2.69200  41.10100 1.000 80.73505  ?  148 GLY A O      1 
ATOM   2363 H H      . GLY A 1 148 ? 29.56100  -1.65100  40.04600 1.000 94.75422  ?  148 GLY A H      1 
ATOM   2364 H HA2    . GLY A 1 148 ? 28.21300  -3.42300  40.08400 1.000 93.95379  ?  148 GLY A HA2    1 
ATOM   2365 H HA3    . GLY A 1 148 ? 28.31400  -3.42800  41.66000 1.000 93.95379  ?  148 GLY A HA3    1 
ATOM   2366 N N      . ALA A 1 149 ? 27.02500  -0.75700  40.87300 1.000 78.65795  ?  149 ALA A N      1 
ATOM   2367 C CA     . ALA A 1 149 ? 25.83500  0.08700   40.88800 1.000 76.59511  ?  149 ALA A CA     1 
ATOM   2368 C C      . ALA A 1 149 ? 25.91700  1.08800   39.74800 1.000 69.33294  ?  149 ALA A C      1 
ATOM   2369 O O      . ALA A 1 149 ? 26.98700  1.63200   39.46600 1.000 65.51333  ?  149 ALA A O      1 
ATOM   2370 C CB     . ALA A 1 149 ? 25.69200  0.83500   42.22300 1.000 77.94887  ?  149 ALA A CB     1 
ATOM   2371 H H      . ALA A 1 149 ? 27.75800  -0.31300  40.80500 1.000 94.50731  ?  149 ALA A H      1 
ATOM   2372 H HA     . ALA A 1 149 ? 25.04600  -0.46300  40.76300 1.000 92.03190  ?  149 ALA A HA     1 
ATOM   2373 H HB1    . ALA A 1 149 ? 24.89400  1.38500   42.19300 1.000 93.65641  ?  149 ALA A HB1    1 
ATOM   2374 H HB2    . ALA A 1 149 ? 25.62000  0.18700   42.94200 1.000 93.65641  ?  149 ALA A HB2    1 
ATOM   2375 H HB3    . ALA A 1 149 ? 26.47400  1.39200   42.35800 1.000 93.65641  ?  149 ALA A HB3    1 
ATOM   2376 N N      . ALA A 1 150 ? 24.79100  1.31600   39.08700 1.000 68.88214  ?  150 ALA A N      1 
ATOM   2377 C CA     . ALA A 1 150 ? 24.75700  2.31500   38.02900 1.000 72.53234  ?  150 ALA A CA     1 
ATOM   2378 C C      . ALA A 1 150 ? 24.90300  3.70800   38.63200 1.000 66.62026  ?  150 ALA A C      1 
ATOM   2379 O O      . ALA A 1 150 ? 24.28900  4.00600   39.66000 1.000 60.69113  ?  150 ALA A O      1 
ATOM   2380 C CB     . ALA A 1 150 ? 23.44900  2.22000   37.24200 1.000 70.49084  ?  150 ALA A CB     1 
ATOM   2381 H H      . ALA A 1 150 ? 24.04400  0.91400   39.22900 1.000 82.77634  ?  150 ALA A H      1 
ATOM   2382 H HA     . ALA A 1 150 ? 25.49000  2.16500   37.41100 1.000 87.15657  ?  150 ALA A HA     1 
ATOM   2383 H HB1    . ALA A 1 150 ? 23.43900  2.91100   36.56100 1.000 84.70678  ?  150 ALA A HB1    1 
ATOM   2384 H HB2    . ALA A 1 150 ? 23.39400  1.34500   36.82600 1.000 84.70678  ?  150 ALA A HB2    1 
ATOM   2385 H HB3    . ALA A 1 150 ? 22.70400  2.34400   37.85100 1.000 84.70678  ?  150 ALA A HB3    1 
ATOM   2386 N N      . PRO A 1 151 ? 25.71100  4.58000   38.02800 1.000 71.91439  ?  151 PRO A N      1 
ATOM   2387 C CA     . PRO A 1 151 ? 25.79900  5.96100   38.53100 1.000 68.09182  ?  151 PRO A CA     1 
ATOM   2388 C C      . PRO A 1 151 ? 24.46500  6.67100   38.36500 1.000 70.30501  ?  151 PRO A C      1 
ATOM   2389 O O      . PRO A 1 151 ? 23.70000  6.40000   37.42800 1.000 68.84033  ?  151 PRO A O      1 
ATOM   2390 C CB     . PRO A 1 151 ? 26.89700  6.59600   37.66300 1.000 78.76646  ?  151 PRO A CB     1 
ATOM   2391 C CG     . PRO A 1 151 ? 26.94400  5.76200   36.41400 1.000 72.49272  ?  151 PRO A CG     1 
ATOM   2392 C CD     . PRO A 1 151 ? 26.52100  4.37100   36.80700 1.000 70.03983  ?  151 PRO A CD     1 
ATOM   2393 H HA     . PRO A 1 151 ? 26.07600  5.98400   39.46000 1.000 81.82795  ?  151 PRO A HA     1 
ATOM   2394 H HB2    . PRO A 1 151 ? 26.66500  7.51500   37.45700 1.000 94.63752  ?  151 PRO A HB2    1 
ATOM   2395 H HB3    . PRO A 1 151 ? 27.74600  6.56500   38.13200 1.000 94.63752  ?  151 PRO A HB3    1 
ATOM   2396 H HG2    . PRO A 1 151 ? 26.33400  6.13000   35.75500 1.000 87.10904  ?  151 PRO A HG2    1 
ATOM   2397 H HG3    . PRO A 1 151 ? 27.84800  5.75600   36.06200 1.000 87.10904  ?  151 PRO A HG3    1 
ATOM   2398 H HD2    . PRO A 1 151 ? 25.98800  3.96300   36.10600 1.000 84.16557  ?  151 PRO A HD2    1 
ATOM   2399 H HD3    . PRO A 1 151 ? 27.29500  3.81800   36.99900 1.000 84.16557  ?  151 PRO A HD3    1 
ATOM   2400 N N      . LEU A 1 152 ? 24.18700  7.59200   39.28500 1.000 69.40679  ?  152 LEU A N      1 
ATOM   2401 C CA     . LEU A 1 152 ? 22.86200  8.19800   39.39100 1.000 77.20278  ?  152 LEU A CA     1 
ATOM   2402 C C      . LEU A 1 152 ? 22.79400  9.64800   38.91500 1.000 75.69507  ?  152 LEU A C      1 
ATOM   2403 O O      . LEU A 1 152 ? 21.70000  10.22500  38.90600 1.000 63.14529  ?  152 LEU A O      1 
ATOM   2404 C CB     . LEU A 1 152 ? 22.37500  8.11000   40.84100 1.000 80.60874  ?  152 LEU A CB     1 
ATOM   2405 C CG     . LEU A 1 152 ? 22.27700  6.68100   41.38900 1.000 83.54313  ?  152 LEU A CG     1 
ATOM   2406 C CD1    . LEU A 1 152 ? 22.13900  6.69300   42.90600 1.000 82.43955  ?  152 LEU A CD1    1 
ATOM   2407 C CD2    . LEU A 1 152 ? 21.12200  5.92300   40.74000 1.000 85.84082  ?  152 LEU A CD2    1 
ATOM   2408 H H      . LEU A 1 152 ? 24.75300  7.88400   39.86300 1.000 83.40592  ?  152 LEU A H      1 
ATOM   2409 H HA     . LEU A 1 152 ? 22.25600  7.69500   38.82600 1.000 92.76111  ?  152 LEU A HA     1 
ATOM   2410 H HB2    . LEU A 1 152 ? 22.99400  8.59900   41.40500 1.000 96.84826  ?  152 LEU A HB2    1 
ATOM   2411 H HB3    . LEU A 1 152 ? 21.49200  8.50700   40.89500 1.000 96.84826  ?  152 LEU A HB3    1 
ATOM   2412 H HG     . LEU A 1 152 ? 23.09400  6.20700   41.17000 1.000 100.36952 ?  152 LEU A HG     1 
ATOM   2413 H HD11   . LEU A 1 152 ? 22.07900  5.77900   43.22600 1.000 99.04523  ?  152 LEU A HD11   1 
ATOM   2414 H HD12   . LEU A 1 152 ? 22.91800  7.12700   43.29000 1.000 99.04523  ?  152 LEU A HD12   1 
ATOM   2415 H HD13   . LEU A 1 152 ? 21.33700  7.18200   43.14700 1.000 99.04523  ?  152 LEU A HD13   1 
ATOM   2416 H HD21   . LEU A 1 152 ? 21.06500  5.03700   41.13100 1.000 103.12675 ?  152 LEU A HD21   1 
ATOM   2417 H HD22   . LEU A 1 152 ? 20.29700  6.40800   40.89800 1.000 103.12675 ?  152 LEU A HD22   1 
ATOM   2418 H HD23   . LEU A 1 152 ? 21.28600  5.85300   39.78600 1.000 103.12675 ?  152 LEU A HD23   1 
ATOM   2419 N N      . THR A 1 153 ? 23.91500  10.25000  38.50600 1.000 69.39034  ?  153 THR A N      1 
ATOM   2420 C CA     . THR A 1 153 ? 23.90500  11.58800  37.94700 1.000 70.10956  ?  153 THR A CA     1 
ATOM   2421 C C      . THR A 1 153 ? 24.57600  11.57300  36.57800 1.000 65.88743  ?  153 THR A C      1 
ATOM   2422 O O      . THR A 1 153 ? 25.44400  10.74000  36.30100 1.000 62.58552  ?  153 THR A O      1 
ATOM   2423 C CB     . THR A 1 153 ? 24.61900  12.61100  38.84200 1.000 65.30545  ?  153 THR A CB     1 
ATOM   2424 O OG1    . THR A 1 153 ? 26.04000  12.46500  38.70500 1.000 69.10466  ?  153 THR A OG1    1 
ATOM   2425 C CG2    . THR A 1 153 ? 24.22200  12.43800  40.30000 1.000 68.83456  ?  153 THR A CG2    1 
ATOM   2426 H H      . THR A 1 153 ? 24.69600  9.89300   38.54600 1.000 83.38617  ?  153 THR A H      1 
ATOM   2427 H HA     . THR A 1 153 ? 22.98200  11.87200  37.84800 1.000 84.24924  ?  153 THR A HA     1 
ATOM   2428 H HB     . THR A 1 153 ? 24.36000  13.50600  38.57000 1.000 78.48431  ?  153 THR A HB     1 
ATOM   2429 H HG1    . THR A 1 153 ? 26.43400  13.00900  39.20900 1.000 83.04336  ?  153 THR A HG1    1 
ATOM   2430 H HG21   . THR A 1 153 ? 24.66500  13.10600  40.84600 1.000 82.71924  ?  153 THR A HG21   1 
ATOM   2431 H HG22   . THR A 1 153 ? 23.26200  12.53800  40.39700 1.000 82.71924  ?  153 THR A HG22   1 
ATOM   2432 H HG23   . THR A 1 153 ? 24.48000  11.55600  40.61100 1.000 82.71924  ?  153 THR A HG23   1 
ATOM   2433 N N      . MET A 1 154 ? 24.15900  12.50900  35.72400 1.000 65.06388  ?  154 MET A N      1 
ATOM   2434 C CA     . MET A 1 154 ? 24.75600  12.62700  34.39600 1.000 63.27210  ?  154 MET A CA     1 
ATOM   2435 C C      . MET A 1 154 ? 26.24900  12.91800  34.49500 1.000 63.66143  ?  154 MET A C      1 
ATOM   2436 O O      . MET A 1 154 ? 27.05100  12.31700  33.77600 1.000 59.75467  ?  154 MET A O      1 
ATOM   2437 C CB     . MET A 1 154 ? 24.04100  13.72400  33.60700 1.000 61.01668  ?  154 MET A CB     1 
ATOM   2438 C CG     . MET A 1 154 ? 24.36400  13.79700  32.11500 1.000 58.65545  ?  154 MET A CG     1 
ATOM   2439 S SD     . MET A 1 154 ? 24.75900  12.23000  31.32200 1.000 68.32274  ?  154 MET A SD     1 
ATOM   2440 C CE     . MET A 1 154 ? 24.78600  12.71100  29.60500 1.000 60.20444  ?  154 MET A CE     1 
ATOM   2441 H H      . MET A 1 154 ? 23.53900  13.08200  35.88800 1.000 78.19443  ?  154 MET A H      1 
ATOM   2442 H HA     . MET A 1 154 ? 24.63400  11.79200  33.91800 1.000 76.04429  ?  154 MET A HA     1 
ATOM   2443 H HB2    . MET A 1 154 ? 23.08500  13.58000  33.68600 1.000 73.33778  ?  154 MET A HB2    1 
ATOM   2444 H HB3    . MET A 1 154 ? 24.28000  14.58100  33.99400 1.000 73.33778  ?  154 MET A HB3    1 
ATOM   2445 H HG2    . MET A 1 154 ? 23.59400  14.16600  31.65400 1.000 70.50431  ?  154 MET A HG2    1 
ATOM   2446 H HG3    . MET A 1 154 ? 25.13100  14.37900  31.99800 1.000 70.50431  ?  154 MET A HG3    1 
ATOM   2447 H HE1    . MET A 1 154 ? 25.00900  11.93800  29.06400 1.000 72.36310  ?  154 MET A HE1    1 
ATOM   2448 H HE2    . MET A 1 154 ? 23.91100  13.04800  29.35800 1.000 72.36310  ?  154 MET A HE2    1 
ATOM   2449 H HE3    . MET A 1 154 ? 25.45400  13.40500  29.48200 1.000 72.36310  ?  154 MET A HE3    1 
ATOM   2450 N N      . GLN A 1 155 ? 26.64100  13.83300  35.38000 1.000 62.75497  ?  155 GLN A N      1 
ATOM   2451 C CA     . GLN A 1 155 ? 28.05200  14.17500  35.50600 1.000 70.41736  ?  155 GLN A CA     1 
ATOM   2452 C C      . GLN A 1 155 ? 28.86900  12.95200  35.92100 1.000 62.29202  ?  155 GLN A C      1 
ATOM   2453 O O      . GLN A 1 155 ? 29.91800  12.66800  35.34100 1.000 56.09515  ?  155 GLN A O      1 
ATOM   2454 C CB     . GLN A 1 155 ? 28.24800  15.30900  36.51600 1.000 74.67020  ?  155 GLN A CB     1 
ATOM   2455 C CG     . GLN A 1 155 ? 27.77800  16.70200  36.06400 1.000 81.61177  ?  155 GLN A CG     1 
ATOM   2456 C CD     . GLN A 1 155 ? 28.21700  17.08200  34.65400 0.000 69.24944  ?  155 GLN A CD     1 
ATOM   2457 O OE1    . GLN A 1 155 ? 27.91200  16.38600  33.68500 0.570 67.75025  ?  155 GLN A OE1    1 
ATOM   2458 N NE2    . GLN A 1 155 ? 28.92100  18.20100  34.53700 0.620 74.63497  ?  155 GLN A NE2    1 
ATOM   2459 H H      . GLN A 1 155 ? 26.11800  14.26300  35.91000 1.000 75.42374  ?  155 GLN A H      1 
ATOM   2460 H HA     . GLN A 1 155 ? 28.36900  14.48800  34.64400 1.000 84.61860  ?  155 GLN A HA     1 
ATOM   2461 H HB2    . GLN A 1 155 ? 27.75300  15.08800  37.32100 1.000 89.72201  ?  155 GLN A HB2    1 
ATOM   2462 H HB3    . GLN A 1 155 ? 29.19400  15.37700  36.71700 1.000 89.72201  ?  155 GLN A HB3    1 
ATOM   2463 H HG2    . GLN A 1 155 ? 26.80900  16.72500  36.08600 1.000 98.05189  ?  155 GLN A HG2    1 
ATOM   2464 H HG3    . GLN A 1 155 ? 28.14000  17.36400  36.67300 1.000 98.05189  ?  155 GLN A HG3    1 
ATOM   2465 H HE21   . GLN A 1 155 ? 29.10600  18.66800  35.23500 1.000 89.67973  ?  155 GLN A HE21   1 
ATOM   2466 H HE22   . GLN A 1 155 ? 29.19200  18.45900  33.76200 1.000 89.67973  ?  155 GLN A HE22   1 
ATOM   2467 N N      . SER A 1 156 ? 28.38900  12.21500  36.92600 1.000 59.11151  ?  156 SER A N      1 
ATOM   2468 C CA     . SER A 1 156 ? 29.09300  11.00700  37.34000 1.000 66.30875  ?  156 SER A CA     1 
ATOM   2469 C C      . SER A 1 156 ? 29.13300  9.97400   36.21700 1.000 65.09472  ?  156 SER A C      1 
ATOM   2470 O O      . SER A 1 156 ? 30.16000  9.32200   36.00200 1.000 58.39114  ?  156 SER A O      1 
ATOM   2471 C CB     . SER A 1 156 ? 28.43200  10.41400  38.58300 1.000 71.22734  ?  156 SER A CB     1 
ATOM   2472 O OG     . SER A 1 156 ? 28.76000  9.04100   38.71900 1.000 79.30061  ?  156 SER A OG     1 
ATOM   2473 H H      . SER A 1 156 ? 27.67500  12.39000  37.37200 1.000 71.05159  ?  156 SER A H      1 
ATOM   2474 H HA     . SER A 1 156 ? 30.00700  11.24300  37.56600 1.000 79.68827  ?  156 SER A HA     1 
ATOM   2475 H HB2    . SER A 1 156 ? 28.74500  10.89300  39.36600 1.000 85.59058  ?  156 SER A HB2    1 
ATOM   2476 H HB3    . SER A 1 156 ? 27.47000  10.50300  38.50200 1.000 85.59058  ?  156 SER A HB3    1 
ATOM   2477 H HG     . SER A 1 156 ? 28.39100  8.72400   39.40400 1.000 95.27850  ?  156 SER A HG     1 
ATOM   2478 N N      . PHE A 1 157 ? 28.02300  9.81200   35.48900 1.000 59.73041  ?  157 PHE A N      1 
ATOM   2479 C CA     . PHE A 1 157 ? 27.99400  8.84300   34.40000 1.000 56.61657  ?  157 PHE A CA     1 
ATOM   2480 C C      . PHE A 1 157 ? 28.99800  9.21000   33.31200 1.000 55.07394  ?  157 PHE A C      1 
ATOM   2481 O O      . PHE A 1 157 ? 29.71400  8.34400   32.79600 1.000 52.54425  ?  157 PHE A O      1 
ATOM   2482 C CB     . PHE A 1 157 ? 26.58800  8.75000   33.81100 1.000 48.27553  ?  157 PHE A CB     1 
ATOM   2483 C CG     . PHE A 1 157 ? 26.49100  7.81900   32.63400 1.000 49.03717  ?  157 PHE A CG     1 
ATOM   2484 C CD1    . PHE A 1 157 ? 26.33200  6.45600   32.82300 1.000 48.93830  ?  157 PHE A CD1    1 
ATOM   2485 C CD2    . PHE A 1 157 ? 26.57000  8.30600   31.34200 1.000 47.31004  ?  157 PHE A CD2    1 
ATOM   2486 C CE1    . PHE A 1 157 ? 26.25300  5.60100   31.74700 1.000 46.99681  ?  157 PHE A CE1    1 
ATOM   2487 C CE2    . PHE A 1 157 ? 26.48800  7.45300   30.25900 1.000 45.12928  ?  157 PHE A CE2    1 
ATOM   2488 C CZ     . PHE A 1 157 ? 26.33400  6.09700   30.46300 1.000 42.99123  ?  157 PHE A CZ     1 
ATOM   2489 H H      . PHE A 1 157 ? 27.28900  10.24500  35.60500 1.000 71.79426  ?  157 PHE A H      1 
ATOM   2490 H HA     . PHE A 1 157 ? 28.23100  7.97100   34.75300 1.000 68.05766  ?  157 PHE A HA     1 
ATOM   2491 H HB2    . PHE A 1 157 ? 25.98300  8.42700   34.49700 1.000 58.04841  ?  157 PHE A HB2    1 
ATOM   2492 H HB3    . PHE A 1 157 ? 26.31400  9.63200   33.51600 1.000 58.04841  ?  157 PHE A HB3    1 
ATOM   2493 H HD1    . PHE A 1 157 ? 26.27700  6.11500   33.68600 1.000 58.84372  ?  157 PHE A HD1    1 
ATOM   2494 H HD2    . PHE A 1 157 ? 26.67900  9.21900   31.20100 1.000 56.88982  ?  157 PHE A HD2    1 
ATOM   2495 H HE1    . PHE A 1 157 ? 26.14600  4.68800   31.88600 1.000 56.51394  ?  157 PHE A HE1    1 
ATOM   2496 H HE2    . PHE A 1 157 ? 26.53600  7.79200   29.39400 1.000 54.27290  ?  157 PHE A HE2    1 
ATOM   2497 H HZ     . PHE A 1 157 ? 26.28400  5.51900   29.73600 1.000 51.70725  ?  157 PHE A HZ     1 
ATOM   2498 N N      A THR A 1 158 ? 29.06000  10.49300  32.94900 0.710 57.55954  ?  158 THR A N      1 
ATOM   2499 N N      B THR A 1 158 ? 29.06300  10.49400  32.95000 0.290 57.72035  ?  158 THR A N      1 
ATOM   2500 C CA     A THR A 1 158 ? 30.04700  10.94300  31.97400 0.710 60.18307  ?  158 THR A CA     1 
ATOM   2501 C CA     B THR A 1 158 ? 30.04900  10.93100  31.96900 0.290 60.08388  ?  158 THR A CA     1 
ATOM   2502 C C      A THR A 1 158 ? 31.46400  10.68900  32.47100 0.710 60.79622  ?  158 THR A C      1 
ATOM   2503 C C      B THR A 1 158 ? 31.46700  10.68900  32.47000 0.290 60.63543  ?  158 THR A C      1 
ATOM   2504 O O      A THR A 1 158 ? 32.36300  10.39300  31.67000 0.710 58.59653  ?  158 THR A O      1 
ATOM   2505 O O      B THR A 1 158 ? 32.37200  10.41200  31.67300 0.290 58.60668  ?  158 THR A O      1 
ATOM   2506 C CB     A THR A 1 158 ? 29.84500  12.42400  31.67400 0.710 58.08479  ?  158 THR A CB     1 
ATOM   2507 C CB     B THR A 1 158 ? 29.84800  12.40800  31.64000 0.290 57.90771  ?  158 THR A CB     1 
ATOM   2508 O OG1    A THR A 1 158 ? 28.54100  12.62100  31.11000 0.710 56.49412  ?  158 THR A OG1    1 
ATOM   2509 O OG1    B THR A 1 158 ? 29.82100  13.17400  32.85200 0.290 59.36633  ?  158 THR A OG1    1 
ATOM   2510 C CG2    A THR A 1 158 ? 30.90500  12.93400  30.70100 0.710 58.26086  ?  158 THR A CG2    1 
ATOM   2511 C CG2    B THR A 1 158 ? 28.54100  12.61200  30.88200 0.290 57.42666  ?  158 THR A CG2    1 
ATOM   2512 H H      A THR A 1 158 ? 28.54600  11.11400  33.25000 0.710 69.18922  ?  158 THR A H      1 
ATOM   2513 H H      B THR A 1 158 ? 28.55600  11.11900  33.25400 0.290 69.38219  ?  158 THR A H      1 
ATOM   2514 H HA     A THR A 1 158 ? 29.92400  10.45200  31.14700 0.710 72.33745  ?  158 THR A HA     1 
ATOM   2515 H HA     B THR A 1 158 ? 29.92500  10.42600  31.15000 0.290 72.21843  ?  158 THR A HA     1 
ATOM   2516 H HB     A THR A 1 158 ? 29.92500  12.93500  32.49500 0.710 69.81952  ?  158 THR A HB     1 
ATOM   2517 H HB     B THR A 1 158 ? 30.57700  12.71800  31.08100 0.290 69.60702  ?  158 THR A HB     1 
ATOM   2518 H HG1    A THR A 1 158 ? 28.40700  13.43900  30.97400 0.710 67.91071  ?  158 THR A HG1    1 
ATOM   2519 H HG1    B THR A 1 158 ? 29.69300  13.98500  32.67600 0.290 71.35736  ?  158 THR A HG1    1 
ATOM   2520 H HG21   A THR A 1 158 ? 30.66700  13.81900  30.38500 0.710 70.03080  ?  158 THR A HG21   1 
ATOM   2521 H HG21   B THR A 1 158 ? 28.40700  13.55500  30.70000 0.290 69.02976  ?  158 THR A HG21   1 
ATOM   2522 H HG22   A THR A 1 158 ? 31.76700  12.97900  31.14400 0.710 70.03080  ?  158 THR A HG22   1 
ATOM   2523 H HG22   B THR A 1 158 ? 28.56700  12.12900  30.04100 0.290 69.02976  ?  158 THR A HG22   1 
ATOM   2524 H HG23   A THR A 1 158 ? 30.97300  12.33500  29.94100 0.710 70.03080  ?  158 THR A HG23   1 
ATOM   2525 H HG23   B THR A 1 158 ? 27.79700  12.28400  31.41100 0.290 69.02976  ?  158 THR A HG23   1 
ATOM   2526 N N      . LYS A 1 159 ? 31.67700  10.79100  33.78800 1.000 60.46789  ?  159 LYS A N      1 
ATOM   2527 C CA     . LYS A 1 159 ? 32.97800  10.44900  34.35500 1.000 62.94633  ?  159 LYS A CA     1 
ATOM   2528 C C      . LYS A 1 159 ? 33.32400  8.98800   34.09800 1.000 62.54089  ?  159 LYS A C      1 
ATOM   2529 O O      . LYS A 1 159 ? 34.45800  8.66400   33.73500 1.000 63.14388  ?  159 LYS A O      1 
ATOM   2530 C CB     . LYS A 1 159 ? 32.95800  10.73200  35.86100 1.000 71.58483  ?  159 LYS A CB     1 
ATOM   2531 C CG     . LYS A 1 159 ? 34.22200  11.33100  36.42900 1.000 84.12604  ?  159 LYS A CG     1 
ATOM   2532 C CD     . LYS A 1 159 ? 34.05400  11.73400  37.90300 1.000 98.41737  ?  159 LYS A CD     1 
ATOM   2533 C CE     . LYS A 1 159 ? 33.11500  10.79200  38.66800 1.000 93.81803  ?  159 LYS A CE     1 
ATOM   2534 N NZ     . LYS A 1 159 ? 33.14900  11.02100  40.14400 1.000 110.38967 ?  159 LYS A NZ     1 
ATOM   2535 H H      A LYS A 1 159 ? 31.09400  11.05200  34.36200 0.710 72.67924  ?  159 LYS A H      1 
ATOM   2536 H H      B LYS A 1 159 ? 31.09300  11.05200  34.36200 0.290 72.67924  ?  159 LYS A H      1 
ATOM   2537 H HA     . LYS A 1 159 ? 33.66400  10.99600  33.94200 1.000 75.65336  ?  159 LYS A HA     1 
ATOM   2538 H HB2    . LYS A 1 159 ? 32.23700  11.35400  36.04400 1.000 86.01957  ?  159 LYS A HB2    1 
ATOM   2539 H HB3    . LYS A 1 159 ? 32.80100  9.89600   36.32600 1.000 86.01957  ?  159 LYS A HB3    1 
ATOM   2540 H HG2    . LYS A 1 159 ? 34.93800  10.67900  36.37300 1.000 101.06902 ?  159 LYS A HG2    1 
ATOM   2541 H HG3    . LYS A 1 159 ? 34.45500  12.12400  35.92300 1.000 101.06902 ?  159 LYS A HG3    1 
ATOM   2542 H HD2    . LYS A 1 159 ? 34.92100  11.71400  38.33800 1.000 118.21861 ?  159 LYS A HD2    1 
ATOM   2543 H HD3    . LYS A 1 159 ? 33.68200  12.62900  37.94600 1.000 118.21861 ?  159 LYS A HD3    1 
ATOM   2544 H HE2    . LYS A 1 159 ? 32.20600  10.93500  38.36300 1.000 112.69941 ?  159 LYS A HE2    1 
ATOM   2545 H HE3    . LYS A 1 159 ? 33.38200  9.87500   38.50100 1.000 112.69941 ?  159 LYS A HE3    1 
ATOM   2546 H HZ1    . LYS A 1 159 ? 32.60800  10.44600  40.55400 1.000 132.58538 ?  159 LYS A HZ1    1 
ATOM   2547 H HZ2    . LYS A 1 159 ? 33.97700  10.90800  40.45000 1.000 132.58538 ?  159 LYS A HZ2    1 
ATOM   2548 H HZ3    . LYS A 1 159 ? 32.88300  11.85000  40.33000 1.000 132.58538 ?  159 LYS A HZ3    1 
ATOM   2549 N N      . LEU A 1 160 ? 32.35000  8.09300   34.27200 1.000 62.86773  ?  160 LEU A N      1 
ATOM   2550 C CA     . LEU A 1 160 ? 32.61800  6.65900   34.18500 1.000 69.12526  ?  160 LEU A CA     1 
ATOM   2551 C C      . LEU A 1 160 ? 32.95600  6.24000   32.75900 1.000 66.42078  ?  160 LEU A C      1 
ATOM   2552 O O      . LEU A 1 160 ? 33.90800  5.47800   32.53600 1.000 54.96112  ?  160 LEU A O      1 
ATOM   2553 C CB     . LEU A 1 160 ? 31.40900  5.87500   34.70200 1.000 69.50670  ?  160 LEU A CB     1 
ATOM   2554 C CG     . LEU A 1 160 ? 31.43300  4.35600   34.51000 1.000 64.02506  ?  160 LEU A CG     1 
ATOM   2555 C CD1    . LEU A 1 160 ? 32.52300  3.71800   35.35700 1.000 63.45142  ?  160 LEU A CD1    1 
ATOM   2556 C CD2    . LEU A 1 160 ? 30.07900  3.75700   34.84500 1.000 65.04995  ?  160 LEU A CD2    1 
ATOM   2557 H H      . LEU A 1 160 ? 31.53000  8.28900   34.44100 1.000 75.55904  ?  160 LEU A H      1 
ATOM   2558 H HA     . LEU A 1 160 ? 33.38200  6.45100   34.74500 1.000 83.06809  ?  160 LEU A HA     1 
ATOM   2559 H HB2    . LEU A 1 160 ? 31.33200  6.03900   35.65500 1.000 83.52580  ?  160 LEU A HB2    1 
ATOM   2560 H HB3    . LEU A 1 160 ? 30.62000  6.20600   34.24400 1.000 83.52580  ?  160 LEU A HB3    1 
ATOM   2561 H HG     . LEU A 1 160 ? 31.62900  4.16300   33.58000 1.000 76.94784  ?  160 LEU A HG     1 
ATOM   2562 H HD11   . LEU A 1 160 ? 32.57300  2.77200   35.14500 1.000 76.25947  ?  160 LEU A HD11   1 
ATOM   2563 H HD12   . LEU A 1 160 ? 33.36900  4.14700   35.15700 1.000 76.25947  ?  160 LEU A HD12   1 
ATOM   2564 H HD13   . LEU A 1 160 ? 32.30400  3.83600   36.29400 1.000 76.25947  ?  160 LEU A HD13   1 
ATOM   2565 H HD21   . LEU A 1 160 ? 30.12300  2.79400   34.73300 1.000 78.17771  ?  160 LEU A HD21   1 
ATOM   2566 H HD22   . LEU A 1 160 ? 29.85600  3.97300   35.76300 1.000 78.17771  ?  160 LEU A HD22   1 
ATOM   2567 H HD23   . LEU A 1 160 ? 29.41200  4.12900   34.24600 1.000 78.17771  ?  160 LEU A HD23   1 
ATOM   2568 N N      . VAL A 1 161 ? 32.17800  6.71500   31.77900 1.000 56.23810  ?  161 VAL A N      1 
ATOM   2569 C CA     . VAL A 1 161 ? 32.42800  6.32200   30.40400 1.000 56.43882  ?  161 VAL A CA     1 
ATOM   2570 C C      . VAL A 1 161 ? 33.76600  6.88200   29.92900 1.000 58.80231  ?  161 VAL A C      1 
ATOM   2571 O O      . VAL A 1 161 ? 34.49200  6.23000   29.16600 1.000 54.73221  ?  161 VAL A O      1 
ATOM   2572 C CB     . VAL A 1 161 ? 31.26900  6.76400   29.49000 1.000 57.52396  ?  161 VAL A CB     1 
ATOM   2573 C CG1    . VAL A 1 161 ? 29.94000  6.25900   30.04600 1.000 57.27433  ?  161 VAL A CG1    1 
ATOM   2574 C CG2    . VAL A 1 161 ? 31.24800  8.27300   29.32400 1.000 58.12934  ?  161 VAL A CG2    1 
ATOM   2575 H H      . VAL A 1 161 ? 31.51700  7.25300   31.88900 1.000 67.60349  ?  161 VAL A H      1 
ATOM   2576 H HA     . VAL A 1 161 ? 32.47500  5.35400   30.36700 1.000 67.84435  ?  161 VAL A HA     1 
ATOM   2577 H HB     . VAL A 1 161 ? 31.40000  6.37700   28.61000 1.000 69.14652  ?  161 VAL A HB     1 
ATOM   2578 H HG11   . VAL A 1 161 ? 29.24400  6.41300   29.38800 1.000 68.84696  ?  161 VAL A HG11   1 
ATOM   2579 H HG12   . VAL A 1 161 ? 30.01500  5.31000   30.23300 1.000 68.84696  ?  161 VAL A HG12   1 
ATOM   2580 H HG13   . VAL A 1 161 ? 29.73600  6.74200   30.86300 1.000 68.84696  ?  161 VAL A HG13   1 
ATOM   2581 H HG21   . VAL A 1 161 ? 30.41900  8.53200   28.89200 1.000 69.87297  ?  161 VAL A HG21   1 
ATOM   2582 H HG22   . VAL A 1 161 ? 31.30800  8.68800   30.19900 1.000 69.87297  ?  161 VAL A HG22   1 
ATOM   2583 H HG23   . VAL A 1 161 ? 32.00300  8.54100   28.77800 1.000 69.87297  ?  161 VAL A HG23   1 
ATOM   2584 N N      . ASP A 1 162 ? 34.11500  8.09000   30.36700 1.000 55.00723  ?  162 ASP A N      1 
ATOM   2585 C CA     . ASP A 1 162 ? 35.43700  8.62000   30.05900 1.000 65.56758  ?  162 ASP A CA     1 
ATOM   2586 C C      . ASP A 1 162 ? 36.52700  7.72600   30.64300 1.000 61.33050  ?  162 ASP A C      1 
ATOM   2587 O O      . ASP A 1 162 ? 37.55900  7.49700   30.00700 1.000 59.95453  ?  162 ASP A O      1 
ATOM   2588 C CB     . ASP A 1 162 ? 35.57500  10.04700  30.58300 1.000 56.24500  ?  162 ASP A CB     1 
ATOM   2589 C CG     . ASP A 1 162 ? 34.91700  11.07400  29.66800 1.000 58.82637  ?  162 ASP A CG     1 
ATOM   2590 O OD1    . ASP A 1 162 ? 34.44200  10.68900  28.57500 1.000 58.61138  ?  162 ASP A OD1    1 
ATOM   2591 O OD2    . ASP A 1 162 ? 34.86800  12.26400  30.04600 1.000 56.27903  -1 162 ASP A OD2    1 
ATOM   2592 H H      . ASP A 1 162 ? 33.61500  8.61000   30.83500 1.000 66.12644  ?  162 ASP A H      1 
ATOM   2593 H HA     . ASP A 1 162 ? 35.54700  8.65000   29.09600 1.000 78.79886  ?  162 ASP A HA     1 
ATOM   2594 H HB2    . ASP A 1 162 ? 35.15300  10.10700  31.45500 1.000 67.61177  ?  162 ASP A HB2    1 
ATOM   2595 H HB3    . ASP A 1 162 ? 36.51700  10.26900  30.65500 1.000 67.61177  ?  162 ASP A HB3    1 
ATOM   2596 N N      . ARG A 1 163 ? 36.30500  7.20400   31.85000 1.000 67.07699  ?  163 ARG A N      1 
ATOM   2597 C CA     . ARG A 1 163 ? 37.23700  6.23900   32.42500 1.000 73.57536  ?  163 ARG A CA     1 
ATOM   2598 C C      . ARG A 1 163 ? 37.29500  4.96400   31.58900 1.000 69.37125  ?  163 ARG A C      1 
ATOM   2599 O O      . ARG A 1 163 ? 38.37400  4.39600   31.38300 1.000 61.70955  ?  163 ARG A O      1 
ATOM   2600 C CB     . ARG A 1 163 ? 36.83700  5.91400   33.86700 1.000 79.40484  ?  163 ARG A CB     1 
ATOM   2601 C CG     . ARG A 1 163 ? 37.47000  6.82400   34.91400 1.000 89.57209  ?  163 ARG A CG     1 
ATOM   2602 C CD     . ARG A 1 163 ? 36.52600  7.09100   36.08600 1.000 92.13018  ?  163 ARG A CD     1 
ATOM   2603 N NE     . ARG A 1 163 ? 35.90000  5.86900   36.58300 1.000 97.42382  ?  163 ARG A NE     1 
ATOM   2604 C CZ     . ARG A 1 163 ? 34.78700  5.83500   37.30600 1.000 101.21224 ?  163 ARG A CZ     1 
ATOM   2605 N NH1    . ARG A 1 163 ? 34.15100  6.94600   37.65100 1.000 87.18111  ?  163 ARG A NH1    1 
ATOM   2606 N NH2    . ARG A 1 163 ? 34.30200  4.65600   37.69500 1.000 97.67128  ?  163 ARG A NH2    1 
ATOM   2607 H H      . ARG A 1 163 ? 35.63000  7.39000   32.34900 1.000 80.61015  ?  163 ARG A H      1 
ATOM   2608 H HA     . ARG A 1 163 ? 38.12400  6.63300   32.43900 1.000 88.40820  ?  163 ARG A HA     1 
ATOM   2609 H HB2    . ARG A 1 163 ? 35.87400  5.99900   33.94700 1.000 95.40357  ?  163 ARG A HB2    1 
ATOM   2610 H HB3    . ARG A 1 163 ? 37.10700  5.00400   34.06600 1.000 95.40357  ?  163 ARG A HB3    1 
ATOM   2611 H HG2    . ARG A 1 163 ? 38.27200  6.40200   35.26100 1.000 107.60427 ?  163 ARG A HG2    1 
ATOM   2612 H HG3    . ARG A 1 163 ? 37.69300  7.67400   34.50500 1.000 107.60427 ?  163 ARG A HG3    1 
ATOM   2613 H HD2    . ARG A 1 163 ? 37.02800  7.49000   36.81400 1.000 110.67399 ?  163 ARG A HD2    1 
ATOM   2614 H HD3    . ARG A 1 163 ? 35.82400  7.69400   35.79800 1.000 110.67399 ?  163 ARG A HD3    1 
ATOM   2615 H HE     . ARG A 1 163 ? 36.27800  5.12000   36.39400 1.000 117.02636 ?  163 ARG A HE     1 
ATOM   2616 H HH11   . ARG A 1 163 ? 34.45800  7.71100   37.40500 1.000 104.73510 ?  163 ARG A HH11   1 
ATOM   2617 H HH12   . ARG A 1 163 ? 33.43200  6.90200   38.12000 1.000 104.73510 ?  163 ARG A HH12   1 
ATOM   2618 H HH21   . ARG A 1 163 ? 34.70900  3.93100   37.47700 1.000 117.32330 ?  163 ARG A HH21   1 
ATOM   2619 H HH22   . ARG A 1 163 ? 33.58200  4.62100   38.16400 1.000 117.32330 ?  163 ARG A HH22   1 
ATOM   2620 N N      . VAL A 1 164 ? 36.14100  4.49200   31.11200 1.000 67.63853  ?  164 VAL A N      1 
ATOM   2621 C CA     . VAL A 1 164 ? 36.10100  3.25000   30.34500 1.000 68.30153  ?  164 VAL A CA     1 
ATOM   2622 C C      . VAL A 1 164 ? 36.76800  3.43800   28.98500 1.000 61.23306  ?  164 VAL A C      1 
ATOM   2623 O O      . VAL A 1 164 ? 37.40000  2.51000   28.45900 1.000 59.26722  ?  164 VAL A O      1 
ATOM   2624 C CB     . VAL A 1 164 ? 34.64500  2.76600   30.19800 1.000 72.68733  ?  164 VAL A CB     1 
ATOM   2625 C CG1    . VAL A 1 164 ? 34.52600  1.73000   29.08500 1.000 70.13824  ?  164 VAL A CG1    1 
ATOM   2626 C CG2    . VAL A 1 164 ? 34.15700  2.19800   31.52100 1.000 75.80224  ?  164 VAL A CG2    1 
ATOM   2627 H H      . VAL A 1 164 ? 35.37500  4.86900   31.21800 1.000 81.28400  ?  164 VAL A H      1 
ATOM   2628 H HA     . VAL A 1 164 ? 36.60000  2.57300   30.82900 1.000 82.07961  ?  164 VAL A HA     1 
ATOM   2629 H HB     . VAL A 1 164 ? 34.08200  3.51700   29.95700 1.000 87.34257  ?  164 VAL A HB     1 
ATOM   2630 H HG11   . VAL A 1 164 ? 33.68800  1.25200   29.18700 1.000 84.28366  ?  164 VAL A HG11   1 
ATOM   2631 H HG12   . VAL A 1 164 ? 34.54400  2.18400   28.22800 1.000 84.28366  ?  164 VAL A HG12   1 
ATOM   2632 H HG13   . VAL A 1 164 ? 35.27000  1.11200   29.14700 1.000 84.28366  ?  164 VAL A HG13   1 
ATOM   2633 H HG21   . VAL A 1 164 ? 33.29000  1.78400   31.38700 1.000 91.08046  ?  164 VAL A HG21   1 
ATOM   2634 H HG22   . VAL A 1 164 ? 34.79400  1.53700   31.83600 1.000 91.08046  ?  164 VAL A HG22   1 
ATOM   2635 H HG23   . VAL A 1 164 ? 34.08300  2.91900   32.16600 1.000 91.08046  ?  164 VAL A HG23   1 
ATOM   2636 N N      . GLY A 1 165 ? 36.62900  4.61200   28.39600 1.000 54.33567  ?  165 GLY A N      1 
ATOM   2637 C CA     . GLY A 1 165 ? 37.19200  4.88900   27.08800 1.000 54.81468  ?  165 GLY A CA     1 
ATOM   2638 C C      . GLY A 1 165 ? 36.14500  4.87800   25.98600 1.000 53.17089  ?  165 GLY A C      1 
ATOM   2639 O O      . GLY A 1 165 ? 34.93100  4.80300   26.21500 1.000 52.29225  ?  165 GLY A O      1 
ATOM   2640 H H      . GLY A 1 165 ? 36.20600  5.27700   28.73900 1.000 65.32057  ?  165 GLY A H      1 
ATOM   2641 H HA2    . GLY A 1 165 ? 37.61300  5.76300   27.09900 1.000 65.89538  ?  165 GLY A HA2    1 
ATOM   2642 H HA3    . GLY A 1 165 ? 37.86100  4.21900   26.87900 1.000 65.89538  ?  165 GLY A HA3    1 
ATOM   2643 N N      . ASP A 1 166 ? 36.65000  4.94200   24.75500 1.000 50.78978  ?  166 ASP A N      1 
ATOM   2644 C CA     . ASP A 1 166 ? 35.77900  5.03000   23.59900 1.000 47.05777  ?  166 ASP A CA     1 
ATOM   2645 C C      . ASP A 1 166 ? 34.91800  3.76800   23.48500 1.000 48.44861  ?  166 ASP A C      1 
ATOM   2646 O O      . ASP A 1 166 ? 35.35000  2.67300   23.84000 1.000 47.74397  ?  166 ASP A O      1 
ATOM   2647 C CB     . ASP A 1 166 ? 36.61300  5.19600   22.32400 1.000 57.22747  ?  166 ASP A CB     1 
ATOM   2648 C CG     . ASP A 1 166 ? 37.21200  6.57800   22.18700 1.000 61.82115  ?  166 ASP A CG     1 
ATOM   2649 O OD1    . ASP A 1 166 ? 36.91600  7.45400   23.03600 1.000 61.40751  ?  166 ASP A OD1    1 
ATOM   2650 O OD2    . ASP A 1 166 ? 37.97000  6.79700   21.21700 1.000 57.43457  -1 166 ASP A OD2    1 
ATOM   2651 H H      . ASP A 1 166 ? 37.49000  4.93600   24.56900 1.000 61.06551  ?  166 ASP A H      1 
ATOM   2652 H HA     . ASP A 1 166 ? 35.19300  5.79600   23.69400 1.000 56.58709  ?  166 ASP A HA     1 
ATOM   2653 H HB2    . ASP A 1 166 ? 37.34000  4.55400   22.33800 1.000 68.79073  ?  166 ASP A HB2    1 
ATOM   2654 H HB3    . ASP A 1 166 ? 36.04500  5.03700   21.55400 1.000 68.79073  ?  166 ASP A HB3    1 
ATOM   2655 N N      . PRO A 1 167 ? 33.68900  3.89000   22.97200 1.000 43.71480  ?  167 PRO A N      1 
ATOM   2656 C CA     . PRO A 1 167 ? 32.89200  2.69600   22.70100 1.000 45.80825  ?  167 PRO A CA     1 
ATOM   2657 C C      . PRO A 1 167 ? 33.50900  1.90000   21.56300 1.000 48.28275  ?  167 PRO A C      1 
ATOM   2658 O O      . PRO A 1 167 ? 34.33500  2.43100   20.80100 1.000 46.04932  ?  167 PRO A O      1 
ATOM   2659 C CB     . PRO A 1 167 ? 31.51400  3.24300   22.31300 1.000 40.91392  ?  167 PRO A CB     1 
ATOM   2660 C CG     . PRO A 1 167 ? 31.59600  4.73300   22.38900 1.000 46.48195  ?  167 PRO A CG     1 
ATOM   2661 C CD     . PRO A 1 167 ? 33.03500  5.12900   22.51100 1.000 41.31737  ?  167 PRO A CD     1 
ATOM   2662 H HA     . PRO A 1 167 ? 32.80400  2.14800   23.49600 1.000 55.08767  ?  167 PRO A HA     1 
ATOM   2663 H HB2    . PRO A 1 167 ? 31.29700  2.96000   21.41100 1.000 49.21447  ?  167 PRO A HB2    1 
ATOM   2664 H HB3    . PRO A 1 167 ? 30.84800  2.90700   22.93500 1.000 49.21447  ?  167 PRO A HB3    1 
ATOM   2665 H HG2    . PRO A 1 167 ? 31.21400  5.11100   21.58100 1.000 55.89611  ?  167 PRO A HG2    1 
ATOM   2666 H HG3    . PRO A 1 167 ? 31.09900  5.03800   23.16400 1.000 55.89611  ?  167 PRO A HG3    1 
ATOM   2667 H HD2    . PRO A 1 167 ? 33.39000  5.40900   21.65300 1.000 49.69861  ?  167 PRO A HD2    1 
ATOM   2668 H HD3    . PRO A 1 167 ? 33.14300  5.84000   23.16200 1.000 49.69861  ?  167 PRO A HD3    1 
ATOM   2669 N N      . PRO A 1 168 ? 33.13100  0.63200   21.40400 1.000 47.67600  ?  168 PRO A N      1 
ATOM   2670 C CA     . PRO A 1 168 ? 33.70300  -0.16600  20.31600 1.000 47.30223  ?  168 PRO A CA     1 
ATOM   2671 C C      . PRO A 1 168 ? 33.40800  0.46900   18.96500 1.000 47.03314  ?  168 PRO A C      1 
ATOM   2672 O O      . PRO A 1 168 ? 32.42900  1.19900   18.78700 1.000 47.15765  ?  168 PRO A O      1 
ATOM   2673 C CB     . PRO A 1 168 ? 33.01300  -1.52600  20.46300 1.000 53.15653  ?  168 PRO A CB     1 
ATOM   2674 C CG     . PRO A 1 168 ? 32.46100  -1.54500  21.85700 1.000 51.89574  ?  168 PRO A CG     1 
ATOM   2675 C CD     . PRO A 1 168 ? 32.12000  -0.12000  22.17300 1.000 48.24023  ?  168 PRO A CD     1 
ATOM   2676 H HA     . PRO A 1 168 ? 34.66000  -0.27600  20.43000 1.000 56.88044  ?  168 PRO A HA     1 
ATOM   2677 H HB2    . PRO A 1 168 ? 32.30100  -1.60500  19.80900 1.000 63.90560  ?  168 PRO A HB2    1 
ATOM   2678 H HB3    . PRO A 1 168 ? 33.65900  -2.23800  20.33800 1.000 63.90560  ?  168 PRO A HB3    1 
ATOM   2679 H HG2    . PRO A 1 168 ? 31.66900  -2.10400  21.88900 1.000 62.39265  ?  168 PRO A HG2    1 
ATOM   2680 H HG3    . PRO A 1 168 ? 33.13100  -1.88400  22.47100 1.000 62.39265  ?  168 PRO A HG3    1 
ATOM   2681 H HD2    . PRO A 1 168 ? 31.22300  0.09700   21.87400 1.000 58.00604  ?  168 PRO A HD2    1 
ATOM   2682 H HD3    . PRO A 1 168 ? 32.20500  0.05500   23.12300 1.000 58.00604  ?  168 PRO A HD3    1 
ATOM   2683 N N      . ALA A 1 169 ? 34.28200  0.20800   18.01300 1.000 46.18264  ?  169 ALA A N      1 
ATOM   2684 C CA     . ALA A 1 169 ? 34.08500  0.71100   16.66900 1.000 52.70671  ?  169 ALA A CA     1 
ATOM   2685 C C      . ALA A 1 169 ? 32.89500  0.00400   16.02200 1.000 49.66619  ?  169 ALA A C      1 
ATOM   2686 O O      . ALA A 1 169 ? 32.52100  -1.09600  16.42100 1.000 43.94212  ?  169 ALA A O      1 
ATOM   2687 C CB     . ALA A 1 169 ? 35.34800  0.49100   15.83100 1.000 61.28370  ?  169 ALA A CB     1 
ATOM   2688 H H      . ALA A 1 169 ? 34.99700  -0.25800  18.11900 1.000 55.53694  ?  169 ALA A H      1 
ATOM   2689 H HA     . ALA A 1 169 ? 33.90400  1.66400   16.69500 1.000 63.36582  ?  169 ALA A HA     1 
ATOM   2690 H HB1    . ALA A 1 169 ? 35.19700  0.83300   14.93600 1.000 73.65821  ?  169 ALA A HB1    1 
ATOM   2691 H HB2    . ALA A 1 169 ? 36.08800  0.96200   16.24400 1.000 73.65821  ?  169 ALA A HB2    1 
ATOM   2692 H HB3    . ALA A 1 169 ? 35.54000  -0.45900  15.79300 1.000 73.65821  ?  169 ALA A HB3    1 
ATOM   2693 N N      . PRO A 1 170 ? 32.26200  0.64100   15.03700 1.000 52.62346  ?  170 PRO A N      1 
ATOM   2694 C CA     . PRO A 1 170 ? 31.19200  -0.04600  14.30300 1.000 50.63938  ?  170 PRO A CA     1 
ATOM   2695 C C      . PRO A 1 170 ? 31.73400  -1.27800  13.59000 1.000 50.07974  ?  170 PRO A C      1 
ATOM   2696 O O      . PRO A 1 170 ? 32.86700  -1.28800  13.10800 1.000 50.42774  ?  170 PRO A O      1 
ATOM   2697 C CB     . PRO A 1 170 ? 30.68200  1.00400   13.32100 1.000 58.81101  ?  170 PRO A CB     1 
ATOM   2698 C CG     . PRO A 1 170 ? 31.53400  2.21700   13.47700 1.000 58.05301  ?  170 PRO A CG     1 
ATOM   2699 C CD     . PRO A 1 170 ? 32.59300  1.97200   14.49400 1.000 54.57130  ?  170 PRO A CD     1 
ATOM   2700 H HA     . PRO A 1 170 ? 30.46900  -0.29700  14.89900 1.000 60.88503  ?  170 PRO A HA     1 
ATOM   2701 H HB2    . PRO A 1 170 ? 30.75000  0.65700   12.41800 1.000 70.69098  ?  170 PRO A HB2    1 
ATOM   2702 H HB3    . PRO A 1 170 ? 29.75700  1.21200   13.52800 1.000 70.69098  ?  170 PRO A HB3    1 
ATOM   2703 H HG2    . PRO A 1 170 ? 31.94300  2.42100   12.62100 1.000 69.78138  ?  170 PRO A HG2    1 
ATOM   2704 H HG3    . PRO A 1 170 ? 30.97200  2.95600   13.76000 1.000 69.78138  ?  170 PRO A HG3    1 
ATOM   2705 H HD2    . PRO A 1 170 ? 33.47000  1.96600   14.08100 1.000 65.60333  ?  170 PRO A HD2    1 
ATOM   2706 H HD3    . PRO A 1 170 ? 32.56000  2.64500   15.19200 1.000 65.60333  ?  170 PRO A HD3    1 
ATOM   2707 N N      . ALA A 1 171 ? 30.91200  -2.32800  13.53700 1.000 47.10036  ?  171 ALA A N      1 
ATOM   2708 C CA     . ALA A 1 171 ? 31.33800  -3.57000  12.91500 1.000 49.10917  ?  171 ALA A CA     1 
ATOM   2709 C C      . ALA A 1 171 ? 31.43600  -3.39800  11.40200 1.000 50.27185  ?  171 ALA A C      1 
ATOM   2710 O O      . ALA A 1 171 ? 30.82800  -2.49900  10.83200 1.000 51.39087  ?  171 ALA A O      1 
ATOM   2711 C CB     . ALA A 1 171 ? 30.36500  -4.70100  13.24700 1.000 43.74540  ?  171 ALA A CB     1 
ATOM   2712 H H      . ALA A 1 171 ? 30.11200  -2.34200  13.85300 1.000 56.63821  ?  171 ALA A H      1 
ATOM   2713 H HA     . ALA A 1 171 ? 32.21300  -3.81600  13.25400 1.000 59.04877  ?  171 ALA A HA     1 
ATOM   2714 H HB1    . ALA A 1 171 ? 30.68700  -5.52300  12.84500 1.000 52.61225  ?  171 ALA A HB1    1 
ATOM   2715 H HB2    . ALA A 1 171 ? 30.31500  -4.80100  14.21000 1.000 52.61225  ?  171 ALA A HB2    1 
ATOM   2716 H HB3    . ALA A 1 171 ? 29.49000  -4.47900  12.89100 1.000 52.61225  ?  171 ALA A HB3    1 
ATOM   2717 N N      . PRO A 1 172 ? 32.19400  -4.26900  10.72900 1.000 47.99731  ?  172 PRO A N      1 
ATOM   2718 C CA     . PRO A 1 172 ? 32.30800  -4.17100  9.27500  1.000 48.74477  ?  172 PRO A CA     1 
ATOM   2719 C C      . PRO A 1 172 ? 30.97400  -4.40800  8.57600  1.000 50.60643  ?  172 PRO A C      1 
ATOM   2720 O O      . PRO A 1 172 ? 30.05300  -5.02500  9.11900  1.000 47.28082  ?  172 PRO A O      1 
ATOM   2721 C CB     . PRO A 1 172 ? 33.31400  -5.27700  8.91700  1.000 51.91100  ?  172 PRO A CB     1 
ATOM   2722 C CG     . PRO A 1 172 ? 33.97600  -5.65000  10.19800 1.000 51.66765  ?  172 PRO A CG     1 
ATOM   2723 C CD     . PRO A 1 172 ? 32.98400  -5.38000  11.28100 1.000 49.38391  ?  172 PRO A CD     1 
ATOM   2724 H HA     . PRO A 1 172 ? 32.66000  -3.30300  9.02400  1.000 58.61149  ?  172 PRO A HA     1 
ATOM   2725 H HB2    . PRO A 1 172 ? 32.84400  -6.03600  8.53800  1.000 62.41097  ?  172 PRO A HB2    1 
ATOM   2726 H HB3    . PRO A 1 172 ? 33.96200  -4.93600  8.28100  1.000 62.41097  ?  172 PRO A HB3    1 
ATOM   2727 H HG2    . PRO A 1 172 ? 34.21300  -6.59100  10.17900 1.000 62.11895  ?  172 PRO A HG2    1 
ATOM   2728 H HG3    . PRO A 1 172 ? 34.77200  -5.11000  10.32200 1.000 62.11895  ?  172 PRO A HG3    1 
ATOM   2729 H HD2    . PRO A 1 172 ? 32.42600  -6.15600  11.44200 1.000 59.37846  ?  172 PRO A HD2    1 
ATOM   2730 H HD3    . PRO A 1 172 ? 33.42900  -5.11500  12.10100 1.000 59.37846  ?  172 PRO A HD3    1 
ATOM   2731 N N      . ASP A 1 173 ? 30.87800  -3.90100  7.35600  1.000 47.57726  ?  173 ASP A N      1 
ATOM   2732 C CA     . ASP A 1 173 ? 29.70200  -4.16500  6.53900  1.000 52.68928  ?  173 ASP A CA     1 
ATOM   2733 C C      . ASP A 1 173 ? 29.65400  -5.64100  6.16500  1.000 53.78294  ?  173 ASP A C      1 
ATOM   2734 O O      . ASP A 1 173 ? 30.69200  -6.30200  6.06000  1.000 52.18980  ?  173 ASP A O      1 
ATOM   2735 C CB     . ASP A 1 173 ? 29.72000  -3.31400  5.27600  1.000 60.32296  ?  173 ASP A CB     1 
ATOM   2736 C CG     . ASP A 1 173 ? 29.45500  -1.84300  5.56000  1.000 66.02116  ?  173 ASP A CG     1 
ATOM   2737 O OD1    . ASP A 1 173 ? 28.64900  -1.54400  6.46900  1.000 57.55721  ?  173 ASP A OD1    1 
ATOM   2738 O OD2    . ASP A 1 173 ? 30.04600  -0.99100  4.87000  1.000 66.85693  -1 173 ASP A OD2    1 
ATOM   2739 H H      . ASP A 1 173 ? 31.47300  -3.40700  6.98000  1.000 57.21048  ?  173 ASP A H      1 
ATOM   2740 H HA     . ASP A 1 173 ? 28.90000  -3.94200  7.03800  1.000 63.34491  ?  173 ASP A HA     1 
ATOM   2741 H HB2    . ASP A 1 173 ? 30.59200  -3.38700  4.85700  1.000 72.50532  ?  173 ASP A HB2    1 
ATOM   2742 H HB3    . ASP A 1 173 ? 29.03300  -3.63100  4.66900  1.000 72.50532  ?  173 ASP A HB3    1 
ATOM   2743 N N      . PRO A 1 174 ? 28.46300  -6.19200  5.97600  1.000 54.75253  ?  174 PRO A N      1 
ATOM   2744 C CA     . PRO A 1 174 ? 28.34900  -7.61400  5.61500  1.000 57.45049  ?  174 PRO A CA     1 
ATOM   2745 C C      . PRO A 1 174 ? 28.76800  -7.84400  4.17500  1.000 53.47447  ?  174 PRO A C      1 
ATOM   2746 O O      . PRO A 1 174 ? 28.95000  -6.88900  3.40900  1.000 50.08642  ?  174 PRO A O      1 
ATOM   2747 C CB     . PRO A 1 174 ? 26.86300  -7.91600  5.82500  1.000 55.04351  ?  174 PRO A CB     1 
ATOM   2748 C CG     . PRO A 1 174 ? 26.18400  -6.59200  5.66000  1.000 58.50314  ?  174 PRO A CG     1 
ATOM   2749 C CD     . PRO A 1 174 ? 27.14100  -5.55600  6.15700  1.000 51.41246  ?  174 PRO A CD     1 
ATOM   2750 H HA     . PRO A 1 174 ? 28.88200  -8.16900  6.20500  1.000 69.05836  ?  174 PRO A HA     1 
ATOM   2751 H HB2    . PRO A 1 174 ? 26.55500  -8.55100  5.15900  1.000 66.16998  ?  174 PRO A HB2    1 
ATOM   2752 H HB3    . PRO A 1 174 ? 26.71900  -8.27300  6.71500  1.000 66.16998  ?  174 PRO A HB3    1 
ATOM   2753 H HG2    . PRO A 1 174 ? 25.98000  -6.44600  4.72300  1.000 70.32154  ?  174 PRO A HG2    1 
ATOM   2754 H HG3    . PRO A 1 174 ? 25.36700  -6.57900  6.18300  1.000 70.32154  ?  174 PRO A HG3    1 
ATOM   2755 H HD2    . PRO A 1 174 ? 27.07500  -4.74400  5.62900  1.000 61.81272  ?  174 PRO A HD2    1 
ATOM   2756 H HD3    . PRO A 1 174 ? 26.98000  -5.35700  7.09200  1.000 61.81272  ?  174 PRO A HD3    1 
ATOM   2757 N N      . PRO A 1 175 ? 28.93100  -9.10100  3.77000  1.000 58.85518  ?  175 PRO A N      1 
ATOM   2758 C CA     . PRO A 1 175 ? 29.40000  -9.38300  2.40600  1.000 59.60352  ?  175 PRO A CA     1 
ATOM   2759 C C      . PRO A 1 175 ? 28.39000  -8.94000  1.36200  1.000 52.46906  ?  175 PRO A C      1 
ATOM   2760 O O      . PRO A 1 175 ? 27.19300  -8.79800  1.63000  1.000 56.23734  ?  175 PRO A O      1 
ATOM   2761 C CB     . PRO A 1 175 ? 29.57600  -10.91000 2.38600  1.000 65.67223  ?  175 PRO A CB     1 
ATOM   2762 C CG     . PRO A 1 175 ? 29.45300  -11.36400 3.81800  1.000 66.29397  ?  175 PRO A CG     1 
ATOM   2763 C CD     . PRO A 1 175 ? 28.64800  -10.33400 4.52800  1.000 64.38081  ?  175 PRO A CD     1 
ATOM   2764 H HA     . PRO A 1 175 ? 30.25400  -8.95200  2.24500  1.000 71.64200  ?  175 PRO A HA     1 
ATOM   2765 H HB2    . PRO A 1 175 ? 28.88300  -11.31000 1.83800  1.000 78.92444  ?  175 PRO A HB2    1 
ATOM   2766 H HB3    . PRO A 1 175 ? 30.45100  -11.13200 2.03000  1.000 78.92444  ?  175 PRO A HB3    1 
ATOM   2767 H HG2    . PRO A 1 175 ? 29.00600  -12.22500 3.84700  1.000 79.67054  ?  175 PRO A HG2    1 
ATOM   2768 H HG3    . PRO A 1 175 ? 30.33700  -11.43600 4.21200  1.000 79.67054  ?  175 PRO A HG3    1 
ATOM   2769 H HD2    . PRO A 1 175 ? 27.70300  -10.55100 4.49400  1.000 77.37474  ?  175 PRO A HD2    1 
ATOM   2770 H HD3    . PRO A 1 175 ? 28.93500  -10.24600 5.45000  1.000 77.37474  ?  175 PRO A HD3    1 
ATOM   2771 N N      . ALA A 1 176 ? 28.89900  -8.72000  0.14500  1.000 47.46736  ?  176 ALA A N      1 
ATOM   2772 C CA     . ALA A 1 176 ? 28.04800  -8.27400  -0.95300 1.000 53.84254  ?  176 ALA A CA     1 
ATOM   2773 C C      . ALA A 1 176 ? 27.07900  -9.36000  -1.40200 1.000 53.44845  ?  176 ALA A C      1 
ATOM   2774 O O      . ALA A 1 176 ? 26.08100  -9.04300  -2.05300 1.000 53.93795  ?  176 ALA A O      1 
ATOM   2775 C CB     . ALA A 1 176 ? 28.90300  -7.82600  -2.13600 1.000 49.75730  ?  176 ALA A CB     1 
ATOM   2776 H H      . ALA A 1 176 ? 29.72600  -8.82200  -0.06600 1.000 57.07860  ?  176 ALA A H      1 
ATOM   2777 H HA     . ALA A 1 176 ? 27.53200  -7.51000  -0.65400 1.000 64.72882  ?  176 ALA A HA     1 
ATOM   2778 H HB1    . ALA A 1 176 ? 28.32100  -7.51700  -2.84800 1.000 59.82653  ?  176 ALA A HB1    1 
ATOM   2779 H HB2    . ALA A 1 176 ? 29.48600  -7.10500  -1.85000 1.000 59.82653  ?  176 ALA A HB2    1 
ATOM   2780 H HB3    . ALA A 1 176 ? 29.43400  -8.57700  -2.44500 1.000 59.82653  ?  176 ALA A HB3    1 
ATOM   2781 N N      . ALA A 1 177 ? 27.35500  -10.62000 -1.07900 1.000 48.14426  ?  177 ALA A N      1 
ATOM   2782 C CA     . ALA A 1 177 ? 26.44700  -11.72600 -1.33400 1.000 52.80023  ?  177 ALA A CA     1 
ATOM   2783 C C      . ALA A 1 177 ? 26.26100  -12.51500 -0.04200 1.000 51.23374  ?  177 ALA A C      1 
ATOM   2784 O O      . ALA A 1 177 ? 27.20300  -12.68400 0.73500  1.000 53.02036  ?  177 ALA A O      1 
ATOM   2785 C CB     . ALA A 1 177 ? 26.97200  -12.64900 -2.44800 1.000 52.23392  ?  177 ALA A CB     1 
ATOM   2786 H H      . ALA A 1 177 ? 28.08700  -10.86400 -0.69800 1.000 57.89088  ?  177 ALA A H      1 
ATOM   2787 H HA     . ALA A 1 177 ? 25.58500  -11.38600 -1.62000 1.000 63.47805  ?  177 ALA A HA     1 
ATOM   2788 H HB1    . ALA A 1 177 ? 26.33600  -13.36800 -2.58800 1.000 62.79848  ?  177 ALA A HB1    1 
ATOM   2789 H HB2    . ALA A 1 177 ? 27.07400  -12.13400 -3.26300 1.000 62.79848  ?  177 ALA A HB2    1 
ATOM   2790 H HB3    . ALA A 1 177 ? 27.82900  -13.01400 -2.17800 1.000 62.79848  ?  177 ALA A HB3    1 
ATOM   2791 N N      . MET A 1 178 ? 25.04600  -12.99900 0.17600  1.000 51.36574  ?  178 MET A N      1 
ATOM   2792 C CA     . MET A 1 178 ? 24.71100  -13.69900 1.40000  1.000 55.65439  ?  178 MET A CA     1 
ATOM   2793 C C      . MET A 1 178 ? 24.21200  -15.10000 1.09500  1.000 52.02637  ?  178 MET A C      1 
ATOM   2794 O O      . MET A 1 178 ? 23.60500  -15.32500 0.04600  1.000 52.57574  ?  178 MET A O      1 
ATOM   2795 C CB     . MET A 1 178 ? 23.63100  -12.93200 2.17100  1.000 57.24900  ?  178 MET A CB     1 
ATOM   2796 C CG     . MET A 1 178 ? 24.12700  -11.62300 2.74200  1.000 66.48106  ?  178 MET A CG     1 
ATOM   2797 S SD     . MET A 1 178 ? 23.16300  -11.05400 4.14500  1.000 69.02089  ?  178 MET A SD     1 
ATOM   2798 C CE     . MET A 1 178 ? 24.35400  -9.95600  4.90500  0.460 63.32441  ?  178 MET A CE     1 
ATOM   2799 H H      . MET A 1 178 ? 24.39200  -12.93200 -0.37900 1.000 61.75665  ?  178 MET A H      1 
ATOM   2800 H HA     . MET A 1 178 ? 25.50000  -13.76900 1.96000  1.000 66.90303  ?  178 MET A HA     1 
ATOM   2801 H HB2    . MET A 1 178 ? 22.89500  -12.73600 1.57100  1.000 68.81657  ?  178 MET A HB2    1 
ATOM   2802 H HB3    . MET A 1 178 ? 23.32100  -13.48100 2.90800  1.000 68.81657  ?  178 MET A HB3    1 
ATOM   2803 H HG2    . MET A 1 178 ? 25.04500  -11.73600 3.03700  1.000 79.89504  ?  178 MET A HG2    1 
ATOM   2804 H HG3    . MET A 1 178 ? 24.08200  -10.94200 2.05300  1.000 79.89504  ?  178 MET A HG3    1 
ATOM   2805 H HE1    . MET A 1 178 ? 23.97100  -9.58700  5.71600  1.000 76.10706  ?  178 MET A HE1    1 
ATOM   2806 H HE2    . MET A 1 178 ? 25.15600  -10.45900 5.11600  1.000 76.10706  ?  178 MET A HE2    1 
ATOM   2807 H HE3    . MET A 1 178 ? 24.56500  -9.24100  4.28400  1.000 76.10706  ?  178 MET A HE3    1 
ATOM   2808 N N      . PRO A 1 179 ? 24.45700  -16.06600 1.97500  1.000 51.57863  ?  179 PRO A N      1 
ATOM   2809 C CA     . PRO A 1 179 ? 23.85300  -17.39700 1.79700  1.000 55.85953  ?  179 PRO A CA     1 
ATOM   2810 C C      . PRO A 1 179 ? 22.34300  -17.29800 1.93200  1.000 56.60262  ?  179 PRO A C      1 
ATOM   2811 O O      . PRO A 1 179 ? 21.84100  -16.77300 2.93400  1.000 51.89374  ?  179 PRO A O      1 
ATOM   2812 C CB     . PRO A 1 179 ? 24.46300  -18.23200 2.93700  1.000 54.48438  ?  179 PRO A CB     1 
ATOM   2813 C CG     . PRO A 1 179 ? 25.65900  -17.45100 3.40800  1.000 58.97828  ?  179 PRO A CG     1 
ATOM   2814 C CD     . PRO A 1 179 ? 25.32700  -16.00900 3.16500  1.000 57.66217  ?  179 PRO A CD     1 
ATOM   2815 H HA     . PRO A 1 179 ? 24.09800  -17.79000 0.94400  1.000 67.14920  ?  179 PRO A HA     1 
ATOM   2816 H HB2    . PRO A 1 179 ? 23.81500  -18.33700 3.65000  1.000 65.49903  ?  179 PRO A HB2    1 
ATOM   2817 H HB3    . PRO A 1 179 ? 24.72900  -19.10200 2.60000  1.000 65.49903  ?  179 PRO A HB3    1 
ATOM   2818 H HG2    . PRO A 1 179 ? 25.80500  -17.61500 4.35300  1.000 70.89170  ?  179 PRO A HG2    1 
ATOM   2819 H HG3    . PRO A 1 179 ? 26.44300  -17.71400 2.90100  1.000 70.89170  ?  179 PRO A HG3    1 
ATOM   2820 H HD2    . PRO A 1 179 ? 24.85500  -15.62900 3.92200  1.000 69.31237  ?  179 PRO A HD2    1 
ATOM   2821 H HD3    . PRO A 1 179 ? 26.13000  -15.49500 2.98300  1.000 69.31237  ?  179 PRO A HD3    1 
ATOM   2822 N N      . PRO A 1 180 ? 21.59300  -17.77400 0.94600  1.000 58.20767  ?  180 PRO A N      1 
ATOM   2823 C CA     . PRO A 1 180 ? 20.14600  -17.57700 0.96200  1.000 58.57202  ?  180 PRO A CA     1 
ATOM   2824 C C      . PRO A 1 180 ? 19.45500  -18.66400 1.76500  1.000 60.94987  ?  180 PRO A C      1 
ATOM   2825 O O      . PRO A 1 180 ? 20.07000  -19.68700 2.10400  1.000 58.01849  ?  180 PRO A O      1 
ATOM   2826 C CB     . PRO A 1 180 ? 19.77200  -17.66800 -0.53000 1.000 61.18660  ?  180 PRO A CB     1 
ATOM   2827 C CG     . PRO A 1 180 ? 20.72100  -18.71300 -1.04900 1.000 53.71332  ?  180 PRO A CG     1 
ATOM   2828 C CD     . PRO A 1 180 ? 22.02100  -18.55100 -0.24300 1.000 59.45430  ?  180 PRO A CD     1 
ATOM   2829 H HA     . PRO A 1 180 ? 19.91300  -16.70600 1.31800  1.000 70.40419  ?  180 PRO A HA     1 
ATOM   2830 H HB2    . PRO A 1 180 ? 18.84800  -17.94700 -0.63100 1.000 73.54169  ?  180 PRO A HB2    1 
ATOM   2831 H HB3    . PRO A 1 180 ? 19.91000  -16.81400 -0.96700 1.000 73.54169  ?  180 PRO A HB3    1 
ATOM   2832 H HG2    . PRO A 1 180 ? 20.34200  -19.59500 -0.91300 1.000 64.57375  ?  180 PRO A HG2    1 
ATOM   2833 H HG3    . PRO A 1 180 ? 20.88400  -18.56400 -1.99400 1.000 64.57375  ?  180 PRO A HG3    1 
ATOM   2834 H HD2    . PRO A 1 180 ? 22.37500  -19.41500 0.01800  1.000 71.46293  ?  180 PRO A HD2    1 
ATOM   2835 H HD3    . PRO A 1 180 ? 22.68400  -18.06100 -0.75400 1.000 71.46293  ?  180 PRO A HD3    1 
ATOM   2836 N N      . PRO A 1 181 ? 18.17800  -18.48200 2.08500  1.000 56.11277  ?  181 PRO A N      1 
ATOM   2837 C CA     . PRO A 1 181 ? 17.40500  -19.57300 2.69300  1.000 56.11289  ?  181 PRO A CA     1 
ATOM   2838 C C      . PRO A 1 181 ? 17.28100  -20.74800 1.72400  1.000 54.20820  ?  181 PRO A C      1 
ATOM   2839 O O      . PRO A 1 181 ? 17.37900  -20.59700 0.50700  1.000 50.94414  ?  181 PRO A O      1 
ATOM   2840 C CB     . PRO A 1 181 ? 16.03800  -18.95300 2.98900  1.000 58.76943  ?  181 PRO A CB     1 
ATOM   2841 C CG     . PRO A 1 181 ? 16.10000  -17.52900 2.56700  1.000 61.89706  ?  181 PRO A CG     1 
ATOM   2842 C CD     . PRO A 1 181 ? 17.43800  -17.21100 2.00100  1.000 59.20245  ?  181 PRO A CD     1 
ATOM   2843 H HA     . PRO A 1 181 ? 17.80800  -19.85900 3.52800  1.000 67.45323  ?  181 PRO A HA     1 
ATOM   2844 H HB2    . PRO A 1 181 ? 15.35600  -19.42600 2.48700  1.000 70.64108  ?  181 PRO A HB2    1 
ATOM   2845 H HB3    . PRO A 1 181 ? 15.85500  -19.01700 3.93900  1.000 70.64108  ?  181 PRO A HB3    1 
ATOM   2846 H HG2    . PRO A 1 181 ? 15.41700  -17.37700 1.89500  1.000 74.39424  ?  181 PRO A HG2    1 
ATOM   2847 H HG3    . PRO A 1 181 ? 15.93200  -16.97000 3.34200  1.000 74.39424  ?  181 PRO A HG3    1 
ATOM   2848 H HD2    . PRO A 1 181 ? 17.35800  -16.92300 1.07800  1.000 71.16072  ?  181 PRO A HD2    1 
ATOM   2849 H HD3    . PRO A 1 181 ? 17.87700  -16.52500 2.52700  1.000 71.16072  ?  181 PRO A HD3    1 
ATOM   2850 N N      . ALA A 1 182 ? 17.08700  -21.93000 2.28700  1.000 50.48551  ?  182 ALA A N      1 
ATOM   2851 C CA     . ALA A 1 182 ? 16.95700  -23.12900 1.46200  1.000 53.80247  ?  182 ALA A CA     1 
ATOM   2852 C C      . ALA A 1 182 ? 15.69000  -23.06300 0.61700  1.000 57.81349  ?  182 ALA A C      1 
ATOM   2853 O O      . ALA A 1 182 ? 14.71800  -22.38400 0.96000  1.000 50.62173  ?  182 ALA A O      1 
ATOM   2854 C CB     . ALA A 1 182 ? 16.94500  -24.39200 2.32700  1.000 58.29394  ?  182 ALA A CB     1 
ATOM   2855 H H      . ALA A 1 182 ? 17.02700  -22.06800 3.13400  1.000 60.70038  ?  182 ALA A H      1 
ATOM   2856 H HA     . ALA A 1 182 ? 17.72100  -23.18800 0.86700  1.000 64.68074  ?  182 ALA A HA     1 
ATOM   2857 H HB1    . ALA A 1 182 ? 16.89300  -25.17000 1.74900  1.000 70.07050  ?  182 ALA A HB1    1 
ATOM   2858 H HB2    . ALA A 1 182 ? 17.76100  -24.42400 2.85100  1.000 70.07050  ?  182 ALA A HB2    1 
ATOM   2859 H HB3    . ALA A 1 182 ? 16.17500  -24.36500 2.91500  1.000 70.07050  ?  182 ALA A HB3    1 
ATOM   2860 N N      . GLU A 1 183 ? 15.71400  -23.77600 -0.49800 1.000 63.62850  ?  183 GLU A N      1 
ATOM   2861 C CA     . GLU A 1 183 ? 14.60000  -23.76300 -1.42900 1.000 76.99733  ?  183 GLU A CA     1 
ATOM   2862 C C      . GLU A 1 183 ? 13.43800  -24.61300 -0.91900 1.000 76.32652  ?  183 GLU A C      1 
ATOM   2863 O O      . GLU A 1 183 ? 13.62800  -25.64500 -0.26100 1.000 62.69204  ?  183 GLU A O      1 
ATOM   2864 C CB     . GLU A 1 183 ? 15.05100  -24.27900 -2.80100 1.000 83.02982  ?  183 GLU A CB     1 
ATOM   2865 C CG     . GLU A 1 183 ? 16.09900  -23.40900 -3.47200 1.000 78.70772  ?  183 GLU A CG     1 
ATOM   2866 C CD     . GLU A 1 183 ? 15.48500  -22.32600 -4.33000 1.000 80.37803  ?  183 GLU A CD     1 
ATOM   2867 O OE1    . GLU A 1 183 ? 14.65600  -22.65800 -5.20200 1.000 82.86120  ?  183 GLU A OE1    1 
ATOM   2868 O OE2    . GLU A 1 183 ? 15.82400  -21.13900 -4.12700 1.000 94.09218  -1 183 GLU A OE2    1 
ATOM   2869 H H      . GLU A 1 183 ? 16.36900  -24.27900 -0.73900 1.000 76.47197  ?  183 GLU A H      1 
ATOM   2870 H HA     . GLU A 1 183 ? 14.28200  -22.85200 -1.52700 1.000 92.51456  ?  183 GLU A HA     1 
ATOM   2871 H HB2    . GLU A 1 183 ? 15.42900  -25.16500 -2.69200 1.000 99.75356  ?  183 GLU A HB2    1 
ATOM   2872 H HB3    . GLU A 1 183 ? 14.27900  -24.31800 -3.38800 1.000 99.75356  ?  183 GLU A HB3    1 
ATOM   2873 H HG2    . GLU A 1 183 ? 16.64100  -22.98300 -2.79100 1.000 94.56703  ?  183 GLU A HG2    1 
ATOM   2874 H HG3    . GLU A 1 183 ? 16.65600  -23.96400 -4.04100 1.000 94.56703  ?  183 GLU A HG3    1 
ATOM   2875 N N      . ASP A 1 184 ? 12.22300  -24.16000 -1.23200 1.000 69.21620  ?  184 ASP A N      1 
ATOM   2876 C CA     . ASP A 1 184 ? 11.00200  -24.92400 -0.99000 1.000 72.95708  ?  184 ASP A CA     1 
ATOM   2877 C C      . ASP A 1 184 ? 10.89100  -25.38600 0.46200  1.000 61.69436  ?  184 ASP A C      1 
ATOM   2878 O O      . ASP A 1 184 ? 10.46400  -26.50500 0.75100  1.000 63.92809  ?  184 ASP A O      1 
ATOM   2879 C CB     . ASP A 1 184 ? 10.91000  -26.13000 -1.93700 1.000 70.22923  ?  184 ASP A CB     1 
ATOM   2880 C CG     . ASP A 1 184 ? 11.39500  -25.81200 -3.33600 1.000 83.54468  ?  184 ASP A CG     1 
ATOM   2881 O OD1    . ASP A 1 184 ? 11.05100  -24.72900 -3.85900 1.000 83.49816  ?  184 ASP A OD1    1 
ATOM   2882 O OD2    . ASP A 1 184 ? 12.11900  -26.65100 -3.91500 1.000 91.36367  -1 184 ASP A OD2    1 
ATOM   2883 H H      . ASP A 1 184 ? 12.07800  -23.39300 -1.59400 1.000 83.17721  ?  184 ASP A H      1 
ATOM   2884 H HA     . ASP A 1 184 ? 10.25300  -24.33300 -1.16300 1.000 87.66627  ?  184 ASP A HA     1 
ATOM   2885 H HB2    . ASP A 1 184 ? 11.45600  -26.85000 -1.58600 1.000 84.39285  ?  184 ASP A HB2    1 
ATOM   2886 H HB3    . ASP A 1 184 ? 9.98400   -26.41400 -1.99700 1.000 84.39285  ?  184 ASP A HB3    1 
ATOM   2887 N N      . MET A 1 185 ? 11.27200  -24.51500 1.38900  1.000 54.93476  ?  185 MET A N      1 
ATOM   2888 C CA     . MET A 1 185 ? 11.02500  -24.76700 2.80600  1.000 47.45801  ?  185 MET A CA     1 
ATOM   2889 C C      . MET A 1 185 ? 9.61900   -24.28100 3.14500  1.000 50.06063  ?  185 MET A C      1 
ATOM   2890 O O      . MET A 1 185 ? 9.33200   -23.08500 2.97400  1.000 46.68326  ?  185 MET A O      1 
ATOM   2891 C CB     . MET A 1 185 ? 12.05000  -24.06400 3.66900  1.000 53.59642  ?  185 MET A CB     1 
ATOM   2892 C CG     . MET A 1 185 ? 13.38200  -24.82700 3.83600  1.000 56.83695  ?  185 MET A CG     1 
ATOM   2893 S SD     . MET A 1 185 ? 13.19600  -26.60200 4.09000  1.000 53.88945  ?  185 MET A SD     1 
ATOM   2894 C CE     . MET A 1 185 ? 14.64100  -26.95400 5.05400  1.000 71.61879  ?  185 MET A CE     1 
ATOM   2895 H H      . MET A 1 185 ? 11.67400  -23.77300 1.22500  1.000 66.03949  ?  185 MET A H      1 
ATOM   2896 H HA     . MET A 1 185 ? 11.09700  -25.71600 2.99200  1.000 57.06738  ?  185 MET A HA     1 
ATOM   2897 H HB2    . MET A 1 185 ? 12.25300  -23.20400 3.26800  1.000 64.43347  ?  185 MET A HB2    1 
ATOM   2898 H HB3    . MET A 1 185 ? 11.67300  -23.93600 4.55400  1.000 64.43347  ?  185 MET A HB3    1 
ATOM   2899 H HG2    . MET A 1 185 ? 13.91500  -24.70000 3.03500  1.000 68.32211  ?  185 MET A HG2    1 
ATOM   2900 H HG3    . MET A 1 185 ? 13.85100  -24.46800 4.60600  1.000 68.32211  ?  185 MET A HG3    1 
ATOM   2901 H HE1    . MET A 1 185 ? 14.65600  -27.90000 5.26700  1.000 86.06032  ?  185 MET A HE1    1 
ATOM   2902 H HE2    . MET A 1 185 ? 15.42900  -26.71900 4.53900  1.000 86.06032  ?  185 MET A HE2    1 
ATOM   2903 H HE3    . MET A 1 185 ? 14.61100  -26.43100 5.87000  1.000 86.06032  ?  185 MET A HE3    1 
ATOM   2904 N N      . PRO A 1 186 ? 8.72700   -25.14700 3.62800  1.000 44.63719  ?  186 PRO A N      1 
ATOM   2905 C CA     . PRO A 1 186 ? 7.32200   -24.72100 3.77900  1.000 46.23283  ?  186 PRO A CA     1 
ATOM   2906 C C      . PRO A 1 186 ? 7.14800   -23.45200 4.59000  1.000 46.71415  ?  186 PRO A C      1 
ATOM   2907 O O      . PRO A 1 186 ? 6.33500   -22.60500 4.22000  1.000 45.03947  ?  186 PRO A O      1 
ATOM   2908 C CB     . PRO A 1 186 ? 6.64300   -25.92100 4.46500  1.000 52.11570  ?  186 PRO A CB     1 
ATOM   2909 C CG     . PRO A 1 186 ? 7.72200   -26.94900 4.72400  1.000 54.25024  ?  186 PRO A CG     1 
ATOM   2910 C CD     . PRO A 1 186 ? 8.91900   -26.58100 3.89800  1.000 51.11948  ?  186 PRO A CD     1 
ATOM   2911 H HA     . PRO A 1 186 ? 6.93800   -24.59900 2.89700  1.000 55.59717  ?  186 PRO A HA     1 
ATOM   2912 H HB2    . PRO A 1 186 ? 6.24200   -25.63200 5.29900  1.000 62.65661  ?  186 PRO A HB2    1 
ATOM   2913 H HB3    . PRO A 1 186 ? 5.96100   -26.28500 3.87800  1.000 62.65661  ?  186 PRO A HB3    1 
ATOM   2914 H HG2    . PRO A 1 186 ? 7.95000   -26.94100 5.66700  1.000 65.21806  ?  186 PRO A HG2    1 
ATOM   2915 H HG3    . PRO A 1 186 ? 7.39500   -27.82600 4.46900  1.000 65.21806  ?  186 PRO A HG3    1 
ATOM   2916 H HD2    . PRO A 1 186 ? 9.73900   -26.73100 4.39400  1.000 61.46115  ?  186 PRO A HD2    1 
ATOM   2917 H HD3    . PRO A 1 186 ? 8.93500   -27.08800 3.07100  1.000 61.46115  ?  186 PRO A HD3    1 
ATOM   2918 N N      . SER A 1 187 ? 7.91900   -23.27800 5.67000  1.000 44.50877  ?  187 SER A N      1 
ATOM   2919 C CA     . SER A 1 187 ? 7.75800   -22.11100 6.52800  1.000 46.95819  ?  187 SER A CA     1 
ATOM   2920 C C      . SER A 1 187 ? 8.36800   -20.84800 5.93700  1.000 46.61528  ?  187 SER A C      1 
ATOM   2921 O O      . SER A 1 187 ? 8.13800   -19.76200 6.47300  1.000 45.97857  ?  187 SER A O      1 
ATOM   2922 C CB     . SER A 1 187 ? 8.38200   -22.38300 7.90100  1.000 51.62775  ?  187 SER A CB     1 
ATOM   2923 O OG     . SER A 1 187 ? 7.71200   -23.46600 8.53900  1.000 51.00224  ?  187 SER A OG     1 
ATOM   2924 H H      . SER A 1 187 ? 8.53700   -23.82200 5.92100  1.000 53.52829  ?  187 SER A H      1 
ATOM   2925 H HA     . SER A 1 187 ? 6.81000   -21.94900 6.65400  1.000 56.46760  ?  187 SER A HA     1 
ATOM   2926 H HB2    . SER A 1 187 ? 9.31800   -22.61100 7.78600  1.000 62.07107  ?  187 SER A HB2    1 
ATOM   2927 H HB3    . SER A 1 187 ? 8.29900   -21.58900 8.45200  1.000 62.07107  ?  187 SER A HB3    1 
ATOM   2928 H HG     . SER A 1 187 ? 8.13600   -23.70200 9.22500  1.000 61.32046  ?  187 SER A HG     1 
ATOM   2929 N N      . ALA A 1 188 ? 9.12700   -20.96000 4.84400  1.000 47.38627  ?  188 ALA A N      1 
ATOM   2930 C CA     . ALA A 1 188 ? 9.71200   -19.80900 4.18100  1.000 46.30259  ?  188 ALA A CA     1 
ATOM   2931 C C      . ALA A 1 188 ? 8.96800   -19.41700 2.91000  1.000 46.98198  ?  188 ALA A C      1 
ATOM   2932 O O      . ALA A 1 188 ? 9.48800   -18.62700 2.11900  1.000 48.11727  ?  188 ALA A O      1 
ATOM   2933 C CB     . ALA A 1 188 ? 11.18700  -20.08700 3.85700  1.000 46.59859  ?  188 ALA A CB     1 
ATOM   2934 H H      . ALA A 1 188 ? 9.31700   -21.70900 4.46600  1.000 56.98130  ?  188 ALA A H      1 
ATOM   2935 H HA     . ALA A 1 188 ? 9.67300   -19.05300 4.78700  1.000 55.68087  ?  188 ALA A HA     1 
ATOM   2936 H HB1    . ALA A 1 188 ? 11.57200  -19.30200 3.43700  1.000 56.03607  ?  188 ALA A HB1    1 
ATOM   2937 H HB2    . ALA A 1 188 ? 11.65900  -20.28700 4.68000  1.000 56.03607  ?  188 ALA A HB2    1 
ATOM   2938 H HB3    . ALA A 1 188 ? 11.24000  -20.84400 3.25300  1.000 56.03607  ?  188 ALA A HB3    1 
ATOM   2939 N N      . ALA A 1 189 ? 7.76200   -19.94600 2.69500  1.000 45.61648  ?  189 ALA A N      1 
ATOM   2940 C CA     . ALA A 1 189 ? 7.02200   -19.63500 1.48100  1.000 50.32537  ?  189 ALA A CA     1 
ATOM   2941 C C      . ALA A 1 189 ? 6.78600   -18.12300 1.38500  1.000 51.95718  ?  189 ALA A C      1 
ATOM   2942 O O      . ALA A 1 189 ? 6.37400   -17.50000 2.37000  1.000 45.53225  ?  189 ALA A O      1 
ATOM   2943 C CB     . ALA A 1 189 ? 5.68700   -20.37500 1.47400  1.000 48.54938  ?  189 ALA A CB     1 
ATOM   2944 H H      . ALA A 1 189 ? 7.35800   -20.48200 3.23300  1.000 54.85755  ?  189 ALA A H      1 
ATOM   2945 H HA     . ALA A 1 189 ? 7.53500   -19.91800 0.70800  1.000 60.50821  ?  189 ALA A HA     1 
ATOM   2946 H HB1    . ALA A 1 189 ? 5.20200   -20.14300 0.66600  1.000 58.37703  ?  189 ALA A HB1    1 
ATOM   2947 H HB2    . ALA A 1 189 ? 5.85500   -21.33000 1.49600  1.000 58.37703  ?  189 ALA A HB2    1 
ATOM   2948 H HB3    . ALA A 1 189 ? 5.17500   -20.11100 2.25400  1.000 58.37703  ?  189 ALA A HB3    1 
ATOM   2949 N N      . PRO A 1 190 ? 7.03100   -17.50300 0.21800  1.000 52.37320  ?  190 PRO A N      1 
ATOM   2950 C CA     . PRO A 1 190 ? 6.88200   -16.04300 0.12400  1.000 49.49297  ?  190 PRO A CA     1 
ATOM   2951 C C      . PRO A 1 190 ? 5.53700   -15.49600 0.58500  1.000 49.86464  ?  190 PRO A C      1 
ATOM   2952 O O      . PRO A 1 190 ? 5.50100   -14.46400 1.25400  1.000 45.01683  ?  190 PRO A O      1 
ATOM   2953 C CB     . PRO A 1 190 ? 7.09000   -15.76400 -1.37700 1.000 52.71412  ?  190 PRO A CB     1 
ATOM   2954 C CG     . PRO A 1 190 ? 7.78500   -16.98500 -1.94300 1.000 61.06378  ?  190 PRO A CG     1 
ATOM   2955 C CD     . PRO A 1 190 ? 7.82200   -18.06600 -0.90200 1.000 52.44843  ?  190 PRO A CD     1 
ATOM   2956 H HA     . PRO A 1 190 ? 7.58700   -15.63700 0.65200  1.000 59.50934  ?  190 PRO A HA     1 
ATOM   2957 H HB2    . PRO A 1 190 ? 6.23000   -15.63100 -1.80600 1.000 63.37471  ?  190 PRO A HB2    1 
ATOM   2958 H HB3    . PRO A 1 190 ? 7.64200   -14.97400 -1.48800 1.000 63.37471  ?  190 PRO A HB3    1 
ATOM   2959 H HG2    . PRO A 1 190 ? 7.29300   -17.29200 -2.72100 1.000 73.39431  ?  190 PRO A HG2    1 
ATOM   2960 H HG3    . PRO A 1 190 ? 8.68800   -16.74000 -2.19700 1.000 73.39431  ?  190 PRO A HG3    1 
ATOM   2961 H HD2    . PRO A 1 190 ? 7.41300   -18.87900 -1.23700 1.000 63.05588  ?  190 PRO A HD2    1 
ATOM   2962 H HD3    . PRO A 1 190 ? 8.73400   -18.24300 -0.62300 1.000 63.05588  ?  190 PRO A HD3    1 
ATOM   2963 N N      . ALA A 1 191 ? 4.42600   -16.16600 0.25500  1.000 51.21016  ?  191 ALA A N      1 
ATOM   2964 C CA     . ALA A 1 191 ? 3.11500   -15.59400 0.55600  1.000 48.64208  ?  191 ALA A CA     1 
ATOM   2965 C C      . ALA A 1 191 ? 2.87500   -15.49200 2.05700  1.000 48.72060  ?  191 ALA A C      1 
ATOM   2966 O O      . ALA A 1 191 ? 2.08600   -14.65900 2.49900  1.000 48.17490  ?  191 ALA A O      1 
ATOM   2967 C CB     . ALA A 1 191 ? 2.00600   -16.43300 -0.09400 1.000 53.55241  ?  191 ALA A CB     1 
ATOM   2968 H H      . ALA A 1 191 ? 4.40600   -16.93300 -0.13400 1.000 61.56996  ?  191 ALA A H      1 
ATOM   2969 H HA     . ALA A 1 191 ? 3.07900   -14.70000 0.18100  1.000 58.48827  ?  191 ALA A HA     1 
ATOM   2970 H HB1    . ALA A 1 191 ? 1.14400   -16.05700 0.14500  1.000 64.38066  ?  191 ALA A HB1    1 
ATOM   2971 H HB2    . ALA A 1 191 ? 2.11900   -16.41500 -1.05700 1.000 64.38066  ?  191 ALA A HB2    1 
ATOM   2972 H HB3    . ALA A 1 191 ? 2.06900   -17.34600 0.22900  1.000 64.38066  ?  191 ALA A HB3    1 
ATOM   2973 N N      . ALA A 1 192 ? 3.53500   -16.33100 2.85200  1.000 51.35388  ?  192 ALA A N      1 
ATOM   2974 C CA     . ALA A 1 192 ? 3.37500   -16.31000 4.29600  1.000 49.35976  ?  192 ALA A CA     1 
ATOM   2975 C C      . ALA A 1 192 ? 4.43600   -15.47800 5.00300  1.000 45.89101  ?  192 ALA A C      1 
ATOM   2976 O O      . ALA A 1 192 ? 4.41900   -15.40700 6.24100  1.000 46.48645  ?  192 ALA A O      1 
ATOM   2977 C CB     . ALA A 1 192 ? 3.39800   -17.74500 4.84100  1.000 45.32889  ?  192 ALA A CB     1 
ATOM   2978 H H      . ALA A 1 192 ? 4.08800   -16.92700 2.57100  1.000 61.74242  ?  192 ALA A H      1 
ATOM   2979 H HA     . ALA A 1 192 ? 2.51200   -15.92000 4.50500  1.000 59.34949  ?  192 ALA A HA     1 
ATOM   2980 H HB1    . ALA A 1 192 ? 3.29100   -17.71800 5.80500  1.000 54.51244  ?  192 ALA A HB1    1 
ATOM   2981 H HB2    . ALA A 1 192 ? 2.67100   -18.24700 4.44100  1.000 54.51244  ?  192 ALA A HB2    1 
ATOM   2982 H HB3    . ALA A 1 192 ? 4.24700   -18.15500 4.61400  1.000 54.51244  ?  192 ALA A HB3    1 
ATOM   2983 N N      . THR A 1 193 ? 5.35100   -14.84500 4.26000  1.000 48.81409  ?  193 THR A N      1 
ATOM   2984 C CA     . THR A 1 193 ? 6.51200   -14.20800 4.87800  1.000 45.26663  ?  193 THR A CA     1 
ATOM   2985 C C      . THR A 1 193 ? 6.81900   -12.82800 4.32600  1.000 45.30436  ?  193 THR A C      1 
ATOM   2986 O O      . THR A 1 193 ? 7.92100   -12.30700 4.57400  1.000 42.68845  ?  193 THR A O      1 
ATOM   2987 C CB     . THR A 1 193 ? 7.75100   -15.10200 4.71400  1.000 49.23708  ?  193 THR A CB     1 
ATOM   2988 O OG1    . THR A 1 193 ? 8.00500   -15.32700 3.31600  1.000 47.75789  ?  193 THR A OG1    1 
ATOM   2989 C CG2    . THR A 1 193 ? 7.53700   -16.42500 5.40800  1.000 45.68472  ?  193 THR A CG2    1 
ATOM   2990 H H      . THR A 1 193 ? 5.32000   -14.77300 3.40300  1.000 58.69468  ?  193 THR A H      1 
ATOM   2991 H HA     . THR A 1 193 ? 6.32300   -14.09800 5.82300  1.000 54.43772  ?  193 THR A HA     1 
ATOM   2992 H HB     . THR A 1 193 ? 8.52100   -14.66700 5.11200  1.000 59.20226  ?  193 THR A HB     1 
ATOM   2993 H HG1    . THR A 1 193 ? 8.65200   -15.85500 3.22300  1.000 57.42723  ?  193 THR A HG1    1 
ATOM   2994 H HG21   . THR A 1 193 ? 8.33600   -16.97000 5.33500  1.000 54.93944  ?  193 THR A HG21   1 
ATOM   2995 H HG22   . THR A 1 193 ? 7.34000   -16.28000 6.34600  1.000 54.93944  ?  193 THR A HG22   1 
ATOM   2996 H HG23   . THR A 1 193 ? 6.79600   -16.89800 5.00000  1.000 54.93944  ?  193 THR A HG23   1 
ATOM   2997 N N      . GLY A 1 194 ? 5.88800   -12.20000 3.58500  1.000 47.01559  ?  194 GLY A N      1 
ATOM   2998 C CA     . GLY A 1 194 ? 6.12100   -10.85400 3.11400  1.000 42.55975  ?  194 GLY A CA     1 
ATOM   2999 C C      . GLY A 1 194 ? 5.88300   -9.79400  4.18800  1.000 47.21222  ?  194 GLY A C      1 
ATOM   3000 O O      . GLY A 1 194 ? 5.28200   -10.04400 5.23700  1.000 40.70833  ?  194 GLY A O      1 
ATOM   3001 H H      . GLY A 1 194 ? 5.13200   -12.53800 3.35300  1.000 56.53648  ?  194 GLY A H      1 
ATOM   3002 H HA2    . GLY A 1 194 ? 7.03900   -10.77700 2.81000  1.000 51.18947  ?  194 GLY A HA2    1 
ATOM   3003 H HA3    . GLY A 1 194 ? 5.52500   -10.67000 2.37000  1.000 51.18947  ?  194 GLY A HA3    1 
ATOM   3004 N N      . VAL A 1 195 ? 6.37200   -8.58800  3.91300  1.000 44.93205  ?  195 VAL A N      1 
ATOM   3005 C CA     . VAL A 1 195 ? 6.14500   -7.44500  4.79400  1.000 48.67181  ?  195 VAL A CA     1 
ATOM   3006 C C      . VAL A 1 195 ? 4.74600   -6.90000  4.53200  1.000 44.38479  ?  195 VAL A C      1 
ATOM   3007 O O      . VAL A 1 195 ? 4.43400   -6.53600  3.39200  1.000 44.93203  ?  195 VAL A O      1 
ATOM   3008 C CB     . VAL A 1 195 ? 7.19800   -6.35100  4.57600  1.000 52.80871  ?  195 VAL A CB     1 
ATOM   3009 C CG1    . VAL A 1 195 ? 6.84500   -5.11000  5.40700  1.000 54.57641  ?  195 VAL A CG1    1 
ATOM   3010 C CG2    . VAL A 1 195 ? 8.59100   -6.85600  4.94000  1.000 43.94576  ?  195 VAL A CG2    1 
ATOM   3011 H H      . VAL A 1 195 ? 6.84200   -8.40400  3.21600  1.000 54.03623  ?  195 VAL A H      1 
ATOM   3012 H HA     . VAL A 1 195 ? 6.20000   -7.74400  5.71500  1.000 58.52394  ?  195 VAL A HA     1 
ATOM   3013 H HB     . VAL A 1 195 ? 7.20700   -6.10700  3.63800  1.000 63.48822  ?  195 VAL A HB     1 
ATOM   3014 H HG11   . VAL A 1 195 ? 7.62100   -4.53100  5.45600  1.000 65.60946  ?  195 VAL A HG11   1 
ATOM   3015 H HG12   . VAL A 1 195 ? 6.11000   -4.64300  4.98000  1.000 65.60946  ?  195 VAL A HG12   1 
ATOM   3016 H HG13   . VAL A 1 195 ? 6.58500   -5.39100  6.29900  1.000 65.60946  ?  195 VAL A HG13   1 
ATOM   3017 H HG21   . VAL A 1 195 ? 9.24000   -6.16200  4.74100  1.000 52.85268  ?  195 VAL A HG21   1 
ATOM   3018 H HG22   . VAL A 1 195 ? 8.61300   -7.06800  5.88600  1.000 52.85268  ?  195 VAL A HG22   1 
ATOM   3019 H HG23   . VAL A 1 195 ? 8.78500   -7.65000  4.41700  1.000 52.85268  ?  195 VAL A HG23   1 
ATOM   3020 N N      . PRO A 1 196 ? 3.88000   -6.82600  5.53400  1.000 47.64324  ?  196 PRO A N      1 
ATOM   3021 C CA     . PRO A 1 196 ? 2.52600   -6.29400  5.30700  1.000 53.81455  ?  196 PRO A CA     1 
ATOM   3022 C C      . PRO A 1 196 ? 2.50500   -4.76800  5.30500  1.000 55.08533  ?  196 PRO A C      1 
ATOM   3023 O O      . PRO A 1 196 ? 3.45600   -4.10000  5.70500  1.000 52.97130  ?  196 PRO A O      1 
ATOM   3024 C CB     . PRO A 1 196 ? 1.73500   -6.85200  6.49100  1.000 56.78822  ?  196 PRO A CB     1 
ATOM   3025 C CG     . PRO A 1 196 ? 2.75100   -6.91100  7.59400  1.000 52.15636  ?  196 PRO A CG     1 
ATOM   3026 C CD     . PRO A 1 196 ? 4.06400   -7.27400  6.92500  1.000 48.15719  ?  196 PRO A CD     1 
ATOM   3027 H HA     . PRO A 1 196 ? 2.16100   -6.62300  4.47100  1.000 64.69522  ?  196 PRO A HA     1 
ATOM   3028 H HB2    . PRO A 1 196 ? 1.00300   -6.25700  6.71700  1.000 68.26364  ?  196 PRO A HB2    1 
ATOM   3029 H HB3    . PRO A 1 196 ? 1.39200   -7.73500  6.28100  1.000 68.26364  ?  196 PRO A HB3    1 
ATOM   3030 H HG2    . PRO A 1 196 ? 2.81300   -6.04600  8.02800  1.000 62.70540  ?  196 PRO A HG2    1 
ATOM   3031 H HG3    . PRO A 1 196 ? 2.49500   -7.58800  8.23900  1.000 62.70540  ?  196 PRO A HG3    1 
ATOM   3032 H HD2    . PRO A 1 196 ? 4.80400   -6.80500  7.34200  1.000 57.90640  ?  196 PRO A HD2    1 
ATOM   3033 H HD3    . PRO A 1 196 ? 4.21600   -8.23100  6.96100  1.000 57.90640  ?  196 PRO A HD3    1 
ATOM   3034 N N      . THR A 1 197 ? 1.38800   -4.22900  4.82300  1.000 59.86102  ?  197 THR A N      1 
ATOM   3035 C CA     . THR A 1 197 ? 1.13500   -2.79600  4.83200  1.000 66.72613  ?  197 THR A CA     1 
ATOM   3036 C C      . THR A 1 197 ? 0.33000   -2.41400  6.07400  1.000 60.85322  ?  197 THR A C      1 
ATOM   3037 O O      . THR A 1 197 ? -0.25300  -3.26200  6.75300  1.000 56.97794  ?  197 THR A O      1 
ATOM   3038 C CB     . THR A 1 197 ? 0.37300   -2.36200  3.57400  1.000 69.46274  ?  197 THR A CB     1 
ATOM   3039 O OG1    . THR A 1 197 ? -0.96800  -2.87700  3.61800  1.000 60.23622  ?  197 THR A OG1    1 
ATOM   3040 C CG2    . THR A 1 197 ? 1.06800   -2.86700  2.31300  1.000 66.63112  ?  197 THR A CG2    1 
ATOM   3041 H H      . THR A 1 197 ? 0.74700   -4.68600  4.47700  1.000 71.95099  ?  197 THR A H      1 
ATOM   3042 H HA     . THR A 1 197 ? 1.98600   -2.33100  4.84500  1.000 80.18912  ?  197 THR A HA     1 
ATOM   3043 H HB     . THR A 1 197 ? 0.34600   -1.39400  3.53700  1.000 83.47306  ?  197 THR A HB     1 
ATOM   3044 H HG1    . THR A 1 197 ? -1.38900  -2.63900  2.93100  1.000 72.40123  ?  197 THR A HG1    1 
ATOM   3045 H HG21   . THR A 1 197 ? 0.57900   -2.57900  1.52700  1.000 80.07512  ?  197 THR A HG21   1 
ATOM   3046 H HG22   . THR A 1 197 ? 1.97100   -2.51500  2.26900  1.000 80.07512  ?  197 THR A HG22   1 
ATOM   3047 H HG23   . THR A 1 197 ? 1.10800   -3.83600  2.32200  1.000 80.07512  ?  197 THR A HG23   1 
ATOM   3048 N N      . TRP A 1 198 ? 0.29300   -1.11200  6.36600  1.000 58.67169  ?  198 TRP A N      1 
ATOM   3049 C CA     . TRP A 1 198 ? -0.47100  -0.66700  7.53400  1.000 63.42837  ?  198 TRP A CA     1 
ATOM   3050 C C      . TRP A 1 198 ? -1.95000  -1.00600  7.38600  1.000 59.57667  ?  198 TRP A C      1 
ATOM   3051 O O      . TRP A 1 198 ? -2.62600  -1.27200  8.38500  1.000 60.11805  ?  198 TRP A O      1 
ATOM   3052 C CB     . TRP A 1 198 ? -0.27300  0.83800   7.76700  1.000 54.80028  ?  198 TRP A CB     1 
ATOM   3053 C CG     . TRP A 1 198 ? -0.73900  1.73000   6.67300  1.000 49.92439  ?  198 TRP A CG     1 
ATOM   3054 C CD1    . TRP A 1 198 ? 0.01200   2.23400   5.64800  1.000 47.98736  ?  198 TRP A CD1    1 
ATOM   3055 C CD2    . TRP A 1 198 ? -2.06500  2.25300   6.49500  1.000 57.06829  ?  198 TRP A CD2    1 
ATOM   3056 N NE1    . TRP A 1 198 ? -0.76500  3.02900   4.83800  1.000 52.38618  ?  198 TRP A NE1    1 
ATOM   3057 C CE2    . TRP A 1 198 ? -2.04600  3.05500   5.33700  1.000 53.61394  ?  198 TRP A CE2    1 
ATOM   3058 C CE3    . TRP A 1 198 ? -3.26300  2.11200   7.19900  1.000 61.43263  ?  198 TRP A CE3    1 
ATOM   3059 C CZ2    . TRP A 1 198 ? -3.17900  3.72000   4.86600  1.000 59.69684  ?  198 TRP A CZ2    1 
ATOM   3060 C CZ3    . TRP A 1 198 ? -4.39500  2.77300   6.73100  1.000 61.83084  ?  198 TRP A CZ3    1 
ATOM   3061 C CH2    . TRP A 1 198 ? -4.34100  3.56600   5.57400  1.000 61.53277  ?  198 TRP A CH2    1 
ATOM   3062 H H      . TRP A 1 198 ? 0.68700   -0.48900  5.92200  1.000 70.52379  ?  198 TRP A H      1 
ATOM   3063 H HA     . TRP A 1 198 ? -0.13600  -1.12400  8.32100  1.000 76.23181  ?  198 TRP A HA     1 
ATOM   3064 H HB2    . TRP A 1 198 ? -0.75900  1.08800   8.56800  1.000 65.87811  ?  198 TRP A HB2    1 
ATOM   3065 H HB3    . TRP A 1 198 ? 0.67500   1.00400   7.88800  1.000 65.87811  ?  198 TRP A HB3    1 
ATOM   3066 H HD1    . TRP A 1 198 ? 0.91700   2.06500   5.51700  1.000 57.70261  ?  198 TRP A HD1    1 
ATOM   3067 H HE1    . TRP A 1 198 ? -0.49400  3.44200   4.13400  1.000 62.98119  ?  198 TRP A HE1    1 
ATOM   3068 H HE3    . TRP A 1 198 ? -3.30400  1.58700   7.96600  1.000 73.83692  ?  198 TRP A HE3    1 
ATOM   3069 H HZ2    . TRP A 1 198 ? -3.14700  4.24700   4.10100  1.000 71.75397  ?  198 TRP A HZ2    1 
ATOM   3070 H HZ3    . TRP A 1 198 ? -5.19800  2.68800   7.19200  1.000 74.31478  ?  198 TRP A HZ3    1 
ATOM   3071 H HH2    . TRP A 1 198 ? -5.11200  3.99600   5.28200  1.000 73.95709  ?  198 TRP A HH2    1 
ATOM   3072 N N      . GLN A 1 199 ? -2.46500  -1.01300  6.15100  1.000 62.10906  ?  199 GLN A N      1 
ATOM   3073 C CA     . GLN A 1 199 ? -3.84600  -1.44100  5.93500  1.000 68.79806  ?  199 GLN A CA     1 
ATOM   3074 C C      . GLN A 1 199 ? -4.04200  -2.90900  6.31400  1.000 71.21757  ?  199 GLN A C      1 
ATOM   3075 O O      . GLN A 1 199 ? -5.02500  -3.25900  6.98700  1.000 63.98835  ?  199 GLN A O      1 
ATOM   3076 C CB     . GLN A 1 199 ? -4.23800  -1.22100  4.47400  1.000 72.19810  ?  199 GLN A CB     1 
ATOM   3077 C CG     . GLN A 1 199 ? -4.23300  0.24200   4.03900  1.000 74.91498  ?  199 GLN A CG     1 
ATOM   3078 C CD     . GLN A 1 199 ? -3.15500  0.55300   3.00600  1.000 80.52463  ?  199 GLN A CD     1 
ATOM   3079 O OE1    . GLN A 1 199 ? -2.04300  0.01000   3.05700  1.000 69.71707  ?  199 GLN A OE1    1 
ATOM   3080 N NE2    . GLN A 1 199 ? -3.47700  1.43700   2.06700  1.000 71.95532  ?  199 GLN A NE2    1 
ATOM   3081 H H      . GLN A 1 199 ? -2.04400  -0.78000  5.43800  1.000 74.64864  ?  199 GLN A H      1 
ATOM   3082 H HA     . GLN A 1 199 ? -4.42800  -0.90400  6.49500  1.000 82.67544  ?  199 GLN A HA     1 
ATOM   3083 H HB2    . GLN A 1 199 ? -3.61000  -1.69800  3.91000  1.000 86.75549  ?  199 GLN A HB2    1 
ATOM   3084 H HB3    . GLN A 1 199 ? -5.13400  -1.56600  4.33800  1.000 86.75549  ?  199 GLN A HB3    1 
ATOM   3085 H HG2    . GLN A 1 199 ? -5.09400  0.45600   3.64700  1.000 90.01575  ?  199 GLN A HG2    1 
ATOM   3086 H HG3    . GLN A 1 199 ? -4.07300  0.80100   4.81600  1.000 90.01575  ?  199 GLN A HG3    1 
ATOM   3087 H HE21   . GLN A 1 199 ? -4.25800  1.79800   2.06700  1.000 86.46415  ?  199 GLN A HE21   1 
ATOM   3088 H HE22   . GLN A 1 199 ? -2.90600  1.64800   1.46000  1.000 86.46415  ?  199 GLN A HE22   1 
ATOM   3089 N N      . GLU A 1 200 ? -3.11800  -3.77600  5.90800  1.000 66.96244  ?  200 GLU A N      1 
ATOM   3090 C CA     . GLU A 1 200 ? -3.30300  -5.20900  6.14500  1.000 72.89154  ?  200 GLU A CA     1 
ATOM   3091 C C      . GLU A 1 200 ? -3.27400  -5.55200  7.62800  1.000 70.48640  ?  200 GLU A C      1 
ATOM   3092 O O      . GLU A 1 200 ? -3.93600  -6.50600  8.04800  1.000 72.24839  ?  200 GLU A O      1 
ATOM   3093 C CB     . GLU A 1 200 ? -2.22200  -6.01600  5.41900  1.000 67.39784  ?  200 GLU A CB     1 
ATOM   3094 C CG     . GLU A 1 200 ? -2.27100  -5.89800  3.90800  1.000 81.86227  ?  200 GLU A CG     1 
ATOM   3095 C CD     . GLU A 1 200 ? -0.98200  -6.36600  3.25900  1.000 78.23701  ?  200 GLU A CD     1 
ATOM   3096 O OE1    . GLU A 1 200 ? -0.29800  -7.22800  3.85300  1.000 76.59147  ?  200 GLU A OE1    1 
ATOM   3097 O OE2    . GLU A 1 200 ? -0.65800  -5.87500  2.15800  1.000 84.53122  -1 200 GLU A OE2    1 
ATOM   3098 H H      . GLU A 1 200 ? -2.39000  -3.56900  5.50200  1.000 80.47269  ?  200 GLU A H      1 
ATOM   3099 H HA     . GLU A 1 200 ? -4.17000  -5.45800  5.78800  1.000 87.58762  ?  200 GLU A HA     1 
ATOM   3100 H HB2    . GLU A 1 200 ? -1.35200  -5.70300  5.71100  1.000 80.99518  ?  200 GLU A HB2    1 
ATOM   3101 H HB3    . GLU A 1 200 ? -2.33100  -6.95300  5.64400  1.000 80.99518  ?  200 GLU A HB3    1 
ATOM   3102 H HG2    . GLU A 1 200 ? -2.99700  -6.44400  3.56800  1.000 98.35250  ?  200 GLU A HG2    1 
ATOM   3103 H HG3    . GLU A 1 200 ? -2.41300  -4.96900  3.66500  1.000 98.35250  ?  200 GLU A HG3    1 
ATOM   3104 N N      . VAL A 1 201 ? -2.50700  -4.80600  8.43400  1.000 62.65737  ?  201 VAL A N      1 
ATOM   3105 C CA     . VAL A 1 201 ? -2.43600  -5.11400  9.86400  1.000 68.89901  ?  201 VAL A CA     1 
ATOM   3106 C C      . VAL A 1 201 ? -3.66300  -4.63600  10.62900 1.000 65.02956  ?  201 VAL A C      1 
ATOM   3107 O O      . VAL A 1 201 ? -3.79400  -4.95000  11.81900 1.000 69.21857  ?  201 VAL A O      1 
ATOM   3108 C CB     . VAL A 1 201 ? -1.17800  -4.50600  10.51500 1.000 71.85639  ?  201 VAL A CB     1 
ATOM   3109 C CG1    . VAL A 1 201 ? 0.07600   -5.17900  9.95500  1.000 70.94716  ?  201 VAL A CG1    1 
ATOM   3110 C CG2    . VAL A 1 201 ? -1.12000  -2.99900  10.29500 1.000 63.85939  ?  201 VAL A CG2    1 
ATOM   3111 H H      . VAL A 1 201 ? -2.03200  -4.13400  8.18300  1.000 75.30661  ?  201 VAL A H      1 
ATOM   3112 H HA     . VAL A 1 201 ? -2.38200  -6.07900  9.94700  1.000 82.79658  ?  201 VAL A HA     1 
ATOM   3113 H HB     . VAL A 1 201 ? -1.21600  -4.66100  11.47200 1.000 86.34544  ?  201 VAL A HB     1 
ATOM   3114 H HG11   . VAL A 1 201 ? 0.85700   -4.80700  10.39400 1.000 85.25436  ?  201 VAL A HG11   1 
ATOM   3115 H HG12   . VAL A 1 201 ? 0.02500   -6.13300  10.12500 1.000 85.25436  ?  201 VAL A HG12   1 
ATOM   3116 H HG13   . VAL A 1 201 ? 0.12300   -5.01500  9.00100  1.000 85.25436  ?  201 VAL A HG13   1 
ATOM   3117 H HG21   . VAL A 1 201 ? -0.37600  -2.63500  10.79900 1.000 76.74903  ?  201 VAL A HG21   1 
ATOM   3118 H HG22   . VAL A 1 201 ? -0.99600  -2.82300  9.34900  1.000 76.74903  ?  201 VAL A HG22   1 
ATOM   3119 H HG23   . VAL A 1 201 ? -1.95100  -2.60300  10.59900 1.000 76.74903  ?  201 VAL A HG23   1 
ATOM   3120 N N      . GLY A 1 202 ? -4.55700  -3.89100  9.98500  1.000 62.45968  ?  202 GLY A N      1 
ATOM   3121 C CA     . GLY A 1 202 ? -5.81900  -3.50500  10.58900 1.000 76.04564  ?  202 GLY A CA     1 
ATOM   3122 C C      . GLY A 1 202 ? -6.02300  -2.01800  10.79300 1.000 74.44574  ?  202 GLY A C      1 
ATOM   3123 O O      . GLY A 1 202 ? -7.10700  -1.62200  11.25000 1.000 78.59258  ?  202 GLY A O      1 
ATOM   3124 H H      . GLY A 1 202 ? -4.45000  -3.59500  9.18500  1.000 75.06938  ?  202 GLY A H      1 
ATOM   3125 H HA2    . GLY A 1 202 ? -6.54000  -3.82400  10.02300 1.000 91.37254  ?  202 GLY A HA2    1 
ATOM   3126 H HA3    . GLY A 1 202 ? -5.88700  -3.93100  11.45700 1.000 91.37254  ?  202 GLY A HA3    1 
ATOM   3127 N N      . PHE A 1 203 ? -5.05700  -1.16000  10.47900 1.000 68.47605  ?  203 PHE A N      1 
ATOM   3128 C CA     . PHE A 1 203 ? -5.23400  0.26800   10.71400 1.000 72.58940  ?  203 PHE A CA     1 
ATOM   3129 C C      . PHE A 1 203 ? -6.21100  0.86500   9.71500  1.000 67.37448  ?  203 PHE A C      1 
ATOM   3130 O O      . PHE A 1 203 ? -6.23000  0.48400   8.54000  1.000 68.17202  ?  203 PHE A O      1 
ATOM   3131 C CB     . PHE A 1 203 ? -3.88500  0.98600   10.62000 1.000 67.15362  ?  203 PHE A CB     1 
ATOM   3132 C CG     . PHE A 1 203 ? -2.98400  0.72100   11.78300 1.000 61.67356  ?  203 PHE A CG     1 
ATOM   3133 C CD1    . PHE A 1 203 ? -3.29200  1.22500   13.03900 1.000 62.84300  ?  203 PHE A CD1    1 
ATOM   3134 C CD2    . PHE A 1 203 ? -1.83300  -0.02900  11.62800 1.000 62.38804  ?  203 PHE A CD2    1 
ATOM   3135 C CE1    . PHE A 1 203 ? -2.46600  0.97900   14.11900 1.000 64.89958  ?  203 PHE A CE1    1 
ATOM   3136 C CE2    . PHE A 1 203 ? -0.99900  -0.27600  12.70200 1.000 61.84043  ?  203 PHE A CE2    1 
ATOM   3137 C CZ     . PHE A 1 203 ? -1.31300  0.22700   13.94800 1.000 59.94052  ?  203 PHE A CZ     1 
ATOM   3138 H H      . PHE A 1 203 ? -4.30000  -1.37700  10.13200 1.000 82.28903  ?  203 PHE A H      1 
ATOM   3139 H HA     . PHE A 1 203 ? -5.59400  0.40500   11.60400 1.000 87.22505  ?  203 PHE A HA     1 
ATOM   3140 H HB2    . PHE A 1 203 ? -3.42800  0.68900   9.81800  1.000 80.70211  ?  203 PHE A HB2    1 
ATOM   3141 H HB3    . PHE A 1 203 ? -4.04200  1.94200   10.57800 1.000 80.70211  ?  203 PHE A HB3    1 
ATOM   3142 H HD1    . PHE A 1 203 ? -4.06300  1.73300   13.15500 1.000 75.52937  ?  203 PHE A HD1    1 
ATOM   3143 H HD2    . PHE A 1 203 ? -1.61800  -0.37100  10.79000 1.000 74.98342  ?  203 PHE A HD2    1 
ATOM   3144 H HE1    . PHE A 1 203 ? -2.68200  1.31700   14.95800 1.000 77.99726  ?  203 PHE A HE1    1 
ATOM   3145 H HE2    . PHE A 1 203 ? -0.22600  -0.78000  12.58500 1.000 74.32629  ?  203 PHE A HE2    1 
ATOM   3146 H HZ     . PHE A 1 203 ? -0.75300  0.06100   14.67200 1.000 72.04639  ?  203 PHE A HZ     1 
ATOM   3147 N N      . LYS A 1 204 ? -7.02300  1.81500   10.19200 1.000 68.22539  ?  204 LYS A N      1 
ATOM   3148 C CA     . LYS A 1 204 ? -8.03100  2.48200   9.37500  1.000 71.37929  ?  204 LYS A CA     1 
ATOM   3149 C C      . LYS A 1 204 ? -7.59000  3.86200   8.89500  1.000 75.42633  ?  204 LYS A C      1 
ATOM   3150 O O      . LYS A 1 204 ? -7.89900  4.24500   7.76000  1.000 68.25579  ?  204 LYS A O      1 
ATOM   3151 C CB     . LYS A 1 204 ? -9.33900  2.63400   10.16500 1.000 75.01407  ?  204 LYS A CB     1 
ATOM   3152 C CG     . LYS A 1 204 ? -9.91500  1.32600   10.68300 0.370 75.72053  ?  204 LYS A CG     1 
ATOM   3153 C CD     . LYS A 1 204 ? -11.43700 1.39300   10.75000 0.250 71.57349  ?  204 LYS A CD     1 
ATOM   3154 C CE     . LYS A 1 204 ? -12.03100 0.13100   11.35300 0.700 77.58035  ?  204 LYS A CE     1 
ATOM   3155 N NZ     . LYS A 1 204 ? -13.40900 0.36300   11.88000 0.630 92.29890  ?  204 LYS A NZ     1 
ATOM   3156 H H      . LYS A 1 204 ? -7.00600  2.09400   11.00600 1.000 81.98823  ?  204 LYS A H      1 
ATOM   3157 H HA     . LYS A 1 204 ? -8.20600  1.93100   8.59600  1.000 85.77291  ?  204 LYS A HA     1 
ATOM   3158 H HB2    . LYS A 1 204 ? -9.17300  3.20500   10.93100 1.000 90.13465  ?  204 LYS A HB2    1 
ATOM   3159 H HB3    . LYS A 1 204 ? -10.00400 3.03900   9.58700  1.000 90.13465  ?  204 LYS A HB3    1 
ATOM   3160 H HG2    . LYS A 1 204 ? -9.66500  0.60300   10.08700 1.000 90.98240  ?  204 LYS A HG2    1 
ATOM   3161 H HG3    . LYS A 1 204 ? -9.57500  1.15300   11.57500 1.000 90.98240  ?  204 LYS A HG3    1 
ATOM   3162 H HD2    . LYS A 1 204 ? -11.70100 2.14700   11.30200 1.000 86.00596  ?  204 LYS A HD2    1 
ATOM   3163 H HD3    . LYS A 1 204 ? -11.79300 1.49800   9.85400  1.000 86.00596  ?  204 LYS A HD3    1 
ATOM   3164 H HE2    . LYS A 1 204 ? -12.07900 -0.55800  10.67200 1.000 93.21419  ?  204 LYS A HE2    1 
ATOM   3165 H HE3    . LYS A 1 204 ? -11.47200 -0.16700  12.08700 1.000 93.21419  ?  204 LYS A HE3    1 
ATOM   3166 H HZ1    . LYS A 1 204 ? -13.73600 -0.39100  12.22100 1.000 110.87645 ?  204 LYS A HZ1    1 
ATOM   3167 H HZ2    . LYS A 1 204 ? -13.39100 0.98400   12.51800 1.000 110.87645 ?  204 LYS A HZ2    1 
ATOM   3168 H HZ3    . LYS A 1 204 ? -13.94400 0.63900   11.22400 1.000 110.87645 ?  204 LYS A HZ3    1 
ATOM   3169 N N      . GLU A 1 205 ? -6.88900  4.62000   9.73600  1.000 73.36898  ?  205 GLU A N      1 
ATOM   3170 C CA     . GLU A 1 205 ? -6.42100  5.94900   9.36100  1.000 81.13419  ?  205 GLU A CA     1 
ATOM   3171 C C      . GLU A 1 205 ? -4.98300  5.86700   8.84200  1.000 71.53380  ?  205 GLU A C      1 
ATOM   3172 O O      . GLU A 1 205 ? -4.15900  5.14200   9.41400  1.000 60.24836  ?  205 GLU A O      1 
ATOM   3173 C CB     . GLU A 1 205 ? -6.47100  6.90000   10.55700 1.000 84.30568  ?  205 GLU A CB     1 
ATOM   3174 C CG     . GLU A 1 205 ? -7.73000  7.76800   10.70200 1.000 99.45576  ?  205 GLU A CG     1 
ATOM   3175 C CD     . GLU A 1 205 ? -8.43700  8.05900   9.39100  1.000 113.29082 ?  205 GLU A CD     1 
ATOM   3176 O OE1    . GLU A 1 205 ? -7.98600  8.96300   8.65100  1.000 102.78374 ?  205 GLU A OE1    1 
ATOM   3177 O OE2    . GLU A 1 205 ? -9.44500  7.37200   9.09700  1.000 114.24399 -1 205 GLU A OE2    1 
ATOM   3178 H H      . GLU A 1 205 ? -6.67000  4.38600   10.53300 1.000 88.16055  ?  205 GLU A H      1 
ATOM   3179 H HA     . GLU A 1 205 ? -6.98900  6.31600   8.66500  1.000 97.47879  ?  205 GLU A HA     1 
ATOM   3180 H HB2    . GLU A 1 205 ? -6.40000  6.36900   11.36600 1.000 101.28459 ?  205 GLU A HB2    1 
ATOM   3181 H HB3    . GLU A 1 205 ? -5.71700  7.50600   10.49100 1.000 101.28459 ?  205 GLU A HB3    1 
ATOM   3182 H HG2    . GLU A 1 205 ? -8.35900  7.30800   11.28000 1.000 119.46468 ?  205 GLU A HG2    1 
ATOM   3183 H HG3    . GLU A 1 205 ? -7.47800  8.61800   11.09500 1.000 119.46468 ?  205 GLU A HG3    1 
ATOM   3184 N N      . PRO A 1 206 ? -4.64700  6.58800   7.77400  1.000 62.15208  ?  206 PRO A N      1 
ATOM   3185 C CA     . PRO A 1 206 ? -3.27500  6.54800   7.25100  1.000 60.72935  ?  206 PRO A CA     1 
ATOM   3186 C C      . PRO A 1 206 ? -2.31000  7.30100   8.15500  1.000 59.18480  ?  206 PRO A C      1 
ATOM   3187 O O      . PRO A 1 206 ? -2.72700  8.12600   8.98000  1.000 52.03025  ?  206 PRO A O      1 
ATOM   3188 C CB     . PRO A 1 206 ? -3.40200  7.22800   5.88100  1.000 57.22053  ?  206 PRO A CB     1 
ATOM   3189 C CG     . PRO A 1 206 ? -4.54500  8.15900   6.03900  1.000 62.33138  ?  206 PRO A CG     1 
ATOM   3190 C CD     . PRO A 1 206 ? -5.51500  7.47100   6.97300  1.000 68.11207  ?  206 PRO A CD     1 
ATOM   3191 H HA     . PRO A 1 206 ? -2.97400  5.63200   7.14500  1.000 72.99298  ?  206 PRO A HA     1 
ATOM   3192 H HB2    . PRO A 1 206 ? -2.58600  7.70800   5.67000  1.000 68.78241  ?  206 PRO A HB2    1 
ATOM   3193 H HB3    . PRO A 1 206 ? -3.58300  6.56500   5.19500  1.000 68.78241  ?  206 PRO A HB3    1 
ATOM   3194 H HG2    . PRO A 1 206 ? -4.23400  8.99500   6.42100  1.000 74.91542  ?  206 PRO A HG2    1 
ATOM   3195 H HG3    . PRO A 1 206 ? -4.95600  8.32200   5.17600  1.000 74.91542  ?  206 PRO A HG3    1 
ATOM   3196 H HD2    . PRO A 1 206 ? -5.96700  8.11600   7.53800  1.000 81.85226  ?  206 PRO A HD2    1 
ATOM   3197 H HD3    . PRO A 1 206 ? -6.16600  6.95400   6.47300  1.000 81.85226  ?  206 PRO A HD3    1 
ATOM   3198 N N      . PRO A 1 207 ? -1.01100  7.04400   8.04100  1.000 51.57907  ?  207 PRO A N      1 
ATOM   3199 C CA     . PRO A 1 207 ? -0.03700  7.81200   8.82100  1.000 46.27520  ?  207 PRO A CA     1 
ATOM   3200 C C      . PRO A 1 207 ? 0.23900   9.15900   8.17700  1.000 47.96485  ?  207 PRO A C      1 
ATOM   3201 O O      . PRO A 1 207 ? 0.25300   9.30400   6.96100  1.000 48.52253  ?  207 PRO A O      1 
ATOM   3202 C CB     . PRO A 1 207 ? 1.21500   6.91600   8.79900  1.000 47.55558  ?  207 PRO A CB     1 
ATOM   3203 C CG     . PRO A 1 207 ? 1.11100   6.16000   7.51400  1.000 47.29315  ?  207 PRO A CG     1 
ATOM   3204 C CD     . PRO A 1 207 ? -0.37000  6.01300   7.19400  1.000 51.17479  ?  207 PRO A CD     1 
ATOM   3205 H HA     . PRO A 1 207 ? -0.32900  7.93600   9.73700  1.000 55.64801  ?  207 PRO A HA     1 
ATOM   3206 H HB2    . PRO A 1 207 ? 2.01600   7.46300   8.81800  1.000 57.18446  ?  207 PRO A HB2    1 
ATOM   3207 H HB3    . PRO A 1 207 ? 1.20600   6.31400   9.56000  1.000 57.18446  ?  207 PRO A HB3    1 
ATOM   3208 H HG2    . PRO A 1 207 ? 1.56100   6.65600   6.81200  1.000 56.86955  ?  207 PRO A HG2    1 
ATOM   3209 H HG3    . PRO A 1 207 ? 1.52200   5.28800   7.62000  1.000 56.86955  ?  207 PRO A HG3    1 
ATOM   3210 H HD2    . PRO A 1 207 ? -0.53800  6.18600   6.25400  1.000 61.52752  ?  207 PRO A HD2    1 
ATOM   3211 H HD3    . PRO A 1 207 ? -0.68700  5.12700   7.43000  1.000 61.52752  ?  207 PRO A HD3    1 
ATOM   3212 N N      . LEU A 1 208 ? 0.46500   10.16700  9.03700  1.000 47.42814  ?  208 LEU A N      1 
ATOM   3213 C CA     . LEU A 1 208 ? 0.65800   11.53400  8.58500  1.000 47.54556  ?  208 LEU A CA     1 
ATOM   3214 C C      . LEU A 1 208 ? 2.07400   12.05600  8.81300  1.000 45.21792  ?  208 LEU A C      1 
ATOM   3215 O O      . LEU A 1 208 ? 2.36700   13.19200  8.42500  1.000 49.16044  ?  208 LEU A O      1 
ATOM   3216 C CB     . LEU A 1 208 ? -0.32600  12.46500  9.28600  1.000 48.95693  ?  208 LEU A CB     1 
ATOM   3217 C CG     . LEU A 1 208 ? -1.81600  12.14000  9.13400  1.000 58.97392  ?  208 LEU A CG     1 
ATOM   3218 C CD1    . LEU A 1 208 ? -2.63500  13.13100  9.93700  1.000 53.14100  ?  208 LEU A CD1    1 
ATOM   3219 C CD2    . LEU A 1 208 ? -2.24900  12.14700  7.67100  1.000 62.40289  ?  208 LEU A CD2    1 
ATOM   3220 H H      . LEU A 1 208 ? 0.50900   10.07200  9.89000  1.000 57.03154  ?  208 LEU A H      1 
ATOM   3221 H HA     . LEU A 1 208 ? 0.48100   11.55800  7.63200  1.000 57.17244  ?  208 LEU A HA     1 
ATOM   3222 H HB2    . LEU A 1 208 ? -0.12800  12.44900  10.23500 1.000 58.86609  ?  208 LEU A HB2    1 
ATOM   3223 H HB3    . LEU A 1 208 ? -0.19400  13.35900  8.93400  1.000 58.86609  ?  208 LEU A HB3    1 
ATOM   3224 H HG     . LEU A 1 208 ? -1.97800  11.24500  9.47100  1.000 70.88648  ?  208 LEU A HG     1 
ATOM   3225 H HD11   . LEU A 1 208 ? -3.57500  12.91700  9.83900  1.000 63.88697  ?  208 LEU A HD11   1 
ATOM   3226 H HD12   . LEU A 1 208 ? -2.37700  13.07000  10.87100 1.000 63.88697  ?  208 LEU A HD12   1 
ATOM   3227 H HD13   . LEU A 1 208 ? -2.46300  14.02600  9.60500  1.000 63.88697  ?  208 LEU A HD13   1 
ATOM   3228 H HD21   . LEU A 1 208 ? -3.19600  11.94400  7.62100  1.000 75.00124  ?  208 LEU A HD21   1 
ATOM   3229 H HD22   . LEU A 1 208 ? -2.07900  13.02600  7.29600  1.000 75.00124  ?  208 LEU A HD22   1 
ATOM   3230 H HD23   . LEU A 1 208 ? -1.74000  11.47800  7.18800  1.000 75.00124  ?  208 LEU A HD23   1 
ATOM   3231 N N      . THR A 1 209 ? 2.94600   11.28300  9.44100  1.000 43.73735  ?  209 THR A N      1 
ATOM   3232 C CA     . THR A 1 209 ? 4.25300   11.81600  9.78200  1.000 44.39631  ?  209 THR A CA     1 
ATOM   3233 C C      . THR A 1 209 ? 5.07700   12.02100  8.51800  1.000 46.02318  ?  209 THR A C      1 
ATOM   3234 O O      . THR A 1 209 ? 4.86000   11.38600  7.49000  1.000 49.16989  ?  209 THR A O      1 
ATOM   3235 C CB     . THR A 1 209 ? 4.99400   10.89500  10.75600 1.000 44.72558  ?  209 THR A CB     1 
ATOM   3236 O OG1    . THR A 1 209 ? 6.17900   11.57900  11.22500 1.000 43.48940  ?  209 THR A OG1    1 
ATOM   3237 C CG2    . THR A 1 209 ? 5.38800   9.59400   10.09900 1.000 42.38464  ?  209 THR A CG2    1 
ATOM   3238 H H      . THR A 1 209 ? 2.80900   10.46700  9.67600  1.000 52.60259  ?  209 THR A H      1 
ATOM   3239 H HA     . THR A 1 209 ? 4.14500   12.67200  10.22500 1.000 53.39334  ?  209 THR A HA     1 
ATOM   3240 H HB     . THR A 1 209 ? 4.41400   10.67500  11.50200 1.000 53.78846  ?  209 THR A HB     1 
ATOM   3241 H HG1    . THR A 1 209 ? 6.58000   11.10400  11.78900 1.000 52.30505  ?  209 THR A HG1    1 
ATOM   3242 H HG21   . THR A 1 209 ? 5.71400   8.97000   10.76600 1.000 50.97934  ?  209 THR A HG21   1 
ATOM   3243 H HG22   . THR A 1 209 ? 4.62100   9.20300   9.65100  1.000 50.97934  ?  209 THR A HG22   1 
ATOM   3244 H HG23   . THR A 1 209 ? 6.08700   9.75000   9.44500  1.000 50.97934  ?  209 THR A HG23   1 
ATOM   3245 N N      . VAL A 1 210 ? 6.03500   12.93900  8.61000  1.000 47.05404  ?  210 VAL A N      1 
ATOM   3246 C CA     . VAL A 1 210 ? 6.88900   13.27600  7.48300  1.000 47.38102  ?  210 VAL A CA     1 
ATOM   3247 C C      . VAL A 1 210 ? 8.22800   12.56800  7.53300  1.000 46.13758  ?  210 VAL A C      1 
ATOM   3248 O O      . VAL A 1 210 ? 9.07600   12.81500  6.67500  1.000 47.80429  ?  210 VAL A O      1 
ATOM   3249 C CB     . VAL A 1 210 ? 7.09400   14.80800  7.39500  1.000 54.12476  ?  210 VAL A CB     1 
ATOM   3250 C CG1    . VAL A 1 210 ? 5.75500   15.49900  7.12800  1.000 50.94854  ?  210 VAL A CG1    1 
ATOM   3251 C CG2    . VAL A 1 210 ? 7.73900   15.35000  8.67300  1.000 55.13437  ?  210 VAL A CG2    1 
ATOM   3252 H H      . VAL A 1 210 ? 6.20900   13.38500  9.32400  1.000 56.58262  ?  210 VAL A H      1 
ATOM   3253 H HA     . VAL A 1 210 ? 6.44700   12.98100  6.67200  1.000 56.97500  ?  210 VAL A HA     1 
ATOM   3254 H HB     . VAL A 1 210 ? 7.69500   15.00400  6.65900  1.000 65.06748  ?  210 VAL A HB     1 
ATOM   3255 H HG11   . VAL A 1 210 ? 5.90500   16.45300  7.03900  1.000 61.25601  ?  210 VAL A HG11   1 
ATOM   3256 H HG12   . VAL A 1 210 ? 5.37500   15.14600  6.30900  1.000 61.25601  ?  210 VAL A HG12   1 
ATOM   3257 H HG13   . VAL A 1 210 ? 5.15700   15.32600  7.87200  1.000 61.25601  ?  210 VAL A HG13   1 
ATOM   3258 H HG21   . VAL A 1 210 ? 7.87400   16.30600  8.57800  1.000 66.27901  ?  210 VAL A HG21   1 
ATOM   3259 H HG22   . VAL A 1 210 ? 7.15100   15.17200  9.42400  1.000 66.27901  ?  210 VAL A HG22   1 
ATOM   3260 H HG23   . VAL A 1 210 ? 8.59200   14.90800  8.80800  1.000 66.27901  ?  210 VAL A HG23   1 
ATOM   3261 N N      . PHE A 1 211 ? 8.43800   11.67900  8.50600  1.000 44.24719  ?  211 PHE A N      1 
ATOM   3262 C CA     . PHE A 1 211 ? 9.71600   10.99900  8.69200  1.000 47.27223  ?  211 PHE A CA     1 
ATOM   3263 C C      . PHE A 1 211 ? 9.56000   9.53000   8.27900  1.000 46.20751  ?  211 PHE A C      1 
ATOM   3264 O O      . PHE A 1 211 ? 8.76600   8.79600   8.87400  1.000 46.72099  ?  211 PHE A O      1 
ATOM   3265 C CB     . PHE A 1 211 ? 10.18100  11.11200  10.13900 1.000 44.81240  ?  211 PHE A CB     1 
ATOM   3266 C CG     . PHE A 1 211 ? 10.28100  12.52800  10.63200 1.000 46.21907  ?  211 PHE A CG     1 
ATOM   3267 C CD1    . PHE A 1 211 ? 11.28600  13.37400  10.15300 1.000 51.27890  ?  211 PHE A CD1    1 
ATOM   3268 C CD2    . PHE A 1 211 ? 9.38000   13.02400  11.54900 1.000 45.28805  ?  211 PHE A CD2    1 
ATOM   3269 C CE1    . PHE A 1 211 ? 11.37900  14.68400  10.59100 1.000 56.15983  ?  211 PHE A CE1    1 
ATOM   3270 C CE2    . PHE A 1 211 ? 9.46100   14.34400  12.00200 1.000 48.11202  ?  211 PHE A CE2    1 
ATOM   3271 C CZ     . PHE A 1 211 ? 10.46500  15.17400  11.52500 1.000 51.79376  ?  211 PHE A CZ     1 
ATOM   3272 H H      . PHE A 1 211 ? 7.84000   11.45100  9.08000  1.000 53.21440  ?  211 PHE A H      1 
ATOM   3273 H HA     . PHE A 1 211 ? 10.39000  11.40300  8.12400  1.000 56.84444  ?  211 PHE A HA     1 
ATOM   3274 H HB2    . PHE A 1 211 ? 9.55000   10.64400  10.70700 1.000 53.89264  ?  211 PHE A HB2    1 
ATOM   3275 H HB3    . PHE A 1 211 ? 11.06000  10.70800  10.21700 1.000 53.89264  ?  211 PHE A HB3    1 
ATOM   3276 H HD1    . PHE A 1 211 ? 11.90000  13.05300  9.53200  1.000 61.65245  ?  211 PHE A HD1    1 
ATOM   3277 H HD2    . PHE A 1 211 ? 8.70700   12.47100  11.87300 1.000 54.46343  ?  211 PHE A HD2    1 
ATOM   3278 H HE1    . PHE A 1 211 ? 12.05100  15.23800  10.26400 1.000 67.50956  ?  211 PHE A HE1    1 
ATOM   3279 H HE2    . PHE A 1 211 ? 8.84400   14.66400  12.62000 1.000 57.85219  ?  211 PHE A HE2    1 
ATOM   3280 H HZ     . PHE A 1 211 ? 10.52700  16.05200  11.82500 1.000 62.27028  ?  211 PHE A HZ     1 
ATOM   3281 N N      . LYS A 1 212 ? 10.32000  9.12100   7.27700  1.000 43.44396  ?  212 LYS A N      1 
ATOM   3282 C CA     . LYS A 1 212 ? 10.22100  7.77900   6.71500  1.000 50.88108  ?  212 LYS A CA     1 
ATOM   3283 C C      . LYS A 1 212 ? 11.18100  6.82600   7.41500  1.000 46.07783  ?  212 LYS A C      1 
ATOM   3284 O O      . LYS A 1 212 ? 12.31200  7.19500   7.76700  1.000 42.98214  ?  212 LYS A O      1 
ATOM   3285 C CB     . LYS A 1 212 ? 10.50800  7.79900   5.20700  1.000 53.59325  ?  212 LYS A CB     1 
ATOM   3286 C CG     . LYS A 1 212 ? 9.83400   8.94200   4.44300  1.000 67.22537  ?  212 LYS A CG     1 
ATOM   3287 C CD     . LYS A 1 212 ? 8.49000   8.51600   3.84100  1.000 82.61703  ?  212 LYS A CD     1 
ATOM   3288 C CE     . LYS A 1 212 ? 7.34700   8.67500   4.85400  1.000 81.83139  ?  212 LYS A CE     1 
ATOM   3289 N NZ     . LYS A 1 212 ? 6.18700   7.76700   4.53700  1.000 70.34422  ?  212 LYS A NZ     1 
ATOM   3290 H H      . LYS A 1 212 ? 10.91500  9.61000   6.89500  1.000 52.25052  ?  212 LYS A H      1 
ATOM   3291 H HA     . LYS A 1 212 ? 9.32000   7.44700   6.85100  1.000 61.17507  ?  212 LYS A HA     1 
ATOM   3292 H HB2    . LYS A 1 212 ? 11.46600  7.88500   5.07700  1.000 64.42967  ?  212 LYS A HB2    1 
ATOM   3293 H HB3    . LYS A 1 212 ? 10.19500  6.96500   4.82200  1.000 64.42967  ?  212 LYS A HB3    1 
ATOM   3294 H HG2    . LYS A 1 212 ? 9.67400   9.68100   5.05000  1.000 80.78822  ?  212 LYS A HG2    1 
ATOM   3295 H HG3    . LYS A 1 212 ? 10.41300  9.22700   3.71900  1.000 80.78822  ?  212 LYS A HG3    1 
ATOM   3296 H HD2    . LYS A 1 212 ? 8.29300   9.07000   3.07000  1.000 99.25821  ?  212 LYS A HD2    1 
ATOM   3297 H HD3    . LYS A 1 212 ? 8.53700   7.58400   3.57700  1.000 99.25821  ?  212 LYS A HD3    1 
ATOM   3298 H HE2    . LYS A 1 212 ? 7.67300   8.45400   5.74100  1.000 98.31543  ?  212 LYS A HE2    1 
ATOM   3299 H HE3    . LYS A 1 212 ? 7.02900   9.59100   4.83600  1.000 98.31543  ?  212 LYS A HE3    1 
ATOM   3300 H HZ1    . LYS A 1 212 ? 5.55400   7.85500   5.15700  1.000 84.53084  ?  212 LYS A HZ1    1 
ATOM   3301 H HZ2    . LYS A 1 212 ? 5.84600   7.97600   3.74300  1.000 84.53084  ?  212 LYS A HZ2    1 
ATOM   3302 H HZ3    . LYS A 1 212 ? 6.46000   6.92000   4.52100  1.000 84.53084  ?  212 LYS A HZ3    1 
ATOM   3303 N N      . GLY A 1 213 ? 10.72600  5.59000   7.62100  1.000 45.33713  ?  213 GLY A N      1 
ATOM   3304 C CA     . GLY A 1 213 ? 11.52700  4.61600   8.33300  1.000 44.61251  ?  213 GLY A CA     1 
ATOM   3305 C C      . GLY A 1 213 ? 12.58900  3.96200   7.46900  1.000 39.33482  ?  213 GLY A C      1 
ATOM   3306 O O      . GLY A 1 213 ? 12.59300  4.05100   6.25500  1.000 40.76166  ?  213 GLY A O      1 
ATOM   3307 H H      . GLY A 1 213 ? 9.96100   5.29900   7.35700  1.000 54.52232  ?  213 GLY A H      1 
ATOM   3308 H HA2    . GLY A 1 213 ? 11.97100  5.05400   9.07600  1.000 53.65278  ?  213 GLY A HA2    1 
ATOM   3309 H HA3    . GLY A 1 213 ? 10.94700  3.91900   8.67800  1.000 53.65278  ?  213 GLY A HA3    1 
ATOM   3310 N N      . GLY A 1 214 ? 13.51500  3.29200   8.14100  1.000 42.63943  ?  214 GLY A N      1 
ATOM   3311 C CA     . GLY A 1 214 ? 14.49000  2.47100   7.45400  1.000 42.79492  ?  214 GLY A CA     1 
ATOM   3312 C C      . GLY A 1 214 ? 15.92700  2.91900   7.59700  1.000 44.09311  ?  214 GLY A C      1 
ATOM   3313 O O      . GLY A 1 214 ? 16.21400  4.10100   7.86800  1.000 40.72090  ?  214 GLY A O      1 
ATOM   3314 H H      . GLY A 1 214 ? 13.59700  3.29800   8.99700  1.000 51.28508  ?  214 GLY A H      1 
ATOM   3315 H HA2    . GLY A 1 214 ? 14.42900  1.56600   7.79600  1.000 51.47167  ?  214 GLY A HA2    1 
ATOM   3316 H HA3    . GLY A 1 214 ? 14.27800  2.46600   6.50700  1.000 51.47167  ?  214 GLY A HA3    1 
ATOM   3317 N N      . GLU A 1 215 ? 16.84100  1.96600   7.40300  1.000 46.98777  ?  215 GLU A N      1 
ATOM   3318 C CA     . GLU A 1 215 ? 18.26700  2.25000   7.51000  1.000 43.88162  ?  215 GLU A CA     1 
ATOM   3319 C C      . GLU A 1 215 ? 18.72200  3.24800   6.44600  1.000 41.84903  ?  215 GLU A C      1 
ATOM   3320 O O      . GLU A 1 215 ? 19.57900  4.10700   6.71300  1.000 42.00896  ?  215 GLU A O      1 
ATOM   3321 C CB     . GLU A 1 215 ? 19.04300  0.93000   7.38600  1.000 40.26931  ?  215 GLU A CB     1 
ATOM   3322 C CG     . GLU A 1 215 ? 20.53100  1.08100   7.17400  1.000 40.36996  ?  215 GLU A CG     1 
ATOM   3323 C CD     . GLU A 1 215 ? 21.23300  -0.26700  7.02500  1.000 41.32054  ?  215 GLU A CD     1 
ATOM   3324 O OE1    . GLU A 1 215 ? 20.57500  -1.25300  6.63200  1.000 45.52696  ?  215 GLU A OE1    1 
ATOM   3325 O OE2    . GLU A 1 215 ? 22.43500  -0.34400  7.31000  1.000 43.16426  -1 215 GLU A OE2    1 
ATOM   3326 H H      . GLU A 1 215 ? 16.66000  1.14800   7.21000  1.000 56.50310  ?  215 GLU A H      1 
ATOM   3327 H HA     . GLU A 1 215 ? 18.45400  2.64700   8.37400  1.000 52.77572  ?  215 GLU A HA     1 
ATOM   3328 H HB2    . GLU A 1 215 ? 18.91600  0.42200   8.20200  1.000 48.44094  ?  215 GLU A HB2    1 
ATOM   3329 H HB3    . GLU A 1 215 ? 18.69000  0.43700   6.62900  1.000 48.44094  ?  215 GLU A HB3    1 
ATOM   3330 H HG2    . GLU A 1 215 ? 20.68600  1.59400   6.36500  1.000 48.56173  ?  215 GLU A HG2    1 
ATOM   3331 H HG3    . GLU A 1 215 ? 20.91600  1.54000   7.93700  1.000 48.56173  ?  215 GLU A HG3    1 
ATOM   3332 N N      . THR A 1 216 ? 18.16800  3.15600   5.24100  1.000 43.45027  ?  216 THR A N      1 
ATOM   3333 C CA     . THR A 1 216 ? 18.59800  4.04100   4.15500  1.000 43.69163  ?  216 THR A CA     1 
ATOM   3334 C C      . THR A 1 216 ? 18.31100  5.50100   4.48800  1.000 45.97418  ?  216 THR A C      1 
ATOM   3335 O O      . THR A 1 216 ? 19.15100  6.38200   4.27600  1.000 40.31033  ?  216 THR A O      1 
ATOM   3336 C CB     . THR A 1 216 ? 17.91400  3.64200   2.85000  1.000 47.88155  ?  216 THR A CB     1 
ATOM   3337 O OG1    . THR A 1 216 ? 18.12900  2.24800   2.59600  1.000 52.41783  ?  216 THR A OG1    1 
ATOM   3338 C CG2    . THR A 1 216 ? 18.48000  4.45700   1.67800  1.000 55.39227  ?  216 THR A CG2    1 
ATOM   3339 H H      . THR A 1 216 ? 17.55000  2.59800   5.02600  1.000 52.25810  ?  216 THR A H      1 
ATOM   3340 H HA     . THR A 1 216 ? 19.55500  3.94300   4.03500  1.000 52.54772  ?  216 THR A HA     1 
ATOM   3341 H HB     . THR A 1 216 ? 16.96200  3.81600   2.92100  1.000 57.57563  ?  216 THR A HB     1 
ATOM   3342 H HG1    . THR A 1 216 ? 17.79300  2.03500   1.85600  1.000 63.01917  ?  216 THR A HG1    1 
ATOM   3343 H HG21   . THR A 1 216 ? 18.10500  4.13900   0.84200  1.000 66.58849  ?  216 THR A HG21   1 
ATOM   3344 H HG22   . THR A 1 216 ? 18.25700  5.39400   1.78800  1.000 66.58849  ?  216 THR A HG22   1 
ATOM   3345 H HG23   . THR A 1 216 ? 19.44500  4.36500   1.64600  1.000 66.58849  ?  216 THR A HG23   1 
ATOM   3346 N N      . GLU A 1 217 ? 17.10000  5.78400   4.99300  1.000 41.42573  ?  217 GLU A N      1 
ATOM   3347 C CA     . GLU A 1 217 ? 16.77200  7.15600   5.36600  1.000 46.17574  ?  217 GLU A CA     1 
ATOM   3348 C C      . GLU A 1 217 ? 17.60100  7.61300   6.56100  1.000 44.70893  ?  217 GLU A C      1 
ATOM   3349 O O      . GLU A 1 217 ? 17.98600  8.79100   6.64600  1.000 44.11109  ?  217 GLU A O      1 
ATOM   3350 C CB     . GLU A 1 217 ? 15.28000  7.27300   5.67900  1.000 49.66920  ?  217 GLU A CB     1 
ATOM   3351 C CG     . GLU A 1 217 ? 14.39900  7.31000   4.43000  1.000 61.92097  ?  217 GLU A CG     1 
ATOM   3352 C CD     . GLU A 1 217 ? 14.31600  8.69500   3.81100  1.000 65.60346  ?  217 GLU A CD     1 
ATOM   3353 O OE1    . GLU A 1 217 ? 14.78400  9.67000   4.44200  1.000 60.19298  ?  217 GLU A OE1    1 
ATOM   3354 O OE2    . GLU A 1 217 ? 13.78000  8.80100   2.68900  1.000 73.38356  -1 217 GLU A OE2    1 
ATOM   3355 H H      . GLU A 1 217 ? 16.47200  5.21200   5.12300  1.000 49.82865  ?  217 GLU A H      1 
ATOM   3356 H HA     . GLU A 1 217 ? 16.97000  7.73800   4.61600  1.000 55.52866  ?  217 GLU A HA     1 
ATOM   3357 H HB2    . GLU A 1 217 ? 15.01100  6.50800   6.21100  1.000 59.72081  ?  217 GLU A HB2    1 
ATOM   3358 H HB3    . GLU A 1 217 ? 15.12800  8.09300   6.17500  1.000 59.72081  ?  217 GLU A HB3    1 
ATOM   3359 H HG2    . GLU A 1 217 ? 14.76700  6.70600   3.76600  1.000 74.42294  ?  217 GLU A HG2    1 
ATOM   3360 H HG3    . GLU A 1 217 ? 13.50000  7.03300   4.66800  1.000 74.42294  ?  217 GLU A HG3    1 
ATOM   3361 N N      . ALA A 1 218 ? 17.86900  6.70500   7.49900  1.000 39.46078  ?  218 ALA A N      1 
ATOM   3362 C CA     . ALA A 1 218 ? 18.66600  7.06200   8.67100  1.000 40.03315  ?  218 ALA A CA     1 
ATOM   3363 C C      . ALA A 1 218 ? 20.03500  7.57000   8.26300  1.000 39.63177  ?  218 ALA A C      1 
ATOM   3364 O O      . ALA A 1 218 ? 20.48900  8.61000   8.73900  1.000 41.43918  ?  218 ALA A O      1 
ATOM   3365 C CB     . ALA A 1 218 ? 18.80800  5.84700   9.59300  1.000 36.86953  ?  218 ALA A CB     1 
ATOM   3366 H H      . ALA A 1 218 ? 17.60600  5.88600   7.48100  1.000 47.47070  ?  218 ALA A H      1 
ATOM   3367 H HA     . ALA A 1 218 ? 18.20900  7.76600   9.15700  1.000 48.15755  ?  218 ALA A HA     1 
ATOM   3368 H HB1    . ALA A 1 218 ? 19.24000  6.12400   10.41600 1.000 44.36120  ?  218 ALA A HB1    1 
ATOM   3369 H HB2    . ALA A 1 218 ? 17.92600  5.49200   9.78600  1.000 44.36120  ?  218 ALA A HB2    1 
ATOM   3370 H HB3    . ALA A 1 218 ? 19.34500  5.17300   9.14700  1.000 44.36120  ?  218 ALA A HB3    1 
ATOM   3371 N N      . LEU A 1 219 ? 20.71900  6.83100   7.38500  1.000 40.92791  ?  219 LEU A N      1 
ATOM   3372 C CA     . LEU A 1 219 ? 22.03900  7.24200   6.93300  1.000 40.99277  ?  219 LEU A CA     1 
ATOM   3373 C C      . LEU A 1 219 ? 21.97400  8.53800   6.13300  1.000 41.31336  ?  219 LEU A C      1 
ATOM   3374 O O      . LEU A 1 219 ? 22.88200  9.37100   6.21400  1.000 44.14444  ?  219 LEU A O      1 
ATOM   3375 C CB     . LEU A 1 219 ? 22.68300  6.12800   6.11300  1.000 42.07590  ?  219 LEU A CB     1 
ATOM   3376 C CG     . LEU A 1 219 ? 22.88500  4.82600   6.88900  1.000 42.74895  ?  219 LEU A CG     1 
ATOM   3377 C CD1    . LEU A 1 219 ? 23.11800  3.66000   5.94800  1.000 42.93658  ?  219 LEU A CD1    1 
ATOM   3378 C CD2    . LEU A 1 219 ? 24.04000  4.98100   7.87500  1.000 48.34963  ?  219 LEU A CD2    1 
ATOM   3379 H H      . LEU A 1 219 ? 20.43900  6.09400   7.04100  1.000 49.23126  ?  219 LEU A H      1 
ATOM   3380 H HA     . LEU A 1 219 ? 22.59900  7.40200   7.70800  1.000 49.30910  ?  219 LEU A HA     1 
ATOM   3381 H HB2    . LEU A 1 219 ? 22.11400  5.93400   5.35200  1.000 50.60885  ?  219 LEU A HB2    1 
ATOM   3382 H HB3    . LEU A 1 219 ? 23.55300  6.42900   5.80800  1.000 50.60885  ?  219 LEU A HB3    1 
ATOM   3383 H HG     . LEU A 1 219 ? 22.08100  4.62700   7.39400  1.000 51.41651  ?  219 LEU A HG     1 
ATOM   3384 H HD11   . LEU A 1 219 ? 23.28900  2.86100   6.47100  1.000 51.64167  ?  219 LEU A HD11   1 
ATOM   3385 H HD12   . LEU A 1 219 ? 22.32800  3.53400   5.40000  1.000 51.64167  ?  219 LEU A HD12   1 
ATOM   3386 H HD13   . LEU A 1 219 ? 23.88300  3.85700   5.38500  1.000 51.64167  ?  219 LEU A HD13   1 
ATOM   3387 H HD21   . LEU A 1 219 ? 24.19500  4.13100   8.31600  1.000 58.13732  ?  219 LEU A HD21   1 
ATOM   3388 H HD22   . LEU A 1 219 ? 24.83500  5.25200   7.39000  1.000 58.13732  ?  219 LEU A HD22   1 
ATOM   3389 H HD23   . LEU A 1 219 ? 23.80700  5.65600   8.53100  1.000 58.13732  ?  219 LEU A HD23   1 
ATOM   3390 N N      . ALA A 1 220 ? 20.91600  8.72700   5.35000  1.000 40.72568  ?  220 ALA A N      1 
ATOM   3391 C CA     . ALA A 1 220 ? 20.77000  9.99600   4.63800  1.000 43.87192  ?  220 ALA A CA     1 
ATOM   3392 C C      . ALA A 1 220 ? 20.62900  11.15400  5.61400  1.000 45.17399  ?  220 ALA A C      1 
ATOM   3393 O O      . ALA A 1 220 ? 21.22300  12.22200  5.42300  1.000 44.53592  ?  220 ALA A O      1 
ATOM   3394 C CB     . ALA A 1 220 ? 19.56800  9.94700   3.69500  1.000 47.84140  ?  220 ALA A CB     1 
ATOM   3395 H H      . ALA A 1 220 ? 20.28700  8.15600   5.21700  1.000 48.98858  ?  220 ALA A H      1 
ATOM   3396 H HA     . ALA A 1 220 ? 21.56300  10.14100  4.10000  1.000 52.76407  ?  220 ALA A HA     1 
ATOM   3397 H HB1    . ALA A 1 220 ? 19.49400  10.79700  3.23300  1.000 57.52745  ?  220 ALA A HB1    1 
ATOM   3398 H HB2    . ALA A 1 220 ? 19.70000  9.23200   3.05300  1.000 57.52745  ?  220 ALA A HB2    1 
ATOM   3399 H HB3    . ALA A 1 220 ? 18.76600  9.78100   4.21400  1.000 57.52745  ?  220 ALA A HB3    1 
ATOM   3400 N N      . ARG A 1 221 ? 19.84300  10.96900  6.67300  1.000 46.83835  ?  221 ARG A N      1 
ATOM   3401 C CA     A ARG A 1 221 ? 19.66300  12.03000  7.65800  0.470 46.98483  ?  221 ARG A CA     1 
ATOM   3402 C CA     B ARG A 1 221 ? 19.66600  12.04000  7.64700  0.530 47.03753  ?  221 ARG A CA     1 
ATOM   3403 C C      . ARG A 1 221 ? 20.95200  12.29200  8.42300  1.000 45.74153  ?  221 ARG A C      1 
ATOM   3404 O O      . ARG A 1 221 ? 21.28200  13.44700  8.72700  1.000 45.39285  ?  221 ARG A O      1 
ATOM   3405 C CB     A ARG A 1 221 ? 18.53500  11.66100  8.61900  0.470 48.55438  ?  221 ARG A CB     1 
ATOM   3406 C CB     B ARG A 1 221 ? 18.51700  11.71200  8.59900  0.530 48.32473  ?  221 ARG A CB     1 
ATOM   3407 C CG     A ARG A 1 221 ? 18.19500  12.74000  9.62700  0.470 50.08245  ?  221 ARG A CG     1 
ATOM   3408 C CG     B ARG A 1 221 ? 17.34100  12.67400  8.49100  0.530 52.45960  ?  221 ARG A CG     1 
ATOM   3409 C CD     A ARG A 1 221 ? 16.82800  12.48900  10.24300 0.470 50.31530  ?  221 ARG A CD     1 
ATOM   3410 C CD     B ARG A 1 221 ? 16.56600  12.78500  9.79700  0.530 51.05449  ?  221 ARG A CD     1 
ATOM   3411 N NE     A ARG A 1 221 ? 15.75300  12.92300  9.35800  0.470 52.99122  ?  221 ARG A NE     1 
ATOM   3412 N NE     B ARG A 1 221 ? 16.13300  14.15200  10.05500 0.530 51.06013  ?  221 ARG A NE     1 
ATOM   3413 C CZ     A ARG A 1 221 ? 15.42100  14.18600  9.15100  0.470 53.64321  ?  221 ARG A CZ     1 
ATOM   3414 C CZ     B ARG A 1 221 ? 15.18000  14.77600  9.37800  0.530 54.34206  ?  221 ARG A CZ     1 
ATOM   3415 N NH1    A ARG A 1 221 ? 16.05900  15.17800  9.75600  0.470 52.05093  ?  221 ARG A NH1    1 
ATOM   3416 N NH1    B ARG A 1 221 ? 14.53500  14.18100  8.38600  0.530 54.49857  ?  221 ARG A NH1    1 
ATOM   3417 N NH2    A ARG A 1 221 ? 14.41500  14.46400  8.32400  0.470 55.78166  ?  221 ARG A NH2    1 
ATOM   3418 N NH2    B ARG A 1 221 ? 14.86400  16.03100  9.70400  0.530 55.09795  ?  221 ARG A NH2    1 
ATOM   3419 H H      A ARG A 1 221 ? 19.40700  10.24700  6.84200  0.470 56.32379  ?  221 ARG A H      1 
ATOM   3420 H H      B ARG A 1 221 ? 19.40900  10.24700  6.84600  0.530 56.32379  ?  221 ARG A H      1 
ATOM   3421 H HA     A ARG A 1 221 ? 19.41300  12.84800  7.20000  0.470 56.49956  ?  221 ARG A HA     1 
ATOM   3422 H HA     B ARG A 1 221 ? 19.43300  12.85500  7.17500  0.530 56.56281  ?  221 ARG A HA     1 
ATOM   3423 H HB2    A ARG A 1 221 ? 17.73500  11.48000  8.10100  0.470 58.38302  ?  221 ARG A HB2    1 
ATOM   3424 H HB2    B ARG A 1 221 ? 18.19000  10.82000  8.39800  0.530 58.10744  ?  221 ARG A HB2    1 
ATOM   3425 H HB3    A ARG A 1 221 ? 18.79700  10.86900  9.11300  0.470 58.38302  ?  221 ARG A HB3    1 
ATOM   3426 H HB3    B ARG A 1 221 ? 18.84600  11.74600  9.51000  0.530 58.10744  ?  221 ARG A HB3    1 
ATOM   3427 H HG2    A ARG A 1 221 ? 18.85700  12.74100  10.33600 0.470 60.21671  ?  221 ARG A HG2    1 
ATOM   3428 H HG2    B ARG A 1 221 ? 17.67200  13.55600  8.26100  0.530 63.06929  ?  221 ARG A HG2    1 
ATOM   3429 H HG3    A ARG A 1 221 ? 18.18000  13.60300  9.18500  0.470 60.21671  ?  221 ARG A HG3    1 
ATOM   3430 H HG3    B ARG A 1 221 ? 16.73300  12.35800  7.80500  0.530 63.06929  ?  221 ARG A HG3    1 
ATOM   3431 H HD2    A ARG A 1 221 ? 16.72100  11.54000  10.41000 0.470 60.49613  ?  221 ARG A HD2    1 
ATOM   3432 H HD2    B ARG A 1 221 ? 15.77800  12.22000  9.75000  0.530 61.38316  ?  221 ARG A HD2    1 
ATOM   3433 H HD3    A ARG A 1 221 ? 16.75600  12.98300  11.07500 0.470 60.49613  ?  221 ARG A HD3    1 
ATOM   3434 H HD3    B ARG A 1 221 ? 17.13300  12.50200  10.53100 0.530 61.38316  ?  221 ARG A HD3    1 
ATOM   3435 H HE     A ARG A 1 221 ? 15.30500  12.31700  8.94400  0.470 63.70723  ?  221 ARG A HE     1 
ATOM   3436 H HE     B ARG A 1 221 ? 16.52200  14.58300  10.68900 0.530 61.38992  ?  221 ARG A HE     1 
ATOM   3437 H HH11   A ARG A 1 221 ? 16.70500  15.00700  10.29700 0.470 62.57888  ?  221 ARG A HH11   1 
ATOM   3438 H HH11   B ARG A 1 221 ? 14.73200  13.37300  8.16800  0.530 65.51605  ?  221 ARG A HH11   1 
ATOM   3439 H HH12   A ARG A 1 221 ? 15.82800  15.99300  9.60700  0.470 62.57888  ?  221 ARG A HH12   1 
ATOM   3440 H HH12   B ARG A 1 221 ? 13.92000  14.60300  7.95900  0.530 65.51605  ?  221 ARG A HH12   1 
ATOM   3441 H HH21   A ARG A 1 221 ? 13.99100  13.82500  7.93400  0.470 67.05576  ?  221 ARG A HH21   1 
ATOM   3442 H HH21   B ARG A 1 221 ? 15.27800  16.42600  10.34600 0.530 66.23531  ?  221 ARG A HH21   1 
ATOM   3443 H HH22   A ARG A 1 221 ? 14.18900  15.28100  8.18100  0.470 67.05576  ?  221 ARG A HH22   1 
ATOM   3444 H HH22   B ARG A 1 221 ? 14.24700  16.44500  9.27100  0.530 66.23531  ?  221 ARG A HH22   1 
ATOM   3445 N N      . LEU A 1 222 ? 21.69200  11.23000  8.75700  1.000 46.49839  ?  222 LEU A N      1 
ATOM   3446 C CA     . LEU A 1 222 ? 22.96300  11.40700  9.44200  1.000 46.93935  ?  222 LEU A CA     1 
ATOM   3447 C C      . LEU A 1 222 ? 23.93000  12.20900  8.58300  1.000 48.26705  ?  222 LEU A C      1 
ATOM   3448 O O      . LEU A 1 222 ? 24.60200  13.12800  9.07400  1.000 48.07769  ?  222 LEU A O      1 
ATOM   3449 C CB     . LEU A 1 222 ? 23.56000  10.04800  9.79700  1.000 45.18478  ?  222 LEU A CB     1 
ATOM   3450 C CG     . LEU A 1 222 ? 24.96800  10.05600  10.40400 1.000 45.88336  ?  222 LEU A CG     1 
ATOM   3451 C CD1    . LEU A 1 222 ? 24.90500  10.36200  11.88400 1.000 49.33322  ?  222 LEU A CD1    1 
ATOM   3452 C CD2    . LEU A 1 222 ? 25.66800  8.71500   10.15800 1.000 63.08125  ?  222 LEU A CD2    1 
ATOM   3453 H H      . LEU A 1 222 ? 21.48000  10.41100  8.59900  1.000 55.91584  ?  222 LEU A H      1 
ATOM   3454 H HA     . LEU A 1 222 ? 22.81400  11.89200  10.26900 1.000 56.44499  ?  222 LEU A HA     1 
ATOM   3455 H HB2    . LEU A 1 222 ? 22.97500  9.62200   10.44300 1.000 54.33950  ?  222 LEU A HB2    1 
ATOM   3456 H HB3    . LEU A 1 222 ? 23.60300  9.51700   8.98700  1.000 54.33950  ?  222 LEU A HB3    1 
ATOM   3457 H HG     . LEU A 1 222 ? 25.49200  10.75000  9.97500  1.000 55.17780  ?  222 LEU A HG     1 
ATOM   3458 H HD11   . LEU A 1 222 ? 25.80800  10.41500  12.23400 1.000 59.31763  ?  222 LEU A HD11   1 
ATOM   3459 H HD12   . LEU A 1 222 ? 24.45000  11.20900  12.01200 1.000 59.31763  ?  222 LEU A HD12   1 
ATOM   3460 H HD13   . LEU A 1 222 ? 24.41700  9.65300   12.33200 1.000 59.31763  ?  222 LEU A HD13   1 
ATOM   3461 H HD21   . LEU A 1 222 ? 26.54500  8.73600   10.57000 1.000 75.81527  ?  222 LEU A HD21   1 
ATOM   3462 H HD22   . LEU A 1 222 ? 25.13600  8.00400   10.55000 1.000 75.81527  ?  222 LEU A HD22   1 
ATOM   3463 H HD23   . LEU A 1 222 ? 25.75400  8.57400   9.20200  1.000 75.81527  ?  222 LEU A HD23   1 
ATOM   3464 N N      . GLU A 1 223 ? 24.00200  11.88700  7.28900  1.000 47.08082  ?  223 GLU A N      1 
ATOM   3465 C CA     . GLU A 1 223 ? 24.89300  12.63100  6.40000  1.000 57.56758  ?  223 GLU A CA     1 
ATOM   3466 C C      . GLU A 1 223 ? 24.49000  14.09900  6.32000  1.000 59.94934  ?  223 GLU A C      1 
ATOM   3467 O O      . GLU A 1 223 ? 25.34900  14.98600  6.23200  1.000 56.47130  ?  223 GLU A O      1 
ATOM   3468 C CB     . GLU A 1 223 ? 24.89400  11.98300  5.01600  1.000 62.74815  ?  223 GLU A CB     1 
ATOM   3469 C CG     . GLU A 1 223 ? 26.26900  11.89400  4.33500  1.000 85.39309  ?  223 GLU A CG     1 
ATOM   3470 C CD     . GLU A 1 223 ? 27.35400  11.34300  5.24200  1.000 75.40609  ?  223 GLU A CD     1 
ATOM   3471 O OE1    . GLU A 1 223 ? 27.22800  10.18400  5.69000  1.000 73.83090  ?  223 GLU A OE1    1 
ATOM   3472 O OE2    . GLU A 1 223 ? 28.33700  12.07300  5.51500  1.000 71.93917  -1 223 GLU A OE2    1 
ATOM   3473 H H      . GLU A 1 223 ? 23.55600  11.25600  6.91100  1.000 56.61476  ?  223 GLU A H      1 
ATOM   3474 H HA     . GLU A 1 223 ? 25.79800  12.59500  6.74800  1.000 69.19887  ?  223 GLU A HA     1 
ATOM   3475 H HB2    . GLU A 1 223 ? 24.55400  11.07800  5.10100  1.000 75.41555  ?  223 GLU A HB2    1 
ATOM   3476 H HB3    . GLU A 1 223 ? 24.31600  12.50100  4.43500  1.000 75.41555  ?  223 GLU A HB3    1 
ATOM   3477 H HG2    . GLU A 1 223 ? 26.20000  11.31000  3.56400  1.000 102.58948 ?  223 GLU A HG2    1 
ATOM   3478 H HG3    . GLU A 1 223 ? 26.53800  12.78300  4.05500  1.000 102.58948 ?  223 GLU A HG3    1 
ATOM   3479 N N      . ALA A 1 224 ? 23.18300  14.37900  6.36200  1.000 56.04442  ?  224 ALA A N      1 
ATOM   3480 C CA     . ALA A 1 224 ? 22.72400  15.76500  6.31700  1.000 60.30659  ?  224 ALA A CA     1 
ATOM   3481 C C      . ALA A 1 224 ? 23.14000  16.53500  7.57000  1.000 55.01084  ?  224 ALA A C      1 
ATOM   3482 O O      . ALA A 1 224 ? 23.50500  17.71300  7.48400  1.000 55.90785  ?  224 ALA A O      1 
ATOM   3483 C CB     . ALA A 1 224 ? 21.20600  15.81400  6.14600  1.000 56.00405  ?  224 ALA A CB     1 
ATOM   3484 H H      . ALA A 1 224 ? 22.55500  13.79400  6.41600  1.000 67.37108  ?  224 ALA A H      1 
ATOM   3485 H HA     . ALA A 1 224 ? 23.13000  16.19700  5.54900  1.000 72.48568  ?  224 ALA A HA     1 
ATOM   3486 H HB1    . ALA A 1 224 ? 20.92100  16.74000  6.11000  1.000 67.32263  ?  224 ALA A HB1    1 
ATOM   3487 H HB2    . ALA A 1 224 ? 20.96600  15.36100  5.32300  1.000 67.32263  ?  224 ALA A HB2    1 
ATOM   3488 H HB3    . ALA A 1 224 ? 20.78900  15.36900  6.90100  1.000 67.32263  ?  224 ALA A HB3    1 
ATOM   3489 N N      . ALA A 1 225 ? 23.07500  15.89500  8.74000  1.000 46.89793  ?  225 ALA A N      1 
ATOM   3490 C CA     . ALA A 1 225 ? 23.48000  16.56800  9.96700  1.000 47.84489  ?  225 ALA A CA     1 
ATOM   3491 C C      . ALA A 1 225 ? 24.97200  16.90000  9.96200  1.000 51.97285  ?  225 ALA A C      1 
ATOM   3492 O O      . ALA A 1 225 ? 25.38400  17.91600  10.52500 1.000 53.78582  ?  225 ALA A O      1 
ATOM   3493 C CB     . ALA A 1 225 ? 23.14300  15.70600  11.18300 1.000 45.65505  ?  225 ALA A CB     1 
ATOM   3494 H H      . ALA A 1 225 ? 22.80500  15.08500  8.84500  1.000 56.39528  ?  225 ALA A H      1 
ATOM   3495 H HA     . ALA A 1 225 ? 22.98300  17.39700  10.03800 1.000 57.53164  ?  225 ALA A HA     1 
ATOM   3496 H HB1    . ALA A 1 225 ? 23.42000  16.17200  11.98700 1.000 54.90384  ?  225 ALA A HB1    1 
ATOM   3497 H HB2    . ALA A 1 225 ? 22.18600  15.55000  11.20400 1.000 54.90384  ?  225 ALA A HB2    1 
ATOM   3498 H HB3    . ALA A 1 225 ? 23.61400  14.86100  11.11200 1.000 54.90384  ?  225 ALA A HB3    1 
ATOM   3499 N N      . PHE A 1 226 ? 25.79100  16.05400  9.34000  1.000 51.72791  ?  226 PHE A N      1 
ATOM   3500 C CA     . PHE A 1 226 ? 27.22400  16.26400  9.27300  1.000 53.72817  ?  226 PHE A CA     1 
ATOM   3501 C C      . PHE A 1 226 ? 27.64700  17.06600  8.04700  1.000 52.78886  ?  226 PHE A C      1 
ATOM   3502 O O      . PHE A 1 226 ? 28.84500  17.20300  7.80300  1.000 52.94834  ?  226 PHE A O      1 
ATOM   3503 C CB     . PHE A 1 226 ? 27.94800  14.91600  9.31300  1.000 48.51704  ?  226 PHE A CB     1 
ATOM   3504 C CG     . PHE A 1 226 ? 28.05800  14.34000  10.69700 1.000 54.82166  ?  226 PHE A CG     1 
ATOM   3505 C CD1    . PHE A 1 226 ? 26.96600  13.73400  11.29900 1.000 55.69962  ?  226 PHE A CD1    1 
ATOM   3506 C CD2    . PHE A 1 226 ? 29.24600  14.42700  11.41200 1.000 50.74448  ?  226 PHE A CD2    1 
ATOM   3507 C CE1    . PHE A 1 226 ? 27.05700  13.21000  12.57700 1.000 52.65651  ?  226 PHE A CE1    1 
ATOM   3508 C CE2    . PHE A 1 226 ? 29.34300  13.90700  12.69200 1.000 49.92147  ?  226 PHE A CE2    1 
ATOM   3509 C CZ     . PHE A 1 226 ? 28.24200  13.30400  13.28000 1.000 48.92855  ?  226 PHE A CZ     1 
ATOM   3510 H H      . PHE A 1 226 ? 25.52900  15.33800  8.94200  1.000 62.19126  ?  226 PHE A H      1 
ATOM   3511 H HA     . PHE A 1 226 ? 27.50500  16.76800  10.05200 1.000 64.59157  ?  226 PHE A HA     1 
ATOM   3512 H HB2    . PHE A 1 226 ? 27.45900  14.28200  8.76500  1.000 58.33822  ?  226 PHE A HB2    1 
ATOM   3513 H HB3    . PHE A 1 226 ? 28.84600  15.03200  8.96500  1.000 58.33822  ?  226 PHE A HB3    1 
ATOM   3514 H HD1    . PHE A 1 226 ? 26.16100  13.67800  10.83800 1.000 66.95731  ?  226 PHE A HD1    1 
ATOM   3515 H HD2    . PHE A 1 226 ? 29.98600  14.83800  11.02600 1.000 61.01115  ?  226 PHE A HD2    1 
ATOM   3516 H HE1    . PHE A 1 226 ? 26.32000  12.79500  12.96300 1.000 63.30558  ?  226 PHE A HE1    1 
ATOM   3517 H HE2    . PHE A 1 226 ? 30.14600  13.96300  13.15700 1.000 60.02353  ?  226 PHE A HE2    1 
ATOM   3518 H HZ     . PHE A 1 226 ? 28.30200  12.96400  14.14400 1.000 58.83203  ?  226 PHE A HZ     1 
ATOM   3519 N N      . GLN A 1 227 ? 26.68500  17.59800  7.28100  1.000 57.54126  ?  227 GLN A N      1 
ATOM   3520 C CA     . GLN A 1 227 ? 27.01900  18.44400  6.14100  1.000 59.11614  ?  227 GLN A CA     1 
ATOM   3521 C C      . GLN A 1 227 ? 27.73000  19.71600  6.57700  1.000 54.90053  ?  227 GLN A C      1 
ATOM   3522 O O      . GLN A 1 227 ? 28.51100  20.28600  5.81000  1.000 53.69202  ?  227 GLN A O      1 
ATOM   3523 C CB     . GLN A 1 227 ? 25.74900  18.81100  5.36000  1.000 65.61267  ?  227 GLN A CB     1 
ATOM   3524 C CG     . GLN A 1 227 ? 25.31700  17.76100  4.33600  1.000 89.49453  ?  227 GLN A CG     1 
ATOM   3525 C CD     . GLN A 1 227 ? 23.94000  18.04300  3.73500  1.000 100.81146 ?  227 GLN A CD     1 
ATOM   3526 O OE1    . GLN A 1 227 ? 23.18900  17.11500  3.40400  1.000 100.78444 ?  227 GLN A OE1    1 
ATOM   3527 N NE2    . GLN A 1 227 ? 23.60600  19.32200  3.58900  1.000 89.70393  ?  227 GLN A NE2    1 
ATOM   3528 H H      . GLN A 1 227 ? 25.84100  17.48200  7.40200  1.000 69.16728  ?  227 GLN A H      1 
ATOM   3529 H HA     . GLN A 1 227 ? 27.60800  17.94400  5.55400  1.000 71.05714  ?  227 GLN A HA     1 
ATOM   3530 H HB2    . GLN A 1 227 ? 25.02000  18.92600  5.98900  1.000 78.85298  ?  227 GLN A HB2    1 
ATOM   3531 H HB3    . GLN A 1 227 ? 25.90800  19.64000  4.88200  1.000 78.85298  ?  227 GLN A HB3    1 
ATOM   3532 H HG2    . GLN A 1 227 ? 25.96200  17.74300  3.61100  1.000 107.51121 ?  227 GLN A HG2    1 
ATOM   3533 H HG3    . GLN A 1 227 ? 25.28200  16.89400  4.77000  1.000 107.51121 ?  227 GLN A HG3    1 
ATOM   3534 H HE21   . GLN A 1 227 ? 24.15400  19.94000  3.82800  1.000 107.76249 ?  227 GLN A HE21   1 
ATOM   3535 H HE22   . GLN A 1 227 ? 22.84100  19.53100  3.25500  1.000 107.76249 ?  227 GLN A HE22   1 
ATOM   3536 N N      . ASP A 1 228 ? 27.46300  20.19500  7.79500  1.000 52.43270  ?  228 ASP A N      1 
ATOM   3537 C CA     . ASP A 1 228 ? 28.11300  21.37800  8.35000  1.000 55.95072  ?  228 ASP A CA     1 
ATOM   3538 C C      . ASP A 1 228 ? 28.84700  20.98100  9.62500  1.000 50.09199  ?  228 ASP A C      1 
ATOM   3539 O O      . ASP A 1 228 ? 28.24600  20.95800  10.70600 1.000 49.70231  ?  228 ASP A O      1 
ATOM   3540 C CB     . ASP A 1 228 ? 27.09400  22.48000  8.64600  1.000 57.39817  ?  228 ASP A CB     1 
ATOM   3541 C CG     . ASP A 1 228 ? 27.76000  23.76300  9.11400  1.000 58.57346  ?  228 ASP A CG     1 
ATOM   3542 O OD1    . ASP A 1 228 ? 29.01000  23.77300  9.23300  1.000 55.55053  ?  228 ASP A OD1    1 
ATOM   3543 O OD2    . ASP A 1 228 ? 27.04200  24.75400  9.37600  1.000 61.63640  -1 228 ASP A OD2    1 
ATOM   3544 H H      . ASP A 1 228 ? 26.89300  19.83900  8.33100  1.000 63.03700  ?  228 ASP A H      1 
ATOM   3545 H HA     . ASP A 1 228 ? 28.75900  21.71000  7.70700  1.000 67.25863  ?  228 ASP A HA     1 
ATOM   3546 H HB2    . ASP A 1 228 ? 26.59400  22.67600  7.83800  1.000 68.99557  ?  228 ASP A HB2    1 
ATOM   3547 H HB3    . ASP A 1 228 ? 26.49300  22.17900  9.34400  1.000 68.99557  ?  228 ASP A HB3    1 
ATOM   3548 N N      . PRO A 1 229 ? 30.15200  20.68000  9.53900  1.000 49.14511  ?  229 PRO A N      1 
ATOM   3549 C CA     . PRO A 1 229 ? 30.87700  20.26400  10.75400 1.000 48.62264  ?  229 PRO A CA     1 
ATOM   3550 C C      . PRO A 1 229 ? 30.88600  21.32000  11.84900 1.000 48.61721  ?  229 PRO A C      1 
ATOM   3551 O O      . PRO A 1 229 ? 30.98200  20.96600  13.03600 1.000 49.57144  ?  229 PRO A O      1 
ATOM   3552 C CB     . PRO A 1 229 ? 32.30600  19.98400  10.24100 1.000 52.45232  ?  229 PRO A CB     1 
ATOM   3553 C CG     . PRO A 1 229 ? 32.20100  19.91100  8.75400  1.000 52.32587  ?  229 PRO A CG     1 
ATOM   3554 C CD     . PRO A 1 229 ? 31.03800  20.78100  8.37200  1.000 54.40160  ?  229 PRO A CD     1 
ATOM   3555 H HA     . PRO A 1 229 ? 30.48900  19.44400  11.09700 1.000 58.46494  ?  229 PRO A HA     1 
ATOM   3556 H HB2    . PRO A 1 229 ? 32.89600  20.70500  10.50900 1.000 63.06056  ?  229 PRO A HB2    1 
ATOM   3557 H HB3    . PRO A 1 229 ? 32.62400  19.14300  10.60500 1.000 63.06056  ?  229 PRO A HB3    1 
ATOM   3558 H HG2    . PRO A 1 229 ? 33.02100  20.24000  8.35300  1.000 62.90881  ?  229 PRO A HG2    1 
ATOM   3559 H HG3    . PRO A 1 229 ? 32.04500  18.99300  8.48300  1.000 62.90881  ?  229 PRO A HG3    1 
ATOM   3560 H HD2    . PRO A 1 229 ? 31.32300  21.69800  8.23100  1.000 65.39969  ?  229 PRO A HD2    1 
ATOM   3561 H HD3    . PRO A 1 229 ? 30.60000  20.44400  7.57400  1.000 65.39969  ?  229 PRO A HD3    1 
ATOM   3562 N N      . LYS A 1 230 ? 30.80900  22.60000  11.49000 1.000 46.57358  ?  230 LYS A N      1 
ATOM   3563 C CA     . LYS A 1 230 ? 30.79300  23.65700  12.49300 1.000 47.98430  ?  230 LYS A CA     1 
ATOM   3564 C C      . LYS A 1 230 ? 29.49500  23.64300  13.28600 1.000 45.61068  ?  230 LYS A C      1 
ATOM   3565 O O      . LYS A 1 230 ? 29.48000  23.95000  14.48500 1.000 45.44508  ?  230 LYS A O      1 
ATOM   3566 C CB     . LYS A 1 230 ? 30.99900  25.02400  11.82800 1.000 46.93141  ?  230 LYS A CB     1 
ATOM   3567 C CG     . LYS A 1 230 ? 32.35500  25.20200  11.16600 0.000 48.72778  ?  230 LYS A CG     1 
ATOM   3568 C CD     . LYS A 1 230 ? 33.16600  26.30500  11.83400 0.000 48.87891  ?  230 LYS A CD     1 
ATOM   3569 C CE     . LYS A 1 230 ? 33.80500  25.82400  13.12800 0.000 49.52061  ?  230 LYS A CE     1 
ATOM   3570 N NZ     . LYS A 1 230 ? 35.09600  26.51300  13.41000 0.000 53.95591  ?  230 LYS A NZ     1 
ATOM   3571 H H      . LYS A 1 230 ? 30.76600  22.88000  10.67800 1.000 56.00606  ?  230 LYS A H      1 
ATOM   3572 H HA     . LYS A 1 230 ? 31.52700  23.51100  13.11000 1.000 57.69893  ?  230 LYS A HA     1 
ATOM   3573 H HB2    . LYS A 1 230 ? 30.32100  25.14000  11.14400 1.000 56.43547  ?  230 LYS A HB2    1 
ATOM   3574 H HB3    . LYS A 1 230 ? 30.91000  25.71300  12.50500 1.000 56.43547  ?  230 LYS A HB3    1 
ATOM   3575 H HG2    . LYS A 1 230 ? 32.85500  24.37300  11.23300 1.000 58.59110  ?  230 LYS A HG2    1 
ATOM   3576 H HG3    . LYS A 1 230 ? 32.22800  25.43900  10.23400 1.000 58.59110  ?  230 LYS A HG3    1 
ATOM   3577 H HD2    . LYS A 1 230 ? 33.87200  26.59200  11.23400 1.000 58.77247  ?  230 LYS A HD2    1 
ATOM   3578 H HD3    . LYS A 1 230 ? 32.58300  27.05200  12.04200 1.000 58.77247  ?  230 LYS A HD3    1 
ATOM   3579 H HE2    . LYS A 1 230 ? 33.20100  26.00000  13.86600 1.000 59.54250  ?  230 LYS A HE2    1 
ATOM   3580 H HE3    . LYS A 1 230 ? 33.98000  24.87200  13.06200 1.000 59.54250  ?  230 LYS A HE3    1 
ATOM   3581 H HZ1    . LYS A 1 230 ? 35.47100  26.17000  14.14000 1.000 64.86486  ?  230 LYS A HZ1    1 
ATOM   3582 H HZ2    . LYS A 1 230 ? 35.65200  26.41100  12.72300 1.000 64.86486  ?  230 LYS A HZ2    1 
ATOM   3583 H HZ3    . LYS A 1 230 ? 34.95400  27.38200  13.54000 1.000 64.86486  ?  230 LYS A HZ3    1 
ATOM   3584 N N      . TRP A 1 231 ? 28.38300  23.30900  12.63100 1.000 48.52239  ?  231 TRP A N      1 
ATOM   3585 C CA     . TRP A 1 231 ? 27.13700  23.14800  13.36900 1.000 50.27124  ?  231 TRP A CA     1 
ATOM   3586 C C      . TRP A 1 231 ? 27.22800  21.96700  14.32600 1.000 47.18767  ?  231 TRP A C      1 
ATOM   3587 O O      . TRP A 1 231 ? 26.78900  22.05800  15.47900 1.000 47.40596  ?  231 TRP A O      1 
ATOM   3588 C CB     . TRP A 1 231 ? 25.96500  22.97600  12.39800 1.000 47.94433  ?  231 TRP A CB     1 
ATOM   3589 C CG     . TRP A 1 231 ? 24.66200  22.75900  13.11200 1.000 51.91347  ?  231 TRP A CG     1 
ATOM   3590 C CD1    . TRP A 1 231 ? 23.83400  23.72700  13.60500 1.000 51.16567  ?  231 TRP A CD1    1 
ATOM   3591 C CD2    . TRP A 1 231 ? 24.05000  21.50600  13.43000 1.000 47.60854  ?  231 TRP A CD2    1 
ATOM   3592 N NE1    . TRP A 1 231 ? 22.74100  23.14800  14.20000 1.000 49.90181  ?  231 TRP A NE1    1 
ATOM   3593 C CE2    . TRP A 1 231 ? 22.85000  21.78700  14.10300 1.000 50.43995  ?  231 TRP A CE2    1 
ATOM   3594 C CE3    . TRP A 1 231 ? 24.39800  20.16900  13.20100 1.000 53.55208  ?  231 TRP A CE3    1 
ATOM   3595 C CZ2    . TRP A 1 231 ? 21.98400  20.78300  14.55000 1.000 47.29367  ?  231 TRP A CZ2    1 
ATOM   3596 C CZ3    . TRP A 1 231 ? 23.54600  19.17100  13.65000 1.000 50.69821  ?  231 TRP A CZ3    1 
ATOM   3597 C CH2    . TRP A 1 231 ? 22.35800  19.48700  14.32100 1.000 49.83418  ?  231 TRP A CH2    1 
ATOM   3598 H H      . TRP A 1 231 ? 28.32600  23.17500  11.78400 1.000 58.34464  ?  231 TRP A H      1 
ATOM   3599 H HA     . TRP A 1 231 ? 26.96900  23.94800  13.89000 1.000 60.44326  ?  231 TRP A HA     1 
ATOM   3600 H HB2    . TRP A 1 231 ? 25.88200  23.77600  11.85500 1.000 57.65097  ?  231 TRP A HB2    1 
ATOM   3601 H HB3    . TRP A 1 231 ? 26.13100  22.20700  11.83100 1.000 57.65097  ?  231 TRP A HB3    1 
ATOM   3602 H HD1    . TRP A 1 231 ? 23.98800  24.64200  13.54600 1.000 61.51657  ?  231 TRP A HD1    1 
ATOM   3603 H HE1    . TRP A 1 231 ? 22.09200  23.57200  14.57300 1.000 59.99994  ?  231 TRP A HE1    1 
ATOM   3604 H HE3    . TRP A 1 231 ? 25.18700  19.95300  12.75700 1.000 64.38026  ?  231 TRP A HE3    1 
ATOM   3605 H HZ2    . TRP A 1 231 ? 21.18900  20.98800  14.98600 1.000 56.87017  ?  231 TRP A HZ2    1 
ATOM   3606 H HZ3    . TRP A 1 231 ? 23.76600  18.28000  13.50400 1.000 60.95563  ?  231 TRP A HZ3    1 
ATOM   3607 H HH2    . TRP A 1 231 ? 21.80800  18.79700  14.61700 1.000 59.91879  ?  231 TRP A HH2    1 
ATOM   3608 N N      . VAL A 1 232 ? 27.80400  20.85200  13.86600 1.000 41.50063  ?  232 VAL A N      1 
ATOM   3609 C CA     . VAL A 1 232 ? 27.96400  19.68800  14.72600 1.000 45.91393  ?  232 VAL A CA     1 
ATOM   3610 C C      . VAL A 1 232 ? 28.88500  20.00700  15.88900 1.000 44.93740  ?  232 VAL A C      1 
ATOM   3611 O O      . VAL A 1 232 ? 28.60200  19.64900  17.04400 1.000 45.38030  ?  232 VAL A O      1 
ATOM   3612 C CB     . VAL A 1 232 ? 28.49000  18.49900  13.90300 1.000 46.61281  ?  232 VAL A CB     1 
ATOM   3613 C CG1    . VAL A 1 232 ? 28.84100  17.33200  14.81800 1.000 48.38571  ?  232 VAL A CG1    1 
ATOM   3614 C CG2    . VAL A 1 232 ? 27.46500  18.08600  12.86200 1.000 49.69495  ?  232 VAL A CG2    1 
ATOM   3615 H H      . VAL A 1 232 ? 28.10700  20.74900  13.06700 1.000 49.91853  ?  232 VAL A H      1 
ATOM   3616 H HA     . VAL A 1 232 ? 27.09700  19.45100  15.09000 1.000 55.21449  ?  232 VAL A HA     1 
ATOM   3617 H HB     . VAL A 1 232 ? 29.29900  18.76400  13.43800 1.000 56.05314  ?  232 VAL A HB     1 
ATOM   3618 H HG11   . VAL A 1 232 ? 28.98200  16.53800  14.27800 1.000 58.18062  ?  232 VAL A HG11   1 
ATOM   3619 H HG12   . VAL A 1 232 ? 29.65000  17.54600  15.30700 1.000 58.18062  ?  232 VAL A HG12   1 
ATOM   3620 H HG13   . VAL A 1 232 ? 28.10900  17.18500  15.43700 1.000 58.18062  ?  232 VAL A HG13   1 
ATOM   3621 H HG21   . VAL A 1 232 ? 27.82700  17.35900  12.33200 1.000 59.75171  ?  232 VAL A HG21   1 
ATOM   3622 H HG22   . VAL A 1 232 ? 26.65600  17.79600  13.31300 1.000 59.75171  ?  232 VAL A HG22   1 
ATOM   3623 H HG23   . VAL A 1 232 ? 27.27000  18.84600  12.29200 1.000 59.75171  ?  232 VAL A HG23   1 
ATOM   3624 N N      . ALA A 1 233 ? 30.01100  20.68500  15.60600 1.000 44.26364  ?  233 ALA A N      1 
ATOM   3625 C CA     . ALA A 1 233 ? 30.99300  20.97500  16.65300 1.000 43.28256  ?  233 ALA A CA     1 
ATOM   3626 C C      . ALA A 1 233 ? 30.43600  21.91400  17.71700 1.000 44.11359  ?  233 ALA A C      1 
ATOM   3627 O O      . ALA A 1 233 ? 30.69600  21.72300  18.90900 1.000 48.56389  ?  233 ALA A O      1 
ATOM   3628 C CB     . ALA A 1 233 ? 32.24900  21.57600  16.02300 1.000 47.20191  ?  233 ALA A CB     1 
ATOM   3629 H H      . ALA A 1 233 ? 30.22200  20.98300  14.82700 1.000 53.23414  ?  233 ALA A H      1 
ATOM   3630 H HA     . ALA A 1 233 ? 31.22900  20.14200  17.09200 1.000 52.05685  ?  233 ALA A HA     1 
ATOM   3631 H HB1    . ALA A 1 233 ? 32.89600  21.76000  16.72200 1.000 56.76006  ?  233 ALA A HB1    1 
ATOM   3632 H HB2    . ALA A 1 233 ? 32.61900  20.94200  15.38800 1.000 56.76006  ?  233 ALA A HB2    1 
ATOM   3633 H HB3    . ALA A 1 233 ? 32.01100  22.39900  15.56700 1.000 56.76006  ?  233 ALA A HB3    1 
ATOM   3634 N N      . GLY A 1 234 ? 29.68000  22.93900  17.31100 1.000 43.92293  ?  234 GLY A N      1 
ATOM   3635 C CA     . GLY A 1 234 ? 29.17100  23.94200  18.21800 1.000 40.35710  ?  234 GLY A CA     1 
ATOM   3636 C C      . GLY A 1 234 ? 27.82700  23.63800  18.83400 1.000 45.95063  ?  234 GLY A C      1 
ATOM   3637 O O      . GLY A 1 234 ? 27.29300  24.47200  19.57800 1.000 49.37000  ?  234 GLY A O      1 
ATOM   3638 H H      . GLY A 1 234 ? 29.44800  23.06800  16.49300 1.000 52.82529  ?  234 GLY A H      1 
ATOM   3639 H HA2    . GLY A 1 234 ? 29.80700  24.05400  18.94200 1.000 48.54628  ?  234 GLY A HA2    1 
ATOM   3640 H HA3    . GLY A 1 234 ? 29.09000  24.78100  17.73700 1.000 48.54628  ?  234 GLY A HA3    1 
ATOM   3641 N N      . PHE A 1 235 ? 27.26500  22.46400  18.55200 1.000 44.63629  ?  235 PHE A N      1 
ATOM   3642 C CA     . PHE A 1 235 ? 25.92200  22.12000  19.01800 1.000 42.40305  ?  235 PHE A CA     1 
ATOM   3643 C C      . PHE A 1 235 ? 25.79300  22.26800  20.52700 1.000 43.45533  ?  235 PHE A C      1 
ATOM   3644 O O      . PHE A 1 235 ? 26.62200  21.76400  21.29600 1.000 46.10082  ?  235 PHE A O      1 
ATOM   3645 C CB     . PHE A 1 235 ? 25.63200  20.66400  18.59200 1.000 47.15736  ?  235 PHE A CB     1 
ATOM   3646 C CG     . PHE A 1 235 ? 24.23000  20.21100  18.84100 1.000 43.95034  ?  235 PHE A CG     1 
ATOM   3647 C CD1    . PHE A 1 235 ? 23.86000  19.68700  20.06900 1.000 46.58644  ?  235 PHE A CD1    1 
ATOM   3648 C CD2    . PHE A 1 235 ? 23.28900  20.25700  17.83000 1.000 49.37215  ?  235 PHE A CD2    1 
ATOM   3649 C CE1    . PHE A 1 235 ? 22.55900  19.24300  20.29700 1.000 46.62068  ?  235 PHE A CE1    1 
ATOM   3650 C CE2    . PHE A 1 235 ? 21.99300  19.81100  18.04400 1.000 47.69104  ?  235 PHE A CE2    1 
ATOM   3651 C CZ     . PHE A 1 235 ? 21.63200  19.31300  19.28100 1.000 45.06180  ?  235 PHE A CZ     1 
ATOM   3652 H H      . PHE A 1 235 ? 27.64200  21.84600  18.08800 1.000 53.68132  ?  235 PHE A H      1 
ATOM   3653 H HA     . PHE A 1 235 ? 25.26900  22.71800  18.62200 1.000 51.00143  ?  235 PHE A HA     1 
ATOM   3654 H HB2    . PHE A 1 235 ? 25.80200  20.58100  17.64100 1.000 56.70660  ?  235 PHE A HB2    1 
ATOM   3655 H HB3    . PHE A 1 235 ? 26.22200  20.07400  19.08700 1.000 56.70660  ?  235 PHE A HB3    1 
ATOM   3656 H HD1    . PHE A 1 235 ? 24.48900  19.63000  20.75100 1.000 56.02150  ?  235 PHE A HD1    1 
ATOM   3657 H HD2    . PHE A 1 235 ? 23.52700  20.59200  16.99500 1.000 59.36435  ?  235 PHE A HD2    1 
ATOM   3658 H HE1    . PHE A 1 235 ? 22.31900  18.90200  21.12900 1.000 56.06258  ?  235 PHE A HE1    1 
ATOM   3659 H HE2    . PHE A 1 235 ? 21.36800  19.84600  17.35600 1.000 57.34702  ?  235 PHE A HE2    1 
ATOM   3660 H HZ     . PHE A 1 235 ? 20.76100  19.02400  19.42800 1.000 54.19193  ?  235 PHE A HZ     1 
ATOM   3661 N N      . GLN A 1 236 ? 24.74700  22.96100  20.95400 1.000 39.43597  ?  236 GLN A N      1 
ATOM   3662 C CA     . GLN A 1 236 ? 24.38400  23.07700  22.36500 1.000 46.92871  ?  236 GLN A CA     1 
ATOM   3663 C C      . GLN A 1 236 ? 22.87400  22.89700  22.48800 1.000 46.35236  ?  236 GLN A C      1 
ATOM   3664 O O      . GLN A 1 236 ? 22.11000  23.80700  22.12300 1.000 44.39158  ?  236 GLN A O      1 
ATOM   3665 C CB     . GLN A 1 236 ? 24.81300  24.42400  22.95700 1.000 54.33141  ?  236 GLN A CB     1 
ATOM   3666 C CG     . GLN A 1 236 ? 26.02300  25.05900  22.28100 1.000 68.45321  ?  236 GLN A CG     1 
ATOM   3667 C CD     . GLN A 1 236 ? 26.83200  25.93200  23.23000 1.000 72.07323  ?  236 GLN A CD     1 
ATOM   3668 O OE1    . GLN A 1 236 ? 26.83700  25.71500  24.44200 1.000 67.59498  ?  236 GLN A OE1    1 
ATOM   3669 N NE2    . GLN A 1 236 ? 27.53100  26.91700  22.67700 1.000 82.86741  ?  236 GLN A NE2    1 
ATOM   3670 H H      . GLN A 1 236 ? 24.21300  23.38800  20.43100 1.000 47.44093  ?  236 GLN A H      1 
ATOM   3671 H HA     . GLN A 1 236 ? 24.82600  22.36900  22.85900 1.000 56.43222  ?  236 GLN A HA     1 
ATOM   3672 H HB2    . GLN A 1 236 ? 24.07300  25.04700  22.87700 1.000 65.31546  ?  236 GLN A HB2    1 
ATOM   3673 H HB3    . GLN A 1 236 ? 25.03600  24.29300  23.89200 1.000 65.31546  ?  236 GLN A HB3    1 
ATOM   3674 H HG2    . GLN A 1 236 ? 26.60400  24.35700  21.94900 1.000 82.26162  ?  236 GLN A HG2    1 
ATOM   3675 H HG3    . GLN A 1 236 ? 25.72000  25.61500  21.54600 1.000 82.26162  ?  236 GLN A HG3    1 
ATOM   3676 H HE21   . GLN A 1 236 ? 27.51000  27.03300  21.82500 1.000 99.55866  ?  236 GLN A HE21   1 
ATOM   3677 H HE22   . GLN A 1 236 ? 28.00400  27.43800  23.17100 1.000 99.55866  ?  236 GLN A HE22   1 
ATOM   3678 N N      . LYS A 1 237 ? 22.45700  21.75200  23.02200 1.000 47.07194  ?  237 LYS A N      1 
ATOM   3679 C CA     . LYS A 1 237 ? 21.03000  21.39900  23.05900 1.000 47.18629  ?  237 LYS A CA     1 
ATOM   3680 C C      . LYS A 1 237 ? 20.13700  22.46800  23.67400 1.000 42.84513  ?  237 LYS A C      1 
ATOM   3681 O O      . LYS A 1 237 ? 19.07800  22.74400  23.09400 1.000 45.54474  ?  237 LYS A O      1 
ATOM   3682 C CB     . LYS A 1 237 ? 20.87600  20.07100  23.82400 1.000 44.86704  ?  237 LYS A CB     1 
ATOM   3683 C CG     . LYS A 1 237 ? 19.43800  19.52200  23.89300 1.000 42.61102  ?  237 LYS A CG     1 
ATOM   3684 C CD     . LYS A 1 237 ? 18.78600  19.46400  22.51600 1.000 42.66253  ?  237 LYS A CD     1 
ATOM   3685 C CE     . LYS A 1 237 ? 17.76100  18.34300  22.41300 1.000 44.65474  ?  237 LYS A CE     1 
ATOM   3686 N NZ     . LYS A 1 237 ? 18.30200  16.99000  22.75500 1.000 44.21710  ?  237 LYS A NZ     1 
ATOM   3687 H H      . LYS A 1 237 ? 22.97400  21.16000  23.37000 1.000 56.60410  ?  237 LYS A H      1 
ATOM   3688 H HA     . LYS A 1 237 ? 20.73100  21.28300  22.14300 1.000 56.74131  ?  237 LYS A HA     1 
ATOM   3689 H HB2    . LYS A 1 237 ? 21.42300  19.40000  23.38800 1.000 53.95822  ?  237 LYS A HB2    1 
ATOM   3690 H HB3    . LYS A 1 237 ? 21.17900  20.20600  24.73600 1.000 53.95822  ?  237 LYS A HB3    1 
ATOM   3691 H HG2    . LYS A 1 237 ? 19.45600  18.62400  24.25800 1.000 51.25099  ?  237 LYS A HG2    1 
ATOM   3692 H HG3    . LYS A 1 237 ? 18.90200  20.10000  24.45800 1.000 51.25099  ?  237 LYS A HG3    1 
ATOM   3693 H HD2    . LYS A 1 237 ? 18.33400  20.30400  22.34200 1.000 51.31280  ?  237 LYS A HD2    1 
ATOM   3694 H HD3    . LYS A 1 237 ? 19.47000  19.31000  21.84600 1.000 51.31280  ?  237 LYS A HD3    1 
ATOM   3695 H HE2    . LYS A 1 237 ? 17.03100  18.53100  23.02400 1.000 53.70346  ?  237 LYS A HE2    1 
ATOM   3696 H HE3    . LYS A 1 237 ? 17.42900  18.30600  21.50200 1.000 53.70346  ?  237 LYS A HE3    1 
ATOM   3697 H HZ1    . LYS A 1 237 ? 17.72500  16.36000  22.50700 1.000 53.17828  ?  237 LYS A HZ1    1 
ATOM   3698 H HZ2    . LYS A 1 237 ? 19.07400  16.85600  22.33300 1.000 53.17828  ?  237 LYS A HZ2    1 
ATOM   3699 H HZ3    . LYS A 1 237 ? 18.43800  16.92900  23.63200 1.000 53.17828  ?  237 LYS A HZ3    1 
ATOM   3700 N N      . PRO A 1 238 ? 20.48600  23.10600  24.79700 1.000 47.87662  ?  238 PRO A N      1 
ATOM   3701 C CA     . PRO A 1 238 ? 19.57600  24.09800  25.39600 1.000 47.21885  ?  238 PRO A CA     1 
ATOM   3702 C C      . PRO A 1 238 ? 19.39600  25.37200  24.58200 1.000 45.88397  ?  238 PRO A C      1 
ATOM   3703 O O      . PRO A 1 238 ? 18.49900  26.16600  24.90700 1.000 47.06518  ?  238 PRO A O      1 
ATOM   3704 C CB     . PRO A 1 238 ? 20.24000  24.41800  26.74800 1.000 49.25533  ?  238 PRO A CB     1 
ATOM   3705 C CG     . PRO A 1 238 ? 21.27800  23.36300  26.95300 1.000 44.54938  ?  238 PRO A CG     1 
ATOM   3706 C CD     . PRO A 1 238 ? 21.71700  22.94200  25.59300 1.000 44.75782  ?  238 PRO A CD     1 
ATOM   3707 H HA     . PRO A 1 238 ? 18.70900  23.68600  25.54000 1.000 56.78038  ?  238 PRO A HA     1 
ATOM   3708 H HB2    . PRO A 1 238 ? 20.64600  25.29800  26.71200 1.000 59.22416  ?  238 PRO A HB2    1 
ATOM   3709 H HB3    . PRO A 1 238 ? 19.57500  24.38800  27.45400 1.000 59.22416  ?  238 PRO A HB3    1 
ATOM   3710 H HG2    . PRO A 1 238 ? 22.02300  23.73100  27.45400 1.000 53.57703  ?  238 PRO A HG2    1 
ATOM   3711 H HG3    . PRO A 1 238 ? 20.89200  22.61500  27.43400 1.000 53.57703  ?  238 PRO A HG3    1 
ATOM   3712 H HD2    . PRO A 1 238 ? 22.42500  23.51600  25.26200 1.000 53.82716  ?  238 PRO A HD2    1 
ATOM   3713 H HD3    . PRO A 1 238 ? 22.01100  22.01800  25.59300 1.000 53.82716  ?  238 PRO A HD3    1 
ATOM   3714 N N      . ASP A 1 239 ? 20.20800  25.61000  23.56100 1.000 46.67639  ?  239 ASP A N      1 
ATOM   3715 C CA     . ASP A 1 239 ? 20.11500  26.83600  22.77300 1.000 54.98881  ?  239 ASP A CA     1 
ATOM   3716 C C      . ASP A 1 239 ? 19.38500  26.64400  21.45000 1.000 51.79320  ?  239 ASP A C      1 
ATOM   3717 O O      . ASP A 1 239 ? 19.34200  27.57800  20.64300 1.000 53.59786  ?  239 ASP A O      1 
ATOM   3718 C CB     . ASP A 1 239 ? 21.52300  27.39200  22.50400 1.000 58.67771  ?  239 ASP A CB     1 
ATOM   3719 C CG     . ASP A 1 239 ? 22.15900  27.96800  23.75100 1.000 63.71160  ?  239 ASP A CG     1 
ATOM   3720 O OD1    . ASP A 1 239 ? 21.41800  28.46700  24.62400 1.000 70.32648  -1 239 ASP A OD1    1 
ATOM   3721 O OD2    . ASP A 1 239 ? 23.39900  27.91900  23.85900 1.000 84.96331  ?  239 ASP A OD2    1 
ATOM   3722 H H      . ASP A 1 239 ? 20.82800  25.07300  23.30200 1.000 56.12944  ?  239 ASP A H      1 
ATOM   3723 H HA     . ASP A 1 239 ? 19.61800  27.48900  23.29100 1.000 66.10434  ?  239 ASP A HA     1 
ATOM   3724 H HB2    . ASP A 1 239 ? 22.09100  26.67700  22.17900 1.000 70.53102  ?  239 ASP A HB2    1 
ATOM   3725 H HB3    . ASP A 1 239 ? 21.46500  28.09800  21.84100 1.000 70.53102  ?  239 ASP A HB3    1 
ATOM   3726 N N      . THR A 1 240 ? 18.81600  25.46400  21.20600 1.000 44.65722  ?  240 THR A N      1 
ATOM   3727 C CA     . THR A 1 240 ? 18.16000  25.18700  19.93600 1.000 47.99087  ?  240 THR A CA     1 
ATOM   3728 C C      . THR A 1 240 ? 16.68500  25.58600  19.98200 1.000 41.21344  ?  240 THR A C      1 
ATOM   3729 O O      . THR A 1 240 ? 16.05900  25.65600  21.03500 1.000 44.46887  ?  240 THR A O      1 
ATOM   3730 C CB     . THR A 1 240 ? 18.29900  23.70000  19.56500 1.000 45.48359  ?  240 THR A CB     1 
ATOM   3731 O OG1    . THR A 1 240 ? 17.77300  22.87500  20.62300 1.000 43.18250  ?  240 THR A OG1    1 
ATOM   3732 C CG2    . THR A 1 240 ? 19.76400  23.35700  19.33400 1.000 44.02098  ?  240 THR A CG2    1 
ATOM   3733 H H      . THR A 1 240 ? 18.79900  24.80900  21.76300 1.000 53.70644  ?  240 THR A H      1 
ATOM   3734 H HA     . THR A 1 240 ? 18.58600  25.71100  19.23900 1.000 57.70682  ?  240 THR A HA     1 
ATOM   3735 H HB     . THR A 1 240 ? 17.80300  23.51900  18.75100 1.000 54.69808  ?  240 THR A HB     1 
ATOM   3736 H HG1    . THR A 1 240 ? 17.95800  22.06900  20.47800 1.000 51.93677  ?  240 THR A HG1    1 
ATOM   3737 H HG21   . THR A 1 240 ? 19.85600  22.41300  19.13300 1.000 52.94294  ?  240 THR A HG21   1 
ATOM   3738 H HG22   . THR A 1 240 ? 20.11200  23.87300  18.59000 1.000 52.94294  ?  240 THR A HG22   1 
ATOM   3739 H HG23   . THR A 1 240 ? 20.28100  23.56200  20.12800 1.000 52.94294  ?  240 THR A HG23   1 
ATOM   3740 N N      . ASP A 1 241 ? 16.13100  25.82600  18.79800 1.000 48.07056  ?  241 ASP A N      1 
ATOM   3741 C CA     . ASP A 1 241 ? 14.83200  26.47800  18.66500 1.000 48.89100  ?  241 ASP A CA     1 
ATOM   3742 C C      . ASP A 1 241 ? 13.71500  25.44000  18.59400 1.000 42.61174  ?  241 ASP A C      1 
ATOM   3743 O O      . ASP A 1 241 ? 13.64900  24.68400  17.61900 1.000 39.22840  ?  241 ASP A O      1 
ATOM   3744 C CB     . ASP A 1 241 ? 14.83000  27.34000  17.40600 1.000 48.52456  ?  241 ASP A CB     1 
ATOM   3745 C CG     . ASP A 1 241 ? 13.52500  28.07600  17.20300 1.000 46.18814  ?  241 ASP A CG     1 
ATOM   3746 O OD1    . ASP A 1 241 ? 12.56100  27.85800  17.98200 1.000 44.66475  ?  241 ASP A OD1    1 
ATOM   3747 O OD2    . ASP A 1 241 ? 13.46700  28.86800  16.25200 1.000 54.93936  -1 241 ASP A OD2    1 
ATOM   3748 H H      . ASP A 1 241 ? 16.49200  25.61700  18.04600 1.000 57.80244  ?  241 ASP A H      1 
ATOM   3749 H HA     . ASP A 1 241 ? 14.65800  27.03400  19.44100 1.000 58.78697  ?  241 ASP A HA     1 
ATOM   3750 H HB2    . ASP A 1 241 ? 15.53900  27.99900  17.47200 1.000 58.34724  ?  241 ASP A HB2    1 
ATOM   3751 H HB3    . ASP A 1 241 ? 14.97700  26.77200  16.63300 1.000 58.34724  ?  241 ASP A HB3    1 
ATOM   3752 N N      . PRO A 1 242 ? 12.80700  25.38800  19.57700 1.000 42.04725  ?  242 PRO A N      1 
ATOM   3753 C CA     . PRO A 1 242 ? 11.73100  24.38100  19.51600 1.000 43.01166  ?  242 PRO A CA     1 
ATOM   3754 C C      . PRO A 1 242 ? 10.63800  24.69700  18.50200 1.000 44.43054  ?  242 PRO A C      1 
ATOM   3755 O O      . PRO A 1 242 ? 9.86900   23.77900  18.15000 1.000 44.40079  ?  242 PRO A O      1 
ATOM   3756 C CB     . PRO A 1 242 ? 11.16900  24.37700  20.94100 1.000 41.67304  ?  242 PRO A CB     1 
ATOM   3757 C CG     . PRO A 1 242 ? 11.43100  25.77700  21.43900 1.000 41.15745  ?  242 PRO A CG     1 
ATOM   3758 C CD     . PRO A 1 242 ? 12.73200  26.20300  20.80900 1.000 40.57795  ?  242 PRO A CD     1 
ATOM   3759 H HA     . PRO A 1 242 ? 12.11200  23.51200  19.31400 1.000 51.73177  ?  242 PRO A HA     1 
ATOM   3760 H HB2    . PRO A 1 242 ? 10.21900  24.18200  20.92500 1.000 50.12541  ?  242 PRO A HB2    1 
ATOM   3761 H HB3    . PRO A 1 242 ? 11.63300  23.71900  21.48200 1.000 50.12541  ?  242 PRO A HB3    1 
ATOM   3762 H HG2    . PRO A 1 242 ? 10.70900  26.36300  21.16400 1.000 49.50671  ?  242 PRO A HG2    1 
ATOM   3763 H HG3    . PRO A 1 242 ? 11.50400  25.77200  22.40600 1.000 49.50671  ?  242 PRO A HG3    1 
ATOM   3764 H HD2    . PRO A 1 242 ? 12.71600  27.14900  20.59500 1.000 48.81131  ?  242 PRO A HD2    1 
ATOM   3765 H HD3    . PRO A 1 242 ? 13.47800  26.00800  21.39600 1.000 48.81131  ?  242 PRO A HD3    1 
ATOM   3766 N N      . SER A 1 243 ? 10.53400  25.94000  18.03300 1.000 42.55479  ?  243 SER A N      1 
ATOM   3767 C CA     . SER A 1 243 ? 9.50900   26.32500  17.06800 1.000 46.24382  ?  243 SER A CA     1 
ATOM   3768 C C      . SER A 1 243 ? 9.92900   26.08000  15.62100 1.000 45.22677  ?  243 SER A C      1 
ATOM   3769 O O      . SER A 1 243 ? 9.12400   26.31000  14.71000 1.000 44.57586  ?  243 SER A O      1 
ATOM   3770 C CB     . SER A 1 243 ? 9.14200   27.81100  17.25200 1.000 43.79768  ?  243 SER A CB     1 
ATOM   3771 O OG     . SER A 1 243 ? 10.19200  28.66800  16.81800 1.000 44.85748  ?  243 SER A OG     1 
ATOM   3772 H H      . SER A 1 243 ? 11.05400  26.58600  18.26200 1.000 51.18351  ?  243 SER A H      1 
ATOM   3773 H HA     . SER A 1 243 ? 8.71400   25.79700  17.23900 1.000 55.61035  ?  243 SER A HA     1 
ATOM   3774 H HB2    . SER A 1 243 ? 8.34600   28.00300  16.73100 1.000 52.67499  ?  243 SER A HB2    1 
ATOM   3775 H HB3    . SER A 1 243 ? 8.97100   27.97700  18.19200 1.000 52.67499  ?  243 SER A HB3    1 
ATOM   3776 H HG     . SER A 1 243 ? 10.20700  29.36500  17.28600 1.000 53.94674  ?  243 SER A HG     1 
ATOM   3777 N N      . ALA A 1 244 ? 11.16500  25.62600  15.38900 1.000 43.29338  ?  244 ALA A N      1 
ATOM   3778 C CA     . ALA A 1 244 ? 11.64000  25.33700  14.03900 1.000 43.16456  ?  244 ALA A CA     1 
ATOM   3779 C C      . ALA A 1 244 ? 11.05900  23.99700  13.58400 1.000 49.61027  ?  244 ALA A C      1 
ATOM   3780 O O      . ALA A 1 244 ? 11.39100  22.94600  14.15200 1.000 44.71091  ?  244 ALA A O      1 
ATOM   3781 C CB     . ALA A 1 244 ? 13.15900  25.31400  14.00500 1.000 51.37209  ?  244 ALA A CB     1 
ATOM   3782 H H      . ALA A 1 244 ? 11.74800  25.47800  16.00300 1.000 52.06983  ?  244 ALA A H      1 
ATOM   3783 H HA     . ALA A 1 244 ? 11.33200  26.02800  13.43200 1.000 51.91524  ?  244 ALA A HA     1 
ATOM   3784 H HB1    . ALA A 1 244 ? 13.45200  25.10600  13.10500 1.000 61.76428  ?  244 ALA A HB1    1 
ATOM   3785 H HB2    . ALA A 1 244 ? 13.49300  26.18600  14.26900 1.000 61.76428  ?  244 ALA A HB2    1 
ATOM   3786 H HB3    . ALA A 1 244 ? 13.47800  24.63700  14.62200 1.000 61.76428  ?  244 ALA A HB3    1 
ATOM   3787 N N      . TRP A 1 245 ? 10.20600  24.03300  12.56100 1.000 47.57972  ?  245 TRP A N      1 
ATOM   3788 C CA     . TRP A 1 245 ? 9.58000   22.84300  12.00700 1.000 48.04297  ?  245 TRP A CA     1 
ATOM   3789 C C      . TRP A 1 245 ? 9.94000   22.58600  10.55100 1.000 50.60158  ?  245 TRP A C      1 
ATOM   3790 O O      . TRP A 1 245 ? 10.11100  21.42400  10.15900 1.000 48.60605  ?  245 TRP A O      1 
ATOM   3791 C CB     . TRP A 1 245 ? 8.04400   22.94400  12.13600 1.000 44.55720  ?  245 TRP A CB     1 
ATOM   3792 C CG     . TRP A 1 245 ? 7.44800   24.11700  11.39900 1.000 52.13255  ?  245 TRP A CG     1 
ATOM   3793 C CD1    . TRP A 1 245 ? 7.31400   25.39100  11.86000 1.000 51.56900  ?  245 TRP A CD1    1 
ATOM   3794 C CD2    . TRP A 1 245 ? 6.91900   24.11100  10.07100 1.000 52.63298  ?  245 TRP A CD2    1 
ATOM   3795 N NE1    . TRP A 1 245 ? 6.73500   26.18500  10.89900 1.000 53.71516  ?  245 TRP A NE1    1 
ATOM   3796 C CE2    . TRP A 1 245 ? 6.48200   25.41700  9.79000  1.000 54.62968  ?  245 TRP A CE2    1 
ATOM   3797 C CE3    . TRP A 1 245 ? 6.77900   23.12800  9.08700  1.000 56.18736  ?  245 TRP A CE3    1 
ATOM   3798 C CZ2    . TRP A 1 245 ? 5.91000   25.76500  8.57200  1.000 62.00469  ?  245 TRP A CZ2    1 
ATOM   3799 C CZ3    . TRP A 1 245 ? 6.20900   23.47800  7.87500  1.000 59.68747  ?  245 TRP A CZ3    1 
ATOM   3800 C CH2    . TRP A 1 245 ? 5.78200   24.78000  7.62900  1.000 59.03681  ?  245 TRP A CH2    1 
ATOM   3801 H H      . TRP A 1 245 ? 9.97000   24.75800  12.16300 1.000 57.21343  ?  245 TRP A H      1 
ATOM   3802 H HA     . TRP A 1 245 ? 9.87700   22.07600  12.52000 1.000 57.76934  ?  245 TRP A HA     1 
ATOM   3803 H HB2    . TRP A 1 245 ? 7.64700   22.13600  11.77600 1.000 53.58641  ?  245 TRP A HB2    1 
ATOM   3804 H HB3    . TRP A 1 245 ? 7.81600   23.03600  13.07400 1.000 53.58641  ?  245 TRP A HB3    1 
ATOM   3805 H HD1    . TRP A 1 245 ? 7.57600   25.68200  12.70300 1.000 62.00057  ?  245 TRP A HD1    1 
ATOM   3806 H HE1    . TRP A 1 245 ? 6.56000   27.02300  10.97900 1.000 64.57596  ?  245 TRP A HE1    1 
ATOM   3807 H HE3    . TRP A 1 245 ? 7.06400   22.25600  9.24300  1.000 67.54260  ?  245 TRP A HE3    1 
ATOM   3808 H HZ2    . TRP A 1 245 ? 5.62500   26.63400  8.40400  1.000 74.52340  ?  245 TRP A HZ2    1 
ATOM   3809 H HZ3    . TRP A 1 245 ? 6.10900   22.83200  7.21300  1.000 71.74274  ?  245 TRP A HZ3    1 
ATOM   3810 H HH2    . TRP A 1 245 ? 5.40200   24.98500  6.80600  1.000 70.96194  ?  245 TRP A HH2    1 
ATOM   3811 N N      . GLU A 1 246 ? 10.05300  23.63600  9.72900  1.000 53.63770  ?  246 GLU A N      1 
ATOM   3812 C CA     . GLU A 1 246 ? 10.44800  23.44100  8.33900  1.000 58.38412  ?  246 GLU A CA     1 
ATOM   3813 C C      . GLU A 1 246 ? 11.78300  22.72100  8.26300  1.000 55.08412  ?  246 GLU A C      1 
ATOM   3814 O O      . GLU A 1 246 ? 11.94000  21.74800  7.51400  1.000 56.59146  ?  246 GLU A O      1 
ATOM   3815 C CB     . GLU A 1 246 ? 10.52600  24.78500  7.61200  1.000 63.10530  ?  246 GLU A CB     1 
ATOM   3816 C CG     . GLU A 1 246 ? 9.34800   25.71000  7.85500  1.000 72.12664  ?  246 GLU A CG     1 
ATOM   3817 C CD     . GLU A 1 246 ? 9.45500   27.01000  7.07400  1.000 77.50347  ?  246 GLU A CD     1 
ATOM   3818 O OE1    . GLU A 1 246 ? 10.21200  27.04700  6.08000  1.000 84.66649  ?  246 GLU A OE1    1 
ATOM   3819 O OE2    . GLU A 1 246 ? 8.78100   27.99200  7.45700  1.000 78.10155  -1 246 GLU A OE2    1 
ATOM   3820 H H      . GLU A 1 246 ? 9.90700   24.45400  9.95200  1.000 64.48301  ?  246 GLU A H      1 
ATOM   3821 H HA     . GLU A 1 246 ? 9.77400   22.90300  7.89500  1.000 70.17872  ?  246 GLU A HA     1 
ATOM   3822 H HB2    . GLU A 1 246 ? 11.32600  25.24800  7.90600  1.000 75.84413  ?  246 GLU A HB2    1 
ATOM   3823 H HB3    . GLU A 1 246 ? 10.57200  24.61700  6.65800  1.000 75.84413  ?  246 GLU A HB3    1 
ATOM   3824 H HG2    . GLU A 1 246 ? 8.53200   25.26200  7.58300  1.000 86.66974  ?  246 GLU A HG2    1 
ATOM   3825 H HG3    . GLU A 1 246 ? 9.30800   25.92900  8.79900  1.000 86.66974  ?  246 GLU A HG3    1 
ATOM   3826 N N      . LYS A 1 247 ? 12.75600  23.18300  9.04600  1.000 53.62957  ?  247 LYS A N      1 
ATOM   3827 C CA     . LYS A 1 247 ? 14.00800  22.47300  9.27400  1.000 54.92274  ?  247 LYS A CA     1 
ATOM   3828 C C      . LYS A 1 247 ? 14.20300  22.39700  10.78400 1.000 50.91066  ?  247 LYS A C      1 
ATOM   3829 O O      . LYS A 1 247 ? 14.65400  23.37400  11.39700 1.000 44.33956  ?  247 LYS A O      1 
ATOM   3830 C CB     . LYS A 1 247 ? 15.18900  23.17400  8.60100  1.000 70.59151  ?  247 LYS A CB     1 
ATOM   3831 C CG     . LYS A 1 247 ? 16.48800  22.36900  8.67500  1.000 73.92067  ?  247 LYS A CG     1 
ATOM   3832 C CD     . LYS A 1 247 ? 17.20900  22.31700  7.33100  1.000 92.26673  ?  247 LYS A CD     1 
ATOM   3833 C CE     . LYS A 1 247 ? 18.69500  22.60400  7.48800  1.000 80.37345  ?  247 LYS A CE     1 
ATOM   3834 N NZ     . LYS A 1 247 ? 19.39000  22.66400  6.17200  1.000 87.86462  ?  247 LYS A NZ     1 
ATOM   3835 H H      . LYS A 1 247 ? 12.71100  23.93100  9.46800  1.000 64.47326  ?  247 LYS A H      1 
ATOM   3836 H HA     . LYS A 1 247 ? 13.96100  21.57700  8.90300  1.000 66.02506  ?  247 LYS A HA     1 
ATOM   3837 H HB2    . LYS A 1 247 ? 14.97800  23.31600  7.66500  1.000 84.82758  ?  247 LYS A HB2    1 
ATOM   3838 H HB3    . LYS A 1 247 ? 15.34000  24.02500  9.04000  1.000 84.82758  ?  247 LYS A HB3    1 
ATOM   3839 H HG2    . LYS A 1 247 ? 17.08200  22.78100  9.32100  1.000 88.82258  ?  247 LYS A HG2    1 
ATOM   3840 H HG3    . LYS A 1 247 ? 16.28400  21.45900  8.94400  1.000 88.82258  ?  247 LYS A HG3    1 
ATOM   3841 H HD2    . LYS A 1 247 ? 17.10800  21.43200  6.94500  1.000 110.83785 ?  247 LYS A HD2    1 
ATOM   3842 H HD3    . LYS A 1 247 ? 16.83000  22.98300  6.73600  1.000 110.83785 ?  247 LYS A HD3    1 
ATOM   3843 H HE2    . LYS A 1 247 ? 18.81000  23.45900  7.93100  1.000 96.56591  ?  247 LYS A HE2    1 
ATOM   3844 H HE3    . LYS A 1 247 ? 19.10300  21.89900  8.01500  1.000 96.56591  ?  247 LYS A HE3    1 
ATOM   3845 H HZ1    . LYS A 1 247 ? 20.25300  22.84800  6.29100  1.000 105.55531 ?  247 LYS A HZ1    1 
ATOM   3846 H HZ2    . LYS A 1 247 ? 19.31800  21.88100  5.75400  1.000 105.55531 ?  247 LYS A HZ2    1 
ATOM   3847 H HZ3    . LYS A 1 247 ? 19.02700  23.29700  5.66400  1.000 105.55531 ?  247 LYS A HZ3    1 
ATOM   3848 N N      . PRO A 1 248 ? 13.87200  21.26900  11.41500 1.000 47.51292  ?  248 PRO A N      1 
ATOM   3849 C CA     . PRO A 1 248 ? 14.04200  21.16400  12.86500 1.000 45.82140  ?  248 PRO A CA     1 
ATOM   3850 C C      . PRO A 1 248 ? 15.45300  21.56600  13.28800 1.000 45.68679  ?  248 PRO A C      1 
ATOM   3851 O O      . PRO A 1 248 ? 16.40400  21.44400  12.52200 1.000 41.09316  ?  248 PRO A O      1 
ATOM   3852 C CB     . PRO A 1 248 ? 13.77000  19.67600  13.14900 1.000 44.89332  ?  248 PRO A CB     1 
ATOM   3853 C CG     . PRO A 1 248 ? 12.87300  19.25000  12.04600 1.000 52.04252  ?  248 PRO A CG     1 
ATOM   3854 C CD     . PRO A 1 248 ? 13.31800  20.03300  10.83300 1.000 50.73810  ?  248 PRO A CD     1 
ATOM   3855 H HA     . PRO A 1 248 ? 13.39100  21.71300  13.33000 1.000 55.10345  ?  248 PRO A HA     1 
ATOM   3856 H HB2    . PRO A 1 248 ? 14.60200  19.17700  13.13500 1.000 53.98975  ?  248 PRO A HB2    1 
ATOM   3857 H HB3    . PRO A 1 248 ? 13.33700  19.57500  14.01100 1.000 53.98975  ?  248 PRO A HB3    1 
ATOM   3858 H HG2    . PRO A 1 248 ? 12.96800  18.29700  11.89400 1.000 62.56880  ?  248 PRO A HG2    1 
ATOM   3859 H HG3    . PRO A 1 248 ? 11.95300  19.46000  12.27200 1.000 62.56880  ?  248 PRO A HG3    1 
ATOM   3860 H HD2    . PRO A 1 248 ? 13.99800  19.54800  10.34000 1.000 61.00349  ?  248 PRO A HD2    1 
ATOM   3861 H HD3    . PRO A 1 248 ? 12.56600  20.23100  10.25400 1.000 61.00349  ?  248 PRO A HD3    1 
ATOM   3862 N N      . ALA A 1 249 ? 15.56400  22.05400  14.51800 1.000 42.55438  ?  249 ALA A N      1 
ATOM   3863 C CA     . ALA A 1 249 ? 16.82500  22.55600  15.03900 1.000 40.06329  ?  249 ALA A CA     1 
ATOM   3864 C C      . ALA A 1 249 ? 17.73600  21.45500  15.57100 1.000 42.68171  ?  249 ALA A C      1 
ATOM   3865 O O      . ALA A 1 249 ? 18.87900  21.74600  15.93300 1.000 43.05297  ?  249 ALA A O      1 
ATOM   3866 C CB     . ALA A 1 249 ? 16.56000  23.57100  16.15200 1.000 40.20761  ?  249 ALA A CB     1 
ATOM   3867 H H      . ALA A 1 249 ? 14.91300  22.10600  15.07700 1.000 51.18303  ?  249 ALA A H      1 
ATOM   3868 H HA     . ALA A 1 249 ? 17.29600  23.00600  14.32000 1.000 48.19372  ?  249 ALA A HA     1 
ATOM   3869 H HB1    . ALA A 1 249 ? 17.40800  23.91700  16.47300 1.000 48.36690  ?  249 ALA A HB1    1 
ATOM   3870 H HB2    . ALA A 1 249 ? 16.02000  24.29500  15.79800 1.000 48.36690  ?  249 ALA A HB2    1 
ATOM   3871 H HB3    . ALA A 1 249 ? 16.08800  23.13000  16.87500 1.000 48.36690  ?  249 ALA A HB3    1 
ATOM   3872 N N      . THR A 1 250 ? 17.26400  20.22200  15.64100 1.000 41.24011  ?  250 THR A N      1 
ATOM   3873 C CA     . THR A 1 250 ? 18.06700  19.06300  16.05600 1.000 43.00797  ?  250 THR A CA     1 
ATOM   3874 C C      . THR A 1 250 ? 18.05000  18.03500  14.93000 1.000 36.75165  ?  250 THR A C      1 
ATOM   3875 O O      . THR A 1 250 ? 17.48500  18.27200  13.86500 1.000 38.95183  ?  250 THR A O      1 
ATOM   3876 C CB     . THR A 1 250 ? 17.55200  18.48000  17.37800 1.000 42.76978  ?  250 THR A CB     1 
ATOM   3877 O OG1    . THR A 1 250 ? 16.13400  18.26000  17.30700 1.000 40.60387  ?  250 THR A OG1    1 
ATOM   3878 C CG2    . THR A 1 250 ? 17.84900  19.44000  18.52500 1.000 40.11484  ?  250 THR A CG2    1 
ATOM   3879 H H      . THR A 1 250 ? 16.45200  20.01500  15.44700 1.000 49.60590  ?  250 THR A H      1 
ATOM   3880 H HA     . THR A 1 250 ? 18.98700  19.33400  16.20600 1.000 51.72733  ?  250 THR A HA     1 
ATOM   3881 H HB     . THR A 1 250 ? 17.99500  17.63400  17.54800 1.000 51.44151  ?  250 THR A HB     1 
ATOM   3882 H HG1    . THR A 1 250 ? 15.85200  17.96600  18.04200 1.000 48.84241  ?  250 THR A HG1    1 
ATOM   3883 H HG21   . THR A 1 250 ? 17.53600  19.06400  19.36200 1.000 48.25558  ?  250 THR A HG21   1 
ATOM   3884 H HG22   . THR A 1 250 ? 18.80500  19.59700  18.58700 1.000 48.25558  ?  250 THR A HG22   1 
ATOM   3885 H HG23   . THR A 1 250 ? 17.40100  20.28700  18.37300 1.000 48.25558  ?  250 THR A HG23   1 
ATOM   3886 N N      . THR A 1 251 ? 18.66400  16.87200  15.18600 1.000 42.62416  ?  251 THR A N      1 
ATOM   3887 C CA     . THR A 1 251 ? 18.90600  15.90300  14.11800 1.000 39.61468  ?  251 THR A CA     1 
ATOM   3888 C C      . THR A 1 251 ? 17.66700  15.10200  13.73300 1.000 42.63405  ?  251 THR A C      1 
ATOM   3889 O O      . THR A 1 251 ? 17.57900  14.62700  12.60100 1.000 41.37128  ?  251 THR A O      1 
ATOM   3890 C CB     . THR A 1 251 ? 20.01800  14.91800  14.53100 1.000 43.59069  ?  251 THR A CB     1 
ATOM   3891 O OG1    . THR A 1 251 ? 19.54600  14.09300  15.60300 1.000 40.35319  ?  251 THR A OG1    1 
ATOM   3892 C CG2    . THR A 1 251 ? 21.28500  15.67200  14.95900 1.000 41.00944  ?  251 THR A CG2    1 
ATOM   3893 H H      . THR A 1 251 ? 18.94500  16.62700  15.96000 1.000 51.26676  ?  251 THR A H      1 
ATOM   3894 H HA     . THR A 1 251 ? 19.19400  16.40400  13.33900 1.000 47.65539  ?  251 THR A HA     1 
ATOM   3895 H HB     . THR A 1 251 ? 20.25500  14.35600  13.77700 1.000 52.42660  ?  251 THR A HB     1 
ATOM   3896 H HG1    . THR A 1 251 ? 20.11600  13.50200  15.78300 1.000 48.54159  ?  251 THR A HG1    1 
ATOM   3897 H HG21   . THR A 1 251 ? 21.99700  15.04200  15.15200 1.000 49.32910  ?  251 THR A HG21   1 
ATOM   3898 H HG22   . THR A 1 251 ? 21.57300  16.26600  14.24900 1.000 49.32910  ?  251 THR A HG22   1 
ATOM   3899 H HG23   . THR A 1 251 ? 21.10500  16.19700  15.75500 1.000 49.32910  ?  251 THR A HG23   1 
ATOM   3900 N N      . VAL A 1 252 ? 16.72100  14.92900  14.65200 1.000 39.81933  ?  252 VAL A N      1 
ATOM   3901 C CA     . VAL A 1 252 ? 15.58400  14.04100  14.43800 1.000 42.26855  ?  252 VAL A CA     1 
ATOM   3902 C C      . VAL A 1 252 ? 16.07900  12.65000  14.03900 1.000 42.51267  ?  252 VAL A C      1 
ATOM   3903 O O      . VAL A 1 252 ? 15.51500  11.99800  13.14100 1.000 41.10343  ?  252 VAL A O      1 
ATOM   3904 C CB     . VAL A 1 252 ? 14.60700  14.59200  13.37300 1.000 43.61046  ?  252 VAL A CB     1 
ATOM   3905 C CG1    . VAL A 1 252 ? 13.26900  13.88400  13.48100 1.000 45.49868  ?  252 VAL A CG1    1 
ATOM   3906 C CG2    . VAL A 1 252 ? 14.43100  16.10000  13.51500 1.000 42.78660  ?  252 VAL A CG2    1 
ATOM   3907 H H      . VAL A 1 252 ? 16.71500  15.32100  15.41800 1.000 47.90096  ?  252 VAL A H      1 
ATOM   3908 H HA     . VAL A 1 252 ? 15.10500  13.96800  15.27800 1.000 50.84003  ?  252 VAL A HA     1 
ATOM   3909 H HB     . VAL A 1 252 ? 14.97800  14.42400  12.49200 1.000 52.45032  ?  252 VAL A HB     1 
ATOM   3910 H HG11   . VAL A 1 252 ? 12.60000  14.39800  13.00200 1.000 54.71618  ?  252 VAL A HG11   1 
ATOM   3911 H HG12   . VAL A 1 252 ? 13.34700  12.99900  13.09300 1.000 54.71618  ?  252 VAL A HG12   1 
ATOM   3912 H HG13   . VAL A 1 252 ? 13.02400  13.81400  14.41700 1.000 54.71618  ?  252 VAL A HG13   1 
ATOM   3913 H HG21   . VAL A 1 252 ? 13.70000  16.38800  12.94600 1.000 51.46170  ?  252 VAL A HG21   1 
ATOM   3914 H HG22   . VAL A 1 252 ? 14.23100  16.30800  14.44100 1.000 51.46170  ?  252 VAL A HG22   1 
ATOM   3915 H HG23   . VAL A 1 252 ? 15.25300  16.54000  13.24700 1.000 51.46170  ?  252 VAL A HG23   1 
ATOM   3916 N N      . LEU A 1 253 ? 17.12500  12.18400  14.69400 1.000 40.45907  ?  253 LEU A N      1 
ATOM   3917 C CA     . LEU A 1 253 ? 17.57500  10.80600  14.52900 1.000 42.25623  ?  253 LEU A CA     1 
ATOM   3918 C C      . LEU A 1 253 ? 16.98600  9.86900   15.56700 1.000 40.06003  ?  253 LEU A C      1 
ATOM   3919 O O      . LEU A 1 253 ? 17.29500  8.66400   15.53600 1.000 40.29077  ?  253 LEU A O      1 
ATOM   3920 C CB     . LEU A 1 253 ? 19.10600  10.73700  14.57800 1.000 34.33596  ?  253 LEU A CB     1 
ATOM   3921 C CG     . LEU A 1 253 ? 19.78800  11.23300  13.28600 1.000 41.78715  ?  253 LEU A CG     1 
ATOM   3922 C CD1    . LEU A 1 253 ? 21.25900  11.50400  13.51900 1.000 45.02209  ?  253 LEU A CD1    1 
ATOM   3923 C CD2    . LEU A 1 253 ? 19.58500  10.23500  12.15600 1.000 43.83044  ?  253 LEU A CD2    1 
ATOM   3924 H H      . LEU A 1 253 ? 17.59800  12.64600  15.24400 1.000 48.66866  ?  253 LEU A H      1 
ATOM   3925 H HA     . LEU A 1 253 ? 17.29600  10.49200  13.65400 1.000 50.82525  ?  253 LEU A HA     1 
ATOM   3926 H HB2    . LEU A 1 253 ? 19.41900  11.29000  15.31100 1.000 41.32092  ?  253 LEU A HB2    1 
ATOM   3927 H HB3    . LEU A 1 253 ? 19.37200  9.81500   14.72000 1.000 41.32092  ?  253 LEU A HB3    1 
ATOM   3928 H HG     . LEU A 1 253 ? 19.37800  12.07000  13.01700 1.000 50.26235  ?  253 LEU A HG     1 
ATOM   3929 H HD11   . LEU A 1 253 ? 21.65900  11.80900  12.69000 1.000 54.14428  ?  253 LEU A HD11   1 
ATOM   3930 H HD12   . LEU A 1 253 ? 21.34900  12.18800  14.20100 1.000 54.14428  ?  253 LEU A HD12   1 
ATOM   3931 H HD13   . LEU A 1 253 ? 21.68800  10.68500  13.81200 1.000 54.14428  ?  253 LEU A HD13   1 
ATOM   3932 H HD21   . LEU A 1 253 ? 20.28000  10.36400  11.49200 1.000 52.71430  ?  253 LEU A HD21   1 
ATOM   3933 H HD22   . LEU A 1 253 ? 19.63400  9.33600   12.51600 1.000 52.71430  ?  253 LEU A HD22   1 
ATOM   3934 H HD23   . LEU A 1 253 ? 18.71400  10.38400  11.75600 1.000 52.71430  ?  253 LEU A HD23   1 
ATOM   3935 N N      . SER A 1 254 ? 16.14600  10.38800  16.47400 1.000 37.69051  ?  254 SER A N      1 
ATOM   3936 C CA     . SER A 1 254 ? 15.63200  9.56200   17.57500 1.000 37.62848  ?  254 SER A CA     1 
ATOM   3937 C C      . SER A 1 254 ? 14.82700  8.35800   17.10600 1.000 42.06349  ?  254 SER A C      1 
ATOM   3938 O O      . SER A 1 254 ? 15.01900  7.26700   17.66000 1.000 39.80508  ?  254 SER A O      1 
ATOM   3939 C CB     . SER A 1 254 ? 14.81600  10.43000  18.53100 1.000 37.86201  ?  254 SER A CB     1 
ATOM   3940 O OG     . SER A 1 254 ? 13.87400  11.25100  17.85700 1.000 40.13828  ?  254 SER A OG     1 
ATOM   3941 H H      . SER A 1 254 ? 15.86300  11.20000  16.47400 1.000 45.34638  ?  254 SER A H      1 
ATOM   3942 H HA     . SER A 1 254 ? 16.40500  9.22000   18.05100 1.000 45.27195  ?  254 SER A HA     1 
ATOM   3943 H HB2    . SER A 1 254 ? 14.33600  9.84800   19.14200 1.000 45.55218  ?  254 SER A HB2    1 
ATOM   3944 H HB3    . SER A 1 254 ? 15.42500  11.00000  19.02600 1.000 45.55218  ?  254 SER A HB3    1 
ATOM   3945 H HG     . SER A 1 254 ? 13.36100  11.61600  18.41300 1.000 48.28371  ?  254 SER A HG     1 
ATOM   3946 N N      . PRO A 1 255 ? 13.89600  8.47100   16.15300 1.000 46.30997  ?  255 PRO A N      1 
ATOM   3947 C CA     . PRO A 1 255 ? 13.18900  7.25200   15.71600 1.000 37.57850  ?  255 PRO A CA     1 
ATOM   3948 C C      . PRO A 1 255 ? 14.13600  6.21800   15.14800 1.000 41.65276  ?  255 PRO A C      1 
ATOM   3949 O O      . PRO A 1 255 ? 13.92700  4.99900   15.32600 1.000 41.54180  ?  255 PRO A O      1 
ATOM   3950 C CB     . PRO A 1 255 ? 12.19900  7.74800   14.64800 1.000 37.68385  ?  255 PRO A CB     1 
ATOM   3951 C CG     . PRO A 1 255 ? 12.49600  9.17400   14.40400 1.000 42.72224  ?  255 PRO A CG     1 
ATOM   3952 C CD     . PRO A 1 255 ? 13.54500  9.66300   15.35900 1.000 37.98829  ?  255 PRO A CD     1 
ATOM   3953 H HA     . PRO A 1 255 ? 12.68400  6.88500   16.45900 1.000 45.21196  ?  255 PRO A HA     1 
ATOM   3954 H HB2    . PRO A 1 255 ? 12.31900  7.23300   13.83500 1.000 45.33839  ?  255 PRO A HB2    1 
ATOM   3955 H HB3    . PRO A 1 255 ? 11.29200  7.64300   14.97700 1.000 45.33839  ?  255 PRO A HB3    1 
ATOM   3956 H HG2    . PRO A 1 255 ? 12.81400  9.27100   13.49300 1.000 51.38446  ?  255 PRO A HG2    1 
ATOM   3957 H HG3    . PRO A 1 255 ? 11.68000  9.68400   14.52600 1.000 51.38446  ?  255 PRO A HG3    1 
ATOM   3958 H HD2    . PRO A 1 255 ? 14.31900  9.99300   14.87700 1.000 45.70372  ?  255 PRO A HD2    1 
ATOM   3959 H HD3    . PRO A 1 255 ? 13.18800  10.36100  15.93100 1.000 45.70372  ?  255 PRO A HD3    1 
ATOM   3960 N N      . TYR A 1 256 ? 15.17600  6.66500   14.44700 1.000 39.09126  ?  256 TYR A N      1 
ATOM   3961 C CA     . TYR A 1 256 ? 16.10700  5.72000   13.81800 1.000 38.10857  ?  256 TYR A CA     1 
ATOM   3962 C C      . TYR A 1 256 ? 16.96100  5.00900   14.84900 1.000 35.52590  ?  256 TYR A C      1 
ATOM   3963 O O      . TYR A 1 256 ? 17.28000  3.82800   14.69400 1.000 37.49035  ?  256 TYR A O      1 
ATOM   3964 C CB     . TYR A 1 256 ? 16.95800  6.47300   12.79700 1.000 33.73675  ?  256 TYR A CB     1 
ATOM   3965 C CG     . TYR A 1 256 ? 16.10000  7.17000   11.76400 1.000 38.70755  ?  256 TYR A CG     1 
ATOM   3966 C CD1    . TYR A 1 256 ? 15.56600  6.46600   10.68000 1.000 38.00802  ?  256 TYR A CD1    1 
ATOM   3967 C CD2    . TYR A 1 256 ? 15.75100  8.51200   11.91000 1.000 37.70830  ?  256 TYR A CD2    1 
ATOM   3968 C CE1    . TYR A 1 256 ? 14.76400  7.09700   9.75900  1.000 37.33631  ?  256 TYR A CE1    1 
ATOM   3969 C CE2    . TYR A 1 256 ? 14.94800  9.14400   10.98800 1.000 38.74066  ?  256 TYR A CE2    1 
ATOM   3970 C CZ     . TYR A 1 256 ? 14.44600  8.43200   9.91800  1.000 40.86425  ?  256 TYR A CZ     1 
ATOM   3971 O OH     . TYR A 1 256 ? 13.62900  9.07000   8.99400  1.000 41.33339  ?  256 TYR A OH     1 
ATOM   3972 H H      . TYR A 1 256 ? 15.36500  7.49400   14.32000 1.000 47.02728  ?  256 TYR A H      1 
ATOM   3973 H HA     . TYR A 1 256 ? 15.61000  5.03100   13.34900 1.000 45.84805  ?  256 TYR A HA     1 
ATOM   3974 H HB2    . TYR A 1 256 ? 17.49000  7.14300   13.25500 1.000 40.60187  ?  256 TYR A HB2    1 
ATOM   3975 H HB3    . TYR A 1 256 ? 17.53900  5.84600   12.33800 1.000 40.60187  ?  256 TYR A HB3    1 
ATOM   3976 H HD1    . TYR A 1 256 ? 15.75500  5.56100   10.58200 1.000 45.72739  ?  256 TYR A HD1    1 
ATOM   3977 H HD2    . TYR A 1 256 ? 16.06700  8.98800   12.64300 1.000 45.36773  ?  256 TYR A HD2    1 
ATOM   3978 H HE1    . TYR A 1 256 ? 14.43600  6.62500   9.02800  1.000 44.92134  ?  256 TYR A HE1    1 
ATOM   3979 H HE2    . TYR A 1 256 ? 14.74400  10.04600  11.08600 1.000 46.60656  ?  256 TYR A HE2    1 
ATOM   3980 H HH     . TYR A 1 256 ? 13.45100  9.84700   9.25600  1.000 49.71784  ?  256 TYR A HH     1 
ATOM   3981 N N      . LEU A 1 257 ? 17.34700  5.71000   15.92400 1.000 39.38345  ?  257 LEU A N      1 
ATOM   3982 C CA     . LEU A 1 257 ? 18.11900  5.05600   16.97800 1.000 41.82611  ?  257 LEU A CA     1 
ATOM   3983 C C      . LEU A 1 257 ? 17.22500  4.13300   17.80900 1.000 40.82367  ?  257 LEU A C      1 
ATOM   3984 O O      . LEU A 1 257 ? 17.70900  3.11600   18.32000 1.000 44.74985  ?  257 LEU A O      1 
ATOM   3985 C CB     . LEU A 1 257 ? 18.78000  6.09500   17.88500 1.000 39.67943  ?  257 LEU A CB     1 
ATOM   3986 C CG     . LEU A 1 257 ? 19.92100  6.89200   17.23300 1.000 45.98745  ?  257 LEU A CG     1 
ATOM   3987 C CD1    . LEU A 1 257 ? 20.26600  8.10500   18.06400 1.000 43.93360  ?  257 LEU A CD1    1 
ATOM   3988 C CD2    . LEU A 1 257 ? 21.15300  5.99700   17.04000 1.000 43.07425  ?  257 LEU A CD2    1 
ATOM   3989 H H      . LEU A 1 257 ? 17.17700  6.54200   16.06000 1.000 47.37790  ?  257 LEU A H      1 
ATOM   3990 H HA     . LEU A 1 257 ? 18.82600  4.53200   16.57100 1.000 50.30910  ?  257 LEU A HA     1 
ATOM   3991 H HB2    . LEU A 1 257 ? 18.10400  6.73100   18.16600 1.000 47.73308  ?  257 LEU A HB2    1 
ATOM   3992 H HB3    . LEU A 1 257 ? 19.14800  5.63800   18.65700 1.000 47.73308  ?  257 LEU A HB3    1 
ATOM   3993 H HG     . LEU A 1 257 ? 19.63300  7.20300   16.36100 1.000 55.30271  ?  257 LEU A HG     1 
ATOM   3994 H HD11   . LEU A 1 257 ? 20.98400  8.59100   17.62900 1.000 52.83809  ?  257 LEU A HD11   1 
ATOM   3995 H HD12   . LEU A 1 257 ? 19.48200  8.67000   18.13800 1.000 52.83809  ?  257 LEU A HD12   1 
ATOM   3996 H HD13   . LEU A 1 257 ? 20.54900  7.81400   18.94500 1.000 52.83809  ?  257 LEU A HD13   1 
ATOM   3997 H HD21   . LEU A 1 257 ? 21.88200  6.53400   16.69200 1.000 51.80687  ?  257 LEU A HD21   1 
ATOM   3998 H HD22   . LEU A 1 257 ? 21.40300  5.61500   17.89600 1.000 51.80687  ?  257 LEU A HD22   1 
ATOM   3999 H HD23   . LEU A 1 257 ? 20.93400  5.28900   16.41400 1.000 51.80687  ?  257 LEU A HD23   1 
ATOM   4000 N N      . LYS A 1 258 ? 15.94200  4.46200   17.93400 1.000 32.58384  ?  258 LYS A N      1 
ATOM   4001 C CA     . LYS A 1 258 ? 15.03800  3.64000   18.72800 1.000 40.56121  ?  258 LYS A CA     1 
ATOM   4002 C C      . LYS A 1 258 ? 14.87000  2.25400   18.11000 1.000 39.99420  ?  258 LYS A C      1 
ATOM   4003 O O      . LYS A 1 258 ? 14.95000  1.23700   18.80900 1.000 40.39400  ?  258 LYS A O      1 
ATOM   4004 C CB     . LYS A 1 258 ? 13.68800  4.34500   18.85800 1.000 38.31275  ?  258 LYS A CB     1 
ATOM   4005 C CG     . LYS A 1 258 ? 12.58500  3.47600   19.50200 1.000 39.91905  ?  258 LYS A CG     1 
ATOM   4006 C CD     . LYS A 1 258 ? 11.73900  2.77800   18.45300 1.000 42.04880  ?  258 LYS A CD     1 
ATOM   4007 C CE     . LYS A 1 258 ? 10.43500  2.26700   19.03100 1.000 46.10778  ?  258 LYS A CE     1 
ATOM   4008 N NZ     . LYS A 1 258 ? 10.66400  1.44400   20.24300 1.000 44.98139  ?  258 LYS A NZ     1 
ATOM   4009 H H      . LYS A 1 258 ? 15.57300  5.14900   17.57100 1.000 39.21837  ?  258 LYS A H      1 
ATOM   4010 H HA     . LYS A 1 258 ? 15.40900  3.52500   19.61700 1.000 48.79122  ?  258 LYS A HA     1 
ATOM   4011 H HB2    . LYS A 1 258 ? 13.80100  5.13500   19.40900 1.000 46.09307  ?  258 LYS A HB2    1 
ATOM   4012 H HB3    . LYS A 1 258 ? 13.38300  4.60000   17.97300 1.000 46.09307  ?  258 LYS A HB3    1 
ATOM   4013 H HG2    . LYS A 1 258 ? 12.99600  2.79900   20.06200 1.000 48.02063  ?  258 LYS A HG2    1 
ATOM   4014 H HG3    . LYS A 1 258 ? 12.00300  4.04000   20.03600 1.000 48.02063  ?  258 LYS A HG3    1 
ATOM   4015 H HD2    . LYS A 1 258 ? 11.53100  3.40300   17.74100 1.000 50.57633  ?  258 LYS A HD2    1 
ATOM   4016 H HD3    . LYS A 1 258 ? 12.23000  2.02100   18.09600 1.000 50.57633  ?  258 LYS A HD3    1 
ATOM   4017 H HE2    . LYS A 1 258 ? 9.87500   3.02100   19.27600 1.000 55.44711  ?  258 LYS A HE2    1 
ATOM   4018 H HE3    . LYS A 1 258 ? 9.98400   1.71900   18.37100 1.000 55.44711  ?  258 LYS A HE3    1 
ATOM   4019 H HZ1    . LYS A 1 258 ? 9.88900   1.12700   20.54600 1.000 54.09543  ?  258 LYS A HZ1    1 
ATOM   4020 H HZ2    . LYS A 1 258 ? 11.20000  0.76100   20.05000 1.000 54.09543  ?  258 LYS A HZ2    1 
ATOM   4021 H HZ3    . LYS A 1 258 ? 11.04300  1.93800   20.88000 1.000 54.09543  ?  258 LYS A HZ3    1 
ATOM   4022 N N      . PHE A 1 259 ? 14.63800  2.20300   16.79900 1.000 38.62808  ?  259 PHE A N      1 
ATOM   4023 C CA     . PHE A 1 259 ? 14.45400  0.94500   16.07900 1.000 43.16979  ?  259 PHE A CA     1 
ATOM   4024 C C      . PHE A 1 259 ? 15.76400  0.30800   15.62700 1.000 43.12641  ?  259 PHE A C      1 
ATOM   4025 O O      . PHE A 1 259 ? 15.74800  -0.82500  15.10000 1.000 42.71318  ?  259 PHE A O      1 
ATOM   4026 C CB     . PHE A 1 259 ? 13.58100  1.17900   14.83300 1.000 42.03667  ?  259 PHE A CB     1 
ATOM   4027 C CG     . PHE A 1 259 ? 12.11200  1.29000   15.14000 1.000 47.19268  ?  259 PHE A CG     1 
ATOM   4028 C CD1    . PHE A 1 259 ? 11.38000  0.17000   15.50100 1.000 46.61877  ?  259 PHE A CD1    1 
ATOM   4029 C CD2    . PHE A 1 259 ? 11.46600  2.51400   15.05100 1.000 47.97453  ?  259 PHE A CD2    1 
ATOM   4030 C CE1    . PHE A 1 259 ? 10.02100  0.26900   15.77400 1.000 47.13292  ?  259 PHE A CE1    1 
ATOM   4031 C CE2    . PHE A 1 259 ? 10.11200  2.62200   15.32700 1.000 52.65128  ?  259 PHE A CE2    1 
ATOM   4032 C CZ     . PHE A 1 259 ? 9.38500   1.49000   15.68100 1.000 51.46437  ?  259 PHE A CZ     1 
ATOM   4033 H H      . PHE A 1 259 ? 14.58200  2.89700   16.29500 1.000 46.47146  ?  259 PHE A H      1 
ATOM   4034 H HA     . PHE A 1 259 ? 14.00200  0.32300   16.67100 1.000 51.92151  ?  259 PHE A HA     1 
ATOM   4035 H HB2    . PHE A 1 259 ? 13.85900  2.00500   14.40800 1.000 50.56177  ?  259 PHE A HB2    1 
ATOM   4036 H HB3    . PHE A 1 259 ? 13.70200  0.43500   14.22300 1.000 50.56177  ?  259 PHE A HB3    1 
ATOM   4037 H HD1    . PHE A 1 259 ? 11.80300  -0.65600  15.56200 1.000 56.06029  ?  259 PHE A HD1    1 
ATOM   4038 H HD2    . PHE A 1 259 ? 11.94600  3.27000   14.80300 1.000 57.68721  ?  259 PHE A HD2    1 
ATOM   4039 H HE1    . PHE A 1 259 ? 9.54000   -0.48800  16.01900 1.000 56.67727  ?  259 PHE A HE1    1 
ATOM   4040 H HE2    . PHE A 1 259 ? 9.69100   3.45000   15.27600 1.000 63.29931  ?  259 PHE A HE2    1 
ATOM   4041 H HZ     . PHE A 1 259 ? 8.47400   1.55600   15.85400 1.000 61.87501  ?  259 PHE A HZ     1 
ATOM   4042 N N      . GLY A 1 260 ? 16.89000  0.97900   15.80500 1.000 43.50690  ?  260 GLY A N      1 
ATOM   4043 C CA     . GLY A 1 260 ? 18.15100  0.43700   15.35500 1.000 37.89216  ?  260 GLY A CA     1 
ATOM   4044 C C      . GLY A 1 260 ? 18.41800  0.60000   13.88700 1.000 38.94906  ?  260 GLY A C      1 
ATOM   4045 O O      . GLY A 1 260 ? 19.34400  -0.03600  13.36600 1.000 36.53640  ?  260 GLY A O      1 
ATOM   4046 H H      . GLY A 1 260 ? 16.94600  1.74900   16.18400 1.000 52.32605  ?  260 GLY A H      1 
ATOM   4047 H HA2    . GLY A 1 260 ? 18.86900  0.87700   15.83700 1.000 45.58836  ?  260 GLY A HA2    1 
ATOM   4048 H HA3    . GLY A 1 260 ? 18.17100  -0.51200  15.55600 1.000 45.58836  ?  260 GLY A HA3    1 
ATOM   4049 N N      . CYS A 1 261 ? 17.62500  1.41200   13.18300 1.000 35.46139  ?  261 CYS A N      1 
ATOM   4050 C CA     . CYS A 1 261 ? 17.93700  1.73300   11.79700 1.000 36.74044  ?  261 CYS A CA     1 
ATOM   4051 C C      . CYS A 1 261 ? 19.28600  2.44400   11.68200 1.000 40.80683  ?  261 CYS A C      1 
ATOM   4052 O O      . CYS A 1 261 ? 19.93200  2.38100   10.64300 1.000 37.02127  ?  261 CYS A O      1 
ATOM   4053 C CB     . CYS A 1 261 ? 16.83800  2.62400   11.19400 1.000 39.71071  ?  261 CYS A CB     1 
ATOM   4054 S SG     . CYS A 1 261 ? 15.21600  1.90400   11.30300 1.000 40.49337  ?  261 CYS A SG     1 
ATOM   4055 H H      . CYS A 1 261 ? 16.91000  1.78400   13.48400 1.000 42.67143  ?  261 CYS A H      1 
ATOM   4056 H HA     . CYS A 1 261 ? 17.97100  0.90700   11.29100 1.000 44.20629  ?  261 CYS A HA     1 
ATOM   4057 H HB2    . CYS A 1 261 ? 16.82300  3.46900   11.66900 1.000 47.77062  ?  261 CYS A HB2    1 
ATOM   4058 H HB3    . CYS A 1 261 ? 17.03600  2.77500   10.25600 1.000 47.77062  ?  261 CYS A HB3    1 
ATOM   4059 H HG     . CYS A 1 261 ? 14.41400  2.68100   10.86300 1.000 48.70981  ?  261 CYS A HG     1 
ATOM   4060 N N      . LEU A 1 262 ? 19.70500  3.13400   12.75000 1.000 38.14763  ?  262 LEU A N      1 
ATOM   4061 C CA     . LEU A 1 262 ? 20.99200  3.80900   12.80100 1.000 39.64049  ?  262 LEU A CA     1 
ATOM   4062 C C      . LEU A 1 262 ? 21.77800  3.24800   13.96900 1.000 34.78728  ?  262 LEU A C      1 
ATOM   4063 O O      . LEU A 1 262 ? 21.24000  3.10900   15.07300 1.000 39.65808  ?  262 LEU A O      1 
ATOM   4064 C CB     . LEU A 1 262 ? 20.82400  5.32500   12.94600 1.000 41.44675  ?  262 LEU A CB     1 
ATOM   4065 C CG     . LEU A 1 262 ? 22.12400  6.14300   12.98000 1.000 36.81587  ?  262 LEU A CG     1 
ATOM   4066 C CD1    . LEU A 1 262 ? 22.83800  6.10400   11.66400 1.000 39.23062  ?  262 LEU A CD1    1 
ATOM   4067 C CD2    . LEU A 1 262 ? 21.82700  7.58200   13.37600 1.000 39.00002  ?  262 LEU A CD2    1 
ATOM   4068 H H      . LEU A 1 262 ? 19.24400  3.22300   13.47000 1.000 45.89493  ?  262 LEU A H      1 
ATOM   4069 H HA     . LEU A 1 262 ? 21.48500  3.64600   11.98100 1.000 47.68635  ?  262 LEU A HA     1 
ATOM   4070 H HB2    . LEU A 1 262 ? 20.30300  5.64500   12.19300 1.000 49.85387  ?  262 LEU A HB2    1 
ATOM   4071 H HB3    . LEU A 1 262 ? 20.35200  5.49900   13.77500 1.000 49.85387  ?  262 LEU A HB3    1 
ATOM   4072 H HG     . LEU A 1 262 ? 22.71400  5.75000   13.64200 1.000 44.29681  ?  262 LEU A HG     1 
ATOM   4073 H HD11   . LEU A 1 262 ? 23.60800  6.69300   11.70500 1.000 47.19451  ?  262 LEU A HD11   1 
ATOM   4074 H HD12   . LEU A 1 262 ? 23.12600  5.19500   11.48800 1.000 47.19451  ?  262 LEU A HD12   1 
ATOM   4075 H HD13   . LEU A 1 262 ? 22.23200  6.40000   10.96700 1.000 47.19451  ?  262 LEU A HD13   1 
ATOM   4076 H HD21   . LEU A 1 262 ? 22.66500  8.04500   13.53400 1.000 46.91779  ?  262 LEU A HD21   1 
ATOM   4077 H HD22   . LEU A 1 262 ? 21.34200  8.01400   12.65500 1.000 46.91779  ?  262 LEU A HD22   1 
ATOM   4078 H HD23   . LEU A 1 262 ? 21.29000  7.58300   14.18400 1.000 46.91779  ?  262 LEU A HD23   1 
ATOM   4079 N N      . SER A 1 263 ? 23.04000  2.94700   13.73300 1.000 37.24833  ?  263 SER A N      1 
ATOM   4080 C CA     . SER A 1 263 ? 23.91000  2.46600   14.77900 1.000 39.68358  ?  263 SER A CA     1 
ATOM   4081 C C      . SER A 1 263 ? 24.32600  3.63000   15.67000 1.000 39.74393  ?  263 SER A C      1 
ATOM   4082 O O      . SER A 1 263 ? 24.84900  4.63500   15.17500 1.000 40.21516  ?  263 SER A O      1 
ATOM   4083 C CB     . SER A 1 263 ? 25.15200  1.79100   14.16900 1.000 37.68047  ?  263 SER A CB     1 
ATOM   4084 O OG     . SER A 1 263 ? 26.20600  1.76100   15.10100 1.000 41.39580  ?  263 SER A OG     1 
ATOM   4085 H H      . SER A 1 263 ? 23.42000  3.01500   12.96400 1.000 44.81576  ?  263 SER A H      1 
ATOM   4086 H HA     . SER A 1 263 ? 23.43500  1.81500   15.31900 1.000 47.73807  ?  263 SER A HA     1 
ATOM   4087 H HB2    . SER A 1 263 ? 24.92600  0.88200   13.91600 1.000 45.33433  ?  263 SER A HB2    1 
ATOM   4088 H HB3    . SER A 1 263 ? 25.43300  2.29300   13.38800 1.000 45.33433  ?  263 SER A HB3    1 
ATOM   4089 H HG     . SER A 1 263 ? 26.88800  1.41600   14.75200 1.000 49.79273  ?  263 SER A HG     1 
ATOM   4090 N N      . ALA A 1 264 ? 24.07900  3.49900   16.97000 1.000 35.30013  ?  264 ALA A N      1 
ATOM   4091 C CA     . ALA A 1 264 ? 24.59200  4.49800   17.90600 1.000 42.30004  ?  264 ALA A CA     1 
ATOM   4092 C C      . ALA A 1 264 ? 26.11600  4.56000   17.84400 1.000 40.08575  ?  264 ALA A C      1 
ATOM   4093 O O      . ALA A 1 264 ? 26.71100  5.63000   17.94400 1.000 39.61267  ?  264 ALA A O      1 
ATOM   4094 C CB     . ALA A 1 264 ? 24.12200  4.18100   19.32300 1.000 42.57289  ?  264 ALA A CB     1 
ATOM   4095 H H      . ALA A 1 264 ? 23.62900  2.86000   17.32800 1.000 42.47792  ?  264 ALA A H      1 
ATOM   4096 H HA     . ALA A 1 264 ? 24.24000  5.37000   17.66600 1.000 50.87781  ?  264 ALA A HA     1 
ATOM   4097 H HB1    . ALA A 1 264 ? 24.47300  4.85100   19.93000 1.000 51.20524  ?  264 ALA A HB1    1 
ATOM   4098 H HB2    . ALA A 1 264 ? 23.15200  4.19100   19.34400 1.000 51.20524  ?  264 ALA A HB2    1 
ATOM   4099 H HB3    . ALA A 1 264 ? 24.44900  3.30300   19.57500 1.000 51.20524  ?  264 ALA A HB3    1 
ATOM   4100 N N      . ARG A 1 265 ? 26.75500  3.41600   17.64200 1.000 45.77151  ?  265 ARG A N      1 
ATOM   4101 C CA     . ARG A 1 265 ? 28.21200  3.36400   17.59800 1.000 41.87627  ?  265 ARG A CA     1 
ATOM   4102 C C      . ARG A 1 265 ? 28.75600  4.10500   16.38300 1.000 42.49900  ?  265 ARG A C      1 
ATOM   4103 O O      . ARG A 1 265 ? 29.78100  4.80500   16.48400 1.000 42.00442  ?  265 ARG A O      1 
ATOM   4104 C CB     . ARG A 1 265 ? 28.67400  1.91600   17.60600 1.000 47.40987  ?  265 ARG A CB     1 
ATOM   4105 C CG     . ARG A 1 265 ? 29.35000  1.48100   18.90200 1.000 54.15254  ?  265 ARG A CG     1 
ATOM   4106 C CD     . ARG A 1 265 ? 28.53600  0.45900   19.68000 1.000 56.69811  ?  265 ARG A CD     1 
ATOM   4107 N NE     . ARG A 1 265 ? 28.93200  -0.89700  19.34800 1.000 58.15892  ?  265 ARG A NE     1 
ATOM   4108 C CZ     . ARG A 1 265 ? 29.03900  -1.89500  20.22500 1.000 54.20189  ?  265 ARG A CZ     1 
ATOM   4109 N NH1    . ARG A 1 265 ? 28.76200  -1.72200  21.51100 1.000 53.40376  ?  265 ARG A NH1    1 
ATOM   4110 N NH2    . ARG A 1 265 ? 29.43400  -3.08500  19.79800 1.000 49.24441  ?  265 ARG A NH2    1 
ATOM   4111 H H      . ARG A 1 265 ? 26.37200  2.65500   17.52600 1.000 55.04359  ?  265 ARG A H      1 
ATOM   4112 H HA     . ARG A 1 265 ? 28.56900  3.79700   18.38900 1.000 50.36930  ?  265 ARG A HA     1 
ATOM   4113 H HB2    . ARG A 1 265 ? 27.90300  1.34300   17.47100 1.000 57.00961  ?  265 ARG A HB2    1 
ATOM   4114 H HB3    . ARG A 1 265 ? 29.31200  1.79000   16.88600 1.000 57.00961  ?  265 ARG A HB3    1 
ATOM   4115 H HG2    . ARG A 1 265 ? 30.20900  1.08100   18.69100 1.000 65.10082  ?  265 ARG A HG2    1 
ATOM   4116 H HG3    . ARG A 1 265 ? 29.47600  2.25800   19.46900 1.000 65.10082  ?  265 ARG A HG3    1 
ATOM   4117 H HD2    . ARG A 1 265 ? 28.67600  0.59400   20.63000 1.000 68.15550  ?  265 ARG A HD2    1 
ATOM   4118 H HD3    . ARG A 1 265 ? 27.59700  0.56500   19.46400 1.000 68.15550  ?  265 ARG A HD3    1 
ATOM   4119 H HE     . ARG A 1 265 ? 29.11100  -1.06900  18.52400 1.000 69.90848  ?  265 ARG A HE     1 
ATOM   4120 H HH11   . ARG A 1 265 ? 28.50600  -0.95200  21.79600 1.000 64.20228  ?  265 ARG A HH11   1 
ATOM   4121 H HH12   . ARG A 1 265 ? 28.83800  -2.38000  22.06000 1.000 64.20228  ?  265 ARG A HH12   1 
ATOM   4122 H HH21   . ARG A 1 265 ? 29.61700  -3.20400  18.96600 1.000 59.21106  ?  265 ARG A HH21   1 
ATOM   4123 H HH22   . ARG A 1 265 ? 29.50800  -3.73800  20.35200 1.000 59.21106  ?  265 ARG A HH22   1 
ATOM   4124 N N      . LEU A 1 266 ? 28.10100  3.97000   15.23200 1.000 39.01365  ?  266 LEU A N      1 
ATOM   4125 C CA     . LEU A 1 266 ? 28.51200  4.74100   14.05500 1.000 41.12984  ?  266 LEU A CA     1 
ATOM   4126 C C      . LEU A 1 266 ? 28.33800  6.24000   14.29300 1.000 38.02220  ?  266 LEU A C      1 
ATOM   4127 O O      . LEU A 1 266 ? 29.21600  7.04400   13.97100 1.000 38.31201  ?  266 LEU A O      1 
ATOM   4128 C CB     . LEU A 1 266 ? 27.69400  4.29300   12.83200 1.000 42.28792  ?  266 LEU A CB     1 
ATOM   4129 C CG     . LEU A 1 266 ? 27.84100  5.14500   11.57000 1.000 45.76236  ?  266 LEU A CG     1 
ATOM   4130 C CD1    . LEU A 1 266 ? 29.25900  5.06300   11.02400 1.000 47.93715  ?  266 LEU A CD1    1 
ATOM   4131 C CD2    . LEU A 1 266 ? 26.83200  4.70700   10.51400 1.000 50.73085  ?  266 LEU A CD2    1 
ATOM   4132 H H      . LEU A 1 266 ? 27.42800  3.45000   15.10600 1.000 46.93415  ?  266 LEU A H      1 
ATOM   4133 H HA     . LEU A 1 266 ? 29.45000  4.56900   13.87700 1.000 49.47358  ?  266 LEU A HA     1 
ATOM   4134 H HB2    . LEU A 1 266 ? 27.96700  3.39100   12.60100 1.000 50.86328  ?  266 LEU A HB2    1 
ATOM   4135 H HB3    . LEU A 1 266 ? 26.75600  4.30400   13.07600 1.000 50.86328  ?  266 LEU A HB3    1 
ATOM   4136 H HG     . LEU A 1 266 ? 27.66400  6.07200   11.79400 1.000 55.03260  ?  266 LEU A HG     1 
ATOM   4137 H HD11   . LEU A 1 266 ? 29.33800  5.65400   10.25900 1.000 57.64234  ?  266 LEU A HD11   1 
ATOM   4138 H HD12   . LEU A 1 266 ? 29.88100  5.33500   11.71700 1.000 57.64234  ?  266 LEU A HD12   1 
ATOM   4139 H HD13   . LEU A 1 266 ? 29.44200  4.14900   10.75500 1.000 57.64234  ?  266 LEU A HD13   1 
ATOM   4140 H HD21   . LEU A 1 266 ? 26.93700  5.26300   9.72700  1.000 60.99479  ?  266 LEU A HD21   1 
ATOM   4141 H HD22   . LEU A 1 266 ? 26.99600  3.77800   10.28700 1.000 60.99479  ?  266 LEU A HD22   1 
ATOM   4142 H HD23   . LEU A 1 266 ? 25.93700  4.80700   10.87300 1.000 60.99479  ?  266 LEU A HD23   1 
ATOM   4143 N N      . PHE A 1 267 ? 27.19000  6.63200   14.84100 1.000 39.39342  ?  267 PHE A N      1 
ATOM   4144 C CA     . PHE A 1 267 ? 26.96300  8.04200   15.18900 1.000 43.77684  ?  267 PHE A CA     1 
ATOM   4145 C C      . PHE A 1 267 ? 28.09700  8.57200   16.06500 1.000 42.91306  ?  267 PHE A C      1 
ATOM   4146 O O      . PHE A 1 267 ? 28.68600  9.63000   15.77600 1.000 42.01619  ?  267 PHE A O      1 
ATOM   4147 C CB     . PHE A 1 267 ? 25.60300  8.16100   15.88900 1.000 43.20438  ?  267 PHE A CB     1 
ATOM   4148 C CG     . PHE A 1 267 ? 25.05100  9.56300   15.97100 1.000 44.99998  ?  267 PHE A CG     1 
ATOM   4149 C CD1    . PHE A 1 267 ? 25.82100  10.67400  15.63600 1.000 48.03965  ?  267 PHE A CD1    1 
ATOM   4150 C CD2    . PHE A 1 267 ? 23.76400  9.76700   16.41100 1.000 43.52205  ?  267 PHE A CD2    1 
ATOM   4151 C CE1    . PHE A 1 267 ? 25.29700  11.95200  15.74100 1.000 43.64283  ?  267 PHE A CE1    1 
ATOM   4152 C CE2    . PHE A 1 267 ? 23.23000  11.05100  16.50900 1.000 49.17733  ?  267 PHE A CE2    1 
ATOM   4153 C CZ     . PHE A 1 267 ? 23.99600  12.13600  16.16900 1.000 41.92995  ?  267 PHE A CZ     1 
ATOM   4154 H H      . PHE A 1 267 ? 26.53000  6.11100   15.02100 1.000 47.38987  ?  267 PHE A H      1 
ATOM   4155 H HA     . PHE A 1 267 ? 26.94100  8.58800   14.38700 1.000 52.64998  ?  267 PHE A HA     1 
ATOM   4156 H HB2    . PHE A 1 267 ? 24.95900  7.62300   15.40300 1.000 51.96303  ?  267 PHE A HB2    1 
ATOM   4157 H HB3    . PHE A 1 267 ? 25.69500  7.83100   16.79600 1.000 51.96303  ?  267 PHE A HB3    1 
ATOM   4158 H HD1    . PHE A 1 267 ? 26.69500  10.55700  15.34000 1.000 57.76535  ?  267 PHE A HD1    1 
ATOM   4159 H HD2    . PHE A 1 267 ? 23.24000  9.03600   16.64700 1.000 52.34423  ?  267 PHE A HD2    1 
ATOM   4160 H HE1    . PHE A 1 267 ? 25.82100  12.68800  15.52200 1.000 52.48916  ?  267 PHE A HE1    1 
ATOM   4161 H HE2    . PHE A 1 267 ? 22.35600  11.17100  16.80500 1.000 59.13056  ?  267 PHE A HE2    1 
ATOM   4162 H HZ     . PHE A 1 267 ? 23.64100  12.99400  16.22700 1.000 50.43371  ?  267 PHE A HZ     1 
ATOM   4163 N N      . HIS A 1 268 ? 28.43500  7.84000   17.13500 1.000 41.55495  ?  268 HIS A N      1 
ATOM   4164 C CA     . HIS A 1 268 ? 29.47200  8.30500   18.04500 1.000 40.14795  ?  268 HIS A CA     1 
ATOM   4165 C C      . HIS A 1 268 ? 30.82100  8.43400   17.32500 1.000 46.27800  ?  268 HIS A C      1 
ATOM   4166 O O      . HIS A 1 268 ? 31.52900  9.43900   17.47000 1.000 39.88006  ?  268 HIS A O      1 
ATOM   4167 C CB     . HIS A 1 268 ? 29.58900  7.34100   19.23100 1.000 41.23713  ?  268 HIS A CB     1 
ATOM   4168 C CG     . HIS A 1 268 ? 30.34300  7.90100   20.39500 1.000 39.59998  ?  268 HIS A CG     1 
ATOM   4169 N ND1    . HIS A 1 268 ? 31.71300  7.81900   20.50500 1.000 46.28442  ?  268 HIS A ND1    1 
ATOM   4170 C CD2    . HIS A 1 268 ? 29.91400  8.55900   21.49800 1.000 37.83880  ?  268 HIS A CD2    1 
ATOM   4171 C CE1    . HIS A 1 268 ? 32.10200  8.40000   21.62900 1.000 43.70218  ?  268 HIS A CE1    1 
ATOM   4172 N NE2    . HIS A 1 268 ? 31.02400  8.85500   22.25400 1.000 41.92117  ?  268 HIS A NE2    1 
ATOM   4173 H H      . HIS A 1 268 ? 28.08200  7.08500   17.34800 1.000 49.98371  ?  268 HIS A H      1 
ATOM   4174 H HA     . HIS A 1 268 ? 29.22400  9.18000   18.38300 1.000 48.29531  ?  268 HIS A HA     1 
ATOM   4175 H HB2    . HIS A 1 268 ? 28.69700  7.11500   19.53800 1.000 49.60232  ?  268 HIS A HB2    1 
ATOM   4176 H HB3    . HIS A 1 268 ? 30.05200  6.54100   18.93700 1.000 49.60232  ?  268 HIS A HB3    1 
ATOM   4177 H HD1    . HIS A 1 268 ? 32.23600  7.44800   19.93100 1.000 55.65908  ?  268 HIS A HD1    1 
ATOM   4178 H HD2    . HIS A 1 268 ? 29.03300  8.77300   21.70600 1.000 45.52433  ?  268 HIS A HD2    1 
ATOM   4179 H HE1    . HIS A 1 268 ? 32.97900  8.47600   21.92900 1.000 52.56038  ?  268 HIS A HE1    1 
ATOM   4180 N N      . ALA A 1 269 ? 31.18900  7.41200   16.54300 1.000 41.51712  ?  269 ALA A N      1 
ATOM   4181 C CA     . ALA A 1 269 ? 32.45600  7.45500   15.82900 1.000 42.80304  ?  269 ALA A CA     1 
ATOM   4182 C C      . ALA A 1 269 ? 32.52700  8.65500   14.89900 1.000 45.88341  ?  269 ALA A C      1 
ATOM   4183 O O      . ALA A 1 269 ? 33.58700  9.28400   14.76600 1.000 47.42583  ?  269 ALA A O      1 
ATOM   4184 C CB     . ALA A 1 269 ? 32.65700  6.15200   15.04800 1.000 44.93063  ?  269 ALA A CB     1 
ATOM   4185 H H      . ALA A 1 269 ? 30.72800  6.69800   16.41400 1.000 49.93831  ?  269 ALA A H      1 
ATOM   4186 H HA     . ALA A 1 269 ? 33.17700  7.53500   16.47300 1.000 51.48142  ?  269 ALA A HA     1 
ATOM   4187 H HB1    . ALA A 1 269 ? 33.50100  6.19700   14.57200 1.000 54.03453  ?  269 ALA A HB1    1 
ATOM   4188 H HB2    . ALA A 1 269 ? 32.66800  5.40900   15.67100 1.000 54.03453  ?  269 ALA A HB2    1 
ATOM   4189 H HB3    . ALA A 1 269 ? 31.92700  6.04600   14.41900 1.000 54.03453  ?  269 ALA A HB3    1 
ATOM   4190 N N      . ARG A 1 270 ? 31.40700  8.99600   14.24900 1.000 41.72146  ?  270 ARG A N      1 
ATOM   4191 C CA     . ARG A 1 270 ? 31.40700  10.14300  13.35300 1.000 43.99637  ?  270 ARG A CA     1 
ATOM   4192 C C      . ARG A 1 270 ? 31.57300  11.45700  14.10500 1.000 46.89085  ?  270 ARG A C      1 
ATOM   4193 O O      . ARG A 1 270 ? 32.19300  12.40400  13.58000 1.000 49.47448  ?  270 ARG A O      1 
ATOM   4194 C CB     . ARG A 1 270 ? 30.12500  10.16800  12.52600 1.000 46.20230  ?  270 ARG A CB     1 
ATOM   4195 C CG     . ARG A 1 270 ? 30.07400  9.11400   11.41900 1.000 53.26407  ?  270 ARG A CG     1 
ATOM   4196 C CD     . ARG A 1 270 ? 31.04100  9.41400   10.29100 1.000 55.63641  ?  270 ARG A CD     1 
ATOM   4197 N NE     . ARG A 1 270 ? 30.64200  10.57900  9.50800  1.000 59.80324  ?  270 ARG A NE     1 
ATOM   4198 C CZ     . ARG A 1 270 ? 29.70600  10.57200  8.57300  1.000 66.74166  ?  270 ARG A CZ     1 
ATOM   4199 N NH1    . ARG A 1 270 ? 29.04500  9.46300   8.26100  1.000 69.51900  ?  270 ARG A NH1    1 
ATOM   4200 N NH2    . ARG A 1 270 ? 29.42200  11.70400  7.93200  1.000 57.65266  ?  270 ARG A NH2    1 
ATOM   4201 H H      . ARG A 1 270 ? 30.65400  8.58500   14.31200 1.000 50.18352  ?  270 ARG A H      1 
ATOM   4202 H HA     . ARG A 1 270 ? 32.15700  10.05200  12.74500 1.000 52.91341  ?  270 ARG A HA     1 
ATOM   4203 H HB2    . ARG A 1 270 ? 29.37100  10.01200  13.11600 1.000 55.56053  ?  270 ARG A HB2    1 
ATOM   4204 H HB3    . ARG A 1 270 ? 30.04300  11.03900  12.10600 1.000 55.56053  ?  270 ARG A HB3    1 
ATOM   4205 H HG2    . ARG A 1 270 ? 30.30500  8.24900   11.79300 1.000 64.03466  ?  270 ARG A HG2    1 
ATOM   4206 H HG3    . ARG A 1 270 ? 29.17800  9.08600   11.04800 1.000 64.03466  ?  270 ARG A HG3    1 
ATOM   4207 H HD2    . ARG A 1 270 ? 31.91900  9.58800   10.66400 1.000 66.88146  ?  270 ARG A HD2    1 
ATOM   4208 H HD3    . ARG A 1 270 ? 31.08000  8.64900   9.69500  1.000 66.88146  ?  270 ARG A HD3    1 
ATOM   4209 H HE     . ARG A 1 270 ? 31.04400  11.32300  9.66500  1.000 71.88166  ?  270 ARG A HE     1 
ATOM   4210 H HH11   . ARG A 1 270 ? 29.22100  8.72800   8.67100  1.000 83.54058  ?  270 ARG A HH11   1 
ATOM   4211 H HH12   . ARG A 1 270 ? 28.44000  9.48100   7.65000  1.000 83.54058  ?  270 ARG A HH12   1 
ATOM   4212 H HH21   . ARG A 1 270 ? 29.84500  12.42700  8.12800  1.000 69.30096  ?  270 ARG A HH21   1 
ATOM   4213 H HH22   . ARG A 1 270 ? 28.81600  11.71200  7.32300  1.000 69.30096  ?  270 ARG A HH22   1 
ATOM   4214 N N      . LEU A 1 271 ? 31.02300  11.55700  15.32300 1.000 44.22512  ?  271 LEU A N      1 
ATOM   4215 C CA     . LEU A 1 271 ? 31.19200  12.77200  16.10700 1.000 41.82147  ?  271 LEU A CA     1 
ATOM   4216 C C      . LEU A 1 271 ? 32.64700  12.97200  16.50600 1.000 46.34315  ?  271 LEU A C      1 
ATOM   4217 O O      . LEU A 1 271 ? 33.16200  14.09300  16.44800 1.000 43.26360  ?  271 LEU A O      1 
ATOM   4218 C CB     . LEU A 1 271 ? 30.30100  12.73200  17.34300 1.000 43.39759  ?  271 LEU A CB     1 
ATOM   4219 C CG     . LEU A 1 271 ? 28.80600  12.94000  17.09100 1.000 44.96598  ?  271 LEU A CG     1 
ATOM   4220 C CD1    . LEU A 1 271 ? 27.98500  12.25500  18.17700 1.000 42.41885  ?  271 LEU A CD1    1 
ATOM   4221 C CD2    . LEU A 1 271 ? 28.47600  14.42200  17.02500 1.000 46.42102  ?  271 LEU A CD2    1 
ATOM   4222 H H      . LEU A 1 271 ? 30.55700  10.94400  15.70600 1.000 53.18792  ?  271 LEU A H      1 
ATOM   4223 H HA     . LEU A 1 271 ? 30.91900  13.52900  15.56600 1.000 50.30353  ?  271 LEU A HA     1 
ATOM   4224 H HB2    . LEU A 1 271 ? 30.40400  11.86500  17.76400 1.000 52.19488  ?  271 LEU A HB2    1 
ATOM   4225 H HB3    . LEU A 1 271 ? 30.59100  13.43200  17.94900 1.000 52.19488  ?  271 LEU A HB3    1 
ATOM   4226 H HG     . LEU A 1 271 ? 28.57000  12.54400  16.23700 1.000 54.07695  ?  271 LEU A HG     1 
ATOM   4227 H HD11   . LEU A 1 271 ? 27.04300  12.40200  18.00000 1.000 51.02039  ?  271 LEU A HD11   1 
ATOM   4228 H HD12   . LEU A 1 271 ? 28.17900  11.30400  18.16700 1.000 51.02039  ?  271 LEU A HD12   1 
ATOM   4229 H HD13   . LEU A 1 271 ? 28.22300  12.63200  19.03800 1.000 51.02039  ?  271 LEU A HD13   1 
ATOM   4230 H HD21   . LEU A 1 271 ? 27.52600  14.52700  16.85800 1.000 55.82300  ?  271 LEU A HD21   1 
ATOM   4231 H HD22   . LEU A 1 271 ? 28.71100  14.83600  17.87000 1.000 55.82300  ?  271 LEU A HD22   1 
ATOM   4232 H HD23   . LEU A 1 271 ? 28.98500  14.82800  16.30600 1.000 55.82300  ?  271 LEU A HD23   1 
ATOM   4233 N N      . LEU A 1 272 ? 33.32300  11.89800  16.93600 1.000 41.71288  ?  272 LEU A N      1 
ATOM   4234 C CA     . LEU A 1 272 ? 34.71700  12.02200  17.31500 1.000 46.73777  ?  272 LEU A CA     1 
ATOM   4235 C C      . LEU A 1 272 ? 35.56700  12.46000  16.12200 1.000 50.11333  ?  272 LEU A C      1 
ATOM   4236 O O      . LEU A 1 272 ? 36.54000  13.20400  16.28700 1.000 47.29445  ?  272 LEU A O      1 
ATOM   4237 C CB     . LEU A 1 272 ? 35.23500  10.69600  17.87800 1.000 48.23009  ?  272 LEU A CB     1 
ATOM   4238 C CG     . LEU A 1 272 ? 34.59500  10.18300  19.17000 1.000 50.11848  ?  272 LEU A CG     1 
ATOM   4239 C CD1    . LEU A 1 272 ? 35.34400  8.95800   19.67300 1.000 47.44261  ?  272 LEU A CD1    1 
ATOM   4240 C CD2    . LEU A 1 272 ? 34.54400  11.25700  20.24700 1.000 54.69049  ?  272 LEU A CD2    1 
ATOM   4241 H H      . LEU A 1 272 ? 32.99600  11.10700  17.01400 1.000 50.17323  ?  272 LEU A H      1 
ATOM   4242 H HA     . LEU A 1 272 ? 34.79300  12.69200  18.01200 1.000 56.20309  ?  272 LEU A HA     1 
ATOM   4243 H HB2    . LEU A 1 272 ? 35.09500  10.01300  17.20400 1.000 57.99388  ?  272 LEU A HB2    1 
ATOM   4244 H HB3    . LEU A 1 272 ? 36.18300  10.79900  18.05500 1.000 57.99388  ?  272 LEU A HB3    1 
ATOM   4245 H HG     . LEU A 1 272 ? 33.67800  9.93300   18.97700 1.000 60.25995  ?  272 LEU A HG     1 
ATOM   4246 H HD11   . LEU A 1 272 ? 34.90000  8.61900   20.46600 1.000 57.04890  ?  272 LEU A HD11   1 
ATOM   4247 H HD12   . LEU A 1 272 ? 35.34300  8.28000   18.97900 1.000 57.04890  ?  272 LEU A HD12   1 
ATOM   4248 H HD13   . LEU A 1 272 ? 36.25600  9.21100   19.88700 1.000 57.04890  ?  272 LEU A HD13   1 
ATOM   4249 H HD21   . LEU A 1 272 ? 34.27400  10.85000  21.08500 1.000 65.74635  ?  272 LEU A HD21   1 
ATOM   4250 H HD22   . LEU A 1 272 ? 35.42500  11.65300  20.34000 1.000 65.74635  ?  272 LEU A HD22   1 
ATOM   4251 H HD23   . LEU A 1 272 ? 33.90200  11.93500  19.98600 1.000 65.74635  ?  272 LEU A HD23   1 
ATOM   4252 N N      . GLU A 1 273 ? 35.21400  12.00300  14.92000 1.000 53.36151  ?  273 GLU A N      1 
ATOM   4253 C CA     . GLU A 1 273 ? 35.89700  12.46400  13.71500 1.000 55.92346  ?  273 GLU A CA     1 
ATOM   4254 C C      . GLU A 1 273 ? 35.83100  13.97700  13.60200 1.000 51.66324  ?  273 GLU A C      1 
ATOM   4255 O O      . GLU A 1 273 ? 36.84100  14.64300  13.34900 1.000 52.79218  ?  273 GLU A O      1 
ATOM   4256 C CB     . GLU A 1 273 ? 35.26800  11.82000  12.48300 1.000 58.49812  ?  273 GLU A CB     1 
ATOM   4257 C CG     . GLU A 1 273 ? 36.12700  10.79200  11.79000 1.000 81.26037  ?  273 GLU A CG     1 
ATOM   4258 C CD     . GLU A 1 273 ? 35.32900  9.95100   10.78500 1.000 85.23807  ?  273 GLU A CD     1 
ATOM   4259 O OE1    . GLU A 1 273 ? 34.74000  10.54600  9.84900  1.000 79.23287  ?  273 GLU A OE1    1 
ATOM   4260 O OE2    . GLU A 1 273 ? 35.29200  8.71100   10.93200 1.000 76.02229  -1 273 GLU A OE2    1 
ATOM   4261 H H      . GLU A 1 273 ? 34.58800  11.43000  14.77700 1.000 64.15158  ?  273 GLU A H      1 
ATOM   4262 H HA     . GLU A 1 273 ? 36.82800  12.19700  13.76200 1.000 67.22593  ?  273 GLU A HA     1 
ATOM   4263 H HB2    . GLU A 1 273 ? 34.44700  11.37900  12.75200 1.000 70.31552  ?  273 GLU A HB2    1 
ATOM   4264 H HB3    . GLU A 1 273 ? 35.07300  12.51800  11.83800 1.000 70.31552  ?  273 GLU A HB3    1 
ATOM   4265 H HG2    . GLU A 1 273 ? 36.83700  11.24400  11.30800 1.000 97.63021  ?  273 GLU A HG2    1 
ATOM   4266 H HG3    . GLU A 1 273 ? 36.50400  10.19300  12.45300 1.000 97.63021  ?  273 GLU A HG3    1 
ATOM   4267 N N      . VAL A 1 274 ? 34.63700  14.54700  13.79700 1.000 51.90542  ?  274 VAL A N      1 
ATOM   4268 C CA     . VAL A 1 274 ? 34.47500  15.99100  13.70100 1.000 50.76159  ?  274 VAL A CA     1 
ATOM   4269 C C      . VAL A 1 274 ? 35.16400  16.68300  14.86300 1.000 47.93115  ?  274 VAL A C      1 
ATOM   4270 O O      . VAL A 1 274 ? 35.79200  17.73800  14.69600 1.000 50.60753  ?  274 VAL A O      1 
ATOM   4271 C CB     . VAL A 1 274 ? 32.97700  16.35300  13.62700 1.000 49.32391  ?  274 VAL A CB     1 
ATOM   4272 C CG1    . VAL A 1 274 ? 32.76700  17.82900  13.91000 1.000 47.79969  ?  274 VAL A CG1    1 
ATOM   4273 C CG2    . VAL A 1 274 ? 32.41000  15.98500  12.27100 1.000 50.90275  ?  274 VAL A CG2    1 
ATOM   4274 H H      . VAL A 1 274 ? 33.91400  14.11900  13.98300 1.000 62.40428  ?  274 VAL A H      1 
ATOM   4275 H HA     . VAL A 1 274 ? 34.89800  16.29700  12.88300 1.000 61.03167  ?  274 VAL A HA     1 
ATOM   4276 H HB     . VAL A 1 274 ? 32.50000  15.84800  14.30400 1.000 59.30646  ?  274 VAL A HB     1 
ATOM   4277 H HG11   . VAL A 1 274 ? 31.88700  18.08900  13.59600 1.000 57.47740  ?  274 VAL A HG11   1 
ATOM   4278 H HG12   . VAL A 1 274 ? 32.83600  17.98100  14.86500 1.000 57.47740  ?  274 VAL A HG12   1 
ATOM   4279 H HG13   . VAL A 1 274 ? 33.44800  18.34000  13.44400 1.000 57.47740  ?  274 VAL A HG13   1 
ATOM   4280 H HG21   . VAL A 1 274 ? 31.46700  16.20900  12.25200 1.000 61.20107  ?  274 VAL A HG21   1 
ATOM   4281 H HG22   . VAL A 1 274 ? 32.88300  16.48200  11.58600 1.000 61.20107  ?  274 VAL A HG22   1 
ATOM   4282 H HG23   . VAL A 1 274 ? 32.52700  15.03200  12.12800 1.000 61.20107  ?  274 VAL A HG23   1 
ATOM   4283 N N      . TYR A 1 275 ? 35.05000  16.11500  16.06500 1.000 47.21173  ?  275 TYR A N      1 
ATOM   4284 C CA     . TYR A 1 275 ? 35.64200  16.75500  17.23900 1.000 48.27548  ?  275 TYR A CA     1 
ATOM   4285 C C      . TYR A 1 275 ? 37.16800  16.84700  17.12200 1.000 46.80516  ?  275 TYR A C      1 
ATOM   4286 O O      . TYR A 1 275 ? 37.75800  17.81700  17.59200 1.000 52.27520  ?  275 TYR A O      1 
ATOM   4287 C CB     . TYR A 1 275 ? 35.25700  15.99800  18.50700 1.000 42.15649  ?  275 TYR A CB     1 
ATOM   4288 C CG     . TYR A 1 275 ? 33.80800  16.15200  18.92500 1.000 48.22620  ?  275 TYR A CG     1 
ATOM   4289 C CD1    . TYR A 1 275 ? 32.96200  17.05800  18.29000 1.000 46.79680  ?  275 TYR A CD1    1 
ATOM   4290 C CD2    . TYR A 1 275 ? 33.28000  15.37200  19.95000 1.000 45.09091  ?  275 TYR A CD2    1 
ATOM   4291 C CE1    . TYR A 1 275 ? 31.63400  17.19000  18.66900 1.000 45.52406  ?  275 TYR A CE1    1 
ATOM   4292 C CE2    . TYR A 1 275 ? 31.95900  15.49600  20.33300 1.000 43.95593  ?  275 TYR A CE2    1 
ATOM   4293 C CZ     . TYR A 1 275 ? 31.13900  16.40800  19.69600 1.000 45.73335  ?  275 TYR A CZ     1 
ATOM   4294 O OH     . TYR A 1 275 ? 29.82300  16.53000  20.09300 1.000 42.08074  ?  275 TYR A OH     1 
ATOM   4295 H H      . TYR A 1 275 ? 34.64200  15.37500  16.22500 1.000 56.77184  ?  275 TYR A H      1 
ATOM   4296 H HA     . TYR A 1 275 ? 35.28800  17.65500  17.31000 1.000 58.04835  ?  275 TYR A HA     1 
ATOM   4297 H HB2    . TYR A 1 275 ? 35.42000  15.05200  18.36200 1.000 50.70555  ?  275 TYR A HB2    1 
ATOM   4298 H HB3    . TYR A 1 275 ? 35.80800  16.32100  19.23800 1.000 50.70555  ?  275 TYR A HB3    1 
ATOM   4299 H HD1    . TYR A 1 275 ? 33.29300  17.58400  17.59800 1.000 56.27393  ?  275 TYR A HD1    1 
ATOM   4300 H HD2    . TYR A 1 275 ? 33.82600  14.75800  20.38500 1.000 54.22686  ?  275 TYR A HD2    1 
ATOM   4301 H HE1    . TYR A 1 275 ? 31.08200  17.80000  18.23600 1.000 54.74664  ?  275 TYR A HE1    1 
ATOM   4302 H HE2    . TYR A 1 275 ? 31.62200  14.96700  21.01900 1.000 52.86488  ?  275 TYR A HE2    1 
ATOM   4303 H HH     . TYR A 1 275 ? 29.68400  16.05900  20.77500 1.000 50.61466  ?  275 TYR A HH     1 
ATOM   4304 N N      . ARG A 1 276 ? 37.81200  15.85200  16.49900 1.000 53.79106  ?  276 ARG A N      1 
ATOM   4305 C CA     . ARG A 1 276 ? 39.26800  15.91000  16.34500 1.000 55.97759  ?  276 ARG A CA     1 
ATOM   4306 C C      . ARG A 1 276 ? 39.68700  17.18300  15.61900 1.000 50.81019  ?  276 ARG A C      1 
ATOM   4307 O O      . ARG A 1 276 ? 40.70200  17.79700  15.96000 1.000 53.07976  ?  276 ARG A O      1 
ATOM   4308 C CB     . ARG A 1 276 ? 39.78300  14.69000  15.57700 1.000 52.73381  ?  276 ARG A CB     1 
ATOM   4309 C CG     . ARG A 1 276 ? 39.53700  13.35300  16.25500 1.000 67.59193  ?  276 ARG A CG     1 
ATOM   4310 C CD     . ARG A 1 276 ? 40.60100  12.31100  15.88800 1.000 78.20527  ?  276 ARG A CD     1 
ATOM   4311 N NE     . ARG A 1 276 ? 40.26500  11.56600  14.68100 1.000 90.20373  ?  276 ARG A NE     1 
ATOM   4312 C CZ     . ARG A 1 276 ? 39.27500  10.68000  14.58900 1.000 96.63746  ?  276 ARG A CZ     1 
ATOM   4313 N NH1    . ARG A 1 276 ? 38.49500  10.39700  15.62500 1.000 74.81868  ?  276 ARG A NH1    1 
ATOM   4314 N NH2    . ARG A 1 276 ? 39.06300  10.06000  13.42600 1.000 92.06885  ?  276 ARG A NH2    1 
ATOM   4315 H H      . ARG A 1 276 ? 37.43900  15.15200  16.16600 1.000 64.66705  ?  276 ARG A H      1 
ATOM   4316 H HA     . ARG A 1 276 ? 39.66700  15.90100  17.22900 1.000 67.29087  ?  276 ARG A HA     1 
ATOM   4317 H HB2    . ARG A 1 276 ? 39.34200  14.66300  14.71400 1.000 63.39834  ?  276 ARG A HB2    1 
ATOM   4318 H HB3    . ARG A 1 276 ? 40.74100  14.78400  15.45800 1.000 63.39834  ?  276 ARG A HB3    1 
ATOM   4319 H HG2    . ARG A 1 276 ? 39.55500  13.47500  17.21700 1.000 81.22809  ?  276 ARG A HG2    1 
ATOM   4320 H HG3    . ARG A 1 276 ? 38.67200  13.01000  15.98100 1.000 81.22809  ?  276 ARG A HG3    1 
ATOM   4321 H HD2    . ARG A 1 276 ? 41.44700  12.76200  15.73600 1.000 93.96409  ?  276 ARG A HD2    1 
ATOM   4322 H HD3    . ARG A 1 276 ? 40.69000  11.67800  16.61700 1.000 93.96409  ?  276 ARG A HD3    1 
ATOM   4323 H HE     . ARG A 1 276 ? 40.73900  11.70800  13.97800 1.000 108.36225 ?  276 ARG A HE     1 
ATOM   4324 H HH11   . ARG A 1 276 ? 38.62300  10.78900  16.38000 1.000 89.90019  ?  276 ARG A HH11   1 
ATOM   4325 H HH12   . ARG A 1 276 ? 37.86200  9.82100   15.54200 1.000 89.90019  ?  276 ARG A HH12   1 
ATOM   4326 H HH21   . ARG A 1 276 ? 39.56300  10.23400  12.74800 1.000 110.60039 ?  276 ARG A HH21   1 
ATOM   4327 H HH22   . ARG A 1 276 ? 38.42700  9.48600   13.35400 1.000 110.60039 ?  276 ARG A HH22   1 
ATOM   4328 N N      . ARG A 1 277 ? 38.90200  17.60500  14.62300 1.000 51.37076  ?  277 ARG A N      1 
ATOM   4329 C CA     . ARG A 1 277 ? 39.26600  18.75600  13.79300 1.000 52.65210  ?  277 ARG A CA     1 
ATOM   4330 C C      . ARG A 1 277 ? 38.72800  20.07900  14.32100 1.000 54.37080  ?  277 ARG A C      1 
ATOM   4331 O O      . ARG A 1 277 ? 39.00500  21.12600  13.71800 1.000 53.17235  ?  277 ARG A O      1 
ATOM   4332 C CB     . ARG A 1 277 ? 38.75600  18.54000  12.36200 1.000 53.14200  ?  277 ARG A CB     1 
ATOM   4333 C CG     . ARG A 1 277 ? 39.28900  17.28300  11.69200 0.000 55.00827  ?  277 ARG A CG     1 
ATOM   4334 C CD     . ARG A 1 277 ? 38.20700  16.57500  10.88800 0.000 52.34142  ?  277 ARG A CD     1 
ATOM   4335 N NE     . ARG A 1 277 ? 38.74900  15.89100  9.72000  0.000 50.66247  ?  277 ARG A NE     1 
ATOM   4336 C CZ     . ARG A 1 277 ? 38.03000  15.50200  8.67500  0.000 51.02423  ?  277 ARG A CZ     1 
ATOM   4337 N NH1    . ARG A 1 277 ? 36.72500  15.71200  8.61800  0.000 51.08213  ?  277 ARG A NH1    1 
ATOM   4338 N NH2    . ARG A 1 277 ? 38.63500  14.88600  7.66400  0.000 50.84021  ?  277 ARG A NH2    1 
ATOM   4339 H H      . ARG A 1 277 ? 38.15300  17.24000  14.40900 1.000 61.76269  ?  277 ARG A H      1 
ATOM   4340 H HA     . ARG A 1 277 ? 40.23300  18.82300  13.77300 1.000 63.30029  ?  277 ARG A HA     1 
ATOM   4341 H HB2    . ARG A 1 277 ? 37.78800  18.47400  12.38400 1.000 63.88816  ?  277 ARG A HB2    1 
ATOM   4342 H HB3    . ARG A 1 277 ? 39.02400  19.29900  11.82000 1.000 63.88816  ?  277 ARG A HB3    1 
ATOM   4343 H HG2    . ARG A 1 277 ? 40.01000  17.52100  11.08900 1.000 66.12770  ?  277 ARG A HG2    1 
ATOM   4344 H HG3    . ARG A 1 277 ? 39.61400  16.67000  12.37100 1.000 66.12770  ?  277 ARG A HG3    1 
ATOM   4345 H HD2    . ARG A 1 277 ? 37.77200  15.91500  11.45000 1.000 62.92747  ?  277 ARG A HD2    1 
ATOM   4346 H HD3    . ARG A 1 277 ? 37.55800  17.22800  10.58200 1.000 62.92747  ?  277 ARG A HD3    1 
ATOM   4347 H HE     . ARG A 1 277 ? 39.59400  15.72900  9.70700  1.000 60.91273  ?  277 ARG A HE     1 
ATOM   4348 H HH11   . ARG A 1 277 ? 36.32400  16.10900  9.26700  1.000 61.41633  ?  277 ARG A HH11   1 
ATOM   4349 H HH12   . ARG A 1 277 ? 36.27700  15.45100  7.93200  1.000 61.41633  ?  277 ARG A HH12   1 
ATOM   4350 H HH21   . ARG A 1 277 ? 39.48200  14.74500  7.69100  1.000 61.12603  ?  277 ARG A HH21   1 
ATOM   4351 H HH22   . ARG A 1 277 ? 38.17800  14.62900  6.98200  1.000 61.12603  ?  277 ARG A HH22   1 
ATOM   4352 N N      . HIS A 1 278 ? 37.97800  20.07300  15.42600 1.000 54.43747  ?  278 HIS A N      1 
ATOM   4353 C CA     . HIS A 1 278 ? 37.36700  21.28100  15.98100 1.000 55.82996  ?  278 HIS A CA     1 
ATOM   4354 C C      . HIS A 1 278 ? 37.62800  21.33500  17.47600 1.000 53.27725  ?  278 HIS A C      1 
ATOM   4355 O O      . HIS A 1 278 ? 36.76500  20.96100  18.28200 1.000 51.35500  ?  278 HIS A O      1 
ATOM   4356 C CB     . HIS A 1 278 ? 35.87300  21.31700  15.66700 1.000 52.23179  ?  278 HIS A CB     1 
ATOM   4357 C CG     . HIS A 1 278 ? 35.57700  21.48000  14.21100 1.000 53.54473  ?  278 HIS A CG     1 
ATOM   4358 N ND1    . HIS A 1 278 ? 35.53600  20.41500  13.33600 1.000 53.37095  ?  278 HIS A ND1    1 
ATOM   4359 C CD2    . HIS A 1 278 ? 35.33500  22.58700  13.47100 1.000 52.80066  ?  278 HIS A CD2    1 
ATOM   4360 C CE1    . HIS A 1 278 ? 35.27200  20.86000  12.11900 1.000 58.45915  ?  278 HIS A CE1    1 
ATOM   4361 N NE2    . HIS A 1 278 ? 35.14500  22.17500  12.17300 1.000 52.00584  ?  278 HIS A NE2    1 
ATOM   4362 H H      . HIS A 1 278 ? 37.80700  19.36400  15.88100 1.000 65.44274  ?  278 HIS A H      1 
ATOM   4363 H HA     . HIS A 1 278 ? 37.78800  22.06200  15.58900 1.000 67.11372  ?  278 HIS A HA     1 
ATOM   4364 H HB2    . HIS A 1 278 ? 35.47100  20.48500  15.96200 1.000 62.79592  ?  278 HIS A HB2    1 
ATOM   4365 H HB3    . HIS A 1 278 ? 35.47200  22.06500  16.13800 1.000 62.79592  ?  278 HIS A HB3    1 
ATOM   4366 H HD1    . HIS A 1 278 ? 35.66300  19.59100  13.54800 1.000 64.16291  ?  278 HIS A HD1    1 
ATOM   4367 H HD2    . HIS A 1 278 ? 35.30400  23.46300  13.78200 1.000 63.47856  ?  278 HIS A HD2    1 
ATOM   4368 H HE1    . HIS A 1 278 ? 35.18900  20.33600  11.35500 1.000 70.26875  ?  278 HIS A HE1    1 
ATOM   4369 N N      . PRO A 1 279 ? 38.79700  21.83000  17.88200 1.000 56.87163  ?  279 PRO A N      1 
ATOM   4370 C CA     . PRO A 1 279 ? 39.18500  21.73800  19.30200 1.000 58.97977  ?  279 PRO A CA     1 
ATOM   4371 C C      . PRO A 1 279 ? 38.27800  22.50300  20.23900 1.000 54.39777  ?  279 PRO A C      1 
ATOM   4372 O O      . PRO A 1 279 ? 38.25700  22.18900  21.44000 1.000 58.64521  ?  279 PRO A O      1 
ATOM   4373 C CB     . PRO A 1 279 ? 40.61400  22.31700  19.32000 1.000 58.31659  ?  279 PRO A CB     1 
ATOM   4374 C CG     . PRO A 1 279 ? 40.64300  23.26000  18.15500 1.000 63.76708  ?  279 PRO A CG     1 
ATOM   4375 C CD     . PRO A 1 279 ? 39.76300  22.63300  17.09400 1.000 70.50198  ?  279 PRO A CD     1 
ATOM   4376 H HA     . PRO A 1 279 ? 39.21000  20.80600  19.57100 1.000 70.89350  ?  279 PRO A HA     1 
ATOM   4377 H HB2    . PRO A 1 279 ? 40.77300  22.78600  20.15400 1.000 70.09768  ?  279 PRO A HB2    1 
ATOM   4378 H HB3    . PRO A 1 279 ? 41.26300  21.60500  19.21000 1.000 70.09768  ?  279 PRO A HB3    1 
ATOM   4379 H HG2    . PRO A 1 279 ? 40.29400  24.12400  18.42500 1.000 76.63826  ?  279 PRO A HG2    1 
ATOM   4380 H HG3    . PRO A 1 279 ? 41.55400  23.35500  17.83400 1.000 76.63826  ?  279 PRO A HG3    1 
ATOM   4381 H HD2    . PRO A 1 279 ? 39.30500  23.31500  16.57800 1.000 84.72014  ?  279 PRO A HD2    1 
ATOM   4382 H HD3    . PRO A 1 279 ? 40.28400  22.06500  16.50400 1.000 84.72014  ?  279 PRO A HD3    1 
ATOM   4383 N N      . ALA A 1 280 ? 37.53000  23.49200  19.74100 1.000 54.67493  ?  280 ALA A N      1 
ATOM   4384 C CA     . ALA A 1 280 ? 36.61700  24.27400  20.55900 1.000 55.96867  ?  280 ALA A CA     1 
ATOM   4385 C C      . ALA A 1 280 ? 35.20800  23.70700  20.57200 1.000 54.52776  ?  280 ALA A C      1 
ATOM   4386 O O      . ALA A 1 280 ? 34.26500  24.42600  20.91600 1.000 51.88894  ?  280 ALA A O      1 
ATOM   4387 C CB     . ALA A 1 280 ? 36.59100  25.73200  20.08000 1.000 55.88938  ?  280 ALA A CB     1 
ATOM   4388 H H      . ALA A 1 280 ? 37.53900  23.72900  18.91500 1.000 65.72768  ?  280 ALA A H      1 
ATOM   4389 H HA     . ALA A 1 280 ? 36.94700  24.26500  21.47100 1.000 67.28018  ?  280 ALA A HA     1 
ATOM   4390 H HB1    . ALA A 1 280 ? 35.98500  26.23800  20.64200 1.000 67.18502  ?  280 ALA A HB1    1 
ATOM   4391 H HB2    . ALA A 1 280 ? 37.48600  26.10100  20.14300 1.000 67.18502  ?  280 ALA A HB2    1 
ATOM   4392 H HB3    . ALA A 1 280 ? 36.28700  25.75700  19.15900 1.000 67.18502  ?  280 ALA A HB3    1 
ATOM   4393 N N      . HIS A 1 281 ? 35.05000  22.43200  20.22000 1.000 55.06077  ?  281 HIS A N      1 
ATOM   4394 C CA     . HIS A 1 281 ? 33.71800  21.84200  20.12800 1.000 50.27734  ?  281 HIS A CA     1 
ATOM   4395 C C      . HIS A 1 281 ? 33.04200  21.80300  21.49300 1.000 48.25447  ?  281 HIS A C      1 
ATOM   4396 O O      . HIS A 1 281 ? 33.69600  21.73500  22.53800 1.000 48.42719  ?  281 HIS A O      1 
ATOM   4397 C CB     . HIS A 1 281 ? 33.79900  20.41900  19.56300 1.000 46.66600  ?  281 HIS A CB     1 
ATOM   4398 C CG     . HIS A 1 281 ? 34.55900  19.46900  20.43400 1.000 46.44425  ?  281 HIS A CG     1 
ATOM   4399 N ND1    . HIS A 1 281 ? 34.02800  18.92400  21.58500 1.000 50.99340  ?  281 HIS A ND1    1 
ATOM   4400 C CD2    . HIS A 1 281 ? 35.80700  18.95600  20.31900 1.000 50.45410  ?  281 HIS A CD2    1 
ATOM   4401 C CE1    . HIS A 1 281 ? 34.91600  18.12500  22.14400 1.000 49.04967  ?  281 HIS A CE1    1 
ATOM   4402 N NE2    . HIS A 1 281 ? 36.00300  18.12000  21.38900 1.000 50.62163  ?  281 HIS A NE2    1 
ATOM   4403 H H      . HIS A 1 281 ? 35.69200  21.89200  20.03000 1.000 66.19069  ?  281 HIS A H      1 
ATOM   4404 H HA     . HIS A 1 281 ? 33.17700  22.38500  19.53300 1.000 60.45058  ?  281 HIS A HA     1 
ATOM   4405 H HB2    . HIS A 1 281 ? 32.89900  20.07200  19.46000 1.000 56.11697  ?  281 HIS A HB2    1 
ATOM   4406 H HB3    . HIS A 1 281 ? 34.24300  20.45100  18.70100 1.000 56.11697  ?  281 HIS A HB3    1 
ATOM   4407 H HD1    . HIS A 1 281 ? 33.24000  19.08200  21.89200 1.000 61.30985  ?  281 HIS A HD1    1 
ATOM   4408 H HD2    . HIS A 1 281 ? 36.41800  19.13700  19.64100 1.000 60.66268  ?  281 HIS A HD2    1 
ATOM   4409 H HE1    . HIS A 1 281 ? 34.79900  17.64700  22.93300 1.000 58.97738  ?  281 HIS A HE1    1 
ATOM   4410 N N      . SER A 1 282 ? 31.71200  21.83600  21.47100 1.000 43.06527  ?  282 SER A N      1 
ATOM   4411 C CA     . SER A 1 282 ? 30.95100  21.73700  22.70300 1.000 45.72949  ?  282 SER A CA     1 
ATOM   4412 C C      . SER A 1 282 ? 31.22000  20.40100  23.39700 1.000 43.06016  ?  282 SER A C      1 
ATOM   4413 O O      . SER A 1 282 ? 31.59100  19.40400  22.77400 1.000 40.57589  ?  282 SER A O      1 
ATOM   4414 C CB     . SER A 1 282 ? 29.45400  21.90600  22.41500 1.000 39.19919  ?  282 SER A CB     1 
ATOM   4415 O OG     . SER A 1 282 ? 28.96100  20.91000  21.54000 1.000 45.30865  ?  282 SER A OG     1 
ATOM   4416 H H      . SER A 1 282 ? 31.23400  21.91300  20.76000 1.000 51.79609  ?  282 SER A H      1 
ATOM   4417 H HA     . SER A 1 282 ? 31.21900  22.44400  23.31000 1.000 54.99315  ?  282 SER A HA     1 
ATOM   4418 H HB2    . SER A 1 282 ? 28.96900  21.85000  23.25300 1.000 47.15680  ?  282 SER A HB2    1 
ATOM   4419 H HB3    . SER A 1 282 ? 29.31300  22.77500  22.00800 1.000 47.15680  ?  282 SER A HB3    1 
ATOM   4420 H HG     . SER A 1 282 ? 28.14500  21.03700  21.39000 1.000 54.48815  ?  282 SER A HG     1 
ATOM   4421 N N      . GLN A 1 283 ? 31.05000  20.40100  24.71900 1.000 45.72221  ?  283 GLN A N      1 
ATOM   4422 C CA     . GLN A 1 283 ? 31.30500  19.23100  25.54900 1.000 45.11912  ?  283 GLN A CA     1 
ATOM   4423 C C      . GLN A 1 283 ? 30.01300  18.77000  26.22000 1.000 48.82880  ?  283 GLN A C      1 
ATOM   4424 O O      . GLN A 1 283 ? 29.00000  19.48700  26.19000 1.000 42.99941  ?  283 GLN A O      1 
ATOM   4425 C CB     . GLN A 1 283 ? 32.36100  19.54800  26.61300 1.000 53.38890  ?  283 GLN A CB     1 
ATOM   4426 C CG     . GLN A 1 283 ? 33.72100  19.97400  26.02700 1.000 55.19146  ?  283 GLN A CG     1 
ATOM   4427 C CD     . GLN A 1 283 ? 34.72100  18.81800  25.82800 1.000 67.30867  ?  283 GLN A CD     1 
ATOM   4428 O OE1    . GLN A 1 283 ? 35.80000  19.02600  25.25700 1.000 71.15377  ?  283 GLN A OE1    1 
ATOM   4429 N NE2    . GLN A 1 283 ? 34.37600  17.62000  26.28600 1.000 67.09995  ?  283 GLN A NE2    1 
ATOM   4430 H H      . GLN A 1 283 ? 30.78100  21.08400  25.16800 1.000 54.98442  ?  283 GLN A H      1 
ATOM   4431 H HA     . GLN A 1 283 ? 31.63500  18.51100  24.98900 1.000 54.26071  ?  283 GLN A HA     1 
ATOM   4432 H HB2    . GLN A 1 283 ? 32.03700  20.27400  27.16900 1.000 64.18445  ?  283 GLN A HB2    1 
ATOM   4433 H HB3    . GLN A 1 283 ? 32.50700  18.75600  27.15400 1.000 64.18445  ?  283 GLN A HB3    1 
ATOM   4434 H HG2    . GLN A 1 283 ? 33.57000  20.38200  25.16000 1.000 66.34753  ?  283 GLN A HG2    1 
ATOM   4435 H HG3    . GLN A 1 283 ? 34.13000  20.61500  26.62800 1.000 66.34753  ?  283 GLN A HG3    1 
ATOM   4436 H HE21   . GLN A 1 283 ? 33.61800  17.51100  26.67700 1.000 80.63771  ?  283 GLN A HE21   1 
ATOM   4437 H HE22   . GLN A 1 283 ? 34.91100  16.95400  26.19200 1.000 80.63771  ?  283 GLN A HE22   1 
ATOM   4438 N N      . PRO A 1 284 ? 30.00400  17.57300  26.81900 1.000 50.07301  ?  284 PRO A N      1 
ATOM   4439 C CA     . PRO A 1 284 ? 28.78700  17.12600  27.49400 1.000 43.47199  ?  284 PRO A CA     1 
ATOM   4440 C C      . PRO A 1 284 ? 28.47100  18.02800  28.65700 1.000 44.11225  ?  284 PRO A C      1 
ATOM   4441 O O      . PRO A 1 284 ? 29.36900  18.66200  29.23800 1.000 47.35813  ?  284 PRO A O      1 
ATOM   4442 C CB     . PRO A 1 284 ? 29.15000  15.70400  27.95700 1.000 46.66347  ?  284 PRO A CB     1 
ATOM   4443 C CG     . PRO A 1 284 ? 30.27200  15.27500  27.06200 1.000 50.55516  ?  284 PRO A CG     1 
ATOM   4444 C CD     . PRO A 1 284 ? 31.04800  16.53700  26.78800 1.000 46.76099  ?  284 PRO A CD     1 
ATOM   4445 H HA     . PRO A 1 284 ? 28.03200  17.09300  26.88500 1.000 52.28416  ?  284 PRO A HA     1 
ATOM   4446 H HB2    . PRO A 1 284 ? 29.43400  15.72200  28.88400 1.000 56.11394  ?  284 PRO A HB2    1 
ATOM   4447 H HB3    . PRO A 1 284 ? 28.38400  15.11800  27.85500 1.000 56.11394  ?  284 PRO A HB3    1 
ATOM   4448 H HG2    . PRO A 1 284 ? 30.82500  14.61900  27.51500 1.000 60.78396  ?  284 PRO A HG2    1 
ATOM   4449 H HG3    . PRO A 1 284 ? 29.91700  14.90000  26.24100 1.000 60.78396  ?  284 PRO A HG3    1 
ATOM   4450 H HD2    . PRO A 1 284 ? 31.71300  16.69300  27.47700 1.000 56.23096  ?  284 PRO A HD2    1 
ATOM   4451 H HD3    . PRO A 1 284 ? 31.47500  16.50000  25.91700 1.000 56.23096  ?  284 PRO A HD3    1 
ATOM   4452 N N      . PRO A 1 285 ? 27.19600  18.12300  29.04800 1.000 49.01215  ?  285 PRO A N      1 
ATOM   4453 C CA     . PRO A 1 285 ? 26.02800  17.39600  28.51300 1.000 48.23654  ?  285 PRO A CA     1 
ATOM   4454 C C      . PRO A 1 285 ? 25.34100  18.07100  27.32300 1.000 46.49893  ?  285 PRO A C      1 
ATOM   4455 O O      . PRO A 1 285 ? 24.45300  17.47700  26.73200 1.000 45.66808  ?  285 PRO A O      1 
ATOM   4456 C CB     . PRO A 1 285 ? 25.09900  17.33700  29.73800 1.000 51.32712  ?  285 PRO A CB     1 
ATOM   4457 C CG     . PRO A 1 285 ? 25.37100  18.63300  30.46600 1.000 49.84860  ?  285 PRO A CG     1 
ATOM   4458 C CD     . PRO A 1 285 ? 26.83600  18.96600  30.20700 1.000 54.12501  ?  285 PRO A CD     1 
ATOM   4459 H HA     . PRO A 1 285 ? 26.30800  16.50900  28.23800 1.000 58.00162  ?  285 PRO A HA     1 
ATOM   4460 H HB2    . PRO A 1 285 ? 24.17300  17.28300  29.45300 1.000 61.71031  ?  285 PRO A HB2    1 
ATOM   4461 H HB3    . PRO A 1 285 ? 25.32200  16.57100  30.29000 1.000 61.71031  ?  285 PRO A HB3    1 
ATOM   4462 H HG2    . PRO A 1 285 ? 24.79400  19.33000  30.11600 1.000 59.93609  ?  285 PRO A HG2    1 
ATOM   4463 H HG3    . PRO A 1 285 ? 25.20900  18.51300  31.41500 1.000 59.93609  ?  285 PRO A HG3    1 
ATOM   4464 H HD2    . PRO A 1 285 ? 26.94000  19.90600  29.99100 1.000 65.06778  ?  285 PRO A HD2    1 
ATOM   4465 H HD3    . PRO A 1 285 ? 27.38000  18.74000  30.97700 1.000 65.06778  ?  285 PRO A HD3    1 
ATOM   4466 N N      . VAL A 1 286 ? 25.73300  19.28800  26.92000 1.000 43.52790  ?  286 VAL A N      1 
ATOM   4467 C CA     . VAL A 1 286 ? 24.96700  19.99900  25.90500 1.000 44.13758  ?  286 VAL A CA     1 
ATOM   4468 C C      . VAL A 1 286 ? 25.33300  19.59000  24.48100 1.000 41.38961  ?  286 VAL A C      1 
ATOM   4469 O O      . VAL A 1 286 ? 24.55200  19.83600  23.55700 1.000 39.28602  ?  286 VAL A O      1 
ATOM   4470 C CB     . VAL A 1 286 ? 25.14100  21.52900  26.04700 1.000 44.21743  ?  286 VAL A CB     1 
ATOM   4471 C CG1    . VAL A 1 286 ? 24.66000  21.99400  27.40700 1.000 45.10494  ?  286 VAL A CG1    1 
ATOM   4472 C CG2    . VAL A 1 286 ? 26.59600  21.93700  25.81200 1.000 47.44398  ?  286 VAL A CG2    1 
ATOM   4473 H H      . VAL A 1 286 ? 26.42300  19.70900  27.21400 1.000 52.35124  ?  286 VAL A H      1 
ATOM   4474 H HA     . VAL A 1 286 ? 24.03600  19.77100  26.05100 1.000 53.08286  ?  286 VAL A HA     1 
ATOM   4475 H HB     . VAL A 1 286 ? 24.60100  21.96800  25.37100 1.000 53.17868  ?  286 VAL A HB     1 
ATOM   4476 H HG11   . VAL A 1 286 ? 24.72900  22.96000  27.45300 1.000 54.24369  ?  286 VAL A HG11   1 
ATOM   4477 H HG12   . VAL A 1 286 ? 23.73600  21.72200  27.52400 1.000 54.24369  ?  286 VAL A HG12   1 
ATOM   4478 H HG13   . VAL A 1 286 ? 25.21300  21.58900  28.09300 1.000 54.24369  ?  286 VAL A HG13   1 
ATOM   4479 H HG21   . VAL A 1 286 ? 26.69700  22.88000  26.01600 1.000 57.05054  ?  286 VAL A HG21   1 
ATOM   4480 H HG22   . VAL A 1 286 ? 27.16900  21.41100  26.39100 1.000 57.05054  ?  286 VAL A HG22   1 
ATOM   4481 H HG23   . VAL A 1 286 ? 26.82500  21.77300  24.88400 1.000 57.05054  ?  286 VAL A HG23   1 
ATOM   4482 N N      . SER A 1 287 ? 26.49800  18.97600  24.27900 1.000 45.28283  ?  287 SER A N      1 
ATOM   4483 C CA     . SER A 1 287 ? 26.94800  18.64800  22.93600 1.000 41.14165  ?  287 SER A CA     1 
ATOM   4484 C C      . SER A 1 287 ? 26.10300  17.52100  22.34000 1.000 40.53300  ?  287 SER A C      1 
ATOM   4485 O O      . SER A 1 287 ? 25.31600  16.87200  23.02000 1.000 41.68353  ?  287 SER A O      1 
ATOM   4486 C CB     . SER A 1 287 ? 28.42500  18.23300  22.94900 1.000 38.57264  ?  287 SER A CB     1 
ATOM   4487 O OG     . SER A 1 287 ? 28.58800  17.06300  23.73700 1.000 42.56397  ?  287 SER A OG     1 
ATOM   4488 H H      . SER A 1 287 ? 27.04100  18.74100  24.90300 1.000 54.45717  ?  287 SER A H      1 
ATOM   4489 H HA     . SER A 1 287 ? 26.85200  19.43400  22.37500 1.000 49.48775  ?  287 SER A HA     1 
ATOM   4490 H HB2    . SER A 1 287 ? 28.71400  18.05100  22.04100 1.000 46.40493  ?  287 SER A HB2    1 
ATOM   4491 H HB3    . SER A 1 287 ? 28.95500  18.95100  23.32800 1.000 46.40493  ?  287 SER A HB3    1 
ATOM   4492 H HG     . SER A 1 287 ? 29.39700  16.83700  23.75200 1.000 51.19453  ?  287 SER A HG     1 
ATOM   4493 N N      . LEU A 1 288 ? 26.30100  17.28900  21.04300 1.000 43.38003  ?  288 LEU A N      1 
ATOM   4494 C CA     A LEU A 1 288 ? 25.61000  16.18600  20.37500 0.320 41.20250  ?  288 LEU A CA     1 
ATOM   4495 C CA     B LEU A 1 288 ? 25.61300  16.18700  20.37200 0.680 42.19335  ?  288 LEU A CA     1 
ATOM   4496 C C      . LEU A 1 288 ? 26.07400  14.83100  20.90400 1.000 40.50591  ?  288 LEU A C      1 
ATOM   4497 O O      . LEU A 1 288 ? 25.27200  13.88800  20.97600 1.000 44.33949  ?  288 LEU A O      1 
ATOM   4498 C CB     A LEU A 1 288 ? 25.82100  16.27300  18.86400 0.320 41.82076  ?  288 LEU A CB     1 
ATOM   4499 C CB     B LEU A 1 288 ? 25.83700  16.26100  18.86200 0.680 44.87097  ?  288 LEU A CB     1 
ATOM   4500 C CG     A LEU A 1 288 ? 24.92000  15.41300  17.97100 0.320 48.85947  ?  288 LEU A CG     1 
ATOM   4501 C CG     B LEU A 1 288 ? 24.64400  16.68600  18.00700 0.680 47.99141  ?  288 LEU A CG     1 
ATOM   4502 C CD1    A LEU A 1 288 ? 23.46200  15.46400  18.41300 0.320 46.21121  ?  288 LEU A CD1    1 
ATOM   4503 C CD1    B LEU A 1 288 ? 25.03100  16.67000  16.53700 0.680 48.49677  ?  288 LEU A CD1    1 
ATOM   4504 C CD2    A LEU A 1 288 ? 25.04400  15.86000  16.52000 0.320 48.33004  ?  288 LEU A CD2    1 
ATOM   4505 C CD2    B LEU A 1 288 ? 23.41900  15.80400  18.24800 0.680 46.66819  ?  288 LEU A CD2    1 
ATOM   4506 H H      A LEU A 1 288 ? 26.82200  17.74700  20.53400 0.320 52.17380  ?  288 LEU A H      1 
ATOM   4507 H H      B LEU A 1 288 ? 26.82200  17.74800  20.53400 0.680 52.17380  ?  288 LEU A H      1 
ATOM   4508 H HA     A LEU A 1 288 ? 24.65800  16.26200  20.54600 0.320 49.56077  ?  288 LEU A HA     1 
ATOM   4509 H HA     B LEU A 1 288 ? 24.66100  16.27100  20.53800 0.680 50.74979  ?  288 LEU A HA     1 
ATOM   4510 H HB2    A LEU A 1 288 ? 25.68100  17.19500  18.59800 0.320 50.30268  ?  288 LEU A HB2    1 
ATOM   4511 H HB2    B LEU A 1 288 ? 26.54700  16.90000  18.69700 0.680 53.96293  ?  288 LEU A HB2    1 
ATOM   4512 H HB3    A LEU A 1 288 ? 26.73500  16.00800  18.67600 0.320 50.30268  ?  288 LEU A HB3    1 
ATOM   4513 H HB3    B LEU A 1 288 ? 26.10500  15.38000  18.55600 0.680 53.96293  ?  288 LEU A HB3    1 
ATOM   4514 H HG     A LEU A 1 288 ? 25.21000  14.49100  18.04800 0.320 58.74913  ?  288 LEU A HG     1 
ATOM   4515 H HG     B LEU A 1 288 ? 24.39300  17.58800  18.26100 0.680 57.70746  ?  288 LEU A HG     1 
ATOM   4516 H HD11   A LEU A 1 288 ? 22.91000  15.05800  17.72700 0.320 55.57122  ?  288 LEU A HD11   1 
ATOM   4517 H HD11   B LEU A 1 288 ? 24.27600  16.97300  16.00800 0.680 58.31390  ?  288 LEU A HD11   1 
ATOM   4518 H HD12   A LEU A 1 288 ? 23.36700  14.97500  19.24600 0.320 55.57122  ?  288 LEU A HD12   1 
ATOM   4519 H HD12   B LEU A 1 288 ? 25.78700  17.26200  16.40300 0.680 58.31390  ?  288 LEU A HD12   1 
ATOM   4520 H HD13   A LEU A 1 288 ? 23.20300  16.39000  18.54100 0.320 55.57122  ?  288 LEU A HD13   1 
ATOM   4521 H HD13   B LEU A 1 288 ? 25.27000  15.76500  16.28300 0.680 58.31390  ?  288 LEU A HD13   1 
ATOM   4522 H HD21   A LEU A 1 288 ? 24.64900  15.18400  15.94700 0.320 58.11382  ?  288 LEU A HD21   1 
ATOM   4523 H HD21   B LEU A 1 288 ? 22.79000  15.93200  17.52000 0.680 56.11960  ?  288 LEU A HD21   1 
ATOM   4524 H HD22   A LEU A 1 288 ? 24.57700  16.70300  16.40800 0.320 58.11382  ?  288 LEU A HD22   1 
ATOM   4525 H HD22   B LEU A 1 288 ? 23.70000  14.87700  18.28300 0.680 56.11960  ?  288 LEU A HD22   1 
ATOM   4526 H HD23   A LEU A 1 288 ? 25.98300  15.97000  16.30300 0.320 58.11382  ?  288 LEU A HD23   1 
ATOM   4527 H HD23   B LEU A 1 288 ? 23.00800  16.05800  19.08900 0.680 56.11960  ?  288 LEU A HD23   1 
ATOM   4528 N N      . ARG A 1 289 ? 27.34600  14.70800  21.27500 1.000 45.29495  ?  289 ARG A N      1 
ATOM   4529 C CA     . ARG A 1 289 ? 27.79900  13.49400  21.95200 1.000 40.41705  ?  289 ARG A CA     1 
ATOM   4530 C C      . ARG A 1 289 ? 27.11400  13.35400  23.30200 1.000 43.55772  ?  289 ARG A C      1 
ATOM   4531 O O      . ARG A 1 289 ? 26.71900  12.24100  23.70400 1.000 40.69973  ?  289 ARG A O      1 
ATOM   4532 C CB     . ARG A 1 289 ? 29.31300  13.51300  22.13600 1.000 44.68038  ?  289 ARG A CB     1 
ATOM   4533 C CG     . ARG A 1 289 ? 29.88300  12.20800  22.72500 1.000 40.64822  ?  289 ARG A CG     1 
ATOM   4534 C CD     . ARG A 1 289 ? 31.33000  12.37400  23.19200 1.000 42.32486  ?  289 ARG A CD     1 
ATOM   4535 N NE     . ARG A 1 289 ? 31.72900  11.29400  24.08100 1.000 42.03014  ?  289 ARG A NE     1 
ATOM   4536 C CZ     . ARG A 1 289 ? 32.29100  11.45100  25.27900 1.000 47.95401  ?  289 ARG A CZ     1 
ATOM   4537 N NH1    . ARG A 1 289 ? 32.55100  12.65300  25.77400 1.000 50.46057  ?  289 ARG A NH1    1 
ATOM   4538 N NH2    . ARG A 1 289 ? 32.60000  10.37300  25.99900 1.000 49.20145  ?  289 ARG A NH2    1 
ATOM   4539 H H      . ARG A 1 289 ? 27.95700  15.30000  21.15000 1.000 54.47171  ?  289 ARG A H      1 
ATOM   4540 H HA     . ARG A 1 289 ? 27.57800  12.72800  21.39900 1.000 48.61823  ?  289 ARG A HA     1 
ATOM   4541 H HB2    . ARG A 1 289 ? 29.73000  13.65400  21.27100 1.000 53.73422  ?  289 ARG A HB2    1 
ATOM   4542 H HB3    . ARG A 1 289 ? 29.54500  14.23700  22.73800 1.000 53.73422  ?  289 ARG A HB3    1 
ATOM   4543 H HG2    . ARG A 1 289 ? 29.34700  11.94200  23.48900 1.000 48.89563  ?  289 ARG A HG2    1 
ATOM   4544 H HG3    . ARG A 1 289 ? 29.86100  11.51500  22.04700 1.000 48.89563  ?  289 ARG A HG3    1 
ATOM   4545 H HD2    . ARG A 1 289 ? 31.91800  12.36900  22.42100 1.000 50.90761  ?  289 ARG A HD2    1 
ATOM   4546 H HD3    . ARG A 1 289 ? 31.41800  13.21300  23.67100 1.000 50.90761  ?  289 ARG A HD3    1 
ATOM   4547 H HE     . ARG A 1 289 ? 31.59200  10.48900  23.81100 1.000 50.55393  ?  289 ARG A HE     1 
ATOM   4548 H HH11   . ARG A 1 289 ? 32.35700  13.35700  25.31900 1.000 60.67045  ?  289 ARG A HH11   1 
ATOM   4549 H HH12   . ARG A 1 289 ? 32.91400  12.73000  26.54900 1.000 60.67045  ?  289 ARG A HH12   1 
ATOM   4550 H HH21   . ARG A 1 289 ? 32.43700  9.58800   25.68900 1.000 59.15951  ?  289 ARG A HH21   1 
ATOM   4551 H HH22   . ARG A 1 289 ? 32.96300  10.46300  26.77300 1.000 59.15951  ?  289 ARG A HH22   1 
ATOM   4552 N N      . GLY A 1 290 ? 26.94200  14.47500  24.00900 1.000 42.33590  ?  290 GLY A N      1 
ATOM   4553 C CA     . GLY A 1 290 ? 26.19800  14.43400  25.26100 1.000 43.69697  ?  290 GLY A CA     1 
ATOM   4554 C C      . GLY A 1 290 ? 24.79500  13.87600  25.07900 1.000 42.41858  ?  290 GLY A C      1 
ATOM   4555 O O      . GLY A 1 290 ? 24.29000  13.15700  25.93800 1.000 42.96828  ?  290 GLY A O      1 
ATOM   4556 H H      . GLY A 1 290 ? 27.24000  15.25100  23.78900 1.000 50.92085  ?  290 GLY A H      1 
ATOM   4557 H HA2    . GLY A 1 290 ? 26.67000  13.87300  25.89700 1.000 52.55414  ?  290 GLY A HA2    1 
ATOM   4558 H HA3    . GLY A 1 290 ? 26.12700  15.33100  25.62200 1.000 52.55414  ?  290 GLY A HA3    1 
ATOM   4559 N N      . GLN A 1 291 ? 24.15600  14.20000  23.95500 1.000 40.67194  ?  291 GLN A N      1 
ATOM   4560 C CA     . GLN A 1 291 ? 22.80700  13.70500  23.71400 1.000 39.37179  ?  291 GLN A CA     1 
ATOM   4561 C C      . GLN A 1 291 ? 22.78900  12.18300  23.62800 1.000 41.36408  ?  291 GLN A C      1 
ATOM   4562 O O      . GLN A 1 291 ? 21.89200  11.53000  24.18200 1.000 39.37520  ?  291 GLN A O      1 
ATOM   4563 C CB     . GLN A 1 291 ? 22.24200  14.32800  22.43900 1.000 40.63524  ?  291 GLN A CB     1 
ATOM   4564 C CG     . GLN A 1 291 ? 22.15800  15.85000  22.47300 1.000 43.15994  ?  291 GLN A CG     1 
ATOM   4565 C CD     . GLN A 1 291 ? 21.69100  16.37100  23.81400 1.000 47.01870  ?  291 GLN A CD     1 
ATOM   4566 O OE1    . GLN A 1 291 ? 20.50400  16.26400  24.15900 1.000 42.10117  ?  291 GLN A OE1    1 
ATOM   4567 N NE2    . GLN A 1 291 ? 22.61500  16.93200  24.59200 1.000 43.87658  ?  291 GLN A NE2    1 
ATOM   4568 H H      . GLN A 1 291 ? 24.47600  14.69400  23.32900 1.000 48.92410  ?  291 GLN A H      1 
ATOM   4569 H HA     . GLN A 1 291 ? 22.23700  13.97000  24.45300 1.000 47.36392  ?  291 GLN A HA     1 
ATOM   4570 H HB2    . GLN A 1 291 ? 22.81100  14.08100  21.69400 1.000 48.88005  ?  291 GLN A HB2    1 
ATOM   4571 H HB3    . GLN A 1 291 ? 21.34500  13.98700  22.29900 1.000 48.88005  ?  291 GLN A HB3    1 
ATOM   4572 H HG2    . GLN A 1 291 ? 23.03600  16.22000  22.29400 1.000 51.90969  ?  291 GLN A HG2    1 
ATOM   4573 H HG3    . GLN A 1 291 ? 21.52900  16.14800  21.79700 1.000 51.90969  ?  291 GLN A HG3    1 
ATOM   4574 H HE21   . GLN A 1 291 ? 23.43000  16.98300  24.32300 1.000 52.76967  ?  291 GLN A HE21   1 
ATOM   4575 H HE22   . GLN A 1 291 ? 22.39600  17.24300  25.36300 1.000 52.76967  ?  291 GLN A HE22   1 
ATOM   4576 N N      . LEU A 1 292 ? 23.76500  11.60200  22.92100 1.000 41.92103  ?  292 LEU A N      1 
ATOM   4577 C CA     . LEU A 1 292 ? 23.89700  10.15400  22.89300 1.000 44.97794  ?  292 LEU A CA     1 
ATOM   4578 C C      . LEU A 1 292 ? 24.15300  9.59600   24.28700 1.000 42.94953  ?  292 LEU A C      1 
ATOM   4579 O O      . LEU A 1 292 ? 23.73500  8.47600   24.59600 1.000 41.59496  ?  292 LEU A O      1 
ATOM   4580 C CB     . LEU A 1 292 ? 25.03900  9.74700   21.95400 1.000 44.97826  ?  292 LEU A CB     1 
ATOM   4581 C CG     . LEU A 1 292 ? 24.70100  9.62900   20.47800 1.000 48.09342  ?  292 LEU A CG     1 
ATOM   4582 C CD1    . LEU A 1 292 ? 25.93900  9.22900   19.67900 1.000 49.88601  ?  292 LEU A CD1    1 
ATOM   4583 C CD2    . LEU A 1 292 ? 23.58000  8.61200   20.27500 1.000 48.81150  ?  292 LEU A CD2    1 
ATOM   4584 H H      . LEU A 1 292 ? 24.35300  12.02300  22.45600 1.000 50.42301  ?  292 LEU A H      1 
ATOM   4585 H HA     . LEU A 1 292 ? 23.07200  9.77200   22.55400 1.000 54.09130  ?  292 LEU A HA     1 
ATOM   4586 H HB2    . LEU A 1 292 ? 25.74200  10.41100  22.03200 1.000 54.09169  ?  292 LEU A HB2    1 
ATOM   4587 H HB3    . LEU A 1 292 ? 25.36700  8.88100   22.24000 1.000 54.09169  ?  292 LEU A HB3    1 
ATOM   4588 H HG     . LEU A 1 292 ? 24.39600  10.48900  20.14800 1.000 57.82988  ?  292 LEU A HG     1 
ATOM   4589 H HD11   . LEU A 1 292 ? 25.72100  9.23400   18.73400 1.000 59.98098  ?  292 LEU A HD11   1 
ATOM   4590 H HD12   . LEU A 1 292 ? 26.65000  9.86400   19.85900 1.000 59.98098  ?  292 LEU A HD12   1 
ATOM   4591 H HD13   . LEU A 1 292 ? 26.21500  8.33900   19.94900 1.000 59.98098  ?  292 LEU A HD13   1 
ATOM   4592 H HD21   . LEU A 1 292 ? 23.57300  8.33000   19.34600 1.000 58.69157  ?  292 LEU A HD21   1 
ATOM   4593 H HD22   . LEU A 1 292 ? 23.73800  7.84800   20.85100 1.000 58.69157  ?  292 LEU A HD22   1 
ATOM   4594 H HD23   . LEU A 1 292 ? 22.73300  9.02600   20.50100 1.000 58.69157  ?  292 LEU A HD23   1 
ATOM   4595 N N      . LEU A 1 293 ? 24.85900  10.35100  25.12700 1.000 42.75641  ?  293 LEU A N      1 
ATOM   4596 C CA     . LEU A 1 293 ? 25.17300  9.88300   26.47100 1.000 45.56093  ?  293 LEU A CA     1 
ATOM   4597 C C      . LEU A 1 293 ? 23.96600  9.98400   27.39900 1.000 41.11292  ?  293 LEU A C      1 
ATOM   4598 O O      . LEU A 1 293 ? 23.85700  9.19800   28.34900 1.000 38.99729  ?  293 LEU A O      1 
ATOM   4599 C CB     . LEU A 1 293 ? 26.34900  10.68300  27.03400 1.000 45.31981  ?  293 LEU A CB     1 
ATOM   4600 C CG     . LEU A 1 293 ? 27.73200  10.40700  26.43000 1.000 53.11362  ?  293 LEU A CG     1 
ATOM   4601 C CD1    . LEU A 1 293 ? 28.80000  11.09900  27.26700 1.000 55.07221  ?  293 LEU A CD1    1 
ATOM   4602 C CD2    . LEU A 1 293 ? 28.03200  8.90700   26.31900 1.000 50.23266  ?  293 LEU A CD2    1 
ATOM   4603 H H      . LEU A 1 293 ? 25.16600  11.13300  24.94400 1.000 51.42546  ?  293 LEU A H      1 
ATOM   4604 H HA     . LEU A 1 293 ? 25.43900  8.95100   26.43300 1.000 54.79089  ?  293 LEU A HA     1 
ATOM   4605 H HB2    . LEU A 1 293 ? 26.16200  11.62500  26.89500 1.000 54.50154  ?  293 LEU A HB2    1 
ATOM   4606 H HB3    . LEU A 1 293 ? 26.41200  10.49400  27.98300 1.000 54.50154  ?  293 LEU A HB3    1 
ATOM   4607 H HG     . LEU A 1 293 ? 27.74600  10.76000  25.52700 1.000 63.85411  ?  293 LEU A HG     1 
ATOM   4608 H HD11   . LEU A 1 293 ? 29.67100  10.91600  26.88200 1.000 66.20442  ?  293 LEU A HD11   1 
ATOM   4609 H HD12   . LEU A 1 293 ? 28.63200  12.05400  27.26700 1.000 66.20442  ?  293 LEU A HD12   1 
ATOM   4610 H HD13   . LEU A 1 293 ? 28.76100  10.75600  28.17400 1.000 66.20442  ?  293 LEU A HD13   1 
ATOM   4611 H HD21   . LEU A 1 293 ? 28.92800  8.78900   25.96900 1.000 60.39696  ?  293 LEU A HD21   1 
ATOM   4612 H HD22   . LEU A 1 293 ? 27.96600  8.50600   27.20000 1.000 60.39696  ?  293 LEU A HD22   1 
ATOM   4613 H HD23   . LEU A 1 293 ? 27.38600  8.49900   25.72100 1.000 60.39696  ?  293 LEU A HD23   1 
ATOM   4614 N N      . TRP A 1 294 ? 23.06300  10.94900  27.15300 1.000 40.11964  ?  294 TRP A N      1 
ATOM   4615 C CA     . TRP A 1 294 ? 21.78800  10.94900  27.86500 1.000 40.96413  ?  294 TRP A CA     1 
ATOM   4616 C C      . TRP A 1 294 ? 21.03700  9.64100   27.61100 1.000 43.74702  ?  294 TRP A C      1 
ATOM   4617 O O      . TRP A 1 294 ? 20.49200  9.02800   28.53600 1.000 40.94771  ?  294 TRP A O      1 
ATOM   4618 C CB     . TRP A 1 294 ? 20.93600  12.13300  27.41300 1.000 44.23868  ?  294 TRP A CB     1 
ATOM   4619 C CG     . TRP A 1 294 ? 21.21200  13.41400  28.13300 1.000 42.92844  ?  294 TRP A CG     1 
ATOM   4620 C CD1    . TRP A 1 294 ? 21.73400  14.56000  27.59600 1.000 44.60993  ?  294 TRP A CD1    1 
ATOM   4621 C CD2    . TRP A 1 294 ? 20.97600  13.69100  29.51700 1.000 45.55427  ?  294 TRP A CD2    1 
ATOM   4622 N NE1    . TRP A 1 294 ? 21.83500  15.52900  28.55800 1.000 44.60590  ?  294 TRP A NE1    1 
ATOM   4623 C CE2    . TRP A 1 294 ? 21.38300  15.02300  29.74900 1.000 49.35307  ?  294 TRP A CE2    1 
ATOM   4624 C CE3    . TRP A 1 294 ? 20.46600  12.94600  30.58200 1.000 46.40074  ?  294 TRP A CE3    1 
ATOM   4625 C CZ2    . TRP A 1 294 ? 21.29200  15.62300  31.00400 1.000 53.22614  ?  294 TRP A CZ2    1 
ATOM   4626 C CZ3    . TRP A 1 294 ? 20.37400  13.54300  31.83300 1.000 50.29943  ?  294 TRP A CZ3    1 
ATOM   4627 C CH2    . TRP A 1 294 ? 20.78500  14.86800  32.03200 1.000 53.86847  ?  294 TRP A CH2    1 
ATOM   4628 H H      . TRP A 1 294 ? 23.16700  11.59400  26.59500 1.000 48.26134  ?  294 TRP A H      1 
ATOM   4629 H HA     . TRP A 1 294 ? 21.95700  11.03900  28.81600 1.000 49.27472  ?  294 TRP A HA     1 
ATOM   4630 H HB2    . TRP A 1 294 ? 21.09900  12.28700  26.47000 1.000 53.20419  ?  294 TRP A HB2    1 
ATOM   4631 H HB3    . TRP A 1 294 ? 20.00200  11.91300  27.55700 1.000 53.20419  ?  294 TRP A HB3    1 
ATOM   4632 H HD1    . TRP A 1 294 ? 21.98400  14.66500  26.70700 1.000 53.64969  ?  294 TRP A HD1    1 
ATOM   4633 H HE1    . TRP A 1 294 ? 22.13400  16.32600  28.43500 1.000 53.64485  ?  294 TRP A HE1    1 
ATOM   4634 H HE3    . TRP A 1 294 ? 20.19300  12.06600  30.45600 1.000 55.79866  ?  294 TRP A HE3    1 
ATOM   4635 H HZ2    . TRP A 1 294 ? 21.56500  16.50100  31.14000 1.000 63.98913  ?  294 TRP A HZ2    1 
ATOM   4636 H HZ3    . TRP A 1 294 ? 20.03400  13.05600  32.54800 1.000 60.47709  ?  294 TRP A HZ3    1 
ATOM   4637 H HH2    . TRP A 1 294 ? 20.71200  15.24400  32.88000 1.000 64.75993  ?  294 TRP A HH2    1 
ATOM   4638 N N      . ARG A 1 295 ? 21.00100  9.20700   26.35000 1.000 39.26015  ?  295 ARG A N      1 
ATOM   4639 C CA     . ARG A 1 295 ? 20.36900  7.93700   26.00400 1.000 44.98955  ?  295 ARG A CA     1 
ATOM   4640 C C      . ARG A 1 295 ? 21.03400  6.77900   26.73300 1.000 42.67022  ?  295 ARG A C      1 
ATOM   4641 O O      . ARG A 1 295 ? 20.35800  5.96600   27.37500 1.000 40.36049  ?  295 ARG A O      1 
ATOM   4642 C CB     . ARG A 1 295 ? 20.42700  7.74800   24.48700 1.000 41.10834  ?  295 ARG A CB     1 
ATOM   4643 C CG     . ARG A 1 295 ? 20.21100  6.33900   23.96600 1.000 42.95181  ?  295 ARG A CG     1 
ATOM   4644 C CD     . ARG A 1 295 ? 20.30800  6.33700   22.44700 1.000 40.54129  ?  295 ARG A CD     1 
ATOM   4645 N NE     . ARG A 1 295 ? 19.62400  5.21200   21.81800 1.000 44.28975  ?  295 ARG A NE     1 
ATOM   4646 C CZ     . ARG A 1 295 ? 20.20200  4.05800   21.49700 1.000 43.85452  ?  295 ARG A CZ     1 
ATOM   4647 N NH1    . ARG A 1 295 ? 21.46000  3.80600   21.80600 1.000 45.40986  ?  295 ARG A NH1    1 
ATOM   4648 N NH2    . ARG A 1 295 ? 19.49600  3.13200   20.84200 1.000 45.02900  ?  295 ARG A NH2    1 
ATOM   4649 H H      . ARG A 1 295 ? 21.33400  9.62800   25.67900 1.000 47.22996  ?  295 ARG A H      1 
ATOM   4650 H HA     . ARG A 1 295 ? 19.43700  7.95000   26.27300 1.000 54.10523  ?  295 ARG A HA     1 
ATOM   4651 H HB2    . ARG A 1 295 ? 19.74200  8.30600   24.08900 1.000 49.44778  ?  295 ARG A HB2    1 
ATOM   4652 H HB3    . ARG A 1 295 ? 21.30400  8.03100   24.18300 1.000 49.44778  ?  295 ARG A HB3    1 
ATOM   4653 H HG2    . ARG A 1 295 ? 20.89100  5.74800   24.32400 1.000 51.65994  ?  295 ARG A HG2    1 
ATOM   4654 H HG3    . ARG A 1 295 ? 19.33000  6.02500   24.22400 1.000 51.65994  ?  295 ARG A HG3    1 
ATOM   4655 H HD2    . ARG A 1 295 ? 19.90900  7.15300   22.10700 1.000 48.76731  ?  295 ARG A HD2    1 
ATOM   4656 H HD3    . ARG A 1 295 ? 21.24300  6.29400   22.19400 1.000 48.76731  ?  295 ARG A HD3    1 
ATOM   4657 H HE     . ARG A 1 295 ? 18.78700  5.30200   21.64200 1.000 53.26547  ?  295 ARG A HE     1 
ATOM   4658 H HH11   . ARG A 1 295 ? 21.92600  4.39500   22.22500 1.000 54.60960  ?  295 ARG A HH11   1 
ATOM   4659 H HH12   . ARG A 1 295 ? 21.81300  3.05300   21.58800 1.000 54.60960  ?  295 ARG A HH12   1 
ATOM   4660 H HH21   . ARG A 1 295 ? 18.67600  3.28500   20.63200 1.000 54.15257  ?  295 ARG A HH21   1 
ATOM   4661 H HH22   . ARG A 1 295 ? 19.86200  2.38300   20.63000 1.000 54.15257  ?  295 ARG A HH22   1 
ATOM   4662 N N      . GLU A 1 296 ? 22.36500  6.69800   26.65800 1.000 41.05432  ?  296 GLU A N      1 
ATOM   4663 C CA     . GLU A 1 296 ? 23.08100  5.61400   27.32900 1.000 42.85723  ?  296 GLU A CA     1 
ATOM   4664 C C      . GLU A 1 296 ? 22.89000  5.66800   28.83600 1.000 45.78853  ?  296 GLU A C      1 
ATOM   4665 O O      . GLU A 1 296 ? 22.70100  4.62800   29.48900 1.000 45.91265  ?  296 GLU A O      1 
ATOM   4666 C CB     . GLU A 1 296 ? 24.57500  5.67700   26.98600 1.000 43.91884  ?  296 GLU A CB     1 
ATOM   4667 C CG     . GLU A 1 296 ? 25.34400  4.40800   27.32600 1.000 41.84225  ?  296 GLU A CG     1 
ATOM   4668 C CD     . GLU A 1 296 ? 25.33600  3.38200   26.19300 1.000 43.23355  ?  296 GLU A CD     1 
ATOM   4669 O OE1    . GLU A 1 296 ? 24.73500  3.66500   25.12800 1.000 43.08407  ?  296 GLU A OE1    1 
ATOM   4670 O OE2    . GLU A 1 296 ? 25.94500  2.29100   26.36300 1.000 41.17672  -1 296 GLU A OE2    1 
ATOM   4671 H H      . GLU A 1 296 ? 22.86900  7.25000   26.23200 1.000 49.38296  ?  296 GLU A H      1 
ATOM   4672 H HA     . GLU A 1 296 ? 22.72800  4.76900   27.00800 1.000 51.54645  ?  296 GLU A HA     1 
ATOM   4673 H HB2    . GLU A 1 296 ? 24.66900  5.83200   26.03400 1.000 52.82037  ?  296 GLU A HB2    1 
ATOM   4674 H HB3    . GLU A 1 296 ? 24.97700  6.40700   27.48300 1.000 52.82037  ?  296 GLU A HB3    1 
ATOM   4675 H HG2    . GLU A 1 296 ? 26.26700  4.63900   27.51300 1.000 50.32847  ?  296 GLU A HG2    1 
ATOM   4676 H HG3    . GLU A 1 296 ? 24.94100  3.99500   28.10600 1.000 50.32847  ?  296 GLU A HG3    1 
ATOM   4677 N N      . PHE A 1 297 ? 22.95600  6.87200   29.41300 1.000 42.70682  ?  297 PHE A N      1 
ATOM   4678 C CA     . PHE A 1 297 ? 22.73700  7.02200   30.85400 1.000 46.21002  ?  297 PHE A CA     1 
ATOM   4679 C C      . PHE A 1 297 ? 21.39300  6.41300   31.27700 1.000 49.61134  ?  297 PHE A C      1 
ATOM   4680 O O      . PHE A 1 297 ? 21.32400  5.62600   32.23100 1.000 44.37444  ?  297 PHE A O      1 
ATOM   4681 C CB     . PHE A 1 297 ? 22.81000  8.50700   31.21300 1.000 45.31507  ?  297 PHE A CB     1 
ATOM   4682 C CG     . PHE A 1 297 ? 22.45700  8.81600   32.64000 1.000 48.78210  ?  297 PHE A CG     1 
ATOM   4683 C CD1    . PHE A 1 297 ? 23.04100  8.12400   33.68300 1.000 49.93743  ?  297 PHE A CD1    1 
ATOM   4684 C CD2    . PHE A 1 297 ? 21.54800  9.82800   32.93500 1.000 51.58064  ?  297 PHE A CD2    1 
ATOM   4685 C CE1    . PHE A 1 297 ? 22.71600  8.42000   34.99900 1.000 59.53921  ?  297 PHE A CE1    1 
ATOM   4686 C CE2    . PHE A 1 297 ? 21.22200  10.13000  34.24700 1.000 55.72969  ?  297 PHE A CE2    1 
ATOM   4687 C CZ     . PHE A 1 297 ? 21.80400  9.42400   35.28000 1.000 58.80234  ?  297 PHE A CZ     1 
ATOM   4688 H H      . PHE A 1 297 ? 23.12300  7.60700   28.99900 1.000 51.36596  ?  297 PHE A H      1 
ATOM   4689 H HA     . PHE A 1 297 ? 23.43200  6.55100   31.34100 1.000 55.56979  ?  297 PHE A HA     1 
ATOM   4690 H HB2    . PHE A 1 297 ? 23.71600  8.81800   31.06100 1.000 54.49585  ?  297 PHE A HB2    1 
ATOM   4691 H HB3    . PHE A 1 297 ? 22.19300  8.99300   30.64500 1.000 54.49585  ?  297 PHE A HB3    1 
ATOM   4692 H HD1    . PHE A 1 297 ? 23.65900  7.45300   33.50200 1.000 60.04268  ?  297 PHE A HD1    1 
ATOM   4693 H HD2    . PHE A 1 297 ? 21.15500  10.30700  32.24200 1.000 62.01454  ?  297 PHE A HD2    1 
ATOM   4694 H HE1    . PHE A 1 297 ? 23.11100  7.94300   35.69400 1.000 71.56482  ?  297 PHE A HE1    1 
ATOM   4695 H HE2    . PHE A 1 297 ? 20.61200  10.80700  34.43100 1.000 66.99340  ?  297 PHE A HE2    1 
ATOM   4696 H HZ     . PHE A 1 297 ? 21.58400  9.62100   36.16200 1.000 70.68058  ?  297 PHE A HZ     1 
ATOM   4697 N N      . PHE A 1 298 ? 20.31700  6.75600   30.56600 1.000 46.18888  ?  298 PHE A N      1 
ATOM   4698 C CA     . PHE A 1 298 ? 18.99200  6.28700   30.96800 1.000 47.98819  ?  298 PHE A CA     1 
ATOM   4699 C C      . PHE A 1 298 ? 18.81500  4.79400   30.70000 1.000 47.35219  ?  298 PHE A C      1 
ATOM   4700 O O      . PHE A 1 298 ? 18.11300  4.11000   31.45300 1.000 47.82657  ?  298 PHE A O      1 
ATOM   4701 C CB     . PHE A 1 298 ? 17.91000  7.08800   30.25200 1.000 43.00231  ?  298 PHE A CB     1 
ATOM   4702 C CG     . PHE A 1 298 ? 17.80100  8.52700   30.71100 1.000 41.25133  ?  298 PHE A CG     1 
ATOM   4703 C CD1    . PHE A 1 298 ? 18.06200  8.87900   32.02700 1.000 47.51658  ?  298 PHE A CD1    1 
ATOM   4704 C CD2    . PHE A 1 298 ? 17.42600  9.51800   29.82300 1.000 47.59670  ?  298 PHE A CD2    1 
ATOM   4705 C CE1    . PHE A 1 298 ? 17.95600  10.19300  32.44700 1.000 51.61035  ?  298 PHE A CE1    1 
ATOM   4706 C CE2    . PHE A 1 298 ? 17.32400  10.84800  30.24100 1.000 46.82002  ?  298 PHE A CE2    1 
ATOM   4707 C CZ     . PHE A 1 298 ? 17.58300  11.17700  31.55100 1.000 50.08920  ?  298 PHE A CZ     1 
ATOM   4708 H H      . PHE A 1 298 ? 20.32700  7.24900   29.86100 1.000 55.54443  ?  298 PHE A H      1 
ATOM   4709 H HA     . PHE A 1 298 ? 18.88800  6.43100   31.92200 1.000 57.70360  ?  298 PHE A HA     1 
ATOM   4710 H HB2    . PHE A 1 298 ? 18.10600  7.09600   29.30200 1.000 51.72055  ?  298 PHE A HB2    1 
ATOM   4711 H HB3    . PHE A 1 298 ? 17.05200  6.66300   30.41000 1.000 51.72055  ?  298 PHE A HB3    1 
ATOM   4712 H HD1    . PHE A 1 298 ? 18.31300  8.22200   32.63500 1.000 57.13766  ?  298 PHE A HD1    1 
ATOM   4713 H HD2    . PHE A 1 298 ? 17.24100  9.29700   28.93900 1.000 57.23381  ?  298 PHE A HD2    1 
ATOM   4714 H HE1    . PHE A 1 298 ? 18.13500  10.41400  33.33300 1.000 62.05019  ?  298 PHE A HE1    1 
ATOM   4715 H HE2    . PHE A 1 298 ? 17.08200  11.51000  29.63400 1.000 56.30180  ?  298 PHE A HE2    1 
ATOM   4716 H HZ     . PHE A 1 298 ? 17.50700  12.06000  31.83400 1.000 60.22481  ?  298 PHE A HZ     1 
ATOM   4717 N N      . TYR A 1 299 ? 19.43100  4.27000   29.64600 1.000 40.73405  ?  299 TYR A N      1 
ATOM   4718 C CA     . TYR A 1 299 ? 19.40900  2.82100   29.44800 1.000 47.44730  ?  299 TYR A CA     1 
ATOM   4719 C C      . TYR A 1 299 ? 20.12100  2.10100   30.58200 1.000 48.18182  ?  299 TYR A C      1 
ATOM   4720 O O      . TYR A 1 299 ? 19.64000  1.07700   31.07900 1.000 43.61549  ?  299 TYR A O      1 
ATOM   4721 C CB     . TYR A 1 299 ? 20.04600  2.46000   28.10800 1.000 46.69016  ?  299 TYR A CB     1 
ATOM   4722 C CG     . TYR A 1 299 ? 19.05200  2.19400   27.00300 1.000 47.09722  ?  299 TYR A CG     1 
ATOM   4723 C CD1    . TYR A 1 299 ? 18.47000  3.23200   26.30300 1.000 46.30512  ?  299 TYR A CD1    1 
ATOM   4724 C CD2    . TYR A 1 299 ? 18.69000  0.88600   26.66700 1.000 52.60399  ?  299 TYR A CD2    1 
ATOM   4725 C CE1    . TYR A 1 299 ? 17.55600  2.99300   25.29100 1.000 48.26814  ?  299 TYR A CE1    1 
ATOM   4726 C CE2    . TYR A 1 299 ? 17.76700  0.63300   25.66500 1.000 45.18616  ?  299 TYR A CE2    1 
ATOM   4727 C CZ     . TYR A 1 299 ? 17.21000  1.69100   24.97900 1.000 46.74025  ?  299 TYR A CZ     1 
ATOM   4728 O OH     . TYR A 1 299 ? 16.29700  1.45200   23.97300 1.000 50.72155  ?  299 TYR A OH     1 
ATOM   4729 H H      . TYR A 1 299 ? 19.85700  4.71500   29.04600 1.000 48.99863  ?  299 TYR A H      1 
ATOM   4730 H HA     . TYR A 1 299 ? 18.48500  2.52500   29.43200 1.000 57.05453  ?  299 TYR A HA     1 
ATOM   4731 H HB2    . TYR A 1 299 ? 20.61100  3.19500   27.82400 1.000 56.14596  ?  299 TYR A HB2    1 
ATOM   4732 H HB3    . TYR A 1 299 ? 20.57900  1.65700   28.22300 1.000 56.14596  ?  299 TYR A HB3    1 
ATOM   4733 H HD1    . TYR A 1 299 ? 18.69500  4.10900   26.51600 1.000 55.68391  ?  299 TYR A HD1    1 
ATOM   4734 H HD2    . TYR A 1 299 ? 19.07500  0.17300   27.12400 1.000 63.24256  ?  299 TYR A HD2    1 
ATOM   4735 H HE1    . TYR A 1 299 ? 17.17800  3.70300   24.82400 1.000 58.03953  ?  299 TYR A HE1    1 
ATOM   4736 H HE2    . TYR A 1 299 ? 17.52600  -0.24100  25.45700 1.000 54.34116  ?  299 TYR A HE2    1 
ATOM   4737 H HH     . TYR A 1 299 ? 16.16300  0.62600   23.89700 1.000 60.98363  ?  299 TYR A HH     1 
ATOM   4738 N N      . THR A 1 300 ? 21.27400  2.62600   31.00700 1.000 42.92198  ?  300 THR A N      1 
ATOM   4739 C CA     . THR A 1 300 ? 22.06000  1.96500   32.04700 1.000 47.01011  ?  300 THR A CA     1 
ATOM   4740 C C      . THR A 1 300 ? 21.31800  1.95400   33.38000 1.000 52.39461  ?  300 THR A C      1 
ATOM   4741 O O      . THR A 1 300 ? 21.27800  0.92800   34.07000 1.000 53.80577  ?  300 THR A O      1 
ATOM   4742 C CB     . THR A 1 300 ? 23.42100  2.65700   32.19600 1.000 45.33163  ?  300 THR A CB     1 
ATOM   4743 O OG1    . THR A 1 300 ? 24.13900  2.58100   30.96200 1.000 48.66104  ?  300 THR A OG1    1 
ATOM   4744 C CG2    . THR A 1 300 ? 24.24600  2.01100   33.31000 1.000 47.51082  ?  300 THR A CG2    1 
ATOM   4745 H H      . THR A 1 300 ? 21.61800  3.35700   30.71200 1.000 51.62414  ?  300 THR A H      1 
ATOM   4746 H HA     . THR A 1 300 ? 22.21400  1.04500   31.78200 1.000 56.52990  ?  300 THR A HA     1 
ATOM   4747 H HB     . THR A 1 300 ? 23.28100  3.58800   32.42900 1.000 54.51573  ?  300 THR A HB     1 
ATOM   4748 H HG1    . THR A 1 300 ? 24.87300  2.98200   31.03100 1.000 58.51101  ?  300 THR A HG1    1 
ATOM   4749 H HG21   . THR A 1 300 ? 25.16500  2.31700   33.26200 1.000 57.13076  ?  300 THR A HG21   1 
ATOM   4750 H HG22   . THR A 1 300 ? 23.88000  2.25100   34.17500 1.000 57.13076  ?  300 THR A HG22   1 
ATOM   4751 H HG23   . THR A 1 300 ? 24.23000  1.04600   33.21800 1.000 57.13076  ?  300 THR A HG23   1 
ATOM   4752 N N      . VAL A 1 301 ? 20.73600  3.09500   33.76400 1.000 52.06414  ?  301 VAL A N      1 
ATOM   4753 C CA     A VAL A 1 301 ? 20.01000  3.16900   35.02700 0.660 59.39842  ?  301 VAL A CA     1 
ATOM   4754 C CA     B VAL A 1 301 ? 20.01600  3.15900   35.03100 0.340 59.26735  ?  301 VAL A CA     1 
ATOM   4755 C C      . VAL A 1 301 ? 18.71200  2.37200   34.94700 1.000 57.93461  ?  301 VAL A C      1 
ATOM   4756 O O      . VAL A 1 301 ? 18.33200  1.67800   35.89500 1.000 58.10628  ?  301 VAL A O      1 
ATOM   4757 C CB     A VAL A 1 301 ? 19.74200  4.64000   35.40300 0.660 60.73253  ?  301 VAL A CB     1 
ATOM   4758 C CB     B VAL A 1 301 ? 19.77600  4.62700   35.43500 0.340 60.73004  ?  301 VAL A CB     1 
ATOM   4759 C CG1    A VAL A 1 301 ? 18.92900  4.72300   36.68900 0.660 67.21358  ?  301 VAL A CG1    1 
ATOM   4760 C CG1    B VAL A 1 301 ? 18.62000  5.23200   34.64900 0.340 59.57158  ?  301 VAL A CG1    1 
ATOM   4761 C CG2    A VAL A 1 301 ? 21.04600  5.39900   35.53900 0.660 58.67301  ?  301 VAL A CG2    1 
ATOM   4762 C CG2    B VAL A 1 301 ? 19.51900  4.72700   36.93400 0.340 68.86638  ?  301 VAL A CG2    1 
ATOM   4763 H H      A VAL A 1 301 ? 20.74900  3.82800   33.31500 0.660 62.59473  ?  301 VAL A H      1 
ATOM   4764 H H      B VAL A 1 301 ? 20.74600  3.82900   33.31600 0.340 62.59473  ?  301 VAL A H      1 
ATOM   4765 H HA     A VAL A 1 301 ? 20.56100  2.77300   35.72000 0.660 71.39588  ?  301 VAL A HA     1 
ATOM   4766 H HA     B VAL A 1 301 ? 20.56300  2.74800   35.71800 0.340 71.23858  ?  301 VAL A HA     1 
ATOM   4767 H HB     A VAL A 1 301 ? 19.22600  5.05700   34.69500 0.660 72.99681  ?  301 VAL A HB     1 
ATOM   4768 H HB     B VAL A 1 301 ? 20.57200  5.14000   35.22500 0.340 72.99382  ?  301 VAL A HB     1 
ATOM   4769 H HG11   A VAL A 1 301 ? 18.92600  5.64100   37.00200 0.660 80.77406  ?  301 VAL A HG11   1 
ATOM   4770 H HG11   B VAL A 1 301 ? 18.64900  6.19700   34.73700 0.340 71.60366  ?  301 VAL A HG11   1 
ATOM   4771 H HG12   A VAL A 1 301 ? 18.02200  4.43100   36.50900 0.660 80.77406  ?  301 VAL A HG12   1 
ATOM   4772 H HG12   B VAL A 1 301 ? 18.70700  4.98100   33.71600 0.340 71.60366  ?  301 VAL A HG12   1 
ATOM   4773 H HG13   A VAL A 1 301 ? 19.33500  4.14700   37.35700 0.660 80.77406  ?  301 VAL A HG13   1 
ATOM   4774 H HG13   B VAL A 1 301 ? 17.78400  4.89300   35.00600 0.340 71.60366  ?  301 VAL A HG13   1 
ATOM   4775 H HG21   A VAL A 1 301 ? 20.85400  6.31100   35.80600 0.660 70.52538  ?  301 VAL A HG21   1 
ATOM   4776 H HG21   B VAL A 1 301 ? 19.37600  5.65700   37.16900 0.340 82.75743  ?  301 VAL A HG21   1 
ATOM   4777 H HG22   A VAL A 1 301 ? 21.59500  4.96600   36.21100 0.660 70.52538  ?  301 VAL A HG22   1 
ATOM   4778 H HG22   B VAL A 1 301 ? 18.73100  4.20500   37.15400 0.340 82.75743  ?  301 VAL A HG22   1 
ATOM   4779 H HG23   A VAL A 1 301 ? 21.50400  5.39400   34.68400 0.660 70.52538  ?  301 VAL A HG23   1 
ATOM   4780 H HG23   B VAL A 1 301 ? 20.28900  4.38000   37.41000 0.340 82.75743  ?  301 VAL A HG23   1 
ATOM   4781 N N      . GLY A 1 302 ? 18.01100  2.46300   33.81500 1.000 55.51777  ?  302 GLY A N      1 
ATOM   4782 C CA     . GLY A 1 302 ? 16.72600  1.79800   33.69700 1.000 59.47205  ?  302 GLY A CA     1 
ATOM   4783 C C      . GLY A 1 302 ? 16.83100  0.28200   33.71500 1.000 60.91890  ?  302 GLY A C      1 
ATOM   4784 O O      . GLY A 1 302 ? 16.01000  -0.39900  34.33900 1.000 60.69170  ?  302 GLY A O      1 
ATOM   4785 H H      . GLY A 1 302 ? 18.25800  2.89800   33.11600 1.000 66.73910  ?  302 GLY A H      1 
ATOM   4786 H HA2    . GLY A 1 302 ? 16.15800  2.07000   34.43400 1.000 71.48423  ?  302 GLY A HA2    1 
ATOM   4787 H HA3    . GLY A 1 302 ? 16.30800  2.06100   32.86200 1.000 71.48423  ?  302 GLY A HA3    1 
ATOM   4788 N N      . SER A 1 303 ? 17.83200  -0.26800  33.03200 1.000 58.87992  ?  303 SER A N      1 
ATOM   4789 C CA     . SER A 1 303 ? 17.93100  -1.71700  32.89300 1.000 60.40128  ?  303 SER A CA     1 
ATOM   4790 C C      . SER A 1 303 ? 18.44500  -2.39300  34.15200 1.000 63.91581  ?  303 SER A C      1 
ATOM   4791 O O      . SER A 1 303 ? 18.23900  -3.59800  34.31200 1.000 63.07338  ?  303 SER A O      1 
ATOM   4792 C CB     . SER A 1 303 ? 18.84000  -2.07600  31.71200 1.000 58.67527  ?  303 SER A CB     1 
ATOM   4793 O OG     . SER A 1 303 ? 20.19600  -1.76300  31.99200 1.000 62.36380  ?  303 SER A OG     1 
ATOM   4794 H H      . SER A 1 303 ? 18.46100  0.17200   32.64300 1.000 70.77367  ?  303 SER A H      1 
ATOM   4795 H HA     . SER A 1 303 ? 17.04700  -2.06900  32.70700 1.000 72.59930  ?  303 SER A HA     1 
ATOM   4796 H HB2    . SER A 1 303 ? 18.76600  -3.02700  31.53600 1.000 70.52810  ?  303 SER A HB2    1 
ATOM   4797 H HB3    . SER A 1 303 ? 18.55600  -1.57200  30.93300 1.000 70.52810  ?  303 SER A HB3    1 
ATOM   4798 H HG     . SER A 1 303 ? 20.68200  -1.98900  31.34500 1.000 74.95433  ?  303 SER A HG     1 
ATOM   4799 N N      . THR A 1 304 ? 19.09200  -1.65100  35.05000 1.000 62.25111  ?  304 THR A N      1 
ATOM   4800 C CA     . THR A 1 304 ? 19.68500  -2.22100  36.25400 1.000 68.26386  ?  304 THR A CA     1 
ATOM   4801 C C      . THR A 1 304 ? 18.99300  -1.76100  37.53200 1.000 69.98273  ?  304 THR A C      1 
ATOM   4802 O O      . THR A 1 304 ? 19.45100  -2.10100  38.62500 1.000 66.05116  ?  304 THR A O      1 
ATOM   4803 C CB     . THR A 1 304 ? 21.18000  -1.87000  36.31800 1.000 67.97165  ?  304 THR A CB     1 
ATOM   4804 O OG1    . THR A 1 304 ? 21.34300  -0.47200  36.60300 1.000 63.80978  ?  304 THR A OG1    1 
ATOM   4805 C CG2    . THR A 1 304 ? 21.86000  -2.19100  34.99000 1.000 62.21347  ?  304 THR A CG2    1 
ATOM   4806 H H      . THR A 1 304 ? 19.20100  -0.80100  34.98000 1.000 74.81910  ?  304 THR A H      1 
ATOM   4807 H HA     . THR A 1 304 ? 19.60600  -3.18700  36.21100 1.000 82.03440  ?  304 THR A HA     1 
ATOM   4808 H HB     . THR A 1 304 ? 21.60100  -2.39300  37.01800 1.000 81.68375  ?  304 THR A HB     1 
ATOM   4809 H HG1    . THR A 1 304 ? 22.16000  -0.28200  36.64900 1.000 76.68951  ?  304 THR A HG1    1 
ATOM   4810 H HG21   . THR A 1 304 ? 22.81400  -2.02800  35.05800 1.000 74.77393  ?  304 THR A HG21   1 
ATOM   4811 H HG22   . THR A 1 304 ? 21.71600  -3.12300  34.76000 1.000 74.77393  ?  304 THR A HG22   1 
ATOM   4812 H HG23   . THR A 1 304 ? 21.49400  -1.63300  34.28600 1.000 74.77393  ?  304 THR A HG23   1 
ATOM   4813 N N      . THR A 1 305 ? 17.90800  -1.00400  37.41800 1.000 77.64048  ?  305 THR A N      1 
ATOM   4814 C CA     . THR A 1 305 ? 17.15800  -0.51700  38.57300 1.000 84.24452  ?  305 THR A CA     1 
ATOM   4815 C C      . THR A 1 305 ? 15.85300  -1.28800  38.67700 1.000 76.37100  ?  305 THR A C      1 
ATOM   4816 O O      . THR A 1 305 ? 14.98900  -1.14500  37.80000 1.000 79.30372  ?  305 THR A O      1 
ATOM   4817 C CB     . THR A 1 305 ? 16.88900  0.98500   38.43600 1.000 89.31987  ?  305 THR A CB     1 
ATOM   4818 O OG1    . THR A 1 305 ? 18.10000  1.71000   38.70700 1.000 86.32219  ?  305 THR A OG1    1 
ATOM   4819 C CG2    . THR A 1 305 ? 15.79400  1.44100   39.40000 1.000 95.08888  ?  305 THR A CG2    1 
ATOM   4820 H H      . THR A 1 305 ? 17.57700  -0.75200  36.66600 1.000 93.28635  ?  305 THR A H      1 
ATOM   4821 H HA     . THR A 1 305 ? 17.67000  -0.66300  39.38400 1.000 101.21120 ?  305 THR A HA     1 
ATOM   4822 H HB     . THR A 1 305 ? 16.58500  1.17600   37.53500 1.000 107.30161 ?  305 THR A HB     1 
ATOM   4823 H HG1    . THR A 1 305 ? 17.95900  2.53600   38.65000 1.000 103.70439 ?  305 THR A HG1    1 
ATOM   4824 H HG21   . THR A 1 305 ? 15.65300  2.39700   39.31300 1.000 114.22443 ?  305 THR A HG21   1 
ATOM   4825 H HG22   . THR A 1 305 ? 14.96400  0.98200   39.20000 1.000 114.22443 ?  305 THR A HG22   1 
ATOM   4826 H HG23   . THR A 1 305 ? 16.05200  1.24200   40.31300 1.000 114.22443 ?  305 THR A HG23   1 
ATOM   4827 N N      . PRO A 1 306 ? 15.65500  -2.11600  39.71900 1.000 83.68781  ?  306 PRO A N      1 
ATOM   4828 C CA     . PRO A 1 306 ? 14.42600  -2.92300  39.78600 1.000 89.05796  ?  306 PRO A CA     1 
ATOM   4829 C C      . PRO A 1 306 ? 13.14800  -2.09600  39.75400 1.000 95.79060  ?  306 PRO A C      1 
ATOM   4830 O O      . PRO A 1 306 ? 12.31700  -2.27200  38.85600 1.000 99.27966  ?  306 PRO A O      1 
ATOM   4831 C CB     . PRO A 1 306 ? 14.57400  -3.67400  41.12000 1.000 90.39387  ?  306 PRO A CB     1 
ATOM   4832 C CG     . PRO A 1 306 ? 16.04300  -3.72300  41.36500 1.000 89.55148  ?  306 PRO A CG     1 
ATOM   4833 C CD     . PRO A 1 306 ? 16.58000  -2.42400  40.82400 1.000 78.10974  ?  306 PRO A CD     1 
ATOM   4834 H HA     . PRO A 1 306 ? 14.40900  -3.55200  39.04800 1.000 106.98732 ?  306 PRO A HA     1 
ATOM   4835 H HB2    . PRO A 1 306 ? 14.11900  -3.18800  41.82600 1.000 108.59042 ?  306 PRO A HB2    1 
ATOM   4836 H HB3    . PRO A 1 306 ? 14.20400  -4.56700  41.04000 1.000 108.59042 ?  306 PRO A HB3    1 
ATOM   4837 H HG2    . PRO A 1 306 ? 16.21600  -3.79900  42.31700 1.000 107.57955 ?  306 PRO A HG2    1 
ATOM   4838 H HG3    . PRO A 1 306 ? 16.43000  -4.47900  40.89700 1.000 107.57955 ?  306 PRO A HG3    1 
ATOM   4839 H HD2    . PRO A 1 306 ? 16.55500  -1.73000  41.50100 1.000 93.84946  ?  306 PRO A HD2    1 
ATOM   4840 H HD3    . PRO A 1 306 ? 17.48600  -2.53500  40.49600 1.000 93.84946  ?  306 PRO A HD3    1 
ATOM   4841 N N      . ASN A 1 307 ? 12.97900  -1.19000  40.71900 1.000 98.73593  ?  307 ASN A N      1 
ATOM   4842 C CA     . ASN A 1 307 ? 11.79100  -0.33400  40.77700 1.000 97.58530  ?  307 ASN A CA     1 
ATOM   4843 C C      . ASN A 1 307 ? 12.09100  0.98400   40.06200 1.000 83.43253  ?  307 ASN A C      1 
ATOM   4844 O O      . ASN A 1 307 ? 12.12100  2.06600   40.64800 1.000 91.61549  ?  307 ASN A O      1 
ATOM   4845 C CB     . ASN A 1 307 ? 11.36200  -0.11200  42.22400 1.000 95.41018  ?  307 ASN A CB     1 
ATOM   4846 C CG     . ASN A 1 307 ? 10.59800  -1.29200  42.79200 1.000 90.00573  ?  307 ASN A CG     1 
ATOM   4847 O OD1    . ASN A 1 307 ? 9.46900   -1.56600  42.39100 1.000 87.31102  ?  307 ASN A OD1    1 
ATOM   4848 N ND2    . ASN A 1 307 ? 11.21400  -2.00400  43.73900 1.000 87.44714  ?  307 ASN A ND2    1 
ATOM   4849 H H      . ASN A 1 307 ? 13.54100  -1.05000  41.35500 1.000 118.60089 ?  307 ASN A H      1 
ATOM   4850 H HA     . ASN A 1 307 ? 11.05900  -0.77400  40.31600 1.000 117.22013 ?  307 ASN A HA     1 
ATOM   4851 H HB2    . ASN A 1 307 ? 12.15200  0.02700   42.77000 1.000 114.60999 ?  307 ASN A HB2    1 
ATOM   4852 H HB3    . ASN A 1 307 ? 10.78700  0.66800   42.26800 1.000 114.60999 ?  307 ASN A HB3    1 
ATOM   4853 H HD21   . ASN A 1 307 ? 12.00400  -1.78400  43.99700 1.000 105.05433 ?  307 ASN A HD21   1 
ATOM   4854 H HD22   . ASN A 1 307 ? 10.82000  -2.68300  44.09100 1.000 105.05433 ?  307 ASN A HD22   1 
ATOM   4855 N N      . PHE A 1 308 ? 12.30800  0.86100   38.75200 1.000 89.15877  ?  308 PHE A N      1 
ATOM   4856 C CA     . PHE A 1 308 ? 12.72800  2.00700   37.95300 1.000 85.75841  ?  308 PHE A CA     1 
ATOM   4857 C C      . PHE A 1 308 ? 11.63400  3.06400   37.85800 1.000 87.40054  ?  308 PHE A C      1 
ATOM   4858 O O      . PHE A 1 308 ? 11.92200  4.26100   37.83500 1.000 82.15465  ?  308 PHE A O      1 
ATOM   4859 C CB     . PHE A 1 308 ? 13.15400  1.53500   36.56200 1.000 88.00947  ?  308 PHE A CB     1 
ATOM   4860 C CG     . PHE A 1 308 ? 13.31300  2.64300   35.56000 1.000 75.17656  ?  308 PHE A CG     1 
ATOM   4861 C CD1    . PHE A 1 308 ? 14.24000  3.65200   35.76000 1.000 77.69932  ?  308 PHE A CD1    1 
ATOM   4862 C CD2    . PHE A 1 308 ? 12.53700  2.66900   34.41100 1.000 76.31704  ?  308 PHE A CD2    1 
ATOM   4863 C CE1    . PHE A 1 308 ? 14.38500  4.67300   34.83500 1.000 74.43902  ?  308 PHE A CE1    1 
ATOM   4864 C CE2    . PHE A 1 308 ? 12.67800  3.68300   33.48400 1.000 74.12331  ?  308 PHE A CE2    1 
ATOM   4865 C CZ     . PHE A 1 308 ? 13.60500  4.68800   33.69400 1.000 70.64671  ?  308 PHE A CZ     1 
ATOM   4866 H H      . PHE A 1 308 ? 12.22000  0.13100   38.30700 1.000 107.10829 ?  308 PHE A H      1 
ATOM   4867 H HA     . PHE A 1 308 ? 13.49300  2.42300   38.38000 1.000 103.02786 ?  308 PHE A HA     1 
ATOM   4868 H HB2    . PHE A 1 308 ? 14.00700  1.08000   36.63600 1.000 105.72914 ?  308 PHE A HB2    1 
ATOM   4869 H HB3    . PHE A 1 308 ? 12.48100  0.92400   36.22200 1.000 105.72914 ?  308 PHE A HB3    1 
ATOM   4870 H HD1    . PHE A 1 308 ? 14.77000  3.64500   36.52300 1.000 93.35695  ?  308 PHE A HD1    1 
ATOM   4871 H HD2    . PHE A 1 308 ? 11.91300  1.99500   34.26300 1.000 91.69821  ?  308 PHE A HD2    1 
ATOM   4872 H HE1    . PHE A 1 308 ? 15.00700  5.34800   34.98200 1.000 89.44459  ?  308 PHE A HE1    1 
ATOM   4873 H HE2    . PHE A 1 308 ? 12.14900  3.69000   32.71900 1.000 89.06575  ?  308 PHE A HE2    1 
ATOM   4874 H HZ     . PHE A 1 308 ? 13.70300  5.37100   33.07100 1.000 84.89383  ?  308 PHE A HZ     1 
ATOM   4875 N N      . HIS A 1 309 ? 10.36800  2.64600   37.79800 1.000 86.35178  ?  309 HIS A N      1 
ATOM   4876 C CA     . HIS A 1 309 ? 9.27300   3.59400   37.61800 1.000 93.34514  ?  309 HIS A CA     1 
ATOM   4877 C C      . HIS A 1 309 ? 8.80800   4.23300   38.92100 1.000 95.44652  ?  309 HIS A C      1 
ATOM   4878 O O      . HIS A 1 309 ? 7.91000   5.07900   38.88600 1.000 84.71947  ?  309 HIS A O      1 
ATOM   4879 C CB     . HIS A 1 309 ? 8.08800   2.89700   36.94000 1.000 93.23291  ?  309 HIS A CB     1 
ATOM   4880 C CG     . HIS A 1 309 ? 8.25600   2.71900   35.46200 1.000 105.61644 ?  309 HIS A CG     1 
ATOM   4881 N ND1    . HIS A 1 309 ? 9.36800   2.11900   34.90400 1.000 106.93765 ?  309 HIS A ND1    1 
ATOM   4882 C CD2    . HIS A 1 309 ? 7.45400   3.06300   34.42400 1.000 95.67712  ?  309 HIS A CD2    1 
ATOM   4883 C CE1    . HIS A 1 309 ? 9.24300   2.10400   33.58900 1.000 98.13268  ?  309 HIS A CE1    1 
ATOM   4884 N NE2    . HIS A 1 309 ? 8.09100   2.66900   33.27100 1.000 90.66804  ?  309 HIS A NE2    1 
ATOM   4885 H H      . HIS A 1 309 ? 10.12300  1.82400   37.85900 1.000 103.73990 ?  309 HIS A H      1 
ATOM   4886 H HA     . HIS A 1 309 ? 9.58000   4.30700   37.03700 1.000 112.13194 ?  309 HIS A HA     1 
ATOM   4887 H HB2    . HIS A 1 309 ? 7.97800   2.01700   37.33300 1.000 111.99726 ?  309 HIS A HB2    1 
ATOM   4888 H HB3    . HIS A 1 309 ? 7.29000   3.42800   37.08600 1.000 111.99726 ?  309 HIS A HB3    1 
ATOM   4889 H HD2    . HIS A 1 309 ? 6.62800   3.48600   34.48100 1.000 114.93032 ?  309 HIS A HD2    1 
ATOM   4890 H HE1    . HIS A 1 309 ? 9.86100   1.75500   32.98800 1.000 117.87699 ?  309 HIS A HE1    1 
ATOM   4891 H HE2    . HIS A 1 309 ? 7.78900   2.77300   32.47300 1.000 108.91942 ?  309 HIS A HE2    1 
ATOM   4892 N N      . ARG A 1 310 ? 9.39900   3.86600   40.06100 1.000 83.75099  ?  310 ARG A N      1 
ATOM   4893 C CA     . ARG A 1 310 ? 8.99200   4.38400   41.35800 1.000 91.51561  ?  310 ARG A CA     1 
ATOM   4894 C C      . ARG A 1 310 ? 9.90900   5.49400   41.87300 1.000 92.96926  ?  310 ARG A C      1 
ATOM   4895 O O      . ARG A 1 310 ? 9.85400   5.83300   43.05800 1.000 105.82710 ?  310 ARG A O      1 
ATOM   4896 C CB     . ARG A 1 310 ? 8.94100   3.25100   42.38600 1.000 90.07704  ?  310 ARG A CB     1 
ATOM   4897 C CG     . ARG A 1 310 ? 8.06100   2.07100   41.99800 1.000 83.33310  ?  310 ARG A CG     1 
ATOM   4898 C CD     . ARG A 1 310 ? 7.86100   1.14400   43.18800 1.000 88.98207  ?  310 ARG A CD     1 
ATOM   4899 N NE     . ARG A 1 310 ? 7.03800   -0.01800  42.87700 1.000 90.34145  ?  310 ARG A NE     1 
ATOM   4900 C CZ     . ARG A 1 310 ? 5.71100   -0.02400  42.87700 1.000 89.57387  ?  310 ARG A CZ     1 
ATOM   4901 N NH1    . ARG A 1 310 ? 5.01400   1.07500   43.12900 1.000 90.08048  ?  310 ARG A NH1    1 
ATOM   4902 N NH2    . ARG A 1 310 ? 5.06700   -1.16100  42.61600 1.000 85.33735  ?  310 ARG A NH2    1 
ATOM   4903 H H      . ARG A 1 310 ? 10.05100  3.30600   40.10400 1.000 100.61896 ?  310 ARG A H      1 
ATOM   4904 H HA     . ARG A 1 310 ? 8.10200   4.75600   41.25900 1.000 109.93650 ?  310 ARG A HA     1 
ATOM   4905 H HB2    . ARG A 1 310 ? 9.84000   2.91300   42.51500 1.000 108.21022 ?  310 ARG A HB2    1 
ATOM   4906 H HB3    . ARG A 1 310 ? 8.59700   3.60800   43.21900 1.000 108.21022 ?  310 ARG A HB3    1 
ATOM   4907 H HG2    . ARG A 1 310 ? 7.19300   2.39400   41.70800 1.000 100.11749 ?  310 ARG A HG2    1 
ATOM   4908 H HG3    . ARG A 1 310 ? 8.48400   1.57000   41.28300 1.000 100.11749 ?  310 ARG A HG3    1 
ATOM   4909 H HD2    . ARG A 1 310 ? 8.72700   0.82500   43.48700 1.000 106.89625 ?  310 ARG A HD2    1 
ATOM   4910 H HD3    . ARG A 1 310 ? 7.42500   1.63600   43.90100 1.000 106.89625 ?  310 ARG A HD3    1 
ATOM   4911 H HE     . ARG A 1 310 ? 7.44100   -0.75200  42.67900 1.000 108.52751 ?  310 ARG A HE     1 
ATOM   4912 H HH11   . ARG A 1 310 ? 5.42100   1.81300   43.29700 1.000 108.21435 ?  310 ARG A HH11   1 
ATOM   4913 H HH12   . ARG A 1 310 ? 4.15400   1.05000   43.12400 1.000 108.21435 ?  310 ARG A HH12   1 
ATOM   4914 H HH21   . ARG A 1 310 ? 5.51000   -1.87900  42.45100 1.000 102.52259 ?  310 ARG A HH21   1 
ATOM   4915 H HH22   . ARG A 1 310 ? 4.20700   -1.17700  42.61400 1.000 102.52259 ?  310 ARG A HH22   1 
ATOM   4916 N N      . MET A 1 311 ? 10.74700  6.06800   41.00600 1.000 96.57117  ?  311 MET A N      1 
ATOM   4917 C CA     . MET A 1 311 ? 11.76400  7.01400   41.44900 1.000 104.89810 ?  311 MET A CA     1 
ATOM   4918 C C      . MET A 1 311 ? 11.23900  8.43600   41.62000 1.000 109.97074 ?  311 MET A C      1 
ATOM   4919 O O      . MET A 1 311 ? 11.96900  9.28500   42.14400 1.000 105.54523 ?  311 MET A O      1 
ATOM   4920 C CB     . MET A 1 311 ? 12.93800  7.04100   40.45800 1.000 102.38610 ?  311 MET A CB     1 
ATOM   4921 C CG     . MET A 1 311 ? 13.34800  5.68400   39.90100 1.000 93.09315  ?  311 MET A CG     1 
ATOM   4922 S SD     . MET A 1 311 ? 14.72200  4.94200   40.79900 1.000 134.49678 ?  311 MET A SD     1 
ATOM   4923 C CE     . MET A 1 311 ? 16.07900  5.27900   39.67800 1.000 89.31087  ?  311 MET A CE     1 
ATOM   4924 H H      . MET A 1 311 ? 10.74400  5.92400   40.15800 1.000 116.00317 ?  311 MET A H      1 
ATOM   4925 H HA     . MET A 1 311 ? 12.09700  6.70000   42.30500 1.000 125.99550 ?  311 MET A HA     1 
ATOM   4926 H HB2    . MET A 1 311 ? 12.69000  7.60000   39.70500 1.000 122.98109 ?  311 MET A HB2    1 
ATOM   4927 H HB3    . MET A 1 311 ? 13.71100  7.41500   40.90800 1.000 122.98109 ?  311 MET A HB3    1 
ATOM   4928 H HG2    . MET A 1 311 ? 12.59200  5.07900   39.95700 1.000 111.82955 ?  311 MET A HG2    1 
ATOM   4929 H HG3    . MET A 1 311 ? 13.61900  5.79200   38.97600 1.000 111.82955 ?  311 MET A HG3    1 
ATOM   4930 H HE1    . MET A 1 311 ? 16.89600  4.91600   40.05300 1.000 107.29082 ?  311 MET A HE1    1 
ATOM   4931 H HE2    . MET A 1 311 ? 15.89300  4.86100   38.82200 1.000 107.29082 ?  311 MET A HE2    1 
ATOM   4932 H HE3    . MET A 1 311 ? 16.16400  6.23900   39.56500 1.000 107.29082 ?  311 MET A HE3    1 
ATOM   4933 N N      . ALA A 1 312 ? 10.00900  8.71800   41.19800 1.000 97.19857  ?  312 ALA A N      1 
ATOM   4934 C CA     . ALA A 1 312 ? 9.43500   10.05400  41.26600 1.000 101.14978 ?  312 ALA A CA     1 
ATOM   4935 C C      . ALA A 1 312 ? 8.22600   10.08800  42.19700 1.000 105.36045 ?  312 ALA A C      1 
ATOM   4936 O O      . ALA A 1 312 ? 7.20400   10.71200  41.90200 1.000 104.58569 ?  312 ALA A O      1 
ATOM   4937 C CB     . ALA A 1 312 ? 9.05000   10.54900  39.87100 1.000 86.92058  ?  312 ALA A CB     1 
ATOM   4938 H H      . ALA A 1 312 ? 9.47500   8.13300   40.86000 1.000 116.75606 ?  312 ALA A H      1 
ATOM   4939 H HA     . ALA A 1 312 ? 10.10300  10.65600  41.62800 1.000 121.49751 ?  312 ALA A HA     1 
ATOM   4940 H HB1    . ALA A 1 312 ? 8.67700   11.44200  39.94500 1.000 104.42246 ?  312 ALA A HB1    1 
ATOM   4941 H HB2    . ALA A 1 312 ? 9.84400   10.56800  39.31300 1.000 104.42246 ?  312 ALA A HB2    1 
ATOM   4942 H HB3    . ALA A 1 312 ? 8.39300   9.94600   39.49200 1.000 104.42246 ?  312 ALA A HB3    1 
ATOM   4943 N N      . GLY A 1 313 ? 8.33300   9.41600   43.33800 1.000 92.85506  ?  313 GLY A N      1 
ATOM   4944 C CA     . GLY A 1 313 ? 7.24900   9.38000   44.29900 1.000 111.27859 ?  313 GLY A CA     1 
ATOM   4945 C C      . GLY A 1 313 ? 5.95500   8.85200   43.71300 1.000 112.37248 ?  313 GLY A C      1 
ATOM   4946 O O      . GLY A 1 313 ? 5.30400   7.98500   44.29500 1.000 98.63511  ?  313 GLY A O      1 
ATOM   4947 H H      . GLY A 1 313 ? 9.02900   8.97100   43.57600 1.000 111.54384 ?  313 GLY A H      1 
ATOM   4948 H HA2    . GLY A 1 313 ? 7.50100   8.80900   45.04200 1.000 133.65208 ?  313 GLY A HA2    1 
ATOM   4949 H HA3    . GLY A 1 313 ? 7.08800   10.27800  44.63100 1.000 133.65208 ?  313 GLY A HA3    1 
ATOM   4950 N N      . ASN A 1 325 ? -10.36400 15.81500  37.74500 1.000 109.47939 ?  325 ASN A N      1 
ATOM   4951 C CA     . ASN A 1 325 ? -8.97500  15.56300  37.35300 1.000 108.70288 ?  325 ASN A CA     1 
ATOM   4952 C C      . ASN A 1 325 ? -8.87700  14.99200  35.93200 1.000 96.87856  ?  325 ASN A C      1 
ATOM   4953 O O      . ASN A 1 325 ? -7.99600  15.39500  35.16900 1.000 91.30581  ?  325 ASN A O      1 
ATOM   4954 C CB     . ASN A 1 325 ? -8.30900  14.61400  38.36400 1.000 109.16446 ?  325 ASN A CB     1 
ATOM   4955 C CG     . ASN A 1 325 ? -6.80300  14.52800  38.18300 1.000 104.42759 ?  325 ASN A CG     1 
ATOM   4956 O OD1    . ASN A 1 325 ? -6.15900  15.48700  37.75600 1.000 101.41247 ?  325 ASN A OD1    1 
ATOM   4957 N ND2    . ASN A 1 325 ? -6.23600  13.37500  38.51300 1.000 103.76978 ?  325 ASN A ND2    1 
ATOM   4958 H H      . ASN A 1 325 ? -10.46500 15.98200  38.58200 1.000 131.49304 ?  325 ASN A H      1 
ATOM   4959 H HA     . ASN A 1 325 ? -8.48900  16.40300  37.35400 1.000 130.56122 ?  325 ASN A HA     1 
ATOM   4960 H HB2    . ASN A 1 325 ? -8.48600  14.93400  39.26200 1.000 131.11512 ?  325 ASN A HB2    1 
ATOM   4961 H HB3    . ASN A 1 325 ? -8.67700  13.72300  38.25000 1.000 131.11512 ?  325 ASN A HB3    1 
ATOM   4962 H HD21   . ASN A 1 325 ? -6.71800  12.72800  38.81100 1.000 124.64151 ?  325 ASN A HD21   1 
ATOM   4963 H HD22   . ASN A 1 325 ? -5.38600  13.27400  38.43000 1.000 124.64151 ?  325 ASN A HD22   1 
ATOM   4964 N N      . PRO A 1 326 ? -9.77000  14.05900  35.56900 1.000 97.01937  ?  326 PRO A N      1 
ATOM   4965 C CA     . PRO A 1 326 ? -9.71400  13.51600  34.20100 1.000 92.30562  ?  326 PRO A CA     1 
ATOM   4966 C C      . PRO A 1 326 ? -9.82000  14.56300  33.10500 1.000 83.83670  ?  326 PRO A C      1 
ATOM   4967 O O      . PRO A 1 326 ? -9.15200  14.43900  32.07300 1.000 73.27071  ?  326 PRO A O      1 
ATOM   4968 C CB     . PRO A 1 326 ? -10.90900 12.54800  34.15900 1.000 88.75207  ?  326 PRO A CB     1 
ATOM   4969 C CG     . PRO A 1 326 ? -11.10900 12.12800  35.55900 1.000 98.65443  ?  326 PRO A CG     1 
ATOM   4970 C CD     . PRO A 1 326 ? -10.66400 13.26800  36.44200 1.000 101.50998 ?  326 PRO A CD     1 
ATOM   4971 H HA     . PRO A 1 326 ? -8.88200  13.02800  34.09300 1.000 110.88452 ?  326 PRO A HA     1 
ATOM   4972 H HB2    . PRO A 1 326 ? -11.69300 13.00700  33.81800 1.000 106.62025 ?  326 PRO A HB2    1 
ATOM   4973 H HB3    . PRO A 1 326 ? -10.69800 11.78800  33.59500 1.000 106.62025 ?  326 PRO A HB3    1 
ATOM   4974 H HG2    . PRO A 1 326 ? -12.04800 11.93500  35.70500 1.000 118.50309 ?  326 PRO A HG2    1 
ATOM   4975 H HG3    . PRO A 1 326 ? -10.57600 11.33700  35.73600 1.000 118.50309 ?  326 PRO A HG3    1 
ATOM   4976 H HD2    . PRO A 1 326 ? -11.42400 13.79900  36.72600 1.000 121.92974 ?  326 PRO A HD2    1 
ATOM   4977 H HD3    . PRO A 1 326 ? -10.18300 12.93600  37.21600 1.000 121.92974 ?  326 PRO A HD3    1 
ATOM   4978 N N      . GLU A 1 327 ? -10.65600 15.58900  33.29100 1.000 88.95120  ?  327 GLU A N      1 
ATOM   4979 C CA     . GLU A 1 327 ? -10.94100 16.50800  32.19100 1.000 76.87288  ?  327 GLU A CA     1 
ATOM   4980 C C      . GLU A 1 327 ? -9.69200  17.25700  31.74900 1.000 73.38519  ?  327 GLU A C      1 
ATOM   4981 O O      . GLU A 1 327 ? -9.46100  17.43500  30.55100 1.000 71.69995  ?  327 GLU A O      1 
ATOM   4982 C CB     . GLU A 1 327 ? -12.04900 17.48000  32.59300 1.000 85.80143  ?  327 GLU A CB     1 
ATOM   4983 C CG     . GLU A 1 327 ? -12.49200 18.50100  31.52200 1.000 99.48195  ?  327 GLU A CG     1 
ATOM   4984 C CD     . GLU A 1 327 ? -12.52100 17.94400  30.09300 1.000 96.77823  ?  327 GLU A CD     1 
ATOM   4985 O OE1    . GLU A 1 327 ? -11.50000 17.43600  29.62600 1.000 94.88617  ?  327 GLU A OE1    1 
ATOM   4986 O OE2    . GLU A 1 327 ? -13.58300 18.03500  29.42100 1.000 113.86865 -1 327 GLU A OE2    1 
ATOM   4987 H H      . GLU A 1 327 ? -11.06200 15.77000  34.02700 1.000 106.85921 ?  327 GLU A H      1 
ATOM   4988 H HA     . GLU A 1 327 ? -11.25800 15.99600  31.43100 1.000 92.36522  ?  327 GLU A HA     1 
ATOM   4989 H HB2    . GLU A 1 327 ? -12.83300 16.96100  32.83300 1.000 103.07948 ?  327 GLU A HB2    1 
ATOM   4990 H HB3    . GLU A 1 327 ? -11.74000 17.98800  33.36000 1.000 103.07948 ?  327 GLU A HB3    1 
ATOM   4991 H HG2    . GLU A 1 327 ? -13.38700 18.80600  31.73600 1.000 119.49611 ?  327 GLU A HG2    1 
ATOM   4992 H HG3    . GLU A 1 327 ? -11.87500 19.24900  31.53200 1.000 119.49611 ?  327 GLU A HG3    1 
ATOM   4993 N N      . PHE A 1 328 ? -8.86900  17.70200  32.69600 1.000 88.32420  ?  328 PHE A N      1 
ATOM   4994 C CA     . PHE A 1 328 ? -7.66000  18.42900  32.31200 1.000 86.74404  ?  328 PHE A CA     1 
ATOM   4995 C C      . PHE A 1 328 ? -6.77400  17.56400  31.41300 1.000 72.43921  ?  328 PHE A C      1 
ATOM   4996 O O      . PHE A 1 328 ? -6.20400  18.05500  30.43300 1.000 65.34892  ?  328 PHE A O      1 
ATOM   4997 C CB     . PHE A 1 328 ? -6.89200  18.88600  33.54900 1.000 94.13061  ?  328 PHE A CB     1 
ATOM   4998 C CG     . PHE A 1 328 ? -7.52300  20.05700  34.26600 0.980 97.97511  ?  328 PHE A CG     1 
ATOM   4999 C CD1    . PHE A 1 328 ? -8.30200  20.98400  33.58600 1.000 100.33342 ?  328 PHE A CD1    1 
ATOM   5000 C CD2    . PHE A 1 328 ? -7.32900  20.23000  35.62600 0.740 107.63109 ?  328 PHE A CD2    1 
ATOM   5001 C CE1    . PHE A 1 328 ? -8.87600  22.05200  34.25100 1.000 99.11937  ?  328 PHE A CE1    1 
ATOM   5002 C CE2    . PHE A 1 328 ? -7.90000  21.29900  36.29400 1.000 103.56878 ?  328 PHE A CE2    1 
ATOM   5003 C CZ     . PHE A 1 328 ? -8.67400  22.20900  35.60500 1.000 110.75887 ?  328 PHE A CZ     1 
ATOM   5004 H H      . PHE A 1 328 ? -8.98300  17.60100  33.54300 1.000 106.10681 ?  328 PHE A H      1 
ATOM   5005 H HA     . PHE A 1 328 ? -7.91500  19.22500  31.82000 1.000 104.21062 ?  328 PHE A HA     1 
ATOM   5006 H HB2    . PHE A 1 328 ? -6.84300  18.14700  34.17600 1.000 113.07450 ?  328 PHE A HB2    1 
ATOM   5007 H HB3    . PHE A 1 328 ? -5.99800  19.15200  33.28000 1.000 113.07450 ?  328 PHE A HB3    1 
ATOM   5008 H HD1    . PHE A 1 328 ? -8.43900  20.88500  32.67200 1.000 120.51788 ?  328 PHE A HD1    1 
ATOM   5009 H HD2    . PHE A 1 328 ? -6.80800  19.62100  36.09700 1.000 129.27507 ?  328 PHE A HD2    1 
ATOM   5010 H HE1    . PHE A 1 328 ? -9.39700  22.66500  33.78400 1.000 119.06101 ?  328 PHE A HE1    1 
ATOM   5011 H HE2    . PHE A 1 328 ? -7.76300  21.40300  37.20800 1.000 124.40030 ?  328 PHE A HE2    1 
ATOM   5012 H HZ     . PHE A 1 328 ? -9.05900  22.92700  36.05400 1.000 133.02841 ?  328 PHE A HZ     1 
ATOM   5013 N N      . LEU A 1 329 ? -6.65700  16.26900  31.72700 1.000 64.99653  ?  329 LEU A N      1 
ATOM   5014 C CA     . LEU A 1 329 ? -5.86300  15.38200  30.88700 1.000 64.42638  ?  329 LEU A CA     1 
ATOM   5015 C C      . LEU A 1 329 ? -6.47600  15.23100  29.50100 1.000 58.14099  ?  329 LEU A C      1 
ATOM   5016 O O      . LEU A 1 329 ? -5.74900  15.17200  28.50200 1.000 51.16328  ?  329 LEU A O      1 
ATOM   5017 C CB     . LEU A 1 329 ? -5.71400  14.01500  31.55200 1.000 66.18699  ?  329 LEU A CB     1 
ATOM   5018 C CG     . LEU A 1 329 ? -4.91900  12.97200  30.75700 1.000 67.53154  ?  329 LEU A CG     1 
ATOM   5019 C CD1    . LEU A 1 329 ? -3.42000  13.16600  30.94600 1.000 67.35770  ?  329 LEU A CD1    1 
ATOM   5020 C CD2    . LEU A 1 329 ? -5.33600  11.56100  31.15700 1.000 69.35123  ?  329 LEU A CD2    1 
ATOM   5021 H H      . LEU A 1 329 ? -7.02000  15.89000  32.40800 1.000 78.11361  ?  329 LEU A H      1 
ATOM   5022 H HA     . LEU A 1 329 ? -4.97800  15.76700  30.78700 1.000 77.42942  ?  329 LEU A HA     1 
ATOM   5023 H HB2    . LEU A 1 329 ? -5.26100  14.13700  32.40100 1.000 79.54216  ?  329 LEU A HB2    1 
ATOM   5024 H HB3    . LEU A 1 329 ? -6.60100  13.65000  31.69900 1.000 79.54216  ?  329 LEU A HB3    1 
ATOM   5025 H HG     . LEU A 1 329 ? -5.11400  13.08800  29.81400 1.000 81.15562  ?  329 LEU A HG     1 
ATOM   5026 H HD11   . LEU A 1 329 ? -2.94700  12.51100  30.41000 1.000 80.94701  ?  329 LEU A HD11   1 
ATOM   5027 H HD12   . LEU A 1 329 ? -3.17900  14.06200  30.66300 1.000 80.94701  ?  329 LEU A HD12   1 
ATOM   5028 H HD13   . LEU A 1 329 ? -3.20200  13.04600  31.88400 1.000 80.94701  ?  329 LEU A HD13   1 
ATOM   5029 H HD21   . LEU A 1 329 ? -4.80600  10.92200  30.65600 1.000 83.33924  ?  329 LEU A HD21   1 
ATOM   5030 H HD22   . LEU A 1 329 ? -5.18400  11.44500  32.10800 1.000 83.33924  ?  329 LEU A HD22   1 
ATOM   5031 H HD23   . LEU A 1 329 ? -6.27700  11.44100  30.95500 1.000 83.33924  ?  329 LEU A HD23   1 
ATOM   5032 N N      . ALA A 1 330 ? -7.80500  15.13900  29.42000 1.000 62.51660  ?  330 ALA A N      1 
ATOM   5033 C CA     . ALA A 1 330 ? -8.45400  14.94500  28.12800 1.000 62.40328  ?  330 ALA A CA     1 
ATOM   5034 C C      . ALA A 1 330 ? -8.23600  16.14300  27.21100 1.000 56.83376  ?  330 ALA A C      1 
ATOM   5035 O O      . ALA A 1 330 ? -7.94400  15.97700  26.02000 1.000 52.43341  ?  330 ALA A O      1 
ATOM   5036 C CB     . ALA A 1 330 ? -9.94700  14.68100  28.32400 1.000 60.64986  ?  330 ALA A CB     1 
ATOM   5037 H H      . ALA A 1 330 ? -8.34400  15.18500  30.08900 1.000 75.13769  ?  330 ALA A H      1 
ATOM   5038 H HA     . ALA A 1 330 ? -8.06500  14.16700  27.69900 1.000 75.00170  ?  330 ALA A HA     1 
ATOM   5039 H HB1    . ALA A 1 330 ? -10.36200 14.55500  27.45700 1.000 72.89760  ?  330 ALA A HB1    1 
ATOM   5040 H HB2    . ALA A 1 330 ? -10.05800 13.88200  28.86300 1.000 72.89760  ?  330 ALA A HB2    1 
ATOM   5041 H HB3    . ALA A 1 330 ? -10.34600 15.44200  28.77400 1.000 72.89760  ?  330 ALA A HB3    1 
ATOM   5042 N N      . ALA A 1 331 ? -8.36700  17.36200  27.74800 1.000 58.60075  ?  331 ALA A N      1 
ATOM   5043 C CA     . ALA A 1 331 ? -8.12700  18.55800  26.94200 1.000 54.80652  ?  331 ALA A CA     1 
ATOM   5044 C C      . ALA A 1 331 ? -6.67400  18.61200  26.47000 1.000 51.90916  ?  331 ALA A C      1 
ATOM   5045 O O      . ALA A 1 331 ? -6.40400  18.94700  25.31200 1.000 44.97286  ?  331 ALA A O      1 
ATOM   5046 C CB     . ALA A 1 331 ? -8.48300  19.80400  27.74400 1.000 55.34713  ?  331 ALA A CB     1 
ATOM   5047 H H      . ALA A 1 331 ? -8.59000  17.51900  28.56300 1.000 70.43867  ?  331 ALA A H      1 
ATOM   5048 H HA     . ALA A 1 331 ? -8.69700  18.53500  26.15700 1.000 65.88559  ?  331 ALA A HA     1 
ATOM   5049 H HB1    . ALA A 1 331 ? -8.31900  20.58900  27.19900 1.000 66.53432  ?  331 ALA A HB1    1 
ATOM   5050 H HB2    . ALA A 1 331 ? -9.42000  19.76300  27.99200 1.000 66.53432  ?  331 ALA A HB2    1 
ATOM   5051 H HB3    . ALA A 1 331 ? -7.93200  19.83400  28.54200 1.000 66.53432  ?  331 ALA A HB3    1 
ATOM   5052 N N      . TRP A 1 332 ? -5.73700  18.28300  27.35800 1.000 54.12238  ?  332 TRP A N      1 
ATOM   5053 C CA     . TRP A 1 332 ? -4.32800  18.20000  26.98500 1.000 52.36254  ?  332 TRP A CA     1 
ATOM   5054 C C      . TRP A 1 332 ? -4.10900  17.14400  25.90900 1.000 52.11702  ?  332 TRP A C      1 
ATOM   5055 O O      . TRP A 1 332 ? -3.40700  17.38900  24.92400 1.000 48.06408  ?  332 TRP A O      1 
ATOM   5056 C CB     . TRP A 1 332 ? -3.50200  17.88300  28.23200 1.000 53.50206  ?  332 TRP A CB     1 
ATOM   5057 C CG     . TRP A 1 332 ? -2.02100  17.82000  28.03400 1.000 59.27454  ?  332 TRP A CG     1 
ATOM   5058 C CD1    . TRP A 1 332 ? -1.15600  18.87000  27.97400 1.000 55.79919  ?  332 TRP A CD1    1 
ATOM   5059 C CD2    . TRP A 1 332 ? -1.22700  16.64100  27.89800 1.000 55.35378  ?  332 TRP A CD2    1 
ATOM   5060 N NE1    . TRP A 1 332 ? 0.12100   18.41800  27.81100 1.000 56.54121  ?  332 TRP A NE1    1 
ATOM   5061 C CE2    . TRP A 1 332 ? 0.10800   17.05200  27.76000 1.000 56.80897  ?  332 TRP A CE2    1 
ATOM   5062 C CE3    . TRP A 1 332 ? -1.51800  15.27200  27.87900 1.000 56.20206  ?  332 TRP A CE3    1 
ATOM   5063 C CZ2    . TRP A 1 332 ? 1.15700   16.14400  27.59600 1.000 56.72687  ?  332 TRP A CZ2    1 
ATOM   5064 C CZ3    . TRP A 1 332 ? -0.47800  14.37500  27.72400 1.000 55.20349  ?  332 TRP A CZ3    1 
ATOM   5065 C CH2    . TRP A 1 332 ? 0.84200   14.81800  27.58100 1.000 53.29508  ?  332 TRP A CH2    1 
ATOM   5066 H H      . TRP A 1 332 ? -5.89200  18.10200  28.18400 1.000 65.06462  ?  332 TRP A H      1 
ATOM   5067 H HA     . TRP A 1 332 ? -4.03200  19.05200  26.62700 1.000 62.95282  ?  332 TRP A HA     1 
ATOM   5068 H HB2    . TRP A 1 332 ? -3.67500  18.57000  28.89400 1.000 64.32024  ?  332 TRP A HB2    1 
ATOM   5069 H HB3    . TRP A 1 332 ? -3.78400  17.01800  28.57000 1.000 64.32024  ?  332 TRP A HB3    1 
ATOM   5070 H HD1    . TRP A 1 332 ? -1.40100  19.76600  28.03500 1.000 67.07679  ?  332 TRP A HD1    1 
ATOM   5071 H HE1    . TRP A 1 332 ? 0.82200   18.91300  27.75100 1.000 67.96722  ?  332 TRP A HE1    1 
ATOM   5072 H HE3    . TRP A 1 332 ? -2.39300  14.97200  27.97000 1.000 67.56025  ?  332 TRP A HE3    1 
ATOM   5073 H HZ2    . TRP A 1 332 ? 2.03600   16.43300  27.50000 1.000 68.19002  ?  332 TRP A HZ2    1 
ATOM   5074 H HZ3    . TRP A 1 332 ? -0.65800  13.46300  27.71400 1.000 66.36195  ?  332 TRP A HZ3    1 
ATOM   5075 H HH2    . TRP A 1 332 ? 1.52100   14.19200  27.47400 1.000 64.07187  ?  332 TRP A HH2    1 
ATOM   5076 N N      . ARG A 1 333 ? -4.73300  15.97900  26.07700 1.000 52.25305  ?  333 ARG A N      1 
ATOM   5077 C CA     . ARG A 1 333 ? -4.60700  14.89000  25.11800 1.000 55.70411  ?  333 ARG A CA     1 
ATOM   5078 C C      . ARG A 1 333 ? -5.11900  15.29200  23.73700 1.000 54.57538  ?  333 ARG A C      1 
ATOM   5079 O O      . ARG A 1 333 ? -4.52900  14.92000  22.71300 1.000 44.73302  ?  333 ARG A O      1 
ATOM   5080 C CB     . ARG A 1 333 ? -5.39000  13.67400  25.63200 1.000 57.73416  ?  333 ARG A CB     1 
ATOM   5081 C CG     . ARG A 1 333 ? -4.89500  12.32800  25.13500 1.000 72.08825  ?  333 ARG A CG     1 
ATOM   5082 C CD     . ARG A 1 333 ? -5.99100  11.26200  25.26000 1.000 73.42289  ?  333 ARG A CD     1 
ATOM   5083 N NE     . ARG A 1 333 ? -6.42300  11.07800  26.64100 1.000 83.79329  ?  333 ARG A NE     1 
ATOM   5084 C CZ     . ARG A 1 333 ? -7.66700  11.25300  27.08500 1.000 83.23814  ?  333 ARG A CZ     1 
ATOM   5085 N NH1    . ARG A 1 333 ? -8.65400  11.60300  26.27400 1.000 75.31263  ?  333 ARG A NH1    1 
ATOM   5086 N NH2    . ARG A 1 333 ? -7.92600  11.07200  28.37900 1.000 84.90643  ?  333 ARG A NH2    1 
ATOM   5087 H H      . ARG A 1 333 ? -5.24000  15.79300  26.74600 1.000 62.82142  ?  333 ARG A H      1 
ATOM   5088 H HA     . ARG A 1 333 ? -3.67000  14.65500  25.03100 1.000 66.96270  ?  333 ARG A HA     1 
ATOM   5089 H HB2    . ARG A 1 333 ? -5.33600  13.66400  26.60000 1.000 69.39876  ?  333 ARG A HB2    1 
ATOM   5090 H HB3    . ARG A 1 333 ? -6.31400  13.76500  25.35100 1.000 69.39876  ?  333 ARG A HB3    1 
ATOM   5091 H HG2    . ARG A 1 333 ? -4.64100  12.40000  24.20200 1.000 86.62366  ?  333 ARG A HG2    1 
ATOM   5092 H HG3    . ARG A 1 333 ? -4.13300  12.04800  25.66600 1.000 86.62366  ?  333 ARG A HG3    1 
ATOM   5093 H HD2    . ARG A 1 333 ? -6.76100  11.53300  24.73500 1.000 88.22523  ?  333 ARG A HD2    1 
ATOM   5094 H HD3    . ARG A 1 333 ? -5.65000  10.41400  24.93400 1.000 88.22523  ?  333 ARG A HD3    1 
ATOM   5095 H HE     . ARG A 1 333 ? -5.82800  10.83800  27.21400 1.000 100.66972 ?  333 ARG A HE     1 
ATOM   5096 H HH11   . ARG A 1 333 ? -8.50000  11.72300  25.43600 1.000 90.49292  ?  333 ARG A HH11   1 
ATOM   5097 H HH12   . ARG A 1 333 ? -9.44900  11.71000  26.58500 1.000 90.49292  ?  333 ARG A HH12   1 
ATOM   5098 H HH21   . ARG A 1 333 ? -7.29400  10.84400  28.91600 1.000 102.00548 ?  333 ARG A HH21   1 
ATOM   5099 H HH22   . ARG A 1 333 ? -8.72500  11.18200  28.67800 1.000 102.00548 ?  333 ARG A HH22   1 
ATOM   5100 N N      . GLU A 1 334 ? -6.23100  16.02500  23.68900 1.000 53.93891  ?  334 GLU A N      1 
ATOM   5101 C CA     . GLU A 1 334 ? -6.92200  16.34600  22.45200 1.000 52.25508  ?  334 GLU A CA     1 
ATOM   5102 C C      . GLU A 1 334 ? -6.57500  17.74000  21.92300 1.000 49.37706  ?  334 GLU A C      1 
ATOM   5103 O O      . GLU A 1 334 ? -7.27100  18.24300  21.04000 1.000 49.30304  ?  334 GLU A O      1 
ATOM   5104 C CB     . GLU A 1 334 ? -8.42900  16.22200  22.66300 1.000 52.42285  ?  334 GLU A CB     1 
ATOM   5105 C CG     . GLU A 1 334 ? -8.82300  14.85500  23.22400 1.000 56.92654  ?  334 GLU A CG     1 
ATOM   5106 C CD     . GLU A 1 334 ? -10.31900 14.70200  23.44200 1.000 54.31924  ?  334 GLU A CD     1 
ATOM   5107 O OE1    . GLU A 1 334 ? -11.00800 15.71500  23.61900 1.000 55.88503  ?  334 GLU A OE1    1 
ATOM   5108 O OE2    . GLU A 1 334 ? -10.79000 13.55100  23.43000 1.000 67.34573  -1 334 GLU A OE2    1 
ATOM   5109 H H      . GLU A 1 334 ? -6.61200  16.35700  24.38500 1.000 64.84446  ?  334 GLU A H      1 
ATOM   5110 H HA     . GLU A 1 334 ? -6.65700  15.70800  21.77200 1.000 62.82386  ?  334 GLU A HA     1 
ATOM   5111 H HB2    . GLU A 1 334 ? -8.72000  16.90200  23.29000 1.000 63.02519  ?  334 GLU A HB2    1 
ATOM   5112 H HB3    . GLU A 1 334 ? -8.88000  16.34100  21.81200 1.000 63.02519  ?  334 GLU A HB3    1 
ATOM   5113 H HG2    . GLU A 1 334 ? -8.54200  14.16600  22.60200 1.000 68.42962  ?  334 GLU A HG2    1 
ATOM   5114 H HG3    . GLU A 1 334 ? -8.38400  14.72800  24.08000 1.000 68.42962  ?  334 GLU A HG3    1 
ATOM   5115 N N      . ALA A 1 335 ? -5.52900  18.36300  22.44700 1.000 43.45416  ?  335 ALA A N      1 
ATOM   5116 C CA     . ALA A 1 335 ? -5.01800  19.62600  21.90900 1.000 51.10822  ?  335 ALA A CA     1 
ATOM   5117 C C      . ALA A 1 335 ? -6.09500  20.71300  21.89100 1.000 49.89857  ?  335 ALA A C      1 
ATOM   5118 O O      . ALA A 1 335 ? -6.27500  21.42400  20.90700 1.000 52.99693  ?  335 ALA A O      1 
ATOM   5119 C CB     . ALA A 1 335 ? -4.44600  19.41000  20.50600 1.000 47.51597  ?  335 ALA A CB     1 
ATOM   5120 H H      . ALA A 1 335 ? -5.08800  18.07300  23.12600 1.000 52.26277  ?  335 ALA A H      1 
ATOM   5121 H HA     . ALA A 1 335 ? -4.30900  19.94000  22.49200 1.000 61.44763  ?  335 ALA A HA     1 
ATOM   5122 H HB1    . ALA A 1 335 ? -4.11500  20.25600  20.16600 1.000 57.13693  ?  335 ALA A HB1    1 
ATOM   5123 H HB2    . ALA A 1 335 ? -3.72000  18.76800  20.55600 1.000 57.13693  ?  335 ALA A HB2    1 
ATOM   5124 H HB3    . ALA A 1 335 ? -5.14700  19.07200  19.92700 1.000 57.13693  ?  335 ALA A HB3    1 
ATOM   5125 N N      . ARG A 1 336 ? -6.82000  20.83400  23.00700 1.000 50.79017  ?  336 ARG A N      1 
ATOM   5126 C CA     . ARG A 1 336 ? -7.84500  21.85800  23.15900 1.000 44.34843  ?  336 ARG A CA     1 
ATOM   5127 C C      . ARG A 1 336 ? -7.73500  22.52800  24.52200 1.000 44.86476  ?  336 ARG A C      1 
ATOM   5128 O O      . ARG A 1 336 ? -8.74100  22.76800  25.20100 1.000 49.24411  ?  336 ARG A O      1 
ATOM   5129 C CB     . ARG A 1 336 ? -9.24300  21.27200  22.95300 1.000 53.19909  ?  336 ARG A CB     1 
ATOM   5130 C CG     . ARG A 1 336 ? -9.60100  20.14000  23.89000 1.000 52.19087  ?  336 ARG A CG     1 
ATOM   5131 C CD     . ARG A 1 336 ? -11.04500 19.68200  23.65200 1.000 58.02756  ?  336 ARG A CD     1 
ATOM   5132 N NE     . ARG A 1 336 ? -11.32100 18.39300  24.29600 1.000 55.96142  ?  336 ARG A NE     1 
ATOM   5133 C CZ     . ARG A 1 336 ? -11.65600 18.25700  25.57200 1.000 62.16568  ?  336 ARG A CZ     1 
ATOM   5134 N NH1    . ARG A 1 336 ? -11.78800 19.31000  26.37200 1.000 60.62263  ?  336 ARG A NH1    1 
ATOM   5135 N NH2    . ARG A 1 336 ? -11.86400 17.03800  26.05900 1.000 65.72476  ?  336 ARG A NH2    1 
ATOM   5136 H H      . ARG A 1 336 ? -6.73200  20.32700  23.69600 1.000 61.06597  ?  336 ARG A H      1 
ATOM   5137 H HA     . ARG A 1 336 ? -7.70100  22.54000  22.48500 1.000 53.33589  ?  336 ARG A HA     1 
ATOM   5138 H HB2    . ARG A 1 336 ? -9.89500  21.97700  23.08500 1.000 63.95667  ?  336 ARG A HB2    1 
ATOM   5139 H HB3    . ARG A 1 336 ? -9.30300  20.93000  22.04700 1.000 63.95667  ?  336 ARG A HB3    1 
ATOM   5140 H HG2    . ARG A 1 336 ? -9.00800  19.38800  23.73300 1.000 62.74682  ?  336 ARG A HG2    1 
ATOM   5141 H HG3    . ARG A 1 336 ? -9.51900  20.44100  24.80900 1.000 62.74682  ?  336 ARG A HG3    1 
ATOM   5142 H HD2    . ARG A 1 336 ? -11.65500 20.34100  24.01900 1.000 69.75084  ?  336 ARG A HD2    1 
ATOM   5143 H HD3    . ARG A 1 336 ? -11.19700 19.58400  22.69900 1.000 69.75084  ?  336 ARG A HD3    1 
ATOM   5144 H HE     . ARG A 1 336 ? -11.26100 17.68200  23.81600 1.000 67.27148  ?  336 ARG A HE     1 
ATOM   5145 H HH11   . ARG A 1 336 ? -11.65600 20.10300  26.06500 1.000 72.86493  ?  336 ARG A HH11   1 
ATOM   5146 H HH12   . ARG A 1 336 ? -12.00600 19.20000  27.19600 1.000 72.86493  ?  336 ARG A HH12   1 
ATOM   5147 H HH21   . ARG A 1 336 ? -11.78100 16.35100  25.54800 1.000 78.98748  ?  336 ARG A HH21   1 
ATOM   5148 H HH22   . ARG A 1 336 ? -12.08200 16.93600  26.88400 1.000 78.98748  ?  336 ARG A HH22   1 
ATOM   5149 N N      . THR A 1 337 ? -6.51700  22.85600  24.93000 1.000 48.15907  ?  337 THR A N      1 
ATOM   5150 C CA     . THR A 1 337 ? -6.29400  23.55800  26.18700 1.000 48.95251  ?  337 THR A CA     1 
ATOM   5151 C C      . THR A 1 337 ? -6.60700  25.04200  26.10300 1.000 51.89294  ?  337 THR A C      1 
ATOM   5152 O O      . THR A 1 337 ? -6.80000  25.68600  27.14400 1.000 52.96468  ?  337 THR A O      1 
ATOM   5153 C CB     . THR A 1 337 ? -4.83700  23.38300  26.65000 1.000 45.62552  ?  337 THR A CB     1 
ATOM   5154 O OG1    . THR A 1 337 ? -3.96800  24.11100  25.77300 1.000 46.00852  ?  337 THR A OG1    1 
ATOM   5155 C CG2    . THR A 1 337 ? -4.44000  21.91100  26.65600 1.000 46.39247  ?  337 THR A CG2    1 
ATOM   5156 H H      . THR A 1 337 ? -5.79600  22.68300  24.49400 1.000 57.90865  ?  337 THR A H      1 
ATOM   5157 H HA     . THR A 1 337 ? -6.87500  23.16200  26.85600 1.000 58.86078  ?  337 THR A HA     1 
ATOM   5158 H HB     . THR A 1 337 ? -4.74400  23.72100  27.55400 1.000 54.86839  ?  337 THR A HB     1 
ATOM   5159 H HG1    . THR A 1 337 ? -3.17000  24.02100  26.01900 1.000 55.32799  ?  337 THR A HG1    1 
ATOM   5160 H HG21   . THR A 1 337 ? -3.55500  21.80800  27.03900 1.000 55.78873  ?  337 THR A HG21   1 
ATOM   5161 H HG22   . THR A 1 337 ? -5.07400  21.39900  27.18300 1.000 55.78873  ?  337 THR A HG22   1 
ATOM   5162 H HG23   . THR A 1 337 ? -4.43300  21.56600  25.75000 1.000 55.78873  ?  337 THR A HG23   1 
ATOM   5163 N N      . GLY A 1 338 ? -6.66600  25.60200  24.90300 1.000 49.80472  ?  338 GLY A N      1 
ATOM   5164 C CA     . GLY A 1 338 ? -6.86100  27.03400  24.74400 1.000 52.39801  ?  338 GLY A CA     1 
ATOM   5165 C C      . GLY A 1 338 ? -5.58300  27.85200  24.78100 1.000 49.53019  ?  338 GLY A C      1 
ATOM   5166 O O      . GLY A 1 338 ? -5.65100  29.08200  24.68200 1.000 45.02707  ?  338 GLY A O      1 
ATOM   5167 H H      . GLY A 1 338 ? -6.59600  25.17200  24.16200 1.000 59.88343  ?  338 GLY A H      1 
ATOM   5168 H HA2    . GLY A 1 338 ? -7.29400  27.19700  23.89100 1.000 62.99538  ?  338 GLY A HA2    1 
ATOM   5169 H HA3    . GLY A 1 338 ? -7.43700  27.35100  25.45700 1.000 62.99538  ?  338 GLY A HA3    1 
ATOM   5170 N N      . PHE A 1 339 ? -4.43500  27.21400  24.93700 1.000 44.29681  ?  339 PHE A N      1 
ATOM   5171 C CA     . PHE A 1 339 ? -3.14600  27.88700  24.83300 1.000 45.59521  ?  339 PHE A CA     1 
ATOM   5172 C C      . PHE A 1 339 ? -2.49700  27.46400  23.52600 1.000 42.47499  ?  339 PHE A C      1 
ATOM   5173 O O      . PHE A 1 339 ? -2.03600  26.30900  23.42100 1.000 43.81375  ?  339 PHE A O      1 
ATOM   5174 C CB     . PHE A 1 339 ? -2.25400  27.53400  26.02500 1.000 48.77075  ?  339 PHE A CB     1 
ATOM   5175 C CG     . PHE A 1 339 ? -2.85300  27.87900  27.35400 1.000 53.62280  ?  339 PHE A CG     1 
ATOM   5176 C CD1    . PHE A 1 339 ? -2.81800  29.18100  27.82800 1.000 52.85009  ?  339 PHE A CD1    1 
ATOM   5177 C CD2    . PHE A 1 339 ? -3.45100  26.90200  28.13500 1.000 58.50389  ?  339 PHE A CD2    1 
ATOM   5178 C CE1    . PHE A 1 339 ? -3.36800  29.50400  29.05300 1.000 56.80324  ?  339 PHE A CE1    1 
ATOM   5179 C CE2    . PHE A 1 339 ? -3.99900  27.22000  29.36000 1.000 65.51559  ?  339 PHE A CE2    1 
ATOM   5180 C CZ     . PHE A 1 339 ? -3.95900  28.52600  29.82100 1.000 62.78145  ?  339 PHE A CZ     1 
ATOM   5181 H H      . PHE A 1 339 ? -4.37200  26.37300  25.10800 1.000 53.27395  ?  339 PHE A H      1 
ATOM   5182 H HA     . PHE A 1 339 ? -3.26800  28.84900  24.83200 1.000 54.83202  ?  339 PHE A HA     1 
ATOM   5183 H HB2    . PHE A 1 339 ? -2.08600  26.57900  26.01600 1.000 58.64267  ?  339 PHE A HB2    1 
ATOM   5184 H HB3    . PHE A 1 339 ? -1.41900  28.02000  25.94300 1.000 58.64267  ?  339 PHE A HB3    1 
ATOM   5185 H HD1    . PHE A 1 339 ? -2.41800  29.84600  27.31500 1.000 63.53788  ?  339 PHE A HD1    1 
ATOM   5186 H HD2    . PHE A 1 339 ? -3.48400  26.02400  27.83000 1.000 70.32244  ?  339 PHE A HD2    1 
ATOM   5187 H HE1    . PHE A 1 339 ? -3.33900  30.38100  29.36000 1.000 68.28166  ?  339 PHE A HE1    1 
ATOM   5188 H HE2    . PHE A 1 339 ? -4.39600  26.55700  29.87800 1.000 78.73648  ?  339 PHE A HE2    1 
ATOM   5189 H HZ     . PHE A 1 339 ? -4.33000  28.74100  30.64600 1.000 75.45552  ?  339 PHE A HZ     1 
ATOM   5190 N N      . PRO A 1 340 ? -2.43100  28.33100  22.51400 1.000 44.33991  ?  340 PRO A N      1 
ATOM   5191 C CA     . PRO A 1 340 ? -1.99400  27.87700  21.18600 1.000 43.34705  ?  340 PRO A CA     1 
ATOM   5192 C C      . PRO A 1 340 ? -0.64300  27.17800  21.16300 1.000 42.61090  ?  340 PRO A C      1 
ATOM   5193 O O      . PRO A 1 340 ? -0.48400  26.18200  20.44400 1.000 47.42807  ?  340 PRO A O      1 
ATOM   5194 C CB     . PRO A 1 340 ? -1.97400  29.16800  20.36400 1.000 41.64150  ?  340 PRO A CB     1 
ATOM   5195 C CG     . PRO A 1 340 ? -3.05000  30.01800  20.99600 1.000 42.88044  ?  340 PRO A CG     1 
ATOM   5196 C CD     . PRO A 1 340 ? -3.00400  29.69900  22.47400 1.000 43.67852  ?  340 PRO A CD     1 
ATOM   5197 H HA     . PRO A 1 340 ? -2.66300  27.27100  20.83200 1.000 52.13422  ?  340 PRO A HA     1 
ATOM   5198 H HB2    . PRO A 1 340 ? -1.10500  29.59400  20.43100 1.000 50.08757  ?  340 PRO A HB2    1 
ATOM   5199 H HB3    . PRO A 1 340 ? -2.17900  28.97600  19.43600 1.000 50.08757  ?  340 PRO A HB3    1 
ATOM   5200 H HG2    . PRO A 1 340 ? -2.86100  30.95700  20.84000 1.000 51.57430  ?  340 PRO A HG2    1 
ATOM   5201 H HG3    . PRO A 1 340 ? -3.91400  29.78700  20.62100 1.000 51.57430  ?  340 PRO A HG3    1 
ATOM   5202 H HD2    . PRO A 1 340 ? -2.43200  30.32600  22.94500 1.000 52.53199  ?  340 PRO A HD2    1 
ATOM   5203 H HD3    . PRO A 1 340 ? -3.89500  29.71100  22.85800 1.000 52.53199  ?  340 PRO A HD3    1 
ATOM   5204 N N      . TRP A 1 341 ? 0.32400   27.65300  21.93400 1.000 42.00648  ?  341 TRP A N      1 
ATOM   5205 C CA     . TRP A 1 341 ? 1.63400   27.00100  21.96400 1.000 39.16449  ?  341 TRP A CA     1 
ATOM   5206 C C      . TRP A 1 341 ? 1.50900   25.56200  22.43300 1.000 43.86982  ?  341 TRP A C      1 
ATOM   5207 O O      . TRP A 1 341 ? 2.12100   24.65600  21.84500 1.000 46.22877  ?  341 TRP A O      1 
ATOM   5208 C CB     . TRP A 1 341 ? 2.57800   27.78700  22.85500 1.000 40.75878  ?  341 TRP A CB     1 
ATOM   5209 C CG     . TRP A 1 341 ? 3.94600   27.19000  23.05700 1.000 42.70268  ?  341 TRP A CG     1 
ATOM   5210 C CD1    . TRP A 1 341 ? 4.48000   26.76500  24.22300 1.000 41.29387  ?  341 TRP A CD1    1 
ATOM   5211 C CD2    . TRP A 1 341 ? 4.95500   26.99100  22.05500 1.000 42.41286  ?  341 TRP A CD2    1 
ATOM   5212 N NE1    . TRP A 1 341 ? 5.74800   26.29700  24.02600 1.000 43.52374  ?  341 TRP A NE1    1 
ATOM   5213 C CE2    . TRP A 1 341 ? 6.06800   26.42800  22.70100 1.000 45.90041  ?  341 TRP A CE2    1 
ATOM   5214 C CE3    . TRP A 1 341 ? 5.01900   27.23200  20.67700 1.000 37.74407  ?  341 TRP A CE3    1 
ATOM   5215 C CZ2    . TRP A 1 341 ? 7.25100   26.09700  22.01800 1.000 42.75146  ?  341 TRP A CZ2    1 
ATOM   5216 C CZ3    . TRP A 1 341 ? 6.18400   26.90400  19.99600 1.000 41.39249  ?  341 TRP A CZ3    1 
ATOM   5217 C CH2    . TRP A 1 341 ? 7.29200   26.34500  20.66900 1.000 40.36696  ?  341 TRP A CH2    1 
ATOM   5218 H H      . TRP A 1 341 ? 0.25500   28.34100  22.44400 1.000 50.52555  ?  341 TRP A H      1 
ATOM   5219 H HA     . TRP A 1 341 ? 2.01200   26.99100  21.07100 1.000 47.11515  ?  341 TRP A HA     1 
ATOM   5220 H HB2    . TRP A 1 341 ? 2.70400   28.66500  22.46300 1.000 49.02831  ?  341 TRP A HB2    1 
ATOM   5221 H HB3    . TRP A 1 341 ? 2.16900   27.87000  23.73100 1.000 49.02831  ?  341 TRP A HB3    1 
ATOM   5222 H HD1    . TRP A 1 341 ? 4.04500   26.78800  25.04400 1.000 49.67042  ?  341 TRP A HD1    1 
ATOM   5223 H HE1    . TRP A 1 341 ? 6.26200   25.97300  24.63500 1.000 52.34625  ?  341 TRP A HE1    1 
ATOM   5224 H HE3    . TRP A 1 341 ? 4.29600   27.60500  20.22700 1.000 45.41065  ?  341 TRP A HE3    1 
ATOM   5225 H HZ2    . TRP A 1 341 ? 7.97800   25.72600  22.46300 1.000 51.41953  ?  341 TRP A HZ2    1 
ATOM   5226 H HZ3    . TRP A 1 341 ? 6.23500   27.05600  19.07900 1.000 49.78876  ?  341 TRP A HZ3    1 
ATOM   5227 H HH2    . TRP A 1 341 ? 8.06200   26.14000  20.18900 1.000 48.55812  ?  341 TRP A HH2    1 
ATOM   5228 N N      . ILE A 1 342 ? 0.71100   25.32400  23.47700 1.000 44.52086  ?  342 ILE A N      1 
ATOM   5229 C CA     . ILE A 1 342 ? 0.53700   23.96800  23.98400 1.000 40.30842  ?  342 ILE A CA     1 
ATOM   5230 C C      . ILE A 1 342 ? -0.21200  23.11300  22.97300 1.000 42.68535  ?  342 ILE A C      1 
ATOM   5231 O O      . ILE A 1 342 ? 0.17400   21.97500  22.68500 1.000 42.82253  ?  342 ILE A O      1 
ATOM   5232 C CB     . ILE A 1 342 ? -0.18800  23.99500  25.34400 1.000 42.30481  ?  342 ILE A CB     1 
ATOM   5233 C CG1    . ILE A 1 342 ? 0.66800   24.70900  26.39800 1.000 46.89348  ?  342 ILE A CG1    1 
ATOM   5234 C CG2    . ILE A 1 342 ? -0.54300  22.58100  25.78400 1.000 46.77153  ?  342 ILE A CG2    1 
ATOM   5235 C CD1    . ILE A 1 342 ? 1.91900   23.95700  26.80000 1.000 55.55205  ?  342 ILE A CD1    1 
ATOM   5236 H H      . ILE A 1 342 ? 0.26700   25.92500  23.90300 1.000 53.54280  ?  342 ILE A H      1 
ATOM   5237 H HA     . ILE A 1 342 ? 1.41400   23.57400  24.11600 1.000 48.48787  ?  342 ILE A HA     1 
ATOM   5238 H HB     . ILE A 1 342 ? -1.01300  24.49500  25.24400 1.000 50.88354  ?  342 ILE A HB     1 
ATOM   5239 H HG12   . ILE A 1 342 ? 0.94400   25.56800  26.04200 1.000 56.38994  ?  342 ILE A HG12   1 
ATOM   5240 H HG13   . ILE A 1 342 ? 0.13300   24.83700  27.19600 1.000 56.38994  ?  342 ILE A HG13   1 
ATOM   5241 H HG21   . ILE A 1 342 ? -0.75800  22.59000  26.73000 1.000 56.24361  ?  342 ILE A HG21   1 
ATOM   5242 H HG22   . ILE A 1 342 ? -1.30900  22.27400  25.27400 1.000 56.24361  ?  342 ILE A HG22   1 
ATOM   5243 H HG23   . ILE A 1 342 ? 0.21700   22.00000  25.62300 1.000 56.24361  ?  342 ILE A HG23   1 
ATOM   5244 H HD11   . ILE A 1 342 ? 2.40200   24.47800  27.46100 1.000 66.78023  ?  342 ILE A HD11   1 
ATOM   5245 H HD12   . ILE A 1 342 ? 1.66500   23.10000  27.17600 1.000 66.78023  ?  342 ILE A HD12   1 
ATOM   5246 H HD13   . ILE A 1 342 ? 2.47300   23.82300  26.01500 1.000 66.78023  ?  342 ILE A HD13   1 
ATOM   5247 N N      . ASP A 1 343 ? -1.30900  23.63500  22.42900 1.000 39.16510  ?  343 ASP A N      1 
ATOM   5248 C CA     . ASP A 1 343 ? -2.12200  22.85000  21.50500 1.000 38.00885  ?  343 ASP A CA     1 
ATOM   5249 C C      . ASP A 1 343 ? -1.37400  22.56800  20.20700 1.000 42.85216  ?  343 ASP A C      1 
ATOM   5250 O O      . ASP A 1 343 ? -1.57700  21.50500  19.60000 1.000 44.82348  ?  343 ASP A O      1 
ATOM   5251 C CB     . ASP A 1 343 ? -3.43200  23.56700  21.21400 1.000 41.02532  ?  343 ASP A CB     1 
ATOM   5252 C CG     . ASP A 1 343 ? -4.30900  23.70900  22.45500 1.000 45.05684  ?  343 ASP A CG     1 
ATOM   5253 O OD1    . ASP A 1 343 ? -4.07400  22.97100  23.44000 1.000 48.34572  ?  343 ASP A OD1    1 
ATOM   5254 O OD2    . ASP A 1 343 ? -5.23100  24.54900  22.43600 1.000 44.65670  -1 343 ASP A OD2    1 
ATOM   5255 H H      . ASP A 1 343 ? -1.60100  24.43000  22.57700 1.000 47.11589  ?  343 ASP A H      1 
ATOM   5256 H HA     . ASP A 1 343 ? -2.33500  22.00100  21.92300 1.000 45.72839  ?  343 ASP A HA     1 
ATOM   5257 H HB2    . ASP A 1 343 ? -3.23900  24.45600  20.87900 1.000 49.34816  ?  343 ASP A HB2    1 
ATOM   5258 H HB3    . ASP A 1 343 ? -3.92900  23.06300  20.55100 1.000 49.34816  ?  343 ASP A HB3    1 
ATOM   5259 N N      . ALA A 1 344 ? -0.52900  23.50100  19.75200 1.000 38.41707  ?  344 ALA A N      1 
ATOM   5260 C CA     . ALA A 1 344 ? 0.24500   23.26900  18.54000 1.000 40.06919  ?  344 ALA A CA     1 
ATOM   5261 C C      . ALA A 1 344 ? 1.22800   22.10800  18.71900 1.000 39.62635  ?  344 ALA A C      1 
ATOM   5262 O O      . ALA A 1 344 ? 1.40700   21.29500  17.81000 1.000 40.23795  ?  344 ALA A O      1 
ATOM   5263 C CB     . ALA A 1 344 ? 0.98200   24.54200  18.12800 1.000 40.56094  ?  344 ALA A CB     1 
ATOM   5264 H H      . ALA A 1 344 ? -0.39200  24.26400  20.12500 1.000 46.21825  ?  344 ALA A H      1 
ATOM   5265 H HA     . ALA A 1 344 ? -0.36600  23.03500  17.82400 1.000 48.20080  ?  344 ALA A HA     1 
ATOM   5266 H HB1    . ALA A 1 344 ? 1.47800   24.37000  17.31200 1.000 48.79090  ?  344 ALA A HB1    1 
ATOM   5267 H HB2    . ALA A 1 344 ? 0.33300   25.24700  17.97800 1.000 48.79090  ?  344 ALA A HB2    1 
ATOM   5268 H HB3    . ALA A 1 344 ? 1.59100   24.79800  18.83800 1.000 48.79090  ?  344 ALA A HB3    1 
ATOM   5269 N N      . ILE A 1 345 ? 1.87900   22.03200  19.87600 1.000 39.31364  ?  345 ILE A N      1 
ATOM   5270 C CA     . ILE A 1 345 ? 2.81400   20.93600  20.13100 1.000 37.97812  ?  345 ILE A CA     1 
ATOM   5271 C C      . ILE A 1 345 ? 2.07100   19.60200  20.21900 1.000 39.93167  ?  345 ILE A C      1 
ATOM   5272 O O      . ILE A 1 345 ? 2.49800   18.58400  19.64200 1.000 45.39773  ?  345 ILE A O      1 
ATOM   5273 C CB     . ILE A 1 345 ? 3.62300   21.20600  21.40700 1.000 44.72886  ?  345 ILE A CB     1 
ATOM   5274 C CG1    . ILE A 1 345 ? 4.46400   22.48200  21.24300 1.000 42.13623  ?  345 ILE A CG1    1 
ATOM   5275 C CG2    . ILE A 1 345 ? 4.53600   20.01700  21.72600 1.000 39.87794  ?  345 ILE A CG2    1 
ATOM   5276 C CD1    . ILE A 1 345 ? 5.08200   22.97000  22.55200 1.000 37.68903  ?  345 ILE A CD1    1 
ATOM   5277 H H      . ILE A 1 345 ? 1.80100   22.59300  20.52300 1.000 47.29414  ?  345 ILE A H      1 
ATOM   5278 H HA     . ILE A 1 345 ? 3.43100   20.88500  19.38400 1.000 45.69151  ?  345 ILE A HA     1 
ATOM   5279 H HB     . ILE A 1 345 ? 3.00000   21.32800  22.14000 1.000 53.79241  ?  345 ILE A HB     1 
ATOM   5280 H HG12   . ILE A 1 345 ? 5.18600   22.30400  20.62100 1.000 50.68124  ?  345 ILE A HG12   1 
ATOM   5281 H HG13   . ILE A 1 345 ? 3.89700   23.19000  20.90000 1.000 50.68124  ?  345 ILE A HG13   1 
ATOM   5282 H HG21   . ILE A 1 345 ? 5.10200   20.24700  22.47900 1.000 47.97130  ?  345 ILE A HG21   1 
ATOM   5283 H HG22   . ILE A 1 345 ? 3.98800   19.24800  21.94700 1.000 47.97130  ?  345 ILE A HG22   1 
ATOM   5284 H HG23   . ILE A 1 345 ? 5.08200   19.82100  20.94800 1.000 47.97130  ?  345 ILE A HG23   1 
ATOM   5285 H HD11   . ILE A 1 345 ? 5.56200   23.79600  22.38600 1.000 45.34460  ?  345 ILE A HD11   1 
ATOM   5286 H HD12   . ILE A 1 345 ? 4.37400   23.12200  23.19800 1.000 45.34460  ?  345 ILE A HD12   1 
ATOM   5287 H HD13   . ILE A 1 345 ? 5.69200   22.29300  22.88500 1.000 45.34460  ?  345 ILE A HD13   1 
ATOM   5288 N N      . MET A 1 346 ? 0.95500   19.57600  20.93900 1.000 39.07174  ?  346 MET A N      1 
ATOM   5289 C CA     . MET A 1 346 ? 0.17300   18.34500  21.03500 1.000 40.98182  ?  346 MET A CA     1 
ATOM   5290 C C      . MET A 1 346 ? -0.35700  17.92400  19.67400 1.000 44.92268  ?  346 MET A C      1 
ATOM   5291 O O      . MET A 1 346 ? -0.52900  16.72200  19.41100 1.000 45.78544  ?  346 MET A O      1 
ATOM   5292 C CB     . MET A 1 346 ? -0.96500  18.52900  22.03000 1.000 41.73592  ?  346 MET A CB     1 
ATOM   5293 C CG     . MET A 1 346 ? -0.51000  18.74500  23.45800 1.000 39.29942  ?  346 MET A CG     1 
ATOM   5294 S SD     . MET A 1 346 ? 0.66900   17.48900  24.04700 1.000 43.94754  ?  346 MET A SD     1 
ATOM   5295 C CE     . MET A 1 346 ? -0.45300  16.12100  24.39400 1.000 43.85314  ?  346 MET A CE     1 
ATOM   5296 H H      . MET A 1 346 ? 0.63200   20.24400  21.37400 1.000 47.00386  ?  346 MET A H      1 
ATOM   5297 H HA     . MET A 1 346 ? 0.74000   17.63600  21.37600 1.000 49.29595  ?  346 MET A HA     1 
ATOM   5298 H HB2    . MET A 1 346 ? -1.48600  19.30400  21.76700 1.000 50.20088  ?  346 MET A HB2    1 
ATOM   5299 H HB3    . MET A 1 346 ? -1.52200  17.73500  22.01500 1.000 50.20088  ?  346 MET A HB3    1 
ATOM   5300 H HG2    . MET A 1 346 ? -0.07700  19.61000  23.52100 1.000 47.27708  ?  346 MET A HG2    1 
ATOM   5301 H HG3    . MET A 1 346 ? -1.28600  18.71900  24.04000 1.000 47.27708  ?  346 MET A HG3    1 
ATOM   5302 H HE1    . MET A 1 346 ? 0.06100   15.36500  24.71600 1.000 52.74154  ?  346 MET A HE1    1 
ATOM   5303 H HE2    . MET A 1 346 ? -1.09100  16.39900  25.07000 1.000 52.74154  ?  346 MET A HE2    1 
ATOM   5304 H HE3    . MET A 1 346 ? -0.91900  15.88000  23.57800 1.000 52.74154  ?  346 MET A HE3    1 
ATOM   5305 N N      . THR A 1 347 ? -0.61800  18.89700  18.78400 1.000 40.58396  ?  347 THR A N      1 
ATOM   5306 C CA     . THR A 1 347 ? -0.98700  18.54700  17.41400 1.000 40.15309  ?  347 THR A CA     1 
ATOM   5307 C C      . THR A 1 347 ? 0.20400   17.94200  16.66600 1.000 40.91240  ?  347 THR A C      1 
ATOM   5308 O O      . THR A 1 347 ? 0.03900   16.97100  15.92600 1.000 42.30565  ?  347 THR A O      1 
ATOM   5309 C CB     . THR A 1 347 ? -1.51200  19.78100  16.68700 1.000 42.22190  ?  347 THR A CB     1 
ATOM   5310 O OG1    . THR A 1 347 ? -2.68900  20.26700  17.35700 1.000 46.59425  ?  347 THR A OG1    1 
ATOM   5311 C CG2    . THR A 1 347 ? -1.85100  19.46400  15.24900 1.000 40.47076  ?  347 THR A CG2    1 
ATOM   5312 H H      . THR A 1 347 ? -0.58800  19.74100  18.94800 1.000 48.81852  ?  347 THR A H      1 
ATOM   5313 H HA     . THR A 1 347 ? -1.69800  17.88700  17.43400 1.000 48.30148  ?  347 THR A HA     1 
ATOM   5314 H HB     . THR A 1 347 ? -0.82700  20.46700  16.68800 1.000 50.78406  ?  347 THR A HB     1 
ATOM   5315 H HG1    . THR A 1 347 ? -3.04700  20.87600  16.90300 1.000 56.03087  ?  347 THR A HG1    1 
ATOM   5316 H HG21   . THR A 1 347 ? -2.40100  20.16900  14.87400 1.000 48.68268  ?  347 THR A HG21   1 
ATOM   5317 H HG22   . THR A 1 347 ? -1.03800  19.38700  14.72600 1.000 48.68268  ?  347 THR A HG22   1 
ATOM   5318 H HG23   . THR A 1 347 ? -2.33700  18.62600  15.19900 1.000 48.68268  ?  347 THR A HG23   1 
ATOM   5319 N N      . GLN A 1 348 ? 1.39600   18.49100  16.87000 1.000 36.73692  ?  348 GLN A N      1 
ATOM   5320 C CA     . GLN A 1 348 ? 2.59000   17.92500  16.23800 1.000 42.38894  ?  348 GLN A CA     1 
ATOM   5321 C C      . GLN A 1 348 ? 2.84300   16.50100  16.72200 1.000 39.81290  ?  348 GLN A C      1 
ATOM   5322 O O      . GLN A 1 348 ? 3.23900   15.62700  15.93600 1.000 39.11862  ?  348 GLN A O      1 
ATOM   5323 C CB     . GLN A 1 348 ? 3.80600   18.81700  16.52800 1.000 40.82576  ?  348 GLN A CB     1 
ATOM   5324 C CG     . GLN A 1 348 ? 5.05000   18.43600  15.71800 1.000 46.34685  ?  348 GLN A CG     1 
ATOM   5325 C CD     . GLN A 1 348 ? 6.26300   19.29600  16.04900 1.000 42.32942  ?  348 GLN A CD     1 
ATOM   5326 O OE1    . GLN A 1 348 ? 6.41500   19.77400  17.17300 1.000 40.55245  ?  348 GLN A OE1    1 
ATOM   5327 N NE2    . GLN A 1 348 ? 7.14000   19.47900  15.06600 1.000 42.10832  ?  348 GLN A NE2    1 
ATOM   5328 H H      . GLN A 1 348 ? 1.54300   19.18200  17.36100 1.000 44.20207  ?  348 GLN A H      1 
ATOM   5329 H HA     . GLN A 1 348 ? 2.45800   17.89700  15.27800 1.000 50.98450  ?  348 GLN A HA     1 
ATOM   5330 H HB2    . GLN A 1 348 ? 3.58000   19.73500  16.31000 1.000 49.10868  ?  348 GLN A HB2    1 
ATOM   5331 H HB3    . GLN A 1 348 ? 4.03000   18.74500  17.46900 1.000 49.10868  ?  348 GLN A HB3    1 
ATOM   5332 H HG2    . GLN A 1 348 ? 5.27700   17.51200  15.90700 1.000 55.73399  ?  348 GLN A HG2    1 
ATOM   5333 H HG3    . GLN A 1 348 ? 4.85600   18.54300  14.77400 1.000 55.73399  ?  348 GLN A HG3    1 
ATOM   5334 H HE21   . GLN A 1 348 ? 7.00400   19.12100  14.29600 1.000 50.64775  ?  348 GLN A HE21   1 
ATOM   5335 H HE22   . GLN A 1 348 ? 7.84200   19.95700  15.20000 1.000 50.64775  ?  348 GLN A HE22   1 
ATOM   5336 N N      . LEU A 1 349 ? 2.60200   16.24700  18.00600 1.000 42.90655  ?  349 LEU A N      1 
ATOM   5337 C CA     . LEU A 1 349 ? 2.74200   14.89700  18.55100 1.000 43.70914  ?  349 LEU A CA     1 
ATOM   5338 C C      . LEU A 1 349 ? 1.90200   13.90100  17.77500 1.000 41.29475  ?  349 LEU A C      1 
ATOM   5339 O O      . LEU A 1 349 ? 2.40500   12.87400  17.30100 1.000 45.06716  ?  349 LEU A O      1 
ATOM   5340 C CB     . LEU A 1 349 ? 2.34300   14.89200  20.02900 1.000 36.84032  ?  349 LEU A CB     1 
ATOM   5341 C CG     . LEU A 1 349 ? 2.21600   13.53200  20.71700 1.000 41.47816  ?  349 LEU A CG     1 
ATOM   5342 C CD1    . LEU A 1 349 ? 3.59100   12.88300  20.88400 1.000 45.31710  ?  349 LEU A CD1    1 
ATOM   5343 C CD2    . LEU A 1 349 ? 1.53400   13.68100  22.05300 1.000 46.39088  ?  349 LEU A CD2    1 
ATOM   5344 H H      . LEU A 1 349 ? 2.35700   16.83600  18.58400 1.000 51.60563  ?  349 LEU A H      1 
ATOM   5345 H HA     . LEU A 1 349 ? 3.67100   14.62700  18.48000 1.000 52.56873  ?  349 LEU A HA     1 
ATOM   5346 H HB2    . LEU A 1 349 ? 3.01300   15.39400  20.51900 1.000 44.32615  ?  349 LEU A HB2    1 
ATOM   5347 H HB3    . LEU A 1 349 ? 1.48000   15.32700  20.10500 1.000 44.32615  ?  349 LEU A HB3    1 
ATOM   5348 H HG     . LEU A 1 349 ? 1.67400   12.94700  20.16400 1.000 49.89157  ?  349 LEU A HG     1 
ATOM   5349 H HD11   . LEU A 1 349 ? 3.48000   12.00800  21.28800 1.000 54.49828  ?  349 LEU A HD11   1 
ATOM   5350 H HD12   . LEU A 1 349 ? 4.00700   12.79500  20.01300 1.000 54.49828  ?  349 LEU A HD12   1 
ATOM   5351 H HD13   . LEU A 1 349 ? 4.13700   13.44400  21.45700 1.000 54.49828  ?  349 LEU A HD13   1 
ATOM   5352 H HD21   . LEU A 1 349 ? 1.46600   12.80900  22.47100 1.000 55.78682  ?  349 LEU A HD21   1 
ATOM   5353 H HD22   . LEU A 1 349 ? 2.06000   14.27600  22.61100 1.000 55.78682  ?  349 LEU A HD22   1 
ATOM   5354 H HD23   . LEU A 1 349 ? 0.64900   14.05300  21.91500 1.000 55.78682  ?  349 LEU A HD23   1 
ATOM   5355 N N      . VAL A 1 350 ? 0.60800   14.19300  17.61400 1.000 46.62147  ?  350 VAL A N      1 
ATOM   5356 C CA     A VAL A 1 350 ? -0.29400  13.25000  16.96300 0.580 49.79345  ?  350 VAL A CA     1 
ATOM   5357 C CA     B VAL A 1 350 ? -0.29000  13.24700  16.96700 0.420 43.33944  ?  350 VAL A CA     1 
ATOM   5358 C C      . VAL A 1 350 ? -0.00500  13.15300  15.47300 1.000 41.15955  ?  350 VAL A C      1 
ATOM   5359 O O      . VAL A 1 350 ? -0.10200  12.07600  14.88200 1.000 49.58775  ?  350 VAL A O      1 
ATOM   5360 C CB     A VAL A 1 350 ? -1.75500  13.66000  17.23500 0.580 47.63391  ?  350 VAL A CB     1 
ATOM   5361 C CB     B VAL A 1 350 ? -1.77000  13.62100  17.21800 0.420 46.73007  ?  350 VAL A CB     1 
ATOM   5362 C CG1    A VAL A 1 350 ? -2.70800  12.83400  16.38900 0.580 53.90291  ?  350 VAL A CG1    1 
ATOM   5363 C CG1    B VAL A 1 350 ? -2.12400  13.40900  18.68800 0.420 48.27449  ?  350 VAL A CG1    1 
ATOM   5364 C CG2    A VAL A 1 350 ? -2.07900  13.50800  18.71900 0.580 48.33048  ?  350 VAL A CG2    1 
ATOM   5365 C CG2    B VAL A 1 350 ? -2.05400  15.05100  16.79200 0.420 51.45678  ?  350 VAL A CG2    1 
ATOM   5366 H H      A VAL A 1 350 ? 0.23400   14.92400  17.87200 0.580 56.06353  ?  350 VAL A H      1 
ATOM   5367 H H      B VAL A 1 350 ? 0.23600   14.92500  17.87000 0.420 56.06353  ?  350 VAL A H      1 
ATOM   5368 H HA     A VAL A 1 350 ? -0.14400  12.37000  17.34100 0.580 59.86991  ?  350 VAL A HA     1 
ATOM   5369 H HA     B VAL A 1 350 ? -0.13200  12.37100  17.35200 0.420 52.12510  ?  350 VAL A HA     1 
ATOM   5370 H HB     A VAL A 1 350 ? -1.87200  14.59200  16.99200 0.580 57.27846  ?  350 VAL A HB     1 
ATOM   5371 H HB     B VAL A 1 350 ? -2.33300  13.04200  16.68000 0.420 56.19386  ?  350 VAL A HB     1 
ATOM   5372 H HG11   A VAL A 1 350 ? -3.60200  12.90900  16.75600 0.580 64.80126  ?  350 VAL A HG11   1 
ATOM   5373 H HG11   B VAL A 1 350 ? -3.06000  13.62700  18.82200 0.420 58.04716  ?  350 VAL A HG11   1 
ATOM   5374 H HG12   A VAL A 1 350 ? -2.69400  13.17000  15.47900 0.580 64.80126  ?  350 VAL A HG12   1 
ATOM   5375 H HG12   B VAL A 1 350 ? -1.96400  12.48100  18.92100 0.420 58.04716  ?  350 VAL A HG12   1 
ATOM   5376 H HG13   A VAL A 1 350 ? -2.42100  11.90700  16.40400 0.580 64.80126  ?  350 VAL A HG13   1 
ATOM   5377 H HG13   B VAL A 1 350 ? -1.56900  13.98800  19.23300 0.420 58.04716  ?  350 VAL A HG13   1 
ATOM   5378 H HG21   A VAL A 1 350 ? -3.00500  13.75700  18.86700 0.580 58.11435  ?  350 VAL A HG21   1 
ATOM   5379 H HG21   B VAL A 1 350 ? -3.00400  15.22600  16.88800 0.420 61.86591  ?  350 VAL A HG21   1 
ATOM   5380 H HG22   A VAL A 1 350 ? -1.94000  12.58400  18.98000 0.580 58.11435  ?  350 VAL A HG22   1 
ATOM   5381 H HG22   B VAL A 1 350 ? -1.54800  15.65500  17.35700 0.420 61.86591  ?  350 VAL A HG22   1 
ATOM   5382 H HG23   A VAL A 1 350 ? -1.49500  14.08800  19.23100 0.580 58.11435  ?  350 VAL A HG23   1 
ATOM   5383 H HG23   B VAL A 1 350 ? -1.78900  15.16300  15.86600 0.420 61.86591  ?  350 VAL A HG23   1 
ATOM   5384 N N      . THR A 1 351 ? 0.34800   14.27700  14.83600 1.000 47.35104  ?  351 THR A N      1 
ATOM   5385 C CA     A THR A 1 351 ? 0.50500   14.30400  13.38300 0.370 45.27190  ?  351 THR A CA     1 
ATOM   5386 C CA     C THR A 1 351 ? 0.49000   14.27400  13.38200 0.630 44.02532  ?  351 THR A CA     1 
ATOM   5387 C C      . THR A 1 351 ? 1.86800   13.77100  12.94900 1.000 42.16835  ?  351 THR A C      1 
ATOM   5388 O O      . THR A 1 351 ? 1.96900   12.94200  12.03400 1.000 44.04974  ?  351 THR A O      1 
ATOM   5389 C CB     A THR A 1 351 ? 0.32400   15.73600  12.86500 0.370 45.96574  ?  351 THR A CB     1 
ATOM   5390 C CB     C THR A 1 351 ? 0.22800   15.67700  12.82400 0.630 45.93560  ?  351 THR A CB     1 
ATOM   5391 O OG1    A THR A 1 351 ? -0.75600  16.36900  13.56000 0.370 46.45638  ?  351 THR A OG1    1 
ATOM   5392 O OG1    C THR A 1 351 ? 0.99600   16.64300  13.53200 0.630 45.83969  ?  351 THR A OG1    1 
ATOM   5393 C CG2    A THR A 1 351 ? 0.04500   15.73000  11.36700 0.370 51.19856  ?  351 THR A CG2    1 
ATOM   5394 C CG2    C THR A 1 351 ? -1.25300  16.02300  12.95300 0.630 49.54765  ?  351 THR A CG2    1 
ATOM   5395 H H      A THR A 1 351 ? 0.50000   15.03000  15.22200 0.370 56.93902  ?  351 THR A H      1 
ATOM   5396 H H      C THR A 1 351 ? 0.50500   15.03200  15.21600 0.630 56.93902  ?  351 THR A H      1 
ATOM   5397 H HA     A THR A 1 351 ? -0.18000  13.73800  12.99300 0.370 54.44405  ?  351 THR A HA     1 
ATOM   5398 H HA     C THR A 1 351 ? -0.17400  13.67300  13.00900 0.630 52.94815  ?  351 THR A HA     1 
ATOM   5399 H HB     A THR A 1 351 ? 1.13700   16.24400  13.01700 0.370 55.27665  ?  351 THR A HB     1 
ATOM   5400 H HB     C THR A 1 351 ? 0.48000   15.70100  11.88800 0.630 55.24049  ?  351 THR A HB     1 
ATOM   5401 H HG1    A THR A 1 351 ? -0.87100  17.14700  13.26600 0.370 55.86543  ?  351 THR A HG1    1 
ATOM   5402 H HG1    C THR A 1 351 ? 0.85300   17.40900  13.21900 0.630 55.12539  ?  351 THR A HG1    1 
ATOM   5403 H HG21   A THR A 1 351 ? -0.13300  16.63300  11.05900 0.370 61.55605  ?  351 THR A HG21   1 
ATOM   5404 H HG21   C THR A 1 351 ? -1.42500  16.89600  12.56500 0.630 59.57495  ?  351 THR A HG21   1 
ATOM   5405 H HG22   A THR A 1 351 ? 0.81200   15.37900  10.88800 0.370 61.55605  ?  351 THR A HG22   1 
ATOM   5406 H HG22   C THR A 1 351 ? -1.79000  15.36200  12.48900 0.630 59.57495  ?  351 THR A HG22   1 
ATOM   5407 H HG23   A THR A 1 351 ? -0.72700  15.17400  11.17600 0.370 61.55605  ?  351 THR A HG23   1 
ATOM   5408 H HG23   C THR A 1 351 ? -1.51000  16.03900  13.88800 0.630 59.57495  ?  351 THR A HG23   1 
ATOM   5409 N N      . TRP A 1 352 ? 2.93400   14.24300  13.59900 1.000 47.28176  ?  352 TRP A N      1 
ATOM   5410 C CA     . TRP A 1 352 ? 4.29200   13.85000  13.24300 1.000 45.62622  ?  352 TRP A CA     1 
ATOM   5411 C C      . TRP A 1 352 ? 4.85300   12.75700  14.12900 1.000 40.77922  ?  352 TRP A C      1 
ATOM   5412 O O      . TRP A 1 352 ? 5.68700   11.97500  13.67000 1.000 41.25366  ?  352 TRP A O      1 
ATOM   5413 C CB     . TRP A 1 352 ? 5.24600   15.05400  13.31600 1.000 44.67404  ?  352 TRP A CB     1 
ATOM   5414 C CG     . TRP A 1 352 ? 5.14900   16.02400  12.16600 1.000 45.16013  ?  352 TRP A CG     1 
ATOM   5415 C CD1    . TRP A 1 352 ? 4.15400   16.11000  11.24000 1.000 48.67075  ?  352 TRP A CD1    1 
ATOM   5416 C CD2    . TRP A 1 352 ? 6.10000   17.04500  11.82400 1.000 45.26744  ?  352 TRP A CD2    1 
ATOM   5417 N NE1    . TRP A 1 352 ? 4.42200   17.11800  10.34200 1.000 47.48082  ?  352 TRP A NE1    1 
ATOM   5418 C CE2    . TRP A 1 352 ? 5.60700   17.71000  10.68300 1.000 48.47927  ?  352 TRP A CE2    1 
ATOM   5419 C CE3    . TRP A 1 352 ? 7.32100   17.45800  12.37300 1.000 46.95537  ?  352 TRP A CE3    1 
ATOM   5420 C CZ2    . TRP A 1 352 ? 6.29000   18.77300  10.07700 1.000 51.24814  ?  352 TRP A CZ2    1 
ATOM   5421 C CZ3    . TRP A 1 352 ? 7.99500   18.51700  11.77400 1.000 46.98785  ?  352 TRP A CZ3    1 
ATOM   5422 C CH2    . TRP A 1 352 ? 7.47900   19.16100  10.64300 1.000 50.66007  ?  352 TRP A CH2    1 
ATOM   5423 H H      . TRP A 1 352 ? 2.89300   14.79700  14.25600 1.000 56.85588  ?  352 TRP A H      1 
ATOM   5424 H HA     . TRP A 1 352 ? 4.27800   13.52900  12.32800 1.000 54.86923  ?  352 TRP A HA     1 
ATOM   5425 H HB2    . TRP A 1 352 ? 5.05300   15.54900  14.12800 1.000 53.72662  ?  352 TRP A HB2    1 
ATOM   5426 H HB3    . TRP A 1 352 ? 6.15700   14.72200  13.33900 1.000 53.72662  ?  352 TRP A HB3    1 
ATOM   5427 H HD1    . TRP A 1 352 ? 3.40000   15.56500  11.21900 1.000 58.52267  ?  352 TRP A HD1    1 
ATOM   5428 H HE1    . TRP A 1 352 ? 3.92500   17.33900  9.67600  1.000 57.09475  ?  352 TRP A HE1    1 
ATOM   5429 H HE3    . TRP A 1 352 ? 7.67300   17.03300  13.12200 1.000 56.46421  ?  352 TRP A HE3    1 
ATOM   5430 H HZ2    . TRP A 1 352 ? 5.95200   19.19800  9.32200  1.000 61.61554  ?  352 TRP A HZ2    1 
ATOM   5431 H HZ3    . TRP A 1 352 ? 8.80500   18.80200  12.13200 1.000 56.50319  ?  352 TRP A HZ3    1 
ATOM   5432 H HH2    . TRP A 1 352 ? 7.95200   19.86800  10.26700 1.000 60.90985  ?  352 TRP A HH2    1 
ATOM   5433 N N      . GLY A 1 353 ? 4.41900   12.68300  15.39500 1.000 43.49333  ?  353 GLY A N      1 
ATOM   5434 C CA     . GLY A 1 353 ? 4.99100   11.73200  16.31700 1.000 45.09163  ?  353 GLY A CA     1 
ATOM   5435 C C      . GLY A 1 353 ? 6.36800   12.11600  16.81100 1.000 46.38465  ?  353 GLY A C      1 
ATOM   5436 O O      . GLY A 1 353 ? 7.07700   11.25900  17.36400 1.000 42.78191  ?  353 GLY A O      1 
ATOM   5437 H H      . GLY A 1 353 ? 3.79900   13.17500  15.73000 1.000 52.30977  ?  353 GLY A H      1 
ATOM   5438 H HA2    . GLY A 1 353 ? 4.40700   11.64900  17.08700 1.000 54.22772  ?  353 GLY A HA2    1 
ATOM   5439 H HA3    . GLY A 1 353 ? 5.05900   10.86900  15.87800 1.000 54.22772  ?  353 GLY A HA3    1 
ATOM   5440 N N      . TRP A 1 354 ? 6.76900   13.35700  16.61700 1.000 39.58416  ?  354 TRP A N      1 
ATOM   5441 C CA     . TRP A 1 354 ? 8.06600   13.85200  17.05600 1.000 38.99101  ?  354 TRP A CA     1 
ATOM   5442 C C      . TRP A 1 354 ? 7.93100   15.35400  17.30300 1.000 43.23508  ?  354 TRP A C      1 
ATOM   5443 O O      . TRP A 1 354 ? 7.28300   16.06300  16.52500 1.000 40.70351  ?  354 TRP A O      1 
ATOM   5444 C CB     . TRP A 1 354 ? 9.15300   13.58000  16.02100 1.000 46.81351  ?  354 TRP A CB     1 
ATOM   5445 C CG     . TRP A 1 354 ? 10.51600  14.07200  16.42800 1.000 47.07885  ?  354 TRP A CG     1 
ATOM   5446 C CD1    . TRP A 1 354 ? 11.52500  13.33600  16.96500 1.000 38.44292  ?  354 TRP A CD1    1 
ATOM   5447 C CD2    . TRP A 1 354 ? 11.01600  15.41600  16.31800 1.000 44.10577  ?  354 TRP A CD2    1 
ATOM   5448 N NE1    . TRP A 1 354 ? 12.61700  14.12900  17.20900 1.000 42.33054  ?  354 TRP A NE1    1 
ATOM   5449 C CE2    . TRP A 1 354 ? 12.33900  15.41000  16.81700 1.000 44.58708  ?  354 TRP A CE2    1 
ATOM   5450 C CE3    . TRP A 1 354 ? 10.48200  16.61300  15.83600 1.000 45.39542  ?  354 TRP A CE3    1 
ATOM   5451 C CZ2    . TRP A 1 354 ? 13.12600  16.55100  16.85600 1.000 44.42671  ?  354 TRP A CZ2    1 
ATOM   5452 C CZ3    . TRP A 1 354 ? 11.25900  17.75600  15.87900 1.000 44.86931  ?  354 TRP A CZ3    1 
ATOM   5453 C CH2    . TRP A 1 354 ? 12.57600  17.71900  16.38300 1.000 44.11165  ?  354 TRP A CH2    1 
ATOM   5454 H H      . TRP A 1 354 ? 6.29500   13.95600  16.22000 1.000 47.61876  ?  354 TRP A H      1 
ATOM   5455 H HA     . TRP A 1 354 ? 8.33200   13.41500  17.88000 1.000 46.90698  ?  354 TRP A HA     1 
ATOM   5456 H HB2    . TRP A 1 354 ? 9.21500   12.62200  15.87900 1.000 56.29398  ?  354 TRP A HB2    1 
ATOM   5457 H HB3    . TRP A 1 354 ? 8.91400   14.02400  15.19300 1.000 56.29398  ?  354 TRP A HB3    1 
ATOM   5458 H HD1    . TRP A 1 354 ? 11.48100  12.42400  17.14200 1.000 46.24927  ?  354 TRP A HD1    1 
ATOM   5459 H HE1    . TRP A 1 354 ? 13.35900  13.86400  17.55400 1.000 50.91441  ?  354 TRP A HE1    1 
ATOM   5460 H HE3    . TRP A 1 354 ? 9.61900   16.64100  15.49100 1.000 54.59228  ?  354 TRP A HE3    1 
ATOM   5461 H HZ2    . TRP A 1 354 ? 13.99300  16.52800  17.19100 1.000 53.42982  ?  354 TRP A HZ2    1 
ATOM   5462 H HZ3    . TRP A 1 354 ? 10.90800  18.56100  15.57100 1.000 53.96094  ?  354 TRP A HZ3    1 
ATOM   5463 H HH2    . TRP A 1 354 ? 13.08200  18.50000  16.39500 1.000 53.05175  ?  354 TRP A HH2    1 
ATOM   5464 N N      . MET A 1 355 ? 8.52600   15.82000  18.38600 1.000 36.18039  ?  355 MET A N      1 
ATOM   5465 C CA     . MET A 1 355 ? 8.59000   17.24300  18.68300 1.000 40.44901  ?  355 MET A CA     1 
ATOM   5466 C C      . MET A 1 355 ? 9.94400   17.53500  19.29000 1.000 45.84304  ?  355 MET A C      1 
ATOM   5467 O O      . MET A 1 355 ? 10.59200  16.65800  19.89100 1.000 39.36352  ?  355 MET A O      1 
ATOM   5468 C CB     . MET A 1 355 ? 7.48100   17.68600  19.64700 1.000 42.36505  ?  355 MET A CB     1 
ATOM   5469 C CG     . MET A 1 355 ? 6.15000   17.01900  19.37300 1.000 42.79212  ?  355 MET A CG     1 
ATOM   5470 S SD     . MET A 1 355 ? 5.92900   15.56300  20.42300 1.000 46.43858  ?  355 MET A SD     1 
ATOM   5471 C CE     . MET A 1 355 ? 5.79000   16.35300  22.03600 1.000 42.29286  ?  355 MET A CE     1 
ATOM   5472 H H      . MET A 1 355 ? 8.90800   15.32500  18.97700 1.000 43.53424  ?  355 MET A H      1 
ATOM   5473 H HA     . MET A 1 355 ? 8.47800   17.74700  17.86100 1.000 48.65659  ?  355 MET A HA     1 
ATOM   5474 H HB2    . MET A 1 355 ? 7.74600   17.46300  20.55300 1.000 50.95583  ?  355 MET A HB2    1 
ATOM   5475 H HB3    . MET A 1 355 ? 7.35700   18.64500  19.56400 1.000 50.95583  ?  355 MET A HB3    1 
ATOM   5476 H HG2    . MET A 1 355 ? 5.43100   17.64400  19.55800 1.000 51.46831  ?  355 MET A HG2    1 
ATOM   5477 H HG3    . MET A 1 355 ? 6.11400   16.73800  18.44500 1.000 51.46831  ?  355 MET A HG3    1 
ATOM   5478 H HE1    . MET A 1 355 ? 5.67600   15.66900  22.71400 1.000 50.86920  ?  355 MET A HE1    1 
ATOM   5479 H HE2    . MET A 1 355 ? 6.59800   16.86000  22.21000 1.000 50.86920  ?  355 MET A HE2    1 
ATOM   5480 H HE3    . MET A 1 355 ? 5.02200   16.94600  22.03100 1.000 50.86920  ?  355 MET A HE3    1 
ATOM   5481 N N      . HIS A 1 356 ? 10.37300  18.79700  19.13800 1.000 43.37748  ?  356 HIS A N      1 
ATOM   5482 C CA     . HIS A 1 356 ? 11.64400  19.20800  19.72100 1.000 40.56355  ?  356 HIS A CA     1 
ATOM   5483 C C      . HIS A 1 356 ? 11.63600  18.95500  21.22200 1.000 45.27381  ?  356 HIS A C      1 
ATOM   5484 O O      . HIS A 1 356 ? 10.59100  18.99300  21.88700 1.000 42.85294  ?  356 HIS A O      1 
ATOM   5485 C CB     . HIS A 1 356 ? 11.90900  20.67600  19.41600 1.000 42.27226  ?  356 HIS A CB     1 
ATOM   5486 C CG     . HIS A 1 356 ? 13.27300  21.13900  19.81600 1.000 38.39268  ?  356 HIS A CG     1 
ATOM   5487 N ND1    . HIS A 1 356 ? 13.55600  21.62200  21.06900 1.000 43.19254  ?  356 HIS A ND1    1 
ATOM   5488 C CD2    . HIS A 1 356 ? 14.43000  21.22200  19.10800 1.000 41.72939  ?  356 HIS A CD2    1 
ATOM   5489 C CE1    . HIS A 1 356 ? 14.83500  21.97400  21.13100 1.000 41.06594  ?  356 HIS A CE1    1 
ATOM   5490 N NE2    . HIS A 1 356 ? 15.38900  21.74300  19.95200 1.000 41.33684  ?  356 HIS A NE2    1 
ATOM   5491 H H      . HIS A 1 356 ? 9.95300   19.41400  18.71100 1.000 52.17075  ?  356 HIS A H      1 
ATOM   5492 H HA     . HIS A 1 356 ? 12.37100  18.69500  19.33600 1.000 48.79402  ?  356 HIS A HA     1 
ATOM   5493 H HB2    . HIS A 1 356 ? 11.81600  20.81800  18.46100 1.000 50.84449  ?  356 HIS A HB2    1 
ATOM   5494 H HB3    . HIS A 1 356 ? 11.26100  21.21600  19.89600 1.000 50.84449  ?  356 HIS A HB3    1 
ATOM   5495 H HD2    . HIS A 1 356 ? 14.55200  20.97300  18.22000 1.000 50.19303  ?  356 HIS A HD2    1 
ATOM   5496 H HE1    . HIS A 1 356 ? 15.26800  22.32300  21.87700 1.000 49.39689  ?  356 HIS A HE1    1 
ATOM   5497 H HE2    . HIS A 1 356 ? 16.21000  21.89400  19.74500 1.000 49.72197  ?  356 HIS A HE2    1 
ATOM   5498 N N      . HIS A 1 357 ? 12.83400  18.67900  21.76000 1.000 43.80782  ?  357 HIS A N      1 
ATOM   5499 C CA     . HIS A 1 357 ? 12.96000  18.36200  23.18000 1.000 43.30352  ?  357 HIS A CA     1 
ATOM   5500 C C      . HIS A 1 357 ? 12.26400  19.40300  24.06900 1.000 46.29233  ?  357 HIS A C      1 
ATOM   5501 O O      . HIS A 1 357 ? 11.55100  19.04100  25.01100 1.000 47.14978  ?  357 HIS A O      1 
ATOM   5502 C CB     . HIS A 1 357 ? 14.44500  18.27500  23.54300 1.000 44.31618  ?  357 HIS A CB     1 
ATOM   5503 C CG     . HIS A 1 357 ? 14.69700  18.03500  24.99100 1.000 42.11345  ?  357 HIS A CG     1 
ATOM   5504 N ND1    . HIS A 1 357 ? 14.43300  16.83300  25.60000 1.000 47.89127  ?  357 HIS A ND1    1 
ATOM   5505 C CD2    . HIS A 1 357 ? 15.19300  18.84900  25.95500 1.000 42.19634  ?  357 HIS A CD2    1 
ATOM   5506 C CE1    . HIS A 1 357 ? 14.74800  16.91000  26.88400 1.000 45.48783  ?  357 HIS A CE1    1 
ATOM   5507 N NE2    . HIS A 1 357 ? 15.22200  18.12300  27.11900 1.000 45.14930  ?  357 HIS A NE2    1 
ATOM   5508 H H      . HIS A 1 357 ? 13.57600  18.66900  21.32500 1.000 52.68716  ?  357 HIS A H      1 
ATOM   5509 H HA     . HIS A 1 357 ? 12.53400  17.50600  23.34300 1.000 52.08200  ?  357 HIS A HA     1 
ATOM   5510 H HB2    . HIS A 1 357 ? 14.84400  17.54200  23.04800 1.000 53.29719  ?  357 HIS A HB2    1 
ATOM   5511 H HB3    . HIS A 1 357 ? 14.87500  19.11100  23.30200 1.000 53.29719  ?  357 HIS A HB3    1 
ATOM   5512 H HD1    . HIS A 1 357 ? 14.11200  16.13800  25.20900 1.000 57.58730  ?  357 HIS A HD1    1 
ATOM   5513 H HD2    . HIS A 1 357 ? 15.46300  19.73200  25.84800 1.000 50.75337  ?  357 HIS A HD2    1 
ATOM   5514 H HE1    . HIS A 1 357 ? 14.65400  16.23000  27.51200 1.000 54.70316  ?  357 HIS A HE1    1 
ATOM   5515 N N      . LEU A 1 358 ? 12.47400  20.68800  23.78300 1.000 45.00093  ?  358 LEU A N      1 
ATOM   5516 C CA     . LEU A 1 358 ? 11.90600  21.74800  24.61900 1.000 46.62692  ?  358 LEU A CA     1 
ATOM   5517 C C      . LEU A 1 358 ? 10.40200  21.95800  24.37400 1.000 44.15091  ?  358 LEU A C      1 
ATOM   5518 O O      . LEU A 1 358 ? 9.73500   22.53000  25.23400 1.000 47.83112  ?  358 LEU A O      1 
ATOM   5519 C CB     . LEU A 1 358 ? 12.64700  23.05100  24.39300 1.000 44.25319  ?  358 LEU A CB     1 
ATOM   5520 C CG     . LEU A 1 358 ? 14.07200  23.12400  24.94800 1.000 50.72801  ?  358 LEU A CG     1 
ATOM   5521 C CD1    . LEU A 1 358 ? 14.66000  24.51000  24.72000 1.000 54.46074  ?  358 LEU A CD1    1 
ATOM   5522 C CD2    . LEU A 1 358 ? 14.13000  22.77100  26.43400 1.000 54.76953  ?  358 LEU A CD2    1 
ATOM   5523 H H      . LEU A 1 358 ? 12.93800  20.97100  23.11700 1.000 54.11889  ?  358 LEU A H      1 
ATOM   5524 H HA     . LEU A 1 358 ? 12.02200  21.50000  25.54900 1.000 56.07007  ?  358 LEU A HA     1 
ATOM   5525 H HB2    . LEU A 1 358 ? 12.70500  23.20300  23.43600 1.000 53.22160  ?  358 LEU A HB2    1 
ATOM   5526 H HB3    . LEU A 1 358 ? 12.14000  23.76300  24.81200 1.000 53.22160  ?  358 LEU A HB3    1 
ATOM   5527 H HG     . LEU A 1 358 ? 14.60700  22.46900  24.47400 1.000 60.99138  ?  358 LEU A HG     1 
ATOM   5528 H HD11   . LEU A 1 358 ? 15.55800  24.53600  25.08400 1.000 65.47066  ?  358 LEU A HD11   1 
ATOM   5529 H HD12   . LEU A 1 358 ? 14.68400  24.69100  23.76700 1.000 65.47066  ?  358 LEU A HD12   1 
ATOM   5530 H HD13   . LEU A 1 358 ? 14.10300  25.16700  25.16700 1.000 65.47066  ?  358 LEU A HD13   1 
ATOM   5531 H HD21   . LEU A 1 358 ? 15.02100  22.95800  26.76800 1.000 65.84120  ?  358 LEU A HD21   1 
ATOM   5532 H HD22   . LEU A 1 358 ? 13.47800  23.30700  26.91200 1.000 65.84120  ?  358 LEU A HD22   1 
ATOM   5533 H HD23   . LEU A 1 358 ? 13.92800  21.82800  26.54300 1.000 65.84120  ?  358 LEU A HD23   1 
ATOM   5534 N N      . ALA A 1 359 ? 9.87700   21.53900  23.22100 1.000 41.36242  ?  359 ALA A N      1 
ATOM   5535 C CA     . ALA A 1 359 ? 8.43900   21.44400  23.06000 1.000 42.60628  ?  359 ALA A CA     1 
ATOM   5536 C C      . ALA A 1 359 ? 7.87000   20.32000  23.93100 1.000 45.48101  ?  359 ALA A C      1 
ATOM   5537 O O      . ALA A 1 359 ? 6.83000   20.49700  24.57800 1.000 43.92633  ?  359 ALA A O      1 
ATOM   5538 C CB     . ALA A 1 359 ? 8.08600   21.21100  21.59600 1.000 47.66317  ?  359 ALA A CB     1 
ATOM   5539 H H      . ALA A 1 359 ? 10.33100  21.30800  22.52800 1.000 49.75267  ?  359 ALA A H      1 
ATOM   5540 H HA     . ALA A 1 359 ? 8.03600   22.28200  23.33400 1.000 51.24530  ?  359 ALA A HA     1 
ATOM   5541 H HB1    . ALA A 1 359 ? 7.12300   21.13100  21.51200 1.000 57.31358  ?  359 ALA A HB1    1 
ATOM   5542 H HB2    . ALA A 1 359 ? 8.40300   21.96300  21.07100 1.000 57.31358  ?  359 ALA A HB2    1 
ATOM   5543 H HB3    . ALA A 1 359 ? 8.51300   20.39400  21.29400 1.000 57.31358  ?  359 ALA A HB3    1 
ATOM   5544 N N      . ARG A 1 360 ? 8.55900   19.17800  23.98400 1.000 39.08278  ?  360 ARG A N      1 
ATOM   5545 C CA     . ARG A 1 360 ? 8.16700   18.10800  24.89900 1.000 44.59045  ?  360 ARG A CA     1 
ATOM   5546 C C      . ARG A 1 360 ? 8.19400   18.58900  26.33800 1.000 46.07123  ?  360 ARG A C      1 
ATOM   5547 O O      . ARG A 1 360 ? 7.29500   18.26500  27.12600 1.000 47.81214  ?  360 ARG A O      1 
ATOM   5548 C CB     . ARG A 1 360 ? 9.09800   16.89200  24.72800 1.000 41.26384  ?  360 ARG A CB     1 
ATOM   5549 C CG     . ARG A 1 360 ? 8.90200   16.16000  23.40500 1.000 40.81599  ?  360 ARG A CG     1 
ATOM   5550 C CD     . ARG A 1 360 ? 9.72600   14.87800  23.28400 1.000 42.03071  ?  360 ARG A CD     1 
ATOM   5551 N NE     . ARG A 1 360 ? 10.08700  14.61700  21.89700 1.000 41.97179  ?  360 ARG A NE     1 
ATOM   5552 C CZ     . ARG A 1 360 ? 10.37400  13.42100  21.39800 1.000 42.03922  ?  360 ARG A CZ     1 
ATOM   5553 N NH1    . ARG A 1 360 ? 10.29700  12.31900  22.13700 1.000 43.16401  ?  360 ARG A NH1    1 
ATOM   5554 N NH2    . ARG A 1 360 ? 10.75100  13.32700  20.12400 1.000 39.86286  ?  360 ARG A NH2    1 
ATOM   5555 H H      . ARG A 1 360 ? 9.25100   19.00000  23.50400 1.000 47.01710  ?  360 ARG A H      1 
ATOM   5556 H HA     . ARG A 1 360 ? 7.26300   17.82800  24.68400 1.000 53.62631  ?  360 ARG A HA     1 
ATOM   5557 H HB2    . ARG A 1 360 ? 10.01800  17.19500  24.76600 1.000 49.63438  ?  360 ARG A HB2    1 
ATOM   5558 H HB3    . ARG A 1 360 ? 8.92500   16.26200  25.44500 1.000 49.63438  ?  360 ARG A HB3    1 
ATOM   5559 H HG2    . ARG A 1 360 ? 7.96600   15.92000  23.31600 1.000 49.09695  ?  360 ARG A HG2    1 
ATOM   5560 H HG3    . ARG A 1 360 ? 9.16300   16.74900  22.68000 1.000 49.09695  ?  360 ARG A HG3    1 
ATOM   5561 H HD2    . ARG A 1 360 ? 10.54100  14.96800  23.80200 1.000 50.55462  ?  360 ARG A HD2    1 
ATOM   5562 H HD3    . ARG A 1 360 ? 9.20500   14.12800  23.61200 1.000 50.55462  ?  360 ARG A HD3    1 
ATOM   5563 H HE     . ARG A 1 360 ? 10.11700  15.28800  21.36100 1.000 50.48392  ?  360 ARG A HE     1 
ATOM   5564 H HH11   . ARG A 1 360 ? 10.05700  12.37000  22.96100 1.000 51.91458  ?  360 ARG A HH11   1 
ATOM   5565 H HH12   . ARG A 1 360 ? 10.48800  11.55500  21.79100 1.000 51.91458  ?  360 ARG A HH12   1 
ATOM   5566 H HH21   . ARG A 1 360 ? 10.80500  14.03400  19.63900 1.000 47.95320  ?  360 ARG A HH21   1 
ATOM   5567 H HH22   . ARG A 1 360 ? 10.93900  12.55800  19.78800 1.000 47.95320  ?  360 ARG A HH22   1 
ATOM   5568 N N      . HIS A 1 361 ? 9.22700   19.35700  26.70400 1.000 46.62016  ?  361 HIS A N      1 
ATOM   5569 C CA     . HIS A 1 361 ? 9.30700   19.92500  28.04300 1.000 46.98053  ?  361 HIS A CA     1 
ATOM   5570 C C      . HIS A 1 361 ? 8.10600   20.82300  28.33500 1.000 53.38352  ?  361 HIS A C      1 
ATOM   5571 O O      . HIS A 1 361 ? 7.51900   20.75000  29.42200 1.000 52.49325  ?  361 HIS A O      1 
ATOM   5572 C CB     . HIS A 1 361 ? 10.61400  20.71900  28.17400 1.000 53.68299  ?  361 HIS A CB     1 
ATOM   5573 C CG     . HIS A 1 361 ? 11.06600  20.92300  29.58300 1.000 56.95204  ?  361 HIS A CG     1 
ATOM   5574 N ND1    . HIS A 1 361 ? 11.61100  19.91200  30.34200 0.520 62.34092  ?  361 HIS A ND1    1 
ATOM   5575 C CD2    . HIS A 1 361 ? 11.06500  22.02600  30.36900 1.000 69.50158  ?  361 HIS A CD2    1 
ATOM   5576 C CE1    . HIS A 1 361 ? 11.91700  20.38100  31.54000 1.000 69.52736  ?  361 HIS A CE1    1 
ATOM   5577 N NE2    . HIS A 1 361 ? 11.59600  21.66300  31.58200 1.000 70.58795  ?  361 HIS A NE2    1 
ATOM   5578 H H      . HIS A 1 361 ? 9.88900   19.56100  26.19500 1.000 56.06196  ?  361 HIS A H      1 
ATOM   5579 H HA     . HIS A 1 361 ? 9.30900   19.20900  28.69800 1.000 56.49441  ?  361 HIS A HA     1 
ATOM   5580 H HB2    . HIS A 1 361 ? 11.31600  20.24000  27.70600 1.000 64.53736  ?  361 HIS A HB2    1 
ATOM   5581 H HB3    . HIS A 1 361 ? 10.48700  21.59400  27.77500 1.000 64.53736  ?  361 HIS A HB3    1 
ATOM   5582 H HD1    . HIS A 1 361 ? 11.73200  19.10200  30.07900 1.000 74.92687  ?  361 HIS A HD1    1 
ATOM   5583 H HD2    . HIS A 1 361 ? 10.76100  22.87200  30.13200 1.000 83.51967  ?  361 HIS A HD2    1 
ATOM   5584 H HE1    . HIS A 1 361 ? 12.29500  19.89200  32.23500 1.000 83.55060  ?  361 HIS A HE1    1 
ATOM   5585 N N      . SER A 1 362 ? 7.72700   21.66800  27.37300 1.000 46.96347  ?  362 SER A N      1 
ATOM   5586 C CA     . SER A 1 362 ? 6.64200   22.62200  27.59800 1.000 52.42633  ?  362 SER A CA     1 
ATOM   5587 C C      . SER A 1 362 ? 5.33600   21.91600  27.95300 1.000 52.43568  ?  362 SER A C      1 
ATOM   5588 O O      . SER A 1 362 ? 4.71400   22.21600  28.97300 1.000 54.38471  ?  362 SER A O      1 
ATOM   5589 C CB     . SER A 1 362 ? 6.44400   23.50000  26.35500 1.000 47.60072  ?  362 SER A CB     1 
ATOM   5590 O OG     . SER A 1 362 ? 7.42300   24.52700  26.29100 1.000 53.78876  ?  362 SER A OG     1 
ATOM   5591 H H      . SER A 1 362 ? 8.07900   21.70900  26.59000 1.000 56.47393  ?  362 SER A H      1 
ATOM   5592 H HA     . SER A 1 362 ? 6.89000   23.19100  28.34300 1.000 63.02936  ?  362 SER A HA     1 
ATOM   5593 H HB2    . SER A 1 362 ? 6.51800   22.94500  25.56300 1.000 57.23864  ?  362 SER A HB2    1 
ATOM   5594 H HB3    . SER A 1 362 ? 5.56400   23.90600  26.39400 1.000 57.23864  ?  362 SER A HB3    1 
ATOM   5595 H HG     . SER A 1 362 ? 7.46600   24.83500  25.51100 1.000 64.66428  ?  362 SER A HG     1 
ATOM   5596 N N      . VAL A 1 363 ? 4.92400   20.95200  27.12700 1.000 50.77574  ?  363 VAL A N      1 
ATOM   5597 C CA     . VAL A 1 363 ? 3.64100   20.29300  27.35600 1.000 58.46327  ?  363 VAL A CA     1 
ATOM   5598 C C      . VAL A 1 363 ? 3.69900   19.40600  28.58900 1.000 62.02444  ?  363 VAL A C      1 
ATOM   5599 O O      . VAL A 1 363 ? 2.68800   19.22800  29.27700 1.000 63.26278  ?  363 VAL A O      1 
ATOM   5600 C CB     . VAL A 1 363 ? 3.20200   19.50200  26.11000 1.000 50.20548  ?  363 VAL A CB     1 
ATOM   5601 C CG1    . VAL A 1 363 ? 2.98400   20.44800  24.92700 1.000 47.89619  ?  363 VAL A CG1    1 
ATOM   5602 C CG2    . VAL A 1 363 ? 4.22300   18.40200  25.75700 1.000 41.22015  ?  363 VAL A CG2    1 
ATOM   5603 H H      . VAL A 1 363 ? 5.36000   20.66700  26.44300 1.000 61.04865  ?  363 VAL A H      1 
ATOM   5604 H HA     . VAL A 1 363 ? 2.97600   20.98100  27.51600 1.000 70.27370  ?  363 VAL A HA     1 
ATOM   5605 H HB     . VAL A 1 363 ? 2.36100   19.06100  26.30600 1.000 60.36434  ?  363 VAL A HB     1 
ATOM   5606 H HG11   . VAL A 1 363 ? 2.64000   19.94100  24.17500 1.000 57.59320  ?  363 VAL A HG11   1 
ATOM   5607 H HG12   . VAL A 1 363 ? 2.34700   21.13300  25.18300 1.000 57.59320  ?  363 VAL A HG12   1 
ATOM   5608 H HG13   . VAL A 1 363 ? 3.83100   20.85800  24.68900 1.000 57.59320  ?  363 VAL A HG13   1 
ATOM   5609 H HG21   . VAL A 1 363 ? 3.93300   17.95000  24.95000 1.000 49.58195  ?  363 VAL A HG21   1 
ATOM   5610 H HG22   . VAL A 1 363 ? 5.09100   18.81100  25.61400 1.000 49.58195  ?  363 VAL A HG22   1 
ATOM   5611 H HG23   . VAL A 1 363 ? 4.27200   17.77000  26.49100 1.000 49.58195  ?  363 VAL A HG23   1 
ATOM   5612 N N      . ALA A 1 364 ? 4.86900   18.82700  28.88300 1.000 50.69658  ?  364 ALA A N      1 
ATOM   5613 C CA     . ALA A 1 364 ? 4.98700   17.96800  30.05700 1.000 67.99087  ?  364 ALA A CA     1 
ATOM   5614 C C      . ALA A 1 364 ? 4.91500   18.77700  31.34800 1.000 74.98037  ?  364 ALA A C      1 
ATOM   5615 O O      . ALA A 1 364 ? 4.23200   18.38200  32.29700 1.000 71.41518  ?  364 ALA A O      1 
ATOM   5616 C CB     . ALA A 1 364 ? 6.28700   17.17100  29.99500 1.000 64.08175  ?  364 ALA A CB     1 
ATOM   5617 H H      . ALA A 1 364 ? 5.59200   18.91500  28.42600 1.000 60.95367  ?  364 ALA A H      1 
ATOM   5618 H HA     . ALA A 1 364 ? 4.24900   17.33900  30.05800 1.000 81.70682  ?  364 ALA A HA     1 
ATOM   5619 H HB1    . ALA A 1 364 ? 6.35400   16.61300  30.78500 1.000 77.01587  ?  364 ALA A HB1    1 
ATOM   5620 H HB2    . ALA A 1 364 ? 6.27900   16.61600  29.19900 1.000 77.01587  ?  364 ALA A HB2    1 
ATOM   5621 H HB3    . ALA A 1 364 ? 7.03400   17.78800  29.96100 1.000 77.01587  ?  364 ALA A HB3    1 
ATOM   5622 N N      . CYS A 1 365 ? 5.62300   19.90800  31.40300 1.000 71.92438  ?  365 CYS A N      1 
ATOM   5623 C CA     . CYS A 1 365 ? 5.54200   20.77100  32.57600 1.000 74.71610  ?  365 CYS A CA     1 
ATOM   5624 C C      . CYS A 1 365 ? 4.14100   21.34900  32.73200 1.000 74.48148  ?  365 CYS A C      1 
ATOM   5625 O O      . CYS A 1 365 ? 3.60400   21.40400  33.84300 1.000 85.01683  ?  365 CYS A O      1 
ATOM   5626 C CB     . CYS A 1 365 ? 6.57900   21.88800  32.48100 1.000 68.61341  ?  365 CYS A CB     1 
ATOM   5627 S SG     . CYS A 1 365 ? 8.27900   21.35300  32.77900 1.000 69.69419  ?  365 CYS A SG     1 
ATOM   5628 H H      . CYS A 1 365 ? 6.14800   20.19200  30.78400 1.000 86.42702  ?  365 CYS A H      1 
ATOM   5629 H HA     . CYS A 1 365 ? 5.74200   20.24600  33.36700 1.000 89.77708  ?  365 CYS A HA     1 
ATOM   5630 H HB2    . CYS A 1 365 ? 6.54200   22.26900  31.59000 1.000 82.45386  ?  365 CYS A HB2    1 
ATOM   5631 H HB3    . CYS A 1 365 ? 6.36400   22.56600  33.14100 1.000 82.45386  ?  365 CYS A HB3    1 
ATOM   5632 H HG     . CYS A 1 365 ? 9.00100   22.31100  32.75400 1.000 83.75080  ?  365 CYS A HG     1 
ATOM   5633 N N      . PHE A 1 366 ? 3.53100   21.78300  31.62700 1.000 72.71889  ?  366 PHE A N      1 
ATOM   5634 C CA     . PHE A 1 366 ? 2.16500   22.28600  31.67700 1.000 80.71845  ?  366 PHE A CA     1 
ATOM   5635 C C      . PHE A 1 366 ? 1.18600   21.22000  32.14400 1.000 85.61968  ?  366 PHE A C      1 
ATOM   5636 O O      . PHE A 1 366 ? 0.08500   21.55500  32.58800 1.000 86.73521  ?  366 PHE A O      1 
ATOM   5637 C CB     . PHE A 1 366 ? 1.75000   22.81100  30.30100 1.000 107.85135 ?  366 PHE A CB     1 
ATOM   5638 C CG     . PHE A 1 366 ? 0.29700   23.18600  30.20200 1.000 112.70751 ?  366 PHE A CG     1 
ATOM   5639 C CD1    . PHE A 1 366 ? -0.16100  24.39000  30.71200 1.000 115.79070 ?  366 PHE A CD1    1 
ATOM   5640 C CD2    . PHE A 1 366 ? -0.61200  22.33800  29.59800 1.000 98.31662  ?  366 PHE A CD2    1 
ATOM   5641 C CE1    . PHE A 1 366 ? -1.49400  24.73600  30.62300 1.000 99.45550  ?  366 PHE A CE1    1 
ATOM   5642 C CE2    . PHE A 1 366 ? -1.94700  22.67800  29.50600 1.000 87.86395  ?  366 PHE A CE2    1 
ATOM   5643 C CZ     . PHE A 1 366 ? -2.38700  23.87900  30.01900 1.000 82.56116  ?  366 PHE A CZ     1 
ATOM   5644 H H      . PHE A 1 366 ? 3.88600   21.79500  30.84400 1.000 87.38044  ?  366 PHE A H      1 
ATOM   5645 H HA     . PHE A 1 366 ? 2.12400   23.02600  32.30200 1.000 96.97990  ?  366 PHE A HA     1 
ATOM   5646 H HB2    . PHE A 1 366 ? 2.27300   23.60200  30.09900 1.000 129.53938 ?  366 PHE A HB2    1 
ATOM   5647 H HB3    . PHE A 1 366 ? 1.92200   22.12200  29.64100 1.000 129.53938 ?  366 PHE A HB3    1 
ATOM   5648 H HD1    . PHE A 1 366 ? 0.43800   24.97200  31.12100 1.000 139.06661 ?  366 PHE A HD1    1 
ATOM   5649 H HD2    . PHE A 1 366 ? -0.32100  21.52600  29.24900 1.000 118.09772 ?  366 PHE A HD2    1 
ATOM   5650 H HE1    . PHE A 1 366 ? -1.78900  25.54700  30.97000 1.000 119.46437 ?  366 PHE A HE1    1 
ATOM   5651 H HE2    . PHE A 1 366 ? -2.54800  22.09800  29.09800 1.000 105.55451 ?  366 PHE A HE2    1 
ATOM   5652 H HZ     . PHE A 1 366 ? -3.28600  24.11000  29.95700 1.000 99.19116  ?  366 PHE A HZ     1 
ATOM   5653 N N      . LEU A 1 367 ? 1.55700   19.94700  32.05000 1.000 82.43374  ?  367 LEU A N      1 
ATOM   5654 C CA     . LEU A 1 367 ? 0.69600   18.87000  32.51500 1.000 90.23142  ?  367 LEU A CA     1 
ATOM   5655 C C      . LEU A 1 367 ? 1.00500   18.46700  33.95000 1.000 109.05058 ?  367 LEU A C      1 
ATOM   5656 O O      . LEU A 1 367 ? 0.08300   18.20200  34.72500 1.000 101.75366 ?  367 LEU A O      1 
ATOM   5657 C CB     . LEU A 1 367 ? 0.83200   17.65600  31.59200 1.000 78.42251  ?  367 LEU A CB     1 
ATOM   5658 C CG     . LEU A 1 367 ? -0.02500  16.44100  31.94800 1.000 92.19966  ?  367 LEU A CG     1 
ATOM   5659 C CD1    . LEU A 1 367 ? -1.47500  16.68000  31.56800 1.000 101.96478 ?  367 LEU A CD1    1 
ATOM   5660 C CD2    . LEU A 1 367 ? 0.50400   15.18400  31.27800 1.000 100.08270 ?  367 LEU A CD2    1 
ATOM   5661 H H      . LEU A 1 367 ? 2.30500   19.68200  31.71900 1.000 99.03826  ?  367 LEU A H      1 
ATOM   5662 H HA     . LEU A 1 367 ? -0.22600  19.16900  32.48000 1.000 108.39547 ?  367 LEU A HA     1 
ATOM   5663 H HB2    . LEU A 1 367 ? 0.58400   17.92900  30.69500 1.000 94.22478  ?  367 LEU A HB2    1 
ATOM   5664 H HB3    . LEU A 1 367 ? 1.75800   17.36800  31.60700 1.000 94.22478  ?  367 LEU A HB3    1 
ATOM   5665 H HG     . LEU A 1 367 ? 0.01700   16.30400  32.90700 1.000 110.75736 ?  367 LEU A HG     1 
ATOM   5666 H HD11   . LEU A 1 367 ? -1.98300  15.87100  31.73700 1.000 122.47551 ?  367 LEU A HD11   1 
ATOM   5667 H HD12   . LEU A 1 367 ? -1.82500  17.40900  32.10300 1.000 122.47551 ?  367 LEU A HD12   1 
ATOM   5668 H HD13   . LEU A 1 367 ? -1.52100  16.90900  30.62600 1.000 122.47551 ?  367 LEU A HD13   1 
ATOM   5669 H HD21   . LEU A 1 367 ? -0.06500  14.43600  31.51600 1.000 120.21701 ?  367 LEU A HD21   1 
ATOM   5670 H HD22   . LEU A 1 367 ? 0.49900   15.31100  30.31700 1.000 120.21701 ?  367 LEU A HD22   1 
ATOM   5671 H HD23   . LEU A 1 367 ? 1.41000   15.02000  31.58500 1.000 120.21701 ?  367 LEU A HD23   1 
ATOM   5672 N N      . THR A 1 368 ? 2.28000   18.43200  34.32600 1.000 104.84882 ?  368 THR A N      1 
ATOM   5673 C CA     . THR A 1 368 ? 2.69600   17.86500  35.60300 1.000 124.89352 ?  368 THR A CA     1 
ATOM   5674 C C      . THR A 1 368 ? 3.34700   18.86500  36.54300 1.000 112.86578 ?  368 THR A C      1 
ATOM   5675 O O      . THR A 1 368 ? 3.05200   18.85200  37.74000 1.000 111.13373 ?  368 THR A O      1 
ATOM   5676 C CB     . THR A 1 368 ? 3.67800   16.70100  35.36600 1.000 94.46238  ?  368 THR A CB     1 
ATOM   5677 O OG1    . THR A 1 368 ? 4.96200   17.22000  34.99900 1.000 100.98068 ?  368 THR A OG1    1 
ATOM   5678 C CG2    . THR A 1 368 ? 3.17000   15.78600  34.26300 1.000 103.18251 ?  368 THR A CG2    1 
ATOM   5679 H H      . THR A 1 368 ? 2.93000   18.73500  33.85200 1.000 125.93636 ?  368 THR A H      1 
ATOM   5680 H HA     . THR A 1 368 ? 1.90500   17.52100  36.04700 1.000 149.98999 ?  368 THR A HA     1 
ATOM   5681 H HB     . THR A 1 368 ? 3.76100   16.17900  36.18000 1.000 113.47263 ?  368 THR A HB     1 
ATOM   5682 H HG1    . THR A 1 368 ? 5.50200   16.58900  34.87300 1.000 121.29459 ?  368 THR A HG1    1 
ATOM   5683 H HG21   . THR A 1 368 ? 3.71600   14.98500  34.21900 1.000 123.93678 ?  368 THR A HG21   1 
ATOM   5684 H HG22   . THR A 1 368 ? 2.25100   15.53100  34.44100 1.000 123.93678 ?  368 THR A HG22   1 
ATOM   5685 H HG23   . THR A 1 368 ? 3.21100   16.24300  33.40900 1.000 123.93678 ?  368 THR A HG23   1 
ATOM   5686 N N      . ARG A 1 369 ? 4.21300   19.74200  36.04200 1.000 112.83133 ?  369 ARG A N      1 
ATOM   5687 C CA     . ARG A 1 369 ? 5.02700   20.59100  36.91900 1.000 101.34837 ?  369 ARG A CA     1 
ATOM   5688 C C      . ARG A 1 369 ? 4.19300   21.62400  37.70200 1.000 109.28080 ?  369 ARG A C      1 
ATOM   5689 O O      . ARG A 1 369 ? 4.77900   22.42900  38.43600 1.000 111.11796 ?  369 ARG A O      1 
ATOM   5690 C CB     . ARG A 1 369 ? 6.11800   21.28500  36.09400 1.000 106.79742 ?  369 ARG A CB     1 
ATOM   5691 C CG     . ARG A 1 369 ? 7.05700   22.18800  36.89600 1.000 105.89939 ?  369 ARG A CG     1 
ATOM   5692 C CD     . ARG A 1 369 ? 8.18800   22.74000  36.03400 1.000 103.00924 ?  369 ARG A CD     1 
ATOM   5693 N NE     . ARG A 1 369 ? 7.77200   23.94400  35.32300 1.000 107.52114 ?  369 ARG A NE     1 
ATOM   5694 C CZ     . ARG A 1 369 ? 8.26900   25.16000  35.52600 1.000 104.60669 ?  369 ARG A CZ     1 
ATOM   5695 N NH1    . ARG A 1 369 ? 9.24200   25.37800  36.39600 1.000 92.70702  ?  369 ARG A NH1    1 
ATOM   5696 N NH2    . ARG A 1 369 ? 7.77300   26.18300  34.83700 1.000 96.05742  ?  369 ARG A NH2    1 
ATOM   5697 H H      . ARG A 1 369 ? 4.34800   19.86700  35.20200 1.000 135.51537 ?  369 ARG A H      1 
ATOM   5698 H HA     . ARG A 1 369 ? 5.47000   20.03200  37.57700 1.000 121.73581 ?  369 ARG A HA     1 
ATOM   5699 H HB2    . ARG A 1 369 ? 6.66100   20.60400  35.66800 1.000 128.27468 ?  369 ARG A HB2    1 
ATOM   5700 H HB3    . ARG A 1 369 ? 5.68900   21.83700  35.42100 1.000 128.27468 ?  369 ARG A HB3    1 
ATOM   5701 H HG2    . ARG A 1 369 ? 6.55400   22.93700  37.25300 1.000 127.19704 ?  369 ARG A HG2    1 
ATOM   5702 H HG3    . ARG A 1 369 ? 7.45000   21.67700  37.62100 1.000 127.19704 ?  369 ARG A HG3    1 
ATOM   5703 H HD2    . ARG A 1 369 ? 8.94300   22.96400  36.60000 1.000 123.72886 ?  369 ARG A HD2    1 
ATOM   5704 H HD3    . ARG A 1 369 ? 8.44900   22.07300  35.38000 1.000 123.72886 ?  369 ARG A HD3    1 
ATOM   5705 H HE     . ARG A 1 369 ? 7.15900   23.86000  34.72700 1.000 129.14314 ?  369 ARG A HE     1 
ATOM   5706 H HH11   . ARG A 1 369 ? 9.56900   24.72300  36.84700 1.000 111.36619 ?  369 ARG A HH11   1 
ATOM   5707 H HH12   . ARG A 1 369 ? 9.54700   26.17400  36.51000 1.000 111.36619 ?  369 ARG A HH12   1 
ATOM   5708 H HH21   . ARG A 1 369 ? 7.13900   26.05300  34.27000 1.000 115.38667 ?  369 ARG A HH21   1 
ATOM   5709 H HH22   . ARG A 1 369 ? 8.08500   26.97500  34.95900 1.000 115.38667 ?  369 ARG A HH22   1 
ATOM   5710 N N      . GLY A 1 370 ? 2.86300   21.61800  37.62500 1.000 108.53712 ?  370 GLY A N      1 
ATOM   5711 C CA     . GLY A 1 370 ? 2.06900   22.47000  38.48900 1.000 111.45447 ?  370 GLY A CA     1 
ATOM   5712 C C      . GLY A 1 370 ? 1.07300   23.39200  37.81800 1.000 110.69125 ?  370 GLY A C      1 
ATOM   5713 O O      . GLY A 1 370 ? 0.69500   24.41800  38.39200 1.000 118.14808 ?  370 GLY A O      1 
ATOM   5714 H H      . GLY A 1 370 ? 2.40500   21.13100  37.08300 1.000 130.36231 ?  370 GLY A H      1 
ATOM   5715 H HA2    . GLY A 1 370 ? 1.56800   21.90300  39.09600 1.000 133.86314 ?  370 GLY A HA2    1 
ATOM   5716 H HA3    . GLY A 1 370 ? 2.67400   23.02800  39.00200 1.000 133.86314 ?  370 GLY A HA3    1 
ATOM   5717 N N      A ASP A 1 371 ? 0.63300   23.04700  36.61000 0.430 107.93852 ?  371 ASP A N      1 
ATOM   5718 N N      B ASP A 1 371 ? 0.65100   23.04500  36.60200 0.570 107.94379 ?  371 ASP A N      1 
ATOM   5719 C CA     A ASP A 1 371 ? -0.46600  23.74800  35.95500 0.430 107.88462 ?  371 ASP A CA     1 
ATOM   5720 C CA     B ASP A 1 371 ? -0.42500  23.74600  35.90900 0.570 107.88994 ?  371 ASP A CA     1 
ATOM   5721 C C      A ASP A 1 371 ? -1.74200  22.92000  35.93100 0.430 105.75026 ?  371 ASP A C      1 
ATOM   5722 C C      B ASP A 1 371 ? -1.72400  22.94700  35.92900 0.570 105.76249 ?  371 ASP A C      1 
ATOM   5723 O O      A ASP A 1 371 ? -2.81300  23.42200  36.28700 0.430 105.53402 ?  371 ASP A O      1 
ATOM   5724 O O      B ASP A 1 371 ? -2.76400  23.46200  36.34800 0.570 105.57754 ?  371 ASP A O      1 
ATOM   5725 C CB     A ASP A 1 371 ? -0.07000  24.14000  34.52300 0.430 105.39870 ?  371 ASP A CB     1 
ATOM   5726 C CB     B ASP A 1 371 ? -0.01600  24.04700  34.46100 0.570 104.68766 ?  371 ASP A CB     1 
ATOM   5727 C CG     A ASP A 1 371 ? 1.29200   24.80500  34.45800 0.430 107.80897 ?  371 ASP A CG     1 
ATOM   5728 C CG     B ASP A 1 371 ? -0.00300  25.53500  34.15600 0.570 106.82093 ?  371 ASP A CG     1 
ATOM   5729 O OD1    A ASP A 1 371 ? 2.29400   24.14300  34.80500 0.430 102.15148 ?  371 ASP A OD1    1 
ATOM   5730 O OD1    B ASP A 1 371 ? -1.09300  26.14200  34.08600 0.570 98.85402  ?  371 ASP A OD1    1 
ATOM   5731 O OD2    A ASP A 1 371 ? 1.36000   25.98600  34.05900 0.430 111.48819 -1 371 ASP A OD2    1 
ATOM   5732 O OD2    B ASP A 1 371 ? 1.09900   26.09900  33.98500 0.570 111.38944 -1 371 ASP A OD2    1 
ATOM   5733 H H      A ASP A 1 371 ? 0.95900   22.40100  36.14600 0.430 129.64400 ?  371 ASP A H      1 
ATOM   5734 H H      B ASP A 1 371 ? 0.98200   22.39300  36.15000 0.570 129.65032 ?  371 ASP A H      1 
ATOM   5735 H HA     A ASP A 1 371 ? -0.64700  24.56900  36.43900 0.430 129.57931 ?  371 ASP A HA     1 
ATOM   5736 H HA     B ASP A 1 371 ? -0.58300  24.59600  36.34800 0.570 129.58570 ?  371 ASP A HA     1 
ATOM   5737 H HB2    A ASP A 1 371 ? -0.04200  23.34200  33.97200 0.430 126.59621 ?  371 ASP A HB2    1 
ATOM   5738 H HB2    B ASP A 1 371 ? 0.87600   23.70000  34.30500 0.570 125.74296 ?  371 ASP A HB2    1 
ATOM   5739 H HB3    A ASP A 1 371 ? -0.72600  24.76200  34.17200 0.430 126.59621 ?  371 ASP A HB3    1 
ATOM   5740 H HB3    B ASP A 1 371 ? -0.64700  23.62200  33.85900 0.570 125.74296 ?  371 ASP A HB3    1 
ATOM   5741 N N      A LEU A 1 372 ? -1.65600  21.65400  35.52000 0.430 105.31916 ?  372 LEU A N      1 
ATOM   5742 N N      B LEU A 1 372 ? -1.68000  21.69200  35.48100 0.570 105.61937 ?  372 LEU A N      1 
ATOM   5743 C CA     A LEU A 1 372 ? -2.78200  20.73200  35.57800 0.430 103.81657 ?  372 LEU A CA     1 
ATOM   5744 C CA     B LEU A 1 372 ? -2.80500  20.77600  35.58800 0.570 104.09818 ?  372 LEU A CA     1 
ATOM   5745 C C      A LEU A 1 372 ? -2.66000  19.70100  36.69100 0.430 104.18534 ?  372 LEU A C      1 
ATOM   5746 C C      B LEU A 1 372 ? -2.57600  19.68800  36.63200 0.570 103.97728 ?  372 LEU A C      1 
ATOM   5747 O O      A LEU A 1 372 ? -3.68200  19.19600  37.16100 0.430 102.60369 ?  372 LEU A O      1 
ATOM   5748 O O      B LEU A 1 372 ? -3.47100  18.86700  36.85900 0.570 103.57203 ?  372 LEU A O      1 
ATOM   5749 C CB     A LEU A 1 372 ? -2.94200  20.00100  34.23800 0.430 99.31657  ?  372 LEU A CB     1 
ATOM   5750 C CB     B LEU A 1 372 ? -3.09200  20.12400  34.22900 0.570 99.06041  ?  372 LEU A CB     1 
ATOM   5751 C CG     A LEU A 1 372 ? -3.11500  20.89300  33.00700 0.430 95.44130  ?  372 LEU A CG     1 
ATOM   5752 C CG     B LEU A 1 372 ? -3.21800  21.05000  33.01900 0.570 95.33251  ?  372 LEU A CG     1 
ATOM   5753 C CD1    A LEU A 1 372 ? -3.19300  20.05000  31.74100 0.430 91.68155  ?  372 LEU A CD1    1 
ATOM   5754 C CD1    B LEU A 1 372 ? -3.23300  20.23300  31.73500 0.570 91.63187  ?  372 LEU A CD1    1 
ATOM   5755 C CD2    A LEU A 1 372 ? -4.34700  21.77900  33.13500 0.430 92.55013  ?  372 LEU A CD2    1 
ATOM   5756 C CD2    B LEU A 1 372 ? -4.46400  21.91300  33.11900 0.570 92.50817  ?  372 LEU A CD2    1 
ATOM   5757 H H      A LEU A 1 372 ? -0.94000  21.30200  35.19900 0.430 126.50076 ?  372 LEU A H      1 
ATOM   5758 H H      B LEU A 1 372 ? -0.99100  21.34300  35.10200 0.570 126.86101 ?  372 LEU A H      1 
ATOM   5759 H HA     A LEU A 1 372 ? -3.59500  21.23900  35.73100 0.430 124.69765 ?  372 LEU A HA     1 
ATOM   5760 H HA     B LEU A 1 372 ? -3.59100  21.28200  35.84700 0.570 125.03558 ?  372 LEU A HA     1 
ATOM   5761 H HB2    A LEU A 1 372 ? -2.15000  19.46000  34.09200 0.430 119.29765 ?  372 LEU A HB2    1 
ATOM   5762 H HB2    B LEU A 1 372 ? -2.36900  19.50700  34.03700 0.570 118.99026 ?  372 LEU A HB2    1 
ATOM   5763 H HB3    A LEU A 1 372 ? -3.72600  19.43300  34.29500 0.430 119.29765 ?  372 LEU A HB3    1 
ATOM   5764 H HB3    B LEU A 1 372 ? -3.93000  19.64200  34.30300 0.570 118.99026 ?  372 LEU A HB3    1 
ATOM   5765 H HG     A LEU A 1 372 ? -2.34200  21.47500  32.93800 0.430 114.64733 ?  372 LEU A HG     1 
ATOM   5766 H HG     B LEU A 1 372 ? -2.45200  21.64400  32.99700 0.570 114.51678 ?  372 LEU A HG     1 
ATOM   5767 H HD11   A LEU A 1 372 ? -3.39300  20.62800  30.98800 0.430 110.13563 ?  372 LEU A HD11   1 
ATOM   5768 H HD11   B LEU A 1 372 ? -3.43500  20.82000  30.99000 0.570 110.07601 ?  372 LEU A HD11   1 
ATOM   5769 H HD12   A LEU A 1 372 ? -2.34100  19.60900  31.60300 0.430 110.13563 ?  372 LEU A HD12   1 
ATOM   5770 H HD12   B LEU A 1 372 ? -2.36100  19.82700  31.60900 0.570 110.07601 ?  372 LEU A HD12   1 
ATOM   5771 H HD13   A LEU A 1 372 ? -3.89500  19.38800  31.84500 0.430 110.13563 ?  372 LEU A HD13   1 
ATOM   5772 H HD13   B LEU A 1 372 ? -3.91100  19.54300  31.80700 0.570 110.07601 ?  372 LEU A HD13   1 
ATOM   5773 H HD21   A LEU A 1 372 ? -4.46500  22.27700  32.31100 0.430 111.17793 ?  372 LEU A HD21   1 
ATOM   5774 H HD21   B LEU A 1 372 ? -4.49800  22.50700  32.35300 0.570 111.12757 ?  372 LEU A HD21   1 
ATOM   5775 H HD22   A LEU A 1 372 ? -5.12200  21.22000  33.29800 0.430 111.17793 ?  372 LEU A HD22   1 
ATOM   5776 H HD22   B LEU A 1 372 ? -5.24600  21.34000  33.12800 0.570 111.12757 ?  372 LEU A HD22   1 
ATOM   5777 H HD23   A LEU A 1 372 ? -4.21900  22.39100  33.87700 0.430 111.17793 ?  372 LEU A HD23   1 
ATOM   5778 H HD23   B LEU A 1 372 ? -4.42400  22.43200  33.93800 0.570 111.12757 ?  372 LEU A HD23   1 
ATOM   5779 N N      A TYR A 1 373 ? -1.43900  19.38000  37.12100 0.430 104.43620 ?  373 TYR A N      1 
ATOM   5780 N N      B TYR A 1 373 ? -1.40400  19.66200  37.27000 0.570 104.69238 ?  373 TYR A N      1 
ATOM   5781 C CA     A TYR A 1 373 ? -1.17200  18.50900  38.26100 0.430 105.77400 ?  373 TYR A CA     1 
ATOM   5782 C CA     B TYR A 1 373 ? -1.03200  18.59500  38.19200 0.570 105.82409 ?  373 TYR A CA     1 
ATOM   5783 C C      A TYR A 1 373 ? -1.60900  17.06500  38.03400 0.430 105.22185 ?  373 TYR A C      1 
ATOM   5784 C C      B TYR A 1 373 ? -1.08700  17.23700  37.49200 0.570 105.84346 ?  373 TYR A C      1 
ATOM   5785 O O      A TYR A 1 373 ? -1.84000  16.33000  39.00000 0.430 103.68542 ?  373 TYR A O      1 
ATOM   5786 O O      B TYR A 1 373 ? -0.11500  16.83400  36.84800 0.570 108.07675 ?  373 TYR A O      1 
ATOM   5787 C CB     A TYR A 1 373 ? -1.84200  19.04600  39.53400 0.430 104.51046 ?  373 TYR A CB     1 
ATOM   5788 C CB     B TYR A 1 373 ? -1.92600  18.59300  39.43500 0.570 104.72545 ?  373 TYR A CB     1 
ATOM   5789 C CG     A TYR A 1 373 ? -1.35500  20.41100  39.96400 0.430 105.73369 ?  373 TYR A CG     1 
ATOM   5790 C CG     B TYR A 1 373 ? -1.71600  17.37200  40.30900 0.570 106.06387 ?  373 TYR A CG     1 
ATOM   5791 C CD1    A TYR A 1 373 ? -1.90100  21.56600  39.42300 0.430 107.96452 ?  373 TYR A CD1    1 
ATOM   5792 C CD1    B TYR A 1 373 ? -0.46000  17.06400  40.81600 0.570 101.27723 ?  373 TYR A CD1    1 
ATOM   5793 C CD2    A TYR A 1 373 ? -0.35200  20.54300  40.91400 0.430 111.48987 ?  373 TYR A CD2    1 
ATOM   5794 C CD2    B TYR A 1 373 ? -2.76800  16.51200  40.59800 0.570 105.53515 ?  373 TYR A CD2    1 
ATOM   5795 C CE1    A TYR A 1 373 ? -1.46000  22.81500  39.81300 0.430 106.14778 ?  373 TYR A CE1    1 
ATOM   5796 C CE1    B TYR A 1 373 ? -0.26100  15.94500  41.60000 0.570 97.68661  ?  373 TYR A CE1    1 
ATOM   5797 C CE2    A TYR A 1 373 ? 0.09400   21.78800  41.31300 0.430 111.98116 ?  373 TYR A CE2    1 
ATOM   5798 C CE2    B TYR A 1 373 ? -2.57700  15.39000  41.38000 0.570 102.45238 ?  373 TYR A CE2    1 
ATOM   5799 C CZ     A TYR A 1 373 ? -0.46200  22.92000  40.75900 0.430 112.33628 ?  373 TYR A CZ     1 
ATOM   5800 C CZ     B TYR A 1 373 ? -1.32100  15.11100  41.87700 0.570 99.21217  ?  373 TYR A CZ     1 
ATOM   5801 O OH     A TYR A 1 373 ? -0.01900  24.16200  41.15000 0.430 111.48476 ?  373 TYR A OH     1 
ATOM   5802 O OH     B TYR A 1 373 ? -1.12500  13.99600  42.65700 0.570 99.28071  ?  373 TYR A OH     1 
ATOM   5803 H H      A TYR A 1 373 ? -0.71900  19.66900  36.75000 0.430 125.44120 ?  373 TYR A H      1 
ATOM   5804 H H      B TYR A 1 373 ? -0.79700  20.26500  37.18300 0.570 125.74862 ?  373 TYR A H      1 
ATOM   5805 H HA     A TYR A 1 373 ? -0.21200  18.49500  38.39400 0.430 127.04657 ?  373 TYR A HA     1 
ATOM   5806 H HA     B TYR A 1 373 ? -0.12300  18.75000  38.49100 0.570 127.10668 ?  373 TYR A HA     1 
ATOM   5807 H HB2    A TYR A 1 373 ? -2.79700  19.11100  39.37800 0.430 125.53032 ?  373 TYR A HB2    1 
ATOM   5808 H HB2    B TYR A 1 373 ? -1.72800  19.38000  39.96700 0.570 125.78831 ?  373 TYR A HB2    1 
ATOM   5809 H HB3    A TYR A 1 373 ? -1.66500  18.42900  40.26100 0.430 125.53032 ?  373 TYR A HB3    1 
ATOM   5810 H HB3    B TYR A 1 373 ? -2.85500  18.60500  39.15600 0.570 125.78831 ?  373 TYR A HB3    1 
ATOM   5811 H HD1    A TYR A 1 373 ? -2.57600  21.49800  38.78600 0.430 129.67520 ?  373 TYR A HD1    1 
ATOM   5812 H HD1    B TYR A 1 373 ? 0.25900   17.62200  40.62400 0.570 121.65045 ?  373 TYR A HD1    1 
ATOM   5813 H HD2    A TYR A 1 373 ? 0.02600   19.78100  41.28900 0.430 133.90562 ?  373 TYR A HD2    1 
ATOM   5814 H HD2    B TYR A 1 373 ? -3.61400  16.69500  40.26000 0.570 126.75995 ?  373 TYR A HD2    1 
ATOM   5815 H HE1    A TYR A 1 373 ? -1.83400  23.58100  39.44100 0.430 127.49510 ?  373 TYR A HE1    1 
ATOM   5816 H HE1    B TYR A 1 373 ? 0.58400   15.75500  41.93900 0.570 117.34170 ?  373 TYR A HE1    1 
ATOM   5817 H HE2    A TYR A 1 373 ? 0.76600   21.86200  41.95200 0.430 134.49516 ?  373 TYR A HE2    1 
ATOM   5818 H HE2    B TYR A 1 373 ? -3.29100  14.82500  41.56900 0.570 123.06063 ?  373 TYR A HE2    1 
ATOM   5819 H HH     A TYR A 1 373 ? -0.37200  24.75700  40.67300 0.430 133.89948 ?  373 TYR A HH     1 
ATOM   5820 H HH     B TYR A 1 373 ? -1.79600  13.49300  42.61400 0.570 119.25462 ?  373 TYR A HH     1 
ATOM   5821 N N      A VAL A 1 374 ? -1.72500  16.63000  36.78200 0.430 103.64165 ?  374 VAL A N      1 
ATOM   5822 N N      B VAL A 1 374 ? -2.21100  16.52600  37.62200 0.570 104.36380 ?  374 VAL A N      1 
ATOM   5823 C CA     A VAL A 1 374 ? -2.07200  15.24300  36.49300 0.430 98.64498  ?  374 VAL A CA     1 
ATOM   5824 C CA     B VAL A 1 374 ? -2.35600  15.15000  37.14800 0.570 100.11061 ?  374 VAL A CA     1 
ATOM   5825 C C      A VAL A 1 374 ? -0.83000  14.37400  36.64500 0.430 97.06524  ?  374 VAL A C      1 
ATOM   5826 C C      B VAL A 1 374 ? -1.12700  14.32900  37.52800 0.570 99.82091  ?  374 VAL A C      1 
ATOM   5827 O O      A VAL A 1 374 ? 0.30300   14.82800  36.44600 0.430 92.96932  ?  374 VAL A O      1 
ATOM   5828 O O      B VAL A 1 374 ? -0.28100  14.77700  38.31000 0.570 102.58173 ?  374 VAL A O      1 
ATOM   5829 C CB     A VAL A 1 374 ? -2.68400  15.11600  35.08400 0.430 95.23998  ?  374 VAL A CB     1 
ATOM   5830 C CB     B VAL A 1 374 ? -2.63300  15.10800  35.62900 0.570 95.26719  ?  374 VAL A CB     1 
ATOM   5831 C CG1    A VAL A 1 374 ? -2.90300  13.65500  34.72800 0.430 96.36520  ?  374 VAL A CG1    1 
ATOM   5832 C CG1    B VAL A 1 374 ? -3.34500  16.38200  35.18200 0.570 94.94811  ?  374 VAL A CG1    1 
ATOM   5833 C CG2    A VAL A 1 374 ? -3.99300  15.88700  35.00400 0.430 94.42739  ?  374 VAL A CG2    1 
ATOM   5834 C CG2    B VAL A 1 374 ? -1.36200  14.90000  34.80700 0.570 102.83371 ?  374 VAL A CG2    1 
ATOM   5835 H H      A VAL A 1 374 ? -1.60700  17.11900  36.08400 0.430 124.48775 ?  374 VAL A H      1 
ATOM   5836 H H      B VAL A 1 374 ? -2.92500  16.82900  37.99400 0.570 125.35432 ?  374 VAL A H      1 
ATOM   5837 H HA     A VAL A 1 374 ? -2.73700  14.94300  37.13200 0.430 118.49175 ?  374 VAL A HA     1 
ATOM   5838 H HA     B VAL A 1 374 ? -3.11500  14.74700  37.59800 0.570 120.25050 ?  374 VAL A HA     1 
ATOM   5839 H HB     A VAL A 1 374 ? -2.06800  15.49500  34.43900 0.430 114.40575 ?  374 VAL A HB     1 
ATOM   5840 H HB     B VAL A 1 374 ? -3.20700  14.34400  35.46100 0.570 114.43840 ?  374 VAL A HB     1 
ATOM   5841 H HG11   A VAL A 1 374 ? -3.54800  13.59900  34.00500 0.430 115.75601 ?  374 VAL A HG11   1 
ATOM   5842 H HG11   B VAL A 1 374 ? -3.69100  16.25200  34.28500 0.570 114.05550 ?  374 VAL A HG11   1 
ATOM   5843 H HG12   A VAL A 1 374 ? -2.05900  13.26800  34.44800 0.430 115.75601 ?  374 VAL A HG12   1 
ATOM   5844 H HG12   B VAL A 1 374 ? -4.07300  16.56800  35.79400 0.570 114.05550 ?  374 VAL A HG12   1 
ATOM   5845 H HG13   A VAL A 1 374 ? -3.24000  13.18600  35.50700 0.430 115.75601 ?  374 VAL A HG13   1 
ATOM   5846 H HG13   B VAL A 1 374 ? -2.71100  17.11600  35.18800 0.570 114.05550 ?  374 VAL A HG13   1 
ATOM   5847 H HG21   A VAL A 1 374 ? -4.33900  15.83000  34.10000 0.430 113.43064 ?  374 VAL A HG21   1 
ATOM   5848 H HG21   B VAL A 1 374 ? -1.50900  15.23600  33.90900 0.570 123.51822 ?  374 VAL A HG21   1 
ATOM   5849 H HG22   A VAL A 1 374 ? -4.62800  15.49700  35.62600 0.430 113.43064 ?  374 VAL A HG22   1 
ATOM   5850 H HG22   B VAL A 1 374 ? -0.63300  15.38300  35.22600 0.570 123.51822 ?  374 VAL A HG22   1 
ATOM   5851 H HG23   A VAL A 1 374 ? -3.82900  16.81400  35.23800 0.430 113.43064 ?  374 VAL A HG23   1 
ATOM   5852 H HG23   B VAL A 1 374 ? -1.15700  13.95300  34.77600 0.570 123.51822 ?  374 VAL A HG23   1 
ATOM   5853 N N      . SER A 1 375 ? -1.04000  13.10900  37.00800 1.000 93.92275  ?  375 SER A N      1 
ATOM   5854 C CA     . SER A 1 375 ? 0.08000   12.21200  37.25600 1.000 87.54420  ?  375 SER A CA     1 
ATOM   5855 C C      . SER A 1 375 ? 0.94000   12.08000  36.00500 1.000 81.44949  ?  375 SER A C      1 
ATOM   5856 O O      . SER A 1 375 ? 0.42200   11.96300  34.88900 1.000 80.24650  ?  375 SER A O      1 
ATOM   5857 C CB     . SER A 1 375 ? -0.42100  10.83200  37.68800 1.000 84.78072  ?  375 SER A CB     1 
ATOM   5858 O OG     . SER A 1 375 ? -1.81800  10.70100  37.46900 1.000 105.25096 ?  375 SER A OG     1 
ATOM   5859 H H      A SER A 1 375 ? -1.81400  12.75100  37.11500 0.430 112.82506 ?  375 SER A H      1 
ATOM   5860 H H      B SER A 1 375 ? -1.63700  12.76900  36.49100 0.570 112.82506 ?  375 SER A H      1 
ATOM   5861 H HA     . SER A 1 375 ? 0.63100   12.57300  37.96800 1.000 105.17080 ?  375 SER A HA     1 
ATOM   5862 H HB2    . SER A 1 375 ? 0.04300   10.15400  37.17400 1.000 101.85463 ?  375 SER A HB2    1 
ATOM   5863 H HB3    . SER A 1 375 ? -0.23900  10.71400  38.63400 1.000 101.85463 ?  375 SER A HB3    1 
ATOM   5864 H HG     . SER A 1 375 ? -2.24100  11.16500  38.02600 1.000 126.41892 ?  375 SER A HG     1 
ATOM   5865 N N      . TRP A 1 376 ? 2.26500   12.10300  36.19600 1.000 77.51279  ?  376 TRP A N      1 
ATOM   5866 C CA     . TRP A 1 376 ? 3.16900   12.04500  35.05400 1.000 72.63580  ?  376 TRP A CA     1 
ATOM   5867 C C      . TRP A 1 376 ? 3.01200   10.74100  34.27500 1.000 67.95873  ?  376 TRP A C      1 
ATOM   5868 O O      . TRP A 1 376 ? 3.25200   10.71200  33.06000 1.000 56.60090  ?  376 TRP A O      1 
ATOM   5869 C CB     . TRP A 1 376 ? 4.62100   12.22000  35.51200 1.000 68.79701  ?  376 TRP A CB     1 
ATOM   5870 C CG     . TRP A 1 376 ? 5.20200   11.03500  36.23200 1.000 69.27632  ?  376 TRP A CG     1 
ATOM   5871 C CD1    . TRP A 1 376 ? 5.27800   10.85500  37.58500 1.000 68.98664  ?  376 TRP A CD1    1 
ATOM   5872 C CD2    . TRP A 1 376 ? 5.79900   9.87000   35.64200 1.000 68.33996  ?  376 TRP A CD2    1 
ATOM   5873 N NE1    . TRP A 1 376 ? 5.87600   9.65600   37.86800 1.000 66.09429  ?  376 TRP A NE1    1 
ATOM   5874 C CE2    . TRP A 1 376 ? 6.20500   9.03100   36.69500 1.000 70.26078  ?  376 TRP A CE2    1 
ATOM   5875 C CE3    . TRP A 1 376 ? 6.02500   9.45800   34.32500 1.000 69.88285  ?  376 TRP A CE3    1 
ATOM   5876 C CZ2    . TRP A 1 376 ? 6.82600   7.80000   36.47300 1.000 80.43951  ?  376 TRP A CZ2    1 
ATOM   5877 C CZ3    . TRP A 1 376 ? 6.63900   8.23500   34.10800 1.000 61.14419  ?  376 TRP A CZ3    1 
ATOM   5878 C CH2    . TRP A 1 376 ? 7.03500   7.42300   35.17600 1.000 68.23405  ?  376 TRP A CH2    1 
ATOM   5879 H H      . TRP A 1 376 ? 2.65300   12.15100  36.96300 1.000 93.13311  ?  376 TRP A H      1 
ATOM   5880 H HA     . TRP A 1 376 ? 2.95700   12.78000  34.45700 1.000 87.28073  ?  376 TRP A HA     1 
ATOM   5881 H HB2    . TRP A 1 376 ? 5.17200   12.38400  34.73100 1.000 82.67418  ?  376 TRP A HB2    1 
ATOM   5882 H HB3    . TRP A 1 376 ? 4.66500   12.97800  36.11500 1.000 82.67418  ?  376 TRP A HB3    1 
ATOM   5883 H HD1    . TRP A 1 376 ? 4.96700   11.45900  38.22000 1.000 82.90174  ?  376 TRP A HD1    1 
ATOM   5884 H HE1    . TRP A 1 376 ? 6.02200   9.34600   38.65700 1.000 79.43092  ?  376 TRP A HE1    1 
ATOM   5885 H HE3    . TRP A 1 376 ? 5.76800   9.99300   33.60900 1.000 83.97719  ?  376 TRP A HE3    1 
ATOM   5886 H HZ2    . TRP A 1 376 ? 7.08900   7.25700   37.18100 1.000 96.64518  ?  376 TRP A HZ2    1 
ATOM   5887 H HZ3    . TRP A 1 376 ? 6.79000   7.94900   33.23600 1.000 73.49080  ?  376 TRP A HZ3    1 
ATOM   5888 H HH2    . TRP A 1 376 ? 7.44800   6.60900   35.00000 1.000 81.99863  ?  376 TRP A HH2    1 
ATOM   5889 N N      . GLU A 1 377 ? 2.60500   9.66100   34.94800 1.000 63.78859  ?  377 GLU A N      1 
ATOM   5890 C CA     . GLU A 1 377 ? 2.42200   8.39400   34.25500 1.000 71.24719  ?  377 GLU A CA     1 
ATOM   5891 C C      . GLU A 1 377 ? 1.36000   8.51200   33.16700 1.000 63.03014  ?  377 GLU A C      1 
ATOM   5892 O O      . GLU A 1 377 ? 1.49300   7.92100   32.09500 1.000 57.06241  ?  377 GLU A O      1 
ATOM   5893 C CB     . GLU A 1 377 ? 2.04700   7.29600   35.25200 1.000 72.47841  ?  377 GLU A CB     1 
ATOM   5894 C CG     . GLU A 1 377 ? 3.01400   7.16500   36.41600 1.000 82.45669  ?  377 GLU A CG     1 
ATOM   5895 C CD     . GLU A 1 377 ? 2.34400   7.40600   37.75400 1.000 95.74044  ?  377 GLU A CD     1 
ATOM   5896 O OE1    . GLU A 1 377 ? 2.05800   8.58500   38.07500 1.000 92.69702  ?  377 GLU A OE1    1 
ATOM   5897 O OE2    . GLU A 1 377 ? 2.09900   6.42000   38.48900 1.000 101.98754 -1 377 GLU A OE2    1 
ATOM   5898 H H      . GLU A 1 377 ? 2.43300   9.64000   35.79000 1.000 76.66407  ?  377 GLU A H      1 
ATOM   5899 H HA     . GLU A 1 377 ? 3.26000   8.14400   33.83500 1.000 85.61439  ?  377 GLU A HA     1 
ATOM   5900 H HB2    . GLU A 1 377 ? 1.17000   7.49300   35.61700 1.000 87.09186  ?  377 GLU A HB2    1 
ATOM   5901 H HB3    . GLU A 1 377 ? 2.02800   6.44500   34.78600 1.000 87.09186  ?  377 GLU A HB3    1 
ATOM   5902 H HG2    . GLU A 1 377 ? 3.38400   6.26800   36.42100 1.000 99.06579  ?  377 GLU A HG2    1 
ATOM   5903 H HG3    . GLU A 1 377 ? 3.72400   7.81700   36.31200 1.000 99.06579  ?  377 GLU A HG3    1 
ATOM   5904 N N      . ARG A 1 378 ? 0.29700   9.27100   33.42800 1.000 64.60527  ?  378 ARG A N      1 
ATOM   5905 C CA     . ARG A 1 378 ? -0.74400  9.44700   32.42000 1.000 60.72666  ?  378 ARG A CA     1 
ATOM   5906 C C      . ARG A 1 378 ? -0.21200  10.19500  31.20100 1.000 60.07064  ?  378 ARG A C      1 
ATOM   5907 O O      . ARG A 1 378 ? -0.55600  9.86400   30.06600 1.000 53.91223  ?  378 ARG A O      1 
ATOM   5908 C CB     . ARG A 1 378 ? -1.94700  10.17700  33.01600 1.000 65.30761  ?  378 ARG A CB     1 
ATOM   5909 C CG     . ARG A 1 378 ? -2.67400  9.46700   34.17900 1.000 72.83500  ?  378 ARG A CG     1 
ATOM   5910 C CD     . ARG A 1 378 ? -2.64400  7.93400   34.12200 1.000 74.79312  ?  378 ARG A CD     1 
ATOM   5911 N NE     . ARG A 1 378 ? -1.80000  7.36600   35.17100 0.180 75.72216  ?  378 ARG A NE     1 
ATOM   5912 C CZ     . ARG A 1 378 ? -1.86900  6.11300   35.60100 0.450 76.47442  ?  378 ARG A CZ     1 
ATOM   5913 N NH1    . ARG A 1 378 ? -2.72600  5.25000   35.08100 0.420 79.69677  ?  378 ARG A NH1    1 
ATOM   5914 N NH2    . ARG A 1 378 ? -1.06000  5.71600   36.58000 0.840 90.52636  ?  378 ARG A NH2    1 
ATOM   5915 H H      . ARG A 1 378 ? 0.15700   9.68800   34.16700 1.000 77.64409  ?  378 ARG A H      1 
ATOM   5916 H HA     . ARG A 1 378 ? -1.04400  8.57100   32.13000 1.000 72.98977  ?  378 ARG A HA     1 
ATOM   5917 H HB2    . ARG A 1 378 ? -1.64200  11.03500  33.35100 1.000 78.48690  ?  378 ARG A HB2    1 
ATOM   5918 H HB3    . ARG A 1 378 ? -2.59900  10.30900  32.31100 1.000 78.48690  ?  378 ARG A HB3    1 
ATOM   5919 H HG2    . ARG A 1 378 ? -2.25600  9.73500   35.01300 1.000 87.51977  ?  378 ARG A HG2    1 
ATOM   5920 H HG3    . ARG A 1 378 ? -3.60500  9.74000   34.17300 1.000 87.51977  ?  378 ARG A HG3    1 
ATOM   5921 H HD2    . ARG A 1 378 ? -3.54400  7.59200   34.23900 1.000 89.86951  ?  378 ARG A HD2    1 
ATOM   5922 H HD3    . ARG A 1 378 ? -2.29100  7.65300   33.26400 1.000 89.86951  ?  378 ARG A HD3    1 
ATOM   5923 H HE     . ARG A 1 378 ? -1.21600  7.88200   35.53700 1.000 90.98437  ?  378 ARG A HE     1 
ATOM   5924 H HH11   . ARG A 1 378 ? -3.25500  5.49700   34.44900 1.000 95.75390  ?  378 ARG A HH11   1 
ATOM   5925 H HH12   . ARG A 1 378 ? -2.75400  4.44200   35.37500 1.000 95.75390  ?  378 ARG A HH12   1 
ATOM   5926 H HH21   . ARG A 1 378 ? -0.50000  6.27000   36.92700 1.000 108.74940 ?  378 ARG A HH21   1 
ATOM   5927 H HH22   . ARG A 1 378 ? -1.09700  4.90600   36.86700 1.000 108.74940 ?  378 ARG A HH22   1 
ATOM   5928 N N      . GLY A 1 379 ? 0.62400   11.21500  31.42000 1.000 55.56161  ?  379 GLY A N      1 
ATOM   5929 C CA     . GLY A 1 379 ? 1.23900   11.89700  30.29800 1.000 53.94756  ?  379 GLY A CA     1 
ATOM   5930 C C      . GLY A 1 379 ? 2.15200   10.99200  29.50000 1.000 52.15361  ?  379 GLY A C      1 
ATOM   5931 O O      . GLY A 1 379 ? 2.19600   11.06300  28.26900 1.000 48.40166  ?  379 GLY A O      1 
ATOM   5932 H H      . GLY A 1 379 ? 0.84400   11.51900  32.19400 1.000 66.79170  ?  379 GLY A H      1 
ATOM   5933 H HA2    . GLY A 1 379 ? 0.54500   12.22900  29.70600 1.000 64.85485  ?  379 GLY A HA2    1 
ATOM   5934 H HA3    . GLY A 1 379 ? 1.76100   12.64600  30.62400 1.000 64.85485  ?  379 GLY A HA3    1 
ATOM   5935 N N      . MET A 1 380 ? 2.89900   10.12700  30.19400 1.000 54.11795  ?  380 MET A N      1 
ATOM   5936 C CA     . MET A 1 380 ? 3.76700   9.17500   29.50200 1.000 51.98742  ?  380 MET A CA     1 
ATOM   5937 C C      . MET A 1 380 ? 2.95400   8.24000   28.61300 1.000 52.16116  ?  380 MET A C      1 
ATOM   5938 O O      . MET A 1 380 ? 3.37300   7.92500   27.49400 1.000 51.09993  ?  380 MET A O      1 
ATOM   5939 C CB     . MET A 1 380 ? 4.57700   8.36500   30.51600 1.000 57.77321  ?  380 MET A CB     1 
ATOM   5940 C CG     . MET A 1 380 ? 5.26800   7.14000   29.91100 1.000 68.28490  ?  380 MET A CG     1 
ATOM   5941 S SD     . MET A 1 380 ? 6.31300   6.26400   31.09400 1.000 73.77889  ?  380 MET A SD     1 
ATOM   5942 C CE     . MET A 1 380 ? 5.08800   5.28900   31.95200 1.000 79.97970  ?  380 MET A CE     1 
ATOM   5943 H H      . MET A 1 380 ? 2.92100   10.07300  31.05200 1.000 65.05931  ?  380 MET A H      1 
ATOM   5944 H HA     . MET A 1 380 ? 4.39100   9.67500   28.95200 1.000 62.50268  ?  380 MET A HA     1 
ATOM   5945 H HB2    . MET A 1 380 ? 5.26400   8.93600   30.89500 1.000 69.44562  ?  380 MET A HB2    1 
ATOM   5946 H HB3    . MET A 1 380 ? 3.98100   8.05400   31.21500 1.000 69.44562  ?  380 MET A HB3    1 
ATOM   5947 H HG2    . MET A 1 380 ? 4.59200   6.52100   29.59400 1.000 82.05965  ?  380 MET A HG2    1 
ATOM   5948 H HG3    . MET A 1 380 ? 5.82800   7.42700   29.17300 1.000 82.05965  ?  380 MET A HG3    1 
ATOM   5949 H HE1    . MET A 1 380 ? 5.53000   4.74800   32.62500 1.000 96.09340  ?  380 MET A HE1    1 
ATOM   5950 H HE2    . MET A 1 380 ? 4.44900   5.88400   32.37300 1.000 96.09340  ?  380 MET A HE2    1 
ATOM   5951 H HE3    . MET A 1 380 ? 4.63600   4.71700   31.31200 1.000 96.09340  ?  380 MET A HE3    1 
ATOM   5952 N N      . GLU A 1 381 ? 1.79300   7.79200   29.09500 1.000 48.59306  ?  381 GLU A N      1 
ATOM   5953 C CA     . GLU A 1 381 ? 0.96600   6.88400   28.29800 1.000 53.37124  ?  381 GLU A CA     1 
ATOM   5954 C C      . GLU A 1 381 ? 0.57600   7.52000   26.96700 1.000 49.33350  ?  381 GLU A C      1 
ATOM   5955 O O      . GLU A 1 381 ? 0.57300   6.84400   25.93200 1.000 45.94022  ?  381 GLU A O      1 
ATOM   5956 C CB     . GLU A 1 381 ? -0.27900  6.48600   29.08100 1.000 54.03382  ?  381 GLU A CB     1 
ATOM   5957 C CG     . GLU A 1 381 ? -0.00100  5.54300   30.24100 1.000 71.85825  ?  381 GLU A CG     1 
ATOM   5958 C CD     . GLU A 1 381 ? -1.20700  5.37600   31.14900 1.000 85.90122  ?  381 GLU A CD     1 
ATOM   5959 O OE1    . GLU A 1 381 ? -2.29000  5.90000   30.79200 1.000 74.83015  ?  381 GLU A OE1    1 
ATOM   5960 O OE2    . GLU A 1 381 ? -1.07200  4.72900   32.21700 1.000 84.48713  -1 381 GLU A OE2    1 
ATOM   5961 H H      . GLU A 1 381 ? 1.46600   7.99500   29.86400 1.000 58.42944  ?  381 GLU A H      1 
ATOM   5962 H HA     . GLU A 1 381 ? 1.47600   6.08000   28.11300 1.000 64.16326  ?  381 GLU A HA     1 
ATOM   5963 H HB2    . GLU A 1 381 ? -0.68900  7.28700   29.44300 1.000 64.95835  ?  381 GLU A HB2    1 
ATOM   5964 H HB3    . GLU A 1 381 ? -0.89600  6.04000   28.47900 1.000 64.95835  ?  381 GLU A HB3    1 
ATOM   5965 H HG2    . GLU A 1 381 ? 0.23700   4.67100   29.89100 1.000 86.34767  ?  381 GLU A HG2    1 
ATOM   5966 H HG3    . GLU A 1 381 ? 0.72900   5.89900   30.77200 1.000 86.34767  ?  381 GLU A HG3    1 
ATOM   5967 N N      . VAL A 1 382 ? 0.23600   8.80700   26.98300 1.000 45.18607  ?  382 VAL A N      1 
ATOM   5968 C CA     . VAL A 1 382 ? -0.10900  9.50700   25.74800 1.000 47.91451  ?  382 VAL A CA     1 
ATOM   5969 C C      . VAL A 1 382 ? 1.09300   9.56600   24.81000 1.000 48.12038  ?  382 VAL A C      1 
ATOM   5970 O O      . VAL A 1 382 ? 0.96600   9.33400   23.59800 1.000 44.76383  ?  382 VAL A O      1 
ATOM   5971 C CB     . VAL A 1 382 ? -0.63400  10.92500  26.07500 1.000 46.25219  ?  382 VAL A CB     1 
ATOM   5972 C CG1    . VAL A 1 382 ? -0.75000  11.75900  24.80800 1.000 45.36261  ?  382 VAL A CG1    1 
ATOM   5973 C CG2    . VAL A 1 382 ? -1.96700  10.83200  26.80600 1.000 45.98035  ?  382 VAL A CG2    1 
ATOM   5974 H H      . VAL A 1 382 ? 0.19700   9.29600   27.69000 1.000 54.34106  ?  382 VAL A H      1 
ATOM   5975 H HA     . VAL A 1 382 ? -0.81400  9.01300   25.30100 1.000 57.61519  ?  382 VAL A HA     1 
ATOM   5976 H HB     . VAL A 1 382 ? -0.00300  11.37500  26.65800 1.000 55.62039  ?  382 VAL A HB     1 
ATOM   5977 H HG11   . VAL A 1 382 ? -1.30600  12.53300  24.98900 1.000 54.55290  ?  382 VAL A HG11   1 
ATOM   5978 H HG12   . VAL A 1 382 ? 0.13700   12.04500  24.53600 1.000 54.55290  ?  382 VAL A HG12   1 
ATOM   5979 H HG13   . VAL A 1 382 ? -1.15200  11.21800  24.11000 1.000 54.55290  ?  382 VAL A HG13   1 
ATOM   5980 H HG21   . VAL A 1 382 ? -2.27900  11.72800  27.00800 1.000 55.29419  ?  382 VAL A HG21   1 
ATOM   5981 H HG22   . VAL A 1 382 ? -2.60900  10.37900  26.23700 1.000 55.29419  ?  382 VAL A HG22   1 
ATOM   5982 H HG23   . VAL A 1 382 ? -1.84200  10.33200  27.62800 1.000 55.29419  ?  382 VAL A HG23   1 
ATOM   5983 N N      . PHE A 1 383 ? 2.27500   9.89300   25.34800 1.000 44.80736  ?  383 PHE A N      1 
ATOM   5984 C CA     . PHE A 1 383 ? 3.48700   9.87800   24.53400 1.000 44.41982  ?  383 PHE A CA     1 
ATOM   5985 C C      . PHE A 1 383 ? 3.75800   8.48400   23.97600 1.000 46.04454  ?  383 PHE A C      1 
ATOM   5986 O O      . PHE A 1 383 ? 4.12300   8.33000   22.80400 1.000 42.49204  ?  383 PHE A O      1 
ATOM   5987 C CB     . PHE A 1 383 ? 4.68000   10.35700  25.35700 1.000 42.75099  ?  383 PHE A CB     1 
ATOM   5988 C CG     . PHE A 1 383 ? 4.84400   11.85900  25.40100 1.000 44.08628  ?  383 PHE A CG     1 
ATOM   5989 C CD1    . PHE A 1 383 ? 3.74800   12.70900  25.25800 1.000 43.59475  ?  383 PHE A CD1    1 
ATOM   5990 C CD2    . PHE A 1 383 ? 6.09500   12.42000  25.58900 1.000 45.40131  ?  383 PHE A CD2    1 
ATOM   5991 C CE1    . PHE A 1 383 ? 3.90100   14.08300  25.30700 1.000 44.80137  ?  383 PHE A CE1    1 
ATOM   5992 C CE2    . PHE A 1 383 ? 6.25800   13.80600  25.63900 1.000 44.20990  ?  383 PHE A CE2    1 
ATOM   5993 C CZ     . PHE A 1 383 ? 5.16600   14.63600  25.49400 1.000 46.29582  ?  383 PHE A CZ     1 
ATOM   5994 H H      . PHE A 1 383 ? 2.39600   10.12400  26.16800 1.000 53.88661  ?  383 PHE A H      1 
ATOM   5995 H HA     . PHE A 1 383 ? 3.36800   10.48800  23.78900 1.000 53.42155  ?  383 PHE A HA     1 
ATOM   5996 H HB2    . PHE A 1 383 ? 4.57000   10.04700  26.26900 1.000 51.41896  ?  383 PHE A HB2    1 
ATOM   5997 H HB3    . PHE A 1 383 ? 5.48900   9.98400   24.97400 1.000 51.41896  ?  383 PHE A HB3    1 
ATOM   5998 H HD1    . PHE A 1 383 ? 2.90200   12.34600  25.12800 1.000 52.43147  ?  383 PHE A HD1    1 
ATOM   5999 H HD2    . PHE A 1 383 ? 6.83600   11.86700  25.68300 1.000 54.59934  ?  383 PHE A HD2    1 
ATOM   6000 H HE1    . PHE A 1 383 ? 3.16000   14.63700  25.21500 1.000 53.87942  ?  383 PHE A HE1    1 
ATOM   6001 H HE2    . PHE A 1 383 ? 7.10400   14.17000  25.77000 1.000 53.16964  ?  383 PHE A HE2    1 
ATOM   6002 H HZ     . PHE A 1 383 ? 5.27400   15.55900  25.52200 1.000 55.67275  ?  383 PHE A HZ     1 
ATOM   6003 N N      . GLU A 1 384 ? 3.57700   7.44800   24.80700 1.000 43.57238  ?  384 GLU A N      1 
ATOM   6004 C CA     . GLU A 1 384 ? 3.86600   6.09300   24.37900 1.000 51.96035  ?  384 GLU A CA     1 
ATOM   6005 C C      . GLU A 1 384 ? 3.03500   5.69400   23.16600 1.000 53.07319  ?  384 GLU A C      1 
ATOM   6006 O O      . GLU A 1 384 ? 3.49800   4.92400   22.31800 1.000 53.34848  ?  384 GLU A O      1 
ATOM   6007 C CB     . GLU A 1 384 ? 3.61200   5.12300   25.54000 1.000 56.48485  ?  384 GLU A CB     1 
ATOM   6008 C CG     . GLU A 1 384 ? 3.76700   3.67100   25.17600 1.000 73.90378  ?  384 GLU A CG     1 
ATOM   6009 C CD     . GLU A 1 384 ? 3.88400   2.77700   26.40100 1.000 89.23951  ?  384 GLU A CD     1 
ATOM   6010 O OE1    . GLU A 1 384 ? 4.08600   3.32300   27.51200 1.000 77.19983  ?  384 GLU A OE1    1 
ATOM   6011 O OE2    . GLU A 1 384 ? 3.76000   1.53700   26.25200 1.000 92.43239  -1 384 GLU A OE2    1 
ATOM   6012 H H      . GLU A 1 384 ? 3.29000   7.51200   25.61600 1.000 52.40462  ?  384 GLU A H      1 
ATOM   6013 H HA     . GLU A 1 384 ? 4.80100   6.03400   24.12800 1.000 62.47019  ?  384 GLU A HA     1 
ATOM   6014 H HB2    . GLU A 1 384 ? 4.24400   5.31700   26.25000 1.000 67.89959  ?  384 GLU A HB2    1 
ATOM   6015 H HB3    . GLU A 1 384 ? 2.70500   5.25200   25.85900 1.000 67.89959  ?  384 GLU A HB3    1 
ATOM   6016 H HG2    . GLU A 1 384 ? 2.99100   3.38600   24.66800 1.000 88.80231  ?  384 GLU A HG2    1 
ATOM   6017 H HG3    . GLU A 1 384 ? 4.57000   3.56000   24.64400 1.000 88.80231  ?  384 GLU A HG3    1 
ATOM   6018 N N      . GLU A 1 385 ? 1.81700   6.21900   23.05700 1.000 52.17633  ?  385 GLU A N      1 
ATOM   6019 C CA     . GLU A 1 385 ? 0.96400   5.88200   21.92500 1.000 56.00412  ?  385 GLU A CA     1 
ATOM   6020 C C      . GLU A 1 385 ? 1.46400   6.51600   20.63100 1.000 51.14432  ?  385 GLU A C      1 
ATOM   6021 O O      . GLU A 1 385 ? 1.49000   5.84900   19.58300 1.000 46.91398  ?  385 GLU A O      1 
ATOM   6022 C CB     . GLU A 1 385 ? -0.47000  6.33300   22.21500 1.000 60.51282  ?  385 GLU A CB     1 
ATOM   6023 C CG     . GLU A 1 385 ? -1.49400  5.80800   21.23200 1.000 69.16262  ?  385 GLU A CG     1 
ATOM   6024 C CD     . GLU A 1 385 ? -2.89000  6.34200   21.50300 1.000 69.31451  ?  385 GLU A CD     1 
ATOM   6025 O OE1    . GLU A 1 385 ? -3.14200  6.80200   22.63700 1.000 60.77238  ?  385 GLU A OE1    1 
ATOM   6026 O OE2    . GLU A 1 385 ? -3.72500  6.30800   20.57300 1.000 73.27145  -1 385 GLU A OE2    1 
ATOM   6027 H H      . GLU A 1 385 ? 1.46500   6.76800   23.61800 1.000 62.72936  ?  385 GLU A H      1 
ATOM   6028 H HA     . GLU A 1 385 ? 0.97300   4.91900   21.80400 1.000 67.32272  ?  385 GLU A HA     1 
ATOM   6029 H HB2    . GLU A 1 385 ? -0.72200  6.01900   23.09800 1.000 72.73316  ?  385 GLU A HB2    1 
ATOM   6030 H HB3    . GLU A 1 385 ? -0.50300  7.30200   22.18600 1.000 72.73316  ?  385 GLU A HB3    1 
ATOM   6031 H HG2    . GLU A 1 385 ? -1.23900  6.07600   20.33500 1.000 83.11292  ?  385 GLU A HG2    1 
ATOM   6032 H HG3    . GLU A 1 385 ? -1.52500  4.84100   21.29300 1.000 83.11292  ?  385 GLU A HG3    1 
ATOM   6033 N N      . HIS A 1 386 ? 1.87500   7.78300   20.68500 1.000 43.03587  ?  386 HIS A N      1 
ATOM   6034 C CA     . HIS A 1 386 ? 2.01200   8.60800   19.48800 1.000 46.16775  ?  386 HIS A CA     1 
ATOM   6035 C C      . HIS A 1 386 ? 3.44600   8.86400   19.04700 1.000 45.53436  ?  386 HIS A C      1 
ATOM   6036 O O      . HIS A 1 386 ? 3.66700   9.11200   17.86300 1.000 45.95988  ?  386 HIS A O      1 
ATOM   6037 C CB     . HIS A 1 386 ? 1.33000   9.97100   19.71000 1.000 41.95085  ?  386 HIS A CB     1 
ATOM   6038 C CG     . HIS A 1 386 ? -0.16100  9.88200   19.87100 1.000 49.17041  ?  386 HIS A CG     1 
ATOM   6039 N ND1    . HIS A 1 386 ? -0.99300  9.42900   18.86800 1.000 51.13249  ?  386 HIS A ND1    1 
ATOM   6040 C CD2    . HIS A 1 386 ? -0.96400  10.17900  20.92000 1.000 51.86437  ?  386 HIS A CD2    1 
ATOM   6041 C CE1    . HIS A 1 386 ? -2.24500  9.44900   19.29700 1.000 54.83006  ?  386 HIS A CE1    1 
ATOM   6042 N NE2    . HIS A 1 386 ? -2.25400  9.90100   20.53900 1.000 53.43524  ?  386 HIS A NE2    1 
ATOM   6043 H H      . HIS A 1 386 ? 2.08400   8.19100   21.41300 1.000 51.76082  ?  386 HIS A H      1 
ATOM   6044 H HA     . HIS A 1 386 ? 1.56700   8.14800   18.75900 1.000 55.51907  ?  386 HIS A HA     1 
ATOM   6045 H HB2    . HIS A 1 386 ? 1.69100   10.37300  20.51500 1.000 50.45879  ?  386 HIS A HB2    1 
ATOM   6046 H HB3    . HIS A 1 386 ? 1.51200   10.53900  18.94500 1.000 50.45879  ?  386 HIS A HB3    1 
ATOM   6047 H HD1    . HIS A 1 386 ? -0.73900  9.17500   18.08700 1.000 61.47676  ?  386 HIS A HD1    1 
ATOM   6048 H HD2    . HIS A 1 386 ? -0.69300  10.51000  21.74600 1.000 62.35501  ?  386 HIS A HD2    1 
ATOM   6049 H HE1    . HIS A 1 386 ? -2.99200  9.18900   18.80800 1.000 65.91384  ?  386 HIS A HE1    1 
ATOM   6050 N N      . LEU A 1 387 ? 4.41500   8.82300   19.95400 1.000 42.09814  ?  387 LEU A N      1 
ATOM   6051 C CA     . LEU A 1 387 ? 5.80000   9.10800   19.57700 1.000 43.10275  ?  387 LEU A CA     1 
ATOM   6052 C C      . LEU A 1 387 ? 6.33600   8.00300   18.67700 1.000 41.33677  ?  387 LEU A C      1 
ATOM   6053 O O      . LEU A 1 387 ? 6.20600   6.81300   18.99100 1.000 41.58688  ?  387 LEU A O      1 
ATOM   6054 C CB     . LEU A 1 387 ? 6.68800   9.23400   20.81700 1.000 41.15771  ?  387 LEU A CB     1 
ATOM   6055 C CG     . LEU A 1 387 ? 6.67600   10.54800  21.58400 1.000 41.22018  ?  387 LEU A CG     1 
ATOM   6056 C CD1    . LEU A 1 387 ? 7.46400   10.38800  22.87700 1.000 42.98382  ?  387 LEU A CD1    1 
ATOM   6057 C CD2    . LEU A 1 387 ? 7.23800   11.69800  20.75500 1.000 43.64695  ?  387 LEU A CD2    1 
ATOM   6058 H H      . LEU A 1 387 ? 4.30200   8.63400   20.78600 1.000 50.63554  ?  387 LEU A H      1 
ATOM   6059 H HA     . LEU A 1 387 ? 5.82600   9.95000   19.09700 1.000 51.84107  ?  387 LEU A HA     1 
ATOM   6060 H HB2    . LEU A 1 387 ? 6.41500   8.54500   21.44300 1.000 49.50703  ?  387 LEU A HB2    1 
ATOM   6061 H HB3    . LEU A 1 387 ? 7.60400   9.08400   20.53700 1.000 49.50703  ?  387 LEU A HB3    1 
ATOM   6062 H HG     . LEU A 1 387 ? 5.75800   10.77700  21.79400 1.000 49.58198  ?  387 LEU A HG     1 
ATOM   6063 H HD11   . LEU A 1 387 ? 7.41700   11.21700  23.38000 1.000 51.69836  ?  387 LEU A HD11   1 
ATOM   6064 H HD12   . LEU A 1 387 ? 7.07800   9.66500   23.39500 1.000 51.69836  ?  387 LEU A HD12   1 
ATOM   6065 H HD13   . LEU A 1 387 ? 8.38700   10.18400  22.66100 1.000 51.69836  ?  387 LEU A HD13   1 
ATOM   6066 H HD21   . LEU A 1 387 ? 7.24200   12.50400  21.29500 1.000 52.49411  ?  387 LEU A HD21   1 
ATOM   6067 H HD22   . LEU A 1 387 ? 8.14200   11.47800  20.48200 1.000 52.49411  ?  387 LEU A HD22   1 
ATOM   6068 H HD23   . LEU A 1 387 ? 6.67800   11.82600  19.97300 1.000 52.49411  ?  387 LEU A HD23   1 
ATOM   6069 N N      . ILE A 1 388 ? 6.95200   8.39700   17.55800 1.000 38.69372  ?  388 ILE A N      1 
ATOM   6070 C CA     . ILE A 1 388 ? 7.61000   7.41400   16.70000 1.000 44.23615  ?  388 ILE A CA     1 
ATOM   6071 C C      . ILE A 1 388 ? 8.98400   7.03000   17.22200 1.000 42.03049  ?  388 ILE A C      1 
ATOM   6072 O O      . ILE A 1 388 ? 9.56300   6.03400   16.75200 1.000 41.51667  ?  388 ILE A O      1 
ATOM   6073 C CB     . ILE A 1 388 ? 7.72200   7.91200   15.24300 1.000 43.56623  ?  388 ILE A CB     1 
ATOM   6074 C CG1    . ILE A 1 388 ? 8.50400   9.23500   15.16900 1.000 46.42881  ?  388 ILE A CG1    1 
ATOM   6075 C CG2    . ILE A 1 388 ? 6.34100   8.10800   14.65100 1.000 46.40581  ?  388 ILE A CG2    1 
ATOM   6076 C CD1    . ILE A 1 388 ? 8.71800   9.73300   13.73400 1.000 46.59789  ?  388 ILE A CD1    1 
ATOM   6077 H H      . ILE A 1 388 ? 7.00100   9.21000   17.28100 1.000 46.55024  ?  388 ILE A H      1 
ATOM   6078 H HA     . ILE A 1 388 ? 7.06200   6.61400   16.68300 1.000 53.20115  ?  388 ILE A HA     1 
ATOM   6079 H HB     . ILE A 1 388 ? 8.20300   7.23900   14.73600 1.000 52.39724  ?  388 ILE A HB     1 
ATOM   6080 H HG12   . ILE A 1 388 ? 8.01200   9.91800   15.65200 1.000 55.83234  ?  388 ILE A HG12   1 
ATOM   6081 H HG13   . ILE A 1 388 ? 9.37600   9.10700   15.57300 1.000 55.83234  ?  388 ILE A HG13   1 
ATOM   6082 H HG21   . ILE A 1 388 ? 6.42300   8.23500   13.69300 1.000 55.80475  ?  388 ILE A HG21   1 
ATOM   6083 H HG22   . ILE A 1 388 ? 5.80400   7.32100   14.83500 1.000 55.80475  ?  388 ILE A HG22   1 
ATOM   6084 H HG23   . ILE A 1 388 ? 5.93200   8.88900   15.05400 1.000 55.80475  ?  388 ILE A HG23   1 
ATOM   6085 H HD11   . ILE A 1 388 ? 9.32900   10.48700  13.74900 1.000 56.03524  ?  388 ILE A HD11   1 
ATOM   6086 H HD12   . ILE A 1 388 ? 9.09300   9.01400   13.20200 1.000 56.03524  ?  388 ILE A HD12   1 
ATOM   6087 H HD13   . ILE A 1 388 ? 7.86400   10.00700  13.36400 1.000 56.03524  ?  388 ILE A HD13   1 
ATOM   6088 N N      . ASP A 1 389 ? 9.53200   7.78300   18.17500 1.000 42.94420  ?  389 ASP A N      1 
ATOM   6089 C CA     . ASP A 1 389 ? 10.74900  7.39700   18.87400 1.000 38.37057  ?  389 ASP A CA     1 
ATOM   6090 C C      . ASP A 1 389 ? 10.46300  6.84300   20.26900 1.000 41.32337  ?  389 ASP A C      1 
ATOM   6091 O O      . ASP A 1 389 ? 11.35600  6.83000   21.11500 1.000 41.23136  ?  389 ASP A O      1 
ATOM   6092 C CB     . ASP A 1 389 ? 11.72200  8.57900   18.96200 1.000 36.79546  ?  389 ASP A CB     1 
ATOM   6093 C CG     . ASP A 1 389 ? 11.15300  9.77300   19.69900 1.000 38.81968  ?  389 ASP A CG     1 
ATOM   6094 O OD1    . ASP A 1 389 ? 10.20900  9.62000   20.49400 1.000 38.80907  ?  389 ASP A OD1    1 
ATOM   6095 O OD2    . ASP A 1 389 ? 11.69400  10.89200  19.49700 1.000 40.76345  -1 389 ASP A OD2    1 
ATOM   6096 H H      . ASP A 1 389 ? 9.20800   8.53600   18.43600 1.000 51.65081  ?  389 ASP A H      1 
ATOM   6097 H HA     . ASP A 1 389 ? 11.18400  6.70000   18.36000 1.000 46.16246  ?  389 ASP A HA     1 
ATOM   6098 H HB2    . ASP A 1 389 ? 12.52100  8.29300   19.43100 1.000 44.27232  ?  389 ASP A HB2    1 
ATOM   6099 H HB3    . ASP A 1 389 ? 11.94900  8.86500   18.06300 1.000 44.27232  ?  389 ASP A HB3    1 
ATOM   6100 N N      . GLN A 1 390 ? 9.23600   6.37600   20.51100 1.000 39.82412  ?  390 GLN A N      1 
ATOM   6101 C CA     . GLN A 1 390 ? 8.84700   5.85200   21.82000 1.000 43.81656  ?  390 GLN A CA     1 
ATOM   6102 C C      . GLN A 1 390 ? 9.84700   4.80400   22.28200 1.000 45.35595  ?  390 GLN A C      1 
ATOM   6103 O O      . GLN A 1 390 ? 10.09200  3.81300   21.58800 1.000 41.33733  ?  390 GLN A O      1 
ATOM   6104 C CB     . GLN A 1 390 ? 7.43400   5.27800   21.75600 1.000 47.57970  ?  390 GLN A CB     1 
ATOM   6105 C CG     . GLN A 1 390 ? 7.08900   4.20700   22.81300 1.000 55.51126  ?  390 GLN A CG     1 
ATOM   6106 C CD     . GLN A 1 390 ? 7.27300   4.69300   24.24900 1.000 54.64718  ?  390 GLN A CD     1 
ATOM   6107 O OE1    . GLN A 1 390 ? 7.33500   5.89300   24.50900 1.000 56.00818  ?  390 GLN A OE1    1 
ATOM   6108 N NE2    . GLN A 1 390 ? 7.34800   3.75300   25.18800 1.000 60.53334  ?  390 GLN A NE2    1 
ATOM   6109 H H      . GLN A 1 390 ? 8.60400   6.35200   19.92800 1.000 47.90671  ?  390 GLN A H      1 
ATOM   6110 H HA     . GLN A 1 390 ? 8.83600   6.57000   22.47200 1.000 52.69764  ?  390 GLN A HA     1 
ATOM   6111 H HB2    . GLN A 1 390 ? 6.80500   6.00800   21.87100 1.000 57.21341  ?  390 GLN A HB2    1 
ATOM   6112 H HB3    . GLN A 1 390 ? 7.31200   4.87000   20.88400 1.000 57.21341  ?  390 GLN A HB3    1 
ATOM   6113 H HG2    . GLN A 1 390 ? 6.16100   3.94500   22.70400 1.000 66.73129  ?  390 GLN A HG2    1 
ATOM   6114 H HG3    . GLN A 1 390 ? 7.66800   3.43900   22.68300 1.000 66.73129  ?  390 GLN A HG3    1 
ATOM   6115 H HE21   . GLN A 1 390 ? 7.29400   2.92300   24.97100 1.000 72.75777  ?  390 GLN A HE21   1 
ATOM   6116 H HE22   . GLN A 1 390 ? 7.45200   3.97600   26.01200 1.000 72.75777  ?  390 GLN A HE22   1 
ATOM   6117 N N      . ASP A 1 391 ? 10.43200  5.04000   23.45600 1.000 42.59150  ?  391 ASP A N      1 
ATOM   6118 C CA     . ASP A 1 391 ? 11.46900  4.17800   24.00400 1.000 47.24134  ?  391 ASP A CA     1 
ATOM   6119 C C      . ASP A 1 391 ? 11.16600  3.95600   25.47800 1.000 48.27969  ?  391 ASP A C      1 
ATOM   6120 O O      . ASP A 1 391 ? 11.06200  4.92000   26.24400 1.000 47.22231  ?  391 ASP A O      1 
ATOM   6121 C CB     . ASP A 1 391 ? 12.85200  4.80300   23.81600 1.000 46.23372  ?  391 ASP A CB     1 
ATOM   6122 C CG     . ASP A 1 391 ? 13.97100  3.83200   24.06700 1.000 44.96126  ?  391 ASP A CG     1 
ATOM   6123 O OD1    . ASP A 1 391 ? 14.15200  3.42100   25.23400 1.000 49.66564  ?  391 ASP A OD1    1 
ATOM   6124 O OD2    . ASP A 1 391 ? 14.68800  3.49300   23.10200 1.000 48.89822  -1 391 ASP A OD2    1 
ATOM   6125 H H      . ASP A 1 391 ? 10.23800  5.70800   23.96200 1.000 51.22756  ?  391 ASP A H      1 
ATOM   6126 H HA     . ASP A 1 391 ? 11.46400  3.31800   23.55600 1.000 56.80737  ?  391 ASP A HA     1 
ATOM   6127 H HB2    . ASP A 1 391 ? 12.93200  5.12300   22.90300 1.000 55.59823  ?  391 ASP A HB2    1 
ATOM   6128 H HB3    . ASP A 1 391 ? 12.95100  5.54200   24.43600 1.000 55.59823  ?  391 ASP A HB3    1 
ATOM   6129 N N      . HIS A 1 392 ? 11.03700  2.68400   25.86400 1.000 47.81719  ?  392 HIS A N      1 
ATOM   6130 C CA     . HIS A 1 392 ? 10.62300  2.34600   27.22100 1.000 55.05031  ?  392 HIS A CA     1 
ATOM   6131 C C      . HIS A 1 392 ? 11.45500  3.07800   28.26900 1.000 49.61692  ?  392 HIS A C      1 
ATOM   6132 O O      . HIS A 1 392 ? 10.91500  3.58200   29.25900 1.000 57.53623  ?  392 HIS A O      1 
ATOM   6133 C CB     . HIS A 1 392 ? 10.72600  0.82400   27.41200 1.000 65.31902  ?  392 HIS A CB     1 
ATOM   6134 C CG     . HIS A 1 392 ? 10.09700  0.32200   28.67100 1.000 72.03309  ?  392 HIS A CG     1 
ATOM   6135 N ND1    . HIS A 1 392 ? 10.83500  -0.00700  29.79300 1.000 73.74840  ?  392 HIS A ND1    1 
ATOM   6136 C CD2    . HIS A 1 392 ? 8.80300   0.06700   28.98000 1.000 84.11802  ?  392 HIS A CD2    1 
ATOM   6137 C CE1    . HIS A 1 392 ? 10.01600  -0.43200  30.74300 1.000 79.54510  ?  392 HIS A CE1    1 
ATOM   6138 N NE2    . HIS A 1 392 ? 8.78000   -0.39800  30.27600 1.000 91.26327  ?  392 HIS A NE2    1 
ATOM   6139 H H      . HIS A 1 392 ? 11.18300  2.00200   25.36100 1.000 57.49839  ?  392 HIS A H      1 
ATOM   6140 H HA     . HIS A 1 392 ? 9.70000   2.61600   27.34900 1.000 66.17814  ?  392 HIS A HA     1 
ATOM   6141 H HB2    . HIS A 1 392 ? 10.28400  0.38700   26.66700 1.000 78.50059  ?  392 HIS A HB2    1 
ATOM   6142 H HB3    . HIS A 1 392 ? 11.66400  0.57700   27.43300 1.000 78.50059  ?  392 HIS A HB3    1 
ATOM   6143 H HD1    . HIS A 1 392 ? 11.69000  0.05400   29.86200 1.000 88.61585  ?  392 HIS A HD1    1 
ATOM   6144 H HD2    . HIS A 1 392 ? 8.06800   0.18500   28.42200 1.000 101.05940 ?  392 HIS A HD2    1 
ATOM   6145 H HE1    . HIS A 1 392 ? 10.26900  -0.70700  31.59500 1.000 95.57189  ?  392 HIS A HE1    1 
ATOM   6146 N N      . TYR A 1 393 ? 12.76700  3.16100   28.06100 1.000 52.74682  ?  393 TYR A N      1 
ATOM   6147 C CA     . TYR A 1 393 ? 13.63400  3.79600   29.04200 1.000 48.58492  ?  393 TYR A CA     1 
ATOM   6148 C C      . TYR A 1 393 ? 13.67400  5.30900   28.87900 1.000 51.42409  ?  393 TYR A C      1 
ATOM   6149 O O      . TYR A 1 393 ? 13.65500  6.04100   29.88000 1.000 55.03774  ?  393 TYR A O      1 
ATOM   6150 C CB     . TYR A 1 393 ? 15.04600  3.22200   28.94300 1.000 50.12657  ?  393 TYR A CB     1 
ATOM   6151 C CG     . TYR A 1 393 ? 15.16400  1.78700   29.43900 1.000 50.90276  ?  393 TYR A CG     1 
ATOM   6152 C CD1    . TYR A 1 393 ? 14.63300  1.41100   30.66400 1.000 56.59939  ?  393 TYR A CD1    1 
ATOM   6153 C CD2    . TYR A 1 393 ? 15.80300  0.82500   28.67700 1.000 54.71290  ?  393 TYR A CD2    1 
ATOM   6154 C CE1    . TYR A 1 393 ? 14.73900  0.10500   31.11700 1.000 54.23603  ?  393 TYR A CE1    1 
ATOM   6155 C CE2    . TYR A 1 393 ? 15.92300  -0.48300  29.12100 1.000 55.56434  ?  393 TYR A CE2    1 
ATOM   6156 C CZ     . TYR A 1 393 ? 15.38700  -0.83500  30.33800 1.000 61.09605  ?  393 TYR A CZ     1 
ATOM   6157 O OH     . TYR A 1 393 ? 15.50500  -2.13000  30.78100 1.000 60.64277  ?  393 TYR A OH     1 
ATOM   6158 H H      . TYR A 1 393 ? 13.17400  2.86000   27.36600 1.000 63.41396  ?  393 TYR A H      1 
ATOM   6159 H HA     . TYR A 1 393 ? 13.28500  3.60100   29.92600 1.000 58.41968  ?  393 TYR A HA     1 
ATOM   6160 H HB2    . TYR A 1 393 ? 15.32400  3.23800   28.01300 1.000 60.26965  ?  393 TYR A HB2    1 
ATOM   6161 H HB3    . TYR A 1 393 ? 15.64300  3.77000   29.47600 1.000 60.26965  ?  393 TYR A HB3    1 
ATOM   6162 H HD1    . TYR A 1 393 ? 14.20000  2.04400   31.18900 1.000 68.03703  ?  393 TYR A HD1    1 
ATOM   6163 H HD2    . TYR A 1 393 ? 16.15900  1.06000   27.85100 1.000 65.77325  ?  393 TYR A HD2    1 
ATOM   6164 H HE1    . TYR A 1 393 ? 14.37600  -0.13700  31.93800 1.000 65.20101  ?  393 TYR A HE1    1 
ATOM   6165 H HE2    . TYR A 1 393 ? 16.36100  -1.11700  28.60000 1.000 66.79497  ?  393 TYR A HE2    1 
ATOM   6166 H HH     . TYR A 1 393 ? 15.14600  -2.20900  31.53600 1.000 72.88910  ?  393 TYR A HH     1 
ATOM   6167 N N      . LEU A 1 394 ? 13.73500  5.80100   27.64300 1.000 45.66499  ?  394 LEU A N      1 
ATOM   6168 C CA     . LEU A 1 394 ? 13.93900  7.23200   27.43400 1.000 46.15968  ?  394 LEU A CA     1 
ATOM   6169 C C      . LEU A 1 394 ? 12.68100  8.02800   27.76300 1.000 47.14583  ?  394 LEU A C      1 
ATOM   6170 O O      . LEU A 1 394 ? 12.76500  9.15200   28.26600 1.000 49.17423  ?  394 LEU A O      1 
ATOM   6171 C CB     . LEU A 1 394 ? 14.37700  7.50500   25.99600 1.000 41.79958  ?  394 LEU A CB     1 
ATOM   6172 C CG     . LEU A 1 394 ? 15.59500  6.74200   25.49100 1.000 47.06062  ?  394 LEU A CG     1 
ATOM   6173 C CD1    . LEU A 1 394 ? 16.03500  7.29500   24.13900 1.000 47.06548  ?  394 LEU A CD1    1 
ATOM   6174 C CD2    . LEU A 1 394 ? 16.74500  6.77400   26.48400 1.000 47.17308  ?  394 LEU A CD2    1 
ATOM   6175 H H      . LEU A 1 394 ? 13.66200  5.33800   26.92300 1.000 54.91576  ?  394 LEU A H      1 
ATOM   6176 H HA     . LEU A 1 394 ? 14.65000  7.52600   28.02500 1.000 55.50939  ?  394 LEU A HA     1 
ATOM   6177 H HB2    . LEU A 1 394 ? 13.63800  7.27900   25.41100 1.000 50.27726  ?  394 LEU A HB2    1 
ATOM   6178 H HB3    . LEU A 1 394 ? 14.58300  8.45000   25.92100 1.000 50.27726  ?  394 LEU A HB3    1 
ATOM   6179 H HG     . LEU A 1 394 ? 15.34600  5.81100   25.38400 1.000 56.59052  ?  394 LEU A HG     1 
ATOM   6180 H HD11   . LEU A 1 394 ? 16.87100  6.87500   23.88200 1.000 56.59635  ?  394 LEU A HD11   1 
ATOM   6181 H HD12   . LEU A 1 394 ? 15.35100  7.10000   23.48000 1.000 56.59635  ?  394 LEU A HD12   1 
ATOM   6182 H HD13   . LEU A 1 394 ? 16.15700  8.25500   24.21400 1.000 56.59635  ?  394 LEU A HD13   1 
ATOM   6183 H HD21   . LEU A 1 394 ? 17.52700  6.37500   26.07400 1.000 56.72547  ?  394 LEU A HD21   1 
ATOM   6184 H HD22   . LEU A 1 394 ? 16.93000  7.69600   26.72300 1.000 56.72547  ?  394 LEU A HD22   1 
ATOM   6185 H HD23   . LEU A 1 394 ? 16.49300  6.27200   27.27500 1.000 56.72547  ?  394 LEU A HD23   1 
ATOM   6186 N N      . ASN A 1 395 ? 11.50800  7.47000   27.47300 1.000 50.24665  ?  395 ASN A N      1 
ATOM   6187 C CA     . ASN A 1 395 ? 10.26600  8.17200   27.75900 1.000 47.53914  ?  395 ASN A CA     1 
ATOM   6188 C C      . ASN A 1 395 ? 10.08900  8.35100   29.26300 1.000 51.48711  ?  395 ASN A C      1 
ATOM   6189 O O      . ASN A 1 395 ? 9.99400   9.48100   29.76500 1.000 50.29787  ?  395 ASN A O      1 
ATOM   6190 C CB     . ASN A 1 395 ? 9.09100   7.40100   27.15200 1.000 51.53766  ?  395 ASN A CB     1 
ATOM   6191 C CG     . ASN A 1 395 ? 7.81600   8.23300   27.07300 1.000 51.18020  ?  395 ASN A CG     1 
ATOM   6192 O OD1    . ASN A 1 395 ? 7.80700   9.41700   27.39300 1.000 50.41064  ?  395 ASN A OD1    1 
ATOM   6193 N ND2    . ASN A 1 395 ? 6.73000   7.60500   26.63400 1.000 51.83296  ?  395 ASN A ND2    1 
ATOM   6194 H H      . ASN A 1 395 ? 11.40700  6.69500   27.11500 1.000 60.41375  ?  395 ASN A H      1 
ATOM   6195 H HA     . ASN A 1 395 ? 10.28700  9.05200   27.35200 1.000 57.16474  ?  395 ASN A HA     1 
ATOM   6196 H HB2    . ASN A 1 395 ? 9.32600   7.12500   26.25200 1.000 61.96297  ?  395 ASN A HB2    1 
ATOM   6197 H HB3    . ASN A 1 395 ? 8.90700   6.62200   27.70000 1.000 61.96297  ?  395 ASN A HB3    1 
ATOM   6198 H HD21   . ASN A 1 395 ? 6.77300   6.77400   26.41500 1.000 62.31732  ?  395 ASN A HD21   1 
ATOM   6199 H HD22   . ASN A 1 395 ? 5.98400   8.02800   26.57100 1.000 62.31732  ?  395 ASN A HD22   1 
ATOM   6200 N N      . ALA A 1 396 ? 10.09900  7.24100   30.00800 1.000 51.82720  ?  396 ALA A N      1 
ATOM   6201 C CA     . ALA A 1 396 ? 9.85100   7.30700   31.44000 1.000 55.85052  ?  396 ALA A CA     1 
ATOM   6202 C C      . ALA A 1 396 ? 10.90100  8.15000   32.15700 1.000 56.06980  ?  396 ALA A C      1 
ATOM   6203 O O      . ALA A 1 396 ? 10.56200  8.98300   33.00500 1.000 54.67911  ?  396 ALA A O      1 
ATOM   6204 C CB     . ALA A 1 396 ? 9.81200   5.89300   32.03600 1.000 62.95362  ?  396 ALA A CB     1 
ATOM   6205 H H      . ALA A 1 396 ? 10.24500  6.44800   29.70800 1.000 62.31041  ?  396 ALA A H      1 
ATOM   6206 H HA     . ALA A 1 396 ? 8.98600   7.72400   31.57900 1.000 67.13839  ?  396 ALA A HA     1 
ATOM   6207 H HB1    . ALA A 1 396 ? 9.64500   5.95700   32.99000 1.000 75.66212  ?  396 ALA A HB1    1 
ATOM   6208 H HB2    . ALA A 1 396 ? 9.10100   5.38900   31.60900 1.000 75.66212  ?  396 ALA A HB2    1 
ATOM   6209 H HB3    . ALA A 1 396 ? 10.66500  5.46000   31.87900 1.000 75.66212  ?  396 ALA A HB3    1 
ATOM   6210 N N      . ALA A 1 397 ? 12.17800  7.95200   31.82000 1.000 54.59273  ?  397 ALA A N      1 
ATOM   6211 C CA     . ALA A 1 397 ? 13.24100  8.66300   32.52400 1.000 55.93140  ?  397 ALA A CA     1 
ATOM   6212 C C      . ALA A 1 397 ? 13.10500  10.17800  32.35500 1.000 53.19569  ?  397 ALA A C      1 
ATOM   6213 O O      . ALA A 1 397 ? 13.33900  10.93400  33.29700 1.000 53.05803  ?  397 ALA A O      1 
ATOM   6214 C CB     . ALA A 1 397 ? 14.60800  8.19700   32.02300 1.000 55.16699  ?  397 ALA A CB     1 
ATOM   6215 H H      . ALA A 1 397 ? 12.44900  7.42100   31.20000 1.000 65.62904  ?  397 ALA A H      1 
ATOM   6216 H HA     . ALA A 1 397 ? 13.17700  8.45600   33.46900 1.000 67.23545  ?  397 ALA A HA     1 
ATOM   6217 H HB1    . ALA A 1 397 ? 15.30000  8.67700   32.50300 1.000 66.31815  ?  397 ALA A HB1    1 
ATOM   6218 H HB2    . ALA A 1 397 ? 14.69400  7.24400   32.18300 1.000 66.31815  ?  397 ALA A HB2    1 
ATOM   6219 H HB3    . ALA A 1 397 ? 14.67600  8.38000   31.07300 1.000 66.31815  ?  397 ALA A HB3    1 
ATOM   6220 N N      . ASN A 1 398 ? 12.73900  10.63100  31.15800 1.000 51.53015  ?  398 ASN A N      1 
ATOM   6221 C CA     . ASN A 1 398 ? 12.64700  12.06400  30.91500 1.000 53.62200  ?  398 ASN A CA     1 
ATOM   6222 C C      . ASN A 1 398 ? 11.46100  12.69100  31.64600 1.000 55.18747  ?  398 ASN A C      1 
ATOM   6223 O O      . ASN A 1 398 ? 11.54200  13.85200  32.06200 1.000 59.02869  ?  398 ASN A O      1 
ATOM   6224 C CB     . ASN A 1 398 ? 12.55500  12.33600  29.41100 1.000 47.33213  ?  398 ASN A CB     1 
ATOM   6225 C CG     . ASN A 1 398 ? 13.92100  12.49900  28.77100 1.000 48.79086  ?  398 ASN A CG     1 
ATOM   6226 O OD1    . ASN A 1 398 ? 14.46400  13.60000  28.71400 1.000 44.63175  ?  398 ASN A OD1    1 
ATOM   6227 N ND2    . ASN A 1 398 ? 14.49800  11.38800  28.29600 1.000 44.64527  ?  398 ASN A ND2    1 
ATOM   6228 H H      . ASN A 1 398 ? 12.54300  10.13700  30.48200 1.000 61.95395  ?  398 ASN A H      1 
ATOM   6229 H HA     . ASN A 1 398 ? 13.45300  12.48800  31.24700 1.000 64.46417  ?  398 ASN A HA     1 
ATOM   6230 H HB2    . ASN A 1 398 ? 12.10700  11.59100  28.98000 1.000 56.91632  ?  398 ASN A HB2    1 
ATOM   6231 H HB3    . ASN A 1 398 ? 12.05400  13.15300  29.26600 1.000 56.91632  ?  398 ASN A HB3    1 
ATOM   6232 H HD21   . ASN A 1 398 ? 14.09400  10.63100  28.36300 1.000 53.69210  ?  398 ASN A HD21   1 
ATOM   6233 H HD22   . ASN A 1 398 ? 15.27200  11.43000  27.92400 1.000 53.69210  ?  398 ASN A HD22   1 
ATOM   6234 N N      . TRP A 1 399 ? 10.35800  11.95700  31.80500 1.000 53.76902  ?  399 TRP A N      1 
ATOM   6235 C CA     . TRP A 1 399 ? 9.25500   12.46500  32.61600 1.000 55.94482  ?  399 TRP A CA     1 
ATOM   6236 C C      . TRP A 1 399 ? 9.68100   12.63800  34.07100 1.000 58.76664  ?  399 TRP A C      1 
ATOM   6237 O O      . TRP A 1 399 ? 9.36300   13.65200  34.70000 1.000 58.04989  ?  399 TRP A O      1 
ATOM   6238 C CB     . TRP A 1 399 ? 8.04900   11.52600  32.53000 1.000 55.96776  ?  399 TRP A CB     1 
ATOM   6239 C CG     . TRP A 1 399 ? 7.23900   11.68900  31.27200 1.000 55.34208  ?  399 TRP A CG     1 
ATOM   6240 C CD1    . TRP A 1 399 ? 7.35200   10.95300  30.12400 1.000 49.93152  ?  399 TRP A CD1    1 
ATOM   6241 C CD2    . TRP A 1 399 ? 6.18800   12.64000  31.03800 1.000 56.93065  ?  399 TRP A CD2    1 
ATOM   6242 N NE1    . TRP A 1 399 ? 6.44000   11.38800  29.19400 1.000 51.76759  ?  399 TRP A NE1    1 
ATOM   6243 C CE2    . TRP A 1 399 ? 5.71400   12.42300  29.72500 1.000 50.27708  ?  399 TRP A CE2    1 
ATOM   6244 C CE3    . TRP A 1 399 ? 5.60700   13.65300  31.80400 1.000 57.54814  ?  399 TRP A CE3    1 
ATOM   6245 C CZ2    . TRP A 1 399 ? 4.69400   13.18400  29.16400 1.000 49.48272  ?  399 TRP A CZ2    1 
ATOM   6246 C CZ3    . TRP A 1 399 ? 4.59000   14.40800  31.24600 1.000 60.58970  ?  399 TRP A CZ3    1 
ATOM   6247 C CH2    . TRP A 1 399 ? 4.14300   14.17100  29.94200 1.000 57.48275  ?  399 TRP A CH2    1 
ATOM   6248 H H      . TRP A 1 399 ? 10.22700  11.17900  31.46200 1.000 64.64059  ?  399 TRP A H      1 
ATOM   6249 H HA     . TRP A 1 399 ? 8.98800   13.32900  32.26500 1.000 67.25155  ?  399 TRP A HA     1 
ATOM   6250 H HB2    . TRP A 1 399 ? 8.36400   10.61000  32.56100 1.000 67.27908  ?  399 TRP A HB2    1 
ATOM   6251 H HB3    . TRP A 1 399 ? 7.46300   11.70200  33.28300 1.000 67.27908  ?  399 TRP A HB3    1 
ATOM   6252 H HD1    . TRP A 1 399 ? 7.95800   10.26000  29.99300 1.000 60.03559  ?  399 TRP A HD1    1 
ATOM   6253 H HE1    . TRP A 1 399 ? 6.34000   11.06200  28.40500 1.000 62.23888  ?  399 TRP A HE1    1 
ATOM   6254 H HE3    . TRP A 1 399 ? 5.89900   13.81700  32.67200 1.000 69.17554  ?  399 TRP A HE3    1 
ATOM   6255 H HZ2    . TRP A 1 399 ? 4.39800   13.03000  28.29600 1.000 59.49703  ?  399 TRP A HZ2    1 
ATOM   6256 H HZ3    . TRP A 1 399 ? 4.19600   15.08600  31.74800 1.000 72.82542  ?  399 TRP A HZ3    1 
ATOM   6257 H HH2    . TRP A 1 399 ? 3.45700   14.69400  29.59500 1.000 69.09707  ?  399 TRP A HH2    1 
ATOM   6258 N N      . MET A 1 400 ? 10.40500  11.65800  34.61700 1.000 57.54699  ?  400 MET A N      1 
ATOM   6259 C CA     . MET A 1 400 ? 10.80000  11.72400  36.02000 1.000 62.40017  ?  400 MET A CA     1 
ATOM   6260 C C      . MET A 1 400 ? 11.88100  12.77300  36.24800 1.000 65.16240  ?  400 MET A C      1 
ATOM   6261 O O      . MET A 1 400 ? 11.87000  13.46700  37.27100 1.000 71.47264  ?  400 MET A O      1 
ATOM   6262 C CB     . MET A 1 400 ? 11.28200  10.35300  36.49500 1.000 61.97796  ?  400 MET A CB     1 
ATOM   6263 C CG     . MET A 1 400 ? 10.38500  9.20400   36.08700 1.000 66.25006  ?  400 MET A CG     1 
ATOM   6264 S SD     . MET A 1 400 ? 10.55600  7.76900   37.16800 1.000 73.26097  ?  400 MET A SD     1 
ATOM   6265 C CE     . MET A 1 400 ? 12.16500  7.18000   36.67700 1.000 76.42785  ?  400 MET A CE     1 
ATOM   6266 H H      . MET A 1 400 ? 10.67600  10.95500  34.20200 1.000 69.17415  ?  400 MET A H      1 
ATOM   6267 H HA     . MET A 1 400 ? 10.01900  11.96600  36.54200 1.000 74.99798  ?  400 MET A HA     1 
ATOM   6268 H HB2    . MET A 1 400 ? 12.16200  10.18700  36.12200 1.000 74.49132  ?  400 MET A HB2    1 
ATOM   6269 H HB3    . MET A 1 400 ? 11.32900  10.36000  37.46400 1.000 74.49132  ?  400 MET A HB3    1 
ATOM   6270 H HG2    . MET A 1 400 ? 9.46100   9.49700   36.12100 1.000 79.61784  ?  400 MET A HG2    1 
ATOM   6271 H HG3    . MET A 1 400 ? 10.61400  8.92900   35.18500 1.000 79.61784  ?  400 MET A HG3    1 
ATOM   6272 H HE1    . MET A 1 400 ? 12.38700  6.39400   37.20100 1.000 91.83119  ?  400 MET A HE1    1 
ATOM   6273 H HE2    . MET A 1 400 ? 12.14400  6.95300   35.73400 1.000 91.83119  ?  400 MET A HE2    1 
ATOM   6274 H HE3    . MET A 1 400 ? 12.81900  7.87800   36.83500 1.000 91.83119  ?  400 MET A HE3    1 
ATOM   6275 N N      . TRP A 1 401 ? 12.83400  12.89400  35.32100 1.000 62.24737  ?  401 TRP A N      1 
ATOM   6276 C CA     . TRP A 1 401 ? 13.87700  13.90600  35.44100 1.000 66.46773  ?  401 TRP A CA     1 
ATOM   6277 C C      . TRP A 1 401 ? 13.33500  15.32000  35.27700 1.000 71.70424  ?  401 TRP A C      1 
ATOM   6278 O O      . TRP A 1 401 ? 14.04800  16.28100  35.59400 1.000 78.98836  ?  401 TRP A O      1 
ATOM   6279 C CB     . TRP A 1 401 ? 14.98100  13.66000  34.40800 1.000 65.30622  ?  401 TRP A CB     1 
ATOM   6280 C CG     . TRP A 1 401 ? 16.22700  13.07500  35.00400 1.000 66.31765  ?  401 TRP A CG     1 
ATOM   6281 C CD1    . TRP A 1 401 ? 17.43100  13.70100  35.17000 1.000 69.93490  ?  401 TRP A CD1    1 
ATOM   6282 C CD2    . TRP A 1 401 ? 16.39000  11.74600  35.51800 1.000 75.70515  ?  401 TRP A CD2    1 
ATOM   6283 N NE1    . TRP A 1 401 ? 18.33300  12.84800  35.76100 1.000 74.56649  ?  401 TRP A NE1    1 
ATOM   6284 C CE2    . TRP A 1 401 ? 17.72000  11.63900  35.98400 1.000 83.78701  ?  401 TRP A CE2    1 
ATOM   6285 C CE3    . TRP A 1 401 ? 15.54100  10.63500  35.63400 1.000 68.63800  ?  401 TRP A CE3    1 
ATOM   6286 C CZ2    . TRP A 1 401 ? 18.22200  10.46400  36.55200 1.000 79.01834  ?  401 TRP A CZ2    1 
ATOM   6287 C CZ3    . TRP A 1 401 ? 16.04400  9.46900   36.19700 1.000 73.46456  ?  401 TRP A CZ3    1 
ATOM   6288 C CH2    . TRP A 1 401 ? 17.37000  9.39200   36.64800 1.000 71.23658  ?  401 TRP A CH2    1 
ATOM   6289 H H      . TRP A 1 401 ? 12.89500  12.40400  34.61700 1.000 74.81461  ?  401 TRP A H      1 
ATOM   6290 H HA     . TRP A 1 401 ? 14.27600  13.83200  36.32200 1.000 79.87905  ?  401 TRP A HA     1 
ATOM   6291 H HB2    . TRP A 1 401 ? 14.65200  13.04100  33.73800 1.000 78.48524  ?  401 TRP A HB2    1 
ATOM   6292 H HB3    . TRP A 1 401 ? 15.21700  14.50400  33.99300 1.000 78.48524  ?  401 TRP A HB3    1 
ATOM   6293 H HD1    . TRP A 1 401 ? 17.61300  14.57800  34.92000 1.000 84.03965  ?  401 TRP A HD1    1 
ATOM   6294 H HE1    . TRP A 1 401 ? 19.14800  13.04000  35.95800 1.000 89.59756  ?  401 TRP A HE1    1 
ATOM   6295 H HE3    . TRP A 1 401 ? 14.66000  10.67800  35.33900 1.000 82.48337  ?  401 TRP A HE3    1 
ATOM   6296 H HZ2    . TRP A 1 401 ? 19.10000  10.41000  36.85300 1.000 94.93978  ?  401 TRP A HZ2    1 
ATOM   6297 H HZ3    . TRP A 1 401 ? 15.49100  8.72600   36.27600 1.000 88.27525  ?  401 TRP A HZ3    1 
ATOM   6298 H HH2    . TRP A 1 401 ? 17.67800  8.59700   37.02000 1.000 85.60167  ?  401 TRP A HH2    1 
ATOM   6299 N N      . LEU A 1 402 ? 12.09900  15.46600  34.79400 1.000 74.45049  ?  402 LEU A N      1 
ATOM   6300 C CA     . LEU A 1 402 ? 11.48300  16.78300  34.69000 1.000 71.27570  ?  402 LEU A CA     1 
ATOM   6301 C C      . LEU A 1 402 ? 11.39900  17.45700  36.05400 1.000 83.98251  ?  402 LEU A C      1 
ATOM   6302 O O      . LEU A 1 402 ? 11.71500  18.64500  36.18900 1.000 84.90192  ?  402 LEU A O      1 
ATOM   6303 C CB     . LEU A 1 402 ? 10.09100  16.65100  34.07600 1.000 75.10690  ?  402 LEU A CB     1 
ATOM   6304 C CG     . LEU A 1 402 ? 9.62500   17.75700  33.13400 1.000 83.04417  ?  402 LEU A CG     1 
ATOM   6305 C CD1    . LEU A 1 402 ? 10.22100  17.55900  31.75300 1.000 82.90023  ?  402 LEU A CD1    1 
ATOM   6306 C CD2    . LEU A 1 402 ? 8.10400   17.78000  33.07100 1.000 82.38276  ?  402 LEU A CD2    1 
ATOM   6307 H H      . LEU A 1 402 ? 11.60000  14.82000  34.52200 1.000 89.45836  ?  402 LEU A H      1 
ATOM   6308 H HA     . LEU A 1 402 ? 12.02300  17.34200  34.11000 1.000 85.64861  ?  402 LEU A HA     1 
ATOM   6309 H HB2    . LEU A 1 402 ? 10.06900  15.82400  33.57000 1.000 90.24604  ?  402 LEU A HB2    1 
ATOM   6310 H HB3    . LEU A 1 402 ? 9.45000   16.61300  34.80300 1.000 90.24604  ?  402 LEU A HB3    1 
ATOM   6311 H HG     . LEU A 1 402 ? 9.92600   18.61700  33.46700 1.000 99.77077  ?  402 LEU A HG     1 
ATOM   6312 H HD11   . LEU A 1 402 ? 9.84200   18.21700  31.14800 1.000 99.59805  ?  402 LEU A HD11   1 
ATOM   6313 H HD12   . LEU A 1 402 ? 11.18300  17.67400  31.80500 1.000 99.59805  ?  402 LEU A HD12   1 
ATOM   6314 H HD13   . LEU A 1 402 ? 10.01000  16.66500  31.44300 1.000 99.59805  ?  402 LEU A HD13   1 
ATOM   6315 H HD21   . LEU A 1 402 ? 7.82400   18.48000  32.46200 1.000 98.97708  ?  402 LEU A HD21   1 
ATOM   6316 H HD22   . LEU A 1 402 ? 7.78800   16.91900  32.75400 1.000 98.97708  ?  402 LEU A HD22   1 
ATOM   6317 H HD23   . LEU A 1 402 ? 7.75400   17.95400  33.95900 1.000 98.97708  ?  402 LEU A HD23   1 
ATOM   6318 N N      . SER A 1 403 ? 10.98000  16.71300  37.07300 1.000 87.97781  ?  403 SER A N      1 
ATOM   6319 C CA     . SER A 1 403 ? 10.82000  17.25500  38.41800 1.000 98.58298  ?  403 SER A CA     1 
ATOM   6320 C C      . SER A 1 403 ? 12.15000  17.73100  38.99700 1.000 101.65242 ?  403 SER A C      1 
ATOM   6321 O O      . SER A 1 403 ? 12.99600  16.92700  39.38900 1.000 93.69048  ?  403 SER A O      1 
ATOM   6322 C CB     . SER A 1 403 ? 10.19700  16.19800  39.33400 1.000 97.88206  ?  403 SER A CB     1 
ATOM   6323 O OG     . SER A 1 403 ? 9.31800   15.35300  38.60700 1.000 94.62574  ?  403 SER A OG     1 
ATOM   6324 H H      . SER A 1 403 ? 10.77800  15.88000  37.01000 1.000 105.69114 ?  403 SER A H      1 
ATOM   6325 H HA     . SER A 1 403 ? 10.22900  18.02300  38.38000 1.000 118.41735 ?  403 SER A HA     1 
ATOM   6326 H HB2    . SER A 1 403 ? 10.90500  15.65900  39.72100 1.000 117.57625 ?  403 SER A HB2    1 
ATOM   6327 H HB3    . SER A 1 403 ? 9.69800   16.64300  40.03700 1.000 117.57625 ?  403 SER A HB3    1 
ATOM   6328 H HG     . SER A 1 403 ? 8.99100   14.77200  39.11800 1.000 113.66866 ?  403 SER A HG     1 
ATOM   6329 N N      . TYR A 1 411 ? 14.28100  27.56400  33.00400 1.000 93.47604  ?  411 TYR A N      1 
ATOM   6330 C CA     . TYR A 1 411 ? 13.88600  27.53900  31.60000 1.000 92.70270  ?  411 TYR A CA     1 
ATOM   6331 C C      . TYR A 1 411 ? 12.76900  28.54000  31.33800 1.000 87.79830  ?  411 TYR A C      1 
ATOM   6332 O O      . TYR A 1 411 ? 12.81400  29.30600  30.37600 1.000 91.23143  ?  411 TYR A O      1 
ATOM   6333 C CB     . TYR A 1 411 ? 13.43300  26.13600  31.19000 1.000 95.50982  ?  411 TYR A CB     1 
ATOM   6334 C CG     . TYR A 1 411 ? 14.46400  25.37100  30.39400 1.000 100.71742 ?  411 TYR A CG     1 
ATOM   6335 C CD1    . TYR A 1 411 ? 14.87400  25.81600  29.14500 1.000 90.16397  ?  411 TYR A CD1    1 
ATOM   6336 C CD2    . TYR A 1 411 ? 15.02800  24.20400  30.89200 1.000 100.93605 ?  411 TYR A CD2    1 
ATOM   6337 C CE1    . TYR A 1 411 ? 15.82000  25.12400  28.41700 1.000 93.16543  ?  411 TYR A CE1    1 
ATOM   6338 C CE2    . TYR A 1 411 ? 15.97200  23.50200  30.17000 1.000 97.73403  ?  411 TYR A CE2    1 
ATOM   6339 C CZ     . TYR A 1 411 ? 16.36600  23.96800  28.93500 1.000 95.16580  ?  411 TYR A CZ     1 
ATOM   6340 O OH     . TYR A 1 411 ? 17.30700  23.27400  28.20900 1.000 96.93921  ?  411 TYR A OH     1 
ATOM   6341 H H      . TYR A 1 411 ? 14.50800  28.34100  33.29000 1.000 112.28902 ?  411 TYR A H      1 
ATOM   6342 H HA     . TYR A 1 411 ? 14.65000  27.77900  31.05300 1.000 111.36101 ?  411 TYR A HA     1 
ATOM   6343 H HB2    . TYR A 1 411 ? 13.23800  25.62500  31.99100 1.000 114.72956 ?  411 TYR A HB2    1 
ATOM   6344 H HB3    . TYR A 1 411 ? 12.63500  26.21300  30.64400 1.000 114.72956 ?  411 TYR A HB3    1 
ATOM   6345 H HD1    . TYR A 1 411 ? 14.50600  26.59400  28.79300 1.000 108.31453 ?  411 TYR A HD1    1 
ATOM   6346 H HD2    . TYR A 1 411 ? 14.76600  23.89000  31.72700 1.000 121.24103 ?  411 TYR A HD2    1 
ATOM   6347 H HE1    . TYR A 1 411 ? 16.08700  25.43500  27.58200 1.000 111.91629 ?  411 TYR A HE1    1 
ATOM   6348 H HE2    . TYR A 1 411 ? 16.34000  22.72100  30.51500 1.000 117.39861 ?  411 TYR A HE2    1 
ATOM   6349 H HH     . TYR A 1 411 ? 17.55500  22.59500  28.63600 1.000 116.44482 ?  411 TYR A HH     1 
ATOM   6350 N N      . PHE A 1 412 ? 11.76100  28.51900  32.20400 1.000 92.34456  ?  412 PHE A N      1 
ATOM   6351 C CA     . PHE A 1 412 ? 10.59800  29.39700  32.10100 1.000 83.68766  ?  412 PHE A CA     1 
ATOM   6352 C C      . PHE A 1 412 ? 10.71000  30.57800  33.05400 1.000 94.50235  ?  412 PHE A C      1 
ATOM   6353 O O      . PHE A 1 412 ? 9.71400   31.04800  33.61300 1.000 92.99125  ?  412 PHE A O      1 
ATOM   6354 C CB     . PHE A 1 412 ? 9.32700   28.59700  32.35600 1.000 88.67657  ?  412 PHE A CB     1 
ATOM   6355 C CG     . PHE A 1 412 ? 9.22900   27.35100  31.51900 1.000 88.08290  ?  412 PHE A CG     1 
ATOM   6356 C CD1    . PHE A 1 412 ? 9.11200   27.43600  30.13900 1.000 82.29987  ?  412 PHE A CD1    1 
ATOM   6357 C CD2    . PHE A 1 412 ? 9.26600   26.09700  32.10400 1.000 80.04236  ?  412 PHE A CD2    1 
ATOM   6358 C CE1    . PHE A 1 412 ? 9.02500   26.28900  29.36100 1.000 73.75330  ?  412 PHE A CE1    1 
ATOM   6359 C CE2    . PHE A 1 412 ? 9.18100   24.95100  31.33100 1.000 77.93061  ?  412 PHE A CE2    1 
ATOM   6360 C CZ     . PHE A 1 412 ? 9.06100   25.04800  29.95800 1.000 67.60103  ?  412 PHE A CZ     1 
ATOM   6361 H H      . PHE A 1 412 ? 11.72600  27.98900  32.88100 1.000 110.93124 ?  412 PHE A H      1 
ATOM   6362 H HA     . PHE A 1 412 ? 10.54000  29.75700  31.20200 1.000 100.54296 ?  412 PHE A HA     1 
ATOM   6363 H HB2    . PHE A 1 412 ? 9.30600   28.33200  33.28900 1.000 106.52965 ?  412 PHE A HB2    1 
ATOM   6364 H HB3    . PHE A 1 412 ? 8.56000   29.15400  32.15200 1.000 106.52965 ?  412 PHE A HB3    1 
ATOM   6365 H HD1    . PHE A 1 412 ? 9.09100   28.27100  29.73000 1.000 98.87761  ?  412 PHE A HD1    1 
ATOM   6366 H HD2    . PHE A 1 412 ? 9.34900   26.02300  33.02700 1.000 96.16861  ?  412 PHE A HD2    1 
ATOM   6367 H HE1    . PHE A 1 412 ? 8.94100   26.35900  28.43700 1.000 88.62172  ?  412 PHE A HE1    1 
ATOM   6368 H HE2    . PHE A 1 412 ? 9.20400   24.11400  31.73700 1.000 93.63450  ?  412 PHE A HE2    1 
ATOM   6369 H HZ     . PHE A 1 412 ? 9.00600   24.27900  29.43900 1.000 81.23901  ?  412 PHE A HZ     1 
ATOM   6370 N N      . ARG A 1 413 ? 11.93700  31.07500  33.24700 1.000 89.28263  ?  413 ARG A N      1 
ATOM   6371 C CA     . ARG A 1 413 ? 12.16000  32.20700  34.13700 1.000 84.19919  ?  413 ARG A CA     1 
ATOM   6372 C C      . ARG A 1 413 ? 11.34400  33.41700  33.70300 1.000 92.63371  ?  413 ARG A C      1 
ATOM   6373 O O      . ARG A 1 413 ? 10.67100  34.05100  34.52200 1.000 87.73239  ?  413 ARG A O      1 
ATOM   6374 C CB     . ARG A 1 413 ? 13.65300  32.55200  34.17300 1.000 105.49795 ?  413 ARG A CB     1 
ATOM   6375 C CG     . ARG A 1 413 ? 14.37400  32.38500  32.83200 1.000 97.12276  ?  413 ARG A CG     1 
ATOM   6376 C CD     . ARG A 1 413 ? 15.75400  33.02300  32.84400 1.000 97.08145  ?  413 ARG A CD     1 
ATOM   6377 N NE     . ARG A 1 413 ? 15.71900  34.41900  32.41400 1.000 104.45648 ?  413 ARG A NE     1 
ATOM   6378 C CZ     . ARG A 1 413 ? 15.90100  35.46400  33.21500 1.000 102.70476 ?  413 ARG A CZ     1 
ATOM   6379 N NH1    . ARG A 1 413 ? 16.11400  35.31700  34.51400 1.000 103.95914 ?  413 ARG A NH1    1 
ATOM   6380 N NH2    . ARG A 1 413 ? 15.86900  36.68900  32.69800 1.000 110.72424 ?  413 ARG A NH2    1 
ATOM   6381 H H      . ARG A 1 413 ? 12.65100  30.77300  32.87500 1.000 107.25693 ?  413 ARG A H      1 
ATOM   6382 H HA     . ARG A 1 413 ? 11.88000  31.96100  35.03300 1.000 101.15679 ?  413 ARG A HA     1 
ATOM   6383 H HB2    . ARG A 1 413 ? 13.74900  33.47900  34.44400 1.000 126.71531 ?  413 ARG A HB2    1 
ATOM   6384 H HB3    . ARG A 1 413 ? 14.08900  31.97200  34.81500 1.000 126.71531 ?  413 ARG A HB3    1 
ATOM   6385 H HG2    . ARG A 1 413 ? 14.47900  31.44000  32.64200 1.000 116.66508 ?  413 ARG A HG2    1 
ATOM   6386 H HG3    . ARG A 1 413 ? 13.85100  32.80800  32.13300 1.000 116.66508 ?  413 ARG A HG3    1 
ATOM   6387 H HD2    . ARG A 1 413 ? 16.11100  32.99300  33.74500 1.000 116.61550 ?  413 ARG A HD2    1 
ATOM   6388 H HD3    . ARG A 1 413 ? 16.33600  32.53500  32.24000 1.000 116.61550 ?  413 ARG A HD3    1 
ATOM   6389 H HE     . ARG A 1 413 ? 15.57000  34.57600  31.58200 1.000 125.46555 ?  413 ARG A HE     1 
ATOM   6390 H HH11   . ARG A 1 413 ? 16.13700  34.53000  34.85900 1.000 124.86874 ?  413 ARG A HH11   1 
ATOM   6391 H HH12   . ARG A 1 413 ? 16.22800  36.00900  35.01200 1.000 124.86874 ?  413 ARG A HH12   1 
ATOM   6392 H HH21   . ARG A 1 413 ? 15.73300  36.79600  31.85500 1.000 132.98685 ?  413 ARG A HH21   1 
ATOM   6393 H HH22   . ARG A 1 413 ? 15.98600  37.37300  33.20500 1.000 132.98685 ?  413 ARG A HH22   1 
ATOM   6394 N N      . VAL A 1 414 ? 11.39100  33.74800  32.41600 1.000 96.87144  ?  414 VAL A N      1 
ATOM   6395 C CA     . VAL A 1 414 ? 10.66600  34.89200  31.87100 1.000 97.68135  ?  414 VAL A CA     1 
ATOM   6396 C C      . VAL A 1 414 ? 9.38700   34.45700  31.16700 1.000 86.51558  ?  414 VAL A C      1 
ATOM   6397 O O      . VAL A 1 414 ? 8.32600   35.05000  31.36600 1.000 96.98111  ?  414 VAL A O      1 
ATOM   6398 C CB     . VAL A 1 414 ? 11.58000  35.70000  30.91900 1.000 100.03789 ?  414 VAL A CB     1 
ATOM   6399 C CG1    . VAL A 1 414 ? 11.01900  37.09800  30.69700 1.000 93.27647  ?  414 VAL A CG1    1 
ATOM   6400 C CG2    . VAL A 1 414 ? 12.99900  35.77200  31.46600 1.000 96.29495  ?  414 VAL A CG2    1 
ATOM   6401 H H      . VAL A 1 414 ? 11.84500  33.31600  31.82700 1.000 116.36349 ?  414 VAL A H      1 
ATOM   6402 H HA     . VAL A 1 414 ? 10.41500  35.47100  32.60700 1.000 117.33539 ?  414 VAL A HA     1 
ATOM   6403 H HB     . VAL A 1 414 ? 11.61100  35.24800  30.06100 1.000 120.16324 ?  414 VAL A HB     1 
ATOM   6404 H HG11   . VAL A 1 414 ? 11.59900  37.57800  30.08600 1.000 112.04954 ?  414 VAL A HG11   1 
ATOM   6405 H HG12   . VAL A 1 414 ? 10.12800  37.02500  30.32000 1.000 112.04954 ?  414 VAL A HG12   1 
ATOM   6406 H HG13   . VAL A 1 414 ? 10.98100  37.56200  31.54900 1.000 112.04954 ?  414 VAL A HG13   1 
ATOM   6407 H HG21   . VAL A 1 414 ? 13.48900  36.45600  30.98300 1.000 115.67171 ?  414 VAL A HG21   1 
ATOM   6408 H HG22   . VAL A 1 414 ? 12.96300  35.99500  32.40900 1.000 115.67171 ?  414 VAL A HG22   1 
ATOM   6409 H HG23   . VAL A 1 414 ? 13.42800  34.91100  31.34500 1.000 115.67171 ?  414 VAL A HG23   1 
ATOM   6410 N N      . TYR A 1 415 ? 9.47100   33.41800  30.33800 1.000 92.66903  ?  415 TYR A N      1 
ATOM   6411 C CA     . TYR A 1 415 ? 8.33400   32.92300  29.57200 1.000 88.27821  ?  415 TYR A CA     1 
ATOM   6412 C C      . TYR A 1 415 ? 7.80700   31.64900  30.22100 1.000 83.83852  ?  415 TYR A C      1 
ATOM   6413 O O      . TYR A 1 415 ? 8.51300   30.63600  30.27400 1.000 70.53097  ?  415 TYR A O      1 
ATOM   6414 C CB     . TYR A 1 415 ? 8.72600   32.65200  28.12000 1.000 74.23346  ?  415 TYR A CB     1 
ATOM   6415 C CG     . TYR A 1 415 ? 9.04000   33.89800  27.33000 1.000 78.43272  ?  415 TYR A CG     1 
ATOM   6416 C CD1    . TYR A 1 415 ? 10.32600  34.43400  27.32300 1.000 84.38131  ?  415 TYR A CD1    1 
ATOM   6417 C CD2    . TYR A 1 415 ? 8.05300   34.54600  26.59400 1.000 78.92949  ?  415 TYR A CD2    1 
ATOM   6418 C CE1    . TYR A 1 415 ? 10.62200  35.58000  26.60600 1.000 77.95674  ?  415 TYR A CE1    1 
ATOM   6419 C CE2    . TYR A 1 415 ? 8.33500   35.69500  25.86900 1.000 75.16313  ?  415 TYR A CE2    1 
ATOM   6420 C CZ     . TYR A 1 415 ? 9.62500   36.20600  25.87800 1.000 84.62901  ?  415 TYR A CZ     1 
ATOM   6421 O OH     . TYR A 1 415 ? 9.91700   37.34700  25.16100 1.000 76.28603  ?  415 TYR A OH     1 
ATOM   6422 H H      . TYR A 1 415 ? 10.19500  32.97500  30.20100 1.000 111.32060 ?  415 TYR A H      1 
ATOM   6423 H HA     . TYR A 1 415 ? 7.63100   33.59100  29.58300 1.000 106.05162 ?  415 TYR A HA     1 
ATOM   6424 H HB2    . TYR A 1 415 ? 9.51500   32.08800  28.11000 1.000 89.19793  ?  415 TYR A HB2    1 
ATOM   6425 H HB3    . TYR A 1 415 ? 7.99000   32.20000  27.67800 1.000 89.19793  ?  415 TYR A HB3    1 
ATOM   6426 H HD1    . TYR A 1 415 ? 10.99800  34.01300  27.81000 1.000 101.37535 ?  415 TYR A HD1    1 
ATOM   6427 H HD2    . TYR A 1 415 ? 7.18900   34.20200  26.58700 1.000 94.83316  ?  415 TYR A HD2    1 
ATOM   6428 H HE1    . TYR A 1 415 ? 11.48500  35.92600  26.61300 1.000 93.66585  ?  415 TYR A HE1    1 
ATOM   6429 H HE2    . TYR A 1 415 ? 7.66600   36.11800  25.38200 1.000 90.31352  ?  415 TYR A HE2    1 
ATOM   6430 H HH     . TYR A 1 415 ? 10.72800  37.54400  25.25300 1.000 91.66101  ?  415 TYR A HH     1 
ATOM   6431 N N      . SER A 1 416 ? 6.56200   31.70200  30.69800 1.000 74.39295  ?  416 SER A N      1 
ATOM   6432 C CA     . SER A 1 416 ? 5.92100   30.52000  31.24400 1.000 70.16796  ?  416 SER A CA     1 
ATOM   6433 C C      . SER A 1 416 ? 5.74200   29.49200  30.13100 1.000 63.28618  ?  416 SER A C      1 
ATOM   6434 O O      . SER A 1 416 ? 5.73500   29.84000  28.94900 1.000 61.32505  ?  416 SER A O      1 
ATOM   6435 C CB     . SER A 1 416 ? 4.57700   30.88000  31.86100 1.000 78.21291  ?  416 SER A CB     1 
ATOM   6436 O OG     . SER A 1 416 ? 3.61600   31.14800  30.85500 1.000 65.41715  ?  416 SER A OG     1 
ATOM   6437 H H      . SER A 1 416 ? 6.07300   32.41000  30.71500 1.000 89.38931  ?  416 SER A H      1 
ATOM   6438 H HA     . SER A 1 416 ? 6.46800   30.13100  31.94500 1.000 84.31933  ?  416 SER A HA     1 
ATOM   6439 H HB2    . SER A 1 416 ? 4.26800   30.13700  32.40200 1.000 93.97326  ?  416 SER A HB2    1 
ATOM   6440 H HB3    . SER A 1 416 ? 4.68400   31.67000  32.41300 1.000 93.97326  ?  416 SER A HB3    1 
ATOM   6441 H HG     . SER A 1 416 ? 2.88800   31.37400  31.20600 1.000 78.61834  ?  416 SER A HG     1 
ATOM   6442 N N      . PRO A 1 417 ? 5.59100   28.21300  30.48300 1.000 68.89037  ?  417 PRO A N      1 
ATOM   6443 C CA     . PRO A 1 417 ? 5.49700   27.18400  29.43200 1.000 61.32919  ?  417 PRO A CA     1 
ATOM   6444 C C      . PRO A 1 417 ? 4.36200   27.44000  28.46300 1.000 61.57532  ?  417 PRO A C      1 
ATOM   6445 O O      . PRO A 1 417 ? 4.40300   26.94200  27.33100 1.000 57.43654  ?  417 PRO A O      1 
ATOM   6446 C CB     . PRO A 1 417 ? 5.29000   25.87400  30.20600 1.000 65.48594  ?  417 PRO A CB     1 
ATOM   6447 C CG     . PRO A 1 417 ? 5.29800   26.22000  31.66100 1.000 74.79739  ?  417 PRO A CG     1 
ATOM   6448 C CD     . PRO A 1 417 ? 5.24800   27.70000  31.82200 1.000 69.47154  ?  417 PRO A CD     1 
ATOM   6449 H HA     . PRO A 1 417 ? 6.33700   27.12300  28.95100 1.000 73.71280  ?  417 PRO A HA     1 
ATOM   6450 H HB2    . PRO A 1 417 ? 4.43800   25.48300  29.95400 1.000 78.70090  ?  417 PRO A HB2    1 
ATOM   6451 H HB3    . PRO A 1 417 ? 6.01100   25.26000  29.99800 1.000 78.70090  ?  417 PRO A HB3    1 
ATOM   6452 H HG2    . PRO A 1 417 ? 4.52300   25.81500  32.08100 1.000 89.87464  ?  417 PRO A HG2    1 
ATOM   6453 H HG3    . PRO A 1 417 ? 6.11100   25.87200  32.05900 1.000 89.87464  ?  417 PRO A HG3    1 
ATOM   6454 H HD2    . PRO A 1 417 ? 4.35800   27.98700  32.08100 1.000 83.48362  ?  417 PRO A HD2    1 
ATOM   6455 H HD3    . PRO A 1 417 ? 5.89700   27.99500  32.48000 1.000 83.48362  ?  417 PRO A HD3    1 
ATOM   6456 N N      . VAL A 1 418 ? 3.35500   28.21600  28.86700 1.000 56.47899  ?  418 VAL A N      1 
ATOM   6457 C CA     . VAL A 1 418 ? 2.18800   28.44300  28.02400 1.000 63.47016  ?  418 VAL A CA     1 
ATOM   6458 C C      . VAL A 1 418 ? 2.45200   29.46800  26.92800 1.000 58.17993  ?  418 VAL A C      1 
ATOM   6459 O O      . VAL A 1 418 ? 1.75300   29.45400  25.90800 1.000 50.21653  ?  418 VAL A O      1 
ATOM   6460 C CB     . VAL A 1 418 ? 1.01300   28.83700  28.94800 1.000 69.78799  ?  418 VAL A CB     1 
ATOM   6461 C CG1    . VAL A 1 418 ? 0.44300   30.20200  28.59000 1.000 60.95685  ?  418 VAL A CG1    1 
ATOM   6462 C CG2    . VAL A 1 418 ? -0.05200  27.76100  28.92000 1.000 67.84672  ?  418 VAL A CG2    1 
ATOM   6463 H H      . VAL A 1 418 ? 3.32600   28.62100  29.62500 1.000 67.89256  ?  418 VAL A H      1 
ATOM   6464 H HA     . VAL A 1 418 ? 1.94400   27.63600  27.54500 1.000 76.28196  ?  418 VAL A HA     1 
ATOM   6465 H HB     . VAL A 1 418 ? 1.34500   28.91200  29.85600 1.000 83.86336  ?  418 VAL A HB     1 
ATOM   6466 H HG11   . VAL A 1 418 ? -0.29400  30.40300  29.18700 1.000 73.26599  ?  418 VAL A HG11   1 
ATOM   6467 H HG12   . VAL A 1 418 ? 1.14000   30.87000  28.68800 1.000 73.26599  ?  418 VAL A HG12   1 
ATOM   6468 H HG13   . VAL A 1 418 ? 0.13000   30.18300  27.67200 1.000 73.26599  ?  418 VAL A HG13   1 
ATOM   6469 H HG21   . VAL A 1 418 ? -0.83500  28.07900  29.39600 1.000 81.53383  ?  418 VAL A HG21   1 
ATOM   6470 H HG22   . VAL A 1 418 ? -0.28100  27.56700  27.99800 1.000 81.53383  ?  418 VAL A HG22   1 
ATOM   6471 H HG23   . VAL A 1 418 ? 0.29400   26.96300  29.35000 1.000 81.53383  ?  418 VAL A HG23   1 
ATOM   6472 N N      . VAL A 1 419 ? 3.44100   30.34400  27.09500 1.000 58.46576  ?  419 VAL A N      1 
ATOM   6473 C CA     . VAL A 1 419 ? 3.82000   31.28800  26.04200 1.000 60.29557  ?  419 VAL A CA     1 
ATOM   6474 C C      . VAL A 1 419 ? 5.31600   31.15500  25.76100 1.000 59.52234  ?  419 VAL A C      1 
ATOM   6475 O O      . VAL A 1 419 ? 5.97100   32.12200  25.36000 1.000 58.40698  ?  419 VAL A O      1 
ATOM   6476 C CB     . VAL A 1 419 ? 3.47500   32.74200  26.42200 1.000 61.39633  ?  419 VAL A CB     1 
ATOM   6477 C CG1    . VAL A 1 419 ? 1.96300   32.91400  26.57800 1.000 72.54222  ?  419 VAL A CG1    1 
ATOM   6478 C CG2    . VAL A 1 419 ? 4.20600   33.15600  27.69700 1.000 61.46060  ?  419 VAL A CG2    1 
ATOM   6479 H H      . VAL A 1 419 ? 3.91100   30.41300  27.81100 1.000 70.27668  ?  419 VAL A H      1 
ATOM   6480 H HA     . VAL A 1 419 ? 3.32600   31.05900  25.24000 1.000 72.47245  ?  419 VAL A HA     1 
ATOM   6481 H HB     . VAL A 1 419 ? 3.76900   33.32900  25.70800 1.000 73.79336  ?  419 VAL A HB     1 
ATOM   6482 H HG11   . VAL A 1 419 ? 1.77100   33.84200  26.78600 1.000 87.16843  ?  419 VAL A HG11   1 
ATOM   6483 H HG12   . VAL A 1 419 ? 1.53000   32.66500  25.74700 1.000 87.16843  ?  419 VAL A HG12   1 
ATOM   6484 H HG13   . VAL A 1 419 ? 1.65300   32.34200  27.29700 1.000 87.16843  ?  419 VAL A HG13   1 
ATOM   6485 H HG21   . VAL A 1 419 ? 3.93300   34.05400  27.94000 1.000 73.87049  ?  419 VAL A HG21   1 
ATOM   6486 H HG22   . VAL A 1 419 ? 3.97700   32.53700  28.40700 1.000 73.87049  ?  419 VAL A HG22   1 
ATOM   6487 H HG23   . VAL A 1 419 ? 5.16200   33.13300  27.53400 1.000 73.87049  ?  419 VAL A HG23   1 
ATOM   6488 N N      . PHE A 1 420 ? 5.86400   29.95800  25.97900 1.000 56.28287  ?  420 PHE A N      1 
ATOM   6489 C CA     . PHE A 1 420 ? 7.30500   29.77400  25.83600 1.000 53.42606  ?  420 PHE A CA     1 
ATOM   6490 C C      . PHE A 1 420 ? 7.76000   30.08400  24.41400 1.000 47.83741  ?  420 PHE A C      1 
ATOM   6491 O O      . PHE A 1 420 ? 8.77400   30.75400  24.21500 1.000 49.40743  ?  420 PHE A O      1 
ATOM   6492 C CB     . PHE A 1 420 ? 7.67800   28.34700  26.23100 1.000 53.37375  ?  420 PHE A CB     1 
ATOM   6493 C CG     . PHE A 1 420 ? 9.15400   28.09900  26.30800 1.000 57.93001  ?  420 PHE A CG     1 
ATOM   6494 C CD1    . PHE A 1 420 ? 9.95800   28.85900  27.14700 1.000 61.09741  ?  420 PHE A CD1    1 
ATOM   6495 C CD2    . PHE A 1 420 ? 9.74100   27.10000  25.54700 1.000 53.41846  ?  420 PHE A CD2    1 
ATOM   6496 C CE1    . PHE A 1 420 ? 11.31600  28.62500  27.22600 1.000 61.81956  ?  420 PHE A CE1    1 
ATOM   6497 C CE2    . PHE A 1 420 ? 11.10300  26.86300  25.61900 1.000 54.66301  ?  420 PHE A CE2    1 
ATOM   6498 C CZ     . PHE A 1 420 ? 11.89200  27.62400  26.46200 1.000 58.53322  ?  420 PHE A CZ     1 
ATOM   6499 H H      . PHE A 1 420 ? 5.43200   29.25100  26.20700 1.000 67.65722  ?  420 PHE A H      1 
ATOM   6500 H HA     . PHE A 1 420 ? 7.76800   30.38300  26.43300 1.000 64.22905  ?  420 PHE A HA     1 
ATOM   6501 H HB2    . PHE A 1 420 ? 7.30200   28.15800  27.10500 1.000 64.16627  ?  420 PHE A HB2    1 
ATOM   6502 H HB3    . PHE A 1 420 ? 7.31100   27.73700  25.57200 1.000 64.16627  ?  420 PHE A HB3    1 
ATOM   6503 H HD1    . PHE A 1 420 ? 9.57700   29.53300  27.66100 1.000 73.43466  ?  420 PHE A HD1    1 
ATOM   6504 H HD2    . PHE A 1 420 ? 9.21300   26.58300  24.98300 1.000 64.21992  ?  420 PHE A HD2    1 
ATOM   6505 H HE1    . PHE A 1 420 ? 11.84400  29.13900  27.79300 1.000 74.30125  ?  420 PHE A HE1    1 
ATOM   6506 H HE2    . PHE A 1 420 ? 11.48700  26.19400  25.10000 1.000 65.71338  ?  420 PHE A HE2    1 
ATOM   6507 H HZ     . PHE A 1 420 ? 12.80600  27.46400  26.51600 1.000 70.35763  ?  420 PHE A HZ     1 
ATOM   6508 N N      . GLY A 1 421 ? 7.01000   29.62100  23.41400 1.000 43.97569  ?  421 GLY A N      1 
ATOM   6509 C CA     . GLY A 1 421 ? 7.41100   29.79400  22.03200 1.000 47.92643  ?  421 GLY A CA     1 
ATOM   6510 C C      . GLY A 1 421 ? 7.56700   31.23900  21.60400 1.000 50.60822  ?  421 GLY A C      1 
ATOM   6511 O O      . GLY A 1 421 ? 8.29800   31.52000  20.64500 1.000 50.49569  ?  421 GLY A O      1 
ATOM   6512 H H      . GLY A 1 421 ? 6.26500   29.20300  23.51500 1.000 52.88859  ?  421 GLY A H      1 
ATOM   6513 H HA2    . GLY A 1 421 ? 8.26200   29.34900  21.89500 1.000 57.62949  ?  421 GLY A HA2    1 
ATOM   6514 H HA3    . GLY A 1 421 ? 6.74400   29.38400  21.45900 1.000 57.62949  ?  421 GLY A HA3    1 
ATOM   6515 N N      . LYS A 1 422 ? 6.90700   32.16500  22.29300 1.000 51.29876  ?  422 LYS A N      1 
ATOM   6516 C CA     . LYS A 1 422 ? 6.97400   33.56800  21.89800 1.000 51.60342  ?  422 LYS A CA     1 
ATOM   6517 C C      . LYS A 1 422 ? 8.40600   34.09100  21.90200 1.000 49.59482  ?  422 LYS A C      1 
ATOM   6518 O O      . LYS A 1 422 ? 8.72700   35.02200  21.15800 1.000 51.11147  ?  422 LYS A O      1 
ATOM   6519 C CB     . LYS A 1 422 ? 6.10200   34.41500  22.82200 1.000 52.41351  ?  422 LYS A CB     1 
ATOM   6520 C CG     . LYS A 1 422 ? 6.04200   35.88800  22.44300 1.000 58.48377  ?  422 LYS A CG     1 
ATOM   6521 C CD     . LYS A 1 422 ? 4.71700   36.52400  22.85000 1.000 74.54413  ?  422 LYS A CD     1 
ATOM   6522 C CE     . LYS A 1 422 ? 4.71300   36.94000  24.31600 1.000 80.67332  ?  422 LYS A CE     1 
ATOM   6523 N NZ     . LYS A 1 422 ? 3.61200   37.91200  24.60700 1.000 85.32528  ?  422 LYS A NZ     1 
ATOM   6524 H H      . LYS A 1 422 ? 6.42000   32.01000  22.98500 1.000 61.67628  ?  422 LYS A H      1 
ATOM   6525 H HA     . LYS A 1 422 ? 6.63000   33.65100  20.99500 1.000 62.04188  ?  422 LYS A HA     1 
ATOM   6526 H HB2    . LYS A 1 422 ? 5.19600   34.06800  22.79800 1.000 63.01399  ?  422 LYS A HB2    1 
ATOM   6527 H HB3    . LYS A 1 422 ? 6.45600   34.35600  23.72300 1.000 63.01399  ?  422 LYS A HB3    1 
ATOM   6528 H HG2    . LYS A 1 422 ? 6.75800   36.36400  22.89300 1.000 70.29830  ?  422 LYS A HG2    1 
ATOM   6529 H HG3    . LYS A 1 422 ? 6.13900   35.97500  21.48200 1.000 70.29830  ?  422 LYS A HG3    1 
ATOM   6530 H HD2    . LYS A 1 422 ? 4.56300   37.31400  22.30900 1.000 89.57072  ?  422 LYS A HD2    1 
ATOM   6531 H HD3    . LYS A 1 422 ? 4.00100   35.88400  22.71400 1.000 89.57072  ?  422 LYS A HD3    1 
ATOM   6532 H HE2    . LYS A 1 422 ? 4.58300   36.15600  24.87200 1.000 96.92576  ?  422 LYS A HE2    1 
ATOM   6533 H HE3    . LYS A 1 422 ? 5.55900   37.36400  24.53200 1.000 96.92576  ?  422 LYS A HE3    1 
ATOM   6534 H HZ1    . LYS A 1 422 ? 3.61900   38.13000  25.47000 1.000 102.50810 ?  422 LYS A HZ1    1 
ATOM   6535 H HZ2    . LYS A 1 422 ? 3.72100   38.65000  24.12200 1.000 102.50810 ?  422 LYS A HZ2    1 
ATOM   6536 H HZ3    . LYS A 1 422 ? 2.82400   37.54800  24.40800 1.000 102.50810 ?  422 LYS A HZ3    1 
ATOM   6537 N N      . LYS A 1 423 ? 9.27400   33.50800  22.72700 1.000 59.63978  ?  423 LYS A N      1 
ATOM   6538 C CA     . LYS A 1 423 ? 10.65800  33.96200  22.78700 1.000 59.33220  ?  423 LYS A CA     1 
ATOM   6539 C C      . LYS A 1 423 ? 11.38000  33.72600  21.46200 1.000 56.45375  ?  423 LYS A C      1 
ATOM   6540 O O      . LYS A 1 423 ? 12.22000  34.54200  21.05000 1.000 58.87738  ?  423 LYS A O      1 
ATOM   6541 C CB     . LYS A 1 423 ? 11.38400  33.24400  23.92700 1.000 68.34138  ?  423 LYS A CB     1 
ATOM   6542 C CG     . LYS A 1 423 ? 12.90300  33.37200  23.89300 1.000 69.54838  ?  423 LYS A CG     1 
ATOM   6543 C CD     . LYS A 1 423 ? 13.52200  32.81900  25.16600 1.000 69.33624  ?  423 LYS A CD     1 
ATOM   6544 C CE     . LYS A 1 423 ? 15.04200  32.85000  25.10200 1.000 94.13835  ?  423 LYS A CE     1 
ATOM   6545 N NZ     . LYS A 1 423 ? 15.66100  32.22900  26.30700 1.000 104.16123 ?  423 LYS A NZ     1 
ATOM   6546 H H      . LYS A 1 423 ? 9.08900   32.85600  23.25600 1.000 71.68551  ?  423 LYS A H      1 
ATOM   6547 H HA     . LYS A 1 423 ? 10.67000  34.91500  22.96500 1.000 71.31641  ?  423 LYS A HA     1 
ATOM   6548 H HB2    . LYS A 1 423 ? 11.07800  33.61500  24.76900 1.000 82.12743  ?  423 LYS A HB2    1 
ATOM   6549 H HB3    . LYS A 1 423 ? 11.16900  32.29900  23.88300 1.000 82.12743  ?  423 LYS A HB3    1 
ATOM   6550 H HG2    . LYS A 1 423 ? 13.25400  32.87300  23.13900 1.000 83.57583  ?  423 LYS A HG2    1 
ATOM   6551 H HG3    . LYS A 1 423 ? 13.14800  34.30800  23.81400 1.000 83.57583  ?  423 LYS A HG3    1 
ATOM   6552 H HD2    . LYS A 1 423 ? 13.23800  33.35600  25.92200 1.000 83.32125  ?  423 LYS A HD2    1 
ATOM   6553 H HD3    . LYS A 1 423 ? 13.24000  31.89900  25.28800 1.000 83.32125  ?  423 LYS A HD3    1 
ATOM   6554 H HE2    . LYS A 1 423 ? 15.33900  32.35700  24.32000 1.000 113.08379 ?  423 LYS A HE2    1 
ATOM   6555 H HE3    . LYS A 1 423 ? 15.34200  33.77100  25.04700 1.000 113.08379 ?  423 LYS A HE3    1 
ATOM   6556 H HZ1    . LYS A 1 423 ? 16.54800  32.24800  26.23700 1.000 125.11125 ?  423 LYS A HZ1    1 
ATOM   6557 H HZ2    . LYS A 1 423 ? 15.41900  32.67600  27.03700 1.000 125.11125 ?  423 LYS A HZ2    1 
ATOM   6558 H HZ3    . LYS A 1 423 ? 15.39600  31.38300  26.38400 1.000 125.11125 ?  423 LYS A HZ3    1 
ATOM   6559 N N      . TYR A 1 424 ? 11.08300  32.61400  20.79900 1.000 54.49407  ?  424 TYR A N      1 
ATOM   6560 C CA     . TYR A 1 424 ? 11.71600  32.23900  19.53800 1.000 54.07831  ?  424 TYR A CA     1 
ATOM   6561 C C      . TYR A 1 424 ? 10.90800  32.63600  18.31200 1.000 53.49458  ?  424 TYR A C      1 
ATOM   6562 O O      . TYR A 1 424 ? 11.49500  32.86200  17.25700 1.000 49.01828  ?  424 TYR A O      1 
ATOM   6563 C CB     . TYR A 1 424 ? 11.92200  30.71300  19.47900 1.000 53.65906  ?  424 TYR A CB     1 
ATOM   6564 C CG     . TYR A 1 424 ? 12.58800  30.12700  20.70200 1.000 48.38683  ?  424 TYR A CG     1 
ATOM   6565 C CD1    . TYR A 1 424 ? 11.82900  29.69600  21.79000 1.000 48.67511  ?  424 TYR A CD1    1 
ATOM   6566 C CD2    . TYR A 1 424 ? 13.96100  29.99900  20.76500 1.000 46.04154  ?  424 TYR A CD2    1 
ATOM   6567 C CE1    . TYR A 1 424 ? 12.43900  29.16200  22.90800 1.000 53.87555  ?  424 TYR A CE1    1 
ATOM   6568 C CE2    . TYR A 1 424 ? 14.57900  29.46000  21.87700 1.000 49.29164  ?  424 TYR A CE2    1 
ATOM   6569 C CZ     . TYR A 1 424 ? 13.82300  29.05000  22.94400 1.000 53.79926  ?  424 TYR A CZ     1 
ATOM   6570 O OH     . TYR A 1 424 ? 14.44900  28.52600  24.04600 1.000 52.63366  ?  424 TYR A OH     1 
ATOM   6571 H H      . TYR A 1 424 ? 10.49800  32.04200  21.06500 1.000 65.51065  ?  424 TYR A H      1 
ATOM   6572 H HA     . TYR A 1 424 ? 12.58100  32.67700  19.49700 1.000 65.01174  ?  424 TYR A HA     1 
ATOM   6573 H HB2    . TYR A 1 424 ? 11.05500  30.28700  19.38500 1.000 64.50865  ?  424 TYR A HB2    1 
ATOM   6574 H HB3    . TYR A 1 424 ? 12.47900  30.50500  18.71300 1.000 64.50865  ?  424 TYR A HB3    1 
ATOM   6575 H HD1    . TYR A 1 424 ? 10.90300  29.76900  21.76200 1.000 58.52790  ?  424 TYR A HD1    1 
ATOM   6576 H HD2    . TYR A 1 424 ? 14.47900  30.27900  20.04500 1.000 55.36762  ?  424 TYR A HD2    1 
ATOM   6577 H HE1    . TYR A 1 424 ? 11.92700  28.87900  23.63100 1.000 64.76843  ?  424 TYR A HE1    1 
ATOM   6578 H HE2    . TYR A 1 424 ? 15.50500  29.37600  21.90100 1.000 59.26774  ?  424 TYR A HE2    1 
ATOM   6579 H HH     . TYR A 1 424 ? 13.87900  28.31900  24.62800 1.000 63.27816  ?  424 TYR A HH     1 
ATOM   6580 N N      . ASP A 1 425 ? 9.58300   32.70500  18.43900 1.000 46.07640  ?  425 ASP A N      1 
ATOM   6581 C CA     . ASP A 1 425 ? 8.67200   32.79100  17.30200 1.000 49.66121  ?  425 ASP A CA     1 
ATOM   6582 C C      . ASP A 1 425 ? 7.58500   33.81400  17.60400 1.000 45.13116  ?  425 ASP A C      1 
ATOM   6583 O O      . ASP A 1 425 ? 6.41000   33.47100  17.75800 1.000 45.19980  ?  425 ASP A O      1 
ATOM   6584 C CB     . ASP A 1 425 ? 8.07200   31.40500  17.01000 1.000 49.03029  ?  425 ASP A CB     1 
ATOM   6585 C CG     . ASP A 1 425 ? 7.28100   31.36500  15.71200 1.000 49.76932  ?  425 ASP A CG     1 
ATOM   6586 O OD1    . ASP A 1 425 ? 7.37600   32.31400  14.90900 1.000 47.46859  ?  425 ASP A OD1    1 
ATOM   6587 O OD2    . ASP A 1 425 ? 6.54700   30.36700  15.51000 1.000 51.40629  -1 425 ASP A OD2    1 
ATOM   6588 H H      . ASP A 1 425 ? 9.17700   32.70200  19.19800 1.000 55.40945  ?  425 ASP A H      1 
ATOM   6589 H HA     . ASP A 1 425 ? 9.15500   33.10100  16.52000 1.000 59.71123  ?  425 ASP A HA     1 
ATOM   6590 H HB2    . ASP A 1 425 ? 8.79200   30.75700  16.94300 1.000 58.95412  ?  425 ASP A HB2    1 
ATOM   6591 H HB3    . ASP A 1 425 ? 7.47400   31.16100  17.73400 1.000 58.95412  ?  425 ASP A HB3    1 
ATOM   6592 N N      . PRO A 1 426 ? 7.95100   35.09900  17.68800 1.000 45.10705  ?  426 PRO A N      1 
ATOM   6593 C CA     . PRO A 1 426 ? 6.94700   36.11600  18.05500 1.000 46.64916  ?  426 PRO A CA     1 
ATOM   6594 C C      . PRO A 1 426 ? 5.79800   36.21000  17.07300 1.000 45.75791  ?  426 PRO A C      1 
ATOM   6595 O O      . PRO A 1 426 ? 4.70600   36.62900  17.46200 1.000 50.21650  ?  426 PRO A O      1 
ATOM   6596 C CB     . PRO A 1 426 ? 7.76000   37.43400  18.10000 1.000 48.42602  ?  426 PRO A CB     1 
ATOM   6597 C CG     . PRO A 1 426 ? 9.01600   37.15200  17.33800 1.000 50.69227  ?  426 PRO A CG     1 
ATOM   6598 C CD     . PRO A 1 426 ? 9.29900   35.67500  17.50700 1.000 45.76267  ?  426 PRO A CD     1 
ATOM   6599 H HA     . PRO A 1 426 ? 6.60200   35.92300  18.94100 1.000 56.09676  ?  426 PRO A HA     1 
ATOM   6600 H HB2    . PRO A 1 426 ? 7.25400   38.14700  17.68100 1.000 58.22900  ?  426 PRO A HB2    1 
ATOM   6601 H HB3    . PRO A 1 426 ? 7.95900   37.66500  19.02100 1.000 58.22900  ?  426 PRO A HB3    1 
ATOM   6602 H HG2    . PRO A 1 426 ? 8.88400   37.36900  16.40200 1.000 60.94850  ?  426 PRO A HG2    1 
ATOM   6603 H HG3    . PRO A 1 426 ? 9.74300   37.68300  17.70200 1.000 60.94850  ?  426 PRO A HG3    1 
ATOM   6604 H HD2    . PRO A 1 426 ? 9.72800   35.31200  16.71700 1.000 55.03297  ?  426 PRO A HD2    1 
ATOM   6605 H HD3    . PRO A 1 426 ? 9.85200   35.51600  18.28800 1.000 55.03297  ?  426 PRO A HD3    1 
ATOM   6606 N N      . GLU A 1 427 ? 6.01100   35.83900  15.80500 1.000 50.95908  ?  427 GLU A N      1 
ATOM   6607 C CA     . GLU A 1 427 ? 4.93500   35.85100  14.82300 1.000 50.83960  ?  427 GLU A CA     1 
ATOM   6608 C C      . GLU A 1 427 ? 4.04600   34.61900  14.89800 1.000 54.10155  ?  427 GLU A C      1 
ATOM   6609 O O      . GLU A 1 427 ? 2.97600   34.61100  14.27300 1.000 52.49608  ?  427 GLU A O      1 
ATOM   6610 C CB     . GLU A 1 427 ? 5.51600   35.95900  13.40800 1.000 61.25528  ?  427 GLU A CB     1 
ATOM   6611 C CG     . GLU A 1 427 ? 5.65600   37.38800  12.92400 1.000 72.56358  ?  427 GLU A CG     1 
ATOM   6612 C CD     . GLU A 1 427 ? 4.36000   37.93200  12.34200 1.000 83.04988  ?  427 GLU A CD     1 
ATOM   6613 O OE1    . GLU A 1 427 ? 3.53300   37.12500  11.84800 1.000 92.41262  ?  427 GLU A OE1    1 
ATOM   6614 O OE2    . GLU A 1 427 ? 4.14800   39.15900  12.38800 1.000 86.29537  -1 427 GLU A OE2    1 
ATOM   6615 H H      . GLU A 1 427 ? 6.76900   35.57800  15.49500 1.000 61.26867  ?  427 GLU A H      1 
ATOM   6616 H HA     . GLU A 1 427 ? 4.38300   36.63100  14.98600 1.000 61.12528  ?  427 GLU A HA     1 
ATOM   6617 H HB2    . GLU A 1 427 ? 6.39700   35.55400  13.40000 1.000 73.62411  ?  427 GLU A HB2    1 
ATOM   6618 H HB3    . GLU A 1 427 ? 4.93000   35.49200  12.79300 1.000 73.62411  ?  427 GLU A HB3    1 
ATOM   6619 H HG2    . GLU A 1 427 ? 5.91200   37.95300  13.66900 1.000 87.19406  ?  427 GLU A HG2    1 
ATOM   6620 H HG3    . GLU A 1 427 ? 6.33500   37.42400  12.23200 1.000 87.19406  ?  427 GLU A HG3    1 
ATOM   6621 N N      . GLY A 1 428 ? 4.43700   33.59700  15.65700 1.000 46.47262  ?  428 GLY A N      1 
ATOM   6622 C CA     . GLY A 1 428 ? 3.63400   32.39400  15.75300 1.000 42.22748  ?  428 GLY A CA     1 
ATOM   6623 C C      . GLY A 1 428 ? 3.56800   31.57500  14.48400 1.000 48.37134  ?  428 GLY A C      1 
ATOM   6624 O O      . GLY A 1 428 ? 2.51800   31.00500  14.16900 1.000 43.80625  ?  428 GLY A O      1 
ATOM   6625 H H      . GLY A 1 428 ? 5.16000   33.58000  16.12100 1.000 55.88491  ?  428 GLY A H      1 
ATOM   6626 H HA2    . GLY A 1 428 ? 4.00100   31.82900  16.45100 1.000 50.79075  ?  428 GLY A HA2    1 
ATOM   6627 H HA3    . GLY A 1 428 ? 2.72700   32.64200  15.99300 1.000 50.79075  ?  428 GLY A HA3    1 
ATOM   6628 N N      . ARG A 1 429 ? 4.68800   31.47500  13.74900 1.000 49.20146  ?  429 ARG A N      1 
ATOM   6629 C CA     A ARG A 1 429 ? 4.69000   30.64800  12.54600 0.580 51.13057  ?  429 ARG A CA     1 
ATOM   6630 C CA     B ARG A 1 429 ? 4.70000   30.64600  12.54800 0.420 51.29141  ?  429 ARG A CA     1 
ATOM   6631 C C      . ARG A 1 429 ? 4.39300   29.19300  12.88800 1.000 49.65669  ?  429 ARG A C      1 
ATOM   6632 O O      . ARG A 1 429 ? 3.62800   28.52800  12.18300 1.000 45.61396  ?  429 ARG A O      1 
ATOM   6633 C CB     A ARG A 1 429 ? 6.03000   30.77600  11.82700 0.580 55.00520  ?  429 ARG A CB     1 
ATOM   6634 C CB     B ARG A 1 429 ? 6.05800   30.74500  11.85400 0.420 55.03211  ?  429 ARG A CB     1 
ATOM   6635 C CG     A ARG A 1 429 ? 6.36400   32.19400  11.39700 0.580 60.20470  ?  429 ARG A CG     1 
ATOM   6636 C CG     B ARG A 1 429 ? 6.36700   32.09500  11.23700 0.420 60.36180  ?  429 ARG A CG     1 
ATOM   6637 C CD     A ARG A 1 429 ? 7.30500   32.21300  10.19300 0.580 67.46391  ?  429 ARG A CD     1 
ATOM   6638 C CD     B ARG A 1 429 ? 7.76000   32.09600  10.59600 0.420 66.93132  ?  429 ARG A CD     1 
ATOM   6639 N NE     A ARG A 1 429 ? 7.26800   33.49100  9.48500  0.580 73.79457  ?  429 ARG A NE     1 
ATOM   6640 N NE     B ARG A 1 429 ? 8.75700   31.46600  11.45600 0.420 67.84946  ?  429 ARG A NE     1 
ATOM   6641 C CZ     A ARG A 1 429 ? 6.22700   33.93400  8.79100  0.580 75.32269  ?  429 ARG A CZ     1 
ATOM   6642 C CZ     B ARG A 1 429 ? 9.51000   32.11200  12.34000 0.420 69.60336  ?  429 ARG A CZ     1 
ATOM   6643 N NH1    A ARG A 1 429 ? 5.11000   33.22900  8.69100  0.580 81.70716  ?  429 ARG A NH1    1 
ATOM   6644 N NH1    B ARG A 1 429 ? 9.43400   33.42600  12.48500 0.420 69.56663  ?  429 ARG A NH1    1 
ATOM   6645 N NH2    A ARG A 1 429 ? 6.30700   35.10900  8.18100  0.580 72.07564  ?  429 ARG A NH2    1 
ATOM   6646 N NH2    B ARG A 1 429 ? 10.35600  31.42200  13.09600 0.420 63.13328  ?  429 ARG A NH2    1 
ATOM   6647 H H      A ARG A 1 429 ? 5.43400   31.86500  13.92400 0.580 59.15952  ?  429 ARG A H      1 
ATOM   6648 H H      B ARG A 1 429 ? 5.43200   31.86800  13.92400 0.420 59.15952  ?  429 ARG A H      1 
ATOM   6649 H HA     A ARG A 1 429 ? 4.00000   30.96200  11.94100 0.580 61.47445  ?  429 ARG A HA     1 
ATOM   6650 H HA     B ARG A 1 429 ? 4.02200   30.97200  11.93700 0.420 61.66747  ?  429 ARG A HA     1 
ATOM   6651 H HB2    A ARG A 1 429 ? 6.73400   30.47500  12.42300 0.580 66.12401  ?  429 ARG A HB2    1 
ATOM   6652 H HB2    B ARG A 1 429 ? 6.75100   30.55700  12.50600 0.420 66.15630  ?  429 ARG A HB2    1 
ATOM   6653 H HB3    A ARG A 1 429 ? 6.01100   30.22300  11.03100 0.580 66.12401  ?  429 ARG A HB3    1 
ATOM   6654 H HB3    B ARG A 1 429 ? 6.08600   30.08700  11.14100 0.420 66.15630  ?  429 ARG A HB3    1 
ATOM   6655 H HG2    A ARG A 1 429 ? 5.54700   32.65500  11.15100 0.580 72.36340  ?  429 ARG A HG2    1 
ATOM   6656 H HG2    B ARG A 1 429 ? 5.71200   32.29500  10.55100 0.420 72.55193  ?  429 ARG A HG2    1 
ATOM   6657 H HG3    A ARG A 1 429 ? 6.79900   32.65800  12.13000 0.580 72.36340  ?  429 ARG A HG3    1 
ATOM   6658 H HG3    B ARG A 1 429 ? 6.34600   32.77800  11.92600 0.420 72.55193  ?  429 ARG A HG3    1 
ATOM   6659 H HD2    A ARG A 1 429 ? 8.21400   32.06200  10.49600 0.580 81.07446  ?  429 ARG A HD2    1 
ATOM   6660 H HD2    B ARG A 1 429 ? 7.72600   31.60500  9.76000  0.420 80.43536  ?  429 ARG A HD2    1 
ATOM   6661 H HD3    A ARG A 1 429 ? 7.04300   31.51500  9.57200  0.580 81.07446  ?  429 ARG A HD3    1 
ATOM   6662 H HD3    B ARG A 1 429 ? 8.03500   33.01200  10.43300 0.420 80.43536  ?  429 ARG A HD3    1 
ATOM   6663 H HE     A ARG A 1 429 ? 7.96700   33.98900  9.52100  0.580 88.67125  ?  429 ARG A HE     1 
ATOM   6664 H HE     B ARG A 1 429 ? 8.86500   30.61500  11.38500 0.420 81.53713  ?  429 ARG A HE     1 
ATOM   6665 H HH11   A ARG A 1 429 ? 5.04700   32.46500  9.08100  0.580 98.16636  ?  429 ARG A HH11   1 
ATOM   6666 H HH11   B ARG A 1 429 ? 8.88900   33.88200  12.00100 0.420 83.59772  ?  429 ARG A HH11   1 
ATOM   6667 H HH12   A ARG A 1 429 ? 4.44800   33.53500  8.23600  0.580 98.16636  ?  429 ARG A HH12   1 
ATOM   6668 H HH12   B ARG A 1 429 ? 9.93100   33.82400  13.06300 0.420 83.59772  ?  429 ARG A HH12   1 
ATOM   6669 H HH21   A ARG A 1 429 ? 7.02800   35.57500  8.23700  0.580 86.60854  ?  429 ARG A HH21   1 
ATOM   6670 H HH21   B ARG A 1 429 ? 10.41100  30.56800  13.01000 0.420 75.87771  ?  429 ARG A HH21   1 
ATOM   6671 H HH22   A ARG A 1 429 ? 5.63800   35.40500  7.72900  0.580 86.60854  ?  429 ARG A HH22   1 
ATOM   6672 H HH22   B ARG A 1 429 ? 10.84800  31.82900  13.67200 0.420 75.87771  ?  429 ARG A HH22   1 
ATOM   6673 N N      . PHE A 1 430 ? 4.98500   28.68700  13.97100 1.000 50.51196  ?  430 PHE A N      1 
ATOM   6674 C CA     . PHE A 1 430 ? 4.76400   27.30600  14.38500 1.000 44.95874  ?  430 PHE A CA     1 
ATOM   6675 C C      . PHE A 1 430 ? 3.29800   27.05800  14.68100 1.000 44.07550  ?  430 PHE A C      1 
ATOM   6676 O O      . PHE A 1 430 ? 2.74600   26.02900  14.27400 1.000 46.00437  ?  430 PHE A O      1 
ATOM   6677 C CB     . PHE A 1 430 ? 5.62900   26.99800  15.60900 1.000 43.96186  ?  430 PHE A CB     1 
ATOM   6678 C CG     . PHE A 1 430 ? 5.52500   25.57100  16.09300 1.000 47.94967  ?  430 PHE A CG     1 
ATOM   6679 C CD1    . PHE A 1 430 ? 6.38300   24.59400  15.60300 1.000 50.52961  ?  430 PHE A CD1    1 
ATOM   6680 C CD2    . PHE A 1 430 ? 4.59900   25.21500  17.05000 1.000 49.56754  ?  430 PHE A CD2    1 
ATOM   6681 C CE1    . PHE A 1 430 ? 6.29600   23.28700  16.05600 1.000 47.37437  ?  430 PHE A CE1    1 
ATOM   6682 C CE2    . PHE A 1 430 ? 4.50500   23.91500  17.50600 1.000 46.25127  ?  430 PHE A CE2    1 
ATOM   6683 C CZ     . PHE A 1 430 ? 5.36600   22.94400  17.00300 1.000 42.49366  ?  430 PHE A CZ     1 
ATOM   6684 H H      . PHE A 1 430 ? 5.52000   29.12500  14.48300 1.000 60.73212  ?  430 PHE A H      1 
ATOM   6685 H HA     . PHE A 1 430 ? 5.02700   26.70500  13.67100 1.000 54.06826  ?  430 PHE A HA     1 
ATOM   6686 H HB2    . PHE A 1 430 ? 6.55800   27.16600  15.38200 1.000 52.87200  ?  430 PHE A HB2    1 
ATOM   6687 H HB3    . PHE A 1 430 ? 5.35600   27.57800  16.33700 1.000 52.87200  ?  430 PHE A HB3    1 
ATOM   6688 H HD1    . PHE A 1 430 ? 7.02100   24.82000  14.96500 1.000 60.75330  ?  430 PHE A HD1    1 
ATOM   6689 H HD2    . PHE A 1 430 ? 4.02700   25.86200  17.39400 1.000 59.59882  ?  430 PHE A HD2    1 
ATOM   6690 H HE1    . PHE A 1 430 ? 6.87200   22.64000  15.71600 1.000 56.96702  ?  430 PHE A HE1    1 
ATOM   6691 H HE2    . PHE A 1 430 ? 3.87000   23.68900  18.14700 1.000 55.61929  ?  430 PHE A HE2    1 
ATOM   6692 H HZ     . PHE A 1 430 ? 5.31000   22.06700  17.30700 1.000 51.11016  ?  430 PHE A HZ     1 
ATOM   6693 N N      . ILE A 1 431 ? 2.64900   27.99300  15.38400 1.000 45.52867  ?  431 ILE A N      1 
ATOM   6694 C CA     . ILE A 1 431 ? 1.24500   27.84900  15.72900 1.000 40.86258  ?  431 ILE A CA     1 
ATOM   6695 C C      . ILE A 1 431 ? 0.37400   27.86200  14.47500 1.000 42.03298  ?  431 ILE A C      1 
ATOM   6696 O O      . ILE A 1 431 ? -0.53400  27.04000  14.32000 1.000 48.76267  ?  431 ILE A O      1 
ATOM   6697 C CB     . ILE A 1 431 ? 0.82600   28.95800  16.71600 1.000 44.32185  ?  431 ILE A CB     1 
ATOM   6698 C CG1    . ILE A 1 431 ? 1.44700   28.70500  18.09000 1.000 46.50352  ?  431 ILE A CG1    1 
ATOM   6699 C CG2    . ILE A 1 431 ? -0.69100  29.06800  16.80100 1.000 44.77102  ?  431 ILE A CG2    1 
ATOM   6700 C CD1    . ILE A 1 431 ? 1.48700   29.93500  18.97500 1.000 51.61654  ?  431 ILE A CD1    1 
ATOM   6701 H H      . ILE A 1 431 ? 3.00600   28.72100  15.67200 1.000 54.75218  ?  431 ILE A H      1 
ATOM   6702 H HA     . ILE A 1 431 ? 1.12300   26.99000  16.16200 1.000 49.15286  ?  431 ILE A HA     1 
ATOM   6703 H HB     . ILE A 1 431 ? 1.16000   29.80600  16.38500 1.000 53.30399  ?  431 ILE A HB     1 
ATOM   6704 H HG12   . ILE A 1 431 ? 0.92700   28.02700  18.54700 1.000 55.92200  ?  431 ILE A HG12   1 
ATOM   6705 H HG13   . ILE A 1 431 ? 2.35900   28.39800  17.96800 1.000 55.92200  ?  431 ILE A HG13   1 
ATOM   6706 H HG21   . ILE A 1 431 ? -0.92900  29.53600  17.61700 1.000 53.84300  ?  431 ILE A HG21   1 
ATOM   6707 H HG22   . ILE A 1 431 ? -1.01600  29.56000  16.03100 1.000 53.84300  ?  431 ILE A HG22   1 
ATOM   6708 H HG23   . ILE A 1 431 ? -1.07200  28.17600  16.80900 1.000 53.84300  ?  431 ILE A HG23   1 
ATOM   6709 H HD11   . ILE A 1 431 ? 1.89200   29.70000  19.82500 1.000 62.05761  ?  431 ILE A HD11   1 
ATOM   6710 H HD12   . ILE A 1 431 ? 2.01200   30.62300  18.53800 1.000 62.05761  ?  431 ILE A HD12   1 
ATOM   6711 H HD13   . ILE A 1 431 ? 0.58100   30.25100  19.11800 1.000 62.05761  ?  431 ILE A HD13   1 
ATOM   6712 N N      . ARG A 1 432 ? 0.64200   28.78700  13.55800 1.000 45.72102  ?  432 ARG A N      1 
ATOM   6713 C CA     . ARG A 1 432 ? -0.15600  28.87600  12.34800 1.000 46.66477  ?  432 ARG A CA     1 
ATOM   6714 C C      . ARG A 1 432 ? -0.02900  27.61700  11.49900 1.000 49.94075  ?  432 ARG A C      1 
ATOM   6715 O O      . ARG A 1 432 ? -0.98300  27.23800  10.81100 1.000 46.29422  ?  432 ARG A O      1 
ATOM   6716 C CB     . ARG A 1 432 ? 0.25200   30.10600  11.53900 1.000 46.80257  ?  432 ARG A CB     1 
ATOM   6717 C CG     . ARG A 1 432 ? 0.02900   31.42100  12.26800 1.000 45.40613  ?  432 ARG A CG     1 
ATOM   6718 C CD     . ARG A 1 432 ? 0.67800   32.57600  11.51500 1.000 51.79034  ?  432 ARG A CD     1 
ATOM   6719 N NE     . ARG A 1 432 ? 0.92200   33.73100  12.37300 1.000 51.92849  ?  432 ARG A NE     1 
ATOM   6720 C CZ     . ARG A 1 432 ? 0.01400   34.66200  12.65800 1.000 55.30965  ?  432 ARG A CZ     1 
ATOM   6721 N NH1    . ARG A 1 432 ? -1.21800  34.60300  12.17500 1.000 54.29425  ?  432 ARG A NH1    1 
ATOM   6722 N NH2    . ARG A 1 432 ? 0.35500   35.67700  13.44900 1.000 53.35019  ?  432 ARG A NH2    1 
ATOM   6723 H H      . ARG A 1 432 ? 1.27400   29.36700  13.61400 1.000 54.98299  ?  432 ARG A H      1 
ATOM   6724 H HA     . ARG A 1 432 ? -1.08900  28.97700  12.59600 1.000 56.11550  ?  432 ARG A HA     1 
ATOM   6725 H HB2    . ARG A 1 432 ? 1.19600   30.04100  11.32800 1.000 56.28086  ?  432 ARG A HB2    1 
ATOM   6726 H HB3    . ARG A 1 432 ? -0.27000  30.12900  10.72200 1.000 56.28086  ?  432 ARG A HB3    1 
ATOM   6727 H HG2    . ARG A 1 432 ? -0.92300  31.59500  12.33700 1.000 54.60513  ?  432 ARG A HG2    1 
ATOM   6728 H HG3    . ARG A 1 432 ? 0.42200   31.37100  13.15300 1.000 54.60513  ?  432 ARG A HG3    1 
ATOM   6729 H HD2    . ARG A 1 432 ? 1.52900   32.28300  11.15500 1.000 62.26618  ?  432 ARG A HD2    1 
ATOM   6730 H HD3    . ARG A 1 432 ? 0.09100   32.85500  10.79400 1.000 62.26618  ?  432 ARG A HD3    1 
ATOM   6731 H HE     . ARG A 1 432 ? 1.70500   33.81500  12.71700 1.000 62.43195  ?  432 ARG A HE     1 
ATOM   6732 H HH11   . ARG A 1 432 ? -1.44800  33.95200  11.66300 1.000 65.27087  ?  432 ARG A HH11   1 
ATOM   6733 H HH12   . ARG A 1 432 ? -1.78700  35.21700  12.37400 1.000 65.27087  ?  432 ARG A HH12   1 
ATOM   6734 H HH21   . ARG A 1 432 ? 1.15200   35.72400  13.76800 1.000 64.13800  ?  432 ARG A HH21   1 
ATOM   6735 H HH22   . ARG A 1 432 ? -0.22200  36.28500  13.64100 1.000 64.13800  ?  432 ARG A HH22   1 
ATOM   6736 N N      . LYS A 1 433 ? 1.13000   26.95500  11.54100 1.000 46.49364  ?  433 LYS A N      1 
ATOM   6737 C CA     . LYS A 1 433 ? 1.31900   25.73900  10.75700 1.000 44.23590  ?  433 LYS A CA     1 
ATOM   6738 C C      . LYS A 1 433 ? 0.43100   24.60800  11.27800 1.000 43.74984  ?  433 LYS A C      1 
ATOM   6739 O O      . LYS A 1 433 ? -0.27000  23.95000  10.50500 1.000 52.72420  ?  433 LYS A O      1 
ATOM   6740 C CB     . LYS A 1 433 ? 2.79300   25.32300  10.77200 1.000 49.99811  ?  433 LYS A CB     1 
ATOM   6741 C CG     . LYS A 1 433 ? 3.05200   23.85000  10.43300 1.000 49.49748  ?  433 LYS A CG     1 
ATOM   6742 C CD     . LYS A 1 433 ? 2.65000   23.52900  9.00600  1.000 56.16607  ?  433 LYS A CD     1 
ATOM   6743 C CE     . LYS A 1 433 ? 3.12000   22.12600  8.60200  1.000 67.63304  ?  433 LYS A CE     1 
ATOM   6744 N NZ     . LYS A 1 433 ? 1.97600   21.24300  8.20300  1.000 71.49091  ?  433 LYS A NZ     1 
ATOM   6745 H H      . LYS A 1 433 ? 1.81200   27.18700  12.01000 1.000 55.91013  ?  433 LYS A H      1 
ATOM   6746 H HA     . LYS A 1 433 ? 1.07100   25.91900  9.83700  1.000 53.20084  ?  433 LYS A HA     1 
ATOM   6747 H HB2    . LYS A 1 433 ? 3.27100   25.86000  10.12100 1.000 60.11551  ?  433 LYS A HB2    1 
ATOM   6748 H HB3    . LYS A 1 433 ? 3.14900   25.48500  11.66000 1.000 60.11551  ?  433 LYS A HB3    1 
ATOM   6749 H HG2    . LYS A 1 433 ? 3.99800   23.65900  10.53400 1.000 59.51475  ?  433 LYS A HG2    1 
ATOM   6750 H HG3    . LYS A 1 433 ? 2.53400   23.28700  11.03000 1.000 59.51475  ?  433 LYS A HG3    1 
ATOM   6751 H HD2    . LYS A 1 433 ? 1.68300   23.56200  8.92700  1.000 67.51706  ?  433 LYS A HD2    1 
ATOM   6752 H HD3    . LYS A 1 433 ? 3.05400   24.17200  8.40400  1.000 67.51706  ?  433 LYS A HD3    1 
ATOM   6753 H HE2    . LYS A 1 433 ? 3.72500   22.19700  7.84800  1.000 81.27742  ?  433 LYS A HE2    1 
ATOM   6754 H HE3    . LYS A 1 433 ? 3.57300   21.71300  9.35400  1.000 81.27742  ?  433 LYS A HE3    1 
ATOM   6755 H HZ1    . LYS A 1 433 ? 2.27700   20.43600  7.98100  1.000 85.90686  ?  433 LYS A HZ1    1 
ATOM   6756 H HZ2    . LYS A 1 433 ? 1.40400   21.16100  8.88000  1.000 85.90686  ?  433 LYS A HZ2    1 
ATOM   6757 H HZ3    . LYS A 1 433 ? 1.55000   21.59400  7.50500  1.000 85.90686  ?  433 LYS A HZ3    1 
ATOM   6758 N N      . PHE A 1 434 ? 0.43500   24.38000  12.59300 1.000 48.96787  ?  434 PHE A N      1 
ATOM   6759 C CA     . PHE A 1 434 ? -0.26700  23.23600  13.16000 1.000 50.51262  ?  434 PHE A CA     1 
ATOM   6760 C C      . PHE A 1 434 ? -1.67200  23.55500  13.65000 1.000 52.63128  ?  434 PHE A C      1 
ATOM   6761 O O      . PHE A 1 434 ? -2.45500  22.61600  13.86100 1.000 46.87788  ?  434 PHE A O      1 
ATOM   6762 C CB     . PHE A 1 434 ? 0.55000   22.63500  14.31200 1.000 51.25229  ?  434 PHE A CB     1 
ATOM   6763 C CG     . PHE A 1 434 ? 1.77800   21.89900  13.85500 1.000 48.89219  ?  434 PHE A CG     1 
ATOM   6764 C CD1    . PHE A 1 434 ? 1.66600   20.66100  13.24000 1.000 52.03994  ?  434 PHE A CD1    1 
ATOM   6765 C CD2    . PHE A 1 434 ? 3.03500   22.45100  14.01700 1.000 47.96350  ?  434 PHE A CD2    1 
ATOM   6766 C CE1    . PHE A 1 434 ? 2.80000   19.98400  12.80600 1.000 53.58846  ?  434 PHE A CE1    1 
ATOM   6767 C CE2    . PHE A 1 434 ? 4.16500   21.79200  13.57800 1.000 51.80467  ?  434 PHE A CE2    1 
ATOM   6768 C CZ     . PHE A 1 434 ? 4.04600   20.54800  12.96700 1.000 49.48121  ?  434 PHE A CZ     1 
ATOM   6769 H H      . PHE A 1 434 ? 0.83700   24.87300  13.17200 1.000 58.87921  ?  434 PHE A H      1 
ATOM   6770 H HA     . PHE A 1 434 ? -0.35600  22.55800  12.47200 1.000 60.73292  ?  434 PHE A HA     1 
ATOM   6771 H HB2    . PHE A 1 434 ? 0.83500   23.35100  14.90000 1.000 61.62051  ?  434 PHE A HB2    1 
ATOM   6772 H HB3    . PHE A 1 434 ? -0.00800  22.00800  14.79800 1.000 61.62051  ?  434 PHE A HB3    1 
ATOM   6773 H HD1    . PHE A 1 434 ? 0.82600   20.28000  13.11900 1.000 62.56570  ?  434 PHE A HD1    1 
ATOM   6774 H HD2    . PHE A 1 434 ? 3.12000   23.28100  14.42800 1.000 57.67397  ?  434 PHE A HD2    1 
ATOM   6775 H HE1    . PHE A 1 434 ? 2.71700   19.14900  12.40500 1.000 64.42392  ?  434 PHE A HE1    1 
ATOM   6776 H HE2    . PHE A 1 434 ? 5.00400   22.17800  13.69000 1.000 62.28338  ?  434 PHE A HE2    1 
ATOM   6777 H HZ     . PHE A 1 434 ? 4.80400   20.09900  12.67000 1.000 59.49523  ?  434 PHE A HZ     1 
ATOM   6778 N N      . LEU A 1 435 ? -2.01500  24.83700  13.82300 1.000 48.60542  ?  435 LEU A N      1 
ATOM   6779 C CA     . LEU A 1 435 ? -3.36900  25.25600  14.18900 1.000 50.34544  ?  435 LEU A CA     1 
ATOM   6780 C C      . LEU A 1 435 ? -3.82900  26.27700  13.14900 1.000 52.61745  ?  435 LEU A C      1 
ATOM   6781 O O      . LEU A 1 435 ? -3.86600  27.48700  13.42200 1.000 51.28519  ?  435 LEU A O      1 
ATOM   6782 C CB     . LEU A 1 435 ? -3.42400  25.83700  15.59900 1.000 50.13760  ?  435 LEU A CB     1 
ATOM   6783 C CG     . LEU A 1 435 ? -2.96900  24.95600  16.75200 1.000 49.85757  ?  435 LEU A CG     1 
ATOM   6784 C CD1    . LEU A 1 435 ? -2.80300  25.78600  18.01500 1.000 46.33974  ?  435 LEU A CD1    1 
ATOM   6785 C CD2    . LEU A 1 435 ? -3.93200  23.80800  16.99700 1.000 53.14452  ?  435 LEU A CD2    1 
ATOM   6786 H H      . LEU A 1 435 ? -1.46700  25.49300  13.73100 1.000 58.44428  ?  435 LEU A H      1 
ATOM   6787 H HA     . LEU A 1 435 ? -3.96200  24.48900  14.16700 1.000 60.53230  ?  435 LEU A HA     1 
ATOM   6788 H HB2    . LEU A 1 435 ? -2.86100  26.62800  15.61400 1.000 60.28289  ?  435 LEU A HB2    1 
ATOM   6789 H HB3    . LEU A 1 435 ? -4.34400  26.08200  15.78100 1.000 60.28289  ?  435 LEU A HB3    1 
ATOM   6790 H HG     . LEU A 1 435 ? -2.11200  24.56700  16.51800 1.000 59.94685  ?  435 LEU A HG     1 
ATOM   6791 H HD11   . LEU A 1 435 ? -2.52300  25.20600  18.73900 1.000 55.72546  ?  435 LEU A HD11   1 
ATOM   6792 H HD12   . LEU A 1 435 ? -2.13200  26.46800  17.85800 1.000 55.72546  ?  435 LEU A HD12   1 
ATOM   6793 H HD13   . LEU A 1 435 ? -3.65200  26.20200  18.23300 1.000 55.72546  ?  435 LEU A HD13   1 
ATOM   6794 H HD21   . LEU A 1 435 ? -3.62300  23.29400  17.76000 1.000 63.89119  ?  435 LEU A HD21   1 
ATOM   6795 H HD22   . LEU A 1 435 ? -4.81400  24.16800  17.17600 1.000 63.89119  ?  435 LEU A HD22   1 
ATOM   6796 H HD23   . LEU A 1 435 ? -3.95800  23.24400  16.20800 1.000 63.89119  ?  435 LEU A HD23   1 
ATOM   6797 N N      . PRO A 1 436 ? -4.18800  25.81900  11.94700 1.000 49.53534  ?  436 PRO A N      1 
ATOM   6798 C CA     . PRO A 1 436 ? -4.53400  26.76600  10.87300 1.000 49.63737  ?  436 PRO A CA     1 
ATOM   6799 C C      . PRO A 1 436 ? -5.74300  27.64200  11.18300 1.000 50.23759  ?  436 PRO A C      1 
ATOM   6800 O O      . PRO A 1 436 ? -5.93500  28.65600  10.50200 1.000 52.74617  ?  436 PRO A O      1 
ATOM   6801 C CB     . PRO A 1 436 ? -4.80400  25.86200  9.65600  1.000 54.28161  ?  436 PRO A CB     1 
ATOM   6802 C CG     . PRO A 1 436 ? -4.75800  24.45600  10.15100 1.000 58.70448  ?  436 PRO A CG     1 
ATOM   6803 C CD     . PRO A 1 436 ? -4.08900  24.42700  11.47800 1.000 53.67396  ?  436 PRO A CD     1 
ATOM   6804 H HA     . PRO A 1 436 ? -3.76700  27.33000  10.68800 1.000 59.68261  ?  436 PRO A HA     1 
ATOM   6805 H HB2    . PRO A 1 436 ? -5.67900  26.06600  9.28900  1.000 65.25571  ?  436 PRO A HB2    1 
ATOM   6806 H HB3    . PRO A 1 436 ? -4.12000  26.01000  8.98500  1.000 65.25571  ?  436 PRO A HB3    1 
ATOM   6807 H HG2    . PRO A 1 436 ? -5.66500  24.12200  10.23100 1.000 70.56315  ?  436 PRO A HG2    1 
ATOM   6808 H HG3    . PRO A 1 436 ? -4.26000  23.91700  9.51800  1.000 70.56315  ?  436 PRO A HG3    1 
ATOM   6809 H HD2    . PRO A 1 436 ? -4.55200  23.82700  12.08400 1.000 64.52652  ?  436 PRO A HD2    1 
ATOM   6810 H HD3    . PRO A 1 436 ? -3.16100  24.15900  11.39000 1.000 64.52652  ?  436 PRO A HD3    1 
ATOM   6811 N N      . VAL A 1 437 ? -6.56800  27.27800  12.16500 1.000 47.77934  ?  437 VAL A N      1 
ATOM   6812 C CA     . VAL A 1 437 ? -7.67300  28.14000  12.56200 1.000 47.64290  ?  437 VAL A CA     1 
ATOM   6813 C C      . VAL A 1 437 ? -7.17600  29.50700  13.02100 1.000 50.49529  ?  437 VAL A C      1 
ATOM   6814 O O      . VAL A 1 437 ? -7.92800  30.49400  12.96700 1.000 49.77911  ?  437 VAL A O      1 
ATOM   6815 C CB     . VAL A 1 437 ? -8.51700  27.45700  13.66500 1.000 52.63491  ?  437 VAL A CB     1 
ATOM   6816 C CG1    . VAL A 1 437 ? -7.67800  27.16600  14.89600 1.000 52.05622  ?  437 VAL A CG1    1 
ATOM   6817 C CG2    . VAL A 1 437 ? -9.72000  28.31600  14.02400 1.000 59.07957  ?  437 VAL A CG2    1 
ATOM   6818 H H      . VAL A 1 437 ? -6.50700  26.54500  12.61100 1.000 57.45298  ?  437 VAL A H      1 
ATOM   6819 H HA     . VAL A 1 437 ? -8.24700  28.27600  11.79200 1.000 57.28925  ?  437 VAL A HA     1 
ATOM   6820 H HB     . VAL A 1 437 ? -8.84000  26.60900  13.32200 1.000 63.27966  ?  437 VAL A HB     1 
ATOM   6821 H HG11   . VAL A 1 437 ? -8.23800  26.74700  15.56800 1.000 62.58523  ?  437 VAL A HG11   1 
ATOM   6822 H HG12   . VAL A 1 437 ? -6.95300  26.57000  14.65100 1.000 62.58523  ?  437 VAL A HG12   1 
ATOM   6823 H HG13   . VAL A 1 437 ? -7.31900  28.00000  15.23800 1.000 62.58523  ?  437 VAL A HG13   1 
ATOM   6824 H HG21   . VAL A 1 437 ? -10.30800 27.80900  14.60500 1.000 71.01326  ?  437 VAL A HG21   1 
ATOM   6825 H HG22   . VAL A 1 437 ? -9.41200  29.11500  14.48100 1.000 71.01326  ?  437 VAL A HG22   1 
ATOM   6826 H HG23   . VAL A 1 437 ? -10.18800 28.56000  13.21100 1.000 71.01326  ?  437 VAL A HG23   1 
ATOM   6827 N N      . LEU A 1 438 ? -5.92000  29.60000  13.45300 1.000 47.70620  ?  438 LEU A N      1 
ATOM   6828 C CA     . LEU A 1 438 ? -5.34200  30.83500  13.94100 1.000 47.87871  ?  438 LEU A CA     1 
ATOM   6829 C C      . LEU A 1 438 ? -4.47400  31.54000  12.90200 1.000 49.04895  ?  438 LEU A C      1 
ATOM   6830 O O      . LEU A 1 438 ? -3.75200  32.49000  13.24900 1.000 50.68797  ?  438 LEU A O      1 
ATOM   6831 C CB     . LEU A 1 438 ? -4.51000  30.56200  15.19400 1.000 46.77131  ?  438 LEU A CB     1 
ATOM   6832 C CG     . LEU A 1 438 ? -5.31100  30.35000  16.47500 1.000 50.51999  ?  438 LEU A CG     1 
ATOM   6833 C CD1    . LEU A 1 438 ? -4.52100  29.50200  17.45300 1.000 46.80019  ?  438 LEU A CD1    1 
ATOM   6834 C CD2    . LEU A 1 438 ? -5.67700  31.69600  17.09000 1.000 56.99782  ?  438 LEU A CD2    1 
ATOM   6835 H H      . LEU A 1 438 ? -5.37200  28.93700  13.47100 1.000 57.36521  ?  438 LEU A H      1 
ATOM   6836 H HA     . LEU A 1 438 ? -6.06800  31.43400  14.17500 1.000 57.57222  ?  438 LEU A HA     1 
ATOM   6837 H HB2    . LEU A 1 438 ? -3.98600  29.76100  15.04400 1.000 56.24334  ?  438 LEU A HB2    1 
ATOM   6838 H HB3    . LEU A 1 438 ? -3.92300  31.32000  15.34200 1.000 56.24334  ?  438 LEU A HB3    1 
ATOM   6839 H HG     . LEU A 1 438 ? -6.13400  29.87900  16.27200 1.000 60.74176  ?  438 LEU A HG     1 
ATOM   6840 H HD11   . LEU A 1 438 ? -5.03900  29.39300  18.26600 1.000 56.27800  ?  438 LEU A HD11   1 
ATOM   6841 H HD12   . LEU A 1 438 ? -4.34800  28.63600  17.05200 1.000 56.27800  ?  438 LEU A HD12   1 
ATOM   6842 H HD13   . LEU A 1 438 ? -3.68300  29.94800  17.65200 1.000 56.27800  ?  438 LEU A HD13   1 
ATOM   6843 H HD21   . LEU A 1 438 ? -6.26200  31.54800  17.84900 1.000 68.51515  ?  438 LEU A HD21   1 
ATOM   6844 H HD22   . LEU A 1 438 ? -4.86600  32.14200  17.37900 1.000 68.51515  ?  438 LEU A HD22   1 
ATOM   6845 H HD23   . LEU A 1 438 ? -6.13100  32.23500  16.42300 1.000 68.51515  ?  438 LEU A HD23   1 
ATOM   6846 N N      . LYS A 1 439 ? -4.52900  31.10400  11.64100 1.000 51.67050  ?  439 LYS A N      1 
ATOM   6847 C CA     . LYS A 1 439 ? -3.56100  31.57400  10.65600 1.000 53.25866  ?  439 LYS A CA     1 
ATOM   6848 C C      . LYS A 1 439 ? -3.69900  33.05700  10.36200 1.000 53.48422  ?  439 LYS A C      1 
ATOM   6849 O O      . LYS A 1 439 ? -2.72500  33.69700  9.95300  1.000 56.71324  ?  439 LYS A O      1 
ATOM   6850 C CB     . LYS A 1 439 ? -3.68700  30.76100  9.36800  1.000 55.30397  ?  439 LYS A CB     1 
ATOM   6851 C CG     . LYS A 1 439 ? -4.96300  31.00200  8.57600  1.000 62.17958  ?  439 LYS A CG     1 
ATOM   6852 C CD     . LYS A 1 439 ? -5.10400  29.94800  7.46500  1.000 75.57856  ?  439 LYS A CD     1 
ATOM   6853 C CE     . LYS A 1 439 ? -5.67500  30.53700  6.18200  1.000 80.49068  ?  439 LYS A CE     1 
ATOM   6854 N NZ     . LYS A 1 439 ? -7.12800  30.81400  6.29300  1.000 94.50275  ?  439 LYS A NZ     1 
ATOM   6855 H H      . LYS A 1 439 ? -5.10900  30.54600  11.33700 1.000 62.12237  ?  439 LYS A H      1 
ATOM   6856 H HA     . LYS A 1 439 ? -2.67100  31.43600  11.01700 1.000 64.02816  ?  439 LYS A HA     1 
ATOM   6857 H HB2    . LYS A 1 439 ? -2.94000  30.98300  8.79000  1.000 66.48254  ?  439 LYS A HB2    1 
ATOM   6858 H HB3    . LYS A 1 439 ? -3.66100  29.81900  9.59600  1.000 66.48254  ?  439 LYS A HB3    1 
ATOM   6859 H HG2    . LYS A 1 439 ? -5.73000  30.93700  9.16600  1.000 74.73326  ?  439 LYS A HG2    1 
ATOM   6860 H HG3    . LYS A 1 439 ? -4.93200  31.88100  8.16700  1.000 74.73326  ?  439 LYS A HG3    1 
ATOM   6861 H HD2    . LYS A 1 439 ? -4.23100  29.57600  7.26400  1.000 90.81204  ?  439 LYS A HD2    1 
ATOM   6862 H HD3    . LYS A 1 439 ? -5.70200  29.24500  7.76600  1.000 90.81204  ?  439 LYS A HD3    1 
ATOM   6863 H HE2    . LYS A 1 439 ? -5.22200  31.37300  5.98700  1.000 96.70659  ?  439 LYS A HE2    1 
ATOM   6864 H HE3    . LYS A 1 439 ? -5.54100  29.90900  5.45600  1.000 96.70659  ?  439 LYS A HE3    1 
ATOM   6865 H HZ1    . LYS A 1 439 ? -7.43600  31.13700  5.52300  1.000 113.52107 ?  439 LYS A HZ1    1 
ATOM   6866 H HZ2    . LYS A 1 439 ? -7.56700  30.06400  6.48700  1.000 113.52107 ?  439 LYS A HZ2    1 
ATOM   6867 H HZ3    . LYS A 1 439 ? -7.27600  31.41000  6.93600  1.000 113.52107 ?  439 LYS A HZ3    1 
ATOM   6868 N N      . ASP A 1 440 ? -4.88500  33.63400  10.56300 1.000 56.18219  ?  440 ASP A N      1 
ATOM   6869 C CA     . ASP A 1 440 ? -5.09500  35.05500  10.30000 1.000 53.08841  ?  440 ASP A CA     1 
ATOM   6870 C C      . ASP A 1 440 ? -5.12700  35.90600  11.56700 1.000 54.81785  ?  440 ASP A C      1 
ATOM   6871 O O      . ASP A 1 440 ? -5.38700  37.10700  11.47700 1.000 55.24615  ?  440 ASP A O      1 
ATOM   6872 C CB     . ASP A 1 440 ? -6.39000  35.24900  9.50900  1.000 59.84528  ?  440 ASP A CB     1 
ATOM   6873 C CG     . ASP A 1 440 ? -6.30600  34.67800  8.10200  1.000 61.91226  ?  440 ASP A CG     1 
ATOM   6874 O OD1    . ASP A 1 440 ? -5.33700  35.00000  7.38100  1.000 64.65890  ?  440 ASP A OD1    1 
ATOM   6875 O OD2    . ASP A 1 440 ? -7.21200  33.90300  7.71600  1.000 81.21333  -1 440 ASP A OD2    1 
ATOM   6876 H H      . ASP A 1 440 ? -5.58300  33.22200  10.85100 1.000 67.53640  ?  440 ASP A H      1 
ATOM   6877 H HA     . ASP A 1 440 ? -4.36000  35.38000  9.75700  1.000 63.82386  ?  440 ASP A HA     1 
ATOM   6878 H HB2    . ASP A 1 440 ? -7.11500  34.80000  9.97300  1.000 71.93211  ?  440 ASP A HB2    1 
ATOM   6879 H HB3    . ASP A 1 440 ? -6.57900  36.19700  9.43800  1.000 71.93211  ?  440 ASP A HB3    1 
ATOM   6880 N N      . MET A 1 441 ? -4.87100  35.31300  12.73400 1.000 52.53016  ?  441 MET A N      1 
ATOM   6881 C CA     . MET A 1 441 ? -4.77800  36.08800  13.97300 1.000 49.50338  ?  441 MET A CA     1 
ATOM   6882 C C      . MET A 1 441 ? -3.57800  37.02700  13.90400 1.000 51.25739  ?  441 MET A C      1 
ATOM   6883 O O      . MET A 1 441 ? -2.48300  36.59700  13.52200 1.000 53.06025  ?  441 MET A O      1 
ATOM   6884 C CB     . MET A 1 441 ? -4.63300  35.13100  15.15800 1.000 51.12056  ?  441 MET A CB     1 
ATOM   6885 C CG     . MET A 1 441 ? -4.98500  35.67500  16.54600 1.000 52.49516  ?  441 MET A CG     1 
ATOM   6886 S SD     . MET A 1 441 ? -6.34700  36.87500  16.62100 1.000 55.89095  ?  441 MET A SD     1 
ATOM   6887 C CE     . MET A 1 441 ? -7.71300  35.86200  17.09200 1.000 51.18214  ?  441 MET A CE     1 
ATOM   6888 H H      . MET A 1 441 ? -4.74800  34.46800  12.83700 1.000 63.15396  ?  441 MET A H      1 
ATOM   6889 H HA     . MET A 1 441 ? -5.58400  36.61300  14.09600 1.000 59.52182  ?  441 MET A HA     1 
ATOM   6890 H HB2    . MET A 1 441 ? -5.21200  34.36900  14.99900 1.000 61.46244  ?  441 MET A HB2    1 
ATOM   6891 H HB3    . MET A 1 441 ? -3.70700  34.84200  15.19600 1.000 61.46244  ?  441 MET A HB3    1 
ATOM   6892 H HG2    . MET A 1 441 ? -5.23500  34.92600  17.10900 1.000 63.11196  ?  441 MET A HG2    1 
ATOM   6893 H HG3    . MET A 1 441 ? -4.19900  36.11400  16.90700 1.000 63.11196  ?  441 MET A HG3    1 
ATOM   6894 H HE1    . MET A 1 441 ? -8.50600  36.41500  17.16500 1.000 61.53634  ?  441 MET A HE1    1 
ATOM   6895 H HE2    . MET A 1 441 ? -7.84700  35.17900  16.41600 1.000 61.53634  ?  441 MET A HE2    1 
ATOM   6896 H HE3    . MET A 1 441 ? -7.51800  35.44700  17.94700 1.000 61.53634  ?  441 MET A HE3    1 
ATOM   6897 N N      . PRO A 1 442 ? -3.73200  38.31100  14.25500 1.000 52.46281  ?  442 PRO A N      1 
ATOM   6898 C CA     . PRO A 1 442 ? -2.54800  39.18000  14.34900 1.000 51.59808  ?  442 PRO A CA     1 
ATOM   6899 C C      . PRO A 1 442 ? -1.56000  38.65300  15.38300 1.000 48.99573  ?  442 PRO A C      1 
ATOM   6900 O O      . PRO A 1 442 ? -1.94000  38.14100  16.43800 1.000 51.79716  ?  442 PRO A O      1 
ATOM   6901 C CB     . PRO A 1 442 ? -3.13600  40.53600  14.75800 1.000 53.61963  ?  442 PRO A CB     1 
ATOM   6902 C CG     . PRO A 1 442 ? -4.53400  40.50100  14.24100 1.000 52.57025  ?  442 PRO A CG     1 
ATOM   6903 C CD     . PRO A 1 442 ? -4.98700  39.08100  14.40900 1.000 52.64431  ?  442 PRO A CD     1 
ATOM   6904 H HA     . PRO A 1 442 ? -2.10700  39.26400  13.48900 1.000 62.03546  ?  442 PRO A HA     1 
ATOM   6905 H HB2    . PRO A 1 442 ? -3.12300  40.62700  15.72300 1.000 64.46133  ?  442 PRO A HB2    1 
ATOM   6906 H HB3    . PRO A 1 442 ? -2.63000  41.25500  14.34900 1.000 64.46133  ?  442 PRO A HB3    1 
ATOM   6907 H HG2    . PRO A 1 442 ? -5.09000  41.10400  14.75700 1.000 63.20207  ?  442 PRO A HG2    1 
ATOM   6908 H HG3    . PRO A 1 442 ? -4.54500  40.75800  13.30500 1.000 63.20207  ?  442 PRO A HG3    1 
ATOM   6909 H HD2    . PRO A 1 442 ? -5.37300  38.94200  15.28800 1.000 63.29094  ?  442 PRO A HD2    1 
ATOM   6910 H HD3    . PRO A 1 442 ? -5.62900  38.83800  13.72300 1.000 63.29094  ?  442 PRO A HD3    1 
ATOM   6911 N N      . ALA A 1 443 ? -0.27400  38.79100  15.07200 1.000 52.05936  ?  443 ALA A N      1 
ATOM   6912 C CA     . ALA A 1 443 ? 0.75700   38.20200  15.92200 1.000 53.89527  ?  443 ALA A CA     1 
ATOM   6913 C C      . ALA A 1 443 ? 0.68700   38.73200  17.35000 1.000 55.65616  ?  443 ALA A C      1 
ATOM   6914 O O      . ALA A 1 443 ? 1.07300   38.02600  18.29100 1.000 55.29213  ?  443 ALA A O      1 
ATOM   6915 C CB     . ALA A 1 443 ? 2.13900   38.47800  15.32600 1.000 58.37752  ?  443 ALA A CB     1 
ATOM   6916 H H      . ALA A 1 443 ? 0.02500   39.21300  14.38500 1.000 62.58900  ?  443 ALA A H      1 
ATOM   6917 H HA     . ALA A 1 443 ? 0.62100   37.24200  15.95300 1.000 64.79209  ?  443 ALA A HA     1 
ATOM   6918 H HB1    . ALA A 1 443 ? 2.81500   38.08400  15.90000 1.000 70.17079  ?  443 ALA A HB1    1 
ATOM   6919 H HB2    . ALA A 1 443 ? 2.18600   38.08500  14.44100 1.000 70.17079  ?  443 ALA A HB2    1 
ATOM   6920 H HB3    . ALA A 1 443 ? 2.27300   39.43700  15.27000 1.000 70.17079  ?  443 ALA A HB3    1 
ATOM   6921 N N      . LYS A 1 444 ? 0.20500   39.96800  17.53500 1.000 55.76310  ?  444 LYS A N      1 
ATOM   6922 C CA     . LYS A 1 444 ? 0.11800   40.53000  18.88300 1.000 57.33842  ?  444 LYS A CA     1 
ATOM   6923 C C      . LYS A 1 444 ? -0.73000  39.66200  19.81000 1.000 48.99267  ?  444 LYS A C      1 
ATOM   6924 O O      . LYS A 1 444 ? -0.50100  39.65200  21.02200 1.000 54.61922  ?  444 LYS A O      1 
ATOM   6925 C CB     . LYS A 1 444 ? -0.45200  41.95300  18.81500 1.000 66.16373  ?  444 LYS A CB     1 
ATOM   6926 C CG     . LYS A 1 444 ? -0.66300  42.61700  20.17400 1.000 70.99369  ?  444 LYS A CG     1 
ATOM   6927 C CD     . LYS A 1 444 ? -1.62000  43.79400  20.08400 1.000 81.13953  ?  444 LYS A CD     1 
ATOM   6928 C CE     . LYS A 1 444 ? -1.00400  44.98300  19.36700 1.000 80.71948  ?  444 LYS A CE     1 
ATOM   6929 N NZ     . LYS A 1 444 ? -1.31800  44.97400  17.90700 1.000 99.23300  ?  444 LYS A NZ     1 
ATOM   6930 H H      . LYS A 1 444 ? -0.07200  40.48900  16.90900 1.000 67.03349  ?  444 LYS A H      1 
ATOM   6931 H HA     . LYS A 1 444 ? 1.01100   40.57700  19.26000 1.000 68.92388  ?  444 LYS A HA     1 
ATOM   6932 H HB2    . LYS A 1 444 ? 0.16300   42.50800  18.31000 1.000 79.51425  ?  444 LYS A HB2    1 
ATOM   6933 H HB3    . LYS A 1 444 ? -1.31200  41.92000  18.36800 1.000 79.51425  ?  444 LYS A HB3    1 
ATOM   6934 H HG2    . LYS A 1 444 ? -1.03700  41.96900  20.79200 1.000 85.31020  ?  444 LYS A HG2    1 
ATOM   6935 H HG3    . LYS A 1 444 ? 0.18800   42.94100  20.50800 1.000 85.31020  ?  444 LYS A HG3    1 
ATOM   6936 H HD2    . LYS A 1 444 ? -2.41200  43.52400  19.59500 1.000 97.48521  ?  444 LYS A HD2    1 
ATOM   6937 H HD3    . LYS A 1 444 ? -1.86300  44.07600  20.98000 1.000 97.48521  ?  444 LYS A HD3    1 
ATOM   6938 H HE2    . LYS A 1 444 ? -1.35500  45.80300  19.74800 1.000 96.98114  ?  444 LYS A HE2    1 
ATOM   6939 H HE3    . LYS A 1 444 ? -0.04000  44.95400  19.47000 1.000 96.98114  ?  444 LYS A HE3    1 
ATOM   6940 H HZ1    . LYS A 1 444 ? -0.94600  45.67900  17.51200 1.000 119.19737 ?  444 LYS A HZ1    1 
ATOM   6941 H HZ2    . LYS A 1 444 ? -1.00200  44.23100  17.53200 1.000 119.19737 ?  444 LYS A HZ2    1 
ATOM   6942 H HZ3    . LYS A 1 444 ? -2.19900  45.00600  17.78500 1.000 119.19737 ?  444 LYS A HZ3    1 
ATOM   6943 N N      . TYR A 1 445 ? -1.69200  38.92300  19.26600 1.000 50.17401  ?  445 TYR A N      1 
ATOM   6944 C CA     . TYR A 1 445 ? -2.57800  38.10600  20.08000 1.000 52.67827  ?  445 TYR A CA     1 
ATOM   6945 C C      . TYR A 1 445 ? -2.45400  36.60200  19.84800 1.000 51.29702  ?  445 TYR A C      1 
ATOM   6946 O O      . TYR A 1 445 ? -3.18200  35.84000  20.49200 1.000 48.29287  ?  445 TYR A O      1 
ATOM   6947 C CB     . TYR A 1 445 ? -4.05100  38.49800  19.83000 1.000 53.02748  ?  445 TYR A CB     1 
ATOM   6948 C CG     . TYR A 1 445 ? -4.30700  39.98400  19.78900 1.000 56.57572  ?  445 TYR A CG     1 
ATOM   6949 C CD1    . TYR A 1 445 ? -4.32100  40.73900  20.95400 1.000 57.25611  ?  445 TYR A CD1    1 
ATOM   6950 C CD2    . TYR A 1 445 ? -4.55300  40.63000  18.58300 1.000 56.67246  ?  445 TYR A CD2    1 
ATOM   6951 C CE1    . TYR A 1 445 ? -4.56400  42.10500  20.92100 1.000 52.20484  ?  445 TYR A CE1    1 
ATOM   6952 C CE2    . TYR A 1 445 ? -4.80200  41.98600  18.53800 1.000 65.44930  ?  445 TYR A CE2    1 
ATOM   6953 C CZ     . TYR A 1 445 ? -4.80900  42.71700  19.70700 1.000 62.63440  ?  445 TYR A CZ     1 
ATOM   6954 O OH     . TYR A 1 445 ? -5.05700  44.06400  19.65300 1.000 64.42628  ?  445 TYR A OH     1 
ATOM   6955 H H      . TYR A 1 445 ? -1.85000  38.88000  18.42200 1.000 60.32658  ?  445 TYR A H      1 
ATOM   6956 H HA     . TYR A 1 445 ? -2.34700  38.28300  21.00600 1.000 63.33170  ?  445 TYR A HA     1 
ATOM   6957 H HB2    . TYR A 1 445 ? -4.32700  38.13100  18.97500 1.000 63.75074  ?  445 TYR A HB2    1 
ATOM   6958 H HB3    . TYR A 1 445 ? -4.59500  38.12700  20.54200 1.000 63.75074  ?  445 TYR A HB3    1 
ATOM   6959 H HD1    . TYR A 1 445 ? -4.16600  40.32300  21.77000 1.000 68.82511  ?  445 TYR A HD1    1 
ATOM   6960 H HD2    . TYR A 1 445 ? -4.55000  40.13900  17.79300 1.000 68.12472  ?  445 TYR A HD2    1 
ATOM   6961 H HE1    . TYR A 1 445 ? -4.56200  42.60200  21.70700 1.000 62.76358  ?  445 TYR A HE1    1 
ATOM   6962 H HE2    . TYR A 1 445 ? -4.96500  42.40500  17.72300 1.000 78.65693  ?  445 TYR A HE2    1 
ATOM   6963 H HH     . TYR A 1 445 ? -5.22600  44.29300  18.86300 1.000 77.42931  ?  445 TYR A HH     1 
ATOM   6964 N N      . ILE A 1 446 ? -1.56600  36.15400  18.96000 1.000 49.33479  ?  446 ILE A N      1 
ATOM   6965 C CA     . ILE A 1 446 ? -1.59800  34.75700  18.54300 1.000 48.93390  ?  446 ILE A CA     1 
ATOM   6966 C C      . ILE A 1 446 ? -1.21900  33.80400  19.67000 1.000 46.57772  ?  446 ILE A C      1 
ATOM   6967 O O      . ILE A 1 446 ? -1.60100  32.63200  19.63000 1.000 47.26942  ?  446 ILE A O      1 
ATOM   6968 C CB     . ILE A 1 446 ? -0.68300  34.50700  17.32000 1.000 46.65240  ?  446 ILE A CB     1 
ATOM   6969 C CG1    . ILE A 1 446 ? -0.91400  33.08300  16.79400 1.000 47.91457  ?  446 ILE A CG1    1 
ATOM   6970 C CG2    . ILE A 1 446 ? 0.77600   34.69900  17.68800 1.000 44.03463  ?  446 ILE A CG2    1 
ATOM   6971 C CD1    . ILE A 1 446 ? -0.90400  32.96600  15.30400 1.000 49.86591  ?  446 ILE A CD1    1 
ATOM   6972 H H      . ILE A 1 446 ? -0.95000  36.62900  18.59300 1.000 59.31952  ?  446 ILE A H      1 
ATOM   6973 H HA     . ILE A 1 446 ? -2.51300  34.57200  18.28100 1.000 58.83845  ?  446 ILE A HA     1 
ATOM   6974 H HB     . ILE A 1 446 ? -0.90800  35.14900  16.62800 1.000 56.10065  ?  446 ILE A HB     1 
ATOM   6975 H HG12   . ILE A 1 446 ? -0.21200  32.50900  17.13800 1.000 57.61526  ?  446 ILE A HG12   1 
ATOM   6976 H HG13   . ILE A 1 446 ? -1.77800  32.77400  17.10700 1.000 57.61526  ?  446 ILE A HG13   1 
ATOM   6977 H HG21   . ILE A 1 446 ? 1.31200   34.66700  16.88000 1.000 52.95933  ?  446 ILE A HG21   1 
ATOM   6978 H HG22   . ILE A 1 446 ? 0.88200   35.56000  18.12100 1.000 52.95933  ?  446 ILE A HG22   1 
ATOM   6979 H HG23   . ILE A 1 446 ? 1.04500   33.98900  18.29100 1.000 52.95933  ?  446 ILE A HG23   1 
ATOM   6980 H HD11   . ILE A 1 446 ? -1.16400  32.06500  15.05600 1.000 59.95686  ?  446 ILE A HD11   1 
ATOM   6981 H HD12   . ILE A 1 446 ? -1.53300  33.60500  14.93300 1.000 59.95686  ?  446 ILE A HD12   1 
ATOM   6982 H HD13   . ILE A 1 446 ? -0.01000  33.15400  14.97800 1.000 59.95686  ?  446 ILE A HD13   1 
ATOM   6983 N N      . TYR A 1 447 ? -0.46700  34.26700  20.66900 1.000 43.75079  ?  447 TYR A N      1 
ATOM   6984 C CA     . TYR A 1 447 ? -0.15100  33.42100  21.81400 1.000 45.20977  ?  447 TYR A CA     1 
ATOM   6985 C C      . TYR A 1 447 ? -1.19600  33.50900  22.91700 1.000 50.30857  ?  447 TYR A C      1 
ATOM   6986 O O      . TYR A 1 447 ? -1.29800  32.57900  23.73400 1.000 45.80826  ?  447 TYR A O      1 
ATOM   6987 C CB     . TYR A 1 447 ? 1.22600   33.79600  22.38300 1.000 47.30389  ?  447 TYR A CB     1 
ATOM   6988 C CG     . TYR A 1 447 ? 2.36700   33.19600  21.60000 1.000 46.42887  ?  447 TYR A CG     1 
ATOM   6989 C CD1    . TYR A 1 447 ? 2.84300   31.92100  21.89700 1.000 45.55365  ?  447 TYR A CD1    1 
ATOM   6990 C CD2    . TYR A 1 447 ? 2.94600   33.88300  20.53800 1.000 47.21174  ?  447 TYR A CD2    1 
ATOM   6991 C CE1    . TYR A 1 447 ? 3.87400   31.35600  21.16600 1.000 45.80130  ?  447 TYR A CE1    1 
ATOM   6992 C CE2    . TYR A 1 447 ? 3.97900   33.32800  19.80400 1.000 48.56908  ?  447 TYR A CE2    1 
ATOM   6993 C CZ     . TYR A 1 447 ? 4.43900   32.06200  20.12100 1.000 46.84267  ?  447 TYR A CZ     1 
ATOM   6994 O OH     . TYR A 1 447 ? 5.45300   31.50500  19.39500 1.000 47.19058  ?  447 TYR A OH     1 
ATOM   6995 H H      . TYR A 1 447 ? -0.13300  35.05900  20.70400 1.000 52.61872  ?  447 TYR A H      1 
ATOM   6996 H HA     . TYR A 1 447 ? -0.10600  32.49800  21.52100 1.000 54.36949  ?  447 TYR A HA     1 
ATOM   6997 H HB2    . TYR A 1 447 ? 1.32400   34.76100  22.36300 1.000 56.88244  ?  447 TYR A HB2    1 
ATOM   6998 H HB3    . TYR A 1 447 ? 1.28800   33.47500  23.29700 1.000 56.88244  ?  447 TYR A HB3    1 
ATOM   6999 H HD1    . TYR A 1 447 ? 2.46300   31.44100  22.59700 1.000 54.78215  ?  447 TYR A HD1    1 
ATOM   7000 H HD2    . TYR A 1 447 ? 2.63400   34.73100  20.31800 1.000 56.77186  ?  447 TYR A HD2    1 
ATOM   7001 H HE1    . TYR A 1 447 ? 4.18500   30.50500  21.37700 1.000 55.07933  ?  447 TYR A HE1    1 
ATOM   7002 H HE2    . TYR A 1 447 ? 4.36100   33.80200  19.10200 1.000 58.40067  ?  447 TYR A HE2    1 
ATOM   7003 H HH     . TYR A 1 447 ? 5.65300   32.00400  18.75000 1.000 56.74647  ?  447 TYR A HH     1 
ATOM   7004 N N      . GLU A 1 448 ? -1.96800  34.60100  22.96100 1.000 47.65064  ?  448 GLU A N      1 
ATOM   7005 C CA     . GLU A 1 448 ? -3.04700  34.78500  23.93400 1.000 50.59725  ?  448 GLU A CA     1 
ATOM   7006 C C      . GLU A 1 448 ? -4.28400  35.28400  23.19900 1.000 51.51052  ?  448 GLU A C      1 
ATOM   7007 O O      . GLU A 1 448 ? -4.71000  36.43200  23.36600 1.000 50.99258  ?  448 GLU A O      1 
ATOM   7008 C CB     . GLU A 1 448 ? -2.61600  35.75400  25.03200 1.000 52.09417  ?  448 GLU A CB     1 
ATOM   7009 C CG     . GLU A 1 448 ? -1.33800  35.32300  25.74200 1.000 61.22140  ?  448 GLU A CG     1 
ATOM   7010 C CD     . GLU A 1 448 ? -0.63500  36.48100  26.41300 1.000 68.91313  ?  448 GLU A CD     1 
ATOM   7011 O OE1    . GLU A 1 448 ? -0.18300  37.40000  25.69100 1.000 67.81438  ?  448 GLU A OE1    1 
ATOM   7012 O OE2    . GLU A 1 448 ? -0.53500  36.46300  27.65500 1.000 80.79000  -1 448 GLU A OE2    1 
ATOM   7013 H H      . GLU A 1 448 ? -1.88200  35.26500  22.42200 1.000 57.29854  ?  448 GLU A H      1 
ATOM   7014 H HA     . GLU A 1 448 ? -3.26700  33.93600  24.34900 1.000 60.83447  ?  448 GLU A HA     1 
ATOM   7015 H HB2    . GLU A 1 448 ? -2.46000  36.62600  24.63800 1.000 62.63077  ?  448 GLU A HB2    1 
ATOM   7016 H HB3    . GLU A 1 448 ? -3.32200  35.81100  25.69500 1.000 62.63077  ?  448 GLU A HB3    1 
ATOM   7017 H HG2    . GLU A 1 448 ? -1.55800  34.66800  26.42300 1.000 73.58345  ?  448 GLU A HG2    1 
ATOM   7018 H HG3    . GLU A 1 448 ? -0.72900  34.93600  25.09300 1.000 73.58345  ?  448 GLU A HG3    1 
ATOM   7019 N N      . PRO A 1 449 ? -4.89000  34.43700  22.37000 1.000 52.27553  ?  449 PRO A N      1 
ATOM   7020 C CA     . PRO A 1 449 ? -5.99100  34.91200  21.51100 1.000 55.77263  ?  449 PRO A CA     1 
ATOM   7021 C C      . PRO A 1 449 ? -7.18100  35.46400  22.28500 1.000 53.55371  ?  449 PRO A C      1 
ATOM   7022 O O      . PRO A 1 449 ? -7.93700  36.26900  21.72700 1.000 51.52280  ?  449 PRO A O      1 
ATOM   7023 C CB     . PRO A 1 449 ? -6.38000  33.66400  20.70000 1.000 52.41404  ?  449 PRO A CB     1 
ATOM   7024 C CG     . PRO A 1 449 ? -5.73700  32.50400  21.39400 1.000 46.69328  ?  449 PRO A CG     1 
ATOM   7025 C CD     . PRO A 1 449 ? -4.55500  33.01300  22.13400 1.000 45.61410  ?  449 PRO A CD     1 
ATOM   7026 H HA     . PRO A 1 449 ? -5.66000  35.59300  20.90500 1.000 67.04493  ?  449 PRO A HA     1 
ATOM   7027 H HB2    . PRO A 1 449 ? -7.34500  33.56800  20.69200 1.000 63.01461  ?  449 PRO A HB2    1 
ATOM   7028 H HB3    . PRO A 1 449 ? -6.04800  33.74900  19.79200 1.000 63.01461  ?  449 PRO A HB3    1 
ATOM   7029 H HG2    . PRO A 1 449 ? -6.37400  32.10800  22.00900 1.000 56.14970  ?  449 PRO A HG2    1 
ATOM   7030 H HG3    . PRO A 1 449 ? -5.46300  31.84900  20.73300 1.000 56.14970  ?  449 PRO A HG3    1 
ATOM   7031 H HD2    . PRO A 1 449 ? -4.44400  32.54100  22.97400 1.000 54.85469  ?  449 PRO A HD2    1 
ATOM   7032 H HD3    . PRO A 1 449 ? -3.75100  32.93200  21.59800 1.000 54.85469  ?  449 PRO A HD3    1 
ATOM   7033 N N      . TRP A 1 450 ? -7.36300  35.06600  23.54800 1.000 54.79885  ?  450 TRP A N      1 
ATOM   7034 C CA     . TRP A 1 450 ? -8.46300  35.59700  24.34400 1.000 56.73736  ?  450 TRP A CA     1 
ATOM   7035 C C      . TRP A 1 450 ? -8.30100  37.07900  24.66700 1.000 54.13368  ?  450 TRP A C      1 
ATOM   7036 O O      . TRP A 1 450 ? -9.26500  37.70100  25.12400 1.000 53.83293  ?  450 TRP A O      1 
ATOM   7037 C CB     . TRP A 1 450 ? -8.60500  34.80100  25.65300 1.000 53.94890  ?  450 TRP A CB     1 
ATOM   7038 C CG     . TRP A 1 450 ? -7.37300  34.83200  26.51200 1.000 60.29431  ?  450 TRP A CG     1 
ATOM   7039 C CD1    . TRP A 1 450 ? -7.08600  35.73400  27.49600 1.000 59.74867  ?  450 TRP A CD1    1 
ATOM   7040 C CD2    . TRP A 1 450 ? -6.26400  33.92700  26.46000 1.000 54.54147  ?  450 TRP A CD2    1 
ATOM   7041 N NE1    . TRP A 1 450 ? -5.87300  35.44000  28.06200 1.000 63.15220  ?  450 TRP A NE1    1 
ATOM   7042 C CE2    . TRP A 1 450 ? -5.34500  34.33800  27.44300 1.000 58.68108  ?  450 TRP A CE2    1 
ATOM   7043 C CE3    . TRP A 1 450 ? -5.96200  32.80600  25.68000 1.000 50.52016  ?  450 TRP A CE3    1 
ATOM   7044 C CZ2    . TRP A 1 450 ? -4.13700  33.66900  27.66500 1.000 58.24500  ?  450 TRP A CZ2    1 
ATOM   7045 C CZ3    . TRP A 1 450 ? -4.76400  32.14100  25.90800 1.000 53.92481  ?  450 TRP A CZ3    1 
ATOM   7046 C CH2    . TRP A 1 450 ? -3.87000  32.57500  26.88800 1.000 52.83382  ?  450 TRP A CH2    1 
ATOM   7047 H H      . TRP A 1 450 ? -6.86700  34.49600  23.95900 1.000 65.87639  ?  450 TRP A H      1 
ATOM   7048 H HA     . TRP A 1 450 ? -9.28400  35.48900  23.83800 1.000 68.20261  ?  450 TRP A HA     1 
ATOM   7049 H HB2    . TRP A 1 450 ? -9.33600  35.17500  26.16900 1.000 64.85645  ?  450 TRP A HB2    1 
ATOM   7050 H HB3    . TRP A 1 450 ? -8.79200  33.87400  25.43600 1.000 64.85645  ?  450 TRP A HB3    1 
ATOM   7051 H HD1    . TRP A 1 450 ? -7.63300  36.44300  27.74600 1.000 71.81618  ?  450 TRP A HD1    1 
ATOM   7052 H HE1    . TRP A 1 450 ? -5.50300  35.87700  28.70300 1.000 75.90041  ?  450 TRP A HE1    1 
ATOM   7053 H HE3    . TRP A 1 450 ? -6.55000  32.51200  25.02300 1.000 60.74196  ?  450 TRP A HE3    1 
ATOM   7054 H HZ2    . TRP A 1 450 ? -3.53800  33.95700  28.31600 1.000 70.01177  ?  450 TRP A HZ2    1 
ATOM   7055 H HZ3    . TRP A 1 450 ? -4.55300  31.39200  25.39700 1.000 64.82754  ?  450 TRP A HZ3    1 
ATOM   7056 H HH2    . TRP A 1 450 ? -3.07500  32.10900  27.01600 1.000 63.51836  ?  450 TRP A HH2    1 
ATOM   7057 N N      . THR A 1 451 ? -7.11400  37.65200  24.45200 1.000 53.55802  ?  451 THR A N      1 
ATOM   7058 C CA     . THR A 1 451 ? -6.89900  39.08000  24.66300 1.000 54.91142  ?  451 THR A CA     1 
ATOM   7059 C C      . THR A 1 451 ? -7.23500  39.92400  23.43900 1.000 53.41544  ?  451 THR A C      1 
ATOM   7060 O O      . THR A 1 451 ? -7.27000  41.15500  23.54300 1.000 51.50146  ?  451 THR A O      1 
ATOM   7061 C CB     . THR A 1 451 ? -5.43900  39.35500  25.05100 1.000 52.48561  ?  451 THR A CB     1 
ATOM   7062 O OG1    . THR A 1 451 ? -4.59100  39.01900  23.94600 1.000 50.28451  ?  451 THR A OG1    1 
ATOM   7063 C CG2    . THR A 1 451 ? -5.04400  38.55900  26.27500 1.000 53.73784  ?  451 THR A CG2    1 
ATOM   7064 H H      . THR A 1 451 ? -6.41500  37.23000  24.18200 1.000 64.38740  ?  451 THR A H      1 
ATOM   7065 H HA     . THR A 1 451 ? -7.46800  39.36100  25.39800 1.000 66.01148  ?  451 THR A HA     1 
ATOM   7066 H HB     . THR A 1 451 ? -5.32700  40.29300  25.27000 1.000 63.10050  ?  451 THR A HB     1 
ATOM   7067 H HG1    . THR A 1 451 ? -3.79400  39.21400  24.12600 1.000 60.45918  ?  451 THR A HG1    1 
ATOM   7068 H HG21   . THR A 1 451 ? -4.14100  38.79300  26.54400 1.000 64.60318  ?  451 THR A HG21   1 
ATOM   7069 H HG22   . THR A 1 451 ? -5.65100  38.75200  27.00600 1.000 64.60318  ?  451 THR A HG22   1 
ATOM   7070 H HG23   . THR A 1 451 ? -5.07800  37.61000  26.07900 1.000 64.60318  ?  451 THR A HG23   1 
ATOM   7071 N N      . ALA A 1 452 ? -7.46300  39.30100  22.29000 1.000 53.06669  ?  452 ALA A N      1 
ATOM   7072 C CA     . ALA A 1 452 ? -7.69200  40.07300  21.07600 1.000 57.68959  ?  452 ALA A CA     1 
ATOM   7073 C C      . ALA A 1 452 ? -8.99500  40.86000  21.19800 1.000 63.20429  ?  452 ALA A C      1 
ATOM   7074 O O      . ALA A 1 452 ? -9.98600  40.34500  21.72400 1.000 58.47852  ?  452 ALA A O      1 
ATOM   7075 C CB     . ALA A 1 452 ? -7.76200  39.15000  19.86200 1.000 55.87558  ?  452 ALA A CB     1 
ATOM   7076 H H      . ALA A 1 452 ? -7.49000  38.44800  22.18600 1.000 63.79780  ?  452 ALA A H      1 
ATOM   7077 H HA     . ALA A 1 452 ? -6.96100  40.69700  20.94600 1.000 69.34528  ?  452 ALA A HA     1 
ATOM   7078 H HB1    . ALA A 1 452 ? -7.91600  39.68500  19.06800 1.000 67.16847  ?  452 ALA A HB1    1 
ATOM   7079 H HB2    . ALA A 1 452 ? -6.92200  38.67200  19.78100 1.000 67.16847  ?  452 ALA A HB2    1 
ATOM   7080 H HB3    . ALA A 1 452 ? -8.49100  38.52200  19.98400 1.000 67.16847  ?  452 ALA A HB3    1 
ATOM   7081 N N      . PRO A 1 453 ? -9.03300  42.10200  20.71800 1.000 65.43149  ?  453 PRO A N      1 
ATOM   7082 C CA     . PRO A 1 453 ? -10.31700 42.80400  20.64900 1.000 71.76084  ?  453 PRO A CA     1 
ATOM   7083 C C      . PRO A 1 453 ? -11.30400 41.95900  19.85800 1.000 71.17227  ?  453 PRO A C      1 
ATOM   7084 O O      . PRO A 1 453 ? -10.96800 41.33300  18.84900 1.000 63.96667  ?  453 PRO A O      1 
ATOM   7085 C CB     . PRO A 1 453 ? -9.98900  44.11800  19.93000 1.000 76.55628  ?  453 PRO A CB     1 
ATOM   7086 C CG     . PRO A 1 453 ? -8.52300  44.26900  19.98800 1.000 65.09007  ?  453 PRO A CG     1 
ATOM   7087 C CD     . PRO A 1 453 ? -7.91000  42.92500  20.22600 1.000 67.18789  ?  453 PRO A CD     1 
ATOM   7088 H HA     . PRO A 1 453 ? -10.66300 43.01500  21.53000 1.000 86.23077  ?  453 PRO A HA     1 
ATOM   7089 H HB2    . PRO A 1 453 ? -10.29300 44.06900  19.01000 1.000 91.98530  ?  453 PRO A HB2    1 
ATOM   7090 H HB3    . PRO A 1 453 ? -10.42700 44.85500  20.38500 1.000 91.98530  ?  453 PRO A HB3    1 
ATOM   7091 H HG2    . PRO A 1 453 ? -8.21000  44.63200  19.14400 1.000 78.22585  ?  453 PRO A HG2    1 
ATOM   7092 H HG3    . PRO A 1 453 ? -8.29600  44.87100  20.71300 1.000 78.22585  ?  453 PRO A HG3    1 
ATOM   7093 H HD2    . PRO A 1 453 ? -7.55400  42.56000  19.40100 1.000 80.74324  ?  453 PRO A HD2    1 
ATOM   7094 H HD3    . PRO A 1 453 ? -7.20800  42.98200  20.89300 1.000 80.74324  ?  453 PRO A HD3    1 
ATOM   7095 N N      . LEU A 1 454 ? -12.53300 41.92200  20.34600 1.000 76.67437  ?  454 LEU A N      1 
ATOM   7096 C CA     . LEU A 1 454 ? -13.49500 40.96900  19.81400 1.000 72.56531  ?  454 LEU A CA     1 
ATOM   7097 C C      . LEU A 1 454 ? -13.79400 41.20600  18.33900 1.000 71.20377  ?  454 LEU A C      1 
ATOM   7098 O O      . LEU A 1 454 ? -14.19200 40.26400  17.64500 1.000 67.40713  ?  454 LEU A O      1 
ATOM   7099 C CB     . LEU A 1 454 ? -14.74800 41.03500  20.67300 1.000 82.55617  ?  454 LEU A CB     1 
ATOM   7100 C CG     . LEU A 1 454 ? -15.92800 40.21000  20.19200 1.000 88.67047  ?  454 LEU A CG     1 
ATOM   7101 C CD1    . LEU A 1 454 ? -16.69800 39.59300  21.33900 1.000 90.04794  ?  454 LEU A CD1    1 
ATOM   7102 C CD2    . LEU A 1 454 ? -16.79400 41.14900  19.41100 1.000 87.85364  ?  454 LEU A CD2    1 
ATOM   7103 H H      . LEU A 1 454 ? -12.83200 42.42800  20.97400 1.000 92.12701  ?  454 LEU A H      1 
ATOM   7104 H HA     . LEU A 1 454 ? -13.14500 40.06500  19.86500 1.000 87.19614  ?  454 LEU A HA     1 
ATOM   7105 H HB2    . LEU A 1 454 ? -14.52300 40.72200  21.56300 1.000 99.18517  ?  454 LEU A HB2    1 
ATOM   7106 H HB3    . LEU A 1 454 ? -15.04000 41.96000  20.71100 1.000 99.18517  ?  454 LEU A HB3    1 
ATOM   7107 H HG     . LEU A 1 454 ? -15.63400 39.46200  19.64900 1.000 106.52234 ?  454 LEU A HG     1 
ATOM   7108 H HD11   . LEU A 1 454 ? -17.42300 39.05800  20.98100 1.000 108.17530 ?  454 LEU A HD11   1 
ATOM   7109 H HD12   . LEU A 1 454 ? -16.09800 39.03400  21.85700 1.000 108.17530 ?  454 LEU A HD12   1 
ATOM   7110 H HD13   . LEU A 1 454 ? -17.05400 40.30200  21.89700 1.000 108.17530 ?  454 LEU A HD13   1 
ATOM   7111 H HD21   . LEU A 1 454 ? -17.60000 40.68300  19.13900 1.000 105.54214 ?  454 LEU A HD21   1 
ATOM   7112 H HD22   . LEU A 1 454 ? -17.02300 41.90700  19.97100 1.000 105.54214 ?  454 LEU A HD22   1 
ATOM   7113 H HD23   . LEU A 1 454 ? -16.30700 41.45200  18.62900 1.000 105.54214 ?  454 LEU A HD23   1 
ATOM   7114 N N      . GLU A 1 455 ? -13.60800 42.42600  17.83100 1.000 70.22230  ?  455 GLU A N      1 
ATOM   7115 C CA     . GLU A 1 455 ? -13.72000 42.64600  16.39000 1.000 69.91308  ?  455 GLU A CA     1 
ATOM   7116 C C      . GLU A 1 455 ? -12.48200 42.17600  15.63600 1.000 66.03294  ?  455 GLU A C      1 
ATOM   7117 O O      . GLU A 1 455 ? -12.57200 41.88700  14.43900 1.000 60.64934  ?  455 GLU A O      1 
ATOM   7118 C CB     . GLU A 1 455 ? -13.99600 44.12700  16.08800 1.000 76.00389  ?  455 GLU A CB     1 
ATOM   7119 C CG     . GLU A 1 455 ? -12.79700 45.06500  16.20600 1.000 78.91692  ?  455 GLU A CG     1 
ATOM   7120 C CD     . GLU A 1 455 ? -12.66500 45.68000  17.59200 1.000 93.90993  ?  455 GLU A CD     1 
ATOM   7121 O OE1    . GLU A 1 455 ? -13.52100 45.38900  18.46700 1.000 94.33862  ?  455 GLU A OE1    1 
ATOM   7122 O OE2    . GLU A 1 455 ? -11.70300 46.45000  17.81000 1.000 99.07765  -1 455 GLU A OE2    1 
ATOM   7123 H H      . GLU A 1 455 ? -13.42000 43.12800  18.29000 1.000 84.38453  ?  455 GLU A H      1 
ATOM   7124 H HA     . GLU A 1 455 ? -14.48000 42.14500  16.05600 1.000 84.01346  ?  455 GLU A HA     1 
ATOM   7125 H HB2    . GLU A 1 455 ? -14.32500 44.19500  15.17900 1.000 91.32244  ?  455 GLU A HB2    1 
ATOM   7126 H HB3    . GLU A 1 455 ? -14.67000 44.44300  16.71000 1.000 91.32244  ?  455 GLU A HB3    1 
ATOM   7127 H HG2    . GLU A 1 455 ? -11.98600 44.56700  16.02000 1.000 94.81807  ?  455 GLU A HG2    1 
ATOM   7128 H HG3    . GLU A 1 455 ? -12.89700 45.78800  15.56600 1.000 94.81807  ?  455 GLU A HG3    1 
ATOM   7129 N N      . VAL A 1 456 ? -11.32500 42.11800  16.29800 1.000 61.29337  ?  456 VAL A N      1 
ATOM   7130 C CA     . VAL A 1 456 ? -10.17000 41.45300  15.69800 1.000 64.94381  ?  456 VAL A CA     1 
ATOM   7131 C C      . VAL A 1 456 ? -10.46100 39.96600  15.52100 1.000 58.76790  ?  456 VAL A C      1 
ATOM   7132 O O      . VAL A 1 456 ? -10.14700 39.37800  14.48100 1.000 53.32611  ?  456 VAL A O      1 
ATOM   7133 C CB     . VAL A 1 456 ? -8.91000  41.68900  16.54700 1.000 62.10506  ?  456 VAL A CB     1 
ATOM   7134 C CG1    . VAL A 1 456 ? -7.73100  40.93600  15.97100 1.000 61.15267  ?  456 VAL A CG1    1 
ATOM   7135 C CG2    . VAL A 1 456 ? -8.59700  43.18500  16.63500 1.000 63.15335  ?  456 VAL A CG2    1 
ATOM   7136 H H      . VAL A 1 456 ? -11.18500 42.44900  17.07900 1.000 73.66981  ?  456 VAL A H      1 
ATOM   7137 H HA     . VAL A 1 456 ? -10.01000 41.83800  14.82200 1.000 78.05034  ?  456 VAL A HA     1 
ATOM   7138 H HB     . VAL A 1 456 ? -9.07200  41.35700  17.44400 1.000 74.64384  ?  456 VAL A HB     1 
ATOM   7139 H HG11   . VAL A 1 456 ? -6.92000  41.23600  16.40900 1.000 73.50097  ?  456 VAL A HG11   1 
ATOM   7140 H HG12   . VAL A 1 456 ? -7.85800  39.98600  16.12300 1.000 73.50097  ?  456 VAL A HG12   1 
ATOM   7141 H HG13   . VAL A 1 456 ? -7.67800  41.11400  15.01900 1.000 73.50097  ?  456 VAL A HG13   1 
ATOM   7142 H HG21   . VAL A 1 456 ? -7.81000  43.31100  17.18800 1.000 75.90179  ?  456 VAL A HG21   1 
ATOM   7143 H HG22   . VAL A 1 456 ? -8.43000  43.52500  15.74200 1.000 75.90179  ?  456 VAL A HG22   1 
ATOM   7144 H HG23   . VAL A 1 456 ? -9.35500  43.64400  17.02800 1.000 75.90179  ?  456 VAL A HG23   1 
ATOM   7145 N N      . GLN A 1 457 ? -11.08000 39.34400  16.53100 1.000 59.36830  ?  457 GLN A N      1 
ATOM   7146 C CA     . GLN A 1 457 ? -11.44600 37.93300  16.42400 1.000 57.75076  ?  457 GLN A CA     1 
ATOM   7147 C C      . GLN A 1 457 ? -12.37200 37.69700  15.24000 1.000 61.19370  ?  457 GLN A C      1 
ATOM   7148 O O      . GLN A 1 457 ? -12.19400 36.73900  14.47700 1.000 58.66821  ?  457 GLN A O      1 
ATOM   7149 C CB     . GLN A 1 457 ? -12.11800 37.46300  17.71000 1.000 58.17925  ?  457 GLN A CB     1 
ATOM   7150 C CG     . GLN A 1 457 ? -11.24200 37.52600  18.94500 1.000 57.78419  ?  457 GLN A CG     1 
ATOM   7151 C CD     . GLN A 1 457 ? -11.90800 36.89800  20.15300 1.000 55.93823  ?  457 GLN A CD     1 
ATOM   7152 O OE1    . GLN A 1 457 ? -12.75900 36.02400  20.01800 1.000 57.41038  ?  457 GLN A OE1    1 
ATOM   7153 N NE2    . GLN A 1 457 ? -11.52400 37.34300  21.34300 1.000 60.62298  ?  457 GLN A NE2    1 
ATOM   7154 H H      . GLN A 1 457 ? -11.29500 39.71300  17.27800 1.000 71.35973  ?  457 GLN A H      1 
ATOM   7155 H HA     . GLN A 1 457 ? -10.63700 37.41500  16.29300 1.000 69.41868  ?  457 GLN A HA     1 
ATOM   7156 H HB2    . GLN A 1 457 ? -12.89400 38.02300  17.87400 1.000 69.93287  ?  457 GLN A HB2    1 
ATOM   7157 H HB3    . GLN A 1 457 ? -12.39400 36.54000  17.59500 1.000 69.93287  ?  457 GLN A HB3    1 
ATOM   7158 H HG2    . GLN A 1 457 ? -10.41600 37.04800  18.77300 1.000 69.45880  ?  457 GLN A HG2    1 
ATOM   7159 H HG3    . GLN A 1 457 ? -11.05200 38.45400  19.15300 1.000 69.45880  ?  457 GLN A HG3    1 
ATOM   7160 H HE21   . GLN A 1 457 ? -10.92500 37.95800  21.39900 1.000 72.86534  ?  457 GLN A HE21   1 
ATOM   7161 H HE22   . GLN A 1 457 ? -11.87400 37.01600  22.05800 1.000 72.86534  ?  457 GLN A HE22   1 
ATOM   7162 N N      . ARG A 1 458 ? -13.37900 38.56500  15.07900 1.000 68.53876  ?  458 ARG A N      1 
ATOM   7163 C CA     . ARG A 1 458 ? -14.30300 38.42700  13.95300 1.000 77.58352  ?  458 ARG A CA     1 
ATOM   7164 C C      . ARG A 1 458 ? -13.55500 38.53200  12.62900 1.000 67.24730  ?  458 ARG A C      1 
ATOM   7165 O O      . ARG A 1 458 ? -13.74600 37.71200  11.72700 1.000 69.12556  ?  458 ARG A O      1 
ATOM   7166 C CB     . ARG A 1 458 ? -15.38900 39.50800  14.02200 1.000 72.51875  ?  458 ARG A CB     1 
ATOM   7167 C CG     . ARG A 1 458 ? -16.53800 39.23400  14.98400 1.000 71.73341  ?  458 ARG A CG     1 
ATOM   7168 C CD     . ARG A 1 458 ? -17.39000 40.50200  15.15700 0.530 75.28027  ?  458 ARG A CD     1 
ATOM   7169 N NE     . ARG A 1 458 ? -18.00900 40.72700  16.46400 0.820 89.84419  ?  458 ARG A NE     1 
ATOM   7170 C CZ     . ARG A 1 458 ? -18.64700 39.82400  17.20200 0.430 81.39492  ?  458 ARG A CZ     1 
ATOM   7171 N NH1    . ARG A 1 458 ? -18.60500 38.53500  16.91300 1.000 94.32948  ?  458 ARG A NH1    1 
ATOM   7172 N NH2    . ARG A 1 458 ? -19.35400 40.22700  18.25500 0.810 83.43841  ?  458 ARG A NH2    1 
ATOM   7173 H H      . ARG A 1 458 ? -13.54500 39.23000  15.59900 1.000 82.36429  ?  458 ARG A H      1 
ATOM   7174 H HA     . ARG A 1 458 ? -14.73100 37.55800  14.00700 1.000 93.21799  ?  458 ARG A HA     1 
ATOM   7175 H HB2    . ARG A 1 458 ? -14.97300 40.33900  14.30100 1.000 87.14027  ?  458 ARG A HB2    1 
ATOM   7176 H HB3    . ARG A 1 458 ? -15.77300 39.61000  13.13700 1.000 87.14027  ?  458 ARG A HB3    1 
ATOM   7177 H HG2    . ARG A 1 458 ? -17.10000 38.52700  14.63000 1.000 86.19786  ?  458 ARG A HG2    1 
ATOM   7178 H HG3    . ARG A 1 458 ? -16.18600 38.97500  15.85000 1.000 86.19786  ?  458 ARG A HG3    1 
ATOM   7179 H HD2    . ARG A 1 458 ? -16.82200 41.26800  14.98100 1.000 90.45410  ?  458 ARG A HD2    1 
ATOM   7180 H HD3    . ARG A 1 458 ? -18.11100 40.46700  14.50900 1.000 90.45410  ?  458 ARG A HD3    1 
ATOM   7181 H HE     . ARG A 1 458 ? -17.95400 41.52200  16.78600 1.000 107.93080 ?  458 ARG A HE     1 
ATOM   7182 H HH11   . ARG A 1 458 ? -18.15600 38.26100  16.23200 1.000 113.31315 ?  458 ARG A HH11   1 
ATOM   7183 H HH12   . ARG A 1 458 ? -19.02600 37.97000  17.40600 1.000 113.31315 ?  458 ARG A HH12   1 
ATOM   7184 H HH21   . ARG A 1 458 ? -19.39500 41.06300  18.45100 1.000 100.24386 ?  458 ARG A HH21   1 
ATOM   7185 H HH22   . ARG A 1 458 ? -19.77100 39.65100  18.73900 1.000 100.24386 ?  458 ARG A HH22   1 
ATOM   7186 N N      . LYS A 1 459 ? -12.69700 39.54300  12.50000 1.000 65.47701  ?  459 LYS A N      1 
ATOM   7187 C CA     . LYS A 1 459 ? -11.95000 39.72600  11.26100 1.000 70.17537  ?  459 LYS A CA     1 
ATOM   7188 C C      . LYS A 1 459 ? -11.06500 38.52000  10.96800 1.000 66.04907  ?  459 LYS A C      1 
ATOM   7189 O O      . LYS A 1 459 ? -10.99400 38.05200  9.82300  1.000 61.60388  ?  459 LYS A O      1 
ATOM   7190 C CB     . LYS A 1 459 ? -11.10600 41.00300  11.35200 1.000 67.19464  ?  459 LYS A CB     1 
ATOM   7191 C CG     . LYS A 1 459 ? -10.88900 41.70500  10.02300 1.000 83.15754  ?  459 LYS A CG     1 
ATOM   7192 C CD     . LYS A 1 459 ? -9.72900  42.68800  10.09900 1.000 88.35260  ?  459 LYS A CD     1 
ATOM   7193 C CE     . LYS A 1 459 ? -8.87600  42.63700  8.83600  1.000 94.05253  ?  459 LYS A CE     1 
ATOM   7194 N NZ     . LYS A 1 459 ? -7.90300  43.77200  8.77400  1.000 96.60664  ?  459 LYS A NZ     1 
ATOM   7195 H H      . LYS A 1 459 ? -12.53100 40.12900  13.10800 1.000 78.69018  ?  459 LYS A H      1 
ATOM   7196 H HA     . LYS A 1 459 ? -12.57500 39.82500  10.52600 1.000 84.32822  ?  459 LYS A HA     1 
ATOM   7197 H HB2    . LYS A 1 459 ? -11.55200 41.62700  11.94500 1.000 80.75134  ?  459 LYS A HB2    1 
ATOM   7198 H HB3    . LYS A 1 459 ? -10.23300 40.77200  11.70800 1.000 80.75134  ?  459 LYS A HB3    1 
ATOM   7199 H HG2    . LYS A 1 459 ? -10.68700 41.04700  9.34000  1.000 99.90682  ?  459 LYS A HG2    1 
ATOM   7200 H HG3    . LYS A 1 459 ? -11.69100 42.19600  9.78500  1.000 99.90682  ?  459 LYS A HG3    1 
ATOM   7201 H HD2    . LYS A 1 459 ? -10.07700 43.58800  10.19700 1.000 106.14089 ?  459 LYS A HD2    1 
ATOM   7202 H HD3    . LYS A 1 459 ? -9.16700  42.46500  10.85700 1.000 106.14089 ?  459 LYS A HD3    1 
ATOM   7203 H HE2    . LYS A 1 459 ? -8.37400  41.80700  8.82300  1.000 112.98080 ?  459 LYS A HE2    1 
ATOM   7204 H HE3    . LYS A 1 459 ? -9.45300  42.69000  8.05800  1.000 112.98080 ?  459 LYS A HE3    1 
ATOM   7205 H HZ1    . LYS A 1 459 ? -7.42300  43.72100  8.02600  1.000 116.04574 ?  459 LYS A HZ1    1 
ATOM   7206 H HZ2    . LYS A 1 459 ? -8.33900  44.54800  8.78400  1.000 116.04574 ?  459 LYS A HZ2    1 
ATOM   7207 H HZ3    . LYS A 1 459 ? -7.35300  43.74100  9.47300  1.000 116.04574 ?  459 LYS A HZ3    1 
ATOM   7208 N N      . ALA A 1 460 ? -10.38800 38.00000  11.98900 1.000 60.63843  ?  460 ALA A N      1 
ATOM   7209 C CA     . ALA A 1 460 ? -9.49300  36.86800  11.80700 1.000 59.70339  ?  460 ALA A CA     1 
ATOM   7210 C C      . ALA A 1 460 ? -10.23400 35.55800  11.58900 1.000 59.03422  ?  460 ALA A C      1 
ATOM   7211 O O      . ALA A 1 460 ? -9.58100  34.53200  11.33100 1.000 60.27461  ?  460 ALA A O      1 
ATOM   7212 C CB     . ALA A 1 460 ? -8.55900  36.74400  13.02100 1.000 56.68412  ?  460 ALA A CB     1 
ATOM   7213 H H      . ALA A 1 460 ? -10.43200 38.28800  12.79800 1.000 72.88389  ?  460 ALA A H      1 
ATOM   7214 H HA     . ALA A 1 460 ? -8.94400  37.02700  11.02400 1.000 71.76183  ?  460 ALA A HA     1 
ATOM   7215 H HB1    . ALA A 1 460 ? -7.97000  35.98500  12.89000 1.000 68.13872  ?  460 ALA A HB1    1 
ATOM   7216 H HB2    . ALA A 1 460 ? -8.03700  37.55800  13.10200 1.000 68.13872  ?  460 ALA A HB2    1 
ATOM   7217 H HB3    . ALA A 1 460 ? -9.09400  36.61400  13.81900 1.000 68.13872  ?  460 ALA A HB3    1 
ATOM   7218 N N      . GLY A 1 461 ? -11.56300 35.55600  11.68000 1.000 62.94069  ?  461 GLY A N      1 
ATOM   7219 C CA     . GLY A 1 461 ? -12.30900 34.31500  11.54600 1.000 59.64717  ?  461 GLY A CA     1 
ATOM   7220 C C      . GLY A 1 461 ? -11.98900 33.30700  12.62900 1.000 60.50407  ?  461 GLY A C      1 
ATOM   7221 O O      . GLY A 1 461 ? -11.99500 32.09500  12.37100 1.000 62.04256  ?  461 GLY A O      1 
ATOM   7222 H H      . GLY A 1 461 ? -12.04800 36.25300  11.81700 1.000 75.64659  ?  461 GLY A H      1 
ATOM   7223 H HA2    . GLY A 1 461 ? -13.25900 34.51000  11.58600 1.000 71.69437  ?  461 GLY A HA2    1 
ATOM   7224 H HA3    . GLY A 1 461 ? -12.10500 33.91300  10.68800 1.000 71.69437  ?  461 GLY A HA3    1 
ATOM   7225 N N      . CYS A 1 462 ? -11.71400 33.77800  13.84400 1.000 59.45820  ?  462 CYS A N      1 
ATOM   7226 C CA     . CYS A 1 462 ? -11.38300 32.89800  14.96200 1.000 58.75113  ?  462 CYS A CA     1 
ATOM   7227 C C      . CYS A 1 462 ? -11.91500 33.55900  16.23400 1.000 57.90410  ?  462 CYS A C      1 
ATOM   7228 O O      . CYS A 1 462 ? -11.21400 34.33900  16.88100 1.000 54.43923  ?  462 CYS A O      1 
ATOM   7229 C CB     . CYS A 1 462 ? -9.88100  32.65200  15.04500 1.000 68.15646  ?  462 CYS A CB     1 
ATOM   7230 S SG     . CYS A 1 462 ? -9.40000  31.44800  16.29000 1.000 60.59234  ?  462 CYS A SG     1 
ATOM   7231 H H      . CYS A 1 462 ? -11.71300 34.61300  14.04900 1.000 71.46761  ?  462 CYS A H      1 
ATOM   7232 H HA     . CYS A 1 462 ? -11.83100 32.04500  14.84600 1.000 70.61912  ?  462 CYS A HA     1 
ATOM   7233 H HB2    . CYS A 1 462 ? -9.57200  32.32600  14.18500 1.000 81.90552  ?  462 CYS A HB2    1 
ATOM   7234 H HB3    . CYS A 1 462 ? -9.44100  33.49000  15.25900 1.000 81.90552  ?  462 CYS A HB3    1 
ATOM   7235 H HG     . CYS A 1 462 ? -8.21400  31.27400  16.22800 1.000 72.82858  ?  462 CYS A HG     1 
ATOM   7236 N N      . VAL A 1 463 ? -13.14200 33.21200  16.59300 1.000 55.79305  ?  463 VAL A N      1 
ATOM   7237 C CA     . VAL A 1 463 ? -13.77800 33.73700  17.79500 1.000 61.33689  ?  463 VAL A CA     1 
ATOM   7238 C C      . VAL A 1 463 ? -13.50300 32.75900  18.92500 1.000 57.72170  ?  463 VAL A C      1 
ATOM   7239 O O      . VAL A 1 463 ? -13.81500 31.56800  18.81600 1.000 56.64891  ?  463 VAL A O      1 
ATOM   7240 C CB     . VAL A 1 463 ? -15.28700 33.94600  17.59100 1.000 69.58812  ?  463 VAL A CB     1 
ATOM   7241 C CG1    . VAL A 1 463 ? -15.95900 34.32800  18.90500 1.000 57.71996  ?  463 VAL A CG1    1 
ATOM   7242 C CG2    . VAL A 1 463 ? -15.54600 35.01600  16.53400 1.000 62.46944  ?  463 VAL A CG2    1 
ATOM   7243 H H      . VAL A 1 463 ? -13.63700 32.66600  16.15000 1.000 67.06943  ?  463 VAL A H      1 
ATOM   7244 H HA     . VAL A 1 463 ? -13.39000 34.59600  18.02100 1.000 73.72203  ?  463 VAL A HA     1 
ATOM   7245 H HB     . VAL A 1 463 ? -15.67500 33.11300  17.28200 1.000 83.62351  ?  463 VAL A HB     1 
ATOM   7246 H HG11   . VAL A 1 463 ? -16.85700 34.64400  18.72000 1.000 69.38173  ?  463 VAL A HG11   1 
ATOM   7247 H HG12   . VAL A 1 463 ? -15.99400 33.54800  19.48000 1.000 69.38173  ?  463 VAL A HG12   1 
ATOM   7248 H HG13   . VAL A 1 463 ? -15.44300 35.03100  19.33000 1.000 69.38173  ?  463 VAL A HG13   1 
ATOM   7249 H HG21   . VAL A 1 463 ? -16.50200 35.15400  16.45200 1.000 75.08109  ?  463 VAL A HG21   1 
ATOM   7250 H HG22   . VAL A 1 463 ? -15.11500 35.84100  16.80800 1.000 75.08109  ?  463 VAL A HG22   1 
ATOM   7251 H HG23   . VAL A 1 463 ? -15.18000 34.71700  15.68700 1.000 75.08109  ?  463 VAL A HG23   1 
ATOM   7252 N N      . VAL A 1 464 ? -12.90900 33.26300  20.00900 1.000 55.12338  ?  464 VAL A N      1 
ATOM   7253 C CA     . VAL A 1 464 ? -12.60400 32.40800  21.14800 1.000 61.15154  ?  464 VAL A CA     1 
ATOM   7254 C C      . VAL A 1 464 ? -13.90600 31.89900  21.74600 1.000 62.12308  ?  464 VAL A C      1 
ATOM   7255 O O      . VAL A 1 464 ? -14.83400 32.67600  22.01000 1.000 59.40416  ?  464 VAL A O      1 
ATOM   7256 C CB     . VAL A 1 464 ? -11.75600 33.16800  22.17600 1.000 60.80612  ?  464 VAL A CB     1 
ATOM   7257 C CG1    . VAL A 1 464 ? -11.55900 32.34300  23.43500 1.000 56.40816  ?  464 VAL A CG1    1 
ATOM   7258 C CG2    . VAL A 1 464 ? -10.39800 33.54000  21.56400 1.000 59.50229  ?  464 VAL A CG2    1 
ATOM   7259 H H      . VAL A 1 464 ? -12.67800 34.08500  20.10600 1.000 66.26583  ?  464 VAL A H      1 
ATOM   7260 H HA     . VAL A 1 464 ? -12.08600 31.64400  20.84900 1.000 73.49962  ?  464 VAL A HA     1 
ATOM   7261 H HB     . VAL A 1 464 ? -12.22200 33.98200  22.42400 1.000 73.08512  ?  464 VAL A HB     1 
ATOM   7262 H HG11   . VAL A 1 464 ? -10.86700 32.75400  23.97700 1.000 67.80756  ?  464 VAL A HG11   1 
ATOM   7263 H HG12   . VAL A 1 464 ? -12.39400 32.31700  23.92900 1.000 67.80756  ?  464 VAL A HG12   1 
ATOM   7264 H HG13   . VAL A 1 464 ? -11.29400 31.44400  23.18600 1.000 67.80756  ?  464 VAL A HG13   1 
ATOM   7265 H HG21   . VAL A 1 464 ? -9.86300  33.99400  22.23400 1.000 71.52052  ?  464 VAL A HG21   1 
ATOM   7266 H HG22   . VAL A 1 464 ? -9.94900  32.73000  21.27400 1.000 71.52052  ?  464 VAL A HG22   1 
ATOM   7267 H HG23   . VAL A 1 464 ? -10.54300 34.12700  20.80500 1.000 71.52052  ?  464 VAL A HG23   1 
ATOM   7268 N N      . GLY A 1 465 ? -13.98300 30.58500  21.95100 1.000 62.16464  ?  465 GLY A N      1 
ATOM   7269 C CA     . GLY A 1 465 ? -15.17600 29.92800  22.41600 1.000 66.01803  ?  465 GLY A CA     1 
ATOM   7270 C C      . GLY A 1 465 ? -16.03100 29.32600  21.31700 1.000 64.28789  ?  465 GLY A C      1 
ATOM   7271 O O      . GLY A 1 465 ? -16.87500 28.47300  21.60400 1.000 63.31575  ?  465 GLY A O      1 
ATOM   7272 H H      . GLY A 1 465 ? -13.32800 30.04400  21.81900 1.000 74.71534  ?  465 GLY A H      1 
ATOM   7273 H HA2    . GLY A 1 465 ? -14.92300 29.21400  23.02200 1.000 79.33940  ?  465 GLY A HA2    1 
ATOM   7274 H HA3    . GLY A 1 465 ? -15.71900 30.57200  22.89700 1.000 79.33940  ?  465 GLY A HA3    1 
ATOM   7275 N N      . ARG A 1 466 ? -15.82800 29.74300  20.06900 1.000 64.10180  ?  466 ARG A N      1 
ATOM   7276 C CA     . ARG A 1 466 ? -16.55900 29.20000  18.92800 1.000 67.49324  ?  466 ARG A CA     1 
ATOM   7277 C C      . ARG A 1 466 ? -15.64300 28.40600  18.00200 1.000 64.47852  ?  466 ARG A C      1 
ATOM   7278 O O      . ARG A 1 466 ? -15.90400 27.23500  17.72900 1.000 54.69604  ?  466 ARG A O      1 
ATOM   7279 C CB     . ARG A 1 466 ? -17.23100 30.34100  18.16100 1.000 66.72146  ?  466 ARG A CB     1 
ATOM   7280 C CG     . ARG A 1 466 ? -17.73300 29.95500  16.77500 1.000 91.56256  ?  466 ARG A CG     1 
ATOM   7281 C CD     . ARG A 1 466 ? -18.44600 31.13000  16.09300 1.000 93.14731  ?  466 ARG A CD     1 
ATOM   7282 N NE     . ARG A 1 466 ? -17.64500 31.67800  15.00300 1.000 97.86699  ?  466 ARG A NE     1 
ATOM   7283 C CZ     . ARG A 1 466 ? -17.66500 32.94800  14.61400 1.000 98.94378  ?  466 ARG A CZ     1 
ATOM   7284 N NH1    . ARG A 1 466 ? -18.45600 33.83700  15.19100 1.000 78.39884  ?  466 ARG A NH1    1 
ATOM   7285 N NH2    . ARG A 1 466 ? -16.86600 33.33100  13.61900 1.000 95.90692  ?  466 ARG A NH2    1 
ATOM   7286 H H      . ARG A 1 466 ? -15.26100 30.35300  19.85500 1.000 77.03993  ?  466 ARG A H      1 
ATOM   7287 H HA     . ARG A 1 466 ? -17.25000 28.59900  19.24800 1.000 81.10965  ?  466 ARG A HA     1 
ATOM   7288 H HB2    . ARG A 1 466 ? -17.99400 30.65100  18.67400 1.000 80.18352  ?  466 ARG A HB2    1 
ATOM   7289 H HB3    . ARG A 1 466 ? -16.59000 31.06100  18.05200 1.000 80.18352  ?  466 ARG A HB3    1 
ATOM   7290 H HG2    . ARG A 1 466 ? -16.98100 29.69200  16.22200 1.000 109.99284 ?  466 ARG A HG2    1 
ATOM   7291 H HG3    . ARG A 1 466 ? -18.36100 29.22000  16.85300 1.000 109.99284 ?  466 ARG A HG3    1 
ATOM   7292 H HD2    . ARG A 1 466 ? -19.29200 30.82600  15.72800 1.000 111.89454 ?  466 ARG A HD2    1 
ATOM   7293 H HD3    . ARG A 1 466 ? -18.60000 31.83400  16.74300 1.000 111.89454 ?  466 ARG A HD3    1 
ATOM   7294 H HE     . ARG A 1 466 ? -17.12300 31.13900  14.58300 1.000 117.55816 ?  466 ARG A HE     1 
ATOM   7295 H HH11   . ARG A 1 466 ? -18.97500 33.59800  15.83400 1.000 94.19638  ?  466 ARG A HH11   1 
ATOM   7296 H HH12   . ARG A 1 466 ? -18.45300 34.65400  14.92200 1.000 94.19638  ?  466 ARG A HH12   1 
ATOM   7297 H HH21   . ARG A 1 466 ? -16.34800 32.76000  13.23900 1.000 115.20607 ?  466 ARG A HH21   1 
ATOM   7298 H HH22   . ARG A 1 466 ? -16.86900 34.15100  13.35700 1.000 115.20607 ?  466 ARG A HH22   1 
ATOM   7299 N N      . ASP A 1 467 ? -14.56300 29.02100  17.52000 1.000 61.96346  ?  467 ASP A N      1 
ATOM   7300 C CA     . ASP A 1 467 ? -13.62600 28.36700  16.62000 1.000 57.23573  ?  467 ASP A CA     1 
ATOM   7301 C C      . ASP A 1 467 ? -12.41700 27.79900  17.34400 1.000 52.62148  ?  467 ASP A C      1 
ATOM   7302 O O      . ASP A 1 467 ? -11.87100 26.78100  16.91500 1.000 54.88679  ?  467 ASP A O      1 
ATOM   7303 C CB     . ASP A 1 467 ? -13.14100 29.34900  15.54300 1.000 59.07661  ?  467 ASP A CB     1 
ATOM   7304 C CG     . ASP A 1 467 ? -14.28600 30.06500  14.84700 1.000 67.60565  ?  467 ASP A CG     1 
ATOM   7305 O OD1    . ASP A 1 467 ? -15.16800 29.37900  14.27400 1.000 65.40864  ?  467 ASP A OD1    1 
ATOM   7306 O OD2    . ASP A 1 467 ? -14.31500 31.30900  14.87400 1.000 64.48707  -1 467 ASP A OD2    1 
ATOM   7307 H H      . ASP A 1 467 ? -14.35100 29.83400  17.70500 1.000 74.47393  ?  467 ASP A H      1 
ATOM   7308 H HA     . ASP A 1 467 ? -14.08200 27.63800  16.17100 1.000 68.80065  ?  467 ASP A HA     1 
ATOM   7309 H HB2    . ASP A 1 467 ? -12.57500 30.01900  15.95700 1.000 71.00970  ?  467 ASP A HB2    1 
ATOM   7310 H HB3    . ASP A 1 467 ? -12.64000 28.86000  14.87100 1.000 71.00970  ?  467 ASP A HB3    1 
ATOM   7311 N N      . TYR A 1 468 ? -11.99200 28.43500  18.43000 1.000 54.57835  ?  468 TYR A N      1 
ATOM   7312 C CA     . TYR A 1 468 ? -10.85900 27.98400  19.22500 1.000 48.88284  ?  468 TYR A CA     1 
ATOM   7313 C C      . TYR A 1 468 ? -11.26100 28.12900  20.68400 1.000 50.09958  ?  468 TYR A C      1 
ATOM   7314 O O      . TYR A 1 468 ? -11.86500 29.15200  21.06000 1.000 53.51282  ?  468 TYR A O      1 
ATOM   7315 C CB     . TYR A 1 468 ? -9.59900  28.80200  18.91900 1.000 47.86812  ?  468 TYR A CB     1 
ATOM   7316 C CG     . TYR A 1 468 ? -8.37100  28.32700  19.65500 1.000 51.27608  ?  468 TYR A CG     1 
ATOM   7317 C CD1    . TYR A 1 468 ? -7.65900  27.20400  19.21900 1.000 52.62280  ?  468 TYR A CD1    1 
ATOM   7318 C CD2    . TYR A 1 468 ? -7.91700  28.98600  20.78500 1.000 50.23013  ?  468 TYR A CD2    1 
ATOM   7319 C CE1    . TYR A 1 468 ? -6.52200  26.77000  19.90200 1.000 47.58105  ?  468 TYR A CE1    1 
ATOM   7320 C CE2    . TYR A 1 468 ? -6.79100  28.55500  21.47100 1.000 48.90095  ?  468 TYR A CE2    1 
ATOM   7321 C CZ     . TYR A 1 468 ? -6.10300  27.44600  21.02600 1.000 41.19606  ?  468 TYR A CZ     1 
ATOM   7322 O OH     . TYR A 1 468 ? -4.99400  27.02600  21.71100 1.000 49.03362  ?  468 TYR A OH     1 
ATOM   7323 H H      . TYR A 1 468 ? -12.35600 29.15200  18.73400 1.000 65.61179  ?  468 TYR A H      1 
ATOM   7324 H HA     . TYR A 1 468 ? -10.64700 27.05500  19.04400 1.000 58.77717  ?  468 TYR A HA     1 
ATOM   7325 H HB2    . TYR A 1 468 ? -9.41400  28.74600  17.96900 1.000 57.55951  ?  468 TYR A HB2    1 
ATOM   7326 H HB3    . TYR A 1 468 ? -9.75700  29.72500  19.17300 1.000 57.55951  ?  468 TYR A HB3    1 
ATOM   7327 H HD1    . TYR A 1 468 ? -7.94800  26.74200  18.46500 1.000 63.26513  ?  468 TYR A HD1    1 
ATOM   7328 H HD2    . TYR A 1 468 ? -8.37700  29.73500  21.09100 1.000 60.39392  ?  468 TYR A HD2    1 
ATOM   7329 H HE1    . TYR A 1 468 ? -6.04900  26.02800  19.60000 1.000 57.21503  ?  468 TYR A HE1    1 
ATOM   7330 H HE2    . TYR A 1 468 ? -6.50100  29.01100  22.22800 1.000 58.79891  ?  468 TYR A HE2    1 
ATOM   7331 H HH     . TYR A 1 468 ? -4.84200  27.54300  22.35500 1.000 58.95811  ?  468 TYR A HH     1 
ATOM   7332 N N      . PRO A 1 469 ? -10.96600 27.14800  21.52500 1.000 51.26184  ?  469 PRO A N      1 
ATOM   7333 C CA     . PRO A 1 469 ? -11.46100 27.19000  22.91000 1.000 56.88742  ?  469 PRO A CA     1 
ATOM   7334 C C      . PRO A 1 469 ? -10.78000 28.28500  23.72300 1.000 57.41959  ?  469 PRO A C      1 
ATOM   7335 O O      . PRO A 1 469 ? -9.66900  28.73800  23.42900 1.000 53.97647  ?  469 PRO A O      1 
ATOM   7336 C CB     . PRO A 1 469 ? -11.11700 25.80300  23.46800 1.000 54.41296  ?  469 PRO A CB     1 
ATOM   7337 C CG     . PRO A 1 469 ? -9.99900  25.31300  22.61900 1.000 54.58896  ?  469 PRO A CG     1 
ATOM   7338 C CD     . PRO A 1 469 ? -10.22700 25.89300  21.24900 1.000 59.42251  ?  469 PRO A CD     1 
ATOM   7339 H HA     . PRO A 1 469 ? -12.42200 27.31900  22.92000 1.000 68.38267  ?  469 PRO A HA     1 
ATOM   7340 H HB2    . PRO A 1 469 ? -10.84200 25.87900  24.39500 1.000 65.41332  ?  469 PRO A HB2    1 
ATOM   7341 H HB3    . PRO A 1 469 ? -11.88800 25.21900  23.39800 1.000 65.41332  ?  469 PRO A HB3    1 
ATOM   7342 H HG2    . PRO A 1 469 ? -9.15500  25.61900  22.98500 1.000 65.62452  ?  469 PRO A HG2    1 
ATOM   7343 H HG3    . PRO A 1 469 ? -10.01500 24.34300  22.58800 1.000 65.62452  ?  469 PRO A HG3    1 
ATOM   7344 H HD2    . PRO A 1 469 ? -9.38300  26.07900  20.80900 1.000 71.42478  ?  469 PRO A HD2    1 
ATOM   7345 H HD3    . PRO A 1 469 ? -10.76000 25.29200  20.70500 1.000 71.42478  ?  469 PRO A HD3    1 
ATOM   7346 N N      . ALA A 1 470 ? -11.50400 28.73100  24.75600 1.000 53.57556  ?  470 ALA A N      1 
ATOM   7347 C CA     . ALA A 1 470 ? -10.92900 29.60100  25.76200 1.000 60.29398  ?  470 ALA A CA     1 
ATOM   7348 C C      . ALA A 1 470 ? -10.00200 28.78700  26.67100 1.000 62.13777  ?  470 ALA A C      1 
ATOM   7349 O O      . ALA A 1 470 ? -10.09800 27.56100  26.73300 1.000 57.99320  ?  470 ALA A O      1 
ATOM   7350 C CB     . ALA A 1 470 ? -12.03400 30.25300  26.58700 1.000 54.48134  ?  470 ALA A CB     1 
ATOM   7351 H H      . ALA A 1 470 ? -12.33200 28.53800  24.89000 1.000 64.40844  ?  470 ALA A H      1 
ATOM   7352 H HA     . ALA A 1 470 ? -10.41300 30.30800  25.34300 1.000 72.47054  ?  470 ALA A HA     1 
ATOM   7353 H HB1    . ALA A 1 470 ? -11.63200 30.83100  27.25300 1.000 65.49537  ?  470 ALA A HB1    1 
ATOM   7354 H HB2    . ALA A 1 470 ? -12.60300 30.77300  25.99700 1.000 65.49537  ?  470 ALA A HB2    1 
ATOM   7355 H HB3    . ALA A 1 470 ? -12.55500 29.55900  27.02100 1.000 65.49537  ?  470 ALA A HB3    1 
ATOM   7356 N N      . PRO A 1 471 ? -9.09700  29.45300  27.38900 1.000 65.90455  ?  471 PRO A N      1 
ATOM   7357 C CA     . PRO A 1 471 ? -8.17600  28.71300  28.26300 1.000 65.45580  ?  471 PRO A CA     1 
ATOM   7358 C C      . PRO A 1 471 ? -8.93800  27.86000  29.26400 1.000 64.10653  ?  471 PRO A C      1 
ATOM   7359 O O      . PRO A 1 471 ? -9.97800  28.26000  29.78100 1.000 62.97204  ?  471 PRO A O      1 
ATOM   7360 C CB     . PRO A 1 471 ? -7.37300  29.81800  28.96100 1.000 63.96453  ?  471 PRO A CB     1 
ATOM   7361 C CG     . PRO A 1 471 ? -7.54200  31.02400  28.11300 1.000 64.05107  ?  471 PRO A CG     1 
ATOM   7362 C CD     . PRO A 1 471 ? -8.87700  30.91300  27.44400 1.000 60.84452  ?  471 PRO A CD     1 
ATOM   7363 H HA     . PRO A 1 471 ? -7.57900  28.15500  27.74000 1.000 78.66473  ?  471 PRO A HA     1 
ATOM   7364 H HB2    . PRO A 1 471 ? -7.72700  29.96900  29.85100 1.000 76.87521  ?  471 PRO A HB2    1 
ATOM   7365 H HB3    . PRO A 1 471 ? -6.43900  29.56100  29.01400 1.000 76.87521  ?  471 PRO A HB3    1 
ATOM   7366 H HG2    . PRO A 1 471 ? -7.50700  31.81600  28.67100 1.000 76.97906  ?  471 PRO A HG2    1 
ATOM   7367 H HG3    . PRO A 1 471 ? -6.83300  31.05300  27.45100 1.000 76.97906  ?  471 PRO A HG3    1 
ATOM   7368 H HD2    . PRO A 1 471 ? -9.56600  31.34800  27.97100 1.000 73.13119  ?  471 PRO A HD2    1 
ATOM   7369 H HD3    . PRO A 1 471 ? -8.85100  31.29400  26.55300 1.000 73.13119  ?  471 PRO A HD3    1 
ATOM   7370 N N      . ILE A 1 472 ? -8.40100  26.66300  29.53000 1.000 64.51797  ?  472 ILE A N      1 
ATOM   7371 C CA     . ILE A 1 472 ? -9.06700  25.73600  30.44300 1.000 73.58645  ?  472 ILE A CA     1 
ATOM   7372 C C      . ILE A 1 472 ? -8.76600  26.01500  31.91000 1.000 69.44938  ?  472 ILE A C      1 
ATOM   7373 O O      . ILE A 1 472 ? -9.43900  25.46100  32.78400 1.000 76.32306  ?  472 ILE A O      1 
ATOM   7374 C CB     . ILE A 1 472 ? -8.68300  24.26900  30.15600 1.000 77.75592  ?  472 ILE A CB     1 
ATOM   7375 C CG1    . ILE A 1 472 ? -7.16700  24.12800  29.96200 1.000 76.43340  ?  472 ILE A CG1    1 
ATOM   7376 C CG2    . ILE A 1 472 ? -9.42000  23.76100  28.92900 1.000 80.90564  ?  472 ILE A CG2    1 
ATOM   7377 C CD1    . ILE A 1 472 ? -6.61200  22.81600  30.46100 1.000 79.61712  ?  472 ILE A CD1    1 
ATOM   7378 H H      . ILE A 1 472 ? -7.66300  26.37200  29.19800 1.000 77.53934  ?  472 ILE A H      1 
ATOM   7379 H HA     . ILE A 1 472 ? -10.01900 25.84600  30.29300 1.000 88.42151  ?  472 ILE A HA     1 
ATOM   7380 H HB     . ILE A 1 472 ? -8.94200  23.73500  30.92300 1.000 93.42487  ?  472 ILE A HB     1 
ATOM   7381 H HG12   . ILE A 1 472 ? -6.96500  24.19500  29.01600 1.000 91.83786  ?  472 ILE A HG12   1 
ATOM   7382 H HG13   . ILE A 1 472 ? -6.72200  24.84100  30.44700 1.000 91.83786  ?  472 ILE A HG13   1 
ATOM   7383 H HG21   . ILE A 1 472 ? -9.16700  22.83800  28.76800 1.000 97.20454  ?  472 ILE A HG21   1 
ATOM   7384 H HG22   . ILE A 1 472 ? -10.37500 23.81900  29.08800 1.000 97.20454  ?  472 ILE A HG22   1 
ATOM   7385 H HG23   . ILE A 1 472 ? -9.17800  24.30800  28.16600 1.000 97.20454  ?  472 ILE A HG23   1 
ATOM   7386 H HD11   . ILE A 1 472 ? -5.65500  22.79600  30.30300 1.000 95.65831  ?  472 ILE A HD11   1 
ATOM   7387 H HD12   . ILE A 1 472 ? -6.79200  22.73800  31.41200 1.000 95.65831  ?  472 ILE A HD12   1 
ATOM   7388 H HD13   . ILE A 1 472 ? -7.04100  22.08900  29.98300 1.000 95.65831  ?  472 ILE A HD13   1 
ATOM   7389 N N      . VAL A 1 473 ? -7.77400  26.85500  32.20400 1.000 67.59371  ?  473 VAL A N      1 
ATOM   7390 C CA     . VAL A 1 473 ? -7.42600  27.19600  33.57800 1.000 85.51154  ?  473 VAL A CA     1 
ATOM   7391 C C      . VAL A 1 473 ? -7.20900  28.70000  33.67100 1.000 78.98853  ?  473 VAL A C      1 
ATOM   7392 O O      . VAL A 1 473 ? -6.61100  29.30800  32.77600 1.000 77.15219  ?  473 VAL A O      1 
ATOM   7393 C CB     . VAL A 1 473 ? -6.17100  26.43100  34.05800 1.000 81.37547  ?  473 VAL A CB     1 
ATOM   7394 C CG1    . VAL A 1 473 ? -6.54700  25.01600  34.47600 1.000 85.15054  ?  473 VAL A CG1    1 
ATOM   7395 C CG2    . VAL A 1 473 ? -5.10700  26.41900  32.97400 1.000 81.12695  ?  473 VAL A CG2    1 
ATOM   7396 H H      . VAL A 1 473 ? -7.28400  27.24500  31.61400 1.000 81.23022  ?  473 VAL A H      1 
ATOM   7397 H HA     . VAL A 1 473 ? -8.16700  26.96000  34.15700 1.000 102.73161 ?  473 VAL A HA     1 
ATOM   7398 H HB     . VAL A 1 473 ? -5.79800  26.88200  34.83200 1.000 97.76833  ?  473 VAL A HB     1 
ATOM   7399 H HG11   . VAL A 1 473 ? -5.74700  24.55000  34.76600 1.000 102.29842 ?  473 VAL A HG11   1 
ATOM   7400 H HG12   . VAL A 1 473 ? -7.18600  25.06100  35.20400 1.000 102.29842 ?  473 VAL A HG12   1 
ATOM   7401 H HG13   . VAL A 1 473 ? -6.94100  24.55700  33.71800 1.000 102.29842 ?  473 VAL A HG13   1 
ATOM   7402 H HG21   . VAL A 1 473 ? -4.28800  26.05100  33.34000 1.000 97.47011  ?  473 VAL A HG21   1 
ATOM   7403 H HG22   . VAL A 1 473 ? -5.41500  25.87100  32.23500 1.000 97.47011  ?  473 VAL A HG22   1 
ATOM   7404 H HG23   . VAL A 1 473 ? -4.95600  27.32800  32.67000 1.000 97.47011  ?  473 VAL A HG23   1 
ATOM   7405 N N      . ASP A 1 474 ? -7.69600  29.29300  34.75700 1.000 86.08159  ?  474 ASP A N      1 
ATOM   7406 C CA     . ASP A 1 474 ? -7.57000  30.72800  34.98600 1.000 91.44848  ?  474 ASP A CA     1 
ATOM   7407 C C      . ASP A 1 474 ? -6.10800  31.17000  34.95300 1.000 92.53828  ?  474 ASP A C      1 
ATOM   7408 O O      . ASP A 1 474 ? -5.19700  30.35300  35.12000 1.000 92.38736  ?  474 ASP A O      1 
ATOM   7409 C CB     . ASP A 1 474 ? -8.20300  31.10800  36.33300 1.000 85.81597  ?  474 ASP A CB     1 
ATOM   7410 C CG     . ASP A 1 474 ? -9.06200  32.35600  36.24300 1.000 95.27405  ?  474 ASP A CG     1 
ATOM   7411 O OD1    . ASP A 1 474 ? -8.72800  33.24800  35.43200 1.000 99.26170  ?  474 ASP A OD1    1 
ATOM   7412 O OD2    . ASP A 1 474 ? -10.06700 32.45200  36.98800 1.000 94.55259  -1 474 ASP A OD2    1 
ATOM   7413 H H      . ASP A 1 474 ? -8.11100  28.87800  35.38600 1.000 103.41567 ?  474 ASP A H      1 
ATOM   7414 H HA     . ASP A 1 474 ? -8.04000  31.20200  34.28300 1.000 109.85595 ?  474 ASP A HA     1 
ATOM   7415 H HB2    . ASP A 1 474 ? -8.76500  30.37800  36.63600 1.000 103.09694 ?  474 ASP A HB2    1 
ATOM   7416 H HB3    . ASP A 1 474 ? -7.49800  31.27500  36.97800 1.000 103.09694 ?  474 ASP A HB3    1 
ATOM   7417 N N      . HIS A 1 475 ? -5.88900  32.46500  34.73800 1.000 81.87023  ?  475 HIS A N      1 
HETATM 7418 P PA     . FDA B 2 .   ? 19.14400  15.37200  19.25900 1.000 37.88420  ?  601 FDA A PA     1 
HETATM 7419 O O1A    . FDA B 2 .   ? 19.61400  15.44300  17.85200 1.000 37.40165  ?  601 FDA A O1A    1 
HETATM 7420 O O2A    . FDA B 2 .   ? 19.18700  16.59700  20.12600 1.000 45.62624  -1 601 FDA A O2A    1 
HETATM 7421 O O5B    . FDA B 2 .   ? 19.87000  14.13600  20.07800 1.000 37.53820  ?  601 FDA A O5B    1 
HETATM 7422 C C5B    . FDA B 2 .   ? 20.42300  13.07400  19.32700 1.000 37.40084  ?  601 FDA A C5B    1 
HETATM 7423 C C4B    . FDA B 2 .   ? 20.03100  11.74800  19.97400 1.000 39.87520  ?  601 FDA A C4B    1 
HETATM 7424 O O4B    . FDA B 2 .   ? 20.39800  11.72700  21.36000 1.000 39.54182  ?  601 FDA A O4B    1 
HETATM 7425 C C3B    . FDA B 2 .   ? 18.53100  11.49900  19.96800 1.000 34.88137  ?  601 FDA A C3B    1 
HETATM 7426 O O3B    . FDA B 2 .   ? 18.14500  10.86100  18.76500 1.000 37.65820  ?  601 FDA A O3B    1 
HETATM 7427 C C2B    . FDA B 2 .   ? 18.40100  10.51300  21.13800 1.000 40.89793  ?  601 FDA A C2B    1 
HETATM 7428 O O2B    . FDA B 2 .   ? 18.72500  9.17500   20.84100 1.000 40.54192  ?  601 FDA A O2B    1 
HETATM 7429 C C1B    . FDA B 2 .   ? 19.41200  11.09600  22.12500 1.000 40.74841  ?  601 FDA A C1B    1 
HETATM 7430 N N9A    . FDA B 2 .   ? 18.81900  12.06300  23.03500 1.000 42.67028  ?  601 FDA A N9A    1 
HETATM 7431 C C8A    . FDA B 2 .   ? 18.68300  13.41500  22.85500 1.000 39.61262  ?  601 FDA A C8A    1 
HETATM 7432 N N7A    . FDA B 2 .   ? 18.10300  14.00100  23.86600 1.000 43.74530  ?  601 FDA A N7A    1 
HETATM 7433 C C5A    . FDA B 2 .   ? 17.85500  12.99300  24.75900 1.000 37.85608  ?  601 FDA A C5A    1 
HETATM 7434 C C6A    . FDA B 2 .   ? 17.26200  12.96600  26.03800 1.000 44.29273  ?  601 FDA A C6A    1 
HETATM 7435 N N6A    . FDA B 2 .   ? 16.78500  14.05100  26.63700 1.000 38.44074  ?  601 FDA A N6A    1 
HETATM 7436 N N1A    . FDA B 2 .   ? 17.15900  11.78000  26.65100 1.000 42.58531  ?  601 FDA A N1A    1 
HETATM 7437 C C2A    . FDA B 2 .   ? 17.62700  10.69200  26.04800 1.000 41.74336  ?  601 FDA A C2A    1 
HETATM 7438 N N3A    . FDA B 2 .   ? 18.20900  10.58400  24.86600 1.000 43.07660  ?  601 FDA A N3A    1 
HETATM 7439 C C4A    . FDA B 2 .   ? 18.28700  11.77700  24.26000 1.000 40.52434  ?  601 FDA A C4A    1 
HETATM 7440 N N1     . FDA B 2 .   ? 13.61800  10.49300  23.49400 1.000 44.05109  ?  601 FDA A N1     1 
HETATM 7441 C C2     . FDA B 2 .   ? 13.53600  9.30800   22.79000 1.000 44.20780  ?  601 FDA A C2     1 
HETATM 7442 O O2     . FDA B 2 .   ? 14.43100  8.90400   22.08000 1.000 45.28502  ?  601 FDA A O2     1 
HETATM 7443 N N3     . FDA B 2 .   ? 12.35200  8.63000   22.95700 1.000 41.22608  ?  601 FDA A N3     1 
HETATM 7444 C C4     . FDA B 2 .   ? 11.27700  9.02700   23.75000 1.000 46.49990  ?  601 FDA A C4     1 
HETATM 7445 O O4     . FDA B 2 .   ? 10.26500  8.33200   23.82700 1.000 48.60873  ?  601 FDA A O4     1 
HETATM 7446 C C4X    . FDA B 2 .   ? 11.46600  10.27900  24.43600 1.000 41.92772  ?  601 FDA A C4X    1 
HETATM 7447 N N5     . FDA B 2 .   ? 10.43900  10.76000  25.25000 1.000 40.74120  ?  601 FDA A N5     1 
HETATM 7448 C C5X    . FDA B 2 .   ? 10.60800  11.95400  25.92200 1.000 45.62757  ?  601 FDA A C5X    1 
HETATM 7449 C C6     . FDA B 2 .   ? 9.60000   12.46100  26.73800 1.000 46.97120  ?  601 FDA A C6     1 
HETATM 7450 C C7     . FDA B 2 .   ? 9.74600   13.66400  27.42000 1.000 43.74236  ?  601 FDA A C7     1 
HETATM 7451 C C7M    . FDA B 2 .   ? 8.62200   14.15800  28.28800 1.000 48.68791  ?  601 FDA A C7M    1 
HETATM 7452 C C8     . FDA B 2 .   ? 10.92700  14.39200  27.27000 1.000 43.58143  ?  601 FDA A C8     1 
HETATM 7453 C C8M    . FDA B 2 .   ? 11.16000  15.70100  27.98200 1.000 45.05468  ?  601 FDA A C8M    1 
HETATM 7454 C C9     . FDA B 2 .   ? 11.92600  13.87800  26.46000 1.000 45.20259  ?  601 FDA A C9     1 
HETATM 7455 C C9A    . FDA B 2 .   ? 11.79700  12.67400  25.77200 1.000 43.72464  ?  601 FDA A C9A    1 
HETATM 7456 N N10    . FDA B 2 .   ? 12.83900  12.18200  24.94300 1.000 40.63540  ?  601 FDA A N10    1 
HETATM 7457 C C10    . FDA B 2 .   ? 12.62500  10.97700  24.29700 1.000 43.82029  ?  601 FDA A C10    1 
HETATM 7458 C "C1'"  . FDA B 2 .   ? 14.12800  12.90300  24.80500 1.000 39.57975  ?  601 FDA A "C1'"  1 
HETATM 7459 C "C2'"  . FDA B 2 .   ? 14.21400  13.96800  23.69800 1.000 40.67180  ?  601 FDA A "C2'"  1 
HETATM 7460 O "O2'"  . FDA B 2 .   ? 13.18100  14.91700  23.78000 1.000 42.73432  ?  601 FDA A "O2'"  1 
HETATM 7461 C "C3'"  . FDA B 2 .   ? 14.39400  13.29000  22.32800 1.000 37.15301  ?  601 FDA A "C3'"  1 
HETATM 7462 O "O3'"  . FDA B 2 .   ? 15.36500  12.27700  22.40900 1.000 40.47005  ?  601 FDA A "O3'"  1 
HETATM 7463 C "C4'"  . FDA B 2 .   ? 14.69300  14.33700  21.23900 1.000 38.19205  ?  601 FDA A "C4'"  1 
HETATM 7464 O "O4'"  . FDA B 2 .   ? 13.65700  15.31000  21.21100 1.000 37.56072  ?  601 FDA A "O4'"  1 
HETATM 7465 C "C5'"  . FDA B 2 .   ? 14.91600  13.67200  19.90200 1.000 38.55005  ?  601 FDA A "C5'"  1 
HETATM 7466 O "O5'"  . FDA B 2 .   ? 15.24800  14.69700  18.98700 1.000 42.39320  ?  601 FDA A "O5'"  1 
HETATM 7467 P P      . FDA B 2 .   ? 16.58700  14.46400  18.08600 1.000 38.03841  ?  601 FDA A P      1 
HETATM 7468 O O1P    . FDA B 2 .   ? 16.64600  15.58700  17.09600 1.000 40.95464  -1 601 FDA A O1P    1 
HETATM 7469 O O2P    . FDA B 2 .   ? 16.66400  13.06300  17.61900 1.000 37.35782  ?  601 FDA A O2P    1 
HETATM 7470 O O3P    . FDA B 2 .   ? 17.62600  14.69600  19.34900 1.000 36.39033  ?  601 FDA A O3P    1 
HETATM 7471 H H51A   . FDA B 2 .   ? 20.10300  13.09400  18.41100 1.000 44.99878  ?  601 FDA A H51A   1 
HETATM 7472 H H52A   . FDA B 2 .   ? 21.38900  13.14300  19.28900 1.000 44.99878  ?  601 FDA A H52A   1 
HETATM 7473 H H4B    . FDA B 2 .   ? 20.50200  11.03800  19.51100 1.000 47.96801  ?  601 FDA A H4B    1 
HETATM 7474 H H3B    . FDA B 2 .   ? 18.04400  12.32500  20.10800 1.000 41.97541  ?  601 FDA A H3B    1 
HETATM 7475 H HO3A   . FDA B 2 .   ? 17.38800  11.16300  18.54700 1.000 45.30761  ?  601 FDA A HO3A   1 
HETATM 7476 H H2B    . FDA B 2 .   ? 17.50800  10.57900  21.51000 1.000 49.19529  ?  601 FDA A H2B    1 
HETATM 7477 H HO2A   . FDA B 2 .   ? 18.46500  8.68700   21.48600 1.000 48.76807  ?  601 FDA A HO2A   1 
HETATM 7478 H H1B    . FDA B 2 .   ? 19.79600  10.39100  22.67000 1.000 49.01586  ?  601 FDA A H1B    1 
HETATM 7479 H H8A    . FDA B 2 .   ? 18.97700  13.85400  22.08900 1.000 47.65292  ?  601 FDA A H8A    1 
HETATM 7480 H H61A   . FDA B 2 .   ? 16.58000  14.03200  27.47100 1.000 46.24666  ?  601 FDA A H61A   1 
HETATM 7481 H H62A   . FDA B 2 .   ? 16.67800  14.79000  26.20500 1.000 46.24666  ?  601 FDA A H62A   1 
HETATM 7482 H H2A    . FDA B 2 .   ? 17.53000  9.90100   26.52700 1.000 50.20980  ?  601 FDA A H2A    1 
HETATM 7483 H HN3    . FDA B 2 .   ? 12.27100  7.88900   22.52900 1.000 49.58906  ?  601 FDA A HN3    1 
HETATM 7484 H HN5    . FDA B 2 .   ? 9.64000   10.68000  24.86500 1.000 49.00720  ?  601 FDA A HN5    1 
HETATM 7485 H H6     . FDA B 2 .   ? 8.81000   11.97700  26.82600 1.000 56.48321  ?  601 FDA A H6     1 
HETATM 7486 H HM71   . FDA B 2 .   ? 8.95600   14.61800  29.07500 1.000 58.54326  ?  601 FDA A HM71   1 
HETATM 7487 H HM72   . FDA B 2 .   ? 8.05100   14.77900  27.81100 1.000 58.54326  ?  601 FDA A HM72   1 
HETATM 7488 H HM73   . FDA B 2 .   ? 8.06300   13.42800  28.59600 1.000 58.54326  ?  601 FDA A HM73   1 
HETATM 7489 H HM81   . FDA B 2 .   ? 12.07700  16.00200  27.88900 1.000 54.18339  ?  601 FDA A HM81   1 
HETATM 7490 H HM82   . FDA B 2 .   ? 10.59100  16.40500  27.63400 1.000 54.18339  ?  601 FDA A HM82   1 
HETATM 7491 H HM83   . FDA B 2 .   ? 10.97800  15.63000  28.93200 1.000 54.18339  ?  601 FDA A HM83   1 
HETATM 7492 H H9     . FDA B 2 .   ? 12.71700  14.35900  26.37300 1.000 54.36088  ?  601 FDA A H9     1 
HETATM 7493 H "H1'1" . FDA B 2 .   ? 14.33700  13.32400  25.65400 1.000 47.61346  ?  601 FDA A "H1'1" 1 
HETATM 7494 H "H1'2" . FDA B 2 .   ? 14.83100  12.25000  24.66000 1.000 47.61346  ?  601 FDA A "H1'2" 1 
HETATM 7495 H "H2'"  . FDA B 2 .   ? 15.01400  14.49500  23.85200 1.000 48.92393  ?  601 FDA A "H2'"  1 
HETATM 7496 H "HO2'" . FDA B 2 .   ? 13.28500  15.50200  23.17400 1.000 51.39896  ?  601 FDA A "HO2'" 1 
HETATM 7497 H "H3'"  . FDA B 2 .   ? 13.58900  12.80500  22.09000 1.000 44.70138  ?  601 FDA A "H3'"  1 
HETATM 7498 H "HO3'" . FDA B 2 .   ? 15.32900  11.79800  21.70600 1.000 48.68183  ?  601 FDA A "HO3'" 1 
HETATM 7499 H "H4'"  . FDA B 2 .   ? 15.49800  14.83700  21.44800 1.000 45.94824  ?  601 FDA A "H4'"  1 
HETATM 7500 H "HO4'" . FDA B 2 .   ? 13.86000  15.89400  20.62500 1.000 45.19064  ?  601 FDA A "HO4'" 1 
HETATM 7501 H "H5'1" . FDA B 2 .   ? 15.62600  13.01500  19.97400 1.000 46.37783  ?  601 FDA A "H5'1" 1 
HETATM 7502 H "H5'2" . FDA B 2 .   ? 14.11300  13.19900  19.63100 1.000 46.37783  ?  601 FDA A "H5'2" 1 
HETATM 7503 O O      . HOH C 3 .   ? 15.87800  11.05200  5.75300  1.000 55.42302  ?  701 HOH A O      1 
HETATM 7504 O O      . HOH C 3 .   ? 17.49800  -2.83800  23.70600 1.000 51.45196  ?  702 HOH A O      1 
HETATM 7505 O O      . HOH C 3 .   ? 4.53500   -2.14100  4.64100  1.000 60.12828  ?  703 HOH A O      1 
HETATM 7506 O O      . HOH C 3 .   ? 14.00200  -6.90500  21.41300 1.000 54.43297  ?  704 HOH A O      1 
HETATM 7507 O O      . HOH C 3 .   ? 20.09400  -15.21400 3.78200  1.000 55.65722  ?  705 HOH A O      1 
HETATM 7508 O O      . HOH C 3 .   ? 3.68000   37.66700  19.41900 1.000 51.30080  ?  706 HOH A O      1 
HETATM 7509 O O      . HOH C 3 .   ? 14.16800  1.15100   26.16400 1.000 55.15510  ?  707 HOH A O      1 
HETATM 7510 O O      . HOH C 3 .   ? 32.43300  -20.66400 11.61700 1.000 61.13215  ?  708 HOH A O      1 
HETATM 7511 O O      . HOH C 3 .   ? 14.62400  0.12900   42.00900 1.000 84.47791  ?  709 HOH A O      1 
HETATM 7512 O O      . HOH C 3 .   ? 18.35900  -1.75100  4.78400  1.000 42.20470  ?  710 HOH A O      1 
HETATM 7513 O O      . HOH C 3 .   ? 13.38600  -26.40700 20.24000 1.000 50.15887  ?  711 HOH A O      1 
HETATM 7514 O O      . HOH C 3 .   ? 18.37500  -24.81200 5.65900  1.000 50.25756  ?  712 HOH A O      1 
HETATM 7515 O O      . HOH C 3 .   ? 31.99500  -8.41900  6.00000  1.000 62.86453  ?  713 HOH A O      1 
HETATM 7516 O O      . HOH C 3 .   ? 17.14800  -9.85100  26.16400 1.000 58.93906  ?  714 HOH A O      1 
HETATM 7517 O O      . HOH C 3 .   ? 13.03000  22.32400  15.94200 1.000 44.38924  ?  715 HOH A O      1 
HETATM 7518 O O      . HOH C 3 .   ? 16.73400  27.28500  23.48100 1.000 43.91497  ?  716 HOH A O      1 
HETATM 7519 O O      . HOH C 3 .   ? 2.12600   10.05700  16.07600 1.000 45.56647  ?  717 HOH A O      1 
HETATM 7520 O O      . HOH C 3 .   ? 22.21600  -23.09700 22.92000 1.000 49.88449  ?  718 HOH A O      1 
HETATM 7521 O O      . HOH C 3 .   ? 38.67900  7.58500   12.94900 1.000 83.80486  ?  719 HOH A O      1 
HETATM 7522 O O      . HOH C 3 .   ? 31.06400  16.53800  23.37500 1.000 40.12275  ?  720 HOH A O      1 
HETATM 7523 O O      . HOH C 3 .   ? 22.34000  0.13500   38.89000 1.000 67.13299  ?  721 HOH A O      1 
HETATM 7524 O O      . HOH C 3 .   ? 29.76800  -2.55300  17.11600 1.000 50.67620  ?  722 HOH A O      1 
HETATM 7525 O O      . HOH C 3 .   ? 16.66800  -12.62700 -3.22500 1.000 59.17469  ?  723 HOH A O      1 
HETATM 7526 O O      . HOH C 3 .   ? 21.83900  -28.62300 9.47200  1.000 60.95508  ?  724 HOH A O      1 
HETATM 7527 O O      . HOH C 3 .   ? 22.31500  -4.51600  22.28700 1.000 42.71995  ?  725 HOH A O      1 
HETATM 7528 O O      . HOH C 3 .   ? 12.03100  -28.15500 21.84500 1.000 58.38901  ?  726 HOH A O      1 
HETATM 7529 O O      . HOH C 3 .   ? -0.80100  24.38300  8.01100  1.000 61.27797  ?  727 HOH A O      1 
HETATM 7530 O O      . HOH C 3 .   ? 7.04000   6.95800   8.27500  1.000 52.24809  ?  728 HOH A O      1 
HETATM 7531 O O      . HOH C 3 .   ? 21.11100  6.20200   2.59400  1.000 45.33441  ?  729 HOH A O      1 
HETATM 7532 O O      . HOH C 3 .   ? 8.71000   34.81600  14.55500 1.000 53.66317  ?  730 HOH A O      1 
HETATM 7533 O O      . HOH C 3 .   ? 14.64300  1.08800   21.39200 1.000 45.45430  ?  731 HOH A O      1 
HETATM 7534 O O      . HOH C 3 .   ? 28.65800  18.80900  19.51700 1.000 43.03211  ?  732 HOH A O      1 
HETATM 7535 O O      . HOH C 3 .   ? 6.45100   -11.55100 20.83100 1.000 72.69886  ?  733 HOH A O      1 
HETATM 7536 O O      . HOH C 3 .   ? 30.10500  -10.56000 14.72500 1.000 46.50435  ?  734 HOH A O      1 
HETATM 7537 O O      . HOH C 3 .   ? 15.93600  7.51100   20.43100 1.000 42.46946  ?  735 HOH A O      1 
HETATM 7538 O O      . HOH C 3 .   ? 8.94700   2.47100   30.60900 1.000 71.26860  ?  736 HOH A O      1 
HETATM 7539 O O      . HOH C 3 .   ? 9.63100   21.17600  15.03900 1.000 46.17511  ?  737 HOH A O      1 
HETATM 7540 O O      . HOH C 3 .   ? 14.13900  11.57200  7.73600  1.000 53.81997  ?  738 HOH A O      1 
HETATM 7541 O O      . HOH C 3 .   ? 10.84200  0.61300   23.73300 1.000 50.69477  ?  739 HOH A O      1 
HETATM 7542 O O      . HOH C 3 .   ? 4.59500   -16.86900 8.46000  1.000 43.69378  ?  740 HOH A O      1 
HETATM 7543 O O      . HOH C 3 .   ? 10.85500  1.45500   3.32200  1.000 52.81431  ?  741 HOH A O      1 
HETATM 7544 O O      . HOH C 3 .   ? 17.02700  -6.94200  18.18100 1.000 42.67050  ?  742 HOH A O      1 
HETATM 7545 O O      . HOH C 3 .   ? -12.06800 16.64800  21.33300 1.000 56.03894  ?  743 HOH A O      1 
HETATM 7546 O O      . HOH C 3 .   ? 29.02900  -1.44000  9.13700  1.000 44.58219  ?  744 HOH A O      1 
HETATM 7547 O O      . HOH C 3 .   ? 4.65700   29.61900  17.29500 1.000 48.17927  ?  745 HOH A O      1 
HETATM 7548 O O      . HOH C 3 .   ? 20.30700  2.06400   17.39000 1.000 42.85339  ?  746 HOH A O      1 
HETATM 7549 O O      . HOH C 3 .   ? 27.46700  -5.13900  9.91900  1.000 44.82020  ?  747 HOH A O      1 
HETATM 7550 O O      . HOH C 3 .   ? 21.42600  -7.65500  30.09900 1.000 68.91326  ?  748 HOH A O      1 
HETATM 7551 O O      . HOH C 3 .   ? 18.33400  16.56300  25.76600 1.000 41.84176  ?  749 HOH A O      1 
HETATM 7552 O O      . HOH C 3 .   ? 23.46400  5.57700   23.67500 1.000 40.90893  ?  750 HOH A O      1 
HETATM 7553 O O      . HOH C 3 .   ? 13.48900  -29.98000 5.96200  1.000 60.19546  ?  751 HOH A O      1 
HETATM 7554 O O      . HOH C 3 .   ? 25.79000  0.53700   18.03900 1.000 46.55766  ?  752 HOH A O      1 
HETATM 7555 O O      . HOH C 3 .   ? 0.07400   29.96400  23.81100 1.000 46.92326  ?  753 HOH A O      1 
HETATM 7556 O O      . HOH C 3 .   ? 22.83000  1.21700   17.81600 1.000 40.42706  ?  754 HOH A O      1 
HETATM 7557 O O      . HOH C 3 .   ? 9.70100   -13.22600 2.48900  1.000 48.22040  ?  755 HOH A O      1 
HETATM 7558 O O      . HOH C 3 .   ? 34.277    0.402     11.481   1.000 69.66432  ?  756 HOH A O      1 
HETATM 7559 O O      . HOH C 3 .   ? 21.15100  -28.87700 6.39400  1.000 65.28791  ?  757 HOH A O      1 
HETATM 7560 O O      . HOH C 3 .   ? 11.11100  -10.21200 15.80900 1.000 38.51983  ?  758 HOH A O      1 
HETATM 7561 O O      . HOH C 3 .   ? -7.68800  30.81300  24.04800 1.000 49.68780  ?  759 HOH A O      1 
HETATM 7562 O O      . HOH C 3 .   ? 33.45300  13.93100  28.37900 1.000 57.75765  ?  760 HOH A O      1 
HETATM 7563 O O      . HOH C 3 .   ? 19.67600  -1.54100  17.45800 1.000 39.40226  ?  761 HOH A O      1 
HETATM 7564 O O      . HOH C 3 .   ? 18.68000  -8.50600  16.29200 1.000 39.80837  ?  762 HOH A O      1 
HETATM 7565 O O      . HOH C 3 .   ? 35.52700  12.12200  26.47300 1.000 63.77728  ?  763 HOH A O      1 
HETATM 7566 O O      . HOH C 3 .   ? 8.94100   20.88800  18.01200 1.000 44.62594  ?  764 HOH A O      1 
HETATM 7567 O O      . HOH C 3 .   ? 18.21200  -5.25000  20.21400 1.000 44.46041  ?  765 HOH A O      1 
HETATM 7568 O O      . HOH C 3 .   ? 4.88900   -18.97000 11.08600 1.000 67.17063  ?  766 HOH A O      1 
HETATM 7569 O O      . HOH C 3 .   ? 20.10800  24.21400  15.42800 1.000 46.75331  ?  767 HOH A O      1 
HETATM 7570 O O      . HOH C 3 .   ? 15.61600  -0.68200  8.29000  1.000 41.69703  ?  768 HOH A O      1 
HETATM 7571 O O      . HOH C 3 .   ? 20.63300  -1.17300  28.97100 1.000 52.54954  ?  769 HOH A O      1 
HETATM 7572 O O      . HOH C 3 .   ? 31.89000  3.91200   18.27200 1.000 47.51356  ?  770 HOH A O      1 
HETATM 7573 O O      . HOH C 3 .   ? 36.05200  7.92500   14.66800 1.000 58.48059  ?  771 HOH A O      1 
HETATM 7574 O O      . HOH C 3 .   ? 23.90100  -7.27300  16.27300 1.000 44.47316  ?  772 HOH A O      1 
HETATM 7575 O O      . HOH C 3 .   ? 20.81700  -21.91900 24.32400 1.000 51.23182  ?  773 HOH A O      1 
HETATM 7576 O O      . HOH C 3 .   ? 8.07300   -8.34800  1.67200  1.000 49.19257  ?  774 HOH A O      1 
HETATM 7577 O O      . HOH C 3 .   ? -7.21500  33.08800  12.06300 1.000 51.69509  ?  775 HOH A O      1 
HETATM 7578 O O      . HOH C 3 .   ? 34.53500  8.70100   23.91400 1.000 45.20395  ?  776 HOH A O      1 
HETATM 7579 O O      . HOH C 3 .   ? 29.405    -14.375   1.289    1.000 49.46963  ?  777 HOH A O      1 
HETATM 7580 O O      . HOH C 3 .   ? 26.96800  -24.51200 13.09000 1.000 62.90031  ?  778 HOH A O      1 
HETATM 7581 O O      . HOH C 3 .   ? 30.60400  22.79500  26.16800 1.000 49.33050  ?  779 HOH A O      1 
HETATM 7582 O O      . HOH C 3 .   ? 16.72600  -0.48600  0.57900  1.000 62.13607  ?  780 HOH A O      1 
HETATM 7583 O O      . HOH C 3 .   ? 27.30200  -10.85100 24.56400 1.000 66.62086  ?  781 HOH A O      1 
HETATM 7584 O O      . HOH C 3 .   ? 29.93900  -20.56900 12.75900 1.000 55.48840  ?  782 HOH A O      1 
HETATM 7585 O O      . HOH C 3 .   ? -0.81400  9.47200   16.02900 1.000 49.50631  ?  783 HOH A O      1 
HETATM 7586 O O      . HOH C 3 .   ? 8.65300   28.87000  13.54100 1.000 48.30696  ?  784 HOH A O      1 
HETATM 7587 O O      . HOH C 3 .   ? 16.81600  4.81200   21.46800 1.000 39.64085  ?  785 HOH A O      1 
HETATM 7588 O O      . HOH C 3 .   ? 13.68700  17.82200  7.80900  1.000 71.77324  ?  786 HOH A O      1 
HETATM 7589 O O      . HOH C 3 .   ? 24.64200  -5.95100  28.52100 1.000 67.32421  ?  787 HOH A O      1 
HETATM 7590 O O      . HOH C 3 .   ? 27.52900  -18.83600 22.04700 1.000 66.98769  ?  788 HOH A O      1 
HETATM 7591 O O      . HOH C 3 .   ? 4.79500   6.09400   9.39000  1.000 48.39693  ?  789 HOH A O      1 
HETATM 7592 O O      . HOH C 3 .   ? 26.75000  -14.62000 22.63800 1.000 52.93023  ?  790 HOH A O      1 
HETATM 7593 O O      . HOH C 3 .   ? 32.63000  12.47100  10.74000 1.000 55.43828  ?  791 HOH A O      1 
HETATM 7594 O O      . HOH C 3 .   ? 0.50200   42.02300  15.54300 1.000 52.95365  ?  792 HOH A O      1 
HETATM 7595 O O      . HOH C 3 .   ? 16.76000  -4.42300  -3.87800 1.000 59.98757  ?  793 HOH A O      1 
HETATM 7596 O O      . HOH C 3 .   ? 9.208     -28.661   11.913   1.000 52.76893  ?  794 HOH A O      1 
HETATM 7597 O O      . HOH C 3 .   ? -11.57900 22.53500  25.68600 1.000 46.45384  ?  795 HOH A O      1 
HETATM 7598 O O      . HOH C 3 .   ? 1.65800   15.88900  7.63700  1.000 57.40323  ?  796 HOH A O      1 
HETATM 7599 O O      . HOH C 3 .   ? 5.86600   -18.81300 8.00400  1.000 53.99018  ?  797 HOH A O      1 
HETATM 7600 O O      . HOH C 3 .   ? 15.06700  17.72100  20.17800 1.000 37.89064  ?  798 HOH A O      1 
HETATM 7601 O O      . HOH C 3 .   ? 33.36800  6.16100   18.78200 1.000 41.63989  ?  799 HOH A O      1 
HETATM 7602 O O      . HOH C 3 .   ? 22.48200  -3.27900  24.89900 1.000 46.60324  ?  800 HOH A O      1 
HETATM 7603 O O      . HOH C 3 .   ? 24.21000  -21.43800 22.93600 1.000 49.20447  ?  801 HOH A O      1 
HETATM 7604 O O      . HOH C 3 .   ? 2.28600   0.02800   42.99100 1.000 73.11295  ?  802 HOH A O      1 
HETATM 7605 O O      . HOH C 3 .   ? 33.17500  -5.28200  4.89400  1.000 57.20593  ?  803 HOH A O      1 
HETATM 7606 O O      . HOH C 3 .   ? 31.44800  7.75700   24.95300 1.000 45.44245  ?  804 HOH A O      1 
HETATM 7607 O O      . HOH C 3 .   ? 14.94200  3.77900   4.51200  1.000 51.07964  ?  805 HOH A O      1 
HETATM 7608 O O      . HOH C 3 .   ? 1.48600   1.28500   23.83800 1.000 74.77370  ?  806 HOH A O      1 
HETATM 7609 O O      . HOH C 3 .   ? 31.93700  -17.34300 5.28300  1.000 52.93258  ?  807 HOH A O      1 
HETATM 7610 O O      . HOH C 3 .   ? 12.15800  10.99800  5.96100  1.000 51.99896  ?  808 HOH A O      1 
HETATM 7611 O O      . HOH C 3 .   ? 25.35500  24.38000  16.60600 1.000 52.54134  ?  809 HOH A O      1 
HETATM 7612 O O      . HOH C 3 .   ? 0.39000   36.93800  21.78500 1.000 54.38410  ?  810 HOH A O      1 
HETATM 7613 O O      . HOH C 3 .   ? 9.29600   37.91100  21.43700 1.000 58.04482  ?  811 HOH A O      1 
HETATM 7614 O O      . HOH C 3 .   ? 20.17300  -7.10000  14.25500 1.000 38.27301  ?  812 HOH A O      1 
HETATM 7615 O O      . HOH C 3 .   ? 24.38100  -0.11900  5.06700  1.000 55.87409  ?  813 HOH A O      1 
HETATM 7616 O O      . HOH C 3 .   ? -4.97700  34.90700  4.41500  1.000 73.06791  ?  814 HOH A O      1 
HETATM 7617 O O      . HOH C 3 .   ? 39.62100  18.43500  19.85000 1.000 55.52014  ?  815 HOH A O      1 
HETATM 7618 O O      . HOH C 3 .   ? 18.29100  26.43500  16.81900 1.000 44.29261  ?  816 HOH A O      1 
HETATM 7619 O O      . HOH C 3 .   ? 31.39700  -1.95200  25.74500 1.000 48.53377  ?  817 HOH A O      1 
HETATM 7620 O O      . HOH C 3 .   ? 22.14500  -5.01800  14.71400 1.000 43.41269  ?  818 HOH A O      1 
HETATM 7621 O O      . HOH C 3 .   ? 31.88400  -8.97500  0.22400  1.000 52.11144  ?  819 HOH A O      1 
HETATM 7622 O O      . HOH C 3 .   ? -3.42500  5.46900   14.93600 1.000 56.29064  ?  820 HOH A O      1 
HETATM 7623 O O      . HOH C 3 .   ? 23.68200  -3.76300  27.06300 1.000 55.45842  ?  821 HOH A O      1 
HETATM 7624 O O      . HOH C 3 .   ? 7.01300   1.97700   27.62300 1.000 77.11002  ?  822 HOH A O      1 
HETATM 7625 O O      . HOH C 3 .   ? 12.92400  26.01300  10.13400 1.000 54.00552  ?  823 HOH A O      1 
HETATM 7626 O O      . HOH C 3 .   ? 36.45500  24.46600  17.06500 1.000 52.49211  ?  824 HOH A O      1 
HETATM 7627 O O      . HOH C 3 .   ? 33.30300  15.02000  24.00800 1.000 46.59301  ?  825 HOH A O      1 
HETATM 7628 O O      . HOH C 3 .   ? 10.41700  26.50400  10.77300 1.000 50.22660  ?  826 HOH A O      1 
HETATM 7629 O O      . HOH C 3 .   ? 3.59900   18.91200  7.06800  1.000 55.85488  ?  827 HOH A O      1 
HETATM 7630 O O      . HOH C 3 .   ? 21.81300  18.83000  27.48300 1.000 44.09575  ?  828 HOH A O      1 
HETATM 7631 O O      . HOH C 3 .   ? -0.62900  8.01400   13.97800 0.720 48.81039  ?  829 HOH A O      1 
HETATM 7632 O O      . HOH C 3 .   ? 20.92600  1.29500   3.42100  1.000 55.17692  ?  830 HOH A O      1 
HETATM 7633 O O      . HOH C 3 .   ? 19.77400  15.52200  10.64000 1.000 53.23791  ?  831 HOH A O      1 
HETATM 7634 O O      . HOH C 3 .   ? -14.02200 43.63400  22.44700 1.000 69.09791  ?  832 HOH A O      1 
HETATM 7635 O O      . HOH C 3 .   ? -14.17200 27.25600  25.37000 1.000 72.05324  ?  833 HOH A O      1 
HETATM 7636 O O      . HOH C 3 .   ? 7.96300   -24.48300 -3.47800 1.000 65.64856  ?  834 HOH A O      1 
HETATM 7637 O O      . HOH C 3 .   ? -6.86100  24.39700  13.34700 1.000 50.08668  ?  835 HOH A O      1 
HETATM 7638 O O      . HOH C 3 .   ? 32.71700  -0.17700  9.86500  1.000 60.80719  ?  836 HOH A O      1 
HETATM 7639 O O      . HOH C 3 .   ? 34.58400  7.98700   26.52000 1.000 49.97162  ?  837 HOH A O      1 
HETATM 7640 O O      . HOH C 3 .   ? 5.55800   -11.41700 17.86700 1.000 63.48384  ?  838 HOH A O      1 
HETATM 7641 O O      . HOH C 3 .   ? 19.59400  -2.88700  24.97400 1.000 50.04377  ?  839 HOH A O      1 
HETATM 7642 O O      . HOH C 3 .   ? -12.00600 25.05200  27.45700 1.000 66.76033  ?  840 HOH A O      1 
HETATM 7643 O O      . HOH C 3 .   ? 4.35100   -7.29000  16.41700 1.000 69.12180  ?  841 HOH A O      1 
HETATM 7644 O O      . HOH C 3 .   ? -4.16500  4.35300   17.03300 1.000 77.28615  ?  842 HOH A O      1 
HETATM 7645 O O      . HOH C 3 .   ? 24.39200  15.98300  36.35200 1.000 63.21895  ?  843 HOH A O      1 
HETATM 7646 O O      . HOH C 3 .   ? 9.67400   -8.58900  17.35600 1.000 52.50729  ?  844 HOH A O      1 
HETATM 7647 O O      . HOH C 3 .   ? 12.57500  -19.70400 29.99500 1.000 73.71153  ?  845 HOH A O      1 
HETATM 7648 O O      . HOH C 3 .   ? 35.26100  11.19900  23.92100 1.000 49.52551  ?  846 HOH A O      1 
HETATM 7649 O O      A HOH C 3 .   ? 7.60100   -0.10200  19.31100 0.390 46.47492  ?  847 HOH A O      1 
HETATM 7650 O O      B HOH C 3 .   ? 5.69300   -0.74300  18.48700 0.610 61.87965  ?  847 HOH A O      1 
HETATM 7651 O O      . HOH C 3 .   ? 7.02900   0.14900   26.37800 1.000 69.86158  ?  848 HOH A O      1 
HETATM 7652 O O      . HOH C 3 .   ? 11.487    0.929     45.733   1.000 71.86577  ?  849 HOH A O      1 
HETATM 7653 O O      . HOH C 3 .   ? 30.23900  -4.86400  23.14100 1.000 53.94431  ?  850 HOH A O      1 
HETATM 7654 O O      . HOH C 3 .   ? 19.07200  18.96500  27.46700 1.000 55.46963  ?  851 HOH A O      1 
HETATM 7655 O O      . HOH C 3 .   ? 34.92700  13.56100  22.71800 1.000 47.56926  ?  852 HOH A O      1 
HETATM 7656 O O      . HOH C 3 .   ? 29.07200  1.38200   10.16600 1.000 52.50538  ?  853 HOH A O      1 
HETATM 7657 O O      . HOH C 3 .   ? 32.70500  -3.21800  2.19300  1.000 70.81385  ?  854 HOH A O      1 
HETATM 7658 O O      . HOH C 3 .   ? 8.75400   -5.07900  1.13800  1.000 57.44436  ?  855 HOH A O      1 
HETATM 7659 O O      . HOH C 3 .   ? 33.54000  4.58800   11.40700 1.000 65.60949  ?  856 HOH A O      1 
HETATM 7660 O O      . HOH C 3 .   ? 7.547     39.584    21.552   1.000 54.16545  ?  857 HOH A O      1 
HETATM 7661 O O      . HOH C 3 .   ? 22.82200  3.88200   2.23100  1.000 63.26040  ?  858 HOH A O      1 
HETATM 7662 O O      . HOH C 3 .   ? 5.82700   -4.12900  17.85400 1.000 76.98115  ?  859 HOH A O      1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 3   ? 1.31114 1.03290 1.58876 0.18324  -0.15018 -0.11244 3   GLY A N   
2    C CA  . GLY A 3   ? 1.28749 1.04952 1.56060 0.21324  -0.14884 -0.14708 3   GLY A CA  
3    C C   . GLY A 3   ? 1.16033 0.98076 1.38835 0.20685  -0.12732 -0.16039 3   GLY A C   
4    O O   . GLY A 3   ? 1.15160 1.01667 1.37591 0.22625  -0.11628 -0.17486 3   GLY A O   
8    N N   . VAL A 4   ? 0.98936 0.80938 1.18943 0.17999  -0.11963 -0.15334 4   VAL A N   
9    C CA  . VAL A 4   ? 1.04078 0.90738 1.19738 0.17169  -0.09985 -0.16068 4   VAL A CA  
10   C C   . VAL A 4   ? 0.84435 0.72162 0.97994 0.14100  -0.09061 -0.12298 4   VAL A C   
11   O O   . VAL A 4   ? 0.88036 0.72559 1.02684 0.12617  -0.09711 -0.09531 4   VAL A O   
12   C CB  . VAL A 4   ? 1.00884 0.86561 1.14405 0.17518  -0.10273 -0.19613 4   VAL A CB  
13   C CG1 . VAL A 4   ? 1.14745 1.00548 1.28355 0.21287  -0.10712 -0.23937 4   VAL A CG1 
14   C CG2 . VAL A 4   ? 1.14077 0.94802 1.30247 0.15630  -0.12161 -0.19362 4   VAL A CG2 
24   N N   . LYS A 5   ? 0.74085 0.66198 0.84590 0.13321  -0.07319 -0.12150 5   LYS A N   
25   C CA  . LYS A 5   ? 0.64703 0.57960 0.72900 0.10678  -0.06534 -0.09367 5   LYS A CA  
26   C C   . LYS A 5   ? 0.67333 0.60030 0.73040 0.09105  -0.05927 -0.10246 5   LYS A C   
27   O O   . LYS A 5   ? 0.61920 0.56720 0.65459 0.09826  -0.04998 -0.12245 5   LYS A O   
28   C CB  . LYS A 5   ? 0.64341 0.62445 0.72032 0.10626  -0.05433 -0.08576 5   LYS A CB  
29   C CG  . LYS A 5   ? 0.61795 0.60538 0.67332 0.08283  -0.05277 -0.06076 5   LYS A CG  
30   C CD  . LYS A 5   ? 0.60540 0.63941 0.66254 0.07749  -0.04241 -0.06044 5   LYS A CD  
31   C CE  . LYS A 5   ? 0.61690 0.65098 0.64692 0.05431  -0.04086 -0.04532 5   LYS A CE  
32   N NZ  . LYS A 5   ? 0.50775 0.57891 0.55402 0.04904  -0.04242 -0.04187 5   LYS A NZ  
46   N N   . ASN A 6   ? 0.59563 0.49477 0.65633 0.07202  -0.06323 -0.08567 6   ASN A N   
47   C CA  . ASN A 6   ? 0.61643 0.51397 0.66171 0.05500  -0.05903 -0.08923 6   ASN A CA  
48   C C   . ASN A 6   ? 0.59180 0.49783 0.62002 0.03479  -0.04792 -0.05855 6   ASN A C   
49   O O   . ASN A 6   ? 0.66204 0.54863 0.69943 0.02994  -0.04787 -0.03360 6   ASN A O   
50   C CB  . ASN A 6   ? 0.60891 0.46841 0.68852 0.05173  -0.07339 -0.10166 6   ASN A CB  
51   C CG  . ASN A 6   ? 0.63943 0.48442 0.73449 0.07596  -0.09048 -0.13863 6   ASN A CG  
52   O OD1 . ASN A 6   ? 0.65787 0.52396 0.72060 0.09331  -0.08886 -0.16426 6   ASN A OD1 
53   N ND2 . ASN A 6   ? 0.66479 0.47098 0.80849 0.07931  -0.10572 -0.14098 6   ASN A ND2 
60   N N   . SER A 7   ? 0.55439 0.48630 0.55454 0.02598  -0.03816 -0.05992 7   SER A N   
61   C CA  . SER A 7   ? 0.61156 0.55426 0.59202 0.01148  -0.02987 -0.03795 7   SER A CA  
62   C C   . SER A 7   ? 0.52751 0.47023 0.49610 -0.00345 -0.02321 -0.03937 7   SER A C   
63   O O   . SER A 7   ? 0.53237 0.47725 0.49886 -0.00126 -0.02562 -0.05789 7   SER A O   
64   C CB  . SER A 7   ? 0.55584 0.53190 0.52532 0.01519  -0.02701 -0.03745 7   SER A CB  
65   O OG  . SER A 7   ? 0.60836 0.60532 0.56910 0.01541  -0.01798 -0.05158 7   SER A OG  
71   N N   . ILE A 8   ? 0.55531 0.49471 0.51279 -0.01493 -0.01593 -0.02031 8   ILE A N   
72   C CA  . ILE A 8   ? 0.53056 0.47362 0.47896 -0.02748 -0.00829 -0.02059 8   ILE A CA  
73   C C   . ILE A 8   ? 0.51859 0.48033 0.43804 -0.03137 -0.00431 -0.01547 8   ILE A C   
74   O O   . ILE A 8   ? 0.56399 0.52704 0.46958 -0.02783 -0.00642 -0.00396 8   ILE A O   
75   C CB  . ILE A 8   ? 0.62591 0.54976 0.59260 -0.03591 0.00078  -0.00500 8   ILE A CB  
76   C CG1 . ILE A 8   ? 0.55593 0.46027 0.56953 -0.03579 -0.00702 -0.01422 8   ILE A CG1 
77   C CG2 . ILE A 8   ? 0.55327 0.48622 0.51168 -0.04599 0.01046  -0.00515 8   ILE A CG2 
78   C CD1 . ILE A 8   ? 0.59196 0.47626 0.64120 -0.04475 0.00625  0.00849  8   ILE A CD1 
90   N N   . ILE A 9   ? 0.47638 0.44987 0.38764 -0.03663 -0.00210 -0.02499 9   ILE A N   
91   C CA  . ILE A 9   ? 0.55539 0.53936 0.44916 -0.04352 0.00063  -0.02200 9   ILE A CA  
92   C C   . ILE A 9   ? 0.55911 0.53360 0.44990 -0.05058 0.00731  -0.02087 9   ILE A C   
93   O O   . ILE A 9   ? 0.51658 0.48851 0.41798 -0.05194 0.00657  -0.02902 9   ILE A O   
94   C CB  . ILE A 9   ? 0.48923 0.49073 0.38401 -0.04446 0.00119  -0.02863 9   ILE A CB  
95   C CG1 . ILE A 9   ? 0.59162 0.59704 0.47949 -0.05381 0.00137  -0.02741 9   ILE A CG1 
96   C CG2 . ILE A 9   ? 0.58750 0.58643 0.47968 -0.04031 0.00413  -0.03671 9   ILE A CG2 
97   C CD1 . ILE A 9   ? 0.59568 0.60082 0.47497 -0.05346 -0.00720 -0.02532 9   ILE A CD1 
109  N N   . TRP A 10  ? 0.56839 0.53827 0.44352 -0.05156 0.01289  -0.01211 10  TRP A N   
110  C CA  . TRP A 10  ? 0.55000 0.51385 0.42608 -0.05512 0.02482  -0.00928 10  TRP A CA  
111  C C   . TRP A 10  ? 0.58596 0.55473 0.44264 -0.05681 0.02328  -0.01760 10  TRP A C   
112  O O   . TRP A 10  ? 0.56588 0.53525 0.39711 -0.05253 0.01810  -0.01841 10  TRP A O   
113  C CB  . TRP A 10  ? 0.57803 0.53108 0.44589 -0.05048 0.03859  0.00892  10  TRP A CB  
114  C CG  . TRP A 10  ? 0.56262 0.51394 0.43379 -0.05158 0.05914  0.01549  10  TRP A CG  
115  C CD1 . TRP A 10  ? 0.56951 0.52741 0.46891 -0.05751 0.06322  0.00535  10  TRP A CD1 
116  C CD2 . TRP A 10  ? 0.53681 0.48060 0.38202 -0.04323 0.08055  0.03510  10  TRP A CD2 
117  N NE1 . TRP A 10  ? 0.55884 0.51773 0.46119 -0.05478 0.08765  0.01573  10  TRP A NE1 
118  C CE2 . TRP A 10  ? 0.55298 0.50291 0.41828 -0.04559 0.10152  0.03536  10  TRP A CE2 
119  C CE3 . TRP A 10  ? 0.60378 0.53592 0.40728 -0.03080 0.08465  0.05388  10  TRP A CE3 
120  C CZ2 . TRP A 10  ? 0.63916 0.58626 0.48394 -0.03614 0.13236  0.05465  10  TRP A CZ2 
121  C CZ3 . TRP A 10  ? 0.63761 0.56237 0.41056 -0.01996 0.11272  0.07472  10  TRP A CZ3 
122  C CH2 . TRP A 10  ? 0.66038 0.59373 0.45421 -0.02288 0.13929  0.07550  10  TRP A CH2 
133  N N   . PHE A 11  ? 0.61581 0.58550 0.48645 -0.06109 0.02388  -0.02569 11  PHE A N   
134  C CA  . PHE A 11  ? 0.51714 0.48613 0.37754 -0.06241 0.02147  -0.03406 11  PHE A CA  
135  C C   . PHE A 11  ? 0.58286 0.54836 0.43815 -0.05787 0.03518  -0.03445 11  PHE A C   
136  O O   . PHE A 11  ? 0.61174 0.57919 0.49286 -0.05834 0.04596  -0.03082 11  PHE A O   
137  C CB  . PHE A 11  ? 0.49305 0.46135 0.36789 -0.06553 0.01525  -0.03909 11  PHE A CB  
138  C CG  . PHE A 11  ? 0.51392 0.48714 0.38750 -0.06698 0.00914  -0.03665 11  PHE A CG  
139  C CD1 . PHE A 11  ? 0.52503 0.50043 0.39853 -0.07180 0.00598  -0.03606 11  PHE A CD1 
140  C CD2 . PHE A 11  ? 0.54986 0.52593 0.42743 -0.06240 0.00766  -0.03606 11  PHE A CD2 
141  C CE1 . PHE A 11  ? 0.58085 0.56532 0.46162 -0.07308 0.00767  -0.02997 11  PHE A CE1 
142  C CE2 . PHE A 11  ? 0.59368 0.57693 0.46647 -0.05971 0.00801  -0.03346 11  PHE A CE2 
143  C CZ  . PHE A 11  ? 0.60808 0.59768 0.48412 -0.06556 0.01120  -0.02788 11  PHE A CZ  
153  N N   . ARG A 12  ? 0.58067 0.54231 0.40620 -0.05165 0.03459  -0.04055 12  ARG A N   
154  C CA  . ARG A 12  ? 0.56034 0.51931 0.37569 -0.04312 0.04903  -0.04592 12  ARG A CA  
155  C C   . ARG A 12  ? 0.62758 0.57892 0.43736 -0.04169 0.03534  -0.06519 12  ARG A C   
156  O O   . ARG A 12  ? 0.52236 0.47183 0.35621 -0.04277 0.03713  -0.07135 12  ARG A O   
157  C CB  . ARG A 12  ? 0.65327 0.60947 0.42725 -0.02976 0.06343  -0.03674 12  ARG A CB  
158  C CG  . ARG A 12  ? 0.66706 0.62418 0.44967 -0.03182 0.07535  -0.01311 12  ARG A CG  
159  C CD  . ARG A 12  ? 0.61643 0.57062 0.38208 -0.03181 0.05437  -0.01023 12  ARG A CD  
160  N NE  . ARG A 12  ? 0.58689 0.53538 0.29963 -0.01732 0.04185  -0.01757 12  ARG A NE  
161  C CZ  . ARG A 12  ? 0.69311 0.63265 0.35715 0.00004  0.05229  -0.00385 12  ARG A CZ  
162  N NH1 . ARG A 12  ? 0.73728 0.67218 0.40533 0.00222  0.08095  0.02327  12  ARG A NH1 
163  N NH2 . ARG A 12  ? 0.75779 0.69104 0.36833 0.01708  0.03270  -0.01697 12  ARG A NH2 
177  N N   . LYS A 13  ? 0.58712 0.53252 0.37320 -0.03909 0.01802  -0.07583 13  LYS A N   
178  C CA  . LYS A 13  ? 0.62646 0.56261 0.42661 -0.04460 -0.00227 -0.09190 13  LYS A CA  
179  C C   . LYS A 13  ? 0.59693 0.54032 0.42481 -0.05913 -0.01316 -0.08202 13  LYS A C   
180  O O   . LYS A 13  ? 0.54225 0.49578 0.37752 -0.06289 -0.00462 -0.06672 13  LYS A O   
181  C CB  . LYS A 13  ? 0.60164 0.52767 0.36851 -0.03159 -0.01745 -0.11391 13  LYS A CB  
182  C CG  . LYS A 13  ? 0.66149 0.57973 0.39854 -0.01308 -0.00264 -0.12668 13  LYS A CG  
183  C CD  . LYS A 13  ? 0.73044 0.63578 0.42222 0.00562  -0.02145 -0.15360 13  LYS A CD  
184  C CE  . LYS A 13  ? 0.79676 0.69901 0.43950 0.03143  0.00268  -0.16118 13  LYS A CE  
185  N NZ  . LYS A 13  ? 0.82240 0.70765 0.41255 0.05529  -0.02008 -0.19515 13  LYS A NZ  
199  N N   . GLY A 14  ? 0.64840 0.58654 0.49734 -0.06658 -0.03057 -0.09142 14  GLY A N   
200  C CA  . GLY A 14  ? 0.52977 0.47940 0.41069 -0.07910 -0.03460 -0.07992 14  GLY A CA  
201  C C   . GLY A 14  ? 0.54269 0.49521 0.43473 -0.08401 -0.01863 -0.06139 14  GLY A C   
202  O O   . GLY A 14  ? 0.51127 0.47783 0.40665 -0.08515 -0.01224 -0.04976 14  GLY A O   
206  N N   . LEU A 15  ? 0.61508 0.55304 0.50982 -0.08323 -0.01453 -0.06075 15  LEU A N   
207  C CA  . LEU A 15  ? 0.51945 0.45603 0.41542 -0.08234 -0.00544 -0.04612 15  LEU A CA  
208  C C   . LEU A 15  ? 0.57461 0.50806 0.48969 -0.09038 -0.00245 -0.03064 15  LEU A C   
209  O O   . LEU A 15  ? 0.56508 0.48037 0.48832 -0.09129 -0.00192 -0.02239 15  LEU A O   
210  C CB  . LEU A 15  ? 0.55090 0.47388 0.44476 -0.07500 -0.00568 -0.05153 15  LEU A CB  
211  C CG  . LEU A 15  ? 0.55149 0.48035 0.43609 -0.06666 -0.00049 -0.06341 15  LEU A CG  
212  C CD1 . LEU A 15  ? 0.64119 0.56381 0.53877 -0.05886 0.00046  -0.06666 15  LEU A CD1 
213  C CD2 . LEU A 15  ? 0.58903 0.53384 0.46585 -0.06589 0.00709  -0.05725 15  LEU A CD2 
225  N N   . ARG A 16  ? 0.55868 0.51022 0.48363 -0.09488 0.00208  -0.02394 16  ARG A N   
226  C CA  . ARG A 16  ? 0.53620 0.49115 0.48827 -0.10302 0.01227  -0.00611 16  ARG A CA  
227  C C   . ARG A 16  ? 0.50069 0.48184 0.45481 -0.10036 0.02292  0.00076  16  ARG A C   
228  O O   . ARG A 16  ? 0.49090 0.48455 0.43567 -0.09568 0.01578  -0.01092 16  ARG A O   
229  C CB  . ARG A 16  ? 0.46666 0.41572 0.46455 -0.11677 0.00174  -0.01228 16  ARG A CB  
230  C CG  . ARG A 16  ? 0.50372 0.46798 0.51403 -0.11839 -0.01660 -0.03376 16  ARG A CG  
231  C CD  . ARG A 16  ? 0.52860 0.48789 0.59372 -0.13125 -0.03359 -0.04455 16  ARG A CD  
232  N NE  . ARG A 16  ? 0.57516 0.54967 0.64875 -0.12858 -0.05742 -0.06705 16  ARG A NE  
233  C CZ  . ARG A 16  ? 0.54316 0.50624 0.58057 -0.11696 -0.07895 -0.09264 16  ARG A CZ  
234  N NH1 . ARG A 16  ? 0.53158 0.47195 0.52922 -0.10817 -0.07622 -0.10016 16  ARG A NH1 
235  N NH2 . ARG A 16  ? 0.59426 0.56973 0.63399 -0.11098 -0.10348 -0.11106 16  ARG A NH2 
249  N N   . LEU A 17  ? 0.48459 0.47268 0.45238 -0.10177 0.04233  0.02177  17  LEU A N   
250  C CA  . LEU A 17  ? 0.57146 0.58772 0.55405 -0.09886 0.05669  0.02851  17  LEU A CA  
251  C C   . LEU A 17  ? 0.58270 0.61823 0.63333 -0.11447 0.05562  0.02947  17  LEU A C   
252  O O   . LEU A 17  ? 0.54419 0.60641 0.61809 -0.11263 0.05301  0.02218  17  LEU A O   
253  C CB  . LEU A 17  ? 0.58492 0.60160 0.54037 -0.08670 0.08363  0.05129  17  LEU A CB  
254  C CG  . LEU A 17  ? 0.66054 0.67488 0.55799 -0.06518 0.08118  0.04157  17  LEU A CG  
255  C CD1 . LEU A 17  ? 0.65492 0.64718 0.52683 -0.06295 0.05780  0.02539  17  LEU A CD1 
256  C CD2 . LEU A 17  ? 0.74945 0.76000 0.60680 -0.04752 0.10462  0.06160  17  LEU A CD2 
268  N N   . HIS A 18  ? 0.52680 0.54850 0.61748 -0.12930 0.05429  0.03671  18  HIS A N   
269  C CA  . HIS A 18  ? 0.51399 0.55335 0.68541 -0.14614 0.04874  0.03485  18  HIS A CA  
270  C C   . HIS A 18  ? 0.48692 0.52872 0.66719 -0.14714 0.01051  0.00111  18  HIS A C   
271  O O   . HIS A 18  ? 0.49467 0.51577 0.62337 -0.13875 -0.00714 -0.01626 18  HIS A O   
272  C CB  . HIS A 18  ? 0.55854 0.57670 0.77778 -0.16230 0.05783  0.05340  18  HIS A CB  
273  C CG  . HIS A 18  ? 0.56758 0.55135 0.78519 -0.16758 0.02802  0.03237  18  HIS A CG  
274  N ND1 . HIS A 18  ? 0.50498 0.45579 0.66708 -0.15825 0.02789  0.03524  18  HIS A ND1 
275  C CD2 . HIS A 18  ? 0.56743 0.54435 0.83533 -0.17868 -0.00376 0.00587  18  HIS A CD2 
276  C CE1 . HIS A 18  ? 0.52824 0.45453 0.70573 -0.16291 0.00118  0.01204  18  HIS A CE1 
277  N NE2 . HIS A 18  ? 0.55917 0.49881 0.79636 -0.17459 -0.01919 -0.00727 18  HIS A NE2 
285  N N   . ASP A 19  ? 0.42677 0.49655 0.67153 -0.15432 -0.00096 -0.00725 19  ASP A N   
286  C CA  . ASP A 19  ? 0.45226 0.52657 0.70274 -0.15040 -0.04124 -0.03916 19  ASP A CA  
287  C C   . ASP A 19  ? 0.49653 0.55828 0.65825 -0.13092 -0.05067 -0.05078 19  ASP A C   
288  O O   . ASP A 19  ? 0.45850 0.49782 0.58147 -0.12468 -0.07224 -0.07001 19  ASP A O   
289  C CB  . ASP A 19  ? 0.47721 0.52911 0.76495 -0.16177 -0.07048 -0.05977 19  ASP A CB  
290  C CG  . ASP A 19  ? 0.53084 0.58736 0.82051 -0.15317 -0.11602 -0.09547 19  ASP A CG  
291  O OD1 . ASP A 19  ? 0.55127 0.63636 0.84781 -0.14438 -0.12484 -0.09895 19  ASP A OD1 
292  O OD2 . ASP A 19  ? 0.58270 0.61297 0.86460 -0.15196 -0.14500 -0.12140 19  ASP A OD2 
297  N N   . ASN A 20  ? 0.41972 0.49617 0.55344 -0.12022 -0.03217 -0.03847 20  ASN A N   
298  C CA  . ASN A 20  ? 0.43254 0.49814 0.49796 -0.10411 -0.03639 -0.04377 20  ASN A CA  
299  C C   . ASN A 20  ? 0.41025 0.49939 0.48484 -0.09327 -0.04258 -0.04520 20  ASN A C   
300  O O   . ASN A 20  ? 0.40905 0.50873 0.47744 -0.08629 -0.02265 -0.03396 20  ASN A O   
301  C CB  . ASN A 20  ? 0.48804 0.53880 0.50963 -0.09974 -0.01184 -0.02989 20  ASN A CB  
302  C CG  . ASN A 20  ? 0.43939 0.47447 0.40684 -0.08818 -0.01691 -0.03593 20  ASN A CG  
303  O OD1 . ASN A 20  ? 0.54836 0.58566 0.50292 -0.08030 -0.03145 -0.04347 20  ASN A OD1 
304  N ND2 . ASN A 20  ? 0.52672 0.54540 0.46526 -0.08604 -0.00522 -0.03102 20  ASN A ND2 
311  N N   . PRO A 21  ? 0.45793 0.55412 0.54648 -0.08852 -0.07324 -0.06109 21  PRO A N   
312  C CA  . PRO A 21  ? 0.45994 0.57694 0.55974 -0.07518 -0.08327 -0.06177 21  PRO A CA  
313  C C   . PRO A 21  ? 0.51863 0.61962 0.55749 -0.05994 -0.07399 -0.05312 21  PRO A C   
314  O O   . PRO A 21  ? 0.44517 0.56047 0.49754 -0.05011 -0.06952 -0.04796 21  PRO A O   
315  C CB  . PRO A 21  ? 0.49602 0.61490 0.60704 -0.06926 -0.12553 -0.08283 21  PRO A CB  
316  C CG  . PRO A 21  ? 0.52794 0.61929 0.60838 -0.07466 -0.13598 -0.09545 21  PRO A CG  
317  C CD  . PRO A 21  ? 0.46416 0.54977 0.56342 -0.09241 -0.10417 -0.08186 21  PRO A CD  
325  N N   . ALA A 22  ? 0.50268 0.57452 0.48325 -0.05763 -0.07032 -0.05171 22  ALA A N   
326  C CA  . ALA A 22  ? 0.54917 0.60530 0.48845 -0.04682 -0.05918 -0.04121 22  ALA A CA  
327  C C   . ALA A 22  ? 0.53382 0.59618 0.48756 -0.04868 -0.03581 -0.03354 22  ALA A C   
328  O O   . ALA A 22  ? 0.52648 0.58719 0.47695 -0.03804 -0.03275 -0.02949 22  ALA A O   
329  C CB  . ALA A 22  ? 0.57433 0.60365 0.46385 -0.04611 -0.05401 -0.03987 22  ALA A CB  
335  N N   . LEU A 23  ? 0.49164 0.55783 0.45805 -0.05931 -0.02067 -0.03204 23  LEU A N   
336  C CA  . LEU A 23  ? 0.52719 0.59819 0.49470 -0.05565 -0.00002 -0.02652 23  LEU A CA  
337  C C   . LEU A 23  ? 0.53740 0.63690 0.54241 -0.04820 0.00664  -0.02567 23  LEU A C   
338  O O   . LEU A 23  ? 0.47016 0.57108 0.46660 -0.03502 0.01605  -0.02697 23  LEU A O   
339  C CB  . LEU A 23  ? 0.51120 0.57658 0.47543 -0.06510 0.01377  -0.02089 23  LEU A CB  
340  C CG  . LEU A 23  ? 0.58666 0.65660 0.54136 -0.05740 0.03529  -0.01363 23  LEU A CG  
341  C CD1 . LEU A 23  ? 0.65380 0.70867 0.57417 -0.04360 0.03237  -0.02158 23  LEU A CD1 
342  C CD2 . LEU A 23  ? 0.56797 0.62669 0.51523 -0.06551 0.04562  -0.00319 23  LEU A CD2 
354  N N   . LEU A 24  ? 0.44135 0.56482 0.49473 -0.05515 0.00078  -0.02621 24  LEU A N   
355  C CA  . LEU A 24  ? 0.43085 0.58791 0.53314 -0.04755 0.00936  -0.02537 24  LEU A CA  
356  C C   . LEU A 24  ? 0.49290 0.64947 0.58876 -0.02985 -0.00616 -0.03227 24  LEU A C   
357  O O   . LEU A 24  ? 0.44822 0.61958 0.55814 -0.01559 0.00690  -0.03340 24  LEU A O   
358  C CB  . LEU A 24  ? 0.41231 0.59713 0.58513 -0.06042 0.00037  -0.02673 24  LEU A CB  
359  C CG  . LEU A 24  ? 0.41099 0.59525 0.60870 -0.07962 0.01639  -0.01672 24  LEU A CG  
360  C CD1 . LEU A 24  ? 0.41002 0.61903 0.69278 -0.09390 -0.00085 -0.02281 24  LEU A CD1 
361  C CD2 . LEU A 24  ? 0.49527 0.68967 0.69085 -0.07613 0.05877  0.00202  24  LEU A CD2 
373  N N   . GLU A 25  ? 0.53459 0.67176 0.60614 -0.02770 -0.03308 -0.03599 25  GLU A N   
374  C CA  . GLU A 25  ? 0.51278 0.64202 0.57476 -0.00987 -0.04775 -0.03661 25  GLU A CA  
375  C C   . GLU A 25  ? 0.52736 0.63407 0.55872 -0.00135 -0.03245 -0.03421 25  GLU A C   
376  O O   . GLU A 25  ? 0.51957 0.63063 0.56709 0.01444  -0.03188 -0.03747 25  GLU A O   
377  C CB  . GLU A 25  ? 0.50659 0.61385 0.53352 -0.00676 -0.07470 -0.03542 25  GLU A CB  
378  C CG  . GLU A 25  ? 0.65036 0.74301 0.66226 0.01310  -0.09041 -0.02921 25  GLU A CG  
379  C CD  . GLU A 25  ? 0.67719 0.80035 0.74561 0.02654  -0.10080 -0.03531 25  GLU A CD  
380  O OE1 . GLU A 25  ? 0.66438 0.82086 0.78214 0.02251  -0.11319 -0.04498 25  GLU A OE1 
381  O OE2 . GLU A 25  ? 0.66238 0.77679 0.73448 0.04140  -0.09719 -0.03182 25  GLU A OE2 
388  N N   . ALA A 26  ? 0.51350 0.59649 0.50783 -0.01030 -0.02270 -0.03170 26  ALA A N   
389  C CA  . ALA A 26  ? 0.52486 0.58445 0.49899 -0.00306 -0.01580 -0.03366 26  ALA A CA  
390  C C   . ALA A 26  ? 0.58699 0.66097 0.57282 0.00842  -0.00089 -0.04357 26  ALA A C   
391  O O   . ALA A 26  ? 0.54107 0.60024 0.52426 0.02228  -0.00319 -0.05219 26  ALA A O   
392  C CB  . ALA A 26  ? 0.49852 0.53576 0.44249 -0.01495 -0.01105 -0.03115 26  ALA A CB  
398  N N   . CYS A 27  ? 0.51220 0.61256 0.51028 0.00470  0.01573  -0.04231 27  CYS A N   
399  C CA  . CYS A 27  ? 0.51200 0.62715 0.50965 0.02029  0.03626  -0.04893 27  CYS A CA  
400  C C   . CYS A 27  ? 0.55035 0.69129 0.58812 0.03726  0.03883  -0.05484 27  CYS A C   
401  O O   . CYS A 27  ? 0.50878 0.65270 0.53881 0.05846  0.05055  -0.06670 27  CYS A O   
402  C CB  . CYS A 27  ? 0.56976 0.70336 0.56713 0.01170  0.06020  -0.03778 27  CYS A CB  
403  S SG  . CYS A 27  ? 0.72624 0.82878 0.67407 -0.00013 0.05856  -0.03309 27  CYS A SG  
409  N N   . LYS A 28  ? 0.46383 0.62376 0.54434 0.03144  0.02574  -0.04974 28  LYS A N   
410  C CA  . LYS A 28  ? 0.55039 0.74225 0.68277 0.04778  0.02702  -0.05515 28  LYS A CA  
411  C C   . LYS A 28  ? 0.52011 0.69076 0.64119 0.07095  0.01728  -0.06762 28  LYS A C   
412  O O   . LYS A 28  ? 0.55182 0.68806 0.65388 0.07030  -0.00628 -0.06568 28  LYS A O   
413  C CB  . LYS A 28  ? 0.54294 0.75180 0.71932 0.03899  0.00204  -0.05084 28  LYS A CB  
414  C CG  . LYS A 28  ? 0.65753 0.89201 0.88829 0.05872  -0.01037 -0.05781 28  LYS A CG  
415  C CD  . LYS A 28  ? 0.66532 0.93222 0.95711 0.05022  -0.03234 -0.05716 28  LYS A CD  
416  C CE  . LYS A 28  ? 0.75129 0.98725 1.00297 0.03918  -0.06659 -0.05394 28  LYS A CE  
417  N NZ  . LYS A 28  ? 0.66279 0.87850 0.89845 0.05874  -0.10061 -0.05386 28  LYS A NZ  
431  N N   . ASP A 29  ? 0.52667 0.71567 0.65940 0.09268  0.03770  -0.07955 29  ASP A N   
432  C CA  . ASP A 29  ? 0.55282 0.72394 0.68573 0.11879  0.02844  -0.09677 29  ASP A CA  
433  C C   . ASP A 29  ? 0.64348 0.76214 0.72771 0.11814  0.01350  -0.10481 29  ASP A C   
434  O O   . ASP A 29  ? 0.61833 0.70878 0.71053 0.13204  -0.00471 -0.11449 29  ASP A O   
435  C CB  . ASP A 29  ? 0.68026 0.85595 0.86018 0.12666  0.00287  -0.09403 29  ASP A CB  
436  C CG  . ASP A 29  ? 0.66726 0.89944 0.91404 0.13155  0.01287  -0.09230 29  ASP A CG  
437  O OD1 . ASP A 29  ? 0.66518 0.93235 0.92953 0.14160  0.04697  -0.09813 29  ASP A OD1 
438  O OD2 . ASP A 29  ? 0.67783 0.92016 0.96075 0.12704  -0.01328 -0.08490 29  ASP A OD2 
443  N N   . ALA A 30  ? 0.55597 0.66079 0.59854 0.10244  0.01983  -0.10095 30  ALA A N   
444  C CA  . ALA A 30  ? 0.55677 0.61721 0.56816 0.09768  0.00368  -0.10785 30  ALA A CA  
445  C C   . ALA A 30  ? 0.61505 0.66441 0.59588 0.11949  0.00880  -0.13400 30  ALA A C   
446  O O   . ALA A 30  ? 0.67658 0.74780 0.62927 0.12791  0.03116  -0.13662 30  ALA A O   
447  C CB  . ALA A 30  ? 0.59311 0.64559 0.58156 0.07070  0.00325  -0.09146 30  ALA A CB  
453  N N   . LYS A 31  ? 0.65737 0.67036 0.64325 0.13071  -0.01275 -0.15326 31  LYS A N   
454  C CA  . LYS A 31  ? 0.69428 0.68881 0.64831 0.15266  -0.01884 -0.18525 31  LYS A CA  
455  C C   . LYS A 31  ? 0.67982 0.65695 0.60171 0.13738  -0.02756 -0.18549 31  LYS A C   
456  O O   . LYS A 31  ? 0.72589 0.70450 0.60115 0.15396  -0.02405 -0.20263 31  LYS A O   
457  C CB  . LYS A 31  ? 0.79190 0.75007 0.77657 0.16894  -0.04442 -0.20943 31  LYS A CB  
458  C CG  . LYS A 31  ? 0.94399 0.88030 0.89930 0.19749  -0.05856 -0.25226 31  LYS A CG  
459  C CD  . LYS A 31  ? 1.04130 1.00836 0.96188 0.23362  -0.03437 -0.27104 31  LYS A CD  
460  C CE  . LYS A 31  ? 1.10388 1.04562 0.98041 0.26845  -0.05195 -0.31826 31  LYS A CE  
461  N NZ  . LYS A 31  ? 1.28398 1.25850 1.09402 0.30130  -0.01906 -0.32742 31  LYS A NZ  
475  N N   . HIS A 32  ? 0.69982 0.66083 0.64394 0.10899  -0.03848 -0.16610 32  HIS A N   
476  C CA  . HIS A 32  ? 0.64627 0.59564 0.57313 0.09284  -0.04584 -0.16387 32  HIS A CA  
477  C C   . HIS A 32  ? 0.60316 0.56445 0.53852 0.06434  -0.03459 -0.13052 32  HIS A C   
478  O O   . HIS A 32  ? 0.58291 0.54270 0.54525 0.05473  -0.03421 -0.11268 32  HIS A O   
479  C CB  . HIS A 32  ? 0.71029 0.62151 0.66799 0.09052  -0.07433 -0.18263 32  HIS A CB  
480  C CG  . HIS A 32  ? 0.65034 0.54388 0.59774 0.12033  -0.09429 -0.22425 32  HIS A CG  
481  N ND1 . HIS A 32  ? 0.76780 0.63952 0.75050 0.13508  -0.10828 -0.24251 32  HIS A ND1 
482  C CD2 . HIS A 32  ? 0.72591 0.61723 0.62701 0.14176  -0.10535 -0.25324 32  HIS A CD2 
483  C CE1 . HIS A 32  ? 0.72959 0.58681 0.69025 0.16436  -0.12780 -0.28522 32  HIS A CE1 
484  N NE2 . HIS A 32  ? 0.82245 0.69162 0.72889 0.17009  -0.12688 -0.29244 32  HIS A NE2 
492  N N   . VAL A 33  ? 0.60932 0.57997 0.51699 0.05435  -0.02726 -0.12321 33  VAL A N   
493  C CA  . VAL A 33  ? 0.61706 0.59487 0.52946 0.03008  -0.01957 -0.09827 33  VAL A CA  
494  C C   . VAL A 33  ? 0.60954 0.57177 0.51769 0.02047  -0.02957 -0.10226 33  VAL A C   
495  O O   . VAL A 33  ? 0.66689 0.62692 0.54824 0.03193  -0.03541 -0.11711 33  VAL A O   
496  C CB  . VAL A 33  ? 0.64095 0.64804 0.53671 0.02650  0.00043  -0.08378 33  VAL A CB  
497  C CG1 . VAL A 33  ? 0.64394 0.65248 0.54269 0.00403  0.00264  -0.06554 33  VAL A CG1 
498  C CG2 . VAL A 33  ? 0.60892 0.63786 0.52584 0.03479  0.00907  -0.08026 33  VAL A CG2 
508  N N   . TYR A 34  ? 0.62774 0.58038 0.56073 0.00238  -0.03079 -0.08828 34  TYR A N   
509  C CA  . TYR A 34  ? 0.60473 0.54739 0.54954 -0.00765 -0.03793 -0.09092 34  TYR A CA  
510  C C   . TYR A 34  ? 0.53989 0.49428 0.47148 -0.02200 -0.02439 -0.07244 34  TYR A C   
511  O O   . TYR A 34  ? 0.57307 0.52675 0.51486 -0.03271 -0.01508 -0.05527 34  TYR A O   
512  C CB  . TYR A 34  ? 0.55554 0.47768 0.55056 -0.01543 -0.04530 -0.08962 34  TYR A CB  
513  C CG  . TYR A 34  ? 0.56369 0.46721 0.58338 -0.00172 -0.06524 -0.11383 34  TYR A CG  
514  C CD1 . TYR A 34  ? 0.60724 0.50470 0.62908 0.00917  -0.06497 -0.11434 34  TYR A CD1 
515  C CD2 . TYR A 34  ? 0.58524 0.47621 0.63023 0.00249  -0.08857 -0.13985 34  TYR A CD2 
516  C CE1 . TYR A 34  ? 0.59322 0.46979 0.63948 0.02420  -0.08516 -0.14059 34  TYR A CE1 
517  C CE2 . TYR A 34  ? 0.62173 0.49191 0.69127 0.01717  -0.11258 -0.16870 34  TYR A CE2 
518  C CZ  . TYR A 34  ? 0.57654 0.43827 0.64536 0.02803  -0.10953 -0.16908 34  TYR A CZ  
519  O OH  . TYR A 34  ? 0.64754 0.48542 0.74187 0.04471  -0.13461 -0.20099 34  TYR A OH  
529  N N   . PRO A 35  ? 0.61236 0.57434 0.51792 -0.02023 -0.02335 -0.07498 35  PRO A N   
530  C CA  . PRO A 35  ? 0.54805 0.51624 0.44726 -0.03308 -0.01350 -0.06097 35  PRO A CA  
531  C C   . PRO A 35  ? 0.54547 0.50573 0.47095 -0.04041 -0.01787 -0.06299 35  PRO A C   
532  O O   . PRO A 35  ? 0.59069 0.54546 0.52626 -0.03442 -0.03250 -0.07725 35  PRO A O   
533  C CB  . PRO A 35  ? 0.60638 0.58045 0.47393 -0.02638 -0.01090 -0.06086 35  PRO A CB  
534  C CG  . PRO A 35  ? 0.65489 0.62883 0.50293 -0.00747 -0.01536 -0.07330 35  PRO A CG  
535  C CD  . PRO A 35  ? 0.61642 0.57873 0.49117 -0.00314 -0.03036 -0.08928 35  PRO A CD  
543  N N   . VAL A 36  ? 0.50228 0.46341 0.43915 -0.05077 -0.00545 -0.04956 36  VAL A N   
544  C CA  . VAL A 36  ? 0.54202 0.49965 0.51477 -0.05725 -0.00096 -0.04734 36  VAL A CA  
545  C C   . VAL A 36  ? 0.55782 0.52164 0.51818 -0.06186 0.01212  -0.03983 36  VAL A C   
546  O O   . VAL A 36  ? 0.53307 0.49897 0.46259 -0.06243 0.02000  -0.03177 36  VAL A O   
547  C CB  . VAL A 36  ? 0.57792 0.52693 0.57800 -0.06096 0.00829  -0.03485 36  VAL A CB  
548  C CG1 . VAL A 36  ? 0.63760 0.58804 0.66690 -0.06851 0.02785  -0.02112 36  VAL A CG1 
549  C CG2 . VAL A 36  ? 0.58207 0.51995 0.61720 -0.05695 -0.00933 -0.04923 36  VAL A CG2 
559  N N   . PHE A 37  ? 0.54940 0.51610 0.53653 -0.06280 0.01061  -0.04631 37  PHE A N   
560  C CA  . PHE A 37  ? 0.52678 0.49905 0.51732 -0.06479 0.02660  -0.04121 37  PHE A CA  
561  C C   . PHE A 37  ? 0.46477 0.44283 0.51389 -0.06863 0.03823  -0.03774 37  PHE A C   
562  O O   . PHE A 37  ? 0.51184 0.49119 0.60694 -0.06932 0.02170  -0.04945 37  PHE A O   
563  C CB  . PHE A 37  ? 0.51577 0.48842 0.49523 -0.06068 0.01600  -0.05135 37  PHE A CB  
564  C CG  . PHE A 37  ? 0.50135 0.47765 0.48176 -0.05935 0.03093  -0.05061 37  PHE A CG  
565  C CD1 . PHE A 37  ? 0.47203 0.45817 0.49944 -0.05757 0.03851  -0.05439 37  PHE A CD1 
566  C CD2 . PHE A 37  ? 0.52178 0.49279 0.46210 -0.05814 0.03610  -0.04933 37  PHE A CD2 
567  C CE1 . PHE A 37  ? 0.50624 0.49714 0.53330 -0.05227 0.05531  -0.05600 37  PHE A CE1 
568  C CE2 . PHE A 37  ? 0.55347 0.52490 0.48980 -0.05260 0.04772  -0.05426 37  PHE A CE2 
569  C CZ  . PHE A 37  ? 0.56602 0.54763 0.54254 -0.04852 0.05956  -0.05710 37  PHE A CZ  
579  N N   . VAL A 38  ? 0.48596 0.46765 0.53521 -0.06956 0.06628  -0.02206 38  VAL A N   
580  C CA  . VAL A 38  ? 0.54498 0.53500 0.65780 -0.07430 0.08764  -0.01151 38  VAL A CA  
581  C C   . VAL A 38  ? 0.56588 0.57154 0.69725 -0.06968 0.10134  -0.01734 38  VAL A C   
582  O O   . VAL A 38  ? 0.58820 0.59409 0.67126 -0.06147 0.11748  -0.01437 38  VAL A O   
583  C CB  . VAL A 38  ? 0.54938 0.53189 0.64889 -0.07479 0.11706  0.01642  38  VAL A CB  
584  C CG1 . VAL A 38  ? 0.55625 0.54894 0.72974 -0.08076 0.14804  0.03368  38  VAL A CG1 
585  C CG2 . VAL A 38  ? 0.55163 0.51729 0.64124 -0.07735 0.10067  0.02070  38  VAL A CG2 
595  N N   . LEU A 39  ? 0.58572 0.60414 0.78993 -0.07263 0.09146  -0.02904 39  LEU A N   
596  C CA  . LEU A 39  ? 0.60516 0.64083 0.84091 -0.06619 0.09843  -0.03868 39  LEU A CA  
597  C C   . LEU A 39  ? 0.61428 0.67133 0.93630 -0.07144 0.13055  -0.02583 39  LEU A C   
598  O O   . LEU A 39  ? 0.60536 0.66659 1.00320 -0.08214 0.12134  -0.02578 39  LEU A O   
599  C CB  . LEU A 39  ? 0.64332 0.67867 0.89805 -0.06173 0.05706  -0.06304 39  LEU A CB  
600  C CG  . LEU A 39  ? 0.73889 0.79136 1.04006 -0.05297 0.05503  -0.07571 39  LEU A CG  
601  C CD1 . LEU A 39  ? 0.88022 0.91732 1.13415 -0.04209 0.02130  -0.09039 39  LEU A CD1 
602  C CD2 . LEU A 39  ? 0.79480 0.86837 1.20389 -0.05738 0.04520  -0.08444 39  LEU A CD2 
614  N N   . ASP A 40  ? 0.74446 0.81470 1.05888 -0.06305 0.16886  -0.01570 40  ASP A N   
615  C CA  . ASP A 40  ? 0.72924 0.82512 1.12900 -0.06594 0.20977  0.00053  40  ASP A CA  
616  C C   . ASP A 40  ? 0.81789 0.93935 1.31011 -0.06452 0.19192  -0.02231 40  ASP A C   
617  O O   . ASP A 40  ? 0.82579 0.95678 1.30244 -0.05003 0.19457  -0.03601 40  ASP A O   
618  C CB  . ASP A 40  ? 0.94618 1.04694 1.28975 -0.05107 0.26092  0.01914  40  ASP A CB  
619  C CG  . ASP A 40  ? 1.08239 1.20537 1.49897 -0.05424 0.31652  0.04959  40  ASP A CG  
620  O OD1 . ASP A 40  ? 0.97686 1.11925 1.51272 -0.06908 0.31394  0.04996  40  ASP A OD1 
621  O OD2 . ASP A 40  ? 1.27913 1.39987 1.63493 -0.04052 0.36278  0.07342  40  ASP A OD2 
626  N N   . PRO A 41  ? 0.80046 0.93215 1.39283 -0.07719 0.16921  -0.02987 41  PRO A N   
627  C CA  . PRO A 41  ? 0.74342 0.89923 1.42339 -0.07255 0.14123  -0.05605 41  PRO A CA  
628  C C   . PRO A 41  ? 0.97128 1.16389 1.72115 -0.06528 0.18574  -0.04929 41  PRO A C   
629  O O   . PRO A 41  ? 0.84033 1.04994 1.62601 -0.05277 0.16639  -0.07178 41  PRO A O   
630  C CB  . PRO A 41  ? 0.87144 1.02956 1.64941 -0.08785 0.10946  -0.06534 41  PRO A CB  
631  C CG  . PRO A 41  ? 0.82344 0.97193 1.60942 -0.10323 0.14876  -0.03270 41  PRO A CG  
632  C CD  . PRO A 41  ? 0.79586 0.91880 1.43990 -0.09475 0.16951  -0.01538 41  PRO A CD  
640  N N   . HIS A 42  ? 0.90931 1.11439 1.67829 -0.06999 0.24677  -0.01729 42  HIS A N   
641  C CA  . HIS A 42  ? 0.90269 1.14604 1.73733 -0.06042 0.29957  -0.00727 42  HIS A CA  
642  C C   . HIS A 42  ? 0.96229 1.19708 1.67835 -0.03719 0.33317  -0.00343 42  HIS A C   
643  O O   . HIS A 42  ? 1.08744 1.32679 1.76976 -0.02855 0.39006  0.02379  42  HIS A O   
644  C CB  . HIS A 42  ? 0.99519 1.23423 1.87305 -0.07026 0.33310  0.02683  42  HIS A CB  
645  C CG  . HIS A 42  ? 1.08745 1.31692 2.05573 -0.08872 0.29209  0.01986  42  HIS A CG  
646  N ND1 . HIS A 42  ? 1.13623 1.37352 2.17398 -0.09005 0.23344  -0.01739 42  HIS A ND1 
647  C CD2 . HIS A 42  ? 1.10233 1.31129 2.09765 -0.10216 0.29794  0.04263  42  HIS A CD2 
648  C CE1 . HIS A 42  ? 0.94445 1.16567 2.04353 -0.10228 0.20472  -0.02007 42  HIS A CE1 
649  N NE2 . HIS A 42  ? 1.09271 1.29753 2.17375 -0.11080 0.24403  0.01588  42  HIS A NE2 
657  N N   . PHE A 43  ? 0.94120 1.15623 1.58300 -0.02459 0.29081  -0.03197 43  PHE A N   
658  C CA  . PHE A 43  ? 1.02191 1.22559 1.56242 -0.00168 0.31131  -0.03781 43  PHE A CA  
659  C C   . PHE A 43  ? 1.09890 1.33855 1.69804 0.01830  0.34998  -0.04534 43  PHE A C   
660  O O   . PHE A 43  ? 1.18399 1.41645 1.70477 0.04134  0.37444  -0.05177 43  PHE A O   
661  C CB  . PHE A 43  ? 1.05001 1.22020 1.51173 0.00345  0.25530  -0.06408 43  PHE A CB  
662  C CG  . PHE A 43  ? 1.04641 1.18518 1.37964 0.01336  0.26120  -0.06269 43  PHE A CG  
663  C CD1 . PHE A 43  ? 1.15658 1.27626 1.42748 0.00344  0.26748  -0.04189 43  PHE A CD1 
664  C CD2 . PHE A 43  ? 1.18243 1.30947 1.46341 0.03385  0.25625  -0.08473 43  PHE A CD2 
665  C CE1 . PHE A 43  ? 1.30379 1.39700 1.46438 0.01408  0.26641  -0.04412 43  PHE A CE1 
666  C CE2 . PHE A 43  ? 1.09916 1.19717 1.27197 0.04307  0.25496  -0.08874 43  PHE A CE2 
667  C CZ  . PHE A 43  ? 1.28681 1.36974 1.40018 0.03330  0.25888  -0.06890 43  PHE A CZ  
677  N N   . LEU A 44  ? 1.11226 1.39086 1.85047 0.01198  0.35348  -0.04815 44  LEU A N   
678  C CA  . LEU A 44  ? 1.01920 1.33107 1.81322 0.03062  0.38778  -0.05234 44  LEU A CA  
679  C C   . LEU A 44  ? 1.25223 1.56390 1.98065 0.04069  0.45018  -0.02074 44  LEU A C   
680  O O   . LEU A 44  ? 1.35749 1.66178 2.08489 0.02475  0.47091  0.01271  44  LEU A O   
681  C CB  . LEU A 44  ? 0.96382 1.30175 1.89642 0.01688  0.36563  -0.05507 44  LEU A CB  
682  C CG  . LEU A 44  ? 0.94422 1.27999 1.92819 -0.00755 0.38119  -0.02334 44  LEU A CG  
683  C CD1 . LEU A 44  ? 0.98604 1.34547 2.01155 -0.00125 0.43757  0.00086  44  LEU A CD1 
684  C CD2 . LEU A 44  ? 0.91497 1.24981 1.99919 -0.02645 0.32219  -0.04067 44  LEU A CD2 
696  N N   . GLN A 45  ? 1.15331 1.47072 1.82505 0.07004  0.47642  -0.03283 45  GLN A N   
697  C CA  . GLN A 45  ? 1.17557 1.49417 1.77042 0.08662  0.53054  -0.00813 45  GLN A CA  
698  C C   . GLN A 45  ? 1.12200 1.46078 1.70123 0.11996  0.55225  -0.03061 45  GLN A C   
699  O O   . GLN A 45  ? 1.00652 1.37869 1.64513 0.12631  0.58796  -0.01851 45  GLN A O   
700  C CB  . GLN A 45  ? 1.23219 1.51115 1.68601 0.09131  0.53170  0.00131  45  GLN A CB  
701  C CG  . GLN A 45  ? 1.23320 1.49765 1.68046 0.06823  0.54194  0.04196  45  GLN A CG  
702  C CD  . GLN A 45  ? 1.29406 1.52058 1.59805 0.07756  0.54101  0.05131  45  GLN A CD  
703  O OE1 . GLN A 45  ? 1.24112 1.45226 1.44705 0.10203  0.53409  0.02661  45  GLN A OE1 
704  N NE2 . GLN A 45  ? 1.43894 1.64735 1.73290 0.05936  0.54270  0.08443  45  GLN A NE2 
713  N N   . LYS A 50  ? 0.89826 1.08944 1.27867 0.19976  0.35422  -0.22260 50  LYS A N   
714  C CA  . LYS A 50  ? 0.97250 1.13248 1.22781 0.20002  0.36261  -0.21684 50  LYS A CA  
715  C C   . LYS A 50  ? 0.96139 1.07160 1.15920 0.17818  0.29954  -0.22142 50  LYS A C   
716  O O   . LYS A 50  ? 0.99007 1.06453 1.09193 0.18598  0.28659  -0.23513 50  LYS A O   
717  C CB  . LYS A 50  ? 1.13171 1.31816 1.38353 0.18611  0.40988  -0.17731 50  LYS A CB  
720  N N   . VAL A 51  ? 1.00325 1.11261 1.26195 0.15264  0.26054  -0.21055 51  VAL A N   
721  C CA  . VAL A 51  ? 0.80952 0.87677 1.02471 0.13223  0.20665  -0.20967 51  VAL A CA  
722  C C   . VAL A 51  ? 0.77151 0.82911 1.04944 0.13232  0.16450  -0.21976 51  VAL A C   
723  O O   . VAL A 51  ? 0.76363 0.85096 1.12538 0.12752  0.16078  -0.21191 51  VAL A O   
724  C CB  . VAL A 51  ? 0.85993 0.93062 1.06270 0.10276  0.20211  -0.18010 51  VAL A CB  
725  C CG1 . VAL A 51  ? 0.83076 0.86341 0.99655 0.08461  0.15147  -0.17872 51  VAL A CG1 
726  C CG2 . VAL A 51  ? 1.06297 1.13754 1.19733 0.10582  0.24107  -0.16682 51  VAL A CG2 
736  N N   . SER A 52  ? 0.72683 0.74108 0.96735 0.13885  0.13060  -0.23669 52  SER A N   
737  C CA  A SER A 52  ? 0.66816 0.66464 0.95628 0.14256  0.09037  -0.24167 52  SER A CA  
738  C CA  B SER A 52  ? 0.66479 0.66119 0.95284 0.14257  0.09033  -0.24170 52  SER A CA  
739  C C   . SER A 52  ? 0.59225 0.57932 0.88099 0.11777  0.05660  -0.21732 52  SER A C   
740  O O   . SER A 52  ? 0.58583 0.56348 0.82274 0.09728  0.05558  -0.20188 52  SER A O   
741  C CB  A SER A 52  ? 0.65913 0.60578 0.91008 0.15584  0.06643  -0.26292 52  SER A CB  
742  C CB  B SER A 52  ? 0.65900 0.60555 0.90940 0.15563  0.06644  -0.26278 52  SER A CB  
743  O OG  A SER A 52  ? 0.72130 0.63014 0.91358 0.13416  0.04123  -0.25081 52  SER A OG  
744  O OG  B SER A 52  ? 0.72060 0.62910 0.91263 0.13401  0.04093  -0.25070 52  SER A OG  
755  N N   . VAL A 53  ? 0.50693 0.61771 0.78681 0.02376  -0.02213 -0.05309 53  VAL A N   
756  C CA  . VAL A 53  ? 0.52067 0.62490 0.78006 0.02572  -0.04072 -0.04807 53  VAL A CA  
757  C C   . VAL A 53  ? 0.51000 0.60544 0.73161 0.02687  -0.04232 -0.04327 53  VAL A C   
758  O O   . VAL A 53  ? 0.50840 0.59730 0.70153 0.02643  -0.04929 -0.03977 53  VAL A O   
759  C CB  . VAL A 53  ? 0.59426 0.69754 0.88157 0.02966  -0.06033 -0.04747 53  VAL A CB  
760  C CG1 . VAL A 53  ? 0.50890 0.60974 0.80972 0.03378  -0.06361 -0.04637 53  VAL A CG1 
761  C CG2 . VAL A 53  ? 0.56938 0.66306 0.83132 0.03053  -0.07937 -0.04295 53  VAL A CG2 
771  N N   . ASN A 54  ? 0.49125 0.58587 0.71312 0.02807  -0.03488 -0.04355 54  ASN A N   
772  C CA  . ASN A 54  ? 0.51032 0.59673 0.69999 0.02897  -0.03561 -0.03932 54  ASN A CA  
773  C C   . ASN A 54  ? 0.52349 0.60908 0.68264 0.02532  -0.02716 -0.03834 54  ASN A C   
774  O O   . ASN A 54  ? 0.44357 0.52174 0.57615 0.02575  -0.03309 -0.03436 54  ASN A O   
775  C CB  . ASN A 54  ? 0.46684 0.55356 0.66506 0.03007  -0.02662 -0.04100 54  ASN A CB  
776  C CG  . ASN A 54  ? 0.47004 0.55292 0.68890 0.03493  -0.03903 -0.03917 54  ASN A CG  
777  O OD1 . ASN A 54  ? 0.48588 0.56186 0.69993 0.03754  -0.05631 -0.03470 54  ASN A OD1 
778  N ND2 . ASN A 54  ? 0.53645 0.62227 0.77761 0.03596  -0.03046 -0.04263 54  ASN A ND2 
785  N N   . ARG A 55  ? 0.53101 0.62294 0.69384 0.02151  -0.01304 -0.04188 55  ARG A N   
786  C CA  . ARG A 55  ? 0.51267 0.60329 0.64874 0.01824  -0.00655 -0.04035 55  ARG A CA  
787  C C   . ARG A 55  ? 0.53833 0.62835 0.66783 0.01744  -0.01349 -0.03873 55  ARG A C   
788  O O   . ARG A 55  ? 0.51570 0.60111 0.62143 0.01696  -0.01555 -0.03575 55  ARG A O   
789  C CB  . ARG A 55  ? 0.56722 0.66167 0.70476 0.01392  0.00933  -0.04384 55  ARG A CB  
790  C CG  . ARG A 55  ? 0.57522 0.66750 0.68622 0.01063  0.01357  -0.04141 55  ARG A CG  
791  C CD  . ARG A 55  ? 0.61344 0.70505 0.71608 0.00633  0.02686  -0.04365 55  ARG A CD  
792  N NE  . ARG A 55  ? 0.75349 0.84712 0.86673 0.00247  0.03640  -0.04662 55  ARG A NE  
793  C CZ  . ARG A 55  ? 0.72304 0.81790 0.85437 0.00081  0.04670  -0.05168 55  ARG A CZ  
794  N NH1 . ARG A 55  ? 0.63811 0.73316 0.78123 0.00310  0.04802  -0.05450 55  ARG A NH1 
795  N NH2 . ARG A 55  ? 0.66035 0.75536 0.79885 -0.00342 0.05696  -0.05411 55  ARG A NH2 
809  N N   . TYR A 56  ? 0.48027 0.57474 0.63248 0.01707  -0.01649 -0.04116 56  TYR A N   
810  C CA  . TYR A 56  ? 0.51034 0.60376 0.65738 0.01599  -0.02307 -0.04030 56  TYR A CA  
811  C C   . TYR A 56  ? 0.51382 0.59843 0.64404 0.01870  -0.03797 -0.03710 56  TYR A C   
812  O O   . TYR A 56  ? 0.49451 0.57434 0.60439 0.01754  -0.03995 -0.03551 56  TYR A O   
813  C CB  . TYR A 56  ? 0.61144 0.71122 0.78962 0.01495  -0.02406 -0.04399 56  TYR A CB  
814  C CG  . TYR A 56  ? 0.68805 0.78828 0.86136 0.01201  -0.02362 -0.04410 56  TYR A CG  
815  C CD1 . TYR A 56  ? 0.68904 0.78364 0.85049 0.01295  -0.03668 -0.04257 56  TYR A CD1 
816  C CD2 . TYR A 56  ? 0.83643 0.94076 1.01463 0.00792  -0.00965 -0.04570 56  TYR A CD2 
817  C CE1 . TYR A 56  ? 0.77751 0.87204 0.93561 0.01025  -0.03587 -0.04311 56  TYR A CE1 
818  C CE2 . TYR A 56  ? 0.95963 1.06355 1.13397 0.00529  -0.00923 -0.04531 56  TYR A CE2 
819  C CZ  . TYR A 56  ? 0.93183 1.03155 1.09763 0.00666  -0.02236 -0.04423 56  TYR A CZ  
820  O OH  . TYR A 56  ? 1.01744 1.11633 1.18070 0.00405  -0.02166 -0.04432 56  TYR A OH  
830  N N   . ASN A 57  ? 0.51099 0.59169 0.64840 0.02207  -0.04819 -0.03609 57  ASN A N   
831  C CA  . ASN A 57  ? 0.51810 0.58672 0.63385 0.02397  -0.06183 -0.03256 57  ASN A CA  
832  C C   . ASN A 57  ? 0.51122 0.57277 0.59556 0.02356  -0.05542 -0.02954 57  ASN A C   
833  O O   . ASN A 57  ? 0.53051 0.58170 0.59079 0.02320  -0.06075 -0.02752 57  ASN A O   
834  C CB  . ASN A 57  ? 0.50455 0.56878 0.63408 0.02759  -0.07481 -0.03114 57  ASN A CB  
835  C CG  . ASN A 57  ? 0.54143 0.58968 0.64514 0.02885  -0.09034 -0.02711 57  ASN A CG  
836  O OD1 . ASN A 57  ? 0.59361 0.63658 0.68960 0.02752  -0.09983 -0.02766 57  ASN A OD1 
837  N ND2 . ASN A 57  ? 0.53764 0.57655 0.62628 0.03093  -0.09239 -0.02320 57  ASN A ND2 
844  N N   . PHE A 58  ? 0.46666 0.53273 0.55131 0.02327  -0.04370 -0.02968 58  PHE A N   
845  C CA  . PHE A 58  ? 0.44417 0.50527 0.50403 0.02248  -0.03699 -0.02740 58  PHE A CA  
846  C C   . PHE A 58  ? 0.47964 0.54105 0.52621 0.01981  -0.03264 -0.02753 58  PHE A C   
847  O O   . PHE A 58  ? 0.47394 0.52726 0.49956 0.01956  -0.03266 -0.02560 58  PHE A O   
848  C CB  . PHE A 58  ? 0.50296 0.56983 0.56877 0.02195  -0.02592 -0.02852 58  PHE A CB  
849  C CG  . PHE A 58  ? 0.49542 0.55714 0.54072 0.02152  -0.02076 -0.02630 58  PHE A CG  
850  C CD1 . PHE A 58  ? 0.48701 0.55034 0.52047 0.01898  -0.01425 -0.02608 58  PHE A CD1 
851  C CD2 . PHE A 58  ? 0.55387 0.60906 0.59456 0.02362  -0.02264 -0.02436 58  PHE A CD2 
852  C CE1 . PHE A 58  ? 0.56472 0.62406 0.58425 0.01853  -0.00978 -0.02445 58  PHE A CE1 
853  C CE2 . PHE A 58  ? 0.51318 0.56382 0.53797 0.02287  -0.01703 -0.02271 58  PHE A CE2 
854  C CZ  . PHE A 58  ? 0.46373 0.51700 0.47932 0.02031  -0.01065 -0.02303 58  PHE A CZ  
864  N N   . LEU A 59  ? 0.51866 0.58851 0.57827 0.01765  -0.02798 -0.02985 59  LEU A N   
865  C CA  . LEU A 59  ? 0.50691 0.57665 0.55673 0.01533  -0.02485 -0.02964 59  LEU A CA  
866  C C   . LEU A 59  ? 0.46170 0.52332 0.50230 0.01578  -0.03447 -0.02958 59  LEU A C   
867  O O   . LEU A 59  ? 0.48940 0.54451 0.51208 0.01505  -0.03296 -0.02863 59  LEU A O   
868  C CB  . LEU A 59  ? 0.40806 0.48651 0.47374 0.01272  -0.01837 -0.03166 59  LEU A CB  
869  C CG  . LEU A 59  ? 0.57725 0.65562 0.63799 0.01040  -0.01654 -0.03132 59  LEU A CG  
870  C CD1 . LEU A 59  ? 0.51493 0.59214 0.56033 0.00916  -0.00966 -0.02883 59  LEU A CD1 
871  C CD2 . LEU A 59  ? 0.50433 0.58918 0.58378 0.00795  -0.01235 -0.03341 59  LEU A CD2 
883  N N   . LEU A 60  ? 0.53698 0.59790 0.59024 0.01679  -0.04467 -0.03101 60  LEU A N   
884  C CA  . LEU A 60  ? 0.53143 0.58262 0.57372 0.01659  -0.05558 -0.03149 60  LEU A CA  
885  C C   . LEU A 60  ? 0.56754 0.60426 0.58149 0.01750  -0.05866 -0.02896 60  LEU A C   
886  O O   . LEU A 60  ? 0.55215 0.57922 0.54649 0.01599  -0.05912 -0.02943 60  LEU A O   
887  C CB  . LEU A 60  ? 0.52684 0.57917 0.58949 0.01765  -0.06856 -0.03319 60  LEU A CB  
888  C CG  . LEU A 60  ? 0.57589 0.64130 0.66963 0.01627  -0.06490 -0.03642 60  LEU A CG  
889  C CD1 . LEU A 60  ? 0.60566 0.67180 0.72318 0.01766  -0.07913 -0.03822 60  LEU A CD1 
890  C CD2 . LEU A 60  ? 0.63967 0.70653 0.72981 0.01320  -0.05991 -0.03800 60  LEU A CD2 
902  N N   . GLU A 61  ? 0.46870 0.50255 0.48007 0.01963  -0.05958 -0.02652 61  GLU A N   
903  C CA  . GLU A 61  ? 0.56776 0.58683 0.55154 0.02000  -0.05983 -0.02373 61  GLU A CA  
904  C C   . GLU A 61  ? 0.52155 0.54019 0.49161 0.01818  -0.04661 -0.02382 61  GLU A C   
905  O O   . GLU A 61  ? 0.53933 0.54468 0.48627 0.01700  -0.04527 -0.02346 61  GLU A O   
906  C CB  . GLU A 61  ? 0.57164 0.58929 0.55872 0.02250  -0.06100 -0.02092 61  GLU A CB  
907  C CG  . GLU A 61  ? 0.55415 0.56588 0.54894 0.02472  -0.07704 -0.01956 61  GLU A CG  
908  C CD  . GLU A 61  ? 0.61584 0.62766 0.61972 0.02755  -0.07770 -0.01687 61  GLU A CD  
909  O OE1 . GLU A 61  ? 0.55129 0.57006 0.55888 0.02755  -0.06514 -0.01706 61  GLU A OE1 
910  O OE2 . GLU A 61  ? 0.66229 0.66665 0.67053 0.02972  -0.09176 -0.01463 61  GLU A OE2 
917  N N   . SER A 62  ? 0.46023 0.49219 0.44453 0.01766  -0.03680 -0.02446 62  SER A N   
918  C CA  . SER A 62  ? 0.52735 0.55976 0.50329 0.01615  -0.02623 -0.02427 62  SER A CA  
919  C C   . SER A 62  ? 0.53650 0.56520 0.50625 0.01436  -0.02586 -0.02611 62  SER A C   
920  O O   . SER A 62  ? 0.53700 0.55872 0.49392 0.01339  -0.01962 -0.02620 62  SER A O   
921  C CB  . SER A 62  ? 0.51596 0.56170 0.50710 0.01557  -0.01873 -0.02426 62  SER A CB  
922  O OG  . SER A 62  ? 0.54915 0.59764 0.54642 0.01692  -0.01837 -0.02355 62  SER A OG  
928  N N   . LEU A 63  ? 0.52922 0.56240 0.51022 0.01375  -0.03160 -0.02802 63  LEU A N   
929  C CA  . LEU A 63  ? 0.55647 0.58526 0.53235 0.01192  -0.03184 -0.03025 63  LEU A CA  
930  C C   . LEU A 63  ? 0.58755 0.59901 0.54057 0.01138  -0.03798 -0.03142 63  LEU A C   
931  O O   . LEU A 63  ? 0.53944 0.54233 0.47941 0.00967  -0.03347 -0.03332 63  LEU A O   
932  C CB  . LEU A 63  ? 0.54152 0.57918 0.53693 0.01104  -0.03635 -0.03218 63  LEU A CB  
933  C CG  . LEU A 63  ? 0.58191 0.63363 0.59613 0.01055  -0.02905 -0.03113 63  LEU A CG  
934  C CD1 . LEU A 63  ? 0.55440 0.61321 0.58891 0.00959  -0.03291 -0.03316 63  LEU A CD1 
935  C CD2 . LEU A 63  ? 0.55519 0.60849 0.56613 0.00918  -0.02030 -0.02999 63  LEU A CD2 
947  N N   . GLU A 64  ? 0.57483 0.57947 0.52229 0.01258  -0.04857 -0.03041 64  GLU A N   
948  C CA  . GLU A 64  ? 0.72436 0.70883 0.64425 0.01152  -0.05539 -0.03078 64  GLU A CA  
949  C C   . GLU A 64  ? 0.68271 0.65557 0.57986 0.01067  -0.04386 -0.02967 64  GLU A C   
950  O O   . GLU A 64  ? 0.60785 0.56443 0.48151 0.00827  -0.04147 -0.03177 64  GLU A O   
951  C CB  . GLU A 64  ? 0.71524 0.69413 0.63436 0.01329  -0.06982 -0.02848 64  GLU A CB  
952  C CG  . GLU A 64  ? 1.02091 0.99459 0.94222 0.01241  -0.08599 -0.03074 64  GLU A CG  
953  C CD  . GLU A 64  ? 1.12991 1.10696 1.06831 0.01504  -0.10017 -0.02852 64  GLU A CD  
954  O OE1 . GLU A 64  ? 1.21207 1.17935 1.13744 0.01662  -0.10386 -0.02457 64  GLU A OE1 
955  O OE2 . GLU A 64  ? 1.05352 1.04285 1.02054 0.01550  -0.10697 -0.03073 64  GLU A OE2 
962  N N   . ASP A 65  ? 0.55528 0.53553 0.45978 0.01223  -0.03597 -0.02694 65  ASP A N   
963  C CA  . ASP A 65  ? 0.64404 0.61549 0.53323 0.01130  -0.02361 -0.02621 65  ASP A CA  
964  C C   . ASP A 65  ? 0.56167 0.53512 0.45359 0.00950  -0.01283 -0.02923 65  ASP A C   
965  O O   . ASP A 65  ? 0.59075 0.54997 0.46457 0.00758  -0.00452 -0.03081 65  ASP A O   
966  C CB  . ASP A 65  ? 0.60697 0.58847 0.50885 0.01315  -0.01820 -0.02330 65  ASP A CB  
967  C CG  . ASP A 65  ? 0.62701 0.59778 0.51424 0.01215  -0.00687 -0.02229 65  ASP A CG  
968  O OD1 . ASP A 65  ? 0.72791 0.67960 0.59023 0.01116  -0.00823 -0.02118 65  ASP A OD1 
969  O OD2 . ASP A 65  ? 0.58281 0.56313 0.48330 0.01204  0.00311  -0.02259 65  ASP A OD2 
974  N N   . LEU A 66  ? 0.54116 0.53123 0.45622 0.00995  -0.01210 -0.02999 66  LEU A N   
975  C CA  A LEU A 66  ? 0.62856 0.62063 0.54921 0.00862  -0.00346 -0.03224 66  LEU A CA  
976  C CA  B LEU A 66  ? 0.60781 0.59984 0.52840 0.00862  -0.00345 -0.03223 66  LEU A CA  
977  C C   . LEU A 66  ? 0.59945 0.57726 0.50398 0.00641  -0.00516 -0.03623 66  LEU A C   
978  O O   . LEU A 66  ? 0.64292 0.61186 0.53967 0.00482  0.00475  -0.03880 66  LEU A O   
979  C CB  A LEU A 66  ? 0.51336 0.52338 0.45880 0.00923  -0.00435 -0.03135 66  LEU A CB  
980  C CB  B LEU A 66  ? 0.55395 0.56385 0.49926 0.00922  -0.00424 -0.03137 66  LEU A CB  
981  C CG  A LEU A 66  ? 0.56039 0.57835 0.51931 0.00914  0.00468  -0.03034 66  LEU A CG  
982  C CG  B LEU A 66  ? 0.51731 0.53929 0.47701 0.01018  0.00105  -0.02846 66  LEU A CG  
983  C CD1 A LEU A 66  ? 0.56649 0.58358 0.52392 0.00976  0.01149  -0.02863 66  LEU A CD1 
984  C CD1 B LEU A 66  ? 0.55082 0.58615 0.52854 0.00992  -0.00107 -0.02744 66  LEU A CD1 
985  C CD2 A LEU A 66  ? 0.56499 0.59774 0.54263 0.00932  0.00172  -0.02833 66  LEU A CD2 
986  C CD2 B LEU A 66  ? 0.56492 0.58349 0.52463 0.00972  0.01125  -0.02862 66  LEU A CD2 
1009 N N   . GLN A 67  ? 0.63165 0.60672 0.53257 0.00608  -0.01761 -0.03733 67  GLN A N   
1010 C CA  . GLN A 67  ? 0.62706 0.58688 0.51030 0.00347  -0.02140 -0.04163 67  GLN A CA  
1011 C C   . GLN A 67  ? 0.71786 0.65485 0.56872 0.00137  -0.01542 -0.04289 67  GLN A C   
1012 O O   . GLN A 67  ? 0.69037 0.61527 0.52853 -0.00124 -0.00704 -0.04716 67  GLN A O   
1013 C CB  . GLN A 67  ? 0.64158 0.60118 0.52651 0.00351  -0.03827 -0.04207 67  GLN A CB  
1014 C CG  . GLN A 67  ? 0.74706 0.69166 0.61562 0.00039  -0.04517 -0.04704 67  GLN A CG  
1015 C CD  . GLN A 67  ? 0.75669 0.70823 0.64017 -0.00098 -0.03854 -0.05084 67  GLN A CD  
1016 O OE1 . GLN A 67  ? 0.71008 0.65650 0.58783 -0.00208 -0.02555 -0.05283 67  GLN A OE1 
1017 N NE2 . GLN A 67  ? 0.86175 0.82471 0.76671 -0.00092 -0.04716 -0.05185 67  GLN A NE2 
1026 N N   . ARG A 68  ? 0.69859 0.62836 0.53582 0.00225  -0.01830 -0.03928 68  ARG A N   
1027 C CA  . ARG A 68  ? 0.76981 0.67571 0.57381 -0.00025 -0.01142 -0.03978 68  ARG A CA  
1028 C C   . ARG A 68  ? 0.68214 0.58755 0.48978 -0.00123 0.00856  -0.04166 68  ARG A C   
1029 O O   . ARG A 68  ? 0.77080 0.65680 0.55577 -0.00459 0.01849  -0.04555 68  ARG A O   
1030 C CB  . ARG A 68  ? 0.77625 0.67627 0.56925 0.00123  -0.01744 -0.03447 68  ARG A CB  
1031 C CG  . ARG A 68  ? 0.84997 0.74473 0.63579 0.00193  -0.03804 -0.03255 68  ARG A CG  
1032 C CD  . ARG A 68  ? 1.04297 0.92158 0.80623 0.00227  -0.04293 -0.02748 68  ARG A CD  
1033 N NE  . ARG A 68  ? 1.05601 0.94960 0.83987 0.00538  -0.03613 -0.02360 68  ARG A NE  
1034 C CZ  . ARG A 68  ? 1.01861 0.93133 0.83086 0.00894  -0.04432 -0.02123 68  ARG A CZ  
1035 N NH1 . ARG A 68  ? 0.94885 0.86863 0.77484 0.01014  -0.05968 -0.02189 68  ARG A NH1 
1036 N NH2 . ARG A 68  ? 1.00762 0.93220 0.83602 0.01103  -0.03625 -0.01873 68  ARG A NH2 
1050 N N   . SER A 69  ? 0.63946 0.56501 0.47585 0.00136  0.01455  -0.03932 69  SER A N   
1051 C CA  . SER A 69  ? 0.68159 0.60855 0.52765 0.00078  0.03157  -0.04080 69  SER A CA  
1052 C C   . SER A 69  ? 0.65385 0.57952 0.50646 -0.00082 0.03836  -0.04588 69  SER A C   
1053 O O   . SER A 69  ? 0.66226 0.57635 0.50873 -0.00291 0.05300  -0.04939 69  SER A O   
1054 C CB  . SER A 69  ? 0.64890 0.59774 0.52484 0.00370  0.03285  -0.03707 69  SER A CB  
1055 O OG  . SER A 69  ? 0.67770 0.62588 0.54767 0.00489  0.02931  -0.03315 69  SER A OG  
1061 N N   . PHE A 70  ? 0.59487 0.53201 0.46189 0.00002  0.02900  -0.04653 70  PHE A N   
1062 C CA  . PHE A 70  ? 0.65511 0.59113 0.53034 -0.00135 0.03510  -0.05113 70  PHE A CA  
1063 C C   . PHE A 70  ? 0.66370 0.57543 0.50807 -0.00519 0.03742  -0.05697 70  PHE A C   
1064 O O   . PHE A 70  ? 0.68578 0.58854 0.52919 -0.00721 0.04984  -0.06198 70  PHE A O   
1065 C CB  . PHE A 70  ? 0.65558 0.60876 0.55336 0.00012  0.02493  -0.04998 70  PHE A CB  
1066 C CG  . PHE A 70  ? 0.65717 0.63060 0.58496 0.00268  0.02715  -0.04576 70  PHE A CG  
1067 C CD1 . PHE A 70  ? 0.65057 0.62652 0.59406 0.00295  0.03839  -0.04640 70  PHE A CD1 
1068 C CD2 . PHE A 70  ? 0.57676 0.56529 0.51693 0.00453  0.01777  -0.04136 70  PHE A CD2 
1069 C CE1 . PHE A 70  ? 0.65248 0.64507 0.62141 0.00497  0.03788  -0.04202 70  PHE A CE1 
1070 C CE2 . PHE A 70  ? 0.57426 0.57812 0.53662 0.00605  0.01923  -0.03760 70  PHE A CE2 
1071 C CZ  . PHE A 70  ? 0.63711 0.64267 0.61285 0.00626  0.02819  -0.03759 70  PHE A CZ  
1081 N N   . GLN A 71  ? 0.72083 0.62054 0.53966 -0.00646 0.02501  -0.05660 71  GLN A N   
1082 C CA  . GLN A 71  ? 0.78866 0.66214 0.57268 -0.01085 0.02500  -0.06212 71  GLN A CA  
1083 C C   . GLN A 71  ? 0.81063 0.66279 0.57015 -0.01379 0.04270  -0.06443 71  GLN A C   
1084 O O   . GLN A 71  ? 0.77402 0.60674 0.51415 -0.01780 0.05289  -0.07101 71  GLN A O   
1085 C CB  . GLN A 71  ? 0.83636 0.70105 0.59927 -0.01145 0.00536  -0.06019 71  GLN A CB  
1086 C CG  . GLN A 71  ? 1.07042 0.94927 0.85334 -0.01038 -0.01034 -0.06097 71  GLN A CG  
1087 C CD  . GLN A 71  ? 1.32466 1.19793 1.09511 -0.01029 -0.03130 -0.05856 71  GLN A CD  
1088 O OE1 . GLN A 71  ? 1.18211 1.04110 0.92823 -0.01064 -0.03536 -0.05532 71  GLN A OE1 
1089 N NE2 . GLN A 71  ? 1.06135 0.94553 0.85045 -0.00984 -0.04488 -0.05992 71  GLN A NE2 
1098 N N   . ALA A 72  ? 0.74654 0.60146 0.50757 -0.01217 0.04797  -0.05957 72  ALA A N   
1099 C CA  . ALA A 72  ? 0.79612 0.63238 0.53911 -0.01506 0.06723  -0.06163 72  ALA A CA  
1100 C C   . ALA A 72  ? 0.80303 0.64347 0.56871 -0.01565 0.08621  -0.06691 72  ALA A C   
1101 O O   . ALA A 72  ? 0.89314 0.71354 0.64192 -0.01932 0.10440  -0.07143 72  ALA A O   
1102 C CB  . ALA A 72  ? 0.80562 0.64838 0.55452 -0.01280 0.06912  -0.05530 72  ALA A CB  
1108 N N   . ARG A 73  ? 0.77772 0.64228 0.58134 -0.01235 0.08279  -0.06639 73  ARG A N   
1109 C CA  . ARG A 73  ? 0.73920 0.60973 0.57019 -0.01212 0.09834  -0.07029 73  ARG A CA  
1110 C C   . ARG A 73  ? 0.77516 0.64333 0.60972 -0.01339 0.09687  -0.07584 73  ARG A C   
1111 O O   . ARG A 73  ? 0.70863 0.58825 0.57478 -0.01183 0.10396  -0.07742 73  ARG A O   
1112 C CB  . ARG A 73  ? 0.72855 0.62660 0.60118 -0.00755 0.09617  -0.06474 73  ARG A CB  
1113 C CG  . ARG A 73  ? 0.82346 0.72442 0.69712 -0.00652 0.09954  -0.06020 73  ARG A CG  
1114 C CD  . ARG A 73  ? 0.78130 0.70868 0.69181 -0.00246 0.09316  -0.05471 73  ARG A CD  
1115 N NE  . ARG A 73  ? 0.82071 0.74993 0.73858 -0.00206 0.10086  -0.05229 73  ARG A NE  
1116 C CZ  . ARG A 73  ? 0.88692 0.81133 0.78630 -0.00221 0.09694  -0.04895 73  ARG A CZ  
1117 N NH1 . ARG A 73  ? 0.82773 0.74541 0.70088 -0.00244 0.08432  -0.04722 73  ARG A NH1 
1118 N NH2 . ARG A 73  ? 0.88254 0.80880 0.79195 -0.00209 0.10521  -0.04726 73  ARG A NH2 
1132 N N   . GLY A 74  ? 0.76968 0.62263 0.57351 -0.01625 0.08689  -0.07878 74  GLY A N   
1133 C CA  . GLY A 74  ? 0.72262 0.56987 0.52618 -0.01831 0.08618  -0.08516 74  GLY A CA  
1134 C C   . GLY A 74  ? 0.75348 0.62333 0.58555 -0.01518 0.07123  -0.08221 74  GLY A C   
1135 O O   . GLY A 74  ? 0.70449 0.57272 0.54423 -0.01643 0.07204  -0.08713 74  GLY A O   
1139 N N   . SER A 75  ? 0.70751 0.59724 0.55528 -0.01149 0.05869  -0.07462 75  SER A N   
1140 C CA  . SER A 75  ? 0.68946 0.59996 0.56405 -0.00894 0.04640  -0.07144 75  SER A CA  
1141 C C   . SER A 75  ? 0.70580 0.62060 0.57093 -0.00833 0.02812  -0.06790 75  SER A C   
1142 O O   . SER A 75  ? 0.67037 0.56939 0.50579 -0.01020 0.02275  -0.06866 75  SER A O   
1143 C CB  . SER A 75  ? 0.65432 0.58649 0.56374 -0.00514 0.05049  -0.06581 75  SER A CB  
1144 O OG  . SER A 75  ? 0.72403 0.67214 0.65695 -0.00361 0.04202  -0.06333 75  SER A OG  
1150 N N   . ARG A 76  ? 0.69238 0.62701 0.58278 -0.00599 0.01863  -0.06410 76  ARG A N   
1151 C CA  . ARG A 76  ? 0.69320 0.63482 0.58272 -0.00494 0.00316  -0.06067 76  ARG A CA  
1152 C C   . ARG A 76  ? 0.66925 0.63423 0.59054 -0.00217 0.00011  -0.05566 76  ARG A C   
1153 O O   . ARG A 76  ? 0.65202 0.62533 0.59295 -0.00175 0.00612  -0.05534 76  ARG A O   
1154 C CB  . ARG A 76  ? 0.78854 0.71892 0.66365 -0.00774 -0.00927 -0.06530 76  ARG A CB  
1155 C CG  . ARG A 76  ? 0.71925 0.65708 0.61456 -0.00865 -0.01095 -0.06825 76  ARG A CG  
1156 C CD  . ARG A 76  ? 0.79872 0.72616 0.68212 -0.01162 -0.02508 -0.07306 76  ARG A CD  
1157 N NE  . ARG A 76  ? 0.80086 0.72457 0.69123 -0.01409 -0.02162 -0.07878 76  ARG A NE  
1158 C CZ  . ARG A 76  ? 0.76610 0.70091 0.67965 -0.01442 -0.02856 -0.07941 76  ARG A CZ  
1159 N NH1 . ARG A 76  ? 0.68020 0.63043 0.61278 -0.01267 -0.03874 -0.07516 76  ARG A NH1 
1160 N NH2 . ARG A 76  ? 0.78007 0.70949 0.69862 -0.01682 -0.02402 -0.08481 76  ARG A NH2 
1174 N N   . LEU A 77  ? 0.63274 0.60658 0.55801 -0.00050 -0.00910 -0.05169 77  LEU A N   
1175 C CA  . LEU A 77  ? 0.63541 0.62875 0.58674 0.00129  -0.01169 -0.04751 77  LEU A CA  
1176 C C   . LEU A 77  ? 0.58276 0.57996 0.54535 -0.00006 -0.02058 -0.04971 77  LEU A C   
1177 O O   . LEU A 77  ? 0.52981 0.51857 0.48193 -0.00134 -0.03055 -0.05279 77  LEU A O   
1178 C CB  . LEU A 77  ? 0.57886 0.57927 0.53126 0.00339  -0.01555 -0.04326 77  LEU A CB  
1179 C CG  . LEU A 77  ? 0.58173 0.59970 0.55707 0.00459  -0.01738 -0.03962 77  LEU A CG  
1180 C CD1 . LEU A 77  ? 0.58072 0.60712 0.56781 0.00510  -0.00821 -0.03651 77  LEU A CD1 
1181 C CD2 . LEU A 77  ? 0.60274 0.62424 0.57710 0.00628  -0.02251 -0.03723 77  LEU A CD2 
1193 N N   . LEU A 78  ? 0.55458 0.56355 0.53868 -0.00005 -0.01733 -0.04792 78  LEU A N   
1194 C CA  . LEU A 78  ? 0.56662 0.58082 0.56587 -0.00157 -0.02351 -0.04951 78  LEU A CA  
1195 C C   . LEU A 78  ? 0.51822 0.54692 0.53484 -0.00053 -0.02533 -0.04529 78  LEU A C   
1196 O O   . LEU A 78  ? 0.50957 0.54657 0.53508 0.00015  -0.01840 -0.04096 78  LEU A O   
1197 C CB  . LEU A 78  ? 0.54607 0.56013 0.55567 -0.00294 -0.01722 -0.05060 78  LEU A CB  
1198 C CG  . LEU A 78  ? 0.64409 0.64347 0.63943 -0.00421 -0.01230 -0.05562 78  LEU A CG  
1199 C CD1 . LEU A 78  ? 0.61746 0.61847 0.62854 -0.00514 -0.00634 -0.05606 78  LEU A CD1 
1200 C CD2 . LEU A 78  ? 0.60409 0.58974 0.58122 -0.00651 -0.02105 -0.06185 78  LEU A CD2 
1212 N N   . VAL A 79  ? 0.53646 0.56706 0.55786 -0.00063 -0.03472 -0.04672 79  VAL A N   
1213 C CA  . VAL A 79  ? 0.54331 0.58661 0.58376 -0.00012 -0.03517 -0.04414 79  VAL A CA  
1214 C C   . VAL A 79  ? 0.55611 0.60439 0.61679 -0.00256 -0.03586 -0.04602 79  VAL A C   
1215 O O   . VAL A 79  ? 0.53350 0.58016 0.60234 -0.00367 -0.04514 -0.04994 79  VAL A O   
1216 C CB  . VAL A 79  ? 0.60987 0.65296 0.64934 0.00146  -0.04422 -0.04457 79  VAL A CB  
1217 C CG1 . VAL A 79  ? 0.68539 0.74120 0.74818 0.00165  -0.04277 -0.04317 79  VAL A CG1 
1218 C CG2 . VAL A 79  ? 0.62848 0.66564 0.64755 0.00358  -0.04216 -0.04222 79  VAL A CG2 
1228 N N   . LEU A 80  ? 0.49679 0.55021 0.56586 -0.00363 -0.02662 -0.04299 80  LEU A N   
1229 C CA  . LEU A 80  ? 0.53362 0.59055 0.62121 -0.00636 -0.02503 -0.04400 80  LEU A CA  
1230 C C   . LEU A 80  ? 0.52331 0.58967 0.62982 -0.00725 -0.02355 -0.04321 80  LEU A C   
1231 O O   . LEU A 80  ? 0.55998 0.63102 0.66457 -0.00627 -0.01858 -0.03994 80  LEU A O   
1232 C CB  . LEU A 80  ? 0.53365 0.58972 0.62075 -0.00733 -0.01603 -0.04022 80  LEU A CB  
1233 C CG  . LEU A 80  ? 0.59521 0.64233 0.66903 -0.00650 -0.01503 -0.04140 80  LEU A CG  
1234 C CD1 . LEU A 80  ? 0.57090 0.61832 0.64878 -0.00691 -0.00724 -0.03646 80  LEU A CD1 
1235 C CD2 . LEU A 80  ? 0.65042 0.68974 0.72423 -0.00816 -0.02091 -0.04793 80  LEU A CD2 
1247 N N   . ARG A 81  ? 0.53295 0.60155 0.65891 -0.00941 -0.02732 -0.04687 81  ARG A N   
1248 C CA  . ARG A 81  ? 0.56594 0.64306 0.71506 -0.01078 -0.02430 -0.04733 81  ARG A CA  
1249 C C   . ARG A 81  ? 0.51448 0.59352 0.67406 -0.01424 -0.01254 -0.04477 81  ARG A C   
1250 O O   . ARG A 81  ? 0.57564 0.65080 0.73812 -0.01618 -0.01227 -0.04556 81  ARG A O   
1251 C CB  . ARG A 81  ? 0.59572 0.67428 0.76459 -0.01127 -0.03597 -0.05307 81  ARG A CB  
1252 C CG  . ARG A 81  ? 0.58897 0.66768 0.75525 -0.00818 -0.04653 -0.05427 81  ARG A CG  
1253 C CD  . ARG A 81  ? 0.65860 0.72623 0.79693 -0.00634 -0.05629 -0.05490 81  ARG A CD  
1254 N NE  . ARG A 81  ? 0.61145 0.67637 0.74923 -0.00418 -0.07011 -0.05645 81  ARG A NE  
1255 C CZ  . ARG A 81  ? 0.62460 0.67924 0.73546 -0.00223 -0.07697 -0.05560 81  ARG A CZ  
1256 N NH1 . ARG A 81  ? 0.55261 0.59946 0.63685 -0.00214 -0.07032 -0.05404 81  ARG A NH1 
1257 N NH2 . ARG A 81  ? 0.61216 0.66333 0.72378 -0.00045 -0.09065 -0.05620 81  ARG A NH2 
1271 N N   . GLY A 82  ? 0.57535 0.65865 0.73892 -0.01535 -0.00252 -0.04177 82  GLY A N   
1272 C CA  . GLY A 82  ? 0.58349 0.66623 0.75415 -0.01937 0.00960  -0.03889 82  GLY A CA  
1273 C C   . GLY A 82  ? 0.58360 0.66398 0.73522 -0.01978 0.01867  -0.03294 82  GLY A C   
1274 O O   . GLY A 82  ? 0.60850 0.69046 0.74859 -0.01721 0.01694  -0.03227 82  GLY A O   
1278 N N   . LYS A 83  ? 0.58811 0.66346 0.73583 -0.02334 0.02767  -0.02851 83  LYS A N   
1279 C CA  . LYS A 83  ? 0.62191 0.69208 0.74908 -0.02472 0.03487  -0.02220 83  LYS A CA  
1280 C C   . LYS A 83  ? 0.62134 0.68584 0.73188 -0.02302 0.03003  -0.01711 83  LYS A C   
1281 O O   . LYS A 83  ? 0.62326 0.68539 0.74024 -0.02297 0.02695  -0.01741 83  LYS A O   
1282 C CB  . LYS A 83  ? 0.70604 0.77106 0.83662 -0.03044 0.04803  -0.01968 83  LYS A CB  
1283 C CG  . LYS A 83  ? 0.81378 0.88413 0.96781 -0.03281 0.05544  -0.02547 83  LYS A CG  
1284 C CD  . LYS A 83  ? 1.05458 1.12559 1.20080 -0.03332 0.06243  -0.02618 83  LYS A CD  
1285 C CE  . LYS A 83  ? 1.12882 1.18903 1.25930 -0.03934 0.07752  -0.02181 83  LYS A CE  
1286 N NZ  . LYS A 83  ? 1.22458 1.27957 1.32626 -0.03904 0.07787  -0.01822 83  LYS A NZ  
1300 N N   . PRO A 84  ? 0.58329 0.64542 0.67479 -0.02162 0.02904  -0.01284 84  PRO A N   
1301 C CA  . PRO A 84  ? 0.56997 0.62737 0.65119 -0.01975 0.02407  -0.00827 84  PRO A CA  
1302 C C   . PRO A 84  ? 0.53639 0.58610 0.61859 -0.02284 0.02743  -0.00306 84  PRO A C   
1303 O O   . PRO A 84  ? 0.62382 0.67112 0.71017 -0.02120 0.02331  -0.00226 84  PRO A O   
1304 C CB  . PRO A 84  ? 0.56734 0.62352 0.63093 -0.01886 0.02322  -0.00446 84  PRO A CB  
1305 C CG  . PRO A 84  ? 0.61365 0.67548 0.67861 -0.01861 0.02557  -0.00897 84  PRO A CG  
1306 C CD  . PRO A 84  ? 0.57902 0.64277 0.66011 -0.02156 0.03181  -0.01264 84  PRO A CD  
1314 N N   . GLU A 85  ? 0.58667 0.63106 0.66493 -0.02757 0.03572  0.00039  85  GLU A N   
1315 C CA  . GLU A 85  ? 0.57665 0.61112 0.65224 -0.03094 0.03908  0.00677  85  GLU A CA  
1316 C C   . GLU A 85  ? 0.65337 0.68887 0.74936 -0.03155 0.03984  0.00338  85  GLU A C   
1317 O O   . GLU A 85  ? 0.61806 0.64593 0.71462 -0.03279 0.03991  0.00831  85  GLU A O   
1318 C CB  . GLU A 85  ? 0.77078 0.79655 0.83408 -0.03686 0.04964  0.01086  85  GLU A CB  
1319 C CG  . GLU A 85  ? 0.91728 0.94335 0.96412 -0.03748 0.05188  0.01041  85  GLU A CG  
1320 C CD  . GLU A 85  ? 0.79229 0.82791 0.85390 -0.03736 0.05760  0.00196  85  GLU A CD  
1321 O OE1 . GLU A 85  ? 0.80347 0.83934 0.88074 -0.04070 0.06652  -0.00116 85  GLU A OE1 
1322 O OE2 . GLU A 85  ? 0.76489 0.80763 0.82457 -0.03388 0.05294  -0.00146 85  GLU A OE2 
1329 N N   . GLU A 86  ? 0.60828 0.65230 0.72160 -0.03080 0.03946  -0.00480 86  GLU A N   
1330 C CA  A GLU A 86  ? 0.68171 0.72679 0.81514 -0.03159 0.03845  -0.00924 86  GLU A CA  
1331 C CA  B GLU A 86  ? 0.68157 0.72674 0.81511 -0.03159 0.03845  -0.00930 86  GLU A CA  
1332 C C   . GLU A 86  ? 0.65609 0.70398 0.79243 -0.02720 0.02827  -0.01385 86  GLU A C   
1333 O O   . GLU A 86  ? 0.61410 0.65806 0.75849 -0.02757 0.02672  -0.01466 86  GLU A O   
1334 C CB  A GLU A 86  ? 0.69382 0.74524 0.84712 -0.03407 0.04297  -0.01574 86  GLU A CB  
1335 C CB  B GLU A 86  ? 0.69378 0.74545 0.84727 -0.03397 0.04275  -0.01593 86  GLU A CB  
1336 C CG  A GLU A 86  ? 0.76111 0.80808 0.91306 -0.03932 0.05648  -0.01241 86  GLU A CG  
1337 C CG  B GLU A 86  ? 0.72578 0.78640 0.89035 -0.03035 0.03293  -0.02411 86  GLU A CG  
1338 C CD  A GLU A 86  ? 0.78998 0.84488 0.96302 -0.04088 0.06161  -0.01943 86  GLU A CD  
1339 C CD  B GLU A 86  ? 0.74401 0.81176 0.92864 -0.03202 0.03608  -0.02957 86  GLU A CD  
1340 O OE1 A GLU A 86  ? 0.76301 0.82678 0.94266 -0.03702 0.05347  -0.02484 86  GLU A OE1 
1341 O OE1 B GLU A 86  ? 0.78388 0.84996 0.98069 -0.03664 0.04717  -0.02888 86  GLU A OE1 
1342 O OE2 A GLU A 86  ? 0.68472 0.73614 0.86870 -0.04609 0.07413  -0.01939 86  GLU A OE2 
1343 O OE2 B GLU A 86  ? 0.63612 0.71030 0.82525 -0.02883 0.02781  -0.03445 86  GLU A OE2 
1356 N N   . VAL A 87  ? 0.59534 0.64827 0.72385 -0.02345 0.02230  -0.01688 87  VAL A N   
1357 C CA  . VAL A 87  ? 0.60175 0.65485 0.72929 -0.02001 0.01424  -0.02178 87  VAL A CA  
1358 C C   . VAL A 87  ? 0.53691 0.58389 0.65604 -0.01819 0.01362  -0.01752 87  VAL A C   
1359 O O   . VAL A 87  ? 0.50838 0.55149 0.63230 -0.01746 0.01128  -0.02088 87  VAL A O   
1360 C CB  . VAL A 87  ? 0.69313 0.75141 0.81287 -0.01695 0.00912  -0.02536 87  VAL A CB  
1361 C CG1 . VAL A 87  ? 0.71308 0.76798 0.82352 -0.01370 0.00298  -0.02867 87  VAL A CG1 
1362 C CG2 . VAL A 87  ? 0.67333 0.73730 0.80761 -0.01814 0.00689  -0.03102 87  VAL A CG2 
1372 N N   . PHE A 88  ? 0.54733 0.59283 0.65485 -0.01749 0.01532  -0.01056 88  PHE A N   
1373 C CA  . PHE A 88  ? 0.48423 0.52536 0.58710 -0.01491 0.01306  -0.00693 88  PHE A CA  
1374 C C   . PHE A 88  ? 0.50344 0.53766 0.61607 -0.01611 0.01449  -0.00414 88  PHE A C   
1375 O O   . PHE A 88  ? 0.49690 0.52824 0.61430 -0.01379 0.01280  -0.00658 88  PHE A O   
1376 C CB  . PHE A 88  ? 0.50845 0.54929 0.59864 -0.01437 0.01261  0.00005  88  PHE A CB  
1377 C CG  . PHE A 88  ? 0.53536 0.58157 0.61722 -0.01142 0.00988  -0.00301 88  PHE A CG  
1378 C CD1 . PHE A 88  ? 0.52263 0.56935 0.60580 -0.00820 0.00748  -0.00790 88  PHE A CD1 
1379 C CD2 . PHE A 88  ? 0.61394 0.66315 0.68584 -0.01234 0.01084  -0.00122 88  PHE A CD2 
1380 C CE1 . PHE A 88  ? 0.61753 0.66769 0.69244 -0.00587 0.00587  -0.01030 88  PHE A CE1 
1381 C CE2 . PHE A 88  ? 0.57336 0.62699 0.63869 -0.00975 0.00858  -0.00391 88  PHE A CE2 
1382 C CZ  . PHE A 88  ? 0.56966 0.62379 0.63657 -0.00647 0.00596  -0.00808 88  PHE A CZ  
1392 N N   . PRO A 89  ? 0.51466 0.54473 0.63071 -0.01981 0.01851  0.00078  89  PRO A N   
1393 C CA  . PRO A 89  ? 0.53343 0.55600 0.66002 -0.02083 0.01965  0.00352  89  PRO A CA  
1394 C C   . PRO A 89  ? 0.53434 0.55739 0.67393 -0.02022 0.01877  -0.00540 89  PRO A C   
1395 O O   . PRO A 89  ? 0.53109 0.54866 0.67808 -0.01890 0.01830  -0.00551 89  PRO A O   
1396 C CB  . PRO A 89  ? 0.56032 0.57823 0.68715 -0.02587 0.02568  0.00876  89  PRO A CB  
1397 C CG  . PRO A 89  ? 0.57466 0.59501 0.68623 -0.02709 0.02754  0.01157  89  PRO A CG  
1398 C CD  . PRO A 89  ? 0.55556 0.58582 0.66550 -0.02355 0.02349  0.00416  89  PRO A CD  
1406 N N   . ARG A 90  ? 0.53003 0.55859 0.67288 -0.02124 0.01795  -0.01323 90  ARG A N   
1407 C CA  A ARG A 90  ? 0.57705 0.60424 0.72875 -0.02127 0.01524  -0.02231 90  ARG A CA  
1408 C CA  B ARG A 90  ? 0.57618 0.60339 0.72785 -0.02127 0.01523  -0.02231 90  ARG A CA  
1409 C C   . ARG A 90  ? 0.57426 0.59899 0.71746 -0.01758 0.01224  -0.02639 90  ARG A C   
1410 O O   . ARG A 90  ? 0.54076 0.55897 0.68936 -0.01729 0.01299  -0.02992 90  ARG A O   
1411 C CB  A ARG A 90  ? 0.64505 0.67821 0.80205 -0.02311 0.01244  -0.02916 90  ARG A CB  
1412 C CB  B ARG A 90  ? 0.64643 0.67962 0.80329 -0.02307 0.01240  -0.02918 90  ARG A CB  
1413 C CG  A ARG A 90  ? 0.71220 0.74423 0.86600 -0.02182 0.00537  -0.03874 90  ARG A CG  
1414 C CG  B ARG A 90  ? 0.70570 0.73600 0.86919 -0.02381 0.00708  -0.03894 90  ARG A CG  
1415 C CD  A ARG A 90  ? 0.75886 0.79505 0.92452 -0.02436 0.00036  -0.04527 90  ARG A CD  
1416 C CD  B ARG A 90  ? 0.75139 0.78478 0.90532 -0.02215 -0.00060 -0.04534 90  ARG A CD  
1417 N NE  A ARG A 90  ? 0.77422 0.81879 0.94256 -0.02455 0.00144  -0.04263 90  ARG A NE  
1418 N NE  B ARG A 90  ? 0.74879 0.79066 0.90906 -0.02302 -0.00182 -0.04475 90  ARG A NE  
1419 C CZ  A ARG A 90  ? 0.74434 0.79219 0.92547 -0.02751 0.00839  -0.03887 90  ARG A CZ  
1420 C CZ  B ARG A 90  ? 0.72331 0.76905 0.87609 -0.02112 -0.00783 -0.04742 90  ARG A CZ  
1421 N NH1 A ARG A 90  ? 0.74057 0.78399 0.93240 -0.03059 0.01437  -0.03635 90  ARG A NH1 
1422 N NH1 B ARG A 90  ? 0.73412 0.77509 0.86983 -0.01862 -0.01321 -0.05066 90  ARG A NH1 
1423 N NH2 A ARG A 90  ? 0.76684 0.82137 0.94969 -0.02763 0.01043  -0.03772 90  ARG A NH2 
1424 N NH2 B ARG A 90  ? 0.62970 0.68318 0.79264 -0.02192 -0.00755 -0.04679 90  ARG A NH2 
1451 N N   . VAL A 91  ? 0.49430 0.52322 0.62457 -0.01504 0.01011  -0.02630 91  VAL A N   
1452 C CA  . VAL A 91  ? 0.54848 0.57389 0.67016 -0.01222 0.00900  -0.03100 91  VAL A CA  
1453 C C   . VAL A 91  ? 0.48983 0.51121 0.61498 -0.00995 0.01240  -0.02614 91  VAL A C   
1454 O O   . VAL A 91  ? 0.52196 0.53775 0.64665 -0.00843 0.01446  -0.03098 91  VAL A O   
1455 C CB  . VAL A 91  ? 0.54298 0.57314 0.65060 -0.01043 0.00598  -0.03254 91  VAL A CB  
1456 C CG1 . VAL A 91  ? 0.57119 0.60373 0.67835 -0.01219 0.00078  -0.03853 91  VAL A CG1 
1457 C CG2 . VAL A 91  ? 0.50945 0.54567 0.61356 -0.00956 0.00707  -0.02456 91  VAL A CG2 
1467 N N   . PHE A 92  ? 0.50675 0.52968 0.63544 -0.00991 0.01293  -0.01676 92  PHE A N   
1468 C CA  . PHE A 92  ? 0.50434 0.52291 0.64096 -0.00776 0.01392  -0.01153 92  PHE A CA  
1469 C C   . PHE A 92  ? 0.52950 0.54067 0.67962 -0.00812 0.01694  -0.01582 92  PHE A C   
1470 O O   . PHE A 92  ? 0.49851 0.50551 0.65474 -0.00578 0.01960  -0.01893 92  PHE A O   
1471 C CB  . PHE A 92  ? 0.48836 0.50633 0.62550 -0.00875 0.01202  -0.00029 92  PHE A CB  
1472 C CG  . PHE A 92  ? 0.53930 0.56230 0.66310 -0.00820 0.00917  0.00432  92  PHE A CG  
1473 C CD1 . PHE A 92  ? 0.48734 0.51533 0.60413 -0.00577 0.00845  -0.00015 92  PHE A CD1 
1474 C CD2 . PHE A 92  ? 0.54114 0.56203 0.65772 -0.01063 0.00771  0.01312  92  PHE A CD2 
1475 C CE1 . PHE A 92  ? 0.50675 0.53900 0.61227 -0.00548 0.00591  0.00370  92  PHE A CE1 
1476 C CE2 . PHE A 92  ? 0.52756 0.55157 0.63032 -0.01068 0.00523  0.01661  92  PHE A CE2 
1477 C CZ  . PHE A 92  ? 0.52269 0.55311 0.62132 -0.00793 0.00408  0.01173  92  PHE A CZ  
1487 N N   . ARG A 93  ? 0.54003 0.54900 0.69645 -0.01131 0.01760  -0.01652 93  ARG A N   
1488 C CA  . ARG A 93  ? 0.58968 0.59095 0.75984 -0.01213 0.02053  -0.02061 93  ARG A CA  
1489 C C   . ARG A 93  ? 0.56823 0.56617 0.73365 -0.01260 0.02158  -0.03308 93  ARG A C   
1490 O O   . ARG A 93  ? 0.54372 0.53411 0.71570 -0.01185 0.02546  -0.03812 93  ARG A O   
1491 C CB  . ARG A 93  ? 0.54747 0.54679 0.72650 -0.01587 0.02124  -0.01720 93  ARG A CB  
1492 C CG  . ARG A 93  ? 0.67826 0.67353 0.86335 -0.01585 0.02143  -0.00496 93  ARG A CG  
1493 C CD  . ARG A 93  ? 0.80102 0.79936 0.97603 -0.01863 0.02104  0.00218  93  ARG A CD  
1494 N NE  . ARG A 93  ? 0.75270 0.74459 0.92603 -0.01892 0.01980  0.01472  93  ARG A NE  
1495 C CZ  . ARG A 93  ? 0.82077 0.81314 0.97882 -0.02008 0.01820  0.02241  93  ARG A CZ  
1496 N NH1 . ARG A 93  ? 0.68499 0.68532 0.83081 -0.02062 0.01865  0.01873  93  ARG A NH1 
1497 N NH2 . ARG A 93  ? 0.75987 0.74311 0.91396 -0.02093 0.01570  0.03405  93  ARG A NH2 
1511 N N   . GLU A 94  ? 0.54683 0.54896 0.70016 -0.01402 0.01796  -0.03822 94  GLU A N   
1512 C CA  . GLU A 94  ? 0.58925 0.58555 0.73362 -0.01510 0.01681  -0.04955 94  GLU A CA  
1513 C C   . GLU A 94  ? 0.57057 0.56137 0.70474 -0.01247 0.02085  -0.05316 94  GLU A C   
1514 O O   . GLU A 94  ? 0.49799 0.47840 0.62951 -0.01341 0.02454  -0.06149 94  GLU A O   
1515 C CB  . GLU A 94  ? 0.63957 0.64131 0.77389 -0.01666 0.01000  -0.05276 94  GLU A CB  
1516 C CG  . GLU A 94  ? 0.57947 0.57314 0.70142 -0.01842 0.00572  -0.06381 94  GLU A CG  
1517 C CD  . GLU A 94  ? 0.54019 0.53919 0.65458 -0.01937 -0.00312 -0.06585 94  GLU A CD  
1518 O OE1 . GLU A 94  ? 0.58779 0.59499 0.71605 -0.02086 -0.00574 -0.06287 94  GLU A OE1 
1519 O OE2 . GLU A 94  ? 0.60640 0.60050 0.70167 -0.01874 -0.00701 -0.07032 94  GLU A OE2 
1526 N N   . TRP A 95  ? 0.54805 0.54473 0.67623 -0.00960 0.02112  -0.04756 95  TRP A N   
1527 C CA  . TRP A 95  ? 0.53790 0.52998 0.65767 -0.00737 0.02601  -0.05088 95  TRP A CA  
1528 C C   . TRP A 95  ? 0.50642 0.49672 0.64367 -0.00477 0.03212  -0.04681 95  TRP A C   
1529 O O   . TRP A 95  ? 0.58459 0.57105 0.72004 -0.00297 0.03808  -0.04981 95  TRP A O   
1530 C CB  . TRP A 95  ? 0.53344 0.53254 0.63901 -0.00581 0.02287  -0.04786 95  TRP A CB  
1531 C CG  . TRP A 95  ? 0.54124 0.54193 0.63210 -0.00775 0.01610  -0.05157 95  TRP A CG  
1532 C CD1 . TRP A 95  ? 0.56991 0.56425 0.65562 -0.01070 0.01231  -0.05908 95  TRP A CD1 
1533 C CD2 . TRP A 95  ? 0.50267 0.51143 0.58436 -0.00689 0.01127  -0.04812 95  TRP A CD2 
1534 N NE1 . TRP A 95  ? 0.51816 0.51652 0.59383 -0.01144 0.00448  -0.06001 95  TRP A NE1 
1535 C CE2 . TRP A 95  ? 0.51713 0.52442 0.59062 -0.00902 0.00444  -0.05340 95  TRP A CE2 
1536 C CE3 . TRP A 95  ? 0.53221 0.54880 0.61281 -0.00464 0.01155  -0.04137 95  TRP A CE3 
1537 C CZ2 . TRP A 95  ? 0.51731 0.53105 0.58373 -0.00856 -0.00146 -0.05186 95  TRP A CZ2 
1538 C CZ3 . TRP A 95  ? 0.51030 0.53282 0.58167 -0.00451 0.00671  -0.04038 95  TRP A CZ3 
1539 C CH2 . TRP A 95  ? 0.53379 0.55506 0.59922 -0.00627 0.00056  -0.04547 95  TRP A CH2 
1550 N N   . GLY A 96  ? 0.48875 0.48074 0.64388 -0.00465 0.03094  -0.04009 96  GLY A N   
1551 C CA  . GLY A 96  ? 0.49871 0.48879 0.67331 -0.00188 0.03439  -0.03528 96  GLY A CA  
1552 C C   . GLY A 96  ? 0.51946 0.51605 0.69389 0.00114  0.03267  -0.02915 96  GLY A C   
1553 O O   . GLY A 96  ? 0.51745 0.51156 0.70287 0.00357  0.03787  -0.03083 96  GLY A O   
1557 N N   . VAL A 97  ? 0.50798 0.51257 0.67138 0.00071  0.02594  -0.02258 97  VAL A N   
1558 C CA  . VAL A 97  ? 0.48213 0.49278 0.64210 0.00290  0.02343  -0.01785 97  VAL A CA  
1559 C C   . VAL A 97  ? 0.51629 0.52730 0.69522 0.00510  0.01980  -0.00864 97  VAL A C   
1560 O O   . VAL A 97  ? 0.51811 0.52671 0.70476 0.00423  0.01585  -0.00186 97  VAL A O   
1561 C CB  . VAL A 97  ? 0.52324 0.54093 0.66526 0.00132  0.01791  -0.01451 97  VAL A CB  
1562 C CG1 . VAL A 97  ? 0.47555 0.49881 0.61363 0.00323  0.01516  -0.01013 97  VAL A CG1 
1563 C CG2 . VAL A 97  ? 0.52244 0.53957 0.64890 -0.00053 0.01930  -0.02312 97  VAL A CG2 
1573 N N   . THR A 98  ? 0.53414 0.54730 0.72132 0.00780  0.02063  -0.00816 98  THR A N   
1574 C CA  . THR A 98  ? 0.49580 0.50991 0.70235 0.01012  0.01452  0.00073  98  THR A CA  
1575 C C   . THR A 98  ? 0.52987 0.55058 0.72812 0.01062  0.00713  0.00661  98  THR A C   
1576 O O   . THR A 98  ? 0.53031 0.55105 0.73933 0.01163  -0.00171 0.01559  98  THR A O   
1577 C CB  . THR A 98  ? 0.51495 0.52560 0.74772 0.01303  0.02144  -0.00377 98  THR A CB  
1578 O OG1 . THR A 98  ? 0.56350 0.57532 0.78923 0.01342  0.02988  -0.01229 98  THR A OG1 
1579 C CG2 . THR A 98  ? 0.60671 0.60925 0.85081 0.01250  0.02827  -0.00886 98  THR A CG2 
1587 N N   . GLN A 99  ? 0.49702 0.52220 0.67629 0.00979  0.00959  0.00196  99  GLN A N   
1588 C CA  . GLN A 99  ? 0.51473 0.54575 0.68629 0.01006  0.00348  0.00638  99  GLN A CA  
1589 C C   . GLN A 99  ? 0.53521 0.56981 0.68095 0.00790  0.00439  0.00335  99  GLN A C   
1590 O O   . GLN A 99  ? 0.50576 0.53923 0.64235 0.00739  0.01100  -0.00457 99  GLN A O   
1591 C CB  . GLN A 99  ? 0.50427 0.53733 0.69138 0.01271  0.00731  0.00294  99  GLN A CB  
1592 C CG  . GLN A 99  ? 0.51491 0.55377 0.69845 0.01297  -0.00001 0.00756  99  GLN A CG  
1593 C CD  . GLN A 99  ? 0.52500 0.56602 0.72448 0.01508  0.00573  0.00292  99  GLN A CD  
1594 O OE1 . GLN A 99  ? 0.48550 0.52576 0.67515 0.01483  0.01570  -0.00485 99  GLN A OE1 
1595 N NE2 . GLN A 99  ? 0.50002 0.54270 0.72495 0.01698  -0.00066 0.00778  99  GLN A NE2 
1604 N N   . LEU A 100 ? 0.55939 0.59706 0.69321 0.00645  -0.00263 0.00957  100 LEU A N   
1605 C CA  . LEU A 100 ? 0.48069 0.52223 0.59362 0.00465  -0.00196 0.00724  100 LEU A CA  
1606 C C   . LEU A 100 ? 0.55977 0.60546 0.66825 0.00521  -0.00606 0.00963  100 LEU A C   
1607 O O   . LEU A 100 ? 0.58141 0.62610 0.69291 0.00479  -0.01370 0.01680  100 LEU A O   
1608 C CB  . LEU A 100 ? 0.52809 0.56801 0.62986 0.00141  -0.00417 0.01134  100 LEU A CB  
1609 C CG  . LEU A 100 ? 0.52642 0.57012 0.61004 -0.00071 -0.00416 0.01069  100 LEU A CG  
1610 C CD1 . LEU A 100 ? 0.51073 0.55800 0.58954 0.00008  0.00061  0.00217  100 LEU A CD1 
1611 C CD2 . LEU A 100 ? 0.51230 0.55259 0.58801 -0.00443 -0.00421 0.01503  100 LEU A CD2 
1623 N N   . CYS A 101 ? 0.50746 0.55651 0.60810 0.00589  -0.00188 0.00387  101 CYS A N   
1624 C CA  . CYS A 101 ? 0.49297 0.54585 0.59107 0.00644  -0.00447 0.00484  101 CYS A CA  
1625 C C   . CYS A 101 ? 0.49474 0.55061 0.57339 0.00491  -0.00366 0.00266  101 CYS A C   
1626 O O   . CYS A 101 ? 0.46631 0.52188 0.53737 0.00476  0.00079  -0.00237 101 CYS A O   
1627 C CB  . CYS A 101 ? 0.40677 0.45978 0.51710 0.00888  0.00139  -0.00011 101 CYS A CB  
1628 S SG  . CYS A 101 ? 0.53036 0.58049 0.67013 0.01105  0.00203  0.00136  101 CYS A SG  
1634 N N   . PHE A 102 ? 0.45125 0.50926 0.52285 0.00373  -0.00854 0.00617  102 PHE A N   
1635 C CA  . PHE A 102 ? 0.48526 0.54604 0.54148 0.00253  -0.00699 0.00366  102 PHE A CA  
1636 C C   . PHE A 102 ? 0.50831 0.57039 0.55981 0.00147  -0.01200 0.00656  102 PHE A C   
1637 O O   . PHE A 102 ? 0.51492 0.57459 0.57012 0.00051  -0.01891 0.01198  102 PHE A O   
1638 C CB  . PHE A 102 ? 0.47071 0.53053 0.51684 0.00002  -0.00571 0.00402  102 PHE A CB  
1639 C CG  . PHE A 102 ? 0.47421 0.52962 0.51650 -0.00285 -0.00962 0.01060  102 PHE A CG  
1640 C CD1 . PHE A 102 ? 0.52672 0.58002 0.55587 -0.00564 -0.01283 0.01404  102 PHE A CD1 
1641 C CD2 . PHE A 102 ? 0.50891 0.56032 0.55830 -0.00327 -0.00982 0.01334  102 PHE A CD2 
1642 C CE1 . PHE A 102 ? 0.52121 0.56699 0.54160 -0.00906 -0.01639 0.02055  102 PHE A CE1 
1643 C CE2 . PHE A 102 ? 0.53017 0.57507 0.57336 -0.00630 -0.01341 0.02031  102 PHE A CE2 
1644 C CZ  . PHE A 102 ? 0.57364 0.61501 0.60081 -0.00936 -0.01673 0.02410  102 PHE A CZ  
1654 N N   . GLU A 103 ? 0.51858 0.58353 0.56157 0.00149  -0.00940 0.00295  103 GLU A N   
1655 C CA  . GLU A 103 ? 0.51105 0.57689 0.54864 0.00017  -0.01339 0.00431  103 GLU A CA  
1656 C C   . GLU A 103 ? 0.49428 0.55627 0.51741 -0.00370 -0.01713 0.00820  103 GLU A C   
1657 O O   . GLU A 103 ? 0.55348 0.61423 0.56797 -0.00537 -0.01294 0.00740  103 GLU A O   
1658 C CB  . GLU A 103 ? 0.49411 0.56298 0.52648 0.00117  -0.00863 -0.00075 103 GLU A CB  
1659 C CG  . GLU A 103 ? 0.47355 0.54345 0.50347 0.00015  -0.01180 -0.00058 103 GLU A CG  
1660 C CD  . GLU A 103 ? 0.51882 0.59078 0.54478 0.00137  -0.00660 -0.00526 103 GLU A CD  
1661 O OE1 . GLU A 103 ? 0.49418 0.56637 0.51005 0.00042  -0.00422 -0.00705 103 GLU A OE1 
1662 O OE2 . GLU A 103 ? 0.56067 0.63332 0.59479 0.00319  -0.00441 -0.00705 103 GLU A OE2 
1669 N N   . HIS A 104 ? 0.50183 0.56075 0.52216 -0.00555 -0.02494 0.01218  104 HIS A N   
1670 C CA  . HIS A 104 ? 0.50683 0.55856 0.50794 -0.01016 -0.02852 0.01585  104 HIS A CA  
1671 C C   . HIS A 104 ? 0.55782 0.61015 0.54434 -0.01223 -0.02199 0.01117  104 HIS A C   
1672 O O   . HIS A 104 ? 0.44483 0.50238 0.43538 -0.01043 -0.01960 0.00668  104 HIS A O   
1673 C CB  . HIS A 104 ? 0.54362 0.59050 0.54352 -0.01187 -0.04043 0.02069  104 HIS A CB  
1674 C CG  . HIS A 104 ? 0.64042 0.67597 0.61536 -0.01745 -0.04514 0.02498  104 HIS A CG  
1675 N ND1 . HIS A 104 ? 0.68191 0.70884 0.64600 -0.02008 -0.04503 0.03009  104 HIS A ND1 
1676 C CD2 . HIS A 104 ? 0.65939 0.68880 0.61594 -0.02147 -0.04948 0.02471  104 HIS A CD2 
1677 C CE1 . HIS A 104 ? 0.72058 0.73546 0.65871 -0.02568 -0.04861 0.03311  104 HIS A CE1 
1678 N NE2 . HIS A 104 ? 0.71091 0.72690 0.64341 -0.02671 -0.05158 0.02963  104 HIS A NE2 
1686 N N   . ASP A 105 ? 0.62458 0.67066 0.59514 -0.01619 -0.01816 0.01222  105 ASP A N   
1687 C CA  . ASP A 105 ? 0.67021 0.71559 0.62878 -0.01865 -0.01041 0.00759  105 ASP A CA  
1688 C C   . ASP A 105 ? 0.69995 0.73284 0.63472 -0.02491 -0.01111 0.01074  105 ASP A C   
1689 O O   . ASP A 105 ? 0.67733 0.70233 0.60454 -0.02747 -0.01239 0.01595  105 ASP A O   
1690 C CB  . ASP A 105 ? 0.67883 0.72909 0.64547 -0.01722 -0.00105 0.00377  105 ASP A CB  
1691 C CG  . ASP A 105 ? 0.69313 0.74457 0.65498 -0.01867 0.00711  -0.00179 105 ASP A CG  
1692 O OD1 . ASP A 105 ? 0.75653 0.80523 0.70818 -0.02054 0.00652  -0.00333 105 ASP A OD1 
1693 O OD2 . ASP A 105 ? 0.72733 0.78237 0.69767 -0.01791 0.01380  -0.00493 105 ASP A OD2 
1698 N N   . THR A 106 ? 0.70319 0.73256 0.62445 -0.02776 -0.00995 0.00754  106 THR A N   
1699 C CA  . THR A 106 ? 0.77577 0.79024 0.66939 -0.03454 -0.01109 0.00989  106 THR A CA  
1700 C C   . THR A 106 ? 0.76930 0.77833 0.64972 -0.03874 0.00339  0.00513  106 THR A C   
1701 O O   . THR A 106 ? 0.77938 0.77389 0.63326 -0.04520 0.00535  0.00567  106 THR A O   
1702 C CB  . THR A 106 ? 0.77060 0.78175 0.65552 -0.03608 -0.02053 0.00924  106 THR A CB  
1703 O OG1 . THR A 106 ? 0.68237 0.70113 0.57406 -0.03439 -0.01363 0.00169  106 THR A OG1 
1704 C CG2 . THR A 106 ? 0.73073 0.74723 0.63312 -0.03219 -0.03445 0.01369  106 THR A CG2 
1712 N N   . GLU A 107 ? 0.75788 0.77706 0.65631 -0.03554 0.01351  0.00025  107 GLU A N   
1713 C CA  . GLU A 107 ? 0.79139 0.80652 0.68401 -0.03920 0.02799  -0.00468 107 GLU A CA  
1714 C C   . GLU A 107 ? 0.82372 0.82668 0.70194 -0.04447 0.03359  -0.00043 107 GLU A C   
1715 O O   . GLU A 107 ? 0.76426 0.76558 0.64402 -0.04361 0.02648  0.00605  107 GLU A O   
1716 C CB  . GLU A 107 ? 0.80832 0.83731 0.72757 -0.03417 0.03460  -0.01012 107 GLU A CB  
1717 C CG  . GLU A 107 ? 0.82250 0.85940 0.75104 -0.03063 0.03360  -0.01535 107 GLU A CG  
1718 C CD  . GLU A 107 ? 0.89748 0.94498 0.84964 -0.02642 0.03954  -0.02032 107 GLU A CD  
1719 O OE1 . GLU A 107 ? 0.91459 0.96196 0.87434 -0.02788 0.04773  -0.02180 107 GLU A OE1 
1720 O OE2 . GLU A 107 ? 0.81622 0.87131 0.77971 -0.02185 0.03561  -0.02258 107 GLU A OE2 
1727 N N   . PRO A 108 ? 0.84240 0.83559 0.70688 -0.05023 0.04749  -0.00411 108 PRO A N   
1728 C CA  . PRO A 108 ? 0.87849 0.85673 0.72510 -0.05640 0.05441  0.00030  108 PRO A CA  
1729 C C   . PRO A 108 ? 0.85213 0.83786 0.72079 -0.05354 0.05658  0.00275  108 PRO A C   
1730 O O   . PRO A 108 ? 0.82882 0.80675 0.68889 -0.05500 0.05080  0.01031  108 PRO A O   
1731 C CB  . PRO A 108 ? 0.99274 0.96119 0.82657 -0.06259 0.07259  -0.00653 108 PRO A CB  
1732 C CG  . PRO A 108 ? 0.92135 0.89545 0.75715 -0.06069 0.07109  -0.01295 108 PRO A CG  
1733 C CD  . PRO A 108 ? 0.84644 0.84004 0.71063 -0.05180 0.05851  -0.01246 108 PRO A CD  
1741 N N   . TYR A 109 ? 0.85874 0.85863 0.75617 -0.04958 0.06372  -0.00334 109 TYR A N   
1742 C CA  . TYR A 109 ? 0.86660 0.87305 0.78543 -0.04739 0.06541  -0.00200 109 TYR A CA  
1743 C C   . TYR A 109 ? 0.84047 0.85312 0.76746 -0.04224 0.05030  0.00354  109 TYR A C   
1744 O O   . TYR A 109 ? 0.76971 0.78006 0.70153 -0.04255 0.04922  0.00789  109 TYR A O   
1745 C CB  . TYR A 109 ? 0.88609 0.90661 0.83529 -0.04381 0.07248  -0.00983 109 TYR A CB  
1746 C CG  . TYR A 109 ? 0.91551 0.94617 0.88992 -0.03961 0.06808  -0.00925 109 TYR A CG  
1747 C CD1 . TYR A 109 ? 1.05775 1.08459 1.03986 -0.04296 0.07639  -0.00841 109 TYR A CD1 
1748 C CD2 . TYR A 109 ? 0.89279 0.93526 0.88195 -0.03288 0.05624  -0.00984 109 TYR A CD2 
1749 C CE1 . TYR A 109 ? 0.99708 1.03243 1.00202 -0.03955 0.07175  -0.00853 109 TYR A CE1 
1750 C CE2 . TYR A 109 ? 0.92696 0.97641 0.93574 -0.02973 0.05212  -0.00999 109 TYR A CE2 
1751 C CZ  . TYR A 109 ? 0.90402 0.95024 0.92108 -0.03303 0.05931  -0.00949 109 TYR A CZ  
1752 O OH  . TYR A 109 ? 0.93457 0.98699 0.97105 -0.03035 0.05476  -0.01028 109 TYR A OH  
1762 N N   . ALA A 110 ? 0.82694 0.84697 0.75706 -0.03764 0.03968  0.00305  110 ALA A N   
1763 C CA  . ALA A 110 ? 0.84164 0.86771 0.78269 -0.03269 0.02757  0.00702  110 ALA A CA  
1764 C C   . ALA A 110 ? 0.76440 0.77859 0.69048 -0.03555 0.02079  0.01558  110 ALA A C   
1765 O O   . ALA A 110 ? 0.70592 0.72213 0.64381 -0.03308 0.01596  0.01921  110 ALA A O   
1766 C CB  . ALA A 110 ? 0.78901 0.82278 0.73442 -0.02835 0.01957  0.00485  110 ALA A CB  
1772 N N   . LYS A 111 ? 0.77961 0.77998 0.67902 -0.04096 0.01983  0.01889  111 LYS A N   
1773 C CA  . LYS A 111 ? 0.90824 0.89497 0.79129 -0.04392 0.01107  0.02807  111 LYS A CA  
1774 C C   . LYS A 111 ? 0.87163 0.85140 0.75522 -0.04661 0.01827  0.03181  111 LYS A C   
1775 O O   . LYS A 111 ? 0.79010 0.76675 0.67862 -0.04527 0.01032  0.03853  111 LYS A O   
1776 C CB  . LYS A 111 ? 1.01137 0.98144 0.86078 -0.05029 0.00844  0.03057  111 LYS A CB  
1777 C CG  . LYS A 111 ? 1.04250 1.01809 0.88952 -0.04920 0.00563  0.02475  111 LYS A CG  
1778 C CD  . LYS A 111 ? 1.16726 1.13983 1.00879 -0.04820 -0.01243 0.02967  111 LYS A CD  
1779 C CE  . LYS A 111 ? 1.17850 1.12975 0.98233 -0.05596 -0.01738 0.03350  111 LYS A CE  
1780 N NZ  . LYS A 111 ? 1.40799 1.35493 1.20952 -0.05513 -0.03803 0.04008  111 LYS A NZ  
1794 N N   . VAL A 112 ? 0.81781 0.79492 0.69886 -0.05048 0.03385  0.02735  112 VAL A N   
1795 C CA  . VAL A 112 ? 0.81794 0.78891 0.70256 -0.05341 0.04251  0.03007  112 VAL A CA  
1796 C C   . VAL A 112 ? 0.75091 0.73693 0.66807 -0.04720 0.03914  0.02851  112 VAL A C   
1797 O O   . VAL A 112 ? 0.75611 0.73752 0.67774 -0.04735 0.03651  0.03405  112 VAL A O   
1798 C CB  . VAL A 112 ? 0.91960 0.88593 0.79992 -0.05883 0.06147  0.02417  112 VAL A CB  
1799 C CG1 . VAL A 112 ? 0.89909 0.86379 0.79353 -0.06087 0.07164  0.02497  112 VAL A CG1 
1800 C CG2 . VAL A 112 ? 0.90167 0.84723 0.74342 -0.06667 0.06657  0.02657  112 VAL A CG2 
1810 N N   . ARG A 113 ? 0.71327 0.71583 0.65208 -0.04200 0.03914  0.02090  113 ARG A N   
1811 C CA  . ARG A 113 ? 0.70004 0.71491 0.66613 -0.03675 0.03610  0.01830  113 ARG A CA  
1812 C C   . ARG A 113 ? 0.72015 0.73530 0.68981 -0.03294 0.02335  0.02371  113 ARG A C   
1813 O O   . ARG A 113 ? 0.66056 0.67597 0.64301 -0.03166 0.02197  0.02567  113 ARG A O   
1814 C CB  . ARG A 113 ? 0.71030 0.73954 0.69299 -0.03241 0.03692  0.00983  113 ARG A CB  
1815 C CG  . ARG A 113 ? 0.71444 0.75447 0.72021 -0.02714 0.03199  0.00650  113 ARG A CG  
1816 C CD  . ARG A 113 ? 0.68929 0.73961 0.70259 -0.02248 0.02814  0.00077  113 ARG A CD  
1817 N NE  . ARG A 113 ? 0.66556 0.71485 0.66665 -0.02089 0.02168  0.00317  113 ARG A NE  
1818 C CZ  . ARG A 113 ? 0.68849 0.74296 0.68882 -0.01867 0.02049  -0.00058 113 ARG A CZ  
1819 N NH1 . ARG A 113 ? 0.77856 0.83926 0.78892 -0.01741 0.02448  -0.00645 113 ARG A NH1 
1820 N NH2 . ARG A 113 ? 0.69141 0.74454 0.68259 -0.01767 0.01455  0.00175  113 ARG A NH2 
1834 N N   . ASP A 114 ? 0.62366 0.63872 0.58462 -0.03117 0.01436  0.02569  114 ASP A N   
1835 C CA  . ASP A 114 ? 0.62715 0.64414 0.59744 -0.02706 0.00307  0.02963  114 ASP A CA  
1836 C C   . ASP A 114 ? 0.67069 0.67455 0.63253 -0.02975 -0.00225 0.03902  114 ASP A C   
1837 O O   . ASP A 114 ? 0.68513 0.69041 0.66244 -0.02657 -0.00775 0.04178  114 ASP A O   
1838 C CB  . ASP A 114 ? 0.62207 0.64276 0.58881 -0.02478 -0.00467 0.02880  114 ASP A CB  
1839 C CG  . ASP A 114 ? 0.61179 0.64498 0.58928 -0.02123 -0.00063 0.02035  114 ASP A CG  
1840 O OD1 . ASP A 114 ? 0.61674 0.65642 0.60731 -0.01945 0.00506  0.01557  114 ASP A OD1 
1841 O OD2 . ASP A 114 ? 0.59697 0.63256 0.56969 -0.02038 -0.00398 0.01870  114 ASP A OD2 
1846 N N   . ALA A 115 ? 0.73993 0.72938 0.67656 -0.03581 -0.00035 0.04400  115 ALA A N   
1847 C CA  . ALA A 115 ? 0.78991 0.76406 0.71550 -0.03893 -0.00548 0.05387  115 ALA A CA  
1848 C C   . ALA A 115 ? 0.76620 0.74071 0.70728 -0.03886 0.00176  0.05419  115 ALA A C   
1849 O O   . ALA A 115 ? 0.74690 0.71692 0.69672 -0.03733 -0.00502 0.06036  115 ALA A O   
1850 C CB  . ALA A 115 ? 0.87900 0.83461 0.76936 -0.04654 -0.00280 0.05851  115 ALA A CB  
1856 N N   . ALA A 116 ? 0.73887 0.71876 0.68612 -0.04045 0.01513  0.04735  116 ALA A N   
1857 C CA  . ALA A 116 ? 0.79507 0.77598 0.75940 -0.04069 0.02182  0.04660  116 ALA A CA  
1858 C C   . ALA A 116 ? 0.76366 0.75654 0.75482 -0.03416 0.01517  0.04362  116 ALA A C   
1859 O O   . ALA A 116 ? 0.72059 0.70945 0.72238 -0.03368 0.01361  0.04727  116 ALA A O   
1860 C CB  . ALA A 116 ? 0.83625 0.82237 0.80679 -0.04336 0.03618  0.03876  116 ALA A CB  
1866 N N   . VAL A 117 ? 0.62061 0.62665 0.62181 -0.02943 0.01198  0.03686  117 VAL A N   
1867 C CA  . VAL A 117 ? 0.60168 0.61648 0.62433 -0.02395 0.00729  0.03336  117 VAL A CA  
1868 C C   . VAL A 117 ? 0.59949 0.60848 0.62505 -0.02186 -0.00255 0.04066  117 VAL A C   
1869 O O   . VAL A 117 ? 0.59440 0.60420 0.63731 -0.01922 -0.00411 0.04049  117 VAL A O   
1870 C CB  . VAL A 117 ? 0.62547 0.65249 0.65381 -0.02004 0.00659  0.02535  117 VAL A CB  
1871 C CG1 . VAL A 117 ? 0.57151 0.60388 0.61659 -0.01501 0.00219  0.02237  117 VAL A CG1 
1872 C CG2 . VAL A 117 ? 0.61538 0.64855 0.64788 -0.02123 0.01454  0.01809  117 VAL A CG2 
1882 N N   . ARG A 118 ? 0.65721 0.65971 0.66720 -0.02312 -0.00977 0.04684  118 ARG A N   
1883 C CA  A ARG A 118 ? 0.64230 0.63880 0.65771 -0.02120 -0.02115 0.05448  118 ARG A CA  
1884 C CA  B ARG A 118 ? 0.64197 0.63861 0.65768 -0.02114 -0.02112 0.05440  118 ARG A CA  
1885 C C   . ARG A 118 ? 0.69128 0.67646 0.70910 -0.02321 -0.02146 0.06171  118 ARG A C   
1886 O O   . ARG A 118 ? 0.67204 0.65638 0.70830 -0.01989 -0.02741 0.06475  118 ARG A O   
1887 C CB  A ARG A 118 ? 0.69751 0.68676 0.69292 -0.02339 -0.03036 0.06024  118 ARG A CB  
1888 C CB  B ARG A 118 ? 0.69737 0.68729 0.69384 -0.02311 -0.03045 0.05993  118 ARG A CB  
1889 C CG  A ARG A 118 ? 0.73040 0.73035 0.73130 -0.02002 -0.03434 0.05493  118 ARG A CG  
1890 C CG  B ARG A 118 ? 0.72842 0.72978 0.73088 -0.01967 -0.03345 0.05394  118 ARG A CG  
1891 C CD  A ARG A 118 ? 0.78173 0.77287 0.76305 -0.02283 -0.04510 0.06083  118 ARG A CD  
1892 C CD  B ARG A 118 ? 0.78421 0.77819 0.76708 -0.02236 -0.04317 0.05875  118 ARG A CD  
1893 N NE  A ARG A 118 ? 0.79982 0.80002 0.78040 -0.02141 -0.04555 0.05464  118 ARG A NE  
1894 N NE  B ARG A 118 ? 0.79227 0.79682 0.77863 -0.02009 -0.04342 0.05211  118 ARG A NE  
1895 C CZ  A ARG A 118 ? 0.79657 0.80571 0.79697 -0.01687 -0.05153 0.05232  118 ARG A CZ  
1896 C CZ  B ARG A 118 ? 0.78171 0.78712 0.75050 -0.02283 -0.03795 0.04768  118 ARG A CZ  
1897 N NH1 A ARG A 118 ? 0.75396 0.76491 0.77835 -0.01305 -0.05706 0.05496  118 ARG A NH1 
1898 N NH1 B ARG A 118 ? 0.83237 0.82898 0.77915 -0.02811 -0.03051 0.04839  118 ARG A NH1 
1899 N NH2 A ARG A 118 ? 0.78215 0.79802 0.77964 -0.01633 -0.05093 0.04696  118 ARG A NH2 
1900 N NH2 B ARG A 118 ? 0.70985 0.72448 0.68448 -0.02038 -0.03892 0.04219  118 ARG A NH2 
1927 N N   . ARG A 119 ? 0.67987 0.65534 0.68021 -0.02884 -0.01412 0.06450  119 ARG A N   
1928 C CA  . ARG A 119 ? 0.69521 0.65859 0.69688 -0.03133 -0.01293 0.07155  119 ARG A CA  
1929 C C   . ARG A 119 ? 0.65601 0.62805 0.68539 -0.02811 -0.00747 0.06545  119 ARG A C   
1930 O O   . ARG A 119 ? 0.69242 0.65933 0.73570 -0.02644 -0.01166 0.07006  119 ARG A O   
1931 C CB  . ARG A 119 ? 0.77472 0.72544 0.75182 -0.03869 -0.00310 0.07456  119 ARG A CB  
1932 C CG  . ARG A 119 ? 1.00956 0.94889 0.99030 -0.04186 0.00244  0.07993  119 ARG A CG  
1933 C CD  . ARG A 119 ? 1.04148 0.97021 1.00263 -0.04943 0.01686  0.08026  119 ARG A CD  
1934 N NE  . ARG A 119 ? 1.20149 1.14239 1.16380 -0.05007 0.02702  0.06968  119 ARG A NE  
1935 C CZ  . ARG A 119 ? 1.25287 1.18691 1.20048 -0.05630 0.04074  0.06784  119 ARG A CZ  
1936 N NH1 . ARG A 119 ? 1.06143 0.97558 0.98944 -0.06305 0.04763  0.07559  119 ARG A NH1 
1937 N NH2 . ARG A 119 ? 1.11238 1.05869 1.06553 -0.05591 0.04835  0.05806  119 ARG A NH2 
1951 N N   . LEU A 120 ? 0.64266 0.62678 0.68036 -0.02739 0.00124  0.05498  120 LEU A N   
1952 C CA  . LEU A 120 ? 0.62748 0.61808 0.68814 -0.02525 0.00574  0.04837  120 LEU A CA  
1953 C C   . LEU A 120 ? 0.62314 0.61897 0.70221 -0.01946 -0.00095 0.04620  120 LEU A C   
1954 O O   . LEU A 120 ? 0.59804 0.59214 0.69422 -0.01810 -0.00002 0.04514  120 LEU A O   
1955 C CB  . LEU A 120 ? 0.64381 0.64526 0.70831 -0.02571 0.01357  0.03793  120 LEU A CB  
1956 C CG  . LEU A 120 ? 0.68230 0.67978 0.73467 -0.03143 0.02280  0.03824  120 LEU A CG  
1957 C CD1 . LEU A 120 ? 0.75593 0.76552 0.81287 -0.03075 0.02740  0.02843  120 LEU A CD1 
1958 C CD2 . LEU A 120 ? 0.72658 0.71636 0.78714 -0.03530 0.02968  0.04039  120 LEU A CD2 
1970 N N   . ALA A 121 ? 0.64142 0.64298 0.71817 -0.01632 -0.00660 0.04506  121 ALA A N   
1971 C CA  . ALA A 121 ? 0.60651 0.61181 0.70171 -0.01129 -0.01126 0.04316  121 ALA A CA  
1972 C C   . ALA A 121 ? 0.54988 0.54535 0.65541 -0.01058 -0.01797 0.05229  121 ALA A C   
1973 O O   . ALA A 121 ? 0.62361 0.61913 0.75035 -0.00772 -0.01699 0.04991  121 ALA A O   
1974 C CB  . ALA A 121 ? 0.57303 0.58497 0.66399 -0.00880 -0.01586 0.04145  121 ALA A CB  
1980 N N   . ALA A 122 ? 0.58961 0.57495 0.67955 -0.01344 -0.02486 0.06277  122 ALA A N   
1981 C CA  . ALA A 122 ? 0.64141 0.61575 0.74064 -0.01265 -0.03385 0.07291  122 ALA A CA  
1982 C C   . ALA A 122 ? 0.70531 0.67334 0.81562 -0.01381 -0.02791 0.07382  122 ALA A C   
1983 O O   . ALA A 122 ? 0.65730 0.62155 0.78917 -0.01086 -0.03192 0.07684  122 ALA A O   
1984 C CB  . ALA A 122 ? 0.62946 0.59086 0.70335 -0.01658 -0.04325 0.08437  122 ALA A CB  
1990 N N   . GLU A 123 ? 0.67435 0.64098 0.77270 -0.01817 -0.01806 0.07104  123 GLU A N   
1991 C CA  . GLU A 123 ? 0.69735 0.65800 0.80692 -0.01989 -0.01185 0.07136  123 GLU A CA  
1992 C C   . GLU A 123 ? 0.64789 0.61714 0.78444 -0.01567 -0.00814 0.06148  123 GLU A C   
1993 O O   . GLU A 123 ? 0.71472 0.67790 0.86734 -0.01544 -0.00652 0.06276  123 GLU A O   
1994 C CB  . GLU A 123 ? 0.73001 0.68946 0.82538 -0.02548 -0.00107 0.06856  123 GLU A CB  
1995 C CG  . GLU A 123 ? 0.90301 0.84693 0.97281 -0.03129 -0.00094 0.07950  123 GLU A CG  
1996 C CD  . GLU A 123 ? 0.89685 0.84053 0.95633 -0.03691 0.01229  0.07522  123 GLU A CD  
1997 O OE1 . GLU A 123 ? 0.82867 0.78349 0.90554 -0.03613 0.01953  0.06489  123 GLU A OE1 
1998 O OE2 . GLU A 123 ? 1.09489 1.02632 1.12911 -0.04237 0.01544  0.08193  123 GLU A OE2 
2005 N N   . ALA A 124 ? 0.62078 0.60233 0.76081 -0.01276 -0.00625 0.05155  124 ALA A N   
2006 C CA  . ALA A 124 ? 0.54969 0.53697 0.70945 -0.00954 -0.00189 0.04130  124 ALA A CA  
2007 C C   . ALA A 124 ? 0.52170 0.51026 0.69813 -0.00457 -0.00650 0.04140  124 ALA A C   
2008 O O   . ALA A 124 ? 0.57258 0.56446 0.76321 -0.00209 -0.00143 0.03222  124 ALA A O   
2009 C CB  . ALA A 124 ? 0.61324 0.61072 0.76518 -0.00988 0.00365  0.02996  124 ALA A CB  
2015 N N   . GLY A 125 ? 0.59169 0.57671 0.76688 -0.00341 -0.01592 0.05121  125 GLY A N   
2016 C CA  . GLY A 125 ? 0.56870 0.55575 0.76454 0.00132  -0.02079 0.05144  125 GLY A CA  
2017 C C   . GLY A 125 ? 0.53572 0.53331 0.73004 0.00358  -0.01828 0.04323  125 GLY A C   
2018 O O   . GLY A 125 ? 0.53795 0.53819 0.75321 0.00726  -0.01633 0.03866  125 GLY A O   
2022 N N   . VAL A 126 ? 0.54585 0.54864 0.71668 0.00131  -0.01746 0.04130  126 VAL A N   
2023 C CA  . VAL A 126 ? 0.50324 0.51510 0.67011 0.00302  -0.01433 0.03349  126 VAL A CA  
2024 C C   . VAL A 126 ? 0.55160 0.56524 0.71347 0.00367  -0.02364 0.03986  126 VAL A C   
2025 O O   . VAL A 126 ? 0.54897 0.55890 0.69207 0.00065  -0.02975 0.04710  126 VAL A O   
2026 C CB  . VAL A 126 ? 0.53247 0.54897 0.67973 0.00043  -0.00782 0.02650  126 VAL A CB  
2027 C CG1 . VAL A 126 ? 0.54430 0.56849 0.68567 0.00216  -0.00551 0.01968  126 VAL A CG1 
2028 C CG2 . VAL A 126 ? 0.51913 0.53350 0.67237 -0.00050 -0.00052 0.01962  126 VAL A CG2 
2038 N N   . GLU A 127 ? 0.55524 0.57350 0.73380 0.00715  -0.02413 0.03666  127 GLU A N   
2039 C CA  . GLU A 127 ? 0.60048 0.62177 0.77681 0.00774  -0.03279 0.04080  127 GLU A CA  
2040 C C   . GLU A 127 ? 0.47252 0.49995 0.62554 0.00596  -0.02916 0.03589  127 GLU A C   
2041 O O   . GLU A 127 ? 0.52631 0.55798 0.67510 0.00628  -0.01948 0.02710  127 GLU A O   
2042 C CB  . GLU A 127 ? 0.65828 0.68303 0.86445 0.01187  -0.03262 0.03791  127 GLU A CB  
2043 C CG  . GLU A 127 ? 0.72720 0.75693 0.93461 0.01253  -0.03993 0.03960  127 GLU A CG  
2044 C CD  . GLU A 127 ? 0.82109 0.85405 1.06376 0.01642  -0.03907 0.03689  127 GLU A CD  
2045 O OE1 . GLU A 127 ? 0.84274 0.87393 1.10677 0.01856  -0.03051 0.03242  127 GLU A OE1 
2046 O OE2 . GLU A 127 ? 1.01558 1.05246 1.26566 0.01705  -0.04625 0.03868  127 GLU A OE2 
2053 N N   . VAL A 128 ? 0.53372 0.56022 0.67100 0.00389  -0.03763 0.04172  128 VAL A N   
2054 C CA  . VAL A 128 ? 0.57066 0.60221 0.68727 0.00215  -0.03495 0.03777  128 VAL A CA  
2055 C C   . VAL A 128 ? 0.51995 0.55534 0.64319 0.00360  -0.04165 0.03843  128 VAL A C   
2056 O O   . VAL A 128 ? 0.55294 0.58397 0.68203 0.00341  -0.05348 0.04594  128 VAL A O   
2057 C CB  . VAL A 128 ? 0.61158 0.63746 0.70131 -0.00255 -0.03670 0.04251  128 VAL A CB  
2058 C CG1 . VAL A 128 ? 0.63865 0.67009 0.71047 -0.00406 -0.03202 0.03708  128 VAL A CG1 
2059 C CG2 . VAL A 128 ? 0.59515 0.61666 0.68306 -0.00426 -0.03037 0.04256  128 VAL A CG2 
2069 N N   . VAL A 129 ? 0.55634 0.59902 0.67920 0.00489  -0.03475 0.03071  129 VAL A N   
2070 C CA  . VAL A 129 ? 0.53756 0.58463 0.66708 0.00594  -0.03898 0.02993  129 VAL A CA  
2071 C C   . VAL A 129 ? 0.47855 0.52905 0.58512 0.00396  -0.03535 0.02603  129 VAL A C   
2072 O O   . VAL A 129 ? 0.52949 0.58279 0.62896 0.00435  -0.02561 0.01963  129 VAL A O   
2073 C CB  . VAL A 129 ? 0.50896 0.56024 0.66484 0.00961  -0.03205 0.02399  129 VAL A CB  
2074 C CG1 . VAL A 129 ? 0.50196 0.55802 0.66626 0.01026  -0.03526 0.02277  129 VAL A CG1 
2075 C CG2 . VAL A 129 ? 0.52619 0.57404 0.70862 0.01178  -0.03467 0.02720  129 VAL A CG2 
2085 N N   . THR A 130 ? 0.53784 0.58709 0.63298 0.00170  -0.04392 0.02982  130 THR A N   
2086 C CA  . THR A 130 ? 0.53084 0.58215 0.60452 -0.00052 -0.04081 0.02650  130 THR A CA  
2087 C C   . THR A 130 ? 0.56784 0.62196 0.64536 -0.00054 -0.04675 0.02595  130 THR A C   
2088 O O   . THR A 130 ? 0.62410 0.67336 0.69099 -0.00342 -0.05710 0.03072  130 THR A O   
2089 C CB  . THR A 130 ? 0.57089 0.61504 0.61941 -0.00493 -0.04301 0.03075  130 THR A CB  
2090 O OG1 . THR A 130 ? 0.64795 0.68407 0.69169 -0.00725 -0.05572 0.03863  130 THR A OG1 
2091 C CG2 . THR A 130 ? 0.58634 0.62797 0.63358 -0.00527 -0.03662 0.03101  130 THR A CG2 
2099 N N   . PRO A 131 ? 0.52874 0.58924 0.61977 0.00212  -0.04034 0.02006  131 PRO A N   
2100 C CA  . PRO A 131 ? 0.61397 0.67748 0.71078 0.00190  -0.04482 0.01890  131 PRO A CA  
2101 C C   . PRO A 131 ? 0.55820 0.62197 0.63162 -0.00071 -0.04299 0.01626  131 PRO A C   
2102 O O   . PRO A 131 ? 0.53433 0.59801 0.59163 -0.00134 -0.03532 0.01354  131 PRO A O   
2103 C CB  . PRO A 131 ? 0.64626 0.71475 0.76505 0.00531  -0.03534 0.01320  131 PRO A CB  
2104 C CG  . PRO A 131 ? 0.63354 0.70037 0.75606 0.00715  -0.02677 0.01138  131 PRO A CG  
2105 C CD  . PRO A 131 ? 0.53770 0.60110 0.63839 0.00500  -0.02841 0.01411  131 PRO A CD  
2113 N N   . ILE A 132 ? 0.48546 0.54947 0.55980 -0.00222 -0.05047 0.01674  132 ILE A N   
2114 C CA  . ILE A 132 ? 0.55881 0.62282 0.61468 -0.00466 -0.04874 0.01349  132 ILE A CA  
2115 C C   . ILE A 132 ? 0.52280 0.59307 0.58952 -0.00209 -0.03931 0.00729  132 ILE A C   
2116 O O   . ILE A 132 ? 0.54825 0.62161 0.63625 -0.00060 -0.04074 0.00635  132 ILE A O   
2117 C CB  . ILE A 132 ? 0.67610 0.73547 0.72575 -0.00822 -0.06216 0.01661  132 ILE A CB  
2118 C CG1 . ILE A 132 ? 0.66428 0.71411 0.70110 -0.01117 -0.07308 0.02400  132 ILE A CG1 
2119 C CG2 . ILE A 132 ? 0.60360 0.66188 0.63315 -0.01110 -0.05887 0.01228  132 ILE A CG2 
2120 C CD1 . ILE A 132 ? 0.78445 0.82912 0.79815 -0.01314 -0.06566 0.02487  132 ILE A CD1 
2132 N N   . SER A 133 ? 0.53151 0.60281 0.58497 -0.00162 -0.02957 0.00329  133 SER A N   
2133 C CA  . SER A 133 ? 0.49556 0.57003 0.55349 0.00007  -0.02181 -0.00175 133 SER A CA  
2134 C C   . SER A 133 ? 0.49125 0.56533 0.53077 -0.00091 -0.01689 -0.00489 133 SER A C   
2135 O O   . SER A 133 ? 0.44988 0.52513 0.49113 0.00059  -0.01065 -0.00839 133 SER A O   
2136 C CB  . SER A 133 ? 0.45731 0.53242 0.52691 0.00334  -0.01295 -0.00401 133 SER A CB  
2137 O OG  . SER A 133 ? 0.56300 0.63633 0.62416 0.00388  -0.01031 -0.00349 133 SER A OG  
2143 N N   . HIS A 134 ? 0.46902 0.54056 0.49201 -0.00344 -0.01860 -0.00381 134 HIS A N   
2144 C CA  . HIS A 134 ? 0.50100 0.57244 0.51137 -0.00425 -0.01325 -0.00739 134 HIS A CA  
2145 C C   . HIS A 134 ? 0.52697 0.59707 0.53223 -0.00682 -0.01633 -0.00905 134 HIS A C   
2146 O O   . HIS A 134 ? 0.53246 0.60348 0.53502 -0.00635 -0.01130 -0.01283 134 HIS A O   
2147 C CB  . HIS A 134 ? 0.45281 0.52163 0.45025 -0.00628 -0.01121 -0.00667 134 HIS A CB  
2148 C CG  . HIS A 134 ? 0.46118 0.53036 0.45085 -0.00681 -0.00486 -0.01080 134 HIS A CG  
2149 N ND1 . HIS A 134 ? 0.49325 0.56563 0.48872 -0.00352 0.00014  -0.01384 134 HIS A ND1 
2150 C CD2 . HIS A 134 ? 0.51788 0.58349 0.49503 -0.01036 -0.00257 -0.01247 134 HIS A CD2 
2151 C CE1 . HIS A 134 ? 0.45662 0.52873 0.44706 -0.00450 0.00429  -0.01691 134 HIS A CE1 
2152 N NE2 . HIS A 134 ? 0.49140 0.55963 0.47126 -0.00869 0.00395  -0.01665 134 HIS A NE2 
2160 N N   . THR A 135 ? 0.51016 0.57713 0.51388 -0.00966 -0.02535 -0.00626 135 THR A N   
2161 C CA  . THR A 135 ? 0.54116 0.60572 0.54022 -0.01267 -0.03031 -0.00807 135 THR A CA  
2162 C C   . THR A 135 ? 0.54200 0.61027 0.56243 -0.01116 -0.03555 -0.00775 135 THR A C   
2163 O O   . THR A 135 ? 0.53843 0.60981 0.57600 -0.00837 -0.03604 -0.00549 135 THR A O   
2164 C CB  . THR A 135 ? 0.52351 0.57933 0.50311 -0.01788 -0.03842 -0.00533 135 THR A CB  
2165 O OG1 . THR A 135 ? 0.54984 0.60371 0.53482 -0.01767 -0.04670 0.00066  135 THR A OG1 
2166 C CG2 . THR A 135 ? 0.62120 0.67250 0.58075 -0.02018 -0.03015 -0.00710 135 THR A CG2 
2174 N N   . LEU A 136 ? 0.50021 0.56771 0.52111 -0.01330 -0.03872 -0.01058 136 LEU A N   
2175 C CA  . LEU A 136 ? 0.51009 0.58102 0.55425 -0.01259 -0.04423 -0.01063 136 LEU A CA  
2176 C C   . LEU A 136 ? 0.55253 0.62159 0.60538 -0.01380 -0.05789 -0.00555 136 LEU A C   
2177 O O   . LEU A 136 ? 0.53212 0.60563 0.61130 -0.01134 -0.05995 -0.00422 136 LEU A O   
2178 C CB  . LEU A 136 ? 0.48407 0.55370 0.52642 -0.01540 -0.04630 -0.01483 136 LEU A CB  
2179 C CG  . LEU A 136 ? 0.48152 0.55296 0.52211 -0.01380 -0.03394 -0.01960 136 LEU A CG  
2180 C CD1 . LEU A 136 ? 0.49532 0.56382 0.53150 -0.01750 -0.03753 -0.02366 136 LEU A CD1 
2181 C CD2 . LEU A 136 ? 0.47237 0.54858 0.53416 -0.00973 -0.02555 -0.02003 136 LEU A CD2 
2193 N N   . TYR A 137 ? 0.54822 0.60936 0.57934 -0.01783 -0.06720 -0.00263 137 TYR A N   
2194 C CA  . TYR A 137 ? 0.52253 0.57905 0.55797 -0.01971 -0.08322 0.00297  137 TYR A CA  
2195 C C   . TYR A 137 ? 0.58257 0.63249 0.59976 -0.02058 -0.08453 0.00831  137 TYR A C   
2196 O O   . TYR A 137 ? 0.55109 0.59875 0.54825 -0.02119 -0.07407 0.00689  137 TYR A O   
2197 C CB  . TYR A 137 ? 0.56099 0.60956 0.58312 -0.02525 -0.09694 0.00234  137 TYR A CB  
2198 C CG  . TYR A 137 ? 0.54398 0.59808 0.58606 -0.02524 -0.09828 -0.00269 137 TYR A CG  
2199 C CD1 . TYR A 137 ? 0.56123 0.62007 0.63574 -0.02401 -0.10899 -0.00119 137 TYR A CD1 
2200 C CD2 . TYR A 137 ? 0.53730 0.59155 0.56818 -0.02661 -0.08871 -0.00908 137 TYR A CD2 
2201 C CE1 . TYR A 137 ? 0.50319 0.56694 0.59828 -0.02442 -0.10949 -0.00604 137 TYR A CE1 
2202 C CE2 . TYR A 137 ? 0.49962 0.55814 0.54897 -0.02689 -0.08938 -0.01359 137 TYR A CE2 
2203 C CZ  . TYR A 137 ? 0.53473 0.59802 0.61604 -0.02597 -0.09956 -0.01213 137 TYR A CZ  
2204 O OH  . TYR A 137 ? 0.55481 0.62223 0.65684 -0.02663 -0.09961 -0.01682 137 TYR A OH  
2214 N N   . ASP A 138 ? 0.56120 0.60766 0.58748 -0.02072 -0.09773 0.01459  138 ASP A N   
2215 C CA  . ASP A 138 ? 0.70808 0.74442 0.71336 -0.02304 -0.10280 0.02095  138 ASP A CA  
2216 C C   . ASP A 138 ? 0.70701 0.72960 0.67573 -0.02989 -0.10907 0.02110  138 ASP A C   
2217 O O   . ASP A 138 ? 0.70870 0.72386 0.67294 -0.03343 -0.12529 0.02323  138 ASP A O   
2218 C CB  . ASP A 138 ? 0.66804 0.70306 0.69451 -0.02140 -0.11721 0.02804  138 ASP A CB  
2219 C CG  . ASP A 138 ? 0.68899 0.71223 0.69438 -0.02367 -0.12247 0.03561  138 ASP A CG  
2220 O OD1 . ASP A 138 ? 0.68646 0.69940 0.65659 -0.02826 -0.11852 0.03582  138 ASP A OD1 
2221 O OD2 . ASP A 138 ? 0.63268 0.65611 0.65801 -0.02101 -0.12995 0.04137  138 ASP A OD2 
2226 N N   . THR A 139 ? 0.71758 0.73585 0.66046 -0.03211 -0.09608 0.01834  139 THR A N   
2227 C CA  . THR A 139 ? 0.86204 0.86668 0.76982 -0.03896 -0.09751 0.01634  139 THR A CA  
2228 C C   . THR A 139 ? 0.87484 0.86198 0.75874 -0.04439 -0.11362 0.02392  139 THR A C   
2229 O O   . THR A 139 ? 0.77518 0.74963 0.63597 -0.05030 -0.12378 0.02329  139 THR A O   
2230 C CB  . THR A 139 ? 0.99724 1.00066 0.88674 -0.04005 -0.07877 0.01197  139 THR A CB  
2231 O OG1 . THR A 139 ? 1.06867 1.06941 0.95419 -0.03934 -0.07436 0.01701  139 THR A OG1 
2232 C CG2 . THR A 139 ? 0.97660 0.99534 0.88807 -0.03482 -0.06548 0.00518  139 THR A CG2 
2240 N N   . ASP A 140 ? 0.86190 0.84656 0.74980 -0.04276 -0.11693 0.03131  140 ASP A N   
2241 C CA  . ASP A 140 ? 0.96164 0.92823 0.82788 -0.04756 -0.13411 0.04007  140 ASP A CA  
2242 C C   . ASP A 140 ? 0.90978 0.87532 0.79114 -0.04784 -0.15653 0.04267  140 ASP A C   
2243 O O   . ASP A 140 ? 0.87116 0.81892 0.72496 -0.05412 -0.17253 0.04642  140 ASP A O   
2244 C CB  . ASP A 140 ? 0.95075 0.91685 0.82578 -0.04468 -0.13336 0.04758  140 ASP A CB  
2245 C CG  . ASP A 140 ? 1.10915 1.06784 0.95798 -0.04752 -0.11635 0.04723  140 ASP A CG  
2246 O OD1 . ASP A 140 ? 0.95659 0.90666 0.77592 -0.05279 -0.10717 0.04241  140 ASP A OD1 
2247 O OD2 . ASP A 140 ? 1.15516 1.11664 1.01503 -0.04459 -0.11133 0.05125  140 ASP A OD2 
2252 N N   . MET A 141 ? 0.77974 0.76304 0.70482 -0.04147 -0.15796 0.04053  141 MET A N   
2253 C CA  . MET A 141 ? 0.83669 0.82128 0.78390 -0.04140 -0.17808 0.04199  141 MET A CA  
2254 C C   . MET A 141 ? 0.85812 0.83660 0.78587 -0.04684 -0.18291 0.03594  141 MET A C   
2255 O O   . MET A 141 ? 0.84335 0.81065 0.76325 -0.05117 -0.20437 0.03898  141 MET A O   
2256 C CB  . MET A 141 ? 0.80507 0.81002 0.80389 -0.03384 -0.17306 0.03915  141 MET A CB  
2257 C CG  . MET A 141 ? 1.05662 1.06524 1.08774 -0.03317 -0.19215 0.04012  141 MET A CG  
2258 S SD  . MET A 141 ? 0.89688 0.91575 0.94240 -0.03375 -0.18667 0.02956  141 MET A SD  
2259 C CE  . MET A 141 ? 1.07688 1.11542 1.15704 -0.02604 -0.16119 0.02394  141 MET A CE  
2269 N N   . LEU A 142 ? 0.84477 0.82973 0.76514 -0.04679 -0.16411 0.02727  142 LEU A N   
2270 C CA  . LEU A 142 ? 0.85075 0.82944 0.75268 -0.05204 -0.16677 0.02070  142 LEU A CA  
2271 C C   . LEU A 142 ? 0.90158 0.85560 0.75396 -0.06084 -0.17719 0.02369  142 LEU A C   
2272 O O   . LEU A 142 ? 0.86606 0.80933 0.70578 -0.06613 -0.19382 0.02267  142 LEU A O   
2273 C CB  . LEU A 142 ? 0.81844 0.80645 0.71903 -0.05036 -0.14356 0.01171  142 LEU A CB  
2274 C CG  . LEU A 142 ? 0.82537 0.83386 0.76745 -0.04332 -0.13325 0.00721  142 LEU A CG  
2275 C CD1 . LEU A 142 ? 0.69105 0.70409 0.62410 -0.04277 -0.11299 -0.00071 142 LEU A CD1 
2276 C CD2 . LEU A 142 ? 0.80793 0.82178 0.77832 -0.04304 -0.14724 0.00568  142 LEU A CD2 
2288 N N   . VAL A 143 ? 0.83429 0.77781 0.65736 -0.06298 -0.16722 0.02711  143 VAL A N   
2289 C CA  . VAL A 143 ? 0.93352 0.85067 0.70498 -0.07207 -0.17355 0.02987  143 VAL A CA  
2290 C C   . VAL A 143 ? 0.94573 0.84842 0.71067 -0.07509 -0.20224 0.03936  143 VAL A C   
2291 O O   . VAL A 143 ? 0.99526 0.87706 0.72476 -0.08302 -0.21661 0.03979  143 VAL A O   
2292 C CB  . VAL A 143 ? 0.91213 0.82207 0.65941 -0.07332 -0.15496 0.03192  143 VAL A CB  
2293 C CG1 . VAL A 143 ? 1.04292 0.92281 0.73822 -0.08262 -0.16353 0.03783  143 VAL A CG1 
2294 C CG2 . VAL A 143 ? 0.90103 0.81937 0.64616 -0.07271 -0.12961 0.02172  143 VAL A CG2 
2304 N N   . ALA A 144 ? 0.90304 0.81526 0.70152 -0.06904 -0.21145 0.04706  144 ALA A N   
2305 C CA  . ALA A 144 ? 0.83945 0.73912 0.63847 -0.07094 -0.24026 0.05682  144 ALA A CA  
2306 C C   . ALA A 144 ? 0.94949 0.85092 0.76447 -0.07255 -0.26041 0.05340  144 ALA A C   
2307 O O   . ALA A 144 ? 0.96849 0.84944 0.75755 -0.07905 -0.28424 0.05805  144 ALA A O   
2308 C CB  . ALA A 144 ? 0.86312 0.77578 0.70374 -0.06310 -0.24359 0.06423  144 ALA A CB  
2314 N N   . ARG A 145 ? 0.95351 0.87791 0.81014 -0.06712 -0.25155 0.04533  145 ARG A N   
2315 C CA  . ARG A 145 ? 1.02893 0.95666 0.90600 -0.06855 -0.26899 0.04131  145 ARG A CA  
2316 C C   . ARG A 145 ? 1.03993 0.95148 0.87349 -0.07721 -0.27015 0.03432  145 ARG A C   
2317 O O   . ARG A 145 ? 1.05815 0.96487 0.89632 -0.08085 -0.29009 0.03227  145 ARG A O   
2318 C CB  . ARG A 145 ? 1.02225 0.97740 0.95452 -0.06084 -0.25628 0.03453  145 ARG A CB  
2319 C CG  . ARG A 145 ? 1.22676 1.19303 1.21204 -0.05596 -0.27433 0.03906  145 ARG A CG  
2320 C CD  . ARG A 145 ? 1.16930 1.16019 1.20461 -0.04739 -0.25472 0.03500  145 ARG A CD  
2321 N NE  . ARG A 145 ? 1.38358 1.38497 1.47312 -0.04325 -0.26972 0.03768  145 ARG A NE  
2322 C CZ  . ARG A 145 ? 1.26703 1.27633 1.38916 -0.04359 -0.27832 0.03257  145 ARG A CZ  
2323 N NH1 . ARG A 145 ? 1.14089 1.14867 1.24614 -0.04783 -0.27415 0.02458  145 ARG A NH1 
2324 N NH2 . ARG A 145 ? 1.25599 1.27481 1.43132 -0.03966 -0.29096 0.03525  145 ARG A NH2 
2338 N N   . ASN A 146 ? 1.04754 0.95041 0.84100 -0.08073 -0.24900 0.03008  146 ASN A N   
2339 C CA  . ASN A 146 ? 1.10004 0.98326 0.84608 -0.08988 -0.24827 0.02360  146 ASN A CA  
2340 C C   . ASN A 146 ? 1.16460 1.01581 0.85462 -0.09880 -0.26266 0.03092  146 ASN A C   
2341 O O   . ASN A 146 ? 1.19653 1.02756 0.83724 -0.10700 -0.25448 0.02587  146 ASN A O   
2342 C CB  . ASN A 146 ? 1.06876 0.95834 0.80310 -0.08930 -0.21668 0.01440  146 ASN A CB  
2343 C CG  . ASN A 146 ? 1.10217 0.97973 0.80704 -0.09666 -0.21333 0.00419  146 ASN A CG  
2344 O OD1 . ASN A 146 ? 1.12552 1.00876 0.84966 -0.09708 -0.22456 -0.00081 146 ASN A OD1 
2345 N ND2 . ASN A 146 ? 1.03970 0.90005 0.69902 -0.10276 -0.19696 0.00058  146 ASN A ND2 
2352 N N   . GLY A 147 ? 1.15318 0.99793 0.84918 -0.09759 -0.28305 0.04269  147 GLY A N   
2353 C CA  . GLY A 147 ? 1.19533 1.00760 0.83776 -0.10604 -0.29902 0.05131  147 GLY A CA  
2354 C C   . GLY A 147 ? 1.17192 0.97233 0.78046 -0.10771 -0.27926 0.05582  147 GLY A C   
2355 O O   . GLY A 147 ? 1.25738 1.02791 0.81667 -0.11543 -0.29002 0.06341  147 GLY A O   
2359 N N   . GLY A 148 ? 1.18082 1.00228 0.81336 -0.10114 -0.25117 0.05153  148 GLY A N   
2360 C CA  . GLY A 148 ? 1.18360 0.99651 0.79101 -0.10229 -0.23123 0.05505  148 GLY A CA  
2361 C C   . GLY A 148 ? 1.17684 0.98619 0.75675 -0.10629 -0.20208 0.04468  148 GLY A C   
2362 O O   . GLY A 148 ? 1.23627 1.03699 0.79430 -0.10825 -0.18408 0.04670  148 GLY A O   
2366 N N   . ALA A 149 ? 1.19674 1.01234 0.77956 -0.10758 -0.19637 0.03354  149 ALA A N   
2367 C CA  . ALA A 149 ? 1.17749 0.99163 0.74115 -0.11064 -0.16846 0.02275  149 ALA A CA  
2368 C C   . ALA A 149 ? 1.06049 0.90373 0.67012 -0.10310 -0.15743 0.01322  149 ALA A C   
2369 O O   . ALA A 149 ? 0.99975 0.85357 0.63589 -0.10049 -0.17326 0.01163  149 ALA A O   
2370 C CB  . ALA A 149 ? 1.22407 1.00730 0.73033 -0.12268 -0.17119 0.01775  149 ALA A CB  
2376 N N   . ALA A 150 ? 1.04726 0.90265 0.66729 -0.09973 -0.13074 0.00725  150 ALA A N   
2377 C CA  . ALA A 150 ? 1.07254 0.95230 0.73106 -0.09316 -0.11938 -0.00146 150 ALA A CA  
2378 C C   . ALA A 150 ? 1.00715 0.87737 0.64674 -0.09917 -0.11927 -0.01130 150 ALA A C   
2379 O O   . ALA A 150 ? 0.95463 0.80179 0.54957 -0.10794 -0.11219 -0.01516 150 ALA A O   
2380 C CB  . ALA A 150 ? 1.03799 0.93046 0.70988 -0.08863 -0.09276 -0.00510 150 ALA A CB  
2386 N N   . PRO A 151 ? 1.05813 0.94422 0.73007 -0.09515 -0.12603 -0.01588 151 PRO A N   
2387 C CA  . PRO A 151 ? 1.01739 0.89544 0.67435 -0.10062 -0.12426 -0.02615 151 PRO A CA  
2388 C C   . PRO A 151 ? 1.04775 0.92670 0.69682 -0.10107 -0.09611 -0.03519 151 PRO A C   
2389 O O   . PRO A 151 ? 1.01544 0.91098 0.68920 -0.09421 -0.07958 -0.03482 151 PRO A O   
2390 C CB  . PRO A 151 ? 1.13021 1.02930 0.83326 -0.09446 -0.13471 -0.02805 151 PRO A CB  
2391 C CG  . PRO A 151 ? 1.02937 0.95116 0.77387 -0.08449 -0.13049 -0.02176 151 PRO A CG  
2392 C CD  . PRO A 151 ? 1.00835 0.92002 0.73282 -0.08559 -0.13266 -0.01265 151 PRO A CD  
2400 N N   . LEU A 152 ? 1.05390 0.91410 0.66914 -0.10939 -0.09114 -0.04371 152 LEU A N   
2401 C CA  . LEU A 152 ? 1.15857 1.01413 0.76066 -0.11158 -0.06411 -0.05253 152 LEU A CA  
2402 C C   . LEU A 152 ? 1.12849 0.99503 0.75255 -0.10935 -0.05409 -0.06335 152 LEU A C   
2403 O O   . LEU A 152 ? 0.97131 0.83620 0.59173 -0.11014 -0.03152 -0.07107 152 LEU A O   
2404 C CB  . LEU A 152 ? 1.23245 1.05476 0.77555 -0.12359 -0.06016 -0.05507 152 LEU A CB  
2405 C CG  . LEU A 152 ? 1.28365 1.09108 0.79953 -0.12674 -0.06717 -0.04409 152 LEU A CG  
2406 C CD1 . LEU A 152 ? 1.30354 1.07347 0.75532 -0.14002 -0.06915 -0.04591 152 LEU A CD1 
2407 C CD2 . LEU A 152 ? 1.30318 1.12235 0.83603 -0.12141 -0.04594 -0.04138 152 LEU A CD2 
2419 N N   . THR A 153 ? 1.03655 0.91416 0.68581 -0.10651 -0.06956 -0.06412 153 THR A N   
2420 C CA  . THR A 153 ? 1.03373 0.92267 0.70744 -0.10371 -0.06040 -0.07325 153 THR A CA  
2421 C C   . THR A 153 ? 0.95428 0.87013 0.67901 -0.09347 -0.06575 -0.06884 153 THR A C   
2422 O O   . THR A 153 ? 0.90529 0.82807 0.64461 -0.09051 -0.08226 -0.06046 153 THR A O   
2423 C CB  . THR A 153 ? 0.98519 0.85821 0.63791 -0.11184 -0.07136 -0.08099 153 THR A CB  
2424 O OG1 . THR A 153 ? 1.02500 0.90440 0.69626 -0.11058 -0.09665 -0.07599 153 THR A OG1 
2425 C CG2 . THR A 153 ? 1.05963 0.90120 0.65457 -0.12344 -0.07123 -0.08385 153 THR A CG2 
2433 N N   . MET A 154 ? 0.93040 0.85991 0.68182 -0.08831 -0.05101 -0.07462 154 MET A N   
2434 C CA  . MET A 154 ? 0.88530 0.83736 0.68140 -0.07940 -0.05351 -0.07125 154 MET A CA  
2435 C C   . MET A 154 ? 0.88513 0.83892 0.69479 -0.08082 -0.07383 -0.07048 154 MET A C   
2436 O O   . MET A 154 ? 0.82199 0.78884 0.65957 -0.07561 -0.08352 -0.06380 154 MET A O   
2437 C CB  . MET A 154 ? 0.84685 0.80840 0.66311 -0.07500 -0.03521 -0.07783 154 MET A CB  
2438 C CG  . MET A 154 ? 0.79628 0.77864 0.65372 -0.06567 -0.03314 -0.07391 154 MET A CG  
2439 S SD  . MET A 154 ? 0.90908 0.90356 0.78331 -0.05958 -0.04127 -0.06243 154 MET A SD  
2440 C CE  . MET A 154 ? 0.78688 0.80005 0.70057 -0.05026 -0.03170 -0.06140 154 MET A CE  
2450 N N   . GLN A 155 ? 0.88412 0.82441 0.67587 -0.08810 -0.08018 -0.07778 155 GLN A N   
2451 C CA  . GLN A 155 ? 0.97538 0.91726 0.78290 -0.08993 -0.10033 -0.07788 155 GLN A CA  
2452 C C   . GLN A 155 ? 0.87516 0.81340 0.67826 -0.09121 -0.12214 -0.06871 155 GLN A C   
2453 O O   . GLN A 155 ? 0.78098 0.73209 0.61829 -0.08706 -0.13470 -0.06411 155 GLN A O   
2454 C CB  . GLN A 155 ? 1.04290 0.96776 0.82647 -0.09876 -0.10446 -0.08789 155 GLN A CB  
2455 C CG  . GLN A 155 ? 1.12466 1.05430 0.92191 -0.09733 -0.08660 -0.09747 155 GLN A CG  
2456 C CD  . GLN A 155 ? 0.94419 0.89657 0.79041 -0.08838 -0.08167 -0.09529 155 GLN A CD  
2457 O OE1 . GLN A 155 ? 0.91402 0.88042 0.77976 -0.08079 -0.07459 -0.08839 155 GLN A OE1 
2458 N NE2 . GLN A 155 ? 1.00564 0.96006 0.87009 -0.08976 -0.08476 -0.10145 155 GLN A NE2 
2467 N N   . SER A 156 ? 0.85485 0.77454 0.61658 -0.09705 -0.12612 -0.06589 156 SER A N   
2468 C CA  . SER A 156 ? 0.94965 0.86409 0.70570 -0.09813 -0.14729 -0.05612 156 SER A CA  
2469 C C   . SER A 156 ? 0.91597 0.85036 0.70697 -0.08862 -0.14383 -0.04738 156 SER A C   
2470 O O   . SER A 156 ? 0.82077 0.76201 0.63582 -0.08598 -0.16134 -0.04075 156 SER A O   
2471 C CB  . SER A 156 ? 1.03888 0.92733 0.74010 -0.10638 -0.14907 -0.05430 156 SER A CB  
2472 O OG  . SER A 156 ? 1.14280 1.02884 0.84143 -0.10510 -0.16324 -0.04292 156 SER A OG  
2478 N N   . PHE A 157 ? 0.84354 0.78689 0.63904 -0.08355 -0.12156 -0.04765 157 PHE A N   
2479 C CA  . PHE A 157 ? 0.78832 0.74892 0.61394 -0.07506 -0.11741 -0.04027 157 PHE A CA  
2480 C C   . PHE A 157 ? 0.74673 0.72644 0.61939 -0.06876 -0.12096 -0.04032 157 PHE A C   
2481 O O   . PHE A 157 ? 0.70310 0.69211 0.60124 -0.06439 -0.12986 -0.03360 157 PHE A O   
2482 C CB  . PHE A 157 ? 0.68206 0.64797 0.50423 -0.07132 -0.09372 -0.04179 157 PHE A CB  
2483 C CG  . PHE A 157 ? 0.67649 0.65904 0.52766 -0.06298 -0.08873 -0.03534 157 PHE A CG  
2484 C CD1 . PHE A 157 ? 0.67927 0.65831 0.52185 -0.06255 -0.09357 -0.02739 157 PHE A CD1 
2485 C CD2 . PHE A 157 ? 0.63755 0.63734 0.52267 -0.05602 -0.07918 -0.03727 157 PHE A CD2 
2486 C CE1 . PHE A 157 ? 0.64128 0.63451 0.50987 -0.05532 -0.08884 -0.02233 157 PHE A CE1 
2487 C CE2 . PHE A 157 ? 0.59803 0.61059 0.50609 -0.04912 -0.07448 -0.03202 157 PHE A CE2 
2488 C CZ  . PHE A 157 ? 0.57443 0.58412 0.47491 -0.04876 -0.07931 -0.02494 157 PHE A CZ  
2498 N N   A THR A 158 ? 0.77233 0.75710 0.65757 -0.06844 -0.11285 -0.04803 158 THR A N   
2499 N N   B THR A 158 ? 0.77436 0.75913 0.65962 -0.06844 -0.11290 -0.04803 158 THR A N   
2500 C CA  A THR A 158 ? 0.78616 0.78647 0.71405 -0.06359 -0.11485 -0.04860 158 THR A CA  
2501 C CA  B THR A 158 ? 0.78483 0.78521 0.71287 -0.06355 -0.11488 -0.04852 158 THR A CA  
2502 C C   A THR A 158 ? 0.78962 0.78819 0.73216 -0.06636 -0.13855 -0.04594 158 THR A C   
2503 C C   B THR A 158 ? 0.78755 0.78614 0.73018 -0.06635 -0.13858 -0.04594 158 THR A C   
2504 O O   A THR A 158 ? 0.74443 0.75624 0.72573 -0.06155 -0.14256 -0.04280 158 THR A O   
2505 O O   B THR A 158 ? 0.74452 0.75631 0.72596 -0.06161 -0.14261 -0.04291 158 THR A O   
2506 C CB  A THR A 158 ? 0.75681 0.75921 0.69094 -0.06402 -0.10290 -0.05731 158 THR A CB  
2507 C CB  B THR A 158 ? 0.75415 0.75697 0.68911 -0.06380 -0.10271 -0.05717 158 THR A CB  
2508 O OG1 A THR A 158 ? 0.73828 0.74350 0.66475 -0.06051 -0.08209 -0.05902 158 THR A OG1 
2509 O OG1 B THR A 158 ? 0.78759 0.77437 0.69369 -0.07204 -0.10924 -0.06371 158 THR A OG1 
2510 C CG2 A THR A 158 ? 0.74016 0.75643 0.71705 -0.05990 -0.10391 -0.05792 158 THR A CG2 
2511 C CG2 B THR A 158 ? 0.74749 0.75532 0.67914 -0.05922 -0.08040 -0.05860 158 THR A CG2 
2526 N N   . LYS A 159 ? 0.80137 0.78260 0.71353 -0.07434 -0.15450 -0.04732 159 LYS A N   
2527 C CA  . LYS A 159 ? 0.82984 0.80754 0.75430 -0.07730 -0.18067 -0.04389 159 LYS A CA  
2528 C C   . LYS A 159 ? 0.81808 0.80091 0.75728 -0.07297 -0.18983 -0.03357 159 LYS A C   
2529 O O   . LYS A 159 ? 0.80965 0.80218 0.78735 -0.07010 -0.20278 -0.03031 159 LYS A O   
2530 C CB  . LYS A 159 ? 0.96216 0.91610 0.84164 -0.08738 -0.19623 -0.04665 159 LYS A CB  
2531 C CG  . LYS A 159 ? 1.11813 1.06765 1.01062 -0.09233 -0.21965 -0.04980 159 LYS A CG  
2532 C CD  . LYS A 159 ? 1.32550 1.24819 1.16572 -0.10325 -0.23281 -0.05399 159 LYS A CD  
2533 C CE  . LYS A 159 ? 1.29025 1.19429 1.08012 -0.10683 -0.23088 -0.04840 159 LYS A CE  
2534 N NZ  . LYS A 159 ? 1.52770 1.40207 1.26454 -0.11830 -0.24730 -0.05106 159 LYS A NZ  
2549 N N   . LEU A 160 ? 0.83363 0.80999 0.74506 -0.07246 -0.18233 -0.02865 160 LEU A N   
2550 C CA  . LEU A 160 ? 0.90937 0.88734 0.82974 -0.06924 -0.19200 -0.01866 160 LEU A CA  
2551 C C   . LEU A 160 ? 0.85200 0.85165 0.82004 -0.06016 -0.18164 -0.01644 160 LEU A C   
2552 O O   . LEU A 160 ? 0.69463 0.70043 0.69321 -0.05723 -0.19481 -0.01087 160 LEU A O   
2553 C CB  . LEU A 160 ? 0.93253 0.89752 0.81088 -0.07140 -0.18385 -0.01471 160 LEU A CB  
2554 C CG  . LEU A 160 ? 0.86014 0.82679 0.74573 -0.06758 -0.18905 -0.00448 160 LEU A CG  
2555 C CD1 . LEU A 160 ? 0.85637 0.81227 0.74223 -0.07091 -0.21823 0.00263  160 LEU A CD1 
2556 C CD2 . LEU A 160 ? 0.88937 0.84531 0.73692 -0.06943 -0.17505 -0.00229 160 LEU A CD2 
2568 N N   . VAL A 161 ? 0.71739 0.72744 0.69196 -0.05581 -0.15809 -0.02077 161 VAL A N   
2569 C CA  . VAL A 161 ? 0.70131 0.72857 0.71454 -0.04800 -0.14694 -0.01900 161 VAL A CA  
2570 C C   . VAL A 161 ? 0.71382 0.75101 0.76939 -0.04656 -0.15367 -0.02155 161 VAL A C   
2571 O O   . VAL A 161 ? 0.64682 0.69440 0.73835 -0.04179 -0.15419 -0.01821 161 VAL A O   
2572 C CB  . VAL A 161 ? 0.71505 0.74849 0.72210 -0.04430 -0.12232 -0.02282 161 VAL A CB  
2573 C CG1 . VAL A 161 ? 0.72805 0.75156 0.69655 -0.04637 -0.11564 -0.02113 161 VAL A CG1 
2574 C CG2 . VAL A 161 ? 0.72145 0.75630 0.73090 -0.04581 -0.11422 -0.03093 161 VAL A CG2 
2584 N N   . ASP A 162 ? 0.66759 0.70132 0.72112 -0.05091 -0.15785 -0.02798 162 ASP A N   
2585 C CA  . ASP A 162 ? 0.78481 0.82676 0.87970 -0.05056 -0.16598 -0.03057 162 ASP A CA  
2586 C C   . ASP A 162 ? 0.72529 0.76558 0.83941 -0.05163 -0.19051 -0.02474 162 ASP A C   
2587 O O   . ASP A 162 ? 0.68879 0.74031 0.84889 -0.04816 -0.19340 -0.02377 162 ASP A O   
2588 C CB  . ASP A 162 ? 0.67154 0.70795 0.75756 -0.05599 -0.16816 -0.03866 162 ASP A CB  
2589 C CG  . ASP A 162 ? 0.70156 0.74406 0.78951 -0.05331 -0.14407 -0.04451 162 ASP A CG  
2590 O OD1 . ASP A 162 ? 0.69276 0.74383 0.79037 -0.04728 -0.12701 -0.04213 162 ASP A OD1 
2591 O OD2 . ASP A 162 ? 0.67396 0.71147 0.75291 -0.05741 -0.14290 -0.05141 162 ASP A OD2 
2596 N N   . ARG A 163 ? 0.81461 0.83977 0.89424 -0.05657 -0.20803 -0.02067 163 ARG A N   
2597 C CA  . ARG A 163 ? 0.89302 0.91458 0.98793 -0.05727 -0.23307 -0.01350 163 ARG A CA  
2598 C C   . ARG A 163 ? 0.82774 0.85945 0.94860 -0.05017 -0.22663 -0.00666 163 ARG A C   
2599 O O   . ARG A 163 ? 0.71445 0.75319 0.87704 -0.04750 -0.23911 -0.00315 163 ARG A O   
2600 C CB  . ARG A 163 ? 0.99110 0.99066 1.03526 -0.06445 -0.25142 -0.00973 163 ARG A CB  
2601 C CG  . ARG A 163 ? 1.12814 1.11539 1.15980 -0.07232 -0.27227 -0.01432 163 ARG A CG  
2602 C CD  . ARG A 163 ? 1.19007 1.15401 1.15645 -0.08038 -0.27421 -0.01587 163 ARG A CD  
2603 N NE  . ARG A 163 ? 1.27227 1.22364 1.20575 -0.08100 -0.27776 -0.00689 163 ARG A NE  
2604 C CZ  . ARG A 163 ? 1.34472 1.27801 1.22288 -0.08623 -0.26955 -0.00727 163 ARG A CZ  
2605 N NH1 . ARG A 163 ? 1.17947 1.10478 1.02824 -0.09128 -0.25747 -0.01650 163 ARG A NH1 
2606 N NH2 . ARG A 163 ? 1.31190 1.23423 1.16493 -0.08659 -0.27254 0.00159  163 ARG A NH2 
2620 N N   . VAL A 164 ? 0.81312 0.84535 0.91148 -0.04719 -0.20738 -0.00508 164 VAL A N   
2621 C CA  . VAL A 164 ? 0.81215 0.85219 0.93080 -0.04100 -0.20074 0.00086  164 VAL A CA  
2622 C C   . VAL A 164 ? 0.70044 0.75769 0.86845 -0.03512 -0.18647 -0.00267 164 VAL A C   
2623 O O   . VAL A 164 ? 0.66185 0.72611 0.86392 -0.03078 -0.18826 0.00126  164 VAL A O   
2624 C CB  . VAL A 164 ? 0.88163 0.91714 0.96302 -0.03999 -0.18401 0.00256  164 VAL A CB  
2625 C CG1 . VAL A 164 ? 0.83773 0.88381 0.94340 -0.03311 -0.17128 0.00595  164 VAL A CG1 
2626 C CG2 . VAL A 164 ? 0.94164 0.95874 0.97976 -0.04557 -0.19866 0.00811  164 VAL A CG2 
2636 N N   . GLY A 165 ? 0.60997 0.67273 0.78181 -0.03509 -0.17127 -0.01005 165 GLY A N   
2637 C CA  . GLY A 165 ? 0.59807 0.67401 0.81063 -0.03043 -0.15513 -0.01364 165 GLY A CA  
2638 C C   . GLY A 165 ? 0.58064 0.66015 0.77946 -0.02639 -0.12973 -0.01515 165 GLY A C   
2639 O O   . GLY A 165 ? 0.58424 0.65778 0.74485 -0.02708 -0.12371 -0.01438 165 GLY A O   
2643 N N   . ASP A 166 ? 0.53651 0.62502 0.76825 -0.02239 -0.11468 -0.01747 166 ASP A N   
2644 C CA  . ASP A 166 ? 0.49246 0.58292 0.71260 -0.01888 -0.09168 -0.01918 166 ASP A CA  
2645 C C   . ASP A 166 ? 0.51715 0.60539 0.71829 -0.01627 -0.08923 -0.01416 166 ASP A C   
2646 O O   . ASP A 166 ? 0.50423 0.59242 0.71741 -0.01544 -0.10041 -0.00937 166 ASP A O   
2647 C CB  . ASP A 166 ? 0.60636 0.70377 0.86425 -0.01583 -0.07664 -0.02214 166 ASP A CB  
2648 C CG  . ASP A 166 ? 0.65901 0.75798 0.93193 -0.01822 -0.07271 -0.02772 166 ASP A CG  
2649 O OD1 . ASP A 166 ? 0.66176 0.75675 0.91470 -0.02200 -0.08118 -0.02982 166 ASP A OD1 
2650 O OD2 . ASP A 166 ? 0.59164 0.69474 0.89587 -0.01663 -0.05985 -0.03037 166 ASP A OD2 
2655 N N   . PRO A 167 ? 0.46712 0.55332 0.64052 -0.01488 -0.07503 -0.01509 167 PRO A N   
2656 C CA  . PRO A 167 ? 0.49857 0.58344 0.65849 -0.01229 -0.07095 -0.01110 167 PRO A CA  
2657 C C   . PRO A 167 ? 0.51836 0.60825 0.70792 -0.00813 -0.06166 -0.01064 167 PRO A C   
2658 O O   . PRO A 167 ? 0.48010 0.57379 0.69577 -0.00718 -0.05335 -0.01417 167 PRO A O   
2659 C CB  . PRO A 167 ? 0.44759 0.52991 0.57704 -0.01190 -0.05777 -0.01348 167 PRO A CB  
2660 C CG  . PRO A 167 ? 0.51920 0.60107 0.64583 -0.01406 -0.05470 -0.01844 167 PRO A CG  
2661 C CD  . PRO A 167 ? 0.44215 0.52744 0.60028 -0.01530 -0.06199 -0.01993 167 PRO A CD  
2669 N N   . PRO A 168 ? 0.51203 0.60101 0.69843 -0.00595 -0.06137 -0.00681 168 PRO A N   
2670 C CA  . PRO A 168 ? 0.49710 0.58937 0.71080 -0.00233 -0.05125 -0.00725 168 PRO A CA  
2671 C C   . PRO A 168 ? 0.49477 0.58688 0.70540 -0.00070 -0.03087 -0.01219 168 PRO A C   
2672 O O   . PRO A 168 ? 0.50638 0.59580 0.68959 -0.00130 -0.02472 -0.01384 168 PRO A O   
2673 C CB  . PRO A 168 ? 0.57633 0.66587 0.77751 -0.00087 -0.05399 -0.00265 168 PRO A CB  
2674 C CG  . PRO A 168 ? 0.57061 0.65539 0.74580 -0.00418 -0.06965 0.00148  168 PRO A CG  
2675 C CD  . PRO A 168 ? 0.53069 0.61445 0.68777 -0.00703 -0.06828 -0.00243 168 PRO A CD  
2683 N N   . ALA A 169 ? 0.47388 0.56761 0.71324 0.00114  -0.02028 -0.01454 169 ALA A N   
2684 C CA  . ALA A 169 ? 0.55943 0.64968 0.79350 0.00216  -0.00045 -0.01876 169 ALA A CA  
2685 C C   . ALA A 169 ? 0.53174 0.61716 0.73819 0.00390  0.00700  -0.01797 169 ALA A C   
2686 O O   . ALA A 169 ? 0.46036 0.54627 0.66298 0.00482  -0.00004 -0.01474 169 ALA A O   
2687 C CB  . ALA A 169 ? 0.65536 0.74639 0.92675 0.00303  0.01086  -0.02188 169 ALA A CB  
2693 N N   . PRO A 170 ? 0.57768 0.65755 0.76422 0.00416  0.02019  -0.02064 170 PRO A N   
2694 C CA  . PRO A 170 ? 0.56221 0.63671 0.72515 0.00564  0.02653  -0.02041 170 PRO A CA  
2695 C C   . PRO A 170 ? 0.55027 0.62246 0.73007 0.00709  0.03401  -0.02141 170 PRO A C   
2696 O O   . PRO A 170 ? 0.54609 0.61772 0.75222 0.00704  0.04242  -0.02399 170 PRO A O   
2697 C CB  . PRO A 170 ? 0.67476 0.74212 0.81768 0.00537  0.03811  -0.02298 170 PRO A CB  
2698 C CG  . PRO A 170 ? 0.65991 0.72870 0.81713 0.00380  0.04015  -0.02466 170 PRO A CG  
2699 C CD  . PRO A 170 ? 0.60309 0.68015 0.79021 0.00297  0.02958  -0.02381 170 PRO A CD  
2707 N N   . ALA A 171 ? 0.51760 0.58815 0.68385 0.00819  0.03168  -0.01981 171 ALA A N   
2708 C CA  . ALA A 171 ? 0.53900 0.60669 0.72023 0.00947  0.03845  -0.02109 171 ALA A CA  
2709 C C   . ALA A 171 ? 0.55975 0.61707 0.73328 0.00920  0.05713  -0.02618 171 ALA A C   
2710 O O   . ALA A 171 ? 0.58402 0.63546 0.73314 0.00836  0.06230  -0.02739 171 ALA A O   
2711 C CB  . ALA A 171 ? 0.47572 0.54342 0.64298 0.01030  0.03128  -0.01827 171 ALA A CB  
2717 N N   . PRO A 172 ? 0.52571 0.57903 0.71894 0.00969  0.06764  -0.02921 172 PRO A N   
2718 C CA  . PRO A 172 ? 0.54338 0.58345 0.72525 0.00855  0.08691  -0.03453 172 PRO A CA  
2719 C C   . PRO A 172 ? 0.58305 0.61381 0.72595 0.00826  0.08803  -0.03506 172 PRO A C   
2720 O O   . PRO A 172 ? 0.54302 0.57822 0.67521 0.00927  0.07639  -0.03220 172 PRO A O   
2721 C CB  . PRO A 172 ? 0.57350 0.61196 0.78692 0.00914  0.09643  -0.03780 172 PRO A CB  
2722 C CG  . PRO A 172 ? 0.55436 0.60656 0.80221 0.01076  0.08135  -0.03368 172 PRO A CG  
2723 C CD  . PRO A 172 ? 0.53019 0.58944 0.75674 0.01108  0.06244  -0.02790 172 PRO A CD  
2731 N N   . ASP A 173 ? 0.55652 0.57311 0.67809 0.00651  0.10195  -0.03868 173 ASP A N   
2732 C CA  . ASP A 173 ? 0.63713 0.64235 0.72247 0.00588  0.10263  -0.03970 173 ASP A CA  
2733 C C   . ASP A 173 ? 0.65103 0.65208 0.74040 0.00607  0.10626  -0.04262 173 ASP A C   
2734 O O   . ASP A 173 ? 0.62181 0.62282 0.73835 0.00611  0.11550  -0.04550 173 ASP A O   
2735 C CB  . ASP A 173 ? 0.74829 0.73586 0.80785 0.00342  0.11636  -0.04254 173 ASP A CB  
2736 C CG  . ASP A 173 ? 0.82316 0.81296 0.87238 0.00335  0.11127  -0.03919 173 ASP A CG  
2737 O OD1 . ASP A 173 ? 0.71323 0.71433 0.75935 0.00501  0.09582  -0.03527 173 ASP A OD1 
2738 O OD2 . ASP A 173 ? 0.83893 0.81816 0.88316 0.00139  0.12377  -0.04072 173 ASP A OD2 
2743 N N   . PRO A 174 ? 0.67232 0.67004 0.73799 0.00618  0.09905  -0.04222 174 PRO A N   
2744 C CA  . PRO A 174 ? 0.70704 0.70012 0.77570 0.00610  0.10215  -0.04537 174 PRO A CA  
2745 C C   . PRO A 174 ? 0.66806 0.64130 0.72243 0.00336  0.12067  -0.05222 174 PRO A C   
2746 O O   . PRO A 174 ? 0.63532 0.59673 0.67101 0.00131  0.12993  -0.05376 174 PRO A O   
2747 C CB  . PRO A 174 ? 0.68345 0.67844 0.72952 0.00651  0.08847  -0.04306 174 PRO A CB  
2748 C CG  . PRO A 174 ? 0.73610 0.72862 0.75814 0.00605  0.08395  -0.04094 174 PRO A CG  
2749 C CD  . PRO A 174 ? 0.63847 0.63751 0.67745 0.00646  0.08696  -0.03899 174 PRO A CD  
2757 N N   . PRO A 175 ? 0.73591 0.70326 0.79705 0.00288  0.12723  -0.05656 175 PRO A N   
2758 C CA  . PRO A 175 ? 0.75725 0.70339 0.80402 -0.00045 0.14710  -0.06420 175 PRO A CA  
2759 C C   . PRO A 175 ? 0.68926 0.61698 0.68734 -0.00341 0.14683  -0.06590 175 PRO A C   
2760 O O   . PRO A 175 ? 0.74178 0.67380 0.72118 -0.00251 0.13053  -0.06221 175 PRO A O   
2761 C CB  . PRO A 175 ? 0.82816 0.77393 0.89316 0.00003  0.15051  -0.06810 175 PRO A CB  
2762 C CG  . PRO A 175 ? 0.81873 0.78652 0.91362 0.00390  0.13321  -0.06148 175 PRO A CG  
2763 C CD  . PRO A 175 ? 0.79608 0.77400 0.87610 0.00495  0.11733  -0.05484 175 PRO A CD  
2771 N N   . ALA A 176 ? 0.64007 0.54564 0.61784 -0.00728 0.16545  -0.07164 176 ALA A N   
2772 C CA  . ALA A 176 ? 0.74476 0.62837 0.67263 -0.01077 0.16530  -0.07310 176 ALA A CA  
2773 C C   . ALA A 176 ? 0.74957 0.62470 0.65653 -0.01204 0.15802  -0.07655 176 ALA A C   
2774 O O   . ALA A 176 ? 0.77316 0.63480 0.64144 -0.01405 0.14943  -0.07610 176 ALA A O   
2775 C CB  . ALA A 176 ? 0.70772 0.56649 0.61635 -0.01544 0.18868  -0.07845 176 ALA A CB  
2781 N N   . ALA A 177 ? 0.67147 0.55358 0.60421 -0.01097 0.16054  -0.07992 177 ALA A N   
2782 C CA  . ALA A 177 ? 0.73642 0.61368 0.65607 -0.01188 0.15254  -0.08309 177 ALA A CA  
2783 C C   . ALA A 177 ? 0.69574 0.59781 0.65310 -0.00753 0.13971  -0.07887 177 ALA A C   
2784 O O   . ALA A 177 ? 0.70099 0.61706 0.69648 -0.00488 0.14395  -0.07695 177 ALA A O   
2785 C CB  . ALA A 177 ? 0.74082 0.59507 0.64876 -0.01616 0.17187  -0.09309 177 ALA A CB  
2791 N N   . MET A 178 ? 0.69961 0.60583 0.64622 -0.00710 0.12376  -0.07731 178 MET A N   
2792 C CA  . MET A 178 ? 0.73696 0.66423 0.71343 -0.00365 0.11118  -0.07257 178 MET A CA  
2793 C C   . MET A 178 ? 0.69325 0.61447 0.66905 -0.00503 0.11030  -0.07750 178 MET A C   
2794 O O   . MET A 178 ? 0.71665 0.61981 0.66118 -0.00858 0.11147  -0.08324 178 MET A O   
2795 C CB  . MET A 178 ? 0.75485 0.69568 0.72467 -0.00177 0.09261  -0.06538 178 MET A CB  
2796 C CG  . MET A 178 ? 0.86625 0.81652 0.84321 0.00006  0.09189  -0.05999 178 MET A CG  
2797 S SD  . MET A 178 ? 0.88828 0.85990 0.87430 0.00297  0.07251  -0.05160 178 MET A SD  
2798 C CE  . MET A 178 ? 0.80577 0.78790 0.81237 0.00481  0.07672  -0.04736 178 MET A CE  
2808 N N   . PRO A 179 ? 0.67220 0.60661 0.68095 -0.00258 0.10769  -0.07537 179 PRO A N   
2809 C CA  . PRO A 179 ? 0.72757 0.65761 0.73722 -0.00378 0.10510  -0.07931 179 PRO A CA  
2810 C C   . PRO A 179 ? 0.74245 0.67572 0.73247 -0.00450 0.08812  -0.07690 179 PRO A C   
2811 O O   . PRO A 179 ? 0.67456 0.62405 0.67312 -0.00212 0.07586  -0.06938 179 PRO A O   
2812 C CB  . PRO A 179 ? 0.69099 0.63667 0.74250 -0.00035 0.10358  -0.07476 179 PRO A CB  
2813 C CG  . PRO A 179 ? 0.73822 0.69185 0.81084 0.00196  0.10942  -0.07111 179 PRO A CG  
2814 C CD  . PRO A 179 ? 0.73067 0.68304 0.77719 0.00113  0.10632  -0.06913 179 PRO A CD  
2822 N N   . PRO A 180 ? 0.77661 0.69408 0.74094 -0.00803 0.08707  -0.08351 180 PRO A N   
2823 C CA  . PRO A 180 ? 0.78617 0.70586 0.73345 -0.00891 0.07034  -0.08179 180 PRO A CA  
2824 C C   . PRO A 180 ? 0.80493 0.73655 0.77434 -0.00801 0.06162  -0.07994 180 PRO A C   
2825 O O   . PRO A 180 ? 0.75924 0.69327 0.75193 -0.00722 0.06866  -0.08094 180 PRO A O   
2826 C CB  . PRO A 180 ? 0.84026 0.73477 0.74978 -0.01371 0.07295  -0.09034 180 PRO A CB  
2827 C CG  . PRO A 180 ? 0.74728 0.62964 0.66394 -0.01553 0.09001  -0.09787 180 PRO A CG  
2828 C CD  . PRO A 180 ? 0.80440 0.70001 0.75458 -0.01180 0.10109  -0.09357 180 PRO A CD  
2836 N N   . PRO A 181 ? 0.74291 0.68159 0.70753 -0.00817 0.04677  -0.07718 181 PRO A N   
2837 C CA  . PRO A 181 ? 0.73419 0.68091 0.71693 -0.00838 0.03972  -0.07653 181 PRO A CA  
2838 C C   . PRO A 181 ? 0.71827 0.64869 0.69270 -0.01190 0.04398  -0.08569 181 PRO A C   
2839 O O   . PRO A 181 ? 0.69240 0.60395 0.63929 -0.01497 0.04810  -0.09280 181 PRO A O   
2840 C CB  . PRO A 181 ? 0.76724 0.72183 0.74389 -0.00852 0.02458  -0.07334 181 PRO A CB  
2841 C CG  . PRO A 181 ? 0.81495 0.76603 0.77083 -0.00795 0.02260  -0.07179 181 PRO A CG  
2842 C CD  . PRO A 181 ? 0.78731 0.72803 0.73408 -0.00790 0.03657  -0.07393 181 PRO A CD  
2850 N N   . ALA A 182 ? 0.66162 0.59787 0.65873 -0.01178 0.04342  -0.08546 182 ALA A N   
2851 C CA  . ALA A 182 ? 0.71005 0.63151 0.70269 -0.01519 0.04759  -0.09445 182 ALA A CA  
2852 C C   . ALA A 182 ? 0.77253 0.68382 0.74029 -0.01908 0.03567  -0.10003 182 ALA A C   
2853 O O   . ALA A 182 ? 0.67913 0.59965 0.64461 -0.01853 0.02251  -0.09573 182 ALA A O   
2854 C CB  . ALA A 182 ? 0.75342 0.68382 0.77766 -0.01413 0.04839  -0.09202 182 ALA A CB  
2860 N N   . GLU A 183 ? 0.85879 0.75011 0.80869 -0.02320 0.04018  -0.11005 183 GLU A N   
2861 C CA  . GLU A 183 ? 1.04139 0.91936 0.96480 -0.02756 0.02768  -0.11629 183 GLU A CA  
2862 C C   . GLU A 183 ? 1.02266 0.91051 0.96689 -0.02850 0.01565  -0.11622 183 GLU A C   
2863 O O   . GLU A 183 ? 0.83830 0.73371 0.81000 -0.02761 0.02120  -0.11541 183 GLU A O   
2864 C CB  . GLU A 183 ? 1.13690 0.98716 1.03070 -0.03256 0.03713  -0.12783 183 GLU A CB  
2865 C CG  . GLU A 183 ? 1.09522 0.93156 0.96375 -0.03289 0.05016  -0.12905 183 GLU A CG  
2866 C CD  . GLU A 183 ? 1.13442 0.95670 0.96287 -0.03554 0.03886  -0.12948 183 GLU A CD  
2867 O OE1 . GLU A 183 ? 1.18005 0.98529 0.98301 -0.04036 0.02822  -0.13622 183 GLU A OE1 
2868 O OE2 . GLU A 183 ? 1.30826 1.13587 1.13094 -0.03291 0.03959  -0.12289 183 GLU A OE2 
2875 N N   . ASP A 184 ? 0.93677 0.82396 0.86917 -0.03037 -0.00114 -0.11687 184 ASP A N   
2876 C CA  . ASP A 184 ? 0.97636 0.86959 0.92609 -0.03240 -0.01336 -0.11878 184 ASP A CA  
2877 C C   . ASP A 184 ? 0.81314 0.72875 0.80221 -0.02915 -0.01046 -0.11092 184 ASP A C   
2878 O O   . ASP A 184 ? 0.83406 0.75196 0.84296 -0.03085 -0.01075 -0.11319 184 ASP A O   
2879 C CB  . ASP A 184 ? 0.95184 0.82572 0.89083 -0.03755 -0.01175 -0.13010 184 ASP A CB  
2880 C CG  . ASP A 184 ? 1.14376 0.99095 1.03961 -0.04129 -0.00848 -0.13820 184 ASP A CG  
2881 O OD1 . ASP A 184 ? 1.15398 0.99470 1.02386 -0.04180 -0.01849 -0.13675 184 ASP A OD1 
2882 O OD2 . ASP A 184 ? 1.25092 1.08218 1.13830 -0.04396 0.00470  -0.14607 184 ASP A OD2 
2887 N N   . MET A 185 ? 0.71926 0.64995 0.71806 -0.02487 -0.00765 -0.10157 185 MET A N   
2888 C CA  . MET A 185 ? 0.60771 0.55768 0.63780 -0.02245 -0.00690 -0.09332 185 MET A CA  
2889 C C   . MET A 185 ? 0.63456 0.59469 0.67282 -0.02318 -0.02044 -0.09132 185 MET A C   
2890 O O   . MET A 185 ? 0.59512 0.55752 0.62111 -0.02195 -0.02723 -0.08929 185 MET A O   
2891 C CB  . MET A 185 ? 0.68028 0.64022 0.71592 -0.01818 0.00140  -0.08479 185 MET A CB  
2892 C CG  . MET A 185 ? 0.71945 0.67554 0.76455 -0.01675 0.01495  -0.08439 185 MET A CG  
2893 S SD  . MET A 185 ? 0.67525 0.62868 0.74362 -0.01876 0.01839  -0.08710 185 MET A SD  
2894 C CE  . MET A 185 ? 0.89074 0.85008 0.98036 -0.01470 0.02970  -0.07930 185 MET A CE  
2904 N N   . PRO A 186 ? 0.55634 0.52254 0.61712 -0.02517 -0.02403 -0.09183 186 PRO A N   
2905 C CA  . PRO A 186 ? 0.57037 0.54466 0.64161 -0.02644 -0.03670 -0.09183 186 PRO A CA  
2906 C C   . PRO A 186 ? 0.57055 0.55850 0.64588 -0.02323 -0.03799 -0.08405 186 PRO A C   
2907 O O   . PRO A 186 ? 0.55014 0.53955 0.62160 -0.02332 -0.04910 -0.08527 186 PRO A O   
2908 C CB  . PRO A 186 ? 0.63327 0.61363 0.73326 -0.02879 -0.03502 -0.09190 186 PRO A CB  
2909 C CG  . PRO A 186 ? 0.66079 0.63617 0.76430 -0.02833 -0.02222 -0.09088 186 PRO A CG  
2910 C CD  . PRO A 186 ? 0.63355 0.59729 0.71147 -0.02679 -0.01698 -0.09361 186 PRO A CD  
2918 N N   . SER A 187 ? 0.53723 0.53407 0.61983 -0.02045 -0.02755 -0.07620 187 SER A N   
2919 C CA  . SER A 187 ? 0.56298 0.57197 0.64924 -0.01793 -0.02776 -0.06932 187 SER A CA  
2920 C C   . SER A 187 ? 0.56767 0.57271 0.63079 -0.01546 -0.02962 -0.06886 187 SER A C   
2921 O O   . SER A 187 ? 0.55621 0.56995 0.62082 -0.01352 -0.03136 -0.06441 187 SER A O   
2922 C CB  . SER A 187 ? 0.61516 0.63253 0.71393 -0.01653 -0.01726 -0.06116 187 SER A CB  
2923 O OG  . SER A 187 ? 0.59931 0.61964 0.71891 -0.01915 -0.01517 -0.06047 187 SER A OG  
2929 N N   . ALA A 188 ? 0.58933 0.58026 0.63086 -0.01584 -0.02823 -0.07364 188 ALA A N   
2930 C CA  . ALA A 188 ? 0.58584 0.57012 0.60333 -0.01419 -0.02888 -0.07349 188 ALA A CA  
2931 C C   . ALA A 188 ? 0.60538 0.57699 0.60273 -0.01633 -0.04146 -0.07946 188 ALA A C   
2932 O O   . ALA A 188 ? 0.63201 0.59253 0.60370 -0.01592 -0.04167 -0.08030 188 ALA A O   
2933 C CB  . ALA A 188 ? 0.59653 0.57180 0.60221 -0.01342 -0.01645 -0.07431 188 ALA A CB  
2939 N N   . ALA A 189 ? 0.58433 0.55627 0.59262 -0.01888 -0.05250 -0.08342 189 ALA A N   
2940 C CA  . ALA A 189 ? 0.65480 0.61324 0.64410 -0.02125 -0.06748 -0.08896 189 ALA A CA  
2941 C C   . ALA A 189 ? 0.67803 0.63861 0.65750 -0.01867 -0.07518 -0.08452 189 ALA A C   
2942 O O   . ALA A 189 ? 0.58382 0.56115 0.58505 -0.01603 -0.07510 -0.07899 189 ALA A O   
2943 C CB  . ALA A 189 ? 0.62378 0.58604 0.63483 -0.02408 -0.07940 -0.09314 189 ALA A CB  
2949 N N   . PRO A 190 ? 0.70053 0.64294 0.64648 -0.01967 -0.08133 -0.08680 190 PRO A N   
2950 C CA  . PRO A 190 ? 0.66704 0.61021 0.60325 -0.01703 -0.08812 -0.08182 190 PRO A CA  
2951 C C   . PRO A 190 ? 0.65850 0.61525 0.62088 -0.01561 -0.10248 -0.07948 190 PRO A C   
2952 O O   . PRO A 190 ? 0.58980 0.55809 0.56254 -0.01221 -0.10085 -0.07375 190 PRO A O   
2953 C CB  . PRO A 190 ? 0.73073 0.64737 0.62479 -0.01992 -0.09569 -0.08588 190 PRO A CB  
2954 C CG  . PRO A 190 ? 0.84630 0.74867 0.72517 -0.02361 -0.08570 -0.09278 190 PRO A CG  
2955 C CD  . PRO A 190 ? 0.71984 0.63960 0.63336 -0.02294 -0.07614 -0.09299 190 PRO A CD  
2963 N N   . ALA A 191 ? 0.67143 0.62711 0.64721 -0.01829 -0.11609 -0.08428 191 ALA A N   
2964 C CA  . ALA A 191 ? 0.62600 0.59313 0.62905 -0.01706 -0.13065 -0.08280 191 ALA A CA  
2965 C C   . ALA A 191 ? 0.60668 0.59750 0.64699 -0.01453 -0.11934 -0.07840 191 ALA A C   
2966 O O   . ALA A 191 ? 0.58908 0.59072 0.65063 -0.01240 -0.12547 -0.07571 191 ALA A O   
2967 C CB  . ALA A 191 ? 0.68666 0.64794 0.70015 -0.02089 -0.14749 -0.08953 191 ALA A CB  
2973 N N   . ALA A 192 ? 0.63515 0.63277 0.68329 -0.01498 -0.10284 -0.07766 192 ALA A N   
2974 C CA  . ALA A 192 ? 0.59389 0.61027 0.67128 -0.01351 -0.09132 -0.07326 192 ALA A CA  
2975 C C   . ALA A 192 ? 0.55193 0.57311 0.61861 -0.01034 -0.07848 -0.06699 192 ALA A C   
2976 O O   . ALA A 192 ? 0.54888 0.58319 0.63420 -0.00951 -0.06843 -0.06305 192 ALA A O   
2977 C CB  . ALA A 192 ? 0.53638 0.55631 0.62960 -0.01619 -0.08233 -0.07516 192 ALA A CB  
2983 N N   . THR A 193 ? 0.60281 0.61250 0.63940 -0.00903 -0.07834 -0.06614 193 THR A N   
2984 C CA  . THR A 193 ? 0.55983 0.57311 0.58698 -0.00651 -0.06555 -0.06095 193 THR A CA  
2985 C C   . THR A 193 ? 0.56904 0.57602 0.57630 -0.00427 -0.06978 -0.05863 193 THR A C   
2986 O O   . THR A 193 ? 0.54007 0.54656 0.53534 -0.00263 -0.05977 -0.05533 193 THR A O   
2987 C CB  . THR A 193 ? 0.61720 0.62290 0.63069 -0.00748 -0.05430 -0.06198 193 THR A CB  
2988 O OG1 . THR A 193 ? 0.61346 0.60053 0.60059 -0.00937 -0.05931 -0.06711 193 THR A OG1 
2989 C CG2 . THR A 193 ? 0.56306 0.57526 0.59749 -0.00933 -0.04902 -0.06289 193 THR A CG2 
2997 N N   . GLY A 194 ? 0.59343 0.59503 0.59792 -0.00416 -0.08497 -0.05996 194 GLY A N   
2998 C CA  . GLY A 194 ? 0.54514 0.54013 0.53181 -0.00196 -0.08939 -0.05683 194 GLY A CA  
2999 C C   . GLY A 194 ? 0.59208 0.60262 0.59915 0.00115  -0.08562 -0.05215 194 GLY A C   
3000 O O   . GLY A 194 ? 0.49513 0.52076 0.53083 0.00126  -0.08177 -0.05184 194 GLY A O   
3004 N N   . VAL A 195 ? 0.57041 0.57560 0.56121 0.00329  -0.08570 -0.04876 195 VAL A N   
3005 C CA  . VAL A 195 ? 0.60821 0.62552 0.61557 0.00614  -0.08301 -0.04496 195 VAL A CA  
3006 C C   . VAL A 195 ? 0.54708 0.56654 0.57279 0.00723  -0.09862 -0.04558 195 VAL A C   
3007 O O   . VAL A 195 ? 0.56411 0.56956 0.57354 0.00728  -0.11294 -0.04572 195 VAL A O   
3008 C CB  . VAL A 195 ? 0.67040 0.68072 0.65538 0.00790  -0.07727 -0.04129 195 VAL A CB  
3009 C CG1 . VAL A 195 ? 0.68329 0.70472 0.68565 0.01068  -0.07606 -0.03812 195 VAL A CG1 
3010 C CG2 . VAL A 195 ? 0.56183 0.57210 0.53581 0.00705  -0.06177 -0.04080 195 VAL A CG2 
3020 N N   . PRO A 196 ? 0.57190 0.60713 0.63120 0.00788  -0.09657 -0.04599 196 PRO A N   
3021 C CA  . PRO A 196 ? 0.64097 0.67934 0.72440 0.00916  -0.11111 -0.04699 196 PRO A CA  
3022 C C   . PRO A 196 ? 0.65742 0.69515 0.74042 0.01261  -0.11406 -0.04325 196 PRO A C   
3023 O O   . PRO A 196 ? 0.63541 0.67324 0.70402 0.01381  -0.10288 -0.04023 196 PRO A O   
3024 C CB  . PRO A 196 ? 0.66067 0.71587 0.78116 0.00799  -0.10283 -0.04937 196 PRO A CB  
3025 C CG  . PRO A 196 ? 0.60242 0.66395 0.71534 0.00758  -0.08329 -0.04706 196 PRO A CG  
3026 C CD  . PRO A 196 ? 0.56762 0.61715 0.64498 0.00703  -0.08075 -0.04572 196 PRO A CD  
3034 N N   . THR A 197 ? 0.71227 0.74893 0.81324 0.01419  -0.13040 -0.04356 197 THR A N   
3035 C CA  . THR A 197 ? 0.79686 0.83352 0.90491 0.01775  -0.13512 -0.04019 197 THR A CA  
3036 C C   . THR A 197 ? 0.70223 0.75724 0.85267 0.01898  -0.12638 -0.04190 197 THR A C   
3037 O O   . THR A 197 ? 0.64108 0.70706 0.81676 0.01688  -0.12027 -0.04567 197 THR A O   
3038 C CB  . THR A 197 ? 0.83723 0.86043 0.94160 0.01900  -0.15953 -0.03892 197 THR A CB  
3039 O OG1 . THR A 197 ? 0.70510 0.73655 0.84705 0.01851  -0.17128 -0.04276 197 THR A OG1 
3040 C CG2 . THR A 197 ? 0.82345 0.82537 0.88285 0.01655  -0.16766 -0.03827 197 THR A CG2 
3048 N N   . TRP A 198 ? 0.67143 0.72844 0.82939 0.02208  -0.12474 -0.03936 198 TRP A N   
3049 C CA  . TRP A 198 ? 0.71340 0.78589 0.91070 0.02294  -0.11472 -0.04180 198 TRP A CA  
3050 C C   . TRP A 198 ? 0.64876 0.72774 0.88714 0.02304  -0.12671 -0.04549 198 TRP A C   
3051 O O   . TRP A 198 ? 0.64002 0.73214 0.91206 0.02171  -0.11510 -0.04943 198 TRP A O   
3052 C CB  . TRP A 198 ? 0.60392 0.67576 0.80248 0.02632  -0.11193 -0.03894 198 TRP A CB  
3053 C CG  . TRP A 198 ? 0.54559 0.60691 0.74440 0.02977  -0.13233 -0.03559 198 TRP A CG  
3054 C CD1 . TRP A 198 ? 0.53898 0.58361 0.70071 0.03087  -0.14175 -0.03055 198 TRP A CD1 
3055 C CD2 . TRP A 198 ? 0.62151 0.68680 0.86003 0.03246  -0.14614 -0.03661 198 TRP A CD2 
3056 N NE1 . TRP A 198 ? 0.59381 0.63041 0.76621 0.03397  -0.16165 -0.02768 198 TRP A NE1 
3057 C CE2 . TRP A 198 ? 0.58865 0.63844 0.80999 0.03528  -0.16562 -0.03131 198 TRP A CE2 
3058 C CE3 . TRP A 198 ? 0.65547 0.73514 0.94356 0.03258  -0.14353 -0.04151 198 TRP A CE3 
3059 C CZ2 . TRP A 198 ? 0.65561 0.70416 0.90845 0.03864  -0.18473 -0.03021 198 TRP A CZ2 
3060 C CZ3 . TRP A 198 ? 0.64874 0.72863 0.97192 0.03596  -0.16113 -0.04127 198 TRP A CZ3 
3061 C CH2 . TRP A 198 ? 0.65591 0.72048 0.96157 0.03915  -0.18261 -0.03538 198 TRP A CH2 
3072 N N   . GLN A 199 ? 0.68505 0.75381 0.92100 0.02417  -0.14987 -0.04441 199 GLN A N   
3073 C CA  . GLN A 199 ? 0.75425 0.82888 1.03088 0.02394  -0.16382 -0.04820 199 GLN A CA  
3074 C C   . GLN A 199 ? 0.77959 0.86102 1.06533 0.01960  -0.15626 -0.05298 199 GLN A C   
3075 O O   . GLN A 199 ? 0.66935 0.76366 0.99826 0.01849  -0.15132 -0.05739 199 GLN A O   
3076 C CB  . GLN A 199 ? 0.80636 0.86544 1.07140 0.02539  -0.19264 -0.04560 199 GLN A CB  
3077 C CG  . GLN A 199 ? 0.84490 0.89589 1.10563 0.02982  -0.20304 -0.04020 199 GLN A CG  
3078 C CD  . GLN A 199 ? 0.94208 0.97161 1.14588 0.02970  -0.21022 -0.03461 199 GLN A CD  
3079 O OE1 . GLN A 199 ? 0.81878 0.84374 0.98641 0.02709  -0.19652 -0.03456 199 GLN A OE1 
3080 N NE2 . GLN A 199 ? 0.84075 0.85604 1.03719 0.03239  -0.23136 -0.02973 199 GLN A NE2 
3089 N N   . GLU A 200 ? 0.74150 0.81398 0.98879 0.01696  -0.15400 -0.05234 200 GLU A N   
3090 C CA  . GLU A 200 ? 0.81256 0.88947 1.06752 0.01289  -0.14882 -0.05658 200 GLU A CA  
3091 C C   . GLU A 200 ? 0.77068 0.86202 1.04546 0.01103  -0.12429 -0.05838 200 GLU A C   
3092 O O   . GLU A 200 ? 0.78202 0.88073 1.08236 0.00803  -0.11989 -0.06235 200 GLU A O   
3093 C CB  . GLU A 200 ? 0.76279 0.82607 0.97195 0.01065  -0.14972 -0.05563 200 GLU A CB  
3094 C CG  . GLU A 200 ? 0.96050 1.00563 1.14427 0.01091  -0.17313 -0.05473 200 GLU A CG  
3095 C CD  . GLU A 200 ? 0.93644 0.96611 1.07010 0.00902  -0.16885 -0.05346 200 GLU A CD  
3096 O OE1 . GLU A 200 ? 0.91626 0.95061 1.04326 0.00688  -0.15209 -0.05485 200 GLU A OE1 
3097 O OE2 . GLU A 200 ? 1.03283 1.04465 1.13432 0.00952  -0.18187 -0.05102 200 GLU A OE2 
3104 N N   . VAL A 201 ? 0.67499 0.76897 0.93674 0.01224  -0.10822 -0.05552 201 VAL A N   
3105 C CA  . VAL A 201 ? 0.74639 0.85072 1.02074 0.00977  -0.08542 -0.05690 201 VAL A CA  
3106 C C   . VAL A 201 ? 0.67816 0.79374 0.99893 0.00988  -0.07944 -0.06055 201 VAL A C   
3107 O O   . VAL A 201 ? 0.72484 0.84724 1.05791 0.00691  -0.05999 -0.06244 201 VAL A O   
3108 C CB  . VAL A 201 ? 0.79477 0.89694 1.03851 0.01037  -0.07098 -0.05309 201 VAL A CB  
3109 C CG1 . VAL A 201 ? 0.79988 0.89245 1.00334 0.00951  -0.07226 -0.05029 201 VAL A CG1 
3110 C CG2 . VAL A 201 ? 0.69452 0.79470 0.93715 0.01436  -0.07576 -0.05095 201 VAL A CG2 
3120 N N   . GLY A 202 ? 0.63669 0.75310 0.98340 0.01300  -0.09528 -0.06155 202 GLY A N   
3121 C CA  . GLY A 202 ? 0.78809 0.91535 1.18595 0.01323  -0.09079 -0.06591 202 GLY A CA  
3122 C C   . GLY A 202 ? 0.76251 0.89161 1.17448 0.01721  -0.08999 -0.06504 202 GLY A C   
3123 O O   . GLY A 202 ? 0.79661 0.93445 1.25510 0.01773  -0.08612 -0.06920 202 GLY A O   
3127 N N   . PHE A 203 ? 0.70121 0.82233 1.07824 0.01996  -0.09269 -0.06022 203 PHE A N   
3128 C CA  . PHE A 203 ? 0.74820 0.87060 1.13927 0.02364  -0.09094 -0.05949 203 PHE A CA  
3129 C C   . PHE A 203 ? 0.67286 0.79353 1.09353 0.02776  -0.11503 -0.05893 203 PHE A C   
3130 O O   . PHE A 203 ? 0.69063 0.80260 1.09700 0.02851  -0.13709 -0.05633 203 PHE A O   
3131 C CB  . PHE A 203 ? 0.69756 0.81113 1.04284 0.02510  -0.08742 -0.05434 203 PHE A CB  
3132 C CG  . PHE A 203 ? 0.63475 0.75071 0.95785 0.02164  -0.06394 -0.05492 203 PHE A CG  
3133 C CD1 . PHE A 203 ? 0.64060 0.76353 0.98362 0.02021  -0.04433 -0.05865 203 PHE A CD1 
3134 C CD2 . PHE A 203 ? 0.65932 0.76931 0.94183 0.01957  -0.06170 -0.05193 203 PHE A CD2 
3135 C CE1 . PHE A 203 ? 0.67463 0.79735 0.99390 0.01650  -0.02470 -0.05885 203 PHE A CE1 
3136 C CE2 . PHE A 203 ? 0.65831 0.76974 0.92160 0.01646  -0.04266 -0.05186 203 PHE A CE2 
3137 C CZ  . PHE A 203 ? 0.62680 0.74401 0.90666 0.01479  -0.02506 -0.05505 203 PHE A CZ  
3147 N N   . LYS A 204 ? 0.66758 0.79529 1.12938 0.03024  -0.11099 -0.06148 204 LYS A N   
3148 C CA  . LYS A 204 ? 0.69572 0.82275 1.19362 0.03461  -0.13377 -0.06083 204 LYS A CA  
3149 C C   . LYS A 204 ? 0.75534 0.87330 1.23722 0.03944  -0.14293 -0.05522 204 LYS A C   
3150 O O   . LYS A 204 ? 0.66745 0.77633 1.14962 0.04280  -0.16908 -0.05085 204 LYS A O   
3151 C CB  . LYS A 204 ? 0.71540 0.85636 1.27843 0.03454  -0.12397 -0.06779 204 LYS A CB  
3152 C CG  . LYS A 204 ? 0.71387 0.86370 1.29947 0.02949  -0.11351 -0.07365 204 LYS A CG  
3153 C CD  . LYS A 204 ? 0.63429 0.79475 1.29042 0.03046  -0.11881 -0.07944 204 LYS A CD  
3154 C CE  . LYS A 204 ? 0.69902 0.86819 1.38049 0.02491  -0.10517 -0.08567 204 LYS A CE  
3155 N NZ  . LYS A 204 ? 0.85727 1.03852 1.61115 0.02493  -0.09767 -0.09292 204 LYS A NZ  
3169 N N   . GLU A 205 ? 0.73377 0.85271 1.20121 0.03955  -0.12261 -0.05514 205 GLU A N   
3170 C CA  . GLU A 205 ? 0.83992 0.95021 1.29260 0.04379  -0.12885 -0.05005 205 GLU A CA  
3171 C C   . GLU A 205 ? 0.74341 0.84095 1.13360 0.04280  -0.13017 -0.04409 205 GLU A C   
3172 O O   . GLU A 205 ? 0.60907 0.70848 0.97161 0.03888  -0.11406 -0.04542 205 GLU A O   
3173 C CB  . GLU A 205 ? 0.87061 0.98822 1.34440 0.04424  -0.10594 -0.05410 205 GLU A CB  
3174 C CG  . GLU A 205 ? 1.04037 1.16454 1.57396 0.04805  -0.10970 -0.05745 205 GLU A CG  
3175 C CD  . GLU A 205 ? 1.21149 1.32931 1.76373 0.05280  -0.14204 -0.05249 205 GLU A CD  
3176 O OE1 . GLU A 205 ? 1.08971 1.19556 1.62004 0.05652  -0.15617 -0.04562 205 GLU A OE1 
3177 O OE2 . GLU A 205 ? 1.20956 1.33331 1.79788 0.05249  -0.15396 -0.05531 205 GLU A OE2 
3184 N N   . PRO A 206 ? 0.63676 0.72038 1.00436 0.04608  -0.14861 -0.03740 206 PRO A N   
3185 C CA  . PRO A 206 ? 0.64228 0.71274 0.95243 0.04483  -0.14792 -0.03218 206 PRO A CA  
3186 C C   . PRO A 206 ? 0.62726 0.69993 0.92157 0.04444  -0.12612 -0.03234 206 PRO A C   
3187 O O   . PRO A 206 ? 0.52405 0.60462 0.84824 0.04596  -0.11539 -0.03536 206 PRO A O   
3188 C CB  . PRO A 206 ? 0.60823 0.66158 0.90431 0.04827  -0.17378 -0.02512 206 PRO A CB  
3189 C CG  . PRO A 206 ? 0.65442 0.71348 1.00040 0.05256  -0.18189 -0.02579 206 PRO A CG  
3190 C CD  . PRO A 206 ? 0.70536 0.78316 1.09943 0.05093  -0.17130 -0.03398 206 PRO A CD  
3198 N N   . PRO A 207 ? 0.54839 0.61389 0.79749 0.04218  -0.11880 -0.02969 207 PRO A N   
3199 C CA  . PRO A 207 ? 0.48609 0.55248 0.71968 0.04172  -0.10081 -0.02959 207 PRO A CA  
3200 C C   . PRO A 207 ? 0.51454 0.56927 0.73864 0.04540  -0.10928 -0.02414 207 PRO A C   
3201 O O   . PRO A 207 ? 0.53220 0.57291 0.73852 0.04709  -0.12746 -0.01851 207 PRO A O   
3202 C CB  . PRO A 207 ? 0.51717 0.57989 0.70983 0.03802  -0.09273 -0.02858 207 PRO A CB  
3203 C CG  . PRO A 207 ? 0.52343 0.57543 0.69806 0.03786  -0.11080 -0.02556 207 PRO A CG  
3204 C CD  . PRO A 207 ? 0.55880 0.61477 0.77084 0.03969  -0.12635 -0.02732 207 PRO A CD  
3212 N N   . LEU A 208 ? 0.50274 0.56190 0.73741 0.04621  -0.09530 -0.02595 208 LEU A N   
3213 C CA  . LEU A 208 ? 0.50860 0.55779 0.74012 0.04974  -0.10112 -0.02132 208 LEU A CA  
3214 C C   . LEU A 208 ? 0.49254 0.53586 0.68967 0.04808  -0.08841 -0.01939 208 LEU A C   
3215 O O   . LEU A 208 ? 0.54769 0.58144 0.73874 0.05054  -0.09181 -0.01524 208 LEU A O   
3216 C CB  . LEU A 208 ? 0.50844 0.56597 0.78573 0.05258  -0.09690 -0.02522 208 LEU A CB  
3217 C CG  . LEU A 208 ? 0.61804 0.68264 0.94005 0.05470  -0.10876 -0.02776 208 LEU A CG  
3218 C CD1 . LEU A 208 ? 0.52617 0.59883 0.89412 0.05720  -0.09993 -0.03256 208 LEU A CD1 
3219 C CD2 . LEU A 208 ? 0.66761 0.71924 0.98418 0.05783  -0.13696 -0.02056 208 LEU A CD2 
3231 N N   . THR A 209 ? 0.47878 0.52730 0.65575 0.04401  -0.07441 -0.02216 209 THR A N   
3232 C CA  . THR A 209 ? 0.49693 0.54167 0.64826 0.04234  -0.06230 -0.02119 209 THR A CA  
3233 C C   . THR A 209 ? 0.53447 0.56263 0.65157 0.04301  -0.07186 -0.01416 209 THR A C   
3234 O O   . THR A 209 ? 0.58159 0.60127 0.68536 0.04325  -0.08520 -0.01084 209 THR A O   
3235 C CB  . THR A 209 ? 0.50213 0.55568 0.64156 0.03783  -0.04713 -0.02536 209 THR A CB  
3236 O OG1 . THR A 209 ? 0.49318 0.54425 0.61497 0.03633  -0.03607 -0.02519 209 THR A OG1 
3237 C CG2 . THR A 209 ? 0.48088 0.53132 0.59822 0.03595  -0.05263 -0.02340 209 THR A CG2 
3245 N N   . VAL A 210 ? 0.55446 0.57672 0.65666 0.04282  -0.06413 -0.01227 210 VAL A N   
3246 C CA  . VAL A 210 ? 0.57519 0.58014 0.64493 0.04289  -0.06956 -0.00580 210 VAL A CA  
3247 C C   . VAL A 210 ? 0.56921 0.57306 0.61075 0.03905  -0.05883 -0.00637 210 VAL A C   
3248 O O   . VAL A 210 ? 0.60423 0.59359 0.61852 0.03831  -0.05931 -0.00191 210 VAL A O   
3249 C CB  . VAL A 210 ? 0.66232 0.65914 0.73504 0.04519  -0.06851 -0.00263 210 VAL A CB  
3250 C CG1 . VAL A 210 ? 0.61310 0.60833 0.71438 0.04961  -0.08203 -0.00087 210 VAL A CG1 
3251 C CG2 . VAL A 210 ? 0.66839 0.67589 0.75058 0.04341  -0.05085 -0.00789 210 VAL A CG2 
3261 N N   . PHE A 211 ? 0.53850 0.55623 0.58646 0.03644  -0.04897 -0.01159 211 PHE A N   
3262 C CA  . PHE A 211 ? 0.58358 0.60192 0.61063 0.03305  -0.03903 -0.01237 211 PHE A CA  
3263 C C   . PHE A 211 ? 0.57274 0.59178 0.59116 0.03155  -0.04350 -0.01297 211 PHE A C   
3264 O O   . PHE A 211 ? 0.56971 0.59966 0.60581 0.03118  -0.04429 -0.01639 211 PHE A O   
3265 C CB  . PHE A 211 ? 0.54437 0.57564 0.58265 0.03088  -0.02558 -0.01719 211 PHE A CB  
3266 C CG  . PHE A 211 ? 0.55905 0.58986 0.60721 0.03189  -0.02062 -0.01792 211 PHE A CG  
3267 C CD1 . PHE A 211 ? 0.63151 0.65235 0.66451 0.03180  -0.01786 -0.01475 211 PHE A CD1 
3268 C CD2 . PHE A 211 ? 0.53613 0.57536 0.60925 0.03264  -0.01759 -0.02214 211 PHE A CD2 
3269 C CE1 . PHE A 211 ? 0.69038 0.71022 0.73321 0.03258  -0.01335 -0.01563 211 PHE A CE1 
3270 C CE2 . PHE A 211 ? 0.56913 0.60703 0.65188 0.03342  -0.01240 -0.02355 211 PHE A CE2 
3271 C CZ  . PHE A 211 ? 0.62399 0.65240 0.69154 0.03346  -0.01086 -0.02019 211 PHE A CZ  
3281 N N   . LYS A 212 ? 0.55080 0.55734 0.54253 0.03036  -0.04509 -0.01005 212 LYS A N   
3282 C CA  . LYS A 212 ? 0.64954 0.65353 0.63019 0.02879  -0.04955 -0.01078 212 LYS A CA  
3283 C C   . LYS A 212 ? 0.58686 0.59944 0.56444 0.02593  -0.03764 -0.01373 212 LYS A C   
3284 O O   . LYS A 212 ? 0.54963 0.56250 0.52100 0.02474  -0.02750 -0.01359 212 LYS A O   
3285 C CB  . LYS A 212 ? 0.70089 0.68379 0.65162 0.02842  -0.05693 -0.00666 212 LYS A CB  
3286 C CG  . LYS A 212 ? 0.87884 0.84877 0.82665 0.03109  -0.06903 -0.00192 212 LYS A CG  
3287 C CD  . LYS A 212 ? 1.07253 1.03909 1.02745 0.03253  -0.08718 -0.00135 212 LYS A CD  
3288 C CE  . LYS A 212 ? 1.04282 1.02807 1.03833 0.03498  -0.09000 -0.00457 212 LYS A CE  
3289 N NZ  . LYS A 212 ? 0.89208 0.88004 0.90064 0.03519  -0.10379 -0.00641 212 LYS A NZ  
3303 N N   . GLY A 213 ? 0.57315 0.59249 0.55696 0.02480  -0.03962 -0.01628 213 GLY A N   
3304 C CA  . GLY A 213 ? 0.56146 0.58876 0.54485 0.02234  -0.03000 -0.01850 213 GLY A CA  
3305 C C   . GLY A 213 ? 0.50566 0.52227 0.46661 0.02068  -0.02665 -0.01767 213 GLY A C   
3306 O O   . GLY A 213 ? 0.53497 0.53663 0.47716 0.02076  -0.03179 -0.01594 213 GLY A O   
3310 N N   . GLY A 214 ? 0.54457 0.56794 0.50759 0.01888  -0.01756 -0.01905 214 GLY A N   
3311 C CA  . GLY A 214 ? 0.55424 0.56953 0.50224 0.01722  -0.01274 -0.01936 214 GLY A CA  
3312 C C   . GLY A 214 ? 0.57256 0.58606 0.51672 0.01630  -0.00230 -0.01872 214 GLY A C   
3313 O O   . GLY A 214 ? 0.52897 0.54275 0.47549 0.01697  0.00008  -0.01741 214 GLY A O   
3317 N N   . GLU A 215 ? 0.61103 0.62258 0.55171 0.01470  0.00408  -0.01998 215 GLU A N   
3318 C CA  . GLU A 215 ? 0.57166 0.58206 0.51358 0.01368  0.01423  -0.01992 215 GLU A CA  
3319 C C   . GLU A 215 ? 0.55676 0.55160 0.48171 0.01341  0.01846  -0.01850 215 GLU A C   
3320 O O   . GLU A 215 ? 0.55691 0.55241 0.48683 0.01308  0.02501  -0.01780 215 GLU A O   
3321 C CB  . GLU A 215 ? 0.52517 0.53541 0.46947 0.01227  0.01987  -0.02186 215 GLU A CB  
3322 C CG  . GLU A 215 ? 0.52695 0.53311 0.47381 0.01109  0.03102  -0.02244 215 GLU A CG  
3323 C CD  . GLU A 215 ? 0.53709 0.54291 0.48999 0.01003  0.03660  -0.02470 215 GLU A CD  
3324 O OE1 . GLU A 215 ? 0.59360 0.59631 0.53990 0.00981  0.03305  -0.02609 215 GLU A OE1 
3325 O OE2 . GLU A 215 ? 0.55493 0.56366 0.52146 0.00942  0.04417  -0.02530 215 GLU A OE2 
3332 N N   . THR A 216 ? 0.58921 0.56861 0.49310 0.01314  0.01451  -0.01796 216 THR A N   
3333 C CA  . THR A 216 ? 0.60567 0.56627 0.48814 0.01221  0.01895  -0.01598 216 THR A CA  
3334 C C   . THR A 216 ? 0.63249 0.59473 0.51959 0.01394  0.01571  -0.01286 216 THR A C   
3335 O O   . THR A 216 ? 0.56441 0.51971 0.44749 0.01311  0.02404  -0.01151 216 THR A O   
3336 C CB  . THR A 216 ? 0.67414 0.61574 0.52940 0.01117  0.01247  -0.01565 216 THR A CB  
3337 O OG1 . THR A 216 ? 0.73293 0.67338 0.58534 0.00942  0.01570  -0.01941 216 THR A OG1 
3338 C CG2 . THR A 216 ? 0.78642 0.70438 0.61385 0.00922  0.01891  -0.01331 216 THR A CG2 
3346 N N   . GLU A 217 ? 0.56862 0.53947 0.46590 0.01625  0.00425  -0.01197 217 GLU A N   
3347 C CA  . GLU A 217 ? 0.62561 0.59845 0.53041 0.01808  0.00155  -0.00962 217 GLU A CA  
3348 C C   . GLU A 217 ? 0.59595 0.58272 0.52006 0.01768  0.00992  -0.01125 217 GLU A C   
3349 O O   . GLU A 217 ? 0.58884 0.57261 0.51456 0.01790  0.01350  -0.00982 217 GLU A O   
3350 C CB  . GLU A 217 ? 0.66384 0.64345 0.57991 0.02057  -0.01132 -0.00926 217 GLU A CB  
3351 C CG  . GLU A 217 ? 0.83069 0.79372 0.72830 0.02134  -0.02315 -0.00644 217 GLU A CG  
3352 C CD  . GLU A 217 ? 0.88559 0.83447 0.77258 0.02259  -0.02636 -0.00177 217 GLU A CD  
3353 O OE1 . GLU A 217 ? 0.81148 0.76585 0.70973 0.02324  -0.01958 -0.00130 217 GLU A OE1 
3354 O OE2 . GLU A 217 ? 0.99691 0.92795 0.86338 0.02271  -0.03638 0.00156  217 GLU A OE2 
3361 N N   . ALA A 218 ? 0.52006 0.52096 0.45831 0.01685  0.01216  -0.01409 218 ALA A N   
3362 C CA  . ALA A 218 ? 0.51797 0.53063 0.47248 0.01594  0.01782  -0.01562 218 ALA A CA  
3363 C C   . ALA A 218 ? 0.51632 0.52177 0.46773 0.01439  0.02753  -0.01525 218 ALA A C   
3364 O O   . ALA A 218 ? 0.53589 0.54355 0.49506 0.01408  0.03059  -0.01527 218 ALA A O   
3365 C CB  . ALA A 218 ? 0.47000 0.49510 0.43577 0.01491  0.01756  -0.01773 218 ALA A CB  
3371 N N   . LEU A 219 ? 0.53910 0.53545 0.48053 0.01308  0.03347  -0.01549 219 LEU A N   
3372 C CA  . LEU A 219 ? 0.54269 0.53131 0.48354 0.01121  0.04495  -0.01570 219 LEU A CA  
3373 C C   . LEU A 219 ? 0.55650 0.53031 0.48291 0.01121  0.04747  -0.01288 219 LEU A C   
3374 O O   . LEU A 219 ? 0.59078 0.56261 0.52390 0.00996  0.05553  -0.01287 219 LEU A O   
3375 C CB  . LEU A 219 ? 0.56175 0.54206 0.49488 0.00958  0.05244  -0.01730 219 LEU A CB  
3376 C CG  . LEU A 219 ? 0.56024 0.55423 0.50979 0.00962  0.05053  -0.01962 219 LEU A CG  
3377 C CD1 . LEU A 219 ? 0.56951 0.55348 0.50841 0.00845  0.05600  -0.02148 219 LEU A CD1 
3378 C CD2 . LEU A 219 ? 0.61905 0.62483 0.59319 0.00880  0.05468  -0.02079 219 LEU A CD2 
3390 N N   . ALA A 220 ? 0.55917 0.52168 0.46654 0.01247  0.03997  -0.01022 220 ALA A N   
3391 C CA  . ALA A 220 ? 0.60885 0.55607 0.50201 0.01270  0.04034  -0.00644 220 ALA A CA  
3392 C C   . ALA A 220 ? 0.61548 0.57355 0.52737 0.01417  0.03809  -0.00617 220 ALA A C   
3393 O O   . ALA A 220 ? 0.61018 0.56071 0.52127 0.01333  0.04459  -0.00461 220 ALA A O   
3394 C CB  . ALA A 220 ? 0.67116 0.60446 0.54214 0.01401  0.02905  -0.00317 220 ALA A CB  
3400 N N   . ARG A 221 ? 0.62548 0.60012 0.55405 0.01597  0.02997  -0.00807 221 ARG A N   
3401 C CA  A ARG A 221 ? 0.61862 0.60261 0.56397 0.01688  0.02875  -0.00897 221 ARG A CA  
3402 C CA  B ARG A 221 ? 0.61940 0.60321 0.56460 0.01688  0.02878  -0.00893 221 ARG A CA  
3403 C C   . ARG A 221 ? 0.59566 0.58726 0.55505 0.01451  0.03761  -0.01176 221 ARG A C   
3404 O O   . ARG A 221 ? 0.58919 0.57991 0.55562 0.01412  0.04072  -0.01188 221 ARG A O   
3405 C CB  A ARG A 221 ? 0.62942 0.62759 0.58783 0.01854  0.02030  -0.01116 221 ARG A CB  
3406 C CB  B ARG A 221 ? 0.62670 0.62447 0.58495 0.01860  0.02021  -0.01105 221 ARG A CB  
3407 C CG  A ARG A 221 ? 0.64100 0.64691 0.61500 0.01918  0.01980  -0.01300 221 ARG A CG  
3408 C CG  B ARG A 221 ? 0.67924 0.67363 0.64035 0.02135  0.01290  -0.00921 221 ARG A CG  
3409 C CD  A ARG A 221 ? 0.63763 0.65235 0.62176 0.02096  0.01250  -0.01468 221 ARG A CD  
3410 C CD  B ARG A 221 ? 0.64979 0.65929 0.63075 0.02201  0.01042  -0.01304 221 ARG A CD  
3411 N NE  A ARG A 221 ? 0.67593 0.68147 0.65603 0.02395  0.00454  -0.01134 221 ARG A NE  
3412 N NE  B ARG A 221 ? 0.64731 0.65499 0.63775 0.02354  0.00998  -0.01296 221 ARG A NE  
3413 C CZ  A ARG A 221 ? 0.68517 0.68414 0.66889 0.02575  0.00298  -0.00944 221 ARG A CZ  
3414 C CZ  B ARG A 221 ? 0.69158 0.69110 0.68207 0.02653  0.00279  -0.00976 221 ARG A CZ  
3415 N NH1 A ARG A 221 ? 0.66200 0.66259 0.65312 0.02471  0.00988  -0.01111 221 ARG A NH1 
3416 N NH1 B ARG A 221 ? 0.69975 0.69148 0.67947 0.02807  -0.00582 -0.00636 221 ARG A NH1 
3417 N NH2 A ARG A 221 ? 0.71617 0.70623 0.69705 0.02862  -0.00670 -0.00576 221 ARG A NH2 
3418 N NH2 B ARG A 221 ? 0.69763 0.69600 0.69984 0.02794  0.00339  -0.01006 221 ARG A NH2 
3445 N N   . LEU A 222 ? 0.60076 0.59973 0.56623 0.01287  0.04089  -0.01409 222 LEU A N   
3446 C CA  . LEU A 222 ? 0.59879 0.60462 0.58006 0.01057  0.04729  -0.01657 222 LEU A CA  
3447 C C   . LEU A 222 ? 0.62109 0.61411 0.59873 0.00904  0.05762  -0.01531 222 LEU A C   
3448 O O   . LEU A 222 ? 0.61358 0.60916 0.60400 0.00769  0.06130  -0.01662 222 LEU A O   
3449 C CB  . LEU A 222 ? 0.57120 0.58522 0.56039 0.00949  0.04785  -0.01844 222 LEU A CB  
3450 C CG  . LEU A 222 ? 0.57147 0.59200 0.57990 0.00716  0.05283  -0.02071 222 LEU A CG  
3451 C CD1 . LEU A 222 ? 0.60656 0.63985 0.62802 0.00634  0.04559  -0.02278 222 LEU A CD1 
3452 C CD2 . LEU A 222 ? 0.78682 0.80901 0.80098 0.00653  0.05604  -0.02147 222 LEU A CD2 
3464 N N   . GLU A 223 ? 0.61740 0.59501 0.57645 0.00873  0.06292  -0.01302 223 GLU A N   
3465 C CA  . GLU A 223 ? 0.75757 0.71982 0.70992 0.00662  0.07492  -0.01161 223 GLU A CA  
3466 C C   . GLU A 223 ? 0.79152 0.74651 0.73977 0.00740  0.07338  -0.00878 223 GLU A C   
3467 O O   . GLU A 223 ? 0.74690 0.69673 0.70202 0.00545  0.08244  -0.00882 223 GLU A O   
3468 C CB  . GLU A 223 ? 0.83785 0.78151 0.76478 0.00557  0.08082  -0.00978 223 GLU A CB  
3469 C CG  . GLU A 223 ? 1.12789 1.06083 1.05583 0.00205  0.09810  -0.01132 223 GLU A CG  
3470 C CD  . GLU A 223 ? 0.98490 0.93521 0.94499 0.00102  0.10256  -0.01592 223 GLU A CD  
3471 O OE1 . GLU A 223 ? 0.95856 0.92010 0.92657 0.00199  0.09722  -0.01798 223 GLU A OE1 
3472 O OE2 . GLU A 223 ? 0.93413 0.88646 0.91277 -0.00084 0.11061  -0.01728 223 GLU A OE2 
3479 N N   . ALA A 224 ? 0.74497 0.69958 0.68489 0.01026  0.06207  -0.00645 224 ALA A N   
3480 C CA  . ALA A 224 ? 0.80155 0.74943 0.74040 0.01151  0.05970  -0.00367 224 ALA A CA  
3481 C C   . ALA A 224 ? 0.72145 0.68357 0.68514 0.01088  0.06092  -0.00752 224 ALA A C   
3482 O O   . ALA A 224 ? 0.73392 0.68920 0.70112 0.01011  0.06579  -0.00649 224 ALA A O   
3483 C CB  . ALA A 224 ? 0.75058 0.69650 0.68082 0.01499  0.04647  -0.00087 224 ALA A CB  
3489 N N   . ALA A 225 ? 0.60745 0.58772 0.58673 0.01081  0.05631  -0.01194 225 ALA A N   
3490 C CA  . ALA A 225 ? 0.60904 0.60081 0.60804 0.00941  0.05649  -0.01614 225 ALA A CA  
3491 C C   . ALA A 225 ? 0.65793 0.64848 0.66832 0.00612  0.06602  -0.01786 225 ALA A C   
3492 O O   . ALA A 225 ? 0.67612 0.66854 0.69896 0.00466  0.06798  -0.02010 225 ALA A O   
3493 C CB  . ALA A 225 ? 0.57281 0.58088 0.58099 0.00923  0.04958  -0.02001 225 ALA A CB  
3499 N N   . PHE A 226 ? 0.65653 0.64386 0.66503 0.00475  0.07242  -0.01741 226 PHE A N   
3500 C CA  . PHE A 226 ? 0.67707 0.66354 0.70081 0.00159  0.08246  -0.01939 226 PHE A CA  
3501 C C   . PHE A 226 ? 0.67519 0.64256 0.68798 0.00036  0.09449  -0.01609 226 PHE A C   
3502 O O   . PHE A 226 ? 0.67397 0.63835 0.69947 -0.00257 0.10558  -0.01768 226 PHE A O   
3503 C CB  . PHE A 226 ? 0.60596 0.59920 0.63826 0.00061  0.08441  -0.02128 226 PHE A CB  
3504 C CG  . PHE A 226 ? 0.67408 0.68524 0.72366 0.00031  0.07438  -0.02473 226 PHE A CG  
3505 C CD1 . PHE A 226 ? 0.68571 0.70416 0.72646 0.00230  0.06380  -0.02446 226 PHE A CD1 
3506 C CD2 . PHE A 226 ? 0.61137 0.63083 0.68586 -0.00232 0.07508  -0.02810 226 PHE A CD2 
3507 C CE1 . PHE A 226 ? 0.63891 0.67070 0.69110 0.00139  0.05513  -0.02707 226 PHE A CE1 
3508 C CE2 . PHE A 226 ? 0.59242 0.62552 0.67884 -0.00302 0.06405  -0.03056 226 PHE A CE2 
3509 C CZ  . PHE A 226 ? 0.58253 0.62088 0.65565 -0.00131 0.05451  -0.02985 226 PHE A CZ  
3519 N N   . GLN A 227 ? 0.74755 0.70106 0.73770 0.00234  0.09234  -0.01136 227 GLN A N   
3520 C CA  . GLN A 227 ? 0.77949 0.71171 0.75495 0.00084  0.10295  -0.00720 227 GLN A CA  
3521 C C   . GLN A 227 ? 0.71972 0.65242 0.71383 -0.00119 0.10900  -0.00874 227 GLN A C   
3522 O O   . GLN A 227 ? 0.71041 0.62828 0.70137 -0.00394 0.12210  -0.00695 227 GLN A O   
3523 C CB  . GLN A 227 ? 0.87578 0.79306 0.82414 0.00365  0.09539  -0.00115 227 GLN A CB  
3524 C CG  . GLN A 227 ? 1.19115 1.09656 1.11267 0.00402  0.09412  0.00165  227 GLN A CG  
3525 C CD  . GLN A 227 ? 1.34609 1.23955 1.24474 0.00714  0.08171  0.00729  227 GLN A CD  
3526 O OE1 . GLN A 227 ? 1.35057 1.24329 1.23549 0.00860  0.07332  0.00802  227 GLN A OE1 
3527 N NE2 . GLN A 227 ? 1.20935 1.09320 1.10579 0.00816  0.07979  0.01130  227 GLN A NE2 
3536 N N   . ASP A 228 ? 0.67718 0.62525 0.68978 -0.00032 0.10046  -0.01234 228 ASP A N   
3537 C CA  . ASP A 228 ? 0.71461 0.66456 0.74670 -0.00253 0.10466  -0.01504 228 ASP A CA  
3538 C C   . ASP A 228 ? 0.62507 0.59465 0.68355 -0.00458 0.10069  -0.02190 228 ASP A C   
3539 O O   . ASP A 228 ? 0.61430 0.59619 0.67797 -0.00355 0.08991  -0.02506 228 ASP A O   
3540 C CB  . ASP A 228 ? 0.73512 0.68217 0.76358 -0.00015 0.09778  -0.01355 228 ASP A CB  
3541 C CG  . ASP A 228 ? 0.74401 0.69042 0.79110 -0.00271 0.10309  -0.01641 228 ASP A CG  
3542 O OD1 . ASP A 228 ? 0.69919 0.64834 0.76313 -0.00644 0.11121  -0.01963 228 ASP A OD1 
3543 O OD2 . ASP A 228 ? 0.78370 0.72709 0.83111 -0.00107 0.09912  -0.01586 228 ASP A OD2 
3548 N N   . PRO A 229 ? 0.60661 0.57828 0.68240 -0.00779 0.10914  -0.02438 229 PRO A N   
3549 C CA  . PRO A 229 ? 0.58548 0.57491 0.68705 -0.00977 0.10252  -0.03030 229 PRO A CA  
3550 C C   . PRO A 229 ? 0.57864 0.57462 0.69397 -0.01136 0.09613  -0.03458 229 PRO A C   
3551 O O   . PRO A 229 ? 0.58267 0.59202 0.70880 -0.01243 0.08547  -0.03897 229 PRO A O   
3552 C CB  . PRO A 229 ? 0.62812 0.61542 0.74942 -0.01291 0.11471  -0.03171 229 PRO A CB  
3553 C CG  . PRO A 229 ? 0.63998 0.60852 0.73965 -0.01248 0.12827  -0.02670 229 PRO A CG  
3554 C CD  . PRO A 229 ? 0.67866 0.63553 0.75282 -0.01015 0.12525  -0.02212 229 PRO A CD  
3562 N N   . LYS A 230 ? 0.55674 0.54212 0.67072 -0.01194 0.10233  -0.03347 230 LYS A N   
3563 C CA  . LYS A 230 ? 0.56887 0.55890 0.69542 -0.01370 0.09723  -0.03823 230 LYS A CA  
3564 C C   . LYS A 230 ? 0.54137 0.53686 0.65477 -0.01114 0.08602  -0.03941 230 LYS A C   
3565 O O   . LYS A 230 ? 0.53358 0.53739 0.65573 -0.01315 0.07862  -0.04525 230 LYS A O   
3566 C CB  . LYS A 230 ? 0.55960 0.53540 0.68818 -0.01477 0.10771  -0.03628 230 LYS A CB  
3567 C CG  . LYS A 230 ? 0.57872 0.54851 0.72420 -0.01838 0.12104  -0.03629 230 LYS A CG  
3568 C CD  . LYS A 230 ? 0.57105 0.54345 0.74268 -0.02244 0.12259  -0.04188 230 LYS A CD  
3569 C CE  . LYS A 230 ? 0.56573 0.55588 0.75994 -0.02508 0.11102  -0.04924 230 LYS A CE  
3570 N NZ  . LYS A 230 ? 0.61056 0.60261 0.83691 -0.03005 0.11546  -0.05433 230 LYS A NZ  
3584 N N   . TRP A 231 ? 0.58718 0.57690 0.67956 -0.00708 0.08492  -0.03429 231 TRP A N   
3585 C CA  . TRP A 231 ? 0.61024 0.60610 0.69374 -0.00469 0.07544  -0.03577 231 TRP A CA  
3586 C C   . TRP A 231 ? 0.56588 0.57551 0.65152 -0.00582 0.06728  -0.03930 231 TRP A C   
3587 O O   . TRP A 231 ? 0.56597 0.58253 0.65271 -0.00696 0.06060  -0.04406 231 TRP A O   
3588 C CB  . TRP A 231 ? 0.59022 0.57713 0.65431 -0.00015 0.07480  -0.02937 231 TRP A CB  
3589 C CG  . TRP A 231 ? 0.63979 0.63353 0.69916 0.00232  0.06628  -0.03117 231 TRP A CG  
3590 C CD1 . TRP A 231 ? 0.62945 0.62187 0.69275 0.00345  0.06457  -0.03343 231 TRP A CD1 
3591 C CD2 . TRP A 231 ? 0.58475 0.58721 0.63695 0.00365  0.05981  -0.03136 231 TRP A CD2 
3592 N NE1 . TRP A 231 ? 0.61220 0.61197 0.67187 0.00528  0.05834  -0.03526 231 TRP A NE1 
3593 C CE2 . TRP A 231 ? 0.61943 0.62534 0.67172 0.00534  0.05517  -0.03380 231 TRP A CE2 
3594 C CE3 . TRP A 231 ? 0.66017 0.66732 0.70724 0.00347  0.05833  -0.02989 231 TRP A CE3 
3595 C CZ2 . TRP A 231 ? 0.57873 0.59240 0.62581 0.00660  0.04954  -0.03464 231 TRP A CZ2 
3596 C CZ3 . TRP A 231 ? 0.62344 0.63832 0.66454 0.00490  0.05169  -0.03043 231 TRP A CZ3 
3597 C CH2 . TRP A 231 ? 0.61149 0.62951 0.65248 0.00628  0.04758  -0.03273 231 TRP A CH2 
3608 N N   . VAL A 232 ? 0.49310 0.50524 0.57849 -0.00582 0.06833  -0.03706 232 VAL A N   
3609 C CA  . VAL A 232 ? 0.54412 0.56806 0.63234 -0.00682 0.06020  -0.03943 232 VAL A CA  
3610 C C   . VAL A 232 ? 0.52357 0.55471 0.62913 -0.01115 0.05516  -0.04521 232 VAL A C   
3611 O O   . VAL A 232 ? 0.52789 0.56587 0.63049 -0.01268 0.04586  -0.04852 232 VAL A O   
3612 C CB  . VAL A 232 ? 0.55319 0.57704 0.64084 -0.00591 0.06362  -0.03601 232 VAL A CB  
3613 C CG1 . VAL A 232 ? 0.56943 0.60496 0.66404 -0.00714 0.05486  -0.03808 232 VAL A CG1 
3614 C CG2 . VAL A 232 ? 0.60185 0.61783 0.66850 -0.00215 0.06587  -0.03091 232 VAL A CG2 
3624 N N   . ALA A 233 ? 0.51004 0.53841 0.63336 -0.01366 0.06105  -0.04658 233 ALA A N   
3625 C CA  . ALA A 233 ? 0.48898 0.52385 0.63171 -0.01813 0.05465  -0.05225 233 ALA A CA  
3626 C C   . ALA A 233 ? 0.50142 0.53588 0.63881 -0.02021 0.04893  -0.05741 233 ALA A C   
3627 O O   . ALA A 233 ? 0.55519 0.59511 0.69490 -0.02359 0.03847  -0.06199 233 ALA A O   
3628 C CB  . ALA A 233 ? 0.53212 0.56350 0.69784 -0.02040 0.06372  -0.05283 233 ALA A CB  
3634 N N   . GLY A 234 ? 0.50423 0.53076 0.63388 -0.01850 0.05552  -0.05683 234 GLY A N   
3635 C CA  . GLY A 234 ? 0.46060 0.48517 0.58762 -0.02048 0.05285  -0.06243 234 GLY A CA  
3636 C C   . GLY A 234 ? 0.53727 0.56302 0.64563 -0.01875 0.04869  -0.06347 234 GLY A C   
3637 O O   . GLY A 234 ? 0.58253 0.60539 0.68791 -0.02039 0.04843  -0.06875 234 GLY A O   
3641 N N   . PHE A 235 ? 0.52318 0.55262 0.62017 -0.01577 0.04642  -0.05913 235 PHE A N   
3642 C CA  . PHE A 235 ? 0.49967 0.53010 0.58136 -0.01394 0.04414  -0.05972 235 PHE A CA  
3643 C C   . PHE A 235 ? 0.51427 0.54625 0.59058 -0.01860 0.03855  -0.06709 235 PHE A C   
3644 O O   . PHE A 235 ? 0.54631 0.58179 0.62352 -0.02262 0.03104  -0.06942 235 PHE A O   
3645 C CB  . PHE A 235 ? 0.56113 0.59631 0.63432 -0.01122 0.04128  -0.05452 235 PHE A CB  
3646 C CG  . PHE A 235 ? 0.52444 0.56066 0.58481 -0.00889 0.04018  -0.05417 235 PHE A CG  
3647 C CD1 . PHE A 235 ? 0.55948 0.59923 0.61136 -0.01183 0.03534  -0.05818 235 PHE A CD1 
3648 C CD2 . PHE A 235 ? 0.59553 0.62816 0.65222 -0.00408 0.04368  -0.04960 235 PHE A CD2 
3649 C CE1 . PHE A 235 ? 0.56278 0.60331 0.60528 -0.01004 0.03618  -0.05820 235 PHE A CE1 
3650 C CE2 . PHE A 235 ? 0.57601 0.61048 0.62555 -0.00195 0.04236  -0.04957 235 PHE A CE2 
3651 C CZ  . PHE A 235 ? 0.54314 0.58203 0.58697 -0.00496 0.03966  -0.05413 235 PHE A CZ  
3661 N N   . GLN A 236 ? 0.46667 0.49468 0.53704 -0.01830 0.04210  -0.07084 236 GLN A N   
3662 C CA  . GLN A 236 ? 0.56556 0.59202 0.62550 -0.02298 0.03940  -0.07834 236 GLN A CA  
3663 C C   . GLN A 236 ? 0.56155 0.58708 0.61255 -0.02029 0.04414  -0.07874 236 GLN A C   
3664 O O   . GLN A 236 ? 0.53578 0.55736 0.59353 -0.01754 0.05087  -0.07977 236 GLN A O   
3665 C CB  . GLN A 236 ? 0.65918 0.67963 0.72553 -0.02714 0.04134  -0.08574 236 GLN A CB  
3666 C CG  . GLN A 236 ? 0.83223 0.85234 0.91634 -0.02750 0.04168  -0.08417 236 GLN A CG  
3667 C CD  . GLN A 236 ? 0.87765 0.89394 0.96687 -0.03392 0.03822  -0.09244 236 GLN A CD  
3668 O OE1 . GLN A 236 ? 0.82583 0.84036 0.90212 -0.03900 0.03175  -0.09839 236 GLN A OE1 
3669 N NE2 . GLN A 236 ? 1.00942 1.02296 1.11621 -0.03416 0.04236  -0.09283 236 GLN A NE2 
3678 N N   . LYS A 237 ? 0.57392 0.60261 0.61199 -0.02123 0.04067  -0.07802 237 LYS A N   
3679 C CA  . LYS A 237 ? 0.57701 0.60597 0.60988 -0.01860 0.04557  -0.07791 237 LYS A CA  
3680 C C   . LYS A 237 ? 0.52350 0.54635 0.55807 -0.01990 0.05369  -0.08531 237 LYS A C   
3681 O O   . LYS A 237 ? 0.55451 0.57757 0.59842 -0.01523 0.05902  -0.08386 237 LYS A O   
3682 C CB  . LYS A 237 ? 0.55209 0.58342 0.56923 -0.02134 0.04115  -0.07740 237 LYS A CB  
3683 C CG  . LYS A 237 ? 0.52444 0.55674 0.53785 -0.01918 0.04660  -0.07723 237 LYS A CG  
3684 C CD  . LYS A 237 ? 0.51917 0.55561 0.54620 -0.01201 0.04812  -0.07110 237 LYS A CD  
3685 C CE  . LYS A 237 ? 0.54405 0.58448 0.56815 -0.00993 0.04852  -0.06840 237 LYS A CE  
3686 N NZ  . LYS A 237 ? 0.54163 0.58519 0.55323 -0.01228 0.04254  -0.06532 237 LYS A NZ  
3700 N N   . PRO A 238 ? 0.59181 0.60838 0.61891 -0.02604 0.05476  -0.09349 238 PRO A N   
3701 C CA  . PRO A 238 ? 0.58515 0.59478 0.61417 -0.02750 0.06458  -0.10156 238 PRO A CA  
3702 C C   . PRO A 238 ? 0.56209 0.56977 0.61152 -0.02325 0.06971  -0.10137 238 PRO A C   
3703 O O   . PRO A 238 ? 0.57643 0.57918 0.63265 -0.02302 0.07849  -0.10724 238 PRO A O   
3704 C CB  . PRO A 238 ? 0.61922 0.62069 0.63157 -0.03604 0.06272  -0.11026 238 PRO A CB  
3705 C CG  . PRO A 238 ? 0.56235 0.56729 0.56303 -0.03869 0.05059  -0.10582 238 PRO A CG  
3706 C CD  . PRO A 238 ? 0.55643 0.57091 0.57326 -0.03224 0.04649  -0.09617 238 PRO A CD  
3714 N N   . ASP A 239 ? 0.56791 0.57799 0.62759 -0.02016 0.06544  -0.09501 239 ASP A N   
3715 C CA  . ASP A 239 ? 0.66888 0.67478 0.74567 -0.01654 0.06994  -0.09382 239 ASP A CA  
3716 C C   . ASP A 239 ? 0.62474 0.63255 0.71061 -0.00896 0.06980  -0.08473 239 ASP A C   
3717 O O   . ASP A 239 ? 0.64522 0.64801 0.74324 -0.00555 0.07198  -0.08158 239 ASP A O   
3718 C CB  . ASP A 239 ? 0.71445 0.71861 0.79643 -0.01893 0.06681  -0.09311 239 ASP A CB  
3719 C CG  . ASP A 239 ? 0.78136 0.78104 0.85835 -0.02636 0.06637  -0.10314 239 ASP A CG  
3720 O OD1 . ASP A 239 ? 0.86837 0.86264 0.94107 -0.02894 0.07208  -0.11128 239 ASP A OD1 
3721 O OD2 . ASP A 239 ? 1.04982 1.05066 1.12774 -0.02990 0.06034  -0.10330 239 ASP A OD2 
3726 N N   . THR A 240 ? 0.53463 0.54819 0.61395 -0.00656 0.06658  -0.08029 240 THR A N   
3727 C CA  . THR A 240 ? 0.57459 0.58891 0.65994 0.00006  0.06421  -0.07170 240 THR A CA  
3728 C C   . THR A 240 ? 0.48506 0.49812 0.58274 0.00357  0.06809  -0.07372 240 THR A C   
3729 O O   . THR A 240 ? 0.52570 0.53929 0.62463 0.00079  0.07379  -0.08159 240 THR A O   
3730 C CB  . THR A 240 ? 0.54440 0.56523 0.61854 0.00092  0.05827  -0.06609 240 THR A CB  
3731 O OG1 . THR A 240 ? 0.51629 0.54175 0.58270 -0.00207 0.05904  -0.07089 240 THR A OG1 
3732 C CG2 . THR A 240 ? 0.52767 0.54950 0.59543 -0.00163 0.05487  -0.06345 240 THR A CG2 
3740 N N   . ASP A 241 ? 0.56979 0.58001 0.67666 0.00957  0.06481  -0.06638 241 ASP A N   
3741 C CA  . ASP A 241 ? 0.57487 0.58257 0.70020 0.01373  0.06696  -0.06739 241 ASP A CA  
3742 C C   . ASP A 241 ? 0.49211 0.50630 0.62064 0.01628  0.06401  -0.06596 241 ASP A C   
3743 O O   . ASP A 241 ? 0.45079 0.46617 0.57354 0.01949  0.05593  -0.05798 241 ASP A O   
3744 C CB  . ASP A 241 ? 0.57043 0.56946 0.70382 0.01875  0.06278  -0.05938 241 ASP A CB  
3745 C CG  . ASP A 241 ? 0.53439 0.53009 0.69045 0.02364  0.06285  -0.05948 241 ASP A CG  
3746 O OD1 . ASP A 241 ? 0.50928 0.51048 0.67730 0.02338  0.06721  -0.06606 241 ASP A OD1 
3747 O OD2 . ASP A 241 ? 0.64605 0.63273 0.80867 0.02763  0.05872  -0.05277 241 ASP A OD2 
3752 N N   . PRO A 242 ? 0.48074 0.49811 0.61875 0.01466  0.07105  -0.07384 242 PRO A N   
3753 C CA  . PRO A 242 ? 0.48879 0.51257 0.63288 0.01676  0.06909  -0.07276 242 PRO A CA  
3754 C C   . PRO A 242 ? 0.49966 0.52224 0.66625 0.02374  0.06279  -0.06731 242 PRO A C   
3755 O O   . PRO A 242 ? 0.49593 0.52373 0.66737 0.02605  0.05761  -0.06439 242 PRO A O   
3756 C CB  . PRO A 242 ? 0.47031 0.49538 0.61770 0.01195  0.08130  -0.08372 242 PRO A CB  
3757 C CG  . PRO A 242 ? 0.46379 0.48156 0.61844 0.01015  0.08893  -0.09023 242 PRO A CG  
3758 C CD  . PRO A 242 ? 0.46167 0.47581 0.60430 0.01015  0.08225  -0.08471 242 PRO A CD  
3766 N N   . SER A 243 ? 0.47351 0.48884 0.65454 0.02701  0.06210  -0.06571 243 SER A N   
3767 C CA  . SER A 243 ? 0.51386 0.52617 0.71702 0.03377  0.05383  -0.05979 243 SER A CA  
3768 C C   . SER A 243 ? 0.50783 0.51402 0.69657 0.03734  0.04010  -0.04772 243 SER A C   
3769 O O   . SER A 243 ? 0.49659 0.49816 0.69893 0.04277  0.02999  -0.04135 243 SER A O   
3770 C CB  . SER A 243 ? 0.47727 0.48281 0.70403 0.03579  0.05923  -0.06335 243 SER A CB  
3771 O OG  . SER A 243 ? 0.49764 0.49414 0.71260 0.03529  0.05826  -0.05952 243 SER A OG  
3777 N N   . ALA A 244 ? 0.49282 0.49761 0.65452 0.03418  0.03951  -0.04462 244 ALA A N   
3778 C CA  . ALA A 244 ? 0.49962 0.49657 0.64386 0.03649  0.02931  -0.03410 244 ALA A CA  
3779 C C   . ALA A 244 ? 0.58144 0.58373 0.71980 0.03787  0.02094  -0.03079 244 ALA A C   
3780 O O   . ALA A 244 ? 0.52002 0.53105 0.64774 0.03439  0.02437  -0.03426 244 ALA A O   
3781 C CB  . ALA A 244 ? 0.61196 0.60594 0.73400 0.03230  0.03387  -0.03321 244 ALA A CB  
3787 N N   . TRP A 245 ? 0.55554 0.55162 0.70065 0.04277  0.00906  -0.02394 245 TRP A N   
3788 C CA  . TRP A 245 ? 0.56170 0.56110 0.70262 0.04424  -0.00078 -0.02065 245 TRP A CA  
3789 C C   . TRP A 245 ? 0.60656 0.59258 0.72349 0.04585  -0.01234 -0.01055 245 TRP A C   
3790 O O   . TRP A 245 ? 0.58635 0.57410 0.68636 0.04454  -0.01631 -0.00877 245 TRP A O   
3791 C CB  . TRP A 245 ? 0.50525 0.50944 0.67828 0.04820  -0.00649 -0.02259 245 TRP A CB  
3792 C CG  . TRP A 245 ? 0.59948 0.59240 0.78892 0.05328  -0.01553 -0.01704 245 TRP A CG  
3793 C CD1 . TRP A 245 ? 0.58651 0.57672 0.79616 0.05455  -0.00905 -0.02007 245 TRP A CD1 
3794 C CD2 . TRP A 245 ? 0.61088 0.59217 0.79677 0.05755  -0.03356 -0.00725 245 TRP A CD2 
3795 N NE1 . TRP A 245 ? 0.61400 0.59206 0.83487 0.05977  -0.02205 -0.01219 245 TRP A NE1 
3796 C CE2 . TRP A 245 ? 0.63286 0.60470 0.83812 0.06158  -0.03798 -0.00397 245 TRP A CE2 
3797 C CE3 . TRP A 245 ? 0.66389 0.64032 0.83065 0.05807  -0.04696 -0.00100 245 TRP A CE3 
3798 C CZ2 . TRP A 245 ? 0.73110 0.68835 0.93645 0.06615  -0.05657 0.00613  245 TRP A CZ2 
3799 C CZ3 . TRP A 245 ? 0.71384 0.67527 0.87874 0.06217  -0.06514 0.00831  245 TRP A CZ3 
3800 C CH2 . TRP A 245 ? 0.70258 0.65435 0.88620 0.06619  -0.07043 0.01220  245 TRP A CH2 
3811 N N   . GLU A 246 ? 0.65119 0.62214 0.76466 0.04833  -0.01741 -0.00389 246 GLU A N   
3812 C CA  . GLU A 246 ? 0.72631 0.68062 0.81140 0.04889  -0.02692 0.00577  246 GLU A CA  
3813 C C   . GLU A 246 ? 0.69390 0.64802 0.75103 0.04415  -0.01811 0.00523  246 GLU A C   
3814 O O   . GLU A 246 ? 0.72167 0.67108 0.75747 0.04324  -0.02340 0.00871  246 GLU A O   
3815 C CB  . GLU A 246 ? 0.79274 0.72900 0.87597 0.05132  -0.03084 0.01292  246 GLU A CB  
3816 C CG  . GLU A 246 ? 0.89547 0.83251 1.01251 0.05610  -0.03724 0.01259  246 GLU A CG  
3817 C CD  . GLU A 246 ? 0.97131 0.88850 1.08497 0.05860  -0.04226 0.02090  246 GLU A CD  
3818 O OE1 . GLU A 246 ? 1.07873 0.97846 1.15975 0.05699  -0.04455 0.02880  246 GLU A OE1 
3819 O OE2 . GLU A 246 ? 0.96861 0.88659 1.11230 0.06195  -0.04304 0.01945  246 GLU A OE2 
3826 N N   . LYS A 247 ? 0.67333 0.63233 0.73202 0.04094  -0.00480 0.00038  247 LYS A N   
3827 C CA  . LYS A 247 ? 0.69399 0.65722 0.73560 0.03637  0.00430  -0.00210 247 LYS A CA  
3828 C C   . LYS A 247 ? 0.63212 0.61221 0.69004 0.03364  0.01356  -0.01166 247 LYS A C   
3829 O O   . LYS A 247 ? 0.54586 0.52601 0.61283 0.03220  0.02096  -0.01521 247 LYS A O   
3830 C CB  . LYS A 247 ? 0.90286 0.85160 0.92769 0.03437  0.01046  0.00235  247 LYS A CB  
3831 C CG  . LYS A 247 ? 0.94874 0.90098 0.95893 0.02992  0.01915  0.00027  247 LYS A CG  
3832 C CD  . LYS A 247 ? 1.19610 1.12949 1.18013 0.02877  0.02054  0.00754  247 LYS A CD  
3833 C CE  . LYS A 247 ? 1.04673 0.97881 1.02828 0.02453  0.03383  0.00549  247 LYS A CE  
3834 N NZ  . LYS A 247 ? 1.15688 1.06819 1.11339 0.02286  0.03825  0.01220  247 LYS A NZ  
3848 N N   . PRO A 248 ? 0.58401 0.57686 0.64441 0.03246  0.01326  -0.01597 248 PRO A N   
3849 C CA  . PRO A 248 ? 0.55481 0.56052 0.62567 0.02916  0.02162  -0.02459 248 PRO A CA  
3850 C C   . PRO A 248 ? 0.55586 0.56079 0.61924 0.02509  0.02967  -0.02693 248 PRO A C   
3851 O O   . PRO A 248 ? 0.50459 0.50276 0.55401 0.02419  0.03021  -0.02251 248 PRO A O   
3852 C CB  . PRO A 248 ? 0.54149 0.55689 0.60736 0.02798  0.01938  -0.02613 248 PRO A CB  
3853 C CG  . PRO A 248 ? 0.63425 0.64445 0.69867 0.03187  0.00883  -0.02033 248 PRO A CG  
3854 C CD  . PRO A 248 ? 0.62705 0.62149 0.67928 0.03367  0.00512  -0.01314 248 PRO A CD  
3862 N N   . ALA A 249 ? 0.51081 0.52183 0.58423 0.02229  0.03621  -0.03439 249 ALA A N   
3863 C CA  . ALA A 249 ? 0.48055 0.49099 0.55069 0.01816  0.04234  -0.03764 249 ALA A CA  
3864 C C   . ALA A 249 ? 0.51463 0.53262 0.57445 0.01418  0.04288  -0.03963 249 ALA A C   
3865 O O   . ALA A 249 ? 0.51981 0.53769 0.57832 0.01066  0.04609  -0.04185 249 ALA A O   
3866 C CB  . ALA A 249 ? 0.47758 0.48929 0.56085 0.01625  0.04820  -0.04544 249 ALA A CB  
3872 N N   . THR A 250 ? 0.49601 0.52027 0.55065 0.01461  0.03928  -0.03888 250 THR A N   
3873 C CA  . THR A 250 ? 0.51929 0.54992 0.56489 0.01143  0.03851  -0.03958 250 THR A CA  
3874 C C   . THR A 250 ? 0.44356 0.47262 0.48021 0.01389  0.03426  -0.03333 250 THR A C   
3875 O O   . THR A 250 ? 0.47445 0.49637 0.50918 0.01744  0.03138  -0.02864 250 THR A O   
3876 C CB  . THR A 250 ? 0.51362 0.55189 0.55955 0.00860  0.03931  -0.04529 250 THR A CB  
3877 O OG1 . THR A 250 ? 0.48356 0.52349 0.53571 0.01142  0.03849  -0.04544 250 THR A OG1 
3878 C CG2 . THR A 250 ? 0.47916 0.51645 0.52857 0.00471  0.04401  -0.05225 250 THR A CG2 
3886 N N   . THR A 251 ? 0.51813 0.55275 0.54864 0.01176  0.03324  -0.03338 251 THR A N   
3887 C CA  . THR A 251 ? 0.48393 0.51585 0.50540 0.01328  0.03091  -0.02840 251 THR A CA  
3888 C C   . THR A 251 ? 0.52256 0.55580 0.54154 0.01598  0.02569  -0.02658 251 THR A C   
3889 O O   . THR A 251 ? 0.51162 0.53860 0.52170 0.01788  0.02285  -0.02226 251 THR A O   
3890 C CB  . THR A 251 ? 0.53308 0.57054 0.55262 0.01028  0.03163  -0.02926 251 THR A CB  
3891 O OG1 . THR A 251 ? 0.48905 0.53495 0.50923 0.00870  0.02890  -0.03208 251 THR A OG1 
3892 C CG2 . THR A 251 ? 0.49840 0.53544 0.52433 0.00728  0.03538  -0.03152 251 THR A CG2 
3900 N N   . VAL A 252 ? 0.48212 0.52233 0.50850 0.01571  0.02484  -0.03018 252 VAL A N   
3901 C CA  . VAL A 252 ? 0.51162 0.55487 0.53952 0.01760  0.02033  -0.02931 252 VAL A CA  
3902 C C   . VAL A 252 ? 0.51750 0.56233 0.53545 0.01681  0.01814  -0.02694 252 VAL A C   
3903 O O   . VAL A 252 ? 0.50199 0.54392 0.51583 0.01893  0.01322  -0.02407 252 VAL A O   
3904 C CB  . VAL A 252 ? 0.52971 0.56596 0.56133 0.02181  0.01486  -0.02588 252 VAL A CB  
3905 C CG1 . VAL A 252 ? 0.54872 0.59027 0.58975 0.02333  0.01031  -0.02690 252 VAL A CG1 
3906 C CG2 . VAL A 252 ? 0.51753 0.54945 0.55871 0.02298  0.01725  -0.02695 252 VAL A CG2 
3916 N N   . LEU A 253 ? 0.49122 0.53995 0.50609 0.01371  0.02098  -0.02828 253 LEU A N   
3917 C CA  . LEU A 253 ? 0.51503 0.56632 0.52420 0.01284  0.01942  -0.02669 253 LEU A CA  
3918 C C   . LEU A 253 ? 0.48400 0.54277 0.49532 0.01104  0.01840  -0.02880 253 LEU A C   
3919 O O   . LEU A 253 ? 0.48732 0.54836 0.49519 0.01028  0.01682  -0.02739 253 LEU A O   
3920 C CB  . LEU A 253 ? 0.41534 0.46608 0.42319 0.01073  0.02221  -0.02630 253 LEU A CB  
3921 C CG  . LEU A 253 ? 0.51437 0.55574 0.51761 0.01206  0.02519  -0.02348 253 LEU A CG  
3922 C CD1 . LEU A 253 ? 0.55338 0.59509 0.56216 0.00965  0.02953  -0.02435 253 LEU A CD1 
3923 C CD2 . LEU A 253 ? 0.54519 0.58132 0.53885 0.01359  0.02383  -0.02065 253 LEU A CD2 
3935 N N   . SER A 254 ? 0.45125 0.51265 0.46816 0.01011  0.02034  -0.03223 254 SER A N   
3936 C CA  . SER A 254 ? 0.44903 0.51518 0.46550 0.00735  0.02159  -0.03444 254 SER A CA  
3937 C C   . SER A 254 ? 0.50392 0.57240 0.52190 0.00876  0.01876  -0.03258 254 SER A C   
3938 O O   . SER A 254 ? 0.47598 0.54692 0.48951 0.00648  0.01856  -0.03200 254 SER A O   
3939 C CB  . SER A 254 ? 0.45009 0.51636 0.47213 0.00579  0.02673  -0.03928 254 SER A CB  
3940 O OG  . SER A 254 ? 0.47552 0.54044 0.50911 0.00938  0.02675  -0.03975 254 SER A OG  
3946 N N   . PRO A 255 ? 0.55595 0.62317 0.58044 0.01217  0.01567  -0.03157 255 PRO A N   
3947 C CA  . PRO A 255 ? 0.44407 0.51332 0.47042 0.01297  0.01200  -0.03030 255 PRO A CA  
3948 C C   . PRO A 255 ? 0.49966 0.56729 0.51567 0.01266  0.00961  -0.02732 255 PRO A C   
3949 O O   . PRO A 255 ? 0.49743 0.56780 0.51316 0.01154  0.00873  -0.02693 255 PRO A O   
3950 C CB  . PRO A 255 ? 0.44380 0.50990 0.47811 0.01676  0.00646  -0.02939 255 PRO A CB  
3951 C CG  . PRO A 255 ? 0.50903 0.57042 0.54380 0.01829  0.00724  -0.02911 255 PRO A CG  
3952 C CD  . PRO A 255 ? 0.45039 0.51296 0.48003 0.01535  0.01382  -0.03095 255 PRO A CD  
3960 N N   . TYR A 256 ? 0.47130 0.53386 0.48012 0.01349  0.00954  -0.02541 256 TYR A N   
3961 C CA  . TYR A 256 ? 0.46220 0.52221 0.46355 0.01321  0.00909  -0.02330 256 TYR A CA  
3962 C C   . TYR A 256 ? 0.42751 0.49251 0.42980 0.01039  0.01107  -0.02350 256 TYR A C   
3963 O O   . TYR A 256 ? 0.45259 0.51822 0.45366 0.00994  0.01014  -0.02229 256 TYR A O   
3964 C CB  . TYR A 256 ? 0.41185 0.46363 0.40637 0.01438  0.01071  -0.02165 256 TYR A CB  
3965 C CG  . TYR A 256 ? 0.47871 0.52283 0.46917 0.01699  0.00689  -0.02034 256 TYR A CG  
3966 C CD1 . TYR A 256 ? 0.47470 0.51239 0.45704 0.01820  0.00194  -0.01893 256 TYR A CD1 
3967 C CD2 . TYR A 256 ? 0.46505 0.50757 0.46013 0.01812  0.00698  -0.02056 256 TYR A CD2 
3968 C CE1 . TYR A 256 ? 0.47063 0.49977 0.44821 0.02039  -0.00418 -0.01714 256 TYR A CE1 
3969 C CE2 . TYR A 256 ? 0.48155 0.51622 0.47420 0.02073  0.00166  -0.01854 256 TYR A CE2 
3970 C CZ  . TYR A 256 ? 0.51381 0.54158 0.49727 0.02185  -0.00475 -0.01656 256 TYR A CZ  
3971 O OH  . TYR A 256 ? 0.52413 0.54235 0.50400 0.02430  -0.01265 -0.01393 256 TYR A OH  
3981 N N   . LEU A 257 ? 0.47492 0.54240 0.47907 0.00829  0.01301  -0.02501 257 LEU A N   
3982 C CA  . LEU A 257 ? 0.50516 0.57558 0.50846 0.00525  0.01235  -0.02466 257 LEU A CA  
3983 C C   . LEU A 257 ? 0.49214 0.56512 0.49386 0.00342  0.01188  -0.02485 257 LEU A C   
3984 O O   . LEU A 257 ? 0.54231 0.61602 0.54197 0.00163  0.00983  -0.02290 257 LEU A O   
3985 C CB  . LEU A 257 ? 0.47811 0.54833 0.48120 0.00285  0.01317  -0.02657 257 LEU A CB  
3986 C CG  . LEU A 257 ? 0.55748 0.62535 0.56449 0.00374  0.01420  -0.02627 257 LEU A CG  
3987 C CD1 . LEU A 257 ? 0.53138 0.59866 0.53924 0.00146  0.01498  -0.02914 257 LEU A CD1 
3988 C CD2 . LEU A 257 ? 0.51880 0.58754 0.53028 0.00330  0.01242  -0.02408 257 LEU A CD2 
4000 N N   . LYS A 258 ? 0.38666 0.46039 0.39098 0.00379  0.01405  -0.02700 258 LYS A N   
4001 C CA  . LYS A 258 ? 0.48719 0.56250 0.49146 0.00155  0.01585  -0.02764 258 LYS A CA  
4002 C C   . LYS A 258 ? 0.47907 0.55545 0.48508 0.00262  0.01300  -0.02515 258 LYS A C   
4003 O O   . LYS A 258 ? 0.48526 0.56162 0.48791 0.00013  0.01306  -0.02358 258 LYS A O   
4004 C CB  . LYS A 258 ? 0.45572 0.53197 0.46802 0.00206  0.01988  -0.03116 258 LYS A CB  
4005 C CG  . LYS A 258 ? 0.47430 0.55198 0.49046 -0.00019 0.02368  -0.03235 258 LYS A CG  
4006 C CD  . LYS A 258 ? 0.49672 0.57709 0.52386 0.00277  0.02000  -0.03160 258 LYS A CD  
4007 C CE  . LYS A 258 ? 0.54394 0.62637 0.58158 0.00081  0.02516  -0.03407 258 LYS A CE  
4008 N NZ  . LYS A 258 ? 0.53414 0.61397 0.56097 -0.00403 0.03042  -0.03322 258 LYS A NZ  
4022 N N   . PHE A 259 ? 0.46078 0.53646 0.47045 0.00598  0.01023  -0.02472 259 PHE A N   
4023 C CA  . PHE A 259 ? 0.51812 0.59344 0.52870 0.00686  0.00745  -0.02333 259 PHE A CA  
4024 C C   . PHE A 259 ? 0.51987 0.59284 0.52590 0.00713  0.00641  -0.02107 259 PHE A C   
4025 O O   . PHE A 259 ? 0.51485 0.58671 0.52135 0.00748  0.00501  -0.02030 259 PHE A O   
4026 C CB  . PHE A 259 ? 0.50339 0.57649 0.51732 0.00979  0.00378  -0.02429 259 PHE A CB  
4027 C CG  . PHE A 259 ? 0.56376 0.64026 0.58909 0.00975  0.00359  -0.02655 259 PHE A CG  
4028 C CD1 . PHE A 259 ? 0.55335 0.63277 0.58518 0.00810  0.00415  -0.02713 259 PHE A CD1 
4029 C CD2 . PHE A 259 ? 0.57135 0.64790 0.60357 0.01136  0.00332  -0.02820 259 PHE A CD2 
4030 C CE1 . PHE A 259 ? 0.55385 0.63668 0.60030 0.00783  0.00517  -0.02974 259 PHE A CE1 
4031 C CE2 . PHE A 259 ? 0.62420 0.70432 0.67199 0.01146  0.00375  -0.03076 259 PHE A CE2 
4032 C CZ  . PHE A 259 ? 0.60542 0.68893 0.66106 0.00960  0.00497  -0.03173 259 PHE A CZ  
4042 N N   . GLY A 260 ? 0.52568 0.59773 0.52966 0.00687  0.00747  -0.02048 260 GLY A N   
4043 C CA  . GLY A 260 ? 0.45499 0.52511 0.45963 0.00720  0.00760  -0.01893 260 GLY A CA  
4044 C C   . GLY A 260 ? 0.47144 0.53565 0.47280 0.00941  0.00930  -0.01946 260 GLY A C   
4045 O O   . GLY A 260 ? 0.44127 0.50275 0.44419 0.00957  0.01140  -0.01898 260 GLY A O   
4049 N N   . CYS A 261 ? 0.43008 0.49074 0.42655 0.01094  0.00860  -0.02042 261 CYS A N   
4050 C CA  . CYS A 261 ? 0.45218 0.50362 0.44017 0.01237  0.01014  -0.02038 261 CYS A CA  
4051 C C   . CYS A 261 ? 0.50435 0.55303 0.49309 0.01193  0.01557  -0.02003 261 CYS A C   
4052 O O   . CYS A 261 ? 0.46135 0.50151 0.44378 0.01211  0.01995  -0.02009 261 CYS A O   
4053 C CB  . CYS A 261 ? 0.49300 0.54007 0.47576 0.01403  0.00630  -0.02049 261 CYS A CB  
4054 S SG  . CYS A 261 ? 0.49984 0.55088 0.48784 0.01451  -0.00041 -0.02151 261 CYS A SG  
4060 N N   . LEU A 262 ? 0.46613 0.52091 0.46240 0.01089  0.01583  -0.02011 262 LEU A N   
4061 C CA  . LEU A 262 ? 0.48370 0.53740 0.48506 0.01009  0.02005  -0.02019 262 LEU A CA  
4062 C C   . LEU A 262 ? 0.41612 0.47719 0.42845 0.00823  0.01784  -0.01991 262 LEU A C   
4063 O O   . LEU A 262 ? 0.47610 0.54231 0.48841 0.00698  0.01344  -0.01980 262 LEU A O   
4064 C CB  . LEU A 262 ? 0.50745 0.55974 0.50760 0.01026  0.02082  -0.02075 262 LEU A CB  
4065 C CG  . LEU A 262 ? 0.44695 0.49782 0.45407 0.00911  0.02543  -0.02122 262 LEU A CG  
4066 C CD1 . LEU A 262 ? 0.48201 0.52335 0.48523 0.00957  0.03247  -0.02063 262 LEU A CD1 
4067 C CD2 . LEU A 262 ? 0.47470 0.52525 0.48188 0.00896  0.02533  -0.02218 262 LEU A CD2 
4079 N N   . SER A 263 ? 0.44444 0.50475 0.46608 0.00780  0.02090  -0.01976 263 SER A N   
4080 C CA  . SER A 263 ? 0.46907 0.53531 0.50341 0.00619  0.01669  -0.01893 263 SER A CA  
4081 C C   . SER A 263 ? 0.46773 0.53658 0.50577 0.00439  0.01404  -0.01983 263 SER A C   
4082 O O   . SER A 263 ? 0.47349 0.53958 0.51492 0.00448  0.01876  -0.02119 263 SER A O   
4083 C CB  . SER A 263 ? 0.43950 0.50422 0.48797 0.00655  0.02106  -0.01896 263 SER A CB  
4084 O OG  . SER A 263 ? 0.47932 0.54917 0.54437 0.00510  0.01609  -0.01825 263 SER A OG  
4090 N N   . ALA A 264 ? 0.41103 0.48354 0.44667 0.00232  0.00697  -0.01924 264 ALA A N   
4091 C CA  . ALA A 264 ? 0.49850 0.57211 0.53660 -0.00018 0.00335  -0.02067 264 ALA A CA  
4092 C C   . ALA A 264 ? 0.46379 0.53879 0.52050 -0.00081 0.00201  -0.02064 264 ALA A C   
4093 O O   . ALA A 264 ? 0.45574 0.53049 0.51887 -0.00198 0.00285  -0.02273 264 ALA A O   
4094 C CB  . ALA A 264 ? 0.50504 0.57920 0.53334 -0.00316 -0.00393 -0.01999 264 ALA A CB  
4100 N N   . ARG A 265 ? 0.53146 0.60791 0.59974 0.00001  0.00043  -0.01858 265 ARG A N   
4101 C CA  . ARG A 265 ? 0.47363 0.55212 0.56535 -0.00042 -0.00088 -0.01873 265 ARG A CA  
4102 C C   . ARG A 265 ? 0.47948 0.55517 0.58012 0.00074  0.01092  -0.02125 265 ARG A C   
4103 O O   . ARG A 265 ? 0.46706 0.54402 0.58490 -0.00057 0.01136  -0.02290 265 ARG A O   
4104 C CB  . ARG A 265 ? 0.53906 0.61919 0.64311 0.00060  -0.00435 -0.01602 265 ARG A CB  
4105 C CG  . ARG A 265 ? 0.62036 0.70300 0.73419 -0.00153 -0.01861 -0.01330 265 ARG A CG  
4106 C CD  . ARG A 265 ? 0.65847 0.73945 0.75635 -0.00220 -0.02604 -0.00950 265 ARG A CD  
4107 N NE  . ARG A 265 ? 0.67193 0.75358 0.78426 -0.00022 -0.02679 -0.00675 265 ARG A NE  
4108 C CZ  . ARG A 265 ? 0.62196 0.70237 0.73509 -0.00113 -0.03774 -0.00212 265 ARG A CZ  
4109 N NH1 . ARG A 265 ? 0.61850 0.69549 0.71510 -0.00450 -0.04886 0.00044  265 ARG A NH1 
4110 N NH2 . ARG A 265 ? 0.55352 0.63446 0.68308 0.00109  -0.03708 -0.00005 265 ARG A NH2 
4124 N N   . LEU A 266 ? 0.44106 0.51159 0.52968 0.00275  0.02034  -0.02157 266 LEU A N   
4125 C CA  . LEU A 266 ? 0.46943 0.53358 0.55973 0.00320  0.03227  -0.02345 266 LEU A CA  
4126 C C   . LEU A 266 ? 0.43232 0.49519 0.51716 0.00209  0.03257  -0.02471 266 LEU A C   
4127 O O   . LEU A 266 ? 0.43261 0.49336 0.52971 0.00103  0.03856  -0.02629 266 LEU A O   
4128 C CB  . LEU A 266 ? 0.49289 0.54897 0.56489 0.00502  0.03978  -0.02315 266 LEU A CB  
4129 C CG  . LEU A 266 ? 0.54338 0.58852 0.60686 0.00503  0.05161  -0.02422 266 LEU A CG  
4130 C CD1 . LEU A 266 ? 0.56521 0.60739 0.64879 0.00386  0.06213  -0.02610 266 LEU A CD1 
4131 C CD2 . LEU A 266 ? 0.61732 0.65298 0.65724 0.00639  0.05473  -0.02351 266 LEU A CD2 
4143 N N   . PHE A 267 ? 0.45502 0.51871 0.52304 0.00222  0.02718  -0.02434 267 PHE A N   
4144 C CA  . PHE A 267 ? 0.51225 0.57476 0.57631 0.00115  0.02712  -0.02598 267 PHE A CA  
4145 C C   . PHE A 267 ? 0.49397 0.56075 0.57578 -0.00163 0.02275  -0.02787 267 PHE A C   
4146 O O   . PHE A 267 ? 0.48075 0.54492 0.57075 -0.00259 0.02782  -0.02963 267 PHE A O   
4147 C CB  . PHE A 267 ? 0.50990 0.57385 0.55782 0.00133  0.02165  -0.02599 267 PHE A CB  
4148 C CG  . PHE A 267 ? 0.53566 0.59658 0.57755 0.00115  0.02372  -0.02781 267 PHE A CG  
4149 C CD1 . PHE A 267 ? 0.57254 0.63010 0.62264 0.00036  0.02854  -0.02913 267 PHE A CD1 
4150 C CD2 . PHE A 267 ? 0.52065 0.58187 0.55111 0.00166  0.02149  -0.02845 267 PHE A CD2 
4151 C CE1 . PHE A 267 ? 0.51944 0.57371 0.56508 0.00028  0.03029  -0.03072 267 PHE A CE1 
4152 C CE2 . PHE A 267 ? 0.59413 0.65245 0.62194 0.00173  0.02368  -0.03042 267 PHE A CE2 
4153 C CZ  . PHE A 267 ? 0.50123 0.55591 0.53601 0.00115  0.02771  -0.03138 267 PHE A CZ  
4163 N N   . HIS A 268 ? 0.47287 0.54515 0.56088 -0.00323 0.01257  -0.02732 268 HIS A N   
4164 C CA  . HIS A 268 ? 0.44870 0.52416 0.55258 -0.00626 0.00512  -0.02904 268 HIS A CA  
4165 C C   . HIS A 268 ? 0.51724 0.59337 0.64774 -0.00621 0.01118  -0.03000 268 HIS A C   
4166 O O   . HIS A 268 ? 0.43187 0.50803 0.57536 -0.00821 0.01192  -0.03263 268 HIS A O   
4167 C CB  . HIS A 268 ? 0.46163 0.54030 0.56490 -0.00798 -0.00830 -0.02710 268 HIS A CB  
4168 C CG  . HIS A 268 ? 0.43810 0.51764 0.54888 -0.01189 -0.01971 -0.02888 268 HIS A CG  
4169 N ND1 . HIS A 268 ? 0.51249 0.59528 0.65083 -0.01297 -0.02533 -0.02917 268 HIS A ND1 
4170 C CD2 . HIS A 268 ? 0.42228 0.49880 0.51663 -0.01534 -0.02674 -0.03095 268 HIS A CD2 
4171 C CE1 . HIS A 268 ? 0.48022 0.56204 0.61821 -0.01694 -0.03726 -0.03103 268 HIS A CE1 
4172 N NE2 . HIS A 268 ? 0.46876 0.54598 0.57808 -0.01866 -0.03783 -0.03231 268 HIS A NE2 
4180 N N   . ALA A 269 ? 0.45371 0.52987 0.59388 -0.00420 0.01659  -0.02841 269 ALA A N   
4181 C CA  . ALA A 269 ? 0.46098 0.53696 0.62838 -0.00438 0.02496  -0.02994 269 ALA A CA  
4182 C C   . ALA A 269 ? 0.50330 0.57240 0.66766 -0.00475 0.03850  -0.03192 269 ALA A C   
4183 O O   . ALA A 269 ? 0.51499 0.58441 0.70257 -0.00653 0.04320  -0.03424 269 ALA A O   
4184 C CB  . ALA A 269 ? 0.48602 0.56092 0.66022 -0.00221 0.03128  -0.02863 269 ALA A CB  
4190 N N   . ARG A 270 ? 0.46203 0.52417 0.59902 -0.00323 0.04442  -0.03080 270 ARG A N   
4191 C CA  . ARG A 270 ? 0.49589 0.54910 0.62668 -0.00358 0.05622  -0.03156 270 ARG A CA  
4192 C C   . ARG A 270 ? 0.52998 0.58524 0.66642 -0.00573 0.05193  -0.03364 270 ARG A C   
4193 O O   . ARG A 270 ? 0.56131 0.61132 0.70718 -0.00711 0.06126  -0.03499 270 ARG A O   
4194 C CB  . ARG A 270 ? 0.53682 0.58133 0.63733 -0.00131 0.06031  -0.02922 270 ARG A CB  
4195 C CG  . ARG A 270 ? 0.63121 0.66889 0.72369 0.00006  0.06840  -0.02802 270 ARG A CG  
4196 C CD  . ARG A 270 ? 0.66229 0.68950 0.76215 -0.00137 0.08451  -0.02913 270 ARG A CD  
4197 N NE  . ARG A 270 ? 0.72556 0.74003 0.80666 -0.00175 0.09194  -0.02779 270 ARG A NE  
4198 C CZ  . ARG A 270 ? 0.82727 0.82938 0.87923 -0.00048 0.09460  -0.02525 270 ARG A CZ  
4199 N NH1 . ARG A 270 ? 0.86744 0.86848 0.90548 0.00107  0.09123  -0.02445 270 ARG A NH1 
4200 N NH2 . ARG A 270 ? 0.72143 0.71109 0.75802 -0.00091 0.09983  -0.02328 270 ARG A NH2 
4214 N N   . LEU A 271 ? 0.49646 0.55774 0.62616 -0.00648 0.03899  -0.03423 271 LEU A N   
4215 C CA  . LEU A 271 ? 0.46422 0.52646 0.59835 -0.00908 0.03468  -0.03720 271 LEU A CA  
4216 C C   . LEU A 271 ? 0.50982 0.57655 0.67446 -0.01199 0.03196  -0.03981 271 LEU A C   
4217 O O   . LEU A 271 ? 0.46790 0.53233 0.64359 -0.01401 0.03614  -0.04244 271 LEU A O   
4218 C CB  . LEU A 271 ? 0.48848 0.55402 0.60641 -0.01000 0.02274  -0.03795 271 LEU A CB  
4219 C CG  . LEU A 271 ? 0.51806 0.57947 0.61098 -0.00767 0.02569  -0.03674 271 LEU A CG  
4220 C CD1 . LEU A 271 ? 0.48926 0.55424 0.56823 -0.00838 0.01608  -0.03671 271 LEU A CD1 
4221 C CD2 . LEU A 271 ? 0.53936 0.59572 0.62871 -0.00826 0.03027  -0.03903 271 LEU A CD2 
4233 N N   . LEU A 272 ? 0.44369 0.51675 0.62446 -0.01227 0.02415  -0.03911 272 LEU A N   
4234 C CA  . LEU A 272 ? 0.49447 0.57240 0.70895 -0.01482 0.01971  -0.04150 272 LEU A CA  
4235 C C   . LEU A 272 ? 0.53145 0.60556 0.76707 -0.01482 0.03677  -0.04284 272 LEU A C   
4236 O O   . LEU A 272 ? 0.48656 0.56234 0.74807 -0.01754 0.03741  -0.04602 272 LEU A O   
4237 C CB  . LEU A 272 ? 0.50629 0.59068 0.73555 -0.01444 0.00804  -0.03957 272 LEU A CB  
4238 C CG  . LEU A 272 ? 0.53606 0.62236 0.74585 -0.01546 -0.00960 -0.03781 272 LEU A CG  
4239 C CD1 . LEU A 272 ? 0.49385 0.58515 0.72361 -0.01530 -0.02174 -0.03528 272 LEU A CD1 
4240 C CD2 . LEU A 272 ? 0.59698 0.68195 0.79905 -0.01942 -0.01976 -0.04107 272 LEU A CD2 
4252 N N   . GLU A 273 ? 0.57858 0.64622 0.80269 -0.01230 0.05098  -0.04072 273 GLU A N   
4253 C CA  . GLU A 273 ? 0.60951 0.66940 0.84593 -0.01295 0.06984  -0.04186 273 GLU A CA  
4254 C C   . GLU A 273 ? 0.55908 0.61305 0.79083 -0.01489 0.07531  -0.04331 273 GLU A C   
4255 O O   . GLU A 273 ? 0.56537 0.61791 0.82258 -0.01744 0.08367  -0.04595 273 GLU A O   
4256 C CB  . GLU A 273 ? 0.65320 0.70327 0.86619 -0.01049 0.08276  -0.03922 273 GLU A CB  
4257 C CG  . GLU A 273 ? 0.93499 0.98413 1.16840 -0.01027 0.09309  -0.04014 273 GLU A CG  
4258 C CD  . GLU A 273 ? 0.99814 1.03769 1.20283 -0.00805 0.10148  -0.03790 273 GLU A CD  
4259 O OE1 . GLU A 273 ? 0.93559 0.96175 1.11315 -0.00811 0.11194  -0.03652 273 GLU A OE1 
4260 O OE2 . GLU A 273 ? 0.87839 0.92280 1.08732 -0.00643 0.09679  -0.03741 273 GLU A OE2 
4267 N N   . VAL A 274 ? 0.57342 0.62375 0.77500 -0.01377 0.07106  -0.04178 274 VAL A N   
4268 C CA  . VAL A 274 ? 0.56276 0.60670 0.75925 -0.01524 0.07583  -0.04288 274 VAL A CA  
4269 C C   . VAL A 274 ? 0.51680 0.56854 0.73583 -0.01863 0.06533  -0.04727 274 VAL A C   
4270 O O   . VAL A 274 ? 0.54672 0.59497 0.78117 -0.02114 0.07208  -0.04969 274 VAL A O   
4271 C CB  . VAL A 274 ? 0.55790 0.59631 0.71988 -0.01275 0.07330  -0.04026 274 VAL A CB  
4272 C CG1 . VAL A 274 ? 0.54056 0.57486 0.70076 -0.01426 0.07390  -0.04207 274 VAL A CG1 
4273 C CG2 . VAL A 274 ? 0.58891 0.61586 0.72930 -0.01018 0.08463  -0.03607 274 VAL A CG2 
4283 N N   . TYR A 275 ? 0.50441 0.56529 0.72413 -0.01920 0.04836  -0.04838 275 TYR A N   
4284 C CA  . TYR A 275 ? 0.51070 0.57682 0.74673 -0.02305 0.03592  -0.05278 275 TYR A CA  
4285 C C   . TYR A 275 ? 0.47702 0.54716 0.75420 -0.02567 0.03798  -0.05551 275 TYR A C   
4286 O O   . TYR A 275 ? 0.54048 0.61122 0.83453 -0.02918 0.03477  -0.05964 275 TYR A O   
4287 C CB  . TYR A 275 ? 0.43498 0.50701 0.65976 -0.02368 0.01728  -0.05273 275 TYR A CB  
4288 C CG  . TYR A 275 ? 0.52502 0.59341 0.71394 -0.02252 0.01450  -0.05193 275 TYR A CG  
4289 C CD1 . TYR A 275 ? 0.51472 0.57616 0.68718 -0.02092 0.02557  -0.05172 275 TYR A CD1 
4290 C CD2 . TYR A 275 ? 0.48982 0.56085 0.66258 -0.02311 0.00112  -0.05120 275 TYR A CD2 
4291 C CE1 . TYR A 275 ? 0.50860 0.56740 0.65371 -0.01969 0.02343  -0.05143 275 TYR A CE1 
4292 C CE2 . TYR A 275 ? 0.48651 0.55402 0.62959 -0.02239 0.00066  -0.05109 275 TYR A CE2 
4293 C CZ  . TYR A 275 ? 0.51469 0.57688 0.64609 -0.02056 0.01184  -0.05153 275 TYR A CZ  
4294 O OH  . TYR A 275 ? 0.47751 0.53685 0.58452 -0.01974 0.01159  -0.05191 275 TYR A OH  
4304 N N   . ARG A 276 ? 0.55847 0.63118 0.85417 -0.02417 0.04376  -0.05378 276 ARG A N   
4305 C CA  . ARG A 276 ? 0.56996 0.64683 0.91010 -0.02655 0.04730  -0.05679 276 ARG A CA  
4306 C C   . ARG A 276 ? 0.50341 0.57294 0.85420 -0.02881 0.06384  -0.05923 276 ARG A C   
4307 O O   . ARG A 276 ? 0.51964 0.59288 0.90426 -0.03231 0.06172  -0.06339 276 ARG A O   
4308 C CB  . ARG A 276 ? 0.52274 0.60115 0.87976 -0.02428 0.05613  -0.05491 276 ARG A CB  
4309 C CG  . ARG A 276 ? 0.70996 0.79547 1.06275 -0.02211 0.04027  -0.05223 276 ARG A CG  
4310 C CD  . ARG A 276 ? 0.82999 0.92055 1.22090 -0.02125 0.04392  -0.05251 276 ARG A CD  
4311 N NE  . ARG A 276 ? 0.98845 1.07229 1.36659 -0.01843 0.06214  -0.05054 276 ARG A NE  
4312 C CZ  . ARG A 276 ? 1.08094 1.16290 1.42794 -0.01542 0.05928  -0.04689 276 ARG A CZ  
4313 N NH1 . ARG A 276 ? 0.81041 0.89663 1.13573 -0.01474 0.04045  -0.04447 276 ARG A NH1 
4314 N NH2 . ARG A 276 ? 1.02904 1.10342 1.36573 -0.01353 0.07636  -0.04600 276 ARG A NH2 
4328 N N   . ARG A 277 ? 0.52387 0.58201 0.84598 -0.02706 0.07956  -0.05643 277 ARG A N   
4329 C CA  . ARG A 277 ? 0.54135 0.58935 0.86984 -0.02916 0.09724  -0.05744 277 ARG A CA  
4330 C C   . ARG A 277 ? 0.56872 0.61341 0.88372 -0.03070 0.09222  -0.05897 277 ARG A C   
4331 O O   . ARG A 277 ? 0.55481 0.59046 0.87504 -0.03263 0.10575  -0.05956 277 ARG A O   
4332 C CB  . ARG A 277 ? 0.56083 0.59478 0.86354 -0.02692 0.11672  -0.05301 277 ARG A CB  
4333 C CG  . ARG A 277 ? 0.58045 0.61476 0.89485 -0.02584 0.12557  -0.05236 277 ARG A CG  
4334 C CD  . ARG A 277 ? 0.56321 0.58825 0.83728 -0.02239 0.13059  -0.04765 277 ARG A CD  
4335 N NE  . ARG A 277 ? 0.54362 0.55933 0.82200 -0.02277 0.14965  -0.04745 277 ARG A NE  
4336 C CZ  . ARG A 277 ? 0.56452 0.56616 0.80801 -0.02123 0.15991  -0.04400 277 ARG A CZ  
4337 N NH1 . ARG A 277 ? 0.57994 0.57633 0.78462 -0.01874 0.15211  -0.03999 277 ARG A NH1 
4338 N NH2 . ARG A 277 ? 0.56382 0.55565 0.81222 -0.02248 0.17837  -0.04501 277 ARG A NH2 
4352 N N   . HIS A 278 ? 0.57337 0.62379 0.87122 -0.03023 0.07437  -0.05983 278 HIS A N   
4353 C CA  . HIS A 278 ? 0.59701 0.64367 0.88061 -0.03163 0.07007  -0.06205 278 HIS A CA  
4354 C C   . HIS A 278 ? 0.55851 0.61414 0.85164 -0.03481 0.04985  -0.06708 278 HIS A C   
4355 O O   . HIS A 278 ? 0.54155 0.59933 0.81038 -0.03392 0.03761  -0.06685 278 HIS A O   
4356 C CB  . HIS A 278 ? 0.56705 0.60684 0.81069 -0.02781 0.07208  -0.05793 278 HIS A CB  
4357 C CG  . HIS A 278 ? 0.59228 0.61973 0.82244 -0.02542 0.08996  -0.05291 278 HIS A CG  
4358 N ND1 . HIS A 278 ? 0.59358 0.61850 0.81578 -0.02298 0.09704  -0.04893 278 HIS A ND1 
4359 C CD2 . HIS A 278 ? 0.58987 0.60479 0.81152 -0.02555 0.10185  -0.05112 278 HIS A CD2 
4360 C CE1 . HIS A 278 ? 0.66806 0.67844 0.87469 -0.02203 0.11220  -0.04502 278 HIS A CE1 
4361 N NE2 . HIS A 278 ? 0.58867 0.59262 0.79470 -0.02343 0.11508  -0.04576 278 HIS A NE2 
4369 N N   . PRO A 279 ? 0.59134 0.65086 0.91866 -0.03903 0.04601  -0.07190 279 PRO A N   
4370 C CA  . PRO A 279 ? 0.61251 0.67924 0.94922 -0.04266 0.02412  -0.07653 279 PRO A CA  
4371 C C   . PRO A 279 ? 0.56543 0.62778 0.87365 -0.04446 0.01521  -0.07980 279 PRO A C   
4372 O O   . PRO A 279 ? 0.62071 0.68593 0.92161 -0.04710 -0.00330 -0.08248 279 PRO A O   
4373 C CB  . PRO A 279 ? 0.58784 0.65792 0.97000 -0.04694 0.02450  -0.08129 279 PRO A CB  
4374 C CG  . PRO A 279 ? 0.65840 0.71987 1.04459 -0.04656 0.04743  -0.08052 279 PRO A CG  
4375 C CD  . PRO A 279 ? 0.75529 0.81087 1.11260 -0.04134 0.06141  -0.07368 279 PRO A CD  
4383 N N   . ALA A 280 ? 0.57729 0.63136 0.86874 -0.04337 0.02784  -0.07969 280 ALA A N   
4384 C CA  . ALA A 280 ? 0.60362 0.65269 0.87025 -0.04487 0.02230  -0.08343 280 ALA A CA  
4385 C C   . ALA A 280 ? 0.59811 0.64507 0.82863 -0.04076 0.02274  -0.07954 280 ALA A C   
4386 O O   . ALA A 280 ? 0.57331 0.61456 0.78367 -0.04078 0.02427  -0.08181 280 ALA A O   
4387 C CB  . ALA A 280 ? 0.60326 0.64428 0.87600 -0.04598 0.03497  -0.08582 280 ALA A CB  
4393 N N   . HIS A 281 ? 0.60539 0.65683 0.82984 -0.03740 0.02170  -0.07421 281 HIS A N   
4394 C CA  . HIS A 281 ? 0.55571 0.60547 0.74912 -0.03345 0.02294  -0.07037 281 HIS A CA  
4395 C C   . HIS A 281 ? 0.53727 0.58658 0.70960 -0.03613 0.01034  -0.07438 281 HIS A C   
4396 O O   . HIS A 281 ? 0.53685 0.58801 0.71515 -0.04077 -0.00310 -0.07854 281 HIS A O   
4397 C CB  . HIS A 281 ? 0.50834 0.56300 0.70176 -0.03006 0.02320  -0.06465 281 HIS A CB  
4398 C CG  . HIS A 281 ? 0.49923 0.56117 0.70427 -0.03243 0.00811  -0.06551 281 HIS A CG  
4399 N ND1 . HIS A 281 ? 0.56316 0.62598 0.74837 -0.03401 -0.00575 -0.06636 281 HIS A ND1 
4400 C CD2 . HIS A 281 ? 0.53810 0.60570 0.77323 -0.03355 0.00453  -0.06534 281 HIS A CD2 
4401 C CE1 . HIS A 281 ? 0.53173 0.59968 0.73225 -0.03594 -0.01877 -0.06599 281 HIS A CE1 
4402 N NE2 . HIS A 281 ? 0.53946 0.61132 0.77261 -0.03541 -0.01317 -0.06548 281 HIS A NE2 
4410 N N   . SER A 282 ? 0.48118 0.52677 0.62833 -0.03345 0.01479  -0.07317 282 SER A N   
4411 C CA  . SER A 282 ? 0.52315 0.56652 0.64785 -0.03610 0.00638  -0.07703 282 SER A CA  
4412 C C   . SER A 282 ? 0.49003 0.53778 0.60828 -0.03746 -0.00645 -0.07496 282 SER A C   
4413 O O   . SER A 282 ? 0.45369 0.50696 0.58104 -0.03451 -0.00667 -0.06952 282 SER A O   
4414 C CB  . SER A 282 ? 0.44849 0.48804 0.55287 -0.03236 0.01526  -0.07566 282 SER A CB  
4415 O OG  . SER A 282 ? 0.52640 0.56930 0.62582 -0.02727 0.01914  -0.06873 282 SER A OG  
4421 N N   . GLN A 283 ? 0.53079 0.57433 0.63212 -0.04237 -0.01709 -0.07950 283 GLN A N   
4422 C CA  . GLN A 283 ? 0.52610 0.57063 0.61759 -0.04465 -0.03118 -0.07746 283 GLN A CA  
4423 C C   . GLN A 283 ? 0.58585 0.62488 0.64454 -0.04512 -0.03010 -0.07751 283 GLN A C   
4424 O O   . GLN A 283 ? 0.51754 0.55218 0.56406 -0.04442 -0.01952 -0.08070 283 GLN A O   
4425 C CB  . GLN A 283 ? 0.62989 0.67118 0.72747 -0.05133 -0.04714 -0.08236 283 GLN A CB  
4426 C CG  . GLN A 283 ? 0.63804 0.68545 0.77354 -0.05146 -0.04880 -0.08293 283 GLN A CG  
4427 C CD  . GLN A 283 ? 0.78145 0.83661 0.93936 -0.05014 -0.05881 -0.07767 283 GLN A CD  
4428 O OE1 . GLN A 283 ? 0.81676 0.87764 1.00912 -0.04979 -0.05792 -0.07785 283 GLN A OE1 
4429 N NE2 . GLN A 283 ? 0.78461 0.83952 0.92535 -0.04950 -0.06733 -0.07319 283 GLN A NE2 
4438 N N   . PRO A 284 ? 0.60608 0.64476 0.65171 -0.04628 -0.04017 -0.07394 284 PRO A N   
4439 C CA  . PRO A 284 ? 0.53499 0.56717 0.54959 -0.04746 -0.03762 -0.07420 284 PRO A CA  
4440 C C   . PRO A 284 ? 0.55415 0.57454 0.54737 -0.05404 -0.03903 -0.08228 284 PRO A C   
4441 O O   . PRO A 284 ? 0.59512 0.61137 0.59290 -0.05897 -0.04867 -0.08686 284 PRO A O   
4442 C CB  . PRO A 284 ? 0.57756 0.61023 0.58521 -0.04834 -0.05039 -0.06842 284 PRO A CB  
4443 C CG  . PRO A 284 ? 0.61266 0.65559 0.65261 -0.04465 -0.05430 -0.06386 284 PRO A CG  
4444 C CD  . PRO A 284 ? 0.55711 0.60127 0.61832 -0.04597 -0.05251 -0.06892 284 PRO A CD  
4452 N N   . PRO A 285 ? 0.62607 0.63994 0.59623 -0.05474 -0.02919 -0.08496 285 PRO A N   
4453 C CA  . PRO A 285 ? 0.61693 0.63460 0.58123 -0.04979 -0.01871 -0.08056 285 PRO A CA  
4454 C C   . PRO A 285 ? 0.58712 0.61110 0.56852 -0.04344 -0.00440 -0.08025 285 PRO A C   
4455 O O   . PRO A 285 ? 0.57543 0.60348 0.55627 -0.03891 0.00247  -0.07627 285 PRO A O   
4456 C CB  . PRO A 285 ? 0.67108 0.67602 0.60310 -0.05545 -0.01569 -0.08537 285 PRO A CB  
4457 C CG  . PRO A 285 ? 0.65764 0.65299 0.58339 -0.06118 -0.01566 -0.09454 285 PRO A CG  
4458 C CD  . PRO A 285 ? 0.70306 0.70334 0.65011 -0.06171 -0.02820 -0.09377 285 PRO A CD  
4466 N N   . VAL A 286 ? 0.54423 0.56837 0.54126 -0.04300 -0.00054 -0.08393 286 VAL A N   
4467 C CA  . VAL A 286 ? 0.54708 0.57383 0.55612 -0.03752 0.01218  -0.08339 286 VAL A CA  
4468 C C   . VAL A 286 ? 0.50330 0.53842 0.53090 -0.03126 0.01384  -0.07576 286 VAL A C   
4469 O O   . VAL A 286 ? 0.47456 0.51089 0.50724 -0.02621 0.02241  -0.07317 286 VAL A O   
4470 C CB  . VAL A 286 ? 0.54728 0.56863 0.56415 -0.03967 0.01694  -0.09027 286 VAL A CB  
4471 C CG1 . VAL A 286 ? 0.56887 0.57974 0.56517 -0.04612 0.01780  -0.09898 286 VAL A CG1 
4472 C CG2 . VAL A 286 ? 0.58142 0.60506 0.61617 -0.04139 0.00995  -0.09026 286 VAL A CG2 
4482 N N   . SER A 287 ? 0.54768 0.58735 0.58551 -0.03172 0.00581  -0.07230 287 SER A N   
4483 C CA  . SER A 287 ? 0.48771 0.53305 0.54244 -0.02673 0.00946  -0.06621 287 SER A CA  
4484 C C   . SER A 287 ? 0.48160 0.53024 0.52823 -0.02228 0.01205  -0.06053 287 SER A C   
4485 O O   . SER A 287 ? 0.50166 0.54957 0.53255 -0.02324 0.00994  -0.06082 287 SER A O   
4486 C CB  . SER A 287 ? 0.44830 0.49765 0.51964 -0.02870 0.00117  -0.06490 287 SER A CB  
4487 O OG  . SER A 287 ? 0.50133 0.55237 0.56354 -0.03074 -0.00962 -0.06317 287 SER A OG  
4493 N N   . LEU A 288 ? 0.51342 0.56442 0.57040 -0.01786 0.01716  -0.05557 288 LEU A N   
4494 C CA  A LEU A 288 ? 0.48724 0.54076 0.53750 -0.01389 0.01876  -0.05044 288 LEU A CA  
4495 C CA  B LEU A 288 ? 0.49978 0.55329 0.55008 -0.01389 0.01877  -0.05043 288 LEU A CA  
4496 C C   . LEU A 288 ? 0.47766 0.53551 0.52588 -0.01534 0.01047  -0.04827 288 LEU A C   
4497 O O   . LEU A 288 ? 0.52940 0.58856 0.56673 -0.01393 0.00964  -0.04592 288 LEU A O   
4498 C CB  A LEU A 288 ? 0.49288 0.54490 0.55122 -0.00981 0.02597  -0.04611 288 LEU A CB  
4499 C CB  B LEU A 288 ? 0.53145 0.58352 0.58992 -0.00982 0.02592  -0.04609 288 LEU A CB  
4500 C CG  A LEU A 288 ? 0.58509 0.63692 0.63443 -0.00556 0.02847  -0.04148 288 LEU A CG  
4501 C CG  B LEU A 288 ? 0.57505 0.62259 0.62582 -0.00578 0.03208  -0.04396 288 LEU A CG  
4502 C CD1 A LEU A 288 ? 0.55545 0.60697 0.59340 -0.00449 0.02813  -0.04273 288 LEU A CD1 
4503 C CD1 B LEU A 288 ? 0.58202 0.62482 0.63582 -0.00290 0.03805  -0.03928 288 LEU A CD1 
4504 C CD2 A LEU A 288 ? 0.57970 0.62526 0.63135 -0.00254 0.03597  -0.03801 288 LEU A CD2 
4505 C CD2 B LEU A 288 ? 0.56135 0.61142 0.60040 -0.00408 0.02962  -0.04288 288 LEU A CD2 
4528 N N   . ARG A 289 ? 0.53356 0.59342 0.59402 -0.01811 0.00383  -0.04888 289 ARG A N   
4529 C CA  . ARG A 289 ? 0.47127 0.53398 0.53041 -0.01982 -0.00636 -0.04669 289 ARG A CA  
4530 C C   . ARG A 289 ? 0.51966 0.57814 0.55720 -0.02372 -0.01270 -0.04903 289 ARG A C   
4531 O O   . ARG A 289 ? 0.48722 0.54574 0.51345 -0.02388 -0.01695 -0.04600 289 ARG A O   
4532 C CB  . ARG A 289 ? 0.51728 0.58262 0.59775 -0.02215 -0.01382 -0.04722 289 ARG A CB  
4533 C CG  . ARG A 289 ? 0.46431 0.53233 0.54781 -0.02325 -0.02583 -0.04387 289 ARG A CG  
4534 C CD  . ARG A 289 ? 0.47734 0.54733 0.58348 -0.02640 -0.03666 -0.04530 289 ARG A CD  
4535 N NE  . ARG A 289 ? 0.47430 0.54418 0.57847 -0.02838 -0.05182 -0.04224 289 ARG A NE  
4536 C CZ  . ARG A 289 ? 0.55176 0.61756 0.65271 -0.03347 -0.06750 -0.04394 289 ARG A CZ  
4537 N NH1 . ARG A 289 ? 0.58499 0.64709 0.68520 -0.03741 -0.06992 -0.04961 289 ARG A NH1 
4538 N NH2 . ARG A 289 ? 0.56930 0.63338 0.66675 -0.03485 -0.08186 -0.03973 289 ARG A NH2 
4552 N N   . GLY A 290 ? 0.50829 0.56159 0.53869 -0.02725 -0.01222 -0.05466 290 GLY A N   
4553 C CA  . GLY A 290 ? 0.53583 0.58223 0.54222 -0.03161 -0.01507 -0.05787 290 GLY A CA  
4554 C C   . GLY A 290 ? 0.52408 0.57031 0.51732 -0.02898 -0.00700 -0.05617 290 GLY A C   
4555 O O   . GLY A 290 ? 0.53857 0.58048 0.51355 -0.03184 -0.00977 -0.05579 290 GLY A O   
4559 N N   . GLN A 291 ? 0.49763 0.54755 0.50017 -0.02379 0.00264  -0.05495 291 GLN A N   
4560 C CA  . GLN A 291 ? 0.48364 0.53409 0.47822 -0.02111 0.00918  -0.05359 291 GLN A CA  
4561 C C   . GLN A 291 ? 0.50904 0.56276 0.49984 -0.02003 0.00465  -0.04818 291 GLN A C   
4562 O O   . GLN A 291 ? 0.48886 0.54048 0.46674 -0.02127 0.00621  -0.04803 291 GLN A O   
4563 C CB  . GLN A 291 ? 0.49500 0.54771 0.50124 -0.01568 0.01717  -0.05246 291 GLN A CB  
4564 C CG  . GLN A 291 ? 0.52659 0.57533 0.53796 -0.01626 0.02229  -0.05730 291 GLN A CG  
4565 C CD  . GLN A 291 ? 0.58149 0.62439 0.58061 -0.02133 0.02386  -0.06402 291 GLN A CD  
4566 O OE1 . GLN A 291 ? 0.52211 0.56317 0.51437 -0.02128 0.02961  -0.06607 291 GLN A OE1 
4567 N NE2 . GLN A 291 ? 0.54388 0.58288 0.54034 -0.02618 0.01916  -0.06802 291 GLN A NE2 
4576 N N   . LEU A 292 ? 0.51039 0.56868 0.51374 -0.01785 0.00024  -0.04397 292 LEU A N   
4577 C CA  . LEU A 292 ? 0.54873 0.60960 0.55063 -0.01707 -0.00466 -0.03911 292 LEU A CA  
4578 C C   . LEU A 292 ? 0.52934 0.58543 0.51711 -0.02229 -0.01378 -0.03902 292 LEU A C   
4579 O O   . LEU A 292 ? 0.51553 0.57069 0.49419 -0.02263 -0.01596 -0.03567 292 LEU A O   
4580 C CB  . LEU A 292 ? 0.54096 0.60647 0.56154 -0.01437 -0.00671 -0.03581 292 LEU A CB  
4581 C CG  . LEU A 292 ? 0.57731 0.64497 0.60505 -0.00934 0.00159  -0.03369 292 LEU A CG  
4582 C CD1 . LEU A 292 ? 0.59339 0.66346 0.63860 -0.00786 0.00152  -0.03148 292 LEU A CD1 
4583 C CD2 . LEU A 292 ? 0.58945 0.65779 0.60738 -0.00737 0.00321  -0.03130 292 LEU A CD2 
4595 N N   . LEU A 293 ? 0.52935 0.58103 0.51417 -0.02668 -0.01983 -0.04244 293 LEU A N   
4596 C CA  . LEU A 293 ? 0.57318 0.61722 0.54071 -0.03238 -0.03056 -0.04210 293 LEU A CA  
4597 C C   . LEU A 293 ? 0.52873 0.56369 0.46968 -0.03625 -0.02464 -0.04527 293 LEU A C   
4598 O O   . LEU A 293 ? 0.51116 0.53818 0.43238 -0.04035 -0.03050 -0.04310 293 LEU A O   
4599 C CB  . LEU A 293 ? 0.56923 0.61037 0.54234 -0.03626 -0.04039 -0.04521 293 LEU A CB  
4600 C CG  . LEU A 293 ? 0.65620 0.70478 0.65710 -0.03400 -0.04851 -0.04208 293 LEU A CG  
4601 C CD1 . LEU A 293 ? 0.68128 0.72548 0.68574 -0.03912 -0.06098 -0.04545 293 LEU A CD1 
4602 C CD2 . LEU A 293 ? 0.61712 0.66853 0.62296 -0.03205 -0.05546 -0.03521 293 LEU A CD2 
4614 N N   . TRP A 294 ? 0.51635 0.55111 0.45690 -0.03526 -0.01261 -0.05037 294 TRP A N   
4615 C CA  . TRP A 294 ? 0.53606 0.56342 0.45697 -0.03815 -0.00361 -0.05366 294 TRP A CA  
4616 C C   . TRP A 294 ? 0.57125 0.60129 0.48964 -0.03589 -0.00091 -0.04850 294 TRP A C   
4617 O O   . TRP A 294 ? 0.54556 0.56697 0.44330 -0.04025 0.00045  -0.04829 294 TRP A O   
4618 C CB  . TRP A 294 ? 0.57410 0.60312 0.50364 -0.03589 0.00888  -0.05930 294 TRP A CB  
4619 C CG  . TRP A 294 ? 0.56231 0.58367 0.48510 -0.04042 0.01000  -0.06655 294 TRP A CG  
4620 C CD1 . TRP A 294 ? 0.57720 0.60172 0.51605 -0.03857 0.01063  -0.06939 294 TRP A CD1 
4621 C CD2 . TRP A 294 ? 0.60884 0.61638 0.50564 -0.04805 0.01132  -0.07227 294 TRP A CD2 
4622 N NE1 . TRP A 294 ? 0.58451 0.59921 0.51111 -0.04433 0.01175  -0.07680 294 TRP A NE1 
4623 C CE2 . TRP A 294 ? 0.65737 0.66097 0.55684 -0.05039 0.01216  -0.07897 294 TRP A CE2 
4624 C CE3 . TRP A 294 ? 0.63232 0.62866 0.50204 -0.05361 0.01254  -0.07247 294 TRP A CE3 
4625 C CZ2 . TRP A 294 ? 0.71941 0.70820 0.59474 -0.05817 0.01387  -0.08647 294 TRP A CZ2 
4626 C CZ3 . TRP A 294 ? 0.69576 0.67615 0.53925 -0.06160 0.01486  -0.07951 294 TRP A CZ3 
4627 C CH2 . TRP A 294 ? 0.74128 0.71802 0.58746 -0.06385 0.01533  -0.08674 294 TRP A CH2 
4638 N N   . ARG A 295 ? 0.50435 0.54490 0.44246 -0.02951 0.00039  -0.04452 295 ARG A N   
4639 C CA  . ARG A 295 ? 0.57584 0.61944 0.51412 -0.02721 0.00197  -0.03986 295 ARG A CA  
4640 C C   . ARG A 295 ? 0.55174 0.59075 0.47879 -0.03038 -0.00821 -0.03486 295 ARG A C   
4641 O O   . ARG A 295 ? 0.52947 0.56264 0.44141 -0.03310 -0.00619 -0.03318 295 ARG A O   
4642 C CB  . ARG A 295 ? 0.51634 0.56990 0.47569 -0.02046 0.00348  -0.03699 295 ARG A CB  
4643 C CG  . ARG A 295 ? 0.53729 0.59456 0.50013 -0.01789 0.00190  -0.03178 295 ARG A CG  
4644 C CD  . ARG A 295 ? 0.49886 0.56296 0.47856 -0.01207 0.00395  -0.03018 295 ARG A CD  
4645 N NE  . ARG A 295 ? 0.54457 0.61142 0.52682 -0.00945 0.00548  -0.02727 295 ARG A NE  
4646 C CZ  . ARG A 295 ? 0.53716 0.60569 0.52342 -0.00839 0.00105  -0.02319 295 ARG A CZ  
4647 N NH1 . ARG A 295 ? 0.55580 0.62396 0.54561 -0.00960 -0.00569 -0.02108 295 ARG A NH1 
4648 N NH2 . ARG A 295 ? 0.55051 0.62101 0.53938 -0.00607 0.00312  -0.02148 295 ARG A NH2 
4662 N N   . GLU A 296 ? 0.52777 0.56866 0.46345 -0.03019 -0.01924 -0.03230 296 GLU A N   
4663 C CA  . GLU A 296 ? 0.55454 0.59083 0.48300 -0.03276 -0.03124 -0.02686 296 GLU A CA  
4664 C C   . GLU A 296 ? 0.60655 0.62818 0.50503 -0.04023 -0.03531 -0.02806 296 GLU A C   
4665 O O   . GLU A 296 ? 0.61598 0.62999 0.49850 -0.04296 -0.03938 -0.02344 296 GLU A O   
4666 C CB  . GLU A 296 ? 0.55964 0.60094 0.50814 -0.03124 -0.04243 -0.02486 296 GLU A CB  
4667 C CG  . GLU A 296 ? 0.53300 0.57256 0.48425 -0.03172 -0.05515 -0.01813 296 GLU A CG  
4668 C CD  . GLU A 296 ? 0.54108 0.58963 0.51196 -0.02591 -0.05127 -0.01407 296 GLU A CD  
4669 O OE1 . GLU A 296 ? 0.53401 0.58924 0.51375 -0.02183 -0.03953 -0.01642 296 GLU A OE1 
4670 O OE2 . GLU A 296 ? 0.51318 0.56099 0.49036 -0.02556 -0.06059 -0.00855 296 GLU A OE2 
4677 N N   . PHE A 297 ? 0.57276 0.58846 0.46144 -0.04406 -0.03410 -0.03426 297 PHE A N   
4678 C CA  . PHE A 297 ? 0.63388 0.63254 0.48935 -0.05213 -0.03651 -0.03661 297 PHE A CA  
4679 C C   . PHE A 297 ? 0.68591 0.67726 0.52183 -0.05433 -0.02418 -0.03651 297 PHE A C   
4680 O O   . PHE A 297 ? 0.63256 0.61054 0.44292 -0.05957 -0.02871 -0.03293 297 PHE A O   
4681 C CB  . PHE A 297 ? 0.62560 0.61991 0.47626 -0.05531 -0.03304 -0.04499 297 PHE A CB  
4682 C CG  . PHE A 297 ? 0.68835 0.66308 0.50206 -0.06418 -0.03220 -0.04936 297 PHE A CG  
4683 C CD1 . PHE A 297 ? 0.71638 0.67668 0.50433 -0.07022 -0.04647 -0.04512 297 PHE A CD1 
4684 C CD2 . PHE A 297 ? 0.72886 0.69799 0.53299 -0.06675 -0.01701 -0.05792 297 PHE A CD2 
4685 C CE1 . PHE A 297 ? 0.85828 0.79713 0.60681 -0.07930 -0.04525 -0.04933 297 PHE A CE1 
4686 C CE2 . PHE A 297 ? 0.80022 0.74912 0.56814 -0.07563 -0.01410 -0.06298 297 PHE A CE2 
4687 C CZ  . PHE A 297 ? 0.85452 0.78740 0.59230 -0.08222 -0.02803 -0.05872 297 PHE A CZ  
4697 N N   . PHE A 298 ? 0.63568 0.63494 0.48435 -0.05050 -0.00883 -0.04013 298 PHE A N   
4698 C CA  . PHE A 298 ? 0.66508 0.65808 0.50017 -0.05281 0.00442  -0.04127 298 PHE A CA  
4699 C C   . PHE A 298 ? 0.65526 0.65092 0.49299 -0.05076 0.00169  -0.03358 298 PHE A C   
4700 O O   . PHE A 298 ? 0.67159 0.65637 0.48923 -0.05526 0.00748  -0.03231 298 PHE A O   
4701 C CB  . PHE A 298 ? 0.59305 0.59450 0.44635 -0.04891 0.01964  -0.04725 298 PHE A CB  
4702 C CG  . PHE A 298 ? 0.57462 0.57031 0.42243 -0.05196 0.02598  -0.05571 298 PHE A CG  
4703 C CD1 . PHE A 298 ? 0.66981 0.64837 0.48723 -0.06024 0.02479  -0.05947 298 PHE A CD1 
4704 C CD2 . PHE A 298 ? 0.64365 0.64942 0.51539 -0.04680 0.03283  -0.05986 298 PHE A CD2 
4705 C CE1 . PHE A 298 ? 0.72540 0.69780 0.53775 -0.06334 0.03131  -0.06808 298 PHE A CE1 
4706 C CE2 . PHE A 298 ? 0.63674 0.63686 0.50534 -0.04947 0.03905  -0.06778 298 PHE A CE2 
4707 C CZ  . PHE A 298 ? 0.69324 0.67710 0.53283 -0.05774 0.03887  -0.07230 298 PHE A CZ  
4717 N N   . TYR A 299 ? 0.55911 0.56778 0.42082 -0.04443 -0.00584 -0.02875 299 TYR A N   
4718 C CA  . TYR A 299 ? 0.64290 0.65289 0.50699 -0.04286 -0.00976 -0.02157 299 TYR A CA  
4719 C C   . TYR A 299 ? 0.66471 0.66067 0.50531 -0.04848 -0.02200 -0.01610 299 TYR A C   
4720 O O   . TYR A 299 ? 0.61443 0.60213 0.44062 -0.05115 -0.02044 -0.01173 299 TYR A O   
4721 C CB  . TYR A 299 ? 0.61861 0.64340 0.51200 -0.03553 -0.01497 -0.01841 299 TYR A CB  
4722 C CG  . TYR A 299 ? 0.61479 0.64952 0.52517 -0.03040 -0.00471 -0.01946 299 TYR A CG  
4723 C CD1 . TYR A 299 ? 0.59877 0.63991 0.52070 -0.02743 0.00357  -0.02487 299 TYR A CD1 
4724 C CD2 . TYR A 299 ? 0.68239 0.71904 0.59728 -0.02871 -0.00446 -0.01487 299 TYR A CD2 
4725 C CE1 . TYR A 299 ? 0.61610 0.66494 0.55293 -0.02295 0.01036  -0.02550 299 TYR A CE1 
4726 C CE2 . TYR A 299 ? 0.58076 0.62550 0.51060 -0.02452 0.00328  -0.01623 299 TYR A CE2 
4727 C CZ  . TYR A 299 ? 0.59497 0.64559 0.53535 -0.02168 0.00987  -0.02143 299 TYR A CZ  
4728 O OH  . TYR A 299 ? 0.63831 0.69574 0.59313 -0.01767 0.01501  -0.02247 299 TYR A OH  
4738 N N   . THR A 300 ? 0.60062 0.59280 0.43742 -0.05054 -0.03509 -0.01601 300 THR A N   
4739 C CA  . THR A 300 ? 0.66406 0.64218 0.47993 -0.05566 -0.05062 -0.01005 300 THR A CA  
4740 C C   . THR A 300 ? 0.75295 0.70995 0.52786 -0.06427 -0.04525 -0.01130 300 THR A C   
4741 O O   . THR A 300 ? 0.78197 0.72606 0.53634 -0.06797 -0.05053 -0.00469 300 THR A O   
4742 C CB  . THR A 300 ? 0.63989 0.61886 0.46365 -0.05623 -0.06644 -0.01077 300 THR A CB  
4743 O OG1 . THR A 300 ? 0.66339 0.66030 0.52521 -0.04876 -0.06944 -0.00945 300 THR A OG1 
4744 C CG2 . THR A 300 ? 0.68000 0.64301 0.48218 -0.06175 -0.08563 -0.00429 300 THR A CG2 
4752 N N   . VAL A 301 ? 0.75488 0.70655 0.51677 -0.06786 -0.03401 -0.01982 301 VAL A N   
4753 C CA  A VAL A 301 ? 0.86857 0.79820 0.59010 -0.07678 -0.02582 -0.02247 301 VAL A CA  
4754 C CA  B VAL A 301 ? 0.86698 0.79652 0.58839 -0.07680 -0.02595 -0.02239 301 VAL A CA  
4755 C C   . VAL A 301 ? 0.85130 0.77972 0.57022 -0.07677 -0.00886 -0.02138 301 VAL A C   
4756 O O   . VAL A 301 ? 0.87023 0.77987 0.55768 -0.08338 -0.00625 -0.01807 301 VAL A O   
4757 C CB  A VAL A 301 ? 0.89034 0.81493 0.60229 -0.08044 -0.01667 -0.03305 301 VAL A CB  
4758 C CB  B VAL A 301 ? 0.89080 0.81484 0.60183 -0.08064 -0.01730 -0.03288 301 VAL A CB  
4759 C CG1 A VAL A 301 ? 0.99490 0.89489 0.66401 -0.09024 -0.00483 -0.03701 301 VAL A CG1 
4760 C CG1 B VAL A 301 ? 0.86411 0.80123 0.59812 -0.07612 0.00338  -0.03980 301 VAL A CG1 
4761 C CG2 A VAL A 301 ? 0.86332 0.78806 0.57793 -0.08118 -0.03413 -0.03428 301 VAL A CG2 
4762 C CG2 B VAL A 301 ? 1.01947 0.91544 0.68170 -0.09166 -0.01488 -0.03524 301 VAL A CG2 
4781 N N   . GLY A 302 ? 0.80352 0.75078 0.55513 -0.06972 0.00258  -0.02405 302 GLY A N   
4782 C CA  . GLY A 302 ? 0.85272 0.80017 0.60678 -0.06969 0.01868  -0.02418 302 GLY A CA  
4783 C C   . GLY A 302 ? 0.87297 0.81761 0.62406 -0.06936 0.01226  -0.01471 302 GLY A C   
4784 O O   . GLY A 302 ? 0.88027 0.81256 0.61318 -0.07418 0.02248  -0.01321 302 GLY A O   
4788 N N   . SER A 303 ? 0.83725 0.79258 0.60734 -0.06388 -0.00351 -0.00846 303 SER A N   
4789 C CA  . SER A 303 ? 0.85561 0.81032 0.62904 -0.06245 -0.00923 0.00022  303 SER A CA  
4790 C C   . SER A 303 ? 0.91920 0.85173 0.65758 -0.06960 -0.02009 0.00737  303 SER A C   
4791 O O   . SER A 303 ? 0.91224 0.83871 0.64555 -0.07040 -0.02097 0.01439  303 SER A O   
4792 C CB  . SER A 303 ? 0.81648 0.78918 0.62374 -0.05425 -0.02096 0.00376  303 SER A CB  
4793 O OG  . SER A 303 ? 0.86446 0.83487 0.67020 -0.05462 -0.03825 0.00626  303 SER A OG  
4799 N N   . THR A 304 ? 0.91107 0.83003 0.62416 -0.07509 -0.02893 0.00589  304 THR A N   
4800 C CA  . THR A 304 ? 1.00714 0.90264 0.68394 -0.08224 -0.04292 0.01319  304 THR A CA  
4801 C C   . THR A 304 ? 1.05286 0.92294 0.68323 -0.09260 -0.03204 0.00910  304 THR A C   
4802 O O   . THR A 304 ? 1.02362 0.86988 0.61615 -0.09991 -0.04370 0.01463  304 THR A O   
4803 C CB  . THR A 304 ? 1.00066 0.89793 0.68403 -0.08097 -0.06668 0.01587  304 THR A CB  
4804 O OG1 . THR A 304 ? 0.95138 0.84681 0.62629 -0.08385 -0.06520 0.00704  304 THR A OG1 
4805 C CG2 . THR A 304 ? 0.90333 0.82570 0.63480 -0.07095 -0.07370 0.01812  304 THR A CG2 
4813 N N   . THR A 305 ? 0.95394 0.83183 1.16421 0.00535  -0.07186 0.42636  305 THR A N   
4814 C CA  . THR A 305 ? 1.06486 0.94115 1.19490 0.00985  -0.07057 0.44273  305 THR A CA  
4815 C C   . THR A 305 ? 0.96275 0.83997 1.09902 0.00509  -0.03630 0.45423  305 THR A C   
4816 O O   . THR A 305 ? 0.98972 0.87249 1.15096 -0.00231 -0.01468 0.43781  305 THR A O   
4817 C CB  . THR A 305 ? 1.14412 1.02794 1.22169 0.01120  -0.07770 0.41793  305 THR A CB  
4818 O OG1 . THR A 305 ? 1.11159 0.99321 1.17506 0.01706  -0.11469 0.41285  305 THR A OG1 
4819 C CG2 . THR A 305 ? 1.24322 1.12800 1.24173 0.01585  -0.06389 0.42592  305 THR A CG2 
4827 N N   . PRO A 306 ? 1.06339 0.93519 1.18118 0.00901  -0.03055 0.48181  306 PRO A N   
4828 C CA  . PRO A 306 ? 1.12361 0.99852 1.26167 0.00384  0.00257  0.49311  306 PRO A CA  
4829 C C   . PRO A 306 ? 1.21897 1.10249 1.31815 0.00212  0.02585  0.48492  306 PRO A C   
4830 O O   . PRO A 306 ? 1.24496 1.13507 1.39215 -0.00704 0.04650  0.46985  306 PRO A O   
4831 C CB  . PRO A 306 ? 1.15388 1.02076 1.25992 0.01135  0.00036  0.52702  306 PRO A CB  
4832 C CG  . PRO A 306 ? 1.14570 1.00438 1.25247 0.01701  -0.03435 0.53001  306 PRO A CG  
4833 C CD  . PRO A 306 ? 1.00654 0.86859 1.09268 0.01814  -0.05489 0.50360  306 PRO A CD  
4841 N N   . ASN A 307 ? 1.28531 1.16837 1.29784 0.01171  0.02178  0.49215  307 ASN A N   
4842 C CA  . ASN A 307 ? 1.28118 1.17440 1.25222 0.01235  0.04527  0.48351  307 ASN A CA  
4843 C C   . ASN A 307 ? 1.10595 1.00557 1.05854 0.01164  0.02848  0.44711  307 ASN A C   
4844 O O   . ASN A 307 ? 1.23379 1.13418 1.11300 0.02054  0.01755  0.43524  307 ASN A O   
4845 C CB  . ASN A 307 ? 1.28387 1.17294 1.16835 0.02508  0.05363  0.50343  307 ASN A CB  
4846 C CG  . ASN A 307 ? 1.20731 1.09652 1.11598 0.02352  0.08172  0.52993  307 ASN A CG  
4847 O OD1 . ASN A 307 ? 1.15528 1.05643 1.10571 0.01626  0.11216  0.52774  307 ASN A OD1 
4848 N ND2 . ASN A 307 ? 1.18676 1.06288 1.07295 0.03047  0.06987  0.55572  307 ASN A ND2 
4855 N N   . PHE A 308 ? 1.15424 1.05798 1.17541 0.00128  0.02603  0.42007  308 PHE A N   
4856 C CA  . PHE A 308 ? 1.11123 1.02166 1.12555 -0.00009 0.00920  0.37944  308 PHE A CA  
4857 C C   . PHE A 308 ? 1.14116 1.06326 1.11640 -0.00029 0.02513  0.35539  308 PHE A C   
4858 O O   . PHE A 308 ? 1.08686 1.01236 1.02228 0.00370  0.00883  0.33134  308 PHE A O   
4859 C CB  . PHE A 308 ? 1.11351 1.02441 1.20604 -0.00881 0.00789  0.35929  308 PHE A CB  
4860 C CG  . PHE A 308 ? 0.94813 0.86795 1.04029 -0.01106 0.00015  0.31928  308 PHE A CG  
4861 C CD1 . PHE A 308 ? 0.99049 0.91134 1.05039 -0.00540 -0.02597 0.30860  308 PHE A CD1 
4862 C CD2 . PHE A 308 ? 0.94891 0.87517 1.07562 -0.01859 0.01728  0.29357  308 PHE A CD2 
4863 C CE1 . PHE A 308 ? 0.94484 0.87422 1.00928 -0.00745 -0.03136 0.27571  308 PHE A CE1 
4864 C CE2 . PHE A 308 ? 0.91958 0.85354 1.04323 -0.01965 0.01088  0.26025  308 PHE A CE2 
4865 C CZ  . PHE A 308 ? 0.88475 0.82090 0.97860 -0.01419 -0.01175 0.25265  308 PHE A CZ  
4875 N N   . HIS A 309 ? 1.11993 1.04836 1.11268 -0.00495 0.05634  0.36202  309 HIS A N   
4876 C CA  . HIS A 309 ? 1.21252 1.15338 1.18079 -0.00554 0.07298  0.33928  309 HIS A CA  
4877 C C   . HIS A 309 ? 1.26613 1.20746 1.15295 0.00694  0.08176  0.35275  309 HIS A C   
4878 O O   . HIS A 309 ? 1.13477 1.08611 0.99807 0.00860  0.09646  0.33456  309 HIS A O   
4879 C CB  . HIS A 309 ? 1.18765 1.13587 1.21890 -0.01599 0.10101  0.33923  309 HIS A CB  
4880 C CG  . HIS A 309 ? 1.32328 1.27195 1.41771 -0.02618 0.09270  0.30985  309 HIS A CG  
4881 N ND1 . HIS A 309 ? 1.33159 1.27001 1.46154 -0.02788 0.07461  0.30810  309 HIS A ND1 
4882 C CD2 . HIS A 309 ? 1.18436 1.14137 1.30957 -0.03351 0.09999  0.28103  309 HIS A CD2 
4883 C CE1 . HIS A 309 ? 1.20500 1.14457 1.37902 -0.03462 0.07320  0.27872  309 HIS A CE1 
4884 N NE2 . HIS A 309 ? 1.10808 1.05828 1.27862 -0.03841 0.08649  0.26196  309 HIS A NE2 
4892 N N   . ARG A 310 ? 1.13719 1.06684 0.97813 0.01719  0.07260  0.38340  310 ARG A N   
4893 C CA  . ARG A 310 ? 1.26585 1.19218 1.01914 0.03235  0.08156  0.39769  310 ARG A CA  
4894 C C   . ARG A 310 ? 1.31157 1.22816 0.99268 0.04357  0.04533  0.37844  310 ARG A C   
4895 O O   . ARG A 310 ? 1.50520 1.41250 1.10324 0.05916  0.04385  0.39107  310 ARG A O   
4896 C CB  . ARG A 310 ? 1.25534 1.17290 0.99427 0.03900  0.09609  0.44755  310 ARG A CB  
4897 C CG  . ARG A 310 ? 1.14102 1.06612 0.95914 0.02752  0.12909  0.46711  310 ARG A CG  
4898 C CD  . ARG A 310 ? 1.22216 1.13976 1.01899 0.03400  0.14197  0.49835  310 ARG A CD  
4899 N NE  . ARG A 310 ? 1.20924 1.13502 1.08830 0.02335  0.16886  0.51292  310 ARG A NE  
4900 C CZ  . ARG A 310 ? 1.18725 1.12751 1.08864 0.02114  0.20287  0.51314  310 ARG A CZ  
4901 N NH1 . ARG A 310 ? 1.20825 1.15709 1.05732 0.02856  0.21797  0.49862  310 ARG A NH1 
4902 N NH2 . ARG A 310 ? 1.10439 1.05102 1.08702 0.01204  0.22065  0.52698  310 ARG A NH2 
4916 N N   . MET A 311 ? 1.34670 1.26423 1.05833 0.03683  0.01600  0.34834  311 MET A N   
4917 C CA  . MET A 311 ? 1.47252 1.37967 1.13346 0.04562  -0.02377 0.33262  311 MET A CA  
4918 C C   . MET A 311 ? 1.55419 1.46402 1.16018 0.05274  -0.02492 0.30045  311 MET A C   
4919 O O   . MET A 311 ? 1.51832 1.41688 1.07504 0.06184  -0.05870 0.28655  311 MET A O   
4920 C CB  . MET A 311 ? 1.41895 1.32704 1.14422 0.03600  -0.05293 0.31748  311 MET A CB  
4921 C CG  . MET A 311 ? 1.27646 1.18445 1.07620 0.02696  -0.04671 0.33967  311 MET A CG  
4922 S SD  . MET A 311 ? 1.80916 1.70031 1.60080 0.03442  -0.08094 0.37326  311 MET A SD  
4923 C CE  . MET A 311 ? 1.21209 1.10677 1.07455 0.02711  -0.11136 0.35028  311 MET A CE  
4933 N N   . ALA A 312 ? 1.38403 1.30743 1.00165 0.04906  0.00860  0.28784  312 ALA A N   
4934 C CA  . ALA A 312 ? 1.44683 1.37377 1.02263 0.05544  0.01023  0.25648  312 ALA A CA  
4935 C C   . ALA A 312 ? 1.51846 1.44688 1.03788 0.06776  0.04632  0.26904  312 ALA A C   
4936 O O   . ALA A 312 ? 1.50324 1.44342 1.02712 0.06753  0.06995  0.25078  312 ALA A O   
4937 C CB  . ALA A 312 ? 1.23948 1.18218 0.88092 0.04162  0.01636  0.22718  312 ALA A CB  
4943 N N   . GLY A 313 ? 1.38163 1.29831 0.84813 0.07975  0.05209  0.30230  313 GLY A N   
4944 C CA  . GLY A 313 ? 1.63404 1.55152 1.04252 0.09423  0.09041  0.31979  313 GLY A CA  
4945 C C   . GLY A 313 ? 1.61882 1.55704 1.09378 0.08388  0.13721  0.33001  313 GLY A C   
4946 O O   . GLY A 313 ? 1.44408 1.38526 0.91834 0.08782  0.17140  0.36616  313 GLY A O   
4950 N N   . ASN A 325 ? 1.27773 1.46517 1.41681 0.05501  0.44109  0.15267  325 ASN A N   
4951 C CA  . ASN A 325 ? 1.28883 1.45819 1.38320 0.04733  0.40640  0.14548  325 ASN A CA  
4952 C C   . ASN A 325 ? 1.11229 1.28385 1.28480 0.02318  0.37125  0.13744  325 ASN A C   
4953 O O   . ASN A 325 ? 1.05328 1.21268 1.20325 0.01632  0.33044  0.11266  325 ASN A O   
4954 C CB  . ASN A 325 ? 1.31769 1.47459 1.35547 0.05412  0.42214  0.17736  325 ASN A CB  
4955 C CG  . ASN A 325 ? 1.28535 1.41953 1.26289 0.04972  0.37962  0.16599  325 ASN A CG  
4956 O OD1 . ASN A 325 ? 1.26161 1.38643 1.20517 0.05036  0.34635  0.13364  325 ASN A OD1 
4957 N ND2 . ASN A 325 ? 1.28228 1.40799 1.25251 0.04541  0.38118  0.19453  325 ASN A ND2 
4964 N N   . PRO A 326 ? 1.07861 1.26454 1.34315 0.01123  0.38660  0.15812  326 PRO A N   
4965 C CA  . PRO A 326 ? 0.99615 1.18070 1.33034 -0.00980 0.35042  0.14655  326 PRO A CA  
4966 C C   . PRO A 326 ? 0.88355 1.07000 1.23186 -0.01447 0.31703  0.11002  326 PRO A C   
4967 O O   . PRO A 326 ? 0.75269 0.92791 1.10336 -0.02571 0.27846  0.09250  326 PRO A O   
4968 C CB  . PRO A 326 ? 0.91441 1.11260 1.34516 -0.01817 0.37077  0.17096  326 PRO A CB  
4969 C CG  . PRO A 326 ? 1.05455 1.24958 1.44429 -0.00392 0.40464  0.20007  326 PRO A CG  
4970 C CD  . PRO A 326 ? 1.12381 1.31641 1.41670 0.01603  0.42070  0.19017  326 PRO A CD  
4978 N N   . GLU A 327 ? 0.94027 1.14045 1.29902 -0.00503 0.33224  0.09927  327 GLU A N   
4979 C CA  . GLU A 327 ? 0.77606 0.98023 1.16453 -0.01054 0.30144  0.06921  327 GLU A CA  
4980 C C   . GLU A 327 ? 0.76205 0.94803 1.07822 -0.00933 0.26494  0.04384  327 GLU A C   
4981 O O   . GLU A 327 ? 0.73520 0.91698 1.07209 -0.01983 0.22935  0.02563  327 GLU A O   
4982 C CB  . GLU A 327 ? 0.87466 1.09665 1.28875 0.00126  0.32741  0.06437  327 GLU A CB  
4983 C CG  . GLU A 327 ? 1.03327 1.26130 1.48529 -0.00302 0.29778  0.03635  327 GLU A CG  
4984 C CD  . GLU A 327 ? 0.98058 1.20610 1.49046 -0.02233 0.25754  0.02818  327 GLU A CD  
4985 O OE1 . GLU A 327 ? 0.97427 1.18284 1.44814 -0.02982 0.23202  0.02423  327 GLU A OE1 
4986 O OE2 . GLU A 327 ? 1.16494 1.40476 1.75678 -0.02888 0.25043  0.02469  327 GLU A OE2 
4993 N N   . PHE A 328 ? 0.98329 1.15766 1.21496 0.00409  0.27251  0.04308  328 PHE A N   
4994 C CA  . PHE A 328 ? 0.98847 1.14632 1.16110 0.00488  0.23756  0.02099  328 PHE A CA  
4995 C C   . PHE A 328 ? 0.80822 0.95499 0.98916 -0.00967 0.20836  0.02256  328 PHE A C   
4996 O O   . PHE A 328 ? 0.72183 0.86216 0.89896 -0.01523 0.17627  0.00354  328 PHE A O   
4997 C CB  . PHE A 328 ? 1.11576 1.26060 1.20017 0.02129  0.24728  0.02145  328 PHE A CB  
4998 C CG  . PHE A 328 ? 1.17072 1.32026 1.23163 0.03844  0.26653  0.00832  328 PHE A CG  
4999 C CD1 . PHE A 328 ? 1.18127 1.34218 1.28876 0.03747  0.26027  -0.01070 328 PHE A CD1 
5000 C CD2 . PHE A 328 ? 1.31969 1.46051 1.30929 0.05703  0.29007  0.01441  328 PHE A CD2 
5001 C CE1 . PHE A 328 ? 1.17091 1.33499 1.26018 0.05438  0.27881  -0.02392 328 PHE A CE1 
5002 C CE2 . PHE A 328 ? 1.27628 1.41866 1.24020 0.07517  0.30865  -0.00065 328 PHE A CE2 
5003 C CZ  . PHE A 328 ? 1.34575 1.50007 1.36251 0.07367  0.30378  -0.02017 328 PHE A CZ  
5013 N N   . LEU A 329 ? 0.71052 0.85461 0.90444 -0.01492 0.22084  0.04615  329 LEU A N   
5014 C CA  . LEU A 329 ? 0.70312 0.83563 0.90916 -0.02728 0.19557  0.04668  329 LEU A CA  
5015 C C   . LEU A 329 ? 0.59956 0.73703 0.87251 -0.03981 0.17468  0.03271  329 LEU A C   
5016 O O   . LEU A 329 ? 0.51713 0.64370 0.78314 -0.04589 0.14518  0.01853  329 LEU A O   
5017 C CB  . LEU A 329 ? 0.72410 0.85245 0.93826 -0.02978 0.21440  0.07600  329 LEU A CB  
5018 C CG  . LEU A 329 ? 0.73975 0.85465 0.97149 -0.04132 0.19131  0.07730  329 LEU A CG  
5019 C CD1 . LEU A 329 ? 0.76559 0.86453 0.92916 -0.03647 0.17335  0.07323  329 LEU A CD1 
5020 C CD2 . LEU A 329 ? 0.74675 0.86246 1.02582 -0.04726 0.21151  0.10605  329 LEU A CD2 
5032 N N   . ALA A 330 ? 0.62790 0.78110 0.96635 -0.04284 0.18937  0.03720  330 ALA A N   
5033 C CA  . ALA A 330 ? 0.60362 0.75992 1.00750 -0.05435 0.16538  0.02378  330 ALA A CA  
5034 C C   . ALA A 330 ? 0.54099 0.69527 0.92316 -0.05258 0.13661  -0.00306 330 ALA A C   
5035 O O   . ALA A 330 ? 0.48554 0.63055 0.87614 -0.05964 0.10600  -0.01740 330 ALA A O   
5036 C CB  . ALA A 330 ? 0.54784 0.72305 1.03353 -0.05738 0.18650  0.03575  330 ALA A CB  
5042 N N   . ALA A 331 ? 0.57085 0.73230 0.92341 -0.04198 0.14638  -0.00987 331 ALA A N   
5043 C CA  . ALA A 331 ? 0.52964 0.68889 0.86386 -0.03982 0.12013  -0.03225 331 ALA A CA  
5044 C C   . ALA A 331 ? 0.51776 0.65941 0.79515 -0.04046 0.09678  -0.03974 331 ALA A C   
5045 O O   . ALA A 331 ? 0.43128 0.56761 0.70987 -0.04419 0.06941  -0.05337 331 ALA A O   
5046 C CB  . ALA A 331 ? 0.54025 0.70805 0.85464 -0.02725 0.13668  -0.03783 331 ALA A CB  
5052 N N   . TRP A 332 ? 0.56503 0.69775 0.79363 -0.03592 0.10785  -0.02930 332 TRP A N   
5053 C CA  . TRP A 332 ? 0.56251 0.67984 0.74719 -0.03671 0.08813  -0.03280 332 TRP A CA  
5054 C C   . TRP A 332 ? 0.55330 0.66275 0.76416 -0.04656 0.07245  -0.03312 332 TRP A C   
5055 O O   . TRP A 332 ? 0.50977 0.61079 0.70566 -0.04775 0.05027  -0.04422 332 TRP A O   
5056 C CB  . TRP A 332 ? 0.59545 0.70525 0.73213 -0.03022 0.10258  -0.01878 332 TRP A CB  
5057 C CG  . TRP A 332 ? 0.68655 0.78200 0.78361 -0.03005 0.08399  -0.01978 332 TRP A CG  
5058 C CD1 . TRP A 332 ? 0.65606 0.74591 0.71815 -0.02482 0.06743  -0.03073 332 TRP A CD1 
5059 C CD2 . TRP A 332 ? 0.64064 0.72590 0.73665 -0.03500 0.08072  -0.00808 332 TRP A CD2 
5060 N NE1 . TRP A 332 ? 0.67602 0.75444 0.71785 -0.02633 0.05500  -0.02539 332 TRP A NE1 
5061 C CE2 . TRP A 332 ? 0.67429 0.74953 0.73466 -0.03205 0.06323  -0.01207 332 TRP A CE2 
5062 C CE3 . TRP A 332 ? 0.64136 0.72472 0.76934 -0.04156 0.09065  0.00588  332 TRP A CE3 
5063 C CZ2 . TRP A 332 ? 0.67872 0.74309 0.73354 -0.03466 0.05677  -0.00279 332 TRP A CZ2 
5064 C CZ3 . TRP A 332 ? 0.63568 0.70645 0.75536 -0.04410 0.08315  0.01382  332 TRP A CZ3 
5065 C CH2 . TRP A 332 ? 0.62675 0.68865 0.70957 -0.04026 0.06704  0.00932  332 TRP A CH2 
5076 N N   . ARG A 333 ? 0.54074 0.65215 0.79249 -0.05265 0.08462  -0.02100 333 ARG A N   
5077 C CA  . ARG A 333 ? 0.57838 0.67944 0.85868 -0.06116 0.06918  -0.02371 333 ARG A CA  
5078 C C   . ARG A 333 ? 0.55629 0.65691 0.86041 -0.06456 0.04329  -0.04399 333 ARG A C   
5079 O O   . ARG A 333 ? 0.43986 0.52672 0.73308 -0.06626 0.02277  -0.05466 333 ARG A O   
5080 C CB  . ARG A 333 ? 0.58534 0.69005 0.91824 -0.06734 0.08722  -0.00628 333 ARG A CB  
5081 C CG  . ARG A 333 ? 0.76648 0.85545 1.11710 -0.07402 0.07733  -0.00343 333 ARG A CG  
5082 C CD  . ARG A 333 ? 0.75675 0.85016 1.18282 -0.08252 0.08692  0.00858  333 ARG A CD  
5083 N NE  . ARG A 333 ? 0.88062 0.98660 1.31655 -0.07985 0.12174  0.03591  333 ARG A NE  
5084 C CZ  . ARG A 333 ? 0.85116 0.97495 1.33657 -0.08063 0.14114  0.04585  333 ARG A CZ  
5085 N NH1 . ARG A 333 ? 0.73071 0.86266 1.26817 -0.08549 0.12617  0.03065  333 ARG A NH1 
5086 N NH2 . ARG A 333 ? 0.86995 1.00354 1.35257 -0.07530 0.17695  0.07291  333 ARG A NH2 
5100 N N   . GLU A 334 ? 0.53282 0.64763 0.86899 -0.06433 0.04421  -0.04904 334 GLU A N   
5101 C CA  . GLU A 334 ? 0.50126 0.61658 0.86761 -0.06762 0.01827  -0.06565 334 GLU A CA  
5102 C C   . GLU A 334 ? 0.47673 0.59316 0.80621 -0.06110 0.00352  -0.07789 334 GLU A C   
5103 O O   . GLU A 334 ? 0.46691 0.58654 0.81984 -0.06201 -0.01628 -0.08909 334 GLU A O   
5104 C CB  . GLU A 334 ? 0.47403 0.60508 0.91272 -0.07216 0.02593  -0.06156 334 GLU A CB  
5105 C CG  . GLU A 334 ? 0.51541 0.64666 1.00089 -0.07906 0.04270  -0.04536 334 GLU A CG  
5106 C CD  . GLU A 334 ? 0.44875 0.59747 1.01766 -0.08385 0.05246  -0.03794 334 GLU A CD  
5107 O OE1 . GLU A 334 ? 0.45876 0.62292 1.04170 -0.07929 0.05860  -0.04047 334 GLU A OE1 
5108 O OE2 . GLU A 334 ? 0.59540 0.74210 1.22132 -0.09212 0.05385  -0.02900 334 GLU A OE2 
5115 N N   . ALA A 335 ? 0.42031 0.53362 0.69713 -0.05465 0.01089  -0.07483 335 ALA A N   
5116 C CA  . ALA A 335 ? 0.52829 0.64037 0.77322 -0.04899 -0.00396 -0.08402 335 ALA A CA  
5117 C C   . ALA A 335 ? 0.49847 0.62439 0.77305 -0.04661 -0.00620 -0.09018 335 ALA A C   
5118 O O   . ALA A 335 ? 0.53676 0.66227 0.81461 -0.04560 -0.02724 -0.09898 335 ALA A O   
5119 C CB  . ALA A 335 ? 0.49280 0.59173 0.72086 -0.04977 -0.02813 -0.09246 335 ALA A CB  
5125 N N   . ARG A 336 ? 0.49854 0.63659 0.79467 -0.04444 0.01730  -0.08414 336 ARG A N   
5126 C CA  . ARG A 336 ? 0.40164 0.55363 0.72977 -0.04039 0.02044  -0.08947 336 ARG A CA  
5127 C C   . ARG A 336 ? 0.41479 0.57147 0.71840 -0.03081 0.04591  -0.08666 336 ARG A C   
5128 O O   . ARG A 336 ? 0.45513 0.62487 0.79105 -0.02658 0.06647  -0.08457 336 ARG A O   
5129 C CB  . ARG A 336 ? 0.48612 0.65020 0.88500 -0.04634 0.02318  -0.08697 336 ARG A CB  
5130 C CG  . ARG A 336 ? 0.46379 0.63275 0.88647 -0.04928 0.05112  -0.07184 336 ARG A CG  
5131 C CD  . ARG A 336 ? 0.50492 0.68789 1.01197 -0.05550 0.05268  -0.06823 336 ARG A CD  
5132 N NE  . ARG A 336 ? 0.46736 0.65269 1.00623 -0.06078 0.07488  -0.05103 336 ARG A NE  
5133 C CZ  . ARG A 336 ? 0.54001 0.73639 1.08562 -0.05523 0.11365  -0.03410 336 ARG A CZ  
5134 N NH1 . ARG A 336 ? 0.52593 0.73087 1.04658 -0.04329 0.13458  -0.03534 336 ARG A NH1 
5135 N NH2 . ARG A 336 ? 0.57424 0.77179 1.15121 -0.06058 0.13237  -0.01524 336 ARG A NH2 
5149 N N   . THR A 337 ? 0.47918 0.62447 0.72617 -0.02611 0.04425  -0.08731 337 THR A N   
5150 C CA  . THR A 337 ? 0.50050 0.64521 0.71426 -0.01533 0.06185  -0.08875 337 THR A CA  
5151 C C   . THR A 337 ? 0.53457 0.68266 0.75447 -0.00798 0.05378  -0.10275 337 THR A C   
5152 O O   . THR A 337 ? 0.55340 0.70219 0.75682 0.00283  0.07033  -0.10791 337 THR A O   
5153 C CB  . THR A 337 ? 0.48277 0.61233 0.63846 -0.01318 0.05705  -0.08531 337 THR A CB  
5154 O OG1 . THR A 337 ? 0.49459 0.61649 0.63703 -0.01455 0.03066  -0.09287 337 THR A OG1 
5155 C CG2 . THR A 337 ? 0.49518 0.61993 0.64760 -0.02033 0.06277  -0.07102 337 THR A CG2 
5163 N N   . GLY A 338 ? 0.50079 0.64952 0.74205 -0.01223 0.02890  -0.10898 338 GLY A N   
5164 C CA  . GLY A 338 ? 0.53011 0.68046 0.78031 -0.00573 0.01827  -0.12027 338 GLY A CA  
5165 C C   . GLY A 338 ? 0.51205 0.64892 0.72095 -0.00193 0.00295  -0.12482 338 GLY A C   
5166 O O   . GLY A 338 ? 0.45212 0.58821 0.67049 0.00351  -0.00727 -0.13380 338 GLY A O   
5170 N N   . PHE A 339 ? 0.46208 0.58846 0.63253 -0.00461 0.00061  -0.11814 339 PHE A N   
5171 C CA  . PHE A 339 ? 0.49193 0.60646 0.63402 -0.00276 -0.01649 -0.11947 339 PHE A CA  
5172 C C   . PHE A 339 ? 0.45280 0.56455 0.59651 -0.01038 -0.03253 -0.11047 339 PHE A C   
5173 O O   . PHE A 339 ? 0.47577 0.58396 0.60500 -0.01511 -0.02789 -0.10231 339 PHE A O   
5174 C CB  . PHE A 339 ? 0.55000 0.65417 0.64889 0.00156  -0.00853 -0.11802 339 PHE A CB  
5175 C CG  . PHE A 339 ? 0.61646 0.72043 0.70053 0.01211  0.00940  -0.12712 339 PHE A CG  
5176 C CD1 . PHE A 339 ? 0.61056 0.70836 0.68914 0.02163  0.00184  -0.14251 339 PHE A CD1 
5177 C CD2 . PHE A 339 ? 0.67953 0.78831 0.75504 0.01381  0.03501  -0.11990 339 PHE A CD2 
5178 C CE1 . PHE A 339 ? 0.66839 0.76355 0.72632 0.03426  0.01988  -0.15339 339 PHE A CE1 
5179 C CE2 . PHE A 339 ? 0.77520 0.88333 0.83076 0.02622  0.05563  -0.12674 339 PHE A CE2 
5180 C CZ  . PHE A 339 ? 0.74717 0.84783 0.79041 0.03732  0.04830  -0.14498 339 PHE A CZ  
5190 N N   . PRO A 340 ? 0.47105 0.58331 0.63035 -0.01054 -0.05005 -0.11075 340 PRO A N   
5191 C CA  . PRO A 340 ? 0.46036 0.56999 0.61664 -0.01522 -0.06181 -0.10193 340 PRO A CA  
5192 C C   . PRO A 340 ? 0.46404 0.56447 0.59051 -0.01677 -0.06047 -0.09295 340 PRO A C   
5193 O O   . PRO A 340 ? 0.52856 0.62614 0.64734 -0.02014 -0.05999 -0.08813 340 PRO A O   
5194 C CB  . PRO A 340 ? 0.43331 0.54371 0.60517 -0.01230 -0.07861 -0.10074 340 PRO A CB  
5195 C CG  . PRO A 340 ? 0.43710 0.55475 0.63741 -0.00845 -0.07603 -0.11171 340 PRO A CG  
5196 C CD  . PRO A 340 ? 0.45305 0.56908 0.63745 -0.00545 -0.05805 -0.11885 340 PRO A CD  
5204 N N   . TRP A 341 ? 0.46305 0.55776 0.57525 -0.01381 -0.06123 -0.09167 341 TRP A N   
5205 C CA  . TRP A 341 ? 0.43644 0.52352 0.52811 -0.01508 -0.06071 -0.08182 341 TRP A CA  
5206 C C   . TRP A 341 ? 0.50095 0.58658 0.57933 -0.01827 -0.04707 -0.07968 341 TRP A C   
5207 O O   . TRP A 341 ? 0.53475 0.61606 0.60567 -0.02068 -0.04554 -0.07206 341 TRP A O   
5208 C CB  . TRP A 341 ? 0.46092 0.54172 0.54601 -0.01145 -0.06794 -0.08249 341 TRP A CB  
5209 C CG  . TRP A 341 ? 0.49242 0.56615 0.56394 -0.01242 -0.06943 -0.07185 341 TRP A CG  
5210 C CD1 . TRP A 341 ? 0.48315 0.55038 0.53545 -0.01104 -0.06822 -0.07230 341 TRP A CD1 
5211 C CD2 . TRP A 341 ? 0.48701 0.55953 0.56495 -0.01363 -0.07228 -0.05807 341 TRP A CD2 
5212 N NE1 . TRP A 341 ? 0.51299 0.57569 0.56502 -0.01245 -0.07227 -0.05987 341 TRP A NE1 
5213 C CE2 . TRP A 341 ? 0.53611 0.60254 0.60536 -0.01376 -0.07275 -0.05096 341 TRP A CE2 
5214 C CE3 . TRP A 341 ? 0.42344 0.49906 0.51160 -0.01315 -0.07345 -0.05006 341 TRP A CE3 
5215 C CZ2 . TRP A 341 ? 0.49387 0.55878 0.57171 -0.01375 -0.07238 -0.03620 341 TRP A CZ2 
5216 C CZ3 . TRP A 341 ? 0.47018 0.54338 0.55917 -0.01190 -0.07077 -0.03534 341 TRP A CZ3 
5217 C CH2 . TRP A 341 ? 0.45917 0.52785 0.54674 -0.01237 -0.06930 -0.02859 341 TRP A CH2 
5228 N N   . ILE A 342 ? 0.50860 0.59740 0.58560 -0.01736 -0.03533 -0.08529 342 ILE A N   
5229 C CA  . ILE A 342 ? 0.45802 0.54586 0.52765 -0.02041 -0.02081 -0.07968 342 ILE A CA  
5230 C C   . ILE A 342 ? 0.47971 0.57098 0.57116 -0.02611 -0.01970 -0.07938 342 ILE A C   
5231 O O   . ILE A 342 ? 0.48453 0.57016 0.57237 -0.02963 -0.01683 -0.07348 342 ILE A O   
5232 C CB  . ILE A 342 ? 0.48461 0.57570 0.54708 -0.01615 -0.00503 -0.08276 342 ILE A CB  
5233 C CG1 . ILE A 342 ? 0.55605 0.63857 0.58712 -0.00892 -0.01015 -0.08563 342 ILE A CG1 
5234 C CG2 . ILE A 342 ? 0.54050 0.63246 0.60415 -0.01976 0.01227  -0.07288 342 ILE A CG2 
5235 C CD1 . ILE A 342 ? 0.67722 0.74984 0.68367 -0.00981 -0.01381 -0.07478 342 ILE A CD1 
5247 N N   . ASP A 343 ? 0.42399 0.52320 0.54091 -0.02664 -0.02412 -0.08681 343 ASP A N   
5248 C CA  . ASP A 343 ? 0.40091 0.50185 0.54139 -0.03176 -0.02819 -0.08894 343 ASP A CA  
5249 C C   . ASP A 343 ? 0.47053 0.56195 0.59571 -0.03196 -0.04234 -0.08809 343 ASP A C   
5250 O O   . ASP A 343 ? 0.49569 0.58134 0.62606 -0.03525 -0.04493 -0.08992 343 ASP A O   
5251 C CB  . ASP A 343 ? 0.42422 0.53583 0.59873 -0.03158 -0.03348 -0.09652 343 ASP A CB  
5252 C CG  . ASP A 343 ? 0.46545 0.58733 0.65918 -0.02968 -0.01405 -0.09714 343 ASP A CG  
5253 O OD1 . ASP A 343 ? 0.51198 0.63220 0.69273 -0.02963 0.00381  -0.09033 343 ASP A OD1 
5254 O OD2 . ASP A 343 ? 0.44799 0.57932 0.66943 -0.02712 -0.01552 -0.10324 343 ASP A OD2 
5259 N N   . ALA A 344 ? 0.42098 0.50977 0.52892 -0.02753 -0.05094 -0.08528 344 ALA A N   
5260 C CA  . ALA A 344 ? 0.45101 0.53111 0.54032 -0.02507 -0.05906 -0.08172 344 ALA A CA  
5261 C C   . ALA A 344 ? 0.45392 0.52495 0.52675 -0.02564 -0.04959 -0.07622 344 ALA A C   
5262 O O   . ALA A 344 ? 0.46792 0.53007 0.53087 -0.02439 -0.05205 -0.07833 344 ALA A O   
5263 C CB  . ALA A 344 ? 0.45953 0.54053 0.54107 -0.01995 -0.06611 -0.07495 344 ALA A CB  
5269 N N   . ILE A 345 ? 0.45120 0.52280 0.51974 -0.02631 -0.04023 -0.06995 345 ILE A N   
5270 C CA  . ILE A 345 ? 0.44049 0.50395 0.49855 -0.02677 -0.03226 -0.06287 345 ILE A CA  
5271 C C   . ILE A 345 ? 0.46248 0.52245 0.53230 -0.03152 -0.02615 -0.06658 345 ILE A C   
5272 O O   . ILE A 345 ? 0.53616 0.58622 0.60252 -0.03121 -0.02505 -0.06657 345 ILE A O   
5273 C CB  . ILE A 345 ? 0.52832 0.59234 0.57884 -0.02596 -0.02810 -0.05489 345 ILE A CB  
5274 C CG1 . ILE A 345 ? 0.49574 0.56124 0.54400 -0.02190 -0.03748 -0.05122 345 ILE A CG1 
5275 C CG2 . ILE A 345 ? 0.47156 0.52755 0.51607 -0.02655 -0.02118 -0.04576 345 ILE A CG2 
5276 C CD1 . ILE A 345 ? 0.44174 0.50616 0.48411 -0.02056 -0.04049 -0.04822 345 ILE A CD1 
5288 N N   . MET A 346 ? 0.44297 0.51055 0.53103 -0.03532 -0.02110 -0.06939 346 MET A N   
5289 C CA  . MET A 346 ? 0.46025 0.52581 0.57106 -0.04073 -0.01519 -0.07034 346 MET A CA  
5290 C C   . MET A 346 ? 0.50854 0.56758 0.63074 -0.04184 -0.02922 -0.08194 346 MET A C   
5291 O O   . MET A 346 ? 0.51775 0.56784 0.65405 -0.04510 -0.02956 -0.08454 346 MET A O   
5292 C CB  . MET A 346 ? 0.45828 0.53568 0.59181 -0.04329 -0.00407 -0.06855 346 MET A CB  
5293 C CG  . MET A 346 ? 0.43317 0.51318 0.54684 -0.04009 0.01046  -0.05823 346 MET A CG  
5294 S SD  . MET A 346 ? 0.50172 0.57005 0.59804 -0.04076 0.01804  -0.04362 346 MET A SD  
5295 C CE  . MET A 346 ? 0.48686 0.55723 0.62214 -0.04741 0.03302  -0.03594 346 MET A CE  
5305 N N   . THR A 347 ? 0.45496 0.51648 0.57057 -0.03844 -0.04297 -0.08933 347 THR A N   
5306 C CA  . THR A 347 ? 0.45336 0.50520 0.56707 -0.03683 -0.05987 -0.10093 347 THR A CA  
5307 C C   . THR A 347 ? 0.47898 0.51540 0.56011 -0.03071 -0.05940 -0.10097 347 THR A C   
5308 O O   . THR A 347 ? 0.50153 0.52424 0.58165 -0.02980 -0.06716 -0.11138 347 THR A O   
5309 C CB  . THR A 347 ? 0.47850 0.53644 0.58930 -0.03333 -0.07466 -0.10532 347 THR A CB  
5310 O OG1 . THR A 347 ? 0.51681 0.58897 0.66460 -0.03813 -0.07397 -0.10653 347 THR A OG1 
5311 C CG2 . THR A 347 ? 0.46458 0.51009 0.56303 -0.02947 -0.09504 -0.11708 347 THR A CG2 
5319 N N   . GLN A 348 ? 0.43316 0.47104 0.49164 -0.02592 -0.05047 -0.09005 348 GLN A N   
5320 C CA  . GLN A 348 ? 0.51713 0.54253 0.55092 -0.01897 -0.04526 -0.08744 348 GLN A CA  
5321 C C   . GLN A 348 ? 0.48360 0.49978 0.52933 -0.02227 -0.03688 -0.08775 348 GLN A C   
5322 O O   . GLN A 348 ? 0.48372 0.48478 0.51784 -0.01705 -0.03743 -0.09499 348 GLN A O   
5323 C CB  . GLN A 348 ? 0.49927 0.53088 0.52104 -0.01460 -0.03700 -0.07249 348 GLN A CB  
5324 C CG  . GLN A 348 ? 0.57956 0.60109 0.58032 -0.00532 -0.02906 -0.06722 348 GLN A CG  
5325 C CD  . GLN A 348 ? 0.52555 0.55475 0.52802 -0.00212 -0.02157 -0.04994 348 GLN A CD  
5326 O OE1 . GLN A 348 ? 0.49484 0.53266 0.51330 -0.00770 -0.02221 -0.04317 348 GLN A OE1 
5327 N NE2 . GLN A 348 ? 0.52939 0.55446 0.51608 0.00787  -0.01453 -0.04268 348 GLN A NE2 
5336 N N   . LEU A 349 ? 0.51292 0.53676 0.58057 -0.02965 -0.02866 -0.07979 349 LEU A N   
5337 C CA  . LEU A 349 ? 0.52020 0.53600 0.60454 -0.03348 -0.02066 -0.07637 349 LEU A CA  
5338 C C   . LEU A 349 ? 0.48773 0.49146 0.58982 -0.03564 -0.03035 -0.09152 349 LEU A C   
5339 O O   . LEU A 349 ? 0.54133 0.52920 0.64182 -0.03250 -0.03014 -0.09677 349 LEU A O   
5340 C CB  . LEU A 349 ? 0.42362 0.45046 0.52568 -0.04004 -0.01026 -0.06403 349 LEU A CB  
5341 C CG  . LEU A 349 ? 0.47638 0.49715 0.60245 -0.04514 -0.00102 -0.05615 349 LEU A CG  
5342 C CD1 . LEU A 349 ? 0.53228 0.54311 0.64645 -0.04122 0.00457  -0.04647 349 LEU A CD1 
5343 C CD2 . LEU A 349 ? 0.53016 0.56318 0.66930 -0.04968 0.01084  -0.04376 349 LEU A CD2 
5355 N N   . VAL A 350 ? 0.54615 0.55611 0.66914 -0.04048 -0.04079 -0.09999 350 VAL A N   
5356 C CA  A VAL A 350 ? 0.58133 0.57964 0.73095 -0.04388 -0.05473 -0.11500 350 VAL A CA  
5357 C CA  B VAL A 350 ? 0.49959 0.49789 0.64922 -0.04389 -0.05464 -0.11494 350 VAL A CA  
5358 C C   . VAL A 350 ? 0.48894 0.46929 0.60565 -0.03443 -0.07141 -0.13324 350 VAL A C   
5359 O O   . VAL A 350 ? 0.59965 0.56115 0.72330 -0.03306 -0.08094 -0.14727 350 VAL A O   
5360 C CB  A VAL A 350 ? 0.53641 0.54839 0.72507 -0.05146 -0.06201 -0.11710 350 VAL A CB  
5361 C CB  B VAL A 350 ? 0.52484 0.53634 0.71435 -0.05156 -0.06238 -0.11747 350 VAL A CB  
5362 C CG1 A VAL A 350 ? 0.60958 0.60875 0.82973 -0.05475 -0.08373 -0.13483 350 VAL A CG1 
5363 C CG1 B VAL A 350 ? 0.52859 0.55444 0.75118 -0.05899 -0.04156 -0.09941 350 VAL A CG1 
5364 C CG2 A VAL A 350 ? 0.52995 0.55673 0.74966 -0.05859 -0.04089 -0.09879 350 VAL A CG2 
5365 C CG2 B VAL A 350 ? 0.58753 0.60996 0.75763 -0.04755 -0.07126 -0.12045 350 VAL A CG2 
5384 N N   . THR A 351 ? 0.57850 0.56290 0.65773 -0.02661 -0.07518 -0.13325 351 THR A N   
5385 C CA  A THR A 351 ? 0.57072 0.53844 0.61097 -0.01537 -0.09014 -0.14874 351 THR A CA  
5386 C CA  C THR A 351 ? 0.55482 0.52222 0.59573 -0.01548 -0.09037 -0.14907 351 THR A CA  
5387 C C   . THR A 351 ? 0.54769 0.50106 0.55345 -0.00440 -0.07655 -0.14767 351 THR A C   
5388 O O   . THR A 351 ? 0.58532 0.51677 0.57160 0.00381  -0.08474 -0.16496 351 THR A O   
5389 C CB  A THR A 351 ? 0.58401 0.56228 0.60020 -0.01058 -0.09764 -0.14476 351 THR A CB  
5390 C CB  C THR A 351 ? 0.58341 0.56078 0.60115 -0.01086 -0.09944 -0.14634 351 THR A CB  
5391 O OG1 A THR A 351 ? 0.57152 0.56756 0.62605 -0.02059 -0.10323 -0.14104 351 THR A OG1 
5392 O OG1 C THR A 351 ? 0.57848 0.57216 0.59106 -0.01094 -0.08191 -0.12681 351 THR A OG1 
5393 C CG2 A THR A 351 ? 0.66883 0.62938 0.64710 0.00040  -0.11884 -0.16173 351 THR A CG2 
5394 C CG2 C THR A 351 ? 0.61356 0.60051 0.66852 -0.01950 -0.11772 -0.15276 351 THR A CG2 
5409 N N   . TRP A 352 ? 0.61064 0.57529 0.61057 -0.00321 -0.05646 -0.12833 352 TRP A N   
5410 C CA  . TRP A 352 ? 0.60094 0.55576 0.57689 0.00752  -0.04092 -0.12348 352 TRP A CA  
5411 C C   . TRP A 352 ? 0.53155 0.48252 0.53535 0.00278  -0.02862 -0.11713 352 TRP A C   
5412 O O   . TRP A 352 ? 0.54613 0.48229 0.53903 0.01180  -0.02006 -0.12098 352 TRP A O   
5413 C CB  . TRP A 352 ? 0.58956 0.55858 0.54926 0.01261  -0.02839 -0.10411 352 TRP A CB  
5414 C CG  . TRP A 352 ? 0.60790 0.57632 0.53167 0.02267  -0.03462 -0.10575 352 TRP A CG  
5415 C CD1 . TRP A 352 ? 0.66212 0.62152 0.56564 0.02603  -0.05389 -0.12210 352 TRP A CD1 
5416 C CD2 . TRP A 352 ? 0.61221 0.58908 0.51867 0.03105  -0.02234 -0.08788 352 TRP A CD2 
5417 N NE1 . TRP A 352 ? 0.65810 0.61931 0.52665 0.03679  -0.05366 -0.11460 352 TRP A NE1 
5418 C CE2 . TRP A 352 ? 0.66570 0.63822 0.53807 0.03974  -0.03285 -0.09264 352 TRP A CE2 
5419 C CE3 . TRP A 352 ? 0.62526 0.61271 0.54612 0.03201  -0.00501 -0.06704 352 TRP A CE3 
5420 C CZ2 . TRP A 352 ? 0.70529 0.68436 0.55754 0.04945  -0.02316 -0.07477 352 TRP A CZ2 
5421 C CZ3 . TRP A 352 ? 0.62776 0.62220 0.53536 0.04070  0.00325  -0.05077 352 TRP A CZ3 
5422 C CH2 . TRP A 352 ? 0.68684 0.67743 0.56058 0.04933  -0.00407 -0.05351 352 TRP A CH2 
5433 N N   . GLY A 353 ? 0.55019 0.51362 0.58873 -0.00983 -0.02639 -0.10644 353 GLY A N   
5434 C CA  . GLY A 353 ? 0.56327 0.52404 0.62596 -0.01387 -0.01483 -0.09549 353 GLY A CA  
5435 C C   . GLY A 353 ? 0.58010 0.54791 0.63440 -0.00944 -0.00093 -0.07681 353 GLY A C   
5436 O O   . GLY A 353 ? 0.53086 0.49328 0.60138 -0.00969 0.00760  -0.06769 353 GLY A O   
5440 N N   . TRP A 354 ? 0.49662 0.47568 0.53172 -0.00551 -0.00014 -0.07008 354 TRP A N   
5441 C CA  . TRP A 354 ? 0.48653 0.47320 0.52175 -0.00186 0.00950  -0.05201 354 TRP A CA  
5442 C C   . TRP A 354 ? 0.53723 0.53962 0.56589 -0.00391 0.00409  -0.04518 354 TRP A C   
5443 O O   . TRP A 354 ? 0.50951 0.51386 0.52318 -0.00172 -0.00268 -0.05363 354 TRP A O   
5444 C CB  . TRP A 354 ? 0.59323 0.57030 0.61517 0.01131  0.02029  -0.05186 354 TRP A CB  
5445 C CG  . TRP A 354 ? 0.58951 0.57571 0.62356 0.01487  0.02986  -0.03135 354 TRP A CG  
5446 C CD1 . TRP A 354 ? 0.47359 0.45696 0.53010 0.01628  0.03788  -0.01986 354 TRP A CD1 
5447 C CD2 . TRP A 354 ? 0.54816 0.54757 0.58009 0.01722  0.03010  -0.01906 354 TRP A CD2 
5448 N NE1 . TRP A 354 ? 0.51459 0.50904 0.58474 0.01908  0.04172  -0.00172 354 TRP A NE1 
5449 C CE2 . TRP A 354 ? 0.54436 0.54851 0.60123 0.01951  0.03740  -0.00084 354 TRP A CE2 
5450 C CE3 . TRP A 354 ? 0.56698 0.57416 0.58368 0.01762  0.02367  -0.02068 354 TRP A CE3 
5451 C CZ2 . TRP A 354 ? 0.53376 0.54999 0.60426 0.02146  0.03775  0.01505  354 TRP A CZ2 
5452 C CZ3 . TRP A 354 ? 0.55268 0.57144 0.58071 0.01977  0.02546  -0.00422 354 TRP A CZ3 
5453 C CH2 . TRP A 354 ? 0.53216 0.55530 0.58857 0.02143  0.03227  0.01327  354 TRP A CH2 
5464 N N   . MET A 355 ? 0.44085 0.45257 0.48127 -0.00759 0.00471  -0.03069 355 MET A N   
5465 C CA  . MET A 355 ? 0.49140 0.51533 0.53015 -0.00855 -0.00171 -0.02481 355 MET A CA  
5466 C C   . MET A 355 ? 0.55407 0.58150 0.60626 -0.00664 -0.00035 -0.00833 355 MET A C   
5467 O O   . MET A 355 ? 0.46995 0.49268 0.53301 -0.00719 0.00320  -0.00074 355 MET A O   
5468 C CB  . MET A 355 ? 0.51258 0.54381 0.55328 -0.01643 -0.00904 -0.02973 355 MET A CB  
5469 C CG  . MET A 355 ? 0.51848 0.54640 0.56103 -0.02052 -0.00987 -0.04299 355 MET A CG  
5470 S SD  . MET A 355 ? 0.56139 0.58359 0.61947 -0.02657 -0.00231 -0.03818 355 MET A SD  
5471 C CE  . MET A 355 ? 0.50655 0.53974 0.56065 -0.02982 -0.00199 -0.02829 355 MET A CE  
5481 N N   . HIS A 356 ? 0.51864 0.55415 0.57536 -0.00454 -0.00529 -0.00177 356 HIS A N   
5482 C CA  . HIS A 356 ? 0.47457 0.51379 0.55287 -0.00346 -0.00862 0.01371  356 HIS A CA  
5483 C C   . HIS A 356 ? 0.53404 0.57209 0.61406 -0.00935 -0.01871 0.01523  356 HIS A C   
5484 O O   . HIS A 356 ? 0.50850 0.54680 0.57292 -0.01392 -0.02281 0.00577  356 HIS A O   
5485 C CB  . HIS A 356 ? 0.48979 0.53728 0.57909 -0.00187 -0.01547 0.01947  356 HIS A CB  
5486 C CG  . HIS A 356 ? 0.42858 0.47974 0.55043 -0.00050 -0.02054 0.03612  356 HIS A CG  
5487 N ND1 . HIS A 356 ? 0.48534 0.53689 0.61889 -0.00518 -0.03886 0.03727  356 HIS A ND1 
5488 C CD2 . HIS A 356 ? 0.46102 0.51539 0.60912 0.00583  -0.01035 0.05255  356 HIS A CD2 
5489 C CE1 . HIS A 356 ? 0.44523 0.49973 0.61537 -0.00318 -0.04376 0.05300  356 HIS A CE1 
5490 N NE2 . HIS A 356 ? 0.44315 0.50089 0.62657 0.00323  -0.02471 0.06405  356 HIS A NE2 
5498 N N   . HIS A 357 ? 0.50949 0.54607 0.60893 -0.00802 -0.02215 0.02870  357 HIS A N   
5499 C CA  . HIS A 357 ? 0.50570 0.53868 0.60095 -0.01158 -0.03360 0.03239  357 HIS A CA  
5500 C C   . HIS A 357 ? 0.54884 0.58406 0.62600 -0.01427 -0.04770 0.02351  357 HIS A C   
5501 O O   . HIS A 357 ? 0.56842 0.60031 0.62275 -0.01629 -0.04852 0.01924  357 HIS A O   
5502 C CB  . HIS A 357 ? 0.50900 0.54120 0.63361 -0.00911 -0.04191 0.04864  357 HIS A CB  
5503 C CG  . HIS A 357 ? 0.48572 0.51236 0.60204 -0.01112 -0.05850 0.05369  357 HIS A CG  
5504 N ND1 . HIS A 357 ? 0.56572 0.58554 0.66839 -0.01227 -0.05329 0.05759  357 HIS A ND1 
5505 C CD2 . HIS A 357 ? 0.48686 0.51199 0.60442 -0.01118 -0.08187 0.05569  357 HIS A CD2 
5506 C CE1 . HIS A 357 ? 0.54104 0.55586 0.63143 -0.01221 -0.07125 0.06356  357 HIS A CE1 
5507 N NE2 . HIS A 357 ? 0.53369 0.55069 0.63109 -0.01122 -0.09024 0.06073  357 HIS A NE2 
5515 N N   . LEU A 358 ? 0.52699 0.56720 0.61564 -0.01324 -0.05727 0.02156  358 LEU A N   
5516 C CA  . LEU A 358 ? 0.55231 0.59240 0.62690 -0.01412 -0.07197 0.01085  358 LEU A CA  
5517 C C   . LEU A 358 ? 0.52664 0.57021 0.58069 -0.01553 -0.06270 -0.00363 358 LEU A C   
5518 O O   . LEU A 358 ? 0.57940 0.62179 0.61618 -0.01505 -0.06932 -0.01380 358 LEU A O   
5519 C CB  . LEU A 358 ? 0.51191 0.55482 0.61469 -0.01286 -0.08712 0.01389  358 LEU A CB  
5520 C CG  . LEU A 358 ? 0.58575 0.62515 0.71653 -0.01199 -0.10421 0.02642  358 LEU A CG  
5521 C CD1 . LEU A 358 ? 0.61990 0.66215 0.78720 -0.01172 -0.12049 0.02887  358 LEU A CD1 
5522 C CD2 . LEU A 358 ? 0.64914 0.67842 0.75343 -0.01146 -0.12056 0.02223  358 LEU A CD2 
5534 N N   . ALA A 359 ? 0.48938 0.53635 0.54584 -0.01611 -0.04878 -0.00540 359 ALA A N   
5535 C CA  . ALA A 359 ? 0.50871 0.55841 0.55173 -0.01822 -0.04158 -0.01771 359 ALA A CA  
5536 C C   . ALA A 359 ? 0.55080 0.59694 0.58033 -0.02071 -0.03311 -0.01801 359 ALA A C   
5537 O O   . ALA A 359 ? 0.53371 0.58252 0.55277 -0.02164 -0.02999 -0.02546 359 ALA A O   
5538 C CB  . ALA A 359 ? 0.57081 0.62207 0.61811 -0.01738 -0.03378 -0.02015 359 ALA A CB  
5544 N N   . ARG A 360 ? 0.47050 0.51087 0.50360 -0.02104 -0.02786 -0.00806 360 ARG A N   
5545 C CA  . ARG A 360 ? 0.54460 0.58087 0.56876 -0.02317 -0.02022 -0.00328 360 ARG A CA  
5546 C C   . ARG A 360 ? 0.57108 0.60594 0.57347 -0.02090 -0.02725 -0.00095 360 ARG A C   
5547 O O   . ARG A 360 ? 0.59797 0.63334 0.58534 -0.02110 -0.01796 -0.00120 360 ARG A O   
5548 C CB  . ARG A 360 ? 0.50085 0.52983 0.53716 -0.02295 -0.01612 0.00864  360 ARG A CB  
5549 C CG  . ARG A 360 ? 0.49149 0.51758 0.54175 -0.02320 -0.00687 0.00302  360 ARG A CG  
5550 C CD  . ARG A 360 ? 0.50514 0.52219 0.56965 -0.02180 -0.00096 0.01254  360 ARG A CD  
5551 N NE  . ARG A 360 ? 0.50309 0.51594 0.57571 -0.01723 0.00474  0.00619  360 ARG A NE  
5552 C CZ  . ARG A 360 ? 0.50350 0.50607 0.58773 -0.01486 0.01271  0.00578  360 ARG A CZ  
5553 N NH1 . ARG A 360 ? 0.51604 0.51208 0.61191 -0.01832 0.01545  0.01299  360 ARG A NH1 
5554 N NH2 . ARG A 360 ? 0.47798 0.47551 0.56112 -0.00764 0.01878  -0.00162 360 ARG A NH2 
5568 N N   . HIS A 361 ? 0.57944 0.61162 0.58029 -0.01773 -0.04378 0.00161  361 HIS A N   
5569 C CA  . HIS A 361 ? 0.59470 0.62176 0.56858 -0.01351 -0.05569 -0.00030 361 HIS A CA  
5570 C C   . HIS A 361 ? 0.67998 0.71108 0.63727 -0.01133 -0.05166 -0.01570 361 HIS A C   
5571 O O   . HIS A 361 ? 0.67999 0.70779 0.60672 -0.00704 -0.04629 -0.01752 361 HIS A O   
5572 C CB  . HIS A 361 ? 0.67694 0.69978 0.66299 -0.01119 -0.07920 0.00206  361 HIS A CB  
5573 C CG  . HIS A 361 ? 0.73153 0.74369 0.68870 -0.00597 -0.09744 0.00264  361 HIS A CG  
5574 N ND1 . HIS A 361 ? 0.80677 0.81154 0.75037 -0.00451 -0.10006 0.01696  361 HIS A ND1 
5575 C CD2 . HIS A 361 ? 0.89954 0.90492 0.83628 -0.00064 -0.11625 -0.01024 361 HIS A CD2 
5576 C CE1 . HIS A 361 ? 0.91232 0.90611 0.82329 0.00191  -0.12045 0.01340  361 HIS A CE1 
5577 N NE2 . HIS A 361 ? 0.92784 0.92097 0.83322 0.00466  -0.13084 -0.00472 361 HIS A NE2 
5585 N N   . SER A 362 ? 0.58978 0.62786 0.56675 -0.01298 -0.05274 -0.02555 362 SER A N   
5586 C CA  . SER A 362 ? 0.66027 0.70241 0.62928 -0.01031 -0.05062 -0.04039 362 SER A CA  
5587 C C   . SER A 362 ? 0.66195 0.70891 0.62146 -0.01081 -0.02921 -0.04129 362 SER A C   
5588 O O   . SER A 362 ? 0.69504 0.74068 0.63065 -0.00501 -0.02306 -0.04683 362 SER A O   
5589 C CB  . SER A 362 ? 0.58753 0.63674 0.58435 -0.01255 -0.05512 -0.04673 362 SER A CB  
5590 O OG  . SER A 362 ? 0.66313 0.70872 0.67188 -0.01059 -0.07434 -0.04708 362 SER A OG  
5596 N N   . VAL A 363 ? 0.63260 0.68431 0.61234 -0.01681 -0.01733 -0.03568 363 VAL A N   
5597 C CA  . VAL A 363 ? 0.72623 0.78380 0.71131 -0.01867 0.00174  -0.03521 363 VAL A CA  
5598 C C   . VAL A 363 ? 0.78053 0.83309 0.74302 -0.01607 0.01355  -0.02211 363 VAL A C   
5599 O O   . VAL A 363 ? 0.79637 0.85359 0.75374 -0.01367 0.03114  -0.02021 363 VAL A O   
5600 C CB  . VAL A 363 ? 0.61017 0.67120 0.62621 -0.02572 0.00592  -0.03501 363 VAL A CB  
5601 C CG1 . VAL A 363 ? 0.57442 0.64010 0.60532 -0.02628 -0.00517 -0.04669 363 VAL A CG1 
5602 C CG2 . VAL A 363 ? 0.49814 0.55077 0.51727 -0.02825 0.00417  -0.02422 363 VAL A CG2 
5612 N N   . ALA A 364 ? 0.64390 0.68741 0.59494 -0.01578 0.00532  -0.01063 364 ALA A N   
5613 C CA  . ALA A 364 ? 0.87299 0.91042 0.79993 -0.01254 0.01448  0.00497  364 ALA A CA  
5614 C C   . ALA A 364 ? 0.97828 1.01079 0.85984 -0.00215 0.01199  0.00069  364 ALA A C   
5615 O O   . ALA A 364 ? 0.94095 0.97339 0.79911 0.00310  0.03035  0.00905  364 ALA A O   
5616 C CB  . ALA A 364 ? 0.82514 0.85380 0.75587 -0.01441 0.00344  0.01852  364 ALA A CB  
5622 N N   . CYS A 365 ? 0.94560 0.97276 0.81444 0.00197  -0.01037 -0.01208 365 CYS A N   
5623 C CA  . CYS A 365 ? 0.99883 1.01775 0.82229 0.01344  -0.01665 -0.02194 365 CYS A CA  
5624 C C   . CYS A 365 ? 0.99416 1.02138 0.81441 0.01806  0.00360  -0.03408 365 CYS A C   
5625 O O   . CYS A 365 ? 1.14252 1.16555 0.92219 0.02877  0.01731  -0.03420 365 CYS A O   
5626 C CB  . CYS A 365 ? 0.92435 0.93495 0.74770 0.01558  -0.04827 -0.03484 365 CYS A CB  
5627 S SG  . CYS A 365 ? 0.94282 0.94144 0.76381 0.01448  -0.07468 -0.02015 365 CYS A SG  
5633 N N   . PHE A 366 ? 0.95398 0.99280 0.81620 0.01138  0.00640  -0.04347 366 PHE A N   
5634 C CA  . PHE A 366 ? 1.04904 1.09772 0.92017 0.01495  0.02522  -0.05356 366 PHE A CA  
5635 C C   . PHE A 366 ? 1.10772 1.16394 0.98149 0.01505  0.05615  -0.03836 366 PHE A C   
5636 O O   . PHE A 366 ? 1.11955 1.18300 0.99299 0.02157  0.07679  -0.04297 366 PHE A O   
5637 C CB  . PHE A 366 ? 1.37307 1.43235 1.29244 0.00680  0.01882  -0.06293 366 PHE A CB  
5638 C CG  . PHE A 366 ? 1.42296 1.49450 1.36492 0.00869  0.03695  -0.07077 366 PHE A CG  
5639 C CD1 . PHE A 366 ? 1.46622 1.53681 1.39649 0.01864  0.03690  -0.08730 366 PHE A CD1 
5640 C CD2 . PHE A 366 ? 1.22411 1.30734 1.20413 0.00094  0.05252  -0.06241 366 PHE A CD2 
5641 C CE1 . PHE A 366 ? 1.24612 1.32905 1.20369 0.02114  0.05464  -0.09359 366 PHE A CE1 
5642 C CE2 . PHE A 366 ? 1.07760 1.17333 1.08751 0.00240  0.06760  -0.06823 366 PHE A CE2 
5643 C CZ  . PHE A 366 ? 1.01366 1.11019 1.01309 0.01268  0.06993  -0.08299 366 PHE A CZ  
5653 N N   . LEU A 367 ? 1.06501 1.11994 0.94716 0.00833  0.06091  -0.01927 367 LEU A N   
5654 C CA  . LEU A 367 ? 1.15836 1.21968 1.05034 0.00764  0.08976  -0.00100 367 LEU A CA  
5655 C C   . LEU A 367 ? 1.41829 1.46969 1.25545 0.01869  0.10071  0.01434  367 LEU A C   
5656 O O   . LEU A 367 ? 1.32743 1.38422 1.15453 0.02571  0.12975  0.02486  367 LEU A O   
5657 C CB  . LEU A 367 ? 0.99301 1.05677 0.92991 -0.00548 0.08895  0.01118  367 LEU A CB  
5658 C CG  . LEU A 367 ? 1.15697 1.22678 1.11941 -0.00867 0.11607  0.03203  367 LEU A CG  
5659 C CD1 . LEU A 367 ? 1.26072 1.34597 1.26751 -0.01122 0.13293  0.02592  367 LEU A CD1 
5660 C CD2 . LEU A 367 ? 1.24793 1.31252 1.24224 -0.01917 0.10928  0.04371  367 LEU A CD2 
5672 N N   . THR A 368 ? 1.38161 1.41864 1.18353 0.02138  0.07815  0.01713  368 THR A N   
5673 C CA  . THR A 368 ? 1.65701 1.68241 1.40597 0.03121  0.08357  0.03515  368 THR A CA  
5674 C C   . THR A 368 ? 1.53152 1.54119 1.21567 0.04550  0.06325  0.02087  368 THR A C   
5675 O O   . THR A 368 ? 1.53107 1.53305 1.15846 0.05994  0.07729  0.02713  368 THR A O   
5676 C CB  . THR A 368 ? 1.26828 1.28771 1.03315 0.02275  0.07215  0.05526  368 THR A CB  
5677 O OG1 . THR A 368 ? 1.35488 1.36523 1.11670 0.02085  0.03757  0.04417  368 THR A OG1 
5678 C CG2 . THR A 368 ? 1.35253 1.38346 1.18448 0.00849  0.08465  0.06274  368 THR A CG2 
5686 N N   . ARG A 369 ? 1.53084 1.53443 1.22180 0.04289  0.03047  0.00192  369 ARG A N   
5687 C CA  . ARG A 369 ? 1.40977 1.39489 1.04611 0.05510  0.00281  -0.01164 369 ARG A CA  
5688 C C   . ARG A 369 ? 1.52671 1.50691 1.11855 0.07096  0.01325  -0.03218 369 ARG A C   
5689 O O   . ARG A 369 ? 1.57193 1.53392 1.11613 0.08273  -0.01188 -0.04881 369 ARG A O   
5690 C CB  . ARG A 369 ? 1.46845 1.45032 1.13905 0.04698  -0.03344 -0.02478 369 ARG A CB  
5691 C CG  . ARG A 369 ? 1.47766 1.43945 1.10659 0.05743  -0.06935 -0.04012 369 ARG A CG  
5692 C CD  . ARG A 369 ? 1.42504 1.38618 1.10266 0.04778  -0.10251 -0.04644 369 ARG A CD  
5693 N NE  . ARG A 369 ? 1.46971 1.43693 1.17868 0.04569  -0.10617 -0.06790 369 ARG A NE  
5694 C CZ  . ARG A 369 ? 1.43735 1.39272 1.14450 0.05075  -0.13592 -0.08835 369 ARG A CZ  
5695 N NH1 . ARG A 369 ? 1.30341 1.23941 0.97963 0.05797  -0.16847 -0.09271 369 ARG A NH1 
5696 N NH2 . ARG A 369 ? 1.31577 1.27788 1.05609 0.04854  -0.13534 -0.10465 369 ARG A NH2 
5710 N N   . GLY A 370 ? 1.50787 1.50214 1.11390 0.07300  0.04846  -0.03223 370 GLY A N   
5711 C CA  . GLY A 370 ? 1.56177 1.55075 1.12224 0.09096  0.06393  -0.04921 370 GLY A CA  
5712 C C   . GLY A 370 ? 1.53314 1.53558 1.13704 0.08957  0.07551  -0.06921 370 GLY A C   
5713 O O   . GLY A 370 ? 1.64117 1.63533 1.21259 0.10460  0.07675  -0.09172 370 GLY A O   
5717 N N   A ASP A 371 ? 1.46779 1.48937 1.14401 0.07282  0.08255  -0.06231 371 ASP A N   
5718 N N   B ASP A 371 ? 1.46785 1.48932 1.14420 0.07266  0.08205  -0.06229 371 ASP A N   
5719 C CA  A ASP A 371 ? 1.44647 1.48314 1.16951 0.07101  0.09613  -0.07605 371 ASP A CA  
5720 C CA  B ASP A 371 ? 1.44604 1.48269 1.17060 0.07032  0.09473  -0.07607 371 ASP A CA  
5721 C C   A ASP A 371 ? 1.40205 1.45746 1.15852 0.06880  0.13643  -0.05781 371 ASP A C   
5722 C C   B ASP A 371 ? 1.40249 1.45759 1.15841 0.06890  0.13567  -0.05839 371 ASP A C   
5723 O O   A ASP A 371 ? 1.39524 1.45849 1.15608 0.07896  0.16157  -0.06519 371 ASP A O   
5724 O O   B ASP A 371 ? 1.39778 1.45971 1.15397 0.07992  0.16068  -0.06603 371 ASP A O   
5725 C CB  A ASP A 371 ? 1.39335 1.43663 1.17468 0.05504  0.06977  -0.08405 371 ASP A CB  
5726 C CB  B ASP A 371 ? 1.38349 1.42711 1.16706 0.05373  0.06910  -0.08236 371 ASP A CB  
5727 C CG  A ASP A 371 ? 1.43546 1.46253 1.19827 0.05474  0.03103  -0.09546 371 ASP A CG  
5728 C CG  B ASP A 371 ? 1.40872 1.44830 1.20169 0.05801  0.04922  -0.10868 371 ASP A CG  
5729 O OD1 A ASP A 371 ? 1.37551 1.39254 1.11324 0.05318  0.01815  -0.08311 371 ASP A OD1 
5730 O OD1 B ASP A 371 ? 1.29776 1.34664 1.11160 0.06306  0.06571  -0.11949 371 ASP A OD1 
5731 O OD2 A ASP A 371 ? 1.47734 1.50200 1.25670 0.05593  0.01299  -0.11528 371 ASP A OD2 
5732 O OD2 B ASP A 371 ? 1.47310 1.50045 1.25874 0.05630  0.01697  -0.11732 371 ASP A OD2 
5741 N N   A LEU A 372 ? 1.38434 1.44691 1.17040 0.05603  0.14320  -0.03396 372 LEU A N   
5742 N N   B LEU A 372 ? 1.38734 1.45034 1.17538 0.05582  0.14290  -0.03480 372 LEU A N   
5743 C CA  A LEU A 372 ? 1.34747 1.42615 1.17094 0.05307  0.17946  -0.01310 372 LEU A CA  
5744 C CA  B LEU A 372 ? 1.35115 1.42990 1.17421 0.05349  0.17970  -0.01387 372 LEU A CA  
5745 C C   A LEU A 372 ? 1.36796 1.44086 1.14974 0.06060  0.20246  0.01407  372 LEU A C   
5746 C C   B LEU A 372 ? 1.36529 1.43758 1.14780 0.05962  0.19969  0.01372  372 LEU A C   
5747 O O   A LEU A 372 ? 1.33874 1.42330 1.13644 0.06519  0.24001  0.03173  372 LEU A O   
5748 O O   B LEU A 372 ? 1.34621 1.43090 1.15815 0.05866  0.23310  0.03583  372 LEU A O   
5749 C CB  A LEU A 372 ? 1.26210 1.35235 1.15913 0.03308  0.17075  -0.00623 372 LEU A CB  
5750 C CB  B LEU A 372 ? 1.25731 1.34915 1.15738 0.03387  0.17264  -0.00821 372 LEU A CB  
5751 C CG  A LEU A 372 ? 1.19668 1.29323 1.13642 0.02518  0.14844  -0.02843 372 LEU A CG  
5752 C CG  B LEU A 372 ? 1.19480 1.29218 1.13522 0.02631  0.14921  -0.03085 372 LEU A CG  
5753 C CD1 A LEU A 372 ? 1.12725 1.23070 1.12553 0.00806  0.13830  -0.02176 372 LEU A CD1 
5754 C CD1 B LEU A 372 ? 1.12683 1.23060 1.12417 0.00904  0.13744  -0.02456 372 LEU A CD1 
5755 C CD2 A LEU A 372 ? 1.14859 1.25727 1.11062 0.03306  0.16648  -0.04063 372 LEU A CD2 
5756 C CD2 B LEU A 372 ? 1.14670 1.25657 1.11162 0.03384  0.16733  -0.04276 372 LEU A CD2 
5779 N N   A TYR A 373 ? 1.39320 1.44890 1.12600 0.06229  0.18103  0.02007  373 TYR A N   
5780 N N   B TYR A 373 ? 1.40152 1.45473 1.12158 0.06590  0.17904  0.01478  373 TYR A N   
5781 C CA  A TYR A 373 ? 1.43038 1.47686 1.11169 0.07174  0.19733  0.04614  373 TYR A CA  
5782 C CA  B TYR A 373 ? 1.43192 1.47692 1.11199 0.07109  0.19183  0.04326  373 TYR A CA  
5783 C C   A TYR A 373 ? 1.40263 1.46050 1.13482 0.06026  0.22061  0.07858  373 TYR A C   
5784 C C   B TYR A 373 ? 1.40804 1.46273 1.15079 0.05358  0.19838  0.06825  373 TYR A C   
5785 O O   A TYR A 373 ? 1.39356 1.44954 1.09647 0.06912  0.24752  0.10571  373 TYR A O   
5786 O O   B TYR A 373 ? 1.43309 1.48141 1.19192 0.04220  0.17050  0.06867  373 TYR A O   
5787 C CB  A TYR A 373 ? 1.43683 1.47915 1.05494 0.09477  0.22647  0.04465  373 TYR A CB  
5788 C CB  B TYR A 373 ? 1.43288 1.47905 1.06716 0.09046  0.23253  0.05534  373 TYR A CB  
5789 C CG  A TYR A 373 ? 1.47793 1.50329 1.03618 0.10921  0.20187  0.01166  373 TYR A CG  
5790 C CG  B TYR A 373 ? 1.46247 1.50308 1.06439 0.09509  0.25154  0.09178  373 TYR A CG  
5791 C CD1 A TYR A 373 ? 1.49428 1.52619 1.08169 0.10992  0.19775  -0.01716 373 TYR A CD1 
5792 C CD1 B TYR A 373 ? 1.42720 1.44780 0.97307 0.09838  0.22369  0.09859  373 TYR A CD1 
5793 C CD2 A TYR A 373 ? 1.58632 1.58769 1.06210 0.12233  0.18001  0.00915  373 TYR A CD2 
5794 C CD2 B TYR A 373 ? 1.43966 1.49555 1.07465 0.09559  0.29624  0.12170  373 TYR A CD2 
5795 C CE1 A TYR A 373 ? 1.49309 1.50771 1.03233 0.12297  0.17377  -0.04811 373 TYR A CE1 
5796 C CE1 B TYR A 373 ? 1.39303 1.40800 0.91062 0.10283  0.23945  0.13421  373 TYR A CE1 
5797 C CE2 A TYR A 373 ? 1.61540 1.59864 1.04073 0.13554  0.15352  -0.02333 373 TYR A CE2 
5798 C CE2 B TYR A 373 ? 1.41080 1.46157 1.02035 0.09970  0.31436  0.15862  373 TYR A CE2 
5799 C CZ  A TYR A 373 ? 1.60655 1.59629 1.06543 0.13565  0.15114  -0.05214 373 TYR A CZ  
5800 C CZ  B TYR A 373 ? 1.39713 1.42700 0.94547 0.10354  0.28553  0.16480  373 TYR A CZ  
5801 O OH  A TYR A 373 ? 1.61695 1.58696 1.03200 0.14860  0.12328  -0.08524 373 TYR A OH  
5802 O OH  B TYR A 373 ? 1.40831 1.43242 0.93149 0.10812  0.30218  0.20373  373 TYR A OH  
5821 N N   A VAL A 374 ? 1.35427 1.42235 1.16129 0.04159  0.21031  0.07685  374 VAL A N   
5822 N N   B VAL A 374 ? 1.37136 1.44075 1.15324 0.05207  0.23534  0.08899  374 VAL A N   
5823 C CA  A VAL A 374 ? 1.27032 1.34587 1.13187 0.02982  0.22642  0.10411  374 VAL A CA  
5824 C CA  B VAL A 374 ? 1.29541 1.37144 1.13691 0.03738  0.24399  0.11467  374 VAL A CA  
5825 C C   A VAL A 374 ? 1.26259 1.32312 1.10232 0.02599  0.20714  0.11986  374 VAL A C   
5826 C C   B VAL A 374 ? 1.30873 1.36841 1.11560 0.03639  0.22678  0.13242  374 VAL A C   
5827 O O   A VAL A 374 ? 1.22473 1.27310 1.03459 0.02601  0.17455  0.10515  374 VAL A O   
5828 O O   B VAL A 374 ? 1.37310 1.41743 1.10710 0.04844  0.21174  0.12855  374 VAL A O   
5829 C CB  A VAL A 374 ? 1.19474 1.28338 1.14056 0.01310  0.21892  0.09243  374 VAL A CB  
5830 C CB  B VAL A 374 ? 1.20418 1.29028 1.12526 0.01911  0.22666  0.09883  374 VAL A CB  
5831 C CG1 A VAL A 374 ? 1.18854 1.28020 1.19270 0.00047  0.22809  0.11654  374 VAL A CG1 
5832 C CG1 B VAL A 374 ? 1.19237 1.28825 1.12697 0.02206  0.22466  0.07119  374 VAL A CG1 
5833 C CG2 A VAL A 374 ? 1.16909 1.27399 1.14473 0.01711  0.23917  0.08122  374 VAL A CG2 
5834 C CG2 B VAL A 374 ? 1.30360 1.37774 1.22587 0.00895  0.18903  0.08946  374 VAL A CG2 
5853 N N   . SER A 375 ? 1.21526 1.27696 1.07642 0.02277  0.22757  0.15180  375 SER A N   
5854 C CA  . SER A 375 ? 1.14511 1.19252 0.98865 0.02044  0.21192  0.17051  375 SER A CA  
5855 C C   . SER A 375 ? 1.05644 1.09939 0.93888 0.00646  0.17811  0.15325  375 SER A C   
5856 O O   . SER A 375 ? 1.01760 1.06943 0.96197 -0.00539 0.17618  0.14092  375 SER A O   
5857 C CB  . SER A 375 ? 1.09764 1.14843 0.97521 0.01725  0.24066  0.20874  375 SER A CB  
5858 O OG  . SER A 375 ? 1.33176 1.40023 1.26706 0.01331  0.27138  0.21404  375 SER A OG  
5865 N N   . TRP A 376 ? 1.02377 1.05231 0.86905 0.00912  0.15114  0.15269  376 TRP A N   
5866 C CA  . TRP A 376 ? 0.95225 0.97676 0.83082 -0.00137 0.12244  0.13753  376 TRP A CA  
5867 C C   . TRP A 376 ? 0.87045 0.89626 0.81541 -0.01397 0.12864  0.14996  376 TRP A C   
5868 O O   . TRP A 376 ? 0.71336 0.73961 0.69761 -0.02282 0.11389  0.13251  376 TRP A O   
5869 C CB  . TRP A 376 ? 0.92301 0.93287 0.75810 0.00441  0.09448  0.13936  376 TRP A CB  
5870 C CG  . TRP A 376 ? 0.93516 0.93502 0.76200 0.00614  0.09643  0.17073  376 TRP A CG  
5871 C CD1 . TRP A 376 ? 0.95342 0.94511 0.72265 0.01837  0.10366  0.19260  376 TRP A CD1 
5872 C CD2 . TRP A 376 ? 0.90838 0.90383 0.78439 -0.00328 0.09051  0.18420  376 TRP A CD2 
5873 N NE1 . TRP A 376 ? 0.91510 0.89862 0.69756 0.01614  0.10174  0.22112  376 TRP A NE1 
5874 C CE2 . TRP A 376 ? 0.94435 0.93005 0.79519 0.00272  0.09393  0.21583  376 TRP A CE2 
5875 C CE3 . TRP A 376 ? 0.90734 0.90463 0.84325 -0.01461 0.08287  0.17200  376 TRP A CE3 
5876 C CZ2 . TRP A 376 ? 1.06215 1.04075 0.95344 -0.00338 0.08958  0.23590  376 TRP A CZ2 
5877 C CZ3 . TRP A 376 ? 0.78736 0.77651 0.75934 -0.01946 0.07977  0.18926  376 TRP A CZ3 
5878 C CH2 . TRP A 376 ? 0.88631 0.86665 0.83963 -0.01441 0.08286  0.22100  376 TRP A CH2 
5889 N N   . GLU A 377 ? 0.81363 0.83870 0.77135 -0.01393 0.15037  0.17994  377 GLU A N   
5890 C CA  . GLU A 377 ? 0.88564 0.90956 0.91187 -0.02571 0.15480  0.19098  377 GLU A CA  
5891 C C   . GLU A 377 ? 0.75852 0.79336 0.84298 -0.03530 0.15953  0.17123  377 GLU A C   
5892 O O   . GLU A 377 ? 0.66827 0.69860 0.80124 -0.04477 0.14713  0.16059  377 GLU A O   
5893 C CB  . GLU A 377 ? 0.89909 0.92138 0.93338 -0.02360 0.17981  0.22987  377 GLU A CB  
5894 C CG  . GLU A 377 ? 1.05070 1.06112 1.02115 -0.01240 0.17426  0.25232  377 GLU A CG  
5895 C CD  . GLU A 377 ? 1.23527 1.24952 1.15290 0.00091  0.20198  0.27456  377 GLU A CD  
5896 O OE1 . GLU A 377 ? 1.21176 1.23030 1.08001 0.01033  0.20361  0.25569  377 GLU A OE1 
5897 O OE2 . GLU A 377 ? 1.31262 1.32482 1.23762 0.00312  0.22345  0.31152  377 GLU A OE2 
5904 N N   . ARG A 378 ? 0.77560 0.82368 0.85542 -0.03179 0.17636  0.16536  378 ARG A N   
5905 C CA  . ARG A 378 ? 0.70376 0.76265 0.84092 -0.04047 0.17743  0.14699  378 ARG A CA  
5906 C C   . ARG A 378 ? 0.69757 0.75321 0.83163 -0.04387 0.14797  0.11387  378 ARG A C   
5907 O O   . ARG A 378 ? 0.60354 0.65883 0.78605 -0.05277 0.13726  0.09956  378 ARG A O   
5908 C CB  . ARG A 378 ? 0.75746 0.83216 0.89177 -0.03433 0.20248  0.14877  378 ARG A CB  
5909 C CG  . ARG A 378 ? 0.84779 0.92878 0.99083 -0.02951 0.23929  0.18454  378 ARG A CG  
5910 C CD  . ARG A 378 ? 0.85622 0.93132 1.05426 -0.03893 0.24520  0.21115  378 ARG A CD  
5911 N NE  . ARG A 378 ? 0.88792 0.95171 1.03748 -0.03110 0.25182  0.23970  378 ARG A NE  
5912 C CZ  . ARG A 378 ? 0.88715 0.94704 1.07149 -0.03454 0.26712  0.27365  378 ARG A CZ  
5913 N NH1 . ARG A 378 ? 0.89654 0.96218 1.16940 -0.04644 0.27704  0.28280  378 ARG A NH1 
5914 N NH2 . ARG A 378 ? 1.08622 1.13521 1.21817 -0.02575 0.27039  0.29966  378 ARG A NH2 
5928 N N   . GLY A 379 ? 0.66052 0.71272 0.73784 -0.03608 0.13396  0.10192  379 GLY A N   
5929 C CA  . GLY A 379 ? 0.64169 0.69084 0.71723 -0.03852 0.10856  0.07610  379 GLY A CA  
5930 C C   . GLY A 379 ? 0.61584 0.65305 0.71270 -0.04402 0.09389  0.07611  379 GLY A C   
5931 O O   . GLY A 379 ? 0.56146 0.59678 0.68081 -0.04841 0.08054  0.05729  379 GLY A O   
5935 N N   . MET A 380 ? 0.64675 0.67475 0.73473 -0.04236 0.09654  0.09755  380 MET A N   
5936 C CA  . MET A 380 ? 0.61537 0.63127 0.72864 -0.04630 0.08530  0.09874  380 MET A CA  
5937 C C   . MET A 380 ? 0.59876 0.61249 0.77064 -0.05495 0.08916  0.09301  380 MET A C   
5938 O O   . MET A 380 ? 0.58190 0.58692 0.77274 -0.05720 0.07589  0.07671  380 MET A O   
5939 C CB  . MET A 380 ? 0.69622 0.70319 0.79571 -0.04284 0.08824  0.12616  380 MET A CB  
5940 C CG  . MET A 380 ? 0.82052 0.81476 0.95923 -0.04694 0.08198  0.13123  380 MET A CG  
5941 S SD  . MET A 380 ? 0.89834 0.88197 1.02295 -0.04219 0.08156  0.16518  380 MET A SD  
5942 C CE  . MET A 380 ? 0.96717 0.95358 1.11811 -0.04576 0.10810  0.19415  380 MET A CE  
5952 N N   . GLU A 381 ? 0.54122 0.56190 0.74320 -0.05888 0.10710  0.10603  381 GLU A N   
5953 C CA  . GLU A 381 ? 0.58128 0.59880 0.84778 -0.06789 0.10712  0.10047  381 GLU A CA  
5954 C C   . GLU A 381 ? 0.52644 0.54521 0.80280 -0.07031 0.08974  0.06785  381 GLU A C   
5955 O O   . GLU A 381 ? 0.47650 0.48355 0.78547 -0.07443 0.07638  0.05287  381 GLU A O   
5956 C CB  . GLU A 381 ? 0.57381 0.60225 0.87698 -0.07147 0.13074  0.12186  381 GLU A CB  
5957 C CG  . GLU A 381 ? 0.80038 0.82469 1.10521 -0.06977 0.14890  0.15817  381 GLU A CG  
5958 C CD  . GLU A 381 ? 0.96499 1.00323 1.29564 -0.07018 0.17862  0.18351  381 GLU A CD  
5959 O OE1 . GLU A 381 ? 0.81098 0.86215 1.17008 -0.07318 0.18365  0.17106  381 GLU A OE1 
5960 O OE2 . GLU A 381 ? 0.94993 0.98657 1.27363 -0.06667 0.19779  0.21753  381 GLU A OE2 
5967 N N   . VAL A 382 ? 0.47957 0.51071 0.72658 -0.06669 0.08885  0.05642  382 VAL A N   
5968 C CA  . VAL A 382 ? 0.51221 0.54473 0.76360 -0.06783 0.07141  0.02841  382 VAL A CA  
5969 C C   . VAL A 382 ? 0.52785 0.54728 0.75322 -0.06400 0.05364  0.01349  382 VAL A C   
5970 O O   . VAL A 382 ? 0.48318 0.49391 0.72373 -0.06533 0.03913  -0.00612 382 VAL A O   
5971 C CB  . VAL A 382 ? 0.49445 0.54265 0.72028 -0.06369 0.07514  0.02229  382 VAL A CB  
5972 C CG1 . VAL A 382 ? 0.48457 0.53298 0.70602 -0.06330 0.05491  -0.00360 382 VAL A CG1 
5973 C CG2 . VAL A 382 ? 0.47475 0.53673 0.73557 -0.06639 0.09533  0.03478  382 VAL A CG2 
5983 N N   . PHE A 383 ? 0.49977 0.51717 0.68554 -0.05804 0.05431  0.02262  383 PHE A N   
5984 C CA  . PHE A 383 ? 0.50404 0.51063 0.67308 -0.05361 0.04204  0.01320  383 PHE A CA  
5985 C C   . PHE A 383 ? 0.51941 0.50987 0.72020 -0.05560 0.04024  0.01222  383 PHE A C   
5986 O O   . PHE A 383 ? 0.47797 0.45795 0.67858 -0.05245 0.03026  -0.00586 383 PHE A O   
5987 C CB  . PHE A 383 ? 0.49421 0.50196 0.62817 -0.04785 0.04211  0.02677  383 PHE A CB  
5988 C CG  . PHE A 383 ? 0.51878 0.53627 0.62003 -0.04364 0.03541  0.01849  383 PHE A CG  
5989 C CD1 . PHE A 383 ? 0.50909 0.53712 0.61019 -0.04508 0.03619  0.00722  383 PHE A CD1 
5990 C CD2 . PHE A 383 ? 0.54378 0.55960 0.62166 -0.03831 0.02713  0.02253  383 PHE A CD2 
5991 C CE1 . PHE A 383 ? 0.53034 0.56572 0.60619 -0.04097 0.02929  -0.00042 383 PHE A CE1 
5992 C CE2 . PHE A 383 ? 0.53382 0.55707 0.58889 -0.03488 0.01900  0.01505  383 PHE A CE2 
5993 C CZ  . PHE A 383 ? 0.55794 0.59028 0.61081 -0.03605 0.02025  0.00322  383 PHE A CZ  
6003 N N   . GLU A 384 ? 0.48033 0.46730 0.70791 -0.05961 0.05062  0.03195  384 GLU A N   
6004 C CA  . GLU A 384 ? 0.58036 0.55033 0.84356 -0.06133 0.04850  0.03209  384 GLU A CA  
6005 C C   . GLU A 384 ? 0.58705 0.54788 0.88161 -0.06470 0.03724  0.00700  384 GLU A C   
6006 O O   . GLU A 384 ? 0.59241 0.53522 0.89936 -0.06182 0.02889  -0.00683 384 GLU A O   
6007 C CB  . GLU A 384 ? 0.62811 0.59760 0.92046 -0.06593 0.06237  0.06114  384 GLU A CB  
6008 C CG  . GLU A 384 ? 0.83883 0.79008 1.17910 -0.06880 0.06009  0.06287  384 GLU A CG  
6009 C CD  . GLU A 384 ? 1.02628 0.97632 1.38809 -0.07123 0.07396  0.09790  384 GLU A CD  
6010 O OE1 . GLU A 384 ? 0.88192 0.84343 1.20789 -0.06822 0.08384  0.11969  384 GLU A OE1 
6011 O OE2 . GLU A 384 ? 1.05414 0.99034 1.46753 -0.07537 0.07401  0.10353  384 GLU A OE2 
6018 N N   . GLU A 385 ? 0.56778 0.53956 0.87512 -0.06962 0.03541  -0.00046 385 GLU A N   
6019 C CA  . GLU A 385 ? 0.60906 0.57148 0.94736 -0.07287 0.01935  -0.02495 385 GLU A CA  
6020 C C   . GLU A 385 ? 0.56372 0.51793 0.86160 -0.06457 0.00329  -0.05188 385 GLU A C   
6021 O O   . GLU A 385 ? 0.51363 0.44840 0.82049 -0.06176 -0.01092 -0.07315 385 GLU A O   
6022 C CB  . GLU A 385 ? 0.65063 0.62928 1.01930 -0.08010 0.02140  -0.02287 385 GLU A CB  
6023 C CG  . GLU A 385 ? 0.74754 0.71639 1.16394 -0.08552 0.00186  -0.04422 385 GLU A CG  
6024 C CD  . GLU A 385 ? 0.73095 0.71844 1.18425 -0.09225 0.00368  -0.04090 385 GLU A CD  
6025 O OE1 . GLU A 385 ? 0.61693 0.62350 1.06864 -0.09322 0.02651  -0.01762 385 GLU A OE1 
6026 O OE2 . GLU A 385 ? 0.77297 0.75516 1.25585 -0.09535 -0.01833 -0.06219 385 GLU A OE2 
6033 N N   . HIS A 386 ? 0.47175 0.43890 0.72452 -0.05950 0.00552  -0.05102 386 HIS A N   
6034 C CA  . HIS A 386 ? 0.52382 0.48805 0.74229 -0.05249 -0.00806 -0.07265 386 HIS A CA  
6035 C C   . HIS A 386 ? 0.53136 0.48906 0.70968 -0.04199 -0.00488 -0.07324 386 HIS A C   
6036 O O   . HIS A 386 ? 0.54819 0.49654 0.70154 -0.03402 -0.01397 -0.09119 386 HIS A O   
6037 C CB  . HIS A 386 ? 0.46834 0.45227 0.67332 -0.05414 -0.00914 -0.07170 386 HIS A CB  
6038 C CG  . HIS A 386 ? 0.54298 0.53473 0.79054 -0.06262 -0.01340 -0.07445 386 HIS A CG  
6039 N ND1 . HIS A 386 ? 0.56278 0.54375 0.83627 -0.06485 -0.03278 -0.09455 386 HIS A ND1 
6040 C CD2 . HIS A 386 ? 0.56342 0.57244 0.83474 -0.06845 -0.00055 -0.05931 386 HIS A CD2 
6041 C CE1 . HIS A 386 ? 0.59019 0.58319 0.90992 -0.07313 -0.03249 -0.09020 386 HIS A CE1 
6042 N NE2 . HIS A 386 ? 0.56693 0.57770 0.88566 -0.07491 -0.01040 -0.06822 386 HIS A NE2 
6050 N N   . LEU A 387 ? 0.41722 0.53602 0.64630 -0.05333 -0.00419 -0.02519 387 LEU A N   
6051 C CA  . LEU A 387 ? 0.44483 0.56529 0.62759 -0.04979 -0.00229 -0.03393 387 LEU A CA  
6052 C C   . LEU A 387 ? 0.42290 0.53565 0.61206 -0.04157 -0.01844 -0.04977 387 LEU A C   
6053 O O   . LEU A 387 ? 0.41430 0.52352 0.64230 -0.04237 -0.02542 -0.04770 387 LEU A O   
6054 C CB  . LEU A 387 ? 0.42297 0.55041 0.59042 -0.05341 0.01375  -0.01928 387 LEU A CB  
6055 C CG  . LEU A 387 ? 0.43197 0.56297 0.57124 -0.05577 0.02614  -0.01082 387 LEU A CG  
6056 C CD1 . LEU A 387 ? 0.45856 0.59015 0.58448 -0.05410 0.03370  0.00039  387 LEU A CD1 
6057 C CD2 . LEU A 387 ? 0.47180 0.60466 0.58193 -0.05558 0.02454  -0.02080 387 LEU A CD2 
6069 N N   . ILE A 388 ? 0.40353 0.51244 0.55422 -0.03095 -0.02272 -0.06412 388 ILE A N   
6070 C CA  . ILE A 388 ? 0.47899 0.57870 0.62308 -0.01723 -0.03484 -0.07990 388 ILE A CA  
6071 C C   . ILE A 388 ? 0.44974 0.55856 0.58867 -0.01880 -0.02094 -0.07195 388 ILE A C   
6072 O O   . ILE A 388 ? 0.44444 0.54672 0.58628 -0.00834 -0.02885 -0.08252 388 ILE A O   
6073 C CB  . ILE A 388 ? 0.48949 0.57863 0.58720 0.00252  -0.04158 -0.09619 388 ILE A CB  
6074 C CG1 . ILE A 388 ? 0.53414 0.63525 0.59469 0.00211  -0.01702 -0.08325 388 ILE A CG1 
6075 C CG2 . ILE A 388 ? 0.52715 0.60315 0.63291 0.00710  -0.06387 -0.10833 388 ILE A CG2 
6076 C CD1 . ILE A 388 ? 0.55626 0.64722 0.56703 0.02616  -0.01594 -0.09219 388 ILE A CD1 
6088 N N   . ASP A 389 ? 0.45904 0.58078 0.59187 -0.02969 -0.00368 -0.05554 389 ASP A N   
6089 C CA  . ASP A 389 ? 0.39686 0.52640 0.53464 -0.03242 0.00430  -0.04740 389 ASP A CA  
6090 C C   . ASP A 389 ? 0.42564 0.55631 0.58815 -0.04164 0.00503  -0.03364 389 ASP A C   
6091 O O   . ASP A 389 ? 0.42358 0.55951 0.58352 -0.04405 0.01015  -0.02474 389 ASP A O   
6092 C CB  . ASP A 389 ? 0.37995 0.51983 0.49828 -0.03436 0.01757  -0.04017 389 ASP A CB  
6093 C CG  . ASP A 389 ? 0.40728 0.54955 0.51814 -0.04382 0.02153  -0.03188 389 ASP A CG  
6094 O OD1 . ASP A 389 ? 0.40578 0.54430 0.52449 -0.04883 0.01915  -0.02691 389 ASP A OD1 
6095 O OD2 . ASP A 389 ? 0.43356 0.58122 0.53404 -0.04468 0.02857  -0.02869 389 ASP A OD2 
6100 N N   . GLN A 390 ? 0.39977 0.52462 0.58874 -0.04434 0.00004  -0.03013 390 GLN A N   
6101 C CA  . GLN A 390 ? 0.44236 0.56765 0.65481 -0.04858 0.00732  -0.01071 390 GLN A CA  
6102 C C   . GLN A 390 ? 0.45842 0.58362 0.68128 -0.04620 0.00594  -0.00638 390 GLN A C   
6103 O O   . GLN A 390 ? 0.40179 0.52226 0.64657 -0.04256 -0.00539 -0.01740 390 GLN A O   
6104 C CB  . GLN A 390 ? 0.47626 0.59619 0.73536 -0.05027 0.00276  -0.00578 390 GLN A CB  
6105 C CG  . GLN A 390 ? 0.56263 0.68136 0.86518 -0.05071 0.01088  0.01698  390 GLN A CG  
6106 C CD  . GLN A 390 ? 0.56030 0.68271 0.83333 -0.04755 0.03265  0.04063  390 GLN A CD  
6107 O OE1 . GLN A 390 ? 0.59108 0.71587 0.82111 -0.04661 0.03940  0.03920  390 GLN A OE1 
6108 N NE2 . GLN A 390 ? 0.62850 0.74864 0.92284 -0.04291 0.04225  0.06224  390 GLN A NE2 
6117 N N   . ASP A 391 ? 0.42863 0.55659 0.63306 -0.04574 0.01477  0.00790  391 ASP A N   
6118 C CA  . ASP A 391 ? 0.48579 0.61342 0.69574 -0.04242 0.01218  0.01310  391 ASP A CA  
6119 C C   . ASP A 391 ? 0.50227 0.62531 0.70683 -0.03736 0.02214  0.03680  391 ASP A C   
6120 O O   . ASP A 391 ? 0.50138 0.62269 0.67017 -0.03333 0.02825  0.04306  391 ASP A O   
6121 C CB  . ASP A 391 ? 0.47887 0.61267 0.66513 -0.04177 0.00823  0.00344  391 ASP A CB  
6122 C CG  . ASP A 391 ? 0.45763 0.59211 0.65858 -0.03821 0.00247  0.00471  391 ASP A CG  
6123 O OD1 . ASP A 391 ? 0.51966 0.64961 0.71780 -0.03452 0.00211  0.01897  391 ASP A OD1 
6124 O OD2 . ASP A 391 ? 0.50249 0.64095 0.71447 -0.03618 -0.00073 -0.00771 391 ASP A OD2 
6129 N N   . HIS A 392 ? 0.48661 0.60553 0.72469 -0.03444 0.02381  0.05031  392 HIS A N   
6130 C CA  . HIS A 392 ? 0.58161 0.69461 0.81544 -0.02479 0.03875  0.07895  392 HIS A CA  
6131 C C   . HIS A 392 ? 0.53407 0.64241 0.70874 -0.01388 0.03809  0.08233  392 HIS A C   
6132 O O   . HIS A 392 ? 0.64783 0.74913 0.78916 -0.00155 0.05117  0.09865  392 HIS A O   
6133 C CB  . HIS A 392 ? 0.69723 0.80647 0.97813 -0.02274 0.03843  0.09284  392 HIS A CB  
6134 C CG  . HIS A 392 ? 0.78198 0.88496 1.06999 -0.01047 0.05969  0.12917  392 HIS A CG  
6135 N ND1 . HIS A 392 ? 0.81754 0.91303 1.07153 0.00438  0.06399  0.14629  392 HIS A ND1 
6136 C CD2 . HIS A 392 ? 0.92190 1.02445 1.24975 -0.00794 0.07967  0.15457  392 HIS A CD2 
6137 C CE1 . HIS A 392 ? 0.88957 0.97929 1.15349 0.01800  0.08886  0.18234  392 HIS A CE1 
6138 N NE2 . HIS A 392 ? 1.01947 1.11482 1.33329 0.00998  0.10075  0.18958  392 HIS A NE2 
6146 N N   . TYR A 393 ? 0.57696 0.68753 0.73964 -0.01566 0.02151  0.06635  393 TYR A N   
6147 C CA  . TYR A 393 ? 0.54197 0.64533 0.65870 -0.00459 0.01194  0.06592  393 TYR A CA  
6148 C C   . TYR A 393 ? 0.58748 0.69181 0.67459 -0.00727 0.00579  0.05043  393 TYR A C   
6149 O O   . TYR A 393 ? 0.65215 0.74449 0.69454 0.00631  0.00209  0.05328  393 TYR A O   
6150 C CB  . TYR A 393 ? 0.55586 0.66177 0.68696 -0.00542 -0.00524 0.05731  393 TYR A CB  
6151 C CG  . TYR A 393 ? 0.56055 0.66124 0.71229 0.00157  -0.00221 0.07477  393 TYR A CG  
6152 C CD1 . TYR A 393 ? 0.64539 0.73302 0.77211 0.01850  0.00908  0.10048  393 TYR A CD1 
6153 C CD2 . TYR A 393 ? 0.59211 0.69969 0.78704 -0.00586 -0.00869 0.06716  393 TYR A CD2 
6154 C CE1 . TYR A 393 ? 0.60946 0.69199 0.75926 0.02569  0.01388  0.12048  393 TYR A CE1 
6155 C CE2 . TYR A 393 ? 0.59677 0.69867 0.81575 0.00015  -0.00731 0.08308  393 TYR A CE2 
6156 C CZ  . TYR A 393 ? 0.67749 0.76738 0.87650 0.01476  0.00400  0.11077  393 TYR A CZ  
6157 O OH  . TYR A 393 ? 0.66448 0.74841 0.89126 0.02151  0.00731  0.13046  393 TYR A OH  
6167 N N   . LEU A 394 ? 0.50352 0.61940 0.61214 -0.02143 0.00392  0.03416  394 LEU A N   
6168 C CA  . LEU A 394 ? 0.51551 0.63294 0.60541 -0.02477 -0.00258 0.02124  394 LEU A CA  
6169 C C   . LEU A 394 ? 0.53844 0.65002 0.60287 -0.02125 0.00878  0.02641  394 LEU A C   
6170 O O   . LEU A 394 ? 0.57651 0.68091 0.61098 -0.01591 0.00161  0.02039  394 LEU A O   
6171 C CB  . LEU A 394 ? 0.44645 0.57729 0.56446 -0.03677 -0.00282 0.00771  394 LEU A CB  
6172 C CG  . LEU A 394 ? 0.50088 0.63938 0.64784 -0.03812 -0.00874 0.00331  394 LEU A CG  
6173 C CD1 . LEU A 394 ? 0.49151 0.64154 0.65523 -0.04333 -0.00333 -0.00632 394 LEU A CD1 
6174 C CD2 . LEU A 394 ? 0.50411 0.63853 0.64973 -0.03240 -0.02521 0.00454  394 LEU A CD2 
6186 N N   . ASN A 395 ? 0.57101 0.68484 0.65329 -0.02348 0.02467  0.03680  395 ASN A N   
6187 C CA  . ASN A 395 ? 0.54287 0.65315 0.61025 -0.01963 0.03817  0.04423  395 ASN A CA  
6188 C C   . ASN A 395 ? 0.61259 0.70835 0.63533 0.00105  0.04529  0.05939  395 ASN A C   
6189 O O   . ASN A 395 ? 0.61378 0.70080 0.59651 0.00996  0.04206  0.05313  395 ASN A O   
6190 C CB  . ASN A 395 ? 0.57685 0.69271 0.68864 -0.02591 0.05071  0.05376  395 ASN A CB  
6191 C CG  . ASN A 395 ? 0.57236 0.68876 0.68350 -0.02596 0.06264  0.05779  395 ASN A CG  
6192 O OD1 . ASN A 395 ? 0.57633 0.68891 0.65013 -0.02166 0.06251  0.05202  395 ASN A OD1 
6193 N ND2 . ASN A 395 ? 0.56318 0.68351 0.72273 -0.03054 0.07046  0.06692  395 ASN A ND2 
6200 N N   . ALA A 396 ? 0.61782 0.70826 0.64311 0.01231  0.05402  0.07920  396 ALA A N   
6201 C CA  . ALA A 396 ? 0.69135 0.76513 0.66559 0.03908  0.06544  0.09807  396 ALA A CA  
6202 C C   . ALA A 396 ? 0.71867 0.77696 0.63477 0.05307  0.04029  0.08036  396 ALA A C   
6203 O O   . ALA A 396 ? 0.72484 0.76694 0.58578 0.07423  0.04205  0.08062  396 ALA A O   
6204 C CB  . ALA A 396 ? 0.77671 0.84741 0.76784 0.04958  0.07945  0.12535  396 ALA A CB  
6210 N N   . ALA A 397 ? 0.69362 0.75533 0.62532 0.04327  0.01489  0.06393  397 ALA A N   
6211 C CA  . ALA A 397 ? 0.72912 0.77503 0.62098 0.05643  -0.01538 0.04666  397 ALA A CA  
6212 C C   . ALA A 397 ? 0.70140 0.74300 0.57679 0.05408  -0.02714 0.02685  397 ALA A C   
6213 O O   . ALA A 397 ? 0.72416 0.74356 0.54824 0.07577  -0.04598 0.01681  397 ALA A O   
6214 C CB  . ALA A 397 ? 0.70294 0.75811 0.63505 0.04272  -0.03832 0.03442  397 ALA A CB  
6220 N N   . ASN A 398 ? 0.66037 0.72031 0.57723 0.03042  -0.01862 0.02013  398 ASN A N   
6221 C CA  . ASN A 398 ? 0.69032 0.74717 0.59991 0.02650  -0.02923 0.00332  398 ASN A CA  
6222 C C   . ASN A 398 ? 0.73114 0.77358 0.59215 0.04518  -0.01450 0.00960  398 ASN A C   
6223 O O   . ASN A 398 ? 0.79468 0.82208 0.62607 0.05522  -0.03126 -0.00589 398 ASN A O   
6224 C CB  . ASN A 398 ? 0.58591 0.66489 0.54760 0.00011  -0.02129 -0.00194 398 ASN A CB  
6225 C CG  . ASN A 398 ? 0.58796 0.67634 0.58953 -0.01257 -0.04033 -0.01377 398 ASN A CG  
6226 O OD1 . ASN A 398 ? 0.53318 0.61826 0.54437 -0.01524 -0.05758 -0.02615 398 ASN A OD1 
6227 N ND2 . ASN A 398 ? 0.52162 0.62158 0.55311 -0.01929 -0.03659 -0.00851 398 ASN A ND2 
6234 N N   . TRP A 399 ? 0.71270 0.75901 0.57126 0.05114  0.01659  0.03263  399 TRP A N   
6235 C CA  . TRP A 399 ? 0.75995 0.79264 0.57306 0.07406  0.03611  0.04376  399 TRP A CA  
6236 C C   . TRP A 399 ? 0.83085 0.83398 0.56803 0.11072  0.02364  0.04253  399 TRP A C   
6237 O O   . TRP A 399 ? 0.84542 0.82915 0.53106 0.13205  0.01837  0.03266  399 TRP A O   
6238 C CB  . TRP A 399 ? 0.74684 0.79115 0.58853 0.07403  0.07376  0.07409  399 TRP A CB  
6239 C CG  . TRP A 399 ? 0.71229 0.77731 0.61314 0.04765  0.08377  0.07231  399 TRP A CG  
6240 C CD1 . TRP A 399 ? 0.61780 0.70061 0.57876 0.02288  0.08027  0.06972  399 TRP A CD1 
6241 C CD2 . TRP A 399 ? 0.73157 0.79853 0.63300 0.04718  0.09597  0.07140  399 TRP A CD2 
6242 N NE1 . TRP A 399 ? 0.62600 0.71983 0.62110 0.00855  0.08684  0.06632  399 TRP A NE1 
6243 C CE2 . TRP A 399 ? 0.62031 0.70627 0.58372 0.02128  0.09704  0.06826  399 TRP A CE2 
6244 C CE3 . TRP A 399 ? 0.76026 0.81276 0.61355 0.06865  0.10447  0.07155  399 TRP A CE3 
6245 C CZ2 . TRP A 399 ? 0.60214 0.69411 0.58386 0.01460  0.10510  0.06634  399 TRP A CZ2 
6246 C CZ3 . TRP A 399 ? 0.78888 0.84921 0.66404 0.06058  0.11557  0.07054  399 TRP A CZ3 
6247 C CH2 . TRP A 399 ? 0.72105 0.80153 0.66151 0.03295  0.11537  0.06858  399 TRP A CH2 
6258 N N   . MET A 400 ? 0.82138 0.81803 0.54712 0.12140  0.01651  0.05102  400 MET A N   
6259 C CA  . MET A 400 ? 0.92049 0.88510 0.56533 0.16193  0.00262  0.05059  400 MET A CA  
6260 C C   . MET A 400 ? 0.96947 0.91516 0.59125 0.16681  -0.04732 0.01390  400 MET A C   
6261 O O   . MET A 400 ? 1.08488 0.99870 0.63206 0.20233  -0.06408 0.00219  400 MET A O   
6262 C CB  . MET A 400 ? 0.91638 0.87914 0.55937 0.17194  0.00757  0.07135  400 MET A CB  
6263 C CG  . MET A 400 ? 0.94634 0.93064 0.64022 0.15975  0.05048  0.10622  400 MET A CG  
6264 S SD  . MET A 400 ? 1.04949 1.02024 0.71385 0.19012  0.06771  0.14178  400 MET A SD  
6265 C CE  . MET A 400 ? 1.07439 1.05192 0.77760 0.16755  0.02532  0.11901  400 MET A CE  
6275 N N   . TRP A 401 ? 0.90485 0.86794 0.59233 0.13446  -0.07228 -0.00409 401 TRP A N   
6276 C CA  . TRP A 401 ? 0.96220 0.91062 0.65265 0.13501  -0.11998 -0.03619 401 TRP A CA  
6277 C C   . TRP A 401 ? 1.03376 0.97479 0.71589 0.13458  -0.12556 -0.05307 401 TRP A C   
6278 O O   . TRP A 401 ? 1.13384 1.05529 0.81207 0.14206  -0.16761 -0.08030 401 TRP A O   
6279 C CB  . TRP A 401 ? 0.91093 0.88404 0.68637 0.10069  -0.13602 -0.04386 401 TRP A CB  
6280 C CG  . TRP A 401 ? 0.92730 0.88889 0.70358 0.11151  -0.16957 -0.05087 401 TRP A CG  
6281 C CD1 . TRP A 401 ? 0.96733 0.91807 0.77181 0.11142  -0.21719 -0.07533 401 TRP A CD1 
6282 C CD2 . TRP A 401 ? 1.05392 1.01321 0.80933 0.12439  -0.15991 -0.03228 401 TRP A CD2 
6283 N NE1 . TRP A 401 ? 1.03062 0.97226 0.83031 0.12399  -0.23955 -0.07473 401 TRP A NE1 
6284 C CE2 . TRP A 401 ? 1.15707 1.10348 0.92297 0.13244  -0.20415 -0.04814 401 TRP A CE2 
6285 C CE3 . TRP A 401 ? 0.96816 0.93467 0.70511 0.12997  -0.11920 -0.00241 401 TRP A CE3 
6286 C CZ2 . TRP A 401 ? 1.10393 1.04418 0.85423 0.14651  -0.20826 -0.03562 401 TRP A CZ2 
6287 C CZ3 . TRP A 401 ? 1.03519 0.99568 0.76046 0.14335  -0.12170 0.01165  401 TRP A CZ3 
6288 C CH2 . TRP A 401 ? 1.01058 0.95786 0.73823 0.15188  -0.16556 -0.00517 401 TRP A CH2 
6299 N N   . LEU A 402 ? 1.06255 1.01774 0.74849 0.12627  -0.08708 -0.03806 402 LEU A N   
6300 C CA  . LEU A 402 ? 1.02880 0.97597 0.70338 0.12833  -0.08964 -0.05202 402 LEU A CA  
6301 C C   . LEU A 402 ? 1.23260 1.13876 0.81959 0.17274  -0.11104 -0.06717 402 LEU A C   
6302 O O   . LEU A 402 ? 1.25205 1.13983 0.83401 0.17795  -0.14491 -0.09479 402 LEU A O   
6303 C CB  . LEU A 402 ? 1.06531 1.03299 0.75541 0.11689  -0.04359 -0.03009 402 LEU A CB  
6304 C CG  . LEU A 402 ? 1.14916 1.12877 0.87737 0.09488  -0.04192 -0.04048 402 LEU A CG  
6305 C CD1 . LEU A 402 ? 1.11215 1.12018 0.91750 0.05707  -0.04490 -0.04153 402 LEU A CD1 
6306 C CD2 . LEU A 402 ? 1.14205 1.12855 0.85957 0.10030  -0.00222 -0.02134 402 LEU A CD2 
6318 N N   . SER A 403 ? 1.31219 1.20141 0.82916 0.20804  -0.09205 -0.04894 403 SER A N   
6319 C CA  . SER A 403 ? 1.49467 1.34062 0.91042 0.25996  -0.10756 -0.06082 403 SER A CA  
6320 C C   . SER A 403 ? 1.55071 1.36565 0.94597 0.27548  -0.17292 -0.09699 403 SER A C   
6321 O O   . SER A 403 ? 1.45461 1.26300 0.84219 0.28339  -0.19204 -0.09542 403 SER A O   
6322 C CB  . SER A 403 ? 1.51144 1.34756 0.86007 0.29659  -0.06836 -0.02648 403 SER A CB  
6323 O OG  . SER A 403 ? 1.43857 1.31132 0.84545 0.27024  -0.01553 0.00977  403 SER A OG  
6329 N N   . TYR A 411 ? 1.23476 1.09282 1.22409 0.07549  -0.34478 -0.22766 411 TYR A N   
6330 C CA  . TYR A 411 ? 1.19262 1.09178 1.23788 0.04099  -0.29666 -0.19705 411 TYR A CA  
6331 C C   . TYR A 411 ? 1.13774 1.03167 1.16652 0.04222  -0.28072 -0.19823 411 TYR A C   
6332 O O   . TYR A 411 ? 1.15225 1.06184 1.25228 0.01910  -0.27247 -0.18781 411 TYR A O   
6333 C CB  . TYR A 411 ? 1.23035 1.15846 1.24013 0.03349  -0.24842 -0.17016 411 TYR A CB  
6334 C CG  . TYR A 411 ? 1.26334 1.22068 1.34278 0.00946  -0.24047 -0.15272 411 TYR A CG  
6335 C CD1 . TYR A 411 ? 1.09231 1.07559 1.25792 -0.01797 -0.22548 -0.13586 411 TYR A CD1 
6336 C CD2 . TYR A 411 ? 1.27332 1.23140 1.33038 0.01736  -0.24554 -0.15114 411 TYR A CD2 
6337 C CE1 . TYR A 411 ? 1.10169 1.11078 1.32739 -0.03500 -0.21407 -0.11835 411 TYR A CE1 
6338 C CE2 . TYR A 411 ? 1.20271 1.18701 1.32373 -0.00251 -0.23728 -0.13570 411 TYR A CE2 
6339 C CZ  . TYR A 411 ? 1.13394 1.14367 1.33825 -0.02775 -0.22072 -0.11960 411 TYR A CZ  
6340 O OH  . TYR A 411 ? 1.12781 1.16298 1.39245 -0.04290 -0.20822 -0.10255 411 TYR A OH  
6350 N N   . PHE A 412 ? 1.23420 1.10592 1.16855 0.07169  -0.27379 -0.20835 412 PHE A N   
6351 C CA  . PHE A 412 ? 1.13529 1.00000 1.04446 0.07801  -0.25720 -0.21023 412 PHE A CA  
6352 C C   . PHE A 412 ? 1.29469 1.11419 1.18178 0.10622  -0.30645 -0.24650 412 PHE A C   
6353 O O   . PHE A 412 ? 1.30481 1.10341 1.12502 0.13210  -0.29883 -0.25643 412 PHE A O   
6354 C CB  . PHE A 412 ? 1.22245 1.09508 1.05178 0.09303  -0.21080 -0.19317 412 PHE A CB  
6355 C CG  . PHE A 412 ? 1.19499 1.10634 1.04542 0.06907  -0.17040 -0.16234 412 PHE A CG  
6356 C CD1 . PHE A 412 ? 1.08930 1.03280 1.00492 0.03597  -0.14683 -0.14305 412 PHE A CD1 
6357 C CD2 . PHE A 412 ? 1.10833 1.02110 0.91181 0.08258  -0.15778 -0.15310 412 PHE A CD2 
6358 C CE1 . PHE A 412 ? 0.96599 0.94008 0.89621 0.01830  -0.11496 -0.11935 412 PHE A CE1 
6359 C CE2 . PHE A 412 ? 1.06251 1.00803 0.89047 0.06133  -0.12494 -0.12757 412 PHE A CE2 
6360 C CZ  . PHE A 412 ? 0.90115 0.87621 0.79117 0.02984  -0.10546 -0.11286 412 PHE A CZ  
6370 N N   . ARG A 413 ? 1.21380 1.01642 1.16211 0.10312  -0.35944 -0.26741 413 ARG A N   
6371 C CA  . ARG A 413 ? 1.16797 0.92446 1.10675 0.13069  -0.41450 -0.30473 413 ARG A CA  
6372 C C   . ARG A 413 ? 1.26976 1.02098 1.22891 0.12538  -0.40842 -0.30937 413 ARG A C   
6373 O O   . ARG A 413 ? 1.23951 0.96067 1.13325 0.15900  -0.41581 -0.32591 413 ARG A O   
6374 C CB  . ARG A 413 ? 1.40558 1.15951 1.44335 0.12090  -0.45494 -0.30722 413 ARG A CB  
6375 C CG  . ARG A 413 ? 1.24621 1.04149 1.40253 0.07435  -0.43945 -0.28138 413 ARG A CG  
6376 C CD  . ARG A 413 ? 1.21143 1.00116 1.47606 0.06912  -0.47445 -0.28057 413 ARG A CD  
6377 N NE  . ARG A 413 ? 1.28146 1.06629 1.62113 0.06125  -0.48392 -0.27934 413 ARG A NE  
6378 C CZ  . ARG A 413 ? 1.26881 1.01796 1.61554 0.08777  -0.52582 -0.30224 413 ARG A CZ  
6379 N NH1 . ARG A 413 ? 1.31954 1.03212 1.59830 0.12641  -0.56262 -0.32899 413 ARG A NH1 
6380 N NH2 . ARG A 413 ? 1.34431 1.09394 1.76877 0.07758  -0.53132 -0.29707 413 ARG A NH2 
6394 N N   . VAL A 414 ? 1.28073 1.06724 1.33271 0.08587  -0.38270 -0.28296 414 VAL A N   
6395 C CA  . VAL A 414 ? 1.28089 1.06684 1.36371 0.07739  -0.37303 -0.28075 414 VAL A CA  
6396 C C   . VAL A 414 ? 1.14291 0.95998 1.18430 0.06773  -0.30894 -0.25056 414 VAL A C   
6397 O O   . VAL A 414 ? 1.29404 1.09863 1.29217 0.08274  -0.29733 -0.25683 414 VAL A O   
6398 C CB  . VAL A 414 ? 1.26064 1.06065 1.47970 0.04429  -0.38969 -0.26965 414 VAL A CB  
6399 C CG1 . VAL A 414 ? 1.16907 0.95306 1.42195 0.04408  -0.39982 -0.27809 414 VAL A CG1 
6400 C CG2 . VAL A 414 ? 1.19836 0.98575 1.47466 0.05067  -0.43358 -0.27909 414 VAL A CG2 
6410 N N   . TYR A 415 ? 1.20245 1.05872 1.25982 0.04422  -0.26943 -0.21899 415 TYR A N   
6411 C CA  . TYR A 415 ? 1.14587 1.03168 1.17661 0.03349  -0.21501 -0.19136 415 TYR A CA  
6412 C C   . TYR A 415 ? 1.11616 1.00526 1.06406 0.05146  -0.19110 -0.18619 415 TYR A C   
6413 O O   . TYR A 415 ? 0.94359 0.84376 0.89251 0.04655  -0.19065 -0.17928 415 TYR A O   
6414 C CB  . TYR A 415 ? 0.93086 0.85476 1.03492 -0.00113 -0.18849 -0.16032 415 TYR A CB  
6415 C CG  . TYR A 415 ? 0.95611 0.88118 1.14279 -0.01802 -0.19849 -0.15461 415 TYR A CG  
6416 C CD1 . TYR A 415 ? 1.00653 0.92427 1.27530 -0.02689 -0.23267 -0.16001 415 TYR A CD1 
6417 C CD2 . TYR A 415 ? 0.95850 0.89176 1.14870 -0.02444 -0.17410 -0.14167 415 TYR A CD2 
6418 C CE1 . TYR A 415 ? 0.89584 0.81502 1.25113 -0.04179 -0.23891 -0.14968 415 TYR A CE1 
6419 C CE2 . TYR A 415 ? 0.88526 0.81874 1.15186 -0.03827 -0.18105 -0.13271 415 TYR A CE2 
6420 C CZ  . TYR A 415 ? 0.97936 0.90614 1.33002 -0.04700 -0.21177 -0.13521 415 TYR A CZ  
6421 O OH  . TYR A 415 ? 0.84458 0.77209 1.28185 -0.06031 -0.21575 -0.12128 415 TYR A OH  
6431 N N   . SER A 416 ? 1.02109 0.90145 0.90405 0.07268  -0.16896 -0.18667 416 SER A N   
6432 C CA  . SER A 416 ? 0.98787 0.87425 0.80394 0.08969  -0.13813 -0.17396 416 SER A CA  
6433 C C   . SER A 416 ? 0.87479 0.80197 0.72783 0.05994  -0.10188 -0.14339 416 SER A C   
6434 O O   . SER A 416 ? 0.82362 0.77180 0.73465 0.03294  -0.09346 -0.13180 416 SER A O   
6435 C CB  . SER A 416 ? 1.11463 0.98680 0.87030 0.11782  -0.11599 -0.17503 416 SER A CB  
6436 O OG  . SER A 416 ? 0.93164 0.82889 0.72502 0.09698  -0.08530 -0.15613 416 SER A OG  
6442 N N   . PRO A 417 ? 0.95413 0.89065 0.77274 0.06728  -0.08097 -0.12992 417 PRO A N   
6443 C CA  . PRO A 417 ? 0.83436 0.80557 0.69030 0.04096  -0.05345 -0.10538 417 PRO A CA  
6444 C C   . PRO A 417 ? 0.82277 0.81308 0.70373 0.02690  -0.02634 -0.09051 417 PRO A C   
6445 O O   . PRO A 417 ? 0.74912 0.76380 0.66941 0.00403  -0.01393 -0.07625 417 PRO A O   
6446 C CB  . PRO A 417 ? 0.90190 0.87360 0.71266 0.05776  -0.03563 -0.09421 417 PRO A CB  
6447 C CG  . PRO A 417 ? 1.05447 0.99147 0.79602 0.09575  -0.05096 -0.11064 417 PRO A CG  
6448 C CD  . PRO A 417 ? 0.99493 0.90943 0.73524 0.10406  -0.07589 -0.13358 417 PRO A CD  
6456 N N   . VAL A 418 ? 0.77022 0.74806 0.62766 0.04274  -0.01874 -0.09468 418 VAL A N   
6457 C CA  . VAL A 418 ? 0.84483 0.83958 0.72717 0.03188  0.00513  -0.08076 418 VAL A CA  
6458 C C   . VAL A 418 ? 0.76011 0.76021 0.69025 0.01092  -0.00787 -0.08374 418 VAL A C   
6459 O O   . VAL A 418 ? 0.64428 0.66211 0.60161 -0.00301 0.00787  -0.07037 418 VAL A O   
6460 C CB  . VAL A 418 ? 0.94360 0.92344 0.78459 0.05996  0.02163  -0.08149 418 VAL A CB  
6461 C CG1 . VAL A 418 ? 0.82868 0.80101 0.68640 0.05877  0.01557  -0.09011 418 VAL A CG1 
6462 C CG2 . VAL A 418 ? 0.91167 0.91051 0.75569 0.06266  0.05791  -0.05700 418 VAL A CG2 
6472 N N   . VAL A 419 ? 0.76406 0.74824 0.70913 0.00978  -0.03723 -0.09960 419 VAL A N   
6473 C CA  . VAL A 419 ? 0.76701 0.75709 0.76687 -0.00971 -0.04641 -0.09643 419 VAL A CA  
6474 C C   . VAL A 419 ? 0.74273 0.73636 0.78249 -0.02279 -0.06514 -0.09667 419 VAL A C   
6475 O O   . VAL A 419 ? 0.71364 0.70247 0.80309 -0.03197 -0.08178 -0.09822 419 VAL A O   
6476 C CB  . VAL A 419 ? 0.78741 0.75444 0.79094 0.00063  -0.06345 -0.11200 419 VAL A CB  
6477 C CG1 . VAL A 419 ? 0.93889 0.90559 0.91180 0.01318  -0.04087 -0.10841 419 VAL A CG1 
6478 C CG2 . VAL A 419 ? 0.80642 0.74182 0.78698 0.02103  -0.09786 -0.13889 419 VAL A CG2 
6488 N N   . PHE A 420 ? 0.70345 0.70589 0.72915 -0.02323 -0.06152 -0.09302 420 PHE A N   
6489 C CA  . PHE A 420 ? 0.65273 0.65840 0.71882 -0.03315 -0.07937 -0.09344 420 PHE A CA  
6490 C C   . PHE A 420 ? 0.55519 0.58127 0.68114 -0.05381 -0.06703 -0.07342 420 PHE A C   
6491 O O   . PHE A 420 ? 0.55694 0.58044 0.73987 -0.06135 -0.08356 -0.07242 420 PHE A O   
6492 C CB  . PHE A 420 ? 0.65865 0.67216 0.69714 -0.02961 -0.07330 -0.09050 420 PHE A CB  
6493 C CG  . PHE A 420 ? 0.70314 0.71759 0.78035 -0.03598 -0.09437 -0.09341 420 PHE A CG  
6494 C CD1 . PHE A 420 ? 0.74534 0.73590 0.84018 -0.02729 -0.13302 -0.11386 420 PHE A CD1 
6495 C CD2 . PHE A 420 ? 0.63085 0.66843 0.73039 -0.04877 -0.07821 -0.07710 420 PHE A CD2 
6496 C CE1 . PHE A 420 ? 0.73819 0.73024 0.88043 -0.03339 -0.15511 -0.11608 420 PHE A CE1 
6497 C CE2 . PHE A 420 ? 0.63160 0.67175 0.77359 -0.05396 -0.09556 -0.07788 420 PHE A CE2 
6498 C CZ  . PHE A 420 ? 0.67931 0.69782 0.84686 -0.04734 -0.13410 -0.09646 420 PHE A CZ  
6508 N N   . GLY A 421 ? 0.50345 0.54816 0.61926 -0.06024 -0.03854 -0.05636 421 GLY A N   
6509 C CA  . GLY A 421 ? 0.53456 0.59613 0.69030 -0.07241 -0.02324 -0.03554 421 GLY A CA  
6510 C C   . GLY A 421 ? 0.55535 0.61019 0.75735 -0.07684 -0.02947 -0.02970 421 GLY A C   
6511 O O   . GLY A 421 ? 0.53491 0.60085 0.78285 -0.08423 -0.01889 -0.00946 421 GLY A O   
6515 N N   . LYS A 422 ? 0.57337 0.60957 0.76618 -0.07031 -0.04442 -0.04496 422 LYS A N   
6516 C CA  . LYS A 422 ? 0.56387 0.59188 0.80494 -0.07447 -0.05174 -0.03961 422 LYS A CA  
6517 C C   . LYS A 422 ? 0.51430 0.53977 0.83031 -0.08222 -0.06933 -0.03493 422 LYS A C   
6518 O O   . LYS A 422 ? 0.51280 0.54072 0.88848 -0.08934 -0.06467 -0.01669 422 LYS A O   
6519 C CB  . LYS A 422 ? 0.59010 0.59465 0.80673 -0.06293 -0.06937 -0.06199 422 LYS A CB  
6520 C CG  . LYS A 422 ? 0.65369 0.64751 0.92091 -0.06664 -0.07856 -0.05802 422 LYS A CG  
6521 C CD  . LYS A 422 ? 0.87446 0.85380 1.10407 -0.05506 -0.07944 -0.07141 422 LYS A CD  
6522 C CE  . LYS A 422 ? 0.97043 0.91961 1.17518 -0.03711 -0.11070 -0.10461 422 LYS A CE  
6523 N NZ  . LYS A 422 ? 1.04091 0.97297 1.22810 -0.02492 -0.11337 -0.11600 422 LYS A NZ  
6537 N N   . LYS A 423 ? 0.64178 0.66229 0.96198 -0.08013 -0.08957 -0.04903 423 LYS A N   
6538 C CA  . LYS A 423 ? 0.61061 0.62886 1.01488 -0.08760 -0.11054 -0.04544 423 LYS A CA  
6539 C C   . LYS A 423 ? 0.54728 0.59267 1.00503 -0.09900 -0.07828 -0.00850 423 LYS A C   
6540 O O   . LYS A 423 ? 0.54752 0.59513 1.09442 -0.10656 -0.08143 0.00888  423 LYS A O   
6541 C CB  . LYS A 423 ? 0.73310 0.74027 1.12329 -0.08051 -0.14009 -0.06882 423 LYS A CB  
6542 C CG  . LYS A 423 ? 0.71602 0.72696 1.19955 -0.08948 -0.15961 -0.06213 423 LYS A CG  
6543 C CD  . LYS A 423 ? 0.72584 0.71843 1.19020 -0.07856 -0.19898 -0.09142 423 LYS A CD  
6544 C CE  . LYS A 423 ? 1.00387 1.00255 1.57041 -0.08821 -0.21966 -0.08395 423 LYS A CE  
6545 N NZ  . LYS A 423 ? 1.14459 1.12460 1.68846 -0.07570 -0.26071 -0.11280 423 LYS A NZ  
6559 N N   . TYR A 424 ? 0.53282 0.59741 0.94030 -0.09771 -0.04719 0.00456  424 TYR A N   
6560 C CA  . TYR A 424 ? 0.50976 0.59741 0.94757 -0.10094 -0.01363 0.03796  424 TYR A CA  
6561 C C   . TYR A 424 ? 0.50736 0.60188 0.92331 -0.09692 0.01711  0.06073  424 TYR A C   
6562 O O   . TYR A 424 ? 0.43331 0.54048 0.88868 -0.09535 0.04352  0.09277  424 TYR A O   
6563 C CB  . TYR A 424 ? 0.51540 0.61639 0.90701 -0.09762 -0.00111 0.03615  424 TYR A CB  
6564 C CG  . TYR A 424 ? 0.44977 0.54321 0.84549 -0.09839 -0.03052 0.01329  424 TYR A CG  
6565 C CD1 . TYR A 424 ? 0.48030 0.55867 0.81046 -0.09156 -0.04950 -0.01455 424 TYR A CD1 
6566 C CD2 . TYR A 424 ? 0.39432 0.49517 0.85988 -0.10321 -0.03791 0.02184  424 TYR A CD2 
6567 C CE1 . TYR A 424 ? 0.55126 0.61963 0.87613 -0.08744 -0.07641 -0.03398 424 TYR A CE1 
6568 C CE2 . TYR A 424 ? 0.43787 0.52966 0.90533 -0.10179 -0.06883 -0.00004 424 TYR A CE2 
6569 C CZ  . TYR A 424 ? 0.52578 0.60008 0.91827 -0.09290 -0.08872 -0.02828 424 TYR A CZ  
6570 O OH  . TYR A 424 ? 0.51691 0.57926 0.90367 -0.08700 -0.11963 -0.04854 424 TYR A OH  
6580 N N   . ASP A 425 ? 0.43695 0.52273 0.79101 -0.09249 0.01487  0.04628  425 ASP A N   
6581 C CA  . ASP A 425 ? 0.49300 0.58404 0.80986 -0.08572 0.03945  0.06265  425 ASP A CA  
6582 C C   . ASP A 425 ? 0.44373 0.51981 0.75124 -0.08537 0.02717  0.05165  425 ASP A C   
6583 O O   . ASP A 425 ? 0.46415 0.53678 0.71646 -0.08071 0.02593  0.03766  425 ASP A O   
6584 C CB  . ASP A 425 ? 0.50560 0.60465 0.75268 -0.07892 0.05007  0.05552  425 ASP A CB  
6585 C CG  . ASP A 425 ? 0.52660 0.62880 0.73561 -0.06801 0.07024  0.07090  425 ASP A CG  
6586 O OD1 . ASP A 425 ? 0.48996 0.59101 0.72263 -0.06383 0.08316  0.09337  425 ASP A OD1 
6587 O OD2 . ASP A 425 ? 0.56413 0.66813 0.72095 -0.06197 0.07089  0.06021  425 ASP A OD2 
6592 N N   . PRO A 426 ? 0.42592 0.49278 0.79516 -0.08989 0.01776  0.05881  426 PRO A N   
6593 C CA  . PRO A 426 ? 0.45308 0.50345 0.81592 -0.08843 0.00373  0.04582  426 PRO A CA  
6594 C C   . PRO A 426 ? 0.45469 0.50895 0.77495 -0.08154 0.02360  0.05860  426 PRO A C   
6595 O O   . PRO A 426 ? 0.52320 0.56688 0.81791 -0.07853 0.01388  0.04298  426 PRO A O   
6596 C CB  . PRO A 426 ? 0.44881 0.48978 0.90138 -0.09485 -0.00864 0.05682  426 PRO A CB  
6597 C CG  . PRO A 426 ? 0.45383 0.51188 0.96037 -0.09839 0.01182  0.08805  426 PRO A CG  
6598 C CD  . PRO A 426 ? 0.40372 0.47420 0.86085 -0.09631 0.01796  0.07894  426 PRO A CD  
6606 N N   . GLU A 427 ? 0.51951 0.58687 0.82983 -0.07577 0.05025  0.08626  427 GLU A N   
6607 C CA  . GLU A 427 ? 0.53361 0.60118 0.79688 -0.06504 0.06352  0.09587  427 GLU A CA  
6608 C C   . GLU A 427 ? 0.59569 0.66705 0.79287 -0.06002 0.06031  0.07645  427 GLU A C   
6609 O O   . GLU A 427 ? 0.58805 0.65663 0.74993 -0.05148 0.06184  0.07681  427 GLU A O   
6610 C CB  . GLU A 427 ? 0.66113 0.73619 0.93010 -0.05346 0.09229  0.13317  427 GLU A CB  
6611 C CG  . GLU A 427 ? 0.78904 0.85757 1.11047 -0.05243 0.10079  0.15985  427 GLU A CG  
6612 C CD  . GLU A 427 ? 0.93808 0.99696 1.22048 -0.04269 0.09959  0.16112  427 GLU A CD  
6613 O OE1 . GLU A 427 ? 1.07927 1.13871 1.29328 -0.03130 0.09971  0.15185  427 GLU A OE1 
6614 O OE2 . GLU A 427 ? 0.96829 1.01779 1.29275 -0.04609 0.09531  0.17000  427 GLU A OE2 
6621 N N   . GLY A 428 ? 0.50106 0.57764 0.68705 -0.06467 0.05378  0.06004  428 GLY A N   
6622 C CA  . GLY A 428 ? 0.46242 0.54284 0.59919 -0.06066 0.05126  0.04464  428 GLY A CA  
6623 C C   . GLY A 428 ? 0.54975 0.63626 0.65187 -0.04872 0.06391  0.05626  428 GLY A C   
6624 O O   . GLY A 428 ? 0.50371 0.58838 0.57234 -0.04222 0.05785  0.04664  428 GLY A O   
6628 N N   . ARG A 429 ? 0.55509 0.64751 0.66683 -0.04309 0.08054  0.07656  429 ARG A N   
6629 C CA  A ARG A 429 ? 0.59374 0.68784 0.66114 -0.02506 0.09232  0.08538  429 ARG A CA  
6630 C CA  B ARG A 429 ? 0.59569 0.68986 0.66330 -0.02510 0.09241  0.08545  429 ARG A CA  
6631 C C   . ARG A 429 ? 0.58399 0.68106 0.62168 -0.02546 0.08099  0.06319  429 ARG A C   
6632 O O   . ARG A 429 ? 0.54804 0.63971 0.54537 -0.01234 0.07419  0.05542  429 ARG A O   
6633 C CB  A ARG A 429 ? 0.63447 0.73520 0.72027 -0.01608 0.11770  0.11369  429 ARG A CB  
6634 C CB  B ARG A 429 ? 0.63450 0.73556 0.72090 -0.01645 0.11759  0.11330  429 ARG A CB  
6635 C CG  A ARG A 429 ? 0.68756 0.78595 0.81400 -0.01428 0.13276  0.14235  429 ARG A CG  
6636 C CG  B ARG A 429 ? 0.69199 0.79038 0.81110 -0.01113 0.13503  0.14391  429 ARG A CG  
6637 C CD  A ARG A 429 ? 0.77885 0.88177 0.90270 0.00704  0.16668  0.17854  429 ARG A CD  
6638 C CD  B ARG A 429 ? 0.76214 0.87018 0.91077 -0.00101 0.16589  0.17680  429 ARG A CD  
6639 N NE  A ARG A 429 ? 0.85351 0.95107 0.99928 0.01637  0.18425  0.21031  429 ARG A NE  
6640 N NE  B ARG A 429 ? 0.75657 0.87583 0.94557 -0.01577 0.16161  0.16789  429 ARG A NE  
6641 C CZ  A ARG A 429 ? 0.89238 0.97720 0.99234 0.03092  0.18089  0.21254  429 ARG A CZ  
6642 C CZ  B ARG A 429 ? 0.75167 0.87503 1.01791 -0.03472 0.15347  0.16996  429 ARG A CZ  
6643 N NH1 A ARG A 429 ? 0.99740 1.07365 1.03344 0.03727  0.15842  0.18392  429 ARG A NH1 
6644 N NH1 B ARG A 429 ? 0.73602 0.85348 1.05372 -0.04225 0.14991  0.18132  429 ARG A NH1 
6645 N NH2 A ARG A 429 ? 0.84432 0.92449 0.96974 0.03974  0.19927  0.24541  429 ARG A NH2 
6646 N NH2 B ARG A 429 ? 0.65766 0.78906 0.95206 -0.04506 0.14511  0.15887  429 ARG A NH2 
6673 N N   . PHE A 430 ? 0.58515 0.68875 0.64532 -0.03902 0.07601  0.05251  430 PHE A N   
6674 C CA  . PHE A 430 ? 0.52058 0.62724 0.56041 -0.04012 0.06716  0.03490  430 PHE A CA  
6675 C C   . PHE A 430 ? 0.51595 0.61731 0.54141 -0.04099 0.05241  0.01896  430 PHE A C   
6676 O O   . PHE A 430 ? 0.54756 0.64774 0.55265 -0.03397 0.04495  0.00986  430 PHE A O   
6677 C CB  . PHE A 430 ? 0.49711 0.60930 0.56395 -0.05301 0.06354  0.02833  430 PHE A CB  
6678 C CG  . PHE A 430 ? 0.55187 0.66746 0.60254 -0.05389 0.05723  0.01450  430 PHE A CG  
6679 C CD1 . PHE A 430 ? 0.58477 0.70639 0.62874 -0.04818 0.06424  0.01798  430 PHE A CD1 
6680 C CD2 . PHE A 430 ? 0.57490 0.68756 0.62089 -0.05866 0.04697  0.00077  430 PHE A CD2 
6681 C CE1 . PHE A 430 ? 0.54721 0.67093 0.58186 -0.04931 0.05741  0.00601  430 PHE A CE1 
6682 C CE2 . PHE A 430 ? 0.53416 0.64994 0.57323 -0.05903 0.04359  -0.00729 430 PHE A CE2 
6683 C CZ  . PHE A 430 ? 0.48638 0.60734 0.52085 -0.05540 0.04707  -0.00556 430 PHE A CZ  
6693 N N   . ILE A 431 ? 0.53022 0.62757 0.57209 -0.04827 0.04731  0.01556  431 ILE A N   
6694 C CA  . ILE A 431 ? 0.47316 0.56743 0.51200 -0.04831 0.03764  0.00440  431 ILE A CA  
6695 C C   . ILE A 431 ? 0.49550 0.58448 0.51709 -0.03646 0.03113  0.00624  431 ILE A C   
6696 O O   . ILE A 431 ? 0.58173 0.66984 0.60118 -0.03278 0.01947  -0.00375 431 ILE A O   
6697 C CB  . ILE A 431 ? 0.51264 0.60198 0.56941 -0.05425 0.03621  0.00128  431 ILE A CB  
6698 C CG1 . ILE A 431 ? 0.53842 0.62775 0.60075 -0.05973 0.03562  -0.00686 431 ILE A CG1 
6699 C CG2 . ILE A 431 ? 0.51820 0.60514 0.57776 -0.05111 0.03113  -0.00421 431 ILE A CG2 
6700 C CD1 . ILE A 431 ? 0.60265 0.68155 0.67699 -0.06075 0.03065  -0.01190 431 ILE A CD1 
6712 N N   . ARG A 432 ? 0.54700 0.63081 0.55938 -0.02847 0.03686  0.01983  432 ARG A N   
6713 C CA  . ARG A 432 ? 0.57056 0.64517 0.55732 -0.01222 0.02801  0.02143  432 ARG A CA  
6714 C C   . ARG A 432 ? 0.62449 0.69525 0.57778 0.00305  0.02013  0.01418  432 ARG A C   
6715 O O   . ARG A 432 ? 0.58715 0.64802 0.52380 0.01580  0.00024  0.00363  432 ARG A O   
6716 C CB  . ARG A 432 ? 0.57668 0.64543 0.55618 -0.00304 0.04038  0.04260  432 ARG A CB  
6717 C CG  . ARG A 432 ? 0.54695 0.61545 0.56282 -0.01605 0.04295  0.04744  432 ARG A CG  
6718 C CD  . ARG A 432 ? 0.62728 0.69137 0.64914 -0.00864 0.05851  0.07326  432 ARG A CD  
6719 N NE  . ARG A 432 ? 0.61336 0.67728 0.68241 -0.02363 0.06046  0.07696  432 ARG A NE  
6720 C CZ  . ARG A 432 ? 0.65352 0.71036 0.73764 -0.02686 0.05138  0.07263  432 ARG A CZ  
6721 N NH1 . ARG A 432 ? 0.64991 0.70152 0.71150 -0.01800 0.04055  0.06631  432 ARG A NH1 
6722 N NH2 . ARG A 432 ? 0.61573 0.66919 0.74215 -0.03801 0.05034  0.07318  432 ARG A NH2 
6736 N N   . LYS A 433 ? 0.58130 0.65796 0.52729 0.00345  0.03218  0.01777  433 LYS A N   
6737 C CA  . LYS A 433 ? 0.56597 0.63677 0.47801 0.02051  0.02443  0.00888  433 LYS A CA  
6738 C C   . LYS A 433 ? 0.55392 0.62469 0.48368 0.01336  0.00158  -0.01325 433 LYS A C   
6739 O O   . LYS A 433 ? 0.67774 0.73611 0.58943 0.02892  -0.02111 -0.02711 433 LYS A O   
6740 C CB  . LYS A 433 ? 0.63757 0.71647 0.54566 0.02187  0.04526  0.01942  433 LYS A CB  
6741 C CG  . LYS A 433 ? 0.64008 0.71554 0.52505 0.03334  0.03634  0.00506  433 LYS A CG  
6742 C CD  . LYS A 433 ? 0.74979 0.80578 0.57849 0.06592  0.02391  -0.00108 433 LYS A CD  
6743 C CE  . LYS A 433 ? 0.90584 0.95544 0.70847 0.08162  0.01613  -0.01559 433 LYS A CE  
6744 N NZ  . LYS A 433 ? 0.96426 0.99637 0.75570 0.09284  -0.02298 -0.04370 433 LYS A NZ  
6758 N N   . PHE A 434 ? 0.60341 0.68607 0.57108 -0.00773 0.00610  -0.01600 434 PHE A N   
6759 C CA  . PHE A 434 ? 0.61381 0.69861 0.60683 -0.01397 -0.00834 -0.02991 434 PHE A CA  
6760 C C   . PHE A 434 ? 0.62878 0.71408 0.65689 -0.02078 -0.01819 -0.03335 434 PHE A C   
6761 O O   . PHE A 434 ? 0.54550 0.63117 0.60447 -0.02240 -0.03207 -0.04199 434 PHE A O   
6762 C CB  . PHE A 434 ? 0.61381 0.70990 0.62364 -0.02763 0.00483  -0.02778 434 PHE A CB  
6763 C CG  . PHE A 434 ? 0.59105 0.68778 0.57885 -0.02065 0.01031  -0.02743 434 PHE A CG  
6764 C CD1 . PHE A 434 ? 0.63614 0.72623 0.61491 -0.00969 -0.00465 -0.03975 434 PHE A CD1 
6765 C CD2 . PHE A 434 ? 0.57904 0.68200 0.56136 -0.02366 0.02876  -0.01516 434 PHE A CD2 
6766 C CE1 . PHE A 434 ? 0.66326 0.75315 0.61970 -0.00039 0.00210  -0.03969 434 PHE A CE1 
6767 C CE2 . PHE A 434 ? 0.63165 0.73681 0.59988 -0.01583 0.03684  -0.01230 434 PHE A CE2 
6768 C CZ  . PHE A 434 ? 0.61017 0.70880 0.56110 -0.00327 0.02501  -0.02464 434 PHE A CZ  
6778 N N   . LEU A 435 ? 0.57671 0.66204 0.60803 -0.02402 -0.01095 -0.02551 435 LEU A N   
6779 C CA  . LEU A 435 ? 0.58747 0.67315 0.65227 -0.02746 -0.01806 -0.02717 435 LEU A CA  
6780 C C   . LEU A 435 ? 0.62566 0.70099 0.67257 -0.01650 -0.02782 -0.02487 435 LEU A C   
6781 O O   . LEU A 435 ? 0.60806 0.68373 0.65681 -0.02037 -0.01697 -0.01623 435 LEU A O   
6782 C CB  . LEU A 435 ? 0.57534 0.66909 0.66057 -0.03918 0.00085  -0.02080 435 LEU A CB  
6783 C CG  . LEU A 435 ? 0.56597 0.66745 0.66094 -0.04601 0.01257  -0.02028 435 LEU A CG  
6784 C CD1 . LEU A 435 ? 0.52172 0.62399 0.61500 -0.04958 0.02876  -0.01596 435 LEU A CD1 
6785 C CD2 . LEU A 435 ? 0.59295 0.69895 0.72735 -0.04608 0.00657  -0.02189 435 LEU A CD2 
6797 N N   . PRO A 436 ? 0.59714 0.66039 0.62458 -0.00011 -0.05069 -0.03340 436 PRO A N   
6798 C CA  . PRO A 436 ? 0.61242 0.66254 0.61103 0.01566  -0.06032 -0.02956 436 PRO A CA  
6799 C C   . PRO A 436 ? 0.60743 0.65856 0.64280 0.01002  -0.06661 -0.02807 436 PRO A C   
6800 O O   . PRO A 436 ? 0.64912 0.69113 0.66386 0.02003  -0.06904 -0.02080 436 PRO A O   
6801 C CB  . PRO A 436 ? 0.68711 0.71991 0.65543 0.03881  -0.09076 -0.04487 436 PRO A CB  
6802 C CG  . PRO A 436 ? 0.73199 0.77016 0.72836 0.03129  -0.09951 -0.05798 436 PRO A CG  
6803 C CD  . PRO A 436 ? 0.65339 0.71101 0.67497 0.00853  -0.06906 -0.04721 436 PRO A CD  
6811 N N   . VAL A 437 ? 0.55452 0.61619 0.64469 -0.00332 -0.06707 -0.03221 437 VAL A N   
6812 C CA  . VAL A 437 ? 0.53902 0.60351 0.66769 -0.00753 -0.06726 -0.02852 437 VAL A CA  
6813 C C   . VAL A 437 ? 0.57992 0.64585 0.69282 -0.01295 -0.04414 -0.01650 437 VAL A C   
6814 O O   . VAL A 437 ? 0.56672 0.62958 0.69508 -0.01120 -0.04650 -0.01291 437 VAL A O   
6815 C CB  . VAL A 437 ? 0.57670 0.65432 0.76887 -0.01817 -0.06183 -0.02917 437 VAL A CB  
6816 C CG1 . VAL A 437 ? 0.56775 0.65600 0.75416 -0.02879 -0.03307 -0.02290 437 VAL A CG1 
6817 C CG2 . VAL A 437 ? 0.64272 0.72366 0.87837 -0.01904 -0.05988 -0.02402 437 VAL A CG2 
6827 N N   . LEU A 438 ? 0.55170 0.62097 0.63996 -0.01897 -0.02485 -0.01100 438 LEU A N   
6828 C CA  . LEU A 438 ? 0.55574 0.62418 0.63925 -0.02445 -0.00808 -0.00197 438 LEU A CA  
6829 C C   . LEU A 438 ? 0.58387 0.64416 0.63561 -0.01644 -0.00496 0.01017  438 LEU A C   
6830 O O   . LEU A 438 ? 0.60319 0.66266 0.66006 -0.02203 0.00819  0.01953  438 LEU A O   
6831 C CB  . LEU A 438 ? 0.53812 0.61362 0.62536 -0.03497 0.00785  -0.00363 438 LEU A CB  
6832 C CG  . LEU A 438 ? 0.57489 0.65583 0.68881 -0.03853 0.01487  -0.00873 438 LEU A CG  
6833 C CD1 . LEU A 438 ? 0.52863 0.61480 0.63477 -0.04293 0.02519  -0.01134 438 LEU A CD1 
6834 C CD2 . LEU A 438 ? 0.65598 0.73090 0.77878 -0.03759 0.02109  -0.00786 438 LEU A CD2 
6846 N N   . LYS A 439 ? 0.63001 0.68239 0.65084 -0.00064 -0.01701 0.01109  439 LYS A N   
6847 C CA  . LYS A 439 ? 0.66467 0.70990 0.64901 0.01230  -0.00626 0.02776  439 LYS A CA  
6848 C C   . LYS A 439 ? 0.66742 0.70609 0.65865 0.01500  0.00064  0.04418  439 LYS A C   
6849 O O   . LYS A 439 ? 0.71166 0.74855 0.69464 0.01945  0.01896  0.06467  439 LYS A O   
6850 C CB  . LYS A 439 ? 0.71025 0.74349 0.64756 0.03644  -0.02196 0.02326  439 LYS A CB  
6851 C CG  . LYS A 439 ? 0.80524 0.82427 0.73303 0.05225  -0.04903 0.01599  439 LYS A CG  
6852 C CD  . LYS A 439 ? 0.99615 0.99916 0.87633 0.07856  -0.07383 0.00246  439 LYS A CD  
6853 C CE  . LYS A 439 ? 1.08105 1.06161 0.91561 0.10862  -0.09244 0.00640  439 LYS A CE  
6854 N NZ  . LYS A 439 ? 1.24647 1.22326 1.12094 0.10452  -0.12248 -0.00676 439 LYS A NZ  
6868 N N   . ASP A 440 ? 0.69519 0.73067 0.70881 0.01276  -0.01225 0.03799  440 ASP A N   
6869 C CA  . ASP A 440 ? 0.65509 0.68312 0.67891 0.01546  -0.00766 0.05282  440 ASP A CA  
6870 C C   . ASP A 440 ? 0.66037 0.69349 0.72897 -0.00291 0.00077  0.04987  440 ASP A C   
6871 O O   . ASP A 440 ? 0.66252 0.68862 0.74796 -0.00214 0.00212  0.05930  440 ASP A O   
6872 C CB  . ASP A 440 ? 0.74707 0.76439 0.76238 0.03018  -0.03042 0.04858  440 ASP A CB  
6873 C CG  . ASP A 440 ? 0.79668 0.80045 0.75525 0.05679  -0.04298 0.05170  440 ASP A CG  
6874 O OD1 . ASP A 440 ? 0.84541 0.84321 0.76812 0.07047  -0.02492 0.07261  440 ASP A OD1 
6875 O OD2 . ASP A 440 ? 1.04550 1.04304 0.99720 0.06669  -0.07147 0.03356  440 ASP A OD2 
6880 N N   . MET A 441 ? 0.62308 0.66546 0.70736 -0.01609 0.00514  0.03652  441 MET A N   
6881 C CA  . MET A 441 ? 0.57497 0.61694 0.68900 -0.02708 0.01095  0.03076  441 MET A CA  
6882 C C   . MET A 441 ? 0.59475 0.63139 0.72141 -0.03091 0.01978  0.04471  441 MET A C   
6883 O O   . MET A 441 ? 0.61923 0.65991 0.73691 -0.03120 0.02822  0.05472  441 MET A O   
6884 C CB  . MET A 441 ? 0.59225 0.64231 0.70779 -0.03423 0.01419  0.01566  441 MET A CB  
6885 C CG  . MET A 441 ? 0.60525 0.65152 0.73781 -0.03672 0.01698  0.00394  441 MET A CG  
6886 S SD  . MET A 441 ? 0.64331 0.68175 0.79855 -0.03043 0.01322  0.00268  441 MET A SD  
6887 C CE  . MET A 441 ? 0.57617 0.62567 0.74285 -0.02571 0.01654  -0.00387 441 MET A CE  
6897 N N   . PRO A 442 ? 0.60363 0.63101 0.75870 -0.03328 0.01794  0.04673  442 PRO A N   
6898 C CA  . PRO A 442 ? 0.58445 0.60621 0.76983 -0.03895 0.02288  0.05879  442 PRO A CA  
6899 C C   . PRO A 442 ? 0.54768 0.57259 0.74134 -0.04777 0.02153  0.04582  442 PRO A C   
6900 O O   . PRO A 442 ? 0.58725 0.61237 0.76844 -0.04884 0.01548  0.02421  442 PRO A O   
6901 C CB  . PRO A 442 ? 0.60398 0.61268 0.82064 -0.03927 0.01477  0.05510  442 PRO A CB  
6902 C CG  . PRO A 442 ? 0.59677 0.60584 0.79482 -0.03064 0.01106  0.05384  442 PRO A CG  
6903 C CD  . PRO A 442 ? 0.60388 0.62458 0.77178 -0.02939 0.01034  0.04088  442 PRO A CD  
6911 N N   . ALA A 443 ? 0.57797 0.60488 0.79517 -0.05189 0.02832  0.06159  443 ALA A N   
6912 C CA  . ALA A 443 ? 0.59673 0.62705 0.82400 -0.05931 0.02446  0.05062  443 ALA A CA  
6913 C C   . ALA A 443 ? 0.61826 0.63483 0.86160 -0.06209 0.00529  0.02475  443 ALA A C   
6914 O O   . ALA A 443 ? 0.61839 0.63492 0.84754 -0.06293 -0.00203 0.00709  443 ALA A O   
6915 C CB  . ALA A 443 ? 0.63846 0.67299 0.90662 -0.06287 0.03501  0.07544  443 ALA A CB  
6921 N N   . LYS A 444 ? 0.61601 0.61822 0.88451 -0.06025 -0.00406 0.02151  444 LYS A N   
6922 C CA  . LYS A 444 ? 0.63971 0.62344 0.91544 -0.05670 -0.02483 -0.00626 444 LYS A CA  
6923 C C   . LYS A 444 ? 0.55171 0.53626 0.77352 -0.04729 -0.02349 -0.02794 444 LYS A C   
6924 O O   . LYS A 444 ? 0.63199 0.60260 0.84069 -0.03964 -0.03745 -0.05082 444 LYS A O   
6925 C CB  . LYS A 444 ? 0.74642 0.71405 1.05346 -0.05357 -0.03372 -0.00640 444 LYS A CB  
6926 C CG  . LYS A 444 ? 0.81587 0.75922 1.12234 -0.04376 -0.05709 -0.03841 444 LYS A CG  
6927 C CD  . LYS A 444 ? 0.94383 0.87358 1.26552 -0.03725 -0.06139 -0.04072 444 LYS A CD  
6928 C CE  . LYS A 444 ? 0.91773 0.83955 1.30969 -0.04619 -0.06893 -0.02169 444 LYS A CE  
6929 N NZ  . LYS A 444 ? 1.14450 1.08390 1.54200 -0.05151 -0.04506 0.01420  444 LYS A NZ  
6943 N N   . TYR A 445 ? 0.57156 0.57061 0.76422 -0.04520 -0.00771 -0.02009 445 TYR A N   
6944 C CA  . TYR A 445 ? 0.61433 0.61655 0.77065 -0.03611 -0.00160 -0.03373 445 TYR A CA  
6945 C C   . TYR A 445 ? 0.59852 0.61845 0.73208 -0.03962 0.00916  -0.02815 445 TYR A C   
6946 O O   . TYR A 445 ? 0.56598 0.59028 0.67865 -0.03244 0.01706  -0.03458 445 TYR A O   
6947 C CB  . TYR A 445 ? 0.61831 0.62151 0.77498 -0.02922 0.00501  -0.03149 445 TYR A CB  
6948 C CG  . TYR A 445 ? 0.66001 0.64716 0.84245 -0.02616 -0.00440 -0.03358 445 TYR A CG  
6949 C CD1 . TYR A 445 ? 0.67627 0.64289 0.85631 -0.01486 -0.01497 -0.05415 445 TYR A CD1 
6950 C CD2 . TYR A 445 ? 0.65260 0.64237 0.85832 -0.03124 -0.00393 -0.01546 445 TYR A CD2 
6951 C CE1 . TYR A 445 ? 0.60873 0.55849 0.81632 -0.01134 -0.02614 -0.05800 445 TYR A CE1 
6952 C CE2 . TYR A 445 ? 0.75934 0.73411 0.99332 -0.02861 -0.01228 -0.01554 445 TYR A CE2 
6953 C CZ  . TYR A 445 ? 0.72870 0.68396 0.96716 -0.02000 -0.02388 -0.03744 445 TYR A CZ  
6954 O OH  . TYR A 445 ? 0.74634 0.68484 1.01673 -0.01688 -0.03451 -0.03912 445 TYR A OH  
6964 N N   . ILE A 446 ? 0.56830 0.59789 0.70830 -0.04840 0.01141  -0.01483 446 ILE A N   
6965 C CA  . ILE A 446 ? 0.56511 0.60978 0.68438 -0.04989 0.01976  -0.01018 446 ILE A CA  
6966 C C   . ILE A 446 ? 0.54078 0.58683 0.64213 -0.04831 0.02024  -0.02227 446 ILE A C   
6967 O O   . ILE A 446 ? 0.55063 0.60728 0.63812 -0.04751 0.02719  -0.02120 446 ILE A O   
6968 C CB  . ILE A 446 ? 0.53235 0.58460 0.65563 -0.05427 0.02428  0.00693  446 ILE A CB  
6969 C CG1 . ILE A 446 ? 0.55275 0.61664 0.65115 -0.05205 0.02886  0.00788  446 ILE A CG1 
6970 C CG2 . ILE A 446 ? 0.49295 0.54317 0.63700 -0.06035 0.02175  0.00872  446 ILE A CG2 
6971 C CD1 . ILE A 446 ? 0.58082 0.64704 0.66682 -0.04569 0.03212  0.02258  446 ILE A CD1 
6983 N N   . TYR A 447 ? 0.50865 0.54214 0.61154 -0.04614 0.01035  -0.03403 447 TYR A N   
6984 C CA  . TYR A 447 ? 0.53653 0.56735 0.61389 -0.03963 0.00930  -0.04565 447 TYR A CA  
6985 C C   . TYR A 447 ? 0.61300 0.63400 0.66449 -0.02299 0.01487  -0.05605 447 TYR A C   
6986 O O   . TYR A 447 ? 0.56451 0.58673 0.58927 -0.01379 0.02300  -0.05851 447 TYR A O   
6987 C CB  . TYR A 447 ? 0.56329 0.58208 0.65196 -0.04110 -0.00912 -0.05537 447 TYR A CB  
6988 C CG  . TYR A 447 ? 0.54055 0.57307 0.65047 -0.05379 -0.00742 -0.04283 447 TYR A CG  
6989 C CD1 . TYR A 447 ? 0.53283 0.57404 0.62397 -0.05406 -0.00359 -0.04358 447 TYR A CD1 
6990 C CD2 . TYR A 447 ? 0.53577 0.57281 0.68525 -0.06313 -0.00608 -0.02716 447 TYR A CD2 
6991 C CE1 . TYR A 447 ? 0.52533 0.57916 0.63575 -0.06334 0.00002  -0.03197 447 TYR A CE1 
6992 C CE2 . TYR A 447 ? 0.54246 0.59253 0.71042 -0.07039 0.00126  -0.01231 447 TYR A CE2 
6993 C CZ  . TYR A 447 ? 0.52454 0.58298 0.67229 -0.07050 0.00369  -0.01616 447 TYR A CZ  
6994 O OH  . TYR A 447 ? 0.51874 0.58984 0.68445 -0.07542 0.01255  -0.00169 447 TYR A OH  
7004 N N   . GLU A 448 ? 0.58011 0.59109 0.63930 -0.01659 0.01334  -0.05980 448 GLU A N   
7005 C CA  . GLU A 448 ? 0.62814 0.62993 0.66440 0.00310  0.02361  -0.06686 448 GLU A CA  
7006 C C   . GLU A 448 ? 0.62889 0.63850 0.68977 0.00102  0.03309  -0.05712 448 GLU A C   
7007 O O   . GLU A 448 ? 0.62468 0.62072 0.69208 0.00858  0.02773  -0.06415 448 GLU A O   
7008 C CB  . GLU A 448 ? 0.66359 0.63702 0.67874 0.02030  0.00613  -0.08846 448 GLU A CB  
7009 C CG  . GLU A 448 ? 0.78965 0.75217 0.78431 0.02369  -0.01100 -0.10072 448 GLU A CG  
7010 C CD  . GLU A 448 ? 0.89713 0.82935 0.89190 0.03448  -0.04258 -0.12465 448 GLU A CD  
7011 O OE1 . GLU A 448 ? 0.86772 0.79772 0.91120 0.01923  -0.05835 -0.12367 448 GLU A OE1 
7012 O OE2 . GLU A 448 ? 1.07124 0.98008 1.01833 0.06047  -0.05256 -0.14385 448 GLU A OE2 
7019 N N   . PRO A 449 ? 0.62638 0.65599 0.70386 -0.00797 0.04373  -0.04250 449 PRO A N   
7020 C CA  . PRO A 449 ? 0.65911 0.69511 0.76489 -0.01054 0.04571  -0.03413 449 PRO A CA  
7021 C C   . PRO A 449 ? 0.63162 0.66178 0.74140 0.00603  0.05785  -0.03660 449 PRO A C   
7022 O O   . PRO A 449 ? 0.59822 0.62755 0.73186 0.00567  0.05475  -0.03367 449 PRO A O   
7023 C CB  . PRO A 449 ? 0.60546 0.66021 0.72582 -0.01872 0.04948  -0.02290 449 PRO A CB  
7024 C CG  . PRO A 449 ? 0.53784 0.59712 0.63918 -0.01807 0.05653  -0.02393 449 PRO A CG  
7025 C CD  . PRO A 449 ? 0.53811 0.58289 0.61213 -0.01531 0.04937  -0.03503 449 PRO A CD  
7033 N N   . TRP A 450 ? 0.65731 0.68249 0.74231 0.02350  0.07327  -0.04025 450 TRP A N   
7034 C CA  . TRP A 450 ? 0.68438 0.70289 0.76850 0.04505  0.09046  -0.04036 450 TRP A CA  
7035 C C   . TRP A 450 ? 0.66384 0.65856 0.73443 0.05520  0.07655  -0.05725 450 TRP A C   
7036 O O   . TRP A 450 ? 0.66119 0.64944 0.73477 0.07307  0.08893  -0.05811 450 TRP A O   
7037 C CB  . TRP A 450 ? 0.66105 0.67697 0.71179 0.06782  0.11446  -0.03694 450 TRP A CB  
7038 C CG  . TRP A 450 ? 0.76649 0.76186 0.76256 0.07802  0.10167  -0.05388 450 TRP A CG  
7039 C CD1 . TRP A 450 ? 0.78392 0.75049 0.73576 0.10246  0.09293  -0.07381 450 TRP A CD1 
7040 C CD2 . TRP A 450 ? 0.69690 0.69651 0.67892 0.06613  0.09176  -0.05465 450 TRP A CD2 
7041 N NE1 . TRP A 450 ? 0.84477 0.79680 0.75793 0.10644  0.07519  -0.08757 450 TRP A NE1 
7042 C CE2 . TRP A 450 ? 0.77448 0.74794 0.70719 0.08341  0.07597  -0.07476 450 TRP A CE2 
7043 C CE3 . TRP A 450 ? 0.63059 0.65165 0.63730 0.04458  0.09235  -0.04200 450 TRP A CE3 
7044 C CZ2 . TRP A 450 ? 0.77664 0.74714 0.68926 0.07790  0.06166  -0.08057 450 TRP A CZ2 
7045 C CZ3 . TRP A 450 ? 0.68228 0.70078 0.66584 0.03965  0.08168  -0.04719 450 TRP A CZ3 
7046 C CH2 . TRP A 450 ? 0.69104 0.68574 0.63067 0.05525  0.06708  -0.06522 450 TRP A CH2 
7057 N N   . THR A 451 ? 0.66363 0.64493 0.72640 0.04524  0.05132  -0.06982 451 THR A N   
7058 C CA  . THR A 451 ? 0.68833 0.64561 0.75244 0.05232  0.03259  -0.08612 451 THR A CA  
7059 C C   . THR A 451 ? 0.65236 0.61530 0.76188 0.03580  0.02413  -0.07658 451 THR A C   
7060 O O   . THR A 451 ? 0.63055 0.57476 0.75152 0.04153  0.01082  -0.08696 451 THR A O   
7061 C CB  . THR A 451 ? 0.66852 0.60705 0.71865 0.04998  0.00627  -0.10300 451 THR A CB  
7062 O OG1 . THR A 451 ? 0.62507 0.57944 0.70608 0.02317  -0.00165 -0.08980 451 THR A OG1 
7063 C CG2 . THR A 451 ? 0.70497 0.63375 0.70308 0.06968  0.01000  -0.11400 451 THR A CG2 
7071 N N   . ALA A 452 ? 0.63267 0.61792 0.76570 0.01824  0.02928  -0.05798 452 ALA A N   
7072 C CA  . ALA A 452 ? 0.67930 0.66704 0.84560 0.00659  0.02016  -0.04728 452 ALA A CA  
7073 C C   . ALA A 452 ? 0.74473 0.72818 0.92856 0.01848  0.02578  -0.04803 452 ALA A C   
7074 O O   . ALA A 452 ? 0.68245 0.67422 0.86526 0.03017  0.04316  -0.04639 452 ALA A O   
7075 C CB  . ALA A 452 ? 0.64655 0.65471 0.82176 -0.00693 0.02232  -0.03023 452 ALA A CB  
7081 N N   . PRO A 453 ? 0.76944 0.74073 0.97593 0.01650  0.01332  -0.04783 453 PRO A N   
7082 C CA  . PRO A 453 ? 0.84279 0.81243 1.07137 0.02637  0.01806  -0.04613 453 PRO A CA  
7083 C C   . PRO A 453 ? 0.82157 0.81386 1.06880 0.02171  0.02644  -0.03035 453 PRO A C   
7084 O O   . PRO A 453 ? 0.72634 0.72968 0.97442 0.00897  0.01952  -0.01924 453 PRO A O   
7085 C CB  . PRO A 453 ? 0.89957 0.85509 1.15412 0.01981  0.00081  -0.04265 453 PRO A CB  
7086 C CG  . PRO A 453 ? 0.75916 0.70467 1.00930 0.01058  -0.01170 -0.04627 453 PRO A CG  
7087 C CD  . PRO A 453 ? 0.79081 0.74978 1.01224 0.00568  -0.00426 -0.04637 453 PRO A CD  
7095 N N   . LEU A 454 ? 0.88369 0.88143 1.14816 0.03483  0.04055  -0.02997 454 LEU A N   
7096 C CA  . LEU A 454 ? 0.81458 0.83373 1.10883 0.03179  0.04655  -0.01699 454 LEU A CA  
7097 C C   . LEU A 454 ? 0.78829 0.81107 1.10606 0.02136  0.02560  -0.00716 454 LEU A C   
7098 O O   . LEU A 454 ? 0.73029 0.76672 1.06415 0.01622  0.01887  -0.00007 454 LEU A O   
7099 C CB  . LEU A 454 ? 0.93072 0.95479 1.25124 0.04986  0.06864  -0.01509 454 LEU A CB  
7100 C CG  . LEU A 454 ? 0.98268 1.02854 1.35786 0.04794  0.07324  -0.00050 454 LEU A CG  
7101 C CD1 . LEU A 454 ? 0.98994 1.04670 1.38477 0.06501  0.10689  0.00756  454 LEU A CD1 
7102 C CD2 . LEU A 454 ? 0.96014 1.00359 1.37430 0.04841  0.05855  0.00258  454 LEU A CD2 
7114 N N   . GLU A 455 ? 0.78006 0.78853 1.09954 0.02056  0.01314  -0.00661 455 GLU A N   
7115 C CA  . GLU A 455 ? 0.77348 0.78175 1.10115 0.01494  -0.00595 0.00530  455 GLU A CA  
7116 C C   . GLU A 455 ? 0.73589 0.74331 1.02975 0.00569  -0.01286 0.01168  455 GLU A C   
7117 O O   . GLU A 455 ? 0.66960 0.67856 0.95624 0.00609  -0.02615 0.02158  455 GLU A O   
7118 C CB  . GLU A 455 ? 0.84990 0.84303 1.19487 0.01938  -0.01374 0.00852  455 GLU A CB  
7119 C CG  . GLU A 455 ? 0.89707 0.87315 1.22826 0.01496  -0.01598 0.00811  455 GLU A CG  
7120 C CD  . GLU A 455 ? 1.09086 1.05416 1.42313 0.02232  -0.00854 -0.01022 455 GLU A CD  
7121 O OE1 . GLU A 455 ? 1.09361 1.06174 1.42909 0.03380  0.00415  -0.01985 455 GLU A OE1 
7122 O OE2 . GLU A 455 ? 1.16202 1.10890 1.49358 0.01930  -0.01580 -0.01456 455 GLU A OE2 
7129 N N   . VAL A 456 ? 0.68455 0.68766 0.95665 0.00051  -0.00514 0.00609  456 VAL A N   
7130 C CA  . VAL A 456 ? 0.73852 0.74493 0.98411 -0.00732 -0.00696 0.01310  456 VAL A CA  
7131 C C   . VAL A 456 ? 0.65876 0.68030 0.89385 -0.00820 -0.00664 0.01120  456 VAL A C   
7132 O O   . VAL A 456 ? 0.59503 0.61916 0.81196 -0.00844 -0.01498 0.01883  456 VAL A O   
7133 C CB  . VAL A 456 ? 0.70830 0.70717 0.94424 -0.01263 -0.00181 0.00598  456 VAL A CB  
7134 C CG1 . VAL A 456 ? 0.70098 0.70593 0.91661 -0.02012 -0.00055 0.01485  456 VAL A CG1 
7135 C CG2 . VAL A 456 ? 0.71994 0.70113 0.97848 -0.01200 -0.00791 0.00725  456 VAL A CG2 
7145 N N   . GLN A 457 ? 0.65947 0.68950 0.90675 -0.00580 0.00356  0.00205  457 GLN A N   
7146 C CA  . GLN A 457 ? 0.63248 0.67679 0.88500 -0.00714 0.00345  0.00188  457 GLN A CA  
7147 C C   . GLN A 457 ? 0.66815 0.71515 0.94178 -0.00374 -0.01637 0.00658  457 GLN A C   
7148 O O   . GLN A 457 ? 0.63886 0.68897 0.90129 -0.00440 -0.02956 0.00640  457 GLN A O   
7149 C CB  . GLN A 457 ? 0.62833 0.68102 0.90119 -0.00169 0.02258  -0.00207 457 GLN A CB  
7150 C CG  . GLN A 457 ? 0.63593 0.68228 0.87733 0.00101  0.03835  -0.00962 457 GLN A CG  
7151 C CD  . GLN A 457 ? 0.60671 0.66052 0.85818 0.01243  0.06155  -0.00882 457 GLN A CD  
7152 O OE1 . GLN A 457 ? 0.60822 0.67696 0.89616 0.01266  0.06720  0.00016  457 GLN A OE1 
7153 N NE2 . GLN A 457 ? 0.68027 0.72185 0.90127 0.02475  0.07452  -0.01733 457 GLN A NE2 
7162 N N   . ARG A 458 ? 0.75225 0.79572 1.05618 0.00228  -0.02186 0.00881  458 ARG A N   
7163 C CA  . ARG A 458 ? 0.85975 0.90251 1.18556 0.00810  -0.04681 0.01133  458 ARG A CA  
7164 C C   . ARG A 458 ? 0.74863 0.77903 1.02744 0.01220  -0.06465 0.01640  458 ARG A C   
7165 O O   . ARG A 458 ? 0.77635 0.80484 1.04526 0.01859  -0.08654 0.01341  458 ARG A O   
7166 C CB  . ARG A 458 ? 0.78365 0.82316 1.14858 0.01447  -0.04913 0.01397  458 ARG A CB  
7167 C CG  . ARG A 458 ? 0.74943 0.80264 1.17347 0.01722  -0.03494 0.01292  458 ARG A CG  
7168 C CD  . ARG A 458 ? 0.78578 0.83375 1.24077 0.02486  -0.03209 0.01553  458 ARG A CD  
7169 N NE  . ARG A 458 ? 0.95722 1.01256 1.44388 0.03189  -0.00278 0.01580  458 ARG A NE  
7170 C CZ  . ARG A 458 ? 0.83123 0.90298 1.35843 0.03532  0.01593  0.02039  458 ARG A CZ  
7171 N NH1 . ARG A 458 ? 0.98630 1.06919 1.52860 0.02851  0.00799  0.02248  458 ARG A NH1 
7172 N NH2 . ARG A 458 ? 0.84622 0.92238 1.40168 0.04823  0.04478  0.02459  458 ARG A NH2 
7186 N N   . LYS A 459 ? 0.73883 0.75900 0.99000 0.01147  -0.05543 0.02492  459 LYS A N   
7187 C CA  . LYS A 459 ? 0.81682 0.82546 1.02406 0.01943  -0.06390 0.03684  459 LYS A CA  
7188 C C   . LYS A 459 ? 0.77537 0.78799 0.94620 0.01913  -0.06290 0.03444  459 LYS A C   
7189 O O   . LYS A 459 ? 0.73358 0.73799 0.86910 0.03311  -0.07885 0.03727  459 LYS A O   
7190 C CB  . LYS A 459 ? 0.78384 0.78341 0.98585 0.01648  -0.04877 0.05053  459 LYS A CB  
7191 C CG  . LYS A 459 ? 0.99961 0.98494 1.17506 0.03051  -0.05521 0.07093  459 LYS A CG  
7192 C CD  . LYS A 459 ? 1.06645 1.04558 1.24497 0.02554  -0.03599 0.08917  459 LYS A CD  
7193 C CE  . LYS A 459 ? 1.15549 1.12699 1.29110 0.04020  -0.02923 0.11402  459 LYS A CE  
7194 N NZ  . LYS A 459 ? 1.18254 1.14773 1.34035 0.03698  -0.00995 0.13924  459 LYS A NZ  
7208 N N   . ALA A 460 ? 0.70216 0.72497 0.87686 0.00656  -0.04567 0.02823  460 ALA A N   
7209 C CA  . ALA A 460 ? 0.69892 0.72622 0.84332 0.00528  -0.04308 0.02599  460 ALA A CA  
7210 C C   . ALA A 460 ? 0.68572 0.71835 0.83896 0.00900  -0.06110 0.01337  460 ALA A C   
7211 O O   . ALA A 460 ? 0.70927 0.74362 0.83726 0.01022  -0.06298 0.00952  460 ALA A O   
7212 C CB  . ALA A 460 ? 0.65667 0.69164 0.80542 -0.00828 -0.02228 0.02269  460 ALA A CB  
7218 N N   . GLY A 461 ? 0.72025 0.75521 0.91599 0.01115  -0.07534 0.00721  461 GLY A N   
7219 C CA  . GLY A 461 ? 0.66726 0.70748 0.89158 0.01318  -0.09500 -0.00409 461 GLY A CA  
7220 C C   . GLY A 461 ? 0.66678 0.72169 0.91041 0.00117  -0.07695 -0.00782 461 GLY A C   
7221 O O   . GLY A 461 ? 0.68354 0.74046 0.93334 0.00220  -0.09078 -0.01549 461 GLY A O   
7225 N N   . CYS A 462 ? 0.64836 0.71095 0.89983 -0.00755 -0.04823 -0.00325 462 CYS A N   
7226 C CA  . CYS A 462 ? 0.63221 0.70636 0.89370 -0.01492 -0.02851 -0.00440 462 CYS A CA  
7227 C C   . CYS A 462 ? 0.61126 0.69043 0.89840 -0.01453 -0.00427 -0.00044 462 CYS A C   
7228 O O   . CYS A 462 ? 0.57912 0.65230 0.83702 -0.01502 0.01042  -0.00100 462 CYS A O   
7229 C CB  . CYS A 462 ? 0.76904 0.84065 0.97994 -0.01965 -0.01922 -0.00494 462 CYS A CB  
7230 S SG  . CYS A 462 ? 0.66783 0.75091 0.88349 -0.02603 0.00008  -0.00644 462 CYS A SG  
7236 N N   . VAL A 463 ? 0.56217 0.65099 0.90672 -0.01121 -0.00095 0.00348  463 VAL A N   
7237 C CA  . VAL A 463 ? 0.62268 0.71628 0.99156 -0.00471 0.02648  0.00972  463 VAL A CA  
7238 C C   . VAL A 463 ? 0.57392 0.67648 0.94276 -0.00321 0.05204  0.01516  463 VAL A C   
7239 O O   . VAL A 463 ? 0.54424 0.65746 0.95070 -0.00658 0.04925  0.02036  463 VAL A O   
7240 C CB  . VAL A 463 ? 0.70132 0.80205 1.14066 0.00087  0.02168  0.01617  463 VAL A CB  
7241 C CG1 . VAL A 463 ? 0.54043 0.64751 1.00516 0.01226  0.05734  0.02594  463 VAL A CG1 
7242 C CG2 . VAL A 463 ? 0.61716 0.70641 1.04999 0.00217  -0.00363 0.01140  463 VAL A CG2 
7252 N N   . VAL A 464 ? 0.55735 0.65302 0.88407 0.00390  0.07436  0.01346  464 VAL A N   
7253 C CA  . VAL A 464 ? 0.63619 0.73666 0.95063 0.01046  0.09951  0.01961  464 VAL A CA  
7254 C C   . VAL A 464 ? 0.62268 0.73731 1.00040 0.02128  0.12413  0.03770  464 VAL A C   
7255 O O   . VAL A 464 ? 0.57908 0.69408 0.98393 0.03238  0.13623  0.04303  464 VAL A O   
7256 C CB  . VAL A 464 ? 0.65808 0.74262 0.90965 0.02146  0.11193  0.01054  464 VAL A CB  
7257 C CG1 . VAL A 464 ? 0.60870 0.69480 0.83975 0.03524  0.13902  0.01814  464 VAL A CG1 
7258 C CG2 . VAL A 464 ? 0.65967 0.73322 0.86794 0.00859  0.08810  -0.00311 464 VAL A CG2 
7268 N N   . GLY A 465 ? 0.60883 0.73563 1.01751 0.01866  0.13299  0.04939  465 GLY A N   
7269 C CA  . GLY A 465 ? 0.62610 0.76906 1.11322 0.02697  0.15695  0.07215  465 GLY A CA  
7270 C C   . GLY A 465 ? 0.57127 0.72559 1.14579 0.01394  0.12898  0.07469  465 GLY A C   
7271 O O   . GLY A 465 ? 0.52649 0.69590 1.18332 0.01646  0.14354  0.09481  465 GLY A O   
7275 N N   . ARG A 466 ? 0.57648 0.72209 1.13700 0.00264  0.08817  0.05559  466 ARG A N   
7276 C CA  . ARG A 466 ? 0.59497 0.74443 1.22503 -0.00544 0.05125  0.05149  466 ARG A CA  
7277 C C   . ARG A 466 ? 0.57187 0.71267 1.16535 -0.01534 0.01749  0.03475  466 ARG A C   
7278 O O   . ARG A 466 ? 0.42814 0.57420 1.07586 -0.01962 0.00223  0.03595  466 ARG A O   
7279 C CB  . ARG A 466 ? 0.58372 0.72649 1.22490 -0.00300 0.02932  0.04370  466 ARG A CB  
7280 C CG  . ARG A 466 ? 0.88608 1.02362 1.56926 -0.00753 -0.02119 0.03126  466 ARG A CG  
7281 C CD  . ARG A 466 ? 0.90539 1.03542 1.59836 -0.00220 -0.04131 0.02607  466 ARG A CD  
7282 N NE  . ARG A 466 ? 0.99880 1.10938 1.61031 -0.00175 -0.07127 0.00918  466 ARG A NE  
7283 C CZ  . ARG A 466 ? 1.02755 1.12770 1.60416 0.00304  -0.07603 0.00680  466 ARG A CZ  
7284 N NH1 . ARG A 466 ? 0.75313 0.85911 1.36656 0.00727  -0.05703 0.01596  466 ARG A NH1 
7285 N NH2 . ARG A 466 ? 1.01890 1.10192 1.52320 0.00565  -0.09818 -0.00293 466 ARG A NH2 
7299 N N   . ASP A 467 ? 0.57355 0.70056 1.08022 -0.01743 0.00653  0.02028  467 ASP A N   
7300 C CA  . ASP A 467 ? 0.53121 0.64907 0.99442 -0.02232 -0.02031 0.00618  467 ASP A CA  
7301 C C   . ASP A 467 ? 0.48850 0.60804 0.90283 -0.02630 0.00111  0.00774  467 ASP A C   
7302 O O   . ASP A 467 ? 0.52020 0.63813 0.92711 -0.02989 -0.01368 0.00119  467 ASP A O   
7303 C CB  . ASP A 467 ? 0.57978 0.68202 0.98284 -0.01932 -0.04250 -0.00542 467 ASP A CB  
7304 C CG  . ASP A 467 ? 0.67634 0.77428 1.11809 -0.01317 -0.06452 -0.00696 467 ASP A CG  
7305 O OD1 . ASP A 467 ? 0.62858 0.72691 1.12975 -0.01065 -0.09308 -0.01163 467 ASP A OD1 
7306 O OD2 . ASP A 467 ? 0.64638 0.73934 1.06450 -0.01035 -0.05633 -0.00425 467 ASP A OD2 
7311 N N   . TYR A 468 ? 0.52434 0.64475 0.90463 -0.02350 0.03246  0.01439  468 TYR A N   
7312 C CA  . TYR A 468 ? 0.46793 0.58783 0.80156 -0.02476 0.05044  0.01510  468 TYR A CA  
7313 C C   . TYR A 468 ? 0.47903 0.60376 0.82077 -0.01387 0.08670  0.02900  468 TYR A C   
7314 O O   . TYR A 468 ? 0.52225 0.64417 0.86682 -0.00506 0.09839  0.03159  468 TYR A O   
7315 C CB  . TYR A 468 ? 0.48243 0.59040 0.74594 -0.02764 0.04353  0.00404  468 TYR A CB  
7316 C CG  . TYR A 468 ? 0.54009 0.64662 0.76155 -0.02924 0.05547  0.00266  468 TYR A CG  
7317 C CD1 . TYR A 468 ? 0.55859 0.66794 0.77290 -0.03542 0.04562  -0.00026 468 TYR A CD1 
7318 C CD2 . TYR A 468 ? 0.54008 0.64000 0.72844 -0.02221 0.07316  0.00222  468 TYR A CD2 
7319 C CE1 . TYR A 468 ? 0.50670 0.61496 0.68621 -0.03666 0.05523  -0.00121 468 TYR A CE1 
7320 C CE2 . TYR A 468 ? 0.53683 0.63319 0.68799 -0.02181 0.07881  -0.00077 468 TYR A CE2 
7321 C CZ  . TYR A 468 ? 0.43795 0.53990 0.58742 -0.03014 0.07077  -0.00125 468 TYR A CZ  
7322 O OH  . TYR A 468 ? 0.54926 0.64792 0.66587 -0.02948 0.07514  -0.00384 468 TYR A OH  
7332 N N   . PRO A 469 ? 0.49177 0.62194 0.83401 -0.01067 0.10612  0.03896  469 PRO A N   
7333 C CA  . PRO A 469 ? 0.56052 0.69368 0.90726 0.00683  0.14464  0.05652  469 PRO A CA  
7334 C C   . PRO A 469 ? 0.59792 0.71512 0.86864 0.01965  0.15512  0.04664  469 PRO A C   
7335 O O   . PRO A 469 ? 0.57546 0.68138 0.79402 0.01233  0.13567  0.02911  469 PRO A O   
7336 C CB  . PRO A 469 ? 0.52323 0.66337 0.88085 0.00752  0.15883  0.06974  469 PRO A CB  
7337 C CG  . PRO A 469 ? 0.53689 0.67273 0.86451 -0.00873 0.12839  0.05213  469 PRO A CG  
7338 C CD  . PRO A 469 ? 0.59490 0.72794 0.93495 -0.01957 0.09550  0.03684  469 PRO A CD  
7346 N N   . ALA A 470 ? 0.54996 0.66519 0.82048 0.04151  0.18603  0.05870  470 ALA A N   
7347 C CA  . ALA A 470 ? 0.66641 0.76208 0.86241 0.06138  0.19632  0.04838  470 ALA A CA  
7348 C C   . ALA A 470 ? 0.70883 0.79784 0.85428 0.07152  0.20705  0.05079  470 ALA A C   
7349 O O   . ALA A 470 ? 0.64158 0.74372 0.81818 0.06768  0.21877  0.06793  470 ALA A O   
7350 C CB  . ALA A 470 ? 0.59053 0.68376 0.79576 0.08794  0.22798  0.06072  470 ALA A CB  
7356 N N   . PRO A 471 ? 0.78874 0.85558 0.85975 0.08554  0.20005  0.03305  471 PRO A N   
7357 C CA  . PRO A 471 ? 0.80349 0.86106 0.82247 0.09756  0.20525  0.03328  471 PRO A CA  
7358 C C   . PRO A 471 ? 0.78264 0.84607 0.80704 0.12350  0.24821  0.06260  471 PRO A C   
7359 O O   . PRO A 471 ? 0.76471 0.82814 0.79980 0.14611  0.27770  0.07704  471 PRO A O   
7360 C CB  . PRO A 471 ? 0.81891 0.84711 0.76434 0.11547  0.18812  0.00740  471 PRO A CB  
7361 C CG  . PRO A 471 ? 0.81314 0.83882 0.78169 0.10049  0.16606  -0.00800 471 PRO A CG  
7362 C CD  . PRO A 471 ? 0.74291 0.78996 0.77895 0.09219  0.18317  0.01092  471 PRO A CD  
7370 N N   . ILE A 472 ? 0.78746 0.85623 0.80771 0.12145  0.25410  0.07414  472 ILE A N   
7371 C CA  . ILE A 472 ? 0.89585 0.97142 0.92868 0.14582  0.29803  0.10829  472 ILE A CA  
7372 C C   . ILE A 472 ? 0.88346 0.93296 0.82235 0.19031  0.31995  0.10975  472 ILE A C   
7373 O O   . ILE A 472 ? 0.96973 1.02156 0.90863 0.22025  0.36490  0.14229  472 ILE A O   
7374 C CB  . ILE A 472 ? 0.93039 1.02136 1.00262 0.12772  0.29709  0.12338  472 ILE A CB  
7375 C CG1 . ILE A 472 ? 0.93561 1.01487 0.95364 0.11375  0.26084  0.09685  472 ILE A CG1 
7376 C CG2 . ILE A 472 ? 0.92749 1.04314 1.10342 0.09654  0.28659  0.13125  472 ILE A CG2 
7377 C CD1 . ILE A 472 ? 0.97757 1.05918 0.98834 0.11799  0.27139  0.11311  472 ILE A CD1 
7389 N N   . VAL A 473 ? 0.89487 0.91782 0.75556 0.19829  0.28868  0.07622  473 VAL A N   
7390 C CA  . VAL A 473 ? 1.16563 1.15652 0.92690 0.24503  0.29888  0.06980  473 VAL A CA  
7391 C C   . VAL A 473 ? 1.10713 1.07187 0.82221 0.25573  0.27019  0.03425  473 VAL A C   
7392 O O   . VAL A 473 ? 1.07526 1.04125 0.81492 0.22310  0.22960  0.00854  473 VAL A O   
7393 C CB  . VAL A 473 ? 1.13530 1.11334 0.84326 0.24903  0.28069  0.06228  473 VAL A CB  
7394 C CG1 . VAL A 473 ? 1.17015 1.16433 0.90086 0.25864  0.32141  0.10306  473 VAL A CG1 
7395 C CG2 . VAL A 473 ? 1.11836 1.10505 0.85905 0.20378  0.23318  0.03729  473 VAL A CG2 
7405 N N   . ASP A 474 ? 1.22732 1.16704 0.87634 0.30419  0.29265  0.03433  474 ASP A N   
7406 C CA  . ASP A 474 ? 1.32079 1.23062 0.92321 0.32137  0.26571  -0.00057 474 ASP A CA  
7407 C C   . ASP A 474 ? 1.35629 1.24133 0.91842 0.31052  0.20724  -0.04093 474 ASP A C   
7408 O O   . ASP A 474 ? 1.36101 1.24502 0.90427 0.30467  0.19380  -0.04139 474 ASP A O   
7409 C CB  . ASP A 474 ? 1.28233 1.16448 0.81381 0.37558  0.29030  0.00705  474 ASP A CB  
7410 C CG  . ASP A 474 ? 1.40168 1.27600 0.94229 0.38719  0.29457  -0.00366 474 ASP A CG  
7411 O OD1 . ASP A 474 ? 1.44617 1.31707 1.00825 0.36638  0.26276  -0.03446 474 ASP A OD1 
7412 O OD2 . ASP A 474 ? 1.39638 1.26710 0.92908 0.41397  0.32567  0.02075  474 ASP A OD2 
7417 N N   . HIS A 475 ? 1.22926 1.09458 0.78686 0.30785  0.17223  -0.07340 475 HIS A N   
# 
