data_9OB6
# 
_entry.id   9OB6 
# 
_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   9OB6         pdb_00009ob6 10.2210/pdb9ob6/pdb 
WWPDB D_1000295107 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9OB6 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
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 mholliday@relaytx.com MICHAEL HOLLIDAY ? 'principal investigator/group leader' 0000-0002-1112-9892 
3 jpbaird@alumni.iu.edu Jason   Baird    ? 'principal investigator/group leader' 0009-0006-0823-7565 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Baird, J.'      1 0000-0002-1112-9892 
'Holliday, M.H.' 2 0009-0006-0823-7565 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Nanoscale direct-to-biology optimization of Cdk2 inhibitors' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Douthwaite, J.L.' 1  ? 
primary 'Houde, D.J.'      2  ? 
primary 'Pardo, E.'        3  ? 
primary 'Moran, M.S.'      4  ? 
primary 'Baird, J.'        5  ? 
primary 'Meyer, S.R.'      6  ? 
primary 'Mahjour, B.'      7  ? 
primary 'Zhao, Q.'         8  ? 
primary 'Larrow, J.F.'     9  ? 
primary 'Juang, Y.'        10 ? 
primary 'Han, C.K.'        11 ? 
primary 'Kelley, B.'       12 ? 
primary 'Dunstan, D.R.'    13 ? 
primary 'Holliday, M.J.'   14 ? 
primary 'Billings, K.J.'   15 ? 
primary 'Mader, M.M.'      16 ? 
primary 'Taylor, A.M.'     17 ? 
primary 'Sexton, J.Z.'     18 ? 
primary 'Boezio, A.A.'     19 ? 
primary 'Cernak, T.'       20 ? 
# 
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 'Cyclin-dependent kinase 2'                                                                    34412.895 1  
2.7.11.22 ? ? ? 
2 polymer     man 'G1/S-specific cyclin-E1'                                                                      33053.500 1  ? ? 
? ? 
3 non-polymer syn '(1R,3R)-3-{3-[2-(4-methoxyphenyl)acetamido]-1H-pyrazol-5-yl}cyclopentyl propan-2-ylcarbamate' 400.471   1  ? ? 
? ? 
4 water       nat water                                                                                          18.015    58 ? ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cell division protein kinase 2,p33 protein kinase' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no yes 
;SHMMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLY
LVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVR
TY(TPO)HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSM
PDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
;SHMMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLY
LVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVR
TYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYK
PSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
A ? 
2 'polypeptide(L)' no no  
;GSIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFF
DRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVY
MQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVP
FAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKA
;
;GSIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFF
DRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVY
MQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVP
FAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKA
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '(1R,3R)-3-{3-[2-(4-methoxyphenyl)acetamido]-1H-pyrazol-5-yl}cyclopentyl propan-2-ylcarbamate' A1CAI 
4 water                                                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   HIS n 
1 3   MET n 
1 4   MET n 
1 5   GLU n 
1 6   ASN n 
1 7   PHE n 
1 8   GLN n 
1 9   LYS n 
1 10  VAL n 
1 11  GLU n 
1 12  LYS n 
1 13  ILE n 
1 14  GLY n 
1 15  GLU n 
1 16  GLY n 
1 17  THR n 
1 18  TYR n 
1 19  GLY n 
1 20  VAL n 
1 21  VAL n 
1 22  TYR n 
1 23  LYS n 
1 24  ALA n 
1 25  ARG n 
1 26  ASN n 
1 27  LYS n 
1 28  LEU n 
1 29  THR n 
1 30  GLY n 
1 31  GLU n 
1 32  VAL n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  LYS n 
1 37  LYS n 
1 38  ILE n 
1 39  ARG n 
1 40  LEU n 
1 41  ASP n 
1 42  THR n 
1 43  GLU n 
1 44  THR n 
1 45  GLU n 
1 46  GLY n 
1 47  VAL n 
1 48  PRO n 
1 49  SER n 
1 50  THR n 
1 51  ALA n 
1 52  ILE n 
1 53  ARG n 
1 54  GLU n 
1 55  ILE n 
1 56  SER n 
1 57  LEU n 
1 58  LEU n 
1 59  LYS n 
1 60  GLU n 
1 61  LEU n 
1 62  ASN n 
1 63  HIS n 
1 64  PRO n 
1 65  ASN n 
1 66  ILE n 
1 67  VAL n 
1 68  LYS n 
1 69  LEU n 
1 70  LEU n 
1 71  ASP n 
1 72  VAL n 
1 73  ILE n 
1 74  HIS n 
1 75  THR n 
1 76  GLU n 
1 77  ASN n 
1 78  LYS n 
1 79  LEU n 
1 80  TYR n 
1 81  LEU n 
1 82  VAL n 
1 83  PHE n 
1 84  GLU n 
1 85  PHE n 
1 86  LEU n 
1 87  HIS n 
1 88  GLN n 
1 89  ASP n 
1 90  LEU n 
1 91  LYS n 
1 92  LYS n 
1 93  PHE n 
1 94  MET n 
1 95  ASP n 
1 96  ALA n 
1 97  SER n 
1 98  ALA n 
1 99  LEU n 
1 100 THR n 
1 101 GLY n 
1 102 ILE n 
1 103 PRO n 
1 104 LEU n 
1 105 PRO n 
1 106 LEU n 
1 107 ILE n 
1 108 LYS n 
1 109 SER n 
1 110 TYR n 
1 111 LEU n 
1 112 PHE n 
1 113 GLN n 
1 114 LEU n 
1 115 LEU n 
1 116 GLN n 
1 117 GLY n 
1 118 LEU n 
1 119 ALA n 
1 120 PHE n 
1 121 CYS n 
1 122 HIS n 
1 123 SER n 
1 124 HIS n 
1 125 ARG n 
1 126 VAL n 
1 127 LEU n 
1 128 HIS n 
1 129 ARG n 
1 130 ASP n 
1 131 LEU n 
1 132 LYS n 
1 133 PRO n 
1 134 GLN n 
1 135 ASN n 
1 136 LEU n 
1 137 LEU n 
1 138 ILE n 
1 139 ASN n 
1 140 THR n 
1 141 GLU n 
1 142 GLY n 
1 143 ALA n 
1 144 ILE n 
1 145 LYS n 
1 146 LEU n 
1 147 ALA n 
1 148 ASP n 
1 149 PHE n 
1 150 GLY n 
1 151 LEU n 
1 152 ALA n 
1 153 ARG n 
1 154 ALA n 
1 155 PHE n 
1 156 GLY n 
1 157 VAL n 
1 158 PRO n 
1 159 VAL n 
1 160 ARG n 
1 161 THR n 
1 162 TYR n 
1 163 TPO n 
1 164 HIS n 
1 165 GLU n 
1 166 VAL n 
1 167 VAL n 
1 168 THR n 
1 169 LEU n 
1 170 TRP n 
1 171 TYR n 
1 172 ARG n 
1 173 ALA n 
1 174 PRO n 
1 175 GLU n 
1 176 ILE n 
1 177 LEU n 
1 178 LEU n 
1 179 GLY n 
1 180 CYS n 
1 181 LYS n 
1 182 TYR n 
1 183 TYR n 
1 184 SER n 
1 185 THR n 
1 186 ALA n 
1 187 VAL n 
1 188 ASP n 
1 189 ILE n 
1 190 TRP n 
1 191 SER n 
1 192 LEU n 
1 193 GLY n 
1 194 CYS n 
1 195 ILE n 
1 196 PHE n 
1 197 ALA n 
1 198 GLU n 
1 199 MET n 
1 200 VAL n 
1 201 THR n 
1 202 ARG n 
1 203 ARG n 
1 204 ALA n 
1 205 LEU n 
1 206 PHE n 
1 207 PRO n 
1 208 GLY n 
1 209 ASP n 
1 210 SER n 
1 211 GLU n 
1 212 ILE n 
1 213 ASP n 
1 214 GLN n 
1 215 LEU n 
1 216 PHE n 
1 217 ARG n 
1 218 ILE n 
1 219 PHE n 
1 220 ARG n 
1 221 THR n 
1 222 LEU n 
1 223 GLY n 
1 224 THR n 
1 225 PRO n 
1 226 ASP n 
1 227 GLU n 
1 228 VAL n 
1 229 VAL n 
1 230 TRP n 
1 231 PRO n 
1 232 GLY n 
1 233 VAL n 
1 234 THR n 
1 235 SER n 
1 236 MET n 
1 237 PRO n 
1 238 ASP n 
1 239 TYR n 
1 240 LYS n 
1 241 PRO n 
1 242 SER n 
1 243 PHE n 
1 244 PRO n 
1 245 LYS n 
1 246 TRP n 
1 247 ALA n 
1 248 ARG n 
1 249 GLN n 
1 250 ASP n 
1 251 PHE n 
1 252 SER n 
1 253 LYS n 
1 254 VAL n 
1 255 VAL n 
1 256 PRO n 
1 257 PRO n 
1 258 LEU n 
1 259 ASP n 
1 260 GLU n 
1 261 ASP n 
1 262 GLY n 
1 263 ARG n 
1 264 SER n 
1 265 LEU n 
1 266 LEU n 
1 267 SER n 
1 268 GLN n 
1 269 MET n 
1 270 LEU n 
1 271 HIS n 
1 272 TYR n 
1 273 ASP n 
1 274 PRO n 
1 275 ASN n 
1 276 LYS n 
1 277 ARG n 
1 278 ILE n 
1 279 SER n 
1 280 ALA n 
1 281 LYS n 
1 282 ALA n 
1 283 ALA n 
1 284 LEU n 
1 285 ALA n 
1 286 HIS n 
1 287 PRO n 
1 288 PHE n 
1 289 PHE n 
1 290 GLN n 
1 291 ASP n 
1 292 VAL n 
1 293 THR n 
1 294 LYS n 
1 295 PRO n 
1 296 VAL n 
1 297 PRO n 
1 298 HIS n 
1 299 LEU n 
1 300 ARG n 
1 301 LEU n 
2 1   GLY n 
2 2   SER n 
2 3   ILE n 
2 4   ILE n 
2 5   ALA n 
2 6   PRO n 
2 7   SER n 
2 8   ARG n 
2 9   GLY n 
2 10  SER n 
2 11  PRO n 
2 12  LEU n 
2 13  PRO n 
2 14  VAL n 
2 15  LEU n 
2 16  SER n 
2 17  TRP n 
2 18  ALA n 
2 19  ASN n 
2 20  ARG n 
2 21  GLU n 
2 22  GLU n 
2 23  VAL n 
2 24  TRP n 
2 25  LYS n 
2 26  ILE n 
2 27  MET n 
2 28  LEU n 
2 29  ASN n 
2 30  LYS n 
2 31  GLU n 
2 32  LYS n 
2 33  THR n 
2 34  TYR n 
2 35  LEU n 
2 36  ARG n 
2 37  ASP n 
2 38  GLN n 
2 39  HIS n 
2 40  PHE n 
2 41  LEU n 
2 42  GLU n 
2 43  GLN n 
2 44  HIS n 
2 45  PRO n 
2 46  LEU n 
2 47  LEU n 
2 48  GLN n 
2 49  PRO n 
2 50  LYS n 
2 51  MET n 
2 52  ARG n 
2 53  ALA n 
2 54  ILE n 
2 55  LEU n 
2 56  LEU n 
2 57  ASP n 
2 58  TRP n 
2 59  LEU n 
2 60  MET n 
2 61  GLU n 
2 62  VAL n 
2 63  CYS n 
2 64  GLU n 
2 65  VAL n 
2 66  TYR n 
2 67  LYS n 
2 68  LEU n 
2 69  HIS n 
2 70  ARG n 
2 71  GLU n 
2 72  THR n 
2 73  PHE n 
2 74  TYR n 
2 75  LEU n 
2 76  ALA n 
2 77  GLN n 
2 78  ASP n 
2 79  PHE n 
2 80  PHE n 
2 81  ASP n 
2 82  ARG n 
2 83  TYR n 
2 84  MET n 
2 85  ALA n 
2 86  THR n 
2 87  GLN n 
2 88  GLU n 
2 89  ASN n 
2 90  VAL n 
2 91  VAL n 
2 92  LYS n 
2 93  THR n 
2 94  LEU n 
2 95  LEU n 
2 96  GLN n 
2 97  LEU n 
2 98  ILE n 
2 99  GLY n 
2 100 ILE n 
2 101 SER n 
2 102 SER n 
2 103 LEU n 
2 104 PHE n 
2 105 ILE n 
2 106 ALA n 
2 107 ALA n 
2 108 LYS n 
2 109 LEU n 
2 110 GLU n 
2 111 GLU n 
2 112 ILE n 
2 113 TYR n 
2 114 PRO n 
2 115 PRO n 
2 116 LYS n 
2 117 LEU n 
2 118 HIS n 
2 119 GLN n 
2 120 PHE n 
2 121 ALA n 
2 122 TYR n 
2 123 VAL n 
2 124 THR n 
2 125 ASP n 
2 126 GLY n 
2 127 ALA n 
2 128 CYS n 
2 129 SER n 
2 130 GLY n 
2 131 ASP n 
2 132 GLU n 
2 133 ILE n 
2 134 LEU n 
2 135 THR n 
2 136 MET n 
2 137 GLU n 
2 138 LEU n 
2 139 MET n 
2 140 ILE n 
2 141 MET n 
2 142 LYS n 
2 143 ALA n 
2 144 LEU n 
2 145 LYS n 
2 146 TRP n 
2 147 ARG n 
2 148 LEU n 
2 149 SER n 
2 150 PRO n 
2 151 LEU n 
2 152 THR n 
2 153 ILE n 
2 154 VAL n 
2 155 SER n 
2 156 TRP n 
2 157 LEU n 
2 158 ASN n 
2 159 VAL n 
2 160 TYR n 
2 161 MET n 
2 162 GLN n 
2 163 VAL n 
2 164 ALA n 
2 165 TYR n 
2 166 LEU n 
2 167 ASN n 
2 168 ASP n 
2 169 LEU n 
2 170 HIS n 
2 171 GLU n 
2 172 VAL n 
2 173 LEU n 
2 174 LEU n 
2 175 PRO n 
2 176 GLN n 
2 177 TYR n 
2 178 PRO n 
2 179 GLN n 
2 180 GLN n 
2 181 ILE n 
2 182 PHE n 
2 183 ILE n 
2 184 GLN n 
2 185 ILE n 
2 186 ALA n 
2 187 GLU n 
2 188 LEU n 
2 189 LEU n 
2 190 ASP n 
2 191 LEU n 
2 192 CYS n 
2 193 VAL n 
2 194 LEU n 
2 195 ASP n 
2 196 VAL n 
2 197 ASP n 
2 198 CYS n 
2 199 LEU n 
2 200 GLU n 
2 201 PHE n 
2 202 PRO n 
2 203 TYR n 
2 204 GLY n 
2 205 ILE n 
2 206 LEU n 
2 207 ALA n 
2 208 ALA n 
2 209 SER n 
2 210 ALA n 
2 211 LEU n 
2 212 TYR n 
2 213 HIS n 
2 214 PHE n 
2 215 SER n 
2 216 SER n 
2 217 SER n 
2 218 GLU n 
2 219 LEU n 
2 220 MET n 
2 221 GLN n 
2 222 LYS n 
2 223 VAL n 
2 224 SER n 
2 225 GLY n 
2 226 TYR n 
2 227 GLN n 
2 228 TRP n 
2 229 CYS n 
2 230 ASP n 
2 231 ILE n 
2 232 GLU n 
2 233 ASN n 
2 234 CYS n 
2 235 VAL n 
2 236 LYS n 
2 237 TRP n 
2 238 MET n 
2 239 VAL n 
2 240 PRO n 
2 241 PHE n 
2 242 ALA n 
2 243 MET n 
2 244 VAL n 
2 245 ILE n 
2 246 ARG n 
2 247 GLU n 
2 248 THR n 
2 249 GLY n 
2 250 SER n 
2 251 SER n 
2 252 LYS n 
2 253 LEU n 
2 254 LYS n 
2 255 HIS n 
2 256 PHE n 
2 257 ARG n 
2 258 GLY n 
2 259 VAL n 
2 260 ALA n 
2 261 ASP n 
2 262 GLU n 
2 263 ASP n 
2 264 ALA n 
2 265 HIS n 
2 266 ASN n 
2 267 ILE n 
2 268 GLN n 
2 269 THR n 
2 270 HIS n 
2 271 ARG n 
2 272 ASP n 
2 273 SER n 
2 274 LEU n 
2 275 ASP n 
2 276 LEU n 
2 277 LEU n 
2 278 ASP n 
2 279 LYS n 
2 280 ALA n 
2 281 ARG n 
2 282 ALA n 
2 283 LYS n 
2 284 LYS n 
2 285 ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 301 human ? 'CDK2, CDKN2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 285 human ? 'CCNE1, CCNE' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1CAI non-polymer         . '(1R,3R)-3-{3-[2-(4-methoxyphenyl)acetamido]-1H-pyrazol-5-yl}cyclopentyl propan-2-ylcarbamate' ? 
'C21 H28 N4 O4'  400.471 
ALA   'L-peptide linking' y ALANINE                                                                                        ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                       ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                     ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                       ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                      ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                        ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                      ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                          ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                     ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                        ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                         ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                     ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                  ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                        ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                         ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                      ? 
'C4 H9 N O3'     119.119 
TPO   'L-peptide linking' n PHOSPHOTHREONINE                                                                               
PHOSPHONOTHREONINE 'C4 H10 N O6 P'  199.099 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                     ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                       ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                         ? 
'C5 H11 N O2'    117.146 
# 
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   SER 1   -2  ?   ?   ?   A . n 
A 1 2   HIS 2   -1  ?   ?   ?   A . n 
A 1 3   MET 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   GLU 5   2   2   GLU GLU A . n 
A 1 6   ASN 6   3   3   ASN ASN A . n 
A 1 7   PHE 7   4   4   PHE PHE A . n 
A 1 8   GLN 8   5   5   GLN GLN A . n 
A 1 9   LYS 9   6   6   LYS LYS A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  GLU 11  8   8   GLU GLU A . n 
A 1 12  LYS 12  9   9   LYS LYS A . n 
A 1 13  ILE 13  10  10  ILE ILE A . n 
A 1 14  GLY 14  11  11  GLY GLY A . n 
A 1 15  GLU 15  12  12  GLU GLU A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  THR 17  14  14  THR THR A . n 
A 1 18  TYR 18  15  15  TYR TYR A . n 
A 1 19  GLY 19  16  16  GLY GLY A . n 
A 1 20  VAL 20  17  17  VAL VAL A . n 
A 1 21  VAL 21  18  18  VAL VAL A . n 
A 1 22  TYR 22  19  19  TYR TYR A . n 
A 1 23  LYS 23  20  20  LYS LYS A . n 
A 1 24  ALA 24  21  21  ALA ALA A . n 
A 1 25  ARG 25  22  22  ARG ARG A . n 
A 1 26  ASN 26  23  23  ASN ASN A . n 
A 1 27  LYS 27  24  24  LYS LYS A . n 
A 1 28  LEU 28  25  25  LEU LEU A . n 
A 1 29  THR 29  26  26  THR THR A . n 
A 1 30  GLY 30  27  27  GLY GLY A . n 
A 1 31  GLU 31  28  28  GLU GLU A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  VAL 33  30  30  VAL VAL A . n 
A 1 34  ALA 34  31  31  ALA ALA A . n 
A 1 35  LEU 35  32  32  LEU LEU A . n 
A 1 36  LYS 36  33  33  LYS LYS A . n 
A 1 37  LYS 37  34  34  LYS LYS A . n 
A 1 38  ILE 38  35  35  ILE ILE A . n 
A 1 39  ARG 39  36  36  ARG ARG A . n 
A 1 40  LEU 40  37  37  LEU LEU A . n 
A 1 41  ASP 41  38  38  ASP ASP A . n 
A 1 42  THR 42  39  39  THR THR A . n 
A 1 43  GLU 43  40  40  GLU GLU A . n 
A 1 44  THR 44  41  41  THR THR A . n 
A 1 45  GLU 45  42  42  GLU GLU A . n 
A 1 46  GLY 46  43  43  GLY GLY A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  PRO 48  45  45  PRO PRO A . n 
A 1 49  SER 49  46  46  SER SER A . n 
A 1 50  THR 50  47  47  THR THR A . n 
A 1 51  ALA 51  48  48  ALA ALA A . n 
A 1 52  ILE 52  49  49  ILE ILE A . n 
A 1 53  ARG 53  50  50  ARG ARG A . n 
A 1 54  GLU 54  51  51  GLU GLU A . n 
A 1 55  ILE 55  52  52  ILE ILE A . n 
A 1 56  SER 56  53  53  SER SER A . n 
A 1 57  LEU 57  54  54  LEU LEU A . n 
A 1 58  LEU 58  55  55  LEU LEU A . n 
A 1 59  LYS 59  56  56  LYS LYS A . n 
A 1 60  GLU 60  57  57  GLU GLU A . n 
A 1 61  LEU 61  58  58  LEU LEU A . n 
A 1 62  ASN 62  59  59  ASN ASN A . n 
A 1 63  HIS 63  60  60  HIS HIS A . n 
A 1 64  PRO 64  61  61  PRO PRO A . n 
A 1 65  ASN 65  62  62  ASN ASN A . n 
A 1 66  ILE 66  63  63  ILE ILE A . n 
A 1 67  VAL 67  64  64  VAL VAL A . n 
A 1 68  LYS 68  65  65  LYS LYS A . n 
A 1 69  LEU 69  66  66  LEU LEU A . n 
A 1 70  LEU 70  67  67  LEU LEU A . n 
A 1 71  ASP 71  68  68  ASP ASP A . n 
A 1 72  VAL 72  69  69  VAL VAL A . n 
A 1 73  ILE 73  70  70  ILE ILE A . n 
A 1 74  HIS 74  71  71  HIS HIS A . n 
A 1 75  THR 75  72  72  THR THR A . n 
A 1 76  GLU 76  73  73  GLU GLU A . n 
A 1 77  ASN 77  74  74  ASN ASN A . n 
A 1 78  LYS 78  75  75  LYS LYS A . n 
A 1 79  LEU 79  76  76  LEU LEU A . n 
A 1 80  TYR 80  77  77  TYR TYR A . n 
A 1 81  LEU 81  78  78  LEU LEU A . n 
A 1 82  VAL 82  79  79  VAL VAL A . n 
A 1 83  PHE 83  80  80  PHE PHE A . n 
A 1 84  GLU 84  81  81  GLU GLU A . n 
A 1 85  PHE 85  82  82  PHE PHE A . n 
A 1 86  LEU 86  83  83  LEU LEU A . n 
A 1 87  HIS 87  84  84  HIS HIS A . n 
A 1 88  GLN 88  85  85  GLN GLN A . n 
A 1 89  ASP 89  86  86  ASP ASP A . n 
A 1 90  LEU 90  87  87  LEU LEU A . n 
A 1 91  LYS 91  88  88  LYS LYS A . n 
A 1 92  LYS 92  89  89  LYS LYS A . n 
A 1 93  PHE 93  90  90  PHE PHE A . n 
A 1 94  MET 94  91  91  MET MET A . n 
A 1 95  ASP 95  92  92  ASP ASP A . n 
A 1 96  ALA 96  93  93  ALA ALA A . n 
A 1 97  SER 97  94  94  SER SER A . n 
A 1 98  ALA 98  95  95  ALA ALA A . n 
A 1 99  LEU 99  96  96  LEU LEU A . n 
A 1 100 THR 100 97  97  THR THR A . n 
A 1 101 GLY 101 98  98  GLY GLY A . n 
A 1 102 ILE 102 99  99  ILE ILE A . n 
A 1 103 PRO 103 100 100 PRO PRO A . n 
A 1 104 LEU 104 101 101 LEU LEU A . n 
A 1 105 PRO 105 102 102 PRO PRO A . n 
A 1 106 LEU 106 103 103 LEU LEU A . n 
A 1 107 ILE 107 104 104 ILE ILE A . n 
A 1 108 LYS 108 105 105 LYS LYS A . n 
A 1 109 SER 109 106 106 SER SER A . n 
A 1 110 TYR 110 107 107 TYR TYR A . n 
A 1 111 LEU 111 108 108 LEU LEU A . n 
A 1 112 PHE 112 109 109 PHE PHE A . n 
A 1 113 GLN 113 110 110 GLN GLN A . n 
A 1 114 LEU 114 111 111 LEU LEU A . n 
A 1 115 LEU 115 112 112 LEU LEU A . n 
A 1 116 GLN 116 113 113 GLN GLN A . n 
A 1 117 GLY 117 114 114 GLY GLY A . n 
A 1 118 LEU 118 115 115 LEU LEU A . n 
A 1 119 ALA 119 116 116 ALA ALA A . n 
A 1 120 PHE 120 117 117 PHE PHE A . n 
A 1 121 CYS 121 118 118 CYS CYS A . n 
A 1 122 HIS 122 119 119 HIS HIS A . n 
A 1 123 SER 123 120 120 SER SER A . n 
A 1 124 HIS 124 121 121 HIS HIS A . n 
A 1 125 ARG 125 122 122 ARG ARG A . n 
A 1 126 VAL 126 123 123 VAL VAL A . n 
A 1 127 LEU 127 124 124 LEU LEU A . n 
A 1 128 HIS 128 125 125 HIS HIS A . n 
A 1 129 ARG 129 126 126 ARG ARG A . n 
A 1 130 ASP 130 127 127 ASP ASP A . n 
A 1 131 LEU 131 128 128 LEU LEU A . n 
A 1 132 LYS 132 129 129 LYS LYS A . n 
A 1 133 PRO 133 130 130 PRO PRO A . n 
A 1 134 GLN 134 131 131 GLN GLN A . n 
A 1 135 ASN 135 132 132 ASN ASN A . n 
A 1 136 LEU 136 133 133 LEU LEU A . n 
A 1 137 LEU 137 134 134 LEU LEU A . n 
A 1 138 ILE 138 135 135 ILE ILE A . n 
A 1 139 ASN 139 136 136 ASN ASN A . n 
A 1 140 THR 140 137 137 THR THR A . n 
A 1 141 GLU 141 138 138 GLU GLU A . n 
A 1 142 GLY 142 139 139 GLY GLY A . n 
A 1 143 ALA 143 140 140 ALA ALA A . n 
A 1 144 ILE 144 141 141 ILE ILE A . n 
A 1 145 LYS 145 142 142 LYS LYS A . n 
A 1 146 LEU 146 143 143 LEU LEU A . n 
A 1 147 ALA 147 144 144 ALA ALA A . n 
A 1 148 ASP 148 145 145 ASP ASP A . n 
A 1 149 PHE 149 146 146 PHE PHE A . n 
A 1 150 GLY 150 147 147 GLY GLY A . n 
A 1 151 LEU 151 148 148 LEU LEU A . n 
A 1 152 ALA 152 149 149 ALA ALA A . n 
A 1 153 ARG 153 150 150 ARG ARG A . n 
A 1 154 ALA 154 151 151 ALA ALA A . n 
A 1 155 PHE 155 152 152 PHE PHE A . n 
A 1 156 GLY 156 153 153 GLY GLY A . n 
A 1 157 VAL 157 154 154 VAL VAL A . n 
A 1 158 PRO 158 155 155 PRO PRO A . n 
A 1 159 VAL 159 156 156 VAL VAL A . n 
A 1 160 ARG 160 157 157 ARG ARG A . n 
A 1 161 THR 161 158 158 THR THR A . n 
A 1 162 TYR 162 159 159 TYR TYR A . n 
A 1 163 TPO 163 160 160 TPO TPO A . n 
A 1 164 HIS 164 161 161 HIS HIS A . n 
A 1 165 GLU 165 162 162 GLU GLU A . n 
A 1 166 VAL 166 163 163 VAL VAL A . n 
A 1 167 VAL 167 164 164 VAL VAL A . n 
A 1 168 THR 168 165 165 THR THR A . n 
A 1 169 LEU 169 166 166 LEU LEU A . n 
A 1 170 TRP 170 167 167 TRP TRP A . n 
A 1 171 TYR 171 168 168 TYR TYR A . n 
A 1 172 ARG 172 169 169 ARG ARG A . n 
A 1 173 ALA 173 170 170 ALA ALA A . n 
A 1 174 PRO 174 171 171 PRO PRO A . n 
A 1 175 GLU 175 172 172 GLU GLU A . n 
A 1 176 ILE 176 173 173 ILE ILE A . n 
A 1 177 LEU 177 174 174 LEU LEU A . n 
A 1 178 LEU 178 175 175 LEU LEU A . n 
A 1 179 GLY 179 176 176 GLY GLY A . n 
A 1 180 CYS 180 177 177 CYS CYS A . n 
A 1 181 LYS 181 178 178 LYS LYS A . n 
A 1 182 TYR 182 179 179 TYR TYR A . n 
A 1 183 TYR 183 180 180 TYR TYR A . n 
A 1 184 SER 184 181 181 SER SER A . n 
A 1 185 THR 185 182 182 THR THR A . n 
A 1 186 ALA 186 183 183 ALA ALA A . n 
A 1 187 VAL 187 184 184 VAL VAL A . n 
A 1 188 ASP 188 185 185 ASP ASP A . n 
A 1 189 ILE 189 186 186 ILE ILE A . n 
A 1 190 TRP 190 187 187 TRP TRP A . n 
A 1 191 SER 191 188 188 SER SER A . n 
A 1 192 LEU 192 189 189 LEU LEU A . n 
A 1 193 GLY 193 190 190 GLY GLY A . n 
A 1 194 CYS 194 191 191 CYS CYS A . n 
A 1 195 ILE 195 192 192 ILE ILE A . n 
A 1 196 PHE 196 193 193 PHE PHE A . n 
A 1 197 ALA 197 194 194 ALA ALA A . n 
A 1 198 GLU 198 195 195 GLU GLU A . n 
A 1 199 MET 199 196 196 MET MET A . n 
A 1 200 VAL 200 197 197 VAL VAL A . n 
A 1 201 THR 201 198 198 THR THR A . n 
A 1 202 ARG 202 199 199 ARG ARG A . n 
A 1 203 ARG 203 200 200 ARG ARG A . n 
A 1 204 ALA 204 201 201 ALA ALA A . n 
A 1 205 LEU 205 202 202 LEU LEU A . n 
A 1 206 PHE 206 203 203 PHE PHE A . n 
A 1 207 PRO 207 204 204 PRO PRO A . n 
A 1 208 GLY 208 205 205 GLY GLY A . n 
A 1 209 ASP 209 206 206 ASP ASP A . n 
A 1 210 SER 210 207 207 SER SER A . n 
A 1 211 GLU 211 208 208 GLU GLU A . n 
A 1 212 ILE 212 209 209 ILE ILE A . n 
A 1 213 ASP 213 210 210 ASP ASP A . n 
A 1 214 GLN 214 211 211 GLN GLN A . n 
A 1 215 LEU 215 212 212 LEU LEU A . n 
A 1 216 PHE 216 213 213 PHE PHE A . n 
A 1 217 ARG 217 214 214 ARG ARG A . n 
A 1 218 ILE 218 215 215 ILE ILE A . n 
A 1 219 PHE 219 216 216 PHE PHE A . n 
A 1 220 ARG 220 217 217 ARG ARG A . n 
A 1 221 THR 221 218 218 THR THR A . n 
A 1 222 LEU 222 219 219 LEU LEU A . n 
A 1 223 GLY 223 220 220 GLY GLY A . n 
A 1 224 THR 224 221 221 THR THR A . n 
A 1 225 PRO 225 222 222 PRO PRO A . n 
A 1 226 ASP 226 223 223 ASP ASP A . n 
A 1 227 GLU 227 224 224 GLU GLU A . n 
A 1 228 VAL 228 225 225 VAL VAL A . n 
A 1 229 VAL 229 226 226 VAL VAL A . n 
A 1 230 TRP 230 227 227 TRP TRP A . n 
A 1 231 PRO 231 228 228 PRO PRO A . n 
A 1 232 GLY 232 229 229 GLY GLY A . n 
A 1 233 VAL 233 230 230 VAL VAL A . n 
A 1 234 THR 234 231 231 THR THR A . n 
A 1 235 SER 235 232 232 SER SER A . n 
A 1 236 MET 236 233 233 MET MET A . n 
A 1 237 PRO 237 234 234 PRO PRO A . n 
A 1 238 ASP 238 235 235 ASP ASP A . n 
A 1 239 TYR 239 236 236 TYR TYR A . n 
A 1 240 LYS 240 237 237 LYS LYS A . n 
A 1 241 PRO 241 238 238 PRO PRO A . n 
A 1 242 SER 242 239 239 SER SER A . n 
A 1 243 PHE 243 240 240 PHE PHE A . n 
A 1 244 PRO 244 241 241 PRO PRO A . n 
A 1 245 LYS 245 242 242 LYS LYS A . n 
A 1 246 TRP 246 243 243 TRP TRP A . n 
A 1 247 ALA 247 244 244 ALA ALA A . n 
A 1 248 ARG 248 245 245 ARG ARG A . n 
A 1 249 GLN 249 246 246 GLN GLN A . n 
A 1 250 ASP 250 247 247 ASP ASP A . n 
A 1 251 PHE 251 248 248 PHE PHE A . n 
A 1 252 SER 252 249 249 SER SER A . n 
A 1 253 LYS 253 250 250 LYS LYS A . n 
A 1 254 VAL 254 251 251 VAL VAL A . n 
A 1 255 VAL 255 252 252 VAL VAL A . n 
A 1 256 PRO 256 253 253 PRO PRO A . n 
A 1 257 PRO 257 254 254 PRO PRO A . n 
A 1 258 LEU 258 255 255 LEU LEU A . n 
A 1 259 ASP 259 256 256 ASP ASP A . n 
A 1 260 GLU 260 257 257 GLU GLU A . n 
A 1 261 ASP 261 258 258 ASP ASP A . n 
A 1 262 GLY 262 259 259 GLY GLY A . n 
A 1 263 ARG 263 260 260 ARG ARG A . n 
A 1 264 SER 264 261 261 SER SER A . n 
A 1 265 LEU 265 262 262 LEU LEU A . n 
A 1 266 LEU 266 263 263 LEU LEU A . n 
A 1 267 SER 267 264 264 SER SER A . n 
A 1 268 GLN 268 265 265 GLN GLN A . n 
A 1 269 MET 269 266 266 MET MET A . n 
A 1 270 LEU 270 267 267 LEU LEU A . n 
A 1 271 HIS 271 268 268 HIS HIS A . n 
A 1 272 TYR 272 269 269 TYR TYR A . n 
A 1 273 ASP 273 270 270 ASP ASP A . n 
A 1 274 PRO 274 271 271 PRO PRO A . n 
A 1 275 ASN 275 272 272 ASN ASN A . n 
A 1 276 LYS 276 273 273 LYS LYS A . n 
A 1 277 ARG 277 274 274 ARG ARG A . n 
A 1 278 ILE 278 275 275 ILE ILE A . n 
A 1 279 SER 279 276 276 SER SER A . n 
A 1 280 ALA 280 277 277 ALA ALA A . n 
A 1 281 LYS 281 278 278 LYS LYS A . n 
A 1 282 ALA 282 279 279 ALA ALA A . n 
A 1 283 ALA 283 280 280 ALA ALA A . n 
A 1 284 LEU 284 281 281 LEU LEU A . n 
A 1 285 ALA 285 282 282 ALA ALA A . n 
A 1 286 HIS 286 283 283 HIS HIS A . n 
A 1 287 PRO 287 284 284 PRO PRO A . n 
A 1 288 PHE 288 285 285 PHE PHE A . n 
A 1 289 PHE 289 286 286 PHE PHE A . n 
A 1 290 GLN 290 287 287 GLN GLN A . n 
A 1 291 ASP 291 288 288 ASP ASP A . n 
A 1 292 VAL 292 289 289 VAL VAL A . n 
A 1 293 THR 293 290 290 THR THR A . n 
A 1 294 LYS 294 291 291 LYS LYS A . n 
A 1 295 PRO 295 292 292 PRO PRO A . n 
A 1 296 VAL 296 293 293 VAL VAL A . n 
A 1 297 PRO 297 294 294 PRO PRO A . n 
A 1 298 HIS 298 295 295 HIS HIS A . n 
A 1 299 LEU 299 296 296 LEU LEU A . n 
A 1 300 ARG 300 297 297 ARG ARG A . n 
A 1 301 LEU 301 298 298 LEU LEU A . n 
B 2 1   GLY 1   94  ?   ?   ?   B . n 
B 2 2   SER 2   95  ?   ?   ?   B . n 
B 2 3   ILE 3   96  ?   ?   ?   B . n 
B 2 4   ILE 4   97  ?   ?   ?   B . n 
B 2 5   ALA 5   98  ?   ?   ?   B . n 
B 2 6   PRO 6   99  ?   ?   ?   B . n 
B 2 7   SER 7   100 ?   ?   ?   B . n 
B 2 8   ARG 8   101 ?   ?   ?   B . n 
B 2 9   GLY 9   102 102 GLY GLY B . n 
B 2 10  SER 10  103 103 SER SER B . n 
B 2 11  PRO 11  104 104 PRO PRO B . n 
B 2 12  LEU 12  105 105 LEU LEU B . n 
B 2 13  PRO 13  106 106 PRO PRO B . n 
B 2 14  VAL 14  107 107 VAL VAL B . n 
B 2 15  LEU 15  108 108 LEU LEU B . n 
B 2 16  SER 16  109 109 SER SER B . n 
B 2 17  TRP 17  110 110 TRP TRP B . n 
B 2 18  ALA 18  111 111 ALA ALA B . n 
B 2 19  ASN 19  112 112 ASN ASN B . n 
B 2 20  ARG 20  113 113 ARG ARG B . n 
B 2 21  GLU 21  114 114 GLU GLU B . n 
B 2 22  GLU 22  115 115 GLU GLU B . n 
B 2 23  VAL 23  116 116 VAL VAL B . n 
B 2 24  TRP 24  117 117 TRP TRP B . n 
B 2 25  LYS 25  118 118 LYS LYS B . n 
B 2 26  ILE 26  119 119 ILE ILE B . n 
B 2 27  MET 27  120 120 MET MET B . n 
B 2 28  LEU 28  121 121 LEU LEU B . n 
B 2 29  ASN 29  122 122 ASN ASN B . n 
B 2 30  LYS 30  123 123 LYS LYS B . n 
B 2 31  GLU 31  124 124 GLU GLU B . n 
B 2 32  LYS 32  125 125 LYS LYS B . n 
B 2 33  THR 33  126 126 THR THR B . n 
B 2 34  TYR 34  127 127 TYR TYR B . n 
B 2 35  LEU 35  128 128 LEU LEU B . n 
B 2 36  ARG 36  129 129 ARG ARG B . n 
B 2 37  ASP 37  130 130 ASP ASP B . n 
B 2 38  GLN 38  131 131 GLN GLN B . n 
B 2 39  HIS 39  132 132 HIS HIS B . n 
B 2 40  PHE 40  133 133 PHE PHE B . n 
B 2 41  LEU 41  134 134 LEU LEU B . n 
B 2 42  GLU 42  135 135 GLU GLU B . n 
B 2 43  GLN 43  136 136 GLN GLN B . n 
B 2 44  HIS 44  137 137 HIS HIS B . n 
B 2 45  PRO 45  138 138 PRO PRO B . n 
B 2 46  LEU 46  139 139 LEU LEU B . n 
B 2 47  LEU 47  140 140 LEU LEU B . n 
B 2 48  GLN 48  141 141 GLN GLN B . n 
B 2 49  PRO 49  142 142 PRO PRO B . n 
B 2 50  LYS 50  143 143 LYS LYS B . n 
B 2 51  MET 51  144 144 MET MET B . n 
B 2 52  ARG 52  145 145 ARG ARG B . n 
B 2 53  ALA 53  146 146 ALA ALA B . n 
B 2 54  ILE 54  147 147 ILE ILE B . n 
B 2 55  LEU 55  148 148 LEU LEU B . n 
B 2 56  LEU 56  149 149 LEU LEU B . n 
B 2 57  ASP 57  150 150 ASP ASP B . n 
B 2 58  TRP 58  151 151 TRP TRP B . n 
B 2 59  LEU 59  152 152 LEU LEU B . n 
B 2 60  MET 60  153 153 MET MET B . n 
B 2 61  GLU 61  154 154 GLU GLU B . n 
B 2 62  VAL 62  155 155 VAL VAL B . n 
B 2 63  CYS 63  156 156 CYS CYS B . n 
B 2 64  GLU 64  157 157 GLU GLU B . n 
B 2 65  VAL 65  158 158 VAL VAL B . n 
B 2 66  TYR 66  159 159 TYR TYR B . n 
B 2 67  LYS 67  160 160 LYS LYS B . n 
B 2 68  LEU 68  161 161 LEU LEU B . n 
B 2 69  HIS 69  162 162 HIS HIS B . n 
B 2 70  ARG 70  163 163 ARG ARG B . n 
B 2 71  GLU 71  164 164 GLU GLU B . n 
B 2 72  THR 72  165 165 THR THR B . n 
B 2 73  PHE 73  166 166 PHE PHE B . n 
B 2 74  TYR 74  167 167 TYR TYR B . n 
B 2 75  LEU 75  168 168 LEU LEU B . n 
B 2 76  ALA 76  169 169 ALA ALA B . n 
B 2 77  GLN 77  170 170 GLN GLN B . n 
B 2 78  ASP 78  171 171 ASP ASP B . n 
B 2 79  PHE 79  172 172 PHE PHE B . n 
B 2 80  PHE 80  173 173 PHE PHE B . n 
B 2 81  ASP 81  174 174 ASP ASP B . n 
B 2 82  ARG 82  175 175 ARG ARG B . n 
B 2 83  TYR 83  176 176 TYR TYR B . n 
B 2 84  MET 84  177 177 MET MET B . n 
B 2 85  ALA 85  178 178 ALA ALA B . n 
B 2 86  THR 86  179 179 THR THR B . n 
B 2 87  GLN 87  180 180 GLN GLN B . n 
B 2 88  GLU 88  181 181 GLU GLU B . n 
B 2 89  ASN 89  182 182 ASN ASN B . n 
B 2 90  VAL 90  183 183 VAL VAL B . n 
B 2 91  VAL 91  184 184 VAL VAL B . n 
B 2 92  LYS 92  185 185 LYS LYS B . n 
B 2 93  THR 93  186 186 THR THR B . n 
B 2 94  LEU 94  187 187 LEU LEU B . n 
B 2 95  LEU 95  188 188 LEU LEU B . n 
B 2 96  GLN 96  189 189 GLN GLN B . n 
B 2 97  LEU 97  190 190 LEU LEU B . n 
B 2 98  ILE 98  191 191 ILE ILE B . n 
B 2 99  GLY 99  192 192 GLY GLY B . n 
B 2 100 ILE 100 193 193 ILE ILE B . n 
B 2 101 SER 101 194 194 SER SER B . n 
B 2 102 SER 102 195 195 SER SER B . n 
B 2 103 LEU 103 196 196 LEU LEU B . n 
B 2 104 PHE 104 197 197 PHE PHE B . n 
B 2 105 ILE 105 198 198 ILE ILE B . n 
B 2 106 ALA 106 199 199 ALA ALA B . n 
B 2 107 ALA 107 200 200 ALA ALA B . n 
B 2 108 LYS 108 201 201 LYS LYS B . n 
B 2 109 LEU 109 202 202 LEU LEU B . n 
B 2 110 GLU 110 203 203 GLU GLU B . n 
B 2 111 GLU 111 204 204 GLU GLU B . n 
B 2 112 ILE 112 205 205 ILE ILE B . n 
B 2 113 TYR 113 206 206 TYR TYR B . n 
B 2 114 PRO 114 207 207 PRO PRO B . n 
B 2 115 PRO 115 208 208 PRO PRO B . n 
B 2 116 LYS 116 209 209 LYS LYS B . n 
B 2 117 LEU 117 210 210 LEU LEU B . n 
B 2 118 HIS 118 211 211 HIS HIS B . n 
B 2 119 GLN 119 212 212 GLN GLN B . n 
B 2 120 PHE 120 213 213 PHE PHE B . n 
B 2 121 ALA 121 214 214 ALA ALA B . n 
B 2 122 TYR 122 215 215 TYR TYR B . n 
B 2 123 VAL 123 216 216 VAL VAL B . n 
B 2 124 THR 124 217 217 THR THR B . n 
B 2 125 ASP 125 218 218 ASP ASP B . n 
B 2 126 GLY 126 219 219 GLY GLY B . n 
B 2 127 ALA 127 220 220 ALA ALA B . n 
B 2 128 CYS 128 221 221 CYS CYS B . n 
B 2 129 SER 129 222 222 SER SER B . n 
B 2 130 GLY 130 223 223 GLY GLY B . n 
B 2 131 ASP 131 224 224 ASP ASP B . n 
B 2 132 GLU 132 225 225 GLU GLU B . n 
B 2 133 ILE 133 226 226 ILE ILE B . n 
B 2 134 LEU 134 227 227 LEU LEU B . n 
B 2 135 THR 135 228 228 THR THR B . n 
B 2 136 MET 136 229 229 MET MET B . n 
B 2 137 GLU 137 230 230 GLU GLU B . n 
B 2 138 LEU 138 231 231 LEU LEU B . n 
B 2 139 MET 139 232 232 MET MET B . n 
B 2 140 ILE 140 233 233 ILE ILE B . n 
B 2 141 MET 141 234 234 MET MET B . n 
B 2 142 LYS 142 235 235 LYS LYS B . n 
B 2 143 ALA 143 236 236 ALA ALA B . n 
B 2 144 LEU 144 237 237 LEU LEU B . n 
B 2 145 LYS 145 238 238 LYS LYS B . n 
B 2 146 TRP 146 239 239 TRP TRP B . n 
B 2 147 ARG 147 240 240 ARG ARG B . n 
B 2 148 LEU 148 241 241 LEU LEU B . n 
B 2 149 SER 149 242 242 SER SER B . n 
B 2 150 PRO 150 243 243 PRO PRO B . n 
B 2 151 LEU 151 244 244 LEU LEU B . n 
B 2 152 THR 152 245 245 THR THR B . n 
B 2 153 ILE 153 246 246 ILE ILE B . n 
B 2 154 VAL 154 247 247 VAL VAL B . n 
B 2 155 SER 155 248 248 SER SER B . n 
B 2 156 TRP 156 249 249 TRP TRP B . n 
B 2 157 LEU 157 250 250 LEU LEU B . n 
B 2 158 ASN 158 251 251 ASN ASN B . n 
B 2 159 VAL 159 252 252 VAL VAL B . n 
B 2 160 TYR 160 253 253 TYR TYR B . n 
B 2 161 MET 161 254 254 MET MET B . n 
B 2 162 GLN 162 255 255 GLN GLN B . n 
B 2 163 VAL 163 256 256 VAL VAL B . n 
B 2 164 ALA 164 257 257 ALA ALA B . n 
B 2 165 TYR 165 258 258 TYR TYR B . n 
B 2 166 LEU 166 259 259 LEU LEU B . n 
B 2 167 ASN 167 260 260 ASN ASN B . n 
B 2 168 ASP 168 261 261 ASP ASP B . n 
B 2 169 LEU 169 262 262 LEU LEU B . n 
B 2 170 HIS 170 263 263 HIS HIS B . n 
B 2 171 GLU 171 264 264 GLU GLU B . n 
B 2 172 VAL 172 265 265 VAL VAL B . n 
B 2 173 LEU 173 266 266 LEU LEU B . n 
B 2 174 LEU 174 267 267 LEU LEU B . n 
B 2 175 PRO 175 268 268 PRO PRO B . n 
B 2 176 GLN 176 269 269 GLN GLN B . n 
B 2 177 TYR 177 270 270 TYR TYR B . n 
B 2 178 PRO 178 271 271 PRO PRO B . n 
B 2 179 GLN 179 272 272 GLN GLN B . n 
B 2 180 GLN 180 273 273 GLN GLN B . n 
B 2 181 ILE 181 274 274 ILE ILE B . n 
B 2 182 PHE 182 275 275 PHE PHE B . n 
B 2 183 ILE 183 276 276 ILE ILE B . n 
B 2 184 GLN 184 277 277 GLN GLN B . n 
B 2 185 ILE 185 278 278 ILE ILE B . n 
B 2 186 ALA 186 279 279 ALA ALA B . n 
B 2 187 GLU 187 280 280 GLU GLU B . n 
B 2 188 LEU 188 281 281 LEU LEU B . n 
B 2 189 LEU 189 282 282 LEU LEU B . n 
B 2 190 ASP 190 283 283 ASP ASP B . n 
B 2 191 LEU 191 284 284 LEU LEU B . n 
B 2 192 CYS 192 285 285 CYS CYS B . n 
B 2 193 VAL 193 286 286 VAL VAL B . n 
B 2 194 LEU 194 287 287 LEU LEU B . n 
B 2 195 ASP 195 288 288 ASP ASP B . n 
B 2 196 VAL 196 289 289 VAL VAL B . n 
B 2 197 ASP 197 290 290 ASP ASP B . n 
B 2 198 CYS 198 291 291 CYS CYS B . n 
B 2 199 LEU 199 292 292 LEU LEU B . n 
B 2 200 GLU 200 293 293 GLU GLU B . n 
B 2 201 PHE 201 294 294 PHE PHE B . n 
B 2 202 PRO 202 295 295 PRO PRO B . n 
B 2 203 TYR 203 296 296 TYR TYR B . n 
B 2 204 GLY 204 297 297 GLY GLY B . n 
B 2 205 ILE 205 298 298 ILE ILE B . n 
B 2 206 LEU 206 299 299 LEU LEU B . n 
B 2 207 ALA 207 300 300 ALA ALA B . n 
B 2 208 ALA 208 301 301 ALA ALA B . n 
B 2 209 SER 209 302 302 SER SER B . n 
B 2 210 ALA 210 303 303 ALA ALA B . n 
B 2 211 LEU 211 304 304 LEU LEU B . n 
B 2 212 TYR 212 305 305 TYR TYR B . n 
B 2 213 HIS 213 306 306 HIS HIS B . n 
B 2 214 PHE 214 307 307 PHE PHE B . n 
B 2 215 SER 215 308 308 SER SER B . n 
B 2 216 SER 216 309 309 SER SER B . n 
B 2 217 SER 217 310 310 SER SER B . n 
B 2 218 GLU 218 311 311 GLU GLU B . n 
B 2 219 LEU 219 312 312 LEU LEU B . n 
B 2 220 MET 220 313 313 MET MET B . n 
B 2 221 GLN 221 314 314 GLN GLN B . n 
B 2 222 LYS 222 315 315 LYS LYS B . n 
B 2 223 VAL 223 316 316 VAL VAL B . n 
B 2 224 SER 224 317 317 SER SER B . n 
B 2 225 GLY 225 318 318 GLY GLY B . n 
B 2 226 TYR 226 319 319 TYR TYR B . n 
B 2 227 GLN 227 320 320 GLN GLN B . n 
B 2 228 TRP 228 321 321 TRP TRP B . n 
B 2 229 CYS 229 322 322 CYS CYS B . n 
B 2 230 ASP 230 323 323 ASP ASP B . n 
B 2 231 ILE 231 324 324 ILE ILE B . n 
B 2 232 GLU 232 325 325 GLU GLU B . n 
B 2 233 ASN 233 326 326 ASN ASN B . n 
B 2 234 CYS 234 327 327 CYS CYS B . n 
B 2 235 VAL 235 328 328 VAL VAL B . n 
B 2 236 LYS 236 329 329 LYS LYS B . n 
B 2 237 TRP 237 330 330 TRP TRP B . n 
B 2 238 MET 238 331 331 MET MET B . n 
B 2 239 VAL 239 332 332 VAL VAL B . n 
B 2 240 PRO 240 333 333 PRO PRO B . n 
B 2 241 PHE 241 334 334 PHE PHE B . n 
B 2 242 ALA 242 335 335 ALA ALA B . n 
B 2 243 MET 243 336 336 MET MET B . n 
B 2 244 VAL 244 337 337 VAL VAL B . n 
B 2 245 ILE 245 338 338 ILE ILE B . n 
B 2 246 ARG 246 339 339 ARG ARG B . n 
B 2 247 GLU 247 340 340 GLU GLU B . n 
B 2 248 THR 248 341 341 THR THR B . n 
B 2 249 GLY 249 342 342 GLY GLY B . n 
B 2 250 SER 250 343 343 SER SER B . n 
B 2 251 SER 251 344 344 SER SER B . n 
B 2 252 LYS 252 345 345 LYS LYS B . n 
B 2 253 LEU 253 346 346 LEU LEU B . n 
B 2 254 LYS 254 347 347 LYS LYS B . n 
B 2 255 HIS 255 348 348 HIS HIS B . n 
B 2 256 PHE 256 349 349 PHE PHE B . n 
B 2 257 ARG 257 350 350 ARG ARG B . n 
B 2 258 GLY 258 351 351 GLY GLY B . n 
B 2 259 VAL 259 352 352 VAL VAL B . n 
B 2 260 ALA 260 353 353 ALA ALA B . n 
B 2 261 ASP 261 354 354 ASP ASP B . n 
B 2 262 GLU 262 355 355 GLU GLU B . n 
B 2 263 ASP 263 356 356 ASP ASP B . n 
B 2 264 ALA 264 357 357 ALA ALA B . n 
B 2 265 HIS 265 358 358 HIS HIS B . n 
B 2 266 ASN 266 359 359 ASN ASN B . n 
B 2 267 ILE 267 360 360 ILE ILE B . n 
B 2 268 GLN 268 361 361 GLN GLN B . n 
B 2 269 THR 269 362 362 THR THR B . n 
B 2 270 HIS 270 363 363 HIS HIS B . n 
B 2 271 ARG 271 364 364 ARG ARG B . n 
B 2 272 ASP 272 365 365 ASP ASP B . n 
B 2 273 SER 273 366 366 SER SER B . n 
B 2 274 LEU 274 367 367 LEU LEU B . n 
B 2 275 ASP 275 368 368 ASP ASP B . n 
B 2 276 LEU 276 369 369 LEU LEU B . n 
B 2 277 LEU 277 370 370 LEU LEU B . n 
B 2 278 ASP 278 371 371 ASP ASP B . n 
B 2 279 LYS 279 372 372 LYS LYS B . n 
B 2 280 ALA 280 373 373 ALA ALA B . n 
B 2 281 ARG 281 374 374 ARG ARG B . n 
B 2 282 ALA 282 375 375 ALA ALA B . n 
B 2 283 LYS 283 376 ?   ?   ?   B . n 
B 2 284 LYS 284 377 ?   ?   ?   B . n 
B 2 285 ALA 285 378 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1CAI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1CAI 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1CAI 1  301 1  A1CAI LI1 A . 
D 4 HOH   1  401 44 HOH   HOH A . 
D 4 HOH   2  402 42 HOH   HOH A . 
D 4 HOH   3  403 39 HOH   HOH A . 
D 4 HOH   4  404 57 HOH   HOH A . 
D 4 HOH   5  405 2  HOH   HOH A . 
D 4 HOH   6  406 32 HOH   HOH A . 
D 4 HOH   7  407 48 HOH   HOH A . 
D 4 HOH   8  408 12 HOH   HOH A . 
D 4 HOH   9  409 38 HOH   HOH A . 
D 4 HOH   10 410 55 HOH   HOH A . 
D 4 HOH   11 411 18 HOH   HOH A . 
D 4 HOH   12 412 10 HOH   HOH A . 
D 4 HOH   13 413 30 HOH   HOH A . 
D 4 HOH   14 414 9  HOH   HOH A . 
D 4 HOH   15 415 26 HOH   HOH A . 
D 4 HOH   16 416 19 HOH   HOH A . 
D 4 HOH   17 417 40 HOH   HOH A . 
D 4 HOH   18 418 28 HOH   HOH A . 
D 4 HOH   19 419 33 HOH   HOH A . 
D 4 HOH   20 420 52 HOH   HOH A . 
D 4 HOH   21 421 14 HOH   HOH A . 
D 4 HOH   22 422 25 HOH   HOH A . 
D 4 HOH   23 423 1  HOH   HOH A . 
D 4 HOH   24 424 13 HOH   HOH A . 
D 4 HOH   25 425 56 HOH   HOH A . 
D 4 HOH   26 426 31 HOH   HOH A . 
D 4 HOH   27 427 15 HOH   HOH A . 
D 4 HOH   28 428 5  HOH   HOH A . 
D 4 HOH   29 429 7  HOH   HOH A . 
D 4 HOH   30 430 54 HOH   HOH A . 
D 4 HOH   31 431 49 HOH   HOH A . 
D 4 HOH   32 432 43 HOH   HOH A . 
D 4 HOH   33 433 8  HOH   HOH A . 
D 4 HOH   34 434 16 HOH   HOH A . 
D 4 HOH   35 435 50 HOH   HOH A . 
D 4 HOH   36 436 21 HOH   HOH A . 
D 4 HOH   37 437 58 HOH   HOH A . 
D 4 HOH   38 438 20 HOH   HOH A . 
D 4 HOH   39 439 4  HOH   HOH A . 
D 4 HOH   40 440 36 HOH   HOH A . 
D 4 HOH   41 441 27 HOH   HOH A . 
D 4 HOH   42 442 3  HOH   HOH A . 
D 4 HOH   43 443 37 HOH   HOH A . 
D 4 HOH   44 444 35 HOH   HOH A . 
D 4 HOH   45 445 22 HOH   HOH A . 
D 4 HOH   46 446 41 HOH   HOH A . 
E 4 HOH   1  401 23 HOH   HOH B . 
E 4 HOH   2  402 6  HOH   HOH B . 
E 4 HOH   3  403 47 HOH   HOH B . 
E 4 HOH   4  404 45 HOH   HOH B . 
E 4 HOH   5  405 34 HOH   HOH B . 
E 4 HOH   6  406 24 HOH   HOH B . 
E 4 HOH   7  407 17 HOH   HOH B . 
E 4 HOH   8  408 51 HOH   HOH B . 
E 4 HOH   9  409 29 HOH   HOH B . 
E 4 HOH   10 410 11 HOH   HOH B . 
E 4 HOH   11 411 53 HOH   HOH B . 
E 4 HOH   12 412 46 HOH   HOH B . 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.2_5419 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           ? 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                     9OB6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.100 
_cell.length_a_esd                 ? 
_cell.length_b                     101.100 
_cell.length_b_esd                 ? 
_cell.length_c                     151.030 
_cell.length_c_esd                 ? 
_cell.volume                       1543709.346 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9OB6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            'P 4abw 2nw' 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9OB6 
_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             2.86 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.00 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.115 M Sodium Citrate, 15% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-08-27 
_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   1.11582 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.11582 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          52.26 
_reflns.entry_id                                       9OB6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2 
_reflns.d_resolution_low                               151.03 
_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                                     53625 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.082 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.079 
_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 
_reflns_shell.d_res_low                                     2.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3890 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_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                                  0.369 
_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                               75.57 
_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                                 9OB6 
_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                            2.00 
_refine.ls_d_res_low                             84.01 
_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                     53530 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  51530 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 3.74 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2277 
_refine.ls_R_factor_R_free                       0.2564 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2266 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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                 30.5052 
_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                            0.3373 
_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                       2.00 
_refine_hist.d_res_low                        84.01 
_refine_hist.number_atoms_solvent             58 
_refine_hist.number_atoms_total               4731 
_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        4644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0014  ? 4842 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.4010  ? 6575 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 0.0368  ? 734  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.0032  ? 826  ? f_plane_restr      ? ? ? 
'X-RAY DIFFRACTION' ? 11.1247 ? 1786 ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.05  . . 139 3605 100.00 . . . . 0.3551 . . . . . . . . . . . . . . . 0.3826 
'X-RAY DIFFRACTION' 2.05 2.11  . . 142 3640 99.97  . . . . 0.3406 . . . . . . . . . . . . . . . 0.4093 
'X-RAY DIFFRACTION' 2.11 2.17  . . 140 3612 99.95  . . . . 0.3268 . . . . . . . . . . . . . . . 0.3867 
'X-RAY DIFFRACTION' 2.17 2.24  . . 141 3628 99.97  . . . . 0.3117 . . . . . . . . . . . . . . . 0.3327 
'X-RAY DIFFRACTION' 2.24 2.32  . . 140 3615 100.00 . . . . 0.3231 . . . . . . . . . . . . . . . 0.3723 
'X-RAY DIFFRACTION' 2.32 2.41  . . 142 3647 99.97  . . . . 0.2972 . . . . . . . . . . . . . . . 0.3175 
'X-RAY DIFFRACTION' 2.41 2.52  . . 142 3651 99.97  . . . . 0.2744 . . . . . . . . . . . . . . . 0.3267 
'X-RAY DIFFRACTION' 2.52 2.65  . . 142 3657 99.95  . . . . 0.2604 . . . . . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 2.65 2.82  . . 141 3651 100.00 . . . . 0.2674 . . . . . . . . . . . . . . . 0.3037 
'X-RAY DIFFRACTION' 2.82 3.04  . . 143 3681 100.00 . . . . 0.2778 . . . . . . . . . . . . . . . 0.2769 
'X-RAY DIFFRACTION' 3.04 3.34  . . 143 3688 99.97  . . . . 0.2474 . . . . . . . . . . . . . . . 0.2977 
'X-RAY DIFFRACTION' 3.34 3.83  . . 144 3722 100.00 . . . . 0.2184 . . . . . . . . . . . . . . . 0.2399 
'X-RAY DIFFRACTION' 3.83 4.82  . . 147 3776 100.00 . . . . 0.1820 . . . . . . . . . . . . . . . 0.2457 
'X-RAY DIFFRACTION' 4.82 84.01 . . 154 3957 99.85  . . . . 0.1926 . . . . . . . . . . . . . . . 0.1999 
# 
_struct.entry_id                     9OB6 
_struct.title                        'CDK2/CyclinE bound to compound 21 with P-loop in the EE and CC conformations' 
_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        9OB6 
_struct_keywords.text            'CDK/Cyclin, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CDK2_HUMAN  P24941 ? 1 
;MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
1  
2 UNP CCNE1_HUMAN P24864 ? 2 
;IIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFFDR
YMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVYMQ
VAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVPFA
MVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKA
;
96 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9OB6 A 4 ? 301 ? P24941 1  ? 298 ? 1  298 
2 2 9OB6 B 3 ? 285 ? P24864 96 ? 378 ? 96 378 
# 
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 9OB6 SER A 1 ? UNP P24941 ? ? 'expression tag' -2 1 
1 9OB6 HIS A 2 ? UNP P24941 ? ? 'expression tag' -1 2 
1 9OB6 MET A 3 ? UNP P24941 ? ? 'expression tag' 0  3 
2 9OB6 GLY B 1 ? UNP P24864 ? ? 'expression tag' 94 4 
2 9OB6 SER B 2 ? UNP P24864 ? ? 'expression tag' 95 5 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 4440  ? 
1 MORE         -23   ? 
1 'SSA (A^2)'  25070 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 ASP A 41  ? GLU A 43  ? ASP A 38  GLU A 40  5 ? 3  
HELX_P HELX_P2  AA2 PRO A 48  ? LYS A 59  ? PRO A 45  LYS A 56  1 ? 12 
HELX_P HELX_P3  AA3 LEU A 90  ? SER A 97  ? LEU A 87  SER A 94  1 ? 8  
HELX_P HELX_P4  AA4 PRO A 103 ? HIS A 124 ? PRO A 100 HIS A 121 1 ? 22 
HELX_P HELX_P5  AA5 LYS A 132 ? GLN A 134 ? LYS A 129 GLN A 131 5 ? 3  
HELX_P HELX_P6  AA6 THR A 168 ? ARG A 172 ? THR A 165 ARG A 169 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 173 ? LEU A 178 ? ALA A 170 LEU A 175 1 ? 6  
HELX_P HELX_P8  AA8 THR A 185 ? ARG A 202 ? THR A 182 ARG A 199 1 ? 18 
HELX_P HELX_P9  AA9 SER A 210 ? GLY A 223 ? SER A 207 GLY A 220 1 ? 14 
HELX_P HELX_P10 AB1 GLY A 232 ? MET A 236 ? GLY A 229 MET A 233 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 250 ? VAL A 255 ? ASP A 247 VAL A 252 1 ? 6  
HELX_P HELX_P12 AB3 ASP A 259 ? LEU A 270 ? ASP A 256 LEU A 267 1 ? 12 
HELX_P HELX_P13 AB4 SER A 279 ? ALA A 285 ? SER A 276 ALA A 282 1 ? 7  
HELX_P HELX_P14 AB5 HIS A 286 ? GLN A 290 ? HIS A 283 GLN A 287 5 ? 5  
HELX_P HELX_P15 AB6 ASN B 19  ? TYR B 34  ? ASN B 112 TYR B 127 1 ? 16 
HELX_P HELX_P16 AB7 HIS B 39  ? HIS B 44  ? HIS B 132 HIS B 137 5 ? 6  
HELX_P HELX_P17 AB8 GLN B 48  ? TYR B 66  ? GLN B 141 TYR B 159 1 ? 19 
HELX_P HELX_P18 AB9 HIS B 69  ? ALA B 85  ? HIS B 162 ALA B 178 1 ? 17 
HELX_P HELX_P19 AC1 VAL B 91  ? THR B 93  ? VAL B 184 THR B 186 5 ? 3  
HELX_P HELX_P20 AC2 LEU B 94  ? GLU B 111 ? LEU B 187 GLU B 204 1 ? 18 
HELX_P HELX_P21 AC3 LYS B 116 ? VAL B 123 ? LYS B 209 VAL B 216 1 ? 8  
HELX_P HELX_P22 AC4 SER B 129 ? LEU B 144 ? SER B 222 LEU B 237 1 ? 16 
HELX_P HELX_P23 AC5 THR B 152 ? TYR B 165 ? THR B 245 TYR B 258 1 ? 14 
HELX_P HELX_P24 AC6 PRO B 178 ? VAL B 193 ? PRO B 271 VAL B 286 1 ? 16 
HELX_P HELX_P25 AC7 LEU B 194 ? PHE B 201 ? LEU B 287 PHE B 294 5 ? 8  
HELX_P HELX_P26 AC8 PRO B 202 ? PHE B 214 ? PRO B 295 PHE B 307 1 ? 13 
HELX_P HELX_P27 AC9 SER B 216 ? GLY B 225 ? SER B 309 GLY B 318 1 ? 10 
HELX_P HELX_P28 AD1 GLN B 227 ? GLY B 249 ? GLN B 320 GLY B 342 1 ? 23 
HELX_P HELX_P29 AD2 ALA B 260 ? ILE B 267 ? ALA B 353 ILE B 360 5 ? 8  
HELX_P HELX_P30 AD3 SER B 273 ? ALA B 280 ? SER B 366 ALA B 373 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A TYR 162 C ? ? ? 1_555 A TPO 163 N ? ? A TYR 159 A TPO 160 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale2 covale both ? A TPO 163 C ? ? ? 1_555 A HIS 164 N ? ? A TPO 160 A HIS 161 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      TPO 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       163 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       TPO 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        160 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                THR 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        TPO 
_pdbx_modification_feature.type                               Phosphorylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          VAL 
_struct_mon_prot_cis.label_seq_id           157 
_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           VAL 
_struct_mon_prot_cis.auth_seq_id            154 
_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    158 
_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     155 
_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       1.98 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 7   ? GLU A 15  ? PHE A 4   GLU A 12  
AA1 2 VAL A 20  ? ASN A 26  ? VAL A 17  ASN A 23  
AA1 3 VAL A 32  ? ARG A 39  ? VAL A 29  ARG A 36  
AA1 4 LYS A 78  ? GLU A 84  ? LYS A 75  GLU A 81  
AA1 5 LEU A 69  ? THR A 75  ? LEU A 66  THR A 72  
AA2 1 GLN A 88  ? ASP A 89  ? GLN A 85  ASP A 86  
AA2 2 LEU A 136 ? ILE A 138 ? LEU A 133 ILE A 135 
AA2 3 ILE A 144 ? LEU A 146 ? ILE A 141 LEU A 143 
AA3 1 VAL A 126 ? LEU A 127 ? VAL A 123 LEU A 124 
AA3 2 ARG A 153 ? ALA A 154 ? ARG A 150 ALA A 151 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 10  ? N VAL A 7   O LYS A 23  ? O LYS A 20  
AA1 2 3 N TYR A 22  ? N TYR A 19  O LEU A 35  ? O LEU A 32  
AA1 3 4 N ALA A 34  ? N ALA A 31  O PHE A 83  ? O PHE A 80  
AA1 4 5 O TYR A 80  ? O TYR A 77  N ILE A 73  ? N ILE A 70  
AA2 1 2 N GLN A 88  ? N GLN A 85  O ILE A 138 ? O ILE A 135 
AA2 2 3 N LEU A 137 ? N LEU A 134 O LYS A 145 ? O LYS A 142 
AA3 1 2 N LEU A 127 ? N LEU A 124 O ARG A 153 ? O ARG A 150 
# 
_pdbx_entry_details.entry_id                   9OB6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 58  ? ? -116.40 68.46   
2  1 GLU A 73  ? ? 59.41   -142.16 
3  1 ASN A 74  ? ? -91.47  34.10   
4  1 ASP A 127 ? ? -155.34 46.82   
5  1 ASP A 145 ? ? 57.92   85.37   
6  1 VAL A 164 ? ? 68.67   136.82  
7  1 SER A 181 ? ? -148.28 -126.46 
8  1 PRO A 284 ? ? -59.89  -9.82   
9  1 ASN B 182 ? ? 59.66   93.49   
10 1 TYR B 258 ? ? -119.38 57.58   
11 1 ASN B 260 ? ? -108.71 -161.65 
12 1 SER B 308 ? ? -146.69 -110.00 
13 1 ASP B 365 ? ? -61.53  83.70   
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    TPO 
_pdbx_struct_mod_residue.label_seq_id     163 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     TPO 
_pdbx_struct_mod_residue.auth_seq_id      160 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   THR 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/4  
3 y+1/2,-x+1/2,z+3/4  
4 x+1/2,-y+1/2,-z+3/4 
5 -x+1/2,y+1/2,-z+1/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         26.3594732964 
_pdbx_refine_tls.origin_y         6.71909488179 
_pdbx_refine_tls.origin_z         -18.3487997159 
_pdbx_refine_tls.T[1][1]          0.354639565798 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.020976950084 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0182855269501 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.504890032006 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.00784648047082 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.455129807229 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.07265443381 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.256409296986 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.808641798617 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.7817244173 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          1.11360678405 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.87703935199 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.20999505725 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.176590272517 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.158295069198 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.111210251946 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0895129720026 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0901884071146 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.50708222803 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.262915483904 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.234357839294 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   D 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    W 
_pdbx_refine_tls_group.end_auth_seq_id     58 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 SER -2  ? A SER 1   
2  1 Y 1 A HIS -1  ? A HIS 2   
3  1 Y 1 A MET 0   ? A MET 3   
4  1 Y 1 B GLY 94  ? B GLY 1   
5  1 Y 1 B SER 95  ? B SER 2   
6  1 Y 1 B ILE 96  ? B ILE 3   
7  1 Y 1 B ILE 97  ? B ILE 4   
8  1 Y 1 B ALA 98  ? B ALA 5   
9  1 Y 1 B PRO 99  ? B PRO 6   
10 1 Y 1 B SER 100 ? B SER 7   
11 1 Y 1 B ARG 101 ? B ARG 8   
12 1 Y 1 B LYS 376 ? B LYS 283 
13 1 Y 1 B LYS 377 ? B LYS 284 
14 1 Y 1 B ALA 378 ? B ALA 285 
# 
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 
A1CAI C13  C Y N 1   
A1CAI C14  C N S 2   
A1CAI C15  C N N 3   
A1CAI C16  C N N 4   
A1CAI C17  C N R 5   
A1CAI C18  C N N 6   
A1CAI C20  C N N 7   
A1CAI C22  C N N 8   
A1CAI C23  C N N 9   
A1CAI C24  C N N 10  
A1CAI C26  C Y N 11  
A1CAI C28  C Y N 12  
A1CAI C29  C Y N 13  
A1CAI C01  C N N 14  
A1CAI C03  C Y N 15  
A1CAI C04  C Y N 16  
A1CAI C05  C Y N 17  
A1CAI C06  C Y N 18  
A1CAI C07  C N N 19  
A1CAI C08  C N N 20  
A1CAI C10  C Y N 21  
A1CAI N09  N N N 22  
A1CAI N11  N Y N 23  
A1CAI N12  N Y N 24  
A1CAI N21  N N N 25  
A1CAI O02  O N N 26  
A1CAI O19  O N N 27  
A1CAI O25  O N N 28  
A1CAI O27  O N N 29  
A1CAI H141 H N N 30  
A1CAI H151 H N N 31  
A1CAI H152 H N N 32  
A1CAI H161 H N N 33  
A1CAI H162 H N N 34  
A1CAI H171 H N N 35  
A1CAI H181 H N N 36  
A1CAI H182 H N N 37  
A1CAI H221 H N N 38  
A1CAI H231 H N N 39  
A1CAI H232 H N N 40  
A1CAI H233 H N N 41  
A1CAI H241 H N N 42  
A1CAI H243 H N N 43  
A1CAI H242 H N N 44  
A1CAI H261 H N N 45  
A1CAI H281 H N N 46  
A1CAI H291 H N N 47  
A1CAI H013 H N N 48  
A1CAI H012 H N N 49  
A1CAI H011 H N N 50  
A1CAI H041 H N N 51  
A1CAI H051 H N N 52  
A1CAI H071 H N N 53  
A1CAI H072 H N N 54  
A1CAI H091 H N N 55  
A1CAI H121 H N N 56  
A1CAI H211 H N N 57  
ALA   N    N N N 58  
ALA   CA   C N S 59  
ALA   C    C N N 60  
ALA   O    O N N 61  
ALA   CB   C N N 62  
ALA   OXT  O N N 63  
ALA   H    H N N 64  
ALA   H2   H N N 65  
ALA   HA   H N N 66  
ALA   HB1  H N N 67  
ALA   HB2  H N N 68  
ALA   HB3  H N N 69  
ALA   HXT  H N N 70  
ARG   N    N N N 71  
ARG   CA   C N S 72  
ARG   C    C N N 73  
ARG   O    O N N 74  
ARG   CB   C N N 75  
ARG   CG   C N N 76  
ARG   CD   C N N 77  
ARG   NE   N N N 78  
ARG   CZ   C N N 79  
ARG   NH1  N N N 80  
ARG   NH2  N N N 81  
ARG   OXT  O N N 82  
ARG   H    H N N 83  
ARG   H2   H N N 84  
ARG   HA   H N N 85  
ARG   HB2  H N N 86  
ARG   HB3  H N N 87  
ARG   HG2  H N N 88  
ARG   HG3  H N N 89  
ARG   HD2  H N N 90  
ARG   HD3  H N N 91  
ARG   HE   H N N 92  
ARG   HH11 H N N 93  
ARG   HH12 H N N 94  
ARG   HH21 H N N 95  
ARG   HH22 H N N 96  
ARG   HXT  H N N 97  
ASN   N    N N N 98  
ASN   CA   C N S 99  
ASN   C    C N N 100 
ASN   O    O N N 101 
ASN   CB   C N N 102 
ASN   CG   C N N 103 
ASN   OD1  O N N 104 
ASN   ND2  N N N 105 
ASN   OXT  O N N 106 
ASN   H    H N N 107 
ASN   H2   H N N 108 
ASN   HA   H N N 109 
ASN   HB2  H N N 110 
ASN   HB3  H N N 111 
ASN   HD21 H N N 112 
ASN   HD22 H N N 113 
ASN   HXT  H N N 114 
ASP   N    N N N 115 
ASP   CA   C N S 116 
ASP   C    C N N 117 
ASP   O    O N N 118 
ASP   CB   C N N 119 
ASP   CG   C N N 120 
ASP   OD1  O N N 121 
ASP   OD2  O N N 122 
ASP   OXT  O N N 123 
ASP   H    H N N 124 
ASP   H2   H N N 125 
ASP   HA   H N N 126 
ASP   HB2  H N N 127 
ASP   HB3  H N N 128 
ASP   HD2  H N N 129 
ASP   HXT  H N N 130 
CYS   N    N N N 131 
CYS   CA   C N R 132 
CYS   C    C N N 133 
CYS   O    O N N 134 
CYS   CB   C N N 135 
CYS   SG   S N N 136 
CYS   OXT  O N N 137 
CYS   H    H N N 138 
CYS   H2   H N N 139 
CYS   HA   H N N 140 
CYS   HB2  H N N 141 
CYS   HB3  H N N 142 
CYS   HG   H N N 143 
CYS   HXT  H N N 144 
GLN   N    N N N 145 
GLN   CA   C N S 146 
GLN   C    C N N 147 
GLN   O    O N N 148 
GLN   CB   C N N 149 
GLN   CG   C N N 150 
GLN   CD   C N N 151 
GLN   OE1  O N N 152 
GLN   NE2  N N N 153 
GLN   OXT  O N N 154 
GLN   H    H N N 155 
GLN   H2   H N N 156 
GLN   HA   H N N 157 
GLN   HB2  H N N 158 
GLN   HB3  H N N 159 
GLN   HG2  H N N 160 
GLN   HG3  H N N 161 
GLN   HE21 H N N 162 
GLN   HE22 H N N 163 
GLN   HXT  H N N 164 
GLU   N    N N N 165 
GLU   CA   C N S 166 
GLU   C    C N N 167 
GLU   O    O N N 168 
GLU   CB   C N N 169 
GLU   CG   C N N 170 
GLU   CD   C N N 171 
GLU   OE1  O N N 172 
GLU   OE2  O N N 173 
GLU   OXT  O N N 174 
GLU   H    H N N 175 
GLU   H2   H N N 176 
GLU   HA   H N N 177 
GLU   HB2  H N N 178 
GLU   HB3  H N N 179 
GLU   HG2  H N N 180 
GLU   HG3  H N N 181 
GLU   HE2  H N N 182 
GLU   HXT  H N N 183 
GLY   N    N N N 184 
GLY   CA   C N N 185 
GLY   C    C N N 186 
GLY   O    O N N 187 
GLY   OXT  O N N 188 
GLY   H    H N N 189 
GLY   H2   H N N 190 
GLY   HA2  H N N 191 
GLY   HA3  H N N 192 
GLY   HXT  H N N 193 
HIS   N    N N N 194 
HIS   CA   C N S 195 
HIS   C    C N N 196 
HIS   O    O N N 197 
HIS   CB   C N N 198 
HIS   CG   C Y N 199 
HIS   ND1  N Y N 200 
HIS   CD2  C Y N 201 
HIS   CE1  C Y N 202 
HIS   NE2  N Y N 203 
HIS   OXT  O N N 204 
HIS   H    H N N 205 
HIS   H2   H N N 206 
HIS   HA   H N N 207 
HIS   HB2  H N N 208 
HIS   HB3  H N N 209 
HIS   HD1  H N N 210 
HIS   HD2  H N N 211 
HIS   HE1  H N N 212 
HIS   HE2  H N N 213 
HIS   HXT  H N N 214 
HOH   O    O N N 215 
HOH   H1   H N N 216 
HOH   H2   H N N 217 
ILE   N    N N N 218 
ILE   CA   C N S 219 
ILE   C    C N N 220 
ILE   O    O N N 221 
ILE   CB   C N S 222 
ILE   CG1  C N N 223 
ILE   CG2  C N N 224 
ILE   CD1  C N N 225 
ILE   OXT  O N N 226 
ILE   H    H N N 227 
ILE   H2   H N N 228 
ILE   HA   H N N 229 
ILE   HB   H N N 230 
ILE   HG12 H N N 231 
ILE   HG13 H N N 232 
ILE   HG21 H N N 233 
ILE   HG22 H N N 234 
ILE   HG23 H N N 235 
ILE   HD11 H N N 236 
ILE   HD12 H N N 237 
ILE   HD13 H N N 238 
ILE   HXT  H N N 239 
LEU   N    N N N 240 
LEU   CA   C N S 241 
LEU   C    C N N 242 
LEU   O    O N N 243 
LEU   CB   C N N 244 
LEU   CG   C N N 245 
LEU   CD1  C N N 246 
LEU   CD2  C N N 247 
LEU   OXT  O N N 248 
LEU   H    H N N 249 
LEU   H2   H N N 250 
LEU   HA   H N N 251 
LEU   HB2  H N N 252 
LEU   HB3  H N N 253 
LEU   HG   H N N 254 
LEU   HD11 H N N 255 
LEU   HD12 H N N 256 
LEU   HD13 H N N 257 
LEU   HD21 H N N 258 
LEU   HD22 H N N 259 
LEU   HD23 H N N 260 
LEU   HXT  H N N 261 
LYS   N    N N N 262 
LYS   CA   C N S 263 
LYS   C    C N N 264 
LYS   O    O N N 265 
LYS   CB   C N N 266 
LYS   CG   C N N 267 
LYS   CD   C N N 268 
LYS   CE   C N N 269 
LYS   NZ   N N N 270 
LYS   OXT  O N N 271 
LYS   H    H N N 272 
LYS   H2   H N N 273 
LYS   HA   H N N 274 
LYS   HB2  H N N 275 
LYS   HB3  H N N 276 
LYS   HG2  H N N 277 
LYS   HG3  H N N 278 
LYS   HD2  H N N 279 
LYS   HD3  H N N 280 
LYS   HE2  H N N 281 
LYS   HE3  H N N 282 
LYS   HZ1  H N N 283 
LYS   HZ2  H N N 284 
LYS   HZ3  H N N 285 
LYS   HXT  H N N 286 
MET   N    N N N 287 
MET   CA   C N S 288 
MET   C    C N N 289 
MET   O    O N N 290 
MET   CB   C N N 291 
MET   CG   C N N 292 
MET   SD   S N N 293 
MET   CE   C N N 294 
MET   OXT  O N N 295 
MET   H    H N N 296 
MET   H2   H N N 297 
MET   HA   H N N 298 
MET   HB2  H N N 299 
MET   HB3  H N N 300 
MET   HG2  H N N 301 
MET   HG3  H N N 302 
MET   HE1  H N N 303 
MET   HE2  H N N 304 
MET   HE3  H N N 305 
MET   HXT  H N N 306 
PHE   N    N N N 307 
PHE   CA   C N S 308 
PHE   C    C N N 309 
PHE   O    O N N 310 
PHE   CB   C N N 311 
PHE   CG   C Y N 312 
PHE   CD1  C Y N 313 
PHE   CD2  C Y N 314 
PHE   CE1  C Y N 315 
PHE   CE2  C Y N 316 
PHE   CZ   C Y N 317 
PHE   OXT  O N N 318 
PHE   H    H N N 319 
PHE   H2   H N N 320 
PHE   HA   H N N 321 
PHE   HB2  H N N 322 
PHE   HB3  H N N 323 
PHE   HD1  H N N 324 
PHE   HD2  H N N 325 
PHE   HE1  H N N 326 
PHE   HE2  H N N 327 
PHE   HZ   H N N 328 
PHE   HXT  H N N 329 
PRO   N    N N N 330 
PRO   CA   C N S 331 
PRO   C    C N N 332 
PRO   O    O N N 333 
PRO   CB   C N N 334 
PRO   CG   C N N 335 
PRO   CD   C N N 336 
PRO   OXT  O N N 337 
PRO   H    H N N 338 
PRO   HA   H N N 339 
PRO   HB2  H N N 340 
PRO   HB3  H N N 341 
PRO   HG2  H N N 342 
PRO   HG3  H N N 343 
PRO   HD2  H N N 344 
PRO   HD3  H N N 345 
PRO   HXT  H N N 346 
SER   N    N N N 347 
SER   CA   C N S 348 
SER   C    C N N 349 
SER   O    O N N 350 
SER   CB   C N N 351 
SER   OG   O N N 352 
SER   OXT  O N N 353 
SER   H    H N N 354 
SER   H2   H N N 355 
SER   HA   H N N 356 
SER   HB2  H N N 357 
SER   HB3  H N N 358 
SER   HG   H N N 359 
SER   HXT  H N N 360 
THR   N    N N N 361 
THR   CA   C N S 362 
THR   C    C N N 363 
THR   O    O N N 364 
THR   CB   C N R 365 
THR   OG1  O N N 366 
THR   CG2  C N N 367 
THR   OXT  O N N 368 
THR   H    H N N 369 
THR   H2   H N N 370 
THR   HA   H N N 371 
THR   HB   H N N 372 
THR   HG1  H N N 373 
THR   HG21 H N N 374 
THR   HG22 H N N 375 
THR   HG23 H N N 376 
THR   HXT  H N N 377 
TPO   N    N N N 378 
TPO   CA   C N S 379 
TPO   CB   C N R 380 
TPO   CG2  C N N 381 
TPO   OG1  O N N 382 
TPO   P    P N N 383 
TPO   O1P  O N N 384 
TPO   O2P  O N N 385 
TPO   O3P  O N N 386 
TPO   C    C N N 387 
TPO   O    O N N 388 
TPO   OXT  O N N 389 
TPO   H    H N N 390 
TPO   H2   H N N 391 
TPO   HA   H N N 392 
TPO   HB   H N N 393 
TPO   HG21 H N N 394 
TPO   HG22 H N N 395 
TPO   HG23 H N N 396 
TPO   HOP2 H N N 397 
TPO   HOP3 H N N 398 
TPO   HXT  H N N 399 
TRP   N    N N N 400 
TRP   CA   C N S 401 
TRP   C    C N N 402 
TRP   O    O N N 403 
TRP   CB   C N N 404 
TRP   CG   C Y N 405 
TRP   CD1  C Y N 406 
TRP   CD2  C Y N 407 
TRP   NE1  N Y N 408 
TRP   CE2  C Y N 409 
TRP   CE3  C Y N 410 
TRP   CZ2  C Y N 411 
TRP   CZ3  C Y N 412 
TRP   CH2  C Y N 413 
TRP   OXT  O N N 414 
TRP   H    H N N 415 
TRP   H2   H N N 416 
TRP   HA   H N N 417 
TRP   HB2  H N N 418 
TRP   HB3  H N N 419 
TRP   HD1  H N N 420 
TRP   HE1  H N N 421 
TRP   HE3  H N N 422 
TRP   HZ2  H N N 423 
TRP   HZ3  H N N 424 
TRP   HH2  H N N 425 
TRP   HXT  H N N 426 
TYR   N    N N N 427 
TYR   CA   C N S 428 
TYR   C    C N N 429 
TYR   O    O N N 430 
TYR   CB   C N N 431 
TYR   CG   C Y N 432 
TYR   CD1  C Y N 433 
TYR   CD2  C Y N 434 
TYR   CE1  C Y N 435 
TYR   CE2  C Y N 436 
TYR   CZ   C Y N 437 
TYR   OH   O N N 438 
TYR   OXT  O N N 439 
TYR   H    H N N 440 
TYR   H2   H N N 441 
TYR   HA   H N N 442 
TYR   HB2  H N N 443 
TYR   HB3  H N N 444 
TYR   HD1  H N N 445 
TYR   HD2  H N N 446 
TYR   HE1  H N N 447 
TYR   HE2  H N N 448 
TYR   HH   H N N 449 
TYR   HXT  H N N 450 
VAL   N    N N N 451 
VAL   CA   C N S 452 
VAL   C    C N N 453 
VAL   O    O N N 454 
VAL   CB   C N N 455 
VAL   CG1  C N N 456 
VAL   CG2  C N N 457 
VAL   OXT  O N N 458 
VAL   H    H N N 459 
VAL   H2   H N N 460 
VAL   HA   H N N 461 
VAL   HB   H N N 462 
VAL   HG11 H N N 463 
VAL   HG12 H N N 464 
VAL   HG13 H N N 465 
VAL   HG21 H N N 466 
VAL   HG22 H N N 467 
VAL   HG23 H N N 468 
VAL   HXT  H N N 469 
# 
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 
A1CAI O02 C01  sing N N 1   
A1CAI C03 O02  sing N N 2   
A1CAI C04 C03  doub Y N 3   
A1CAI C05 C04  sing Y N 4   
A1CAI C06 C05  doub Y N 5   
A1CAI C08 C07  sing N N 6   
A1CAI C10 N09  sing N N 7   
A1CAI N11 C10  doub Y N 8   
A1CAI N12 N11  sing Y N 9   
A1CAI C13 N12  sing Y N 10  
A1CAI C15 C14  sing N N 11  
A1CAI C16 C15  sing N N 12  
A1CAI C17 C16  sing N N 13  
A1CAI C18 C17  sing N N 14  
A1CAI O19 C17  sing N N 15  
A1CAI C20 O19  sing N N 16  
A1CAI C22 N21  sing N N 17  
A1CAI C23 C22  sing N N 18  
A1CAI C24 C22  sing N N 19  
A1CAI N21 C20  sing N N 20  
A1CAI O25 C20  doub N N 21  
A1CAI C14 C13  sing N N 22  
A1CAI C26 C13  doub Y N 23  
A1CAI N09 C08  sing N N 24  
A1CAI O27 C08  doub N N 25  
A1CAI C07 C06  sing N N 26  
A1CAI C28 C06  sing Y N 27  
A1CAI C29 C28  doub Y N 28  
A1CAI C03 C29  sing Y N 29  
A1CAI C10 C26  sing Y N 30  
A1CAI C14 C18  sing N N 31  
A1CAI C14 H141 sing N N 32  
A1CAI C15 H151 sing N N 33  
A1CAI C15 H152 sing N N 34  
A1CAI C16 H161 sing N N 35  
A1CAI C16 H162 sing N N 36  
A1CAI C17 H171 sing N N 37  
A1CAI C18 H181 sing N N 38  
A1CAI C18 H182 sing N N 39  
A1CAI C22 H221 sing N N 40  
A1CAI C23 H231 sing N N 41  
A1CAI C23 H232 sing N N 42  
A1CAI C23 H233 sing N N 43  
A1CAI C24 H241 sing N N 44  
A1CAI C24 H243 sing N N 45  
A1CAI C24 H242 sing N N 46  
A1CAI C26 H261 sing N N 47  
A1CAI C28 H281 sing N N 48  
A1CAI C29 H291 sing N N 49  
A1CAI C01 H013 sing N N 50  
A1CAI C01 H012 sing N N 51  
A1CAI C01 H011 sing N N 52  
A1CAI C04 H041 sing N N 53  
A1CAI C05 H051 sing N N 54  
A1CAI C07 H071 sing N N 55  
A1CAI C07 H072 sing N N 56  
A1CAI N09 H091 sing N N 57  
A1CAI N12 H121 sing N N 58  
A1CAI N21 H211 sing N N 59  
ALA   N   CA   sing N N 60  
ALA   N   H    sing N N 61  
ALA   N   H2   sing N N 62  
ALA   CA  C    sing N N 63  
ALA   CA  CB   sing N N 64  
ALA   CA  HA   sing N N 65  
ALA   C   O    doub N N 66  
ALA   C   OXT  sing N N 67  
ALA   CB  HB1  sing N N 68  
ALA   CB  HB2  sing N N 69  
ALA   CB  HB3  sing N N 70  
ALA   OXT HXT  sing N N 71  
ARG   N   CA   sing N N 72  
ARG   N   H    sing N N 73  
ARG   N   H2   sing N N 74  
ARG   CA  C    sing N N 75  
ARG   CA  CB   sing N N 76  
ARG   CA  HA   sing N N 77  
ARG   C   O    doub N N 78  
ARG   C   OXT  sing N N 79  
ARG   CB  CG   sing N N 80  
ARG   CB  HB2  sing N N 81  
ARG   CB  HB3  sing N N 82  
ARG   CG  CD   sing N N 83  
ARG   CG  HG2  sing N N 84  
ARG   CG  HG3  sing N N 85  
ARG   CD  NE   sing N N 86  
ARG   CD  HD2  sing N N 87  
ARG   CD  HD3  sing N N 88  
ARG   NE  CZ   sing N N 89  
ARG   NE  HE   sing N N 90  
ARG   CZ  NH1  sing N N 91  
ARG   CZ  NH2  doub N N 92  
ARG   NH1 HH11 sing N N 93  
ARG   NH1 HH12 sing N N 94  
ARG   NH2 HH21 sing N N 95  
ARG   NH2 HH22 sing N N 96  
ARG   OXT HXT  sing N N 97  
ASN   N   CA   sing N N 98  
ASN   N   H    sing N N 99  
ASN   N   H2   sing N N 100 
ASN   CA  C    sing N N 101 
ASN   CA  CB   sing N N 102 
ASN   CA  HA   sing N N 103 
ASN   C   O    doub N N 104 
ASN   C   OXT  sing N N 105 
ASN   CB  CG   sing N N 106 
ASN   CB  HB2  sing N N 107 
ASN   CB  HB3  sing N N 108 
ASN   CG  OD1  doub N N 109 
ASN   CG  ND2  sing N N 110 
ASN   ND2 HD21 sing N N 111 
ASN   ND2 HD22 sing N N 112 
ASN   OXT HXT  sing N N 113 
ASP   N   CA   sing N N 114 
ASP   N   H    sing N N 115 
ASP   N   H2   sing N N 116 
ASP   CA  C    sing N N 117 
ASP   CA  CB   sing N N 118 
ASP   CA  HA   sing N N 119 
ASP   C   O    doub N N 120 
ASP   C   OXT  sing N N 121 
ASP   CB  CG   sing N N 122 
ASP   CB  HB2  sing N N 123 
ASP   CB  HB3  sing N N 124 
ASP   CG  OD1  doub N N 125 
ASP   CG  OD2  sing N N 126 
ASP   OD2 HD2  sing N N 127 
ASP   OXT HXT  sing N N 128 
CYS   N   CA   sing N N 129 
CYS   N   H    sing N N 130 
CYS   N   H2   sing N N 131 
CYS   CA  C    sing N N 132 
CYS   CA  CB   sing N N 133 
CYS   CA  HA   sing N N 134 
CYS   C   O    doub N N 135 
CYS   C   OXT  sing N N 136 
CYS   CB  SG   sing N N 137 
CYS   CB  HB2  sing N N 138 
CYS   CB  HB3  sing N N 139 
CYS   SG  HG   sing N N 140 
CYS   OXT HXT  sing N N 141 
GLN   N   CA   sing N N 142 
GLN   N   H    sing N N 143 
GLN   N   H2   sing N N 144 
GLN   CA  C    sing N N 145 
GLN   CA  CB   sing N N 146 
GLN   CA  HA   sing N N 147 
GLN   C   O    doub N N 148 
GLN   C   OXT  sing N N 149 
GLN   CB  CG   sing N N 150 
GLN   CB  HB2  sing N N 151 
GLN   CB  HB3  sing N N 152 
GLN   CG  CD   sing N N 153 
GLN   CG  HG2  sing N N 154 
GLN   CG  HG3  sing N N 155 
GLN   CD  OE1  doub N N 156 
GLN   CD  NE2  sing N N 157 
GLN   NE2 HE21 sing N N 158 
GLN   NE2 HE22 sing N N 159 
GLN   OXT HXT  sing N N 160 
GLU   N   CA   sing N N 161 
GLU   N   H    sing N N 162 
GLU   N   H2   sing N N 163 
GLU   CA  C    sing N N 164 
GLU   CA  CB   sing N N 165 
GLU   CA  HA   sing N N 166 
GLU   C   O    doub N N 167 
GLU   C   OXT  sing N N 168 
GLU   CB  CG   sing N N 169 
GLU   CB  HB2  sing N N 170 
GLU   CB  HB3  sing N N 171 
GLU   CG  CD   sing N N 172 
GLU   CG  HG2  sing N N 173 
GLU   CG  HG3  sing N N 174 
GLU   CD  OE1  doub N N 175 
GLU   CD  OE2  sing N N 176 
GLU   OE2 HE2  sing N N 177 
GLU   OXT HXT  sing N N 178 
GLY   N   CA   sing N N 179 
GLY   N   H    sing N N 180 
GLY   N   H2   sing N N 181 
GLY   CA  C    sing N N 182 
GLY   CA  HA2  sing N N 183 
GLY   CA  HA3  sing N N 184 
GLY   C   O    doub N N 185 
GLY   C   OXT  sing N N 186 
GLY   OXT HXT  sing N N 187 
HIS   N   CA   sing N N 188 
HIS   N   H    sing N N 189 
HIS   N   H2   sing N N 190 
HIS   CA  C    sing N N 191 
HIS   CA  CB   sing N N 192 
HIS   CA  HA   sing N N 193 
HIS   C   O    doub N N 194 
HIS   C   OXT  sing N N 195 
HIS   CB  CG   sing N N 196 
HIS   CB  HB2  sing N N 197 
HIS   CB  HB3  sing N N 198 
HIS   CG  ND1  sing Y N 199 
HIS   CG  CD2  doub Y N 200 
HIS   ND1 CE1  doub Y N 201 
HIS   ND1 HD1  sing N N 202 
HIS   CD2 NE2  sing Y N 203 
HIS   CD2 HD2  sing N N 204 
HIS   CE1 NE2  sing Y N 205 
HIS   CE1 HE1  sing N N 206 
HIS   NE2 HE2  sing N N 207 
HIS   OXT HXT  sing N N 208 
HOH   O   H1   sing N N 209 
HOH   O   H2   sing N N 210 
ILE   N   CA   sing N N 211 
ILE   N   H    sing N N 212 
ILE   N   H2   sing N N 213 
ILE   CA  C    sing N N 214 
ILE   CA  CB   sing N N 215 
ILE   CA  HA   sing N N 216 
ILE   C   O    doub N N 217 
ILE   C   OXT  sing N N 218 
ILE   CB  CG1  sing N N 219 
ILE   CB  CG2  sing N N 220 
ILE   CB  HB   sing N N 221 
ILE   CG1 CD1  sing N N 222 
ILE   CG1 HG12 sing N N 223 
ILE   CG1 HG13 sing N N 224 
ILE   CG2 HG21 sing N N 225 
ILE   CG2 HG22 sing N N 226 
ILE   CG2 HG23 sing N N 227 
ILE   CD1 HD11 sing N N 228 
ILE   CD1 HD12 sing N N 229 
ILE   CD1 HD13 sing N N 230 
ILE   OXT HXT  sing N N 231 
LEU   N   CA   sing N N 232 
LEU   N   H    sing N N 233 
LEU   N   H2   sing N N 234 
LEU   CA  C    sing N N 235 
LEU   CA  CB   sing N N 236 
LEU   CA  HA   sing N N 237 
LEU   C   O    doub N N 238 
LEU   C   OXT  sing N N 239 
LEU   CB  CG   sing N N 240 
LEU   CB  HB2  sing N N 241 
LEU   CB  HB3  sing N N 242 
LEU   CG  CD1  sing N N 243 
LEU   CG  CD2  sing N N 244 
LEU   CG  HG   sing N N 245 
LEU   CD1 HD11 sing N N 246 
LEU   CD1 HD12 sing N N 247 
LEU   CD1 HD13 sing N N 248 
LEU   CD2 HD21 sing N N 249 
LEU   CD2 HD22 sing N N 250 
LEU   CD2 HD23 sing N N 251 
LEU   OXT HXT  sing N N 252 
LYS   N   CA   sing N N 253 
LYS   N   H    sing N N 254 
LYS   N   H2   sing N N 255 
LYS   CA  C    sing N N 256 
LYS   CA  CB   sing N N 257 
LYS   CA  HA   sing N N 258 
LYS   C   O    doub N N 259 
LYS   C   OXT  sing N N 260 
LYS   CB  CG   sing N N 261 
LYS   CB  HB2  sing N N 262 
LYS   CB  HB3  sing N N 263 
LYS   CG  CD   sing N N 264 
LYS   CG  HG2  sing N N 265 
LYS   CG  HG3  sing N N 266 
LYS   CD  CE   sing N N 267 
LYS   CD  HD2  sing N N 268 
LYS   CD  HD3  sing N N 269 
LYS   CE  NZ   sing N N 270 
LYS   CE  HE2  sing N N 271 
LYS   CE  HE3  sing N N 272 
LYS   NZ  HZ1  sing N N 273 
LYS   NZ  HZ2  sing N N 274 
LYS   NZ  HZ3  sing N N 275 
LYS   OXT HXT  sing N N 276 
MET   N   CA   sing N N 277 
MET   N   H    sing N N 278 
MET   N   H2   sing N N 279 
MET   CA  C    sing N N 280 
MET   CA  CB   sing N N 281 
MET   CA  HA   sing N N 282 
MET   C   O    doub N N 283 
MET   C   OXT  sing N N 284 
MET   CB  CG   sing N N 285 
MET   CB  HB2  sing N N 286 
MET   CB  HB3  sing N N 287 
MET   CG  SD   sing N N 288 
MET   CG  HG2  sing N N 289 
MET   CG  HG3  sing N N 290 
MET   SD  CE   sing N N 291 
MET   CE  HE1  sing N N 292 
MET   CE  HE2  sing N N 293 
MET   CE  HE3  sing N N 294 
MET   OXT HXT  sing N N 295 
PHE   N   CA   sing N N 296 
PHE   N   H    sing N N 297 
PHE   N   H2   sing N N 298 
PHE   CA  C    sing N N 299 
PHE   CA  CB   sing N N 300 
PHE   CA  HA   sing N N 301 
PHE   C   O    doub N N 302 
PHE   C   OXT  sing N N 303 
PHE   CB  CG   sing N N 304 
PHE   CB  HB2  sing N N 305 
PHE   CB  HB3  sing N N 306 
PHE   CG  CD1  doub Y N 307 
PHE   CG  CD2  sing Y N 308 
PHE   CD1 CE1  sing Y N 309 
PHE   CD1 HD1  sing N N 310 
PHE   CD2 CE2  doub Y N 311 
PHE   CD2 HD2  sing N N 312 
PHE   CE1 CZ   doub Y N 313 
PHE   CE1 HE1  sing N N 314 
PHE   CE2 CZ   sing Y N 315 
PHE   CE2 HE2  sing N N 316 
PHE   CZ  HZ   sing N N 317 
PHE   OXT HXT  sing N N 318 
PRO   N   CA   sing N N 319 
PRO   N   CD   sing N N 320 
PRO   N   H    sing N N 321 
PRO   CA  C    sing N N 322 
PRO   CA  CB   sing N N 323 
PRO   CA  HA   sing N N 324 
PRO   C   O    doub N N 325 
PRO   C   OXT  sing N N 326 
PRO   CB  CG   sing N N 327 
PRO   CB  HB2  sing N N 328 
PRO   CB  HB3  sing N N 329 
PRO   CG  CD   sing N N 330 
PRO   CG  HG2  sing N N 331 
PRO   CG  HG3  sing N N 332 
PRO   CD  HD2  sing N N 333 
PRO   CD  HD3  sing N N 334 
PRO   OXT HXT  sing N N 335 
SER   N   CA   sing N N 336 
SER   N   H    sing N N 337 
SER   N   H2   sing N N 338 
SER   CA  C    sing N N 339 
SER   CA  CB   sing N N 340 
SER   CA  HA   sing N N 341 
SER   C   O    doub N N 342 
SER   C   OXT  sing N N 343 
SER   CB  OG   sing N N 344 
SER   CB  HB2  sing N N 345 
SER   CB  HB3  sing N N 346 
SER   OG  HG   sing N N 347 
SER   OXT HXT  sing N N 348 
THR   N   CA   sing N N 349 
THR   N   H    sing N N 350 
THR   N   H2   sing N N 351 
THR   CA  C    sing N N 352 
THR   CA  CB   sing N N 353 
THR   CA  HA   sing N N 354 
THR   C   O    doub N N 355 
THR   C   OXT  sing N N 356 
THR   CB  OG1  sing N N 357 
THR   CB  CG2  sing N N 358 
THR   CB  HB   sing N N 359 
THR   OG1 HG1  sing N N 360 
THR   CG2 HG21 sing N N 361 
THR   CG2 HG22 sing N N 362 
THR   CG2 HG23 sing N N 363 
THR   OXT HXT  sing N N 364 
TPO   N   CA   sing N N 365 
TPO   N   H    sing N N 366 
TPO   N   H2   sing N N 367 
TPO   CA  CB   sing N N 368 
TPO   CA  C    sing N N 369 
TPO   CA  HA   sing N N 370 
TPO   CB  CG2  sing N N 371 
TPO   CB  OG1  sing N N 372 
TPO   CB  HB   sing N N 373 
TPO   CG2 HG21 sing N N 374 
TPO   CG2 HG22 sing N N 375 
TPO   CG2 HG23 sing N N 376 
TPO   OG1 P    sing N N 377 
TPO   P   O1P  doub N N 378 
TPO   P   O2P  sing N N 379 
TPO   P   O3P  sing N N 380 
TPO   O2P HOP2 sing N N 381 
TPO   O3P HOP3 sing N N 382 
TPO   C   O    doub N N 383 
TPO   C   OXT  sing N N 384 
TPO   OXT HXT  sing N N 385 
TRP   N   CA   sing N N 386 
TRP   N   H    sing N N 387 
TRP   N   H2   sing N N 388 
TRP   CA  C    sing N N 389 
TRP   CA  CB   sing N N 390 
TRP   CA  HA   sing N N 391 
TRP   C   O    doub N N 392 
TRP   C   OXT  sing N N 393 
TRP   CB  CG   sing N N 394 
TRP   CB  HB2  sing N N 395 
TRP   CB  HB3  sing N N 396 
TRP   CG  CD1  doub Y N 397 
TRP   CG  CD2  sing Y N 398 
TRP   CD1 NE1  sing Y N 399 
TRP   CD1 HD1  sing N N 400 
TRP   CD2 CE2  doub Y N 401 
TRP   CD2 CE3  sing Y N 402 
TRP   NE1 CE2  sing Y N 403 
TRP   NE1 HE1  sing N N 404 
TRP   CE2 CZ2  sing Y N 405 
TRP   CE3 CZ3  doub Y N 406 
TRP   CE3 HE3  sing N N 407 
TRP   CZ2 CH2  doub Y N 408 
TRP   CZ2 HZ2  sing N N 409 
TRP   CZ3 CH2  sing Y N 410 
TRP   CZ3 HZ3  sing N N 411 
TRP   CH2 HH2  sing N N 412 
TRP   OXT HXT  sing N N 413 
TYR   N   CA   sing N N 414 
TYR   N   H    sing N N 415 
TYR   N   H2   sing N N 416 
TYR   CA  C    sing N N 417 
TYR   CA  CB   sing N N 418 
TYR   CA  HA   sing N N 419 
TYR   C   O    doub N N 420 
TYR   C   OXT  sing N N 421 
TYR   CB  CG   sing N N 422 
TYR   CB  HB2  sing N N 423 
TYR   CB  HB3  sing N N 424 
TYR   CG  CD1  doub Y N 425 
TYR   CG  CD2  sing Y N 426 
TYR   CD1 CE1  sing Y N 427 
TYR   CD1 HD1  sing N N 428 
TYR   CD2 CE2  doub Y N 429 
TYR   CD2 HD2  sing N N 430 
TYR   CE1 CZ   doub Y N 431 
TYR   CE1 HE1  sing N N 432 
TYR   CE2 CZ   sing Y N 433 
TYR   CE2 HE2  sing N N 434 
TYR   CZ  OH   sing N N 435 
TYR   OH  HH   sing N N 436 
TYR   OXT HXT  sing N N 437 
VAL   N   CA   sing N N 438 
VAL   N   H    sing N N 439 
VAL   N   H2   sing N N 440 
VAL   CA  C    sing N N 441 
VAL   CA  CB   sing N N 442 
VAL   CA  HA   sing N N 443 
VAL   C   O    doub N N 444 
VAL   C   OXT  sing N N 445 
VAL   CB  CG1  sing N N 446 
VAL   CB  CG2  sing N N 447 
VAL   CB  HB   sing N N 448 
VAL   CG1 HG11 sing N N 449 
VAL   CG1 HG12 sing N N 450 
VAL   CG1 HG13 sing N N 451 
VAL   CG2 HG21 sing N N 452 
VAL   CG2 HG22 sing N N 453 
VAL   CG2 HG23 sing N N 454 
VAL   OXT HXT  sing N N 455 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Internal Model' 
# 
_space_group.name_H-M_alt     'P 41 21 2' 
_space_group.name_Hall        'P 4abw 2nw' 
_space_group.IT_number        92 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9OB6 
_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]   0.009891 
_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]   0.009891 
_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]   0.006621 
_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.
;
? 
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.
;
? 
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   . MET   A 1 4   ? 52.67470 10.56008  -3.82138  1.000 122.46513 ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 4   ? 51.88323 11.73047  -3.46109  1.000 132.80702 ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 4   ? 52.74367 12.77169  -2.74906  1.000 152.48288 ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 4   ? 52.77765 12.82495  -1.52121  1.000 149.36961 ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 4   ? 50.70166 11.32223  -2.57475  1.000 135.93824 ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 4   ? 49.70059 12.43453  -2.27160  1.000 129.36346 ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 4   ? 48.69950 12.93209  -3.68951  1.000 117.49208 ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 4   ? 49.58979 14.37801  -4.26168  1.000 120.33801 ? 1   MET   A CE  1 
ATOM   9    N N   . GLU   A 1 5   ? 53.44569 13.59544  -3.52038  1.000 180.47463 ? 2   GLU   A N   1 
ATOM   10   C CA  . GLU   A 1 5   ? 54.28838 14.64102  -2.95455  1.000 174.18427 ? 2   GLU   A CA  1 
ATOM   11   C C   . GLU   A 1 5   ? 54.26931 15.83221  -3.90252  1.000 167.04151 ? 2   GLU   A C   1 
ATOM   12   O O   . GLU   A 1 5   ? 53.51076 15.85676  -4.87682  1.000 164.15807 ? 2   GLU   A O   1 
ATOM   13   C CB  . GLU   A 1 5   ? 55.71160 14.12536  -2.70115  1.000 163.94795 ? 2   GLU   A CB  1 
ATOM   14   C CG  . GLU   A 1 5   ? 56.44885 13.64729  -3.94600  1.000 163.55778 ? 2   GLU   A CG  1 
ATOM   15   C CD  . GLU   A 1 5   ? 57.91258 13.34862  -3.67121  1.000 168.59867 ? 2   GLU   A CD  1 
ATOM   16   O OE1 . GLU   A 1 5   ? 58.41780 13.77457  -2.61042  1.000 170.07623 ? 2   GLU   A OE1 1 
ATOM   17   O OE2 . GLU   A 1 5   ? 58.55790 12.68852  -4.51281  1.000 161.78868 ? 2   GLU   A OE2 1 
ATOM   18   N N   . ASN   A 1 6   ? 55.10067 16.83210  -3.60019  1.000 134.38302 ? 3   ASN   A N   1 
ATOM   19   C CA  . ASN   A 1 6   ? 55.24107 18.03071  -4.42312  1.000 117.73437 ? 3   ASN   A CA  1 
ATOM   20   C C   . ASN   A 1 6   ? 53.95836 18.85486  -4.45010  1.000 103.09147 ? 3   ASN   A C   1 
ATOM   21   O O   . ASN   A 1 6   ? 53.87990 19.86565  -5.15582  1.000 101.94606 ? 3   ASN   A O   1 
ATOM   22   C CB  . ASN   A 1 6   ? 55.66944 17.66637  -5.84992  1.000 105.97425 ? 3   ASN   A CB  1 
ATOM   23   C CG  . ASN   A 1 6   ? 57.16425 17.45736  -5.97017  1.000 123.56877 ? 3   ASN   A CG  1 
ATOM   24   O OD1 . ASN   A 1 6   ? 57.93938 18.00084  -5.18361  1.000 124.21453 ? 3   ASN   A OD1 1 
ATOM   25   N ND2 . ASN   A 1 6   ? 57.57974 16.67633  -6.96357  1.000 120.20871 ? 3   ASN   A ND2 1 
ATOM   26   N N   . PHE   A 1 7   ? 52.94820 18.43024  -3.69532  1.000 100.32787 ? 4   PHE   A N   1 
ATOM   27   C CA  . PHE   A 1 7   ? 51.67760 19.13355  -3.59913  1.000 92.01743  ? 4   PHE   A CA  1 
ATOM   28   C C   . PHE   A 1 7   ? 51.43118 19.51702  -2.14834  1.000 83.88739  ? 4   PHE   A C   1 
ATOM   29   O O   . PHE   A 1 7   ? 51.48811 18.66377  -1.25602  1.000 85.01514  ? 4   PHE   A O   1 
ATOM   30   C CB  . PHE   A 1 7   ? 50.52699 18.27618  -4.13343  1.000 98.99199  ? 4   PHE   A CB  1 
ATOM   31   C CG  . PHE   A 1 7   ? 50.28196 18.44227  -5.60658  1.000 106.73045 ? 4   PHE   A CG  1 
ATOM   32   C CD1 . PHE   A 1 7   ? 50.60707 19.62768  -6.24594  1.000 101.66023 ? 4   PHE   A CD1 1 
ATOM   33   C CD2 . PHE   A 1 7   ? 49.72606 17.41532  -6.35155  1.000 100.08758 ? 4   PHE   A CD2 1 
ATOM   34   C CE1 . PHE   A 1 7   ? 50.38306 19.78553  -7.59970  1.000 101.60102 ? 4   PHE   A CE1 1 
ATOM   35   C CE2 . PHE   A 1 7   ? 49.50050 17.56694  -7.70651  1.000 102.50924 ? 4   PHE   A CE2 1 
ATOM   36   C CZ  . PHE   A 1 7   ? 49.83003 18.75432  -8.33112  1.000 114.35190 ? 4   PHE   A CZ  1 
ATOM   37   N N   . GLN   A 1 8   ? 51.16140 20.79883  -1.92017  1.000 79.00048  ? 5   GLN   A N   1 
ATOM   38   C CA  . GLN   A 1 8   ? 50.94155 21.34367  -0.58868  1.000 79.53489  ? 5   GLN   A CA  1 
ATOM   39   C C   . GLN   A 1 8   ? 49.53600 21.91868  -0.51506  1.000 75.81189  ? 5   GLN   A C   1 
ATOM   40   O O   . GLN   A 1 8   ? 49.16445 22.76278  -1.33713  1.000 72.26952  ? 5   GLN   A O   1 
ATOM   41   C CB  . GLN   A 1 8   ? 51.97775 22.42278  -0.25977  1.000 70.27934  ? 5   GLN   A CB  1 
ATOM   42   C CG  . GLN   A 1 8   ? 51.79671 23.07192  1.10050   1.000 95.70259  ? 5   GLN   A CG  1 
ATOM   43   C CD  . GLN   A 1 8   ? 52.84640 24.12871  1.38262   1.000 101.51100 ? 5   GLN   A CD  1 
ATOM   44   O OE1 . GLN   A 1 8   ? 52.78260 24.82708  2.39335   1.000 112.71046 ? 5   GLN   A OE1 1 
ATOM   45   N NE2 . GLN   A 1 8   ? 53.82158 24.25035  0.48792   1.000 105.66332 ? 5   GLN   A NE2 1 
ATOM   46   N N   . LYS   A 1 9   ? 48.75915 21.45653  0.46265   1.000 75.53803  ? 6   LYS   A N   1 
ATOM   47   C CA  . LYS   A 1 9   ? 47.40521 21.96220  0.64494   1.000 72.09332  ? 6   LYS   A CA  1 
ATOM   48   C C   . LYS   A 1 9   ? 47.43697 23.43917  1.01506   1.000 62.93362  ? 6   LYS   A C   1 
ATOM   49   O O   . LYS   A 1 9   ? 48.16419 23.84977  1.92319   1.000 62.26991  ? 6   LYS   A O   1 
ATOM   50   C CB  . LYS   A 1 9   ? 46.68134 21.15794  1.72521   1.000 73.30902  ? 6   LYS   A CB  1 
ATOM   51   C CG  . LYS   A 1 9   ? 46.43967 19.70219  1.35659   1.000 76.81584  ? 6   LYS   A CG  1 
ATOM   52   C CD  . LYS   A 1 9   ? 45.72017 18.95910  2.47129   1.000 79.09728  ? 6   LYS   A CD  1 
ATOM   53   C CE  . LYS   A 1 9   ? 45.46870 17.50752  2.09262   1.000 88.27423  ? 6   LYS   A CE  1 
ATOM   54   N NZ  . LYS   A 1 9   ? 44.80077 16.75179  3.18878   1.000 102.12720 ? 6   LYS   A NZ  1 
ATOM   55   N N   . VAL   A 1 10  ? 46.64699 24.23729  0.30404   1.000 57.53426  ? 7   VAL   A N   1 
ATOM   56   C CA  . VAL   A 1 10  ? 46.59657 25.67667  0.51805   1.000 72.40605  ? 7   VAL   A CA  1 
ATOM   57   C C   . VAL   A 1 10  ? 45.34425 26.08970  1.28034   1.000 63.58864  ? 7   VAL   A C   1 
ATOM   58   O O   . VAL   A 1 10  ? 45.41701 26.90797  2.19742   1.000 66.33255  ? 7   VAL   A O   1 
ATOM   59   C CB  . VAL   A 1 10  ? 46.69324 26.41785  -0.83294  1.000 73.98495  ? 7   VAL   A CB  1 
ATOM   60   C CG1 . VAL   A 1 10  ? 46.60526 27.92251  -0.62285  1.000 69.91059  ? 7   VAL   A CG1 1 
ATOM   61   C CG2 . VAL   A 1 10  ? 47.98167 26.04719  -1.54891  1.000 77.21006  ? 7   VAL   A CG2 1 
ATOM   62   N N   . GLU   A 1 11  ? 44.19220 25.53161  0.91652   1.000 65.07330  ? 8   GLU   A N   1 
ATOM   63   C CA  . GLU   A 1 11  ? 42.93100 25.90614  1.53833   1.000 66.04808  ? 8   GLU   A CA  1 
ATOM   64   C C   . GLU   A 1 11  ? 41.89287 24.83946  1.22350   1.000 59.48946  ? 8   GLU   A C   1 
ATOM   65   O O   . GLU   A 1 11  ? 41.93181 24.21316  0.16123   1.000 57.85659  ? 8   GLU   A O   1 
ATOM   66   C CB  . GLU   A 1 11  ? 42.45701 27.27951  1.04769   1.000 66.76143  ? 8   GLU   A CB  1 
ATOM   67   C CG  . GLU   A 1 11  ? 41.27124 27.84931  1.80706   1.000 88.82923  ? 8   GLU   A CG  1 
ATOM   68   C CD  . GLU   A 1 11  ? 40.83456 29.19618  1.26783   1.000 101.04049 ? 8   GLU   A CD  1 
ATOM   69   O OE1 . GLU   A 1 11  ? 41.32039 29.58869  0.18586   1.000 81.89471  ? 8   GLU   A OE1 1 
ATOM   70   O OE2 . GLU   A 1 11  ? 40.00678 29.86265  1.92436   1.000 95.00026  ? 8   GLU   A OE2 1 
ATOM   71   N N   . LYS   A 1 12  ? 40.97039 24.63498  2.16107   1.000 52.12489  ? 9   LYS   A N   1 
ATOM   72   C CA  . LYS   A 1 12  ? 39.85997 23.71970  1.94030   1.000 58.62060  ? 9   LYS   A CA  1 
ATOM   73   C C   . LYS   A 1 12  ? 38.80191 24.39223  1.07652   1.000 56.61603  ? 9   LYS   A C   1 
ATOM   74   O O   . LYS   A 1 12  ? 38.30973 25.47387  1.41139   1.000 58.64442  ? 9   LYS   A O   1 
ATOM   75   C CB  . LYS   A 1 12  ? 39.25351 23.27486  3.27022   1.000 64.01166  ? 9   LYS   A CB  1 
ATOM   76   C CG  . LYS   A 1 12  ? 38.03926 22.36578  3.12165   1.000 61.09269  ? 9   LYS   A CG  1 
ATOM   77   C CD  . LYS   A 1 12  ? 37.52456 21.90728  4.47779   1.000 65.00879  ? 9   LYS   A CD  1 
ATOM   78   C CE  . LYS   A 1 12  ? 36.29655 21.02095  4.34297   1.000 57.33293  ? 9   LYS   A CE  1 
ATOM   79   N NZ  . LYS   A 1 12  ? 35.84663 20.50136  5.66534   1.000 72.86957  ? 9   LYS   A NZ  1 
ATOM   80   N N   . ILE   A 1 13  ? 38.45326 23.74660  -0.03620  1.000 51.31703  ? 10  ILE   A N   1 
ATOM   81   C CA  . ILE   A 1 13  ? 37.46014 24.30664  -0.94593  1.000 59.14580  ? 10  ILE   A CA  1 
ATOM   82   C C   . ILE   A 1 13  ? 36.04654 23.97602  -0.47958  1.000 57.32669  ? 10  ILE   A C   1 
ATOM   83   O O   . ILE   A 1 13  ? 35.15123 24.82710  -0.52759  1.000 64.64933  ? 10  ILE   A O   1 
ATOM   84   C CB  . ILE   A 1 13  ? 37.72223 23.80726  -2.37895  1.000 49.29545  ? 10  ILE   A CB  1 
ATOM   85   C CG1 . ILE   A 1 13  ? 39.03216 24.38756  -2.91629  1.000 61.03686  ? 10  ILE   A CG1 1 
ATOM   86   C CG2 . ILE   A 1 13  ? 36.56266 24.16048  -3.29797  1.000 64.69739  ? 10  ILE   A CG2 1 
ATOM   87   C CD1 . ILE   A 1 13  ? 39.36096 23.94859  -4.32660  1.000 58.95857  ? 10  ILE   A CD1 1 
ATOM   88   N N   A GLY   A 1 14  ? 35.81893 22.74325  -0.04255  0.472 58.95962  ? 11  GLY   A N   1 
ATOM   89   N N   B GLY   A 1 14  ? 35.82366 22.75388  -0.00270  0.528 59.38873  ? 11  GLY   A N   1 
ATOM   90   C CA  A GLY   A 1 14  ? 34.48898 22.32718  0.36360   0.472 65.02192  ? 11  GLY   A CA  1 
ATOM   91   C CA  B GLY   A 1 14  ? 34.52218 22.39700  0.52555   0.528 64.98124  ? 11  GLY   A CA  1 
ATOM   92   C C   A GLY   A 1 14  ? 34.50141 20.87646  0.79063   0.472 67.23227  ? 11  GLY   A C   1 
ATOM   93   C C   B GLY   A 1 14  ? 34.35923 20.93125  0.86813   0.528 67.43529  ? 11  GLY   A C   1 
ATOM   94   O O   A GLY   A 1 14  ? 35.53864 20.20487  0.77038   0.472 55.80608  ? 11  GLY   A O   1 
ATOM   95   O O   B GLY   A 1 14  ? 35.14585 20.08613  0.43008   0.528 57.45503  ? 11  GLY   A O   1 
ATOM   96   N N   A GLU   A 1 15  ? 33.32025 20.39451  1.17570   0.472 69.70727  ? 12  GLU   A N   1 
ATOM   97   N N   B GLU   A 1 15  ? 33.33520 20.62172  1.66068   0.528 66.46339  ? 12  GLU   A N   1 
ATOM   98   C CA  A GLU   A 1 15  ? 33.17091 19.03794  1.68214   0.472 67.78031  ? 12  GLU   A CA  1 
ATOM   99   C CA  B GLU   A 1 15  ? 32.97741 19.24826  1.99215   0.528 67.19054  ? 12  GLU   A CA  1 
ATOM   100  C C   A GLU   A 1 15  ? 31.94440 18.38330  1.06413   0.472 67.64976  ? 12  GLU   A C   1 
ATOM   101  C C   B GLU   A 1 15  ? 31.48440 19.07406  1.76714   0.528 69.27391  ? 12  GLU   A C   1 
ATOM   102  O O   A GLU   A 1 15  ? 30.91972 19.03794  0.85255   0.472 68.77828  ? 12  GLU   A O   1 
ATOM   103  O O   B GLU   A 1 15  ? 30.67682 19.77818  2.38199   0.528 71.01262  ? 12  GLU   A O   1 
ATOM   104  C CB  A GLU   A 1 15  ? 33.06228 19.02922  3.21430   0.472 65.46799  ? 12  GLU   A CB  1 
ATOM   105  C CB  B GLU   A 1 15  ? 33.34398 18.90787  3.43783   0.528 65.10527  ? 12  GLU   A CB  1 
ATOM   106  C CG  A GLU   A 1 15  ? 32.97960 17.64251  3.83282   0.472 68.67229  ? 12  GLU   A CG  1 
ATOM   107  C CG  B GLU   A 1 15  ? 32.97061 17.49402  3.84512   0.528 68.72053  ? 12  GLU   A CG  1 
ATOM   108  C CD  A GLU   A 1 15  ? 33.06522 17.67449  5.34563   0.472 69.61359  ? 12  GLU   A CD  1 
ATOM   109  C CD  B GLU   A 1 15  ? 33.11757 17.26578  5.33289   0.528 70.77917  ? 12  GLU   A CD  1 
ATOM   110  O OE1 A GLU   A 1 15  ? 33.12077 18.78371  5.91745   0.472 64.14851  ? 12  GLU   A OE1 1 
ATOM   111  O OE1 B GLU   A 1 15  ? 33.30909 18.25736  6.06790   0.528 66.07632  ? 12  GLU   A OE1 1 
ATOM   112  O OE2 A GLU   A 1 15  ? 33.08096 16.58949  5.96287   0.472 76.69677  ? 12  GLU   A OE2 1 
ATOM   113  O OE2 B GLU   A 1 15  ? 33.04130 16.09739  5.76674   0.528 78.68401  ? 12  GLU   A OE2 1 
ATOM   114  N N   A GLY   A 1 16  ? 32.06051 17.08838  0.77559   0.472 67.57279  ? 13  GLY   A N   1 
ATOM   115  N N   B GLY   A 1 16  ? 31.12275 18.14773  0.90066   0.528 67.43943  ? 13  GLY   A N   1 
ATOM   116  C CA  A GLY   A 1 16  ? 30.95739 16.31742  0.23705   0.472 75.30877  ? 13  GLY   A CA  1 
ATOM   117  C CA  B GLY   A 1 16  ? 29.72985 17.91519  0.57292   0.528 69.75131  ? 13  GLY   A CA  1 
ATOM   118  C C   A GLY   A 1 16  ? 30.67450 15.05959  1.03375   0.472 71.61040  ? 13  GLY   A C   1 
ATOM   119  C C   B GLY   A 1 16  ? 29.51855 16.52446  0.02565   0.528 71.01577  ? 13  GLY   A C   1 
ATOM   120  O O   A GLY   A 1 16  ? 31.19318 14.88924  2.14144   0.472 67.66345  ? 13  GLY   A O   1 
ATOM   121  O O   B GLY   A 1 16  ? 30.22081 15.58301  0.39082   0.528 76.49709  ? 13  GLY   A O   1 
ATOM   122  N N   A THR   A 1 17  ? 29.85052 14.16845  0.47756   0.472 64.85941  ? 14  THR   A N   1 
ATOM   123  N N   B THR   A 1 17  ? 28.52737 16.40185  -0.86360  0.528 64.65187  ? 14  THR   A N   1 
ATOM   124  C CA  A THR   A 1 17  ? 29.51468 12.92919  1.17282   0.472 60.56805  ? 14  THR   A CA  1 
ATOM   125  C CA  B THR   A 1 17  ? 28.25032 15.11526  -1.49445  0.528 69.92029  ? 14  THR   A CA  1 
ATOM   126  C C   A THR   A 1 17  ? 30.73039 12.01628  1.29105   0.472 63.78783  ? 14  THR   A C   1 
ATOM   127  C C   B THR   A 1 17  ? 29.43132 14.63281  -2.32544  0.528 62.54688  ? 14  THR   A C   1 
ATOM   128  O O   A THR   A 1 17  ? 31.07475 11.56367  2.38985   0.472 60.41026  ? 14  THR   A O   1 
ATOM   129  O O   B THR   A 1 17  ? 29.60985 13.42300  -2.50836  0.528 69.18748  ? 14  THR   A O   1 
ATOM   130  C CB  A THR   A 1 17  ? 28.36923 12.21566  0.45008   0.472 71.00256  ? 14  THR   A CB  1 
ATOM   131  C CB  B THR   A 1 17  ? 27.00016 15.21762  -2.36868  0.528 71.33664  ? 14  THR   A CB  1 
ATOM   132  O OG1 A THR   A 1 17  ? 27.14514 12.93288  0.65876   0.472 69.71846  ? 14  THR   A OG1 1 
ATOM   133  O OG1 B THR   A 1 17  ? 27.20923 16.20438  -3.38642  0.528 70.61207  ? 14  THR   A OG1 1 
ATOM   134  C CG2 A THR   A 1 17  ? 28.21235 10.79038  0.96164   0.472 65.83355  ? 14  THR   A CG2 1 
ATOM   135  C CG2 B THR   A 1 17  ? 25.79455 15.61366  -1.52971  0.528 65.21199  ? 14  THR   A CG2 1 
ATOM   136  N N   A TYR   A 1 18  ? 31.39873 11.73844  0.16763   0.472 71.83431  ? 15  TYR   A N   1 
ATOM   137  N N   B TYR   A 1 18  ? 30.24462 15.55968  -2.83462  0.528 72.39349  ? 15  TYR   A N   1 
ATOM   138  C CA  A TYR   A 1 18  ? 32.57068 10.87440  0.15927   0.472 74.60087  ? 15  TYR   A CA  1 
ATOM   139  C CA  B TYR   A 1 18  ? 31.41455 15.17826  -3.61830  0.528 61.00578  ? 15  TYR   A CA  1 
ATOM   140  C C   A TYR   A 1 18  ? 33.88835 11.61846  0.00386   0.472 77.91271  ? 15  TYR   A C   1 
ATOM   141  C C   B TYR   A 1 18  ? 32.45721 14.48328  -2.75065  0.528 69.97253  ? 15  TYR   A C   1 
ATOM   142  O O   A TYR   A 1 18  ? 34.92762 11.08127  0.39918   0.472 75.66067  ? 15  TYR   A O   1 
ATOM   143  O O   B TYR   A 1 18  ? 33.02305 13.45677  -3.14411  0.528 75.70290  ? 15  TYR   A O   1 
ATOM   144  C CB  A TYR   A 1 18  ? 32.47140 9.83862   -0.97038  0.472 61.55290  ? 15  TYR   A CB  1 
ATOM   145  C CB  B TYR   A 1 18  ? 32.00932 16.41224  -4.29968  0.528 71.30572  ? 15  TYR   A CB  1 
ATOM   146  C CG  A TYR   A 1 18  ? 31.28162 8.91642   -0.86540  0.472 64.43682  ? 15  TYR   A CG  1 
ATOM   147  C CG  B TYR   A 1 18  ? 31.90352 17.68263  -3.48083  0.528 66.51013  ? 15  TYR   A CG  1 
ATOM   148  C CD1 A TYR   A 1 18  ? 31.22041 7.93976   0.11870   0.472 64.79451  ? 15  TYR   A CD1 1 
ATOM   149  C CD1 B TYR   A 1 18  ? 32.86780 18.00954  -2.53623  0.528 58.27049  ? 15  TYR   A CD1 1 
ATOM   150  C CD2 A TYR   A 1 18  ? 30.22371 9.01411   -1.75878  0.472 68.06004  ? 15  TYR   A CD2 1 
ATOM   151  C CD2 B TYR   A 1 18  ? 30.83997 18.55787  -3.65876  0.528 57.51490  ? 15  TYR   A CD2 1 
ATOM   152  C CE1 A TYR   A 1 18  ? 30.13568 7.08996   0.21518   0.472 68.39329  ? 15  TYR   A CE1 1 
ATOM   153  C CE1 B TYR   A 1 18  ? 32.77350 19.17006  -1.78890  0.528 63.30118  ? 15  TYR   A CE1 1 
ATOM   154  C CE2 A TYR   A 1 18  ? 29.13378 8.16880   -1.67058  0.472 68.14992  ? 15  TYR   A CE2 1 
ATOM   155  C CE2 B TYR   A 1 18  ? 30.73673 19.71852  -2.91694  0.528 57.64645  ? 15  TYR   A CE2 1 
ATOM   156  C CZ  A TYR   A 1 18  ? 29.09554 7.20895   -0.68174  0.472 64.73617  ? 15  TYR   A CZ  1 
ATOM   157  C CZ  B TYR   A 1 18  ? 31.70572 20.02032  -1.98405  0.528 61.98852  ? 15  TYR   A CZ  1 
ATOM   158  O OH  A TYR   A 1 18  ? 28.01302 6.36566   -0.59029  0.472 68.46645  ? 15  TYR   A OH  1 
ATOM   159  O OH  B TYR   A 1 18  ? 31.60459 21.17683  -1.24511  0.528 66.39199  ? 15  TYR   A OH  1 
ATOM   160  N N   A GLY   A 1 19  ? 33.87869 12.81859  -0.55232  0.472 96.52613  ? 16  GLY   A N   1 
ATOM   161  N N   B GLY   A 1 19  ? 32.71879 15.02421  -1.56400  0.528 94.23818  ? 16  GLY   A N   1 
ATOM   162  C CA  A GLY   A 1 19  ? 35.11307 13.53140  -0.84369  0.472 86.82329  ? 16  GLY   A CA  1 
ATOM   163  C CA  B GLY   A 1 19  ? 33.73008 14.47627  -0.68232  0.528 85.51116  ? 16  GLY   A CA  1 
ATOM   164  C C   A GLY   A 1 19  ? 35.15110 14.91670  -0.23903  0.472 80.94586  ? 16  GLY   A C   1 
ATOM   165  C C   B GLY   A 1 19  ? 34.42238 15.54737  0.13395   0.528 80.36818  ? 16  GLY   A C   1 
ATOM   166  O O   A GLY   A 1 19  ? 34.16481 15.65202  -0.27361  0.472 80.37371  ? 16  GLY   A O   1 
ATOM   167  O O   B GLY   A 1 19  ? 33.76261 16.33797  0.81424   0.528 77.81640  ? 16  GLY   A O   1 
ATOM   168  N N   A VAL   A 1 20  ? 36.30964 15.26475  0.31676   0.472 77.67764  ? 17  VAL   A N   1 
ATOM   169  N N   B VAL   A 1 20  ? 35.75240 15.57930  0.08362   0.528 77.89939  ? 17  VAL   A N   1 
ATOM   170  C CA  A VAL   A 1 20  ? 36.60577 16.61445  0.78323   0.472 66.05050  ? 17  VAL   A CA  1 
ATOM   171  C CA  B VAL   A 1 20  ? 36.55133 16.60383  0.74956   0.528 66.36431  ? 17  VAL   A CA  1 
ATOM   172  C C   A VAL   A 1 20  ? 37.58833 17.23737  -0.19843  0.472 64.19012  ? 17  VAL   A C   1 
ATOM   173  C C   B VAL   A 1 20  ? 37.49765 17.17939  -0.29549  0.528 64.07071  ? 17  VAL   A C   1 
ATOM   174  O O   A VAL   A 1 20  ? 38.63460 16.64843  -0.49493  0.472 65.59117  ? 17  VAL   A O   1 
ATOM   175  O O   B VAL   A 1 20  ? 38.43860 16.50176  -0.72481  0.528 64.07400  ? 17  VAL   A O   1 
ATOM   176  C CB  A VAL   A 1 20  ? 37.17964 16.61094  2.21092   0.472 65.20588  ? 17  VAL   A CB  1 
ATOM   177  C CB  B VAL   A 1 20  ? 37.33614 16.05397  1.94988   0.528 67.00746  ? 17  VAL   A CB  1 
ATOM   178  C CG1 A VAL   A 1 20  ? 37.53594 18.02594  2.64445   0.472 64.16777  ? 17  VAL   A CG1 1 
ATOM   179  C CG1 B VAL   A 1 20  ? 37.60577 17.16270  2.95902   0.528 66.68771  ? 17  VAL   A CG1 1 
ATOM   180  C CG2 A VAL   A 1 20  ? 36.18903 15.98516  3.18104   0.472 72.20352  ? 17  VAL   A CG2 1 
ATOM   181  C CG2 B VAL   A 1 20  ? 36.59544 14.89226  2.59907   0.528 75.63863  ? 17  VAL   A CG2 1 
ATOM   182  N N   . VAL   A 1 21  ? 37.25241 18.42065  -0.70457  1.000 55.35325  ? 18  VAL   A N   1 
ATOM   183  C CA  . VAL   A 1 21  ? 38.03763 19.07978  -1.74325  1.000 55.57308  ? 18  VAL   A CA  1 
ATOM   184  C C   . VAL   A 1 21  ? 38.97187 20.09503  -1.10154  1.000 67.75906  ? 18  VAL   A C   1 
ATOM   185  O O   . VAL   A 1 21  ? 38.53577 20.94750  -0.31747  1.000 51.85634  ? 18  VAL   A O   1 
ATOM   186  C CB  . VAL   A 1 21  ? 37.12847 19.75121  -2.78645  1.000 57.07543  ? 18  VAL   A CB  1 
ATOM   187  C CG1 . VAL   A 1 21  ? 37.96571 20.41604  -3.87001  1.000 52.90329  ? 18  VAL   A CG1 1 
ATOM   188  C CG2 . VAL   A 1 21  ? 36.18662 18.73050  -3.39615  1.000 60.40655  ? 18  VAL   A CG2 1 
ATOM   189  N N   . TYR   A 1 22  ? 40.25700 20.00430  -1.43670  1.000 50.08506  ? 19  TYR   A N   1 
ATOM   190  C CA  . TYR   A 1 22  ? 41.26241 20.96265  -1.00660  1.000 53.09436  ? 19  TYR   A CA  1 
ATOM   191  C C   . TYR   A 1 22  ? 41.89198 21.62748  -2.22241  1.000 58.79909  ? 19  TYR   A C   1 
ATOM   192  O O   . TYR   A 1 22  ? 41.94977 21.04561  -3.30977  1.000 63.16333  ? 19  TYR   A O   1 
ATOM   193  C CB  . TYR   A 1 22  ? 42.37033 20.29786  -0.17596  1.000 56.24022  ? 19  TYR   A CB  1 
ATOM   194  C CG  . TYR   A 1 22  ? 41.91363 19.68325  1.12587   1.000 68.29568  ? 19  TYR   A CG  1 
ATOM   195  C CD1 . TYR   A 1 22  ? 41.87215 20.43333  2.29393   1.000 66.88272  ? 19  TYR   A CD1 1 
ATOM   196  C CD2 . TYR   A 1 22  ? 41.54243 18.34710  1.19128   1.000 72.71580  ? 19  TYR   A CD2 1 
ATOM   197  C CE1 . TYR   A 1 22  ? 41.46260 19.87207  3.48907   1.000 78.07724  ? 19  TYR   A CE1 1 
ATOM   198  C CE2 . TYR   A 1 22  ? 41.13234 17.77703  2.38122   1.000 75.13435  ? 19  TYR   A CE2 1 
ATOM   199  C CZ  . TYR   A 1 22  ? 41.09377 18.54371  3.52616   1.000 72.88631  ? 19  TYR   A CZ  1 
ATOM   200  O OH  . TYR   A 1 22  ? 40.68541 17.98015  4.71282   1.000 91.54139  ? 19  TYR   A OH  1 
ATOM   201  N N   . LYS   A 1 23  ? 42.36802 22.85275  -2.02775  1.000 65.55310  ? 20  LYS   A N   1 
ATOM   202  C CA  . LYS   A 1 23  ? 43.17982 23.53533  -3.02596  1.000 55.04198  ? 20  LYS   A CA  1 
ATOM   203  C C   . LYS   A 1 23  ? 44.64673 23.26010  -2.72247  1.000 55.90833  ? 20  LYS   A C   1 
ATOM   204  O O   . LYS   A 1 23  ? 45.11890 23.54387  -1.61637  1.000 61.27452  ? 20  LYS   A O   1 
ATOM   205  C CB  . LYS   A 1 23  ? 42.90150 25.03769  -3.02948  1.000 52.55275  ? 20  LYS   A CB  1 
ATOM   206  C CG  . LYS   A 1 23  ? 43.80386 25.82691  -3.96627  1.000 58.71882  ? 20  LYS   A CG  1 
ATOM   207  C CD  . LYS   A 1 23  ? 43.51834 27.31710  -3.88677  1.000 62.55123  ? 20  LYS   A CD  1 
ATOM   208  C CE  . LYS   A 1 23  ? 44.41685 28.10415  -4.82649  1.000 63.64145  ? 20  LYS   A CE  1 
ATOM   209  N NZ  . LYS   A 1 23  ? 44.10984 29.56056  -4.79338  1.000 67.00139  ? 20  LYS   A NZ  1 
ATOM   210  N N   . ALA   A 1 24  ? 45.35915 22.69754  -3.69399  1.000 54.67726  ? 21  ALA   A N   1 
ATOM   211  C CA  . ALA   A 1 24  ? 46.76592 22.36559  -3.54108  1.000 54.80972  ? 21  ALA   A CA  1 
ATOM   212  C C   . ALA   A 1 24  ? 47.58423 23.07372  -4.61189  1.000 68.02178  ? 21  ALA   A C   1 
ATOM   213  O O   . ALA   A 1 24  ? 47.07530 23.43390  -5.67630  1.000 66.21488  ? 21  ALA   A O   1 
ATOM   214  C CB  . ALA   A 1 24  ? 46.99486 20.85089  -3.61957  1.000 76.71778  ? 21  ALA   A CB  1 
ATOM   215  N N   . ARG   A 1 25  ? 48.86839 23.26729  -4.31918  1.000 64.96837  ? 22  ARG   A N   1 
ATOM   216  C CA  . ARG   A 1 25  ? 49.76399 23.98369  -5.21712  1.000 71.70586  ? 22  ARG   A CA  1 
ATOM   217  C C   . ARG   A 1 25  ? 51.09545 23.25536  -5.30346  1.000 77.95909  ? 22  ARG   A C   1 
ATOM   218  O O   . ARG   A 1 25  ? 51.65722 22.85969  -4.27797  1.000 73.09965  ? 22  ARG   A O   1 
ATOM   219  C CB  . ARG   A 1 25  ? 49.98082 25.42568  -4.74367  1.000 71.77109  ? 22  ARG   A CB  1 
ATOM   220  C CG  . ARG   A 1 25  ? 51.00835 26.19361  -5.55366  1.000 79.61294  ? 22  ARG   A CG  1 
ATOM   221  C CD  . ARG   A 1 25  ? 51.26655 27.56360  -4.95710  1.000 90.56340  ? 22  ARG   A CD  1 
ATOM   222  N NE  . ARG   A 1 25  ? 52.63009 28.00789  -5.21577  1.000 107.05437 ? 22  ARG   A NE  1 
ATOM   223  C CZ  . ARG   A 1 25  ? 53.67657 27.66469  -4.47749  1.000 117.22267 ? 22  ARG   A CZ  1 
ATOM   224  N NH1 . ARG   A 1 25  ? 53.54881 26.87513  -3.42357  1.000 116.22232 ? 22  ARG   A NH1 1 
ATOM   225  N NH2 . ARG   A 1 25  ? 54.88120 28.12289  -4.80571  1.000 119.48785 ? 22  ARG   A NH2 1 
ATOM   226  N N   . ASN   A 1 26  ? 51.59381 23.08220  -6.52598  1.000 85.01793  ? 23  ASN   A N   1 
ATOM   227  C CA  . ASN   A 1 26  ? 52.90430 22.47857  -6.72405  1.000 91.07422  ? 23  ASN   A CA  1 
ATOM   228  C C   . ASN   A 1 26  ? 53.99549 23.48323  -6.37625  1.000 93.61325  ? 23  ASN   A C   1 
ATOM   229  O O   . ASN   A 1 26  ? 54.00516 24.60716  -6.88710  1.000 94.39872  ? 23  ASN   A O   1 
ATOM   230  C CB  . ASN   A 1 26  ? 53.05832 22.00264  -8.16803  1.000 93.39478  ? 23  ASN   A CB  1 
ATOM   231  C CG  . ASN   A 1 26  ? 54.32220 21.19268  -8.38413  1.000 102.33865 ? 23  ASN   A CG  1 
ATOM   232  O OD1 . ASN   A 1 26  ? 55.39957 21.74700  -8.60173  1.000 100.71798 ? 23  ASN   A OD1 1 
ATOM   233  N ND2 . ASN   A 1 26  ? 54.19492 19.87158  -8.32856  1.000 98.89792  ? 23  ASN   A ND2 1 
ATOM   234  N N   . LYS   A 1 27  ? 54.91781 23.07648  -5.50233  1.000 104.77072 ? 24  LYS   A N   1 
ATOM   235  C CA  . LYS   A 1 27  ? 55.96219 23.98773  -5.04962  1.000 108.87162 ? 24  LYS   A CA  1 
ATOM   236  C C   . LYS   A 1 27  ? 57.03419 24.20665  -6.11014  1.000 112.58674 ? 24  LYS   A C   1 
ATOM   237  O O   . LYS   A 1 27  ? 57.63895 25.28359  -6.15920  1.000 119.74868 ? 24  LYS   A O   1 
ATOM   238  C CB  . LYS   A 1 27  ? 56.59856 23.45669  -3.76347  1.000 129.83655 ? 24  LYS   A CB  1 
ATOM   239  C CG  . LYS   A 1 27  ? 57.27404 24.51935  -2.90946  1.000 134.12254 ? 24  LYS   A CG  1 
ATOM   240  C CD  . LYS   A 1 27  ? 56.24737 25.41666  -2.23688  1.000 136.00264 ? 24  LYS   A CD  1 
ATOM   241  C CE  . LYS   A 1 27  ? 56.91117 26.44122  -1.33116  1.000 121.08531 ? 24  LYS   A CE  1 
ATOM   242  N NZ  . LYS   A 1 27  ? 57.69552 25.79744  -0.24117  1.000 116.47812 ? 24  LYS   A NZ  1 
ATOM   243  N N   . LEU   A 1 28  ? 57.27906 23.21147  -6.96500  1.000 110.75859 ? 25  LEU   A N   1 
ATOM   244  C CA  . LEU   A 1 28  ? 58.34488 23.32758  -7.95496  1.000 117.58283 ? 25  LEU   A CA  1 
ATOM   245  C C   . LEU   A 1 28  ? 57.87507 24.03860  -9.21881  1.000 109.60690 ? 25  LEU   A C   1 
ATOM   246  O O   . LEU   A 1 28  ? 58.63518 24.80742  -9.81819  1.000 107.03676 ? 25  LEU   A O   1 
ATOM   247  C CB  . LEU   A 1 28  ? 58.89238 21.94253  -8.30285  1.000 109.97224 ? 25  LEU   A CB  1 
ATOM   248  C CG  . LEU   A 1 28  ? 59.59288 21.17418  -7.18073  1.000 115.70986 ? 25  LEU   A CG  1 
ATOM   249  C CD1 . LEU   A 1 28  ? 60.06541 19.81494  -7.67460  1.000 110.52021 ? 25  LEU   A CD1 1 
ATOM   250  C CD2 . LEU   A 1 28  ? 60.75648 21.97944  -6.62315  1.000 94.69481  ? 25  LEU   A CD2 1 
ATOM   251  N N   . THR   A 1 29  ? 56.63349 23.79667  -9.64042  1.000 103.44128 ? 26  THR   A N   1 
ATOM   252  C CA  . THR   A 1 29  ? 56.12293 24.34098  -10.88997 1.000 95.87047  ? 26  THR   A CA  1 
ATOM   253  C C   . THR   A 1 29  ? 55.13630 25.48472  -10.70355 1.000 89.70912  ? 26  THR   A C   1 
ATOM   254  O O   . THR   A 1 29  ? 54.80699 26.15888  -11.68582 1.000 91.29303  ? 26  THR   A O   1 
ATOM   255  C CB  . THR   A 1 29  ? 55.44964 23.23389  -11.71521 1.000 91.37924  ? 26  THR   A CB  1 
ATOM   256  O OG1 . THR   A 1 29  ? 54.22001 22.84935  -11.08917 1.000 86.38121  ? 26  THR   A OG1 1 
ATOM   257  C CG2 . THR   A 1 29  ? 56.35829 22.01824  -11.81137 1.000 105.54252 ? 26  THR   A CG2 1 
ATOM   258  N N   . GLY   A 1 30  ? 54.66034 25.72492  -9.48439  1.000 90.15799  ? 27  GLY   A N   1 
ATOM   259  C CA  . GLY   A 1 30  ? 53.65623 26.74276  -9.25606  1.000 89.59202  ? 27  GLY   A CA  1 
ATOM   260  C C   . GLY   A 1 30  ? 52.26356 26.37483  -9.71062  1.000 77.30746  ? 27  GLY   A C   1 
ATOM   261  O O   . GLY   A 1 30  ? 51.37266 27.23125  -9.68085  1.000 80.82193  ? 27  GLY   A O   1 
ATOM   262  N N   . GLU   A 1 31  ? 52.04576 25.12996  -10.12599 1.000 73.98506  ? 28  GLU   A N   1 
ATOM   263  C CA  . GLU   A 1 31  ? 50.74547 24.69959  -10.61929 1.000 70.09739  ? 28  GLU   A CA  1 
ATOM   264  C C   . GLU   A 1 31  ? 49.80477 24.41765  -9.45422  1.000 80.07803  ? 28  GLU   A C   1 
ATOM   265  O O   . GLU   A 1 31  ? 50.18052 23.74166  -8.49138  1.000 72.76014  ? 28  GLU   A O   1 
ATOM   266  C CB  . GLU   A 1 31  ? 50.90353 23.45414  -11.49076 1.000 77.63956  ? 28  GLU   A CB  1 
ATOM   267  C CG  . GLU   A 1 31  ? 49.60142 22.88174  -12.02365 1.000 87.10401  ? 28  GLU   A CG  1 
ATOM   268  C CD  . GLU   A 1 31  ? 49.82193 21.65398  -12.88756 1.000 102.33390 ? 28  GLU   A CD  1 
ATOM   269  O OE1 . GLU   A 1 31  ? 50.99538 21.29889  -13.12746 1.000 95.34442  ? 28  GLU   A OE1 1 
ATOM   270  O OE2 . GLU   A 1 31  ? 48.82407 21.04355  -13.32598 1.000 87.78236  ? 28  GLU   A OE2 1 
ATOM   271  N N   . VAL   A 1 32  ? 48.58262 24.93865  -9.54095  1.000 64.56697  ? 29  VAL   A N   1 
ATOM   272  C CA  . VAL   A 1 32  ? 47.55633 24.72099  -8.52829  1.000 60.24825  ? 29  VAL   A CA  1 
ATOM   273  C C   . VAL   A 1 32  ? 46.53383 23.73476  -9.07363  1.000 70.96142  ? 29  VAL   A C   1 
ATOM   274  O O   . VAL   A 1 32  ? 46.22562 23.73846  -10.27181 1.000 60.19910  ? 29  VAL   A O   1 
ATOM   275  C CB  . VAL   A 1 32  ? 46.87715 26.03754  -8.09908  1.000 64.25620  ? 29  VAL   A CB  1 
ATOM   276  C CG1 . VAL   A 1 32  ? 47.89277 26.97799  -7.46772  1.000 63.39477  ? 29  VAL   A CG1 1 
ATOM   277  C CG2 . VAL   A 1 32  ? 46.18504 26.70017  -9.28114  1.000 73.81721  ? 29  VAL   A CG2 1 
ATOM   278  N N   . VAL   A 1 33  ? 46.01918 22.87785  -8.19147  1.000 52.84541  ? 30  VAL   A N   1 
ATOM   279  C CA  . VAL   A 1 33  ? 45.02378 21.87406  -8.54359  1.000 55.30745  ? 30  VAL   A CA  1 
ATOM   280  C C   . VAL   A 1 33  ? 43.98146 21.81668  -7.43460  1.000 61.80048  ? 30  VAL   A C   1 
ATOM   281  O O   . VAL   A 1 33  ? 44.10943 22.46168  -6.39235  1.000 57.33955  ? 30  VAL   A O   1 
ATOM   282  C CB  . VAL   A 1 33  ? 45.64306 20.47576  -8.76082  1.000 57.57477  ? 30  VAL   A CB  1 
ATOM   283  C CG1 . VAL   A 1 33  ? 46.61000 20.48426  -9.93942  1.000 64.47874  ? 30  VAL   A CG1 1 
ATOM   284  C CG2 . VAL   A 1 33  ? 46.33547 20.00096  -7.49020  1.000 58.78045  ? 30  VAL   A CG2 1 
ATOM   285  N N   . ALA   A 1 34  ? 42.93794 21.02908  -7.67614  1.000 57.40530  ? 31  ALA   A N   1 
ATOM   286  C CA  . ALA   A 1 34  ? 41.91091 20.74050  -6.68407  1.000 51.06640  ? 31  ALA   A CA  1 
ATOM   287  C C   . ALA   A 1 34  ? 41.98034 19.25835  -6.34478  1.000 62.15399  ? 31  ALA   A C   1 
ATOM   288  O O   . ALA   A 1 34  ? 41.83383 18.40885  -7.23048  1.000 64.10076  ? 31  ALA   A O   1 
ATOM   289  C CB  . ALA   A 1 34  ? 40.52254 21.11698  -7.19970  1.000 56.10631  ? 31  ALA   A CB  1 
ATOM   290  N N   . LEU   A 1 35  ? 42.21096 18.95334  -5.07134  1.000 49.73635  ? 32  LEU   A N   1 
ATOM   291  C CA  . LEU   A 1 35  ? 42.37159 17.58500  -4.59556  1.000 55.50124  ? 32  LEU   A CA  1 
ATOM   292  C C   . LEU   A 1 35  ? 41.10498 17.14870  -3.87328  1.000 66.47321  ? 32  LEU   A C   1 
ATOM   293  O O   . LEU   A 1 35  ? 40.72761 17.74865  -2.86123  1.000 64.53347  ? 32  LEU   A O   1 
ATOM   294  C CB  . LEU   A 1 35  ? 43.57727 17.47001  -3.66208  1.000 58.54833  ? 32  LEU   A CB  1 
ATOM   295  C CG  . LEU   A 1 35  ? 44.92724 17.08251  -4.26415  1.000 74.57898  ? 32  LEU   A CG  1 
ATOM   296  C CD1 . LEU   A 1 35  ? 46.02895 17.26121  -3.23416  1.000 72.52335  ? 32  LEU   A CD1 1 
ATOM   297  C CD2 . LEU   A 1 35  ? 44.89208 15.64685  -4.76017  1.000 73.07032  ? 32  LEU   A CD2 1 
ATOM   298  N N   . LYS   A 1 36  ? 40.45640 16.10673  -4.38696  1.000 63.96876  ? 33  LYS   A N   1 
ATOM   299  C CA  . LYS   A 1 36  ? 39.34218 15.46726  -3.69963  1.000 64.75706  ? 33  LYS   A CA  1 
ATOM   300  C C   . LYS   A 1 36  ? 39.86472 14.22864  -2.98280  1.000 69.10231  ? 33  LYS   A C   1 
ATOM   301  O O   . LYS   A 1 36  ? 40.33990 13.28640  -3.62657  1.000 65.38994  ? 33  LYS   A O   1 
ATOM   302  C CB  . LYS   A 1 36  ? 38.21809 15.10116  -4.66813  1.000 57.24442  ? 33  LYS   A CB  1 
ATOM   303  C CG  . LYS   A 1 36  ? 37.06460 14.36563  -3.99875  1.000 69.16862  ? 33  LYS   A CG  1 
ATOM   304  C CD  . LYS   A 1 36  ? 35.73728 14.63747  -4.68795  1.000 66.50410  ? 33  LYS   A CD  1 
ATOM   305  C CE  . LYS   A 1 36  ? 35.73522 14.14241  -6.12206  1.000 78.33138  ? 33  LYS   A CE  1 
ATOM   306  N NZ  . LYS   A 1 36  ? 34.40719 14.34617  -6.76437  1.000 63.98309  ? 33  LYS   A NZ  1 
ATOM   307  N N   . LYS   A 1 37  ? 39.77893 14.23710  -1.65641  1.000 65.34770  ? 34  LYS   A N   1 
ATOM   308  C CA  . LYS   A 1 37  ? 40.33150 13.18166  -0.81907  1.000 63.31400  ? 34  LYS   A CA  1 
ATOM   309  C C   . LYS   A 1 37  ? 39.23513 12.19678  -0.43554  1.000 71.86300  ? 34  LYS   A C   1 
ATOM   310  O O   . LYS   A 1 37  ? 38.16991 12.60077  0.04275   1.000 75.46421  ? 34  LYS   A O   1 
ATOM   311  C CB  . LYS   A 1 37  ? 40.97505 13.77705  0.43405   1.000 68.79470  ? 34  LYS   A CB  1 
ATOM   312  C CG  . LYS   A 1 37  ? 41.57460 12.75806  1.38564   1.000 78.41324  ? 34  LYS   A CG  1 
ATOM   313  C CD  . LYS   A 1 37  ? 42.18066 13.44950  2.59683   1.000 83.01260  ? 34  LYS   A CD  1 
ATOM   314  C CE  . LYS   A 1 37  ? 42.77852 12.44967  3.56906   1.000 79.81779  ? 34  LYS   A CE  1 
ATOM   315  N NZ  . LYS   A 1 37  ? 43.40943 13.12448  4.73677   1.000 92.80096  ? 34  LYS   A NZ  1 
ATOM   316  N N   . ILE   A 1 38  ? 39.49983 10.90988  -0.64557  1.000 63.81616  ? 35  ILE   A N   1 
ATOM   317  C CA  . ILE   A 1 38  ? 38.56443 9.83907   -0.31908  1.000 67.80156  ? 35  ILE   A CA  1 
ATOM   318  C C   . ILE   A 1 38  ? 39.26582 8.89703   0.64866   1.000 72.70062  ? 35  ILE   A C   1 
ATOM   319  O O   . ILE   A 1 38  ? 40.17513 8.15507   0.25496   1.000 78.74670  ? 35  ILE   A O   1 
ATOM   320  C CB  . ILE   A 1 38  ? 38.08564 9.08749   -1.56811  1.000 68.42697  ? 35  ILE   A CB  1 
ATOM   321  C CG1 . ILE   A 1 38  ? 37.37496 10.04349  -2.52797  1.000 69.69832  ? 35  ILE   A CG1 1 
ATOM   322  C CG2 . ILE   A 1 38  ? 37.16724 7.93997   -1.17758  1.000 67.09059  ? 35  ILE   A CG2 1 
ATOM   323  C CD1 . ILE   A 1 38  ? 36.89628 9.38419   -3.80188  1.000 65.01935  ? 35  ILE   A CD1 1 
ATOM   324  N N   . ARG   A 1 39  ? 38.84750 8.92320   1.91175   1.000 67.14951  ? 36  ARG   A N   1 
ATOM   325  C CA  . ARG   A 1 39  ? 39.41588 8.04956   2.93313   1.000 79.48389  ? 36  ARG   A CA  1 
ATOM   326  C C   . ARG   A 1 39  ? 38.73352 6.68914   2.84682   1.000 75.29609  ? 36  ARG   A C   1 
ATOM   327  O O   . ARG   A 1 39  ? 37.56191 6.54834   3.21219   1.000 84.22408  ? 36  ARG   A O   1 
ATOM   328  C CB  . ARG   A 1 39  ? 39.25270 8.67703   4.31476   1.000 84.20119  ? 36  ARG   A CB  1 
ATOM   329  C CG  . ARG   A 1 39  ? 39.96579 10.01613  4.45619   1.000 88.38621  ? 36  ARG   A CG  1 
ATOM   330  C CD  . ARG   A 1 39  ? 39.57571 10.75506  5.72938   1.000 104.26316 ? 36  ARG   A CD  1 
ATOM   331  N NE  . ARG   A 1 39  ? 40.00379 10.05953  6.93712   1.000 109.85114 ? 36  ARG   A NE  1 
ATOM   332  C CZ  . ARG   A 1 39  ? 39.19913 9.35430   7.72016   1.000 114.03618 ? 36  ARG   A CZ  1 
ATOM   333  N NH1 . ARG   A 1 39  ? 37.90959 9.22901   7.45214   1.000 112.03810 ? 36  ARG   A NH1 1 
ATOM   334  N NH2 . ARG   A 1 39  ? 39.70004 8.76307   8.80113   1.000 105.42933 ? 36  ARG   A NH2 1 
ATOM   335  N N   . LEU   A 1 40  ? 39.46639 5.68497   2.36017   1.000 81.08360  ? 37  LEU   A N   1 
ATOM   336  C CA  . LEU   A 1 40  ? 38.88500 4.37213   2.10650   1.000 86.73145  ? 37  LEU   A CA  1 
ATOM   337  C C   . LEU   A 1 40  ? 38.66085 3.56124   3.37563   1.000 82.27451  ? 37  LEU   A C   1 
ATOM   338  O O   . LEU   A 1 40  ? 37.88529 2.59954   3.34810   1.000 78.86634  ? 37  LEU   A O   1 
ATOM   339  C CB  . LEU   A 1 40  ? 39.77630 3.57984   1.14761   1.000 80.19904  ? 37  LEU   A CB  1 
ATOM   340  C CG  . LEU   A 1 40  ? 40.06340 4.23025   -0.20672  1.000 68.02658  ? 37  LEU   A CG  1 
ATOM   341  C CD1 . LEU   A 1 40  ? 41.03027 3.37839   -1.01327  1.000 76.21266  ? 37  LEU   A CD1 1 
ATOM   342  C CD2 . LEU   A 1 40  ? 38.77294 4.45809   -0.97763  1.000 60.95373  ? 37  LEU   A CD2 1 
ATOM   343  N N   . ASP   A 1 41  ? 39.31899 3.91870   4.48053   1.000 80.93184  ? 38  ASP   A N   1 
ATOM   344  C CA  . ASP   A 1 41  ? 39.13196 3.17363   5.72120   1.000 84.75677  ? 38  ASP   A CA  1 
ATOM   345  C C   . ASP   A 1 41  ? 37.71778 3.32930   6.26769   1.000 77.23444  ? 38  ASP   A C   1 
ATOM   346  O O   . ASP   A 1 41  ? 37.23426 2.44959   6.98940   1.000 79.21604  ? 38  ASP   A O   1 
ATOM   347  C CB  . ASP   A 1 41  ? 40.16097 3.62018   6.75994   1.000 96.73150  ? 38  ASP   A CB  1 
ATOM   348  C CG  . ASP   A 1 41  ? 40.41997 5.11398   6.71901   1.000 99.07252  ? 38  ASP   A CG  1 
ATOM   349  O OD1 . ASP   A 1 41  ? 40.43730 5.68524   5.60810   1.000 98.74407  ? 38  ASP   A OD1 1 
ATOM   350  O OD2 . ASP   A 1 41  ? 40.60737 5.71749   7.79612   1.000 107.12427 ? 38  ASP   A OD2 1 
ATOM   351  N N   . THR   A 1 42  ? 37.04149 4.42768   5.93477   1.000 74.03453  ? 39  THR   A N   1 
ATOM   352  C CA  . THR   A 1 42  ? 35.67364 4.66271   6.37637   1.000 81.13341  ? 39  THR   A CA  1 
ATOM   353  C C   . THR   A 1 42  ? 34.63489 4.12366   5.40002   1.000 88.33713  ? 39  THR   A C   1 
ATOM   354  O O   . THR   A 1 42  ? 33.44195 4.12141   5.72391   1.000 78.34926  ? 39  THR   A O   1 
ATOM   355  C CB  . THR   A 1 42  ? 35.44062 6.16414   6.59082   1.000 96.21633  ? 39  THR   A CB  1 
ATOM   356  O OG1 . THR   A 1 42  ? 36.66209 6.78075   7.01629   1.000 100.22153 ? 39  THR   A OG1 1 
ATOM   357  C CG2 . THR   A 1 42  ? 34.37738 6.39719   7.65651   1.000 90.05341  ? 39  THR   A CG2 1 
ATOM   358  N N   . GLU   A 1 43  ? 35.05414 3.66296   4.22420   1.000 79.06544  ? 40  GLU   A N   1 
ATOM   359  C CA  . GLU   A 1 43  ? 34.14218 3.16136   3.19848   1.000 69.56207  ? 40  GLU   A CA  1 
ATOM   360  C C   . GLU   A 1 43  ? 34.10724 1.63948   3.28966   1.000 79.83212  ? 40  GLU   A C   1 
ATOM   361  O O   . GLU   A 1 43  ? 35.04810 0.95887   2.87266   1.000 83.15052  ? 40  GLU   A O   1 
ATOM   362  C CB  . GLU   A 1 43  ? 34.57969 3.63023   1.81533   1.000 74.36398  ? 40  GLU   A CB  1 
ATOM   363  C CG  . GLU   A 1 43  ? 34.74329 5.13689   1.69351   1.000 71.77363  ? 40  GLU   A CG  1 
ATOM   364  C CD  . GLU   A 1 43  ? 33.43935 5.88531   1.89052   1.000 86.49542  ? 40  GLU   A CD  1 
ATOM   365  O OE1 . GLU   A 1 43  ? 32.37139 5.31831   1.57625   1.000 84.35176  ? 40  GLU   A OE1 1 
ATOM   366  O OE2 . GLU   A 1 43  ? 33.48257 7.04105   2.36291   1.000 87.82407  ? 40  GLU   A OE2 1 
ATOM   367  N N   . THR   A 1 44  ? 33.01059 1.10592   3.83405   1.000 75.86800  ? 41  THR   A N   1 
ATOM   368  C CA  . THR   A 1 44  ? 32.89177 -0.34002  3.99058   1.000 86.54231  ? 41  THR   A CA  1 
ATOM   369  C C   . THR   A 1 44  ? 32.67799 -1.03984  2.65466   1.000 83.99228  ? 41  THR   A C   1 
ATOM   370  O O   . THR   A 1 44  ? 33.01150 -2.22237  2.51695   1.000 73.63119  ? 41  THR   A O   1 
ATOM   371  C CB  . THR   A 1 44  ? 31.74876 -0.67496  4.94822   1.000 89.67166  ? 41  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 44  ? 30.54029 -0.05622  4.48848   1.000 96.22490  ? 41  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 44  ? 32.06874 -0.17903  6.34863   1.000 91.53381  ? 41  THR   A CG2 1 
ATOM   374  N N   . GLU   A 1 45  ? 32.12528 -0.33730  1.66657   1.000 69.20253  ? 42  GLU   A N   1 
ATOM   375  C CA  . GLU   A 1 45  ? 31.89757 -0.89742  0.34265   1.000 68.48110  ? 42  GLU   A CA  1 
ATOM   376  C C   . GLU   A 1 45  ? 33.02749 -0.58027  -0.62927  1.000 69.40873  ? 42  GLU   A C   1 
ATOM   377  O O   . GLU   A 1 45  ? 32.80848 -0.59123  -1.84610  1.000 77.34712  ? 42  GLU   A O   1 
ATOM   378  C CB  . GLU   A 1 45  ? 30.56399 -0.39817  -0.21813  1.000 66.58523  ? 42  GLU   A CB  1 
ATOM   379  C CG  . GLU   A 1 45  ? 29.36276 -0.75296  0.64225   1.000 92.18756  ? 42  GLU   A CG  1 
ATOM   380  C CD  . GLU   A 1 45  ? 29.18266 -2.25015  0.80217   1.000 96.65753  ? 42  GLU   A CD  1 
ATOM   381  O OE1 . GLU   A 1 45  ? 29.42323 -2.98786  -0.17646  1.000 86.52339  ? 42  GLU   A OE1 1 
ATOM   382  O OE2 . GLU   A 1 45  ? 28.80769 -2.69012  1.90962   1.000 94.80985  ? 42  GLU   A OE2 1 
ATOM   383  N N   . GLY   A 1 46  ? 34.22657 -0.30029  -0.12121  1.000 66.66219  ? 43  GLY   A N   1 
ATOM   384  C CA  . GLY   A 1 46  ? 35.33466 0.02852   -0.99417  1.000 72.01619  ? 43  GLY   A CA  1 
ATOM   385  C C   . GLY   A 1 46  ? 35.16390 1.39641   -1.63216  1.000 65.92066  ? 43  GLY   A C   1 
ATOM   386  O O   . GLY   A 1 46  ? 34.57504 2.31694   -1.05795  1.000 73.52315  ? 43  GLY   A O   1 
ATOM   387  N N   . VAL   A 1 47  ? 35.69128 1.52662   -2.84488  1.000 60.67931  ? 44  VAL   A N   1 
ATOM   388  C CA  . VAL   A 1 47  ? 35.57571 2.79972   -3.56279  1.000 58.05679  ? 44  VAL   A CA  1 
ATOM   389  C C   . VAL   A 1 47  ? 34.10449 3.08519   -3.83711  1.000 59.66065  ? 44  VAL   A C   1 
ATOM   390  O O   . VAL   A 1 47  ? 33.39406 2.21199   -4.37445  1.000 59.82639  ? 44  VAL   A O   1 
ATOM   391  C CB  . VAL   A 1 47  ? 36.38315 2.75721   -4.87003  1.000 54.53145  ? 44  VAL   A CB  1 
ATOM   392  C CG1 . VAL   A 1 47  ? 36.40590 4.12890   -5.52376  1.000 58.76727  ? 44  VAL   A CG1 1 
ATOM   393  C CG2 . VAL   A 1 47  ? 37.79462 2.27027   -4.59684  1.000 57.20968  ? 44  VAL   A CG2 1 
ATOM   394  N N   . PRO   A 1 48  ? 33.59223 4.26251   -3.47826  1.000 55.62003  ? 45  PRO   A N   1 
ATOM   395  C CA  . PRO   A 1 48  ? 32.16478 4.53842   -3.67441  1.000 49.96445  ? 45  PRO   A CA  1 
ATOM   396  C C   . PRO   A 1 48  ? 31.77289 4.45423   -5.14128  1.000 54.54274  ? 45  PRO   A C   1 
ATOM   397  O O   . PRO   A 1 48  ? 32.56844 4.74128   -6.03838  1.000 57.13600  ? 45  PRO   A O   1 
ATOM   398  C CB  . PRO   A 1 48  ? 32.00162 5.96384   -3.13303  1.000 57.16858  ? 45  PRO   A CB  1 
ATOM   399  C CG  . PRO   A 1 48  ? 33.14598 6.14065   -2.18665  1.000 65.33426  ? 45  PRO   A CG  1 
ATOM   400  C CD  . PRO   A 1 48  ? 34.27947 5.36176   -2.78044  1.000 63.92896  ? 45  PRO   A CD  1 
ATOM   401  N N   . SER   A 1 49  ? 30.52364 4.04265   -5.37468  1.000 55.88105  ? 46  SER   A N   1 
ATOM   402  C CA  . SER   A 1 49  ? 30.02880 3.90933   -6.74105  1.000 52.42030  ? 46  SER   A CA  1 
ATOM   403  C C   . SER   A 1 49  ? 30.06537 5.24379   -7.47314  1.000 59.17342  ? 46  SER   A C   1 
ATOM   404  O O   . SER   A 1 49  ? 30.39356 5.29855   -8.66439  1.000 53.46076  ? 46  SER   A O   1 
ATOM   405  C CB  . SER   A 1 49  ? 28.61016 3.34135   -6.73070  1.000 59.59235  ? 46  SER   A CB  1 
ATOM   406  O OG  . SER   A 1 49  ? 27.71846 4.21302   -6.05857  1.000 74.99962  ? 46  SER   A OG  1 
ATOM   407  N N   . THR   A 1 50  ? 29.73354 6.33286   -6.77488  1.000 50.40182  ? 47  THR   A N   1 
ATOM   408  C CA  . THR   A 1 50  ? 29.80865 7.65471   -7.38752  1.000 53.38216  ? 47  THR   A CA  1 
ATOM   409  C C   . THR   A 1 50  ? 31.24065 8.02564   -7.74549  1.000 51.42332  ? 47  THR   A C   1 
ATOM   410  O O   . THR   A 1 50  ? 31.46659 8.76908   -8.70680  1.000 49.61346  ? 47  THR   A O   1 
ATOM   411  C CB  . THR   A 1 50  ? 29.21317 8.70664   -6.45212  1.000 61.25528  ? 47  THR   A CB  1 
ATOM   412  O OG1 . THR   A 1 50  ? 29.91876 8.68994   -5.20441  1.000 53.47304  ? 47  THR   A OG1 1 
ATOM   413  C CG2 . THR   A 1 50  ? 27.73982 8.42378   -6.20285  1.000 56.35336  ? 47  THR   A CG2 1 
ATOM   414  N N   . ALA   A 1 51  ? 32.21782 7.52509   -6.98727  1.000 43.54529  ? 48  ALA   A N   1 
ATOM   415  C CA  . ALA   A 1 51  ? 33.61231 7.80241   -7.31248  1.000 47.71786  ? 48  ALA   A CA  1 
ATOM   416  C C   . ALA   A 1 51  ? 34.06838 6.99154   -8.51860  1.000 50.64717  ? 48  ALA   A C   1 
ATOM   417  O O   . ALA   A 1 51  ? 34.75023 7.51919   -9.40537  1.000 50.83457  ? 48  ALA   A O   1 
ATOM   418  C CB  . ALA   A 1 51  ? 34.50204 7.51845   -6.10309  1.000 47.39944  ? 48  ALA   A CB  1 
ATOM   419  N N   . ILE   A 1 52  ? 33.69813 5.70936   -8.57328  1.000 51.69253  ? 49  ILE   A N   1 
ATOM   420  C CA  . ILE   A 1 52  ? 34.06114 4.88292   -9.72196  1.000 56.92222  ? 49  ILE   A CA  1 
ATOM   421  C C   . ILE   A 1 52  ? 33.40275 5.41447   -10.98887 1.000 47.19705  ? 49  ILE   A C   1 
ATOM   422  O O   . ILE   A 1 52  ? 34.01246 5.42677   -12.06556 1.000 53.52697  ? 49  ILE   A O   1 
ATOM   423  C CB  . ILE   A 1 52  ? 33.68789 3.41067   -9.46667  1.000 50.45951  ? 49  ILE   A CB  1 
ATOM   424  C CG1 . ILE   A 1 52  ? 34.25682 2.93421   -8.13041  1.000 58.09378  ? 49  ILE   A CG1 1 
ATOM   425  C CG2 . ILE   A 1 52  ? 34.21042 2.52930   -10.58425 1.000 56.86600  ? 49  ILE   A CG2 1 
ATOM   426  C CD1 . ILE   A 1 52  ? 33.97701 1.47537   -7.83206  1.000 53.00551  ? 49  ILE   A CD1 1 
ATOM   427  N N   . ARG   A 1 53  ? 32.15039 5.86569   -10.88151 1.000 57.44765  ? 50  ARG   A N   1 
ATOM   428  C CA  . ARG   A 1 53  ? 31.45600 6.41514   -12.04263 1.000 54.58088  ? 50  ARG   A CA  1 
ATOM   429  C C   . ARG   A 1 53  ? 32.12270 7.69588   -12.52753 1.000 47.57634  ? 50  ARG   A C   1 
ATOM   430  O O   . ARG   A 1 53  ? 32.38597 7.85717   -13.72403 1.000 48.91891  ? 50  ARG   A O   1 
ATOM   431  C CB  . ARG   A 1 53  ? 29.98696 6.67975   -11.70807 1.000 59.97418  ? 50  ARG   A CB  1 
ATOM   432  C CG  . ARG   A 1 53  ? 29.09765 5.44792   -11.67975 1.000 71.21377  ? 50  ARG   A CG  1 
ATOM   433  C CD  . ARG   A 1 53  ? 27.64899 5.84580   -11.43151 1.000 71.40297  ? 50  ARG   A CD  1 
ATOM   434  N NE  . ARG   A 1 53  ? 26.75065 4.69893   -11.37224 1.000 63.15917  ? 50  ARG   A NE  1 
ATOM   435  C CZ  . ARG   A 1 53  ? 25.44591 4.78476   -11.14887 1.000 81.29861  ? 50  ARG   A CZ  1 
ATOM   436  N NH1 . ARG   A 1 53  ? 24.85250 5.95245   -10.95913 1.000 60.67190  ? 50  ARG   A NH1 1 
ATOM   437  N NH2 . ARG   A 1 53  ? 24.71813 3.67175   -11.11423 1.000 63.69743  ? 50  ARG   A NH2 1 
ATOM   438  N N   . GLU   A 1 54  ? 32.40170 8.62332   -11.60742 1.000 42.51193  ? 51  GLU   A N   1 
ATOM   439  C CA  . GLU   A 1 54  ? 32.94605 9.91751   -12.00746 1.000 49.34558  ? 51  GLU   A CA  1 
ATOM   440  C C   . GLU   A 1 54  ? 34.32736 9.77373   -12.63384 1.000 44.83492  ? 51  GLU   A C   1 
ATOM   441  O O   . GLU   A 1 54  ? 34.64527 10.45750  -13.61339 1.000 49.96699  ? 51  GLU   A O   1 
ATOM   442  C CB  . GLU   A 1 54  ? 33.00040 10.86264  -10.80767 1.000 49.79111  ? 51  GLU   A CB  1 
ATOM   443  C CG  . GLU   A 1 54  ? 33.53117 12.24478  -11.14997 1.000 59.53920  ? 51  GLU   A CG  1 
ATOM   444  C CD  . GLU   A 1 54  ? 33.41649 13.22342  -9.99953  1.000 63.65754  ? 51  GLU   A CD  1 
ATOM   445  O OE1 . GLU   A 1 54  ? 33.30830 12.77409  -8.83997  1.000 70.64707  ? 51  GLU   A OE1 1 
ATOM   446  O OE2 . GLU   A 1 54  ? 33.42857 14.44565  -10.25907 1.000 64.53521  ? 51  GLU   A OE2 1 
ATOM   447  N N   . ILE   A 1 55  ? 35.16272 8.89150   -12.08410 1.000 49.47249  ? 52  ILE   A N   1 
ATOM   448  C CA  . ILE   A 1 55  ? 36.51365 8.72232   -12.61141 1.000 48.82344  ? 52  ILE   A CA  1 
ATOM   449  C C   . ILE   A 1 55  ? 36.46808 8.16296   -14.02850 1.000 54.42793  ? 52  ILE   A C   1 
ATOM   450  O O   . ILE   A 1 55  ? 37.10547 8.69623   -14.94395 1.000 50.65826  ? 52  ILE   A O   1 
ATOM   451  C CB  . ILE   A 1 55  ? 37.34783 7.82758   -11.67706 1.000 54.10699  ? 52  ILE   A CB  1 
ATOM   452  C CG1 . ILE   A 1 55  ? 37.60015 8.53319   -10.34401 1.000 43.91128  ? 52  ILE   A CG1 1 
ATOM   453  C CG2 . ILE   A 1 55  ? 38.66477 7.45665   -12.33362 1.000 61.02695  ? 52  ILE   A CG2 1 
ATOM   454  C CD1 . ILE   A 1 55  ? 38.30794 7.66952   -9.32109  1.000 50.41252  ? 52  ILE   A CD1 1 
ATOM   455  N N   . SER   A 1 56  ? 35.70673 7.08510   -14.23259 1.000 49.80658  ? 53  SER   A N   1 
ATOM   456  C CA  . SER   A 1 56  ? 35.65760 6.45350   -15.54776 1.000 53.90351  ? 53  SER   A CA  1 
ATOM   457  C C   . SER   A 1 56  ? 35.03389 7.37745   -16.58744 1.000 51.29895  ? 53  SER   A C   1 
ATOM   458  O O   . SER   A 1 56  ? 35.46360 7.39449   -17.74656 1.000 60.95903  ? 53  SER   A O   1 
ATOM   459  C CB  . SER   A 1 56  ? 34.88572 5.13679   -15.46879 1.000 57.17954  ? 53  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 56  ? 33.55095 5.35622   -15.04574 1.000 68.84262  ? 53  SER   A OG  1 
ATOM   461  N N   . LEU   A 1 57  ? 34.02286 8.15613   -16.19430 1.000 49.49654  ? 54  LEU   A N   1 
ATOM   462  C CA  . LEU   A 1 57  ? 33.38319 9.06098   -17.14492 1.000 49.18090  ? 54  LEU   A CA  1 
ATOM   463  C C   . LEU   A 1 57  ? 34.30100 10.21981  -17.51602 1.000 50.03060  ? 54  LEU   A C   1 
ATOM   464  O O   . LEU   A 1 57  ? 34.40497 10.58208  -18.69345 1.000 51.63485  ? 54  LEU   A O   1 
ATOM   465  C CB  . LEU   A 1 57  ? 32.06579 9.58426   -16.57165 1.000 46.28351  ? 54  LEU   A CB  1 
ATOM   466  C CG  . LEU   A 1 57  ? 30.91518 8.58310   -16.45531 1.000 50.80732  ? 54  LEU   A CG  1 
ATOM   467  C CD1 . LEU   A 1 57  ? 29.71654 9.22267   -15.77010 1.000 54.00619  ? 54  LEU   A CD1 1 
ATOM   468  C CD2 . LEU   A 1 57  ? 30.52913 8.04280   -17.82264 1.000 49.87254  ? 54  LEU   A CD2 1 
ATOM   469  N N   . LEU   A 1 58  ? 34.98221 10.80887  -16.52945 1.000 52.56110  ? 55  LEU   A N   1 
ATOM   470  C CA  . LEU   A 1 58  ? 35.78846 11.99473  -16.80194 1.000 50.72796  ? 55  LEU   A CA  1 
ATOM   471  C C   . LEU   A 1 58  ? 37.05838 11.66194  -17.57580 1.000 56.46943  ? 55  LEU   A C   1 
ATOM   472  O O   . LEU   A 1 58  ? 37.55756 12.50605  -18.32859 1.000 63.90299  ? 55  LEU   A O   1 
ATOM   473  C CB  . LEU   A 1 58  ? 36.13059 12.71164  -15.49629 1.000 41.35372  ? 55  LEU   A CB  1 
ATOM   474  C CG  . LEU   A 1 58  ? 34.96010 13.44897  -14.84122 1.000 48.79699  ? 55  LEU   A CG  1 
ATOM   475  C CD1 . LEU   A 1 58  ? 35.42696 14.23119  -13.62510 1.000 55.37231  ? 55  LEU   A CD1 1 
ATOM   476  C CD2 . LEU   A 1 58  ? 34.27827 14.36516  -15.84748 1.000 56.58672  ? 55  LEU   A CD2 1 
ATOM   477  N N   . LYS   A 1 59  ? 37.59711 10.45136  -17.41176 1.000 54.77864  ? 56  LYS   A N   1 
ATOM   478  C CA  . LYS   A 1 59  ? 38.77600 10.06581  -18.17865 1.000 58.87241  ? 56  LYS   A CA  1 
ATOM   479  C C   . LYS   A 1 59  ? 38.46878 9.85633   -19.65445 1.000 68.17931  ? 56  LYS   A C   1 
ATOM   480  O O   . LYS   A 1 59  ? 39.39646 9.62598   -20.43636 1.000 68.69469  ? 56  LYS   A O   1 
ATOM   481  C CB  . LYS   A 1 59  ? 39.40684 8.80135   -17.58935 1.000 73.21162  ? 56  LYS   A CB  1 
ATOM   482  C CG  . LYS   A 1 59  ? 39.98120 8.99667   -16.19481 1.000 66.84447  ? 56  LYS   A CG  1 
ATOM   483  C CD  . LYS   A 1 59  ? 40.79259 7.79374   -15.74293 1.000 79.62945  ? 56  LYS   A CD  1 
ATOM   484  C CE  . LYS   A 1 59  ? 42.24349 7.90503   -16.18262 1.000 97.20533  ? 56  LYS   A CE  1 
ATOM   485  N NZ  . LYS   A 1 59  ? 42.93220 9.05029   -15.52484 1.000 77.84397  ? 56  LYS   A NZ  1 
ATOM   486  N N   . GLU   A 1 60  ? 37.19838 9.92972   -20.04899 1.000 61.59061  ? 57  GLU   A N   1 
ATOM   487  C CA  . GLU   A 1 60  ? 36.80109 9.86293   -21.44828 1.000 69.71458  ? 57  GLU   A CA  1 
ATOM   488  C C   . GLU   A 1 60  ? 36.00811 11.09017  -21.87622 1.000 60.59700  ? 57  GLU   A C   1 
ATOM   489  O O   . GLU   A 1 60  ? 35.51654 11.13384  -23.01000 1.000 68.34825  ? 57  GLU   A O   1 
ATOM   490  C CB  . GLU   A 1 60  ? 35.99113 8.58908   -21.70912 1.000 73.81189  ? 57  GLU   A CB  1 
ATOM   491  C CG  . GLU   A 1 60  ? 36.77159 7.30429   -21.47272 1.000 78.94752  ? 57  GLU   A CG  1 
ATOM   492  C CD  . GLU   A 1 60  ? 35.94390 6.06165   -21.73809 1.000 87.64471  ? 57  GLU   A CD  1 
ATOM   493  O OE1 . GLU   A 1 60  ? 34.71095 6.18937   -21.89187 1.000 91.33349  ? 57  GLU   A OE1 1 
ATOM   494  O OE2 . GLU   A 1 60  ? 36.52421 4.95754   -21.79398 1.000 90.84206  ? 57  GLU   A OE2 1 
ATOM   495  N N   . LEU   A 1 61  ? 35.86895 12.07981  -21.00077 1.000 54.12598  ? 58  LEU   A N   1 
ATOM   496  C CA  . LEU   A 1 61  ? 35.16602 13.32562  -21.29419 1.000 51.99226  ? 58  LEU   A CA  1 
ATOM   497  C C   . LEU   A 1 61  ? 36.16581 14.47670  -21.21563 1.000 64.91870  ? 58  LEU   A C   1 
ATOM   498  O O   . LEU   A 1 61  ? 36.09928 15.31617  -20.31282 1.000 66.74670  ? 58  LEU   A O   1 
ATOM   499  C CB  . LEU   A 1 61  ? 33.99016 13.53680  -20.32717 1.000 56.78439  ? 58  LEU   A CB  1 
ATOM   500  C CG  . LEU   A 1 61  ? 32.75487 12.65378  -20.51406 1.000 53.12549  ? 58  LEU   A CG  1 
ATOM   501  C CD1 . LEU   A 1 61  ? 31.68560 13.01394  -19.49306 1.000 45.12114  ? 58  LEU   A CD1 1 
ATOM   502  C CD2 . LEU   A 1 61  ? 32.21466 12.77439  -21.93010 1.000 49.94163  ? 58  LEU   A CD2 1 
ATOM   503  N N   . ASN   A 1 62  ? 37.09795 14.51104  -22.16392 1.000 58.13265  ? 59  ASN   A N   1 
ATOM   504  C CA  . ASN   A 1 62  ? 38.09409 15.57456  -22.24035 1.000 60.85636  ? 59  ASN   A CA  1 
ATOM   505  C C   . ASN   A 1 62  ? 37.54812 16.67441  -23.14447 1.000 53.42383  ? 59  ASN   A C   1 
ATOM   506  O O   . ASN   A 1 62  ? 37.42614 16.48583  -24.35884 1.000 60.62714  ? 59  ASN   A O   1 
ATOM   507  C CB  . ASN   A 1 62  ? 39.42332 15.03401  -22.76211 1.000 64.44342  ? 59  ASN   A CB  1 
ATOM   508  C CG  . ASN   A 1 62  ? 40.61902 15.76678  -22.18312 1.000 79.34613  ? 59  ASN   A CG  1 
ATOM   509  O OD1 . ASN   A 1 62  ? 41.55273 15.14738  -21.67292 1.000 101.99145 ? 59  ASN   A OD1 1 
ATOM   510  N ND2 . ASN   A 1 62  ? 40.59305 17.09265  -22.25314 1.000 87.00671  ? 59  ASN   A ND2 1 
ATOM   511  N N   . HIS   A 1 63  ? 37.21653 17.81983  -22.55372 1.000 55.47562  ? 60  HIS   A N   1 
ATOM   512  C CA  . HIS   A 1 63  ? 36.60068 18.92273  -23.27683 1.000 55.56490  ? 60  HIS   A CA  1 
ATOM   513  C C   . HIS   A 1 63  ? 36.97178 20.22413  -22.58538 1.000 52.06889  ? 60  HIS   A C   1 
ATOM   514  O O   . HIS   A 1 63  ? 37.10369 20.25193  -21.35587 1.000 51.77397  ? 60  HIS   A O   1 
ATOM   515  C CB  . HIS   A 1 63  ? 35.07265 18.76766  -23.33576 1.000 48.52029  ? 60  HIS   A CB  1 
ATOM   516  C CG  . HIS   A 1 63  ? 34.40109 19.72909  -24.26571 1.000 47.68617  ? 60  HIS   A CG  1 
ATOM   517  N ND1 . HIS   A 1 63  ? 33.92487 20.95486  -23.85311 1.000 50.80159  ? 60  HIS   A ND1 1 
ATOM   518  C CD2 . HIS   A 1 63  ? 34.13235 19.64762  -25.59049 1.000 51.15094  ? 60  HIS   A CD2 1 
ATOM   519  C CE1 . HIS   A 1 63  ? 33.38912 21.58581  -24.88296 1.000 56.68630  ? 60  HIS   A CE1 1 
ATOM   520  N NE2 . HIS   A 1 63  ? 33.50192 20.81424  -25.94917 1.000 49.55054  ? 60  HIS   A NE2 1 
ATOM   521  N N   . PRO   A 1 64  ? 37.15223 21.31304  -23.33976 1.000 55.88774  ? 61  PRO   A N   1 
ATOM   522  C CA  . PRO   A 1 64  ? 37.52415 22.59209  -22.70998 1.000 50.29264  ? 61  PRO   A CA  1 
ATOM   523  C C   . PRO   A 1 64  ? 36.50368 23.11897  -21.71706 1.000 62.47592  ? 61  PRO   A C   1 
ATOM   524  O O   . PRO   A 1 64  ? 36.87949 23.89012  -20.82737 1.000 50.71262  ? 61  PRO   A O   1 
ATOM   525  C CB  . PRO   A 1 64  ? 37.67437 23.54114  -23.90665 1.000 63.44448  ? 61  PRO   A CB  1 
ATOM   526  C CG  . PRO   A 1 64  ? 37.98445 22.64423  -25.05958 1.000 59.08726  ? 61  PRO   A CG  1 
ATOM   527  C CD  . PRO   A 1 64  ? 37.21410 21.38174  -24.80993 1.000 52.85361  ? 61  PRO   A CD  1 
ATOM   528  N N   . ASN   A 1 65  ? 35.23094 22.74157  -21.83280 1.000 53.90825  ? 62  ASN   A N   1 
ATOM   529  C CA  . ASN   A 1 65  ? 34.20158 23.21141  -20.91529 1.000 51.44123  ? 62  ASN   A CA  1 
ATOM   530  C C   . ASN   A 1 65  ? 33.80469 22.15273  -19.89218 1.000 48.73281  ? 62  ASN   A C   1 
ATOM   531  O O   . ASN   A 1 65  ? 32.69256 22.19949  -19.35554 1.000 46.68781  ? 62  ASN   A O   1 
ATOM   532  C CB  . ASN   A 1 65  ? 32.97847 23.69081  -21.69646 1.000 44.65501  ? 62  ASN   A CB  1 
ATOM   533  C CG  . ASN   A 1 65  ? 33.30133 24.84965  -22.62263 1.000 63.72932  ? 62  ASN   A CG  1 
ATOM   534  O OD1 . ASN   A 1 65  ? 33.22681 24.72229  -23.84303 1.000 51.73535  ? 62  ASN   A OD1 1 
ATOM   535  N ND2 . ASN   A 1 65  ? 33.66683 25.98831  -22.04274 1.000 49.60878  ? 62  ASN   A ND2 1 
ATOM   536  N N   . ILE   A 1 66  ? 34.69115 21.20069  -19.61457 1.000 51.23261  ? 63  ILE   A N   1 
ATOM   537  C CA  . ILE   A 1 66  ? 34.48863 20.19566  -18.57890 1.000 51.65682  ? 63  ILE   A CA  1 
ATOM   538  C C   . ILE   A 1 66  ? 35.72841 20.18119  -17.69690 1.000 46.21591  ? 63  ILE   A C   1 
ATOM   539  O O   . ILE   A 1 66  ? 36.85127 20.07966  -18.20416 1.000 50.29546  ? 63  ILE   A O   1 
ATOM   540  C CB  . ILE   A 1 66  ? 34.22925 18.79861  -19.17562 1.000 50.87912  ? 63  ILE   A CB  1 
ATOM   541  C CG1 . ILE   A 1 66  ? 32.98785 18.82102  -20.07022 1.000 45.07009  ? 63  ILE   A CG1 1 
ATOM   542  C CG2 . ILE   A 1 66  ? 34.07834 17.76536  -18.07045 1.000 48.19229  ? 63  ILE   A CG2 1 
ATOM   543  C CD1 . ILE   A 1 66  ? 32.67062 17.48739  -20.70971 1.000 55.47669  ? 63  ILE   A CD1 1 
ATOM   544  N N   . VAL   A 1 67  ? 35.52741 20.29578  -16.38096 1.000 42.13457  ? 64  VAL   A N   1 
ATOM   545  C CA  . VAL   A 1 67  ? 36.65558 20.30874  -15.45622 1.000 46.23857  ? 64  VAL   A CA  1 
ATOM   546  C C   . VAL   A 1 67  ? 37.41500 18.99689  -15.57143 1.000 50.03563  ? 64  VAL   A C   1 
ATOM   547  O O   . VAL   A 1 67  ? 36.83982 17.91003  -15.43286 1.000 53.06671  ? 64  VAL   A O   1 
ATOM   548  C CB  . VAL   A 1 67  ? 36.17235 20.55900  -14.02028 1.000 51.94007  ? 64  VAL   A CB  1 
ATOM   549  C CG1 . VAL   A 1 67  ? 37.35412 20.58558  -13.05955 1.000 52.00089  ? 64  VAL   A CG1 1 
ATOM   550  C CG2 . VAL   A 1 67  ? 35.39723 21.86285  -13.94622 1.000 46.19830  ? 64  VAL   A CG2 1 
ATOM   551  N N   . LYS   A 1 68  ? 38.71559 19.09479  -15.83178 1.000 48.62484  ? 65  LYS   A N   1 
ATOM   552  C CA  . LYS   A 1 68  ? 39.51977 17.92336  -16.14566 1.000 57.98419  ? 65  LYS   A CA  1 
ATOM   553  C C   . LYS   A 1 68  ? 39.91155 17.15711  -14.88998 1.000 54.60972  ? 65  LYS   A C   1 
ATOM   554  O O   . LYS   A 1 68  ? 40.30121 17.74522  -13.87695 1.000 56.97008  ? 65  LYS   A O   1 
ATOM   555  C CB  . LYS   A 1 68  ? 40.78277 18.32996  -16.90552 1.000 62.05542  ? 65  LYS   A CB  1 
ATOM   556  C CG  . LYS   A 1 68  ? 40.55094 18.74418  -18.34592 1.000 67.53125  ? 65  LYS   A CG  1 
ATOM   557  C CD  . LYS   A 1 68  ? 41.87289 18.88240  -19.08350 1.000 74.38315  ? 65  LYS   A CD  1 
ATOM   558  C CE  . LYS   A 1 68  ? 42.68000 17.59456  -19.00181 1.000 83.12819  ? 65  LYS   A CE  1 
ATOM   559  N NZ  . LYS   A 1 68  ? 44.01405 17.72147  -19.65188 1.000 104.84097 ? 65  LYS   A NZ  1 
ATOM   560  N N   . LEU   A 1 69  ? 39.80944 15.83290  -14.96955 1.000 54.67284  ? 66  LEU   A N   1 
ATOM   561  C CA  . LEU   A 1 69  ? 40.39185 14.93875  -13.97574 1.000 60.04888  ? 66  LEU   A CA  1 
ATOM   562  C C   . LEU   A 1 69  ? 41.83107 14.66152  -14.39387 1.000 62.70645  ? 66  LEU   A C   1 
ATOM   563  O O   . LEU   A 1 69  ? 42.07350 14.01548  -15.41855 1.000 66.73182  ? 66  LEU   A O   1 
ATOM   564  C CB  . LEU   A 1 69  ? 39.58681 13.64719  -13.86707 1.000 55.12549  ? 66  LEU   A CB  1 
ATOM   565  C CG  . LEU   A 1 69  ? 40.20095 12.54040  -13.00819 1.000 61.17141  ? 66  LEU   A CG  1 
ATOM   566  C CD1 . LEU   A 1 69  ? 40.34313 12.99448  -11.56455 1.000 53.13321  ? 66  LEU   A CD1 1 
ATOM   567  C CD2 . LEU   A 1 69  ? 39.36841 11.27128  -13.09825 1.000 60.02742  ? 66  LEU   A CD2 1 
ATOM   568  N N   . LEU   A 1 70  ? 42.78697 15.15709  -13.60713 1.000 60.91348  ? 67  LEU   A N   1 
ATOM   569  C CA  . LEU   A 1 70  ? 44.18570 15.08186  -14.01394 1.000 61.53589  ? 67  LEU   A CA  1 
ATOM   570  C C   . LEU   A 1 70  ? 44.81564 13.74202  -13.65221 1.000 64.35105  ? 67  LEU   A C   1 
ATOM   571  O O   . LEU   A 1 70  ? 45.54388 13.16033  -14.46394 1.000 72.72073  ? 67  LEU   A O   1 
ATOM   572  C CB  . LEU   A 1 70  ? 44.97437 16.23202  -13.38698 1.000 67.99070  ? 67  LEU   A CB  1 
ATOM   573  C CG  . LEU   A 1 70  ? 44.53060 17.63356  -13.81256 1.000 63.53510  ? 67  LEU   A CG  1 
ATOM   574  C CD1 . LEU   A 1 70  ? 45.39286 18.70052  -13.15617 1.000 68.48250  ? 67  LEU   A CD1 1 
ATOM   575  C CD2 . LEU   A 1 70  ? 44.56285 17.76825  -15.32826 1.000 71.63055  ? 67  LEU   A CD2 1 
ATOM   576  N N   . ASP   A 1 71  ? 44.55099 13.23483  -12.45083 1.000 67.41662  ? 68  ASP   A N   1 
ATOM   577  C CA  . ASP   A 1 71  ? 45.18281 11.99973  -12.00930 1.000 70.06863  ? 68  ASP   A CA  1 
ATOM   578  C C   . ASP   A 1 71  ? 44.34960 11.38050  -10.89706 1.000 59.88151  ? 68  ASP   A C   1 
ATOM   579  O O   . ASP   A 1 71  ? 43.54199 12.05292  -10.25037 1.000 64.17100  ? 68  ASP   A O   1 
ATOM   580  C CB  . ASP   A 1 71  ? 46.61979 12.25051  -11.53441 1.000 76.49120  ? 68  ASP   A CB  1 
ATOM   581  C CG  . ASP   A 1 71  ? 47.43417 10.97517  -11.43058 1.000 81.49014  ? 68  ASP   A CG  1 
ATOM   582  O OD1 . ASP   A 1 71  ? 46.91637 9.90234   -11.80575 1.000 92.87079  ? 68  ASP   A OD1 1 
ATOM   583  O OD2 . ASP   A 1 71  ? 48.59441 11.04715  -10.97400 1.000 84.06903  ? 68  ASP   A OD2 1 
ATOM   584  N N   . VAL   A 1 72  ? 44.55466 10.08120  -10.69211 1.000 64.80310  ? 69  VAL   A N   1 
ATOM   585  C CA  . VAL   A 1 72  ? 43.93827 9.32999   -9.60336  1.000 61.93233  ? 69  VAL   A CA  1 
ATOM   586  C C   . VAL   A 1 72  ? 45.06360 8.61675   -8.86759  1.000 67.86653  ? 69  VAL   A C   1 
ATOM   587  O O   . VAL   A 1 72  ? 45.64430 7.65931   -9.39401  1.000 77.50669  ? 69  VAL   A O   1 
ATOM   588  C CB  . VAL   A 1 72  ? 42.88837 8.32706   -10.10207 1.000 65.40239  ? 69  VAL   A CB  1 
ATOM   589  C CG1 . VAL   A 1 72  ? 42.29118 7.56121   -8.93122  1.000 60.58968  ? 69  VAL   A CG1 1 
ATOM   590  C CG2 . VAL   A 1 72  ? 41.79885 9.04142   -10.88893 1.000 56.27932  ? 69  VAL   A CG2 1 
ATOM   591  N N   . ILE   A 1 73  ? 45.37506 9.07812   -7.65888  1.000 66.92744  ? 70  ILE   A N   1 
ATOM   592  C CA  . ILE   A 1 73  ? 46.50290 8.57642   -6.88270  1.000 67.01418  ? 70  ILE   A CA  1 
ATOM   593  C C   . ILE   A 1 73  ? 45.96884 7.78674   -5.69672  1.000 67.85381  ? 70  ILE   A C   1 
ATOM   594  O O   . ILE   A 1 73  ? 45.12044 8.28015   -4.94334  1.000 70.71111  ? 70  ILE   A O   1 
ATOM   595  C CB  . ILE   A 1 73  ? 47.41615 9.72244   -6.41439  1.000 71.18952  ? 70  ILE   A CB  1 
ATOM   596  C CG1 . ILE   A 1 73  ? 47.87114 10.56124  -7.61021  1.000 74.85088  ? 70  ILE   A CG1 1 
ATOM   597  C CG2 . ILE   A 1 73  ? 48.61752 9.17337   -5.66134  1.000 72.30648  ? 70  ILE   A CG2 1 
ATOM   598  C CD1 . ILE   A 1 73  ? 48.76218 11.72497  -7.23616  1.000 87.64314  ? 70  ILE   A CD1 1 
ATOM   599  N N   . HIS   A 1 74  ? 46.46797 6.56493   -5.53142  1.000 64.28733  ? 71  HIS   A N   1 
ATOM   600  C CA  . HIS   A 1 74  ? 46.10998 5.69569   -4.41324  1.000 78.89704  ? 71  HIS   A CA  1 
ATOM   601  C C   . HIS   A 1 74  ? 47.29529 5.66413   -3.45329  1.000 78.98054  ? 71  HIS   A C   1 
ATOM   602  O O   . HIS   A 1 74  ? 48.27443 4.94908   -3.68480  1.000 83.43141  ? 71  HIS   A O   1 
ATOM   603  C CB  . HIS   A 1 74  ? 45.74795 4.29708   -4.90401  1.000 71.33976  ? 71  HIS   A CB  1 
ATOM   604  C CG  . HIS   A 1 74  ? 45.39059 3.34417   -3.80639  1.000 66.22826  ? 71  HIS   A CG  1 
ATOM   605  N ND1 . HIS   A 1 74  ? 44.86449 3.75861   -2.60183  1.000 87.42437  ? 71  HIS   A ND1 1 
ATOM   606  C CD2 . HIS   A 1 74  ? 45.48775 1.99587   -3.73007  1.000 77.06418  ? 71  HIS   A CD2 1 
ATOM   607  C CE1 . HIS   A 1 74  ? 44.65047 2.70677   -1.83173  1.000 83.51300  ? 71  HIS   A CE1 1 
ATOM   608  N NE2 . HIS   A 1 74  ? 45.02099 1.62484   -2.49241  1.000 84.05601  ? 71  HIS   A NE2 1 
ATOM   609  N N   . THR   A 1 75  ? 47.20374 6.44242   -2.37797  1.000 86.24546  ? 72  THR   A N   1 
ATOM   610  C CA  . THR   A 1 75  ? 48.26152 6.54823   -1.38182  1.000 96.94346  ? 72  THR   A CA  1 
ATOM   611  C C   . THR   A 1 75  ? 47.70302 6.18117   -0.01503  1.000 94.87129  ? 72  THR   A C   1 
ATOM   612  O O   . THR   A 1 75  ? 46.65846 6.70266   0.39162   1.000 87.64040  ? 72  THR   A O   1 
ATOM   613  C CB  . THR   A 1 75  ? 48.85325 7.96169   -1.35229  1.000 93.36459  ? 72  THR   A CB  1 
ATOM   614  O OG1 . THR   A 1 75  ? 49.46373 8.25170   -2.61561  1.000 118.58308 ? 72  THR   A OG1 1 
ATOM   615  C CG2 . THR   A 1 75  ? 49.89829 8.08399   -0.25440  1.000 112.76573 ? 72  THR   A CG2 1 
ATOM   616  N N   . GLU   A 1 76  ? 48.39894 5.28905   0.68176   1.000 107.21908 ? 73  GLU   A N   1 
ATOM   617  C CA  . GLU   A 1 76  ? 48.00212 4.80343   2.01565   1.000 108.75152 ? 73  GLU   A CA  1 
ATOM   618  C C   . GLU   A 1 76  ? 46.61952 4.15981   1.87205   1.000 94.08446  ? 73  GLU   A C   1 
ATOM   619  O O   . GLU   A 1 76  ? 46.34891 3.49759   0.85851   1.000 103.76324 ? 73  GLU   A O   1 
ATOM   620  C CB  . GLU   A 1 76  ? 48.08285 5.93316   3.02402   1.000 109.41677 ? 73  GLU   A CB  1 
ATOM   621  C CG  . GLU   A 1 76  ? 49.43223 6.62823   3.07729   1.000 120.36688 ? 73  GLU   A CG  1 
ATOM   622  C CD  . GLU   A 1 76  ? 49.41501 7.86244   3.95758   1.000 131.21312 ? 73  GLU   A CD  1 
ATOM   623  O OE1 . GLU   A 1 76  ? 48.43154 8.04762   4.70515   1.000 130.79219 ? 73  GLU   A OE1 1 
ATOM   624  O OE2 . GLU   A 1 76  ? 50.38263 8.64995   3.89869   1.000 141.42346 ? 73  GLU   A OE2 1 
ATOM   625  N N   . ASN   A 1 77  ? 45.73166 4.32585   2.85333   1.000 89.55754  ? 74  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 77  ? 44.35277 3.86646   2.74962   1.000 93.36119  ? 74  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 77  ? 43.42826 4.94287   2.19316   1.000 86.47053  ? 74  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 77  ? 42.25864 5.02346   2.59245   1.000 79.14870  ? 74  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 77  ? 43.85850 3.38560   4.11512   1.000 104.24149 ? 74  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 77  ? 42.84555 2.26160   4.00787   1.000 112.70385 ? 74  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 77  ? 42.16962 2.11280   2.99026   1.000 99.06846  ? 74  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 77  ? 42.73661 1.46188   5.06295   1.000 116.63393 ? 74  ASN   A ND2 1 
ATOM   633  N N   . LYS   A 1 78  ? 43.92775 5.77728   1.28332   1.000 77.69075  ? 75  LYS   A N   1 
ATOM   634  C CA  . LYS   A 1 78  ? 43.18612 6.91212   0.75838   1.000 75.74418  ? 75  LYS   A CA  1 
ATOM   635  C C   . LYS   A 1 78  ? 43.25156 6.91394   -0.76281  1.000 86.42623  ? 75  LYS   A C   1 
ATOM   636  O O   . LYS   A 1 78  ? 44.12389 6.28905   -1.37210  1.000 73.32499  ? 75  LYS   A O   1 
ATOM   637  C CB  . LYS   A 1 78  ? 43.73588 8.23781   1.30460   1.000 86.17976  ? 75  LYS   A CB  1 
ATOM   638  C CG  . LYS   A 1 78  ? 43.82356 8.29879   2.82081   1.000 91.15194  ? 75  LYS   A CG  1 
ATOM   639  C CD  . LYS   A 1 78  ? 44.70557 9.44902   3.27480   1.000 99.75561  ? 75  LYS   A CD  1 
ATOM   640  C CE  . LYS   A 1 78  ? 46.11649 9.31140   2.72564   1.000 100.42505 ? 75  LYS   A CE  1 
ATOM   641  N NZ  . LYS   A 1 78  ? 46.98931 10.44206  3.14624   1.000 92.64616  ? 75  LYS   A NZ  1 
ATOM   642  N N   . LEU   A 1 79  ? 42.31195 7.63453   -1.37141  1.000 71.58344  ? 76  LEU   A N   1 
ATOM   643  C CA  . LEU   A 1 79  ? 42.25299 7.79662   -2.81895  1.000 65.83340  ? 76  LEU   A CA  1 
ATOM   644  C C   . LEU   A 1 79  ? 42.17080 9.28254   -3.12872  1.000 66.82732  ? 76  LEU   A C   1 
ATOM   645  O O   . LEU   A 1 79  ? 41.22352 9.95408   -2.70707  1.000 68.70890  ? 76  LEU   A O   1 
ATOM   646  C CB  . LEU   A 1 79  ? 41.05327 7.05189   -3.41295  1.000 64.75430  ? 76  LEU   A CB  1 
ATOM   647  C CG  . LEU   A 1 79  ? 41.01849 6.92014   -4.93624  1.000 63.89325  ? 76  LEU   A CG  1 
ATOM   648  C CD1 . LEU   A 1 79  ? 42.20606 6.10500   -5.42458  1.000 60.51344  ? 76  LEU   A CD1 1 
ATOM   649  C CD2 . LEU   A 1 79  ? 39.70715 6.29830   -5.39779  1.000 54.44561  ? 76  LEU   A CD2 1 
ATOM   650  N N   . TYR   A 1 80  ? 43.15880 9.79342   -3.85653  1.000 59.61184  ? 77  TYR   A N   1 
ATOM   651  C CA  . TYR   A 1 80  ? 43.23763 11.20692  -4.19802  1.000 63.26270  ? 77  TYR   A CA  1 
ATOM   652  C C   . TYR   A 1 80  ? 42.86175 11.40740  -5.65930  1.000 69.83888  ? 77  TYR   A C   1 
ATOM   653  O O   . TYR   A 1 80  ? 43.40163 10.73390  -6.54357  1.000 61.05416  ? 77  TYR   A O   1 
ATOM   654  C CB  . TYR   A 1 80  ? 44.64005 11.75899  -3.93138  1.000 73.90678  ? 77  TYR   A CB  1 
ATOM   655  C CG  . TYR   A 1 80  ? 44.94644 11.97268  -2.46572  1.000 83.90381  ? 77  TYR   A CG  1 
ATOM   656  C CD1 . TYR   A 1 80  ? 44.60885 13.16244  -1.83340  1.000 81.45178  ? 77  TYR   A CD1 1 
ATOM   657  C CD2 . TYR   A 1 80  ? 45.57415 10.98727  -1.71480  1.000 90.17593  ? 77  TYR   A CD2 1 
ATOM   658  C CE1 . TYR   A 1 80  ? 44.88622 13.36484  -0.49410  1.000 88.66801  ? 77  TYR   A CE1 1 
ATOM   659  C CE2 . TYR   A 1 80  ? 45.85600 11.18078  -0.37392  1.000 94.77576  ? 77  TYR   A CE2 1 
ATOM   660  C CZ  . TYR   A 1 80  ? 45.50978 12.37124  0.23078   1.000 92.42322  ? 77  TYR   A CZ  1 
ATOM   661  O OH  . TYR   A 1 80  ? 45.78783 12.56907  1.56418   1.000 101.18061 ? 77  TYR   A OH  1 
ATOM   662  N N   . LEU   A 1 81  ? 41.93820 12.33165  -5.90536  1.000 61.37974  ? 78  LEU   A N   1 
ATOM   663  C CA  . LEU   A 1 81  ? 41.50937 12.69585  -7.24983  1.000 59.85322  ? 78  LEU   A CA  1 
ATOM   664  C C   . LEU   A 1 81  ? 41.98416 14.11409  -7.53407  1.000 58.28726  ? 78  LEU   A C   1 
ATOM   665  O O   . LEU   A 1 81  ? 41.55580 15.06000  -6.86403  1.000 58.83289  ? 78  LEU   A O   1 
ATOM   666  C CB  . LEU   A 1 81  ? 39.98944 12.59509  -7.39386  1.000 62.88321  ? 78  LEU   A CB  1 
ATOM   667  C CG  . LEU   A 1 81  ? 39.34655 11.21752  -7.59079  1.000 60.64279  ? 78  LEU   A CG  1 
ATOM   668  C CD1 . LEU   A 1 81  ? 39.50407 10.33112  -6.36322  1.000 56.25221  ? 78  LEU   A CD1 1 
ATOM   669  C CD2 . LEU   A 1 81  ? 37.87602 11.37149  -7.95281  1.000 53.42694  ? 78  LEU   A CD2 1 
ATOM   670  N N   . VAL   A 1 82  ? 42.86603 14.25845  -8.51847  1.000 52.82986  ? 79  VAL   A N   1 
ATOM   671  C CA  . VAL   A 1 82  ? 43.46878 15.54276  -8.85638  1.000 52.62890  ? 79  VAL   A CA  1 
ATOM   672  C C   . VAL   A 1 82  ? 42.65985 16.17369  -9.98072  1.000 63.74579  ? 79  VAL   A C   1 
ATOM   673  O O   . VAL   A 1 82  ? 42.56303 15.61279  -11.07916 1.000 59.96315  ? 79  VAL   A O   1 
ATOM   674  C CB  . VAL   A 1 82  ? 44.94271 15.38255  -9.25880  1.000 61.77011  ? 79  VAL   A CB  1 
ATOM   675  C CG1 . VAL   A 1 82  ? 45.58605 16.74425  -9.45881  1.000 69.04125  ? 79  VAL   A CG1 1 
ATOM   676  C CG2 . VAL   A 1 82  ? 45.69316 14.57747  -8.20952  1.000 63.02711  ? 79  VAL   A CG2 1 
ATOM   677  N N   . PHE   A 1 83  ? 42.08610 17.34121  -9.71070  1.000 52.69729  ? 80  PHE   A N   1 
ATOM   678  C CA  . PHE   A 1 83  ? 41.25972 18.05924  -10.66675 1.000 55.49602  ? 80  PHE   A CA  1 
ATOM   679  C C   . PHE   A 1 83  ? 41.91944 19.37060  -11.07221 1.000 61.43257  ? 80  PHE   A C   1 
ATOM   680  O O   . PHE   A 1 83  ? 42.76270 19.92168  -10.35817 1.000 51.67247  ? 80  PHE   A O   1 
ATOM   681  C CB  . PHE   A 1 83  ? 39.87032 18.35372  -10.08789 1.000 49.76935  ? 80  PHE   A CB  1 
ATOM   682  C CG  . PHE   A 1 83  ? 38.98403 17.14813  -9.97738  1.000 50.78091  ? 80  PHE   A CG  1 
ATOM   683  C CD1 . PHE   A 1 83  ? 38.19760 16.75259  -11.04563 1.000 59.47706  ? 80  PHE   A CD1 1 
ATOM   684  C CD2 . PHE   A 1 83  ? 38.92221 16.42121  -8.80004  1.000 60.24599  ? 80  PHE   A CD2 1 
ATOM   685  C CE1 . PHE   A 1 83  ? 37.37405 15.64650  -10.94645 1.000 54.94189  ? 80  PHE   A CE1 1 
ATOM   686  C CE2 . PHE   A 1 83  ? 38.10106 15.31551  -8.69429  1.000 58.55800  ? 80  PHE   A CE2 1 
ATOM   687  C CZ  . PHE   A 1 83  ? 37.32620 14.92750  -9.76914  1.000 52.72315  ? 80  PHE   A CZ  1 
ATOM   688  N N   . GLU   A 1 84  ? 41.51857 19.85954  -12.24296 1.000 59.21778  ? 81  GLU   A N   1 
ATOM   689  C CA  . GLU   A 1 84  ? 41.82515 21.22642  -12.63770 1.000 51.58198  ? 81  GLU   A CA  1 
ATOM   690  C C   . GLU   A 1 84  ? 41.15613 22.20135  -11.67468 1.000 60.21786  ? 81  GLU   A C   1 
ATOM   691  O O   . GLU   A 1 84  ? 40.03213 21.97303  -11.21863 1.000 54.46025  ? 81  GLU   A O   1 
ATOM   692  C CB  . GLU   A 1 84  ? 41.34294 21.46695  -14.06967 1.000 51.79556  ? 81  GLU   A CB  1 
ATOM   693  C CG  . GLU   A 1 84  ? 41.33523 22.91490  -14.51881 1.000 72.35370  ? 81  GLU   A CG  1 
ATOM   694  C CD  . GLU   A 1 84  ? 40.55898 23.11087  -15.80672 1.000 65.24468  ? 81  GLU   A CD  1 
ATOM   695  O OE1 . GLU   A 1 84  ? 39.88252 22.15522  -16.24511 1.000 61.36334  ? 81  GLU   A OE1 1 
ATOM   696  O OE2 . GLU   A 1 84  ? 40.62295 24.21803  -16.38079 1.000 76.78512  ? 81  GLU   A OE2 1 
ATOM   697  N N   . PHE   A 1 85  ? 41.85176 23.29040  -11.35692 1.000 57.35074  ? 82  PHE   A N   1 
ATOM   698  C CA  . PHE   A 1 85  ? 41.37170 24.25815  -10.37856 1.000 51.95157  ? 82  PHE   A CA  1 
ATOM   699  C C   . PHE   A 1 85  ? 40.76692 25.47252  -11.07185 1.000 53.02851  ? 82  PHE   A C   1 
ATOM   700  O O   . PHE   A 1 85  ? 41.36356 26.02858  -12.00016 1.000 60.88438  ? 82  PHE   A O   1 
ATOM   701  C CB  . PHE   A 1 85  ? 42.49767 24.70364  -9.44364  1.000 57.19463  ? 82  PHE   A CB  1 
ATOM   702  C CG  . PHE   A 1 85  ? 42.08101 25.76709  -8.46515  1.000 52.64544  ? 82  PHE   A CG  1 
ATOM   703  C CD1 . PHE   A 1 85  ? 41.35395 25.43803  -7.33303  1.000 52.68593  ? 82  PHE   A CD1 1 
ATOM   704  C CD2 . PHE   A 1 85  ? 42.40777 27.09628  -8.68224  1.000 61.76477  ? 82  PHE   A CD2 1 
ATOM   705  C CE1 . PHE   A 1 85  ? 40.96312 26.41363  -6.43321  1.000 58.43860  ? 82  PHE   A CE1 1 
ATOM   706  C CE2 . PHE   A 1 85  ? 42.01988 28.07637  -7.78546  1.000 53.75254  ? 82  PHE   A CE2 1 
ATOM   707  C CZ  . PHE   A 1 85  ? 41.29683 27.73428  -6.66085  1.000 47.82723  ? 82  PHE   A CZ  1 
ATOM   708  N N   . LEU   A 1 86  ? 39.58584 25.87983  -10.60929 1.000 52.02696  ? 83  LEU   A N   1 
ATOM   709  C CA  . LEU   A 1 86  ? 38.93826 27.11652  -11.02187 1.000 49.48476  ? 83  LEU   A CA  1 
ATOM   710  C C   . LEU   A 1 86  ? 38.54763 27.88904  -9.76937  1.000 51.16322  ? 83  LEU   A C   1 
ATOM   711  O O   . LEU   A 1 86  ? 38.15959 27.29280  -8.76025  1.000 45.74673  ? 83  LEU   A O   1 
ATOM   712  C CB  . LEU   A 1 86  ? 37.70987 26.84920  -11.90630 1.000 56.53346  ? 83  LEU   A CB  1 
ATOM   713  C CG  . LEU   A 1 86  ? 37.98330 26.24740  -13.29189 1.000 65.60691  ? 83  LEU   A CG  1 
ATOM   714  C CD1 . LEU   A 1 86  ? 38.05072 24.72459  -13.24218 1.000 50.29917  ? 83  LEU   A CD1 1 
ATOM   715  C CD2 . LEU   A 1 86  ? 36.94547 26.71025  -14.30563 1.000 47.93347  ? 83  LEU   A CD2 1 
ATOM   716  N N   . HIS   A 1 87  ? 38.64851 29.21832  -9.83823  1.000 53.71749  ? 84  HIS   A N   1 
ATOM   717  C CA  . HIS   A 1 87  ? 38.66326 30.03239  -8.62717  1.000 57.76617  ? 84  HIS   A CA  1 
ATOM   718  C C   . HIS   A 1 87  ? 37.28230 30.28171  -8.03120  1.000 55.36413  ? 84  HIS   A C   1 
ATOM   719  O O   . HIS   A 1 87  ? 37.19844 30.70123  -6.87176  1.000 58.31672  ? 84  HIS   A O   1 
ATOM   720  C CB  . HIS   A 1 87  ? 39.34354 31.37646  -8.90697  1.000 51.87800  ? 84  HIS   A CB  1 
ATOM   721  C CG  . HIS   A 1 87  ? 38.47627 32.35627  -9.63457  1.000 62.25037  ? 84  HIS   A CG  1 
ATOM   722  N ND1 . HIS   A 1 87  ? 37.97736 32.11695  -10.89680 1.000 67.19636  ? 84  HIS   A ND1 1 
ATOM   723  C CD2 . HIS   A 1 87  ? 38.02530 33.58246  -9.27857  1.000 66.31555  ? 84  HIS   A CD2 1 
ATOM   724  C CE1 . HIS   A 1 87  ? 37.25261 33.15109  -11.28522 1.000 61.93952  ? 84  HIS   A CE1 1 
ATOM   725  N NE2 . HIS   A 1 87  ? 37.26610 34.05436  -10.32169 1.000 71.22658  ? 84  HIS   A NE2 1 
ATOM   726  N N   . GLN   A 1 88  ? 36.20470 30.03628  -8.77340  1.000 50.42234  ? 85  GLN   A N   1 
ATOM   727  C CA  . GLN   A 1 88  ? 34.88360 30.39950  -8.27909  1.000 51.80834  ? 85  GLN   A CA  1 
ATOM   728  C C   . GLN   A 1 88  ? 33.82256 29.61675  -9.03877  1.000 56.91917  ? 85  GLN   A C   1 
ATOM   729  O O   . GLN   A 1 88  ? 34.03380 29.21200  -10.18544 1.000 49.86171  ? 85  GLN   A O   1 
ATOM   730  C CB  . GLN   A 1 88  ? 34.64311 31.90838  -8.42435  1.000 59.55193  ? 85  GLN   A CB  1 
ATOM   731  C CG  . GLN   A 1 88  ? 33.47169 32.44839  -7.62279  1.000 62.13851  ? 85  GLN   A CG  1 
ATOM   732  C CD  . GLN   A 1 88  ? 33.28180 33.94140  -7.80944  1.000 65.16189  ? 85  GLN   A CD  1 
ATOM   733  O OE1 . GLN   A 1 88  ? 32.87375 34.64844  -6.88711  1.000 91.73386  ? 85  GLN   A OE1 1 
ATOM   734  N NE2 . GLN   A 1 88  ? 33.57647 34.42884  -9.00849  1.000 55.60507  ? 85  GLN   A NE2 1 
ATOM   735  N N   . ASP   A 1 89  ? 32.68310 29.40589  -8.38540  1.000 46.38226  ? 86  ASP   A N   1 
ATOM   736  C CA  . ASP   A 1 89  ? 31.52267 28.80951  -9.02781  1.000 52.26390  ? 86  ASP   A CA  1 
ATOM   737  C C   . ASP   A 1 89  ? 30.56431 29.90180  -9.49189  1.000 48.63613  ? 86  ASP   A C   1 
ATOM   738  O O   . ASP   A 1 89  ? 30.68126 31.07029  -9.11583  1.000 48.37191  ? 86  ASP   A O   1 
ATOM   739  C CB  . ASP   A 1 89  ? 30.81849 27.81909  -8.08885  1.000 45.49173  ? 86  ASP   A CB  1 
ATOM   740  C CG  . ASP   A 1 89  ? 30.28271 28.46969  -6.81940  1.000 53.39203  ? 86  ASP   A CG  1 
ATOM   741  O OD1 . ASP   A 1 89  ? 30.42808 29.69726  -6.64411  1.000 80.55539  ? 86  ASP   A OD1 1 
ATOM   742  O OD2 . ASP   A 1 89  ? 29.71053 27.73667  -5.98515  1.000 62.21246  ? 86  ASP   A OD2 1 
ATOM   743  N N   . LEU   A 1 90  ? 29.60086 29.50268  -10.32393 1.000 47.19047  ? 87  LEU   A N   1 
ATOM   744  C CA  . LEU   A 1 90  ? 28.69121 30.48047  -10.91011 1.000 53.84775  ? 87  LEU   A CA  1 
ATOM   745  C C   . LEU   A 1 90  ? 27.78438 31.11610  -9.86277  1.000 46.05537  ? 87  LEU   A C   1 
ATOM   746  O O   . LEU   A 1 90  ? 27.43455 32.29436  -9.98865  1.000 49.20823  ? 87  LEU   A O   1 
ATOM   747  C CB  . LEU   A 1 90  ? 27.85516 29.82830  -12.01176 1.000 44.45225  ? 87  LEU   A CB  1 
ATOM   748  C CG  . LEU   A 1 90  ? 26.93490 30.76520  -12.79728 1.000 42.97627  ? 87  LEU   A CG  1 
ATOM   749  C CD1 . LEU   A 1 90  ? 27.73276 31.89646  -13.42930 1.000 50.17371  ? 87  LEU   A CD1 1 
ATOM   750  C CD2 . LEU   A 1 90  ? 26.16011 29.99241  -13.85290 1.000 42.50926  ? 87  LEU   A CD2 1 
ATOM   751  N N   . LYS   A 1 91  ? 27.40289 30.36832  -8.82328  1.000 45.21102  ? 88  LYS   A N   1 
ATOM   752  C CA  . LYS   A 1 91  ? 26.47801 30.91287  -7.83212  1.000 39.73200  ? 88  LYS   A CA  1 
ATOM   753  C C   . LYS   A 1 91  ? 27.08646 32.10325  -7.10042  1.000 48.25858  ? 88  LYS   A C   1 
ATOM   754  O O   . LYS   A 1 91  ? 26.41244 33.11773  -6.88460  1.000 51.79973  ? 88  LYS   A O   1 
ATOM   755  C CB  . LYS   A 1 91  ? 26.06194 29.82822  -6.83948  1.000 48.94052  ? 88  LYS   A CB  1 
ATOM   756  C CG  . LYS   A 1 91  ? 24.80022 30.17780  -6.05841  1.000 50.99614  ? 88  LYS   A CG  1 
ATOM   757  C CD  . LYS   A 1 91  ? 25.05975 30.28234  -4.56533  1.000 67.64904  ? 88  LYS   A CD  1 
ATOM   758  C CE  . LYS   A 1 91  ? 25.09800 28.91177  -3.91136  1.000 86.70048  ? 88  LYS   A CE  1 
ATOM   759  N NZ  . LYS   A 1 91  ? 25.25345 29.00400  -2.43405  1.000 75.80271  ? 88  LYS   A NZ  1 
ATOM   760  N N   . LYS   A 1 92  ? 28.36053 32.00010  -6.71197  1.000 45.72823  ? 89  LYS   A N   1 
ATOM   761  C CA  . LYS   A 1 92  ? 29.03538 33.13654  -6.09156  1.000 52.92625  ? 89  LYS   A CA  1 
ATOM   762  C C   . LYS   A 1 92  ? 29.15081 34.30524  -7.06097  1.000 56.25717  ? 89  LYS   A C   1 
ATOM   763  O O   . LYS   A 1 92  ? 29.03524 35.46918  -6.65959  1.000 49.88937  ? 89  LYS   A O   1 
ATOM   764  C CB  . LYS   A 1 92  ? 30.42125 32.72593  -5.59533  1.000 57.97557  ? 89  LYS   A CB  1 
ATOM   765  C CG  . LYS   A 1 92  ? 30.44057 32.06133  -4.23183  1.000 70.77828  ? 89  LYS   A CG  1 
ATOM   766  C CD  . LYS   A 1 92  ? 31.87074 31.77411  -3.80154  1.000 87.80983  ? 89  LYS   A CD  1 
ATOM   767  C CE  . LYS   A 1 92  ? 32.73871 33.01996  -3.91320  1.000 83.04127  ? 89  LYS   A CE  1 
ATOM   768  N NZ  . LYS   A 1 92  ? 34.17413 32.73013  -3.64228  1.000 96.38702  ? 89  LYS   A NZ  1 
ATOM   769  N N   . PHE   A 1 93  ? 29.38460 34.01466  -8.34260  1.000 51.29512  ? 90  PHE   A N   1 
ATOM   770  C CA  . PHE   A 1 93  ? 29.50870 35.08031  -9.33075  1.000 49.28666  ? 90  PHE   A CA  1 
ATOM   771  C C   . PHE   A 1 93  ? 28.17397 35.77904  -9.55733  1.000 49.87924  ? 90  PHE   A C   1 
ATOM   772  O O   . PHE   A 1 93  ? 28.12737 37.00549  -9.70622  1.000 53.79062  ? 90  PHE   A O   1 
ATOM   773  C CB  . PHE   A 1 93  ? 30.05698 34.51375  -10.64046 1.000 53.12389  ? 90  PHE   A CB  1 
ATOM   774  C CG  . PHE   A 1 93  ? 30.23150 35.54083  -11.72170 1.000 49.21174  ? 90  PHE   A CG  1 
ATOM   775  C CD1 . PHE   A 1 93  ? 31.27812 36.44686  -11.67217 1.000 57.47617  ? 90  PHE   A CD1 1 
ATOM   776  C CD2 . PHE   A 1 93  ? 29.35546 35.59380  -12.79355 1.000 51.59549  ? 90  PHE   A CD2 1 
ATOM   777  C CE1 . PHE   A 1 93  ? 31.44358 37.39242  -12.66769 1.000 53.67915  ? 90  PHE   A CE1 1 
ATOM   778  C CE2 . PHE   A 1 93  ? 29.51572 36.53593  -13.79208 1.000 61.45815  ? 90  PHE   A CE2 1 
ATOM   779  C CZ  . PHE   A 1 93  ? 30.56095 37.43651  -13.72850 1.000 55.83492  ? 90  PHE   A CZ  1 
ATOM   780  N N   . MET   A 1 94  ? 27.07766 35.01659  -9.58330  1.000 49.22172  ? 91  MET   A N   1 
ATOM   781  C CA  . MET   A 1 94  ? 25.75838 35.62519  -9.72337  1.000 53.63537  ? 91  MET   A CA  1 
ATOM   782  C C   . MET   A 1 94  ? 25.41179 36.47301  -8.50571  1.000 48.25323  ? 91  MET   A C   1 
ATOM   783  O O   . MET   A 1 94  ? 24.86969 37.57561  -8.64437  1.000 53.45364  ? 91  MET   A O   1 
ATOM   784  C CB  . MET   A 1 94  ? 24.70090 34.54371  -9.93936  1.000 48.13164  ? 91  MET   A CB  1 
ATOM   785  C CG  . MET   A 1 94  ? 24.94196 33.67840  -11.16212 1.000 53.33944  ? 91  MET   A CG  1 
ATOM   786  S SD  . MET   A 1 94  ? 24.06883 32.10454  -11.06097 1.000 71.95716  ? 91  MET   A SD  1 
ATOM   787  C CE  . MET   A 1 94  ? 22.68859 32.43528  -12.14144 1.000 62.69240  ? 91  MET   A CE  1 
ATOM   788  N N   . ASP   A 1 95  ? 25.71795 35.97647  -7.30427  1.000 47.89755  ? 92  ASP   A N   1 
ATOM   789  C CA  . ASP   A 1 95  ? 25.44339 36.74832  -6.09619  1.000 54.95536  ? 92  ASP   A CA  1 
ATOM   790  C C   . ASP   A 1 95  ? 26.30110 38.00579  -6.03779  1.000 50.89003  ? 92  ASP   A C   1 
ATOM   791  O O   . ASP   A 1 95  ? 25.81948 39.07366  -5.64304  1.000 53.31065  ? 92  ASP   A O   1 
ATOM   792  C CB  . ASP   A 1 95  ? 25.67112 35.88497  -4.85625  1.000 56.48718  ? 92  ASP   A CB  1 
ATOM   793  C CG  . ASP   A 1 95  ? 24.68741 34.73477  -4.75716  1.000 62.81891  ? 92  ASP   A CG  1 
ATOM   794  O OD1 . ASP   A 1 95  ? 23.75243 34.67475  -5.58306  1.000 69.32832  ? 92  ASP   A OD1 1 
ATOM   795  O OD2 . ASP   A 1 95  ? 24.85159 33.88856  -3.85305  1.000 64.55355  ? 92  ASP   A OD2 1 
ATOM   796  N N   . ALA   A 1 96  ? 27.57372 37.90106  -6.42810  1.000 52.54632  ? 93  ALA   A N   1 
ATOM   797  C CA  . ALA   A 1 96  ? 28.43052 39.08085  -6.45931  1.000 57.81356  ? 93  ALA   A CA  1 
ATOM   798  C C   . ALA   A 1 96  ? 27.96882 40.07728  -7.51332  1.000 51.78334  ? 93  ALA   A C   1 
ATOM   799  O O   . ALA   A 1 96  ? 28.17519 41.28646  -7.35739  1.000 59.59602  ? 93  ALA   A O   1 
ATOM   800  C CB  . ALA   A 1 96  ? 29.88143 38.67194  -6.71109  1.000 54.93658  ? 93  ALA   A CB  1 
ATOM   801  N N   . SER   A 1 97  ? 27.34191 39.59401  -8.58368  1.000 57.01649  ? 94  SER   A N   1 
ATOM   802  C CA  . SER   A 1 97  ? 26.83612 40.44157  -9.65279  1.000 49.01413  ? 94  SER   A CA  1 
ATOM   803  C C   . SER   A 1 97  ? 25.35901 40.77751  -9.48733  1.000 65.84671  ? 94  SER   A C   1 
ATOM   804  O O   . SER   A 1 97  ? 24.74226 41.27744  -10.43187 1.000 58.65005  ? 94  SER   A O   1 
ATOM   805  C CB  . SER   A 1 97  ? 27.05957 39.76392  -11.00900 1.000 52.15615  ? 94  SER   A CB  1 
ATOM   806  O OG  . SER   A 1 97  ? 28.37762 39.25402  -11.12165 1.000 59.63441  ? 94  SER   A OG  1 
ATOM   807  N N   . ALA   A 1 98  ? 24.78184 40.52358  -8.31062  1.000 56.88820  ? 95  ALA   A N   1 
ATOM   808  C CA  . ALA   A 1 98  ? 23.33721 40.66232  -8.15026  1.000 65.06305  ? 95  ALA   A CA  1 
ATOM   809  C C   . ALA   A 1 98  ? 22.88992 42.11297  -8.28354  1.000 61.85198  ? 95  ALA   A C   1 
ATOM   810  O O   . ALA   A 1 98  ? 21.80597 42.38592  -8.81167  1.000 62.10374  ? 95  ALA   A O   1 
ATOM   811  C CB  . ALA   A 1 98  ? 22.90174 40.09167  -6.80215  1.000 59.55719  ? 95  ALA   A CB  1 
ATOM   812  N N   . LEU   A 1 99  ? 23.70319 43.05717  -7.81014  1.000 60.73082  ? 96  LEU   A N   1 
ATOM   813  C CA  . LEU   A 1 99  ? 23.30853 44.46013  -7.87058  1.000 68.69510  ? 96  LEU   A CA  1 
ATOM   814  C C   . LEU   A 1 99  ? 23.52540 45.03959  -9.26337  1.000 74.38988  ? 96  LEU   A C   1 
ATOM   815  O O   . LEU   A 1 99  ? 22.63155 45.68513  -9.82158  1.000 73.88323  ? 96  LEU   A O   1 
ATOM   816  C CB  . LEU   A 1 99  ? 24.07891 45.26942  -6.82633  1.000 65.75827  ? 96  LEU   A CB  1 
ATOM   817  C CG  . LEU   A 1 99  ? 23.88534 44.85517  -5.36660  1.000 74.39676  ? 96  LEU   A CG  1 
ATOM   818  C CD1 . LEU   A 1 99  ? 24.61251 45.81762  -4.44362  1.000 72.09122  ? 96  LEU   A CD1 1 
ATOM   819  C CD2 . LEU   A 1 99  ? 22.40726 44.77942  -5.01378  1.000 71.99194  ? 96  LEU   A CD2 1 
ATOM   820  N N   . THR   A 1 100 ? 24.70702 44.81621  -9.84018  1.000 75.51013  ? 97  THR   A N   1 
ATOM   821  C CA  . THR   A 1 100 ? 25.01571 45.37914  -11.14925 1.000 81.43718  ? 97  THR   A CA  1 
ATOM   822  C C   . THR   A 1 100 ? 24.43573 44.54889  -12.28707 1.000 75.06039  ? 97  THR   A C   1 
ATOM   823  O O   . THR   A 1 100 ? 24.14810 45.09274  -13.35908 1.000 72.73018  ? 97  THR   A O   1 
ATOM   824  C CB  . THR   A 1 100 ? 26.53000 45.50796  -11.32233 1.000 87.49044  ? 97  THR   A CB  1 
ATOM   825  O OG1 . THR   A 1 100 ? 27.13362 44.21097  -11.23496 1.000 85.19271  ? 97  THR   A OG1 1 
ATOM   826  C CG2 . THR   A 1 100 ? 27.11386 46.40574  -10.24114 1.000 83.35533  ? 97  THR   A CG2 1 
ATOM   827  N N   . GLY   A 1 101 ? 24.25628 43.24730  -12.08000 1.000 74.85368  ? 98  GLY   A N   1 
ATOM   828  C CA  . GLY   A 1 101 ? 23.77104 42.37969  -13.13441 1.000 62.63904  ? 98  GLY   A CA  1 
ATOM   829  C C   . GLY   A 1 101 ? 24.88636 41.89231  -14.03423 1.000 66.17221  ? 98  GLY   A C   1 
ATOM   830  O O   . GLY   A 1 101 ? 25.77808 42.66475  -14.39738 1.000 74.47633  ? 98  GLY   A O   1 
ATOM   831  N N   . ILE   A 1 102 ? 24.85839 40.61519  -14.38941 1.000 69.36865  ? 99  ILE   A N   1 
ATOM   832  C CA  . ILE   A 1 102 ? 25.85650 40.08659  -15.32550 1.000 60.78321  ? 99  ILE   A CA  1 
ATOM   833  C C   . ILE   A 1 102 ? 25.60745 40.68814  -16.70376 1.000 60.66965  ? 99  ILE   A C   1 
ATOM   834  O O   . ILE   A 1 102 ? 24.45560 40.68891  -17.17479 1.000 61.85414  ? 99  ILE   A O   1 
ATOM   835  C CB  . ILE   A 1 102 ? 25.79003 38.55901  -15.37053 1.000 65.51481  ? 99  ILE   A CB  1 
ATOM   836  C CG1 . ILE   A 1 102 ? 25.90633 37.97755  -13.96020 1.000 66.74966  ? 99  ILE   A CG1 1 
ATOM   837  C CG2 . ILE   A 1 102 ? 26.89338 38.00402  -16.25978 1.000 59.70812  ? 99  ILE   A CG2 1 
ATOM   838  C CD1 . ILE   A 1 102 ? 25.81072 36.46778  -13.91223 1.000 56.58194  ? 99  ILE   A CD1 1 
ATOM   839  N N   . PRO   A 1 103 ? 26.62706 41.22537  -17.37381 1.000 66.81480  ? 100 PRO   A N   1 
ATOM   840  C CA  . PRO   A 1 103 ? 26.40919 41.79872  -18.70710 1.000 62.37579  ? 100 PRO   A CA  1 
ATOM   841  C C   . PRO   A 1 103 ? 25.88273 40.75260  -19.67856 1.000 54.57025  ? 100 PRO   A C   1 
ATOM   842  O O   . PRO   A 1 103 ? 26.26973 39.58330  -19.63039 1.000 58.58048  ? 100 PRO   A O   1 
ATOM   843  C CB  . PRO   A 1 103 ? 27.80165 42.29592  -19.11214 1.000 71.14810  ? 100 PRO   A CB  1 
ATOM   844  C CG  . PRO   A 1 103 ? 28.52796 42.48489  -17.82062 1.000 63.08939  ? 100 PRO   A CG  1 
ATOM   845  C CD  . PRO   A 1 103 ? 28.01168 41.41280  -16.90930 1.000 56.83565  ? 100 PRO   A CD  1 
ATOM   846  N N   . LEU   A 1 104 ? 24.98195 41.18882  -20.55926 1.000 67.40430  ? 101 LEU   A N   1 
ATOM   847  C CA  . LEU   A 1 104 ? 24.37672 40.26823  -21.51837 1.000 63.12429  ? 101 LEU   A CA  1 
ATOM   848  C C   . LEU   A 1 104 ? 25.39481 39.52668  -22.37958 1.000 66.93996  ? 101 LEU   A C   1 
ATOM   849  O O   . LEU   A 1 104 ? 25.20925 38.31429  -22.58727 1.000 57.28956  ? 101 LEU   A O   1 
ATOM   850  C CB  . LEU   A 1 104 ? 23.36724 41.02246  -22.39499 1.000 69.07962  ? 101 LEU   A CB  1 
ATOM   851  C CG  . LEU   A 1 104 ? 22.67679 40.20096  -23.48681 1.000 84.47203  ? 101 LEU   A CG  1 
ATOM   852  C CD1 . LEU   A 1 104 ? 21.92653 39.02133  -22.88424 1.000 72.70430  ? 101 LEU   A CD1 1 
ATOM   853  C CD2 . LEU   A 1 104 ? 21.74045 41.07242  -24.31036 1.000 89.16366  ? 101 LEU   A CD2 1 
ATOM   854  N N   . PRO   A 1 105 ? 26.45417 40.15409  -22.90937 1.000 62.98743  ? 102 PRO   A N   1 
ATOM   855  C CA  . PRO   A 1 105 ? 27.44990 39.36660  -23.65601 1.000 67.49864  ? 102 PRO   A CA  1 
ATOM   856  C C   . PRO   A 1 105 ? 28.10361 38.27607  -22.82737 1.000 61.97638  ? 102 PRO   A C   1 
ATOM   857  O O   . PRO   A 1 105 ? 28.45497 37.22378  -23.37504 1.000 60.65833  ? 102 PRO   A O   1 
ATOM   858  C CB  . PRO   A 1 105 ? 28.46945 40.42377  -24.10298 1.000 70.64449  ? 102 PRO   A CB  1 
ATOM   859  C CG  . PRO   A 1 105 ? 27.69798 41.68452  -24.15033 1.000 64.85849  ? 102 PRO   A CG  1 
ATOM   860  C CD  . PRO   A 1 105 ? 26.73261 41.59954  -23.00694 1.000 55.57715  ? 102 PRO   A CD  1 
ATOM   861  N N   . LEU   A 1 106 ? 28.27794 38.48914  -21.52138 1.000 56.99877  ? 103 LEU   A N   1 
ATOM   862  C CA  . LEU   A 1 106 ? 28.86695 37.44716  -20.68636 1.000 57.06111  ? 103 LEU   A CA  1 
ATOM   863  C C   . LEU   A 1 106 ? 27.86615 36.33163  -20.40981 1.000 58.61355  ? 103 LEU   A C   1 
ATOM   864  O O   . LEU   A 1 106 ? 28.24541 35.15716  -20.32747 1.000 56.10751  ? 103 LEU   A O   1 
ATOM   865  C CB  . LEU   A 1 106 ? 29.38593 38.04644  -19.38020 1.000 52.51468  ? 103 LEU   A CB  1 
ATOM   866  C CG  . LEU   A 1 106 ? 30.15948 37.09035  -18.47081 1.000 58.37776  ? 103 LEU   A CG  1 
ATOM   867  C CD1 . LEU   A 1 106 ? 31.28434 36.41418  -19.24008 1.000 64.49388  ? 103 LEU   A CD1 1 
ATOM   868  C CD2 . LEU   A 1 106 ? 30.70792 37.82942  -17.26349 1.000 62.43883  ? 103 LEU   A CD2 1 
ATOM   869  N N   . ILE   A 1 107 ? 26.58541 36.67939  -20.26144 1.000 58.38243  ? 104 ILE   A N   1 
ATOM   870  C CA  . ILE   A 1 107 ? 25.54515 35.66227  -20.12287 1.000 61.20408  ? 104 ILE   A CA  1 
ATOM   871  C C   . ILE   A 1 107 ? 25.48640 34.79621  -21.37442 1.000 50.97635  ? 104 ILE   A C   1 
ATOM   872  O O   . ILE   A 1 107 ? 25.41553 33.56339  -21.29980 1.000 48.39565  ? 104 ILE   A O   1 
ATOM   873  C CB  . ILE   A 1 107 ? 24.18461 36.32175  -19.83332 1.000 55.47350  ? 104 ILE   A CB  1 
ATOM   874  C CG1 . ILE   A 1 107 ? 24.19258 36.98915  -18.45669 1.000 65.85088  ? 104 ILE   A CG1 1 
ATOM   875  C CG2 . ILE   A 1 107 ? 23.06153 35.30092  -19.93223 1.000 50.63986  ? 104 ILE   A CG2 1 
ATOM   876  C CD1 . ILE   A 1 107 ? 22.88028 37.64544  -18.09052 1.000 62.21297  ? 104 ILE   A CD1 1 
ATOM   877  N N   . LYS   A 1 108 ? 25.51671 35.43368  -22.54620 1.000 49.76924  ? 105 LYS   A N   1 
ATOM   878  C CA  . LYS   A 1 108 ? 25.48103 34.68767  -23.79868 1.000 60.97509  ? 105 LYS   A CA  1 
ATOM   879  C C   . LYS   A 1 108 ? 26.71940 33.81297  -23.95373 1.000 51.51696  ? 105 LYS   A C   1 
ATOM   880  O O   . LYS   A 1 108 ? 26.62199 32.65653  -24.38015 1.000 57.24300  ? 105 LYS   A O   1 
ATOM   881  C CB  . LYS   A 1 108 ? 25.34800 35.65673  -24.97405 1.000 51.93689  ? 105 LYS   A CB  1 
ATOM   882  C CG  . LYS   A 1 108 ? 25.11274 34.98949  -26.31487 1.000 64.99035  ? 105 LYS   A CG  1 
ATOM   883  C CD  . LYS   A 1 108 ? 24.92591 36.02573  -27.41373 1.000 72.79176  ? 105 LYS   A CD  1 
ATOM   884  C CE  . LYS   A 1 108 ? 23.76280 36.95590  -27.10816 1.000 75.35935  ? 105 LYS   A CE  1 
ATOM   885  N NZ  . LYS   A 1 108 ? 23.51622 37.92509  -28.21210 1.000 87.61933  ? 105 LYS   A NZ  1 
ATOM   886  N N   . SER   A 1 109 ? 27.89387 34.34569  -23.60669 1.000 51.23422  ? 106 SER   A N   1 
ATOM   887  C CA  . SER   A 1 109 ? 29.11861 33.55661  -23.69871 1.000 51.38863  ? 106 SER   A CA  1 
ATOM   888  C C   . SER   A 1 109 ? 29.07746 32.35652  -22.76064 1.000 55.25368  ? 106 SER   A C   1 
ATOM   889  O O   . SER   A 1 109 ? 29.46692 31.24729  -23.14393 1.000 49.44370  ? 106 SER   A O   1 
ATOM   890  C CB  . SER   A 1 109 ? 30.33493 34.43010  -23.39097 1.000 56.87994  ? 106 SER   A CB  1 
ATOM   891  O OG  . SER   A 1 109 ? 31.50627 33.63792  -23.27871 1.000 60.81950  ? 106 SER   A OG  1 
ATOM   892  N N   . TYR   A 1 110 ? 28.60793 32.55693  -21.52693 1.000 52.10025  ? 107 TYR   A N   1 
ATOM   893  C CA  . TYR   A 1 110 ? 28.56101 31.45817  -20.56634 1.000 55.72717  ? 107 TYR   A CA  1 
ATOM   894  C C   . TYR   A 1 110 ? 27.57925 30.37992  -21.00793 1.000 52.76374  ? 107 TYR   A C   1 
ATOM   895  O O   . TYR   A 1 110 ? 27.89215 29.18483  -20.96135 1.000 46.27686  ? 107 TYR   A O   1 
ATOM   896  C CB  . TYR   A 1 110 ? 28.19725 31.98425  -19.17719 1.000 51.53210  ? 107 TYR   A CB  1 
ATOM   897  C CG  . TYR   A 1 110 ? 29.37261 32.54530  -18.40980 1.000 50.98017  ? 107 TYR   A CG  1 
ATOM   898  C CD1 . TYR   A 1 110 ? 30.66924 32.40133  -18.88534 1.000 47.30327  ? 107 TYR   A CD1 1 
ATOM   899  C CD2 . TYR   A 1 110 ? 29.18701 33.20849  -17.20401 1.000 54.80063  ? 107 TYR   A CD2 1 
ATOM   900  C CE1 . TYR   A 1 110 ? 31.74877 32.90958  -18.18545 1.000 49.10889  ? 107 TYR   A CE1 1 
ATOM   901  C CE2 . TYR   A 1 110 ? 30.25984 33.71946  -16.49617 1.000 53.94812  ? 107 TYR   A CE2 1 
ATOM   902  C CZ  . TYR   A 1 110 ? 31.53784 33.56727  -16.99137 1.000 52.83266  ? 107 TYR   A CZ  1 
ATOM   903  O OH  . TYR   A 1 110 ? 32.60897 34.07434  -16.29081 1.000 56.75352  ? 107 TYR   A OH  1 
ATOM   904  N N   . LEU   A 1 111 ? 26.38120 30.78383  -21.43891 1.000 49.90064  ? 108 LEU   A N   1 
ATOM   905  C CA  . LEU   A 1 111 ? 25.39676 29.80732  -21.89519 1.000 51.55206  ? 108 LEU   A CA  1 
ATOM   906  C C   . LEU   A 1 111 ? 25.89976 29.04988  -23.11751 1.000 50.57807  ? 108 LEU   A C   1 
ATOM   907  O O   . LEU   A 1 111 ? 25.67897 27.83974  -23.24247 1.000 50.39986  ? 108 LEU   A O   1 
ATOM   908  C CB  . LEU   A 1 111 ? 24.07048 30.50054  -22.20519 1.000 45.18616  ? 108 LEU   A CB  1 
ATOM   909  C CG  . LEU   A 1 111 ? 22.92831 29.57093  -22.62013 1.000 45.93939  ? 108 LEU   A CG  1 
ATOM   910  C CD1 . LEU   A 1 111 ? 22.50756 28.69421  -21.44928 1.000 45.77162  ? 108 LEU   A CD1 1 
ATOM   911  C CD2 . LEU   A 1 111 ? 21.74837 30.36357  -23.16275 1.000 52.45571  ? 108 LEU   A CD2 1 
ATOM   912  N N   . PHE   A 1 112 ? 26.58165 29.74749  -24.02808 1.000 42.42068  ? 109 PHE   A N   1 
ATOM   913  C CA  . PHE   A 1 112 ? 27.12894 29.09742  -25.21463 1.000 49.70910  ? 109 PHE   A CA  1 
ATOM   914  C C   . PHE   A 1 112 ? 28.14811 28.03058  -24.83258 1.000 53.68354  ? 109 PHE   A C   1 
ATOM   915  O O   . PHE   A 1 112 ? 28.12946 26.91698  -25.36901 1.000 47.46692  ? 109 PHE   A O   1 
ATOM   916  C CB  . PHE   A 1 112 ? 27.75292 30.14767  -26.13554 1.000 51.99438  ? 109 PHE   A CB  1 
ATOM   917  C CG  . PHE   A 1 112 ? 28.18802 29.61119  -27.46898 1.000 48.00751  ? 109 PHE   A CG  1 
ATOM   918  C CD1 . PHE   A 1 112 ? 27.25773 29.33386  -28.45660 1.000 54.03956  ? 109 PHE   A CD1 1 
ATOM   919  C CD2 . PHE   A 1 112 ? 29.52966 29.40195  -27.74140 1.000 57.49229  ? 109 PHE   A CD2 1 
ATOM   920  C CE1 . PHE   A 1 112 ? 27.65593 28.84677  -29.68771 1.000 57.46394  ? 109 PHE   A CE1 1 
ATOM   921  C CE2 . PHE   A 1 112 ? 29.93464 28.91660  -28.97230 1.000 62.85112  ? 109 PHE   A CE2 1 
ATOM   922  C CZ  . PHE   A 1 112 ? 28.99657 28.63778  -29.94501 1.000 54.98958  ? 109 PHE   A CZ  1 
ATOM   923  N N   . GLN   A 1 113 ? 29.03951 28.35062  -23.89115 1.000 47.48998  ? 110 GLN   A N   1 
ATOM   924  C CA  . GLN   A 1 113 ? 30.03494 27.37768  -23.45366 1.000 51.94822  ? 110 GLN   A CA  1 
ATOM   925  C C   . GLN   A 1 113 ? 29.38777 26.21856  -22.70701 1.000 51.90340  ? 110 GLN   A C   1 
ATOM   926  O O   . GLN   A 1 113 ? 29.79994 25.06402  -22.86863 1.000 48.63220  ? 110 GLN   A O   1 
ATOM   927  C CB  . GLN   A 1 113 ? 31.08261 28.05861  -22.57629 1.000 51.29385  ? 110 GLN   A CB  1 
ATOM   928  C CG  . GLN   A 1 113 ? 31.85563 29.15803  -23.28087 1.000 53.42242  ? 110 GLN   A CG  1 
ATOM   929  C CD  . GLN   A 1 113 ? 32.80902 29.87106  -22.34696 1.000 59.39018  ? 110 GLN   A CD  1 
ATOM   930  O OE1 . GLN   A 1 113 ? 33.62541 29.23957  -21.67751 1.000 55.54298  ? 110 GLN   A OE1 1 
ATOM   931  N NE2 . GLN   A 1 113 ? 32.70196 31.19305  -22.28626 1.000 58.19928  ? 110 GLN   A NE2 1 
ATOM   932  N N   . LEU   A 1 114 ? 28.37893 26.50654  -21.87929 1.000 45.58061  ? 111 LEU   A N   1 
ATOM   933  C CA  . LEU   A 1 114 ? 27.67942 25.44132  -21.16813 1.000 48.06585  ? 111 LEU   A CA  1 
ATOM   934  C C   . LEU   A 1 114 ? 26.99585 24.48913  -22.14046 1.000 46.24092  ? 111 LEU   A C   1 
ATOM   935  O O   . LEU   A 1 114 ? 27.01937 23.26799  -21.94690 1.000 47.37436  ? 111 LEU   A O   1 
ATOM   936  C CB  . LEU   A 1 114 ? 26.65994 26.03749  -20.19753 1.000 43.14247  ? 111 LEU   A CB  1 
ATOM   937  C CG  . LEU   A 1 114 ? 27.20261 26.78921  -18.98120 1.000 56.67804  ? 111 LEU   A CG  1 
ATOM   938  C CD1 . LEU   A 1 114 ? 26.06441 27.43492  -18.20883 1.000 47.83074  ? 111 LEU   A CD1 1 
ATOM   939  C CD2 . LEU   A 1 114 ? 28.00269 25.85831  -18.08460 1.000 51.34740  ? 111 LEU   A CD2 1 
ATOM   940  N N   . LEU   A 1 115 ? 26.37995 25.03009  -23.19342 1.000 43.63553  ? 112 LEU   A N   1 
ATOM   941  C CA  . LEU   A 1 115 ? 25.74483 24.17885  -24.19329 1.000 44.91035  ? 112 LEU   A CA  1 
ATOM   942  C C   . LEU   A 1 115 ? 26.77059 23.36510  -24.97174 1.000 44.83889  ? 112 LEU   A C   1 
ATOM   943  O O   . LEU   A 1 115 ? 26.47451 22.24166  -25.39314 1.000 54.39860  ? 112 LEU   A O   1 
ATOM   944  C CB  . LEU   A 1 115 ? 24.90138 25.02764  -25.14436 1.000 44.00105  ? 112 LEU   A CB  1 
ATOM   945  C CG  . LEU   A 1 115 ? 23.64560 25.66843  -24.55236 1.000 46.32344  ? 112 LEU   A CG  1 
ATOM   946  C CD1 . LEU   A 1 115 ? 23.11535 26.75034  -25.47533 1.000 45.61720  ? 112 LEU   A CD1 1 
ATOM   947  C CD2 . LEU   A 1 115 ? 22.58135 24.61394  -24.29523 1.000 41.83567  ? 112 LEU   A CD2 1 
ATOM   948  N N   . GLN   A 1 116 ? 27.97477 23.90760  -25.17002 1.000 47.13120  ? 113 GLN   A N   1 
ATOM   949  C CA  . GLN   A 1 116 ? 29.02357 23.15498  -25.85182 1.000 45.22384  ? 113 GLN   A CA  1 
ATOM   950  C C   . GLN   A 1 116 ? 29.49352 21.97959  -25.00423 1.000 50.70449  ? 113 GLN   A C   1 
ATOM   951  O O   . GLN   A 1 116 ? 29.63324 20.85716  -25.50338 1.000 42.74989  ? 113 GLN   A O   1 
ATOM   952  C CB  . GLN   A 1 116 ? 30.19492 24.07524  -26.19367 1.000 50.73552  ? 113 GLN   A CB  1 
ATOM   953  C CG  . GLN   A 1 116 ? 29.91157 25.04787  -27.32272 1.000 44.74141  ? 113 GLN   A CG  1 
ATOM   954  C CD  . GLN   A 1 116 ? 31.06846 25.99145  -27.57740 1.000 61.25578  ? 113 GLN   A CD  1 
ATOM   955  O OE1 . GLN   A 1 116 ? 31.58590 26.62108  -26.65431 1.000 63.18285  ? 113 GLN   A OE1 1 
ATOM   956  N NE2 . GLN   A 1 116 ? 31.48699 26.08891  -28.83397 1.000 63.56093  ? 113 GLN   A NE2 1 
ATOM   957  N N   . GLY   A 1 117 ? 29.74795 22.21957  -23.71728 1.000 47.00470  ? 114 GLY   A N   1 
ATOM   958  C CA  . GLY   A 1 117 ? 30.12529 21.12701  -22.83655 1.000 49.61487  ? 114 GLY   A CA  1 
ATOM   959  C C   . GLY   A 1 117 ? 29.01773 20.10392  -22.67598 1.000 45.32687  ? 114 GLY   A C   1 
ATOM   960  O O   . GLY   A 1 117 ? 29.27798 18.90279  -22.58016 1.000 49.97912  ? 114 GLY   A O   1 
ATOM   961  N N   . LEU   A 1 118 ? 27.76464 20.56420  -22.65808 1.000 45.48998  ? 115 LEU   A N   1 
ATOM   962  C CA  . LEU   A 1 118 ? 26.64320 19.64165  -22.51647 1.000 48.20842  ? 115 LEU   A CA  1 
ATOM   963  C C   . LEU   A 1 118 ? 26.43190 18.83012  -23.78923 1.000 46.47911  ? 115 LEU   A C   1 
ATOM   964  O O   . LEU   A 1 118 ? 26.17981 17.62078  -23.72599 1.000 45.77754  ? 115 LEU   A O   1 
ATOM   965  C CB  . LEU   A 1 118 ? 25.37473 20.41076  -22.15145 1.000 43.14737  ? 115 LEU   A CB  1 
ATOM   966  C CG  . LEU   A 1 118 ? 24.21044 19.54615  -21.67163 1.000 53.99070  ? 115 LEU   A CG  1 
ATOM   967  C CD1 . LEU   A 1 118 ? 24.61729 18.76527  -20.43043 1.000 47.67493  ? 115 LEU   A CD1 1 
ATOM   968  C CD2 . LEU   A 1 118 ? 22.98071 20.39703  -21.39961 1.000 52.12923  ? 115 LEU   A CD2 1 
ATOM   969  N N   . ALA   A 1 119 ? 26.52624 19.47893  -24.95397 1.000 42.14332  ? 116 ALA   A N   1 
ATOM   970  C CA  . ALA   A 1 119 ? 26.43457 18.75192  -26.21666 1.000 53.23078  ? 116 ALA   A CA  1 
ATOM   971  C C   . ALA   A 1 119 ? 27.53540 17.70751  -26.33885 1.000 47.41959  ? 116 ALA   A C   1 
ATOM   972  O O   . ALA   A 1 119 ? 27.31694 16.64025  -26.92440 1.000 43.53312  ? 116 ALA   A O   1 
ATOM   973  C CB  . ALA   A 1 119 ? 26.49528 19.72530  -27.39454 1.000 46.38708  ? 116 ALA   A CB  1 
ATOM   974  N N   . PHE   A 1 120 ? 28.71908 17.99323  -25.79108 1.000 48.98092  ? 117 PHE   A N   1 
ATOM   975  C CA  . PHE   A 1 120 ? 29.79720 17.01033  -25.79472 1.000 48.80147  ? 117 PHE   A CA  1 
ATOM   976  C C   . PHE   A 1 120 ? 29.45235 15.82026  -24.90708 1.000 46.37120  ? 117 PHE   A C   1 
ATOM   977  O O   . PHE   A 1 120 ? 29.69150 14.66556  -25.27960 1.000 50.82389  ? 117 PHE   A O   1 
ATOM   978  C CB  . PHE   A 1 120 ? 31.10101 17.66818  -25.34314 1.000 53.38213  ? 117 PHE   A CB  1 
ATOM   979  C CG  . PHE   A 1 120 ? 32.30339 16.76941  -25.43448 1.000 48.32201  ? 117 PHE   A CG  1 
ATOM   980  C CD1 . PHE   A 1 120 ? 32.98366 16.62081  -26.63132 1.000 55.98223  ? 117 PHE   A CD1 1 
ATOM   981  C CD2 . PHE   A 1 120 ? 32.76521 16.08914  -24.31921 1.000 49.91137  ? 117 PHE   A CD2 1 
ATOM   982  C CE1 . PHE   A 1 120 ? 34.09825 15.80304  -26.71832 1.000 55.02732  ? 117 PHE   A CE1 1 
ATOM   983  C CE2 . PHE   A 1 120 ? 33.87747 15.26909  -24.39828 1.000 54.78545  ? 117 PHE   A CE2 1 
ATOM   984  C CZ  . PHE   A 1 120 ? 34.54574 15.12692  -25.59948 1.000 50.19230  ? 117 PHE   A CZ  1 
ATOM   985  N N   . CYS   A 1 121 ? 28.88535 16.08463  -23.72608 1.000 42.72664  ? 118 CYS   A N   1 
ATOM   986  C CA  . CYS   A 1 121 ? 28.47295 15.00159  -22.83718 1.000 41.39791  ? 118 CYS   A CA  1 
ATOM   987  C C   . CYS   A 1 121 ? 27.41182 14.12644  -23.49188 1.000 50.20485  ? 118 CYS   A C   1 
ATOM   988  O O   . CYS   A 1 121 ? 27.48422 12.89333  -23.43724 1.000 46.22389  ? 118 CYS   A O   1 
ATOM   989  C CB  . CYS   A 1 121 ? 27.94426 15.57025  -21.51915 1.000 50.53463  ? 118 CYS   A CB  1 
ATOM   990  S SG  . CYS   A 1 121 ? 29.16757 16.41619  -20.50202 1.000 51.57047  ? 118 CYS   A SG  1 
ATOM   991  N N   . HIS   A 1 122 ? 26.41136 14.75208  -24.11444 1.000 42.42419  ? 119 HIS   A N   1 
ATOM   992  C CA  . HIS   A 1 122 ? 25.29737 13.99348  -24.67145 1.000 47.07643  ? 119 HIS   A CA  1 
ATOM   993  C C   . HIS   A 1 122 ? 25.72014 13.20199  -25.90415 1.000 38.95495  ? 119 HIS   A C   1 
ATOM   994  O O   . HIS   A 1 122 ? 25.24593 12.07998  -26.11590 1.000 46.66452  ? 119 HIS   A O   1 
ATOM   995  C CB  . HIS   A 1 122 ? 24.13914 14.93749  -24.98944 1.000 39.50578  ? 119 HIS   A CB  1 
ATOM   996  C CG  . HIS   A 1 122 ? 23.50413 15.53576  -23.77175 1.000 43.33743  ? 119 HIS   A CG  1 
ATOM   997  N ND1 . HIS   A 1 122 ? 22.53190 16.51050  -23.83828 1.000 50.09786  ? 119 HIS   A ND1 1 
ATOM   998  C CD2 . HIS   A 1 122 ? 23.69997 15.28961  -22.45434 1.000 50.37297  ? 119 HIS   A CD2 1 
ATOM   999  C CE1 . HIS   A 1 122 ? 22.15838 16.84093  -22.61461 1.000 55.60524  ? 119 HIS   A CE1 1 
ATOM   1000 N NE2 . HIS   A 1 122 ? 22.85126 16.11404  -21.75638 1.000 44.04845  ? 119 HIS   A NE2 1 
ATOM   1001 N N   . SER   A 1 123 ? 26.61290 13.76286  -26.72679 1.000 44.08622  ? 120 SER   A N   1 
ATOM   1002 C CA  . SER   A 1 123 ? 27.12645 13.01221  -27.86905 1.000 46.49234  ? 120 SER   A CA  1 
ATOM   1003 C C   . SER   A 1 123 ? 27.94020 11.80655  -27.41816 1.000 51.45970  ? 120 SER   A C   1 
ATOM   1004 O O   . SER   A 1 123 ? 28.01254 10.80352  -28.13774 1.000 51.97883  ? 120 SER   A O   1 
ATOM   1005 C CB  . SER   A 1 123 ? 27.97021 13.91799  -28.76700 1.000 46.24724  ? 120 SER   A CB  1 
ATOM   1006 O OG  . SER   A 1 123 ? 29.18271 14.27951  -28.13092 1.000 57.18648  ? 120 SER   A OG  1 
ATOM   1007 N N   . HIS   A 1 124 ? 28.55572 11.88532  -26.23975 1.000 44.72204  ? 121 HIS   A N   1 
ATOM   1008 C CA  . HIS   A 1 124 ? 29.22579 10.74980  -25.62348 1.000 43.82463  ? 121 HIS   A CA  1 
ATOM   1009 C C   . HIS   A 1 124 ? 28.27874 9.90200   -24.78654 1.000 48.73630  ? 121 HIS   A C   1 
ATOM   1010 O O   . HIS   A 1 124 ? 28.74070 9.03684   -24.03491 1.000 48.19808  ? 121 HIS   A O   1 
ATOM   1011 C CB  . HIS   A 1 124 ? 30.39738 11.22775  -24.76198 1.000 51.14966  ? 121 HIS   A CB  1 
ATOM   1012 C CG  . HIS   A 1 124 ? 31.61336 11.59828  -25.55113 1.000 51.02208  ? 121 HIS   A CG  1 
ATOM   1013 N ND1 . HIS   A 1 124 ? 31.61291 12.60756  -26.48950 1.000 62.17133  ? 121 HIS   A ND1 1 
ATOM   1014 C CD2 . HIS   A 1 124 ? 32.86776 11.08872  -25.54723 1.000 58.81010  ? 121 HIS   A CD2 1 
ATOM   1015 C CE1 . HIS   A 1 124 ? 32.81524 12.70540  -27.02820 1.000 58.01346  ? 121 HIS   A CE1 1 
ATOM   1016 N NE2 . HIS   A 1 124 ? 33.59564 11.79598  -26.47303 1.000 67.15591  ? 121 HIS   A NE2 1 
ATOM   1017 N N   . ARG   A 1 125 ? 26.97077 10.14164  -24.89633 1.000 41.05947  ? 122 ARG   A N   1 
ATOM   1018 C CA  . ARG   A 1 125 ? 25.95141 9.34963   -24.20958 1.000 49.26095  ? 122 ARG   A CA  1 
ATOM   1019 C C   . ARG   A 1 125 ? 26.13485 9.39499   -22.69233 1.000 62.61215  ? 122 ARG   A C   1 
ATOM   1020 O O   . ARG   A 1 125 ? 26.13059 8.36852   -22.01102 1.000 51.74045  ? 122 ARG   A O   1 
ATOM   1021 C CB  . ARG   A 1 125 ? 25.94157 7.90879   -24.72759 1.000 49.26727  ? 122 ARG   A CB  1 
ATOM   1022 C CG  . ARG   A 1 125 ? 25.42456 7.78732   -26.15565 1.000 53.88892  ? 122 ARG   A CG  1 
ATOM   1023 C CD  . ARG   A 1 125 ? 25.96106 6.55358   -26.86731 1.000 62.13918  ? 122 ARG   A CD  1 
ATOM   1024 N NE  . ARG   A 1 125 ? 25.61294 5.31197   -26.18779 1.000 61.30059  ? 122 ARG   A NE  1 
ATOM   1025 C CZ  . ARG   A 1 125 ? 26.46335 4.58598   -25.47515 1.000 77.55590  ? 122 ARG   A CZ  1 
ATOM   1026 N NH1 . ARG   A 1 125 ? 27.72836 4.94657   -25.33167 1.000 71.78563  ? 122 ARG   A NH1 1 
ATOM   1027 N NH2 . ARG   A 1 125 ? 26.03482 3.46869   -24.89485 1.000 77.61181  ? 122 ARG   A NH2 1 
ATOM   1028 N N   . VAL   A 1 126 ? 26.28725 10.60784  -22.16197 1.000 46.47277  ? 123 VAL   A N   1 
ATOM   1029 C CA  . VAL   A 1 126 ? 26.45634 10.83264  -20.73080 1.000 43.72798  ? 123 VAL   A CA  1 
ATOM   1030 C C   . VAL   A 1 126 ? 25.47786 11.91112  -20.28599 1.000 43.31268  ? 123 VAL   A C   1 
ATOM   1031 O O   . VAL   A 1 126 ? 25.42590 12.99386  -20.88101 1.000 47.19762  ? 123 VAL   A O   1 
ATOM   1032 C CB  . VAL   A 1 126 ? 27.90031 11.24078  -20.37820 1.000 43.14836  ? 123 VAL   A CB  1 
ATOM   1033 C CG1 . VAL   A 1 126 ? 27.99470 11.64925  -18.91585 1.000 46.69273  ? 123 VAL   A CG1 1 
ATOM   1034 C CG2 . VAL   A 1 126 ? 28.86496 10.10404  -20.67621 1.000 54.01243  ? 123 VAL   A CG2 1 
ATOM   1035 N N   . LEU   A 1 127 ? 24.70178 11.61158  -19.24865 1.000 44.46379  ? 124 LEU   A N   1 
ATOM   1036 C CA  . LEU   A 1 127 ? 23.83730 12.58459  -18.59690 1.000 41.68399  ? 124 LEU   A CA  1 
ATOM   1037 C C   . LEU   A 1 127 ? 24.53785 13.12772  -17.36109 1.000 48.42001  ? 124 LEU   A C   1 
ATOM   1038 O O   . LEU   A 1 127 ? 25.13200 12.36648  -16.59499 1.000 46.83402  ? 124 LEU   A O   1 
ATOM   1039 C CB  . LEU   A 1 127 ? 22.50498 11.95452  -18.18876 1.000 41.96340  ? 124 LEU   A CB  1 
ATOM   1040 C CG  . LEU   A 1 127 ? 21.75704 11.16046  -19.25559 1.000 53.06719  ? 124 LEU   A CG  1 
ATOM   1041 C CD1 . LEU   A 1 127 ? 20.49682 10.54513  -18.67043 1.000 50.53434  ? 124 LEU   A CD1 1 
ATOM   1042 C CD2 . LEU   A 1 127 ? 21.43052 12.05505  -20.43271 1.000 48.81573  ? 124 LEU   A CD2 1 
ATOM   1043 N N   . HIS   A 1 128 ? 24.46379 14.44525  -17.16626 1.000 40.58261  ? 125 HIS   A N   1 
ATOM   1044 C CA  . HIS   A 1 128 ? 25.06605 15.04191  -15.97769 1.000 43.07911  ? 125 HIS   A CA  1 
ATOM   1045 C C   . HIS   A 1 128 ? 24.16675 14.86920  -14.75716 1.000 38.65975  ? 125 HIS   A C   1 
ATOM   1046 O O   . HIS   A 1 128 ? 24.61544 14.39258  -13.70756 1.000 46.13183  ? 125 HIS   A O   1 
ATOM   1047 C CB  . HIS   A 1 128 ? 25.36494 16.52196  -16.22130 1.000 41.49111  ? 125 HIS   A CB  1 
ATOM   1048 C CG  . HIS   A 1 128 ? 26.12073 17.17053  -15.10487 1.000 43.05329  ? 125 HIS   A CG  1 
ATOM   1049 N ND1 . HIS   A 1 128 ? 25.51632 17.56990  -13.93253 1.000 43.29377  ? 125 HIS   A ND1 1 
ATOM   1050 C CD2 . HIS   A 1 128 ? 27.43317 17.47712  -14.97518 1.000 43.84442  ? 125 HIS   A CD2 1 
ATOM   1051 C CE1 . HIS   A 1 128 ? 26.42269 18.09778  -13.12986 1.000 41.89195  ? 125 HIS   A CE1 1 
ATOM   1052 N NE2 . HIS   A 1 128 ? 27.59404 18.05391  -13.73859 1.000 45.64866  ? 125 HIS   A NE2 1 
ATOM   1053 N N   . ARG   A 1 129 ? 22.90060 15.27190  -14.87588 1.000 40.88091  ? 126 ARG   A N   1 
ATOM   1054 C CA  . ARG   A 1 129 ? 21.83640 15.05003  -13.89749 1.000 43.14330  ? 126 ARG   A CA  1 
ATOM   1055 C C   . ARG   A 1 129 ? 22.00641 15.84639  -12.60853 1.000 45.66304  ? 126 ARG   A C   1 
ATOM   1056 O O   . ARG   A 1 129 ? 21.33551 15.54097  -11.61582 1.000 47.13183  ? 126 ARG   A O   1 
ATOM   1057 C CB  . ARG   A 1 129 ? 21.68340 13.56320  -13.54879 1.000 40.53351  ? 126 ARG   A CB  1 
ATOM   1058 C CG  . ARG   A 1 129 ? 21.46321 12.65746  -14.75079 1.000 41.63746  ? 126 ARG   A CG  1 
ATOM   1059 C CD  . ARG   A 1 129 ? 21.02834 11.26709  -14.31632 1.000 46.25239  ? 126 ARG   A CD  1 
ATOM   1060 N NE  . ARG   A 1 129 ? 21.98882 10.64065  -13.41540 1.000 45.77061  ? 126 ARG   A NE  1 
ATOM   1061 C CZ  . ARG   A 1 129 ? 21.83593 9.43555   -12.88274 1.000 65.86282  ? 126 ARG   A CZ  1 
ATOM   1062 N NH1 . ARG   A 1 129 ? 20.76974 8.69630   -13.14184 1.000 45.00908  ? 126 ARG   A NH1 1 
ATOM   1063 N NH2 . ARG   A 1 129 ? 22.77569 8.96004   -12.06971 1.000 50.96851  ? 126 ARG   A NH2 1 
ATOM   1064 N N   . ASP   A 1 130 ? 22.86927 16.85697  -12.58376 1.000 43.73885  ? 127 ASP   A N   1 
ATOM   1065 C CA  . ASP   A 1 130 ? 22.98454 17.71667  -11.40772 1.000 44.95500  ? 127 ASP   A CA  1 
ATOM   1066 C C   . ASP   A 1 130 ? 23.53167 19.08067  -11.82011 1.000 46.93452  ? 127 ASP   A C   1 
ATOM   1067 O O   . ASP   A 1 130 ? 24.44268 19.62763  -11.19622 1.000 44.82722  ? 127 ASP   A O   1 
ATOM   1068 C CB  . ASP   A 1 130 ? 23.85763 17.07092  -10.33148 1.000 35.98378  ? 127 ASP   A CB  1 
ATOM   1069 C CG  . ASP   A 1 130 ? 23.55831 17.60709  -8.93847  1.000 68.77751  ? 127 ASP   A CG  1 
ATOM   1070 O OD1 . ASP   A 1 130 ? 22.46954 18.19044  -8.74480  1.000 48.70635  ? 127 ASP   A OD1 1 
ATOM   1071 O OD2 . ASP   A 1 130 ? 24.41008 17.44958  -8.03866  1.000 66.38155  ? 127 ASP   A OD2 1 
ATOM   1072 N N   . LEU   A 1 131 ? 22.97181 19.64858  -12.88444 1.000 41.72366  ? 128 LEU   A N   1 
ATOM   1073 C CA  . LEU   A 1 131 ? 23.38781 20.96335  -13.35924 1.000 49.91733  ? 128 LEU   A CA  1 
ATOM   1074 C C   . LEU   A 1 131 ? 22.75899 22.02989  -12.47130 1.000 51.75747  ? 128 LEU   A C   1 
ATOM   1075 O O   . LEU   A 1 131 ? 21.54869 22.27070  -12.53375 1.000 58.57412  ? 128 LEU   A O   1 
ATOM   1076 C CB  . LEU   A 1 131 ? 22.99135 21.15846  -14.81899 1.000 41.29052  ? 128 LEU   A CB  1 
ATOM   1077 C CG  . LEU   A 1 131 ? 23.74173 20.31172  -15.84824 1.000 51.18233  ? 128 LEU   A CG  1 
ATOM   1078 C CD1 . LEU   A 1 131 ? 23.20726 20.57514  -17.24594 1.000 52.59323  ? 128 LEU   A CD1 1 
ATOM   1079 C CD2 . LEU   A 1 131 ? 25.23476 20.58681  -15.78550 1.000 41.73817  ? 128 LEU   A CD2 1 
ATOM   1080 N N   . LYS   A 1 132 ? 23.57616 22.65756  -11.63892 1.000 50.14581  ? 129 LYS   A N   1 
ATOM   1081 C CA  . LYS   A 1 132 ? 23.17562 23.76781  -10.79281 1.000 52.45337  ? 129 LYS   A CA  1 
ATOM   1082 C C   . LYS   A 1 132 ? 24.32406 24.75978  -10.75934 1.000 40.47314  ? 129 LYS   A C   1 
ATOM   1083 O O   . LYS   A 1 132 ? 25.46931 24.39755  -11.05884 1.000 44.63799  ? 129 LYS   A O   1 
ATOM   1084 C CB  . LYS   A 1 132 ? 22.81347 23.29816  -9.37526  1.000 47.41031  ? 129 LYS   A CB  1 
ATOM   1085 C CG  . LYS   A 1 132 ? 23.86847 22.43879  -8.69782  1.000 42.06938  ? 129 LYS   A CG  1 
ATOM   1086 C CD  . LYS   A 1 132 ? 23.37807 21.94700  -7.34313  1.000 49.15981  ? 129 LYS   A CD  1 
ATOM   1087 C CE  . LYS   A 1 132 ? 24.41180 21.06263  -6.66338  1.000 59.09478  ? 129 LYS   A CE  1 
ATOM   1088 N NZ  . LYS   A 1 132 ? 23.97219 20.63047  -5.30669  1.000 68.71063  ? 129 LYS   A NZ  1 
ATOM   1089 N N   . PRO   A 1 133 ? 24.05529 26.02709  -10.42620 1.000 43.45658  ? 130 PRO   A N   1 
ATOM   1090 C CA  . PRO   A 1 133 ? 25.13747 27.02571  -10.43368 1.000 41.65806  ? 130 PRO   A CA  1 
ATOM   1091 C C   . PRO   A 1 133 ? 26.31877 26.65055  -9.55774  1.000 41.07248  ? 130 PRO   A C   1 
ATOM   1092 O O   . PRO   A 1 133 ? 27.45139 27.03881  -9.86822  1.000 46.57727  ? 130 PRO   A O   1 
ATOM   1093 C CB  . PRO   A 1 133 ? 24.44152 28.29812  -9.93136  1.000 39.47413  ? 130 PRO   A CB  1 
ATOM   1094 C CG  . PRO   A 1 133 ? 23.01308 28.10765  -10.29476 1.000 59.50922  ? 130 PRO   A CG  1 
ATOM   1095 C CD  . PRO   A 1 133 ? 22.74851 26.63982  -10.12750 1.000 47.29855  ? 130 PRO   A CD  1 
ATOM   1096 N N   . GLN   A 1 134 ? 26.09527 25.89771  -8.47720  1.000 42.43415  ? 131 GLN   A N   1 
ATOM   1097 C CA  . GLN   A 1 134 ? 27.20224 25.47600  -7.62682  1.000 40.80227  ? 131 GLN   A CA  1 
ATOM   1098 C C   . GLN   A 1 134 ? 28.14589 24.51082  -8.33276  1.000 45.10801  ? 131 GLN   A C   1 
ATOM   1099 O O   . GLN   A 1 134 ? 29.30147 24.38160  -7.91536  1.000 48.51339  ? 131 GLN   A O   1 
ATOM   1100 C CB  . GLN   A 1 134 ? 26.67562 24.82754  -6.34504  1.000 49.55585  ? 131 GLN   A CB  1 
ATOM   1101 C CG  . GLN   A 1 134 ? 25.84630 25.74744  -5.46357  1.000 56.07826  ? 131 GLN   A CG  1 
ATOM   1102 C CD  . GLN   A 1 134 ? 24.35948 25.64293  -5.74226  1.000 65.99774  ? 131 GLN   A CD  1 
ATOM   1103 O OE1 . GLN   A 1 134 ? 23.92213 25.70892  -6.89207  1.000 45.61107  ? 131 GLN   A OE1 1 
ATOM   1104 N NE2 . GLN   A 1 134 ? 23.57348 25.47136  -4.68659  1.000 74.84980  ? 131 GLN   A NE2 1 
ATOM   1105 N N   . ASN   A 1 135 ? 27.68638 23.83484  -9.38552  1.000 40.56815  ? 132 ASN   A N   1 
ATOM   1106 C CA  . ASN   A 1 135 ? 28.50089 22.87713  -10.12128 1.000 47.49496  ? 132 ASN   A CA  1 
ATOM   1107 C C   . ASN   A 1 135 ? 29.05407 23.44813  -11.41991 1.000 47.23130  ? 132 ASN   A C   1 
ATOM   1108 O O   . ASN   A 1 135 ? 29.61060 22.69847  -12.22864 1.000 43.03690  ? 132 ASN   A O   1 
ATOM   1109 C CB  . ASN   A 1 135 ? 27.69347 21.61008  -10.40852 1.000 48.00649  ? 132 ASN   A CB  1 
ATOM   1110 C CG  . ASN   A 1 135 ? 27.45423 20.78276  -9.16461  1.000 49.86153  ? 132 ASN   A CG  1 
ATOM   1111 O OD1 . ASN   A 1 135 ? 28.21063 20.86853  -8.19720  1.000 56.15599  ? 132 ASN   A OD1 1 
ATOM   1112 N ND2 . ASN   A 1 135 ? 26.40264 19.97336  -9.18231  1.000 42.49985  ? 132 ASN   A ND2 1 
ATOM   1113 N N   . LEU   A 1 136 ? 28.91097 24.75077  -11.63890 1.000 48.25453  ? 133 LEU   A N   1 
ATOM   1114 C CA  . LEU   A 1 136 ? 29.45832 25.42667  -12.80713 1.000 43.45975  ? 133 LEU   A CA  1 
ATOM   1115 C C   . LEU   A 1 136 ? 30.56776 26.35615  -12.33731 1.000 52.05062  ? 133 LEU   A C   1 
ATOM   1116 O O   . LEU   A 1 136 ? 30.30914 27.30970  -11.59456 1.000 51.24921  ? 133 LEU   A O   1 
ATOM   1117 C CB  . LEU   A 1 136 ? 28.37273 26.20373  -13.55079 1.000 44.14333  ? 133 LEU   A CB  1 
ATOM   1118 C CG  . LEU   A 1 136 ? 27.09924 25.42127  -13.87360 1.000 49.79799  ? 133 LEU   A CG  1 
ATOM   1119 C CD1 . LEU   A 1 136 ? 26.14787 26.26657  -14.70214 1.000 54.24671  ? 133 LEU   A CD1 1 
ATOM   1120 C CD2 . LEU   A 1 136 ? 27.43373 24.12480  -14.58926 1.000 44.57359  ? 133 LEU   A CD2 1 
ATOM   1121 N N   . LEU   A 1 137 ? 31.79435 26.07521  -12.76507 1.000 42.59754  ? 134 LEU   A N   1 
ATOM   1122 C CA  . LEU   A 1 137 ? 32.97583 26.78105  -12.29442 1.000 47.38323  ? 134 LEU   A CA  1 
ATOM   1123 C C   . LEU   A 1 137 ? 33.50516 27.69841  -13.38822 1.000 50.75506  ? 134 LEU   A C   1 
ATOM   1124 O O   . LEU   A 1 137 ? 33.44453 27.36334  -14.57572 1.000 52.83394  ? 134 LEU   A O   1 
ATOM   1125 C CB  . LEU   A 1 137 ? 34.06014 25.79028  -11.86554 1.000 41.75074  ? 134 LEU   A CB  1 
ATOM   1126 C CG  . LEU   A 1 137 ? 33.60660 24.71988  -10.86858 1.000 43.49686  ? 134 LEU   A CG  1 
ATOM   1127 C CD1 . LEU   A 1 137 ? 34.74719 23.77022  -10.53957 1.000 48.52680  ? 134 LEU   A CD1 1 
ATOM   1128 C CD2 . LEU   A 1 137 ? 33.05700 25.36330  -9.60564  1.000 50.62402  ? 134 LEU   A CD2 1 
ATOM   1129 N N   . ILE   A 1 138 ? 34.02505 28.85660  -12.98272 1.000 45.77601  ? 135 ILE   A N   1 
ATOM   1130 C CA  . ILE   A 1 138 ? 34.54486 29.85140  -13.91081 1.000 46.69045  ? 135 ILE   A CA  1 
ATOM   1131 C C   . ILE   A 1 138 ? 35.97881 30.18383  -13.53067 1.000 59.27977  ? 135 ILE   A C   1 
ATOM   1132 O O   . ILE   A 1 138 ? 36.37278 30.07915  -12.36459 1.000 53.11553  ? 135 ILE   A O   1 
ATOM   1133 C CB  . ILE   A 1 138 ? 33.68372 31.13444  -13.92748 1.000 49.42160  ? 135 ILE   A CB  1 
ATOM   1134 C CG1 . ILE   A 1 138 ? 33.71567 31.81536  -12.55754 1.000 62.64121  ? 135 ILE   A CG1 1 
ATOM   1135 C CG2 . ILE   A 1 138 ? 32.25214 30.81637  -14.33073 1.000 46.82779  ? 135 ILE   A CG2 1 
ATOM   1136 C CD1 . ILE   A 1 138 ? 32.96429 33.12786  -12.50821 1.000 64.12101  ? 135 ILE   A CD1 1 
ATOM   1137 N N   . ASN   A 1 139 ? 36.76272 30.58808  -14.52706 1.000 56.97848  ? 136 ASN   A N   1 
ATOM   1138 C CA  . ASN   A 1 139 ? 38.12068 31.05610  -14.30658 1.000 58.71044  ? 136 ASN   A CA  1 
ATOM   1139 C C   . ASN   A 1 139 ? 38.19312 32.55929  -14.57425 1.000 60.59203  ? 136 ASN   A C   1 
ATOM   1140 O O   . ASN   A 1 139 ? 37.17734 33.21953  -14.82397 1.000 56.48461  ? 136 ASN   A O   1 
ATOM   1141 C CB  . ASN   A 1 139 ? 39.11138 30.26367  -15.17012 1.000 61.19839  ? 136 ASN   A CB  1 
ATOM   1142 C CG  . ASN   A 1 139 ? 38.86036 30.41650  -16.66523 1.000 56.65595  ? 136 ASN   A CG  1 
ATOM   1143 O OD1 . ASN   A 1 139 ? 38.08033 31.26212  -17.10415 1.000 64.74210  ? 136 ASN   A OD1 1 
ATOM   1144 N ND2 . ASN   A 1 139 ? 39.53747 29.59331  -17.45639 1.000 62.13344  ? 136 ASN   A ND2 1 
ATOM   1145 N N   . THR   A 1 140 ? 39.40660 33.10262  -14.52532 1.000 55.91120  ? 137 THR   A N   1 
ATOM   1146 C CA  . THR   A 1 140 ? 39.63556 34.51912  -14.77070 1.000 62.64591  ? 137 THR   A CA  1 
ATOM   1147 C C   . THR   A 1 140 ? 39.88850 34.82889  -16.24016 1.000 69.17580  ? 137 THR   A C   1 
ATOM   1148 O O   . THR   A 1 140 ? 40.37435 35.91952  -16.55630 1.000 70.94311  ? 137 THR   A O   1 
ATOM   1149 C CB  . THR   A 1 140 ? 40.81317 35.01808  -13.92997 1.000 57.79202  ? 137 THR   A CB  1 
ATOM   1150 O OG1 . THR   A 1 140 ? 42.00356 34.31783  -14.31082 1.000 69.10172  ? 137 THR   A OG1 1 
ATOM   1151 C CG2 . THR   A 1 140 ? 40.54582 34.78624  -12.44917 1.000 56.25048  ? 137 THR   A CG2 1 
ATOM   1152 N N   . GLU   A 1 141 ? 39.57251 33.89819  -17.14188 1.000 69.50171  ? 138 GLU   A N   1 
ATOM   1153 C CA  . GLU   A 1 141 ? 39.78730 34.08949  -18.57111 1.000 69.99221  ? 138 GLU   A CA  1 
ATOM   1154 C C   . GLU   A 1 141 ? 38.48945 33.97715  -19.36542 1.000 62.89410  ? 138 GLU   A C   1 
ATOM   1155 O O   . GLU   A 1 141 ? 38.52723 33.75388  -20.57905 1.000 61.47107  ? 138 GLU   A O   1 
ATOM   1156 C CB  . GLU   A 1 141 ? 40.82342 33.09043  -19.09145 1.000 66.55304  ? 138 GLU   A CB  1 
ATOM   1157 C CG  . GLU   A 1 141 ? 42.17404 33.17896  -18.39306 1.000 72.56831  ? 138 GLU   A CG  1 
ATOM   1158 C CD  . GLU   A 1 141 ? 43.17826 32.17352  -18.92548 1.000 92.92228  ? 138 GLU   A CD  1 
ATOM   1159 O OE1 . GLU   A 1 141 ? 42.78296 31.30409  -19.73016 1.000 71.40604  ? 138 GLU   A OE1 1 
ATOM   1160 O OE2 . GLU   A 1 141 ? 44.36453 32.25399  -18.54079 1.000 85.62517  ? 138 GLU   A OE2 1 
ATOM   1161 N N   . GLY   A 1 142 ? 37.34163 34.12451  -18.70541 1.000 59.99954  ? 139 GLY   A N   1 
ATOM   1162 C CA  . GLY   A 1 142 ? 36.06330 34.12802  -19.38718 1.000 57.24182  ? 139 GLY   A CA  1 
ATOM   1163 C C   . GLY   A 1 142 ? 35.46875 32.76702  -19.66367 1.000 54.68060  ? 139 GLY   A C   1 
ATOM   1164 O O   . GLY   A 1 142 ? 34.44497 32.68625  -20.35133 1.000 57.12709  ? 139 GLY   A O   1 
ATOM   1165 N N   . ALA   A 1 143 ? 36.06729 31.69863  -19.14916 1.000 51.43018  ? 140 ALA   A N   1 
ATOM   1166 C CA  . ALA   A 1 143 ? 35.60405 30.34095  -19.38835 1.000 56.85527  ? 140 ALA   A CA  1 
ATOM   1167 C C   . ALA   A 1 143 ? 34.71257 29.86199  -18.24788 1.000 50.59925  ? 140 ALA   A C   1 
ATOM   1168 O O   . ALA   A 1 143 ? 34.84611 30.30112  -17.10273 1.000 50.46223  ? 140 ALA   A O   1 
ATOM   1169 C CB  . ALA   A 1 143 ? 36.79041 29.38766  -19.55223 1.000 57.85266  ? 140 ALA   A CB  1 
ATOM   1170 N N   . ILE   A 1 144 ? 33.79428 28.95533  -18.57711 1.000 44.51663  ? 141 ILE   A N   1 
ATOM   1171 C CA  . ILE   A 1 144 ? 32.94980 28.28951  -17.59172 1.000 40.69566  ? 141 ILE   A CA  1 
ATOM   1172 C C   . ILE   A 1 144 ? 32.92629 26.80296  -17.92719 1.000 54.99637  ? 141 ILE   A C   1 
ATOM   1173 O O   . ILE   A 1 144 ? 32.94750 26.42339  -19.10298 1.000 49.15133  ? 141 ILE   A O   1 
ATOM   1174 C CB  . ILE   A 1 144 ? 31.52722 28.89132  -17.55651 1.000 41.50167  ? 141 ILE   A CB  1 
ATOM   1175 C CG1 . ILE   A 1 144 ? 30.70717 28.27979  -16.41796 1.000 45.62804  ? 141 ILE   A CG1 1 
ATOM   1176 C CG2 . ILE   A 1 144 ? 30.82273 28.71552  -18.89948 1.000 48.41154  ? 141 ILE   A CG2 1 
ATOM   1177 C CD1 . ILE   A 1 144 ? 29.36158 28.94181  -16.21211 1.000 45.80001  ? 141 ILE   A CD1 1 
ATOM   1178 N N   . LYS   A 1 145 ? 32.91060 25.95526  -16.89638 1.000 50.32064  ? 142 LYS   A N   1 
ATOM   1179 C CA  . LYS   A 1 145 ? 33.08988 24.52224  -17.09267 1.000 44.72513  ? 142 LYS   A CA  1 
ATOM   1180 C C   . LYS   A 1 145 ? 32.13591 23.73212  -16.20854 1.000 51.41322  ? 142 LYS   A C   1 
ATOM   1181 O O   . LYS   A 1 145 ? 31.79818 24.15030  -15.09842 1.000 47.82013  ? 142 LYS   A O   1 
ATOM   1182 C CB  . LYS   A 1 145 ? 34.53924 24.09233  -16.80223 1.000 44.36761  ? 142 LYS   A CB  1 
ATOM   1183 C CG  . LYS   A 1 145 ? 35.58980 24.92135  -17.53077 1.000 49.21607  ? 142 LYS   A CG  1 
ATOM   1184 C CD  . LYS   A 1 145 ? 36.98519 24.33372  -17.40610 1.000 47.05207  ? 142 LYS   A CD  1 
ATOM   1185 C CE  . LYS   A 1 145 ? 37.99513 25.18707  -18.16295 1.000 47.55935  ? 142 LYS   A CE  1 
ATOM   1186 N NZ  . LYS   A 1 145 ? 39.30802 24.50765  -18.33494 1.000 60.32668  ? 142 LYS   A NZ  1 
ATOM   1187 N N   . LEU   A 1 146 ? 31.71332 22.57533  -16.71735 1.000 42.37806  ? 143 LEU   A N   1 
ATOM   1188 C CA  . LEU   A 1 146 ? 30.88193 21.65510  -15.95369 1.000 41.65561  ? 143 LEU   A CA  1 
ATOM   1189 C C   . LEU   A 1 146 ? 31.73148 20.87164  -14.96344 1.000 40.74889  ? 143 LEU   A C   1 
ATOM   1190 O O   . LEU   A 1 146 ? 32.82217 20.39965  -15.29644 1.000 45.54936  ? 143 LEU   A O   1 
ATOM   1191 C CB  . LEU   A 1 146 ? 30.15507 20.67904  -16.88027 1.000 50.43505  ? 143 LEU   A CB  1 
ATOM   1192 C CG  . LEU   A 1 146 ? 29.29106 21.23170  -18.01502 1.000 55.19719  ? 143 LEU   A CG  1 
ATOM   1193 C CD1 . LEU   A 1 146 ? 28.69408 20.08338  -18.80664 1.000 48.67074  ? 143 LEU   A CD1 1 
ATOM   1194 C CD2 . LEU   A 1 146 ? 28.20058 22.13735  -17.47709 1.000 56.41300  ? 143 LEU   A CD2 1 
ATOM   1195 N N   . ALA   A 1 147 ? 31.21798 20.72187  -13.74449 1.000 45.38196  ? 144 ALA   A N   1 
ATOM   1196 C CA  . ALA   A 1 147 ? 31.94216 20.04524  -12.68039 1.000 41.50020  ? 144 ALA   A CA  1 
ATOM   1197 C C   . ALA   A 1 147 ? 30.99229 19.13043  -11.92092 1.000 51.56604  ? 144 ALA   A C   1 
ATOM   1198 O O   . ALA   A 1 147 ? 29.77219 19.17153  -12.10343 1.000 47.60221  ? 144 ALA   A O   1 
ATOM   1199 C CB  . ALA   A 1 147 ? 32.59745 21.04586  -11.72009 1.000 56.52659  ? 144 ALA   A CB  1 
ATOM   1200 N N   . ASP   A 1 148 ? 31.57999 18.29998  -11.05638 1.000 51.94931  ? 145 ASP   A N   1 
ATOM   1201 C CA  . ASP   A 1 148 ? 30.86103 17.34024  -10.22366 1.000 52.72719  ? 145 ASP   A CA  1 
ATOM   1202 C C   . ASP   A 1 148 ? 30.03571 16.37412  -11.06512 1.000 46.71755  ? 145 ASP   A C   1 
ATOM   1203 O O   . ASP   A 1 148 ? 28.84079 16.59469  -11.28816 1.000 51.02927  ? 145 ASP   A O   1 
ATOM   1204 C CB  . ASP   A 1 148 ? 29.96612 18.05921  -9.20937  1.000 45.76452  ? 145 ASP   A CB  1 
ATOM   1205 C CG  . ASP   A 1 148 ? 29.54922 17.15794  -8.05961  1.000 69.40994  ? 145 ASP   A CG  1 
ATOM   1206 O OD1 . ASP   A 1 148 ? 29.88544 15.95450  -8.09175  1.000 63.21453  ? 145 ASP   A OD1 1 
ATOM   1207 O OD2 . ASP   A 1 148 ? 28.89266 17.65294  -7.11940  1.000 63.24699  ? 145 ASP   A OD2 1 
ATOM   1208 N N   . PHE   A 1 149 ? 30.66870 15.29757  -11.53063 1.000 48.74254  ? 146 PHE   A N   1 
ATOM   1209 C CA  . PHE   A 1 149 ? 29.99730 14.24249  -12.27570 1.000 50.65840  ? 146 PHE   A CA  1 
ATOM   1210 C C   . PHE   A 1 149 ? 29.67684 13.03256  -11.40346 1.000 47.97493  ? 146 PHE   A C   1 
ATOM   1211 O O   . PHE   A 1 149 ? 29.53726 11.91992  -11.92259 1.000 49.51708  ? 146 PHE   A O   1 
ATOM   1212 C CB  . PHE   A 1 149 ? 30.84723 13.82333  -13.47638 1.000 44.83154  ? 146 PHE   A CB  1 
ATOM   1213 C CG  . PHE   A 1 149 ? 30.74127 14.75553  -14.65207 1.000 53.61757  ? 146 PHE   A CG  1 
ATOM   1214 C CD1 . PHE   A 1 149 ? 31.33580 16.00680  -14.62144 1.000 48.75867  ? 146 PHE   A CD1 1 
ATOM   1215 C CD2 . PHE   A 1 149 ? 30.05075 14.37600  -15.79168 1.000 45.34059  ? 146 PHE   A CD2 1 
ATOM   1216 C CE1 . PHE   A 1 149 ? 31.23860 16.86310  -15.70484 1.000 45.25594  ? 146 PHE   A CE1 1 
ATOM   1217 C CE2 . PHE   A 1 149 ? 29.95173 15.22715  -16.87626 1.000 44.07372  ? 146 PHE   A CE2 1 
ATOM   1218 C CZ  . PHE   A 1 149 ? 30.54704 16.47180  -16.83189 1.000 44.93943  ? 146 PHE   A CZ  1 
ATOM   1219 N N   . GLY   A 1 150 ? 29.55673 13.22936  -10.08816 1.000 46.62227  ? 147 GLY   A N   1 
ATOM   1220 C CA  . GLY   A 1 150 ? 29.24537 12.12007  -9.20267  1.000 46.25349  ? 147 GLY   A CA  1 
ATOM   1221 C C   . GLY   A 1 150 ? 27.84901 11.56582  -9.39901  1.000 54.76272  ? 147 GLY   A C   1 
ATOM   1222 O O   . GLY   A 1 150 ? 27.61253 10.37582  -9.16901  1.000 58.86094  ? 147 GLY   A O   1 
ATOM   1223 N N   . LEU   A 1 151 ? 26.90832 12.40878  -9.82059  1.000 44.47593  ? 148 LEU   A N   1 
ATOM   1224 C CA  . LEU   A 1 151 ? 25.54509 11.98207  -10.10126 1.000 47.57702  ? 148 LEU   A CA  1 
ATOM   1225 C C   . LEU   A 1 151 ? 25.32401 11.67096  -11.57493 1.000 41.23800  ? 148 LEU   A C   1 
ATOM   1226 O O   . LEU   A 1 151 ? 24.18848 11.40137  -11.97898 1.000 45.83384  ? 148 LEU   A O   1 
ATOM   1227 C CB  . LEU   A 1 151 ? 24.55105 13.04686  -9.63638  1.000 51.48061  ? 148 LEU   A CB  1 
ATOM   1228 C CG  . LEU   A 1 151 ? 24.48813 13.27532  -8.12491  1.000 60.26670  ? 148 LEU   A CG  1 
ATOM   1229 C CD1 . LEU   A 1 151 ? 23.42835 14.30728  -7.77816  1.000 62.07439  ? 148 LEU   A CD1 1 
ATOM   1230 C CD2 . LEU   A 1 151 ? 24.22191 11.96613  -7.39837  1.000 60.37203  ? 148 LEU   A CD2 1 
ATOM   1231 N N   . ALA   A 1 152 ? 26.37939 11.70125  -12.38157 1.000 40.88957  ? 149 ALA   A N   1 
ATOM   1232 C CA  . ALA   A 1 152 ? 26.26084 11.44740  -13.80636 1.000 42.10540  ? 149 ALA   A CA  1 
ATOM   1233 C C   . ALA   A 1 152 ? 26.10270 9.95358   -14.07861 1.000 42.21855  ? 149 ALA   A C   1 
ATOM   1234 O O   . ALA   A 1 152 ? 26.41369 9.10321   -13.23978 1.000 45.77290  ? 149 ALA   A O   1 
ATOM   1235 C CB  . ALA   A 1 152 ? 27.48121 11.99266  -14.54946 1.000 39.18519  ? 149 ALA   A CB  1 
ATOM   1236 N N   . ARG   A 1 153 ? 25.60455 9.64042   -15.27305 1.000 46.28981  ? 150 ARG   A N   1 
ATOM   1237 C CA  . ARG   A 1 153 ? 25.45682 8.25751   -15.70286 1.000 47.09742  ? 150 ARG   A CA  1 
ATOM   1238 C C   . ARG   A 1 153 ? 25.48552 8.19955   -17.22186 1.000 52.66000  ? 150 ARG   A C   1 
ATOM   1239 O O   . ARG   A 1 153 ? 24.84572 9.01386   -17.89348 1.000 47.56268  ? 150 ARG   A O   1 
ATOM   1240 C CB  . ARG   A 1 153 ? 24.15422 7.62994   -15.18790 1.000 58.29284  ? 150 ARG   A CB  1 
ATOM   1241 C CG  . ARG   A 1 153 ? 23.91199 6.22188   -15.72185 1.000 70.81497  ? 150 ARG   A CG  1 
ATOM   1242 C CD  . ARG   A 1 153 ? 22.48190 5.75539   -15.49630 1.000 68.19952  ? 150 ARG   A CD  1 
ATOM   1243 N NE  . ARG   A 1 153 ? 22.33298 4.98432   -14.26749 1.000 88.72234  ? 150 ARG   A NE  1 
ATOM   1244 C CZ  . ARG   A 1 153 ? 22.45777 3.66589   -14.19142 1.000 83.57948  ? 150 ARG   A CZ  1 
ATOM   1245 N NH1 . ARG   A 1 153 ? 22.75144 2.93677   -15.25563 1.000 75.07663  ? 150 ARG   A NH1 1 
ATOM   1246 N NH2 . ARG   A 1 153 ? 22.28248 3.06342   -13.01826 1.000 69.88703  ? 150 ARG   A NH2 1 
ATOM   1247 N N   . ALA   A 1 154 ? 26.23460 7.23865   -17.75558 1.000 48.19936  ? 151 ALA   A N   1 
ATOM   1248 C CA  . ALA   A 1 154 ? 26.17442 6.96093   -19.18267 1.000 53.78798  ? 151 ALA   A CA  1 
ATOM   1249 C C   . ALA   A 1 154 ? 24.88852 6.20953   -19.49736 1.000 50.94102  ? 151 ALA   A C   1 
ATOM   1250 O O   . ALA   A 1 154 ? 24.53189 5.25430   -18.80120 1.000 63.77324  ? 151 ALA   A O   1 
ATOM   1251 C CB  . ALA   A 1 154 ? 27.39101 6.14878   -19.62284 1.000 50.30673  ? 151 ALA   A CB  1 
ATOM   1252 N N   . PHE   A 1 155 ? 24.18165 6.64501   -20.53577 1.000 55.51641  ? 152 PHE   A N   1 
ATOM   1253 C CA  . PHE   A 1 155 ? 22.93460 6.01126   -20.93523 1.000 51.98370  ? 152 PHE   A CA  1 
ATOM   1254 C C   . PHE   A 1 155 ? 23.14617 5.19427   -22.20122 1.000 64.47291  ? 152 PHE   A C   1 
ATOM   1255 O O   . PHE   A 1 155 ? 23.90557 5.59086   -23.09106 1.000 58.83512  ? 152 PHE   A O   1 
ATOM   1256 C CB  . PHE   A 1 155 ? 21.81464 7.04219   -21.14404 1.000 56.61220  ? 152 PHE   A CB  1 
ATOM   1257 C CG  . PHE   A 1 155 ? 22.04034 7.98780   -22.29714 1.000 61.05961  ? 152 PHE   A CG  1 
ATOM   1258 C CD1 . PHE   A 1 155 ? 21.62367 7.65979   -23.57964 1.000 51.68219  ? 152 PHE   A CD1 1 
ATOM   1259 C CD2 . PHE   A 1 155 ? 22.63168 9.22111   -22.09009 1.000 54.17298  ? 152 PHE   A CD2 1 
ATOM   1260 C CE1 . PHE   A 1 155 ? 21.81822 8.53199   -24.63399 1.000 54.42120  ? 152 PHE   A CE1 1 
ATOM   1261 C CE2 . PHE   A 1 155 ? 22.82088 10.10187  -23.13822 1.000 58.39440  ? 152 PHE   A CE2 1 
ATOM   1262 C CZ  . PHE   A 1 155 ? 22.41715 9.75472   -24.41402 1.000 58.84504  ? 152 PHE   A CZ  1 
ATOM   1263 N N   . GLY   A 1 156 ? 22.47656 4.04636   -22.26832 1.000 58.13470  ? 153 GLY   A N   1 
ATOM   1264 C CA  . GLY   A 1 156 ? 22.54537 3.21199   -23.44497 1.000 72.68484  ? 153 GLY   A CA  1 
ATOM   1265 C C   . GLY   A 1 156 ? 21.58013 3.65854   -24.52296 1.000 75.66286  ? 153 GLY   A C   1 
ATOM   1266 O O   . GLY   A 1 156 ? 20.76119 4.55790   -24.33817 1.000 70.94566  ? 153 GLY   A O   1 
ATOM   1267 N N   . VAL   A 1 157 ? 21.69249 3.01370   -25.67539 1.000 78.07775  ? 154 VAL   A N   1 
ATOM   1268 C CA  . VAL   A 1 157 ? 20.83276 3.27201   -26.82087 1.000 72.58566  ? 154 VAL   A CA  1 
ATOM   1269 C C   . VAL   A 1 157 ? 20.14877 1.96539   -27.20215 1.000 82.14741  ? 154 VAL   A C   1 
ATOM   1270 O O   . VAL   A 1 157 ? 20.74198 1.11087   -27.85972 1.000 78.78343  ? 154 VAL   A O   1 
ATOM   1271 C CB  . VAL   A 1 157 ? 21.62876 3.84889   -28.00572 1.000 79.55513  ? 154 VAL   A CB  1 
ATOM   1272 C CG1 . VAL   A 1 157 ? 20.70238 4.14573   -29.17337 1.000 64.15130  ? 154 VAL   A CG1 1 
ATOM   1273 C CG2 . VAL   A 1 157 ? 22.38050 5.10324   -27.58257 1.000 66.25861  ? 154 VAL   A CG2 1 
ATOM   1274 N N   . PRO   A 1 158 ? 18.88605 1.77082   -26.80237 1.000 79.10325  ? 155 PRO   A N   1 
ATOM   1275 C CA  . PRO   A 1 158 ? 18.02106 2.68985   -26.05206 1.000 73.88342  ? 155 PRO   A CA  1 
ATOM   1276 C C   . PRO   A 1 158 ? 18.31361 2.68543   -24.55598 1.000 81.32548  ? 155 PRO   A C   1 
ATOM   1277 O O   . PRO   A 1 158 ? 19.01848 1.81452   -24.05223 1.000 63.87877  ? 155 PRO   A O   1 
ATOM   1278 C CB  . PRO   A 1 158 ? 16.62140 2.14847   -26.35761 1.000 76.62462  ? 155 PRO   A CB  1 
ATOM   1279 C CG  . PRO   A 1 158 ? 16.83744 0.66545   -26.45556 1.000 80.37459  ? 155 PRO   A CG  1 
ATOM   1280 C CD  . PRO   A 1 158 ? 18.19472 0.50387   -27.10486 1.000 85.37085  ? 155 PRO   A CD  1 
ATOM   1281 N N   . VAL   A 1 159 ? 17.77665 3.65844   -23.82243 1.000 68.80372  ? 156 VAL   A N   1 
ATOM   1282 C CA  . VAL   A 1 159 ? 17.97727 3.73973   -22.38092 1.000 72.42766  ? 156 VAL   A CA  1 
ATOM   1283 C C   . VAL   A 1 159 ? 17.05029 2.74860   -21.69290 1.000 71.47045  ? 156 VAL   A C   1 
ATOM   1284 O O   . VAL   A 1 159 ? 16.17744 2.14922   -22.33086 1.000 71.56713  ? 156 VAL   A O   1 
ATOM   1285 C CB  . VAL   A 1 159 ? 17.72988 5.16738   -21.85958 1.000 60.79308  ? 156 VAL   A CB  1 
ATOM   1286 C CG1 . VAL   A 1 159 ? 18.46331 6.18452   -22.71687 1.000 61.84355  ? 156 VAL   A CG1 1 
ATOM   1287 C CG2 . VAL   A 1 159 ? 16.23657 5.46680   -21.82076 1.000 67.45834  ? 156 VAL   A CG2 1 
ATOM   1288 N N   . ARG   A 1 160 ? 17.23826 2.56661   -20.38969 1.000 68.07696  ? 157 ARG   A N   1 
ATOM   1289 C CA  . ARG   A 1 160 ? 16.31550 1.81436   -19.55386 1.000 70.60553  ? 157 ARG   A CA  1 
ATOM   1290 C C   . ARG   A 1 160 ? 15.99154 2.65468   -18.32405 1.000 64.70310  ? 157 ARG   A C   1 
ATOM   1291 O O   . ARG   A 1 160 ? 16.43801 3.79884   -18.19423 1.000 64.64572  ? 157 ARG   A O   1 
ATOM   1292 C CB  . ARG   A 1 160 ? 16.89251 0.44569   -19.16561 1.000 71.16803  ? 157 ARG   A CB  1 
ATOM   1293 C CG  . ARG   A 1 160 ? 17.98052 0.48812   -18.10588 1.000 73.36496  ? 157 ARG   A CG  1 
ATOM   1294 C CD  . ARG   A 1 160 ? 18.33927 -0.91623  -17.64470 1.000 80.16068  ? 157 ARG   A CD  1 
ATOM   1295 N NE  . ARG   A 1 160 ? 19.08959 -0.90869  -16.39488 1.000 84.85737  ? 157 ARG   A NE  1 
ATOM   1296 C CZ  . ARG   A 1 160 ? 20.41276 -0.90020  -16.31379 1.000 82.94356  ? 157 ARG   A CZ  1 
ATOM   1297 N NH1 . ARG   A 1 160 ? 21.17163 -0.90113  -17.39741 1.000 78.69068  ? 157 ARG   A NH1 1 
ATOM   1298 N NH2 . ARG   A 1 160 ? 20.98912 -0.89150  -15.11500 1.000 68.47338  ? 157 ARG   A NH2 1 
ATOM   1299 N N   . THR   A 1 161 ? 15.20354 2.08420   -17.41631 1.000 63.28702  ? 158 THR   A N   1 
ATOM   1300 C CA  . THR   A 1 161 ? 14.79059 2.80565   -16.21879 1.000 61.44100  ? 158 THR   A CA  1 
ATOM   1301 C C   . THR   A 1 161 ? 15.99783 3.07398   -15.32684 1.000 75.06628  ? 158 THR   A C   1 
ATOM   1302 O O   . THR   A 1 161 ? 16.62350 2.13867   -14.81610 1.000 64.95189  ? 158 THR   A O   1 
ATOM   1303 C CB  . THR   A 1 161 ? 13.72994 2.01201   -15.46096 1.000 58.36704  ? 158 THR   A CB  1 
ATOM   1304 O OG1 . THR   A 1 161 ? 12.60695 1.77514   -16.31861 1.000 76.57370  ? 158 THR   A OG1 1 
ATOM   1305 C CG2 . THR   A 1 161 ? 13.26791 2.78320   -14.23303 1.000 69.06637  ? 158 THR   A CG2 1 
ATOM   1306 N N   . TYR   A 1 162 ? 16.32321 4.34967   -15.14132 1.000 63.33898  ? 159 TYR   A N   1 
ATOM   1307 C CA  . TYR   A 1 162 ? 17.45607 4.74205   -14.31039 1.000 61.35876  ? 159 TYR   A CA  1 
ATOM   1308 C C   . TYR   A 1 162 ? 16.98183 5.25502   -12.95231 1.000 64.54002  ? 159 TYR   A C   1 
ATOM   1309 O O   . TYR   A 1 162 ? 15.79949 5.15388   -12.62406 1.000 60.86988  ? 159 TYR   A O   1 
ATOM   1310 C CB  . TYR   A 1 162 ? 18.29657 5.80513   -15.02183 1.000 68.83226  ? 159 TYR   A CB  1 
ATOM   1311 C CG  . TYR   A 1 162 ? 18.89469 5.33211   -16.32934 1.000 56.10276  ? 159 TYR   A CG  1 
ATOM   1312 C CD1 . TYR   A 1 162 ? 19.27631 4.00738   -16.50145 1.000 65.29316  ? 159 TYR   A CD1 1 
ATOM   1313 C CD2 . TYR   A 1 162 ? 19.07076 6.20728   -17.39315 1.000 69.09704  ? 159 TYR   A CD2 1 
ATOM   1314 C CE1 . TYR   A 1 162 ? 19.82136 3.56837   -17.69411 1.000 62.49757  ? 159 TYR   A CE1 1 
ATOM   1315 C CE2 . TYR   A 1 162 ? 19.61437 5.77721   -18.59099 1.000 59.75935  ? 159 TYR   A CE2 1 
ATOM   1316 C CZ  . TYR   A 1 162 ? 19.98782 4.45658   -18.73534 1.000 70.29106  ? 159 TYR   A CZ  1 
ATOM   1317 O OH  . TYR   A 1 162 ? 20.52917 4.02038   -19.92333 1.000 60.51284  ? 159 TYR   A OH  1 
HETATM 1318 N N   . TPO   A 1 163 ? 17.90920 5.80261   -12.17031 1.000 61.65149  ? 160 TPO   A N   1 
HETATM 1319 C CA  . TPO   A 1 163 ? 17.60724 6.27614   -10.82062 1.000 66.39033  ? 160 TPO   A CA  1 
HETATM 1320 C CB  . TPO   A 1 163 ? 18.88418 6.75352   -10.09683 1.000 67.35148  ? 160 TPO   A CB  1 
HETATM 1321 C CG2 . TPO   A 1 163 ? 18.58474 7.27904   -8.69607  1.000 61.97279  ? 160 TPO   A CG2 1 
HETATM 1322 O OG1 . TPO   A 1 163 ? 19.78404 5.67719   -10.01727 1.000 62.45256  ? 160 TPO   A OG1 1 
HETATM 1323 P P   . TPO   A 1 163 ? 21.26739 5.77595   -10.87458 1.000 61.37165  ? 160 TPO   A P   1 
HETATM 1324 O O1P . TPO   A 1 163 ? 21.87049 4.41547   -10.54364 1.000 67.14007  ? 160 TPO   A O1P 1 
HETATM 1325 O O2P . TPO   A 1 163 ? 20.86397 5.96921   -12.33474 1.000 52.96497  ? 160 TPO   A O2P 1 
HETATM 1326 O O3P . TPO   A 1 163 ? 22.00626 6.97333   -10.27739 1.000 55.83321  ? 160 TPO   A O3P 1 
HETATM 1327 C C   . TPO   A 1 163 ? 16.58378 7.40944   -10.83078 1.000 61.59169  ? 160 TPO   A C   1 
HETATM 1328 O O   . TPO   A 1 163 ? 16.70803 8.36664   -11.59525 1.000 61.75155  ? 160 TPO   A O   1 
ATOM   1329 N N   . HIS   A 1 164 ? 15.57183 7.28889   -9.97680  1.000 57.91032  ? 161 HIS   A N   1 
ATOM   1330 C CA  . HIS   A 1 164 ? 14.51895 8.29283   -9.88051  1.000 78.45772  ? 161 HIS   A CA  1 
ATOM   1331 C C   . HIS   A 1 164 ? 14.91300 9.43348   -8.94549  1.000 79.37256  ? 161 HIS   A C   1 
ATOM   1332 O O   . HIS   A 1 164 ? 15.84722 9.30307   -8.15285  1.000 65.55553  ? 161 HIS   A O   1 
ATOM   1333 C CB  . HIS   A 1 164 ? 13.21465 7.65529   -9.39468  1.000 74.22059  ? 161 HIS   A CB  1 
ATOM   1334 C CG  . HIS   A 1 164 ? 13.22501 7.28840   -7.94236  1.000 88.61976  ? 161 HIS   A CG  1 
ATOM   1335 N ND1 . HIS   A 1 164 ? 14.36563 6.88176   -7.28349  1.000 90.32600  ? 161 HIS   A ND1 1 
ATOM   1336 C CD2 . HIS   A 1 164 ? 12.23382 7.27537   -7.01978  1.000 91.07200  ? 161 HIS   A CD2 1 
ATOM   1337 C CE1 . HIS   A 1 164 ? 14.07595 6.63044   -6.01932  1.000 96.88223  ? 161 HIS   A CE1 1 
ATOM   1338 N NE2 . HIS   A 1 164 ? 12.78889 6.86133   -5.83324  1.000 89.74547  ? 161 HIS   A NE2 1 
ATOM   1339 N N   . GLU   A 1 165 ? 14.18437 10.54720  -9.05063  1.000 80.02046  ? 162 GLU   A N   1 
ATOM   1340 C CA  . GLU   A 1 165 ? 14.35700 11.70548  -8.17121  1.000 79.09121  ? 162 GLU   A CA  1 
ATOM   1341 C C   . GLU   A 1 165 ? 15.79157 12.23199  -8.21410  1.000 72.57339  ? 162 GLU   A C   1 
ATOM   1342 O O   . GLU   A 1 165 ? 16.42829 12.46165  -7.18365  1.000 90.05182  ? 162 GLU   A O   1 
ATOM   1343 C CB  . GLU   A 1 165 ? 13.93453 11.37350  -6.73762  1.000 75.44087  ? 162 GLU   A CB  1 
ATOM   1344 C CG  . GLU   A 1 165 ? 12.50632 10.86778  -6.61926  1.000 73.14352  ? 162 GLU   A CG  1 
ATOM   1345 C CD  . GLU   A 1 165 ? 12.07182 10.67653  -5.17993  1.000 102.38793 ? 162 GLU   A CD  1 
ATOM   1346 O OE1 . GLU   A 1 165 ? 12.61621 11.37091  -4.29581  1.000 103.14945 ? 162 GLU   A OE1 1 
ATOM   1347 O OE2 . GLU   A 1 165 ? 11.18796 9.82923   -4.93256  1.000 100.66168 ? 162 GLU   A OE2 1 
ATOM   1348 N N   . VAL   A 1 166 ? 16.29995 12.42442  -9.42917  1.000 62.42067  ? 163 VAL   A N   1 
ATOM   1349 C CA  . VAL   A 1 166 ? 17.62655 12.99610  -9.62719  1.000 61.48537  ? 163 VAL   A CA  1 
ATOM   1350 C C   . VAL   A 1 166 ? 17.49517 14.50535  -9.78103  1.000 58.76500  ? 163 VAL   A C   1 
ATOM   1351 O O   . VAL   A 1 166 ? 16.37929 15.03564  -9.83960  1.000 65.20057  ? 163 VAL   A O   1 
ATOM   1352 C CB  . VAL   A 1 166 ? 18.32963 12.36991  -10.84556 1.000 52.78327  ? 163 VAL   A CB  1 
ATOM   1353 C CG1 . VAL   A 1 166 ? 18.70060 10.92309  -10.55658 1.000 70.00990  ? 163 VAL   A CG1 1 
ATOM   1354 C CG2 . VAL   A 1 166 ? 17.43651 12.45593  -12.07317 1.000 44.43083  ? 163 VAL   A CG2 1 
ATOM   1355 N N   . VAL   A 1 167 ? 18.63760 15.19730  -9.84075  1.000 47.91504  ? 164 VAL   A N   1 
ATOM   1356 C CA  . VAL   A 1 167 ? 18.73604 16.64788  -10.01096 1.000 60.15886  ? 164 VAL   A CA  1 
ATOM   1357 C C   . VAL   A 1 167 ? 18.22864 17.37291  -8.76827  1.000 49.76890  ? 164 VAL   A C   1 
ATOM   1358 O O   . VAL   A 1 167 ? 17.19866 17.00437  -8.19288  1.000 46.29385  ? 164 VAL   A O   1 
ATOM   1359 C CB  . VAL   A 1 167 ? 17.98682 17.13148  -11.27004 1.000 58.17741  ? 164 VAL   A CB  1 
ATOM   1360 C CG1 . VAL   A 1 167 ? 18.27075 18.60338  -11.52089 1.000 58.78350  ? 164 VAL   A CG1 1 
ATOM   1361 C CG2 . VAL   A 1 167 ? 18.37090 16.29772  -12.48788 1.000 54.60376  ? 164 VAL   A CG2 1 
ATOM   1362 N N   . THR   A 1 168 ? 18.95716 18.40666  -8.34614  1.000 51.42359  ? 165 THR   A N   1 
ATOM   1363 C CA  . THR   A 1 168 ? 18.50913 19.25337  -7.24788  1.000 47.95439  ? 165 THR   A CA  1 
ATOM   1364 C C   . THR   A 1 168 ? 17.14039 19.84785  -7.57216  1.000 59.00371  ? 165 THR   A C   1 
ATOM   1365 O O   . THR   A 1 168 ? 16.80203 20.08341  -8.73584  1.000 55.44998  ? 165 THR   A O   1 
ATOM   1366 C CB  . THR   A 1 168 ? 19.53821 20.35851  -6.98325  1.000 55.97692  ? 165 THR   A CB  1 
ATOM   1367 O OG1 . THR   A 1 168 ? 20.83528 19.76825  -6.82596  1.000 58.47183  ? 165 THR   A OG1 1 
ATOM   1368 C CG2 . THR   A 1 168 ? 19.19977 21.14029  -5.71865  1.000 54.21350  ? 165 THR   A CG2 1 
ATOM   1369 N N   . LEU   A 1 169 ? 16.35060 20.08974  -6.52109  1.000 46.30016  ? 166 LEU   A N   1 
ATOM   1370 C CA  . LEU   A 1 169 ? 14.92184 20.34928  -6.69036  1.000 49.37593  ? 166 LEU   A CA  1 
ATOM   1371 C C   . LEU   A 1 169 ? 14.65928 21.56642  -7.57317  1.000 54.25873  ? 166 LEU   A C   1 
ATOM   1372 O O   . LEU   A 1 169 ? 13.81321 21.51894  -8.47394  1.000 46.49955  ? 166 LEU   A O   1 
ATOM   1373 C CB  . LEU   A 1 169 ? 14.26209 20.52485  -5.32366  1.000 46.28858  ? 166 LEU   A CB  1 
ATOM   1374 C CG  . LEU   A 1 169 ? 12.73845 20.65248  -5.33199  1.000 55.14592  ? 166 LEU   A CG  1 
ATOM   1375 C CD1 . LEU   A 1 169 ? 12.10281 19.42983  -5.97829  1.000 56.10732  ? 166 LEU   A CD1 1 
ATOM   1376 C CD2 . LEU   A 1 169 ? 12.21209 20.85150  -3.92059  1.000 48.71108  ? 166 LEU   A CD2 1 
ATOM   1377 N N   . TRP   A 1 170 ? 15.37132 22.67018  -7.32822  1.000 42.02476  ? 167 TRP   A N   1 
ATOM   1378 C CA  . TRP   A 1 170 ? 15.10585 23.90459  -8.06277  1.000 46.74897  ? 167 TRP   A CA  1 
ATOM   1379 C C   . TRP   A 1 170 ? 15.35479 23.76589  -9.55870  1.000 46.12996  ? 167 TRP   A C   1 
ATOM   1380 O O   . TRP   A 1 170 ? 14.79832 24.54143  -10.34350 1.000 45.87890  ? 167 TRP   A O   1 
ATOM   1381 C CB  . TRP   A 1 170 ? 15.96231 25.04620  -7.51574  1.000 42.87744  ? 167 TRP   A CB  1 
ATOM   1382 C CG  . TRP   A 1 170 ? 15.54488 25.53599  -6.16812  1.000 48.06679  ? 167 TRP   A CG  1 
ATOM   1383 C CD1 . TRP   A 1 170 ? 14.58351 25.00315  -5.36025  1.000 46.60431  ? 167 TRP   A CD1 1 
ATOM   1384 C CD2 . TRP   A 1 170 ? 16.07470 26.66794  -5.47096  1.000 38.74893  ? 167 TRP   A CD2 1 
ATOM   1385 N NE1 . TRP   A 1 170 ? 14.48432 25.73280  -4.19904  1.000 51.97685  ? 167 TRP   A NE1 1 
ATOM   1386 C CE2 . TRP   A 1 170 ? 15.38996 26.76057  -4.24347  1.000 47.75527  ? 167 TRP   A CE2 1 
ATOM   1387 C CE3 . TRP   A 1 170 ? 17.06403 27.61171  -5.76520  1.000 49.09426  ? 167 TRP   A CE3 1 
ATOM   1388 C CZ2 . TRP   A 1 170 ? 15.66186 27.75952  -3.31204  1.000 49.89070  ? 167 TRP   A CZ2 1 
ATOM   1389 C CZ3 . TRP   A 1 170 ? 17.33207 28.60171  -4.83932  1.000 51.13419  ? 167 TRP   A CZ3 1 
ATOM   1390 C CH2 . TRP   A 1 170 ? 16.63374 28.66807  -3.62802  1.000 55.06833  ? 167 TRP   A CH2 1 
ATOM   1391 N N   . TYR   A 1 171 ? 16.17276 22.80070  -9.97183  1.000 38.93772  ? 168 TYR   A N   1 
ATOM   1392 C CA  . TYR   A 1 171 ? 16.55166 22.63711  -11.36784 1.000 42.80658  ? 168 TYR   A CA  1 
ATOM   1393 C C   . TYR   A 1 171 ? 16.07428 21.30621  -11.93623 1.000 42.29860  ? 168 TYR   A C   1 
ATOM   1394 O O   . TYR   A 1 171 ? 16.54097 20.88112  -12.99815 1.000 42.63713  ? 168 TYR   A O   1 
ATOM   1395 C CB  . TYR   A 1 171 ? 18.06704 22.79057  -11.50497 1.000 43.14548  ? 168 TYR   A CB  1 
ATOM   1396 C CG  . TYR   A 1 171 ? 18.57465 24.04907  -10.83468 1.000 48.14298  ? 168 TYR   A CG  1 
ATOM   1397 C CD1 . TYR   A 1 171 ? 18.60240 25.25782  -11.51758 1.000 44.28248  ? 168 TYR   A CD1 1 
ATOM   1398 C CD2 . TYR   A 1 171 ? 18.99626 24.03470  -9.51047  1.000 44.36772  ? 168 TYR   A CD2 1 
ATOM   1399 C CE1 . TYR   A 1 171 ? 19.04855 26.41220  -10.90708 1.000 50.10502  ? 168 TYR   A CE1 1 
ATOM   1400 C CE2 . TYR   A 1 171 ? 19.44339 25.18682  -8.88955  1.000 44.97996  ? 168 TYR   A CE2 1 
ATOM   1401 C CZ  . TYR   A 1 171 ? 19.46542 26.37255  -9.59205  1.000 46.94084  ? 168 TYR   A CZ  1 
ATOM   1402 O OH  . TYR   A 1 171 ? 19.91193 27.52283  -8.98244  1.000 47.03718  ? 168 TYR   A OH  1 
ATOM   1403 N N   . ARG   A 1 172 ? 15.13709 20.65398  -11.25313 1.000 38.99423  ? 169 ARG   A N   1 
ATOM   1404 C CA  . ARG   A 1 172 ? 14.62998 19.35081  -11.65638 1.000 42.93061  ? 169 ARG   A CA  1 
ATOM   1405 C C   . ARG   A 1 172 ? 13.53001 19.51811  -12.69793 1.000 43.31298  ? 169 ARG   A C   1 
ATOM   1406 O O   . ARG   A 1 172 ? 12.61464 20.32924  -12.52150 1.000 41.21714  ? 169 ARG   A O   1 
ATOM   1407 C CB  . ARG   A 1 172 ? 14.10151 18.58811  -10.44098 1.000 42.63753  ? 169 ARG   A CB  1 
ATOM   1408 C CG  . ARG   A 1 172 ? 13.70447 17.15119  -10.72593 1.000 44.48988  ? 169 ARG   A CG  1 
ATOM   1409 C CD  . ARG   A 1 172 ? 13.25446 16.45936  -9.45079  1.000 47.19912  ? 169 ARG   A CD  1 
ATOM   1410 N NE  . ARG   A 1 172 ? 14.25221 16.56660  -8.39296  1.000 47.27659  ? 169 ARG   A NE  1 
ATOM   1411 C CZ  . ARG   A 1 172 ? 14.05846 16.17817  -7.13987  1.000 47.53781  ? 169 ARG   A CZ  1 
ATOM   1412 N NH1 . ARG   A 1 172 ? 12.91228 15.64349  -6.75146  1.000 39.39868  ? 169 ARG   A NH1 1 
ATOM   1413 N NH2 . ARG   A 1 172 ? 15.03765 16.33393  -6.25338  1.000 53.02809  ? 169 ARG   A NH2 1 
ATOM   1414 N N   . ALA   A 1 173 ? 13.62072 18.74079  -13.77371 1.000 48.51188  ? 170 ALA   A N   1 
ATOM   1415 C CA  . ALA   A 1 173 ? 12.67499 18.85320  -14.87087 1.000 40.09650  ? 170 ALA   A CA  1 
ATOM   1416 C C   . ALA   A 1 173 ? 11.29691 18.33845  -14.45164 1.000 48.10296  ? 170 ALA   A C   1 
ATOM   1417 O O   . ALA   A 1 173 ? 11.18587 17.49178  -13.56075 1.000 46.23636  ? 170 ALA   A O   1 
ATOM   1418 C CB  . ALA   A 1 173 ? 13.18176 18.07473  -16.08250 1.000 41.81213  ? 170 ALA   A CB  1 
ATOM   1419 N N   . PRO   A 1 174 ? 10.22674 18.83742  -15.07971 1.000 44.90976  ? 171 PRO   A N   1 
ATOM   1420 C CA  . PRO   A 1 174 ? 8.87937  18.40933  -14.66865 1.000 46.75810  ? 171 PRO   A CA  1 
ATOM   1421 C C   . PRO   A 1 174 ? 8.59817  16.93865  -14.92236 1.000 45.05876  ? 171 PRO   A C   1 
ATOM   1422 O O   . PRO   A 1 174 ? 7.78539  16.34682  -14.20071 1.000 49.23253  ? 171 PRO   A O   1 
ATOM   1423 C CB  . PRO   A 1 174 ? 7.95614  19.31365  -15.49888 1.000 51.82402  ? 171 PRO   A CB  1 
ATOM   1424 C CG  . PRO   A 1 174 ? 8.78138  19.72259  -16.67062 1.000 43.17373  ? 171 PRO   A CG  1 
ATOM   1425 C CD  . PRO   A 1 174 ? 10.18023 19.84834  -16.14995 1.000 48.81698  ? 171 PRO   A CD  1 
ATOM   1426 N N   . GLU   A 1 175 ? 9.23860  16.32344  -15.92151 1.000 47.76748  ? 172 GLU   A N   1 
ATOM   1427 C CA  . GLU   A 1 175 ? 9.00510  14.90158  -16.15526 1.000 52.34260  ? 172 GLU   A CA  1 
ATOM   1428 C C   . GLU   A 1 175 ? 9.54360  14.05214  -15.01106 1.000 51.06708  ? 172 GLU   A C   1 
ATOM   1429 O O   . GLU   A 1 175 ? 8.98507  12.98970  -14.71534 1.000 49.93890  ? 172 GLU   A O   1 
ATOM   1430 C CB  . GLU   A 1 175 ? 9.62124  14.46086  -17.48523 1.000 49.85078  ? 172 GLU   A CB  1 
ATOM   1431 C CG  . GLU   A 1 175 ? 11.13264 14.59855  -17.57971 1.000 43.08941  ? 172 GLU   A CG  1 
ATOM   1432 C CD  . GLU   A 1 175 ? 11.56241 15.91771  -18.18807 1.000 42.80115  ? 172 GLU   A CD  1 
ATOM   1433 O OE1 . GLU   A 1 175 ? 10.78517 16.89278  -18.11370 1.000 46.04845  ? 172 GLU   A OE1 1 
ATOM   1434 O OE2 . GLU   A 1 175 ? 12.67850 15.97773  -18.74629 1.000 40.46689  ? 172 GLU   A OE2 1 
ATOM   1435 N N   . ILE   A 1 176 ? 10.61249 14.50327  -14.35093 1.000 43.90576  ? 173 ILE   A N   1 
ATOM   1436 C CA  . ILE   A 1 176 ? 11.10446 13.79299  -13.17541 1.000 43.46777  ? 173 ILE   A CA  1 
ATOM   1437 C C   . ILE   A 1 176 ? 10.14572 13.97575  -12.00562 1.000 49.08983  ? 173 ILE   A C   1 
ATOM   1438 O O   . ILE   A 1 176 ? 9.87173  13.03107  -11.25489 1.000 51.33236  ? 173 ILE   A O   1 
ATOM   1439 C CB  . ILE   A 1 176 ? 12.52626 14.26488  -12.82293 1.000 41.70158  ? 173 ILE   A CB  1 
ATOM   1440 C CG1 . ILE   A 1 176 ? 13.45697 14.09850  -14.02571 1.000 40.59903  ? 173 ILE   A CG1 1 
ATOM   1441 C CG2 . ILE   A 1 176 ? 13.06420 13.49567  -11.62462 1.000 44.50918  ? 173 ILE   A CG2 1 
ATOM   1442 C CD1 . ILE   A 1 176 ? 14.87739 14.53968  -13.75629 1.000 62.89518  ? 173 ILE   A CD1 1 
ATOM   1443 N N   . LEU   A 1 177 ? 9.61359  15.18983  -11.83659 1.000 44.44132  ? 174 LEU   A N   1 
ATOM   1444 C CA  . LEU   A 1 177 ? 8.68529  15.45196  -10.74060 1.000 46.73759  ? 174 LEU   A CA  1 
ATOM   1445 C C   . LEU   A 1 177 ? 7.38441  14.67363  -10.89781 1.000 55.35953  ? 174 LEU   A C   1 
ATOM   1446 O O   . LEU   A 1 177 ? 6.71620  14.37987  -9.89974  1.000 51.93947  ? 174 LEU   A O   1 
ATOM   1447 C CB  . LEU   A 1 177 ? 8.39692  16.95029  -10.64923 1.000 53.65328  ? 174 LEU   A CB  1 
ATOM   1448 C CG  . LEU   A 1 177 ? 9.57168  17.85075  -10.26513 1.000 48.26904  ? 174 LEU   A CG  1 
ATOM   1449 C CD1 . LEU   A 1 177 ? 9.26125  19.30144  -10.59286 1.000 44.83947  ? 174 LEU   A CD1 1 
ATOM   1450 C CD2 . LEU   A 1 177 ? 9.89391  17.69301  -8.78653  1.000 56.67749  ? 174 LEU   A CD2 1 
ATOM   1451 N N   . LEU   A 1 178 ? 7.00734  14.33625  -12.12910 1.000 51.06542  ? 175 LEU   A N   1 
ATOM   1452 C CA  . LEU   A 1 178 ? 5.79262  13.57623  -12.39052 1.000 54.03688  ? 175 LEU   A CA  1 
ATOM   1453 C C   . LEU   A 1 178 ? 6.02863  12.07145  -12.42962 1.000 59.18399  ? 175 LEU   A C   1 
ATOM   1454 O O   . LEU   A 1 178 ? 5.07750  11.31580  -12.65530 1.000 64.92115  ? 175 LEU   A O   1 
ATOM   1455 C CB  . LEU   A 1 178 ? 5.15467  14.03816  -13.70499 1.000 56.79196  ? 175 LEU   A CB  1 
ATOM   1456 C CG  . LEU   A 1 178 ? 4.52115  15.43050  -13.66359 1.000 63.91503  ? 175 LEU   A CG  1 
ATOM   1457 C CD1 . LEU   A 1 178 ? 3.98958  15.82984  -15.02994 1.000 64.90064  ? 175 LEU   A CD1 1 
ATOM   1458 C CD2 . LEU   A 1 178 ? 3.41290  15.47354  -12.62505 1.000 51.91391  ? 175 LEU   A CD2 1 
ATOM   1459 N N   . GLY   A 1 179 ? 7.26350  11.62109  -12.22056 1.000 62.04694  ? 176 GLY   A N   1 
ATOM   1460 C CA  . GLY   A 1 179 ? 7.55271  10.20356  -12.12303 1.000 59.49574  ? 176 GLY   A CA  1 
ATOM   1461 C C   . GLY   A 1 179 ? 7.62599  9.47240   -13.44770 1.000 54.92666  ? 176 GLY   A C   1 
ATOM   1462 O O   . GLY   A 1 179 ? 7.03166  8.40163   -13.59990 1.000 63.92833  ? 176 GLY   A O   1 
ATOM   1463 N N   . CYS   A 1 180 ? 8.35657  10.02880  -14.41022 1.000 50.40969  ? 177 CYS   A N   1 
ATOM   1464 C CA  . CYS   A 1 180 ? 8.51006  9.37163   -15.70088 1.000 54.16515  ? 177 CYS   A CA  1 
ATOM   1465 C C   . CYS   A 1 180 ? 9.33497  8.09744   -15.55874 1.000 59.23175  ? 177 CYS   A C   1 
ATOM   1466 O O   . CYS   A 1 180 ? 10.26637 8.02555   -14.75172 1.000 57.28871  ? 177 CYS   A O   1 
ATOM   1467 C CB  . CYS   A 1 180 ? 9.17083  10.31533  -16.70521 1.000 51.16934  ? 177 CYS   A CB  1 
ATOM   1468 S SG  . CYS   A 1 180 ? 10.82774 10.86612  -16.23383 1.000 65.26643  ? 177 CYS   A SG  1 
ATOM   1469 N N   . LYS   A 1 181 ? 8.98590  7.08457   -16.35494 1.000 61.12225  ? 178 LYS   A N   1 
ATOM   1470 C CA  . LYS   A 1 181 ? 9.70212  5.81401   -16.29416 1.000 56.34783  ? 178 LYS   A CA  1 
ATOM   1471 C C   . LYS   A 1 181 ? 11.08172 5.92972   -16.93255 1.000 62.34502  ? 178 LYS   A C   1 
ATOM   1472 O O   . LYS   A 1 181 ? 12.07734 5.45210   -16.37579 1.000 64.83101  ? 178 LYS   A O   1 
ATOM   1473 C CB  . LYS   A 1 181 ? 8.88167  4.71623   -16.97319 1.000 74.42621  ? 178 LYS   A CB  1 
ATOM   1474 C CG  . LYS   A 1 181 ? 9.51343  3.33402   -16.90597 1.000 75.51175  ? 178 LYS   A CG  1 
ATOM   1475 C CD  . LYS   A 1 181 ? 8.70453  2.31491   -17.69406 1.000 83.58386  ? 178 LYS   A CD  1 
ATOM   1476 C CE  . LYS   A 1 181 ? 7.30089  2.16160   -17.13117 1.000 97.66431  ? 178 LYS   A CE  1 
ATOM   1477 N NZ  . LYS   A 1 181 ? 7.31069  1.62302   -15.74297 1.000 102.31156 ? 178 LYS   A NZ  1 
ATOM   1478 N N   . TYR   A 1 182 ? 11.16069 6.56009   -18.10109 1.000 57.83144  ? 179 TYR   A N   1 
ATOM   1479 C CA  . TYR   A 1 182 ? 12.41775 6.75258   -18.80596 1.000 57.74253  ? 179 TYR   A CA  1 
ATOM   1480 C C   . TYR   A 1 182 ? 12.71792 8.23950   -18.93324 1.000 64.47300  ? 179 TYR   A C   1 
ATOM   1481 O O   . TYR   A 1 182 ? 11.80744 9.07181   -18.98903 1.000 62.31319  ? 179 TYR   A O   1 
ATOM   1482 C CB  . TYR   A 1 182 ? 12.38607 6.11940   -20.20544 1.000 61.89885  ? 179 TYR   A CB  1 
ATOM   1483 C CG  . TYR   A 1 182 ? 11.97672 4.66326   -20.23369 1.000 65.76621  ? 179 TYR   A CG  1 
ATOM   1484 C CD1 . TYR   A 1 182 ? 12.80458 3.67626   -19.71395 1.000 64.01868  ? 179 TYR   A CD1 1 
ATOM   1485 C CD2 . TYR   A 1 182 ? 10.77022 4.27402   -20.80089 1.000 64.28002  ? 179 TYR   A CD2 1 
ATOM   1486 C CE1 . TYR   A 1 182 ? 12.43495 2.34328   -19.74596 1.000 68.48566  ? 179 TYR   A CE1 1 
ATOM   1487 C CE2 . TYR   A 1 182 ? 10.39274 2.94449   -20.83859 1.000 68.42979  ? 179 TYR   A CE2 1 
ATOM   1488 C CZ  . TYR   A 1 182 ? 11.22822 1.98358   -20.30998 1.000 77.44656  ? 179 TYR   A CZ  1 
ATOM   1489 O OH  . TYR   A 1 182 ? 10.85407 0.65964   -20.34648 1.000 67.29706  ? 179 TYR   A OH  1 
ATOM   1490 N N   . TYR   A 1 183 ? 14.00706 8.56508   -18.97978 1.000 56.10315  ? 180 TYR   A N   1 
ATOM   1491 C CA  . TYR   A 1 183 ? 14.44107 9.93336   -19.22212 1.000 63.46550  ? 180 TYR   A CA  1 
ATOM   1492 C C   . TYR   A 1 183 ? 15.84798 9.89907   -19.79672 1.000 54.21639  ? 180 TYR   A C   1 
ATOM   1493 O O   . TYR   A 1 183 ? 16.57326 8.91160   -19.65144 1.000 54.76762  ? 180 TYR   A O   1 
ATOM   1494 C CB  . TYR   A 1 183 ? 14.39118 10.78484  -17.94554 1.000 66.04610  ? 180 TYR   A CB  1 
ATOM   1495 C CG  . TYR   A 1 183 ? 15.34204 10.35155  -16.84809 1.000 57.32593  ? 180 TYR   A CG  1 
ATOM   1496 C CD1 . TYR   A 1 183 ? 16.66007 10.79531  -16.82540 1.000 52.39396  ? 180 TYR   A CD1 1 
ATOM   1497 C CD2 . TYR   A 1 183 ? 14.91598 9.51747   -15.82322 1.000 57.78285  ? 180 TYR   A CD2 1 
ATOM   1498 C CE1 . TYR   A 1 183 ? 17.52830 10.40729  -15.82433 1.000 57.43532  ? 180 TYR   A CE1 1 
ATOM   1499 C CE2 . TYR   A 1 183 ? 15.77857 9.12582   -14.81405 1.000 52.34413  ? 180 TYR   A CE2 1 
ATOM   1500 C CZ  . TYR   A 1 183 ? 17.08216 9.57397   -14.82007 1.000 52.73384  ? 180 TYR   A CZ  1 
ATOM   1501 O OH  . TYR   A 1 183 ? 17.94405 9.18779   -13.81983 1.000 57.06502  ? 180 TYR   A OH  1 
ATOM   1502 N N   . SER   A 1 184 ? 16.22537 10.99530  -20.45294 1.000 48.73279  ? 181 SER   A N   1 
ATOM   1503 C CA  . SER   A 1 184 ? 17.56622 11.10257  -21.01303 1.000 58.16283  ? 181 SER   A CA  1 
ATOM   1504 C C   . SER   A 1 184 ? 18.06042 12.54378  -21.00456 1.000 54.67505  ? 181 SER   A C   1 
ATOM   1505 O O   . SER   A 1 184 ? 18.04158 13.20927  -19.96423 1.000 53.20142  ? 181 SER   A O   1 
ATOM   1506 C CB  . SER   A 1 184 ? 17.60343 10.53773  -22.43623 1.000 62.78867  ? 181 SER   A CB  1 
ATOM   1507 O OG  . SER   A 1 184 ? 16.79724 11.30128  -23.31568 1.000 69.98669  ? 181 SER   A OG  1 
ATOM   1508 N N   . THR   A 1 185 ? 18.48964 13.03492  -22.16917 1.000 46.10649  ? 182 THR   A N   1 
ATOM   1509 C CA  . THR   A 1 185 ? 19.22959 14.29012  -22.24213 1.000 49.61507  ? 182 THR   A CA  1 
ATOM   1510 C C   . THR   A 1 185 ? 18.37568 15.51434  -21.93884 1.000 39.98623  ? 182 THR   A C   1 
ATOM   1511 O O   . THR   A 1 185 ? 18.93121 16.57408  -21.63105 1.000 51.13958  ? 182 THR   A O   1 
ATOM   1512 C CB  . THR   A 1 185 ? 19.85929 14.44007  -23.62669 1.000 46.01125  ? 182 THR   A CB  1 
ATOM   1513 O OG1 . THR   A 1 185 ? 18.83356 14.39266  -24.62643 1.000 51.73052  ? 182 THR   A OG1 1 
ATOM   1514 C CG2 . THR   A 1 185 ? 20.85365 13.31863  -23.87764 1.000 43.98880  ? 182 THR   A CG2 1 
ATOM   1515 N N   . ALA   A 1 186 ? 17.04829 15.39993  -22.01355 1.000 43.87187  ? 183 ALA   A N   1 
ATOM   1516 C CA  . ALA   A 1 186 ? 16.20060 16.57597  -21.84199 1.000 40.86328  ? 183 ALA   A CA  1 
ATOM   1517 C C   . ALA   A 1 186 ? 16.27952 17.14221  -20.42847 1.000 46.07371  ? 183 ALA   A C   1 
ATOM   1518 O O   . ALA   A 1 186 ? 16.01157 18.33259  -20.22588 1.000 43.94447  ? 183 ALA   A O   1 
ATOM   1519 C CB  . ALA   A 1 186 ? 14.75244 16.23796  -22.19319 1.000 40.84008  ? 183 ALA   A CB  1 
ATOM   1520 N N   . VAL   A 1 187 ? 16.64379 16.31870  -19.44127 1.000 42.82355  ? 184 VAL   A N   1 
ATOM   1521 C CA  . VAL   A 1 187 ? 16.66289 16.80253  -18.06326 1.000 48.12506  ? 184 VAL   A CA  1 
ATOM   1522 C C   . VAL   A 1 187 ? 17.80014 17.79586  -17.84736 1.000 44.13000  ? 184 VAL   A C   1 
ATOM   1523 O O   . VAL   A 1 187 ? 17.67117 18.72887  -17.04595 1.000 43.10940  ? 184 VAL   A O   1 
ATOM   1524 C CB  . VAL   A 1 187 ? 16.73771 15.62026  -17.07680 1.000 50.25646  ? 184 VAL   A CB  1 
ATOM   1525 C CG1 . VAL   A 1 187 ? 15.56994 14.67122  -17.30332 1.000 47.76592  ? 184 VAL   A CG1 1 
ATOM   1526 C CG2 . VAL   A 1 187 ? 18.06215 14.88239  -17.20526 1.000 48.46852  ? 184 VAL   A CG2 1 
ATOM   1527 N N   . ASP   A 1 188 ? 18.91872 17.63123  -18.55824 1.000 42.50771  ? 185 ASP   A N   1 
ATOM   1528 C CA  . ASP   A 1 188 ? 20.01830 18.58209  -18.42790 1.000 42.05676  ? 185 ASP   A CA  1 
ATOM   1529 C C   . ASP   A 1 188 ? 19.68549 19.90786  -19.10035 1.000 46.99518  ? 185 ASP   A C   1 
ATOM   1530 O O   . ASP   A 1 188 ? 20.09622 20.97246  -18.62317 1.000 42.73868  ? 185 ASP   A O   1 
ATOM   1531 C CB  . ASP   A 1 188 ? 21.29891 17.99320  -19.01806 1.000 47.16067  ? 185 ASP   A CB  1 
ATOM   1532 C CG  . ASP   A 1 188 ? 21.87036 16.87355  -18.17322 1.000 44.53502  ? 185 ASP   A CG  1 
ATOM   1533 O OD1 . ASP   A 1 188 ? 21.56649 16.82184  -16.96220 1.000 40.25382  ? 185 ASP   A OD1 1 
ATOM   1534 O OD2 . ASP   A 1 188 ? 22.63145 16.04873  -18.72029 1.000 44.58116  ? 185 ASP   A OD2 1 
ATOM   1535 N N   . ILE   A 1 189 ? 18.94730 19.86252  -20.21169 1.000 41.56602  ? 186 ILE   A N   1 
ATOM   1536 C CA  . ILE   A 1 189 ? 18.57441 21.08875  -20.90899 1.000 36.14130  ? 186 ILE   A CA  1 
ATOM   1537 C C   . ILE   A 1 189 ? 17.63604 21.92956  -20.05191 1.000 44.09552  ? 186 ILE   A C   1 
ATOM   1538 O O   . ILE   A 1 189 ? 17.75118 23.16100  -20.00886 1.000 41.97922  ? 186 ILE   A O   1 
ATOM   1539 C CB  . ILE   A 1 189 ? 17.95177 20.75207  -22.27550 1.000 41.70830  ? 186 ILE   A CB  1 
ATOM   1540 C CG1 . ILE   A 1 189 ? 18.99919 20.11991  -23.19402 1.000 50.83025  ? 186 ILE   A CG1 1 
ATOM   1541 C CG2 . ILE   A 1 189 ? 17.35880 21.99623  -22.91615 1.000 43.19216  ? 186 ILE   A CG2 1 
ATOM   1542 C CD1 . ILE   A 1 189 ? 20.10695 21.06710  -23.59364 1.000 42.93075  ? 186 ILE   A CD1 1 
ATOM   1543 N N   . TRP   A 1 190 ? 16.69600 21.28362  -19.35607 1.000 37.04779  ? 187 TRP   A N   1 
ATOM   1544 C CA  . TRP   A 1 190 ? 15.81043 22.01444  -18.45523 1.000 43.74846  ? 187 TRP   A CA  1 
ATOM   1545 C C   . TRP   A 1 190 ? 16.60781 22.74948  -17.38596 1.000 41.19170  ? 187 TRP   A C   1 
ATOM   1546 O O   . TRP   A 1 190 ? 16.36791 23.93295  -17.11993 1.000 40.96247  ? 187 TRP   A O   1 
ATOM   1547 C CB  . TRP   A 1 190 ? 14.80379 21.05875  -17.81371 1.000 41.42273  ? 187 TRP   A CB  1 
ATOM   1548 C CG  . TRP   A 1 190 ? 13.88944 21.73119  -16.83170 1.000 36.75730  ? 187 TRP   A CG  1 
ATOM   1549 C CD1 . TRP   A 1 190 ? 14.14091 21.97670  -15.51092 1.000 39.59298  ? 187 TRP   A CD1 1 
ATOM   1550 C CD2 . TRP   A 1 190 ? 12.57821 22.24746  -17.09174 1.000 43.36488  ? 187 TRP   A CD2 1 
ATOM   1551 N NE1 . TRP   A 1 190 ? 13.06899 22.61405  -14.93533 1.000 40.28981  ? 187 TRP   A NE1 1 
ATOM   1552 C CE2 . TRP   A 1 190 ? 12.09641 22.79163  -15.88378 1.000 40.16802  ? 187 TRP   A CE2 1 
ATOM   1553 C CE3 . TRP   A 1 190 ? 11.76502 22.30220  -18.22758 1.000 52.34568  ? 187 TRP   A CE3 1 
ATOM   1554 C CZ2 . TRP   A 1 190 ? 10.83996 23.38153  -15.78000 1.000 39.16579  ? 187 TRP   A CZ2 1 
ATOM   1555 C CZ3 . TRP   A 1 190 ? 10.51680 22.88893  -18.12142 1.000 47.79651  ? 187 TRP   A CZ3 1 
ATOM   1556 C CH2 . TRP   A 1 190 ? 10.06719 23.42016  -16.90667 1.000 47.25203  ? 187 TRP   A CH2 1 
ATOM   1557 N N   . SER   A 1 191 ? 17.56375 22.05738  -16.76030 1.000 38.95125  ? 188 SER   A N   1 
ATOM   1558 C CA  . SER   A 1 191 ? 18.39338 22.69040  -15.74054 1.000 39.85308  ? 188 SER   A CA  1 
ATOM   1559 C C   . SER   A 1 191 ? 19.13646 23.89366  -16.30412 1.000 42.27108  ? 188 SER   A C   1 
ATOM   1560 O O   . SER   A 1 191 ? 19.22078 24.94058  -15.65254 1.000 44.21510  ? 188 SER   A O   1 
ATOM   1561 C CB  . SER   A 1 191 ? 19.38183 21.67772  -15.16019 1.000 39.44142  ? 188 SER   A CB  1 
ATOM   1562 O OG  . SER   A 1 191 ? 18.70644 20.55474  -14.62393 1.000 44.31458  ? 188 SER   A OG  1 
ATOM   1563 N N   . LEU   A 1 192 ? 19.67211 23.76946  -17.52035 1.000 37.04851  ? 189 LEU   A N   1 
ATOM   1564 C CA  . LEU   A 1 192 ? 20.39011 24.88953  -18.11796 1.000 42.42726  ? 189 LEU   A CA  1 
ATOM   1565 C C   . LEU   A 1 192 ? 19.44767 26.04636  -18.42687 1.000 40.15571  ? 189 LEU   A C   1 
ATOM   1566 O O   . LEU   A 1 192 ? 19.83735 27.21533  -18.32137 1.000 43.56182  ? 189 LEU   A O   1 
ATOM   1567 C CB  . LEU   A 1 192 ? 21.12512 24.43058  -19.37717 1.000 42.93291  ? 189 LEU   A CB  1 
ATOM   1568 C CG  . LEU   A 1 192 ? 22.60188 24.82003  -19.45940 1.000 63.65357  ? 189 LEU   A CG  1 
ATOM   1569 C CD1 . LEU   A 1 192 ? 23.34182 24.38441  -18.20266 1.000 59.95452  ? 189 LEU   A CD1 1 
ATOM   1570 C CD2 . LEU   A 1 192 ? 23.24397 24.21502  -20.69776 1.000 57.76066  ? 189 LEU   A CD2 1 
ATOM   1571 N N   . GLY   A 1 193 ? 18.20361 25.74247  -18.80249 1.000 40.84727  ? 190 GLY   A N   1 
ATOM   1572 C CA  . GLY   A 1 193 ? 17.22462 26.79958  -18.99724 1.000 42.39830  ? 190 GLY   A CA  1 
ATOM   1573 C C   . GLY   A 1 193 ? 16.91277 27.54453  -17.71287 1.000 47.76667  ? 190 GLY   A C   1 
ATOM   1574 O O   . GLY   A 1 193 ? 16.75329 28.76783  -17.71560 1.000 41.55008  ? 190 GLY   A O   1 
ATOM   1575 N N   . CYS   A 1 194 ? 16.82157 26.81682  -16.59638 1.000 40.02128  ? 191 CYS   A N   1 
ATOM   1576 C CA  . CYS   A 1 194 ? 16.64568 27.46908  -15.30246 1.000 42.52482  ? 191 CYS   A CA  1 
ATOM   1577 C C   . CYS   A 1 194 ? 17.85062 28.33441  -14.95747 1.000 46.34561  ? 191 CYS   A C   1 
ATOM   1578 O O   . CYS   A 1 194 ? 17.69927 29.43929  -14.42286 1.000 44.33322  ? 191 CYS   A O   1 
ATOM   1579 C CB  . CYS   A 1 194 ? 16.41167 26.42318  -14.21198 1.000 43.02219  ? 191 CYS   A CB  1 
ATOM   1580 S SG  . CYS   A 1 194 ? 14.90617 25.44711  -14.40626 1.000 43.34541  ? 191 CYS   A SG  1 
ATOM   1581 N N   . ILE   A 1 195 ? 19.05686 27.84406  -15.25243 1.000 44.55554  ? 192 ILE   A N   1 
ATOM   1582 C CA  . ILE   A 1 195 ? 20.26605 28.61540  -14.98449 1.000 49.24848  ? 192 ILE   A CA  1 
ATOM   1583 C C   . ILE   A 1 195 ? 20.33260 29.83412  -15.89546 1.000 52.35810  ? 192 ILE   A C   1 
ATOM   1584 O O   . ILE   A 1 195 ? 20.75108 30.91933  -15.47360 1.000 49.57272  ? 192 ILE   A O   1 
ATOM   1585 C CB  . ILE   A 1 195 ? 21.50780 27.71731  -15.13603 1.000 50.02943  ? 192 ILE   A CB  1 
ATOM   1586 C CG1 . ILE   A 1 195 ? 21.47414 26.59213  -14.09808 1.000 42.85283  ? 192 ILE   A CG1 1 
ATOM   1587 C CG2 . ILE   A 1 195 ? 22.78604 28.53223  -15.00243 1.000 46.89405  ? 192 ILE   A CG2 1 
ATOM   1588 C CD1 . ILE   A 1 195 ? 22.55511 25.55235  -14.28584 1.000 49.23143  ? 192 ILE   A CD1 1 
ATOM   1589 N N   . PHE   A 1 196 ? 19.91730 29.67573  -17.15468 1.000 43.05410  ? 193 PHE   A N   1 
ATOM   1590 C CA  . PHE   A 1 196 ? 19.87382 30.79443  -18.09094 1.000 43.68081  ? 193 PHE   A CA  1 
ATOM   1591 C C   . PHE   A 1 196 ? 19.02689 31.93593  -17.53604 1.000 41.79813  ? 193 PHE   A C   1 
ATOM   1592 O O   . PHE   A 1 196 ? 19.48781 33.07799  -17.43046 1.000 48.03520  ? 193 PHE   A O   1 
ATOM   1593 C CB  . PHE   A 1 196 ? 19.33073 30.30591  -19.43884 1.000 41.02921  ? 193 PHE   A CB  1 
ATOM   1594 C CG  . PHE   A 1 196 ? 19.31708 31.35448  -20.52174 1.000 50.13771  ? 193 PHE   A CG  1 
ATOM   1595 C CD1 . PHE   A 1 196 ? 20.14788 32.46343  -20.46176 1.000 56.01570  ? 193 PHE   A CD1 1 
ATOM   1596 C CD2 . PHE   A 1 196 ? 18.46170 31.22477  -21.60539 1.000 50.59721  ? 193 PHE   A CD2 1 
ATOM   1597 C CE1 . PHE   A 1 196 ? 20.12266 33.42261  -21.46217 1.000 54.22701  ? 193 PHE   A CE1 1 
ATOM   1598 C CE2 . PHE   A 1 196 ? 18.43376 32.17870  -22.60660 1.000 49.98872  ? 193 PHE   A CE2 1 
ATOM   1599 C CZ  . PHE   A 1 196 ? 19.26427 33.27763  -22.53427 1.000 44.24786  ? 193 PHE   A CZ  1 
ATOM   1600 N N   . ALA   A 1 197 ? 17.77856 31.63563  -17.16594 1.000 48.94478  ? 194 ALA   A N   1 
ATOM   1601 C CA  . ALA   A 1 197 ? 16.89918 32.66445  -16.61997 1.000 46.93819  ? 194 ALA   A CA  1 
ATOM   1602 C C   . ALA   A 1 197 ? 17.43777 33.22944  -15.31245 1.000 47.75059  ? 194 ALA   A C   1 
ATOM   1603 O O   . ALA   A 1 197 ? 17.24192 34.41517  -15.02236 1.000 52.19994  ? 194 ALA   A O   1 
ATOM   1604 C CB  . ALA   A 1 197 ? 15.49287 32.10106  -16.41203 1.000 52.13971  ? 194 ALA   A CB  1 
ATOM   1605 N N   . GLU   A 1 198 ? 18.12111 32.40496  -14.51442 1.000 45.48287  ? 195 GLU   A N   1 
ATOM   1606 C CA  . GLU   A 1 198 ? 18.65308 32.88853  -13.24408 1.000 50.81093  ? 195 GLU   A CA  1 
ATOM   1607 C C   . GLU   A 1 198 ? 19.77649 33.89574  -13.46287 1.000 60.20898  ? 195 GLU   A C   1 
ATOM   1608 O O   . GLU   A 1 198 ? 19.93121 34.83965  -12.67954 1.000 51.96994  ? 195 GLU   A O   1 
ATOM   1609 C CB  . GLU   A 1 198 ? 19.13287 31.71228  -12.39453 1.000 51.31028  ? 195 GLU   A CB  1 
ATOM   1610 C CG  . GLU   A 1 198 ? 19.38362 32.05563  -10.93346 1.000 45.86254  ? 195 GLU   A CG  1 
ATOM   1611 C CD  . GLU   A 1 198 ? 19.73969 30.83434  -10.10677 1.000 54.23916  ? 195 GLU   A CD  1 
ATOM   1612 O OE1 . GLU   A 1 198 ? 19.29028 29.72427  -10.46461 1.000 46.68758  ? 195 GLU   A OE1 1 
ATOM   1613 O OE2 . GLU   A 1 198 ? 20.47097 30.98086  -9.10495  1.000 48.46676  ? 195 GLU   A OE2 1 
ATOM   1614 N N   . MET   A 1 199 ? 20.56909 33.71504  -14.52289 1.000 47.23242  ? 196 MET   A N   1 
ATOM   1615 C CA  . MET   A 1 199 ? 21.57753 34.71360  -14.86562 1.000 48.85264  ? 196 MET   A CA  1 
ATOM   1616 C C   . MET   A 1 199 ? 20.93056 36.02272  -15.29953 1.000 58.07804  ? 196 MET   A C   1 
ATOM   1617 O O   . MET   A 1 199 ? 21.45199 37.10686  -15.01362 1.000 53.93246  ? 196 MET   A O   1 
ATOM   1618 C CB  . MET   A 1 199 ? 22.49554 34.18624  -15.96990 1.000 57.85756  ? 196 MET   A CB  1 
ATOM   1619 C CG  . MET   A 1 199 ? 23.50027 33.14300  -15.51389 1.000 47.49314  ? 196 MET   A CG  1 
ATOM   1620 S SD  . MET   A 1 199 ? 24.71324 32.73088  -16.78308 1.000 58.01131  ? 196 MET   A SD  1 
ATOM   1621 C CE  . MET   A 1 199 ? 23.69711 31.84249  -17.96145 1.000 45.24701  ? 196 MET   A CE  1 
ATOM   1622 N N   . VAL   A 1 200 ? 19.78880 35.94163  -15.98540 1.000 55.36850  ? 197 VAL   A N   1 
ATOM   1623 C CA  . VAL   A 1 200 ? 19.14113 37.14324  -16.50133 1.000 58.50821  ? 197 VAL   A CA  1 
ATOM   1624 C C   . VAL   A 1 200 ? 18.47252 37.92575  -15.37671 1.000 63.82340  ? 197 VAL   A C   1 
ATOM   1625 O O   . VAL   A 1 200 ? 18.57182 39.15722  -15.31597 1.000 56.22505  ? 197 VAL   A O   1 
ATOM   1626 C CB  . VAL   A 1 200 ? 18.13466 36.76855  -17.60412 1.000 50.24231  ? 197 VAL   A CB  1 
ATOM   1627 C CG1 . VAL   A 1 200 ? 17.41379 38.00712  -18.10975 1.000 58.43092  ? 197 VAL   A CG1 1 
ATOM   1628 C CG2 . VAL   A 1 200 ? 18.83910 36.05172  -18.74484 1.000 51.11212  ? 197 VAL   A CG2 1 
ATOM   1629 N N   . THR   A 1 201 ? 17.78305 37.23245  -14.47258 1.000 55.27206  ? 198 THR   A N   1 
ATOM   1630 C CA  . THR   A 1 201 ? 16.97958 37.87690  -13.44252 1.000 56.69820  ? 198 THR   A CA  1 
ATOM   1631 C C   . THR   A 1 201 ? 17.67149 37.94512  -12.08676 1.000 56.81246  ? 198 THR   A C   1 
ATOM   1632 O O   . THR   A 1 201 ? 17.11102 38.53107  -11.15495 1.000 64.10512  ? 198 THR   A O   1 
ATOM   1633 C CB  . THR   A 1 201 ? 15.63807 37.15066  -13.29272 1.000 63.06921  ? 198 THR   A CB  1 
ATOM   1634 O OG1 . THR   A 1 201 ? 15.86819 35.80162  -12.86679 1.000 62.55675  ? 198 THR   A OG1 1 
ATOM   1635 C CG2 . THR   A 1 201 ? 14.89088 37.13604  -14.61648 1.000 57.79154  ? 198 THR   A CG2 1 
ATOM   1636 N N   . ARG   A 1 202 ? 18.86489 37.36264  -11.95236 1.000 54.63328  ? 199 ARG   A N   1 
ATOM   1637 C CA  . ARG   A 1 202 ? 19.61025 37.31471  -10.69313 1.000 62.57517  ? 199 ARG   A CA  1 
ATOM   1638 C C   . ARG   A 1 202 ? 18.81885 36.64101  -9.57550  1.000 60.78825  ? 199 ARG   A C   1 
ATOM   1639 O O   . ARG   A 1 202 ? 19.08611 36.87401  -8.39248  1.000 54.41904  ? 199 ARG   A O   1 
ATOM   1640 C CB  . ARG   A 1 202 ? 20.06145 38.71327  -10.24883 1.000 68.19388  ? 199 ARG   A CB  1 
ATOM   1641 C CG  . ARG   A 1 202 ? 21.12371 39.34668  -11.13744 1.000 80.47138  ? 199 ARG   A CG  1 
ATOM   1642 C CD  . ARG   A 1 202 ? 20.50853 40.11799  -12.29454 1.000 72.28173  ? 199 ARG   A CD  1 
ATOM   1643 N NE  . ARG   A 1 202 ? 20.71023 41.55555  -12.15843 1.000 72.26838  ? 199 ARG   A NE  1 
ATOM   1644 C CZ  . ARG   A 1 202 ? 19.86869 42.37789  -11.54717 1.000 81.53260  ? 199 ARG   A CZ  1 
ATOM   1645 N NH1 . ARG   A 1 202 ? 18.74600 41.93884  -11.00226 1.000 96.94866  ? 199 ARG   A NH1 1 
ATOM   1646 N NH2 . ARG   A 1 202 ? 20.16104 43.67379  -11.48112 1.000 90.93141  ? 199 ARG   A NH2 1 
ATOM   1647 N N   . ARG   A 1 203 ? 17.85099 35.80025  -9.93211  1.000 52.93819  ? 200 ARG   A N   1 
ATOM   1648 C CA  . ARG   A 1 203 ? 17.00158 35.12664  -8.96186  1.000 59.13423  ? 200 ARG   A CA  1 
ATOM   1649 C C   . ARG   A 1 203 ? 16.61925 33.76533  -9.52215  1.000 58.87293  ? 200 ARG   A C   1 
ATOM   1650 O O   . ARG   A 1 203 ? 16.42456 33.62247  -10.73229 1.000 55.64738  ? 200 ARG   A O   1 
ATOM   1651 C CB  . ARG   A 1 203 ? 15.74812 35.95634  -8.65084  1.000 62.97456  ? 200 ARG   A CB  1 
ATOM   1652 C CG  . ARG   A 1 203 ? 14.78256 35.30501  -7.67235  1.000 85.04770  ? 200 ARG   A CG  1 
ATOM   1653 C CD  . ARG   A 1 203 ? 13.56519 36.18145  -7.40426  1.000 90.15971  ? 200 ARG   A CD  1 
ATOM   1654 N NE  . ARG   A 1 203 ? 12.80358 36.46436  -8.61574  1.000 104.06273 ? 200 ARG   A NE  1 
ATOM   1655 C CZ  . ARG   A 1 203 ? 12.82300 37.62307  -9.26067  1.000 95.30227  ? 200 ARG   A CZ  1 
ATOM   1656 N NH1 . ARG   A 1 203 ? 13.55061 38.64108  -8.83099  1.000 102.34065 ? 200 ARG   A NH1 1 
ATOM   1657 N NH2 . ARG   A 1 203 ? 12.09227 37.76466  -10.36290 1.000 83.21979  ? 200 ARG   A NH2 1 
ATOM   1658 N N   . ALA   A 1 204 ? 16.52720 32.77011  -8.64097  1.000 52.11036  ? 201 ALA   A N   1 
ATOM   1659 C CA  . ALA   A 1 204 ? 16.15115 31.42889  -9.06761  1.000 54.38117  ? 201 ALA   A CA  1 
ATOM   1660 C C   . ALA   A 1 204 ? 14.77896 31.44613  -9.72892  1.000 50.21115  ? 201 ALA   A C   1 
ATOM   1661 O O   . ALA   A 1 204 ? 13.85224 32.11398  -9.26162  1.000 48.95053  ? 201 ALA   A O   1 
ATOM   1662 C CB  . ALA   A 1 204 ? 16.15288 30.46919  -7.87690  1.000 44.15859  ? 201 ALA   A CB  1 
ATOM   1663 N N   . LEU   A 1 205 ? 14.65464 30.70341  -10.83012 1.000 45.22847  ? 202 LEU   A N   1 
ATOM   1664 C CA  . LEU   A 1 205 ? 13.41784 30.72770  -11.60486 1.000 41.16258  ? 202 LEU   A CA  1 
ATOM   1665 C C   . LEU   A 1 205 ? 12.29357 30.00209  -10.87455 1.000 45.21564  ? 202 LEU   A C   1 
ATOM   1666 O O   . LEU   A 1 205 ? 11.18475 30.53229  -10.74069 1.000 52.01490  ? 202 LEU   A O   1 
ATOM   1667 C CB  . LEU   A 1 205 ? 13.65716 30.11494  -12.98628 1.000 43.13835  ? 202 LEU   A CB  1 
ATOM   1668 C CG  . LEU   A 1 205 ? 12.51838 30.17386  -14.00651 1.000 56.75805  ? 202 LEU   A CG  1 
ATOM   1669 C CD1 . LEU   A 1 205 ? 12.05729 31.60719  -14.22859 1.000 47.98799  ? 202 LEU   A CD1 1 
ATOM   1670 C CD2 . LEU   A 1 205 ? 12.95860 29.54259  -15.31938 1.000 47.27692  ? 202 LEU   A CD2 1 
ATOM   1671 N N   . PHE   A 1 206 ? 12.55921 28.78780  -10.39250 1.000 44.31259  ? 203 PHE   A N   1 
ATOM   1672 C CA  . PHE   A 1 206 ? 11.56370 27.97231  -9.69529  1.000 46.11157  ? 203 PHE   A CA  1 
ATOM   1673 C C   . PHE   A 1 206 ? 12.12930 27.53644  -8.34956  1.000 48.24616  ? 203 PHE   A C   1 
ATOM   1674 O O   . PHE   A 1 206 ? 12.60139 26.40101  -8.20041  1.000 47.85663  ? 203 PHE   A O   1 
ATOM   1675 C CB  . PHE   A 1 206 ? 11.15854 26.75465  -10.52802 1.000 45.22450  ? 203 PHE   A CB  1 
ATOM   1676 C CG  . PHE   A 1 206 ? 10.71202 27.08580  -11.92473 1.000 47.10028  ? 203 PHE   A CG  1 
ATOM   1677 C CD1 . PHE   A 1 206 ? 9.60278  27.88607  -12.14355 1.000 52.74781  ? 203 PHE   A CD1 1 
ATOM   1678 C CD2 . PHE   A 1 206 ? 11.38838 26.57244  -13.01964 1.000 46.49956  ? 203 PHE   A CD2 1 
ATOM   1679 C CE1 . PHE   A 1 206 ? 9.18676  28.18295  -13.43006 1.000 49.11962  ? 203 PHE   A CE1 1 
ATOM   1680 C CE2 . PHE   A 1 206 ? 10.97504 26.86259  -14.30867 1.000 45.87564  ? 203 PHE   A CE2 1 
ATOM   1681 C CZ  . PHE   A 1 206 ? 9.87452  27.66965  -14.51295 1.000 51.20079  ? 203 PHE   A CZ  1 
ATOM   1682 N N   . PRO   A 1 207 ? 12.09415 28.41394  -7.33988  1.000 46.93792  ? 204 PRO   A N   1 
ATOM   1683 C CA  . PRO   A 1 207 ? 12.63630 28.06700  -6.00585  1.000 51.64318  ? 204 PRO   A CA  1 
ATOM   1684 C C   . PRO   A 1 207 ? 11.62413 27.37206  -5.09334  1.000 61.39871  ? 204 PRO   A C   1 
ATOM   1685 O O   . PRO   A 1 207 ? 11.05841 27.94353  -4.15959  1.000 60.59313  ? 204 PRO   A O   1 
ATOM   1686 C CB  . PRO   A 1 207 ? 13.04832 29.43124  -5.45147  1.000 50.06915  ? 204 PRO   A CB  1 
ATOM   1687 C CG  . PRO   A 1 207 ? 12.04157 30.37075  -6.04246  1.000 51.92489  ? 204 PRO   A CG  1 
ATOM   1688 C CD  . PRO   A 1 207 ? 11.68098 29.82707  -7.41109  1.000 46.34307  ? 204 PRO   A CD  1 
ATOM   1689 N N   . GLY   A 1 208 ? 11.38527 26.08928  -5.36523  1.000 49.90966  ? 205 GLY   A N   1 
ATOM   1690 C CA  . GLY   A 1 208 ? 10.44706 25.32599  -4.57344  1.000 56.14071  ? 205 GLY   A CA  1 
ATOM   1691 C C   . GLY   A 1 208 ? 11.08270 24.68504  -3.35215  1.000 56.16226  ? 205 GLY   A C   1 
ATOM   1692 O O   . GLY   A 1 208 ? 12.28758 24.44393  -3.30432  1.000 53.23873  ? 205 GLY   A O   1 
ATOM   1693 N N   . ASP   A 1 209 ? 10.24344 24.41220  -2.35109  1.000 59.04232  ? 206 ASP   A N   1 
ATOM   1694 C CA  . ASP   A 1 209 ? 10.68344 23.76891  -1.12140  1.000 66.08258  ? 206 ASP   A CA  1 
ATOM   1695 C C   . ASP   A 1 209 ? 10.19744 22.33279  -0.98307  1.000 59.82090  ? 206 ASP   A C   1 
ATOM   1696 O O   . ASP   A 1 209 ? 10.60137 21.64849  -0.03682  1.000 71.06260  ? 206 ASP   A O   1 
ATOM   1697 C CB  . ASP   A 1 209 ? 10.22752 24.58379  0.09996   1.000 55.84483  ? 206 ASP   A CB  1 
ATOM   1698 C CG  . ASP   A 1 209 ? 8.73695  24.86648  0.09454   1.000 70.39518  ? 206 ASP   A CG  1 
ATOM   1699 O OD1 . ASP   A 1 209 ? 8.03443  24.37259  -0.81133  1.000 82.05124  ? 206 ASP   A OD1 1 
ATOM   1700 O OD2 . ASP   A 1 209 ? 8.26659  25.58890  0.99897   1.000 88.67403  ? 206 ASP   A OD2 1 
ATOM   1701 N N   . SER   A 1 210 ? 9.34249  21.86491  -1.88800  1.000 53.76400  ? 207 SER   A N   1 
ATOM   1702 C CA  . SER   A 1 210 ? 8.91588  20.47464  -1.91494  1.000 59.17749  ? 207 SER   A CA  1 
ATOM   1703 C C   . SER   A 1 210 ? 8.70629  20.07767  -3.36776  1.000 59.45437  ? 207 SER   A C   1 
ATOM   1704 O O   . SER   A 1 210 ? 8.77984  20.91023  -4.27392  1.000 52.51545  ? 207 SER   A O   1 
ATOM   1705 C CB  . SER   A 1 210 ? 7.64058  20.25555  -1.09339  1.000 63.95746  ? 207 SER   A CB  1 
ATOM   1706 O OG  . SER   A 1 210 ? 6.52896  20.90128  -1.68986  1.000 67.53936  ? 207 SER   A OG  1 
ATOM   1707 N N   . GLU   A 1 211 ? 8.44533  18.78709  -3.58562  1.000 51.36372  ? 208 GLU   A N   1 
ATOM   1708 C CA  . GLU   A 1 211 ? 8.22208  18.31120  -4.94715  1.000 61.84627  ? 208 GLU   A CA  1 
ATOM   1709 C C   . GLU   A 1 211 ? 6.93980  18.89016  -5.53160  1.000 52.34065  ? 208 GLU   A C   1 
ATOM   1710 O O   . GLU   A 1 211 ? 6.90388  19.26906  -6.70806  1.000 58.88876  ? 208 GLU   A O   1 
ATOM   1711 C CB  . GLU   A 1 211 ? 8.18199  16.78350  -4.97668  1.000 61.85117  ? 208 GLU   A CB  1 
ATOM   1712 C CG  . GLU   A 1 211 ? 9.49410  16.11516  -4.60108  1.000 56.20296  ? 208 GLU   A CG  1 
ATOM   1713 C CD  . GLU   A 1 211 ? 9.46381  14.61404  -4.81753  1.000 91.89682  ? 208 GLU   A CD  1 
ATOM   1714 O OE1 . GLU   A 1 211 ? 8.97413  14.17355  -5.87935  1.000 87.21963  ? 208 GLU   A OE1 1 
ATOM   1715 O OE2 . GLU   A 1 211 ? 9.92375  13.87412  -3.92275  1.000 105.75109 ? 208 GLU   A OE2 1 
ATOM   1716 N N   . ILE   A 1 212 ? 5.87936  18.97272  -4.72569  1.000 54.05953  ? 209 ILE   A N   1 
ATOM   1717 C CA  . ILE   A 1 212 ? 4.61150  19.49267  -5.22699  1.000 57.55278  ? 209 ILE   A CA  1 
ATOM   1718 C C   . ILE   A 1 212 ? 4.67881  21.00786  -5.38736  1.000 61.54633  ? 209 ILE   A C   1 
ATOM   1719 O O   . ILE   A 1 212 ? 4.11842  21.56968  -6.33653  1.000 59.34468  ? 209 ILE   A O   1 
ATOM   1720 C CB  . ILE   A 1 212 ? 3.45324  19.05836  -4.30742  1.000 63.53690  ? 209 ILE   A CB  1 
ATOM   1721 C CG1 . ILE   A 1 212 ? 2.11193  19.52230  -4.87856  1.000 71.23691  ? 209 ILE   A CG1 1 
ATOM   1722 C CG2 . ILE   A 1 212 ? 3.65538  19.56858  -2.88457  1.000 63.87763  ? 209 ILE   A CG2 1 
ATOM   1723 C CD1 . ILE   A 1 212 ? 1.79456  18.92549  -6.23149  1.000 68.25594  ? 209 ILE   A CD1 1 
ATOM   1724 N N   . ASP   A 1 213 ? 5.37219  21.69352  -4.47353  1.000 56.90261  ? 210 ASP   A N   1 
ATOM   1725 C CA  . ASP   A 1 213 ? 5.53265  23.13776  -4.60288  1.000 53.45787  ? 210 ASP   A CA  1 
ATOM   1726 C C   . ASP   A 1 213 ? 6.44364  23.49448  -5.76972  1.000 49.27205  ? 210 ASP   A C   1 
ATOM   1727 O O   . ASP   A 1 213 ? 6.24159  24.52675  -6.41889  1.000 51.86980  ? 210 ASP   A O   1 
ATOM   1728 C CB  . ASP   A 1 213 ? 6.07870  23.72736  -3.30294  1.000 60.54764  ? 210 ASP   A CB  1 
ATOM   1729 C CG  . ASP   A 1 213 ? 6.25742  25.23154  -3.37483  1.000 62.10607  ? 210 ASP   A CG  1 
ATOM   1730 O OD1 . ASP   A 1 213 ? 5.23788  25.95276  -3.40574  1.000 65.55565  ? 210 ASP   A OD1 1 
ATOM   1731 O OD2 . ASP   A 1 213 ? 7.41757  25.69325  -3.40050  1.000 60.29874  ? 210 ASP   A OD2 1 
ATOM   1732 N N   . GLN   A 1 214 ? 7.44719  22.66000  -6.04800  1.000 51.39247  ? 211 GLN   A N   1 
ATOM   1733 C CA  . GLN   A 1 214 ? 8.28982  22.87601  -7.21939  1.000 42.93073  ? 211 GLN   A CA  1 
ATOM   1734 C C   . GLN   A 1 214 ? 7.47839  22.74105  -8.50098  1.000 50.22921  ? 211 GLN   A C   1 
ATOM   1735 O O   . GLN   A 1 214 ? 7.61907  23.54410  -9.43025  1.000 47.89237  ? 211 GLN   A O   1 
ATOM   1736 C CB  . GLN   A 1 214 ? 9.45285  21.88464  -7.21566  1.000 50.26483  ? 211 GLN   A CB  1 
ATOM   1737 C CG  . GLN   A 1 214 ? 10.41664 22.05168  -8.37552  1.000 46.30504  ? 211 GLN   A CG  1 
ATOM   1738 C CD  . GLN   A 1 214 ? 11.29633 23.27447  -8.22493  1.000 56.46711  ? 211 GLN   A CD  1 
ATOM   1739 O OE1 . GLN   A 1 214 ? 11.48348 23.78481  -7.12124  1.000 47.71459  ? 211 GLN   A OE1 1 
ATOM   1740 N NE2 . GLN   A 1 214 ? 11.84437 23.74997  -9.33539  1.000 45.91241  ? 211 GLN   A NE2 1 
ATOM   1741 N N   . LEU   A 1 215 ? 6.61789  21.72327  -8.56349  1.000 51.24213  ? 212 LEU   A N   1 
ATOM   1742 C CA  . LEU   A 1 215 ? 5.79427  21.51312  -9.74838  1.000 51.08802  ? 212 LEU   A CA  1 
ATOM   1743 C C   . LEU   A 1 215 ? 4.80847  22.65807  -9.94503  1.000 58.73357  ? 212 LEU   A C   1 
ATOM   1744 O O   . LEU   A 1 215 ? 4.57278  23.09808  -11.07659 1.000 56.44941  ? 212 LEU   A O   1 
ATOM   1745 C CB  . LEU   A 1 215 ? 5.05663  20.17998  -9.63109  1.000 54.60688  ? 212 LEU   A CB  1 
ATOM   1746 C CG  . LEU   A 1 215 ? 4.38889  19.62808  -10.88871 1.000 61.54709  ? 212 LEU   A CG  1 
ATOM   1747 C CD1 . LEU   A 1 215 ? 5.43305  19.18198  -11.90214 1.000 50.87756  ? 212 LEU   A CD1 1 
ATOM   1748 C CD2 . LEU   A 1 215 ? 3.45138  18.48561  -10.53487 1.000 65.60793  ? 212 LEU   A CD2 1 
ATOM   1749 N N   . PHE   A 1 216 ? 4.22756  23.15968  -8.85229  1.000 50.38105  ? 213 PHE   A N   1 
ATOM   1750 C CA  . PHE   A 1 216 ? 3.25813  24.24422  -8.96492  1.000 56.34732  ? 213 PHE   A CA  1 
ATOM   1751 C C   . PHE   A 1 216 ? 3.92167  25.56271  -9.34111  1.000 56.38642  ? 213 PHE   A C   1 
ATOM   1752 O O   . PHE   A 1 216 ? 3.30456  26.38860  -10.02337 1.000 60.25530  ? 213 PHE   A O   1 
ATOM   1753 C CB  . PHE   A 1 216 ? 2.47704  24.39615  -7.65896  1.000 57.86921  ? 213 PHE   A CB  1 
ATOM   1754 C CG  . PHE   A 1 216 ? 1.41408  23.35186  -7.46102  1.000 58.24680  ? 213 PHE   A CG  1 
ATOM   1755 C CD1 . PHE   A 1 216 ? 1.17435  22.39199  -8.43108  1.000 72.99946  ? 213 PHE   A CD1 1 
ATOM   1756 C CD2 . PHE   A 1 216 ? 0.64417  23.33929  -6.30962  1.000 62.26928  ? 213 PHE   A CD2 1 
ATOM   1757 C CE1 . PHE   A 1 216 ? 0.19432  21.43413  -8.25172  1.000 79.95913  ? 213 PHE   A CE1 1 
ATOM   1758 C CE2 . PHE   A 1 216 ? -0.33793 22.38441  -6.12513  1.000 63.33559  ? 213 PHE   A CE2 1 
ATOM   1759 C CZ  . PHE   A 1 216 ? -0.56335 21.43157  -7.09723  1.000 70.76420  ? 213 PHE   A CZ  1 
ATOM   1760 N N   . ARG   A 1 217 ? 5.16485  25.78552  -8.90578  1.000 49.41702  ? 214 ARG   A N   1 
ATOM   1761 C CA  . ARG   A 1 217 ? 5.87977  26.98543  -9.32936  1.000 51.10977  ? 214 ARG   A CA  1 
ATOM   1762 C C   . ARG   A 1 217 ? 6.15138  26.95842  -10.82738 1.000 48.37460  ? 214 ARG   A C   1 
ATOM   1763 O O   . ARG   A 1 217 ? 6.08866  27.99773  -11.49430 1.000 52.13483  ? 214 ARG   A O   1 
ATOM   1764 C CB  . ARG   A 1 217 ? 7.18457  27.13338  -8.54708  1.000 46.23497  ? 214 ARG   A CB  1 
ATOM   1765 C CG  . ARG   A 1 217 ? 6.98844  27.55518  -7.10103  1.000 58.71601  ? 214 ARG   A CG  1 
ATOM   1766 C CD  . ARG   A 1 217 ? 8.31197  27.87787  -6.43172  1.000 66.20045  ? 214 ARG   A CD  1 
ATOM   1767 N NE  . ARG   A 1 217 ? 8.12771  28.28272  -5.04342  1.000 68.35594  ? 214 ARG   A NE  1 
ATOM   1768 C CZ  . ARG   A 1 217 ? 7.86399  29.52242  -4.65405  1.000 72.82450  ? 214 ARG   A CZ  1 
ATOM   1769 N NH1 . ARG   A 1 217 ? 7.75063  30.51150  -5.52550  1.000 77.56674  ? 214 ARG   A NH1 1 
ATOM   1770 N NH2 . ARG   A 1 217 ? 7.70787  29.77585  -3.35805  1.000 80.71854  ? 214 ARG   A NH2 1 
ATOM   1771 N N   . ILE   A 1 218 ? 6.45397  25.77866  -11.37306 1.000 48.21689  ? 215 ILE   A N   1 
ATOM   1772 C CA  . ILE   A 1 218 ? 6.59551  25.64563  -12.81898 1.000 48.44783  ? 215 ILE   A CA  1 
ATOM   1773 C C   . ILE   A 1 218 ? 5.25625  25.88003  -13.50383 1.000 55.44728  ? 215 ILE   A C   1 
ATOM   1774 O O   . ILE   A 1 218 ? 5.18317  26.53955  -14.54773 1.000 56.85952  ? 215 ILE   A O   1 
ATOM   1775 C CB  . ILE   A 1 218 ? 7.17748  24.26511  -13.17442 1.000 47.45468  ? 215 ILE   A CB  1 
ATOM   1776 C CG1 . ILE   A 1 218 ? 8.54728  24.07501  -12.52251 1.000 44.36848  ? 215 ILE   A CG1 1 
ATOM   1777 C CG2 . ILE   A 1 218 ? 7.27195  24.09538  -14.68537 1.000 53.48849  ? 215 ILE   A CG2 1 
ATOM   1778 C CD1 . ILE   A 1 218 ? 9.09694  22.67069  -12.66152 1.000 39.94669  ? 215 ILE   A CD1 1 
ATOM   1779 N N   . PHE   A 1 219 ? 4.17517  25.35311  -12.92203 1.000 56.68730  ? 216 PHE   A N   1 
ATOM   1780 C CA  . PHE   A 1 219 ? 2.85511  25.51158  -13.52367 1.000 53.57067  ? 216 PHE   A CA  1 
ATOM   1781 C C   . PHE   A 1 219 ? 2.41991  26.97119  -13.52611 1.000 70.00708  ? 216 PHE   A C   1 
ATOM   1782 O O   . PHE   A 1 219 ? 1.78705  27.43567  -14.48100 1.000 61.24738  ? 216 PHE   A O   1 
ATOM   1783 C CB  . PHE   A 1 219 ? 1.82565  24.65783  -12.78138 1.000 57.96642  ? 216 PHE   A CB  1 
ATOM   1784 C CG  . PHE   A 1 219 ? 1.96417  23.17834  -13.01663 1.000 49.53288  ? 216 PHE   A CG  1 
ATOM   1785 C CD1 . PHE   A 1 219 ? 2.97727  22.67071  -13.81265 1.000 47.55734  ? 216 PHE   A CD1 1 
ATOM   1786 C CD2 . PHE   A 1 219 ? 1.06340  22.29442  -12.44448 1.000 52.01218  ? 216 PHE   A CD2 1 
ATOM   1787 C CE1 . PHE   A 1 219 ? 3.09752  21.30968  -14.02201 1.000 53.54498  ? 216 PHE   A CE1 1 
ATOM   1788 C CE2 . PHE   A 1 219 ? 1.17502  20.93468  -12.65383 1.000 52.42055  ? 216 PHE   A CE2 1 
ATOM   1789 C CZ  . PHE   A 1 219 ? 2.19124  20.44157  -13.44633 1.000 53.31659  ? 216 PHE   A CZ  1 
ATOM   1790 N N   . ARG   A 1 220 ? 2.74313  27.71041  -12.46196 1.000 59.01938  ? 217 ARG   A N   1 
ATOM   1791 C CA  . ARG   A 1 220 ? 2.33053  29.10653  -12.37699 1.000 64.60633  ? 217 ARG   A CA  1 
ATOM   1792 C C   . ARG   A 1 220 ? 3.03095  29.98595  -13.40319 1.000 60.98498  ? 217 ARG   A C   1 
ATOM   1793 O O   . ARG   A 1 220 ? 2.51245  31.05577  -13.73860 1.000 75.26137  ? 217 ARG   A O   1 
ATOM   1794 C CB  . ARG   A 1 220 ? 2.58604  29.65299  -10.97116 1.000 64.30337  ? 217 ARG   A CB  1 
ATOM   1795 C CG  . ARG   A 1 220 ? 1.58671  29.18167  -9.93012  1.000 79.77487  ? 217 ARG   A CG  1 
ATOM   1796 C CD  . ARG   A 1 220 ? 1.67056  30.02300  -8.66662  1.000 77.56856  ? 217 ARG   A CD  1 
ATOM   1797 N NE  . ARG   A 1 220 ? 2.84946  29.71604  -7.86549  1.000 97.38745  ? 217 ARG   A NE  1 
ATOM   1798 C CZ  . ARG   A 1 220 ? 2.84121  28.93718  -6.79215  1.000 90.06962  ? 217 ARG   A CZ  1 
ATOM   1799 N NH1 . ARG   A 1 220 ? 1.72774  28.36851  -6.35944  1.000 93.48767  ? 217 ARG   A NH1 1 
ATOM   1800 N NH2 . ARG   A 1 220 ? 3.97761  28.72643  -6.13425  1.000 80.02060  ? 217 ARG   A NH2 1 
ATOM   1801 N N   . THR   A 1 221 ? 4.18723  29.56327  -13.91080 1.000 57.07517  ? 218 THR   A N   1 
ATOM   1802 C CA  . THR   A 1 221 ? 4.95036  30.34913  -14.87220 1.000 55.69347  ? 218 THR   A CA  1 
ATOM   1803 C C   . THR   A 1 221 ? 4.71484  29.90354  -16.31020 1.000 66.60660  ? 218 THR   A C   1 
ATOM   1804 O O   . THR   A 1 221 ? 4.46107  30.73672  -17.18442 1.000 63.77960  ? 218 THR   A O   1 
ATOM   1805 C CB  . THR   A 1 221 ? 6.44579  30.27093  -14.54370 1.000 61.05605  ? 218 THR   A CB  1 
ATOM   1806 O OG1 . THR   A 1 221 ? 6.65615  30.64851  -13.17791 1.000 63.28830  ? 218 THR   A OG1 1 
ATOM   1807 C CG2 . THR   A 1 221 ? 7.24107  31.20033  -15.44865 1.000 64.93448  ? 218 THR   A CG2 1 
ATOM   1808 N N   . LEU   A 1 222 ? 4.79046  28.60116  -16.57289 1.000 58.92604  ? 219 LEU   A N   1 
ATOM   1809 C CA  . LEU   A 1 222 ? 4.64053  28.06399  -17.91732 1.000 57.68328  ? 219 LEU   A CA  1 
ATOM   1810 C C   . LEU   A 1 222 ? 3.23468  27.55665  -18.20513 1.000 59.10158  ? 219 LEU   A C   1 
ATOM   1811 O O   . LEU   A 1 222 ? 2.98422  27.06543  -19.30947 1.000 65.50379  ? 219 LEU   A O   1 
ATOM   1812 C CB  . LEU   A 1 222 ? 5.65047  26.93433  -18.14511 1.000 58.63007  ? 219 LEU   A CB  1 
ATOM   1813 C CG  . LEU   A 1 222 ? 7.11328  27.28243  -17.87768 1.000 50.68108  ? 219 LEU   A CG  1 
ATOM   1814 C CD1 . LEU   A 1 222 ? 7.99165  26.05032  -18.02292 1.000 53.24302  ? 219 LEU   A CD1 1 
ATOM   1815 C CD2 . LEU   A 1 222 ? 7.58332  28.39295  -18.80647 1.000 67.03352  ? 219 LEU   A CD2 1 
ATOM   1816 N N   . GLY   A 1 223 ? 2.32001  27.66532  -17.25605 1.000 56.38272  ? 220 GLY   A N   1 
ATOM   1817 C CA  . GLY   A 1 223 ? 0.99126  27.13014  -17.48247 1.000 55.71252  ? 220 GLY   A CA  1 
ATOM   1818 C C   . GLY   A 1 223 ? 0.89222  25.66311  -17.13179 1.000 52.28200  ? 220 GLY   A C   1 
ATOM   1819 O O   . GLY   A 1 223 ? 1.83253  24.88936  -17.28606 1.000 57.34891  ? 220 GLY   A O   1 
ATOM   1820 N N   . THR   A 1 224 ? -0.27549 25.28188  -16.64083 1.000 54.04197  ? 221 THR   A N   1 
ATOM   1821 C CA  . THR   A 1 224 ? -0.53922 23.88586  -16.33987 1.000 64.50228  ? 221 THR   A CA  1 
ATOM   1822 C C   . THR   A 1 224 ? -0.61729 23.09309  -17.63671 1.000 56.32465  ? 221 THR   A C   1 
ATOM   1823 O O   . THR   A 1 224 ? -1.52010 23.33618  -18.44666 1.000 55.07814  ? 221 THR   A O   1 
ATOM   1824 C CB  . THR   A 1 224 ? -1.83669 23.74072  -15.54956 1.000 62.66695  ? 221 THR   A CB  1 
ATOM   1825 O OG1 . THR   A 1 224 ? -1.73802 24.48903  -14.33241 1.000 67.44823  ? 221 THR   A OG1 1 
ATOM   1826 C CG2 . THR   A 1 224 ? -2.08990 22.27508  -15.21362 1.000 63.61382  ? 221 THR   A CG2 1 
ATOM   1827 N N   . PRO   A 1 225 ? 0.28075  22.14257  -17.86964 1.000 56.24059  ? 222 PRO   A N   1 
ATOM   1828 C CA  . PRO   A 1 225 ? 0.30044  21.44257  -19.15660 1.000 54.69431  ? 222 PRO   A CA  1 
ATOM   1829 C C   . PRO   A 1 225 ? -0.87246 20.48629  -19.30055 1.000 60.62229  ? 222 PRO   A C   1 
ATOM   1830 O O   . PRO   A 1 225 ? -1.47836 20.04084  -18.32337 1.000 63.13493  ? 222 PRO   A O   1 
ATOM   1831 C CB  . PRO   A 1 225 ? 1.63156  20.68549  -19.12520 1.000 57.56806  ? 222 PRO   A CB  1 
ATOM   1832 C CG  . PRO   A 1 225 ? 1.90045  20.47559  -17.66725 1.000 60.87290  ? 222 PRO   A CG  1 
ATOM   1833 C CD  . PRO   A 1 225 ? 1.34680  21.68267  -16.96443 1.000 50.17405  ? 222 PRO   A CD  1 
ATOM   1834 N N   . ASP   A 1 226 ? -1.18845 20.17527  -20.55769 1.000 55.56310  ? 223 ASP   A N   1 
ATOM   1835 C CA  . ASP   A 1 226 ? -2.24952 19.23645  -20.89300 1.000 58.79715  ? 223 ASP   A CA  1 
ATOM   1836 C C   . ASP   A 1 226 ? -1.75394 18.31043  -21.99837 1.000 57.08724  ? 223 ASP   A C   1 
ATOM   1837 O O   . ASP   A 1 226 ? -0.58765 18.35925  -22.40149 1.000 56.22876  ? 223 ASP   A O   1 
ATOM   1838 C CB  . ASP   A 1 226 ? -3.53392 19.97021  -21.30038 1.000 61.85137  ? 223 ASP   A CB  1 
ATOM   1839 C CG  . ASP   A 1 226 ? -3.30090 21.00712  -22.38344 1.000 63.68985  ? 223 ASP   A CG  1 
ATOM   1840 O OD1 . ASP   A 1 226 ? -2.15436 21.13524  -22.86159 1.000 71.78042  ? 223 ASP   A OD1 1 
ATOM   1841 O OD2 . ASP   A 1 226 ? -4.27087 21.70041  -22.75392 1.000 78.95550  ? 223 ASP   A OD2 1 
ATOM   1842 N N   . GLU   A 1 227 ? -2.65625 17.45885  -22.49513 1.000 58.03908  ? 224 GLU   A N   1 
ATOM   1843 C CA  . GLU   A 1 227 ? -2.26610 16.46246  -23.48850 1.000 57.62282  ? 224 GLU   A CA  1 
ATOM   1844 C C   . GLU   A 1 227 ? -1.82710 17.10212  -24.79947 1.000 65.88454  ? 224 GLU   A C   1 
ATOM   1845 O O   . GLU   A 1 227 ? -1.01566 16.52152  -25.52940 1.000 69.85607  ? 224 GLU   A O   1 
ATOM   1846 C CB  . GLU   A 1 227 ? -3.41777 15.48663  -23.73356 1.000 58.32689  ? 224 GLU   A CB  1 
ATOM   1847 C CG  . GLU   A 1 227 ? -3.61604 14.46688  -22.62138 1.000 67.09763  ? 224 GLU   A CG  1 
ATOM   1848 C CD  . GLU   A 1 227 ? -2.48493 13.45717  -22.54732 1.000 80.98087  ? 224 GLU   A CD  1 
ATOM   1849 O OE1 . GLU   A 1 227 ? -1.76868 13.28621  -23.55683 1.000 74.00901  ? 224 GLU   A OE1 1 
ATOM   1850 O OE2 . GLU   A 1 227 ? -2.31028 12.83391  -21.47937 1.000 75.04229  ? 224 GLU   A OE2 1 
ATOM   1851 N N   . VAL   A 1 228 ? -2.34008 18.29142  -25.11565 1.000 62.90156  ? 225 VAL   A N   1 
ATOM   1852 C CA  . VAL   A 1 228 ? -1.98490 18.93282  -26.37784 1.000 71.69591  ? 225 VAL   A CA  1 
ATOM   1853 C C   . VAL   A 1 228 ? -0.54045 19.41884  -26.34279 1.000 60.33865  ? 225 VAL   A C   1 
ATOM   1854 O O   . VAL   A 1 228 ? 0.24889  19.13507  -27.25108 1.000 73.10601  ? 225 VAL   A O   1 
ATOM   1855 C CB  . VAL   A 1 228 ? -2.96107 20.07948  -26.69330 1.000 69.97485  ? 225 VAL   A CB  1 
ATOM   1856 C CG1 . VAL   A 1 228 ? -2.59507 20.72613  -28.01572 1.000 65.24869  ? 225 VAL   A CG1 1 
ATOM   1857 C CG2 . VAL   A 1 228 ? -4.39185 19.56342  -26.72533 1.000 71.94094  ? 225 VAL   A CG2 1 
ATOM   1858 N N   . VAL   A 1 229 ? -0.17010 20.15548  -25.29342 1.000 64.88451  ? 226 VAL   A N   1 
ATOM   1859 C CA  . VAL   A 1 229 ? 1.19219  20.66933  -25.19819 1.000 60.63480  ? 226 VAL   A CA  1 
ATOM   1860 C C   . VAL   A 1 229 ? 2.18263  19.59879  -24.75867 1.000 65.19416  ? 226 VAL   A C   1 
ATOM   1861 O O   . VAL   A 1 229 ? 3.38776  19.74533  -24.99812 1.000 61.04707  ? 226 VAL   A O   1 
ATOM   1862 C CB  . VAL   A 1 229 ? 1.25669  21.86882  -24.23742 1.000 65.21987  ? 226 VAL   A CB  1 
ATOM   1863 C CG1 . VAL   A 1 229 ? 0.19750  22.89802  -24.60299 1.000 77.79675  ? 226 VAL   A CG1 1 
ATOM   1864 C CG2 . VAL   A 1 229 ? 1.09218  21.41279  -22.79546 1.000 73.83339  ? 226 VAL   A CG2 1 
ATOM   1865 N N   . TRP   A 1 230 ? 1.70915  18.52267  -24.13243 1.000 63.09193  ? 227 TRP   A N   1 
ATOM   1866 C CA  . TRP   A 1 230 ? 2.58628  17.46975  -23.62138 1.000 56.00056  ? 227 TRP   A CA  1 
ATOM   1867 C C   . TRP   A 1 230 ? 1.82304  16.15840  -23.68189 1.000 55.08233  ? 227 TRP   A C   1 
ATOM   1868 O O   . TRP   A 1 230 ? 1.13168  15.77803  -22.72776 1.000 57.30898  ? 227 TRP   A O   1 
ATOM   1869 C CB  . TRP   A 1 230 ? 3.05157  17.77071  -22.19694 1.000 53.41264  ? 227 TRP   A CB  1 
ATOM   1870 C CG  . TRP   A 1 230 ? 4.03658  16.78736  -21.62525 1.000 57.94527  ? 227 TRP   A CG  1 
ATOM   1871 C CD1 . TRP   A 1 230 ? 4.53803  15.67070  -22.23198 1.000 60.43897  ? 227 TRP   A CD1 1 
ATOM   1872 C CD2 . TRP   A 1 230 ? 4.64002  16.84112  -20.32638 1.000 51.97845  ? 227 TRP   A CD2 1 
ATOM   1873 N NE1 . TRP   A 1 230 ? 5.41185  15.02618  -21.39012 1.000 54.11744  ? 227 TRP   A NE1 1 
ATOM   1874 C CE2 . TRP   A 1 230 ? 5.49278  15.72484  -20.21457 1.000 51.75450  ? 227 TRP   A CE2 1 
ATOM   1875 C CE3 . TRP   A 1 230 ? 4.54125  17.72520  -19.24710 1.000 57.40327  ? 227 TRP   A CE3 1 
ATOM   1876 C CZ2 . TRP   A 1 230 ? 6.24181  15.46956  -19.06774 1.000 49.35102  ? 227 TRP   A CZ2 1 
ATOM   1877 C CZ3 . TRP   A 1 230 ? 5.28527  17.46947  -18.10897 1.000 55.96292  ? 227 TRP   A CZ3 1 
ATOM   1878 C CH2 . TRP   A 1 230 ? 6.12455  16.35146  -18.02861 1.000 66.94849  ? 227 TRP   A CH2 1 
ATOM   1879 N N   . PRO   A 1 231 ? 1.91832  15.43763  -24.79852 1.000 58.02083  ? 228 PRO   A N   1 
ATOM   1880 C CA  . PRO   A 1 231 ? 1.15745  14.18850  -24.93915 1.000 59.17380  ? 228 PRO   A CA  1 
ATOM   1881 C C   . PRO   A 1 231 ? 1.57644  13.15810  -23.89987 1.000 53.44065  ? 228 PRO   A C   1 
ATOM   1882 O O   . PRO   A 1 231 ? 2.75899  12.84115  -23.75238 1.000 63.43199  ? 228 PRO   A O   1 
ATOM   1883 C CB  . PRO   A 1 231 ? 1.49285  13.72831  -26.36351 1.000 62.30327  ? 228 PRO   A CB  1 
ATOM   1884 C CG  . PRO   A 1 231 ? 1.93731  14.97202  -27.07257 1.000 64.23752  ? 228 PRO   A CG  1 
ATOM   1885 C CD  . PRO   A 1 231 ? 2.64428  15.78556  -26.03129 1.000 55.20782  ? 228 PRO   A CD  1 
ATOM   1886 N N   . GLY   A 1 232 ? 0.58843  12.63773  -23.17489 1.000 62.59111  ? 229 GLY   A N   1 
ATOM   1887 C CA  . GLY   A 1 232 ? 0.81961  11.63631  -22.15842 1.000 62.70803  ? 229 GLY   A CA  1 
ATOM   1888 C C   . GLY   A 1 232 ? 1.00850  12.16876  -20.75554 1.000 59.54664  ? 229 GLY   A C   1 
ATOM   1889 O O   . GLY   A 1 232 ? 1.27543  11.37530  -19.84376 1.000 73.42905  ? 229 GLY   A O   1 
ATOM   1890 N N   . VAL   A 1 233 ? 0.87435  13.48141  -20.54843 1.000 63.91426  ? 230 VAL   A N   1 
ATOM   1891 C CA  . VAL   A 1 233 ? 1.10150  14.04827  -19.22242 1.000 60.80175  ? 230 VAL   A CA  1 
ATOM   1892 C C   . VAL   A 1 233 ? 0.01968  13.60381  -18.24529 1.000 67.33801  ? 230 VAL   A C   1 
ATOM   1893 O O   . VAL   A 1 233 ? 0.29555  13.39962  -17.05685 1.000 57.39588  ? 230 VAL   A O   1 
ATOM   1894 C CB  . VAL   A 1 233 ? 1.19658  15.58501  -19.30577 1.000 56.92443  ? 230 VAL   A CB  1 
ATOM   1895 C CG1 . VAL   A 1 233 ? -0.11366 16.18621  -19.79917 1.000 56.07718  ? 230 VAL   A CG1 1 
ATOM   1896 C CG2 . VAL   A 1 233 ? 1.58537  16.17308  -17.95721 1.000 52.76763  ? 230 VAL   A CG2 1 
ATOM   1897 N N   . THR   A 1 234 ? -1.21642 13.42874  -18.71859 1.000 54.87892  ? 231 THR   A N   1 
ATOM   1898 C CA  . THR   A 1 234 ? -2.30439 13.03378  -17.83324 1.000 63.30895  ? 231 THR   A CA  1 
ATOM   1899 C C   . THR   A 1 234 ? -2.23140 11.56819  -17.42931 1.000 61.97452  ? 231 THR   A C   1 
ATOM   1900 O O   . THR   A 1 234 ? -2.97515 11.15367  -16.53395 1.000 71.09601  ? 231 THR   A O   1 
ATOM   1901 C CB  . THR   A 1 234 ? -3.65583 13.31874  -18.49318 1.000 78.42955  ? 231 THR   A CB  1 
ATOM   1902 O OG1 . THR   A 1 234 ? -3.77458 12.55288  -19.69851 1.000 72.72586  ? 231 THR   A OG1 1 
ATOM   1903 C CG2 . THR   A 1 234 ? -3.78387 14.79778  -18.82442 1.000 76.75969  ? 231 THR   A CG2 1 
ATOM   1904 N N   . SER   A 1 235 ? -1.36100 10.78216  -18.05861 1.000 67.15006  ? 232 SER   A N   1 
ATOM   1905 C CA  . SER   A 1 235 ? -1.19342 9.37403   -17.73103 1.000 75.60853  ? 232 SER   A CA  1 
ATOM   1906 C C   . SER   A 1 235 ? 0.02964  9.11058   -16.86378 1.000 77.48470  ? 232 SER   A C   1 
ATOM   1907 O O   . SER   A 1 235 ? 0.30864  7.95056   -16.54551 1.000 74.65755  ? 232 SER   A O   1 
ATOM   1908 C CB  . SER   A 1 235 ? -1.10199 8.54292   -19.01516 1.000 67.87884  ? 232 SER   A CB  1 
ATOM   1909 O OG  . SER   A 1 235 ? -2.22844 8.76325   -19.84663 1.000 82.84703  ? 232 SER   A OG  1 
ATOM   1910 N N   . MET   A 1 236 ? 0.76022  10.15194  -16.47428 1.000 68.11421  ? 233 MET   A N   1 
ATOM   1911 C CA  . MET   A 1 236 ? 1.97226  9.98066   -15.69212 1.000 66.15925  ? 233 MET   A CA  1 
ATOM   1912 C C   . MET   A 1 236 ? 1.63288  9.63695   -14.24091 1.000 70.29388  ? 233 MET   A C   1 
ATOM   1913 O O   . MET   A 1 236 ? 0.57672  10.02650  -13.73427 1.000 74.86169  ? 233 MET   A O   1 
ATOM   1914 C CB  . MET   A 1 236 ? 2.82085  11.24612  -15.75412 1.000 63.40354  ? 233 MET   A CB  1 
ATOM   1915 C CG  . MET   A 1 236 ? 3.14091  11.67796  -17.17905 1.000 66.46214  ? 233 MET   A CG  1 
ATOM   1916 S SD  . MET   A 1 236 ? 4.44093  12.91805  -17.29444 1.000 74.65468  ? 233 MET   A SD  1 
ATOM   1917 C CE  . MET   A 1 236 ? 5.86376  11.96677  -16.76359 1.000 70.55813  ? 233 MET   A CE  1 
ATOM   1918 N N   . PRO   A 1 237 ? 2.51480  8.89850   -13.55573 1.000 67.35676  ? 234 PRO   A N   1 
ATOM   1919 C CA  . PRO   A 1 237 ? 2.15249  8.37651   -12.22402 1.000 74.64352  ? 234 PRO   A CA  1 
ATOM   1920 C C   . PRO   A 1 237 ? 1.82596  9.44950   -11.19925 1.000 68.75437  ? 234 PRO   A C   1 
ATOM   1921 O O   . PRO   A 1 237 ? 0.89714  9.26979   -10.40178 1.000 71.60701  ? 234 PRO   A O   1 
ATOM   1922 C CB  . PRO   A 1 237 ? 3.39566  7.57002   -11.82076 1.000 65.74755  ? 234 PRO   A CB  1 
ATOM   1923 C CG  . PRO   A 1 237 ? 4.05136  7.21260   -13.11168 1.000 68.43040  ? 234 PRO   A CG  1 
ATOM   1924 C CD  . PRO   A 1 237 ? 3.81664  8.38418   -14.01463 1.000 69.04914  ? 234 PRO   A CD  1 
ATOM   1925 N N   . ASP   A 1 238 ? 2.56007  10.55795  -11.18883 1.000 64.98185  ? 235 ASP   A N   1 
ATOM   1926 C CA  . ASP   A 1 238 ? 2.34343  11.60401  -10.19881 1.000 69.52774  ? 235 ASP   A CA  1 
ATOM   1927 C C   . ASP   A 1 238 ? 1.40748  12.70324  -10.68249 1.000 68.09709  ? 235 ASP   A C   1 
ATOM   1928 O O   . ASP   A 1 238 ? 1.20632  13.68501  -9.96003  1.000 65.50826  ? 235 ASP   A O   1 
ATOM   1929 C CB  . ASP   A 1 238 ? 3.68222  12.21466  -9.77367  1.000 62.43610  ? 235 ASP   A CB  1 
ATOM   1930 C CG  . ASP   A 1 238 ? 4.52876  11.25255  -8.96393  1.000 77.21626  ? 235 ASP   A CG  1 
ATOM   1931 O OD1 . ASP   A 1 238 ? 3.95413  10.47597  -8.17190  1.000 86.13802  ? 235 ASP   A OD1 1 
ATOM   1932 O OD2 . ASP   A 1 238 ? 5.76780  11.27131  -9.11960  1.000 89.59461  ? 235 ASP   A OD2 1 
ATOM   1933 N N   . TYR   A 1 239 ? 0.83383  12.56988  -11.87506 1.000 69.37787  ? 236 TYR   A N   1 
ATOM   1934 C CA  . TYR   A 1 239 ? -0.13482 13.55192  -12.33882 1.000 67.68074  ? 236 TYR   A CA  1 
ATOM   1935 C C   . TYR   A 1 239 ? -1.45361 13.38021  -11.59781 1.000 63.05925  ? 236 TYR   A C   1 
ATOM   1936 O O   . TYR   A 1 239 ? -1.90837 12.25908  -11.35344 1.000 72.53334  ? 236 TYR   A O   1 
ATOM   1937 C CB  . TYR   A 1 239 ? -0.36090 13.42275  -13.84583 1.000 65.99519  ? 236 TYR   A CB  1 
ATOM   1938 C CG  . TYR   A 1 239 ? -1.37844 14.40406  -14.39469 1.000 72.20906  ? 236 TYR   A CG  1 
ATOM   1939 C CD1 . TYR   A 1 239 ? -0.99254 15.66744  -14.82408 1.000 67.17662  ? 236 TYR   A CD1 1 
ATOM   1940 C CD2 . TYR   A 1 239 ? -2.72527 14.06744  -14.48060 1.000 71.80804  ? 236 TYR   A CD2 1 
ATOM   1941 C CE1 . TYR   A 1 239 ? -1.91806 16.56711  -15.32399 1.000 60.93033  ? 236 TYR   A CE1 1 
ATOM   1942 C CE2 . TYR   A 1 239 ? -3.65649 14.96051  -14.97760 1.000 75.78892  ? 236 TYR   A CE2 1 
ATOM   1943 C CZ  . TYR   A 1 239 ? -3.24741 16.20810  -15.39820 1.000 72.64021  ? 236 TYR   A CZ  1 
ATOM   1944 O OH  . TYR   A 1 239 ? -4.17109 17.09956  -15.89443 1.000 79.75354  ? 236 TYR   A OH  1 
ATOM   1945 N N   . LYS   A 1 240 ? -2.07021 14.50507  -11.24144 1.000 62.22657  ? 237 LYS   A N   1 
ATOM   1946 C CA  . LYS   A 1 240 ? -3.36217 14.50676  -10.57606 1.000 75.70629  ? 237 LYS   A CA  1 
ATOM   1947 C C   . LYS   A 1 240 ? -4.30194 15.43292  -11.33594 1.000 80.84281  ? 237 LYS   A C   1 
ATOM   1948 O O   . LYS   A 1 240 ? -3.91740 16.56779  -11.67151 1.000 75.24908  ? 237 LYS   A O   1 
ATOM   1949 C CB  . LYS   A 1 240 ? -3.23521 14.95310  -9.11264  1.000 76.82922  ? 237 LYS   A CB  1 
ATOM   1950 C CG  . LYS   A 1 240 ? -2.28954 14.10047  -8.28086  1.000 82.18040  ? 237 LYS   A CG  1 
ATOM   1951 C CD  . LYS   A 1 240 ? -2.23628 14.57901  -6.83828  1.000 103.01227 ? 237 LYS   A CD  1 
ATOM   1952 C CE  . LYS   A 1 240 ? -1.21548 13.79224  -6.03056  1.000 93.66727  ? 237 LYS   A CE  1 
ATOM   1953 N NZ  . LYS   A 1 240 ? -1.50193 12.33141  -6.04030  1.000 100.61137 ? 237 LYS   A NZ  1 
ATOM   1954 N N   . PRO   A 1 241 ? -5.52969 14.99627  -11.63507 1.000 85.49721  ? 238 PRO   A N   1 
ATOM   1955 C CA  . PRO   A 1 241 ? -6.49257 15.89065  -12.29973 1.000 89.33758  ? 238 PRO   A CA  1 
ATOM   1956 C C   . PRO   A 1 241 ? -6.85937 17.11312  -11.47670 1.000 86.26856  ? 238 PRO   A C   1 
ATOM   1957 O O   . PRO   A 1 241 ? -7.44325 18.05328  -12.03074 1.000 74.70242  ? 238 PRO   A O   1 
ATOM   1958 C CB  . PRO   A 1 241 ? -7.71619 14.99057  -12.52529 1.000 87.02246  ? 238 PRO   A CB  1 
ATOM   1959 C CG  . PRO   A 1 241 ? -7.18512 13.59136  -12.45723 1.000 94.92855  ? 238 PRO   A CG  1 
ATOM   1960 C CD  . PRO   A 1 241 ? -6.05361 13.62975  -11.47802 1.000 73.87218  ? 238 PRO   A CD  1 
ATOM   1961 N N   . SER   A 1 242 ? -6.53679 17.13363  -10.18481 1.000 83.26894  ? 239 SER   A N   1 
ATOM   1962 C CA  . SER   A 1 242 ? -6.85581 18.25462  -9.31092  1.000 74.51016  ? 239 SER   A CA  1 
ATOM   1963 C C   . SER   A 1 242 ? -5.81316 19.36497  -9.35753  1.000 72.87088  ? 239 SER   A C   1 
ATOM   1964 O O   . SER   A 1 242 ? -5.89086 20.29396  -8.54665  1.000 81.35687  ? 239 SER   A O   1 
ATOM   1965 C CB  . SER   A 1 242 ? -7.02179 17.76398  -7.87026  1.000 89.10306  ? 239 SER   A CB  1 
ATOM   1966 O OG  . SER   A 1 242 ? -5.83167 17.15299  -7.40162  1.000 102.12425 ? 239 SER   A OG  1 
ATOM   1967 N N   . PHE   A 1 243 ? -4.84675 19.29101  -10.26703 1.000 67.04068  ? 240 PHE   A N   1 
ATOM   1968 C CA  . PHE   A 1 243 ? -3.86778 20.36099  -10.39394 1.000 77.46281  ? 240 PHE   A CA  1 
ATOM   1969 C C   . PHE   A 1 243 ? -4.57019 21.65327  -10.80001 1.000 75.32346  ? 240 PHE   A C   1 
ATOM   1970 O O   . PHE   A 1 243 ? -5.38010 21.64378  -11.73782 1.000 80.87787  ? 240 PHE   A O   1 
ATOM   1971 C CB  . PHE   A 1 243 ? -2.79678 20.00281  -11.42458 1.000 72.39686  ? 240 PHE   A CB  1 
ATOM   1972 C CG  . PHE   A 1 243 ? -1.81501 18.96589  -10.95336 1.000 74.58941  ? 240 PHE   A CG  1 
ATOM   1973 C CD1 . PHE   A 1 243 ? -1.69859 18.65568  -9.60825  1.000 76.97623  ? 240 PHE   A CD1 1 
ATOM   1974 C CD2 . PHE   A 1 243 ? -0.99966 18.30753  -11.86048 1.000 73.69645  ? 240 PHE   A CD2 1 
ATOM   1975 C CE1 . PHE   A 1 243 ? -0.79162 17.70329  -9.17820  1.000 77.12571  ? 240 PHE   A CE1 1 
ATOM   1976 C CE2 . PHE   A 1 243 ? -0.09112 17.35589  -11.43678 1.000 71.90244  ? 240 PHE   A CE2 1 
ATOM   1977 C CZ  . PHE   A 1 243 ? 0.01287  17.05341  -10.09413 1.000 71.83611  ? 240 PHE   A CZ  1 
ATOM   1978 N N   . PRO   A 1 244 ? -4.30704 22.76890  -10.12349 1.000 77.04601  ? 241 PRO   A N   1 
ATOM   1979 C CA  . PRO   A 1 244 ? -4.94316 24.03116  -10.51287 1.000 74.19037  ? 241 PRO   A CA  1 
ATOM   1980 C C   . PRO   A 1 244 ? -4.49274 24.48139  -11.89301 1.000 74.68909  ? 241 PRO   A C   1 
ATOM   1981 O O   . PRO   A 1 244 ? -3.36303 24.23019  -12.32060 1.000 72.98992  ? 241 PRO   A O   1 
ATOM   1982 C CB  . PRO   A 1 244 ? -4.48184 25.01345  -9.42876  1.000 84.23661  ? 241 PRO   A CB  1 
ATOM   1983 C CG  . PRO   A 1 244 ? -4.07622 24.14927  -8.27558  1.000 83.89619  ? 241 PRO   A CG  1 
ATOM   1984 C CD  . PRO   A 1 244 ? -3.51196 22.90698  -8.89263  1.000 79.44857  ? 241 PRO   A CD  1 
ATOM   1985 N N   . LYS   A 1 245 ? -5.40108 25.15890  -12.59085 1.000 68.25166  ? 242 LYS   A N   1 
ATOM   1986 C CA  . LYS   A 1 245 ? -5.15443 25.62756  -13.95001 1.000 67.15056  ? 242 LYS   A CA  1 
ATOM   1987 C C   . LYS   A 1 245 ? -4.59742 27.04575  -13.89251 1.000 73.65553  ? 242 LYS   A C   1 
ATOM   1988 O O   . LYS   A 1 245 ? -5.32466 27.99641  -13.58586 1.000 89.36833  ? 242 LYS   A O   1 
ATOM   1989 C CB  . LYS   A 1 245 ? -6.43486 25.57328  -14.77968 1.000 69.65044  ? 242 LYS   A CB  1 
ATOM   1990 C CG  . LYS   A 1 245 ? -7.04912 24.18711  -14.88472 1.000 67.32093  ? 242 LYS   A CG  1 
ATOM   1991 C CD  . LYS   A 1 245 ? -6.08014 23.19963  -15.51373 1.000 64.47810  ? 242 LYS   A CD  1 
ATOM   1992 C CE  . LYS   A 1 245 ? -6.72214 21.83292  -15.68882 1.000 75.07198  ? 242 LYS   A CE  1 
ATOM   1993 N NZ  . LYS   A 1 245 ? -5.79507 20.86327  -16.33535 1.000 76.27340  ? 242 LYS   A NZ  1 
ATOM   1994 N N   . TRP   A 1 246 ? -3.30869 27.18632  -14.18331 1.000 61.75039  ? 243 TRP   A N   1 
ATOM   1995 C CA  . TRP   A 1 246 ? -2.66158 28.48330  -14.29375 1.000 69.62913  ? 243 TRP   A CA  1 
ATOM   1996 C C   . TRP   A 1 246 ? -2.36070 28.78583  -15.75529 1.000 74.71195  ? 243 TRP   A C   1 
ATOM   1997 O O   . TRP   A 1 246 ? -2.04831 27.88693  -16.54145 1.000 75.95624  ? 243 TRP   A O   1 
ATOM   1998 C CB  . TRP   A 1 246 ? -1.36368 28.53464  -13.47994 1.000 68.87744  ? 243 TRP   A CB  1 
ATOM   1999 C CG  . TRP   A 1 246 ? -1.56939 28.56303  -11.99562 1.000 76.03294  ? 243 TRP   A CG  1 
ATOM   2000 C CD1 . TRP   A 1 246 ? -2.00433 29.61872  -11.24849 1.000 67.17819  ? 243 TRP   A CD1 1 
ATOM   2001 C CD2 . TRP   A 1 246 ? -1.33310 27.49095  -11.07533 1.000 76.29077  ? 243 TRP   A CD2 1 
ATOM   2002 N NE1 . TRP   A 1 246 ? -2.06160 29.26797  -9.92155  1.000 79.66160  ? 243 TRP   A NE1 1 
ATOM   2003 C CE2 . TRP   A 1 246 ? -1.65434 27.96665  -9.78862  1.000 79.08215  ? 243 TRP   A CE2 1 
ATOM   2004 C CE3 . TRP   A 1 246 ? -0.88609 26.17384  -11.21508 1.000 70.55978  ? 243 TRP   A CE3 1 
ATOM   2005 C CZ2 . TRP   A 1 246 ? -1.54091 27.17248  -8.64919  1.000 76.23238  ? 243 TRP   A CZ2 1 
ATOM   2006 C CZ3 . TRP   A 1 246 ? -0.77361 25.38704  -10.08256 1.000 83.44471  ? 243 TRP   A CZ3 1 
ATOM   2007 C CH2 . TRP   A 1 246 ? -1.09855 25.88934  -8.81654  1.000 74.65282  ? 243 TRP   A CH2 1 
ATOM   2008 N N   . ALA   A 1 247 ? -2.45670 30.06284  -16.11173 1.000 73.03511  ? 244 ALA   A N   1 
ATOM   2009 C CA  . ALA   A 1 247 ? -2.17367 30.50653  -17.46795 1.000 76.79580  ? 244 ALA   A CA  1 
ATOM   2010 C C   . ALA   A 1 247 ? -0.68212 30.76478  -17.63652 1.000 69.76151  ? 244 ALA   A C   1 
ATOM   2011 O O   . ALA   A 1 247 ? -0.00951 31.22267  -16.70785 1.000 74.83927  ? 244 ALA   A O   1 
ATOM   2012 C CB  . ALA   A 1 247 ? -2.96624 31.77170  -17.79743 1.000 64.72592  ? 244 ALA   A CB  1 
ATOM   2013 N N   . ARG   A 1 248 ? -0.16861 30.46266  -18.82727 1.000 63.12882  ? 245 ARG   A N   1 
ATOM   2014 C CA  . ARG   A 1 248 ? 1.24053  30.69458  -19.11366 1.000 64.59813  ? 245 ARG   A CA  1 
ATOM   2015 C C   . ARG   A 1 248 ? 1.53384  32.18910  -19.10176 1.000 71.06800  ? 245 ARG   A C   1 
ATOM   2016 O O   . ARG   A 1 248 ? 0.80904  32.98013  -19.71261 1.000 82.63061  ? 245 ARG   A O   1 
ATOM   2017 C CB  . ARG   A 1 248 ? 1.61550  30.08860  -20.46504 1.000 61.22534  ? 245 ARG   A CB  1 
ATOM   2018 C CG  . ARG   A 1 248 ? 3.07932  30.25705  -20.83889 1.000 64.57563  ? 245 ARG   A CG  1 
ATOM   2019 C CD  . ARG   A 1 248 ? 3.35634  29.71108  -22.23220 1.000 79.47918  ? 245 ARG   A CD  1 
ATOM   2020 N NE  . ARG   A 1 248 ? 4.76119  29.83558  -22.60392 1.000 79.99743  ? 245 ARG   A NE  1 
ATOM   2021 C CZ  . ARG   A 1 248 ? 5.66936  28.88513  -22.42920 1.000 75.05299  ? 245 ARG   A CZ  1 
ATOM   2022 N NH1 . ARG   A 1 248 ? 5.35379  27.71826  -21.89159 1.000 70.37472  ? 245 ARG   A NH1 1 
ATOM   2023 N NH2 . ARG   A 1 248 ? 6.92562  29.11080  -22.80371 1.000 75.43293  ? 245 ARG   A NH2 1 
ATOM   2024 N N   . GLN   A 1 249 ? 2.59252  32.57630  -18.39867 1.000 75.33918  ? 246 GLN   A N   1 
ATOM   2025 C CA  . GLN   A 1 249 ? 2.95111  33.98131  -18.29531 1.000 77.43471  ? 246 GLN   A CA  1 
ATOM   2026 C C   . GLN   A 1 249 ? 3.77882  34.41981  -19.49703 1.000 78.73016  ? 246 GLN   A C   1 
ATOM   2027 O O   . GLN   A 1 249 ? 4.56843  33.65014  -20.05266 1.000 72.29883  ? 246 GLN   A O   1 
ATOM   2028 C CB  . GLN   A 1 249 ? 3.72927  34.24577  -17.00611 1.000 75.77204  ? 246 GLN   A CB  1 
ATOM   2029 C CG  . GLN   A 1 249 ? 2.95774  33.92763  -15.73604 1.000 83.64892  ? 246 GLN   A CG  1 
ATOM   2030 C CD  . GLN   A 1 249 ? 3.73811  34.26941  -14.48149 1.000 98.93167  ? 246 GLN   A CD  1 
ATOM   2031 O OE1 . GLN   A 1 249 ? 4.82310  34.84776  -14.54907 1.000 99.00789  ? 246 GLN   A OE1 1 
ATOM   2032 N NE2 . GLN   A 1 249 ? 3.18804  33.91218  -13.32692 1.000 106.92718 ? 246 GLN   A NE2 1 
ATOM   2033 N N   . ASP   A 1 250 ? 3.58571  35.67446  -19.89602 1.000 78.20297  ? 247 ASP   A N   1 
ATOM   2034 C CA  . ASP   A 1 250 ? 4.37264  36.24859  -20.97778 1.000 80.15810  ? 247 ASP   A CA  1 
ATOM   2035 C C   . ASP   A 1 250 ? 5.82887  36.36256  -20.54578 1.000 74.96994  ? 247 ASP   A C   1 
ATOM   2036 O O   . ASP   A 1 250 ? 6.12861  36.89791  -19.47411 1.000 82.74345  ? 247 ASP   A O   1 
ATOM   2037 C CB  . ASP   A 1 250 ? 3.81712  37.62048  -21.36330 1.000 93.26813  ? 247 ASP   A CB  1 
ATOM   2038 C CG  . ASP   A 1 250 ? 4.29498  38.08876  -22.72880 1.000 98.71638  ? 247 ASP   A CG  1 
ATOM   2039 O OD1 . ASP   A 1 250 ? 5.44393  37.77882  -23.10900 1.000 105.06556 ? 247 ASP   A OD1 1 
ATOM   2040 O OD2 . ASP   A 1 250 ? 3.51492  38.77212  -23.42542 1.000 112.25085 ? 247 ASP   A OD2 1 
ATOM   2041 N N   . PHE   A 1 251 ? 6.73804  35.85511  -21.38138 1.000 72.95577  ? 248 PHE   A N   1 
ATOM   2042 C CA  . PHE   A 1 251 ? 8.15690  35.90437  -21.04915 1.000 81.40067  ? 248 PHE   A CA  1 
ATOM   2043 C C   . PHE   A 1 251 ? 8.70725  37.32333  -21.01289 1.000 88.09641  ? 248 PHE   A C   1 
ATOM   2044 O O   . PHE   A 1 251 ? 9.83718  37.51634  -20.55177 1.000 87.15073  ? 248 PHE   A O   1 
ATOM   2045 C CB  . PHE   A 1 251 ? 8.96706  35.05750  -22.03312 1.000 76.68325  ? 248 PHE   A CB  1 
ATOM   2046 C CG  . PHE   A 1 251 ? 9.04955  33.60398  -21.65551 1.000 64.56430  ? 248 PHE   A CG  1 
ATOM   2047 C CD1 . PHE   A 1 251 ? 8.09136  33.03057  -20.83485 1.000 70.47313  ? 248 PHE   A CD1 1 
ATOM   2048 C CD2 . PHE   A 1 251 ? 10.09704 32.81669  -22.10380 1.000 63.97798  ? 248 PHE   A CD2 1 
ATOM   2049 C CE1 . PHE   A 1 251 ? 8.16770  31.69641  -20.48181 1.000 72.51876  ? 248 PHE   A CE1 1 
ATOM   2050 C CE2 . PHE   A 1 251 ? 10.18024 31.48194  -21.75172 1.000 63.53768  ? 248 PHE   A CE2 1 
ATOM   2051 C CZ  . PHE   A 1 251 ? 9.21390  30.92147  -20.94065 1.000 72.52019  ? 248 PHE   A CZ  1 
ATOM   2052 N N   . SER   A 1 252 ? 7.94640  38.31425  -21.48423 1.000 93.06708  ? 249 SER   A N   1 
ATOM   2053 C CA  . SER   A 1 252 ? 8.34342  39.70342  -21.29436 1.000 96.66125  ? 249 SER   A CA  1 
ATOM   2054 C C   . SER   A 1 252 ? 8.34513  40.09386  -19.82303 1.000 91.95317  ? 249 SER   A C   1 
ATOM   2055 O O   . SER   A 1 252 ? 9.02203  41.05728  -19.44787 1.000 97.58060  ? 249 SER   A O   1 
ATOM   2056 C CB  . SER   A 1 252 ? 7.41655  40.63019  -22.08276 1.000 100.19266 ? 249 SER   A CB  1 
ATOM   2057 O OG  . SER   A 1 252 ? 7.46103  40.33722  -23.46845 1.000 113.31983 ? 249 SER   A OG  1 
ATOM   2058 N N   . LYS   A 1 253 ? 7.60189  39.37074  -18.98554 1.000 85.02251  ? 250 LYS   A N   1 
ATOM   2059 C CA  . LYS   A 1 253 ? 7.61569  39.58258  -17.54435 1.000 90.09286  ? 250 LYS   A CA  1 
ATOM   2060 C C   . LYS   A 1 253 ? 8.46778  38.56495  -16.80128 1.000 83.60834  ? 250 LYS   A C   1 
ATOM   2061 O O   . LYS   A 1 253 ? 9.01563  38.88907  -15.74257 1.000 93.22839  ? 250 LYS   A O   1 
ATOM   2062 C CB  . LYS   A 1 253 ? 6.18905  39.54242  -16.98446 1.000 88.72354  ? 250 LYS   A CB  1 
ATOM   2063 C CG  . LYS   A 1 253 ? 5.23732  40.53905  -17.62506 1.000 106.53588 ? 250 LYS   A CG  1 
ATOM   2064 C CD  . LYS   A 1 253 ? 3.92512  40.61780  -16.85958 1.000 116.99180 ? 250 LYS   A CD  1 
ATOM   2065 C CE  . LYS   A 1 253 ? 3.27255  39.25056  -16.72857 1.000 117.60725 ? 250 LYS   A CE  1 
ATOM   2066 N NZ  . LYS   A 1 253 ? 2.93605  38.66112  -18.05353 1.000 101.72423 ? 250 LYS   A NZ  1 
ATOM   2067 N N   . VAL   A 1 254 ? 8.58910  37.34402  -17.32660 1.000 72.74331  ? 251 VAL   A N   1 
ATOM   2068 C CA  . VAL   A 1 254 ? 9.43195  36.33793  -16.68679 1.000 76.03094  ? 251 VAL   A CA  1 
ATOM   2069 C C   . VAL   A 1 254 ? 10.90148 36.71700  -16.82017 1.000 78.76897  ? 251 VAL   A C   1 
ATOM   2070 O O   . VAL   A 1 254 ? 11.65934 36.69052  -15.84342 1.000 79.59199  ? 251 VAL   A O   1 
ATOM   2071 C CB  . VAL   A 1 254 ? 9.15115  34.94575  -17.28040 1.000 69.55326  ? 251 VAL   A CB  1 
ATOM   2072 C CG1 . VAL   A 1 254 ? 10.05939 33.90386  -16.64486 1.000 65.68105  ? 251 VAL   A CG1 1 
ATOM   2073 C CG2 . VAL   A 1 254 ? 7.68916  34.57284  -17.08963 1.000 76.07396  ? 251 VAL   A CG2 1 
ATOM   2074 N N   . VAL   A 1 255 ? 11.32362 37.07548  -18.02831 1.000 71.21014  ? 252 VAL   A N   1 
ATOM   2075 C CA  . VAL   A 1 255 ? 12.68602 37.54103  -18.27439 1.000 71.49509  ? 252 VAL   A CA  1 
ATOM   2076 C C   . VAL   A 1 255 ? 12.61712 38.88542  -18.99162 1.000 80.64140  ? 252 VAL   A C   1 
ATOM   2077 O O   . VAL   A 1 255 ? 12.76078 38.94127  -20.22202 1.000 85.34441  ? 252 VAL   A O   1 
ATOM   2078 C CB  . VAL   A 1 255 ? 13.49293 36.50610  -19.07476 1.000 72.51833  ? 252 VAL   A CB  1 
ATOM   2079 C CG1 . VAL   A 1 255 ? 14.09849 35.47534  -18.13584 1.000 69.48766  ? 252 VAL   A CG1 1 
ATOM   2080 C CG2 . VAL   A 1 255 ? 12.60579 35.81784  -20.10451 1.000 63.93524  ? 252 VAL   A CG2 1 
ATOM   2081 N N   . PRO   A 1 256 ? 12.38954 39.98153  -18.27127 1.000 80.05482  ? 253 PRO   A N   1 
ATOM   2082 C CA  . PRO   A 1 256 ? 12.25483 41.29887  -18.91768 1.000 77.78448  ? 253 PRO   A CA  1 
ATOM   2083 C C   . PRO   A 1 256 ? 13.47507 41.68352  -19.74215 1.000 80.68700  ? 253 PRO   A C   1 
ATOM   2084 O O   . PRO   A 1 256 ? 13.31450 42.12314  -20.89095 1.000 79.18493  ? 253 PRO   A O   1 
ATOM   2085 C CB  . PRO   A 1 256 ? 12.04626 42.25347  -17.73114 1.000 81.38815  ? 253 PRO   A CB  1 
ATOM   2086 C CG  . PRO   A 1 256 ? 11.41340 41.39761  -16.68587 1.000 80.94937  ? 253 PRO   A CG  1 
ATOM   2087 C CD  . PRO   A 1 256 ? 12.02383 40.02823  -16.84313 1.000 78.03140  ? 253 PRO   A CD  1 
ATOM   2088 N N   . PRO   A 1 257 ? 14.70783 41.55373  -19.22376 1.000 80.14238  ? 254 PRO   A N   1 
ATOM   2089 C CA  . PRO   A 1 257 ? 15.86404 42.01193  -20.01590 1.000 77.11929  ? 254 PRO   A CA  1 
ATOM   2090 C C   . PRO   A 1 257 ? 16.12379 41.19143  -21.26930 1.000 85.24910  ? 254 PRO   A C   1 
ATOM   2091 O O   . PRO   A 1 257 ? 16.92861 41.62001  -22.10690 1.000 77.64258  ? 254 PRO   A O   1 
ATOM   2092 C CB  . PRO   A 1 257 ? 17.04072 41.89280  -19.03425 1.000 79.23107  ? 254 PRO   A CB  1 
ATOM   2093 C CG  . PRO   A 1 257 ? 16.42428 41.78502  -17.68923 1.000 81.35211  ? 254 PRO   A CG  1 
ATOM   2094 C CD  . PRO   A 1 257 ? 15.15905 41.03898  -17.91714 1.000 73.69195  ? 254 PRO   A CD  1 
ATOM   2095 N N   . LEU   A 1 258 ? 15.47625 40.04142  -21.43006 1.000 81.26723  ? 255 LEU   A N   1 
ATOM   2096 C CA  . LEU   A 1 258 ? 15.75699 39.16459  -22.55672 1.000 79.25009  ? 255 LEU   A CA  1 
ATOM   2097 C C   . LEU   A 1 258 ? 15.06283 39.66503  -23.81770 1.000 80.14079  ? 255 LEU   A C   1 
ATOM   2098 O O   . LEU   A 1 258 ? 13.89368 40.06018  -23.78809 1.000 78.53783  ? 255 LEU   A O   1 
ATOM   2099 C CB  . LEU   A 1 258 ? 15.31226 37.73780  -22.23621 1.000 74.21588  ? 255 LEU   A CB  1 
ATOM   2100 C CG  . LEU   A 1 258 ? 16.27918 36.62692  -22.64641 1.000 77.16978  ? 255 LEU   A CG  1 
ATOM   2101 C CD1 . LEU   A 1 258 ? 17.69410 36.96221  -22.20367 1.000 65.85754  ? 255 LEU   A CD1 1 
ATOM   2102 C CD2 . LEU   A 1 258 ? 15.83854 35.29582  -22.05986 1.000 63.39174  ? 255 LEU   A CD2 1 
ATOM   2103 N N   . ASP   A 1 259 ? 15.79336 39.64438  -24.92971 1.000 80.65417  ? 256 ASP   A N   1 
ATOM   2104 C CA  . ASP   A 1 259 ? 15.27140 40.11764  -26.20469 1.000 82.40164  ? 256 ASP   A CA  1 
ATOM   2105 C C   . ASP   A 1 259 ? 14.44678 39.01245  -26.86454 1.000 84.25837  ? 256 ASP   A C   1 
ATOM   2106 O O   . ASP   A 1 259 ? 14.11999 37.99365  -26.24984 1.000 70.80314  ? 256 ASP   A O   1 
ATOM   2107 C CB  . ASP   A 1 259 ? 16.41356 40.59642  -27.09766 1.000 87.06100  ? 256 ASP   A CB  1 
ATOM   2108 C CG  . ASP   A 1 259 ? 17.44666 39.51606  -27.35471 1.000 97.44273  ? 256 ASP   A CG  1 
ATOM   2109 O OD1 . ASP   A 1 259 ? 17.16939 38.60203  -28.15984 1.000 95.60230  ? 256 ASP   A OD1 1 
ATOM   2110 O OD2 . ASP   A 1 259 ? 18.53806 39.58123  -26.75106 1.000 112.96517 ? 256 ASP   A OD2 1 
ATOM   2111 N N   . GLU   A 1 260 ? 14.10655 39.20560  -28.14136 1.000 68.92787  ? 257 GLU   A N   1 
ATOM   2112 C CA  . GLU   A 1 260 ? 13.25082 38.25025  -28.83946 1.000 79.36722  ? 257 GLU   A CA  1 
ATOM   2113 C C   . GLU   A 1 260 ? 13.94442 36.90387  -29.00972 1.000 73.71330  ? 257 GLU   A C   1 
ATOM   2114 O O   . GLU   A 1 260 ? 13.34999 35.85132  -28.74837 1.000 72.37402  ? 257 GLU   A O   1 
ATOM   2115 C CB  . GLU   A 1 260 ? 12.83370 38.81631  -30.19678 1.000 77.28589  ? 257 GLU   A CB  1 
ATOM   2116 C CG  . GLU   A 1 260 ? 12.05322 37.84004  -31.06200 1.000 91.39593  ? 257 GLU   A CG  1 
ATOM   2117 C CD  . GLU   A 1 260 ? 11.69146 38.42032  -32.41517 1.000 115.62990 ? 257 GLU   A CD  1 
ATOM   2118 O OE1 . GLU   A 1 260 ? 11.86078 39.64350  -32.60432 1.000 114.49631 ? 257 GLU   A OE1 1 
ATOM   2119 O OE2 . GLU   A 1 260 ? 11.23998 37.65241  -33.29068 1.000 121.39518 ? 257 GLU   A OE2 1 
ATOM   2120 N N   . ASP   A 1 261 ? 15.20371 36.91616  -29.45388 1.000 65.71599  ? 258 ASP   A N   1 
ATOM   2121 C CA  . ASP   A 1 261 ? 15.93173 35.66426  -29.63060 1.000 56.71141  ? 258 ASP   A CA  1 
ATOM   2122 C C   . ASP   A 1 261 ? 16.18519 34.96886  -28.29984 1.000 59.40609  ? 258 ASP   A C   1 
ATOM   2123 O O   . ASP   A 1 261 ? 16.22178 33.73469  -28.24504 1.000 56.67050  ? 258 ASP   A O   1 
ATOM   2124 C CB  . ASP   A 1 261 ? 17.25194 35.91957  -30.35785 1.000 62.74500  ? 258 ASP   A CB  1 
ATOM   2125 C CG  . ASP   A 1 261 ? 17.05098 36.32762  -31.80564 1.000 78.92372  ? 258 ASP   A CG  1 
ATOM   2126 O OD1 . ASP   A 1 261 ? 16.08632 35.84158  -32.43329 1.000 84.20870  ? 258 ASP   A OD1 1 
ATOM   2127 O OD2 . ASP   A 1 261 ? 17.85802 37.13269  -32.31650 1.000 77.37920  ? 258 ASP   A OD2 1 
ATOM   2128 N N   . GLY   A 1 262 ? 16.35713 35.73556  -27.22215 1.000 66.58552  ? 259 GLY   A N   1 
ATOM   2129 C CA  . GLY   A 1 262 ? 16.57839 35.12345  -25.92294 1.000 58.97761  ? 259 GLY   A CA  1 
ATOM   2130 C C   . GLY   A 1 262 ? 15.34032 34.43491  -25.38135 1.000 53.38748  ? 259 GLY   A C   1 
ATOM   2131 O O   . GLY   A 1 262 ? 15.42107 33.32442  -24.84850 1.000 52.40890  ? 259 GLY   A O   1 
ATOM   2132 N N   . ARG   A 1 263 ? 14.17858 35.08341  -25.50527 1.000 60.82587  ? 260 ARG   A N   1 
ATOM   2133 C CA  . ARG   A 1 263 ? 12.93736 34.46709  -25.04710 1.000 63.27301  ? 260 ARG   A CA  1 
ATOM   2134 C C   . ARG   A 1 263 ? 12.61437 33.21556  -25.85209 1.000 65.75935  ? 260 ARG   A C   1 
ATOM   2135 O O   . ARG   A 1 263 ? 12.05745 32.25073  -25.31579 1.000 61.34747  ? 260 ARG   A O   1 
ATOM   2136 C CB  . ARG   A 1 263 ? 11.78265 35.46524  -25.13642 1.000 68.38920  ? 260 ARG   A CB  1 
ATOM   2137 C CG  . ARG   A 1 263 ? 11.96487 36.72412  -24.30861 1.000 65.24740  ? 260 ARG   A CG  1 
ATOM   2138 C CD  . ARG   A 1 263 ? 10.70553 37.57662  -24.33140 1.000 81.49752  ? 260 ARG   A CD  1 
ATOM   2139 N NE  . ARG   A 1 263 ? 10.17847 37.74287  -25.68137 1.000 81.50054  ? 260 ARG   A NE  1 
ATOM   2140 C CZ  . ARG   A 1 263 ? 10.48587 38.74806  -26.48994 1.000 83.13417  ? 260 ARG   A CZ  1 
ATOM   2141 N NH1 . ARG   A 1 263 ? 11.31848 39.70596  -26.11664 1.000 96.79280  ? 260 ARG   A NH1 1 
ATOM   2142 N NH2 . ARG   A 1 263 ? 9.94326  38.79385  -27.70359 1.000 83.45160  ? 260 ARG   A NH2 1 
ATOM   2143 N N   . SER   A 1 264 ? 12.95253 33.21473  -27.14373 1.000 59.65093  ? 261 SER   A N   1 
ATOM   2144 C CA  . SER   A 1 264 ? 12.69224 32.04693  -27.97950 1.000 58.38017  ? 261 SER   A CA  1 
ATOM   2145 C C   . SER   A 1 264 ? 13.52289 30.85321  -27.52813 1.000 51.49362  ? 261 SER   A C   1 
ATOM   2146 O O   . SER   A 1 264 ? 13.00246 29.74234  -27.37452 1.000 52.74495  ? 261 SER   A O   1 
ATOM   2147 C CB  . SER   A 1 264 ? 12.97778 32.37531  -29.44438 1.000 55.85824  ? 261 SER   A CB  1 
ATOM   2148 O OG  . SER   A 1 264 ? 12.96952 31.19881  -30.23444 1.000 67.11211  ? 261 SER   A OG  1 
ATOM   2149 N N   . LEU   A 1 265 ? 14.82358 31.06498  -27.31348 1.000 52.66840  ? 262 LEU   A N   1 
ATOM   2150 C CA  . LEU   A 1 265 ? 15.68509 29.97455  -26.87050 1.000 49.45301  ? 262 LEU   A CA  1 
ATOM   2151 C C   . LEU   A 1 265 ? 15.26476 29.46054  -25.49957 1.000 50.60442  ? 262 LEU   A C   1 
ATOM   2152 O O   . LEU   A 1 265 ? 15.21709 28.24603  -25.27369 1.000 52.28862  ? 262 LEU   A O   1 
ATOM   2153 C CB  . LEU   A 1 265 ? 17.14288 30.43215  -26.84809 1.000 52.32690  ? 262 LEU   A CB  1 
ATOM   2154 C CG  . LEU   A 1 265 ? 18.14708 29.42144  -26.29165 1.000 48.06293  ? 262 LEU   A CG  1 
ATOM   2155 C CD1 . LEU   A 1 265 ? 18.10228 28.12445  -27.08743 1.000 48.96996  ? 262 LEU   A CD1 1 
ATOM   2156 C CD2 . LEU   A 1 265 ? 19.54926 30.00529  -26.28847 1.000 48.81712  ? 262 LEU   A CD2 1 
ATOM   2157 N N   . LEU   A 1 266 ? 14.95079 30.36977  -24.57243 1.000 51.21914  ? 263 LEU   A N   1 
ATOM   2158 C CA  . LEU   A 1 266 ? 14.53512 29.94869  -23.23773 1.000 51.70456  ? 263 LEU   A CA  1 
ATOM   2159 C C   . LEU   A 1 266 ? 13.23563 29.15440  -23.28868 1.000 50.46445  ? 263 LEU   A C   1 
ATOM   2160 O O   . LEU   A 1 266 ? 13.06877 28.17658  -22.55005 1.000 45.55792  ? 263 LEU   A O   1 
ATOM   2161 C CB  . LEU   A 1 266 ? 14.38524 31.16522  -22.32369 1.000 47.75612  ? 263 LEU   A CB  1 
ATOM   2162 C CG  . LEU   A 1 266 ? 13.99741 30.86195  -20.87411 1.000 53.39894  ? 263 LEU   A CG  1 
ATOM   2163 C CD1 . LEU   A 1 266 ? 15.08394 30.04531  -20.19310 1.000 46.65424  ? 263 LEU   A CD1 1 
ATOM   2164 C CD2 . LEU   A 1 266 ? 13.71738 32.14354  -20.10202 1.000 45.81216  ? 263 LEU   A CD2 1 
ATOM   2165 N N   . SER   A 1 267 ? 12.30327 29.55812  -24.15668 1.000 49.75413  ? 264 SER   A N   1 
ATOM   2166 C CA  . SER   A 1 267 ? 11.04813 28.82383  -24.28838 1.000 57.67436  ? 264 SER   A CA  1 
ATOM   2167 C C   . SER   A 1 267 ? 11.29019 27.39704  -24.76376 1.000 56.09152  ? 264 SER   A C   1 
ATOM   2168 O O   . SER   A 1 267 ? 10.64291 26.45715  -24.28731 1.000 49.86998  ? 264 SER   A O   1 
ATOM   2169 C CB  . SER   A 1 267 ? 10.10845 29.55204  -25.25018 1.000 53.75299  ? 264 SER   A CB  1 
ATOM   2170 O OG  . SER   A 1 267 ? 9.76883  30.83776  -24.76339 1.000 76.98669  ? 264 SER   A OG  1 
ATOM   2171 N N   . GLN   A 1 268 ? 12.22351 27.21452  -25.70075 1.000 49.41262  ? 265 GLN   A N   1 
ATOM   2172 C CA  . GLN   A 1 268 ? 12.48820 25.88014  -26.22624 1.000 49.00070  ? 265 GLN   A CA  1 
ATOM   2173 C C   . GLN   A 1 268 ? 13.25939 25.02512  -25.22946 1.000 46.39323  ? 265 GLN   A C   1 
ATOM   2174 O O   . GLN   A 1 268 ? 13.14333 23.79471  -25.25304 1.000 50.15260  ? 265 GLN   A O   1 
ATOM   2175 C CB  . GLN   A 1 268 ? 13.24448 25.98132  -27.55050 1.000 45.06022  ? 265 GLN   A CB  1 
ATOM   2176 C CG  . GLN   A 1 268 ? 12.51094 26.79408  -28.60597 1.000 51.32637  ? 265 GLN   A CG  1 
ATOM   2177 C CD  . GLN   A 1 268 ? 13.27805 26.89039  -29.90863 1.000 55.63380  ? 265 GLN   A CD  1 
ATOM   2178 O OE1 . GLN   A 1 268 ? 13.54974 27.98467  -30.40205 1.000 63.41745  ? 265 GLN   A OE1 1 
ATOM   2179 N NE2 . GLN   A 1 268 ? 13.62490 25.74209  -30.47769 1.000 49.85364  ? 265 GLN   A NE2 1 
ATOM   2180 N N   . MET   A 1 269 ? 14.04803 25.64979  -24.35215 1.000 48.24865  ? 266 MET   A N   1 
ATOM   2181 C CA  . MET   A 1 269 ? 14.72648 24.91092  -23.29499 1.000 45.76514  ? 266 MET   A CA  1 
ATOM   2182 C C   . MET   A 1 269 ? 13.79252 24.54284  -22.15098 1.000 49.32486  ? 266 MET   A C   1 
ATOM   2183 O O   . MET   A 1 269 ? 14.10577 23.62733  -21.38245 1.000 46.49847  ? 266 MET   A O   1 
ATOM   2184 C CB  . MET   A 1 269 ? 15.90396 25.72217  -22.74823 1.000 49.57405  ? 266 MET   A CB  1 
ATOM   2185 C CG  . MET   A 1 269 ? 16.95951 26.06833  -23.78436 1.000 45.63279  ? 266 MET   A CG  1 
ATOM   2186 S SD  . MET   A 1 269 ? 18.30387 27.06666  -23.11299 1.000 51.08390  ? 266 MET   A SD  1 
ATOM   2187 C CE  . MET   A 1 269 ? 19.21323 25.83449  -22.18681 1.000 45.15407  ? 266 MET   A CE  1 
ATOM   2188 N N   . LEU   A 1 270 ? 12.65957 25.23387  -22.02008 1.000 42.25841  ? 267 LEU   A N   1 
ATOM   2189 C CA  . LEU   A 1 270 ? 11.69426 24.97263  -20.96097 1.000 44.67272  ? 267 LEU   A CA  1 
ATOM   2190 C C   . LEU   A 1 270 ? 10.40510 24.35856  -21.49496 1.000 43.63270  ? 267 LEU   A C   1 
ATOM   2191 O O   . LEU   A 1 270 ? 9.35731  24.46317  -20.84931 1.000 47.87198  ? 267 LEU   A O   1 
ATOM   2192 C CB  . LEU   A 1 270 ? 11.39585 26.25821  -20.18913 1.000 45.56172  ? 267 LEU   A CB  1 
ATOM   2193 C CG  . LEU   A 1 270 ? 12.58319 26.86762  -19.44099 1.000 51.62208  ? 267 LEU   A CG  1 
ATOM   2194 C CD1 . LEU   A 1 270 ? 12.16299 28.13130  -18.70832 1.000 46.53409  ? 267 LEU   A CD1 1 
ATOM   2195 C CD2 . LEU   A 1 270 ? 13.18419 25.85651  -18.47428 1.000 48.10628  ? 267 LEU   A CD2 1 
ATOM   2196 N N   . HIS   A 1 271 ? 10.46295 23.72679  -22.66534 1.000 51.36742  ? 268 HIS   A N   1 
ATOM   2197 C CA  . HIS   A 1 271 ? 9.30475  23.02389  -23.19747 1.000 48.65952  ? 268 HIS   A CA  1 
ATOM   2198 C C   . HIS   A 1 271 ? 8.93049  21.86453  -22.28113 1.000 49.85396  ? 268 HIS   A C   1 
ATOM   2199 O O   . HIS   A 1 271 ? 9.79798  21.14068  -21.78305 1.000 48.08428  ? 268 HIS   A O   1 
ATOM   2200 C CB  . HIS   A 1 271 ? 9.60584  22.51158  -24.60710 1.000 49.23074  ? 268 HIS   A CB  1 
ATOM   2201 C CG  . HIS   A 1 271 ? 8.38424  22.19975  -25.41401 1.000 64.82441  ? 268 HIS   A CG  1 
ATOM   2202 N ND1 . HIS   A 1 271 ? 7.51078  21.18608  -25.08347 1.000 66.75629  ? 268 HIS   A ND1 1 
ATOM   2203 C CD2 . HIS   A 1 271 ? 7.89421  22.76507  -26.54272 1.000 67.35550  ? 268 HIS   A CD2 1 
ATOM   2204 C CE1 . HIS   A 1 271 ? 6.53281  21.14335  -25.97065 1.000 76.38794  ? 268 HIS   A CE1 1 
ATOM   2205 N NE2 . HIS   A 1 271 ? 6.74224  22.09046  -26.86727 1.000 71.64506  ? 268 HIS   A NE2 1 
ATOM   2206 N N   . TYR   A 1 272 ? 7.62556  21.69665  -22.05084 1.000 44.76951  ? 269 TYR   A N   1 
ATOM   2207 C CA  . TYR   A 1 272 ? 7.15974  20.62671  -21.17255 1.000 46.26139  ? 269 TYR   A CA  1 
ATOM   2208 C C   . TYR   A 1 272 ? 7.51303  19.25545  -21.73581 1.000 56.97271  ? 269 TYR   A C   1 
ATOM   2209 O O   . TYR   A 1 272 ? 8.03696  18.39355  -21.02041 1.000 53.25560  ? 269 TYR   A O   1 
ATOM   2210 C CB  . TYR   A 1 272 ? 5.65061  20.74050  -20.95386 1.000 46.40095  ? 269 TYR   A CB  1 
ATOM   2211 C CG  . TYR   A 1 272 ? 5.25067  21.66957  -19.83134 1.000 49.64596  ? 269 TYR   A CG  1 
ATOM   2212 C CD1 . TYR   A 1 272 ? 5.63088  21.40900  -18.52071 1.000 53.44293  ? 269 TYR   A CD1 1 
ATOM   2213 C CD2 . TYR   A 1 272 ? 4.47678  22.79583  -20.07745 1.000 56.33927  ? 269 TYR   A CD2 1 
ATOM   2214 C CE1 . TYR   A 1 272 ? 5.26265  22.25206  -17.48817 1.000 52.15127  ? 269 TYR   A CE1 1 
ATOM   2215 C CE2 . TYR   A 1 272 ? 4.10265  23.64391  -19.05202 1.000 48.03841  ? 269 TYR   A CE2 1 
ATOM   2216 C CZ  . TYR   A 1 272 ? 4.49810  23.36711  -17.75945 1.000 57.69025  ? 269 TYR   A CZ  1 
ATOM   2217 O OH  . TYR   A 1 272 ? 4.12745  24.20816  -16.73606 1.000 55.13018  ? 269 TYR   A OH  1 
ATOM   2218 N N   . ASP   A 1 273 ? 7.23091  19.03684  -23.01145 1.000 48.80811  ? 270 ASP   A N   1 
ATOM   2219 C CA  . ASP   A 1 273 ? 7.47079  17.75071  -23.65353 1.000 51.90573  ? 270 ASP   A CA  1 
ATOM   2220 C C   . ASP   A 1 273 ? 8.96678  17.49525  -23.78366 1.000 51.14714  ? 270 ASP   A C   1 
ATOM   2221 O O   . ASP   A 1 273 ? 9.64870  18.24472  -24.49589 1.000 48.84480  ? 270 ASP   A O   1 
ATOM   2222 C CB  . ASP   A 1 273 ? 6.79800  17.72375  -25.02775 1.000 53.28042  ? 270 ASP   A CB  1 
ATOM   2223 C CG  . ASP   A 1 273 ? 6.76283  16.33346  -25.64201 1.000 64.82400  ? 270 ASP   A CG  1 
ATOM   2224 O OD1 . ASP   A 1 273 ? 7.36149  15.39918  -25.06837 1.000 59.26544  ? 270 ASP   A OD1 1 
ATOM   2225 O OD2 . ASP   A 1 273 ? 6.12562  16.17446  -26.70533 1.000 69.88818  ? 270 ASP   A OD2 1 
ATOM   2226 N N   . PRO   A 1 274 ? 9.51842  16.47079  -23.12697 1.000 53.05703  ? 271 PRO   A N   1 
ATOM   2227 C CA  . PRO   A 1 274 ? 10.95659 16.19669  -23.27955 1.000 45.59062  ? 271 PRO   A CA  1 
ATOM   2228 C C   . PRO   A 1 274 ? 11.35000 15.83487  -24.69932 1.000 50.12468  ? 271 PRO   A C   1 
ATOM   2229 O O   . PRO   A 1 274 ? 12.49981 16.06864  -25.09265 1.000 47.62358  ? 271 PRO   A O   1 
ATOM   2230 C CB  . PRO   A 1 274 ? 11.19585 15.02639  -22.31337 1.000 42.11205  ? 271 PRO   A CB  1 
ATOM   2231 C CG  . PRO   A 1 274 ? 10.03239 15.04845  -21.37427 1.000 50.65251  ? 271 PRO   A CG  1 
ATOM   2232 C CD  . PRO   A 1 274 ? 8.87668  15.54852  -22.17708 1.000 44.64460  ? 271 PRO   A CD  1 
ATOM   2233 N N   . ASN   A 1 275 ? 10.42785 15.26830  -25.48222 1.000 55.82103  ? 272 ASN   A N   1 
ATOM   2234 C CA  . ASN   A 1 275 ? 10.73422 14.93435  -26.86889 1.000 54.23267  ? 272 ASN   A CA  1 
ATOM   2235 C C   . ASN   A 1 275 ? 10.81995 16.18067  -27.74031 1.000 58.56278  ? 272 ASN   A C   1 
ATOM   2236 O O   . ASN   A 1 275 ? 11.53256 16.18220  -28.75076 1.000 61.01612  ? 272 ASN   A O   1 
ATOM   2237 C CB  . ASN   A 1 275 ? 9.68022  13.97346  -27.41944 1.000 54.99457  ? 272 ASN   A CB  1 
ATOM   2238 C CG  . ASN   A 1 275 ? 9.56673  12.70100  -26.60045 1.000 72.46426  ? 272 ASN   A CG  1 
ATOM   2239 O OD1 . ASN   A 1 275 ? 10.56577 12.17173  -26.11281 1.000 73.83116  ? 272 ASN   A OD1 1 
ATOM   2240 N ND2 . ASN   A 1 275 ? 8.34467  12.20566  -26.44182 1.000 80.93590  ? 272 ASN   A ND2 1 
ATOM   2241 N N   . LYS   A 1 276 ? 10.10284 17.24281  -27.37095 1.000 51.89476  ? 273 LYS   A N   1 
ATOM   2242 C CA  . LYS   A 1 276 ? 10.12356 18.49466  -28.11536 1.000 51.95051  ? 273 LYS   A CA  1 
ATOM   2243 C C   . LYS   A 1 276 ? 11.12428 19.50101  -27.56841 1.000 58.71217  ? 273 LYS   A C   1 
ATOM   2244 O O   . LYS   A 1 276 ? 11.44527 20.47019  -28.26564 1.000 51.12494  ? 273 LYS   A O   1 
ATOM   2245 C CB  . LYS   A 1 276 ? 8.73004  19.13666  -28.11969 1.000 56.37223  ? 273 LYS   A CB  1 
ATOM   2246 C CG  . LYS   A 1 276 ? 7.65930  18.30484  -28.80438 1.000 70.94039  ? 273 LYS   A CG  1 
ATOM   2247 C CD  . LYS   A 1 276 ? 7.99134  18.07746  -30.26840 1.000 67.92523  ? 273 LYS   A CD  1 
ATOM   2248 C CE  . LYS   A 1 276 ? 6.86335  17.35128  -30.98007 1.000 88.45588  ? 273 LYS   A CE  1 
ATOM   2249 N NZ  . LYS   A 1 276 ? 7.14429  17.17356  -32.43073 1.000 91.01436  ? 273 LYS   A NZ  1 
ATOM   2250 N N   . ARG   A 1 277 ? 11.61273 19.29873  -26.34585 1.000 45.98512  ? 274 ARG   A N   1 
ATOM   2251 C CA  . ARG   A 1 277 ? 12.56952 20.22229  -25.75344 1.000 44.79473  ? 274 ARG   A CA  1 
ATOM   2252 C C   . ARG   A 1 277 ? 13.83124 20.28777  -26.60414 1.000 47.56580  ? 274 ARG   A C   1 
ATOM   2253 O O   . ARG   A 1 277 ? 14.33871 19.26407  -27.07121 1.000 47.25887  ? 274 ARG   A O   1 
ATOM   2254 C CB  . ARG   A 1 277 ? 12.90339 19.78038  -24.32769 1.000 39.58636  ? 274 ARG   A CB  1 
ATOM   2255 C CG  . ARG   A 1 277 ? 13.53483 20.85019  -23.45092 1.000 38.33792  ? 274 ARG   A CG  1 
ATOM   2256 C CD  . ARG   A 1 277 ? 13.65619 20.34818  -22.01795 1.000 40.69931  ? 274 ARG   A CD  1 
ATOM   2257 N NE  . ARG   A 1 277 ? 12.35561 19.97098  -21.47559 1.000 45.00749  ? 274 ARG   A NE  1 
ATOM   2258 C CZ  . ARG   A 1 277 ? 12.17545 19.11635  -20.47763 1.000 40.34707  ? 274 ARG   A CZ  1 
ATOM   2259 N NH1 . ARG   A 1 277 ? 13.19609 18.50908  -19.89380 1.000 42.21809  ? 274 ARG   A NH1 1 
ATOM   2260 N NH2 . ARG   A 1 277 ? 10.93937 18.85771  -20.06077 1.000 37.57677  ? 274 ARG   A NH2 1 
ATOM   2261 N N   . ILE   A 1 278 ? 14.33210 21.50835  -26.81115 1.000 47.60809  ? 275 ILE   A N   1 
ATOM   2262 C CA  . ILE   A 1 278 ? 15.46273 21.70260  -27.70729 1.000 43.16601  ? 275 ILE   A CA  1 
ATOM   2263 C C   . ILE   A 1 278 ? 16.68978 20.97140  -27.16633 1.000 50.16065  ? 275 ILE   A C   1 
ATOM   2264 O O   . ILE   A 1 278 ? 16.88495 20.84127  -25.95103 1.000 46.01252  ? 275 ILE   A O   1 
ATOM   2265 C CB  . ILE   A 1 278 ? 15.74563 23.20266  -27.90564 1.000 47.93948  ? 275 ILE   A CB  1 
ATOM   2266 C CG1 . ILE   A 1 278 ? 16.71357 23.42338  -29.06898 1.000 49.94495  ? 275 ILE   A CG1 1 
ATOM   2267 C CG2 . ILE   A 1 278 ? 16.29455 23.82883  -26.62664 1.000 38.15211  ? 275 ILE   A CG2 1 
ATOM   2268 C CD1 . ILE   A 1 278 ? 16.90520 24.87905  -29.43591 1.000 52.76389  ? 275 ILE   A CD1 1 
ATOM   2269 N N   . SER   A 1 279 ? 17.50867 20.46289  -28.08004 1.000 49.62943  ? 276 SER   A N   1 
ATOM   2270 C CA  . SER   A 1 279 ? 18.73011 19.77185  -27.70299 1.000 47.76040  ? 276 SER   A CA  1 
ATOM   2271 C C   . SER   A 1 279 ? 19.87738 20.76503  -27.56925 1.000 47.08754  ? 276 SER   A C   1 
ATOM   2272 O O   . SER   A 1 279 ? 19.81508 21.89460  -28.06096 1.000 45.62547  ? 276 SER   A O   1 
ATOM   2273 C CB  . SER   A 1 279 ? 19.08742 18.69743  -28.72912 1.000 52.26369  ? 276 SER   A CB  1 
ATOM   2274 O OG  . SER   A 1 279 ? 19.51755 19.27766  -29.94864 1.000 48.68316  ? 276 SER   A OG  1 
ATOM   2275 N N   . ALA   A 1 280 ? 20.93649 20.32479  -26.88690 1.000 43.91614  ? 277 ALA   A N   1 
ATOM   2276 C CA  . ALA   A 1 280 ? 22.11328 21.17137  -26.72149 1.000 50.30586  ? 277 ALA   A CA  1 
ATOM   2277 C C   . ALA   A 1 280 ? 22.72344 21.52970  -28.07091 1.000 51.99062  ? 277 ALA   A C   1 
ATOM   2278 O O   . ALA   A 1 280 ? 23.11046 22.68052  -28.30521 1.000 48.67261  ? 277 ALA   A O   1 
ATOM   2279 C CB  . ALA   A 1 280 ? 23.14096 20.47339  -25.83143 1.000 44.06909  ? 277 ALA   A CB  1 
ATOM   2280 N N   . LYS   A 1 281 ? 22.81074 20.55265  -28.97618 1.000 53.28782  ? 278 LYS   A N   1 
ATOM   2281 C CA  . LYS   A 1 281 ? 23.36502 20.81373  -30.30074 1.000 52.92224  ? 278 LYS   A CA  1 
ATOM   2282 C C   . LYS   A 1 281 ? 22.51656 21.82910  -31.05802 1.000 56.02577  ? 278 LYS   A C   1 
ATOM   2283 O O   . LYS   A 1 281 ? 23.04357 22.77352  -31.65802 1.000 51.07469  ? 278 LYS   A O   1 
ATOM   2284 C CB  . LYS   A 1 281 ? 23.47718 19.50463  -31.08331 1.000 51.32251  ? 278 LYS   A CB  1 
ATOM   2285 C CG  . LYS   A 1 281 ? 24.11959 19.64544  -32.45659 1.000 51.52050  ? 278 LYS   A CG  1 
ATOM   2286 C CD  . LYS   A 1 281 ? 24.11308 18.31799  -33.20074 1.000 74.09481  ? 278 LYS   A CD  1 
ATOM   2287 C CE  . LYS   A 1 281 ? 24.81567 18.42609  -34.54534 1.000 89.85058  ? 278 LYS   A CE  1 
ATOM   2288 N NZ  . LYS   A 1 281 ? 26.26431 18.73139  -34.39203 1.000 84.39902  ? 278 LYS   A NZ  1 
ATOM   2289 N N   . ALA   A 1 282 ? 21.19198 21.65628  -31.02957 1.000 50.29412  ? 279 ALA   A N   1 
ATOM   2290 C CA  . ALA   A 1 282 ? 20.30936 22.59059  -31.72110 1.000 52.13880  ? 279 ALA   A CA  1 
ATOM   2291 C C   . ALA   A 1 282 ? 20.32577 23.96814  -31.07093 1.000 51.74831  ? 279 ALA   A C   1 
ATOM   2292 O O   . ALA   A 1 282 ? 20.18307 24.98090  -31.76566 1.000 50.80451  ? 279 ALA   A O   1 
ATOM   2293 C CB  . ALA   A 1 282 ? 18.88301 22.04122  -31.76099 1.000 49.23438  ? 279 ALA   A CB  1 
ATOM   2294 N N   . ALA   A 1 283 ? 20.49703 24.03115  -29.74802 1.000 48.50835  ? 280 ALA   A N   1 
ATOM   2295 C CA  . ALA   A 1 283 ? 20.53845 25.32650  -29.07625 1.000 49.38473  ? 280 ALA   A CA  1 
ATOM   2296 C C   . ALA   A 1 283 ? 21.74350 26.14244  -29.52639 1.000 47.62582  ? 280 ALA   A C   1 
ATOM   2297 O O   . ALA   A 1 283 ? 21.67430 27.37475  -29.60795 1.000 56.50458  ? 280 ALA   A O   1 
ATOM   2298 C CB  . ALA   A 1 283 ? 20.55330 25.13376  -27.55977 1.000 44.04967  ? 280 ALA   A CB  1 
ATOM   2299 N N   . LEU   A 1 284 ? 22.85713 25.47087  -29.82939 1.000 49.60825  ? 281 LEU   A N   1 
ATOM   2300 C CA  . LEU   A 1 284 ? 24.03871 26.17706  -30.31154 1.000 43.95951  ? 281 LEU   A CA  1 
ATOM   2301 C C   . LEU   A 1 284 ? 23.78167 26.85299  -31.65212 1.000 56.31516  ? 281 LEU   A C   1 
ATOM   2302 O O   . LEU   A 1 284 ? 24.41957 27.86345  -31.96892 1.000 54.18317  ? 281 LEU   A O   1 
ATOM   2303 C CB  . LEU   A 1 284 ? 25.21837 25.21021  -30.41711 1.000 56.67726  ? 281 LEU   A CB  1 
ATOM   2304 C CG  . LEU   A 1 284 ? 25.76257 24.67005  -29.09260 1.000 57.75745  ? 281 LEU   A CG  1 
ATOM   2305 C CD1 . LEU   A 1 284 ? 26.76274 23.55436  -29.33832 1.000 55.66482  ? 281 LEU   A CD1 1 
ATOM   2306 C CD2 . LEU   A 1 284 ? 26.40101 25.78972  -28.28914 1.000 55.03241  ? 281 LEU   A CD2 1 
ATOM   2307 N N   . ALA   A 1 285 ? 22.85437 26.32082  -32.44494 1.000 58.05238  ? 282 ALA   A N   1 
ATOM   2308 C CA  . ALA   A 1 285 ? 22.51310 26.88556  -33.74314 1.000 53.87415  ? 282 ALA   A CA  1 
ATOM   2309 C C   . ALA   A 1 285 ? 21.39708 27.91904  -33.66763 1.000 58.76573  ? 282 ALA   A C   1 
ATOM   2310 O O   . ALA   A 1 285 ? 20.95680 28.41171  -34.71178 1.000 66.01483  ? 282 ALA   A O   1 
ATOM   2311 C CB  . ALA   A 1 285 ? 22.11667 25.76629  -34.71187 1.000 57.38664  ? 282 ALA   A CB  1 
ATOM   2312 N N   . HIS   A 1 286 ? 20.93575 28.25698  -32.46686 1.000 55.41139  ? 283 HIS   A N   1 
ATOM   2313 C CA  . HIS   A 1 286 ? 19.85877 29.22107  -32.31978 1.000 58.30622  ? 283 HIS   A CA  1 
ATOM   2314 C C   . HIS   A 1 286 ? 20.34927 30.62608  -32.67322 1.000 62.40496  ? 283 HIS   A C   1 
ATOM   2315 O O   . HIS   A 1 286 ? 21.50075 30.97606  -32.40469 1.000 67.25908  ? 283 HIS   A O   1 
ATOM   2316 C CB  . HIS   A 1 286 ? 19.31916 29.20160  -30.89027 1.000 58.46523  ? 283 HIS   A CB  1 
ATOM   2317 C CG  . HIS   A 1 286 ? 18.00574 29.90167  -30.72844 1.000 60.44510  ? 283 HIS   A CG  1 
ATOM   2318 N ND1 . HIS   A 1 286 ? 17.90763 31.25411  -30.48212 1.000 54.38443  ? 283 HIS   A ND1 1 
ATOM   2319 C CD2 . HIS   A 1 286 ? 16.73535 29.43565  -30.77922 1.000 60.04846  ? 283 HIS   A CD2 1 
ATOM   2320 C CE1 . HIS   A 1 286 ? 16.63374 31.59125  -30.38829 1.000 65.50471  ? 283 HIS   A CE1 1 
ATOM   2321 N NE2 . HIS   A 1 286 ? 15.90162 30.50603  -30.56388 1.000 60.49469  ? 283 HIS   A NE2 1 
ATOM   2322 N N   . PRO   A 1 287 ? 19.48918 31.44845  -33.28499 1.000 68.03009  ? 284 PRO   A N   1 
ATOM   2323 C CA  . PRO   A 1 287 ? 19.89505 32.82352  -33.62591 1.000 67.48480  ? 284 PRO   A CA  1 
ATOM   2324 C C   . PRO   A 1 287 ? 20.30145 33.67134  -32.42786 1.000 70.19985  ? 284 PRO   A C   1 
ATOM   2325 O O   . PRO   A 1 287 ? 20.81412 34.77960  -32.62784 1.000 70.56491  ? 284 PRO   A O   1 
ATOM   2326 C CB  . PRO   A 1 287 ? 18.64662 33.39516  -34.30994 1.000 73.02816  ? 284 PRO   A CB  1 
ATOM   2327 C CG  . PRO   A 1 287 ? 17.92828 32.19897  -34.84113 1.000 71.48363  ? 284 PRO   A CG  1 
ATOM   2328 C CD  . PRO   A 1 287 ? 18.16989 31.10552  -33.84111 1.000 65.10000  ? 284 PRO   A CD  1 
ATOM   2329 N N   . PHE   A 1 288 ? 20.07650 33.20380  -31.19808 1.000 67.93087  ? 285 PHE   A N   1 
ATOM   2330 C CA  . PHE   A 1 288 ? 20.56630 33.93396  -30.03440 1.000 69.53879  ? 285 PHE   A CA  1 
ATOM   2331 C C   . PHE   A 1 288 ? 22.08804 33.99505  -30.02072 1.000 62.81408  ? 285 PHE   A C   1 
ATOM   2332 O O   . PHE   A 1 288 ? 22.66681 34.94150  -29.47560 1.000 71.02069  ? 285 PHE   A O   1 
ATOM   2333 C CB  . PHE   A 1 288 ? 20.03792 33.28656  -28.75272 1.000 60.04649  ? 285 PHE   A CB  1 
ATOM   2334 C CG  . PHE   A 1 288 ? 20.43809 34.00578  -27.49464 1.000 61.80171  ? 285 PHE   A CG  1 
ATOM   2335 C CD1 . PHE   A 1 288 ? 19.93102 35.26227  -27.20710 1.000 69.94689  ? 285 PHE   A CD1 1 
ATOM   2336 C CD2 . PHE   A 1 288 ? 21.30890 33.41790  -26.59194 1.000 55.45198  ? 285 PHE   A CD2 1 
ATOM   2337 C CE1 . PHE   A 1 288 ? 20.29349 35.92444  -26.04762 1.000 62.45771  ? 285 PHE   A CE1 1 
ATOM   2338 C CE2 . PHE   A 1 288 ? 21.67456 34.07452  -25.42944 1.000 61.70863  ? 285 PHE   A CE2 1 
ATOM   2339 C CZ  . PHE   A 1 288 ? 21.16589 35.32907  -25.15751 1.000 63.85772  ? 285 PHE   A CZ  1 
ATOM   2340 N N   . PHE   A 1 289 ? 22.75020 33.00420  -30.62175 1.000 71.80955  ? 286 PHE   A N   1 
ATOM   2341 C CA  . PHE   A 1 289 ? 24.20252 32.97642  -30.73980 1.000 72.07937  ? 286 PHE   A CA  1 
ATOM   2342 C C   . PHE   A 1 289 ? 24.67230 33.28947  -32.15687 1.000 83.94947  ? 286 PHE   A C   1 
ATOM   2343 O O   . PHE   A 1 289 ? 25.79485 32.92955  -32.52513 1.000 95.11963  ? 286 PHE   A O   1 
ATOM   2344 C CB  . PHE   A 1 289 ? 24.75166 31.61705  -30.30249 1.000 60.61295  ? 286 PHE   A CB  1 
ATOM   2345 C CG  . PHE   A 1 289 ? 24.24780 31.15428  -28.96556 1.000 59.47426  ? 286 PHE   A CG  1 
ATOM   2346 C CD1 . PHE   A 1 289 ? 24.71742 31.72705  -27.79556 1.000 59.48806  ? 286 PHE   A CD1 1 
ATOM   2347 C CD2 . PHE   A 1 289 ? 23.31757 30.13274  -28.87913 1.000 52.50352  ? 286 PHE   A CD2 1 
ATOM   2348 C CE1 . PHE   A 1 289 ? 24.25960 31.29801  -26.56470 1.000 54.32585  ? 286 PHE   A CE1 1 
ATOM   2349 C CE2 . PHE   A 1 289 ? 22.85594 29.69751  -27.65040 1.000 51.39725  ? 286 PHE   A CE2 1 
ATOM   2350 C CZ  . PHE   A 1 289 ? 23.32718 30.28110  -26.49196 1.000 50.35320  ? 286 PHE   A CZ  1 
ATOM   2351 N N   . GLN   A 1 290 ? 23.83555 33.95068  -32.96200 1.000 79.33164  ? 287 GLN   A N   1 
ATOM   2352 C CA  . GLN   A 1 290 ? 24.19566 34.21374  -34.35173 1.000 98.57333  ? 287 GLN   A CA  1 
ATOM   2353 C C   . GLN   A 1 290 ? 25.41340 35.12084  -34.47197 1.000 115.93397 ? 287 GLN   A C   1 
ATOM   2354 O O   . GLN   A 1 290 ? 26.08012 35.10972  -35.51243 1.000 123.73014 ? 287 GLN   A O   1 
ATOM   2355 C CB  . GLN   A 1 290 ? 23.00548 34.82368  -35.09933 1.000 88.34979  ? 287 GLN   A CB  1 
ATOM   2356 C CG  . GLN   A 1 290 ? 22.67608 36.26069  -34.71640 1.000 95.54057  ? 287 GLN   A CG  1 
ATOM   2357 C CD  . GLN   A 1 290 ? 23.34499 37.27867  -35.62095 1.000 116.36865 ? 287 GLN   A CD  1 
ATOM   2358 O OE1 . GLN   A 1 290 ? 23.44926 37.07800  -36.83146 1.000 119.88749 ? 287 GLN   A OE1 1 
ATOM   2359 N NE2 . GLN   A 1 290 ? 23.80648 38.37731  -35.03488 1.000 114.42137 ? 287 GLN   A NE2 1 
ATOM   2360 N N   . ASP   A 1 291 ? 25.71842 35.90179  -33.43561 1.000 113.70833 ? 288 ASP   A N   1 
ATOM   2361 C CA  . ASP   A 1 291 ? 26.89846 36.75475  -33.43343 1.000 113.45839 ? 288 ASP   A CA  1 
ATOM   2362 C C   . ASP   A 1 291 ? 28.10980 36.08969  -32.79437 1.000 124.38654 ? 288 ASP   A C   1 
ATOM   2363 O O   . ASP   A 1 291 ? 29.24467 36.46299  -33.11405 1.000 129.38963 ? 288 ASP   A O   1 
ATOM   2364 C CB  . ASP   A 1 291 ? 26.59784 38.06984  -32.70544 1.000 121.40153 ? 288 ASP   A CB  1 
ATOM   2365 C CG  . ASP   A 1 291 ? 25.99277 37.85013  -31.32996 1.000 118.21123 ? 288 ASP   A CG  1 
ATOM   2366 O OD1 . ASP   A 1 291 ? 25.69255 36.68646  -30.98811 1.000 110.72002 ? 288 ASP   A OD1 1 
ATOM   2367 O OD2 . ASP   A 1 291 ? 25.81813 38.84059  -30.58913 1.000 112.38035 ? 288 ASP   A OD2 1 
ATOM   2368 N N   . VAL   A 1 292 ? 27.89855 35.11619  -31.90669 1.000 119.41663 ? 289 VAL   A N   1 
ATOM   2369 C CA  . VAL   A 1 292 ? 29.01909 34.45530  -31.24543 1.000 117.19816 ? 289 VAL   A CA  1 
ATOM   2370 C C   . VAL   A 1 292 ? 29.65208 33.41573  -32.16104 1.000 120.51786 ? 289 VAL   A C   1 
ATOM   2371 O O   . VAL   A 1 292 ? 30.87982 33.28061  -32.20904 1.000 128.62490 ? 289 VAL   A O   1 
ATOM   2372 C CB  . VAL   A 1 292 ? 28.55797 33.83326  -29.91424 1.000 108.31107 ? 289 VAL   A CB  1 
ATOM   2373 C CG1 . VAL   A 1 292 ? 29.71497 33.12106  -29.22538 1.000 101.75137 ? 289 VAL   A CG1 1 
ATOM   2374 C CG2 . VAL   A 1 292 ? 27.97099 34.90007  -29.00731 1.000 102.24759 ? 289 VAL   A CG2 1 
ATOM   2375 N N   . THR   A 1 293 ? 28.83527 32.67262  -32.90322 1.000 105.71722 ? 290 THR   A N   1 
ATOM   2376 C CA  . THR   A 1 293 ? 29.32107 31.61006  -33.76841 1.000 100.58615 ? 290 THR   A CA  1 
ATOM   2377 C C   . THR   A 1 293 ? 28.78079 31.80046  -35.17832 1.000 116.54631 ? 290 THR   A C   1 
ATOM   2378 O O   . THR   A 1 293 ? 27.80659 32.52286  -35.40497 1.000 115.96184 ? 290 THR   A O   1 
ATOM   2379 C CB  . THR   A 1 293 ? 28.91765 30.22292  -33.24565 1.000 95.06011  ? 290 THR   A CB  1 
ATOM   2380 O OG1 . THR   A 1 293 ? 29.46880 29.20950  -34.09600 1.000 96.35455  ? 290 THR   A OG1 1 
ATOM   2381 C CG2 . THR   A 1 293 ? 27.40247 30.08390  -33.22029 1.000 78.31263  ? 290 THR   A CG2 1 
ATOM   2382 N N   . LYS   A 1 294 ? 29.43701 31.13760  -36.12915 1.000 109.10900 ? 291 LYS   A N   1 
ATOM   2383 C CA  . LYS   A 1 294 ? 29.00906 31.10227  -37.51361 1.000 120.24255 ? 291 LYS   A CA  1 
ATOM   2384 C C   . LYS   A 1 294 ? 28.77914 29.65984  -37.94739 1.000 127.42824 ? 291 LYS   A C   1 
ATOM   2385 O O   . LYS   A 1 294 ? 29.52062 28.76386  -37.52880 1.000 124.22033 ? 291 LYS   A O   1 
ATOM   2386 C CB  . LYS   A 1 294 ? 30.04830 31.76019  -38.43476 1.000 129.69894 ? 291 LYS   A CB  1 
ATOM   2387 C CG  . LYS   A 1 294 ? 29.52179 32.96978  -39.19174 1.000 126.92502 ? 291 LYS   A CG  1 
ATOM   2388 C CD  . LYS   A 1 294 ? 28.94923 34.00824  -38.23890 1.000 130.43848 ? 291 LYS   A CD  1 
ATOM   2389 C CE  . LYS   A 1 294 ? 28.35206 35.18602  -38.99253 1.000 128.63232 ? 291 LYS   A CE  1 
ATOM   2390 N NZ  . LYS   A 1 294 ? 27.74975 36.18626  -38.06737 1.000 114.84589 ? 291 LYS   A NZ  1 
ATOM   2391 N N   . PRO   A 1 295 ? 27.76467 29.40098  -38.77270 1.000 133.92460 ? 292 PRO   A N   1 
ATOM   2392 C CA  . PRO   A 1 295 ? 27.45282 28.01345  -39.14388 1.000 132.87603 ? 292 PRO   A CA  1 
ATOM   2393 C C   . PRO   A 1 295 ? 28.54825 27.41174  -40.01275 1.000 133.55187 ? 292 PRO   A C   1 
ATOM   2394 O O   . PRO   A 1 295 ? 29.03068 28.04085  -40.95704 1.000 124.96167 ? 292 PRO   A O   1 
ATOM   2395 C CB  . PRO   A 1 295 ? 26.12953 28.13918  -39.90761 1.000 129.80492 ? 292 PRO   A CB  1 
ATOM   2396 C CG  . PRO   A 1 295 ? 26.13777 29.53506  -40.43741 1.000 134.61422 ? 292 PRO   A CG  1 
ATOM   2397 C CD  . PRO   A 1 295 ? 26.84109 30.36334  -39.39814 1.000 132.17038 ? 292 PRO   A CD  1 
ATOM   2398 N N   . VAL   A 1 296 ? 28.93913 26.18564  -39.68067 1.000 150.51319 ? 293 VAL   A N   1 
ATOM   2399 C CA  . VAL   A 1 296 ? 29.94160 25.44975  -40.44624 1.000 143.31553 ? 293 VAL   A CA  1 
ATOM   2400 C C   . VAL   A 1 296 ? 29.25137 24.83065  -41.65682 1.000 138.75489 ? 293 VAL   A C   1 
ATOM   2401 O O   . VAL   A 1 296 ? 28.09470 24.39559  -41.55183 1.000 141.37465 ? 293 VAL   A O   1 
ATOM   2402 C CB  . VAL   A 1 296 ? 30.64290 24.39283  -39.57343 1.000 136.78962 ? 293 VAL   A CB  1 
ATOM   2403 C CG1 . VAL   A 1 296 ? 29.98877 24.31635  -38.20025 1.000 137.70479 ? 293 VAL   A CG1 1 
ATOM   2404 C CG2 . VAL   A 1 296 ? 30.63774 23.02351  -40.24581 1.000 128.40389 ? 293 VAL   A CG2 1 
ATOM   2405 N N   . PRO   A 1 297 ? 29.89837 24.79699  -42.82151 1.000 116.44467 ? 294 PRO   A N   1 
ATOM   2406 C CA  . PRO   A 1 297 ? 29.26815 24.18525  -43.99930 1.000 111.58265 ? 294 PRO   A CA  1 
ATOM   2407 C C   . PRO   A 1 297 ? 28.98471 22.70804  -43.76758 1.000 105.42620 ? 294 PRO   A C   1 
ATOM   2408 O O   . PRO   A 1 297 ? 29.87131 21.93774  -43.39232 1.000 120.29620 ? 294 PRO   A O   1 
ATOM   2409 C CB  . PRO   A 1 297 ? 30.30690 24.39720  -45.10746 1.000 113.55122 ? 294 PRO   A CB  1 
ATOM   2410 C CG  . PRO   A 1 297 ? 31.14643 25.54116  -44.63210 1.000 115.39632 ? 294 PRO   A CG  1 
ATOM   2411 C CD  . PRO   A 1 297 ? 31.20125 25.40293  -43.14138 1.000 112.22432 ? 294 PRO   A CD  1 
ATOM   2412 N N   . HIS   A 1 298 ? 27.73424 22.31809  -43.99478 1.000 103.22760 ? 295 HIS   A N   1 
ATOM   2413 C CA  . HIS   A 1 298 ? 27.28218 20.95291  -43.76533 1.000 117.17053 ? 295 HIS   A CA  1 
ATOM   2414 C C   . HIS   A 1 298 ? 27.30076 20.17025  -45.07096 1.000 98.94994  ? 295 HIS   A C   1 
ATOM   2415 O O   . HIS   A 1 298 ? 26.73828 20.61560  -46.07677 1.000 103.40707 ? 295 HIS   A O   1 
ATOM   2416 C CB  . HIS   A 1 298 ? 25.87554 20.93786  -43.16411 1.000 122.80063 ? 295 HIS   A CB  1 
ATOM   2417 C CG  . HIS   A 1 298 ? 25.81935 21.40877  -41.74436 1.000 128.59951 ? 295 HIS   A CG  1 
ATOM   2418 N ND1 . HIS   A 1 298 ? 26.94659 21.74665  -41.02684 1.000 135.69993 ? 295 HIS   A ND1 1 
ATOM   2419 C CD2 . HIS   A 1 298 ? 24.77109 21.59482  -40.90763 1.000 129.46509 ? 295 HIS   A CD2 1 
ATOM   2420 C CE1 . HIS   A 1 298 ? 26.59521 22.12194  -39.80989 1.000 138.54034 ? 295 HIS   A CE1 1 
ATOM   2421 N NE2 . HIS   A 1 298 ? 25.28060 22.03895  -39.71168 1.000 137.48910 ? 295 HIS   A NE2 1 
ATOM   2422 N N   . LEU   A 1 299 ? 27.94781 19.00742  -45.04880 1.000 105.83687 ? 296 LEU   A N   1 
ATOM   2423 C CA  . LEU   A 1 299 ? 27.94657 18.10360  -46.19412 1.000 102.32557 ? 296 LEU   A CA  1 
ATOM   2424 C C   . LEU   A 1 299 ? 26.58127 17.43625  -46.30133 1.000 111.48162 ? 296 LEU   A C   1 
ATOM   2425 O O   . LEU   A 1 299 ? 26.23111 16.58459  -45.47808 1.000 112.33413 ? 296 LEU   A O   1 
ATOM   2426 C CB  . LEU   A 1 299 ? 29.05439 17.06487  -46.04661 1.000 90.92938  ? 296 LEU   A CB  1 
ATOM   2427 C CG  . LEU   A 1 299 ? 29.04670 15.89428  -47.03320 1.000 96.00383  ? 296 LEU   A CG  1 
ATOM   2428 C CD1 . LEU   A 1 299 ? 29.30725 16.37240  -48.45304 1.000 98.35172  ? 296 LEU   A CD1 1 
ATOM   2429 C CD2 . LEU   A 1 299 ? 30.06151 14.83784  -46.62328 1.000 91.80664  ? 296 LEU   A CD2 1 
ATOM   2430 N N   . ARG   A 1 300 ? 25.80390 17.82360  -47.31150 1.000 132.78973 ? 297 ARG   A N   1 
ATOM   2431 C CA  . ARG   A 1 300 ? 24.46140 17.27514  -47.50779 1.000 142.45188 ? 297 ARG   A CA  1 
ATOM   2432 C C   . ARG   A 1 300 ? 24.53683 16.04650  -48.41630 1.000 139.83420 ? 297 ARG   A C   1 
ATOM   2433 O O   . ARG   A 1 300 ? 24.03404 16.01667  -49.54118 1.000 139.20048 ? 297 ARG   A O   1 
ATOM   2434 C CB  . ARG   A 1 300 ? 23.52791 18.34323  -48.06397 1.000 151.57155 ? 297 ARG   A CB  1 
ATOM   2435 C CG  . ARG   A 1 300 ? 24.11969 19.17355  -49.19338 1.000 148.31407 ? 297 ARG   A CG  1 
ATOM   2436 C CD  . ARG   A 1 300 ? 23.24721 20.37976  -49.51791 1.000 161.38987 ? 297 ARG   A CD  1 
ATOM   2437 N NE  . ARG   A 1 300 ? 23.22306 21.35311  -48.43144 1.000 171.16983 ? 297 ARG   A NE  1 
ATOM   2438 C CZ  . ARG   A 1 300 ? 22.25060 21.45730  -47.53541 1.000 178.17748 ? 297 ARG   A CZ  1 
ATOM   2439 N NH1 . ARG   A 1 300 ? 21.19178 20.66468  -47.56847 1.000 180.97378 ? 297 ARG   A NH1 1 
ATOM   2440 N NH2 . ARG   A 1 300 ? 22.34258 22.38064  -46.58248 1.000 177.63655 ? 297 ARG   A NH2 1 
ATOM   2441 N N   . LEU   A 1 301 ? 25.18590 15.01207  -47.89144 1.000 112.49122 ? 298 LEU   A N   1 
ATOM   2442 C CA  . LEU   A 1 301 ? 25.33443 13.75159  -48.60860 1.000 118.37837 ? 298 LEU   A CA  1 
ATOM   2443 C C   . LEU   A 1 301 ? 24.44376 12.67248  -48.00219 1.000 130.80169 ? 298 LEU   A C   1 
ATOM   2444 O O   . LEU   A 1 301 ? 23.92417 12.83199  -46.89753 1.000 136.17066 ? 298 LEU   A O   1 
ATOM   2445 C CB  . LEU   A 1 301 ? 26.79516 13.29650  -48.59834 1.000 119.24255 ? 298 LEU   A CB  1 
ATOM   2446 C CG  . LEU   A 1 301 ? 27.09086 11.94747  -49.25690 1.000 113.02119 ? 298 LEU   A CG  1 
ATOM   2447 C CD1 . LEU   A 1 301 ? 26.68247 11.96168  -50.72201 1.000 124.36090 ? 298 LEU   A CD1 1 
ATOM   2448 C CD2 . LEU   A 1 301 ? 28.56166 11.58923  -49.10983 1.000 108.38535 ? 298 LEU   A CD2 1 
ATOM   2449 N N   . GLY   B 2 9   ? 29.45502 1.79806   -42.15778 1.000 88.45520  ? 102 GLY   B N   1 
ATOM   2450 C CA  . GLY   B 2 9   ? 28.23960 2.59027   -42.19405 1.000 101.02138 ? 102 GLY   B CA  1 
ATOM   2451 C C   . GLY   B 2 9   ? 27.59321 2.75668   -40.83287 1.000 103.01739 ? 102 GLY   B C   1 
ATOM   2452 O O   . GLY   B 2 9   ? 27.87339 1.99655   -39.90612 1.000 104.06859 ? 102 GLY   B O   1 
ATOM   2453 N N   . SER   B 2 10  ? 26.72172 3.75726   -40.71207 1.000 105.74767 ? 103 SER   B N   1 
ATOM   2454 C CA  . SER   B 2 10  ? 26.03358 4.03993   -39.46051 1.000 91.16367  ? 103 SER   B CA  1 
ATOM   2455 C C   . SER   B 2 10  ? 24.56747 3.65781   -39.58371 1.000 102.42714 ? 103 SER   B C   1 
ATOM   2456 O O   . SER   B 2 10  ? 23.86103 4.20555   -40.44364 1.000 98.35528  ? 103 SER   B O   1 
ATOM   2457 C CB  . SER   B 2 10  ? 26.16924 5.51555   -39.08949 1.000 107.92430 ? 103 SER   B CB  1 
ATOM   2458 O OG  . SER   B 2 10  ? 25.47809 5.80311   -37.88601 1.000 91.88424  ? 103 SER   B OG  1 
ATOM   2459 N N   . PRO   B 2 11  ? 24.06867 2.73150   -38.76060 1.000 89.73030  ? 104 PRO   B N   1 
ATOM   2460 C CA  . PRO   B 2 11  ? 22.65492 2.34787   -38.83189 1.000 87.00551  ? 104 PRO   B CA  1 
ATOM   2461 C C   . PRO   B 2 11  ? 21.71576 3.23359   -38.03016 1.000 80.48699  ? 104 PRO   B C   1 
ATOM   2462 O O   . PRO   B 2 11  ? 20.49345 3.06763   -38.14696 1.000 78.87461  ? 104 PRO   B O   1 
ATOM   2463 C CB  . PRO   B 2 11  ? 22.67256 0.92658   -38.25549 1.000 80.33334  ? 104 PRO   B CB  1 
ATOM   2464 C CG  . PRO   B 2 11  ? 23.76380 0.97627   -37.23966 1.000 82.84112  ? 104 PRO   B CG  1 
ATOM   2465 C CD  . PRO   B 2 11  ? 24.81665 1.90704   -37.79525 1.000 84.88296  ? 104 PRO   B CD  1 
ATOM   2466 N N   . LEU   B 2 12  ? 22.24104 4.15315   -37.22763 1.000 83.54022  ? 105 LEU   B N   1 
ATOM   2467 C CA  . LEU   B 2 12  ? 21.38729 4.98822   -36.39802 1.000 77.46011  ? 105 LEU   B CA  1 
ATOM   2468 C C   . LEU   B 2 12  ? 20.63189 5.99573   -37.26236 1.000 78.08732  ? 105 LEU   B C   1 
ATOM   2469 O O   . LEU   B 2 12  ? 21.19021 6.53317   -38.22416 1.000 86.78034  ? 105 LEU   B O   1 
ATOM   2470 C CB  . LEU   B 2 12  ? 22.21703 5.72415   -35.34669 1.000 75.44311  ? 105 LEU   B CB  1 
ATOM   2471 C CG  . LEU   B 2 12  ? 23.02378 4.85729   -34.37863 1.000 76.63152  ? 105 LEU   B CG  1 
ATOM   2472 C CD1 . LEU   B 2 12  ? 23.87135 5.72626   -33.46254 1.000 67.80960  ? 105 LEU   B CD1 1 
ATOM   2473 C CD2 . LEU   B 2 12  ? 22.10275 3.95829   -33.56903 1.000 82.47648  ? 105 LEU   B CD2 1 
ATOM   2474 N N   . PRO   B 2 13  ? 19.37212 6.27112   -36.95058 1.000 75.44010  ? 106 PRO   B N   1 
ATOM   2475 C CA  . PRO   B 2 13  ? 18.61535 7.28501   -37.68842 1.000 76.56356  ? 106 PRO   B CA  1 
ATOM   2476 C C   . PRO   B 2 13  ? 19.05288 8.68321   -37.26489 1.000 81.75592  ? 106 PRO   B C   1 
ATOM   2477 O O   . PRO   B 2 13  ? 19.96490 8.85934   -36.45926 1.000 87.73573  ? 106 PRO   B O   1 
ATOM   2478 C CB  . PRO   B 2 13  ? 17.16937 6.99924   -37.28161 1.000 89.97101  ? 106 PRO   B CB  1 
ATOM   2479 C CG  . PRO   B 2 13  ? 17.29080 6.45658   -35.89986 1.000 71.45480  ? 106 PRO   B CG  1 
ATOM   2480 C CD  . PRO   B 2 13  ? 18.56430 5.64572   -35.88828 1.000 83.68496  ? 106 PRO   B CD  1 
ATOM   2481 N N   . VAL   B 2 14  ? 18.37669 9.68632   -37.82557 1.000 83.20015  ? 107 VAL   B N   1 
ATOM   2482 C CA  . VAL   B 2 14  ? 18.66777 11.06911  -37.46462 1.000 90.66684  ? 107 VAL   B CA  1 
ATOM   2483 C C   . VAL   B 2 14  ? 18.34737 11.27265  -35.99048 1.000 83.23484  ? 107 VAL   B C   1 
ATOM   2484 O O   . VAL   B 2 14  ? 17.22591 11.01178  -35.53711 1.000 79.81776  ? 107 VAL   B O   1 
ATOM   2485 C CB  . VAL   B 2 14  ? 17.88974 12.03969  -38.36028 1.000 88.47211  ? 107 VAL   B CB  1 
ATOM   2486 C CG1 . VAL   B 2 14  ? 18.54536 12.13106  -39.73092 1.000 73.33881  ? 107 VAL   B CG1 1 
ATOM   2487 C CG2 . VAL   B 2 14  ? 16.43820 11.59896  -38.49747 1.000 95.30816  ? 107 VAL   B CG2 1 
ATOM   2488 N N   . LEU   B 2 15  ? 19.33970 11.72215  -35.22978 1.000 79.84245  ? 108 LEU   B N   1 
ATOM   2489 C CA  . LEU   B 2 15  ? 19.19537 11.93038  -33.79626 1.000 82.71102  ? 108 LEU   B CA  1 
ATOM   2490 C C   . LEU   B 2 15  ? 18.89991 13.39864  -33.52410 1.000 82.40909  ? 108 LEU   B C   1 
ATOM   2491 O O   . LEU   B 2 15  ? 19.55925 14.28370  -34.07931 1.000 89.63189  ? 108 LEU   B O   1 
ATOM   2492 C CB  . LEU   B 2 15  ? 20.45817 11.49362  -33.05194 1.000 76.94228  ? 108 LEU   B CB  1 
ATOM   2493 C CG  . LEU   B 2 15  ? 20.93012 10.06168  -33.31360 1.000 79.71989  ? 108 LEU   B CG  1 
ATOM   2494 C CD1 . LEU   B 2 15  ? 22.15459 9.73383   -32.47409 1.000 71.03775  ? 108 LEU   B CD1 1 
ATOM   2495 C CD2 . LEU   B 2 15  ? 19.81101 9.06912   -33.04517 1.000 74.69556  ? 108 LEU   B CD2 1 
ATOM   2496 N N   . SER   B 2 16  ? 17.90432 13.65246  -32.67412 1.000 77.03555  ? 109 SER   B N   1 
ATOM   2497 C CA  . SER   B 2 16  ? 17.54651 15.02574  -32.34239 1.000 86.40723  ? 109 SER   B CA  1 
ATOM   2498 C C   . SER   B 2 16  ? 18.50905 15.64129  -31.33601 1.000 86.57352  ? 109 SER   B C   1 
ATOM   2499 O O   . SER   B 2 16  ? 18.66935 16.86652  -31.31030 1.000 83.08426  ? 109 SER   B O   1 
ATOM   2500 C CB  . SER   B 2 16  ? 16.11796 15.08045  -31.79895 1.000 90.53828  ? 109 SER   B CB  1 
ATOM   2501 O OG  . SER   B 2 16  ? 15.98748 14.28908  -30.63060 1.000 96.72835  ? 109 SER   B OG  1 
ATOM   2502 N N   . TRP   B 2 17  ? 19.15936 14.81894  -30.51375 1.000 81.67211  ? 110 TRP   B N   1 
ATOM   2503 C CA  . TRP   B 2 17  ? 20.02978 15.31323  -29.45576 1.000 82.89273  ? 110 TRP   B CA  1 
ATOM   2504 C C   . TRP   B 2 17  ? 21.48373 15.46795  -29.88488 1.000 72.54918  ? 110 TRP   B C   1 
ATOM   2505 O O   . TRP   B 2 17  ? 22.25126 16.12545  -29.17408 1.000 84.38377  ? 110 TRP   B O   1 
ATOM   2506 C CB  . TRP   B 2 17  ? 19.94748 14.39427  -28.22822 1.000 74.86762  ? 110 TRP   B CB  1 
ATOM   2507 C CG  . TRP   B 2 17  ? 19.82492 12.93019  -28.54824 1.000 75.54377  ? 110 TRP   B CG  1 
ATOM   2508 C CD1 . TRP   B 2 17  ? 18.69700 12.26809  -28.94309 1.000 86.62127  ? 110 TRP   B CD1 1 
ATOM   2509 C CD2 . TRP   B 2 17  ? 20.86235 11.94383  -28.47574 1.000 74.18254  ? 110 TRP   B CD2 1 
ATOM   2510 N NE1 . TRP   B 2 17  ? 18.97121 10.93567  -29.13318 1.000 67.55055  ? 110 TRP   B NE1 1 
ATOM   2511 C CE2 . TRP   B 2 17  ? 20.29286 10.71004  -28.85179 1.000 71.19356  ? 110 TRP   B CE2 1 
ATOM   2512 C CE3 . TRP   B 2 17  ? 22.21795 11.98470  -28.13453 1.000 65.36484  ? 110 TRP   B CE3 1 
ATOM   2513 C CZ2 . TRP   B 2 17  ? 21.03161 9.52897   -28.89637 1.000 61.47505  ? 110 TRP   B CZ2 1 
ATOM   2514 C CZ3 . TRP   B 2 17  ? 22.94965 10.81034  -28.17956 1.000 67.72929  ? 110 TRP   B CZ3 1 
ATOM   2515 C CH2 . TRP   B 2 17  ? 22.35486 9.59967   -28.55751 1.000 65.65066  ? 110 TRP   B CH2 1 
ATOM   2516 N N   . ALA   B 2 18  ? 21.87896 14.89533  -31.01894 1.000 73.67993  ? 111 ALA   B N   1 
ATOM   2517 C CA  . ALA   B 2 18  ? 23.24115 15.03854  -31.51602 1.000 80.71255  ? 111 ALA   B CA  1 
ATOM   2518 C C   . ALA   B 2 18  ? 23.27857 14.58800  -32.96818 1.000 92.47841  ? 111 ALA   B C   1 
ATOM   2519 O O   . ALA   B 2 18  ? 22.29286 14.08183  -33.50836 1.000 94.50520  ? 111 ALA   B O   1 
ATOM   2520 C CB  . ALA   B 2 18  ? 24.23812 14.23794  -30.67176 1.000 81.48890  ? 111 ALA   B CB  1 
ATOM   2521 N N   . ASN   B 2 19  ? 24.43471 14.78347  -33.59675 1.000 86.28365  ? 112 ASN   B N   1 
ATOM   2522 C CA  . ASN   B 2 19  ? 24.63382 14.29641  -34.95407 1.000 103.72571 ? 112 ASN   B CA  1 
ATOM   2523 C C   . ASN   B 2 19  ? 24.69222 12.77427  -34.94746 1.000 100.05749 ? 112 ASN   B C   1 
ATOM   2524 O O   . ASN   B 2 19  ? 25.43641 12.17506  -34.16473 1.000 96.48900  ? 112 ASN   B O   1 
ATOM   2525 C CB  . ASN   B 2 19  ? 25.91466 14.88030  -35.54890 1.000 102.41899 ? 112 ASN   B CB  1 
ATOM   2526 C CG  . ASN   B 2 19  ? 26.15096 14.43364  -36.98021 1.000 122.73238 ? 112 ASN   B CG  1 
ATOM   2527 O OD1 . ASN   B 2 19  ? 25.21457 14.07244  -37.69332 1.000 121.94477 ? 112 ASN   B OD1 1 
ATOM   2528 N ND2 . ASN   B 2 19  ? 27.40876 14.45606  -37.40727 1.000 112.96621 ? 112 ASN   B ND2 1 
ATOM   2529 N N   . ARG   B 2 20  ? 23.89353 12.15009  -35.81717 1.000 97.25134  ? 113 ARG   B N   1 
ATOM   2530 C CA  . ARG   B 2 20  ? 23.82818 10.69213  -35.85321 1.000 84.60966  ? 113 ARG   B CA  1 
ATOM   2531 C C   . ARG   B 2 20  ? 25.19013 10.08061  -36.15730 1.000 98.52092  ? 113 ARG   B C   1 
ATOM   2532 O O   . ARG   B 2 20  ? 25.59106 9.09502   -35.52697 1.000 77.99233  ? 113 ARG   B O   1 
ATOM   2533 C CB  . ARG   B 2 20  ? 22.79273 10.24188  -36.88310 1.000 97.85957  ? 113 ARG   B CB  1 
ATOM   2534 C CG  . ARG   B 2 20  ? 22.86243 10.98982  -38.20487 1.000 103.48899 ? 113 ARG   B CG  1 
ATOM   2535 C CD  . ARG   B 2 20  ? 21.92266 10.38412  -39.23285 1.000 103.74653 ? 113 ARG   B CD  1 
ATOM   2536 N NE  . ARG   B 2 20  ? 22.26415 8.99744   -39.52597 1.000 108.25556 ? 113 ARG   B NE  1 
ATOM   2537 C CZ  . ARG   B 2 20  ? 23.15289 8.62156   -40.43547 1.000 117.92341 ? 113 ARG   B CZ  1 
ATOM   2538 N NH1 . ARG   B 2 20  ? 23.81214 9.50680   -41.16495 1.000 121.46247 ? 113 ARG   B NH1 1 
ATOM   2539 N NH2 . ARG   B 2 20  ? 23.38721 7.32497   -40.61671 1.000 111.54118 ? 113 ARG   B NH2 1 
ATOM   2540 N N   . GLU   B 2 21  ? 25.91863 10.65273  -37.11797 1.000 115.50545 ? 114 GLU   B N   1 
ATOM   2541 C CA  . GLU   B 2 21  ? 27.25077 10.15381  -37.43332 1.000 116.90355 ? 114 GLU   B CA  1 
ATOM   2542 C C   . GLU   B 2 21  ? 28.25579 10.45215  -36.33001 1.000 119.52036 ? 114 GLU   B C   1 
ATOM   2543 O O   . GLU   B 2 21  ? 29.26506 9.74849   -36.22383 1.000 115.67258 ? 114 GLU   B O   1 
ATOM   2544 C CB  . GLU   B 2 21  ? 27.73807 10.74742  -38.75655 1.000 123.61950 ? 114 GLU   B CB  1 
ATOM   2545 C CG  . GLU   B 2 21  ? 27.04738 10.18005  -39.98801 1.000 135.61284 ? 114 GLU   B CG  1 
ATOM   2546 C CD  . GLU   B 2 21  ? 27.44982 8.74496   -40.27809 1.000 140.05119 ? 114 GLU   B CD  1 
ATOM   2547 O OE1 . GLU   B 2 21  ? 28.47614 8.28763   -39.73141 1.000 135.60802 ? 114 GLU   B OE1 1 
ATOM   2548 O OE2 . GLU   B 2 21  ? 26.73951 8.07361   -41.05564 1.000 149.01805 ? 114 GLU   B OE2 1 
ATOM   2549 N N   . GLU   B 2 22  ? 28.00401 11.47299  -35.50844 1.000 101.73699 ? 115 GLU   B N   1 
ATOM   2550 C CA  . GLU   B 2 22  ? 28.92724 11.79699  -34.42605 1.000 93.42120  ? 115 GLU   B CA  1 
ATOM   2551 C C   . GLU   B 2 22  ? 28.79597 10.80306  -33.27849 1.000 73.69724  ? 115 GLU   B C   1 
ATOM   2552 O O   . GLU   B 2 22  ? 29.80136 10.31151  -32.75248 1.000 74.38205  ? 115 GLU   B O   1 
ATOM   2553 C CB  . GLU   B 2 22  ? 28.68027 13.22383  -33.93643 1.000 93.38365  ? 115 GLU   B CB  1 
ATOM   2554 C CG  . GLU   B 2 22  ? 29.68371 13.70882  -32.90446 1.000 97.06884  ? 115 GLU   B CG  1 
ATOM   2555 C CD  . GLU   B 2 22  ? 29.35483 15.09171  -32.37950 1.000 100.06454 ? 115 GLU   B CD  1 
ATOM   2556 O OE1 . GLU   B 2 22  ? 28.18962 15.52101  -32.51900 1.000 99.06084  ? 115 GLU   B OE1 1 
ATOM   2557 O OE2 . GLU   B 2 22  ? 30.26206 15.75054  -31.82955 1.000 96.48662  ? 115 GLU   B OE2 1 
ATOM   2558 N N   . VAL   B 2 23  ? 27.55952 10.49568  -32.87676 1.000 71.02764  ? 116 VAL   B N   1 
ATOM   2559 C CA  . VAL   B 2 23  ? 27.34050 9.53779   -31.79522 1.000 66.99117  ? 116 VAL   B CA  1 
ATOM   2560 C C   . VAL   B 2 23  ? 27.89003 8.16979   -32.17460 1.000 78.31458  ? 116 VAL   B C   1 
ATOM   2561 O O   . VAL   B 2 23  ? 28.54254 7.49855   -31.36529 1.000 53.97401  ? 116 VAL   B O   1 
ATOM   2562 C CB  . VAL   B 2 23  ? 25.84372 9.46578   -31.44173 1.000 61.12956  ? 116 VAL   B CB  1 
ATOM   2563 C CG1 . VAL   B 2 23  ? 25.59070 8.38095   -30.40475 1.000 64.33385  ? 116 VAL   B CG1 1 
ATOM   2564 C CG2 . VAL   B 2 23  ? 25.35564 10.81086  -30.94051 1.000 61.97888  ? 116 VAL   B CG2 1 
ATOM   2565 N N   . TRP   B 2 24  ? 27.64125 7.73866   -33.41291 1.000 63.13486  ? 117 TRP   B N   1 
ATOM   2566 C CA  . TRP   B 2 24  ? 28.12155 6.43473   -33.85627 1.000 65.76907  ? 117 TRP   B CA  1 
ATOM   2567 C C   . TRP   B 2 24  ? 29.64193 6.41048   -33.95670 1.000 74.12679  ? 117 TRP   B C   1 
ATOM   2568 O O   . TRP   B 2 24  ? 30.27457 5.40239   -33.62072 1.000 57.73284  ? 117 TRP   B O   1 
ATOM   2569 C CB  . TRP   B 2 24  ? 27.48121 6.07670   -35.19802 1.000 66.76699  ? 117 TRP   B CB  1 
ATOM   2570 C CG  . TRP   B 2 24  ? 27.79897 4.69547   -35.67868 1.000 70.45761  ? 117 TRP   B CG  1 
ATOM   2571 C CD1 . TRP   B 2 24  ? 28.67985 4.35215   -36.66223 1.000 82.91585  ? 117 TRP   B CD1 1 
ATOM   2572 C CD2 . TRP   B 2 24  ? 27.23519 3.46851   -35.19888 1.000 68.13211  ? 117 TRP   B CD2 1 
ATOM   2573 N NE1 . TRP   B 2 24  ? 28.69895 2.98800   -36.82538 1.000 75.80873  ? 117 TRP   B NE1 1 
ATOM   2574 C CE2 . TRP   B 2 24  ? 27.82244 2.42212   -35.93777 1.000 72.50654  ? 117 TRP   B CE2 1 
ATOM   2575 C CE3 . TRP   B 2 24  ? 26.29222 3.15339   -34.21606 1.000 70.90779  ? 117 TRP   B CE3 1 
ATOM   2576 C CZ2 . TRP   B 2 24  ? 27.49873 1.08384   -35.72420 1.000 78.22889  ? 117 TRP   B CZ2 1 
ATOM   2577 C CZ3 . TRP   B 2 24  ? 25.97102 1.82409   -34.00634 1.000 78.96131  ? 117 TRP   B CZ3 1 
ATOM   2578 C CH2 . TRP   B 2 24  ? 26.57180 0.80634   -34.75742 1.000 65.83932  ? 117 TRP   B CH2 1 
ATOM   2579 N N   . LYS   B 2 25  ? 30.24518 7.51239   -34.41293 1.000 82.08011  ? 118 LYS   B N   1 
ATOM   2580 C CA  . LYS   B 2 25  ? 31.70061 7.57654   -34.50897 1.000 65.04932  ? 118 LYS   B CA  1 
ATOM   2581 C C   . LYS   B 2 25  ? 32.34789 7.45004   -33.13653 1.000 67.00305  ? 118 LYS   B C   1 
ATOM   2582 O O   . LYS   B 2 25  ? 33.35245 6.74672   -32.97765 1.000 69.54135  ? 118 LYS   B O   1 
ATOM   2583 C CB  . LYS   B 2 25  ? 32.12630 8.88332   -35.17853 1.000 84.06560  ? 118 LYS   B CB  1 
ATOM   2584 C CG  . LYS   B 2 25  ? 33.13937 8.71770   -36.29997 1.000 99.55508  ? 118 LYS   B CG  1 
ATOM   2585 C CD  . LYS   B 2 25  ? 32.50307 8.08766   -37.52831 1.000 108.90011 ? 118 LYS   B CD  1 
ATOM   2586 C CE  . LYS   B 2 25  ? 33.47521 8.04836   -38.69633 1.000 106.65871 ? 118 LYS   B CE  1 
ATOM   2587 N NZ  . LYS   B 2 25  ? 32.83254 7.52465   -39.93324 1.000 113.45927 ? 118 LYS   B NZ  1 
ATOM   2588 N N   . ILE   B 2 26  ? 31.78556 8.12749   -32.13258 1.000 60.61314  ? 119 ILE   B N   1 
ATOM   2589 C CA  . ILE   B 2 26  ? 32.31726 8.03472   -30.77547 1.000 67.42255  ? 119 ILE   B CA  1 
ATOM   2590 C C   . ILE   B 2 26  ? 32.22823 6.60269   -30.26538 1.000 58.18055  ? 119 ILE   B C   1 
ATOM   2591 O O   . ILE   B 2 26  ? 33.17061 6.08669   -29.65132 1.000 62.90860  ? 119 ILE   B O   1 
ATOM   2592 C CB  . ILE   B 2 26  ? 31.57770 9.01614   -29.84711 1.000 69.79199  ? 119 ILE   B CB  1 
ATOM   2593 C CG1 . ILE   B 2 26  ? 31.83175 10.45850  -30.28951 1.000 71.62431  ? 119 ILE   B CG1 1 
ATOM   2594 C CG2 . ILE   B 2 26  ? 32.00162 8.81210   -28.39982 1.000 63.47028  ? 119 ILE   B CG2 1 
ATOM   2595 C CD1 . ILE   B 2 26  ? 30.92712 11.46864  -29.62352 1.000 69.84907  ? 119 ILE   B CD1 1 
ATOM   2596 N N   . MET   B 2 27  ? 31.09855 5.93534   -30.51733 1.000 57.10289  ? 120 MET   B N   1 
ATOM   2597 C CA  . MET   B 2 27  ? 30.95292 4.54518   -30.09709 1.000 57.87465  ? 120 MET   B CA  1 
ATOM   2598 C C   . MET   B 2 27  ? 31.97073 3.65036   -30.79396 1.000 62.91629  ? 120 MET   B C   1 
ATOM   2599 O O   . MET   B 2 27  ? 32.53170 2.73703   -30.17668 1.000 56.12934  ? 120 MET   B O   1 
ATOM   2600 C CB  . MET   B 2 27  ? 29.52822 4.06054   -30.37062 1.000 59.84896  ? 120 MET   B CB  1 
ATOM   2601 C CG  . MET   B 2 27  ? 28.45696 4.80817   -29.58794 1.000 61.58368  ? 120 MET   B CG  1 
ATOM   2602 S SD  . MET   B 2 27  ? 26.77721 4.31942   -30.03432 1.000 66.08758  ? 120 MET   B SD  1 
ATOM   2603 C CE  . MET   B 2 27  ? 26.76633 2.61414   -29.48844 1.000 77.52419  ? 120 MET   B CE  1 
ATOM   2604 N N   . LEU   B 2 28  ? 32.22848 3.90171   -32.08012 1.000 55.95648  ? 121 LEU   B N   1 
ATOM   2605 C CA  . LEU   B 2 28  ? 33.23878 3.12642   -32.79285 1.000 70.25088  ? 121 LEU   B CA  1 
ATOM   2606 C C   . LEU   B 2 28  ? 34.64325 3.48887   -32.32755 1.000 70.14936  ? 121 LEU   B C   1 
ATOM   2607 O O   . LEU   B 2 28  ? 35.48590 2.60447   -32.13484 1.000 72.04635  ? 121 LEU   B O   1 
ATOM   2608 C CB  . LEU   B 2 28  ? 33.10556 3.34034   -34.30041 1.000 57.65479  ? 121 LEU   B CB  1 
ATOM   2609 C CG  . LEU   B 2 28  ? 31.82967 2.83424   -34.97424 1.000 67.23258  ? 121 LEU   B CG  1 
ATOM   2610 C CD1 . LEU   B 2 28  ? 31.95130 2.95418   -36.48576 1.000 81.26112  ? 121 LEU   B CD1 1 
ATOM   2611 C CD2 . LEU   B 2 28  ? 31.53473 1.39982   -34.56577 1.000 66.95777  ? 121 LEU   B CD2 1 
ATOM   2612 N N   . ASN   B 2 29  ? 34.91485 4.78404   -32.14242 1.000 66.10855  ? 122 ASN   B N   1 
ATOM   2613 C CA  . ASN   B 2 29  ? 36.23550 5.21177   -31.69539 1.000 80.72412  ? 122 ASN   B CA  1 
ATOM   2614 C C   . ASN   B 2 29  ? 36.54970 4.74004   -30.28322 1.000 75.74786  ? 122 ASN   B C   1 
ATOM   2615 O O   . ASN   B 2 29  ? 37.72853 4.62347   -29.93207 1.000 80.38551  ? 122 ASN   B O   1 
ATOM   2616 C CB  . ASN   B 2 29  ? 36.35596 6.73535   -31.77338 1.000 88.52928  ? 122 ASN   B CB  1 
ATOM   2617 C CG  . ASN   B 2 29  ? 36.38821 7.24562   -33.20177 1.000 98.52437  ? 122 ASN   B CG  1 
ATOM   2618 O OD1 . ASN   B 2 29  ? 36.83580 6.54809   -34.11212 1.000 93.40315  ? 122 ASN   B OD1 1 
ATOM   2619 N ND2 . ASN   B 2 29  ? 35.91395 8.46966   -33.40448 1.000 104.21940 ? 122 ASN   B ND2 1 
ATOM   2620 N N   . LYS   B 2 30  ? 35.52767 4.46849   -29.46811 1.000 83.98392  ? 123 LYS   B N   1 
ATOM   2621 C CA  . LYS   B 2 30  ? 35.77485 3.95333   -28.12582 1.000 88.33041  ? 123 LYS   B CA  1 
ATOM   2622 C C   . LYS   B 2 30  ? 36.37924 2.55574   -28.17593 1.000 85.51448  ? 123 LYS   B C   1 
ATOM   2623 O O   . LYS   B 2 30  ? 37.24029 2.21540   -27.35607 1.000 91.63932  ? 123 LYS   B O   1 
ATOM   2624 C CB  . LYS   B 2 30  ? 34.47831 3.95116   -27.31559 1.000 94.32956  ? 123 LYS   B CB  1 
ATOM   2625 C CG  . LYS   B 2 30  ? 34.61512 3.33644   -25.93036 1.000 95.38324  ? 123 LYS   B CG  1 
ATOM   2626 C CD  . LYS   B 2 30  ? 33.28136 3.29222   -25.20396 1.000 84.47419  ? 123 LYS   B CD  1 
ATOM   2627 C CE  . LYS   B 2 30  ? 32.78600 4.68707   -24.86640 1.000 79.46397  ? 123 LYS   B CE  1 
ATOM   2628 N NZ  . LYS   B 2 30  ? 33.68814 5.36916   -23.89939 1.000 97.56873  ? 123 LYS   B NZ  1 
ATOM   2629 N N   . GLU   B 2 31  ? 35.94906 1.73479   -29.13700 1.000 99.82560  ? 124 GLU   B N   1 
ATOM   2630 C CA  . GLU   B 2 31  ? 36.49089 0.38691   -29.25902 1.000 105.78858 ? 124 GLU   B CA  1 
ATOM   2631 C C   . GLU   B 2 31  ? 37.95711 0.38569   -29.67058 1.000 109.10629 ? 124 GLU   B C   1 
ATOM   2632 O O   . GLU   B 2 31  ? 38.63748 -0.62858  -29.48446 1.000 118.39406 ? 124 GLU   B O   1 
ATOM   2633 C CB  . GLU   B 2 31  ? 35.66238 -0.42734  -30.25363 1.000 115.44455 ? 124 GLU   B CB  1 
ATOM   2634 C CG  . GLU   B 2 31  ? 34.24538 -0.70893  -29.77915 1.000 107.65373 ? 124 GLU   B CG  1 
ATOM   2635 C CD  . GLU   B 2 31  ? 33.52852 -1.72952  -30.64104 1.000 117.69083 ? 124 GLU   B CD  1 
ATOM   2636 O OE1 . GLU   B 2 31  ? 33.90674 -1.89028  -31.82064 1.000 114.88115 ? 124 GLU   B OE1 1 
ATOM   2637 O OE2 . GLU   B 2 31  ? 32.58881 -2.37725  -30.13416 1.000 110.96569 ? 124 GLU   B OE2 1 
ATOM   2638 N N   . LYS   B 2 32  ? 38.45808 1.49071   -30.22792 1.000 110.79228 ? 125 LYS   B N   1 
ATOM   2639 C CA  . LYS   B 2 32  ? 39.89081 1.61114   -30.46618 1.000 97.31193  ? 125 LYS   B CA  1 
ATOM   2640 C C   . LYS   B 2 32  ? 40.66273 1.85271   -29.17681 1.000 98.79357  ? 125 LYS   B C   1 
ATOM   2641 O O   . LYS   B 2 32  ? 41.85800 1.54628   -29.11597 1.000 111.07906 ? 125 LYS   B O   1 
ATOM   2642 C CB  . LYS   B 2 32  ? 40.17322 2.73869   -31.46047 1.000 106.31487 ? 125 LYS   B CB  1 
ATOM   2643 C CG  . LYS   B 2 32  ? 39.69093 2.46129   -32.87464 1.000 106.00722 ? 125 LYS   B CG  1 
ATOM   2644 C CD  . LYS   B 2 32  ? 40.10102 3.57818   -33.82134 1.000 120.00286 ? 125 LYS   B CD  1 
ATOM   2645 C CE  . LYS   B 2 32  ? 39.73334 3.25067   -35.25951 1.000 132.80355 ? 125 LYS   B CE  1 
ATOM   2646 N NZ  . LYS   B 2 32  ? 38.26774 3.05425   -35.43003 1.000 130.22414 ? 125 LYS   B NZ  1 
ATOM   2647 N N   . THR   B 2 33  ? 40.00674 2.39266   -28.14829 1.000 94.25260  ? 126 THR   B N   1 
ATOM   2648 C CA  . THR   B 2 33  ? 40.66584 2.60189   -26.86459 1.000 88.59496  ? 126 THR   B CA  1 
ATOM   2649 C C   . THR   B 2 33  ? 40.71391 1.31586   -26.04759 1.000 89.81415  ? 126 THR   B C   1 
ATOM   2650 O O   . THR   B 2 33  ? 41.71329 1.04102   -25.37402 1.000 96.00584  ? 126 THR   B O   1 
ATOM   2651 C CB  . THR   B 2 33  ? 39.94813 3.70341   -26.08179 1.000 98.20028  ? 126 THR   B CB  1 
ATOM   2652 O OG1 . THR   B 2 33  ? 39.87065 4.88851   -26.88393 1.000 92.96268  ? 126 THR   B OG1 1 
ATOM   2653 C CG2 . THR   B 2 33  ? 40.69057 4.01827   -24.78875 1.000 99.11984  ? 126 THR   B CG2 1 
ATOM   2654 N N   . TYR   B 2 34  ? 39.65040 0.51754   -26.09996 1.000 88.39175  ? 127 TYR   B N   1 
ATOM   2655 C CA  . TYR   B 2 34  ? 39.56480 -0.72828  -25.34505 1.000 77.07859  ? 127 TYR   B CA  1 
ATOM   2656 C C   . TYR   B 2 34  ? 40.08806 -1.86617  -26.21406 1.000 85.19263  ? 127 TYR   B C   1 
ATOM   2657 O O   . TYR   B 2 34  ? 39.47265 -2.21963  -27.22517 1.000 88.13162  ? 127 TYR   B O   1 
ATOM   2658 C CB  . TYR   B 2 34  ? 38.12812 -0.98683  -24.89845 1.000 78.24125  ? 127 TYR   B CB  1 
ATOM   2659 C CG  . TYR   B 2 34  ? 37.63322 -0.01828  -23.84723 1.000 74.18250  ? 127 TYR   B CG  1 
ATOM   2660 C CD1 . TYR   B 2 34  ? 37.18260 1.24805   -24.19710 1.000 64.20040  ? 127 TYR   B CD1 1 
ATOM   2661 C CD2 . TYR   B 2 34  ? 37.61724 -0.37091  -22.50423 1.000 66.76996  ? 127 TYR   B CD2 1 
ATOM   2662 C CE1 . TYR   B 2 34  ? 36.73226 2.13702   -23.23758 1.000 69.97062  ? 127 TYR   B CE1 1 
ATOM   2663 C CE2 . TYR   B 2 34  ? 37.16767 0.50991   -21.53867 1.000 59.76539  ? 127 TYR   B CE2 1 
ATOM   2664 C CZ  . TYR   B 2 34  ? 36.72664 1.76193   -21.91039 1.000 64.33550  ? 127 TYR   B CZ  1 
ATOM   2665 O OH  . TYR   B 2 34  ? 36.27867 2.64095   -20.94989 1.000 54.83521  ? 127 TYR   B OH  1 
ATOM   2666 N N   . LEU   B 2 35  ? 41.22014 -2.43919  -25.81907 1.000 82.13566  ? 128 LEU   B N   1 
ATOM   2667 C CA  . LEU   B 2 35  ? 41.86581 -3.50650  -26.56740 1.000 87.75113  ? 128 LEU   B CA  1 
ATOM   2668 C C   . LEU   B 2 35  ? 41.59489 -4.85757  -25.91748 1.000 86.89484  ? 128 LEU   B C   1 
ATOM   2669 O O   . LEU   B 2 35  ? 41.50408 -4.97319  -24.69264 1.000 97.05856  ? 128 LEU   B O   1 
ATOM   2670 C CB  . LEU   B 2 35  ? 43.37721 -3.27605  -26.66211 1.000 91.72816  ? 128 LEU   B CB  1 
ATOM   2671 C CG  . LEU   B 2 35  ? 43.91078 -2.30277  -27.71831 1.000 94.18201  ? 128 LEU   B CG  1 
ATOM   2672 C CD1 . LEU   B 2 35  ? 43.51072 -0.86456  -27.42078 1.000 99.91818  ? 128 LEU   B CD1 1 
ATOM   2673 C CD2 . LEU   B 2 35  ? 45.42343 -2.42595  -27.83271 1.000 102.90077 ? 128 LEU   B CD2 1 
ATOM   2674 N N   . ARG   B 2 36  ? 41.46625 -5.88293  -26.75689 1.000 85.16103  ? 129 ARG   B N   1 
ATOM   2675 C CA  . ARG   B 2 36  ? 41.28734 -7.25447  -26.30413 1.000 94.97558  ? 129 ARG   B CA  1 
ATOM   2676 C C   . ARG   B 2 36  ? 42.26826 -8.15898  -27.03394 1.000 98.08235  ? 129 ARG   B C   1 
ATOM   2677 O O   . ARG   B 2 36  ? 42.53368 -7.97123  -28.22507 1.000 91.08102  ? 129 ARG   B O   1 
ATOM   2678 C CB  . ARG   B 2 36  ? 39.85096 -7.74932  -26.53222 1.000 101.44426 ? 129 ARG   B CB  1 
ATOM   2679 C CG  . ARG   B 2 36  ? 38.82451 -7.16440  -25.57223 1.000 104.10022 ? 129 ARG   B CG  1 
ATOM   2680 C CD  . ARG   B 2 36  ? 38.26895 -5.84269  -26.07642 1.000 98.44246  ? 129 ARG   B CD  1 
ATOM   2681 N NE  . ARG   B 2 36  ? 37.39851 -5.20739  -25.09440 1.000 85.26731  ? 129 ARG   B NE  1 
ATOM   2682 C CZ  . ARG   B 2 36  ? 36.66215 -4.13065  -25.33203 1.000 92.91004  ? 129 ARG   B CZ  1 
ATOM   2683 N NH1 . ARG   B 2 36  ? 36.65216 -3.54836  -26.52015 1.000 88.35148  ? 129 ARG   B NH1 1 
ATOM   2684 N NH2 . ARG   B 2 36  ? 35.91510 -3.62664  -24.35379 1.000 83.89576  ? 129 ARG   B NH2 1 
ATOM   2685 N N   . ASP   B 2 37  ? 42.80411 -9.13922  -26.31148 1.000 99.51338  ? 130 ASP   B N   1 
ATOM   2686 C CA  . ASP   B 2 37  ? 43.77157 -10.09089 -26.84803 1.000 106.01657 ? 130 ASP   B CA  1 
ATOM   2687 C C   . ASP   B 2 37  ? 43.19466 -11.48938 -26.67500 1.000 97.43797  ? 130 ASP   B C   1 
ATOM   2688 O O   . ASP   B 2 37  ? 43.01660 -11.95429 -25.54489 1.000 88.48805  ? 130 ASP   B O   1 
ATOM   2689 C CB  . ASP   B 2 37  ? 45.11900 -9.95374  -26.13827 1.000 97.56594  ? 130 ASP   B CB  1 
ATOM   2690 C CG  . ASP   B 2 37  ? 46.25770 -10.60086 -26.90607 1.000 117.94926 ? 130 ASP   B CG  1 
ATOM   2691 O OD1 . ASP   B 2 37  ? 46.01212 -11.58238 -27.63875 1.000 111.90792 ? 130 ASP   B OD1 1 
ATOM   2692 O OD2 . ASP   B 2 37  ? 47.40478 -10.12473 -26.77364 1.000 118.82816 ? 130 ASP   B OD2 1 
ATOM   2693 N N   . GLN   B 2 38  ? 42.90462 -12.16131 -27.79119 1.000 89.43957  ? 131 GLN   B N   1 
ATOM   2694 C CA  . GLN   B 2 38  ? 42.31489 -13.49337 -27.72391 1.000 96.85807  ? 131 GLN   B CA  1 
ATOM   2695 C C   . GLN   B 2 38  ? 43.27359 -14.54193 -27.17553 1.000 101.29599 ? 131 GLN   B C   1 
ATOM   2696 O O   . GLN   B 2 38  ? 42.83741 -15.66273 -26.89127 1.000 99.20905  ? 131 GLN   B O   1 
ATOM   2697 C CB  . GLN   B 2 38  ? 41.81750 -13.92581 -29.10620 1.000 106.11845 ? 131 GLN   B CB  1 
ATOM   2698 C CG  . GLN   B 2 38  ? 42.88976 -13.97340 -30.18673 1.000 103.00332 ? 131 GLN   B CG  1 
ATOM   2699 C CD  . GLN   B 2 38  ? 43.09344 -12.63572 -30.87405 1.000 113.06695 ? 131 GLN   B CD  1 
ATOM   2700 O OE1 . GLN   B 2 38  ? 42.78407 -11.58240 -30.31615 1.000 109.28094 ? 131 GLN   B OE1 1 
ATOM   2701 N NE2 . GLN   B 2 38  ? 43.60981 -12.67297 -32.09708 1.000 102.62818 ? 131 GLN   B NE2 1 
ATOM   2702 N N   . HIS   B 2 39  ? 44.55240 -14.21190 -27.01545 1.000 103.53709 ? 132 HIS   B N   1 
ATOM   2703 C CA  . HIS   B 2 39  ? 45.55511 -15.13993 -26.50836 1.000 102.08381 ? 132 HIS   B CA  1 
ATOM   2704 C C   . HIS   B 2 39  ? 46.28703 -14.54450 -25.31499 1.000 110.80679 ? 132 HIS   B C   1 
ATOM   2705 O O   . HIS   B 2 39  ? 47.50081 -14.71198 -25.16163 1.000 107.25058 ? 132 HIS   B O   1 
ATOM   2706 C CB  . HIS   B 2 39  ? 46.54410 -15.52812 -27.60512 1.000 114.31016 ? 132 HIS   B CB  1 
ATOM   2707 C CG  . HIS   B 2 39  ? 45.92257 -16.27609 -28.74310 1.000 109.37033 ? 132 HIS   B CG  1 
ATOM   2708 N ND1 . HIS   B 2 39  ? 46.42662 -16.23346 -30.02510 1.000 113.40535 ? 132 HIS   B ND1 1 
ATOM   2709 C CD2 . HIS   B 2 39  ? 44.84138 -17.08988 -28.79105 1.000 115.98216 ? 132 HIS   B CD2 1 
ATOM   2710 C CE1 . HIS   B 2 39  ? 45.68078 -16.98571 -30.81450 1.000 121.86310 ? 132 HIS   B CE1 1 
ATOM   2711 N NE2 . HIS   B 2 39  ? 44.71227 -17.51687 -30.09031 1.000 118.26311 ? 132 HIS   B NE2 1 
ATOM   2712 N N   . PHE   B 2 40  ? 45.56059 -13.83596 -24.44501 1.000 106.27739 ? 133 PHE   B N   1 
ATOM   2713 C CA  . PHE   B 2 40  ? 46.18990 -13.27829 -23.25325 1.000 106.61653 ? 133 PHE   B CA  1 
ATOM   2714 C C   . PHE   B 2 40  ? 46.60974 -14.36007 -22.26805 1.000 98.16782  ? 133 PHE   B C   1 
ATOM   2715 O O   . PHE   B 2 40  ? 47.45171 -14.09963 -21.40206 1.000 106.69814 ? 133 PHE   B O   1 
ATOM   2716 C CB  . PHE   B 2 40  ? 45.25593 -12.27336 -22.56683 1.000 95.03318  ? 133 PHE   B CB  1 
ATOM   2717 C CG  . PHE   B 2 40  ? 44.00554 -12.88539 -21.98672 1.000 91.90400  ? 133 PHE   B CG  1 
ATOM   2718 C CD1 . PHE   B 2 40  ? 44.00698 -13.43458 -20.71444 1.000 90.41445  ? 133 PHE   B CD1 1 
ATOM   2719 C CD2 . PHE   B 2 40  ? 42.82249 -12.88638 -22.70410 1.000 99.20369  ? 133 PHE   B CD2 1 
ATOM   2720 C CE1 . PHE   B 2 40  ? 42.85917 -13.98879 -20.17992 1.000 91.76441  ? 133 PHE   B CE1 1 
ATOM   2721 C CE2 . PHE   B 2 40  ? 41.67125 -13.43747 -22.17414 1.000 99.82140  ? 133 PHE   B CE2 1 
ATOM   2722 C CZ  . PHE   B 2 40  ? 41.68966 -13.98861 -20.91085 1.000 86.20191  ? 133 PHE   B CZ  1 
ATOM   2723 N N   . LEU   B 2 41  ? 46.04152 -15.56233 -22.37834 1.000 100.16528 ? 134 LEU   B N   1 
ATOM   2724 C CA  . LEU   B 2 41  ? 46.42040 -16.66339 -21.50338 1.000 111.44495 ? 134 LEU   B CA  1 
ATOM   2725 C C   . LEU   B 2 41  ? 47.81896 -17.19061 -21.79096 1.000 114.34667 ? 134 LEU   B C   1 
ATOM   2726 O O   . LEU   B 2 41  ? 48.35988 -17.93543 -20.96730 1.000 114.73531 ? 134 LEU   B O   1 
ATOM   2727 C CB  . LEU   B 2 41  ? 45.40007 -17.79554 -21.61921 1.000 104.27710 ? 134 LEU   B CB  1 
ATOM   2728 C CG  . LEU   B 2 41  ? 44.02442 -17.47148 -21.03570 1.000 103.21494 ? 134 LEU   B CG  1 
ATOM   2729 C CD1 . LEU   B 2 41  ? 43.03614 -18.57740 -21.34585 1.000 103.98767 ? 134 LEU   B CD1 1 
ATOM   2730 C CD2 . LEU   B 2 41  ? 44.12703 -17.24805 -19.53487 1.000 102.63388 ? 134 LEU   B CD2 1 
ATOM   2731 N N   . GLU   B 2 42  ? 48.41332 -16.83238 -22.93183 1.000 117.22026 ? 135 GLU   B N   1 
ATOM   2732 C CA  . GLU   B 2 42  ? 49.80967 -17.17214 -23.17367 1.000 113.14820 ? 135 GLU   B CA  1 
ATOM   2733 C C   . GLU   B 2 42  ? 50.74292 -16.43891 -22.22052 1.000 121.53089 ? 135 GLU   B C   1 
ATOM   2734 O O   . GLU   B 2 42  ? 51.86306 -16.90494 -21.98554 1.000 120.54923 ? 135 GLU   B O   1 
ATOM   2735 C CB  . GLU   B 2 42  ? 50.18516 -16.86396 -24.62343 1.000 113.30608 ? 135 GLU   B CB  1 
ATOM   2736 C CG  . GLU   B 2 42  ? 49.44657 -17.71521 -25.64472 1.000 112.24474 ? 135 GLU   B CG  1 
ATOM   2737 C CD  . GLU   B 2 42  ? 49.83013 -17.37859 -27.07150 1.000 115.54215 ? 135 GLU   B CD  1 
ATOM   2738 O OE1 . GLU   B 2 42  ? 50.59499 -16.41172 -27.26935 1.000 113.77542 ? 135 GLU   B OE1 1 
ATOM   2739 O OE2 . GLU   B 2 42  ? 49.36730 -18.08114 -27.99505 1.000 134.01391 ? 135 GLU   B OE2 1 
ATOM   2740 N N   . GLN   B 2 43  ? 50.30498 -15.30492 -21.67034 1.000 116.29861 ? 136 GLN   B N   1 
ATOM   2741 C CA  . GLN   B 2 43  ? 51.03934 -14.61363 -20.61992 1.000 116.12201 ? 136 GLN   B CA  1 
ATOM   2742 C C   . GLN   B 2 43  ? 50.93284 -15.31566 -19.27353 1.000 108.77606 ? 136 GLN   B C   1 
ATOM   2743 O O   . GLN   B 2 43  ? 51.69568 -14.98668 -18.35871 1.000 104.76794 ? 136 GLN   B O   1 
ATOM   2744 C CB  . GLN   B 2 43  ? 50.53416 -13.17409 -20.48629 1.000 114.26309 ? 136 GLN   B CB  1 
ATOM   2745 C CG  . GLN   B 2 43  ? 50.56679 -12.37911 -21.78160 1.000 120.98964 ? 136 GLN   B CG  1 
ATOM   2746 C CD  . GLN   B 2 43  ? 49.98741 -10.98557 -21.62652 1.000 116.14550 ? 136 GLN   B CD  1 
ATOM   2747 O OE1 . GLN   B 2 43  ? 49.92873 -10.21536 -22.58475 1.000 123.16777 ? 136 GLN   B OE1 1 
ATOM   2748 N NE2 . GLN   B 2 43  ? 49.55480 -10.65520 -20.41503 1.000 112.93059 ? 136 GLN   B NE2 1 
ATOM   2749 N N   . HIS   B 2 44  ? 50.00391 -16.26446 -19.13117 1.000 104.60768 ? 137 HIS   B N   1 
ATOM   2750 C CA  . HIS   B 2 44  ? 49.81818 -17.04571 -17.91079 1.000 106.28528 ? 137 HIS   B CA  1 
ATOM   2751 C C   . HIS   B 2 44  ? 49.91739 -18.51785 -18.29395 1.000 108.77450 ? 137 HIS   B C   1 
ATOM   2752 O O   . HIS   B 2 44  ? 48.89351 -19.18587 -18.50512 1.000 115.14773 ? 137 HIS   B O   1 
ATOM   2753 C CB  . HIS   B 2 44  ? 48.47948 -16.73180 -17.24576 1.000 106.26290 ? 137 HIS   B CB  1 
ATOM   2754 C CG  . HIS   B 2 44  ? 48.17655 -15.26831 -17.16071 1.000 105.28296 ? 137 HIS   B CG  1 
ATOM   2755 N ND1 . HIS   B 2 44  ? 48.49131 -14.50502 -16.05708 1.000 90.55276  ? 137 HIS   B ND1 1 
ATOM   2756 C CD2 . HIS   B 2 44  ? 47.58890 -14.42721 -18.04445 1.000 107.44556 ? 137 HIS   B CD2 1 
ATOM   2757 C CE1 . HIS   B 2 44  ? 48.10992 -13.25723 -16.26401 1.000 88.86647  ? 137 HIS   B CE1 1 
ATOM   2758 N NE2 . HIS   B 2 44  ? 47.55927 -13.18321 -17.46235 1.000 106.69492 ? 137 HIS   B NE2 1 
ATOM   2759 N N   . PRO   B 2 45  ? 51.13508 -19.05755 -18.39282 1.000 124.17537 ? 138 PRO   B N   1 
ATOM   2760 C CA  . PRO   B 2 45  ? 51.29379 -20.43069 -18.90301 1.000 119.09498 ? 138 PRO   B CA  1 
ATOM   2761 C C   . PRO   B 2 45  ? 50.62587 -21.49280 -18.04685 1.000 110.23894 ? 138 PRO   B C   1 
ATOM   2762 O O   . PRO   B 2 45  ? 50.34769 -22.58628 -18.55418 1.000 124.15063 ? 138 PRO   B O   1 
ATOM   2763 C CB  . PRO   B 2 45  ? 52.81796 -20.61948 -18.93449 1.000 116.11279 ? 138 PRO   B CB  1 
ATOM   2764 C CG  . PRO   B 2 45  ? 53.38210 -19.23015 -18.93817 1.000 120.80163 ? 138 PRO   B CG  1 
ATOM   2765 C CD  . PRO   B 2 45  ? 52.43050 -18.41330 -18.12164 1.000 116.48839 ? 138 PRO   B CD  1 
ATOM   2766 N N   . LEU   B 2 46  ? 50.35653 -21.21360 -16.77201 1.000 113.29147 ? 139 LEU   B N   1 
ATOM   2767 C CA  . LEU   B 2 46  ? 49.75357 -22.20596 -15.89209 1.000 117.42068 ? 139 LEU   B CA  1 
ATOM   2768 C C   . LEU   B 2 46  ? 48.23774 -22.28282 -16.03172 1.000 119.26194 ? 139 LEU   B C   1 
ATOM   2769 O O   . LEU   B 2 46  ? 47.63194 -23.22870 -15.51585 1.000 118.48413 ? 139 LEU   B O   1 
ATOM   2770 C CB  . LEU   B 2 46  ? 50.12836 -21.90595 -14.43709 1.000 130.96249 ? 139 LEU   B CB  1 
ATOM   2771 C CG  . LEU   B 2 46  ? 50.03124 -23.06012 -13.43636 1.000 127.52971 ? 139 LEU   B CG  1 
ATOM   2772 C CD1 . LEU   B 2 46  ? 50.91148 -24.22159 -13.87155 1.000 128.79748 ? 139 LEU   B CD1 1 
ATOM   2773 C CD2 . LEU   B 2 46  ? 50.40769 -22.59472 -12.03886 1.000 113.89700 ? 139 LEU   B CD2 1 
ATOM   2774 N N   . LEU   B 2 47  ? 47.61644 -21.32853 -16.71681 1.000 117.73966 ? 140 LEU   B N   1 
ATOM   2775 C CA  . LEU   B 2 47  ? 46.17206 -21.30963 -16.88634 1.000 112.15452 ? 140 LEU   B CA  1 
ATOM   2776 C C   . LEU   B 2 47  ? 45.77000 -21.96712 -18.20321 1.000 110.66095 ? 140 LEU   B C   1 
ATOM   2777 O O   . LEU   B 2 47  ? 46.56408 -22.08401 -19.13940 1.000 111.55997 ? 140 LEU   B O   1 
ATOM   2778 C CB  . LEU   B 2 47  ? 45.64238 -19.87548 -16.83630 1.000 105.57903 ? 140 LEU   B CB  1 
ATOM   2779 C CG  . LEU   B 2 47  ? 45.82749 -19.12701 -15.51528 1.000 107.55579 ? 140 LEU   B CG  1 
ATOM   2780 C CD1 . LEU   B 2 47  ? 45.27974 -17.71182 -15.61632 1.000 96.58736  ? 140 LEU   B CD1 1 
ATOM   2781 C CD2 . LEU   B 2 47  ? 45.16108 -19.88301 -14.37666 1.000 100.47601 ? 140 LEU   B CD2 1 
ATOM   2782 N N   . GLN   B 2 48  ? 44.51243 -22.39402 -18.26294 1.000 114.82376 ? 141 GLN   B N   1 
ATOM   2783 C CA  . GLN   B 2 48  ? 43.94076 -23.02756 -19.43897 1.000 118.96964 ? 141 GLN   B CA  1 
ATOM   2784 C C   . GLN   B 2 48  ? 42.67759 -22.29265 -19.86063 1.000 117.04773 ? 141 GLN   B C   1 
ATOM   2785 O O   . GLN   B 2 48  ? 42.01113 -21.66820 -19.02868 1.000 112.37534 ? 141 GLN   B O   1 
ATOM   2786 C CB  . GLN   B 2 48  ? 43.61562 -24.50503 -19.17028 1.000 123.67682 ? 141 GLN   B CB  1 
ATOM   2787 C CG  . GLN   B 2 48  ? 44.83006 -25.35173 -18.81908 1.000 124.43441 ? 141 GLN   B CG  1 
ATOM   2788 C CD  . GLN   B 2 48  ? 45.86954 -25.37229 -19.92428 1.000 128.54407 ? 141 GLN   B CD  1 
ATOM   2789 O OE1 . GLN   B 2 48  ? 45.53777 -25.29798 -21.10787 1.000 139.29835 ? 141 GLN   B OE1 1 
ATOM   2790 N NE2 . GLN   B 2 48  ? 47.13728 -25.46957 -19.54123 1.000 124.67480 ? 141 GLN   B NE2 1 
ATOM   2791 N N   . PRO   B 2 49  ? 42.33056 -22.33928 -21.15068 1.000 123.11858 ? 142 PRO   B N   1 
ATOM   2792 C CA  . PRO   B 2 49  ? 41.12712 -21.62293 -21.60779 1.000 108.98263 ? 142 PRO   B CA  1 
ATOM   2793 C C   . PRO   B 2 49  ? 39.84112 -22.10704 -20.96181 1.000 104.35771 ? 142 PRO   B C   1 
ATOM   2794 O O   . PRO   B 2 49  ? 38.89321 -21.32185 -20.83320 1.000 103.93975 ? 142 PRO   B O   1 
ATOM   2795 C CB  . PRO   B 2 49  ? 41.12737 -21.87504 -23.12219 1.000 113.89637 ? 142 PRO   B CB  1 
ATOM   2796 C CG  . PRO   B 2 49  ? 42.55524 -22.14989 -23.45749 1.000 115.88728 ? 142 PRO   B CG  1 
ATOM   2797 C CD  . PRO   B 2 49  ? 43.10417 -22.89223 -22.27568 1.000 122.82130 ? 142 PRO   B CD  1 
ATOM   2798 N N   . LYS   B 2 50  ? 39.77512 -23.37523 -20.54939 1.000 100.96980 ? 143 LYS   B N   1 
ATOM   2799 C CA  . LYS   B 2 50  ? 38.55596 -23.88146 -19.92789 1.000 101.60470 ? 143 LYS   B CA  1 
ATOM   2800 C C   . LYS   B 2 50  ? 38.32006 -23.25438 -18.55940 1.000 110.57224 ? 143 LYS   B C   1 
ATOM   2801 O O   . LYS   B 2 50  ? 37.16797 -23.12817 -18.12827 1.000 102.13348 ? 143 LYS   B O   1 
ATOM   2802 C CB  . LYS   B 2 50  ? 38.61674 -25.40627 -19.81521 1.000 116.78113 ? 143 LYS   B CB  1 
ATOM   2803 C CG  . LYS   B 2 50  ? 37.31457 -26.06707 -19.36814 1.000 108.31800 ? 143 LYS   B CG  1 
ATOM   2804 C CD  . LYS   B 2 50  ? 36.54322 -26.67414 -20.53874 1.000 125.78719 ? 143 LYS   B CD  1 
ATOM   2805 C CE  . LYS   B 2 50  ? 35.86469 -25.61338 -21.39545 1.000 116.03625 ? 143 LYS   B CE  1 
ATOM   2806 N NZ  . LYS   B 2 50  ? 35.11709 -26.20843 -22.53788 1.000 114.44371 ? 143 LYS   B NZ  1 
ATOM   2807 N N   . MET   B 2 51  ? 39.38991 -22.85281 -17.86752 1.000 102.00901 ? 144 MET   B N   1 
ATOM   2808 C CA  . MET   B 2 51  ? 39.23079 -22.20926 -16.56699 1.000 103.90900 ? 144 MET   B CA  1 
ATOM   2809 C C   . MET   B 2 51  ? 38.47809 -20.89077 -16.69391 1.000 89.39877  ? 144 MET   B C   1 
ATOM   2810 O O   . MET   B 2 51  ? 37.67665 -20.53753 -15.82096 1.000 87.21497  ? 144 MET   B O   1 
ATOM   2811 C CB  . MET   B 2 51  ? 40.59809 -21.98512 -15.92177 1.000 94.01854  ? 144 MET   B CB  1 
ATOM   2812 C CG  . MET   B 2 51  ? 41.45412 -23.23626 -15.83064 1.000 111.24333 ? 144 MET   B CG  1 
ATOM   2813 S SD  . MET   B 2 51  ? 43.09389 -22.90620 -15.15802 1.000 106.72614 ? 144 MET   B SD  1 
ATOM   2814 C CE  . MET   B 2 51  ? 43.84383 -24.52682 -15.29194 1.000 118.28043 ? 144 MET   B CE  1 
ATOM   2815 N N   . ARG   B 2 52  ? 38.72300 -20.14932 -17.77698 1.000 87.28385  ? 145 ARG   B N   1 
ATOM   2816 C CA  . ARG   B 2 52  ? 38.00363 -18.89896 -17.99650 1.000 90.79165  ? 145 ARG   B CA  1 
ATOM   2817 C C   . ARG   B 2 52  ? 36.51721 -19.15052 -18.21628 1.000 86.82692  ? 145 ARG   B C   1 
ATOM   2818 O O   . ARG   B 2 52  ? 35.67365 -18.36218 -17.77332 1.000 84.24986  ? 145 ARG   B O   1 
ATOM   2819 C CB  . ARG   B 2 52  ? 38.60676 -18.15196 -19.18642 1.000 88.58563  ? 145 ARG   B CB  1 
ATOM   2820 C CG  . ARG   B 2 52  ? 37.88642 -16.86191 -19.54747 1.000 88.68619  ? 145 ARG   B CG  1 
ATOM   2821 C CD  . ARG   B 2 52  ? 38.53218 -16.18858 -20.74722 1.000 78.27298  ? 145 ARG   B CD  1 
ATOM   2822 N NE  . ARG   B 2 52  ? 37.77709 -15.02481 -21.19515 1.000 81.24799  ? 145 ARG   B NE  1 
ATOM   2823 C CZ  . ARG   B 2 52  ? 36.78195 -15.07068 -22.07015 1.000 83.41775  ? 145 ARG   B CZ  1 
ATOM   2824 N NH1 . ARG   B 2 52  ? 36.38862 -16.21268 -22.60998 1.000 86.08372  ? 145 ARG   B NH1 1 
ATOM   2825 N NH2 . ARG   B 2 52  ? 36.16511 -13.94274 -22.41121 1.000 79.06153  ? 145 ARG   B NH2 1 
ATOM   2826 N N   . ALA   B 2 53  ? 36.17652 -20.25012 -18.89234 1.000 86.30031  ? 146 ALA   B N   1 
ATOM   2827 C CA  . ALA   B 2 53  ? 34.77190 -20.56531 -19.13071 1.000 85.12262  ? 146 ALA   B CA  1 
ATOM   2828 C C   . ALA   B 2 53  ? 34.05595 -20.92511 -17.83472 1.000 87.07155  ? 146 ALA   B C   1 
ATOM   2829 O O   . ALA   B 2 53  ? 32.91439 -20.50444 -17.61311 1.000 87.47794  ? 146 ALA   B O   1 
ATOM   2830 C CB  . ALA   B 2 53  ? 34.65440 -21.70337 -20.14360 1.000 83.24909  ? 146 ALA   B CB  1 
ATOM   2831 N N   . ILE   B 2 54  ? 34.71025 -21.70062 -16.96686 1.000 91.12848  ? 147 ILE   B N   1 
ATOM   2832 C CA  . ILE   B 2 54  ? 34.09194 -22.09230 -15.70276 1.000 87.34362  ? 147 ILE   B CA  1 
ATOM   2833 C C   . ILE   B 2 54  ? 33.87128 -20.87316 -14.81648 1.000 90.59981  ? 147 ILE   B C   1 
ATOM   2834 O O   . ILE   B 2 54  ? 32.85117 -20.76520 -14.12423 1.000 90.24732  ? 147 ILE   B O   1 
ATOM   2835 C CB  . ILE   B 2 54  ? 34.95096 -23.15858 -14.99722 1.000 101.79113 ? 147 ILE   B CB  1 
ATOM   2836 C CG1 . ILE   B 2 54  ? 35.13613 -24.37912 -15.90090 1.000 95.28393  ? 147 ILE   B CG1 1 
ATOM   2837 C CG2 . ILE   B 2 54  ? 34.32112 -23.56722 -13.67365 1.000 108.10867 ? 147 ILE   B CG2 1 
ATOM   2838 C CD1 . ILE   B 2 54  ? 36.01008 -25.45685 -15.29702 1.000 107.55598 ? 147 ILE   B CD1 1 
ATOM   2839 N N   . LEU   B 2 55  ? 34.81844 -19.93310 -14.82777 1.000 85.27361  ? 148 LEU   B N   1 
ATOM   2840 C CA  . LEU   B 2 55  ? 34.68320 -18.73600 -14.00450 1.000 81.97695  ? 148 LEU   B CA  1 
ATOM   2841 C C   . LEU   B 2 55  ? 33.55563 -17.84412 -14.51039 1.000 82.46550  ? 148 LEU   B C   1 
ATOM   2842 O O   . LEU   B 2 55  ? 32.71123 -17.39082 -13.72872 1.000 83.60282  ? 148 LEU   B O   1 
ATOM   2843 C CB  . LEU   B 2 55  ? 36.00419 -17.96783 -13.97390 1.000 92.97592  ? 148 LEU   B CB  1 
ATOM   2844 C CG  . LEU   B 2 55  ? 35.98955 -16.67396 -13.15767 1.000 98.25713  ? 148 LEU   B CG  1 
ATOM   2845 C CD1 . LEU   B 2 55  ? 35.70312 -16.96845 -11.69271 1.000 82.04410  ? 148 LEU   B CD1 1 
ATOM   2846 C CD2 . LEU   B 2 55  ? 37.30066 -15.92247 -13.31369 1.000 102.70924 ? 148 LEU   B CD2 1 
ATOM   2847 N N   . LEU   B 2 56  ? 33.52775 -17.57780 -15.81892 1.000 83.05457  ? 149 LEU   B N   1 
ATOM   2848 C CA  . LEU   B 2 56  ? 32.47688 -16.73193 -16.37627 1.000 75.63367  ? 149 LEU   B CA  1 
ATOM   2849 C C   . LEU   B 2 56  ? 31.10507 -17.37075 -16.20331 1.000 81.17242  ? 149 LEU   B C   1 
ATOM   2850 O O   . LEU   B 2 56  ? 30.12514 -16.68017 -15.89948 1.000 80.64887  ? 149 LEU   B O   1 
ATOM   2851 C CB  . LEU   B 2 56  ? 32.75674 -16.44808 -17.85188 1.000 79.93516  ? 149 LEU   B CB  1 
ATOM   2852 C CG  . LEU   B 2 56  ? 33.98708 -15.59197 -18.15883 1.000 76.51980  ? 149 LEU   B CG  1 
ATOM   2853 C CD1 . LEU   B 2 56  ? 34.16384 -15.42387 -19.65960 1.000 85.05123  ? 149 LEU   B CD1 1 
ATOM   2854 C CD2 . LEU   B 2 56  ? 33.88443 -14.23810 -17.47338 1.000 72.87948  ? 149 LEU   B CD2 1 
ATOM   2855 N N   . ASP   B 2 57  ? 31.01643 -18.69093 -16.38783 1.000 78.32243  ? 150 ASP   B N   1 
ATOM   2856 C CA  . ASP   B 2 57  ? 29.74563 -19.38093 -16.18999 1.000 81.12459  ? 150 ASP   B CA  1 
ATOM   2857 C C   . ASP   B 2 57  ? 29.29051 -19.28732 -14.73947 1.000 89.24455  ? 150 ASP   B C   1 
ATOM   2858 O O   . ASP   B 2 57  ? 28.09009 -19.17853 -14.46206 1.000 85.80066  ? 150 ASP   B O   1 
ATOM   2859 C CB  . ASP   B 2 57  ? 29.86911 -20.84190 -16.62106 1.000 94.46154  ? 150 ASP   B CB  1 
ATOM   2860 C CG  . ASP   B 2 57  ? 28.55635 -21.59165 -16.52136 1.000 107.82017 ? 150 ASP   B CG  1 
ATOM   2861 O OD1 . ASP   B 2 57  ? 27.67870 -21.37330 -17.38308 1.000 121.25524 ? 150 ASP   B OD1 1 
ATOM   2862 O OD2 . ASP   B 2 57  ? 28.40112 -22.39795 -15.58068 1.000 102.07747 ? 150 ASP   B OD2 1 
ATOM   2863 N N   . TRP   B 2 58  ? 30.23701 -19.32897 -13.79907 1.000 87.69504  ? 151 TRP   B N   1 
ATOM   2864 C CA  . TRP   B 2 58  ? 29.88834 -19.15999 -12.39290 1.000 86.83087  ? 151 TRP   B CA  1 
ATOM   2865 C C   . TRP   B 2 58  ? 29.39912 -17.74474 -12.11505 1.000 85.29493  ? 151 TRP   B C   1 
ATOM   2866 O O   . TRP   B 2 58  ? 28.44661 -17.54981 -11.35102 1.000 84.45943  ? 151 TRP   B O   1 
ATOM   2867 C CB  . TRP   B 2 58  ? 31.09001 -19.50180 -11.51240 1.000 101.23596 ? 151 TRP   B CB  1 
ATOM   2868 C CG  . TRP   B 2 58  ? 30.91825 -19.12177 -10.07361 1.000 103.64652 ? 151 TRP   B CG  1 
ATOM   2869 C CD1 . TRP   B 2 58  ? 30.04666 -19.67058 -9.17892  1.000 104.98772 ? 151 TRP   B CD1 1 
ATOM   2870 C CD2 . TRP   B 2 58  ? 31.64846 -18.11734 -9.35812  1.000 99.40248  ? 151 TRP   B CD2 1 
ATOM   2871 N NE1 . TRP   B 2 58  ? 30.18305 -19.06524 -7.95294  1.000 112.61073 ? 151 TRP   B NE1 1 
ATOM   2872 C CE2 . TRP   B 2 58  ? 31.16061 -18.10878 -8.03625  1.000 111.50264 ? 151 TRP   B CE2 1 
ATOM   2873 C CE3 . TRP   B 2 58  ? 32.66493 -17.22296 -9.70774  1.000 99.46777  ? 151 TRP   B CE3 1 
ATOM   2874 C CZ2 . TRP   B 2 58  ? 31.65406 -17.24097 -7.06371  1.000 107.89596 ? 151 TRP   B CZ2 1 
ATOM   2875 C CZ3 . TRP   B 2 58  ? 33.15377 -16.36213 -8.74027  1.000 96.73498  ? 151 TRP   B CZ3 1 
ATOM   2876 C CH2 . TRP   B 2 58  ? 32.64789 -16.37753 -7.43469  1.000 101.97579 ? 151 TRP   B CH2 1 
ATOM   2877 N N   . LEU   B 2 59  ? 30.03347 -16.74446 -12.73182 1.000 86.29282  ? 152 LEU   B N   1 
ATOM   2878 C CA  . LEU   B 2 59  ? 29.58095 -15.36861 -12.55900 1.000 74.09193  ? 152 LEU   B CA  1 
ATOM   2879 C C   . LEU   B 2 59  ? 28.19173 -15.15810 -13.14733 1.000 71.81690  ? 152 LEU   B C   1 
ATOM   2880 O O   . LEU   B 2 59  ? 27.42390 -14.33286 -12.63914 1.000 72.70927  ? 152 LEU   B O   1 
ATOM   2881 C CB  . LEU   B 2 59  ? 30.58188 -14.40163 -13.19171 1.000 69.63782  ? 152 LEU   B CB  1 
ATOM   2882 C CG  . LEU   B 2 59  ? 31.98308 -14.36740 -12.57823 1.000 80.21223  ? 152 LEU   B CG  1 
ATOM   2883 C CD1 . LEU   B 2 59  ? 32.89035 -13.44453 -13.37535 1.000 79.85603  ? 152 LEU   B CD1 1 
ATOM   2884 C CD2 . LEU   B 2 59  ? 31.92343 -13.93503 -11.12089 1.000 69.42989  ? 152 LEU   B CD2 1 
ATOM   2885 N N   . MET   B 2 60  ? 27.85153 -15.88739 -14.21430 1.000 67.03994  ? 153 MET   B N   1 
ATOM   2886 C CA  . MET   B 2 60  ? 26.49843 -15.81684 -14.75905 1.000 73.76358  ? 153 MET   B CA  1 
ATOM   2887 C C   . MET   B 2 60  ? 25.47393 -16.27300 -13.72964 1.000 70.81266  ? 153 MET   B C   1 
ATOM   2888 O O   . MET   B 2 60  ? 24.44108 -15.62288 -13.53038 1.000 79.32096  ? 153 MET   B O   1 
ATOM   2889 C CB  . MET   B 2 60  ? 26.38572 -16.67043 -16.02288 1.000 76.54441  ? 153 MET   B CB  1 
ATOM   2890 C CG  . MET   B 2 60  ? 27.20027 -16.18976 -17.20414 1.000 86.00308  ? 153 MET   B CG  1 
ATOM   2891 S SD  . MET   B 2 60  ? 26.74806 -17.08617 -18.70192 1.000 86.10831  ? 153 MET   B SD  1 
ATOM   2892 C CE  . MET   B 2 60  ? 28.04353 -16.57256 -19.82209 1.000 84.86321  ? 153 MET   B CE  1 
ATOM   2893 N N   . GLU   B 2 61  ? 25.74320 -17.40207 -13.07057 1.000 75.73015  ? 154 GLU   B N   1 
ATOM   2894 C CA  . GLU   B 2 61  ? 24.81817 -17.91330 -12.06559 1.000 78.21313  ? 154 GLU   B CA  1 
ATOM   2895 C C   . GLU   B 2 61  ? 24.70583 -16.95653 -10.88567 1.000 81.77887  ? 154 GLU   B C   1 
ATOM   2896 O O   . GLU   B 2 61  ? 23.61500 -16.76297 -10.33626 1.000 78.46797  ? 154 GLU   B O   1 
ATOM   2897 C CB  . GLU   B 2 61  ? 25.26919 -19.29893 -11.60319 1.000 94.00193  ? 154 GLU   B CB  1 
ATOM   2898 C CG  . GLU   B 2 61  ? 24.25055 -20.04673 -10.75977 1.000 102.17898 ? 154 GLU   B CG  1 
ATOM   2899 C CD  . GLU   B 2 61  ? 24.65516 -21.48720 -10.50711 1.000 109.68246 ? 154 GLU   B CD  1 
ATOM   2900 O OE1 . GLU   B 2 61  ? 25.78053 -21.86711 -10.89495 1.000 107.63421 ? 154 GLU   B OE1 1 
ATOM   2901 O OE2 . GLU   B 2 61  ? 23.84716 -22.24088 -9.92500  1.000 111.71879 ? 154 GLU   B OE2 1 
ATOM   2902 N N   . VAL   B 2 62  ? 25.82280 -16.34040 -10.48933 1.000 82.30698  ? 155 VAL   B N   1 
ATOM   2903 C CA  . VAL   B 2 62  ? 25.79388 -15.37013 -9.39758  1.000 68.22330  ? 155 VAL   B CA  1 
ATOM   2904 C C   . VAL   B 2 62  ? 24.90546 -14.18670 -9.75922  1.000 78.61554  ? 155 VAL   B C   1 
ATOM   2905 O O   . VAL   B 2 62  ? 24.15051 -13.67838 -8.92072  1.000 72.34936  ? 155 VAL   B O   1 
ATOM   2906 C CB  . VAL   B 2 62  ? 27.22456 -14.92001 -9.04487  1.000 78.47325  ? 155 VAL   B CB  1 
ATOM   2907 C CG1 . VAL   B 2 62  ? 27.19522 -13.78922 -8.02740  1.000 76.07087  ? 155 VAL   B CG1 1 
ATOM   2908 C CG2 . VAL   B 2 62  ? 28.03340 -16.09204 -8.51236  1.000 84.57728  ? 155 VAL   B CG2 1 
ATOM   2909 N N   . CYS   B 2 63  ? 24.97125 -13.73671 -11.01529 1.000 82.20052  ? 156 CYS   B N   1 
ATOM   2910 C CA  . CYS   B 2 63  ? 24.14863 -12.60845 -11.43993 1.000 75.40188  ? 156 CYS   B CA  1 
ATOM   2911 C C   . CYS   B 2 63  ? 22.66588 -12.95508 -11.40050 1.000 69.40461  ? 156 CYS   B C   1 
ATOM   2912 O O   . CYS   B 2 63  ? 21.83463 -12.11295 -11.04130 1.000 73.09052  ? 156 CYS   B O   1 
ATOM   2913 C CB  . CYS   B 2 63  ? 24.55348 -12.15880 -12.84404 1.000 70.35415  ? 156 CYS   B CB  1 
ATOM   2914 S SG  . CYS   B 2 63  ? 26.19243 -11.41071 -12.95168 1.000 74.03355  ? 156 CYS   B SG  1 
ATOM   2915 N N   . GLU   B 2 64  ? 22.31299 -14.18903 -11.76891 1.000 75.73467  ? 157 GLU   B N   1 
ATOM   2916 C CA  . GLU   B 2 64  ? 20.90551 -14.57529 -11.78448 1.000 85.86435  ? 157 GLU   B CA  1 
ATOM   2917 C C   . GLU   B 2 64  ? 20.34611 -14.69428 -10.37179 1.000 78.59665  ? 157 GLU   B C   1 
ATOM   2918 O O   . GLU   B 2 64  ? 19.17414 -14.37747 -10.13573 1.000 87.91509  ? 157 GLU   B O   1 
ATOM   2919 C CB  . GLU   B 2 64  ? 20.72678 -15.88873 -12.54620 1.000 82.21165  ? 157 GLU   B CB  1 
ATOM   2920 C CG  . GLU   B 2 64  ? 19.27305 -16.27912 -12.77270 1.000 88.42865  ? 157 GLU   B CG  1 
ATOM   2921 C CD  . GLU   B 2 64  ? 19.12813 -17.56775 -13.55843 1.000 99.83004  ? 157 GLU   B CD  1 
ATOM   2922 O OE1 . GLU   B 2 64  ? 20.14495 -18.26696 -13.75045 1.000 101.27250 ? 157 GLU   B OE1 1 
ATOM   2923 O OE2 . GLU   B 2 64  ? 17.99710 -17.88058 -13.98636 1.000 105.02472 ? 157 GLU   B OE2 1 
ATOM   2924 N N   . VAL   B 2 65  ? 21.16632 -15.14767 -9.42068  1.000 88.43174  ? 158 VAL   B N   1 
ATOM   2925 C CA  . VAL   B 2 65  ? 20.70494 -15.28144 -8.04022  1.000 85.38369  ? 158 VAL   B CA  1 
ATOM   2926 C C   . VAL   B 2 65  ? 20.34389 -13.91632 -7.46775  1.000 84.65103  ? 158 VAL   B C   1 
ATOM   2927 O O   . VAL   B 2 65  ? 19.26874 -13.72980 -6.88551  1.000 88.50490  ? 158 VAL   B O   1 
ATOM   2928 C CB  . VAL   B 2 65  ? 21.76919 -15.98995 -7.18348  1.000 92.39567  ? 158 VAL   B CB  1 
ATOM   2929 C CG1 . VAL   B 2 65  ? 21.36947 -15.96459 -5.71682  1.000 99.35771  ? 158 VAL   B CG1 1 
ATOM   2930 C CG2 . VAL   B 2 65  ? 21.96383 -17.42079 -7.65853  1.000 96.09353  ? 158 VAL   B CG2 1 
ATOM   2931 N N   . TYR   B 2 66  ? 21.23429 -12.94135 -7.62865  1.000 84.63038  ? 159 TYR   B N   1 
ATOM   2932 C CA  . TYR   B 2 66  ? 20.99122 -11.58146 -7.17007  1.000 80.95593  ? 159 TYR   B CA  1 
ATOM   2933 C C   . TYR   B 2 66  ? 20.27184 -10.73226 -8.20957  1.000 77.18397  ? 159 TYR   B C   1 
ATOM   2934 O O   . TYR   B 2 66  ? 20.13640 -9.51966  -8.01421  1.000 73.00675  ? 159 TYR   B O   1 
ATOM   2935 C CB  . TYR   B 2 66  ? 22.31096 -10.91995 -6.76667  1.000 78.29156  ? 159 TYR   B CB  1 
ATOM   2936 C CG  . TYR   B 2 66  ? 22.93113 -11.53312 -5.53198  1.000 77.41958  ? 159 TYR   B CG  1 
ATOM   2937 C CD1 . TYR   B 2 66  ? 23.73624 -12.66077 -5.62210  1.000 83.50981  ? 159 TYR   B CD1 1 
ATOM   2938 C CD2 . TYR   B 2 66  ? 22.70336 -10.98977 -4.27434  1.000 78.39755  ? 159 TYR   B CD2 1 
ATOM   2939 C CE1 . TYR   B 2 66  ? 24.30054 -13.22766 -4.49507  1.000 86.38069  ? 159 TYR   B CE1 1 
ATOM   2940 C CE2 . TYR   B 2 66  ? 23.26427 -11.54935 -3.14193  1.000 91.13869  ? 159 TYR   B CE2 1 
ATOM   2941 C CZ  . TYR   B 2 66  ? 24.06212 -12.66793 -3.25783  1.000 82.52504  ? 159 TYR   B CZ  1 
ATOM   2942 O OH  . TYR   B 2 66  ? 24.62278 -13.22878 -2.13291  1.000 96.85690  ? 159 TYR   B OH  1 
ATOM   2943 N N   . LYS   B 2 67  ? 19.81206 -11.34482 -9.30338  1.000 87.26907  ? 160 LYS   B N   1 
ATOM   2944 C CA  . LYS   B 2 67  ? 19.02679 -10.66248 -10.33298 1.000 74.21646  ? 160 LYS   B CA  1 
ATOM   2945 C C   . LYS   B 2 67  ? 19.77562 -9.45974  -10.90301 1.000 64.10073  ? 160 LYS   B C   1 
ATOM   2946 O O   . LYS   B 2 67  ? 19.20306 -8.38807  -11.11178 1.000 63.29938  ? 160 LYS   B O   1 
ATOM   2947 C CB  . LYS   B 2 67  ? 17.65433 -10.25280 -9.79407  1.000 76.35430  ? 160 LYS   B CB  1 
ATOM   2948 C CG  . LYS   B 2 67  ? 16.84504 -11.42108 -9.25013  1.000 85.41186  ? 160 LYS   B CG  1 
ATOM   2949 C CD  . LYS   B 2 67  ? 15.46702 -10.98597 -8.78155  1.000 98.49314  ? 160 LYS   B CD  1 
ATOM   2950 C CE  . LYS   B 2 67  ? 14.66369 -12.17360 -8.27322  1.000 102.53944 ? 160 LYS   B CE  1 
ATOM   2951 N NZ  . LYS   B 2 67  ? 13.28913 -11.78449 -7.85366  1.000 100.90514 ? 160 LYS   B NZ  1 
ATOM   2952 N N   . LEU   B 2 68  ? 21.06878 -9.63925  -11.15532 1.000 70.43720  ? 161 LEU   B N   1 
ATOM   2953 C CA  . LEU   B 2 68  ? 21.87921 -8.58258  -11.73969 1.000 61.32715  ? 161 LEU   B CA  1 
ATOM   2954 C C   . LEU   B 2 68  ? 21.65357 -8.51315  -13.24502 1.000 55.44448  ? 161 LEU   B C   1 
ATOM   2955 O O   . LEU   B 2 68  ? 21.30517 -9.50608  -13.88953 1.000 58.79408  ? 161 LEU   B O   1 
ATOM   2956 C CB  . LEU   B 2 68  ? 23.36094 -8.81179  -11.43909 1.000 64.99873  ? 161 LEU   B CB  1 
ATOM   2957 C CG  . LEU   B 2 68  ? 23.74067 -8.88569  -9.95862  1.000 63.38628  ? 161 LEU   B CG  1 
ATOM   2958 C CD1 . LEU   B 2 68  ? 25.23389 -9.12638  -9.79670  1.000 64.58647  ? 161 LEU   B CD1 1 
ATOM   2959 C CD2 . LEU   B 2 68  ? 23.31402 -7.62081  -9.22848  1.000 56.27849  ? 161 LEU   B CD2 1 
ATOM   2960 N N   . HIS   B 2 69  ? 21.85374 -7.32277  -13.80245 1.000 54.86460  ? 162 HIS   B N   1 
ATOM   2961 C CA  . HIS   B 2 69  ? 21.60389 -7.11344  -15.21893 1.000 62.46674  ? 162 HIS   B CA  1 
ATOM   2962 C C   . HIS   B 2 69  ? 22.67004 -7.79851  -16.07103 1.000 56.92541  ? 162 HIS   B C   1 
ATOM   2963 O O   . HIS   B 2 69  ? 23.79001 -8.06541  -15.62561 1.000 57.03680  ? 162 HIS   B O   1 
ATOM   2964 C CB  . HIS   B 2 69  ? 21.55376 -5.61863  -15.54021 1.000 59.02141  ? 162 HIS   B CB  1 
ATOM   2965 C CG  . HIS   B 2 69  ? 20.30495 -4.94045  -15.06902 1.000 68.97782  ? 162 HIS   B CG  1 
ATOM   2966 N ND1 . HIS   B 2 69  ? 20.07097 -4.64923  -13.74253 1.000 76.89853  ? 162 HIS   B ND1 1 
ATOM   2967 C CD2 . HIS   B 2 69  ? 19.21731 -4.50383  -15.74770 1.000 76.92025  ? 162 HIS   B CD2 1 
ATOM   2968 C CE1 . HIS   B 2 69  ? 18.89514 -4.05867  -13.62470 1.000 74.25191  ? 162 HIS   B CE1 1 
ATOM   2969 N NE2 . HIS   B 2 69  ? 18.35652 -3.95856  -14.82662 1.000 79.66470  ? 162 HIS   B NE2 1 
ATOM   2970 N N   . ARG   B 2 70  ? 22.29578 -8.08933  -17.32044 1.000 63.14365  ? 163 ARG   B N   1 
ATOM   2971 C CA  . ARG   B 2 70  ? 23.24088 -8.68100  -18.26231 1.000 63.35511  ? 163 ARG   B CA  1 
ATOM   2972 C C   . ARG   B 2 70  ? 24.42831 -7.75846  -18.50077 1.000 53.11440  ? 163 ARG   B C   1 
ATOM   2973 O O   . ARG   B 2 70  ? 25.56384 -8.22259  -18.66014 1.000 57.44381  ? 163 ARG   B O   1 
ATOM   2974 C CB  . ARG   B 2 70  ? 22.53881 -8.99579  -19.58333 1.000 55.34118  ? 163 ARG   B CB  1 
ATOM   2975 C CG  . ARG   B 2 70  ? 21.33297 -9.90906  -19.44963 1.000 61.05131  ? 163 ARG   B CG  1 
ATOM   2976 C CD  . ARG   B 2 70  ? 20.70360 -10.19053 -20.80433 1.000 68.40076  ? 163 ARG   B CD  1 
ATOM   2977 N NE  . ARG   B 2 70  ? 19.55996 -11.08844 -20.69746 1.000 61.29525  ? 163 ARG   B NE  1 
ATOM   2978 C CZ  . ARG   B 2 70  ? 19.64438 -12.41163 -20.71008 1.000 65.37028  ? 163 ARG   B CZ  1 
ATOM   2979 N NH1 . ARG   B 2 70  ? 20.80878 -13.02866 -20.82649 1.000 63.49194  ? 163 ARG   B NH1 1 
ATOM   2980 N NH2 . ARG   B 2 70  ? 18.53298 -13.13396 -20.60085 1.000 74.65810  ? 163 ARG   B NH2 1 
ATOM   2981 N N   . GLU   B 2 71  ? 24.18146 -6.44623  -18.53490 1.000 54.01009  ? 164 GLU   B N   1 
ATOM   2982 C CA  . GLU   B 2 71  ? 25.26852 -5.48565  -18.69355 1.000 55.02809  ? 164 GLU   B CA  1 
ATOM   2983 C C   . GLU   B 2 71  ? 26.29338 -5.62458  -17.57554 1.000 55.94999  ? 164 GLU   B C   1 
ATOM   2984 O O   . GLU   B 2 71  ? 27.49948 -5.47528  -17.80564 1.000 56.72966  ? 164 GLU   B O   1 
ATOM   2985 C CB  . GLU   B 2 71  ? 24.70360 -4.06425  -18.73686 1.000 60.40961  ? 164 GLU   B CB  1 
ATOM   2986 C CG  . GLU   B 2 71  ? 25.75177 -2.95852  -18.71084 1.000 65.11249  ? 164 GLU   B CG  1 
ATOM   2987 C CD  . GLU   B 2 71  ? 26.52228 -2.83872  -20.01292 1.000 62.84070  ? 164 GLU   B CD  1 
ATOM   2988 O OE1 . GLU   B 2 71  ? 26.10234 -3.44922  -21.01851 1.000 58.22607  ? 164 GLU   B OE1 1 
ATOM   2989 O OE2 . GLU   B 2 71  ? 27.54926 -2.12817  -20.03003 1.000 63.16683  ? 164 GLU   B OE2 1 
ATOM   2990 N N   . THR   B 2 72  ? 25.83231 -5.92682  -16.35950 1.000 59.40565  ? 165 THR   B N   1 
ATOM   2991 C CA  . THR   B 2 72  ? 26.75016 -6.08059  -15.23582 1.000 55.07293  ? 165 THR   B CA  1 
ATOM   2992 C C   . THR   B 2 72  ? 27.68730 -7.26468  -15.44329 1.000 54.42894  ? 165 THR   B C   1 
ATOM   2993 O O   . THR   B 2 72  ? 28.88561 -7.17536  -15.15047 1.000 59.87923  ? 165 THR   B O   1 
ATOM   2994 C CB  . THR   B 2 72  ? 25.96271 -6.23735  -13.93381 1.000 59.99145  ? 165 THR   B CB  1 
ATOM   2995 O OG1 . THR   B 2 72  ? 25.12552 -5.08970  -13.74071 1.000 62.83038  ? 165 THR   B OG1 1 
ATOM   2996 C CG2 . THR   B 2 72  ? 26.90528 -6.37017  -12.75048 1.000 60.20129  ? 165 THR   B CG2 1 
ATOM   2997 N N   . PHE   B 2 73  ? 27.16510 -8.38130  -15.95501 1.000 56.48271  ? 166 PHE   B N   1 
ATOM   2998 C CA  . PHE   B 2 73  ? 28.01608 -9.54291  -16.19334 1.000 63.28582  ? 166 PHE   B CA  1 
ATOM   2999 C C   . PHE   B 2 73  ? 29.06821 -9.24878  -17.25491 1.000 55.18490  ? 166 PHE   B C   1 
ATOM   3000 O O   . PHE   B 2 73  ? 30.25639 -9.53327  -17.06353 1.000 59.67122  ? 166 PHE   B O   1 
ATOM   3001 C CB  . PHE   B 2 73  ? 27.17923 -10.75124 -16.60919 1.000 57.85192  ? 166 PHE   B CB  1 
ATOM   3002 C CG  . PHE   B 2 73  ? 27.99511 -11.84829 -17.22638 1.000 61.88771  ? 166 PHE   B CG  1 
ATOM   3003 C CD1 . PHE   B 2 73  ? 28.82712 -12.62887 -16.44205 1.000 60.21807  ? 166 PHE   B CD1 1 
ATOM   3004 C CD2 . PHE   B 2 73  ? 27.95456 -12.08137 -18.59126 1.000 67.71629  ? 166 PHE   B CD2 1 
ATOM   3005 C CE1 . PHE   B 2 73  ? 29.59358 -13.62776 -17.00215 1.000 67.45288  ? 166 PHE   B CE1 1 
ATOM   3006 C CE2 . PHE   B 2 73  ? 28.71946 -13.08169 -19.15741 1.000 66.72246  ? 166 PHE   B CE2 1 
ATOM   3007 C CZ  . PHE   B 2 73  ? 29.54157 -13.85391 -18.36026 1.000 75.48475  ? 166 PHE   B CZ  1 
ATOM   3008 N N   . TYR   B 2 74  ? 28.64686 -8.68721  -18.39140 1.000 52.60860  ? 167 TYR   B N   1 
ATOM   3009 C CA  . TYR   B 2 74  ? 29.58928 -8.44440  -19.47819 1.000 56.85008  ? 167 TYR   B CA  1 
ATOM   3010 C C   . TYR   B 2 74  ? 30.59483 -7.35715  -19.12433 1.000 59.35144  ? 167 TYR   B C   1 
ATOM   3011 O O   . TYR   B 2 74  ? 31.70383 -7.34423  -19.67036 1.000 58.46263  ? 167 TYR   B O   1 
ATOM   3012 C CB  . TYR   B 2 74  ? 28.83691 -8.09618  -20.76215 1.000 51.50837  ? 167 TYR   B CB  1 
ATOM   3013 C CG  . TYR   B 2 74  ? 28.33111 -9.31351  -21.50206 1.000 56.42340  ? 167 TYR   B CG  1 
ATOM   3014 C CD1 . TYR   B 2 74  ? 29.15143 -9.99906  -22.38971 1.000 65.27335  ? 167 TYR   B CD1 1 
ATOM   3015 C CD2 . TYR   B 2 74  ? 27.03971 -9.78465  -21.30650 1.000 53.13030  ? 167 TYR   B CD2 1 
ATOM   3016 C CE1 . TYR   B 2 74  ? 28.69869 -11.11486 -23.06567 1.000 58.63270  ? 167 TYR   B CE1 1 
ATOM   3017 C CE2 . TYR   B 2 74  ? 26.57768 -10.90133 -21.97936 1.000 59.29250  ? 167 TYR   B CE2 1 
ATOM   3018 C CZ  . TYR   B 2 74  ? 27.41200 -11.56176 -22.85711 1.000 58.14298  ? 167 TYR   B CZ  1 
ATOM   3019 O OH  . TYR   B 2 74  ? 26.95924 -12.67350 -23.53016 1.000 61.26532  ? 167 TYR   B OH  1 
ATOM   3020 N N   . LEU   B 2 75  ? 30.23578 -6.44273  -18.22110 1.000 51.86310  ? 168 LEU   B N   1 
ATOM   3021 C CA  . LEU   B 2 75  ? 31.23201 -5.52671  -17.67466 1.000 50.24629  ? 168 LEU   B CA  1 
ATOM   3022 C C   . LEU   B 2 75  ? 32.30191 -6.29268  -16.90708 1.000 51.69634  ? 168 LEU   B C   1 
ATOM   3023 O O   . LEU   B 2 75  ? 33.50269 -6.05899  -17.08794 1.000 62.44651  ? 168 LEU   B O   1 
ATOM   3024 C CB  . LEU   B 2 75  ? 30.56274 -4.48912  -16.77187 1.000 48.01265  ? 168 LEU   B CB  1 
ATOM   3025 C CG  . LEU   B 2 75  ? 29.86754 -3.30023  -17.43428 1.000 54.17844  ? 168 LEU   B CG  1 
ATOM   3026 C CD1 . LEU   B 2 75  ? 29.18392 -2.44011  -16.38338 1.000 59.72904  ? 168 LEU   B CD1 1 
ATOM   3027 C CD2 . LEU   B 2 75  ? 30.86295 -2.47863  -18.23383 1.000 60.23849  ? 168 LEU   B CD2 1 
ATOM   3028 N N   . ALA   B 2 76  ? 31.87886 -7.22216  -16.04563 1.000 61.00146  ? 169 ALA   B N   1 
ATOM   3029 C CA  . ALA   B 2 76  ? 32.83345 -8.02647  -15.28995 1.000 67.16787  ? 169 ALA   B CA  1 
ATOM   3030 C C   . ALA   B 2 76  ? 33.67201 -8.90067  -16.21250 1.000 60.41471  ? 169 ALA   B C   1 
ATOM   3031 O O   . ALA   B 2 76  ? 34.85851 -9.13215  -15.95172 1.000 63.23346  ? 169 ALA   B O   1 
ATOM   3032 C CB  . ALA   B 2 76  ? 32.09788 -8.88444  -14.26208 1.000 64.75435  ? 169 ALA   B CB  1 
ATOM   3033 N N   . GLN   B 2 77  ? 33.07234 -9.39664  -17.29623 1.000 57.15483  ? 170 GLN   B N   1 
ATOM   3034 C CA  . GLN   B 2 77  ? 33.82491 -10.19122 -18.26143 1.000 60.17473  ? 170 GLN   B CA  1 
ATOM   3035 C C   . GLN   B 2 77  ? 34.90265 -9.35182  -18.93618 1.000 67.26197  ? 170 GLN   B C   1 
ATOM   3036 O O   . GLN   B 2 77  ? 36.05079 -9.78937  -19.07646 1.000 68.31793  ? 170 GLN   B O   1 
ATOM   3037 C CB  . GLN   B 2 77  ? 32.87261 -10.79354 -19.29688 1.000 62.30061  ? 170 GLN   B CB  1 
ATOM   3038 C CG  . GLN   B 2 77  ? 33.56143 -11.49190 -20.46199 1.000 65.46133  ? 170 GLN   B CG  1 
ATOM   3039 C CD  . GLN   B 2 77  ? 33.73228 -10.59016 -21.67190 1.000 67.45600  ? 170 GLN   B CD  1 
ATOM   3040 O OE1 . GLN   B 2 77  ? 32.94278 -9.67217  -21.89371 1.000 66.31041  ? 170 GLN   B OE1 1 
ATOM   3041 N NE2 . GLN   B 2 77  ? 34.76923 -10.84825 -22.46032 1.000 81.55182  ? 170 GLN   B NE2 1 
ATOM   3042 N N   . ASP   B 2 78  ? 34.55080 -8.13301  -19.35377 1.000 62.36175  ? 171 ASP   B N   1 
ATOM   3043 C CA  . ASP   B 2 78  ? 35.52376 -7.27119  -20.01743 1.000 68.13568  ? 171 ASP   B CA  1 
ATOM   3044 C C   . ASP   B 2 78  ? 36.60064 -6.80052  -19.04701 1.000 66.37209  ? 171 ASP   B C   1 
ATOM   3045 O O   . ASP   B 2 78  ? 37.77510 -6.69593  -19.42006 1.000 62.28758  ? 171 ASP   B O   1 
ATOM   3046 C CB  . ASP   B 2 78  ? 34.81794 -6.07727  -20.65981 1.000 60.14899  ? 171 ASP   B CB  1 
ATOM   3047 C CG  . ASP   B 2 78  ? 35.76677 -5.19571  -21.44819 1.000 67.62260  ? 171 ASP   B CG  1 
ATOM   3048 O OD1 . ASP   B 2 78  ? 36.23513 -5.63175  -22.52154 1.000 70.71938  ? 171 ASP   B OD1 1 
ATOM   3049 O OD2 . ASP   B 2 78  ? 36.04624 -4.06731  -20.99405 1.000 69.86382  ? 171 ASP   B OD2 1 
ATOM   3050 N N   . PHE   B 2 79  ? 36.22208 -6.50555  -17.80009 1.000 56.72883  ? 172 PHE   B N   1 
ATOM   3051 C CA  . PHE   B 2 79  ? 37.21973 -6.13877  -16.79915 1.000 64.78886  ? 172 PHE   B CA  1 
ATOM   3052 C C   . PHE   B 2 79  ? 38.18789 -7.28724  -16.55087 1.000 62.05339  ? 172 PHE   B C   1 
ATOM   3053 O O   . PHE   B 2 79  ? 39.39491 -7.07151  -16.39457 1.000 69.98172  ? 172 PHE   B O   1 
ATOM   3054 C CB  . PHE   B 2 79  ? 36.54083 -5.72971  -15.49061 1.000 58.62443  ? 172 PHE   B CB  1 
ATOM   3055 C CG  . PHE   B 2 79  ? 35.70370 -4.48405  -15.59443 1.000 60.97889  ? 172 PHE   B CG  1 
ATOM   3056 C CD1 . PHE   B 2 79  ? 35.83742 -3.62209  -16.67097 1.000 57.27506  ? 172 PHE   B CD1 1 
ATOM   3057 C CD2 . PHE   B 2 79  ? 34.78601 -4.17262  -14.60357 1.000 61.99531  ? 172 PHE   B CD2 1 
ATOM   3058 C CE1 . PHE   B 2 79  ? 35.06542 -2.47707  -16.76098 1.000 53.34052  ? 172 PHE   B CE1 1 
ATOM   3059 C CE2 . PHE   B 2 79  ? 34.01260 -3.02985  -14.68721 1.000 54.80961  ? 172 PHE   B CE2 1 
ATOM   3060 C CZ  . PHE   B 2 79  ? 34.15242 -2.18090  -15.76727 1.000 53.18252  ? 172 PHE   B CZ  1 
ATOM   3061 N N   . PHE   B 2 80  ? 37.67315 -8.51767  -16.52068 1.000 64.00687  ? 173 PHE   B N   1 
ATOM   3062 C CA  . PHE   B 2 80  ? 38.51757 -9.68109  -16.27289 1.000 70.40830  ? 173 PHE   B CA  1 
ATOM   3063 C C   . PHE   B 2 80  ? 39.50532 -9.90037  -17.41249 1.000 78.76884  ? 173 PHE   B C   1 
ATOM   3064 O O   . PHE   B 2 80  ? 40.70050 -10.11560 -17.18046 1.000 78.25850  ? 173 PHE   B O   1 
ATOM   3065 C CB  . PHE   B 2 80  ? 37.64084 -10.91755 -16.06864 1.000 72.30483  ? 173 PHE   B CB  1 
ATOM   3066 C CG  . PHE   B 2 80  ? 38.40918 -12.20510 -16.00035 1.000 73.59252  ? 173 PHE   B CG  1 
ATOM   3067 C CD1 . PHE   B 2 80  ? 39.01284 -12.60407 -14.82077 1.000 80.88551  ? 173 PHE   B CD1 1 
ATOM   3068 C CD2 . PHE   B 2 80  ? 38.51659 -13.02397 -17.11335 1.000 78.80257  ? 173 PHE   B CD2 1 
ATOM   3069 C CE1 . PHE   B 2 80  ? 39.71669 -13.78991 -14.75403 1.000 87.08151  ? 173 PHE   B CE1 1 
ATOM   3070 C CE2 . PHE   B 2 80  ? 39.22008 -14.21068 -17.05234 1.000 76.05814  ? 173 PHE   B CE2 1 
ATOM   3071 C CZ  . PHE   B 2 80  ? 39.82044 -14.59421 -15.87097 1.000 80.38252  ? 173 PHE   B CZ  1 
ATOM   3072 N N   . ASP   B 2 81  ? 39.02177 -9.84945  -18.65641 1.000 72.98051  ? 174 ASP   B N   1 
ATOM   3073 C CA  . ASP   B 2 81  ? 39.88765 -10.13896 -19.79555 1.000 75.35320  ? 174 ASP   B CA  1 
ATOM   3074 C C   . ASP   B 2 81  ? 40.94166 -9.05593  -19.98946 1.000 82.26063  ? 174 ASP   B C   1 
ATOM   3075 O O   . ASP   B 2 81  ? 42.09401 -9.35910  -20.31927 1.000 90.30470  ? 174 ASP   B O   1 
ATOM   3076 C CB  . ASP   B 2 81  ? 39.05290 -10.30652 -21.06475 1.000 78.34593  ? 174 ASP   B CB  1 
ATOM   3077 C CG  . ASP   B 2 81  ? 38.18572 -11.54843 -21.03191 1.000 90.45371  ? 174 ASP   B CG  1 
ATOM   3078 O OD1 . ASP   B 2 81  ? 38.55530 -12.51573 -20.33334 1.000 94.93660  ? 174 ASP   B OD1 1 
ATOM   3079 O OD2 . ASP   B 2 81  ? 37.13600 -11.55858 -21.70884 1.000 83.77489  ? 174 ASP   B OD2 1 
ATOM   3080 N N   . ARG   B 2 82  ? 40.57263 -7.78838  -19.79283 1.000 68.63362  ? 175 ARG   B N   1 
ATOM   3081 C CA  . ARG   B 2 82  ? 41.54318 -6.71715  -19.99191 1.000 69.11346  ? 175 ARG   B CA  1 
ATOM   3082 C C   . ARG   B 2 82  ? 42.55169 -6.64483  -18.85237 1.000 86.24067  ? 175 ARG   B C   1 
ATOM   3083 O O   . ARG   B 2 82  ? 43.71028 -6.27738  -19.07859 1.000 82.65251  ? 175 ARG   B O   1 
ATOM   3084 C CB  . ARG   B 2 82  ? 40.82819 -5.37686  -20.16421 1.000 71.17038  ? 175 ARG   B CB  1 
ATOM   3085 C CG  . ARG   B 2 82  ? 40.15990 -5.21352  -21.51936 1.000 65.11518  ? 175 ARG   B CG  1 
ATOM   3086 C CD  . ARG   B 2 82  ? 39.73465 -3.77571  -21.78252 1.000 66.26257  ? 175 ARG   B CD  1 
ATOM   3087 N NE  . ARG   B 2 82  ? 38.61497 -3.35817  -20.94721 1.000 72.76631  ? 175 ARG   B NE  1 
ATOM   3088 C CZ  . ARG   B 2 82  ? 38.68384 -2.42837  -20.00397 1.000 59.92685  ? 175 ARG   B CZ  1 
ATOM   3089 N NH1 . ARG   B 2 82  ? 39.81065 -1.78362  -19.74836 1.000 69.88063  ? 175 ARG   B NH1 1 
ATOM   3090 N NH2 . ARG   B 2 82  ? 37.59170 -2.13164  -19.30560 1.000 59.24755  ? 175 ARG   B NH2 1 
ATOM   3091 N N   . TYR   B 2 83  ? 42.14000 -6.99089  -17.63063 1.000 74.91543  ? 176 TYR   B N   1 
ATOM   3092 C CA  . TYR   B 2 83  ? 43.08279 -7.00570  -16.51665 1.000 75.33712  ? 176 TYR   B CA  1 
ATOM   3093 C C   . TYR   B 2 83  ? 44.12160 -8.10659  -16.68967 1.000 82.70627  ? 176 TYR   B C   1 
ATOM   3094 O O   . TYR   B 2 83  ? 45.29736 -7.91664  -16.35705 1.000 89.19721  ? 176 TYR   B O   1 
ATOM   3095 C CB  . TYR   B 2 83  ? 42.33401 -7.17398  -15.19348 1.000 73.48859  ? 176 TYR   B CB  1 
ATOM   3096 C CG  . TYR   B 2 83  ? 43.23552 -7.34383  -13.99054 1.000 79.38396  ? 176 TYR   B CG  1 
ATOM   3097 C CD1 . TYR   B 2 83  ? 43.85340 -6.24877  -13.40091 1.000 81.61419  ? 176 TYR   B CD1 1 
ATOM   3098 C CD2 . TYR   B 2 83  ? 43.46345 -8.59902  -13.44084 1.000 89.69238  ? 176 TYR   B CD2 1 
ATOM   3099 C CE1 . TYR   B 2 83  ? 44.67822 -6.39978  -12.30055 1.000 79.48516  ? 176 TYR   B CE1 1 
ATOM   3100 C CE2 . TYR   B 2 83  ? 44.28600 -8.75949  -12.34110 1.000 79.79914  ? 176 TYR   B CE2 1 
ATOM   3101 C CZ  . TYR   B 2 83  ? 44.89036 -7.65682  -11.77524 1.000 88.22244  ? 176 TYR   B CZ  1 
ATOM   3102 O OH  . TYR   B 2 83  ? 45.71033 -7.81226  -10.68020 1.000 90.25657  ? 176 TYR   B OH  1 
ATOM   3103 N N   . MET   B 2 84  ? 43.70739 -9.26377  -17.21079 1.000 89.59307  ? 177 MET   B N   1 
ATOM   3104 C CA  . MET   B 2 84  ? 44.64858 -10.35750 -17.42354 1.000 84.47519  ? 177 MET   B CA  1 
ATOM   3105 C C   . MET   B 2 84  ? 45.67114 -10.02029 -18.50068 1.000 93.09725  ? 177 MET   B C   1 
ATOM   3106 O O   . MET   B 2 84  ? 46.81978 -10.47089 -18.42511 1.000 88.16648  ? 177 MET   B O   1 
ATOM   3107 C CB  . MET   B 2 84  ? 43.89321 -11.63350 -17.78776 1.000 84.10304  ? 177 MET   B CB  1 
ATOM   3108 C CG  . MET   B 2 84  ? 43.12813 -12.25027 -16.63253 1.000 82.46850  ? 177 MET   B CG  1 
ATOM   3109 S SD  . MET   B 2 84  ? 44.20125 -12.55764 -15.22058 1.000 97.19904  ? 177 MET   B SD  1 
ATOM   3110 C CE  . MET   B 2 84  ? 43.16327 -13.63226 -14.23856 1.000 99.76213  ? 177 MET   B CE  1 
ATOM   3111 N N   . ALA   B 2 85  ? 45.27823 -9.23061  -19.50264 1.000 90.76020  ? 178 ALA   B N   1 
ATOM   3112 C CA  . ALA   B 2 85  ? 46.20241 -8.79432  -20.54187 1.000 82.08043  ? 178 ALA   B CA  1 
ATOM   3113 C C   . ALA   B 2 85  ? 47.30862 -7.89445  -20.00757 1.000 100.05451 ? 178 ALA   B C   1 
ATOM   3114 O O   . ALA   B 2 85  ? 48.30646 -7.68779  -20.70735 1.000 95.99175  ? 178 ALA   B O   1 
ATOM   3115 C CB  . ALA   B 2 85  ? 45.43924 -8.06916  -21.65097 1.000 84.34365  ? 178 ALA   B CB  1 
ATOM   3116 N N   . THR   B 2 86  ? 47.15985 -7.35936  -18.79669 1.000 86.78715  ? 179 THR   B N   1 
ATOM   3117 C CA  . THR   B 2 86  ? 48.17659 -6.52138  -18.17789 1.000 86.04264  ? 179 THR   B CA  1 
ATOM   3118 C C   . THR   B 2 86  ? 48.97793 -7.25506  -17.11217 1.000 91.26973  ? 179 THR   B C   1 
ATOM   3119 O O   . THR   B 2 86  ? 49.92878 -6.68361  -16.56988 1.000 95.83407  ? 179 THR   B O   1 
ATOM   3120 C CB  . THR   B 2 86  ? 47.53472 -5.27314  -17.56050 1.000 89.90298  ? 179 THR   B CB  1 
ATOM   3121 O OG1 . THR   B 2 86  ? 46.68624 -5.65706  -16.47072 1.000 81.68711  ? 179 THR   B OG1 1 
ATOM   3122 C CG2 . THR   B 2 86  ? 46.71026 -4.52644  -18.59836 1.000 86.32845  ? 179 THR   B CG2 1 
ATOM   3123 N N   . GLN   B 2 87  ? 48.61968 -8.49578  -16.79854 1.000 85.40244  ? 180 GLN   B N   1 
ATOM   3124 C CA  . GLN   B 2 87  ? 49.27316 -9.27244  -15.75621 1.000 93.08593  ? 180 GLN   B CA  1 
ATOM   3125 C C   . GLN   B 2 87  ? 49.99925 -10.46784 -16.36051 1.000 93.09874  ? 180 GLN   B C   1 
ATOM   3126 O O   . GLN   B 2 87  ? 49.83774 -10.79963 -17.53784 1.000 104.31947 ? 180 GLN   B O   1 
ATOM   3127 C CB  . GLN   B 2 87  ? 48.25564 -9.74066  -14.70900 1.000 85.83584  ? 180 GLN   B CB  1 
ATOM   3128 C CG  . GLN   B 2 87  ? 47.48826 -8.60968  -14.04609 1.000 95.80205  ? 180 GLN   B CG  1 
ATOM   3129 C CD  . GLN   B 2 87  ? 48.39708 -7.63188  -13.32919 1.000 86.06048  ? 180 GLN   B CD  1 
ATOM   3130 O OE1 . GLN   B 2 87  ? 49.38387 -8.02476  -12.70688 1.000 96.01442  ? 180 GLN   B OE1 1 
ATOM   3131 N NE2 . GLN   B 2 87  ? 48.07147 -6.34767  -13.41852 1.000 89.74440  ? 180 GLN   B NE2 1 
ATOM   3132 N N   . GLU   B 2 88  ? 50.81237 -11.11587 -15.52724 1.000 108.72457 ? 181 GLU   B N   1 
ATOM   3133 C CA  . GLU   B 2 88  ? 51.58704 -12.28189 -15.92674 1.000 116.31200 ? 181 GLU   B CA  1 
ATOM   3134 C C   . GLU   B 2 88  ? 51.59040 -13.29688 -14.79429 1.000 103.83277 ? 181 GLU   B C   1 
ATOM   3135 O O   . GLU   B 2 88  ? 51.73006 -12.92721 -13.62508 1.000 122.93245 ? 181 GLU   B O   1 
ATOM   3136 C CB  . GLU   B 2 88  ? 53.03245 -11.90551 -16.28543 1.000 117.62933 ? 181 GLU   B CB  1 
ATOM   3137 C CG  . GLU   B 2 88  ? 53.16766 -10.95262 -17.46215 1.000 125.25168 ? 181 GLU   B CG  1 
ATOM   3138 C CD  . GLU   B 2 88  ? 54.60332 -10.52991 -17.70537 1.000 133.94648 ? 181 GLU   B CD  1 
ATOM   3139 O OE1 . GLU   B 2 88  ? 55.48994 -10.96064 -16.93812 1.000 136.81284 ? 181 GLU   B OE1 1 
ATOM   3140 O OE2 . GLU   B 2 88  ? 54.84524 -9.76598  -18.66327 1.000 140.91627 ? 181 GLU   B OE2 1 
ATOM   3141 N N   . ASN   B 2 89  ? 51.43266 -14.57373 -15.15301 1.000 103.57310 ? 182 ASN   B N   1 
ATOM   3142 C CA  . ASN   B 2 89  ? 51.51091 -15.68868 -14.21238 1.000 108.29661 ? 182 ASN   B CA  1 
ATOM   3143 C C   . ASN   B 2 89  ? 50.47049 -15.58162 -13.10239 1.000 113.29688 ? 182 ASN   B C   1 
ATOM   3144 O O   . ASN   B 2 89  ? 50.71525 -14.94590 -12.07191 1.000 126.06070 ? 182 ASN   B O   1 
ATOM   3145 C CB  . ASN   B 2 89  ? 52.91580 -15.77951 -13.60880 1.000 102.62577 ? 182 ASN   B CB  1 
ATOM   3146 C CG  . ASN   B 2 89  ? 53.99641 -15.91657 -14.66400 1.000 118.98800 ? 182 ASN   B CG  1 
ATOM   3147 O OD1 . ASN   B 2 89  ? 54.84179 -15.03538 -14.82111 1.000 120.65196 ? 182 ASN   B OD1 1 
ATOM   3148 N ND2 . ASN   B 2 89  ? 53.97583 -17.02692 -15.39203 1.000 107.32940 ? 182 ASN   B ND2 1 
ATOM   3149 N N   . VAL   B 2 90  ? 49.31422 -16.21268 -13.29509 1.000 109.04673 ? 183 VAL   B N   1 
ATOM   3150 C CA  . VAL   B 2 90  ? 48.23528 -16.20552 -12.31480 1.000 112.77201 ? 183 VAL   B CA  1 
ATOM   3151 C C   . VAL   B 2 90  ? 47.85448 -17.64447 -11.99622 1.000 97.19701  ? 183 VAL   B C   1 
ATOM   3152 O O   . VAL   B 2 90  ? 47.71747 -18.47536 -12.90061 1.000 108.26679 ? 183 VAL   B O   1 
ATOM   3153 C CB  . VAL   B 2 90  ? 47.01054 -15.41204 -12.82065 1.000 112.09879 ? 183 VAL   B CB  1 
ATOM   3154 C CG1 . VAL   B 2 90  ? 45.82423 -15.59621 -11.88574 1.000 101.70769 ? 183 VAL   B CG1 1 
ATOM   3155 C CG2 . VAL   B 2 90  ? 47.35488 -13.93850 -12.95059 1.000 92.29163  ? 183 VAL   B CG2 1 
ATOM   3156 N N   . VAL   B 2 91  ? 47.69333 -17.93804 -10.70816 1.000 119.48015 ? 184 VAL   B N   1 
ATOM   3157 C CA  . VAL   B 2 91  ? 47.29455 -19.26281 -10.25637 1.000 122.84625 ? 184 VAL   B CA  1 
ATOM   3158 C C   . VAL   B 2 91  ? 45.77382 -19.36909 -10.31138 1.000 116.47960 ? 184 VAL   B C   1 
ATOM   3159 O O   . VAL   B 2 91  ? 45.05324 -18.36837 -10.27245 1.000 117.77756 ? 184 VAL   B O   1 
ATOM   3160 C CB  . VAL   B 2 91  ? 47.83681 -19.54861 -8.83766  1.000 122.58740 ? 184 VAL   B CB  1 
ATOM   3161 C CG1 . VAL   B 2 91  ? 47.13411 -18.67541 -7.80826  1.000 120.20013 ? 184 VAL   B CG1 1 
ATOM   3162 C CG2 . VAL   B 2 91  ? 47.72095 -21.02948 -8.48574  1.000 119.76481 ? 184 VAL   B CG2 1 
ATOM   3163 N N   . LYS   B 2 92  ? 45.27584 -20.60562 -10.41561 1.000 110.73852 ? 185 LYS   B N   1 
ATOM   3164 C CA  . LYS   B 2 92  ? 43.83699 -20.81531 -10.54737 1.000 119.24052 ? 185 LYS   B CA  1 
ATOM   3165 C C   . LYS   B 2 92  ? 43.08226 -20.41293 -9.28556  1.000 112.69103 ? 185 LYS   B C   1 
ATOM   3166 O O   . LYS   B 2 92  ? 41.91116 -20.02487 -9.36630  1.000 102.90599 ? 185 LYS   B O   1 
ATOM   3167 C CB  . LYS   B 2 92  ? 43.54407 -22.27542 -10.89780 1.000 112.56595 ? 185 LYS   B CB  1 
ATOM   3168 C CG  . LYS   B 2 92  ? 43.93707 -23.27442 -9.82120  1.000 129.04864 ? 185 LYS   B CG  1 
ATOM   3169 C CD  . LYS   B 2 92  ? 43.50665 -24.68305 -10.19740 1.000 134.97353 ? 185 LYS   B CD  1 
ATOM   3170 C CE  . LYS   B 2 92  ? 43.84470 -25.67792 -9.09920  1.000 151.73199 ? 185 LYS   B CE  1 
ATOM   3171 N NZ  . LYS   B 2 92  ? 43.41588 -27.05963 -9.45292  1.000 151.00635 ? 185 LYS   B NZ  1 
ATOM   3172 N N   . THR   B 2 93  ? 43.72447 -20.49510 -8.11749  1.000 105.73719 ? 186 THR   B N   1 
ATOM   3173 C CA  . THR   B 2 93  ? 43.06406 -20.08184 -6.88468  1.000 112.89591 ? 186 THR   B CA  1 
ATOM   3174 C C   . THR   B 2 93  ? 42.86520 -18.57372 -6.81871  1.000 111.80649 ? 186 THR   B C   1 
ATOM   3175 O O   . THR   B 2 93  ? 42.02522 -18.10394 -6.04374  1.000 109.23562 ? 186 THR   B O   1 
ATOM   3176 C CB  . THR   B 2 93  ? 43.86109 -20.55431 -5.66721  1.000 120.42023 ? 186 THR   B CB  1 
ATOM   3177 O OG1 . THR   B 2 93  ? 45.12222 -19.87623 -5.62428  1.000 119.90419 ? 186 THR   B OG1 1 
ATOM   3178 C CG2 . THR   B 2 93  ? 44.10156 -22.05489 -5.74003  1.000 113.29698 ? 186 THR   B CG2 1 
ATOM   3179 N N   . LEU   B 2 94  ? 43.61537 -17.81005 -7.61045  1.000 112.95985 ? 187 LEU   B N   1 
ATOM   3180 C CA  . LEU   B 2 94  ? 43.44631 -16.36687 -7.69220  1.000 106.83645 ? 187 LEU   B CA  1 
ATOM   3181 C C   . LEU   B 2 94  ? 42.36848 -15.95665 -8.68838  1.000 111.01091 ? 187 LEU   B C   1 
ATOM   3182 O O   . LEU   B 2 94  ? 41.95514 -14.79173 -8.68769  1.000 105.85847 ? 187 LEU   B O   1 
ATOM   3183 C CB  . LEU   B 2 94  ? 44.78015 -15.70742 -8.06865  1.000 104.73294 ? 187 LEU   B CB  1 
ATOM   3184 C CG  . LEU   B 2 94  ? 44.92291 -14.19133 -7.91284  1.000 107.88567 ? 187 LEU   B CG  1 
ATOM   3185 C CD1 . LEU   B 2 94  ? 44.72577 -13.77504 -6.46330  1.000 109.26662 ? 187 LEU   B CD1 1 
ATOM   3186 C CD2 . LEU   B 2 94  ? 46.27531 -13.72681 -8.42959  1.000 104.60552 ? 187 LEU   B CD2 1 
ATOM   3187 N N   . LEU   B 2 95  ? 41.89515 -16.88634 -9.52323  1.000 101.03169 ? 188 LEU   B N   1 
ATOM   3188 C CA  . LEU   B 2 95  ? 40.90295 -16.54212 -10.53748 1.000 99.45250  ? 188 LEU   B CA  1 
ATOM   3189 C C   . LEU   B 2 95  ? 39.57739 -16.13037 -9.90887  1.000 88.35604  ? 188 LEU   B C   1 
ATOM   3190 O O   . LEU   B 2 95  ? 38.93723 -15.17814 -10.36972 1.000 91.28727  ? 188 LEU   B O   1 
ATOM   3191 C CB  . LEU   B 2 95  ? 40.69522 -17.71936 -11.49036 1.000 99.75555  ? 188 LEU   B CB  1 
ATOM   3192 C CG  . LEU   B 2 95  ? 41.89864 -18.16152 -12.32411 1.000 101.77334 ? 188 LEU   B CG  1 
ATOM   3193 C CD1 . LEU   B 2 95  ? 41.53535 -19.35134 -13.19963 1.000 99.71311  ? 188 LEU   B CD1 1 
ATOM   3194 C CD2 . LEU   B 2 95  ? 42.41497 -17.01052 -13.16870 1.000 95.00782  ? 188 LEU   B CD2 1 
ATOM   3195 N N   . GLN   B 2 96  ? 39.14694 -16.83518 -8.85918  1.000 91.85884  ? 189 GLN   B N   1 
ATOM   3196 C CA  . GLN   B 2 96  ? 37.85396 -16.53502 -8.25155  1.000 92.76735  ? 189 GLN   B CA  1 
ATOM   3197 C C   . GLN   B 2 96  ? 37.84928 -15.15251 -7.61160  1.000 90.52242  ? 189 GLN   B C   1 
ATOM   3198 O O   . GLN   B 2 96  ? 36.83792 -14.44207 -7.65925  1.000 84.24230  ? 189 GLN   B O   1 
ATOM   3199 C CB  . GLN   B 2 96  ? 37.49452 -17.60480 -7.22098  1.000 86.98270  ? 189 GLN   B CB  1 
ATOM   3200 C CG  . GLN   B 2 96  ? 36.09986 -17.44780 -6.63432  1.000 98.38162  ? 189 GLN   B CG  1 
ATOM   3201 C CD  . GLN   B 2 96  ? 35.78658 -18.49111 -5.58185  1.000 110.76106 ? 189 GLN   B CD  1 
ATOM   3202 O OE1 . GLN   B 2 96  ? 36.68625 -19.13402 -5.04147  1.000 126.81067 ? 189 GLN   B OE1 1 
ATOM   3203 N NE2 . GLN   B 2 96  ? 34.50371 -18.66699 -5.28672  1.000 105.44217 ? 189 GLN   B NE2 1 
ATOM   3204 N N   . LEU   B 2 97  ? 38.97164 -14.75174 -7.00990  1.000 90.62817  ? 190 LEU   B N   1 
ATOM   3205 C CA  . LEU   B 2 97  ? 39.05001 -13.42523 -6.40640  1.000 96.86882  ? 190 LEU   B CA  1 
ATOM   3206 C C   . LEU   B 2 97  ? 38.99431 -12.33192 -7.46618  1.000 91.05370  ? 190 LEU   B C   1 
ATOM   3207 O O   . LEU   B 2 97  ? 38.30056 -11.32352 -7.28971  1.000 86.54171  ? 190 LEU   B O   1 
ATOM   3208 C CB  . LEU   B 2 97  ? 40.32506 -13.30104 -5.57255  1.000 88.08237  ? 190 LEU   B CB  1 
ATOM   3209 C CG  . LEU   B 2 97  ? 40.58303 -11.92941 -4.94576  1.000 79.46907  ? 190 LEU   B CG  1 
ATOM   3210 C CD1 . LEU   B 2 97  ? 39.44260 -11.54018 -4.01673  1.000 93.84443  ? 190 LEU   B CD1 1 
ATOM   3211 C CD2 . LEU   B 2 97  ? 41.91256 -11.91353 -4.20686  1.000 96.34823  ? 190 LEU   B CD2 1 
ATOM   3212 N N   . ILE   B 2 98  ? 39.71693 -12.51371 -8.57323  1.000 77.26297  ? 191 ILE   B N   1 
ATOM   3213 C CA  . ILE   B 2 98  ? 39.69469 -11.52381 -9.64523  1.000 95.69751  ? 191 ILE   B CA  1 
ATOM   3214 C C   . ILE   B 2 98  ? 38.31424 -11.46211 -10.28696 1.000 81.85415  ? 191 ILE   B C   1 
ATOM   3215 O O   . ILE   B 2 98  ? 37.82322 -10.38083 -10.63539 1.000 73.70383  ? 191 ILE   B O   1 
ATOM   3216 C CB  . ILE   B 2 98  ? 40.79066 -11.83796 -10.68024 1.000 88.84147  ? 191 ILE   B CB  1 
ATOM   3217 C CG1 . ILE   B 2 98  ? 42.16921 -11.80653 -10.01819 1.000 87.30823  ? 191 ILE   B CG1 1 
ATOM   3218 C CG2 . ILE   B 2 98  ? 40.73145 -10.85755 -11.84289 1.000 78.31084  ? 191 ILE   B CG2 1 
ATOM   3219 C CD1 . ILE   B 2 98  ? 43.30997 -12.11246 -10.96027 1.000 92.80043  ? 191 ILE   B CD1 1 
ATOM   3220 N N   . GLY   B 2 99  ? 37.66084 -12.61505 -10.43954 1.000 82.90512  ? 192 GLY   B N   1 
ATOM   3221 C CA  . GLY   B 2 99  ? 36.35526 -12.63323 -11.07965 1.000 73.64079  ? 192 GLY   B CA  1 
ATOM   3222 C C   . GLY   B 2 99  ? 35.27929 -11.97234 -10.23809 1.000 81.27644  ? 192 GLY   B C   1 
ATOM   3223 O O   . GLY   B 2 99  ? 34.51396 -11.13881 -10.73138 1.000 73.49909  ? 192 GLY   B O   1 
ATOM   3224 N N   . ILE   B 2 100 ? 35.20543 -12.33327 -8.95420  1.000 74.60469  ? 193 ILE   B N   1 
ATOM   3225 C CA  . ILE   B 2 100 ? 34.15461 -11.78367 -8.10317  1.000 83.96593  ? 193 ILE   B CA  1 
ATOM   3226 C C   . ILE   B 2 100 ? 34.39068 -10.30091 -7.83897  1.000 73.42886  ? 193 ILE   B C   1 
ATOM   3227 O O   . ILE   B 2 100 ? 33.43399 -9.53642  -7.66209  1.000 69.74344  ? 193 ILE   B O   1 
ATOM   3228 C CB  . ILE   B 2 100 ? 34.04271 -12.58912 -6.79317  1.000 85.50602  ? 193 ILE   B CB  1 
ATOM   3229 C CG1 . ILE   B 2 100 ? 32.72004 -12.28100 -6.08884  1.000 76.82396  ? 193 ILE   B CG1 1 
ATOM   3230 C CG2 . ILE   B 2 100 ? 35.21549 -12.29966 -5.86609  1.000 78.66685  ? 193 ILE   B CG2 1 
ATOM   3231 C CD1 . ILE   B 2 100 ? 31.49682 -12.62754 -6.91203  1.000 70.42381  ? 193 ILE   B CD1 1 
ATOM   3232 N N   . SER   B 2 101 ? 35.65262 -9.86248  -7.82229  1.000 76.42033  ? 194 SER   B N   1 
ATOM   3233 C CA  . SER   B 2 101 ? 35.93219 -8.44200  -7.64039  1.000 70.38337  ? 194 SER   B CA  1 
ATOM   3234 C C   . SER   B 2 101 ? 35.59031 -7.65149  -8.89564  1.000 64.74395  ? 194 SER   B C   1 
ATOM   3235 O O   . SER   B 2 101 ? 35.16371 -6.49439  -8.80937  1.000 60.31188  ? 194 SER   B O   1 
ATOM   3236 C CB  . SER   B 2 101 ? 37.39572 -8.23642  -7.25743  1.000 75.21018  ? 194 SER   B CB  1 
ATOM   3237 O OG  . SER   B 2 101 ? 37.71369 -8.95608  -6.07986  1.000 78.81984  ? 194 SER   B OG  1 
ATOM   3238 N N   . SER   B 2 102 ? 35.77813 -8.25621  -10.07147 1.000 67.55930  ? 195 SER   B N   1 
ATOM   3239 C CA  . SER   B 2 102 ? 35.32410 -7.62244  -11.30445 1.000 60.36989  ? 195 SER   B CA  1 
ATOM   3240 C C   . SER   B 2 102 ? 33.81239 -7.43795  -11.29403 1.000 61.35866  ? 195 SER   B C   1 
ATOM   3241 O O   . SER   B 2 102 ? 33.30146 -6.39580  -11.72092 1.000 62.57446  ? 195 SER   B O   1 
ATOM   3242 C CB  . SER   B 2 102 ? 35.75667 -8.45308  -12.51336 1.000 64.10762  ? 195 SER   B CB  1 
ATOM   3243 O OG  . SER   B 2 102 ? 37.16420 -8.60741  -12.55040 1.000 73.00225  ? 195 SER   B OG  1 
ATOM   3244 N N   . LEU   B 2 103 ? 33.08013 -8.44051  -10.80221 1.000 64.28748  ? 196 LEU   B N   1 
ATOM   3245 C CA  . LEU   B 2 103 ? 31.63176 -8.31474  -10.68792 1.000 57.94893  ? 196 LEU   B CA  1 
ATOM   3246 C C   . LEU   B 2 103 ? 31.24075 -7.28805  -9.63329  1.000 56.50875  ? 196 LEU   B C   1 
ATOM   3247 O O   . LEU   B 2 103 ? 30.20524 -6.62625  -9.76796  1.000 59.92815  ? 196 LEU   B O   1 
ATOM   3248 C CB  . LEU   B 2 103 ? 31.01272 -9.67495  -10.36539 1.000 62.25108  ? 196 LEU   B CB  1 
ATOM   3249 C CG  . LEU   B 2 103 ? 29.48532 -9.74886  -10.35467 1.000 66.54050  ? 196 LEU   B CG  1 
ATOM   3250 C CD1 . LEU   B 2 103 ? 28.92297 -9.29243  -11.69036 1.000 70.25042  ? 196 LEU   B CD1 1 
ATOM   3251 C CD2 . LEU   B 2 103 ? 29.02430 -11.15963 -10.02836 1.000 68.53673  ? 196 LEU   B CD2 1 
ATOM   3252 N N   . PHE   B 2 104 ? 32.05152 -7.13833  -8.58401  1.000 62.23363  ? 197 PHE   B N   1 
ATOM   3253 C CA  . PHE   B 2 104 ? 31.76435 -6.13378  -7.56539  1.000 58.74408  ? 197 PHE   B CA  1 
ATOM   3254 C C   . PHE   B 2 104 ? 31.88764 -4.72792  -8.13924  1.000 56.29625  ? 197 PHE   B C   1 
ATOM   3255 O O   . PHE   B 2 104 ? 31.02764 -3.87024  -7.90519  1.000 60.67277  ? 197 PHE   B O   1 
ATOM   3256 C CB  . PHE   B 2 104 ? 32.69868 -6.32250  -6.36960  1.000 62.73563  ? 197 PHE   B CB  1 
ATOM   3257 C CG  . PHE   B 2 104 ? 32.44412 -5.36409  -5.24175  1.000 72.17666  ? 197 PHE   B CG  1 
ATOM   3258 C CD1 . PHE   B 2 104 ? 31.17804 -5.23755  -4.69365  1.000 74.22009  ? 197 PHE   B CD1 1 
ATOM   3259 C CD2 . PHE   B 2 104 ? 33.47536 -4.60216  -4.71745  1.000 73.12317  ? 197 PHE   B CD2 1 
ATOM   3260 C CE1 . PHE   B 2 104 ? 30.94293 -4.35887  -3.65071  1.000 83.30844  ? 197 PHE   B CE1 1 
ATOM   3261 C CE2 . PHE   B 2 104 ? 33.24745 -3.72454  -3.67445  1.000 74.20463  ? 197 PHE   B CE2 1 
ATOM   3262 C CZ  . PHE   B 2 104 ? 31.97966 -3.60236  -3.14062  1.000 67.80421  ? 197 PHE   B CZ  1 
ATOM   3263 N N   . ILE   B 2 105 ? 32.95476 -4.47593  -8.90122  1.000 64.33009  ? 198 ILE   B N   1 
ATOM   3264 C CA  . ILE   B 2 105 ? 33.10302 -3.18900  -9.57513  1.000 55.77707  ? 198 ILE   B CA  1 
ATOM   3265 C C   . ILE   B 2 105 ? 31.96534 -2.97286  -10.56358 1.000 52.01292  ? 198 ILE   B C   1 
ATOM   3266 O O   . ILE   B 2 105 ? 31.40258 -1.87472  -10.65702 1.000 47.58803  ? 198 ILE   B O   1 
ATOM   3267 C CB  . ILE   B 2 105 ? 34.47391 -3.10568  -10.27095 1.000 58.48921  ? 198 ILE   B CB  1 
ATOM   3268 C CG1 . ILE   B 2 105 ? 35.60062 -3.35283  -9.26746  1.000 56.62852  ? 198 ILE   B CG1 1 
ATOM   3269 C CG2 . ILE   B 2 105 ? 34.64729 -1.75410  -10.94912 1.000 59.72044  ? 198 ILE   B CG2 1 
ATOM   3270 C CD1 . ILE   B 2 105 ? 36.95358 -3.54676  -9.91283  1.000 58.60405  ? 198 ILE   B CD1 1 
ATOM   3271 N N   . ALA   B 2 106 ? 31.60513 -4.01781  -11.31275 1.000 56.46250  ? 199 ALA   B N   1 
ATOM   3272 C CA  . ALA   B 2 106 ? 30.55810 -3.88239  -12.31996 1.000 60.07769  ? 199 ALA   B CA  1 
ATOM   3273 C C   . ALA   B 2 106 ? 29.20080 -3.61192  -11.68254 1.000 47.24000  ? 199 ALA   B C   1 
ATOM   3274 O O   . ALA   B 2 106 ? 28.41157 -2.81802  -12.20722 1.000 51.70902  ? 199 ALA   B O   1 
ATOM   3275 C CB  . ALA   B 2 106 ? 30.50186 -5.13825  -13.18893 1.000 58.60607  ? 199 ALA   B CB  1 
ATOM   3276 N N   . ALA   B 2 107 ? 28.91036 -4.26133  -10.55237 1.000 57.05130  ? 200 ALA   B N   1 
ATOM   3277 C CA  . ALA   B 2 107 ? 27.61380 -4.07621  -9.90776  1.000 59.36146  ? 200 ALA   B CA  1 
ATOM   3278 C C   . ALA   B 2 107 ? 27.45354 -2.65656  -9.37931  1.000 50.16625  ? 200 ALA   B C   1 
ATOM   3279 O O   . ALA   B 2 107 ? 26.37573 -2.06163  -9.49573  1.000 56.66070  ? 200 ALA   B O   1 
ATOM   3280 C CB  . ALA   B 2 107 ? 27.43612 -5.09157  -8.77937  1.000 62.01578  ? 200 ALA   B CB  1 
ATOM   3281 N N   . LYS   B 2 108 ? 28.51530 -2.09432  -8.79611  1.000 58.68563  ? 201 LYS   B N   1 
ATOM   3282 C CA  . LYS   B 2 108 ? 28.43321 -0.73167  -8.27975  1.000 51.63514  ? 201 LYS   B CA  1 
ATOM   3283 C C   . LYS   B 2 108 ? 28.29205 0.29166   -9.39914  1.000 60.93330  ? 201 LYS   B C   1 
ATOM   3284 O O   . LYS   B 2 108 ? 27.75415 1.38180   -9.17412  1.000 53.13817  ? 201 LYS   B O   1 
ATOM   3285 C CB  . LYS   B 2 108 ? 29.66004 -0.41406  -7.42341  1.000 58.98013  ? 201 LYS   B CB  1 
ATOM   3286 C CG  . LYS   B 2 108 ? 29.66995 -1.11532  -6.07405  1.000 60.92668  ? 201 LYS   B CG  1 
ATOM   3287 C CD  . LYS   B 2 108 ? 30.81788 -0.63819  -5.19524  1.000 63.49412  ? 201 LYS   B CD  1 
ATOM   3288 C CE  . LYS   B 2 108 ? 32.16768 -1.03784  -5.76868  1.000 67.36557  ? 201 LYS   B CE  1 
ATOM   3289 N NZ  . LYS   B 2 108 ? 33.28816 -0.66371  -4.86074  1.000 62.33155  ? 201 LYS   B NZ  1 
ATOM   3290 N N   . LEU   B 2 109 ? 28.76052 -0.03598  -10.60483 1.000 56.61594  ? 202 LEU   B N   1 
ATOM   3291 C CA  . LEU   B 2 109 ? 28.65755 0.90016   -11.71850 1.000 53.66997  ? 202 LEU   B CA  1 
ATOM   3292 C C   . LEU   B 2 109 ? 27.26790 0.88870   -12.34403 1.000 54.56629  ? 202 LEU   B C   1 
ATOM   3293 O O   . LEU   B 2 109 ? 26.74566 1.94493   -12.71736 1.000 52.47897  ? 202 LEU   B O   1 
ATOM   3294 C CB  . LEU   B 2 109 ? 29.71350 0.57601   -12.77704 1.000 53.90489  ? 202 LEU   B CB  1 
ATOM   3295 C CG  . LEU   B 2 109 ? 31.13780 1.05330   -12.49387 1.000 63.29757  ? 202 LEU   B CG  1 
ATOM   3296 C CD1 . LEU   B 2 109 ? 32.11489 0.43027   -13.47634 1.000 56.48682  ? 202 LEU   B CD1 1 
ATOM   3297 C CD2 . LEU   B 2 109 ? 31.20124 2.56990   -12.56488 1.000 57.29842  ? 202 LEU   B CD2 1 
ATOM   3298 N N   . GLU   B 2 110 ? 26.65061 -0.28621  -12.45601 1.000 55.45739  ? 203 GLU   B N   1 
ATOM   3299 C CA  . GLU   B 2 110 ? 25.43783 -0.45024  -13.24861 1.000 57.52802  ? 203 GLU   B CA  1 
ATOM   3300 C C   . GLU   B 2 110 ? 24.16248 -0.50875  -12.41708 1.000 67.50398  ? 203 GLU   B C   1 
ATOM   3301 O O   . GLU   B 2 110 ? 23.14817 0.07287   -12.81427 1.000 61.63520  ? 203 GLU   B O   1 
ATOM   3302 C CB  . GLU   B 2 110 ? 25.54248 -1.71812  -14.10307 1.000 54.86085  ? 203 GLU   B CB  1 
ATOM   3303 C CG  . GLU   B 2 110 ? 24.44352 -1.85858  -15.14199 1.000 68.26401  ? 203 GLU   B CG  1 
ATOM   3304 C CD  . GLU   B 2 110 ? 24.50772 -0.78180  -16.20899 1.000 67.81614  ? 203 GLU   B CD  1 
ATOM   3305 O OE1 . GLU   B 2 110 ? 25.60665 -0.23574  -16.44502 1.000 74.47674  ? 203 GLU   B OE1 1 
ATOM   3306 O OE2 . GLU   B 2 110 ? 23.45734 -0.47937  -16.81227 1.000 92.63407  ? 203 GLU   B OE2 1 
ATOM   3307 N N   . GLU   B 2 111 ? 24.18017 -1.19564  -11.27776 1.000 56.70291  ? 204 GLU   B N   1 
ATOM   3308 C CA  . GLU   B 2 111 ? 22.96049 -1.41740  -10.51336 1.000 56.22785  ? 204 GLU   B CA  1 
ATOM   3309 C C   . GLU   B 2 111 ? 22.59285 -0.18546  -9.69602  1.000 71.80811  ? 204 GLU   B C   1 
ATOM   3310 O O   . GLU   B 2 111 ? 23.46346 0.51780   -9.17484  1.000 63.82956  ? 204 GLU   B O   1 
ATOM   3311 C CB  . GLU   B 2 111 ? 23.12087 -2.62642  -9.59115  1.000 51.48619  ? 204 GLU   B CB  1 
ATOM   3312 C CG  . GLU   B 2 111 ? 23.56282 -3.90083  -10.29666 1.000 61.84235  ? 204 GLU   B CG  1 
ATOM   3313 C CD  . GLU   B 2 111 ? 22.52318 -4.43585  -11.26638 1.000 76.73107  ? 204 GLU   B CD  1 
ATOM   3314 O OE1 . GLU   B 2 111 ? 21.34286 -4.03703  -11.16731 1.000 71.16597  ? 204 GLU   B OE1 1 
ATOM   3315 O OE2 . GLU   B 2 111 ? 22.88964 -5.25988  -12.13026 1.000 65.44227  ? 204 GLU   B OE2 1 
ATOM   3316 N N   . ILE   B 2 112 ? 21.28757 0.07133   -9.58801  1.000 60.57533  ? 205 ILE   B N   1 
ATOM   3317 C CA  . ILE   B 2 112 ? 20.81296 1.18658   -8.77411  1.000 72.92603  ? 205 ILE   B CA  1 
ATOM   3318 C C   . ILE   B 2 112 ? 21.03413 0.89384   -7.29524  1.000 68.95756  ? 205 ILE   B C   1 
ATOM   3319 O O   . ILE   B 2 112 ? 21.57094 1.72509   -6.55354  1.000 67.74928  ? 205 ILE   B O   1 
ATOM   3320 C CB  . ILE   B 2 112 ? 19.33314 1.48203   -9.07771  1.000 68.40988  ? 205 ILE   B CB  1 
ATOM   3321 C CG1 . ILE   B 2 112 ? 19.16530 1.92570   -10.53279 1.000 60.56307  ? 205 ILE   B CG1 1 
ATOM   3322 C CG2 . ILE   B 2 112 ? 18.79218 2.53777   -8.12537  1.000 62.37178  ? 205 ILE   B CG2 1 
ATOM   3323 C CD1 . ILE   B 2 112 ? 17.74252 2.28825   -10.90092 1.000 63.83715  ? 205 ILE   B CD1 1 
ATOM   3324 N N   . TYR   B 2 113 ? 20.62194 -0.29392  -6.84456  1.000 61.66070  ? 206 TYR   B N   1 
ATOM   3325 C CA  . TYR   B 2 113 ? 20.85206 -0.76669  -5.48093  1.000 69.55456  ? 206 TYR   B CA  1 
ATOM   3326 C C   . TYR   B 2 113 ? 21.68045 -2.04313  -5.56888  1.000 66.17489  ? 206 TYR   B C   1 
ATOM   3327 O O   . TYR   B 2 113 ? 21.13135 -3.15554  -5.54626  1.000 71.08790  ? 206 TYR   B O   1 
ATOM   3328 C CB  . TYR   B 2 113 ? 19.54064 -1.01230  -4.73597  1.000 72.34499  ? 206 TYR   B CB  1 
ATOM   3329 C CG  . TYR   B 2 113 ? 18.64214 0.19987   -4.64065  1.000 75.43668  ? 206 TYR   B CG  1 
ATOM   3330 C CD1 . TYR   B 2 113 ? 18.93457 1.23883   -3.76696  1.000 66.85355  ? 206 TYR   B CD1 1 
ATOM   3331 C CD2 . TYR   B 2 113 ? 17.49398 0.29925   -5.41583  1.000 76.27790  ? 206 TYR   B CD2 1 
ATOM   3332 C CE1 . TYR   B 2 113 ? 18.11328 2.34772   -3.67424  1.000 76.86302  ? 206 TYR   B CE1 1 
ATOM   3333 C CE2 . TYR   B 2 113 ? 16.66605 1.40355   -5.32965  1.000 77.92446  ? 206 TYR   B CE2 1 
ATOM   3334 C CZ  . TYR   B 2 113 ? 16.98042 2.42436   -4.45750  1.000 84.17721  ? 206 TYR   B CZ  1 
ATOM   3335 O OH  . TYR   B 2 113 ? 16.15939 3.52535   -4.36847  1.000 89.28779  ? 206 TYR   B OH  1 
ATOM   3336 N N   . PRO   B 2 114 ? 23.00057 -1.92486  -5.67135  1.000 69.13457  ? 207 PRO   B N   1 
ATOM   3337 C CA  . PRO   B 2 114 ? 23.84644 -3.11174  -5.82124  1.000 60.46869  ? 207 PRO   B CA  1 
ATOM   3338 C C   . PRO   B 2 114 ? 23.92180 -3.89496  -4.52411  1.000 69.62745  ? 207 PRO   B C   1 
ATOM   3339 O O   . PRO   B 2 114 ? 23.63527 -3.35483  -3.44523  1.000 77.71064  ? 207 PRO   B O   1 
ATOM   3340 C CB  . PRO   B 2 114 ? 25.21304 -2.52116  -6.19522  1.000 66.02175  ? 207 PRO   B CB  1 
ATOM   3341 C CG  . PRO   B 2 114 ? 25.20989 -1.17580  -5.55914  1.000 71.20582  ? 207 PRO   B CG  1 
ATOM   3342 C CD  . PRO   B 2 114 ? 23.79023 -0.68075  -5.65671  1.000 71.11608  ? 207 PRO   B CD  1 
ATOM   3343 N N   . PRO   B 2 115 ? 24.29303 -5.17117  -4.58618  1.000 73.38574  ? 208 PRO   B N   1 
ATOM   3344 C CA  . PRO   B 2 115 ? 24.48149 -5.94303  -3.35466  1.000 77.89182  ? 208 PRO   B CA  1 
ATOM   3345 C C   . PRO   B 2 115 ? 25.66408 -5.42113  -2.55384  1.000 85.15329  ? 208 PRO   B C   1 
ATOM   3346 O O   . PRO   B 2 115 ? 26.57869 -4.78262  -3.07975  1.000 63.20156  ? 208 PRO   B O   1 
ATOM   3347 C CB  . PRO   B 2 115 ? 24.73999 -7.36860  -3.85770  1.000 76.31523  ? 208 PRO   B CB  1 
ATOM   3348 C CG  . PRO   B 2 115 ? 24.22545 -7.38613  -5.26384  1.000 73.32002  ? 208 PRO   B CG  1 
ATOM   3349 C CD  . PRO   B 2 115 ? 24.45348 -6.00431  -5.78862  1.000 78.34794  ? 208 PRO   B CD  1 
ATOM   3350 N N   . LYS   B 2 116 ? 25.63267 -5.70655  -1.25504  1.000 80.39442  ? 209 LYS   B N   1 
ATOM   3351 C CA  . LYS   B 2 116 ? 26.69015 -5.26152  -0.36386  1.000 80.24159  ? 209 LYS   B CA  1 
ATOM   3352 C C   . LYS   B 2 116 ? 27.95127 -6.10035  -0.56488  1.000 76.39206  ? 209 LYS   B C   1 
ATOM   3353 O O   . LYS   B 2 116 ? 27.94861 -7.13106  -1.24339  1.000 83.57260  ? 209 LYS   B O   1 
ATOM   3354 C CB  . LYS   B 2 116 ? 26.22706 -5.32465  1.09098   1.000 84.51098  ? 209 LYS   B CB  1 
ATOM   3355 C CG  . LYS   B 2 116 ? 25.14685 -4.31230  1.44022   1.000 81.40660  ? 209 LYS   B CG  1 
ATOM   3356 C CD  . LYS   B 2 116 ? 25.63315 -2.89007  1.20682   1.000 87.82762  ? 209 LYS   B CD  1 
ATOM   3357 C CE  . LYS   B 2 116 ? 24.57839 -1.86614  1.59530   1.000 84.25226  ? 209 LYS   B CE  1 
ATOM   3358 N NZ  . LYS   B 2 116 ? 23.34710 -1.98775  0.76784   1.000 67.08047  ? 209 LYS   B NZ  1 
ATOM   3359 N N   . LEU   B 2 117 ? 29.04565 -5.63841  0.04552   1.000 73.44176  ? 210 LEU   B N   1 
ATOM   3360 C CA  . LEU   B 2 117 ? 30.33154 -6.30918  -0.12037  1.000 73.59652  ? 210 LEU   B CA  1 
ATOM   3361 C C   . LEU   B 2 117 ? 30.30509 -7.72203  0.44910   1.000 85.73216  ? 210 LEU   B C   1 
ATOM   3362 O O   . LEU   B 2 117 ? 30.83064 -8.65634  -0.16804  1.000 92.47904  ? 210 LEU   B O   1 
ATOM   3363 C CB  . LEU   B 2 117 ? 31.43795 -5.48946  0.54300   1.000 79.61864  ? 210 LEU   B CB  1 
ATOM   3364 C CG  . LEU   B 2 117 ? 32.78241 -6.19603  0.73011   1.000 75.84277  ? 210 LEU   B CG  1 
ATOM   3365 C CD1 . LEU   B 2 117 ? 33.44978 -6.46719  -0.61049  1.000 75.42991  ? 210 LEU   B CD1 1 
ATOM   3366 C CD2 . LEU   B 2 117 ? 33.69446 -5.38868  1.64176   1.000 80.90057  ? 210 LEU   B CD2 1 
ATOM   3367 N N   . HIS   B 2 118 ? 29.69860 -7.89991  1.62623   1.000 82.87535  ? 211 HIS   B N   1 
ATOM   3368 C CA  . HIS   B 2 118 ? 29.71391 -9.21046  2.26880   1.000 95.56088  ? 211 HIS   B CA  1 
ATOM   3369 C C   . HIS   B 2 118 ? 28.94677 -10.24784 1.45833   1.000 81.91336  ? 211 HIS   B C   1 
ATOM   3370 O O   . HIS   B 2 118 ? 29.24835 -11.44336 1.54532   1.000 90.58024  ? 211 HIS   B O   1 
ATOM   3371 C CB  . HIS   B 2 118 ? 29.14420 -9.11441  3.68451   1.000 94.18011  ? 211 HIS   B CB  1 
ATOM   3372 C CG  . HIS   B 2 118 ? 27.65729 -8.95241  3.72892   1.000 94.41513  ? 211 HIS   B CG  1 
ATOM   3373 N ND1 . HIS   B 2 118 ? 27.03551 -7.73433  3.55883   1.000 101.34323 ? 211 HIS   B ND1 1 
ATOM   3374 C CD2 . HIS   B 2 118 ? 26.66806 -9.85551  3.92694   1.000 102.64672 ? 211 HIS   B CD2 1 
ATOM   3375 C CE1 . HIS   B 2 118 ? 25.72722 -7.89400  3.64838   1.000 100.89535 ? 211 HIS   B CE1 1 
ATOM   3376 N NE2 . HIS   B 2 118 ? 25.47789 -9.17181  3.87151   1.000 113.72091 ? 211 HIS   B NE2 1 
ATOM   3377 N N   . GLN   B 2 119 ? 27.95985 -9.81833  0.66797   1.000 88.97579  ? 212 GLN   B N   1 
ATOM   3378 C CA  . GLN   B 2 119 ? 27.24597 -10.76109 -0.18783  1.000 99.77380  ? 212 GLN   B CA  1 
ATOM   3379 C C   . GLN   B 2 119 ? 28.14840 -11.28933 -1.29618  1.000 84.20492  ? 212 GLN   B C   1 
ATOM   3380 O O   . GLN   B 2 119 ? 28.06962 -12.46896 -1.65891  1.000 89.96763  ? 212 GLN   B O   1 
ATOM   3381 C CB  . GLN   B 2 119 ? 25.99777 -10.10216 -0.77434  1.000 84.02920  ? 212 GLN   B CB  1 
ATOM   3382 C CG  . GLN   B 2 119 ? 24.93215 -9.76760  0.25746   1.000 97.35781  ? 212 GLN   B CG  1 
ATOM   3383 C CD  . GLN   B 2 119 ? 23.72898 -9.07033  -0.34864  1.000 92.55472  ? 212 GLN   B CD  1 
ATOM   3384 O OE1 . GLN   B 2 119 ? 23.79365 -7.89424  -0.70763  1.000 92.58589  ? 212 GLN   B OE1 1 
ATOM   3385 N NE2 . GLN   B 2 119 ? 22.62176 -9.79476  -0.46538  1.000 100.16322 ? 212 GLN   B NE2 1 
ATOM   3386 N N   . PHE   B 2 120 ? 29.01332 -10.43193 -1.84533  1.000 87.99637  ? 213 PHE   B N   1 
ATOM   3387 C CA  . PHE   B 2 120 ? 29.98634 -10.89520 -2.82890  1.000 86.46375  ? 213 PHE   B CA  1 
ATOM   3388 C C   . PHE   B 2 120 ? 31.00669 -11.83628 -2.20235  1.000 82.00305  ? 213 PHE   B C   1 
ATOM   3389 O O   . PHE   B 2 120 ? 31.47922 -12.76699 -2.86368  1.000 77.74127  ? 213 PHE   B O   1 
ATOM   3390 C CB  . PHE   B 2 120 ? 30.68726 -9.70308  -3.48052  1.000 87.23741  ? 213 PHE   B CB  1 
ATOM   3391 C CG  . PHE   B 2 120 ? 29.84691 -8.99119  -4.50298  1.000 76.54144  ? 213 PHE   B CG  1 
ATOM   3392 C CD1 . PHE   B 2 120 ? 28.93783 -8.01962  -4.11942  1.000 79.16178  ? 213 PHE   B CD1 1 
ATOM   3393 C CD2 . PHE   B 2 120 ? 29.96742 -9.29453  -5.84923  1.000 76.90439  ? 213 PHE   B CD2 1 
ATOM   3394 C CE1 . PHE   B 2 120 ? 28.16358 -7.36464  -5.05885  1.000 82.57276  ? 213 PHE   B CE1 1 
ATOM   3395 C CE2 . PHE   B 2 120 ? 29.19718 -8.64369  -6.79332  1.000 75.35655  ? 213 PHE   B CE2 1 
ATOM   3396 C CZ  . PHE   B 2 120 ? 28.29371 -7.67720  -6.39783  1.000 73.15572  ? 213 PHE   B CZ  1 
ATOM   3397 N N   . ALA   B 2 121 ? 31.35834 -11.61181 -0.93552  1.000 87.88803  ? 214 ALA   B N   1 
ATOM   3398 C CA  . ALA   B 2 121 ? 32.22252 -12.54383 -0.22228  1.000 89.84624  ? 214 ALA   B CA  1 
ATOM   3399 C C   . ALA   B 2 121 ? 31.47072 -13.79635 0.20757   1.000 89.12374  ? 214 ALA   B C   1 
ATOM   3400 O O   . ALA   B 2 121 ? 32.08516 -14.85534 0.37782   1.000 97.65781  ? 214 ALA   B O   1 
ATOM   3401 C CB  . ALA   B 2 121 ? 32.84121 -11.86050 0.99834   1.000 80.69283  ? 214 ALA   B CB  1 
ATOM   3402 N N   . TYR   B 2 122 ? 30.15034 -13.69549 0.38223   1.000 82.75587  ? 215 TYR   B N   1 
ATOM   3403 C CA  . TYR   B 2 122 ? 29.36598 -14.83979 0.83558   1.000 80.42922  ? 215 TYR   B CA  1 
ATOM   3404 C C   . TYR   B 2 122 ? 29.28046 -15.91912 -0.23676  1.000 92.28781  ? 215 TYR   B C   1 
ATOM   3405 O O   . TYR   B 2 122 ? 29.34913 -17.11436 0.07242   1.000 89.54791  ? 215 TYR   B O   1 
ATOM   3406 C CB  . TYR   B 2 122 ? 27.96879 -14.37695 1.25048   1.000 84.24381  ? 215 TYR   B CB  1 
ATOM   3407 C CG  . TYR   B 2 122 ? 26.97532 -15.49732 1.46264   1.000 90.43518  ? 215 TYR   B CG  1 
ATOM   3408 C CD1 . TYR   B 2 122 ? 26.97563 -16.24010 2.63558   1.000 98.42874  ? 215 TYR   B CD1 1 
ATOM   3409 C CD2 . TYR   B 2 122 ? 26.02850 -15.80389 0.49352   1.000 95.14180  ? 215 TYR   B CD2 1 
ATOM   3410 C CE1 . TYR   B 2 122 ? 26.06641 -17.26268 2.83425   1.000 85.49887  ? 215 TYR   B CE1 1 
ATOM   3411 C CE2 . TYR   B 2 122 ? 25.11560 -16.82414 0.68240   1.000 104.94150 ? 215 TYR   B CE2 1 
ATOM   3412 C CZ  . TYR   B 2 122 ? 25.13858 -17.54989 1.85469   1.000 96.59887  ? 215 TYR   B CZ  1 
ATOM   3413 O OH  . TYR   B 2 122 ? 24.23093 -18.56598 2.04695   1.000 94.01813  ? 215 TYR   B OH  1 
ATOM   3414 N N   . VAL   B 2 123 ? 29.13569 -15.52051 -1.50354  1.000 88.02939  ? 216 VAL   B N   1 
ATOM   3415 C CA  . VAL   B 2 123 ? 28.97943 -16.48911 -2.58328  1.000 81.87836  ? 216 VAL   B CA  1 
ATOM   3416 C C   . VAL   B 2 123 ? 30.26727 -17.22510 -2.91402  1.000 95.51403  ? 216 VAL   B C   1 
ATOM   3417 O O   . VAL   B 2 123 ? 30.22678 -18.22777 -3.63590  1.000 104.08986 ? 216 VAL   B O   1 
ATOM   3418 C CB  . VAL   B 2 123 ? 28.44045 -15.80411 -3.85545  1.000 95.46895  ? 216 VAL   B CB  1 
ATOM   3419 C CG1 . VAL   B 2 123 ? 27.10605 -15.13630 -3.57027  1.000 94.69200  ? 216 VAL   B CG1 1 
ATOM   3420 C CG2 . VAL   B 2 123 ? 29.44805 -14.79678 -4.38537  1.000 83.72083  ? 216 VAL   B CG2 1 
ATOM   3421 N N   . THR   B 2 124 ? 31.40727 -16.75948 -2.40749  1.000 88.34289  ? 217 THR   B N   1 
ATOM   3422 C CA  . THR   B 2 124 ? 32.68579 -17.40854 -2.66795  1.000 96.44875  ? 217 THR   B CA  1 
ATOM   3423 C C   . THR   B 2 124 ? 32.95984 -18.58178 -1.73557  1.000 107.29657 ? 217 THR   B C   1 
ATOM   3424 O O   . THR   B 2 124 ? 34.04494 -19.16882 -1.81579  1.000 94.98792  ? 217 THR   B O   1 
ATOM   3425 C CB  . THR   B 2 124 ? 33.82637 -16.39249 -2.55579  1.000 101.30221 ? 217 THR   B CB  1 
ATOM   3426 O OG1 . THR   B 2 124 ? 33.86335 -15.85753 -1.22666  1.000 102.54921 ? 217 THR   B OG1 1 
ATOM   3427 C CG2 . THR   B 2 124 ? 33.62765 -15.25693 -3.54862  1.000 86.36462  ? 217 THR   B CG2 1 
ATOM   3428 N N   . ASP   B 2 125 ? 32.00950 -18.93321 -0.86515  1.000 112.36528 ? 218 ASP   B N   1 
ATOM   3429 C CA  . ASP   B 2 125 ? 32.17054 -20.02721 0.09609   1.000 122.54227 ? 218 ASP   B CA  1 
ATOM   3430 C C   . ASP   B 2 125 ? 33.39814 -19.80715 0.97794   1.000 119.17893 ? 218 ASP   B C   1 
ATOM   3431 O O   . ASP   B 2 125 ? 34.17426 -20.72858 1.24014   1.000 130.89182 ? 218 ASP   B O   1 
ATOM   3432 C CB  . ASP   B 2 125 ? 32.23840 -21.38441 -0.61088  1.000 128.76418 ? 218 ASP   B CB  1 
ATOM   3433 C CG  . ASP   B 2 125 ? 31.84005 -22.53899 0.29413   1.000 131.83295 ? 218 ASP   B CG  1 
ATOM   3434 O OD1 . ASP   B 2 125 ? 31.95630 -22.40431 1.53041   1.000 141.70808 ? 218 ASP   B OD1 1 
ATOM   3435 O OD2 . ASP   B 2 125 ? 31.40828 -23.58549 -0.23401  1.000 136.37594 ? 218 ASP   B OD2 1 
ATOM   3436 N N   . GLY   B 2 126 ? 33.57825 -18.56934 1.43340   1.000 105.49410 ? 219 GLY   B N   1 
ATOM   3437 C CA  . GLY   B 2 126 ? 34.68563 -18.22514 2.29770   1.000 120.69576 ? 219 GLY   B CA  1 
ATOM   3438 C C   . GLY   B 2 126 ? 36.04208 -18.16188 1.63334   1.000 122.13023 ? 219 GLY   B C   1 
ATOM   3439 O O   . GLY   B 2 126 ? 37.02491 -17.83996 2.31060   1.000 126.04617 ? 219 GLY   B O   1 
ATOM   3440 N N   . ALA   B 2 127 ? 36.13884 -18.45552 0.33480   1.000 110.30616 ? 220 ALA   B N   1 
ATOM   3441 C CA  . ALA   B 2 127 ? 37.43519 -18.41116 -0.33054  1.000 102.82657 ? 220 ALA   B CA  1 
ATOM   3442 C C   . ALA   B 2 127 ? 37.90745 -16.98527 -0.58041  1.000 108.19240 ? 220 ALA   B C   1 
ATOM   3443 O O   . ALA   B 2 127 ? 39.08847 -16.77966 -0.87883  1.000 114.18211 ? 220 ALA   B O   1 
ATOM   3444 C CB  . ALA   B 2 127 ? 37.37912 -19.18520 -1.64890  1.000 111.61115 ? 220 ALA   B CB  1 
ATOM   3445 N N   . CYS   B 2 128 ? 37.01645 -16.00268 -0.46508  1.000 100.31559 ? 221 CYS   B N   1 
ATOM   3446 C CA  . CYS   B 2 128 ? 37.35512 -14.60062 -0.67999  1.000 108.12549 ? 221 CYS   B CA  1 
ATOM   3447 C C   . CYS   B 2 128 ? 36.71443 -13.77677 0.42483   1.000 107.24734 ? 221 CYS   B C   1 
ATOM   3448 O O   . CYS   B 2 128 ? 35.48610 -13.75690 0.55246   1.000 109.21515 ? 221 CYS   B O   1 
ATOM   3449 C CB  . CYS   B 2 128 ? 36.88263 -14.11853 -2.05602  1.000 98.52385  ? 221 CYS   B CB  1 
ATOM   3450 S SG  . CYS   B 2 128 ? 37.59752 -15.02706 -3.44444  1.000 97.50205  ? 221 CYS   B SG  1 
ATOM   3451 N N   . SER   B 2 129 ? 37.54233 -13.10908 1.22361   1.000 90.87656  ? 222 SER   B N   1 
ATOM   3452 C CA  . SER   B 2 129 ? 37.03873 -12.25766 2.28742   1.000 97.83429  ? 222 SER   B CA  1 
ATOM   3453 C C   . SER   B 2 129 ? 36.65776 -10.88696 1.73392   1.000 93.41812  ? 222 SER   B C   1 
ATOM   3454 O O   . SER   B 2 129 ? 36.92730 -10.55415 0.57689   1.000 97.07443  ? 222 SER   B O   1 
ATOM   3455 C CB  . SER   B 2 129 ? 38.07762 -12.11049 3.39751   1.000 101.40103 ? 222 SER   B CB  1 
ATOM   3456 O OG  . SER   B 2 129 ? 39.20262 -11.37737 2.94565   1.000 91.98651  ? 222 SER   B OG  1 
ATOM   3457 N N   . GLY   B 2 130 ? 36.01567 -10.08410 2.58410   1.000 90.41259  ? 223 GLY   B N   1 
ATOM   3458 C CA  . GLY   B 2 130 ? 35.63977 -8.74195  2.17210   1.000 75.52784  ? 223 GLY   B CA  1 
ATOM   3459 C C   . GLY   B 2 130 ? 36.84142 -7.85515  1.90943   1.000 92.84877  ? 223 GLY   B C   1 
ATOM   3460 O O   . GLY   B 2 130 ? 36.86397 -7.09536  0.93787   1.000 81.35445  ? 223 GLY   B O   1 
ATOM   3461 N N   . ASP   B 2 131 ? 37.86006 -7.94299  2.76936   1.000 88.59124  ? 224 ASP   B N   1 
ATOM   3462 C CA  . ASP   B 2 131 ? 39.06404 -7.14216  2.57367   1.000 97.33252  ? 224 ASP   B CA  1 
ATOM   3463 C C   . ASP   B 2 131 ? 39.84932 -7.59440  1.34942   1.000 85.55992  ? 224 ASP   B C   1 
ATOM   3464 O O   . ASP   B 2 131 ? 40.50969 -6.77340  0.70235   1.000 91.37746  ? 224 ASP   B O   1 
ATOM   3465 C CB  . ASP   B 2 131 ? 39.94515 -7.19963  3.82218   1.000 103.23201 ? 224 ASP   B CB  1 
ATOM   3466 C CG  . ASP   B 2 131 ? 39.31728 -6.49855  5.01121   1.000 113.55329 ? 224 ASP   B CG  1 
ATOM   3467 O OD1 . ASP   B 2 131 ? 38.53305 -5.55005  4.79721   1.000 122.22540 ? 224 ASP   B OD1 1 
ATOM   3468 O OD2 . ASP   B 2 131 ? 39.60978 -6.89341  6.15969   1.000 132.57652 ? 224 ASP   B OD2 1 
ATOM   3469 N N   . GLU   B 2 132 ? 39.79723 -8.88759  1.01974   1.000 88.17924  ? 225 GLU   B N   1 
ATOM   3470 C CA  . GLU   B 2 132 ? 40.45021 -9.36377  -0.19552  1.000 87.71160  ? 225 GLU   B CA  1 
ATOM   3471 C C   . GLU   B 2 132 ? 39.78516 -8.78769  -1.43905  1.000 77.46990  ? 225 GLU   B C   1 
ATOM   3472 O O   . GLU   B 2 132 ? 40.46697 -8.44070  -2.41061  1.000 78.05291  ? 225 GLU   B O   1 
ATOM   3473 C CB  . GLU   B 2 132 ? 40.43480 -10.89198 -0.24044  1.000 92.54151  ? 225 GLU   B CB  1 
ATOM   3474 C CG  . GLU   B 2 132 ? 41.46609 -11.56082 0.65408   1.000 102.87478 ? 225 GLU   B CG  1 
ATOM   3475 C CD  . GLU   B 2 132 ? 41.36005 -13.07488 0.63210   1.000 114.48376 ? 225 GLU   B CD  1 
ATOM   3476 O OE1 . GLU   B 2 132 ? 40.22762 -13.59189 0.53215   1.000 112.96976 ? 225 GLU   B OE1 1 
ATOM   3477 O OE2 . GLU   B 2 132 ? 42.40898 -13.74862 0.70861   1.000 120.89593 ? 225 GLU   B OE2 1 
ATOM   3478 N N   . ILE   B 2 133 ? 38.45545 -8.67711  -1.42660  1.000 72.60133  ? 226 ILE   B N   1 
ATOM   3479 C CA  . ILE   B 2 133 ? 37.74617 -8.12159  -2.57434  1.000 76.45717  ? 226 ILE   B CA  1 
ATOM   3480 C C   . ILE   B 2 133 ? 38.06643 -6.64025  -2.73383  1.000 82.37988  ? 226 ILE   B C   1 
ATOM   3481 O O   . ILE   B 2 133 ? 38.28747 -6.15587  -3.85049  1.000 75.62471  ? 226 ILE   B O   1 
ATOM   3482 C CB  . ILE   B 2 133 ? 36.23257 -8.36771  -2.43332  1.000 71.69076  ? 226 ILE   B CB  1 
ATOM   3483 C CG1 . ILE   B 2 133 ? 35.93318 -9.86905  -2.43469  1.000 79.86543  ? 226 ILE   B CG1 1 
ATOM   3484 C CG2 . ILE   B 2 133 ? 35.46831 -7.67108  -3.54839  1.000 67.58843  ? 226 ILE   B CG2 1 
ATOM   3485 C CD1 . ILE   B 2 133 ? 34.46871 -10.20099 -2.24373  1.000 81.14879  ? 226 ILE   B CD1 1 
ATOM   3486 N N   . LEU   B 2 134 ? 38.10622 -5.89911  -1.62238  1.000 79.08609  ? 227 LEU   B N   1 
ATOM   3487 C CA  . LEU   B 2 134 ? 38.43248 -4.47825  -1.69039  1.000 70.65731  ? 227 LEU   B CA  1 
ATOM   3488 C C   . LEU   B 2 134 ? 39.86925 -4.25222  -2.14177  1.000 73.20321  ? 227 LEU   B C   1 
ATOM   3489 O O   . LEU   B 2 134 ? 40.15369 -3.26207  -2.82563  1.000 79.63660  ? 227 LEU   B O   1 
ATOM   3490 C CB  . LEU   B 2 134 ? 38.19161 -3.81642  -0.33428  1.000 78.72739  ? 227 LEU   B CB  1 
ATOM   3491 C CG  . LEU   B 2 134 ? 36.76384 -3.91819  0.20644   1.000 83.91992  ? 227 LEU   B CG  1 
ATOM   3492 C CD1 . LEU   B 2 134 ? 36.59242 -3.04399  1.44117   1.000 88.32175  ? 227 LEU   B CD1 1 
ATOM   3493 C CD2 . LEU   B 2 134 ? 35.75514 -3.54981  -0.87005  1.000 68.17370  ? 227 LEU   B CD2 1 
ATOM   3494 N N   . THR   B 2 135 ? 40.78601 -5.14828  -1.76886  1.000 73.29941  ? 228 THR   B N   1 
ATOM   3495 C CA  . THR   B 2 135 ? 42.15112 -5.05290  -2.27527  1.000 75.57348  ? 228 THR   B CA  1 
ATOM   3496 C C   . THR   B 2 135 ? 42.20240 -5.36414  -3.76547  1.000 80.04952  ? 228 THR   B C   1 
ATOM   3497 O O   . THR   B 2 135 ? 42.92468 -4.70336  -4.52167  1.000 83.35336  ? 228 THR   B O   1 
ATOM   3498 C CB  . THR   B 2 135 ? 43.07034 -5.99891  -1.50092  1.000 84.01400  ? 228 THR   B CB  1 
ATOM   3499 O OG1 . THR   B 2 135 ? 43.07336 -5.63884  -0.11409  1.000 91.69388  ? 228 THR   B OG1 1 
ATOM   3500 C CG2 . THR   B 2 135 ? 44.49312 -5.92993  -2.04230  1.000 77.90442  ? 228 THR   B CG2 1 
ATOM   3501 N N   . MET   B 2 136 ? 41.42253 -6.35256  -4.20800  1.000 82.49295  ? 229 MET   B N   1 
ATOM   3502 C CA  . MET   B 2 136 ? 41.46984 -6.76606  -5.60552  1.000 69.59024  ? 229 MET   B CA  1 
ATOM   3503 C C   . MET   B 2 136 ? 40.82583 -5.72775  -6.51548  1.000 70.45114  ? 229 MET   B C   1 
ATOM   3504 O O   . MET   B 2 136 ? 41.30641 -5.49323  -7.63012  1.000 73.35705  ? 229 MET   B O   1 
ATOM   3505 C CB  . MET   B 2 136 ? 40.78922 -8.12442  -5.76915  1.000 74.74903  ? 229 MET   B CB  1 
ATOM   3506 C CG  . MET   B 2 136 ? 40.96779 -8.76545  -7.13933  1.000 76.72720  ? 229 MET   B CG  1 
ATOM   3507 S SD  . MET   B 2 136 ? 42.65485 -9.31940  -7.45208  1.000 102.29003 ? 229 MET   B SD  1 
ATOM   3508 C CE  . MET   B 2 136 ? 43.23520 -8.04783  -8.56947  1.000 69.70829  ? 229 MET   B CE  1 
ATOM   3509 N N   . GLU   B 2 137 ? 39.74083 -5.09143  -6.06113  1.000 66.26213  ? 230 GLU   B N   1 
ATOM   3510 C CA  . GLU   B 2 137 ? 39.06568 -4.11202  -6.90740  1.000 64.31141  ? 230 GLU   B CA  1 
ATOM   3511 C C   . GLU   B 2 137 ? 39.94946 -2.90188  -7.18229  1.000 70.84350  ? 230 GLU   B C   1 
ATOM   3512 O O   . GLU   B 2 137 ? 39.86697 -2.31192  -8.26510  1.000 64.43819  ? 230 GLU   B O   1 
ATOM   3513 C CB  . GLU   B 2 137 ? 37.74276 -3.67189  -6.27524  1.000 65.11960  ? 230 GLU   B CB  1 
ATOM   3514 C CG  . GLU   B 2 137 ? 37.88513 -2.82574  -5.02010  1.000 75.57587  ? 230 GLU   B CG  1 
ATOM   3515 C CD  . GLU   B 2 137 ? 36.68508 -1.92991  -4.78160  1.000 77.11720  ? 230 GLU   B CD  1 
ATOM   3516 O OE1 . GLU   B 2 137 ? 35.78213 -1.90112  -5.64436  1.000 69.11178  ? 230 GLU   B OE1 1 
ATOM   3517 O OE2 . GLU   B 2 137 ? 36.64611 -1.25066  -3.73404  1.000 83.36870  ? 230 GLU   B OE2 1 
ATOM   3518 N N   . LEU   B 2 138 ? 40.80200 -2.52132  -6.22796  1.000 67.91158  ? 231 LEU   B N   1 
ATOM   3519 C CA  . LEU   B 2 138 ? 41.71183 -1.40571  -6.46359  1.000 75.38074  ? 231 LEU   B CA  1 
ATOM   3520 C C   . LEU   B 2 138 ? 42.81145 -1.79084  -7.44414  1.000 71.39043  ? 231 LEU   B C   1 
ATOM   3521 O O   . LEU   B 2 138 ? 43.19212 -0.98887  -8.30470  1.000 70.23966  ? 231 LEU   B O   1 
ATOM   3522 C CB  . LEU   B 2 138 ? 42.30865 -0.92515  -5.14181  1.000 73.82250  ? 231 LEU   B CB  1 
ATOM   3523 C CG  . LEU   B 2 138 ? 41.42601 0.01476   -4.32006  1.000 81.36636  ? 231 LEU   B CG  1 
ATOM   3524 C CD1 . LEU   B 2 138 ? 42.00410 0.22636   -2.93069  1.000 77.24748  ? 231 LEU   B CD1 1 
ATOM   3525 C CD2 . LEU   B 2 138 ? 41.26690 1.34376   -5.04112  1.000 72.45941  ? 231 LEU   B CD2 1 
ATOM   3526 N N   . MET   B 2 139 ? 43.33142 -3.01486  -7.33305  1.000 72.07479  ? 232 MET   B N   1 
ATOM   3527 C CA  . MET   B 2 139 ? 44.35383 -3.46557  -8.27068  1.000 72.46443  ? 232 MET   B CA  1 
ATOM   3528 C C   . MET   B 2 139 ? 43.78725 -3.61018  -9.67745  1.000 64.69501  ? 232 MET   B C   1 
ATOM   3529 O O   . MET   B 2 139 ? 44.47895 -3.32498  -10.66151 1.000 68.83812  ? 232 MET   B O   1 
ATOM   3530 C CB  . MET   B 2 139 ? 44.96151 -4.78408  -7.79316  1.000 72.93578  ? 232 MET   B CB  1 
ATOM   3531 C CG  . MET   B 2 139 ? 45.78985 -4.65533  -6.52396  1.000 75.29146  ? 232 MET   B CG  1 
ATOM   3532 S SD  . MET   B 2 139 ? 46.56250 -6.20618  -6.03035  1.000 129.38542 ? 232 MET   B SD  1 
ATOM   3533 C CE  . MET   B 2 139 ? 45.12557 -7.17529  -5.58565  1.000 72.54244  ? 232 MET   B CE  1 
ATOM   3534 N N   . ILE   B 2 140 ? 42.52997 -4.04285  -9.79333  1.000 75.48524  ? 233 ILE   B N   1 
ATOM   3535 C CA  . ILE   B 2 140 ? 41.90492 -4.16794  -11.10706 1.000 60.48694  ? 233 ILE   B CA  1 
ATOM   3536 C C   . ILE   B 2 140 ? 41.71840 -2.79505  -11.74073 1.000 65.33512  ? 233 ILE   B C   1 
ATOM   3537 O O   . ILE   B 2 140 ? 42.08590 -2.57322  -12.90004 1.000 68.31977  ? 233 ILE   B O   1 
ATOM   3538 C CB  . ILE   B 2 140 ? 40.56708 -4.92182  -10.99930 1.000 67.87084  ? 233 ILE   B CB  1 
ATOM   3539 C CG1 . ILE   B 2 140 ? 40.80206 -6.38880  -10.63932 1.000 70.64635  ? 233 ILE   B CG1 1 
ATOM   3540 C CG2 . ILE   B 2 140 ? 39.78647 -4.81334  -12.30367 1.000 66.91781  ? 233 ILE   B CG2 1 
ATOM   3541 C CD1 . ILE   B 2 140 ? 39.52616 -7.19152  -10.48880 1.000 73.96158  ? 233 ILE   B CD1 1 
ATOM   3542 N N   . MET   B 2 141 ? 41.15393 -1.84956  -10.98572 1.000 69.62815  ? 234 MET   B N   1 
ATOM   3543 C CA  . MET   B 2 141 ? 40.84455 -0.54012  -11.55195 1.000 68.54181  ? 234 MET   B CA  1 
ATOM   3544 C C   . MET   B 2 141 ? 42.11046 0.24421   -11.87610 1.000 68.98876  ? 234 MET   B C   1 
ATOM   3545 O O   . MET   B 2 141 ? 42.15495 0.97135   -12.87541 1.000 67.26901  ? 234 MET   B O   1 
ATOM   3546 C CB  . MET   B 2 141 ? 39.94885 0.24653   -10.59479 1.000 59.54374  ? 234 MET   B CB  1 
ATOM   3547 C CG  . MET   B 2 141 ? 38.55595 -0.34299  -10.44072 1.000 63.44421  ? 234 MET   B CG  1 
ATOM   3548 S SD  . MET   B 2 141 ? 37.45720 0.64920   -9.41001  1.000 71.12311  ? 234 MET   B SD  1 
ATOM   3549 C CE  . MET   B 2 141 ? 38.30450 0.56999   -7.83505  1.000 58.51538  ? 234 MET   B CE  1 
ATOM   3550 N N   . LYS   B 2 142 ? 43.15005 0.11106   -11.04883 1.000 60.19493  ? 235 LYS   B N   1 
ATOM   3551 C CA  . LYS   B 2 142 ? 44.39711 0.81880   -11.32307 1.000 67.58195  ? 235 LYS   B CA  1 
ATOM   3552 C C   . LYS   B 2 142 ? 45.12291 0.22093   -12.52245 1.000 69.41000  ? 235 LYS   B C   1 
ATOM   3553 O O   . LYS   B 2 142 ? 45.70161 0.95477   -13.33223 1.000 75.62507  ? 235 LYS   B O   1 
ATOM   3554 C CB  . LYS   B 2 142 ? 45.29796 0.80487   -10.08808 1.000 65.86793  ? 235 LYS   B CB  1 
ATOM   3555 C CG  . LYS   B 2 142 ? 44.80819 1.68920   -8.95225  1.000 68.48762  ? 235 LYS   B CG  1 
ATOM   3556 C CD  . LYS   B 2 142 ? 45.82336 1.75571   -7.82088  1.000 72.46648  ? 235 LYS   B CD  1 
ATOM   3557 C CE  . LYS   B 2 142 ? 46.09519 0.38150   -7.23007  1.000 74.61691  ? 235 LYS   B CE  1 
ATOM   3558 N NZ  . LYS   B 2 142 ? 47.07543 0.44697   -6.10858  1.000 72.48790  ? 235 LYS   B NZ  1 
ATOM   3559 N N   . ALA   B 2 143 ? 45.10616 -1.10792  -12.65454 1.000 66.16249  ? 236 ALA   B N   1 
ATOM   3560 C CA  . ALA   B 2 143 ? 45.76422 -1.73942  -13.79386 1.000 72.41891  ? 236 ALA   B CA  1 
ATOM   3561 C C   . ALA   B 2 143 ? 45.04776 -1.42794  -15.10107 1.000 74.14431  ? 236 ALA   B C   1 
ATOM   3562 O O   . ALA   B 2 143 ? 45.68803 -1.36131  -16.15637 1.000 79.19149  ? 236 ALA   B O   1 
ATOM   3563 C CB  . ALA   B 2 143 ? 45.85216 -3.25053  -13.58466 1.000 74.28726  ? 236 ALA   B CB  1 
ATOM   3564 N N   . LEU   B 2 144 ? 43.73204 -1.23338  -15.05450 1.000 73.26147  ? 237 LEU   B N   1 
ATOM   3565 C CA  . LEU   B 2 144 ? 42.95617 -0.87852  -16.23500 1.000 67.82420  ? 237 LEU   B CA  1 
ATOM   3566 C C   . LEU   B 2 144 ? 42.96929 0.61669   -16.52571 1.000 67.57318  ? 237 LEU   B C   1 
ATOM   3567 O O   . LEU   B 2 144 ? 42.20064 1.06707   -17.38284 1.000 75.69136  ? 237 LEU   B O   1 
ATOM   3568 C CB  . LEU   B 2 144 ? 41.51111 -1.36098  -16.07972 1.000 64.91789  ? 237 LEU   B CB  1 
ATOM   3569 C CG  . LEU   B 2 144 ? 41.31209 -2.87566  -16.01154 1.000 74.95102  ? 237 LEU   B CG  1 
ATOM   3570 C CD1 . LEU   B 2 144 ? 39.84014 -3.22368  -15.84928 1.000 55.52030  ? 237 LEU   B CD1 1 
ATOM   3571 C CD2 . LEU   B 2 144 ? 41.89255 -3.54022  -17.24650 1.000 66.77349  ? 237 LEU   B CD2 1 
ATOM   3572 N N   . LYS   B 2 145 ? 43.81610 1.38598   -15.83554 1.000 69.32565  ? 238 LYS   B N   1 
ATOM   3573 C CA  . LYS   B 2 145 ? 43.88640 2.83982   -15.99542 1.000 63.96139  ? 238 LYS   B CA  1 
ATOM   3574 C C   . LYS   B 2 145 ? 42.52906 3.49765   -15.76289 1.000 67.76839  ? 238 LYS   B C   1 
ATOM   3575 O O   . LYS   B 2 145 ? 42.23367 4.55350   -16.32993 1.000 67.99126  ? 238 LYS   B O   1 
ATOM   3576 C CB  . LYS   B 2 145 ? 44.43830 3.22488   -17.37212 1.000 81.49300  ? 238 LYS   B CB  1 
ATOM   3577 C CG  . LYS   B 2 145 ? 45.85364 2.73661   -17.64156 1.000 76.67749  ? 238 LYS   B CG  1 
ATOM   3578 C CD  . LYS   B 2 145 ? 46.86323 3.42181   -16.73416 1.000 90.48490  ? 238 LYS   B CD  1 
ATOM   3579 C CE  . LYS   B 2 145 ? 48.28348 2.99594   -17.07431 1.000 94.67033  ? 238 LYS   B CE  1 
ATOM   3580 N NZ  . LYS   B 2 145 ? 49.29723 3.69484   -16.23631 1.000 100.12622 ? 238 LYS   B NZ  1 
ATOM   3581 N N   . TRP   B 2 146 ? 41.69779 2.86797   -14.93093 1.000 61.15615  ? 239 TRP   B N   1 
ATOM   3582 C CA  . TRP   B 2 146 ? 40.34601 3.32774   -14.61836 1.000 61.92352  ? 239 TRP   B CA  1 
ATOM   3583 C C   . TRP   B 2 146 ? 39.47023 3.45656   -15.86225 1.000 67.19919  ? 239 TRP   B C   1 
ATOM   3584 O O   . TRP   B 2 146 ? 38.49537 4.21533   -15.86300 1.000 64.10933  ? 239 TRP   B O   1 
ATOM   3585 C CB  . TRP   B 2 146 ? 40.37590 4.65088   -13.84404 1.000 63.01269  ? 239 TRP   B CB  1 
ATOM   3586 C CG  . TRP   B 2 146 ? 41.12040 4.55697   -12.54455 1.000 66.16603  ? 239 TRP   B CG  1 
ATOM   3587 C CD1 . TRP   B 2 146 ? 42.46146 4.72097   -12.35539 1.000 65.69987  ? 239 TRP   B CD1 1 
ATOM   3588 C CD2 . TRP   B 2 146 ? 40.56585 4.27021   -11.25417 1.000 64.63232  ? 239 TRP   B CD2 1 
ATOM   3589 N NE1 . TRP   B 2 146 ? 42.77653 4.55642   -11.02861 1.000 63.28785  ? 239 TRP   B NE1 1 
ATOM   3590 C CE2 . TRP   B 2 146 ? 41.63035 4.27926   -10.33119 1.000 57.40412  ? 239 TRP   B CE2 1 
ATOM   3591 C CE3 . TRP   B 2 146 ? 39.27284 4.00868   -10.78988 1.000 59.55744  ? 239 TRP   B CE3 1 
ATOM   3592 C CZ2 . TRP   B 2 146 ? 41.44240 4.03643   -8.97185  1.000 57.61302  ? 239 TRP   B CZ2 1 
ATOM   3593 C CZ3 . TRP   B 2 146 ? 39.08837 3.76847   -9.43988  1.000 63.90626  ? 239 TRP   B CZ3 1 
ATOM   3594 C CH2 . TRP   B 2 146 ? 40.16754 3.78346   -8.54697  1.000 66.61072  ? 239 TRP   B CH2 1 
ATOM   3595 N N   . ARG   B 2 147 ? 39.80024 2.72587   -16.92654 1.000 63.29662  ? 240 ARG   B N   1 
ATOM   3596 C CA  . ARG   B 2 147 ? 38.96604 2.66192   -18.12595 1.000 58.66522  ? 240 ARG   B CA  1 
ATOM   3597 C C   . ARG   B 2 147 ? 37.89226 1.61039   -17.88454 1.000 54.33246  ? 240 ARG   B C   1 
ATOM   3598 O O   . ARG   B 2 147 ? 38.04362 0.43892   -18.23386 1.000 60.72804  ? 240 ARG   B O   1 
ATOM   3599 C CB  . ARG   B 2 147 ? 39.80275 2.33382   -19.35652 1.000 69.20404  ? 240 ARG   B CB  1 
ATOM   3600 C CG  . ARG   B 2 147 ? 40.74177 3.44325   -19.79741 1.000 64.40369  ? 240 ARG   B CG  1 
ATOM   3601 C CD  . ARG   B 2 147 ? 39.97971 4.72050   -20.11242 1.000 79.34885  ? 240 ARG   B CD  1 
ATOM   3602 N NE  . ARG   B 2 147 ? 40.76967 5.64294   -20.91953 1.000 98.91652  ? 240 ARG   B NE  1 
ATOM   3603 C CZ  . ARG   B 2 147 ? 41.68737 6.46799   -20.43441 1.000 101.06989 ? 240 ARG   B CZ  1 
ATOM   3604 N NH1 . ARG   B 2 147 ? 41.97067 6.50425   -19.14294 1.000 106.06425 ? 240 ARG   B NH1 1 
ATOM   3605 N NH2 . ARG   B 2 147 ? 42.33966 7.27483   -21.26664 1.000 102.96237 ? 240 ARG   B NH2 1 
ATOM   3606 N N   . LEU   B 2 148 ? 36.78526 2.03672   -17.27648 1.000 54.30479  ? 241 LEU   B N   1 
ATOM   3607 C CA  . LEU   B 2 148 ? 35.74095 1.12037   -16.83501 1.000 57.18854  ? 241 LEU   B CA  1 
ATOM   3608 C C   . LEU   B 2 148 ? 34.41008 1.37597   -17.53173 1.000 59.95533  ? 241 LEU   B C   1 
ATOM   3609 O O   . LEU   B 2 148 ? 33.35645 1.02641   -16.99104 1.000 66.60704  ? 241 LEU   B O   1 
ATOM   3610 C CB  . LEU   B 2 148 ? 35.56954 1.20912   -15.31769 1.000 59.46360  ? 241 LEU   B CB  1 
ATOM   3611 C CG  . LEU   B 2 148 ? 36.83785 0.98074   -14.49448 1.000 60.51063  ? 241 LEU   B CG  1 
ATOM   3612 C CD1 . LEU   B 2 148 ? 36.58092 1.27020   -13.02735 1.000 58.48931  ? 241 LEU   B CD1 1 
ATOM   3613 C CD2 . LEU   B 2 148 ? 37.35499 -0.43780  -14.67989 1.000 60.13297  ? 241 LEU   B CD2 1 
ATOM   3614 N N   . SER   B 2 149 ? 34.43012 1.96633   -18.72452 1.000 60.83108  ? 242 SER   B N   1 
ATOM   3615 C CA  . SER   B 2 149 ? 33.20936 2.25861   -19.47822 1.000 52.38863  ? 242 SER   B CA  1 
ATOM   3616 C C   . SER   B 2 149 ? 33.30994 1.71303   -20.89916 1.000 64.25468  ? 242 SER   B C   1 
ATOM   3617 O O   . SER   B 2 149 ? 33.31098 2.47268   -21.87260 1.000 72.26070  ? 242 SER   B O   1 
ATOM   3618 C CB  . SER   B 2 149 ? 32.93875 3.76185   -19.49063 1.000 60.14196  ? 242 SER   B CB  1 
ATOM   3619 O OG  . SER   B 2 149 ? 32.88021 4.27955   -18.17244 1.000 74.72773  ? 242 SER   B OG  1 
ATOM   3620 N N   . PRO   B 2 150 ? 33.38000 0.39483   -21.05899 1.000 71.29827  ? 243 PRO   B N   1 
ATOM   3621 C CA  . PRO   B 2 150 ? 33.43590 -0.19082  -22.39718 1.000 57.35165  ? 243 PRO   B CA  1 
ATOM   3622 C C   . PRO   B 2 150 ? 32.03696 -0.43669  -22.95279 1.000 65.72823  ? 243 PRO   B C   1 
ATOM   3623 O O   . PRO   B 2 150 ? 31.03571 -0.40578  -22.23501 1.000 63.80703  ? 243 PRO   B O   1 
ATOM   3624 C CB  . PRO   B 2 150 ? 34.16318 -1.51542  -22.15056 1.000 66.57791  ? 243 PRO   B CB  1 
ATOM   3625 C CG  . PRO   B 2 150 ? 33.66437 -1.92539  -20.80487 1.000 57.80633  ? 243 PRO   B CG  1 
ATOM   3626 C CD  . PRO   B 2 150 ? 33.44149 -0.64860  -20.01747 1.000 61.56202  ? 243 PRO   B CD  1 
ATOM   3627 N N   . LEU   B 2 151 ? 31.99005 -0.68268  -24.25923 1.000 59.75031  ? 244 LEU   B N   1 
ATOM   3628 C CA  . LEU   B 2 151 ? 30.75871 -1.09542  -24.92847 1.000 65.52429  ? 244 LEU   B CA  1 
ATOM   3629 C C   . LEU   B 2 151 ? 30.74101 -2.61786  -24.94629 1.000 65.95120  ? 244 LEU   B C   1 
ATOM   3630 O O   . LEU   B 2 151 ? 31.40936 -3.24991  -25.76740 1.000 77.56233  ? 244 LEU   B O   1 
ATOM   3631 C CB  . LEU   B 2 151 ? 30.67724 -0.51009  -26.33351 1.000 50.00892  ? 244 LEU   B CB  1 
ATOM   3632 C CG  . LEU   B 2 151 ? 30.68923 1.01753   -26.41250 1.000 63.29883  ? 244 LEU   B CG  1 
ATOM   3633 C CD1 . LEU   B 2 151 ? 30.53633 1.48635   -27.85004 1.000 56.86509  ? 244 LEU   B CD1 1 
ATOM   3634 C CD2 . LEU   B 2 151 ? 29.60211 1.61276   -25.52847 1.000 60.51337  ? 244 LEU   B CD2 1 
ATOM   3635 N N   . THR   B 2 152 ? 29.97549 -3.20853  -24.03321 1.000 57.22864  ? 245 THR   B N   1 
ATOM   3636 C CA  . THR   B 2 152 ? 29.97002 -4.65228  -23.86794 1.000 63.28428  ? 245 THR   B CA  1 
ATOM   3637 C C   . THR   B 2 152 ? 29.31459 -5.33501  -25.06853 1.000 61.46312  ? 245 THR   B C   1 
ATOM   3638 O O   . THR   B 2 152 ? 28.76127 -4.69340  -25.96684 1.000 61.77123  ? 245 THR   B O   1 
ATOM   3639 C CB  . THR   B 2 152 ? 29.24113 -5.03946  -22.58214 1.000 57.41665  ? 245 THR   B CB  1 
ATOM   3640 O OG1 . THR   B 2 152 ? 27.86583 -4.64845  -22.67537 1.000 56.54053  ? 245 THR   B OG1 1 
ATOM   3641 C CG2 . THR   B 2 152 ? 29.87687 -4.35235  -21.38120 1.000 57.89318  ? 245 THR   B CG2 1 
ATOM   3642 N N   . ILE   B 2 153 ? 29.38907 -6.66805  -25.07330 1.000 55.09427  ? 246 ILE   B N   1 
ATOM   3643 C CA  . ILE   B 2 153 ? 28.74316 -7.44687  -26.12594 1.000 57.38379  ? 246 ILE   B CA  1 
ATOM   3644 C C   . ILE   B 2 153 ? 27.23185 -7.26629  -26.06708 1.000 63.26253  ? 246 ILE   B C   1 
ATOM   3645 O O   . ILE   B 2 153 ? 26.56719 -7.11733  -27.09997 1.000 57.21313  ? 246 ILE   B O   1 
ATOM   3646 C CB  . ILE   B 2 153 ? 29.13962 -8.93131  -26.01170 1.000 57.25664  ? 246 ILE   B CB  1 
ATOM   3647 C CG1 . ILE   B 2 153 ? 30.65896 -9.08945  -26.09244 1.000 65.28531  ? 246 ILE   B CG1 1 
ATOM   3648 C CG2 . ILE   B 2 153 ? 28.46285 -9.75303  -27.09549 1.000 70.83523  ? 246 ILE   B CG2 1 
ATOM   3649 C CD1 . ILE   B 2 153 ? 31.13429 -10.51908 -25.93290 1.000 65.76624  ? 246 ILE   B CD1 1 
ATOM   3650 N N   . VAL   B 2 154 ? 26.66659 -7.26299  -24.85865 1.000 55.94834  ? 247 VAL   B N   1 
ATOM   3651 C CA  . VAL   B 2 154 ? 25.21793 -7.16081  -24.72296 1.000 55.70084  ? 247 VAL   B CA  1 
ATOM   3652 C C   . VAL   B 2 154 ? 24.73447 -5.74196  -25.00921 1.000 50.66799  ? 247 VAL   B C   1 
ATOM   3653 O O   . VAL   B 2 154 ? 23.58659 -5.54865  -25.42733 1.000 58.68715  ? 247 VAL   B O   1 
ATOM   3654 C CB  . VAL   B 2 154 ? 24.78113 -7.64257  -23.32700 1.000 58.98907  ? 247 VAL   B CB  1 
ATOM   3655 C CG1 . VAL   B 2 154 ? 25.22198 -6.66089  -22.24915 1.000 55.37927  ? 247 VAL   B CG1 1 
ATOM   3656 C CG2 . VAL   B 2 154 ? 23.27524 -7.87112  -23.28095 1.000 53.91424  ? 247 VAL   B CG2 1 
ATOM   3657 N N   . SER   B 2 155 ? 25.58630 -4.73311  -24.80638 1.000 50.49515  ? 248 SER   B N   1 
ATOM   3658 C CA  . SER   B 2 155 ? 25.18334 -3.36564  -25.11877 1.000 53.25749  ? 248 SER   B CA  1 
ATOM   3659 C C   . SER   B 2 155 ? 24.95340 -3.18932  -26.61418 1.000 60.73201  ? 248 SER   B C   1 
ATOM   3660 O O   . SER   B 2 155 ? 24.03366 -2.47293  -27.02551 1.000 54.60461  ? 248 SER   B O   1 
ATOM   3661 C CB  . SER   B 2 155 ? 26.23312 -2.37536  -24.61731 1.000 55.72815  ? 248 SER   B CB  1 
ATOM   3662 O OG  . SER   B 2 155 ? 27.45508 -2.52946  -25.31695 1.000 65.04941  ? 248 SER   B OG  1 
ATOM   3663 N N   . TRP   B 2 156 ? 25.77603 -3.83726  -27.44313 1.000 55.78417  ? 249 TRP   B N   1 
ATOM   3664 C CA  . TRP   B 2 156 ? 25.57449 -3.76041  -28.88624 1.000 54.74912  ? 249 TRP   B CA  1 
ATOM   3665 C C   . TRP   B 2 156 ? 24.27388 -4.43639  -29.29784 1.000 56.96546  ? 249 TRP   B C   1 
ATOM   3666 O O   . TRP   B 2 156 ? 23.55961 -3.93666  -30.17451 1.000 50.57277  ? 249 TRP   B O   1 
ATOM   3667 C CB  . TRP   B 2 156 ? 26.75843 -4.38685  -29.62074 1.000 53.07568  ? 249 TRP   B CB  1 
ATOM   3668 C CG  . TRP   B 2 156 ? 27.98127 -3.52756  -29.63335 1.000 54.31031  ? 249 TRP   B CG  1 
ATOM   3669 C CD1 . TRP   B 2 156 ? 29.14189 -3.74098  -28.94917 1.000 56.60058  ? 249 TRP   B CD1 1 
ATOM   3670 C CD2 . TRP   B 2 156 ? 28.16476 -2.31103  -30.36611 1.000 55.48600  ? 249 TRP   B CD2 1 
ATOM   3671 N NE1 . TRP   B 2 156 ? 30.03861 -2.73392  -29.21319 1.000 63.11572  ? 249 TRP   B NE1 1 
ATOM   3672 C CE2 . TRP   B 2 156 ? 29.46224 -1.84307  -30.08010 1.000 59.64921  ? 249 TRP   B CE2 1 
ATOM   3673 C CE3 . TRP   B 2 156 ? 27.35793 -1.57273  -31.23741 1.000 63.14204  ? 249 TRP   B CE3 1 
ATOM   3674 C CZ2 . TRP   B 2 156 ? 29.97135 -0.67061  -30.63391 1.000 67.99929  ? 249 TRP   B CZ2 1 
ATOM   3675 C CZ3 . TRP   B 2 156 ? 27.86503 -0.40931  -31.78572 1.000 65.98748  ? 249 TRP   B CZ3 1 
ATOM   3676 C CH2 . TRP   B 2 156 ? 29.15921 0.03028   -31.48211 1.000 68.02814  ? 249 TRP   B CH2 1 
ATOM   3677 N N   . LEU   B 2 157 ? 23.94962 -5.57335  -28.67719 1.000 54.00549  ? 250 LEU   B N   1 
ATOM   3678 C CA  . LEU   B 2 157 ? 22.69180 -6.24695  -28.98315 1.000 58.14003  ? 250 LEU   B CA  1 
ATOM   3679 C C   . LEU   B 2 157 ? 21.49931 -5.35807  -28.65455 1.000 54.92624  ? 250 LEU   B C   1 
ATOM   3680 O O   . LEU   B 2 157 ? 20.48804 -5.37384  -29.36609 1.000 58.81221  ? 250 LEU   B O   1 
ATOM   3681 C CB  . LEU   B 2 157 ? 22.60532 -7.56866  -28.21999 1.000 52.66917  ? 250 LEU   B CB  1 
ATOM   3682 C CG  . LEU   B 2 157 ? 21.30656 -8.35817  -28.38989 1.000 56.01423  ? 250 LEU   B CG  1 
ATOM   3683 C CD1 . LEU   B 2 157 ? 21.04456 -8.64843  -29.86008 1.000 53.25889  ? 250 LEU   B CD1 1 
ATOM   3684 C CD2 . LEU   B 2 157 ? 21.35049 -9.64533  -27.58090 1.000 68.39469  ? 250 LEU   B CD2 1 
ATOM   3685 N N   . ASN   B 2 158 ? 21.60176 -4.57175  -27.58050 1.000 60.41877  ? 251 ASN   B N   1 
ATOM   3686 C CA  . ASN   B 2 158 ? 20.53080 -3.64121  -27.24198 1.000 68.64923  ? 251 ASN   B CA  1 
ATOM   3687 C C   . ASN   B 2 158 ? 20.36148 -2.58498  -28.32713 1.000 66.30088  ? 251 ASN   B C   1 
ATOM   3688 O O   . ASN   B 2 158 ? 19.23519 -2.18845  -28.64877 1.000 71.70687  ? 251 ASN   B O   1 
ATOM   3689 C CB  . ASN   B 2 158 ? 20.81609 -2.98789  -25.88981 1.000 57.68892  ? 251 ASN   B CB  1 
ATOM   3690 C CG  . ASN   B 2 158 ? 19.60274 -2.28449  -25.31352 1.000 79.01689  ? 251 ASN   B CG  1 
ATOM   3691 O OD1 . ASN   B 2 158 ? 18.46936 -2.73203  -25.48822 1.000 77.80488  ? 251 ASN   B OD1 1 
ATOM   3692 N ND2 . ASN   B 2 158 ? 19.83540 -1.17489  -24.62239 1.000 82.65730  ? 251 ASN   B ND2 1 
ATOM   3693 N N   . VAL   B 2 159 ? 21.47065 -2.12386  -28.90867 1.000 72.18872  ? 252 VAL   B N   1 
ATOM   3694 C CA  . VAL   B 2 159 ? 21.39502 -1.15686  -30.00002 1.000 51.07928  ? 252 VAL   B CA  1 
ATOM   3695 C C   . VAL   B 2 159 ? 20.77601 -1.79791  -31.23530 1.000 67.55328  ? 252 VAL   B C   1 
ATOM   3696 O O   . VAL   B 2 159 ? 19.90523 -1.21286  -31.88995 1.000 78.11379  ? 252 VAL   B O   1 
ATOM   3697 C CB  . VAL   B 2 159 ? 22.79008 -0.58267  -30.30839 1.000 64.27037  ? 252 VAL   B CB  1 
ATOM   3698 C CG1 . VAL   B 2 159 ? 22.69684 0.48660   -31.38626 1.000 83.98876  ? 252 VAL   B CG1 1 
ATOM   3699 C CG2 . VAL   B 2 159 ? 23.43446 -0.02457  -29.05080 1.000 58.02039  ? 252 VAL   B CG2 1 
ATOM   3700 N N   . TYR   B 2 160 ? 21.21513 -3.01368  -31.56960 1.000 59.49197  ? 253 TYR   B N   1 
ATOM   3701 C CA  . TYR   B 2 160 ? 20.74238 -3.66560  -32.78567 1.000 64.68786  ? 253 TYR   B CA  1 
ATOM   3702 C C   . TYR   B 2 160 ? 19.25617 -3.99055  -32.71129 1.000 73.38132  ? 253 TYR   B C   1 
ATOM   3703 O O   . TYR   B 2 160 ? 18.57004 -3.98155  -33.73957 1.000 64.10199  ? 253 TYR   B O   1 
ATOM   3704 C CB  . TYR   B 2 160 ? 21.54864 -4.93856  -33.04972 1.000 70.79717  ? 253 TYR   B CB  1 
ATOM   3705 C CG  . TYR   B 2 160 ? 23.03808 -4.71823  -33.22493 1.000 64.76715  ? 253 TYR   B CG  1 
ATOM   3706 C CD1 . TYR   B 2 160 ? 23.55085 -3.45789  -33.50855 1.000 65.00737  ? 253 TYR   B CD1 1 
ATOM   3707 C CD2 . TYR   B 2 160 ? 23.93096 -5.77612  -33.11185 1.000 58.97017  ? 253 TYR   B CD2 1 
ATOM   3708 C CE1 . TYR   B 2 160 ? 24.90986 -3.25763  -33.66724 1.000 62.19754  ? 253 TYR   B CE1 1 
ATOM   3709 C CE2 . TYR   B 2 160 ? 25.29093 -5.58523  -33.27091 1.000 54.71424  ? 253 TYR   B CE2 1 
ATOM   3710 C CZ  . TYR   B 2 160 ? 25.77414 -4.32506  -33.54861 1.000 58.80518  ? 253 TYR   B CZ  1 
ATOM   3711 O OH  . TYR   B 2 160 ? 27.12691 -4.13100  -33.70765 1.000 60.20307  ? 253 TYR   B OH  1 
ATOM   3712 N N   . MET   B 2 161 ? 18.74053 -4.27509  -31.51305 1.000 70.67104  ? 254 MET   B N   1 
ATOM   3713 C CA  . MET   B 2 161 ? 17.32470 -4.60156  -31.38418 1.000 67.64698  ? 254 MET   B CA  1 
ATOM   3714 C C   . MET   B 2 161 ? 16.44466 -3.36609  -31.51833 1.000 72.53628  ? 254 MET   B C   1 
ATOM   3715 O O   . MET   B 2 161 ? 15.31610 -3.46302  -32.01402 1.000 79.24541  ? 254 MET   B O   1 
ATOM   3716 C CB  . MET   B 2 161 ? 17.06387 -5.29881  -30.04976 1.000 66.89372  ? 254 MET   B CB  1 
ATOM   3717 C CG  . MET   B 2 161 ? 17.60262 -6.71638  -29.98180 1.000 59.92505  ? 254 MET   B CG  1 
ATOM   3718 S SD  . MET   B 2 161 ? 16.94574 -7.74832  -31.30364 1.000 77.65357  ? 254 MET   B SD  1 
ATOM   3719 C CE  . MET   B 2 161 ? 15.18514 -7.54903  -31.03861 1.000 79.06970  ? 254 MET   B CE  1 
ATOM   3720 N N   . GLN   B 2 162 ? 16.93600 -2.20285  -31.08644 1.000 72.75388  ? 255 GLN   B N   1 
ATOM   3721 C CA  . GLN   B 2 162 ? 16.15030 -0.98044  -31.21742 1.000 73.86199  ? 255 GLN   B CA  1 
ATOM   3722 C C   . GLN   B 2 162 ? 16.04154 -0.54732  -32.67387 1.000 84.53937  ? 255 GLN   B C   1 
ATOM   3723 O O   . GLN   B 2 162 ? 14.96027 -0.16078  -33.13350 1.000 74.84684  ? 255 GLN   B O   1 
ATOM   3724 C CB  . GLN   B 2 162 ? 16.76653 0.13384   -30.37303 1.000 69.34510  ? 255 GLN   B CB  1 
ATOM   3725 C CG  . GLN   B 2 162 ? 15.95394 1.41847   -30.35202 1.000 83.40727  ? 255 GLN   B CG  1 
ATOM   3726 C CD  . GLN   B 2 162 ? 14.62495 1.25609   -29.64052 1.000 78.80729  ? 255 GLN   B CD  1 
ATOM   3727 O OE1 . GLN   B 2 162 ? 14.45195 0.35304   -28.82171 1.000 82.09192  ? 255 GLN   B OE1 1 
ATOM   3728 N NE2 . GLN   B 2 162 ? 13.67626 2.13145   -29.95184 1.000 89.40530  ? 255 GLN   B NE2 1 
ATOM   3729 N N   . VAL   B 2 163 ? 17.15092 -0.60603  -33.41469 1.000 67.76084  ? 256 VAL   B N   1 
ATOM   3730 C CA  . VAL   B 2 163 ? 17.13159 -0.19927  -34.81589 1.000 84.11981  ? 256 VAL   B CA  1 
ATOM   3731 C C   . VAL   B 2 163 ? 16.26380 -1.13998  -35.64207 1.000 77.31122  ? 256 VAL   B C   1 
ATOM   3732 O O   . VAL   B 2 163 ? 15.62145 -0.71339  -36.60980 1.000 78.66006  ? 256 VAL   B O   1 
ATOM   3733 C CB  . VAL   B 2 163 ? 18.56807 -0.12162  -35.36549 1.000 74.77797  ? 256 VAL   B CB  1 
ATOM   3734 C CG1 . VAL   B 2 163 ? 18.56813 0.39471   -36.79796 1.000 83.57869  ? 256 VAL   B CG1 1 
ATOM   3735 C CG2 . VAL   B 2 163 ? 19.42509 0.76384   -34.47535 1.000 68.87888  ? 256 VAL   B CG2 1 
ATOM   3736 N N   . ALA   B 2 164 ? 16.21709 -2.42399  -35.27699 1.000 71.09836  ? 257 ALA   B N   1 
ATOM   3737 C CA  . ALA   B 2 164 ? 15.37415 -3.36603  -36.00552 1.000 80.80728  ? 257 ALA   B CA  1 
ATOM   3738 C C   . ALA   B 2 164 ? 13.89728 -3.03217  -35.85174 1.000 89.94408  ? 257 ALA   B C   1 
ATOM   3739 O O   . ALA   B 2 164 ? 13.09502 -3.34005  -36.74101 1.000 78.44428  ? 257 ALA   B O   1 
ATOM   3740 C CB  . ALA   B 2 164 ? 15.64891 -4.79336  -35.53216 1.000 70.70438  ? 257 ALA   B CB  1 
ATOM   3741 N N   . TYR   B 2 165 ? 13.52030 -2.40201  -34.74053 1.000 73.30806  ? 258 TYR   B N   1 
ATOM   3742 C CA  . TYR   B 2 165 ? 12.12932 -2.03882  -34.50689 1.000 80.50932  ? 258 TYR   B CA  1 
ATOM   3743 C C   . TYR   B 2 165 ? 11.97832 -0.53054  -34.35974 1.000 90.94770  ? 258 TYR   B C   1 
ATOM   3744 O O   . TYR   B 2 165 ? 11.48908 -0.04323  -33.33539 1.000 110.78537 ? 258 TYR   B O   1 
ATOM   3745 C CB  . TYR   B 2 165 ? 11.59090 -2.76203  -33.27115 1.000 77.86375  ? 258 TYR   B CB  1 
ATOM   3746 C CG  . TYR   B 2 165 ? 11.37286 -4.24017  -33.49611 1.000 90.52090  ? 258 TYR   B CG  1 
ATOM   3747 C CD1 . TYR   B 2 165 ? 12.41064 -5.14910  -33.33439 1.000 80.50993  ? 258 TYR   B CD1 1 
ATOM   3748 C CD2 . TYR   B 2 165 ? 10.13046 -4.72563  -33.88131 1.000 90.89127  ? 258 TYR   B CD2 1 
ATOM   3749 C CE1 . TYR   B 2 165 ? 12.21505 -6.50149  -33.54652 1.000 89.32955  ? 258 TYR   B CE1 1 
ATOM   3750 C CE2 . TYR   B 2 165 ? 9.92467  -6.07439  -34.09367 1.000 93.56676  ? 258 TYR   B CE2 1 
ATOM   3751 C CZ  . TYR   B 2 165 ? 10.96936 -6.95809  -33.92539 1.000 84.80550  ? 258 TYR   B CZ  1 
ATOM   3752 O OH  . TYR   B 2 165 ? 10.76605 -8.30253  -34.13580 1.000 93.39142  ? 258 TYR   B OH  1 
ATOM   3753 N N   . LEU   B 2 166 ? 12.40165 0.21274   -35.37705 1.000 84.08141  ? 259 LEU   B N   1 
ATOM   3754 C CA  . LEU   B 2 166 ? 12.21926 1.65512   -35.42739 1.000 96.46615  ? 259 LEU   B CA  1 
ATOM   3755 C C   . LEU   B 2 166 ? 10.99588 1.98840   -36.26859 1.000 102.83434 ? 259 LEU   B C   1 
ATOM   3756 O O   . LEU   B 2 166 ? 10.71926 1.32507   -37.27252 1.000 92.65362  ? 259 LEU   B O   1 
ATOM   3757 C CB  . LEU   B 2 166 ? 13.45334 2.34865   -36.00685 1.000 90.00317  ? 259 LEU   B CB  1 
ATOM   3758 C CG  . LEU   B 2 166 ? 14.65732 2.49403   -35.07668 1.000 93.41851  ? 259 LEU   B CG  1 
ATOM   3759 C CD1 . LEU   B 2 166 ? 15.82678 3.12318   -35.81480 1.000 90.30023  ? 259 LEU   B CD1 1 
ATOM   3760 C CD2 . LEU   B 2 166 ? 14.28848 3.31451   -33.84994 1.000 90.56629  ? 259 LEU   B CD2 1 
ATOM   3761 N N   . ASN   B 2 167 ? 10.26550 3.01967   -35.85176 1.000 127.68286 ? 260 ASN   B N   1 
ATOM   3762 C CA  . ASN   B 2 167 ? 9.07169  3.46975   -36.54097 1.000 142.73569 ? 260 ASN   B CA  1 
ATOM   3763 C C   . ASN   B 2 167 ? 9.35702  4.80756   -37.22879 1.000 159.64437 ? 260 ASN   B C   1 
ATOM   3764 O O   . ASN   B 2 167 ? 10.52178 5.17619   -37.44040 1.000 156.81401 ? 260 ASN   B O   1 
ATOM   3765 C CB  . ASN   B 2 167 ? 7.91409  3.54757   -35.54116 1.000 149.98066 ? 260 ASN   B CB  1 
ATOM   3766 C CG  . ASN   B 2 167 ? 6.62760  2.96171   -36.09069 1.000 156.83723 ? 260 ASN   B CG  1 
ATOM   3767 O OD1 . ASN   B 2 167 ? 5.99312  2.12221   -35.45203 1.000 161.42445 ? 260 ASN   B OD1 1 
ATOM   3768 N ND2 . ASN   B 2 167 ? 6.23840  3.39840   -37.28273 1.000 163.35753 ? 260 ASN   B ND2 1 
ATOM   3769 N N   . ASP   B 2 168 ? 8.29304  5.53384   -37.57796 1.000 194.69258 ? 261 ASP   B N   1 
ATOM   3770 C CA  . ASP   B 2 168 ? 8.45629  6.83845   -38.20725 1.000 194.92972 ? 261 ASP   B CA  1 
ATOM   3771 C C   . ASP   B 2 168 ? 8.95900  7.89189   -37.23001 1.000 182.89893 ? 261 ASP   B C   1 
ATOM   3772 O O   . ASP   B 2 168 ? 9.53962  8.89343   -37.66207 1.000 179.16408 ? 261 ASP   B O   1 
ATOM   3773 C CB  . ASP   B 2 168 ? 7.13386  7.29270   -38.82692 1.000 205.31777 ? 261 ASP   B CB  1 
ATOM   3774 C CG  . ASP   B 2 168 ? 6.01398  7.38276   -37.80863 1.000 201.35505 ? 261 ASP   B CG  1 
ATOM   3775 O OD1 . ASP   B 2 168 ? 6.03124  6.60261   -36.83333 1.000 198.09352 ? 261 ASP   B OD1 1 
ATOM   3776 O OD2 . ASP   B 2 168 ? 5.11639  8.23354   -37.98321 1.000 196.25132 ? 261 ASP   B OD2 1 
ATOM   3777 N N   . LEU   B 2 169 ? 8.75069  7.68899   -35.92720 1.000 171.63387 ? 262 LEU   B N   1 
ATOM   3778 C CA  . LEU   B 2 169 ? 9.21538  8.64984   -34.93454 1.000 168.01575 ? 262 LEU   B CA  1 
ATOM   3779 C C   . LEU   B 2 169 ? 10.73143 8.64661   -34.78696 1.000 160.55941 ? 262 LEU   B C   1 
ATOM   3780 O O   . LEU   B 2 169 ? 11.29371 9.63989   -34.31273 1.000 158.22430 ? 262 LEU   B O   1 
ATOM   3781 C CB  . LEU   B 2 169 ? 8.55560  8.37244   -33.57988 1.000 165.81026 ? 262 LEU   B CB  1 
ATOM   3782 C CG  . LEU   B 2 169 ? 8.27349  6.91796   -33.19105 1.000 155.86642 ? 262 LEU   B CG  1 
ATOM   3783 C CD1 . LEU   B 2 169 ? 8.46654  6.71941   -31.69778 1.000 142.82258 ? 262 LEU   B CD1 1 
ATOM   3784 C CD2 . LEU   B 2 169 ? 6.86028  6.51656   -33.59335 1.000 148.06477 ? 262 LEU   B CD2 1 
ATOM   3785 N N   . HIS   B 2 170 ? 11.39874 7.55801   -35.17919 1.000 161.76925 ? 263 HIS   B N   1 
ATOM   3786 C CA  . HIS   B 2 170 ? 12.85789 7.44367   -35.11426 1.000 154.89295 ? 263 HIS   B CA  1 
ATOM   3787 C C   . HIS   B 2 170 ? 13.38956 7.66827   -33.70067 1.000 151.61734 ? 263 HIS   B C   1 
ATOM   3788 O O   . HIS   B 2 170 ? 14.53015 8.10109   -33.51753 1.000 142.02294 ? 263 HIS   B O   1 
ATOM   3789 C CB  . HIS   B 2 170 ? 13.53810 8.40399   -36.09630 1.000 150.47390 ? 263 HIS   B CB  1 
ATOM   3790 C CG  . HIS   B 2 170 ? 13.43974 7.97732   -37.52818 1.000 153.46707 ? 263 HIS   B CG  1 
ATOM   3791 N ND1 . HIS   B 2 170 ? 12.98912 6.73041   -37.90482 1.000 154.99129 ? 263 HIS   B ND1 1 
ATOM   3792 C CD2 . HIS   B 2 170 ? 13.73734 8.63182   -38.67574 1.000 144.91525 ? 263 HIS   B CD2 1 
ATOM   3793 C CE1 . HIS   B 2 170 ? 13.01219 6.63546   -39.22234 1.000 152.76035 ? 263 HIS   B CE1 1 
ATOM   3794 N NE2 . HIS   B 2 170 ? 13.46199 7.77573   -39.71429 1.000 145.45714 ? 263 HIS   B NE2 1 
ATOM   3795 N N   . GLU   B 2 171 ? 12.57342 7.37618   -32.69054 1.000 157.14166 ? 264 GLU   B N   1 
ATOM   3796 C CA  . GLU   B 2 171 ? 12.98113 7.54077   -31.29702 1.000 150.08539 ? 264 GLU   B CA  1 
ATOM   3797 C C   . GLU   B 2 171 ? 13.83592 6.34253   -30.90715 1.000 137.11057 ? 264 GLU   B C   1 
ATOM   3798 O O   . GLU   B 2 171 ? 13.32033 5.25820   -30.62605 1.000 132.94368 ? 264 GLU   B O   1 
ATOM   3799 C CB  . GLU   B 2 171 ? 11.76449 7.67882   -30.38950 1.000 147.11160 ? 264 GLU   B CB  1 
ATOM   3800 C CG  . GLU   B 2 171 ? 12.10307 8.08032   -28.96327 1.000 147.54420 ? 264 GLU   B CG  1 
ATOM   3801 C CD  . GLU   B 2 171 ? 12.74197 9.45417   -28.88074 1.000 155.15980 ? 264 GLU   B CD  1 
ATOM   3802 O OE1 . GLU   B 2 171 ? 12.40067 10.32299  -29.71121 1.000 151.70680 ? 264 GLU   B OE1 1 
ATOM   3803 O OE2 . GLU   B 2 171 ? 13.58978 9.66409   -27.98790 1.000 153.39607 ? 264 GLU   B OE2 1 
ATOM   3804 N N   . VAL   B 2 172 ? 15.15758 6.53879   -30.88902 1.000 107.97900 ? 265 VAL   B N   1 
ATOM   3805 C CA  . VAL   B 2 172 ? 16.08622 5.44421   -30.62046 1.000 99.34322  ? 265 VAL   B CA  1 
ATOM   3806 C C   . VAL   B 2 172 ? 16.40861 5.29149   -29.13988 1.000 88.88131  ? 265 VAL   B C   1 
ATOM   3807 O O   . VAL   B 2 172 ? 17.06255 4.30887   -28.75646 1.000 83.02201  ? 265 VAL   B O   1 
ATOM   3808 C CB  . VAL   B 2 172 ? 17.38641 5.64149   -31.42812 1.000 99.52853  ? 265 VAL   B CB  1 
ATOM   3809 C CG1 . VAL   B 2 172 ? 18.33339 6.59066   -30.70325 1.000 88.78083  ? 265 VAL   B CG1 1 
ATOM   3810 C CG2 . VAL   B 2 172 ? 18.05348 4.30214   -31.72501 1.000 94.19605  ? 265 VAL   B CG2 1 
ATOM   3811 N N   . LEU   B 2 173 ? 15.96451 6.21907   -28.29173 1.000 81.92302  ? 266 LEU   B N   1 
ATOM   3812 C CA  . LEU   B 2 173 ? 16.27772 6.15162   -26.86968 1.000 80.01461  ? 266 LEU   B CA  1 
ATOM   3813 C C   . LEU   B 2 173 ? 15.21110 5.43076   -26.05690 1.000 77.80039  ? 266 LEU   B C   1 
ATOM   3814 O O   . LEU   B 2 173 ? 15.51949 4.89555   -24.98573 1.000 75.16361  ? 266 LEU   B O   1 
ATOM   3815 C CB  . LEU   B 2 173 ? 16.48530 7.56039   -26.30606 1.000 84.00547  ? 266 LEU   B CB  1 
ATOM   3816 C CG  . LEU   B 2 173 ? 17.70908 8.31421   -26.83108 1.000 82.16090  ? 266 LEU   B CG  1 
ATOM   3817 C CD1 . LEU   B 2 173 ? 17.89148 9.63193   -26.09150 1.000 79.52947  ? 266 LEU   B CD1 1 
ATOM   3818 C CD2 . LEU   B 2 173 ? 18.95834 7.45195   -26.71954 1.000 80.15845  ? 266 LEU   B CD2 1 
ATOM   3819 N N   . LEU   B 2 174 ? 13.96737 5.40403   -26.53082 1.000 77.26207  ? 267 LEU   B N   1 
ATOM   3820 C CA  . LEU   B 2 174 ? 12.90544 4.69631   -25.82830 1.000 75.41686  ? 267 LEU   B CA  1 
ATOM   3821 C C   . LEU   B 2 174 ? 12.90099 3.23908   -26.26713 1.000 85.58308  ? 267 LEU   B C   1 
ATOM   3822 O O   . LEU   B 2 174 ? 12.71589 2.96562   -27.46120 1.000 86.22715  ? 267 LEU   B O   1 
ATOM   3823 C CB  . LEU   B 2 174 ? 11.55453 5.33639   -26.10626 1.000 72.74449  ? 267 LEU   B CB  1 
ATOM   3824 C CG  . LEU   B 2 174 ? 10.50992 5.31056   -24.98430 1.000 85.46127  ? 267 LEU   B CG  1 
ATOM   3825 C CD1 . LEU   B 2 174 ? 9.38916  6.29669   -25.27822 1.000 104.00872 ? 267 LEU   B CD1 1 
ATOM   3826 C CD2 . LEU   B 2 174 ? 9.94371  3.91345   -24.77789 1.000 77.32072  ? 267 LEU   B CD2 1 
ATOM   3827 N N   . PRO   B 2 175 ? 13.09385 2.28358   -25.35748 1.000 78.78064  ? 268 PRO   B N   1 
ATOM   3828 C CA  . PRO   B 2 175 ? 13.21821 0.87851   -25.77208 1.000 68.33804  ? 268 PRO   B CA  1 
ATOM   3829 C C   . PRO   B 2 175 ? 11.90009 0.33246   -26.30286 1.000 77.03476  ? 268 PRO   B C   1 
ATOM   3830 O O   . PRO   B 2 175 ? 10.83990 0.54201   -25.70899 1.000 77.43202  ? 268 PRO   B O   1 
ATOM   3831 C CB  . PRO   B 2 175 ? 13.64550 0.16549   -24.48452 1.000 80.99698  ? 268 PRO   B CB  1 
ATOM   3832 C CG  . PRO   B 2 175 ? 13.12947 1.03872   -23.38556 1.000 73.96523  ? 268 PRO   B CG  1 
ATOM   3833 C CD  . PRO   B 2 175 ? 13.22079 2.44844   -23.89875 1.000 76.57185  ? 268 PRO   B CD  1 
ATOM   3834 N N   . GLN   B 2 176 ? 11.97692 -0.37628  -27.43342 1.000 66.18711  ? 269 GLN   B N   1 
ATOM   3835 C CA  . GLN   B 2 176 ? 10.78688 -0.97517  -28.03758 1.000 79.28346  ? 269 GLN   B CA  1 
ATOM   3836 C C   . GLN   B 2 176 ? 11.24973 -2.12487  -28.93331 1.000 76.09480  ? 269 GLN   B C   1 
ATOM   3837 O O   . GLN   B 2 176 ? 11.65715 -1.89415  -30.07513 1.000 91.18893  ? 269 GLN   B O   1 
ATOM   3838 C CB  . GLN   B 2 176 ? 9.98732  0.05783   -28.81762 1.000 72.29399  ? 269 GLN   B CB  1 
ATOM   3839 C CG  . GLN   B 2 176 ? 8.60155  -0.40975  -29.25440 1.000 90.63288  ? 269 GLN   B CG  1 
ATOM   3840 C CD  . GLN   B 2 176 ? 8.61806  -1.17945  -30.56445 1.000 101.28613 ? 269 GLN   B CD  1 
ATOM   3841 O OE1 . GLN   B 2 176 ? 9.42889  -0.90447  -31.44909 1.000 105.29874 ? 269 GLN   B OE1 1 
ATOM   3842 N NE2 . GLN   B 2 176 ? 7.71873  -2.14959  -30.69363 1.000 84.04222  ? 269 GLN   B NE2 1 
ATOM   3843 N N   . TYR   B 2 177 ? 11.18511 -3.34708  -28.40254 1.000 73.37525  ? 270 TYR   B N   1 
ATOM   3844 C CA  . TYR   B 2 177 ? 11.49879 -4.55816  -29.15202 1.000 75.90373  ? 270 TYR   B CA  1 
ATOM   3845 C C   . TYR   B 2 177 ? 11.01422 -5.77965  -28.37820 1.000 66.08026  ? 270 TYR   B C   1 
ATOM   3846 O O   . TYR   B 2 177 ? 10.89403 -5.72417  -27.14721 1.000 77.79397  ? 270 TYR   B O   1 
ATOM   3847 C CB  . TYR   B 2 177 ? 13.00122 -4.65637  -29.43978 1.000 75.30823  ? 270 TYR   B CB  1 
ATOM   3848 C CG  . TYR   B 2 177 ? 13.89520 -4.53078  -28.22444 1.000 73.78059  ? 270 TYR   B CG  1 
ATOM   3849 C CD1 . TYR   B 2 177 ? 14.16612 -5.62959  -27.41808 1.000 67.58672  ? 270 TYR   B CD1 1 
ATOM   3850 C CD2 . TYR   B 2 177 ? 14.48616 -3.31720  -27.89695 1.000 66.49131  ? 270 TYR   B CD2 1 
ATOM   3851 C CE1 . TYR   B 2 177 ? 14.98814 -5.51952  -26.31173 1.000 60.18714  ? 270 TYR   B CE1 1 
ATOM   3852 C CE2 . TYR   B 2 177 ? 15.31026 -3.19789  -26.79372 1.000 74.23255  ? 270 TYR   B CE2 1 
ATOM   3853 C CZ  . TYR   B 2 177 ? 15.55780 -4.30178  -26.00508 1.000 71.07545  ? 270 TYR   B CZ  1 
ATOM   3854 O OH  . TYR   B 2 177 ? 16.37738 -4.18686  -24.90600 1.000 76.29230  ? 270 TYR   B OH  1 
ATOM   3855 N N   . PRO   B 2 178 ? 10.71319 -6.88721  -29.05646 1.000 65.13696  ? 271 PRO   B N   1 
ATOM   3856 C CA  . PRO   B 2 178 ? 10.25847 -8.08929  -28.34438 1.000 60.72398  ? 271 PRO   B CA  1 
ATOM   3857 C C   . PRO   B 2 178 ? 11.32139 -8.60734  -27.38625 1.000 69.31802  ? 271 PRO   B C   1 
ATOM   3858 O O   . PRO   B 2 178 ? 12.48543 -8.78386  -27.75335 1.000 62.34087  ? 271 PRO   B O   1 
ATOM   3859 C CB  . PRO   B 2 178 ? 9.98011  -9.08652  -29.47491 1.000 55.27699  ? 271 PRO   B CB  1 
ATOM   3860 C CG  . PRO   B 2 178 ? 9.72161  -8.23532  -30.67298 1.000 74.75799  ? 271 PRO   B CG  1 
ATOM   3861 C CD  . PRO   B 2 178 ? 10.61882 -7.04356  -30.51748 1.000 70.71183  ? 271 PRO   B CD  1 
ATOM   3862 N N   . GLN   B 2 179 ? 10.90278 -8.85601  -26.14400 1.000 61.59402  ? 272 GLN   B N   1 
ATOM   3863 C CA  . GLN   B 2 179 ? 11.83625 -9.31005  -25.12042 1.000 64.07003  ? 272 GLN   B CA  1 
ATOM   3864 C C   . GLN   B 2 179 ? 12.23785 -10.76477 -25.32139 1.000 60.39594  ? 272 GLN   B C   1 
ATOM   3865 O O   . GLN   B 2 179 ? 13.35444 -11.15190 -24.95813 1.000 65.81238  ? 272 GLN   B O   1 
ATOM   3866 C CB  . GLN   B 2 179 ? 11.21953 -9.12327  -23.73468 1.000 61.87708  ? 272 GLN   B CB  1 
ATOM   3867 C CG  . GLN   B 2 179 ? 10.79022 -7.69955  -23.43172 1.000 75.63440  ? 272 GLN   B CG  1 
ATOM   3868 C CD  . GLN   B 2 179 ? 9.98440  -7.59599  -22.15217 1.000 90.81739  ? 272 GLN   B CD  1 
ATOM   3869 O OE1 . GLN   B 2 179 ? 9.16341  -8.46198  -21.84995 1.000 96.48190  ? 272 GLN   B OE1 1 
ATOM   3870 N NE2 . GLN   B 2 179 ? 10.21877 -6.53495  -21.39000 1.000 86.37527  ? 272 GLN   B NE2 1 
ATOM   3871 N N   . GLN   B 2 180 ? 11.35152 -11.58272 -25.89433 1.000 61.85177  ? 273 GLN   B N   1 
ATOM   3872 C CA  . GLN   B 2 180 ? 11.62981 -13.01235 -25.98467 1.000 73.23822  ? 273 GLN   B CA  1 
ATOM   3873 C C   . GLN   B 2 180 ? 12.71504 -13.30695 -27.01307 1.000 63.01266  ? 273 GLN   B C   1 
ATOM   3874 O O   . GLN   B 2 180 ? 13.57417 -14.16461 -26.78356 1.000 75.96652  ? 273 GLN   B O   1 
ATOM   3875 C CB  . GLN   B 2 180 ? 10.35080 -13.78204 -26.31307 1.000 80.19811  ? 273 GLN   B CB  1 
ATOM   3876 C CG  . GLN   B 2 180 ? 10.47429 -15.28351 -26.10361 1.000 81.11204  ? 273 GLN   B CG  1 
ATOM   3877 C CD  . GLN   B 2 180 ? 9.15311  -16.00966 -26.26237 1.000 104.00593 ? 273 GLN   B CD  1 
ATOM   3878 O OE1 . GLN   B 2 180 ? 8.98804  -17.13228 -25.78451 1.000 108.15266 ? 273 GLN   B OE1 1 
ATOM   3879 N NE2 . GLN   B 2 180 ? 8.20423  -15.37256 -26.93814 1.000 106.66201 ? 273 GLN   B NE2 1 
ATOM   3880 N N   . ILE   B 2 181 ? 12.69755 -12.61267 -28.15365 1.000 71.86701  ? 274 ILE   B N   1 
ATOM   3881 C CA  . ILE   B 2 181 ? 13.74447 -12.83046 -29.14453 1.000 66.23274  ? 274 ILE   B CA  1 
ATOM   3882 C C   . ILE   B 2 181 ? 15.05970 -12.20199 -28.70080 1.000 67.63130  ? 274 ILE   B C   1 
ATOM   3883 O O   . ILE   B 2 181 ? 16.13013 -12.62469 -29.15421 1.000 64.26116  ? 274 ILE   B O   1 
ATOM   3884 C CB  . ILE   B 2 181 ? 13.30374 -12.30550 -30.52717 1.000 73.88522  ? 274 ILE   B CB  1 
ATOM   3885 C CG1 . ILE   B 2 181 ? 13.99571 -10.98394 -30.87124 1.000 67.03230  ? 274 ILE   B CG1 1 
ATOM   3886 C CG2 . ILE   B 2 181 ? 11.78986 -12.14859 -30.58336 1.000 88.55606  ? 274 ILE   B CG2 1 
ATOM   3887 C CD1 . ILE   B 2 181 ? 15.07966 -11.11772 -31.92666 1.000 78.36740  ? 274 ILE   B CD1 1 
ATOM   3888 N N   . PHE   B 2 182 ? 15.00976 -11.20779 -27.81107 1.000 65.23578  ? 275 PHE   B N   1 
ATOM   3889 C CA  . PHE   B 2 182 ? 16.23771 -10.61603 -27.28995 1.000 61.65188  ? 275 PHE   B CA  1 
ATOM   3890 C C   . PHE   B 2 182 ? 17.01420 -11.62231 -26.44940 1.000 62.48319  ? 275 PHE   B C   1 
ATOM   3891 O O   . PHE   B 2 182 ? 18.22635 -11.79274 -26.62495 1.000 58.34117  ? 275 PHE   B O   1 
ATOM   3892 C CB  . PHE   B 2 182 ? 15.90961 -9.36517  -26.47142 1.000 59.01332  ? 275 PHE   B CB  1 
ATOM   3893 C CG  . PHE   B 2 182 ? 17.09605 -8.77355  -25.75958 1.000 57.96399  ? 275 PHE   B CG  1 
ATOM   3894 C CD1 . PHE   B 2 182 ? 17.93348 -7.87937  -26.40597 1.000 62.55291  ? 275 PHE   B CD1 1 
ATOM   3895 C CD2 . PHE   B 2 182 ? 17.36775 -9.10373  -24.44026 1.000 60.87600  ? 275 PHE   B CD2 1 
ATOM   3896 C CE1 . PHE   B 2 182 ? 19.02363 -7.33081  -25.75314 1.000 53.39916  ? 275 PHE   B CE1 1 
ATOM   3897 C CE2 . PHE   B 2 182 ? 18.45642 -8.56047  -23.78321 1.000 57.58139  ? 275 PHE   B CE2 1 
ATOM   3898 C CZ  . PHE   B 2 182 ? 19.28503 -7.67186  -24.44085 1.000 57.24718  ? 275 PHE   B CZ  1 
ATOM   3899 N N   . ILE   B 2 183 ? 16.32786 -12.30263 -25.52671 1.000 63.29969  ? 276 ILE   B N   1 
ATOM   3900 C CA  . ILE   B 2 183 ? 17.00245 -13.25662 -24.65501 1.000 69.14005  ? 276 ILE   B CA  1 
ATOM   3901 C C   . ILE   B 2 183 ? 17.46917 -14.48666 -25.42169 1.000 67.67070  ? 276 ILE   B C   1 
ATOM   3902 O O   . ILE   B 2 183 ? 18.34225 -15.21749 -24.93975 1.000 73.88183  ? 276 ILE   B O   1 
ATOM   3903 C CB  . ILE   B 2 183 ? 16.08782 -13.65252 -23.47871 1.000 69.87903  ? 276 ILE   B CB  1 
ATOM   3904 C CG1 . ILE   B 2 183 ? 14.91091 -14.50253 -23.96197 1.000 77.60400  ? 276 ILE   B CG1 1 
ATOM   3905 C CG2 . ILE   B 2 183 ? 15.57962 -12.41161 -22.75988 1.000 59.11547  ? 276 ILE   B CG2 1 
ATOM   3906 C CD1 . ILE   B 2 183 ? 15.00087 -15.96352 -23.56735 1.000 72.55565  ? 276 ILE   B CD1 1 
ATOM   3907 N N   . GLN   B 2 184 ? 16.91181 -14.73649 -26.60911 1.000 68.37454  ? 277 GLN   B N   1 
ATOM   3908 C CA  . GLN   B 2 184 ? 17.38293 -15.85216 -27.42285 1.000 73.18673  ? 277 GLN   B CA  1 
ATOM   3909 C C   . GLN   B 2 184 ? 18.73765 -15.54353 -28.04693 1.000 67.93312  ? 277 GLN   B C   1 
ATOM   3910 O O   . GLN   B 2 184 ? 19.62414 -16.40495 -28.07724 1.000 70.26775  ? 277 GLN   B O   1 
ATOM   3911 C CB  . GLN   B 2 184 ? 16.35583 -16.18612 -28.50472 1.000 79.47680  ? 277 GLN   B CB  1 
ATOM   3912 C CG  . GLN   B 2 184 ? 15.02138 -16.66966 -27.96389 1.000 80.18630  ? 277 GLN   B CG  1 
ATOM   3913 C CD  . GLN   B 2 184 ? 14.01721 -16.96315 -29.06191 1.000 92.67580  ? 277 GLN   B CD  1 
ATOM   3914 O OE1 . GLN   B 2 184 ? 14.29364 -16.75760 -30.24403 1.000 103.94322 ? 277 GLN   B OE1 1 
ATOM   3915 N NE2 . GLN   B 2 184 ? 12.84264 -17.44720 -28.67515 1.000 78.57605  ? 277 GLN   B NE2 1 
ATOM   3916 N N   . ILE   B 2 185 ? 18.91682 -14.32075 -28.55057 1.000 64.18346  ? 278 ILE   B N   1 
ATOM   3917 C CA  . ILE   B 2 185 ? 20.20391 -13.93808 -29.12148 1.000 63.94889  ? 278 ILE   B CA  1 
ATOM   3918 C C   . ILE   B 2 185 ? 21.25390 -13.80727 -28.02585 1.000 66.61503  ? 278 ILE   B C   1 
ATOM   3919 O O   . ILE   B 2 185 ? 22.40643 -14.22278 -28.19796 1.000 63.49419  ? 278 ILE   B O   1 
ATOM   3920 C CB  . ILE   B 2 185 ? 20.06314 -12.63777 -29.93270 1.000 62.44943  ? 278 ILE   B CB  1 
ATOM   3921 C CG1 . ILE   B 2 185 ? 19.00001 -12.80151 -31.01991 1.000 68.64793  ? 278 ILE   B CG1 1 
ATOM   3922 C CG2 . ILE   B 2 185 ? 21.39678 -12.24781 -30.54897 1.000 64.61800  ? 278 ILE   B CG2 1 
ATOM   3923 C CD1 . ILE   B 2 185 ? 18.76494 -11.54911 -31.83312 1.000 63.76115  ? 278 ILE   B CD1 1 
ATOM   3924 N N   . ALA   B 2 186 ? 20.87543 -13.22950 -26.88248 1.000 63.40053  ? 279 ALA   B N   1 
ATOM   3925 C CA  . ALA   B 2 186 ? 21.79686 -13.15327 -25.75429 1.000 61.22897  ? 279 ALA   B CA  1 
ATOM   3926 C C   . ALA   B 2 186 ? 22.20523 -14.53936 -25.27578 1.000 64.03799  ? 279 ALA   B C   1 
ATOM   3927 O O   . ALA   B 2 186 ? 23.32378 -14.72169 -24.78127 1.000 68.88111  ? 279 ALA   B O   1 
ATOM   3928 C CB  . ALA   B 2 186 ? 21.16436 -12.35903 -24.61144 1.000 58.71550  ? 279 ALA   B CB  1 
ATOM   3929 N N   . GLU   B 2 187 ? 21.31577 -15.52512 -25.41781 1.000 65.27240  ? 280 GLU   B N   1 
ATOM   3930 C CA  . GLU   B 2 187 ? 21.65742 -16.89561 -25.05302 1.000 71.42079  ? 280 GLU   B CA  1 
ATOM   3931 C C   . GLU   B 2 187 ? 22.79096 -17.42735 -25.92128 1.000 76.65406  ? 280 GLU   B C   1 
ATOM   3932 O O   . GLU   B 2 187 ? 23.66725 -18.15345 -25.43724 1.000 66.69647  ? 280 GLU   B O   1 
ATOM   3933 C CB  . GLU   B 2 187 ? 20.41935 -17.78448 -25.17098 1.000 79.18548  ? 280 GLU   B CB  1 
ATOM   3934 C CG  . GLU   B 2 187 ? 20.62629 -19.22534 -24.74465 1.000 79.65286  ? 280 GLU   B CG  1 
ATOM   3935 C CD  . GLU   B 2 187 ? 19.36660 -20.05588 -24.89701 1.000 107.09703 ? 280 GLU   B CD  1 
ATOM   3936 O OE1 . GLU   B 2 187 ? 18.41679 -19.58196 -25.55531 1.000 103.45533 ? 280 GLU   B OE1 1 
ATOM   3937 O OE2 . GLU   B 2 187 ? 19.32292 -21.17992 -24.35641 1.000 118.02506 ? 280 GLU   B OE2 1 
ATOM   3938 N N   . LEU   B 2 188 ? 22.79282 -17.07310 -27.20884 1.000 73.19069  ? 281 LEU   B N   1 
ATOM   3939 C CA  . LEU   B 2 188 ? 23.89174 -17.47353 -28.08140 1.000 70.34940  ? 281 LEU   B CA  1 
ATOM   3940 C C   . LEU   B 2 188 ? 25.17849 -16.74543 -27.71446 1.000 70.68159  ? 281 LEU   B C   1 
ATOM   3941 O O   . LEU   B 2 188 ? 26.25988 -17.34527 -27.71392 1.000 71.40384  ? 281 LEU   B O   1 
ATOM   3942 C CB  . LEU   B 2 188 ? 23.52533 -17.21395 -29.54273 1.000 70.94310  ? 281 LEU   B CB  1 
ATOM   3943 C CG  . LEU   B 2 188 ? 24.62737 -17.47156 -30.57341 1.000 73.17182  ? 281 LEU   B CG  1 
ATOM   3944 C CD1 . LEU   B 2 188 ? 25.11601 -18.90934 -30.49161 1.000 72.48647  ? 281 LEU   B CD1 1 
ATOM   3945 C CD2 . LEU   B 2 188 ? 24.14422 -17.14476 -31.97986 1.000 75.12485  ? 281 LEU   B CD2 1 
ATOM   3946 N N   . LEU   B 2 189 ? 25.08212 -15.45252 -27.39609 1.000 61.93493  ? 282 LEU   B N   1 
ATOM   3947 C CA  . LEU   B 2 189 ? 26.27088 -14.69757 -27.01705 1.000 64.95147  ? 282 LEU   B CA  1 
ATOM   3948 C C   . LEU   B 2 189 ? 26.82936 -15.16094 -25.67847 1.000 64.96124  ? 282 LEU   B C   1 
ATOM   3949 O O   . LEU   B 2 189 ? 28.04969 -15.14440 -25.48133 1.000 70.73494  ? 282 LEU   B O   1 
ATOM   3950 C CB  . LEU   B 2 189 ? 25.95226 -13.20391 -26.97497 1.000 62.93827  ? 282 LEU   B CB  1 
ATOM   3951 C CG  . LEU   B 2 189 ? 25.71584 -12.54744 -28.33551 1.000 65.46099  ? 282 LEU   B CG  1 
ATOM   3952 C CD1 . LEU   B 2 189 ? 25.16044 -11.14381 -28.16637 1.000 56.93801  ? 282 LEU   B CD1 1 
ATOM   3953 C CD2 . LEU   B 2 189 ? 27.00800 -12.52376 -29.13975 1.000 58.06199  ? 282 LEU   B CD2 1 
ATOM   3954 N N   . ASP   B 2 190 ? 25.96008 -15.57330 -24.75093 1.000 68.11103  ? 283 ASP   B N   1 
ATOM   3955 C CA  . ASP   B 2 190 ? 26.43526 -16.09736 -23.47404 1.000 69.12128  ? 283 ASP   B CA  1 
ATOM   3956 C C   . ASP   B 2 190 ? 27.27288 -17.35465 -23.66271 1.000 79.65239  ? 283 ASP   B C   1 
ATOM   3957 O O   . ASP   B 2 190 ? 28.20361 -17.60315 -22.88816 1.000 86.20126  ? 283 ASP   B O   1 
ATOM   3958 C CB  . ASP   B 2 190 ? 25.25316 -16.38308 -22.54664 1.000 69.58738  ? 283 ASP   B CB  1 
ATOM   3959 C CG  . ASP   B 2 190 ? 24.64100 -15.11963 -21.97307 1.000 79.61723  ? 283 ASP   B CG  1 
ATOM   3960 O OD1 . ASP   B 2 190 ? 25.25207 -14.03977 -22.11842 1.000 66.50777  ? 283 ASP   B OD1 1 
ATOM   3961 O OD2 . ASP   B 2 190 ? 23.54618 -15.20723 -21.37765 1.000 80.05519  ? 283 ASP   B OD2 1 
ATOM   3962 N N   . LEU   B 2 191 ? 26.96134 -18.15740 -24.68094 1.000 73.62555  ? 284 LEU   B N   1 
ATOM   3963 C CA  . LEU   B 2 191 ? 27.76449 -19.34263 -24.95913 1.000 73.56245  ? 284 LEU   B CA  1 
ATOM   3964 C C   . LEU   B 2 191 ? 29.08635 -18.96438 -25.61588 1.000 87.40277  ? 284 LEU   B C   1 
ATOM   3965 O O   . LEU   B 2 191 ? 30.15010 -19.45947 -25.22485 1.000 80.93885  ? 284 LEU   B O   1 
ATOM   3966 C CB  . LEU   B 2 191 ? 26.97865 -20.31027 -25.84459 1.000 92.58732  ? 284 LEU   B CB  1 
ATOM   3967 C CG  . LEU   B 2 191 ? 27.67585 -21.62023 -26.21737 1.000 91.74636  ? 284 LEU   B CG  1 
ATOM   3968 C CD1 . LEU   B 2 191 ? 27.98354 -22.43288 -24.97066 1.000 95.53976  ? 284 LEU   B CD1 1 
ATOM   3969 C CD2 . LEU   B 2 191 ? 26.82687 -22.42415 -27.19142 1.000 90.57139  ? 284 LEU   B CD2 1 
ATOM   3970 N N   . CYS   B 2 192 ? 29.03708 -18.07746 -26.61431 1.000 75.88382  ? 285 CYS   B N   1 
ATOM   3971 C CA  . CYS   B 2 192 ? 30.24534 -17.70284 -27.34228 1.000 74.82520  ? 285 CYS   B CA  1 
ATOM   3972 C C   . CYS   B 2 192 ? 31.24889 -16.98467 -26.45014 1.000 81.68420  ? 285 CYS   B C   1 
ATOM   3973 O O   . CYS   B 2 192 ? 32.46058 -17.09259 -26.67131 1.000 85.06851  ? 285 CYS   B O   1 
ATOM   3974 C CB  . CYS   B 2 192 ? 29.88450 -16.82343 -28.53969 1.000 86.34011  ? 285 CYS   B CB  1 
ATOM   3975 S SG  . CYS   B 2 192 ? 28.79634 -17.61022 -29.74837 1.000 91.93363  ? 285 CYS   B SG  1 
ATOM   3976 N N   . VAL   B 2 193 ? 30.77249 -16.24948 -25.44152 1.000 76.36894  ? 286 VAL   B N   1 
ATOM   3977 C CA  . VAL   B 2 193 ? 31.68508 -15.51387 -24.57494 1.000 73.11107  ? 286 VAL   B CA  1 
ATOM   3978 C C   . VAL   B 2 193 ? 32.47998 -16.45167 -23.67495 1.000 68.92103  ? 286 VAL   B C   1 
ATOM   3979 O O   . VAL   B 2 193 ? 33.53138 -16.06133 -23.15448 1.000 81.77328  ? 286 VAL   B O   1 
ATOM   3980 C CB  . VAL   B 2 193 ? 30.91642 -14.46737 -23.74294 1.000 73.11252  ? 286 VAL   B CB  1 
ATOM   3981 C CG1 . VAL   B 2 193 ? 30.22232 -15.11966 -22.55727 1.000 74.12930  ? 286 VAL   B CG1 1 
ATOM   3982 C CG2 . VAL   B 2 193 ? 31.85011 -13.35550 -23.28515 1.000 62.42914  ? 286 VAL   B CG2 1 
ATOM   3983 N N   . LEU   B 2 194 ? 32.01131 -17.68820 -23.48361 1.000 73.53023  ? 287 LEU   B N   1 
ATOM   3984 C CA  . LEU   B 2 194 ? 32.77457 -18.65139 -22.69754 1.000 74.94144  ? 287 LEU   B CA  1 
ATOM   3985 C C   . LEU   B 2 194 ? 34.02912 -19.10320 -23.43247 1.000 86.87163  ? 287 LEU   B C   1 
ATOM   3986 O O   . LEU   B 2 194 ? 35.02201 -19.46980 -22.79421 1.000 96.45295  ? 287 LEU   B O   1 
ATOM   3987 C CB  . LEU   B 2 194 ? 31.90234 -19.85665 -22.34615 1.000 75.75771  ? 287 LEU   B CB  1 
ATOM   3988 C CG  . LEU   B 2 194 ? 30.63393 -19.56869 -21.54184 1.000 76.01306  ? 287 LEU   B CG  1 
ATOM   3989 C CD1 . LEU   B 2 194 ? 29.89018 -20.85885 -21.22978 1.000 82.21523  ? 287 LEU   B CD1 1 
ATOM   3990 C CD2 . LEU   B 2 194 ? 30.96766 -18.81488 -20.26450 1.000 73.06635  ? 287 LEU   B CD2 1 
ATOM   3991 N N   . ASP   B 2 195 ? 34.00549 -19.08580 -24.76223 1.000 80.45787  ? 288 ASP   B N   1 
ATOM   3992 C CA  . ASP   B 2 195 ? 35.17355 -19.44710 -25.55561 1.000 93.66092  ? 288 ASP   B CA  1 
ATOM   3993 C C   . ASP   B 2 195 ? 36.08649 -18.23251 -25.67624 1.000 86.35586  ? 288 ASP   B C   1 
ATOM   3994 O O   . ASP   B 2 195 ? 35.65138 -17.16290 -26.11579 1.000 88.26058  ? 288 ASP   B O   1 
ATOM   3995 C CB  . ASP   B 2 195 ? 34.74306 -19.95272 -26.93226 1.000 94.72315  ? 288 ASP   B CB  1 
ATOM   3996 C CG  . ASP   B 2 195 ? 35.85287 -20.68823 -27.66612 1.000 98.79280  ? 288 ASP   B CG  1 
ATOM   3997 O OD1 . ASP   B 2 195 ? 37.02994 -20.28480 -27.54728 1.000 104.92632 ? 288 ASP   B OD1 1 
ATOM   3998 O OD2 . ASP   B 2 195 ? 35.54690 -21.67500 -28.36750 1.000 115.97583 ? 288 ASP   B OD2 1 
ATOM   3999 N N   . VAL   B 2 196 ? 37.35256 -18.39897 -25.28477 1.000 90.53125  ? 289 VAL   B N   1 
ATOM   4000 C CA  . VAL   B 2 196 ? 38.28603 -17.27884 -25.25939 1.000 98.45303  ? 289 VAL   B CA  1 
ATOM   4001 C C   . VAL   B 2 196 ? 38.61371 -16.77682 -26.65971 1.000 91.46192  ? 289 VAL   B C   1 
ATOM   4002 O O   . VAL   B 2 196 ? 39.07701 -15.64058 -26.81468 1.000 93.13031  ? 289 VAL   B O   1 
ATOM   4003 C CB  . VAL   B 2 196 ? 39.57188 -17.67825 -24.51066 1.000 105.14195 ? 289 VAL   B CB  1 
ATOM   4004 C CG1 . VAL   B 2 196 ? 40.30745 -16.44158 -24.00754 1.000 82.17174  ? 289 VAL   B CG1 1 
ATOM   4005 C CG2 . VAL   B 2 196 ? 39.24477 -18.62275 -23.36323 1.000 94.50314  ? 289 VAL   B CG2 1 
ATOM   4006 N N   . ASP   B 2 197 ? 38.37659 -17.58860 -27.69025 1.000 95.06678  ? 290 ASP   B N   1 
ATOM   4007 C CA  . ASP   B 2 197 ? 38.66099 -17.17989 -29.06097 1.000 98.85635  ? 290 ASP   B CA  1 
ATOM   4008 C C   . ASP   B 2 197 ? 37.69963 -16.11737 -29.58100 1.000 90.21611  ? 290 ASP   B C   1 
ATOM   4009 O O   . ASP   B 2 197 ? 37.88053 -15.65084 -30.71143 1.000 97.18529  ? 290 ASP   B O   1 
ATOM   4010 C CB  . ASP   B 2 197 ? 38.63683 -18.40054 -29.98396 1.000 95.63809  ? 290 ASP   B CB  1 
ATOM   4011 C CG  . ASP   B 2 197 ? 39.79300 -19.34975 -29.72547 1.000 106.44652 ? 290 ASP   B CG  1 
ATOM   4012 O OD1 . ASP   B 2 197 ? 40.90791 -18.86518 -29.43891 1.000 110.78382 ? 290 ASP   B OD1 1 
ATOM   4013 O OD2 . ASP   B 2 197 ? 39.58799 -20.57946 -29.80634 1.000 102.72418 ? 290 ASP   B OD2 1 
ATOM   4014 N N   . CYS   B 2 198 ? 36.69438 -15.72012 -28.79571 1.000 95.69359  ? 291 CYS   B N   1 
ATOM   4015 C CA  . CYS   B 2 198 ? 35.76545 -14.68984 -29.24887 1.000 80.18184  ? 291 CYS   B CA  1 
ATOM   4016 C C   . CYS   B 2 198 ? 36.41594 -13.31343 -29.26980 1.000 88.25132  ? 291 CYS   B C   1 
ATOM   4017 O O   . CYS   B 2 198 ? 35.98514 -12.43854 -30.03011 1.000 83.82618  ? 291 CYS   B O   1 
ATOM   4018 C CB  . CYS   B 2 198 ? 34.52438 -14.66673 -28.35708 1.000 75.59175  ? 291 CYS   B CB  1 
ATOM   4019 S SG  . CYS   B 2 198 ? 34.82807 -14.10624 -26.66570 1.000 81.68602  ? 291 CYS   B SG  1 
ATOM   4020 N N   . LEU   B 2 199 ? 37.44875 -13.10363 -28.44835 1.000 86.27946  ? 292 LEU   B N   1 
ATOM   4021 C CA  . LEU   B 2 199 ? 38.10780 -11.80439 -28.37724 1.000 87.65652  ? 292 LEU   B CA  1 
ATOM   4022 C C   . LEU   B 2 199 ? 38.81310 -11.43383 -29.67505 1.000 85.91885  ? 292 LEU   B C   1 
ATOM   4023 O O   . LEU   B 2 199 ? 39.17965 -10.26682 -29.85166 1.000 89.48519  ? 292 LEU   B O   1 
ATOM   4024 C CB  . LEU   B 2 199 ? 39.10688 -11.78432 -27.21910 1.000 89.32758  ? 292 LEU   B CB  1 
ATOM   4025 C CG  . LEU   B 2 199 ? 38.51106 -11.93708 -25.81816 1.000 85.68564  ? 292 LEU   B CG  1 
ATOM   4026 C CD1 . LEU   B 2 199 ? 39.59689 -11.86205 -24.75384 1.000 81.40928  ? 292 LEU   B CD1 1 
ATOM   4027 C CD2 . LEU   B 2 199 ? 37.44332 -10.88086 -25.57739 1.000 77.06708  ? 292 LEU   B CD2 1 
ATOM   4028 N N   . GLU   B 2 200 ? 39.01896 -12.39692 -30.57874 1.000 89.72701  ? 293 GLU   B N   1 
ATOM   4029 C CA  . GLU   B 2 200 ? 39.56677 -12.07562 -31.89257 1.000 95.75662  ? 293 GLU   B CA  1 
ATOM   4030 C C   . GLU   B 2 200 ? 38.67470 -11.09453 -32.64065 1.000 94.04745  ? 293 GLU   B C   1 
ATOM   4031 O O   . GLU   B 2 200 ? 39.17166 -10.25257 -33.39823 1.000 95.49994  ? 293 GLU   B O   1 
ATOM   4032 C CB  . GLU   B 2 200 ? 39.75169 -13.35587 -32.70991 1.000 95.06227  ? 293 GLU   B CB  1 
ATOM   4033 C CG  . GLU   B 2 200 ? 40.22171 -13.13080 -34.13942 1.000 109.53174 ? 293 GLU   B CG  1 
ATOM   4034 C CD  . GLU   B 2 200 ? 40.18913 -14.39880 -34.97124 1.000 107.74326 ? 293 GLU   B CD  1 
ATOM   4035 O OE1 . GLU   B 2 200 ? 40.00862 -15.48870 -34.38896 1.000 111.19077 ? 293 GLU   B OE1 1 
ATOM   4036 O OE2 . GLU   B 2 200 ? 40.33902 -14.30528 -36.20790 1.000 114.12550 ? 293 GLU   B OE2 1 
ATOM   4037 N N   . PHE   B 2 201 ? 37.36425 -11.17665 -32.43147 1.000 81.86180  ? 294 PHE   B N   1 
ATOM   4038 C CA  . PHE   B 2 201 ? 36.40828 -10.30668 -33.09663 1.000 81.88925  ? 294 PHE   B CA  1 
ATOM   4039 C C   . PHE   B 2 201 ? 35.92832 -9.21510  -32.14990 1.000 81.20790  ? 294 PHE   B C   1 
ATOM   4040 O O   . PHE   B 2 201 ? 35.73827 -9.46953  -30.95457 1.000 70.08911  ? 294 PHE   B O   1 
ATOM   4041 C CB  . PHE   B 2 201 ? 35.20672 -11.11038 -33.59395 1.000 82.45668  ? 294 PHE   B CB  1 
ATOM   4042 C CG  . PHE   B 2 201 ? 35.57650 -12.42525 -34.21617 1.000 80.85637  ? 294 PHE   B CG  1 
ATOM   4043 C CD1 . PHE   B 2 201 ? 36.08946 -12.47912 -35.50105 1.000 77.36778  ? 294 PHE   B CD1 1 
ATOM   4044 C CD2 . PHE   B 2 201 ? 35.41268 -13.60836 -33.51446 1.000 78.05976  ? 294 PHE   B CD2 1 
ATOM   4045 C CE1 . PHE   B 2 201 ? 36.43241 -13.68856 -36.07506 1.000 88.29194  ? 294 PHE   B CE1 1 
ATOM   4046 C CE2 . PHE   B 2 201 ? 35.75321 -14.82165 -34.08391 1.000 87.03860  ? 294 PHE   B CE2 1 
ATOM   4047 C CZ  . PHE   B 2 201 ? 36.26358 -14.86112 -35.36553 1.000 83.88383  ? 294 PHE   B CZ  1 
ATOM   4048 N N   . PRO   B 2 202 ? 35.74169 -7.99670  -32.65557 1.000 74.82749  ? 295 PRO   B N   1 
ATOM   4049 C CA  . PRO   B 2 202 ? 35.22007 -6.91853  -31.80973 1.000 66.09203  ? 295 PRO   B CA  1 
ATOM   4050 C C   . PRO   B 2 202 ? 33.84615 -7.26157  -31.25509 1.000 75.93215  ? 295 PRO   B C   1 
ATOM   4051 O O   . PRO   B 2 202 ? 33.10014 -8.06664  -31.81703 1.000 61.65722  ? 295 PRO   B O   1 
ATOM   4052 C CB  . PRO   B 2 202 ? 35.15347 -5.71712  -32.76089 1.000 70.27390  ? 295 PRO   B CB  1 
ATOM   4053 C CG  . PRO   B 2 202 ? 36.13016 -6.03656  -33.84447 1.000 77.16194  ? 295 PRO   B CG  1 
ATOM   4054 C CD  . PRO   B 2 202 ? 36.08108 -7.52686  -34.00890 1.000 71.23355  ? 295 PRO   B CD  1 
ATOM   4055 N N   . TYR   B 2 203 ? 33.52153 -6.63034  -30.12332 1.000 64.57182  ? 296 TYR   B N   1 
ATOM   4056 C CA  . TYR   B 2 203 ? 32.25213 -6.90227  -29.45564 1.000 63.09245  ? 296 TYR   B CA  1 
ATOM   4057 C C   . TYR   B 2 203 ? 31.06684 -6.60053  -30.36495 1.000 52.87446  ? 296 TYR   B C   1 
ATOM   4058 O O   . TYR   B 2 203 ? 30.08646 -7.35459  -30.38940 1.000 61.92168  ? 296 TYR   B O   1 
ATOM   4059 C CB  . TYR   B 2 203 ? 32.15436 -6.09043  -28.16351 1.000 58.20946  ? 296 TYR   B CB  1 
ATOM   4060 C CG  . TYR   B 2 203 ? 33.05297 -6.57741  -27.04631 1.000 61.92189  ? 296 TYR   B CG  1 
ATOM   4061 C CD1 . TYR   B 2 203 ? 33.72728 -7.78901  -27.14284 1.000 58.07382  ? 296 TYR   B CD1 1 
ATOM   4062 C CD2 . TYR   B 2 203 ? 33.21712 -5.82851  -25.88870 1.000 60.67644  ? 296 TYR   B CD2 1 
ATOM   4063 C CE1 . TYR   B 2 203 ? 34.54430 -8.23646  -26.11882 1.000 65.36267  ? 296 TYR   B CE1 1 
ATOM   4064 C CE2 . TYR   B 2 203 ? 34.02985 -6.26690  -24.86179 1.000 64.40948  ? 296 TYR   B CE2 1 
ATOM   4065 C CZ  . TYR   B 2 203 ? 34.69110 -7.46992  -24.98099 1.000 69.19822  ? 296 TYR   B CZ  1 
ATOM   4066 O OH  . TYR   B 2 203 ? 35.50061 -7.90462  -23.95635 1.000 65.09506  ? 296 TYR   B OH  1 
ATOM   4067 N N   . GLY   B 2 204 ? 31.13556 -5.49986  -31.11738 1.000 63.98628  ? 297 GLY   B N   1 
ATOM   4068 C CA  . GLY   B 2 204 ? 30.05847 -5.17610  -32.03750 1.000 61.63290  ? 297 GLY   B CA  1 
ATOM   4069 C C   . GLY   B 2 204 ? 29.89753 -6.19559  -33.14702 1.000 67.76381  ? 297 GLY   B C   1 
ATOM   4070 O O   . GLY   B 2 204 ? 28.78919 -6.40519  -33.64824 1.000 61.81242  ? 297 GLY   B O   1 
ATOM   4071 N N   . ILE   B 2 205 ? 30.99375 -6.84346  -33.54538 1.000 67.25498  ? 298 ILE   B N   1 
ATOM   4072 C CA  . ILE   B 2 205 ? 30.91366 -7.87875  -34.57014 1.000 62.69167  ? 298 ILE   B CA  1 
ATOM   4073 C C   . ILE   B 2 205 ? 30.25598 -9.13395  -34.01038 1.000 64.56430  ? 298 ILE   B C   1 
ATOM   4074 O O   . ILE   B 2 205 ? 29.42560 -9.76582  -34.67538 1.000 63.79173  ? 298 ILE   B O   1 
ATOM   4075 C CB  . ILE   B 2 205 ? 32.31471 -8.17577  -35.13535 1.000 74.12757  ? 298 ILE   B CB  1 
ATOM   4076 C CG1 . ILE   B 2 205 ? 32.89628 -6.93132  -35.80723 1.000 86.51455  ? 298 ILE   B CG1 1 
ATOM   4077 C CG2 . ILE   B 2 205 ? 32.25854 -9.32337  -36.12194 1.000 66.36234  ? 298 ILE   B CG2 1 
ATOM   4078 C CD1 . ILE   B 2 205 ? 32.18465 -6.54085  -37.08115 1.000 84.61037  ? 298 ILE   B CD1 1 
ATOM   4079 N N   . LEU   B 2 206 ? 30.61285 -9.51231  -32.78005 1.000 62.90937  ? 299 LEU   B N   1 
ATOM   4080 C CA  . LEU   B 2 206 ? 30.04055 -10.70718 -32.16586 1.000 64.60755  ? 299 LEU   B CA  1 
ATOM   4081 C C   . LEU   B 2 206 ? 28.53008 -10.57871 -32.01077 1.000 63.00981  ? 299 LEU   B C   1 
ATOM   4082 O O   . LEU   B 2 206 ? 27.78157 -11.51750 -32.30674 1.000 65.21286  ? 299 LEU   B O   1 
ATOM   4083 C CB  . LEU   B 2 206 ? 30.69834 -10.96225 -30.80867 1.000 58.80283  ? 299 LEU   B CB  1 
ATOM   4084 C CG  . LEU   B 2 206 ? 32.17837 -11.34752 -30.81075 1.000 63.86869  ? 299 LEU   B CG  1 
ATOM   4085 C CD1 . LEU   B 2 206 ? 32.74363 -11.29775 -29.40037 1.000 79.73190  ? 299 LEU   B CD1 1 
ATOM   4086 C CD2 . LEU   B 2 206 ? 32.36666 -12.72986 -31.41215 1.000 67.00423  ? 299 LEU   B CD2 1 
ATOM   4087 N N   . ALA   B 2 207 ? 28.06334 -9.41913  -31.54037 1.000 54.91948  ? 300 ALA   B N   1 
ATOM   4088 C CA  . ALA   B 2 207 ? 26.62836 -9.21741  -31.36836 1.000 62.78039  ? 300 ALA   B CA  1 
ATOM   4089 C C   . ALA   B 2 207 ? 25.90392 -9.23830  -32.70826 1.000 53.65312  ? 300 ALA   B C   1 
ATOM   4090 O O   . ALA   B 2 207 ? 24.80457 -9.79393  -32.81993 1.000 60.28329  ? 300 ALA   B O   1 
ATOM   4091 C CB  . ALA   B 2 207 ? 26.36621 -7.90231  -30.63492 1.000 52.49590  ? 300 ALA   B CB  1 
ATOM   4092 N N   . ALA   B 2 208 ? 26.50749 -8.64286  -33.73973 1.000 54.78253  ? 301 ALA   B N   1 
ATOM   4093 C CA  . ALA   B 2 208 ? 25.88466 -8.64491  -35.05965 1.000 65.74767  ? 301 ALA   B CA  1 
ATOM   4094 C C   . ALA   B 2 208 ? 25.85562 -10.04593 -35.65651 1.000 65.14833  ? 301 ALA   B C   1 
ATOM   4095 O O   . ALA   B 2 208 ? 24.89648 -10.41276 -36.34604 1.000 60.64982  ? 301 ALA   B O   1 
ATOM   4096 C CB  . ALA   B 2 208 ? 26.61923 -7.68011  -35.98960 1.000 58.78228  ? 301 ALA   B CB  1 
ATOM   4097 N N   . SER   B 2 209 ? 26.89601 -10.84376 -35.40254 1.000 61.34832  ? 302 SER   B N   1 
ATOM   4098 C CA  . SER   B 2 209 ? 26.93024 -12.20117 -35.93719 1.000 60.06721  ? 302 SER   B CA  1 
ATOM   4099 C C   . SER   B 2 209 ? 25.89243 -13.08757 -35.26018 1.000 66.83164  ? 302 SER   B C   1 
ATOM   4100 O O   . SER   B 2 209 ? 25.30412 -13.96516 -35.90270 1.000 68.57818  ? 302 SER   B O   1 
ATOM   4101 C CB  . SER   B 2 209 ? 28.33032 -12.79259 -35.77935 1.000 72.68677  ? 302 SER   B CB  1 
ATOM   4102 O OG  . SER   B 2 209 ? 29.29296 -12.01134 -36.46613 1.000 73.07632  ? 302 SER   B OG  1 
ATOM   4103 N N   . ALA   B 2 210 ? 25.65572 -12.87696 -33.96287 1.000 59.38357  ? 303 ALA   B N   1 
ATOM   4104 C CA  . ALA   B 2 210 ? 24.61520 -13.63372 -33.27467 1.000 63.11060  ? 303 ALA   B CA  1 
ATOM   4105 C C   . ALA   B 2 210 ? 23.23101 -13.24595 -33.77733 1.000 65.96547  ? 303 ALA   B C   1 
ATOM   4106 O O   . ALA   B 2 210 ? 22.36088 -14.10850 -33.94586 1.000 60.26387  ? 303 ALA   B O   1 
ATOM   4107 C CB  . ALA   B 2 210 ? 24.71828 -13.41949 -31.76623 1.000 61.56372  ? 303 ALA   B CB  1 
ATOM   4108 N N   . LEU   B 2 211 ? 23.00964 -11.95183 -34.02071 1.000 61.51084  ? 304 LEU   B N   1 
ATOM   4109 C CA  . LEU   B 2 211 ? 21.73541 -11.50929 -34.57729 1.000 68.20204  ? 304 LEU   B CA  1 
ATOM   4110 C C   . LEU   B 2 211 ? 21.50953 -12.09075 -35.96688 1.000 58.54864  ? 304 LEU   B C   1 
ATOM   4111 O O   . LEU   B 2 211 ? 20.37734 -12.43284 -36.32895 1.000 62.98831  ? 304 LEU   B O   1 
ATOM   4112 C CB  . LEU   B 2 211 ? 21.68710 -9.98274  -34.62305 1.000 75.48716  ? 304 LEU   B CB  1 
ATOM   4113 C CG  . LEU   B 2 211 ? 20.42034 -9.36888  -35.22267 1.000 66.86662  ? 304 LEU   B CG  1 
ATOM   4114 C CD1 . LEU   B 2 211 ? 19.55848 -8.74399  -34.13785 1.000 72.10434  ? 304 LEU   B CD1 1 
ATOM   4115 C CD2 . LEU   B 2 211 ? 20.76970 -8.35026  -36.29382 1.000 75.31642  ? 304 LEU   B CD2 1 
ATOM   4116 N N   . TYR   B 2 212 ? 22.57842 -12.21478 -36.75780 1.000 68.92962  ? 305 TYR   B N   1 
ATOM   4117 C CA  . TYR   B 2 212 ? 22.44564 -12.76191 -38.10444 1.000 66.07012  ? 305 TYR   B CA  1 
ATOM   4118 C C   . TYR   B 2 212 ? 21.93239 -14.19577 -38.07449 1.000 67.64702  ? 305 TYR   B C   1 
ATOM   4119 O O   . TYR   B 2 212 ? 21.08760 -14.57723 -38.89312 1.000 68.34805  ? 305 TYR   B O   1 
ATOM   4120 C CB  . TYR   B 2 212 ? 23.78623 -12.69122 -38.83616 1.000 60.65476  ? 305 TYR   B CB  1 
ATOM   4121 C CG  . TYR   B 2 212 ? 23.85701 -13.58879 -40.05112 1.000 66.10486  ? 305 TYR   B CG  1 
ATOM   4122 C CD1 . TYR   B 2 212 ? 23.24266 -13.22639 -41.24149 1.000 71.08967  ? 305 TYR   B CD1 1 
ATOM   4123 C CD2 . TYR   B 2 212 ? 24.53543 -14.80034 -40.00626 1.000 68.68866  ? 305 TYR   B CD2 1 
ATOM   4124 C CE1 . TYR   B 2 212 ? 23.30071 -14.04403 -42.35383 1.000 72.74514  ? 305 TYR   B CE1 1 
ATOM   4125 C CE2 . TYR   B 2 212 ? 24.59887 -15.62541 -41.11384 1.000 85.68580  ? 305 TYR   B CE2 1 
ATOM   4126 C CZ  . TYR   B 2 212 ? 23.97983 -15.24206 -42.28440 1.000 80.57929  ? 305 TYR   B CZ  1 
ATOM   4127 O OH  . TYR   B 2 212 ? 24.04166 -16.05898 -43.39001 1.000 85.68831  ? 305 TYR   B OH  1 
ATOM   4128 N N   . HIS   B 2 213 ? 22.43017 -15.00652 -37.13746 1.000 67.46590  ? 306 HIS   B N   1 
ATOM   4129 C CA  . HIS   B 2 213 ? 22.01301 -16.40198 -37.06633 1.000 74.05772  ? 306 HIS   B CA  1 
ATOM   4130 C C   . HIS   B 2 213 ? 20.54980 -16.55532 -36.67413 1.000 64.59047  ? 306 HIS   B C   1 
ATOM   4131 O O   . HIS   B 2 213 ? 19.96005 -17.60868 -36.93647 1.000 77.53193  ? 306 HIS   B O   1 
ATOM   4132 C CB  . HIS   B 2 213 ? 22.90269 -17.16882 -36.08714 1.000 75.34149  ? 306 HIS   B CB  1 
ATOM   4133 C CG  . HIS   B 2 213 ? 24.27298 -17.45461 -36.61750 1.000 82.17147  ? 306 HIS   B CG  1 
ATOM   4134 N ND1 . HIS   B 2 213 ? 25.34733 -16.62018 -36.39583 1.000 75.01006  ? 306 HIS   B ND1 1 
ATOM   4135 C CD2 . HIS   B 2 213 ? 24.74065 -18.47815 -37.37085 1.000 77.65460  ? 306 HIS   B CD2 1 
ATOM   4136 C CE1 . HIS   B 2 213 ? 26.41933 -17.12124 -36.98348 1.000 83.09514  ? 306 HIS   B CE1 1 
ATOM   4137 N NE2 . HIS   B 2 213 ? 26.07811 -18.24801 -37.58250 1.000 86.55408  ? 306 HIS   B NE2 1 
ATOM   4138 N N   . PHE   B 2 214 ? 19.95278 -15.53825 -36.05738 1.000 69.06765  ? 307 PHE   B N   1 
ATOM   4139 C CA  . PHE   B 2 214 ? 18.53438 -15.55125 -35.73062 1.000 70.82283  ? 307 PHE   B CA  1 
ATOM   4140 C C   . PHE   B 2 214 ? 17.70084 -14.71560 -36.69154 1.000 81.50623  ? 307 PHE   B C   1 
ATOM   4141 O O   . PHE   B 2 214 ? 16.49117 -14.57980 -36.48383 1.000 81.51232  ? 307 PHE   B O   1 
ATOM   4142 C CB  . PHE   B 2 214 ? 18.31498 -15.06073 -34.29529 1.000 67.99757  ? 307 PHE   B CB  1 
ATOM   4143 C CG  . PHE   B 2 214 ? 18.79944 -16.02041 -33.24656 1.000 62.31451  ? 307 PHE   B CG  1 
ATOM   4144 C CD1 . PHE   B 2 214 ? 20.10239 -15.96079 -32.78305 1.000 71.54731  ? 307 PHE   B CD1 1 
ATOM   4145 C CD2 . PHE   B 2 214 ? 17.95109 -16.98333 -32.72429 1.000 68.05064  ? 307 PHE   B CD2 1 
ATOM   4146 C CE1 . PHE   B 2 214 ? 20.55153 -16.84290 -31.81839 1.000 68.12727  ? 307 PHE   B CE1 1 
ATOM   4147 C CE2 . PHE   B 2 214 ? 18.39428 -17.86812 -31.75889 1.000 72.24001  ? 307 PHE   B CE2 1 
ATOM   4148 C CZ  . PHE   B 2 214 ? 19.69629 -17.79756 -31.30606 1.000 66.26433  ? 307 PHE   B CZ  1 
ATOM   4149 N N   . SER   B 2 215 ? 18.31291 -14.15757 -37.73564 1.000 77.20770  ? 308 SER   B N   1 
ATOM   4150 C CA  . SER   B 2 215 ? 17.58484 -13.33851 -38.69601 1.000 60.87871  ? 308 SER   B CA  1 
ATOM   4151 C C   . SER   B 2 215 ? 18.16384 -13.49169 -40.09683 1.000 62.21085  ? 308 SER   B C   1 
ATOM   4152 O O   . SER   B 2 215 ? 18.02684 -14.55000 -40.71887 1.000 66.42197  ? 308 SER   B O   1 
ATOM   4153 C CB  . SER   B 2 215 ? 17.60608 -11.87001 -38.26892 1.000 58.59155  ? 308 SER   B CB  1 
ATOM   4154 O OG  . SER   B 2 215 ? 18.93337 -11.38496 -38.17076 1.000 68.12362  ? 308 SER   B OG  1 
ATOM   4155 N N   . SER   B 2 216 ? 18.81291 -12.44465 -40.59948 1.000 61.82576  ? 309 SER   B N   1 
ATOM   4156 C CA  . SER   B 2 216 ? 19.33667 -12.45290 -41.95841 1.000 76.59545  ? 309 SER   B CA  1 
ATOM   4157 C C   . SER   B 2 216 ? 20.46561 -11.43763 -42.05884 1.000 64.96683  ? 309 SER   B C   1 
ATOM   4158 O O   . SER   B 2 216 ? 20.66125 -10.60290 -41.17244 1.000 64.34348  ? 309 SER   B O   1 
ATOM   4159 C CB  . SER   B 2 216 ? 18.23767 -12.14514 -42.97985 1.000 65.23650  ? 309 SER   B CB  1 
ATOM   4160 O OG  . SER   B 2 216 ? 17.69536 -10.85399 -42.76014 1.000 66.29312  ? 309 SER   B OG  1 
ATOM   4161 N N   . SER   B 2 217 ? 21.20997 -11.52167 -43.16457 1.000 72.41997  ? 310 SER   B N   1 
ATOM   4162 C CA  . SER   B 2 217 ? 22.27551 -10.55688 -43.41205 1.000 70.63430  ? 310 SER   B CA  1 
ATOM   4163 C C   . SER   B 2 217 ? 21.71670 -9.18025  -43.74438 1.000 73.06555  ? 310 SER   B C   1 
ATOM   4164 O O   . SER   B 2 217 ? 22.37021 -8.16580  -43.47510 1.000 75.97044  ? 310 SER   B O   1 
ATOM   4165 C CB  . SER   B 2 217 ? 23.18080 -11.05110 -44.54063 1.000 88.95698  ? 310 SER   B CB  1 
ATOM   4166 O OG  . SER   B 2 217 ? 22.43821 -11.28398 -45.72547 1.000 83.08117  ? 310 SER   B OG  1 
ATOM   4167 N N   . GLU   B 2 218 ? 20.51641 -9.12386  -44.32515 1.000 77.75345  ? 311 GLU   B N   1 
ATOM   4168 C CA  . GLU   B 2 218 ? 19.90051 -7.83710  -44.63231 1.000 78.28596  ? 311 GLU   B CA  1 
ATOM   4169 C C   . GLU   B 2 218 ? 19.51799 -7.09668  -43.35688 1.000 62.07738  ? 311 GLU   B C   1 
ATOM   4170 O O   . GLU   B 2 218 ? 19.78989 -5.89841  -43.21697 1.000 75.32586  ? 311 GLU   B O   1 
ATOM   4171 C CB  . GLU   B 2 218 ? 18.67699 -8.03719  -45.52997 1.000 76.59025  ? 311 GLU   B CB  1 
ATOM   4172 C CG  . GLU   B 2 218 ? 18.99554 -8.50879  -46.94437 1.000 81.33338  ? 311 GLU   B CG  1 
ATOM   4173 C CD  . GLU   B 2 218 ? 19.35662 -9.98180  -47.01310 1.000 97.15651  ? 311 GLU   B CD  1 
ATOM   4174 O OE1 . GLU   B 2 218 ? 19.18676 -10.68716 -45.99633 1.000 92.44119  ? 311 GLU   B OE1 1 
ATOM   4175 O OE2 . GLU   B 2 218 ? 19.81124 -10.43479 -48.08493 1.000 107.02524 ? 311 GLU   B OE2 1 
ATOM   4176 N N   . LEU   B 2 219 ? 18.88318 -7.79514  -42.41233 1.000 69.93666  ? 312 LEU   B N   1 
ATOM   4177 C CA  . LEU   B 2 219 ? 18.54638 -7.16632  -41.13929 1.000 56.67939  ? 312 LEU   B CA  1 
ATOM   4178 C C   . LEU   B 2 219 ? 19.80012 -6.85228  -40.33435 1.000 64.29620  ? 312 LEU   B C   1 
ATOM   4179 O O   . LEU   B 2 219 ? 19.87029 -5.81591  -39.66301 1.000 59.38514  ? 312 LEU   B O   1 
ATOM   4180 C CB  . LEU   B 2 219 ? 17.60631 -8.06463  -40.33585 1.000 67.77203  ? 312 LEU   B CB  1 
ATOM   4181 C CG  . LEU   B 2 219 ? 17.15145 -7.49379  -38.99038 1.000 71.28665  ? 312 LEU   B CG  1 
ATOM   4182 C CD1 . LEU   B 2 219 ? 16.37419 -6.20229  -39.19538 1.000 84.34135  ? 312 LEU   B CD1 1 
ATOM   4183 C CD2 . LEU   B 2 219 ? 16.32300 -8.50536  -38.21373 1.000 84.57546  ? 312 LEU   B CD2 1 
ATOM   4184 N N   . MET   B 2 220 ? 20.79786 -7.73781  -40.38802 1.000 68.65468  ? 313 MET   B N   1 
ATOM   4185 C CA  . MET   B 2 220 ? 22.05741 -7.48738  -39.69416 1.000 69.06633  ? 313 MET   B CA  1 
ATOM   4186 C C   . MET   B 2 220 ? 22.70974 -6.20718  -40.19896 1.000 69.73696  ? 313 MET   B C   1 
ATOM   4187 O O   . MET   B 2 220 ? 23.11715 -5.34853  -39.40852 1.000 70.96207  ? 313 MET   B O   1 
ATOM   4188 C CB  . MET   B 2 220 ? 22.99270 -8.68665  -39.87241 1.000 69.34730  ? 313 MET   B CB  1 
ATOM   4189 C CG  . MET   B 2 220 ? 24.36305 -8.55706  -39.21257 1.000 76.16598  ? 313 MET   B CG  1 
ATOM   4190 S SD  . MET   B 2 220 ? 25.57917 -7.64840  -40.19299 1.000 72.64793  ? 313 MET   B SD  1 
ATOM   4191 C CE  . MET   B 2 220 ? 25.31312 -8.36203  -41.81552 1.000 84.08791  ? 313 MET   B CE  1 
ATOM   4192 N N   . GLN   B 2 221 ? 22.81364 -6.06226  -41.52153 1.000 73.69218  ? 314 GLN   B N   1 
ATOM   4193 C CA  . GLN   B 2 221 ? 23.43802 -4.87457  -42.09215 1.000 77.43171  ? 314 GLN   B CA  1 
ATOM   4194 C C   . GLN   B 2 221 ? 22.60316 -3.62515  -41.84304 1.000 70.93996  ? 314 GLN   B C   1 
ATOM   4195 O O   . GLN   B 2 221 ? 23.15674 -2.52787  -41.70917 1.000 79.72407  ? 314 GLN   B O   1 
ATOM   4196 C CB  . GLN   B 2 221 ? 23.66467 -5.07974  -43.59023 1.000 78.03723  ? 314 GLN   B CB  1 
ATOM   4197 C CG  . GLN   B 2 221 ? 24.49525 -3.99979  -44.25844 1.000 68.41075  ? 314 GLN   B CG  1 
ATOM   4198 C CD  . GLN   B 2 221 ? 24.85164 -4.35013  -45.68904 1.000 70.69507  ? 314 GLN   B CD  1 
ATOM   4199 O OE1 . GLN   B 2 221 ? 24.39733 -5.36208  -46.22367 1.000 76.64711  ? 314 GLN   B OE1 1 
ATOM   4200 N NE2 . GLN   B 2 221 ? 25.67221 -3.51616  -46.31600 1.000 84.28290  ? 314 GLN   B NE2 1 
ATOM   4201 N N   . LYS   B 2 222 ? 21.27853 -3.77021  -41.76793 1.000 77.25659  ? 315 LYS   B N   1 
ATOM   4202 C CA  . LYS   B 2 222 ? 20.41831 -2.61105  -41.55429 1.000 71.11042  ? 315 LYS   B CA  1 
ATOM   4203 C C   . LYS   B 2 222 ? 20.58806 -2.04124  -40.15106 1.000 73.58676  ? 315 LYS   B C   1 
ATOM   4204 O O   . LYS   B 2 222 ? 20.58601 -0.81834  -39.96837 1.000 82.68899  ? 315 LYS   B O   1 
ATOM   4205 C CB  . LYS   B 2 222 ? 18.95825 -2.99009  -41.80511 1.000 79.38492  ? 315 LYS   B CB  1 
ATOM   4206 C CG  . LYS   B 2 222 ? 17.96048 -1.89571  -41.45552 1.000 89.30705  ? 315 LYS   B CG  1 
ATOM   4207 C CD  . LYS   B 2 222 ? 16.52776 -2.39559  -41.55651 1.000 99.12751  ? 315 LYS   B CD  1 
ATOM   4208 C CE  . LYS   B 2 222 ? 15.53977 -1.33877  -41.08654 1.000 109.61994 ? 315 LYS   B CE  1 
ATOM   4209 N NZ  . LYS   B 2 222 ? 14.13569 -1.83475  -41.11572 1.000 101.90297 ? 315 LYS   B NZ  1 
ATOM   4210 N N   . VAL   B 2 223 ? 20.74452 -2.90740  -39.14970 1.000 74.14850  ? 316 VAL   B N   1 
ATOM   4211 C CA  . VAL   B 2 223 ? 20.77504 -2.46558  -37.75956 1.000 79.15370  ? 316 VAL   B CA  1 
ATOM   4212 C C   . VAL   B 2 223 ? 22.18726 -2.32962  -37.19983 1.000 70.27711  ? 316 VAL   B C   1 
ATOM   4213 O O   . VAL   B 2 223 ? 22.36051 -1.69887  -36.14509 1.000 62.78831  ? 316 VAL   B O   1 
ATOM   4214 C CB  . VAL   B 2 223 ? 19.94997 -3.41505  -36.86685 1.000 78.53735  ? 316 VAL   B CB  1 
ATOM   4215 C CG1 . VAL   B 2 223 ? 18.61162 -3.71075  -37.51485 1.000 70.34760  ? 316 VAL   B CG1 1 
ATOM   4216 C CG2 . VAL   B 2 223 ? 20.71796 -4.69924  -36.60311 1.000 58.75775  ? 316 VAL   B CG2 1 
ATOM   4217 N N   . SER   B 2 224 ? 23.19659 -2.89918  -37.86103 1.000 72.90646  ? 317 SER   B N   1 
ATOM   4218 C CA  . SER   B 2 224 ? 24.56973 -2.80923  -37.38754 1.000 74.11631  ? 317 SER   B CA  1 
ATOM   4219 C C   . SER   B 2 224 ? 25.47186 -1.97504  -38.28236 1.000 81.85037  ? 317 SER   B C   1 
ATOM   4220 O O   . SER   B 2 224 ? 26.49150 -1.47088  -37.80157 1.000 74.67472  ? 317 SER   B O   1 
ATOM   4221 C CB  . SER   B 2 224 ? 25.18196 -4.21075  -37.24383 1.000 67.27974  ? 317 SER   B CB  1 
ATOM   4222 O OG  . SER   B 2 224 ? 25.31515 -4.84098  -38.50711 1.000 76.88777  ? 317 SER   B OG  1 
ATOM   4223 N N   . GLY   B 2 225 ? 25.12650 -1.81582  -39.55945 1.000 72.20148  ? 318 GLY   B N   1 
ATOM   4224 C CA  . GLY   B 2 225 ? 25.94621 -1.07386  -40.49059 1.000 71.80133  ? 318 GLY   B CA  1 
ATOM   4225 C C   . GLY   B 2 225 ? 27.11820 -1.83613  -41.06491 1.000 94.17335  ? 318 GLY   B C   1 
ATOM   4226 O O   . GLY   B 2 225 ? 27.77982 -1.32472  -41.97766 1.000 99.60817  ? 318 GLY   B O   1 
ATOM   4227 N N   . TYR   B 2 226 ? 27.39695 -3.03921  -40.57254 1.000 79.58324  ? 319 TYR   B N   1 
ATOM   4228 C CA  . TYR   B 2 226 ? 28.53491 -3.81997  -41.03262 1.000 79.88769  ? 319 TYR   B CA  1 
ATOM   4229 C C   . TYR   B 2 226 ? 28.13574 -4.69669  -42.21234 1.000 97.09523  ? 319 TYR   B C   1 
ATOM   4230 O O   . TYR   B 2 226 ? 27.06857 -5.31790  -42.21003 1.000 83.25539  ? 319 TYR   B O   1 
ATOM   4231 C CB  . TYR   B 2 226 ? 29.08445 -4.68550  -39.89740 1.000 88.99993  ? 319 TYR   B CB  1 
ATOM   4232 C CG  . TYR   B 2 226 ? 29.48266 -3.90024  -38.66586 1.000 90.37733  ? 319 TYR   B CG  1 
ATOM   4233 C CD1 . TYR   B 2 226 ? 29.97932 -2.60680  -38.77168 1.000 92.62958  ? 319 TYR   B CD1 1 
ATOM   4234 C CD2 . TYR   B 2 226 ? 29.35447 -4.44988  -37.39679 1.000 87.72627  ? 319 TYR   B CD2 1 
ATOM   4235 C CE1 . TYR   B 2 226 ? 30.34159 -1.88511  -37.64861 1.000 91.82538  ? 319 TYR   B CE1 1 
ATOM   4236 C CE2 . TYR   B 2 226 ? 29.71515 -3.73603  -36.26765 1.000 95.89113  ? 319 TYR   B CE2 1 
ATOM   4237 C CZ  . TYR   B 2 226 ? 30.20739 -2.45462  -36.39970 1.000 83.94514  ? 319 TYR   B CZ  1 
ATOM   4238 O OH  . TYR   B 2 226 ? 30.56634 -1.74114  -35.27952 1.000 84.83247  ? 319 TYR   B OH  1 
ATOM   4239 N N   . GLN   B 2 227 ? 29.00150 -4.74066  -43.22129 1.000 86.77619  ? 320 GLN   B N   1 
ATOM   4240 C CA  . GLN   B 2 227 ? 28.74815 -5.56718  -44.38922 1.000 97.16293  ? 320 GLN   B CA  1 
ATOM   4241 C C   . GLN   B 2 227 ? 28.92131 -7.04419  -44.03941 1.000 94.14387  ? 320 GLN   B C   1 
ATOM   4242 O O   . GLN   B 2 227 ? 29.48648 -7.40535  -43.00246 1.000 99.04027  ? 320 GLN   B O   1 
ATOM   4243 C CB  . GLN   B 2 227 ? 29.68484 -5.17643  -45.53437 1.000 97.98852  ? 320 GLN   B CB  1 
ATOM   4244 C CG  . GLN   B 2 227 ? 29.18292 -5.56383  -46.91882 1.000 121.12793 ? 320 GLN   B CG  1 
ATOM   4245 C CD  . GLN   B 2 227 ? 30.17380 -5.22449  -48.01464 1.000 124.35845 ? 320 GLN   B CD  1 
ATOM   4246 O OE1 . GLN   B 2 227 ? 29.93820 -5.50634  -49.18966 1.000 122.45613 ? 320 GLN   B OE1 1 
ATOM   4247 N NE2 . GLN   B 2 227 ? 31.29119 -4.61634  -47.63449 1.000 126.07364 ? 320 GLN   B NE2 1 
ATOM   4248 N N   . TRP   B 2 228 ? 28.41325 -7.90529  -44.92510 1.000 78.93430  ? 321 TRP   B N   1 
ATOM   4249 C CA  . TRP   B 2 228 ? 28.52567 -9.34446  -44.71263 1.000 88.62891  ? 321 TRP   B CA  1 
ATOM   4250 C C   . TRP   B 2 228 ? 29.97842 -9.80065  -44.66866 1.000 100.46580 ? 321 TRP   B C   1 
ATOM   4251 O O   . TRP   B 2 228 ? 30.30832 -10.74817 -43.94603 1.000 101.18688 ? 321 TRP   B O   1 
ATOM   4252 C CB  . TRP   B 2 228 ? 27.76901 -10.09688 -45.80733 1.000 78.52009  ? 321 TRP   B CB  1 
ATOM   4253 C CG  . TRP   B 2 228 ? 28.11572 -11.54808 -45.86656 1.000 80.06783  ? 321 TRP   B CG  1 
ATOM   4254 C CD1 . TRP   B 2 228 ? 28.83736 -12.17996 -46.83653 1.000 89.75105  ? 321 TRP   B CD1 1 
ATOM   4255 C CD2 . TRP   B 2 228 ? 27.77453 -12.54978 -44.90264 1.000 78.94049  ? 321 TRP   B CD2 1 
ATOM   4256 N NE1 . TRP   B 2 228 ? 28.95740 -13.51641 -46.54168 1.000 96.67867  ? 321 TRP   B NE1 1 
ATOM   4257 C CE2 . TRP   B 2 228 ? 28.31393 -13.76859 -45.35858 1.000 89.14946  ? 321 TRP   B CE2 1 
ATOM   4258 C CE3 . TRP   B 2 228 ? 27.06087 -12.53527 -43.70058 1.000 75.84057  ? 321 TRP   B CE3 1 
ATOM   4259 C CZ2 . TRP   B 2 228 ? 28.16193 -14.96059 -44.65532 1.000 87.70957  ? 321 TRP   B CZ2 1 
ATOM   4260 C CZ3 . TRP   B 2 228 ? 26.91170 -13.71904 -43.00398 1.000 90.59708  ? 321 TRP   B CZ3 1 
ATOM   4261 C CH2 . TRP   B 2 228 ? 27.45954 -14.91503 -43.48291 1.000 95.23356  ? 321 TRP   B CH2 1 
ATOM   4262 N N   . CYS   B 2 229 ? 30.85903 -9.14347  -45.42732 1.000 105.69745 ? 322 CYS   B N   1 
ATOM   4263 C CA  . CYS   B 2 229 ? 32.26294 -9.54105  -45.44096 1.000 106.79384 ? 322 CYS   B CA  1 
ATOM   4264 C C   . CYS   B 2 229 ? 32.93944 -9.28128  -44.10080 1.000 96.67064  ? 322 CYS   B C   1 
ATOM   4265 O O   . CYS   B 2 229 ? 33.90691 -9.96873  -43.75433 1.000 104.99022 ? 322 CYS   B O   1 
ATOM   4266 C CB  . CYS   B 2 229 ? 33.00389 -8.80849  -46.55924 1.000 102.42271 ? 322 CYS   B CB  1 
ATOM   4267 S SG  . CYS   B 2 229 ? 32.89561 -7.00544  -46.46836 1.000 107.10576 ? 322 CYS   B SG  1 
ATOM   4268 N N   . ASP   B 2 230 ? 32.44957 -8.30217  -43.33632 1.000 93.08610  ? 323 ASP   B N   1 
ATOM   4269 C CA  . ASP   B 2 230 ? 33.06973 -7.98683  -42.05363 1.000 110.38947 ? 323 ASP   B CA  1 
ATOM   4270 C C   . ASP   B 2 230 ? 32.79732 -9.06406  -41.01304 1.000 99.99927  ? 323 ASP   B C   1 
ATOM   4271 O O   . ASP   B 2 230 ? 33.65067 -9.32844  -40.15834 1.000 93.63151  ? 323 ASP   B O   1 
ATOM   4272 C CB  . ASP   B 2 230 ? 32.57476 -6.63177  -41.54650 1.000 84.46195  ? 323 ASP   B CB  1 
ATOM   4273 C CG  . ASP   B 2 230 ? 32.86643 -5.50436  -42.51564 1.000 99.82085  ? 323 ASP   B CG  1 
ATOM   4274 O OD1 . ASP   B 2 230 ? 33.80787 -5.64184  -43.32495 1.000 119.53555 ? 323 ASP   B OD1 1 
ATOM   4275 O OD2 . ASP   B 2 230 ? 32.15437 -4.47896  -42.46654 1.000 96.85171  ? 323 ASP   B OD2 1 
ATOM   4276 N N   . ILE   B 2 231 ? 31.62351 -9.69711  -41.06834 1.000 86.96099  ? 324 ILE   B N   1 
ATOM   4277 C CA  . ILE   B 2 231 ? 31.22540 -10.67035 -40.06004 1.000 85.51546  ? 324 ILE   B CA  1 
ATOM   4278 C C   . ILE   B 2 231 ? 31.33433 -12.10378 -40.55208 1.000 93.07252  ? 324 ILE   B C   1 
ATOM   4279 O O   . ILE   B 2 231 ? 31.11393 -13.03386 -39.76395 1.000 85.88381  ? 324 ILE   B O   1 
ATOM   4280 C CB  . ILE   B 2 231 ? 29.79204 -10.39575 -39.56538 1.000 80.07837  ? 324 ILE   B CB  1 
ATOM   4281 C CG1 . ILE   B 2 231 ? 28.77450 -10.81057 -40.62928 1.000 88.78297  ? 324 ILE   B CG1 1 
ATOM   4282 C CG2 . ILE   B 2 231 ? 29.62643 -8.92466  -39.21924 1.000 71.43233  ? 324 ILE   B CG2 1 
ATOM   4283 C CD1 . ILE   B 2 231 ? 27.34655 -10.82406 -40.13481 1.000 84.01920  ? 324 ILE   B CD1 1 
ATOM   4284 N N   . GLU   B 2 232 ? 31.66862 -12.31417 -41.82940 1.000 85.31701  ? 325 GLU   B N   1 
ATOM   4285 C CA  . GLU   B 2 232 ? 31.73365 -13.67146 -42.36429 1.000 95.27793  ? 325 GLU   B CA  1 
ATOM   4286 C C   . GLU   B 2 232 ? 32.72449 -14.52761 -41.58657 1.000 82.76205  ? 325 GLU   B C   1 
ATOM   4287 O O   . GLU   B 2 232 ? 32.44178 -15.69166 -41.27850 1.000 88.62606  ? 325 GLU   B O   1 
ATOM   4288 C CB  . GLU   B 2 232 ? 32.10482 -13.64084 -43.84717 1.000 93.34796  ? 325 GLU   B CB  1 
ATOM   4289 C CG  . GLU   B 2 232 ? 32.24766 -15.02400 -44.46350 1.000 91.56406  ? 325 GLU   B CG  1 
ATOM   4290 C CD  . GLU   B 2 232 ? 32.65521 -14.97942 -45.91986 1.000 94.70113  ? 325 GLU   B CD  1 
ATOM   4291 O OE1 . GLU   B 2 232 ? 32.81868 -13.86468 -46.45922 1.000 98.20412  ? 325 GLU   B OE1 1 
ATOM   4292 O OE2 . GLU   B 2 232 ? 32.81222 -16.06083 -46.52470 1.000 114.03625 ? 325 GLU   B OE2 1 
ATOM   4293 N N   . ASN   B 2 233 ? 33.89304 -13.97007 -41.26143 1.000 86.30706  ? 326 ASN   B N   1 
ATOM   4294 C CA  . ASN   B 2 233 ? 34.85635 -14.70741 -40.45161 1.000 81.59471  ? 326 ASN   B CA  1 
ATOM   4295 C C   . ASN   B 2 233 ? 34.30159 -14.97671 -39.05875 1.000 88.24827  ? 326 ASN   B C   1 
ATOM   4296 O O   . ASN   B 2 233 ? 34.49386 -16.06502 -38.50347 1.000 83.38900  ? 326 ASN   B O   1 
ATOM   4297 C CB  . ASN   B 2 233 ? 36.17307 -13.93491 -40.36993 1.000 102.34019 ? 326 ASN   B CB  1 
ATOM   4298 C CG  . ASN   B 2 233 ? 37.32050 -14.78988 -39.86858 1.000 107.96669 ? 326 ASN   B CG  1 
ATOM   4299 O OD1 . ASN   B 2 233 ? 37.33301 -16.00596 -40.06015 1.000 100.67926 ? 326 ASN   B OD1 1 
ATOM   4300 N ND2 . ASN   B 2 233 ? 38.29247 -14.15665 -39.22135 1.000 106.62393 ? 326 ASN   B ND2 1 
ATOM   4301 N N   . CYS   B 2 234 ? 33.59864 -13.99800 -38.48324 1.000 81.51797  ? 327 CYS   B N   1 
ATOM   4302 C CA  . CYS   B 2 234 ? 32.98830 -14.19462 -37.17281 1.000 75.43458  ? 327 CYS   B CA  1 
ATOM   4303 C C   . CYS   B 2 234 ? 31.80876 -15.15565 -37.25069 1.000 83.67268  ? 327 CYS   B C   1 
ATOM   4304 O O   . CYS   B 2 234 ? 31.62509 -15.99380 -36.36009 1.000 77.82821  ? 327 CYS   B O   1 
ATOM   4305 C CB  . CYS   B 2 234 ? 32.54948 -12.85028 -36.59568 1.000 81.84876  ? 327 CYS   B CB  1 
ATOM   4306 S SG  . CYS   B 2 234 ? 31.81116 -12.93896 -34.94939 1.000 75.58980  ? 327 CYS   B SG  1 
ATOM   4307 N N   . VAL   B 2 235 ? 30.99832 -15.04901 -38.30666 1.000 81.12323  ? 328 VAL   B N   1 
ATOM   4308 C CA  . VAL   B 2 235 ? 29.86609 -15.95772 -38.47146 1.000 69.91171  ? 328 VAL   B CA  1 
ATOM   4309 C C   . VAL   B 2 235 ? 30.35663 -17.39214 -38.61937 1.000 82.41434  ? 328 VAL   B C   1 
ATOM   4310 O O   . VAL   B 2 235 ? 29.82537 -18.31606 -37.99180 1.000 86.60676  ? 328 VAL   B O   1 
ATOM   4311 C CB  . VAL   B 2 235 ? 28.99949 -15.52788 -39.66930 1.000 93.44204  ? 328 VAL   B CB  1 
ATOM   4312 C CG1 . VAL   B 2 235 ? 28.07172 -16.65674 -40.09038 1.000 87.01255  ? 328 VAL   B CG1 1 
ATOM   4313 C CG2 . VAL   B 2 235 ? 28.19501 -14.28663 -39.31860 1.000 80.29804  ? 328 VAL   B CG2 1 
ATOM   4314 N N   . LYS   B 2 236 ? 31.38874 -17.59783 -39.44372 1.000 88.84551  ? 329 LYS   B N   1 
ATOM   4315 C CA  . LYS   B 2 236 ? 31.93278 -18.94070 -39.61921 1.000 93.46754  ? 329 LYS   B CA  1 
ATOM   4316 C C   . LYS   B 2 236 ? 32.52250 -19.47909 -38.32242 1.000 82.66141  ? 329 LYS   B C   1 
ATOM   4317 O O   . LYS   B 2 236 ? 32.45563 -20.68656 -38.06491 1.000 89.12009  ? 329 LYS   B O   1 
ATOM   4318 C CB  . LYS   B 2 236 ? 32.98641 -18.94769 -40.72742 1.000 105.39511 ? 329 LYS   B CB  1 
ATOM   4319 C CG  . LYS   B 2 236 ? 33.41788 -20.34485 -41.15083 1.000 112.44063 ? 329 LYS   B CG  1 
ATOM   4320 C CD  . LYS   B 2 236 ? 34.41481 -20.30556 -42.29752 1.000 117.98734 ? 329 LYS   B CD  1 
ATOM   4321 C CE  . LYS   B 2 236 ? 35.72248 -19.65794 -41.87495 1.000 119.76727 ? 329 LYS   B CE  1 
ATOM   4322 N NZ  . LYS   B 2 236 ? 36.73190 -19.68605 -42.96931 1.000 121.28415 ? 329 LYS   B NZ  1 
ATOM   4323 N N   . TRP   B 2 237 ? 33.10057 -18.60602 -37.49443 1.000 87.24706  ? 330 TRP   B N   1 
ATOM   4324 C CA  . TRP   B 2 237 ? 33.57275 -19.04318 -36.18511 1.000 86.12677  ? 330 TRP   B CA  1 
ATOM   4325 C C   . TRP   B 2 237 ? 32.40547 -19.33090 -35.24947 1.000 95.59867  ? 330 TRP   B C   1 
ATOM   4326 O O   . TRP   B 2 237 ? 32.45595 -20.27789 -34.45646 1.000 96.34939  ? 330 TRP   B O   1 
ATOM   4327 C CB  . TRP   B 2 237 ? 34.49999 -17.99045 -35.57815 1.000 80.41738  ? 330 TRP   B CB  1 
ATOM   4328 C CG  . TRP   B 2 237 ? 34.83580 -18.25538 -34.14310 1.000 100.69830 ? 330 TRP   B CG  1 
ATOM   4329 C CD1 . TRP   B 2 237 ? 35.85499 -19.02780 -33.66758 1.000 101.38003 ? 330 TRP   B CD1 1 
ATOM   4330 C CD2 . TRP   B 2 237 ? 34.14511 -17.75047 -32.99419 1.000 94.28448  ? 330 TRP   B CD2 1 
ATOM   4331 N NE1 . TRP   B 2 237 ? 35.84249 -19.03422 -32.29335 1.000 98.21574  ? 330 TRP   B NE1 1 
ATOM   4332 C CE2 . TRP   B 2 237 ? 34.80184 -18.25772 -31.85566 1.000 99.95072  ? 330 TRP   B CE2 1 
ATOM   4333 C CE3 . TRP   B 2 237 ? 33.03440 -16.91942 -32.81832 1.000 92.31622  ? 330 TRP   B CE3 1 
ATOM   4334 C CZ2 . TRP   B 2 237 ? 34.38580 -17.95979 -30.55988 1.000 100.59143 ? 330 TRP   B CZ2 1 
ATOM   4335 C CZ3 . TRP   B 2 237 ? 32.62317 -16.62502 -31.53182 1.000 85.37975  ? 330 TRP   B CZ3 1 
ATOM   4336 C CH2 . TRP   B 2 237 ? 33.29631 -17.14484 -30.41978 1.000 81.34859  ? 330 TRP   B CH2 1 
ATOM   4337 N N   . MET   B 2 238 ? 31.34670 -18.52501 -35.32766 1.000 87.60014  ? 331 MET   B N   1 
ATOM   4338 C CA  . MET   B 2 238 ? 30.16471 -18.71240 -34.49722 1.000 78.57530  ? 331 MET   B CA  1 
ATOM   4339 C C   . MET   B 2 238 ? 29.28544 -19.86213 -34.97437 1.000 89.78808  ? 331 MET   B C   1 
ATOM   4340 O O   . MET   B 2 238 ? 28.32186 -20.21213 -34.28223 1.000 84.34570  ? 331 MET   B O   1 
ATOM   4341 C CB  . MET   B 2 238 ? 29.36003 -17.40655 -34.45747 1.000 77.44398  ? 331 MET   B CB  1 
ATOM   4342 C CG  . MET   B 2 238 ? 28.32414 -17.31725 -33.34891 1.000 81.34237  ? 331 MET   B CG  1 
ATOM   4343 S SD  . MET   B 2 238 ? 27.56788 -15.68563 -33.24780 1.000 74.45779  ? 331 MET   B SD  1 
ATOM   4344 C CE  . MET   B 2 238 ? 28.92573 -14.72666 -32.57922 1.000 71.05611  ? 331 MET   B CE  1 
ATOM   4345 N N   . VAL   B 2 239 ? 29.60571 -20.45994 -36.11902 1.000 93.56416  ? 332 VAL   B N   1 
ATOM   4346 C CA  . VAL   B 2 239 ? 28.81028 -21.52684 -36.72575 1.000 99.52949  ? 332 VAL   B CA  1 
ATOM   4347 C C   . VAL   B 2 239 ? 28.53641 -22.66351 -35.74119 1.000 89.15102  ? 332 VAL   B C   1 
ATOM   4348 O O   . VAL   B 2 239 ? 27.36385 -23.02138 -35.55369 1.000 96.07923  ? 332 VAL   B O   1 
ATOM   4349 C CB  . VAL   B 2 239 ? 29.48277 -22.04393 -38.01091 1.000 92.28416  ? 332 VAL   B CB  1 
ATOM   4350 C CG1 . VAL   B 2 239 ? 29.09385 -23.48869 -38.28720 1.000 87.63628  ? 332 VAL   B CG1 1 
ATOM   4351 C CG2 . VAL   B 2 239 ? 29.11560 -21.16149 -39.19149 1.000 93.85479  ? 332 VAL   B CG2 1 
ATOM   4352 N N   . PRO   B 2 240 ? 29.54391 -23.26160 -35.08636 1.000 99.42487  ? 333 PRO   B N   1 
ATOM   4353 C CA  . PRO   B 2 240 ? 29.22626 -24.38354 -34.18556 1.000 101.33403 ? 333 PRO   B CA  1 
ATOM   4354 C C   . PRO   B 2 240 ? 28.38499 -23.97231 -32.99168 1.000 97.31904  ? 333 PRO   B C   1 
ATOM   4355 O O   . PRO   B 2 240 ? 27.52570 -24.74396 -32.54936 1.000 90.74578  ? 333 PRO   B O   1 
ATOM   4356 C CB  . PRO   B 2 240 ? 30.61013 -24.89465 -33.75865 1.000 115.30017 ? 333 PRO   B CB  1 
ATOM   4357 C CG  . PRO   B 2 240 ? 31.55810 -24.35735 -34.77486 1.000 107.56919 ? 333 PRO   B CG  1 
ATOM   4358 C CD  . PRO   B 2 240 ? 30.99778 -23.02775 -35.14716 1.000 103.15065 ? 333 PRO   B CD  1 
ATOM   4359 N N   . PHE   B 2 241 ? 28.60372 -22.76768 -32.46124 1.000 96.38482  ? 334 PHE   B N   1 
ATOM   4360 C CA  . PHE   B 2 241 ? 27.84315 -22.32057 -31.29917 1.000 102.84249 ? 334 PHE   B CA  1 
ATOM   4361 C C   . PHE   B 2 241 ? 26.37278 -22.11619 -31.64299 1.000 85.42711  ? 334 PHE   B C   1 
ATOM   4362 O O   . PHE   B 2 241 ? 25.49331 -22.38135 -30.81507 1.000 84.51512  ? 334 PHE   B O   1 
ATOM   4363 C CB  . PHE   B 2 241 ? 28.44565 -21.02983 -30.74579 1.000 78.03074  ? 334 PHE   B CB  1 
ATOM   4364 C CG  . PHE   B 2 241 ? 29.92659 -21.10440 -30.50529 1.000 92.28821  ? 334 PHE   B CG  1 
ATOM   4365 C CD1 . PHE   B 2 241 ? 30.42490 -21.60075 -29.31220 1.000 97.81111  ? 334 PHE   B CD1 1 
ATOM   4366 C CD2 . PHE   B 2 241 ? 30.82103 -20.67109 -31.47056 1.000 98.20576  ? 334 PHE   B CD2 1 
ATOM   4367 C CE1 . PHE   B 2 241 ? 31.78835 -21.66741 -29.08799 1.000 100.37758 ? 334 PHE   B CE1 1 
ATOM   4368 C CE2 . PHE   B 2 241 ? 32.18463 -20.73535 -31.25264 1.000 102.71579 ? 334 PHE   B CE2 1 
ATOM   4369 C CZ  . PHE   B 2 241 ? 32.66867 -21.23379 -30.05957 1.000 99.61726  ? 334 PHE   B CZ  1 
ATOM   4370 N N   . ALA   B 2 242 ? 26.08671 -21.64900 -32.86040 1.000 81.58893  ? 335 ALA   B N   1 
ATOM   4371 C CA  . ALA   B 2 242 ? 24.70636 -21.36417 -33.23912 1.000 91.37958  ? 335 ALA   B CA  1 
ATOM   4372 C C   . ALA   B 2 242 ? 23.87750 -22.63927 -33.33612 1.000 88.12899  ? 335 ALA   B C   1 
ATOM   4373 O O   . ALA   B 2 242 ? 22.72368 -22.66958 -32.89255 1.000 84.43955  ? 335 ALA   B O   1 
ATOM   4374 C CB  . ALA   B 2 242 ? 24.67351 -20.59997 -34.56216 1.000 79.83073  ? 335 ALA   B CB  1 
ATOM   4375 N N   . MET   B 2 243 ? 24.44609 -23.70357 -33.90715 1.000 79.41801  ? 336 MET   B N   1 
ATOM   4376 C CA  . MET   B 2 243 ? 23.67803 -24.93089 -34.09332 1.000 88.90199  ? 336 MET   B CA  1 
ATOM   4377 C C   . MET   B 2 243 ? 23.41315 -25.63492 -32.77014 1.000 94.68247  ? 336 MET   B C   1 
ATOM   4378 O O   . MET   B 2 243 ? 22.34310 -26.22548 -32.58295 1.000 89.94644  ? 336 MET   B O   1 
ATOM   4379 C CB  . MET   B 2 243 ? 24.39837 -25.86554 -35.06023 1.000 94.09135  ? 336 MET   B CB  1 
ATOM   4380 C CG  . MET   B 2 243 ? 24.01458 -25.64852 -36.50754 1.000 111.05701 ? 336 MET   B CG  1 
ATOM   4381 S SD  . MET   B 2 243 ? 22.24319 -25.80365 -36.81573 1.000 127.71950 ? 336 MET   B SD  1 
ATOM   4382 C CE  . MET   B 2 243 ? 21.78108 -24.09906 -37.09398 1.000 88.49973  ? 336 MET   B CE  1 
ATOM   4383 N N   . VAL   B 2 244 ? 24.37457 -25.59297 -31.84475 1.000 97.69636  ? 337 VAL   B N   1 
ATOM   4384 C CA  . VAL   B 2 244 ? 24.16142 -26.19593 -30.53197 1.000 92.29206  ? 337 VAL   B CA  1 
ATOM   4385 C C   . VAL   B 2 244 ? 22.96719 -25.54903 -29.84158 1.000 102.44529 ? 337 VAL   B C   1 
ATOM   4386 O O   . VAL   B 2 244 ? 22.18458 -26.22163 -29.15857 1.000 103.43897 ? 337 VAL   B O   1 
ATOM   4387 C CB  . VAL   B 2 244 ? 25.44190 -26.09263 -29.68239 1.000 112.79840 ? 337 VAL   B CB  1 
ATOM   4388 C CG1 . VAL   B 2 244 ? 25.20712 -26.65569 -28.29420 1.000 106.16224 ? 337 VAL   B CG1 1 
ATOM   4389 C CG2 . VAL   B 2 244 ? 26.58488 -26.82893 -30.36204 1.000 103.11257 ? 337 VAL   B CG2 1 
ATOM   4390 N N   . ILE   B 2 245 ? 22.79732 -24.23762 -30.02344 1.000 95.18213  ? 338 ILE   B N   1 
ATOM   4391 C CA  . ILE   B 2 245 ? 21.60751 -23.56632 -29.51091 1.000 93.04197  ? 338 ILE   B CA  1 
ATOM   4392 C C   . ILE   B 2 245 ? 20.37577 -23.99112 -30.30171 1.000 90.25137  ? 338 ILE   B C   1 
ATOM   4393 O O   . ILE   B 2 245 ? 19.28716 -24.16117 -29.73930 1.000 100.67962 ? 338 ILE   B O   1 
ATOM   4394 C CB  . ILE   B 2 245 ? 21.80382 -22.03924 -29.53986 1.000 90.04922  ? 338 ILE   B CB  1 
ATOM   4395 C CG1 . ILE   B 2 245 ? 23.03690 -21.64414 -28.72496 1.000 89.43069  ? 338 ILE   B CG1 1 
ATOM   4396 C CG2 . ILE   B 2 245 ? 20.56705 -21.32658 -29.01199 1.000 95.04612  ? 338 ILE   B CG2 1 
ATOM   4397 C CD1 . ILE   B 2 245 ? 22.95021 -22.02418 -27.26373 1.000 100.55348 ? 338 ILE   B CD1 1 
ATOM   4398 N N   . ARG   B 2 246 ? 20.52757 -24.17893 -31.61574 1.000 78.85831  ? 339 ARG   B N   1 
ATOM   4399 C CA  . ARG   B 2 246 ? 19.39506 -24.58327 -32.44274 1.000 88.03412  ? 339 ARG   B CA  1 
ATOM   4400 C C   . ARG   B 2 246 ? 18.98364 -26.02651 -32.17909 1.000 95.39116  ? 339 ARG   B C   1 
ATOM   4401 O O   . ARG   B 2 246 ? 17.79925 -26.35968 -32.29697 1.000 88.59602  ? 339 ARG   B O   1 
ATOM   4402 C CB  . ARG   B 2 246 ? 19.72842 -24.39495 -33.92337 1.000 96.45491  ? 339 ARG   B CB  1 
ATOM   4403 C CG  . ARG   B 2 246 ? 19.80164 -22.94537 -34.37438 1.000 88.05407  ? 339 ARG   B CG  1 
ATOM   4404 C CD  . ARG   B 2 246 ? 18.42792 -22.29960 -34.40621 1.000 77.75990  ? 339 ARG   B CD  1 
ATOM   4405 N NE  . ARG   B 2 246 ? 18.47942 -20.94851 -34.95180 1.000 87.71694  ? 339 ARG   B NE  1 
ATOM   4406 C CZ  . ARG   B 2 246 ? 17.45072 -20.11271 -34.98119 1.000 81.28322  ? 339 ARG   B CZ  1 
ATOM   4407 N NH1 . ARG   B 2 246 ? 16.26889 -20.45406 -34.49447 1.000 81.67271  ? 339 ARG   B NH1 1 
ATOM   4408 N NH2 . ARG   B 2 246 ? 17.61250 -18.90311 -35.50981 1.000 81.47189  ? 339 ARG   B NH2 1 
ATOM   4409 N N   . GLU   B 2 247 ? 19.93688 -26.89476 -31.82914 1.000 100.75915 ? 340 GLU   B N   1 
ATOM   4410 C CA  . GLU   B 2 247 ? 19.60338 -28.29601 -31.58863 1.000 95.15351  ? 340 GLU   B CA  1 
ATOM   4411 C C   . GLU   B 2 247 ? 18.74348 -28.45771 -30.34152 1.000 96.25304  ? 340 GLU   B C   1 
ATOM   4412 O O   . GLU   B 2 247 ? 17.83334 -29.29415 -30.31351 1.000 100.23543 ? 340 GLU   B O   1 
ATOM   4413 C CB  . GLU   B 2 247 ? 20.87788 -29.13164 -31.46924 1.000 106.22642 ? 340 GLU   B CB  1 
ATOM   4414 C CG  . GLU   B 2 247 ? 21.63764 -29.30141 -32.77210 1.000 110.92556 ? 340 GLU   B CG  1 
ATOM   4415 C CD  . GLU   B 2 247 ? 22.83911 -30.21395 -32.63211 1.000 127.55587 ? 340 GLU   B CD  1 
ATOM   4416 O OE1 . GLU   B 2 247 ? 22.91690 -30.94464 -31.62224 1.000 143.61934 ? 340 GLU   B OE1 1 
ATOM   4417 O OE2 . GLU   B 2 247 ? 23.70663 -30.19932 -33.53066 1.000 125.65856 ? 340 GLU   B OE2 1 
ATOM   4418 N N   . THR   B 2 248 ? 19.01513 -27.67161 -29.30192 1.000 91.35362  ? 341 THR   B N   1 
ATOM   4419 C CA  . THR   B 2 248 ? 18.26036 -27.75423 -28.05964 1.000 94.02574  ? 341 THR   B CA  1 
ATOM   4420 C C   . THR   B 2 248 ? 17.09951 -26.77160 -27.99835 1.000 108.11030 ? 341 THR   B C   1 
ATOM   4421 O O   . THR   B 2 248 ? 16.24612 -26.90134 -27.11404 1.000 110.13174 ? 341 THR   B O   1 
ATOM   4422 C CB  . THR   B 2 248 ? 19.18273 -27.51526 -26.85941 1.000 94.10010  ? 341 THR   B CB  1 
ATOM   4423 O OG1 . THR   B 2 248 ? 18.43417 -27.65563 -25.64567 1.000 124.56849 ? 341 THR   B OG1 1 
ATOM   4424 C CG2 . THR   B 2 248 ? 19.78274 -26.11778 -26.91817 1.000 106.02024 ? 341 THR   B CG2 1 
ATOM   4425 N N   . GLY   B 2 249 ? 17.04443 -25.80148 -28.90685 1.000 121.08142 ? 342 GLY   B N   1 
ATOM   4426 C CA  . GLY   B 2 249 ? 15.99339 -24.80644 -28.88884 1.000 115.68844 ? 342 GLY   B CA  1 
ATOM   4427 C C   . GLY   B 2 249 ? 16.37856 -23.56740 -28.10819 1.000 120.70153 ? 342 GLY   B C   1 
ATOM   4428 O O   . GLY   B 2 249 ? 17.49123 -23.41985 -27.59388 1.000 115.75324 ? 342 GLY   B O   1 
ATOM   4429 N N   . SER   B 2 250 ? 15.42047 -22.65141 -28.01960 1.000 111.43573 ? 343 SER   B N   1 
ATOM   4430 C CA  . SER   B 2 250 ? 15.60329 -21.38754 -27.32532 1.000 102.05624 ? 343 SER   B CA  1 
ATOM   4431 C C   . SER   B 2 250 ? 14.76565 -21.36078 -26.05327 1.000 103.88760 ? 343 SER   B C   1 
ATOM   4432 O O   . SER   B 2 250 ? 13.71945 -22.00974 -25.96326 1.000 105.03781 ? 343 SER   B O   1 
ATOM   4433 C CB  . SER   B 2 250 ? 15.22652 -20.20863 -28.22609 1.000 79.76221  ? 343 SER   B CB  1 
ATOM   4434 O OG  . SER   B 2 250 ? 13.88512 -20.31382 -28.66966 1.000 113.03945 ? 343 SER   B OG  1 
ATOM   4435 N N   . SER   B 2 251 ? 15.23678 -20.59977 -25.06987 1.000 111.61253 ? 344 SER   B N   1 
ATOM   4436 C CA  . SER   B 2 251 ? 14.56451 -20.52258 -23.78397 1.000 99.68561  ? 344 SER   B CA  1 
ATOM   4437 C C   . SER   B 2 251 ? 13.42879 -19.50341 -23.82362 1.000 101.29136 ? 344 SER   B C   1 
ATOM   4438 O O   . SER   B 2 251 ? 13.33298 -18.66812 -24.72705 1.000 87.21479  ? 344 SER   B O   1 
ATOM   4439 C CB  . SER   B 2 251 ? 15.55706 -20.15577 -22.68041 1.000 101.98487 ? 344 SER   B CB  1 
ATOM   4440 O OG  . SER   B 2 251 ? 16.57645 -21.13282 -22.56611 1.000 104.97464 ? 344 SER   B OG  1 
ATOM   4441 N N   . LYS   B 2 252 ? 12.56143 -19.58466 -22.82111 1.000 95.88035  ? 345 LYS   B N   1 
ATOM   4442 C CA  . LYS   B 2 252 ? 11.44872 -18.66049 -22.67521 1.000 94.70136  ? 345 LYS   B CA  1 
ATOM   4443 C C   . LYS   B 2 252 ? 11.85552 -17.46282 -21.82170 1.000 89.32258  ? 345 LYS   B C   1 
ATOM   4444 O O   . LYS   B 2 252 ? 12.85559 -17.49057 -21.10073 1.000 79.51528  ? 345 LYS   B O   1 
ATOM   4445 C CB  . LYS   B 2 252 ? 10.24382 -19.36198 -22.04534 1.000 100.68788 ? 345 LYS   B CB  1 
ATOM   4446 C CG  . LYS   B 2 252 ? 9.66722  -20.50198 -22.87336 1.000 108.00390 ? 345 LYS   B CG  1 
ATOM   4447 C CD  . LYS   B 2 252 ? 8.87276  -19.98410 -24.06175 1.000 91.97322  ? 345 LYS   B CD  1 
ATOM   4448 C CE  . LYS   B 2 252 ? 8.17880  -21.11986 -24.79781 1.000 106.01168 ? 345 LYS   B CE  1 
ATOM   4449 N NZ  . LYS   B 2 252 ? 7.30874  -20.61595 -25.89564 1.000 99.02030  ? 345 LYS   B NZ  1 
ATOM   4450 N N   . LEU   B 2 253 ? 11.05696 -16.40196 -21.91278 1.000 83.53408  ? 346 LEU   B N   1 
ATOM   4451 C CA  . LEU   B 2 253 ? 11.27017 -15.21146 -21.10134 1.000 76.55359  ? 346 LEU   B CA  1 
ATOM   4452 C C   . LEU   B 2 253 ? 10.81995 -15.47036 -19.66855 1.000 83.91267  ? 346 LEU   B C   1 
ATOM   4453 O O   . LEU   B 2 253 ? 9.69336  -15.91954 -19.43302 1.000 91.88718  ? 346 LEU   B O   1 
ATOM   4454 C CB  . LEU   B 2 253 ? 10.50992 -14.02342 -21.69010 1.000 76.66695  ? 346 LEU   B CB  1 
ATOM   4455 C CG  . LEU   B 2 253 ? 10.54249 -12.72215 -20.88402 1.000 85.08195  ? 346 LEU   B CG  1 
ATOM   4456 C CD1 . LEU   B 2 253 ? 11.96986 -12.22262 -20.72635 1.000 77.09709  ? 346 LEU   B CD1 1 
ATOM   4457 C CD2 . LEU   B 2 253 ? 9.66345  -11.65959 -21.52905 1.000 76.06272  ? 346 LEU   B CD2 1 
ATOM   4458 N N   . LYS   B 2 254 ? 11.69860 -15.18356 -18.71448 1.000 91.19417  ? 347 LYS   B N   1 
ATOM   4459 C CA  . LYS   B 2 254 ? 11.41917 -15.44034 -17.31108 1.000 87.02632  ? 347 LYS   B CA  1 
ATOM   4460 C C   . LYS   B 2 254 ? 10.81504 -14.21352 -16.63584 1.000 96.04773  ? 347 LYS   B C   1 
ATOM   4461 O O   . LYS   B 2 254 ? 10.91536 -13.08516 -17.12382 1.000 92.25270  ? 347 LYS   B O   1 
ATOM   4462 C CB  . LYS   B 2 254 ? 12.69179 -15.85742 -16.57301 1.000 81.11953  ? 347 LYS   B CB  1 
ATOM   4463 C CG  . LYS   B 2 254 ? 13.21524 -17.23404 -16.94077 1.000 78.08243  ? 347 LYS   B CG  1 
ATOM   4464 C CD  . LYS   B 2 254 ? 14.38837 -17.61617 -16.05229 1.000 87.26007  ? 347 LYS   B CD  1 
ATOM   4465 C CE  . LYS   B 2 254 ? 14.84785 -19.04048 -16.31367 1.000 105.14057 ? 347 LYS   B CE  1 
ATOM   4466 N NZ  . LYS   B 2 254 ? 15.94218 -19.44432 -15.38637 1.000 92.79312  ? 347 LYS   B NZ  1 
ATOM   4467 N N   . HIS   B 2 255 ? 10.17838 -14.45591 -15.49455 1.000 105.11357 ? 348 HIS   B N   1 
ATOM   4468 C CA  . HIS   B 2 255 ? 9.67223  -13.40455 -14.62668 1.000 103.64320 ? 348 HIS   B CA  1 
ATOM   4469 C C   . HIS   B 2 255 ? 10.43244 -13.43096 -13.30875 1.000 102.95036 ? 348 HIS   B C   1 
ATOM   4470 O O   . HIS   B 2 255 ? 10.66809 -14.50090 -12.73839 1.000 99.71874  ? 348 HIS   B O   1 
ATOM   4471 C CB  . HIS   B 2 255 ? 8.17319  -13.56847 -14.36559 1.000 114.23338 ? 348 HIS   B CB  1 
ATOM   4472 C CG  . HIS   B 2 255 ? 7.66285  -12.71895 -13.24361 1.000 122.75148 ? 348 HIS   B CG  1 
ATOM   4473 N ND1 . HIS   B 2 255 ? 7.62408  -11.34275 -13.30971 1.000 124.93550 ? 348 HIS   B ND1 1 
ATOM   4474 C CD2 . HIS   B 2 255 ? 7.18096  -13.05047 -12.02234 1.000 117.92733 ? 348 HIS   B CD2 1 
ATOM   4475 C CE1 . HIS   B 2 255 ? 7.13472  -10.86338 -12.18004 1.000 119.09525 ? 348 HIS   B CE1 1 
ATOM   4476 N NE2 . HIS   B 2 255 ? 6.85801  -11.87881 -11.38191 1.000 113.17790 ? 348 HIS   B NE2 1 
ATOM   4477 N N   . PHE   B 2 256 ? 10.81738 -12.25160 -12.83098 1.000 108.43153 ? 349 PHE   B N   1 
ATOM   4478 C CA  . PHE   B 2 256 ? 11.56488 -12.11005 -11.58991 1.000 109.41503 ? 349 PHE   B CA  1 
ATOM   4479 C C   . PHE   B 2 256 ? 10.78974 -11.20908 -10.64105 1.000 102.33650 ? 349 PHE   B C   1 
ATOM   4480 O O   . PHE   B 2 256 ? 10.41865 -10.08892 -11.00820 1.000 90.41402  ? 349 PHE   B O   1 
ATOM   4481 C CB  . PHE   B 2 256 ? 12.96179 -11.53893 -11.85125 1.000 101.88640 ? 349 PHE   B CB  1 
ATOM   4482 C CG  . PHE   B 2 256 ? 13.77774 -12.35211 -12.81723 1.000 88.95881  ? 349 PHE   B CG  1 
ATOM   4483 C CD1 . PHE   B 2 256 ? 14.55221 -13.41063 -12.37169 1.000 89.10523  ? 349 PHE   B CD1 1 
ATOM   4484 C CD2 . PHE   B 2 256 ? 13.76937 -12.05814 -14.17110 1.000 93.43599  ? 349 PHE   B CD2 1 
ATOM   4485 C CE1 . PHE   B 2 256 ? 15.30322 -14.16072 -13.25760 1.000 81.27591  ? 349 PHE   B CE1 1 
ATOM   4486 C CE2 . PHE   B 2 256 ? 14.51825 -12.80478 -15.06264 1.000 85.66811  ? 349 PHE   B CE2 1 
ATOM   4487 C CZ  . PHE   B 2 256 ? 15.28623 -13.85708 -14.60489 1.000 93.32575  ? 349 PHE   B CZ  1 
ATOM   4488 N N   . ARG   B 2 257 ? 10.54108 -11.70312 -9.42942  1.000 109.31246 ? 350 ARG   B N   1 
ATOM   4489 C CA  . ARG   B 2 257 ? 9.82274  -10.91601 -8.43694  1.000 96.89920  ? 350 ARG   B CA  1 
ATOM   4490 C C   . ARG   B 2 257 ? 10.61934 -9.67127  -8.06757  1.000 91.32898  ? 350 ARG   B C   1 
ATOM   4491 O O   . ARG   B 2 257 ? 11.83264 -9.72903  -7.84931  1.000 85.60429  ? 350 ARG   B O   1 
ATOM   4492 C CB  . ARG   B 2 257 ? 9.54139  -11.75766 -7.19147  1.000 112.93607 ? 350 ARG   B CB  1 
ATOM   4493 C CG  . ARG   B 2 257 ? 8.42175  -12.77098 -7.37204  1.000 119.02748 ? 350 ARG   B CG  1 
ATOM   4494 C CD  . ARG   B 2 257 ? 8.13832  -13.53670 -6.08663  1.000 131.16417 ? 350 ARG   B CD  1 
ATOM   4495 N NE  . ARG   B 2 257 ? 9.09418  -14.61418 -5.85775  1.000 132.94059 ? 350 ARG   B NE  1 
ATOM   4496 C CZ  . ARG   B 2 257 ? 10.17495 -14.51370 -5.09580  1.000 132.89422 ? 350 ARG   B CZ  1 
ATOM   4497 N NH1 . ARG   B 2 257 ? 10.47722 -13.38875 -4.46829  1.000 120.02978 ? 350 ARG   B NH1 1 
ATOM   4498 N NH2 . ARG   B 2 257 ? 10.97170 -15.56976 -4.95826  1.000 125.77468 ? 350 ARG   B NH2 1 
ATOM   4499 N N   . GLY   B 2 258 ? 9.92497  -8.53656  -8.00124  1.000 83.63398  ? 351 GLY   B N   1 
ATOM   4500 C CA  . GLY   B 2 258 ? 10.56033 -7.25943  -7.77336  1.000 86.92461  ? 351 GLY   B CA  1 
ATOM   4501 C C   . GLY   B 2 258 ? 11.06513 -6.57142  -9.02232  1.000 92.01904  ? 351 GLY   B C   1 
ATOM   4502 O O   . GLY   B 2 258 ? 11.40922 -5.38397  -8.95977  1.000 92.45714  ? 351 GLY   B O   1 
ATOM   4503 N N   . VAL   B 2 259 ? 11.11993 -7.27414  -10.15122 1.000 88.88498  ? 352 VAL   B N   1 
ATOM   4504 C CA  . VAL   B 2 259 ? 11.56753 -6.71719  -11.42214 1.000 87.94247  ? 352 VAL   B CA  1 
ATOM   4505 C C   . VAL   B 2 259 ? 10.35302 -6.55275  -12.32365 1.000 75.83799  ? 352 VAL   B C   1 
ATOM   4506 O O   . VAL   B 2 259 ? 9.58208  -7.50116  -12.51576 1.000 85.12627  ? 352 VAL   B O   1 
ATOM   4507 C CB  . VAL   B 2 259 ? 12.62809 -7.61083  -12.08888 1.000 84.01567  ? 352 VAL   B CB  1 
ATOM   4508 C CG1 . VAL   B 2 259 ? 13.14604 -6.96066  -13.36340 1.000 77.84668  ? 352 VAL   B CG1 1 
ATOM   4509 C CG2 . VAL   B 2 259 ? 13.76896 -7.89567  -11.12425 1.000 84.43707  ? 352 VAL   B CG2 1 
ATOM   4510 N N   . ALA   B 2 260 ? 10.18156 -5.35204  -12.87131 1.000 85.65245  ? 353 ALA   B N   1 
ATOM   4511 C CA  . ALA   B 2 260 ? 9.07168  -5.10075  -13.77875 1.000 100.68773 ? 353 ALA   B CA  1 
ATOM   4512 C C   . ALA   B 2 260 ? 9.21400  -5.94635  -15.03939 1.000 94.55708  ? 353 ALA   B C   1 
ATOM   4513 O O   . ALA   B 2 260 ? 10.32157 -6.27042  -15.47653 1.000 90.42245  ? 353 ALA   B O   1 
ATOM   4514 C CB  . ALA   B 2 260 ? 9.00421  -3.61677  -14.14160 1.000 86.81911  ? 353 ALA   B CB  1 
ATOM   4515 N N   . ASP   B 2 261 ? 8.07011  -6.31219  -15.62388 1.000 98.04096  ? 354 ASP   B N   1 
ATOM   4516 C CA  . ASP   B 2 261 ? 8.09221  -7.14559  -16.82173 1.000 103.85469 ? 354 ASP   B CA  1 
ATOM   4517 C C   . ASP   B 2 261 ? 8.67797  -6.40441  -18.01648 1.000 89.43428  ? 354 ASP   B C   1 
ATOM   4518 O O   . ASP   B 2 261 ? 9.20419  -7.03859  -18.93783 1.000 95.92869  ? 354 ASP   B O   1 
ATOM   4519 C CB  . ASP   B 2 261 ? 6.68494  -7.64801  -17.14220 1.000 117.93561 ? 354 ASP   B CB  1 
ATOM   4520 C CG  . ASP   B 2 261 ? 6.21363  -8.71420  -16.17291 1.000 123.02997 ? 354 ASP   B CG  1 
ATOM   4521 O OD1 . ASP   B 2 261 ? 7.06628  -9.46365  -15.65119 1.000 108.66638 ? 354 ASP   B OD1 1 
ATOM   4522 O OD2 . ASP   B 2 261 ? 4.99125  -8.80443  -15.93415 1.000 134.22210 ? 354 ASP   B OD2 1 
ATOM   4523 N N   . GLU   B 2 262 ? 8.60285  -5.07279  -18.02141 1.000 76.96093  ? 355 GLU   B N   1 
ATOM   4524 C CA  . GLU   B 2 262 ? 9.22430  -4.28393  -19.07877 1.000 91.38329  ? 355 GLU   B CA  1 
ATOM   4525 C C   . GLU   B 2 262 ? 10.74279 -4.23833  -18.96689 1.000 91.25060  ? 355 GLU   B C   1 
ATOM   4526 O O   . GLU   B 2 262 ? 11.38996 -3.61436  -19.81537 1.000 89.99228  ? 355 GLU   B O   1 
ATOM   4527 C CB  . GLU   B 2 262 ? 8.65723  -2.86301  -19.07241 1.000 96.06607  ? 355 GLU   B CB  1 
ATOM   4528 C CG  . GLU   B 2 262 ? 8.66833  -2.19740  -17.70724 1.000 97.38521  ? 355 GLU   B CG  1 
ATOM   4529 C CD  . GLU   B 2 262 ? 7.27887  -1.81299  -17.23693 1.000 102.88099 ? 355 GLU   B CD  1 
ATOM   4530 O OE1 . GLU   B 2 262 ? 6.35702  -1.76514  -18.07835 1.000 99.84449  ? 355 GLU   B OE1 1 
ATOM   4531 O OE2 . GLU   B 2 262 ? 7.10750  -1.56186  -16.02548 1.000 114.38648 ? 355 GLU   B OE2 1 
ATOM   4532 N N   . ASP   B 2 263 ? 11.32138 -4.87863  -17.94793 1.000 90.14532  ? 356 ASP   B N   1 
ATOM   4533 C CA  . ASP   B 2 263 ? 12.76634 -4.94205  -17.77489 1.000 69.09806  ? 356 ASP   B CA  1 
ATOM   4534 C C   . ASP   B 2 263 ? 13.24288 -6.36349  -17.49407 1.000 68.53628  ? 356 ASP   B C   1 
ATOM   4535 O O   . ASP   B 2 263 ? 14.42034 -6.55894  -17.17033 1.000 67.88200  ? 356 ASP   B O   1 
ATOM   4536 C CB  . ASP   B 2 263 ? 13.20862 -4.00156  -16.64486 1.000 77.12048  ? 356 ASP   B CB  1 
ATOM   4537 C CG  . ASP   B 2 263 ? 14.69368 -3.68989  -16.68636 1.000 95.28522  ? 356 ASP   B CG  1 
ATOM   4538 O OD1 . ASP   B 2 263 ? 15.12859 -2.97986  -17.61718 1.000 96.73831  ? 356 ASP   B OD1 1 
ATOM   4539 O OD2 . ASP   B 2 263 ? 15.42511 -4.15431  -15.78630 1.000 90.93613  ? 356 ASP   B OD2 1 
ATOM   4540 N N   . ALA   B 2 264 ? 12.36276 -7.36060  -17.62042 1.000 66.59895  ? 357 ALA   B N   1 
ATOM   4541 C CA  . ALA   B 2 264 ? 12.72655 -8.72861  -17.26544 1.000 63.68919  ? 357 ALA   B CA  1 
ATOM   4542 C C   . ALA   B 2 264 ? 13.76082 -9.31317  -18.21926 1.000 69.91980  ? 357 ALA   B C   1 
ATOM   4543 O O   . ALA   B 2 264 ? 14.53414 -10.19394 -17.82563 1.000 72.86380  ? 357 ALA   B O   1 
ATOM   4544 C CB  . ALA   B 2 264 ? 11.47849 -9.61058  -17.23458 1.000 75.84595  ? 357 ALA   B CB  1 
ATOM   4545 N N   . HIS   B 2 265 ? 13.79148 -8.84568  -19.46917 1.000 69.49993  ? 358 HIS   B N   1 
ATOM   4546 C CA  . HIS   B 2 265 ? 14.75340 -9.36585  -20.43399 1.000 68.78323  ? 358 HIS   B CA  1 
ATOM   4547 C C   . HIS   B 2 265 ? 16.17836 -8.92161  -20.13163 1.000 69.21516  ? 358 HIS   B C   1 
ATOM   4548 O O   . HIS   B 2 265 ? 17.12624 -9.57183  -20.58582 1.000 59.13702  ? 358 HIS   B O   1 
ATOM   4549 C CB  . HIS   B 2 265 ? 14.36678 -8.93159  -21.84813 1.000 65.33584  ? 358 HIS   B CB  1 
ATOM   4550 C CG  . HIS   B 2 265 ? 14.44727 -7.45314  -22.06819 1.000 64.52432  ? 358 HIS   B CG  1 
ATOM   4551 N ND1 . HIS   B 2 265 ? 13.54181 -6.56871  -21.52261 1.000 67.90623  ? 358 HIS   B ND1 1 
ATOM   4552 C CD2 . HIS   B 2 265 ? 15.32541 -6.70368  -22.77561 1.000 56.46840  ? 358 HIS   B CD2 1 
ATOM   4553 C CE1 . HIS   B 2 265 ? 13.85921 -5.33816  -21.88334 1.000 69.54734  ? 358 HIS   B CE1 1 
ATOM   4554 N NE2 . HIS   B 2 265 ? 14.93738 -5.39240  -22.64436 1.000 66.78759  ? 358 HIS   B NE2 1 
ATOM   4555 N N   . ASN   B 2 266 ? 16.35045 -7.83593  -19.37940 1.000 64.83152  ? 359 ASN   B N   1 
ATOM   4556 C CA  . ASN   B 2 266 ? 17.67294 -7.31547  -19.05724 1.000 68.58733  ? 359 ASN   B CA  1 
ATOM   4557 C C   . ASN   B 2 266 ? 18.32928 -8.02997  -17.88392 1.000 69.19776  ? 359 ASN   B C   1 
ATOM   4558 O O   . ASN   B 2 266 ? 19.46481 -7.69081  -17.53418 1.000 59.75507  ? 359 ASN   B O   1 
ATOM   4559 C CB  . ASN   B 2 266 ? 17.58789 -5.81611  -18.75873 1.000 53.67728  ? 359 ASN   B CB  1 
ATOM   4560 C CG  . ASN   B 2 266 ? 17.22427 -4.99856  -19.98158 1.000 62.83678  ? 359 ASN   B CG  1 
ATOM   4561 O OD1 . ASN   B 2 266 ? 17.72081 -5.24908  -21.07957 1.000 69.46242  ? 359 ASN   B OD1 1 
ATOM   4562 N ND2 . ASN   B 2 266 ? 16.35148 -4.01469  -19.79787 1.000 59.76931  ? 359 ASN   B ND2 1 
ATOM   4563 N N   . ILE   B 2 267 ? 17.65620 -8.99823  -17.27186 1.000 64.55531  ? 360 ILE   B N   1 
ATOM   4564 C CA  . ILE   B 2 267 ? 18.20154 -9.72238  -16.12997 1.000 68.73655  ? 360 ILE   B CA  1 
ATOM   4565 C C   . ILE   B 2 267 ? 19.02303 -10.89782 -16.63995 1.000 69.71906  ? 360 ILE   B C   1 
ATOM   4566 O O   . ILE   B 2 267 ? 18.57665 -11.64735 -17.51707 1.000 70.04412  ? 360 ILE   B O   1 
ATOM   4567 C CB  . ILE   B 2 267 ? 17.07978 -10.19693 -15.19168 1.000 68.53039  ? 360 ILE   B CB  1 
ATOM   4568 C CG1 . ILE   B 2 267 ? 16.22154 -9.01113  -14.74530 1.000 63.56872  ? 360 ILE   B CG1 1 
ATOM   4569 C CG2 . ILE   B 2 267 ? 17.66143 -10.92181 -13.98901 1.000 63.36180  ? 360 ILE   B CG2 1 
ATOM   4570 C CD1 . ILE   B 2 267 ? 17.00684 -7.90260  -14.07945 1.000 71.42460  ? 360 ILE   B CD1 1 
ATOM   4571 N N   . GLN   B 2 268 ? 20.22575 -11.05761 -16.09421 1.000 58.97399  ? 361 GLN   B N   1 
ATOM   4572 C CA  . GLN   B 2 268 ? 21.09320 -12.15191 -16.50494 1.000 64.10120  ? 361 GLN   B CA  1 
ATOM   4573 C C   . GLN   B 2 268 ? 20.53460 -13.48501 -16.02455 1.000 82.25697  ? 361 GLN   B C   1 
ATOM   4574 O O   . GLN   B 2 268 ? 20.09406 -13.61755 -14.87943 1.000 78.22870  ? 361 GLN   B O   1 
ATOM   4575 C CB  . GLN   B 2 268 ? 22.50593 -11.94670 -15.95736 1.000 60.03226  ? 361 GLN   B CB  1 
ATOM   4576 C CG  . GLN   B 2 268 ? 23.49324 -13.02912 -16.36681 1.000 63.69320  ? 361 GLN   B CG  1 
ATOM   4577 C CD  . GLN   B 2 268 ? 23.72979 -13.06332 -17.86458 1.000 68.89437  ? 361 GLN   B CD  1 
ATOM   4578 O OE1 . GLN   B 2 268 ? 23.96940 -12.03045 -18.48960 1.000 63.73852  ? 361 GLN   B OE1 1 
ATOM   4579 N NE2 . GLN   B 2 268 ? 23.65778 -14.25365 -18.44931 1.000 72.78367  ? 361 GLN   B NE2 1 
ATOM   4580 N N   . THR   B 2 269 ? 20.54826 -14.47237 -16.91141 1.000 76.30247  ? 362 THR   B N   1 
ATOM   4581 C CA  . THR   B 2 269 ? 20.11032 -15.82740 -16.60952 1.000 83.32690  ? 362 THR   B CA  1 
ATOM   4582 C C   . THR   B 2 269 ? 21.29839 -16.77812 -16.71613 1.000 82.30691  ? 362 THR   B C   1 
ATOM   4583 O O   . THR   B 2 269 ? 22.40183 -16.39056 -17.10834 1.000 75.13361  ? 362 THR   B O   1 
ATOM   4584 C CB  . THR   B 2 269 ? 18.97953 -16.26244 -17.54650 1.000 82.43559  ? 362 THR   B CB  1 
ATOM   4585 O OG1 . THR   B 2 269 ? 19.42692 -16.18706 -18.90593 1.000 78.22434  ? 362 THR   B OG1 1 
ATOM   4586 C CG2 . THR   B 2 269 ? 17.76388 -15.36623 -17.36617 1.000 79.11682  ? 362 THR   B CG2 1 
ATOM   4587 N N   . HIS   B 2 270 ? 21.06291 -18.03827 -16.35919 1.000 86.82749  ? 363 HIS   B N   1 
ATOM   4588 C CA  . HIS   B 2 270 ? 22.11354 -19.05057 -16.42557 1.000 90.12308  ? 363 HIS   B CA  1 
ATOM   4589 C C   . HIS   B 2 270 ? 21.47356 -20.42558 -16.49250 1.000 96.78084  ? 363 HIS   B C   1 
ATOM   4590 O O   . HIS   B 2 270 ? 20.74858 -20.81658 -15.57187 1.000 116.79846 ? 363 HIS   B O   1 
ATOM   4591 C CB  . HIS   B 2 270 ? 23.04950 -18.95608 -15.21981 1.000 90.11973  ? 363 HIS   B CB  1 
ATOM   4592 C CG  . HIS   B 2 270 ? 23.98488 -20.11856 -15.09206 1.000 94.72104  ? 363 HIS   B CG  1 
ATOM   4593 N ND1 . HIS   B 2 270 ? 23.65955 -21.26218 -14.39440 1.000 106.12503 ? 363 HIS   B ND1 1 
ATOM   4594 C CD2 . HIS   B 2 270 ? 25.23321 -20.31714 -15.57774 1.000 94.58085  ? 363 HIS   B CD2 1 
ATOM   4595 C CE1 . HIS   B 2 270 ? 24.66749 -22.11400 -14.45391 1.000 92.48549  ? 363 HIS   B CE1 1 
ATOM   4596 N NE2 . HIS   B 2 270 ? 25.63509 -21.56481 -15.16578 1.000 96.46805  ? 363 HIS   B NE2 1 
ATOM   4597 N N   . ARG   B 2 271 ? 21.73857 -21.15176 -17.57307 1.000 96.63264  ? 364 ARG   B N   1 
ATOM   4598 C CA  . ARG   B 2 271 ? 21.41252 -22.56357 -17.67287 1.000 115.92741 ? 364 ARG   B CA  1 
ATOM   4599 C C   . ARG   B 2 271 ? 22.69959 -23.34900 -17.88412 1.000 120.87683 ? 364 ARG   B C   1 
ATOM   4600 O O   . ARG   B 2 271 ? 23.70036 -22.81750 -18.37350 1.000 116.95049 ? 364 ARG   B O   1 
ATOM   4601 C CB  . ARG   B 2 271 ? 20.41025 -22.83658 -18.80712 1.000 110.11927 ? 364 ARG   B CB  1 
ATOM   4602 C CG  . ARG   B 2 271 ? 20.83299 -22.34719 -20.18741 1.000 122.64895 ? 364 ARG   B CG  1 
ATOM   4603 C CD  . ARG   B 2 271 ? 21.52219 -23.44283 -20.98837 1.000 124.46943 ? 364 ARG   B CD  1 
ATOM   4604 N NE  . ARG   B 2 271 ? 21.48155 -23.18131 -22.42186 1.000 122.06207 ? 364 ARG   B NE  1 
ATOM   4605 C CZ  . ARG   B 2 271 ? 20.57224 -23.68207 -23.24706 1.000 116.17308 ? 364 ARG   B CZ  1 
ATOM   4606 N NH1 . ARG   B 2 271 ? 19.61138 -24.48159 -22.81385 1.000 124.47103 ? 364 ARG   B NH1 1 
ATOM   4607 N NH2 . ARG   B 2 271 ? 20.62957 -23.37462 -24.53981 1.000 110.38906 ? 364 ARG   B NH2 1 
ATOM   4608 N N   . ASP   B 2 272 ? 22.66859 -24.62353 -17.49721 1.000 142.61785 ? 365 ASP   B N   1 
ATOM   4609 C CA  . ASP   B 2 272 ? 23.85362 -25.46820 -17.58475 1.000 157.65387 ? 365 ASP   B CA  1 
ATOM   4610 C C   . ASP   B 2 272 ? 24.32351 -25.61001 -19.02692 1.000 154.27704 ? 365 ASP   B C   1 
ATOM   4611 O O   . ASP   B 2 272 ? 23.98830 -26.58548 -19.70679 1.000 155.60517 ? 365 ASP   B O   1 
ATOM   4612 C CB  . ASP   B 2 272 ? 23.57787 -26.84255 -16.97255 1.000 161.60928 ? 365 ASP   B CB  1 
ATOM   4613 C CG  . ASP   B 2 272 ? 23.41565 -26.78501 -15.46665 1.000 169.71637 ? 365 ASP   B CG  1 
ATOM   4614 O OD1 . ASP   B 2 272 ? 23.50356 -25.67462 -14.90136 1.000 163.78546 ? 365 ASP   B OD1 1 
ATOM   4615 O OD2 . ASP   B 2 272 ? 23.20365 -27.84876 -14.84763 1.000 180.32500 ? 365 ASP   B OD2 1 
ATOM   4616 N N   . SER   B 2 273 ? 25.09918 -24.63380 -19.49927 1.000 116.61278 ? 366 SER   B N   1 
ATOM   4617 C CA  . SER   B 2 273 ? 25.66050 -24.64784 -20.84213 1.000 131.02409 ? 366 SER   B CA  1 
ATOM   4618 C C   . SER   B 2 273 ? 27.11454 -25.10517 -20.85637 1.000 130.90144 ? 366 SER   B C   1 
ATOM   4619 O O   . SER   B 2 273 ? 27.85684 -24.76416 -21.78370 1.000 132.54743 ? 366 SER   B O   1 
ATOM   4620 C CB  . SER   B 2 273 ? 25.53478 -23.26416 -21.48172 1.000 119.60434 ? 366 SER   B CB  1 
ATOM   4621 O OG  . SER   B 2 273 ? 26.25935 -22.29409 -20.74601 1.000 111.26833 ? 366 SER   B OG  1 
ATOM   4622 N N   . LEU   B 2 274 ? 27.53655 -25.86466 -19.84301 1.000 129.39636 ? 367 LEU   B N   1 
ATOM   4623 C CA  . LEU   B 2 274 ? 28.90715 -26.36435 -19.81064 1.000 121.69466 ? 367 LEU   B CA  1 
ATOM   4624 C C   . LEU   B 2 274 ? 29.15133 -27.35982 -20.93777 1.000 120.75599 ? 367 LEU   B C   1 
ATOM   4625 O O   . LEU   B 2 274 ? 30.09682 -27.20899 -21.72058 1.000 104.31482 ? 367 LEU   B O   1 
ATOM   4626 C CB  . LEU   B 2 274 ? 29.19984 -27.00116 -18.45213 1.000 123.80085 ? 367 LEU   B CB  1 
ATOM   4627 C CG  . LEU   B 2 274 ? 28.99954 -26.10299 -17.22986 1.000 125.17378 ? 367 LEU   B CG  1 
ATOM   4628 C CD1 . LEU   B 2 274 ? 29.34611 -26.85007 -15.95046 1.000 128.83907 ? 367 LEU   B CD1 1 
ATOM   4629 C CD2 . LEU   B 2 274 ? 29.82526 -24.83140 -17.35608 1.000 108.24238 ? 367 LEU   B CD2 1 
ATOM   4630 N N   . ASP   B 2 275 ? 28.30453 -28.38678 -21.03723 1.000 129.75199 ? 368 ASP   B N   1 
ATOM   4631 C CA  . ASP   B 2 275 ? 28.41171 -29.33112 -22.14173 1.000 140.88239 ? 368 ASP   B CA  1 
ATOM   4632 C C   . ASP   B 2 275 ? 28.03385 -28.70043 -23.47488 1.000 132.57980 ? 368 ASP   B C   1 
ATOM   4633 O O   . ASP   B 2 275 ? 28.41082 -29.22853 -24.52491 1.000 134.81768 ? 368 ASP   B O   1 
ATOM   4634 C CB  . ASP   B 2 275 ? 27.53872 -30.55849 -21.87289 1.000 146.48674 ? 368 ASP   B CB  1 
ATOM   4635 C CG  . ASP   B 2 275 ? 26.12277 -30.19184 -21.47359 1.000 149.89679 ? 368 ASP   B CG  1 
ATOM   4636 O OD1 . ASP   B 2 275 ? 25.36787 -29.69665 -22.33551 1.000 148.66931 ? 368 ASP   B OD1 1 
ATOM   4637 O OD2 . ASP   B 2 275 ? 25.76365 -30.40095 -20.29589 1.000 162.01848 ? 368 ASP   B OD2 1 
ATOM   4638 N N   . LEU   B 2 276 ? 27.29958 -27.58629 -23.45803 1.000 128.47643 ? 369 LEU   B N   1 
ATOM   4639 C CA  . LEU   B 2 276 ? 26.97896 -26.89720 -24.70275 1.000 129.29582 ? 369 LEU   B CA  1 
ATOM   4640 C C   . LEU   B 2 276 ? 28.21701 -26.27363 -25.33318 1.000 122.67982 ? 369 LEU   B C   1 
ATOM   4641 O O   . LEU   B 2 276 ? 28.29032 -26.15014 -26.56109 1.000 113.75431 ? 369 LEU   B O   1 
ATOM   4642 C CB  . LEU   B 2 276 ? 25.91418 -25.82998 -24.45032 1.000 130.73097 ? 369 LEU   B CB  1 
ATOM   4643 C CG  . LEU   B 2 276 ? 24.46485 -26.17935 -24.79649 1.000 119.40078 ? 369 LEU   B CG  1 
ATOM   4644 C CD1 . LEU   B 2 276 ? 24.14417 -27.62694 -24.46446 1.000 128.92654 ? 369 LEU   B CD1 1 
ATOM   4645 C CD2 . LEU   B 2 276 ? 23.51920 -25.24601 -24.06629 1.000 113.13452 ? 369 LEU   B CD2 1 
ATOM   4646 N N   . LEU   B 2 277 ? 29.19724 -25.88253 -24.51653 1.000 118.31561 ? 370 LEU   B N   1 
ATOM   4647 C CA  . LEU   B 2 277 ? 30.40831 -25.26733 -25.04722 1.000 113.76604 ? 370 LEU   B CA  1 
ATOM   4648 C C   . LEU   B 2 277 ? 31.33721 -26.29999 -25.67479 1.000 126.13942 ? 370 LEU   B C   1 
ATOM   4649 O O   . LEU   B 2 277 ? 31.96446 -26.02710 -26.70452 1.000 116.89072 ? 370 LEU   B O   1 
ATOM   4650 C CB  . LEU   B 2 277 ? 31.13492 -24.50045 -23.94181 1.000 98.09419  ? 370 LEU   B CB  1 
ATOM   4651 C CG  . LEU   B 2 277 ? 32.45080 -23.82665 -24.33745 1.000 113.11560 ? 370 LEU   B CG  1 
ATOM   4652 C CD1 . LEU   B 2 277 ? 32.20993 -22.72279 -25.35653 1.000 102.30340 ? 370 LEU   B CD1 1 
ATOM   4653 C CD2 . LEU   B 2 277 ? 33.16967 -23.28600 -23.11257 1.000 98.00784  ? 370 LEU   B CD2 1 
ATOM   4654 N N   . ASP   B 2 278 ? 31.44011 -27.48875 -25.07449 1.000 130.72149 ? 371 ASP   B N   1 
ATOM   4655 C CA  . ASP   B 2 278 ? 32.33985 -28.50356 -25.61000 1.000 147.97301 ? 371 ASP   B CA  1 
ATOM   4656 C C   . ASP   B 2 278 ? 31.79336 -29.14941 -26.87680 1.000 157.68194 ? 371 ASP   B C   1 
ATOM   4657 O O   . ASP   B 2 278 ? 32.57473 -29.68862 -27.66761 1.000 152.24990 ? 371 ASP   B O   1 
ATOM   4658 C CB  . ASP   B 2 278 ? 32.63143 -29.57077 -24.54946 1.000 158.93209 ? 371 ASP   B CB  1 
ATOM   4659 C CG  . ASP   B 2 278 ? 31.84997 -30.85440 -24.77087 1.000 172.43696 ? 371 ASP   B CG  1 
ATOM   4660 O OD1 . ASP   B 2 278 ? 30.60269 -30.81524 -24.75087 1.000 170.94015 ? 371 ASP   B OD1 1 
ATOM   4661 O OD2 . ASP   B 2 278 ? 32.48933 -31.90928 -24.96668 1.000 184.24517 ? 371 ASP   B OD2 1 
ATOM   4662 N N   . LYS   B 2 279 ? 30.47501 -29.10838 -27.08807 1.000 143.22061 ? 372 LYS   B N   1 
ATOM   4663 C CA  . LYS   B 2 279 ? 29.90629 -29.61675 -28.33069 1.000 132.86605 ? 372 LYS   B CA  1 
ATOM   4664 C C   . LYS   B 2 279 ? 30.27710 -28.75238 -29.52731 1.000 122.38979 ? 372 LYS   B C   1 
ATOM   4665 O O   . LYS   B 2 279 ? 30.28026 -29.24986 -30.65816 1.000 125.16145 ? 372 LYS   B O   1 
ATOM   4666 C CB  . LYS   B 2 279 ? 28.38381 -29.71674 -28.21759 1.000 116.82518 ? 372 LYS   B CB  1 
ATOM   4667 C CG  . LYS   B 2 279 ? 27.89637 -30.76738 -27.23429 1.000 122.90306 ? 372 LYS   B CG  1 
ATOM   4668 C CD  . LYS   B 2 279 ? 26.38814 -30.69512 -27.05539 1.000 118.66382 ? 372 LYS   B CD  1 
ATOM   4669 C CE  . LYS   B 2 279 ? 25.90939 -31.67021 -25.99198 1.000 123.18743 ? 372 LYS   B CE  1 
ATOM   4670 N NZ  . LYS   B 2 279 ? 24.44351 -31.55845 -25.75378 1.000 121.16166 ? 372 LYS   B NZ  1 
ATOM   4671 N N   . ALA   B 2 280 ? 30.58846 -27.47333 -29.30481 1.000 131.20894 ? 373 ALA   B N   1 
ATOM   4672 C CA  . ALA   B 2 280 ? 30.98314 -26.59868 -30.40139 1.000 127.64250 ? 373 ALA   B CA  1 
ATOM   4673 C C   . ALA   B 2 280 ? 32.37101 -26.92727 -30.93383 1.000 144.97394 ? 373 ALA   B C   1 
ATOM   4674 O O   . ALA   B 2 280 ? 32.66431 -26.61967 -32.09372 1.000 143.23166 ? 373 ALA   B O   1 
ATOM   4675 C CB  . ALA   B 2 280 ? 30.92954 -25.13712 -29.95512 1.000 112.00202 ? 373 ALA   B CB  1 
ATOM   4676 N N   . ARG   B 2 281 ? 33.22759 -27.53970 -30.12076 1.000 145.81799 ? 374 ARG   B N   1 
ATOM   4677 C CA  . ARG   B 2 281 ? 34.56085 -27.90275 -30.57979 1.000 132.95083 ? 374 ARG   B CA  1 
ATOM   4678 C C   . ARG   B 2 281 ? 34.47501 -29.04128 -31.58891 1.000 147.59957 ? 374 ARG   B C   1 
ATOM   4679 O O   . ARG   B 2 281 ? 33.78856 -30.04126 -31.35415 1.000 148.63322 ? 374 ARG   B O   1 
ATOM   4680 C CB  . ARG   B 2 281 ? 35.43959 -28.30308 -29.39635 1.000 143.16814 ? 374 ARG   B CB  1 
ATOM   4681 C CG  . ARG   B 2 281 ? 36.87202 -28.63820 -29.77620 1.000 152.66438 ? 374 ARG   B CG  1 
ATOM   4682 C CD  . ARG   B 2 281 ? 37.70538 -28.97535 -28.55136 1.000 149.45951 ? 374 ARG   B CD  1 
ATOM   4683 N NE  . ARG   B 2 281 ? 39.07768 -29.31821 -28.90456 1.000 158.32391 ? 374 ARG   B NE  1 
ATOM   4684 C CZ  . ARG   B 2 281 ? 40.01603 -29.65066 -28.02872 1.000 167.79738 ? 374 ARG   B CZ  1 
ATOM   4685 N NH1 . ARG   B 2 281 ? 39.76557 -29.69410 -26.73037 1.000 177.04758 ? 374 ARG   B NH1 1 
ATOM   4686 N NH2 . ARG   B 2 281 ? 41.23640 -29.94713 -28.46650 1.000 169.59183 ? 374 ARG   B NH2 1 
ATOM   4687 N N   . ALA   B 2 282 ? 35.17146 -28.88040 -32.71270 1.000 148.27241 ? 375 ALA   B N   1 
ATOM   4688 C CA  . ALA   B 2 282 ? 35.17379 -29.85840 -33.80017 1.000 130.16078 ? 375 ALA   B CA  1 
ATOM   4689 C C   . ALA   B 2 282 ? 33.75904 -30.16159 -34.28635 1.000 135.10500 ? 375 ALA   B C   1 
ATOM   4690 O O   . ALA   B 2 282 ? 32.99541 -29.25149 -34.61012 1.000 125.09794 ? 375 ALA   B O   1 
ATOM   4691 C CB  . ALA   B 2 282 ? 35.87394 -31.14194 -33.36490 1.000 132.26231 ? 375 ALA   B CB  1 
HETATM 4692 C C13 . A1CAI C 3 .   ? 37.42419 21.61386  -8.69368  1.000 50.62058  ? 301 A1CAI A C13 1 
HETATM 4693 C C14 . A1CAI C 3 .   ? 37.20246 20.09951  -8.70730  1.000 45.16106  ? 301 A1CAI A C14 1 
HETATM 4694 C C15 . A1CAI C 3 .   ? 36.97472 19.43972  -7.31674  1.000 48.76002  ? 301 A1CAI A C15 1 
HETATM 4695 C C16 . A1CAI C 3 .   ? 35.90269 18.36672  -7.48081  1.000 48.86604  ? 301 A1CAI A C16 1 
HETATM 4696 C C17 . A1CAI C 3 .   ? 34.99393 18.87888  -8.62273  1.000 50.05417  ? 301 A1CAI A C17 1 
HETATM 4697 C C18 . A1CAI C 3 .   ? 35.98875 19.66827  -9.54519  1.000 48.76574  ? 301 A1CAI A C18 1 
HETATM 4698 C C20 . A1CAI C 3 .   ? 32.97801 19.14871  -7.34745  1.000 52.31662  ? 301 A1CAI A C20 1 
HETATM 4699 C C22 . A1CAI C 3 .   ? 32.68322 21.48814  -6.39180  1.000 59.15443  ? 301 A1CAI A C22 1 
HETATM 4700 C C23 . A1CAI C 3 .   ? 31.64639 22.19731  -7.30818  1.000 55.03489  ? 301 A1CAI A C23 1 
HETATM 4701 C C24 . A1CAI C 3 .   ? 32.64773 22.11134  -4.96645  1.000 71.61925  ? 301 A1CAI A C24 1 
HETATM 4702 C C26 . A1CAI C 3 .   ? 36.79215 22.60590  -7.93169  1.000 41.56610  ? 301 A1CAI A C26 1 
HETATM 4703 C C28 . A1CAI C 3 .   ? 35.55273 27.72144  -3.72812  1.000 66.82748  ? 301 A1CAI A C28 1 
HETATM 4704 C C29 . A1CAI C 3 .   ? 36.18645 28.17834  -2.55233  1.000 59.31996  ? 301 A1CAI A C29 1 
HETATM 4705 C C01 . A1CAI C 3 .   ? 37.76308 28.34381  -0.12453  1.000 73.83803  ? 301 A1CAI A C01 1 
HETATM 4706 C C03 . A1CAI C 3 .   ? 37.56549 28.45048  -2.53877  1.000 56.73165  ? 301 A1CAI A C03 1 
HETATM 4707 C C04 . A1CAI C 3 .   ? 38.26591 28.24157  -3.73749  1.000 60.04950  ? 301 A1CAI A C04 1 
HETATM 4708 C C05 . A1CAI C 3 .   ? 37.60567 27.78383  -4.90229  1.000 63.87768  ? 301 A1CAI A C05 1 
HETATM 4709 C C06 . A1CAI C 3 .   ? 36.21751 27.50224  -4.94843  1.000 59.49025  ? 301 A1CAI A C06 1 
HETATM 4710 C C07 . A1CAI C 3 .   ? 35.45352 26.99151  -6.23047  1.000 60.83230  ? 301 A1CAI A C07 1 
HETATM 4711 C C08 . A1CAI C 3 .   ? 35.84964 25.53507  -6.81717  1.000 49.68113  ? 301 A1CAI A C08 1 
HETATM 4712 C C10 . A1CAI C 3 .   ? 37.34701 23.91060  -8.27297  1.000 49.96956  ? 301 A1CAI A C10 1 
HETATM 4713 N N09 . A1CAI C 3 .   ? 36.96246 25.22776  -7.71055  1.000 50.50796  ? 301 A1CAI A N09 1 
HETATM 4714 N N11 . A1CAI C 3 .   ? 38.30543 23.68079  -9.24095  1.000 52.26969  ? 301 A1CAI A N11 1 
HETATM 4715 N N12 . A1CAI C 3 .   ? 38.33643 22.32582  -9.47298  1.000 48.42026  ? 301 A1CAI A N12 1 
HETATM 4716 N N21 . A1CAI C 3 .   ? 32.42012 20.00359  -6.36205  1.000 66.05114  ? 301 A1CAI A N21 1 
HETATM 4717 O O02 . A1CAI C 3 .   ? 38.17452 28.89777  -1.37247  1.000 73.17909  ? 301 A1CAI A O02 1 
HETATM 4718 O O19 . A1CAI C 3 .   ? 33.95523 19.75009  -8.17474  1.000 49.81512  ? 301 A1CAI A O19 1 
HETATM 4719 O O25 . A1CAI C 3 .   ? 32.69357 17.99412  -7.52190  1.000 60.92242  ? 301 A1CAI A O25 1 
HETATM 4720 O O27 . A1CAI C 3 .   ? 35.12558 24.63412  -6.46214  1.000 55.42053  ? 301 A1CAI A O27 1 
HETATM 4721 O O   . HOH   D 4 .   ? 26.34577 18.34237  -6.81978  1.000 57.92677  ? 401 HOH   A O   1 
HETATM 4722 O O   . HOH   D 4 .   ? 34.87846 33.07216  -16.54045 1.000 54.81141  ? 402 HOH   A O   1 
HETATM 4723 O O   . HOH   D 4 .   ? 29.43936 6.33579   -26.51951 1.000 59.30494  ? 403 HOH   A O   1 
HETATM 4724 O O   . HOH   D 4 .   ? 44.73619 23.26317  -12.26464 1.000 55.16188  ? 404 HOH   A O   1 
HETATM 4725 O O   . HOH   D 4 .   ? 18.35641 16.64317  -25.73833 1.000 48.28639  ? 405 HOH   A O   1 
HETATM 4726 O O   . HOH   D 4 .   ? 30.31807 25.26832  -5.55835  1.000 47.04961  ? 406 HOH   A O   1 
HETATM 4727 O O   . HOH   D 4 .   ? 8.25812  26.89636  -22.56196 1.000 64.63021  ? 407 HOH   A O   1 
HETATM 4728 O O   . HOH   D 4 .   ? 15.97002 6.36822   -18.19894 1.000 56.52921  ? 408 HOH   A O   1 
HETATM 4729 O O   . HOH   D 4 .   ? -3.95714 19.49964  -17.67333 1.000 72.90823  ? 409 HOH   A O   1 
HETATM 4730 O O   . HOH   D 4 .   ? 28.07141 15.12832  -5.61871  1.000 58.37799  ? 410 HOH   A O   1 
HETATM 4731 O O   . HOH   D 4 .   ? 25.95704 8.66894   -10.66573 1.000 52.38765  ? 411 HOH   A O   1 
HETATM 4732 O O   . HOH   D 4 .   ? 21.07675 17.46106  -25.84585 1.000 45.57625  ? 412 HOH   A O   1 
HETATM 4733 O O   . HOH   D 4 .   ? 16.33455 18.60510  -14.75068 1.000 45.01711  ? 413 HOH   A O   1 
HETATM 4734 O O   . HOH   D 4 .   ? 26.60717 14.77257  -11.96708 1.000 45.00672  ? 414 HOH   A O   1 
HETATM 4735 O O   . HOH   D 4 .   ? 38.82210 21.72433  -19.01368 1.000 51.72583  ? 415 HOH   A O   1 
HETATM 4736 O O   . HOH   D 4 .   ? 14.99525 13.02489  -21.77012 1.000 47.03384  ? 416 HOH   A O   1 
HETATM 4737 O O   . HOH   D 4 .   ? 33.53279 34.77342  -21.87104 1.000 64.61307  ? 417 HOH   A O   1 
HETATM 4738 O O   . HOH   D 4 .   ? 28.35695 8.15841   -28.65336 1.000 49.32971  ? 418 HOH   A O   1 
HETATM 4739 O O   . HOH   D 4 .   ? 25.32465 16.72241  -28.79014 1.000 62.33232  ? 419 HOH   A O   1 
HETATM 4740 O O   . HOH   D 4 .   ? 23.13169 4.19565   -8.13083  1.000 66.18269  ? 420 HOH   A O   1 
HETATM 4741 O O   . HOH   D 4 .   ? 16.90502 29.19113  -11.71152 1.000 48.54643  ? 421 HOH   A O   1 
HETATM 4742 O O   . HOH   D 4 .   ? 34.05572 17.23510  -11.58038 1.000 51.06540  ? 422 HOH   A O   1 
HETATM 4743 O O   . HOH   D 4 .   ? 13.47799 13.69891  -20.05306 1.000 47.72954  ? 423 HOH   A O   1 
HETATM 4744 O O   . HOH   D 4 .   ? 10.97471 14.22953  -8.16450  1.000 54.29387  ? 424 HOH   A O   1 
HETATM 4745 O O   . HOH   D 4 .   ? 36.82246 35.92336  -16.63705 1.000 71.81513  ? 425 HOH   A O   1 
HETATM 4746 O O   . HOH   D 4 .   ? 23.90441 30.10613  -33.56638 1.000 65.42360  ? 426 HOH   A O   1 
HETATM 4747 O O   . HOH   D 4 .   ? 34.23266 17.80149  -14.38819 1.000 49.62466  ? 427 HOH   A O   1 
HETATM 4748 O O   . HOH   D 4 .   ? 15.00506 27.40753  -10.62867 1.000 47.15407  ? 428 HOH   A O   1 
HETATM 4749 O O   . HOH   D 4 .   ? 20.92907 18.39834  -14.71234 1.000 43.52480  ? 429 HOH   A O   1 
HETATM 4750 O O   . HOH   D 4 .   ? 32.97011 25.72497  -2.09156  1.000 62.80758  ? 430 HOH   A O   1 
HETATM 4751 O O   . HOH   D 4 .   ? 20.71390 33.70858  -8.36380  1.000 61.68879  ? 431 HOH   A O   1 
HETATM 4752 O O   . HOH   D 4 .   ? 16.45477 18.31244  -24.72410 1.000 45.35094  ? 432 HOH   A O   1 
HETATM 4753 O O   . HOH   D 4 .   ? 12.80058 23.27554  -12.17031 1.000 41.77063  ? 433 HOH   A O   1 
HETATM 4754 O O   . HOH   D 4 .   ? 37.66276 17.67946  -19.52920 1.000 58.87341  ? 434 HOH   A O   1 
HETATM 4755 O O   . HOH   D 4 .   ? 8.65008  30.37097  -9.41043  1.000 67.93179  ? 435 HOH   A O   1 
HETATM 4756 O O   . HOH   D 4 .   ? 40.35833 30.20211  -11.96042 1.000 64.43274  ? 436 HOH   A O   1 
HETATM 4757 O O   . HOH   D 4 .   ? 43.70809 25.48973  -13.61956 1.000 68.44502  ? 437 HOH   A O   1 
HETATM 4758 O O   . HOH   D 4 .   ? 11.65994 11.87267  -19.84112 1.000 47.65966  ? 438 HOH   A O   1 
HETATM 4759 O O   . HOH   D 4 .   ? 16.28135 19.92747  -30.72001 1.000 51.48671  ? 439 HOH   A O   1 
HETATM 4760 O O   . HOH   D 4 .   ? 32.75428 25.43713  -4.76781  1.000 55.55518  ? 440 HOH   A O   1 
HETATM 4761 O O   . HOH   D 4 .   ? 5.82384  23.74047  -23.37516 1.000 58.39367  ? 441 HOH   A O   1 
HETATM 4762 O O   . HOH   D 4 .   ? 25.81135 1.99554   -4.83829  1.000 63.30423  ? 442 HOH   A O   1 
HETATM 4763 O O   . HOH   D 4 .   ? 27.03376 34.70753  -1.54636  1.000 75.88210  ? 443 HOH   A O   1 
HETATM 4764 O O   . HOH   D 4 .   ? 29.25799 23.73943  -3.63458  1.000 58.29745  ? 444 HOH   A O   1 
HETATM 4765 O O   . HOH   D 4 .   ? 14.79316 21.65312  -31.66565 1.000 63.16823  ? 445 HOH   A O   1 
HETATM 4766 O O   . HOH   D 4 .   ? 34.40562 36.95078  -21.51379 1.000 72.14933  ? 446 HOH   A O   1 
HETATM 4767 O O   . HOH   E 4 .   ? 22.94935 17.94136  -28.11405 1.000 53.67050  ? 401 HOH   B O   1 
HETATM 4768 O O   . HOH   E 4 .   ? 17.45762 18.55773  -32.82929 1.000 71.55299  ? 402 HOH   B O   1 
HETATM 4769 O O   . HOH   E 4 .   ? 28.46798 -1.06288  -22.41493 1.000 62.78186  ? 403 HOH   B O   1 
HETATM 4770 O O   . HOH   E 4 .   ? 20.17987 -6.25135  -21.18163 1.000 55.59814  ? 404 HOH   B O   1 
HETATM 4771 O O   . HOH   E 4 .   ? 23.01486 -0.34791  -25.74776 1.000 61.62077  ? 405 HOH   B O   1 
HETATM 4772 O O   . HOH   E 4 .   ? 16.17163 -12.16705 -18.61432 1.000 61.17874  ? 406 HOH   B O   1 
HETATM 4773 O O   . HOH   E 4 .   ? 25.24848 1.88403   -7.69628  1.000 62.73055  ? 407 HOH   B O   1 
HETATM 4774 O O   . HOH   E 4 .   ? 23.49052 -12.15742 -21.14169 1.000 62.19564  ? 408 HOH   B O   1 
HETATM 4775 O O   . HOH   E 4 .   ? 30.00929 17.21478  -29.48602 1.000 67.53174  ? 409 HOH   B O   1 
HETATM 4776 O O   . HOH   E 4 .   ? 23.64957 -2.84764  -22.25775 1.000 58.93674  ? 410 HOH   B O   1 
HETATM 4777 O O   . HOH   E 4 .   ? 30.46819 1.32611   -16.95607 1.000 55.92418  ? 411 HOH   B O   1 
HETATM 4778 O O   . HOH   E 4 .   ? 21.53416 -5.22228  -18.94220 1.000 58.73843  ? 412 HOH   B 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   . MET   A 4   ? 1.18626 1.85939 1.60747 0.19360  -0.21757 -0.32174 1   MET   A N   
2    C CA  . MET   A 4   ? 1.31912 1.98761 1.73933 0.16477  -0.20357 -0.30302 1   MET   A CA  
3    C C   . MET   A 4   ? 1.55299 2.24960 1.99107 0.15053  -0.20086 -0.31103 1   MET   A C   
4    O O   . MET   A 4   ? 1.52602 2.19992 1.94943 0.15751  -0.22025 -0.30974 1   MET   A O   
5    C CB  . MET   A 4   ? 1.39423 1.99797 1.77283 0.17067  -0.21937 -0.28249 1   MET   A CB  
6    C CG  . MET   A 4   ? 1.32684 1.90144 1.68694 0.13839  -0.19736 -0.25696 1   MET   A CG  
7    S SD  . MET   A 4   ? 1.17530 1.75088 1.53799 0.11250  -0.16253 -0.23917 1   MET   A SD  
8    C CE  . MET   A 4   ? 1.17121 1.81935 1.58174 0.08601  -0.14072 -0.25198 1   MET   A CE  
9    N N   . GLU   A 5   ? 1.88242 2.62582 2.34898 0.12997  -0.17746 -0.31911 2   GLU   A N   
10   C CA  . GLU   A 5   ? 1.78742 2.55900 2.27178 0.11366  -0.17316 -0.32689 2   GLU   A CA  
11   C C   . GLU   A 5   ? 1.68192 2.48205 2.18284 0.07862  -0.14105 -0.32041 2   GLU   A C   
12   O O   . GLU   A 5   ? 1.64933 2.44286 2.14507 0.06779  -0.12376 -0.30823 2   GLU   A O   
13   C CB  . GLU   A 5   ? 1.64272 2.44343 2.14313 0.13462  -0.18798 -0.35290 2   GLU   A CB  
14   C CG  . GLU   A 5   ? 1.61900 2.45725 2.13820 0.14030  -0.17643 -0.36962 2   GLU   A CG  
15   C CD  . GLU   A 5   ? 1.66403 2.53860 2.20335 0.15684  -0.18870 -0.39739 2   GLU   A CD  
16   O OE1 . GLU   A 5   ? 1.68052 2.55778 2.22383 0.15724  -0.20103 -0.40258 2   GLU   A OE1 
17   O OE2 . GLU   A 5   ? 1.56497 2.46619 2.11608 0.16966  -0.18644 -0.41500 2   GLU   A OE2 
18   N N   . ASN   A 6   ? 1.25322 2.08154 1.77119 0.06058  -0.13405 -0.32800 3   ASN   A N   
19   C CA  . ASN   A 6   ? 1.03075 1.88222 1.56040 0.02633  -0.10573 -0.32265 3   ASN   A CA  
20   C C   . ASN   A 6   ? 0.86202 1.68052 1.37446 0.00271  -0.09211 -0.29765 3   ASN   A C   
21   O O   . ASN   A 6   ? 0.84432 1.67018 1.35898 -0.02606 -0.06918 -0.28928 3   ASN   A O   
22   C CB  . ASN   A 6   ? 0.86879 1.74893 1.40882 0.02530  -0.08948 -0.33104 3   ASN   A CB  
23   C CG  . ASN   A 6   ? 1.06811 1.99504 1.63190 0.03395  -0.09331 -0.35763 3   ASN   A CG  
24   O OD1 . ASN   A 6   ? 1.06638 2.01064 1.64257 0.02941  -0.09996 -0.36746 3   ASN   A OD1 
25   N ND2 . ASN   A 6   ? 1.01590 1.96495 1.58654 0.04622  -0.08919 -0.37051 3   ASN   A ND2 
26   N N   . PHE   A 7   ? 0.84622 1.62653 1.33925 0.01467  -0.10665 -0.28600 4   PHE   A N   
27   C CA  . PHE   A 7   ? 0.75687 1.50585 1.23352 -0.00495 -0.09614 -0.26431 4   PHE   A CA  
28   C C   . PHE   A 7   ? 0.66446 1.39217 1.13071 -0.00454 -0.11302 -0.26184 4   PHE   A C   
29   O O   . PHE   A 7   ? 0.68714 1.39988 1.14316 0.02079  -0.13824 -0.26785 4   PHE   A O   
30   C CB  . PHE   A 7   ? 0.85901 1.58220 1.32004 0.00646  -0.09596 -0.25210 4   PHE   A CB  
31   C CG  . PHE   A 7   ? 0.95281 1.68569 1.41677 -0.00779 -0.07144 -0.24534 4   PHE   A CG  
32   C CD1 . PHE   A 7   ? 0.88164 1.62911 1.35188 -0.03694 -0.04897 -0.24156 4   PHE   A CD1 
33   C CD2 . PHE   A 7   ? 0.87404 1.59784 1.33100 0.00795  -0.07225 -0.24254 4   PHE   A CD2 
34   C CE1 . PHE   A 7   ? 0.88039 1.63213 1.34785 -0.04982 -0.02824 -0.23468 4   PHE   A CE1 
35   C CE2 . PHE   A 7   ? 0.90217 1.63348 1.35924 -0.00495 -0.05070 -0.23658 4   PHE   A CE2 
36   C CZ  . PHE   A 7   ? 1.04632 1.79098 1.50755 -0.03375 -0.02891 -0.23240 4   PHE   A CZ  
37   N N   . GLN   A 8   ? 0.60496 1.32700 1.06970 -0.03235 -0.10001 -0.25290 5   GLN   A N   
38   C CA  . GLN   A 8   ? 0.62809 1.31953 1.07435 -0.03550 -0.11130 -0.24781 5   GLN   A CA  
39   C C   . GLN   A 8   ? 0.61257 1.24527 1.02266 -0.04970 -0.09675 -0.22082 5   GLN   A C   
40   O O   . GLN   A 8   ? 0.56608 1.20044 0.97939 -0.07296 -0.07519 -0.21141 5   GLN   A O   
41   C CB  . GLN   A 8   ? 0.49167 1.21769 0.96094 -0.05455 -0.10898 -0.26094 5   GLN   A CB  
42   C CG  . GLN   A 8   ? 0.82719 1.52801 1.28105 -0.05972 -0.12129 -0.25873 5   GLN   A CG  
43   C CD  . GLN   A 8   ? 0.88490 1.61412 1.35793 -0.07877 -0.11826 -0.27042 5   GLN   A CD  
44   O OE1 . GLN   A 8   ? 1.03430 1.74927 1.49891 -0.08747 -0.12653 -0.27084 5   GLN   A OE1 
45   N NE2 . GLN   A 8   ? 0.91855 1.68326 1.41291 -0.08538 -0.10569 -0.27919 5   GLN   A NE2 
46   N N   . LYS   A 9   ? 0.63805 1.21919 1.01286 -0.03564 -0.10888 -0.20910 6   LYS   A N   
47   C CA  . LYS   A 9   ? 0.62297 1.15148 0.96476 -0.04701 -0.09624 -0.18589 6   LYS   A CA  
48   C C   . LYS   A 9   ? 0.50678 1.03383 0.85058 -0.07182 -0.08654 -0.18373 6   LYS   A C   
49   O O   . LYS   A 9   ? 0.49250 1.03100 0.84247 -0.07321 -0.09854 -0.19531 6   LYS   A O   
50   C CB  . LYS   A 9   ? 0.66764 1.14615 0.97162 -0.02844 -0.11152 -0.17652 6   LYS   A CB  
51   C CG  . LYS   A 9   ? 0.71943 1.18622 1.01300 -0.00584 -0.12069 -0.17498 6   LYS   A CG  
52   C CD  . LYS   A 9   ? 0.78023 1.19354 1.03157 0.00839  -0.13518 -0.16462 6   LYS   A CD  
53   C CE  . LYS   A 9   ? 0.90678 1.30296 1.14427 0.02917  -0.14513 -0.16250 6   LYS   A CE  
54   N NZ  . LYS   A 9   ? 1.11561 1.45688 1.30788 0.04049  -0.15949 -0.15200 6   LYS   A NZ  
55   N N   . VAL   A 10  ? 0.44592 0.95692 0.78320 -0.09082 -0.06614 -0.16935 7   VAL   A N   
56   C CA  . VAL   A 10  ? 0.63715 1.14077 0.97319 -0.11494 -0.05636 -0.16617 7   VAL   A CA  
57   C C   . VAL   A 10  ? 0.55569 1.00403 0.85636 -0.11543 -0.05402 -0.14963 7   VAL   A C   
58   O O   . VAL   A 10  ? 0.59800 1.03252 0.88982 -0.12332 -0.05809 -0.15164 7   VAL   A O   
59   C CB  . VAL   A 10  ? 0.64481 1.16902 0.99727 -0.13744 -0.03622 -0.16331 7   VAL   A CB  
60   C CG1 . VAL   A 10  ? 0.60038 1.10921 0.94670 -0.16281 -0.02748 -0.15907 7   VAL   A CG1 
61   C CG2 . VAL   A 10  ? 0.65333 1.23807 1.04223 -0.13873 -0.03687 -0.18205 7   VAL   A CG2 
62   N N   . GLU   A 11  ? 0.59104 1.00941 0.87204 -0.10717 -0.04746 -0.13455 8   GLU   A N   
63   C CA  . GLU   A 11  ? 0.62931 1.00060 0.87962 -0.10794 -0.04302 -0.12006 8   GLU   A CA  
64   C C   . GLU   A 11  ? 0.55946 0.90817 0.79270 -0.09392 -0.04081 -0.10805 8   GLU   A C   
65   O O   . GLU   A 11  ? 0.52940 0.89426 0.77463 -0.09032 -0.03621 -0.10697 8   GLU   A O   
66   C CB  . GLU   A 11  ? 0.64277 1.00193 0.89193 -0.12894 -0.02740 -0.11248 8   GLU   A CB  
67   C CG  . GLU   A 11  ? 0.94627 1.26161 1.16723 -0.12936 -0.02401 -0.10178 8   GLU   A CG  
68   C CD  . GLU   A 11  ? 1.10638 1.40726 1.32544 -0.14752 -0.01114 -0.09548 8   GLU   A CD  
69   O OE1 . GLU   A 11  ? 0.85172 1.17243 1.08748 -0.16070 -0.00329 -0.09623 8   GLU   A OE1 
70   O OE2 . GLU   A 11  ? 1.04731 1.31584 1.24643 -0.14851 -0.00919 -0.09024 8   GLU   A OE2 
71   N N   . LYS   A 12  ? 0.48799 0.80000 0.69252 -0.08711 -0.04382 -0.09976 9   LYS   A N   
72   C CA  . LYS   A 12  ? 0.58449 0.87233 0.77050 -0.07759 -0.04031 -0.08766 9   LYS   A CA  
73   C C   . LYS   A 12  ? 0.56307 0.83947 0.74861 -0.08844 -0.02256 -0.07584 9   LYS   A C   
74   O O   . LYS   A 12  ? 0.59626 0.85729 0.77467 -0.09835 -0.01564 -0.07247 9   LYS   A O   
75   C CB  . LYS   A 12  ? 0.67452 0.92900 0.82864 -0.06916 -0.04856 -0.08363 9   LYS   A CB  
76   C CG  . LYS   A 12  ? 0.65323 0.88173 0.78629 -0.06290 -0.04379 -0.07105 9   LYS   A CG  
77   C CD  . LYS   A 12  ? 0.72496 0.92139 0.82369 -0.05732 -0.05137 -0.06767 9   LYS   A CD  
78   C CE  . LYS   A 12  ? 0.64304 0.81482 0.72053 -0.05471 -0.04532 -0.05546 9   LYS   A CE  
79   N NZ  . LYS   A 12  ? 0.86267 1.00285 0.90318 -0.05158 -0.05218 -0.05211 9   LYS   A NZ  
80   N N   . ILE   A 13  ? 0.49163 0.77439 0.68380 -0.08532 -0.01658 -0.07036 10  ILE   A N   
81   C CA  . ILE   A 13  ? 0.59435 0.86692 0.78600 -0.09386 -0.00174 -0.05956 10  ILE   A CA  
82   C C   . ILE   A 13  ? 0.58936 0.83067 0.75812 -0.08877 0.00173  -0.04896 10  ILE   A C   
83   O O   . ILE   A 13  ? 0.68919 0.91513 0.85206 -0.09542 0.01103  -0.04270 10  ILE   A O   
84   C CB  . ILE   A 13  ? 0.45675 0.75122 0.66503 -0.09372 0.00324  -0.05917 10  ILE   A CB  
85   C CG1 . ILE   A 13  ? 0.58620 0.91481 0.81812 -0.10367 0.00415  -0.06994 10  ILE   A CG1 
86   C CG2 . ILE   A 13  ? 0.65849 0.93805 0.86167 -0.09926 0.01591  -0.04704 10  ILE   A CG2 
87   C CD1 . ILE   A 13  ? 0.54645 0.89973 0.79398 -0.10478 0.01041  -0.07114 10  ILE   A CD1 
88   N N   A GLY   A 14  ? 0.61784 0.84934 0.77302 -0.07730 -0.00587 -0.04745 11  GLY   A N   
89   N N   B GLY   A 14  ? 0.62353 0.85466 0.77831 -0.07730 -0.00606 -0.04756 11  GLY   A N   
90   C CA  A GLY   A 14  ? 0.71056 0.91570 0.84428 -0.07500 -0.00144 -0.03795 11  GLY   A CA  
91   C CA  B GLY   A 14  ? 0.71092 0.91487 0.84320 -0.07519 -0.00206 -0.03854 11  GLY   A CA  
92   C C   A GLY   A 14  ? 0.74795 0.94162 0.86496 -0.06415 -0.01200 -0.03708 11  GLY   A C   
93   C C   B GLY   A 14  ? 0.75209 0.94313 0.86702 -0.06486 -0.01097 -0.03620 11  GLY   A C   
94   O O   A GLY   A 14  ? 0.59765 0.80275 0.71997 -0.05582 -0.02419 -0.04441 11  GLY   A O   
95   O O   B GLY   A 14  ? 0.61935 0.82209 0.74159 -0.05671 -0.02015 -0.04081 11  GLY   A O   
96   N N   A GLU   A 15  ? 0.79403 0.96450 0.89003 -0.06451 -0.00760 -0.02863 12  GLU   A N   
97   N N   B GLU   A 15  ? 0.75625 0.92232 0.84674 -0.06550 -0.00843 -0.02969 12  GLU   A N   
98   C CA  A GLU   A 15  ? 0.78404 0.93481 0.85650 -0.05715 -0.01719 -0.02583 12  GLU   A CA  
99   C CA  B GLU   A 15  ? 0.77957 0.92601 0.84735 -0.05922 -0.01543 -0.02516 12  GLU   A CA  
100  C C   A GLU   A 15  ? 0.78825 0.92810 0.85403 -0.05987 -0.00853 -0.01624 12  GLU   A C   
101  C C   B GLU   A 15  ? 0.81338 0.94693 0.87179 -0.06552 -0.00269 -0.01546 12  GLU   A C   
102  O O   A GLU   A 15  ? 0.80110 0.94129 0.87087 -0.06758 0.00481  -0.01146 12  GLU   A O   
103  O O   B GLU   A 15  ? 0.84039 0.96678 0.89098 -0.07222 0.00652  -0.01354 12  GLU   A O   
104  C CB  A GLU   A 15  ? 0.77191 0.89997 0.81561 -0.05770 -0.02282 -0.02620 12  GLU   A CB  
105  C CB  B GLU   A 15  ? 0.76896 0.89541 0.80933 -0.05556 -0.02731 -0.02797 12  GLU   A CB  
106  C CG  A GLU   A 15  ? 0.83188 0.93300 0.84435 -0.05146 -0.03455 -0.02260 12  GLU   A CG  
107  C CG  B GLU   A 15  ? 0.83408 0.93289 0.84410 -0.05080 -0.03563 -0.02217 12  GLU   A CG  
108  C CD  A GLU   A 15  ? 0.86172 0.94019 0.84309 -0.05212 -0.04178 -0.02371 12  GLU   A CD  
109  C CD  B GLU   A 15  ? 0.88013 0.95319 0.85596 -0.04982 -0.04547 -0.02284 12  GLU   A CD  
110  O OE1 A GLU   A 15  ? 0.78887 0.87405 0.77443 -0.05724 -0.03669 -0.02779 12  GLU   A OE1 
111  O OE1 B GLU   A 15  ? 0.81902 0.89641 0.79516 -0.05364 -0.04329 -0.02744 12  GLU   A OE1 
112  O OE2 A GLU   A 15  ? 0.97094 1.02219 0.92100 -0.04767 -0.05327 -0.02052 12  GLU   A OE2 
113  O OE2 B GLU   A 15  ? 0.99928 1.04508 0.94527 -0.04556 -0.05602 -0.01871 12  GLU   A OE2 
114  N N   A GLY   A 16  ? 0.79387 0.92394 0.84965 -0.05286 -0.01736 -0.01450 13  GLY   A N   
115  N N   B GLY   A 16  ? 0.78999 0.92233 0.85006 -0.06310 -0.00249 -0.01079 13  GLY   A N   
116  C CA  A GLY   A 16  ? 0.89883 1.01656 0.94600 -0.05614 -0.01128 -0.00605 13  GLY   A CA  
117  C CA  B GLY   A 16  ? 0.82372 0.94806 0.87846 -0.06953 0.00881  -0.00275 13  GLY   A CA  
118  C C   A GLY   A 16  ? 0.87434 0.95978 0.88674 -0.05451 -0.02070 -0.00163 13  GLY   A C   
119  C C   B GLY   A 16  ? 0.84655 0.95996 0.89176 -0.06610 0.00325  0.00160  13  GLY   A C   
120  O O   A GLY   A 16  ? 0.83676 0.90622 0.82793 -0.05134 -0.03099 -0.00404 13  GLY   A O   
121  O O   B GLY   A 16  ? 0.92578 1.02551 0.95525 -0.05885 -0.01050 -0.00022 13  GLY   A O   
122  N N   A THR   A 17  ? 0.79572 0.86900 0.79965 -0.05749 -0.01802 0.00500  14  THR   A N   
123  N N   B THR   A 17  ? 0.76150 0.87948 0.81549 -0.07070 0.01276  0.00680  14  THR   A N   
124  C CA  A THR   A 17  ? 0.76566 0.80319 0.73246 -0.05878 -0.02673 0.01045  14  THR   A CA  
125  C CA  B THR   A 17  ? 0.83456 0.94176 0.88034 -0.06864 0.00795  0.01071  14  THR   A CA  
126  C C   A THR   A 17  ? 0.81488 0.83883 0.76994 -0.04357 -0.04810 0.00500  14  THR   A C   
127  C C   B THR   A 17  ? 0.73378 0.85104 0.79167 -0.05722 -0.00309 0.00515  14  THR   A C   
128  O O   A THR   A 17  ? 0.79141 0.78835 0.71555 -0.04078 -0.06026 0.00526  14  THR   A O   
129  O O   B THR   A 17  ? 0.82750 0.92947 0.87184 -0.05135 -0.01324 0.00562  14  THR   A O   
130  C CB  A THR   A 17  ? 0.90183 0.93119 0.86475 -0.06696 -0.01903 0.01792  14  THR   A CB  
131  C CB  B THR   A 17  ? 0.84610 0.96112 0.90325 -0.07570 0.02000  0.01577  14  THR   A CB  
132  O OG1 A THR   A 17  ? 0.88128 0.91921 0.84850 -0.08084 -0.00121 0.02205  14  THR   A OG1 
133  O OG1 B THR   A 17  ? 0.81961 0.95869 0.90464 -0.07372 0.02562  0.01332  14  THR   A OG1 
134  C CG2 A THR   A 17  ? 0.86298 0.85196 0.78644 -0.06810 -0.03088 0.02327  14  THR   A CG2 
135  C CG2 B THR   A 17  ? 0.77368 0.88324 0.82083 -0.08622 0.03108  0.01890  14  THR   A CG2 
136  N N   A TYR   A 18  ? 0.90277 0.94530 0.88131 -0.03275 -0.05359 -0.00090 15  TYR   A N   
137  N N   B TYR   A 18  ? 0.84186 0.98449 0.92427 -0.05445 -0.00123 -0.00088 15  TYR   A N   
138  C CA  A TYR   A 18  ? 0.94231 0.97741 0.91477 -0.01543 -0.07441 -0.00896 15  TYR   A CA  
139  C CA  B TYR   A 18  ? 0.68735 0.84641 0.78419 -0.04450 -0.00986 -0.00843 15  TYR   A CA  
140  C C   A TYR   A 18  ? 0.96240 1.03292 0.96501 -0.00503 -0.07959 -0.02189 15  TYR   A C   
141  C C   B TYR   A 18  ? 0.80859 0.95804 0.89201 -0.03384 -0.02658 -0.01532 15  TYR   A C   
142  O O   A TYR   A 18  ? 0.93762 1.00346 0.93368 0.00984  -0.09844 -0.03065 15  TYR   A O   
143  O O   B TYR   A 18  ? 0.88301 1.02971 0.96365 -0.02269 -0.03818 -0.01988 15  TYR   A O   
144  C CB  A TYR   A 18  ? 0.77775 0.80816 0.75282 -0.00866 -0.07911 -0.00911 15  TYR   A CB  
145  C CB  B TYR   A 18  ? 0.79878 0.98760 0.92292 -0.04794 -0.00218 -0.01315 15  TYR   A CB  
146  C CG  A TYR   A 18  ? 0.83705 0.83037 0.78089 -0.01896 -0.07705 0.00242  15  TYR   A CG  
147  C CG  B TYR   A 18  ? 0.73733 0.92698 0.86277 -0.05591 0.00405  -0.01290 15  TYR   A CG  
148  C CD1 A TYR   A 18  ? 0.87130 0.81905 0.77154 -0.01822 -0.09125 0.00702  15  TYR   A CD1 
149  C CD1 B TYR   A 18  ? 0.63243 0.82523 0.75635 -0.05348 -0.00379 -0.02012 15  TYR   A CD1 
150  C CD2 A TYR   A 18  ? 0.87552 0.87846 0.83199 -0.03034 -0.06160 0.00851  15  TYR   A CD2 
151  C CD2 B TYR   A 18  ? 0.62337 0.81042 0.75151 -0.06471 0.01650  -0.00662 15  TYR   A CD2 
152  C CE1 A TYR   A 18  ? 0.93856 0.85161 0.80846 -0.03096 -0.08861 0.01768  15  TYR   A CE1 
153  C CE1 B TYR   A 18  ? 0.69661 0.88826 0.82029 -0.06076 0.00128  -0.02063 15  TYR   A CE1 
154  C CE2 A TYR   A 18  ? 0.89573 0.86798 0.82568 -0.04175 -0.05941 0.01796  15  TYR   A CE2 
155  C CE2 B TYR   A 18  ? 0.62554 0.81111 0.75365 -0.07048 0.02121  -0.00762 15  TYR   A CE2 
156  C CZ  A TYR   A 18  ? 0.88182 0.80936 0.76850 -0.04318 -0.07221 0.02263  15  TYR   A CZ  
157  C CZ  B TYR   A 18  ? 0.68099 0.86807 0.80622 -0.06905 0.01392  -0.01441 15  TYR   A CZ  
158  O OH  A TYR   A 18  ? 0.94889 0.84510 0.80743 -0.05777 -0.06925 0.03217  15  TYR   A OH  
159  O OH  B TYR   A 18  ? 0.73833 0.92211 0.86215 -0.07483 0.01804  -0.01609 15  TYR   A OH  
160  N N   A GLY   A 19  ? 1.17623 1.28093 1.21039 -0.01264 -0.06441 -0.02383 16  GLY   A N   
161  N N   B GLY   A 19  ? 1.12119 1.26432 1.19511 -0.03585 -0.02931 -0.01698 16  GLY   A N   
162  C CA  A GLY   A 19  ? 1.03116 1.17218 1.09555 -0.00642 -0.06731 -0.03622 16  GLY   A CA  
163  C CA  B GLY   A 19  ? 1.01814 1.15214 1.07875 -0.02505 -0.04682 -0.02413 16  GLY   A CA  
164  C C   A GLY   A 19  ? 0.94901 1.10340 1.02316 -0.01707 -0.05788 -0.03678 16  GLY   A C   
165  C C   B GLY   A 19  ? 0.94613 1.09313 1.01436 -0.02731 -0.04771 -0.03051 16  GLY   A C   
166  O O   A GLY   A 19  ? 0.94277 1.09411 1.01696 -0.02989 -0.04242 -0.02860 16  GLY   A O   
167  O O   B GLY   A 19  ? 0.91930 1.05803 0.97933 -0.03745 -0.03852 -0.02572 16  GLY   A O   
168  N N   A VAL   A 20  ? 0.89967 1.06922 0.98251 -0.01082 -0.06847 -0.04775 17  VAL   A N   
169  N N   B VAL   A 20  ? 0.90218 1.07094 0.98670 -0.01778 -0.05906 -0.04266 17  VAL   A N   
170  C CA  A VAL   A 20  ? 0.74244 0.92868 0.83850 -0.02025 -0.06163 -0.05125 17  VAL   A CA  
171  C CA  B VAL   A 20  ? 0.74667 0.93236 0.84250 -0.02054 -0.06102 -0.05072 17  VAL   A CA  
172  C C   A VAL   A 20  ? 0.69232 0.92096 0.82565 -0.02111 -0.05801 -0.06166 17  VAL   A C   
173  C C   B VAL   A 20  ? 0.69120 0.91895 0.82425 -0.02120 -0.05712 -0.06074 17  VAL   A C   
174  O O   A VAL   A 20  ? 0.69908 0.94748 0.84561 -0.00915 -0.06996 -0.07316 17  VAL   A O   
175  O O   B VAL   A 20  ? 0.68086 0.92708 0.82659 -0.00916 -0.06804 -0.07111 17  VAL   A O   
176  C CB  A VAL   A 20  ? 0.74291 0.91494 0.81968 -0.01510 -0.07634 -0.05645 17  VAL   A CB  
177  C CB  B VAL   A 20  ? 0.76612 0.93743 0.84243 -0.00908 -0.08137 -0.05767 17  VAL   A CB  
178  C CG1 A VAL   A 20  ? 0.71895 0.90870 0.81043 -0.02520 -0.06991 -0.06136 17  VAL   A CG1 
179  C CG1 B VAL   A 20  ? 0.76141 0.93578 0.83664 -0.01647 -0.08049 -0.06112 17  VAL   A CG1 
180  C CG2 A VAL   A 20  ? 0.85979 0.98837 0.89525 -0.01687 -0.07839 -0.04554 17  VAL   A CG2 
181  C CG2 B VAL   A 20  ? 0.90350 1.03094 0.93948 -0.00462 -0.08953 -0.04841 17  VAL   A CG2 
182  N N   . VAL   A 21  ? 0.57062 0.81284 0.71971 -0.03534 -0.04182 -0.05830 18  VAL   A N   
183  C CA  . VAL   A 21  ? 0.55066 0.82983 0.73103 -0.04096 -0.03506 -0.06579 18  VAL   A CA  
184  C C   . VAL   A 21  ? 0.69484 0.99204 0.88765 -0.04747 -0.03786 -0.07540 18  VAL   A C   
185  O O   . VAL   A 21  ? 0.50254 0.78343 0.68433 -0.05598 -0.03400 -0.07115 18  VAL   A O   
186  C CB  . VAL   A 21  ? 0.56774 0.84667 0.75420 -0.05330 -0.01714 -0.05575 18  VAL   A CB  
187  C CG1 . VAL   A 21  ? 0.49423 0.80810 0.70774 -0.06140 -0.00980 -0.06264 18  VAL   A CG1 
188  C CG2 . VAL   A 21  ? 0.61939 0.88159 0.79419 -0.04739 -0.01531 -0.04713 18  VAL   A CG2 
189  N N   . TYR   A 22  ? 0.45133 0.78383 0.66784 -0.04358 -0.04460 -0.08963 19  TYR   A N   
190  C CA  . TYR   A 22  ? 0.47552 0.83258 0.70925 -0.05192 -0.04679 -0.10080 19  TYR   A CA  
191  C C   . TYR   A 22  ? 0.52546 0.92032 0.78832 -0.06490 -0.03461 -0.10660 19  TYR   A C   
192  O O   . TYR   A 22  ? 0.57196 0.98274 0.84521 -0.06117 -0.03004 -0.10751 19  TYR   A O   
193  C CB  . TYR   A 22  ? 0.50947 0.88026 0.74714 -0.03664 -0.06753 -0.11581 19  TYR   A CB  
194  C CG  . TYR   A 22  ? 0.68622 1.01792 0.89079 -0.02516 -0.08153 -0.11093 19  TYR   A CG  
195  C CD1 . TYR   A 22  ? 0.67799 0.99431 0.86894 -0.03139 -0.08478 -0.11059 19  TYR   A CD1 
196  C CD2 . TYR   A 22  ? 0.75685 1.06502 0.94100 -0.00899 -0.09180 -0.10689 19  TYR   A CD2 
197  C CE1 . TYR   A 22  ? 0.84317 1.12312 1.00029 -0.02230 -0.09681 -0.10606 19  TYR   A CE1 
198  C CE2 . TYR   A 22  ? 0.81212 1.08136 0.96128 -0.00095 -0.10427 -0.10157 19  TYR   A CE2 
199  C CZ  . TYR   A 22  ? 0.79260 1.04869 0.92806 -0.00785 -0.10624 -0.10108 19  TYR   A CZ  
200  O OH  . TYR   A 22  ? 1.05477 1.27142 1.15196 -0.00124 -0.11779 -0.09563 19  TYR   A OH  
201  N N   . LYS   A 23  ? 0.60312 1.01077 0.87683 -0.08132 -0.02932 -0.11067 20  LYS   A N   
202  C CA  . LYS   A 23  ? 0.44858 0.89417 0.74860 -0.09683 -0.01898 -0.11825 20  LYS   A CA  
203  C C   . LYS   A 23  ? 0.43658 0.92561 0.76207 -0.09146 -0.03098 -0.13893 20  LYS   A C   
204  O O   . LYS   A 23  ? 0.50508 0.99342 0.82966 -0.08999 -0.04246 -0.14624 20  LYS   A O   
205  C CB  . LYS   A 23  ? 0.42263 0.85562 0.71851 -0.11966 -0.00709 -0.11146 20  LYS   A CB  
206  C CG  . LYS   A 23  ? 0.48110 0.95005 0.79990 -0.13999 0.00356  -0.11898 20  LYS   A CG  
207  C CD  . LYS   A 23  ? 0.53988 0.98779 0.84900 -0.16258 0.01278  -0.11168 20  LYS   A CD  
208  C CE  . LYS   A 23  ? 0.53687 1.01690 0.86431 -0.18638 0.02395  -0.11809 20  LYS   A CE  
209  N NZ  . LYS   A 23  ? 0.59355 1.04556 0.90663 -0.20899 0.03165  -0.10990 20  LYS   A NZ  
210  N N   . ALA   A 24  ? 0.40031 0.92845 0.74873 -0.08767 -0.02888 -0.14955 21  ALA   A N   
211  C CA  . ALA   A 24  ? 0.37598 0.95306 0.75348 -0.08069 -0.03997 -0.17198 21  ALA   A CA  
212  C C   . ALA   A 24  ? 0.51774 1.14268 0.92410 -0.10178 -0.02450 -0.18154 21  ALA   A C   
213  O O   . ALA   A 24  ? 0.49806 1.11792 0.89988 -0.11576 -0.00710 -0.17096 21  ALA   A O   
214  C CB  . ALA   A 24  ? 0.65025 1.23483 1.02984 -0.05231 -0.05483 -0.18059 21  ALA   A CB  
215  N N   . ARG   A 25  ? 0.45364 1.12589 0.88897 -0.10471 -0.03126 -0.20222 22  ARG   A N   
216  C CA  . ARG   A 25  ? 0.52490 1.22577 0.97382 -0.12420 -0.01554 -0.20787 22  ARG   A CA  
217  C C   . ARG   A 25  ? 0.58363 1.32494 1.05351 -0.10774 -0.02446 -0.22900 22  ARG   A C   
218  O O   . ARG   A 25  ? 0.51561 1.26746 0.99439 -0.09168 -0.04377 -0.24200 22  ARG   A O   
219  C CB  . ARG   A 25  ? 0.52982 1.22183 0.97533 -0.15058 -0.00937 -0.20449 22  ARG   A CB  
220  C CG  . ARG   A 25  ? 0.61857 1.33391 1.07244 -0.17071 0.00496  -0.20991 22  ARG   A CG  
221  C CD  . ARG   A 25  ? 0.76213 1.46678 1.21208 -0.19523 0.00762  -0.20795 22  ARG   A CD  
222  N NE  . ARG   A 25  ? 0.95382 1.69363 1.42013 -0.20694 0.01193  -0.22195 22  ARG   A NE  
223  C CZ  . ARG   A 25  ? 1.06487 1.83718 1.55188 -0.19541 -0.00182 -0.24093 22  ARG   A CZ  
224  N NH1 . ARG   A 25  ? 1.05101 1.82238 1.54253 -0.17110 -0.02225 -0.24788 22  ARG   A NH1 
225  N NH2 . ARG   A 25  ? 1.07725 1.88325 1.57949 -0.20854 0.00441  -0.25356 22  ARG   A NH2 
226  N N   . ASN   A 26  ? 0.66374 1.42672 1.13984 -0.11135 -0.01103 -0.23306 23  ASN   A N   
227  C CA  . ASN   A 26  ? 0.71958 1.52441 1.21641 -0.09806 -0.01676 -0.25490 23  ASN   A CA  
228  C C   . ASN   A 26  ? 0.73923 1.56829 1.24936 -0.11678 -0.01349 -0.26514 23  ASN   A C   
229  O O   . ASN   A 26  ? 0.75281 1.57720 1.25671 -0.14543 0.00375  -0.25647 23  ASN   A O   
230  C CB  . ASN   A 26  ? 0.74317 1.56440 1.24101 -0.09758 -0.00261 -0.25704 23  ASN   A CB  
231  C CG  . ASN   A 26  ? 0.83500 1.69952 1.35388 -0.07957 -0.00987 -0.28166 23  ASN   A CG  
232  O OD1 . ASN   A 26  ? 0.79873 1.69618 1.33192 -0.09283 -0.00269 -0.29424 23  ASN   A OD1 
233  N ND2 . ASN   A 26  ? 0.79118 1.65521 1.31128 -0.04912 -0.02464 -0.28937 23  ASN   A ND2 
234  N N   . LYS   A 27  ? 0.86694 1.71999 1.39388 -0.10029 -0.03116 -0.28372 24  LYS   A N   
235  C CA  . LYS   A 27  ? 0.90599 1.78344 1.44720 -0.11682 -0.03025 -0.29476 24  LYS   A CA  
236  C C   . LYS   A 27  ? 0.93413 1.85297 1.49068 -0.12959 -0.01463 -0.30752 24  LYS   A C   
237  O O   . LYS   A 27  ? 1.01868 1.95075 1.58047 -0.15532 -0.00445 -0.30952 24  LYS   A O   
238  C CB  . LYS   A 27  ? 1.16351 2.05284 1.71685 -0.09378 -0.05553 -0.31104 24  LYS   A CB  
239  C CG  . LYS   A 27  ? 1.21173 2.11078 1.77354 -0.11141 -0.05869 -0.31693 24  LYS   A CG  
240  C CD  . LYS   A 27  ? 1.25667 2.11288 1.79793 -0.12825 -0.05792 -0.29807 24  LYS   A CD  
241  C CE  . LYS   A 27  ? 1.06307 1.92635 1.61127 -0.14469 -0.06310 -0.30482 24  LYS   A CE  
242  N NZ  . LYS   A 27  ? 0.99413 1.87605 1.55546 -0.12024 -0.08790 -0.32329 24  LYS   A NZ  
243  N N   . LEU   A 28  ? 0.90217 1.84133 1.46482 -0.11282 -0.01272 -0.31681 25  LEU   A N   
244  C CA  . LEU   A 28  ? 0.96908 1.95179 1.54674 -0.12338 0.00116  -0.33199 25  LEU   A CA  
245  C C   . LEU   A 28  ? 0.87754 1.84832 1.43870 -0.15099 0.02575  -0.31629 25  LEU   A C   
246  O O   . LEU   A 28  ? 0.83487 1.83049 1.40154 -0.17498 0.04055  -0.32200 25  LEU   A O   
247  C CB  . LEU   A 28  ? 0.85859 1.87000 1.44985 -0.09238 -0.00881 -0.35185 25  LEU   A CB  
248  C CG  . LEU   A 28  ? 0.92036 1.94799 1.52810 -0.06294 -0.03432 -0.37159 25  LEU   A CG  
249  C CD1 . LEU   A 28  ? 0.84378 1.89449 1.46099 -0.03247 -0.04340 -0.39067 25  LEU   A CD1 
250  C CD2 . LEU   A 28  ? 0.63591 1.69805 1.26402 -0.07696 -0.03509 -0.38680 25  LEU   A CD2 
251  N N   . THR   A 29  ? 0.81937 1.75185 1.35908 -0.14827 0.02985  -0.29675 26  THR   A N   
252  C CA  . THR   A 29  ? 0.73452 1.65233 1.25580 -0.17056 0.05099  -0.28175 26  THR   A CA  
253  C C   . THR   A 29  ? 0.67961 1.55125 1.17767 -0.19386 0.05850  -0.25751 26  THR   A C   
254  O O   . THR   A 29  ? 0.71045 1.56729 1.19098 -0.21582 0.07548  -0.24490 26  THR   A O   
255  C CB  . THR   A 29  ? 0.68310 1.59278 1.19612 -0.15132 0.05170  -0.27820 26  THR   A CB  
256  O OG1 . THR   A 29  ? 0.63785 1.50670 1.13754 -0.13730 0.04112  -0.26271 26  THR   A OG1 
257  C CG2 . THR   A 29  ? 0.84177 1.79229 1.37608 -0.12439 0.04119  -0.30315 26  THR   A CG2 
258  N N   . GLY   A 30  ? 0.69404 1.54164 1.18992 -0.18938 0.04565  -0.25140 27  GLY   A N   
259  C CA  . GLY   A 30  ? 0.70945 1.51171 1.18293 -0.20862 0.05122  -0.22986 27  GLY   A CA  
260  C C   . GLY   A 30  ? 0.57334 1.33795 1.02605 -0.20199 0.05454  -0.21108 27  GLY   A C   
261  O O   . GLY   A 30  ? 0.63754 1.36344 1.06988 -0.21805 0.06059  -0.19308 27  GLY   A O   
262  N N   . GLU   A 31  ? 0.52664 1.30084 0.98361 -0.17852 0.05016  -0.21542 28  GLU   A N   
263  C CA  . GLU   A 31  ? 0.49427 1.23610 0.93301 -0.17182 0.05339  -0.19878 28  GLU   A CA  
264  C C   . GLU   A 31  ? 0.63146 1.34563 1.06551 -0.15833 0.03908  -0.19132 28  GLU   A C   
265  O O   . GLU   A 31  ? 0.52963 1.25758 0.97735 -0.13872 0.02191  -0.20374 28  GLU   A O   
266  C CB  . GLU   A 31  ? 0.58065 1.34366 1.02564 -0.15208 0.05328  -0.20767 28  GLU   A CB  
267  C CG  . GLU   A 31  ? 0.71614 1.44923 1.14419 -0.14345 0.05553  -0.19233 28  GLU   A CG  
268  C CD  . GLU   A 31  ? 0.89986 1.65434 1.33402 -0.12414 0.05466  -0.20283 28  GLU   A CD  
269  O OE1 . GLU   A 31  ? 0.79299 1.58574 1.24392 -0.11825 0.05341  -0.22221 28  GLU   A OE1 
270  O OE2 . GLU   A 31  ? 0.72641 1.46012 1.14880 -0.11479 0.05499  -0.19267 28  GLU   A OE2 
271  N N   . VAL   A 32  ? 0.45502 1.12980 0.86842 -0.16867 0.04548  -0.17167 29  VAL   A N   
272  C CA  . VAL   A 32  ? 0.41162 1.05942 0.81812 -0.15872 0.03453  -0.16371 29  VAL   A CA  
273  C C   . VAL   A 32  ? 0.55470 1.18880 0.95271 -0.14329 0.03473  -0.15528 29  VAL   A C   
274  O O   . VAL   A 32  ? 0.42340 1.05209 0.81180 -0.14953 0.04760  -0.14746 29  VAL   A O   
275  C CB  . VAL   A 32  ? 0.47941 1.09272 0.86932 -0.18089 0.04052  -0.14949 29  VAL   A CB  
276  C CG1 . VAL   A 32  ? 0.46142 1.08749 0.85980 -0.19579 0.03840  -0.15886 29  VAL   A CG1 
277  C CG2 . VAL   A 32  ? 0.61596 1.20347 0.98529 -0.19805 0.05749  -0.13275 29  VAL   A CG2 
278  N N   . VAL   A 33  ? 0.33366 0.94890 0.72533 -0.12079 0.01914  -0.15436 30  VAL   A N   
279  C CA  . VAL   A 33  ? 0.38109 0.96628 0.75406 -0.10267 0.01648  -0.14353 30  VAL   A CA  
280  C C   . VAL   A 33  ? 0.48954 1.02281 0.83579 -0.09388 0.00717  -0.12943 30  VAL   A C   
281  O O   . VAL   A 33  ? 0.43763 0.96051 0.78050 -0.09897 0.00169  -0.12978 30  VAL   A O   
282  C CB  . VAL   A 33  ? 0.39572 1.00871 0.78315 -0.07806 0.00485  -0.15934 30  VAL   A CB  
283  C CG1 . VAL   A 33  ? 0.45623 1.12361 0.87006 -0.08607 0.01607  -0.17452 30  VAL   A CG1 
284  C CG2 . VAL   A 33  ? 0.40607 1.02629 0.80102 -0.06059 -0.01596 -0.17273 30  VAL   A CG2 
285  N N   . ALA   A 34  ? 0.45086 0.95259 0.77769 -0.08153 0.00592  -0.11770 31  ALA   A N   
286  C CA  . ALA   A 34  ? 0.39444 0.85028 0.69557 -0.07212 -0.00229 -0.10560 31  ALA   A CA  
287  C C   . ALA   A 34  ? 0.53896 0.98859 0.83402 -0.04774 -0.01830 -0.11116 31  ALA   A C   
288  O O   . ALA   A 34  ? 0.56173 1.01603 0.85778 -0.03886 -0.01740 -0.11187 31  ALA   A O   
289  C CB  . ALA   A 34  ? 0.47624 0.89770 0.75785 -0.08046 0.00965  -0.08676 31  ALA   A CB  
290  N N   . LEU   A 35  ? 0.38908 0.82545 0.67522 -0.03707 -0.03379 -0.11519 32  LEU   A N   
291  C CA  . LEU   A 35  ? 0.46952 0.89415 0.74513 -0.01379 -0.05230 -0.12082 32  LEU   A CA  
292  C C   . LEU   A 35  ? 0.63770 1.00969 0.87829 -0.01032 -0.05563 -0.10436 32  LEU   A C   
293  O O   . LEU   A 35  ? 0.62515 0.97567 0.85117 -0.01705 -0.05611 -0.09805 32  LEU   A O   
294  C CB  . LEU   A 35  ? 0.49733 0.94282 0.78441 -0.00321 -0.06981 -0.13785 32  LEU   A CB  
295  C CG  . LEU   A 35  ? 0.67196 1.16992 0.99179 0.00671  -0.07606 -0.15988 32  LEU   A CG  
296  C CD1 . LEU   A 35  ? 0.63445 1.15394 0.96716 0.01347  -0.09246 -0.17615 32  LEU   A CD1 
297  C CD2 . LEU   A 35  ? 0.65712 1.14848 0.97074 0.02938  -0.08697 -0.16434 32  LEU   A CD2 
298  N N   . LYS   A 36  ? 0.61713 0.96944 0.84396 -0.00081 -0.05755 -0.09832 33  LYS   A N   
299  C CA  . LYS   A 36  ? 0.65423 0.95886 0.84738 0.00276  -0.06229 -0.08478 33  LYS   A CA  
300  C C   . LYS   A 36  ? 0.72009 1.00832 0.89717 0.02327  -0.08501 -0.09233 33  LYS   A C   
301  O O   . LYS   A 36  ? 0.66781 0.96559 0.85111 0.03790  -0.09383 -0.10106 33  LYS   A O   
302  C CB  . LYS   A 36  ? 0.56691 0.85604 0.75208 -0.00171 -0.05098 -0.07275 33  LYS   A CB  
303  C CG  . LYS   A 36  ? 0.74447 0.98763 0.89600 -0.00018 -0.05510 -0.05988 33  LYS   A CG  
304  C CD  . LYS   A 36  ? 0.71612 0.94745 0.86328 -0.01259 -0.03891 -0.04625 33  LYS   A CD  
305  C CE  . LYS   A 36  ? 0.85663 1.10305 1.01655 -0.00920 -0.03481 -0.04822 33  LYS   A CE  
306  N NZ  . LYS   A 36  ? 0.68104 0.91458 0.83545 -0.02000 -0.02152 -0.03541 33  LYS   A NZ  
307  N N   . LYS   A 37  ? 0.68898 0.95066 0.84328 0.02491  -0.09523 -0.08942 34  LYS   A N   
308  C CA  . LYS   A 37  ? 0.67683 0.91790 0.81091 0.04402  -0.11927 -0.09623 34  LYS   A CA  
309  C C   . LYS   A 37  ? 0.81645 1.00450 0.90951 0.04571  -0.12375 -0.08181 34  LYS   A C   
310  O O   . LYS   A 37  ? 0.87684 1.04008 0.95038 0.03092  -0.11226 -0.06768 34  LYS   A O   
311  C CB  . LYS   A 37  ? 0.74693 0.98960 0.87736 0.04431  -0.12938 -0.10236 34  LYS   A CB  
312  C CG  . LYS   A 37  ? 0.88502 1.10328 0.99105 0.06474  -0.15665 -0.10940 34  LYS   A CG  
313  C CD  . LYS   A 37  ? 0.94329 1.16474 1.04607 0.06367  -0.16600 -0.11552 34  LYS   A CD  
314  C CE  . LYS   A 37  ? 0.92132 1.11515 0.99624 0.08498  -0.19537 -0.12232 34  LYS   A CE  
315  N NZ  . LYS   A 37  ? 1.08532 1.28361 1.15709 0.08459  -0.20590 -0.12937 34  LYS   A NZ  
316  N N   . ILE   A 38  ? 0.72457 0.89572 0.80443 0.06331  -0.14050 -0.08632 35  ILE   A N   
317  C CA  . ILE   A 38  ? 0.80668 0.92460 0.84487 0.06455  -0.14713 -0.07363 35  ILE   A CA  
318  C C   . ILE   A 38  ? 0.88842 0.97597 0.89791 0.08385  -0.17535 -0.08023 35  ILE   A C   
319  O O   . ILE   A 38  ? 0.95845 1.05623 0.97734 0.10494  -0.19281 -0.09434 35  ILE   A O   
320  C CB  . ILE   A 38  ? 0.81383 0.92982 0.85626 0.06685  -0.14205 -0.07122 35  ILE   A CB  
321  C CG1 . ILE   A 38  ? 0.81214 0.95581 0.88027 0.04842  -0.11579 -0.06440 35  ILE   A CG1 
322  C CG2 . ILE   A 38  ? 0.83100 0.88971 0.82843 0.06649  -0.15041 -0.05875 35  ILE   A CG2 
323  C CD1 . ILE   A 38  ? 0.75108 0.89522 0.82414 0.04986  -0.11032 -0.06242 35  ILE   A CD1 
324  N N   . ARG   A 39  ? 0.84282 0.89256 0.81599 0.07747  -0.18051 -0.07082 36  ARG   A N   
325  C CA  . ARG   A 39  ? 1.02349 1.03565 0.96089 0.09435  -0.20844 -0.07469 36  ARG   A CA  
326  C C   . ARG   A 39  ? 1.00245 0.96031 0.89815 0.09815  -0.21846 -0.06474 36  ARG   A C   
327  O O   . ARG   A 39  ? 1.13836 1.05985 1.00193 0.08001  -0.20752 -0.04784 36  ARG   A O   
328  C CB  . ARG   A 39  ? 1.09791 1.09100 1.01035 0.08430  -0.20908 -0.06859 36  ARG   A CB  
329  C CG  . ARG   A 39  ? 1.12139 1.16431 1.07257 0.08020  -0.20127 -0.07915 36  ARG   A CG  
330  C CD  . ARG   A 39  ? 1.33705 1.36087 1.26360 0.06669  -0.19699 -0.07163 36  ARG   A CD  
331  N NE  . ARG   A 39  ? 1.43554 1.41873 1.31957 0.07924  -0.22281 -0.07291 36  ARG   A NE  
332  C CZ  . ARG   A 39  ? 1.52559 1.45174 1.35552 0.07348  -0.22734 -0.05877 36  ARG   A CZ  
333  N NH1 . ARG   A 39  ? 1.51214 1.41835 1.32644 0.05511  -0.20740 -0.04325 36  ARG   A NH1 
334  N NH2 . ARG   A 39  ? 1.44260 1.33103 1.23220 0.08568  -0.25276 -0.06061 36  ARG   A NH2 
335  N N   . LEU   A 40  ? 1.07721 1.03014 0.97346 0.12140  -0.23937 -0.07623 37  LEU   A N   
336  C CA  . LEU   A 40  ? 1.17825 1.07991 1.03724 0.12580  -0.24980 -0.06837 37  LEU   A CA  
337  C C   . LEU   A 40  ? 1.16562 0.99836 0.96208 0.12764  -0.27048 -0.05869 37  LEU   A C   
338  O O   . LEU   A 40  ? 1.15298 0.93415 0.90943 0.12197  -0.27444 -0.04688 37  LEU   A O   
339  C CB  . LEU   A 40  ? 1.08292 1.00150 0.96278 0.15206  -0.26640 -0.08576 37  LEU   A CB  
340  C CG  . LEU   A 40  ? 0.88752 0.87218 0.82500 0.15098  -0.24713 -0.09637 37  LEU   A CG  
341  C CD1 . LEU   A 40  ? 0.98004 0.98100 0.93469 0.17923  -0.26569 -0.11616 37  LEU   A CD1 
342  C CD2 . LEU   A 40  ? 0.79814 0.78029 0.73753 0.12723  -0.22071 -0.08062 37  LEU   A CD2 
343  N N   . ASP   A 41  ? 1.15377 0.98266 0.93861 0.13428  -0.28409 -0.06331 38  ASP   A N   
344  C CA  . ASP   A 41  ? 1.24652 1.00688 0.96697 0.13542  -0.30447 -0.05359 38  ASP   A CA  
345  C C   . ASP   A 41  ? 1.17533 0.90027 0.85896 0.10404  -0.28339 -0.03155 38  ASP   A C   
346  O O   . ASP   A 41  ? 1.24204 0.90182 0.86599 0.09895  -0.29549 -0.01952 38  ASP   A O   
347  C CB  . ASP   A 41  ? 1.39605 1.16470 1.11461 0.14922  -0.32319 -0.06440 38  ASP   A CB  
348  C CG  . ASP   A 41  ? 1.38733 1.22070 1.15628 0.13847  -0.30204 -0.07095 38  ASP   A CG  
349  O OD1 . ASP   A 41  ? 1.34845 1.23475 1.16862 0.13422  -0.28270 -0.07681 38  ASP   A OD1 
350  O OD2 . ASP   A 41  ? 1.49559 1.32431 1.25034 0.13377  -0.30531 -0.07017 38  ASP   A OD2 
351  N N   . THR   A 42  ? 1.10990 0.87616 0.82692 0.08269  -0.25235 -0.02664 39  THR   A N   
352  C CA  . THR   A 42  ? 1.21639 0.95966 0.90665 0.05353  -0.23007 -0.00866 39  THR   A CA  
353  C C   . THR   A 42  ? 1.30981 1.04514 1.00146 0.04049  -0.21524 0.00055  39  THR   A C   
354  O O   . THR   A 42  ? 1.19862 0.91251 0.86578 0.01630  -0.19835 0.01477  39  THR   A O   
355  C CB  . THR   A 42  ? 1.38065 1.17057 1.10457 0.03875  -0.20589 -0.00932 39  THR   A CB  
356  O OG1 . THR   A 42  ? 1.41531 1.23275 1.15989 0.05481  -0.21916 -0.02348 39  THR   A OG1 
357  C CG2 . THR   A 42  ? 1.32653 1.08519 1.00990 0.01489  -0.19237 0.00515  39  THR   A CG2 
358  N N   . GLU   A 43  ? 1.17690 0.93060 0.89662 0.05560  -0.22109 -0.00825 40  GLU   A N   
359  C CA  . GLU   A 43  ? 1.05648 0.80580 0.78076 0.04492  -0.20846 -0.00134 40  GLU   A CA  
360  C C   . GLU   A 43  ? 1.22420 0.90996 0.89909 0.05312  -0.23184 0.00263  40  GLU   A C   
361  O O   . GLU   A 43  ? 1.26665 0.94752 0.94517 0.07885  -0.25455 -0.00956 40  GLU   A O   
362  C CB  . GLU   A 43  ? 1.07833 0.88589 0.86128 0.05493  -0.19924 -0.01335 40  GLU   A CB  
363  C CG  . GLU   A 43  ? 1.01058 0.87677 0.83971 0.04778  -0.17897 -0.01790 40  GLU   A CG  
364  C CD  . GLU   A 43  ? 1.19615 1.06609 1.02418 0.02058  -0.15256 -0.00432 40  GLU   A CD  
365  O OE1 . GLU   A 43  ? 1.18260 1.02932 0.99306 0.00689  -0.14431 0.00621  40  GLU   A OE1 
366  O OE2 . GLU   A 43  ? 1.19828 1.09509 1.04354 0.01321  -0.14065 -0.00530 40  GLU   A OE2 
367  N N   . THR   A 44  ? 1.20597 0.84276 0.83392 0.03066  -0.22626 0.01899  41  THR   A N   
368  C CA  . THR   A 44  ? 1.38227 0.95015 0.95579 0.03434  -0.24834 0.02485  41  THR   A CA  
369  C C   . THR   A 44  ? 1.34327 0.91416 0.93389 0.03977  -0.24882 0.02136  41  THR   A C   
370  O O   . THR   A 44  ? 1.23882 0.76195 0.79688 0.05430  -0.27333 0.01922  41  THR   A O   
371  C CB  . THR   A 44  ? 1.45775 0.97412 0.97524 0.00435  -0.23975 0.04356  41  THR   A CB  
372  O OG1 . THR   A 44  ? 1.52109 1.07078 1.06424 -0.02254 -0.20742 0.05109  41  THR   A OG1 
373  C CG2 . THR   A 44  ? 1.49524 0.99774 0.98489 0.00201  -0.24450 0.04628  41  THR   A CG2 
374  N N   . GLU   A 45  ? 1.12236 0.74584 0.76117 0.02907  -0.22347 0.02042  42  GLU   A N   
375  C CA  . GLU   A 45  ? 1.10424 0.73571 0.76202 0.03341  -0.22209 0.01652  42  GLU   A CA  
376  C C   . GLU   A 45  ? 1.08213 0.76485 0.79024 0.06062  -0.22789 -0.00224 42  GLU   A C   
377  O O   . GLU   A 45  ? 1.16315 0.87391 0.90178 0.06137  -0.21813 -0.00656 42  GLU   A O   
378  C CB  . GLU   A 45  ? 1.06569 0.72140 0.74285 0.00539  -0.19236 0.02651  42  GLU   A CB  
379  C CG  . GLU   A 45  ? 1.42010 1.03157 1.05104 -0.02415 -0.18386 0.04343  42  GLU   A CG  
380  C CD  . GLU   A 45  ? 1.51971 1.05881 1.09402 -0.02553 -0.20484 0.04966  42  GLU   A CD  
381  O OE1 . GLU   A 45  ? 1.39195 0.92315 0.97240 -0.01183 -0.21645 0.04312  42  GLU   A OE1 
382  O OE2 . GLU   A 45  ? 1.53110 1.01902 1.05222 -0.04073 -0.21003 0.06095  42  GLU   A OE2 
383  N N   . GLY   A 46  ? 1.03963 0.73656 0.75667 0.08210  -0.24336 -0.01413 43  GLY   A N   
384  C CA  . GLY   A 46  ? 1.07316 0.82380 0.83933 0.10600  -0.24752 -0.03347 43  GLY   A CA  
385  C C   . GLY   A 46  ? 0.95520 0.77398 0.77550 0.09347  -0.21873 -0.03512 43  GLY   A C   
386  O O   . GLY   A 46  ? 1.04673 0.87672 0.87009 0.07336  -0.20068 -0.02526 43  GLY   A O   
387  N N   . VAL   A 47  ? 0.86034 0.72345 0.72174 0.10578  -0.21487 -0.04825 44  VAL   A N   
388  C CA  . VAL   A 47  ? 0.79065 0.71487 0.70037 0.09401  -0.18883 -0.04978 44  VAL   A CA  
389  C C   . VAL   A 47  ? 0.81578 0.73136 0.71969 0.06708  -0.16640 -0.03281 44  VAL   A C   
390  O O   . VAL   A 47  ? 0.83361 0.72048 0.71905 0.06294  -0.16805 -0.02723 44  VAL   A O   
391  C CB  . VAL   A 47  ? 0.71807 0.68704 0.66683 0.11086  -0.18903 -0.06674 44  VAL   A CB  
392  C CG1 . VAL   A 47  ? 0.73665 0.76545 0.73079 0.09834  -0.16401 -0.06834 44  VAL   A CG1 
393  C CG2 . VAL   A 47  ? 0.74838 0.72411 0.70122 0.13981  -0.21395 -0.08582 44  VAL   A CG2 
394  N N   . PRO   A 48  ? 0.75195 0.69073 0.67063 0.04882  -0.14632 -0.02523 45  PRO   A N   
395  C CA  . PRO   A 48  ? 0.68380 0.61649 0.59813 0.02484  -0.12625 -0.01088 45  PRO   A CA  
396  C C   . PRO   A 48  ? 0.72617 0.68132 0.66489 0.02356  -0.11629 -0.01270 45  PRO   A C   
397  O O   . PRO   A 48  ? 0.73627 0.72827 0.70636 0.03602  -0.11582 -0.02427 45  PRO   A O   
398  C CB  . PRO   A 48  ? 0.75829 0.72140 0.69246 0.01237  -0.10898 -0.00783 45  PRO   A CB  
399  C CG  . PRO   A 48  ? 0.86327 0.82647 0.79266 0.02570  -0.12372 -0.01602 45  PRO   A CG  
400  C CD  . PRO   A 48  ? 0.84110 0.80953 0.77838 0.04972  -0.14291 -0.03018 45  PRO   A CD  
401  N N   . SER   A 49  ? 0.75571 0.68885 0.67866 0.00727  -0.10817 -0.00159 46  SER   A N   
402  C CA  . SER   A 49  ? 0.69980 0.65004 0.64189 0.00491  -0.09977 -0.00247 46  SER   A CA  
403  C C   . SER   A 49  ? 0.75386 0.75659 0.73787 0.00099  -0.08124 -0.00512 46  SER   A C   
404  O O   . SER   A 49  ? 0.66536 0.69386 0.67205 0.00844  -0.07871 -0.01224 46  SER   A O   
405  C CB  . SER   A 49  ? 0.80831 0.72849 0.72744 -0.01467 -0.09363 0.00983  46  SER   A CB  
406  O OG  . SER   A 49  ? 0.99954 0.92880 0.92130 -0.03403 -0.07673 0.01906  46  SER   A OG  
407  N N   . THR   A 50  ? 0.63542 0.65216 0.62746 -0.01086 -0.06851 0.00036  47  THR   A N   
408  C CA  . THR   A 50  ? 0.64683 0.70722 0.67424 -0.01466 -0.05275 -0.00174 47  THR   A CA  
409  C C   . THR   A 50  ? 0.60441 0.69506 0.65438 0.00053  -0.05810 -0.01466 47  THR   A C   
410  O O   . THR   A 50  ? 0.56101 0.68580 0.63827 -0.00032 -0.04781 -0.01845 47  THR   A O   
411  C CB  . THR   A 50  ? 0.74494 0.80947 0.77302 -0.02854 -0.04050 0.00533  47  THR   A CB  
412  O OG1 . THR   A 50  ? 0.65632 0.70698 0.66843 -0.02355 -0.05030 0.00300  47  THR   A OG1 
413  C CG2 . THR   A 50  ? 0.69519 0.73931 0.70668 -0.04492 -0.03232 0.01607  47  THR   A CG2 
414  N N   . ALA   A 51  ? 0.51233 0.59153 0.55066 0.01390  -0.07434 -0.02202 48  ALA   A N   
415  C CA  . ALA   A 51  ? 0.54605 0.65861 0.60840 0.02873  -0.08024 -0.03682 48  ALA   A CA  
416  C C   . ALA   A 51  ? 0.57683 0.69953 0.64800 0.04231  -0.08653 -0.04679 48  ALA   A C   
417  O O   . ALA   A 51  ? 0.55599 0.71931 0.65618 0.04589  -0.07958 -0.05635 48  ALA   A O   
418  C CB  . ALA   A 51  ? 0.55133 0.65011 0.59952 0.04049  -0.09756 -0.04313 48  ALA   A CB  
419  N N   . ILE   A 52  ? 0.61144 0.69659 0.65606 0.04898  -0.09937 -0.04504 49  ILE   A N   
420  C CA  . ILE   A 52  ? 0.67375 0.76499 0.72405 0.06269  -0.10607 -0.05520 49  ILE   A CA  
421  C C   . ILE   A 52  ? 0.53582 0.65191 0.60554 0.05091  -0.08756 -0.05126 49  ILE   A C   
422  O O   . ILE   A 52  ? 0.59907 0.74570 0.68901 0.05937  -0.08502 -0.06233 49  ILE   A O   
423  C CB  . ILE   A 52  ? 0.62204 0.66019 0.63501 0.07031  -0.12446 -0.05277 49  ILE   A CB  
424  C CG1 . ILE   A 52  ? 0.73778 0.74441 0.72511 0.08069  -0.14384 -0.05448 49  ILE   A CG1 
425  C CG2 . ILE   A 52  ? 0.69960 0.74325 0.71780 0.08819  -0.13411 -0.06623 49  ILE   A CG2 
426  C CD1 . ILE   A 52  ? 0.70710 0.65478 0.65208 0.08835  -0.16437 -0.05192 49  ILE   A CD1 
427  N N   . ARG   A 53  ? 0.67169 0.77604 0.73502 0.03156  -0.07469 -0.03630 50  ARG   A N   
428  C CA  . ARG   A 53  ? 0.62294 0.74819 0.70270 0.02094  -0.05895 -0.03202 50  ARG   A CA  
429  C C   . ARG   A 53  ? 0.50914 0.67938 0.61916 0.01851  -0.04604 -0.03700 50  ARG   A C   
430  O O   . ARG   A 53  ? 0.51276 0.70792 0.63802 0.02048  -0.03985 -0.04265 50  ARG   A O   
431  C CB  . ARG   A 53  ? 0.70132 0.80741 0.77002 0.00213  -0.04927 -0.01678 50  ARG   A CB  
432  C CG  . ARG   A 53  ? 0.86585 0.93253 0.90743 -0.00125 -0.05755 -0.01114 50  ARG   A CG  
433  C CD  . ARG   A 53  ? 0.87208 0.93117 0.90973 -0.02132 -0.04533 0.00165  50  ARG   A CD  
434  N NE  . ARG   A 53  ? 0.78820 0.81133 0.80023 -0.02857 -0.05185 0.00712  50  ARG   A NE  
435  C CZ  . ARG   A 53  ? 1.02233 1.03767 1.02898 -0.04659 -0.04289 0.01648  50  ARG   A CZ  
436  N NH1 . ARG   A 53  ? 0.74678 0.78672 0.77176 -0.05679 -0.02796 0.02093  50  ARG   A NH1 
437  N NH2 . ARG   A 53  ? 0.81849 0.80087 0.80084 -0.05466 -0.04945 0.02049  50  ARG   A NH2 
438  N N   . GLU   A 54  ? 0.43978 0.61911 0.55637 0.01293  -0.04179 -0.03494 51  GLU   A N   
439  C CA  . GLU   A 54  ? 0.50521 0.72237 0.64733 0.00687  -0.02907 -0.03808 51  GLU   A CA  
440  C C   . GLU   A 54  ? 0.43115 0.68100 0.59137 0.01937  -0.03298 -0.05443 51  GLU   A C   
441  O O   . GLU   A 54  ? 0.47986 0.76051 0.65815 0.01401  -0.02143 -0.05788 51  GLU   A O   
442  C CB  . GLU   A 54  ? 0.51070 0.72733 0.65381 -0.00095 -0.02583 -0.03381 51  GLU   A CB  
443  C CG  . GLU   A 54  ? 0.61526 0.86549 0.78146 -0.00947 -0.01339 -0.03627 51  GLU   A CG  
444  C CD  . GLU   A 54  ? 0.66933 0.91493 0.83443 -0.01823 -0.00987 -0.03138 51  GLU   A CD  
445  O OE1 . GLU   A 54  ? 0.77093 0.99377 0.91957 -0.01460 -0.01902 -0.02976 51  GLU   A OE1 
446  O OE2 . GLU   A 54  ? 0.67059 0.93279 0.84867 -0.02906 0.00163  -0.02913 51  GLU   A OE2 
447  N N   . ILE   A 55  ? 0.49369 0.73761 0.64843 0.03603  -0.04946 -0.06533 52  ILE   A N   
448  C CA  . ILE   A 55  ? 0.46663 0.74672 0.64171 0.04983  -0.05402 -0.08394 52  ILE   A CA  
449  C C   . ILE   A 55  ? 0.53239 0.82398 0.71165 0.05488  -0.05065 -0.08979 52  ILE   A C   
450  O O   . ILE   A 55  ? 0.46422 0.79569 0.66487 0.05244  -0.04001 -0.09859 52  ILE   A O   
451  C CB  . ILE   A 55  ? 0.54054 0.80826 0.70703 0.06970  -0.07564 -0.09525 52  ILE   A CB  
452  C CG1 . ILE   A 55  ? 0.41275 0.67739 0.57830 0.06457  -0.07817 -0.09202 52  ILE   A CG1 
453  C CG2 . ILE   A 55  ? 0.60776 0.91453 0.79646 0.08732  -0.08196 -0.11730 52  ILE   A CG2 
454  C CD1 . ILE   A 55  ? 0.50619 0.75163 0.65762 0.08381  -0.10148 -0.10111 52  ILE   A CD1 
455  N N   . SER   A 56  ? 0.49312 0.74915 0.65015 0.06051  -0.05929 -0.08509 53  SER   A N   
456  C CA  . SER   A 56  ? 0.54217 0.80559 0.70033 0.06685  -0.05815 -0.09172 53  SER   A CA  
457  C C   . SER   A 56  ? 0.49979 0.78176 0.66758 0.04929  -0.03841 -0.08315 53  SER   A C   
458  O O   . SER   A 56  ? 0.60928 0.91872 0.78817 0.05177  -0.03187 -0.09222 53  SER   A O   
459  C CB  . SER   A 56  ? 0.60899 0.82509 0.73848 0.07407  -0.07232 -0.08723 53  SER   A CB  
460  O OG  . SER   A 56  ? 0.77229 0.95781 0.88561 0.05666  -0.06659 -0.06838 53  SER   A OG  
461  N N   . LEU   A 57  ? 0.48377 0.75076 0.64611 0.03207  -0.02926 -0.06643 54  LEU   A N   
462  C CA  . LEU   A 57  ? 0.47332 0.75325 0.64208 0.01694  -0.01313 -0.05794 54  LEU   A CA  
463  C C   . LEU   A 57  ? 0.46382 0.78366 0.65346 0.01004  -0.00083 -0.06366 54  LEU   A C   
464  O O   . LEU   A 57  ? 0.47553 0.81554 0.67082 0.00471  0.00926  -0.06560 54  LEU   A O   
465  C CB  . LEU   A 57  ? 0.44839 0.70299 0.60718 0.00276  -0.00826 -0.04074 54  LEU   A CB  
466  C CG  . LEU   A 57  ? 0.52442 0.74296 0.66307 0.00288  -0.01591 -0.03323 54  LEU   A CG  
467  C CD1 . LEU   A 57  ? 0.57193 0.77446 0.70559 -0.01154 -0.00948 -0.01899 54  LEU   A CD1 
468  C CD2 . LEU   A 57  ? 0.51320 0.73290 0.64883 0.00480  -0.01513 -0.03522 54  LEU   A CD2 
469  N N   . LEU   A 58  ? 0.48907 0.81968 0.68834 0.00873  -0.00161 -0.06650 55  LEU   A N   
470  C CA  . LEU   A 58  ? 0.44787 0.81386 0.66570 -0.00181 0.01063  -0.07077 55  LEU   A CA  
471  C C   . LEU   A 58  ? 0.50202 0.90748 0.73608 0.00676  0.01142  -0.08952 55  LEU   A C   
472  O O   . LEU   A 58  ? 0.58218 1.01794 0.82790 -0.00516 0.02503  -0.09258 55  LEU   A O   
473  C CB  . LEU   A 58  ? 0.32745 0.69310 0.55070 -0.00628 0.00877  -0.06921 55  LEU   A CB  
474  C CG  . LEU   A 58  ? 0.43531 0.77201 0.64675 -0.01876 0.01329  -0.05200 55  LEU   A CG  
475  C CD1 . LEU   A 58  ? 0.51569 0.85543 0.73278 -0.02330 0.01221  -0.05257 55  LEU   A CD1 
476  C CD2 . LEU   A 58  ? 0.53350 0.87222 0.74432 -0.03336 0.02728  -0.04220 55  LEU   A CD2 
477  N N   . LYS   A 59  ? 0.48065 0.88614 0.71455 0.02699  -0.00303 -0.10288 56  LYS   A N   
478  C CA  . LYS   A 59  ? 0.51315 0.95952 0.76421 0.03763  -0.00266 -0.12345 56  LYS   A CA  
479  C C   . LYS   A 59  ? 0.62984 1.08440 0.87626 0.03474  0.00689  -0.12428 56  LYS   A C   
480  O O   . LYS   A 59  ? 0.61921 1.11143 0.87944 0.04117  0.01062  -0.14164 56  LYS   A O   
481  C CB  . LYS   A 59  ? 0.69684 1.13752 0.94734 0.06324  -0.02340 -0.13872 56  LYS   A CB  
482  C CG  . LYS   A 59  ? 0.61445 1.05433 0.87101 0.06821  -0.03416 -0.14198 56  LYS   A CG  
483  C CD  . LYS   A 59  ? 0.77648 1.21549 1.03359 0.09567  -0.05606 -0.16015 56  LYS   A CD  
484  C CE  . LYS   A 59  ? 0.96850 1.46742 1.25744 0.10503  -0.05441 -0.18515 56  LYS   A CE  
485  N NZ  . LYS   A 59  ? 0.70553 1.23640 1.01579 0.09208  -0.04729 -0.18753 56  LYS   A NZ  
486  N N   . GLU   A 60  ? 0.56339 0.98570 0.79108 0.02547  0.01074  -0.10718 57  GLU   A N   
487  C CA  . GLU   A 60  ? 0.66712 1.09413 0.88758 0.02063  0.01979  -0.10586 57  GLU   A CA  
488  C C   . GLU   A 60  ? 0.55611 0.97618 0.77011 -0.00150 0.03428  -0.08844 57  GLU   A C   
489  O O   . GLU   A 60  ? 0.65833 1.07637 0.86222 -0.00707 0.04101  -0.08439 57  GLU   A O   
490  C CB  . GLU   A 60  ? 0.73656 1.12955 0.93841 0.03356  0.00726  -0.10427 57  GLU   A CB  
491  C CG  . GLU   A 60  ? 0.80034 1.19528 1.00403 0.05747  -0.00888 -0.12259 57  GLU   A CG  
492  C CD  . GLU   A 60  ? 0.93087 1.28666 1.11257 0.06815  -0.02184 -0.12029 57  GLU   A CD  
493  O OE1 . GLU   A 60  ? 0.99206 1.31919 1.15900 0.05614  -0.01899 -0.10365 57  GLU   A OE1 
494  O OE2 . GLU   A 60  ? 0.97291 1.32651 1.15217 0.08869  -0.03561 -0.13599 57  GLU   A OE2 
495  N N   . LEU   A 61  ? 0.47477 0.88915 0.69262 -0.01312 0.03789  -0.07866 58  LEU   A N   
496  C CA  . LEU   A 61  ? 0.45309 0.85811 0.66427 -0.03242 0.04955  -0.06306 58  LEU   A CA  
497  C C   . LEU   A 61  ? 0.60237 1.03725 0.82699 -0.04609 0.06068  -0.06725 58  LEU   A C   
498  O O   . LEU   A 61  ? 0.62712 1.05416 0.85480 -0.05443 0.06161  -0.06044 58  LEU   A O   
499  C CB  . LEU   A 61  ? 0.52904 0.89761 0.73089 -0.03491 0.04398  -0.04782 58  LEU   A CB  
500  C CG  . LEU   A 61  ? 0.49793 0.83574 0.68486 -0.02855 0.03620  -0.04037 58  LEU   A CG  
501  C CD1 . LEU   A 61  ? 0.40775 0.71777 0.58887 -0.03365 0.03351  -0.02726 58  LEU   A CD1 
502  C CD2 . LEU   A 61  ? 0.46062 0.79852 0.63841 -0.03394 0.04252  -0.03628 58  LEU   A CD2 
503  N N   . ASN   A 62  ? 0.50232 0.97209 0.73437 -0.04936 0.06951  -0.07928 59  ASN   A N   
504  C CA  . ASN   A 62  ? 0.52217 1.02376 0.76633 -0.06581 0.08184  -0.08440 59  ASN   A CA  
505  C C   . ASN   A 62  ? 0.43796 0.92721 0.66469 -0.08693 0.09484  -0.07000 59  ASN   A C   
506  O O   . ASN   A 62  ? 0.53144 1.02538 0.74674 -0.08978 0.10123  -0.07042 59  ASN   A O   
507  C CB  . ASN   A 62  ? 0.54548 1.09542 0.80766 -0.05955 0.08549  -0.10676 59  ASN   A CB  
508  C CG  . ASN   A 62  ? 0.71474 1.30120 0.99885 -0.06954 0.09110  -0.11750 59  ASN   A CG  
509  O OD1 . ASN   A 62  ? 0.98478 1.60058 1.28985 -0.05532 0.08357  -0.13576 59  ASN   A OD1 
510  N ND2 . ASN   A 62  ? 0.81451 1.39808 1.09326 -0.09382 0.10306  -0.10676 59  ASN   A ND2 
511  N N   . HIS   A 63  ? 0.47153 0.94247 0.69383 -0.10098 0.09764  -0.05758 60  HIS   A N   
512  C CA  . HIS   A 63  ? 0.48641 0.93639 0.68841 -0.11934 0.10652  -0.04247 60  HIS   A CA  
513  C C   . HIS   A 63  ? 0.44204 0.88960 0.64674 -0.13647 0.11150  -0.03770 60  HIS   A C   
514  O O   . HIS   A 63  ? 0.43468 0.88030 0.65219 -0.13078 0.10450  -0.03997 60  HIS   A O   
515  C CB  . HIS   A 63  ? 0.41689 0.82505 0.60161 -0.11215 0.09854  -0.02730 60  HIS   A CB  
516  C CG  . HIS   A 63  ? 0.42147 0.80724 0.58314 -0.12659 0.10472  -0.01343 60  HIS   A CG  
517  N ND1 . HIS   A 63  ? 0.47256 0.83288 0.62480 -0.13795 0.10538  -0.00108 60  HIS   A ND1 
518  C CD2 . HIS   A 63  ? 0.47242 0.85495 0.61614 -0.13061 0.10915  -0.01033 60  HIS   A CD2 
519  C CE1 . HIS   A 63  ? 0.56141 0.90208 0.69033 -0.14768 0.10891  0.00933  60  HIS   A CE1 
520  N NE2 . HIS   A 63  ? 0.46868 0.82251 0.59150 -0.14401 0.11146  0.00436  60  HIS   A NE2 
521  N N   . PRO   A 64  ? 0.49614 0.94107 0.68627 -0.15813 0.12291  -0.03106 61  PRO   A N   
522  C CA  . PRO   A 64  ? 0.42735 0.86618 0.61736 -0.17620 0.12713  -0.02659 61  PRO   A CA  
523  C C   . PRO   A 64  ? 0.59713 0.99598 0.78069 -0.17125 0.11758  -0.01403 61  PRO   A C   
524  O O   . PRO   A 64  ? 0.44670 0.84357 0.63657 -0.17957 0.11737  -0.01438 61  PRO   A O   
525  C CB  . PRO   A 64  ? 0.60378 1.03654 0.77029 -0.19993 0.13978  -0.01909 61  PRO   A CB  
526  C CG  . PRO   A 64  ? 0.54044 0.99905 0.70555 -0.19561 0.14565  -0.02765 61  PRO   A CG  
527  C CD  . PRO   A 64  ? 0.46185 0.91226 0.63409 -0.16848 0.13290  -0.02949 61  PRO   A CD  
528  N N   . ASN   A 65  ? 0.50244 0.87143 0.67440 -0.15842 0.10986  -0.00418 62  ASN   A N   
529  C CA  . ASN   A 65  ? 0.48400 0.81922 0.65131 -0.15297 0.10168  0.00590  62  ASN   A CA  
530  C C   . ASN   A 65  ? 0.44466 0.78073 0.62624 -0.13332 0.09162  0.00129  62  ASN   A C   
531  O O   . ASN   A 65  ? 0.42918 0.73915 0.60560 -0.12585 0.08514  0.00922  62  ASN   A O   
532  C CB  . ASN   A 65  ? 0.41717 0.71811 0.56140 -0.15407 0.09980  0.01992  62  ASN   A CB  
533  C CG  . ASN   A 65  ? 0.66945 0.95951 0.79246 -0.17463 0.10797  0.02675  62  ASN   A CG  
534  O OD1 . ASN   A 65  ? 0.52302 0.81240 0.63029 -0.17913 0.11198  0.02966  62  ASN   A OD1 
535  N ND2 . ASN   A 65  ? 0.49544 0.77439 0.61508 -0.18812 0.11009  0.02944  62  ASN   A ND2 
536  N N   . ILE   A 66  ? 0.46106 0.82628 0.65926 -0.12499 0.08988  -0.01194 63  ILE   A N   
537  C CA  . ILE   A 66  ? 0.46387 0.82713 0.67172 -0.10780 0.07934  -0.01670 63  ILE   A CA  
538  C C   . ILE   A 66  ? 0.38056 0.76948 0.60596 -0.10754 0.07773  -0.02926 63  ILE   A C   
539  O O   . ILE   A 66  ? 0.41739 0.83956 0.65405 -0.11160 0.08284  -0.04083 63  ILE   A O   
540  C CB  . ILE   A 66  ? 0.45298 0.82026 0.65994 -0.09305 0.07421  -0.02117 63  ILE   A CB  
541  C CG1 . ILE   A 66  ? 0.39281 0.73639 0.58326 -0.09376 0.07488  -0.00954 63  ILE   A CG1 
542  C CG2 . ILE   A 66  ? 0.41960 0.77970 0.63179 -0.07718 0.06246  -0.02549 63  ILE   A CG2 
543  C CD1 . ILE   A 66  ? 0.52519 0.86986 0.71281 -0.08088 0.06953  -0.01366 63  ILE   A CD1 
544  N N   . VAL   A 67  ? 0.33252 0.70798 0.56042 -0.10296 0.07067  -0.02799 64  VAL   A N   
545  C CA  . VAL   A 67  ? 0.37199 0.76946 0.61541 -0.10179 0.06690  -0.03989 64  VAL   A CA  
546  C C   . VAL   A 67  ? 0.40781 0.83029 0.66303 -0.08606 0.05998  -0.05417 64  VAL   A C   
547  O O   . VAL   A 67  ? 0.45364 0.86062 0.70204 -0.07075 0.05120  -0.05310 64  VAL   A O   
548  C CB  . VAL   A 67  ? 0.45339 0.82738 0.69271 -0.09806 0.05944  -0.03533 64  VAL   A CB  
549  C CG1 . VAL   A 67  ? 0.44192 0.83788 0.69600 -0.09643 0.05388  -0.04802 64  VAL   A CG1 
550  C CG2 . VAL   A 67  ? 0.39281 0.74187 0.62065 -0.11128 0.06546  -0.02304 64  VAL   A CG2 
551  N N   . LYS   A 68  ? 0.37110 0.83254 0.64388 -0.08999 0.06352  -0.06852 65  LYS   A N   
552  C CA  . LYS   A 68  ? 0.47563 0.96602 0.76148 -0.07424 0.05762  -0.08481 65  LYS   A CA  
553  C C   . LYS   A 68  ? 0.43116 0.92009 0.72367 -0.05632 0.04131  -0.09373 65  LYS   A C   
554  O O   . LYS   A 68  ? 0.45847 0.94913 0.75699 -0.06058 0.03788  -0.09548 65  LYS   A O   
555  C CB  . LYS   A 68  ? 0.50494 1.04341 0.80948 -0.08538 0.06831  -0.09917 65  LYS   A CB  
556  C CG  . LYS   A 68  ? 0.57601 1.11910 0.87076 -0.10010 0.08335  -0.09342 65  LYS   A CG  
557  C CD  . LYS   A 68  ? 0.63883 1.23483 0.95257 -0.10943 0.09398  -0.11085 65  LYS   A CD  
558  C CE  . LYS   A 68  ? 0.73190 1.36111 1.06549 -0.08602 0.08408  -0.13209 65  LYS   A CE  
559  N NZ  . LYS   A 68  ? 0.99158 1.65702 1.33488 -0.09120 0.09135  -0.14813 65  LYS   A NZ  
560  N N   . LEU   A 69  ? 0.43524 0.91808 0.72399 -0.03618 0.03019  -0.09943 66  LEU   A N   
561  C CA  . LEU   A 69  ? 0.50137 0.98535 0.79486 -0.01661 0.01267  -0.11104 66  LEU   A CA  
562  C C   . LEU   A 69  ? 0.50926 1.04464 0.82867 -0.00923 0.01148  -0.13390 66  LEU   A C   
563  O O   . LEU   A 69  ? 0.55250 1.10640 0.87661 -0.00181 0.01394  -0.14287 66  LEU   A O   
564  C CB  . LEU   A 69  ? 0.45765 0.90570 0.73116 0.00075  0.00011  -0.10621 66  LEU   A CB  
565  C CG  . LEU   A 69  ? 0.53609 0.97947 0.80867 0.02347  -0.02050 -0.11866 66  LEU   A CG  
566  C CD1 . LEU   A 69  ? 0.43966 0.87024 0.70892 0.02189  -0.02840 -0.11592 66  LEU   A CD1 
567  C CD2 . LEU   A 69  ? 0.54253 0.94676 0.79148 0.03723  -0.03154 -0.11293 66  LEU   A CD2 
568  N N   . LEU   A 70  ? 0.47218 1.03293 0.80933 -0.01124 0.00773  -0.14467 67  LEU   A N   
569  C CA  . LEU   A 70  ? 0.45112 1.06911 0.81785 -0.00768 0.00889  -0.16801 67  LEU   A CA  
570  C C   . LEU   A 70  ? 0.48143 1.10840 0.85522 0.02247  -0.01170 -0.18617 67  LEU   A C   
571  O O   . LEU   A 70  ? 0.56930 1.23379 0.95996 0.03305  -0.01116 -0.20428 67  LEU   A O   
572  C CB  . LEU   A 70  ? 0.51772 1.16292 0.90270 -0.02447 0.01370  -0.17334 67  LEU   A CB  
573  C CG  . LEU   A 70  ? 0.46592 1.10407 0.84406 -0.05504 0.03342  -0.15795 67  LEU   A CG  
574  C CD1 . LEU   A 70  ? 0.51455 1.17777 0.90970 -0.07143 0.03630  -0.16492 67  LEU   A CD1 
575  C CD2 . LEU   A 70  ? 0.56094 1.22028 0.94042 -0.06702 0.05079  -0.15847 67  LEU   A CD2 
576  N N   . ASP   A 71  ? 0.53686 1.12866 0.89600 0.03699  -0.03042 -0.18222 68  ASP   A N   
577  C CA  . ASP   A 71  ? 0.56880 1.16291 0.93058 0.06653  -0.05314 -0.19919 68  ASP   A CA  
578  C C   . ASP   A 71  ? 0.47103 1.00416 0.80003 0.07738  -0.07043 -0.18505 68  ASP   A C   
579  O O   . ASP   A 71  ? 0.54158 1.04297 0.85366 0.06199  -0.06502 -0.16652 68  ASP   A O   
580  C CB  . ASP   A 71  ? 0.62208 1.26817 1.01607 0.07290  -0.06066 -0.22271 68  ASP   A CB  
581  C CG  . ASP   A 71  ? 0.67756 1.33824 1.08045 0.10583  -0.08310 -0.24551 68  ASP   A CG  
582  O OD1 . ASP   A 71  ? 0.83868 1.46829 1.22170 0.12266  -0.09185 -0.24307 68  ASP   A OD1 
583  O OD2 . ASP   A 71  ? 0.68724 1.39006 1.11693 0.11534  -0.09304 -0.26673 68  ASP   A OD2 
584  N N   . VAL   A 72  ? 0.54248 1.05872 0.86103 0.10393  -0.09139 -0.19464 69  VAL   A N   
585  C CA  . VAL   A 72  ? 0.53689 0.99491 0.82134 0.11581  -0.11072 -0.18397 69  VAL   A CA  
586  C C   . VAL   A 72  ? 0.60602 1.07514 0.89746 0.14238  -0.13633 -0.20476 69  VAL   A C   
587  O O   . VAL   A 72  ? 0.72130 1.20369 1.01991 0.16506  -0.14859 -0.22210 69  VAL   A O   
588  C CB  . VAL   A 72  ? 0.60608 1.01796 0.86096 0.12149  -0.11362 -0.17215 69  VAL   A CB  
589  C CG1 . VAL   A 72  ? 0.57813 0.92902 0.79499 0.13052  -0.13298 -0.16107 69  VAL   A CG1 
590  C CG2 . VAL   A 72  ? 0.49410 0.89938 0.74487 0.09689  -0.08967 -0.15360 69  VAL   A CG2 
591  N N   . ILE   A 73  ? 0.59688 1.06032 0.88574 0.14094  -0.14555 -0.20413 70  ILE   A N   
592  C CA  . ILE   A 73  ? 0.59033 1.06798 0.88792 0.16520  -0.17077 -0.22456 70  ILE   A CA  
593  C C   . ILE   A 73  ? 0.63819 1.04856 0.89139 0.17770  -0.19355 -0.21306 70  ILE   A C   
594  O O   . ILE   A 73  ? 0.69507 1.06827 0.92337 0.16048  -0.18745 -0.19276 70  ILE   A O   
595  C CB  . ILE   A 73  ? 0.61595 1.14314 0.94579 0.15403  -0.16560 -0.23550 70  ILE   A CB  
596  C CG1 . ILE   A 73  ? 0.62849 1.21818 0.99732 0.13628  -0.14053 -0.24445 70  ILE   A CG1 
597  C CG2 . ILE   A 73  ? 0.61956 1.16620 0.96155 0.18109  -0.19343 -0.25907 70  ILE   A CG2 
598  C CD1 . ILE   A 73  ? 0.76342 1.40255 1.16407 0.12118  -0.13365 -0.25518 70  ILE   A CD1 
599  N N   . HIS   A 74  ? 0.60240 0.99625 0.84398 0.20757  -0.21996 -0.22659 71  HIS   A N   
600  C CA  . HIS   A 74  ? 0.82509 1.15222 1.02042 0.22161  -0.24527 -0.21775 71  HIS   A CA  
601  C C   . HIS   A 74  ? 0.81684 1.16185 1.02221 0.24177  -0.27000 -0.23673 71  HIS   A C   
602  O O   . HIS   A 74  ? 0.85994 1.22845 1.08163 0.27008  -0.29002 -0.26048 71  HIS   A O   
603  C CB  . HIS   A 74  ? 0.75260 1.03760 0.92039 0.24090  -0.26002 -0.21789 71  HIS   A CB  
604  C CG  . HIS   A 74  ? 0.73002 0.94121 0.84515 0.25393  -0.28676 -0.20832 71  HIS   A CG  
605  N ND1 . HIS   A 74  ? 1.02120 1.19437 1.10616 0.23928  -0.28786 -0.19077 71  HIS   A ND1 
606  C CD2 . HIS   A 74  ? 0.89278 1.05847 0.97684 0.27958  -0.31373 -0.21386 71  HIS   A CD2 
607  C CE1 . HIS   A 74  ? 1.00977 1.11730 1.04604 0.25375  -0.31347 -0.18509 71  HIS   A CE1 
608  N NE2 . HIS   A 74  ? 1.02004 1.11967 1.05404 0.27837  -0.33032 -0.19849 71  HIS   A NE2 
609  N N   . THR   A 75  ? 0.91538 1.25020 1.11136 0.22816  -0.26934 -0.22746 72  THR   A N   
610  C CA  . THR   A 75  ? 1.04275 1.39369 1.24696 0.24411  -0.29222 -0.24388 72  THR   A CA  
611  C C   . THR   A 75  ? 1.05854 1.33788 1.20826 0.24595  -0.31047 -0.22734 72  THR   A C   
612  O O   . THR   A 75  ? 0.98667 1.23229 1.11098 0.22117  -0.29393 -0.20399 72  THR   A O   
613  C CB  . THR   A 75  ? 0.96215 1.37574 1.20954 0.22449  -0.27440 -0.25158 72  THR   A CB  
614  O OG1 . THR   A 75  ? 1.24299 1.72393 1.53871 0.22227  -0.25824 -0.26837 72  THR   A OG1 
615  C CG2 . THR   A 75  ? 1.20035 1.62917 1.45506 0.23987  -0.29912 -0.26831 72  THR   A CG2 
616  N N   . GLU   A 76  ? 1.22874 1.48535 1.35974 0.27553  -0.34470 -0.24020 73  GLU   A N   
617  C CA  . GLU   A 76  ? 1.29139 1.47589 1.36478 0.28038  -0.36661 -0.22637 73  GLU   A CA  
618  C C   . GLU   A 76  ? 1.14448 1.26096 1.16934 0.26728  -0.35779 -0.20053 73  GLU   A C   
619  O O   . GLU   A 76  ? 1.26663 1.38063 1.29528 0.27295  -0.35358 -0.20163 73  GLU   A O   
620  C CB  . GLU   A 76  ? 1.29555 1.49077 1.37102 0.26259  -0.36033 -0.22125 73  GLU   A CB  
621  C CG  . GLU   A 76  ? 1.39271 1.66037 1.52032 0.27178  -0.36678 -0.24744 73  GLU   A CG  
622  C CD  . GLU   A 76  ? 1.52501 1.80417 1.65632 0.24969  -0.35649 -0.24122 73  GLU   A CD  
623  O OE1 . GLU   A 76  ? 1.55208 1.77751 1.63991 0.23274  -0.34987 -0.21822 73  GLU   A OE1 
624  O OE2 . GLU   A 76  ? 1.61763 1.96048 1.79534 0.24856  -0.35466 -0.26018 73  GLU   A OE2 
625  N N   . ASN   A 77  ? 1.12023 1.18291 1.09963 0.24922  -0.35457 -0.17824 74  ASN   A N   
626  C CA  . ASN   A 77  ? 1.20148 1.20701 1.13881 0.23116  -0.34195 -0.15367 74  ASN   A CA  
627  C C   . ASN   A 77  ? 1.09742 1.13044 1.05763 0.19861  -0.30376 -0.13945 74  ASN   A C   
628  O O   . ASN   A 77  ? 1.02967 1.02162 0.95600 0.17705  -0.29052 -0.11795 74  ASN   A O   
629  C CB  . ASN   A 77  ? 1.38569 1.31702 1.25799 0.22856  -0.35898 -0.13794 74  ASN   A CB  
630  C CG  . ASN   A 77  ? 1.53334 1.39503 1.35386 0.22422  -0.36276 -0.12070 74  ASN   A CG  
631  O OD1 . ASN   A 77  ? 1.35420 1.22286 1.18709 0.21370  -0.34424 -0.11470 74  ASN   A OD1 
632  N ND2 . ASN   A 77  ? 1.62640 1.41875 1.38640 0.23125  -0.38740 -0.11259 74  ASN   A ND2 
633  N N   . LYS   A 78  ? 0.94477 1.04636 0.96077 0.19439  -0.28613 -0.15159 75  LYS   A N   
634  C CA  . LYS   A 78  ? 0.90310 1.03260 0.94224 0.16549  -0.25242 -0.14005 75  LYS   A CA  
635  C C   . LYS   A 78  ? 1.01198 1.18325 1.08856 0.16522  -0.23688 -0.14725 75  LYS   A C   
636  O O   . LYS   A 78  ? 0.83133 1.02708 0.92760 0.18721  -0.25020 -0.16588 75  LYS   A O   
637  C CB  . LYS   A 78  ? 1.01254 1.18288 1.07903 0.15441  -0.24408 -0.14585 75  LYS   A CB  
638  C CG  . LYS   A 78  ? 1.09895 1.23363 1.13078 0.15629  -0.26076 -0.14178 75  LYS   A CG  
639  C CD  . LYS   A 78  ? 1.18131 1.36308 1.24588 0.15209  -0.25920 -0.15440 75  LYS   A CD  
640  C CE  . LYS   A 78  ? 1.15638 1.39433 1.26499 0.17279  -0.27275 -0.18090 75  LYS   A CE  
641  N NZ  . LYS   A 78  ? 1.03050 1.31691 1.17272 0.16606  -0.27084 -0.19402 75  LYS   A NZ  
642  N N   . LEU   A 79  ? 0.81832 0.99777 0.90375 0.14070  -0.20886 -0.13309 76  LEU   A N   
643  C CA  . LEU   A 79  ? 0.72219 0.93939 0.83979 0.13609  -0.19113 -0.13719 76  LEU   A CA  
644  C C   . LEU   A 79  ? 0.71040 0.96945 0.85928 0.11282  -0.16557 -0.13402 76  LEU   A C   
645  O O   . LEU   A 79  ? 0.74610 0.98429 0.88024 0.09292  -0.15149 -0.11706 76  LEU   A O   
646  C CB  . LEU   A 79  ? 0.73059 0.90772 0.82206 0.13009  -0.18445 -0.12184 76  LEU   A CB  
647  C CG  . LEU   A 79  ? 0.70077 0.90876 0.81812 0.13036  -0.17157 -0.12739 76  LEU   A CG  
648  C CD1 . LEU   A 79  ? 0.64420 0.87655 0.77849 0.15791  -0.19002 -0.15062 76  LEU   A CD1 
649  C CD2 . LEU   A 79  ? 0.60425 0.77033 0.69410 0.12097  -0.16452 -0.11053 76  LEU   A CD2 
650  N N   . TYR   A 80  ? 0.58569 0.90291 0.77638 0.11501  -0.15983 -0.15095 77  TYR   A N   
651  C CA  . TYR   A 80  ? 0.60921 0.96582 0.82866 0.09269  -0.13735 -0.14959 77  TYR   A CA  
652  C C   . TYR   A 80  ? 0.67922 1.05825 0.91609 0.08218  -0.11678 -0.14679 77  TYR   A C   
653  O O   . TYR   A 80  ? 0.55517 0.95764 0.80697 0.09568  -0.12050 -0.16001 77  TYR   A O   
654  C CB  . TYR   A 80  ? 0.71588 1.12343 0.96881 0.09769  -0.14402 -0.17042 77  TYR   A CB  
655  C CG  . TYR   A 80  ? 0.85345 1.24298 1.09153 0.10143  -0.16003 -0.17132 77  TYR   A CG  
656  C CD1 . TYR   A 80  ? 0.82421 1.21037 1.06022 0.08034  -0.14801 -0.16151 77  TYR   A CD1 
657  C CD2 . TYR   A 80  ? 0.94292 1.31650 1.16685 0.12694  -0.18840 -0.18247 77  TYR   A CD2 
658  C CE1 . TYR   A 80  ? 0.92632 1.29565 1.14700 0.08358  -0.16263 -0.16287 77  TYR   A CE1 
659  C CE2 . TYR   A 80  ? 1.01286 1.36809 1.22010 0.13046  -0.20408 -0.18316 77  TYR   A CE2 
660  C CZ  . TYR   A 80  ? 0.98384 1.33804 1.18978 0.10824  -0.19050 -0.17338 77  TYR   A CZ  
661  O OH  . TYR   A 80  ? 1.10702 1.44267 1.29471 0.11161  -0.20607 -0.17461 77  TYR   A OH  
662  N N   . LEU   A 81  ? 0.57580 0.94689 0.80946 0.05922  -0.09606 -0.13041 78  LEU   A N   
663  C CA  . LEU   A 81  ? 0.54612 0.93510 0.79293 0.04674  -0.07618 -0.12572 78  LEU   A CA  
664  C C   . LEU   A 81  ? 0.50469 0.93236 0.77760 0.02725  -0.05962 -0.12855 78  LEU   A C   
665  O O   . LEU   A 81  ? 0.51849 0.93240 0.78449 0.01250  -0.05307 -0.11837 78  LEU   A O   
666  C CB  . LEU   A 81  ? 0.60765 0.95369 0.82794 0.03660  -0.06708 -0.10468 78  LEU   A CB  
667  C CG  . LEU   A 81  ? 0.59946 0.90953 0.79515 0.04977  -0.07764 -0.10016 78  LEU   A CG  
668  C CD1 . LEU   A 81  ? 0.56410 0.83922 0.73401 0.06485  -0.09978 -0.10160 78  LEU   A CD1 
669  C CD2 . LEU   A 81  ? 0.52316 0.80476 0.70206 0.03487  -0.06399 -0.08123 78  LEU   A CD2 
670  N N   . VAL   A 82  ? 0.41043 0.88531 0.71155 0.02653  -0.05282 -0.14284 79  VAL   A N   
671  C CA  . VAL   A 82  ? 0.38685 0.90061 0.71220 0.00637  -0.03754 -0.14739 79  VAL   A CA  
672  C C   . VAL   A 82  ? 0.53065 1.03965 0.85175 -0.01247 -0.01661 -0.13363 79  VAL   A C   
673  O O   . VAL   A 82  ? 0.47884 0.99739 0.80210 -0.00821 -0.01157 -0.13586 79  VAL   A O   
674  C CB  . VAL   A 82  ? 0.47204 1.04410 0.83084 0.01377  -0.04103 -0.17223 79  VAL   A CB  
675  C CG1 . VAL   A 82  ? 0.54397 1.15389 0.92539 -0.01068 -0.02563 -0.17662 79  VAL   A CG1 
676  C CG2 . VAL   A 82  ? 0.48665 1.06032 0.84778 0.03769  -0.06573 -0.18698 79  VAL   A CG2 
677  N N   . PHE   A 83  ? 0.39856 0.89146 0.71223 -0.03224 -0.00564 -0.12014 80  PHE   A N   
678  C CA  . PHE   A 83  ? 0.44002 0.92241 0.74616 -0.04970 0.01186  -0.10606 80  PHE   A CA  
679  C C   . PHE   A 83  ? 0.50049 1.01153 0.82214 -0.07220 0.02565  -0.10927 80  PHE   A C   
680  O O   . PHE   A 83  ? 0.36590 0.89636 0.70106 -0.07752 0.02233  -0.11861 80  PHE   A O   
681  C CB  . PHE   A 83  ? 0.39203 0.82605 0.67292 -0.05372 0.01286  -0.08679 80  PHE   A CB  
682  C CG  . PHE   A 83  ? 0.42146 0.82446 0.68352 -0.03821 0.00410  -0.08020 80  PHE   A CG  
683  C CD1 . PHE   A 83  ? 0.53735 0.93066 0.79185 -0.03849 0.01076  -0.07259 80  PHE   A CD1 
684  C CD2 . PHE   A 83  ? 0.55283 0.93406 0.80217 -0.02482 -0.01114 -0.08128 80  PHE   A CD2 
685  C CE1 . PHE   A 83  ? 0.49545 0.85975 0.73234 -0.02655 0.00270  -0.06682 80  PHE   A CE1 
686  C CE2 . PHE   A 83  ? 0.54886 0.89843 0.77765 -0.01365 -0.01884 -0.07457 80  PHE   A CE2 
687  C CZ  . PHE   A 83  ? 0.47924 0.82111 0.70289 -0.01500 -0.01171 -0.06759 80  PHE   A CZ  
688  N N   . GLU   A 84  ? 0.47371 0.98519 0.79111 -0.08628 0.04060  -0.10128 81  GLU   A N   
689  C CA  . GLU   A 84  ? 0.37207 0.89450 0.69331 -0.11149 0.05451  -0.09841 81  GLU   A CA  
690  C C   . GLU   A 84  ? 0.49815 0.98483 0.80503 -0.12040 0.05330  -0.08604 81  GLU   A C   
691  O O   . GLU   A 84  ? 0.44390 0.89269 0.73265 -0.11185 0.04862  -0.07393 81  GLU   A O   
692  C CB  . GLU   A 84  ? 0.37917 0.89840 0.69043 -0.12284 0.06856  -0.08964 81  GLU   A CB  
693  C CG  . GLU   A 84  ? 0.64405 1.15727 0.94779 -0.14978 0.08202  -0.08115 81  GLU   A CG  
694  C CD  . GLU   A 84  ? 0.56616 1.06164 0.85120 -0.15785 0.09235  -0.06857 81  GLU   A CD  
695  O OE1 . GLU   A 84  ? 0.52281 1.00777 0.80095 -0.14219 0.08863  -0.06528 81  GLU   A OE1 
696  O OE2 . GLU   A 84  ? 0.71751 1.20727 0.99270 -0.18022 0.10324  -0.06191 81  GLU   A OE2 
697  N N   . PHE   A 85  ? 0.45467 0.95455 0.76985 -0.13814 0.05770  -0.09022 82  PHE   A N   
698  C CA  . PHE   A 85  ? 0.40087 0.86936 0.70369 -0.14605 0.05552  -0.08162 82  PHE   A CA  
699  C C   . PHE   A 85  ? 0.42781 0.87232 0.71472 -0.16657 0.06784  -0.06803 82  PHE   A C   
700  O O   . PHE   A 85  ? 0.51928 0.98331 0.81074 -0.18469 0.07862  -0.07028 82  PHE   A O   
701  C CB  . PHE   A 85  ? 0.45362 0.94636 0.77316 -0.15176 0.04959  -0.09535 82  PHE   A CB  
702  C CG  . PHE   A 85  ? 0.41100 0.87211 0.71717 -0.16102 0.04761  -0.08803 82  PHE   A CG  
703  C CD1 . PHE   A 85  ? 0.42619 0.85699 0.71865 -0.14597 0.03709  -0.08313 82  PHE   A CD1 
704  C CD2 . PHE   A 85  ? 0.52729 0.98723 0.83226 -0.18553 0.05639  -0.08636 82  PHE   A CD2 
705  C CE1 . PHE   A 85  ? 0.51256 0.91552 0.79232 -0.15348 0.03565  -0.07797 82  PHE   A CE1 
706  C CE2 . PHE   A 85  ? 0.44079 0.86932 0.73224 -0.19274 0.05355  -0.08077 82  PHE   A CE2 
707  C CZ  . PHE   A 85  ? 0.37863 0.78015 0.65845 -0.17584 0.04333  -0.07719 82  PHE   A CZ  
708  N N   . LEU   A 86  ? 0.43597 0.83781 0.70300 -0.16365 0.06580  -0.05459 83  LEU   A N   
709  C CA  . LEU   A 86  ? 0.41976 0.79132 0.66911 -0.17963 0.07335  -0.04225 83  LEU   A CA  
710  C C   . LEU   A 86  ? 0.45318 0.79705 0.69374 -0.17996 0.06737  -0.03966 83  LEU   A C   
711  O O   . LEU   A 86  ? 0.38755 0.72324 0.62738 -0.16408 0.05876  -0.04112 83  LEU   A O   
712  C CB  . LEU   A 86  ? 0.52266 0.86944 0.75592 -0.17318 0.07668  -0.02916 83  LEU   A CB  
713  C CG  . LEU   A 86  ? 0.62922 0.99772 0.86582 -0.17502 0.08372  -0.03021 83  LEU   A CG  
714  C CD1 . LEU   A 86  ? 0.42505 0.81301 0.67308 -0.15449 0.07743  -0.03752 83  LEU   A CD1 
715  C CD2 . LEU   A 86  ? 0.42228 0.76111 0.63786 -0.17984 0.08900  -0.01589 83  LEU   A CD2 
716  N N   . HIS   A 87  ? 0.49420 0.82143 0.72540 -0.19869 0.07183  -0.03595 84  HIS   A N   
717  C CA  . HIS   A 87  ? 0.55317 0.86210 0.77958 -0.20187 0.06605  -0.03808 84  HIS   A CA  
718  C C   . HIS   A 87  ? 0.54234 0.81066 0.75058 -0.18989 0.06217  -0.02859 84  HIS   A C   
719  O O   . HIS   A 87  ? 0.58554 0.84037 0.78986 -0.18733 0.05636  -0.03186 84  HIS   A O   
720  C CB  . HIS   A 87  ? 0.48171 0.78592 0.70350 -0.22768 0.07140  -0.03874 84  HIS   A CB  
721  C CG  . HIS   A 87  ? 0.63485 0.89834 0.83204 -0.23703 0.07607  -0.02506 84  HIS   A CG  
722  N ND1 . HIS   A 87  ? 0.70221 0.96050 0.89044 -0.23732 0.08228  -0.01605 84  HIS   A ND1 
723  C CD2 . HIS   A 87  ? 0.70593 0.92985 0.88391 -0.24523 0.07383  -0.01952 84  HIS   A CD2 
724  C CE1 . HIS   A 87  ? 0.65748 0.87428 0.82165 -0.24486 0.08290  -0.00515 84  HIS   A CE1 
725  N NE2 . HIS   A 87  ? 0.78462 0.97939 0.94227 -0.24933 0.07769  -0.00724 84  HIS   A NE2 
726  N N   . GLN   A 88  ? 0.48906 0.73988 0.68688 -0.18235 0.06510  -0.01830 85  GLN   A N   
727  C CA  . GLN   A 88  ? 0.52307 0.73937 0.70604 -0.17234 0.06228  -0.01105 85  GLN   A CA  
728  C C   . GLN   A 88  ? 0.59053 0.80204 0.77010 -0.16003 0.06395  -0.00325 85  GLN   A C   
729  O O   . GLN   A 88  ? 0.49601 0.72036 0.67815 -0.16344 0.06826  -0.00064 85  GLN   A O   
730  C CB  . GLN   A 88  ? 0.63720 0.82153 0.80397 -0.18522 0.06340  -0.00618 85  GLN   A CB  
731  C CG  . GLN   A 88  ? 0.68485 0.83700 0.83914 -0.17415 0.05898  -0.00350 85  GLN   A CG  
732  C CD  . GLN   A 88  ? 0.74081 0.85782 0.87723 -0.18520 0.05796  0.00029  85  GLN   A CD  
733  O OE1 . GLN   A 88  ? 1.08745 1.18229 1.21573 -0.18112 0.05344  -0.00267 85  GLN   A OE1 
734  N NE2 . GLN   A 88  ? 0.62526 0.73466 0.75282 -0.19935 0.06174  0.00665  85  GLN   A NE2 
735  N N   . ASP   A 89  ? 0.46464 0.65924 0.63844 -0.14650 0.06084  -0.00050 86  ASP   A N   
736  C CA  . ASP   A 89  ? 0.54246 0.73038 0.71295 -0.13595 0.06191  0.00647  86  ASP   A CA  
737  C C   . ASP   A 89  ? 0.51065 0.66936 0.66794 -0.13711 0.06227  0.01336  86  ASP   A C   
738  O O   . ASP   A 89  ? 0.51660 0.65594 0.66537 -0.14386 0.06087  0.01261  86  ASP   A O   
739  C CB  . ASP   A 89  ? 0.45511 0.64554 0.62783 -0.12174 0.05887  0.00452  86  ASP   A CB  
740  C CG  . ASP   A 89  ? 0.56311 0.73655 0.72899 -0.11836 0.05682  0.00180  86  ASP   A CG  
741  O OD1 . ASP   A 89  ? 0.91431 1.07222 1.07421 -0.12525 0.05654  0.00094  86  ASP   A OD1 
742  O OD2 . ASP   A 89  ? 0.67495 0.84934 0.83951 -0.10936 0.05554  0.00021  86  ASP   A OD2 
743  N N   . LEU   A 90  ? 0.49463 0.64889 0.64950 -0.12960 0.06274  0.01945  87  LEU   A N   
744  C CA  . LEU   A 90  ? 0.59233 0.71921 0.73443 -0.12847 0.06089  0.02551  87  LEU   A CA  
745  C C   . LEU   A 90  ? 0.50065 0.60965 0.63960 -0.11915 0.05733  0.02229  87  LEU   A C   
746  O O   . LEU   A 90  ? 0.55361 0.63574 0.68034 -0.12024 0.05392  0.02400  87  LEU   A O   
747  C CB  . LEU   A 90  ? 0.47263 0.60193 0.61442 -0.12125 0.06081  0.03138  87  LEU   A CB  
748  C CG  . LEU   A 90  ? 0.46803 0.56930 0.59558 -0.11847 0.05665  0.03762  87  LEU   A CG  
749  C CD1 . LEU   A 90  ? 0.57179 0.65245 0.68213 -0.13409 0.05679  0.04195  87  LEU   A CD1 
750  C CD2 . LEU   A 90  ? 0.45958 0.56719 0.58839 -0.11103 0.05565  0.04224  87  LEU   A CD2 
751  N N   . LYS   A 91  ? 0.48277 0.60464 0.63041 -0.11014 0.05780  0.01715  88  LYS   A N   
752  C CA  . LYS   A 91  ? 0.41851 0.52759 0.56354 -0.10112 0.05606  0.01263  88  LYS   A CA  
753  C C   . LYS   A 91  ? 0.53527 0.62662 0.67172 -0.10763 0.05373  0.00824  88  LYS   A C   
754  O O   . LYS   A 91  ? 0.59038 0.65910 0.71867 -0.10249 0.05044  0.00633  88  LYS   A O   
755  C CB  . LYS   A 91  ? 0.52688 0.65339 0.67925 -0.09382 0.05843  0.00830  88  LYS   A CB  
756  C CG  . LYS   A 91  ? 0.55533 0.67530 0.70699 -0.08349 0.05896  0.00346  88  LYS   A CG  
757  C CD  . LYS   A 91  ? 0.76762 0.88758 0.91515 -0.08366 0.06001  -0.00396 88  LYS   A CD  
758  C CE  . LYS   A 91  ? 1.00241 1.13995 1.15186 -0.08334 0.06288  -0.00455 88  LYS   A CE  
759  N NZ  . LYS   A 91  ? 0.86794 1.00303 1.00919 -0.08328 0.06354  -0.01143 88  LYS   A NZ  
760  N N   . LYS   A 92  ? 0.49918 0.60063 0.63766 -0.11829 0.05439  0.00543  89  LYS   A N   
761  C CA  . LYS   A 92  ? 0.59853 0.68353 0.72889 -0.12709 0.05171  0.00101  89  LYS   A CA  
762  C C   . LYS   A 92  ? 0.65377 0.71264 0.77111 -0.13664 0.04973  0.00645  89  LYS   A C   
763  O O   . LYS   A 92  ? 0.58646 0.61768 0.69142 -0.13850 0.04555  0.00405  89  LYS   A O   
764  C CB  . LYS   A 92  ? 0.65305 0.75886 0.79089 -0.13719 0.05204  -0.00394 89  LYS   A CB  
765  C CG  . LYS   A 92  ? 0.81008 0.92757 0.95160 -0.12937 0.05049  -0.01102 89  LYS   A CG  
766  C CD  . LYS   A 92  ? 1.01699 1.15369 1.16570 -0.13833 0.04808  -0.01698 89  LYS   A CD  
767  C CE  . LYS   A 92  ? 0.96145 1.08740 1.10635 -0.15412 0.04669  -0.01956 89  LYS   A CE  
768  N NZ  . LYS   A 92  ? 1.11817 1.26958 1.27452 -0.16392 0.04450  -0.02677 89  LYS   A NZ  
769  N N   . PHE   A 93  ? 0.58917 0.65363 0.70618 -0.14314 0.05221  0.01374  90  PHE   A N   
770  C CA  . PHE   A 93  ? 0.57900 0.61528 0.67839 -0.15420 0.05034  0.02038  90  PHE   A CA  
771  C C   . PHE   A 93  ? 0.60134 0.60586 0.68798 -0.14066 0.04394  0.02333  90  PHE   A C   
772  O O   . PHE   A 93  ? 0.66928 0.63779 0.73673 -0.14558 0.03837  0.02517  90  PHE   A O   
773  C CB  . PHE   A 93  ? 0.62196 0.67409 0.72241 -0.16427 0.05540  0.02691  90  PHE   A CB  
774  C CG  . PHE   A 93  ? 0.59005 0.61200 0.66777 -0.17838 0.05429  0.03500  90  PHE   A CG  
775  C CD1 . PHE   A 93  ? 0.70226 0.71232 0.76926 -0.19950 0.05560  0.03435  90  PHE   A CD1 
776  C CD2 . PHE   A 93  ? 0.63038 0.63455 0.69546 -0.17171 0.05139  0.04331  90  PHE   A CD2 
777  C CE1 . PHE   A 93  ? 0.67352 0.65140 0.71464 -0.21515 0.05474  0.04283  90  PHE   A CE1 
778  C CE2 . PHE   A 93  ? 0.77501 0.74640 0.81372 -0.18520 0.04930  0.05174  90  PHE   A CE2 
779  C CZ  . PHE   A 93  ? 0.71315 0.66991 0.73841 -0.20769 0.05135  0.05201  90  PHE   A CZ  
780  N N   . MET   A 94  ? 0.58549 0.60242 0.68229 -0.12348 0.04376  0.02298  91  MET   A N   
781  C CA  . MET   A 94  ? 0.65167 0.64508 0.74114 -0.10800 0.03692  0.02288  91  MET   A CA  
782  C C   . MET   A 94  ? 0.59028 0.56689 0.67623 -0.10047 0.03295  0.01381  91  MET   A C   
783  O O   . MET   A 94  ? 0.67246 0.61517 0.74336 -0.09437 0.02483  0.01313  91  MET   A O   
784  C CB  . MET   A 94  ? 0.56886 0.58616 0.67377 -0.09319 0.03861  0.02256  91  MET   A CB  
785  C CG  . MET   A 94  ? 0.62899 0.66133 0.73634 -0.09862 0.04156  0.03053  91  MET   A CG  
786  S SD  . MET   A 94  ? 0.84604 0.91349 0.97451 -0.08634 0.04548  0.02822  91  MET   A SD  
787  C CE  . MET   A 94  ? 0.73511 0.78793 0.85899 -0.07321 0.03766  0.03172  91  MET   A CE  
788  N N   . ASP   A 95  ? 0.57486 0.57268 0.67235 -0.10002 0.03761  0.00630  92  ASP   A N   
789  C CA  . ASP   A 95  ? 0.67057 0.65402 0.76347 -0.09344 0.03461  -0.00338 92  ASP   A CA  
790  C C   . ASP   A 95  ? 0.63598 0.58688 0.71073 -0.10655 0.02940  -0.00337 92  ASP   A C   
791  O O   . ASP   A 95  ? 0.68093 0.60152 0.74311 -0.09930 0.02252  -0.00862 92  ASP   A O   
792  C CB  . ASP   A 95  ? 0.67647 0.68826 0.78153 -0.09212 0.04060  -0.01042 92  ASP   A CB  
793  C CG  . ASP   A 95  ? 0.74310 0.78157 0.86216 -0.08020 0.04554  -0.01128 92  ASP   A CG  
794  O OD1 . ASP   A 95  ? 0.82488 0.86214 0.94715 -0.07141 0.04398  -0.00818 92  ASP   A OD1 
795  O OD2 . ASP   A 95  ? 0.75603 0.81537 0.88134 -0.08039 0.05032  -0.01508 92  ASP   A OD2 
796  N N   . ALA   A 96  ? 0.65541 0.61251 0.72860 -0.12619 0.03239  0.00145  93  ALA   A N   
797  C CA  . ALA   A 96  ? 0.73810 0.66504 0.79351 -0.14280 0.02821  0.00194  93  ALA   A CA  
798  C C   . ALA   A 96  ? 0.68336 0.56830 0.71588 -0.14386 0.02105  0.00958  93  ALA   A C   
799  O O   . ALA   A 96  ? 0.80223 0.64811 0.81404 -0.15072 0.01408  0.00849  93  ALA   A O   
800  C CB  . ALA   A 96  ? 0.69167 0.64183 0.75384 -0.16460 0.03418  0.00408  93  ALA   A CB  
801  N N   . SER   A 97  ? 0.74791 0.63713 0.78133 -0.13709 0.02138  0.01727  94  SER   A N   
802  C CA  . SER   A 97  ? 0.66825 0.51655 0.67751 -0.13614 0.01296  0.02526  94  SER   A CA  
803  C C   . SER   A 97  ? 0.88750 0.71884 0.89553 -0.10969 0.00367  0.02036  94  SER   A C   
804  O O   . SER   A 97  ? 0.81204 0.61363 0.80277 -0.10338 -0.00512 0.02647  94  SER   A O   
805  C CB  . SER   A 97  ? 0.70391 0.56558 0.71220 -0.14484 0.01768  0.03621  94  SER   A CB  
806  O OG  . SER   A 97  ? 0.78687 0.67587 0.80309 -0.16636 0.02772  0.03779  94  SER   A OG  
807  N N   . ALA   A 98  ? 0.76201 0.61224 0.78724 -0.09408 0.00510  0.00869  95  ALA   A N   
808  C CA  . ALA   A 98  ? 0.86487 0.71159 0.89563 -0.06833 -0.00147 0.00158  95  ALA   A CA  
809  C C   . ALA   A 98  ? 0.85045 0.64391 0.85573 -0.05965 -0.01611 -0.00086 95  ALA   A C   
810  O O   . ALA   A 98  ? 0.85923 0.63901 0.86142 -0.04071 -0.02560 -0.00223 95  ALA   A O   
811  C CB  . ALA   A 98  ? 0.77681 0.65676 0.82933 -0.05690 0.00530  -0.01112 95  ALA   A CB  
812  N N   . LEU   A 99  ? 0.85315 0.61491 0.83944 -0.07264 -0.01948 -0.00218 96  LEU   A N   
813  C CA  . LEU   A 99  ? 0.98212 0.68731 0.94067 -0.06429 -0.03493 -0.00510 96  LEU   A CA  
814  C C   . LEU   A 99  ? 1.07854 0.74095 1.00699 -0.07525 -0.04371 0.00936  96  LEU   A C   
815  O O   . LEU   A 99  ? 1.08952 0.71649 1.00122 -0.05801 -0.05805 0.00957  96  LEU   A O   
816  C CB  . LEU   A 99  ? 0.95596 0.63964 0.90291 -0.07510 -0.03613 -0.01233 96  LEU   A CB  
817  C CG  . LEU   A 99  ? 1.04627 0.76450 1.01597 -0.06458 -0.02894 -0.02724 96  LEU   A CG  
818  C CD1 . LEU   A 99  ? 1.03251 0.72109 0.98554 -0.07465 -0.03318 -0.03447 96  LEU   A CD1 
819  C CD2 . LEU   A 99  ? 1.00746 0.73720 0.99071 -0.03356 -0.03276 -0.03917 96  LEU   A CD2 
820  N N   . THR   A 100 ? 1.09440 0.75996 1.01468 -0.10372 -0.03561 0.02085  97  THR   A N   
821  C CA  . THR   A 100 ? 1.19431 0.81833 1.08160 -0.11865 -0.04202 0.03521  97  THR   A CA  
822  C C   . THR   A 100 ? 1.10478 0.74851 0.99867 -0.11090 -0.04065 0.04354  97  THR   A C   
823  O O   . THR   A 100 ? 1.09878 0.70157 0.96307 -0.11128 -0.05118 0.05324  97  THR   A O   
824  C CB  . THR   A 100 ? 1.27508 0.89797 1.15119 -0.15435 -0.03248 0.04262  97  THR   A CB  
825  O OG1 . THR   A 100 ? 1.21435 0.89980 1.12279 -0.16295 -0.01615 0.04233  97  THR   A OG1 
826  C CG2 . THR   A 100 ? 1.23352 0.83296 1.10064 -0.16350 -0.03560 0.03427  97  THR   A CG2 
827  N N   . GLY   A 101 ? 1.07080 0.77320 1.00010 -0.10420 -0.02894 0.04006  98  GLY   A N   
828  C CA  . GLY   A 101 ? 0.90654 0.63017 0.84329 -0.09849 -0.02707 0.04722  98  GLY   A CA  
829  C C   . GLY   A 101 ? 0.94969 0.68539 0.87916 -0.12531 -0.01646 0.05890  98  GLY   A C   
830  O O   . GLY   A 101 ? 1.07472 0.77823 0.97682 -0.14807 -0.01675 0.06595  98  GLY   A O   
831  N N   . ILE   A 102 ? 0.96670 0.74901 0.91998 -0.12372 -0.00675 0.06014  99  ILE   A N   
832  C CA  . ILE   A 102 ? 0.85475 0.65230 0.80244 -0.14657 0.00341  0.06946  99  ILE   A CA  
833  C C   . ILE   A 102 ? 0.87937 0.63462 0.79118 -0.15145 -0.00521 0.08166  99  ILE   A C   
834  O O   . ILE   A 102 ? 0.90018 0.64217 0.80782 -0.13054 -0.01622 0.08266  99  ILE   A O   
835  C CB  . ILE   A 102 ? 0.88514 0.73889 0.86523 -0.14040 0.01372  0.06669  99  ILE   A CB  
836  C CG1 . ILE   A 102 ? 0.87888 0.76793 0.88937 -0.13363 0.01996  0.05516  99  ILE   A CG1 
837  C CG2 . ILE   A 102 ? 0.80629 0.67954 0.78280 -0.16271 0.02467  0.07347  99  ILE   A CG2 
838  C CD1 . ILE   A 102 ? 0.72420 0.66257 0.76308 -0.12722 0.02843  0.05239  99  ILE   A CD1 
839  N N   . PRO   A 103 ? 0.97394 0.70667 0.85805 -0.17879 -0.00117 0.09066  100 PRO   A N   
840  C CA  . PRO   A 103 ? 0.94597 0.63418 0.78985 -0.18540 -0.00938 0.10348  100 PRO   A CA  
841  C C   . PRO   A 103 ? 0.83508 0.55041 0.68793 -0.17542 -0.00732 0.10737  100 PRO   A C   
842  O O   . PRO   A 103 ? 0.85822 0.62670 0.74087 -0.17776 0.00575  0.10355  100 PRO   A O   
843  C CB  . PRO   A 103 ? 1.06935 0.74478 0.88917 -0.22194 0.00059  0.11062  100 PRO   A CB  
844  C CG  . PRO   A 103 ? 0.95442 0.64757 0.79513 -0.22997 0.00679  0.10055  100 PRO   A CG  
845  C CD  . PRO   A 103 ? 0.84282 0.58765 0.72902 -0.20587 0.01032  0.08890  100 PRO   A CD  
846  N N   . LEU   A 104 ? 1.01985 0.69591 0.84529 -0.16320 -0.02200 0.11443  101 LEU   A N   
847  C CA  . LEU   A 104 ? 0.95660 0.65395 0.78789 -0.15236 -0.02264 0.11778  101 LEU   A CA  
848  C C   . LEU   A 104 ? 0.99687 0.72184 0.82471 -0.17637 -0.00663 0.12408  101 LEU   A C   
849  O O   . LEU   A 104 ? 0.85032 0.62100 0.70542 -0.16811 0.00025  0.12037  101 LEU   A O   
850  C CB  . LEU   A 104 ? 1.06190 0.70543 0.85738 -0.13776 -0.04315 0.12499  101 LEU   A CB  
851  C CG  . LEU   A 104 ? 1.25176 0.91015 1.04765 -0.12636 -0.04699 0.12887  101 LEU   A CG  
852  C CD1 . LEU   A 104 ? 1.06672 0.78263 0.91309 -0.10428 -0.04325 0.11678  101 LEU   A CD1 
853  C CD2 . LEU   A 104 ? 1.34365 0.94370 1.10046 -0.11178 -0.06992 0.13567  101 LEU   A CD2 
854  N N   . PRO   A 105 ? 0.96535 0.66665 0.76123 -0.20608 0.00006  0.13253  102 PRO   A N   
855  C CA  . PRO   A 105 ? 1.00955 0.74714 0.80795 -0.22802 0.01740  0.13524  102 PRO   A CA  
856  C C   . PRO   A 105 ? 0.90165 0.70502 0.74815 -0.22820 0.03257  0.12329  102 PRO   A C   
857  O O   . PRO   A 105 ? 0.86653 0.71049 0.72772 -0.23118 0.04303  0.12159  102 PRO   A O   
858  C CB  . PRO   A 105 ? 1.07581 0.77538 0.83298 -0.26167 0.02213  0.14424  102 PRO   A CB  
859  C CG  . PRO   A 105 ? 1.03895 0.66771 0.75766 -0.25363 0.00227  0.15140  102 PRO   A CG  
860  C CD  . PRO   A 105 ? 0.90743 0.54510 0.65915 -0.22165 -0.00853 0.14037  102 PRO   A CD  
861  N N   . LEU   A 106 ? 0.82768 0.64084 0.69717 -0.22421 0.03298  0.11450  103 LEU   A N   
862  C CA  . LEU   A 106 ? 0.79472 0.66635 0.70699 -0.22251 0.04490  0.10324  103 LEU   A CA  
863  C C   . LEU   A 106 ? 0.79437 0.69599 0.73670 -0.19471 0.04141  0.09742  103 LEU   A C   
864  O O   . LEU   A 106 ? 0.73826 0.68623 0.70734 -0.19306 0.05067  0.09163  103 LEU   A O   
865  C CB  . LEU   A 106 ? 0.73381 0.60403 0.65748 -0.22797 0.04563  0.09587  103 LEU   A CB  
866  C CG  . LEU   A 106 ? 0.77640 0.70231 0.73938 -0.22867 0.05650  0.08433  103 LEU   A CG  
867  C CD1 . LEU   A 106 ? 0.83991 0.80241 0.80815 -0.24802 0.07034  0.08388  103 LEU   A CD1 
868  C CD2 . LEU   A 106 ? 0.82855 0.74715 0.79670 -0.23627 0.05577  0.07776  103 LEU   A CD2 
869  N N   . ILE   A 107 ? 0.80146 0.67723 0.73958 -0.17292 0.02766  0.09802  104 ILE   A N   
870  C CA  . ILE   A 107 ? 0.81938 0.72247 0.78363 -0.14901 0.02433  0.09285  104 ILE   A CA  
871  C C   . ILE   A 107 ? 0.68624 0.60472 0.64591 -0.15044 0.02728  0.09793  104 ILE   A C   
872  O O   . ILE   A 107 ? 0.63150 0.59013 0.61719 -0.14335 0.03310  0.09270  104 ILE   A O   
873  C CB  . ILE   A 107 ? 0.75818 0.63162 0.71794 -0.12642 0.00863  0.09120  104 ILE   A CB  
874  C CG1 . ILE   A 107 ? 0.88882 0.75482 0.85839 -0.12207 0.00693  0.08320  104 ILE   A CG1 
875  C CG2 . ILE   A 107 ? 0.67958 0.58115 0.66336 -0.10495 0.00520  0.08655  104 ILE   A CG2 
876  C CD1 . ILE   A 107 ? 0.85144 0.69281 0.81956 -0.09827 -0.00791 0.07852  104 ILE   A CD1 
877  N N   . LYS   A 108 ? 0.69467 0.57830 0.61803 -0.16003 0.02266  0.10824  105 LYS   A N   
878  C CA  . LYS   A 108 ? 0.83589 0.73083 0.75006 -0.16234 0.02518  0.11313  105 LYS   A CA  
879  C C   . LYS   A 108 ? 0.69726 0.63465 0.62550 -0.17942 0.04249  0.10955  105 LYS   A C   
880  O O   . LYS   A 108 ? 0.75384 0.72345 0.69768 -0.17287 0.04658  0.10630  105 LYS   A O   
881  C CB  . LYS   A 108 ? 0.75439 0.59828 0.62069 -0.17151 0.01662  0.12552  105 LYS   A CB  
882  C CG  . LYS   A 108 ? 0.92301 0.77180 0.77453 -0.17116 0.01626  0.13089  105 LYS   A CG  
883  C CD  . LYS   A 108 ? 1.05847 0.85007 0.85721 -0.17971 0.00576  0.14394  105 LYS   A CD  
884  C CE  . LYS   A 108 ? 1.10999 0.85680 0.89651 -0.15900 -0.01545 0.14547  105 LYS   A CE  
885  N NZ  . LYS   A 108 ? 1.30414 0.98973 1.03527 -0.16474 -0.02898 0.15855  105 LYS   A NZ  
886  N N   . SER   A 109 ? 0.69473 0.63352 0.61841 -0.20094 0.05209  0.10883  106 SER   A N   
887  C CA  . SER   A 109 ? 0.67621 0.65969 0.61663 -0.21596 0.06793  0.10277  106 SER   A CA  
888  C C   . SER   A 109 ? 0.69594 0.72465 0.67880 -0.19981 0.07077  0.09121  106 SER   A C   
889  O O   . SER   A 109 ? 0.60529 0.67017 0.60318 -0.19857 0.07791  0.08617  106 SER   A O   
890  C CB  . SER   A 109 ? 0.75072 0.72907 0.68139 -0.24210 0.07654  0.10250  106 SER   A CB  
891  O OG  . SER   A 109 ? 0.77574 0.80460 0.73053 -0.25320 0.09077  0.09308  106 SER   A OG  
892  N N   . TYR   A 110 ? 0.65147 0.67661 0.65149 -0.18731 0.06484  0.08661  107 TYR   A N   
893  C CA  . TYR   A 110 ? 0.67323 0.73585 0.70829 -0.17364 0.06701  0.07664  107 TYR   A CA  
894  C C   . TYR   A 110 ? 0.62833 0.70334 0.67311 -0.15561 0.06267  0.07636  107 TYR   A C   
895  O O   . TYR   A 110 ? 0.52858 0.63721 0.59252 -0.15153 0.06757  0.07032  107 TYR   A O   
896  C CB  . TYR   A 110 ? 0.61972 0.67230 0.66597 -0.16532 0.06183  0.07227  107 TYR   A CB  
897  C CG  . TYR   A 110 ? 0.60973 0.66781 0.65947 -0.18134 0.06770  0.06771  107 TYR   A CG  
898  C CD1 . TYR   A 110 ? 0.55600 0.63574 0.60557 -0.20076 0.07783  0.06585  107 TYR   A CD1 
899  C CD2 . TYR   A 110 ? 0.66119 0.70551 0.71547 -0.17709 0.06316  0.06384  107 TYR   A CD2 
900  C CE1 . TYR   A 110 ? 0.57408 0.66249 0.62934 -0.21616 0.08267  0.06032  107 TYR   A CE1 
901  C CE2 . TYR   A 110 ? 0.64763 0.69704 0.70511 -0.19204 0.06746  0.05901  107 TYR   A CE2 
902  C CZ  . TYR   A 110 ? 0.62555 0.69755 0.68431 -0.21183 0.07691  0.05728  107 TYR   A CZ  
903  O OH  . TYR   A 110 ? 0.67053 0.75102 0.73483 -0.22745 0.08068  0.05119  107 TYR   A OH  
904  N N   . LEU   A 111 ? 0.60568 0.65312 0.63720 -0.14426 0.05229  0.08206  108 LEU   A N   
905  C CA  . LEU   A 111 ? 0.61947 0.67887 0.66040 -0.12850 0.04738  0.08128  108 LEU   A CA  
906  C C   . LEU   A 111 ? 0.60505 0.67917 0.63752 -0.13575 0.05287  0.08329  108 LEU   A C   
907  O O   . LEU   A 111 ? 0.58892 0.68846 0.63759 -0.12723 0.05392  0.07868  108 LEU   A O   
908  C CB  . LEU   A 111 ? 0.55360 0.58168 0.58159 -0.11530 0.03397  0.08581  108 LEU   A CB  
909  C CG  . LEU   A 111 ? 0.55469 0.59613 0.59467 -0.09900 0.02750  0.08381  108 LEU   A CG  
910  C CD1 . LEU   A 111 ? 0.53205 0.60267 0.60440 -0.08868 0.03002  0.07478  108 LEU   A CD1 
911  C CD2 . LEU   A 111 ? 0.65291 0.66324 0.67693 -0.08693 0.01287  0.08789  108 LEU   A CD2 
912  N N   . PHE   A 112 ? 0.51650 0.57367 0.52162 -0.15239 0.05658  0.08981  109 PHE   A N   
913  C CA  . PHE   A 112 ? 0.60732 0.67952 0.60188 -0.16083 0.06338  0.09076  109 PHE   A CA  
914  C C   . PHE   A 112 ? 0.63424 0.75091 0.65458 -0.16397 0.07452  0.08033  109 PHE   A C   
915  O O   . PHE   A 112 ? 0.54545 0.68447 0.57361 -0.15756 0.07625  0.07610  109 PHE   A O   
916  C CB  . PHE   A 112 ? 0.65751 0.70260 0.61543 -0.18174 0.06711  0.09953  109 PHE   A CB  
917  C CG  . PHE   A 112 ? 0.60905 0.66516 0.54985 -0.19093 0.07395  0.10119  109 PHE   A CG  
918  C CD1 . PHE   A 112 ? 0.69653 0.73668 0.62005 -0.18072 0.06497  0.10654  109 PHE   A CD1 
919  C CD2 . PHE   A 112 ? 0.71940 0.80356 0.66149 -0.20975 0.08923  0.09618  109 PHE   A CD2 
920  C CE1 . PHE   A 112 ? 0.74291 0.79225 0.64820 -0.18917 0.07132  0.10755  109 PHE   A CE1 
921  C CE2 . PHE   A 112 ? 0.78864 0.88506 0.71435 -0.21819 0.09663  0.09624  109 PHE   A CE2 
922  C CZ  . PHE   A 112 ? 0.70196 0.77951 0.60788 -0.20798 0.08777  0.10231  109 PHE   A CZ  
923  N N   . GLN   A 113 ? 0.54733 0.67630 0.58078 -0.17264 0.08070  0.07517  110 GLN   A N   
924  C CA  . GLN   A 113 ? 0.58146 0.75227 0.64006 -0.17343 0.08890  0.06388  110 GLN   A CA  
925  C C   . GLN   A 113 ? 0.56747 0.75400 0.65062 -0.15313 0.08299  0.05782  110 GLN   A C   
926  O O   . GLN   A 113 ? 0.51232 0.72670 0.60878 -0.14781 0.08576  0.05026  110 GLN   A O   
927  C CB  . GLN   A 113 ? 0.56772 0.74674 0.63446 -0.18693 0.09477  0.05935  110 GLN   A CB  
928  C CG  . GLN   A 113 ? 0.60731 0.77295 0.64954 -0.21137 0.10223  0.06454  110 GLN   A CG  
929  C CD  . GLN   A 113 ? 0.67755 0.85011 0.72890 -0.22539 0.10675  0.05958  110 GLN   A CD  
930  O OE1 . GLN   A 113 ? 0.60767 0.81712 0.68560 -0.22395 0.11096  0.04804  110 GLN   A OE1 
931  N NE2 . GLN   A 113 ? 0.68264 0.81775 0.71092 -0.23833 0.10438  0.06777  110 GLN   A NE2 
932  N N   . LEU   A 114 ? 0.49181 0.66016 0.57988 -0.14210 0.07483  0.06040  111 LEU   A N   
933  C CA  . LEU   A 114 ? 0.51258 0.69330 0.62041 -0.12582 0.07002  0.05556  111 LEU   A CA  
934  C C   . LEU   A 114 ? 0.48910 0.67381 0.59404 -0.11736 0.06657  0.05660  111 LEU   A C   
935  O O   . LEU   A 114 ? 0.49257 0.69628 0.61116 -0.10956 0.06614  0.05055  111 LEU   A O   
936  C CB  . LEU   A 114 ? 0.45521 0.61705 0.56695 -0.11742 0.06338  0.05757  111 LEU   A CB  
937  C CG  . LEU   A 114 ? 0.62576 0.78452 0.74322 -0.12245 0.06536  0.05457  111 LEU   A CG  
938  C CD1 . LEU   A 114 ? 0.52009 0.65886 0.63840 -0.11289 0.05875  0.05591  111 LEU   A CD1 
939  C CD2 . LEU   A 114 ? 0.54291 0.72889 0.67917 -0.12099 0.06890  0.04593  111 LEU   A CD2 
940  N N   . LEU   A 115 ? 0.46959 0.63375 0.55461 -0.11868 0.06279  0.06414  112 LEU   A N   
941  C CA  . LEU   A 115 ? 0.48629 0.65345 0.56666 -0.11143 0.05872  0.06484  112 LEU   A CA  
942  C C   . LEU   A 115 ? 0.47861 0.66819 0.55688 -0.11730 0.06630  0.05981  112 LEU   A C   
943  O O   . LEU   A 115 ? 0.59412 0.79529 0.67748 -0.10903 0.06377  0.05585  112 LEU   A O   
944  C CB  . LEU   A 115 ? 0.49234 0.63037 0.54913 -0.11110 0.05133  0.07384  112 LEU   A CB  
945  C CG  . LEU   A 115 ? 0.52695 0.64543 0.58771 -0.10009 0.04104  0.07640  112 LEU   A CG  
946  C CD1 . LEU   A 115 ? 0.53851 0.62350 0.57123 -0.10096 0.03278  0.08510  112 LEU   A CD1 
947  C CD2 . LEU   A 115 ? 0.45869 0.59172 0.53915 -0.08613 0.03522  0.07156  112 LEU   A CD2 
948  N N   . GLN   A 116 ? 0.50751 0.70455 0.57872 -0.13180 0.07563  0.05872  113 GLN   A N   
949  C CA  . GLN   A 116 ? 0.47379 0.69829 0.54622 -0.13697 0.08404  0.05110  113 GLN   A CA  
950  C C   . GLN   A 116 ? 0.52511 0.77742 0.62401 -0.12674 0.08406  0.03953  113 GLN   A C   
951  O O   . GLN   A 116 ? 0.41760 0.68609 0.52061 -0.11926 0.08362  0.03272  113 GLN   A O   
952  C CB  . GLN   A 116 ? 0.54588 0.77540 0.60644 -0.15707 0.09503  0.05148  113 GLN   A CB  
953  C CG  . GLN   A 116 ? 0.49093 0.69172 0.51732 -0.16945 0.09572  0.06275  113 GLN   A CG  
954  C CD  . GLN   A 116 ? 0.70376 0.90733 0.71635 -0.19307 0.10747  0.06364  113 GLN   A CD  
955  O OE1 . GLN   A 116 ? 0.72427 0.92935 0.74704 -0.20057 0.10999  0.06204  113 GLN   A OE1 
956  N NE2 . GLN   A 116 ? 0.74070 0.94538 0.72894 -0.20633 0.11510  0.06578  113 GLN   A NE2 
957  N N   . GLY   A 117 ? 0.47199 0.72741 0.58657 -0.12578 0.08343  0.03690  114 GLY   A N   
958  C CA  . GLY   A 117 ? 0.49137 0.76690 0.62687 -0.11511 0.08098  0.02695  114 GLY   A CA  
959  C C   . GLY   A 117 ? 0.43890 0.70545 0.57787 -0.10058 0.07205  0.02780  114 GLY   A C   
960  O O   . GLY   A 117 ? 0.49065 0.77046 0.63787 -0.09161 0.06923  0.01995  114 GLY   A O   
961  N N   . LEU   A 118 ? 0.45079 0.69452 0.58311 -0.09826 0.06690  0.03652  115 LEU   A N   
962  C CA  . LEU   A 118 ? 0.48587 0.72334 0.62248 -0.08724 0.05918  0.03692  115 LEU   A CA  
963  C C   . LEU   A 118 ? 0.46591 0.70641 0.59368 -0.08391 0.05707  0.03567  115 LEU   A C   
964  O O   . LEU   A 118 ? 0.45377 0.69874 0.58683 -0.07594 0.05243  0.03085  115 LEU   A O   
965  C CB  . LEU   A 118 ? 0.42870 0.64673 0.56397 -0.08539 0.05452  0.04419  115 LEU   A CB  
966  C CG  . LEU   A 118 ? 0.56372 0.77970 0.70798 -0.07665 0.04810  0.04323  115 LEU   A CG  
967  C CD1 . LEU   A 118 ? 0.47724 0.70139 0.63279 -0.07419 0.04870  0.03764  115 LEU   A CD1 
968  C CD2 . LEU   A 118 ? 0.54420 0.74684 0.68964 -0.07424 0.04409  0.04801  115 LEU   A CD2 
969  N N   . ALA   A 119 ? 0.41822 0.65348 0.52956 -0.09057 0.05989  0.04007  116 ALA   A N   
970  C CA  . ALA   A 119 ? 0.56118 0.79995 0.66140 -0.08813 0.05852  0.03810  116 ALA   A CA  
971  C C   . ALA   A 119 ? 0.47737 0.73985 0.58451 -0.08532 0.06261  0.02663  116 ALA   A C   
972  O O   . ALA   A 119 ? 0.42781 0.69358 0.53267 -0.07781 0.05837  0.02173  116 ALA   A O   
973  C CB  . ALA   A 119 ? 0.48604 0.71351 0.56295 -0.09777 0.06176  0.04510  116 ALA   A CB  
974  N N   . PHE   A 120 ? 0.48850 0.76797 0.60458 -0.09044 0.06980  0.02103  117 PHE   A N   
975  C CA  . PHE   A 120 ? 0.47439 0.77934 0.60050 -0.08501 0.07210  0.00770  117 PHE   A CA  
976  C C   . PHE   A 120 ? 0.44079 0.74240 0.57871 -0.07119 0.06246  0.00269  117 PHE   A C   
977  O O   . PHE   A 120 ? 0.49452 0.80366 0.63290 -0.06174 0.05848  -0.00618 117 PHE   A O   
978  C CB  . PHE   A 120 ? 0.52214 0.84843 0.65771 -0.09398 0.08098  0.00198  117 PHE   A CB  
979  C CG  . PHE   A 120 ? 0.44343 0.80133 0.59126 -0.08769 0.08338  -0.01409 117 PHE   A CG  
980  C CD1 . PHE   A 120 ? 0.53586 0.91448 0.67672 -0.09203 0.09142  -0.02140 117 PHE   A CD1 
981  C CD2 . PHE   A 120 ? 0.45469 0.82177 0.61994 -0.07687 0.07712  -0.02280 117 PHE   A CD2 
982  C CE1 . PHE   A 120 ? 0.50826 0.91977 0.66276 -0.08435 0.09338  -0.03873 117 PHE   A CE1 
983  C CE2 . PHE   A 120 ? 0.50271 0.89894 0.67995 -0.06831 0.07712  -0.03924 117 PHE   A CE2 
984  C CZ  . PHE   A 120 ? 0.43769 0.85804 0.61134 -0.07144 0.08539  -0.04804 117 PHE   A CZ  
985  N N   . CYS   A 121 ? 0.39672 0.68494 0.54176 -0.07029 0.05842  0.00807  118 CYS   A N   
986  C CA  . CYS   A 121 ? 0.38049 0.66072 0.53172 -0.06013 0.04961  0.00513  118 CYS   A CA  
987  C C   . CYS   A 121 ? 0.49930 0.76598 0.64227 -0.05496 0.04273  0.00720  118 CYS   A C   
988  O O   . CYS   A 121 ? 0.44982 0.71441 0.59206 -0.04644 0.03606  0.00059  118 CYS   A O   
989  C CB  . CYS   A 121 ? 0.49827 0.76639 0.65543 -0.06260 0.04833  0.01129  118 CYS   A CB  
990  S SG  . CYS   A 121 ? 0.50348 0.78508 0.67088 -0.06752 0.05361  0.00741  118 CYS   A SG  
991  N N   . HIS   A 122 ? 0.40675 0.66258 0.54259 -0.05973 0.04291  0.01584  119 HIS   A N   
992  C CA  . HIS   A 122 ? 0.47145 0.71570 0.60154 -0.05586 0.03552  0.01758  119 HIS   A CA  
993  C C   . HIS   A 122 ? 0.36973 0.62035 0.49003 -0.05175 0.03429  0.01082  119 HIS   A C   
994  O O   . HIS   A 122 ? 0.47084 0.71415 0.58806 -0.04590 0.02672  0.00717  119 HIS   A O   
995  C CB  . HIS   A 122 ? 0.38030 0.61367 0.50708 -0.06027 0.03447  0.02703  119 HIS   A CB  
996  C CG  . HIS   A 122 ? 0.42744 0.65462 0.56456 -0.06206 0.03437  0.03160  119 HIS   A CG  
997  N ND1 . HIS   A 122 ? 0.51572 0.73480 0.65297 -0.06386 0.03292  0.03816  119 HIS   A ND1 
998  C CD2 . HIS   A 122 ? 0.51327 0.74099 0.65968 -0.06151 0.03505  0.02962  119 HIS   A CD2 
999  C CE1 . HIS   A 122 ? 0.58254 0.79987 0.73033 -0.06435 0.03383  0.03914  119 HIS   A CE1 
1000 N NE2 . HIS   A 122 ? 0.43313 0.65503 0.58548 -0.06382 0.03552  0.03462  119 HIS   A NE2 
1001 N N   . SER   A 123 ? 0.43244 0.69628 0.54636 -0.05574 0.04197  0.00853  120 SER   A N   
1002 C CA  . SER   A 123 ? 0.46285 0.73635 0.56729 -0.05159 0.04234  0.00003  120 SER   A CA  
1003 C C   . SER   A 123 ? 0.51976 0.80318 0.63230 -0.04096 0.03869  -0.01287 120 SER   A C   
1004 O O   . SER   A 123 ? 0.52848 0.81246 0.63402 -0.03324 0.03408  -0.02099 120 SER   A O   
1005 C CB  . SER   A 123 ? 0.45810 0.74601 0.55307 -0.06065 0.05342  -0.00021 120 SER   A CB  
1006 O OG  . SER   A 123 ? 0.58602 0.89393 0.69288 -0.06388 0.06124  -0.00618 120 SER   A OG  
1007 N N   . HIS   A 124 ? 0.42806 0.71745 0.55372 -0.03938 0.03931  -0.01551 121 HIS   A N   
1008 C CA  . HIS   A 124 ? 0.41344 0.70633 0.54537 -0.02736 0.03239  -0.02697 121 HIS   A CA  
1009 C C   . HIS   A 124 ? 0.48531 0.75177 0.61467 -0.02289 0.02111  -0.02287 121 HIS   A C   
1010 O O   . HIS   A 124 ? 0.47967 0.74093 0.61072 -0.01378 0.01352  -0.02990 121 HIS   A O   
1011 C CB  . HIS   A 124 ? 0.49510 0.80737 0.64098 -0.02752 0.03703  -0.03271 121 HIS   A CB  
1012 C CG  . HIS   A 124 ? 0.48140 0.82551 0.63169 -0.02973 0.04687  -0.04290 121 HIS   A CG  
1013 N ND1 . HIS   A 124 ? 0.62227 0.97477 0.76519 -0.04299 0.05811  -0.03728 121 HIS   A ND1 
1014 C CD2 . HIS   A 124 ? 0.56774 0.93832 0.72845 -0.02090 0.04718  -0.05920 121 HIS   A CD2 
1015 C CE1 . HIS   A 124 ? 0.55742 0.94127 0.70556 -0.04462 0.06671  -0.04923 121 HIS   A CE1 
1016 N NE2 . HIS   A 124 ? 0.66404 1.06221 0.82537 -0.03060 0.06040  -0.06360 121 HIS   A NE2 
1017 N N   . ARG   A 125 ? 0.39527 0.64506 0.51974 -0.02956 0.01952  -0.01214 122 ARG   A N   
1018 C CA  . ARG   A 125 ? 0.50780 0.73477 0.62913 -0.02906 0.01055  -0.00826 122 ARG   A CA  
1019 C C   . ARG   A 125 ? 0.67706 0.89758 0.80434 -0.02959 0.00938  -0.00637 122 ARG   A C   
1020 O O   . ARG   A 125 ? 0.54674 0.75113 0.66803 -0.02479 0.00087  -0.00940 122 ARG   A O   
1021 C CB  . ARG   A 125 ? 0.51538 0.73059 0.62596 -0.02043 0.00059  -0.01646 122 ARG   A CB  
1022 C CG  . ARG   A 125 ? 0.57635 0.79271 0.67848 -0.02120 0.00008  -0.01702 122 ARG   A CG  
1023 C CD  . ARG   A 125 ? 0.68537 0.89834 0.77729 -0.01006 -0.00729 -0.02942 122 ARG   A CD  
1024 N NE  . ARG   A 125 ? 0.68573 0.87306 0.77035 -0.00566 -0.01946 -0.03185 122 ARG   A NE  
1025 C CZ  . ARG   A 125 ? 0.89440 1.07517 0.97720 0.00444  -0.02585 -0.03990 122 ARG   A CZ  
1026 N NH1 . ARG   A 125 ? 0.81085 1.01390 0.90278 0.01208  -0.02116 -0.04792 122 ARG   A NH1 
1027 N NH2 . ARG   A 125 ? 0.90929 1.05975 0.97986 0.00652  -0.03799 -0.04031 122 ARG   A NH2 
1028 N N   . VAL   A 126 ? 0.46647 0.69662 0.60267 -0.03589 0.01731  -0.00111 123 VAL   A N   
1029 C CA  . VAL   A 126 ? 0.43171 0.65701 0.57275 -0.03727 0.01718  0.00087  123 VAL   A CA  
1030 C C   . VAL   A 126 ? 0.42589 0.64799 0.57180 -0.04671 0.02274  0.01082  123 VAL   A C   
1031 O O   . VAL   A 126 ? 0.47097 0.70209 0.62023 -0.05119 0.02910  0.01447  123 VAL   A O   
1032 C CB  . VAL   A 126 ? 0.41576 0.65916 0.56453 -0.03357 0.02043  -0.00631 123 VAL   A CB  
1033 C CG1 . VAL   A 126 ? 0.46124 0.69900 0.61387 -0.03603 0.02031  -0.00340 123 VAL   A CG1 
1034 C CG2 . VAL   A 126 ? 0.55258 0.80094 0.69871 -0.02122 0.01322  -0.01878 123 VAL   A CG2 
1035 N N   . LEU   A 127 ? 0.44557 0.65378 0.59007 -0.04974 0.02005  0.01463  124 LEU   A N   
1036 C CA  . LEU   A 127 ? 0.40850 0.61604 0.55926 -0.05688 0.02521  0.02139  124 LEU   A CA  
1037 C C   . LEU   A 127 ? 0.49235 0.70128 0.64611 -0.05748 0.02808  0.02079  124 LEU   A C   
1038 O O   . LEU   A 127 ? 0.47656 0.67837 0.62455 -0.05390 0.02329  0.01712  124 LEU   A O   
1039 C CB  . LEU   A 127 ? 0.41681 0.61261 0.56499 -0.06177 0.02230  0.02457  124 LEU   A CB  
1040 C CG  . LEU   A 127 ? 0.56000 0.75205 0.70426 -0.06191 0.01720  0.02401  124 LEU   A CG  
1041 C CD1 . LEU   A 127 ? 0.53136 0.71427 0.67445 -0.06976 0.01529  0.02623  124 LEU   A CD1 
1042 C CD2 . LEU   A 127 ? 0.50060 0.70380 0.65037 -0.06125 0.01963  0.02602  124 LEU   A CD2 
1043 N N   . HIS   A 128 ? 0.38851 0.60407 0.54937 -0.06148 0.03450  0.02412  125 HIS   A N   
1044 C CA  . HIS   A 128 ? 0.41903 0.63535 0.58243 -0.06279 0.03699  0.02323  125 HIS   A CA  
1045 C C   . HIS   A 128 ? 0.36767 0.57293 0.52829 -0.06614 0.03693  0.02587  125 HIS   A C   
1046 O O   . HIS   A 128 ? 0.46685 0.66485 0.62110 -0.06531 0.03416  0.02387  125 HIS   A O   
1047 C CB  . HIS   A 128 ? 0.39432 0.61845 0.56370 -0.06663 0.04327  0.02528  125 HIS   A CB  
1048 C CG  . HIS   A 128 ? 0.41262 0.63852 0.58469 -0.06842 0.04533  0.02318  125 HIS   A CG  
1049 N ND1 . HIS   A 128 ? 0.41845 0.63623 0.59028 -0.07048 0.04655  0.02508  125 HIS   A ND1 
1050 C CD2 . HIS   A 128 ? 0.41796 0.65456 0.59337 -0.06878 0.04626  0.01822  125 HIS   A CD2 
1051 C CE1 . HIS   A 128 ? 0.39931 0.61989 0.57250 -0.07162 0.04737  0.02201  125 HIS   A CE1 
1052 N NE2 . HIS   A 128 ? 0.44177 0.67447 0.61820 -0.07088 0.04695  0.01774  125 HIS   A NE2 
1053 N N   . ARG   A 129 ? 0.39456 0.59941 0.55932 -0.06991 0.03980  0.02960  126 ARG   A N   
1054 C CA  . ARG   A 129 ? 0.42541 0.62479 0.58905 -0.07481 0.04152  0.03093  126 ARG   A CA  
1055 C C   . ARG   A 129 ? 0.45749 0.65602 0.62148 -0.07678 0.04595  0.03041  126 ARG   A C   
1056 O O   . ARG   A 129 ? 0.47919 0.67293 0.63867 -0.08162 0.04811  0.03053  126 ARG   A O   
1057 C CB  . ARG   A 129 ? 0.40066 0.58740 0.55203 -0.07713 0.03645  0.03047  126 ARG   A CB  
1058 C CG  . ARG   A 129 ? 0.41607 0.60084 0.56512 -0.07537 0.03104  0.02999  126 ARG   A CG  
1059 C CD  . ARG   A 129 ? 0.48496 0.65258 0.61984 -0.08030 0.02594  0.03022  126 ARG   A CD  
1060 N NE  . ARG   A 129 ? 0.48917 0.64091 0.60900 -0.07746 0.02092  0.02884  126 ARG   A NE  
1061 C CZ  . ARG   A 129 ? 0.75746 0.88663 0.85839 -0.08127 0.01464  0.02959  126 ARG   A CZ  
1062 N NH1 . ARG   A 129 ? 0.49784 0.61890 0.59340 -0.09024 0.01384  0.03163  126 ARG   A NH1 
1063 N NH2 . ARG   A 129 ? 0.57931 0.69223 0.66504 -0.07639 0.00807  0.02805  126 ARG   A NH2 
1064 N N   . ASP   A 130 ? 0.43044 0.63318 0.59826 -0.07452 0.04773  0.02951  127 ASP   A N   
1065 C CA  . ASP   A 130 ? 0.44634 0.64745 0.61429 -0.07628 0.05143  0.02836  127 ASP   A CA  
1066 C C   . ASP   A 130 ? 0.46796 0.67321 0.64213 -0.07553 0.05368  0.02835  127 ASP   A C   
1067 O O   . ASP   A 130 ? 0.44180 0.64663 0.61480 -0.07643 0.05418  0.02613  127 ASP   A O   
1068 C CB  . ASP   A 130 ? 0.33863 0.53248 0.49611 -0.07616 0.04819  0.02601  127 ASP   A CB  
1069 C CG  . ASP   A 130 ? 0.75704 0.94613 0.91006 -0.07941 0.05192  0.02502  127 ASP   A CG  
1070 O OD1 . ASP   A 130 ? 0.50006 0.69234 0.65822 -0.08187 0.05749  0.02541  127 ASP   A OD1 
1071 O OD2 . ASP   A 130 ? 0.73156 0.91470 0.87594 -0.07869 0.04878  0.02279  127 ASP   A OD2 
1072 N N   . LEU   A 131 ? 0.39970 0.60697 0.57864 -0.07460 0.05419  0.03089  128 LEU   A N   
1073 C CA  . LEU   A 131 ? 0.50393 0.70898 0.68371 -0.07550 0.05556  0.03221  128 LEU   A CA  
1074 C C   . LEU   A 131 ? 0.52853 0.72763 0.71038 -0.07486 0.05767  0.03099  128 LEU   A C   
1075 O O   . LEU   A 131 ? 0.61334 0.81245 0.79977 -0.07143 0.05748  0.03080  128 LEU   A O   
1076 C CB  . LEU   A 131 ? 0.39516 0.59958 0.57411 -0.07430 0.05368  0.03587  128 LEU   A CB  
1077 C CG  . LEU   A 131 ? 0.51952 0.73024 0.69494 -0.07493 0.05236  0.03602  128 LEU   A CG  
1078 C CD1 . LEU   A 131 ? 0.53972 0.74749 0.71110 -0.07401 0.05028  0.03991  128 LEU   A CD1 
1079 C CD2 . LEU   A 131 ? 0.39858 0.61490 0.57238 -0.07902 0.05486  0.03350  128 LEU   A CD2 
1080 N N   . LYS   A 132 ? 0.51012 0.70572 0.68947 -0.07749 0.05915  0.02875  129 LYS   A N   
1081 C CA  . LYS   A 132 ? 0.54190 0.72986 0.72123 -0.07659 0.06071  0.02641  129 LYS   A CA  
1082 C C   . LYS   A 132 ? 0.39390 0.57501 0.56889 -0.08156 0.06060  0.02615  129 LYS   A C   
1083 O O   . LYS   A 132 ? 0.44467 0.63238 0.61899 -0.08612 0.06044  0.02606  129 LYS   A O   
1084 C CB  . LYS   A 132 ? 0.47750 0.66787 0.65601 -0.07622 0.06314  0.02228  129 LYS   A CB  
1085 C CG  . LYS   A 132 ? 0.41121 0.60342 0.58382 -0.07919 0.06189  0.02098  129 LYS   A CG  
1086 C CD  . LYS   A 132 ? 0.50384 0.69397 0.67004 -0.07990 0.06397  0.01821  129 LYS   A CD  
1087 C CE  . LYS   A 132 ? 0.63381 0.82113 0.79039 -0.08122 0.05994  0.01716  129 LYS   A CE  
1088 N NZ  . LYS   A 132 ? 0.76188 0.94252 0.90628 -0.08342 0.06166  0.01544  129 LYS   A NZ  
1089 N N   . PRO   A 133 ? 0.43684 0.60527 0.60904 -0.08105 0.06035  0.02503  130 PRO   A N   
1090 C CA  . PRO   A 133 ? 0.41914 0.57830 0.58537 -0.08845 0.06002  0.02501  130 PRO   A CA  
1091 C C   . PRO   A 133 ? 0.40813 0.57669 0.57574 -0.09357 0.06094  0.02067  130 PRO   A C   
1092 O O   . PRO   A 133 ? 0.47749 0.64824 0.64400 -0.10186 0.06119  0.02027  130 PRO   A O   
1093 C CB  . PRO   A 133 ? 0.39900 0.54005 0.56079 -0.08467 0.05829  0.02289  130 PRO   A CB  
1094 C CG  . PRO   A 133 ? 0.65075 0.79300 0.81733 -0.07472 0.05685  0.02323  130 PRO   A CG  
1095 C CD  . PRO   A 133 ? 0.48695 0.64886 0.66132 -0.07360 0.05968  0.02281  130 PRO   A CD  
1096 N N   . GLN   A 134 ? 0.42291 0.59743 0.59196 -0.08950 0.06112  0.01699  131 GLN   A N   
1097 C CA  . GLN   A 134 ? 0.40003 0.58176 0.56851 -0.09236 0.05950  0.01251  131 GLN   A CA  
1098 C C   . GLN   A 134 ? 0.44803 0.64477 0.62110 -0.09360 0.05771  0.01245  131 GLN   A C   
1099 O O   . GLN   A 134 ? 0.48743 0.69308 0.66278 -0.09616 0.05516  0.00749  131 GLN   A O   
1100 C CB  . GLN   A 134 ? 0.51302 0.69330 0.67657 -0.08796 0.05932  0.00963  131 GLN   A CB  
1101 C CG  . GLN   A 134 ? 0.60058 0.77014 0.76000 -0.08619 0.06188  0.00676  131 GLN   A CG  
1102 C CD  . GLN   A 134 ? 0.72510 0.89492 0.88760 -0.08106 0.06530  0.00829  131 GLN   A CD  
1103 O OE1 . GLN   A 134 ? 0.46459 0.63568 0.63274 -0.07935 0.06490  0.01220  131 GLN   A OE1 
1104 N NE2 . GLN   A 134 ? 0.83838 1.00860 0.99697 -0.07901 0.06870  0.00442  131 GLN   A NE2 
1105 N N   . ASN   A 135 ? 0.38842 0.58944 0.56355 -0.09098 0.05830  0.01646  132 ASN   A N   
1106 C CA  . ASN   A 135 ? 0.47006 0.68542 0.64911 -0.09036 0.05654  0.01505  132 ASN   A CA  
1107 C C   . ASN   A 135 ? 0.46384 0.68549 0.64525 -0.09683 0.05962  0.01679  132 ASN   A C   
1108 O O   . ASN   A 135 ? 0.40500 0.64039 0.58981 -0.09601 0.05943  0.01505  132 ASN   A O   
1109 C CB  . ASN   A 135 ? 0.47732 0.69223 0.65447 -0.08381 0.05465  0.01741  132 ASN   A CB  
1110 C CG  . ASN   A 135 ? 0.50483 0.71396 0.67572 -0.07999 0.05133  0.01541  132 ASN   A CG  
1111 O OD1 . ASN   A 135 ? 0.58535 0.79454 0.75378 -0.08012 0.04855  0.01106  132 ASN   A OD1 
1112 N ND2 . ASN   A 135 ? 0.41497 0.61826 0.58156 -0.07769 0.05126  0.01851  132 ASN   A ND2 
1113 N N   . LEU   A 136 ? 0.48202 0.69212 0.65931 -0.10347 0.06222  0.01987  133 LEU   A N   
1114 C CA  . LEU   A 136 ? 0.42207 0.63317 0.59603 -0.11289 0.06557  0.02257  133 LEU   A CA  
1115 C C   . LEU   A 136 ? 0.52984 0.74330 0.70455 -0.12407 0.06724  0.01846  133 LEU   A C   
1116 O O   . LEU   A 136 ? 0.52698 0.72355 0.69670 -0.12624 0.06605  0.01884  133 LEU   A O   
1117 C CB  . LEU   A 136 ? 0.44118 0.63112 0.60494 -0.11253 0.06537  0.03029  133 LEU   A CB  
1118 C CG  . LEU   A 136 ? 0.51309 0.70098 0.67803 -0.10161 0.06282  0.03327  133 LEU   A CG  
1119 C CD1 . LEU   A 136 ? 0.57899 0.74770 0.73444 -0.10033 0.06067  0.03953  133 LEU   A CD1 
1120 C CD2 . LEU   A 136 ? 0.43974 0.64502 0.60884 -0.09925 0.06313  0.03204  133 LEU   A CD2 
1121 N N   . LEU   A 137 ? 0.40034 0.63617 0.58200 -0.13115 0.06987  0.01328  134 LEU   A N   
1122 C CA  . LEU   A 137 ? 0.45611 0.70175 0.64249 -0.14290 0.07137  0.00708  134 LEU   A CA  
1123 C C   . LEU   A 137 ? 0.50183 0.74602 0.68061 -0.16008 0.07792  0.01037  134 LEU   A C   
1124 O O   . LEU   A 137 ? 0.52761 0.77748 0.70236 -0.16198 0.08181  0.01374  134 LEU   A O   
1125 C CB  . LEU   A 137 ? 0.36913 0.64592 0.57129 -0.13857 0.06894  -0.00388 134 LEU   A CB  
1126 C CG  . LEU   A 137 ? 0.39113 0.66598 0.59557 -0.12231 0.06148  -0.00635 134 LEU   A CG  
1127 C CD1 . LEU   A 137 ? 0.44133 0.74367 0.65879 -0.11649 0.05652  -0.01770 134 LEU   A CD1 
1128 C CD2 . LEU   A 137 ? 0.49072 0.74452 0.68823 -0.12103 0.05843  -0.00485 134 LEU   A CD2 
1129 N N   . ILE   A 138 ? 0.44344 0.67809 0.61774 -0.17376 0.07905  0.00943  135 ILE   A N   
1130 C CA  . ILE   A 138 ? 0.46141 0.68891 0.62371 -0.19388 0.08527  0.01334  135 ILE   A CA  
1131 C C   . ILE   A 138 ? 0.60843 0.86131 0.78262 -0.20971 0.08874  0.00336  135 ILE   A C   
1132 O O   . ILE   A 138 ? 0.52296 0.78569 0.70950 -0.20517 0.08392  -0.00469 135 ILE   A O   
1133 C CB  . ILE   A 138 ? 0.51838 0.70124 0.65818 -0.19816 0.08233  0.02300  135 ILE   A CB  
1134 C CG1 . ILE   A 138 ? 0.68966 0.85929 0.83113 -0.19737 0.07720  0.01851  135 ILE   A CG1 
1135 C CG2 . ILE   A 138 ? 0.49514 0.65771 0.62639 -0.18168 0.07808  0.03093  135 ILE   A CG2 
1136 C CD1 . ILE   A 138 ? 0.73067 0.85560 0.85003 -0.20044 0.07303  0.02562  135 ILE   A CD1 
1137 N N   . ASN   A 139 ? 0.57688 0.84139 0.74665 -0.22928 0.09720  0.00340  136 ASN   A N   
1138 C CA  . ASN   A 139 ? 0.58654 0.87684 0.76735 -0.24883 0.10202  -0.00637 136 ASN   A CA  
1139 C C   . ASN   A 139 ? 0.62930 0.88625 0.78667 -0.27268 0.10522  0.00131  136 ASN   A C   
1140 O O   . ASN   A 139 ? 0.60037 0.81256 0.73323 -0.27052 0.10168  0.01349  136 ASN   A O   
1141 C CB  . ASN   A 139 ? 0.59698 0.93439 0.79389 -0.25458 0.11047  -0.01557 136 ASN   A CB  
1142 C CG  . ASN   A 139 ? 0.54901 0.87742 0.72624 -0.26550 0.11939  -0.00647 136 ASN   A CG  
1143 O OD1 . ASN   A 139 ? 0.67489 0.96033 0.82468 -0.27224 0.11893  0.00707  136 ASN   A OD1 
1144 N ND2 . ASN   A 139 ? 0.60212 0.96786 0.79081 -0.26430 0.12575  -0.01458 136 ASN   A ND2 
1145 N N   . THR   A 140 ? 0.56050 0.83892 0.72496 -0.29567 0.11110  -0.00657 137 THR   A N   
1146 C CA  . THR   A 140 ? 0.66432 0.91101 0.80493 -0.32241 0.11434  -0.00009 137 THR   A CA  
1147 C C   . THR   A 140 ? 0.75636 0.99659 0.87541 -0.33880 0.12375  0.00720  137 THR   A C   
1148 O O   . THR   A 140 ? 0.79324 1.01092 0.89135 -0.35996 0.12637  0.01078  137 THR   A O   
1149 C CB  . THR   A 140 ? 0.59117 0.85802 0.74664 -0.33597 0.11369  -0.01232 137 THR   A CB  
1150 O OG1 . THR   A 140 ? 0.71102 1.02697 0.88756 -0.33385 0.11854  -0.02469 137 THR   A OG1 
1151 C CG2 . THR   A 140 ? 0.56609 0.83364 0.73754 -0.31912 0.10301  -0.01912 137 THR   A CG2 
1152 N N   . GLU   A 141 ? 0.75454 1.01079 0.87541 -0.32759 0.12771  0.00928  138 GLU   A N   
1153 C CA  . GLU   A 141 ? 0.77037 1.02035 0.86867 -0.33955 0.13584  0.01545  138 GLU   A CA  
1154 C C   . GLU   A 141 ? 0.69941 0.91646 0.77382 -0.33422 0.13458  0.03039  138 GLU   A C   
1155 O O   . GLU   A 141 ? 0.68586 0.90467 0.74509 -0.33815 0.14064  0.03444  138 GLU   A O   
1156 C CB  . GLU   A 141 ? 0.70152 1.00499 0.82220 -0.33370 0.14258  0.00174  138 GLU   A CB  
1157 C CG  . GLU   A 141 ? 0.75798 1.09697 0.90231 -0.33925 0.14332  -0.01401 138 GLU   A CG  
1158 C CD  . GLU   A 141 ? 0.99112 1.38239 1.15711 -0.33224 0.14900  -0.02881 138 GLU   A CD  
1159 O OE1 . GLU   A 141 ? 0.71588 1.11649 0.88074 -0.32070 0.15165  -0.02753 138 GLU   A OE1 
1160 O OE2 . GLU   A 141 ? 0.88208 1.30524 1.06605 -0.33828 0.15040  -0.04252 138 GLU   A OE2 
1161 N N   . GLY   A 142 ? 0.67607 0.85853 0.74511 -0.31630 0.12312  0.03718  139 GLY   A N   
1162 C CA  . GLY   A 142 ? 0.66166 0.80610 0.70717 -0.30229 0.11667  0.04996  139 GLY   A CA  
1163 C C   . GLY   A 142 ? 0.61561 0.78412 0.67788 -0.27770 0.11492  0.04751  139 GLY   A C   
1164 O O   . GLY   A 142 ? 0.66124 0.80362 0.70571 -0.26698 0.10994  0.05702  139 GLY   A O   
1165 N N   . ALA   A 143 ? 0.54801 0.76341 0.64269 -0.26814 0.11748  0.03471  140 ALA   A N   
1166 C CA  . ALA   A 143 ? 0.60444 0.84181 0.71399 -0.24614 0.11539  0.03139  140 ALA   A CA  
1167 C C   . ALA   A 143 ? 0.52369 0.75215 0.64671 -0.22202 0.10451  0.03030  140 ALA   A C   
1168 O O   . ALA   A 143 ? 0.52114 0.74431 0.65188 -0.22139 0.10044  0.02675  140 ALA   A O   
1169 C CB  . ALA   A 143 ? 0.59069 0.88238 0.72506 -0.24847 0.12326  0.01714  140 ALA   A CB  
1170 N N   . ILE   A 144 ? 0.44671 0.67357 0.57115 -0.20345 0.10019  0.03307  141 ILE   A N   
1171 C CA  . ILE   A 144 ? 0.39507 0.61880 0.53238 -0.18214 0.09172  0.03132  141 ILE   A CA  
1172 C C   . ILE   A 144 ? 0.56280 0.81321 0.71360 -0.16848 0.09144  0.02594  141 ILE   A C   
1173 O O   . ILE   A 144 ? 0.48897 0.74605 0.63251 -0.17066 0.09527  0.02779  141 ILE   A O   
1174 C CB  . ILE   A 144 ? 0.42359 0.60810 0.54518 -0.17340 0.08453  0.04134  141 ILE   A CB  
1175 C CG1 . ILE   A 144 ? 0.47110 0.65595 0.60661 -0.15484 0.07795  0.03815  141 ILE   A CG1 
1176 C CG2 . ILE   A 144 ? 0.52045 0.69289 0.62608 -0.17114 0.08403  0.04931  141 ILE   A CG2 
1177 C CD1 . ILE   A 144 ? 0.48746 0.64031 0.61243 -0.14583 0.07135  0.04453  141 ILE   A CD1 
1178 N N   . LYS   A 145 ? 0.49361 0.75702 0.66132 -0.15482 0.08639  0.01907  142 LYS   A N   
1179 C CA  . LYS   A 145 ? 0.41090 0.69802 0.59043 -0.14251 0.08472  0.01230  142 LYS   A CA  
1180 C C   . LYS   A 145 ? 0.49799 0.77410 0.68138 -0.12575 0.07660  0.01324  142 LYS   A C   
1181 O O   . LYS   A 145 ? 0.45655 0.71968 0.64071 -0.12362 0.07319  0.01412  142 LYS   A O   
1182 C CB  . LYS   A 145 ? 0.38866 0.71155 0.58556 -0.14538 0.08699  -0.00105 142 LYS   A CB  
1183 C CG  . LYS   A 145 ? 0.44497 0.78444 0.64058 -0.16560 0.09682  -0.00395 142 LYS   A CG  
1184 C CD  . LYS   A 145 ? 0.39583 0.77908 0.61285 -0.16636 0.09917  -0.01994 142 LYS   A CD  
1185 C CE  . LYS   A 145 ? 0.39599 0.79905 0.61199 -0.18988 0.11104  -0.02336 142 LYS   A CE  
1186 N NZ  . LYS   A 145 ? 0.53320 0.98671 0.77223 -0.18978 0.11486  -0.04110 142 LYS   A NZ  
1187 N N   . LEU   A 146 ? 0.38160 0.66271 0.56587 -0.11506 0.07390  0.01260  143 LEU   A N   
1188 C CA  . LEU   A 146 ? 0.37473 0.64691 0.56109 -0.10169 0.06686  0.01296  143 LEU   A CA  
1189 C C   . LEU   A 146 ? 0.35495 0.64182 0.55150 -0.09505 0.06213  0.00336  143 LEU   A C   
1190 O O   . LEU   A 146 ? 0.40521 0.71544 0.61002 -0.09421 0.06247  -0.00562 143 LEU   A O   
1191 C CB  . LEU   A 146 ? 0.48816 0.75812 0.67002 -0.09420 0.06472  0.01537  143 LEU   A CB  
1192 C CG  . LEU   A 146 ? 0.55675 0.81316 0.72734 -0.09810 0.06695  0.02396  143 LEU   A CG  
1193 C CD1 . LEU   A 146 ? 0.47463 0.73204 0.64260 -0.08991 0.06344  0.02398  143 LEU   A CD1 
1194 C CD2 . LEU   A 146 ? 0.58109 0.81519 0.74716 -0.09835 0.06513  0.03116  143 LEU   A CD2 
1195 N N   . ALA   A 147 ? 0.41861 0.69204 0.61365 -0.08972 0.05723  0.00448  144 ALA   A N   
1196 C CA  . ALA   A 147 ? 0.36540 0.64622 0.56520 -0.08301 0.05068  -0.00348 144 ALA   A CA  
1197 C C   . ALA   A 147 ? 0.50204 0.76426 0.69297 -0.07431 0.04460  -0.00015 144 ALA   A C   
1198 O O   . ALA   A 147 ? 0.45888 0.70627 0.64352 -0.07495 0.04672  0.00739  144 ALA   A O   
1199 C CB  . ALA   A 147 ? 0.55357 0.83686 0.75732 -0.08979 0.05131  -0.00672 144 ALA   A CB  
1200 N N   . ASP   A 148 ? 0.50696 0.77025 0.69663 -0.06667 0.03649  -0.00643 145 ASP   A N   
1201 C CA  . ASP   A 148 ? 0.52787 0.77097 0.70455 -0.06035 0.02996  -0.00367 145 ASP   A CA  
1202 C C   . ASP   A 148 ? 0.45644 0.69136 0.62725 -0.05691 0.02901  0.00035  145 ASP   A C   
1203 O O   . ASP   A 148 ? 0.51562 0.74035 0.68291 -0.06143 0.03383  0.00778  145 ASP   A O   
1204 C CB  . ASP   A 148 ? 0.44748 0.67448 0.61688 -0.06597 0.03357  0.00224  145 ASP   A CB  
1205 C CG  . ASP   A 148 ? 0.75852 0.96670 0.91204 -0.06214 0.02718  0.00331  145 ASP   A CG  
1206 O OD1 . ASP   A 148 ? 0.68426 0.88717 0.83043 -0.05487 0.01866  0.00069  145 ASP   A OD1 
1207 O OD2 . ASP   A 148 ? 0.68656 0.88368 0.83286 -0.06657 0.03045  0.00643  145 ASP   A OD2 
1208 N N   . PHE   A 149 ? 0.48052 0.72061 0.65086 -0.04819 0.02194  -0.00584 146 PHE   A N   
1209 C CA  . PHE   A 149 ? 0.51070 0.74064 0.67345 -0.04419 0.01892  -0.00353 146 PHE   A CA  
1210 C C   . PHE   A 149 ? 0.49075 0.69612 0.63595 -0.03870 0.00869  -0.00283 146 PHE   A C   
1211 O O   . PHE   A 149 ? 0.51617 0.71192 0.65333 -0.03278 0.00215  -0.00432 146 PHE   A O   
1212 C CB  . PHE   A 149 ? 0.42772 0.67696 0.59872 -0.03796 0.01773  -0.01154 146 PHE   A CB  
1213 C CG  . PHE   A 149 ? 0.53075 0.79578 0.71069 -0.04596 0.02842  -0.00890 146 PHE   A CG  
1214 C CD1 . PHE   A 149 ? 0.46092 0.74125 0.65044 -0.05416 0.03585  -0.00959 146 PHE   A CD1 
1215 C CD2 . PHE   A 149 ? 0.42836 0.69011 0.60426 -0.04608 0.03017  -0.00557 146 PHE   A CD2 
1216 C CE1 . PHE   A 149 ? 0.41279 0.70182 0.60491 -0.06284 0.04482  -0.00604 146 PHE   A CE1 
1217 C CE2 . PHE   A 149 ? 0.40762 0.67993 0.58705 -0.05340 0.03873  -0.00248 146 PHE   A CE2 
1218 C CZ  . PHE   A 149 ? 0.41228 0.69677 0.59845 -0.06203 0.04606  -0.00226 146 PHE   A CZ  
1219 N N   . GLY   A 150 ? 0.48095 0.67334 0.61715 -0.04129 0.00688  -0.00052 147 GLY   A N   
1220 C CA  . GLY   A 150 ? 0.49293 0.65756 0.60693 -0.03852 -0.00262 0.00141  147 GLY   A CA  
1221 C C   . GLY   A 150 ? 0.61048 0.75720 0.71305 -0.04623 0.00065  0.00960  147 GLY   A C   
1222 O O   . GLY   A 150 ? 0.67683 0.79965 0.75997 -0.04440 -0.00801 0.01080  147 GLY   A O   
1223 N N   . LEU   A 151 ? 0.47302 0.63014 0.58673 -0.05504 0.01216  0.01470  148 LEU   A N   
1224 C CA  . LEU   A 151 ? 0.51731 0.66476 0.62563 -0.06282 0.01587  0.02070  148 LEU   A CA  
1225 C C   . LEU   A 151 ? 0.43126 0.58736 0.54824 -0.06032 0.01574  0.02003  148 LEU   A C   
1226 O O   . LEU   A 151 ? 0.49094 0.64335 0.60718 -0.06668 0.01853  0.02400  148 LEU   A O   
1227 C CB  . LEU   A 151 ? 0.56186 0.71654 0.67763 -0.07200 0.02689  0.02483  148 LEU   A CB  
1228 C CG  . LEU   A 151 ? 0.68069 0.82482 0.78435 -0.07651 0.02842  0.02571  148 LEU   A CG  
1229 C CD1 . LEU   A 151 ? 0.69719 0.85128 0.81007 -0.08395 0.03960  0.02762  148 LEU   A CD1 
1230 C CD2 . LEU   A 151 ? 0.69925 0.81723 0.77738 -0.08032 0.02189  0.02818  148 LEU   A CD2 
1231 N N   . ALA   A 152 ? 0.41968 0.58902 0.54491 -0.05172 0.01276  0.01418  149 ALA   A N   
1232 C CA  . ALA   A 152 ? 0.43013 0.60828 0.56140 -0.04916 0.01306  0.01277  149 ALA   A CA  
1233 C C   . ALA   A 152 ? 0.44288 0.60199 0.55925 -0.04474 0.00307  0.01084  149 ALA   A C   
1234 O O   . ALA   A 152 ? 0.49974 0.63887 0.60055 -0.04124 -0.00579 0.00932  149 ALA   A O   
1235 C CB  . ALA   A 152 ? 0.38144 0.58227 0.52515 -0.04317 0.01486  0.00610  149 ALA   A CB  
1236 N N   . ARG   A 153 ? 0.49260 0.65494 0.61126 -0.04491 0.00343  0.01093  150 ARG   A N   
1237 C CA  . ARG   A 153 ? 0.51379 0.65747 0.61822 -0.04073 -0.00646 0.00820  150 ARG   A CA  
1238 C C   . ARG   A 153 ? 0.57746 0.73467 0.68871 -0.03676 -0.00551 0.00456  150 ARG   A C   
1239 O O   . ARG   A 153 ? 0.50499 0.67579 0.62638 -0.04281 0.00232  0.00873  150 ARG   A O   
1240 C CB  . ARG   A 153 ? 0.66744 0.78859 0.75884 -0.05200 -0.00776 0.01504  150 ARG   A CB  
1241 C CG  . ARG   A 153 ? 0.83913 0.93755 0.91396 -0.04999 -0.01835 0.01269  150 ARG   A CG  
1242 C CD  . ARG   A 153 ? 0.81396 0.89710 0.88022 -0.06521 -0.01699 0.01925  150 ARG   A CD  
1243 N NE  . ARG   A 153 ? 1.09171 1.14457 1.13477 -0.07198 -0.02233 0.02267  150 ARG   A NE  
1244 C CZ  . ARG   A 153 ? 1.04600 1.06545 1.06418 -0.07066 -0.03485 0.02137  150 ARG   A CZ  
1245 N NH1 . ARG   A 153 ? 0.94136 0.95484 0.95637 -0.06143 -0.04354 0.01544  150 ARG   A NH1 
1246 N NH2 . ARG   A 153 ? 0.89115 0.87993 0.88431 -0.07895 -0.03923 0.02600  150 ARG   A NH2 
1247 N N   . ALA   A 154 ? 0.52502 0.67731 0.62903 -0.02563 -0.01438 -0.00389 151 ALA   A N   
1248 C CA  . ALA   A 154 ? 0.59243 0.75326 0.69800 -0.02198 -0.01459 -0.00809 151 ALA   A CA  
1249 C C   . ALA   A 154 ? 0.56687 0.70708 0.66158 -0.02928 -0.01883 -0.00321 151 ALA   A C   
1250 O O   . ALA   A 154 ? 0.74358 0.85672 0.82279 -0.03140 -0.02707 -0.00183 151 ALA   A O   
1251 C CB  . ALA   A 154 ? 0.54857 0.71243 0.65042 -0.00643 -0.02286 -0.02097 151 ALA   A CB  
1252 N N   . PHE   A 155 ? 0.61876 0.77057 0.72004 -0.03417 -0.01379 -0.00058 152 PHE   A N   
1253 C CA  . PHE   A 155 ? 0.58105 0.71859 0.67550 -0.04179 -0.01783 0.00279  152 PHE   A CA  
1254 C C   . PHE   A 155 ? 0.74309 0.87725 0.82934 -0.03412 -0.02471 -0.00462 152 PHE   A C   
1255 O O   . PHE   A 155 ? 0.66396 0.81656 0.75495 -0.02646 -0.02136 -0.00996 152 PHE   A O   
1256 C CB  . PHE   A 155 ? 0.63057 0.78236 0.73807 -0.05204 -0.00968 0.01020  152 PHE   A CB  
1257 C CG  . PHE   A 155 ? 0.67719 0.84970 0.79310 -0.04859 -0.00431 0.00977  152 PHE   A CG  
1258 C CD1 . PHE   A 155 ? 0.55958 0.73300 0.67111 -0.04725 -0.00805 0.00759  152 PHE   A CD1 
1259 C CD2 . PHE   A 155 ? 0.58154 0.76990 0.70689 -0.04808 0.00408  0.01198  152 PHE   A CD2 
1260 C CE1 . PHE   A 155 ? 0.58831 0.77698 0.70247 -0.04527 -0.00344 0.00814  152 PHE   A CE1 
1261 C CE2 . PHE   A 155 ? 0.62941 0.83183 0.75748 -0.04729 0.00886  0.01279  152 PHE   A CE2 
1262 C CZ  . PHE   A 155 ? 0.63747 0.83953 0.75884 -0.04585 0.00516  0.01118  152 PHE   A CZ  
1263 N N   . GLY   A 156 ? 0.67553 0.78545 0.74787 -0.03739 -0.03403 -0.00534 153 GLY   A N   
1264 C CA  . GLY   A 156 ? 0.86526 0.96853 0.92790 -0.03068 -0.04169 -0.01280 153 GLY   A CA  
1265 C C   . GLY   A 156 ? 0.89650 1.01260 0.96574 -0.03738 -0.03839 -0.00990 153 GLY   A C   
1266 O O   . GLY   A 156 ? 0.82842 0.95710 0.91009 -0.04685 -0.03144 -0.00231 153 GLY   A O   
1267 N N   . VAL   A 157 ? 0.93138 1.04385 0.99137 -0.03093 -0.04460 -0.01715 154 VAL   A N   
1268 C CA  . VAL   A 157 ? 0.85825 0.97948 0.92019 -0.03548 -0.04447 -0.01591 154 VAL   A CA  
1269 C C   . VAL   A 157 ? 0.99243 1.08902 1.03978 -0.03849 -0.05667 -0.02006 154 VAL   A C   
1270 O O   . VAL   A 157 ? 0.95819 1.04358 0.99164 -0.02837 -0.06417 -0.02947 154 VAL   A O   
1271 C CB  . VAL   A 157 ? 0.93977 1.08136 1.00160 -0.02623 -0.03948 -0.02099 154 VAL   A CB  
1272 C CG1 . VAL   A 157 ? 0.74338 0.89057 0.80351 -0.03075 -0.04090 -0.01886 154 VAL   A CG1 
1273 C CG2 . VAL   A 157 ? 0.76010 0.92319 0.83424 -0.02552 -0.02763 -0.01711 154 VAL   A CG2 
1274 N N   . PRO   A 158 ? 0.95568 1.04399 1.00589 -0.05289 -0.05898 -0.01428 155 PRO   A N   
1275 C CA  . PRO   A 158 ? 0.87888 0.98197 0.94638 -0.06473 -0.05085 -0.00537 155 PRO   A CA  
1276 C C   . PRO   A 158 ? 0.97625 1.07015 1.04359 -0.06897 -0.04692 -0.00104 155 PRO   A C   
1277 O O   . PRO   A 158 ? 0.76824 0.83908 0.81978 -0.06445 -0.05292 -0.00416 155 PRO   A O   
1278 C CB  . PRO   A 158 ? 0.91509 1.01288 0.98342 -0.07789 -0.05694 -0.00502 155 PRO   A CB  
1279 C CG  . PRO   A 158 ? 0.98078 1.04634 1.02675 -0.07780 -0.06841 -0.01081 155 PRO   A CG  
1280 C CD  . PRO   A 158 ? 1.04843 1.11141 1.08387 -0.05911 -0.07078 -0.01807 155 PRO   A CD  
1281 N N   . VAL   A 159 ? 0.80685 0.91724 0.89014 -0.07668 -0.03781 0.00555  156 VAL   A N   
1282 C CA  . VAL   A 159 ? 0.85563 0.95851 0.93779 -0.08174 -0.03328 0.00978  156 VAL   A CA  
1283 C C   . VAL   A 159 ? 0.85422 0.93574 0.92558 -0.09755 -0.03746 0.01168  156 VAL   A C   
1284 O O   . VAL   A 159 ? 0.85743 0.93485 0.92694 -0.10553 -0.04284 0.00971  156 VAL   A O   
1285 C CB  . VAL   A 159 ? 0.69322 0.82134 0.79529 -0.08393 -0.02188 0.01489  156 VAL   A CB  
1286 C CG1 . VAL   A 159 ? 0.69746 0.84452 0.80779 -0.07214 -0.01801 0.01387  156 VAL   A CG1 
1287 C CG2 . VAL   A 159 ? 0.76852 0.91004 0.88455 -0.09658 -0.01913 0.01712  156 VAL   A CG2 
1288 N N   . ARG   A 160 ? 0.81907 0.88609 0.88146 -0.10347 -0.03514 0.01544  157 ARG   A N   
1289 C CA  . ARG   A 160 ? 0.86112 0.90955 0.91201 -0.12255 -0.03583 0.01883  157 ARG   A CA  
1290 C C   . ARG   A 160 ? 0.77828 0.84098 0.83916 -0.13118 -0.02399 0.02402  157 ARG   A C   
1291 O O   . ARG   A 160 ? 0.76469 0.84988 0.84168 -0.12173 -0.01671 0.02472  157 ARG   A O   
1292 C CB  . ARG   A 160 ? 0.89388 0.89798 0.91220 -0.12247 -0.04776 0.01800  157 ARG   A CB  
1293 C CG  . ARG   A 160 ? 0.93153 0.91962 0.93639 -0.11388 -0.04868 0.01989  157 ARG   A CG  
1294 C CD  . ARG   A 160 ? 1.04603 0.98476 1.01496 -0.11535 -0.06267 0.01960  157 ARG   A CD  
1295 N NE  . ARG   A 160 ? 1.11697 1.03725 1.06998 -0.11181 -0.06406 0.02289  157 ARG   A NE  
1296 C CZ  . ARG   A 160 ? 1.09597 1.01100 1.04451 -0.09088 -0.07127 0.01795  157 ARG   A CZ  
1297 N NH1 . ARG   A 160 ? 1.03429 0.96251 0.99309 -0.07210 -0.07626 0.00911  157 ARG   A NH1 
1298 N NH2 . ARG   A 160 ? 0.92346 0.82133 0.85689 -0.08897 -0.07353 0.02106  157 ARG   A NH2 
1299 N N   . THR   A 161 ? 0.76878 0.81749 0.81836 -0.15038 -0.02176 0.02731  158 THR   A N   
1300 C CA  . THR   A 161 ? 0.73817 0.80096 0.79535 -0.16033 -0.00967 0.03108  158 THR   A CA  
1301 C C   . THR   A 161 ? 0.91969 0.96840 0.96409 -0.14946 -0.00967 0.03366  158 THR   A C   
1302 O O   . THR   A 161 ? 0.81334 0.82563 0.82890 -0.14926 -0.01832 0.03533  158 THR   A O   
1303 C CB  . THR   A 161 ? 0.70826 0.75759 0.75183 -0.18570 -0.00673 0.03350  158 THR   A CB  
1304 O OG1 . THR   A 161 ? 0.92809 0.99461 0.98676 -0.19613 -0.00734 0.02959  158 THR   A OG1 
1305 C CG2 . THR   A 161 ? 0.83498 0.90259 0.88663 -0.19618 0.00729  0.03592  158 THR   A CG2 
1306 N N   . TYR   A 162 ? 0.75535 0.83117 0.82007 -0.14011 -0.00136 0.03351  159 TYR   A N   
1307 C CA  . TYR   A 162 ? 0.73566 0.80346 0.79223 -0.13006 -0.00104 0.03491  159 TYR   A CA  
1308 C C   . TYR   A 162 ? 0.77475 0.84729 0.83019 -0.14202 0.00938  0.03840  159 TYR   A C   
1309 O O   . TYR   A 162 ? 0.72459 0.80491 0.78328 -0.15905 0.01640  0.03929  159 TYR   A O   
1310 C CB  . TYR   A 162 ? 0.81566 0.90732 0.89233 -0.11231 0.00062  0.03193  159 TYR   A CB  
1311 C CG  . TYR   A 162 ? 0.65574 0.74444 0.73146 -0.10012 -0.00831 0.02753  159 TYR   A CG  
1312 C CD1 . TYR   A 162 ? 0.78979 0.84832 0.84273 -0.09788 -0.02014 0.02532  159 TYR   A CD1 
1313 C CD2 . TYR   A 162 ? 0.80552 0.91945 0.90040 -0.09097 -0.00525 0.02522  159 TYR   A CD2 
1314 C CE1 . TYR   A 162 ? 0.75515 0.81243 0.80705 -0.08581 -0.02794 0.01956  159 TYR   A CE1 
1315 C CE2 . TYR   A 162 ? 0.68866 0.80120 0.78072 -0.08080 -0.01212 0.02056  159 TYR   A CE2 
1316 C CZ  . TYR   A 162 ? 0.83761 0.92366 0.90947 -0.07777 -0.02307 0.01706  159 TYR   A CZ  
1317 O OH  . TYR   A 162 ? 0.71476 0.80078 0.78367 -0.06670 -0.02960 0.01075  159 TYR   A OH  
1318 N N   . TPO   A 163 ? 0.74044 0.81033 0.79171 -0.13343 0.01056  0.03923  160 TPO   A N   
1319 C CA  . TPO   A 163 ? 0.80167 0.87304 0.84782 -0.14323 0.01968  0.04193  160 TPO   A CA  
1320 C CB  . TPO   A 163 ? 0.81863 0.88284 0.85758 -0.13059 0.01695  0.04188  160 TPO   A CB  
1321 C CG2 . TPO   A 163 ? 0.75262 0.81767 0.78439 -0.14024 0.02619  0.04413  160 TPO   A CG2 
1322 O OG1 . TPO   A 163 ? 0.77637 0.80718 0.78937 -0.12406 0.00321  0.04218  160 TPO   A OG1 
1323 P P   . TPO   A 163 ? 0.75819 0.79377 0.77988 -0.10065 -0.00704 0.03619  160 TPO   A P   
1324 O O1P . TPO   A 163 ? 0.85569 0.85047 0.84485 -0.09668 -0.02253 0.03595  160 TPO   A O1P 
1325 O O2P . TPO   A 163 ? 0.63715 0.69466 0.68061 -0.09758 -0.00491 0.03343  160 TPO   A O2P 
1326 O O3P . TPO   A 163 ? 0.67717 0.73206 0.71217 -0.09318 -0.00144 0.03468  160 TPO   A O3P 
1327 C C   . TPO   A 163 ? 0.71923 0.82731 0.79367 -0.14862 0.03288  0.03991  160 TPO   A C   
1328 O O   . TPO   A 163 ? 0.70531 0.83737 0.80360 -0.13715 0.03465  0.03718  160 TPO   A O   
1329 N N   . HIS   A 164 ? 0.67290 0.78442 0.74301 -0.16622 0.04177  0.04068  161 HIS   A N   
1330 C CA  . HIS   A 164 ? 0.91192 1.05993 1.00918 -0.17080 0.05389  0.03646  161 HIS   A CA  
1331 C C   . HIS   A 164 ? 0.91839 1.07678 1.02063 -0.16441 0.06133  0.03537  161 HIS   A C   
1332 O O   . HIS   A 164 ? 0.75774 0.89405 0.83902 -0.16149 0.05842  0.03850  161 HIS   A O   
1333 C CB  . HIS   A 164 ? 0.85789 1.01113 0.95102 -0.19378 0.06160  0.03545  161 HIS   A CB  
1334 C CG  . HIS   A 164 ? 1.05583 1.18995 1.12137 -0.20853 0.06792  0.03886  161 HIS   A CG  
1335 N ND1 . HIS   A 164 ? 1.09966 1.19776 1.13455 -0.20357 0.06053  0.04443  161 HIS   A ND1 
1336 C CD2 . HIS   A 164 ? 1.08363 1.23027 1.14642 -0.22824 0.08085  0.03690  161 HIS   A CD2 
1337 C CE1 . HIS   A 164 ? 1.19480 1.28014 1.20614 -0.21968 0.06784  0.04696  161 HIS   A CE1 
1338 N NE2 . HIS   A 164 ? 1.08922 1.20414 1.11657 -0.23577 0.08128  0.04251  161 HIS   A NE2 
1339 N N   . GLU   A 165 ? 0.90655 1.09773 1.03613 -0.16139 0.06955  0.03007  162 GLU   A N   
1340 C CA  . GLU   A 165 ? 0.88877 1.09158 1.02475 -0.15606 0.07717  0.02740  162 GLU   A CA  
1341 C C   . GLU   A 165 ? 0.81285 1.00160 0.94301 -0.14065 0.07054  0.03004  162 GLU   A C   
1342 O O   . GLU   A 165 ? 1.04276 1.22008 1.15871 -0.14028 0.07220  0.03101  162 GLU   A O   
1343 C CB  . GLU   A 165 ? 0.85071 1.04760 0.96809 -0.17219 0.08651  0.02740  162 GLU   A CB  
1344 C CG  . GLU   A 165 ? 0.81336 1.02853 0.93723 -0.19079 0.09529  0.02356  162 GLU   A CG  
1345 C CD  . GLU   A 165 ? 1.19093 1.40358 1.29576 -0.20826 0.10706  0.02284  162 GLU   A CD  
1346 O OE1 . GLU   A 165 ? 1.20448 1.41317 1.30156 -0.20231 0.11055  0.02236  162 GLU   A OE1 
1347 O OE2 . GLU   A 165 ? 1.17145 1.38568 1.26756 -0.22921 0.11304  0.02258  162 GLU   A OE2 
1348 N N   . VAL   A 166 ? 0.67990 0.87091 0.82090 -0.12876 0.06312  0.03058  163 VAL   A N   
1349 C CA  . VAL   A 166 ? 0.67077 0.85490 0.81049 -0.11566 0.05807  0.03168  163 VAL   A CA  
1350 C C   . VAL   A 166 ? 0.62332 0.82652 0.78297 -0.10775 0.06276  0.02862  163 VAL   A C   
1351 O O   . VAL   A 166 ? 0.69368 0.91495 0.86870 -0.10965 0.06807  0.02507  163 VAL   A O   
1352 C CB  . VAL   A 166 ? 0.56396 0.73997 0.70159 -0.10838 0.04849  0.03321  163 VAL   A CB  
1353 C CG1 . VAL   A 166 ? 0.79860 0.94912 0.91234 -0.11314 0.04137  0.03545  163 VAL   A CG1 
1354 C CG2 . VAL   A 166 ? 0.44761 0.63891 0.60166 -0.10781 0.04790  0.03200  163 VAL   A CG2 
1355 N N   . VAL   A 167 ? 0.48751 0.68642 0.64662 -0.09891 0.06008  0.02916  164 VAL   A N   
1356 C CA  . VAL   A 167 ? 0.63462 0.84389 0.80725 -0.09180 0.06268  0.02718  164 VAL   A CA  
1357 C C   . VAL   A 167 ? 0.50097 0.71519 0.67484 -0.09450 0.07006  0.02346  164 VAL   A C   
1358 O O   . VAL   A 167 ? 0.45434 0.67581 0.62880 -0.10192 0.07560  0.02104  164 VAL   A O   
1359 C CB  . VAL   A 167 ? 0.60026 0.82166 0.78856 -0.08720 0.06106  0.02668  164 VAL   A CB  
1360 C CG1 . VAL   A 167 ? 0.60470 0.82824 0.80056 -0.07960 0.06126  0.02586  164 VAL   A CG1 
1361 C CG2 . VAL   A 167 ? 0.55767 0.77453 0.74249 -0.08563 0.05441  0.02961  164 VAL   A CG2 
1362 N N   . THR   A 168 ? 0.52294 0.73414 0.69678 -0.08947 0.07059  0.02219  165 THR   A N   
1363 C CA  . THR   A 168 ? 0.47706 0.69265 0.65234 -0.08999 0.07703  0.01734  165 THR   A CA  
1364 C C   . THR   A 168 ? 0.60537 0.83841 0.79810 -0.08732 0.08085  0.01235  165 THR   A C   
1365 O O   . THR   A 168 ? 0.55473 0.79323 0.75889 -0.08190 0.07655  0.01319  165 THR   A O   
1366 C CB  . THR   A 168 ? 0.58174 0.78984 0.75529 -0.08450 0.07515  0.01650  165 THR   A CB  
1367 O OG1 . THR   A 168 ? 0.62109 0.81806 0.78251 -0.08573 0.07023  0.01950  165 THR   A OG1 
1368 C CG2 . THR   A 168 ? 0.55983 0.76908 0.73096 -0.08486 0.08102  0.01071  165 THR   A CG2 
1369 N N   . LEU   A 169 ? 0.44074 0.68349 0.63497 -0.09063 0.08859  0.00613  166 LEU   A N   
1370 C CA  . LEU   A 169 ? 0.46607 0.73147 0.67852 -0.08934 0.09291  -0.00109 166 LEU   A CA  
1371 C C   . LEU   A 169 ? 0.52114 0.79092 0.74953 -0.07550 0.08719  -0.00423 166 LEU   A C   
1372 O O   . LEU   A 169 ? 0.41355 0.69654 0.65668 -0.07160 0.08385  -0.00633 166 LEU   A O   
1373 C CB  . LEU   A 169 ? 0.42374 0.70068 0.63434 -0.09482 0.10342  -0.00902 166 LEU   A CB  
1374 C CG  . LEU   A 169 ? 0.51883 0.82619 0.75027 -0.09521 0.10976  -0.01925 166 LEU   A CG  
1375 C CD1 . LEU   A 169 ? 0.52629 0.84346 0.76207 -0.10572 0.10968  -0.01643 166 LEU   A CD1 
1376 C CD2 . LEU   A 169 ? 0.43448 0.75440 0.66192 -0.10143 0.12183  -0.02808 166 LEU   A CD2 
1377 N N   . TRP   A 170 ? 0.37216 0.62871 0.59588 -0.06825 0.08486  -0.00466 167 TRP   A N   
1378 C CA  . TRP   A 170 ? 0.42956 0.68365 0.66304 -0.05556 0.07847  -0.00745 167 TRP   A CA  
1379 C C   . TRP   A 170 ? 0.42389 0.67066 0.65819 -0.05261 0.06981  -0.00011 167 TRP   A C   
1380 O O   . TRP   A 170 ? 0.41817 0.66468 0.66034 -0.04259 0.06328  -0.00225 167 TRP   A O   
1381 C CB  . TRP   A 170 ? 0.38996 0.62557 0.61362 -0.05134 0.07708  -0.00812 167 TRP   A CB  
1382 C CG  . TRP   A 170 ? 0.45340 0.69564 0.67728 -0.05012 0.08401  -0.01775 167 TRP   A CG  
1383 C CD1 . TRP   A 170 ? 0.42551 0.68942 0.65582 -0.05428 0.09289  -0.02528 167 TRP   A CD1 
1384 C CD2 . TRP   A 170 ? 0.34301 0.57026 0.55901 -0.04541 0.08313  -0.02166 167 TRP   A CD2 
1385 N NE1 . TRP   A 170 ? 0.49459 0.75907 0.72122 -0.05156 0.09814  -0.03401 167 TRP   A NE1 
1386 C CE2 . TRP   A 170 ? 0.45183 0.69293 0.66972 -0.04541 0.09156  -0.03205 167 TRP   A CE2 
1387 C CE3 . TRP   A 170 ? 0.48519 0.68849 0.69167 -0.04266 0.07636  -0.01776 167 TRP   A CE3 
1388 C CZ2 . TRP   A 170 ? 0.48478 0.71559 0.69526 -0.04086 0.09253  -0.03903 167 TRP   A CZ2 
1389 C CZ3 . TRP   A 170 ? 0.51714 0.70914 0.71659 -0.03937 0.07688  -0.02421 167 TRP   A CZ3 
1390 C CH2 . TRP   A 170 ? 0.56189 0.76713 0.76333 -0.03754 0.08446  -0.03492 167 TRP   A CH2 
1391 N N   . TYR   A 171 ? 0.33829 0.57812 0.56305 -0.06022 0.06887  0.00779  168 TYR   A N   
1392 C CA  . TYR   A 171 ? 0.39039 0.62309 0.61297 -0.05834 0.06178  0.01435  168 TYR   A CA  
1393 C C   . TYR   A 171 ? 0.37945 0.62239 0.60531 -0.06348 0.06109  0.01610  168 TYR   A C   
1394 O O   . TYR   A 171 ? 0.38741 0.62429 0.60832 -0.06364 0.05614  0.02143  168 TYR   A O   
1395 C CB  . TYR   A 171 ? 0.40475 0.62098 0.61361 -0.06152 0.06051  0.02037  168 TYR   A CB  
1396 C CG  . TYR   A 171 ? 0.47329 0.67823 0.67769 -0.05914 0.06128  0.01827  168 TYR   A CG  
1397 C CD1 . TYR   A 171 ? 0.42947 0.62152 0.63154 -0.05346 0.05608  0.01948  168 TYR   A CD1 
1398 C CD2 . TYR   A 171 ? 0.42728 0.63142 0.62707 -0.06293 0.06624  0.01505  168 TYR   A CD2 
1399 C CE1 . TYR   A 171 ? 0.50984 0.68804 0.70589 -0.05220 0.05592  0.01732  168 TYR   A CE1 
1400 C CE2 . TYR   A 171 ? 0.44024 0.63331 0.63548 -0.06103 0.06629  0.01229  168 TYR   A CE2 
1401 C CZ  . TYR   A 171 ? 0.46990 0.64986 0.66377 -0.05592 0.06118  0.01328  168 TYR   A CZ  
1402 O OH  . TYR   A 171 ? 0.47817 0.64352 0.66550 -0.05498 0.06037  0.01040  168 TYR   A OH  
1403 N N   . ARG   A 172 ? 0.33009 0.58835 0.56317 -0.06870 0.06631  0.01113  169 ARG   A N   
1404 C CA  . ARG   A 172 ? 0.37686 0.64291 0.61140 -0.07628 0.06592  0.01229  169 ARG   A CA  
1405 C C   . ARG   A 172 ? 0.37139 0.65225 0.62206 -0.07050 0.06048  0.00874  169 ARG   A C   
1406 O O   . ARG   A 172 ? 0.33494 0.63057 0.60056 -0.06367 0.06083  0.00119  169 ARG   A O   
1407 C CB  . ARG   A 172 ? 0.37106 0.64561 0.60336 -0.08770 0.07449  0.00876  169 ARG   A CB  
1408 C CG  . ARG   A 172 ? 0.39537 0.67146 0.62358 -0.09885 0.07402  0.01093  169 ARG   A CG  
1409 C CD  . ARG   A 172 ? 0.43124 0.71075 0.65136 -0.11289 0.08315  0.00861  169 ARG   A CD  
1410 N NE  . ARG   A 172 ? 0.44456 0.70595 0.64578 -0.11424 0.08586  0.01167  169 ARG   A NE  
1411 C CZ  . ARG   A 172 ? 0.45295 0.71205 0.64123 -0.12531 0.09367  0.01039  169 ARG   A CZ  
1412 N NH1 . ARG   A 172 ? 0.34329 0.61826 0.53542 -0.13807 0.10132  0.00610  169 ARG   A NH1 
1413 N NH2 . ARG   A 172 ? 0.53450 0.77561 0.70472 -0.12456 0.09386  0.01308  169 ARG   A NH2 
1414 N N   . ALA   A 173 ? 0.43950 0.71673 0.68700 -0.07215 0.05452  0.01304  170 ALA   A N   
1415 C CA  . ALA   A 173 ? 0.32469 0.61374 0.58505 -0.06625 0.04724  0.01014  170 ALA   A CA  
1416 C C   . ALA   A 173 ? 0.41138 0.72678 0.68953 -0.07236 0.05091  0.00155  170 ALA   A C   
1417 O O   . ALA   A 173 ? 0.38758 0.70706 0.66213 -0.08524 0.05885  0.00071  170 ALA   A O   
1418 C CB  . ALA   A 173 ? 0.35367 0.63145 0.60355 -0.06752 0.04040  0.01638  170 ALA   A CB  
1419 N N   . PRO   A 174 ? 0.35862 0.69242 0.65533 -0.06387 0.04487  -0.00544 171 PRO   A N   
1420 C CA  . PRO   A 174 ? 0.36429 0.73004 0.68227 -0.07026 0.04910  -0.01603 171 PRO   A CA  
1421 C C   . PRO   A 174 ? 0.34231 0.71217 0.65755 -0.08613 0.05014  -0.01421 171 PRO   A C   
1422 O O   . PRO   A 174 ? 0.38484 0.77582 0.70995 -0.09918 0.05829  -0.02075 171 PRO   A O   
1423 C CB  . PRO   A 174 ? 0.41652 0.79842 0.75414 -0.05409 0.03852  -0.02401 171 PRO   A CB  
1424 C CG  . PRO   A 174 ? 0.32204 0.67562 0.64274 -0.04427 0.02735  -0.01434 171 PRO   A CG  
1425 C CD  . PRO   A 174 ? 0.41000 0.73648 0.70834 -0.04821 0.03345  -0.00479 171 PRO   A CD  
1426 N N   . GLU   A 175 ? 0.38811 0.73792 0.68891 -0.08638 0.04241  -0.00610 172 GLU   A N   
1427 C CA  . GLU   A 175 ? 0.44816 0.79710 0.74353 -0.10115 0.04211  -0.00472 172 GLU   A CA  
1428 C C   . GLU   A 175 ? 0.44266 0.77739 0.72027 -0.11628 0.05161  -0.00053 172 GLU   A C   
1429 O O   . GLU   A 175 ? 0.42760 0.76669 0.70317 -0.13251 0.05488  -0.00213 172 GLU   A O   
1430 C CB  . GLU   A 175 ? 0.42747 0.75697 0.70966 -0.09620 0.03133  0.00177  172 GLU   A CB  
1431 C CG  . GLU   A 175 ? 0.35889 0.65968 0.61863 -0.09089 0.03096  0.01085  172 GLU   A CG  
1432 C CD  . GLU   A 175 ? 0.35695 0.65250 0.61680 -0.07564 0.02637  0.01294  172 GLU   A CD  
1433 O OE1 . GLU   A 175 ? 0.38793 0.69825 0.66345 -0.06779 0.02497  0.00752  172 GLU   A OE1 
1434 O OE2 . GLU   A 175 ? 0.33931 0.61558 0.58267 -0.07177 0.02390  0.01941  172 GLU   A OE2 
1435 N N   . ILE   A 176 ? 0.36298 0.67922 0.62601 -0.11198 0.05530  0.00471  173 ILE   A N   
1436 C CA  . ILE   A 176 ? 0.36853 0.67004 0.61300 -0.12460 0.06284  0.00818  173 ILE   A CA  
1437 C C   . ILE   A 176 ? 0.42896 0.75258 0.68364 -0.13469 0.07426  0.00090  173 ILE   A C   
1438 O O   . ILE   A 176 ? 0.46256 0.78241 0.70542 -0.15215 0.08054  0.00154  173 ILE   A O   
1439 C CB  . ILE   A 176 ? 0.35934 0.63784 0.58728 -0.11621 0.06228  0.01438  173 ILE   A CB  
1440 C CG1 . ILE   A 176 ? 0.35352 0.61581 0.57325 -0.10720 0.05263  0.01974  173 ILE   A CG1 
1441 C CG2 . ILE   A 176 ? 0.40816 0.66865 0.61434 -0.12755 0.06740  0.01786  173 ILE   A CG2 
1442 C CD1 . ILE   A 176 ? 0.64607 0.89097 0.85269 -0.10013 0.05221  0.02421  173 ILE   A CD1 
1443 N N   . LEU   A 177 ? 0.35589 0.70184 0.63084 -0.12415 0.07700  -0.00666 174 LEU   A N   
1444 C CA  . LEU   A 177 ? 0.37228 0.74422 0.65931 -0.13197 0.08873  -0.01611 174 LEU   A CA  
1445 C C   . LEU   A 177 ? 0.46681 0.86683 0.76978 -0.14650 0.09213  -0.02364 174 LEU   A C   
1446 O O   . LEU   A 177 ? 0.41694 0.83462 0.72190 -0.16179 0.10430  -0.02959 174 LEU   A O   
1447 C CB  . LEU   A 177 ? 0.44782 0.83677 0.75399 -0.11417 0.08853  -0.02434 174 LEU   A CB  
1448 C CG  . LEU   A 177 ? 0.39280 0.75699 0.68421 -0.10283 0.08733  -0.01886 174 LEU   A CG  
1449 C CD1 . LEU   A 177 ? 0.34033 0.71447 0.64889 -0.08345 0.08220  -0.02596 174 LEU   A CD1 
1450 C CD2 . LEU   A 177 ? 0.50640 0.86479 0.78229 -0.11351 0.09890  -0.01887 174 LEU   A CD2 
1451 N N   . LEU   A 178 ? 0.40704 0.81248 0.72074 -0.14327 0.08195  -0.02402 175 LEU   A N   
1452 C CA  . LEU   A 178 ? 0.42997 0.86291 0.76028 -0.15767 0.08351  -0.03176 175 LEU   A CA  
1453 C C   . LEU   A 178 ? 0.51089 0.92019 0.81764 -0.17831 0.08327  -0.02373 175 LEU   A C   
1454 O O   . LEU   A 178 ? 0.57391 1.00188 0.89092 -0.19385 0.08435  -0.02921 175 LEU   A O   
1455 C CB  . LEU   A 178 ? 0.45008 0.90266 0.80510 -0.14269 0.07090  -0.03804 175 LEU   A CB  
1456 C CG  . LEU   A 178 ? 0.52149 1.00326 0.90373 -0.12372 0.06969  -0.04975 175 LEU   A CG  
1457 C CD1 . LEU   A 178 ? 0.52403 1.01743 0.92448 -0.10772 0.05400  -0.05435 175 LEU   A CD1 
1458 C CD2 . LEU   A 178 ? 0.34853 0.87157 0.75240 -0.13498 0.08327  -0.06398 175 LEU   A CD2 
1459 N N   . GLY   A 179 ? 0.57109 0.93973 0.84668 -0.17855 0.08091  -0.01187 176 GLY   A N   
1460 C CA  . GLY   A 179 ? 0.55722 0.89737 0.80597 -0.19647 0.07943  -0.00457 176 GLY   A CA  
1461 C C   . GLY   A 179 ? 0.50418 0.83212 0.75067 -0.19421 0.06637  -0.00196 176 GLY   A C   
1462 O O   . GLY   A 179 ? 0.62074 0.94636 0.86189 -0.21217 0.06543  -0.00282 176 GLY   A O   
1463 N N   . CYS   A 180 ? 0.44933 0.76824 0.69777 -0.17361 0.05648  0.00105  177 CYS   A N   
1464 C CA  . CYS   A 180 ? 0.50264 0.80902 0.74636 -0.17005 0.04419  0.00311  177 CYS   A CA  
1465 C C   . CYS   A 180 ? 0.59078 0.85783 0.80193 -0.17905 0.04028  0.01064  177 CYS   A C   
1466 O O   . CYS   A 180 ? 0.58064 0.82458 0.77149 -0.17803 0.04314  0.01629  177 CYS   A O   
1467 C CB  . CYS   A 180 ? 0.46346 0.76805 0.71269 -0.14722 0.03611  0.00490  177 CYS   A CB  
1468 S SG  . CYS   A 180 ? 0.65784 0.93522 0.88677 -0.13480 0.03784  0.01310  177 CYS   A SG  
1469 N N   . LYS   A 181 ? 0.61947 0.87783 0.82506 -0.18692 0.03222  0.00985  178 LYS   A N   
1470 C CA  . LYS   A 181 ? 0.58327 0.80113 0.75656 -0.19418 0.02611  0.01566  178 LYS   A CA  
1471 C C   . LYS   A 181 ? 0.67120 0.86652 0.83110 -0.17389 0.01771  0.01983  178 LYS   A C   
1472 O O   . LYS   A 181 ? 0.72067 0.88631 0.85631 -0.17205 0.01591  0.02455  178 LYS   A O   
1473 C CB  . LYS   A 181 ? 0.81418 1.02853 0.98515 -0.20902 0.01938  0.01247  178 LYS   A CB  
1474 C CG  . LYS   A 181 ? 0.85532 1.02344 0.99034 -0.21716 0.01137  0.01756  178 LYS   A CG  
1475 C CD  . LYS   A 181 ? 0.95979 1.12330 1.09271 -0.23120 0.00343  0.01372  178 LYS   A CD  
1476 C CE  . LYS   A 181 ? 1.12434 1.31426 1.27220 -0.25678 0.01277  0.00905  178 LYS   A CE  
1477 N NZ  . LYS   A 181 ? 1.19864 1.36692 1.32181 -0.27737 0.02171  0.01427  178 LYS   A NZ  
1478 N N   . TYR   A 182 ? 0.60432 0.81402 0.77899 -0.15869 0.01227  0.01750  179 TYR   A N   
1479 C CA  . TYR   A 182 ? 0.61170 0.80633 0.77592 -0.14101 0.00617  0.02011  179 TYR   A CA  
1480 C C   . TYR   A 182 ? 0.68496 0.89926 0.86546 -0.12682 0.01063  0.02052  179 TYR   A C   
1481 O O   . TYR   A 182 ? 0.64200 0.88181 0.84380 -0.12645 0.01374  0.01739  179 TYR   A O   
1482 C CB  . TYR   A 182 ? 0.66801 0.85609 0.82777 -0.13653 -0.00481 0.01754  179 TYR   A CB  
1483 C CG  . TYR   A 182 ? 0.72946 0.89636 0.87299 -0.15091 -0.01111 0.01623  179 TYR   A CG  
1484 C CD1 . TYR   A 182 ? 0.72815 0.86006 0.84421 -0.15310 -0.01489 0.01896  179 TYR   A CD1 
1485 C CD2 . TYR   A 182 ? 0.70250 0.88272 0.85713 -0.16200 -0.01473 0.01167  179 TYR   A CD2 
1486 C CE1 . TYR   A 182 ? 0.79958 0.90591 0.89666 -0.16664 -0.02210 0.01811  179 TYR   A CE1 
1487 C CE2 . TYR   A 182 ? 0.76788 0.92619 0.90595 -0.17723 -0.02085 0.01045  179 TYR   A CE2 
1488 C CZ  . TYR   A 182 ? 0.90524 1.02436 1.01301 -0.17978 -0.02454 0.01414  179 TYR   A CZ  
1489 O OH  . TYR   A 182 ? 0.79276 0.88413 0.88009 -0.19536 -0.03197 0.01329  179 TYR   A OH  
1490 N N   . TYR   A 183 ? 0.58657 0.78849 0.75660 -0.11513 0.01020  0.02358  180 TYR   A N   
1491 C CA  . TYR   A 183 ? 0.67202 0.88679 0.85259 -0.10302 0.01340  0.02468  180 TYR   A CA  
1492 C C   . TYR   A 183 ? 0.56379 0.76530 0.73089 -0.09239 0.01022  0.02630  180 TYR   A C   
1493 O O   . TYR   A 183 ? 0.58206 0.76553 0.73333 -0.09262 0.00665  0.02591  180 TYR   A O   
1494 C CB  . TYR   A 183 ? 0.69953 0.92236 0.88756 -0.10500 0.02263  0.02557  180 TYR   A CB  
1495 C CG  . TYR   A 183 ? 0.60068 0.80521 0.77224 -0.10768 0.02561  0.02819  180 TYR   A CG  
1496 C CD1 . TYR   A 183 ? 0.54302 0.73998 0.70774 -0.09774 0.02539  0.02995  180 TYR   A CD1 
1497 C CD2 . TYR   A 183 ? 0.61290 0.80785 0.77474 -0.12090 0.02828  0.02858  180 TYR   A CD2 
1498 C CE1 . TYR   A 183 ? 0.61674 0.79821 0.76733 -0.09859 0.02611  0.03119  180 TYR   A CE1 
1499 C CE2 . TYR   A 183 ? 0.55692 0.73169 0.70023 -0.12235 0.02899  0.03123  180 TYR   A CE2 
1500 C CZ  . TYR   A 183 ? 0.56537 0.73412 0.70416 -0.10999 0.02712  0.03212  180 TYR   A CZ  
1501 O OH  . TYR   A 183 ? 0.63236 0.78223 0.75362 -0.10988 0.02588  0.03364  180 TYR   A OH  
1502 N N   . SER   A 184 ? 0.48946 0.69994 0.66222 -0.08321 0.01124  0.02742  181 SER   A N   
1503 C CA  . SER   A 184 ? 0.61464 0.81847 0.77681 -0.07502 0.01052  0.02793  181 SER   A CA  
1504 C C   . SER   A 184 ? 0.56608 0.77770 0.73363 -0.07009 0.01587  0.03062  181 SER   A C   
1505 O O   . SER   A 184 ? 0.54436 0.75880 0.71825 -0.07189 0.02132  0.03188  181 SER   A O   
1506 C CB  . SER   A 184 ? 0.67670 0.87783 0.83115 -0.07110 0.00352  0.02573  181 SER   A CB  
1507 O OG  . SER   A 184 ? 0.76219 0.97325 0.92374 -0.06921 0.00125  0.02681  181 SER   A OG  
1508 N N   . THR   A 185 ? 0.45868 0.67187 0.62129 -0.06490 0.01428  0.03148  182 THR   A N   
1509 C CA  . THR   A 185 ? 0.50274 0.71805 0.66436 -0.06235 0.01921  0.03440  182 THR   A CA  
1510 C C   . THR   A 185 ? 0.37661 0.59508 0.54761 -0.06197 0.02018  0.03719  182 THR   A C   
1511 O O   . THR   A 185 ? 0.51886 0.73531 0.68890 -0.06142 0.02442  0.03962  182 THR   A O   
1512 C CB  . THR   A 185 ? 0.46132 0.67582 0.61108 -0.05943 0.01779  0.03480  182 THR   A CB  
1513 O OG1 . THR   A 185 ? 0.53466 0.74829 0.68257 -0.05790 0.01094  0.03555  182 THR   A OG1 
1514 C CG2 . THR   A 185 ? 0.43848 0.65260 0.58029 -0.05757 0.01736  0.02967  182 THR   A CG2 
1515 N N   . ALA   A 186 ? 0.42085 0.64476 0.60133 -0.06198 0.01576  0.03574  183 ALA   A N   
1516 C CA  . ALA   A 186 ? 0.37796 0.60636 0.56830 -0.05841 0.01473  0.03621  183 ALA   A CA  
1517 C C   . ALA   A 186 ? 0.44036 0.67135 0.63888 -0.06013 0.02177  0.03535  183 ALA   A C   
1518 O O   . ALA   A 186 ? 0.41227 0.64250 0.61492 -0.05564 0.02179  0.03573  183 ALA   A O   
1519 C CB  . ALA   A 186 ? 0.36992 0.60941 0.57241 -0.05750 0.00807  0.03220  183 ALA   A CB  
1520 N N   . VAL   A 187 ? 0.39912 0.63046 0.59752 -0.06605 0.02674  0.03395  184 VAL   A N   
1521 C CA  . VAL   A 187 ? 0.46371 0.69717 0.66765 -0.06821 0.03327  0.03272  184 VAL   A CA  
1522 C C   . VAL   A 187 ? 0.41810 0.64333 0.61532 -0.06563 0.03642  0.03544  184 VAL   A C   
1523 O O   . VAL   A 187 ? 0.40347 0.62904 0.60545 -0.06439 0.03977  0.03445  184 VAL   A O   
1524 C CB  . VAL   A 187 ? 0.49241 0.72419 0.69292 -0.07608 0.03650  0.03127  184 VAL   A CB  
1525 C CG1 . VAL   A 187 ? 0.45656 0.69561 0.66272 -0.08183 0.03381  0.02859  184 VAL   A CG1 
1526 C CG2 . VAL   A 187 ? 0.47852 0.69829 0.66478 -0.07593 0.03510  0.03298  184 VAL   A CG2 
1527 N N   . ASP   A 188 ? 0.40320 0.62226 0.58964 -0.06534 0.03562  0.03781  185 ASP   A N   
1528 C CA  . ASP   A 188 ? 0.40109 0.61494 0.58194 -0.06550 0.03911  0.03973  185 ASP   A CA  
1529 C C   . ASP   A 188 ? 0.46669 0.67396 0.64495 -0.06263 0.03693  0.04288  185 ASP   A C   
1530 O O   . ASP   A 188 ? 0.41566 0.61630 0.59191 -0.06338 0.03949  0.04397  185 ASP   A O   
1531 C CB  . ASP   A 188 ? 0.46854 0.68280 0.64055 -0.06683 0.03975  0.03940  185 ASP   A CB  
1532 C CG  . ASP   A 188 ? 0.43478 0.65069 0.60666 -0.06755 0.04015  0.03571  185 ASP   A CG  
1533 O OD1 . ASP   A 188 ? 0.37995 0.59415 0.55536 -0.06919 0.04181  0.03485  185 ASP   A OD1 
1534 O OD2 . ASP   A 188 ? 0.43655 0.65429 0.60304 -0.06591 0.03824  0.03315  185 ASP   A OD2 
1535 N N   . ILE   A 189 ? 0.39905 0.60522 0.57505 -0.05921 0.03090  0.04429  186 ILE   A N   
1536 C CA  . ILE   A 189 ? 0.33638 0.53121 0.50561 -0.05520 0.02613  0.04769  186 ILE   A CA  
1537 C C   . ILE   A 189 ? 0.43331 0.62826 0.61386 -0.04968 0.02450  0.04468  186 ILE   A C   
1538 O O   . ILE   A 189 ? 0.41349 0.59431 0.58722 -0.04717 0.02275  0.04672  186 ILE   A O   
1539 C CB  . ILE   A 189 ? 0.40950 0.60281 0.57242 -0.05170 0.01825  0.04918  186 ILE   A CB  
1540 C CG1 . ILE   A 189 ? 0.53025 0.72223 0.67884 -0.05671 0.02067  0.05137  186 ILE   A CG1 
1541 C CG2 . ILE   A 189 ? 0.43614 0.61444 0.59053 -0.04550 0.01033  0.05239  186 ILE   A CG2 
1542 C CD1 . ILE   A 189 ? 0.43967 0.61989 0.57162 -0.06206 0.02488  0.05613  186 ILE   A CD1 
1543 N N   . TRP   A 190 ? 0.33344 0.54389 0.53031 -0.04826 0.02515  0.03908  187 TRP   A N   
1544 C CA  . TRP   A 190 ? 0.41212 0.62819 0.62193 -0.04291 0.02527  0.03375  187 TRP   A CA  
1545 C C   . TRP   A 190 ? 0.38375 0.59161 0.58973 -0.04532 0.03165  0.03389  187 TRP   A C   
1546 O O   . TRP   A 190 ? 0.38402 0.58280 0.58957 -0.03932 0.02923  0.03234  187 TRP   A O   
1547 C CB  . TRP   A 190 ? 0.36974 0.60739 0.59675 -0.04518 0.02791  0.02718  187 TRP   A CB  
1548 C CG  . TRP   A 190 ? 0.30173 0.55106 0.54382 -0.04034 0.03006  0.01950  187 TRP   A CG  
1549 C CD1 . TRP   A 190 ? 0.33639 0.58760 0.58036 -0.04344 0.03826  0.01656  187 TRP   A CD1 
1550 C CD2 . TRP   A 190 ? 0.37582 0.63838 0.63346 -0.03049 0.02351  0.01219  187 TRP   A CD2 
1551 N NE1 . TRP   A 190 ? 0.33535 0.60071 0.59476 -0.03651 0.03845  0.00758  187 TRP   A NE1 
1552 C CE2 . TRP   A 190 ? 0.32761 0.60147 0.59713 -0.02788 0.02922  0.00417  187 TRP   A CE2 
1553 C CE3 . TRP   A 190 ? 0.48641 0.75334 0.74914 -0.02272 0.01257  0.01058  187 TRP   A CE3 
1554 C CZ2 . TRP   A 190 ? 0.30255 0.59452 0.59105 -0.01706 0.02484  -0.00652 187 TRP   A CZ2 
1555 C CZ3 . TRP   A 190 ? 0.41686 0.70073 0.69846 -0.01168 0.00683  0.00046  187 TRP   A CZ3 
1556 C CH2 . TRP   A 190 ? 0.40082 0.69832 0.69622 -0.00857 0.01321  -0.00854 187 TRP   A CH2 
1557 N N   . SER   A 191 ? 0.35604 0.56559 0.55833 -0.05324 0.03845  0.03501  188 SER   A N   
1558 C CA  . SER   A 191 ? 0.37103 0.57376 0.56945 -0.05607 0.04363  0.03457  188 SER   A CA  
1559 C C   . SER   A 191 ? 0.41175 0.59658 0.59778 -0.05598 0.04126  0.03889  188 SER   A C   
1560 O O   . SER   A 191 ? 0.44020 0.61530 0.62447 -0.05444 0.04173  0.03735  188 SER   A O   
1561 C CB  . SER   A 191 ? 0.36570 0.57235 0.56055 -0.06319 0.04853  0.03489  188 SER   A CB  
1562 O OG  . SER   A 191 ? 0.42192 0.63899 0.62285 -0.06529 0.05016  0.03203  188 SER   A OG  
1563 N N   . LEU   A 192 ? 0.35114 0.53007 0.52646 -0.05867 0.03883  0.04409  189 LEU   A N   
1564 C CA  . LEU   A 192 ? 0.43074 0.59090 0.59040 -0.06205 0.03747  0.04904  189 LEU   A CA  
1565 C C   . LEU   A 192 ? 0.40934 0.55225 0.56414 -0.05379 0.02938  0.04986  189 LEU   A C   
1566 O O   . LEU   A 192 ? 0.46327 0.58576 0.60611 -0.05558 0.02791  0.05213  189 LEU   A O   
1567 C CB  . LEU   A 192 ? 0.44124 0.60114 0.58888 -0.06791 0.03793  0.05368  189 LEU   A CB  
1568 C CG  . LEU   A 192 ? 0.70824 0.86482 0.84548 -0.07898 0.04410  0.05574  189 LEU   A CG  
1569 C CD1 . LEU   A 192 ? 0.65293 0.82316 0.80191 -0.08185 0.04992  0.05039  189 LEU   A CD1 
1570 C CD2 . LEU   A 192 ? 0.63489 0.79739 0.76236 -0.08420 0.04597  0.05802  189 LEU   A CD2 
1571 N N   . GLY   A 193 ? 0.41276 0.56285 0.57640 -0.04441 0.02297  0.04723  190 GLY   A N   
1572 C CA  . GLY   A 193 ? 0.43757 0.57383 0.59954 -0.03307 0.01325  0.04550  190 GLY   A CA  
1573 C C   . GLY   A 193 ? 0.50259 0.63835 0.67397 -0.02787 0.01497  0.03871  190 GLY   A C   
1574 O O   . GLY   A 193 ? 0.43469 0.54789 0.59614 -0.02153 0.00822  0.03857  190 GLY   A O   
1575 N N   . CYS   A 194 ? 0.39156 0.54962 0.57945 -0.03054 0.02349  0.03281  191 CYS   A N   
1576 C CA  . CYS   A 194 ? 0.42085 0.57945 0.61545 -0.02711 0.02686  0.02585  191 CYS   A CA  
1577 C C   . CYS   A 194 ? 0.48212 0.61826 0.66054 -0.03404 0.02901  0.02984  191 CYS   A C   
1578 O O   . CYS   A 194 ? 0.46308 0.58383 0.63755 -0.02846 0.02590  0.02612  191 CYS   A O   
1579 C CB  . CYS   A 194 ? 0.41339 0.59791 0.62335 -0.03157 0.03630  0.02015  191 CYS   A CB  
1580 S SG  . CYS   A 194 ? 0.40087 0.61446 0.63159 -0.02693 0.03539  0.01354  191 CYS   A SG  
1581 N N   . ILE   A 195 ? 0.46273 0.59785 0.63233 -0.04616 0.03399  0.03617  192 ILE   A N   
1582 C CA  . ILE   A 195 ? 0.53233 0.65042 0.68847 -0.05522 0.03648  0.03917  192 ILE   A CA  
1583 C C   . ILE   A 195 ? 0.58849 0.67596 0.72491 -0.05497 0.02868  0.04477  192 ILE   A C   
1584 O O   . ILE   A 195 ? 0.56407 0.62999 0.68947 -0.05774 0.02716  0.04467  192 ILE   A O   
1585 C CB  . ILE   A 195 ? 0.53848 0.66903 0.69338 -0.06722 0.04336  0.04235  192 ILE   A CB  
1586 C CG1 . ILE   A 195 ? 0.43540 0.58831 0.60451 -0.06691 0.04888  0.03708  192 ILE   A CG1 
1587 C CG2 . ILE   A 195 ? 0.50726 0.62439 0.65011 -0.07837 0.04590  0.04457  192 ILE   A CG2 
1588 C CD1 . ILE   A 195 ? 0.51194 0.67761 0.68102 -0.07450 0.05287  0.03849  192 ILE   A CD1 
1589 N N   . PHE   A 196 ? 0.47498 0.55704 0.60384 -0.05220 0.02281  0.04988  193 PHE   A N   
1590 C CA  . PHE   A 196 ? 0.50216 0.55035 0.60716 -0.05159 0.01364  0.05621  193 PHE   A CA  
1591 C C   . PHE   A 196 ? 0.48570 0.51337 0.58906 -0.03827 0.00438  0.05096  193 PHE   A C   
1592 O O   . PHE   A 196 ? 0.58152 0.57787 0.66573 -0.04218 0.00073  0.05355  193 PHE   A O   
1593 C CB  . PHE   A 196 ? 0.47063 0.51907 0.56922 -0.04766 0.00737  0.06096  193 PHE   A CB  
1594 C CG  . PHE   A 196 ? 0.60885 0.61906 0.67710 -0.04810 -0.00296 0.06902  193 PHE   A CG  
1595 C CD1 . PHE   A 196 ? 0.70156 0.68035 0.74644 -0.05879 -0.00285 0.07416  193 PHE   A CD1 
1596 C CD2 . PHE   A 196 ? 0.61941 0.62291 0.68014 -0.03862 -0.01369 0.07156  193 PHE   A CD2 
1597 C CE1 . PHE   A 196 ? 0.70359 0.64163 0.71516 -0.06085 -0.01300 0.08266  193 PHE   A CE1 
1598 C CE2 . PHE   A 196 ? 0.63584 0.59967 0.66383 -0.03882 -0.02470 0.07971  193 PHE   A CE2 
1599 C CZ  . PHE   A 196 ? 0.58331 0.51271 0.58520 -0.05037 -0.02422 0.08577  193 PHE   A CZ  
1600 N N   . ALA   A 197 ? 0.56343 0.60921 0.68703 -0.02266 0.00043  0.04241  194 ALA   A N   
1601 C CA  . ALA   A 197 ? 0.54207 0.57370 0.66767 -0.00702 -0.00863 0.03437  194 ALA   A CA  
1602 C C   . ALA   A 197 ? 0.55352 0.58043 0.68036 -0.01077 -0.00237 0.02915  194 ALA   A C   
1603 O O   . ALA   A 197 ? 0.62293 0.62198 0.73845 -0.00291 -0.01049 0.02574  194 ALA   A O   
1604 C CB  . ALA   A 197 ? 0.58893 0.65105 0.74110 0.00871  -0.01153 0.02381  194 ALA   A CB  
1605 N N   . GLU   A 198 ? 0.51280 0.56405 0.65129 -0.02197 0.01062  0.02805  195 GLU   A N   
1606 C CA  . GLU   A 198 ? 0.58135 0.62905 0.72018 -0.02573 0.01603  0.02269  195 GLU   A CA  
1607 C C   . GLU   A 198 ? 0.72003 0.73329 0.83435 -0.03750 0.01368  0.02944  195 GLU   A C   
1608 O O   . GLU   A 198 ? 0.62429 0.61870 0.73164 -0.03601 0.01145  0.02465  195 GLU   A O   
1609 C CB  . GLU   A 198 ? 0.57212 0.65145 0.72598 -0.03456 0.02846  0.02051  195 GLU   A CB  
1610 C CG  . GLU   A 198 ? 0.50141 0.58274 0.65842 -0.03524 0.03355  0.01262  195 GLU   A CG  
1611 C CD  . GLU   A 198 ? 0.59439 0.70374 0.76271 -0.04250 0.04377  0.01080  195 GLU   A CD  
1612 O OE1 . GLU   A 198 ? 0.48827 0.61870 0.66694 -0.04224 0.04648  0.01221  195 GLU   A OE1 
1613 O OE2 . GLU   A 198 ? 0.52296 0.63077 0.68779 -0.04855 0.04794  0.00796  195 GLU   A OE2 
1614 N N   . MET   A 199 ? 0.56311 0.56814 0.66337 -0.05037 0.01454  0.03989  196 MET   A N   
1615 C CA  . MET   A 199 ? 0.60315 0.57499 0.67803 -0.06434 0.01266  0.04663  196 MET   A CA  
1616 C C   . MET   A 199 ? 0.74180 0.67032 0.79458 -0.05481 -0.00149 0.04808  196 MET   A C   
1617 O O   . MET   A 199 ? 0.70658 0.60242 0.74018 -0.06163 -0.00504 0.04905  196 MET   A O   
1618 C CB  . MET   A 199 ? 0.71898 0.69559 0.78375 -0.08067 0.01797  0.05634  196 MET   A CB  
1619 C CG  . MET   A 199 ? 0.57061 0.58218 0.65173 -0.09221 0.03041  0.05435  196 MET   A CG  
1620 S SD  . MET   A 199 ? 0.70603 0.72363 0.77451 -0.11171 0.03714  0.06285  196 MET   A SD  
1621 C CE  . MET   A 199 ? 0.54069 0.56743 0.61106 -0.09998 0.03283  0.06659  196 MET   A CE  
1622 N N   . VAL   A 200 ? 0.70776 0.63395 0.76205 -0.03861 -0.01105 0.04764  197 VAL   A N   
1623 C CA  . VAL   A 200 ? 0.76985 0.65223 0.80096 -0.02683 -0.02751 0.04886  197 VAL   A CA  
1624 C C   . VAL   A 200 ? 0.83730 0.71128 0.87642 -0.01032 -0.03356 0.03623  197 VAL   A C   
1625 O O   . VAL   A 200 ? 0.76384 0.59370 0.77875 -0.00823 -0.04387 0.03660  197 VAL   A O   
1626 C CB  . VAL   A 200 ? 0.66412 0.54930 0.69556 -0.01323 -0.03747 0.05105  197 VAL   A CB  
1627 C CG1 . VAL   A 200 ? 0.79193 0.62980 0.79838 0.00219  -0.05741 0.05128  197 VAL   A CG1 
1628 C CG2 . VAL   A 200 ? 0.67725 0.56779 0.69699 -0.02984 -0.03152 0.06303  197 VAL   A CG2 
1629 N N   . THR   A 201 ? 0.70482 0.61938 0.77589 0.00098  -0.02724 0.02448  198 THR   A N   
1630 C CA  . THR   A 201 ? 0.71956 0.63343 0.80128 0.01901  -0.03209 0.01005  198 THR   A CA  
1631 C C   . THR   A 201 ? 0.71597 0.63889 0.80376 0.01008  -0.02101 0.00411  198 THR   A C   
1632 O O   . THR   A 201 ? 0.80684 0.72794 0.90092 0.02367  -0.02387 -0.00859 198 THR   A O   
1633 C CB  . THR   A 201 ? 0.77649 0.73090 0.88895 0.03732  -0.03218 -0.00116 198 THR   A CB  
1634 O OG1 . THR   A 201 ? 0.74778 0.74667 0.88241 0.02601  -0.01611 -0.00091 198 THR   A OG1 
1635 C CG2 . THR   A 201 ? 0.71445 0.65988 0.82148 0.04818  -0.04555 0.00310  198 THR   A CG2 
1636 N N   . ARG   A 202 ? 0.68534 0.61898 0.77149 -0.01127 -0.00919 0.01174  199 ARG   A N   
1637 C CA  . ARG   A 202 ? 0.78059 0.72480 0.87218 -0.02064 0.00054  0.00654  199 ARG   A CA  
1638 C C   . ARG   A 202 ? 0.73686 0.71865 0.85417 -0.00951 0.00795  -0.00600 199 ARG   A C   
1639 O O   . ARG   A 202 ? 0.65464 0.63927 0.77377 -0.01079 0.01268  -0.01374 199 ARG   A O   
1640 C CB  . ARG   A 202 ? 0.87330 0.77513 0.94263 -0.02256 -0.00687 0.00415  199 ARG   A CB  
1641 C CG  . ARG   A 202 ? 1.05038 0.91570 1.09147 -0.04140 -0.01064 0.01698  199 ARG   A CG  
1642 C CD  . ARG   A 202 ? 0.96729 0.79332 0.98577 -0.03256 -0.02550 0.02296  199 ARG   A CD  
1643 N NE  . ARG   A 202 ? 0.99468 0.76717 0.98402 -0.03311 -0.03715 0.02248  199 ARG   A NE  
1644 C CZ  . ARG   A 202 ? 1.11938 0.87176 1.10673 -0.01235 -0.04812 0.01092  199 ARG   A CZ  
1645 N NH1 . ARG   A 202 ? 1.29463 1.07974 1.30923 0.01013  -0.04783 -0.00193 199 ARG   A NH1 
1646 N NH2 . ARG   A 202 ? 1.26662 0.96490 1.22346 -0.01471 -0.05962 0.01140  199 ARG   A NH2 
1647 N N   . ARG   A 203 ? 0.62165 0.63231 0.75745 -0.00010 0.00931  -0.00827 200 ARG   A N   
1648 C CA  . ARG   A 203 ? 0.68008 0.72764 0.83912 0.00809  0.01726  -0.02000 200 ARG   A CA  
1649 C C   . ARG   A 203 ? 0.66044 0.74091 0.83555 0.00458  0.02299  -0.01576 200 ARG   A C   
1650 O O   . ARG   A 203 ? 0.62247 0.69718 0.79470 0.00615  0.01636  -0.00862 200 ARG   A O   
1651 C CB  . ARG   A 203 ? 0.72702 0.77225 0.89347 0.03004  0.00923  -0.03420 200 ARG   A CB  
1652 C CG  . ARG   A 203 ? 0.98431 1.07168 1.17543 0.03732  0.01895  -0.04800 200 ARG   A CG  
1653 C CD  . ARG   A 203 ? 1.04529 1.13427 1.24609 0.06051  0.01081  -0.06461 200 ARG   A CD  
1654 N NE  . ARG   A 203 ? 1.22305 1.30421 1.42664 0.07463  -0.00329 -0.06380 200 ARG   A NE  
1655 C CZ  . ARG   A 203 ? 1.13266 1.17130 1.31709 0.08592  -0.01996 -0.06216 200 ARG   A CZ  
1656 N NH1 . ARG   A 203 ? 1.24245 1.24192 1.40411 0.08392  -0.02435 -0.06137 200 ARG   A NH1 
1657 N NH2 . ARG   A 203 ? 0.98102 1.01389 1.16707 0.09913  -0.03356 -0.06129 200 ARG   A NH2 
1658 N N   . ALA   A 204 ? 0.55975 0.67155 0.74866 -0.00091 0.03467  -0.01995 201 ALA   A N   
1659 C CA  . ALA   A 204 ? 0.57443 0.71501 0.77680 -0.00554 0.04002  -0.01656 201 ALA   A CA  
1660 C C   . ALA   A 204 ? 0.51199 0.66646 0.72934 0.00874  0.03359  -0.02266 201 ALA   A C   
1661 O O   . ALA   A 204 ? 0.49092 0.65123 0.71774 0.02289  0.03062  -0.03514 201 ALA   A O   
1662 C CB  . ALA   A 204 ? 0.43365 0.60007 0.64410 -0.01343 0.05250  -0.02108 201 ALA   A CB  
1663 N N   . LEU   A 205 ? 0.44569 0.60694 0.66585 0.00575  0.03080  -0.01510 202 LEU   A N   
1664 C CA  . LEU   A 205 ? 0.38567 0.55900 0.61932 0.01917  0.02234  -0.02042 202 LEU   A CA  
1665 C C   . LEU   A 205 ? 0.41490 0.62919 0.67389 0.02184  0.03032  -0.03279 202 LEU   A C   
1666 O O   . LEU   A 205 ? 0.49127 0.71945 0.76562 0.03709  0.02550  -0.04574 202 LEU   A O   
1667 C CB  . LEU   A 205 ? 0.41460 0.58268 0.64178 0.01397  0.01710  -0.00893 202 LEU   A CB  
1668 C CG  . LEU   A 205 ? 0.58153 0.75669 0.81833 0.02751  0.00526  -0.01251 202 LEU   A CG  
1669 C CD1 . LEU   A 205 ? 0.48161 0.63110 0.71062 0.04548  -0.00903 -0.01783 202 LEU   A CD1 
1670 C CD2 . LEU   A 205 ? 0.46814 0.63475 0.69342 0.01991  0.00128  -0.00017 202 LEU   A CD2 
1671 N N   . PHE   A 206 ? 0.39563 0.62955 0.65849 0.00686  0.04225  -0.02972 203 PHE   A N   
1672 C CA  . PHE   A 206 ? 0.39926 0.67065 0.68213 0.00397  0.05172  -0.03979 203 PHE   A CA  
1673 C C   . PHE   A 206 ? 0.42760 0.70267 0.70286 -0.00865 0.06496  -0.04023 203 PHE   A C   
1674 O O   . PHE   A 206 ? 0.42345 0.70230 0.69258 -0.02329 0.07157  -0.03282 203 PHE   A O   
1675 C CB  . PHE   A 206 ? 0.37916 0.66834 0.67082 -0.00349 0.05164  -0.03517 203 PHE   A CB  
1676 C CG  . PHE   A 206 ? 0.40376 0.68679 0.69905 0.00778  0.03758  -0.03324 203 PHE   A CG  
1677 C CD1 . PHE   A 206 ? 0.46628 0.76051 0.77739 0.02547  0.02871  -0.04535 203 PHE   A CD1 
1678 C CD2 . PHE   A 206 ? 0.40597 0.67265 0.68815 0.00148  0.03258  -0.02033 203 PHE   A CD2 
1679 C CE1 . PHE   A 206 ? 0.42296 0.70883 0.73453 0.03670  0.01374  -0.04343 203 PHE   A CE1 
1680 C CE2 . PHE   A 206 ? 0.40070 0.65985 0.68252 0.01122  0.01936  -0.01821 203 PHE   A CE2 
1681 C CZ  . PHE   A 206 ? 0.46088 0.72813 0.75638 0.02880  0.00930  -0.02921 203 PHE   A CZ  
1682 N N   . PRO   A 207 ? 0.41276 0.68458 0.68609 -0.00261 0.06796  -0.04928 204 PRO   A N   
1683 C CA  . PRO   A 207 ? 0.47541 0.74854 0.73826 -0.01405 0.07963  -0.05015 204 PRO   A CA  
1684 C C   . PRO   A 207 ? 0.58319 0.89109 0.85859 -0.01987 0.09220  -0.06085 204 PRO   A C   
1685 O O   . PRO   A 207 ? 0.56674 0.88789 0.84763 -0.01420 0.09805  -0.07412 204 PRO   A O   
1686 C CB  . PRO   A 207 ? 0.46597 0.71710 0.71933 -0.00424 0.07565  -0.05553 204 PRO   A CB  
1687 C CG  . PRO   A 207 ? 0.48350 0.73834 0.75107 0.01478  0.06615  -0.06556 204 PRO   A CG  
1688 C CD  . PRO   A 207 ? 0.40814 0.66841 0.68427 0.01580  0.05876  -0.05851 204 PRO   A CD  
1689 N N   . GLY   A 208 ? 0.43157 0.75450 0.71026 -0.03266 0.09694  -0.05548 205 GLY   A N   
1690 C CA  . GLY   A 208 ? 0.49693 0.85149 0.78467 -0.04271 0.10965  -0.06410 205 GLY   A CA  
1691 C C   . GLY   A 208 ? 0.50733 0.85347 0.77311 -0.05853 0.12030  -0.06002 205 GLY   A C   
1692 O O   . GLY   A 208 ? 0.48639 0.80463 0.73181 -0.06370 0.11670  -0.04839 205 GLY   A O   
1693 N N   . ASP   A 209 ? 0.53395 0.90580 0.80359 -0.06626 0.13335  -0.07066 206 ASP   A N   
1694 C CA  . ASP   A 209 ? 0.63384 0.99776 0.87923 -0.08238 0.14388  -0.06753 206 ASP   A CA  
1695 C C   . ASP   A 209 ? 0.55232 0.92851 0.79209 -0.10299 0.15245  -0.06330 206 ASP   A C   
1696 O O   . ASP   A 209 ? 0.70753 1.07095 0.92158 -0.11801 0.15950  -0.05830 206 ASP   A O   
1697 C CB  . ASP   A 209 ? 0.49946 0.87762 0.74477 -0.07831 0.15374  -0.08249 206 ASP   A CB  
1698 C CG  . ASP   A 209 ? 0.65955 1.08128 0.93386 -0.07310 0.16120  -0.10018 206 ASP   A CG  
1699 O OD1 . ASP   A 209 ? 0.79394 1.23542 1.08821 -0.07431 0.15876  -0.10043 206 ASP   A OD1 
1700 O OD2 . ASP   A 209 ? 0.88442 1.32239 1.16240 -0.06722 0.16916  -0.11517 206 ASP   A OD2 
1701 N N   . SER   A 210 ? 0.46126 0.85942 0.72210 -0.10459 0.15108  -0.06521 207 SER   A N   
1702 C CA  . SER   A 210 ? 0.52939 0.93503 0.78405 -0.12540 0.15726  -0.06019 207 SER   A CA  
1703 C C   . SER   A 210 ? 0.52641 0.93491 0.79767 -0.12129 0.14640  -0.05528 207 SER   A C   
1704 O O   . SER   A 210 ? 0.43346 0.84114 0.72075 -0.10285 0.13553  -0.05674 207 SER   A O   
1705 C CB  . SER   A 210 ? 0.57343 1.01793 0.83873 -0.13827 0.17372  -0.07419 207 SER   A CB  
1706 O OG  . SER   A 210 ? 0.59342 1.07681 0.89596 -0.12566 0.17290  -0.08915 207 SER   A OG  
1707 N N   . GLU   A 211 ? 0.42618 0.83503 0.69037 -0.13933 0.14881  -0.04922 208 GLU   A N   
1708 C CA  . GLU   A 211 ? 0.55356 0.96480 0.83151 -0.13683 0.13854  -0.04508 208 GLU   A CA  
1709 C C   . GLU   A 211 ? 0.40724 0.85960 0.72187 -0.12734 0.13807  -0.05963 208 GLU   A C   
1710 O O   . GLU   A 211 ? 0.48535 0.93737 0.81478 -0.11267 0.12546  -0.05888 208 GLU   A O   
1711 C CB  . GLU   A 211 ? 0.56307 0.96354 0.82345 -0.15909 0.14087  -0.03657 208 GLU   A CB  
1712 C CG  . GLU   A 211 ? 0.51825 0.87487 0.74234 -0.16498 0.13679  -0.02224 208 GLU   A CG  
1713 C CD  . GLU   A 211 ? 0.98201 1.32213 1.18752 -0.18383 0.13524  -0.01387 208 GLU   A CD  
1714 O OE1 . GLU   A 211 ? 0.91452 1.26437 1.13505 -0.18448 0.12939  -0.01414 208 GLU   A OE1 
1715 O OE2 . GLU   A 211 ? 1.17646 1.49136 1.35024 -0.19780 0.13878  -0.00719 208 GLU   A OE2 
1716 N N   . ILE   A 212 ? 0.41197 0.90092 0.74113 -0.13519 0.15134  -0.07382 209 ILE   A N   
1717 C CA  . ILE   A 212 ? 0.42863 0.96220 0.79592 -0.12516 0.15041  -0.09049 209 ILE   A CA  
1718 C C   . ILE   A 212 ? 0.47401 1.00882 0.85565 -0.09701 0.14206  -0.09902 209 ILE   A C   
1719 O O   . ILE   A 212 ? 0.43286 0.98290 0.83907 -0.07971 0.13060  -0.10620 209 ILE   A O   
1720 C CB  . ILE   A 212 ? 0.49519 1.05468 0.86425 -0.13930 0.16349  -0.10086 209 ILE   A CB  
1721 C CG1 . ILE   A 212 ? 0.56745 1.16695 0.97228 -0.12642 0.15879  -0.11731 209 ILE   A CG1 
1722 C CG2 . ILE   A 212 ? 0.50515 1.06314 0.85877 -0.14144 0.17625  -0.10609 209 ILE   A CG2 
1723 C CD1 . ILE   A 212 ? 0.52397 1.12686 0.94259 -0.12648 0.14652  -0.11318 209 ILE   A CD1 
1724 N N   . ASP   A 213 ? 0.42738 0.94303 0.79163 -0.09182 0.14620  -0.09833 210 ASP   A N   
1725 C CA  . ASP   A 213 ? 0.38320 0.89207 0.75589 -0.06614 0.13711  -0.10533 210 ASP   A CA  
1726 C C   . ASP   A 213 ? 0.34580 0.81723 0.70908 -0.05323 0.11954  -0.09153 210 ASP   A C   
1727 O O   . ASP   A 213 ? 0.37519 0.84458 0.75105 -0.03206 0.10755  -0.09711 210 ASP   A O   
1728 C CB  . ASP   A 213 ? 0.48344 0.97947 0.83762 -0.06600 0.14597  -0.10810 210 ASP   A CB  
1729 C CG  . ASP   A 213 ? 0.50503 0.98977 0.86495 -0.04052 0.13615  -0.11577 210 ASP   A CG  
1730 O OD1 . ASP   A 213 ? 0.52961 1.04537 0.91583 -0.02527 0.13504  -0.13384 210 ASP   A OD1 
1731 O OD2 . ASP   A 213 ? 0.50280 0.94748 0.84079 -0.03577 0.12891  -0.10449 210 ASP   A OD2 
1732 N N   . GLN   A 214 ? 0.39065 0.83164 0.73039 -0.06559 0.11753  -0.07416 211 GLN   A N   
1733 C CA  . GLN   A 214 ? 0.29656 0.70684 0.62777 -0.05618 0.10280  -0.06175 211 GLN   A CA  
1734 C C   . GLN   A 214 ? 0.37658 0.80337 0.72853 -0.04897 0.09272  -0.06459 211 GLN   A C   
1735 O O   . GLN   A 214 ? 0.35064 0.76378 0.70527 -0.03241 0.07941  -0.06300 211 GLN   A O   
1736 C CB  . GLN   A 214 ? 0.40799 0.78912 0.71273 -0.07084 0.10358  -0.04555 211 GLN   A CB  
1737 C CG  . GLN   A 214 ? 0.37066 0.72312 0.66560 -0.06321 0.09072  -0.03361 211 GLN   A CG  
1738 C CD  . GLN   A 214 ? 0.51064 0.83934 0.79551 -0.05144 0.08599  -0.03165 211 GLN   A CD  
1739 O OE1 . GLN   A 214 ? 0.40236 0.72911 0.68147 -0.05137 0.09243  -0.03648 211 GLN   A OE1 
1740 N NE2 . GLN   A 214 ? 0.38476 0.69420 0.66551 -0.04281 0.07484  -0.02464 211 GLN   A NE2 
1741 N N   . LEU   A 215 ? 0.37584 0.83055 0.74057 -0.06237 0.09843  -0.06876 212 LEU   A N   
1742 C CA  . LEU   A 215 ? 0.36080 0.83409 0.74622 -0.05675 0.08846  -0.07266 212 LEU   A CA  
1743 C C   . LEU   A 215 ? 0.43983 0.93923 0.85255 -0.03544 0.08171  -0.08926 212 LEU   A C   
1744 O O   . LEU   A 215 ? 0.40941 0.90490 0.83051 -0.02005 0.06637  -0.08956 212 LEU   A O   
1745 C CB  . LEU   A 215 ? 0.39414 0.89318 0.78749 -0.07833 0.09709  -0.07506 212 LEU   A CB  
1746 C CG  . LEU   A 215 ? 0.47197 0.98520 0.88133 -0.07801 0.08663  -0.07615 212 LEU   A CG  
1747 C CD1 . LEU   A 215 ? 0.35770 0.83139 0.74402 -0.07758 0.07577  -0.05912 212 LEU   A CD1 
1748 C CD2 . LEU   A 215 ? 0.50857 1.05431 0.92993 -0.10076 0.09731  -0.08289 212 LEU   A CD2 
1749 N N   . PHE   A 216 ? 0.32130 0.84643 0.74652 -0.03326 0.09218  -0.10389 213 PHE   A N   
1750 C CA  . PHE   A 216 ? 0.37877 0.93083 0.83133 -0.01067 0.08514  -0.12248 213 PHE   A CA  
1751 C C   . PHE   A 216 ? 0.39609 0.91070 0.83564 0.01249  0.07071  -0.11872 213 PHE   A C   
1752 O O   . PHE   A 216 ? 0.43786 0.95849 0.89308 0.03446  0.05610  -0.12820 213 PHE   A O   
1753 C CB  . PHE   A 216 ? 0.37931 0.97119 0.84827 -0.01493 0.10158  -0.14084 213 PHE   A CB  
1754 C CG  . PHE   A 216 ? 0.36053 1.00084 0.85174 -0.03413 0.11356  -0.15081 213 PHE   A CG  
1755 C CD1 . PHE   A 216 ? 0.54412 1.18890 1.04062 -0.04484 0.10766  -0.14384 213 PHE   A CD1 
1756 C CD2 . PHE   A 216 ? 0.40170 1.06781 0.89644 -0.04153 0.12817  -0.16355 213 PHE   A CD2 
1757 C CE1 . PHE   A 216 ? 0.62454 1.28946 1.12409 -0.06246 0.11461  -0.14707 213 PHE   A CE1 
1758 C CE2 . PHE   A 216 ? 0.40730 1.09449 0.90468 -0.05974 0.13556  -0.16654 213 PHE   A CE2 
1759 C CZ  . PHE   A 216 ? 0.50083 1.18695 1.00093 -0.07032 0.12868  -0.15830 213 PHE   A CZ  
1760 N N   . ARG   A 217 ? 0.33085 0.80579 0.74097 0.00775  0.07360  -0.10548 214 ARG   A N   
1761 C CA  . ARG   A 217 ? 0.37071 0.80619 0.76504 0.02557  0.06005  -0.10008 214 ARG   A CA  
1762 C C   . ARG   A 217 ? 0.34622 0.75853 0.73326 0.03145  0.04382  -0.08837 214 ARG   A C   
1763 O O   . ARG   A 217 ? 0.40140 0.79396 0.78552 0.05071  0.02844  -0.08984 214 ARG   A O   
1764 C CB  . ARG   A 217 ? 0.32970 0.73144 0.69557 0.01612  0.06723  -0.08886 214 ARG   A CB  
1765 C CG  . ARG   A 217 ? 0.48244 0.89812 0.85038 0.01599  0.07959  -0.10134 214 ARG   A CG  
1766 C CD  . ARG   A 217 ? 0.59903 0.97789 0.93839 0.00987  0.08275  -0.09091 214 ARG   A CD  
1767 N NE  . ARG   A 217 ? 0.62258 1.01325 0.96138 0.00985  0.09408  -0.10313 214 ARG   A NE  
1768 C CZ  . ARG   A 217 ? 0.67922 1.06601 1.02177 0.02788  0.08954  -0.11591 214 ARG   A CZ  
1769 N NH1 . ARG   A 217 ? 0.74449 1.11269 1.09000 0.04757  0.07294  -0.11760 214 ARG   A NH1 
1770 N NH2 . ARG   A 217 ? 0.77568 1.17496 1.11630 0.02626  0.10127  -0.12745 214 ARG   A NH2 
1771 N N   . ILE   A 218 ? 0.34632 0.75816 0.72755 0.01507  0.04642  -0.07683 215 ILE   A N   
1772 C CA  . ILE   A 218 ? 0.35688 0.75184 0.73207 0.01978  0.03204  -0.06743 215 ILE   A CA  
1773 C C   . ILE   A 218 ? 0.42700 0.85089 0.82885 0.03487  0.02058  -0.08112 215 ILE   A C   
1774 O O   . ILE   A 218 ? 0.45294 0.85785 0.84961 0.05063  0.00351  -0.07889 215 ILE   A O   
1775 C CB  . ILE   A 218 ? 0.34971 0.73988 0.71347 -0.00057 0.03778  -0.05437 215 ILE   A CB  
1776 C CG1 . ILE   A 218 ? 0.32856 0.69048 0.66677 -0.01252 0.04661  -0.04224 215 ILE   A CG1 
1777 C CG2 . ILE   A 218 ? 0.43327 0.80854 0.79051 0.00424  0.02355  -0.04612 215 ILE   A CG2 
1778 C CD1 . ILE   A 218 ? 0.27750 0.63563 0.60466 -0.03107 0.05240  -0.03199 215 ILE   A CD1 
1779 N N   . PHE   A 219 ? 0.41781 0.88834 0.84771 0.02983  0.02941  -0.09602 216 PHE   A N   
1780 C CA  . PHE   A 219 ? 0.35651 0.86224 0.81669 0.04378  0.01866  -0.11170 216 PHE   A CA  
1781 C C   . PHE   A 219 ? 0.56350 1.06500 1.03146 0.07206  0.00548  -0.12433 216 PHE   A C   
1782 O O   . PHE   A 219 ? 0.44854 0.95211 0.92646 0.09082  -0.01302 -0.13029 216 PHE   A O   
1783 C CB  . PHE   A 219 ? 0.38413 0.94466 0.87367 0.02942  0.03346  -0.12649 216 PHE   A CB  
1784 C CG  . PHE   A 219 ? 0.27731 0.84308 0.76163 0.00355  0.04155  -0.11638 216 PHE   A CG  
1785 C CD1 . PHE   A 219 ? 0.27498 0.80047 0.73152 -0.00353 0.03582  -0.09666 216 PHE   A CD1 
1786 C CD2 . PHE   A 219 ? 0.28619 0.89730 0.79273 -0.01418 0.05486  -0.12761 216 PHE   A CD2 
1787 C CE1 . PHE   A 219 ? 0.35214 0.87973 0.80260 -0.02550 0.04179  -0.08864 216 PHE   A CE1 
1788 C CE2 . PHE   A 219 ? 0.29410 0.90496 0.79268 -0.03856 0.06099  -0.11830 216 PHE   A CE2 
1789 C CZ  . PHE   A 219 ? 0.32921 0.89700 0.79958 -0.04299 0.05361  -0.09899 216 PHE   A CZ  
1790 N N   . ARG   A 220 ? 0.42908 0.92247 0.89092 0.07634  0.01335  -0.12908 217 ARG   A N   
1791 C CA  . ARG   A 220 ? 0.50026 0.98673 0.96776 0.10400  0.00042  -0.14247 217 ARG   A CA  
1792 C C   . ARG   A 220 ? 0.48273 0.91317 0.92125 0.11838  -0.01976 -0.12900 217 ARG   A C   
1793 O O   . ARG   A 220 ? 0.66552 1.08638 1.10769 0.14391  -0.03717 -0.13930 217 ARG   A O   
1794 C CB  . ARG   A 220 ? 0.49708 0.98478 0.96138 0.10363  0.01408  -0.15037 217 ARG   A CB  
1795 C CG  . ARG   A 220 ? 0.66266 1.20995 1.15846 0.09698  0.03120  -0.17049 217 ARG   A CG  
1796 C CD  . ARG   A 220 ? 0.63540 1.18314 1.12871 0.10463  0.04004  -0.18253 217 ARG   A CD  
1797 N NE  . ARG   A 220 ? 0.90615 1.42454 1.36959 0.08441  0.05427  -0.16708 217 ARG   A NE  
1798 C CZ  . ARG   A 220 ? 0.80499 1.34795 1.26930 0.06319  0.07546  -0.16923 217 ARG   A CZ  
1799 N NH1 . ARG   A 220 ? 0.82020 1.41866 1.31325 0.05635  0.08738  -0.18581 217 ARG   A NH1 
1800 N NH2 . ARG   A 220 ? 0.69826 1.20933 1.13283 0.04777  0.08461  -0.15476 217 ARG   A NH2 
1801 N N   . THR   A 221 ? 0.45559 0.84862 0.86438 0.10259  -0.01813 -0.10698 218 THR   A N   
1802 C CA  . THR   A 221 ? 0.46650 0.80574 0.84385 0.11121  -0.03442 -0.09281 218 THR   A CA  
1803 C C   . THR   A 221 ? 0.60770 0.94161 0.98143 0.11293  -0.04831 -0.08522 218 THR   A C   
1804 O O   . THR   A 221 ? 0.58387 0.89254 0.94692 0.13163  -0.06852 -0.08528 218 THR   A O   
1805 C CB  . THR   A 221 ? 0.55699 0.85955 0.90331 0.09298  -0.02379 -0.07479 218 THR   A CB  
1806 O OG1 . THR   A 221 ? 0.58269 0.89050 0.93148 0.09101  -0.01142 -0.08225 218 THR   A OG1 
1807 C CG2 . THR   A 221 ? 0.63557 0.88330 0.94835 0.09960  -0.03881 -0.06138 218 THR   A CG2 
1808 N N   . LEU   A 222 ? 0.50157 0.85598 0.88137 0.09396  -0.03886 -0.07881 219 LEU   A N   
1809 C CA  . LEU   A 222 ? 0.48929 0.83864 0.86377 0.09331  -0.05068 -0.07135 219 LEU   A CA  
1810 C C   . LEU   A 222 ? 0.47956 0.87677 0.88926 0.10036  -0.05671 -0.08755 219 LEU   A C   
1811 O O   . LEU   A 222 ? 0.56130 0.95835 0.96920 0.10035  -0.06749 -0.08345 219 LEU   A O   
1812 C CB  . LEU   A 222 ? 0.51073 0.84927 0.86767 0.06902  -0.03871 -0.05465 219 LEU   A CB  
1813 C CG  . LEU   A 222 ? 0.43414 0.73204 0.75947 0.05948  -0.03155 -0.03951 219 LEU   A CG  
1814 C CD1 . LEU   A 222 ? 0.47096 0.76691 0.78511 0.03777  -0.02000 -0.02709 219 LEU   A CD1 
1815 C CD2 . LEU   A 222 ? 0.66588 0.91831 0.96278 0.07146  -0.04759 -0.03075 219 LEU   A CD2 
1816 N N   . GLY   A 223 ? 0.42036 0.85994 0.86199 0.10578  -0.04992 -0.10665 220 GLY   A N   
1817 C CA  . GLY   A 223 ? 0.38224 0.87380 0.86078 0.10966  -0.05387 -0.12365 220 GLY   A CA  
1818 C C   . GLY   A 223 ? 0.32373 0.84783 0.81492 0.08201  -0.03575 -0.12199 220 GLY   A C   
1819 O O   . GLY   A 223 ? 0.40394 0.90361 0.87145 0.06274  -0.02762 -0.10457 220 GLY   A O   
1820 N N   . THR   A 224 ? 0.31476 0.89502 0.84357 0.07998  -0.02964 -0.14143 221 THR   A N   
1821 C CA  . THR   A 224 ? 0.43256 1.04461 0.97363 0.05250  -0.01379 -0.14143 221 THR   A CA  
1822 C C   . THR   A 224 ? 0.33275 0.93818 0.86915 0.04707  -0.02599 -0.13323 221 THR   A C   
1823 O O   . THR   A 224 ? 0.30324 0.92949 0.86000 0.06277  -0.04303 -0.14465 221 THR   A O   
1824 C CB  . THR   A 224 ? 0.37356 1.05056 0.95694 0.05046  -0.00422 -0.16586 221 THR   A CB  
1825 O OG1 . THR   A 224 ? 0.43170 1.11395 1.01707 0.05598  0.00762  -0.17414 221 THR   A OG1 
1826 C CG2 . THR   A 224 ? 0.37352 1.07869 0.96483 0.01811  0.01282  -0.16455 221 THR   A CG2 
1827 N N   . PRO   A 225 ? 0.34957 0.92735 0.85997 0.02651  -0.01895 -0.11510 222 PRO   A N   
1828 C CA  . PRO   A 225 ? 0.33666 0.90305 0.83843 0.02295  -0.03141 -0.10710 222 PRO   A CA  
1829 C C   . PRO   A 225 ? 0.38476 1.00029 0.91832 0.01090  -0.03046 -0.12075 222 PRO   A C   
1830 O O   . PRO   A 225 ? 0.39605 1.05057 0.95221 -0.00368 -0.01493 -0.13210 222 PRO   A O   
1831 C CB  . PRO   A 225 ? 0.39813 0.92445 0.86475 0.00419  -0.02134 -0.08650 222 PRO   A CB  
1832 C CG  . PRO   A 225 ? 0.43662 0.97197 0.90430 -0.01050 -0.00053 -0.08768 222 PRO   A CG  
1833 C CD  . PRO   A 225 ? 0.28848 0.84290 0.77500 0.00730  -0.00056 -0.10197 222 PRO   A CD  
1834 N N   . ASP   A 226 ? 0.32151 0.93451 0.85513 0.01593  -0.04738 -0.11971 223 ASP   A N   
1835 C CA  . ASP   A 226 ? 0.33882 0.99476 0.90044 0.00392  -0.04951 -0.13182 223 ASP   A CA  
1836 C C   . ASP   A 226 ? 0.33494 0.96181 0.87231 -0.00637 -0.05753 -0.11787 223 ASP   A C   
1837 O O   . ASP   A 226 ? 0.35254 0.93053 0.85337 -0.00532 -0.05883 -0.09985 223 ASP   A O   
1838 C CB  . ASP   A 226 ? 0.35143 1.04893 0.94971 0.02663  -0.06635 -0.15323 223 ASP   A CB  
1839 C CG  . ASP   A 226 ? 0.39256 1.05455 0.97282 0.05597  -0.09081 -0.14821 223 ASP   A CG  
1840 O OD1 . ASP   A 226 ? 0.52665 1.13420 1.06647 0.05629  -0.09320 -0.12803 223 ASP   A OD1 
1841 O OD2 . ASP   A 226 ? 0.56849 1.25718 1.17428 0.07862  -0.10801 -0.16507 223 ASP   A OD2 
1842 N N   . GLU   A 227 ? 0.32909 0.98837 0.88777 -0.01673 -0.06283 -0.12760 224 GLU   A N   
1843 C CA  . GLU   A 227 ? 0.33941 0.97382 0.87617 -0.02828 -0.06975 -0.11647 224 GLU   A CA  
1844 C C   . GLU   A 227 ? 0.46417 1.06212 0.97702 -0.00610 -0.09084 -0.10780 224 GLU   A C   
1845 O O   . GLU   A 227 ? 0.53703 1.09852 1.01866 -0.01264 -0.09356 -0.09357 224 GLU   A O   
1846 C CB  . GLU   A 227 ? 0.32369 1.00238 0.89009 -0.04412 -0.07226 -0.13067 224 GLU   A CB  
1847 C CG  . GLU   A 227 ? 0.42440 1.12498 1.00003 -0.07543 -0.05015 -0.13344 224 GLU   A CG  
1848 C CD  . GLU   A 227 ? 0.62900 1.28268 1.16522 -0.09528 -0.04082 -0.11424 224 GLU   A CD  
1849 O OE1 . GLU   A 227 ? 0.56274 1.17778 1.07149 -0.08806 -0.05256 -0.10229 224 GLU   A OE1 
1850 O OE2 . GLU   A 227 ? 0.55490 1.20999 1.08637 -0.11758 -0.02222 -0.11174 224 GLU   A OE2 
1851 N N   . VAL   A 228 ? 0.41996 1.02543 0.94459 0.02023  -0.10619 -0.11647 225 VAL   A N   
1852 C CA  . VAL   A 228 ? 0.55287 1.12063 1.05061 0.04041  -0.12738 -0.10793 225 VAL   A CA  
1853 C C   . VAL   A 228 ? 0.44152 0.95420 0.89687 0.04183  -0.12081 -0.08780 225 VAL   A C   
1854 O O   . VAL   A 228 ? 0.62672 1.10231 1.04866 0.03924  -0.12592 -0.07375 225 VAL   A O   
1855 C CB  . VAL   A 228 ? 0.51733 1.10459 1.03681 0.06918  -0.14779 -0.12323 225 VAL   A CB  
1856 C CG1 . VAL   A 228 ? 0.48380 1.02621 0.96914 0.08856  -0.17071 -0.11298 225 VAL   A CG1 
1857 C CG2 . VAL   A 228 ? 0.50634 1.15499 1.07210 0.06710  -0.15403 -0.14541 225 VAL   A CG2 
1858 N N   . VAL   A 229 ? 0.50012 1.00860 0.95660 0.04532  -0.10905 -0.08717 226 VAL   A N   
1859 C CA  . VAL   A 229 ? 0.47504 0.93472 0.89409 0.04564  -0.10266 -0.06956 226 VAL   A CA  
1860 C C   . VAL   A 229 ? 0.54274 0.98913 0.94521 0.02135  -0.08379 -0.05761 226 VAL   A C   
1861 O O   . VAL   A 229 ? 0.51427 0.92127 0.88397 0.01920  -0.08037 -0.04258 226 VAL   A O   
1862 C CB  . VAL   A 229 ? 0.53197 0.98943 0.95666 0.05848  -0.09831 -0.07373 226 VAL   A CB  
1863 C CG1 . VAL   A 229 ? 0.68020 1.15229 1.12343 0.08487  -0.11856 -0.08823 226 VAL   A CG1 
1864 C CG2 . VAL   A 229 ? 0.62266 1.11213 1.07054 0.04318  -0.07679 -0.08119 226 VAL   A CG2 
1865 N N   . TRP   A 230 ? 0.49875 0.97646 0.92199 0.00279  -0.07210 -0.06443 227 TRP   A N   
1866 C CA  . TRP   A 230 ? 0.41934 0.88248 0.82594 -0.01925 -0.05587 -0.05423 227 TRP   A CA  
1867 C C   . TRP   A 230 ? 0.39305 0.88354 0.81629 -0.03748 -0.05379 -0.06150 227 TRP   A C   
1868 O O   . TRP   A 230 ? 0.40233 0.92577 0.84939 -0.05012 -0.04267 -0.07134 227 TRP   A O   
1869 C CB  . TRP   A 230 ? 0.38611 0.84956 0.79378 -0.02533 -0.03818 -0.05300 227 TRP   A CB  
1870 C CG  . TRP   A 230 ? 0.45695 0.90061 0.84410 -0.04503 -0.02375 -0.04221 227 TRP   A CG  
1871 C CD1 . TRP   A 230 ? 0.50049 0.92644 0.86948 -0.05682 -0.02492 -0.03449 227 TRP   A CD1 
1872 C CD2 . TRP   A 230 ? 0.38519 0.82319 0.76657 -0.05348 -0.00769 -0.03893 227 TRP   A CD2 
1873 N NE1 . TRP   A 230 ? 0.43144 0.84060 0.78418 -0.07092 -0.01155 -0.02690 227 TRP   A NE1 
1874 C CE2 . TRP   A 230 ? 0.39695 0.81304 0.75645 -0.06957 -0.00093 -0.02903 227 TRP   A CE2 
1875 C CE3 . TRP   A 230 ? 0.44709 0.89544 0.83853 -0.04809 0.00064  -0.04414 227 TRP   A CE3 
1876 C CZ2 . TRP   A 230 ? 0.37476 0.77858 0.72177 -0.08007 0.01279  -0.02374 227 TRP   A CZ2 
1877 C CZ3 . TRP   A 230 ? 0.43691 0.87379 0.81564 -0.05986 0.01546  -0.03866 227 TRP   A CZ3 
1878 C CH2 . TRP   A 230 ? 0.59086 1.00548 0.94740 -0.07556 0.02093  -0.02831 227 TRP   A CH2 
1879 N N   . PRO   A 231 ? 0.43921 0.91638 0.84894 -0.04061 -0.06412 -0.05729 228 PRO   A N   
1880 C CA  . PRO   A 231 ? 0.44122 0.94173 0.86538 -0.05864 -0.06416 -0.06469 228 PRO   A CA  
1881 C C   . PRO   A 231 ? 0.37259 0.86840 0.78952 -0.08288 -0.04599 -0.06030 228 PRO   A C   
1882 O O   . PRO   A 231 ? 0.52081 0.98083 0.90849 -0.08712 -0.03957 -0.04743 228 PRO   A O   
1883 C CB  . PRO   A 231 ? 0.49681 0.97212 0.89832 -0.05486 -0.07886 -0.05832 228 PRO   A CB  
1884 C CG  . PRO   A 231 ? 0.53418 0.98680 0.91975 -0.03141 -0.09017 -0.05250 228 PRO   A CG  
1885 C CD  . PRO   A 231 ? 0.42530 0.86665 0.80570 -0.02784 -0.07705 -0.04687 228 PRO   A CD  
1886 N N   . GLY   A 232 ? 0.46745 1.00011 0.91062 -0.09906 -0.03814 -0.07178 229 GLY   A N   
1887 C CA  . GLY   A 232 ? 0.47342 1.00128 0.90793 -0.12424 -0.02182 -0.06829 229 GLY   A CA  
1888 C C   . GLY   A 232 ? 0.42962 0.96486 0.86802 -0.12719 -0.00515 -0.06856 229 GLY   A C   
1889 O O   . GLY   A 232 ? 0.61261 1.13884 1.03852 -0.14801 0.00830  -0.06432 229 GLY   A O   
1890 N N   . VAL   A 233 ? 0.47574 1.02427 0.92844 -0.10692 -0.00654 -0.07358 230 VAL   A N   
1891 C CA  . VAL   A 233 ? 0.43403 0.98764 0.88852 -0.10822 0.00878  -0.07437 230 VAL   A CA  
1892 C C   . VAL   A 233 ? 0.49353 1.09119 0.97382 -0.12772 0.02224  -0.08797 230 VAL   A C   
1893 O O   . VAL   A 233 ? 0.37168 0.96634 0.84276 -0.14185 0.03857  -0.08551 230 VAL   A O   
1894 C CB  . VAL   A 233 ? 0.38228 0.93634 0.84425 -0.08082 0.00213  -0.07740 230 VAL   A CB  
1895 C CG1 . VAL   A 233 ? 0.34548 0.94188 0.84332 -0.06654 -0.00944 -0.09492 230 VAL   A CG1 
1896 C CG2 . VAL   A 233 ? 0.33091 0.88403 0.78999 -0.08157 0.01734  -0.07728 230 VAL   A CG2 
1897 N N   . THR   A 234 ? 0.31111 0.95101 0.82303 -0.13005 0.01590  -0.10288 231 THR   A N   
1898 C CA  . THR   A 234 ? 0.40611 1.07028 0.92906 -0.14503 0.02839  -0.11212 231 THR   A CA  
1899 C C   . THR   A 234 ? 0.40288 1.04835 0.90352 -0.17619 0.03844  -0.10428 231 THR   A C   
1900 O O   . THR   A 234 ? 0.51388 1.17201 1.01543 -0.19205 0.05124  -0.10931 231 THR   A O   
1901 C CB  . THR   A 234 ? 0.57441 1.27658 1.12897 -0.13424 0.01705  -0.12809 231 THR   A CB  
1902 O OG1 . THR   A 234 ? 0.50338 1.20183 1.05805 -0.13947 0.00280  -0.12651 231 THR   A OG1 
1903 C CG2 . THR   A 234 ? 0.54193 1.25878 1.11580 -0.10175 0.00540  -0.13671 231 THR   A CG2 
1904 N N   . SER   A 235 ? 0.48568 1.10082 0.96489 -0.18524 0.03244  -0.09280 232 SER   A N   
1905 C CA  . SER   A 235 ? 0.60960 1.19980 1.06338 -0.21359 0.03927  -0.08488 232 SER   A CA  
1906 C C   . SER   A 235 ? 0.65715 1.20930 1.07762 -0.22237 0.04969  -0.07105 232 SER   A C   
1907 O O   . SER   A 235 ? 0.63953 1.16367 1.03345 -0.24469 0.05387  -0.06327 232 SER   A O   
1908 C CB  . SER   A 235 ? 0.51637 1.09648 0.96624 -0.21927 0.02412  -0.08288 232 SER   A CB  
1909 O OG  . SER   A 235 ? 0.68462 1.29896 1.16423 -0.21074 0.01278  -0.09584 232 SER   A OG  
1910 N N   . MET   A 236 ? 0.53991 1.08840 0.95971 -0.20518 0.05281  -0.06807 233 MET   A N   
1911 C CA  . MET   A 236 ? 0.54119 1.04684 0.92572 -0.20805 0.06011  -0.05411 233 MET   A CA  
1912 C C   . MET   A 236 ? 0.59565 1.10450 0.97070 -0.22790 0.07747  -0.05534 233 MET   A C   
1913 O O   . MET   A 236 ? 0.63715 1.17614 1.03111 -0.22717 0.08417  -0.06629 233 MET   A O   
1914 C CB  . MET   A 236 ? 0.51156 1.00408 0.89341 -0.18049 0.05644  -0.04971 233 MET   A CB  
1915 C CG  . MET   A 236 ? 0.55355 1.03467 0.93704 -0.15867 0.03912  -0.04694 233 MET   A CG  
1916 S SD  . MET   A 236 ? 0.67261 1.12378 1.04015 -0.13286 0.03522  -0.03739 233 MET   A SD  
1917 C CE  . MET   A 236 ? 0.64967 1.05391 0.97731 -0.14469 0.04068  -0.02238 233 MET   A CE  
1918 N N   . PRO   A 237 ? 0.58269 1.05372 0.92284 -0.24277 0.08328  -0.04350 234 PRO   A N   
1919 C CA  . PRO   A 237 ? 0.68439 1.14665 1.00508 -0.26168 0.09730  -0.04266 234 PRO   A CA  
1920 C C   . PRO   A 237 ? 0.59839 1.08326 0.93070 -0.25169 0.10868  -0.04985 234 PRO   A C   
1921 O O   . PRO   A 237 ? 0.62832 1.12996 0.96246 -0.26361 0.11907  -0.05688 234 PRO   A O   
1922 C CB  . PRO   A 237 ? 0.60183 1.01487 0.88141 -0.27358 0.09721  -0.02782 234 PRO   A CB  
1923 C CG  . PRO   A 237 ? 0.64487 1.03582 0.91936 -0.26318 0.08098  -0.02189 234 PRO   A CG  
1924 C CD  . PRO   A 237 ? 0.63151 1.05271 0.93933 -0.23718 0.07363  -0.02930 234 PRO   A CD  
1925 N N   . ASP   A 238 ? 0.54792 1.03392 0.88718 -0.23102 0.10712  -0.04894 235 ASP   A N   
1926 C CA  . ASP   A 238 ? 0.59667 1.10053 0.94454 -0.22109 0.11707  -0.05603 235 ASP   A CA  
1927 C C   . ASP   A 238 ? 0.55131 1.09764 0.93843 -0.20102 0.11294  -0.07099 235 ASP   A C   
1928 O O   . ASP   A 238 ? 0.50970 1.07262 0.90669 -0.18979 0.11947  -0.07879 235 ASP   A O   
1929 C CB  . ASP   A 238 ? 0.52083 0.99979 0.85167 -0.21106 0.11811  -0.04731 235 ASP   A CB  
1930 C CG  . ASP   A 238 ? 0.73486 1.17373 1.02528 -0.22987 0.12349  -0.03466 235 ASP   A CG  
1931 O OD1 . ASP   A 238 ? 0.85483 1.28900 1.12901 -0.24943 0.13192  -0.03500 235 ASP   A OD1 
1932 O OD2 . ASP   A 238 ? 0.90899 1.31529 1.17991 -0.22213 0.11716  -0.02401 235 ASP   A OD2 
1933 N N   . TYR   A 239 ? 0.55468 1.11807 0.96329 -0.19565 0.10122  -0.07588 236 TYR   A N   
1934 C CA  . TYR   A 239 ? 0.50798 1.11094 0.95264 -0.17623 0.09520  -0.09103 236 TYR   A CA  
1935 C C   . TYR   A 239 ? 0.43477 1.06915 0.89204 -0.18669 0.10545  -0.10394 236 TYR   A C   
1936 O O   . TYR   A 239 ? 0.55962 1.19089 1.00542 -0.21025 0.11141  -0.10219 236 TYR   A O   
1937 C CB  . TYR   A 239 ? 0.47819 1.08934 0.93999 -0.16750 0.07811  -0.09268 236 TYR   A CB  
1938 C CG  . TYR   A 239 ? 0.53221 1.18180 1.02961 -0.14583 0.06872  -0.10863 236 TYR   A CG  
1939 C CD1 . TYR   A 239 ? 0.46347 1.11584 0.97309 -0.11889 0.05883  -0.11161 236 TYR   A CD1 
1940 C CD2 . TYR   A 239 ? 0.50949 1.19160 1.02729 -0.15208 0.06879  -0.12129 236 TYR   A CD2 
1941 C CE1 . TYR   A 239 ? 0.36418 1.04741 0.90348 -0.09710 0.04777  -0.12655 236 TYR   A CE1 
1942 C CE2 . TYR   A 239 ? 0.53780 1.25445 1.08738 -0.13076 0.05867  -0.13681 236 TYR   A CE2 
1943 C CZ  . TYR   A 239 ? 0.49511 1.21054 1.05435 -0.10252 0.04746  -0.13926 236 TYR   A CZ  
1944 O OH  . TYR   A 239 ? 0.56565 1.31106 1.15356 -0.07944 0.03506  -0.15497 236 TYR   A OH  
1945 N N   . LYS   A 240 ? 0.40637 1.07117 0.88678 -0.16920 0.10725  -0.11779 237 LYS   A N   
1946 C CA  . LYS   A 240 ? 0.55958 1.26082 1.05610 -0.17606 0.11667  -0.13309 237 LYS   A CA  
1947 C C   . LYS   A 240 ? 0.59911 1.33883 1.13372 -0.15216 0.10467  -0.14995 237 LYS   A C   
1948 O O   . LYS   A 240 ? 0.52494 1.26407 1.07012 -0.12631 0.09535  -0.15269 237 LYS   A O   
1949 C CB  . LYS   A 240 ? 0.57800 1.27946 1.06171 -0.17948 0.13282  -0.13598 237 LYS   A CB  
1950 C CG  . LYS   A 240 ? 0.67261 1.33394 1.11593 -0.20135 0.14332  -0.11976 237 LYS   A CG  
1951 C CD  . LYS   A 240 ? 0.93978 1.60367 1.37055 -0.20427 0.15845  -0.12401 237 LYS   A CD  
1952 C CE  . LYS   A 240 ? 0.85002 1.47067 1.23825 -0.22358 0.16640  -0.10754 237 LYS   A CE  
1953 N NZ  . LYS   A 240 ? 0.94953 1.55556 1.31768 -0.25135 0.16930  -0.10040 237 LYS   A NZ  
1954 N N   . PRO   A 241 ? 0.64034 1.41279 1.19537 -0.15943 0.10348  -0.16194 238 PRO   A N   
1955 C CA  . PRO   A 241 ? 0.66431 1.47465 1.25546 -0.13540 0.09103  -0.17982 238 PRO   A CA  
1956 C C   . PRO   A 241 ? 0.61311 1.44634 1.21836 -0.11675 0.09623  -0.19465 238 PRO   A C   
1957 O O   . PRO   A 241 ? 0.44996 1.30671 1.08168 -0.09101 0.08313  -0.20871 238 PRO   A O   
1958 C CB  . PRO   A 241 ? 0.61977 1.46068 1.22601 -0.15341 0.09289  -0.18957 238 PRO   A CB  
1959 C CG  . PRO   A 241 ? 0.74019 1.54957 1.31709 -0.18346 0.09968  -0.17302 238 PRO   A CG  
1960 C CD  . PRO   A 241 ? 0.49605 1.26977 1.04099 -0.18974 0.11142  -0.15945 238 PRO   A CD  
1961 N N   . SER   A 242 ? 0.58378 1.40929 1.17077 -0.12805 0.11365  -0.19255 239 SER   A N   
1962 C CA  . SER   A 242 ? 0.46220 1.30858 1.06027 -0.11189 0.11974  -0.20733 239 SER   A CA  
1963 C C   . SER   A 242 ? 0.45215 1.27299 1.04362 -0.08772 0.11232  -0.20192 239 SER   A C   
1964 O O   . SER   A 242 ? 0.55485 1.38585 1.15049 -0.07488 0.11781  -0.21253 239 SER   A O   
1965 C CB  . SER   A 242 ? 0.65156 1.50236 1.23159 -0.13604 0.14190  -0.20858 239 SER   A CB  
1966 O OG  . SER   A 242 ? 0.84340 1.65014 1.38672 -0.15268 0.14943  -0.18814 239 SER   A OG  
1967 N N   . PHE   A 243 ? 0.39247 1.18125 0.97351 -0.08188 0.10028  -0.18663 240 PHE   A N   
1968 C CA  . PHE   A 243 ? 0.53386 1.29956 1.10981 -0.05936 0.09239  -0.18219 240 PHE   A CA  
1969 C C   . PHE   A 243 ? 0.48947 1.27885 1.09363 -0.02700 0.07806  -0.20057 240 PHE   A C   
1970 O O   . PHE   A 243 ? 0.54637 1.35531 1.17131 -0.01721 0.06416  -0.20885 240 PHE   A O   
1971 C CB  . PHE   A 243 ? 0.48572 1.21737 1.04766 -0.05964 0.08110  -0.16417 240 PHE   A CB  
1972 C CG  . PHE   A 243 ? 0.53492 1.23444 1.06469 -0.08573 0.09315  -0.14567 240 PHE   A CG  
1973 C CD1 . PHE   A 243 ? 0.57284 1.26770 1.08420 -0.10287 0.11143  -0.14412 240 PHE   A CD1 
1974 C CD2 . PHE   A 243 ? 0.53703 1.20980 1.05330 -0.09215 0.08501  -0.13048 240 PHE   A CD2 
1975 C CE1 . PHE   A 243 ? 0.59656 1.25817 1.07570 -0.12497 0.12001  -0.12731 240 PHE   A CE1 
1976 C CE2 . PHE   A 243 ? 0.53499 1.17634 1.02064 -0.11414 0.09427  -0.11454 240 PHE   A CE2 
1977 C CZ  . PHE   A 243 ? 0.54278 1.17726 1.00940 -0.13002 0.11108  -0.11273 240 PHE   A CZ  
1978 N N   . PRO   A 244 ? 0.51202 1.29883 1.11654 -0.00921 0.07974  -0.20804 241 PRO   A N   
1979 C CA  . PRO   A 244 ? 0.46250 1.26578 1.09061 0.02399  0.06364  -0.22585 241 PRO   A CA  
1980 C C   . PRO   A 244 ? 0.47522 1.25667 1.10595 0.04519  0.03988  -0.21923 241 PRO   A C   
1981 O O   . PRO   A 244 ? 0.47053 1.21966 1.08309 0.03967  0.03738  -0.20150 241 PRO   A O   
1982 C CB  . PRO   A 244 ? 0.59509 1.39005 1.21547 0.03517  0.07163  -0.23166 241 PRO   A CB  
1983 C CG  . PRO   A 244 ? 0.59975 1.38969 1.19823 0.00435  0.09539  -0.22245 241 PRO   A CG  
1984 C CD  . PRO   A 244 ? 0.55556 1.32500 1.13812 -0.01884 0.09631  -0.20236 241 PRO   A CD  
1985 N N   . LYS   A 245 ? 0.38059 1.17968 1.03299 0.06996  0.02156  -0.23433 242 LYS   A N   
1986 C CA  . LYS   A 245 ? 0.37322 1.15151 1.02669 0.09227  -0.00405 -0.22978 242 LYS   A CA  
1987 C C   . LYS   A 245 ? 0.46649 1.21820 1.11389 0.12257  -0.01699 -0.23304 242 LYS   A C   
1988 O O   . LYS   A 245 ? 0.65716 1.42145 1.31698 0.14518  -0.02413 -0.25108 242 LYS   A O   
1989 C CB  . LYS   A 245 ? 0.38791 1.19449 1.06400 0.10329  -0.01939 -0.24374 242 LYS   A CB  
1990 C CG  . LYS   A 245 ? 0.34742 1.17992 1.03055 0.07392  -0.00822 -0.24192 242 LYS   A CG  
1991 C CD  . LYS   A 245 ? 0.32729 1.13199 0.99060 0.05385  -0.00721 -0.21968 242 LYS   A CD  
1992 C CE  . LYS   A 245 ? 0.45263 1.27851 1.12125 0.02617  0.00111  -0.21843 242 LYS   A CE  
1993 N NZ  . LYS   A 245 ? 0.48418 1.28137 1.13249 0.00795  0.00052  -0.19815 242 LYS   A NZ  
1994 N N   . TRP   A 246 ? 0.33485 1.04885 0.96253 0.12304  -0.02058 -0.21633 243 TRP   A N   
1995 C CA  . TRP   A 246 ? 0.45838 1.12408 1.06312 0.14787  -0.03498 -0.21184 243 TRP   A CA  
1996 C C   . TRP   A 246 ? 0.54480 1.16622 1.12769 0.16186  -0.06043 -0.19811 243 TRP   A C   
1997 O O   . TRP   A 246 ? 0.56774 1.17891 1.13933 0.14543  -0.06126 -0.18312 243 TRP   A O   
1998 C CB  . TRP   A 246 ? 0.47497 1.09795 1.04411 0.13189  -0.01898 -0.19387 243 TRP   A CB  
1999 C CG  . TRP   A 246 ? 0.55046 1.20550 1.13295 0.12376  0.00282  -0.20743 243 TRP   A CG  
2000 C CD1 . TRP   A 246 ? 0.42971 1.09779 1.02497 0.14502  0.00173  -0.22683 243 TRP   A CD1 
2001 C CD2 . TRP   A 246 ? 0.54769 1.22265 1.12837 0.09221  0.02844  -0.20264 243 TRP   A CD2 
2002 N NE1 . TRP   A 246 ? 0.57558 1.27335 1.17784 0.12796  0.02632  -0.23477 243 TRP   A NE1 
2003 C CE2 . TRP   A 246 ? 0.57051 1.27159 1.16266 0.09498  0.04280  -0.21950 243 TRP   A CE2 
2004 C CE3 . TRP   A 246 ? 0.48073 1.15141 1.04881 0.06244  0.03966  -0.18610 243 TRP   A CE3 
2005 C CZ2 . TRP   A 246 ? 0.53350 1.24705 1.11594 0.06691  0.06746  -0.21652 243 TRP   A CZ2 
2006 C CZ3 . TRP   A 246 ? 0.63888 1.32773 1.20390 0.03635  0.06349  -0.18569 243 TRP   A CZ3 
2007 C CH2 . TRP   A 246 ? 0.52083 1.22661 1.08902 0.03804  0.07689  -0.19914 243 TRP   A CH2 
2008 N N   . ALA   A 247 ? 0.53599 1.12877 1.11024 0.19231  -0.08164 -0.20354 244 ALA   A N   
2009 C CA  . ALA   A 247 ? 0.60858 1.15320 1.15611 0.20690  -0.10711 -0.19054 244 ALA   A CA  
2010 C C   . ALA   A 247 ? 0.55920 1.03488 1.05655 0.19537  -0.10430 -0.16349 244 ALA   A C   
2011 O O   . ALA   A 247 ? 0.63444 1.09112 1.11799 0.19105  -0.09225 -0.16030 244 ALA   A O   
2012 C CB  . ALA   A 247 ? 0.45419 0.99412 1.01098 0.24513  -0.13342 -0.20848 244 ALA   A CB  
2013 N N   . ARG   A 248 ? 0.49584 0.93638 0.96639 0.18980  -0.11521 -0.14505 245 ARG   A N   
2014 C CA  . ARG   A 248 ? 0.55046 0.92941 0.97456 0.17806  -0.11287 -0.12041 245 ARG   A CA  
2015 C C   . ARG   A 248 ? 0.65715 0.98722 1.05589 0.19974  -0.12836 -0.11996 245 ARG   A C   
2016 O O   . ARG   A 248 ? 0.80653 1.12669 1.20637 0.22616  -0.15222 -0.12951 245 ARG   A O   
2017 C CB  . ARG   A 248 ? 0.52292 0.87864 0.92472 0.16926  -0.12208 -0.10355 245 ARG   A CB  
2018 C CG  . ARG   A 248 ? 0.60001 0.89802 0.95555 0.15519  -0.11827 -0.07926 245 ARG   A CG  
2019 C CD  . ARG   A 248 ? 0.80285 1.08058 1.13641 0.14875  -0.12815 -0.06515 245 ARG   A CD  
2020 N NE  . ARG   A 248 ? 0.83988 1.06842 1.13124 0.13384  -0.12266 -0.04362 245 ARG   A NE  
2021 C CZ  . ARG   A 248 ? 0.77845 1.01018 1.06304 0.10977  -0.10408 -0.03236 245 ARG   A CZ  
2022 N NH1 . ARG   A 248 ? 0.69542 0.97057 1.00792 0.09673  -0.08966 -0.03850 245 ARG   A NH1 
2023 N NH2 . ARG   A 248 ? 0.80934 0.99929 1.05748 0.09826  -0.10033 -0.01514 245 ARG   A NH2 
2024 N N   . GLN   A 249 ? 0.72990 1.02785 1.10479 0.18880  -0.11605 -0.10940 246 GLN   A N   
2025 C CA  . GLN   A 249 ? 0.78207 1.02997 1.13013 0.20586  -0.12927 -0.10839 246 GLN   A CA  
2026 C C   . GLN   A 249 ? 0.83509 1.01970 1.13660 0.20353  -0.14408 -0.08695 246 GLN   A C   
2027 O O   . GLN   A 249 ? 0.76268 0.93723 1.04711 0.18155  -0.13529 -0.06934 246 GLN   A O   
2028 C CB  . GLN   A 249 ? 0.76540 1.00613 1.10746 0.19420  -0.11027 -0.10727 246 GLN   A CB  
2029 C CG  . GLN   A 249 ? 0.83239 1.13125 1.21464 0.19583  -0.09464 -0.12850 246 GLN   A CG  
2030 C CD  . GLN   A 249 ? 1.03344 1.32032 1.40520 0.18586  -0.07805 -0.12741 246 GLN   A CD  
2031 O OE1 . GLN   A 249 ? 1.06340 1.29849 1.39996 0.17971  -0.07997 -0.11230 246 GLN   A OE1 
2032 N NE2 . GLN   A 249 ? 1.10859 1.44408 1.51007 0.18302  -0.06147 -0.14389 246 GLN   A NE2 
2033 N N   . ASP   A 250 ? 0.85042 0.99121 1.12972 0.22650  -0.16700 -0.08923 247 ASP   A N   
2034 C CA  . ASP   A 250 ? 0.91406 0.98844 1.14314 0.22341  -0.18135 -0.06885 247 ASP   A CA  
2035 C C   . ASP   A 250 ? 0.86958 0.91002 1.06891 0.19817  -0.16385 -0.05125 247 ASP   A C   
2036 O O   . ASP   A 250 ? 0.96868 1.00473 1.17046 0.19819  -0.15535 -0.05694 247 ASP   A O   
2037 C CB  . ASP   A 250 ? 1.10141 1.13187 1.31049 0.25394  -0.21067 -0.07610 247 ASP   A CB  
2038 C CG  . ASP   A 250 ? 1.20890 1.17518 1.36669 0.25305  -0.22999 -0.05665 247 ASP   A CG  
2039 O OD1 . ASP   A 250 ? 1.30837 1.24794 1.43570 0.22632  -0.21758 -0.03559 247 ASP   A OD1 
2040 O OD2 . ASP   A 250 ? 1.39172 1.33453 1.53878 0.27941  -0.25804 -0.06315 247 ASP   A OD2 
2041 N N   . PHE   A 251 ? 0.86050 0.87905 1.03244 0.17678  -0.15857 -0.03111 248 PHE   A N   
2042 C CA  . PHE   A 251 ? 0.98503 0.97658 1.13124 0.15195  -0.14203 -0.01543 248 PHE   A CA  
2043 C C   . PHE   A 251 ? 1.10364 1.03258 1.21104 0.15674  -0.15355 -0.00949 248 PHE   A C   
2044 O O   . PHE   A 251 ? 1.10427 1.01314 1.19392 0.13731  -0.14018 0.00024  248 PHE   A O   
2045 C CB  . PHE   A 251 ? 0.93392 0.91914 1.06055 0.12972  -0.13467 0.00250  248 PHE   A CB  
2046 C CG  . PHE   A 251 ? 0.75215 0.79090 0.91010 0.11393  -0.11433 0.00065  248 PHE   A CG  
2047 C CD1 . PHE   A 251 ? 0.79525 0.88621 0.99619 0.12190  -0.10828 -0.01627 248 PHE   A CD1 
2048 C CD2 . PHE   A 251 ? 0.75066 0.78659 0.89361 0.09066  -0.10127 0.01516  248 PHE   A CD2 
2049 C CE1 . PHE   A 251 ? 0.79895 0.93282 1.02362 0.10579  -0.09054 -0.01699 248 PHE   A CE1 
2050 C CE2 . PHE   A 251 ? 0.72208 0.80156 0.89050 0.07750  -0.08474 0.01327  248 PHE   A CE2 
2051 C CZ  . PHE   A 251 ? 0.80743 0.93314 1.01488 0.08444  -0.07978 -0.00197 248 PHE   A CZ  
2052 N N   . SER   A 252 ? 1.18220 1.07871 1.27522 0.18194  -0.17897 -0.01555 249 SER   A N   
2053 C CA  . SER   A 252 ? 1.26005 1.09543 1.31721 0.18860  -0.19134 -0.01259 249 SER   A CA  
2054 C C   . SER   A 252 ? 1.18765 1.03941 1.26674 0.19317  -0.18080 -0.02677 249 SER   A C   
2055 O O   . SER   A 252 ? 1.28427 1.08906 1.33429 0.18915  -0.18324 -0.02213 249 SER   A O   
2056 C CB  . SER   A 252 ? 1.32401 1.12106 1.36179 0.21831  -0.22354 -0.01809 249 SER   A CB  
2057 O OG  . SER   A 252 ? 1.50628 1.28201 1.51735 0.21345  -0.23446 -0.00392 249 SER   A OG  
2058 N N   . LYS   A 253 ? 1.06211 0.97849 1.18987 0.20018  -0.16901 -0.04411 250 LYS   A N   
2059 C CA  . LYS   A 253 ? 1.11177 1.05023 1.26111 0.20184  -0.15567 -0.05780 250 LYS   A CA  
2060 C C   . LYS   A 253 ? 1.01364 0.98613 1.17697 0.17320  -0.12702 -0.05115 250 LYS   A C   
2061 O O   . LYS   A 253 ? 1.13713 1.10577 1.29935 0.16620  -0.11577 -0.05414 250 LYS   A O   
2062 C CB  . LYS   A 253 ? 1.06334 1.05165 1.25609 0.22880  -0.16094 -0.08384 250 LYS   A CB  
2063 C CG  . LYS   A 253 ? 1.30106 1.26144 1.48538 0.26223  -0.19154 -0.09470 250 LYS   A CG  
2064 C CD  . LYS   A 253 ? 1.40043 1.41409 1.63063 0.28921  -0.19460 -0.12410 250 LYS   A CD  
2065 C CE  . LYS   A 253 ? 1.36684 1.45802 1.64368 0.28032  -0.17778 -0.13231 250 LYS   A CE  
2066 N NZ  . LYS   A 253 ? 1.16540 1.25955 1.44010 0.28021  -0.18988 -0.12358 250 LYS   A NZ  
2067 N N   . VAL   A 254 ? 0.86173 0.86545 1.03673 0.15749  -0.11640 -0.04280 251 VAL   A N   
2068 C CA  . VAL   A 254 ? 0.89084 0.92225 1.07574 0.13157  -0.09172 -0.03602 251 VAL   A CA  
2069 C C   . VAL   A 254 ? 0.95246 0.93948 1.10093 0.11084  -0.08649 -0.01832 251 VAL   A C   
2070 O O   . VAL   A 254 ? 0.96143 0.95197 1.11073 0.09776  -0.07205 -0.01798 251 VAL   A O   
2071 C CB  . VAL   A 254 ? 0.78887 0.86062 0.99321 0.12175  -0.08426 -0.03245 251 VAL   A CB  
2072 C CG1 . VAL   A 254 ? 0.73019 0.82458 0.94081 0.09654  -0.06125 -0.02527 251 VAL   A CG1 
2073 C CG2 . VAL   A 254 ? 0.84257 0.96245 1.08544 0.13962  -0.08836 -0.05140 251 VAL   A CG2 
2074 N N   . VAL   A 255 ? 0.88143 0.82727 0.99697 0.10675  -0.09811 -0.00399 252 VAL   A N   
2075 C CA  . VAL   A 255 ? 0.91149 0.81441 0.99060 0.08599  -0.09402 0.01213  252 VAL   A CA  
2076 C C   . VAL   A 255 ? 1.06129 0.90149 1.10123 0.09642  -0.11579 0.01732  252 VAL   A C   
2077 O O   . VAL   A 255 ? 1.13922 0.95172 1.15176 0.09227  -0.12534 0.02967  252 VAL   A O   
2078 C CB  . VAL   A 255 ? 0.92267 0.83748 0.99521 0.06368  -0.08261 0.02655  252 VAL   A CB  
2079 C CG1 . VAL   A 255 ? 0.86190 0.81896 0.95936 0.04773  -0.06051 0.02457  252 VAL   A CG1 
2080 C CG2 . VAL   A 255 ? 0.80477 0.73798 0.88650 0.07358  -0.09150 0.02620  252 VAL   A CG2 
2081 N N   . PRO   A 256 ? 1.06490 0.87861 1.09821 0.11010  -0.12488 0.00815  253 PRO   A N   
2082 C CA  . PRO   A 256 ? 1.07171 0.81933 1.06441 0.12201  -0.14840 0.01235  253 PRO   A CA  
2083 C C   . PRO   A 256 ? 1.14121 0.83787 1.08666 0.09623  -0.14767 0.03359  253 PRO   A C   
2084 O O   . PRO   A 256 ? 1.14759 0.80216 1.05891 0.09979  -0.16459 0.04333  253 PRO   A O   
2085 C CB  . PRO   A 256 ? 1.12056 0.85431 1.11751 0.13611  -0.15254 -0.00208 253 PRO   A CB  
2086 C CG  . PRO   A 256 ? 1.07496 0.87776 1.12298 0.14392  -0.13757 -0.01913 253 PRO   A CG  
2087 C CD  . PRO   A 256 ? 1.01854 0.86361 1.08269 0.11948  -0.11628 -0.00910 253 PRO   A CD  
2088 N N   . PRO   A 257 ? 1.13545 0.83380 1.07579 0.06950  -0.12903 0.04093  254 PRO   A N   
2089 C CA  . PRO   A 257 ? 1.12794 0.77910 1.02314 0.04355  -0.12801 0.05957  254 PRO   A CA  
2090 C C   . PRO   A 257 ? 1.23086 0.89218 1.11604 0.03030  -0.12378 0.07260  254 PRO   A C   
2091 O O   . PRO   A 257 ? 1.16203 0.78218 1.00586 0.01038  -0.12489 0.08775  254 PRO   A O   
2092 C CB  . PRO   A 257 ? 1.14674 0.81318 1.05050 0.02004  -0.10763 0.06012  254 PRO   A CB  
2093 C CG  . PRO   A 257 ? 1.14967 0.85050 1.09084 0.03756  -0.10392 0.04214  254 PRO   A CG  
2094 C CD  . PRO   A 257 ? 1.02907 0.76974 1.00115 0.06038  -0.10879 0.03271  254 PRO   A CD  
2095 N N   . LEU   A 258 ? 1.15150 0.86509 1.07120 0.03945  -0.11875 0.06689  255 LEU   A N   
2096 C CA  . LEU   A 258 ? 1.12392 0.85094 1.03628 0.02676  -0.11344 0.07774  255 LEU   A CA  
2097 C C   . LEU   A 258 ? 1.15976 0.84587 1.03935 0.03978  -0.13601 0.08402  255 LEU   A C   
2098 O O   . LEU   A 258 ? 1.13895 0.81872 1.02641 0.06741  -0.15482 0.07398  255 LEU   A O   
2099 C CB  . LEU   A 258 ? 1.02202 0.81647 0.98138 0.03109  -0.10086 0.06897  255 LEU   A CB  
2100 C CG  . LEU   A 258 ? 1.04875 0.87165 1.01169 0.00742  -0.08215 0.07755  255 LEU   A CG  
2101 C CD1 . LEU   A 258 ? 0.91463 0.72485 0.86281 -0.01721 -0.06790 0.08423  255 LEU   A CD1 
2102 C CD2 . LEU   A 258 ? 0.83873 0.72269 0.84718 0.01212  -0.07052 0.06750  255 LEU   A CD2 
2103 N N   . ASP   A 259 ? 1.18765 0.84698 1.02986 0.01999  -0.13434 0.09985  256 ASP   A N   
2104 C CA  . ASP   A 259 ? 1.23791 0.85240 1.04058 0.02880  -0.15556 0.10828  256 ASP   A CA  
2105 C C   . ASP   A 259 ? 1.23932 0.89560 1.06652 0.04147  -0.15851 0.10392  256 ASP   A C   
2106 O O   . ASP   A 259 ? 1.03288 0.74907 0.90824 0.04634  -0.14655 0.09300  256 ASP   A O   
2107 C CB  . ASP   A 259 ? 1.33085 0.89775 1.07933 -0.00023 -0.15133 0.12701  256 ASP   A CB  
2108 C CG  . ASP   A 259 ? 1.44454 1.05347 1.20438 -0.02710 -0.12592 0.13270  256 ASP   A CG  
2109 O OD1 . ASP   A 259 ? 1.41056 1.04509 1.17680 -0.02518 -0.12464 0.13414  256 ASP   A OD1 
2110 O OD2 . ASP   A 259 ? 1.63756 1.25433 1.40027 -0.04930 -0.10809 0.13462  256 ASP   A OD2 
2111 N N   . GLU   A 260 ? 1.06853 0.69073 0.85969 0.04580  -0.17517 0.11276  257 GLU   A N   
2112 C CA  . GLU   A 260 ? 1.18258 0.83937 0.99364 0.05919  -0.18152 0.10807  257 GLU   A CA  
2113 C C   . GLU   A 260 ? 1.08763 0.79383 0.91931 0.03823  -0.15751 0.11092  257 GLU   A C   
2114 O O   . GLU   A 260 ? 1.03833 0.79830 0.91326 0.04704  -0.15232 0.10033  257 GLU   A O   
2115 C CB  . GLU   A 260 ? 1.19057 0.79402 0.95191 0.06715  -0.20568 0.11796  257 GLU   A CB  
2116 C CG  . GLU   A 260 ? 1.35387 0.98904 1.12972 0.07814  -0.21298 0.11447  257 GLU   A CG  
2117 C CD  . GLU   A 260 ? 1.69749 1.27645 1.41947 0.08553  -0.23787 0.12488  257 GLU   A CD  
2118 O OE1 . GLU   A 260 ? 1.72065 1.23388 1.39580 0.08658  -0.25272 0.13330  257 GLU   A OE1 
2119 O OE2 . GLU   A 260 ? 1.76358 1.36136 1.48752 0.08992  -0.24341 0.12479  257 GLU   A OE2 
2120 N N   . ASP   A 261 ? 1.00253 0.69120 0.80318 0.01010  -0.14295 0.12434  258 ASP   A N   
2121 C CA  . ASP   A 261 ? 0.86720 0.60147 0.68610 -0.00831 -0.12102 0.12565  258 ASP   A CA  
2122 C C   . ASP   A 261 ? 0.86732 0.65352 0.73632 -0.01047 -0.10265 0.11466  258 ASP   A C   
2123 O O   . ASP   A 261 ? 0.80705 0.64035 0.70582 -0.01330 -0.09081 0.10978  258 ASP   A O   
2124 C CB  . ASP   A 261 ? 0.96724 0.67389 0.74290 -0.03779 -0.10904 0.14029  258 ASP   A CB  
2125 C CG  . ASP   A 261 ? 1.20488 0.86546 0.92841 -0.03918 -0.12429 0.15212  258 ASP   A CG  
2126 O OD1 . ASP   A 261 ? 1.26684 0.93658 0.99613 -0.02116 -0.13817 0.14858  258 ASP   A OD1 
2127 O OD2 . ASP   A 261 ? 1.21667 0.83139 0.89200 -0.05940 -0.12253 0.16490  258 ASP   A OD2 
2128 N N   . GLY   A 262 ? 0.95940 0.73498 0.83556 -0.00910 -0.10101 0.11061  259 GLY   A N   
2129 C CA  . GLY   A 262 ? 0.83331 0.65457 0.75300 -0.01081 -0.08479 0.10038  259 GLY   A CA  
2130 C C   . GLY   A 262 ? 0.73439 0.59685 0.69724 0.01118  -0.08947 0.08629  259 GLY   A C   
2131 O O   . GLY   A 262 ? 0.69529 0.60442 0.69159 0.00707  -0.07541 0.08025  259 GLY   A O   
2132 N N   . ARG   A 263 ? 0.83448 0.68011 0.79651 0.03448  -0.10970 0.08020  260 ARG   A N   
2133 C CA  . ARG   A 263 ? 0.83706 0.72559 0.84143 0.05460  -0.11425 0.06520  260 ARG   A CA  
2134 C C   . ARG   A 263 ? 0.85353 0.77445 0.87057 0.05236  -0.11216 0.06563  260 ARG   A C   
2135 O O   . ARG   A 263 ? 0.76873 0.73736 0.82483 0.05615  -0.10493 0.05527  260 ARG   A O   
2136 C CB  . ARG   A 263 ? 0.91130 0.77573 0.91144 0.08152  -0.13832 0.05716  260 ARG   A CB  
2137 C CG  . ARG   A 263 ? 0.88686 0.71729 0.87496 0.08728  -0.14296 0.05435  260 ARG   A CG  
2138 C CD  . ARG   A 263 ? 1.09732 0.91135 1.08786 0.11830  -0.16774 0.04254  260 ARG   A CD  
2139 N NE  . ARG   A 263 ? 1.11561 0.90171 1.07932 0.12884  -0.18899 0.04850  260 ARG   A NE  
2140 C CZ  . ARG   A 263 ? 1.17568 0.89585 1.08719 0.12869  -0.20551 0.06074  260 ARG   A CZ  
2141 N NH1 . ARG   A 263 ? 1.37428 1.04861 1.25480 0.11750  -0.20330 0.06838  260 ARG   A NH1 
2142 N NH2 . ARG   A 263 ? 1.19514 0.89288 1.08276 0.13904  -0.22529 0.06554  260 ARG   A NH2 
2143 N N   . SER   A 264 ? 0.79680 0.69074 0.77892 0.04516  -0.11843 0.07742  261 SER   A N   
2144 C CA  . SER   A 264 ? 0.76897 0.68999 0.75922 0.04279  -0.11731 0.07775  261 SER   A CA  
2145 C C   . SER   A 264 ? 0.66203 0.62127 0.67322 0.02430  -0.09413 0.07771  261 SER   A C   
2146 O O   . SER   A 264 ? 0.65409 0.65379 0.69619 0.02700  -0.08997 0.06991  261 SER   A O   
2147 C CB  . SER   A 264 ? 0.76642 0.64664 0.70929 0.03771  -0.12812 0.09073  261 SER   A CB  
2148 O OG  . SER   A 264 ? 0.89889 0.80459 0.84647 0.03173  -0.12381 0.09162  261 SER   A OG  
2149 N N   . LEU   A 265 ? 0.68700 0.63316 0.68100 0.00524  -0.07974 0.08581  262 LEU   A N   
2150 C CA  . LEU   A 265 ? 0.62864 0.60911 0.64124 -0.01032 -0.05963 0.08482  262 LEU   A CA  
2151 C C   . LEU   A 265 ? 0.61723 0.63420 0.67131 -0.00450 -0.05201 0.07324  262 LEU   A C   
2152 O O   . LEU   A 265 ? 0.61920 0.67097 0.69656 -0.00789 -0.04337 0.06856  262 LEU   A O   
2153 C CB  . LEU   A 265 ? 0.67943 0.64092 0.66783 -0.03066 -0.04706 0.09366  262 LEU   A CB  
2154 C CG  . LEU   A 265 ? 0.60753 0.60337 0.61527 -0.04495 -0.02765 0.09115  262 LEU   A CG  
2155 C CD1 . LEU   A 265 ? 0.60893 0.62933 0.62238 -0.04657 -0.02475 0.09014  262 LEU   A CD1 
2156 C CD2 . LEU   A 265 ? 0.62992 0.60935 0.61556 -0.06455 -0.01665 0.09807  262 LEU   A CD2 
2157 N N   . LEU   A 266 ? 0.62587 0.63321 0.68701 0.00389  -0.05538 0.06834  263 LEU   A N   
2158 C CA  . LEU   A 266 ? 0.60878 0.64973 0.70602 0.00855  -0.04741 0.05706  263 LEU   A CA  
2159 C C   . LEU   A 266 ? 0.57252 0.64649 0.69840 0.02114  -0.05324 0.04708  263 LEU   A C   
2160 O O   . LEU   A 266 ? 0.48969 0.59880 0.64251 0.01706  -0.04257 0.04057  263 LEU   A O   
2161 C CB  . LEU   A 266 ? 0.56532 0.58745 0.66175 0.01675  -0.05133 0.05254  263 LEU   A CB  
2162 C CG  . LEU   A 266 ? 0.61492 0.66940 0.74459 0.02078  -0.04215 0.04052  263 LEU   A CG  
2163 C CD1 . LEU   A 266 ? 0.52131 0.59389 0.65745 0.00277  -0.02397 0.04327  263 LEU   A CD1 
2164 C CD2 . LEU   A 266 ? 0.52675 0.56036 0.65354 0.03215  -0.04867 0.03441  263 LEU   A CD2 
2165 N N   . SER   A 267 ? 0.56961 0.63198 0.68884 0.03577  -0.07082 0.04555  264 SER   A N   
2166 C CA  . SER   A 267 ? 0.64906 0.74546 0.79685 0.04694  -0.07744 0.03494  264 SER   A CA  
2167 C C   . SER   A 267 ? 0.61892 0.73910 0.77320 0.03425  -0.06891 0.03758  264 SER   A C   
2168 O O   . SER   A 267 ? 0.51792 0.67489 0.70202 0.03375  -0.06392 0.02868  264 SER   A O   
2169 C CB  . SER   A 267 ? 0.60986 0.68655 0.74596 0.06564  -0.10031 0.03306  264 SER   A CB  
2170 O OG  . SER   A 267 ? 0.91300 0.96748 1.04467 0.08047  -0.11038 0.02834  264 SER   A OG  
2171 N N   . GLN   A 268 ? 0.55103 0.65007 0.67635 0.02316  -0.06695 0.04919  265 GLN   A N   
2172 C CA  . GLN   A 268 ? 0.53819 0.65666 0.66695 0.01287  -0.06027 0.05074  265 GLN   A CA  
2173 C C   . GLN   A 268 ? 0.49295 0.63274 0.63704 -0.00043 -0.04190 0.04942  265 GLN   A C   
2174 O O   . GLN   A 268 ? 0.52839 0.69127 0.68591 -0.00581 -0.03703 0.04625  265 GLN   A O   
2175 C CB  . GLN   A 268 ? 0.50970 0.60056 0.60182 0.00597  -0.06349 0.06191  265 GLN   A CB  
2176 C CG  . GLN   A 268 ? 0.60527 0.66929 0.67560 0.01880  -0.08350 0.06455  265 GLN   A CG  
2177 C CD  . GLN   A 268 ? 0.68305 0.71824 0.71254 0.00967  -0.08535 0.07616  265 GLN   A CD  
2178 O OE1 . GLN   A 268 ? 0.80570 0.80202 0.80186 0.01004  -0.09297 0.08442  265 GLN   A OE1 
2179 N NE2 . GLN   A 268 ? 0.60401 0.65653 0.63367 0.00091  -0.07848 0.07651  265 GLN   A NE2 
2180 N N   . MET   A 269 ? 0.52085 0.65097 0.66140 -0.00566 -0.03293 0.05159  266 MET   A N   
2181 C CA  . MET   A 269 ? 0.47832 0.62739 0.63315 -0.01610 -0.01771 0.04940  266 MET   A CA  
2182 C C   . MET   A 269 ? 0.50440 0.68036 0.68936 -0.01130 -0.01487 0.03904  266 MET   A C   
2183 O O   . MET   A 269 ? 0.45892 0.65241 0.65540 -0.01980 -0.00426 0.03678  266 MET   A O   
2184 C CB  . MET   A 269 ? 0.53743 0.66805 0.67810 -0.02383 -0.00993 0.05444  266 MET   A CB  
2185 C CG  . MET   A 269 ? 0.50519 0.61269 0.61596 -0.03301 -0.00929 0.06418  266 MET   A CG  
2186 S SD  . MET   A 269 ? 0.58521 0.67400 0.68174 -0.04460 -0.00020 0.06868  266 MET   A SD  
2187 C CE  . MET   A 269 ? 0.49332 0.61295 0.60939 -0.05407 0.01465  0.06413  266 MET   A CE  
2188 N N   . LEU   A 270 ? 0.40986 0.58924 0.60653 0.00210  -0.02436 0.03208  267 LEU   A N   
2189 C CA  . LEU   A 270 ? 0.42084 0.62962 0.64689 0.00629  -0.02079 0.02044  267 LEU   A CA  
2190 C C   . LEU   A 270 ? 0.39300 0.62654 0.63831 0.01272  -0.02920 0.01254  267 LEU   A C   
2191 O O   . LEU   A 270 ? 0.43011 0.68853 0.70028 0.01979  -0.03000 0.00082  267 LEU   A O   
2192 C CB  . LEU   A 270 ? 0.43380 0.63401 0.66333 0.01726  -0.02357 0.01481  267 LEU   A CB  
2193 C CG  . LEU   A 270 ? 0.52257 0.70194 0.73689 0.00979  -0.01470 0.02038  267 LEU   A CG  
2194 C CD1 . LEU   A 270 ? 0.46033 0.62996 0.67779 0.02211  -0.01918 0.01321  267 LEU   A CD1 
2195 C CD2 . LEU   A 270 ? 0.46887 0.66692 0.69203 -0.00419 0.00083  0.02017  267 LEU   A CD2 
2196 N N   . HIS   A 271 ? 0.49596 0.72505 0.73071 0.01005  -0.03534 0.01761  268 HIS   A N   
2197 C CA  . HIS   A 271 ? 0.44747 0.70099 0.70039 0.01391  -0.04343 0.00993  268 HIS   A CA  
2198 C C   . HIS   A 271 ? 0.44405 0.72961 0.72056 0.00226  -0.03148 0.00305  268 HIS   A C   
2199 O O   . HIS   A 271 ? 0.42530 0.70726 0.69442 -0.01101 -0.01948 0.00831  268 HIS   A O   
2200 C CB  . HIS   A 271 ? 0.46627 0.70542 0.69886 0.01148  -0.05129 0.01738  268 HIS   A CB  
2201 C CG  . HIS   A 271 ? 0.65385 0.90972 0.89947 0.01987  -0.06551 0.00990  268 HIS   A CG  
2202 N ND1 . HIS   A 271 ? 0.65761 0.94811 0.93071 0.01448  -0.06301 0.00018  268 HIS   A ND1 
2203 C CD2 . HIS   A 271 ? 0.69448 0.93653 0.92819 0.03257  -0.08318 0.01047  268 HIS   A CD2 
2204 C CE1 . HIS   A 271 ? 0.77360 1.07436 1.05443 0.02367  -0.07840 -0.00590 268 HIS   A CE1 
2205 N NE2 . HIS   A 271 ? 0.73138 1.00261 0.98820 0.03582  -0.09153 0.00020  268 HIS   A NE2 
2206 N N   . TYR   A 272 ? 0.36000 0.67685 0.66419 0.00698  -0.03532 -0.00935 269 TYR   A N   
2207 C CA  . TYR   A 272 ? 0.36194 0.70900 0.68677 -0.00667 -0.02362 -0.01618 269 TYR   A CA  
2208 C C   . TYR   A 272 ? 0.50182 0.84585 0.81703 -0.02082 -0.02172 -0.01043 269 TYR   A C   
2209 O O   . TYR   A 272 ? 0.45632 0.79985 0.76731 -0.03526 -0.00984 -0.00740 269 TYR   A O   
2210 C CB  . TYR   A 272 ? 0.34001 0.72529 0.69772 0.00013  -0.02836 -0.03208 269 TYR   A CB  
2211 C CG  . TYR   A 272 ? 0.37091 0.77064 0.74477 0.00828  -0.02286 -0.04174 269 TYR   A CG  
2212 C CD1 . TYR   A 272 ? 0.41656 0.82229 0.79174 -0.00403 -0.00573 -0.04196 269 TYR   A CD1 
2213 C CD2 . TYR   A 272 ? 0.44930 0.85567 0.83566 0.02929  -0.03584 -0.05156 269 TYR   A CD2 
2214 C CE1 . TYR   A 272 ? 0.39115 0.81055 0.77981 0.00349  -0.00026 -0.05184 269 TYR   A CE1 
2215 C CE2 . TYR   A 272 ? 0.33476 0.75459 0.73588 0.03833  -0.03124 -0.06223 269 TYR   A CE2 
2216 C CZ  . TYR   A 272 ? 0.45409 0.88134 0.85653 0.02489  -0.01271 -0.06246 269 TYR   A CZ  
2217 O OH  . TYR   A 272 ? 0.41267 0.85359 0.82844 0.03396  -0.00773 -0.07400 269 TYR   A OH  
2218 N N   . ASP   A 273 ? 0.40175 0.74142 0.71132 -0.01608 -0.03448 -0.00932 270 ASP   A N   
2219 C CA  . ASP   A 273 ? 0.44520 0.78154 0.74545 -0.02762 -0.03479 -0.00566 270 ASP   A CA  
2220 C C   . ASP   A 273 ? 0.45494 0.76157 0.72684 -0.03334 -0.02821 0.00618  270 ASP   A C   
2221 O O   . ASP   A 273 ? 0.43987 0.72400 0.69200 -0.02560 -0.03303 0.01316  270 ASP   A O   
2222 C CB  . ASP   A 273 ? 0.46232 0.80029 0.76181 -0.01916 -0.05145 -0.00818 270 ASP   A CB  
2223 C CG  . ASP   A 273 ? 0.60944 0.94937 0.90421 -0.03102 -0.05300 -0.00792 270 ASP   A CG  
2224 O OD1 . ASP   A 273 ? 0.54270 0.87781 0.83131 -0.04488 -0.04199 -0.00469 270 ASP   A OD1 
2225 O OD2 . ASP   A 273 ? 0.67177 1.01610 0.96756 -0.02576 -0.06664 -0.01139 270 ASP   A OD2 
2226 N N   . PRO   A 274 ? 0.48084 0.78618 0.74890 -0.04676 -0.01781 0.00820  271 PRO   A N   
2227 C CA  . PRO   A 274 ? 0.40246 0.68348 0.64629 -0.05013 -0.01286 0.01708  271 PRO   A CA  
2228 C C   . PRO   A 274 ? 0.47050 0.73782 0.69618 -0.04746 -0.02123 0.02085  271 PRO   A C   
2229 O O   . PRO   A 274 ? 0.45141 0.70080 0.65727 -0.04617 -0.01877 0.02726  271 PRO   A O   
2230 C CB  . PRO   A 274 ? 0.35716 0.64080 0.60211 -0.06351 -0.00367 0.01619  271 PRO   A CB  
2231 C CG  . PRO   A 274 ? 0.44965 0.75730 0.71762 -0.06832 0.00024  0.00849  271 PRO   A CG  
2232 C CD  . PRO   A 274 ? 0.36240 0.68742 0.64647 -0.05965 -0.01034 0.00206  271 PRO   A CD  
2233 N N   . ASN   A 275 ? 0.53730 0.81436 0.76928 -0.04728 -0.03076 0.01612  272 ASN   A N   
2234 C CA  . ASN   A 275 ? 0.52790 0.79182 0.74087 -0.04430 -0.03938 0.01885  272 ASN   A CA  
2235 C C   . ASN   A 275 ? 0.59128 0.84268 0.79117 -0.03259 -0.04728 0.02318  272 ASN   A C   
2236 O O   . ASN   A 275 ? 0.63607 0.87029 0.81198 -0.03116 -0.05003 0.02833  272 ASN   A O   
2237 C CB  . ASN   A 275 ? 0.52964 0.80709 0.75282 -0.04808 -0.04838 0.01184  272 ASN   A CB  
2238 C CG  . ASN   A 275 ? 0.74599 1.03022 0.97710 -0.06213 -0.04146 0.00836  272 ASN   A CG  
2239 O OD1 . ASN   A 275 ? 0.77223 1.04244 0.99058 -0.06752 -0.03332 0.01232  272 ASN   A OD1 
2240 N ND2 . ASN   A 275 ? 0.83952 1.14480 1.09087 -0.06854 -0.04533 0.00048  272 ASN   A ND2 
2241 N N   . LYS   A 276 ? 0.50012 0.75838 0.71327 -0.02423 -0.05128 0.02073  273 LYS   A N   
2242 C CA  . LYS   A 276 ? 0.51192 0.75246 0.70950 -0.01260 -0.06074 0.02515  273 LYS   A CA  
2243 C C   . LYS   A 276 ? 0.60811 0.83013 0.79256 -0.01243 -0.05228 0.03229  273 LYS   A C   
2244 O O   . LYS   A 276 ? 0.52704 0.72604 0.68943 -0.00658 -0.05852 0.03854  273 LYS   A O   
2245 C CB  . LYS   A 276 ? 0.55598 0.81184 0.77408 -0.00049 -0.07347 0.01687  273 LYS   A CB  
2246 C CG  . LYS   A 276 ? 0.72945 1.00490 0.96106 0.00017  -0.08464 0.00880  273 LYS   A CG  
2247 C CD  . LYS   A 276 ? 0.70770 0.96239 0.91076 0.00207  -0.09482 0.01444  273 LYS   A CD  
2248 C CE  . LYS   A 276 ? 0.95698 1.23054 1.17340 0.00391  -0.10832 0.00552  273 LYS   A CE  
2249 N NZ  . LYS   A 276 ? 1.00660 1.25880 1.19274 0.00669  -0.11928 0.01044  273 LYS   A NZ  
2250 N N   . ARG   A 277 ? 0.44075 0.67040 0.63608 -0.01959 -0.03898 0.03157  274 ARG   A N   
2251 C CA  . ARG   A 277 ? 0.43444 0.64841 0.61915 -0.02049 -0.03110 0.03721  274 ARG   A CA  
2252 C C   . ARG   A 277 ? 0.48617 0.67909 0.64203 -0.02561 -0.02821 0.04579  274 ARG   A C   
2253 O O   . ARG   A 277 ? 0.48348 0.67947 0.63267 -0.03176 -0.02504 0.04612  274 ARG   A O   
2254 C CB  . ARG   A 277 ? 0.35910 0.58596 0.55904 -0.02814 -0.01802 0.03434  274 ARG   A CB  
2255 C CG  . ARG   A 277 ? 0.34787 0.56417 0.54462 -0.02736 -0.01151 0.03692  274 ARG   A CG  
2256 C CD  . ARG   A 277 ? 0.36794 0.59854 0.57991 -0.03405 -0.00035 0.03287  274 ARG   A CD  
2257 N NE  . ARG   A 277 ? 0.40695 0.66082 0.64231 -0.03263 -0.00155 0.02416  274 ARG   A NE  
2258 C CZ  . ARG   A 277 ? 0.33913 0.60789 0.58598 -0.04142 0.00688  0.02021  274 ARG   A CZ  
2259 N NH1 . ARG   A 277 ? 0.36883 0.62962 0.60565 -0.05009 0.01519  0.02413  274 ARG   A NH1 
2260 N NH2 . ARG   A 277 ? 0.28915 0.58146 0.55714 -0.04190 0.00654  0.01162  274 ARG   A NH2 
2261 N N   . ILE   A 278 ? 0.49994 0.67117 0.63778 -0.02350 -0.02934 0.05197  275 ILE   A N   
2262 C CA  . ILE   A 278 ? 0.45960 0.61209 0.56842 -0.03019 -0.02615 0.05975  275 ILE   A CA  
2263 C C   . ILE   A 278 ? 0.54423 0.70645 0.65520 -0.04074 -0.01178 0.05943  275 ILE   A C   
2264 O O   . ILE   A 278 ? 0.48255 0.65527 0.61045 -0.04291 -0.00434 0.05630  275 ILE   A O   
2265 C CB  . ILE   A 278 ? 0.53643 0.66108 0.62397 -0.02865 -0.02970 0.06670  275 ILE   A CB  
2266 C CG1 . ILE   A 278 ? 0.57977 0.68460 0.63331 -0.03725 -0.02765 0.07485  275 ILE   A CG1 
2267 C CG2 . ILE   A 278 ? 0.40949 0.53367 0.50644 -0.03221 -0.02038 0.06636  275 ILE   A CG2 
2268 C CD1 . ILE   A 278 ? 0.63611 0.70694 0.66173 -0.03784 -0.03309 0.08305  275 ILE   A CD1 
2269 N N   . SER   A 279 ? 0.54429 0.70383 0.63758 -0.04643 -0.00856 0.06161  276 SER   A N   
2270 C CA  . SER   A 279 ? 0.51658 0.68663 0.61146 -0.05415 0.00330  0.05953  276 SER   A CA  
2271 C C   . SER   A 279 ? 0.51580 0.67605 0.59726 -0.06188 0.01168  0.06429  276 SER   A C   
2272 O O   . SER   A 279 ? 0.50994 0.65034 0.57328 -0.06318 0.00823  0.07066  276 SER   A O   
2273 C CB  . SER   A 279 ? 0.57528 0.75088 0.65962 -0.05557 0.00311  0.05690  276 SER   A CB  
2274 O OG  . SER   A 279 ? 0.54350 0.70559 0.60065 -0.05893 0.00248  0.06202  276 SER   A OG  
2275 N N   . ALA   A 280 ? 0.46860 0.64185 0.55817 -0.06739 0.02184  0.06074  277 ALA   A N   
2276 C CA  . ALA   A 280 ? 0.55406 0.72327 0.63407 -0.07671 0.03064  0.06348  277 ALA   A CA  
2277 C C   . ALA   A 280 ? 0.58725 0.74778 0.64038 -0.08434 0.03305  0.06769  277 ALA   A C   
2278 O O   . ALA   A 280 ? 0.55671 0.70050 0.59213 -0.09250 0.03531  0.07400  277 ALA   A O   
2279 C CB  . ALA   A 280 ? 0.46346 0.65230 0.55866 -0.07960 0.03932  0.05682  277 ALA   A CB  
2280 N N   . LYS   A 281 ? 0.60250 0.77242 0.64978 -0.08273 0.03260  0.06414  278 LYS   A N   
2281 C CA  . LYS   A 281 ? 0.60933 0.77263 0.62884 -0.09055 0.03584  0.06731  278 LYS   A CA  
2282 C C   . LYS   A 281 ? 0.66655 0.80028 0.66189 -0.09006 0.02610  0.07695  278 LYS   A C   
2283 O O   . LYS   A 281 ? 0.61848 0.73496 0.58717 -0.10085 0.02968  0.08380  278 LYS   A O   
2284 C CB  . LYS   A 281 ? 0.58436 0.76285 0.60281 -0.08640 0.03564  0.06012  278 LYS   A CB  
2285 C CG  . LYS   A 281 ? 0.59747 0.77337 0.58671 -0.09482 0.04084  0.06145  278 LYS   A CG  
2286 C CD  . LYS   A 281 ? 0.87900 1.06871 0.86756 -0.08836 0.03906  0.05289  278 LYS   A CD  
2287 C CE  . LYS   A 281 ? 1.08825 1.27861 1.04705 -0.09718 0.04604  0.05262  278 LYS   A CE  
2288 N NZ  . LYS   A 281 ? 1.01267 1.22229 0.97182 -0.10926 0.06216  0.04830  278 LYS   A NZ  
2289 N N   . ALA   A 282 ? 0.59352 0.72047 0.59696 -0.07793 0.01303  0.07718  279 ALA   A N   
2290 C CA  . ALA   A 282 ? 0.63342 0.73225 0.61537 -0.07388 0.00053  0.08480  279 ALA   A CA  
2291 C C   . ALA   A 282 ? 0.63735 0.71485 0.61400 -0.07622 -0.00056 0.09085  279 ALA   A C   
2292 O O   . ALA   A 282 ? 0.64565 0.69247 0.59221 -0.07868 -0.00731 0.09911  279 ALA   A O   
2293 C CB  . ALA   A 282 ? 0.58994 0.69309 0.58765 -0.05951 -0.01357 0.08089  279 ALA   A CB  
2294 N N   . ALA   A 283 ? 0.58357 0.67354 0.58599 -0.07548 0.00505  0.08686  280 ALA   A N   
2295 C CA  . ALA   A 283 ? 0.60325 0.67242 0.60072 -0.07737 0.00385  0.09131  280 ALA   A CA  
2296 C C   . ALA   A 283 ? 0.59610 0.64843 0.56503 -0.09461 0.01269  0.09813  280 ALA   A C   
2297 O O   . ALA   A 283 ? 0.72664 0.74678 0.67350 -0.09803 0.00749  0.10535  280 ALA   A O   
2298 C CB  . ALA   A 283 ? 0.51866 0.60672 0.54831 -0.07406 0.00916  0.08471  280 ALA   A CB  
2299 N N   . LEU   A 284 ? 0.61430 0.68791 0.58268 -0.10601 0.02580  0.09515  281 LEU   A N   
2300 C CA  . LEU   A 284 ? 0.55451 0.61845 0.49731 -0.12517 0.03625  0.10011  281 LEU   A CA  
2301 C C   . LEU   A 284 ? 0.73637 0.76670 0.63665 -0.13089 0.02971  0.11012  281 LEU   A C   
2302 O O   . LEU   A 284 ? 0.72695 0.73349 0.59828 -0.14705 0.03407  0.11765  281 LEU   A O   
2303 C CB  . LEU   A 284 ? 0.69961 0.79977 0.65410 -0.13373 0.05107  0.09190  281 LEU   A CB  
2304 C CG  . LEU   A 284 ? 0.69166 0.82107 0.68179 -0.13100 0.05786  0.08261  281 LEU   A CG  
2305 C CD1 . LEU   A 284 ? 0.64959 0.81426 0.65116 -0.13401 0.06838  0.07266  281 LEU   A CD1 
2306 C CD2 . LEU   A 284 ? 0.66076 0.78033 0.64989 -0.14246 0.06297  0.08529  281 LEU   A CD2 
2307 N N   . ALA   A 285 ? 0.76201 0.78797 0.65574 -0.11891 0.01866  0.11047  282 ALA   A N   
2308 C CA  . ALA   A 285 ? 0.73460 0.72673 0.58564 -0.12210 0.00987  0.11983  282 ALA   A CA  
2309 C C   . ALA   A 285 ? 0.81408 0.76716 0.65159 -0.11030 -0.00904 0.12665  282 ALA   A C   
2310 O O   . ALA   A 285 ? 0.92926 0.84926 0.72974 -0.10957 -0.02052 0.13460  282 ALA   A O   
2311 C CB  . ALA   A 285 ? 0.77483 0.78201 0.62359 -0.11483 0.00628  0.11571  282 ALA   A CB  
2312 N N   . HIS   A 286 ? 0.76149 0.71719 0.62670 -0.10024 -0.01321 0.12294  283 HIS   A N   
2313 C CA  . HIS   A 286 ? 0.81219 0.73452 0.66866 -0.08606 -0.03177 0.12649  283 HIS   A CA  
2314 C C   . HIS   A 286 ? 0.89494 0.76879 0.70738 -0.09900 -0.03448 0.13804  283 HIS   A C   
2315 O O   . HIS   A 286 ? 0.95919 0.83280 0.76354 -0.11869 -0.01964 0.14077  283 HIS   A O   
2316 C CB  . HIS   A 286 ? 0.79409 0.73536 0.69196 -0.07315 -0.03310 0.11782  283 HIS   A CB  
2317 C CG  . HIS   A 286 ? 0.82587 0.74556 0.72521 -0.05312 -0.05306 0.11660  283 HIS   A CG  
2318 N ND1 . HIS   A 286 ? 0.76954 0.64916 0.64766 -0.05115 -0.06214 0.12160  283 HIS   A ND1 
2319 C CD2 . HIS   A 286 ? 0.80909 0.74302 0.72946 -0.03369 -0.06629 0.10951  283 HIS   A CD2 
2320 C CE1 . HIS   A 286 ? 0.91047 0.78125 0.79717 -0.02923 -0.08066 0.11690  283 HIS   A CE1 
2321 N NE2 . HIS   A 286 ? 0.82637 0.73208 0.74007 -0.01888 -0.08302 0.10927  283 HIS   A NE2 
2322 N N   . PRO   A 287 ? 0.99050 0.82155 0.77278 -0.08855 -0.05435 0.14460  284 PRO   A N   
2323 C CA  . PRO   A 287 ? 1.01778 0.79403 0.75230 -0.10092 -0.05941 0.15657  284 PRO   A CA  
2324 C C   . PRO   A 287 ? 1.05184 0.81825 0.79718 -0.10559 -0.05495 0.15544  284 PRO   A C   
2325 O O   . PRO   A 287 ? 1.08462 0.80610 0.79043 -0.12018 -0.05653 0.16518  284 PRO   A O   
2326 C CB  . PRO   A 287 ? 1.10990 0.84583 0.81900 -0.08079 -0.08613 0.16052  284 PRO   A CB  
2327 C CG  . PRO   A 287 ? 1.07159 0.84212 0.80235 -0.06715 -0.09047 0.15350  284 PRO   A CG  
2328 C CD  . PRO   A 287 ? 0.95277 0.78207 0.73866 -0.06652 -0.07375 0.14153  284 PRO   A CD  
2329 N N   . PHE   A 288 ? 0.99421 0.79822 0.78864 -0.09460 -0.04998 0.14406  285 PHE   A N   
2330 C CA  . PHE   A 288 ? 1.01314 0.81104 0.81797 -0.10042 -0.04414 0.14206  285 PHE   A CA  
2331 C C   . PHE   A 288 ? 0.92929 0.73439 0.72297 -0.12944 -0.02378 0.14601  285 PHE   A C   
2332 O O   . PHE   A 288 ? 1.04520 0.82676 0.82651 -0.14152 -0.02102 0.14899  285 PHE   A O   
2333 C CB  . PHE   A 288 ? 0.86108 0.70121 0.71920 -0.08400 -0.04151 0.12874  285 PHE   A CB  
2334 C CG  . PHE   A 288 ? 0.88113 0.71604 0.75101 -0.08739 -0.03685 0.12527  285 PHE   A CG  
2335 C CD1 . PHE   A 288 ? 1.00507 0.79621 0.85638 -0.07851 -0.05163 0.12715  285 PHE   A CD1 
2336 C CD2 . PHE   A 288 ? 0.77864 0.65107 0.67720 -0.09808 -0.01920 0.11925  285 PHE   A CD2 
2337 C CE1 . PHE   A 288 ? 0.90897 0.69421 0.76993 -0.08140 -0.04779 0.12308  285 PHE   A CE1 
2338 C CE2 . PHE   A 288 ? 0.85632 0.72374 0.76459 -0.10114 -0.01573 0.11558  285 PHE   A CE2 
2339 C CZ  . PHE   A 288 ? 0.90423 0.72832 0.79375 -0.09329 -0.02951 0.11744  285 PHE   A CZ  
2340 N N   . PHE   A 289 ? 1.03059 0.86895 0.82890 -0.14079 -0.00983 0.14484  286 PHE   A N   
2341 C CA  . PHE   A 289 ? 1.03212 0.88461 0.82196 -0.16793 0.00994  0.14636  286 PHE   A CA  
2342 C C   . PHE   A 289 ? 1.20777 1.03377 0.94816 -0.18687 0.01259  0.15704  286 PHE   A C   
2343 O O   . PHE   A 289 ? 1.34245 1.19264 1.07903 -0.20798 0.03059  0.15589  286 PHE   A O   
2344 C CB  . PHE   A 289 ? 0.85253 0.76554 0.68494 -0.16719 0.02510  0.13479  286 PHE   A CB  
2345 C CG  . PHE   A 289 ? 0.81427 0.75355 0.69194 -0.14935 0.02280  0.12476  286 PHE   A CG  
2346 C CD1 . PHE   A 289 ? 0.80953 0.74934 0.70141 -0.15431 0.02730  0.12165  286 PHE   A CD1 
2347 C CD2 . PHE   A 289 ? 0.70915 0.67237 0.61338 -0.12930 0.01656  0.11826  286 PHE   A CD2 
2348 C CE1 . PHE   A 289 ? 0.72382 0.68672 0.65360 -0.13900 0.02583  0.11259  286 PHE   A CE1 
2349 C CE2 . PHE   A 289 ? 0.67465 0.66118 0.61703 -0.11566 0.01574  0.10945  286 PHE   A CE2 
2350 C CZ  . PHE   A 289 ? 0.65760 0.64374 0.61186 -0.12026 0.02057  0.10677  286 PHE   A CZ  
2351 N N   . GLN   A 290 ? 1.17847 0.95578 0.88000 -0.17950 -0.00531 0.16666  287 GLN   A N   
2352 C CA  . GLN   A 290 ? 1.44915 1.19768 1.09851 -0.19714 -0.00395 0.17760  287 GLN   A CA  
2353 C C   . GLN   A 290 ? 1.68793 1.41368 1.30335 -0.23015 0.00963  0.18546  287 GLN   A C   
2354 O O   . GLN   A 290 ? 1.80060 1.52032 1.38026 -0.25210 0.01984  0.19175  287 GLN   A O   
2355 C CB  . GLN   A 290 ? 1.34986 1.04503 0.96200 -0.18061 -0.02929 0.18644  287 GLN   A CB  
2356 C CG  . GLN   A 290 ? 1.47052 1.10574 1.05385 -0.17893 -0.04504 0.19429  287 GLN   A CG  
2357 C CD  . GLN   A 290 ? 1.77568 1.35402 1.29178 -0.20649 -0.04427 0.20985  287 GLN   A CD  
2358 O OE1 . GLN   A 290 ? 1.83716 1.40245 1.31557 -0.21640 -0.04360 0.21733  287 GLN   A OE1 
2359 N NE2 . GLN   A 290 ? 1.76880 1.31145 1.26724 -0.22034 -0.04422 0.21477  287 GLN   A NE2 
2360 N N   . ASP   A 291 ? 1.66047 1.37431 1.28562 -0.23539 0.01045  0.18464  288 ASP   A N   
2361 C CA  . ASP   A 291 ? 1.67271 1.36818 1.27002 -0.26864 0.02380  0.19069  288 ASP   A CA  
2362 C C   . ASP   A 291 ? 1.77685 1.53437 1.41490 -0.28432 0.04777  0.17916  288 ASP   A C   
2363 O O   . ASP   A 291 ? 1.84640 1.60583 1.46398 -0.31575 0.06386  0.18193  288 ASP   A O   
2364 C CB  . ASP   A 291 ? 1.79686 1.43892 1.37693 -0.26722 0.00977  0.19612  288 ASP   A CB  
2365 C CG  . ASP   A 291 ? 1.73101 1.39719 1.36329 -0.24086 0.00295  0.18429  288 ASP   A CG  
2366 O OD1 . ASP   A 291 ? 1.60307 1.32233 1.28146 -0.22322 0.00724  0.17347  288 ASP   A OD1 
2367 O OD2 . ASP   A 291 ? 1.67148 1.30192 1.29655 -0.23849 -0.00669 0.18562  288 ASP   A OD2 
2368 N N   . VAL   A 292 ? 1.67846 1.48641 1.37242 -0.26373 0.05003  0.16590  289 VAL   A N   
2369 C CA  . VAL   A 292 ? 1.61814 1.48358 1.35127 -0.27498 0.06970  0.15392  289 VAL   A CA  
2370 C C   . VAL   A 292 ? 1.64508 1.55276 1.38128 -0.28349 0.08461  0.14883  289 VAL   A C   
2371 O O   . VAL   A 292 ? 1.73480 1.67513 1.47723 -0.30588 0.10315  0.14308  289 VAL   A O   
2372 C CB  . VAL   A 292 ? 1.47722 1.37458 1.26352 -0.25018 0.06520  0.14236  289 VAL   A CB  
2373 C CG1 . VAL   A 292 ? 1.36235 1.31656 1.18717 -0.25956 0.08283  0.12968  289 VAL   A CG1 
2374 C CG2 . VAL   A 292 ? 1.41506 1.27241 1.19747 -0.24211 0.05161  0.14573  289 VAL   A CG2 
2375 N N   . THR   A 293 ? 1.45828 1.36763 1.19086 -0.26568 0.07654  0.14948  290 THR   A N   
2376 C CA  . THR   A 293 ? 1.37915 1.32753 1.11514 -0.26977 0.08878  0.14319  290 THR   A CA  
2377 C C   . THR   A 293 ? 1.60992 1.52176 1.29655 -0.27240 0.08133  0.15423  290 THR   A C   
2378 O O   . THR   A 293 ? 1.62904 1.48969 1.28730 -0.26294 0.06289  0.16510  290 THR   A O   
2379 C CB  . THR   A 293 ? 1.27750 1.27180 1.06256 -0.24407 0.08686  0.13009  290 THR   A CB  
2380 O OG1 . THR   A 293 ? 1.28128 1.31181 1.06794 -0.24805 0.09850  0.12270  290 THR   A OG1 
2381 C CG2 . THR   A 293 ? 1.07305 1.04249 0.85997 -0.21717 0.06594  0.13396  290 THR   A CG2 
2382 N N   . LYS   A 294 ? 1.51015 1.44933 1.18616 -0.28446 0.09527  0.15028  291 LYS   A N   
2383 C CA  . LYS   A 294 ? 1.67520 1.58764 1.30584 -0.28676 0.09009  0.15862  291 LYS   A CA  
2384 C C   . LYS   A 294 ? 1.74393 1.69861 1.39916 -0.26910 0.09168  0.14718  291 LYS   A C   
2385 O O   . LYS   A 294 ? 1.67235 1.68091 1.36655 -0.26835 0.10562  0.13284  291 LYS   A O   
2386 C CB  . LYS   A 294 ? 1.81510 1.71473 1.39814 -0.32250 0.10665  0.16549  291 LYS   A CB  
2387 C CG  . LYS   A 294 ? 1.82644 1.65203 1.34411 -0.33344 0.09327  0.18469  291 LYS   A CG  
2388 C CD  . LYS   A 294 ? 1.88530 1.66707 1.40371 -0.32547 0.07676  0.19219  291 LYS   A CD  
2389 C CE  . LYS   A 294 ? 1.91116 1.61376 1.36253 -0.33227 0.05954  0.21076  291 LYS   A CE  
2390 N NZ  . LYS   A 294 ? 1.75087 1.40957 1.20318 -0.32113 0.04160  0.21621  291 LYS   A NZ  
2391 N N   . PRO   A 295 ? 1.84171 1.77212 1.47469 -0.25404 0.07631  0.15240  292 PRO   A N   
2392 C CA  . PRO   A 295 ? 1.80833 1.77546 1.46489 -0.23626 0.07564  0.14115  292 PRO   A CA  
2393 C C   . PRO   A 295 ? 1.80953 1.81057 1.45426 -0.25386 0.09619  0.13352  292 PRO   A C   
2394 O O   . PRO   A 295 ? 1.72388 1.70331 1.32078 -0.27670 0.10418  0.14167  292 PRO   A O   
2395 C CB  . PRO   A 295 ? 1.79301 1.71868 1.42030 -0.22002 0.05312  0.15022  292 PRO   A CB  
2396 C CG  . PRO   A 295 ? 1.89179 1.75987 1.46307 -0.23734 0.04784  0.16675  292 PRO   A CG  
2397 C CD  . PRO   A 295 ? 1.85694 1.72348 1.44146 -0.25157 0.05695  0.16816  292 PRO   A CD  
2398 N N   . VAL   A 296 ? 1.99267 2.04628 1.67987 -0.24312 0.10451  0.11720  293 VAL   A N   
2399 C CA  . VAL   A 296 ? 1.88959 1.98274 1.57300 -0.25451 0.12308  0.10574  293 VAL   A CA  
2400 C C   . VAL   A 296 ? 1.84528 1.92612 1.50066 -0.24467 0.11442  0.10668  293 VAL   A C   
2401 O O   . VAL   A 296 ? 1.87983 1.94607 1.54570 -0.22156 0.09531  0.10815  293 VAL   A O   
2402 C CB  . VAL   A 296 ? 1.76915 1.92009 1.50814 -0.24431 0.13276  0.08680  293 VAL   A CB  
2403 C CG1 . VAL   A 296 ? 1.76828 1.91628 1.54759 -0.22510 0.11961  0.08668  293 VAL   A CG1 
2404 C CG2 . VAL   A 296 ? 1.64977 1.83129 1.39770 -0.23019 0.13401  0.07317  293 VAL   A CG2 
2405 N N   . PRO   A 297 ? 1.57313 1.65941 1.19182 -0.26235 0.12778  0.10554  294 PRO   A N   
2406 C CA  . PRO   A 297 ? 1.52510 1.59964 1.11490 -0.25303 0.11935  0.10558  294 PRO   A CA  
2407 C C   . PRO   A 297 ? 1.42036 1.53265 1.05271 -0.22766 0.11455  0.08897  294 PRO   A C   
2408 O O   . PRO   A 297 ? 1.58134 1.74190 1.24746 -0.22661 0.12869  0.07267  294 PRO   A O   
2409 C CB  . PRO   A 297 ? 1.56058 1.64501 1.10884 -0.28033 0.14045  0.10413  294 PRO   A CB  
2410 C CG  . PRO   A 297 ? 1.58886 1.66699 1.12868 -0.30717 0.15412  0.11129  294 PRO   A CG  
2411 C CD  . PRO   A 297 ? 1.52152 1.62269 1.11980 -0.29384 0.15116  0.10468  294 PRO   A CD  
2412 N N   . HIS   A 298 ? 1.40114 1.49006 1.03098 -0.20713 0.09335  0.09265  295 HIS   A N   
2413 C CA  . HIS   A 298 ? 1.55661 1.67238 1.22296 -0.18372 0.08553  0.07886  295 HIS   A CA  
2414 C C   . HIS   A 298 ? 1.33304 1.45498 0.97163 -0.18212 0.08687  0.07169  295 HIS   A C   
2415 O O   . HIS   A 298 ? 1.41642 1.50325 1.00933 -0.18623 0.07802  0.08214  295 HIS   A O   
2416 C CB  . HIS   A 298 ? 1.62983 1.72132 1.31471 -0.16323 0.06194  0.08516  295 HIS   A CB  
2417 C CG  . HIS   A 298 ? 1.69044 1.78431 1.41145 -0.16014 0.06067  0.08769  295 HIS   A CG  
2418 N ND1 . HIS   A 298 ? 1.76740 1.88351 1.50507 -0.17342 0.07788  0.08420  295 HIS   A ND1 
2419 C CD2 . HIS   A 298 ? 1.69890 1.77755 1.44263 -0.14541 0.04441  0.09223  295 HIS   A CD2 
2420 C CE1 . HIS   A 298 ? 1.79516 1.90668 1.56205 -0.16674 0.07173  0.08722  295 HIS   A CE1 
2421 N NE2 . HIS   A 298 ? 1.78781 1.87731 1.55884 -0.14986 0.05218  0.09195  295 HIS   A NE2 
2422 N N   . LEU   A 299 ? 1.39734 1.56209 1.06189 -0.17516 0.09675  0.05332  296 LEU   A N   
2423 C CA  . LEU   A 299 ? 1.35680 1.53071 1.00040 -0.17009 0.09713  0.04326  296 LEU   A CA  
2424 C C   . LEU   A 299 ? 1.47773 1.63095 1.12712 -0.14842 0.07307  0.04442  296 LEU   A C   
2425 O O   . LEU   A 299 ? 1.46944 1.63813 1.16062 -0.13146 0.06520  0.03589  296 LEU   A O   
2426 C CB  . LEU   A 299 ? 1.18563 1.41121 0.85806 -0.16662 0.11330  0.02143  296 LEU   A CB  
2427 C CG  . LEU   A 299 ? 1.24910 1.48883 0.90978 -0.15583 0.11215  0.00654  296 LEU   A CG  
2428 C CD1 . LEU   A 299 ? 1.30179 1.52915 0.90597 -0.17329 0.12139  0.01081  296 LEU   A CD1 
2429 C CD2 . LEU   A 299 ? 1.16708 1.45645 0.86471 -0.14685 0.12407  -0.01649 296 LEU   A CD2 
2430 N N   . ARG   A 300 ? 1.77386 1.89142 1.38012 -0.14982 0.06081  0.05485  297 ARG   A N   
2431 C CA  . ARG   A 300 ? 1.90146 1.99983 1.51123 -0.13079 0.03684  0.05576  297 ARG   A CA  
2432 C C   . ARG   A 300 ? 1.86584 1.98065 1.46657 -0.12289 0.03668  0.04081  297 ARG   A C   
2433 O O   . ARG   A 300 ? 1.87813 1.97130 1.43955 -0.12251 0.02736  0.04369  297 ARG   A O   
2434 C CB  . ARG   A 300 ? 2.04610 2.09673 1.61620 -0.13356 0.02026  0.07372  297 ARG   A CB  
2435 C CG  . ARG   A 300 ? 2.03243 2.06075 1.54208 -0.15414 0.03019  0.08287  297 ARG   A CG  
2436 C CD  . ARG   A 300 ? 2.22862 2.20367 1.69979 -0.15626 0.01200  0.10222  297 ARG   A CD  
2437 N NE  . ARG   A 300 ? 2.35004 2.31306 1.84057 -0.15952 0.01137  0.11201  297 ARG   A NE  
2438 C CZ  . ARG   A 300 ? 2.42948 2.38562 1.95483 -0.14234 -0.00604 0.11412  297 ARG   A CZ  
2439 N NH1 . ARG   A 300 ? 2.45627 2.41719 2.00272 -0.12194 -0.02438 0.10762  297 ARG   A NH1 
2440 N NH2 . ARG   A 300 ? 2.42159 2.36696 1.96084 -0.14660 -0.00463 0.12207  297 ARG   A NH2 
2441 N N   . LEU   A 301 ? 1.49499 1.64717 1.13199 -0.11552 0.04605  0.02396  298 LEU   A N   
2442 C CA  . LEU   A 301 ? 1.56495 1.73441 1.19847 -0.10579 0.04579  0.00701  298 LEU   A CA  
2443 C C   . LEU   A 301 ? 1.71004 1.88046 1.37937 -0.08580 0.02783  -0.00035 298 LEU   A C   
2444 O O   . LEU   A 301 ? 1.76829 1.93495 1.47062 -0.08056 0.02012  0.00543  298 LEU   A O   
2445 C CB  . LEU   A 301 ? 1.55879 1.76947 1.20242 -0.11116 0.06890  -0.00948 298 LEU   A CB  
2446 C CG  . LEU   A 301 ? 1.47321 1.70489 1.11618 -0.09894 0.06965  -0.03029 298 LEU   A CG  
2447 C CD1 . LEU   A 301 ? 1.64084 1.85172 1.23258 -0.10280 0.06489  -0.02830 298 LEU   A CD1 
2448 C CD2 . LEU   A 301 ? 1.39427 1.67077 1.05311 -0.10234 0.09203  -0.04812 298 LEU   A CD2 
2449 N N   . GLY   B 9   ? 1.04692 1.35820 0.95577 0.05200  0.00744  -0.16085 102 GLY   B N   
2450 C CA  . GLY   B 9   ? 1.21650 1.50470 1.11716 0.03619  0.00407  -0.13800 102 GLY   B CA  
2451 C C   . GLY   B 9   ? 1.24065 1.51045 1.16309 0.03274  -0.00404 -0.12355 102 GLY   B C   
2452 O O   . GLY   B 9   ? 1.25046 1.51482 1.18885 0.04340  -0.01154 -0.13059 102 GLY   B O   
2453 N N   . SER   B 10  ? 1.27916 1.53831 1.20046 0.01829  -0.00308 -0.10380 103 SER   B N   
2454 C CA  . SER   B 10  ? 1.09270 1.33715 1.03395 0.01352  -0.00903 -0.08998 103 SER   B CA  
2455 C C   . SER   B 10  ? 1.24705 1.46256 1.18216 0.01076  -0.02463 -0.08179 103 SER   B C   
2456 O O   . SER   B 10  ? 1.20261 1.41238 1.12206 0.00368  -0.02606 -0.07408 103 SER   B O   
2457 C CB  . SER   B 10  ? 1.29861 1.55501 1.24701 0.00016  0.00356  -0.07537 103 SER   B CB  
2458 O OG  . SER   B 10  ? 1.09353 1.33691 1.06074 -0.00376 -0.00185 -0.06323 103 SER   B OG  
2459 N N   . PRO   B 11  ? 1.08901 1.28557 1.03475 0.01533  -0.03701 -0.08345 104 PRO   B N   
2460 C CA  . PRO   B 11  ? 1.06352 1.23620 1.00609 0.01020  -0.05113 -0.07675 104 PRO   B CA  
2461 C C   . PRO   B 11  ? 0.97658 1.14634 0.93522 -0.00123 -0.05103 -0.06004 104 PRO   B C   
2462 O O   . PRO   B 11  ? 0.96061 1.11693 0.91934 -0.00669 -0.06161 -0.05492 104 PRO   B O   
2463 C CB  . PRO   B 11  ? 0.98502 1.13787 0.92941 0.01847  -0.06315 -0.08696 104 PRO   B CB  
2464 C CG  . PRO   B 11  ? 1.00827 1.17219 0.96712 0.02455  -0.05579 -0.09035 104 PRO   B CG  
2465 C CD  . PRO   B 11  ? 1.02396 1.21906 0.98215 0.02553  -0.03963 -0.09314 104 PRO   B CD  
2466 N N   . LEU   B 12  ? 1.00595 1.18932 0.97888 -0.00474 -0.03984 -0.05286 105 LEU   B N   
2467 C CA  . LEU   B 12  ? 0.92451 1.10547 0.91315 -0.01393 -0.03970 -0.03875 105 LEU   B CA  
2468 C C   . LEU   B 12  ? 0.93535 1.11718 0.91443 -0.02003 -0.04028 -0.02956 105 LEU   B C   
2469 O O   . LEU   B 12  ? 1.04885 1.23800 1.01040 -0.02001 -0.03378 -0.03024 105 LEU   B O   
2470 C CB  . LEU   B 12  ? 0.88948 1.08342 0.89359 -0.01546 -0.02808 -0.03458 105 LEU   B CB  
2471 C CG  . LEU   B 12  ? 0.90177 1.09461 0.91527 -0.00827 -0.02857 -0.04304 105 LEU   B CG  
2472 C CD1 . LEU   B 12  ? 0.78001 0.98856 0.80789 -0.01021 -0.01714 -0.03923 105 LEU   B CD1 
2473 C CD2 . LEU   B 12  ? 0.98120 1.15218 1.00035 -0.01004 -0.04039 -0.04143 105 LEU   B CD2 
2474 N N   . PRO   B 13  ? 0.90094 1.07550 0.88994 -0.02527 -0.04831 -0.02154 106 PRO   B N   
2475 C CA  . PRO   B 13  ? 0.91820 1.09196 0.89891 -0.02871 -0.05149 -0.01310 106 PRO   B CA  
2476 C C   . PRO   B 13  ? 0.98034 1.16116 0.96486 -0.03252 -0.04060 -0.00315 106 PRO   B C   
2477 O O   . PRO   B 13  ? 1.05011 1.23912 1.04433 -0.03320 -0.02999 -0.00340 106 PRO   B O   
2478 C CB  . PRO   B 13  ? 1.08456 1.25284 1.08108 -0.03181 -0.06390 -0.01085 106 PRO   B CB  
2479 C CG  . PRO   B 13  ? 0.84301 1.01190 0.86005 -0.03414 -0.06063 -0.01196 106 PRO   B CG  
2480 C CD  . PRO   B 13  ? 1.00157 1.16870 1.00938 -0.02850 -0.05527 -0.02071 106 PRO   B CD  
2481 N N   . VAL   B 14  ? 1.00341 1.17897 0.97885 -0.03465 -0.04485 0.00527  107 VAL   B N   
2482 C CA  . VAL   B 14  ? 1.09770 1.27389 1.07334 -0.03864 -0.03689 0.01532  107 VAL   B CA  
2483 C C   . VAL   B 14  ? 0.99212 1.17340 0.99703 -0.03986 -0.03495 0.01837  107 VAL   B C   
2484 O O   . VAL   B 14  ? 0.94343 1.12426 0.96502 -0.03900 -0.04414 0.01832  107 VAL   B O   
2485 C CB  . VAL   B 14  ? 1.08029 1.24385 1.03740 -0.03879 -0.04560 0.02337  107 VAL   B CB  
2486 C CG1 . VAL   B 14  ? 0.90245 1.05986 0.82423 -0.04048 -0.04262 0.02255  107 VAL   B CG1 
2487 C CG2 . VAL   B 14  ? 1.16434 1.32485 1.13208 -0.03449 -0.06238 0.02131  107 VAL   B CG2 
2488 N N   . LEU   B 15  ? 0.94477 1.13276 0.95612 -0.04265 -0.02259 0.02008  108 LEU   B N   
2489 C CA  . LEU   B 15  ? 0.97141 1.16384 1.00739 -0.04402 -0.01943 0.02252  108 LEU   B CA  
2490 C C   . LEU   B 15  ? 0.96879 1.15665 1.00573 -0.04662 -0.01777 0.03228  108 LEU   B C   
2491 O O   . LEU   B 15  ? 1.06781 1.25108 1.08671 -0.05006 -0.01195 0.03706  108 LEU   B O   
2492 C CB  . LEU   B 15  ? 0.89291 1.09470 0.93584 -0.04425 -0.00898 0.01728  108 LEU   B CB  
2493 C CG  . LEU   B 15  ? 0.92865 1.13229 0.96805 -0.03924 -0.01138 0.00620  108 LEU   B CG  
2494 C CD1 . LEU   B 15  ? 0.81257 1.02578 0.86076 -0.03714 -0.00318 0.00040  108 LEU   B CD1 
2495 C CD2 . LEU   B 15  ? 0.86531 1.05995 0.91283 -0.03806 -0.02306 0.00372  108 LEU   B CD2 
2496 N N   . SER   B 16  ? 0.89397 1.08240 0.95063 -0.04553 -0.02289 0.03458  109 SER   B N   
2497 C CA  . SER   B 16  ? 1.01390 1.19656 1.07262 -0.04560 -0.02313 0.04217  109 SER   B CA  
2498 C C   . SER   B 16  ? 1.01284 1.19842 1.07814 -0.04983 -0.01102 0.04474  109 SER   B C   
2499 O O   . SER   B 16  ? 0.97432 1.15078 1.03173 -0.05166 -0.00893 0.05131  109 SER   B O   
2500 C CB  . SER   B 16  ? 1.05786 1.24466 1.13752 -0.04176 -0.03270 0.04113  109 SER   B CB  
2501 O OG  . SER   B 16  ? 1.12509 1.32317 1.22698 -0.04434 -0.02866 0.03647  109 SER   B OG  
2502 N N   . TRP   B 17  ? 0.94325 1.13898 1.02093 -0.05129 -0.00431 0.03948  110 TRP   B N   
2503 C CA  . TRP   B 17  ? 0.95437 1.15457 1.04061 -0.05470 0.00565  0.04062  110 TRP   B CA  
2504 C C   . TRP   B 17  ? 0.82608 1.03115 0.89931 -0.05881 0.01540  0.03915  110 TRP   B C   
2505 O O   . TRP   B 17  ? 0.97316 1.18190 1.05114 -0.06302 0.02338  0.04063  110 TRP   B O   
2506 C CB  . TRP   B 17  ? 0.84405 1.05123 0.94935 -0.05385 0.00645  0.03570  110 TRP   B CB  
2507 C CG  . TRP   B 17  ? 0.85277 1.06078 0.95677 -0.05141 0.00129  0.02891  110 TRP   B CG  
2508 C CD1 . TRP   B 17  ? 0.99348 1.19841 1.09932 -0.05042 -0.00805 0.02717  110 TRP   B CD1 
2509 C CD2 . TRP   B 17  ? 0.83569 1.04679 0.93612 -0.04930 0.00397  0.02191  110 TRP   B CD2 
2510 N NE1 . TRP   B 17  ? 0.75433 0.95678 0.85551 -0.04899 -0.01122 0.02041  110 TRP   B NE1 
2511 C CE2 . TRP   B 17  ? 0.80074 1.00611 0.89818 -0.04700 -0.00448 0.01685  110 TRP   B CE2 
2512 C CE3 . TRP   B 17  ? 0.72153 0.94041 0.82162 -0.04853 0.01173  0.01828  110 TRP   B CE3 
2513 C CZ2 . TRP   B 17  ? 0.68026 0.88345 0.77205 -0.04265 -0.00619 0.00860  110 TRP   B CZ2 
2514 C CZ3 . TRP   B 17  ? 0.75172 0.97269 0.84899 -0.04311 0.01000  0.00913  110 TRP   B CZ3 
2515 C CH2 . TRP   B 17  ? 0.73040 0.94162 0.82241 -0.03958 0.00073  0.00454  110 TRP   B CH2 
2516 N N   . ALA   B 18  ? 0.84490 1.05212 0.90248 -0.05820 0.01527  0.03522  111 ALA   B N   
2517 C CA  . ALA   B 18  ? 0.93458 1.15161 0.98052 -0.06292 0.02578  0.03190  111 ALA   B CA  
2518 C C   . ALA   B 18  ? 1.09126 1.30704 1.11546 -0.06212 0.02377  0.02885  111 ALA   B C   
2519 O O   . ALA   B 18  ? 1.12146 1.32826 1.14104 -0.05717 0.01326  0.02888  111 ALA   B O   
2520 C CB  . ALA   B 18  ? 0.93364 1.16716 0.99541 -0.06018 0.03133  0.02255  111 ALA   B CB  
2521 N N   . ASN   B 19  ? 1.01361 1.24027 1.02450 -0.06784 0.03435  0.02534  112 ASN   B N   
2522 C CA  . ASN   B 19  ? 1.24121 1.46982 1.23007 -0.06745 0.03462  0.02047  112 ASN   B CA  
2523 C C   . ASN   B 19  ? 1.18842 1.42627 1.18703 -0.05666 0.02960  0.00785  112 ASN   B C   
2524 O O   . ASN   B 19  ? 1.13267 1.38481 1.14866 -0.05235 0.03321  -0.00065 112 ASN   B O   
2525 C CB  . ASN   B 19  ? 1.22522 1.46753 1.19870 -0.07810 0.04947  0.01831  112 ASN   B CB  
2526 C CG  . ASN   B 19  ? 1.49000 1.73554 1.43773 -0.07883 0.05151  0.01273  112 ASN   B CG  
2527 O OD1 . ASN   B 19  ? 1.48980 1.71955 1.42400 -0.07355 0.04047  0.01484  112 ASN   B OD1 
2528 N ND2 . ASN   B 19  ? 1.36094 1.62909 1.30217 -0.08571 0.06582  0.00447  112 ASN   B ND2 
2529 N N   . ARG   B 20  ? 1.16067 1.38790 1.14654 -0.05184 0.01969  0.00638  113 ARG   B N   
2530 C CA  . ARG   B 20  ? 0.99775 1.22754 0.98949 -0.04202 0.01273  -0.00524 113 ARG   B CA  
2531 C C   . ARG   B 20  ? 1.16808 1.41792 1.15735 -0.03831 0.02181  -0.01899 113 ARG   B C   
2532 O O   . ARG   B 20  ? 0.90152 1.15698 0.90485 -0.02958 0.01901  -0.02905 113 ARG   B O   
2533 C CB  . ARG   B 20  ? 1.17584 1.39112 1.15125 -0.03921 0.00084  -0.00489 113 ARG   B CB  
2534 C CG  . ARG   B 20  ? 1.25835 1.46941 1.20434 -0.04481 0.00387  -0.00049 113 ARG   B CG  
2535 C CD  . ARG   B 20  ? 1.27153 1.46943 1.20094 -0.04038 -0.00930 -0.00256 113 ARG   B CD  
2536 N NE  . ARG   B 20  ? 1.32685 1.53041 1.25596 -0.03246 -0.01202 -0.01697 113 ARG   B NE  
2537 C CZ  . ARG   B 20  ? 1.45217 1.66563 1.36275 -0.03072 -0.00506 -0.02696 113 ARG   B CZ  
2538 N NH1 . ARG   B 20  ? 1.50176 1.72184 1.39141 -0.03872 0.00653  -0.02362 113 ARG   B NH1 
2539 N NH2 . ARG   B 20  ? 1.37018 1.58614 1.28173 -0.02126 -0.00975 -0.04118 113 ARG   B NH2 
2540 N N   . GLU   B 21  ? 1.38583 1.64658 1.35627 -0.04484 0.03244  -0.02031 114 GLU   B N   
2541 C CA  . GLU   B 21  ? 1.39491 1.68146 1.36543 -0.04177 0.04281  -0.03546 114 GLU   B CA  
2542 C C   . GLU   B 21  ? 1.41354 1.72027 1.40742 -0.04307 0.05177  -0.03910 114 GLU   B C   
2543 O O   . GLU   B 21  ? 1.35394 1.68324 1.35786 -0.03520 0.05584  -0.05468 114 GLU   B O   
2544 C CB  . GLU   B 21  ? 1.48655 1.78135 1.42908 -0.05154 0.05372  -0.03579 114 GLU   B CB  
2545 C CG  . GLU   B 21  ? 1.65167 1.93218 1.56881 -0.04743 0.04530  -0.03790 114 GLU   B CG  
2546 C CD  . GLU   B 21  ? 1.70302 1.99465 1.62364 -0.03306 0.04138  -0.05680 114 GLU   B CD  
2547 O OE1 . GLU   B 21  ? 1.63292 1.94773 1.57183 -0.02671 0.04768  -0.06974 114 GLU   B OE1 
2548 O OE2 . GLU   B 21  ? 1.82701 2.10338 1.73162 -0.02731 0.03077  -0.05953 114 GLU   B OE2 
2549 N N   . GLU   B 22  ? 1.18777 1.48717 1.19060 -0.05167 0.05384  -0.02631 115 GLU   B N   
2550 C CA  . GLU   B 22  ? 1.06919 1.38670 1.09369 -0.05348 0.06129  -0.02962 115 GLU   B CA  
2551 C C   . GLU   B 22  ? 0.81343 1.12731 0.85942 -0.04025 0.05105  -0.03553 115 GLU   B C   
2552 O O   . GLU   B 22  ? 0.81060 1.14430 0.87128 -0.03332 0.05353  -0.04788 115 GLU   B O   
2553 C CB  . GLU   B 22  ? 1.07218 1.37965 1.09633 -0.06696 0.06600  -0.01442 115 GLU   B CB  
2554 C CG  . GLU   B 22  ? 1.10583 1.43246 1.14989 -0.07141 0.07449  -0.01765 115 GLU   B CG  
2555 C CD  . GLU   B 22  ? 1.14933 1.46114 1.19153 -0.08393 0.07731  -0.00291 115 GLU   B CD  
2556 O OE1 . GLU   B 22  ? 1.14910 1.43412 1.18064 -0.08469 0.06945  0.00927  115 GLU   B OE1 
2557 O OE2 . GLU   B 22  ? 1.09567 1.42295 1.14743 -0.09245 0.08658  -0.00456 115 GLU   B OE2 
2558 N N   . VAL   B 23  ? 0.78767 1.07627 0.83478 -0.03702 0.03904  -0.02730 116 VAL   B N   
2559 C CA  . VAL   B 23  ? 0.73451 1.01436 0.79649 -0.02731 0.02922  -0.03126 116 VAL   B CA  
2560 C C   . VAL   B 23  ? 0.87731 1.16192 0.93637 -0.01401 0.02356  -0.04731 116 VAL   B C   
2561 O O   . VAL   B 23  ? 0.56374 0.85275 0.63427 -0.00473 0.01996  -0.05633 116 VAL   B O   
2562 C CB  . VAL   B 23  ? 0.66873 0.92327 0.73065 -0.02933 0.01894  -0.02021 116 VAL   B CB  
2563 C CG1 . VAL   B 23  ? 0.71016 0.95244 0.78179 -0.02208 0.00925  -0.02406 116 VAL   B CG1 
2564 C CG2 . VAL   B 23  ? 0.67906 0.92980 0.74606 -0.03935 0.02347  -0.00674 116 VAL   B CG2 
2565 N N   . TRP   B 24  ? 0.69163 0.97363 0.73358 -0.01184 0.02147  -0.05175 117 TRP   B N   
2566 C CA  . TRP   B 24  ? 0.72587 1.01021 0.76284 0.00200  0.01516  -0.06828 117 TRP   B CA  
2567 C C   . TRP   B 24  ? 0.81829 1.13525 0.86295 0.00798  0.02498  -0.08369 117 TRP   B C   
2568 O O   . TRP   B 24  ? 0.60712 0.92805 0.65842 0.02280  0.01829  -0.09839 117 TRP   B O   
2569 C CB  . TRP   B 24  ? 0.74896 1.02348 0.76440 0.00204  0.01110  -0.06961 117 TRP   B CB  
2570 C CG  . TRP   B 24  ? 0.79937 1.07055 0.80715 0.01676  0.00249  -0.08656 117 TRP   B CG  
2571 C CD1 . TRP   B 24  ? 0.95364 1.24498 0.95180 0.02381  0.00820  -0.10215 117 TRP   B CD1 
2572 C CD2 . TRP   B 24  ? 0.77899 1.02353 0.78619 0.02593  -0.01365 -0.09037 117 TRP   B CD2 
2573 N NE1 . TRP   B 24  ? 0.86995 1.14817 0.86227 0.03901  -0.00447 -0.11619 117 TRP   B NE1 
2574 C CE2 . TRP   B 24  ? 0.83712 1.08426 0.83354 0.03991  -0.01846 -0.10860 117 TRP   B CE2 
2575 C CE3 . TRP   B 24  ? 0.82091 1.03917 0.83409 0.02258  -0.02410 -0.08056 117 TRP   B CE3 
2576 C CZ2 . TRP   B 24  ? 0.92093 1.14073 0.91068 0.05095  -0.03487 -0.11652 117 TRP   B CZ2 
2577 C CZ3 . TRP   B 24  ? 0.93388 1.12640 0.93989 0.03110  -0.03899 -0.08770 117 TRP   B CZ3 
2578 C CH2 . TRP   B 24  ? 0.77229 0.96345 0.76585 0.04533  -0.04502 -0.10514 117 TRP   B CH2 
2579 N N   . LYS   B 25  ? 0.91163 1.25201 0.95503 -0.00362 0.04029  -0.08124 118 LYS   B N   
2580 C CA  . LYS   B 25  ? 0.68000 1.05787 0.73371 -0.00076 0.05155  -0.09688 118 LYS   B CA  
2581 C C   . LYS   B 25  ? 0.69366 1.08038 0.77177 0.00614  0.04844  -0.10158 118 LYS   B C   
2582 O O   . LYS   B 25  ? 0.71463 1.12327 0.80435 0.01986  0.04697  -0.12006 118 LYS   B O   
2583 C CB  . LYS   B 25  ? 0.91706 1.31458 0.96247 -0.01944 0.06917  -0.09071 118 LYS   B CB  
2584 C CG  . LYS   B 25  ? 1.10480 1.53579 1.14205 -0.01956 0.08145  -0.10735 118 LYS   B CG  
2585 C CD  . LYS   B 25  ? 1.23677 1.65253 1.24840 -0.01509 0.07644  -0.10969 118 LYS   B CD  
2586 C CE  . LYS   B 25  ? 1.20088 1.65075 1.20091 -0.01772 0.09100  -0.12560 118 LYS   B CE  
2587 N NZ  . LYS   B 25  ? 1.30208 1.73539 1.27346 -0.01463 0.08637  -0.12711 118 LYS   B NZ  
2588 N N   . ILE   B 26  ? 0.61574 0.98590 0.70138 -0.00212 0.04658  -0.08603 119 ILE   B N   
2589 C CA  . ILE   B 26  ? 0.69380 1.06847 0.79949 0.00377  0.04255  -0.08913 119 ILE   B CA  
2590 C C   . ILE   B 26  ? 0.58249 0.93915 0.68896 0.02268  0.02588  -0.09874 119 ILE   B C   
2591 O O   . ILE   B 26  ? 0.63346 1.00406 0.75272 0.03542  0.02144  -0.11241 119 ILE   B O   
2592 C CB  . ILE   B 26  ? 0.72843 1.08507 0.83828 -0.00885 0.04338  -0.07030 119 ILE   B CB  
2593 C CG1 . ILE   B 26  ? 0.74747 1.11918 0.85476 -0.02683 0.05862  -0.06210 119 ILE   B CG1 
2594 C CG2 . ILE   B 26  ? 0.64298 0.99894 0.76966 -0.00217 0.03726  -0.07292 119 ILE   B CG2 
2595 C CD1 . ILE   B 26  ? 0.73256 1.08216 0.83923 -0.03824 0.05840  -0.04363 119 ILE   B CD1 
2596 N N   . MET   B 27  ? 0.58462 0.90878 0.67626 0.02463  0.01533  -0.09221 120 MET   B N   
2597 C CA  . MET   B 27  ? 0.60388 0.90429 0.69080 0.04031  -0.00131 -0.10037 120 MET   B CA  
2598 C C   . MET   B 27  ? 0.66211 0.98076 0.74766 0.05765  -0.00415 -0.12264 120 MET   B C   
2599 O O   . MET   B 27  ? 0.57702 0.88945 0.66620 0.07424  -0.01600 -0.13477 120 MET   B O   
2600 C CB  . MET   B 27  ? 0.64607 0.91096 0.71696 0.03559  -0.01058 -0.08967 120 MET   B CB  
2601 C CG  . MET   B 27  ? 0.67243 0.92057 0.74690 0.02093  -0.00945 -0.07037 120 MET   B CG  
2602 S SD  . MET   B 27  ? 0.74501 0.96106 0.80496 0.01377  -0.01896 -0.06021 120 MET   B SD  
2603 C CE  . MET   B 27  ? 0.90357 1.08863 0.95337 0.02638  -0.03673 -0.06980 120 MET   B CE  
2604 N N   . LEU   B 28  ? 0.56888 0.90953 0.64768 0.05472  0.00608  -0.12901 121 LEU   B N   
2605 C CA  . LEU   B 28  ? 0.74205 1.10621 0.82095 0.07121  0.00557  -0.15239 121 LEU   B CA  
2606 C C   . LEU   B 28  ? 0.71919 1.12519 0.82097 0.07658  0.01364  -0.16633 121 LEU   B C   
2607 O O   . LEU   B 28  ? 0.73681 1.15406 0.84656 0.09702  0.00492  -0.18645 121 LEU   B O   
2608 C CB  . LEU   B 28  ? 0.58352 0.96062 0.64648 0.06465  0.01575  -0.15520 121 LEU   B CB  
2609 C CG  . LEU   B 28  ? 0.72463 1.06526 0.76465 0.06232  0.00620  -0.14649 121 LEU   B CG  
2610 C CD1 . LEU   B 28  ? 0.90242 1.25978 0.92535 0.05910  0.01568  -0.15355 121 LEU   B CD1 
2611 C CD2 . LEU   B 28  ? 0.73393 1.04218 0.76798 0.07970  -0.01412 -0.15479 121 LEU   B CD2 
2612 N N   . ASN   B 29  ? 0.65674 1.08584 0.76925 0.05882  0.02921  -0.15685 122 ASN   B N   
2613 C CA  . ASN   B 29  ? 0.81975 1.29163 0.95577 0.06079  0.03765  -0.17004 122 ASN   B CA  
2614 C C   . ASN   B 29  ? 0.75527 1.21665 0.90615 0.07450  0.02317  -0.17352 122 ASN   B C   
2615 O O   . ASN   B 29  ? 0.79593 1.29159 0.96677 0.08532  0.02345  -0.19143 122 ASN   B O   
2616 C CB  . ASN   B 29  ? 0.91047 1.40224 1.05100 0.03585  0.05646  -0.15703 122 ASN   B CB  
2617 C CG  . ASN   B 29  ? 1.03654 1.54569 1.16124 0.02228  0.07227  -0.15725 122 ASN   B CG  
2618 O OD1 . ASN   B 29  ? 0.96737 1.49478 1.08675 0.03248  0.07390  -0.17451 122 ASN   B OD1 
2619 N ND2 . ASN   B 29  ? 1.11456 1.61608 1.22923 -0.00044 0.08337  -0.13839 122 ASN   B ND2 
2620 N N   . LYS   B 30  ? 0.87799 1.29397 1.01904 0.07388  0.01045  -0.15749 123 LYS   B N   
2621 C CA  . LYS   B 30  ? 0.93578 1.33574 1.08463 0.08639  -0.00441 -0.15982 123 LYS   B CA  
2622 C C   . LYS   B 30  ? 0.90247 1.29791 1.04878 0.11316  -0.02107 -0.18125 123 LYS   B C   
2623 O O   . LYS   B 30  ? 0.97253 1.37768 1.13166 0.12828  -0.03053 -0.19363 123 LYS   B O   
2624 C CB  . LYS   B 30  ? 1.03214 1.38438 1.16757 0.07727  -0.01260 -0.13797 123 LYS   B CB  
2625 C CG  . LYS   B 30  ? 1.05343 1.38126 1.18943 0.08862  -0.02877 -0.13854 123 LYS   B CG  
2626 C CD  . LYS   B 30  ? 0.93531 1.21816 1.05617 0.07723  -0.03475 -0.11782 123 LYS   B CD  
2627 C CE  . LYS   B 30  ? 0.86604 1.15780 0.99544 0.05611  -0.02025 -0.10058 123 LYS   B CE  
2628 N NZ  . LYS   B 30  ? 1.08237 1.39569 1.22910 0.05606  -0.01692 -0.10338 123 LYS   B NZ  
2629 N N   . GLU   B 31  ? 1.09482 1.47436 1.22373 0.12040  -0.02622 -0.18674 124 GLU   B N   
2630 C CA  . GLU   B 31  ? 1.17490 1.54609 1.29850 0.14714  -0.04334 -0.20812 124 GLU   B CA  
2631 C C   . GLU   B 31  ? 1.19116 1.61786 1.33651 0.16202  -0.03723 -0.23480 124 GLU   B C   
2632 O O   . GLU   B 31  ? 1.30848 1.73411 1.45584 0.18797  -0.05323 -0.25540 124 GLU   B O   
2633 C CB  . GLU   B 31  ? 1.31527 1.65676 1.41434 0.14977  -0.04953 -0.20811 124 GLU   B CB  
2634 C CG  . GLU   B 31  ? 1.24197 1.52788 1.32049 0.13841  -0.05956 -0.18617 124 GLU   B CG  
2635 C CD  . GLU   B 31  ? 1.38784 1.64155 1.44233 0.14406  -0.07017 -0.18969 124 GLU   B CD  
2636 O OE1 . GLU   B 31  ? 1.34524 1.62224 1.39748 0.15050  -0.06434 -0.20401 124 GLU   B OE1 
2637 O OE2 . GLU   B 31  ? 1.32470 1.52990 1.36159 0.14099  -0.08410 -0.17862 124 GLU   B OE2 
2638 N N   . LYS   B 32  ? 1.19128 1.66615 1.35217 0.14603  -0.01490 -0.23568 125 LYS   B N   
2639 C CA  . LYS   B 32  ? 0.99231 1.52672 1.17838 0.15643  -0.00695 -0.26111 125 LYS   B CA  
2640 C C   . LYS   B 32  ? 0.99832 1.54775 1.20764 0.16300  -0.01355 -0.26573 125 LYS   B C   
2641 O O   . LYS   B 32  ? 1.13274 1.72386 1.36390 0.18088  -0.01629 -0.29123 125 LYS   B O   
2642 C CB  . LYS   B 32  ? 1.08946 1.66860 1.28142 0.13329  0.01997  -0.25960 125 LYS   B CB  
2643 C CG  . LYS   B 32  ? 1.09438 1.66921 1.26420 0.12990  0.02705  -0.26122 125 LYS   B CG  
2644 C CD  . LYS   B 32  ? 1.25603 1.87509 1.42845 0.10656  0.05359  -0.26075 125 LYS   B CD  
2645 C CE  . LYS   B 32  ? 1.42683 2.04397 1.57513 0.10491  0.06016  -0.26499 125 LYS   B CE  
2646 N NZ  . LYS   B 32  ? 1.42310 1.98154 1.54329 0.09903  0.05007  -0.24238 125 LYS   B NZ  
2647 N N   . THR   B 33  ? 0.95253 1.47062 1.15802 0.14959  -0.01657 -0.24294 126 THR   B N   
2648 C CA  . THR   B 33  ? 0.87182 1.39870 1.09568 0.15570  -0.02456 -0.24611 126 THR   B CA  
2649 C C   . THR   B 33  ? 0.90341 1.39196 1.11715 0.18315  -0.05235 -0.25446 126 THR   B C   
2650 O O   . THR   B 33  ? 0.96919 1.47831 1.20028 0.20152  -0.06338 -0.27191 126 THR   B O   
2651 C CB  . THR   B 33  ? 1.00060 1.50840 1.22216 0.13073  -0.01659 -0.21933 126 THR   B CB  
2652 O OG1 . THR   B 33  ? 0.92327 1.45959 1.14930 0.10566  0.00724  -0.21094 126 THR   B OG1 
2653 C CG2 . THR   B 33  ? 1.00167 1.52224 1.24219 0.13545  -0.02346 -0.22336 126 THR   B CG2 
2654 N N   . TYR   B 34  ? 0.91404 1.34587 1.09858 0.18585  -0.06480 -0.24260 127 TYR   B N   
2655 C CA  . TYR   B 34  ? 0.79245 1.17687 0.95931 0.20864  -0.09194 -0.24741 127 TYR   B CA  
2656 C C   . TYR   B 34  ? 0.89509 1.28461 1.05723 0.23493  -0.10316 -0.27272 127 TYR   B C   
2657 O O   . TYR   B 34  ? 0.94201 1.31839 1.08820 0.23139  -0.09933 -0.27118 127 TYR   B O   
2658 C CB  . TYR   B 34  ? 0.83869 1.15863 0.97549 0.19472  -0.09896 -0.22143 127 TYR   B CB  
2659 C CG  . TYR   B 34  ? 0.78941 1.09986 0.92933 0.17358  -0.09184 -0.19912 127 TYR   B CG  
2660 C CD1 . TYR   B 34  ? 0.65191 0.98533 0.80208 0.14785  -0.06935 -0.18407 127 TYR   B CD1 
2661 C CD2 . TYR   B 34  ? 0.71028 0.98642 0.84026 0.17992  -0.10841 -0.19355 127 TYR   B CD2 
2662 C CE1 . TYR   B 34  ? 0.72712 1.05149 0.87996 0.13023  -0.06349 -0.16539 127 TYR   B CE1 
2663 C CE2 . TYR   B 34  ? 0.62350 0.89190 0.75541 0.16108  -0.10146 -0.17450 127 TYR   B CE2 
2664 C CZ  . TYR   B 34  ? 0.66880 0.96231 0.81335 0.13688  -0.07895 -0.16113 127 TYR   B CZ  
2665 O OH  . TYR   B 34  ? 0.55063 0.83596 0.69690 0.11978  -0.07270 -0.14377 127 TYR   B OH  
2666 N N   . LEU   B 35  ? 0.84540 1.25406 1.02132 0.26239  -0.11804 -0.29708 128 LEU   B N   
2667 C CA  . LEU   B 35  ? 0.91362 1.33204 1.08849 0.29162  -0.13019 -0.32539 128 LEU   B CA  
2668 C C   . LEU   B 35  ? 0.93515 1.28620 1.08026 0.31547  -0.16230 -0.32770 128 LEU   B C   
2669 O O   . LEU   B 35  ? 1.07856 1.39473 1.21449 0.31777  -0.17747 -0.31740 128 LEU   B O   
2670 C CB  . LEU   B 35  ? 0.92749 1.41792 1.13984 0.30913  -0.12615 -0.35551 128 LEU   B CB  
2671 C CG  . LEU   B 35  ? 0.92517 1.48898 1.16434 0.29241  -0.09574 -0.36467 128 LEU   B CG  
2672 C CD1 . LEU   B 35  ? 0.99039 1.56791 1.23814 0.25642  -0.07320 -0.33920 128 LEU   B CD1 
2673 C CD2 . LEU   B 35  ? 1.00097 1.63329 1.27550 0.31545  -0.09652 -0.40036 128 LEU   B CD2 
2674 N N   . ARG   B 36  ? 0.92611 1.25643 1.05320 0.33257  -0.17292 -0.34134 129 ARG   B N   
2675 C CA  . ARG   B 36  ? 1.08295 1.34721 1.17847 0.35695  -0.20472 -0.34682 129 ARG   B CA  
2676 C C   . ARG   B 36  ? 1.11224 1.39965 1.21479 0.39286  -0.21753 -0.38288 129 ARG   B C   
2677 O O   . ARG   B 36  ? 1.00324 1.33732 1.12011 0.39251  -0.20050 -0.39738 129 ARG   B O   
2678 C CB  . ARG   B 36  ? 1.20038 1.39688 1.25716 0.33958  -0.20886 -0.32379 129 ARG   B CB  
2679 C CG  . ARG   B 36  ? 1.25054 1.41038 1.29442 0.30999  -0.20405 -0.29036 129 ARG   B CG  
2680 C CD  . ARG   B 36  ? 1.15970 1.35885 1.22181 0.27746  -0.17303 -0.27265 129 ARG   B CD  
2681 N NE  . ARG   B 36  ? 1.00445 1.17625 1.05908 0.25202  -0.16815 -0.24407 129 ARG   B NE  
2682 C CZ  . ARG   B 36  ? 1.09261 1.28169 1.15585 0.22309  -0.14572 -0.22445 129 ARG   B CZ  
2683 N NH1 . ARG   B 36  ? 1.01705 1.24650 1.09340 0.21395  -0.12632 -0.22790 129 ARG   B NH1 
2684 N NH2 . ARG   B 36  ? 0.98900 1.15299 1.04567 0.20336  -0.14329 -0.20131 129 ARG   B NH2 
2685 N N   . ASP   B 37  ? 1.14562 1.39917 1.23626 0.42436  -0.24817 -0.39784 130 ASP   B N   
2686 C CA  . ASP   B 37  ? 1.22055 1.49073 1.31687 0.46400  -0.26560 -0.43455 130 ASP   B CA  
2687 C C   . ASP   B 37  ? 1.15750 1.33837 1.20633 0.48211  -0.29751 -0.43342 130 ASP   B C   
2688 O O   . ASP   B 37  ? 1.07219 1.19367 1.09628 0.48825  -0.32120 -0.42239 130 ASP   B O   
2689 C CB  . ASP   B 37  ? 1.08919 1.40377 1.21409 0.48322  -0.27498 -0.45442 130 ASP   B CB  
2690 C CG  . ASP   B 37  ? 1.33140 1.68486 1.46528 0.50181  -0.28157 -0.48435 130 ASP   B CG  
2691 O OD1 . ASP   B 37  ? 1.27336 1.59526 1.38338 0.51596  -0.29396 -0.49353 130 ASP   B OD1 
2692 O OD2 . ASP   B 37  ? 1.31150 1.72712 1.47630 0.50176  -0.27477 -0.49910 130 ASP   B OD2 
2693 N N   . GLN   B 38  ? 1.06534 1.23426 1.09870 0.48967  -0.29849 -0.44472 131 GLN   B N   
2694 C CA  . GLN   B 38  ? 1.20429 1.28571 1.19017 0.50440  -0.32828 -0.44378 131 GLN   B CA  
2695 C C   . GLN   B 38  ? 1.27197 1.33101 1.24581 0.53668  -0.36180 -0.46252 131 GLN   B C   
2696 O O   . GLN   B 38  ? 1.28685 1.26599 1.21666 0.54639  -0.38992 -0.45784 131 GLN   B O   
2697 C CB  . GLN   B 38  ? 1.32702 1.40527 1.29973 0.50213  -0.32059 -0.45137 131 GLN   B CB  
2698 C CG  . GLN   B 38  ? 1.25329 1.40538 1.25499 0.52014  -0.31123 -0.48241 131 GLN   B CG  
2699 C CD  . GLN   B 38  ? 1.33890 1.57676 1.38037 0.49960  -0.27250 -0.48364 131 GLN   B CD  
2700 O OE1 . GLN   B 38  ? 1.28052 1.53516 1.33649 0.47306  -0.25476 -0.46131 131 GLN   B OE1 
2701 N NE2 . GLN   B 38  ? 1.18480 1.47489 1.23971 0.50187  -0.25905 -0.50165 131 GLN   B NE2 
2702 N N   . HIS   B 39  ? 1.26667 1.39266 1.27460 0.54690  -0.35927 -0.48029 132 HIS   B N   
2703 C CA  . HIS   B 39  ? 1.25620 1.36898 1.25354 0.57325  -0.38997 -0.49812 132 HIS   B CA  
2704 C C   . HIS   B 39  ? 1.35279 1.48865 1.36872 0.57311  -0.39300 -0.49700 132 HIS   B C   
2705 O O   . HIS   B 39  ? 1.28850 1.46462 1.32192 0.58967  -0.40252 -0.51943 132 HIS   B O   
2706 C CB  . HIS   B 39  ? 1.38450 1.55629 1.40248 0.59004  -0.38819 -0.52822 132 HIS   B CB  
2707 C CG  . HIS   B 39  ? 1.33846 1.48284 1.33428 0.59398  -0.39003 -0.53161 132 HIS   B CG  
2708 N ND1 . HIS   B 39  ? 1.36115 1.56772 1.38001 0.59765  -0.37405 -0.55184 132 HIS   B ND1 
2709 C CD2 . HIS   B 39  ? 1.46520 1.52533 1.41627 0.59322  -0.40596 -0.51724 132 HIS   B CD2 
2710 C CE1 . HIS   B 39  ? 1.49266 1.65502 1.48257 0.60060  -0.38033 -0.55015 132 HIS   B CE1 
2711 N NE2 . HIS   B 39  ? 1.49048 1.56371 1.43927 0.59745  -0.39975 -0.52943 132 HIS   B NE2 
2712 N N   . PHE   B 40  ? 1.30503 1.41575 1.31727 0.55437  -0.38534 -0.47154 133 PHE   B N   
2713 C CA  . PHE   B 40  ? 1.29916 1.42608 1.32570 0.55334  -0.38919 -0.46872 133 PHE   B CA  
2714 C C   . PHE   B 40  ? 1.22585 1.28928 1.21480 0.57519  -0.42769 -0.47390 133 PHE   B C   
2715 O O   . PHE   B 40  ? 1.32322 1.40672 1.32411 0.58139  -0.43513 -0.48105 133 PHE   B O   
2716 C CB  . PHE   B 40  ? 1.15545 1.26944 1.18594 0.52811  -0.37267 -0.43902 133 PHE   B CB  
2717 C CG  . PHE   B 40  ? 1.16525 1.18055 1.14614 0.52303  -0.39033 -0.41395 133 PHE   B CG  
2718 C CD1 . PHE   B 40  ? 1.18026 1.12966 1.12541 0.52920  -0.41788 -0.40371 133 PHE   B CD1 
2719 C CD2 . PHE   B 40  ? 1.27233 1.26022 1.23674 0.50195  -0.37631 -0.39703 133 PHE   B CD2 
2720 C CE1 . PHE   B 40  ? 1.24462 1.10153 1.14048 0.51966  -0.43275 -0.37912 133 PHE   B CE1 
2721 C CE2 . PHE   B 40  ? 1.32609 1.22592 1.24074 0.48354  -0.38819 -0.36983 133 PHE   B CE2 
2722 C CZ  . PHE   B 40  ? 1.18686 1.02109 1.06733 0.49256  -0.41601 -0.36116 133 PHE   B CZ  
2723 N N   . LEU   B 41  ? 1.29284 1.27848 1.23451 0.58573  -0.45242 -0.47043 134 LEU   B N   
2724 C CA  . LEU   B 41  ? 1.47130 1.39178 1.37131 0.60564  -0.49026 -0.47531 134 LEU   B CA  
2725 C C   . LEU   B 41  ? 1.48762 1.45305 1.40399 0.63346  -0.50521 -0.50973 134 LEU   B C   
2726 O O   . LEU   B 41  ? 1.51518 1.44014 1.40410 0.65170  -0.53571 -0.51777 134 LEU   B O   
2727 C CB  . LEU   B 41  ? 1.43130 1.25624 1.27451 0.60552  -0.51137 -0.46112 134 LEU   B CB  
2728 C CG  . LEU   B 41  ? 1.44821 1.20995 1.26354 0.57833  -0.50448 -0.42619 134 LEU   B CG  
2729 C CD1 . LEU   B 41  ? 1.50486 1.17938 1.26682 0.57436  -0.52184 -0.41424 134 LEU   B CD1 
2730 C CD2 . LEU   B 41  ? 1.45807 1.18565 1.25590 0.57345  -0.51666 -0.41170 134 LEU   B CD2 
2731 N N   . GLU   B 42  ? 1.48295 1.52960 1.44129 0.63662  -0.48493 -0.53051 135 GLU   B N   
2732 C CA  . GLU   B 42  ? 1.40614 1.50643 1.38655 0.66074  -0.49596 -0.56421 135 GLU   B CA  
2733 C C   . GLU   B 42  ? 1.48903 1.63212 1.49647 0.66073  -0.49363 -0.57165 135 GLU   B C   
2734 O O   . GLU   B 42  ? 1.46826 1.63108 1.48098 0.68376  -0.51313 -0.59763 135 GLU   B O   
2735 C CB  . GLU   B 42  ? 1.36894 1.54837 1.38780 0.65933  -0.47129 -0.58264 135 GLU   B CB  
2736 C CG  . GLU   B 42  ? 1.37699 1.51810 1.36970 0.66431  -0.47665 -0.58120 135 GLU   B CG  
2737 C CD  . GLU   B 42  ? 1.38040 1.60017 1.40950 0.66189  -0.45112 -0.59924 135 GLU   B CD  
2738 O OE1 . GLU   B 42  ? 1.31532 1.61846 1.38917 0.65232  -0.42690 -0.61010 135 GLU   B OE1 
2739 O OE2 . GLU   B 42  ? 1.62808 1.82474 1.63910 0.66809  -0.45510 -0.60215 135 GLU   B OE2 
2740 N N   . GLN   B 43  ? 1.41217 1.56990 1.43674 0.63583  -0.47087 -0.55012 136 GLN   B N   
2741 C CA  . GLN   B 43  ? 1.39411 1.57969 1.43830 0.63367  -0.47028 -0.55259 136 GLN   B CA  
2742 C C   . GLN   B 43  ? 1.34408 1.44658 1.34233 0.64570  -0.50389 -0.54368 136 GLN   B C   
2743 O O   . GLN   B 43  ? 1.28449 1.40307 1.29315 0.65073  -0.51072 -0.55092 136 GLN   B O   
2744 C CB  . GLN   B 43  ? 1.34704 1.57214 1.42230 0.60219  -0.43553 -0.53072 136 GLN   B CB  
2745 C CG  . GLN   B 43  ? 1.39240 1.69578 1.50887 0.58561  -0.40014 -0.53629 136 GLN   B CG  
2746 C CD  . GLN   B 43  ? 1.31204 1.64698 1.45398 0.55388  -0.36791 -0.51302 136 GLN   B CD  
2747 O OE1 . GLN   B 43  ? 1.37137 1.76524 1.54321 0.53594  -0.33753 -0.51357 136 GLN   B OE1 
2748 N NE2 . GLN   B 43  ? 1.28938 1.58395 1.41752 0.54622  -0.37491 -0.49214 136 GLN   B NE2 
2749 N N   . HIS   B 44  ? 1.33867 1.35145 1.28449 0.64872  -0.52462 -0.52782 137 HIS   B N   
2750 C CA  . HIS   B 44  ? 1.40726 1.33103 1.30007 0.65752  -0.55751 -0.51758 137 HIS   B CA  
2751 C C   . HIS   B 44  ? 1.47077 1.34003 1.32214 0.68148  -0.58974 -0.53174 137 HIS   B C   
2752 O O   . HIS   B 44  ? 1.58857 1.38800 1.39852 0.67463  -0.59830 -0.51385 137 HIS   B O   
2753 C CB  . HIS   B 44  ? 1.43877 1.29758 1.30116 0.63169  -0.55118 -0.47973 137 HIS   B CB  
2754 C CG  . HIS   B 44  ? 1.39319 1.30872 1.29837 0.60648  -0.51643 -0.46407 137 HIS   B CG  
2755 N ND1 . HIS   B 44  ? 1.19873 1.12657 1.11529 0.59907  -0.51331 -0.45643 137 HIS   B ND1 
2756 C CD2 . HIS   B 44  ? 1.39389 1.35654 1.33201 0.58701  -0.48413 -0.45484 137 HIS   B CD2 
2757 C CE1 . HIS   B 44  ? 1.14688 1.12763 1.10201 0.57584  -0.48107 -0.44273 137 HIS   B CE1 
2758 N NE2 . HIS   B 44  ? 1.36101 1.36343 1.32948 0.56816  -0.46290 -0.44162 137 HIS   B NE2 
2759 N N   . PRO   B 45  ? 1.65269 1.55181 1.51359 0.70942  -0.60882 -0.56410 138 PRO   B N   
2760 C CA  . PRO   B 45  ? 1.61393 1.47075 1.44039 0.73402  -0.63887 -0.58037 138 PRO   B CA  
2761 C C   . PRO   B 45  ? 1.56407 1.30565 1.31886 0.73700  -0.67250 -0.56280 138 PRO   B C   
2762 O O   . PRO   B 45  ? 1.76837 1.46112 1.48767 0.74885  -0.69335 -0.56641 138 PRO   B O   
2763 C CB  . PRO   B 45  ? 1.54695 1.46339 1.40141 0.76266  -0.65251 -0.61871 138 PRO   B CB  
2764 C CG  . PRO   B 45  ? 1.55479 1.56503 1.47010 0.74813  -0.61920 -0.62359 138 PRO   B CG  
2765 C CD  . PRO   B 45  ? 1.51411 1.49166 1.42026 0.71938  -0.60287 -0.58853 138 PRO   B CD  
2766 N N   . LEU   B 46  ? 1.62610 1.32177 1.35669 0.72535  -0.67826 -0.54348 139 LEU   B N   
2767 C CA  . LEU   B 46  ? 1.73937 1.32409 1.39799 0.72496  -0.70957 -0.52618 139 LEU   B CA  
2768 C C   . LEU   B 46  ? 1.79495 1.31667 1.41979 0.69594  -0.69923 -0.49120 139 LEU   B C   
2769 O O   . LEU   B 46  ? 1.83771 1.26507 1.39907 0.69233  -0.72409 -0.47621 139 LEU   B O   
2770 C CB  . LEU   B 46  ? 1.92413 1.48410 1.56774 0.72418  -0.72060 -0.52077 139 LEU   B CB  
2771 C CG  . LEU   B 46  ? 1.93999 1.39548 1.51008 0.73358  -0.76043 -0.51541 139 LEU   B CG  
2772 C CD1 . LEU   B 46  ? 1.96384 1.41155 1.51833 0.76891  -0.79338 -0.54759 139 LEU   B CD1 
2773 C CD2 . LEU   B 46  ? 1.77520 1.21565 1.33672 0.73102  -0.76640 -0.50994 139 LEU   B CD2 
2774 N N   . LEU   B 47  ? 1.74637 1.31689 1.41031 0.67447  -0.66371 -0.47843 140 LEU   B N   
2775 C CA  . LEU   B 47  ? 1.70252 1.21951 1.33933 0.64622  -0.65186 -0.44660 140 LEU   B CA  
2776 C C   . LEU   B 47  ? 1.68578 1.19981 1.31902 0.65078  -0.65139 -0.45294 140 LEU   B C   
2777 O O   . LEU   B 47  ? 1.66534 1.24096 1.33248 0.67158  -0.64939 -0.48048 140 LEU   B O   
2778 C CB  . LEU   B 47  ? 1.58888 1.15526 1.26738 0.61999  -0.61464 -0.42803 140 LEU   B CB  
2779 C CG  . LEU   B 47  ? 1.61356 1.17870 1.29437 0.61045  -0.61202 -0.41591 140 LEU   B CG  
2780 C CD1 . LEU   B 47  ? 1.44225 1.06086 1.16677 0.58557  -0.57529 -0.39826 140 LEU   B CD1 
2781 C CD2 . LEU   B 47  ? 1.58305 1.04125 1.19333 0.59997  -0.63676 -0.39301 140 LEU   B CD2 
2782 N N   . GLN   B 48  ? 1.77671 1.21828 1.36779 0.62952  -0.65267 -0.42693 141 GLN   B N   
2783 C CA  . GLN   B 48  ? 1.83734 1.26413 1.41883 0.62940  -0.65200 -0.42834 141 GLN   B CA  
2784 C C   . GLN   B 48  ? 1.81021 1.23560 1.40147 0.59726  -0.62164 -0.40317 141 GLN   B C   
2785 O O   . GLN   B 48  ? 1.76231 1.16305 1.34439 0.57290  -0.61094 -0.37845 141 GLN   B O   
2786 C CB  . GLN   B 48  ? 1.95289 1.28144 1.46482 0.63525  -0.68825 -0.42312 141 GLN   B CB  
2787 C CG  . GLN   B 48  ? 1.96949 1.29211 1.46635 0.66952  -0.72209 -0.44994 141 GLN   B CG  
2788 C CD  . GLN   B 48  ? 1.97782 1.38321 1.52306 0.69872  -0.71904 -0.48496 141 GLN   B CD  
2789 O OE1 . GLN   B 48  ? 2.09560 1.53335 1.66375 0.69623  -0.70200 -0.48867 141 GLN   B OE1 
2790 N NE2 . GLN   B 48  ? 1.91201 1.35258 1.47248 0.72570  -0.73513 -0.51151 141 GLN   B NE2 
2791 N N   . PRO   B 49  ? 1.87214 1.32408 1.48173 0.59661  -0.60734 -0.40982 142 PRO   B N   
2792 C CA  . PRO   B 49  ? 1.69013 1.14150 1.30921 0.56648  -0.57848 -0.38865 142 PRO   B CA  
2793 C C   . PRO   B 49  ? 1.68349 1.03667 1.24495 0.53807  -0.58754 -0.35718 142 PRO   B C   
2794 O O   . PRO   B 49  ? 1.67794 1.02613 1.24517 0.50939  -0.56500 -0.33609 142 PRO   B O   
2795 C CB  . PRO   B 49  ? 1.73332 1.22157 1.37265 0.57574  -0.56876 -0.40622 142 PRO   B CB  
2796 C CG  . PRO   B 49  ? 1.72967 1.27725 1.39626 0.60957  -0.57988 -0.43873 142 PRO   B CG  
2797 C CD  . PRO   B 49  ? 1.84738 1.34269 1.47658 0.62359  -0.61360 -0.43947 142 PRO   B CD  
2798 N N   . LYS   B 50  ? 1.68536 0.96071 1.19032 0.54353  -0.61960 -0.35366 143 LYS   B N   
2799 C CA  . LYS   B 50  ? 1.74340 0.92629 1.19082 0.51232  -0.62716 -0.32321 143 LYS   B CA  
2800 C C   . LYS   B 50  ? 1.86846 1.02939 1.30339 0.49257  -0.62307 -0.30167 143 LYS   B C   
2801 O O   . LYS   B 50  ? 1.78760 0.89871 1.19430 0.45782  -0.61399 -0.27392 143 LYS   B O   
2802 C CB  . LYS   B 50  ? 1.98058 1.08755 1.36902 0.52319  -0.66295 -0.32562 143 LYS   B CB  
2803 C CG  . LYS   B 50  ? 1.92522 0.93819 1.25218 0.48808  -0.66973 -0.29541 143 LYS   B CG  
2804 C CD  . LYS   B 50  ? 2.15658 1.14927 1.47349 0.47907  -0.66675 -0.29472 143 LYS   B CD  
2805 C CE  . LYS   B 50  ? 1.99965 1.04612 1.36308 0.46005  -0.63044 -0.29127 143 LYS   B CE  
2806 N NZ  . LYS   B 50  ? 1.98965 1.01640 1.34229 0.45060  -0.62799 -0.29210 143 LYS   B NZ  
2807 N N   . MET   B 51  ? 1.74038 0.93936 1.19614 0.51267  -0.62894 -0.31451 144 MET   B N   
2808 C CA  . MET   B 51  ? 1.77318 0.95565 1.21924 0.49542  -0.62455 -0.29523 144 MET   B CA  
2809 C C   . MET   B 51  ? 1.56347 0.78574 1.04753 0.46992  -0.58926 -0.27833 144 MET   B C   
2810 O O   . MET   B 51  ? 1.55711 0.73925 1.01741 0.44116  -0.58244 -0.25150 144 MET   B O   
2811 C CB  . MET   B 51  ? 1.62680 0.85122 1.09425 0.52351  -0.63632 -0.31611 144 MET   B CB  
2812 C CG  . MET   B 51  ? 1.86720 1.05836 1.30118 0.55253  -0.67229 -0.33721 144 MET   B CG  
2813 S SD  . MET   B 51  ? 1.78066 1.02866 1.24579 0.58518  -0.68420 -0.36573 144 MET   B SD  
2814 C CE  . MET   B 51  ? 1.95885 1.15696 1.37831 0.61763  -0.72781 -0.38969 144 MET   B CE  
2815 N N   . ARG   B 52  ? 1.49102 0.79258 1.03280 0.47934  -0.56636 -0.29408 145 ARG   B N   
2816 C CA  . ARG   B 52  ? 1.51076 0.85047 1.08845 0.45679  -0.53359 -0.28016 145 ARG   B CA  
2817 C C   . ARG   B 52  ? 1.49000 0.77516 1.03387 0.41726  -0.52325 -0.25469 145 ARG   B C   
2818 O O   . ARG   B 52  ? 1.45095 0.74916 1.00100 0.37831  -0.49855 -0.22864 145 ARG   B O   
2819 C CB  . ARG   B 52  ? 1.42813 0.86734 1.07038 0.47185  -0.51041 -0.30349 145 ARG   B CB  
2820 C CG  . ARG   B 52  ? 1.39418 0.89965 1.07585 0.43215  -0.46794 -0.28444 145 ARG   B CG  
2821 C CD  . ARG   B 52  ? 1.21138 0.81234 0.95030 0.44448  -0.44556 -0.30691 145 ARG   B CD  
2822 N NE  . ARG   B 52  ? 1.22072 0.87561 0.99073 0.40700  -0.40753 -0.28839 145 ARG   B NE  
2823 C CZ  . ARG   B 52  ? 1.25275 0.90057 1.01617 0.38385  -0.39303 -0.27837 145 ARG   B CZ  
2824 N NH1 . ARG   B 52  ? 1.31785 0.90776 1.04518 0.39169  -0.41169 -0.28443 145 ARG   B NH1 
2825 N NH2 . ARG   B 52  ? 1.17092 0.86938 0.96367 0.35259  -0.36037 -0.26239 145 ARG   B NH2 
2826 N N   . ALA   B 53  ? 1.51240 0.74451 1.02211 0.42264  -0.54007 -0.26124 146 ALA   B N   
2827 C CA  . ALA   B 53  ? 1.52589 0.70544 1.00294 0.38445  -0.53201 -0.23925 146 ALA   B CA  
2828 C C   . ALA   B 53  ? 1.59656 0.69349 1.01828 0.35720  -0.54353 -0.21144 146 ALA   B C   
2829 O O   . ALA   B 53  ? 1.60459 0.69780 1.02137 0.31346  -0.52153 -0.18584 146 ALA   B O   
2830 C CB  . ALA   B 53  ? 1.52021 0.66844 0.97443 0.39560  -0.54782 -0.25242 146 ALA   B CB  
2831 N N   . ILE   B 54  ? 1.67281 0.73106 1.05860 0.37253  -0.57081 -0.21231 147 ILE   B N   
2832 C CA  . ILE   B 54  ? 1.66789 0.65315 0.99762 0.34443  -0.58054 -0.18598 147 ILE   B CA  
2833 C C   . ILE   B 54  ? 1.69470 0.70337 1.04431 0.32612  -0.56013 -0.16926 147 ILE   B C   
2834 O O   . ILE   B 54  ? 1.71495 0.68045 1.03359 0.28776  -0.55097 -0.14274 147 ILE   B O   
2835 C CB  . ILE   B 54  ? 1.87955 0.82172 1.16633 0.36769  -0.61519 -0.19487 147 ILE   B CB  
2836 C CG1 . ILE   B 54  ? 1.81250 0.72946 1.07839 0.38619  -0.63644 -0.21070 147 ILE   B CG1 
2837 C CG2 . ILE   B 54  ? 2.00521 0.87208 1.23034 0.33726  -0.62421 -0.16860 147 ILE   B CG2 
2838 C CD1 . ILE   B 54  ? 1.99646 0.87038 1.21979 0.41154  -0.67266 -0.22257 147 ILE   B CD1 
2839 N N   . LEU   B 55  ? 1.58552 0.66652 0.98797 0.35195  -0.55187 -0.18442 148 LEU   B N   
2840 C CA  . LEU   B 55  ? 1.51906 0.64743 0.94826 0.32961  -0.52739 -0.16755 148 LEU   B CA  
2841 C C   . LEU   B 55  ? 1.49773 0.67654 0.95905 0.28726  -0.48766 -0.14995 148 LEU   B C   
2842 O O   . LEU   B 55  ? 1.52057 0.68722 0.96874 0.25122  -0.47205 -0.12524 148 LEU   B O   
2843 C CB  . LEU   B 55  ? 1.61442 0.82147 1.09677 0.36335  -0.52565 -0.18895 148 LEU   B CB  
2844 C CG  . LEU   B 55  ? 1.65283 0.91409 1.16640 0.34305  -0.50101 -0.17436 148 LEU   B CG  
2845 C CD1 . LEU   B 55  ? 1.49055 0.67799 0.94876 0.32919  -0.51690 -0.15366 148 LEU   B CD1 
2846 C CD2 . LEU   B 55  ? 1.66232 1.00731 1.23285 0.37490  -0.49790 -0.19808 148 LEU   B CD2 
2847 N N   . LEU   B 56  ? 1.47221 0.70841 0.97508 0.29179  -0.47138 -0.16324 149 LEU   B N   
2848 C CA  . LEU   B 56  ? 1.35203 0.63616 0.88555 0.25475  -0.43610 -0.14819 149 LEU   B CA  
2849 C C   . LEU   B 56  ? 1.46030 0.67622 0.94766 0.21761  -0.43638 -0.12650 149 LEU   B C   
2850 O O   . LEU   B 56  ? 1.44469 0.67857 0.94102 0.18034  -0.41177 -0.10583 149 LEU   B O   
2851 C CB  . LEU   B 56  ? 1.36939 0.71934 0.94844 0.26901  -0.42261 -0.16769 149 LEU   B CB  
2852 C CG  . LEU   B 56  ? 1.27968 0.71425 0.91347 0.29710  -0.41325 -0.18803 149 LEU   B CG  
2853 C CD1 . LEU   B 56  ? 1.35685 0.84799 1.02672 0.30746  -0.39986 -0.20622 149 LEU   B CD1 
2854 C CD2 . LEU   B 56  ? 1.20465 0.69306 0.87138 0.27581  -0.38732 -0.17266 149 LEU   B CD2 
2855 N N   . ASP   B 57  ? 1.46691 0.60444 0.90455 0.22695  -0.46441 -0.13187 150 ASP   B N   
2856 C CA  . ASP   B 57  ? 1.54155 0.60941 0.93140 0.18991  -0.46650 -0.11199 150 ASP   B CA  
2857 C C   . ASP   B 57  ? 1.67136 0.69501 1.02451 0.16296  -0.46645 -0.08812 150 ASP   B C   
2858 O O   . ASP   B 57  ? 1.63745 0.64610 0.97649 0.12059  -0.44998 -0.06732 150 ASP   B O   
2859 C CB  . ASP   B 57  ? 1.75436 0.74076 1.09399 0.20779  -0.49984 -0.12382 150 ASP   B CB  
2860 C CG  . ASP   B 57  ? 1.96374 0.87868 1.25425 0.16740  -0.50193 -0.10471 150 ASP   B CG  
2861 O OD1 . ASP   B 57  ? 2.11606 1.06212 1.42898 0.14373  -0.48196 -0.10147 150 ASP   B OD1 
2862 O OD2 . ASP   B 57  ? 1.93686 0.77328 1.16834 0.15746  -0.52187 -0.09217 150 ASP   B OD2 
2863 N N   . TRP   B 58  ? 1.66357 0.66761 1.00083 0.18699  -0.48483 -0.09176 151 TRP   B N   
2864 C CA  . TRP   B 58  ? 1.67686 0.64297 0.97935 0.16291  -0.48404 -0.06983 151 TRP   B CA  
2865 C C   . TRP   B 58  ? 1.61493 0.65983 0.96606 0.13607  -0.44638 -0.05680 151 TRP   B C   
2866 O O   . TRP   B 58  ? 1.61857 0.64275 0.94775 0.09783  -0.43262 -0.03481 151 TRP   B O   
2867 C CB  . TRP   B 58  ? 1.87999 0.81027 1.15624 0.19871  -0.51439 -0.07894 151 TRP   B CB  
2868 C CG  . TRP   B 58  ? 1.92782 0.83393 1.17634 0.17856  -0.51157 -0.05883 151 TRP   B CG  
2869 C CD1 . TRP   B 58  ? 1.99058 0.82147 1.17701 0.14348  -0.51550 -0.03599 151 TRP   B CD1 
2870 C CD2 . TRP   B 58  ? 1.84511 0.80549 1.12625 0.19083  -0.50332 -0.06064 151 TRP   B CD2 
2871 N NE1 . TRP   B 58  ? 2.09012 0.92203 1.26654 0.13440  -0.51056 -0.02332 151 TRP   B NE1 
2872 C CE2 . TRP   B 58  ? 2.03076 0.94090 1.26494 0.16365  -0.50377 -0.03813 151 TRP   B CE2 
2873 C CE3 . TRP   B 58  ? 1.79605 0.84272 1.14056 0.22052  -0.49517 -0.07940 151 TRP   B CE3 
2874 C CZ2 . TRP   B 58  ? 1.96953 0.91194 1.21808 0.16699  -0.49738 -0.03420 151 TRP   B CZ2 
2875 C CZ3 . TRP   B 58  ? 1.74575 0.82427 1.10547 0.22261  -0.48903 -0.07529 151 TRP   B CZ3 
2876 C CH2 . TRP   B 58  ? 1.84552 0.87159 1.15750 0.19688  -0.49067 -0.05304 151 TRP   B CH2 
2877 N N   . LEU   B 59  ? 1.57578 0.71094 0.99201 0.15502  -0.42926 -0.07073 152 LEU   B N   
2878 C CA  . LEU   B 59  ? 1.38108 0.59011 0.84396 0.13128  -0.39449 -0.05960 152 LEU   B CA  
2879 C C   . LEU   B 59  ? 1.34418 0.56750 0.81703 0.09291  -0.37013 -0.04643 152 LEU   B C   
2880 O O   . LEU   B 59  ? 1.34165 0.59268 0.82829 0.06258  -0.34600 -0.03034 152 LEU   B O   
2881 C CB  . LEU   B 59  ? 1.27385 0.57151 0.80056 0.15910  -0.38288 -0.07809 152 LEU   B CB  
2882 C CG  . LEU   B 59  ? 1.40501 0.70795 0.93474 0.19578  -0.40267 -0.09272 152 LEU   B CG  
2883 C CD1 . LEU   B 59  ? 1.34804 0.74304 0.94308 0.21868  -0.38838 -0.11220 152 LEU   B CD1 
2884 C CD2 . LEU   B 59  ? 1.28163 0.56563 0.79076 0.18135  -0.40168 -0.07620 152 LEU   B CD2 
2885 N N   . MET   B 60  ? 1.29141 0.49760 0.75820 0.09456  -0.37669 -0.05427 153 MET   B N   
2886 C CA  . MET   B 60  ? 1.37234 0.58591 0.84443 0.05810  -0.35736 -0.04264 153 MET   B CA  
2887 C C   . MET   B 60  ? 1.37206 0.52355 0.79495 0.01992  -0.35768 -0.02080 153 MET   B C   
2888 O O   . MET   B 60  ? 1.46459 0.64562 0.90362 -0.01460 -0.33263 -0.00661 153 MET   B O   
2889 C CB  . MET   B 60  ? 1.41548 0.61104 0.88181 0.06843  -0.36924 -0.05606 153 MET   B CB  
2890 C CG  . MET   B 60  ? 1.49614 0.75924 1.01235 0.09983  -0.36382 -0.07734 153 MET   B CG  
2891 S SD  . MET   B 60  ? 1.50585 0.75108 1.01479 0.10256  -0.37217 -0.08992 153 MET   B SD  
2892 C CE  . MET   B 60  ? 1.44853 0.76784 1.00805 0.14572  -0.36927 -0.11717 153 MET   B CE  
2893 N N   . GLU   B 61  ? 1.48406 0.54830 0.84503 0.02549  -0.38635 -0.01854 154 GLU   B N   
2894 C CA  . GLU   B 61  ? 1.55548 0.55402 0.86225 -0.01256 -0.38764 0.00242  154 GLU   B CA  
2895 C C   . GLU   B 61  ? 1.58855 0.61490 0.90378 -0.02904 -0.36926 0.01652  154 GLU   B C   
2896 O O   . GLU   B 61  ? 1.55218 0.57377 0.85548 -0.06966 -0.35111 0.03363  154 GLU   B O   
2897 C CB  . GLU   B 61  ? 1.81424 0.70869 1.04871 0.00044  -0.42499 0.00136  154 GLU   B CB  
2898 C CG  . GLU   B 61  ? 1.96617 0.78073 1.13544 -0.04221 -0.42865 0.02246  154 GLU   B CG  
2899 C CD  . GLU   B 61  ? 2.10766 0.84524 1.21454 -0.02859 -0.46152 0.01958  154 GLU   B CD  
2900 O OE1 . GLU   B 61  ? 2.08296 0.81438 1.19227 0.01588  -0.48549 0.00113  154 GLU   B OE1 
2901 O OE2 . GLU   B 61  ? 2.16348 0.85841 1.22292 -0.06217 -0.46145 0.03433  154 GLU   B OE2 
2902 N N   . VAL   B 62  ? 1.57735 0.63557 0.91436 0.00182  -0.37332 0.00828  155 VAL   B N   
2903 C CA  . VAL   B 62  ? 1.38564 0.47348 0.73306 -0.01107 -0.35636 0.01982  155 VAL   B CA  
2904 C C   . VAL   B 62  ? 1.47230 0.64008 0.87464 -0.03685 -0.31948 0.02579  155 VAL   B C   
2905 O O   . VAL   B 62  ? 1.39256 0.56701 0.78937 -0.06762 -0.30114 0.04099  155 VAL   B O   
2906 C CB  . VAL   B 62  ? 1.50096 0.61368 0.86698 0.02919  -0.36882 0.00684  155 VAL   B CB  
2907 C CG1 . VAL   B 62  ? 1.45139 0.60375 0.83521 0.01631  -0.34916 0.01717  155 VAL   B CG1 
2908 C CG2 . VAL   B 62  ? 1.62625 0.65446 0.93284 0.05405  -0.40746 0.00190  155 VAL   B CG2 
2909 N N   . CYS   B 63  ? 1.48021 0.70857 0.93447 -0.02431 -0.30867 0.01336  156 CYS   B N   
2910 C CA  . CYS   B 63  ? 1.35247 0.65444 0.85802 -0.04563 -0.27640 0.01799  156 CYS   B CA  
2911 C C   . CYS   B 63  ? 1.28995 0.57045 0.77666 -0.08783 -0.26445 0.03173  156 CYS   B C   
2912 O O   . CYS   B 63  ? 1.31583 0.63633 0.82495 -0.11394 -0.23972 0.04145  156 CYS   B O   
2913 C CB  . CYS   B 63  ? 1.25111 0.61371 0.80832 -0.02313 -0.27026 0.00191  156 CYS   B CB  
2914 S SG  . CYS   B 63  ? 1.26822 0.68154 0.86318 0.02005  -0.27477 -0.01504 156 CYS   B SG  
2915 N N   . GLU   B 64  ? 1.40426 0.62285 0.85047 -0.09513 -0.28199 0.03152  157 GLU   B N   
2916 C CA  . GLU   B 64  ? 1.54461 0.74410 0.97373 -0.13706 -0.27118 0.04308  157 GLU   B CA  
2917 C C   . GLU   B 64  ? 1.47988 0.63961 0.86682 -0.16888 -0.26616 0.06054  157 GLU   B C   
2918 O O   . GLU   B 64  ? 1.58839 0.76891 0.98307 -0.20585 -0.24458 0.07044  157 GLU   B O   
2919 C CB  . GLU   B 64  ? 1.52993 0.66971 0.92403 -0.13692 -0.29274 0.03767  157 GLU   B CB  
2920 C CG  . GLU   B 64  ? 1.61594 0.74427 0.99967 -0.18014 -0.28139 0.04672  157 GLU   B CG  
2921 C CD  . GLU   B 64  ? 1.79212 0.86006 1.14091 -0.17972 -0.30377 0.04046  157 GLU   B CD  
2922 O OE1 . GLU   B 64  ? 1.83395 0.85698 1.15696 -0.14672 -0.33022 0.03050  157 GLU   B OE1 
2923 O OE2 . GLU   B 64  ? 1.85881 0.92505 1.20660 -0.21186 -0.29554 0.04433  157 GLU   B OE2 
2924 N N   . VAL   B 65  ? 1.63826 0.74186 0.97988 -0.15494 -0.28605 0.06368  158 VAL   B N   
2925 C CA  . VAL   B 65  ? 1.62932 0.69041 0.92447 -0.18471 -0.28228 0.08057  158 VAL   B CA  
2926 C C   . VAL   B 65  ? 1.58178 0.71512 0.91946 -0.19796 -0.25203 0.08602  158 VAL   B C   
2927 O O   . VAL   B 65  ? 1.63179 0.77006 0.96093 -0.23666 -0.23242 0.09785  158 VAL   B O   
2928 C CB  . VAL   B 65  ? 1.76186 0.74866 1.00009 -0.16181 -0.31255 0.08155  158 VAL   B CB  
2929 C CG1 . VAL   B 65  ? 1.87816 0.82725 1.06973 -0.19124 -0.30672 0.09916  158 VAL   B CG1 
2930 C CG2 . VAL   B 65  ? 1.85284 0.75768 1.04060 -0.15302 -0.34345 0.07737  158 VAL   B CG2 
2931 N N   . TYR   B 66  ? 1.54682 0.73786 0.93089 -0.16650 -0.24772 0.07646  159 TYR   B N   
2932 C CA  . TYR   B 66  ? 1.46290 0.72317 0.88988 -0.17463 -0.22078 0.07966  159 TYR   B CA  
2933 C C   . TYR   B 66  ? 1.36850 0.70586 0.85828 -0.18176 -0.19692 0.07431  159 TYR   B C   
2934 O O   . TYR   B 66  ? 1.28097 0.68044 0.81251 -0.18333 -0.17576 0.07448  159 TYR   B O   
2935 C CB  . TYR   B 66  ? 1.41655 0.69828 0.85989 -0.13951 -0.22844 0.07240  159 TYR   B CB  
2936 C CG  . TYR   B 66  ? 1.44850 0.66124 0.83185 -0.13472 -0.24937 0.07902  159 TYR   B CG  
2937 C CD1 . TYR   B 66  ? 1.56190 0.70819 0.90290 -0.11131 -0.28198 0.07357  159 TYR   B CD1 
2938 C CD2 . TYR   B 66  ? 1.46656 0.67874 0.83345 -0.15273 -0.23764 0.09012  159 TYR   B CD2 
2939 C CE1 . TYR   B 66  ? 1.63997 0.71921 0.92289 -0.10553 -0.30365 0.07967  159 TYR   B CE1 
2940 C CE2 . TYR   B 66  ? 1.66941 0.81580 0.97765 -0.14853 -0.25785 0.09665  159 TYR   B CE2 
2941 C CZ  . TYR   B 66  ? 1.59690 0.67592 0.86276 -0.12473 -0.29149 0.09176  159 TYR   B CZ  
2942 O OH  . TYR   B 66  ? 1.82191 0.83176 1.02645 -0.11904 -0.31407 0.09827  159 TYR   B OH  
2943 N N   . LYS   B 67  ? 1.49634 0.82814 0.99135 -0.18544 -0.20132 0.06928  160 LYS   B N   
2944 C CA  . LYS   B 67  ? 1.29125 0.68891 0.83973 -0.19395 -0.18140 0.06460  160 LYS   B CA  
2945 C C   . LYS   B 67  ? 1.12092 0.58861 0.72600 -0.16465 -0.17224 0.05463  160 LYS   B C   
2946 O O   . LYS   B 67  ? 1.07564 0.60500 0.72444 -0.17355 -0.15010 0.05511  160 LYS   B O   
2947 C CB  . LYS   B 67  ? 1.30867 0.72903 0.86342 -0.23435 -0.15753 0.07490  160 LYS   B CB  
2948 C CG  . LYS   B 67  ? 1.46412 0.81828 0.96287 -0.26882 -0.16387 0.08496  160 LYS   B CG  
2949 C CD  . LYS   B 67  ? 1.61491 1.00160 1.12578 -0.30949 -0.13811 0.09244  160 LYS   B CD  
2950 C CE  . LYS   B 67  ? 1.70696 1.02829 1.16079 -0.34743 -0.14332 0.10219  160 LYS   B CE  
2951 N NZ  . LYS   B 67  ? 1.66879 1.02782 1.13732 -0.38874 -0.11699 0.10723  160 LYS   B NZ  
2952 N N   . LEU   B 68  ? 1.20508 0.66271 0.80850 -0.12965 -0.18990 0.04483  161 LEU   B N   
2953 C CA  . LEU   B 68  ? 1.05191 0.57273 0.70551 -0.10276 -0.18231 0.03448  161 LEU   B CA  
2954 C C   . LEU   B 68  ? 0.95471 0.51040 0.64153 -0.09561 -0.17851 0.02493  161 LEU   B C   
2955 O O   . LEU   B 68  ? 1.01548 0.53674 0.68168 -0.09952 -0.19022 0.02220  161 LEU   B O   
2956 C CB  . LEU   B 68  ? 1.10874 0.61073 0.75019 -0.06878 -0.20221 0.02560  161 LEU   B CB  
2957 C CG  . LEU   B 68  ? 1.11238 0.57749 0.71853 -0.07121 -0.20960 0.03382  161 LEU   B CG  
2958 C CD1 . LEU   B 68  ? 1.13443 0.58604 0.73352 -0.03420 -0.23163 0.02208  161 LEU   B CD1 
2959 C CD2 . LEU   B 68  ? 0.99812 0.50987 0.63034 -0.08771 -0.18523 0.04201  161 LEU   B CD2 
2960 N N   . HIS   B 69  ? 0.90890 0.53088 0.64482 -0.08572 -0.16254 0.01999  162 HIS   B N   
2961 C CA  . HIS   B 69  ? 0.98269 0.64098 0.74978 -0.08030 -0.15711 0.01197  162 HIS   B CA  
2962 C C   . HIS   B 69  ? 0.91912 0.56346 0.68033 -0.05014 -0.17558 -0.00252 162 HIS   B C   
2963 O O   . HIS   B 69  ? 0.93092 0.55729 0.67892 -0.02776 -0.18936 -0.00872 162 HIS   B O   
2964 C CB  . HIS   B 69  ? 0.89955 0.62737 0.71562 -0.07849 -0.13586 0.01156  162 HIS   B CB  
2965 C CG  . HIS   B 69  ? 1.01396 0.76382 0.84307 -0.10682 -0.11713 0.02229  162 HIS   B CG  
2966 N ND1 . HIS   B 69  ? 1.12153 0.86212 0.93815 -0.12119 -0.11038 0.03158  162 HIS   B ND1 
2967 C CD2 . HIS   B 69  ? 1.09559 0.87772 0.94931 -0.12243 -0.10435 0.02377  162 HIS   B CD2 
2968 C CE1 . HIS   B 69  ? 1.07269 0.84124 0.90730 -0.14427 -0.09324 0.03747  162 HIS   B CE1 
2969 N NE2 . HIS   B 69  ? 1.12482 0.91914 0.98294 -0.14490 -0.08998 0.03272  162 HIS   B NE2 
2970 N N   . ARG   B 70  ? 0.99111 0.64541 0.76265 -0.04914 -0.17623 -0.00918 163 ARG   B N   
2971 C CA  . ARG   B 70  ? 0.99659 0.64467 0.76595 -0.02060 -0.19140 -0.02495 163 ARG   B CA  
2972 C C   . ARG   B 70  ? 0.83891 0.53762 0.64158 0.00482  -0.18517 -0.03485 163 ARG   B C   
2973 O O   . ARG   B 70  ? 0.89898 0.58849 0.69514 0.03200  -0.19985 -0.04814 163 ARG   B O   
2974 C CB  . ARG   B 70  ? 0.88978 0.54608 0.66685 -0.02644 -0.19018 -0.02988 163 ARG   B CB  
2975 C CG  . ARG   B 70  ? 0.98754 0.59765 0.73448 -0.05380 -0.19599 -0.02154 163 ARG   B CG  
2976 C CD  . ARG   B 70  ? 1.07375 0.69492 0.83025 -0.05762 -0.19610 -0.02812 163 ARG   B CD  
2977 N NE  . ARG   B 70  ? 1.00737 0.58554 0.73603 -0.08533 -0.20218 -0.02133 163 ARG   B NE  
2978 C CZ  . ARG   B 70  ? 1.09439 0.60852 0.78086 -0.08417 -0.22331 -0.02491 163 ARG   B CZ  
2979 N NH1 . ARG   B 70  ? 1.08670 0.57168 0.75402 -0.05410 -0.24174 -0.03623 163 ARG   B NH1 
2980 N NH2 . ARG   B 70  ? 1.23181 0.71026 0.89460 -0.11399 -0.22655 -0.01785 163 ARG   B NH2 
2981 N N   . GLU   B 71  ? 0.82026 0.57307 0.65880 -0.00384 -0.16383 -0.02946 164 GLU   B N   
2982 C CA  . GLU   B 71  ? 0.80691 0.60772 0.67619 0.01558  -0.15621 -0.03748 164 GLU   B CA  
2983 C C   . GLU   B 71  ? 0.82875 0.61203 0.68507 0.03032  -0.16711 -0.03999 164 GLU   B C   
2984 O O   . GLU   B 71  ? 0.82670 0.63207 0.69670 0.05467  -0.17199 -0.05332 164 GLU   B O   
2985 C CB  . GLU   B 71  ? 0.84706 0.69813 0.75010 0.00025  -0.13296 -0.02876 164 GLU   B CB  
2986 C CG  . GLU   B 71  ? 0.88140 0.77890 0.81367 0.01459  -0.12352 -0.03435 164 GLU   B CG  
2987 C CD  . GLU   B 71  ? 0.83589 0.76546 0.78632 0.03280  -0.12262 -0.04862 164 GLU   B CD  
2988 O OE1 . GLU   B 71  ? 0.78267 0.70338 0.72627 0.03309  -0.12684 -0.05301 164 GLU   B OE1 
2989 O OE2 . GLU   B 71  ? 0.82150 0.78606 0.79249 0.04568  -0.11723 -0.05593 164 GLU   B OE2 
2990 N N   . THR   B 72  ? 0.89458 0.63885 0.72372 0.01550  -0.17137 -0.02806 165 THR   B N   
2991 C CA  . THR   B 72  ? 0.85246 0.57529 0.66478 0.02889  -0.18359 -0.02952 165 THR   B CA  
2992 C C   . THR   B 72  ? 0.86536 0.54997 0.65273 0.05575  -0.20952 -0.04353 165 THR   B C   
2993 O O   . THR   B 72  ? 0.92857 0.62400 0.72257 0.08017  -0.21910 -0.05464 165 THR   B O   
2994 C CB  . THR   B 72  ? 0.93788 0.62166 0.71986 0.00497  -0.18280 -0.01312 165 THR   B CB  
2995 O OG1 . THR   B 72  ? 0.95161 0.67564 0.76002 -0.01716 -0.15872 -0.00272 165 THR   B OG1 
2996 C CG2 . THR   B 72  ? 0.95548 0.61493 0.71697 0.01894  -0.19656 -0.01411 165 THR   B CG2 
2997 N N   . PHE   B 73  ? 0.91553 0.55586 0.67470 0.05238  -0.22206 -0.04450 166 PHE   B N   
2998 C CA  . PHE   B 73  ? 1.02371 0.62376 0.75710 0.07960  -0.24846 -0.05909 166 PHE   B CA  
2999 C C   . PHE   B 73  ? 0.89248 0.54336 0.66093 0.10848  -0.24771 -0.07963 166 PHE   B C   
3000 O O   . PHE   B 73  ? 0.94973 0.59998 0.71752 0.13732  -0.26330 -0.09438 166 PHE   B O   
3001 C CB  . PHE   B 73  ? 0.98657 0.52876 0.68277 0.06810  -0.26116 -0.05617 166 PHE   B CB  
3002 C CG  . PHE   B 73  ? 1.05471 0.56493 0.73181 0.09835  -0.28618 -0.07451 166 PHE   B CG  
3003 C CD1 . PHE   B 73  ? 1.06144 0.52184 0.70474 0.11970  -0.31197 -0.08037 166 PHE   B CD1 
3004 C CD2 . PHE   B 73  ? 1.11674 0.64702 0.80915 0.10719  -0.28486 -0.08706 166 PHE   B CD2 
3005 C CE1 . PHE   B 73  ? 1.16829 0.59976 0.79485 0.15044  -0.33642 -0.09926 166 PHE   B CE1 
3006 C CE2 . PHE   B 73  ? 1.11912 0.62160 0.79443 0.13667  -0.30782 -0.10591 166 PHE   B CE2 
3007 C CZ  . PHE   B 73  ? 1.25707 0.71061 0.90039 0.15903  -0.33382 -0.11253 166 PHE   B CZ  
3008 N N   . TYR   B 74  ? 0.83475 0.53078 0.63336 0.10107  -0.22998 -0.08166 167 TYR   B N   
3009 C CA  . TYR   B 74  ? 0.86272 0.60632 0.69100 0.12537  -0.22755 -0.10111 167 TYR   B CA  
3010 C C   . TYR   B 74  ? 0.86456 0.66328 0.72724 0.13651  -0.21685 -0.10672 167 TYR   B C   
3011 O O   . TYR   B 74  ? 0.83628 0.66734 0.71770 0.16155  -0.22057 -0.12596 167 TYR   B O   
3012 C CB  . TYR   B 74  ? 0.77878 0.55273 0.62558 0.11250  -0.21152 -0.10027 167 TYR   B CB  
3013 C CG  . TYR   B 74  ? 0.86528 0.59487 0.68369 0.11394  -0.22644 -0.10547 167 TYR   B CG  
3014 C CD1 . TYR   B 74  ? 0.97783 0.70813 0.79413 0.14139  -0.23929 -0.12659 167 TYR   B CD1 
3015 C CD2 . TYR   B 74  ? 0.84562 0.53362 0.63947 0.08749  -0.22771 -0.09053 167 TYR   B CD2 
3016 C CE1 . TYR   B 74  ? 0.91729 0.60449 0.70600 0.14328  -0.25393 -0.13221 167 TYR   B CE1 
3017 C CE2 . TYR   B 74  ? 0.94672 0.59244 0.71368 0.08727  -0.24204 -0.09559 167 TYR   B CE2 
3018 C CZ  . TYR   B 74  ? 0.93402 0.57759 0.69756 0.11567  -0.25563 -0.11621 167 TYR   B CZ  
3019 O OH  . TYR   B 74  ? 0.99778 0.59696 0.73307 0.11601  -0.27079 -0.12206 167 TYR   B OH  
3020 N N   . LEU   B 75  ? 0.76244 0.57397 0.63415 0.11792  -0.20343 -0.09146 168 LEU   B N   
3021 C CA  . LEU   B 75  ? 0.71919 0.57269 0.61725 0.12826  -0.19731 -0.09661 168 LEU   B CA  
3022 C C   . LEU   B 75  ? 0.75318 0.57834 0.63270 0.15418  -0.22185 -0.10854 168 LEU   B C   
3023 O O   . LEU   B 75  ? 0.86896 0.73183 0.77189 0.17718  -0.22509 -0.12607 168 LEU   B O   
3024 C CB  . LEU   B 75  ? 0.68479 0.54898 0.59049 0.10333  -0.18050 -0.07788 168 LEU   B CB  
3025 C CG  . LEU   B 75  ? 0.73716 0.64790 0.67348 0.08369  -0.15474 -0.06961 168 LEU   B CG  
3026 C CD1 . LEU   B 75  ? 0.80642 0.71841 0.74461 0.06174  -0.14217 -0.05259 168 LEU   B CD1 
3027 C CD2 . LEU   B 75  ? 0.78201 0.75228 0.75450 0.09706  -0.14425 -0.08315 168 LEU   B CD2 
3028 N N   . ALA   B 76  ? 0.90778 0.66595 0.74404 0.15043  -0.23998 -0.09973 169 ALA   B N   
3029 C CA  . ALA   B 76  ? 1.00613 0.72786 0.81808 0.17609  -0.26700 -0.11025 169 ALA   B CA  
3030 C C   . ALA   B 76  ? 0.92055 0.64169 0.73324 0.20775  -0.28467 -0.13389 169 ALA   B C   
3031 O O   . ALA   B 76  ? 0.95158 0.68122 0.76978 0.23711  -0.30113 -0.15147 169 ALA   B O   
3032 C CB  . ALA   B 76  ? 1.01974 0.66247 0.77817 0.16223  -0.28267 -0.09417 169 ALA   B CB  
3033 N N   . GLN   B 77  ? 0.88371 0.59638 0.69153 0.20311  -0.28211 -0.13603 170 GLN   B N   
3034 C CA  . GLN   B 77  ? 0.92045 0.63592 0.73000 0.23300  -0.29702 -0.15988 170 GLN   B CA  
3035 C C   . GLN   B 77  ? 0.96661 0.76312 0.82593 0.25054  -0.28359 -0.17906 170 GLN   B C   
3036 O O   . GLN   B 77  ? 0.97321 0.78248 0.84008 0.28282  -0.29939 -0.20228 170 GLN   B O   
3037 C CB  . GLN   B 77  ? 0.96019 0.65226 0.75469 0.22091  -0.29476 -0.15706 170 GLN   B CB  
3038 C CG  . GLN   B 77  ? 0.99495 0.69764 0.79464 0.24968  -0.30580 -0.18238 170 GLN   B CG  
3039 C CD  . GLN   B 77  ? 0.98023 0.75892 0.82388 0.24753  -0.28059 -0.19102 170 GLN   B CD  
3040 O OE1 . GLN   B 77  ? 0.95063 0.75751 0.81135 0.21994  -0.25683 -0.17495 170 GLN   B OE1 
3041 N NE2 . GLN   B 77  ? 1.14207 0.95375 1.00278 0.27693  -0.28608 -0.21713 170 GLN   B NE2 
3042 N N   . ASP   B 78  ? 0.87476 0.72684 0.76787 0.22921  -0.25465 -0.17026 171 ASP   B N   
3043 C CA  . ASP   B 78  ? 0.90756 0.83588 0.84540 0.24055  -0.23944 -0.18669 171 ASP   B CA  
3044 C C   . ASP   B 78  ? 0.87109 0.82459 0.82616 0.25437  -0.24466 -0.19431 171 ASP   B C   
3045 O O   . ASP   B 78  ? 0.79473 0.79507 0.77685 0.27738  -0.24657 -0.21724 171 ASP   B O   
3046 C CB  . ASP   B 78  ? 0.78329 0.75562 0.74648 0.21256  -0.20899 -0.17322 171 ASP   B CB  
3047 C CG  . ASP   B 78  ? 0.83920 0.88652 0.84363 0.22016  -0.19190 -0.18898 171 ASP   B CG  
3048 O OD1 . ASP   B 78  ? 0.86949 0.93697 0.88055 0.23613  -0.19328 -0.20768 171 ASP   B OD1 
3049 O OD2 . ASP   B 78  ? 0.84673 0.93227 0.87552 0.20917  -0.17681 -0.18306 171 ASP   B OD2 
3050 N N   . PHE   B 79  ? 0.76320 0.68869 0.70355 0.24017  -0.24672 -0.17639 172 PHE   B N   
3051 C CA  . PHE   B 79  ? 0.85550 0.79842 0.80776 0.25388  -0.25493 -0.18351 172 PHE   B CA  
3052 C C   . PHE   B 79  ? 0.83571 0.75096 0.77108 0.29015  -0.28666 -0.20474 172 PHE   B C   
3053 O O   . PHE   B 79  ? 0.91360 0.87033 0.87506 0.31281  -0.29305 -0.22459 172 PHE   B O   
3054 C CB  . PHE   B 79  ? 0.79529 0.70470 0.72748 0.23179  -0.25299 -0.15993 172 PHE   B CB  
3055 C CG  . PHE   B 79  ? 0.80770 0.74900 0.76022 0.19962  -0.22319 -0.14152 172 PHE   B CG  
3056 C CD1 . PHE   B 79  ? 0.72806 0.73018 0.71795 0.19363  -0.20086 -0.14714 172 PHE   B CD1 
3057 C CD2 . PHE   B 79  ? 0.83803 0.74722 0.77029 0.17570  -0.21806 -0.11918 172 PHE   B CD2 
3058 C CE1 . PHE   B 79  ? 0.66486 0.69133 0.67051 0.16599  -0.17609 -0.13050 172 PHE   B CE1 
3059 C CE2 . PHE   B 79  ? 0.73096 0.66922 0.68234 0.14884  -0.19231 -0.10413 172 PHE   B CE2 
3060 C CZ  . PHE   B 79  ? 0.67928 0.67444 0.66697 0.14483  -0.17237 -0.10966 172 PHE   B CZ  
3061 N N   . PHE   B 80  ? 0.89849 0.74341 0.79007 0.29620  -0.30768 -0.20174 173 PHE   B N   
3062 C CA  . PHE   B 80  ? 0.99934 0.80738 0.86847 0.33210  -0.34124 -0.22137 173 PHE   B CA  
3063 C C   . PHE   B 80  ? 1.07733 0.93722 0.97830 0.36141  -0.34311 -0.25213 173 PHE   B C   
3064 O O   . PHE   B 80  ? 1.05858 0.94069 0.97420 0.39306  -0.36000 -0.27538 173 PHE   B O   
3065 C CB  . PHE   B 80  ? 1.07306 0.78962 0.88457 0.32779  -0.36182 -0.20954 173 PHE   B CB  
3066 C CG  . PHE   B 80  ? 1.11415 0.78453 0.89750 0.36563  -0.39805 -0.23019 173 PHE   B CG  
3067 C CD1 . PHE   B 80  ? 1.22800 0.85906 0.98623 0.38392  -0.42470 -0.23235 173 PHE   B CD1 
3068 C CD2 . PHE   B 80  ? 1.18362 0.84721 0.96330 0.38393  -0.40688 -0.24794 173 PHE   B CD2 
3069 C CE1 . PHE   B 80  ? 1.33115 0.91612 1.06144 0.42099  -0.46060 -0.25198 173 PHE   B CE1 
3070 C CE2 . PHE   B 80  ? 1.17273 0.79157 0.92557 0.42090  -0.44179 -0.26833 173 PHE   B CE2 
3071 C CZ  . PHE   B 80  ? 1.24912 0.82786 0.97719 0.44001  -0.46929 -0.27036 173 PHE   B CZ  
3072 N N   . ASP   B 81  ? 0.99308 0.87464 0.90521 0.35155  -0.32599 -0.25377 174 ASP   B N   
3073 C CA  . ASP   B 81  ? 0.99929 0.92689 0.93690 0.37823  -0.32702 -0.28341 174 ASP   B CA  
3074 C C   . ASP   B 81  ? 1.03860 1.05696 1.02997 0.38357  -0.30861 -0.29913 174 ASP   B C   
3075 O O   . ASP   B 81  ? 1.12062 1.17682 1.13373 0.41490  -0.31889 -0.32875 174 ASP   B O   
3076 C CB  . ASP   B 81  ? 1.03908 0.96567 0.97204 0.36372  -0.31244 -0.27970 174 ASP   B CB  
3077 C CG  . ASP   B 81  ? 1.23856 1.07840 1.11987 0.36324  -0.33389 -0.27101 174 ASP   B CG  
3078 O OD1 . ASP   B 81  ? 1.32408 1.10881 1.17426 0.38587  -0.36447 -0.27802 174 ASP   B OD1 
3079 O OD2 . ASP   B 81  ? 1.16232 0.98777 1.03297 0.33992  -0.32111 -0.25744 174 ASP   B OD2 
3080 N N   . ARG   B 82  ? 0.84648 0.90135 0.85994 0.35317  -0.28162 -0.28082 175 ARG   B N   
3081 C CA  . ARG   B 82  ? 0.80828 0.94707 0.87064 0.35407  -0.26306 -0.29451 175 ARG   B CA  
3082 C C   . ARG   B 82  ? 1.01817 1.16733 1.09126 0.37323  -0.28021 -0.30545 175 ARG   B C   
3083 O O   . ARG   B 82  ? 0.93788 1.15302 1.04952 0.38938  -0.27687 -0.32948 175 ARG   B O   
3084 C CB  . ARG   B 82  ? 0.81838 0.98792 0.89785 0.31602  -0.23051 -0.27173 175 ARG   B CB  
3085 C CG  . ARG   B 82  ? 0.73579 0.92050 0.81779 0.30060  -0.21042 -0.26803 175 ARG   B CG  
3086 C CD  . ARG   B 82  ? 0.72882 0.95534 0.83351 0.26817  -0.17917 -0.25112 175 ARG   B CD  
3087 N NE  . ARG   B 82  ? 0.83138 1.01646 0.91694 0.24255  -0.17518 -0.22171 175 ARG   B NE  
3088 C CZ  . ARG   B 82  ? 0.66073 0.85831 0.75791 0.22895  -0.16755 -0.21013 175 ARG   B CZ  
3089 N NH1 . ARG   B 82  ? 0.75922 1.00861 0.88731 0.23666  -0.16326 -0.22416 175 ARG   B NH1 
3090 N NH2 . ARG   B 82  ? 0.67136 0.83041 0.74937 0.20655  -0.16381 -0.18492 175 ARG   B NH2 
3091 N N   . TYR   B 83  ? 0.90699 0.99332 0.94614 0.37107  -0.29857 -0.28893 176 TYR   B N   
3092 C CA  . TYR   B 83  ? 0.90960 0.99912 0.95375 0.39125  -0.31853 -0.29943 176 TYR   B CA  
3093 C C   . TYR   B 83  ? 1.00446 1.09070 1.04730 0.43527  -0.34860 -0.33111 176 TYR   B C   
3094 O O   . TYR   B 83  ? 1.06142 1.19377 1.13389 0.45782  -0.35786 -0.35350 176 TYR   B O   
3095 C CB  . TYR   B 83  ? 0.92464 0.94164 0.92595 0.37754  -0.33141 -0.27338 176 TYR   B CB  
3096 C CG  . TYR   B 83  ? 1.00430 1.01109 1.00084 0.40011  -0.35688 -0.28303 176 TYR   B CG  
3097 C CD1 . TYR   B 83  ? 1.00309 1.06402 1.03386 0.39341  -0.34572 -0.28489 176 TYR   B CD1 
3098 C CD2 . TYR   B 83  ? 1.17084 1.11079 1.12628 0.42806  -0.39354 -0.29028 176 TYR   B CD2 
3099 C CE1 . TYR   B 83  ? 0.98046 1.03281 1.00681 0.41443  -0.37027 -0.29440 176 TYR   B CE1 
3100 C CE2 . TYR   B 83  ? 1.05176 0.97993 1.00031 0.45006  -0.41904 -0.29924 176 TYR   B CE2 
3101 C CZ  . TYR   B 83  ? 1.12692 1.11310 1.11203 0.44331  -0.40721 -0.30153 176 TYR   B CZ  
3102 O OH  . TYR   B 83  ? 1.16003 1.13353 1.13578 0.46054  -0.42959 -0.31033 176 TYR   B OH  
3103 N N   . MET   B 84  ? 1.12073 1.15338 1.13002 0.44862  -0.36499 -0.33465 177 MET   B N   
3104 C CA  . MET   B 84  ? 1.05998 1.08471 1.06498 0.49205  -0.39491 -0.36581 177 MET   B CA  
3105 C C   . MET   B 84  ? 1.12418 1.23767 1.17541 0.49882  -0.37630 -0.39444 177 MET   B C   
3106 O O   . MET   B 84  ? 1.05310 1.18703 1.10979 0.51800  -0.38929 -0.41908 177 MET   B O   
3107 C CB  . MET   B 84  ? 1.09920 1.04223 1.05411 0.50003  -0.41467 -0.36133 177 MET   B CB  
3108 C CG  . MET   B 84  ? 1.13054 0.97585 1.02704 0.49115  -0.43692 -0.33628 177 MET   B CG  
3109 S SD  . MET   B 84  ? 1.32898 1.15457 1.20958 0.51013  -0.46452 -0.34594 177 MET   B SD  
3110 C CE  . MET   B 84  ? 1.43134 1.12811 1.23106 0.50201  -0.49295 -0.31913 177 MET   B CE  
3111 N N   . ALA   B 85  ? 1.06649 1.23278 1.14921 0.48222  -0.34622 -0.39162 178 ALA   B N   
3112 C CA  . ALA   B 85  ? 0.91451 1.16591 1.03826 0.48222  -0.32483 -0.41562 178 ALA   B CA  
3113 C C   . ALA   B 85  ? 1.10841 1.42471 1.26849 0.47621  -0.31451 -0.42551 178 ALA   B C   
3114 O O   . ALA   B 85  ? 1.02552 1.40710 1.21463 0.47850  -0.30254 -0.44848 178 ALA   B O   
3115 C CB  . ALA   B 85  ? 0.92557 1.21154 1.06757 0.45977  -0.29320 -0.40596 178 ALA   B CB  
3116 N N   . THR   B 86  ? 0.94694 1.24597 1.10460 0.46752  -0.31909 -0.40887 179 THR   B N   
3117 C CA  . THR   B 86  ? 0.90924 1.26220 1.09779 0.46151  -0.31143 -0.41749 179 THR   B CA  
3118 C C   . THR   B 86  ? 0.99344 1.31258 1.16182 0.48472  -0.34256 -0.42980 179 THR   B C   
3119 O O   . THR   B 86  ? 1.02916 1.39055 1.22155 0.48356  -0.33983 -0.44064 179 THR   B O   
3120 C CB  . THR   B 86  ? 0.94919 1.31433 1.15239 0.43396  -0.29321 -0.39178 179 THR   B CB  
3121 O OG1 . THR   B 86  ? 0.88300 1.17210 1.04864 0.43650  -0.31491 -0.36938 179 THR   B OG1 
3122 C CG2 . THR   B 86  ? 0.88731 1.28414 1.10864 0.41063  -0.26313 -0.37947 179 THR   B CG2 
3123 N N   . GLN   B 87  ? 0.95997 1.20204 1.08290 0.50459  -0.37218 -0.42839 180 GLN   B N   
3124 C CA  . GLN   B 87  ? 1.08093 1.27949 1.17642 0.52636  -0.40400 -0.43820 180 GLN   B CA  
3125 C C   . GLN   B 87  ? 1.08776 1.27910 1.17047 0.55424  -0.42446 -0.46652 180 GLN   B C   
3126 O O   . GLN   B 87  ? 1.22237 1.43054 1.31075 0.55666  -0.41620 -0.47519 180 GLN   B O   
3127 C CB  . GLN   B 87  ? 1.03759 1.14198 1.08179 0.52361  -0.42448 -0.41071 180 GLN   B CB  
3128 C CG  . GLN   B 87  ? 1.15952 1.26764 1.21288 0.49685  -0.40750 -0.38208 180 GLN   B CG  
3129 C CD  . GLN   B 87  ? 1.00615 1.17016 1.09360 0.49144  -0.39900 -0.38914 180 GLN   B CD  
3130 O OE1 . GLN   B 87  ? 1.13463 1.29620 1.21728 0.50968  -0.41765 -0.40708 180 GLN   B OE1 
3131 N NE2 . GLN   B 87  ? 1.02479 1.23886 1.14622 0.46599  -0.37138 -0.37567 180 GLN   B NE2 
3132 N N   . GLU   B 88  ? 1.30027 1.46611 1.36465 0.57587  -0.45240 -0.48147 181 GLU   B N   
3133 C CA  . GLU   B 88  ? 1.40433 1.56063 1.45437 0.60496  -0.47685 -0.50986 181 GLU   B CA  
3134 C C   . GLU   B 88  ? 1.29312 1.36224 1.28981 0.62335  -0.51467 -0.50729 181 GLU   B C   
3135 O O   . GLU   B 88  ? 1.54345 1.59466 1.53276 0.61988  -0.52138 -0.49814 181 GLU   B O   
3136 C CB  . GLU   B 88  ? 1.37601 1.62073 1.47263 0.61502  -0.46945 -0.54262 181 GLU   B CB  
3137 C CG  . GLU   B 88  ? 1.42702 1.75898 1.57300 0.59558  -0.43232 -0.54769 181 GLU   B CG  
3138 C CD  . GLU   B 88  ? 1.49450 1.91109 1.68376 0.60155  -0.42472 -0.57835 181 GLU   B CD  
3139 O OE1 . GLU   B 88  ? 1.53504 1.94459 1.71863 0.62251  -0.44879 -0.59657 181 GLU   B OE1 
3140 O OE2 . GLU   B 88  ? 1.54598 2.03488 1.77332 0.58445  -0.39484 -0.58434 181 GLU   B OE2 
3141 N N   . ASN   B 89  ? 1.32133 1.33507 1.27890 0.64189  -0.53943 -0.51511 182 ASN   B N   
3142 C CA  . ASN   B 89  ? 1.42834 1.35640 1.33004 0.66059  -0.57783 -0.51596 182 ASN   B CA  
3143 C C   . ASN   B 89  ? 1.53195 1.38154 1.39128 0.64185  -0.58280 -0.48109 182 ASN   B C   
3144 O O   . ASN   B 89  ? 1.69031 1.54416 1.55526 0.63567  -0.58153 -0.47379 182 ASN   B O   
3145 C CB  . ASN   B 89  ? 1.34096 1.30101 1.25735 0.68371  -0.59519 -0.54486 182 ASN   B CB  
3146 C CG  . ASN   B 89  ? 1.50846 1.54704 1.46550 0.70200  -0.59157 -0.58078 182 ASN   B CG  
3147 O OD1 . ASN   B 89  ? 1.48424 1.60736 1.49262 0.69861  -0.57241 -0.59635 182 ASN   B OD1 
3148 N ND2 . ASN   B 89  ? 1.37808 1.38881 1.31114 0.72031  -0.61016 -0.59397 182 ASN   B ND2 
3149 N N   . VAL   B 90  ? 1.51686 1.29409 1.33233 0.63186  -0.58882 -0.45958 183 VAL   B N   
3150 C CA  . VAL   B 90  ? 1.60568 1.30365 1.37550 0.61116  -0.59343 -0.42545 183 VAL   B CA  
3151 C C   . VAL   B 90  ? 1.46592 1.06212 1.16501 0.62035  -0.62736 -0.42134 183 VAL   B C   
3152 O O   . VAL   B 90  ? 1.61567 1.19650 1.30148 0.63016  -0.63617 -0.43099 183 VAL   B O   
3153 C CB  . VAL   B 90  ? 1.58893 1.29701 1.37330 0.58163  -0.56335 -0.39798 183 VAL   B CB  
3154 C CG1 . VAL   B 90  ? 1.50543 1.12383 1.23517 0.55963  -0.57075 -0.36310 183 VAL   B CG1 
3155 C CG2 . VAL   B 90  ? 1.28539 1.08738 1.13389 0.56965  -0.53156 -0.39902 183 VAL   B CG2 
3156 N N   . VAL   B 91  ? 1.78700 1.31354 1.43916 0.61614  -0.64646 -0.40694 184 VAL   B N   
3157 C CA  . VAL   B 91  ? 1.88837 1.31213 1.46710 0.62010  -0.67856 -0.40005 184 VAL   B CA  
3158 C C   . VAL   B 91  ? 1.84108 1.20227 1.38234 0.58850  -0.66872 -0.36522 184 VAL   B C   
3159 O O   . VAL   B 91  ? 1.84191 1.22704 1.40606 0.56366  -0.64136 -0.34333 184 VAL   B O   
3160 C CB  . VAL   B 91  ? 1.91338 1.28914 1.45524 0.62865  -0.70353 -0.40120 184 VAL   B CB  
3161 C CG1 . VAL   B 91  ? 1.89236 1.24907 1.42562 0.60000  -0.68785 -0.37010 184 VAL   B CG1 
3162 C CG2 . VAL   B 91  ? 1.93487 1.21272 1.40293 0.63912  -0.74079 -0.40272 184 VAL   B CG2 
3163 N N   . LYS   B 92  ? 1.81489 1.09539 1.29728 0.58875  -0.69185 -0.36033 185 LYS   B N   
3164 C CA  . LYS   B 92  ? 1.95513 1.17536 1.40011 0.55745  -0.68327 -0.32908 185 LYS   B CA  
3165 C C   . LYS   B 92  ? 1.90105 1.06974 1.31095 0.52799  -0.67838 -0.29772 185 LYS   B C   
3166 O O   . LYS   B 92  ? 1.78590 0.93618 1.18787 0.49693  -0.65881 -0.27032 185 LYS   B O   
3167 C CB  . LYS   B 92  ? 1.91467 1.05997 1.30235 0.56354  -0.71077 -0.33175 185 LYS   B CB  
3168 C CG  . LYS   B 92  ? 2.17061 1.23791 1.49475 0.57357  -0.74662 -0.33467 185 LYS   B CG  
3169 C CD  . LYS   B 92  ? 2.29085 1.28163 1.55589 0.57527  -0.77241 -0.33357 185 LYS   B CD  
3170 C CE  . LYS   B 92  ? 2.55346 1.46145 1.75022 0.58346  -0.80873 -0.33524 185 LYS   B CE  
3171 N NZ  . LYS   B 92  ? 2.58981 1.42136 1.72638 0.58412  -0.83482 -0.33331 185 LYS   B NZ  
3172 N N   . THR   B 93  ? 1.82805 0.97337 1.21612 0.53664  -0.69566 -0.30158 186 THR   B N   
3173 C CA  . THR   B 93  ? 1.94490 1.04490 1.29972 0.50873  -0.69031 -0.27270 186 THR   B CA  
3174 C C   . THR   B 93  ? 1.88875 1.05993 1.29946 0.49359  -0.65736 -0.26055 186 THR   B C   
3175 O O   . THR   B 93  ? 1.87391 1.01455 1.26199 0.46415  -0.64594 -0.23196 186 THR   B O   
3176 C CB  . THR   B 93  ? 2.06680 1.12452 1.38411 0.52387  -0.71808 -0.28183 186 THR   B CB  
3177 O OG1 . THR   B 93  ? 2.01516 1.15144 1.38922 0.55097  -0.71623 -0.30775 186 THR   B OG1 
3178 C CG2 . THR   B 93  ? 2.01898 1.00624 1.27955 0.54072  -0.75330 -0.29511 186 THR   B CG2 
3179 N N   . LEU   B 94  ? 1.84808 1.11431 1.32957 0.51165  -0.64182 -0.28170 187 LEU   B N   
3180 C CA  . LEU   B 94  ? 1.72726 1.06728 1.26476 0.49767  -0.61061 -0.27175 187 LEU   B CA  
3181 C C   . LEU   B 94  ? 1.76813 1.12549 1.32428 0.47674  -0.58598 -0.25546 187 LEU   B C   
3182 O O   . LEU   B 94  ? 1.67539 1.07978 1.26697 0.45940  -0.56111 -0.24086 187 LEU   B O   
3183 C CB  . LEU   B 94  ? 1.64588 1.08307 1.25043 0.52344  -0.60397 -0.30255 187 LEU   B CB  
3184 C CG  . LEU   B 94  ? 1.63968 1.15755 1.30193 0.51195  -0.57630 -0.29682 187 LEU   B CG  
3185 C CD1 . LEU   B 94  ? 1.67857 1.16037 1.31269 0.49718  -0.58066 -0.27640 187 LEU   B CD1 
3186 C CD2 . LEU   B 94  ? 1.54626 1.15748 1.27079 0.53560  -0.57031 -0.33028 187 LEU   B CD2 
3187 N N   . LEU   B 95  ? 1.66256 0.98194 1.19424 0.47783  -0.59353 -0.25768 188 LEU   B N   
3188 C CA  . LEU   B 95  ? 1.63126 0.96628 1.18120 0.45995  -0.57117 -0.24481 188 LEU   B CA  
3189 C C   . LEU   B 95  ? 1.51650 0.80476 1.03586 0.42227  -0.55848 -0.20782 188 LEU   B C   
3190 O O   . LEU   B 95  ? 1.52637 0.86100 1.08113 0.40145  -0.52963 -0.19527 188 LEU   B O   
3191 C CB  . LEU   B 95  ? 1.65607 0.95354 1.18064 0.46888  -0.58468 -0.25551 188 LEU   B CB  
3192 C CG  . LEU   B 95  ? 1.65471 1.00231 1.20990 0.50464  -0.59544 -0.29227 188 LEU   B CG  
3193 C CD1 . LEU   B 95  ? 1.65457 0.95669 1.17738 0.51008  -0.61004 -0.29837 188 LEU   B CD1 
3194 C CD2 . LEU   B 95  ? 1.50737 0.96295 1.13955 0.51235  -0.56762 -0.30741 188 LEU   B CD2 
3195 N N   . GLN   B 96  ? 1.61106 0.81435 1.06480 0.40681  -0.57521 -0.19096 189 GLN   B N   
3196 C CA  . GLN   B 96  ? 1.64947 0.80617 1.06910 0.36713  -0.56204 -0.15619 189 GLN   B CA  
3197 C C   . GLN   B 96  ? 1.59084 0.80299 1.04561 0.35373  -0.54036 -0.14392 189 GLN   B C   
3198 O O   . GLN   B 96  ? 1.49965 0.73456 0.96661 0.31407  -0.50761 -0.12388 189 GLN   B O   
3199 C CB  . GLN   B 96  ? 1.63474 0.69427 0.97593 0.35176  -0.58324 -0.14331 189 GLN   B CB  
3200 C CG  . GLN   B 96  ? 1.80940 0.81840 1.11025 0.30612  -0.56801 -0.10865 189 GLN   B CG  
3201 C CD  . GLN   B 96  ? 2.02216 0.94077 1.24549 0.28884  -0.58733 -0.09715 189 GLN   B CD  
3202 O OE1 . GLN   B 96  ? 2.24144 1.13548 1.44130 0.31209  -0.61288 -0.11288 189 GLN   B OE1 
3203 N NE2 . GLN   B 96  ? 1.98430 0.85461 1.16741 0.24674  -0.57475 -0.07053 189 GLN   B NE2 
3204 N N   . LEU   B 97  ? 1.57275 0.82111 1.04960 0.37753  -0.54995 -0.15919 190 LEU   B N   
3205 C CA  . LEU   B 97  ? 1.62036 0.92736 1.13286 0.36372  -0.52857 -0.15026 190 LEU   B CA  
3206 C C   . LEU   B 97  ? 1.48874 0.89625 1.07463 0.35266  -0.49123 -0.15725 190 LEU   B C   
3207 O O   . LEU   B 97  ? 1.41338 0.85558 1.01923 0.31915  -0.45985 -0.13991 190 LEU   B O   
3208 C CB  . LEU   B 97  ? 1.50033 0.82488 1.02151 0.39110  -0.54708 -0.16811 190 LEU   B CB  
3209 C CG  . LEU   B 97  ? 1.35799 0.74427 0.91720 0.38381  -0.53144 -0.16228 190 LEU   B CG  
3210 C CD1 . LEU   B 97  ? 1.56577 0.91244 1.08744 0.34092  -0.51398 -0.13011 190 LEU   B CD1 
3211 C CD2 . LEU   B 97  ? 1.56113 0.96760 1.13207 0.40873  -0.54681 -0.18427 190 LEU   B CD2 
3212 N N   . ILE   B 98  ? 1.28570 0.73957 0.91037 0.38060  -0.49445 -0.18298 191 ILE   B N   
3213 C CA  . ILE   B 98  ? 1.46718 1.01238 1.15651 0.37000  -0.45999 -0.18987 191 ILE   B CA  
3214 C C   . ILE   B 98  ? 1.29925 0.83100 0.97984 0.33330  -0.43477 -0.16938 191 ILE   B C   
3215 O O   . ILE   B 98  ? 1.16474 0.75304 0.88263 0.30739  -0.40156 -0.15994 191 ILE   B O   
3216 C CB  . ILE   B 98  ? 1.35136 0.94550 1.07871 0.40836  -0.47023 -0.22331 191 ILE   B CB  
3217 C CG1 . ILE   B 98  ? 1.31903 0.93647 1.06181 0.44436  -0.49425 -0.24549 191 ILE   B CG1 
3218 C CG2 . ILE   B 98  ? 1.16820 0.85136 0.95589 0.39482  -0.43419 -0.22925 191 ILE   B CG2 
3219 C CD1 . ILE   B 98  ? 1.35709 1.03047 1.13843 0.47561  -0.49832 -0.28113 191 ILE   B CD1 
3220 N N   . GLY   B 99  ? 1.35481 0.81013 0.98507 0.33039  -0.45126 -0.16252 192 GLY   B N   
3221 C CA  . GLY   B 99  ? 1.24410 0.68721 0.86670 0.29641  -0.42952 -0.14518 192 GLY   B CA  
3222 C C   . GLY   B 99  ? 1.34978 0.78041 0.95794 0.25486  -0.40830 -0.11648 192 GLY   B C   
3223 O O   . GLY   B 99  ? 1.22595 0.70178 0.86489 0.22777  -0.37720 -0.10633 192 GLY   B O   
3224 N N   . ILE   B 100 ? 1.30199 0.67082 0.86184 0.24990  -0.42534 -0.10376 193 ILE   B N   
3225 C CA  . ILE   B 100 ? 1.43155 0.78549 0.97329 0.20997  -0.40549 -0.07745 193 ILE   B CA  
3226 C C   . ILE   B 100 ? 1.25447 0.68743 0.84806 0.20184  -0.37928 -0.07631 193 ILE   B C   
3227 O O   . ILE   B 100 ? 1.19798 0.65057 0.80139 0.16848  -0.35209 -0.05909 193 ILE   B O   
3228 C CB  . ILE   B 100 ? 1.50456 0.76852 0.97576 0.20606  -0.43086 -0.06433 193 ILE   B CB  
3229 C CG1 . ILE   B 100 ? 1.41176 0.65106 0.85615 0.15997  -0.40933 -0.03701 193 ILE   B CG1 
3230 C CG2 . ILE   B 100 ? 1.41472 0.68675 0.88751 0.23289  -0.44903 -0.07399 193 ILE   B CG2 
3231 C CD1 . ILE   B 100 ? 1.33607 0.56391 0.77580 0.13153  -0.39338 -0.02731 193 ILE   B CD1 
3232 N N   . SER   B 101 ? 1.26497 0.74543 0.89323 0.23181  -0.38707 -0.09555 194 SER   B N   
3233 C CA  . SER   B 101 ? 1.14683 0.70244 0.82498 0.22382  -0.36271 -0.09577 194 SER   B CA  
3234 C C   . SER   B 101 ? 1.03481 0.65967 0.76549 0.21220  -0.33271 -0.09907 194 SER   B C   
3235 O O   . SER   B 101 ? 0.95407 0.62377 0.71374 0.18981  -0.30579 -0.08920 194 SER   B O   
3236 C CB  . SER   B 101 ? 1.19040 0.77710 0.89014 0.25771  -0.38063 -0.11644 194 SER   B CB  
3237 O OG  . SER   B 101 ? 1.27558 0.79534 0.92388 0.26975  -0.41056 -0.11321 194 SER   B OG  
3238 N N   . SER   B 102 ? 1.06442 0.69679 0.80574 0.22787  -0.33785 -0.11333 195 SER   B N   
3239 C CA  . SER   B 102 ? 0.94138 0.62909 0.72331 0.21469  -0.31075 -0.11444 195 SER   B CA  
3240 C C   . SER   B 102 ? 0.96655 0.63235 0.73245 0.17693  -0.29125 -0.09068 195 SER   B C   
3241 O O   . SER   B 102 ? 0.95399 0.66959 0.75396 0.15726  -0.26383 -0.08387 195 SER   B O   
3242 C CB  . SER   B 102 ? 0.98581 0.67634 0.77364 0.23863  -0.32238 -0.13415 195 SER   B CB  
3243 O OG  . SER   B 102 ? 1.08296 0.80086 0.88993 0.27465  -0.33966 -0.15889 195 SER   B OG  
3244 N N   . LEU   B 103 ? 1.04607 0.63712 0.75944 0.16606  -0.30565 -0.07843 196 LEU   B N   
3245 C CA  . LEU   B 103 ? 0.97770 0.54884 0.67526 0.12877  -0.28775 -0.05698 196 LEU   B CA  
3246 C C   . LEU   B 103 ? 0.95186 0.54016 0.65506 0.10652  -0.27019 -0.04179 196 LEU   B C   
3247 O O   . LEU   B 103 ? 0.98318 0.59333 0.70049 0.07847  -0.24607 -0.02905 196 LEU   B O   
3248 C CB  . LEU   B 103 ? 1.08100 0.56614 0.71811 0.12089  -0.30813 -0.04838 196 LEU   B CB  
3249 C CG  . LEU   B 103 ? 1.14885 0.61145 0.76794 0.08162  -0.29149 -0.02877 196 LEU   B CG  
3250 C CD1 . LEU   B 103 ? 1.16484 0.67907 0.82528 0.07322  -0.27079 -0.03238 196 LEU   B CD1 
3251 C CD2 . LEU   B 103 ? 1.22471 0.59865 0.78072 0.07438  -0.31409 -0.02186 196 LEU   B CD2 
3252 N N   . PHE   B 104 ? 1.03086 0.61029 0.72345 0.11966  -0.28273 -0.04409 197 PHE   B N   
3253 C CA  . PHE   B 104 ? 0.97903 0.57602 0.67696 0.10059  -0.26676 -0.03155 197 PHE   B CA  
3254 C C   . PHE   B 104 ? 0.90113 0.57926 0.65861 0.09668  -0.24038 -0.03581 197 PHE   B C   
3255 O O   . PHE   B 104 ? 0.94564 0.64460 0.71505 0.07107  -0.21744 -0.02295 197 PHE   B O   
3256 C CB  . PHE   B 104 ? 1.04738 0.61638 0.71991 0.11830  -0.28878 -0.03501 197 PHE   B CB  
3257 C CG  . PHE   B 104 ? 1.16297 0.74415 0.83526 0.09982  -0.27474 -0.02288 197 PHE   B CG  
3258 C CD1 . PHE   B 104 ? 1.20488 0.76213 0.85301 0.06585  -0.25868 -0.00327 197 PHE   B CD1 
3259 C CD2 . PHE   B 104 ? 1.15483 0.77248 0.85104 0.11627  -0.27783 -0.03241 197 PHE   B CD2 
3260 C CE1 . PHE   B 104 ? 1.31636 0.88547 0.96351 0.04988  -0.24556 0.00633  197 PHE   B CE1 
3261 C CE2 . PHE   B 104 ? 1.16610 0.79299 0.86035 0.09981  -0.26572 -0.02210 197 PHE   B CE2 
3262 C CZ  . PHE   B 104 ? 1.10168 0.70379 0.77078 0.06725  -0.24949 -0.00284 197 PHE   B CZ  
3263 N N   . ILE   B 105 ? 0.97522 0.69948 0.76955 0.12172  -0.24351 -0.05455 198 ILE   B N   
3264 C CA  . ILE   B 105 ? 0.82472 0.62240 0.67215 0.11692  -0.21904 -0.05879 198 ILE   B CA  
3265 C C   . ILE   B 105 ? 0.76838 0.57975 0.62812 0.09584  -0.19876 -0.05025 198 ILE   B C   
3266 O O   . ILE   B 105 ? 0.69175 0.53973 0.57665 0.07715  -0.17571 -0.04200 198 ILE   B O   
3267 C CB  . ILE   B 105 ? 0.83295 0.67549 0.71388 0.14639  -0.22671 -0.08183 198 ILE   B CB  
3268 C CG1 . ILE   B 105 ? 0.81711 0.64739 0.68713 0.16900  -0.24934 -0.09200 198 ILE   B CG1 
3269 C CG2 . ILE   B 105 ? 0.80773 0.72242 0.73896 0.13832  -0.20106 -0.08511 198 ILE   B CG2 
3270 C CD1 . ILE   B 105 ? 0.81971 0.68857 0.71841 0.20089  -0.26154 -0.11770 198 ILE   B CD1 
3271 N N   . ALA   B 106 ? 0.84116 0.62178 0.68238 0.09933  -0.20846 -0.05276 199 ALA   B N   
3272 C CA  . ALA   B 106 ? 0.87865 0.67248 0.73154 0.08117  -0.19171 -0.04646 199 ALA   B CA  
3273 C C   . ALA   B 106 ? 0.72776 0.50214 0.56500 0.04927  -0.17807 -0.02655 199 ALA   B C   
3274 O O   . ALA   B 106 ? 0.76471 0.57316 0.62684 0.03209  -0.15720 -0.02033 199 ALA   B O   
3275 C CB  . ALA   B 106 ? 0.87777 0.63835 0.71065 0.09239  -0.20756 -0.05452 199 ALA   B CB  
3276 N N   . ALA   B 107 ? 0.88418 0.60419 0.67932 0.04105  -0.18983 -0.01705 200 ALA   B N   
3277 C CA  . ALA   B 107 ? 0.92470 0.62740 0.70336 0.00936  -0.17617 0.00042  200 ALA   B CA  
3278 C C   . ALA   B 107 ? 0.78298 0.53195 0.59116 -0.00181 -0.15493 0.00592  200 ALA   B C   
3279 O O   . ALA   B 107 ? 0.85416 0.62289 0.67580 -0.02425 -0.13553 0.01482  200 ALA   B O   
3280 C CB  . ALA   B 107 ? 1.00055 0.63272 0.72305 0.00227  -0.19356 0.00909  200 ALA   B CB  
3281 N N   . LYS   B 108 ? 0.88122 0.64831 0.70026 0.01423  -0.15921 -0.00039 201 LYS   B N   
3282 C CA  . LYS   B 108 ? 0.76937 0.57764 0.61489 0.00462  -0.14052 0.00381  201 LYS   B CA  
3283 C C   . LYS   B 108 ? 0.85211 0.71863 0.74445 0.00313  -0.12155 -0.00023 201 LYS   B C   
3284 O O   . LYS   B 108 ? 0.73721 0.63265 0.64915 -0.01121 -0.10321 0.00609  201 LYS   B O   
3285 C CB  . LYS   B 108 ? 0.86078 0.67383 0.70637 0.02234  -0.15150 -0.00327 201 LYS   B CB  
3286 C CG  . LYS   B 108 ? 0.92039 0.67704 0.71751 0.01952  -0.16718 0.00393  201 LYS   B CG  
3287 C CD  . LYS   B 108 ? 0.94838 0.71524 0.74887 0.03587  -0.17692 -0.00307 201 LYS   B CD  
3288 C CE  . LYS   B 108 ? 0.98786 0.76818 0.80354 0.06744  -0.19572 -0.02138 201 LYS   B CE  
3289 N NZ  . LYS   B 108 ? 0.92047 0.70953 0.73831 0.08365  -0.20790 -0.02943 201 LYS   B NZ  
3290 N N   . LEU   B 109 ? 0.78683 0.66921 0.69511 0.01794  -0.12612 -0.01098 202 LEU   B N   
3291 C CA  . LEU   B 109 ? 0.71942 0.65293 0.66687 0.01607  -0.10909 -0.01436 202 LEU   B CA  
3292 C C   . LEU   B 109 ? 0.73106 0.66283 0.67938 -0.00376 -0.09721 -0.00511 202 LEU   B C   
3293 O O   . LEU   B 109 ? 0.68438 0.65109 0.65849 -0.01424 -0.07987 -0.00117 202 LEU   B O   
3294 C CB  . LEU   B 109 ? 0.71034 0.66432 0.67348 0.03872  -0.11729 -0.03041 202 LEU   B CB  
3295 C CG  . LEU   B 109 ? 0.81338 0.79656 0.79507 0.05737  -0.12203 -0.04297 202 LEU   B CG  
3296 C CD1 . LEU   B 109 ? 0.71915 0.71659 0.71050 0.08040  -0.13268 -0.06080 202 LEU   B CD1 
3297 C CD2 . LEU   B 109 ? 0.71036 0.74164 0.72508 0.04733  -0.10181 -0.04040 202 LEU   B CD2 
3298 N N   . GLU   B 110 ? 0.76564 0.65608 0.68542 -0.00916 -0.10736 -0.00204 203 GLU   B N   
3299 C CA  . GLU   B 110 ? 0.79060 0.68184 0.71336 -0.02538 -0.09900 0.00333  203 GLU   B CA  
3300 C C   . GLU   B 110 ? 0.92944 0.80018 0.83523 -0.05137 -0.09139 0.01645  203 GLU   B C   
3301 O O   . GLU   B 110 ? 0.84081 0.73586 0.76519 -0.06673 -0.07673 0.02115  203 GLU   B O   
3302 C CB  . GLU   B 110 ? 0.77240 0.63487 0.67719 -0.01587 -0.11452 -0.00367 203 GLU   B CB  
3303 C CG  . GLU   B 110 ? 0.93730 0.80680 0.84962 -0.02938 -0.10725 -0.00110 203 GLU   B CG  
3304 C CD  . GLU   B 110 ? 0.90117 0.82393 0.85160 -0.02527 -0.09301 -0.00529 203 GLU   B CD  
3305 O OE1 . GLU   B 110 ? 0.97054 0.92069 0.93855 -0.00835 -0.09206 -0.01360 203 GLU   B OE1 
3306 O OE2 . GLU   B 110 ? 1.20699 1.14390 1.16878 -0.03959 -0.08320 -0.00053 203 GLU   B OE2 
3307 N N   . GLU   B 111 ? 0.81903 0.64623 0.68919 -0.05685 -0.10115 0.02181  204 GLU   B N   
3308 C CA  . GLU   B 111 ? 0.82736 0.63239 0.67666 -0.08397 -0.09383 0.03345  204 GLU   B CA  
3309 C C   . GLU   B 111 ? 1.00820 0.84474 0.87544 -0.09524 -0.07589 0.03892  204 GLU   B C   
3310 O O   . GLU   B 111 ? 0.89898 0.75068 0.77557 -0.08278 -0.07565 0.03614  204 GLU   B O   
3311 C CB  . GLU   B 111 ? 0.80542 0.54708 0.60374 -0.08747 -0.11114 0.03796  204 GLU   B CB  
3312 C CG  . GLU   B 111 ? 0.95713 0.65993 0.73267 -0.07372 -0.13213 0.03150  204 GLU   B CG  
3313 C CD  . GLU   B 111 ? 1.14633 0.84557 0.92353 -0.08873 -0.12874 0.03263  204 GLU   B CD  
3314 O OE1 . GLU   B 111 ? 1.06678 0.78332 0.85388 -0.11369 -0.11218 0.04008  204 GLU   B OE1 
3315 O OE2 . GLU   B 111 ? 1.01228 0.69271 0.78151 -0.07491 -0.14322 0.02478  204 GLU   B OE2 
3316 N N   . ILE   B 112 ? 0.86038 0.70802 0.73319 -0.11875 -0.06123 0.04544  205 ILE   B N   
3317 C CA  . ILE   B 112 ? 1.00239 0.87818 0.89028 -0.12993 -0.04423 0.04950  205 ILE   B CA  
3318 C C   . ILE   B 112 ? 0.97567 0.81693 0.82746 -0.13718 -0.04807 0.05536  205 ILE   B C   
3319 O O   . ILE   B 112 ? 0.95345 0.80891 0.81180 -0.13074 -0.04394 0.05481  205 ILE   B O   
3320 C CB  . ILE   B 112 ? 0.93151 0.83125 0.83651 -0.15165 -0.02852 0.05243  205 ILE   B CB  
3321 C CG1 . ILE   B 112 ? 0.80844 0.74361 0.74908 -0.14238 -0.02562 0.04661  205 ILE   B CG1 
3322 C CG2 . ILE   B 112 ? 0.84250 0.76798 0.75937 -0.16293 -0.01180 0.05518  205 ILE   B CG2 
3323 C CD1 . ILE   B 112 ? 0.83364 0.79668 0.79520 -0.16026 -0.01231 0.04757  205 ILE   B CD1 
3324 N N   . TYR   B 113 ? 0.91321 0.70604 0.72358 -0.15163 -0.05656 0.06123  206 TYR   B N   
3325 C CA  . TYR   B 113 ? 1.04250 0.79170 0.80856 -0.15926 -0.06330 0.06783  206 TYR   B CA  
3326 C C   . TYR   B 113 ? 1.03076 0.72469 0.75889 -0.14561 -0.08853 0.06682  206 TYR   B C   
3327 O O   . TYR   B 113 ? 1.11976 0.76893 0.81232 -0.16075 -0.09615 0.07211  206 TYR   B O   
3328 C CB  . TYR   B 113 ? 1.08928 0.82601 0.83349 -0.19256 -0.04991 0.07658  206 TYR   B CB  
3329 C CG  . TYR   B 113 ? 1.09733 0.88950 0.87942 -0.20486 -0.02582 0.07546  206 TYR   B CG  
3330 C CD1 . TYR   B 113 ? 0.97837 0.79217 0.76959 -0.20089 -0.01663 0.07494  206 TYR   B CD1 
3331 C CD2 . TYR   B 113 ? 1.08929 0.91141 0.89751 -0.21947 -0.01362 0.07382  206 TYR   B CD2 
3332 C CE1 . TYR   B 113 ? 1.07784 0.94004 0.90256 -0.21002 0.00394  0.07253  206 TYR   B CE1 
3333 C CE2 . TYR   B 113 ? 1.08166 0.95427 0.92485 -0.22800 0.00638  0.07113  206 TYR   B CE2 
3334 C CZ  . TYR   B 113 ? 1.15198 1.04354 1.00283 -0.22275 0.01504  0.07038  206 TYR   B CZ  
3335 O OH  . TYR   B 113 ? 1.18942 1.12907 1.07404 -0.22918 0.03355  0.06637  206 TYR   B OH  
3336 N N   . PRO   B 114 ? 1.06567 0.76105 0.80008 -0.11713 -0.10259 0.05915  207 PRO   B N   
3337 C CA  . PRO   B 114 ? 0.98312 0.62933 0.68509 -0.09938 -0.12851 0.05525  207 PRO   B CA  
3338 C C   . PRO   B 114 ? 1.13942 0.72278 0.78332 -0.10810 -0.14185 0.06386  207 PRO   B C   
3339 O O   . PRO   B 114 ? 1.24492 0.82986 0.87787 -0.12236 -0.13142 0.07091  207 PRO   B O   
3340 C CB  . PRO   B 114 ? 1.03213 0.71130 0.76510 -0.06749 -0.13601 0.04281  207 PRO   B CB  
3341 C CG  . PRO   B 114 ? 1.07508 0.79649 0.83393 -0.07241 -0.11857 0.04459  207 PRO   B CG  
3342 C CD  . PRO   B 114 ? 1.06205 0.80558 0.83446 -0.09989 -0.09576 0.05244  207 PRO   B CD  
3343 N N   . PRO   B 115 ? 1.22037 0.74485 0.82311 -0.09993 -0.16551 0.06341  208 PRO   B N   
3344 C CA  . PRO   B 115 ? 1.32025 0.77759 0.86170 -0.10574 -0.18181 0.07180  208 PRO   B CA  
3345 C C   . PRO   B 115 ? 1.41028 0.87327 0.95189 -0.08248 -0.19221 0.06681  208 PRO   B C   
3346 O O   . PRO   B 115 ? 1.10308 0.61131 0.68698 -0.05649 -0.19400 0.05441  208 PRO   B O   
3347 C CB  . PRO   B 115 ? 1.33306 0.72958 0.83699 -0.09578 -0.20758 0.06937  208 PRO   B CB  
3348 C CG  . PRO   B 115 ? 1.27120 0.70192 0.81271 -0.09734 -0.19823 0.06332  208 PRO   B CG  
3349 C CD  . PRO   B 115 ? 1.28630 0.79827 0.89229 -0.08693 -0.17864 0.05567  208 PRO   B CD  
3350 N N   . LYS   B 116 ? 1.38226 0.79823 0.87414 -0.09361 -0.19909 0.07649  209 LYS   B N   
3351 C CA  . LYS   B 116 ? 1.38235 0.79822 0.86825 -0.07374 -0.21053 0.07253  209 LYS   B CA  
3352 C C   . LYS   B 116 ? 1.35123 0.73179 0.81953 -0.03883 -0.24394 0.06179  209 LYS   B C   
3353 O O   . LYS   B 116 ? 1.46016 0.80477 0.91046 -0.03203 -0.25943 0.05919  209 LYS   B O   
3354 C CB  . LYS   B 116 ? 1.46757 0.84182 0.90163 -0.09722 -0.20781 0.08633  209 LYS   B CB  
3355 C CG  . LYS   B 116 ? 1.40584 0.82467 0.86256 -0.12693 -0.17464 0.09331  209 LYS   B CG  
3356 C CD  . LYS   B 116 ? 1.44162 0.93511 0.96032 -0.11153 -0.16045 0.08333  209 LYS   B CD  
3357 C CE  . LYS   B 116 ? 1.37544 0.91062 0.91514 -0.13798 -0.12963 0.08875  209 LYS   B CE  
3358 N NZ  . LYS   B 116 ? 1.14520 0.69967 0.70388 -0.15995 -0.11148 0.09186  209 LYS   B NZ  
3359 N N   . LEU   B 117 ? 1.30794 0.70017 0.78234 -0.01574 -0.25579 0.05416  210 LEU   B N   
3360 C CA  . LEU   B 117 ? 1.32045 0.68993 0.78595 0.02109  -0.28775 0.04055  210 LEU   B CA  
3361 C C   . LEU   B 117 ? 1.53024 0.80607 0.92112 0.02131  -0.31611 0.04797  210 LEU   B C   
3362 O O   . LEU   B 117 ? 1.62955 0.87528 1.00895 0.04407  -0.33981 0.03861  210 LEU   B O   
3363 C CB  . LEU   B 117 ? 1.37898 0.78110 0.86506 0.04246  -0.29428 0.03107  210 LEU   B CB  
3364 C CG  . LEU   B 117 ? 1.34687 0.71960 0.81521 0.08015  -0.33061 0.01711  210 LEU   B CG  
3365 C CD1 . LEU   B 117 ? 1.31632 0.72309 0.82658 0.10739  -0.33831 -0.00145 210 LEU   B CD1 
3366 C CD2 . LEU   B 117 ? 1.39852 0.79685 0.87848 0.09420  -0.33638 0.01068  210 LEU   B CD2 
3367 N N   . HIS   B 118 ? 1.52837 0.75514 0.86538 -0.00403 -0.31442 0.06443  211 HIS   B N   
3368 C CA  . HIS   B 118 ? 1.74722 0.87793 1.00573 -0.00536 -0.34272 0.07298  211 HIS   B CA  
3369 C C   . HIS   B 118 ? 1.59519 0.68546 0.83169 -0.01944 -0.34523 0.07774  211 HIS   B C   
3370 O O   . HIS   B 118 ? 1.74808 0.76278 0.93078 -0.00834 -0.37519 0.07832  211 HIS   B O   
3371 C CB  . HIS   B 118 ? 1.76161 0.85112 0.96569 -0.03440 -0.33643 0.09061  211 HIS   B CB  
3372 C CG  . HIS   B 118 ? 1.76479 0.85987 0.96268 -0.07976 -0.30489 0.10575  211 HIS   B CG  
3373 N ND1 . HIS   B 118 ? 1.80842 0.98049 1.06167 -0.09663 -0.27015 0.10560  211 HIS   B ND1 
3374 C CD2 . HIS   B 118 ? 1.90756 0.94175 1.05080 -0.11192 -0.30331 0.12040  211 HIS   B CD2 
3375 C CE1 . HIS   B 118 ? 1.81181 0.97406 1.04769 -0.13556 -0.24866 0.11827  211 HIS   B CE1 
3376 N NE2 . HIS   B 118 ? 2.02351 1.10398 1.19339 -0.14705 -0.26726 0.12758  211 HIS   B NE2 
3377 N N   . GLN   B 119 ? 1.65583 0.79309 0.93175 -0.04311 -0.31581 0.08060  212 GLN   B N   
3378 C CA  . GLN   B 119 ? 1.80853 0.91341 1.06900 -0.05603 -0.31809 0.08334  212 GLN   B CA  
3379 C C   . GLN   B 119 ? 1.60246 0.71146 0.88548 -0.01814 -0.34010 0.06532  212 GLN   B C   
3380 O O   . GLN   B 119 ? 1.70932 0.75635 0.95268 -0.01509 -0.36083 0.06531  212 GLN   B O   
3381 C CB  . GLN   B 119 ? 1.57679 0.73741 0.87852 -0.08838 -0.28211 0.08887  212 GLN   B CB  
3382 C CG  . GLN   B 119 ? 1.75731 0.90948 1.03237 -0.12932 -0.25993 0.10570  212 GLN   B CG  
3383 C CD  . GLN   B 119 ? 1.66037 0.87426 0.98203 -0.15743 -0.22574 0.10813  212 GLN   B CD  
3384 O OE1 . GLN   B 119 ? 1.61523 0.90484 0.99777 -0.14975 -0.20648 0.10098  212 GLN   B OE1 
3385 N NE2 . GLN   B 119 ? 1.77756 0.95828 1.06991 -0.19038 -0.21906 0.11778  212 GLN   B NE2 
3386 N N   . PHE   B 120 ? 1.60565 0.78681 0.95100 0.01026  -0.33571 0.04918  213 PHE   B N   
3387 C CA  . PHE   B 120 ? 1.57580 0.76603 0.94340 0.04824  -0.35639 0.02964  213 PHE   B CA  
3388 C C   . PHE   B 120 ? 1.55838 0.68127 0.87609 0.07821  -0.39591 0.02321  213 PHE   B C   
3389 O O   . PHE   B 120 ? 1.51898 0.61036 0.82447 0.10246  -0.41985 0.01144  213 PHE   B O   
3390 C CB  . PHE   B 120 ? 1.52863 0.81351 0.97249 0.06812  -0.34066 0.01418  213 PHE   B CB  
3391 C CG  . PHE   B 120 ? 1.35575 0.70241 0.85007 0.04870  -0.30913 0.01553  213 PHE   B CG  
3392 C CD1 . PHE   B 120 ? 1.37149 0.75292 0.88338 0.01783  -0.27945 0.02831  213 PHE   B CD1 
3393 C CD2 . PHE   B 120 ? 1.34329 0.71253 0.86619 0.06258  -0.31024 0.00311  213 PHE   B CD2 
3394 C CE1 . PHE   B 120 ? 1.38145 0.81752 0.93842 0.00217  -0.25306 0.02888  213 PHE   B CE1 
3395 C CE2 . PHE   B 120 ? 1.29136 0.71442 0.85743 0.04551  -0.28318 0.00456  213 PHE   B CE2 
3396 C CZ  . PHE   B 120 ? 1.24688 0.70268 0.83002 0.01578  -0.25535 0.01756  213 PHE   B CZ  
3397 N N   . ALA   B 121 ? 1.65088 0.75008 0.93838 0.07829  -0.40444 0.02987  214 ALA   B N   
3398 C CA  . ALA   B 121 ? 1.71895 0.74466 0.95013 0.10455  -0.44416 0.02597  214 ALA   B CA  
3399 C C   . ALA   B 121 ? 1.77174 0.69400 0.92056 0.08278  -0.46031 0.04259  214 ALA   B C   
3400 O O   . ALA   B 121 ? 1.91290 0.77642 1.02123 0.10438  -0.49207 0.03355  214 ALA   B O   
3401 C CB  . ALA   B 121 ? 1.60242 0.63670 0.82684 0.11126  -0.44856 0.02766  214 ALA   B CB  
3402 N N   . TYR   B 122 ? 1.69985 0.61252 0.83198 0.03718  -0.43398 0.06180  215 TYR   B N   
3403 C CA  . TYR   B 122 ? 1.72419 0.54926 0.78250 0.00902  -0.44330 0.07613  215 TYR   B CA  
3404 C C   . TYR   B 122 ? 1.88555 0.68294 0.93803 0.01794  -0.45758 0.06622  215 TYR   B C   
3405 O O   . TYR   B 122 ? 1.88849 0.62454 0.88939 0.01733  -0.47856 0.06258  215 TYR   B O   
3406 C CB  . TYR   B 122 ? 1.77359 0.60544 0.82185 -0.04272 -0.40939 0.09752  215 TYR   B CB  
3407 C CG  . TYR   B 122 ? 1.88771 0.66455 0.88387 -0.07854 -0.40745 0.10566  215 TYR   B CG  
3408 C CD1 . TYR   B 122 ? 2.02894 0.74843 0.96248 -0.09091 -0.41992 0.10951  215 TYR   B CD1 
3409 C CD2 . TYR   B 122 ? 1.94059 0.72431 0.95006 -0.10060 -0.39342 0.10897  215 TYR   B CD2 
3410 C CE1 . TYR   B 122 ? 1.89759 0.56885 0.78213 -0.12412 -0.41866 0.11695  215 TYR   B CE1 
3411 C CE2 . TYR   B 122 ? 2.09499 0.83394 1.05837 -0.13354 -0.39198 0.11581  215 TYR   B CE2 
3412 C CZ  . TYR   B 122 ? 2.02892 0.71201 0.92939 -0.14525 -0.40457 0.12010  215 TYR   B CZ  
3413 O OH  . TYR   B 122 ? 2.02681 0.66573 0.87973 -0.17848 -0.40355 0.12705  215 TYR   B OH  
3414 N N   . VAL   B 123 ? 1.79674 0.64437 0.90360 0.02575  -0.44538 0.05954  216 VAL   B N   
3415 C CA  . VAL   B 123 ? 1.73128 0.54898 0.83075 0.03322  -0.45863 0.05166  216 VAL   B CA  
3416 C C   . VAL   B 123 ? 1.90884 0.71315 1.00710 0.08111  -0.49238 0.02773  216 VAL   B C   
3417 O O   . VAL   B 123 ? 2.03271 0.80691 1.11533 0.08826  -0.50689 0.01852  216 VAL   B O   
3418 C CB  . VAL   B 123 ? 1.85096 0.75354 1.02288 0.02481  -0.42815 0.04465  216 VAL   B CB  
3419 C CG1 . VAL   B 123 ? 1.82798 0.75989 1.01000 -0.02373 -0.39176 0.06274  216 VAL   B CG1 
3420 C CG2 . VAL   B 123 ? 1.64752 0.64046 0.89303 0.05936  -0.42104 0.02538  216 VAL   B CG2 
3421 N N   . THR   B 124 ? 1.80389 0.63322 0.91951 0.11356  -0.50497 0.01606  217 THR   B N   
3422 C CA  . THR   B 124 ? 1.90646 0.73192 1.02624 0.15907  -0.53549 -0.00995 217 THR   B CA  
3423 C C   . THR   B 124 ? 2.09190 0.84170 1.14318 0.15928  -0.56224 -0.01236 217 THR   B C   
3424 O O   . THR   B 124 ? 1.93943 0.68102 0.98866 0.19637  -0.58942 -0.03467 217 THR   B O   
3425 C CB  . THR   B 124 ? 1.92733 0.82069 1.10100 0.19328  -0.53671 -0.02449 217 THR   B CB  
3426 O OG1 . THR   B 124 ? 1.95264 0.83814 1.10563 0.17970  -0.53271 -0.01234 217 THR   B OG1 
3427 C CG2 . THR   B 124 ? 1.68437 0.66573 0.93136 0.19232  -0.50804 -0.02663 217 THR   B CG2 
3428 N N   . ASP   B 125 ? 2.19222 0.88911 1.18804 0.11861  -0.55492 0.00880  218 ASP   B N   
3429 C CA  . ASP   B 125 ? 2.37025 0.99087 1.29493 0.11449  -0.57947 0.00885  218 ASP   B CA  
3430 C C   . ASP   B 125 ? 2.32712 0.95005 1.25109 0.14597  -0.59893 -0.00472 218 ASP   B C   
3431 O O   . ASP   B 125 ? 2.50120 1.08049 1.39160 0.17023  -0.62998 -0.02013 218 ASP   B O   
3432 C CB  . ASP   B 125 ? 2.47545 1.04839 1.36861 0.12587  -0.60386 -0.00248 218 ASP   B CB  
3433 C CG  . ASP   B 125 ? 2.57087 1.05726 1.38092 0.10325  -0.62117 0.00667  218 ASP   B CG  
3434 O OD1 . ASP   B 125 ? 2.71575 1.17610 1.49241 0.09329  -0.62377 0.01380  218 ASP   B OD1 
3435 O OD2 . ASP   B 125 ? 2.65368 1.09743 1.43055 0.09522  -0.63248 0.00667  218 ASP   B OD2 
3436 N N   . GLY   B 126 ? 2.12390 0.79897 1.08542 0.14571  -0.58108 0.00045  219 GLY   B N   
3437 C CA  . GLY   B 126 ? 2.31176 0.99632 1.27780 0.17260  -0.59621 -0.01135 219 GLY   B CA  
3438 C C   . GLY   B 126 ? 2.29813 1.02848 1.31378 0.22314  -0.61475 -0.04071 219 GLY   B C   
3439 O O   . GLY   B 126 ? 2.33927 1.08483 1.36508 0.24686  -0.62697 -0.05289 219 GLY   B O   
3440 N N   . ALA   B 127 ? 2.12912 0.88487 1.17714 0.23993  -0.61650 -0.05374 220 ALA   B N   
3441 C CA  . ALA   B 127 ? 2.00117 0.80717 1.09860 0.28684  -0.63187 -0.08419 220 ALA   B CA  
3442 C C   . ALA   B 127 ? 2.01310 0.91251 1.18521 0.29951  -0.61178 -0.08932 220 ALA   B C   
3443 O O   . ALA   B 127 ? 2.05751 1.00748 1.27341 0.33608  -0.62202 -0.11512 220 ALA   B O   
3444 C CB  . ALA   B 127 ? 2.10944 0.91481 1.21647 0.30001  -0.63921 -0.09743 220 ALA   B CB  
3445 N N   . CYS   B 128 ? 1.89968 0.82511 1.08674 0.26912  -0.58346 -0.06622 221 CYS   B N   
3446 C CA  . CYS   B 128 ? 1.94713 0.96031 1.20083 0.27705  -0.56424 -0.06856 221 CYS   B CA  
3447 C C   . CYS   B 128 ? 1.94448 0.95165 1.17878 0.24552  -0.54745 -0.04391 221 CYS   B C   
3448 O O   . CYS   B 128 ? 1.98968 0.96594 1.19406 0.20778  -0.53016 -0.01957 221 CYS   B O   
3449 C CB  . CYS   B 128 ? 1.79087 0.85808 1.09450 0.27503  -0.54468 -0.06834 221 CYS   B CB  
3450 S SG  . CYS   B 128 ? 1.76475 0.84596 1.09392 0.31110  -0.56102 -0.09858 221 CYS   B SG  
3451 N N   . SER   B 129 ? 1.72112 0.75926 0.97251 0.25989  -0.55179 -0.05135 222 SER   B N   
3452 C CA  . SER   B 129 ? 1.81449 0.85287 1.04990 0.23280  -0.53640 -0.03067 222 SER   B CA  
3453 C C   . SER   B 129 ? 1.70946 0.83323 1.00678 0.21919  -0.50417 -0.02550 222 SER   B C   
3454 O O   . SER   B 129 ? 1.71313 0.90319 1.07206 0.23134  -0.49169 -0.04096 222 SER   B O   
3455 C CB  . SER   B 129 ? 1.86252 0.89923 1.09103 0.25204  -0.55329 -0.04213 222 SER   B CB  
3456 O OG  . SER   B 129 ? 1.69361 0.81135 0.99011 0.28437  -0.55553 -0.06527 222 SER   B OG  
3457 N N   . GLY   B 130 ? 1.67112 0.80367 0.96047 0.18747  -0.48117 -0.00824 223 GLY   B N   
3458 C CA  . GLY   B 130 ? 1.43080 0.65235 0.78657 0.16826  -0.44178 -0.00783 223 GLY   B CA  
3459 C C   . GLY   B 130 ? 1.60173 0.90326 1.02283 0.19720  -0.44257 -0.02981 223 GLY   B C   
3460 O O   . GLY   B 130 ? 1.40956 0.78647 0.89507 0.19604  -0.41888 -0.03876 223 GLY   B O   
3461 N N   . ASP   B 131 ? 1.55881 0.84439 0.96286 0.22274  -0.47039 -0.03904 224 ASP   B N   
3462 C CA  . ASP   B 131 ? 1.62347 0.98558 1.08914 0.24995  -0.47312 -0.06163 224 ASP   B CA  
3463 C C   . ASP   B 131 ? 1.44917 0.84589 0.95583 0.28227  -0.48497 -0.08554 224 ASP   B C   
3464 O O   . ASP   B 131 ? 1.47261 0.95284 1.04647 0.29321  -0.47172 -0.10278 224 ASP   B O   
3465 C CB  . ASP   B 131 ? 1.71789 1.05176 1.15270 0.27000  -0.50277 -0.06657 224 ASP   B CB  
3466 C CG  . ASP   B 131 ? 1.86351 1.18161 1.26939 0.23934  -0.48728 -0.04664 224 ASP   B CG  
3467 O OD1 . ASP   B 131 ? 1.94793 1.31096 1.38511 0.20907  -0.45031 -0.03663 224 ASP   B OD1 
3468 O OD2 . ASP   B 131 ? 2.14221 1.40230 1.49280 0.24636  -0.51277 -0.04167 224 ASP   B OD2 
3469 N N   . GLU   B 132 ? 1.51713 0.85034 0.98293 0.29716  -0.50965 -0.08749 225 GLU   B N   
3470 C CA  . GLU   B 132 ? 1.48848 0.85305 0.99111 0.32708  -0.51945 -0.11073 225 GLU   B CA  
3471 C C   . GLU   B 132 ? 1.32175 0.74659 0.87516 0.30599  -0.48241 -0.10909 225 GLU   B C   
3472 O O   . GLU   B 132 ? 1.28639 0.78110 0.89816 0.32427  -0.47563 -0.13001 225 GLU   B O   
3473 C CB  . GLU   B 132 ? 1.59542 0.87726 1.04347 0.33923  -0.54514 -0.11425 225 GLU   B CB  
3474 C CG  . GLU   B 132 ? 1.74662 0.99349 1.16867 0.36237  -0.57163 -0.13080 225 GLU   B CG  
3475 C CD  . GLU   B 132 ? 1.94095 1.10370 1.30521 0.36875  -0.59466 -0.13436 225 GLU   B CD  
3476 O OE1 . GLU   B 132 ? 1.95555 1.06114 1.27565 0.34235  -0.58961 -0.11328 225 GLU   B OE1 
3477 O OE2 . GLU   B 132 ? 2.02541 1.18018 1.38791 0.39916  -0.61802 -0.15911 225 GLU   B OE2 
3478 N N   . ILE   B 133 ? 1.27576 0.67553 0.80722 0.26725  -0.45832 -0.08506 226 ILE   B N   
3479 C CA  . ILE   B 133 ? 1.29188 0.74502 0.86813 0.24666  -0.42454 -0.08240 226 ILE   B CA  
3480 C C   . ILE   B 133 ? 1.31511 0.85891 0.95604 0.23975  -0.39691 -0.08794 226 ILE   B C   
3481 O O   . ILE   B 133 ? 1.19022 0.79857 0.88460 0.24404  -0.38012 -0.10005 226 ILE   B O   
3482 C CB  . ILE   B 133 ? 1.26076 0.66561 0.79755 0.20708  -0.40729 -0.05644 226 ILE   B CB  
3483 C CG1 . ILE   B 133 ? 1.41532 0.73024 0.88896 0.21246  -0.43439 -0.05206 226 ILE   B CG1 
3484 C CG2 . ILE   B 133 ? 1.17326 0.63671 0.75808 0.18559  -0.37251 -0.05347 226 ILE   B CG2 
3485 C CD1 . ILE   B 133 ? 1.46227 0.72714 0.89388 0.17174  -0.41907 -0.02743 226 ILE   B CD1 
3486 N N   . LEU   B 134 ? 1.27429 0.82193 0.90869 0.22843  -0.39225 -0.07929 227 LEU   B N   
3487 C CA  . LEU   B 134 ? 1.12174 0.74953 0.81339 0.22130  -0.36798 -0.08439 227 LEU   B CA  
3488 C C   . LEU   B 134 ? 1.11852 0.80496 0.85790 0.25471  -0.38024 -0.11183 227 LEU   B C   
3489 O O   . LEU   B 134 ? 1.15618 0.91720 0.95244 0.25058  -0.35782 -0.12049 227 LEU   B O   
3490 C CB  . LEU   B 134 ? 1.23642 0.84935 0.90551 0.20366  -0.36343 -0.07042 227 LEU   B CB  
3491 C CG  . LEU   B 134 ? 1.33348 0.89684 0.95826 0.16787  -0.34789 -0.04442 227 LEU   B CG  
3492 C CD1 . LEU   B 134 ? 1.39236 0.95769 1.00578 0.15084  -0.33849 -0.03392 227 LEU   B CD1 
3493 C CD2 . LEU   B 134 ? 1.11342 0.70882 0.76805 0.14474  -0.31721 -0.03724 227 LEU   B CD2 
3494 N N   . THR   B 135 ? 1.13803 0.79232 0.85469 0.28754  -0.41587 -0.12637 228 THR   B N   
3495 C CA  . THR   B 135 ? 1.13138 0.84458 0.89548 0.32124  -0.42866 -0.15568 228 THR   B CA  
3496 C C   . THR   B 135 ? 1.16534 0.91330 0.96288 0.33015  -0.41951 -0.16904 228 THR   B C   
3497 O O   . THR   B 135 ? 1.16175 0.98779 1.01750 0.33866  -0.40675 -0.18752 228 THR   B O   
3498 C CB  . THR   B 135 ? 1.26534 0.93218 0.99463 0.35666  -0.47182 -0.16904 228 THR   B CB  
3499 O OG1 . THR   B 135 ? 1.38255 1.02039 1.08101 0.34823  -0.48002 -0.15725 228 THR   B OG1 
3500 C CG2 . THR   B 135 ? 1.14792 0.88180 0.93030 0.39302  -0.48545 -0.20246 228 THR   B CG2 
3501 N N   . MET   B 136 ? 1.22794 0.91856 0.98786 0.32625  -0.42495 -0.15978 229 MET   B N   
3502 C CA  . MET   B 136 ? 1.04740 0.76382 0.83289 0.33672  -0.41944 -0.17325 229 MET   B CA  
3503 C C   . MET   B 136 ? 1.02356 0.80051 0.85275 0.30794  -0.37933 -0.16559 229 MET   B C   
3504 O O   . MET   B 136 ? 1.02575 0.86186 0.89963 0.31791  -0.36860 -0.18282 229 MET   B O   
3505 C CB  . MET   B 136 ? 1.15944 0.79209 0.88859 0.33932  -0.43813 -0.16502 229 MET   B CB  
3506 C CG  . MET   B 136 ? 1.17283 0.82177 0.92068 0.35702  -0.44021 -0.18239 229 MET   B CG  
3507 S SD  . MET   B 136 ? 1.47659 1.15861 1.25135 0.41088  -0.47173 -0.22130 229 MET   B SD  
3508 C CE  . MET   B 136 ? 0.99498 0.79902 0.85460 0.40692  -0.43685 -0.23884 229 MET   B CE  
3509 N N   . GLU   B 137 ? 0.97952 0.74269 0.79544 0.27255  -0.35717 -0.14056 230 GLU   B N   
3510 C CA  . GLU   B 137 ? 0.92497 0.73988 0.77869 0.24630  -0.32144 -0.13271 230 GLU   B CA  
3511 C C   . GLU   B 137 ? 0.96035 0.85901 0.87237 0.24983  -0.30570 -0.14682 230 GLU   B C   
3512 O O   . GLU   B 137 ? 0.84917 0.79981 0.79937 0.24154  -0.28319 -0.15108 230 GLU   B O   
3513 C CB  . GLU   B 137 ? 0.95398 0.73811 0.78216 0.21006  -0.30290 -0.10517 230 GLU   B CB  
3514 C CG  . GLU   B 137 ? 1.08562 0.87500 0.91092 0.20011  -0.29959 -0.09729 230 GLU   B CG  
3515 C CD  . GLU   B 137 ? 1.10292 0.89804 0.92914 0.16407  -0.27051 -0.07601 230 GLU   B CD  
3516 O OE1 . GLU   B 137 ? 0.99695 0.79801 0.83097 0.14747  -0.25261 -0.06828 230 GLU   B OE1 
3517 O OE2 . GLU   B 137 ? 1.18451 0.97912 1.00400 0.15337  -0.26628 -0.06816 230 GLU   B OE2 
3518 N N   . LEU   B 138 ? 0.91702 0.82850 0.83482 0.26104  -0.31763 -0.15426 231 LEU   B N   
3519 C CA  . LEU   B 138 ? 0.96690 0.95762 0.93960 0.26358  -0.30419 -0.16916 231 LEU   B CA  
3520 C C   . LEU   B 138 ? 0.88897 0.92675 0.89679 0.29216  -0.31301 -0.19762 231 LEU   B C   
3521 O O   . LEU   B 138 ? 0.83600 0.94203 0.89076 0.28636  -0.29177 -0.20771 231 LEU   B O   
3522 C CB  . LEU   B 138 ? 0.94877 0.93919 0.91696 0.26729  -0.31597 -0.17009 231 LEU   B CB  
3523 C CG  . LEU   B 138 ? 1.05268 1.03070 1.00817 0.23532  -0.29663 -0.14669 231 LEU   B CG  
3524 C CD1 . LEU   B 138 ? 1.01071 0.97419 0.95015 0.24247  -0.31423 -0.14798 231 LEU   B CD1 
3525 C CD2 . LEU   B 138 ? 0.90235 0.94550 0.90527 0.21371  -0.26353 -0.14512 231 LEU   B CD2 
3526 N N   . MET   B 139 ? 0.91767 0.91906 0.90178 0.32305  -0.34435 -0.21142 232 MET   B N   
3527 C CA  . MET   B 139 ? 0.89696 0.94279 0.91357 0.35274  -0.35381 -0.24085 232 MET   B CA  
3528 C C   . MET   B 139 ? 0.78932 0.85079 0.81800 0.34352  -0.33398 -0.24036 232 MET   B C   
3529 O O   . MET   B 139 ? 0.80545 0.93253 0.87756 0.35242  -0.32309 -0.26068 232 MET   B O   
3530 C CB  . MET   B 139 ? 0.93071 0.92614 0.91438 0.38977  -0.39454 -0.25552 232 MET   B CB  
3531 C CG  . MET   B 139 ? 0.96366 0.95495 0.94212 0.40590  -0.41781 -0.26278 232 MET   B CG  
3532 S SD  . MET   B 139 ? 1.68454 1.61158 1.61993 0.44295  -0.45799 -0.28086 232 MET   B SD  
3533 C CE  . MET   B 139 ? 1.02840 0.84212 0.88576 0.43185  -0.47429 -0.24968 232 MET   B CE  
3534 N N   . ILE   B 140 ? 0.95808 0.96152 0.94849 0.32458  -0.32868 -0.21785 233 ILE   B N   
3535 C CA  . ILE   B 140 ? 0.76129 0.77639 0.76055 0.31433  -0.31054 -0.21606 233 ILE   B CA  
3536 C C   . ILE   B 140 ? 0.78620 0.86794 0.82830 0.28831  -0.27497 -0.21074 233 ILE   B C   
3537 O O   . ILE   B 140 ? 0.79584 0.92930 0.87069 0.29174  -0.26132 -0.22487 233 ILE   B O   
3538 C CB  . ILE   B 140 ? 0.89751 0.83526 0.84602 0.29780  -0.31379 -0.19299 233 ILE   B CB  
3539 C CG1 . ILE   B 140 ? 0.97032 0.83963 0.87429 0.32493  -0.34988 -0.20068 233 ILE   B CG1 
3540 C CG2 . ILE   B 140 ? 0.87567 0.83055 0.83636 0.28128  -0.29120 -0.18803 233 ILE   B CG2 
3541 C CD1 . ILE   B 140 ? 1.05659 0.84633 0.90729 0.30672  -0.35442 -0.17852 233 ILE   B CD1 
3542 N N   . MET   B 141 ? 0.84190 0.92158 0.88207 0.26207  -0.25993 -0.19071 234 MET   B N   
3543 C CA  . MET   B 141 ? 0.79933 0.93149 0.87345 0.23603  -0.22759 -0.18306 234 MET   B CA  
3544 C C   . MET   B 141 ? 0.76354 0.97169 0.88603 0.24489  -0.22015 -0.20449 234 MET   B C   
3545 O O   . MET   B 141 ? 0.71510 0.97289 0.86793 0.23249  -0.19699 -0.20765 234 MET   B O   
3546 C CB  . MET   B 141 ? 0.69836 0.80704 0.75699 0.20846  -0.21569 -0.15832 234 MET   B CB  
3547 C CG  . MET   B 141 ? 0.78265 0.82813 0.79981 0.19231  -0.21542 -0.13647 234 MET   B CG  
3548 S SD  . MET   B 141 ? 0.89034 0.91791 0.89411 0.15938  -0.19788 -0.11010 234 MET   B SD  
3549 C CE  . MET   B 141 ? 0.74297 0.75068 0.72966 0.17326  -0.22014 -0.11442 234 MET   B CE  
3550 N N   . LYS   B 142 ? 0.64655 0.86478 0.77580 0.26537  -0.23981 -0.21968 235 LYS   B N   
3551 C CA  . LYS   B 142 ? 0.69877 0.99295 0.87609 0.27316  -0.23352 -0.24223 235 LYS   B CA  
3552 C C   . LYS   B 142 ? 0.70102 1.03459 0.90166 0.29462  -0.23571 -0.26773 235 LYS   B C   
3553 O O   . LYS   B 142 ? 0.74384 1.14507 0.98449 0.28765  -0.21591 -0.28043 235 LYS   B O   
3554 C CB  . LYS   B 142 ? 0.67626 0.97137 0.85505 0.29027  -0.25598 -0.25291 235 LYS   B CB  
3555 C CG  . LYS   B 142 ? 0.72011 0.99582 0.88629 0.26721  -0.24910 -0.23198 235 LYS   B CG  
3556 C CD  . LYS   B 142 ? 0.76534 1.05069 0.93737 0.28457  -0.27091 -0.24544 235 LYS   B CD  
3557 C CE  . LYS   B 142 ? 0.82260 1.05364 0.95886 0.31643  -0.30738 -0.25343 235 LYS   B CE  
3558 N NZ  . LYS   B 142 ? 0.79185 1.03049 0.93187 0.33468  -0.33092 -0.26671 235 LYS   B NZ  
3559 N N   . ALA   B 143 ? 0.68286 0.97389 0.85712 0.32017  -0.25952 -0.27598 236 ALA   B N   
3560 C CA  . ALA   B 143 ? 0.74380 1.06979 0.93800 0.34272  -0.26262 -0.30176 236 ALA   B CA  
3561 C C   . ALA   B 143 ? 0.75791 1.10062 0.95862 0.32166  -0.23513 -0.29346 236 ALA   B C   
3562 O O   . ALA   B 143 ? 0.79299 1.19184 1.02409 0.32907  -0.22456 -0.31403 236 ALA   B O   
3563 C CB  . ALA   B 143 ? 0.79845 1.06628 0.95784 0.37561  -0.29679 -0.31175 236 ALA   B CB  
3564 N N   . LEU   B 144 ? 0.77149 1.06809 0.94402 0.29553  -0.22346 -0.26459 237 LEU   B N   
3565 C CA  . LEU   B 144 ? 0.69744 1.00596 0.87362 0.27443  -0.19868 -0.25462 237 LEU   B CA  
3566 C C   . LEU   B 144 ? 0.66600 1.02832 0.87315 0.24630  -0.16852 -0.24695 237 LEU   B C   
3567 O O   . LEU   B 144 ? 0.76778 1.13415 0.97399 0.22537  -0.14779 -0.23436 237 LEU   B O   
3568 C CB  . LEU   B 144 ? 0.69866 0.93564 0.83228 0.25946  -0.20082 -0.22871 237 LEU   B CB  
3569 C CG  . LEU   B 144 ? 0.85844 1.03426 0.95510 0.28211  -0.22837 -0.23361 237 LEU   B CG  
3570 C CD1 . LEU   B 144 ? 0.64723 0.75791 0.70438 0.26099  -0.22685 -0.20703 237 LEU   B CD1 
3571 C CD2 . LEU   B 144 ? 0.74142 0.94439 0.85128 0.30384  -0.23156 -0.25795 237 LEU   B CD2 
3572 N N   . LYS   B 145 ? 0.66688 1.06776 0.89942 0.24538  -0.16700 -0.25436 238 LYS   B N   
3573 C CA  . LYS   B 145 ? 0.57465 1.02177 0.83383 0.21789  -0.14038 -0.24705 238 LYS   B CA  
3574 C C   . LYS   B 145 ? 0.64323 1.05123 0.88043 0.18873  -0.12596 -0.21595 238 LYS   B C   
3575 O O   . LYS   B 145 ? 0.63277 1.06719 0.88341 0.16481  -0.10208 -0.20674 238 LYS   B O   
3576 C CB  . LYS   B 145 ? 0.76618 1.27521 1.05497 0.21344  -0.12027 -0.26261 238 LYS   B CB  
3577 C CG  . LYS   B 145 ? 0.67779 1.23969 0.99591 0.24032  -0.13060 -0.29657 238 LYS   B CG  
3578 C CD  . LYS   B 145 ? 0.82980 1.43206 1.17615 0.24119  -0.13394 -0.30770 238 LYS   B CD  
3579 C CE  . LYS   B 145 ? 0.85756 1.51022 1.22926 0.26263  -0.14074 -0.34062 238 LYS   B CE  
3580 N NZ  . LYS   B 145 ? 0.91182 1.59194 1.30058 0.25616  -0.14096 -0.34823 238 LYS   B NZ  
3581 N N   . TRP   B 146 ? 0.59237 0.93679 0.79449 0.19065  -0.14086 -0.20038 239 TRP   B N   
3582 C CA  . TRP   B 146 ? 0.62259 0.92776 0.80246 0.16559  -0.12969 -0.17279 239 TRP   B CA  
3583 C C   . TRP   B 146 ? 0.68978 0.99604 0.86744 0.15086  -0.11212 -0.16370 239 TRP   B C   
3584 O O   . TRP   B 146 ? 0.65605 0.95155 0.82827 0.12754  -0.09673 -0.14415 239 TRP   B O   
3585 C CB  . TRP   B 146 ? 0.62571 0.94935 0.81913 0.14603  -0.11686 -0.16275 239 TRP   B CB  
3586 C CG  . TRP   B 146 ? 0.66801 0.98601 0.85999 0.15869  -0.13476 -0.16968 239 TRP   B CG  
3587 C CD1 . TRP   B 146 ? 0.63801 1.00076 0.85753 0.17327  -0.14195 -0.19120 239 TRP   B CD1 
3588 C CD2 . TRP   B 146 ? 0.67666 0.94198 0.83709 0.15754  -0.14814 -0.15573 239 TRP   B CD2 
3589 N NE1 . TRP   B 146 ? 0.61937 0.95905 0.82623 0.18265  -0.16056 -0.19137 239 TRP   B NE1 
3590 C CE2 . TRP   B 146 ? 0.57802 0.85637 0.74671 0.17286  -0.16433 -0.16923 239 TRP   B CE2 
3591 C CE3 . TRP   B 146 ? 0.64229 0.85251 0.76811 0.14413  -0.14761 -0.13386 239 TRP   B CE3 
3592 C CZ2 . TRP   B 146 ? 0.60492 0.83924 0.74488 0.17548  -0.18040 -0.16049 239 TRP   B CZ2 
3593 C CZ3 . TRP   B 146 ? 0.72037 0.88924 0.81854 0.14519  -0.16174 -0.12552 239 TRP   B CZ3 
3594 C CH2 . TRP   B 146 ? 0.74940 0.92853 0.85298 0.16093  -0.17820 -0.13826 239 TRP   B CH2 
3595 N N   . ARG   B 147 ? 0.63478 0.95405 0.81616 0.16528  -0.11508 -0.17864 240 ARG   B N   
3596 C CA  . ARG   B 147 ? 0.57993 0.89467 0.75441 0.15429  -0.10218 -0.17133 240 ARG   B CA  
3597 C C   . ARG   B 147 ? 0.55862 0.80902 0.69674 0.15641  -0.11634 -0.15905 240 ARG   B C   
3598 O O   . ARG   B 147 ? 0.65152 0.88061 0.77527 0.17559  -0.13238 -0.17026 240 ARG   B O   
3599 C CB  . ARG   B 147 ? 0.69327 1.05039 0.88578 0.16832  -0.09883 -0.19375 240 ARG   B CB  
3600 C CG  . ARG   B 147 ? 0.59867 1.02239 0.82599 0.15962  -0.08000 -0.20455 240 ARG   B CG  
3601 C CD  . ARG   B 147 ? 0.78511 1.21534 1.01444 0.12878  -0.05662 -0.18402 240 ARG   B CD  
3602 N NE  . ARG   B 147 ? 1.00464 1.49359 1.26015 0.11809  -0.03700 -0.19416 240 ARG   B NE  
3603 C CZ  . ARG   B 147 ? 1.01063 1.53907 1.29049 0.11253  -0.03092 -0.20177 240 ARG   B CZ  
3604 N NH1 . ARG   B 147 ? 1.07666 1.59399 1.35931 0.11857  -0.04365 -0.20122 240 ARG   B NH1 
3605 N NH2 . ARG   B 147 ? 1.01076 1.59038 1.31097 0.09937  -0.01165 -0.21025 240 ARG   B NH2 
3606 N N   . LEU   B 148 ? 0.57383 0.79299 0.69651 0.13577  -0.11027 -0.13649 241 LEU   B N   
3607 C CA  . LEU   B 148 ? 0.64224 0.80070 0.72997 0.13314  -0.12257 -0.12353 241 LEU   B CA  
3608 C C   . LEU   B 148 ? 0.68358 0.83037 0.76408 0.11188  -0.10825 -0.10736 241 LEU   B C   
3609 O O   . LEU   B 148 ? 0.78995 0.89419 0.84662 0.10030  -0.11188 -0.09230 241 LEU   B O   
3610 C CB  . LEU   B 148 ? 0.68676 0.81422 0.75836 0.12856  -0.13108 -0.11263 241 LEU   B CB  
3611 C CG  . LEU   B 148 ? 0.69576 0.83114 0.77223 0.14977  -0.14787 -0.12770 241 LEU   B CG  
3612 C CD1 . LEU   B 148 ? 0.68517 0.79228 0.74488 0.14121  -0.15295 -0.11478 241 LEU   B CD1 
3613 C CD2 . LEU   B 148 ? 0.70611 0.81420 0.76447 0.17659  -0.17230 -0.14309 241 LEU   B CD2 
3614 N N   . SER   B 149 ? 0.67594 0.85987 0.77549 0.10607  -0.09241 -0.11069 242 SER   B N   
3615 C CA  . SER   B 149 ? 0.57341 0.74955 0.66757 0.08778  -0.08014 -0.09692 242 SER   B CA  
3616 C C   . SER   B 149 ? 0.71988 0.90729 0.81421 0.09599  -0.07964 -0.10803 242 SER   B C   
3617 O O   . SER   B 149 ? 0.80550 1.02587 0.91420 0.08772  -0.06398 -0.10833 242 SER   B O   
3618 C CB  . SER   B 149 ? 0.65548 0.86122 0.76842 0.06846  -0.05997 -0.08595 242 SER   B CB  
3619 O OG  . SER   B 149 ? 0.84346 1.03978 0.95607 0.06178  -0.06043 -0.07726 242 SER   B OG  
3620 N N   . PRO   B 150 ? 0.82534 0.98287 0.90080 0.11198  -0.09713 -0.11724 243 PRO   B N   
3621 C CA  . PRO   B 150 ? 0.64698 0.81213 0.71999 0.12062  -0.09771 -0.12878 243 PRO   B CA  
3622 C C   . PRO   B 150 ? 0.76858 0.90455 0.82424 0.10499  -0.09533 -0.11492 243 PRO   B C   
3623 O O   . PRO   B 150 ? 0.75861 0.86385 0.80192 0.08995  -0.09638 -0.09838 243 PRO   B O   
3624 C CB  . PRO   B 150 ? 0.77663 0.91762 0.83541 0.14670  -0.12063 -0.14575 243 PRO   B CB  
3625 C CG  . PRO   B 150 ? 0.68918 0.78135 0.72584 0.14252  -0.13390 -0.13287 243 PRO   B CG  
3626 C CD  . PRO   B 150 ? 0.72520 0.83674 0.77713 0.12355  -0.11862 -0.11806 243 PRO   B CD  
3627 N N   . LEU   B 151 ? 0.68876 0.83735 0.74413 0.10853  -0.09188 -0.12313 244 LEU   B N   
3628 C CA  . LEU   B 151 ? 0.77652 0.89816 0.81495 0.09725  -0.09294 -0.11407 244 LEU   B CA  
3629 C C   . LEU   B 151 ? 0.80468 0.88321 0.81796 0.11234  -0.11429 -0.12358 244 LEU   B C   
3630 O O   . LEU   B 151 ? 0.94972 1.03638 0.96092 0.13039  -0.12051 -0.14150 244 LEU   B O   
3631 C CB  . LEU   B 151 ? 0.56572 0.72077 0.61362 0.09210  -0.07862 -0.11707 244 LEU   B CB  
3632 C CG  . LEU   B 151 ? 0.71488 0.90724 0.78295 0.07650  -0.05854 -0.10728 244 LEU   B CG  
3633 C CD1 . LEU   B 151 ? 0.62491 0.84140 0.69430 0.07087  -0.04671 -0.10923 244 LEU   B CD1 
3634 C CD2 . LEU   B 151 ? 0.68622 0.85954 0.75347 0.05787  -0.05523 -0.08688 244 LEU   B CD2 
3635 N N   . THR   B 152 ? 0.71691 0.74825 0.70927 0.10440  -0.12553 -0.11202 245 THR   B N   
3636 C CA  . THR   B 152 ? 0.81992 0.80139 0.78321 0.11707  -0.14779 -0.11926 245 THR   B CA  
3637 C C   . THR   B 152 ? 0.80617 0.77298 0.75617 0.11553  -0.15141 -0.12338 245 THR   B C   
3638 O O   . THR   B 152 ? 0.79728 0.79047 0.75927 0.10337  -0.13710 -0.11892 245 THR   B O   
3639 C CB  . THR   B 152 ? 0.76926 0.70237 0.70994 0.10380  -0.15682 -0.10373 245 THR   B CB  
3640 O OG1 . THR   B 152 ? 0.76032 0.68792 0.70004 0.07706  -0.14575 -0.08663 245 THR   B OG1 
3641 C CG2 . THR   B 152 ? 0.76715 0.71363 0.71890 0.10540  -0.15379 -0.09982 245 THR   B CG2 
3642 N N   . ILE   B 153 ? 0.74996 0.67093 0.67244 0.12868  -0.17244 -0.13236 246 ILE   B N   
3643 C CA  . ILE   B 153 ? 0.79173 0.69117 0.69742 0.12720  -0.17886 -0.13687 246 ILE   B CA  
3644 C C   . ILE   B 153 ? 0.87462 0.75580 0.77326 0.09749  -0.17243 -0.11726 246 ILE   B C   
3645 O O   . ILE   B 153 ? 0.79248 0.68640 0.69496 0.08850  -0.16564 -0.11651 246 ILE   B O   
3646 C CB  . ILE   B 153 ? 0.81806 0.66507 0.69236 0.14742  -0.20496 -0.15032 246 ILE   B CB  
3647 C CG1 . ILE   B 153 ? 0.90792 0.77929 0.79333 0.17964  -0.21200 -0.17277 246 ILE   B CG1 
3648 C CG2 . ILE   B 153 ? 1.00459 0.82682 0.86001 0.14526  -0.21243 -0.15561 246 ILE   B CG2 
3649 C CD1 . ILE   B 153 ? 0.94185 0.76065 0.79632 0.20389  -0.24016 -0.18790 246 ILE   B CD1 
3650 N N   . VAL   B 154 ? 0.79465 0.64796 0.68317 0.08179  -0.17439 -0.10200 247 VAL   B N   
3651 C CA  . VAL   B 154 ? 0.79844 0.63653 0.68141 0.05322  -0.16858 -0.08536 247 VAL   B CA  
3652 C C   . VAL   B 154 ? 0.70706 0.59636 0.62173 0.03873  -0.14623 -0.07580 247 VAL   B C   
3653 O O   . VAL   B 154 ? 0.80669 0.69872 0.72443 0.01998  -0.14025 -0.06746 247 VAL   B O   
3654 C CB  . VAL   B 154 ? 0.86318 0.65546 0.72268 0.03990  -0.17689 -0.07316 247 VAL   B CB  
3655 C CG1 . VAL   B 154 ? 0.80387 0.62020 0.68009 0.03839  -0.16619 -0.06553 247 VAL   B CG1 
3656 C CG2 . VAL   B 154 ? 0.80946 0.58054 0.65849 0.01060  -0.17409 -0.05997 247 VAL   B CG2 
3657 N N   . SER   B 155 ? 0.68363 0.61324 0.62172 0.04720  -0.13470 -0.07753 248 SER   B N   
3658 C CA  . SER   B 155 ? 0.69509 0.66863 0.65982 0.03467  -0.11504 -0.06888 248 SER   B CA  
3659 C C   . SER   B 155 ? 0.78028 0.77605 0.75121 0.03600  -0.11003 -0.07476 248 SER   B C   
3660 O O   . SER   B 155 ? 0.69381 0.70577 0.67515 0.02074  -0.10014 -0.06541 248 SER   B O   
3661 C CB  . SER   B 155 ? 0.70786 0.71628 0.69328 0.04305  -0.10501 -0.07062 248 SER   B CB  
3662 O OG  . SER   B 155 ? 0.81697 0.84666 0.80795 0.06418  -0.10702 -0.08760 248 SER   B OG  
3663 N N   . TRP   B 156 ? 0.71973 0.71643 0.68338 0.05501  -0.11745 -0.09110 249 TRP   B N   
3664 C CA  . TRP   B 156 ? 0.70032 0.71489 0.66500 0.05645  -0.11349 -0.09755 249 TRP   B CA  
3665 C C   . TRP   B 156 ? 0.74386 0.72798 0.69259 0.04286  -0.12182 -0.09219 249 TRP   B C   
3666 O O   . TRP   B 156 ? 0.65528 0.65636 0.60990 0.03321  -0.11497 -0.08825 249 TRP   B O   
3667 C CB  . TRP   B 156 ? 0.67836 0.70067 0.63760 0.08049  -0.11974 -0.11833 249 TRP   B CB  
3668 C CG  . TRP   B 156 ? 0.67196 0.73933 0.65225 0.09102  -0.10732 -0.12581 249 TRP   B CG  
3669 C CD1 . TRP   B 156 ? 0.69705 0.77056 0.68295 0.10797  -0.11217 -0.13659 249 TRP   B CD1 
3670 C CD2 . TRP   B 156 ? 0.66613 0.77834 0.66375 0.08409  -0.08854 -0.12341 249 TRP   B CD2 
3671 N NE1 . TRP   B 156 ? 0.75547 0.87873 0.76391 0.11081  -0.09648 -0.14182 249 TRP   B NE1 
3672 C CE2 . TRP   B 156 ? 0.70225 0.84781 0.71634 0.09537  -0.08145 -0.13319 249 TRP   B CE2 
3673 C CE3 . TRP   B 156 ? 0.75810 0.88381 0.75720 0.06925  -0.07808 -0.11409 249 TRP   B CE3 
3674 C CZ2 . TRP   B 156 ? 0.78757 0.97802 0.81807 0.08965  -0.06300 -0.13322 249 TRP   B CZ2 
3675 C CZ3 . TRP   B 156 ? 0.77612 0.94241 0.78869 0.06535  -0.06114 -0.11345 249 TRP   B CZ3 
3676 C CH2 . TRP   B 156 ? 0.78658 0.98418 0.81400 0.07422  -0.05308 -0.12260 249 TRP   B CH2 
3677 N N   . LEU   B 157 ? 0.72904 0.66684 0.65608 0.04124  -0.13743 -0.09212 250 LEU   B N   
3678 C CA  . LEU   B 157 ? 0.79626 0.70454 0.70826 0.02511  -0.14541 -0.08714 250 LEU   B CA  
3679 C C   . LEU   B 157 ? 0.74447 0.66957 0.67290 0.00101  -0.13351 -0.07085 250 LEU   B C   
3680 O O   . LEU   B 157 ? 0.79265 0.72000 0.72195 -0.01123 -0.13372 -0.06838 250 LEU   B O   
3681 C CB  . LEU   B 157 ? 0.75546 0.60736 0.63837 0.02481  -0.16370 -0.08842 250 LEU   B CB  
3682 C CG  . LEU   B 157 ? 0.81544 0.63241 0.68044 0.00446  -0.17261 -0.08315 250 LEU   B CG  
3683 C CD1 . LEU   B 157 ? 0.77908 0.60322 0.64129 0.00911  -0.17636 -0.09341 250 LEU   B CD1 
3684 C CD2 . LEU   B 157 ? 1.00384 0.75981 0.83503 0.00360  -0.19101 -0.08385 250 LEU   B CD2 
3685 N N   . ASN   B 158 ? 0.80507 0.74333 0.74724 -0.00502 -0.12380 -0.06092 251 ASN   B N   
3686 C CA  . ASN   B 158 ? 0.89664 0.85495 0.85676 -0.02514 -0.11199 -0.04748 251 ASN   B CA  
3687 C C   . ASN   B 158 ? 0.84716 0.84558 0.82640 -0.02390 -0.10130 -0.04748 251 ASN   B C   
3688 O O   . ASN   B 158 ? 0.90915 0.91795 0.89744 -0.03791 -0.09813 -0.04122 251 ASN   B O   
3689 C CB  . ASN   B 158 ? 0.75268 0.71714 0.72209 -0.02903 -0.10390 -0.03878 251 ASN   B CB  
3690 C CG  . ASN   B 158 ? 1.01401 0.99070 0.99758 -0.05051 -0.09425 -0.02628 251 ASN   B CG  
3691 O OD1 . ASN   B 158 ? 1.00374 0.96930 0.98319 -0.06603 -0.09779 -0.02353 251 ASN   B OD1 
3692 N ND2 . ASN   B 158 ? 1.04602 1.04732 1.04726 -0.05143 -0.08217 -0.01995 251 ASN   B ND2 
3693 N N   . VAL   B 159 ? 0.91238 0.93358 0.89688 -0.00754 -0.09613 -0.05502 252 VAL   B N   
3694 C CA  . VAL   B 159 ? 0.63027 0.68428 0.62623 -0.00692 -0.08659 -0.05480 252 VAL   B CA  
3695 C C   . VAL   B 159 ? 0.84630 0.89091 0.82950 -0.00742 -0.09512 -0.06089 252 VAL   B C   
3696 O O   . VAL   B 159 ? 0.97340 1.03163 0.96294 -0.01631 -0.09215 -0.05567 252 VAL   B O   
3697 C CB  . VAL   B 159 ? 0.78663 0.86679 0.78857 0.00807  -0.07810 -0.06226 252 VAL   B CB  
3698 C CG1 . VAL   B 159 ? 1.02412 1.13402 1.03305 0.00555  -0.06747 -0.05996 252 VAL   B CG1 
3699 C CG2 . VAL   B 159 ? 0.70081 0.78881 0.71490 0.00875  -0.07159 -0.05752 252 VAL   B CG2 
3700 N N   . TYR   B 160 ? 0.75887 0.77866 0.72290 0.00319  -0.10725 -0.07282 253 TYR   B N   
3701 C CA  . TYR   B 160 ? 0.83276 0.84257 0.78251 0.00436  -0.11608 -0.08059 253 TYR   B CA  
3702 C C   . TYR   B 160 ? 0.94893 0.94195 0.89728 -0.01478 -0.12293 -0.07297 253 TYR   B C   
3703 O O   . TYR   B 160 ? 0.83057 0.82887 0.77615 -0.01876 -0.12623 -0.07496 253 TYR   B O   
3704 C CB  . TYR   B 160 ? 0.92601 0.90938 0.85457 0.02103  -0.12892 -0.09624 253 TYR   B CB  
3705 C CG  . TYR   B 160 ? 0.84125 0.84634 0.77326 0.04149  -0.12299 -0.10777 253 TYR   B CG  
3706 C CD1 . TYR   B 160 ? 0.82458 0.87141 0.77400 0.04219  -0.10634 -0.10475 253 TYR   B CD1 
3707 C CD2 . TYR   B 160 ? 0.77974 0.76359 0.69727 0.05990  -0.13466 -0.12266 253 TYR   B CD2 
3708 C CE1 . TYR   B 160 ? 0.77929 0.85021 0.73372 0.05836  -0.09980 -0.11643 253 TYR   B CE1 
3709 C CE2 . TYR   B 160 ? 0.71503 0.72452 0.63934 0.07913  -0.12929 -0.13564 253 TYR   B CE2 
3710 C CZ  . TYR   B 160 ? 0.74514 0.80023 0.68896 0.07714  -0.11100 -0.13258 253 TYR   B CZ  
3711 O OH  . TYR   B 160 ? 0.75009 0.83489 0.70246 0.09382  -0.10449 -0.14655 253 TYR   B OH  
3712 N N   . MET   B 161 ? 0.92035 0.89461 0.87022 -0.02755 -0.12503 -0.06489 254 MET   B N   
3713 C CA  . MET   B 161 ? 0.88572 0.84824 0.83632 -0.04819 -0.13017 -0.05892 254 MET   B CA  
3714 C C   . MET   B 161 ? 0.92742 0.92580 0.90284 -0.05892 -0.11962 -0.04991 254 MET   B C   
3715 O O   . MET   B 161 ? 1.00993 1.01162 0.98942 -0.07092 -0.12432 -0.04935 254 MET   B O   
3716 C CB  . MET   B 161 ? 0.88967 0.82083 0.83116 -0.06056 -0.13442 -0.05335 254 MET   B CB  
3717 C CG  . MET   B 161 ? 0.82707 0.71163 0.73818 -0.05299 -0.15009 -0.06208 254 MET   B CG  
3718 S SD  . MET   B 161 ? 1.06488 0.92786 0.95774 -0.05559 -0.16518 -0.07254 254 MET   B SD  
3719 C CE  . MET   B 161 ? 1.07506 0.94690 0.98233 -0.08732 -0.16238 -0.06218 254 MET   B CE  
3720 N N   . GLN   B 162 ? 0.91584 0.94063 0.90784 -0.05430 -0.10664 -0.04372 255 GLN   B N   
3721 C CA  . GLN   B 162 ? 0.91238 0.96805 0.92599 -0.06179 -0.09819 -0.03592 255 GLN   B CA  
3722 C C   . GLN   B 162 ? 1.04310 1.11446 1.05455 -0.05478 -0.09999 -0.03988 255 GLN   B C   
3723 O O   . GLN   B 162 ? 0.91314 0.99669 0.93401 -0.06278 -0.10265 -0.03733 255 GLN   B O   
3724 C CB  . GLN   B 162 ? 0.84392 0.91868 0.87220 -0.05840 -0.08497 -0.02875 255 GLN   B CB  
3725 C CG  . GLN   B 162 ? 1.00578 1.10807 1.05525 -0.06506 -0.07736 -0.02087 255 GLN   B CG  
3726 C CD  . GLN   B 162 ? 0.94321 1.04606 1.00505 -0.08202 -0.07902 -0.01693 255 GLN   B CD  
3727 O OE1 . GLN   B 162 ? 0.99402 1.07638 1.04872 -0.09140 -0.08204 -0.01702 255 GLN   B OE1 
3728 N NE2 . GLN   B 162 ? 1.06376 1.19004 1.14320 -0.08625 -0.07736 -0.01406 255 GLN   B NE2 
3729 N N   . VAL   B 163 ? 0.83463 0.90686 0.83311 -0.03978 -0.09885 -0.04690 256 VAL   B N   
3730 C CA  . VAL   B 163 ? 1.03997 1.12504 1.03116 -0.03379 -0.09968 -0.05053 256 VAL   B CA  
3731 C C   . VAL   B 163 ? 0.96314 1.03216 0.94217 -0.03809 -0.11380 -0.05710 256 VAL   B C   
3732 O O   . VAL   B 163 ? 0.97704 1.05672 0.95497 -0.03955 -0.11715 -0.05678 256 VAL   B O   
3733 C CB  . VAL   B 163 ? 0.92329 1.01520 0.90273 -0.01844 -0.09352 -0.05819 256 VAL   B CB  
3734 C CG1 . VAL   B 163 ? 1.03407 1.13919 1.00235 -0.01438 -0.09240 -0.06076 256 VAL   B CG1 
3735 C CG2 . VAL   B 163 ? 0.83867 0.94683 0.83159 -0.01602 -0.08032 -0.05246 256 VAL   B CG2 
3736 N N   . ALA   B 164 ? 0.89759 0.93840 0.86542 -0.04047 -0.12349 -0.06315 257 ALA   B N   
3737 C CA  . ALA   B 164 ? 1.03064 1.05348 0.98619 -0.04658 -0.13769 -0.06980 257 ALA   B CA  
3738 C C   . ALA   B 164 ? 1.13679 1.17084 1.10984 -0.06411 -0.14051 -0.06312 257 ALA   B C   
3739 O O   . ALA   B 164 ? 0.99296 1.02598 0.96158 -0.06856 -0.15066 -0.06782 257 ALA   B O   
3740 C CB  . ALA   B 164 ? 0.92136 0.90631 0.85878 -0.04677 -0.14808 -0.07689 257 ALA   B CB  
3741 N N   . TYR   B 165 ? 0.91492 0.96184 0.90862 -0.07368 -0.13199 -0.05356 258 TYR   B N   
3742 C CA  . TYR   B 165 ? 0.99369 1.05724 1.00806 -0.08951 -0.13347 -0.04913 258 TYR   B CA  
3743 C C   . TYR   B 165 ? 1.10796 1.20389 1.14375 -0.08601 -0.12312 -0.04120 258 TYR   B C   
3744 O O   . TYR   B 165 ? 1.34832 1.45714 1.40388 -0.09515 -0.11616 -0.03508 258 TYR   B O   
3745 C CB  . TYR   B 165 ? 0.96375 1.01224 0.98247 -0.10730 -0.13365 -0.04653 258 TYR   B CB  
3746 C CG  . TYR   B 165 ? 1.14289 1.15660 1.13990 -0.11544 -0.14692 -0.05396 258 TYR   B CG  
3747 C CD1 . TYR   B 165 ? 1.03623 1.01519 1.00759 -0.10636 -0.15126 -0.05813 258 TYR   B CD1 
3748 C CD2 . TYR   B 165 ? 1.14546 1.16057 1.14742 -0.13175 -0.15629 -0.05783 258 TYR   B CD2 
3749 C CE1 . TYR   B 165 ? 1.16802 1.10981 1.11628 -0.11305 -0.16507 -0.06521 258 TYR   B CE1 
3750 C CE2 . TYR   B 165 ? 1.19835 1.17840 1.17836 -0.14085 -0.16907 -0.06463 258 TYR   B CE2 
3751 C CZ  . TYR   B 165 ? 1.10982 1.05089 1.06151 -0.13130 -0.17366 -0.06793 258 TYR   B CZ  
3752 O OH  . TYR   B 165 ? 1.24023 1.14121 1.16701 -0.13968 -0.18796 -0.07493 258 TYR   B OH  
3753 N N   . LEU   B 166 ? 1.01935 1.12649 1.04887 -0.07316 -0.12221 -0.04153 259 LEU   B N   
3754 C CA  . LEU   B 166 ? 1.16306 1.29493 1.20728 -0.06928 -0.11533 -0.03422 259 LEU   B CA  
3755 C C   . LEU   B 166 ? 1.23672 1.38203 1.28849 -0.07206 -0.12599 -0.03598 259 LEU   B C   
3756 O O   . LEU   B 166 ? 1.11552 1.25184 1.15305 -0.07121 -0.13732 -0.04300 259 LEU   B O   
3757 C CB  . LEU   B 166 ? 1.08549 1.21931 1.11491 -0.05548 -0.10754 -0.03250 259 LEU   B CB  
3758 C CG  . LEU   B 166 ? 1.12930 1.26086 1.15931 -0.05135 -0.09516 -0.02971 259 LEU   B CG  
3759 C CD1 . LEU   B 166 ? 1.09268 1.23006 1.10826 -0.04011 -0.08760 -0.03013 259 LEU   B CD1 
3760 C CD2 . LEU   B 166 ? 1.08134 1.22553 1.13423 -0.05790 -0.08708 -0.02114 259 LEU   B CD2 
3761 N N   . ASN   B 167 ? 1.53678 1.70367 1.61092 -0.07423 -0.12340 -0.03069 260 ASN   B N   
3762 C CA  . ASN   B 167 ? 1.71829 1.90148 1.80353 -0.07465 -0.13461 -0.03304 260 ASN   B CA  
3763 C C   . ASN   B 167 ? 1.93280 2.12234 2.01062 -0.06152 -0.13384 -0.02724 260 ASN   B C   
3764 O O   . ASN   B 167 ? 1.90655 2.08598 1.96569 -0.05398 -0.12532 -0.02289 260 ASN   B O   
3765 C CB  . ASN   B 167 ? 1.79255 1.99638 1.90966 -0.08687 -0.13411 -0.03393 260 ASN   B CB  
3766 C CG  . ASN   B 167 ? 1.87224 2.08675 2.00010 -0.09545 -0.14860 -0.04272 260 ASN   B CG  
3767 O OD1 . ASN   B 167 ? 1.92526 2.14261 2.06552 -0.11153 -0.14907 -0.04711 260 ASN   B OD1 
3768 N ND2 . ASN   B 167 ? 1.95520 2.17491 2.07674 -0.08584 -0.16087 -0.04544 260 ASN   B ND2 
3769 N N   . ASP   B 168 ? 2.36663 2.57254 2.45827 -0.05918 -0.14334 -0.02772 261 ASP   B N   
3770 C CA  . ASP   B 168 ? 2.37287 2.57938 2.45419 -0.04712 -0.14509 -0.02150 261 ASP   B CA  
3771 C C   . ASP   B 168 ? 2.21551 2.42677 2.30704 -0.04462 -0.13167 -0.01309 261 ASP   B C   
3772 O O   . ASP   B 168 ? 2.17654 2.37964 2.25125 -0.03643 -0.12906 -0.00619 261 ASP   B O   
3773 C CB  . ASP   B 168 ? 2.49576 2.71659 2.58879 -0.04313 -0.16205 -0.02563 261 ASP   B CB  
3774 C CG  . ASP   B 168 ? 2.42357 2.67113 2.55587 -0.04978 -0.16284 -0.03002 261 ASP   B CG  
3775 O OD1 . ASP   B 168 ? 2.37596 2.62798 2.52271 -0.06225 -0.15374 -0.03220 261 ASP   B OD1 
3776 O OD2 . ASP   B 168 ? 2.34840 2.61230 2.49595 -0.04240 -0.17286 -0.03190 261 ASP   B OD2 
3777 N N   . LEU   B 169 ? 2.06084 2.28336 2.17710 -0.05267 -0.12317 -0.01351 262 LEU   B N   
3778 C CA  . LEU   B 169 ? 2.01033 2.23714 2.13636 -0.05060 -0.11071 -0.00650 262 LEU   B CA  
3779 C C   . LEU   B 169 ? 1.92815 2.13860 2.03378 -0.04893 -0.09797 -0.00106 262 LEU   B C   
3780 O O   . LEU   B 169 ? 1.89848 2.10882 2.00450 -0.04539 -0.08915 0.00553  262 LEU   B O   
3781 C CB  . LEU   B 169 ? 1.96682 2.21057 2.12265 -0.06064 -0.10485 -0.00932 262 LEU   B CB  
3782 C CG  . LEU   B 169 ? 1.84014 2.08184 2.00024 -0.07447 -0.10520 -0.01536 262 LEU   B CG  
3783 C CD1 . LEU   B 169 ? 1.66967 1.91424 1.84270 -0.08415 -0.09218 -0.01319 262 LEU   B CD1 
3784 C CD2 . LEU   B 169 ? 1.72959 1.98910 1.90710 -0.08058 -0.11801 -0.02399 262 LEU   B CD2 
3785 N N   . HIS   B 170 ? 1.95340 2.15101 2.04208 -0.05103 -0.09749 -0.00492 263 HIS   B N   
3786 C CA  . HIS   B 170 ? 1.87584 2.06227 1.94712 -0.04813 -0.08650 -0.00286 263 HIS   B CA  
3787 C C   . HIS   B 170 ? 1.82834 2.01834 1.91408 -0.05150 -0.07411 0.00094  263 HIS   B C   
3788 O O   . HIS   B 170 ? 1.71058 1.89776 1.78789 -0.04805 -0.06420 0.00419  263 HIS   B O   
3789 C CB  . HIS   B 170 ? 1.82871 2.01057 1.87804 -0.04071 -0.08434 0.00183  263 HIS   B CB  
3790 C CG  . HIS   B 170 ? 1.87720 2.05082 1.90303 -0.03713 -0.09411 -0.00262 263 HIS   B CG  
3791 N ND1 . HIS   B 170 ? 1.89862 2.06793 1.92241 -0.03933 -0.10343 -0.01124 263 HIS   B ND1 
3792 C CD2 . HIS   B 170 ? 1.77957 1.94644 1.78011 -0.03238 -0.09616 0.00034  263 HIS   B CD2 
3793 C CE1 . HIS   B 170 ? 1.88086 2.04278 1.88056 -0.03490 -0.11096 -0.01412 263 HIS   B CE1 
3794 N NE2 . HIS   B 170 ? 1.79398 1.95434 1.77839 -0.03084 -0.10644 -0.00693 263 HIS   B NE2 
3795 N N   . GLU   B 171 ? 1.88873 2.08613 1.99580 -0.05922 -0.07433 -0.00002 264 GLU   B N   
3796 C CA  . GLU   B 171 ? 1.79469 1.99427 1.91360 -0.06324 -0.06337 0.00333  264 GLU   B CA  
3797 C C   . GLU   B 171 ? 1.63954 1.82334 1.74669 -0.06561 -0.06098 0.00003  264 GLU   B C   
3798 O O   . GLU   B 171 ? 1.58917 1.76511 1.69697 -0.07360 -0.06619 -0.00408 264 GLU   B O   
3799 C CB  . GLU   B 171 ? 1.74381 1.95821 1.88755 -0.07151 -0.06373 0.00273  264 GLU   B CB  
3800 C CG  . GLU   B 171 ? 1.74443 1.96238 1.89919 -0.07509 -0.05210 0.00663  264 GLU   B CG  
3801 C CD  . GLU   B 171 ? 1.83989 2.06118 1.99430 -0.06637 -0.04552 0.01248  264 GLU   B CD  
3802 O OE1 . GLU   B 171 ? 1.79512 2.02078 1.94827 -0.05944 -0.05080 0.01392  264 GLU   B OE1 
3803 O OE2 . GLU   B 171 ? 1.81917 2.03653 1.97265 -0.06677 -0.03605 0.01561  264 GLU   B OE2 
3804 N N   . VAL   B 172 ? 1.27617 1.45471 1.37183 -0.05876 -0.05379 0.00117  265 VAL   B N   
3805 C CA  . VAL   B 172 ? 1.17579 1.33952 1.25928 -0.05686 -0.05352 -0.00377 265 VAL   B CA  
3806 C C   . VAL   B 172 ? 1.04210 1.20156 1.13343 -0.06113 -0.04744 -0.00123 265 VAL   B C   
3807 O O   . VAL   B 172 ? 0.97677 1.12020 1.05749 -0.05941 -0.04968 -0.00535 265 VAL   B O   
3808 C CB  . VAL   B 172 ? 1.18297 1.34753 1.25113 -0.04649 -0.04947 -0.00675 265 VAL   B CB  
3809 C CG1 . VAL   B 172 ? 1.04150 1.21563 1.11614 -0.04424 -0.03775 -0.00225 265 VAL   B CG1 
3810 C CG2 . VAL   B 172 ? 1.12558 1.27510 1.17834 -0.04119 -0.05501 -0.01620 265 VAL   B CG2 
3811 N N   . LEU   B 173 ? 0.94451 1.11598 1.05220 -0.06576 -0.04091 0.00479  266 LEU   B N   
3812 C CA  . LEU   B 173 ? 0.91998 1.08734 1.03287 -0.07003 -0.03474 0.00738  266 LEU   B CA  
3813 C C   . LEU   B 173 ? 0.89201 1.05362 1.01043 -0.08315 -0.03737 0.00743  266 LEU   B C   
3814 O O   . LEU   B 173 ? 0.86477 1.01325 0.97786 -0.08797 -0.03523 0.00847  266 LEU   B O   
3815 C CB  . LEU   B 173 ? 0.96134 1.14370 1.08679 -0.06815 -0.02527 0.01301  266 LEU   B CB  
3816 C CG  . LEU   B 173 ? 0.93873 1.12553 1.05748 -0.05899 -0.02015 0.01374  266 LEU   B CG  
3817 C CD1 . LEU   B 173 ? 0.89847 1.09520 1.02809 -0.05939 -0.01156 0.01932  266 LEU   B CD1 
3818 C CD2 . LEU   B 173 ? 0.92062 1.09773 1.02731 -0.05345 -0.02030 0.00846  266 LEU   B CD2 
3819 N N   . LEU   B 174 ? 0.87872 1.05012 1.00677 -0.08988 -0.04214 0.00596  267 LEU   B N   
3820 C CA  . LEU   B 174 ? 0.85385 1.02362 0.98803 -0.10540 -0.04360 0.00482  267 LEU   B CA  
3821 C C   . LEU   B 174 ? 0.99694 1.14240 1.11243 -0.11047 -0.05343 0.00034  267 LEU   B C   
3822 O O   . LEU   B 174 ? 1.00688 1.15184 1.11752 -0.10611 -0.06174 -0.00395 267 LEU   B O   
3823 C CB  . LEU   B 174 ? 0.80384 0.99979 0.96033 -0.11039 -0.04466 0.00314  267 LEU   B CB  
3824 C CG  . LEU   B 174 ? 0.95459 1.16455 1.12800 -0.12586 -0.03887 0.00254  267 LEU   B CG  
3825 C CD1 . LEU   B 174 ? 1.16982 1.41238 1.36965 -0.12408 -0.03940 -0.00077 267 LEU   B CD1 
3826 C CD2 . LEU   B 174 ? 0.85953 1.05463 1.02368 -0.14322 -0.04344 -0.00052 267 LEU   B CD2 
3827 N N   . PRO   B 175 ? 0.92312 1.04519 1.02499 -0.11950 -0.05387 0.00109  268 PRO   B N   
3828 C CA  . PRO   B 175 ? 0.80849 0.90023 0.88781 -0.12267 -0.06496 -0.00335 268 PRO   B CA  
3829 C C   . PRO   B 175 ? 0.91536 1.01140 1.00021 -0.13726 -0.07167 -0.00712 268 PRO   B C   
3830 O O   . PRO   B 175 ? 0.90930 1.02224 1.01052 -0.15281 -0.06683 -0.00587 268 PRO   B O   
3831 C CB  . PRO   B 175 ? 0.98371 1.04765 1.04616 -0.13012 -0.06374 -0.00003 268 PRO   B CB  
3832 C CG  . PRO   B 175 ? 0.88161 0.96672 0.96201 -0.13960 -0.05158 0.00555  268 PRO   B CG  
3833 C CD  . PRO   B 175 ? 0.89593 1.01457 0.99887 -0.12700 -0.04521 0.00608  268 PRO   B CD  
3834 N N   . GLN   B 176 ? 0.78683 0.86946 0.85852 -0.13229 -0.08283 -0.01305 269 GLN   B N   
3835 C CA  . GLN   B 176 ? 0.95064 1.03574 1.02603 -0.14591 -0.09123 -0.01792 269 GLN   B CA  
3836 C C   . GLN   B 176 ? 0.92958 0.98301 0.97867 -0.14042 -0.10437 -0.02438 269 GLN   B C   
3837 O O   . GLN   B 176 ? 1.12009 1.17907 1.16560 -0.12527 -0.10888 -0.02863 269 GLN   B O   
3838 C CB  . GLN   B 176 ? 0.84133 0.96381 0.94170 -0.14211 -0.09078 -0.01960 269 GLN   B CB  
3839 C CG  . GLN   B 176 ? 1.06591 1.20004 1.17768 -0.15788 -0.09866 -0.02544 269 GLN   B CG  
3840 C CD  . GLN   B 176 ? 1.21181 1.32978 1.30682 -0.15324 -0.11278 -0.03234 269 GLN   B CD  
3841 O OE1 . GLN   B 176 ? 1.26811 1.38135 1.35142 -0.13497 -0.11570 -0.03333 269 GLN   B OE1 
3842 N NE2 . GLN   B 176 ? 0.99686 1.10666 1.08971 -0.17106 -0.12117 -0.03767 269 GLN   B NE2 
3843 N N   . TYR   B 177 ? 0.91368 0.93216 0.94209 -0.15302 -0.11056 -0.02525 270 TYR   B N   
3844 C CA  . TYR   B 177 ? 0.96645 0.94967 0.96788 -0.14955 -0.12481 -0.03245 270 TYR   B CA  
3845 C C   . TYR   B 177 ? 0.86116 0.80706 0.84253 -0.17120 -0.13102 -0.03146 270 TYR   B C   
3846 O O   . TYR   B 177 ? 1.01118 0.95208 0.99255 -0.18382 -0.12323 -0.02438 270 TYR   B O   
3847 C CB  . TYR   B 177 ? 0.97027 0.93701 0.95409 -0.12513 -0.12694 -0.03560 270 TYR   B CB  
3848 C CG  . TYR   B 177 ? 0.95685 0.91170 0.93477 -0.12028 -0.12033 -0.03002 270 TYR   B CG  
3849 C CD1 . TYR   B 177 ? 0.90168 0.81296 0.85335 -0.12644 -0.12791 -0.02947 270 TYR   B CD1 
3850 C CD2 . TYR   B 177 ? 0.84867 0.83297 0.84472 -0.10942 -0.10789 -0.02547 270 TYR   B CD2 
3851 C CE1 . TYR   B 177 ? 0.81443 0.71356 0.75885 -0.12091 -0.12373 -0.02471 270 TYR   B CE1 
3852 C CE2 . TYR   B 177 ? 0.95172 0.92612 0.94267 -0.10482 -0.10289 -0.02122 270 TYR   B CE2 
3853 C CZ  . TYR   B 177 ? 0.93417 0.86678 0.89960 -0.10997 -0.11110 -0.02099 270 TYR   B CZ  
3854 O OH  . TYR   B 177 ? 1.00620 0.92774 0.96482 -0.10444 -0.10788 -0.01704 270 TYR   B OH  
3855 N N   . PRO   B 178 ? 0.86535 0.78258 0.82697 -0.17731 -0.14499 -0.03825 271 PRO   B N   
3856 C CA  . PRO   B 178 ? 0.83148 0.70684 0.76892 -0.20021 -0.15191 -0.03679 271 PRO   B CA  
3857 C C   . PRO   B 178 ? 0.96381 0.79726 0.87271 -0.19288 -0.15378 -0.03253 271 PRO   B C   
3858 O O   . PRO   B 178 ? 0.88594 0.70253 0.78020 -0.16809 -0.16008 -0.03717 271 PRO   B O   
3859 C CB  . PRO   B 178 ? 0.77657 0.62748 0.69623 -0.20143 -0.16842 -0.04655 271 PRO   B CB  
3860 C CG  . PRO   B 178 ? 1.00034 0.89483 0.94529 -0.18865 -0.16715 -0.05184 271 PRO   B CG  
3861 C CD  . PRO   B 178 ? 0.93449 0.85735 0.89489 -0.16674 -0.15501 -0.04746 271 PRO   B CD  
3862 N N   . GLN   B 179 ? 0.87401 0.69170 0.77459 -0.21486 -0.14852 -0.02444 272 GLN   B N   
3863 C CA  . GLN   B 179 ? 0.92886 0.70510 0.80041 -0.20922 -0.15119 -0.01934 272 GLN   B CA  
3864 C C   . GLN   B 179 ? 0.91826 0.63005 0.74646 -0.20782 -0.17084 -0.02409 272 GLN   B C   
3865 O O   . GLN   B 179 ? 1.00631 0.68396 0.81031 -0.18902 -0.17881 -0.02489 272 GLN   B O   
3866 C CB  . GLN   B 179 ? 0.90056 0.67793 0.77255 -0.23474 -0.13935 -0.00894 272 GLN   B CB  
3867 C CG  . GLN   B 179 ? 1.04052 0.87913 0.95411 -0.23578 -0.12057 -0.00532 272 GLN   B CG  
3868 C CD  . GLN   B 179 ? 1.23084 1.07418 1.14563 -0.26424 -0.10832 0.00256  272 GLN   B CD  
3869 O OE1 . GLN   B 179 ? 1.31616 1.13599 1.21372 -0.29237 -0.11113 0.00378  272 GLN   B OE1 
3870 N NE2 . GLN   B 179 ? 1.15813 1.03173 1.09200 -0.25824 -0.09423 0.00748  272 GLN   B NE2 
3871 N N   . GLN   B 180 ? 0.94618 0.63999 0.76391 -0.22669 -0.18004 -0.02823 273 GLN   B N   
3872 C CA  . GLN   B 180 ? 1.12819 0.75387 0.90066 -0.22874 -0.19973 -0.03220 273 GLN   B CA  
3873 C C   . GLN   B 180 ? 1.00646 0.61901 0.76872 -0.19411 -0.21295 -0.04417 273 GLN   B C   
3874 O O   . GLN   B 180 ? 1.19981 0.75986 0.92672 -0.18015 -0.22753 -0.04752 273 GLN   B O   
3875 C CB  . GLN   B 180 ? 1.22387 0.83485 0.98844 -0.26095 -0.20563 -0.03383 273 GLN   B CB  
3876 C CG  . GLN   B 180 ? 1.27931 0.81118 0.99140 -0.27149 -0.22512 -0.03486 273 GLN   B CG  
3877 C CD  . GLN   B 180 ? 1.57669 1.09436 1.28070 -0.30946 -0.22899 -0.03517 273 GLN   B CD  
3878 O OE1 . GLN   B 180 ? 1.66479 1.11877 1.32575 -0.32957 -0.24080 -0.03212 273 GLN   B OE1 
3879 N NE2 . GLN   B 180 ? 1.57742 1.15344 1.32182 -0.31985 -0.21995 -0.03923 273 GLN   B NE2 
3880 N N   . ILE   B 181 ? 1.09344 0.75252 0.88467 -0.17941 -0.20860 -0.05149 274 ILE   B N   
3881 C CA  . ILE   B 181 ? 1.02727 0.67961 0.80966 -0.14727 -0.21857 -0.06383 274 ILE   B CA  
3882 C C   . ILE   B 181 ? 1.03840 0.70429 0.82699 -0.12021 -0.21216 -0.06355 274 ILE   B C   
3883 O O   . ILE   B 181 ? 1.00661 0.65504 0.77998 -0.09358 -0.22215 -0.07428 274 ILE   B O   
3884 C CB  . ILE   B 181 ? 1.10192 0.79696 0.90843 -0.14187 -0.21605 -0.07141 274 ILE   B CB  
3885 C CG1 . ILE   B 181 ? 0.98722 0.73602 0.82368 -0.11978 -0.20167 -0.07134 274 ILE   B CG1 
3886 C CG2 . ILE   B 181 ? 1.27479 0.99078 1.09916 -0.17290 -0.21168 -0.06667 274 ILE   B CG2 
3887 C CD1 . ILE   B 181 ? 1.13365 0.88278 0.96118 -0.08952 -0.20796 -0.08452 274 ILE   B CD1 
3888 N N   . PHE   B 182 ? 0.98985 0.68776 0.80106 -0.12636 -0.19596 -0.05280 275 PHE   B N   
3889 C CA  . PHE   B 182 ? 0.93845 0.64852 0.75552 -0.10335 -0.19023 -0.05236 275 PHE   B CA  
3890 C C   . PHE   B 182 ? 0.98057 0.63283 0.76068 -0.09555 -0.20470 -0.05334 275 PHE   B C   
3891 O O   . PHE   B 182 ? 0.93319 0.57790 0.70561 -0.06733 -0.21199 -0.06270 275 PHE   B O   
3892 C CB  . PHE   B 182 ? 0.88083 0.63363 0.72778 -0.11406 -0.17082 -0.04061 275 PHE   B CB  
3893 C CG  . PHE   B 182 ? 0.86269 0.62521 0.71447 -0.09478 -0.16514 -0.03909 275 PHE   B CG  
3894 C CD1 . PHE   B 182 ? 0.89974 0.70299 0.77400 -0.07249 -0.15749 -0.04480 275 PHE   B CD1 
3895 C CD2 . PHE   B 182 ? 0.91661 0.64730 0.74910 -0.10040 -0.16756 -0.03199 275 PHE   B CD2 
3896 C CE1 . PHE   B 182 ? 0.77788 0.59264 0.65840 -0.05642 -0.15235 -0.04441 275 PHE   B CE1 
3897 C CE2 . PHE   B 182 ? 0.86978 0.61057 0.70748 -0.08249 -0.16364 -0.03151 275 PHE   B CE2 
3898 C CZ  . PHE   B 182 ? 0.84244 0.62683 0.70586 -0.06065 -0.15596 -0.03818 275 PHE   B CZ  
3899 N N   . ILE   B 183 ? 1.01286 0.62359 0.76865 -0.12058 -0.20948 -0.04431 276 ILE   B N   
3900 C CA  . ILE   B 183 ? 1.12095 0.66993 0.83613 -0.11473 -0.22490 -0.04352 276 ILE   B CA  
3901 C C   . ILE   B 183 ? 1.12967 0.62917 0.81234 -0.09833 -0.24770 -0.05685 276 ILE   B C   
3902 O O   . ILE   B 183 ? 1.23470 0.68658 0.88589 -0.08140 -0.26368 -0.06083 276 ILE   B O   
3903 C CB  . ILE   B 183 ? 1.14900 0.66395 0.84213 -0.14944 -0.22311 -0.02934 276 ILE   B CB  
3904 C CG1 . ILE   B 183 ? 1.26097 0.74944 0.93820 -0.17736 -0.23003 -0.02955 276 ILE   B CG1 
3905 C CG2 . ILE   B 183 ? 0.98375 0.55148 0.71089 -0.16466 -0.19995 -0.01828 276 ILE   B CG2 
3906 C CD1 . ILE   B 183 ? 1.24371 0.64803 0.86505 -0.18510 -0.25199 -0.02940 276 ILE   B CD1 
3907 N N   . GLN   B 184 ? 1.13359 0.64218 0.82215 -0.10162 -0.25088 -0.06481 277 GLN   B N   
3908 C CA  . GLN   B 184 ? 1.21904 0.68371 0.87801 -0.08368 -0.27227 -0.07952 277 GLN   B CA  
3909 C C   . GLN   B 184 ? 1.14002 0.62998 0.81115 -0.04368 -0.27398 -0.09419 277 GLN   B C   
3910 O O   . GLN   B 184 ? 1.19293 0.64083 0.83609 -0.02027 -0.29240 -0.10568 277 GLN   B O   
3911 C CB  . GLN   B 184 ? 1.29659 0.76503 0.95814 -0.10015 -0.27504 -0.08416 277 GLN   B CB  
3912 C CG  . GLN   B 184 ? 1.31945 0.76039 0.96688 -0.14103 -0.27552 -0.07277 277 GLN   B CG  
3913 C CD  . GLN   B 184 ? 1.47273 0.92232 1.12621 -0.15679 -0.27901 -0.07888 277 GLN   B CD  
3914 O OE1 . GLN   B 184 ? 1.60193 1.07815 1.26928 -0.13685 -0.28067 -0.09079 277 GLN   B OE1 
3915 N NE2 . GLN   B 184 ? 1.30506 0.73305 0.94742 -0.19378 -0.28001 -0.07124 277 GLN   B NE2 
3916 N N   . ILE   B 185 ? 1.05614 0.61448 0.76806 -0.03558 -0.25525 -0.09477 278 ILE   B N   
3917 C CA  . ILE   B 185 ? 1.03846 0.62727 0.76404 -0.00121 -0.25366 -0.10855 278 ILE   B CA  
3918 C C   . ILE   B 185 ? 1.07593 0.65700 0.79814 0.01491  -0.25521 -0.10725 278 ILE   B C   
3919 O O   . ILE   B 185 ? 1.04267 0.61405 0.75577 0.04473  -0.26630 -0.12203 278 ILE   B O   
3920 C CB  . ILE   B 185 ? 0.98240 0.64219 0.74820 -0.00084 -0.23299 -0.10776 278 ILE   B CB  
3921 C CG1 . ILE   B 185 ? 1.05870 0.72388 0.82573 -0.01577 -0.23407 -0.10957 278 ILE   B CG1 
3922 C CG2 . ILE   B 185 ? 0.99463 0.68749 0.77307 0.03121  -0.22958 -0.12236 278 ILE   B CG2 
3923 C CD1 . ILE   B 185 ? 0.96445 0.69258 0.76560 -0.01638 -0.21625 -0.10772 278 ILE   B CD1 
3924 N N   . ALA   B 186 ? 1.03071 0.61757 0.76066 -0.00378 -0.24462 -0.09089 279 ALA   B N   
3925 C CA  . ALA   B 186 ? 1.00961 0.58413 0.73269 0.00937  -0.24785 -0.08875 279 ALA   B CA  
3926 C C   . ALA   B 186 ? 1.08559 0.58545 0.76211 0.01926  -0.27384 -0.09427 279 ALA   B C   
3927 O O   . ALA   B 186 ? 1.15378 0.64148 0.82191 0.04439  -0.28391 -0.10172 279 ALA   B O   
3928 C CB  . ALA   B 186 ? 0.96895 0.55797 0.70400 -0.01570 -0.23236 -0.06992 279 ALA   B CB  
3929 N N   . GLU   B 187 ? 1.12891 0.57713 0.77402 -0.00008 -0.28607 -0.09128 280 GLU   B N   
3930 C CA  . GLU   B 187 ? 1.24967 0.61895 0.84504 0.00874  -0.31304 -0.09664 280 GLU   B CA  
3931 C C   . GLU   B 187 ? 1.31907 0.68378 0.90965 0.04838  -0.32894 -0.11969 280 GLU   B C   
3932 O O   . GLU   B 187 ? 1.21721 0.53725 0.77970 0.07153  -0.34934 -0.12789 280 GLU   B O   
3933 C CB  . GLU   B 187 ? 1.37518 0.69384 0.93967 -0.02304 -0.32138 -0.08946 280 GLU   B CB  
3934 C CG  . GLU   B 187 ? 1.43094 0.65817 0.93734 -0.01946 -0.35009 -0.09242 280 GLU   B CG  
3935 C CD  . GLU   B 187 ? 1.80424 0.98387 1.28108 -0.05495 -0.35674 -0.08516 280 GLU   B CD  
3936 O OE1 . GLU   B 187 ? 1.73445 0.95689 1.23949 -0.07646 -0.34120 -0.08229 280 GLU   B OE1 
3937 O OE2 . GLU   B 187 ? 1.98713 1.08566 1.41163 -0.06184 -0.37825 -0.08256 280 GLU   B OE2 
3938 N N   . LEU   B 188 ? 1.25102 0.66196 0.86793 0.05741  -0.32033 -0.13126 281 LEU   B N   
3939 C CA  . LEU   B 188 ? 1.21313 0.63013 0.82970 0.09509  -0.33187 -0.15496 281 LEU   B CA  
3940 C C   . LEU   B 188 ? 1.19376 0.65532 0.83650 0.12269  -0.32497 -0.16261 281 LEU   B C   
3941 O O   . LEU   B 188 ? 1.21313 0.65658 0.84331 0.15514  -0.34208 -0.18019 281 LEU   B O   
3942 C CB  . LEU   B 188 ? 1.20067 0.65785 0.83699 0.09482  -0.32237 -0.16437 281 LEU   B CB  
3943 C CG  . LEU   B 188 ? 1.22086 0.69754 0.86180 0.13204  -0.32912 -0.19009 281 LEU   B CG  
3944 C CD1 . LEU   B 188 ? 1.25058 0.65535 0.84822 0.15349  -0.35953 -0.20512 281 LEU   B CD1 
3945 C CD2 . LEU   B 188 ? 1.22731 0.74266 0.88444 0.12711  -0.31807 -0.19659 281 LEU   B CD2 
3946 N N   . LEU   B 189 ? 1.05112 0.57142 0.73070 0.11060  -0.30081 -0.15072 282 LEU   B N   
3947 C CA  . LEU   B 189 ? 1.06572 0.63053 0.77161 0.13320  -0.29317 -0.15734 282 LEU   B CA  
3948 C C   . LEU   B 189 ? 1.08851 0.60895 0.77078 0.14215  -0.30925 -0.15400 282 LEU   B C   
3949 O O   . LEU   B 189 ? 1.15426 0.68900 0.84434 0.17204  -0.31632 -0.16838 282 LEU   B O   
3950 C CB  . LEU   B 189 ? 1.00426 0.63586 0.75125 0.11558  -0.26459 -0.14426 282 LEU   B CB  
3951 C CG  . LEU   B 189 ? 1.00979 0.69431 0.78312 0.11365  -0.24833 -0.14990 282 LEU   B CG  
3952 C CD1 . LEU   B 189 ? 0.87388 0.60955 0.67995 0.09192  -0.22337 -0.13348 282 LEU   B CD1 
3953 C CD2 . LEU   B 189 ? 0.90020 0.61922 0.68667 0.14637  -0.24910 -0.17298 282 LEU   B CD2 
3954 N N   . ASP   B 190 ? 1.15582 0.62346 0.80863 0.11626  -0.31530 -0.13582 283 ASP   B N   
3955 C CA  . ASP   B 190 ? 1.19602 0.61221 0.81807 0.12331  -0.33274 -0.13151 283 ASP   B CA  
3956 C C   . ASP   B 190 ? 1.35897 0.72078 0.94668 0.15568  -0.36336 -0.15080 283 ASP   B C   
3957 O O   . ASP   B 190 ? 1.45289 0.79426 1.02810 0.17855  -0.37877 -0.15680 283 ASP   B O   
3958 C CB  . ASP   B 190 ? 1.22868 0.59506 0.82026 0.08576  -0.33271 -0.10858 283 ASP   B CB  
3959 C CG  . ASP   B 190 ? 1.32831 0.74504 0.95174 0.05934  -0.30539 -0.09063 283 ASP   B CG  
3960 O OD1 . ASP   B 190 ? 1.12687 0.60876 0.79136 0.07184  -0.28931 -0.09472 283 ASP   B OD1 
3961 O OD2 . ASP   B 190 ? 1.34786 0.73909 0.95479 0.02558  -0.29997 -0.07322 283 ASP   B OD2 
3962 N N   . LEU   B 191 ? 1.29624 0.63336 0.86784 0.15932  -0.37384 -0.16168 284 LEU   B N   
3963 C CA  . LEU   B 191 ? 1.32280 0.60954 0.86270 0.19291  -0.40359 -0.18268 284 LEU   B CA  
3964 C C   . LEU   B 191 ? 1.46629 0.81336 1.04126 0.23280  -0.40144 -0.20790 284 LEU   B C   
3965 O O   . LEU   B 191 ? 1.39478 0.72226 0.95826 0.26593  -0.42188 -0.22344 284 LEU   B O   
3966 C CB  . LEU   B 191 ? 1.58892 0.82938 1.09960 0.18291  -0.41534 -0.18688 284 LEU   B CB  
3967 C CG  . LEU   B 191 ? 1.61078 0.79122 1.08395 0.21653  -0.44791 -0.20932 284 LEU   B CG  
3968 C CD1 . LEU   B 191 ? 1.70161 0.80159 1.12688 0.22306  -0.47473 -0.20349 284 LEU   B CD1 
3969 C CD2 . LEU   B 191 ? 1.61622 0.75957 1.06551 0.20339  -0.45589 -0.21323 284 LEU   B CD2 
3970 N N   . CYS   B 192 ? 1.28143 0.70299 0.89881 0.22972  -0.37694 -0.21277 285 CYS   B N   
3971 C CA  . CYS   B 192 ? 1.23638 0.71965 0.88699 0.26349  -0.37183 -0.23734 285 CYS   B CA  
3972 C C   . CYS   B 192 ? 1.30229 0.82339 0.97795 0.27841  -0.36703 -0.23898 285 CYS   B C   
3973 O O   . CYS   B 192 ? 1.33114 0.87973 1.02135 0.31329  -0.37468 -0.26279 285 CYS   B O   
3974 C CB  . CYS   B 192 ? 1.34770 0.89915 1.03369 0.25121  -0.34488 -0.23835 285 CYS   B CB  
3975 S SG  . CYS   B 192 ? 1.43845 0.95518 1.09943 0.23690  -0.35060 -0.24028 285 CYS   B SG  
3976 N N   . VAL   B 193 ? 1.23150 0.75675 0.91343 0.25280  -0.35456 -0.21545 286 VAL   B N   
3977 C CA  . VAL   B 193 ? 1.17014 0.73180 0.87595 0.26486  -0.34965 -0.21634 286 VAL   B CA  
3978 C C   . VAL   B 193 ? 1.14629 0.65205 0.82034 0.29213  -0.38085 -0.22604 286 VAL   B C   
3979 O O   . VAL   B 193 ? 1.29168 0.82934 0.98599 0.31379  -0.38321 -0.23619 286 VAL   B O   
3980 C CB  . VAL   B 193 ? 1.15977 0.73919 0.87898 0.23007  -0.32809 -0.18908 286 VAL   B CB  
3981 C CG1 . VAL   B 193 ? 1.21285 0.71590 0.88782 0.21195  -0.34346 -0.17015 286 VAL   B CG1 
3982 C CG2 . VAL   B 193 ? 0.98998 0.63345 0.74860 0.24002  -0.31389 -0.19251 286 VAL   B CG2 
3983 N N   . LEU   B 194 ? 1.24979 0.67101 0.87302 0.29170  -0.40621 -0.22367 287 LEU   B N   
3984 C CA  . LEU   B 194 ? 1.29999 0.66021 0.88723 0.32024  -0.43950 -0.23389 287 LEU   B CA  
3985 C C   . LEU   B 194 ? 1.43828 0.82279 1.03966 0.36674  -0.45481 -0.26823 287 LEU   B C   
3986 O O   . LEU   B 194 ? 1.56731 0.93653 1.16093 0.39810  -0.47690 -0.28205 287 LEU   B O   
3987 C CB  . LEU   B 194 ? 1.36510 0.62346 0.88989 0.30494  -0.46270 -0.22158 287 LEU   B CB  
3988 C CG  . LEU   B 194 ? 1.38490 0.61300 0.89024 0.25792  -0.44970 -0.18908 287 LEU   B CG  
3989 C CD1 . LEU   B 194 ? 1.51949 0.64445 0.95986 0.24368  -0.47449 -0.17974 287 LEU   B CD1 
3990 C CD2 . LEU   B 194 ? 1.33937 0.58315 0.85367 0.25289  -0.44318 -0.17599 287 LEU   B CD2 
3991 N N   . ASP   B 195 ? 1.33732 0.76061 0.95910 0.37243  -0.44392 -0.28335 288 ASP   B N   
3992 C CA  . ASP   B 195 ? 1.48766 0.94411 1.12692 0.41522  -0.45442 -0.31799 288 ASP   B CA  
3993 C C   . ASP   B 195 ? 1.34236 0.89868 1.04009 0.42438  -0.43024 -0.32822 288 ASP   B C   
3994 O O   . ASP   B 195 ? 1.33607 0.95109 1.06634 0.39816  -0.39858 -0.31620 288 ASP   B O   
3995 C CB  . ASP   B 195 ? 1.50395 0.95827 1.13683 0.41585  -0.45237 -0.33003 288 ASP   B CB  
3996 C CG  . ASP   B 195 ? 1.55113 1.01573 1.18681 0.46254  -0.47111 -0.36753 288 ASP   B CG  
3997 O OD1 . ASP   B 195 ? 1.59668 1.12242 1.26763 0.48818  -0.46833 -0.38492 288 ASP   B OD1 
3998 O OD2 . ASP   B 195 ? 1.79031 1.21717 1.39907 0.46638  -0.48502 -0.37242 288 ASP   B OD2 
3999 N N   . VAL   B 196 ? 1.38499 0.95955 1.09523 0.46145  -0.44616 -0.35096 289 VAL   B N   
4000 C CA  . VAL   B 196 ? 1.43634 1.10344 1.20099 0.46923  -0.42522 -0.36126 289 VAL   B CA  
4001 C C   . VAL   B 196 ? 1.30866 1.05450 1.11197 0.47326  -0.40106 -0.38005 289 VAL   B C   
4002 O O   . VAL   B 196 ? 1.28821 1.11402 1.13630 0.46570  -0.37487 -0.38167 289 VAL   B O   
4003 C CB  . VAL   B 196 ? 1.51994 1.18674 1.28823 0.50982  -0.45123 -0.38387 289 VAL   B CB  
4004 C CG1 . VAL   B 196 ? 1.18620 0.93262 1.00334 0.50677  -0.43105 -0.38412 289 VAL   B CG1 
4005 C CG2 . VAL   B 196 ? 1.43565 1.00613 1.14890 0.50937  -0.48319 -0.36797 289 VAL   B CG2 
4006 N N   . ASP   B 197 ? 1.36805 1.09142 1.15263 0.48360  -0.40904 -0.39407 290 ASP   B N   
4007 C CA  . ASP   B 197 ? 1.38237 1.17599 1.19773 0.48714  -0.38673 -0.41232 290 ASP   B CA  
4008 C C   . ASP   B 197 ? 1.25625 1.08438 1.08717 0.44488  -0.35283 -0.38743 290 ASP   B C   
4009 O O   . ASP   B 197 ? 1.31717 1.20394 1.17149 0.44337  -0.33190 -0.39917 290 ASP   B O   
4010 C CB  . ASP   B 197 ? 1.36455 1.11826 1.15100 0.51066  -0.40687 -0.43453 290 ASP   B CB  
4011 C CG  . ASP   B 197 ? 1.50205 1.25590 1.28652 0.54302  -0.43389 -0.45139 290 ASP   B CG  
4012 O OD1 . ASP   B 197 ? 1.52352 1.34162 1.34414 0.55748  -0.42901 -0.46474 290 ASP   B OD1 
4013 O OD2 . ASP   B 197 ? 1.48904 1.17916 1.23485 0.55263  -0.46056 -0.45173 290 ASP   B OD2 
4014 N N   . CYS   B 198 ? 1.34148 1.13533 1.15911 0.41126  -0.34723 -0.35443 291 CYS   B N   
4015 C CA  . CYS   B 198 ? 1.12908 0.95523 0.96223 0.37333  -0.31710 -0.33168 291 CYS   B CA  
4016 C C   . CYS   B 198 ? 1.18721 1.09859 1.06734 0.36679  -0.28925 -0.33203 291 CYS   B C   
4017 O O   . CYS   B 198 ? 1.11095 1.06509 1.00898 0.34462  -0.26340 -0.32328 291 CYS   B O   
4018 C CB  . CYS   B 198 ? 1.09864 0.86726 0.90624 0.34067  -0.31938 -0.29879 291 CYS   B CB  
4019 S SG  . CYS   B 198 ? 1.17560 0.93854 0.98955 0.33495  -0.32172 -0.28237 291 CYS   B SG  
4020 N N   . LEU   B 199 ? 1.14814 1.08312 1.04697 0.38537  -0.29512 -0.34216 292 LEU   B N   
4021 C CA  . LEU   B 199 ? 1.12479 1.13833 1.06743 0.37774  -0.26991 -0.34274 292 LEU   B CA  
4022 C C   . LEU   B 199 ? 1.06941 1.15482 1.04030 0.38726  -0.25130 -0.36614 292 LEU   B C   
4023 O O   . LEU   B 199 ? 1.08177 1.23240 1.08586 0.37323  -0.22575 -0.36378 292 LEU   B O   
4024 C CB  . LEU   B 199 ? 1.13917 1.16042 1.09445 0.39804  -0.28377 -0.35162 292 LEU   B CB  
4025 C CG  . LEU   B 199 ? 1.12279 1.08096 1.05191 0.38574  -0.29851 -0.32704 292 LEU   B CG  
4026 C CD1 . LEU   B 199 ? 1.05944 1.03127 1.00248 0.40782  -0.31230 -0.33823 292 LEU   B CD1 
4027 C CD2 . LEU   B 199 ? 1.01014 0.97390 0.94416 0.34412  -0.27398 -0.29487 292 LEU   B CD2 
4028 N N   . GLU   B 200 ? 1.12635 1.20006 1.08280 0.40997  -0.26341 -0.38896 293 GLU   B N   
4029 C CA  . GLU   B 200 ? 1.17357 1.31292 1.15183 0.41588  -0.24398 -0.41033 293 GLU   B CA  
4030 C C   . GLU   B 200 ? 1.14327 1.30494 1.12516 0.37913  -0.21527 -0.38827 293 GLU   B C   
4031 O O   . GLU   B 200 ? 1.13048 1.35988 1.13820 0.37232  -0.19050 -0.39649 293 GLU   B O   
4032 C CB  . GLU   B 200 ? 1.18152 1.29341 1.13700 0.44515  -0.26376 -0.43661 293 GLU   B CB  
4033 C CG  . GLU   B 200 ? 1.33848 1.51296 1.31027 0.45063  -0.24397 -0.45925 293 GLU   B CG  
4034 C CD  . GLU   B 200 ? 1.33698 1.47585 1.28092 0.47614  -0.26349 -0.48223 293 GLU   B CD  
4035 O OE1 . GLU   B 200 ? 1.41380 1.48237 1.32857 0.49449  -0.29467 -0.48464 293 GLU   B OE1 
4036 O OE2 . GLU   B 200 ? 1.40306 1.58161 1.35158 0.47724  -0.24802 -0.49778 293 GLU   B OE2 
4037 N N   . PHE   B 201 ? 1.01624 1.12216 0.97197 0.35476  -0.21851 -0.36067 294 PHE   B N   
4038 C CA  . PHE   B 201 ? 1.01157 1.13168 0.96817 0.32163  -0.19537 -0.33931 294 PHE   B CA  
4039 C C   . PHE   B 201 ? 0.99668 1.12220 0.96665 0.29397  -0.18224 -0.31084 294 PHE   B C   
4040 O O   . PHE   B 201 ? 0.87180 0.95800 0.83327 0.29363  -0.19656 -0.29940 294 PHE   B O   
4041 C CB  . PHE   B 201 ? 1.05073 1.11040 0.97185 0.31249  -0.20739 -0.32975 294 PHE   B CB  
4042 C CG  . PHE   B 201 ? 1.04670 1.07909 0.94639 0.34200  -0.22847 -0.35623 294 PHE   B CG  
4043 C CD1 . PHE   B 201 ? 0.98662 1.06070 0.89230 0.35453  -0.21875 -0.37923 294 PHE   B CD1 
4044 C CD2 . PHE   B 201 ? 1.04413 1.00683 0.91495 0.35699  -0.25836 -0.35845 294 PHE   B CD2 
4045 C CE1 . PHE   B 201 ? 1.13999 1.18900 1.02570 0.38324  -0.23857 -0.40531 294 PHE   B CE1 
4046 C CE2 . PHE   B 201 ? 1.17497 1.10821 1.02390 0.38544  -0.27954 -0.38356 294 PHE   B CE2 
4047 C CZ  . PHE   B 201 ? 1.11734 1.09490 0.97496 0.39947  -0.26969 -0.40769 294 PHE   B CZ  
4048 N N   . PRO   B 202 ? 0.89431 1.06603 0.88277 0.27101  -0.15572 -0.29958 295 PRO   B N   
4049 C CA  . PRO   B 202 ? 0.77858 0.95397 0.77865 0.24484  -0.14330 -0.27293 295 PRO   B CA  
4050 C C   . PRO   B 202 ? 0.93225 1.04527 0.90755 0.22697  -0.15394 -0.24873 295 PRO   B C   
4051 O O   . PRO   B 202 ? 0.77247 0.84705 0.72317 0.22628  -0.16448 -0.24852 295 PRO   B O   
4052 C CB  . PRO   B 202 ? 0.80915 1.03617 0.82477 0.22500  -0.11567 -0.26734 295 PRO   B CB  
4053 C CG  . PRO   B 202 ? 0.88079 1.14849 0.90252 0.24441  -0.11103 -0.29581 295 PRO   B CG  
4054 C CD  . PRO   B 202 ? 0.82849 1.05148 0.82657 0.26889  -0.13611 -0.31199 295 PRO   B CD  
4055 N N   . TYR   B 203 ? 0.78867 0.89366 0.77111 0.21150  -0.15065 -0.22905 296 TYR   B N   
4056 C CA  . TYR   B 203 ? 0.79498 0.84585 0.75639 0.19281  -0.15896 -0.20662 296 TYR   B CA  
4057 C C   . TYR   B 203 ? 0.66902 0.71663 0.62334 0.17098  -0.14872 -0.19373 296 TYR   B C   
4058 O O   . TYR   B 203 ? 0.80711 0.80776 0.73787 0.16307  -0.16071 -0.18630 296 TYR   B O   
4059 C CB  . TYR   B 203 ? 0.72824 0.78168 0.70177 0.17893  -0.15290 -0.18899 296 TYR   B CB  
4060 C CG  . TYR   B 203 ? 0.78068 0.81950 0.75257 0.19839  -0.16894 -0.19776 296 TYR   B CG  
4061 C CD1 . TYR   B 203 ? 0.74533 0.75963 0.70158 0.22638  -0.19073 -0.21838 296 TYR   B CD1 
4062 C CD2 . TYR   B 203 ? 0.75788 0.80533 0.74222 0.18988  -0.16383 -0.18601 296 TYR   B CD2 
4063 C CE1 . TYR   B 203 ? 0.84400 0.84253 0.79695 0.24604  -0.20796 -0.22679 296 TYR   B CE1 
4064 C CE2 . TYR   B 203 ? 0.81116 0.84398 0.79213 0.20806  -0.18001 -0.19398 296 TYR   B CE2 
4065 C CZ  . TYR   B 203 ? 0.88530 0.89345 0.85047 0.23642  -0.20255 -0.21420 296 TYR   B CZ  
4066 O OH  . TYR   B 203 ? 0.84051 0.83205 0.80076 0.25633  -0.22104 -0.22255 296 TYR   B OH  
4067 N N   . GLY   B 204 ? 0.78739 0.88329 0.76051 0.16037  -0.12740 -0.19107 297 GLY   B N   
4068 C CA  . GLY   B 204 ? 0.76064 0.85474 0.72639 0.14199  -0.11928 -0.18008 297 GLY   B CA  
4069 C C   . GLY   B 204 ? 0.85136 0.92710 0.79626 0.15297  -0.12994 -0.19459 297 GLY   B C   
4070 O O   . GLY   B 204 ? 0.78867 0.84081 0.71911 0.13944  -0.13301 -0.18543 297 GLY   B O   
4071 N N   . ILE   B 205 ? 0.84131 0.92895 0.78512 0.17815  -0.13628 -0.21871 298 ILE   B N   
4072 C CA  . ILE   B 205 ? 0.79711 0.86536 0.71953 0.19141  -0.14786 -0.23513 298 ILE   B CA  
4073 C C   . ILE   B 205 ? 0.85207 0.85339 0.74769 0.19462  -0.17252 -0.23269 298 ILE   B C   
4074 O O   . ILE   B 205 ? 0.85968 0.83006 0.73406 0.18893  -0.18102 -0.23207 298 ILE   B O   
4075 C CB  . ILE   B 205 ? 0.92701 1.03157 0.85793 0.21878  -0.14683 -0.26395 298 ILE   B CB  
4076 C CG1 . ILE   B 205 ? 1.05444 1.22467 1.00806 0.21061  -0.12049 -0.26579 298 ILE   B CG1 
4077 C CG2 . ILE   B 205 ? 0.84457 0.92537 0.75152 0.23515  -0.16074 -0.28292 298 ILE   B CG2 
4078 C CD1 . ILE   B 205 ? 1.03116 1.21048 0.97318 0.19527  -0.10891 -0.26024 298 ILE   B CD1 
4079 N N   . LEU   B 206 ? 0.84007 0.81617 0.73404 0.20261  -0.18487 -0.23110 299 LEU   B N   
4080 C CA  . LEU   B 206 ? 0.89458 0.80188 0.75833 0.20398  -0.20880 -0.22777 299 LEU   B CA  
4081 C C   . LEU   B 206 ? 0.88786 0.76562 0.74061 0.17282  -0.20670 -0.20402 299 LEU   B C   
4082 O O   . LEU   B 206 ? 0.93998 0.77141 0.76641 0.16812  -0.22131 -0.20407 299 LEU   B O   
4083 C CB  . LEU   B 206 ? 0.82802 0.71538 0.69084 0.21580  -0.22081 -0.22772 299 LEU   B CB  
4084 C CG  . LEU   B 206 ? 0.88268 0.79028 0.75376 0.25049  -0.22974 -0.25408 299 LEU   B CG  
4085 C CD1 . LEU   B 206 ? 1.08639 0.98206 0.96100 0.25782  -0.23863 -0.24999 299 LEU   B CD1 
4086 C CD2 . LEU   B 206 ? 0.94540 0.81205 0.78840 0.27393  -0.25271 -0.27483 299 LEU   B CD2 
4087 N N   . ALA   B 207 ? 0.76948 0.67445 0.64276 0.15122  -0.18899 -0.18467 300 ALA   B N   
4088 C CA  . ALA   B 207 ? 0.87761 0.76241 0.74535 0.12235  -0.18594 -0.16391 300 ALA   B CA  
4089 C C   . ALA   B 207 ? 0.76097 0.65356 0.62405 0.11460  -0.18261 -0.16625 300 ALA   B C   
4090 O O   . ALA   B 207 ? 0.86195 0.71997 0.70857 0.09910  -0.19134 -0.15898 300 ALA   B O   
4091 C CB  . ALA   B 207 ? 0.72836 0.64524 0.62101 0.10453  -0.16760 -0.14563 300 ALA   B CB  
4092 N N   . ALA   B 208 ? 0.75581 0.69369 0.63198 0.12415  -0.17015 -0.17672 301 ALA   B N   
4093 C CA  . ALA   B 208 ? 0.89478 0.83988 0.76345 0.11819  -0.16761 -0.17970 301 ALA   B CA  
4094 C C   . ALA   B 208 ? 0.91008 0.81459 0.75067 0.13152  -0.18758 -0.19605 301 ALA   B C   
4095 O O   . ALA   B 208 ? 0.86422 0.74950 0.69070 0.12015  -0.19346 -0.19368 301 ALA   B O   
4096 C CB  . ALA   B 208 ? 0.78273 0.78343 0.66730 0.12448  -0.14908 -0.18703 301 ALA   B CB  
4097 N N   . SER   B 209 ? 0.86950 0.75995 0.70150 0.15644  -0.19948 -0.21373 302 SER   B N   
4098 C CA  . SER   B 209 ? 0.87712 0.72486 0.68030 0.17175  -0.22036 -0.23092 302 SER   B CA  
4099 C C   . SER   B 209 ? 0.99249 0.77572 0.77109 0.15608  -0.23851 -0.21907 302 SER   B C   
4100 O O   . SER   B 209 ? 1.03453 0.78199 0.78914 0.15403  -0.25222 -0.22512 302 SER   B O   
4101 C CB  . SER   B 209 ? 1.03679 0.88667 0.83830 0.20475  -0.22980 -0.25412 302 SER   B CB  
4102 O OG  . SER   B 209 ? 1.01294 0.92617 0.83745 0.21711  -0.21173 -0.26703 302 SER   B OG  
4103 N N   . ALA   B 210 ? 0.90216 0.66936 0.68478 0.14352  -0.23858 -0.20249 303 ALA   B N   
4104 C CA  . ALA   B 210 ? 0.97681 0.68553 0.73557 0.12351  -0.25279 -0.18948 303 ALA   B CA  
4105 C C   . ALA   B 210 ? 1.00883 0.72501 0.77255 0.09431  -0.24460 -0.17558 303 ALA   B C   
4106 O O   . ALA   B 210 ? 0.95891 0.63146 0.69938 0.08119  -0.25826 -0.17416 303 ALA   B O   
4107 C CB  . ALA   B 210 ? 0.96130 0.65533 0.72251 0.11613  -0.25260 -0.17518 303 ALA   B CB  
4108 N N   . LEU   B 211 ? 0.92445 0.69484 0.71784 0.08390  -0.22344 -0.16585 304 LEU   B N   
4109 C CA  . LEU   B 211 ? 1.00274 0.78532 0.80331 0.05975  -0.21674 -0.15476 304 LEU   B CA  
4110 C C   . LEU   B 211 ? 0.88785 0.66387 0.67287 0.06588  -0.22510 -0.16868 304 LEU   B C   
4111 O O   . LEU   B 211 ? 0.95307 0.71076 0.72943 0.04742  -0.23165 -0.16397 304 LEU   B O   
4112 C CB  . LEU   B 211 ? 1.06531 0.90494 0.89792 0.05220  -0.19440 -0.14362 304 LEU   B CB  
4113 C CG  . LEU   B 211 ? 0.94657 0.80446 0.78960 0.03065  -0.18779 -0.13303 304 LEU   B CG  
4114 C CD1 . LEU   B 211 ? 1.00577 0.86840 0.86547 0.00792  -0.18017 -0.11412 304 LEU   B CD1 
4115 C CD2 . LEU   B 211 ? 1.03319 0.93854 0.88995 0.03810  -0.17388 -0.13629 304 LEU   B CD2 
4116 N N   . TYR   B 212 ? 1.01491 0.80759 0.79651 0.09141  -0.22491 -0.18706 305 TYR   B N   
4117 C CA  . TYR   B 212 ? 0.98603 0.77354 0.75080 0.09905  -0.23235 -0.20202 305 TYR   B CA  
4118 C C   . TYR   B 212 ? 1.03770 0.76193 0.77065 0.09700  -0.25614 -0.20857 305 TYR   B C   
4119 O O   . TYR   B 212 ? 1.05534 0.76584 0.77573 0.08644  -0.26333 -0.21072 305 TYR   B O   
4120 C CB  . TYR   B 212 ? 0.90688 0.72454 0.67318 0.12768  -0.22706 -0.22256 305 TYR   B CB  
4121 C CG  . TYR   B 212 ? 0.98983 0.79025 0.73160 0.14136  -0.23926 -0.24278 305 TYR   B CG  
4122 C CD1 . TYR   B 212 ? 1.04742 0.86730 0.78637 0.13236  -0.23353 -0.24301 305 TYR   B CD1 
4123 C CD2 . TYR   B 212 ? 1.04253 0.80520 0.76212 0.16433  -0.25781 -0.26228 305 TYR   B CD2 
4124 C CE1 . TYR   B 212 ? 1.08181 0.88552 0.79666 0.14472  -0.24477 -0.26205 305 TYR   B CE1 
4125 C CE2 . TYR   B 212 ? 1.27120 1.01706 0.96742 0.17778  -0.26940 -0.28209 305 TYR   B CE2 
4126 C CZ  . TYR   B 212 ? 1.20012 0.96737 0.89416 0.16732  -0.26221 -0.28186 305 TYR   B CZ  
4127 O OH  . TYR   B 212 ? 1.27875 1.02905 0.94796 0.18063  -0.27377 -0.30216 305 TYR   B OH  
4128 N N   . HIS   B 213 ? 1.05444 0.73702 0.77194 0.10666  -0.26977 -0.21186 306 HIS   B N   
4129 C CA  . HIS   B 213 ? 1.17222 0.78727 0.85437 0.10477  -0.29394 -0.21802 306 HIS   B CA  
4130 C C   . HIS   B 213 ? 1.06311 0.65139 0.73964 0.06938  -0.29717 -0.19995 306 HIS   B C   
4131 O O   . HIS   B 213 ? 1.25309 0.79150 0.90128 0.06142  -0.31516 -0.20474 306 HIS   B O   
4132 C CB  . HIS   B 213 ? 1.20826 0.78184 0.87254 0.12358  -0.30881 -0.22439 306 HIS   B CB  
4133 C CG  . HIS   B 213 ? 1.29089 0.87807 0.95318 0.16134  -0.31347 -0.24903 306 HIS   B CG  
4134 N ND1 . HIS   B 213 ? 1.17377 0.81284 0.86343 0.17892  -0.29864 -0.25350 306 HIS   B ND1 
4135 C CD2 . HIS   B 213 ? 1.25166 0.80987 0.88899 0.18482  -0.33110 -0.27212 306 HIS   B CD2 
4136 C CE1 . HIS   B 213 ? 1.27628 0.92115 0.95981 0.21132  -0.30625 -0.27881 306 HIS   B CE1 
4137 N NE2 . HIS   B 213 ? 1.34703 0.94298 0.99866 0.21662  -0.32608 -0.29081 306 HIS   B NE2 
4138 N N   . PHE   B 214 ? 1.10009 0.72107 0.80309 0.04780  -0.28035 -0.18059 307 PHE   B N   
4139 C CA  . PHE   B 214 ? 1.12616 0.73438 0.83040 0.01368  -0.28042 -0.16508 307 PHE   B CA  
4140 C C   . PHE   B 214 ? 1.23852 0.89305 0.96529 0.00111  -0.26892 -0.16158 307 PHE   B C   
4141 O O   . PHE   B 214 ? 1.23562 0.89112 0.97036 -0.02648 -0.26739 -0.15008 307 PHE   B O   
4142 C CB  . PHE   B 214 ? 1.08582 0.69542 0.80236 -0.00304 -0.27116 -0.14667 307 PHE   B CB  
4143 C CG  . PHE   B 214 ? 1.04310 0.59446 0.73010 0.00144  -0.28610 -0.14670 307 PHE   B CG  
4144 C CD1 . PHE   B 214 ? 1.15996 0.71247 0.84604 0.02870  -0.28712 -0.15338 307 PHE   B CD1 
4145 C CD2 . PHE   B 214 ? 1.14412 0.63866 0.80283 -0.02227 -0.29988 -0.14031 307 PHE   B CD2 
4146 C CE1 . PHE   B 214 ? 1.14548 0.64130 0.80175 0.03468  -0.30334 -0.15357 307 PHE   B CE1 
4147 C CE2 . PHE   B 214 ? 1.22811 0.66280 0.85389 -0.01868 -0.31506 -0.13927 307 PHE   B CE2 
4148 C CZ  . PHE   B 214 ? 1.15321 0.58739 0.77714 0.01106  -0.31766 -0.14584 307 PHE   B CZ  
4149 N N   . SER   B 215 ? 1.16813 0.86110 0.90431 0.02041  -0.26122 -0.17176 308 SER   B N   
4150 C CA  . SER   B 215 ? 0.94220 0.67570 0.69521 0.01070  -0.25201 -0.16848 308 SER   B CA  
4151 C C   . SER   B 215 ? 0.95941 0.70430 0.70002 0.03159  -0.25471 -0.18626 308 SER   B C   
4152 O O   . SER   B 215 ? 1.03324 0.74255 0.74794 0.03594  -0.27135 -0.19943 308 SER   B O   
4153 C CB  . SER   B 215 ? 0.88508 0.67001 0.67112 0.00551  -0.23088 -0.15403 308 SER   B CB  
4154 O OG  . SER   B 215 ? 0.99593 0.80388 0.78857 0.02787  -0.22065 -0.15934 308 SER   B OG  
4155 N N   . SER   B 216 ? 0.93308 0.72609 0.68992 0.04354  -0.23826 -0.18705 309 SER   B N   
4156 C CA  . SER   B 216 ? 1.11856 0.92829 0.86344 0.06070  -0.23748 -0.20300 309 SER   B CA  
4157 C C   . SER   B 216 ? 0.95045 0.80674 0.71126 0.07579  -0.21811 -0.20447 309 SER   B C   
4158 O O   . SER   B 216 ? 0.92798 0.80575 0.71102 0.07038  -0.20547 -0.19133 309 SER   B O   
4159 C CB  . SER   B 216 ? 0.97159 0.79242 0.71469 0.04616  -0.23947 -0.19973 309 SER   B CB  
4160 O OG  . SER   B 216 ? 0.96393 0.82212 0.73279 0.03175  -0.22502 -0.18223 309 SER   B OG  
4161 N N   . SER   B 217 ? 1.04373 0.91593 0.79197 0.09376  -0.21553 -0.22145 310 SER   B N   
4162 C CA  . SER   B 217 ? 1.00097 0.92044 0.76237 0.10534  -0.19585 -0.22437 310 SER   B CA  
4163 C C   . SER   B 217 ? 1.01497 0.97021 0.79098 0.08868  -0.18037 -0.20734 310 SER   B C   
4164 O O   . SER   B 217 ? 1.03442 1.02478 0.82734 0.08963  -0.16298 -0.20120 310 SER   B O   
4165 C CB  . SER   B 217 ? 1.23642 1.16477 0.97877 0.12732  -0.19637 -0.24849 310 SER   B CB  
4166 O OG  . SER   B 217 ? 1.17168 1.09134 0.89369 0.12191  -0.20333 -0.25283 310 SER   B OG  
4167 N N   . GLU   B 218 ? 1.07978 1.02558 0.84892 0.07366  -0.18760 -0.20016 311 GLU   B N   
4168 C CA  . GLU   B 218 ? 1.07282 1.04778 0.85391 0.05940  -0.17637 -0.18421 311 GLU   B CA  
4169 C C   . GLU   B 218 ? 0.85574 0.83866 0.66426 0.04592  -0.16933 -0.16519 311 GLU   B C   
4170 O O   . GLU   B 218 ? 1.00851 1.02208 0.83144 0.04283  -0.15385 -0.15482 311 GLU   B O   
4171 C CB  . GLU   B 218 ? 1.05999 1.02216 0.82793 0.04848  -0.18900 -0.18310 311 GLU   B CB  
4172 C CG  . GLU   B 218 ? 1.13051 1.09028 0.86951 0.06041  -0.19375 -0.20039 311 GLU   B CG  
4173 C CD  . GLU   B 218 ? 1.34865 1.27394 1.06892 0.07330  -0.20867 -0.21953 311 GLU   B CD  
4174 O OE1 . GLU   B 218 ? 1.29606 1.19339 1.02289 0.07024  -0.21795 -0.21763 311 GLU   B OE1 
4175 O OE2 . GLU   B 218 ? 1.48192 1.40602 1.17853 0.08651  -0.21153 -0.23675 311 GLU   B OE2 
4176 N N   . LEU   B 219 ? 0.96308 0.91717 0.77702 0.03679  -0.18041 -0.16060 312 LEU   B N   
4177 C CA  . LEU   B 219 ? 0.78474 0.74577 0.62305 0.02422  -0.17334 -0.14404 312 LEU   B CA  
4178 C C   . LEU   B 219 ? 0.87358 0.84755 0.72183 0.03613  -0.16177 -0.14478 312 LEU   B C   
4179 O O   . LEU   B 219 ? 0.79685 0.79399 0.66552 0.02989  -0.14892 -0.13205 312 LEU   B O   
4180 C CB  . LEU   B 219 ? 0.93711 0.86313 0.77479 0.00981  -0.18716 -0.14002 312 LEU   B CB  
4181 C CG  . LEU   B 219 ? 0.97182 0.90400 0.83274 -0.00508 -0.17992 -0.12370 312 LEU   B CG  
4182 C CD1 . LEU   B 219 ? 1.11871 1.08543 1.00045 -0.01627 -0.17029 -0.11127 312 LEU   B CD1 
4183 C CD2 . LEU   B 219 ? 1.15444 1.04954 1.00950 -0.02077 -0.19277 -0.12129 312 LEU   B CD2 
4184 N N   . MET   B 220 ? 0.93821 0.89774 0.77262 0.05414  -0.16720 -0.16075 313 MET   B N   
4185 C CA  . MET   B 220 ? 0.93473 0.90990 0.77958 0.06772  -0.15780 -0.16453 313 MET   B CA  
4186 C C   . MET   B 220 ? 0.92360 0.94552 0.78057 0.06997  -0.13813 -0.16223 313 MET   B C   
4187 O O   . MET   B 220 ? 0.92561 0.96864 0.80198 0.06682  -0.12596 -0.15284 313 MET   B O   
4188 C CB  . MET   B 220 ? 0.95128 0.90531 0.77829 0.08980  -0.16916 -0.18569 313 MET   B CB  
4189 C CG  . MET   B 220 ? 1.02795 0.99975 0.86627 0.10724  -0.16226 -0.19374 313 MET   B CG  
4190 S SD  . MET   B 220 ? 0.96133 0.99065 0.80831 0.11998  -0.14193 -0.20584 313 MET   B SD  
4191 C CE  . MET   B 220 ? 1.11860 1.13874 0.93762 0.12698  -0.14978 -0.22226 313 MET   B CE  
4192 N N   . GLN   B 221 ? 0.97342 1.01001 0.81654 0.07419  -0.13491 -0.17065 314 GLN   B N   
4193 C CA  . GLN   B 221 ? 1.00541 1.08267 0.85397 0.07392  -0.11610 -0.16842 314 GLN   B CA  
4194 C C   . GLN   B 221 ? 0.91464 1.00411 0.77664 0.05528  -0.10809 -0.14687 314 GLN   B C   
4195 O O   . GLN   B 221 ? 1.01286 1.13060 0.88569 0.05224  -0.09228 -0.14006 314 GLN   B O   
4196 C CB  . GLN   B 221 ? 1.01815 1.10369 0.84321 0.08120  -0.11541 -0.18228 314 GLN   B CB  
4197 C CG  . GLN   B 221 ? 0.88308 1.00876 0.70746 0.08104  -0.09525 -0.18304 314 GLN   B CG  
4198 C CD  . GLN   B 221 ? 0.91825 1.05157 0.71627 0.08948  -0.09401 -0.19959 314 GLN   B CD  
4199 O OE1 . GLN   B 221 ? 1.00810 1.11569 0.78845 0.09575  -0.10932 -0.21000 314 GLN   B OE1 
4200 N NE2 . GLN   B 221 ? 1.08023 1.24836 0.87378 0.08849  -0.07544 -0.20245 314 GLN   B NE2 
4201 N N   . LYS   B 222 ? 1.00150 1.07050 0.86340 0.04276  -0.11925 -0.13698 315 LYS   B N   
4202 C CA  . LYS   B 222 ? 0.91511 0.99611 0.79066 0.02751  -0.11375 -0.11867 315 LYS   B CA  
4203 C C   . LYS   B 222 ? 0.93599 1.02409 0.83588 0.02228  -0.10579 -0.10732 315 LYS   B C   
4204 O O   . LYS   B 222 ? 1.04061 1.14918 0.95202 0.01581  -0.09432 -0.09569 315 LYS   B O   
4205 C CB  . LYS   B 222 ? 1.02733 1.08898 0.89995 0.01644  -0.12862 -0.11406 315 LYS   B CB  
4206 C CG  . LYS   B 222 ? 1.14307 1.21679 1.03340 0.00256  -0.12574 -0.09720 315 LYS   B CG  
4207 C CD  . LYS   B 222 ? 1.27174 1.33025 1.16440 -0.00846 -0.14111 -0.09531 315 LYS   B CD  
4208 C CE  . LYS   B 222 ? 1.39222 1.46610 1.30674 -0.02015 -0.13878 -0.08092 315 LYS   B CE  
4209 N NZ  . LYS   B 222 ? 1.29500 1.36026 1.21659 -0.03178 -0.15318 -0.08094 315 LYS   B NZ  
4210 N N   . VAL   B 223 ? 0.94788 1.01644 0.85299 0.02502  -0.11249 -0.11055 316 VAL   B N   
4211 C CA  . VAL   B 223 ? 1.00368 1.07468 0.92912 0.01887  -0.10685 -0.09960 316 VAL   B CA  
4212 C C   . VAL   B 223 ? 0.88452 0.96941 0.81629 0.03112  -0.09771 -0.10569 316 VAL   B C   
4213 O O   . VAL   B 223 ? 0.78118 0.87459 0.72990 0.02649  -0.09033 -0.09633 316 VAL   B O   
4214 C CB  . VAL   B 223 ? 1.00649 1.04535 0.93221 0.01052  -0.11984 -0.09671 316 VAL   B CB  
4215 C CG1 . VAL   B 223 ? 0.90849 0.93597 0.82843 -0.00128 -0.13019 -0.09451 316 VAL   B CG1 
4216 C CG2 . VAL   B 223 ? 0.76992 0.78200 0.68060 0.02367  -0.13002 -0.11016 316 VAL   B CG2 
4217 N N   . SER   B 224 ? 0.92035 1.00972 0.84004 0.04696  -0.09827 -0.12233 317 SER   B N   
4218 C CA  . SER   B 224 ? 0.92671 1.03438 0.85499 0.05993  -0.09048 -0.13116 317 SER   B CA  
4219 C C   . SER   B 224 ? 1.01172 1.15767 0.94055 0.06387  -0.07457 -0.13730 317 SER   B C   
4220 O O   . SER   B 224 ? 0.90793 1.07870 0.85066 0.06844  -0.06380 -0.14026 317 SER   B O   
4221 C CB  . SER   B 224 ? 0.85183 0.93619 0.76831 0.07774  -0.10446 -0.14878 317 SER   B CB  
4222 O OG  . SER   B 224 ? 0.98050 1.06286 0.87802 0.08744  -0.10937 -0.16397 317 SER   B OG  
4223 N N   . GLY   B 225 ? 0.89310 1.04430 0.80592 0.06098  -0.07283 -0.13941 318 GLY   B N   
4224 C CA  . GLY   B 225 ? 0.87871 1.06326 0.78616 0.06218  -0.05729 -0.14516 318 GLY   B CA  
4225 C C   . GLY   B 225 ? 1.15971 1.35895 1.05950 0.08017  -0.05578 -0.16877 318 GLY   B C   
4226 O O   . GLY   B 225 ? 1.22148 1.44971 1.11347 0.08003  -0.04213 -0.17579 318 GLY   B O   
4227 N N   . TYR   B 226 ? 0.98136 1.16097 0.88148 0.09561  -0.06953 -0.18189 319 TYR   B N   
4228 C CA  . TYR   B 226 ? 0.98218 1.17590 0.87729 0.11639  -0.07020 -0.20699 319 TYR   B CA  
4229 C C   . TYR   B 226 ? 1.21499 1.39047 1.08372 0.12333  -0.08038 -0.21941 319 TYR   B C   
4230 O O   . TYR   B 226 ? 1.05654 1.19363 0.91316 0.11873  -0.09611 -0.21313 319 TYR   B O   
4231 C CB  . TYR   B 226 ? 1.09929 1.27704 1.00526 0.13237  -0.08259 -0.21609 319 TYR   B CB  
4232 C CG  . TYR   B 226 ? 1.10331 1.29656 1.03405 0.12656  -0.07454 -0.20485 319 TYR   B CG  
4233 C CD1 . TYR   B 226 ? 1.11336 1.34774 1.05841 0.11564  -0.05397 -0.19836 319 TYR   B CD1 
4234 C CD2 . TYR   B 226 ? 1.07746 1.24146 1.01428 0.13087  -0.08793 -0.20048 319 TYR   B CD2 
4235 C CE1 . TYR   B 226 ? 1.09150 1.33898 1.05846 0.11010  -0.04732 -0.18881 319 TYR   B CE1 
4236 C CE2 . TYR   B 226 ? 1.16944 1.34688 1.12711 0.12580  -0.08112 -0.19073 319 TYR   B CE2 
4237 C CZ  . TYR   B 226 ? 0.99860 1.21854 0.97239 0.11585  -0.06099 -0.18537 319 TYR   B CZ  
4238 O OH  . TYR   B 226 ? 0.99901 1.23134 0.99289 0.11060  -0.05489 -0.17640 319 TYR   B OH  
4239 N N   . GLN   B 227 ? 1.07754 1.28222 0.93733 0.13343  -0.07086 -0.23791 320 GLN   B N   
4240 C CA  . GLN   B 227 ? 1.22275 1.41300 1.05600 0.14177  -0.07958 -0.25244 320 GLN   B CA  
4241 C C   . GLN   B 227 ? 1.19732 1.35505 1.02467 0.16300  -0.10049 -0.27022 320 GLN   B C   
4242 O O   . GLN   B 227 ? 1.25560 1.40889 1.09859 0.17421  -0.10623 -0.27472 320 GLN   B O   
4243 C CB  . GLN   B 227 ? 1.22182 1.45513 1.04617 0.14614  -0.06168 -0.26842 320 GLN   B CB  
4244 C CG  . GLN   B 227 ? 1.52921 1.75126 1.32184 0.14617  -0.06576 -0.27602 320 GLN   B CG  
4245 C CD  . GLN   B 227 ? 1.55927 1.82492 1.34086 0.15005  -0.04670 -0.29328 320 GLN   B CD  
4246 O OE1 . GLN   B 227 ? 1.54581 1.80731 1.29965 0.15113  -0.04771 -0.30197 320 GLN   B OE1 
4247 N NE2 . GLN   B 227 ? 1.55953 1.86843 1.36226 0.15105  -0.02886 -0.29895 320 GLN   B NE2 
4248 N N   . TRP   B 228 ? 1.02193 1.15344 0.82378 0.16857  -0.11338 -0.28038 321 TRP   B N   
4249 C CA  . TRP   B 228 ? 1.16108 1.25502 0.95139 0.18850  -0.13513 -0.29790 321 TRP   B CA  
4250 C C   . TRP   B 228 ? 1.29960 1.41966 1.09798 0.21528  -0.13263 -0.32473 321 TRP   B C   
4251 O O   . TRP   B 228 ? 1.31780 1.41015 1.11669 0.23307  -0.14976 -0.33548 321 TRP   B O   
4252 C CB  . TRP   B 228 ? 1.05281 1.11759 0.81300 0.18889  -0.14796 -0.30552 321 TRP   B CB  
4253 C CG  . TRP   B 228 ? 1.08914 1.12016 0.83291 0.21265  -0.16841 -0.32907 321 TRP   B CG  
4254 C CD1 . TRP   B 228 ? 1.21348 1.25525 0.94140 0.23391  -0.16982 -0.35667 321 TRP   B CD1 
4255 C CD2 . TRP   B 228 ? 1.09387 1.07251 0.83301 0.21792  -0.19093 -0.32772 321 TRP   B CD2 
4256 N NE1 . TRP   B 228 ? 1.32050 1.31815 1.03471 0.25383  -0.19328 -0.37311 321 TRP   B NE1 
4257 C CE2 . TRP   B 228 ? 1.23729 1.19353 0.95645 0.24364  -0.20685 -0.35498 321 TRP   B CE2 
4258 C CE3 . TRP   B 228 ? 1.06225 1.00945 0.80989 0.20274  -0.19909 -0.30637 321 TRP   B CE3 
4259 C CZ2 . TRP   B 228 ? 1.24276 1.14184 0.94796 0.25437  -0.23191 -0.36036 321 TRP   B CZ2 
4260 C CZ3 . TRP   B 228 ? 1.27206 1.16477 1.00545 0.21146  -0.22227 -0.31130 321 TRP   B CZ3 
4261 C CH2 . TRP   B 228 ? 1.34676 1.21363 1.05805 0.23696  -0.23912 -0.33754 321 TRP   B CH2 
4262 N N   . CYS   B 229 ? 1.34633 1.51942 1.15027 0.21833  -0.11197 -0.33641 322 CYS   B N   
4263 C CA  . CYS   B 229 ? 1.34519 1.55193 1.16056 0.24391  -0.10817 -0.36479 322 CYS   B CA  
4264 C C   . CYS   B 229 ? 1.20278 1.42227 1.04799 0.24932  -0.10743 -0.36147 322 CYS   B C   
4265 O O   . CYS   B 229 ? 1.30223 1.53014 1.15678 0.27518  -0.11548 -0.38457 322 CYS   B O   
4266 C CB  . CYS   B 229 ? 1.27070 1.53551 1.08538 0.24098  -0.08330 -0.37692 322 CYS   B CB  
4267 S SG  . CYS   B 229 ? 1.31210 1.61585 1.14158 0.20855  -0.05569 -0.34926 322 CYS   B SG  
4268 N N   . ASP   B 230 ? 1.15203 1.37283 1.01198 0.22664  -0.09905 -0.33417 323 ASP   B N   
4269 C CA  . ASP   B 230 ? 1.35803 1.59113 1.24514 0.23024  -0.09796 -0.33013 323 ASP   B CA  
4270 C C   . ASP   B 230 ? 1.24610 1.42538 1.12803 0.24363  -0.12416 -0.33019 323 ASP   B C   
4271 O O   . ASP   B 230 ? 1.15793 1.34410 1.05554 0.26071  -0.13029 -0.34070 323 ASP   B O   
4272 C CB  . ASP   B 230 ? 1.02034 1.26692 0.92191 0.20215  -0.08217 -0.30129 323 ASP   B CB  
4273 C CG  . ASP   B 230 ? 1.19859 1.49288 1.10127 0.18703  -0.05694 -0.29923 323 ASP   B CG  
4274 O OD1 . ASP   B 230 ? 1.43607 1.76787 1.33787 0.19909  -0.04714 -0.32243 323 ASP   B OD1 
4275 O OD2 . ASP   B 230 ? 1.16115 1.45464 1.06414 0.16296  -0.04710 -0.27488 323 ASP   B OD2 
4276 N N   . ILE   B 231 ? 1.10688 1.23168 0.96557 0.23543  -0.14038 -0.31885 324 ILE   B N   
4277 C CA  . ILE   B 231 ? 1.11111 1.17844 0.95965 0.24204  -0.16455 -0.31495 324 ILE   B CA  
4278 C C   . ILE   B 231 ? 1.22847 1.25692 1.05094 0.26515  -0.18682 -0.33763 324 ILE   B C   
4279 O O   . ILE   B 231 ? 1.15973 1.13507 0.96839 0.27292  -0.20913 -0.33715 324 ILE   B O   
4280 C CB  . ILE   B 231 ? 1.05671 1.08729 0.89861 0.21362  -0.16794 -0.28532 324 ILE   B CB  
4281 C CG1 . ILE   B 231 ? 1.18324 1.18927 1.00083 0.20397  -0.17413 -0.28406 324 ILE   B CG1 
4282 C CG2 . ILE   B 231 ? 0.92651 0.99540 0.79220 0.19167  -0.14600 -0.26412 324 ILE   B CG2 
4283 C CD1 . ILE   B 231 ? 1.13861 1.10477 0.94896 0.17903  -0.18207 -0.25997 324 ILE   B CD1 
4284 N N   . GLU   B 232 ? 1.12613 1.17684 0.93869 0.27602  -0.18183 -0.35765 325 GLU   B N   
4285 C CA  . GLU   B 232 ? 1.27407 1.28614 1.05992 0.29848  -0.20353 -0.38041 325 GLU   B CA  
4286 C C   . GLU   B 232 ? 1.11951 1.11663 0.90845 0.32950  -0.22123 -0.40068 325 GLU   B C   
4287 O O   . GLU   B 232 ? 1.22240 1.15819 0.98680 0.34157  -0.24741 -0.40649 325 GLU   B O   
4288 C CB  . GLU   B 232 ? 1.24036 1.28871 1.01773 0.30683  -0.19208 -0.40114 325 GLU   B CB  
4289 C CG  . GLU   B 232 ? 1.23925 1.25077 0.98899 0.33246  -0.21404 -0.42783 325 GLU   B CG  
4290 C CD  . GLU   B 232 ? 1.26914 1.31939 1.00968 0.34112  -0.20144 -0.44977 325 GLU   B CD  
4291 O OE1 . GLU   B 232 ? 1.29119 1.39536 1.04476 0.32549  -0.17534 -0.44295 325 GLU   B OE1 
4292 O OE2 . GLU   B 232 ? 1.53018 1.55475 1.24793 0.36316  -0.21791 -0.47397 325 GLU   B OE2 
4293 N N   . ASN   B 233 ? 1.13674 1.18797 0.95456 0.34262  -0.20842 -0.41209 326 ASN   B N   
4294 C CA  . ASN   B 233 ? 1.07879 1.11904 0.90240 0.37337  -0.22645 -0.43139 326 ASN   B CA  
4295 C C   . ASN   B 233 ? 1.18455 1.16770 1.00078 0.36481  -0.24407 -0.40936 326 ASN   B C   
4296 O O   . ASN   B 233 ? 1.14638 1.07809 0.94394 0.38615  -0.27085 -0.41993 326 ASN   B O   
4297 C CB  . ASN   B 233 ? 1.30380 1.42060 1.16406 0.38545  -0.20736 -0.44706 326 ASN   B CB  
4298 C CG  . ASN   B 233 ? 1.37292 1.48929 1.24003 0.42443  -0.22672 -0.47651 326 ASN   B CG  
4299 O OD1 . ASN   B 233 ? 1.30443 1.37450 1.14643 0.44852  -0.25145 -0.49448 326 ASN   B OD1 
4300 N ND2 . ASN   B 233 ? 1.32781 1.49484 1.22857 0.43145  -0.21687 -0.48237 326 ASN   B ND2 
4301 N N   . CYS   B 234 ? 1.09329 1.08258 0.92144 0.33357  -0.22978 -0.37888 327 CYS   B N   
4302 C CA  . CYS   B 234 ? 1.03642 0.97365 0.85610 0.32171  -0.24379 -0.35675 327 CYS   B CA  
4303 C C   . CYS   B 234 ? 1.17748 1.04119 0.96051 0.31085  -0.26374 -0.34707 327 CYS   B C   
4304 O O   . CYS   B 234 ? 1.13038 0.93425 0.89249 0.31580  -0.28635 -0.34331 327 CYS   B O   
4305 C CB  . CYS   B 234 ? 1.09954 1.06747 0.94287 0.29177  -0.22183 -0.32894 327 CYS   B CB  
4306 S SG  . CYS   B 234 ? 1.04136 0.95429 0.87642 0.27447  -0.23448 -0.30149 327 CYS   B SG  
4307 N N   . VAL   B 235 ? 1.14776 1.01368 0.92087 0.29493  -0.25624 -0.34293 328 VAL   B N   
4308 C CA  . VAL   B 235 ? 1.03877 0.83896 0.77859 0.28296  -0.27478 -0.33551 328 VAL   B CA  
4309 C C   . VAL   B 235 ? 1.22311 0.97417 0.93409 0.31294  -0.30229 -0.36049 328 VAL   B C   
4310 O O   . VAL   B 235 ? 1.30889 0.99023 0.99154 0.30983  -0.32518 -0.35426 328 VAL   B O   
4311 C CB  . VAL   B 235 ? 1.33169 1.15027 1.06841 0.26302  -0.26192 -0.32945 328 VAL   B CB  
4312 C CG1 . VAL   B 235 ? 1.28310 1.03845 0.98453 0.25788  -0.28353 -0.33141 328 VAL   B CG1 
4313 C CG2 . VAL   B 235 ? 1.14950 0.99453 0.90694 0.23064  -0.24211 -0.30056 328 VAL   B CG2 
4314 N N   . LYS   B 236 ? 1.29108 1.07710 1.00755 0.34227  -0.30058 -0.38982 329 LYS   B N   
4315 C CA  . LYS   B 236 ? 1.37302 1.11507 1.06326 0.37505  -0.32753 -0.41690 329 LYS   B CA  
4316 C C   . LYS   B 236 ? 1.25007 0.95508 0.93561 0.39327  -0.34793 -0.41887 329 LYS   B C   
4317 O O   . LYS   B 236 ? 1.36640 1.00175 1.01801 0.40858  -0.37703 -0.42788 329 LYS   B O   
4318 C CB  . LYS   B 236 ? 1.50177 1.29906 1.20370 0.40364  -0.31879 -0.44984 329 LYS   B CB  
4319 C CG  . LYS   B 236 ? 1.61539 1.36838 1.28847 0.43746  -0.34620 -0.47964 329 LYS   B CG  
4320 C CD  . LYS   B 236 ? 1.65648 1.47661 1.34989 0.45862  -0.33205 -0.50374 329 LYS   B CD  
4321 C CE  . LYS   B 236 ? 1.64227 1.53233 1.37601 0.47562  -0.31802 -0.51503 329 LYS   B CE  
4322 N NZ  . LYS   B 236 ? 1.63272 1.58897 1.38656 0.49394  -0.30485 -0.53875 329 LYS   B NZ  
4323 N N   . TRP   B 237 ? 1.28373 1.03102 1.00025 0.39179  -0.33441 -0.41054 330 TRP   B N   
4324 C CA  . TRP   B 237 ? 1.28403 0.99402 0.99437 0.40614  -0.35411 -0.40912 330 TRP   B CA  
4325 C C   . TRP   B 237 ? 1.43671 1.07579 1.11981 0.37711  -0.36581 -0.37891 330 TRP   B C   
4326 O O   . TRP   B 237 ? 1.47882 1.05017 1.13184 0.38852  -0.39294 -0.37986 330 TRP   B O   
4327 C CB  . TRP   B 237 ? 1.17545 0.95292 0.92713 0.41107  -0.33595 -0.40897 330 TRP   B CB  
4328 C CG  . TRP   B 237 ? 1.44650 1.18718 1.19239 0.41965  -0.35394 -0.40187 330 TRP   B CG  
4329 C CD1 . TRP   B 237 ? 1.46348 1.18565 1.20285 0.45716  -0.37803 -0.42504 330 TRP   B CD1 
4330 C CD2 . TRP   B 237 ? 1.37370 1.09076 1.11791 0.39081  -0.35018 -0.37008 330 TRP   B CD2 
4331 N NE1 . TRP   B 237 ? 1.43814 1.12401 1.16959 0.45290  -0.39015 -0.40847 330 TRP   B NE1 
4332 C CE2 . TRP   B 237 ? 1.46032 1.14302 1.19433 0.41172  -0.37248 -0.37472 330 TRP   B CE2 
4333 C CE3 . TRP   B 237 ? 1.34513 1.06734 1.09513 0.35041  -0.33070 -0.33928 330 TRP   B CE3 
4334 C CZ2 . TRP   B 237 ? 1.48056 1.13354 1.20792 0.39192  -0.37459 -0.34891 330 TRP   B CZ2 
4335 C CZ3 . TRP   B 237 ? 1.26737 0.96306 1.01361 0.33167  -0.33226 -0.31508 330 TRP   B CZ3 
4336 C CH2 . TRP   B 237 ? 1.23195 0.89302 0.96591 0.35155  -0.35345 -0.31961 330 TRP   B CH2 
4337 N N   . MET   B 238 ? 1.32771 0.98101 1.01969 0.33938  -0.34597 -0.35253 331 MET   B N   
4338 C CA  . MET   B 238 ? 1.23990 0.83560 0.91001 0.30812  -0.35312 -0.32442 331 MET   B CA  
4339 C C   . MET   B 238 ? 1.41890 0.94488 1.04776 0.30078  -0.37368 -0.32583 331 MET   B C   
4340 O O   . MET   B 238 ? 1.37601 0.84707 0.98167 0.27506  -0.38260 -0.30517 331 MET   B O   
4341 C CB  . MET   B 238 ? 1.20096 0.84276 0.89880 0.27267  -0.32463 -0.29873 331 MET   B CB  
4342 C CG  . MET   B 238 ? 1.26762 0.86872 0.95430 0.24088  -0.32641 -0.26976 331 MET   B CG  
4343 S SD  . MET   B 238 ? 1.14713 0.81033 0.87160 0.20636  -0.29340 -0.24391 331 MET   B SD  
4344 C CE  . MET   B 238 ? 1.07314 0.79430 0.83237 0.22527  -0.27988 -0.24904 331 MET   B CE  
4345 N N   . VAL   B 239 ? 1.46975 0.99696 1.08830 0.32190  -0.38116 -0.35038 332 VAL   B N   
4346 C CA  . VAL   B 239 ? 1.57892 1.04376 1.15899 0.31584  -0.40032 -0.35453 332 VAL   B CA  
4347 C C   . VAL   B 239 ? 1.49241 0.86483 1.03010 0.31516  -0.43032 -0.34854 332 VAL   B C   
4348 O O   . VAL   B 239 ? 1.60445 0.92778 1.11835 0.28380  -0.43628 -0.33010 332 VAL   B O   
4349 C CB  . VAL   B 239 ? 1.48340 0.96466 1.05832 0.34701  -0.40593 -0.38705 332 VAL   B CB  
4350 C CG1 . VAL   B 239 ? 1.46723 0.86671 0.99583 0.35431  -0.43612 -0.39697 332 VAL   B CG1 
4351 C CG2 . VAL   B 239 ? 1.47417 1.01973 1.07215 0.33225  -0.37973 -0.38594 332 VAL   B CG2 
4352 N N   . PRO   B 240 ? 1.63605 0.98034 1.16130 0.34729  -0.45040 -0.36320 333 PRO   B N   
4353 C CA  . PRO   B 240 ? 1.70346 0.96013 1.18664 0.34247  -0.47744 -0.35039 333 PRO   B CA  
4354 C C   . PRO   B 240 ? 1.66699 0.89094 1.13975 0.30695  -0.47401 -0.32251 333 PRO   B C   
4355 O O   . PRO   B 240 ? 1.61948 0.77331 1.05514 0.28344  -0.48837 -0.30585 333 PRO   B O   
4356 C CB  . PRO   B 240 ? 1.87710 1.13922 1.36456 0.38356  -0.49285 -0.36471 333 PRO   B CB  
4357 C CG  . PRO   B 240 ? 1.73896 1.08310 1.26508 0.41123  -0.47728 -0.39092 333 PRO   B CG  
4358 C CD  . PRO   B 240 ? 1.65697 1.05339 1.20889 0.38689  -0.44826 -0.38697 333 PRO   B CD  
4359 N N   . PHE   B 241 ? 1.62048 0.90849 1.13322 0.29807  -0.44957 -0.30941 334 PHE   B N   
4360 C CA  . PHE   B 241 ? 1.70865 0.97985 1.21905 0.26342  -0.44156 -0.27894 334 PHE   B CA  
4361 C C   . PHE   B 241 ? 1.49025 0.75707 0.99852 0.22031  -0.42871 -0.25890 334 PHE   B C   
4362 O O   . PHE   B 241 ? 1.50279 0.72097 0.98743 0.18990  -0.43333 -0.23784 334 PHE   B O   
4363 C CB  . PHE   B 241 ? 1.35488 0.69957 0.91037 0.26558  -0.41798 -0.27194 334 PHE   B CB  
4364 C CG  . PHE   B 241 ? 1.52532 0.88956 1.09165 0.30788  -0.42790 -0.29408 334 PHE   B CG  
4365 C CD1 . PHE   B 241 ? 1.61970 0.93437 1.16230 0.32088  -0.44892 -0.29192 334 PHE   B CD1 
4366 C CD2 . PHE   B 241 ? 1.56593 0.99958 1.16586 0.33411  -0.41627 -0.31767 334 PHE   B CD2 
4367 C CE1 . PHE   B 241 ? 1.64102 0.97679 1.19608 0.36128  -0.45966 -0.31399 334 PHE   B CE1 
4368 C CE2 . PHE   B 241 ? 1.61034 1.06830 1.22409 0.37261  -0.42487 -0.34020 334 PHE   B CE2 
4369 C CZ  . PHE   B 241 ? 1.59406 1.00405 1.18689 0.38718  -0.44730 -0.33887 334 PHE   B CZ  
4370 N N   . ALA   B 242 ? 1.41662 0.73467 0.94871 0.21682  -0.41278 -0.26584 335 ALA   B N   
4371 C CA  . ALA   B 242 ? 1.53808 0.86056 1.07337 0.17792  -0.40059 -0.24852 335 ALA   B CA  
4372 C C   . ALA   B 242 ? 1.54006 0.78014 1.02830 0.16289  -0.42436 -0.24789 335 ALA   B C   
4373 O O   . ALA   B 242 ? 1.50467 0.72035 0.98330 0.12534  -0.42149 -0.22761 335 ALA   B O   
4374 C CB  . ALA   B 242 ? 1.35765 0.75042 0.92513 0.18104  -0.38088 -0.25760 335 ALA   B CB  
4375 N N   . MET   B 243 ? 1.45413 0.65087 0.91252 0.19118  -0.44804 -0.27084 336 MET   B N   
4376 C CA  . MET   B 243 ? 1.61691 0.73263 1.02833 0.17696  -0.47170 -0.27175 336 MET   B CA  
4377 C C   . MET   B 243 ? 1.72668 0.76914 1.10168 0.16098  -0.48745 -0.25342 336 MET   B C   
4378 O O   . MET   B 243 ? 1.68976 0.68756 1.04024 0.12738  -0.49233 -0.23706 336 MET   B O   
4379 C CB  . MET   B 243 ? 1.69177 0.79428 1.08899 0.21243  -0.48790 -0.29560 336 MET   B CB  
4380 C CG  . MET   B 243 ? 1.88955 1.02998 1.30013 0.21099  -0.47881 -0.30910 336 MET   B CG  
4381 S SD  . MET   B 243 ? 2.11414 1.22745 1.51117 0.16004  -0.47705 -0.29094 336 MET   B SD  
4382 C CE  . MET   B 243 ? 1.56654 0.77735 1.01870 0.13965  -0.44149 -0.27794 336 MET   B CE  
4383 N N   . VAL   B 244 ? 1.76749 0.80363 1.14090 0.18357  -0.49337 -0.25355 337 VAL   B N   
4384 C CA  . VAL   B 244 ? 1.73131 0.70484 1.07053 0.16791  -0.50577 -0.23248 337 VAL   B CA  
4385 C C   . VAL   B 244 ? 1.85984 0.83108 1.20154 0.11946  -0.48996 -0.20883 337 VAL   B C   
4386 O O   . VAL   B 244 ? 1.90134 0.81864 1.21023 0.08950  -0.49650 -0.18889 337 VAL   B O   
4387 C CB  . VAL   B 244 ? 1.98892 0.96609 1.33081 0.20191  -0.51392 -0.23798 337 VAL   B CB  
4388 C CG1 . VAL   B 244 ? 1.93913 0.85231 1.24225 0.18438  -0.52651 -0.21508 337 VAL   B CG1 
4389 C CG2 . VAL   B 244 ? 1.86525 0.84696 1.20560 0.24862  -0.53092 -0.26181 337 VAL   B CG2 
4390 N N   . ILE   B 245 ? 1.72374 0.77716 1.11559 0.10994  -0.46127 -0.20331 338 ILE   B N   
4391 C CA  . ILE   B 245 ? 1.68423 0.75920 1.09173 0.06482  -0.44030 -0.17829 338 ILE   B CA  
4392 C C   . ILE   B 245 ? 1.65718 0.71679 1.05518 0.03460  -0.44107 -0.17613 338 ILE   B C   
4393 O O   . ILE   B 245 ? 1.80319 0.83540 1.18678 -0.00548 -0.43829 -0.15828 338 ILE   B O   
4394 C CB  . ILE   B 245 ? 1.59467 0.76606 1.06073 0.06617  -0.40937 -0.17241 338 ILE   B CB  
4395 C CG1 . ILE   B 245 ? 1.57887 0.76489 1.05419 0.09478  -0.40964 -0.17537 338 ILE   B CG1 
4396 C CG2 . ILE   B 245 ? 1.64389 0.83966 1.12777 0.02224  -0.38846 -0.14867 338 ILE   B CG2 
4397 C CD1 . ILE   B 245 ? 1.75032 0.87791 1.19234 0.08083  -0.41998 -0.15908 338 ILE   B CD1 
4398 N N   . ARG   B 246 ? 1.50415 0.58235 0.90975 0.05264  -0.44486 -0.19518 339 ARG   B N   
4399 C CA  . ARG   B 246 ? 1.62728 0.69296 1.02466 0.02606  -0.44716 -0.19522 339 ARG   B CA  
4400 C C   . ARG   B 246 ? 1.76904 0.74331 1.11208 0.01327  -0.47231 -0.19293 339 ARG   B C   
4401 O O   . ARG   B 246 ? 1.69038 0.65013 1.02574 -0.02320 -0.47011 -0.18164 339 ARG   B O   
4402 C CB  . ARG   B 246 ? 1.71207 0.82280 1.12998 0.05050  -0.44426 -0.21612 339 ARG   B CB  
4403 C CG  . ARG   B 246 ? 1.55487 0.76261 1.02817 0.05301  -0.41480 -0.21282 339 ARG   B CG  
4404 C CD  . ARG   B 246 ? 1.40616 0.64612 0.90224 0.01188  -0.39774 -0.19475 339 ARG   B CD  
4405 N NE  . ARG   B 246 ? 1.48748 0.81367 1.03169 0.01609  -0.37262 -0.19273 339 ARG   B NE  
4406 C CZ  . ARG   B 246 ? 1.38205 0.75131 0.95503 -0.01263 -0.35523 -0.17830 339 ARG   B CZ  
4407 N NH1 . ARG   B 246 ? 1.39927 0.74134 0.96259 -0.04897 -0.35795 -0.16532 339 ARG   B NH1 
4408 N NH2 . ARG   B 246 ? 1.34749 0.78880 0.95927 -0.00492 -0.33495 -0.17754 339 ARG   B NH2 
4409 N N   . GLU   B 247 ? 1.86088 0.79176 1.17575 0.04366  -0.49035 -0.19792 340 GLU   B N   
4410 C CA  . GLU   B 247 ? 1.82893 0.68834 1.09813 0.03446  -0.50949 -0.18944 340 GLU   B CA  
4411 C C   . GLU   B 247 ? 1.86214 0.68554 1.10950 -0.00727 -0.50555 -0.16282 340 GLU   B C   
4412 O O   . GLU   B 247 ? 1.93502 0.71824 1.15523 -0.03647 -0.51113 -0.15202 340 GLU   B O   
4413 C CB  . GLU   B 247 ? 1.98891 0.81365 1.23356 0.07890  -0.53155 -0.20139 340 GLU   B CB  
4414 C CG  . GLU   B 247 ? 2.03446 0.88684 1.29337 0.11813  -0.53758 -0.22820 340 GLU   B CG  
4415 C CD  . GLU   B 247 ? 2.26410 1.08316 1.49928 0.16082  -0.56096 -0.24022 340 GLU   B CD  
4416 O OE1 . GLU   B 247 ? 2.49912 1.26040 1.69736 0.15663  -0.57686 -0.22647 340 GLU   B OE1 
4417 O OE2 . GLU   B 247 ? 2.22287 1.07572 1.47586 0.19827  -0.56358 -0.26373 340 GLU   B OE2 
4418 N N   . THR   B 248 ? 1.79126 0.63015 1.04962 -0.01128 -0.49519 -0.15245 341 THR   B N   
4419 C CA  . THR   B 248 ? 1.84144 0.65158 1.07953 -0.05014 -0.48903 -0.12745 341 THR   B CA  
4420 C C   . THR   B 248 ? 1.99257 0.85088 1.26425 -0.09212 -0.46405 -0.11640 341 THR   B C   
4421 O O   . THR   B 248 ? 2.02863 0.86973 1.28614 -0.13028 -0.45600 -0.09637 341 THR   B O   
4422 C CB  . THR   B 248 ? 1.85070 0.64684 1.07784 -0.03225 -0.49278 -0.12105 341 THR   B CB  
4423 O OG1 . THR   B 248 ? 2.25450 1.02125 1.45728 -0.07091 -0.48643 -0.09658 341 THR   B OG1 
4424 C CG2 . THR   B 248 ? 1.96420 0.82576 1.23832 -0.01485 -0.47689 -0.13045 341 THR   B CG2 
4425 N N   . GLY   B 249 ? 2.12170 1.04211 1.43673 -0.08596 -0.45180 -0.12933 342 GLY   B N   
4426 C CA  . GLY   B 249 ? 2.02360 0.99735 1.37469 -0.12206 -0.42922 -0.11974 342 GLY   B CA  
4427 C C   . GLY   B 249 ? 2.05346 1.08946 1.44319 -0.11632 -0.40606 -0.10869 342 GLY   B C   
4428 O O   . GLY   B 249 ? 1.99366 1.02495 1.37948 -0.08619 -0.41035 -0.11155 342 GLY   B O   
4429 N N   . SER   B 250 ? 1.90303 0.99942 1.33160 -0.14571 -0.38174 -0.09681 343 SER   B N   
4430 C CA  . SER   B 250 ? 1.75004 0.90951 1.21811 -0.14467 -0.35795 -0.08592 343 SER   B CA  
4431 C C   . SER   B 250 ? 1.78367 0.92462 1.23897 -0.18489 -0.34873 -0.06608 343 SER   B C   
4432 O O   . SER   B 250 ? 1.81660 0.92399 1.25037 -0.22125 -0.35251 -0.06032 343 SER   B O   
4433 C CB  . SER   B 250 ? 1.41875 0.66777 0.94408 -0.14270 -0.33641 -0.08906 343 SER   B CB  
4434 O OG  . SER   B 250 ? 1.83384 1.09357 1.36758 -0.17709 -0.33192 -0.08581 343 SER   B OG  
4435 N N   . SER   B 251 ? 1.86927 1.03374 1.33775 -0.17917 -0.33604 -0.05637 344 SER   B N   
4436 C CA  . SER   B 251 ? 1.72818 0.87662 1.18280 -0.21462 -0.32612 -0.03816 344 SER   B CA  
4437 C C   . SER   B 251 ? 1.70783 0.93021 1.21057 -0.24370 -0.29932 -0.03057 344 SER   B C   
4438 O O   . SER   B 251 ? 1.49174 0.78116 1.04086 -0.23129 -0.28774 -0.03779 344 SER   B O   
4439 C CB  . SER   B 251 ? 1.76300 0.90308 1.20888 -0.19550 -0.32522 -0.03175 344 SER   B CB  
4440 O OG  . SER   B 251 ? 1.83972 0.90911 1.23973 -0.16814 -0.35220 -0.03942 344 SER   B OG  
4441 N N   . LYS   B 252 ? 1.64834 0.85687 1.13780 -0.28272 -0.28999 -0.01639 345 LYS   B N   
4442 C CA  . LYS   B 252 ? 1.59612 0.87278 1.12932 -0.31157 -0.26495 -0.00982 345 LYS   B CA  
4443 C C   . LYS   B 252 ? 1.50204 0.82747 1.06434 -0.30162 -0.24555 -0.00197 345 LYS   B C   
4444 O O   . LYS   B 252 ? 1.39454 0.69139 0.93529 -0.28170 -0.25147 0.00143  345 LYS   B O   
4445 C CB  . LYS   B 252 ? 1.69243 0.93484 1.19841 -0.36162 -0.26289 -0.00044 345 LYS   B CB  
4446 C CG  . LYS   B 252 ? 1.80892 1.00632 1.28842 -0.37814 -0.28059 -0.00785 345 LYS   B CG  
4447 C CD  . LYS   B 252 ? 1.56680 0.83159 1.09617 -0.38151 -0.27236 -0.01795 345 LYS   B CD  
4448 C CE  . LYS   B 252 ? 1.76533 0.99175 1.27087 -0.40038 -0.28734 -0.02434 345 LYS   B CE  
4449 N NZ  . LYS   B 252 ? 1.64130 0.92873 1.19229 -0.40953 -0.28183 -0.03461 345 LYS   B NZ  
4450 N N   . LEU   B 253 ? 1.38763 0.78700 0.99928 -0.31509 -0.22340 -0.00000 346 LEU   B N   
4451 C CA  . LEU   B 253 ? 1.27317 0.72131 0.91421 -0.30975 -0.20373 0.00721  346 LEU   B CA  
4452 C C   . LEU   B 253 ? 1.38621 0.80385 0.99824 -0.34207 -0.19652 0.02068  346 LEU   B C   
4453 O O   . LEU   B 253 ? 1.49311 0.90234 1.09584 -0.38089 -0.19169 0.02465  346 LEU   B O   
4454 C CB  . LEU   B 253 ? 1.22657 0.75938 0.92705 -0.31300 -0.18450 0.00386  346 LEU   B CB  
4455 C CG  . LEU   B 253 ? 1.30406 0.89081 1.03786 -0.31067 -0.16318 0.01053  346 LEU   B CG  
4456 C CD1 . LEU   B 253 ? 1.20305 0.78935 0.93694 -0.27303 -0.16602 0.00976  346 LEU   B CD1 
4457 C CD2 . LEU   B 253 ? 1.14614 0.80938 0.93452 -0.31502 -0.14767 0.00616  346 LEU   B CD2 
4458 N N   . LYS   B 254 ? 1.48843 0.89083 1.08570 -0.32710 -0.19555 0.02717  347 LYS   B N   
4459 C CA  . LYS   B 254 ? 1.45869 0.82625 1.02167 -0.35486 -0.19000 0.04030  347 LYS   B CA  
4460 C C   . LYS   B 254 ? 1.53667 0.97244 1.14027 -0.36936 -0.16286 0.04573  347 LYS   B C   
4461 O O   . LYS   B 254 ? 1.44895 0.95246 1.10378 -0.34993 -0.15083 0.04024  347 LYS   B O   
4462 C CB  . LYS   B 254 ? 1.41797 0.72642 0.93779 -0.33086 -0.20615 0.04412  347 LYS   B CB  
4463 C CG  . LYS   B 254 ? 1.42454 0.65042 0.89182 -0.32102 -0.23511 0.03998  347 LYS   B CG  
4464 C CD  . LYS   B 254 ? 1.57475 0.74239 0.99834 -0.29890 -0.25156 0.04404  347 LYS   B CD  
4465 C CE  . LYS   B 254 ? 1.85040 0.92828 1.21619 -0.29000 -0.28245 0.03993  347 LYS   B CE  
4466 N NZ  . LYS   B 254 ? 1.72921 0.74691 1.04960 -0.26845 -0.30085 0.04367  347 LYS   B NZ  
4467 N N   . HIS   B 255 ? 1.66724 1.08200 1.24460 -0.40449 -0.15354 0.05636  348 HIS   B N   
4468 C CA  . HIS   B 255 ? 1.62076 1.09020 1.22701 -0.41905 -0.12868 0.06160  348 HIS   B CA  
4469 C C   . HIS   B 255 ? 1.63869 1.06711 1.20584 -0.41556 -0.13000 0.07203  348 HIS   B C   
4470 O O   . HIS   B 255 ? 1.64347 0.99470 1.15069 -0.42774 -0.14484 0.07931  348 HIS   B O   
4471 C CB  . HIS   B 255 ? 1.74552 1.23633 1.35850 -0.46628 -0.11288 0.06354  348 HIS   B CB  
4472 C CG  . HIS   B 255 ? 1.83244 1.36856 1.46300 -0.48171 -0.08814 0.06876  348 HIS   B CG  
4473 N ND1 . HIS   B 255 ? 1.81772 1.42669 1.50257 -0.46750 -0.07190 0.06426  348 HIS   B ND1 
4474 C CD2 . HIS   B 255 ? 1.78439 1.30948 1.38683 -0.50155 -0.07652 0.07620  348 HIS   B CD2 
4475 C CE1 . HIS   B 255 ? 1.73473 1.36838 1.42196 -0.48506 -0.05232 0.06898  348 HIS   B CE1 
4476 N NE2 . HIS   B 255 ? 1.69152 1.27840 1.33032 -0.50314 -0.05418 0.07561  348 HIS   B NE2 
4477 N N   . PHE   B 256 ? 1.68123 1.15857 1.28010 -0.39873 -0.11576 0.07265  349 PHE   B N   
4478 C CA  . PHE   B 256 ? 1.71404 1.16149 1.28174 -0.39270 -0.11615 0.08139  349 PHE   B CA  
4479 C C   . PHE   B 256 ? 1.60128 1.09717 1.18986 -0.41674 -0.08977 0.08621  349 PHE   B C   
4480 O O   . PHE   B 256 ? 1.40674 0.97685 1.05174 -0.40948 -0.07319 0.07984  349 PHE   B O   
4481 C CB  . PHE   B 256 ? 1.61019 1.06747 1.19357 -0.34586 -0.12602 0.07613  349 PHE   B CB  
4482 C CG  . PHE   B 256 ? 1.46492 0.88264 1.03247 -0.31872 -0.15082 0.06852  349 PHE   B CG  
4483 C CD1 . PHE   B 256 ? 1.51258 0.85060 1.02241 -0.31034 -0.17406 0.07185  349 PHE   B CD1 
4484 C CD2 . PHE   B 256 ? 1.49410 0.95331 1.10274 -0.30074 -0.15164 0.05729  349 PHE   B CD2 
4485 C CE1 . PHE   B 256 ? 1.42961 0.73272 0.92578 -0.28334 -0.19734 0.06267  349 PHE   B CE1 
4486 C CE2 . PHE   B 256 ? 1.41202 0.83713 1.00585 -0.27555 -0.17345 0.04876  349 PHE   B CE2 
4487 C CZ  . PHE   B 256 ? 1.55288 0.90123 1.09184 -0.26625 -0.19617 0.05073  349 PHE   B CZ  
4488 N N   . ARG   B 257 ? 1.72014 1.17224 1.26100 -0.44514 -0.08644 0.09699  350 ARG   B N   
4489 C CA  . ARG   B 257 ? 1.54166 1.04089 1.09918 -0.46514 -0.06080 0.09986  350 ARG   B CA  
4490 C C   . ARG   B 257 ? 1.44905 0.98570 1.03533 -0.43745 -0.05366 0.09884  350 ARG   B C   
4491 O O   . ARG   B 257 ? 1.39500 0.89732 0.96025 -0.40844 -0.06918 0.10089  350 ARG   B O   
4492 C CB  . ARG   B 257 ? 1.77815 1.23306 1.27984 -0.48437 -0.05987 0.10797  350 ARG   B CB  
4493 C CG  . ARG   B 257 ? 1.86315 1.30974 1.34961 -0.51132 -0.05801 0.10635  350 ARG   B CG  
4494 C CD  . ARG   B 257 ? 2.04988 1.45423 1.47953 -0.53266 -0.05606 0.11434  350 ARG   B CD  
4495 N NE  . ARG   B 257 ? 2.12381 1.43883 1.48850 -0.52246 -0.08299 0.12196  350 ARG   B NE  
4496 C CZ  . ARG   B 257 ? 2.14796 1.42203 1.47939 -0.50458 -0.09429 0.12830  350 ARG   B CZ  
4497 N NH1 . ARG   B 257 ? 1.96464 1.27646 1.31948 -0.49634 -0.08049 0.12902  350 ARG   B NH1 
4498 N NH2 . ARG   B 257 ? 2.10413 1.29748 1.37726 -0.49345 -0.12115 0.13325  350 ARG   B NH2 
4499 N N   . GLY   B 258 ? 1.30961 0.92134 0.94675 -0.44285 -0.03065 0.09374  351 GLY   B N   
4500 C CA  . GLY   B 258 ? 1.32456 0.98152 0.99665 -0.41428 -0.02265 0.09054  351 GLY   B CA  
4501 C C   . GLY   B 258 ? 1.35888 1.05741 1.08001 -0.37882 -0.02829 0.08088  351 GLY   B C   
4502 O O   . GLY   B 258 ? 1.33691 1.08192 1.09412 -0.35857 -0.01907 0.07722  351 GLY   B O   
4503 N N   . VAL   B 259 ? 1.32487 1.00635 1.04600 -0.37165 -0.04309 0.07662  352 VAL   B N   
4504 C CA  . VAL   B 259 ? 1.28703 1.00462 1.04977 -0.34041 -0.04867 0.06745  352 VAL   B CA  
4505 C C   . VAL   B 259 ? 1.10593 0.86942 0.90615 -0.35583 -0.03995 0.06059  352 VAL   B C   
4506 O O   . VAL   B 259 ? 1.23762 0.97765 1.01914 -0.38185 -0.04360 0.06110  352 VAL   B O   
4507 C CB  . VAL   B 259 ? 1.26371 0.92971 0.99880 -0.31667 -0.07310 0.06562  352 VAL   B CB  
4508 C CG1 . VAL   B 259 ? 1.15811 0.86470 0.93501 -0.28513 -0.07649 0.05592  352 VAL   B CG1 
4509 C CG2 . VAL   B 259 ? 1.29878 0.91586 0.99359 -0.30274 -0.08425 0.07150  352 VAL   B CG2 
4510 N N   . ALA   B 260 ? 1.19190 1.01897 1.04354 -0.34012 -0.02957 0.05393  353 ALA   B N   
4511 C CA  . ALA   B 260 ? 1.35401 1.22772 1.24394 -0.35017 -0.02347 0.04616  353 ALA   B CA  
4512 C C   . ALA   B 260 ? 1.28685 1.13651 1.16938 -0.34230 -0.04117 0.04171  353 ALA   B C   
4513 O O   . ALA   B 260 ? 1.25099 1.06843 1.11622 -0.31739 -0.05599 0.04160  353 ALA   B O   
4514 C CB  . ALA   B 260 ? 1.13956 1.07831 1.08087 -0.33007 -0.01236 0.04027  353 ALA   B CB  
4515 N N   . ASP   B 261 ? 1.32034 1.18789 1.21688 -0.36388 -0.03966 0.03664  354 ASP   B N   
4516 C CA  . ASP   B 261 ? 1.40426 1.24897 1.29277 -0.35906 -0.05647 0.03160  354 ASP   B CA  
4517 C C   . ASP   B 261 ? 1.20109 1.07640 1.12060 -0.32438 -0.06205 0.02475  354 ASP   B C   
4518 O O   . ASP   B 261 ? 1.29725 1.14495 1.20266 -0.30988 -0.07781 0.02105  354 ASP   B O   
4519 C CB  . ASP   B 261 ? 1.57364 1.43486 1.47251 -0.39188 -0.05318 0.02692  354 ASP   B CB  
4520 C CG  . ASP   B 261 ? 1.66779 1.48285 1.52394 -0.42903 -0.05188 0.03384  354 ASP   B CG  
4521 O OD1 . ASP   B 261 ? 1.52334 1.27414 1.33134 -0.42574 -0.06275 0.04156  354 ASP   B OD1 
4522 O OD2 . ASP   B 261 ? 1.79574 1.63855 1.66554 -0.46184 -0.04041 0.03110  354 ASP   B OD2 
4523 N N   . GLU   B 262 ? 1.01171 0.94168 0.97078 -0.31114 -0.04956 0.02270  355 GLU   B N   
4524 C CA  . GLU   B 262 ? 1.17742 1.13338 1.16136 -0.27966 -0.05375 0.01776  355 GLU   B CA  
4525 C C   . GLU   B 262 ? 1.19177 1.11922 1.15612 -0.25266 -0.06068 0.02067  355 GLU   B C   
4526 O O   . GLU   B 262 ? 1.16389 1.11039 1.14502 -0.22751 -0.06337 0.01674  355 GLU   B O   
4527 C CB  . GLU   B 262 ? 1.20124 1.21914 1.22969 -0.27480 -0.03948 0.01503  355 GLU   B CB  
4528 C CG  . GLU   B 262 ? 1.21306 1.24291 1.24423 -0.28152 -0.02461 0.02023  355 GLU   B CG  
4529 C CD  . GLU   B 262 ? 1.25992 1.33189 1.31720 -0.30534 -0.01081 0.01652  355 GLU   B CD  
4530 O OE1 . GLU   B 262 ? 1.20285 1.30529 1.28550 -0.31078 -0.01274 0.00897  355 GLU   B OE1 
4531 O OE2 . GLU   B 262 ? 1.40578 1.48198 1.45841 -0.31830 0.00175  0.02010  355 GLU   B OE2 
4532 N N   . ASP   B 263 ? 1.20446 1.08748 1.13317 -0.25774 -0.06392 0.02692  356 ASP   B N   
4533 C CA  . ASP   B 263 ? 0.95351 0.80883 0.86307 -0.23222 -0.07252 0.02804  356 ASP   B CA  
4534 C C   . ASP   B 263 ? 0.98489 0.77317 0.84600 -0.23583 -0.08925 0.02994  356 ASP   B C   
4535 O O   . ASP   B 263 ? 0.99266 0.75290 0.83365 -0.21586 -0.09828 0.03026  356 ASP   B O   
4536 C CB  . ASP   B 263 ? 1.04735 0.91889 0.96400 -0.22764 -0.06053 0.03339  356 ASP   B CB  
4537 C CG  . ASP   B 263 ? 1.28132 1.14509 1.19400 -0.19743 -0.06714 0.03176  356 ASP   B CG  
4538 O OD1 . ASP   B 263 ? 1.28047 1.17584 1.21931 -0.17745 -0.06620 0.02626  356 ASP   B OD1 
4539 O OD2 . ASP   B 263 ? 1.24874 1.07508 1.13134 -0.19432 -0.07355 0.03561  356 ASP   B OD2 
4540 N N   . ALA   B 264 ? 0.97592 0.73709 0.81744 -0.26051 -0.09472 0.03045  357 ALA   B N   
4541 C CA  . ALA   B 264 ? 0.97985 0.67009 0.76996 -0.26682 -0.11153 0.03324  357 ALA   B CA  
4542 C C   . ALA   B 264 ? 1.07227 0.73505 0.84931 -0.23727 -0.13068 0.02510  357 ALA   B C   
4543 O O   . ALA   B 264 ? 1.14199 0.74793 0.87858 -0.22871 -0.14651 0.02600  357 ALA   B O   
4544 C CB  . ALA   B 264 ? 1.14643 0.81580 0.91957 -0.30326 -0.11204 0.03533  357 ALA   B CB  
4545 N N   . HIS   B 265 ? 1.04345 0.74485 0.85238 -0.22089 -0.13013 0.01642  358 HIS   B N   
4546 C CA  . HIS   B 265 ? 1.04464 0.72582 0.84299 -0.19298 -0.14643 0.00684  358 HIS   B CA  
4547 C C   . HIS   B 265 ? 1.04907 0.73268 0.84812 -0.16234 -0.14872 0.00452  358 HIS   B C   
4548 O O   . HIS   B 265 ? 0.93701 0.59224 0.71769 -0.13947 -0.16442 -0.00371 358 HIS   B O   
4549 C CB  . HIS   B 265 ? 0.97618 0.69971 0.80657 -0.18566 -0.14384 -0.00150 358 HIS   B CB  
4550 C CG  . HIS   B 265 ? 0.93051 0.71723 0.80389 -0.17457 -0.12747 -0.00124 358 HIS   B CG  
4551 N ND1 . HIS   B 265 ? 0.95195 0.77689 0.85129 -0.19263 -0.11107 0.00508  358 HIS   B ND1 
4552 C CD2 . HIS   B 265 ? 0.81192 0.62860 0.70502 -0.14785 -0.12527 -0.00695 358 HIS   B CD2 
4553 C CE1 . HIS   B 265 ? 0.94644 0.81804 0.87799 -0.17643 -0.10101 0.00375  358 HIS   B CE1 
4554 N NE2 . HIS   B 265 ? 0.91430 0.78142 0.84190 -0.15068 -0.10883 -0.00284 358 HIS   B NE2 
4555 N N   . ASN   B 266 ? 0.97488 0.69300 0.79543 -0.16117 -0.13386 0.01021  359 ASN   B N   
4556 C CA  . ASN   B 266 ? 1.01817 0.74451 0.84332 -0.13431 -0.13484 0.00759  359 ASN   B CA  
4557 C C   . ASN   B 266 ? 1.05646 0.73028 0.84246 -0.13211 -0.14650 0.01175  359 ASN   B C   
4558 O O   . ASN   B 266 ? 0.93478 0.61285 0.72279 -0.10951 -0.14964 0.00855  359 ASN   B O   
4559 C CB  . ASN   B 266 ? 0.79755 0.58094 0.66101 -0.13412 -0.11504 0.01153  359 ASN   B CB  
4560 C CG  . ASN   B 266 ? 0.88473 0.71800 0.78478 -0.12887 -0.10629 0.00653  359 ASN   B CG  
4561 O OD1 . ASN   B 266 ? 0.96732 0.80269 0.86925 -0.11191 -0.11411 -0.00231 359 ASN   B OD1 
4562 N ND2 . ASN   B 266 ? 0.82355 0.69628 0.75114 -0.14281 -0.09063 0.01155  359 ASN   B ND2 
4563 N N   . ILE   B 267 ? 1.02643 0.65055 0.77583 -0.15547 -0.15354 0.01858  360 ILE   B N   
4564 C CA  . ILE   B 267 ? 1.11330 0.67989 0.81848 -0.15546 -0.16626 0.02397  360 ILE   B CA  
4565 C C   . ILE   B 267 ? 1.15403 0.66825 0.82673 -0.13383 -0.19155 0.01483  360 ILE   B C   
4566 O O   . ILE   B 267 ? 1.16744 0.66294 0.83098 -0.13861 -0.20009 0.00984  360 ILE   B O   
4567 C CB  . ILE   B 267 ? 1.13093 0.66562 0.80729 -0.19357 -0.16118 0.03636  360 ILE   B CB  
4568 C CG1 . ILE   B 267 ? 1.03679 0.62932 0.74922 -0.21323 -0.13562 0.04255  360 ILE   B CG1 
4569 C CG2 . ILE   B 267 ? 1.10406 0.57440 0.72901 -0.19394 -0.17517 0.04319  360 ILE   B CG2 
4570 C CD1 . ILE   B 267 ? 1.11854 0.74393 0.85135 -0.19583 -0.12635 0.04368  360 ILE   B CD1 
4571 N N   . GLN   B 268 ? 1.03127 0.52247 0.68701 -0.10895 -0.20449 0.01135  361 GLN   B N   
4572 C CA  . GLN   B 268 ? 1.12273 0.56475 0.74807 -0.08409 -0.23023 0.00053  361 GLN   B CA  
4573 C C   . GLN   B 268 ? 1.39864 0.76009 0.96666 -0.10443 -0.24725 0.00762  361 GLN   B C   
4574 O O   . GLN   B 268 ? 1.36761 0.69773 0.90699 -0.12777 -0.24479 0.02103  361 GLN   B O   
4575 C CB  . GLN   B 268 ? 1.07202 0.51317 0.69577 -0.05207 -0.24046 -0.00606 361 GLN   B CB  
4576 C CG  . GLN   B 268 ? 1.14295 0.53824 0.73886 -0.02137 -0.26829 -0.02027 361 GLN   B CG  
4577 C CD  . GLN   B 268 ? 1.18868 0.61694 0.81206 -0.00289 -0.26867 -0.03613 361 GLN   B CD  
4578 O OE1 . GLN   B 268 ? 1.08516 0.58155 0.75506 0.00569  -0.25153 -0.04153 361 GLN   B OE1 
4579 N NE2 . GLN   B 268 ? 1.26540 0.64284 0.85720 0.00251  -0.28849 -0.04361 361 GLN   B NE2 
4580 N N   . THR   B 269 ? 1.34122 0.66763 0.89030 -0.09661 -0.26440 -0.00155 362 THR   B N   
4581 C CA  . THR   B 269 ? 1.47727 0.72042 0.96836 -0.11355 -0.28398 0.00332  362 THR   B CA  
4582 C C   . THR   B 269 ? 1.49441 0.68194 0.95093 -0.07806 -0.31415 -0.00890 362 THR   B C   
4583 O O   . THR   B 269 ? 1.38392 0.60465 0.86616 -0.04157 -0.31816 -0.02257 362 THR   B O   
4584 C CB  . THR   B 269 ? 1.46504 0.70785 0.95929 -0.13776 -0.28038 0.00251  362 THR   B CB  
4585 O OG1 . THR   B 269 ? 1.39104 0.66678 0.91435 -0.11079 -0.28412 -0.01397 362 THR   B OG1 
4586 C CG2 . THR   B 269 ? 1.39372 0.69080 0.92155 -0.17243 -0.25240 0.01329  362 THR   B CG2 
4587 N N   . HIS   B 270 ? 1.60011 0.70188 0.99706 -0.08937 -0.33592 -0.00464 363 HIS   B N   
4588 C CA  . HIS   B 270 ? 1.67569 0.71492 1.03366 -0.05551 -0.36813 -0.01674 363 HIS   B CA  
4589 C C   . HIS   B 270 ? 1.80921 0.76020 1.10781 -0.07555 -0.38863 -0.01288 363 HIS   B C   
4590 O O   . HIS   B 270 ? 2.09339 0.99408 1.35033 -0.11025 -0.38850 0.00420  363 HIS   B O   
4591 C CB  . HIS   B 270 ? 1.69132 0.70565 1.02717 -0.03758 -0.37931 -0.01320 363 HIS   B CB  
4592 C CG  . HIS   B 270 ? 1.79218 0.72881 1.07797 -0.00652 -0.41589 -0.02370 363 HIS   B CG  
4593 N ND1 . HIS   B 270 ? 1.99352 0.83101 1.20774 -0.02310 -0.43818 -0.01337 363 HIS   B ND1 
4594 C CD2 . HIS   B 270 ? 1.78479 0.72787 1.08098 0.04049  -0.43476 -0.04457 363 HIS   B CD2 
4595 C CE1 . HIS   B 270 ? 1.84765 0.63540 1.03098 0.01436  -0.46995 -0.02696 363 HIS   B CE1 
4596 N NE2 . HIS   B 270 ? 1.86161 0.70983 1.09391 0.05400  -0.46929 -0.04720 363 HIS   B NE2 
4597 N N   . ARG   B 271 ? 1.81562 0.74725 1.10874 -0.05507 -0.40578 -0.02896 364 ARG   B N   
4598 C CA  . ARG   B 271 ? 2.11182 0.94964 1.34326 -0.06481 -0.43195 -0.02905 364 ARG   B CA  
4599 C C   . ARG   B 271 ? 2.19469 0.99495 1.40313 -0.01636 -0.46262 -0.04625 364 ARG   B C   
4600 O O   . ARG   B 271 ? 2.11769 0.96305 1.36284 0.02245  -0.46397 -0.06418 364 ARG   B O   
4601 C CB  . ARG   B 271 ? 2.02976 0.88012 1.27414 -0.08690 -0.42479 -0.03272 364 ARG   B CB  
4602 C CG  . ARG   B 271 ? 2.14728 1.06766 1.44516 -0.05708 -0.41810 -0.05245 364 ARG   B CG  
4603 C CD  . ARG   B 271 ? 2.19765 1.06558 1.46604 -0.02430 -0.44827 -0.07227 364 ARG   B CD  
4604 N NE  . ARG   B 271 ? 2.13494 1.05867 1.44420 -0.01076 -0.44031 -0.08852 364 ARG   B NE  
4605 C CZ  . ARG   B 271 ? 2.06757 0.97705 1.36943 -0.03216 -0.44142 -0.09025 364 ARG   B CZ  
4606 N NH1 . ARG   B 271 ? 2.20524 1.05761 1.46649 -0.06862 -0.44693 -0.07558 364 ARG   B NH1 
4607 N NH2 . ARG   B 271 ? 1.96419 0.92710 1.30299 -0.01676 -0.43432 -0.10557 364 ARG   B NH2 
4608 N N   . ASP   B 272 ? 2.50921 1.24635 1.66327 -0.01834 -0.48331 -0.03954 365 ASP   B N   
4609 C CA  . ASP   B 272 ? 2.71851 1.42320 1.84841 0.02650  -0.51348 -0.05429 365 ASP   B CA  
4610 C C   . ASP   B 272 ? 2.65662 1.38866 1.81654 0.05877  -0.52024 -0.07870 365 ASP   B C   
4611 O O   . ASP   B 272 ? 2.69124 1.39236 1.82869 0.05679  -0.53230 -0.08227 365 ASP   B O   
4612 C CB  . ASP   B 272 ? 2.81652 1.44523 1.87866 0.01322  -0.53473 -0.04233 365 ASP   B CB  
4613 C CG  . ASP   B 272 ? 2.94087 1.54047 1.96711 -0.00939 -0.53268 -0.02240 365 ASP   B CG  
4614 O OD1 . ASP   B 272 ? 2.84286 1.48182 1.89843 -0.01461 -0.51442 -0.01718 365 ASP   B OD1 
4615 O OD2 . ASP   B 272 ? 3.11594 1.65265 2.08294 -0.02212 -0.54952 -0.01251 365 ASP   B OD2 
4616 N N   . SER   B 273 ? 2.14304 0.93458 1.35313 0.08806  -0.51183 -0.09621 366 SER   B N   
4617 C CA  . SER   B 273 ? 2.30295 1.13071 1.54466 0.12112  -0.51559 -0.12190 366 SER   B CA  
4618 C C   . SER   B 273 ? 2.30216 1.12993 1.54157 0.17313  -0.53905 -0.14167 366 SER   B C   
4619 O O   . SER   B 273 ? 2.29332 1.17170 1.57117 0.20600  -0.53714 -0.16543 366 SER   B O   
4620 C CB  . SER   B 273 ? 2.10738 1.02387 1.41317 0.11748  -0.48550 -0.12794 366 SER   B CB  
4621 O OG  . SER   B 273 ? 1.97417 0.94215 1.31136 0.13053  -0.47338 -0.12521 366 SER   B OG  
4622 N N   . LEU   B 274 ? 2.31520 1.09102 1.51025 0.18039  -0.56092 -0.13337 367 LEU   B N   
4623 C CA  . LEU   B 274 ? 2.21865 0.99508 1.41011 0.22889  -0.58596 -0.15310 367 LEU   B CA  
4624 C C   . LEU   B 274 ? 2.21338 0.97814 1.39665 0.25194  -0.60322 -0.17101 367 LEU   B C   
4625 O O   . LEU   B 274 ? 1.97748 0.79023 1.19578 0.29063  -0.60652 -0.19621 367 LEU   B O   
4626 C CB  . LEU   B 274 ? 2.28213 1.00033 1.42141 0.22751  -0.60742 -0.14004 367 LEU   B CB  
4627 C CG  . LEU   B 274 ? 2.29672 1.02141 1.43790 0.20523  -0.59231 -0.12174 367 LEU   B CG  
4628 C CD1 . LEU   B 274 ? 2.38234 1.04665 1.46632 0.20602  -0.61625 -0.11183 367 LEU   B CD1 
4629 C CD2 . LEU   B 274 ? 2.03674 0.83712 1.23886 0.23074  -0.57740 -0.13638 367 LEU   B CD2 
4630 N N   . ASP   B 275 ? 2.36306 1.06646 1.50046 0.22779  -0.61359 -0.15871 368 ASP   B N   
4631 C CA  . ASP   B 275 ? 2.51186 1.20098 1.64005 0.24620  -0.62901 -0.17427 368 ASP   B CA  
4632 C C   . ASP   B 275 ? 2.37175 1.11779 1.54789 0.24385  -0.60669 -0.18660 368 ASP   B C   
4633 O O   . ASP   B 275 ? 2.39453 1.15027 1.57765 0.26906  -0.61631 -0.20599 368 ASP   B O   
4634 C CB  . ASP   B 275 ? 2.63073 1.23864 1.69646 0.21768  -0.64484 -0.15693 368 ASP   B CB  
4635 C CG  . ASP   B 275 ? 2.68113 1.27595 1.73832 0.16211  -0.62186 -0.13114 368 ASP   B CG  
4636 O OD1 . ASP   B 275 ? 2.64321 1.27302 1.73253 0.14289  -0.60073 -0.13219 368 ASP   B OD1 
4637 O OD2 . ASP   B 275 ? 2.86190 1.41400 1.88006 0.13716  -0.62493 -0.11083 368 ASP   B OD2 
4638 N N   . LEU   B 276 ? 2.29664 1.08065 1.50423 0.21402  -0.57779 -0.17659 369 LEU   B N   
4639 C CA  . LEU   B 276 ? 2.27306 1.11444 1.52515 0.21207  -0.55718 -0.18977 369 LEU   B CA  
4640 C C   . LEU   B 276 ? 2.15111 1.06084 1.44932 0.25655  -0.55362 -0.21709 369 LEU   B C   
4641 O O   . LEU   B 276 ? 2.01625 0.96548 1.34042 0.26894  -0.54627 -0.23510 369 LEU   B O   
4642 C CB  . LEU   B 276 ? 2.27611 1.14217 1.54891 0.16909  -0.52923 -0.17302 369 LEU   B CB  
4643 C CG  . LEU   B 276 ? 2.14700 0.98692 1.40277 0.12416  -0.52139 -0.15779 369 LEU   B CG  
4644 C CD1 . LEU   B 276 ? 2.31234 1.07530 1.51098 0.11498  -0.54422 -0.14685 369 LEU   B CD1 
4645 C CD2 . LEU   B 276 ? 2.05853 0.91381 1.32626 0.08103  -0.49830 -0.13711 369 LEU   B CD2 
4646 N N   . LEU   B 277 ? 2.08644 1.01377 1.39524 0.27998  -0.55814 -0.22098 370 LEU   B N   
4647 C CA  . LEU   B 277 ? 1.98927 0.98851 1.34481 0.32054  -0.55312 -0.24726 370 LEU   B CA  
4648 C C   . LEU   B 277 ? 2.15040 1.14518 1.49714 0.36040  -0.57689 -0.26912 370 LEU   B C   
4649 O O   . LEU   B 277 ? 2.00099 1.05566 1.38466 0.38604  -0.56920 -0.29295 370 LEU   B O   
4650 C CB  . LEU   B 277 ? 1.77754 0.80021 1.14938 0.33092  -0.55018 -0.24444 370 LEU   B CB  
4651 C CG  . LEU   B 277 ? 1.92430 1.02679 1.34678 0.37105  -0.54411 -0.27104 370 LEU   B CG  
4652 C CD1 . LEU   B 277 ? 1.74773 0.92136 1.21797 0.36453  -0.51387 -0.28211 370 LEU   B CD1 
4653 C CD2 . LEU   B 277 ? 1.72632 0.84051 1.15702 0.38103  -0.54688 -0.26667 370 LEU   B CD2 
4654 N N   . ASP   B 278 ? 2.24816 1.17378 1.54489 0.36531  -0.60577 -0.26200 371 ASP   B N   
4655 C CA  . ASP   B 278 ? 2.47272 1.39116 1.75842 0.40381  -0.63124 -0.28354 371 ASP   B CA  
4656 C C   . ASP   B 278 ? 2.60175 1.50900 1.88044 0.40066  -0.63193 -0.29112 371 ASP   B C   
4657 O O   . ASP   B 278 ? 2.52361 1.45050 1.81070 0.43482  -0.64446 -0.31458 371 ASP   B O   
4658 C CB  . ASP   B 278 ? 2.65445 1.49971 1.88454 0.41024  -0.66406 -0.27462 371 ASP   B CB  
4659 C CG  . ASP   B 278 ? 2.87018 1.63658 2.04506 0.39409  -0.68307 -0.26421 371 ASP   B CG  
4660 O OD1 . ASP   B 278 ? 2.86734 1.60244 2.02517 0.35251  -0.66985 -0.24300 371 ASP   B OD1 
4661 O OD2 . ASP   B 278 ? 3.03818 1.77530 2.18699 0.42265  -0.71164 -0.27812 371 ASP   B OD2 
4662 N N   . LYS   B 279 ? 2.43297 1.31154 1.69722 0.35998  -0.61890 -0.27267 372 LYS   B N   
4663 C CA  . LYS   B 279 ? 2.30463 1.17799 1.56569 0.35482  -0.61750 -0.28032 372 LYS   B CA  
4664 C C   . LYS   B 279 ? 2.12599 1.08310 1.44116 0.37127  -0.59524 -0.30271 372 LYS   B C   
4665 O O   . LYS   B 279 ? 2.15815 1.12259 1.47483 0.38315  -0.59847 -0.31785 372 LYS   B O   
4666 C CB  . LYS   B 279 ? 2.12476 0.95363 1.36043 0.30435  -0.60805 -0.25549 372 LYS   B CB  
4667 C CG  . LYS   B 279 ? 2.25076 0.99286 1.42613 0.28424  -0.62980 -0.23400 372 LYS   B CG  
4668 C CD  . LYS   B 279 ? 2.21256 0.92509 1.37103 0.23051  -0.61524 -0.20957 372 LYS   B CD  
4669 C CE  . LYS   B 279 ? 2.31731 0.94817 1.41508 0.20723  -0.63372 -0.18740 372 LYS   B CE  
4670 N NZ  . LYS   B 279 ? 2.30263 0.91323 1.38774 0.15253  -0.61692 -0.16400 372 LYS   B NZ  
4671 N N   . ALA   B 280 ? 2.20266 1.22261 1.56007 0.37150  -0.57261 -0.30521 373 ALA   B N   
4672 C CA  . ALA   B 280 ? 2.11362 1.21611 1.52011 0.38577  -0.55018 -0.32634 373 ALA   B CA  
4673 C C   . ALA   B 280 ? 2.31217 1.45731 1.73888 0.43284  -0.56037 -0.35463 373 ALA   B C   
4674 O O   . ALA   B 280 ? 2.26137 1.46333 1.71745 0.44600  -0.54662 -0.37425 373 ALA   B O   
4675 C CB  . ALA   B 280 ? 1.88552 1.04146 1.32859 0.37148  -0.52381 -0.32066 373 ALA   B CB  
4676 N N   . ARG   B 281 ? 2.33601 1.45743 1.74699 0.45724  -0.58418 -0.35765 374 ARG   B N   
4677 C CA  . ARG   B 281 ? 2.15244 1.31620 1.58289 0.50115  -0.59611 -0.38571 374 ARG   B CA  
4678 C C   . ARG   B 281 ? 2.35531 1.49018 1.76262 0.51403  -0.61258 -0.39800 374 ARG   B C   
4679 O O   . ARG   B 281 ? 2.41121 1.46626 1.76992 0.50070  -0.63286 -0.38395 374 ARG   B O   
4680 C CB  . ARG   B 281 ? 2.29424 1.43593 1.70957 0.52195  -0.62060 -0.38578 374 ARG   B CB  
4681 C CG  . ARG   B 281 ? 2.39049 1.58144 1.82862 0.56655  -0.63410 -0.41637 374 ARG   B CG  
4682 C CD  . ARG   B 281 ? 2.36239 1.53203 1.78437 0.58485  -0.65922 -0.41688 374 ARG   B CD  
4683 N NE  . ARG   B 281 ? 2.45091 1.66958 1.89510 0.62642  -0.67358 -0.44804 374 ARG   B NE  
4684 C CZ  . ARG   B 281 ? 2.57574 1.78865 2.01115 0.64900  -0.69740 -0.45676 374 ARG   B CZ  
4685 N NH1 . ARG   B 281 ? 2.72178 1.88055 2.12467 0.63514  -0.70978 -0.43633 374 ARG   B NH1 
4686 N NH2 . ARG   B 281 ? 2.57386 1.83719 2.03267 0.68549  -0.70910 -0.48762 374 ARG   B NH2 
4687 N N   . ALA   B 282 ? 2.33044 1.53130 1.77193 0.53864  -0.60303 -0.42418 375 ALA   B N   
4688 C CA  . ALA   B 282 ? 2.11182 1.29641 1.53729 0.55347  -0.61577 -0.43932 375 ALA   B CA  
4689 C C   . ALA   B 282 ? 2.20180 1.33374 1.59784 0.51900  -0.61130 -0.42216 375 ALA   B C   
4690 O O   . ALA   B 282 ? 2.06011 1.21871 1.47433 0.49121  -0.58486 -0.41318 375 ALA   B O   
4691 C CB  . ALA   B 282 ? 2.16638 1.30112 1.55786 0.58245  -0.65359 -0.44758 375 ALA   B CB  
4692 C C13 . A1CAI C .   ? 0.44077 0.79688 0.68569 -0.09176 0.03200  -0.04997 301 A1CAI A C13 
4693 C C14 . A1CAI C .   ? 0.37473 0.72654 0.61464 -0.07386 0.02293  -0.05172 301 A1CAI A C14 
4694 C C15 . A1CAI C .   ? 0.43208 0.76226 0.65832 -0.06215 0.01021  -0.05191 301 A1CAI A C15 
4695 C C16 . A1CAI C .   ? 0.44742 0.75243 0.65684 -0.05310 0.00755  -0.04349 301 A1CAI A C16 
4696 C C17 . A1CAI C .   ? 0.46366 0.76486 0.67331 -0.06259 0.02063  -0.03364 301 A1CAI A C17 
4697 C C18 . A1CAI C .   ? 0.43070 0.76323 0.65894 -0.07218 0.02821  -0.04036 301 A1CAI A C18 
4698 C C20 . A1CAI C .   ? 0.51684 0.77107 0.69988 -0.06574 0.02309  -0.01767 301 A1CAI A C20 
4699 C C22 . A1CAI C .   ? 0.60641 0.85155 0.78964 -0.08179 0.03266  -0.01458 301 A1CAI A C22 
4700 C C23 . A1CAI C .   ? 0.55688 0.79410 0.74009 -0.08777 0.04213  -0.00614 301 A1CAI A C23 
4701 C C24 . A1CAI C .   ? 0.77140 1.00400 0.94581 -0.08362 0.03021  -0.01643 301 A1CAI A C24 
4702 C C26 . A1CAI C .   ? 0.33771 0.66975 0.57186 -0.09955 0.03434  -0.04262 301 A1CAI A C26 
4703 C C28 . A1CAI C .   ? 0.70076 0.94368 0.89470 -0.13141 0.03550  -0.03609 301 A1CAI A C28 
4704 C C29 . A1CAI C .   ? 0.60645 0.84870 0.79873 -0.13384 0.02893  -0.04424 301 A1CAI A C29 
4705 C C01 . A1CAI C .   ? 0.78749 1.03947 0.97855 -0.13209 0.00964  -0.06418 301 A1CAI A C01 
4706 C C03 . A1CAI C .   ? 0.56056 0.82748 0.76751 -0.14298 0.02528  -0.05431 301 A1CAI A C03 
4707 C C04 . A1CAI C .   ? 0.58834 0.88185 0.81142 -0.14987 0.02996  -0.05612 301 A1CAI A C04 
4708 C C05 . A1CAI C .   ? 0.63777 0.92958 0.85971 -0.14705 0.03715  -0.04742 301 A1CAI A C05 
4709 C C06 . A1CAI C .   ? 0.59578 0.86145 0.80313 -0.13745 0.03946  -0.03688 301 A1CAI A C06 
4710 C C07 . A1CAI C .   ? 0.61384 0.87761 0.81990 -0.13414 0.04594  -0.02794 301 A1CAI A C07 
4711 C C08 . A1CAI C .   ? 0.46126 0.74903 0.67737 -0.12389 0.04338  -0.03135 301 A1CAI A C08 
4712 C C10 . A1CAI C .   ? 0.43845 0.78045 0.67971 -0.11706 0.04212  -0.04400 301 A1CAI A C10 
4713 N N09 . A1CAI C .   ? 0.45559 0.77576 0.68773 -0.12850 0.04532  -0.03872 301 A1CAI A N09 
4714 N N11 . A1CAI C .   ? 0.45149 0.82633 0.70819 -0.12133 0.04590  -0.05199 301 A1CAI A N11 
4715 N N12 . A1CAI C .   ? 0.39863 0.78273 0.65839 -0.10504 0.03981  -0.05612 301 A1CAI A N12 
4716 N N21 . A1CAI C .   ? 0.69838 0.93771 0.87356 -0.07142 0.02606  -0.01392 301 A1CAI A N21 
4717 O O02 . A1CAI C .   ? 0.76961 1.03595 0.97491 -0.14526 0.01755  -0.06297 301 A1CAI A O02 
4718 O O19 . A1CAI C .   ? 0.47108 0.75075 0.67092 -0.07090 0.02700  -0.02362 301 A1CAI A O19 
4719 O O25 . A1CAI C .   ? 0.63084 0.87749 0.80645 -0.05784 0.01787  -0.01674 301 A1CAI A O25 
4720 O O27 . A1CAI C .   ? 0.54001 0.81709 0.74862 -0.11146 0.03959  -0.02814 301 A1CAI A O27 
4721 O O   . HOH   D .   ? 0.62509 0.80902 0.76684 -0.07596 0.04417  0.01608  401 HOH   A O   
4722 O O   . HOH   D .   ? 0.61086 0.76658 0.70515 -0.25035 0.09713  0.03684  402 HOH   A O   
4723 O O   . HOH   D .   ? 0.62761 0.88971 0.73599 0.01328  -0.00134 -0.05901 403 HOH   A O   
4724 O O   . HOH   D .   ? 0.37758 0.97816 0.74016 -0.15083 0.06525  -0.12640 404 HOH   A O   
4725 O O   . HOH   D .   ? 0.49679 0.70263 0.63524 -0.05447 0.00810  0.04395  405 HOH   A O   
4726 O O   . HOH   D .   ? 0.47305 0.67234 0.64228 -0.09947 0.05005  -0.00301 406 HOH   A O   
4727 O O   . HOH   D .   ? 0.66382 0.87869 0.91314 0.05873  -0.06931 -0.00178 407 HOH   A O   
4728 O O   . HOH   D .   ? 0.62821 0.77061 0.74904 -0.11537 0.00057  0.02620  408 HOH   A O   
4729 O O   . HOH   D .   ? 0.47235 1.21407 1.08376 -0.01413 -0.00655 -0.16468 409 HOH   A O   
4730 O O   . HOH   D .   ? 0.65323 0.80764 0.75723 -0.06269 0.01713  0.01089  410 HOH   A O   
4731 O O   . HOH   D .   ? 0.60716 0.70679 0.67654 -0.05092 -0.01061 0.01674  411 HOH   A O   
4732 O O   . HOH   D .   ? 0.46941 0.67368 0.58860 -0.06232 0.02383  0.04638  412 HOH   A O   
4733 O O   . HOH   D .   ? 0.41751 0.65825 0.63468 -0.07009 0.04890  0.02656  413 HOH   A O   
4734 O O   . HOH   D .   ? 0.45307 0.65253 0.60445 -0.06089 0.03066  0.01673  414 HOH   A O   
4735 O O   . HOH   D .   ? 0.41437 0.88729 0.66369 -0.14733 0.10370  -0.05206 415 HOH   A O   
4736 O O   . HOH   D .   ? 0.45330 0.68726 0.64651 -0.07353 0.00834  0.02792  416 HOH   A O   
4737 O O   . HOH   D .   ? 0.81349 0.85959 0.78192 -0.28907 0.10320  0.08261  417 HOH   A O   
4738 O O   . HOH   D .   ? 0.50024 0.77664 0.59743 -0.00968 0.01733  -0.04285 418 HOH   A O   
4739 O O   . HOH   D .   ? 0.68514 0.92135 0.76185 -0.07559 0.04693  0.03322  419 HOH   A O   
4740 O O   . HOH   D .   ? 0.87164 0.82470 0.81830 -0.09228 -0.03346 0.03884  420 HOH   A O   
4741 O O   . HOH   D .   ? 0.49721 0.65014 0.69719 -0.02351 0.03869  0.00765  421 HOH   A O   
4742 O O   . HOH   D .   ? 0.47496 0.78171 0.68358 -0.05466 0.02714  -0.02834 422 HOH   A O   
4743 O O   . HOH   D .   ? 0.44613 0.70204 0.66534 -0.08034 0.01612  0.02358  423 HOH   A O   
4744 O O   . HOH   D .   ? 0.51450 0.81886 0.72956 -0.15416 0.10025  0.00191  424 HOH   A O   
4745 O O   . HOH   D .   ? 0.85071 0.96965 0.90828 -0.31562 0.10616  0.03905  425 HOH   A O   
4746 O O   . HOH   D .   ? 0.93138 0.84200 0.71242 -0.16078 0.01612  0.14188  426 HOH   A O   
4747 O O   . HOH   D .   ? 0.44344 0.78004 0.66204 -0.06678 0.04460  -0.02765 427 HOH   A O   
4748 O O   . HOH   D .   ? 0.44877 0.66001 0.68286 -0.02181 0.05051  -0.00629 428 HOH   A O   
4749 O O   . HOH   D .   ? 0.41903 0.63163 0.60308 -0.07196 0.04931  0.03402  429 HOH   A O   
4750 O O   . HOH   D .   ? 0.67325 0.87858 0.83457 -0.10206 0.03175  -0.02568 430 HOH   A O   
4751 O O   . HOH   D .   ? 0.71581 0.77028 0.85781 -0.04278 0.03748  0.00045  431 HOH   A O   
4752 O O   . HOH   D .   ? 0.45202 0.65878 0.61233 -0.04775 0.00196  0.04504  432 HOH   A O   
4753 O O   . HOH   D .   ? 0.34624 0.62635 0.61450 -0.03940 0.05532  -0.00532 433 HOH   A O   
4754 O O   . HOH   D .   ? 0.50812 0.97215 0.75665 -0.08515 0.07776  -0.06371 434 HOH   A O   
4755 O O   . HOH   D .   ? 0.64984 0.95517 0.97608 0.05419  0.03488  -0.08102 435 HOH   A O   
4756 O O   . HOH   D .   ? 0.61446 0.98203 0.85166 -0.24227 0.09217  -0.04040 436 HOH   A O   
4757 O O   . HOH   D .   ? 0.57809 1.12342 0.89909 -0.19426 0.09047  -0.09593 437 HOH   A O   
4758 O O   . HOH   D .   ? 0.43629 0.70743 0.66712 -0.09982 0.01368  0.01599  438 HOH   A O   
4759 O O   . HOH   D .   ? 0.58198 0.72859 0.64568 -0.03802 -0.03036 0.06300  439 HOH   A O   
4760 O O   . HOH   D .   ? 0.56977 0.79222 0.74885 -0.10606 0.04139  -0.01672 440 HOH   A O   
4761 O O   . HOH   D .   ? 0.52958 0.84447 0.84465 0.04805  -0.07180 -0.02298 441 HOH   A O   
4762 O O   . HOH   D .   ? 0.91461 0.74212 0.74854 -0.06732 -0.08608 0.03945  442 HOH   A O   
4763 O O   . HOH   D .   ? 0.90769 0.95710 1.01839 -0.09768 0.04687  -0.02802 443 HOH   A O   
4764 O O   . HOH   D .   ? 0.62646 0.81237 0.77620 -0.08836 0.04607  -0.00361 444 HOH   A O   
4765 O O   . HOH   D .   ? 0.74726 0.86216 0.79069 -0.02308 -0.05474 0.06900  445 HOH   A O   
4766 O O   . HOH   D .   ? 0.93950 0.93173 0.87011 -0.32801 0.10365  0.08919  446 HOH   A O   
4767 O O   . HOH   E .   ? 0.58461 0.78877 0.66586 -0.07173 0.03286  0.04795  401 HOH   B O   
4768 O O   . HOH   E .   ? 0.84948 0.99458 0.87462 -0.04615 -0.02656 0.06232  402 HOH   B O   
4769 O O   . HOH   E .   ? 0.77581 0.82146 0.78816 0.05992  -0.09854 -0.07394 403 HOH   B O   
4770 O O   . HOH   E .   ? 0.81635 0.60936 0.68677 -0.06608 -0.13805 -0.01754 404 HOH   B O   
4771 O O   . HOH   E .   ? 0.76056 0.80685 0.77390 -0.00631 -0.07662 -0.04049 405 HOH   B O   
4772 O O   . HOH   E .   ? 1.04862 0.55417 0.72172 -0.19040 -0.18971 0.01314  406 HOH   B O   
4773 O O   . HOH   E .   ? 0.87394 0.74837 0.76116 -0.06130 -0.07743 0.03103  407 HOH   B O   
4774 O O   . HOH   E .   ? 1.03869 0.58161 0.74286 0.01376  -0.24581 -0.06031 408 HOH   B O   
4775 O O   . HOH   E .   ? 0.72612 1.03659 0.80319 -0.09926 0.08429  0.00889  409 HOH   B O   
4776 O O   . HOH   E .   ? 0.78119 0.71958 0.73856 -0.00395 -0.10852 -0.03723 410 HOH   B O   
4777 O O   . HOH   E .   ? 0.67751 0.73699 0.71036 0.05656  -0.09478 -0.05680 411 HOH   B O   
4778 O O   . HOH   E .   ? 0.85346 0.65278 0.72555 -0.05545 -0.13075 -0.00932 412 HOH   B O   
# 
