data_8YJ2
# 
_entry.id   8YJ2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YJ2         pdb_00008yj2 10.2210/pdb8yj2/pdb 
WWPDB D_1300045750 ?            ?                   
# 
_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       2024-12-04 
# 
_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                        8YJ2 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rmariuzz@umd.edu 
_pdbx_contact_author.name_first         Roy 
_pdbx_contact_author.name_last          Mariuzza 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0748-5875 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wu, D.C.'       1 0000-0003-2086-0190 
'Mariuzza, R.A.' 2 0000-0003-0748-5875 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                eadq6150 
_citation.page_last                 eadq6150 
_citation.title                     
'Structural characterization and AlphaFold modeling of human T cell receptor recognition of NRAS cancer neoantigens.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/sciadv.adq6150 
_citation.pdbx_database_id_PubMed   39576860 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wu, D.'              1 0000-0003-2086-0190 
primary 'Yin, R.'             2 0000-0001-5330-8306 
primary 'Chen, G.'            3 0009-0003-5196-2007 
primary 'Ribeiro-Filho, H.V.' 4 0000-0001-8471-207X 
primary 'Cheung, M.'          5 ?                   
primary 'Robbins, P.F.'       6 0000-0002-1260-8123 
primary 'Mariuzza, R.A.'      7 0000-0003-0748-5875 
primary 'Pierce, B.G.'        8 0000-0003-4821-0368 
# 
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 'human leukocyte antigen'               31897.266 1   ? ? ? ? 
2 polymer man Beta-2-microglobulin                    11879.356 1   ? ? ? ? 
3 polymer syn ILE-LEU-ASP-THR-ALA-GLY-ARG-GLU-GLU-TYR 1167.247  1   ? ? ? ? 
4 polymer man 'tcr beta'                              28186.664 1   ? ? ? ? 
5 polymer man 'tcr alpha'                             23074.811 1   ? ? ? ? 
6 water   nat water                                   18.015    426 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLG
TLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVY
LEGRCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDG
TFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWE
;
;MGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLG
TLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVY
LEGRCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDG
TFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWE
;
A ? 
2 'polypeptide(L)' no no 
;MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
;
;MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
;
B ? 
3 'polypeptide(L)' no no ILDTAGREEY ILDTAGREEY C ? 
4 'polypeptide(L)' no no 
;MEAQVTQNPRYLITVTGKKLTVTCSQNMNHEYMSWYRQDPGLGLRQIYYSMNVEVTDKGDVPEGYKVSRKEKRNFPLILE
SPSPNQTSLYFCASSLVSTPLPKETQYFGPGTRLLVLEDLKNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVEL
SWWVNGKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSA
EAWGRAD
;
;MEAQVTQNPRYLITVTGKKLTVTCSQNMNHEYMSWYRQDPGLGLRQIYYSMNVEVTDKGDVPEGYKVSRKEKRNFPLILE
SPSPNQTSLYFCASSLVSTPLPKETQYFGPGTRLLVLEDLKNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVEL
SWWVNGKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSA
EAWGRAD
;
E ? 
5 'polypeptide(L)' no no 
;MAQKVTQAQSSVSMPVRKAVTLNCLYETSWWSYYIFWYKQLPSKEMIFLIRQGSDEQNAKSGRYSVNFKKAAKSVALTIS
ALQLEDSAKYFCALGDTAGKSTFGDGTTLTVKPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDK
CVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS
;
;MAQKVTQAQSSVSMPVRKAVTLNCLYETSWWSYYIFWYKQLPSKEMIFLIRQGSDEQNAKSGRYSVNFKKAAKSVALTIS
ALQLEDSAKYFCALGDTAGKSTFGDGTTLTVKPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDK
CVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS
;
D ? 
# 
_pdbx_entity_nonpoly.entity_id   6 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   HIS n 
1 5   SER n 
1 6   MET n 
1 7   ARG n 
1 8   TYR n 
1 9   PHE n 
1 10  PHE n 
1 11  THR n 
1 12  SER n 
1 13  VAL n 
1 14  SER n 
1 15  ARG n 
1 16  PRO n 
1 17  GLY n 
1 18  ARG n 
1 19  GLY n 
1 20  GLU n 
1 21  PRO n 
1 22  ARG n 
1 23  PHE n 
1 24  ILE n 
1 25  ALA n 
1 26  VAL n 
1 27  GLY n 
1 28  TYR n 
1 29  VAL n 
1 30  ASP n 
1 31  ASP n 
1 32  THR n 
1 33  GLN n 
1 34  PHE n 
1 35  VAL n 
1 36  ARG n 
1 37  PHE n 
1 38  ASP n 
1 39  SER n 
1 40  ASP n 
1 41  ALA n 
1 42  ALA n 
1 43  SER n 
1 44  GLN n 
1 45  LYS n 
1 46  MET n 
1 47  GLU n 
1 48  PRO n 
1 49  ARG n 
1 50  ALA n 
1 51  PRO n 
1 52  TRP n 
1 53  ILE n 
1 54  GLU n 
1 55  GLN n 
1 56  GLU n 
1 57  GLY n 
1 58  PRO n 
1 59  GLU n 
1 60  TYR n 
1 61  TRP n 
1 62  ASP n 
1 63  GLN n 
1 64  GLU n 
1 65  THR n 
1 66  ARG n 
1 67  ASN n 
1 68  MET n 
1 69  LYS n 
1 70  ALA n 
1 71  HIS n 
1 72  SER n 
1 73  GLN n 
1 74  THR n 
1 75  ASP n 
1 76  ARG n 
1 77  ALA n 
1 78  ASN n 
1 79  LEU n 
1 80  GLY n 
1 81  THR n 
1 82  LEU n 
1 83  ARG n 
1 84  GLY n 
1 85  TYR n 
1 86  TYR n 
1 87  ASN n 
1 88  GLN n 
1 89  SER n 
1 90  GLU n 
1 91  ASP n 
1 92  GLY n 
1 93  SER n 
1 94  HIS n 
1 95  THR n 
1 96  ILE n 
1 97  GLN n 
1 98  ILE n 
1 99  MET n 
1 100 TYR n 
1 101 GLY n 
1 102 CYS n 
1 103 ASP n 
1 104 VAL n 
1 105 GLY n 
1 106 PRO n 
1 107 ASP n 
1 108 GLY n 
1 109 ARG n 
1 110 PHE n 
1 111 LEU n 
1 112 ARG n 
1 113 GLY n 
1 114 TYR n 
1 115 ARG n 
1 116 GLN n 
1 117 ASP n 
1 118 ALA n 
1 119 TYR n 
1 120 ASP n 
1 121 GLY n 
1 122 LYS n 
1 123 ASP n 
1 124 TYR n 
1 125 ILE n 
1 126 ALA n 
1 127 LEU n 
1 128 ASN n 
1 129 GLU n 
1 130 ASP n 
1 131 LEU n 
1 132 ARG n 
1 133 SER n 
1 134 TRP n 
1 135 THR n 
1 136 ALA n 
1 137 ALA n 
1 138 ASP n 
1 139 MET n 
1 140 ALA n 
1 141 ALA n 
1 142 GLN n 
1 143 ILE n 
1 144 THR n 
1 145 LYS n 
1 146 ARG n 
1 147 LYS n 
1 148 TRP n 
1 149 GLU n 
1 150 ALA n 
1 151 VAL n 
1 152 HIS n 
1 153 ALA n 
1 154 ALA n 
1 155 GLU n 
1 156 GLN n 
1 157 ARG n 
1 158 ARG n 
1 159 VAL n 
1 160 TYR n 
1 161 LEU n 
1 162 GLU n 
1 163 GLY n 
1 164 ARG n 
1 165 CYS n 
1 166 VAL n 
1 167 ASP n 
1 168 GLY n 
1 169 LEU n 
1 170 ARG n 
1 171 ARG n 
1 172 TYR n 
1 173 LEU n 
1 174 GLU n 
1 175 ASN n 
1 176 GLY n 
1 177 LYS n 
1 178 GLU n 
1 179 THR n 
1 180 LEU n 
1 181 GLN n 
1 182 ARG n 
1 183 THR n 
1 184 ASP n 
1 185 PRO n 
1 186 PRO n 
1 187 LYS n 
1 188 THR n 
1 189 HIS n 
1 190 MET n 
1 191 THR n 
1 192 HIS n 
1 193 HIS n 
1 194 PRO n 
1 195 ILE n 
1 196 SER n 
1 197 ASP n 
1 198 HIS n 
1 199 GLU n 
1 200 ALA n 
1 201 THR n 
1 202 LEU n 
1 203 ARG n 
1 204 CYS n 
1 205 TRP n 
1 206 ALA n 
1 207 LEU n 
1 208 GLY n 
1 209 PHE n 
1 210 TYR n 
1 211 PRO n 
1 212 ALA n 
1 213 GLU n 
1 214 ILE n 
1 215 THR n 
1 216 LEU n 
1 217 THR n 
1 218 TRP n 
1 219 GLN n 
1 220 ARG n 
1 221 ASP n 
1 222 GLY n 
1 223 GLU n 
1 224 ASP n 
1 225 GLN n 
1 226 THR n 
1 227 GLN n 
1 228 ASP n 
1 229 THR n 
1 230 GLU n 
1 231 LEU n 
1 232 VAL n 
1 233 GLU n 
1 234 THR n 
1 235 ARG n 
1 236 PRO n 
1 237 ALA n 
1 238 GLY n 
1 239 ASP n 
1 240 GLY n 
1 241 THR n 
1 242 PHE n 
1 243 GLN n 
1 244 LYS n 
1 245 TRP n 
1 246 ALA n 
1 247 ALA n 
1 248 VAL n 
1 249 VAL n 
1 250 VAL n 
1 251 PRO n 
1 252 SER n 
1 253 GLY n 
1 254 GLU n 
1 255 GLU n 
1 256 GLN n 
1 257 ARG n 
1 258 TYR n 
1 259 THR n 
1 260 CYS n 
1 261 HIS n 
1 262 VAL n 
1 263 GLN n 
1 264 HIS n 
1 265 GLU n 
1 266 GLY n 
1 267 LEU n 
1 268 PRO n 
1 269 LYS n 
1 270 PRO n 
1 271 LEU n 
1 272 THR n 
1 273 LEU n 
1 274 ARG n 
1 275 TRP n 
1 276 GLU n 
2 1   MET n 
2 2   ILE n 
2 3   GLN n 
2 4   ARG n 
2 5   THR n 
2 6   PRO n 
2 7   LYS n 
2 8   ILE n 
2 9   GLN n 
2 10  VAL n 
2 11  TYR n 
2 12  SER n 
2 13  ARG n 
2 14  HIS n 
2 15  PRO n 
2 16  ALA n 
2 17  GLU n 
2 18  ASN n 
2 19  GLY n 
2 20  LYS n 
2 21  SER n 
2 22  ASN n 
2 23  PHE n 
2 24  LEU n 
2 25  ASN n 
2 26  CYS n 
2 27  TYR n 
2 28  VAL n 
2 29  SER n 
2 30  GLY n 
2 31  PHE n 
2 32  HIS n 
2 33  PRO n 
2 34  SER n 
2 35  ASP n 
2 36  ILE n 
2 37  GLU n 
2 38  VAL n 
2 39  ASP n 
2 40  LEU n 
2 41  LEU n 
2 42  LYS n 
2 43  ASN n 
2 44  GLY n 
2 45  GLU n 
2 46  ARG n 
2 47  ILE n 
2 48  GLU n 
2 49  LYS n 
2 50  VAL n 
2 51  GLU n 
2 52  HIS n 
2 53  SER n 
2 54  ASP n 
2 55  LEU n 
2 56  SER n 
2 57  PHE n 
2 58  SER n 
2 59  LYS n 
2 60  ASP n 
2 61  TRP n 
2 62  SER n 
2 63  PHE n 
2 64  TYR n 
2 65  LEU n 
2 66  LEU n 
2 67  TYR n 
2 68  TYR n 
2 69  THR n 
2 70  GLU n 
2 71  PHE n 
2 72  THR n 
2 73  PRO n 
2 74  THR n 
2 75  GLU n 
2 76  LYS n 
2 77  ASP n 
2 78  GLU n 
2 79  TYR n 
2 80  ALA n 
2 81  CYS n 
2 82  ARG n 
2 83  VAL n 
2 84  ASN n 
2 85  HIS n 
2 86  VAL n 
2 87  THR n 
2 88  LEU n 
2 89  SER n 
2 90  GLN n 
2 91  PRO n 
2 92  LYS n 
2 93  ILE n 
2 94  VAL n 
2 95  LYS n 
2 96  TRP n 
2 97  ASP n 
2 98  ARG n 
2 99  ASP n 
2 100 MET n 
3 1   ILE n 
3 2   LEU n 
3 3   ASP n 
3 4   THR n 
3 5   ALA n 
3 6   GLY n 
3 7   ARG n 
3 8   GLU n 
3 9   GLU n 
3 10  TYR n 
4 1   MET n 
4 2   GLU n 
4 3   ALA n 
4 4   GLN n 
4 5   VAL n 
4 6   THR n 
4 7   GLN n 
4 8   ASN n 
4 9   PRO n 
4 10  ARG n 
4 11  TYR n 
4 12  LEU n 
4 13  ILE n 
4 14  THR n 
4 15  VAL n 
4 16  THR n 
4 17  GLY n 
4 18  LYS n 
4 19  LYS n 
4 20  LEU n 
4 21  THR n 
4 22  VAL n 
4 23  THR n 
4 24  CYS n 
4 25  SER n 
4 26  GLN n 
4 27  ASN n 
4 28  MET n 
4 29  ASN n 
4 30  HIS n 
4 31  GLU n 
4 32  TYR n 
4 33  MET n 
4 34  SER n 
4 35  TRP n 
4 36  TYR n 
4 37  ARG n 
4 38  GLN n 
4 39  ASP n 
4 40  PRO n 
4 41  GLY n 
4 42  LEU n 
4 43  GLY n 
4 44  LEU n 
4 45  ARG n 
4 46  GLN n 
4 47  ILE n 
4 48  TYR n 
4 49  TYR n 
4 50  SER n 
4 51  MET n 
4 52  ASN n 
4 53  VAL n 
4 54  GLU n 
4 55  VAL n 
4 56  THR n 
4 57  ASP n 
4 58  LYS n 
4 59  GLY n 
4 60  ASP n 
4 61  VAL n 
4 62  PRO n 
4 63  GLU n 
4 64  GLY n 
4 65  TYR n 
4 66  LYS n 
4 67  VAL n 
4 68  SER n 
4 69  ARG n 
4 70  LYS n 
4 71  GLU n 
4 72  LYS n 
4 73  ARG n 
4 74  ASN n 
4 75  PHE n 
4 76  PRO n 
4 77  LEU n 
4 78  ILE n 
4 79  LEU n 
4 80  GLU n 
4 81  SER n 
4 82  PRO n 
4 83  SER n 
4 84  PRO n 
4 85  ASN n 
4 86  GLN n 
4 87  THR n 
4 88  SER n 
4 89  LEU n 
4 90  TYR n 
4 91  PHE n 
4 92  CYS n 
4 93  ALA n 
4 94  SER n 
4 95  SER n 
4 96  LEU n 
4 97  VAL n 
4 98  SER n 
4 99  THR n 
4 100 PRO n 
4 101 LEU n 
4 102 PRO n 
4 103 LYS n 
4 104 GLU n 
4 105 THR n 
4 106 GLN n 
4 107 TYR n 
4 108 PHE n 
4 109 GLY n 
4 110 PRO n 
4 111 GLY n 
4 112 THR n 
4 113 ARG n 
4 114 LEU n 
4 115 LEU n 
4 116 VAL n 
4 117 LEU n 
4 118 GLU n 
4 119 ASP n 
4 120 LEU n 
4 121 LYS n 
4 122 ASN n 
4 123 VAL n 
4 124 PHE n 
4 125 PRO n 
4 126 PRO n 
4 127 GLU n 
4 128 VAL n 
4 129 ALA n 
4 130 VAL n 
4 131 PHE n 
4 132 GLU n 
4 133 PRO n 
4 134 SER n 
4 135 GLU n 
4 136 ALA n 
4 137 GLU n 
4 138 ILE n 
4 139 SER n 
4 140 HIS n 
4 141 THR n 
4 142 GLN n 
4 143 LYS n 
4 144 ALA n 
4 145 THR n 
4 146 LEU n 
4 147 VAL n 
4 148 CYS n 
4 149 LEU n 
4 150 ALA n 
4 151 THR n 
4 152 GLY n 
4 153 PHE n 
4 154 TYR n 
4 155 PRO n 
4 156 ASP n 
4 157 HIS n 
4 158 VAL n 
4 159 GLU n 
4 160 LEU n 
4 161 SER n 
4 162 TRP n 
4 163 TRP n 
4 164 VAL n 
4 165 ASN n 
4 166 GLY n 
4 167 LYS n 
4 168 GLU n 
4 169 VAL n 
4 170 HIS n 
4 171 SER n 
4 172 GLY n 
4 173 VAL n 
4 174 CYS n 
4 175 THR n 
4 176 ASP n 
4 177 PRO n 
4 178 GLN n 
4 179 PRO n 
4 180 LEU n 
4 181 LYS n 
4 182 GLU n 
4 183 GLN n 
4 184 PRO n 
4 185 ALA n 
4 186 LEU n 
4 187 ASN n 
4 188 ASP n 
4 189 SER n 
4 190 ARG n 
4 191 TYR n 
4 192 ALA n 
4 193 LEU n 
4 194 SER n 
4 195 SER n 
4 196 ARG n 
4 197 LEU n 
4 198 ARG n 
4 199 VAL n 
4 200 SER n 
4 201 ALA n 
4 202 THR n 
4 203 PHE n 
4 204 TRP n 
4 205 GLN n 
4 206 ASN n 
4 207 PRO n 
4 208 ARG n 
4 209 ASN n 
4 210 HIS n 
4 211 PHE n 
4 212 ARG n 
4 213 CYS n 
4 214 GLN n 
4 215 VAL n 
4 216 GLN n 
4 217 PHE n 
4 218 TYR n 
4 219 GLY n 
4 220 LEU n 
4 221 SER n 
4 222 GLU n 
4 223 ASN n 
4 224 ASP n 
4 225 GLU n 
4 226 TRP n 
4 227 THR n 
4 228 GLN n 
4 229 ASP n 
4 230 ARG n 
4 231 ALA n 
4 232 LYS n 
4 233 PRO n 
4 234 VAL n 
4 235 THR n 
4 236 GLN n 
4 237 ILE n 
4 238 VAL n 
4 239 SER n 
4 240 ALA n 
4 241 GLU n 
4 242 ALA n 
4 243 TRP n 
4 244 GLY n 
4 245 ARG n 
4 246 ALA n 
4 247 ASP n 
5 1   MET n 
5 2   ALA n 
5 3   GLN n 
5 4   LYS n 
5 5   VAL n 
5 6   THR n 
5 7   GLN n 
5 8   ALA n 
5 9   GLN n 
5 10  SER n 
5 11  SER n 
5 12  VAL n 
5 13  SER n 
5 14  MET n 
5 15  PRO n 
5 16  VAL n 
5 17  ARG n 
5 18  LYS n 
5 19  ALA n 
5 20  VAL n 
5 21  THR n 
5 22  LEU n 
5 23  ASN n 
5 24  CYS n 
5 25  LEU n 
5 26  TYR n 
5 27  GLU n 
5 28  THR n 
5 29  SER n 
5 30  TRP n 
5 31  TRP n 
5 32  SER n 
5 33  TYR n 
5 34  TYR n 
5 35  ILE n 
5 36  PHE n 
5 37  TRP n 
5 38  TYR n 
5 39  LYS n 
5 40  GLN n 
5 41  LEU n 
5 42  PRO n 
5 43  SER n 
5 44  LYS n 
5 45  GLU n 
5 46  MET n 
5 47  ILE n 
5 48  PHE n 
5 49  LEU n 
5 50  ILE n 
5 51  ARG n 
5 52  GLN n 
5 53  GLY n 
5 54  SER n 
5 55  ASP n 
5 56  GLU n 
5 57  GLN n 
5 58  ASN n 
5 59  ALA n 
5 60  LYS n 
5 61  SER n 
5 62  GLY n 
5 63  ARG n 
5 64  TYR n 
5 65  SER n 
5 66  VAL n 
5 67  ASN n 
5 68  PHE n 
5 69  LYS n 
5 70  LYS n 
5 71  ALA n 
5 72  ALA n 
5 73  LYS n 
5 74  SER n 
5 75  VAL n 
5 76  ALA n 
5 77  LEU n 
5 78  THR n 
5 79  ILE n 
5 80  SER n 
5 81  ALA n 
5 82  LEU n 
5 83  GLN n 
5 84  LEU n 
5 85  GLU n 
5 86  ASP n 
5 87  SER n 
5 88  ALA n 
5 89  LYS n 
5 90  TYR n 
5 91  PHE n 
5 92  CYS n 
5 93  ALA n 
5 94  LEU n 
5 95  GLY n 
5 96  ASP n 
5 97  THR n 
5 98  ALA n 
5 99  GLY n 
5 100 LYS n 
5 101 SER n 
5 102 THR n 
5 103 PHE n 
5 104 GLY n 
5 105 ASP n 
5 106 GLY n 
5 107 THR n 
5 108 THR n 
5 109 LEU n 
5 110 THR n 
5 111 VAL n 
5 112 LYS n 
5 113 PRO n 
5 114 ASN n 
5 115 ILE n 
5 116 GLN n 
5 117 ASN n 
5 118 PRO n 
5 119 ASP n 
5 120 PRO n 
5 121 ALA n 
5 122 VAL n 
5 123 TYR n 
5 124 GLN n 
5 125 LEU n 
5 126 ARG n 
5 127 ASP n 
5 128 SER n 
5 129 LYS n 
5 130 SER n 
5 131 SER n 
5 132 ASP n 
5 133 LYS n 
5 134 SER n 
5 135 VAL n 
5 136 CYS n 
5 137 LEU n 
5 138 PHE n 
5 139 THR n 
5 140 ASP n 
5 141 PHE n 
5 142 ASP n 
5 143 SER n 
5 144 GLN n 
5 145 THR n 
5 146 ASN n 
5 147 VAL n 
5 148 SER n 
5 149 GLN n 
5 150 SER n 
5 151 LYS n 
5 152 ASP n 
5 153 SER n 
5 154 ASP n 
5 155 VAL n 
5 156 TYR n 
5 157 ILE n 
5 158 THR n 
5 159 ASP n 
5 160 LYS n 
5 161 CYS n 
5 162 VAL n 
5 163 LEU n 
5 164 ASP n 
5 165 MET n 
5 166 ARG n 
5 167 SER n 
5 168 MET n 
5 169 ASP n 
5 170 PHE n 
5 171 LYS n 
5 172 SER n 
5 173 ASN n 
5 174 SER n 
5 175 ALA n 
5 176 VAL n 
5 177 ALA n 
5 178 TRP n 
5 179 SER n 
5 180 ASN n 
5 181 LYS n 
5 182 SER n 
5 183 ASP n 
5 184 PHE n 
5 185 ALA n 
5 186 CYS n 
5 187 ALA n 
5 188 ASN n 
5 189 ALA n 
5 190 PHE n 
5 191 ASN n 
5 192 ASN n 
5 193 SER n 
5 194 ILE n 
5 195 ILE n 
5 196 PRO n 
5 197 GLU n 
5 198 ASP n 
5 199 THR n 
5 200 PHE n 
5 201 PHE n 
5 202 PRO n 
5 203 SER n 
5 204 PRO n 
5 205 GLU n 
5 206 SER n 
5 207 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 276 human ? HLA-A ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 100 human ? B2M   ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 247 ?     ? ?     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5 1 sample 'Biological sequence' 1 207 ?     ? ?     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       10 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   GLY 2   1   1   GLY GLY A . n 
A 1 3   SER 3   2   2   SER SER A . n 
A 1 4   HIS 4   3   3   HIS HIS A . n 
A 1 5   SER 5   4   4   SER SER A . n 
A 1 6   MET 6   5   5   MET MET A . n 
A 1 7   ARG 7   6   6   ARG ARG A . n 
A 1 8   TYR 8   7   7   TYR TYR A . n 
A 1 9   PHE 9   8   8   PHE PHE A . n 
A 1 10  PHE 10  9   9   PHE PHE A . n 
A 1 11  THR 11  10  10  THR THR A . n 
A 1 12  SER 12  11  11  SER SER A . n 
A 1 13  VAL 13  12  12  VAL VAL A . n 
A 1 14  SER 14  13  13  SER SER A . n 
A 1 15  ARG 15  14  14  ARG ARG A . n 
A 1 16  PRO 16  15  15  PRO PRO A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ARG 18  17  17  ARG ARG A . n 
A 1 19  GLY 19  18  18  GLY GLY A . n 
A 1 20  GLU 20  19  19  GLU GLU A . n 
A 1 21  PRO 21  20  20  PRO PRO A . n 
A 1 22  ARG 22  21  21  ARG ARG A . n 
A 1 23  PHE 23  22  22  PHE PHE A . n 
A 1 24  ILE 24  23  23  ILE ILE A . n 
A 1 25  ALA 25  24  24  ALA ALA A . n 
A 1 26  VAL 26  25  25  VAL VAL A . n 
A 1 27  GLY 27  26  26  GLY GLY A . n 
A 1 28  TYR 28  27  27  TYR TYR A . n 
A 1 29  VAL 29  28  28  VAL VAL A . n 
A 1 30  ASP 30  29  29  ASP ASP A . n 
A 1 31  ASP 31  30  30  ASP ASP A . n 
A 1 32  THR 32  31  31  THR THR A . n 
A 1 33  GLN 33  32  32  GLN GLN A . n 
A 1 34  PHE 34  33  33  PHE PHE A . n 
A 1 35  VAL 35  34  34  VAL VAL A . n 
A 1 36  ARG 36  35  35  ARG ARG A . n 
A 1 37  PHE 37  36  36  PHE PHE A . n 
A 1 38  ASP 38  37  37  ASP ASP A . n 
A 1 39  SER 39  38  38  SER SER A . n 
A 1 40  ASP 40  39  39  ASP ASP A . n 
A 1 41  ALA 41  40  40  ALA ALA A . n 
A 1 42  ALA 42  41  41  ALA ALA A . n 
A 1 43  SER 43  42  42  SER SER A . n 
A 1 44  GLN 44  43  43  GLN GLN A . n 
A 1 45  LYS 45  44  44  LYS LYS A . n 
A 1 46  MET 46  45  45  MET MET A . n 
A 1 47  GLU 47  46  46  GLU GLU A . n 
A 1 48  PRO 48  47  47  PRO PRO A . n 
A 1 49  ARG 49  48  48  ARG ARG A . n 
A 1 50  ALA 50  49  49  ALA ALA A . n 
A 1 51  PRO 51  50  50  PRO PRO A . n 
A 1 52  TRP 52  51  51  TRP TRP A . n 
A 1 53  ILE 53  52  52  ILE ILE A . n 
A 1 54  GLU 54  53  53  GLU GLU A . n 
A 1 55  GLN 55  54  54  GLN GLN A . n 
A 1 56  GLU 56  55  55  GLU GLU A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  PRO 58  57  57  PRO PRO A . n 
A 1 59  GLU 59  58  58  GLU GLU A . n 
A 1 60  TYR 60  59  59  TYR TYR A . n 
A 1 61  TRP 61  60  60  TRP TRP A . n 
A 1 62  ASP 62  61  61  ASP ASP A . n 
A 1 63  GLN 63  62  62  GLN GLN A . n 
A 1 64  GLU 64  63  63  GLU GLU A . n 
A 1 65  THR 65  64  64  THR THR A . n 
A 1 66  ARG 66  65  65  ARG ARG A . n 
A 1 67  ASN 67  66  66  ASN ASN A . n 
A 1 68  MET 68  67  67  MET MET A . n 
A 1 69  LYS 69  68  68  LYS LYS A . n 
A 1 70  ALA 70  69  69  ALA ALA A . n 
A 1 71  HIS 71  70  70  HIS HIS A . n 
A 1 72  SER 72  71  71  SER SER A . n 
A 1 73  GLN 73  72  72  GLN GLN A . n 
A 1 74  THR 74  73  73  THR THR A . n 
A 1 75  ASP 75  74  74  ASP ASP A . n 
A 1 76  ARG 76  75  75  ARG ARG A . n 
A 1 77  ALA 77  76  76  ALA ALA A . n 
A 1 78  ASN 78  77  77  ASN ASN A . n 
A 1 79  LEU 79  78  78  LEU LEU A . n 
A 1 80  GLY 80  79  79  GLY GLY A . n 
A 1 81  THR 81  80  80  THR THR A . n 
A 1 82  LEU 82  81  81  LEU LEU A . n 
A 1 83  ARG 83  82  82  ARG ARG A . n 
A 1 84  GLY 84  83  83  GLY GLY A . n 
A 1 85  TYR 85  84  84  TYR TYR A . n 
A 1 86  TYR 86  85  85  TYR TYR A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  GLN 88  87  87  GLN GLN A . n 
A 1 89  SER 89  88  88  SER SER A . n 
A 1 90  GLU 90  89  89  GLU GLU A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  GLY 92  91  91  GLY GLY A . n 
A 1 93  SER 93  92  92  SER SER A . n 
A 1 94  HIS 94  93  93  HIS HIS A . n 
A 1 95  THR 95  94  94  THR THR A . n 
A 1 96  ILE 96  95  95  ILE ILE A . n 
A 1 97  GLN 97  96  96  GLN GLN A . n 
A 1 98  ILE 98  97  97  ILE ILE A . n 
A 1 99  MET 99  98  98  MET MET A . n 
A 1 100 TYR 100 99  99  TYR TYR A . n 
A 1 101 GLY 101 100 100 GLY GLY A . n 
A 1 102 CYS 102 101 101 CYS CYS A . n 
A 1 103 ASP 103 102 102 ASP ASP A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 GLY 105 104 104 GLY GLY A . n 
A 1 106 PRO 106 105 105 PRO PRO A . n 
A 1 107 ASP 107 106 106 ASP ASP A . n 
A 1 108 GLY 108 107 107 GLY GLY A . n 
A 1 109 ARG 109 108 108 ARG ARG A . n 
A 1 110 PHE 110 109 109 PHE PHE A . n 
A 1 111 LEU 111 110 110 LEU LEU A . n 
A 1 112 ARG 112 111 111 ARG ARG A . n 
A 1 113 GLY 113 112 112 GLY GLY A . n 
A 1 114 TYR 114 113 113 TYR TYR A . n 
A 1 115 ARG 115 114 114 ARG ARG A . n 
A 1 116 GLN 116 115 115 GLN GLN A . n 
A 1 117 ASP 117 116 116 ASP ASP A . n 
A 1 118 ALA 118 117 117 ALA ALA A . n 
A 1 119 TYR 119 118 118 TYR TYR A . n 
A 1 120 ASP 120 119 119 ASP ASP A . n 
A 1 121 GLY 121 120 120 GLY GLY A . n 
A 1 122 LYS 122 121 121 LYS LYS A . n 
A 1 123 ASP 123 122 122 ASP ASP A . n 
A 1 124 TYR 124 123 123 TYR TYR A . n 
A 1 125 ILE 125 124 124 ILE ILE A . n 
A 1 126 ALA 126 125 125 ALA ALA A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 ASN 128 127 127 ASN ASN A . n 
A 1 129 GLU 129 128 128 GLU GLU A . n 
A 1 130 ASP 130 129 129 ASP ASP A . n 
A 1 131 LEU 131 130 130 LEU LEU A . n 
A 1 132 ARG 132 131 131 ARG ARG A . n 
A 1 133 SER 133 132 132 SER SER A . n 
A 1 134 TRP 134 133 133 TRP TRP A . n 
A 1 135 THR 135 134 134 THR THR A . n 
A 1 136 ALA 136 135 135 ALA ALA A . n 
A 1 137 ALA 137 136 136 ALA ALA A . n 
A 1 138 ASP 138 137 137 ASP ASP A . n 
A 1 139 MET 139 138 138 MET MET A . n 
A 1 140 ALA 140 139 139 ALA ALA A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLN 142 141 141 GLN GLN A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 THR 144 143 143 THR THR A . n 
A 1 145 LYS 145 144 144 LYS LYS A . n 
A 1 146 ARG 146 145 145 ARG ARG A . n 
A 1 147 LYS 147 146 146 LYS LYS A . n 
A 1 148 TRP 148 147 147 TRP TRP A . n 
A 1 149 GLU 149 148 148 GLU GLU A . n 
A 1 150 ALA 150 149 149 ALA ALA A . n 
A 1 151 VAL 151 150 150 VAL VAL A . n 
A 1 152 HIS 152 151 151 HIS HIS A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 ALA 154 153 153 ALA ALA A . n 
A 1 155 GLU 155 154 154 GLU GLU A . n 
A 1 156 GLN 156 155 155 GLN GLN A . n 
A 1 157 ARG 157 156 156 ARG ARG A . n 
A 1 158 ARG 158 157 157 ARG ARG A . n 
A 1 159 VAL 159 158 158 VAL VAL A . n 
A 1 160 TYR 160 159 159 TYR TYR A . n 
A 1 161 LEU 161 160 160 LEU LEU A . n 
A 1 162 GLU 162 161 161 GLU GLU A . n 
A 1 163 GLY 163 162 162 GLY GLY A . n 
A 1 164 ARG 164 163 163 ARG ARG A . n 
A 1 165 CYS 165 164 164 CYS CYS A . n 
A 1 166 VAL 166 165 165 VAL VAL A . n 
A 1 167 ASP 167 166 166 ASP ASP A . n 
A 1 168 GLY 168 167 167 GLY GLY A . n 
A 1 169 LEU 169 168 168 LEU LEU A . n 
A 1 170 ARG 170 169 169 ARG ARG A . n 
A 1 171 ARG 171 170 170 ARG ARG A . n 
A 1 172 TYR 172 171 171 TYR TYR A . n 
A 1 173 LEU 173 172 172 LEU LEU A . n 
A 1 174 GLU 174 173 173 GLU GLU A . n 
A 1 175 ASN 175 174 174 ASN ASN A . n 
A 1 176 GLY 176 175 175 GLY GLY A . n 
A 1 177 LYS 177 176 176 LYS LYS A . n 
A 1 178 GLU 178 177 177 GLU GLU A . n 
A 1 179 THR 179 178 178 THR THR A . n 
A 1 180 LEU 180 179 179 LEU LEU A . n 
A 1 181 GLN 181 180 180 GLN GLN A . n 
A 1 182 ARG 182 181 181 ARG ARG A . n 
A 1 183 THR 183 182 182 THR THR A . n 
A 1 184 ASP 184 183 183 ASP ASP A . n 
A 1 185 PRO 185 184 184 PRO PRO A . n 
A 1 186 PRO 186 185 185 PRO PRO A . n 
A 1 187 LYS 187 186 186 LYS LYS A . n 
A 1 188 THR 188 187 187 THR THR A . n 
A 1 189 HIS 189 188 188 HIS HIS A . n 
A 1 190 MET 190 189 189 MET MET A . n 
A 1 191 THR 191 190 190 THR THR A . n 
A 1 192 HIS 192 191 191 HIS HIS A . n 
A 1 193 HIS 193 192 192 HIS HIS A . n 
A 1 194 PRO 194 193 193 PRO PRO A . n 
A 1 195 ILE 195 194 194 ILE ILE A . n 
A 1 196 SER 196 195 195 SER SER A . n 
A 1 197 ASP 197 196 196 ASP ASP A . n 
A 1 198 HIS 198 197 197 HIS HIS A . n 
A 1 199 GLU 199 198 198 GLU GLU A . n 
A 1 200 ALA 200 199 199 ALA ALA A . n 
A 1 201 THR 201 200 200 THR THR A . n 
A 1 202 LEU 202 201 201 LEU LEU A . n 
A 1 203 ARG 203 202 202 ARG ARG A . n 
A 1 204 CYS 204 203 203 CYS CYS A . n 
A 1 205 TRP 205 204 204 TRP TRP A . n 
A 1 206 ALA 206 205 205 ALA ALA A . n 
A 1 207 LEU 207 206 206 LEU LEU A . n 
A 1 208 GLY 208 207 207 GLY GLY A . n 
A 1 209 PHE 209 208 208 PHE PHE A . n 
A 1 210 TYR 210 209 209 TYR TYR A . n 
A 1 211 PRO 211 210 210 PRO PRO A . n 
A 1 212 ALA 212 211 211 ALA ALA A . n 
A 1 213 GLU 213 212 212 GLU GLU A . n 
A 1 214 ILE 214 213 213 ILE ILE A . n 
A 1 215 THR 215 214 214 THR THR A . n 
A 1 216 LEU 216 215 215 LEU LEU A . n 
A 1 217 THR 217 216 216 THR THR A . n 
A 1 218 TRP 218 217 217 TRP TRP A . n 
A 1 219 GLN 219 218 218 GLN GLN A . n 
A 1 220 ARG 220 219 219 ARG ARG A . n 
A 1 221 ASP 221 220 220 ASP ASP A . n 
A 1 222 GLY 222 221 221 GLY GLY A . n 
A 1 223 GLU 223 222 222 GLU GLU A . n 
A 1 224 ASP 224 223 223 ASP ASP A . n 
A 1 225 GLN 225 224 224 GLN GLN A . n 
A 1 226 THR 226 225 225 THR THR A . n 
A 1 227 GLN 227 226 226 GLN GLN A . n 
A 1 228 ASP 228 227 227 ASP ASP A . n 
A 1 229 THR 229 228 228 THR THR A . n 
A 1 230 GLU 230 229 229 GLU GLU A . n 
A 1 231 LEU 231 230 230 LEU LEU A . n 
A 1 232 VAL 232 231 231 VAL VAL A . n 
A 1 233 GLU 233 232 232 GLU GLU A . n 
A 1 234 THR 234 233 233 THR THR A . n 
A 1 235 ARG 235 234 234 ARG ARG A . n 
A 1 236 PRO 236 235 235 PRO PRO A . n 
A 1 237 ALA 237 236 236 ALA ALA A . n 
A 1 238 GLY 238 237 237 GLY GLY A . n 
A 1 239 ASP 239 238 238 ASP ASP A . n 
A 1 240 GLY 240 239 239 GLY GLY A . n 
A 1 241 THR 241 240 240 THR THR A . n 
A 1 242 PHE 242 241 241 PHE PHE A . n 
A 1 243 GLN 243 242 242 GLN GLN A . n 
A 1 244 LYS 244 243 243 LYS LYS A . n 
A 1 245 TRP 245 244 244 TRP TRP A . n 
A 1 246 ALA 246 245 245 ALA ALA A . n 
A 1 247 ALA 247 246 246 ALA ALA A . n 
A 1 248 VAL 248 247 247 VAL VAL A . n 
A 1 249 VAL 249 248 248 VAL VAL A . n 
A 1 250 VAL 250 249 249 VAL VAL A . n 
A 1 251 PRO 251 250 250 PRO PRO A . n 
A 1 252 SER 252 251 251 SER SER A . n 
A 1 253 GLY 253 252 252 GLY GLY A . n 
A 1 254 GLU 254 253 253 GLU GLU A . n 
A 1 255 GLU 255 254 254 GLU GLU A . n 
A 1 256 GLN 256 255 255 GLN GLN A . n 
A 1 257 ARG 257 256 256 ARG ARG A . n 
A 1 258 TYR 258 257 257 TYR TYR A . n 
A 1 259 THR 259 258 258 THR THR A . n 
A 1 260 CYS 260 259 259 CYS CYS A . n 
A 1 261 HIS 261 260 260 HIS HIS A . n 
A 1 262 VAL 262 261 261 VAL VAL A . n 
A 1 263 GLN 263 262 262 GLN GLN A . n 
A 1 264 HIS 264 263 263 HIS HIS A . n 
A 1 265 GLU 265 264 264 GLU GLU A . n 
A 1 266 GLY 266 265 265 GLY GLY A . n 
A 1 267 LEU 267 266 266 LEU LEU A . n 
A 1 268 PRO 268 267 267 PRO PRO A . n 
A 1 269 LYS 269 268 268 LYS LYS A . n 
A 1 270 PRO 270 269 269 PRO PRO A . n 
A 1 271 LEU 271 270 270 LEU LEU A . n 
A 1 272 THR 272 271 271 THR THR A . n 
A 1 273 LEU 273 272 272 LEU LEU A . n 
A 1 274 ARG 274 273 273 ARG ARG A . n 
A 1 275 TRP 275 274 274 TRP TRP A . n 
A 1 276 GLU 276 275 275 GLU GLU A . n 
B 2 1   MET 1   0   0   MET MET B . n 
B 2 2   ILE 2   1   1   ILE ILE B . n 
B 2 3   GLN 3   2   2   GLN GLN B . n 
B 2 4   ARG 4   3   3   ARG ARG B . n 
B 2 5   THR 5   4   4   THR THR B . n 
B 2 6   PRO 6   5   5   PRO PRO B . n 
B 2 7   LYS 7   6   6   LYS LYS B . n 
B 2 8   ILE 8   7   7   ILE ILE B . n 
B 2 9   GLN 9   8   8   GLN GLN B . n 
B 2 10  VAL 10  9   9   VAL VAL B . n 
B 2 11  TYR 11  10  10  TYR TYR B . n 
B 2 12  SER 12  11  11  SER SER B . n 
B 2 13  ARG 13  12  12  ARG ARG B . n 
B 2 14  HIS 14  13  13  HIS HIS B . n 
B 2 15  PRO 15  14  14  PRO PRO B . n 
B 2 16  ALA 16  15  15  ALA ALA B . n 
B 2 17  GLU 17  16  16  GLU GLU B . n 
B 2 18  ASN 18  17  17  ASN ASN B . n 
B 2 19  GLY 19  18  18  GLY GLY B . n 
B 2 20  LYS 20  19  19  LYS LYS B . n 
B 2 21  SER 21  20  20  SER SER B . n 
B 2 22  ASN 22  21  21  ASN ASN B . n 
B 2 23  PHE 23  22  22  PHE PHE B . n 
B 2 24  LEU 24  23  23  LEU LEU B . n 
B 2 25  ASN 25  24  24  ASN ASN B . n 
B 2 26  CYS 26  25  25  CYS CYS B . n 
B 2 27  TYR 27  26  26  TYR TYR B . n 
B 2 28  VAL 28  27  27  VAL VAL B . n 
B 2 29  SER 29  28  28  SER SER B . n 
B 2 30  GLY 30  29  29  GLY GLY B . n 
B 2 31  PHE 31  30  30  PHE PHE B . n 
B 2 32  HIS 32  31  31  HIS HIS B . n 
B 2 33  PRO 33  32  32  PRO PRO B . n 
B 2 34  SER 34  33  33  SER SER B . n 
B 2 35  ASP 35  34  34  ASP ASP B . n 
B 2 36  ILE 36  35  35  ILE ILE B . n 
B 2 37  GLU 37  36  36  GLU GLU B . n 
B 2 38  VAL 38  37  37  VAL VAL B . n 
B 2 39  ASP 39  38  38  ASP ASP B . n 
B 2 40  LEU 40  39  39  LEU LEU B . n 
B 2 41  LEU 41  40  40  LEU LEU B . n 
B 2 42  LYS 42  41  41  LYS LYS B . n 
B 2 43  ASN 43  42  42  ASN ASN B . n 
B 2 44  GLY 44  43  43  GLY GLY B . n 
B 2 45  GLU 45  44  44  GLU GLU B . n 
B 2 46  ARG 46  45  45  ARG ARG B . n 
B 2 47  ILE 47  46  46  ILE ILE B . n 
B 2 48  GLU 48  47  47  GLU GLU B . n 
B 2 49  LYS 49  48  48  LYS LYS B . n 
B 2 50  VAL 50  49  49  VAL VAL B . n 
B 2 51  GLU 51  50  50  GLU GLU B . n 
B 2 52  HIS 52  51  51  HIS HIS B . n 
B 2 53  SER 53  52  52  SER SER B . n 
B 2 54  ASP 54  53  53  ASP ASP B . n 
B 2 55  LEU 55  54  54  LEU LEU B . n 
B 2 56  SER 56  55  55  SER SER B . n 
B 2 57  PHE 57  56  56  PHE PHE B . n 
B 2 58  SER 58  57  57  SER SER B . n 
B 2 59  LYS 59  58  58  LYS LYS B . n 
B 2 60  ASP 60  59  59  ASP ASP B . n 
B 2 61  TRP 61  60  60  TRP TRP B . n 
B 2 62  SER 62  61  61  SER SER B . n 
B 2 63  PHE 63  62  62  PHE PHE B . n 
B 2 64  TYR 64  63  63  TYR TYR B . n 
B 2 65  LEU 65  64  64  LEU LEU B . n 
B 2 66  LEU 66  65  65  LEU LEU B . n 
B 2 67  TYR 67  66  66  TYR TYR B . n 
B 2 68  TYR 68  67  67  TYR TYR B . n 
B 2 69  THR 69  68  68  THR THR B . n 
B 2 70  GLU 70  69  69  GLU GLU B . n 
B 2 71  PHE 71  70  70  PHE PHE B . n 
B 2 72  THR 72  71  71  THR THR B . n 
B 2 73  PRO 73  72  72  PRO PRO B . n 
B 2 74  THR 74  73  73  THR THR B . n 
B 2 75  GLU 75  74  74  GLU GLU B . n 
B 2 76  LYS 76  75  75  LYS LYS B . n 
B 2 77  ASP 77  76  76  ASP ASP B . n 
B 2 78  GLU 78  77  77  GLU GLU B . n 
B 2 79  TYR 79  78  78  TYR TYR B . n 
B 2 80  ALA 80  79  79  ALA ALA B . n 
B 2 81  CYS 81  80  80  CYS CYS B . n 
B 2 82  ARG 82  81  81  ARG ARG B . n 
B 2 83  VAL 83  82  82  VAL VAL B . n 
B 2 84  ASN 84  83  83  ASN ASN B . n 
B 2 85  HIS 85  84  84  HIS HIS B . n 
B 2 86  VAL 86  85  85  VAL VAL B . n 
B 2 87  THR 87  86  86  THR THR B . n 
B 2 88  LEU 88  87  87  LEU LEU B . n 
B 2 89  SER 89  88  88  SER SER B . n 
B 2 90  GLN 90  89  89  GLN GLN B . n 
B 2 91  PRO 91  90  90  PRO PRO B . n 
B 2 92  LYS 92  91  91  LYS LYS B . n 
B 2 93  ILE 93  92  92  ILE ILE B . n 
B 2 94  VAL 94  93  93  VAL VAL B . n 
B 2 95  LYS 95  94  94  LYS LYS B . n 
B 2 96  TRP 96  95  95  TRP TRP B . n 
B 2 97  ASP 97  96  96  ASP ASP B . n 
B 2 98  ARG 98  97  97  ARG ARG B . n 
B 2 99  ASP 99  98  98  ASP ASP B . n 
B 2 100 MET 100 99  99  MET MET B . n 
C 3 1   ILE 1   1   1   ILE ILE C . n 
C 3 2   LEU 2   2   2   LEU LEU C . n 
C 3 3   ASP 3   3   3   ASP ASP C . n 
C 3 4   THR 4   4   4   THR THR C . n 
C 3 5   ALA 5   5   5   ALA ALA C . n 
C 3 6   GLY 6   6   6   GLY GLY C . n 
C 3 7   ARG 7   7   7   ARG ARG C . n 
C 3 8   GLU 8   8   8   GLU GLU C . n 
C 3 9   GLU 9   9   9   GLU GLU C . n 
C 3 10  TYR 10  10  10  TYR TYR C . n 
D 4 1   MET 1   0   ?   ?   ?   E . n 
D 4 2   GLU 2   1   ?   ?   ?   E . n 
D 4 3   ALA 3   2   2   ALA ALA E . n 
D 4 4   GLN 4   3   3   GLN GLN E . n 
D 4 5   VAL 5   4   4   VAL VAL E . n 
D 4 6   THR 6   5   5   THR THR E . n 
D 4 7   GLN 7   6   6   GLN GLN E . n 
D 4 8   ASN 8   7   7   ASN ASN E . n 
D 4 9   PRO 9   8   8   PRO PRO E . n 
D 4 10  ARG 10  9   9   ARG ARG E . n 
D 4 11  TYR 11  10  10  TYR TYR E . n 
D 4 12  LEU 12  11  11  LEU LEU E . n 
D 4 13  ILE 13  12  12  ILE ILE E . n 
D 4 14  THR 14  13  13  THR THR E . n 
D 4 15  VAL 15  14  14  VAL VAL E . n 
D 4 16  THR 16  15  15  THR THR E . n 
D 4 17  GLY 17  16  16  GLY GLY E . n 
D 4 18  LYS 18  17  17  LYS LYS E . n 
D 4 19  LYS 19  18  18  LYS LYS E . n 
D 4 20  LEU 20  19  19  LEU LEU E . n 
D 4 21  THR 21  20  20  THR THR E . n 
D 4 22  VAL 22  21  21  VAL VAL E . n 
D 4 23  THR 23  22  22  THR THR E . n 
D 4 24  CYS 24  23  23  CYS CYS E . n 
D 4 25  SER 25  24  24  SER SER E . n 
D 4 26  GLN 26  25  25  GLN GLN E . n 
D 4 27  ASN 27  26  26  ASN ASN E . n 
D 4 28  MET 28  27  27  MET MET E . n 
D 4 29  ASN 29  28  28  ASN ASN E . n 
D 4 30  HIS 30  29  29  HIS HIS E . n 
D 4 31  GLU 31  30  30  GLU GLU E . n 
D 4 32  TYR 32  31  31  TYR TYR E . n 
D 4 33  MET 33  32  32  MET MET E . n 
D 4 34  SER 34  33  33  SER SER E . n 
D 4 35  TRP 35  34  34  TRP TRP E . n 
D 4 36  TYR 36  35  35  TYR TYR E . n 
D 4 37  ARG 37  36  36  ARG ARG E . n 
D 4 38  GLN 38  37  37  GLN GLN E . n 
D 4 39  ASP 39  38  38  ASP ASP E . n 
D 4 40  PRO 40  39  39  PRO PRO E . n 
D 4 41  GLY 41  40  40  GLY GLY E . n 
D 4 42  LEU 42  41  41  LEU LEU E . n 
D 4 43  GLY 43  42  42  GLY GLY E . n 
D 4 44  LEU 44  43  43  LEU LEU E . n 
D 4 45  ARG 45  44  44  ARG ARG E . n 
D 4 46  GLN 46  45  45  GLN GLN E . n 
D 4 47  ILE 47  46  46  ILE ILE E . n 
D 4 48  TYR 48  47  47  TYR TYR E . n 
D 4 49  TYR 49  48  48  TYR TYR E . n 
D 4 50  SER 50  49  49  SER SER E . n 
D 4 51  MET 51  50  50  MET MET E . n 
D 4 52  ASN 52  51  51  ASN ASN E . n 
D 4 53  VAL 53  52  52  VAL VAL E . n 
D 4 54  GLU 54  53  53  GLU GLU E . n 
D 4 55  VAL 55  54  54  VAL VAL E . n 
D 4 56  THR 56  55  55  THR THR E . n 
D 4 57  ASP 57  56  56  ASP ASP E . n 
D 4 58  LYS 58  57  57  LYS LYS E . n 
D 4 59  GLY 59  58  58  GLY GLY E . n 
D 4 60  ASP 60  59  59  ASP ASP E . n 
D 4 61  VAL 61  60  60  VAL VAL E . n 
D 4 62  PRO 62  61  61  PRO PRO E . n 
D 4 63  GLU 63  62  62  GLU GLU E . n 
D 4 64  GLY 64  63  63  GLY GLY E . n 
D 4 65  TYR 65  64  64  TYR TYR E . n 
D 4 66  LYS 66  65  65  LYS LYS E . n 
D 4 67  VAL 67  66  66  VAL VAL E . n 
D 4 68  SER 68  67  67  SER SER E . n 
D 4 69  ARG 69  68  68  ARG ARG E . n 
D 4 70  LYS 70  69  69  LYS LYS E . n 
D 4 71  GLU 71  70  70  GLU GLU E . n 
D 4 72  LYS 72  71  71  LYS LYS E . n 
D 4 73  ARG 73  72  72  ARG ARG E . n 
D 4 74  ASN 74  73  73  ASN ASN E . n 
D 4 75  PHE 75  74  74  PHE PHE E . n 
D 4 76  PRO 76  75  75  PRO PRO E . n 
D 4 77  LEU 77  76  76  LEU LEU E . n 
D 4 78  ILE 78  77  77  ILE ILE E . n 
D 4 79  LEU 79  78  78  LEU LEU E . n 
D 4 80  GLU 80  79  79  GLU GLU E . n 
D 4 81  SER 81  80  80  SER SER E . n 
D 4 82  PRO 82  81  81  PRO PRO E . n 
D 4 83  SER 83  82  82  SER SER E . n 
D 4 84  PRO 84  83  83  PRO PRO E . n 
D 4 85  ASN 85  84  84  ASN ASN E . n 
D 4 86  GLN 86  85  85  GLN GLN E . n 
D 4 87  THR 87  86  86  THR THR E . n 
D 4 88  SER 88  87  87  SER SER E . n 
D 4 89  LEU 89  88  88  LEU LEU E . n 
D 4 90  TYR 90  89  89  TYR TYR E . n 
D 4 91  PHE 91  90  90  PHE PHE E . n 
D 4 92  CYS 92  91  91  CYS CYS E . n 
D 4 93  ALA 93  92  92  ALA ALA E . n 
D 4 94  SER 94  93  93  SER SER E . n 
D 4 95  SER 95  94  94  SER SER E . n 
D 4 96  LEU 96  95  95  LEU LEU E . n 
D 4 97  VAL 97  96  96  VAL VAL E . n 
D 4 98  SER 98  97  97  SER SER E . n 
D 4 99  THR 99  98  98  THR THR E . n 
D 4 100 PRO 100 99  99  PRO PRO E . n 
D 4 101 LEU 101 100 100 LEU LEU E . n 
D 4 102 PRO 102 101 101 PRO PRO E . n 
D 4 103 LYS 103 102 102 LYS LYS E . n 
D 4 104 GLU 104 103 103 GLU GLU E . n 
D 4 105 THR 105 104 104 THR THR E . n 
D 4 106 GLN 106 105 105 GLN GLN E . n 
D 4 107 TYR 107 106 106 TYR TYR E . n 
D 4 108 PHE 108 107 107 PHE PHE E . n 
D 4 109 GLY 109 108 108 GLY GLY E . n 
D 4 110 PRO 110 109 109 PRO PRO E . n 
D 4 111 GLY 111 110 110 GLY GLY E . n 
D 4 112 THR 112 111 111 THR THR E . n 
D 4 113 ARG 113 112 112 ARG ARG E . n 
D 4 114 LEU 114 113 113 LEU LEU E . n 
D 4 115 LEU 115 114 114 LEU LEU E . n 
D 4 116 VAL 116 115 115 VAL VAL E . n 
D 4 117 LEU 117 116 116 LEU LEU E . n 
D 4 118 GLU 118 117 117 GLU GLU E . n 
D 4 119 ASP 119 118 118 ASP ASP E . n 
D 4 120 LEU 120 119 119 LEU LEU E . n 
D 4 121 LYS 121 120 120 LYS LYS E . n 
D 4 122 ASN 122 121 121 ASN ASN E . n 
D 4 123 VAL 123 122 122 VAL VAL E . n 
D 4 124 PHE 124 123 123 PHE PHE E . n 
D 4 125 PRO 125 124 124 PRO PRO E . n 
D 4 126 PRO 126 125 125 PRO PRO E . n 
D 4 127 GLU 127 126 126 GLU GLU E . n 
D 4 128 VAL 128 127 127 VAL VAL E . n 
D 4 129 ALA 129 128 128 ALA ALA E . n 
D 4 130 VAL 130 129 129 VAL VAL E . n 
D 4 131 PHE 131 130 130 PHE PHE E . n 
D 4 132 GLU 132 131 131 GLU GLU E . n 
D 4 133 PRO 133 132 132 PRO PRO E . n 
D 4 134 SER 134 133 133 SER SER E . n 
D 4 135 GLU 135 134 134 GLU GLU E . n 
D 4 136 ALA 136 135 135 ALA ALA E . n 
D 4 137 GLU 137 136 136 GLU GLU E . n 
D 4 138 ILE 138 137 137 ILE ILE E . n 
D 4 139 SER 139 138 138 SER SER E . n 
D 4 140 HIS 140 139 139 HIS HIS E . n 
D 4 141 THR 141 140 140 THR THR E . n 
D 4 142 GLN 142 141 141 GLN GLN E . n 
D 4 143 LYS 143 142 142 LYS LYS E . n 
D 4 144 ALA 144 143 143 ALA ALA E . n 
D 4 145 THR 145 144 144 THR THR E . n 
D 4 146 LEU 146 145 145 LEU LEU E . n 
D 4 147 VAL 147 146 146 VAL VAL E . n 
D 4 148 CYS 148 147 147 CYS CYS E . n 
D 4 149 LEU 149 148 148 LEU LEU E . n 
D 4 150 ALA 150 149 149 ALA ALA E . n 
D 4 151 THR 151 150 150 THR THR E . n 
D 4 152 GLY 152 151 151 GLY GLY E . n 
D 4 153 PHE 153 152 152 PHE PHE E . n 
D 4 154 TYR 154 153 153 TYR TYR E . n 
D 4 155 PRO 155 154 154 PRO PRO E . n 
D 4 156 ASP 156 155 155 ASP ASP E . n 
D 4 157 HIS 157 156 156 HIS HIS E . n 
D 4 158 VAL 158 157 157 VAL VAL E . n 
D 4 159 GLU 159 158 158 GLU GLU E . n 
D 4 160 LEU 160 159 159 LEU LEU E . n 
D 4 161 SER 161 160 160 SER SER E . n 
D 4 162 TRP 162 161 161 TRP TRP E . n 
D 4 163 TRP 163 162 162 TRP TRP E . n 
D 4 164 VAL 164 163 163 VAL VAL E . n 
D 4 165 ASN 165 164 164 ASN ASN E . n 
D 4 166 GLY 166 165 165 GLY GLY E . n 
D 4 167 LYS 167 166 166 LYS LYS E . n 
D 4 168 GLU 168 167 167 GLU GLU E . n 
D 4 169 VAL 169 168 168 VAL VAL E . n 
D 4 170 HIS 170 169 169 HIS HIS E . n 
D 4 171 SER 171 170 170 SER SER E . n 
D 4 172 GLY 172 171 171 GLY GLY E . n 
D 4 173 VAL 173 172 172 VAL VAL E . n 
D 4 174 CYS 174 173 173 CYS CYS E . n 
D 4 175 THR 175 174 174 THR THR E . n 
D 4 176 ASP 176 175 175 ASP ASP E . n 
D 4 177 PRO 177 176 176 PRO PRO E . n 
D 4 178 GLN 178 177 177 GLN GLN E . n 
D 4 179 PRO 179 178 178 PRO PRO E . n 
D 4 180 LEU 180 179 179 LEU LEU E . n 
D 4 181 LYS 181 180 180 LYS LYS E . n 
D 4 182 GLU 182 181 181 GLU GLU E . n 
D 4 183 GLN 183 182 182 GLN GLN E . n 
D 4 184 PRO 184 183 183 PRO PRO E . n 
D 4 185 ALA 185 184 184 ALA ALA E . n 
D 4 186 LEU 186 185 185 LEU LEU E . n 
D 4 187 ASN 187 186 186 ASN ASN E . n 
D 4 188 ASP 188 187 187 ASP ASP E . n 
D 4 189 SER 189 188 188 SER SER E . n 
D 4 190 ARG 190 189 189 ARG ARG E . n 
D 4 191 TYR 191 190 190 TYR TYR E . n 
D 4 192 ALA 192 191 191 ALA ALA E . n 
D 4 193 LEU 193 192 192 LEU LEU E . n 
D 4 194 SER 194 193 193 SER SER E . n 
D 4 195 SER 195 194 194 SER SER E . n 
D 4 196 ARG 196 195 195 ARG ARG E . n 
D 4 197 LEU 197 196 196 LEU LEU E . n 
D 4 198 ARG 198 197 197 ARG ARG E . n 
D 4 199 VAL 199 198 198 VAL VAL E . n 
D 4 200 SER 200 199 199 SER SER E . n 
D 4 201 ALA 201 200 200 ALA ALA E . n 
D 4 202 THR 202 201 201 THR THR E . n 
D 4 203 PHE 203 202 202 PHE PHE E . n 
D 4 204 TRP 204 203 203 TRP TRP E . n 
D 4 205 GLN 205 204 204 GLN GLN E . n 
D 4 206 ASN 206 205 205 ASN ASN E . n 
D 4 207 PRO 207 206 206 PRO PRO E . n 
D 4 208 ARG 208 207 207 ARG ARG E . n 
D 4 209 ASN 209 208 208 ASN ASN E . n 
D 4 210 HIS 210 209 209 HIS HIS E . n 
D 4 211 PHE 211 210 210 PHE PHE E . n 
D 4 212 ARG 212 211 211 ARG ARG E . n 
D 4 213 CYS 213 212 212 CYS CYS E . n 
D 4 214 GLN 214 213 213 GLN GLN E . n 
D 4 215 VAL 215 214 214 VAL VAL E . n 
D 4 216 GLN 216 215 215 GLN GLN E . n 
D 4 217 PHE 217 216 216 PHE PHE E . n 
D 4 218 TYR 218 217 217 TYR TYR E . n 
D 4 219 GLY 219 218 218 GLY GLY E . n 
D 4 220 LEU 220 219 219 LEU LEU E . n 
D 4 221 SER 221 220 220 SER SER E . n 
D 4 222 GLU 222 221 221 GLU GLU E . n 
D 4 223 ASN 223 222 222 ASN ASN E . n 
D 4 224 ASP 224 223 223 ASP ASP E . n 
D 4 225 GLU 225 224 224 GLU GLU E . n 
D 4 226 TRP 226 225 225 TRP TRP E . n 
D 4 227 THR 227 226 226 THR THR E . n 
D 4 228 GLN 228 227 227 GLN GLN E . n 
D 4 229 ASP 229 228 228 ASP ASP E . n 
D 4 230 ARG 230 229 229 ARG ARG E . n 
D 4 231 ALA 231 230 230 ALA ALA E . n 
D 4 232 LYS 232 231 231 LYS LYS E . n 
D 4 233 PRO 233 232 232 PRO PRO E . n 
D 4 234 VAL 234 233 233 VAL VAL E . n 
D 4 235 THR 235 234 234 THR THR E . n 
D 4 236 GLN 236 235 235 GLN GLN E . n 
D 4 237 ILE 237 236 236 ILE ILE E . n 
D 4 238 VAL 238 237 237 VAL VAL E . n 
D 4 239 SER 239 238 238 SER SER E . n 
D 4 240 ALA 240 239 239 ALA ALA E . n 
D 4 241 GLU 241 240 240 GLU GLU E . n 
D 4 242 ALA 242 241 241 ALA ALA E . n 
D 4 243 TRP 243 242 242 TRP TRP E . n 
D 4 244 GLY 244 243 243 GLY GLY E . n 
D 4 245 ARG 245 244 244 ARG ARG E . n 
D 4 246 ALA 246 245 245 ALA ALA E . n 
D 4 247 ASP 247 246 246 ASP ASP E . n 
E 5 1   MET 1   0   ?   ?   ?   D . n 
E 5 2   ALA 2   1   1   ALA ALA D . n 
E 5 3   GLN 3   2   2   GLN GLN D . n 
E 5 4   LYS 4   3   3   LYS LYS D . n 
E 5 5   VAL 5   4   4   VAL VAL D . n 
E 5 6   THR 6   5   5   THR THR D . n 
E 5 7   GLN 7   6   6   GLN GLN D . n 
E 5 8   ALA 8   7   7   ALA ALA D . n 
E 5 9   GLN 9   8   8   GLN GLN D . n 
E 5 10  SER 10  9   9   SER SER D . n 
E 5 11  SER 11  10  10  SER SER D . n 
E 5 12  VAL 12  11  11  VAL VAL D . n 
E 5 13  SER 13  12  12  SER SER D . n 
E 5 14  MET 14  13  13  MET MET D . n 
E 5 15  PRO 15  14  14  PRO PRO D . n 
E 5 16  VAL 16  15  15  VAL VAL D . n 
E 5 17  ARG 17  16  16  ARG ARG D . n 
E 5 18  LYS 18  17  17  LYS LYS D . n 
E 5 19  ALA 19  18  18  ALA ALA D . n 
E 5 20  VAL 20  19  19  VAL VAL D . n 
E 5 21  THR 21  20  20  THR THR D . n 
E 5 22  LEU 22  21  21  LEU LEU D . n 
E 5 23  ASN 23  22  22  ASN ASN D . n 
E 5 24  CYS 24  23  23  CYS CYS D . n 
E 5 25  LEU 25  24  24  LEU LEU D . n 
E 5 26  TYR 26  25  25  TYR TYR D . n 
E 5 27  GLU 27  26  26  GLU GLU D . n 
E 5 28  THR 28  27  27  THR THR D . n 
E 5 29  SER 29  28  28  SER SER D . n 
E 5 30  TRP 30  29  29  TRP TRP D . n 
E 5 31  TRP 31  30  30  TRP TRP D . n 
E 5 32  SER 32  31  31  SER SER D . n 
E 5 33  TYR 33  32  32  TYR TYR D . n 
E 5 34  TYR 34  33  33  TYR TYR D . n 
E 5 35  ILE 35  34  34  ILE ILE D . n 
E 5 36  PHE 36  35  35  PHE PHE D . n 
E 5 37  TRP 37  36  36  TRP TRP D . n 
E 5 38  TYR 38  37  37  TYR TYR D . n 
E 5 39  LYS 39  38  38  LYS LYS D . n 
E 5 40  GLN 40  39  39  GLN GLN D . n 
E 5 41  LEU 41  40  40  LEU LEU D . n 
E 5 42  PRO 42  41  41  PRO PRO D . n 
E 5 43  SER 43  42  42  SER SER D . n 
E 5 44  LYS 44  43  43  LYS LYS D . n 
E 5 45  GLU 45  44  44  GLU GLU D . n 
E 5 46  MET 46  45  45  MET MET D . n 
E 5 47  ILE 47  46  46  ILE ILE D . n 
E 5 48  PHE 48  47  47  PHE PHE D . n 
E 5 49  LEU 49  48  48  LEU LEU D . n 
E 5 50  ILE 50  49  49  ILE ILE D . n 
E 5 51  ARG 51  50  50  ARG ARG D . n 
E 5 52  GLN 52  51  51  GLN GLN D . n 
E 5 53  GLY 53  52  52  GLY GLY D . n 
E 5 54  SER 54  53  53  SER SER D . n 
E 5 55  ASP 55  54  54  ASP ASP D . n 
E 5 56  GLU 56  55  55  GLU GLU D . n 
E 5 57  GLN 57  56  56  GLN GLN D . n 
E 5 58  ASN 58  57  57  ASN ASN D . n 
E 5 59  ALA 59  58  58  ALA ALA D . n 
E 5 60  LYS 60  59  59  LYS LYS D . n 
E 5 61  SER 61  60  60  SER SER D . n 
E 5 62  GLY 62  61  61  GLY GLY D . n 
E 5 63  ARG 63  62  62  ARG ARG D . n 
E 5 64  TYR 64  63  63  TYR TYR D . n 
E 5 65  SER 65  64  64  SER SER D . n 
E 5 66  VAL 66  65  65  VAL VAL D . n 
E 5 67  ASN 67  66  66  ASN ASN D . n 
E 5 68  PHE 68  67  67  PHE PHE D . n 
E 5 69  LYS 69  68  68  LYS LYS D . n 
E 5 70  LYS 70  69  69  LYS LYS D . n 
E 5 71  ALA 71  70  70  ALA ALA D . n 
E 5 72  ALA 72  71  71  ALA ALA D . n 
E 5 73  LYS 73  72  72  LYS LYS D . n 
E 5 74  SER 74  73  73  SER SER D . n 
E 5 75  VAL 75  74  74  VAL VAL D . n 
E 5 76  ALA 76  75  75  ALA ALA D . n 
E 5 77  LEU 77  76  76  LEU LEU D . n 
E 5 78  THR 78  77  77  THR THR D . n 
E 5 79  ILE 79  78  78  ILE ILE D . n 
E 5 80  SER 80  79  79  SER SER D . n 
E 5 81  ALA 81  80  80  ALA ALA D . n 
E 5 82  LEU 82  81  81  LEU LEU D . n 
E 5 83  GLN 83  82  82  GLN GLN D . n 
E 5 84  LEU 84  83  83  LEU LEU D . n 
E 5 85  GLU 85  84  84  GLU GLU D . n 
E 5 86  ASP 86  85  85  ASP ASP D . n 
E 5 87  SER 87  86  86  SER SER D . n 
E 5 88  ALA 88  87  87  ALA ALA D . n 
E 5 89  LYS 89  88  88  LYS LYS D . n 
E 5 90  TYR 90  89  89  TYR TYR D . n 
E 5 91  PHE 91  90  90  PHE PHE D . n 
E 5 92  CYS 92  91  91  CYS CYS D . n 
E 5 93  ALA 93  92  92  ALA ALA D . n 
E 5 94  LEU 94  93  93  LEU LEU D . n 
E 5 95  GLY 95  94  94  GLY GLY D . n 
E 5 96  ASP 96  95  95  ASP ASP D . n 
E 5 97  THR 97  96  96  THR THR D . n 
E 5 98  ALA 98  97  97  ALA ALA D . n 
E 5 99  GLY 99  98  98  GLY GLY D . n 
E 5 100 LYS 100 99  99  LYS LYS D . n 
E 5 101 SER 101 100 100 SER SER D . n 
E 5 102 THR 102 101 101 THR THR D . n 
E 5 103 PHE 103 102 102 PHE PHE D . n 
E 5 104 GLY 104 103 103 GLY GLY D . n 
E 5 105 ASP 105 104 104 ASP ASP D . n 
E 5 106 GLY 106 105 105 GLY GLY D . n 
E 5 107 THR 107 106 106 THR THR D . n 
E 5 108 THR 108 107 107 THR THR D . n 
E 5 109 LEU 109 108 108 LEU LEU D . n 
E 5 110 THR 110 109 109 THR THR D . n 
E 5 111 VAL 111 110 110 VAL VAL D . n 
E 5 112 LYS 112 111 111 LYS LYS D . n 
E 5 113 PRO 113 112 112 PRO PRO D . n 
E 5 114 ASN 114 113 113 ASN ASN D . n 
E 5 115 ILE 115 114 114 ILE ILE D . n 
E 5 116 GLN 116 115 115 GLN GLN D . n 
E 5 117 ASN 117 116 116 ASN ASN D . n 
E 5 118 PRO 118 117 117 PRO PRO D . n 
E 5 119 ASP 119 118 118 ASP ASP D . n 
E 5 120 PRO 120 119 119 PRO PRO D . n 
E 5 121 ALA 121 120 120 ALA ALA D . n 
E 5 122 VAL 122 121 121 VAL VAL D . n 
E 5 123 TYR 123 122 122 TYR TYR D . n 
E 5 124 GLN 124 123 123 GLN GLN D . n 
E 5 125 LEU 125 124 124 LEU LEU D . n 
E 5 126 ARG 126 125 125 ARG ARG D . n 
E 5 127 ASP 127 126 126 ASP ASP D . n 
E 5 128 SER 128 127 127 SER SER D . n 
E 5 129 LYS 129 128 128 LYS LYS D . n 
E 5 130 SER 130 129 129 SER SER D . n 
E 5 131 SER 131 130 130 SER SER D . n 
E 5 132 ASP 132 131 131 ASP ASP D . n 
E 5 133 LYS 133 132 132 LYS LYS D . n 
E 5 134 SER 134 133 133 SER SER D . n 
E 5 135 VAL 135 134 134 VAL VAL D . n 
E 5 136 CYS 136 135 135 CYS CYS D . n 
E 5 137 LEU 137 136 136 LEU LEU D . n 
E 5 138 PHE 138 137 137 PHE PHE D . n 
E 5 139 THR 139 138 138 THR THR D . n 
E 5 140 ASP 140 139 139 ASP ASP D . n 
E 5 141 PHE 141 140 140 PHE PHE D . n 
E 5 142 ASP 142 141 141 ASP ASP D . n 
E 5 143 SER 143 142 142 SER SER D . n 
E 5 144 GLN 144 143 143 GLN GLN D . n 
E 5 145 THR 145 144 144 THR THR D . n 
E 5 146 ASN 146 145 145 ASN ASN D . n 
E 5 147 VAL 147 146 146 VAL VAL D . n 
E 5 148 SER 148 147 147 SER SER D . n 
E 5 149 GLN 149 148 148 GLN GLN D . n 
E 5 150 SER 150 149 149 SER SER D . n 
E 5 151 LYS 151 150 150 LYS LYS D . n 
E 5 152 ASP 152 151 151 ASP ASP D . n 
E 5 153 SER 153 152 152 SER SER D . n 
E 5 154 ASP 154 153 153 ASP ASP D . n 
E 5 155 VAL 155 154 154 VAL VAL D . n 
E 5 156 TYR 156 155 155 TYR TYR D . n 
E 5 157 ILE 157 156 156 ILE ILE D . n 
E 5 158 THR 158 157 157 THR THR D . n 
E 5 159 ASP 159 158 158 ASP ASP D . n 
E 5 160 LYS 160 159 159 LYS LYS D . n 
E 5 161 CYS 161 160 160 CYS CYS D . n 
E 5 162 VAL 162 161 161 VAL VAL D . n 
E 5 163 LEU 163 162 162 LEU LEU D . n 
E 5 164 ASP 164 163 163 ASP ASP D . n 
E 5 165 MET 165 164 164 MET MET D . n 
E 5 166 ARG 166 165 165 ARG ARG D . n 
E 5 167 SER 167 166 166 SER SER D . n 
E 5 168 MET 168 167 167 MET MET D . n 
E 5 169 ASP 169 168 168 ASP ASP D . n 
E 5 170 PHE 170 169 169 PHE PHE D . n 
E 5 171 LYS 171 170 170 LYS LYS D . n 
E 5 172 SER 172 171 171 SER SER D . n 
E 5 173 ASN 173 172 172 ASN ASN D . n 
E 5 174 SER 174 173 173 SER SER D . n 
E 5 175 ALA 175 174 174 ALA ALA D . n 
E 5 176 VAL 176 175 175 VAL VAL D . n 
E 5 177 ALA 177 176 176 ALA ALA D . n 
E 5 178 TRP 178 177 177 TRP TRP D . n 
E 5 179 SER 179 178 178 SER SER D . n 
E 5 180 ASN 180 179 179 ASN ASN D . n 
E 5 181 LYS 181 180 180 LYS LYS D . n 
E 5 182 SER 182 181 181 SER SER D . n 
E 5 183 ASP 183 182 182 ASP ASP D . n 
E 5 184 PHE 184 183 183 PHE PHE D . n 
E 5 185 ALA 185 184 184 ALA ALA D . n 
E 5 186 CYS 186 185 185 CYS CYS D . n 
E 5 187 ALA 187 186 186 ALA ALA D . n 
E 5 188 ASN 188 187 187 ASN ASN D . n 
E 5 189 ALA 189 188 188 ALA ALA D . n 
E 5 190 PHE 190 189 189 PHE PHE D . n 
E 5 191 ASN 191 190 190 ASN ASN D . n 
E 5 192 ASN 192 191 191 ASN ASN D . n 
E 5 193 SER 193 192 192 SER SER D . n 
E 5 194 ILE 194 193 193 ILE ILE D . n 
E 5 195 ILE 195 194 194 ILE ILE D . n 
E 5 196 PRO 196 195 195 PRO PRO D . n 
E 5 197 GLU 197 196 196 GLU GLU D . n 
E 5 198 ASP 198 197 197 ASP ASP D . n 
E 5 199 THR 199 198 198 THR THR D . n 
E 5 200 PHE 200 199 199 PHE PHE D . n 
E 5 201 PHE 201 200 200 PHE PHE D . n 
E 5 202 PRO 202 201 201 PRO PRO D . n 
E 5 203 SER 203 202 202 SER SER D . n 
E 5 204 PRO 204 203 ?   ?   ?   D . n 
E 5 205 GLU 205 204 ?   ?   ?   D . n 
E 5 206 SER 206 205 ?   ?   ?   D . n 
E 5 207 SER 207 206 ?   ?   ?   D . n 
# 
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 
F 6 HOH 1   301 376 HOH HOH A . 
F 6 HOH 2   302 330 HOH HOH A . 
F 6 HOH 3   303 141 HOH HOH A . 
F 6 HOH 4   304 172 HOH HOH A . 
F 6 HOH 5   305 409 HOH HOH A . 
F 6 HOH 6   306 31  HOH HOH A . 
F 6 HOH 7   307 257 HOH HOH A . 
F 6 HOH 8   308 320 HOH HOH A . 
F 6 HOH 9   309 245 HOH HOH A . 
F 6 HOH 10  310 300 HOH HOH A . 
F 6 HOH 11  311 44  HOH HOH A . 
F 6 HOH 12  312 285 HOH HOH A . 
F 6 HOH 13  313 293 HOH HOH A . 
F 6 HOH 14  314 252 HOH HOH A . 
F 6 HOH 15  315 149 HOH HOH A . 
F 6 HOH 16  316 107 HOH HOH A . 
F 6 HOH 17  317 340 HOH HOH A . 
F 6 HOH 18  318 117 HOH HOH A . 
F 6 HOH 19  319 168 HOH HOH A . 
F 6 HOH 20  320 4   HOH HOH A . 
F 6 HOH 21  321 27  HOH HOH A . 
F 6 HOH 22  322 66  HOH HOH A . 
F 6 HOH 23  323 61  HOH HOH A . 
F 6 HOH 24  324 198 HOH HOH A . 
F 6 HOH 25  325 102 HOH HOH A . 
F 6 HOH 26  326 11  HOH HOH A . 
F 6 HOH 27  327 123 HOH HOH A . 
F 6 HOH 28  328 98  HOH HOH A . 
F 6 HOH 29  329 215 HOH HOH A . 
F 6 HOH 30  330 195 HOH HOH A . 
F 6 HOH 31  331 354 HOH HOH A . 
F 6 HOH 32  332 30  HOH HOH A . 
F 6 HOH 33  333 422 HOH HOH A . 
F 6 HOH 34  334 25  HOH HOH A . 
F 6 HOH 35  335 15  HOH HOH A . 
F 6 HOH 36  336 38  HOH HOH A . 
F 6 HOH 37  337 206 HOH HOH A . 
F 6 HOH 38  338 96  HOH HOH A . 
F 6 HOH 39  339 12  HOH HOH A . 
F 6 HOH 40  340 254 HOH HOH A . 
F 6 HOH 41  341 73  HOH HOH A . 
F 6 HOH 42  342 297 HOH HOH A . 
F 6 HOH 43  343 33  HOH HOH A . 
F 6 HOH 44  344 238 HOH HOH A . 
F 6 HOH 45  345 321 HOH HOH A . 
F 6 HOH 46  346 301 HOH HOH A . 
F 6 HOH 47  347 204 HOH HOH A . 
F 6 HOH 48  348 113 HOH HOH A . 
F 6 HOH 49  349 54  HOH HOH A . 
F 6 HOH 50  350 14  HOH HOH A . 
F 6 HOH 51  351 16  HOH HOH A . 
F 6 HOH 52  352 316 HOH HOH A . 
F 6 HOH 53  353 92  HOH HOH A . 
F 6 HOH 54  354 235 HOH HOH A . 
F 6 HOH 55  355 131 HOH HOH A . 
F 6 HOH 56  356 276 HOH HOH A . 
F 6 HOH 57  357 155 HOH HOH A . 
F 6 HOH 58  358 418 HOH HOH A . 
F 6 HOH 59  359 267 HOH HOH A . 
F 6 HOH 60  360 90  HOH HOH A . 
F 6 HOH 61  361 292 HOH HOH A . 
F 6 HOH 62  362 163 HOH HOH A . 
F 6 HOH 63  363 171 HOH HOH A . 
F 6 HOH 64  364 392 HOH HOH A . 
F 6 HOH 65  365 303 HOH HOH A . 
F 6 HOH 66  366 147 HOH HOH A . 
F 6 HOH 67  367 162 HOH HOH A . 
F 6 HOH 68  368 145 HOH HOH A . 
F 6 HOH 69  369 365 HOH HOH A . 
F 6 HOH 70  370 136 HOH HOH A . 
F 6 HOH 71  371 398 HOH HOH A . 
F 6 HOH 72  372 120 HOH HOH A . 
F 6 HOH 73  373 250 HOH HOH A . 
F 6 HOH 74  374 248 HOH HOH A . 
F 6 HOH 75  375 277 HOH HOH A . 
F 6 HOH 76  376 234 HOH HOH A . 
F 6 HOH 77  377 82  HOH HOH A . 
F 6 HOH 78  378 135 HOH HOH A . 
F 6 HOH 79  379 210 HOH HOH A . 
F 6 HOH 80  380 52  HOH HOH A . 
F 6 HOH 81  381 72  HOH HOH A . 
F 6 HOH 82  382 232 HOH HOH A . 
F 6 HOH 83  383 280 HOH HOH A . 
F 6 HOH 84  384 423 HOH HOH A . 
F 6 HOH 85  385 338 HOH HOH A . 
F 6 HOH 86  386 59  HOH HOH A . 
F 6 HOH 87  387 230 HOH HOH A . 
F 6 HOH 88  388 249 HOH HOH A . 
F 6 HOH 89  389 430 HOH HOH A . 
F 6 HOH 90  390 375 HOH HOH A . 
F 6 HOH 91  391 101 HOH HOH A . 
F 6 HOH 92  392 357 HOH HOH A . 
F 6 HOH 93  393 144 HOH HOH A . 
F 6 HOH 94  394 269 HOH HOH A . 
F 6 HOH 95  395 346 HOH HOH A . 
F 6 HOH 96  396 119 HOH HOH A . 
F 6 HOH 97  397 406 HOH HOH A . 
F 6 HOH 98  398 304 HOH HOH A . 
F 6 HOH 99  399 390 HOH HOH A . 
F 6 HOH 100 400 322 HOH HOH A . 
F 6 HOH 101 401 400 HOH HOH A . 
F 6 HOH 102 402 324 HOH HOH A . 
F 6 HOH 103 403 366 HOH HOH A . 
F 6 HOH 104 404 348 HOH HOH A . 
F 6 HOH 105 405 393 HOH HOH A . 
F 6 HOH 106 406 339 HOH HOH A . 
F 6 HOH 107 407 429 HOH HOH A . 
F 6 HOH 108 408 246 HOH HOH A . 
F 6 HOH 109 409 396 HOH HOH A . 
F 6 HOH 110 410 391 HOH HOH A . 
G 6 HOH 1   101 97  HOH HOH B . 
G 6 HOH 2   102 384 HOH HOH B . 
G 6 HOH 3   103 94  HOH HOH B . 
G 6 HOH 4   104 387 HOH HOH B . 
G 6 HOH 5   105 129 HOH HOH B . 
G 6 HOH 6   106 353 HOH HOH B . 
G 6 HOH 7   107 333 HOH HOH B . 
G 6 HOH 8   108 29  HOH HOH B . 
G 6 HOH 9   109 228 HOH HOH B . 
G 6 HOH 10  110 407 HOH HOH B . 
G 6 HOH 11  111 176 HOH HOH B . 
G 6 HOH 12  112 64  HOH HOH B . 
G 6 HOH 13  113 130 HOH HOH B . 
G 6 HOH 14  114 50  HOH HOH B . 
G 6 HOH 15  115 229 HOH HOH B . 
G 6 HOH 16  116 35  HOH HOH B . 
G 6 HOH 17  117 256 HOH HOH B . 
G 6 HOH 18  118 290 HOH HOH B . 
G 6 HOH 19  119 140 HOH HOH B . 
G 6 HOH 20  120 344 HOH HOH B . 
G 6 HOH 21  121 296 HOH HOH B . 
G 6 HOH 22  122 13  HOH HOH B . 
G 6 HOH 23  123 146 HOH HOH B . 
G 6 HOH 24  124 191 HOH HOH B . 
G 6 HOH 25  125 192 HOH HOH B . 
G 6 HOH 26  126 240 HOH HOH B . 
G 6 HOH 27  127 328 HOH HOH B . 
G 6 HOH 28  128 314 HOH HOH B . 
G 6 HOH 29  129 174 HOH HOH B . 
G 6 HOH 30  130 424 HOH HOH B . 
G 6 HOH 31  131 199 HOH HOH B . 
G 6 HOH 32  132 212 HOH HOH B . 
G 6 HOH 33  133 81  HOH HOH B . 
G 6 HOH 34  134 378 HOH HOH B . 
G 6 HOH 35  135 288 HOH HOH B . 
G 6 HOH 36  136 190 HOH HOH B . 
G 6 HOH 37  137 253 HOH HOH B . 
G 6 HOH 38  138 428 HOH HOH B . 
G 6 HOH 39  139 382 HOH HOH B . 
G 6 HOH 40  140 201 HOH HOH B . 
G 6 HOH 41  141 374 HOH HOH B . 
G 6 HOH 42  142 143 HOH HOH B . 
G 6 HOH 43  143 188 HOH HOH B . 
G 6 HOH 44  144 412 HOH HOH B . 
G 6 HOH 45  145 404 HOH HOH B . 
G 6 HOH 46  146 166 HOH HOH B . 
G 6 HOH 47  147 318 HOH HOH B . 
G 6 HOH 48  148 319 HOH HOH B . 
H 6 HOH 1   101 345 HOH HOH C . 
H 6 HOH 2   102 110 HOH HOH C . 
H 6 HOH 3   103 126 HOH HOH C . 
H 6 HOH 4   104 278 HOH HOH C . 
H 6 HOH 5   105 84  HOH HOH C . 
H 6 HOH 6   106 336 HOH HOH C . 
H 6 HOH 7   107 128 HOH HOH C . 
H 6 HOH 8   108 203 HOH HOH C . 
H 6 HOH 9   109 265 HOH HOH C . 
I 6 HOH 1   301 175 HOH HOH E . 
I 6 HOH 2   302 161 HOH HOH E . 
I 6 HOH 3   303 150 HOH HOH E . 
I 6 HOH 4   304 227 HOH HOH E . 
I 6 HOH 5   305 17  HOH HOH E . 
I 6 HOH 6   306 137 HOH HOH E . 
I 6 HOH 7   307 34  HOH HOH E . 
I 6 HOH 8   308 349 HOH HOH E . 
I 6 HOH 9   309 77  HOH HOH E . 
I 6 HOH 10  310 37  HOH HOH E . 
I 6 HOH 11  311 95  HOH HOH E . 
I 6 HOH 12  312 216 HOH HOH E . 
I 6 HOH 13  313 89  HOH HOH E . 
I 6 HOH 14  314 259 HOH HOH E . 
I 6 HOH 15  315 62  HOH HOH E . 
I 6 HOH 16  316 109 HOH HOH E . 
I 6 HOH 17  317 388 HOH HOH E . 
I 6 HOH 18  318 261 HOH HOH E . 
I 6 HOH 19  319 76  HOH HOH E . 
I 6 HOH 20  320 68  HOH HOH E . 
I 6 HOH 21  321 121 HOH HOH E . 
I 6 HOH 22  322 373 HOH HOH E . 
I 6 HOH 23  323 289 HOH HOH E . 
I 6 HOH 24  324 305 HOH HOH E . 
I 6 HOH 25  325 5   HOH HOH E . 
I 6 HOH 26  326 182 HOH HOH E . 
I 6 HOH 27  327 138 HOH HOH E . 
I 6 HOH 28  328 208 HOH HOH E . 
I 6 HOH 29  329 213 HOH HOH E . 
I 6 HOH 30  330 326 HOH HOH E . 
I 6 HOH 31  331 122 HOH HOH E . 
I 6 HOH 32  332 397 HOH HOH E . 
I 6 HOH 33  333 7   HOH HOH E . 
I 6 HOH 34  334 42  HOH HOH E . 
I 6 HOH 35  335 46  HOH HOH E . 
I 6 HOH 36  336 185 HOH HOH E . 
I 6 HOH 37  337 362 HOH HOH E . 
I 6 HOH 38  338 421 HOH HOH E . 
I 6 HOH 39  339 43  HOH HOH E . 
I 6 HOH 40  340 74  HOH HOH E . 
I 6 HOH 41  341 273 HOH HOH E . 
I 6 HOH 42  342 159 HOH HOH E . 
I 6 HOH 43  343 420 HOH HOH E . 
I 6 HOH 44  344 23  HOH HOH E . 
I 6 HOH 45  345 114 HOH HOH E . 
I 6 HOH 46  346 270 HOH HOH E . 
I 6 HOH 47  347 83  HOH HOH E . 
I 6 HOH 48  348 271 HOH HOH E . 
I 6 HOH 49  349 200 HOH HOH E . 
I 6 HOH 50  350 224 HOH HOH E . 
I 6 HOH 51  351 108 HOH HOH E . 
I 6 HOH 52  352 395 HOH HOH E . 
I 6 HOH 53  353 80  HOH HOH E . 
I 6 HOH 54  354 40  HOH HOH E . 
I 6 HOH 55  355 148 HOH HOH E . 
I 6 HOH 56  356 385 HOH HOH E . 
I 6 HOH 57  357 197 HOH HOH E . 
I 6 HOH 58  358 85  HOH HOH E . 
I 6 HOH 59  359 69  HOH HOH E . 
I 6 HOH 60  360 167 HOH HOH E . 
I 6 HOH 61  361 142 HOH HOH E . 
I 6 HOH 62  362 19  HOH HOH E . 
I 6 HOH 63  363 3   HOH HOH E . 
I 6 HOH 64  364 127 HOH HOH E . 
I 6 HOH 65  365 10  HOH HOH E . 
I 6 HOH 66  366 284 HOH HOH E . 
I 6 HOH 67  367 88  HOH HOH E . 
I 6 HOH 68  368 99  HOH HOH E . 
I 6 HOH 69  369 116 HOH HOH E . 
I 6 HOH 70  370 2   HOH HOH E . 
I 6 HOH 71  371 223 HOH HOH E . 
I 6 HOH 72  372 205 HOH HOH E . 
I 6 HOH 73  373 222 HOH HOH E . 
I 6 HOH 74  374 60  HOH HOH E . 
I 6 HOH 75  375 218 HOH HOH E . 
I 6 HOH 76  376 370 HOH HOH E . 
I 6 HOH 77  377 247 HOH HOH E . 
I 6 HOH 78  378 93  HOH HOH E . 
I 6 HOH 79  379 151 HOH HOH E . 
I 6 HOH 80  380 411 HOH HOH E . 
I 6 HOH 81  381 325 HOH HOH E . 
I 6 HOH 82  382 53  HOH HOH E . 
I 6 HOH 83  383 323 HOH HOH E . 
I 6 HOH 84  384 295 HOH HOH E . 
I 6 HOH 85  385 87  HOH HOH E . 
I 6 HOH 86  386 196 HOH HOH E . 
I 6 HOH 87  387 309 HOH HOH E . 
I 6 HOH 88  388 233 HOH HOH E . 
I 6 HOH 89  389 63  HOH HOH E . 
I 6 HOH 90  390 298 HOH HOH E . 
I 6 HOH 91  391 286 HOH HOH E . 
I 6 HOH 92  392 152 HOH HOH E . 
I 6 HOH 93  393 266 HOH HOH E . 
I 6 HOH 94  394 255 HOH HOH E . 
I 6 HOH 95  395 24  HOH HOH E . 
I 6 HOH 96  396 8   HOH HOH E . 
I 6 HOH 97  397 65  HOH HOH E . 
I 6 HOH 98  398 260 HOH HOH E . 
I 6 HOH 99  399 403 HOH HOH E . 
I 6 HOH 100 400 369 HOH HOH E . 
I 6 HOH 101 401 20  HOH HOH E . 
I 6 HOH 102 402 194 HOH HOH E . 
I 6 HOH 103 403 307 HOH HOH E . 
I 6 HOH 104 404 118 HOH HOH E . 
I 6 HOH 105 405 209 HOH HOH E . 
I 6 HOH 106 406 156 HOH HOH E . 
I 6 HOH 107 407 361 HOH HOH E . 
I 6 HOH 108 408 425 HOH HOH E . 
I 6 HOH 109 409 359 HOH HOH E . 
I 6 HOH 110 410 181 HOH HOH E . 
I 6 HOH 111 411 47  HOH HOH E . 
I 6 HOH 112 412 139 HOH HOH E . 
I 6 HOH 113 413 173 HOH HOH E . 
I 6 HOH 114 414 177 HOH HOH E . 
I 6 HOH 115 415 251 HOH HOH E . 
I 6 HOH 116 416 220 HOH HOH E . 
I 6 HOH 117 417 48  HOH HOH E . 
I 6 HOH 118 418 317 HOH HOH E . 
I 6 HOH 119 419 160 HOH HOH E . 
I 6 HOH 120 420 243 HOH HOH E . 
I 6 HOH 121 421 291 HOH HOH E . 
I 6 HOH 122 422 115 HOH HOH E . 
I 6 HOH 123 423 268 HOH HOH E . 
I 6 HOH 124 424 381 HOH HOH E . 
I 6 HOH 125 425 410 HOH HOH E . 
I 6 HOH 126 426 394 HOH HOH E . 
I 6 HOH 127 427 299 HOH HOH E . 
I 6 HOH 128 428 91  HOH HOH E . 
I 6 HOH 129 429 32  HOH HOH E . 
I 6 HOH 130 430 39  HOH HOH E . 
I 6 HOH 131 431 380 HOH HOH E . 
I 6 HOH 132 432 274 HOH HOH E . 
I 6 HOH 133 433 311 HOH HOH E . 
I 6 HOH 134 434 170 HOH HOH E . 
I 6 HOH 135 435 310 HOH HOH E . 
I 6 HOH 136 436 242 HOH HOH E . 
I 6 HOH 137 437 55  HOH HOH E . 
I 6 HOH 138 438 45  HOH HOH E . 
I 6 HOH 139 439 165 HOH HOH E . 
I 6 HOH 140 440 383 HOH HOH E . 
I 6 HOH 141 441 283 HOH HOH E . 
I 6 HOH 142 442 327 HOH HOH E . 
I 6 HOH 143 443 352 HOH HOH E . 
I 6 HOH 144 444 225 HOH HOH E . 
I 6 HOH 145 445 331 HOH HOH E . 
I 6 HOH 146 446 312 HOH HOH E . 
I 6 HOH 147 447 287 HOH HOH E . 
I 6 HOH 148 448 347 HOH HOH E . 
I 6 HOH 149 449 105 HOH HOH E . 
I 6 HOH 150 450 419 HOH HOH E . 
I 6 HOH 151 451 426 HOH HOH E . 
I 6 HOH 152 452 402 HOH HOH E . 
I 6 HOH 153 453 125 HOH HOH E . 
I 6 HOH 154 454 415 HOH HOH E . 
I 6 HOH 155 455 405 HOH HOH E . 
I 6 HOH 156 456 364 HOH HOH E . 
I 6 HOH 157 457 389 HOH HOH E . 
I 6 HOH 158 458 211 HOH HOH E . 
I 6 HOH 159 459 416 HOH HOH E . 
I 6 HOH 160 460 263 HOH HOH E . 
I 6 HOH 161 461 106 HOH HOH E . 
I 6 HOH 162 462 187 HOH HOH E . 
I 6 HOH 163 463 157 HOH HOH E . 
J 6 HOH 1   301 413 HOH HOH D . 
J 6 HOH 2   302 356 HOH HOH D . 
J 6 HOH 3   303 28  HOH HOH D . 
J 6 HOH 4   304 335 HOH HOH D . 
J 6 HOH 5   305 56  HOH HOH D . 
J 6 HOH 6   306 219 HOH HOH D . 
J 6 HOH 7   307 334 HOH HOH D . 
J 6 HOH 8   308 132 HOH HOH D . 
J 6 HOH 9   309 377 HOH HOH D . 
J 6 HOH 10  310 21  HOH HOH D . 
J 6 HOH 11  311 1   HOH HOH D . 
J 6 HOH 12  312 79  HOH HOH D . 
J 6 HOH 13  313 363 HOH HOH D . 
J 6 HOH 14  314 103 HOH HOH D . 
J 6 HOH 15  315 315 HOH HOH D . 
J 6 HOH 16  316 70  HOH HOH D . 
J 6 HOH 17  317 154 HOH HOH D . 
J 6 HOH 18  318 49  HOH HOH D . 
J 6 HOH 19  319 164 HOH HOH D . 
J 6 HOH 20  320 282 HOH HOH D . 
J 6 HOH 21  321 264 HOH HOH D . 
J 6 HOH 22  322 18  HOH HOH D . 
J 6 HOH 23  323 86  HOH HOH D . 
J 6 HOH 24  324 329 HOH HOH D . 
J 6 HOH 25  325 217 HOH HOH D . 
J 6 HOH 26  326 57  HOH HOH D . 
J 6 HOH 27  327 371 HOH HOH D . 
J 6 HOH 28  328 360 HOH HOH D . 
J 6 HOH 29  329 9   HOH HOH D . 
J 6 HOH 30  330 6   HOH HOH D . 
J 6 HOH 31  331 26  HOH HOH D . 
J 6 HOH 32  332 51  HOH HOH D . 
J 6 HOH 33  333 58  HOH HOH D . 
J 6 HOH 34  334 36  HOH HOH D . 
J 6 HOH 35  335 67  HOH HOH D . 
J 6 HOH 36  336 275 HOH HOH D . 
J 6 HOH 37  337 100 HOH HOH D . 
J 6 HOH 38  338 112 HOH HOH D . 
J 6 HOH 39  339 180 HOH HOH D . 
J 6 HOH 40  340 236 HOH HOH D . 
J 6 HOH 41  341 332 HOH HOH D . 
J 6 HOH 42  342 71  HOH HOH D . 
J 6 HOH 43  343 193 HOH HOH D . 
J 6 HOH 44  344 306 HOH HOH D . 
J 6 HOH 45  345 262 HOH HOH D . 
J 6 HOH 46  346 237 HOH HOH D . 
J 6 HOH 47  347 183 HOH HOH D . 
J 6 HOH 48  348 186 HOH HOH D . 
J 6 HOH 49  349 337 HOH HOH D . 
J 6 HOH 50  350 231 HOH HOH D . 
J 6 HOH 51  351 158 HOH HOH D . 
J 6 HOH 52  352 414 HOH HOH D . 
J 6 HOH 53  353 189 HOH HOH D . 
J 6 HOH 54  354 184 HOH HOH D . 
J 6 HOH 55  355 41  HOH HOH D . 
J 6 HOH 56  356 308 HOH HOH D . 
J 6 HOH 57  357 399 HOH HOH D . 
J 6 HOH 58  358 258 HOH HOH D . 
J 6 HOH 59  359 342 HOH HOH D . 
J 6 HOH 60  360 294 HOH HOH D . 
J 6 HOH 61  361 239 HOH HOH D . 
J 6 HOH 62  362 169 HOH HOH D . 
J 6 HOH 63  363 355 HOH HOH D . 
J 6 HOH 64  364 124 HOH HOH D . 
J 6 HOH 65  365 134 HOH HOH D . 
J 6 HOH 66  366 368 HOH HOH D . 
J 6 HOH 67  367 244 HOH HOH D . 
J 6 HOH 68  368 133 HOH HOH D . 
J 6 HOH 69  369 207 HOH HOH D . 
J 6 HOH 70  370 241 HOH HOH D . 
J 6 HOH 71  371 221 HOH HOH D . 
J 6 HOH 72  372 350 HOH HOH D . 
J 6 HOH 73  373 431 HOH HOH D . 
J 6 HOH 74  374 179 HOH HOH D . 
J 6 HOH 75  375 178 HOH HOH D . 
J 6 HOH 76  376 153 HOH HOH D . 
J 6 HOH 77  377 272 HOH HOH D . 
J 6 HOH 78  378 358 HOH HOH D . 
J 6 HOH 79  379 408 HOH HOH D . 
J 6 HOH 80  380 214 HOH HOH D . 
J 6 HOH 81  381 226 HOH HOH D . 
J 6 HOH 82  382 111 HOH HOH D . 
J 6 HOH 83  383 313 HOH HOH D . 
J 6 HOH 84  384 427 HOH HOH D . 
J 6 HOH 85  385 379 HOH HOH D . 
J 6 HOH 86  386 281 HOH HOH D . 
J 6 HOH 87  387 401 HOH HOH D . 
J 6 HOH 88  388 386 HOH HOH D . 
J 6 HOH 89  389 202 HOH HOH D . 
J 6 HOH 90  390 351 HOH HOH D . 
J 6 HOH 91  391 279 HOH HOH D . 
J 6 HOH 92  392 343 HOH HOH D . 
J 6 HOH 93  393 417 HOH HOH D . 
J 6 HOH 94  394 367 HOH HOH D . 
J 6 HOH 95  395 372 HOH HOH D . 
J 6 HOH 96  396 302 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 17  ? CG  ? A ARG 18  CG  
2  1 Y 1 A ARG 17  ? CD  ? A ARG 18  CD  
3  1 Y 1 A ARG 17  ? NE  ? A ARG 18  NE  
4  1 Y 1 A ARG 17  ? CZ  ? A ARG 18  CZ  
5  1 Y 1 A ARG 17  ? NH1 ? A ARG 18  NH1 
6  1 Y 1 A ARG 17  ? NH2 ? A ARG 18  NH2 
7  1 Y 1 A ASP 227 ? CG  ? A ASP 228 CG  
8  1 Y 1 A ASP 227 ? OD1 ? A ASP 228 OD1 
9  1 Y 1 A ASP 227 ? OD2 ? A ASP 228 OD2 
10 1 Y 1 B LYS 19  ? CG  ? B LYS 20  CG  
11 1 Y 1 B LYS 19  ? CD  ? B LYS 20  CD  
12 1 Y 1 B LYS 19  ? CE  ? B LYS 20  CE  
13 1 Y 1 B LYS 19  ? NZ  ? B LYS 20  NZ  
14 1 Y 1 B LYS 48  ? CG  ? B LYS 49  CG  
15 1 Y 1 B LYS 48  ? CD  ? B LYS 49  CD  
16 1 Y 1 B LYS 48  ? CE  ? B LYS 49  CE  
17 1 Y 1 B LYS 48  ? NZ  ? B LYS 49  NZ  
18 1 Y 1 B LYS 75  ? CG  ? B LYS 76  CG  
19 1 Y 1 B LYS 75  ? CD  ? B LYS 76  CD  
20 1 Y 1 B LYS 75  ? CE  ? B LYS 76  CE  
21 1 Y 1 B LYS 75  ? NZ  ? B LYS 76  NZ  
22 1 Y 1 D LYS 150 ? CG  ? E LYS 151 CG  
23 1 Y 1 D LYS 150 ? CD  ? E LYS 151 CD  
24 1 Y 1 D LYS 150 ? CE  ? E LYS 151 CE  
25 1 Y 1 D LYS 150 ? NZ  ? E LYS 151 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.16_3549: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YJ2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.524 
_cell.length_a_esd                 ? 
_cell.length_b                     134.158 
_cell.length_b_esd                 ? 
_cell.length_c                     222.128 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8YJ2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YJ2 
_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             2.77 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.59 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10mg/ml, 0.2 M NH4 citrate tribasic, 16% PEG3350, pH 7.4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9793 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9793 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YJ2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.26 
_reflns.d_resolution_low                               42.8 
_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                                     464104 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.985 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.26 
_reflns_shell.d_res_low                                     2.34 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             ? 
_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                                  0.883 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YJ2 
_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                            2.261 
_refine.ls_d_res_low                             42.776 
_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                     49611 
_refine.ls_number_reflns_R_free                  2476 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.50 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1909 
_refine.ls_R_factor_R_free                       0.2286 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1890 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.93 
_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                            0.25 
_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.pdbx_number_atoms_protein        6680 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             426 
_refine_hist.number_atoms_total               7106 
_refine_hist.d_res_high                       2.261 
_refine_hist.d_res_low                        42.776 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 6860 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.929 ? 9316 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.671 ? 4099 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054 ? 983  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1223 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.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' 2.2613 2.3048 . . 128 2333 88.00  . . . . 0.2274 . . . . . . . . . . . 0.2601 
'X-RAY DIFFRACTION' 2.3048 2.3518 . . 125 2472 96.00  . . . . 0.2280 . . . . . . . . . . . 0.2883 
'X-RAY DIFFRACTION' 2.3518 2.4029 . . 145 2624 99.00  . . . . 0.2195 . . . . . . . . . . . 0.2547 
'X-RAY DIFFRACTION' 2.4029 2.4588 . . 159 2596 100.00 . . . . 0.2201 . . . . . . . . . . . 0.2918 
'X-RAY DIFFRACTION' 2.4588 2.5203 . . 149 2597 100.00 . . . . 0.2131 . . . . . . . . . . . 0.2671 
'X-RAY DIFFRACTION' 2.5203 2.5885 . . 170 2613 100.00 . . . . 0.2152 . . . . . . . . . . . 0.2660 
'X-RAY DIFFRACTION' 2.5885 2.6646 . . 124 2611 100.00 . . . . 0.2136 . . . . . . . . . . . 0.2548 
'X-RAY DIFFRACTION' 2.6646 2.7506 . . 153 2623 99.00  . . . . 0.2069 . . . . . . . . . . . 0.2483 
'X-RAY DIFFRACTION' 2.7506 2.8489 . . 112 2639 100.00 . . . . 0.2141 . . . . . . . . . . . 0.2834 
'X-RAY DIFFRACTION' 2.8489 2.9629 . . 112 2669 100.00 . . . . 0.2135 . . . . . . . . . . . 0.2542 
'X-RAY DIFFRACTION' 2.9629 3.0977 . . 125 2614 98.00  . . . . 0.2112 . . . . . . . . . . . 0.2439 
'X-RAY DIFFRACTION' 3.0977 3.2610 . . 121 2671 100.00 . . . . 0.2037 . . . . . . . . . . . 0.2565 
'X-RAY DIFFRACTION' 3.2610 3.4652 . . 119 2665 100.00 . . . . 0.1875 . . . . . . . . . . . 0.2332 
'X-RAY DIFFRACTION' 3.4652 3.7326 . . 156 2640 100.00 . . . . 0.1872 . . . . . . . . . . . 0.2306 
'X-RAY DIFFRACTION' 3.7326 4.1080 . . 127 2657 99.00  . . . . 0.1735 . . . . . . . . . . . 0.2193 
'X-RAY DIFFRACTION' 4.1080 4.7018 . . 150 2652 98.00  . . . . 0.1462 . . . . . . . . . . . 0.1775 
'X-RAY DIFFRACTION' 4.7018 5.9213 . . 170 2689 100.00 . . . . 0.1535 . . . . . . . . . . . 0.1903 
'X-RAY DIFFRACTION' 5.9213 42.776 . . 131 2770 97.00  . . . . 0.1846 . . . . . . . . . . . 0.2016 
# 
_struct.entry_id                     8YJ2 
_struct.title                        'N17.1.2 recognition of NRAS neoantigens' 
_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        8YJ2 
_struct_keywords.text            'T cell receptor, p-MHC, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 5 ? 
F N N 6 ? 
G N N 6 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
# 
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 F6IQR9_HUMAN F6IQR9 ? 1 
;GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGT
LRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYL
EGRCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWE
;
25 
2 UNP B2MG_HUMAN   P61769 ? 2 
;IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDRDM
;
21 
3 PDB 8YJ2         8YJ2   ? 3 ? 1  
4 PDB 8YJ2         8YJ2   ? 4 ? 1  
5 PDB 8YJ2         8YJ2   ? 5 ? 1  
# 
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 8YJ2 A 2 ? 276 ? F6IQR9 25 ? 299 ? 1 275 
2 2 8YJ2 B 2 ? 100 ? P61769 21 ? 119 ? 1 99  
3 3 8YJ2 C 1 ? 10  ? 8YJ2   1  ? 10  ? 1 10  
4 4 8YJ2 E 1 ? 247 ? 8YJ2   0  ? 246 ? 0 246 
5 5 8YJ2 D 1 ? 207 ? 8YJ2   0  ? 206 ? 0 206 
# 
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 8YJ2 MET A 1 ? UNP F6IQR9 ? ? 'initiating methionine' 0 1 
2 8YJ2 MET B 1 ? UNP P61769 ? ? 'expression tag'        0 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
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)' 11510 ? 
1 MORE         -36   ? 
1 'SSA (A^2)'  37860 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_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 ALA A 50  ? GLU A 54  ? ALA A 49  GLU A 53  5 ? 5  
HELX_P HELX_P2  AA2 GLY A 57  ? TYR A 86  ? GLY A 56  TYR A 85  1 ? 30 
HELX_P HELX_P3  AA3 ASP A 138 ? VAL A 151 ? ASP A 137 VAL A 150 1 ? 14 
HELX_P HELX_P4  AA4 HIS A 152 ? GLY A 163 ? HIS A 151 GLY A 162 1 ? 12 
HELX_P HELX_P5  AA5 GLY A 163 ? GLY A 176 ? GLY A 162 GLY A 175 1 ? 14 
HELX_P HELX_P6  AA6 GLY A 176 ? GLN A 181 ? GLY A 175 GLN A 180 1 ? 6  
HELX_P HELX_P7  AA7 GLU A 254 ? GLN A 256 ? GLU A 253 GLN A 255 5 ? 3  
HELX_P HELX_P8  AA8 SER D 83  ? THR D 87  ? SER E 82  THR E 86  5 ? 5  
HELX_P HELX_P9  AA9 SER D 134 ? GLN D 142 ? SER E 133 GLN E 141 1 ? 9  
HELX_P HELX_P10 AB1 ALA D 201 ? GLN D 205 ? ALA E 200 GLN E 204 1 ? 5  
HELX_P HELX_P11 AB2 GLN E 83  ? SER E 87  ? GLN D 82  SER D 86  5 ? 5  
HELX_P HELX_P12 AB3 ARG E 166 ? ASP E 169 ? ARG D 165 ASP D 168 5 ? 4  
HELX_P HELX_P13 AB4 ALA E 185 ? PHE E 190 ? ALA D 184 PHE D 189 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 102 SG ? ? ? 1_555 A CYS 165 SG ? ? A CYS 101 A CYS 164 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
disulf2 disulf ? ? A CYS 204 SG ? ? ? 1_555 A CYS 260 SG ? ? A CYS 203 A CYS 259 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf3 disulf ? ? B CYS 26  SG ? ? ? 1_555 B CYS 81  SG ? ? B CYS 25  B CYS 80  1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf4 disulf ? ? D CYS 24  SG ? ? ? 1_555 D CYS 92  SG ? ? E CYS 23  E CYS 91  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf5 disulf ? ? D CYS 148 SG ? ? ? 1_555 D CYS 213 SG ? ? E CYS 147 E CYS 212 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
disulf6 disulf ? ? D CYS 174 SG ? ? ? 1_555 E CYS 161 SG ? ? E CYS 173 D CYS 160 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf7 disulf ? ? E CYS 24  SG ? ? ? 1_555 E CYS 92  SG ? ? D CYS 23  D CYS 91  1_555 ? ? ? ? ? ? ? 2.053 ? ? 
disulf8 disulf ? ? E CYS 136 SG ? ? ? 1_555 E CYS 186 SG ? ? D CYS 135 D CYS 185 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 102 ? CYS A 165 ? CYS A 101 ? 1_555 CYS A 164 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 204 ? CYS A 260 ? CYS A 203 ? 1_555 CYS A 259 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 26  ? CYS B 81  ? CYS B 25  ? 1_555 CYS B 80  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 24  ? CYS D 92  ? CYS E 23  ? 1_555 CYS E 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS D 148 ? CYS D 213 ? CYS E 147 ? 1_555 CYS E 212 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6 CYS D 174 ? CYS E 161 ? CYS E 173 ? 1_555 CYS D 160 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7 CYS E 24  ? CYS E 92  ? CYS D 23  ? 1_555 CYS D 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
8 CYS E 136 ? CYS E 186 ? CYS D 135 ? 1_555 CYS D 185 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 210 A . ? TYR 209 A PRO 211 A ? PRO 210 A 1 1.63  
2 HIS 32  B . ? HIS 31  B PRO 33  B ? PRO 32  B 1 3.66  
3 ASN 8   D . ? ASN 7   E PRO 9   D ? PRO 8   E 1 4.83  
4 TYR 154 D . ? TYR 153 E PRO 155 D ? PRO 154 E 1 -3.19 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 6 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 2 ? 
AB6 ? 5 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 4 ? 
AC1 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 47  ? PRO A 48  ? GLU A 46  PRO A 47  
AA1 2 THR A 32  ? ASP A 38  ? THR A 31  ASP A 37  
AA1 3 ARG A 22  ? VAL A 29  ? ARG A 21  VAL A 28  
AA1 4 HIS A 4   ? VAL A 13  ? HIS A 3   VAL A 12  
AA1 5 THR A 95  ? VAL A 104 ? THR A 94  VAL A 103 
AA1 6 PHE A 110 ? TYR A 119 ? PHE A 109 TYR A 118 
AA1 7 LYS A 122 ? LEU A 127 ? LYS A 121 LEU A 126 
AA1 8 TRP A 134 ? ALA A 136 ? TRP A 133 ALA A 135 
AA2 1 LYS A 187 ? PRO A 194 ? LYS A 186 PRO A 193 
AA2 2 GLU A 199 ? PHE A 209 ? GLU A 198 PHE A 208 
AA2 3 PHE A 242 ? PRO A 251 ? PHE A 241 PRO A 250 
AA2 4 THR A 229 ? LEU A 231 ? THR A 228 LEU A 230 
AA3 1 LYS A 187 ? PRO A 194 ? LYS A 186 PRO A 193 
AA3 2 GLU A 199 ? PHE A 209 ? GLU A 198 PHE A 208 
AA3 3 PHE A 242 ? PRO A 251 ? PHE A 241 PRO A 250 
AA3 4 ARG A 235 ? PRO A 236 ? ARG A 234 PRO A 235 
AA4 1 GLU A 223 ? ASP A 224 ? GLU A 222 ASP A 223 
AA4 2 THR A 215 ? ARG A 220 ? THR A 214 ARG A 219 
AA4 3 TYR A 258 ? GLN A 263 ? TYR A 257 GLN A 262 
AA4 4 LEU A 271 ? LEU A 273 ? LEU A 270 LEU A 272 
AA5 1 LYS B 7   ? SER B 12  ? LYS B 6   SER B 11  
AA5 2 ASN B 22  ? PHE B 31  ? ASN B 21  PHE B 30  
AA5 3 PHE B 63  ? PHE B 71  ? PHE B 62  PHE B 70  
AA5 4 GLU B 51  ? HIS B 52  ? GLU B 50  HIS B 51  
AA6 1 LYS B 7   ? SER B 12  ? LYS B 6   SER B 11  
AA6 2 ASN B 22  ? PHE B 31  ? ASN B 21  PHE B 30  
AA6 3 PHE B 63  ? PHE B 71  ? PHE B 62  PHE B 70  
AA6 4 SER B 56  ? PHE B 57  ? SER B 55  PHE B 56  
AA7 1 GLU B 45  ? ARG B 46  ? GLU B 44  ARG B 45  
AA7 2 GLU B 37  ? LYS B 42  ? GLU B 36  LYS B 41  
AA7 3 TYR B 79  ? ASN B 84  ? TYR B 78  ASN B 83  
AA7 4 LYS B 92  ? LYS B 95  ? LYS B 91  LYS B 94  
AA8 1 VAL D 5   ? ASN D 8   ? VAL E 4   ASN E 7   
AA8 2 LEU D 20  ? GLN D 26  ? LEU E 19  GLN E 25  
AA8 3 LEU D 77  ? LEU D 79  ? LEU E 76  LEU E 78  
AA8 4 LYS D 66  ? VAL D 67  ? LYS E 65  VAL E 66  
AA9 1 TYR D 11  ? VAL D 15  ? TYR E 10  VAL E 14  
AA9 2 THR D 112 ? LEU D 117 ? THR E 111 LEU E 116 
AA9 3 SER D 88  ? SER D 95  ? SER E 87  SER E 94  
AA9 4 TYR D 32  ? GLN D 38  ? TYR E 31  GLN E 37  
AA9 5 LEU D 44  ? ASN D 52  ? LEU E 43  ASN E 51  
AA9 6 VAL D 55  ? LYS D 58  ? VAL E 54  LYS E 57  
AB1 1 TYR D 11  ? VAL D 15  ? TYR E 10  VAL E 14  
AB1 2 THR D 112 ? LEU D 117 ? THR E 111 LEU E 116 
AB1 3 SER D 88  ? SER D 95  ? SER E 87  SER E 94  
AB1 4 TYR D 107 ? PHE D 108 ? TYR E 106 PHE E 107 
AB2 1 GLU D 127 ? PHE D 131 ? GLU E 126 PHE E 130 
AB2 2 LYS D 143 ? PHE D 153 ? LYS E 142 PHE E 152 
AB2 3 TYR D 191 ? SER D 200 ? TYR E 190 SER E 199 
AB2 4 VAL D 173 ? THR D 175 ? VAL E 172 THR E 174 
AB3 1 GLU D 127 ? PHE D 131 ? GLU E 126 PHE E 130 
AB3 2 LYS D 143 ? PHE D 153 ? LYS E 142 PHE E 152 
AB3 3 TYR D 191 ? SER D 200 ? TYR E 190 SER E 199 
AB3 4 LEU D 180 ? LYS D 181 ? LEU E 179 LYS E 180 
AB4 1 LYS D 167 ? VAL D 169 ? LYS E 166 VAL E 168 
AB4 2 VAL D 158 ? VAL D 164 ? VAL E 157 VAL E 163 
AB4 3 HIS D 210 ? PHE D 217 ? HIS E 209 PHE E 216 
AB4 4 GLN D 236 ? TRP D 243 ? GLN E 235 TRP E 242 
AB5 1 LYS E 4   ? THR E 6   ? LYS D 3   THR D 5   
AB5 2 LEU E 25  ? GLU E 27  ? LEU D 24  GLU D 26  
AB6 1 SER E 11  ? PRO E 15  ? SER D 10  PRO D 14  
AB6 2 THR E 107 ? LYS E 112 ? THR D 106 LYS D 111 
AB6 3 ALA E 88  ? GLY E 95  ? ALA D 87  GLY D 94  
AB6 4 TYR E 34  ? GLN E 40  ? TYR D 33  GLN D 39  
AB6 5 MET E 46  ? GLY E 53  ? MET D 45  GLY D 52  
AB7 1 SER E 11  ? PRO E 15  ? SER D 10  PRO D 14  
AB7 2 THR E 107 ? LYS E 112 ? THR D 106 LYS D 111 
AB7 3 ALA E 88  ? GLY E 95  ? ALA D 87  GLY D 94  
AB7 4 SER E 101 ? PHE E 103 ? SER D 100 PHE D 102 
AB8 1 VAL E 20  ? LEU E 22  ? VAL D 19  LEU D 21  
AB8 2 SER E 74  ? ILE E 79  ? SER D 73  ILE D 78  
AB8 3 TYR E 64  ? LYS E 69  ? TYR D 63  LYS D 68  
AB8 4 LYS E 60  ? SER E 61  ? LYS D 59  SER D 60  
AB9 1 ALA E 121 ? ARG E 126 ? ALA D 120 ARG D 125 
AB9 2 SER E 134 ? THR E 139 ? SER D 133 THR D 138 
AB9 3 PHE E 170 ? SER E 179 ? PHE D 169 SER D 178 
AB9 4 VAL E 155 ? ILE E 157 ? VAL D 154 ILE D 156 
AC1 1 ALA E 121 ? ARG E 126 ? ALA D 120 ARG D 125 
AC1 2 SER E 134 ? THR E 139 ? SER D 133 THR D 138 
AC1 3 PHE E 170 ? SER E 179 ? PHE D 169 SER D 178 
AC1 4 CYS E 161 ? MET E 165 ? CYS D 160 MET D 164 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 47  ? O GLU A 46  N ARG A 36  ? N ARG A 35  
AA1 2 3 O THR A 32  ? O THR A 31  N VAL A 29  ? N VAL A 28  
AA1 3 4 O ILE A 24  ? O ILE A 23  N THR A 11  ? N THR A 10  
AA1 4 5 N PHE A 10  ? N PHE A 9   O ILE A 98  ? O ILE A 97  
AA1 5 6 N GLN A 97  ? N GLN A 96  O ALA A 118 ? O ALA A 117 
AA1 6 7 N ASP A 117 ? N ASP A 116 O ILE A 125 ? O ILE A 124 
AA1 7 8 N ALA A 126 ? N ALA A 125 O THR A 135 ? O THR A 134 
AA2 1 2 N HIS A 193 ? N HIS A 192 O THR A 201 ? O THR A 200 
AA2 2 3 N CYS A 204 ? N CYS A 203 O ALA A 246 ? O ALA A 245 
AA2 3 4 O ALA A 247 ? O ALA A 246 N GLU A 230 ? N GLU A 229 
AA3 1 2 N HIS A 193 ? N HIS A 192 O THR A 201 ? O THR A 200 
AA3 2 3 N CYS A 204 ? N CYS A 203 O ALA A 246 ? O ALA A 245 
AA3 3 4 O GLN A 243 ? O GLN A 242 N ARG A 235 ? N ARG A 234 
AA4 1 2 O GLU A 223 ? O GLU A 222 N ARG A 220 ? N ARG A 219 
AA4 2 3 N THR A 217 ? N THR A 216 O HIS A 261 ? O HIS A 260 
AA4 3 4 N CYS A 260 ? N CYS A 259 O LEU A 273 ? O LEU A 272 
AA5 1 2 N TYR B 11  ? N TYR B 10  O ASN B 25  ? O ASN B 24  
AA5 2 3 N LEU B 24  ? N LEU B 23  O THR B 69  ? O THR B 68  
AA5 3 4 O TYR B 68  ? O TYR B 67  N GLU B 51  ? N GLU B 50  
AA6 1 2 N TYR B 11  ? N TYR B 10  O ASN B 25  ? O ASN B 24  
AA6 2 3 N LEU B 24  ? N LEU B 23  O THR B 69  ? O THR B 68  
AA6 3 4 O TYR B 64  ? O TYR B 63  N SER B 56  ? N SER B 55  
AA7 1 2 O GLU B 45  ? O GLU B 44  N LYS B 42  ? N LYS B 41  
AA7 2 3 N LEU B 41  ? N LEU B 40  O ALA B 80  ? O ALA B 79  
AA7 3 4 N VAL B 83  ? N VAL B 82  O LYS B 92  ? O LYS B 91  
AA8 1 2 N THR D 6   ? N THR E 5   O SER D 25  ? O SER E 24  
AA8 2 3 N VAL D 22  ? N VAL E 21  O LEU D 77  ? O LEU E 76  
AA8 3 4 O ILE D 78  ? O ILE E 77  N LYS D 66  ? N LYS E 65  
AA9 1 2 N THR D 14  ? N THR E 13  O LEU D 117 ? O LEU E 116 
AA9 2 3 O THR D 112 ? O THR E 111 N TYR D 90  ? N TYR E 89  
AA9 3 4 O ALA D 93  ? O ALA E 92  N SER D 34  ? N SER E 33  
AA9 4 5 N MET D 33  ? N MET E 32  O SER D 50  ? O SER E 49  
AA9 5 6 N TYR D 49  ? N TYR E 48  O ASP D 57  ? O ASP E 56  
AB1 1 2 N THR D 14  ? N THR E 13  O LEU D 117 ? O LEU E 116 
AB1 2 3 O THR D 112 ? O THR E 111 N TYR D 90  ? N TYR E 89  
AB1 3 4 N SER D 94  ? N SER E 93  O TYR D 107 ? O TYR E 106 
AB2 1 2 N PHE D 131 ? N PHE E 130 O VAL D 147 ? O VAL E 146 
AB2 2 3 N ALA D 144 ? N ALA E 143 O VAL D 199 ? O VAL E 198 
AB2 3 4 O ARG D 196 ? O ARG E 195 N CYS D 174 ? N CYS E 173 
AB3 1 2 N PHE D 131 ? N PHE E 130 O VAL D 147 ? O VAL E 146 
AB3 2 3 N ALA D 144 ? N ALA E 143 O VAL D 199 ? O VAL E 198 
AB3 3 4 O ALA D 192 ? O ALA E 191 N LEU D 180 ? N LEU E 179 
AB4 1 2 O LYS D 167 ? O LYS E 166 N VAL D 164 ? N VAL E 163 
AB4 2 3 N GLU D 159 ? N GLU E 158 O GLN D 216 ? O GLN E 215 
AB4 3 4 N PHE D 217 ? N PHE E 216 O GLN D 236 ? O GLN E 235 
AB5 1 2 N THR E 6   ? N THR D 5   O LEU E 25  ? O LEU D 24  
AB6 1 2 N VAL E 12  ? N VAL D 11  O THR E 108 ? O THR D 107 
AB6 2 3 O LEU E 109 ? O LEU D 108 N ALA E 88  ? N ALA D 87  
AB6 3 4 O ALA E 93  ? O ALA D 92  N PHE E 36  ? N PHE D 35  
AB6 4 5 N LYS E 39  ? N LYS D 38  O ILE E 47  ? O ILE D 46  
AB7 1 2 N VAL E 12  ? N VAL D 11  O THR E 108 ? O THR D 107 
AB7 2 3 O LEU E 109 ? O LEU D 108 N ALA E 88  ? N ALA D 87  
AB7 3 4 N LEU E 94  ? N LEU D 93  O THR E 102 ? O THR D 101 
AB8 1 2 N LEU E 22  ? N LEU D 21  O LEU E 77  ? O LEU D 76  
AB8 2 3 O SER E 74  ? O SER D 73  N LYS E 69  ? N LYS D 68  
AB8 3 4 O TYR E 64  ? O TYR D 63  N SER E 61  ? N SER D 60  
AB9 1 2 N TYR E 123 ? N TYR D 122 O LEU E 137 ? O LEU D 136 
AB9 2 3 N CYS E 136 ? N CYS D 135 O ALA E 177 ? O ALA D 176 
AB9 3 4 O TRP E 178 ? O TRP D 177 N TYR E 156 ? N TYR D 155 
AC1 1 2 N TYR E 123 ? N TYR D 122 O LEU E 137 ? O LEU D 136 
AC1 2 3 N CYS E 136 ? N CYS D 135 O ALA E 177 ? O ALA D 176 
AC1 3 4 O PHE E 170 ? O PHE D 169 N MET E 165 ? N MET D 164 
# 
_pdbx_entry_details.entry_id                   8YJ2 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE1 A GLU 232 ? ? OG B SER 28  ? ? 1.19 
2  1 O   E HOH 450 ? ? O  E HOH 451 ? ? 1.80 
3  1 NH1 E ARG 244 ? ? O  E HOH 301 ? ? 1.81 
4  1 NE2 D GLN 148 ? ? O  D HOH 301 ? ? 1.86 
5  1 O   E HOH 372 ? ? O  E HOH 445 ? ? 1.86 
6  1 OH  E TYR 190 ? ? O  E HOH 302 ? ? 1.89 
7  1 NZ  A LYS 176 ? ? O  A HOH 301 ? ? 1.93 
8  1 O   A VAL 231 ? ? NZ A LYS 243 ? ? 1.93 
9  1 O   A HOH 354 ? ? O  B HOH 146 ? ? 1.98 
10 1 O   D SER 133 ? ? O  D HOH 302 ? ? 1.99 
11 1 O   B HOH 131 ? ? O  B HOH 140 ? ? 2.00 
12 1 OG  D SER 73  ? ? O  D HOH 303 ? ? 2.04 
13 1 O   D SER 202 ? ? O  D HOH 304 ? ? 2.07 
14 1 OH  E TYR 35  ? ? O  E HOH 303 ? ? 2.07 
15 1 O   D HOH 371 ? ? O  D HOH 390 ? ? 2.07 
16 1 O   D HOH 313 ? ? O  D HOH 388 ? ? 2.09 
17 1 O   B HIS 84  ? ? O  B HOH 101 ? ? 2.09 
18 1 NZ  D LYS 99  ? ? O  D HOH 305 ? ? 2.10 
19 1 O   D ILE 193 ? ? O  D HOH 306 ? ? 2.15 
20 1 O   B HOH 127 ? ? O  B HOH 133 ? ? 2.18 
21 1 OG1 D THR 107 ? ? O  D HOH 307 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   E HOH 372 ? ? 1_555 O E HOH 428 ? ? 3_654 2.05 
2 1 NH1 A ARG 108 ? ? 1_555 O D SER 129 ? ? 7_554 2.07 
3 1 O   E HOH 430 ? ? 1_555 O E HOH 445 ? ? 3_654 2.12 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD E GLU 103 ? ? OE1 E GLU 103 ? ? 1.169 1.252 -0.083 0.011 N 
2 1 CD E GLU 103 ? ? OE2 E GLU 103 ? ? 1.175 1.252 -0.077 0.011 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              108 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              108 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              108 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                115.79 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -4.51 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 17  ? ? -153.09 21.69   
2  1 ASP A 29  ? ? 52.74   -124.68 
3  1 TYR A 123 ? ? -109.05 -61.01  
4  1 SER A 195 ? ? -112.30 -151.48 
5  1 THR A 225 ? ? -98.02  34.57   
6  1 PRO B 32  ? ? -76.36  -167.99 
7  1 TRP B 60  ? ? 80.01   -0.22   
8  1 GLU C 8   ? ? -141.94 28.08   
9  1 ILE E 46  ? ? -94.50  -63.04  
10 1 HIS E 156 ? ? -103.42 78.76   
11 1 ARG D 16  ? ? 71.84   -5.39   
12 1 ALA D 97  ? ? -150.46 43.69   
13 1 ASP D 118 ? ? -154.01 58.01   
14 1 PHE D 189 ? ? -98.37  33.79   
15 1 ASP D 197 ? ? -89.84  30.41   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    E 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     327 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   I 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 0   ? A MET 1   
2 1 Y 1 E MET 0   ? D MET 1   
3 1 Y 1 E GLU 1   ? D GLU 2   
4 1 Y 1 D MET 0   ? E MET 1   
5 1 Y 1 D PRO 203 ? E PRO 204 
6 1 Y 1 D GLU 204 ? E GLU 205 
7 1 Y 1 D SER 205 ? E SER 206 
8 1 Y 1 D SER 206 ? E SER 207 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 32270995 1 
'National Natural Science Foundation of China (NSFC)' China 32100985 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8YIV 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YJ2 
_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]   0.013981 
_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]   0.007454 
_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]   0.004502 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 2   ? 8.483  35.918  -25.497 1.00 67.25  ? 1   GLY A N   1 
ATOM   2    C CA  . GLY A 1 2   ? 8.234  34.909  -24.482 1.00 57.98  ? 1   GLY A CA  1 
ATOM   3    C C   . GLY A 1 2   ? 8.845  33.585  -24.885 1.00 55.17  ? 1   GLY A C   1 
ATOM   4    O O   . GLY A 1 2   ? 8.167  32.713  -25.436 1.00 56.16  ? 1   GLY A O   1 
ATOM   5    N N   . SER A 1 3   ? 10.138 33.443  -24.622 1.00 45.55  ? 2   SER A N   1 
ATOM   6    C CA  . SER A 1 3   ? 10.858 32.236  -24.980 1.00 44.58  ? 2   SER A CA  1 
ATOM   7    C C   . SER A 1 3   ? 10.729 31.191  -23.875 1.00 38.13  ? 2   SER A C   1 
ATOM   8    O O   . SER A 1 3   ? 10.338 31.484  -22.743 1.00 41.90  ? 2   SER A O   1 
ATOM   9    C CB  . SER A 1 3   ? 12.326 32.553  -25.255 1.00 44.33  ? 2   SER A CB  1 
ATOM   10   O OG  . SER A 1 3   ? 12.889 33.277  -24.176 1.00 56.09  ? 2   SER A OG  1 
ATOM   11   N N   . HIS A 1 4   ? 11.036 29.949  -24.222 1.00 38.03  ? 3   HIS A N   1 
ATOM   12   C CA  . HIS A 1 4   ? 10.954 28.869  -23.258 1.00 35.70  ? 3   HIS A CA  1 
ATOM   13   C C   . HIS A 1 4   ? 12.206 28.010  -23.339 1.00 37.82  ? 3   HIS A C   1 
ATOM   14   O O   . HIS A 1 4   ? 13.036 28.158  -24.247 1.00 33.73  ? 3   HIS A O   1 
ATOM   15   C CB  . HIS A 1 4   ? 9.701  28.014  -23.462 1.00 31.87  ? 3   HIS A CB  1 
ATOM   16   C CG  . HIS A 1 4   ? 8.427  28.778  -23.313 1.00 39.39  ? 3   HIS A CG  1 
ATOM   17   N ND1 . HIS A 1 4   ? 7.783  28.918  -22.105 1.00 35.69  ? 3   HIS A ND1 1 
ATOM   18   C CD2 . HIS A 1 4   ? 7.675  29.447  -24.221 1.00 39.37  ? 3   HIS A CD2 1 
ATOM   19   C CE1 . HIS A 1 4   ? 6.681  29.627  -22.276 1.00 40.64  ? 3   HIS A CE1 1 
ATOM   20   N NE2 . HIS A 1 4   ? 6.594  29.962  -23.551 1.00 40.35  ? 3   HIS A NE2 1 
ATOM   21   N N   . SER A 1 5   ? 12.328 27.103  -22.364 1.00 31.16  ? 4   SER A N   1 
ATOM   22   C CA  . SER A 1 5   ? 13.530 26.304  -22.194 1.00 33.66  ? 4   SER A CA  1 
ATOM   23   C C   . SER A 1 5   ? 13.164 24.880  -21.823 1.00 27.21  ? 4   SER A C   1 
ATOM   24   O O   . SER A 1 5   ? 12.157 24.636  -21.155 1.00 30.15  ? 4   SER A O   1 
ATOM   25   C CB  . SER A 1 5   ? 14.449 26.887  -21.096 1.00 31.19  ? 4   SER A CB  1 
ATOM   26   O OG  . SER A 1 5   ? 15.177 27.980  -21.612 1.00 38.51  ? 4   SER A OG  1 
ATOM   27   N N   . MET A 1 6   ? 14.011 23.941  -22.230 1.00 27.95  ? 5   MET A N   1 
ATOM   28   C CA  . MET A 1 6   ? 13.992 22.604  -21.644 1.00 31.71  ? 5   MET A CA  1 
ATOM   29   C C   . MET A 1 6   ? 15.411 22.244  -21.250 1.00 28.74  ? 5   MET A C   1 
ATOM   30   O O   . MET A 1 6   ? 16.357 22.578  -21.965 1.00 27.28  ? 5   MET A O   1 
ATOM   31   C CB  . MET A 1 6   ? 13.422 21.542  -22.584 1.00 23.42  ? 5   MET A CB  1 
ATOM   32   C CG  . MET A 1 6   ? 13.205 20.211  -21.897 1.00 25.27  ? 5   MET A CG  1 
ATOM   33   S SD  . MET A 1 6   ? 12.267 19.015  -22.866 1.00 35.30  ? 5   MET A SD  1 
ATOM   34   C CE  . MET A 1 6   ? 13.360 18.760  -24.278 1.00 25.49  ? 5   MET A CE  1 
ATOM   35   N N   . ARG A 1 7   ? 15.563 21.608  -20.090 1.00 27.41  ? 6   ARG A N   1 
ATOM   36   C CA  . ARG A 1 7   ? 16.888 21.363  -19.539 1.00 25.25  ? 6   ARG A CA  1 
ATOM   37   C C   . ARG A 1 7   ? 16.900 20.042  -18.790 1.00 25.09  ? 6   ARG A C   1 
ATOM   38   O O   . ARG A 1 7   ? 15.931 19.691  -18.115 1.00 25.88  ? 6   ARG A O   1 
ATOM   39   C CB  . ARG A 1 7   ? 17.328 22.477  -18.578 1.00 24.40  ? 6   ARG A CB  1 
ATOM   40   C CG  . ARG A 1 7   ? 17.513 23.870  -19.175 1.00 27.61  ? 6   ARG A CG  1 
ATOM   41   C CD  . ARG A 1 7   ? 18.849 24.014  -19.886 1.00 32.72  ? 6   ARG A CD  1 
ATOM   42   N NE  . ARG A 1 7   ? 19.122 25.418  -20.203 1.00 38.60  ? 6   ARG A NE  1 
ATOM   43   C CZ  . ARG A 1 7   ? 18.705 26.035  -21.308 1.00 39.83  ? 6   ARG A CZ  1 
ATOM   44   N NH1 . ARG A 1 7   ? 17.989 25.371  -22.225 1.00 30.06  ? 6   ARG A NH1 1 
ATOM   45   N NH2 . ARG A 1 7   ? 19.004 27.318  -21.494 1.00 37.87  ? 6   ARG A NH2 1 
ATOM   46   N N   . TYR A 1 8   ? 18.011 19.330  -18.892 1.00 23.25  ? 7   TYR A N   1 
ATOM   47   C CA  . TYR A 1 8   ? 18.246 18.139  -18.095 1.00 22.13  ? 7   TYR A CA  1 
ATOM   48   C C   . TYR A 1 8   ? 19.490 18.352  -17.249 1.00 19.97  ? 7   TYR A C   1 
ATOM   49   O O   . TYR A 1 8   ? 20.489 18.900  -17.716 1.00 22.70  ? 7   TYR A O   1 
ATOM   50   C CB  . TYR A 1 8   ? 18.399 16.897  -18.976 1.00 20.82  ? 7   TYR A CB  1 
ATOM   51   C CG  . TYR A 1 8   ? 17.073 16.334  -19.424 1.00 24.80  ? 7   TYR A CG  1 
ATOM   52   C CD1 . TYR A 1 8   ? 16.377 15.435  -18.629 1.00 19.42  ? 7   TYR A CD1 1 
ATOM   53   C CD2 . TYR A 1 8   ? 16.501 16.728  -20.633 1.00 21.84  ? 7   TYR A CD2 1 
ATOM   54   C CE1 . TYR A 1 8   ? 15.158 14.930  -19.027 1.00 22.90  ? 7   TYR A CE1 1 
ATOM   55   C CE2 . TYR A 1 8   ? 15.273 16.228  -21.040 1.00 23.88  ? 7   TYR A CE2 1 
ATOM   56   C CZ  . TYR A 1 8   ? 14.611 15.320  -20.244 1.00 24.66  ? 7   TYR A CZ  1 
ATOM   57   O OH  . TYR A 1 8   ? 13.393 14.794  -20.650 1.00 24.12  ? 7   TYR A OH  1 
ATOM   58   N N   . PHE A 1 9   ? 19.412 17.939  -15.997 1.00 22.97  ? 8   PHE A N   1 
ATOM   59   C CA  . PHE A 1 9   ? 20.499 18.123  -15.041 1.00 22.66  ? 8   PHE A CA  1 
ATOM   60   C C   . PHE A 1 9   ? 20.851 16.747  -14.489 1.00 18.87  ? 8   PHE A C   1 
ATOM   61   O O   . PHE A 1 9   ? 20.044 16.145  -13.783 1.00 21.44  ? 8   PHE A O   1 
ATOM   62   C CB  . PHE A 1 9   ? 20.076 19.078  -13.927 1.00 23.20  ? 8   PHE A CB  1 
ATOM   63   C CG  . PHE A 1 9   ? 19.727 20.473  -14.400 1.00 21.27  ? 8   PHE A CG  1 
ATOM   64   C CD1 . PHE A 1 9   ? 20.699 21.441  -14.521 1.00 26.12  ? 8   PHE A CD1 1 
ATOM   65   C CD2 . PHE A 1 9   ? 18.416 20.820  -14.673 1.00 27.37  ? 8   PHE A CD2 1 
ATOM   66   C CE1 . PHE A 1 9   ? 20.376 22.755  -14.936 1.00 30.10  ? 8   PHE A CE1 1 
ATOM   67   C CE2 . PHE A 1 9   ? 18.079 22.121  -15.076 1.00 25.13  ? 8   PHE A CE2 1 
ATOM   68   C CZ  . PHE A 1 9   ? 19.070 23.087  -15.213 1.00 26.47  ? 8   PHE A CZ  1 
ATOM   69   N N   . PHE A 1 10  ? 22.025 16.238  -14.835 1.00 15.24  ? 9   PHE A N   1 
ATOM   70   C CA  . PHE A 1 10  ? 22.469 14.913  -14.410 1.00 20.78  ? 9   PHE A CA  1 
ATOM   71   C C   . PHE A 1 10  ? 23.546 15.038  -13.337 1.00 21.92  ? 9   PHE A C   1 
ATOM   72   O O   . PHE A 1 10  ? 24.461 15.859  -13.466 1.00 19.55  ? 9   PHE A O   1 
ATOM   73   C CB  . PHE A 1 10  ? 23.037 14.105  -15.596 1.00 22.72  ? 9   PHE A CB  1 
ATOM   74   C CG  . PHE A 1 10  ? 22.070 13.920  -16.743 1.00 24.90  ? 9   PHE A CG  1 
ATOM   75   C CD1 . PHE A 1 10  ? 21.884 14.918  -17.689 1.00 26.33  ? 9   PHE A CD1 1 
ATOM   76   C CD2 . PHE A 1 10  ? 21.355 12.745  -16.876 1.00 24.41  ? 9   PHE A CD2 1 
ATOM   77   C CE1 . PHE A 1 10  ? 20.991 14.728  -18.748 1.00 25.43  ? 9   PHE A CE1 1 
ATOM   78   C CE2 . PHE A 1 10  ? 20.470 12.560  -17.917 1.00 25.64  ? 9   PHE A CE2 1 
ATOM   79   C CZ  . PHE A 1 10  ? 20.284 13.544  -18.851 1.00 23.00  ? 9   PHE A CZ  1 
ATOM   80   N N   . THR A 1 11  ? 23.447 14.214  -12.284 1.00 19.81  ? 10  THR A N   1 
ATOM   81   C CA  . THR A 1 11  ? 24.483 14.136  -11.258 1.00 20.61  ? 10  THR A CA  1 
ATOM   82   C C   . THR A 1 11  ? 24.843 12.677  -11.020 1.00 23.31  ? 10  THR A C   1 
ATOM   83   O O   . THR A 1 11  ? 23.971 11.858  -10.709 1.00 22.87  ? 10  THR A O   1 
ATOM   84   C CB  . THR A 1 11  ? 24.044 14.785  -9.928  1.00 26.64  ? 10  THR A CB  1 
ATOM   85   O OG1 . THR A 1 11  ? 23.612 16.131  -10.150 1.00 24.70  ? 10  THR A OG1 1 
ATOM   86   C CG2 . THR A 1 11  ? 25.217 14.821  -8.939  1.00 20.95  ? 10  THR A CG2 1 
ATOM   87   N N   . SER A 1 12  ? 26.131 12.367  -11.101 1.00 20.62  ? 11  SER A N   1 
ATOM   88   C CA  . SER A 1 12  ? 26.619 10.998  -10.961 1.00 27.10  ? 11  SER A CA  1 
ATOM   89   C C   . SER A 1 12  ? 27.788 11.003  -9.985  1.00 25.47  ? 11  SER A C   1 
ATOM   90   O O   . SER A 1 12  ? 28.799 11.670  -10.229 1.00 25.17  ? 11  SER A O   1 
ATOM   91   C CB  . SER A 1 12  ? 27.042 10.440  -12.322 1.00 24.12  ? 11  SER A CB  1 
ATOM   92   O OG  . SER A 1 12  ? 25.937 10.433  -13.224 1.00 24.97  ? 11  SER A OG  1 
ATOM   93   N N   . VAL A 1 13  ? 27.655 10.271  -8.886  1.00 21.85  ? 12  VAL A N   1 
ATOM   94   C CA  . VAL A 1 13  ? 28.555 10.413  -7.740  1.00 26.37  ? 12  VAL A CA  1 
ATOM   95   C C   . VAL A 1 13  ? 29.160 9.050   -7.408  1.00 25.82  ? 12  VAL A C   1 
ATOM   96   O O   . VAL A 1 13  ? 28.434 8.113   -7.056  1.00 30.07  ? 12  VAL A O   1 
ATOM   97   C CB  . VAL A 1 13  ? 27.818 10.998  -6.515  1.00 28.29  ? 12  VAL A CB  1 
ATOM   98   C CG1 . VAL A 1 13  ? 28.739 11.163  -5.327  1.00 28.17  ? 12  VAL A CG1 1 
ATOM   99   C CG2 . VAL A 1 13  ? 27.193 12.345  -6.853  1.00 25.78  ? 12  VAL A CG2 1 
ATOM   100  N N   . SER A 1 14  ? 30.482 8.940   -7.505  1.00 26.37  ? 13  SER A N   1 
ATOM   101  C CA  . SER A 1 14  ? 31.160 7.753   -7.002  1.00 27.97  ? 13  SER A CA  1 
ATOM   102  C C   . SER A 1 14  ? 31.146 7.749   -5.476  1.00 33.82  ? 13  SER A C   1 
ATOM   103  O O   . SER A 1 14  ? 31.278 8.787   -4.825  1.00 32.31  ? 13  SER A O   1 
ATOM   104  C CB  . SER A 1 14  ? 32.584 7.663   -7.554  1.00 27.93  ? 13  SER A CB  1 
ATOM   105  O OG  . SER A 1 14  ? 33.451 8.640   -7.014  1.00 29.44  ? 13  SER A OG  1 
ATOM   106  N N   . ARG A 1 15  ? 30.949 6.578   -4.908  1.00 34.55  ? 14  ARG A N   1 
ATOM   107  C CA  . ARG A 1 15  ? 30.824 6.384   -3.449  1.00 45.18  ? 14  ARG A CA  1 
ATOM   108  C C   . ARG A 1 15  ? 31.751 5.253   -3.023  1.00 55.17  ? 14  ARG A C   1 
ATOM   109  O O   . ARG A 1 15  ? 31.299 4.157   -2.912  1.00 59.94  ? 14  ARG A O   1 
ATOM   110  C CB  . ARG A 1 15  ? 29.388 5.992   -3.106  1.00 50.10  ? 14  ARG A CB  1 
ATOM   111  C CG  . ARG A 1 15  ? 28.340 7.045   -3.399  1.00 42.51  ? 14  ARG A CG  1 
ATOM   112  C CD  . ARG A 1 15  ? 26.955 6.601   -3.015  1.00 49.48  ? 14  ARG A CD  1 
ATOM   113  N NE  . ARG A 1 15  ? 26.444 5.522   -3.822  1.00 49.25  ? 14  ARG A NE  1 
ATOM   114  C CZ  . ARG A 1 15  ? 25.188 5.155   -3.861  1.00 46.94  ? 14  ARG A CZ  1 
ATOM   115  N NH1 . ARG A 1 15  ? 24.290 5.778   -3.136  1.00 45.41  ? 14  ARG A NH1 1 
ATOM   116  N NH2 . ARG A 1 15  ? 24.827 4.168   -4.633  1.00 44.81  ? 14  ARG A NH2 1 
ATOM   117  N N   . PRO A 1 16  ? 33.030 5.513   -2.729  1.00 57.75  ? 15  PRO A N   1 
ATOM   118  C CA  . PRO A 1 16  ? 33.966 4.460   -2.390  1.00 65.59  ? 15  PRO A CA  1 
ATOM   119  C C   . PRO A 1 16  ? 33.654 4.043   -0.957  1.00 72.72  ? 15  PRO A C   1 
ATOM   120  O O   . PRO A 1 16  ? 33.895 4.793   -0.100  1.00 69.34  ? 15  PRO A O   1 
ATOM   121  C CB  . PRO A 1 16  ? 35.304 5.175   -2.465  1.00 58.67  ? 15  PRO A CB  1 
ATOM   122  C CG  . PRO A 1 16  ? 34.994 6.611   -2.123  1.00 57.19  ? 15  PRO A CG  1 
ATOM   123  C CD  . PRO A 1 16  ? 33.578 6.839   -2.581  1.00 52.09  ? 15  PRO A CD  1 
ATOM   124  N N   . GLY A 1 17  ? 33.128 2.847   -0.781  1.00 86.17  ? 16  GLY A N   1 
ATOM   125  C CA  . GLY A 1 17  ? 32.659 2.408   0.538   1.00 100.03 ? 16  GLY A CA  1 
ATOM   126  C C   . GLY A 1 17  ? 31.158 2.178   0.658   1.00 118.09 ? 16  GLY A C   1 
ATOM   127  O O   . GLY A 1 17  ? 30.694 1.987   1.786   1.00 124.75 ? 16  GLY A O   1 
ATOM   128  N N   . ARG A 1 18  ? 30.436 2.218   -0.469  1.00 153.66 ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 18  ? 28.951 2.234   -0.542  1.00 159.43 ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 18  ? 28.530 1.622   -1.873  1.00 123.93 ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 18  ? 27.451 1.911   -2.339  1.00 104.98 ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 18  ? 28.381 3.640   -0.394  1.00 141.19 ? 17  ARG A CB  1 
ATOM   133  N N   . GLY A 1 19  ? 29.417 0.833   -2.454  1.00 105.80 ? 18  GLY A N   1 
ATOM   134  C CA  . GLY A 1 19  ? 29.170 0.067   -3.683  1.00 98.14  ? 18  GLY A CA  1 
ATOM   135  C C   . GLY A 1 19  ? 29.163 0.894   -4.948  1.00 86.49  ? 18  GLY A C   1 
ATOM   136  O O   . GLY A 1 19  ? 30.077 1.645   -5.186  1.00 83.92  ? 18  GLY A O   1 
ATOM   137  N N   . GLU A 1 20  ? 28.110 0.710   -5.720  1.00 74.51  ? 19  GLU A N   1 
ATOM   138  C CA  . GLU A 1 20  ? 27.846 1.349   -7.023  1.00 65.01  ? 19  GLU A CA  1 
ATOM   139  C C   . GLU A 1 20  ? 27.706 2.875   -6.885  1.00 52.76  ? 19  GLU A C   1 
ATOM   140  O O   . GLU A 1 20  ? 27.342 3.376   -5.842  1.00 48.05  ? 19  GLU A O   1 
ATOM   141  C CB  . GLU A 1 20  ? 26.532 0.716   -7.477  1.00 63.64  ? 19  GLU A CB  1 
ATOM   142  C CG  . GLU A 1 20  ? 25.535 0.594   -6.328  1.00 66.85  ? 19  GLU A CG  1 
ATOM   143  C CD  . GLU A 1 20  ? 24.295 -0.289  -6.472  1.00 67.98  ? 19  GLU A CD  1 
ATOM   144  O OE1 . GLU A 1 20  ? 24.263 -1.354  -5.826  1.00 69.19  ? 19  GLU A OE1 1 
ATOM   145  O OE2 . GLU A 1 20  ? 23.338 0.105   -7.201  1.00 62.53  ? 19  GLU A OE2 1 
ATOM   146  N N   . PRO A 1 21  ? 27.980 3.651   -7.933  1.00 42.04  ? 20  PRO A N   1 
ATOM   147  C CA  . PRO A 1 21  ? 27.766 5.076   -7.874  1.00 38.23  ? 20  PRO A CA  1 
ATOM   148  C C   . PRO A 1 21  ? 26.286 5.495   -7.856  1.00 34.63  ? 20  PRO A C   1 
ATOM   149  O O   . PRO A 1 21  ? 25.478 4.745   -8.204  1.00 37.77  ? 20  PRO A O   1 
ATOM   150  C CB  . PRO A 1 21  ? 28.449 5.577   -9.153  1.00 34.87  ? 20  PRO A CB  1 
ATOM   151  C CG  . PRO A 1 21  ? 29.277 4.437   -9.637  1.00 33.75  ? 20  PRO A CG  1 
ATOM   152  C CD  . PRO A 1 21  ? 28.595 3.197   -9.143  1.00 40.48  ? 20  PRO A CD  1 
ATOM   153  N N   . ARG A 1 22  ? 25.978 6.701   -7.415  1.00 27.82  ? 21  ARG A N   1 
ATOM   154  C CA  . ARG A 1 22  ? 24.575 7.171   -7.470  1.00 31.00  ? 21  ARG A CA  1 
ATOM   155  C C   . ARG A 1 22  ? 24.345 7.985   -8.748  1.00 26.45  ? 21  ARG A C   1 
ATOM   156  O O   . ARG A 1 22  ? 25.106 8.818   -9.047  1.00 27.20  ? 21  ARG A O   1 
ATOM   157  C CB  . ARG A 1 22  ? 24.146 7.923   -6.211  1.00 31.28  ? 21  ARG A CB  1 
ATOM   158  C CG  . ARG A 1 22  ? 22.648 8.011   -6.018  1.00 31.96  ? 21  ARG A CG  1 
ATOM   159  C CD  . ARG A 1 22  ? 22.227 8.995   -4.962  1.00 35.85  ? 21  ARG A CD  1 
ATOM   160  N NE  . ARG A 1 22  ? 20.885 8.821   -4.469  1.00 40.66  ? 21  ARG A NE  1 
ATOM   161  C CZ  . ARG A 1 22  ? 20.357 9.550   -3.510  1.00 43.21  ? 21  ARG A CZ  1 
ATOM   162  N NH1 . ARG A 1 22  ? 21.086 10.467  -2.928  1.00 45.29  ? 21  ARG A NH1 1 
ATOM   163  N NH2 . ARG A 1 22  ? 19.121 9.371   -3.116  1.00 37.54  ? 21  ARG A NH2 1 
ATOM   164  N N   . PHE A 1 23  ? 23.270 7.708   -9.449  1.00 26.05  ? 22  PHE A N   1 
ATOM   165  C CA  . PHE A 1 23  ? 22.952 8.400   -10.691 1.00 24.32  ? 22  PHE A CA  1 
ATOM   166  C C   . PHE A 1 23  ? 21.623 9.120   -10.529 1.00 22.84  ? 22  PHE A C   1 
ATOM   167  O O   . PHE A 1 23  ? 20.609 8.486   -10.242 1.00 23.33  ? 22  PHE A O   1 
ATOM   168  C CB  . PHE A 1 23  ? 22.892 7.415   -11.862 1.00 22.26  ? 22  PHE A CB  1 
ATOM   169  C CG  . PHE A 1 23  ? 24.147 6.589   -12.033 1.00 22.36  ? 22  PHE A CG  1 
ATOM   170  C CD1 . PHE A 1 23  ? 25.262 7.131   -12.651 1.00 22.04  ? 22  PHE A CD1 1 
ATOM   171  C CD2 . PHE A 1 23  ? 24.200 5.262   -11.597 1.00 24.61  ? 22  PHE A CD2 1 
ATOM   172  C CE1 . PHE A 1 23  ? 26.430 6.386   -12.816 1.00 23.45  ? 22  PHE A CE1 1 
ATOM   173  C CE2 . PHE A 1 23  ? 25.366 4.499   -11.759 1.00 26.22  ? 22  PHE A CE2 1 
ATOM   174  C CZ  . PHE A 1 23  ? 26.484 5.068   -12.372 1.00 25.05  ? 22  PHE A CZ  1 
ATOM   175  N N   . ILE A 1 24  ? 21.623 10.437  -10.733 1.00 20.68  ? 23  ILE A N   1 
ATOM   176  C CA  . ILE A 1 24  ? 20.429 11.250  -10.574 1.00 22.58  ? 23  ILE A CA  1 
ATOM   177  C C   . ILE A 1 24  ? 20.265 12.115  -11.813 1.00 23.33  ? 23  ILE A C   1 
ATOM   178  O O   . ILE A 1 24  ? 21.253 12.552  -12.413 1.00 21.70  ? 23  ILE A O   1 
ATOM   179  C CB  . ILE A 1 24  ? 20.499 12.115  -9.293  1.00 24.20  ? 23  ILE A CB  1 
ATOM   180  C CG1 . ILE A 1 24  ? 20.370 11.231  -8.041  1.00 29.07  ? 23  ILE A CG1 1 
ATOM   181  C CG2 . ILE A 1 24  ? 19.392 13.133  -9.259  1.00 23.07  ? 23  ILE A CG2 1 
ATOM   182  C CD1 . ILE A 1 24  ? 20.663 11.999  -6.721  1.00 25.19  ? 23  ILE A CD1 1 
ATOM   183  N N   . ALA A 1 25  ? 19.016 12.349  -12.210 1.00 22.46  ? 24  ALA A N   1 
ATOM   184  C CA  . ALA A 1 25  ? 18.752 13.254  -13.318 1.00 22.07  ? 24  ALA A CA  1 
ATOM   185  C C   . ALA A 1 25  ? 17.404 13.897  -13.080 1.00 23.68  ? 24  ALA A C   1 
ATOM   186  O O   . ALA A 1 25  ? 16.483 13.240  -12.587 1.00 22.25  ? 24  ALA A O   1 
ATOM   187  C CB  . ALA A 1 25  ? 18.758 12.528  -14.674 1.00 23.85  ? 24  ALA A CB  1 
ATOM   188  N N   . VAL A 1 26  ? 17.291 15.179  -13.422 1.00 22.69  ? 25  VAL A N   1 
ATOM   189  C CA  . VAL A 1 26  ? 16.009 15.867  -13.365 1.00 23.96  ? 25  VAL A CA  1 
ATOM   190  C C   . VAL A 1 26  ? 15.836 16.654  -14.656 1.00 24.41  ? 25  VAL A C   1 
ATOM   191  O O   . VAL A 1 26  ? 16.811 17.126  -15.252 1.00 23.84  ? 25  VAL A O   1 
ATOM   192  C CB  . VAL A 1 26  ? 15.890 16.787  -12.115 1.00 24.88  ? 25  VAL A CB  1 
ATOM   193  C CG1 . VAL A 1 26  ? 16.039 15.977  -10.826 1.00 22.52  ? 25  VAL A CG1 1 
ATOM   194  C CG2 . VAL A 1 26  ? 16.946 17.861  -12.145 1.00 23.21  ? 25  VAL A CG2 1 
ATOM   195  N N   . GLY A 1 27  ? 14.586 16.768  -15.104 1.00 24.91  ? 26  GLY A N   1 
ATOM   196  C CA  . GLY A 1 27  ? 14.254 17.561  -16.270 1.00 21.00  ? 26  GLY A CA  1 
ATOM   197  C C   . GLY A 1 27  ? 13.361 18.735  -15.900 1.00 29.00  ? 26  GLY A C   1 
ATOM   198  O O   . GLY A 1 27  ? 12.513 18.637  -15.005 1.00 23.27  ? 26  GLY A O   1 
ATOM   199  N N   . TYR A 1 28  ? 13.554 19.853  -16.611 1.00 24.53  ? 27  TYR A N   1 
ATOM   200  C CA  . TYR A 1 28  ? 12.771 21.066  -16.426 1.00 27.10  ? 27  TYR A CA  1 
ATOM   201  C C   . TYR A 1 28  ? 12.260 21.592  -17.762 1.00 28.39  ? 27  TYR A C   1 
ATOM   202  O O   . TYR A 1 28  ? 12.965 21.533  -18.774 1.00 28.62  ? 27  TYR A O   1 
ATOM   203  C CB  . TYR A 1 28  ? 13.596 22.172  -15.780 1.00 27.05  ? 27  TYR A CB  1 
ATOM   204  C CG  . TYR A 1 28  ? 13.810 22.049  -14.281 1.00 33.69  ? 27  TYR A CG  1 
ATOM   205  C CD1 . TYR A 1 28  ? 14.759 21.175  -13.768 1.00 31.25  ? 27  TYR A CD1 1 
ATOM   206  C CD2 . TYR A 1 28  ? 13.089 22.839  -13.383 1.00 32.34  ? 27  TYR A CD2 1 
ATOM   207  C CE1 . TYR A 1 28  ? 14.974 21.068  -12.402 1.00 31.30  ? 27  TYR A CE1 1 
ATOM   208  C CE2 . TYR A 1 28  ? 13.297 22.737  -12.018 1.00 33.45  ? 27  TYR A CE2 1 
ATOM   209  C CZ  . TYR A 1 28  ? 14.246 21.850  -11.540 1.00 32.15  ? 27  TYR A CZ  1 
ATOM   210  O OH  . TYR A 1 28  ? 14.482 21.740  -10.204 1.00 32.45  ? 27  TYR A OH  1 
ATOM   211  N N   . VAL A 1 29  ? 11.033 22.110  -17.756 1.00 31.33  ? 28  VAL A N   1 
ATOM   212  C CA  . VAL A 1 29  ? 10.574 23.095  -18.738 1.00 30.28  ? 28  VAL A CA  1 
ATOM   213  C C   . VAL A 1 29  ? 10.489 24.441  -18.018 1.00 30.91  ? 28  VAL A C   1 
ATOM   214  O O   . VAL A 1 29  ? 9.756  24.580  -17.031 1.00 25.14  ? 28  VAL A O   1 
ATOM   215  C CB  . VAL A 1 29  ? 9.224  22.700  -19.355 1.00 29.49  ? 28  VAL A CB  1 
ATOM   216  C CG1 . VAL A 1 29  ? 8.741  23.792  -20.301 1.00 30.95  ? 28  VAL A CG1 1 
ATOM   217  C CG2 . VAL A 1 29  ? 9.350  21.369  -20.105 1.00 23.94  ? 28  VAL A CG2 1 
ATOM   218  N N   . ASP A 1 30  ? 11.245 25.430  -18.501 1.00 32.53  ? 29  ASP A N   1 
ATOM   219  C CA  . ASP A 1 30  ? 11.377 26.736  -17.822 1.00 35.36  ? 29  ASP A CA  1 
ATOM   220  C C   . ASP A 1 30  ? 11.785 26.454  -16.373 1.00 36.65  ? 29  ASP A C   1 
ATOM   221  O O   . ASP A 1 30  ? 12.790 25.765  -16.145 1.00 32.98  ? 29  ASP A O   1 
ATOM   222  C CB  . ASP A 1 30  ? 10.098 27.554  -17.988 1.00 34.66  ? 29  ASP A CB  1 
ATOM   223  C CG  . ASP A 1 30  ? 9.789  27.893  -19.445 1.00 33.81  ? 29  ASP A CG  1 
ATOM   224  O OD1 . ASP A 1 30  ? 10.727 28.017  -20.262 1.00 34.03  ? 29  ASP A OD1 1 
ATOM   225  O OD2 . ASP A 1 30  ? 8.591  28.025  -19.766 1.00 33.78  ? 29  ASP A OD2 1 
ATOM   226  N N   . ASP A 1 31  ? 11.050 26.942  -15.375 1.00 30.23  ? 30  ASP A N   1 
ATOM   227  C CA  . ASP A 1 31  ? 11.406 26.740  -13.980 1.00 36.57  ? 30  ASP A CA  1 
ATOM   228  C C   . ASP A 1 31  ? 10.510 25.710  -13.316 1.00 34.17  ? 30  ASP A C   1 
ATOM   229  O O   . ASP A 1 31  ? 10.375 25.704  -12.086 1.00 39.11  ? 30  ASP A O   1 
ATOM   230  C CB  . ASP A 1 31  ? 11.372 28.074  -13.226 1.00 33.08  ? 30  ASP A CB  1 
ATOM   231  C CG  . ASP A 1 31  ? 12.306 29.110  -13.840 1.00 35.71  ? 30  ASP A CG  1 
ATOM   232  O OD1 . ASP A 1 31  ? 13.492 28.782  -14.065 1.00 39.15  ? 30  ASP A OD1 1 
ATOM   233  O OD2 . ASP A 1 31  ? 11.869 30.252  -14.100 1.00 36.01  ? 30  ASP A OD2 1 
ATOM   234  N N   . THR A 1 32  ? 9.900  24.838  -14.114 1.00 31.11  ? 31  THR A N   1 
ATOM   235  C CA  . THR A 1 32  ? 9.038  23.771  -13.639 1.00 30.51  ? 31  THR A CA  1 
ATOM   236  C C   . THR A 1 32  ? 9.721  22.439  -13.898 1.00 31.94  ? 31  THR A C   1 
ATOM   237  O O   . THR A 1 32  ? 10.112 22.150  -15.037 1.00 31.87  ? 31  THR A O   1 
ATOM   238  C CB  . THR A 1 32  ? 7.681  23.800  -14.353 1.00 36.79  ? 31  THR A CB  1 
ATOM   239  O OG1 . THR A 1 32  ? 7.122  25.118  -14.277 1.00 33.30  ? 31  THR A OG1 1 
ATOM   240  C CG2 . THR A 1 32  ? 6.722  22.775  -13.742 1.00 29.03  ? 31  THR A CG2 1 
ATOM   241  N N   . GLN A 1 33  ? 9.864  21.638  -12.847 1.00 29.48  ? 32  GLN A N   1 
ATOM   242  C CA  . GLN A 1 33  ? 10.403 20.296  -12.989 1.00 29.73  ? 32  GLN A CA  1 
ATOM   243  C C   . GLN A 1 33  ? 9.314  19.361  -13.480 1.00 31.20  ? 32  GLN A C   1 
ATOM   244  O O   . GLN A 1 33  ? 8.155  19.469  -13.062 1.00 30.83  ? 32  GLN A O   1 
ATOM   245  C CB  . GLN A 1 33  ? 10.949 19.783  -11.659 1.00 30.31  ? 32  GLN A CB  1 
ATOM   246  C CG  . GLN A 1 33  ? 11.811 18.559  -11.830 1.00 29.91  ? 32  GLN A CG  1 
ATOM   247  C CD  . GLN A 1 33  ? 12.090 17.858  -10.532 1.00 33.81  ? 32  GLN A CD  1 
ATOM   248  O OE1 . GLN A 1 33  ? 12.031 18.468  -9.454  1.00 32.57  ? 32  GLN A OE1 1 
ATOM   249  N NE2 . GLN A 1 33  ? 12.399 16.561  -10.615 1.00 27.80  ? 32  GLN A NE2 1 
ATOM   250  N N   . PHE A 1 34  ? 9.682  18.438  -14.370 1.00 27.22  ? 33  PHE A N   1 
ATOM   251  C CA  . PHE A 1 34  ? 8.700  17.477  -14.859 1.00 30.00  ? 33  PHE A CA  1 
ATOM   252  C C   . PHE A 1 34  ? 9.116  16.009  -14.796 1.00 27.96  ? 33  PHE A C   1 
ATOM   253  O O   . PHE A 1 34  ? 8.221  15.160  -14.772 1.00 30.08  ? 33  PHE A O   1 
ATOM   254  C CB  . PHE A 1 34  ? 8.265  17.829  -16.291 1.00 27.49  ? 33  PHE A CB  1 
ATOM   255  C CG  . PHE A 1 34  ? 9.304  17.588  -17.351 1.00 25.90  ? 33  PHE A CG  1 
ATOM   256  C CD1 . PHE A 1 34  ? 10.276 18.536  -17.619 1.00 22.44  ? 33  PHE A CD1 1 
ATOM   257  C CD2 . PHE A 1 34  ? 9.250  16.435  -18.141 1.00 26.95  ? 33  PHE A CD2 1 
ATOM   258  C CE1 . PHE A 1 34  ? 11.217 18.325  -18.624 1.00 27.28  ? 33  PHE A CE1 1 
ATOM   259  C CE2 . PHE A 1 34  ? 10.178 16.212  -19.163 1.00 26.90  ? 33  PHE A CE2 1 
ATOM   260  C CZ  . PHE A 1 34  ? 11.169 17.161  -19.406 1.00 27.97  ? 33  PHE A CZ  1 
ATOM   261  N N   . VAL A 1 35  ? 10.411 15.667  -14.732 1.00 25.44  ? 34  VAL A N   1 
ATOM   262  C CA  . VAL A 1 35  ? 10.819 14.278  -14.532 1.00 27.57  ? 34  VAL A CA  1 
ATOM   263  C C   . VAL A 1 35  ? 12.003 14.188  -13.574 1.00 24.69  ? 34  VAL A C   1 
ATOM   264  O O   . VAL A 1 35  ? 12.712 15.162  -13.314 1.00 22.62  ? 34  VAL A O   1 
ATOM   265  C CB  . VAL A 1 35  ? 11.181 13.536  -15.848 1.00 25.40  ? 34  VAL A CB  1 
ATOM   266  C CG1 . VAL A 1 35  ? 9.919  13.161  -16.631 1.00 25.87  ? 34  VAL A CG1 1 
ATOM   267  C CG2 . VAL A 1 35  ? 12.136 14.353  -16.686 1.00 24.50  ? 34  VAL A CG2 1 
ATOM   268  N N   . ARG A 1 36  ? 12.218 12.977  -13.069 1.00 24.11  ? 35  ARG A N   1 
ATOM   269  C CA  . ARG A 1 36  ? 13.322 12.683  -12.173 1.00 29.56  ? 35  ARG A CA  1 
ATOM   270  C C   . ARG A 1 36  ? 13.696 11.214  -12.309 1.00 30.19  ? 35  ARG A C   1 
ATOM   271  O O   . ARG A 1 36  ? 12.851 10.362  -12.604 1.00 26.48  ? 35  ARG A O   1 
ATOM   272  C CB  . ARG A 1 36  ? 12.959 12.979  -10.707 1.00 29.19  ? 35  ARG A CB  1 
ATOM   273  C CG  . ARG A 1 36  ? 11.968 11.981  -10.119 1.00 27.53  ? 35  ARG A CG  1 
ATOM   274  C CD  . ARG A 1 36  ? 12.399 11.510  -8.744  1.00 33.86  ? 35  ARG A CD  1 
ATOM   275  N NE  . ARG A 1 36  ? 11.409 10.630  -8.119  1.00 41.01  ? 35  ARG A NE  1 
ATOM   276  C CZ  . ARG A 1 36  ? 10.738 10.917  -7.003  1.00 42.70  ? 35  ARG A CZ  1 
ATOM   277  N NH1 . ARG A 1 36  ? 10.948 12.066  -6.369  1.00 41.49  ? 35  ARG A NH1 1 
ATOM   278  N NH2 . ARG A 1 36  ? 9.861  10.048  -6.509  1.00 42.21  ? 35  ARG A NH2 1 
ATOM   279  N N   . PHE A 1 37  ? 14.967 10.928  -12.066 1.00 28.12  ? 36  PHE A N   1 
ATOM   280  C CA  . PHE A 1 37  ? 15.452 9.560   -11.957 1.00 28.71  ? 36  PHE A CA  1 
ATOM   281  C C   . PHE A 1 37  ? 16.428 9.492   -10.788 1.00 26.20  ? 36  PHE A C   1 
ATOM   282  O O   . PHE A 1 37  ? 17.242 10.400  -10.608 1.00 24.96  ? 36  PHE A O   1 
ATOM   283  C CB  . PHE A 1 37  ? 16.137 9.110   -13.263 1.00 24.37  ? 36  PHE A CB  1 
ATOM   284  C CG  . PHE A 1 37  ? 16.698 7.723   -13.205 1.00 26.30  ? 36  PHE A CG  1 
ATOM   285  C CD1 . PHE A 1 37  ? 17.996 7.497   -12.732 1.00 28.39  ? 36  PHE A CD1 1 
ATOM   286  C CD2 . PHE A 1 37  ? 15.934 6.635   -13.616 1.00 26.51  ? 36  PHE A CD2 1 
ATOM   287  C CE1 . PHE A 1 37  ? 18.522 6.209   -12.669 1.00 27.27  ? 36  PHE A CE1 1 
ATOM   288  C CE2 . PHE A 1 37  ? 16.458 5.336   -13.563 1.00 29.28  ? 36  PHE A CE2 1 
ATOM   289  C CZ  . PHE A 1 37  ? 17.754 5.125   -13.087 1.00 27.60  ? 36  PHE A CZ  1 
ATOM   290  N N   . ASP A 1 38  ? 16.380 8.401   -10.020 1.00 30.61  ? 37  ASP A N   1 
ATOM   291  C CA  . ASP A 1 38  ? 17.327 8.210   -8.919  1.00 29.94  ? 37  ASP A CA  1 
ATOM   292  C C   . ASP A 1 38  ? 17.659 6.726   -8.800  1.00 33.79  ? 37  ASP A C   1 
ATOM   293  O O   . ASP A 1 38  ? 16.788 5.918   -8.456  1.00 33.91  ? 37  ASP A O   1 
ATOM   294  C CB  . ASP A 1 38  ? 16.755 8.760   -7.613  1.00 31.41  ? 37  ASP A CB  1 
ATOM   295  C CG  . ASP A 1 38  ? 17.741 8.664   -6.436  1.00 36.96  ? 37  ASP A CG  1 
ATOM   296  O OD1 . ASP A 1 38  ? 18.913 8.261   -6.628  1.00 30.81  ? 37  ASP A OD1 1 
ATOM   297  O OD2 . ASP A 1 38  ? 17.321 8.995   -5.307  1.00 38.63  ? 37  ASP A OD2 1 
ATOM   298  N N   . SER A 1 39  ? 18.924 6.373   -9.069  1.00 30.54  ? 38  SER A N   1 
ATOM   299  C CA  . SER A 1 39  ? 19.346 4.977   -9.008  1.00 32.38  ? 38  SER A CA  1 
ATOM   300  C C   . SER A 1 39  ? 19.258 4.385   -7.602  1.00 37.17  ? 38  SER A C   1 
ATOM   301  O O   . SER A 1 39  ? 19.332 3.162   -7.455  1.00 37.55  ? 38  SER A O   1 
ATOM   302  C CB  . SER A 1 39  ? 20.774 4.847   -9.519  1.00 28.44  ? 38  SER A CB  1 
ATOM   303  O OG  . SER A 1 39  ? 21.656 5.542   -8.660  1.00 30.53  ? 38  SER A OG  1 
ATOM   304  N N   . ASP A 1 40  ? 19.131 5.214   -6.567  1.00 34.30  ? 39  ASP A N   1 
ATOM   305  C CA  . ASP A 1 40  ? 18.900 4.720   -5.216  1.00 38.97  ? 39  ASP A CA  1 
ATOM   306  C C   . ASP A 1 40  ? 17.429 4.478   -4.917  1.00 40.98  ? 39  ASP A C   1 
ATOM   307  O O   . ASP A 1 40  ? 17.118 3.820   -3.921  1.00 42.29  ? 39  ASP A O   1 
ATOM   308  C CB  . ASP A 1 40  ? 19.444 5.702   -4.170  1.00 39.71  ? 39  ASP A CB  1 
ATOM   309  C CG  . ASP A 1 40  ? 20.912 5.488   -3.875  1.00 41.29  ? 39  ASP A CG  1 
ATOM   310  O OD1 . ASP A 1 40  ? 21.535 4.625   -4.535  1.00 41.46  ? 39  ASP A OD1 1 
ATOM   311  O OD2 . ASP A 1 40  ? 21.440 6.191   -2.988  1.00 43.96  ? 39  ASP A OD2 1 
ATOM   312  N N   . ALA A 1 41  ? 16.523 5.009   -5.733  1.00 40.31  ? 40  ALA A N   1 
ATOM   313  C CA  . ALA A 1 41  ? 15.104 4.797   -5.500  1.00 43.02  ? 40  ALA A CA  1 
ATOM   314  C C   . ALA A 1 41  ? 14.711 3.378   -5.898  1.00 39.91  ? 40  ALA A C   1 
ATOM   315  O O   . ALA A 1 41  ? 15.457 2.661   -6.567  1.00 43.31  ? 40  ALA A O   1 
ATOM   316  C CB  . ALA A 1 41  ? 14.268 5.821   -6.268  1.00 44.86  ? 40  ALA A CB  1 
ATOM   317  N N   . ALA A 1 42  ? 13.521 2.971   -5.469  1.00 43.87  ? 41  ALA A N   1 
ATOM   318  C CA  . ALA A 1 42  ? 13.145 1.569   -5.616  1.00 47.13  ? 41  ALA A CA  1 
ATOM   319  C C   . ALA A 1 42  ? 12.716 1.224   -7.039  1.00 41.82  ? 41  ALA A C   1 
ATOM   320  O O   . ALA A 1 42  ? 12.930 0.091   -7.487  1.00 45.86  ? 41  ALA A O   1 
ATOM   321  C CB  . ALA A 1 42  ? 12.031 1.222   -4.624  1.00 43.41  ? 41  ALA A CB  1 
ATOM   322  N N   . SER A 1 43  ? 12.144 2.182   -7.771  1.00 45.21  ? 42  SER A N   1 
ATOM   323  C CA  . SER A 1 43  ? 11.538 1.863   -9.062  1.00 42.03  ? 42  SER A CA  1 
ATOM   324  C C   . SER A 1 43  ? 12.574 1.586   -10.146 1.00 40.19  ? 42  SER A C   1 
ATOM   325  O O   . SER A 1 43  ? 12.311 0.780   -11.048 1.00 42.56  ? 42  SER A O   1 
ATOM   326  C CB  . SER A 1 43  ? 10.611 2.996   -9.504  1.00 39.79  ? 42  SER A CB  1 
ATOM   327  O OG  . SER A 1 43  ? 11.355 4.099   -9.994  1.00 42.30  ? 42  SER A OG  1 
ATOM   328  N N   . GLN A 1 44  ? 13.741 2.235   -10.088 1.00 38.98  ? 43  GLN A N   1 
ATOM   329  C CA  . GLN A 1 44  ? 14.732 2.186   -11.171 1.00 37.14  ? 43  GLN A CA  1 
ATOM   330  C C   . GLN A 1 44  ? 14.157 2.752   -12.472 1.00 35.50  ? 43  GLN A C   1 
ATOM   331  O O   . GLN A 1 44  ? 14.593 2.400   -13.569 1.00 33.14  ? 43  GLN A O   1 
ATOM   332  C CB  . GLN A 1 44  ? 15.266 0.762   -11.393 1.00 38.83  ? 43  GLN A CB  1 
ATOM   333  C CG  . GLN A 1 44  ? 16.030 0.157   -10.202 1.00 43.88  ? 43  GLN A CG  1 
ATOM   334  C CD  . GLN A 1 44  ? 17.231 0.989   -9.784  1.00 43.09  ? 43  GLN A CD  1 
ATOM   335  O OE1 . GLN A 1 44  ? 18.282 0.956   -10.429 1.00 41.91  ? 43  GLN A OE1 1 
ATOM   336  N NE2 . GLN A 1 44  ? 17.081 1.740   -8.694  1.00 39.82  ? 43  GLN A NE2 1 
ATOM   337  N N   . LYS A 1 45  ? 13.235 3.669   -12.322 1.00 31.52  ? 44  LYS A N   1 
ATOM   338  C CA  . LYS A 1 45  ? 12.611 4.156   -13.542 1.00 34.41  ? 44  LYS A CA  1 
ATOM   339  C C   . LYS A 1 45  ? 12.537 5.663   -13.546 1.00 31.70  ? 44  LYS A C   1 
ATOM   340  O O   . LYS A 1 45  ? 12.522 6.253   -12.509 1.00 30.57  ? 44  LYS A O   1 
ATOM   341  C CB  . LYS A 1 45  ? 11.204 3.572   -13.629 1.00 37.37  ? 44  LYS A CB  1 
ATOM   342  C CG  . LYS A 1 45  ? 11.127 2.345   -14.513 1.00 40.01  ? 44  LYS A CG  1 
ATOM   343  C CD  . LYS A 1 45  ? 10.084 1.344   -14.150 1.00 45.88  ? 44  LYS A CD  1 
ATOM   344  C CE  . LYS A 1 45  ? 10.338 -0.009  -14.784 1.00 49.34  ? 44  LYS A CE  1 
ATOM   345  N NZ  . LYS A 1 45  ? 11.728 -0.203  -15.260 1.00 53.44  ? 44  LYS A NZ  1 
ATOM   346  N N   . MET A 1 46  ? 12.569 6.216   -14.742 1.00 29.13  ? 45  MET A N   1 
ATOM   347  C CA  . MET A 1 46  ? 12.202 7.616   -14.923 1.00 26.96  ? 45  MET A CA  1 
ATOM   348  C C   . MET A 1 46  ? 10.761 7.787   -14.462 1.00 31.10  ? 45  MET A C   1 
ATOM   349  O O   . MET A 1 46  ? 9.897  6.964   -14.791 1.00 33.01  ? 45  MET A O   1 
ATOM   350  C CB  . MET A 1 46  ? 12.354 8.038   -16.388 1.00 24.25  ? 45  MET A CB  1 
ATOM   351  C CG  . MET A 1 46  ? 12.198 9.543   -16.619 1.00 29.72  ? 45  MET A CG  1 
ATOM   352  S SD  . MET A 1 46  ? 13.606 10.519  -15.987 1.00 36.55  ? 45  MET A SD  1 
ATOM   353  C CE  . MET A 1 46  ? 14.442 10.887  -17.517 1.00 23.53  ? 45  MET A CE  1 
ATOM   354  N N   . GLU A 1 47  ? 10.513 8.830   -13.669 1.00 27.75  ? 46  GLU A N   1 
ATOM   355  C CA  . GLU A 1 47  ? 9.256  9.043   -12.965 1.00 30.47  ? 46  GLU A CA  1 
ATOM   356  C C   . GLU A 1 47  ? 8.709  10.438  -13.239 1.00 28.83  ? 46  GLU A C   1 
ATOM   357  O O   . GLU A 1 47  ? 9.470  11.409  -13.340 1.00 26.17  ? 46  GLU A O   1 
ATOM   358  C CB  . GLU A 1 47  ? 9.407  8.886   -11.441 1.00 28.07  ? 46  GLU A CB  1 
ATOM   359  C CG  . GLU A 1 47  ? 9.899  7.556   -10.889 1.00 30.52  ? 46  GLU A CG  1 
ATOM   360  C CD  . GLU A 1 47  ? 10.277 7.682   -9.403  1.00 39.53  ? 46  GLU A CD  1 
ATOM   361  O OE1 . GLU A 1 47  ? 9.364  7.826   -8.571  1.00 44.02  ? 46  GLU A OE1 1 
ATOM   362  O OE2 . GLU A 1 47  ? 11.484 7.683   -9.060  1.00 47.49  ? 46  GLU A OE2 1 
ATOM   363  N N   . PRO A 1 48  ? 7.384  10.567  -13.326 1.00 28.77  ? 47  PRO A N   1 
ATOM   364  C CA  . PRO A 1 48  ? 6.777  11.883  -13.570 1.00 30.71  ? 47  PRO A CA  1 
ATOM   365  C C   . PRO A 1 48  ? 6.865  12.783  -12.343 1.00 30.44  ? 47  PRO A C   1 
ATOM   366  O O   . PRO A 1 48  ? 6.718  12.325  -11.210 1.00 30.10  ? 47  PRO A O   1 
ATOM   367  C CB  . PRO A 1 48  ? 5.318  11.535  -13.891 1.00 31.07  ? 47  PRO A CB  1 
ATOM   368  C CG  . PRO A 1 48  ? 5.080  10.258  -13.125 1.00 28.72  ? 47  PRO A CG  1 
ATOM   369  C CD  . PRO A 1 48  ? 6.373  9.493   -13.225 1.00 25.37  ? 47  PRO A CD  1 
ATOM   370  N N   . ARG A 1 49  ? 7.082  14.085  -12.577 1.00 30.54  ? 48  ARG A N   1 
ATOM   371  C CA  . ARG A 1 49  ? 7.037  15.062  -11.490 1.00 36.32  ? 48  ARG A CA  1 
ATOM   372  C C   . ARG A 1 49  ? 6.205  16.301  -11.817 1.00 36.37  ? 48  ARG A C   1 
ATOM   373  O O   . ARG A 1 49  ? 6.289  17.291  -11.084 1.00 31.04  ? 48  ARG A O   1 
ATOM   374  C CB  . ARG A 1 49  ? 8.457  15.504  -11.070 1.00 32.74  ? 48  ARG A CB  1 
ATOM   375  C CG  . ARG A 1 49  ? 9.320  14.382  -10.481 1.00 29.47  ? 48  ARG A CG  1 
ATOM   376  C CD  . ARG A 1 49  ? 8.811  13.921  -9.121  1.00 35.91  ? 48  ARG A CD  1 
ATOM   377  N NE  . ARG A 1 49  ? 9.374  14.750  -8.054  1.00 36.88  ? 48  ARG A NE  1 
ATOM   378  C CZ  . ARG A 1 49  ? 8.986  14.722  -6.781  1.00 42.39  ? 48  ARG A CZ  1 
ATOM   379  N NH1 . ARG A 1 49  ? 8.023  13.892  -6.375  1.00 41.74  ? 48  ARG A NH1 1 
ATOM   380  N NH2 . ARG A 1 49  ? 9.568  15.535  -5.910  1.00 41.01  ? 48  ARG A NH2 1 
ATOM   381  N N   . ALA A 1 50  ? 5.434  16.293  -12.902 1.00 37.27  ? 49  ALA A N   1 
ATOM   382  C CA  . ALA A 1 50  ? 4.472  17.349  -13.196 1.00 38.82  ? 49  ALA A CA  1 
ATOM   383  C C   . ALA A 1 50  ? 3.212  16.712  -13.769 1.00 44.02  ? 49  ALA A C   1 
ATOM   384  O O   . ALA A 1 50  ? 3.291  15.667  -14.429 1.00 42.49  ? 49  ALA A O   1 
ATOM   385  C CB  . ALA A 1 50  ? 5.025  18.388  -14.183 1.00 33.91  ? 49  ALA A CB  1 
ATOM   386  N N   . PRO A 1 51  ? 2.036  17.309  -13.530 1.00 44.65  ? 50  PRO A N   1 
ATOM   387  C CA  . PRO A 1 51  ? 0.791  16.630  -13.929 1.00 43.24  ? 50  PRO A CA  1 
ATOM   388  C C   . PRO A 1 51  ? 0.629  16.471  -15.433 1.00 40.67  ? 50  PRO A C   1 
ATOM   389  O O   . PRO A 1 51  ? 0.051  15.471  -15.866 1.00 37.86  ? 50  PRO A O   1 
ATOM   390  C CB  . PRO A 1 51  ? -0.309 17.525  -13.332 1.00 41.36  ? 50  PRO A CB  1 
ATOM   391  C CG  . PRO A 1 51  ? 0.329  18.875  -13.224 1.00 44.10  ? 50  PRO A CG  1 
ATOM   392  C CD  . PRO A 1 51  ? 1.768  18.601  -12.865 1.00 44.08  ? 50  PRO A CD  1 
ATOM   393  N N   . TRP A 1 52  ? 1.120  17.415  -16.238 1.00 38.59  ? 51  TRP A N   1 
ATOM   394  C CA  . TRP A 1 52  ? 0.963  17.354  -17.684 1.00 39.15  ? 51  TRP A CA  1 
ATOM   395  C C   . TRP A 1 52  ? 1.874  16.331  -18.362 1.00 41.66  ? 51  TRP A C   1 
ATOM   396  O O   . TRP A 1 52  ? 1.701  16.079  -19.561 1.00 36.55  ? 51  TRP A O   1 
ATOM   397  C CB  . TRP A 1 52  ? 1.209  18.730  -18.301 1.00 37.30  ? 51  TRP A CB  1 
ATOM   398  C CG  . TRP A 1 52  ? 2.407  19.498  -17.768 1.00 43.40  ? 51  TRP A CG  1 
ATOM   399  C CD1 . TRP A 1 52  ? 2.399  20.476  -16.801 1.00 43.60  ? 51  TRP A CD1 1 
ATOM   400  C CD2 . TRP A 1 52  ? 3.773  19.387  -18.206 1.00 40.89  ? 51  TRP A CD2 1 
ATOM   401  N NE1 . TRP A 1 52  ? 3.673  20.963  -16.607 1.00 43.02  ? 51  TRP A NE1 1 
ATOM   402  C CE2 . TRP A 1 52  ? 4.533  20.314  -17.453 1.00 39.43  ? 51  TRP A CE2 1 
ATOM   403  C CE3 . TRP A 1 52  ? 4.425  18.592  -19.155 1.00 35.45  ? 51  TRP A CE3 1 
ATOM   404  C CZ2 . TRP A 1 52  ? 5.908  20.465  -17.621 1.00 36.49  ? 51  TRP A CZ2 1 
ATOM   405  C CZ3 . TRP A 1 52  ? 5.791  18.742  -19.319 1.00 35.77  ? 51  TRP A CZ3 1 
ATOM   406  C CH2 . TRP A 1 52  ? 6.518  19.673  -18.559 1.00 35.48  ? 51  TRP A CH2 1 
ATOM   407  N N   . ILE A 1 53  ? 2.843  15.750  -17.644 1.00 37.42  ? 52  ILE A N   1 
ATOM   408  C CA  . ILE A 1 53  ? 3.670  14.687  -18.217 1.00 35.34  ? 52  ILE A CA  1 
ATOM   409  C C   . ILE A 1 53  ? 3.108  13.312  -17.899 1.00 35.22  ? 52  ILE A C   1 
ATOM   410  O O   . ILE A 1 53  ? 3.546  12.321  -18.502 1.00 35.80  ? 52  ILE A O   1 
ATOM   411  C CB  . ILE A 1 53  ? 5.136  14.781  -17.734 1.00 33.95  ? 52  ILE A CB  1 
ATOM   412  C CG1 . ILE A 1 53  ? 6.081  14.066  -18.704 1.00 31.20  ? 52  ILE A CG1 1 
ATOM   413  C CG2 . ILE A 1 53  ? 5.295  14.162  -16.348 1.00 33.27  ? 52  ILE A CG2 1 
ATOM   414  C CD1 . ILE A 1 53  ? 6.335  14.826  -19.979 1.00 30.90  ? 52  ILE A CD1 1 
ATOM   415  N N   . GLU A 1 54  ? 2.144  13.216  -16.980 1.00 35.68  ? 53  GLU A N   1 
ATOM   416  C CA  . GLU A 1 54  ? 1.555  11.926  -16.637 1.00 38.12  ? 53  GLU A CA  1 
ATOM   417  C C   . GLU A 1 54  ? 0.725  11.340  -17.775 1.00 39.43  ? 53  GLU A C   1 
ATOM   418  O O   . GLU A 1 54  ? 0.445  10.140  -17.742 1.00 38.03  ? 53  GLU A O   1 
ATOM   419  C CB  . GLU A 1 54  ? 0.687  12.042  -15.381 1.00 38.47  ? 53  GLU A CB  1 
ATOM   420  C CG  . GLU A 1 54  ? 1.445  11.845  -14.071 1.00 41.70  ? 53  GLU A CG  1 
ATOM   421  C CD  . GLU A 1 54  ? 0.819  12.617  -12.916 1.00 46.81  ? 53  GLU A CD  1 
ATOM   422  O OE1 . GLU A 1 54  ? 1.402  12.626  -11.811 1.00 53.46  ? 53  GLU A OE1 1 
ATOM   423  O OE2 . GLU A 1 54  ? -0.261 13.211  -13.111 1.00 51.33  ? 53  GLU A OE2 1 
ATOM   424  N N   . GLN A 1 55  ? 0.322  12.153  -18.768 1.00 37.91  ? 54  GLN A N   1 
ATOM   425  C CA  . GLN A 1 55  ? -0.359 11.606  -19.943 1.00 42.17  ? 54  GLN A CA  1 
ATOM   426  C C   . GLN A 1 55  ? 0.541  10.660  -20.717 1.00 43.42  ? 54  GLN A C   1 
ATOM   427  O O   . GLN A 1 55  ? 0.046  9.779   -21.429 1.00 44.01  ? 54  GLN A O   1 
ATOM   428  C CB  . GLN A 1 55  ? -0.810 12.692  -20.930 1.00 40.39  ? 54  GLN A CB  1 
ATOM   429  C CG  . GLN A 1 55  ? -1.070 14.062  -20.402 1.00 45.39  ? 54  GLN A CG  1 
ATOM   430  C CD  . GLN A 1 55  ? -1.181 15.089  -21.512 1.00 48.61  ? 54  GLN A CD  1 
ATOM   431  O OE1 . GLN A 1 55  ? -1.195 14.748  -22.705 1.00 52.82  ? 54  GLN A OE1 1 
ATOM   432  N NE2 . GLN A 1 55  ? -1.254 16.358  -21.130 1.00 45.12  ? 54  GLN A NE2 1 
ATOM   433  N N   . GLU A 1 56  ? 1.852  10.873  -20.652 1.00 41.59  ? 55  GLU A N   1 
ATOM   434  C CA  . GLU A 1 56  ? 2.758  10.075  -21.459 1.00 36.67  ? 55  GLU A CA  1 
ATOM   435  C C   . GLU A 1 56  ? 2.584  8.608   -21.104 1.00 29.07  ? 55  GLU A C   1 
ATOM   436  O O   . GLU A 1 56  ? 2.411  8.253   -19.939 1.00 37.48  ? 55  GLU A O   1 
ATOM   437  C CB  . GLU A 1 56  ? 4.202  10.533  -21.251 1.00 35.22  ? 55  GLU A CB  1 
ATOM   438  C CG  . GLU A 1 56  ? 4.423  12.031  -21.477 1.00 31.68  ? 55  GLU A CG  1 
ATOM   439  C CD  . GLU A 1 56  ? 4.411  12.427  -22.947 1.00 35.43  ? 55  GLU A CD  1 
ATOM   440  O OE1 . GLU A 1 56  ? 4.418  13.647  -23.251 1.00 32.65  ? 55  GLU A OE1 1 
ATOM   441  O OE2 . GLU A 1 56  ? 4.402  11.520  -23.805 1.00 35.74  ? 55  GLU A OE2 1 
ATOM   442  N N   . GLY A 1 57  ? 2.593  7.759   -22.122 1.00 33.86  ? 56  GLY A N   1 
ATOM   443  C CA  . GLY A 1 57  ? 2.279  6.362   -21.942 1.00 34.43  ? 56  GLY A CA  1 
ATOM   444  C C   . GLY A 1 57  ? 3.462  5.504   -21.542 1.00 32.91  ? 56  GLY A C   1 
ATOM   445  O O   . GLY A 1 57  ? 4.604  5.970   -21.462 1.00 33.88  ? 56  GLY A O   1 
ATOM   446  N N   . PRO A 1 58  ? 3.203  4.213   -21.308 1.00 30.43  ? 57  PRO A N   1 
ATOM   447  C CA  . PRO A 1 58  ? 4.237  3.345   -20.714 1.00 33.04  ? 57  PRO A CA  1 
ATOM   448  C C   . PRO A 1 58  ? 5.469  3.173   -21.582 1.00 34.84  ? 57  PRO A C   1 
ATOM   449  O O   . PRO A 1 58  ? 6.556  2.888   -21.058 1.00 32.08  ? 57  PRO A O   1 
ATOM   450  C CB  . PRO A 1 58  ? 3.506  2.005   -20.514 1.00 36.50  ? 57  PRO A CB  1 
ATOM   451  C CG  . PRO A 1 58  ? 2.025  2.319   -20.695 1.00 35.48  ? 57  PRO A CG  1 
ATOM   452  C CD  . PRO A 1 58  ? 1.945  3.498   -21.588 1.00 29.96  ? 57  PRO A CD  1 
ATOM   453  N N   . GLU A 1 59  ? 5.336  3.330   -22.896 1.00 31.47  ? 58  GLU A N   1 
ATOM   454  C CA  . GLU A 1 59  ? 6.501  3.213   -23.758 1.00 35.24  ? 58  GLU A CA  1 
ATOM   455  C C   . GLU A 1 59  ? 7.402  4.440   -23.671 1.00 31.56  ? 58  GLU A C   1 
ATOM   456  O O   . GLU A 1 59  ? 8.611  4.329   -23.898 1.00 28.24  ? 58  GLU A O   1 
ATOM   457  C CB  . GLU A 1 59  ? 6.057  2.975   -25.202 1.00 30.93  ? 58  GLU A CB  1 
ATOM   458  C CG  . GLU A 1 59  ? 5.299  1.658   -25.392 1.00 39.05  ? 58  GLU A CG  1 
ATOM   459  C CD  . GLU A 1 59  ? 3.847  1.864   -25.784 1.00 46.76  ? 58  GLU A CD  1 
ATOM   460  O OE1 . GLU A 1 59  ? 3.176  2.756   -25.194 1.00 47.11  ? 58  GLU A OE1 1 
ATOM   461  O OE2 . GLU A 1 59  ? 3.373  1.129   -26.679 1.00 52.21  ? 58  GLU A OE2 1 
ATOM   462  N N   . TYR A 1 60  ? 6.841  5.616   -23.386 1.00 27.02  ? 59  TYR A N   1 
ATOM   463  C CA  . TYR A 1 60  ? 7.689  6.779   -23.149 1.00 29.05  ? 59  TYR A CA  1 
ATOM   464  C C   . TYR A 1 60  ? 8.527  6.581   -21.884 1.00 27.94  ? 59  TYR A C   1 
ATOM   465  O O   . TYR A 1 60  ? 9.739  6.807   -21.896 1.00 26.41  ? 59  TYR A O   1 
ATOM   466  C CB  . TYR A 1 60  ? 6.831  8.043   -23.073 1.00 29.23  ? 59  TYR A CB  1 
ATOM   467  C CG  . TYR A 1 60  ? 7.542  9.302   -22.586 1.00 32.01  ? 59  TYR A CG  1 
ATOM   468  C CD1 . TYR A 1 60  ? 8.199  10.140  -23.478 1.00 28.85  ? 59  TYR A CD1 1 
ATOM   469  C CD2 . TYR A 1 60  ? 7.537  9.660   -21.233 1.00 29.68  ? 59  TYR A CD2 1 
ATOM   470  C CE1 . TYR A 1 60  ? 8.835  11.295  -23.040 1.00 30.79  ? 59  TYR A CE1 1 
ATOM   471  C CE2 . TYR A 1 60  ? 8.170  10.808  -20.787 1.00 25.89  ? 59  TYR A CE2 1 
ATOM   472  C CZ  . TYR A 1 60  ? 8.813  11.619  -21.689 1.00 28.38  ? 59  TYR A CZ  1 
ATOM   473  O OH  . TYR A 1 60  ? 9.445  12.755  -21.248 1.00 25.62  ? 59  TYR A OH  1 
ATOM   474  N N   . TRP A 1 61  ? 7.910  6.107   -20.794 1.00 25.12  ? 60  TRP A N   1 
ATOM   475  C CA  . TRP A 1 61  ? 8.676  5.908   -19.563 1.00 32.22  ? 60  TRP A CA  1 
ATOM   476  C C   . TRP A 1 61  ? 9.715  4.803   -19.732 1.00 32.15  ? 60  TRP A C   1 
ATOM   477  O O   . TRP A 1 61  ? 10.842 4.924   -19.241 1.00 31.89  ? 60  TRP A O   1 
ATOM   478  C CB  . TRP A 1 61  ? 7.732  5.631   -18.383 1.00 28.51  ? 60  TRP A CB  1 
ATOM   479  C CG  . TRP A 1 61  ? 6.780  6.779   -18.205 1.00 34.34  ? 60  TRP A CG  1 
ATOM   480  C CD1 . TRP A 1 61  ? 5.457  6.818   -18.545 1.00 33.40  ? 60  TRP A CD1 1 
ATOM   481  C CD2 . TRP A 1 61  ? 7.106  8.086   -17.715 1.00 34.72  ? 60  TRP A CD2 1 
ATOM   482  N NE1 . TRP A 1 61  ? 4.940  8.065   -18.285 1.00 32.27  ? 60  TRP A NE1 1 
ATOM   483  C CE2 . TRP A 1 61  ? 5.931  8.860   -17.773 1.00 33.62  ? 60  TRP A CE2 1 
ATOM   484  C CE3 . TRP A 1 61  ? 8.281  8.675   -17.229 1.00 34.21  ? 60  TRP A CE3 1 
ATOM   485  C CZ2 . TRP A 1 61  ? 5.891  10.190  -17.353 1.00 32.58  ? 60  TRP A CZ2 1 
ATOM   486  C CZ3 . TRP A 1 61  ? 8.243  10.004  -16.822 1.00 33.03  ? 60  TRP A CZ3 1 
ATOM   487  C CH2 . TRP A 1 61  ? 7.055  10.743  -16.886 1.00 32.90  ? 60  TRP A CH2 1 
ATOM   488  N N   . ASP A 1 62  ? 9.378  3.738   -20.455 1.00 32.98  ? 61  ASP A N   1 
ATOM   489  C CA  . ASP A 1 62  ? 10.365 2.692   -20.699 1.00 29.63  ? 61  ASP A CA  1 
ATOM   490  C C   . ASP A 1 62  ? 11.499 3.199   -21.589 1.00 27.34  ? 61  ASP A C   1 
ATOM   491  O O   . ASP A 1 62  ? 12.670 2.887   -21.358 1.00 29.88  ? 61  ASP A O   1 
ATOM   492  C CB  . ASP A 1 62  ? 9.672  1.470   -21.303 1.00 33.78  ? 61  ASP A CB  1 
ATOM   493  C CG  . ASP A 1 62  ? 10.631 0.331   -21.574 1.00 38.17  ? 61  ASP A CG  1 
ATOM   494  O OD1 . ASP A 1 62  ? 11.112 -0.284  -20.602 1.00 43.91  ? 61  ASP A OD1 1 
ATOM   495  O OD2 . ASP A 1 62  ? 10.924 0.063   -22.758 1.00 40.41  ? 61  ASP A OD2 1 
ATOM   496  N N   . GLN A 1 63  ? 11.185 4.017   -22.588 1.00 29.78  ? 62  GLN A N   1 
ATOM   497  C CA  . GLN A 1 63  ? 12.230 4.560   -23.449 1.00 25.67  ? 62  GLN A CA  1 
ATOM   498  C C   . GLN A 1 63  ? 13.151 5.524   -22.689 1.00 28.19  ? 62  GLN A C   1 
ATOM   499  O O   . GLN A 1 63  ? 14.378 5.490   -22.864 1.00 23.36  ? 62  GLN A O   1 
ATOM   500  C CB  . GLN A 1 63  ? 11.582 5.244   -24.651 1.00 25.94  ? 62  GLN A CB  1 
ATOM   501  C CG  . GLN A 1 63  ? 12.525 6.032   -25.522 1.00 29.14  ? 62  GLN A CG  1 
ATOM   502  C CD  . GLN A 1 63  ? 11.791 6.969   -26.468 1.00 36.88  ? 62  GLN A CD  1 
ATOM   503  O OE1 . GLN A 1 63  ? 11.593 6.648   -27.647 1.00 35.64  ? 62  GLN A OE1 1 
ATOM   504  N NE2 . GLN A 1 63  ? 11.382 8.138   -25.960 1.00 34.34  ? 62  GLN A NE2 1 
ATOM   505  N N   . GLU A 1 64  ? 12.585 6.384   -21.831 1.00 25.49  ? 63  GLU A N   1 
ATOM   506  C CA  . GLU A 1 64  ? 13.414 7.287   -21.040 1.00 24.53  ? 63  GLU A CA  1 
ATOM   507  C C   . GLU A 1 64  ? 14.249 6.516   -20.016 1.00 23.72  ? 63  GLU A C   1 
ATOM   508  O O   . GLU A 1 64  ? 15.409 6.855   -19.770 1.00 24.68  ? 63  GLU A O   1 
ATOM   509  C CB  . GLU A 1 64  ? 12.536 8.343   -20.355 1.00 26.52  ? 63  GLU A CB  1 
ATOM   510  C CG  . GLU A 1 64  ? 11.753 9.196   -21.334 1.00 25.94  ? 63  GLU A CG  1 
ATOM   511  C CD  . GLU A 1 64  ? 12.648 9.929   -22.321 1.00 29.25  ? 63  GLU A CD  1 
ATOM   512  O OE1 . GLU A 1 64  ? 13.171 11.009  -21.946 1.00 25.90  ? 63  GLU A OE1 1 
ATOM   513  O OE2 . GLU A 1 64  ? 12.825 9.438   -23.473 1.00 26.99  ? 63  GLU A OE2 1 
ATOM   514  N N   . THR A 1 65  ? 13.684 5.469   -19.419 1.00 25.05  ? 64  THR A N   1 
ATOM   515  C CA  . THR A 1 65  ? 14.453 4.662   -18.475 1.00 23.52  ? 64  THR A CA  1 
ATOM   516  C C   . THR A 1 65  ? 15.651 3.999   -19.157 1.00 28.86  ? 64  THR A C   1 
ATOM   517  O O   . THR A 1 65  ? 16.759 3.982   -18.600 1.00 27.17  ? 64  THR A O   1 
ATOM   518  C CB  . THR A 1 65  ? 13.546 3.624   -17.824 1.00 26.52  ? 64  THR A CB  1 
ATOM   519  O OG1 . THR A 1 65  ? 12.450 4.294   -17.192 1.00 28.35  ? 64  THR A OG1 1 
ATOM   520  C CG2 . THR A 1 65  ? 14.306 2.830   -16.758 1.00 28.57  ? 64  THR A CG2 1 
ATOM   521  N N   . ARG A 1 66  ? 15.459 3.490   -20.382 1.00 23.73  ? 65  ARG A N   1 
ATOM   522  C CA  . ARG A 1 66  ? 16.568 2.883   -21.115 1.00 25.41  ? 65  ARG A CA  1 
ATOM   523  C C   . ARG A 1 66  ? 17.653 3.907   -21.452 1.00 25.41  ? 65  ARG A C   1 
ATOM   524  O O   . ARG A 1 66  ? 18.851 3.599   -21.376 1.00 25.36  ? 65  ARG A O   1 
ATOM   525  C CB  . ARG A 1 66  ? 16.056 2.206   -22.393 1.00 21.77  ? 65  ARG A CB  1 
ATOM   526  C CG  . ARG A 1 66  ? 15.479 0.809   -22.177 1.00 27.47  ? 65  ARG A CG  1 
ATOM   527  C CD  . ARG A 1 66  ? 14.976 0.195   -23.504 1.00 32.79  ? 65  ARG A CD  1 
ATOM   528  N NE  . ARG A 1 66  ? 13.587 0.563   -23.797 1.00 31.53  ? 65  ARG A NE  1 
ATOM   529  C CZ  . ARG A 1 66  ? 13.183 1.171   -24.914 1.00 27.13  ? 65  ARG A CZ  1 
ATOM   530  N NH1 . ARG A 1 66  ? 14.042 1.485   -25.867 1.00 21.85  ? 65  ARG A NH1 1 
ATOM   531  N NH2 . ARG A 1 66  ? 11.904 1.462   -25.077 1.00 34.42  ? 65  ARG A NH2 1 
ATOM   532  N N   . ASN A 1 67  ? 17.269 5.127   -21.835 1.00 22.69  ? 66  ASN A N   1 
ATOM   533  C CA  . ASN A 1 67  ? 18.313 6.106   -22.102 1.00 22.68  ? 66  ASN A CA  1 
ATOM   534  C C   . ASN A 1 67  ? 19.017 6.535   -20.817 1.00 25.09  ? 66  ASN A C   1 
ATOM   535  O O   . ASN A 1 67  ? 20.222 6.799   -20.845 1.00 26.76  ? 66  ASN A O   1 
ATOM   536  C CB  . ASN A 1 67  ? 17.755 7.298   -22.879 1.00 23.52  ? 66  ASN A CB  1 
ATOM   537  C CG  . ASN A 1 67  ? 17.958 7.137   -24.392 1.00 28.19  ? 66  ASN A CG  1 
ATOM   538  O OD1 . ASN A 1 67  ? 18.984 6.612   -24.830 1.00 31.02  ? 66  ASN A OD1 1 
ATOM   539  N ND2 . ASN A 1 67  ? 16.976 7.552   -25.184 1.00 24.79  ? 66  ASN A ND2 1 
ATOM   540  N N   . MET A 1 68  ? 18.305 6.551   -19.683 1.00 21.77  ? 67  MET A N   1 
ATOM   541  C CA  . MET A 1 68  ? 18.939 6.831   -18.396 1.00 25.66  ? 67  MET A CA  1 
ATOM   542  C C   . MET A 1 68  ? 19.933 5.739   -18.019 1.00 27.99  ? 67  MET A C   1 
ATOM   543  O O   . MET A 1 68  ? 21.028 6.025   -17.513 1.00 26.19  ? 67  MET A O   1 
ATOM   544  C CB  . MET A 1 68  ? 17.878 6.946   -17.294 1.00 23.31  ? 67  MET A CB  1 
ATOM   545  C CG  . MET A 1 68  ? 17.312 8.330   -17.082 1.00 30.10  ? 67  MET A CG  1 
ATOM   546  S SD  . MET A 1 68  ? 18.567 9.629   -16.996 1.00 38.53  ? 67  MET A SD  1 
ATOM   547  C CE  . MET A 1 68  ? 19.630 9.022   -15.680 1.00 20.91  ? 67  MET A CE  1 
ATOM   548  N N   . LYS A 1 69  ? 19.541 4.476   -18.212 1.00 25.40  ? 68  LYS A N   1 
ATOM   549  C CA  . LYS A 1 69  ? 20.420 3.357   -17.905 1.00 23.80  ? 68  LYS A CA  1 
ATOM   550  C C   . LYS A 1 69  ? 21.681 3.404   -18.764 1.00 24.37  ? 68  LYS A C   1 
ATOM   551  O O   . LYS A 1 69  ? 22.788 3.149   -18.277 1.00 26.75  ? 68  LYS A O   1 
ATOM   552  C CB  . LYS A 1 69  ? 19.654 2.035   -18.097 1.00 22.84  ? 68  LYS A CB  1 
ATOM   553  C CG  . LYS A 1 69  ? 20.488 0.761   -17.863 1.00 26.15  ? 68  LYS A CG  1 
ATOM   554  C CD  . LYS A 1 69  ? 19.641 -0.466  -17.475 1.00 25.72  ? 68  LYS A CD  1 
ATOM   555  C CE  . LYS A 1 69  ? 18.558 -0.807  -18.568 1.00 27.92  ? 68  LYS A CE  1 
ATOM   556  N NZ  . LYS A 1 69  ? 19.190 -1.233  -19.865 1.00 26.11  ? 68  LYS A NZ  1 
ATOM   557  N N   . ALA A 1 70  ? 21.542 3.754   -20.038 1.00 24.41  ? 69  ALA A N   1 
ATOM   558  C CA  . ALA A 1 70  ? 22.715 3.828   -20.901 1.00 26.16  ? 69  ALA A CA  1 
ATOM   559  C C   . ALA A 1 70  ? 23.592 5.006   -20.511 1.00 23.86  ? 69  ALA A C   1 
ATOM   560  O O   . ALA A 1 70  ? 24.821 4.885   -20.444 1.00 21.01  ? 69  ALA A O   1 
ATOM   561  C CB  . ALA A 1 70  ? 22.288 3.930   -22.374 1.00 21.22  ? 69  ALA A CB  1 
ATOM   562  N N   . HIS A 1 71  ? 22.974 6.154   -20.239 1.00 25.23  ? 70  HIS A N   1 
ATOM   563  C CA  . HIS A 1 71  ? 23.725 7.291   -19.717 1.00 25.26  ? 70  HIS A CA  1 
ATOM   564  C C   . HIS A 1 71  ? 24.491 6.928   -18.440 1.00 24.87  ? 70  HIS A C   1 
ATOM   565  O O   . HIS A 1 71  ? 25.665 7.293   -18.296 1.00 21.29  ? 70  HIS A O   1 
ATOM   566  C CB  . HIS A 1 71  ? 22.776 8.468   -19.473 1.00 24.51  ? 70  HIS A CB  1 
ATOM   567  C CG  . HIS A 1 71  ? 23.446 9.645   -18.847 1.00 29.75  ? 70  HIS A CG  1 
ATOM   568  N ND1 . HIS A 1 71  ? 23.410 9.883   -17.489 1.00 32.80  ? 70  HIS A ND1 1 
ATOM   569  C CD2 . HIS A 1 71  ? 24.209 10.627  -19.384 1.00 33.33  ? 70  HIS A CD2 1 
ATOM   570  C CE1 . HIS A 1 71  ? 24.104 10.975  -17.220 1.00 35.54  ? 70  HIS A CE1 1 
ATOM   571  N NE2 . HIS A 1 71  ? 24.597 11.447  -18.352 1.00 38.44  ? 70  HIS A NE2 1 
ATOM   572  N N   . SER A 1 72  ? 23.860 6.173   -17.519 1.00 20.45  ? 71  SER A N   1 
ATOM   573  C CA  . SER A 1 72  ? 24.497 5.890   -16.225 1.00 23.16  ? 71  SER A CA  1 
ATOM   574  C C   . SER A 1 72  ? 25.719 4.996   -16.380 1.00 26.37  ? 71  SER A C   1 
ATOM   575  O O   . SER A 1 72  ? 26.686 5.122   -15.620 1.00 23.56  ? 71  SER A O   1 
ATOM   576  C CB  . SER A 1 72  ? 23.508 5.226   -15.259 1.00 21.39  ? 71  SER A CB  1 
ATOM   577  O OG  . SER A 1 72  ? 22.360 6.036   -15.051 1.00 26.18  ? 71  SER A OG  1 
ATOM   578  N N   . GLN A 1 73  ? 25.675 4.053   -17.330 1.00 25.17  ? 72  GLN A N   1 
ATOM   579  C CA  . GLN A 1 73  ? 26.825 3.183   -17.571 1.00 21.35  ? 72  GLN A CA  1 
ATOM   580  C C   . GLN A 1 73  ? 28.007 3.973   -18.115 1.00 22.73  ? 72  GLN A C   1 
ATOM   581  O O   . GLN A 1 73  ? 29.156 3.718   -17.746 1.00 30.24  ? 72  GLN A O   1 
ATOM   582  C CB  . GLN A 1 73  ? 26.443 2.066   -18.547 1.00 29.15  ? 72  GLN A CB  1 
ATOM   583  C CG  . GLN A 1 73  ? 27.575 1.099   -18.825 1.00 25.21  ? 72  GLN A CG  1 
ATOM   584  C CD  . GLN A 1 73  ? 27.896 0.266   -17.613 1.00 30.77  ? 72  GLN A CD  1 
ATOM   585  O OE1 . GLN A 1 73  ? 27.023 -0.011  -16.789 1.00 33.42  ? 72  GLN A OE1 1 
ATOM   586  N NE2 . GLN A 1 73  ? 29.151 -0.142  -17.493 1.00 33.71  ? 72  GLN A NE2 1 
ATOM   587  N N   . THR A 1 74  ? 27.751 4.927   -19.003 1.00 22.71  ? 73  THR A N   1 
ATOM   588  C CA  . THR A 1 74  ? 28.834 5.755   -19.527 1.00 20.56  ? 73  THR A CA  1 
ATOM   589  C C   . THR A 1 74  ? 29.331 6.761   -18.486 1.00 23.96  ? 73  THR A C   1 
ATOM   590  O O   . THR A 1 74  ? 30.511 7.126   -18.495 1.00 22.86  ? 73  THR A O   1 
ATOM   591  C CB  . THR A 1 74  ? 28.357 6.443   -20.815 1.00 23.91  ? 73  THR A CB  1 
ATOM   592  O OG1 . THR A 1 74  ? 28.487 5.518   -21.905 1.00 36.80  ? 73  THR A OG1 1 
ATOM   593  C CG2 . THR A 1 74  ? 29.168 7.696   -21.141 1.00 26.04  ? 73  THR A CG2 1 
ATOM   594  N N   . ASP A 1 75  ? 28.465 7.209   -17.567 1.00 23.40  ? 74  ASP A N   1 
ATOM   595  C CA  . ASP A 1 75  ? 28.974 8.022   -16.477 1.00 23.66  ? 74  ASP A CA  1 
ATOM   596  C C   . ASP A 1 75  ? 29.815 7.164   -15.544 1.00 24.85  ? 74  ASP A C   1 
ATOM   597  O O   . ASP A 1 75  ? 30.863 7.608   -15.064 1.00 21.51  ? 74  ASP A O   1 
ATOM   598  C CB  . ASP A 1 75  ? 27.827 8.703   -15.729 1.00 26.49  ? 74  ASP A CB  1 
ATOM   599  C CG  . ASP A 1 75  ? 27.499 10.084  -16.289 1.00 33.74  ? 74  ASP A CG  1 
ATOM   600  O OD1 . ASP A 1 75  ? 27.978 10.425  -17.394 1.00 28.43  ? 74  ASP A OD1 1 
ATOM   601  O OD2 . ASP A 1 75  ? 26.753 10.839  -15.621 1.00 34.59  ? 74  ASP A OD2 1 
ATOM   602  N N   . ARG A 1 76  ? 29.398 5.922   -15.364 1.00 22.47  ? 75  ARG A N   1 
ATOM   603  C CA  . ARG A 1 76  ? 30.167 4.969   -14.546 1.00 24.02  ? 75  ARG A CA  1 
ATOM   604  C C   . ARG A 1 76  ? 31.583 4.815   -15.132 1.00 24.54  ? 75  ARG A C   1 
ATOM   605  O O   . ARG A 1 76  ? 32.520 4.962   -14.395 1.00 24.48  ? 75  ARG A O   1 
ATOM   606  C CB  . ARG A 1 76  ? 29.378 3.683   -14.325 1.00 26.96  ? 75  ARG A CB  1 
ATOM   607  C CG  . ARG A 1 76  ? 30.188 2.521   -13.789 1.00 26.92  ? 75  ARG A CG  1 
ATOM   608  C CD  . ARG A 1 76  ? 29.395 1.248   -13.904 1.00 35.32  ? 75  ARG A CD  1 
ATOM   609  N NE  . ARG A 1 76  ? 29.410 0.621   -12.617 1.00 39.92  ? 75  ARG A NE  1 
ATOM   610  C CZ  . ARG A 1 76  ? 28.376 0.527   -11.791 1.00 55.76  ? 75  ARG A CZ  1 
ATOM   611  N NH1 . ARG A 1 76  ? 27.185 0.958   -12.162 1.00 53.35  ? 75  ARG A NH1 1 
ATOM   612  N NH2 . ARG A 1 76  ? 28.529 -0.049  -10.612 1.00 49.68  ? 75  ARG A NH2 1 
ATOM   613  N N   . ALA A 1 77  ? 31.703 4.598   -16.438 1.00 24.44  ? 76  ALA A N   1 
ATOM   614  C CA  . ALA A 1 77  ? 33.015 4.481   -17.064 1.00 26.36  ? 76  ALA A CA  1 
ATOM   615  C C   . ALA A 1 77  ? 33.758 5.814   -17.070 1.00 27.41  ? 76  ALA A C   1 
ATOM   616  O O   . ALA A 1 77  ? 34.997 5.837   -17.019 1.00 26.77  ? 76  ALA A O   1 
ATOM   617  C CB  . ALA A 1 77  ? 32.870 3.938   -18.496 1.00 19.41  ? 76  ALA A CB  1 
ATOM   618  N N   . ASN A 1 78  ? 33.029 6.930   -17.151 1.00 24.38  ? 77  ASN A N   1 
ATOM   619  C CA  . ASN A 1 78  ? 33.690 8.229   -17.234 1.00 22.39  ? 77  ASN A CA  1 
ATOM   620  C C   . ASN A 1 78  ? 34.295 8.641   -15.891 1.00 23.59  ? 77  ASN A C   1 
ATOM   621  O O   . ASN A 1 78  ? 35.344 9.294   -15.857 1.00 24.91  ? 77  ASN A O   1 
ATOM   622  C CB  . ASN A 1 78  ? 32.707 9.287   -17.728 1.00 24.47  ? 77  ASN A CB  1 
ATOM   623  C CG  . ASN A 1 78  ? 32.589 9.325   -19.255 1.00 24.28  ? 77  ASN A CG  1 
ATOM   624  O OD1 . ASN A 1 78  ? 33.459 8.848   -19.973 1.00 24.72  ? 77  ASN A OD1 1 
ATOM   625  N ND2 . ASN A 1 78  ? 31.522 9.937   -19.742 1.00 23.85  ? 77  ASN A ND2 1 
ATOM   626  N N   . LEU A 1 79  ? 33.652 8.274   -14.782 1.00 19.43  ? 78  LEU A N   1 
ATOM   627  C CA  . LEU A 1 79  ? 34.271 8.458   -13.472 1.00 23.23  ? 78  LEU A CA  1 
ATOM   628  C C   . LEU A 1 79  ? 35.632 7.769   -13.400 1.00 26.17  ? 78  LEU A C   1 
ATOM   629  O O   . LEU A 1 79  ? 36.603 8.356   -12.912 1.00 25.99  ? 78  LEU A O   1 
ATOM   630  C CB  . LEU A 1 79  ? 33.338 7.929   -12.376 1.00 21.28  ? 78  LEU A CB  1 
ATOM   631  C CG  . LEU A 1 79  ? 32.133 8.831   -12.104 1.00 23.53  ? 78  LEU A CG  1 
ATOM   632  C CD1 . LEU A 1 79  ? 31.063 8.077   -11.341 1.00 25.74  ? 78  LEU A CD1 1 
ATOM   633  C CD2 . LEU A 1 79  ? 32.577 10.081  -11.333 1.00 24.94  ? 78  LEU A CD2 1 
ATOM   634  N N   . GLY A 1 80  ? 35.724 6.524   -13.891 1.00 27.32  ? 79  GLY A N   1 
ATOM   635  C CA  . GLY A 1 80  ? 36.995 5.814   -13.853 1.00 24.30  ? 79  GLY A CA  1 
ATOM   636  C C   . GLY A 1 80  ? 38.037 6.451   -14.751 1.00 28.66  ? 79  GLY A C   1 
ATOM   637  O O   . GLY A 1 80  ? 39.202 6.586   -14.368 1.00 26.93  ? 79  GLY A O   1 
ATOM   638  N N   . THR A 1 81  ? 37.626 6.871   -15.949 1.00 23.44  ? 80  THR A N   1 
ATOM   639  C CA  . THR A 1 81  ? 38.542 7.561   -16.848 1.00 26.34  ? 80  THR A CA  1 
ATOM   640  C C   . THR A 1 81  ? 39.089 8.826   -16.205 1.00 24.49  ? 80  THR A C   1 
ATOM   641  O O   . THR A 1 81  ? 40.292 9.078   -16.246 1.00 26.12  ? 80  THR A O   1 
ATOM   642  C CB  . THR A 1 81  ? 37.836 7.880   -18.169 1.00 26.23  ? 80  THR A CB  1 
ATOM   643  O OG1 . THR A 1 81  ? 37.421 6.652   -18.783 1.00 28.76  ? 80  THR A OG1 1 
ATOM   644  C CG2 . THR A 1 81  ? 38.762 8.607   -19.118 1.00 25.47  ? 80  THR A CG2 1 
ATOM   645  N N   . LEU A 1 82  ? 38.220 9.629   -15.587 1.00 24.45  ? 81  LEU A N   1 
ATOM   646  C CA  . LEU A 1 82  ? 38.686 10.889  -15.016 1.00 26.81  ? 81  LEU A CA  1 
ATOM   647  C C   . LEU A 1 82  ? 39.586 10.656  -13.804 1.00 24.96  ? 81  LEU A C   1 
ATOM   648  O O   . LEU A 1 82  ? 40.538 11.411  -13.577 1.00 26.40  ? 81  LEU A O   1 
ATOM   649  C CB  . LEU A 1 82  ? 37.492 11.778  -14.651 1.00 21.68  ? 81  LEU A CB  1 
ATOM   650  C CG  . LEU A 1 82  ? 36.703 12.304  -15.850 1.00 25.63  ? 81  LEU A CG  1 
ATOM   651  C CD1 . LEU A 1 82  ? 35.687 13.353  -15.451 1.00 24.09  ? 81  LEU A CD1 1 
ATOM   652  C CD2 . LEU A 1 82  ? 37.621 12.849  -16.943 1.00 23.50  ? 81  LEU A CD2 1 
ATOM   653  N N   . ARG A 1 83  ? 39.315 9.617   -13.026 1.00 27.76  ? 82  ARG A N   1 
ATOM   654  C CA  . ARG A 1 83  ? 40.225 9.254   -11.948 1.00 27.76  ? 82  ARG A CA  1 
ATOM   655  C C   . ARG A 1 83  ? 41.637 9.042   -12.486 1.00 31.07  ? 82  ARG A C   1 
ATOM   656  O O   . ARG A 1 83  ? 42.615 9.515   -11.893 1.00 29.63  ? 82  ARG A O   1 
ATOM   657  C CB  . ARG A 1 83  ? 39.699 8.002   -11.241 1.00 28.04  ? 82  ARG A CB  1 
ATOM   658  C CG  . ARG A 1 83  ? 40.608 7.422   -10.177 1.00 37.87  ? 82  ARG A CG  1 
ATOM   659  C CD  . ARG A 1 83  ? 39.928 6.248   -9.482  1.00 41.57  ? 82  ARG A CD  1 
ATOM   660  N NE  . ARG A 1 83  ? 39.882 5.053   -10.328 1.00 44.53  ? 82  ARG A NE  1 
ATOM   661  C CZ  . ARG A 1 83  ? 38.772 4.373   -10.601 1.00 46.30  ? 82  ARG A CZ  1 
ATOM   662  N NH1 . ARG A 1 83  ? 37.605 4.765   -10.096 1.00 44.95  ? 82  ARG A NH1 1 
ATOM   663  N NH2 . ARG A 1 83  ? 38.827 3.301   -11.379 1.00 45.90  ? 82  ARG A NH2 1 
ATOM   664  N N   . GLY A 1 84  ? 41.757 8.364   -13.633 1.00 29.91  ? 83  GLY A N   1 
ATOM   665  C CA  . GLY A 1 84  ? 43.067 8.147   -14.226 1.00 28.61  ? 83  GLY A CA  1 
ATOM   666  C C   . GLY A 1 84  ? 43.684 9.415   -14.790 1.00 28.85  ? 83  GLY A C   1 
ATOM   667  O O   . GLY A 1 84  ? 44.896 9.632   -14.673 1.00 29.64  ? 83  GLY A O   1 
ATOM   668  N N   . TYR A 1 85  ? 42.868 10.268  -15.415 1.00 25.62  ? 84  TYR A N   1 
ATOM   669  C CA  . TYR A 1 85  ? 43.397 11.516  -15.963 1.00 27.39  ? 84  TYR A CA  1 
ATOM   670  C C   . TYR A 1 85  ? 43.989 12.403  -14.865 1.00 29.41  ? 84  TYR A C   1 
ATOM   671  O O   . TYR A 1 85  ? 44.996 13.082  -15.087 1.00 28.14  ? 84  TYR A O   1 
ATOM   672  C CB  . TYR A 1 85  ? 42.301 12.288  -16.703 1.00 28.44  ? 84  TYR A CB  1 
ATOM   673  C CG  . TYR A 1 85  ? 41.834 11.742  -18.036 1.00 30.12  ? 84  TYR A CG  1 
ATOM   674  C CD1 . TYR A 1 85  ? 42.463 10.663  -18.655 1.00 29.76  ? 84  TYR A CD1 1 
ATOM   675  C CD2 . TYR A 1 85  ? 40.743 12.326  -18.679 1.00 31.67  ? 84  TYR A CD2 1 
ATOM   676  C CE1 . TYR A 1 85  ? 42.015 10.192  -19.902 1.00 28.90  ? 84  TYR A CE1 1 
ATOM   677  C CE2 . TYR A 1 85  ? 40.287 11.867  -19.895 1.00 28.26  ? 84  TYR A CE2 1 
ATOM   678  C CZ  . TYR A 1 85  ? 40.923 10.806  -20.506 1.00 29.62  ? 84  TYR A CZ  1 
ATOM   679  O OH  . TYR A 1 85  ? 40.424 10.373  -21.705 1.00 28.43  ? 84  TYR A OH  1 
ATOM   680  N N   . TYR A 1 86  ? 43.366 12.428  -13.683 1.00 27.51  ? 85  TYR A N   1 
ATOM   681  C CA  . TYR A 1 86  ? 43.766 13.329  -12.605 1.00 30.17  ? 85  TYR A CA  1 
ATOM   682  C C   . TYR A 1 86  ? 44.586 12.647  -11.526 1.00 29.56  ? 85  TYR A C   1 
ATOM   683  O O   . TYR A 1 86  ? 44.854 13.267  -10.497 1.00 32.38  ? 85  TYR A O   1 
ATOM   684  C CB  . TYR A 1 86  ? 42.537 13.972  -11.966 1.00 30.77  ? 85  TYR A CB  1 
ATOM   685  C CG  . TYR A 1 86  ? 41.843 14.982  -12.856 1.00 25.46  ? 85  TYR A CG  1 
ATOM   686  C CD1 . TYR A 1 86  ? 42.371 16.249  -13.042 1.00 27.02  ? 85  TYR A CD1 1 
ATOM   687  C CD2 . TYR A 1 86  ? 40.661 14.660  -13.506 1.00 25.71  ? 85  TYR A CD2 1 
ATOM   688  C CE1 . TYR A 1 86  ? 41.741 17.174  -13.849 1.00 31.29  ? 85  TYR A CE1 1 
ATOM   689  C CE2 . TYR A 1 86  ? 40.013 15.581  -14.318 1.00 29.16  ? 85  TYR A CE2 1 
ATOM   690  C CZ  . TYR A 1 86  ? 40.557 16.837  -14.491 1.00 30.53  ? 85  TYR A CZ  1 
ATOM   691  O OH  . TYR A 1 86  ? 39.917 17.756  -15.302 1.00 26.22  ? 85  TYR A OH  1 
ATOM   692  N N   . ASN A 1 87  ? 44.973 11.384  -11.730 1.00 32.43  ? 86  ASN A N   1 
ATOM   693  C CA  . ASN A 1 87  ? 45.801 10.626  -10.788 1.00 26.74  ? 86  ASN A CA  1 
ATOM   694  C C   . ASN A 1 87  ? 45.172 10.596  -9.404  1.00 32.62  ? 86  ASN A C   1 
ATOM   695  O O   . ASN A 1 87  ? 45.832 10.803  -8.386  1.00 33.26  ? 86  ASN A O   1 
ATOM   696  C CB  . ASN A 1 87  ? 47.231 11.171  -10.730 1.00 33.27  ? 86  ASN A CB  1 
ATOM   697  C CG  . ASN A 1 87  ? 47.978 10.992  -12.050 1.00 41.65  ? 86  ASN A CG  1 
ATOM   698  O OD1 . ASN A 1 87  ? 47.657 10.098  -12.844 1.00 41.50  ? 86  ASN A OD1 1 
ATOM   699  N ND2 . ASN A 1 87  ? 48.974 11.838  -12.290 1.00 42.07  ? 86  ASN A ND2 1 
ATOM   700  N N   . GLN A 1 88  ? 43.876 10.329  -9.377  1.00 33.99  ? 87  GLN A N   1 
ATOM   701  C CA  . GLN A 1 88  ? 43.127 10.257  -8.137  1.00 33.62  ? 87  GLN A CA  1 
ATOM   702  C C   . GLN A 1 88  ? 43.050 8.796   -7.691  1.00 38.21  ? 87  GLN A C   1 
ATOM   703  O O   . GLN A 1 88  ? 43.711 7.913   -8.242  1.00 38.93  ? 87  GLN A O   1 
ATOM   704  C CB  . GLN A 1 88  ? 41.755 10.918  -8.319  1.00 30.37  ? 87  GLN A CB  1 
ATOM   705  C CG  . GLN A 1 88  ? 41.853 12.447  -8.375  1.00 33.67  ? 87  GLN A CG  1 
ATOM   706  C CD  . GLN A 1 88  ? 40.654 13.140  -9.020  1.00 30.95  ? 87  GLN A CD  1 
ATOM   707  O OE1 . GLN A 1 88  ? 39.874 12.528  -9.761  1.00 28.84  ? 87  GLN A OE1 1 
ATOM   708  N NE2 . GLN A 1 88  ? 40.509 14.435  -8.742  1.00 25.47  ? 87  GLN A NE2 1 
ATOM   709  N N   . SER A 1 89  ? 42.242 8.528   -6.679  1.00 37.27  ? 88  SER A N   1 
ATOM   710  C CA  . SER A 1 89  ? 42.197 7.229   -6.041  1.00 40.80  ? 88  SER A CA  1 
ATOM   711  C C   . SER A 1 89  ? 40.801 6.631   -6.144  1.00 42.63  ? 88  SER A C   1 
ATOM   712  O O   . SER A 1 89  ? 39.798 7.346   -6.267  1.00 39.11  ? 88  SER A O   1 
ATOM   713  C CB  . SER A 1 89  ? 42.617 7.343   -4.573  1.00 37.46  ? 88  SER A CB  1 
ATOM   714  O OG  . SER A 1 89  ? 41.977 6.357   -3.805  1.00 45.04  ? 88  SER A OG  1 
ATOM   715  N N   . GLU A 1 90  ? 40.759 5.292   -6.113  1.00 39.72  ? 89  GLU A N   1 
ATOM   716  C CA  . GLU A 1 90  ? 39.502 4.571   -5.968  1.00 36.96  ? 89  GLU A CA  1 
ATOM   717  C C   . GLU A 1 90  ? 38.864 4.814   -4.611  1.00 42.57  ? 89  GLU A C   1 
ATOM   718  O O   . GLU A 1 90  ? 37.676 4.538   -4.443  1.00 47.34  ? 89  GLU A O   1 
ATOM   719  C CB  . GLU A 1 90  ? 39.724 3.074   -6.169  1.00 50.68  ? 89  GLU A CB  1 
ATOM   720  C CG  . GLU A 1 90  ? 40.700 2.719   -7.291  1.00 51.43  ? 89  GLU A CG  1 
ATOM   721  C CD  . GLU A 1 90  ? 40.415 1.352   -7.891  1.00 63.13  ? 89  GLU A CD  1 
ATOM   722  O OE1 . GLU A 1 90  ? 40.343 1.248   -9.137  1.00 68.73  ? 89  GLU A OE1 1 
ATOM   723  O OE2 . GLU A 1 90  ? 40.248 0.383   -7.116  1.00 70.70  ? 89  GLU A OE2 1 
ATOM   724  N N   . ASP A 1 91  ? 39.625 5.322   -3.645  1.00 42.59  ? 90  ASP A N   1 
ATOM   725  C CA  . ASP A 1 91  ? 39.106 5.649   -2.325  1.00 45.41  ? 90  ASP A CA  1 
ATOM   726  C C   . ASP A 1 91  ? 38.415 7.007   -2.270  1.00 45.79  ? 90  ASP A C   1 
ATOM   727  O O   . ASP A 1 91  ? 37.816 7.337   -1.241  1.00 48.50  ? 90  ASP A O   1 
ATOM   728  C CB  . ASP A 1 91  ? 40.245 5.622   -1.297  1.00 46.80  ? 90  ASP A CB  1 
ATOM   729  C CG  . ASP A 1 91  ? 40.807 4.226   -1.084  1.00 55.12  ? 90  ASP A CG  1 
ATOM   730  O OD1 . ASP A 1 91  ? 40.160 3.249   -1.531  1.00 54.79  ? 90  ASP A OD1 1 
ATOM   731  O OD2 . ASP A 1 91  ? 41.894 4.109   -0.473  1.00 61.36  ? 90  ASP A OD2 1 
ATOM   732  N N   . GLY A 1 92  ? 38.499 7.808   -3.326  1.00 39.76  ? 91  GLY A N   1 
ATOM   733  C CA  . GLY A 1 92  ? 37.932 9.146   -3.329  1.00 35.62  ? 91  GLY A CA  1 
ATOM   734  C C   . GLY A 1 92  ? 36.566 9.183   -3.992  1.00 37.98  ? 91  GLY A C   1 
ATOM   735  O O   . GLY A 1 92  ? 36.336 8.540   -5.020  1.00 37.92  ? 91  GLY A O   1 
ATOM   736  N N   . SER A 1 93  ? 35.664 9.941   -3.383  1.00 30.87  ? 92  SER A N   1 
ATOM   737  C CA  . SER A 1 93  ? 34.365 10.226  -3.969  1.00 34.02  ? 92  SER A CA  1 
ATOM   738  C C   . SER A 1 93  ? 34.491 11.356  -4.994  1.00 32.23  ? 92  SER A C   1 
ATOM   739  O O   . SER A 1 93  ? 35.144 12.365  -4.733  1.00 29.79  ? 92  SER A O   1 
ATOM   740  C CB  . SER A 1 93  ? 33.387 10.611  -2.858  1.00 31.42  ? 92  SER A CB  1 
ATOM   741  O OG  . SER A 1 93  ? 32.054 10.675  -3.338  1.00 34.96  ? 92  SER A OG  1 
ATOM   742  N N   . HIS A 1 94  ? 33.866 11.196  -6.164  1.00 27.07  ? 93  HIS A N   1 
ATOM   743  C CA  . HIS A 1 94  ? 33.926 12.248  -7.177  1.00 28.54  ? 93  HIS A CA  1 
ATOM   744  C C   . HIS A 1 94  ? 32.577 12.427  -7.860  1.00 26.73  ? 93  HIS A C   1 
ATOM   745  O O   . HIS A 1 94  ? 31.710 11.552  -7.820  1.00 24.24  ? 93  HIS A O   1 
ATOM   746  C CB  . HIS A 1 94  ? 35.028 11.965  -8.209  1.00 26.74  ? 93  HIS A CB  1 
ATOM   747  C CG  . HIS A 1 94  ? 36.387 11.894  -7.595  1.00 29.20  ? 93  HIS A CG  1 
ATOM   748  N ND1 . HIS A 1 94  ? 37.212 12.993  -7.487  1.00 31.92  ? 93  HIS A ND1 1 
ATOM   749  C CD2 . HIS A 1 94  ? 37.031 10.875  -6.979  1.00 30.14  ? 93  HIS A CD2 1 
ATOM   750  C CE1 . HIS A 1 94  ? 38.323 12.644  -6.862  1.00 31.08  ? 93  HIS A CE1 1 
ATOM   751  N NE2 . HIS A 1 94  ? 38.238 11.365  -6.541  1.00 32.78  ? 93  HIS A NE2 1 
ATOM   752  N N   . THR A 1 95  ? 32.417 13.580  -8.509  1.00 25.95  ? 94  THR A N   1 
ATOM   753  C CA  . THR A 1 95  ? 31.135 13.989  -9.072  1.00 26.51  ? 94  THR A CA  1 
ATOM   754  C C   . THR A 1 95  ? 31.282 14.415  -10.529 1.00 24.39  ? 94  THR A C   1 
ATOM   755  O O   . THR A 1 95  ? 32.103 15.284  -10.851 1.00 25.38  ? 94  THR A O   1 
ATOM   756  C CB  . THR A 1 95  ? 30.530 15.147  -8.269  1.00 26.56  ? 94  THR A CB  1 
ATOM   757  O OG1 . THR A 1 95  ? 30.488 14.787  -6.878  1.00 29.55  ? 94  THR A OG1 1 
ATOM   758  C CG2 . THR A 1 95  ? 29.107 15.478  -8.776  1.00 21.70  ? 94  THR A CG2 1 
ATOM   759  N N   . ILE A 1 96  ? 30.462 13.830  -11.399 1.00 18.22  ? 95  ILE A N   1 
ATOM   760  C CA  . ILE A 1 96  ? 30.275 14.324  -12.759 1.00 20.82  ? 95  ILE A CA  1 
ATOM   761  C C   . ILE A 1 96  ? 28.904 14.984  -12.845 1.00 19.86  ? 95  ILE A C   1 
ATOM   762  O O   . ILE A 1 96  ? 27.896 14.404  -12.425 1.00 20.77  ? 95  ILE A O   1 
ATOM   763  C CB  . ILE A 1 96  ? 30.409 13.202  -13.802 1.00 21.53  ? 95  ILE A CB  1 
ATOM   764  C CG1 . ILE A 1 96  ? 31.859 12.743  -13.934 1.00 19.59  ? 95  ILE A CG1 1 
ATOM   765  C CG2 . ILE A 1 96  ? 29.891 13.668  -15.180 1.00 18.92  ? 95  ILE A CG2 1 
ATOM   766  C CD1 . ILE A 1 96  ? 31.998 11.527  -14.895 1.00 18.19  ? 95  ILE A CD1 1 
ATOM   767  N N   . GLN A 1 97  ? 28.858 16.190  -13.398 1.00 21.65  ? 96  GLN A N   1 
ATOM   768  C CA  . GLN A 1 97  ? 27.594 16.876  -13.620 1.00 23.82  ? 96  GLN A CA  1 
ATOM   769  C C   . GLN A 1 97  ? 27.480 17.243  -15.093 1.00 23.01  ? 96  GLN A C   1 
ATOM   770  O O   . GLN A 1 97  ? 28.471 17.615  -15.725 1.00 18.80  ? 96  GLN A O   1 
ATOM   771  C CB  . GLN A 1 97  ? 27.473 18.139  -12.751 1.00 18.22  ? 96  GLN A CB  1 
ATOM   772  C CG  . GLN A 1 97  ? 27.162 17.879  -11.283 1.00 21.67  ? 96  GLN A CG  1 
ATOM   773  C CD  . GLN A 1 97  ? 27.503 19.084  -10.406 1.00 23.79  ? 96  GLN A CD  1 
ATOM   774  O OE1 . GLN A 1 97  ? 28.613 19.192  -9.886  1.00 24.42  ? 96  GLN A OE1 1 
ATOM   775  N NE2 . GLN A 1 97  ? 26.548 19.997  -10.254 1.00 20.97  ? 96  GLN A NE2 1 
ATOM   776  N N   . ILE A 1 98  ? 26.257 17.160  -15.620 1.00 22.24  ? 97  ILE A N   1 
ATOM   777  C CA  . ILE A 1 98  ? 25.963 17.431  -17.024 1.00 22.56  ? 97  ILE A CA  1 
ATOM   778  C C   . ILE A 1 98  ? 24.672 18.236  -17.113 1.00 18.93  ? 97  ILE A C   1 
ATOM   779  O O   . ILE A 1 98  ? 23.650 17.856  -16.533 1.00 21.02  ? 97  ILE A O   1 
ATOM   780  C CB  . ILE A 1 98  ? 25.826 16.126  -17.837 1.00 22.20  ? 97  ILE A CB  1 
ATOM   781  C CG1 . ILE A 1 98  ? 27.168 15.373  -17.908 1.00 19.91  ? 97  ILE A CG1 1 
ATOM   782  C CG2 . ILE A 1 98  ? 25.262 16.425  -19.236 1.00 19.13  ? 97  ILE A CG2 1 
ATOM   783  C CD1 . ILE A 1 98  ? 27.043 13.905  -18.396 1.00 19.80  ? 97  ILE A CD1 1 
ATOM   784  N N   . MET A 1 99  ? 24.702 19.326  -17.856 1.00 21.36  ? 98  MET A N   1 
ATOM   785  C CA  . MET A 1 99  ? 23.481 20.039  -18.196 1.00 24.36  ? 98  MET A CA  1 
ATOM   786  C C   . MET A 1 99  ? 23.360 20.105  -19.715 1.00 23.34  ? 98  MET A C   1 
ATOM   787  O O   . MET A 1 99  ? 24.348 20.363  -20.405 1.00 26.02  ? 98  MET A O   1 
ATOM   788  C CB  . MET A 1 99  ? 23.478 21.450  -17.584 1.00 23.34  ? 98  MET A CB  1 
ATOM   789  C CG  . MET A 1 99  ? 22.203 22.256  -17.862 1.00 30.92  ? 98  MET A CG  1 
ATOM   790  S SD  . MET A 1 99  ? 22.243 23.124  -19.453 1.00 38.70  ? 98  MET A SD  1 
ATOM   791  C CE  . MET A 1 99  ? 23.843 23.910  -19.463 1.00 30.16  ? 98  MET A CE  1 
ATOM   792  N N   . TYR A 1 100 ? 22.154 19.872  -20.239 1.00 24.08  ? 99  TYR A N   1 
ATOM   793  C CA  . TYR A 1 100 ? 21.913 20.149  -21.654 1.00 24.12  ? 99  TYR A CA  1 
ATOM   794  C C   . TYR A 1 100 ? 20.445 20.486  -21.876 1.00 24.21  ? 99  TYR A C   1 
ATOM   795  O O   . TYR A 1 100 ? 19.586 20.157  -21.049 1.00 24.52  ? 99  TYR A O   1 
ATOM   796  C CB  . TYR A 1 100 ? 22.376 18.985  -22.557 1.00 21.34  ? 99  TYR A CB  1 
ATOM   797  C CG  . TYR A 1 100 ? 21.635 17.662  -22.463 1.00 21.11  ? 99  TYR A CG  1 
ATOM   798  C CD1 . TYR A 1 100 ? 20.324 17.531  -22.908 1.00 20.91  ? 99  TYR A CD1 1 
ATOM   799  C CD2 . TYR A 1 100 ? 22.282 16.520  -22.000 1.00 21.19  ? 99  TYR A CD2 1 
ATOM   800  C CE1 . TYR A 1 100 ? 19.667 16.322  -22.867 1.00 19.38  ? 99  TYR A CE1 1 
ATOM   801  C CE2 . TYR A 1 100 ? 21.631 15.303  -21.948 1.00 24.56  ? 99  TYR A CE2 1 
ATOM   802  C CZ  . TYR A 1 100 ? 20.316 15.210  -22.385 1.00 24.26  ? 99  TYR A CZ  1 
ATOM   803  O OH  . TYR A 1 100 ? 19.651 13.997  -22.336 1.00 27.91  ? 99  TYR A OH  1 
ATOM   804  N N   . GLY A 1 101 ? 20.166 21.149  -22.997 1.00 23.94  ? 100 GLY A N   1 
ATOM   805  C CA  . GLY A 1 101 ? 18.802 21.501  -23.348 1.00 21.86  ? 100 GLY A CA  1 
ATOM   806  C C   . GLY A 1 101 ? 18.735 22.567  -24.429 1.00 25.82  ? 100 GLY A C   1 
ATOM   807  O O   . GLY A 1 101 ? 19.743 22.951  -25.030 1.00 24.19  ? 100 GLY A O   1 
ATOM   808  N N   . CYS A 1 102 ? 17.513 23.038  -24.674 1.00 27.13  ? 101 CYS A N   1 
ATOM   809  C CA  . CYS A 1 102 ? 17.318 23.989  -25.761 1.00 30.45  ? 101 CYS A CA  1 
ATOM   810  C C   . CYS A 1 102 ? 16.299 25.057  -25.389 1.00 29.84  ? 101 CYS A C   1 
ATOM   811  O O   . CYS A 1 102 ? 15.395 24.839  -24.580 1.00 31.98  ? 101 CYS A O   1 
ATOM   812  C CB  . CYS A 1 102 ? 16.851 23.283  -27.026 1.00 26.33  ? 101 CYS A CB  1 
ATOM   813  S SG  . CYS A 1 102 ? 15.417 22.264  -26.670 1.00 33.01  ? 101 CYS A SG  1 
ATOM   814  N N   . ASP A 1 103 ? 16.441 26.208  -26.030 1.00 33.52  ? 102 ASP A N   1 
ATOM   815  C CA  . ASP A 1 103 ? 15.487 27.304  -25.943 1.00 37.17  ? 102 ASP A CA  1 
ATOM   816  C C   . ASP A 1 103 ? 14.735 27.437  -27.261 1.00 34.88  ? 102 ASP A C   1 
ATOM   817  O O   . ASP A 1 103 ? 15.330 27.319  -28.336 1.00 37.58  ? 102 ASP A O   1 
ATOM   818  C CB  . ASP A 1 103 ? 16.201 28.623  -25.633 1.00 38.39  ? 102 ASP A CB  1 
ATOM   819  C CG  . ASP A 1 103 ? 17.003 28.570  -24.348 1.00 34.47  ? 102 ASP A CG  1 
ATOM   820  O OD1 . ASP A 1 103 ? 16.633 27.804  -23.443 1.00 31.26  ? 102 ASP A OD1 1 
ATOM   821  O OD2 . ASP A 1 103 ? 17.986 29.325  -24.226 1.00 42.34  ? 102 ASP A OD2 1 
ATOM   822  N N   . VAL A 1 104 ? 13.432 27.672  -27.173 1.00 34.52  ? 103 VAL A N   1 
ATOM   823  C CA  . VAL A 1 104 ? 12.633 28.037  -28.333 1.00 38.25  ? 103 VAL A CA  1 
ATOM   824  C C   . VAL A 1 104 ? 12.067 29.436  -28.134 1.00 42.87  ? 103 VAL A C   1 
ATOM   825  O O   . VAL A 1 104 ? 11.921 29.926  -27.009 1.00 46.11  ? 103 VAL A O   1 
ATOM   826  C CB  . VAL A 1 104 ? 11.496 27.039  -28.604 1.00 39.08  ? 103 VAL A CB  1 
ATOM   827  C CG1 . VAL A 1 104 ? 12.065 25.658  -28.930 1.00 36.89  ? 103 VAL A CG1 1 
ATOM   828  C CG2 . VAL A 1 104 ? 10.527 27.002  -27.425 1.00 33.48  ? 103 VAL A CG2 1 
ATOM   829  N N   . GLY A 1 105 ? 11.722 30.075  -29.255 1.00 50.81  ? 104 GLY A N   1 
ATOM   830  C CA  . GLY A 1 105 ? 11.050 31.356  -29.245 1.00 48.39  ? 104 GLY A CA  1 
ATOM   831  C C   . GLY A 1 105 ? 9.566  31.251  -28.940 1.00 56.91  ? 104 GLY A C   1 
ATOM   832  O O   . GLY A 1 105 ? 9.060  30.215  -28.482 1.00 54.14  ? 104 GLY A O   1 
ATOM   833  N N   . PRO A 1 106 ? 8.834  32.347  -29.174 1.00 64.33  ? 105 PRO A N   1 
ATOM   834  C CA  . PRO A 1 106 ? 7.374  32.312  -28.972 1.00 64.50  ? 105 PRO A CA  1 
ATOM   835  C C   . PRO A 1 106 ? 6.634  31.588  -30.086 1.00 59.42  ? 105 PRO A C   1 
ATOM   836  O O   . PRO A 1 106 ? 5.520  31.088  -29.854 1.00 61.74  ? 105 PRO A O   1 
ATOM   837  C CB  . PRO A 1 106 ? 6.994  33.797  -28.913 1.00 60.51  ? 105 PRO A CB  1 
ATOM   838  C CG  . PRO A 1 106 ? 8.050  34.474  -29.747 1.00 58.60  ? 105 PRO A CG  1 
ATOM   839  C CD  . PRO A 1 106 ? 9.315  33.667  -29.620 1.00 58.39  ? 105 PRO A CD  1 
ATOM   840  N N   . ASP A 1 107 ? 7.228  31.509  -31.277 1.00 55.53  ? 106 ASP A N   1 
ATOM   841  C CA  . ASP A 1 107 ? 6.707  30.683  -32.360 1.00 60.30  ? 106 ASP A CA  1 
ATOM   842  C C   . ASP A 1 107 ? 6.986  29.199  -32.153 1.00 62.85  ? 106 ASP A C   1 
ATOM   843  O O   . ASP A 1 107 ? 6.359  28.363  -32.815 1.00 62.23  ? 106 ASP A O   1 
ATOM   844  C CB  . ASP A 1 107 ? 7.320  31.133  -33.685 1.00 56.13  ? 106 ASP A CB  1 
ATOM   845  C CG  . ASP A 1 107 ? 8.832  31.229  -33.618 1.00 58.63  ? 106 ASP A CG  1 
ATOM   846  O OD1 . ASP A 1 107 ? 9.387  30.994  -32.523 1.00 59.74  ? 106 ASP A OD1 1 
ATOM   847  O OD2 . ASP A 1 107 ? 9.471  31.540  -34.650 1.00 52.84  ? 106 ASP A OD2 1 
ATOM   848  N N   . GLY A 1 108 ? 7.913  28.857  -31.264 1.00 56.60  ? 107 GLY A N   1 
ATOM   849  C CA  . GLY A 1 108 ? 8.220  27.479  -30.967 1.00 49.86  ? 107 GLY A CA  1 
ATOM   850  C C   . GLY A 1 108 ? 9.396  26.907  -31.718 1.00 44.35  ? 107 GLY A C   1 
ATOM   851  O O   . GLY A 1 108 ? 9.572  25.684  -31.710 1.00 43.35  ? 107 GLY A O   1 
ATOM   852  N N   . ARG A 1 109 ? 10.207 27.742  -32.361 1.00 43.04  ? 108 ARG A N   1 
ATOM   853  C CA  . ARG A 1 109 ? 11.320 27.273  -33.171 1.00 46.33  ? 108 ARG A CA  1 
ATOM   854  C C   . ARG A 1 109 ? 12.638 27.453  -32.427 1.00 39.19  ? 108 ARG A C   1 
ATOM   855  O O   . ARG A 1 109 ? 12.780 28.303  -31.539 1.00 34.02  ? 108 ARG A O   1 
ATOM   856  C CB  . ARG A 1 109 ? 11.361 27.981  -34.551 1.00 45.10  ? 108 ARG A CB  1 
ATOM   857  C CG  . ARG A 1 109 ? 10.136 27.665  -35.505 1.00 49.51  ? 108 ARG A CG  1 
ATOM   858  C CD  . ARG A 1 109 ? 9.860  28.719  -36.460 1.00 60.41  ? 108 ARG A CD  1 
ATOM   859  N NE  . ARG A 1 109 ? 11.040 28.947  -37.303 1.00 64.01  ? 108 ARG A NE  1 
ATOM   860  C CZ  . ARG A 1 109 ? 10.988 29.203  -38.558 1.00 62.75  ? 108 ARG A CZ  1 
ATOM   861  N NH1 . ARG A 1 109 ? 12.098 29.395  -39.275 1.00 61.39  ? 108 ARG A NH1 1 
ATOM   862  N NH2 . ARG A 1 109 ? 9.805  29.302  -39.062 1.00 60.29  ? 108 ARG A NH2 1 
ATOM   863  N N   . PHE A 1 110 ? 13.615 26.654  -32.851 1.00 36.49  ? 109 PHE A N   1 
ATOM   864  C CA  . PHE A 1 110 ? 14.911 26.608  -32.197 1.00 38.14  ? 109 PHE A CA  1 
ATOM   865  C C   . PHE A 1 110 ? 15.528 27.992  -32.092 1.00 36.82  ? 109 PHE A C   1 
ATOM   866  O O   . PHE A 1 110 ? 15.446 28.796  -33.021 1.00 36.81  ? 109 PHE A O   1 
ATOM   867  C CB  . PHE A 1 110 ? 15.857 25.686  -32.969 1.00 32.94  ? 109 PHE A CB  1 
ATOM   868  C CG  . PHE A 1 110 ? 17.281 25.736  -32.476 1.00 36.71  ? 109 PHE A CG  1 
ATOM   869  C CD1 . PHE A 1 110 ? 17.658 25.036  -31.326 1.00 35.25  ? 109 PHE A CD1 1 
ATOM   870  C CD2 . PHE A 1 110 ? 18.243 26.478  -33.152 1.00 35.52  ? 109 PHE A CD2 1 
ATOM   871  C CE1 . PHE A 1 110 ? 18.966 25.071  -30.869 1.00 28.87  ? 109 PHE A CE1 1 
ATOM   872  C CE2 . PHE A 1 110 ? 19.548 26.523  -32.698 1.00 37.15  ? 109 PHE A CE2 1 
ATOM   873  C CZ  . PHE A 1 110 ? 19.912 25.816  -31.544 1.00 33.38  ? 109 PHE A CZ  1 
ATOM   874  N N   . LEU A 1 111 ? 16.174 28.257  -30.956 1.00 40.12  ? 110 LEU A N   1 
ATOM   875  C CA  . LEU A 1 111 ? 16.949 29.486  -30.834 1.00 38.28  ? 110 LEU A CA  1 
ATOM   876  C C   . LEU A 1 111 ? 18.371 29.215  -30.354 1.00 37.67  ? 110 LEU A C   1 
ATOM   877  O O   . LEU A 1 111 ? 19.327 29.757  -30.914 1.00 39.66  ? 110 LEU A O   1 
ATOM   878  C CB  . LEU A 1 111 ? 16.233 30.472  -29.912 1.00 41.36  ? 110 LEU A CB  1 
ATOM   879  C CG  . LEU A 1 111 ? 16.892 31.842  -29.788 1.00 52.57  ? 110 LEU A CG  1 
ATOM   880  C CD1 . LEU A 1 111 ? 16.904 32.591  -31.133 1.00 47.07  ? 110 LEU A CD1 1 
ATOM   881  C CD2 . LEU A 1 111 ? 16.101 32.618  -28.758 1.00 57.65  ? 110 LEU A CD2 1 
ATOM   882  N N   . ARG A 1 112 ? 18.539 28.379  -29.331 1.00 35.54  ? 111 ARG A N   1 
ATOM   883  C CA  . ARG A 1 112 ? 19.890 28.044  -28.900 1.00 35.45  ? 111 ARG A CA  1 
ATOM   884  C C   . ARG A 1 112 ? 19.890 26.693  -28.205 1.00 32.07  ? 111 ARG A C   1 
ATOM   885  O O   . ARG A 1 112 ? 18.857 26.204  -27.739 1.00 31.00  ? 111 ARG A O   1 
ATOM   886  C CB  . ARG A 1 112 ? 20.484 29.114  -27.983 1.00 39.18  ? 111 ARG A CB  1 
ATOM   887  C CG  . ARG A 1 112 ? 19.605 29.483  -26.826 1.00 44.80  ? 111 ARG A CG  1 
ATOM   888  C CD  . ARG A 1 112 ? 20.125 30.715  -26.087 1.00 48.73  ? 111 ARG A CD  1 
ATOM   889  N NE  . ARG A 1 112 ? 19.968 31.940  -26.851 1.00 51.27  ? 111 ARG A NE  1 
ATOM   890  C CZ  . ARG A 1 112 ? 18.887 32.707  -26.796 1.00 58.01  ? 111 ARG A CZ  1 
ATOM   891  N NH1 . ARG A 1 112 ? 17.879 32.359  -26.003 1.00 49.21  ? 111 ARG A NH1 1 
ATOM   892  N NH2 . ARG A 1 112 ? 18.812 33.809  -27.540 1.00 53.84  ? 111 ARG A NH2 1 
ATOM   893  N N   . GLY A 1 113 ? 21.078 26.088  -28.170 1.00 30.45  ? 112 GLY A N   1 
ATOM   894  C CA  . GLY A 1 113 ? 21.262 24.813  -27.524 1.00 31.74  ? 112 GLY A CA  1 
ATOM   895  C C   . GLY A 1 113 ? 22.461 24.856  -26.597 1.00 32.10  ? 112 GLY A C   1 
ATOM   896  O O   . GLY A 1 113 ? 23.376 25.670  -26.758 1.00 30.38  ? 112 GLY A O   1 
ATOM   897  N N   . TYR A 1 114 ? 22.448 23.940  -25.627 1.00 25.90  ? 113 TYR A N   1 
ATOM   898  C CA  . TYR A 1 114 ? 23.441 23.899  -24.560 1.00 28.69  ? 113 TYR A CA  1 
ATOM   899  C C   . TYR A 1 114 ? 23.834 22.466  -24.253 1.00 27.27  ? 113 TYR A C   1 
ATOM   900  O O   . TYR A 1 114 ? 22.982 21.571  -24.271 1.00 26.37  ? 113 TYR A O   1 
ATOM   901  C CB  . TYR A 1 114 ? 22.898 24.541  -23.292 1.00 27.18  ? 113 TYR A CB  1 
ATOM   902  C CG  . TYR A 1 114 ? 22.639 25.998  -23.469 1.00 30.71  ? 113 TYR A CG  1 
ATOM   903  C CD1 . TYR A 1 114 ? 23.688 26.907  -23.418 1.00 36.04  ? 113 TYR A CD1 1 
ATOM   904  C CD2 . TYR A 1 114 ? 21.353 26.474  -23.731 1.00 35.49  ? 113 TYR A CD2 1 
ATOM   905  C CE1 . TYR A 1 114 ? 23.474 28.258  -23.587 1.00 46.25  ? 113 TYR A CE1 1 
ATOM   906  C CE2 . TYR A 1 114 ? 21.120 27.837  -23.902 1.00 43.90  ? 113 TYR A CE2 1 
ATOM   907  C CZ  . TYR A 1 114 ? 22.193 28.723  -23.831 1.00 50.30  ? 113 TYR A CZ  1 
ATOM   908  O OH  . TYR A 1 114 ? 22.012 30.072  -23.991 1.00 53.83  ? 113 TYR A OH  1 
ATOM   909  N N   . ARG A 1 115 ? 25.126 22.265  -23.975 1.00 26.08  ? 114 ARG A N   1 
ATOM   910  C CA  . ARG A 1 115 ? 25.654 21.000  -23.447 1.00 27.55  ? 114 ARG A CA  1 
ATOM   911  C C   . ARG A 1 115 ? 26.935 21.319  -22.698 1.00 25.79  ? 114 ARG A C   1 
ATOM   912  O O   . ARG A 1 115 ? 27.873 21.857  -23.293 1.00 25.32  ? 114 ARG A O   1 
ATOM   913  C CB  . ARG A 1 115 ? 25.923 19.977  -24.568 1.00 25.29  ? 114 ARG A CB  1 
ATOM   914  C CG  . ARG A 1 115 ? 26.830 18.778  -24.186 1.00 28.25  ? 114 ARG A CG  1 
ATOM   915  C CD  . ARG A 1 115 ? 26.112 17.721  -23.337 1.00 21.94  ? 114 ARG A CD  1 
ATOM   916  N NE  . ARG A 1 115 ? 27.033 16.783  -22.690 1.00 23.39  ? 114 ARG A NE  1 
ATOM   917  C CZ  . ARG A 1 115 ? 26.940 15.449  -22.747 1.00 24.46  ? 114 ARG A CZ  1 
ATOM   918  N NH1 . ARG A 1 115 ? 25.971 14.845  -23.440 1.00 25.07  ? 114 ARG A NH1 1 
ATOM   919  N NH2 . ARG A 1 115 ? 27.836 14.709  -22.119 1.00 25.27  ? 114 ARG A NH2 1 
ATOM   920  N N   . GLN A 1 116 ? 26.982 20.996  -21.405 1.00 27.73  ? 115 GLN A N   1 
ATOM   921  C CA  . GLN A 1 116 ? 28.116 21.380  -20.569 1.00 27.79  ? 115 GLN A CA  1 
ATOM   922  C C   . GLN A 1 116 ? 28.351 20.320  -19.507 1.00 26.65  ? 115 GLN A C   1 
ATOM   923  O O   . GLN A 1 116 ? 27.406 19.915  -18.826 1.00 24.05  ? 115 GLN A O   1 
ATOM   924  C CB  . GLN A 1 116 ? 27.879 22.728  -19.886 1.00 29.25  ? 115 GLN A CB  1 
ATOM   925  C CG  . GLN A 1 116 ? 28.031 23.922  -20.783 1.00 31.51  ? 115 GLN A CG  1 
ATOM   926  C CD  . GLN A 1 116 ? 27.179 25.103  -20.319 1.00 43.05  ? 115 GLN A CD  1 
ATOM   927  O OE1 . GLN A 1 116 ? 26.712 25.908  -21.136 1.00 44.31  ? 115 GLN A OE1 1 
ATOM   928  N NE2 . GLN A 1 116 ? 26.954 25.197  -19.009 1.00 31.90  ? 115 GLN A NE2 1 
ATOM   929  N N   . ASP A 1 117 ? 29.608 19.899  -19.363 1.00 23.43  ? 116 ASP A N   1 
ATOM   930  C CA  . ASP A 1 117 ? 30.006 18.866  -18.423 1.00 22.97  ? 116 ASP A CA  1 
ATOM   931  C C   . ASP A 1 117 ? 30.945 19.467  -17.374 1.00 27.45  ? 116 ASP A C   1 
ATOM   932  O O   . ASP A 1 117 ? 31.768 20.347  -17.682 1.00 23.42  ? 116 ASP A O   1 
ATOM   933  C CB  . ASP A 1 117 ? 30.705 17.703  -19.149 1.00 24.86  ? 116 ASP A CB  1 
ATOM   934  C CG  . ASP A 1 117 ? 29.785 16.977  -20.136 1.00 25.87  ? 116 ASP A CG  1 
ATOM   935  O OD1 . ASP A 1 117 ? 28.990 17.654  -20.835 1.00 24.57  ? 116 ASP A OD1 1 
ATOM   936  O OD2 . ASP A 1 117 ? 29.862 15.725  -20.218 1.00 25.22  ? 116 ASP A OD2 1 
ATOM   937  N N   . ALA A 1 118 ? 30.823 18.973  -16.141 1.00 23.89  ? 117 ALA A N   1 
ATOM   938  C CA  . ALA A 1 118 ? 31.639 19.397  -15.016 1.00 22.69  ? 117 ALA A CA  1 
ATOM   939  C C   . ALA A 1 118 ? 32.146 18.186  -14.249 1.00 23.00  ? 117 ALA A C   1 
ATOM   940  O O   . ALA A 1 118 ? 31.474 17.157  -14.169 1.00 22.72  ? 117 ALA A O   1 
ATOM   941  C CB  . ALA A 1 118 ? 30.840 20.290  -14.058 1.00 25.10  ? 117 ALA A CB  1 
ATOM   942  N N   . TYR A 1 119 ? 33.321 18.340  -13.640 1.00 24.92  ? 118 TYR A N   1 
ATOM   943  C CA  . TYR A 1 119 ? 33.926 17.311  -12.808 1.00 20.52  ? 118 TYR A CA  1 
ATOM   944  C C   . TYR A 1 119 ? 34.278 17.939  -11.468 1.00 23.67  ? 118 TYR A C   1 
ATOM   945  O O   . TYR A 1 119 ? 35.024 18.919  -11.421 1.00 20.14  ? 118 TYR A O   1 
ATOM   946  C CB  . TYR A 1 119 ? 35.172 16.727  -13.477 1.00 24.07  ? 118 TYR A CB  1 
ATOM   947  C CG  . TYR A 1 119 ? 35.801 15.581  -12.727 1.00 23.94  ? 118 TYR A CG  1 
ATOM   948  C CD1 . TYR A 1 119 ? 35.050 14.455  -12.381 1.00 20.11  ? 118 TYR A CD1 1 
ATOM   949  C CD2 . TYR A 1 119 ? 37.151 15.614  -12.372 1.00 23.89  ? 118 TYR A CD2 1 
ATOM   950  C CE1 . TYR A 1 119 ? 35.625 13.391  -11.698 1.00 21.60  ? 118 TYR A CE1 1 
ATOM   951  C CE2 . TYR A 1 119 ? 37.738 14.549  -11.676 1.00 23.31  ? 118 TYR A CE2 1 
ATOM   952  C CZ  . TYR A 1 119 ? 36.968 13.446  -11.348 1.00 22.68  ? 118 TYR A CZ  1 
ATOM   953  O OH  . TYR A 1 119 ? 37.535 12.394  -10.676 1.00 26.53  ? 118 TYR A OH  1 
ATOM   954  N N   . ASP A 1 120 ? 33.743 17.374  -10.382 1.00 23.76  ? 119 ASP A N   1 
ATOM   955  C CA  . ASP A 1 120 ? 33.982 17.877  -9.024  1.00 28.05  ? 119 ASP A CA  1 
ATOM   956  C C   . ASP A 1 120 ? 33.712 19.381  -8.911  1.00 28.25  ? 119 ASP A C   1 
ATOM   957  O O   . ASP A 1 120 ? 34.486 20.134  -8.319  1.00 27.55  ? 119 ASP A O   1 
ATOM   958  C CB  . ASP A 1 120 ? 35.400 17.541  -8.554  1.00 26.68  ? 119 ASP A CB  1 
ATOM   959  C CG  . ASP A 1 120 ? 35.554 16.072  -8.182  1.00 30.45  ? 119 ASP A CG  1 
ATOM   960  O OD1 . ASP A 1 120 ? 34.537 15.459  -7.787  1.00 26.47  ? 119 ASP A OD1 1 
ATOM   961  O OD2 . ASP A 1 120 ? 36.690 15.538  -8.273  1.00 30.44  ? 119 ASP A OD2 1 
ATOM   962  N N   . GLY A 1 121 ? 32.590 19.816  -9.480  1.00 27.19  ? 120 GLY A N   1 
ATOM   963  C CA  . GLY A 1 121 ? 32.133 21.181  -9.299  1.00 27.94  ? 120 GLY A CA  1 
ATOM   964  C C   . GLY A 1 121 ? 32.783 22.223  -10.182 1.00 29.00  ? 120 GLY A C   1 
ATOM   965  O O   . GLY A 1 121 ? 32.533 23.418  -9.986  1.00 33.25  ? 120 GLY A O   1 
ATOM   966  N N   . LYS A 1 122 ? 33.594 21.825  -11.155 1.00 25.68  ? 121 LYS A N   1 
ATOM   967  C CA  . LYS A 1 122 ? 34.234 22.779  -12.051 1.00 27.49  ? 121 LYS A CA  1 
ATOM   968  C C   . LYS A 1 122 ? 34.034 22.358  -13.498 1.00 26.21  ? 121 LYS A C   1 
ATOM   969  O O   . LYS A 1 122 ? 33.945 21.161  -13.813 1.00 25.58  ? 121 LYS A O   1 
ATOM   970  C CB  . LYS A 1 122 ? 35.743 22.917  -11.771 1.00 28.06  ? 121 LYS A CB  1 
ATOM   971  C CG  . LYS A 1 122 ? 36.087 23.366  -10.354 1.00 32.79  ? 121 LYS A CG  1 
ATOM   972  C CD  . LYS A 1 122 ? 37.583 23.599  -10.221 1.00 38.91  ? 121 LYS A CD  1 
ATOM   973  C CE  . LYS A 1 122 ? 37.953 25.016  -10.623 1.00 49.06  ? 121 LYS A CE  1 
ATOM   974  N NZ  . LYS A 1 122 ? 37.991 25.924  -9.435  1.00 56.86  ? 121 LYS A NZ  1 
ATOM   975  N N   . ASP A 1 123 ? 33.979 23.365  -14.372 1.00 26.93  ? 122 ASP A N   1 
ATOM   976  C CA  . ASP A 1 123 ? 33.895 23.129  -15.804 1.00 24.85  ? 122 ASP A CA  1 
ATOM   977  C C   . ASP A 1 123 ? 34.910 22.077  -16.218 1.00 27.92  ? 122 ASP A C   1 
ATOM   978  O O   . ASP A 1 123 ? 36.087 22.151  -15.858 1.00 25.82  ? 122 ASP A O   1 
ATOM   979  C CB  . ASP A 1 123 ? 34.162 24.422  -16.580 1.00 24.70  ? 122 ASP A CB  1 
ATOM   980  C CG  . ASP A 1 123 ? 33.038 25.434  -16.456 1.00 29.58  ? 122 ASP A CG  1 
ATOM   981  O OD1 . ASP A 1 123 ? 32.011 25.156  -15.790 1.00 29.87  ? 122 ASP A OD1 1 
ATOM   982  O OD2 . ASP A 1 123 ? 33.195 26.534  -17.026 1.00 34.80  ? 122 ASP A OD2 1 
ATOM   983  N N   . TYR A 1 124 ? 34.444 21.084  -16.967 1.00 24.98  ? 123 TYR A N   1 
ATOM   984  C CA  . TYR A 1 124 ? 35.344 20.164  -17.635 1.00 24.37  ? 123 TYR A CA  1 
ATOM   985  C C   . TYR A 1 124 ? 35.339 20.395  -19.146 1.00 26.44  ? 123 TYR A C   1 
ATOM   986  O O   . TYR A 1 124 ? 36.353 20.812  -19.716 1.00 26.56  ? 123 TYR A O   1 
ATOM   987  C CB  . TYR A 1 124 ? 34.971 18.719  -17.243 1.00 22.05  ? 123 TYR A CB  1 
ATOM   988  C CG  . TYR A 1 124 ? 35.908 17.669  -17.815 1.00 24.90  ? 123 TYR A CG  1 
ATOM   989  C CD1 . TYR A 1 124 ? 37.186 17.486  -17.295 1.00 24.21  ? 123 TYR A CD1 1 
ATOM   990  C CD2 . TYR A 1 124 ? 35.511 16.860  -18.875 1.00 24.19  ? 123 TYR A CD2 1 
ATOM   991  C CE1 . TYR A 1 124 ? 38.035 16.520  -17.813 1.00 27.02  ? 123 TYR A CE1 1 
ATOM   992  C CE2 . TYR A 1 124 ? 36.354 15.899  -19.395 1.00 25.00  ? 123 TYR A CE2 1 
ATOM   993  C CZ  . TYR A 1 124 ? 37.614 15.737  -18.869 1.00 23.79  ? 123 TYR A CZ  1 
ATOM   994  O OH  . TYR A 1 124 ? 38.457 14.786  -19.400 1.00 28.56  ? 123 TYR A OH  1 
ATOM   995  N N   . ILE A 1 125 ? 34.204 20.238  -19.816 1.00 23.49  ? 124 ILE A N   1 
ATOM   996  C CA  . ILE A 1 125 ? 34.142 20.487  -21.255 1.00 26.09  ? 124 ILE A CA  1 
ATOM   997  C C   . ILE A 1 125 ? 32.750 21.006  -21.602 1.00 26.40  ? 124 ILE A C   1 
ATOM   998  O O   . ILE A 1 125 ? 31.751 20.560  -21.026 1.00 25.67  ? 124 ILE A O   1 
ATOM   999  C CB  . ILE A 1 125 ? 34.487 19.205  -22.045 1.00 23.22  ? 124 ILE A CB  1 
ATOM   1000 C CG1 . ILE A 1 125 ? 34.514 19.460  -23.550 1.00 24.50  ? 124 ILE A CG1 1 
ATOM   1001 C CG2 . ILE A 1 125 ? 33.492 18.116  -21.725 1.00 20.37  ? 124 ILE A CG2 1 
ATOM   1002 C CD1 . ILE A 1 125 ? 35.326 18.442  -24.293 1.00 23.82  ? 124 ILE A CD1 1 
ATOM   1003 N N   . ALA A 1 126 ? 32.680 21.941  -22.561 1.00 24.50  ? 125 ALA A N   1 
ATOM   1004 C CA  . ALA A 1 126 ? 31.404 22.537  -22.937 1.00 28.18  ? 125 ALA A CA  1 
ATOM   1005 C C   . ALA A 1 126 ? 31.280 22.646  -24.453 1.00 29.44  ? 125 ALA A C   1 
ATOM   1006 O O   . ALA A 1 126 ? 32.251 22.935  -25.155 1.00 29.21  ? 125 ALA A O   1 
ATOM   1007 C CB  . ALA A 1 126 ? 31.219 23.937  -22.310 1.00 26.27  ? 125 ALA A CB  1 
ATOM   1008 N N   . LEU A 1 127 ? 30.072 22.412  -24.948 1.00 28.44  ? 126 LEU A N   1 
ATOM   1009 C CA  . LEU A 1 127 ? 29.754 22.716  -26.334 1.00 30.34  ? 126 LEU A CA  1 
ATOM   1010 C C   . LEU A 1 127 ? 29.622 24.228  -26.494 1.00 31.28  ? 126 LEU A C   1 
ATOM   1011 O O   . LEU A 1 127 ? 28.944 24.881  -25.694 1.00 29.85  ? 126 LEU A O   1 
ATOM   1012 C CB  . LEU A 1 127 ? 28.454 22.013  -26.725 1.00 27.56  ? 126 LEU A CB  1 
ATOM   1013 C CG  . LEU A 1 127 ? 27.965 22.043  -28.179 1.00 32.28  ? 126 LEU A CG  1 
ATOM   1014 C CD1 . LEU A 1 127 ? 28.958 21.396  -29.100 1.00 28.43  ? 126 LEU A CD1 1 
ATOM   1015 C CD2 . LEU A 1 127 ? 26.612 21.351  -28.268 1.00 28.46  ? 126 LEU A CD2 1 
ATOM   1016 N N   . ASN A 1 128 ? 30.270 24.789  -27.514 1.00 28.47  ? 127 ASN A N   1 
ATOM   1017 C CA  . ASN A 1 128 ? 30.163 26.226  -27.733 1.00 31.61  ? 127 ASN A CA  1 
ATOM   1018 C C   . ASN A 1 128 ? 28.794 26.577  -28.325 1.00 33.28  ? 127 ASN A C   1 
ATOM   1019 O O   . ASN A 1 128 ? 28.011 25.701  -28.708 1.00 32.87  ? 127 ASN A O   1 
ATOM   1020 C CB  . ASN A 1 128 ? 31.268 26.719  -28.664 1.00 33.04  ? 127 ASN A CB  1 
ATOM   1021 C CG  . ASN A 1 128 ? 32.648 26.563  -28.075 1.00 34.91  ? 127 ASN A CG  1 
ATOM   1022 O OD1 . ASN A 1 128 ? 33.607 26.266  -28.795 1.00 36.01  ? 127 ASN A OD1 1 
ATOM   1023 N ND2 . ASN A 1 128 ? 32.768 26.768  -26.769 1.00 33.61  ? 127 ASN A ND2 1 
ATOM   1024 N N   . GLU A 1 129 ? 28.526 27.887  -28.430 1.00 30.59  ? 128 GLU A N   1 
ATOM   1025 C CA  . GLU A 1 129 ? 27.231 28.352  -28.932 1.00 37.67  ? 128 GLU A CA  1 
ATOM   1026 C C   . GLU A 1 129 ? 26.955 27.896  -30.368 1.00 31.00  ? 128 GLU A C   1 
ATOM   1027 O O   . GLU A 1 129 ? 25.795 27.670  -30.727 1.00 31.55  ? 128 GLU A O   1 
ATOM   1028 C CB  . GLU A 1 129 ? 27.129 29.883  -28.849 1.00 37.79  ? 128 GLU A CB  1 
ATOM   1029 C CG  . GLU A 1 129 ? 25.766 30.427  -29.398 1.00 42.19  ? 128 GLU A CG  1 
ATOM   1030 C CD  . GLU A 1 129 ? 25.681 31.959  -29.536 1.00 55.27  ? 128 GLU A CD  1 
ATOM   1031 O OE1 . GLU A 1 129 ? 26.535 32.683  -28.975 1.00 52.24  ? 128 GLU A OE1 1 
ATOM   1032 O OE2 . GLU A 1 129 ? 24.732 32.442  -30.202 1.00 63.11  ? 128 GLU A OE2 1 
ATOM   1033 N N   . ASP A 1 130 ? 27.983 27.760  -31.206 1.00 28.84  ? 129 ASP A N   1 
ATOM   1034 C CA  . ASP A 1 130 ? 27.740 27.317  -32.578 1.00 31.70  ? 129 ASP A CA  1 
ATOM   1035 C C   . ASP A 1 130 ? 27.439 25.825  -32.686 1.00 34.96  ? 129 ASP A C   1 
ATOM   1036 O O   . ASP A 1 130 ? 27.211 25.344  -33.802 1.00 34.74  ? 129 ASP A O   1 
ATOM   1037 C CB  . ASP A 1 130 ? 28.923 27.674  -33.494 1.00 34.24  ? 129 ASP A CB  1 
ATOM   1038 C CG  . ASP A 1 130 ? 30.248 27.014  -33.077 1.00 37.79  ? 129 ASP A CG  1 
ATOM   1039 O OD1 . ASP A 1 130 ? 30.270 26.137  -32.189 1.00 38.50  ? 129 ASP A OD1 1 
ATOM   1040 O OD2 . ASP A 1 130 ? 31.290 27.388  -33.661 1.00 42.06  ? 129 ASP A OD2 1 
ATOM   1041 N N   . LEU A 1 131 ? 27.432 25.094  -31.563 1.00 33.15  ? 130 LEU A N   1 
ATOM   1042 C CA  . LEU A 1 131 ? 27.082 23.671  -31.520 1.00 29.57  ? 130 LEU A CA  1 
ATOM   1043 C C   . LEU A 1 131 ? 27.930 22.850  -32.479 1.00 29.14  ? 130 LEU A C   1 
ATOM   1044 O O   . LEU A 1 131 ? 27.499 21.803  -32.967 1.00 31.51  ? 130 LEU A O   1 
ATOM   1045 C CB  . LEU A 1 131 ? 25.601 23.443  -31.810 1.00 27.73  ? 130 LEU A CB  1 
ATOM   1046 C CG  . LEU A 1 131 ? 24.616 24.367  -31.131 1.00 29.27  ? 130 LEU A CG  1 
ATOM   1047 C CD1 . LEU A 1 131 ? 23.213 23.976  -31.556 1.00 29.99  ? 130 LEU A CD1 1 
ATOM   1048 C CD2 . LEU A 1 131 ? 24.779 24.306  -29.609 1.00 31.60  ? 130 LEU A CD2 1 
ATOM   1049 N N   . ARG A 1 132 ? 29.147 23.324  -32.740 1.00 33.12  ? 131 ARG A N   1 
ATOM   1050 C CA  . ARG A 1 132 ? 30.057 22.678  -33.679 1.00 34.47  ? 131 ARG A CA  1 
ATOM   1051 C C   . ARG A 1 132 ? 31.472 22.637  -33.130 1.00 34.15  ? 131 ARG A C   1 
ATOM   1052 O O   . ARG A 1 132 ? 32.381 22.183  -33.835 1.00 39.35  ? 131 ARG A O   1 
ATOM   1053 C CB  . ARG A 1 132 ? 30.062 23.408  -35.039 1.00 34.06  ? 131 ARG A CB  1 
ATOM   1054 C CG  . ARG A 1 132 ? 28.760 23.275  -35.805 1.00 36.99  ? 131 ARG A CG  1 
ATOM   1055 C CD  . ARG A 1 132 ? 28.576 24.380  -36.853 1.00 37.37  ? 131 ARG A CD  1 
ATOM   1056 N NE  . ARG A 1 132 ? 27.508 24.009  -37.772 1.00 41.37  ? 131 ARG A NE  1 
ATOM   1057 C CZ  . ARG A 1 132 ? 26.236 24.342  -37.609 1.00 44.45  ? 131 ARG A CZ  1 
ATOM   1058 N NH1 . ARG A 1 132 ? 25.875 25.083  -36.563 1.00 45.05  ? 131 ARG A NH1 1 
ATOM   1059 N NH2 . ARG A 1 132 ? 25.328 23.941  -38.497 1.00 44.71  ? 131 ARG A NH2 1 
ATOM   1060 N N   . SER A 1 133 ? 31.673 23.060  -31.887 1.00 35.18  ? 132 SER A N   1 
ATOM   1061 C CA  . SER A 1 133 ? 32.976 23.417  -31.359 1.00 36.18  ? 132 SER A CA  1 
ATOM   1062 C C   . SER A 1 133 ? 32.971 23.213  -29.841 1.00 31.90  ? 132 SER A C   1 
ATOM   1063 O O   . SER A 1 133 ? 31.930 23.356  -29.195 1.00 30.42  ? 132 SER A O   1 
ATOM   1064 C CB  . SER A 1 133 ? 33.269 24.870  -31.750 1.00 31.41  ? 132 SER A CB  1 
ATOM   1065 O OG  . SER A 1 133 ? 34.394 25.362  -31.068 1.00 48.33  ? 132 SER A OG  1 
ATOM   1066 N N   . TRP A 1 134 ? 34.133 22.879  -29.266 1.00 30.67  ? 133 TRP A N   1 
ATOM   1067 C CA  . TRP A 1 134 ? 34.212 22.553  -27.839 1.00 32.30  ? 133 TRP A CA  1 
ATOM   1068 C C   . TRP A 1 134 ? 35.217 23.442  -27.099 1.00 32.21  ? 133 TRP A C   1 
ATOM   1069 O O   . TRP A 1 134 ? 36.275 23.781  -27.631 1.00 31.80  ? 133 TRP A O   1 
ATOM   1070 C CB  . TRP A 1 134 ? 34.608 21.079  -27.607 1.00 29.47  ? 133 TRP A CB  1 
ATOM   1071 C CG  . TRP A 1 134 ? 33.647 20.043  -28.164 1.00 30.00  ? 133 TRP A CG  1 
ATOM   1072 C CD1 . TRP A 1 134 ? 33.777 19.359  -29.343 1.00 28.78  ? 133 TRP A CD1 1 
ATOM   1073 C CD2 . TRP A 1 134 ? 32.439 19.556  -27.554 1.00 27.95  ? 133 TRP A CD2 1 
ATOM   1074 N NE1 . TRP A 1 134 ? 32.720 18.488  -29.504 1.00 28.77  ? 133 TRP A NE1 1 
ATOM   1075 C CE2 . TRP A 1 134 ? 31.888 18.589  -28.425 1.00 27.38  ? 133 TRP A CE2 1 
ATOM   1076 C CE3 . TRP A 1 134 ? 31.770 19.845  -26.364 1.00 27.84  ? 133 TRP A CE3 1 
ATOM   1077 C CZ2 . TRP A 1 134 ? 30.693 17.925  -28.148 1.00 25.17  ? 133 TRP A CZ2 1 
ATOM   1078 C CZ3 . TRP A 1 134 ? 30.602 19.177  -26.083 1.00 23.38  ? 133 TRP A CZ3 1 
ATOM   1079 C CH2 . TRP A 1 134 ? 30.069 18.231  -26.975 1.00 27.65  ? 133 TRP A CH2 1 
ATOM   1080 N N   . THR A 1 135 ? 34.892 23.790  -25.843 1.00 28.12  ? 134 THR A N   1 
ATOM   1081 C CA  . THR A 1 135 ? 35.828 24.454  -24.925 1.00 28.76  ? 134 THR A CA  1 
ATOM   1082 C C   . THR A 1 135 ? 36.231 23.476  -23.822 1.00 27.80  ? 134 THR A C   1 
ATOM   1083 O O   . THR A 1 135 ? 35.396 23.080  -23.001 1.00 27.42  ? 134 THR A O   1 
ATOM   1084 C CB  . THR A 1 135 ? 35.220 25.714  -24.300 1.00 34.61  ? 134 THR A CB  1 
ATOM   1085 O OG1 . THR A 1 135 ? 34.957 26.680  -25.318 1.00 33.76  ? 134 THR A OG1 1 
ATOM   1086 C CG2 . THR A 1 135 ? 36.167 26.334  -23.231 1.00 26.12  ? 134 THR A CG2 1 
ATOM   1087 N N   . ALA A 1 136 ? 37.511 23.111  -23.795 1.00 32.98  ? 135 ALA A N   1 
ATOM   1088 C CA  . ALA A 1 136 ? 38.080 22.258  -22.760 1.00 25.27  ? 135 ALA A CA  1 
ATOM   1089 C C   . ALA A 1 136 ? 38.675 23.127  -21.661 1.00 30.77  ? 135 ALA A C   1 
ATOM   1090 O O   . ALA A 1 136 ? 39.425 24.062  -21.945 1.00 32.14  ? 135 ALA A O   1 
ATOM   1091 C CB  . ALA A 1 136 ? 39.158 21.351  -23.351 1.00 28.96  ? 135 ALA A CB  1 
ATOM   1092 N N   . ALA A 1 137 ? 38.354 22.811  -20.404 1.00 31.60  ? 136 ALA A N   1 
ATOM   1093 C CA  . ALA A 1 137 ? 38.728 23.705  -19.315 1.00 31.18  ? 136 ALA A CA  1 
ATOM   1094 C C   . ALA A 1 137 ? 40.157 23.505  -18.828 1.00 33.93  ? 136 ALA A C   1 
ATOM   1095 O O   . ALA A 1 137 ? 40.730 24.442  -18.263 1.00 34.74  ? 136 ALA A O   1 
ATOM   1096 C CB  . ALA A 1 137 ? 37.763 23.543  -18.147 1.00 29.17  ? 136 ALA A CB  1 
ATOM   1097 N N   . ASP A 1 138 ? 40.745 22.328  -19.034 1.00 31.13  ? 137 ASP A N   1 
ATOM   1098 C CA  . ASP A 1 138 ? 42.105 22.053  -18.574 1.00 32.47  ? 137 ASP A CA  1 
ATOM   1099 C C   . ASP A 1 138 ? 42.701 20.954  -19.447 1.00 31.29  ? 137 ASP A C   1 
ATOM   1100 O O   . ASP A 1 138 ? 42.084 20.494  -20.405 1.00 35.21  ? 137 ASP A O   1 
ATOM   1101 C CB  . ASP A 1 138 ? 42.131 21.670  -17.089 1.00 26.79  ? 137 ASP A CB  1 
ATOM   1102 C CG  . ASP A 1 138 ? 41.277 20.439  -16.777 1.00 33.25  ? 137 ASP A CG  1 
ATOM   1103 O OD1 . ASP A 1 138 ? 41.000 19.632  -17.693 1.00 34.85  ? 137 ASP A OD1 1 
ATOM   1104 O OD2 . ASP A 1 138 ? 40.887 20.269  -15.603 1.00 35.80  ? 137 ASP A OD2 1 
ATOM   1105 N N   . MET A 1 139 ? 43.911 20.521  -19.089 1.00 37.00  ? 138 MET A N   1 
ATOM   1106 C CA  . MET A 1 139 ? 44.650 19.581  -19.924 1.00 36.40  ? 138 MET A CA  1 
ATOM   1107 C C   . MET A 1 139 ? 43.964 18.224  -19.995 1.00 37.41  ? 138 MET A C   1 
ATOM   1108 O O   . MET A 1 139 ? 44.028 17.547  -21.030 1.00 39.01  ? 138 MET A O   1 
ATOM   1109 C CB  . MET A 1 139 ? 46.075 19.430  -19.398 1.00 36.02  ? 138 MET A CB  1 
ATOM   1110 C CG  . MET A 1 139 ? 46.957 20.655  -19.626 1.00 42.77  ? 138 MET A CG  1 
ATOM   1111 S SD  . MET A 1 139 ? 46.590 21.527  -21.168 1.00 69.26  ? 138 MET A SD  1 
ATOM   1112 C CE  . MET A 1 139 ? 47.358 20.473  -22.383 1.00 42.06  ? 138 MET A CE  1 
ATOM   1113 N N   . ALA A 1 140 ? 43.324 17.794  -18.904 1.00 31.56  ? 139 ALA A N   1 
ATOM   1114 C CA  . ALA A 1 140 ? 42.578 16.539  -18.947 1.00 32.51  ? 139 ALA A CA  1 
ATOM   1115 C C   . ALA A 1 140 ? 41.440 16.633  -19.951 1.00 34.00  ? 139 ALA A C   1 
ATOM   1116 O O   . ALA A 1 140 ? 41.287 15.778  -20.830 1.00 31.42  ? 139 ALA A O   1 
ATOM   1117 C CB  . ALA A 1 140 ? 42.042 16.194  -17.557 1.00 31.28  ? 139 ALA A CB  1 
ATOM   1118 N N   . ALA A 1 141 ? 40.636 17.690  -19.842 1.00 31.99  ? 140 ALA A N   1 
ATOM   1119 C CA  . ALA A 1 141 ? 39.544 17.894  -20.779 1.00 31.25  ? 140 ALA A CA  1 
ATOM   1120 C C   . ALA A 1 141 ? 40.034 17.976  -22.224 1.00 33.58  ? 140 ALA A C   1 
ATOM   1121 O O   . ALA A 1 141 ? 39.280 17.644  -23.147 1.00 29.63  ? 140 ALA A O   1 
ATOM   1122 C CB  . ALA A 1 141 ? 38.782 19.150  -20.386 1.00 25.70  ? 140 ALA A CB  1 
ATOM   1123 N N   . GLN A 1 142 ? 41.295 18.382  -22.440 1.00 33.91  ? 141 GLN A N   1 
ATOM   1124 C CA  . GLN A 1 142 ? 41.830 18.453  -23.804 1.00 37.95  ? 141 GLN A CA  1 
ATOM   1125 C C   . GLN A 1 142 ? 41.921 17.071  -24.447 1.00 37.99  ? 141 GLN A C   1 
ATOM   1126 O O   . GLN A 1 142 ? 41.748 16.941  -25.665 1.00 38.66  ? 141 GLN A O   1 
ATOM   1127 C CB  . GLN A 1 142 ? 43.204 19.123  -23.810 1.00 36.86  ? 141 GLN A CB  1 
ATOM   1128 C CG  . GLN A 1 142 ? 43.180 20.641  -23.639 1.00 40.70  ? 141 GLN A CG  1 
ATOM   1129 C CD  . GLN A 1 142 ? 42.665 21.365  -24.851 1.00 49.96  ? 141 GLN A CD  1 
ATOM   1130 O OE1 . GLN A 1 142 ? 42.575 20.793  -25.949 1.00 60.81  ? 141 GLN A OE1 1 
ATOM   1131 N NE2 . GLN A 1 142 ? 42.315 22.636  -24.671 1.00 49.03  ? 141 GLN A NE2 1 
ATOM   1132 N N   . ILE A 1 143 ? 42.193 16.030  -23.658 1.00 33.47  ? 142 ILE A N   1 
ATOM   1133 C CA  . ILE A 1 143 ? 42.152 14.678  -24.208 1.00 34.37  ? 142 ILE A CA  1 
ATOM   1134 C C   . ILE A 1 143 ? 40.743 14.355  -24.668 1.00 34.40  ? 142 ILE A C   1 
ATOM   1135 O O   . ILE A 1 143 ? 40.522 13.873  -25.788 1.00 36.18  ? 142 ILE A O   1 
ATOM   1136 C CB  . ILE A 1 143 ? 42.644 13.657  -23.169 1.00 33.20  ? 142 ILE A CB  1 
ATOM   1137 C CG1 . ILE A 1 143 ? 44.035 14.037  -22.676 1.00 30.29  ? 142 ILE A CG1 1 
ATOM   1138 C CG2 . ILE A 1 143 ? 42.623 12.258  -23.769 1.00 30.01  ? 142 ILE A CG2 1 
ATOM   1139 C CD1 . ILE A 1 143 ? 44.459 13.285  -21.449 1.00 33.50  ? 142 ILE A CD1 1 
ATOM   1140 N N   . THR A 1 144 ? 39.763 14.630  -23.804 1.00 30.80  ? 143 THR A N   1 
ATOM   1141 C CA  . THR A 1 144 ? 38.373 14.404  -24.168 1.00 32.16  ? 143 THR A CA  1 
ATOM   1142 C C   . THR A 1 144 ? 37.994 15.183  -25.421 1.00 29.52  ? 143 THR A C   1 
ATOM   1143 O O   . THR A 1 144 ? 37.309 14.654  -26.304 1.00 32.01  ? 143 THR A O   1 
ATOM   1144 C CB  . THR A 1 144 ? 37.470 14.787  -23.005 1.00 30.86  ? 143 THR A CB  1 
ATOM   1145 O OG1 . THR A 1 144 ? 37.716 13.895  -21.909 1.00 25.85  ? 143 THR A OG1 1 
ATOM   1146 C CG2 . THR A 1 144 ? 35.991 14.709  -23.439 1.00 28.23  ? 143 THR A CG2 1 
ATOM   1147 N N   . LYS A 1 145 ? 38.465 16.428  -25.539 1.00 31.11  ? 144 LYS A N   1 
ATOM   1148 C CA  . LYS A 1 145 ? 38.099 17.235  -26.702 1.00 35.89  ? 144 LYS A CA  1 
ATOM   1149 C C   . LYS A 1 145 ? 38.571 16.593  -27.999 1.00 33.72  ? 144 LYS A C   1 
ATOM   1150 O O   . LYS A 1 145 ? 37.811 16.524  -28.971 1.00 31.79  ? 144 LYS A O   1 
ATOM   1151 C CB  . LYS A 1 145 ? 38.665 18.647  -26.587 1.00 36.72  ? 144 LYS A CB  1 
ATOM   1152 C CG  . LYS A 1 145 ? 38.006 19.603  -27.565 1.00 33.42  ? 144 LYS A CG  1 
ATOM   1153 C CD  . LYS A 1 145 ? 38.992 20.551  -28.170 1.00 42.13  ? 144 LYS A CD  1 
ATOM   1154 C CE  . LYS A 1 145 ? 38.880 21.925  -27.572 1.00 39.96  ? 144 LYS A CE  1 
ATOM   1155 N NZ  . LYS A 1 145 ? 39.951 22.784  -28.120 1.00 42.97  ? 144 LYS A NZ  1 
ATOM   1156 N N   . ARG A 1 146 ? 39.823 16.116  -28.029 1.00 36.66  ? 145 ARG A N   1 
ATOM   1157 C CA  . ARG A 1 146 ? 40.354 15.458  -29.225 1.00 39.03  ? 145 ARG A CA  1 
ATOM   1158 C C   . ARG A 1 146 ? 39.578 14.188  -29.563 1.00 34.11  ? 145 ARG A C   1 
ATOM   1159 O O   . ARG A 1 146 ? 39.317 13.915  -30.740 1.00 37.76  ? 145 ARG A O   1 
ATOM   1160 C CB  . ARG A 1 146 ? 41.836 15.136  -29.033 1.00 39.73  ? 145 ARG A CB  1 
ATOM   1161 C CG  . ARG A 1 146 ? 42.735 16.334  -29.196 1.00 37.26  ? 145 ARG A CG  1 
ATOM   1162 C CD  . ARG A 1 146 ? 44.194 15.931  -29.153 1.00 42.93  ? 145 ARG A CD  1 
ATOM   1163 N NE  . ARG A 1 146 ? 44.570 15.497  -27.811 1.00 50.06  ? 145 ARG A NE  1 
ATOM   1164 C CZ  . ARG A 1 146 ? 45.068 16.298  -26.876 1.00 41.60  ? 145 ARG A CZ  1 
ATOM   1165 N NH1 . ARG A 1 146 ? 45.261 17.582  -27.129 1.00 43.14  ? 145 ARG A NH1 1 
ATOM   1166 N NH2 . ARG A 1 146 ? 45.368 15.812  -25.680 1.00 43.62  ? 145 ARG A NH2 1 
ATOM   1167 N N   . LYS A 1 147 ? 39.212 13.394  -28.545 1.00 36.77  ? 146 LYS A N   1 
ATOM   1168 C CA  . LYS A 1 147 ? 38.371 12.221  -28.779 1.00 32.16  ? 146 LYS A CA  1 
ATOM   1169 C C   . LYS A 1 147 ? 37.068 12.621  -29.452 1.00 33.30  ? 146 LYS A C   1 
ATOM   1170 O O   . LYS A 1 147 ? 36.599 11.949  -30.375 1.00 37.75  ? 146 LYS A O   1 
ATOM   1171 C CB  . LYS A 1 147 ? 38.056 11.505  -27.465 1.00 28.54  ? 146 LYS A CB  1 
ATOM   1172 C CG  . LYS A 1 147 ? 39.187 10.755  -26.777 1.00 34.61  ? 146 LYS A CG  1 
ATOM   1173 C CD  . LYS A 1 147 ? 38.619 9.981   -25.563 1.00 28.41  ? 146 LYS A CD  1 
ATOM   1174 C CE  . LYS A 1 147 ? 39.691 9.178   -24.838 1.00 34.70  ? 146 LYS A CE  1 
ATOM   1175 N NZ  . LYS A 1 147 ? 39.104 8.129   -23.921 1.00 34.46  ? 146 LYS A NZ  1 
ATOM   1176 N N   . TRP A 1 148 ? 36.454 13.702  -28.968 1.00 31.68  ? 147 TRP A N   1 
ATOM   1177 C CA  . TRP A 1 148 ? 35.116 14.089  -29.388 1.00 31.01  ? 147 TRP A CA  1 
ATOM   1178 C C   . TRP A 1 148 ? 35.126 14.739  -30.773 1.00 33.38  ? 147 TRP A C   1 
ATOM   1179 O O   . TRP A 1 148 ? 34.121 14.681  -31.493 1.00 30.62  ? 147 TRP A O   1 
ATOM   1180 C CB  . TRP A 1 148 ? 34.497 15.019  -28.330 1.00 26.18  ? 147 TRP A CB  1 
ATOM   1181 C CG  . TRP A 1 148 ? 33.918 14.293  -27.125 1.00 28.40  ? 147 TRP A CG  1 
ATOM   1182 C CD1 . TRP A 1 148 ? 34.046 12.965  -26.830 1.00 26.91  ? 147 TRP A CD1 1 
ATOM   1183 C CD2 . TRP A 1 148 ? 33.107 14.859  -26.067 1.00 29.07  ? 147 TRP A CD2 1 
ATOM   1184 N NE1 . TRP A 1 148 ? 33.373 12.670  -25.665 1.00 25.64  ? 147 TRP A NE1 1 
ATOM   1185 C CE2 . TRP A 1 148 ? 32.789 13.811  -25.179 1.00 24.97  ? 147 TRP A CE2 1 
ATOM   1186 C CE3 . TRP A 1 148 ? 32.622 16.148  -25.793 1.00 26.71  ? 147 TRP A CE3 1 
ATOM   1187 C CZ2 . TRP A 1 148 ? 32.022 14.008  -24.033 1.00 23.82  ? 147 TRP A CZ2 1 
ATOM   1188 C CZ3 . TRP A 1 148 ? 31.861 16.348  -24.654 1.00 24.69  ? 147 TRP A CZ3 1 
ATOM   1189 C CH2 . TRP A 1 148 ? 31.560 15.279  -23.790 1.00 29.20  ? 147 TRP A CH2 1 
ATOM   1190 N N   . GLU A 1 149 ? 36.252 15.347  -31.160 1.00 35.99  ? 148 GLU A N   1 
ATOM   1191 C CA  . GLU A 1 149 ? 36.416 15.821  -32.532 1.00 36.16  ? 148 GLU A CA  1 
ATOM   1192 C C   . GLU A 1 149 ? 36.537 14.666  -33.520 1.00 37.57  ? 148 GLU A C   1 
ATOM   1193 O O   . GLU A 1 149 ? 36.073 14.781  -34.663 1.00 39.63  ? 148 GLU A O   1 
ATOM   1194 C CB  . GLU A 1 149 ? 37.642 16.731  -32.627 1.00 35.28  ? 148 GLU A CB  1 
ATOM   1195 C CG  . GLU A 1 149 ? 37.400 18.128  -32.075 1.00 32.28  ? 148 GLU A CG  1 
ATOM   1196 C CD  . GLU A 1 149 ? 38.664 18.796  -31.571 1.00 37.29  ? 148 GLU A CD  1 
ATOM   1197 O OE1 . GLU A 1 149 ? 38.644 20.027  -31.392 1.00 39.91  ? 148 GLU A OE1 1 
ATOM   1198 O OE2 . GLU A 1 149 ? 39.681 18.105  -31.349 1.00 42.92  ? 148 GLU A OE2 1 
ATOM   1199 N N   . ALA A 1 150 ? 37.144 13.548  -33.103 1.00 33.89  ? 149 ALA A N   1 
ATOM   1200 C CA  . ALA A 1 150 ? 37.270 12.383  -33.971 1.00 32.65  ? 149 ALA A CA  1 
ATOM   1201 C C   . ALA A 1 150 ? 35.970 11.604  -34.124 1.00 42.07  ? 149 ALA A C   1 
ATOM   1202 O O   . ALA A 1 150 ? 35.806 10.909  -35.131 1.00 39.04  ? 149 ALA A O   1 
ATOM   1203 C CB  . ALA A 1 150 ? 38.359 11.439  -33.447 1.00 33.74  ? 149 ALA A CB  1 
ATOM   1204 N N   . VAL A 1 151 ? 35.046 11.681  -33.163 1.00 40.24  ? 150 VAL A N   1 
ATOM   1205 C CA  . VAL A 1 151 ? 33.847 10.850  -33.219 1.00 34.14  ? 150 VAL A CA  1 
ATOM   1206 C C   . VAL A 1 151 ? 32.586 11.678  -33.466 1.00 31.73  ? 150 VAL A C   1 
ATOM   1207 O O   . VAL A 1 151 ? 31.482 11.214  -33.175 1.00 28.55  ? 150 VAL A O   1 
ATOM   1208 C CB  . VAL A 1 151 ? 33.700 9.977   -31.963 1.00 34.94  ? 150 VAL A CB  1 
ATOM   1209 C CG1 . VAL A 1 151 ? 34.912 9.072   -31.805 1.00 35.47  ? 150 VAL A CG1 1 
ATOM   1210 C CG2 . VAL A 1 151 ? 33.471 10.847  -30.709 1.00 34.74  ? 150 VAL A CG2 1 
ATOM   1211 N N   . HIS A 1 152 ? 32.737 12.888  -34.013 1.00 31.74  ? 151 HIS A N   1 
ATOM   1212 C CA  . HIS A 1 152 ? 31.599 13.734  -34.400 1.00 33.02  ? 151 HIS A CA  1 
ATOM   1213 C C   . HIS A 1 152 ? 30.645 13.954  -33.233 1.00 32.37  ? 151 HIS A C   1 
ATOM   1214 O O   . HIS A 1 152 ? 29.422 13.857  -33.379 1.00 30.86  ? 151 HIS A O   1 
ATOM   1215 C CB  . HIS A 1 152 ? 30.845 13.143  -35.596 1.00 36.64  ? 151 HIS A CB  1 
ATOM   1216 C CG  . HIS A 1 152 ? 31.738 12.628  -36.679 1.00 41.83  ? 151 HIS A CG  1 
ATOM   1217 N ND1 . HIS A 1 152 ? 32.073 11.294  -36.797 1.00 43.25  ? 151 HIS A ND1 1 
ATOM   1218 C CD2 . HIS A 1 152 ? 32.371 13.266  -37.692 1.00 43.14  ? 151 HIS A CD2 1 
ATOM   1219 C CE1 . HIS A 1 152 ? 32.876 11.135  -37.833 1.00 38.35  ? 151 HIS A CE1 1 
ATOM   1220 N NE2 . HIS A 1 152 ? 33.075 12.316  -38.391 1.00 42.84  ? 151 HIS A NE2 1 
ATOM   1221 N N   . ALA A 1 153 ? 31.208 14.234  -32.052 1.00 30.35  ? 152 ALA A N   1 
ATOM   1222 C CA  . ALA A 1 153 ? 30.367 14.481  -30.889 1.00 27.52  ? 152 ALA A CA  1 
ATOM   1223 C C   . ALA A 1 153 ? 29.482 15.710  -31.094 1.00 26.25  ? 152 ALA A C   1 
ATOM   1224 O O   . ALA A 1 153 ? 28.282 15.682  -30.786 1.00 24.08  ? 152 ALA A O   1 
ATOM   1225 C CB  . ALA A 1 153 ? 31.234 14.632  -29.638 1.00 29.36  ? 152 ALA A CB  1 
ATOM   1226 N N   . ALA A 1 154 ? 30.050 16.798  -31.626 1.00 26.59  ? 153 ALA A N   1 
ATOM   1227 C CA  . ALA A 1 154 ? 29.292 18.048  -31.729 1.00 25.90  ? 153 ALA A CA  1 
ATOM   1228 C C   . ALA A 1 154 ? 28.051 17.865  -32.591 1.00 26.99  ? 153 ALA A C   1 
ATOM   1229 O O   . ALA A 1 154 ? 26.941 18.259  -32.204 1.00 26.94  ? 153 ALA A O   1 
ATOM   1230 C CB  . ALA A 1 154 ? 30.181 19.160  -32.282 1.00 25.81  ? 153 ALA A CB  1 
ATOM   1231 N N   . GLU A 1 155 ? 28.216 17.226  -33.755 1.00 29.18  ? 154 GLU A N   1 
ATOM   1232 C CA  . GLU A 1 155 ? 27.077 16.985  -34.635 1.00 29.52  ? 154 GLU A CA  1 
ATOM   1233 C C   . GLU A 1 155 ? 26.027 16.115  -33.949 1.00 24.93  ? 154 GLU A C   1 
ATOM   1234 O O   . GLU A 1 155 ? 24.821 16.381  -34.050 1.00 25.16  ? 154 GLU A O   1 
ATOM   1235 C CB  . GLU A 1 155 ? 27.553 16.344  -35.952 1.00 28.99  ? 154 GLU A CB  1 
ATOM   1236 C CG  . GLU A 1 155 ? 26.426 16.211  -36.976 1.00 31.47  ? 154 GLU A CG  1 
ATOM   1237 C CD  . GLU A 1 155 ? 26.866 15.723  -38.359 1.00 40.24  ? 154 GLU A CD  1 
ATOM   1238 O OE1 . GLU A 1 155 ? 28.087 15.565  -38.606 1.00 40.03  ? 154 GLU A OE1 1 
ATOM   1239 O OE2 . GLU A 1 155 ? 25.965 15.479  -39.199 1.00 42.13  ? 154 GLU A OE2 1 
ATOM   1240 N N   . GLN A 1 156 ? 26.465 15.073  -33.238 1.00 29.01  ? 155 GLN A N   1 
ATOM   1241 C CA  . GLN A 1 156 ? 25.522 14.221  -32.513 1.00 26.60  ? 155 GLN A CA  1 
ATOM   1242 C C   . GLN A 1 156 ? 24.710 15.025  -31.492 1.00 28.54  ? 155 GLN A C   1 
ATOM   1243 O O   . GLN A 1 156 ? 23.498 14.811  -31.343 1.00 24.35  ? 155 GLN A O   1 
ATOM   1244 C CB  . GLN A 1 156 ? 26.272 13.068  -31.832 1.00 23.42  ? 155 GLN A CB  1 
ATOM   1245 C CG  . GLN A 1 156 ? 25.345 11.990  -31.270 1.00 25.77  ? 155 GLN A CG  1 
ATOM   1246 C CD  . GLN A 1 156 ? 24.794 11.080  -32.376 1.00 33.79  ? 155 GLN A CD  1 
ATOM   1247 O OE1 . GLN A 1 156 ? 25.539 10.640  -33.252 1.00 31.98  ? 155 GLN A OE1 1 
ATOM   1248 N NE2 . GLN A 1 156 ? 23.488 10.804  -32.338 1.00 31.14  ? 155 GLN A NE2 1 
ATOM   1249 N N   . ARG A 1 157 ? 25.356 15.952  -30.773 1.00 27.80  ? 156 ARG A N   1 
ATOM   1250 C CA  . ARG A 1 157 ? 24.604 16.780  -29.832 1.00 27.56  ? 156 ARG A CA  1 
ATOM   1251 C C   . ARG A 1 157 ? 23.690 17.743  -30.577 1.00 25.12  ? 156 ARG A C   1 
ATOM   1252 O O   . ARG A 1 157 ? 22.506 17.874  -30.240 1.00 23.50  ? 156 ARG A O   1 
ATOM   1253 C CB  . ARG A 1 157 ? 25.554 17.543  -28.892 1.00 23.72  ? 156 ARG A CB  1 
ATOM   1254 C CG  . ARG A 1 157 ? 26.504 16.637  -28.083 1.00 24.92  ? 156 ARG A CG  1 
ATOM   1255 C CD  . ARG A 1 157 ? 25.825 15.963  -26.858 1.00 22.63  ? 156 ARG A CD  1 
ATOM   1256 N NE  . ARG A 1 157 ? 25.081 14.743  -27.188 1.00 27.67  ? 156 ARG A NE  1 
ATOM   1257 C CZ  . ARG A 1 157 ? 25.648 13.560  -27.463 1.00 30.18  ? 156 ARG A CZ  1 
ATOM   1258 N NH1 . ARG A 1 157 ? 26.976 13.423  -27.461 1.00 23.52  ? 156 ARG A NH1 1 
ATOM   1259 N NH2 . ARG A 1 157 ? 24.883 12.514  -27.761 1.00 24.96  ? 156 ARG A NH2 1 
ATOM   1260 N N   . ARG A 1 158 ? 24.223 18.416  -31.609 1.00 25.45  ? 157 ARG A N   1 
ATOM   1261 C CA  . ARG A 1 158 ? 23.433 19.417  -32.333 1.00 26.58  ? 157 ARG A CA  1 
ATOM   1262 C C   . ARG A 1 158 ? 22.194 18.806  -32.984 1.00 31.31  ? 157 ARG A C   1 
ATOM   1263 O O   . ARG A 1 158 ? 21.145 19.461  -33.063 1.00 35.01  ? 157 ARG A O   1 
ATOM   1264 C CB  . ARG A 1 158 ? 24.301 20.120  -33.383 1.00 28.36  ? 157 ARG A CB  1 
ATOM   1265 C CG  . ARG A 1 158 ? 23.503 20.969  -34.374 1.00 36.15  ? 157 ARG A CG  1 
ATOM   1266 C CD  . ARG A 1 158 ? 24.370 21.875  -35.254 1.00 37.63  ? 157 ARG A CD  1 
ATOM   1267 N NE  . ARG A 1 158 ? 25.403 21.161  -36.011 1.00 36.74  ? 157 ARG A NE  1 
ATOM   1268 C CZ  . ARG A 1 158 ? 25.185 20.440  -37.105 1.00 43.93  ? 157 ARG A CZ  1 
ATOM   1269 N NH1 . ARG A 1 158 ? 23.952 20.318  -37.591 1.00 47.51  ? 157 ARG A NH1 1 
ATOM   1270 N NH2 . ARG A 1 158 ? 26.211 19.840  -37.715 1.00 41.58  ? 157 ARG A NH2 1 
ATOM   1271 N N   . VAL A 1 159 ? 22.271 17.555  -33.437 1.00 24.99  ? 158 VAL A N   1 
ATOM   1272 C CA  . VAL A 1 159 ? 21.081 16.944  -34.022 1.00 25.91  ? 158 VAL A CA  1 
ATOM   1273 C C   . VAL A 1 159 ? 19.980 16.816  -32.980 1.00 27.38  ? 158 VAL A C   1 
ATOM   1274 O O   . VAL A 1 159 ? 18.790 16.989  -33.282 1.00 28.73  ? 158 VAL A O   1 
ATOM   1275 C CB  . VAL A 1 159 ? 21.433 15.590  -34.666 1.00 30.76  ? 158 VAL A CB  1 
ATOM   1276 C CG1 . VAL A 1 159 ? 20.159 14.813  -35.025 1.00 29.30  ? 158 VAL A CG1 1 
ATOM   1277 C CG2 . VAL A 1 159 ? 22.281 15.833  -35.921 1.00 32.78  ? 158 VAL A CG2 1 
ATOM   1278 N N   . TYR A 1 160 ? 20.346 16.519  -31.735 1.00 24.26  ? 159 TYR A N   1 
ATOM   1279 C CA  . TYR A 1 160 ? 19.320 16.454  -30.705 1.00 21.02  ? 159 TYR A CA  1 
ATOM   1280 C C   . TYR A 1 160 ? 18.852 17.854  -30.323 1.00 23.35  ? 159 TYR A C   1 
ATOM   1281 O O   . TYR A 1 160 ? 17.648 18.106  -30.219 1.00 26.07  ? 159 TYR A O   1 
ATOM   1282 C CB  . TYR A 1 160 ? 19.847 15.683  -29.478 1.00 23.70  ? 159 TYR A CB  1 
ATOM   1283 C CG  . TYR A 1 160 ? 19.012 15.863  -28.225 1.00 19.86  ? 159 TYR A CG  1 
ATOM   1284 C CD1 . TYR A 1 160 ? 17.855 15.123  -28.029 1.00 21.34  ? 159 TYR A CD1 1 
ATOM   1285 C CD2 . TYR A 1 160 ? 19.362 16.809  -27.258 1.00 22.08  ? 159 TYR A CD2 1 
ATOM   1286 C CE1 . TYR A 1 160 ? 17.066 15.296  -26.880 1.00 25.23  ? 159 TYR A CE1 1 
ATOM   1287 C CE2 . TYR A 1 160 ? 18.598 16.974  -26.089 1.00 23.70  ? 159 TYR A CE2 1 
ATOM   1288 C CZ  . TYR A 1 160 ? 17.455 16.220  -25.911 1.00 23.59  ? 159 TYR A CZ  1 
ATOM   1289 O OH  . TYR A 1 160 ? 16.686 16.394  -24.780 1.00 24.16  ? 159 TYR A OH  1 
ATOM   1290 N N   . LEU A 1 161 ? 19.795 18.777  -30.110 1.00 25.01  ? 160 LEU A N   1 
ATOM   1291 C CA  . LEU A 1 161 ? 19.455 20.106  -29.599 1.00 27.53  ? 160 LEU A CA  1 
ATOM   1292 C C   . LEU A 1 161 ? 18.542 20.863  -30.565 1.00 30.60  ? 160 LEU A C   1 
ATOM   1293 O O   . LEU A 1 161 ? 17.548 21.474  -30.151 1.00 31.66  ? 160 LEU A O   1 
ATOM   1294 C CB  . LEU A 1 161 ? 20.737 20.895  -29.334 1.00 23.95  ? 160 LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 161 ? 21.604 20.285  -28.227 1.00 26.27  ? 160 LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 161 ? 22.972 20.942  -28.148 1.00 25.94  ? 160 LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 161 ? 20.866 20.381  -26.891 1.00 22.52  ? 160 LEU A CD2 1 
ATOM   1298 N N   . GLU A 1 162 ? 18.862 20.825  -31.860 1.00 31.07  ? 161 GLU A N   1 
ATOM   1299 C CA  . GLU A 1 162 ? 18.038 21.460  -32.884 1.00 33.22  ? 161 GLU A CA  1 
ATOM   1300 C C   . GLU A 1 162 ? 16.836 20.619  -33.302 1.00 35.26  ? 161 GLU A C   1 
ATOM   1301 O O   . GLU A 1 162 ? 15.934 21.155  -33.961 1.00 36.66  ? 161 GLU A O   1 
ATOM   1302 C CB  . GLU A 1 162 ? 18.896 21.781  -34.118 1.00 32.68  ? 161 GLU A CB  1 
ATOM   1303 C CG  . GLU A 1 162 ? 20.016 22.780  -33.840 1.00 33.63  ? 161 GLU A CG  1 
ATOM   1304 C CD  . GLU A 1 162 ? 20.884 23.069  -35.059 1.00 35.28  ? 161 GLU A CD  1 
ATOM   1305 O OE1 . GLU A 1 162 ? 21.484 24.160  -35.112 1.00 40.12  ? 161 GLU A OE1 1 
ATOM   1306 O OE2 . GLU A 1 162 ? 20.989 22.208  -35.956 1.00 36.49  ? 161 GLU A OE2 1 
ATOM   1307 N N   . GLY A 1 163 ? 16.788 19.330  -32.943 1.00 29.44  ? 162 GLY A N   1 
ATOM   1308 C CA  . GLY A 1 163 ? 15.694 18.483  -33.380 1.00 28.46  ? 162 GLY A CA  1 
ATOM   1309 C C   . GLY A 1 163 ? 14.753 17.973  -32.300 1.00 30.67  ? 162 GLY A C   1 
ATOM   1310 O O   . GLY A 1 163 ? 13.778 18.644  -31.944 1.00 31.87  ? 162 GLY A O   1 
ATOM   1311 N N   . ARG A 1 164 ? 15.031 16.765  -31.798 1.00 28.22  ? 163 ARG A N   1 
ATOM   1312 C CA  . ARG A 1 164 ? 14.204 16.127  -30.777 1.00 25.91  ? 163 ARG A CA  1 
ATOM   1313 C C   . ARG A 1 164 ? 13.917 17.065  -29.603 1.00 24.17  ? 163 ARG A C   1 
ATOM   1314 O O   . ARG A 1 164 ? 12.780 17.168  -29.132 1.00 26.09  ? 163 ARG A O   1 
ATOM   1315 C CB  . ARG A 1 164 ? 14.915 14.860  -30.288 1.00 25.72  ? 163 ARG A CB  1 
ATOM   1316 C CG  . ARG A 1 164 ? 14.083 13.959  -29.413 1.00 27.80  ? 163 ARG A CG  1 
ATOM   1317 C CD  . ARG A 1 164 ? 14.923 12.856  -28.775 1.00 27.09  ? 163 ARG A CD  1 
ATOM   1318 N NE  . ARG A 1 164 ? 15.658 12.028  -29.736 1.00 28.80  ? 163 ARG A NE  1 
ATOM   1319 C CZ  . ARG A 1 164 ? 16.608 11.155  -29.391 1.00 34.49  ? 163 ARG A CZ  1 
ATOM   1320 N NH1 . ARG A 1 164 ? 16.949 11.005  -28.106 1.00 25.41  ? 163 ARG A NH1 1 
ATOM   1321 N NH2 . ARG A 1 164 ? 17.223 10.429  -30.320 1.00 28.65  ? 163 ARG A NH2 1 
ATOM   1322 N N   . CYS A 1 165 ? 14.957 17.736  -29.105 1.00 24.15  ? 164 CYS A N   1 
ATOM   1323 C CA  . CYS A 1 165 ? 14.817 18.671  -27.984 1.00 26.39  ? 164 CYS A CA  1 
ATOM   1324 C C   . CYS A 1 165 ? 13.714 19.700  -28.230 1.00 26.22  ? 164 CYS A C   1 
ATOM   1325 O O   . CYS A 1 165 ? 12.806 19.863  -27.407 1.00 23.89  ? 164 CYS A O   1 
ATOM   1326 C CB  . CYS A 1 165 ? 16.157 19.378  -27.729 1.00 25.76  ? 164 CYS A CB  1 
ATOM   1327 S SG  . CYS A 1 165 ? 16.193 20.383  -26.165 1.00 30.27  ? 164 CYS A SG  1 
ATOM   1328 N N   . VAL A 1 166 ? 13.793 20.418  -29.355 1.00 27.08  ? 165 VAL A N   1 
ATOM   1329 C CA  . VAL A 1 166 ? 12.793 21.429  -29.698 1.00 26.76  ? 165 VAL A CA  1 
ATOM   1330 C C   . VAL A 1 166 ? 11.411 20.802  -29.852 1.00 29.92  ? 165 VAL A C   1 
ATOM   1331 O O   . VAL A 1 166 ? 10.401 21.367  -29.413 1.00 33.30  ? 165 VAL A O   1 
ATOM   1332 C CB  . VAL A 1 166 ? 13.222 22.159  -30.984 1.00 32.63  ? 165 VAL A CB  1 
ATOM   1333 C CG1 . VAL A 1 166 ? 12.136 23.061  -31.500 1.00 34.81  ? 165 VAL A CG1 1 
ATOM   1334 C CG2 . VAL A 1 166 ? 14.507 22.934  -30.762 1.00 30.61  ? 165 VAL A CG2 1 
ATOM   1335 N N   . ASP A 1 167 ? 11.342 19.621  -30.470 1.00 29.86  ? 166 ASP A N   1 
ATOM   1336 C CA  . ASP A 1 167 ? 10.045 18.997  -30.705 1.00 31.06  ? 166 ASP A CA  1 
ATOM   1337 C C   . ASP A 1 167 ? 9.421  18.506  -29.404 1.00 29.04  ? 166 ASP A C   1 
ATOM   1338 O O   . ASP A 1 167 ? 8.201  18.589  -29.227 1.00 29.98  ? 166 ASP A O   1 
ATOM   1339 C CB  . ASP A 1 167 ? 10.173 17.848  -31.723 1.00 36.05  ? 166 ASP A CB  1 
ATOM   1340 C CG  . ASP A 1 167 ? 8.848  17.083  -31.931 1.00 41.03  ? 166 ASP A CG  1 
ATOM   1341 O OD1 . ASP A 1 167 ? 7.867  17.678  -32.439 1.00 46.20  ? 166 ASP A OD1 1 
ATOM   1342 O OD2 . ASP A 1 167 ? 8.780  15.886  -31.563 1.00 43.53  ? 166 ASP A OD2 1 
ATOM   1343 N N   . GLY A 1 168 ? 10.228 17.978  -28.481 1.00 27.37  ? 167 GLY A N   1 
ATOM   1344 C CA  . GLY A 1 168 ? 9.681  17.635  -27.180 1.00 29.31  ? 167 GLY A CA  1 
ATOM   1345 C C   . GLY A 1 168 ? 9.214  18.861  -26.406 1.00 26.23  ? 167 GLY A C   1 
ATOM   1346 O O   . GLY A 1 168 ? 8.177  18.831  -25.740 1.00 27.10  ? 167 GLY A O   1 
ATOM   1347 N N   . LEU A 1 169 ? 9.984  19.950  -26.473 1.00 27.59  ? 168 LEU A N   1 
ATOM   1348 C CA  . LEU A 1 169 ? 9.621  21.157  -25.736 1.00 31.32  ? 168 LEU A CA  1 
ATOM   1349 C C   . LEU A 1 169 ? 8.260  21.669  -26.181 1.00 31.47  ? 168 LEU A C   1 
ATOM   1350 O O   . LEU A 1 169 ? 7.405  21.973  -25.341 1.00 28.45  ? 168 LEU A O   1 
ATOM   1351 C CB  . LEU A 1 169 ? 10.699 22.229  -25.911 1.00 24.69  ? 168 LEU A CB  1 
ATOM   1352 C CG  . LEU A 1 169 ? 10.524 23.577  -25.184 1.00 31.36  ? 168 LEU A CG  1 
ATOM   1353 C CD1 . LEU A 1 169 ? 10.055 23.411  -23.743 1.00 22.03  ? 168 LEU A CD1 1 
ATOM   1354 C CD2 . LEU A 1 169 ? 11.820 24.376  -25.235 1.00 25.83  ? 168 LEU A CD2 1 
ATOM   1355 N N   . ARG A 1 170 ? 8.019  21.700  -27.502 1.00 27.85  ? 169 ARG A N   1 
ATOM   1356 C CA  . ARG A 1 170 ? 6.721  22.138  -28.021 1.00 30.61  ? 169 ARG A CA  1 
ATOM   1357 C C   . ARG A 1 170 ? 5.590  21.252  -27.537 1.00 30.72  ? 169 ARG A C   1 
ATOM   1358 O O   . ARG A 1 170 ? 4.545  21.751  -27.100 1.00 32.17  ? 169 ARG A O   1 
ATOM   1359 C CB  . ARG A 1 170 ? 6.731  22.186  -29.546 1.00 30.74  ? 169 ARG A CB  1 
ATOM   1360 C CG  . ARG A 1 170 ? 7.707  23.190  -30.090 1.00 37.85  ? 169 ARG A CG  1 
ATOM   1361 C CD  . ARG A 1 170 ? 7.350  23.534  -31.530 1.00 47.05  ? 169 ARG A CD  1 
ATOM   1362 N NE  . ARG A 1 170 ? 7.733  22.431  -32.388 1.00 46.26  ? 169 ARG A NE  1 
ATOM   1363 C CZ  . ARG A 1 170 ? 8.513  22.529  -33.451 1.00 52.30  ? 169 ARG A CZ  1 
ATOM   1364 N NH1 . ARG A 1 170 ? 9.010  23.705  -33.827 1.00 54.72  ? 169 ARG A NH1 1 
ATOM   1365 N NH2 . ARG A 1 170 ? 8.795  21.427  -34.133 1.00 58.61  ? 169 ARG A NH2 1 
ATOM   1366 N N   . ARG A 1 171 ? 5.776  19.932  -27.605 1.00 28.19  ? 170 ARG A N   1 
ATOM   1367 C CA  . ARG A 1 171 ? 4.754  19.018  -27.107 1.00 29.07  ? 170 ARG A CA  1 
ATOM   1368 C C   . ARG A 1 171 ? 4.405  19.314  -25.646 1.00 31.64  ? 170 ARG A C   1 
ATOM   1369 O O   . ARG A 1 171 ? 3.227  19.396  -25.280 1.00 38.59  ? 170 ARG A O   1 
ATOM   1370 C CB  . ARG A 1 171 ? 5.237  17.576  -27.275 1.00 29.39  ? 170 ARG A CB  1 
ATOM   1371 C CG  . ARG A 1 171 ? 4.263  16.526  -26.771 1.00 26.52  ? 170 ARG A CG  1 
ATOM   1372 C CD  . ARG A 1 171 ? 4.914  15.143  -26.694 1.00 27.18  ? 170 ARG A CD  1 
ATOM   1373 N NE  . ARG A 1 171 ? 4.026  14.145  -26.090 1.00 29.69  ? 170 ARG A NE  1 
ATOM   1374 C CZ  . ARG A 1 171 ? 3.120  13.434  -26.760 1.00 30.42  ? 170 ARG A CZ  1 
ATOM   1375 N NH1 . ARG A 1 171 ? 2.362  12.543  -26.127 1.00 29.26  ? 170 ARG A NH1 1 
ATOM   1376 N NH2 . ARG A 1 171 ? 2.963  13.617  -28.067 1.00 33.20  ? 170 ARG A NH2 1 
ATOM   1377 N N   . TYR A 1 172 ? 5.425  19.475  -24.794 1.00 30.71  ? 171 TYR A N   1 
ATOM   1378 C CA  . TYR A 1 172 ? 5.191  19.730  -23.371 1.00 31.40  ? 171 TYR A CA  1 
ATOM   1379 C C   . TYR A 1 172 ? 4.531  21.089  -23.150 1.00 31.00  ? 171 TYR A C   1 
ATOM   1380 O O   . TYR A 1 172 ? 3.615  21.211  -22.333 1.00 26.39  ? 171 TYR A O   1 
ATOM   1381 C CB  . TYR A 1 172 ? 6.514  19.664  -22.600 1.00 31.97  ? 171 TYR A CB  1 
ATOM   1382 C CG  . TYR A 1 172 ? 7.277  18.348  -22.707 1.00 27.17  ? 171 TYR A CG  1 
ATOM   1383 C CD1 . TYR A 1 172 ? 6.622  17.154  -22.962 1.00 29.79  ? 171 TYR A CD1 1 
ATOM   1384 C CD2 . TYR A 1 172 ? 8.657  18.313  -22.545 1.00 29.59  ? 171 TYR A CD2 1 
ATOM   1385 C CE1 . TYR A 1 172 ? 7.322  15.959  -23.056 1.00 30.89  ? 171 TYR A CE1 1 
ATOM   1386 C CE2 . TYR A 1 172 ? 9.368  17.123  -22.627 1.00 27.57  ? 171 TYR A CE2 1 
ATOM   1387 C CZ  . TYR A 1 172 ? 8.691  15.948  -22.881 1.00 27.93  ? 171 TYR A CZ  1 
ATOM   1388 O OH  . TYR A 1 172 ? 9.387  14.769  -22.986 1.00 25.91  ? 171 TYR A OH  1 
ATOM   1389 N N   . LEU A 1 173 ? 4.999  22.121  -23.863 1.00 27.24  ? 172 LEU A N   1 
ATOM   1390 C CA  . LEU A 1 173 ? 4.371  23.437  -23.779 1.00 35.32  ? 172 LEU A CA  1 
ATOM   1391 C C   . LEU A 1 173 ? 2.894  23.384  -24.156 1.00 41.30  ? 172 LEU A C   1 
ATOM   1392 O O   . LEU A 1 173 ? 2.071  24.078  -23.547 1.00 41.80  ? 172 LEU A O   1 
ATOM   1393 C CB  . LEU A 1 173 ? 5.112  24.429  -24.671 1.00 31.99  ? 172 LEU A CB  1 
ATOM   1394 C CG  . LEU A 1 173 ? 6.427  24.914  -24.065 1.00 35.29  ? 172 LEU A CG  1 
ATOM   1395 C CD1 . LEU A 1 173 ? 7.219  25.705  -25.088 1.00 33.44  ? 172 LEU A CD1 1 
ATOM   1396 C CD2 . LEU A 1 173 ? 6.158  25.746  -22.818 1.00 38.90  ? 172 LEU A CD2 1 
ATOM   1397 N N   . GLU A 1 174 ? 2.541  22.571  -25.163 1.00 40.27  ? 173 GLU A N   1 
ATOM   1398 C CA  . GLU A 1 174 ? 1.137  22.372  -25.515 1.00 39.11  ? 173 GLU A CA  1 
ATOM   1399 C C   . GLU A 1 174 ? 0.413  21.577  -24.438 1.00 40.21  ? 173 GLU A C   1 
ATOM   1400 O O   . GLU A 1 174 ? -0.645 21.991  -23.945 1.00 38.65  ? 173 GLU A O   1 
ATOM   1401 C CB  . GLU A 1 174 ? 1.021  21.645  -26.860 1.00 39.90  ? 173 GLU A CB  1 
ATOM   1402 C CG  . GLU A 1 174 ? 0.551  22.494  -28.018 1.00 49.23  ? 173 GLU A CG  1 
ATOM   1403 C CD  . GLU A 1 174 ? -0.722 23.265  -27.710 1.00 49.12  ? 173 GLU A CD  1 
ATOM   1404 O OE1 . GLU A 1 174 ? -1.732 22.650  -27.289 1.00 43.53  ? 173 GLU A OE1 1 
ATOM   1405 O OE2 . GLU A 1 174 ? -0.694 24.503  -27.884 1.00 51.64  ? 173 GLU A OE2 1 
ATOM   1406 N N   . ASN A 1 175 ? 0.961  20.417  -24.073 1.00 37.62  ? 174 ASN A N   1 
ATOM   1407 C CA  . ASN A 1 175 ? 0.247  19.533  -23.152 1.00 39.34  ? 174 ASN A CA  1 
ATOM   1408 C C   . ASN A 1 175 ? 0.077  20.161  -21.772 1.00 41.03  ? 174 ASN A C   1 
ATOM   1409 O O   . ASN A 1 175 ? -0.907 19.877  -21.076 1.00 46.38  ? 174 ASN A O   1 
ATOM   1410 C CB  . ASN A 1 175 ? 0.974  18.190  -23.052 1.00 38.47  ? 174 ASN A CB  1 
ATOM   1411 C CG  . ASN A 1 175 ? 0.742  17.310  -24.282 1.00 40.60  ? 174 ASN A CG  1 
ATOM   1412 O OD1 . ASN A 1 175 ? -0.053 17.653  -25.162 1.00 42.95  ? 174 ASN A OD1 1 
ATOM   1413 N ND2 . ASN A 1 175 ? 1.434  16.181  -24.346 1.00 29.41  ? 174 ASN A ND2 1 
ATOM   1414 N N   . GLY A 1 176 ? 1.017  21.000  -21.350 1.00 37.77  ? 175 GLY A N   1 
ATOM   1415 C CA  . GLY A 1 176 ? 0.869  21.686  -20.081 1.00 43.74  ? 175 GLY A CA  1 
ATOM   1416 C C   . GLY A 1 176 ? 0.641  23.178  -20.242 1.00 48.31  ? 175 GLY A C   1 
ATOM   1417 O O   . GLY A 1 176 ? 1.175  23.972  -19.462 1.00 46.98  ? 175 GLY A O   1 
ATOM   1418 N N   . LYS A 1 177 ? -0.170 23.562  -21.239 1.00 44.10  ? 176 LYS A N   1 
ATOM   1419 C CA  . LYS A 1 177 ? -0.313 24.970  -21.608 1.00 48.50  ? 176 LYS A CA  1 
ATOM   1420 C C   . LYS A 1 177 ? -0.859 25.806  -20.452 1.00 50.45  ? 176 LYS A C   1 
ATOM   1421 O O   . LYS A 1 177 ? -0.394 26.927  -20.219 1.00 52.29  ? 176 LYS A O   1 
ATOM   1422 C CB  . LYS A 1 177 ? -1.223 25.105  -22.838 1.00 45.78  ? 176 LYS A CB  1 
ATOM   1423 C CG  . LYS A 1 177 ? -2.597 24.451  -22.692 1.00 52.12  ? 176 LYS A CG  1 
ATOM   1424 C CD  . LYS A 1 177 ? -3.231 24.153  -24.048 1.00 55.58  ? 176 LYS A CD  1 
ATOM   1425 C CE  . LYS A 1 177 ? -4.745 24.037  -23.952 1.00 57.56  ? 176 LYS A CE  1 
ATOM   1426 N NZ  . LYS A 1 177 ? -5.399 24.184  -25.290 1.00 60.61  ? 176 LYS A NZ  1 
ATOM   1427 N N   . GLU A 1 178 ? -1.833 25.274  -19.706 1.00 51.16  ? 177 GLU A N   1 
ATOM   1428 C CA  . GLU A 1 178 ? -2.500 26.052  -18.660 1.00 55.68  ? 177 GLU A CA  1 
ATOM   1429 C C   . GLU A 1 178 ? -1.523 26.570  -17.600 1.00 55.73  ? 177 GLU A C   1 
ATOM   1430 O O   . GLU A 1 178 ? -1.538 27.761  -17.271 1.00 60.22  ? 177 GLU A O   1 
ATOM   1431 C CB  . GLU A 1 178 ? -3.587 25.217  -17.995 1.00 58.37  ? 177 GLU A CB  1 
ATOM   1432 C CG  . GLU A 1 178 ? -4.665 24.579  -18.896 1.00 67.47  ? 177 GLU A CG  1 
ATOM   1433 C CD  . GLU A 1 178 ? -4.915 23.121  -18.513 1.00 78.73  ? 177 GLU A CD  1 
ATOM   1434 O OE1 . GLU A 1 178 ? -4.892 22.833  -17.295 1.00 82.44  ? 177 GLU A OE1 1 
ATOM   1435 O OE2 . GLU A 1 178 ? -5.155 22.273  -19.404 1.00 73.36  ? 177 GLU A OE2 1 
ATOM   1436 N N   . THR A 1 179 ? -0.607 25.709  -17.121 1.00 58.68  ? 178 THR A N   1 
ATOM   1437 C CA  . THR A 1 179 ? 0.430  26.098  -16.150 1.00 53.57  ? 178 THR A CA  1 
ATOM   1438 C C   . THR A 1 179 ? 1.716  26.667  -16.742 1.00 48.37  ? 178 THR A C   1 
ATOM   1439 O O   . THR A 1 179 ? 2.311  27.556  -16.128 1.00 49.20  ? 178 THR A O   1 
ATOM   1440 C CB  . THR A 1 179 ? 0.867  24.925  -15.260 1.00 51.25  ? 178 THR A CB  1 
ATOM   1441 O OG1 . THR A 1 179 ? 1.106  23.742  -16.042 1.00 58.81  ? 178 THR A OG1 1 
ATOM   1442 C CG2 . THR A 1 179 ? -0.094 24.693  -14.109 1.00 51.87  ? 178 THR A CG2 1 
ATOM   1443 N N   . LEU A 1 180 ? 2.212  26.148  -17.863 1.00 43.93  ? 179 LEU A N   1 
ATOM   1444 C CA  . LEU A 1 180 ? 3.542  26.543  -18.325 1.00 44.91  ? 179 LEU A CA  1 
ATOM   1445 C C   . LEU A 1 180 ? 3.555  27.923  -18.976 1.00 45.47  ? 179 LEU A C   1 
ATOM   1446 O O   . LEU A 1 180 ? 4.602  28.586  -19.011 1.00 41.54  ? 179 LEU A O   1 
ATOM   1447 C CB  . LEU A 1 180 ? 4.094  25.500  -19.298 1.00 40.60  ? 179 LEU A CB  1 
ATOM   1448 C CG  . LEU A 1 180 ? 4.260  24.110  -18.680 1.00 44.35  ? 179 LEU A CG  1 
ATOM   1449 C CD1 . LEU A 1 180 ? 4.433  23.060  -19.771 1.00 43.11  ? 179 LEU A CD1 1 
ATOM   1450 C CD2 . LEU A 1 180 ? 5.442  24.115  -17.710 1.00 36.62  ? 179 LEU A CD2 1 
ATOM   1451 N N   . GLN A 1 181 ? 2.424  28.376  -19.495 1.00 44.57  ? 180 GLN A N   1 
ATOM   1452 C CA  . GLN A 1 181 ? 2.376  29.682  -20.131 1.00 45.86  ? 180 GLN A CA  1 
ATOM   1453 C C   . GLN A 1 181 ? 2.027  30.802  -19.156 1.00 48.52  ? 180 GLN A C   1 
ATOM   1454 O O   . GLN A 1 181 ? 1.990  31.965  -19.566 1.00 53.09  ? 180 GLN A O   1 
ATOM   1455 C CB  . GLN A 1 181 ? 1.381  29.652  -21.296 1.00 52.68  ? 180 GLN A CB  1 
ATOM   1456 C CG  . GLN A 1 181 ? 1.745  28.632  -22.394 1.00 48.02  ? 180 GLN A CG  1 
ATOM   1457 C CD  . GLN A 1 181 ? 2.815  29.139  -23.340 1.00 48.27  ? 180 GLN A CD  1 
ATOM   1458 O OE1 . GLN A 1 181 ? 3.614  30.004  -22.985 1.00 50.52  ? 180 GLN A OE1 1 
ATOM   1459 N NE2 . GLN A 1 181 ? 2.833  28.605  -24.560 1.00 49.64  ? 180 GLN A NE2 1 
ATOM   1460 N N   . ARG A 1 182 ? 1.805  30.485  -17.880 1.00 46.12  ? 181 ARG A N   1 
ATOM   1461 C CA  . ARG A 1 182 ? 1.457  31.479  -16.875 1.00 47.58  ? 181 ARG A CA  1 
ATOM   1462 C C   . ARG A 1 182 ? 2.612  32.450  -16.630 1.00 49.38  ? 181 ARG A C   1 
ATOM   1463 O O   . ARG A 1 182 ? 3.788  32.158  -16.877 1.00 49.64  ? 181 ARG A O   1 
ATOM   1464 C CB  . ARG A 1 182 ? 1.065  30.806  -15.551 1.00 50.52  ? 181 ARG A CB  1 
ATOM   1465 C CG  . ARG A 1 182 ? 2.254  30.319  -14.702 1.00 50.64  ? 181 ARG A CG  1 
ATOM   1466 C CD  . ARG A 1 182 ? 1.817  29.482  -13.481 1.00 44.22  ? 181 ARG A CD  1 
ATOM   1467 N NE  . ARG A 1 182 ? 2.764  28.394  -13.193 1.00 49.35  ? 181 ARG A NE  1 
ATOM   1468 C CZ  . ARG A 1 182 ? 3.612  28.386  -12.164 1.00 47.20  ? 181 ARG A CZ  1 
ATOM   1469 N NH1 . ARG A 1 182 ? 3.640  29.411  -11.327 1.00 47.12  ? 181 ARG A NH1 1 
ATOM   1470 N NH2 . ARG A 1 182 ? 4.440  27.364  -11.973 1.00 46.98  ? 181 ARG A NH2 1 
ATOM   1471 N N   . THR A 1 183 ? 2.249  33.632  -16.143 1.00 46.16  ? 182 THR A N   1 
ATOM   1472 C CA  . THR A 1 183 ? 3.210  34.638  -15.706 1.00 47.72  ? 182 THR A CA  1 
ATOM   1473 C C   . THR A 1 183 ? 2.623  35.315  -14.478 1.00 47.17  ? 182 THR A C   1 
ATOM   1474 O O   . THR A 1 183 ? 1.671  36.093  -14.594 1.00 50.62  ? 182 THR A O   1 
ATOM   1475 C CB  . THR A 1 183 ? 3.501  35.657  -16.802 1.00 48.00  ? 182 THR A CB  1 
ATOM   1476 O OG1 . THR A 1 183 ? 4.167  35.010  -17.890 1.00 53.43  ? 182 THR A OG1 1 
ATOM   1477 C CG2 . THR A 1 183 ? 4.397  36.723  -16.268 1.00 48.74  ? 182 THR A CG2 1 
ATOM   1478 N N   . ASP A 1 184 ? 3.180  35.013  -13.303 1.00 46.82  ? 183 ASP A N   1 
ATOM   1479 C CA  . ASP A 1 184 ? 2.659  35.537  -12.047 1.00 41.03  ? 183 ASP A CA  1 
ATOM   1480 C C   . ASP A 1 184 ? 3.513  36.714  -11.597 1.00 40.19  ? 183 ASP A C   1 
ATOM   1481 O O   . ASP A 1 184 ? 4.695  36.516  -11.270 1.00 35.95  ? 183 ASP A O   1 
ATOM   1482 C CB  . ASP A 1 184 ? 2.639  34.445  -10.980 1.00 38.44  ? 183 ASP A CB  1 
ATOM   1483 C CG  . ASP A 1 184 ? 1.657  33.298  -11.312 1.00 43.79  ? 183 ASP A CG  1 
ATOM   1484 O OD1 . ASP A 1 184 ? 0.541  33.574  -11.796 1.00 45.72  ? 183 ASP A OD1 1 
ATOM   1485 O OD2 . ASP A 1 184 ? 1.991  32.114  -11.080 1.00 45.88  ? 183 ASP A OD2 1 
ATOM   1486 N N   . PRO A 1 185 ? 2.988  37.943  -11.575 1.00 39.29  ? 184 PRO A N   1 
ATOM   1487 C CA  . PRO A 1 185 ? 3.794  39.072  -11.118 1.00 37.18  ? 184 PRO A CA  1 
ATOM   1488 C C   . PRO A 1 185 ? 4.076  38.960  -9.621  1.00 33.69  ? 184 PRO A C   1 
ATOM   1489 O O   . PRO A 1 185 ? 3.315  38.315  -8.882  1.00 32.03  ? 184 PRO A O   1 
ATOM   1490 C CB  . PRO A 1 185 ? 2.915  40.293  -11.434 1.00 36.17  ? 184 PRO A CB  1 
ATOM   1491 C CG  . PRO A 1 185 ? 1.521  39.787  -11.332 1.00 30.23  ? 184 PRO A CG  1 
ATOM   1492 C CD  . PRO A 1 185 ? 1.566  38.311  -11.739 1.00 37.23  ? 184 PRO A CD  1 
ATOM   1493 N N   . PRO A 1 186 ? 5.155  39.562  -9.150  1.00 33.45  ? 185 PRO A N   1 
ATOM   1494 C CA  . PRO A 1 186 ? 5.453  39.502  -7.711  1.00 34.50  ? 185 PRO A CA  1 
ATOM   1495 C C   . PRO A 1 186 ? 4.569  40.434  -6.893  1.00 36.83  ? 185 PRO A C   1 
ATOM   1496 O O   . PRO A 1 186 ? 4.336  41.586  -7.269  1.00 37.73  ? 185 PRO A O   1 
ATOM   1497 C CB  . PRO A 1 186 ? 6.914  39.958  -7.646  1.00 32.41  ? 185 PRO A CB  1 
ATOM   1498 C CG  . PRO A 1 186 ? 7.011  40.963  -8.802  1.00 34.93  ? 185 PRO A CG  1 
ATOM   1499 C CD  . PRO A 1 186 ? 6.159  40.338  -9.896  1.00 31.90  ? 185 PRO A CD  1 
ATOM   1500 N N   . LYS A 1 187 ? 4.097  39.931  -5.746  1.00 37.43  ? 186 LYS A N   1 
ATOM   1501 C CA  . LYS A 1 187 ? 3.512  40.788  -4.718  1.00 28.21  ? 186 LYS A CA  1 
ATOM   1502 C C   . LYS A 1 187 ? 4.621  41.330  -3.826  1.00 34.10  ? 186 LYS A C   1 
ATOM   1503 O O   . LYS A 1 187 ? 5.435  40.563  -3.298  1.00 34.39  ? 186 LYS A O   1 
ATOM   1504 C CB  . LYS A 1 187 ? 2.492  40.024  -3.880  1.00 33.09  ? 186 LYS A CB  1 
ATOM   1505 C CG  . LYS A 1 187 ? 1.379  39.343  -4.681  1.00 42.93  ? 186 LYS A CG  1 
ATOM   1506 C CD  . LYS A 1 187 ? 0.715  38.233  -3.839  1.00 47.36  ? 186 LYS A CD  1 
ATOM   1507 C CE  . LYS A 1 187 ? -0.067 37.255  -4.710  1.00 59.30  ? 186 LYS A CE  1 
ATOM   1508 N NZ  . LYS A 1 187 ? 0.545  37.103  -6.073  1.00 54.28  ? 186 LYS A NZ  1 
ATOM   1509 N N   . THR A 1 188 ? 4.659  42.651  -3.652  1.00 29.34  ? 187 THR A N   1 
ATOM   1510 C CA  . THR A 1 188 ? 5.800  43.298  -3.032  1.00 32.17  ? 187 THR A CA  1 
ATOM   1511 C C   . THR A 1 188 ? 5.406  44.026  -1.748  1.00 32.36  ? 187 THR A C   1 
ATOM   1512 O O   . THR A 1 188 ? 4.267  44.467  -1.579  1.00 33.14  ? 187 THR A O   1 
ATOM   1513 C CB  . THR A 1 188 ? 6.462  44.274  -3.998  1.00 31.29  ? 187 THR A CB  1 
ATOM   1514 O OG1 . THR A 1 188 ? 5.482  45.190  -4.485  1.00 37.54  ? 187 THR A OG1 1 
ATOM   1515 C CG2 . THR A 1 188 ? 7.062  43.516  -5.190  1.00 36.50  ? 187 THR A CG2 1 
ATOM   1516 N N   . HIS A 1 189 ? 6.368  44.141  -0.843  1.00 31.05  ? 188 HIS A N   1 
ATOM   1517 C CA  . HIS A 1 189 ? 6.189  44.908  0.380   1.00 34.79  ? 188 HIS A CA  1 
ATOM   1518 C C   . HIS A 1 189 ? 7.562  45.163  0.990   1.00 35.91  ? 188 HIS A C   1 
ATOM   1519 O O   . HIS A 1 189 ? 8.593  44.691  0.495   1.00 30.07  ? 188 HIS A O   1 
ATOM   1520 C CB  . HIS A 1 189 ? 5.247  44.202  1.362   1.00 29.99  ? 188 HIS A CB  1 
ATOM   1521 C CG  . HIS A 1 189 ? 5.776  42.916  1.904   1.00 31.62  ? 188 HIS A CG  1 
ATOM   1522 N ND1 . HIS A 1 189 ? 6.352  42.818  3.153   1.00 33.93  ? 188 HIS A ND1 1 
ATOM   1523 C CD2 . HIS A 1 189 ? 5.781  41.666  1.387   1.00 33.82  ? 188 HIS A CD2 1 
ATOM   1524 C CE1 . HIS A 1 189 ? 6.707  41.565  3.374   1.00 29.74  ? 188 HIS A CE1 1 
ATOM   1525 N NE2 . HIS A 1 189 ? 6.367  40.844  2.319   1.00 34.27  ? 188 HIS A NE2 1 
ATOM   1526 N N   . MET A 1 190 ? 7.565  45.927  2.069   1.00 32.52  ? 189 MET A N   1 
ATOM   1527 C CA  . MET A 1 190 ? 8.800  46.367  2.685   1.00 33.44  ? 189 MET A CA  1 
ATOM   1528 C C   . MET A 1 190 ? 8.681  46.225  4.194   1.00 36.52  ? 189 MET A C   1 
ATOM   1529 O O   . MET A 1 190 ? 7.636  46.533  4.768   1.00 40.70  ? 189 MET A O   1 
ATOM   1530 C CB  . MET A 1 190 ? 9.096  47.808  2.287   1.00 33.78  ? 189 MET A CB  1 
ATOM   1531 C CG  . MET A 1 190 ? 10.562 48.155  2.263   1.00 42.37  ? 189 MET A CG  1 
ATOM   1532 S SD  . MET A 1 190 ? 10.846 49.921  2.073   1.00 48.08  ? 189 MET A SD  1 
ATOM   1533 C CE  . MET A 1 190 ? 10.814 50.040  0.287   1.00 33.60  ? 189 MET A CE  1 
ATOM   1534 N N   . THR A 1 191 ? 9.730  45.712  4.824   1.00 32.93  ? 190 THR A N   1 
ATOM   1535 C CA  . THR A 1 191 ? 9.844  45.705  6.272   1.00 32.02  ? 190 THR A CA  1 
ATOM   1536 C C   . THR A 1 191 ? 10.918 46.701  6.684   1.00 38.45  ? 190 THR A C   1 
ATOM   1537 O O   . THR A 1 191 ? 11.723 47.162  5.866   1.00 35.37  ? 190 THR A O   1 
ATOM   1538 C CB  . THR A 1 191 ? 10.195 44.316  6.821   1.00 35.88  ? 190 THR A CB  1 
ATOM   1539 O OG1 . THR A 1 191 ? 11.359 43.816  6.147   1.00 35.68  ? 190 THR A OG1 1 
ATOM   1540 C CG2 . THR A 1 191 ? 9.010  43.322  6.679   1.00 30.76  ? 190 THR A CG2 1 
ATOM   1541 N N   . HIS A 1 192 ? 10.927 47.022  7.975   1.00 36.61  ? 191 HIS A N   1 
ATOM   1542 C CA  . HIS A 1 192 ? 11.828 48.026  8.527   1.00 37.27  ? 191 HIS A CA  1 
ATOM   1543 C C   . HIS A 1 192 ? 12.251 47.547  9.901   1.00 39.09  ? 191 HIS A C   1 
ATOM   1544 O O   . HIS A 1 192 ? 11.396 47.274  10.749  1.00 39.90  ? 191 HIS A O   1 
ATOM   1545 C CB  . HIS A 1 192 ? 11.148 49.397  8.605   1.00 33.40  ? 191 HIS A CB  1 
ATOM   1546 C CG  . HIS A 1 192 ? 11.965 50.455  9.285   1.00 39.81  ? 191 HIS A CG  1 
ATOM   1547 N ND1 . HIS A 1 192 ? 11.744 50.837  10.590  1.00 38.30  ? 191 HIS A ND1 1 
ATOM   1548 C CD2 . HIS A 1 192 ? 12.974 51.237  8.832   1.00 36.72  ? 191 HIS A CD2 1 
ATOM   1549 C CE1 . HIS A 1 192 ? 12.592 51.797  10.916  1.00 40.46  ? 191 HIS A CE1 1 
ATOM   1550 N NE2 . HIS A 1 192 ? 13.350 52.058  9.867   1.00 36.43  ? 191 HIS A NE2 1 
ATOM   1551 N N   . HIS A 1 193 ? 13.555 47.441  10.111  1.00 36.38  ? 192 HIS A N   1 
ATOM   1552 C CA  . HIS A 1 193 ? 14.097 46.843  11.318  1.00 44.35  ? 192 HIS A CA  1 
ATOM   1553 C C   . HIS A 1 193 ? 15.246 47.680  11.852  1.00 48.76  ? 192 HIS A C   1 
ATOM   1554 O O   . HIS A 1 193 ? 16.319 47.728  11.234  1.00 47.63  ? 192 HIS A O   1 
ATOM   1555 C CB  . HIS A 1 193 ? 14.569 45.420  11.042  1.00 48.74  ? 192 HIS A CB  1 
ATOM   1556 C CG  . HIS A 1 193 ? 13.452 44.466  10.761  1.00 56.67  ? 192 HIS A CG  1 
ATOM   1557 N ND1 . HIS A 1 193 ? 12.572 44.049  11.737  1.00 52.19  ? 192 HIS A ND1 1 
ATOM   1558 C CD2 . HIS A 1 193 ? 13.060 43.861  9.612   1.00 47.82  ? 192 HIS A CD2 1 
ATOM   1559 C CE1 . HIS A 1 193 ? 11.693 43.220  11.204  1.00 55.39  ? 192 HIS A CE1 1 
ATOM   1560 N NE2 . HIS A 1 193 ? 11.966 43.089  9.916   1.00 50.56  ? 192 HIS A NE2 1 
ATOM   1561 N N   . PRO A 1 194 ? 15.052 48.355  12.985  1.00 53.58  ? 193 PRO A N   1 
ATOM   1562 C CA  . PRO A 1 194 ? 16.137 49.152  13.573  1.00 53.67  ? 193 PRO A CA  1 
ATOM   1563 C C   . PRO A 1 194 ? 17.311 48.273  13.980  1.00 52.55  ? 193 PRO A C   1 
ATOM   1564 O O   . PRO A 1 194 ? 17.143 47.271  14.673  1.00 48.40  ? 193 PRO A O   1 
ATOM   1565 C CB  . PRO A 1 194 ? 15.468 49.808  14.786  1.00 48.66  ? 193 PRO A CB  1 
ATOM   1566 C CG  . PRO A 1 194 ? 14.000 49.845  14.421  1.00 46.92  ? 193 PRO A CG  1 
ATOM   1567 C CD  . PRO A 1 194 ? 13.769 48.563  13.681  1.00 47.67  ? 193 PRO A CD  1 
ATOM   1568 N N   . ILE A 1 195 ? 18.506 48.646  13.519  1.00 59.05  ? 194 ILE A N   1 
ATOM   1569 C CA  . ILE A 1 195 ? 19.727 47.967  13.953  1.00 61.17  ? 194 ILE A CA  1 
ATOM   1570 C C   . ILE A 1 195 ? 20.208 48.532  15.283  1.00 61.45  ? 194 ILE A C   1 
ATOM   1571 O O   . ILE A 1 195 ? 20.346 47.814  16.279  1.00 66.20  ? 194 ILE A O   1 
ATOM   1572 C CB  . ILE A 1 195 ? 20.828 48.084  12.883  1.00 59.77  ? 194 ILE A CB  1 
ATOM   1573 C CG1 . ILE A 1 195 ? 20.320 47.614  11.517  1.00 56.96  ? 194 ILE A CG1 1 
ATOM   1574 C CG2 . ILE A 1 195 ? 22.065 47.310  13.320  1.00 61.75  ? 194 ILE A CG2 1 
ATOM   1575 C CD1 . ILE A 1 195 ? 21.423 47.143  10.594  1.00 54.11  ? 194 ILE A CD1 1 
ATOM   1576 N N   . SER A 1 196 ? 20.509 49.828  15.300  1.00 64.52  ? 195 SER A N   1 
ATOM   1577 C CA  . SER A 1 196 ? 20.871 50.583  16.480  1.00 66.63  ? 195 SER A CA  1 
ATOM   1578 C C   . SER A 1 196 ? 19.747 51.582  16.762  1.00 68.68  ? 195 SER A C   1 
ATOM   1579 O O   . SER A 1 196 ? 18.582 51.326  16.402  1.00 67.59  ? 195 SER A O   1 
ATOM   1580 C CB  . SER A 1 196 ? 22.229 51.236  16.248  1.00 65.51  ? 195 SER A CB  1 
ATOM   1581 O OG  . SER A 1 196 ? 22.245 51.936  15.012  1.00 61.51  ? 195 SER A OG  1 
ATOM   1582 N N   . ASP A 1 197 ? 20.081 52.709  17.377  1.00 67.60  ? 196 ASP A N   1 
ATOM   1583 C CA  . ASP A 1 197 ? 19.157 53.827  17.429  1.00 67.85  ? 196 ASP A CA  1 
ATOM   1584 C C   . ASP A 1 197 ? 19.541 54.904  16.433  1.00 64.73  ? 196 ASP A C   1 
ATOM   1585 O O   . ASP A 1 197 ? 18.923 55.971  16.414  1.00 64.58  ? 196 ASP A O   1 
ATOM   1586 C CB  . ASP A 1 197 ? 19.069 54.376  18.851  1.00 70.58  ? 196 ASP A CB  1 
ATOM   1587 C CG  . ASP A 1 197 ? 18.496 53.351  19.830  1.00 78.74  ? 196 ASP A CG  1 
ATOM   1588 O OD1 . ASP A 1 197 ? 18.995 52.198  19.849  1.00 79.12  ? 196 ASP A OD1 1 
ATOM   1589 O OD2 . ASP A 1 197 ? 17.544 53.685  20.571  1.00 77.85  ? 196 ASP A OD2 1 
ATOM   1590 N N   . HIS A 1 198 ? 20.535 54.622  15.583  1.00 65.36  ? 197 HIS A N   1 
ATOM   1591 C CA  . HIS A 1 198 ? 20.873 55.474  14.456  1.00 62.48  ? 197 HIS A CA  1 
ATOM   1592 C C   . HIS A 1 198 ? 20.957 54.725  13.126  1.00 55.00  ? 197 HIS A C   1 
ATOM   1593 O O   . HIS A 1 198 ? 21.309 55.343  12.118  1.00 53.52  ? 197 HIS A O   1 
ATOM   1594 C CB  . HIS A 1 198 ? 22.196 56.213  14.723  1.00 62.52  ? 197 HIS A CB  1 
ATOM   1595 C CG  . HIS A 1 198 ? 23.398 55.322  14.760  1.00 65.80  ? 197 HIS A CG  1 
ATOM   1596 N ND1 . HIS A 1 198 ? 23.588 54.364  15.734  1.00 68.18  ? 197 HIS A ND1 1 
ATOM   1597 C CD2 . HIS A 1 198 ? 24.479 55.250  13.945  1.00 64.98  ? 197 HIS A CD2 1 
ATOM   1598 C CE1 . HIS A 1 198 ? 24.731 53.737  15.514  1.00 64.07  ? 197 HIS A CE1 1 
ATOM   1599 N NE2 . HIS A 1 198 ? 25.291 54.256  14.435  1.00 65.32  ? 197 HIS A NE2 1 
ATOM   1600 N N   . GLU A 1 199 ? 20.617 53.433  13.086  1.00 57.10  ? 198 GLU A N   1 
ATOM   1601 C CA  . GLU A 1 199 ? 20.642 52.639  11.859  1.00 55.62  ? 198 GLU A CA  1 
ATOM   1602 C C   . GLU A 1 199 ? 19.433 51.713  11.783  1.00 54.87  ? 198 GLU A C   1 
ATOM   1603 O O   . GLU A 1 199 ? 18.938 51.227  12.807  1.00 50.12  ? 198 GLU A O   1 
ATOM   1604 C CB  . GLU A 1 199 ? 21.902 51.773  11.752  1.00 57.32  ? 198 GLU A CB  1 
ATOM   1605 C CG  . GLU A 1 199 ? 23.176 52.512  11.465  1.00 58.52  ? 198 GLU A CG  1 
ATOM   1606 C CD  . GLU A 1 199 ? 24.348 51.565  11.352  1.00 60.98  ? 198 GLU A CD  1 
ATOM   1607 O OE1 . GLU A 1 199 ? 24.495 50.690  12.236  1.00 60.86  ? 198 GLU A OE1 1 
ATOM   1608 O OE2 . GLU A 1 199 ? 25.115 51.691  10.373  1.00 62.45  ? 198 GLU A OE2 1 
ATOM   1609 N N   . ALA A 1 200 ? 18.992 51.433  10.551  1.00 50.23  ? 199 ALA A N   1 
ATOM   1610 C CA  . ALA A 1 200 ? 17.873 50.526  10.327  1.00 45.83  ? 199 ALA A CA  1 
ATOM   1611 C C   . ALA A 1 200 ? 18.059 49.741  9.029   1.00 49.90  ? 199 ALA A C   1 
ATOM   1612 O O   . ALA A 1 200 ? 18.704 50.210  8.083   1.00 46.77  ? 199 ALA A O   1 
ATOM   1613 C CB  . ALA A 1 200 ? 16.545 51.288  10.285  1.00 44.85  ? 199 ALA A CB  1 
ATOM   1614 N N   . THR A 1 201 ? 17.462 48.545  8.988   1.00 46.76  ? 200 THR A N   1 
ATOM   1615 C CA  . THR A 1 201 ? 17.460 47.685  7.807   1.00 43.24  ? 200 THR A CA  1 
ATOM   1616 C C   . THR A 1 201 ? 16.129 47.819  7.081   1.00 38.65  ? 200 THR A C   1 
ATOM   1617 O O   . THR A 1 201 ? 15.083 47.474  7.638   1.00 42.33  ? 200 THR A O   1 
ATOM   1618 C CB  . THR A 1 201 ? 17.678 46.219  8.186   1.00 43.58  ? 200 THR A CB  1 
ATOM   1619 O OG1 . THR A 1 201 ? 18.962 46.054  8.794   1.00 46.19  ? 200 THR A OG1 1 
ATOM   1620 C CG2 . THR A 1 201 ? 17.572 45.317  6.949   1.00 39.66  ? 200 THR A CG2 1 
ATOM   1621 N N   . LEU A 1 202 ? 16.166 48.311  5.849   1.00 35.25  ? 201 LEU A N   1 
ATOM   1622 C CA  . LEU A 1 202 ? 15.014 48.254  4.960   1.00 37.06  ? 201 LEU A CA  1 
ATOM   1623 C C   . LEU A 1 202 ? 15.122 46.994  4.114   1.00 38.80  ? 201 LEU A C   1 
ATOM   1624 O O   . LEU A 1 202 ? 16.163 46.747  3.500   1.00 35.61  ? 201 LEU A O   1 
ATOM   1625 C CB  . LEU A 1 202 ? 14.948 49.486  4.052   1.00 37.80  ? 201 LEU A CB  1 
ATOM   1626 C CG  . LEU A 1 202 ? 14.632 50.842  4.691   1.00 40.42  ? 201 LEU A CG  1 
ATOM   1627 C CD1 . LEU A 1 202 ? 14.678 51.938  3.641   1.00 40.32  ? 201 LEU A CD1 1 
ATOM   1628 C CD2 . LEU A 1 202 ? 13.271 50.834  5.409   1.00 34.42  ? 201 LEU A CD2 1 
ATOM   1629 N N   . ARG A 1 203 ? 14.053 46.196  4.085   1.00 37.10  ? 202 ARG A N   1 
ATOM   1630 C CA  . ARG A 1 203 ? 14.014 44.980  3.286   1.00 37.14  ? 202 ARG A CA  1 
ATOM   1631 C C   . ARG A 1 203 ? 12.878 45.057  2.270   1.00 34.00  ? 202 ARG A C   1 
ATOM   1632 O O   . ARG A 1 203 ? 11.716 45.274  2.631   1.00 33.46  ? 202 ARG A O   1 
ATOM   1633 C CB  . ARG A 1 203 ? 13.871 43.731  4.169   1.00 30.49  ? 202 ARG A CB  1 
ATOM   1634 C CG  . ARG A 1 203 ? 13.912 42.411  3.377   1.00 32.27  ? 202 ARG A CG  1 
ATOM   1635 C CD  . ARG A 1 203 ? 14.182 41.194  4.289   1.00 32.98  ? 202 ARG A CD  1 
ATOM   1636 N NE  . ARG A 1 203 ? 15.575 41.132  4.731   1.00 33.77  ? 202 ARG A NE  1 
ATOM   1637 C CZ  . ARG A 1 203 ? 15.977 41.373  5.980   1.00 40.42  ? 202 ARG A CZ  1 
ATOM   1638 N NH1 . ARG A 1 203 ? 15.092 41.684  6.915   1.00 32.70  ? 202 ARG A NH1 1 
ATOM   1639 N NH2 . ARG A 1 203 ? 17.267 41.305  6.296   1.00 39.33  ? 202 ARG A NH2 1 
ATOM   1640 N N   . CYS A 1 204 ? 13.221 44.863  1.008   1.00 36.04  ? 203 CYS A N   1 
ATOM   1641 C CA  . CYS A 1 204 ? 12.273 44.866  -0.095  1.00 31.32  ? 203 CYS A CA  1 
ATOM   1642 C C   . CYS A 1 204 ? 11.983 43.422  -0.490  1.00 33.45  ? 203 CYS A C   1 
ATOM   1643 O O   . CYS A 1 204 ? 12.910 42.682  -0.844  1.00 33.53  ? 203 CYS A O   1 
ATOM   1644 C CB  . CYS A 1 204 ? 12.865 45.641  -1.269  1.00 30.77  ? 203 CYS A CB  1 
ATOM   1645 S SG  . CYS A 1 204 ? 11.768 45.873  -2.677  1.00 44.91  ? 203 CYS A SG  1 
ATOM   1646 N N   . TRP A 1 205 ? 10.706 43.036  -0.463  1.00 32.24  ? 204 TRP A N   1 
ATOM   1647 C CA  . TRP A 1 205 ? 10.272 41.649  -0.613  1.00 31.21  ? 204 TRP A CA  1 
ATOM   1648 C C   . TRP A 1 205 ? 9.480  41.472  -1.906  1.00 34.84  ? 204 TRP A C   1 
ATOM   1649 O O   . TRP A 1 205 ? 8.608  42.289  -2.216  1.00 34.50  ? 204 TRP A O   1 
ATOM   1650 C CB  . TRP A 1 205 ? 9.369  41.226  0.560   1.00 26.54  ? 204 TRP A CB  1 
ATOM   1651 C CG  . TRP A 1 205 ? 10.024 40.800  1.843   1.00 29.23  ? 204 TRP A CG  1 
ATOM   1652 C CD1 . TRP A 1 205 ? 10.304 41.588  2.928   1.00 32.88  ? 204 TRP A CD1 1 
ATOM   1653 C CD2 . TRP A 1 205 ? 10.417 39.470  2.207   1.00 31.48  ? 204 TRP A CD2 1 
ATOM   1654 N NE1 . TRP A 1 205 ? 10.877 40.836  3.931   1.00 28.02  ? 204 TRP A NE1 1 
ATOM   1655 C CE2 . TRP A 1 205 ? 10.948 39.531  3.519   1.00 34.14  ? 204 TRP A CE2 1 
ATOM   1656 C CE3 . TRP A 1 205 ? 10.383 38.234  1.552   1.00 30.73  ? 204 TRP A CE3 1 
ATOM   1657 C CZ2 . TRP A 1 205 ? 11.440 38.402  4.180   1.00 33.01  ? 204 TRP A CZ2 1 
ATOM   1658 C CZ3 . TRP A 1 205 ? 10.881 37.114  2.213   1.00 32.46  ? 204 TRP A CZ3 1 
ATOM   1659 C CH2 . TRP A 1 205 ? 11.397 37.208  3.511   1.00 33.11  ? 204 TRP A CH2 1 
ATOM   1660 N N   . ALA A 1 206 ? 9.744  40.383  -2.639  1.00 27.34  ? 205 ALA A N   1 
ATOM   1661 C CA  . ALA A 1 206 ? 8.903  39.980  -3.764  1.00 32.32  ? 205 ALA A CA  1 
ATOM   1662 C C   . ALA A 1 206 ? 8.466  38.533  -3.566  1.00 26.96  ? 205 ALA A C   1 
ATOM   1663 O O   . ALA A 1 206 ? 9.299  37.662  -3.311  1.00 29.71  ? 205 ALA A O   1 
ATOM   1664 C CB  . ALA A 1 206 ? 9.627  40.148  -5.110  1.00 30.89  ? 205 ALA A CB  1 
ATOM   1665 N N   . LEU A 1 207 ? 7.166  38.277  -3.671  1.00 24.84  ? 206 LEU A N   1 
ATOM   1666 C CA  . LEU A 1 207 ? 6.618  36.970  -3.345  1.00 29.31  ? 206 LEU A CA  1 
ATOM   1667 C C   . LEU A 1 207 ? 5.682  36.493  -4.444  1.00 30.10  ? 206 LEU A C   1 
ATOM   1668 O O   . LEU A 1 207 ? 5.068  37.295  -5.157  1.00 32.37  ? 206 LEU A O   1 
ATOM   1669 C CB  . LEU A 1 207 ? 5.851  36.983  -2.001  1.00 25.73  ? 206 LEU A CB  1 
ATOM   1670 C CG  . LEU A 1 207 ? 6.588  37.348  -0.708  1.00 33.84  ? 206 LEU A CG  1 
ATOM   1671 C CD1 . LEU A 1 207 ? 5.608  37.603  0.464   1.00 31.61  ? 206 LEU A CD1 1 
ATOM   1672 C CD2 . LEU A 1 207 ? 7.599  36.275  -0.322  1.00 27.60  ? 206 LEU A CD2 1 
ATOM   1673 N N   . GLY A 1 208 ? 5.575  35.169  -4.559  1.00 26.54  ? 207 GLY A N   1 
ATOM   1674 C CA  . GLY A 1 208 ? 4.589  34.552  -5.430  1.00 27.85  ? 207 GLY A CA  1 
ATOM   1675 C C   . GLY A 1 208 ? 4.787  34.793  -6.912  1.00 32.94  ? 207 GLY A C   1 
ATOM   1676 O O   . GLY A 1 208 ? 3.814  34.737  -7.668  1.00 35.68  ? 207 GLY A O   1 
ATOM   1677 N N   . PHE A 1 209 ? 6.010  35.055  -7.360  1.00 28.75  ? 208 PHE A N   1 
ATOM   1678 C CA  . PHE A 1 209 ? 6.229  35.324  -8.772  1.00 31.76  ? 208 PHE A CA  1 
ATOM   1679 C C   . PHE A 1 209 ? 6.705  34.074  -9.517  1.00 37.72  ? 208 PHE A C   1 
ATOM   1680 O O   . PHE A 1 209 ? 7.276  33.147  -8.930  1.00 36.98  ? 208 PHE A O   1 
ATOM   1681 C CB  . PHE A 1 209 ? 7.208  36.489  -8.980  1.00 32.15  ? 208 PHE A CB  1 
ATOM   1682 C CG  . PHE A 1 209 ? 8.545  36.319  -8.308  1.00 33.70  ? 208 PHE A CG  1 
ATOM   1683 C CD1 . PHE A 1 209 ? 8.713  36.634  -6.965  1.00 33.47  ? 208 PHE A CD1 1 
ATOM   1684 C CD2 . PHE A 1 209 ? 9.649  35.886  -9.032  1.00 33.68  ? 208 PHE A CD2 1 
ATOM   1685 C CE1 . PHE A 1 209 ? 9.954  36.486  -6.354  1.00 34.08  ? 208 PHE A CE1 1 
ATOM   1686 C CE2 . PHE A 1 209 ? 10.892 35.739  -8.429  1.00 33.41  ? 208 PHE A CE2 1 
ATOM   1687 C CZ  . PHE A 1 209 ? 11.051 36.029  -7.098  1.00 26.83  ? 208 PHE A CZ  1 
ATOM   1688 N N   . TYR A 1 210 ? 6.408  34.044  -10.824 1.00 36.70  ? 209 TYR A N   1 
ATOM   1689 C CA  . TYR A 1 210 ? 6.803  33.006  -11.771 1.00 36.14  ? 209 TYR A CA  1 
ATOM   1690 C C   . TYR A 1 210 ? 6.840  33.590  -13.178 1.00 39.56  ? 209 TYR A C   1 
ATOM   1691 O O   . TYR A 1 210 ? 5.860  34.214  -13.598 1.00 38.90  ? 209 TYR A O   1 
ATOM   1692 C CB  . TYR A 1 210 ? 5.842  31.813  -11.759 1.00 37.41  ? 209 TYR A CB  1 
ATOM   1693 C CG  . TYR A 1 210 ? 6.299  30.704  -12.685 1.00 37.29  ? 209 TYR A CG  1 
ATOM   1694 C CD1 . TYR A 1 210 ? 6.015  30.732  -14.055 1.00 35.07  ? 209 TYR A CD1 1 
ATOM   1695 C CD2 . TYR A 1 210 ? 7.051  29.643  -12.193 1.00 38.76  ? 209 TYR A CD2 1 
ATOM   1696 C CE1 . TYR A 1 210 ? 6.457  29.721  -14.900 1.00 36.39  ? 209 TYR A CE1 1 
ATOM   1697 C CE2 . TYR A 1 210 ? 7.491  28.629  -13.021 1.00 35.47  ? 209 TYR A CE2 1 
ATOM   1698 C CZ  . TYR A 1 210 ? 7.201  28.670  -14.371 1.00 39.50  ? 209 TYR A CZ  1 
ATOM   1699 O OH  . TYR A 1 210 ? 7.659  27.642  -15.165 1.00 34.49  ? 209 TYR A OH  1 
ATOM   1700 N N   . PRO A 1 211 ? 7.911  33.350  -13.968 1.00 39.30  ? 210 PRO A N   1 
ATOM   1701 C CA  . PRO A 1 211 ? 9.078  32.528  -13.619 1.00 34.74  ? 210 PRO A CA  1 
ATOM   1702 C C   . PRO A 1 211 ? 10.067 33.198  -12.646 1.00 38.49  ? 210 PRO A C   1 
ATOM   1703 O O   . PRO A 1 211 ? 9.848  34.332  -12.208 1.00 34.96  ? 210 PRO A O   1 
ATOM   1704 C CB  . PRO A 1 211 ? 9.737  32.279  -14.974 1.00 39.89  ? 210 PRO A CB  1 
ATOM   1705 C CG  . PRO A 1 211 ? 9.338  33.440  -15.806 1.00 41.35  ? 210 PRO A CG  1 
ATOM   1706 C CD  . PRO A 1 211 ? 7.917  33.715  -15.395 1.00 43.80  ? 210 PRO A CD  1 
ATOM   1707 N N   . ALA A 1 212 ? 11.157 32.480  -12.351 1.00 36.66  ? 211 ALA A N   1 
ATOM   1708 C CA  . ALA A 1 212 ? 12.031 32.807  -11.227 1.00 38.71  ? 211 ALA A CA  1 
ATOM   1709 C C   . ALA A 1 212 ? 12.851 34.071  -11.457 1.00 40.31  ? 211 ALA A C   1 
ATOM   1710 O O   . ALA A 1 212 ? 13.243 34.729  -10.484 1.00 43.02  ? 211 ALA A O   1 
ATOM   1711 C CB  . ALA A 1 212 ? 12.967 31.631  -10.930 1.00 30.98  ? 211 ALA A CB  1 
ATOM   1712 N N   . GLU A 1 213 ? 13.145 34.420  -12.706 1.00 39.77  ? 212 GLU A N   1 
ATOM   1713 C CA  . GLU A 1 213 ? 14.054 35.532  -12.952 1.00 40.00  ? 212 GLU A CA  1 
ATOM   1714 C C   . GLU A 1 213 ? 13.411 36.841  -12.516 1.00 39.18  ? 212 GLU A C   1 
ATOM   1715 O O   . GLU A 1 213 ? 12.241 37.113  -12.813 1.00 35.61  ? 212 GLU A O   1 
ATOM   1716 C CB  . GLU A 1 213 ? 14.449 35.601  -14.427 1.00 48.54  ? 212 GLU A CB  1 
ATOM   1717 C CG  . GLU A 1 213 ? 15.882 36.111  -14.636 1.00 56.47  ? 212 GLU A CG  1 
ATOM   1718 C CD  . GLU A 1 213 ? 15.937 37.596  -14.920 1.00 60.35  ? 212 GLU A CD  1 
ATOM   1719 O OE1 . GLU A 1 213 ? 15.101 38.049  -15.725 1.00 64.94  ? 212 GLU A OE1 1 
ATOM   1720 O OE2 . GLU A 1 213 ? 16.794 38.310  -14.329 1.00 64.74  ? 212 GLU A OE2 1 
ATOM   1721 N N   . ILE A 1 214 ? 14.184 37.650  -11.797 1.00 41.75  ? 213 ILE A N   1 
ATOM   1722 C CA  . ILE A 1 214 ? 13.680 38.888  -11.224 1.00 42.23  ? 213 ILE A CA  1 
ATOM   1723 C C   . ILE A 1 214 ? 14.874 39.785  -10.947 1.00 41.62  ? 213 ILE A C   1 
ATOM   1724 O O   . ILE A 1 214 ? 15.994 39.307  -10.741 1.00 40.67  ? 213 ILE A O   1 
ATOM   1725 C CB  . ILE A 1 214 ? 12.844 38.616  -9.944  1.00 30.53  ? 213 ILE A CB  1 
ATOM   1726 C CG1 . ILE A 1 214 ? 11.953 39.825  -9.614  1.00 35.33  ? 213 ILE A CG1 1 
ATOM   1727 C CG2 . ILE A 1 214 ? 13.744 38.234  -8.753  1.00 30.41  ? 213 ILE A CG2 1 
ATOM   1728 C CD1 . ILE A 1 214 ? 10.790 39.506  -8.667  1.00 31.54  ? 213 ILE A CD1 1 
ATOM   1729 N N   . THR A 1 215 ? 14.637 41.091  -10.954 1.00 39.33  ? 214 THR A N   1 
ATOM   1730 C CA  . THR A 1 215 ? 15.631 42.071  -10.546 1.00 42.14  ? 214 THR A CA  1 
ATOM   1731 C C   . THR A 1 215 ? 15.080 42.900  -9.388  1.00 42.84  ? 214 THR A C   1 
ATOM   1732 O O   . THR A 1 215 ? 13.942 43.375  -9.448  1.00 40.94  ? 214 THR A O   1 
ATOM   1733 C CB  . THR A 1 215 ? 16.009 42.969  -11.728 1.00 45.99  ? 214 THR A CB  1 
ATOM   1734 O OG1 . THR A 1 215 ? 16.191 42.159  -12.902 1.00 48.39  ? 214 THR A OG1 1 
ATOM   1735 C CG2 . THR A 1 215 ? 17.291 43.737  -11.426 1.00 39.03  ? 214 THR A CG2 1 
ATOM   1736 N N   . LEU A 1 216 ? 15.884 43.051  -8.332  1.00 45.54  ? 215 LEU A N   1 
ATOM   1737 C CA  . LEU A 1 216 ? 15.592 43.937  -7.209  1.00 43.22  ? 215 LEU A CA  1 
ATOM   1738 C C   . LEU A 1 216 ? 16.793 44.842  -6.978  1.00 47.25  ? 215 LEU A C   1 
ATOM   1739 O O   . LEU A 1 216 ? 17.864 44.355  -6.604  1.00 44.24  ? 215 LEU A O   1 
ATOM   1740 C CB  . LEU A 1 216 ? 15.301 43.157  -5.924  1.00 41.56  ? 215 LEU A CB  1 
ATOM   1741 C CG  . LEU A 1 216 ? 14.185 42.121  -5.775  1.00 41.25  ? 215 LEU A CG  1 
ATOM   1742 C CD1 . LEU A 1 216 ? 14.027 41.785  -4.297  1.00 36.82  ? 215 LEU A CD1 1 
ATOM   1743 C CD2 . LEU A 1 216 ? 12.883 42.621  -6.359  1.00 38.93  ? 215 LEU A CD2 1 
ATOM   1744 N N   . THR A 1 217 ? 16.615 46.155  -7.163  1.00 47.48  ? 216 THR A N   1 
ATOM   1745 C CA  . THR A 1 217 ? 17.695 47.106  -6.923  1.00 47.13  ? 216 THR A CA  1 
ATOM   1746 C C   . THR A 1 217 ? 17.252 48.198  -5.953  1.00 47.30  ? 216 THR A C   1 
ATOM   1747 O O   . THR A 1 217 ? 16.086 48.600  -5.927  1.00 47.77  ? 216 THR A O   1 
ATOM   1748 C CB  . THR A 1 217 ? 18.190 47.752  -8.229  1.00 49.60  ? 216 THR A CB  1 
ATOM   1749 O OG1 . THR A 1 217 ? 17.071 48.170  -9.013  1.00 57.42  ? 216 THR A OG1 1 
ATOM   1750 C CG2 . THR A 1 217 ? 19.026 46.761  -9.036  1.00 45.75  ? 216 THR A CG2 1 
ATOM   1751 N N   . TRP A 1 218 ? 18.203 48.664  -5.149  1.00 47.48  ? 217 TRP A N   1 
ATOM   1752 C CA  . TRP A 1 218 ? 18.006 49.786  -4.244  1.00 50.70  ? 217 TRP A CA  1 
ATOM   1753 C C   . TRP A 1 218 ? 18.635 51.040  -4.835  1.00 55.52  ? 217 TRP A C   1 
ATOM   1754 O O   . TRP A 1 218 ? 19.804 51.026  -5.236  1.00 54.32  ? 217 TRP A O   1 
ATOM   1755 C CB  . TRP A 1 218 ? 18.636 49.510  -2.879  1.00 52.98  ? 217 TRP A CB  1 
ATOM   1756 C CG  . TRP A 1 218 ? 17.823 48.641  -1.982  1.00 50.79  ? 217 TRP A CG  1 
ATOM   1757 C CD1 . TRP A 1 218 ? 18.039 47.325  -1.703  1.00 46.94  ? 217 TRP A CD1 1 
ATOM   1758 C CD2 . TRP A 1 218 ? 16.669 49.031  -1.224  1.00 49.61  ? 217 TRP A CD2 1 
ATOM   1759 N NE1 . TRP A 1 218 ? 17.083 46.865  -0.825  1.00 47.13  ? 217 TRP A NE1 1 
ATOM   1760 C CE2 . TRP A 1 218 ? 16.234 47.894  -0.513  1.00 44.05  ? 217 TRP A CE2 1 
ATOM   1761 C CE3 . TRP A 1 218 ? 15.961 50.230  -1.079  1.00 49.16  ? 217 TRP A CE3 1 
ATOM   1762 C CZ2 . TRP A 1 218 ? 15.118 47.917  0.327   1.00 40.68  ? 217 TRP A CZ2 1 
ATOM   1763 C CZ3 . TRP A 1 218 ? 14.852 50.253  -0.241  1.00 44.98  ? 217 TRP A CZ3 1 
ATOM   1764 C CH2 . TRP A 1 218 ? 14.445 49.102  0.452   1.00 42.53  ? 217 TRP A CH2 1 
ATOM   1765 N N   . GLN A 1 219 ? 17.868 52.123  -4.873  1.00 49.34  ? 218 GLN A N   1 
ATOM   1766 C CA  . GLN A 1 219 ? 18.399 53.422  -5.244  1.00 56.50  ? 218 GLN A CA  1 
ATOM   1767 C C   . GLN A 1 219 ? 18.359 54.352  -4.039  1.00 56.29  ? 218 GLN A C   1 
ATOM   1768 O O   . GLN A 1 219 ? 17.470 54.253  -3.190  1.00 50.58  ? 218 GLN A O   1 
ATOM   1769 C CB  . GLN A 1 219 ? 17.624 54.030  -6.420  1.00 54.53  ? 218 GLN A CB  1 
ATOM   1770 C CG  . GLN A 1 219 ? 17.830 53.288  -7.739  1.00 56.34  ? 218 GLN A CG  1 
ATOM   1771 C CD  . GLN A 1 219 ? 17.241 54.018  -8.937  1.00 59.56  ? 218 GLN A CD  1 
ATOM   1772 O OE1 . GLN A 1 219 ? 16.870 55.188  -8.848  1.00 63.43  ? 218 GLN A OE1 1 
ATOM   1773 N NE2 . GLN A 1 219 ? 17.155 53.324  -10.070 1.00 64.96  ? 218 GLN A NE2 1 
ATOM   1774 N N   . ARG A 1 220 ? 19.346 55.244  -3.955  1.00 59.86  ? 219 ARG A N   1 
ATOM   1775 C CA  . ARG A 1 220 ? 19.380 56.293  -2.937  1.00 57.73  ? 219 ARG A CA  1 
ATOM   1776 C C   . ARG A 1 220 ? 19.409 57.641  -3.643  1.00 62.74  ? 219 ARG A C   1 
ATOM   1777 O O   . ARG A 1 220 ? 20.437 58.020  -4.216  1.00 64.75  ? 219 ARG A O   1 
ATOM   1778 C CB  . ARG A 1 220 ? 20.582 56.145  -2.008  1.00 58.66  ? 219 ARG A CB  1 
ATOM   1779 C CG  . ARG A 1 220 ? 20.596 57.188  -0.903  1.00 56.73  ? 219 ARG A CG  1 
ATOM   1780 C CD  . ARG A 1 220 ? 21.975 57.387  -0.324  1.00 60.44  ? 219 ARG A CD  1 
ATOM   1781 N NE  . ARG A 1 220 ? 22.109 58.699  0.304   1.00 64.89  ? 219 ARG A NE  1 
ATOM   1782 C CZ  . ARG A 1 220 ? 21.755 58.969  1.559   1.00 71.11  ? 219 ARG A CZ  1 
ATOM   1783 N NH1 . ARG A 1 220 ? 21.918 60.193  2.048   1.00 68.91  ? 219 ARG A NH1 1 
ATOM   1784 N NH2 . ARG A 1 220 ? 21.248 58.013  2.333   1.00 67.61  ? 219 ARG A NH2 1 
ATOM   1785 N N   . ASP A 1 221 ? 18.292 58.370  -3.583  1.00 60.68  ? 220 ASP A N   1 
ATOM   1786 C CA  . ASP A 1 221 ? 18.135 59.633  -4.311  1.00 63.92  ? 220 ASP A CA  1 
ATOM   1787 C C   . ASP A 1 221 ? 18.416 59.448  -5.801  1.00 67.67  ? 220 ASP A C   1 
ATOM   1788 O O   . ASP A 1 221 ? 19.148 60.229  -6.412  1.00 69.14  ? 220 ASP A O   1 
ATOM   1789 C CB  . ASP A 1 221 ? 19.029 60.735  -3.732  1.00 62.63  ? 220 ASP A CB  1 
ATOM   1790 C CG  . ASP A 1 221 ? 18.771 60.991  -2.262  1.00 66.83  ? 220 ASP A CG  1 
ATOM   1791 O OD1 . ASP A 1 221 ? 17.631 61.373  -1.917  1.00 69.03  ? 220 ASP A OD1 1 
ATOM   1792 O OD2 . ASP A 1 221 ? 19.711 60.818  -1.457  1.00 63.69  ? 220 ASP A OD2 1 
ATOM   1793 N N   . GLY A 1 222 ? 17.832 58.403  -6.392  1.00 68.83  ? 221 GLY A N   1 
ATOM   1794 C CA  . GLY A 1 222 ? 18.087 58.053  -7.777  1.00 66.44  ? 221 GLY A CA  1 
ATOM   1795 C C   . GLY A 1 222 ? 19.368 57.284  -8.015  1.00 66.10  ? 221 GLY A C   1 
ATOM   1796 O O   . GLY A 1 222 ? 19.503 56.637  -9.062  1.00 66.77  ? 221 GLY A O   1 
ATOM   1797 N N   . GLU A 1 223 ? 20.304 57.327  -7.071  1.00 66.48  ? 222 GLU A N   1 
ATOM   1798 C CA  . GLU A 1 223 ? 21.596 56.667  -7.215  1.00 72.65  ? 222 GLU A CA  1 
ATOM   1799 C C   . GLU A 1 223 ? 21.459 55.159  -7.068  1.00 70.56  ? 222 GLU A C   1 
ATOM   1800 O O   . GLU A 1 223 ? 20.906 54.679  -6.078  1.00 67.05  ? 222 GLU A O   1 
ATOM   1801 C CB  . GLU A 1 223 ? 22.556 57.187  -6.146  1.00 69.99  ? 222 GLU A CB  1 
ATOM   1802 C CG  . GLU A 1 223 ? 24.012 56.989  -6.437  1.00 75.92  ? 222 GLU A CG  1 
ATOM   1803 C CD  . GLU A 1 223 ? 24.637 58.241  -7.007  1.00 85.60  ? 222 GLU A CD  1 
ATOM   1804 O OE1 . GLU A 1 223 ? 25.634 58.125  -7.753  1.00 82.74  ? 222 GLU A OE1 1 
ATOM   1805 O OE2 . GLU A 1 223 ? 24.116 59.343  -6.711  1.00 83.58  ? 222 GLU A OE2 1 
ATOM   1806 N N   . ASP A 1 224 ? 21.989 54.408  -8.033  1.00 74.10  ? 223 ASP A N   1 
ATOM   1807 C CA  . ASP A 1 224 ? 22.213 52.984  -7.810  1.00 71.98  ? 223 ASP A CA  1 
ATOM   1808 C C   . ASP A 1 224 ? 23.038 52.800  -6.544  1.00 69.08  ? 223 ASP A C   1 
ATOM   1809 O O   . ASP A 1 224 ? 24.089 53.423  -6.375  1.00 71.90  ? 223 ASP A O   1 
ATOM   1810 C CB  . ASP A 1 224 ? 22.925 52.349  -9.008  1.00 78.50  ? 223 ASP A CB  1 
ATOM   1811 C CG  . ASP A 1 224 ? 22.127 52.462  -10.297 1.00 80.43  ? 223 ASP A CG  1 
ATOM   1812 O OD1 . ASP A 1 224 ? 21.809 53.599  -10.722 1.00 72.64  ? 223 ASP A OD1 1 
ATOM   1813 O OD2 . ASP A 1 224 ? 21.823 51.403  -10.884 1.00 84.32  ? 223 ASP A OD2 1 
ATOM   1814 N N   . GLN A 1 225 ? 22.541 51.970  -5.637  1.00 67.98  ? 224 GLN A N   1 
ATOM   1815 C CA  . GLN A 1 225 ? 23.113 51.855  -4.299  1.00 74.20  ? 224 GLN A CA  1 
ATOM   1816 C C   . GLN A 1 225 ? 23.533 50.408  -4.080  1.00 76.02  ? 224 GLN A C   1 
ATOM   1817 O O   . GLN A 1 225 ? 22.849 49.635  -3.404  1.00 77.31  ? 224 GLN A O   1 
ATOM   1818 C CB  . GLN A 1 225 ? 22.105 52.334  -3.230  1.00 66.52  ? 224 GLN A CB  1 
ATOM   1819 C CG  . GLN A 1 225 ? 22.645 52.320  -1.818  1.00 62.11  ? 224 GLN A CG  1 
ATOM   1820 C CD  . GLN A 1 225 ? 23.577 53.479  -1.533  1.00 65.90  ? 224 GLN A CD  1 
ATOM   1821 O OE1 . GLN A 1 225 ? 23.738 54.379  -2.357  1.00 74.06  ? 224 GLN A OE1 1 
ATOM   1822 N NE2 . GLN A 1 225 ? 24.187 53.470  -0.358  1.00 66.64  ? 224 GLN A NE2 1 
ATOM   1823 N N   . THR A 1 226 ? 24.671 50.038  -4.661  1.00 79.42  ? 225 THR A N   1 
ATOM   1824 C CA  . THR A 1 226 ? 25.249 48.718  -4.436  1.00 82.76  ? 225 THR A CA  1 
ATOM   1825 C C   . THR A 1 226 ? 26.344 48.760  -3.375  1.00 86.97  ? 225 THR A C   1 
ATOM   1826 O O   . THR A 1 226 ? 27.332 48.016  -3.438  1.00 83.62  ? 225 THR A O   1 
ATOM   1827 C CB  . THR A 1 226 ? 25.760 48.120  -5.743  1.00 80.53  ? 225 THR A CB  1 
ATOM   1828 O OG1 . THR A 1 226 ? 26.338 46.837  -5.478  1.00 83.42  ? 225 THR A OG1 1 
ATOM   1829 C CG2 . THR A 1 226 ? 26.789 49.034  -6.397  1.00 81.02  ? 225 THR A CG2 1 
ATOM   1830 N N   . GLN A 1 227 ? 26.163 49.628  -2.373  1.00 85.84  ? 226 GLN A N   1 
ATOM   1831 C CA  . GLN A 1 227 ? 27.109 49.805  -1.276  1.00 89.81  ? 226 GLN A CA  1 
ATOM   1832 C C   . GLN A 1 227 ? 27.165 48.821  -0.113  1.00 86.70  ? 226 GLN A C   1 
ATOM   1833 O O   . GLN A 1 227 ? 28.183 48.148  0.086   1.00 89.38  ? 226 GLN A O   1 
ATOM   1834 C CB  . GLN A 1 227 ? 26.855 51.147  -0.576  1.00 84.73  ? 226 GLN A CB  1 
ATOM   1835 C CG  . GLN A 1 227 ? 27.812 51.511  0.564   1.00 87.28  ? 226 GLN A CG  1 
ATOM   1836 C CD  . GLN A 1 227 ? 29.178 50.859  0.450   1.00 92.37  ? 226 GLN A CD  1 
ATOM   1837 O OE1 . GLN A 1 227 ? 29.431 49.812  1.048   1.00 92.61  ? 226 GLN A OE1 1 
ATOM   1838 N NE2 . GLN A 1 227 ? 30.071 51.482  -0.315  1.00 91.55  ? 226 GLN A NE2 1 
ATOM   1839 N N   . ASP A 1 228 ? 26.090 48.739  0.665   1.00 84.03  ? 227 ASP A N   1 
ATOM   1840 C CA  . ASP A 1 228 ? 25.777 47.629  1.558   1.00 80.57  ? 227 ASP A CA  1 
ATOM   1841 C C   . ASP A 1 228 ? 24.361 47.146  1.259   1.00 70.30  ? 227 ASP A C   1 
ATOM   1842 O O   . ASP A 1 228 ? 23.446 47.253  2.078   1.00 71.73  ? 227 ASP A O   1 
ATOM   1843 C CB  . ASP A 1 228 ? 25.956 48.034  3.052   1.00 84.20  ? 227 ASP A CB  1 
ATOM   1844 N N   . THR A 1 229 ? 24.186 46.608  0.056   1.00 69.16  ? 228 THR A N   1 
ATOM   1845 C CA  . THR A 1 229 ? 22.906 46.059  -0.385  1.00 66.14  ? 228 THR A CA  1 
ATOM   1846 C C   . THR A 1 229 ? 23.020 44.536  -0.360  1.00 62.88  ? 228 THR A C   1 
ATOM   1847 O O   . THR A 1 229 ? 23.674 43.932  -1.216  1.00 67.88  ? 228 THR A O   1 
ATOM   1848 C CB  . THR A 1 229 ? 22.521 46.582  -1.769  1.00 62.66  ? 228 THR A CB  1 
ATOM   1849 O OG1 . THR A 1 229 ? 21.409 45.834  -2.275  1.00 64.93  ? 228 THR A OG1 1 
ATOM   1850 C CG2 . THR A 1 229 ? 23.665 46.435  -2.723  1.00 72.90  ? 228 THR A CG2 1 
ATOM   1851 N N   . GLU A 1 230 ? 22.397 43.919  0.638   1.00 52.02  ? 229 GLU A N   1 
ATOM   1852 C CA  . GLU A 1 230 ? 22.392 42.470  0.735   1.00 47.63  ? 229 GLU A CA  1 
ATOM   1853 C C   . GLU A 1 230 ? 21.250 41.887  -0.093  1.00 52.16  ? 229 GLU A C   1 
ATOM   1854 O O   . GLU A 1 230 ? 20.146 42.438  -0.135  1.00 48.96  ? 229 GLU A O   1 
ATOM   1855 C CB  . GLU A 1 230 ? 22.271 42.034  2.192   1.00 47.89  ? 229 GLU A CB  1 
ATOM   1856 C CG  . GLU A 1 230 ? 21.841 40.602  2.356   1.00 47.05  ? 229 GLU A CG  1 
ATOM   1857 C CD  . GLU A 1 230 ? 21.829 40.158  3.798   1.00 53.71  ? 229 GLU A CD  1 
ATOM   1858 O OE1 . GLU A 1 230 ? 22.039 38.947  4.039   1.00 55.02  ? 229 GLU A OE1 1 
ATOM   1859 O OE2 . GLU A 1 230 ? 21.604 41.013  4.688   1.00 58.27  ? 229 GLU A OE2 1 
ATOM   1860 N N   . LEU A 1 231 ? 21.527 40.767  -0.758  1.00 50.17  ? 230 LEU A N   1 
ATOM   1861 C CA  . LEU A 1 231 ? 20.592 40.129  -1.674  1.00 48.02  ? 230 LEU A CA  1 
ATOM   1862 C C   . LEU A 1 231 ? 20.649 38.628  -1.443  1.00 47.09  ? 230 LEU A C   1 
ATOM   1863 O O   . LEU A 1 231 ? 21.743 38.060  -1.390  1.00 48.75  ? 230 LEU A O   1 
ATOM   1864 C CB  . LEU A 1 231 ? 20.956 40.471  -3.123  1.00 49.66  ? 230 LEU A CB  1 
ATOM   1865 C CG  . LEU A 1 231 ? 20.084 40.013  -4.285  1.00 51.39  ? 230 LEU A CG  1 
ATOM   1866 C CD1 . LEU A 1 231 ? 18.733 40.732  -4.272  1.00 50.73  ? 230 LEU A CD1 1 
ATOM   1867 C CD2 . LEU A 1 231 ? 20.822 40.276  -5.587  1.00 49.39  ? 230 LEU A CD2 1 
ATOM   1868 N N   . VAL A 1 232 ? 19.488 37.988  -1.269  1.00 43.55  ? 231 VAL A N   1 
ATOM   1869 C CA  . VAL A 1 232 ? 19.479 36.542  -1.071  1.00 39.49  ? 231 VAL A CA  1 
ATOM   1870 C C   . VAL A 1 232 ? 19.227 35.843  -2.389  1.00 42.50  ? 231 VAL A C   1 
ATOM   1871 O O   . VAL A 1 232 ? 18.784 36.457  -3.367  1.00 38.24  ? 231 VAL A O   1 
ATOM   1872 C CB  . VAL A 1 232 ? 18.441 36.051  -0.042  1.00 36.34  ? 231 VAL A CB  1 
ATOM   1873 C CG1 . VAL A 1 232 ? 18.843 36.431  1.347   1.00 38.86  ? 231 VAL A CG1 1 
ATOM   1874 C CG2 . VAL A 1 232 ? 17.019 36.534  -0.395  1.00 34.09  ? 231 VAL A CG2 1 
ATOM   1875 N N   . GLU A 1 233 ? 19.495 34.534  -2.372  1.00 40.91  ? 232 GLU A N   1 
ATOM   1876 C CA  . GLU A 1 233 ? 19.271 33.566  -3.471  1.00 45.39  ? 232 GLU A CA  1 
ATOM   1877 C C   . GLU A 1 233 ? 17.741 33.518  -3.686  1.00 41.40  ? 232 GLU A C   1 
ATOM   1878 O O   . GLU A 1 233 ? 17.049 33.395  -2.695  1.00 34.45  ? 232 GLU A O   1 
ATOM   1879 C CB  . GLU A 1 233 ? 19.759 32.149  -3.072  1.00 40.45  ? 232 GLU A CB  1 
ATOM   1880 C CG  . GLU A 1 233 ? 21.243 31.735  -3.259  1.00 44.30  ? 232 GLU A CG  1 
ATOM   1881 C CD  . GLU A 1 233 ? 21.929 30.400  -2.800  1.00 62.34  ? 232 GLU A CD  1 
ATOM   1882 O OE1 . GLU A 1 233 ? 21.274 29.316  -2.490  1.00 58.48  ? 232 GLU A OE1 1 
ATOM   1883 O OE2 . GLU A 1 233 ? 23.182 30.398  -2.741  1.00 57.35  ? 232 GLU A OE2 1 
ATOM   1884 N N   . THR A 1 234 ? 17.230 33.692  -4.914  1.00 34.48  ? 233 THR A N   1 
ATOM   1885 C CA  . THR A 1 234 ? 15.833 33.423  -5.200  1.00 30.47  ? 233 THR A CA  1 
ATOM   1886 C C   . THR A 1 234 ? 15.489 31.998  -4.784  1.00 35.85  ? 233 THR A C   1 
ATOM   1887 O O   . THR A 1 234 ? 16.240 31.055  -5.055  1.00 37.12  ? 233 THR A O   1 
ATOM   1888 C CB  . THR A 1 234 ? 15.568 33.645  -6.682  1.00 36.39  ? 233 THR A CB  1 
ATOM   1889 O OG1 . THR A 1 234 ? 15.957 34.982  -7.021  1.00 34.61  ? 233 THR A OG1 1 
ATOM   1890 C CG2 . THR A 1 234 ? 14.087 33.437  -7.008  1.00 32.41  ? 233 THR A CG2 1 
ATOM   1891 N N   . ARG A 1 235 ? 14.370 31.848  -4.097  1.00 29.27  ? 234 ARG A N   1 
ATOM   1892 C CA  . ARG A 1 235 ? 14.024 30.602  -3.438  1.00 33.53  ? 234 ARG A CA  1 
ATOM   1893 C C   . ARG A 1 235 ? 12.638 30.160  -3.868  1.00 33.37  ? 234 ARG A C   1 
ATOM   1894 O O   . ARG A 1 235 ? 11.813 30.984  -4.272  1.00 31.64  ? 234 ARG A O   1 
ATOM   1895 C CB  . ARG A 1 235 ? 14.074 30.758  -1.909  1.00 31.66  ? 234 ARG A CB  1 
ATOM   1896 C CG  . ARG A 1 235 ? 13.237 31.919  -1.387  1.00 29.29  ? 234 ARG A CG  1 
ATOM   1897 C CD  . ARG A 1 235 ? 13.527 32.200  0.075   1.00 29.82  ? 234 ARG A CD  1 
ATOM   1898 N NE  . ARG A 1 235 ? 12.358 32.768  0.748   1.00 33.06  ? 234 ARG A NE  1 
ATOM   1899 C CZ  . ARG A 1 235 ? 12.403 33.473  1.879   1.00 33.88  ? 234 ARG A CZ  1 
ATOM   1900 N NH1 . ARG A 1 235 ? 13.559 33.707  2.498   1.00 29.39  ? 234 ARG A NH1 1 
ATOM   1901 N NH2 . ARG A 1 235 ? 11.278 33.932  2.405   1.00 35.50  ? 234 ARG A NH2 1 
ATOM   1902 N N   . PRO A 1 236 ? 12.355 28.859  -3.806  1.00 34.52  ? 235 PRO A N   1 
ATOM   1903 C CA  . PRO A 1 236 ? 11.020 28.375  -4.168  1.00 29.87  ? 235 PRO A CA  1 
ATOM   1904 C C   . PRO A 1 236 ? 10.049 28.427  -3.004  1.00 30.47  ? 235 PRO A C   1 
ATOM   1905 O O   . PRO A 1 236 ? 10.342 28.011  -1.880  1.00 34.96  ? 235 PRO A O   1 
ATOM   1906 C CB  . PRO A 1 236 ? 11.286 26.922  -4.592  1.00 32.16  ? 235 PRO A CB  1 
ATOM   1907 C CG  . PRO A 1 236 ? 12.524 26.526  -3.781  1.00 29.21  ? 235 PRO A CG  1 
ATOM   1908 C CD  . PRO A 1 236 ? 13.345 27.768  -3.685  1.00 30.27  ? 235 PRO A CD  1 
ATOM   1909 N N   . ALA A 1 237 ? 8.851  28.922  -3.298  1.00 30.74  ? 236 ALA A N   1 
ATOM   1910 C CA  . ALA A 1 237 ? 7.768  28.841  -2.329  1.00 32.94  ? 236 ALA A CA  1 
ATOM   1911 C C   . ALA A 1 237 ? 7.356  27.398  -2.086  1.00 32.53  ? 236 ALA A C   1 
ATOM   1912 O O   . ALA A 1 237 ? 6.809  27.075  -1.022  1.00 33.14  ? 236 ALA A O   1 
ATOM   1913 C CB  . ALA A 1 237 ? 6.572  29.663  -2.818  1.00 30.92  ? 236 ALA A CB  1 
ATOM   1914 N N   . GLY A 1 238 ? 7.606  26.523  -3.059  1.00 33.38  ? 237 GLY A N   1 
ATOM   1915 C CA  . GLY A 1 238 ? 7.160  25.148  -3.007  1.00 34.34  ? 237 GLY A CA  1 
ATOM   1916 C C   . GLY A 1 238 ? 5.799  24.885  -3.619  1.00 37.56  ? 237 GLY A C   1 
ATOM   1917 O O   . GLY A 1 238 ? 5.367  23.732  -3.629  1.00 34.22  ? 237 GLY A O   1 
ATOM   1918 N N   . ASP A 1 239 ? 5.101  25.919  -4.105  1.00 37.56  ? 238 ASP A N   1 
ATOM   1919 C CA  . ASP A 1 239 ? 3.819  25.771  -4.787  1.00 35.13  ? 238 ASP A CA  1 
ATOM   1920 C C   . ASP A 1 239 ? 3.913  26.174  -6.257  1.00 39.42  ? 238 ASP A C   1 
ATOM   1921 O O   . ASP A 1 239 ? 2.892  26.448  -6.898  1.00 36.96  ? 238 ASP A O   1 
ATOM   1922 C CB  . ASP A 1 239 ? 2.727  26.581  -4.073  1.00 36.35  ? 238 ASP A CB  1 
ATOM   1923 C CG  . ASP A 1 239 ? 2.950  28.109  -4.149  1.00 38.84  ? 238 ASP A CG  1 
ATOM   1924 O OD1 . ASP A 1 239 ? 3.962  28.559  -4.722  1.00 37.47  ? 238 ASP A OD1 1 
ATOM   1925 O OD2 . ASP A 1 239 ? 2.105  28.864  -3.614  1.00 40.84  ? 238 ASP A OD2 1 
ATOM   1926 N N   . GLY A 1 240 ? 5.125  26.238  -6.790  1.00 35.26  ? 239 GLY A N   1 
ATOM   1927 C CA  . GLY A 1 240 ? 5.352  26.643  -8.154  1.00 36.01  ? 239 GLY A CA  1 
ATOM   1928 C C   . GLY A 1 240 ? 5.742  28.090  -8.339  1.00 40.03  ? 239 GLY A C   1 
ATOM   1929 O O   . GLY A 1 240 ? 6.001  28.493  -9.478  1.00 39.32  ? 239 GLY A O   1 
ATOM   1930 N N   . THR A 1 241 ? 5.779  28.887  -7.271  1.00 37.53  ? 240 THR A N   1 
ATOM   1931 C CA  . THR A 1 241 ? 6.200  30.281  -7.342  1.00 35.46  ? 240 THR A CA  1 
ATOM   1932 C C   . THR A 1 241 ? 7.487  30.474  -6.548  1.00 33.66  ? 240 THR A C   1 
ATOM   1933 O O   . THR A 1 241 ? 7.964  29.568  -5.860  1.00 30.50  ? 240 THR A O   1 
ATOM   1934 C CB  . THR A 1 241 ? 5.109  31.228  -6.817  1.00 37.32  ? 240 THR A CB  1 
ATOM   1935 O OG1 . THR A 1 241 ? 4.940  31.022  -5.414  1.00 35.49  ? 240 THR A OG1 1 
ATOM   1936 C CG2 . THR A 1 241 ? 3.770  30.978  -7.520  1.00 39.39  ? 240 THR A CG2 1 
ATOM   1937 N N   . PHE A 1 242 ? 8.039  31.683  -6.645  1.00 28.65  ? 241 PHE A N   1 
ATOM   1938 C CA  . PHE A 1 242 ? 9.360  31.994  -6.122  1.00 31.65  ? 241 PHE A CA  1 
ATOM   1939 C C   . PHE A 1 242 ? 9.308  33.237  -5.227  1.00 35.59  ? 241 PHE A C   1 
ATOM   1940 O O   . PHE A 1 242 ? 8.323  33.989  -5.219  1.00 28.41  ? 241 PHE A O   1 
ATOM   1941 C CB  . PHE A 1 242 ? 10.361 32.151  -7.291  1.00 30.45  ? 241 PHE A CB  1 
ATOM   1942 C CG  . PHE A 1 242 ? 10.617 30.847  -8.026  1.00 32.62  ? 241 PHE A CG  1 
ATOM   1943 C CD1 . PHE A 1 242 ? 11.584 29.950  -7.571  1.00 36.24  ? 241 PHE A CD1 1 
ATOM   1944 C CD2 . PHE A 1 242 ? 9.844  30.484  -9.113  1.00 32.34  ? 241 PHE A CD2 1 
ATOM   1945 C CE1 . PHE A 1 242 ? 11.791 28.731  -8.213  1.00 37.24  ? 241 PHE A CE1 1 
ATOM   1946 C CE2 . PHE A 1 242 ? 10.055 29.284  -9.765  1.00 37.10  ? 241 PHE A CE2 1 
ATOM   1947 C CZ  . PHE A 1 242 ? 11.030 28.405  -9.315  1.00 35.98  ? 241 PHE A CZ  1 
ATOM   1948 N N   . GLN A 1 243 ? 10.379 33.428  -4.447  1.00 25.65  ? 242 GLN A N   1 
ATOM   1949 C CA  . GLN A 1 243 ? 10.502 34.543  -3.515  1.00 31.55  ? 242 GLN A CA  1 
ATOM   1950 C C   . GLN A 1 243 ? 11.914 35.094  -3.543  1.00 32.05  ? 242 GLN A C   1 
ATOM   1951 O O   . GLN A 1 243 ? 12.879 34.345  -3.710  1.00 34.18  ? 242 GLN A O   1 
ATOM   1952 C CB  . GLN A 1 243 ? 10.193 34.143  -2.062  1.00 26.39  ? 242 GLN A CB  1 
ATOM   1953 C CG  . GLN A 1 243 ? 8.882  33.386  -1.884  1.00 30.02  ? 242 GLN A CG  1 
ATOM   1954 C CD  . GLN A 1 243 ? 8.740  32.842  -0.477  1.00 27.51  ? 242 GLN A CD  1 
ATOM   1955 O OE1 . GLN A 1 243 ? 9.683  32.901  0.311   1.00 24.85  ? 242 GLN A OE1 1 
ATOM   1956 N NE2 . GLN A 1 243 ? 7.575  32.293  -0.164  1.00 27.41  ? 242 GLN A NE2 1 
ATOM   1957 N N   . LYS A 1 244 ? 12.030 36.402  -3.318  1.00 25.47  ? 243 LYS A N   1 
ATOM   1958 C CA  . LYS A 1 244 ? 13.335 37.025  -3.182  1.00 26.53  ? 243 LYS A CA  1 
ATOM   1959 C C   . LYS A 1 244 ? 13.212 38.256  -2.294  1.00 29.60  ? 243 LYS A C   1 
ATOM   1960 O O   . LYS A 1 244 ? 12.126 38.824  -2.130  1.00 32.24  ? 243 LYS A O   1 
ATOM   1961 C CB  . LYS A 1 244 ? 13.923 37.398  -4.553  1.00 28.88  ? 243 LYS A CB  1 
ATOM   1962 C CG  . LYS A 1 244 ? 15.442 37.538  -4.563  1.00 30.87  ? 243 LYS A CG  1 
ATOM   1963 C CD  . LYS A 1 244 ? 15.951 38.056  -5.928  1.00 31.82  ? 243 LYS A CD  1 
ATOM   1964 C CE  . LYS A 1 244 ? 17.385 37.659  -6.219  1.00 31.96  ? 243 LYS A CE  1 
ATOM   1965 N NZ  . LYS A 1 244 ? 18.105 37.025  -5.085  1.00 51.33  ? 243 LYS A NZ  1 
ATOM   1966 N N   . TRP A 1 245 ? 14.339 38.664  -1.713  1.00 30.50  ? 244 TRP A N   1 
ATOM   1967 C CA  . TRP A 1 245 ? 14.388 39.965  -1.063  1.00 32.51  ? 244 TRP A CA  1 
ATOM   1968 C C   . TRP A 1 245 ? 15.765 40.593  -1.208  1.00 38.23  ? 244 TRP A C   1 
ATOM   1969 O O   . TRP A 1 245 ? 16.767 39.912  -1.450  1.00 39.04  ? 244 TRP A O   1 
ATOM   1970 C CB  . TRP A 1 245 ? 13.980 39.895  0.405   1.00 27.50  ? 244 TRP A CB  1 
ATOM   1971 C CG  . TRP A 1 245 ? 14.828 39.077  1.343   1.00 35.25  ? 244 TRP A CG  1 
ATOM   1972 C CD1 . TRP A 1 245 ? 14.501 37.872  1.889   1.00 32.46  ? 244 TRP A CD1 1 
ATOM   1973 C CD2 . TRP A 1 245 ? 16.092 39.445  1.917   1.00 33.98  ? 244 TRP A CD2 1 
ATOM   1974 N NE1 . TRP A 1 245 ? 15.489 37.455  2.741   1.00 31.50  ? 244 TRP A NE1 1 
ATOM   1975 C CE2 . TRP A 1 245 ? 16.478 38.401  2.777   1.00 36.06  ? 244 TRP A CE2 1 
ATOM   1976 C CE3 . TRP A 1 245 ? 16.943 40.549  1.773   1.00 39.75  ? 244 TRP A CE3 1 
ATOM   1977 C CZ2 . TRP A 1 245 ? 17.672 38.432  3.511   1.00 39.16  ? 244 TRP A CZ2 1 
ATOM   1978 C CZ3 . TRP A 1 245 ? 18.140 40.568  2.492   1.00 42.18  ? 244 TRP A CZ3 1 
ATOM   1979 C CH2 . TRP A 1 245 ? 18.492 39.511  3.340   1.00 38.46  ? 244 TRP A CH2 1 
ATOM   1980 N N   . ALA A 1 246 ? 15.778 41.923  -1.091  1.00 33.37  ? 245 ALA A N   1 
ATOM   1981 C CA  . ALA A 1 246 ? 16.972 42.749  -1.150  1.00 32.51  ? 245 ALA A CA  1 
ATOM   1982 C C   . ALA A 1 246 ? 16.915 43.716  0.022   1.00 38.41  ? 245 ALA A C   1 
ATOM   1983 O O   . ALA A 1 246 ? 15.867 44.324  0.271   1.00 36.05  ? 245 ALA A O   1 
ATOM   1984 C CB  . ALA A 1 246 ? 17.057 43.525  -2.472  1.00 33.70  ? 245 ALA A CB  1 
ATOM   1985 N N   . ALA A 1 247 ? 18.028 43.858  0.742   1.00 39.40  ? 246 ALA A N   1 
ATOM   1986 C CA  . ALA A 1 247 ? 18.070 44.712  1.920   1.00 41.27  ? 246 ALA A CA  1 
ATOM   1987 C C   . ALA A 1 247 ? 19.210 45.712  1.817   1.00 44.14  ? 246 ALA A C   1 
ATOM   1988 O O   . ALA A 1 247 ? 20.236 45.461  1.184   1.00 45.41  ? 246 ALA A O   1 
ATOM   1989 C CB  . ALA A 1 247 ? 18.218 43.909  3.216   1.00 33.46  ? 246 ALA A CB  1 
ATOM   1990 N N   . VAL A 1 248 ? 19.009 46.858  2.448   1.00 45.10  ? 247 VAL A N   1 
ATOM   1991 C CA  . VAL A 1 248 ? 20.041 47.873  2.583   1.00 50.98  ? 247 VAL A CA  1 
ATOM   1992 C C   . VAL A 1 248 ? 19.939 48.453  3.989   1.00 46.44  ? 247 VAL A C   1 
ATOM   1993 O O   . VAL A 1 248 ? 18.840 48.603  4.533   1.00 41.79  ? 247 VAL A O   1 
ATOM   1994 C CB  . VAL A 1 248 ? 19.901 48.964  1.498   1.00 48.85  ? 247 VAL A CB  1 
ATOM   1995 C CG1 . VAL A 1 248 ? 18.566 49.684  1.641   1.00 41.23  ? 247 VAL A CG1 1 
ATOM   1996 C CG2 . VAL A 1 248 ? 21.071 49.944  1.557   1.00 55.47  ? 247 VAL A CG2 1 
ATOM   1997 N N   . VAL A 1 249 ? 21.087 48.735  4.592   1.00 54.45  ? 248 VAL A N   1 
ATOM   1998 C CA  . VAL A 1 249 ? 21.145 49.409  5.884   1.00 48.79  ? 248 VAL A CA  1 
ATOM   1999 C C   . VAL A 1 249 ? 21.201 50.911  5.636   1.00 52.34  ? 248 VAL A C   1 
ATOM   2000 O O   . VAL A 1 249 ? 22.007 51.390  4.829   1.00 53.09  ? 248 VAL A O   1 
ATOM   2001 C CB  . VAL A 1 249 ? 22.352 48.928  6.703   1.00 50.03  ? 248 VAL A CB  1 
ATOM   2002 C CG1 . VAL A 1 249 ? 22.353 49.569  8.080   1.00 51.56  ? 248 VAL A CG1 1 
ATOM   2003 C CG2 . VAL A 1 249 ? 22.324 47.413  6.826   1.00 52.21  ? 248 VAL A CG2 1 
ATOM   2004 N N   . VAL A 1 250 ? 20.324 51.653  6.305   1.00 50.32  ? 249 VAL A N   1 
ATOM   2005 C CA  . VAL A 1 250 ? 20.196 53.086  6.056   1.00 50.29  ? 249 VAL A CA  1 
ATOM   2006 C C   . VAL A 1 250 ? 20.344 53.854  7.365   1.00 50.25  ? 249 VAL A C   1 
ATOM   2007 O O   . VAL A 1 250 ? 20.045 53.317  8.445   1.00 46.72  ? 249 VAL A O   1 
ATOM   2008 C CB  . VAL A 1 250 ? 18.859 53.408  5.363   1.00 54.06  ? 249 VAL A CB  1 
ATOM   2009 C CG1 . VAL A 1 250 ? 18.677 52.542  4.129   1.00 48.77  ? 249 VAL A CG1 1 
ATOM   2010 C CG2 . VAL A 1 250 ? 17.685 53.235  6.325   1.00 50.33  ? 249 VAL A CG2 1 
ATOM   2011 N N   . PRO A 1 251 ? 20.805 55.106  7.322   1.00 54.37  ? 250 PRO A N   1 
ATOM   2012 C CA  . PRO A 1 251 ? 20.901 55.900  8.557   1.00 57.01  ? 250 PRO A CA  1 
ATOM   2013 C C   . PRO A 1 251 ? 19.515 56.283  9.062   1.00 49.72  ? 250 PRO A C   1 
ATOM   2014 O O   . PRO A 1 251 ? 18.660 56.728  8.292   1.00 47.14  ? 250 PRO A O   1 
ATOM   2015 C CB  . PRO A 1 251 ? 21.717 57.134  8.136   1.00 54.17  ? 250 PRO A CB  1 
ATOM   2016 C CG  . PRO A 1 251 ? 22.164 56.885  6.722   1.00 53.98  ? 250 PRO A CG  1 
ATOM   2017 C CD  . PRO A 1 251 ? 21.226 55.873  6.139   1.00 53.14  ? 250 PRO A CD  1 
ATOM   2018 N N   . SER A 1 252 ? 19.305 56.116  10.366  1.00 45.86  ? 251 SER A N   1 
ATOM   2019 C CA  . SER A 1 252 ? 17.985 56.330  10.948  1.00 50.36  ? 251 SER A CA  1 
ATOM   2020 C C   . SER A 1 252 ? 17.502 57.746  10.664  1.00 48.68  ? 251 SER A C   1 
ATOM   2021 O O   . SER A 1 252 ? 18.230 58.717  10.875  1.00 48.93  ? 251 SER A O   1 
ATOM   2022 C CB  . SER A 1 252 ? 18.028 56.075  12.452  1.00 53.09  ? 251 SER A CB  1 
ATOM   2023 O OG  . SER A 1 252 ? 16.783 55.596  12.922  1.00 63.29  ? 251 SER A OG  1 
ATOM   2024 N N   . GLY A 1 253 ? 16.276 57.862  10.162  1.00 48.99  ? 252 GLY A N   1 
ATOM   2025 C CA  . GLY A 1 253 ? 15.759 59.138  9.727   1.00 47.51  ? 252 GLY A CA  1 
ATOM   2026 C C   . GLY A 1 253 ? 15.986 59.463  8.262   1.00 45.99  ? 252 GLY A C   1 
ATOM   2027 O O   . GLY A 1 253 ? 15.430 60.452  7.776   1.00 41.57  ? 252 GLY A O   1 
ATOM   2028 N N   . GLU A 1 254 ? 16.774 58.669  7.539   1.00 43.09  ? 253 GLU A N   1 
ATOM   2029 C CA  . GLU A 1 254 ? 16.970 58.865  6.107   1.00 47.76  ? 253 GLU A CA  1 
ATOM   2030 C C   . GLU A 1 254 ? 16.137 57.901  5.267   1.00 48.10  ? 253 GLU A C   1 
ATOM   2031 O O   . GLU A 1 254 ? 16.385 57.764  4.061   1.00 42.54  ? 253 GLU A O   1 
ATOM   2032 C CB  . GLU A 1 254 ? 18.448 58.712  5.739   1.00 52.01  ? 253 GLU A CB  1 
ATOM   2033 C CG  . GLU A 1 254 ? 19.424 59.536  6.571   1.00 56.94  ? 253 GLU A CG  1 
ATOM   2034 C CD  . GLU A 1 254 ? 20.725 59.821  5.816   1.00 64.54  ? 253 GLU A CD  1 
ATOM   2035 O OE1 . GLU A 1 254 ? 21.574 60.580  6.340   1.00 64.73  ? 253 GLU A OE1 1 
ATOM   2036 O OE2 . GLU A 1 254 ? 20.892 59.280  4.696   1.00 62.05  ? 253 GLU A OE2 1 
ATOM   2037 N N   . GLU A 1 255 ? 15.142 57.252  5.879   1.00 39.56  ? 254 GLU A N   1 
ATOM   2038 C CA  . GLU A 1 255 ? 14.455 56.138  5.231   1.00 39.77  ? 254 GLU A CA  1 
ATOM   2039 C C   . GLU A 1 255 ? 13.839 56.539  3.895   1.00 43.01  ? 254 GLU A C   1 
ATOM   2040 O O   . GLU A 1 255 ? 13.858 55.752  2.939   1.00 38.57  ? 254 GLU A O   1 
ATOM   2041 C CB  . GLU A 1 255 ? 13.390 55.572  6.168   1.00 34.45  ? 254 GLU A CB  1 
ATOM   2042 C CG  . GLU A 1 255 ? 13.933 54.599  7.197   1.00 32.92  ? 254 GLU A CG  1 
ATOM   2043 C CD  . GLU A 1 255 ? 14.337 55.280  8.502   1.00 41.24  ? 254 GLU A CD  1 
ATOM   2044 O OE1 . GLU A 1 255 ? 14.639 54.564  9.493   1.00 39.30  ? 254 GLU A OE1 1 
ATOM   2045 O OE2 . GLU A 1 255 ? 14.355 56.530  8.532   1.00 43.24  ? 254 GLU A OE2 1 
ATOM   2046 N N   . GLN A 1 256 ? 13.303 57.763  3.796   1.00 41.22  ? 255 GLN A N   1 
ATOM   2047 C CA  . GLN A 1 256 ? 12.563 58.163  2.599   1.00 43.91  ? 255 GLN A CA  1 
ATOM   2048 C C   . GLN A 1 256 ? 13.457 58.550  1.423   1.00 43.15  ? 255 GLN A C   1 
ATOM   2049 O O   . GLN A 1 256 ? 12.936 58.794  0.327   1.00 42.68  ? 255 GLN A O   1 
ATOM   2050 C CB  . GLN A 1 256 ? 11.612 59.324  2.915   1.00 39.63  ? 255 GLN A CB  1 
ATOM   2051 C CG  . GLN A 1 256 ? 10.337 58.889  3.615   1.00 39.61  ? 255 GLN A CG  1 
ATOM   2052 C CD  . GLN A 1 256 ? 10.571 58.581  5.092   1.00 41.45  ? 255 GLN A CD  1 
ATOM   2053 O OE1 . GLN A 1 256 ? 11.171 59.377  5.811   1.00 35.87  ? 255 GLN A OE1 1 
ATOM   2054 N NE2 . GLN A 1 256 ? 10.105 57.420  5.541   1.00 38.04  ? 255 GLN A NE2 1 
ATOM   2055 N N   . ARG A 1 257 ? 14.774 58.615  1.620   1.00 46.83  ? 256 ARG A N   1 
ATOM   2056 C CA  . ARG A 1 257 ? 15.712 58.842  0.532   1.00 44.90  ? 256 ARG A CA  1 
ATOM   2057 C C   . ARG A 1 257 ? 15.982 57.585  -0.283  1.00 51.47  ? 256 ARG A C   1 
ATOM   2058 O O   . ARG A 1 257 ? 16.679 57.665  -1.300  1.00 51.40  ? 256 ARG A O   1 
ATOM   2059 C CB  . ARG A 1 257 ? 17.033 59.378  1.085   1.00 49.60  ? 256 ARG A CB  1 
ATOM   2060 C CG  . ARG A 1 257 ? 17.002 60.847  1.478   1.00 51.14  ? 256 ARG A CG  1 
ATOM   2061 C CD  . ARG A 1 257 ? 18.313 61.266  2.132   1.00 58.74  ? 256 ARG A CD  1 
ATOM   2062 N NE  . ARG A 1 257 ? 19.427 61.316  1.184   1.00 65.64  ? 256 ARG A NE  1 
ATOM   2063 C CZ  . ARG A 1 257 ? 20.183 62.391  0.957   1.00 71.35  ? 256 ARG A CZ  1 
ATOM   2064 N NH1 . ARG A 1 257 ? 19.956 63.525  1.608   1.00 70.61  ? 256 ARG A NH1 1 
ATOM   2065 N NH2 . ARG A 1 257 ? 21.172 62.327  0.074   1.00 69.64  ? 256 ARG A NH2 1 
ATOM   2066 N N   . TYR A 1 258 ? 15.448 56.436  0.129   1.00 50.09  ? 257 TYR A N   1 
ATOM   2067 C CA  . TYR A 1 258 ? 15.718 55.157  -0.514  1.00 45.71  ? 257 TYR A CA  1 
ATOM   2068 C C   . TYR A 1 258 ? 14.489 54.648  -1.259  1.00 43.83  ? 257 TYR A C   1 
ATOM   2069 O O   . TYR A 1 258 ? 13.355 54.813  -0.799  1.00 44.99  ? 257 TYR A O   1 
ATOM   2070 C CB  . TYR A 1 258 ? 16.162 54.120  0.515   1.00 41.07  ? 257 TYR A CB  1 
ATOM   2071 C CG  . TYR A 1 258 ? 17.566 54.332  1.017   1.00 47.31  ? 257 TYR A CG  1 
ATOM   2072 C CD1 . TYR A 1 258 ? 17.845 55.307  1.969   1.00 53.01  ? 257 TYR A CD1 1 
ATOM   2073 C CD2 . TYR A 1 258 ? 18.619 53.557  0.545   1.00 49.23  ? 257 TYR A CD2 1 
ATOM   2074 C CE1 . TYR A 1 258 ? 19.140 55.505  2.435   1.00 56.90  ? 257 TYR A CE1 1 
ATOM   2075 C CE2 . TYR A 1 258 ? 19.912 53.745  1.001   1.00 54.57  ? 257 TYR A CE2 1 
ATOM   2076 C CZ  . TYR A 1 258 ? 20.169 54.722  1.949   1.00 57.47  ? 257 TYR A CZ  1 
ATOM   2077 O OH  . TYR A 1 258 ? 21.450 54.919  2.418   1.00 56.24  ? 257 TYR A OH  1 
ATOM   2078 N N   . THR A 1 259 ? 14.717 54.024  -2.409  1.00 41.67  ? 258 THR A N   1 
ATOM   2079 C CA  . THR A 1 259 ? 13.655 53.396  -3.179  1.00 41.94  ? 258 THR A CA  1 
ATOM   2080 C C   . THR A 1 259 ? 14.084 51.987  -3.563  1.00 46.14  ? 258 THR A C   1 
ATOM   2081 O O   . THR A 1 259 ? 15.275 51.699  -3.702  1.00 48.41  ? 258 THR A O   1 
ATOM   2082 C CB  . THR A 1 259 ? 13.303 54.193  -4.459  1.00 42.23  ? 258 THR A CB  1 
ATOM   2083 O OG1 . THR A 1 259 ? 14.506 54.608  -5.123  1.00 45.77  ? 258 THR A OG1 1 
ATOM   2084 C CG2 . THR A 1 259 ? 12.472 55.420  -4.115  1.00 45.59  ? 258 THR A CG2 1 
ATOM   2085 N N   . CYS A 1 260 ? 13.104 51.108  -3.736  1.00 44.32  ? 259 CYS A N   1 
ATOM   2086 C CA  . CYS A 1 260 ? 13.350 49.752  -4.194  1.00 44.86  ? 259 CYS A CA  1 
ATOM   2087 C C   . CYS A 1 260 ? 12.640 49.553  -5.525  1.00 43.16  ? 259 CYS A C   1 
ATOM   2088 O O   . CYS A 1 260 ? 11.457 49.878  -5.650  1.00 41.19  ? 259 CYS A O   1 
ATOM   2089 C CB  . CYS A 1 260 ? 12.872 48.712  -3.174  1.00 39.79  ? 259 CYS A CB  1 
ATOM   2090 S SG  . CYS A 1 260 ? 12.902 47.050  -3.899  1.00 45.97  ? 259 CYS A SG  1 
ATOM   2091 N N   . HIS A 1 261 ? 13.351 49.010  -6.512  1.00 40.24  ? 260 HIS A N   1 
ATOM   2092 C CA  . HIS A 1 261 ? 12.800 48.846  -7.855  1.00 48.57  ? 260 HIS A CA  1 
ATOM   2093 C C   . HIS A 1 261 ? 12.704 47.369  -8.214  1.00 43.92  ? 260 HIS A C   1 
ATOM   2094 O O   . HIS A 1 261 ? 13.663 46.609  -8.039  1.00 42.72  ? 260 HIS A O   1 
ATOM   2095 C CB  . HIS A 1 261 ? 13.633 49.625  -8.875  1.00 47.97  ? 260 HIS A CB  1 
ATOM   2096 C CG  . HIS A 1 261 ? 13.845 51.054  -8.484  1.00 49.94  ? 260 HIS A CG  1 
ATOM   2097 N ND1 . HIS A 1 261 ? 12.998 52.070  -8.880  1.00 50.44  ? 260 HIS A ND1 1 
ATOM   2098 C CD2 . HIS A 1 261 ? 14.776 51.630  -7.684  1.00 49.35  ? 260 HIS A CD2 1 
ATOM   2099 C CE1 . HIS A 1 261 ? 13.418 53.214  -8.366  1.00 49.70  ? 260 HIS A CE1 1 
ATOM   2100 N NE2 . HIS A 1 261 ? 14.494 52.974  -7.636  1.00 49.88  ? 260 HIS A NE2 1 
ATOM   2101 N N   . VAL A 1 262 ? 11.531 46.963  -8.687  1.00 41.77  ? 261 VAL A N   1 
ATOM   2102 C CA  . VAL A 1 262 ? 11.244 45.563  -8.963  1.00 42.65  ? 261 VAL A CA  1 
ATOM   2103 C C   . VAL A 1 262 ? 10.979 45.407  -10.454 1.00 45.57  ? 261 VAL A C   1 
ATOM   2104 O O   . VAL A 1 262 ? 10.065 46.040  -10.999 1.00 44.62  ? 261 VAL A O   1 
ATOM   2105 C CB  . VAL A 1 262 ? 10.057 45.051  -8.139  1.00 38.83  ? 261 VAL A CB  1 
ATOM   2106 C CG1 . VAL A 1 262 ? 9.880  43.563  -8.375  1.00 36.59  ? 261 VAL A CG1 1 
ATOM   2107 C CG2 . VAL A 1 262 ? 10.293 45.331  -6.667  1.00 39.87  ? 261 VAL A CG2 1 
ATOM   2108 N N   . GLN A 1 263 ? 11.780 44.564  -11.106 1.00 43.44  ? 262 GLN A N   1 
ATOM   2109 C CA  . GLN A 1 263 ? 11.653 44.258  -12.525 1.00 45.61  ? 262 GLN A CA  1 
ATOM   2110 C C   . GLN A 1 263 ? 11.313 42.779  -12.657 1.00 40.31  ? 262 GLN A C   1 
ATOM   2111 O O   . GLN A 1 263 ? 12.100 41.917  -12.249 1.00 41.96  ? 262 GLN A O   1 
ATOM   2112 C CB  . GLN A 1 263 ? 12.942 44.584  -13.289 1.00 44.59  ? 262 GLN A CB  1 
ATOM   2113 C CG  . GLN A 1 263 ? 13.157 46.059  -13.624 1.00 49.78  ? 262 GLN A CG  1 
ATOM   2114 C CD  . GLN A 1 263 ? 14.032 46.794  -12.605 1.00 58.37  ? 262 GLN A CD  1 
ATOM   2115 O OE1 . GLN A 1 263 ? 14.633 46.181  -11.710 1.00 59.10  ? 262 GLN A OE1 1 
ATOM   2116 N NE2 . GLN A 1 263 ? 14.099 48.121  -12.733 1.00 61.36  ? 262 GLN A NE2 1 
ATOM   2117 N N   . HIS A 1 264 ? 10.142 42.491  -13.208 1.00 40.00  ? 263 HIS A N   1 
ATOM   2118 C CA  . HIS A 1 264 ? 9.736  41.124  -13.474 1.00 40.06  ? 263 HIS A CA  1 
ATOM   2119 C C   . HIS A 1 264 ? 8.990  41.090  -14.796 1.00 44.64  ? 263 HIS A C   1 
ATOM   2120 O O   . HIS A 1 264 ? 8.348  42.067  -15.186 1.00 45.79  ? 263 HIS A O   1 
ATOM   2121 C CB  . HIS A 1 264 ? 8.857  40.574  -12.355 1.00 38.82  ? 263 HIS A CB  1 
ATOM   2122 C CG  . HIS A 1 264 ? 8.566  39.112  -12.479 1.00 38.58  ? 263 HIS A CG  1 
ATOM   2123 N ND1 . HIS A 1 264 ? 7.386  38.631  -13.005 1.00 38.03  ? 263 HIS A ND1 1 
ATOM   2124 C CD2 . HIS A 1 264 ? 9.295  38.024  -12.132 1.00 35.51  ? 263 HIS A CD2 1 
ATOM   2125 C CE1 . HIS A 1 264 ? 7.403  37.310  -12.987 1.00 38.27  ? 263 HIS A CE1 1 
ATOM   2126 N NE2 . HIS A 1 264 ? 8.549  36.916  -12.459 1.00 37.87  ? 263 HIS A NE2 1 
ATOM   2127 N N   . GLU A 1 265 ? 9.077  39.947  -15.479 1.00 47.56  ? 264 GLU A N   1 
ATOM   2128 C CA  . GLU A 1 265 ? 8.395  39.785  -16.760 1.00 47.91  ? 264 GLU A CA  1 
ATOM   2129 C C   . GLU A 1 265 ? 6.881  39.952  -16.623 1.00 49.03  ? 264 GLU A C   1 
ATOM   2130 O O   . GLU A 1 265 ? 6.209  40.331  -17.589 1.00 46.84  ? 264 GLU A O   1 
ATOM   2131 C CB  . GLU A 1 265 ? 8.769  38.421  -17.349 1.00 49.86  ? 264 GLU A CB  1 
ATOM   2132 C CG  . GLU A 1 265 ? 7.695  37.702  -18.137 1.00 56.27  ? 264 GLU A CG  1 
ATOM   2133 C CD  . GLU A 1 265 ? 8.102  36.274  -18.492 1.00 64.22  ? 264 GLU A CD  1 
ATOM   2134 O OE1 . GLU A 1 265 ? 7.261  35.523  -19.038 1.00 67.84  ? 264 GLU A OE1 1 
ATOM   2135 O OE2 . GLU A 1 265 ? 9.264  35.902  -18.206 1.00 63.92  ? 264 GLU A OE2 1 
ATOM   2136 N N   . GLY A 1 266 ? 6.325  39.700  -15.435 1.00 44.99  ? 265 GLY A N   1 
ATOM   2137 C CA  . GLY A 1 266 ? 4.904  39.893  -15.209 1.00 39.39  ? 265 GLY A CA  1 
ATOM   2138 C C   . GLY A 1 266 ? 4.469  41.303  -14.868 1.00 46.30  ? 265 GLY A C   1 
ATOM   2139 O O   . GLY A 1 266 ? 3.287  41.533  -14.582 1.00 37.91  ? 265 GLY A O   1 
ATOM   2140 N N   . LEU A 1 267 ? 5.393  42.264  -14.893 1.00 46.65  ? 266 LEU A N   1 
ATOM   2141 C CA  . LEU A 1 267 ? 5.078  43.638  -14.533 1.00 50.88  ? 266 LEU A CA  1 
ATOM   2142 C C   . LEU A 1 267 ? 5.033  44.502  -15.786 1.00 54.17  ? 266 LEU A C   1 
ATOM   2143 O O   . LEU A 1 267 ? 6.054  44.626  -16.481 1.00 51.08  ? 266 LEU A O   1 
ATOM   2144 C CB  . LEU A 1 267 ? 6.102  44.189  -13.538 1.00 40.29  ? 266 LEU A CB  1 
ATOM   2145 C CG  . LEU A 1 267 ? 6.096  43.525  -12.156 1.00 45.03  ? 266 LEU A CG  1 
ATOM   2146 C CD1 . LEU A 1 267 ? 7.116  44.189  -11.223 1.00 40.07  ? 266 LEU A CD1 1 
ATOM   2147 C CD2 . LEU A 1 267 ? 4.685  43.514  -11.534 1.00 42.82  ? 266 LEU A CD2 1 
ATOM   2148 N N   . PRO A 1 268 ? 3.871  45.111  -16.112 1.00 54.41  ? 267 PRO A N   1 
ATOM   2149 C CA  . PRO A 1 268 ? 3.814  46.066  -17.233 1.00 61.11  ? 267 PRO A CA  1 
ATOM   2150 C C   . PRO A 1 268 ? 4.937  47.087  -17.163 1.00 59.93  ? 267 PRO A C   1 
ATOM   2151 O O   . PRO A 1 268 ? 5.732  47.227  -18.100 1.00 54.70  ? 267 PRO A O   1 
ATOM   2152 C CB  . PRO A 1 268 ? 2.445  46.736  -17.057 1.00 57.02  ? 267 PRO A CB  1 
ATOM   2153 C CG  . PRO A 1 268 ? 1.624  45.745  -16.281 1.00 52.68  ? 267 PRO A CG  1 
ATOM   2154 C CD  . PRO A 1 268 ? 2.567  44.927  -15.449 1.00 46.26  ? 267 PRO A CD  1 
ATOM   2155 N N   . LYS A 1 269 ? 5.013  47.796  -16.035 1.00 57.34  ? 268 LYS A N   1 
ATOM   2156 C CA  . LYS A 1 269 ? 6.081  48.747  -15.777 1.00 58.20  ? 268 LYS A CA  1 
ATOM   2157 C C   . LYS A 1 269 ? 6.788  48.380  -14.477 1.00 56.63  ? 268 LYS A C   1 
ATOM   2158 O O   . LYS A 1 269 ? 6.183  47.763  -13.591 1.00 51.34  ? 268 LYS A O   1 
ATOM   2159 C CB  . LYS A 1 269 ? 5.548  50.187  -15.688 1.00 59.48  ? 268 LYS A CB  1 
ATOM   2160 C CG  . LYS A 1 269 ? 5.253  50.853  -17.046 1.00 61.00  ? 268 LYS A CG  1 
ATOM   2161 C CD  . LYS A 1 269 ? 3.993  50.286  -17.704 1.00 67.78  ? 268 LYS A CD  1 
ATOM   2162 C CE  . LYS A 1 269 ? 3.139  51.355  -18.379 1.00 68.04  ? 268 LYS A CE  1 
ATOM   2163 N NZ  . LYS A 1 269 ? 1.704  50.925  -18.466 1.00 69.19  ? 268 LYS A NZ  1 
ATOM   2164 N N   . PRO A 1 270 ? 8.071  48.713  -14.348 1.00 52.88  ? 269 PRO A N   1 
ATOM   2165 C CA  . PRO A 1 270 ? 8.778  48.432  -13.095 1.00 51.75  ? 269 PRO A CA  1 
ATOM   2166 C C   . PRO A 1 270 ? 8.094  49.096  -11.904 1.00 52.66  ? 269 PRO A C   1 
ATOM   2167 O O   . PRO A 1 270 ? 7.547  50.196  -12.007 1.00 53.66  ? 269 PRO A O   1 
ATOM   2168 C CB  . PRO A 1 270 ? 10.177 49.007  -13.340 1.00 48.08  ? 269 PRO A CB  1 
ATOM   2169 C CG  . PRO A 1 270 ? 10.346 48.973  -14.810 1.00 52.89  ? 269 PRO A CG  1 
ATOM   2170 C CD  . PRO A 1 270 ? 8.977  49.229  -15.389 1.00 55.80  ? 269 PRO A CD  1 
ATOM   2171 N N   . LEU A 1 271 ? 8.100  48.392  -10.774 1.00 49.79  ? 270 LEU A N   1 
ATOM   2172 C CA  . LEU A 1 271 ? 7.559  48.913  -9.527  1.00 43.79  ? 270 LEU A CA  1 
ATOM   2173 C C   . LEU A 1 271 ? 8.626  49.675  -8.757  1.00 41.62  ? 270 LEU A C   1 
ATOM   2174 O O   . LEU A 1 271 ? 9.781  49.251  -8.680  1.00 42.86  ? 270 LEU A O   1 
ATOM   2175 C CB  . LEU A 1 271 ? 7.034  47.782  -8.649  1.00 44.33  ? 270 LEU A CB  1 
ATOM   2176 C CG  . LEU A 1 271 ? 5.744  47.099  -9.060  1.00 47.32  ? 270 LEU A CG  1 
ATOM   2177 C CD1 . LEU A 1 271 ? 5.472  45.947  -8.105  1.00 43.33  ? 270 LEU A CD1 1 
ATOM   2178 C CD2 . LEU A 1 271 ? 4.609  48.093  -9.051  1.00 49.47  ? 270 LEU A CD2 1 
ATOM   2179 N N   . THR A 1 272 ? 8.223  50.790  -8.162  1.00 47.12  ? 271 THR A N   1 
ATOM   2180 C CA  . THR A 1 272 ? 9.063  51.534  -7.238  1.00 42.21  ? 271 THR A CA  1 
ATOM   2181 C C   . THR A 1 272 ? 8.407  51.520  -5.868  1.00 41.36  ? 271 THR A C   1 
ATOM   2182 O O   . THR A 1 272 ? 7.200  51.751  -5.750  1.00 39.89  ? 271 THR A O   1 
ATOM   2183 C CB  . THR A 1 272 ? 9.278  52.958  -7.733  1.00 46.15  ? 271 THR A CB  1 
ATOM   2184 O OG1 . THR A 1 272 ? 10.009 52.899  -8.963  1.00 51.83  ? 271 THR A OG1 1 
ATOM   2185 C CG2 . THR A 1 272 ? 10.069 53.786  -6.704  1.00 42.66  ? 271 THR A CG2 1 
ATOM   2186 N N   . LEU A 1 273 ? 9.196  51.219  -4.844  1.00 40.48  ? 272 LEU A N   1 
ATOM   2187 C CA  . LEU A 1 273 ? 8.705  51.089  -3.484  1.00 40.44  ? 272 LEU A CA  1 
ATOM   2188 C C   . LEU A 1 273 ? 9.544  51.972  -2.578  1.00 38.95  ? 272 LEU A C   1 
ATOM   2189 O O   . LEU A 1 273 ? 10.754 52.114  -2.775  1.00 36.94  ? 272 LEU A O   1 
ATOM   2190 C CB  . LEU A 1 273 ? 8.751  49.625  -2.987  1.00 36.46  ? 272 LEU A CB  1 
ATOM   2191 C CG  . LEU A 1 273 ? 7.797  48.618  -3.631  1.00 40.68  ? 272 LEU A CG  1 
ATOM   2192 C CD1 . LEU A 1 273 ? 8.484  47.875  -4.752  1.00 43.01  ? 272 LEU A CD1 1 
ATOM   2193 C CD2 . LEU A 1 273 ? 7.277  47.634  -2.600  1.00 43.69  ? 272 LEU A CD2 1 
ATOM   2194 N N   . ARG A 1 274 ? 8.893  52.562  -1.587  1.00 38.65  ? 273 ARG A N   1 
ATOM   2195 C CA  . ARG A 1 274 ? 9.547  53.468  -0.659  1.00 37.28  ? 273 ARG A CA  1 
ATOM   2196 C C   . ARG A 1 274 ? 8.952  53.223  0.714   1.00 38.62  ? 273 ARG A C   1 
ATOM   2197 O O   . ARG A 1 274 ? 7.758  52.941  0.837   1.00 36.41  ? 273 ARG A O   1 
ATOM   2198 C CB  . ARG A 1 274 ? 9.363  54.940  -1.081  1.00 39.33  ? 273 ARG A CB  1 
ATOM   2199 C CG  . ARG A 1 274 ? 10.153 55.941  -0.243  1.00 44.26  ? 273 ARG A CG  1 
ATOM   2200 C CD  . ARG A 1 274 ? 9.733  57.373  -0.547  1.00 46.71  ? 273 ARG A CD  1 
ATOM   2201 N NE  . ARG A 1 274 ? 9.431  57.542  -1.967  1.00 50.13  ? 273 ARG A NE  1 
ATOM   2202 C CZ  . ARG A 1 274 ? 10.283 58.053  -2.852  1.00 51.76  ? 273 ARG A CZ  1 
ATOM   2203 N NH1 . ARG A 1 274 ? 11.489 58.448  -2.456  1.00 46.83  ? 273 ARG A NH1 1 
ATOM   2204 N NH2 . ARG A 1 274 ? 9.935  58.165  -4.131  1.00 50.81  ? 273 ARG A NH2 1 
ATOM   2205 N N   . TRP A 1 275 ? 9.789  53.298  1.738   1.00 37.93  ? 274 TRP A N   1 
ATOM   2206 C CA  . TRP A 1 275 ? 9.303  53.207  3.105   1.00 31.97  ? 274 TRP A CA  1 
ATOM   2207 C C   . TRP A 1 275 ? 8.687  54.547  3.486   1.00 38.55  ? 274 TRP A C   1 
ATOM   2208 O O   . TRP A 1 275 ? 9.401  55.546  3.639   1.00 38.96  ? 274 TRP A O   1 
ATOM   2209 C CB  . TRP A 1 275 ? 10.432 52.844  4.056   1.00 34.63  ? 274 TRP A CB  1 
ATOM   2210 C CG  . TRP A 1 275 ? 9.953  52.751  5.444   1.00 38.00  ? 274 TRP A CG  1 
ATOM   2211 C CD1 . TRP A 1 275 ? 10.084 53.689  6.419   1.00 35.08  ? 274 TRP A CD1 1 
ATOM   2212 C CD2 . TRP A 1 275 ? 9.230  51.660  6.022   1.00 35.88  ? 274 TRP A CD2 1 
ATOM   2213 N NE1 . TRP A 1 275 ? 9.500  53.243  7.580   1.00 36.12  ? 274 TRP A NE1 1 
ATOM   2214 C CE2 . TRP A 1 275 ? 8.969  51.999  7.364   1.00 34.26  ? 274 TRP A CE2 1 
ATOM   2215 C CE3 . TRP A 1 275 ? 8.790  50.425  5.538   1.00 33.66  ? 274 TRP A CE3 1 
ATOM   2216 C CZ2 . TRP A 1 275 ? 8.271  51.154  8.231   1.00 31.65  ? 274 TRP A CZ2 1 
ATOM   2217 C CZ3 . TRP A 1 275 ? 8.107  49.574  6.408   1.00 36.47  ? 274 TRP A CZ3 1 
ATOM   2218 C CH2 . TRP A 1 275 ? 7.850  49.953  7.739   1.00 33.66  ? 274 TRP A CH2 1 
ATOM   2219 N N   . GLU A 1 276 ? 7.366  54.574  3.626   1.00 33.13  ? 275 GLU A N   1 
ATOM   2220 C CA  . GLU A 1 276 ? 6.667  55.793  4.008   1.00 39.10  ? 275 GLU A CA  1 
ATOM   2221 C C   . GLU A 1 276 ? 5.360  55.477  4.756   1.00 42.02  ? 275 GLU A C   1 
ATOM   2222 O O   . GLU A 1 276 ? 4.951  54.309  4.864   1.00 33.18  ? 275 GLU A O   1 
ATOM   2223 C CB  . GLU A 1 276 ? 6.388  56.665  2.770   1.00 37.80  ? 275 GLU A CB  1 
ATOM   2224 C CG  . GLU A 1 276 ? 5.505  56.014  1.728   1.00 41.54  ? 275 GLU A CG  1 
ATOM   2225 C CD  . GLU A 1 276 ? 5.541  56.738  0.378   1.00 44.74  ? 275 GLU A CD  1 
ATOM   2226 O OE1 . GLU A 1 276 ? 4.947  56.214  -0.591  1.00 42.71  ? 275 GLU A OE1 1 
ATOM   2227 O OE2 . GLU A 1 276 ? 6.159  57.826  0.288   1.00 43.70  ? 275 GLU A OE2 1 
ATOM   2228 O OXT . GLU A 1 276 ? 4.703  56.393  5.287   1.00 35.71  ? 275 GLU A OXT 1 
ATOM   2229 N N   . MET B 2 1   ? 40.073 19.735  -4.852  1.00 57.33  ? 0   MET B N   1 
ATOM   2230 C CA  . MET B 2 1   ? 38.628 19.764  -5.062  1.00 62.76  ? 0   MET B CA  1 
ATOM   2231 C C   . MET B 2 1   ? 38.000 21.016  -4.476  1.00 59.99  ? 0   MET B C   1 
ATOM   2232 O O   . MET B 2 1   ? 38.427 21.499  -3.421  1.00 54.96  ? 0   MET B O   1 
ATOM   2233 C CB  . MET B 2 1   ? 37.967 18.531  -4.445  1.00 59.21  ? 0   MET B CB  1 
ATOM   2234 C CG  . MET B 2 1   ? 36.968 17.870  -5.366  1.00 57.61  ? 0   MET B CG  1 
ATOM   2235 S SD  . MET B 2 1   ? 36.017 16.592  -4.549  1.00 62.63  ? 0   MET B SD  1 
ATOM   2236 C CE  . MET B 2 1   ? 37.015 15.154  -4.915  1.00 43.83  ? 0   MET B CE  1 
ATOM   2237 N N   . ILE B 2 2   ? 36.973 21.535  -5.143  1.00 60.42  ? 1   ILE B N   1 
ATOM   2238 C CA  . ILE B 2 2   ? 36.261 22.694  -4.620  1.00 55.56  ? 1   ILE B CA  1 
ATOM   2239 C C   . ILE B 2 2   ? 35.186 22.219  -3.652  1.00 56.45  ? 1   ILE B C   1 
ATOM   2240 O O   . ILE B 2 2   ? 34.456 21.256  -3.929  1.00 53.88  ? 1   ILE B O   1 
ATOM   2241 C CB  . ILE B 2 2   ? 35.670 23.540  -5.758  1.00 56.02  ? 1   ILE B CB  1 
ATOM   2242 C CG1 . ILE B 2 2   ? 34.605 22.761  -6.530  1.00 47.56  ? 1   ILE B CG1 1 
ATOM   2243 C CG2 . ILE B 2 2   ? 36.775 24.027  -6.684  1.00 57.94  ? 1   ILE B CG2 1 
ATOM   2244 C CD1 . ILE B 2 2   ? 33.416 23.602  -6.887  1.00 50.87  ? 1   ILE B CD1 1 
ATOM   2245 N N   . GLN B 2 3   ? 35.112 22.868  -2.494  1.00 48.05  ? 2   GLN B N   1 
ATOM   2246 C CA  . GLN B 2 3   ? 34.089 22.588  -1.500  1.00 44.13  ? 2   GLN B CA  1 
ATOM   2247 C C   . GLN B 2 3   ? 33.353 23.876  -1.185  1.00 45.85  ? 2   GLN B C   1 
ATOM   2248 O O   . GLN B 2 3   ? 33.982 24.906  -0.912  1.00 48.11  ? 2   GLN B O   1 
ATOM   2249 C CB  . GLN B 2 3   ? 34.682 21.991  -0.220  1.00 41.39  ? 2   GLN B CB  1 
ATOM   2250 C CG  . GLN B 2 3   ? 35.226 20.586  -0.432  1.00 44.04  ? 2   GLN B CG  1 
ATOM   2251 C CD  . GLN B 2 3   ? 35.151 19.716  0.804   1.00 42.41  ? 2   GLN B CD  1 
ATOM   2252 O OE1 . GLN B 2 3   ? 34.979 18.498  0.702   1.00 41.97  ? 2   GLN B OE1 1 
ATOM   2253 N NE2 . GLN B 2 3   ? 35.278 20.332  1.981   1.00 39.07  ? 2   GLN B NE2 1 
ATOM   2254 N N   . ARG B 2 4   ? 32.035 23.807  -1.247  1.00 36.20  ? 3   ARG B N   1 
ATOM   2255 C CA  . ARG B 2 4   ? 31.208 24.984  -0.966  1.00 32.17  ? 3   ARG B CA  1 
ATOM   2256 C C   . ARG B 2 4   ? 30.241 24.692  0.179   1.00 33.07  ? 3   ARG B C   1 
ATOM   2257 O O   . ARG B 2 4   ? 29.705 23.623  0.218   1.00 31.78  ? 3   ARG B O   1 
ATOM   2258 C CB  . ARG B 2 4   ? 30.506 25.385  -2.250  1.00 31.21  ? 3   ARG B CB  1 
ATOM   2259 C CG  . ARG B 2 4   ? 31.442 25.581  -3.421  1.00 34.92  ? 3   ARG B CG  1 
ATOM   2260 C CD  . ARG B 2 4   ? 30.472 26.016  -4.458  1.00 36.37  ? 3   ARG B CD  1 
ATOM   2261 N NE  . ARG B 2 4   ? 30.927 26.157  -5.801  1.00 45.78  ? 3   ARG B NE  1 
ATOM   2262 C CZ  . ARG B 2 4   ? 31.297 27.313  -6.317  1.00 46.96  ? 3   ARG B CZ  1 
ATOM   2263 N NH1 . ARG B 2 4   ? 31.693 27.359  -7.567  1.00 46.80  ? 3   ARG B NH1 1 
ATOM   2264 N NH2 . ARG B 2 4   ? 31.261 28.418  -5.592  1.00 36.64  ? 3   ARG B NH2 1 
ATOM   2265 N N   . THR B 2 5   ? 30.036 25.676  1.046   1.00 32.61  ? 4   THR B N   1 
ATOM   2266 C CA  . THR B 2 5   ? 29.161 25.576  2.205   1.00 31.49  ? 4   THR B CA  1 
ATOM   2267 C C   . THR B 2 5   ? 27.724 25.893  1.805   1.00 29.08  ? 4   THR B C   1 
ATOM   2268 O O   . THR B 2 5   ? 27.486 26.835  1.042   1.00 29.54  ? 4   THR B O   1 
ATOM   2269 C CB  . THR B 2 5   ? 29.603 26.550  3.306   1.00 38.42  ? 4   THR B CB  1 
ATOM   2270 O OG1 . THR B 2 5   ? 31.033 26.633  3.336   1.00 42.48  ? 4   THR B OG1 1 
ATOM   2271 C CG2 . THR B 2 5   ? 29.110 26.074  4.649   1.00 33.68  ? 4   THR B CG2 1 
ATOM   2272 N N   . PRO B 2 6   ? 26.754 25.129  2.298   1.00 26.70  ? 5   PRO B N   1 
ATOM   2273 C CA  . PRO B 2 6   ? 25.357 25.454  2.002   1.00 29.39  ? 5   PRO B CA  1 
ATOM   2274 C C   . PRO B 2 6   ? 25.006 26.838  2.522   1.00 31.29  ? 5   PRO B C   1 
ATOM   2275 O O   . PRO B 2 6   ? 25.464 27.259  3.583   1.00 33.42  ? 5   PRO B O   1 
ATOM   2276 C CB  . PRO B 2 6   ? 24.572 24.355  2.735   1.00 24.19  ? 5   PRO B CB  1 
ATOM   2277 C CG  . PRO B 2 6   ? 25.517 23.814  3.746   1.00 27.84  ? 5   PRO B CG  1 
ATOM   2278 C CD  . PRO B 2 6   ? 26.870 23.911  3.114   1.00 29.30  ? 5   PRO B CD  1 
ATOM   2279 N N   . LYS B 2 7   ? 24.230 27.564  1.734   1.00 31.25  ? 6   LYS B N   1 
ATOM   2280 C CA  . LYS B 2 7   ? 23.498 28.724  2.218   1.00 33.93  ? 6   LYS B CA  1 
ATOM   2281 C C   . LYS B 2 7   ? 22.111 28.245  2.614   1.00 29.28  ? 6   LYS B C   1 
ATOM   2282 O O   . LYS B 2 7   ? 21.552 27.354  1.970   1.00 32.63  ? 6   LYS B O   1 
ATOM   2283 C CB  . LYS B 2 7   ? 23.430 29.810  1.144   1.00 31.73  ? 6   LYS B CB  1 
ATOM   2284 C CG  . LYS B 2 7   ? 24.749 30.581  0.994   1.00 44.35  ? 6   LYS B CG  1 
ATOM   2285 C CD  . LYS B 2 7   ? 25.777 29.826  0.146   1.00 47.28  ? 6   LYS B CD  1 
ATOM   2286 C CE  . LYS B 2 7   ? 27.010 30.682  -0.128  1.00 55.56  ? 6   LYS B CE  1 
ATOM   2287 N NZ  . LYS B 2 7   ? 26.702 31.990  -0.823  1.00 47.55  ? 6   LYS B NZ  1 
ATOM   2288 N N   . ILE B 2 8   ? 21.583 28.776  3.712   1.00 29.16  ? 7   ILE B N   1 
ATOM   2289 C CA  . ILE B 2 8   ? 20.395 28.210  4.339   1.00 29.06  ? 7   ILE B CA  1 
ATOM   2290 C C   . ILE B 2 8   ? 19.355 29.301  4.527   1.00 33.65  ? 7   ILE B C   1 
ATOM   2291 O O   . ILE B 2 8   ? 19.671 30.395  5.009   1.00 33.50  ? 7   ILE B O   1 
ATOM   2292 C CB  . ILE B 2 8   ? 20.726 27.541  5.686   1.00 32.93  ? 7   ILE B CB  1 
ATOM   2293 C CG1 . ILE B 2 8   ? 21.843 26.507  5.521   1.00 27.23  ? 7   ILE B CG1 1 
ATOM   2294 C CG2 . ILE B 2 8   ? 19.490 26.876  6.263   1.00 28.66  ? 7   ILE B CG2 1 
ATOM   2295 C CD1 . ILE B 2 8   ? 22.503 26.111  6.859   1.00 29.23  ? 7   ILE B CD1 1 
ATOM   2296 N N   . GLN B 2 9   ? 18.117 29.001  4.153   1.00 28.80  ? 8   GLN B N   1 
ATOM   2297 C CA  . GLN B 2 9   ? 17.014 29.926  4.347   1.00 32.31  ? 8   GLN B CA  1 
ATOM   2298 C C   . GLN B 2 9   ? 15.846 29.123  4.881   1.00 29.14  ? 8   GLN B C   1 
ATOM   2299 O O   . GLN B 2 9   ? 15.533 28.061  4.340   1.00 27.75  ? 8   GLN B O   1 
ATOM   2300 C CB  . GLN B 2 9   ? 16.625 30.634  3.043   1.00 31.23  ? 8   GLN B CB  1 
ATOM   2301 C CG  . GLN B 2 9   ? 17.694 31.530  2.459   1.00 28.79  ? 8   GLN B CG  1 
ATOM   2302 C CD  . GLN B 2 9   ? 17.180 32.316  1.250   1.00 38.22  ? 8   GLN B CD  1 
ATOM   2303 O OE1 . GLN B 2 9   ? 16.390 33.259  1.390   1.00 35.80  ? 8   GLN B OE1 1 
ATOM   2304 N NE2 . GLN B 2 9   ? 17.618 31.921  0.060   1.00 34.57  ? 8   GLN B NE2 1 
ATOM   2305 N N   . VAL B 2 10  ? 15.240 29.603  5.962   1.00 30.14  ? 9   VAL B N   1 
ATOM   2306 C CA  . VAL B 2 10  ? 14.056 28.991  6.549   1.00 30.17  ? 9   VAL B CA  1 
ATOM   2307 C C   . VAL B 2 10  ? 12.929 30.005  6.470   1.00 34.54  ? 9   VAL B C   1 
ATOM   2308 O O   . VAL B 2 10  ? 13.114 31.178  6.815   1.00 33.12  ? 9   VAL B O   1 
ATOM   2309 C CB  . VAL B 2 10  ? 14.289 28.561  8.008   1.00 32.59  ? 9   VAL B CB  1 
ATOM   2310 C CG1 . VAL B 2 10  ? 13.183 27.597  8.478   1.00 27.42  ? 9   VAL B CG1 1 
ATOM   2311 C CG2 . VAL B 2 10  ? 15.644 27.929  8.125   1.00 36.12  ? 9   VAL B CG2 1 
ATOM   2312 N N   . TYR B 2 11  ? 11.766 29.558  6.022   1.00 34.00  ? 10  TYR B N   1 
ATOM   2313 C CA  . TYR B 2 11  ? 10.694 30.492  5.721   1.00 32.62  ? 10  TYR B CA  1 
ATOM   2314 C C   . TYR B 2 11  ? 9.436  29.672  5.511   1.00 33.62  ? 10  TYR B C   1 
ATOM   2315 O O   . TYR B 2 11  ? 9.489  28.444  5.396   1.00 34.34  ? 10  TYR B O   1 
ATOM   2316 C CB  . TYR B 2 11  ? 11.033 31.355  4.496   1.00 29.87  ? 10  TYR B CB  1 
ATOM   2317 C CG  . TYR B 2 11  ? 11.427 30.571  3.261   1.00 33.80  ? 10  TYR B CG  1 
ATOM   2318 C CD1 . TYR B 2 11  ? 12.719 30.068  3.108   1.00 33.31  ? 10  TYR B CD1 1 
ATOM   2319 C CD2 . TYR B 2 11  ? 10.508 30.332  2.245   1.00 31.12  ? 10  TYR B CD2 1 
ATOM   2320 C CE1 . TYR B 2 11  ? 13.078 29.353  1.981   1.00 33.64  ? 10  TYR B CE1 1 
ATOM   2321 C CE2 . TYR B 2 11  ? 10.862 29.620  1.111   1.00 31.88  ? 10  TYR B CE2 1 
ATOM   2322 C CZ  . TYR B 2 11  ? 12.143 29.134  0.985   1.00 31.38  ? 10  TYR B CZ  1 
ATOM   2323 O OH  . TYR B 2 11  ? 12.489 28.421  -0.134  1.00 28.62  ? 10  TYR B OH  1 
ATOM   2324 N N   . SER B 2 12  ? 8.303  30.360  5.493   1.00 36.84  ? 11  SER B N   1 
ATOM   2325 C CA  . SER B 2 12  ? 7.024  29.741  5.187   1.00 36.44  ? 11  SER B CA  1 
ATOM   2326 C C   . SER B 2 12  ? 6.662  30.004  3.729   1.00 34.21  ? 11  SER B C   1 
ATOM   2327 O O   . SER B 2 12  ? 7.111  30.974  3.118   1.00 32.19  ? 11  SER B O   1 
ATOM   2328 C CB  . SER B 2 12  ? 5.916  30.267  6.107   1.00 34.64  ? 11  SER B CB  1 
ATOM   2329 O OG  . SER B 2 12  ? 5.765  31.666  5.959   1.00 34.16  ? 11  SER B OG  1 
ATOM   2330 N N   . ARG B 2 13  ? 5.830  29.118  3.183   1.00 31.06  ? 12  ARG B N   1 
ATOM   2331 C CA  . ARG B 2 13  ? 5.407  29.251  1.794   1.00 36.72  ? 12  ARG B CA  1 
ATOM   2332 C C   . ARG B 2 13  ? 4.556  30.502  1.591   1.00 39.34  ? 12  ARG B C   1 
ATOM   2333 O O   . ARG B 2 13  ? 4.788  31.274  0.654   1.00 38.99  ? 12  ARG B O   1 
ATOM   2334 C CB  . ARG B 2 13  ? 4.642  28.001  1.361   1.00 32.13  ? 12  ARG B CB  1 
ATOM   2335 C CG  . ARG B 2 13  ? 3.904  28.167  0.036   1.00 38.74  ? 12  ARG B CG  1 
ATOM   2336 C CD  . ARG B 2 13  ? 3.187  26.895  -0.349  1.00 38.20  ? 12  ARG B CD  1 
ATOM   2337 N NE  . ARG B 2 13  ? 4.090  25.749  -0.407  1.00 40.22  ? 12  ARG B NE  1 
ATOM   2338 C CZ  . ARG B 2 13  ? 3.684  24.507  -0.651  1.00 41.31  ? 12  ARG B CZ  1 
ATOM   2339 N NH1 . ARG B 2 13  ? 2.397  24.275  -0.860  1.00 41.25  ? 12  ARG B NH1 1 
ATOM   2340 N NH2 . ARG B 2 13  ? 4.550  23.499  -0.679  1.00 38.14  ? 12  ARG B NH2 1 
ATOM   2341 N N   . HIS B 2 14  ? 3.558  30.705  2.451   1.00 40.07  ? 13  HIS B N   1 
ATOM   2342 C CA  . HIS B 2 14  ? 2.684  31.869  2.497   1.00 42.85  ? 13  HIS B CA  1 
ATOM   2343 C C   . HIS B 2 14  ? 3.014  32.721  3.716   1.00 42.37  ? 13  HIS B C   1 
ATOM   2344 O O   . HIS B 2 14  ? 3.578  32.219  4.695   1.00 41.29  ? 13  HIS B O   1 
ATOM   2345 C CB  . HIS B 2 14  ? 1.208  31.443  2.573   1.00 38.54  ? 13  HIS B CB  1 
ATOM   2346 C CG  . HIS B 2 14  ? 0.809  30.437  1.542   1.00 37.20  ? 13  HIS B CG  1 
ATOM   2347 N ND1 . HIS B 2 14  ? 0.663  30.754  0.210   1.00 39.90  ? 13  HIS B ND1 1 
ATOM   2348 C CD2 . HIS B 2 14  ? 0.527  29.117  1.647   1.00 39.76  ? 13  HIS B CD2 1 
ATOM   2349 C CE1 . HIS B 2 14  ? 0.299  29.675  -0.462  1.00 37.85  ? 13  HIS B CE1 1 
ATOM   2350 N NE2 . HIS B 2 14  ? 0.214  28.667  0.385   1.00 40.53  ? 13  HIS B NE2 1 
ATOM   2351 N N   . PRO B 2 15  ? 2.663  34.011  3.699   1.00 44.95  ? 14  PRO B N   1 
ATOM   2352 C CA  . PRO B 2 15  ? 2.844  34.852  4.896   1.00 42.22  ? 14  PRO B CA  1 
ATOM   2353 C C   . PRO B 2 15  ? 2.230  34.210  6.131   1.00 45.81  ? 14  PRO B C   1 
ATOM   2354 O O   . PRO B 2 15  ? 1.101  33.711  6.100   1.00 47.68  ? 14  PRO B O   1 
ATOM   2355 C CB  . PRO B 2 15  ? 2.126  36.154  4.527   1.00 47.59  ? 14  PRO B CB  1 
ATOM   2356 C CG  . PRO B 2 15  ? 2.135  36.186  3.021   1.00 46.87  ? 14  PRO B CG  1 
ATOM   2357 C CD  . PRO B 2 15  ? 2.089  34.758  2.564   1.00 41.16  ? 14  PRO B CD  1 
ATOM   2358 N N   . ALA B 2 16  ? 2.989  34.209  7.223   1.00 42.11  ? 15  ALA B N   1 
ATOM   2359 C CA  . ALA B 2 16  ? 2.585  33.471  8.410   1.00 44.71  ? 15  ALA B CA  1 
ATOM   2360 C C   . ALA B 2 16  ? 1.422  34.163  9.108   1.00 45.73  ? 15  ALA B C   1 
ATOM   2361 O O   . ALA B 2 16  ? 1.483  35.362  9.401   1.00 47.69  ? 15  ALA B O   1 
ATOM   2362 C CB  . ALA B 2 16  ? 3.765  33.329  9.369   1.00 46.48  ? 15  ALA B CB  1 
ATOM   2363 N N   . GLU B 2 17  ? 0.361  33.399  9.369   1.00 49.00  ? 16  GLU B N   1 
ATOM   2364 C CA  . GLU B 2 17  ? -0.798 33.855  10.132  1.00 53.82  ? 16  GLU B CA  1 
ATOM   2365 C C   . GLU B 2 17  ? -1.130 32.785  11.161  1.00 53.38  ? 16  GLU B C   1 
ATOM   2366 O O   . GLU B 2 17  ? -1.475 31.655  10.793  1.00 48.72  ? 16  GLU B O   1 
ATOM   2367 C CB  . GLU B 2 17  ? -2.010 34.124  9.229   1.00 51.90  ? 16  GLU B CB  1 
ATOM   2368 C CG  . GLU B 2 17  ? -1.957 35.459  8.471   1.00 60.66  ? 16  GLU B CG  1 
ATOM   2369 C CD  . GLU B 2 17  ? -3.274 36.240  8.532   1.00 64.75  ? 16  GLU B CD  1 
ATOM   2370 O OE1 . GLU B 2 17  ? -4.048 36.191  7.548   1.00 66.05  ? 16  GLU B OE1 1 
ATOM   2371 O OE2 . GLU B 2 17  ? -3.533 36.908  9.562   1.00 62.24  ? 16  GLU B OE2 1 
ATOM   2372 N N   . ASN B 2 18  ? -1.026 33.152  12.441  1.00 51.77  ? 17  ASN B N   1 
ATOM   2373 C CA  . ASN B 2 18  ? -1.247 32.224  13.545  1.00 53.00  ? 17  ASN B CA  1 
ATOM   2374 C C   . ASN B 2 18  ? -2.577 31.496  13.399  1.00 53.43  ? 17  ASN B C   1 
ATOM   2375 O O   . ASN B 2 18  ? -3.630 32.116  13.218  1.00 56.15  ? 17  ASN B O   1 
ATOM   2376 C CB  . ASN B 2 18  ? -1.202 32.983  14.873  1.00 50.58  ? 17  ASN B CB  1 
ATOM   2377 C CG  . ASN B 2 18  ? 0.210  33.123  15.416  1.00 53.01  ? 17  ASN B CG  1 
ATOM   2378 O OD1 . ASN B 2 18  ? 1.161  32.575  14.854  1.00 50.84  ? 17  ASN B OD1 1 
ATOM   2379 N ND2 . ASN B 2 18  ? 0.353  33.859  16.513  1.00 48.76  ? 17  ASN B ND2 1 
ATOM   2380 N N   . GLY B 2 19  ? -2.518 30.169  13.458  1.00 51.88  ? 18  GLY B N   1 
ATOM   2381 C CA  . GLY B 2 19  ? -3.698 29.344  13.348  1.00 47.38  ? 18  GLY B CA  1 
ATOM   2382 C C   . GLY B 2 19  ? -4.093 28.932  11.946  1.00 54.47  ? 18  GLY B C   1 
ATOM   2383 O O   . GLY B 2 19  ? -5.042 28.149  11.801  1.00 53.16  ? 18  GLY B O   1 
ATOM   2384 N N   . LYS B 2 20  ? -3.408 29.426  10.910  1.00 52.15  ? 19  LYS B N   1 
ATOM   2385 C CA  . LYS B 2 20  ? -3.726 29.094  9.525   1.00 50.37  ? 19  LYS B CA  1 
ATOM   2386 C C   . LYS B 2 20  ? -2.699 28.114  8.964   1.00 50.53  ? 19  LYS B C   1 
ATOM   2387 O O   . LYS B 2 20  ? -1.493 28.263  9.188   1.00 51.29  ? 19  LYS B O   1 
ATOM   2388 C CB  . LYS B 2 20  ? -3.773 30.351  8.651   1.00 48.72  ? 19  LYS B CB  1 
ATOM   2389 N N   . SER B 2 21  ? -3.183 27.126  8.215   1.00 52.08  ? 20  SER B N   1 
ATOM   2390 C CA  . SER B 2 21  ? -2.317 26.077  7.695   1.00 43.77  ? 20  SER B CA  1 
ATOM   2391 C C   . SER B 2 21  ? -1.356 26.609  6.642   1.00 45.38  ? 20  SER B C   1 
ATOM   2392 O O   . SER B 2 21  ? -1.726 27.407  5.778   1.00 41.72  ? 20  SER B O   1 
ATOM   2393 C CB  . SER B 2 21  ? -3.152 24.945  7.116   1.00 43.67  ? 20  SER B CB  1 
ATOM   2394 O OG  . SER B 2 21  ? -2.421 23.737  7.172   1.00 55.64  ? 20  SER B OG  1 
ATOM   2395 N N   . ASN B 2 22  ? -0.116 26.141  6.709   1.00 42.41  ? 21  ASN B N   1 
ATOM   2396 C CA  . ASN B 2 22  ? 0.968  26.722  5.937   1.00 43.60  ? 21  ASN B CA  1 
ATOM   2397 C C   . ASN B 2 22  ? 1.974  25.617  5.640   1.00 41.25  ? 21  ASN B C   1 
ATOM   2398 O O   . ASN B 2 22  ? 1.766  24.450  5.984   1.00 39.45  ? 21  ASN B O   1 
ATOM   2399 C CB  . ASN B 2 22  ? 1.589  27.903  6.707   1.00 41.12  ? 21  ASN B CB  1 
ATOM   2400 C CG  . ASN B 2 22  ? 2.172  28.980  5.794   1.00 40.61  ? 21  ASN B CG  1 
ATOM   2401 O OD1 . ASN B 2 22  ? 2.910  28.686  4.855   1.00 43.16  ? 21  ASN B OD1 1 
ATOM   2402 N ND2 . ASN B 2 22  ? 1.861  30.237  6.088   1.00 38.94  ? 21  ASN B ND2 1 
ATOM   2403 N N   . PHE B 2 23  ? 3.073  25.993  4.998   1.00 35.86  ? 22  PHE B N   1 
ATOM   2404 C CA  . PHE B 2 23  ? 4.169  25.075  4.738   1.00 37.98  ? 22  PHE B CA  1 
ATOM   2405 C C   . PHE B 2 23  ? 5.453  25.713  5.231   1.00 35.39  ? 22  PHE B C   1 
ATOM   2406 O O   . PHE B 2 23  ? 5.687  26.900  4.988   1.00 35.62  ? 22  PHE B O   1 
ATOM   2407 C CB  . PHE B 2 23  ? 4.292  24.748  3.240   1.00 37.94  ? 22  PHE B CB  1 
ATOM   2408 C CG  . PHE B 2 23  ? 3.379  23.657  2.777   1.00 40.62  ? 22  PHE B CG  1 
ATOM   2409 C CD1 . PHE B 2 23  ? 3.764  22.326  2.867   1.00 44.35  ? 22  PHE B CD1 1 
ATOM   2410 C CD2 . PHE B 2 23  ? 2.134  23.956  2.248   1.00 38.43  ? 22  PHE B CD2 1 
ATOM   2411 C CE1 . PHE B 2 23  ? 2.919  21.311  2.428   1.00 43.59  ? 22  PHE B CE1 1 
ATOM   2412 C CE2 . PHE B 2 23  ? 1.288  22.952  1.816   1.00 38.92  ? 22  PHE B CE2 1 
ATOM   2413 C CZ  . PHE B 2 23  ? 1.677  21.629  1.904   1.00 36.75  ? 22  PHE B CZ  1 
ATOM   2414 N N   . LEU B 2 24  ? 6.271  24.930  5.935   1.00 34.67  ? 23  LEU B N   1 
ATOM   2415 C CA  . LEU B 2 24  ? 7.579  25.375  6.402   1.00 33.60  ? 23  LEU B CA  1 
ATOM   2416 C C   . LEU B 2 24  ? 8.652  24.845  5.456   1.00 32.06  ? 23  LEU B C   1 
ATOM   2417 O O   . LEU B 2 24  ? 8.683  23.648  5.144   1.00 29.11  ? 23  LEU B O   1 
ATOM   2418 C CB  . LEU B 2 24  ? 7.849  24.908  7.838   1.00 34.24  ? 23  LEU B CB  1 
ATOM   2419 C CG  . LEU B 2 24  ? 9.185  25.330  8.492   1.00 33.54  ? 23  LEU B CG  1 
ATOM   2420 C CD1 . LEU B 2 24  ? 9.250  26.815  8.819   1.00 30.72  ? 23  LEU B CD1 1 
ATOM   2421 C CD2 . LEU B 2 24  ? 9.457  24.523  9.742   1.00 34.88  ? 23  LEU B CD2 1 
ATOM   2422 N N   . ASN B 2 25  ? 9.519  25.736  4.993   1.00 33.45  ? 24  ASN B N   1 
ATOM   2423 C CA  . ASN B 2 25  ? 10.547 25.385  4.021   1.00 31.51  ? 24  ASN B CA  1 
ATOM   2424 C C   . ASN B 2 25  ? 11.929 25.610  4.605   1.00 32.16  ? 24  ASN B C   1 
ATOM   2425 O O   . ASN B 2 25  ? 12.156 26.570  5.356   1.00 27.98  ? 24  ASN B O   1 
ATOM   2426 C CB  . ASN B 2 25  ? 10.436 26.212  2.737   1.00 27.10  ? 24  ASN B CB  1 
ATOM   2427 C CG  . ASN B 2 25  ? 9.132  26.013  2.033   1.00 35.41  ? 24  ASN B CG  1 
ATOM   2428 O OD1 . ASN B 2 25  ? 8.512  24.944  2.143   1.00 29.59  ? 24  ASN B OD1 1 
ATOM   2429 N ND2 . ASN B 2 25  ? 8.677  27.057  1.313   1.00 30.68  ? 24  ASN B ND2 1 
ATOM   2430 N N   . CYS B 2 26  ? 12.853 24.739  4.220   1.00 30.53  ? 25  CYS B N   1 
ATOM   2431 C CA  . CYS B 2 26  ? 14.276 24.980  4.407   1.00 28.31  ? 25  CYS B CA  1 
ATOM   2432 C C   . CYS B 2 26  ? 14.946 24.796  3.055   1.00 28.20  ? 25  CYS B C   1 
ATOM   2433 O O   . CYS B 2 26  ? 14.975 23.681  2.525   1.00 27.75  ? 25  CYS B O   1 
ATOM   2434 C CB  . CYS B 2 26  ? 14.877 24.030  5.436   1.00 27.79  ? 25  CYS B CB  1 
ATOM   2435 S SG  . CYS B 2 26  ? 16.590 24.427  5.718   1.00 31.69  ? 25  CYS B SG  1 
ATOM   2436 N N   . TYR B 2 27  ? 15.484 25.875  2.498   1.00 26.72  ? 26  TYR B N   1 
ATOM   2437 C CA  . TYR B 2 27  ? 16.131 25.833  1.191   1.00 26.10  ? 26  TYR B CA  1 
ATOM   2438 C C   . TYR B 2 27  ? 17.637 25.928  1.398   1.00 29.28  ? 26  TYR B C   1 
ATOM   2439 O O   . TYR B 2 27  ? 18.129 26.918  1.951   1.00 29.95  ? 26  TYR B O   1 
ATOM   2440 C CB  . TYR B 2 27  ? 15.619 26.961  0.296   1.00 26.07  ? 26  TYR B CB  1 
ATOM   2441 C CG  . TYR B 2 27  ? 16.124 26.974  -1.139  1.00 27.89  ? 26  TYR B CG  1 
ATOM   2442 C CD1 . TYR B 2 27  ? 15.787 25.957  -2.039  1.00 30.22  ? 26  TYR B CD1 1 
ATOM   2443 C CD2 . TYR B 2 27  ? 16.915 28.019  -1.598  1.00 26.57  ? 26  TYR B CD2 1 
ATOM   2444 C CE1 . TYR B 2 27  ? 16.235 25.987  -3.371  1.00 32.49  ? 26  TYR B CE1 1 
ATOM   2445 C CE2 . TYR B 2 27  ? 17.367 28.058  -2.907  1.00 31.73  ? 26  TYR B CE2 1 
ATOM   2446 C CZ  . TYR B 2 27  ? 17.022 27.036  -3.788  1.00 31.69  ? 26  TYR B CZ  1 
ATOM   2447 O OH  . TYR B 2 27  ? 17.475 27.067  -5.079  1.00 37.91  ? 26  TYR B OH  1 
ATOM   2448 N N   . VAL B 2 28  ? 18.359 24.893  0.972   1.00 24.84  ? 27  VAL B N   1 
ATOM   2449 C CA  . VAL B 2 28  ? 19.809 24.842  1.077   1.00 24.09  ? 27  VAL B CA  1 
ATOM   2450 C C   . VAL B 2 28  ? 20.383 24.855  -0.332  1.00 24.42  ? 27  VAL B C   1 
ATOM   2451 O O   . VAL B 2 28  ? 19.967 24.075  -1.197  1.00 27.79  ? 27  VAL B O   1 
ATOM   2452 C CB  . VAL B 2 28  ? 20.274 23.622  1.898   1.00 25.15  ? 27  VAL B CB  1 
ATOM   2453 C CG1 . VAL B 2 28  ? 19.612 23.641  3.257   1.00 29.40  ? 27  VAL B CG1 1 
ATOM   2454 C CG2 . VAL B 2 28  ? 19.878 22.309  1.219   1.00 25.92  ? 27  VAL B CG2 1 
ATOM   2455 N N   . SER B 2 29  ? 21.327 25.754  -0.569  1.00 26.28  ? 28  SER B N   1 
ATOM   2456 C CA  . SER B 2 29  ? 21.780 26.024  -1.920  1.00 27.94  ? 28  SER B CA  1 
ATOM   2457 C C   . SER B 2 29  ? 23.237 26.447  -1.863  1.00 30.32  ? 28  SER B C   1 
ATOM   2458 O O   . SER B 2 29  ? 23.773 26.767  -0.793  1.00 27.32  ? 28  SER B O   1 
ATOM   2459 C CB  . SER B 2 29  ? 20.930 27.113  -2.577  1.00 29.79  ? 28  SER B CB  1 
ATOM   2460 O OG  . SER B 2 29  ? 21.054 28.326  -1.861  1.00 29.67  ? 28  SER B OG  1 
ATOM   2461 N N   . GLY B 2 30  ? 23.869 26.459  -3.035  1.00 20.31  ? 29  GLY B N   1 
ATOM   2462 C CA  . GLY B 2 30  ? 25.274 26.810  -3.125  1.00 21.67  ? 29  GLY B CA  1 
ATOM   2463 C C   . GLY B 2 30  ? 26.260 25.803  -2.558  1.00 25.61  ? 29  GLY B C   1 
ATOM   2464 O O   . GLY B 2 30  ? 27.408 26.157  -2.324  1.00 29.25  ? 29  GLY B O   1 
ATOM   2465 N N   . PHE B 2 31  ? 25.879 24.551  -2.355  1.00 23.97  ? 30  PHE B N   1 
ATOM   2466 C CA  . PHE B 2 31  ? 26.800 23.625  -1.709  1.00 29.64  ? 30  PHE B CA  1 
ATOM   2467 C C   . PHE B 2 31  ? 27.364 22.596  -2.682  1.00 27.98  ? 30  PHE B C   1 
ATOM   2468 O O   . PHE B 2 31  ? 26.819 22.355  -3.768  1.00 29.44  ? 30  PHE B O   1 
ATOM   2469 C CB  . PHE B 2 31  ? 26.136 22.919  -0.521  1.00 26.14  ? 30  PHE B CB  1 
ATOM   2470 C CG  . PHE B 2 31  ? 24.958 22.066  -0.884  1.00 26.59  ? 30  PHE B CG  1 
ATOM   2471 C CD1 . PHE B 2 31  ? 23.705 22.628  -1.024  1.00 24.05  ? 30  PHE B CD1 1 
ATOM   2472 C CD2 . PHE B 2 31  ? 25.096 20.688  -1.020  1.00 25.04  ? 30  PHE B CD2 1 
ATOM   2473 C CE1 . PHE B 2 31  ? 22.609 21.846  -1.322  1.00 26.54  ? 30  PHE B CE1 1 
ATOM   2474 C CE2 . PHE B 2 31  ? 23.999 19.891  -1.318  1.00 24.95  ? 30  PHE B CE2 1 
ATOM   2475 C CZ  . PHE B 2 31  ? 22.757 20.468  -1.478  1.00 24.95  ? 30  PHE B CZ  1 
ATOM   2476 N N   . HIS B 2 32  ? 28.490 21.997  -2.268  1.00 25.61  ? 31  HIS B N   1 
ATOM   2477 C CA  . HIS B 2 32  ? 29.248 21.005  -3.027  1.00 28.91  ? 31  HIS B CA  1 
ATOM   2478 C C   . HIS B 2 32  ? 30.273 20.375  -2.097  1.00 28.57  ? 31  HIS B C   1 
ATOM   2479 O O   . HIS B 2 32  ? 31.028 21.106  -1.439  1.00 29.11  ? 31  HIS B O   1 
ATOM   2480 C CB  . HIS B 2 32  ? 29.957 21.633  -4.240  1.00 26.37  ? 31  HIS B CB  1 
ATOM   2481 C CG  . HIS B 2 32  ? 29.988 20.750  -5.452  1.00 26.69  ? 31  HIS B CG  1 
ATOM   2482 N ND1 . HIS B 2 32  ? 30.715 19.578  -5.502  1.00 27.20  ? 31  HIS B ND1 1 
ATOM   2483 C CD2 . HIS B 2 32  ? 29.388 20.871  -6.663  1.00 25.33  ? 31  HIS B CD2 1 
ATOM   2484 C CE1 . HIS B 2 32  ? 30.554 19.010  -6.684  1.00 28.51  ? 31  HIS B CE1 1 
ATOM   2485 N NE2 . HIS B 2 32  ? 29.756 19.777  -7.409  1.00 31.95  ? 31  HIS B NE2 1 
ATOM   2486 N N   . PRO B 2 33  ? 30.366 19.027  -2.032  1.00 32.29  ? 32  PRO B N   1 
ATOM   2487 C CA  . PRO B 2 33  ? 29.610 18.061  -2.842  1.00 27.91  ? 32  PRO B CA  1 
ATOM   2488 C C   . PRO B 2 33  ? 28.157 17.886  -2.388  1.00 28.59  ? 32  PRO B C   1 
ATOM   2489 O O   . PRO B 2 33  ? 27.691 18.670  -1.556  1.00 29.61  ? 32  PRO B O   1 
ATOM   2490 C CB  . PRO B 2 33  ? 30.408 16.760  -2.659  1.00 29.73  ? 32  PRO B CB  1 
ATOM   2491 C CG  . PRO B 2 33  ? 30.948 16.860  -1.279  1.00 25.38  ? 32  PRO B CG  1 
ATOM   2492 C CD  . PRO B 2 33  ? 31.267 18.345  -1.077  1.00 28.83  ? 32  PRO B CD  1 
ATOM   2493 N N   . SER B 2 34  ? 27.468 16.857  -2.902  1.00 26.50  ? 33  SER B N   1 
ATOM   2494 C CA  . SER B 2 34  ? 26.007 16.796  -2.849  1.00 25.88  ? 33  SER B CA  1 
ATOM   2495 C C   . SER B 2 34  ? 25.443 16.161  -1.583  1.00 29.60  ? 33  SER B C   1 
ATOM   2496 O O   . SER B 2 34  ? 24.295 16.455  -1.223  1.00 31.52  ? 33  SER B O   1 
ATOM   2497 C CB  . SER B 2 34  ? 25.465 16.024  -4.062  1.00 27.04  ? 33  SER B CB  1 
ATOM   2498 O OG  . SER B 2 34  ? 26.136 14.787  -4.207  1.00 28.89  ? 33  SER B OG  1 
ATOM   2499 N N   . ASP B 2 35  ? 26.188 15.284  -0.912  1.00 27.89  ? 34  ASP B N   1 
ATOM   2500 C CA  . ASP B 2 35  ? 25.715 14.713  0.342   1.00 30.45  ? 34  ASP B CA  1 
ATOM   2501 C C   . ASP B 2 35  ? 25.459 15.821  1.364   1.00 32.81  ? 34  ASP B C   1 
ATOM   2502 O O   . ASP B 2 35  ? 26.285 16.714  1.555   1.00 31.39  ? 34  ASP B O   1 
ATOM   2503 C CB  . ASP B 2 35  ? 26.739 13.716  0.889   1.00 34.11  ? 34  ASP B CB  1 
ATOM   2504 C CG  . ASP B 2 35  ? 26.788 12.429  0.082   1.00 40.55  ? 34  ASP B CG  1 
ATOM   2505 O OD1 . ASP B 2 35  ? 25.714 11.931  -0.320  1.00 45.79  ? 34  ASP B OD1 1 
ATOM   2506 O OD2 . ASP B 2 35  ? 27.899 11.915  -0.159  1.00 54.71  ? 34  ASP B OD2 1 
ATOM   2507 N N   . ILE B 2 36  ? 24.302 15.767  2.018   1.00 26.51  ? 35  ILE B N   1 
ATOM   2508 C CA  . ILE B 2 36  ? 23.897 16.818  2.939   1.00 31.41  ? 35  ILE B CA  1 
ATOM   2509 C C   . ILE B 2 36  ? 22.794 16.236  3.800   1.00 32.61  ? 35  ILE B C   1 
ATOM   2510 O O   . ILE B 2 36  ? 22.057 15.354  3.360   1.00 29.74  ? 35  ILE B O   1 
ATOM   2511 C CB  . ILE B 2 36  ? 23.433 18.077  2.162   1.00 32.86  ? 35  ILE B CB  1 
ATOM   2512 C CG1 . ILE B 2 36  ? 23.292 19.279  3.084   1.00 25.82  ? 35  ILE B CG1 1 
ATOM   2513 C CG2 . ILE B 2 36  ? 22.129 17.786  1.371   1.00 29.66  ? 35  ILE B CG2 1 
ATOM   2514 C CD1 . ILE B 2 36  ? 23.518 20.608  2.378   1.00 27.29  ? 35  ILE B CD1 1 
ATOM   2515 N N   . GLU B 2 37  ? 22.696 16.705  5.044   1.00 29.90  ? 36  GLU B N   1 
ATOM   2516 C CA  . GLU B 2 37  ? 21.656 16.223  5.947   1.00 34.33  ? 36  GLU B CA  1 
ATOM   2517 C C   . GLU B 2 37  ? 20.862 17.411  6.469   1.00 33.08  ? 36  GLU B C   1 
ATOM   2518 O O   . GLU B 2 37  ? 21.440 18.403  6.912   1.00 30.44  ? 36  GLU B O   1 
ATOM   2519 C CB  . GLU B 2 37  ? 22.255 15.410  7.098   1.00 40.84  ? 36  GLU B CB  1 
ATOM   2520 C CG  . GLU B 2 37  ? 21.226 14.665  7.946   1.00 47.15  ? 36  GLU B CG  1 
ATOM   2521 C CD  . GLU B 2 37  ? 21.800 14.239  9.302   1.00 59.57  ? 36  GLU B CD  1 
ATOM   2522 O OE1 . GLU B 2 37  ? 21.012 14.025  10.261  1.00 56.05  ? 36  GLU B OE1 1 
ATOM   2523 O OE2 . GLU B 2 37  ? 23.046 14.119  9.403   1.00 58.96  ? 36  GLU B OE2 1 
ATOM   2524 N N   . VAL B 2 38  ? 19.541 17.319  6.388   1.00 32.52  ? 37  VAL B N   1 
ATOM   2525 C CA  . VAL B 2 38  ? 18.667 18.439  6.697   1.00 30.43  ? 37  VAL B CA  1 
ATOM   2526 C C   . VAL B 2 38  ? 17.488 17.929  7.509   1.00 33.20  ? 37  VAL B C   1 
ATOM   2527 O O   . VAL B 2 38  ? 16.794 16.998  7.084   1.00 30.68  ? 37  VAL B O   1 
ATOM   2528 C CB  . VAL B 2 38  ? 18.154 19.149  5.430   1.00 31.46  ? 37  VAL B CB  1 
ATOM   2529 C CG1 . VAL B 2 38  ? 17.321 20.332  5.835   1.00 24.14  ? 37  VAL B CG1 1 
ATOM   2530 C CG2 . VAL B 2 38  ? 19.312 19.562  4.510   1.00 26.11  ? 37  VAL B CG2 1 
ATOM   2531 N N   . ASP B 2 39  ? 17.259 18.551  8.667   1.00 29.81  ? 38  ASP B N   1 
ATOM   2532 C CA  . ASP B 2 39  ? 16.081 18.334  9.490   1.00 29.79  ? 38  ASP B CA  1 
ATOM   2533 C C   . ASP B 2 39  ? 15.331 19.639  9.677   1.00 31.21  ? 38  ASP B C   1 
ATOM   2534 O O   . ASP B 2 39  ? 15.931 20.720  9.728   1.00 30.92  ? 38  ASP B O   1 
ATOM   2535 C CB  . ASP B 2 39  ? 16.442 17.795  10.881  1.00 33.85  ? 38  ASP B CB  1 
ATOM   2536 C CG  . ASP B 2 39  ? 17.017 16.426  10.820  1.00 40.55  ? 38  ASP B CG  1 
ATOM   2537 O OD1 . ASP B 2 39  ? 16.306 15.519  10.314  1.00 40.64  ? 38  ASP B OD1 1 
ATOM   2538 O OD2 . ASP B 2 39  ? 18.174 16.264  11.279  1.00 50.71  ? 38  ASP B OD2 1 
ATOM   2539 N N   . LEU B 2 40  ? 14.016 19.523  9.801   1.00 30.70  ? 39  LEU B N   1 
ATOM   2540 C CA  . LEU B 2 40  ? 13.186 20.616  10.277  1.00 31.54  ? 39  LEU B CA  1 
ATOM   2541 C C   . LEU B 2 40  ? 12.879 20.363  11.751  1.00 34.64  ? 39  LEU B C   1 
ATOM   2542 O O   . LEU B 2 40  ? 12.558 19.235  12.141  1.00 36.43  ? 39  LEU B O   1 
ATOM   2543 C CB  . LEU B 2 40  ? 11.907 20.733  9.445   1.00 33.59  ? 39  LEU B CB  1 
ATOM   2544 C CG  . LEU B 2 40  ? 12.155 21.163  7.990   1.00 34.12  ? 39  LEU B CG  1 
ATOM   2545 C CD1 . LEU B 2 40  ? 10.868 21.316  7.199   1.00 27.19  ? 39  LEU B CD1 1 
ATOM   2546 C CD2 . LEU B 2 40  ? 12.974 22.456  7.967   1.00 33.25  ? 39  LEU B CD2 1 
ATOM   2547 N N   . LEU B 2 41  ? 13.019 21.400  12.573  1.00 35.91  ? 40  LEU B N   1 
ATOM   2548 C CA  . LEU B 2 41  ? 12.852 21.274  14.014  1.00 36.24  ? 40  LEU B CA  1 
ATOM   2549 C C   . LEU B 2 41  ? 11.616 22.034  14.467  1.00 36.11  ? 40  LEU B C   1 
ATOM   2550 O O   . LEU B 2 41  ? 11.372 23.162  14.026  1.00 38.23  ? 40  LEU B O   1 
ATOM   2551 C CB  . LEU B 2 41  ? 14.086 21.786  14.772  1.00 34.38  ? 40  LEU B CB  1 
ATOM   2552 C CG  . LEU B 2 41  ? 15.434 21.157  14.402  1.00 35.06  ? 40  LEU B CG  1 
ATOM   2553 C CD1 . LEU B 2 41  ? 16.557 21.697  15.285  1.00 29.67  ? 40  LEU B CD1 1 
ATOM   2554 C CD2 . LEU B 2 41  ? 15.351 19.633  14.445  1.00 29.40  ? 40  LEU B CD2 1 
ATOM   2555 N N   . LYS B 2 42  ? 10.831 21.398  15.334  1.00 37.91  ? 41  LYS B N   1 
ATOM   2556 C CA  . LYS B 2 42  ? 9.749  22.050  16.061  1.00 36.43  ? 41  LYS B CA  1 
ATOM   2557 C C   . LYS B 2 42  ? 10.094 22.026  17.541  1.00 35.33  ? 41  LYS B C   1 
ATOM   2558 O O   . LYS B 2 42  ? 10.198 20.946  18.134  1.00 36.77  ? 41  LYS B O   1 
ATOM   2559 C CB  . LYS B 2 42  ? 8.401  21.368  15.826  1.00 37.72  ? 41  LYS B CB  1 
ATOM   2560 C CG  . LYS B 2 42  ? 7.278  22.056  16.603  1.00 37.98  ? 41  LYS B CG  1 
ATOM   2561 C CD  . LYS B 2 42  ? 5.939  21.372  16.432  1.00 40.39  ? 41  LYS B CD  1 
ATOM   2562 C CE  . LYS B 2 42  ? 4.854  22.123  17.190  1.00 41.19  ? 41  LYS B CE  1 
ATOM   2563 N NZ  . LYS B 2 42  ? 3.511  21.536  16.928  1.00 44.12  ? 41  LYS B NZ  1 
ATOM   2564 N N   . ASN B 2 43  ? 10.267 23.213  18.126  1.00 34.31  ? 42  ASN B N   1 
ATOM   2565 C CA  . ASN B 2 43  ? 10.687 23.371  19.524  1.00 37.99  ? 42  ASN B CA  1 
ATOM   2566 C C   . ASN B 2 43  ? 11.908 22.518  19.842  1.00 33.42  ? 42  ASN B C   1 
ATOM   2567 O O   . ASN B 2 43  ? 11.996 21.896  20.897  1.00 34.57  ? 42  ASN B O   1 
ATOM   2568 C CB  . ASN B 2 43  ? 9.541  23.061  20.482  1.00 34.12  ? 42  ASN B CB  1 
ATOM   2569 C CG  . ASN B 2 43  ? 8.357  23.970  20.255  1.00 41.70  ? 42  ASN B CG  1 
ATOM   2570 O OD1 . ASN B 2 43  ? 8.521  25.190  20.123  1.00 39.72  ? 42  ASN B OD1 1 
ATOM   2571 N ND2 . ASN B 2 43  ? 7.159  23.386  20.168  1.00 38.12  ? 42  ASN B ND2 1 
ATOM   2572 N N   . GLY B 2 44  ? 12.861 22.486  18.910  1.00 40.50  ? 43  GLY B N   1 
ATOM   2573 C CA  . GLY B 2 44  ? 14.085 21.732  19.084  1.00 31.51  ? 43  GLY B CA  1 
ATOM   2574 C C   . GLY B 2 44  ? 13.985 20.249  18.805  1.00 29.75  ? 43  GLY B C   1 
ATOM   2575 O O   . GLY B 2 44  ? 14.979 19.541  18.991  1.00 37.20  ? 43  GLY B O   1 
ATOM   2576 N N   . GLU B 2 45  ? 12.825 19.751  18.380  1.00 33.45  ? 44  GLU B N   1 
ATOM   2577 C CA  . GLU B 2 45  ? 12.612 18.333  18.114  1.00 32.86  ? 44  GLU B CA  1 
ATOM   2578 C C   . GLU B 2 45  ? 12.490 18.107  16.613  1.00 37.19  ? 44  GLU B C   1 
ATOM   2579 O O   . GLU B 2 45  ? 11.823 18.874  15.915  1.00 38.64  ? 44  GLU B O   1 
ATOM   2580 C CB  . GLU B 2 45  ? 11.346 17.823  18.814  1.00 37.68  ? 44  GLU B CB  1 
ATOM   2581 C CG  . GLU B 2 45  ? 11.428 17.796  20.357  1.00 33.58  ? 44  GLU B CG  1 
ATOM   2582 C CD  . GLU B 2 45  ? 12.692 17.107  20.853  1.00 36.53  ? 44  GLU B CD  1 
ATOM   2583 O OE1 . GLU B 2 45  ? 12.822 15.869  20.671  1.00 37.78  ? 44  GLU B OE1 1 
ATOM   2584 O OE2 . GLU B 2 45  ? 13.568 17.806  21.408  1.00 35.28  ? 44  GLU B OE2 1 
ATOM   2585 N N   . ARG B 2 46  ? 13.136 17.055  16.120  1.00 37.99  ? 45  ARG B N   1 
ATOM   2586 C CA  . ARG B 2 46  ? 13.103 16.757  14.700  1.00 39.70  ? 45  ARG B CA  1 
ATOM   2587 C C   . ARG B 2 46  ? 11.677 16.438  14.276  1.00 40.62  ? 45  ARG B C   1 
ATOM   2588 O O   . ARG B 2 46  ? 11.008 15.611  14.900  1.00 40.90  ? 45  ARG B O   1 
ATOM   2589 C CB  . ARG B 2 46  ? 14.044 15.587  14.400  1.00 42.50  ? 45  ARG B CB  1 
ATOM   2590 C CG  . ARG B 2 46  ? 13.944 15.003  13.001  1.00 45.23  ? 45  ARG B CG  1 
ATOM   2591 C CD  . ARG B 2 46  ? 14.979 13.891  12.791  1.00 51.89  ? 45  ARG B CD  1 
ATOM   2592 N NE  . ARG B 2 46  ? 14.520 12.615  13.341  1.00 58.29  ? 45  ARG B NE  1 
ATOM   2593 C CZ  . ARG B 2 46  ? 14.900 12.129  14.523  1.00 69.99  ? 45  ARG B CZ  1 
ATOM   2594 N NH1 . ARG B 2 46  ? 15.756 12.808  15.285  1.00 65.38  ? 45  ARG B NH1 1 
ATOM   2595 N NH2 . ARG B 2 46  ? 14.427 10.960  14.946  1.00 69.36  ? 45  ARG B NH2 1 
ATOM   2596 N N   . ILE B 2 47  ? 11.187 17.131  13.240  1.00 34.04  ? 46  ILE B N   1 
ATOM   2597 C CA  . ILE B 2 47  ? 9.892  16.785  12.660  1.00 37.85  ? 46  ILE B CA  1 
ATOM   2598 C C   . ILE B 2 47  ? 10.078 15.571  11.760  1.00 40.81  ? 46  ILE B C   1 
ATOM   2599 O O   . ILE B 2 47  ? 11.084 15.457  11.048  1.00 43.67  ? 46  ILE B O   1 
ATOM   2600 C CB  . ILE B 2 47  ? 9.294  17.979  11.897  1.00 38.80  ? 46  ILE B CB  1 
ATOM   2601 C CG1 . ILE B 2 47  ? 9.179  19.193  12.818  1.00 38.01  ? 46  ILE B CG1 1 
ATOM   2602 C CG2 . ILE B 2 47  ? 7.932  17.616  11.317  1.00 36.31  ? 46  ILE B CG2 1 
ATOM   2603 C CD1 . ILE B 2 47  ? 8.949  20.506  12.084  1.00 34.92  ? 46  ILE B CD1 1 
ATOM   2604 N N   . GLU B 2 48  ? 9.123  14.641  11.797  1.00 45.23  ? 47  GLU B N   1 
ATOM   2605 C CA  . GLU B 2 48  ? 9.365  13.323  11.208  1.00 52.83  ? 47  GLU B CA  1 
ATOM   2606 C C   . GLU B 2 48  ? 9.001  13.247  9.723   1.00 56.97  ? 47  GLU B C   1 
ATOM   2607 O O   . GLU B 2 48  ? 9.858  12.936  8.886   1.00 59.82  ? 47  GLU B O   1 
ATOM   2608 C CB  . GLU B 2 48  ? 8.622  12.247  12.008  1.00 55.12  ? 47  GLU B CB  1 
ATOM   2609 C CG  . GLU B 2 48  ? 9.392  10.928  12.053  1.00 64.64  ? 47  GLU B CG  1 
ATOM   2610 C CD  . GLU B 2 48  ? 9.285  10.214  13.384  1.00 75.17  ? 47  GLU B CD  1 
ATOM   2611 O OE1 . GLU B 2 48  ? 9.530  8.985   13.421  1.00 80.22  ? 47  GLU B OE1 1 
ATOM   2612 O OE2 . GLU B 2 48  ? 8.960  10.879  14.392  1.00 76.73  ? 47  GLU B OE2 1 
ATOM   2613 N N   . LYS B 2 49  ? 7.740  13.523  9.376   1.00 48.95  ? 48  LYS B N   1 
ATOM   2614 C CA  . LYS B 2 49  ? 7.288  13.405  7.983   1.00 55.47  ? 48  LYS B CA  1 
ATOM   2615 C C   . LYS B 2 49  ? 7.696  14.662  7.210   1.00 52.32  ? 48  LYS B C   1 
ATOM   2616 O O   . LYS B 2 49  ? 6.928  15.615  7.050   1.00 56.04  ? 48  LYS B O   1 
ATOM   2617 C CB  . LYS B 2 49  ? 5.779  13.174  7.924   1.00 47.16  ? 48  LYS B CB  1 
ATOM   2618 N N   . VAL B 2 50  ? 8.940  14.663  6.728   1.00 42.77  ? 49  VAL B N   1 
ATOM   2619 C CA  . VAL B 2 50  ? 9.502  15.790  5.989   1.00 41.07  ? 49  VAL B CA  1 
ATOM   2620 C C   . VAL B 2 50  ? 9.957  15.298  4.621   1.00 41.61  ? 49  VAL B C   1 
ATOM   2621 O O   . VAL B 2 50  ? 10.681 14.299  4.517   1.00 43.38  ? 49  VAL B O   1 
ATOM   2622 C CB  . VAL B 2 50  ? 10.673 16.459  6.736   1.00 39.31  ? 49  VAL B CB  1 
ATOM   2623 C CG1 . VAL B 2 50  ? 11.416 17.442  5.800   1.00 33.94  ? 49  VAL B CG1 1 
ATOM   2624 C CG2 . VAL B 2 50  ? 10.173 17.185  7.987   1.00 40.31  ? 49  VAL B CG2 1 
ATOM   2625 N N   . GLU B 2 51  ? 9.544  16.008  3.584   1.00 38.26  ? 50  GLU B N   1 
ATOM   2626 C CA  . GLU B 2 51  ? 9.841  15.674  2.202   1.00 40.37  ? 50  GLU B CA  1 
ATOM   2627 C C   . GLU B 2 51  ? 10.885 16.643  1.662   1.00 39.41  ? 50  GLU B C   1 
ATOM   2628 O O   . GLU B 2 51  ? 11.194 17.665  2.287   1.00 32.17  ? 50  GLU B O   1 
ATOM   2629 C CB  . GLU B 2 51  ? 8.554  15.712  1.367   1.00 37.82  ? 50  GLU B CB  1 
ATOM   2630 C CG  . GLU B 2 51  ? 7.429  14.843  1.940   1.00 41.23  ? 50  GLU B CG  1 
ATOM   2631 C CD  . GLU B 2 51  ? 6.339  14.524  0.923   1.00 54.06  ? 50  GLU B CD  1 
ATOM   2632 O OE1 . GLU B 2 51  ? 6.013  13.328  0.755   1.00 56.81  ? 50  GLU B OE1 1 
ATOM   2633 O OE2 . GLU B 2 51  ? 5.812  15.467  0.289   1.00 56.62  ? 50  GLU B OE2 1 
ATOM   2634 N N   . HIS B 2 52  ? 11.447 16.311  0.496   1.00 32.34  ? 51  HIS B N   1 
ATOM   2635 C CA  . HIS B 2 52  ? 12.424 17.197  -0.122  1.00 31.41  ? 51  HIS B CA  1 
ATOM   2636 C C   . HIS B 2 52  ? 12.367 17.047  -1.634  1.00 29.52  ? 51  HIS B C   1 
ATOM   2637 O O   . HIS B 2 52  ? 11.879 16.053  -2.162  1.00 30.03  ? 51  HIS B O   1 
ATOM   2638 C CB  . HIS B 2 52  ? 13.856 16.932  0.373   1.00 32.11  ? 51  HIS B CB  1 
ATOM   2639 C CG  . HIS B 2 52  ? 14.338 15.532  0.126   1.00 37.77  ? 51  HIS B CG  1 
ATOM   2640 N ND1 . HIS B 2 52  ? 14.825 15.112  -1.096  1.00 37.09  ? 51  HIS B ND1 1 
ATOM   2641 C CD2 . HIS B 2 52  ? 14.420 14.460  0.950   1.00 37.44  ? 51  HIS B CD2 1 
ATOM   2642 C CE1 . HIS B 2 52  ? 15.179 13.841  -1.017  1.00 35.26  ? 51  HIS B CE1 1 
ATOM   2643 N NE2 . HIS B 2 52  ? 14.950 13.423  0.216   1.00 43.06  ? 51  HIS B NE2 1 
ATOM   2644 N N   . SER B 2 53  ? 12.883 18.056  -2.322  1.00 30.99  ? 52  SER B N   1 
ATOM   2645 C CA  . SER B 2 53  ? 12.905 18.073  -3.773  1.00 28.79  ? 52  SER B CA  1 
ATOM   2646 C C   . SER B 2 53  ? 14.043 17.201  -4.307  1.00 27.17  ? 52  SER B C   1 
ATOM   2647 O O   . SER B 2 53  ? 14.967 16.835  -3.582  1.00 27.91  ? 52  SER B O   1 
ATOM   2648 C CB  . SER B 2 53  ? 13.068 19.503  -4.264  1.00 25.71  ? 52  SER B CB  1 
ATOM   2649 O OG  . SER B 2 53  ? 14.318 20.012  -3.836  1.00 27.47  ? 52  SER B OG  1 
ATOM   2650 N N   . ASP B 2 54  ? 13.970 16.869  -5.593  1.00 26.15  ? 53  ASP B N   1 
ATOM   2651 C CA  . ASP B 2 54  ? 15.032 16.098  -6.226  1.00 24.44  ? 53  ASP B CA  1 
ATOM   2652 C C   . ASP B 2 54  ? 16.243 16.987  -6.497  1.00 25.56  ? 53  ASP B C   1 
ATOM   2653 O O   . ASP B 2 54  ? 16.109 18.143  -6.913  1.00 29.23  ? 53  ASP B O   1 
ATOM   2654 C CB  . ASP B 2 54  ? 14.558 15.478  -7.546  1.00 27.16  ? 53  ASP B CB  1 
ATOM   2655 C CG  . ASP B 2 54  ? 13.182 14.842  -7.455  1.00 29.71  ? 53  ASP B CG  1 
ATOM   2656 O OD1 . ASP B 2 54  ? 13.000 13.882  -6.679  1.00 31.42  ? 53  ASP B OD1 1 
ATOM   2657 O OD2 . ASP B 2 54  ? 12.272 15.296  -8.182  1.00 32.90  ? 53  ASP B OD2 1 
ATOM   2658 N N   . LEU B 2 55  ? 17.430 16.416  -6.318  1.00 25.39  ? 54  LEU B N   1 
ATOM   2659 C CA  . LEU B 2 55  ? 18.683 17.150  -6.458  1.00 22.47  ? 54  LEU B CA  1 
ATOM   2660 C C   . LEU B 2 55  ? 18.831 17.815  -7.830  1.00 25.69  ? 54  LEU B C   1 
ATOM   2661 O O   . LEU B 2 55  ? 18.679 17.165  -8.869  1.00 23.61  ? 54  LEU B O   1 
ATOM   2662 C CB  . LEU B 2 55  ? 19.842 16.185  -6.218  1.00 23.31  ? 54  LEU B CB  1 
ATOM   2663 C CG  . LEU B 2 55  ? 21.225 16.817  -6.070  1.00 22.46  ? 54  LEU B CG  1 
ATOM   2664 C CD1 . LEU B 2 55  ? 21.266 17.634  -4.779  1.00 23.56  ? 54  LEU B CD1 1 
ATOM   2665 C CD2 . LEU B 2 55  ? 22.298 15.732  -6.092  1.00 21.64  ? 54  LEU B CD2 1 
ATOM   2666 N N   . SER B 2 56  ? 19.169 19.111  -7.834  1.00 20.85  ? 55  SER B N   1 
ATOM   2667 C CA  . SER B 2 56  ? 19.592 19.777  -9.061  1.00 26.76  ? 55  SER B CA  1 
ATOM   2668 C C   . SER B 2 56  ? 20.660 20.797  -8.695  1.00 25.34  ? 55  SER B C   1 
ATOM   2669 O O   . SER B 2 56  ? 21.083 20.882  -7.540  1.00 23.28  ? 55  SER B O   1 
ATOM   2670 C CB  . SER B 2 56  ? 18.414 20.429  -9.806  1.00 26.55  ? 55  SER B CB  1 
ATOM   2671 O OG  . SER B 2 56  ? 18.841 20.912  -11.077 1.00 28.83  ? 55  SER B OG  1 
ATOM   2672 N N   . PHE B 2 57  ? 21.125 21.556  -9.692  1.00 21.17  ? 56  PHE B N   1 
ATOM   2673 C CA  . PHE B 2 57  ? 22.215 22.495  -9.453  1.00 26.01  ? 56  PHE B CA  1 
ATOM   2674 C C   . PHE B 2 57  ? 22.026 23.750  -10.297 1.00 24.20  ? 56  PHE B C   1 
ATOM   2675 O O   . PHE B 2 57  ? 21.219 23.780  -11.226 1.00 30.59  ? 56  PHE B O   1 
ATOM   2676 C CB  . PHE B 2 57  ? 23.583 21.853  -9.720  1.00 21.63  ? 56  PHE B CB  1 
ATOM   2677 C CG  . PHE B 2 57  ? 23.666 21.087  -11.016 1.00 22.75  ? 56  PHE B CG  1 
ATOM   2678 C CD1 . PHE B 2 57  ? 23.998 21.736  -12.206 1.00 21.57  ? 56  PHE B CD1 1 
ATOM   2679 C CD2 . PHE B 2 57  ? 23.445 19.719  -11.039 1.00 19.76  ? 56  PHE B CD2 1 
ATOM   2680 C CE1 . PHE B 2 57  ? 24.093 21.033  -13.399 1.00 23.20  ? 56  PHE B CE1 1 
ATOM   2681 C CE2 . PHE B 2 57  ? 23.526 18.997  -12.247 1.00 22.39  ? 56  PHE B CE2 1 
ATOM   2682 C CZ  . PHE B 2 57  ? 23.861 19.651  -13.419 1.00 20.78  ? 56  PHE B CZ  1 
ATOM   2683 N N   . SER B 2 58  ? 22.791 24.790  -9.960  1.00 21.73  ? 57  SER B N   1 
ATOM   2684 C CA  . SER B 2 58  ? 22.743 26.079  -10.631 1.00 24.62  ? 57  SER B CA  1 
ATOM   2685 C C   . SER B 2 58  ? 23.854 26.193  -11.665 1.00 29.34  ? 57  SER B C   1 
ATOM   2686 O O   . SER B 2 58  ? 24.687 25.296  -11.832 1.00 26.69  ? 57  SER B O   1 
ATOM   2687 C CB  . SER B 2 58  ? 22.864 27.235  -9.630  1.00 28.25  ? 57  SER B CB  1 
ATOM   2688 O OG  . SER B 2 58  ? 22.129 26.995  -8.447  1.00 26.88  ? 57  SER B OG  1 
ATOM   2689 N N   . LYS B 2 59  ? 23.879 27.353  -12.332 1.00 31.64  ? 58  LYS B N   1 
ATOM   2690 C CA  . LYS B 2 59  ? 24.833 27.623  -13.408 1.00 33.21  ? 58  LYS B CA  1 
ATOM   2691 C C   . LYS B 2 59  ? 26.282 27.435  -12.967 1.00 32.43  ? 58  LYS B C   1 
ATOM   2692 O O   . LYS B 2 59  ? 27.126 27.017  -13.772 1.00 29.74  ? 58  LYS B O   1 
ATOM   2693 C CB  . LYS B 2 59  ? 24.602 29.046  -13.928 1.00 37.12  ? 58  LYS B CB  1 
ATOM   2694 C CG  . LYS B 2 59  ? 25.599 29.530  -14.962 1.00 45.90  ? 58  LYS B CG  1 
ATOM   2695 C CD  . LYS B 2 59  ? 25.695 31.068  -14.964 1.00 54.46  ? 58  LYS B CD  1 
ATOM   2696 C CE  . LYS B 2 59  ? 25.572 31.673  -16.370 1.00 57.22  ? 58  LYS B CE  1 
ATOM   2697 N NZ  . LYS B 2 59  ? 26.222 30.832  -17.427 1.00 56.00  ? 58  LYS B NZ  1 
ATOM   2698 N N   . ASP B 2 60  ? 26.596 27.715  -11.700 1.00 30.52  ? 59  ASP B N   1 
ATOM   2699 C CA  . ASP B 2 60  ? 27.955 27.526  -11.210 1.00 27.33  ? 59  ASP B CA  1 
ATOM   2700 C C   . ASP B 2 60  ? 28.217 26.109  -10.697 1.00 26.58  ? 59  ASP B C   1 
ATOM   2701 O O   . ASP B 2 60  ? 29.253 25.876  -10.065 1.00 28.33  ? 59  ASP B O   1 
ATOM   2702 C CB  . ASP B 2 60  ? 28.284 28.562  -10.125 1.00 30.55  ? 59  ASP B CB  1 
ATOM   2703 C CG  . ASP B 2 60  ? 27.573 28.301  -8.804  1.00 32.91  ? 59  ASP B CG  1 
ATOM   2704 O OD1 . ASP B 2 60  ? 26.664 27.438  -8.723  1.00 30.41  ? 59  ASP B OD1 1 
ATOM   2705 O OD2 . ASP B 2 60  ? 27.927 28.988  -7.827  1.00 36.74  ? 59  ASP B OD2 1 
ATOM   2706 N N   . TRP B 2 61  ? 27.295 25.176  -10.927 1.00 24.74  ? 60  TRP B N   1 
ATOM   2707 C CA  . TRP B 2 61  ? 27.384 23.741  -10.612 1.00 26.37  ? 60  TRP B CA  1 
ATOM   2708 C C   . TRP B 2 61  ? 27.090 23.423  -9.140  1.00 28.68  ? 60  TRP B C   1 
ATOM   2709 O O   . TRP B 2 61  ? 27.136 22.230  -8.765  1.00 24.83  ? 60  TRP B O   1 
ATOM   2710 C CB  . TRP B 2 61  ? 28.748 23.124  -10.987 1.00 21.55  ? 60  TRP B CB  1 
ATOM   2711 C CG  . TRP B 2 61  ? 29.149 23.344  -12.429 1.00 25.64  ? 60  TRP B CG  1 
ATOM   2712 C CD1 . TRP B 2 61  ? 30.102 24.211  -12.898 1.00 29.05  ? 60  TRP B CD1 1 
ATOM   2713 C CD2 . TRP B 2 61  ? 28.593 22.700  -13.589 1.00 25.33  ? 60  TRP B CD2 1 
ATOM   2714 N NE1 . TRP B 2 61  ? 30.178 24.145  -14.275 1.00 24.17  ? 60  TRP B NE1 1 
ATOM   2715 C CE2 . TRP B 2 61  ? 29.263 23.222  -14.722 1.00 27.98  ? 60  TRP B CE2 1 
ATOM   2716 C CE3 . TRP B 2 61  ? 27.612 21.718  -13.776 1.00 22.80  ? 60  TRP B CE3 1 
ATOM   2717 C CZ2 . TRP B 2 61  ? 28.986 22.790  -16.017 1.00 22.93  ? 60  TRP B CZ2 1 
ATOM   2718 C CZ3 . TRP B 2 61  ? 27.325 21.300  -15.068 1.00 25.33  ? 60  TRP B CZ3 1 
ATOM   2719 C CH2 . TRP B 2 61  ? 28.010 21.836  -16.169 1.00 27.49  ? 60  TRP B CH2 1 
ATOM   2720 N N   . SER B 2 62  ? 26.795 24.409  -8.291  1.00 25.73  ? 61  SER B N   1 
ATOM   2721 C CA  . SER B 2 62  ? 26.497 24.100  -6.899  1.00 26.14  ? 61  SER B CA  1 
ATOM   2722 C C   . SER B 2 62  ? 25.057 23.610  -6.769  1.00 23.27  ? 61  SER B C   1 
ATOM   2723 O O   . SER B 2 62  ? 24.161 24.041  -7.499  1.00 25.83  ? 61  SER B O   1 
ATOM   2724 C CB  . SER B 2 62  ? 26.756 25.326  -5.996  1.00 28.45  ? 61  SER B CB  1 
ATOM   2725 O OG  . SER B 2 62  ? 25.992 26.468  -6.388  1.00 30.60  ? 61  SER B OG  1 
ATOM   2726 N N   . PHE B 2 63  ? 24.838 22.698  -5.830  1.00 24.06  ? 62  PHE B N   1 
ATOM   2727 C CA  . PHE B 2 63  ? 23.551 22.033  -5.703  1.00 20.91  ? 62  PHE B CA  1 
ATOM   2728 C C   . PHE B 2 63  ? 22.553 22.865  -4.896  1.00 29.12  ? 62  PHE B C   1 
ATOM   2729 O O   . PHE B 2 63  ? 22.911 23.819  -4.189  1.00 26.55  ? 62  PHE B O   1 
ATOM   2730 C CB  . PHE B 2 63  ? 23.725 20.662  -5.045  1.00 23.45  ? 62  PHE B CB  1 
ATOM   2731 C CG  . PHE B 2 63  ? 24.617 19.728  -5.828  1.00 25.10  ? 62  PHE B CG  1 
ATOM   2732 C CD1 . PHE B 2 63  ? 24.140 19.082  -6.967  1.00 23.64  ? 62  PHE B CD1 1 
ATOM   2733 C CD2 . PHE B 2 63  ? 25.933 19.523  -5.448  1.00 22.27  ? 62  PHE B CD2 1 
ATOM   2734 C CE1 . PHE B 2 63  ? 24.967 18.223  -7.698  1.00 21.83  ? 62  PHE B CE1 1 
ATOM   2735 C CE2 . PHE B 2 63  ? 26.754 18.677  -6.162  1.00 24.54  ? 62  PHE B CE2 1 
ATOM   2736 C CZ  . PHE B 2 63  ? 26.276 18.025  -7.296  1.00 23.95  ? 62  PHE B CZ  1 
ATOM   2737 N N   . TYR B 2 64  ? 21.279 22.475  -5.000  1.00 22.94  ? 63  TYR B N   1 
ATOM   2738 C CA  . TYR B 2 64  ? 20.229 23.080  -4.203  1.00 24.21  ? 63  TYR B CA  1 
ATOM   2739 C C   . TYR B 2 64  ? 19.155 22.044  -3.930  1.00 24.44  ? 63  TYR B C   1 
ATOM   2740 O O   . TYR B 2 64  ? 18.899 21.159  -4.750  1.00 25.72  ? 63  TYR B O   1 
ATOM   2741 C CB  . TYR B 2 64  ? 19.621 24.330  -4.868  1.00 25.24  ? 63  TYR B CB  1 
ATOM   2742 C CG  . TYR B 2 64  ? 18.932 24.154  -6.224  1.00 24.55  ? 63  TYR B CG  1 
ATOM   2743 C CD1 . TYR B 2 64  ? 17.597 23.767  -6.304  1.00 29.22  ? 63  TYR B CD1 1 
ATOM   2744 C CD2 . TYR B 2 64  ? 19.607 24.424  -7.417  1.00 27.91  ? 63  TYR B CD2 1 
ATOM   2745 C CE1 . TYR B 2 64  ? 16.956 23.632  -7.527  1.00 26.70  ? 63  TYR B CE1 1 
ATOM   2746 C CE2 . TYR B 2 64  ? 18.971 24.284  -8.661  1.00 27.26  ? 63  TYR B CE2 1 
ATOM   2747 C CZ  . TYR B 2 64  ? 17.646 23.889  -8.701  1.00 28.17  ? 63  TYR B CZ  1 
ATOM   2748 O OH  . TYR B 2 64  ? 16.995 23.755  -9.902  1.00 34.71  ? 63  TYR B OH  1 
ATOM   2749 N N   . LEU B 2 65  ? 18.515 22.186  -2.774  1.00 23.81  ? 64  LEU B N   1 
ATOM   2750 C CA  . LEU B 2 65  ? 17.450 21.296  -2.349  1.00 25.77  ? 64  LEU B CA  1 
ATOM   2751 C C   . LEU B 2 65  ? 16.472 22.111  -1.521  1.00 27.49  ? 64  LEU B C   1 
ATOM   2752 O O   . LEU B 2 65  ? 16.878 23.012  -0.778  1.00 28.30  ? 64  LEU B O   1 
ATOM   2753 C CB  . LEU B 2 65  ? 17.976 20.117  -1.503  1.00 24.92  ? 64  LEU B CB  1 
ATOM   2754 C CG  . LEU B 2 65  ? 18.715 18.920  -2.120  1.00 30.07  ? 64  LEU B CG  1 
ATOM   2755 C CD1 . LEU B 2 65  ? 19.482 18.141  -1.032  1.00 24.48  ? 64  LEU B CD1 1 
ATOM   2756 C CD2 . LEU B 2 65  ? 17.777 17.971  -2.863  1.00 22.36  ? 64  LEU B CD2 1 
ATOM   2757 N N   . LEU B 2 66  ? 15.194 21.763  -1.620  1.00 25.75  ? 65  LEU B N   1 
ATOM   2758 C CA  . LEU B 2 66  ? 14.159 22.294  -0.748  1.00 26.82  ? 65  LEU B CA  1 
ATOM   2759 C C   . LEU B 2 66  ? 13.634 21.171  0.129   1.00 25.32  ? 65  LEU B C   1 
ATOM   2760 O O   . LEU B 2 66  ? 13.151 20.166  -0.393  1.00 26.90  ? 65  LEU B O   1 
ATOM   2761 C CB  . LEU B 2 66  ? 13.020 22.902  -1.561  1.00 26.68  ? 65  LEU B CB  1 
ATOM   2762 C CG  . LEU B 2 66  ? 11.814 23.394  -0.754  1.00 29.89  ? 65  LEU B CG  1 
ATOM   2763 C CD1 . LEU B 2 66  ? 12.165 24.655  0.041   1.00 28.34  ? 65  LEU B CD1 1 
ATOM   2764 C CD2 . LEU B 2 66  ? 10.607 23.637  -1.660  1.00 27.69  ? 65  LEU B CD2 1 
ATOM   2765 N N   . TYR B 2 67  ? 13.723 21.342  1.459   1.00 27.02  ? 66  TYR B N   1 
ATOM   2766 C CA  . TYR B 2 67  ? 13.015 20.482  2.406   1.00 25.43  ? 66  TYR B CA  1 
ATOM   2767 C C   . TYR B 2 67  ? 11.799 21.218  2.949   1.00 28.09  ? 66  TYR B C   1 
ATOM   2768 O O   . TYR B 2 67  ? 11.851 22.427  3.206   1.00 35.68  ? 66  TYR B O   1 
ATOM   2769 C CB  . TYR B 2 67  ? 13.906 20.046  3.572   1.00 29.42  ? 66  TYR B CB  1 
ATOM   2770 C CG  . TYR B 2 67  ? 14.978 19.058  3.193   1.00 29.86  ? 66  TYR B CG  1 
ATOM   2771 C CD1 . TYR B 2 67  ? 16.062 19.457  2.424   1.00 28.78  ? 66  TYR B CD1 1 
ATOM   2772 C CD2 . TYR B 2 67  ? 14.913 17.731  3.609   1.00 28.31  ? 66  TYR B CD2 1 
ATOM   2773 C CE1 . TYR B 2 67  ? 17.061 18.557  2.074   1.00 34.08  ? 66  TYR B CE1 1 
ATOM   2774 C CE2 . TYR B 2 67  ? 15.903 16.820  3.259   1.00 31.91  ? 66  TYR B CE2 1 
ATOM   2775 C CZ  . TYR B 2 67  ? 16.976 17.247  2.491   1.00 31.42  ? 66  TYR B CZ  1 
ATOM   2776 O OH  . TYR B 2 67  ? 17.982 16.381  2.145   1.00 32.15  ? 66  TYR B OH  1 
ATOM   2777 N N   . TYR B 2 68  ? 10.707 20.491  3.141   1.00 24.79  ? 67  TYR B N   1 
ATOM   2778 C CA  . TYR B 2 68  ? 9.456  21.180  3.410   1.00 31.42  ? 67  TYR B CA  1 
ATOM   2779 C C   . TYR B 2 68  ? 8.499  20.254  4.141   1.00 34.58  ? 67  TYR B C   1 
ATOM   2780 O O   . TYR B 2 68  ? 8.549  19.033  3.975   1.00 34.10  ? 67  TYR B O   1 
ATOM   2781 C CB  . TYR B 2 68  ? 8.815  21.713  2.114   1.00 30.26  ? 67  TYR B CB  1 
ATOM   2782 C CG  . TYR B 2 68  ? 8.476  20.656  1.083   1.00 34.44  ? 67  TYR B CG  1 
ATOM   2783 C CD1 . TYR B 2 68  ? 9.416  20.254  0.126   1.00 31.06  ? 67  TYR B CD1 1 
ATOM   2784 C CD2 . TYR B 2 68  ? 7.209  20.073  1.049   1.00 33.00  ? 67  TYR B CD2 1 
ATOM   2785 C CE1 . TYR B 2 68  ? 9.101  19.283  -0.832  1.00 30.40  ? 67  TYR B CE1 1 
ATOM   2786 C CE2 . TYR B 2 68  ? 6.886  19.111  0.109   1.00 32.70  ? 67  TYR B CE2 1 
ATOM   2787 C CZ  . TYR B 2 68  ? 7.836  18.721  -0.832  1.00 38.81  ? 67  TYR B CZ  1 
ATOM   2788 O OH  . TYR B 2 68  ? 7.510  17.768  -1.765  1.00 39.33  ? 67  TYR B OH  1 
ATOM   2789 N N   . THR B 2 69  ? 7.629  20.863  4.953   1.00 37.50  ? 68  THR B N   1 
ATOM   2790 C CA  . THR B 2 69  ? 6.595  20.157  5.700   1.00 36.28  ? 68  THR B CA  1 
ATOM   2791 C C   . THR B 2 69  ? 5.411  21.090  5.929   1.00 36.35  ? 68  THR B C   1 
ATOM   2792 O O   . THR B 2 69  ? 5.568  22.310  6.021   1.00 36.87  ? 68  THR B O   1 
ATOM   2793 C CB  . THR B 2 69  ? 7.126  19.622  7.049   1.00 39.17  ? 68  THR B CB  1 
ATOM   2794 O OG1 . THR B 2 69  ? 6.294  18.547  7.499   1.00 45.43  ? 68  THR B OG1 1 
ATOM   2795 C CG2 . THR B 2 69  ? 7.160  20.707  8.121   1.00 33.22  ? 68  THR B CG2 1 
ATOM   2796 N N   . GLU B 2 70  ? 4.223  20.503  6.012   1.00 42.35  ? 69  GLU B N   1 
ATOM   2797 C CA  . GLU B 2 70  ? 3.038  21.258  6.401   1.00 44.10  ? 69  GLU B CA  1 
ATOM   2798 C C   . GLU B 2 70  ? 3.062  21.531  7.899   1.00 43.18  ? 69  GLU B C   1 
ATOM   2799 O O   . GLU B 2 70  ? 3.533  20.703  8.686   1.00 42.91  ? 69  GLU B O   1 
ATOM   2800 C CB  . GLU B 2 70  ? 1.769  20.489  6.041   1.00 45.99  ? 69  GLU B CB  1 
ATOM   2801 C CG  . GLU B 2 70  ? 0.581  21.361  5.698   1.00 50.93  ? 69  GLU B CG  1 
ATOM   2802 C CD  . GLU B 2 70  ? -0.426 20.616  4.833   1.00 61.52  ? 69  GLU B CD  1 
ATOM   2803 O OE1 . GLU B 2 70  ? -0.056 19.541  4.298   1.00 58.97  ? 69  GLU B OE1 1 
ATOM   2804 O OE2 . GLU B 2 70  ? -1.574 21.101  4.693   1.00 59.77  ? 69  GLU B OE2 1 
ATOM   2805 N N   . PHE B 2 71  ? 2.549  22.696  8.287   1.00 41.19  ? 70  PHE B N   1 
ATOM   2806 C CA  . PHE B 2 71  ? 2.473  23.075  9.691   1.00 43.72  ? 70  PHE B CA  1 
ATOM   2807 C C   . PHE B 2 71  ? 1.503  24.239  9.816   1.00 47.67  ? 70  PHE B C   1 
ATOM   2808 O O   . PHE B 2 71  ? 1.216  24.939  8.839   1.00 44.46  ? 70  PHE B O   1 
ATOM   2809 C CB  . PHE B 2 71  ? 3.850  23.443  10.268  1.00 39.65  ? 70  PHE B CB  1 
ATOM   2810 C CG  . PHE B 2 71  ? 4.298  24.858  9.966   1.00 40.26  ? 70  PHE B CG  1 
ATOM   2811 C CD1 . PHE B 2 71  ? 4.317  25.340  8.671   1.00 40.25  ? 70  PHE B CD1 1 
ATOM   2812 C CD2 . PHE B 2 71  ? 4.713  25.696  10.985  1.00 42.03  ? 70  PHE B CD2 1 
ATOM   2813 C CE1 . PHE B 2 71  ? 4.726  26.640  8.400   1.00 39.99  ? 70  PHE B CE1 1 
ATOM   2814 C CE2 . PHE B 2 71  ? 5.129  26.993  10.720  1.00 40.57  ? 70  PHE B CE2 1 
ATOM   2815 C CZ  . PHE B 2 71  ? 5.134  27.465  9.425   1.00 42.60  ? 70  PHE B CZ  1 
ATOM   2816 N N   . THR B 2 72  ? 0.988  24.419  11.028  1.00 44.51  ? 71  THR B N   1 
ATOM   2817 C CA  . THR B 2 72  ? 0.166  25.583  11.364  1.00 50.35  ? 71  THR B CA  1 
ATOM   2818 C C   . THR B 2 72  ? 0.873  26.337  12.482  1.00 46.88  ? 71  THR B C   1 
ATOM   2819 O O   . THR B 2 72  ? 0.956  25.826  13.615  1.00 47.92  ? 71  THR B O   1 
ATOM   2820 C CB  . THR B 2 72  ? -1.252 25.178  11.784  1.00 50.97  ? 71  THR B CB  1 
ATOM   2821 O OG1 . THR B 2 72  ? -1.192 24.194  12.827  1.00 61.16  ? 71  THR B OG1 1 
ATOM   2822 C CG2 . THR B 2 72  ? -2.003 24.584  10.615  1.00 46.96  ? 71  THR B CG2 1 
ATOM   2823 N N   . PRO B 2 73  ? 1.416  27.522  12.224  1.00 46.23  ? 72  PRO B N   1 
ATOM   2824 C CA  . PRO B 2 73  ? 2.200  28.213  13.252  1.00 50.90  ? 72  PRO B CA  1 
ATOM   2825 C C   . PRO B 2 73  ? 1.325  28.788  14.362  1.00 54.68  ? 72  PRO B C   1 
ATOM   2826 O O   . PRO B 2 73  ? 0.132  29.049  14.194  1.00 50.82  ? 72  PRO B O   1 
ATOM   2827 C CB  . PRO B 2 73  ? 2.906  29.328  12.470  1.00 45.29  ? 72  PRO B CB  1 
ATOM   2828 C CG  . PRO B 2 73  ? 1.984  29.628  11.342  1.00 50.16  ? 72  PRO B CG  1 
ATOM   2829 C CD  . PRO B 2 73  ? 1.307  28.312  10.983  1.00 49.54  ? 72  PRO B CD  1 
ATOM   2830 N N   . THR B 2 74  ? 1.959  28.976  15.517  1.00 52.97  ? 73  THR B N   1 
ATOM   2831 C CA  . THR B 2 74  ? 1.376  29.627  16.680  1.00 49.83  ? 73  THR B CA  1 
ATOM   2832 C C   . THR B 2 74  ? 2.308  30.758  17.103  1.00 55.11  ? 73  THR B C   1 
ATOM   2833 O O   . THR B 2 74  ? 3.329  31.015  16.454  1.00 55.53  ? 73  THR B O   1 
ATOM   2834 C CB  . THR B 2 74  ? 1.172  28.618  17.810  1.00 46.84  ? 73  THR B CB  1 
ATOM   2835 O OG1 . THR B 2 74  ? 2.450  28.125  18.231  1.00 49.07  ? 73  THR B OG1 1 
ATOM   2836 C CG2 . THR B 2 74  ? 0.329  27.450  17.336  1.00 48.15  ? 73  THR B CG2 1 
ATOM   2837 N N   . GLU B 2 75  ? 1.967  31.442  18.203  1.00 56.96  ? 74  GLU B N   1 
ATOM   2838 C CA  . GLU B 2 75  ? 2.903  32.428  18.738  1.00 53.06  ? 74  GLU B CA  1 
ATOM   2839 C C   . GLU B 2 75  ? 3.971  31.767  19.600  1.00 49.49  ? 74  GLU B C   1 
ATOM   2840 O O   . GLU B 2 75  ? 5.070  32.306  19.745  1.00 52.17  ? 74  GLU B O   1 
ATOM   2841 C CB  . GLU B 2 75  ? 2.155  33.519  19.523  1.00 59.68  ? 74  GLU B CB  1 
ATOM   2842 C CG  . GLU B 2 75  ? 1.573  33.123  20.871  1.00 67.78  ? 74  GLU B CG  1 
ATOM   2843 C CD  . GLU B 2 75  ? 0.976  34.327  21.604  1.00 74.66  ? 74  GLU B CD  1 
ATOM   2844 O OE1 . GLU B 2 75  ? -0.068 34.839  21.145  1.00 76.24  ? 74  GLU B OE1 1 
ATOM   2845 O OE2 . GLU B 2 75  ? 1.553  34.770  22.623  1.00 72.80  ? 74  GLU B OE2 1 
ATOM   2846 N N   . LYS B 2 76  ? 3.687  30.587  20.141  1.00 51.78  ? 75  LYS B N   1 
ATOM   2847 C CA  . LYS B 2 76  ? 4.582  29.932  21.089  1.00 57.12  ? 75  LYS B CA  1 
ATOM   2848 C C   . LYS B 2 76  ? 5.585  28.963  20.454  1.00 52.45  ? 75  LYS B C   1 
ATOM   2849 O O   . LYS B 2 76  ? 6.611  28.661  21.077  1.00 52.51  ? 75  LYS B O   1 
ATOM   2850 C CB  . LYS B 2 76  ? 3.760  29.170  22.146  1.00 61.35  ? 75  LYS B CB  1 
ATOM   2851 N N   . ASP B 2 77  ? 5.335  28.462  19.249  1.00 51.22  ? 76  ASP B N   1 
ATOM   2852 C CA  . ASP B 2 77  ? 6.141  27.377  18.697  1.00 45.79  ? 76  ASP B CA  1 
ATOM   2853 C C   . ASP B 2 77  ? 7.292  27.932  17.863  1.00 43.62  ? 76  ASP B C   1 
ATOM   2854 O O   . ASP B 2 77  ? 7.072  28.699  16.918  1.00 44.71  ? 76  ASP B O   1 
ATOM   2855 C CB  . ASP B 2 77  ? 5.259  26.444  17.874  1.00 43.74  ? 76  ASP B CB  1 
ATOM   2856 C CG  . ASP B 2 77  ? 4.296  25.654  18.742  1.00 48.12  ? 76  ASP B CG  1 
ATOM   2857 O OD1 . ASP B 2 77  ? 4.624  25.422  19.928  1.00 52.40  ? 76  ASP B OD1 1 
ATOM   2858 O OD2 . ASP B 2 77  ? 3.207  25.286  18.250  1.00 46.86  ? 76  ASP B OD2 1 
ATOM   2859 N N   . GLU B 2 78  ? 8.518  27.542  18.218  1.00 42.80  ? 77  GLU B N   1 
ATOM   2860 C CA  . GLU B 2 78  ? 9.703  27.907  17.455  1.00 45.37  ? 77  GLU B CA  1 
ATOM   2861 C C   . GLU B 2 78  ? 10.005 26.837  16.410  1.00 42.38  ? 77  GLU B C   1 
ATOM   2862 O O   . GLU B 2 78  ? 9.836  25.638  16.657  1.00 38.51  ? 77  GLU B O   1 
ATOM   2863 C CB  . GLU B 2 78  ? 10.913 28.095  18.373  1.00 42.73  ? 77  GLU B CB  1 
ATOM   2864 C CG  . GLU B 2 78  ? 10.647 28.977  19.584  1.00 56.83  ? 77  GLU B CG  1 
ATOM   2865 C CD  . GLU B 2 78  ? 11.027 30.436  19.357  1.00 68.09  ? 77  GLU B CD  1 
ATOM   2866 O OE1 . GLU B 2 78  ? 12.240 30.741  19.286  1.00 70.54  ? 77  GLU B OE1 1 
ATOM   2867 O OE2 . GLU B 2 78  ? 10.110 31.281  19.252  1.00 71.56  ? 77  GLU B OE2 1 
ATOM   2868 N N   . TYR B 2 79  ? 10.446 27.279  15.233  1.00 38.24  ? 78  TYR B N   1 
ATOM   2869 C CA  . TYR B 2 79  ? 10.793 26.365  14.154  1.00 37.58  ? 78  TYR B CA  1 
ATOM   2870 C C   . TYR B 2 79  ? 12.190 26.666  13.651  1.00 33.70  ? 78  TYR B C   1 
ATOM   2871 O O   . TYR B 2 79  ? 12.674 27.796  13.746  1.00 32.66  ? 78  TYR B O   1 
ATOM   2872 C CB  . TYR B 2 79  ? 9.795  26.439  13.004  1.00 34.42  ? 78  TYR B CB  1 
ATOM   2873 C CG  . TYR B 2 79  ? 8.479  25.818  13.379  1.00 36.12  ? 78  TYR B CG  1 
ATOM   2874 C CD1 . TYR B 2 79  ? 8.275  24.459  13.229  1.00 34.96  ? 78  TYR B CD1 1 
ATOM   2875 C CD2 . TYR B 2 79  ? 7.454  26.584  13.930  1.00 37.86  ? 78  TYR B CD2 1 
ATOM   2876 C CE1 . TYR B 2 79  ? 7.089  23.875  13.587  1.00 35.49  ? 78  TYR B CE1 1 
ATOM   2877 C CE2 . TYR B 2 79  ? 6.250  26.005  14.290  1.00 39.02  ? 78  TYR B CE2 1 
ATOM   2878 C CZ  . TYR B 2 79  ? 6.077  24.646  14.115  1.00 39.18  ? 78  TYR B CZ  1 
ATOM   2879 O OH  . TYR B 2 79  ? 4.890  24.038  14.456  1.00 42.18  ? 78  TYR B OH  1 
ATOM   2880 N N   . ALA B 2 80  ? 12.846 25.640  13.126  1.00 28.78  ? 79  ALA B N   1 
ATOM   2881 C CA  . ALA B 2 80  ? 14.225 25.818  12.711  1.00 33.91  ? 79  ALA B CA  1 
ATOM   2882 C C   . ALA B 2 80  ? 14.587 24.741  11.706  1.00 29.77  ? 79  ALA B C   1 
ATOM   2883 O O   . ALA B 2 80  ? 13.889 23.733  11.553  1.00 31.23  ? 79  ALA B O   1 
ATOM   2884 C CB  . ALA B 2 80  ? 15.176 25.790  13.917  1.00 34.46  ? 79  ALA B CB  1 
ATOM   2885 N N   . CYS B 2 81  ? 15.712 24.969  11.041  1.00 30.68  ? 80  CYS B N   1 
ATOM   2886 C CA  . CYS B 2 81  ? 16.313 24.019  10.115  1.00 38.19  ? 80  CYS B CA  1 
ATOM   2887 C C   . CYS B 2 81  ? 17.714 23.676  10.610  1.00 33.51  ? 80  CYS B C   1 
ATOM   2888 O O   . CYS B 2 81  ? 18.496 24.577  10.936  1.00 37.80  ? 80  CYS B O   1 
ATOM   2889 C CB  . CYS B 2 81  ? 16.367 24.602  8.701   1.00 31.59  ? 80  CYS B CB  1 
ATOM   2890 S SG  . CYS B 2 81  ? 17.013 23.481  7.484   1.00 48.62  ? 80  CYS B SG  1 
ATOM   2891 N N   . ARG B 2 82  ? 18.018 22.382  10.681  1.00 32.25  ? 81  ARG B N   1 
ATOM   2892 C CA  . ARG B 2 82  ? 19.310 21.879  11.139  1.00 31.96  ? 81  ARG B CA  1 
ATOM   2893 C C   . ARG B 2 82  ? 20.003 21.184  9.969   1.00 30.10  ? 81  ARG B C   1 
ATOM   2894 O O   . ARG B 2 82  ? 19.493 20.188  9.447   1.00 28.55  ? 81  ARG B O   1 
ATOM   2895 C CB  . ARG B 2 82  ? 19.124 20.919  12.317  1.00 32.59  ? 81  ARG B CB  1 
ATOM   2896 C CG  . ARG B 2 82  ? 20.415 20.388  12.968  1.00 36.21  ? 81  ARG B CG  1 
ATOM   2897 C CD  . ARG B 2 82  ? 20.249 18.912  13.377  1.00 39.80  ? 81  ARG B CD  1 
ATOM   2898 N NE  . ARG B 2 82  ? 19.601 18.747  14.669  1.00 43.29  ? 81  ARG B NE  1 
ATOM   2899 C CZ  . ARG B 2 82  ? 18.711 17.801  14.968  1.00 41.69  ? 81  ARG B CZ  1 
ATOM   2900 N NH1 . ARG B 2 82  ? 18.333 16.903  14.067  1.00 35.86  ? 81  ARG B NH1 1 
ATOM   2901 N NH2 . ARG B 2 82  ? 18.203 17.754  16.194  1.00 40.28  ? 81  ARG B NH2 1 
ATOM   2902 N N   . VAL B 2 83  ? 21.165 21.698  9.571   1.00 28.67  ? 82  VAL B N   1 
ATOM   2903 C CA  . VAL B 2 83  ? 21.863 21.239  8.375   1.00 35.23  ? 82  VAL B CA  1 
ATOM   2904 C C   . VAL B 2 83  ? 23.248 20.718  8.739   1.00 32.89  ? 82  VAL B C   1 
ATOM   2905 O O   . VAL B 2 83  ? 23.975 21.343  9.521   1.00 28.35  ? 82  VAL B O   1 
ATOM   2906 C CB  . VAL B 2 83  ? 21.984 22.363  7.322   1.00 32.27  ? 82  VAL B CB  1 
ATOM   2907 C CG1 . VAL B 2 83  ? 22.807 21.881  6.114   1.00 28.21  ? 82  VAL B CG1 1 
ATOM   2908 C CG2 . VAL B 2 83  ? 20.610 22.844  6.897   1.00 26.34  ? 82  VAL B CG2 1 
ATOM   2909 N N   . ASN B 2 84  ? 23.631 19.597  8.131   1.00 28.33  ? 83  ASN B N   1 
ATOM   2910 C CA  . ASN B 2 84  ? 25.005 19.137  8.204   1.00 31.57  ? 83  ASN B CA  1 
ATOM   2911 C C   . ASN B 2 84  ? 25.572 18.819  6.823   1.00 35.64  ? 83  ASN B C   1 
ATOM   2912 O O   . ASN B 2 84  ? 24.883 18.302  5.934   1.00 32.05  ? 83  ASN B O   1 
ATOM   2913 C CB  . ASN B 2 84  ? 25.152 17.916  9.106   1.00 36.81  ? 83  ASN B CB  1 
ATOM   2914 C CG  . ASN B 2 84  ? 26.337 18.050  10.027  1.00 43.94  ? 83  ASN B CG  1 
ATOM   2915 O OD1 . ASN B 2 84  ? 27.392 18.569  9.629   1.00 40.19  ? 83  ASN B OD1 1 
ATOM   2916 N ND2 . ASN B 2 84  ? 26.172 17.614  11.269  1.00 49.71  ? 83  ASN B ND2 1 
ATOM   2917 N N   . HIS B 2 85  ? 26.867 19.087  6.688   1.00 31.79  ? 84  HIS B N   1 
ATOM   2918 C CA  . HIS B 2 85  ? 27.572 19.015  5.419   1.00 36.40  ? 84  HIS B CA  1 
ATOM   2919 C C   . HIS B 2 85  ? 29.056 18.887  5.731   1.00 34.91  ? 84  HIS B C   1 
ATOM   2920 O O   . HIS B 2 85  ? 29.501 19.231  6.829   1.00 36.63  ? 84  HIS B O   1 
ATOM   2921 C CB  . HIS B 2 85  ? 27.278 20.259  4.568   1.00 30.81  ? 84  HIS B CB  1 
ATOM   2922 C CG  . HIS B 2 85  ? 27.822 20.189  3.181   1.00 30.83  ? 84  HIS B CG  1 
ATOM   2923 N ND1 . HIS B 2 85  ? 28.872 20.974  2.757   1.00 30.89  ? 84  HIS B ND1 1 
ATOM   2924 C CD2 . HIS B 2 85  ? 27.462 19.430  2.119   1.00 25.54  ? 84  HIS B CD2 1 
ATOM   2925 C CE1 . HIS B 2 85  ? 29.139 20.700  1.492   1.00 29.10  ? 84  HIS B CE1 1 
ATOM   2926 N NE2 . HIS B 2 85  ? 28.293 19.771  1.081   1.00 28.82  ? 84  HIS B NE2 1 
ATOM   2927 N N   . VAL B 2 86  ? 29.822 18.388  4.757   1.00 33.03  ? 85  VAL B N   1 
ATOM   2928 C CA  . VAL B 2 86  ? 31.244 18.148  5.010   1.00 34.35  ? 85  VAL B CA  1 
ATOM   2929 C C   . VAL B 2 86  ? 31.975 19.454  5.314   1.00 34.59  ? 85  VAL B C   1 
ATOM   2930 O O   . VAL B 2 86  ? 32.988 19.452  6.014   1.00 37.50  ? 85  VAL B O   1 
ATOM   2931 C CB  . VAL B 2 86  ? 31.903 17.392  3.834   1.00 37.06  ? 85  VAL B CB  1 
ATOM   2932 C CG1 . VAL B 2 86  ? 31.890 18.234  2.572   1.00 29.09  ? 85  VAL B CG1 1 
ATOM   2933 C CG2 . VAL B 2 86  ? 33.340 16.978  4.198   1.00 33.40  ? 85  VAL B CG2 1 
ATOM   2934 N N   . THR B 2 87  ? 31.476 20.586  4.815   1.00 34.78  ? 86  THR B N   1 
ATOM   2935 C CA  . THR B 2 87  ? 32.078 21.874  5.139   1.00 36.24  ? 86  THR B CA  1 
ATOM   2936 C C   . THR B 2 87  ? 31.744 22.368  6.548   1.00 39.03  ? 86  THR B C   1 
ATOM   2937 O O   . THR B 2 87  ? 32.304 23.384  6.969   1.00 32.58  ? 86  THR B O   1 
ATOM   2938 C CB  . THR B 2 87  ? 31.631 22.947  4.150   1.00 33.34  ? 86  THR B CB  1 
ATOM   2939 O OG1 . THR B 2 87  ? 30.204 22.916  4.044   1.00 39.14  ? 86  THR B OG1 1 
ATOM   2940 C CG2 . THR B 2 87  ? 32.253 22.730  2.779   1.00 36.07  ? 86  THR B CG2 1 
ATOM   2941 N N   . LEU B 2 88  ? 30.847 21.703  7.276   1.00 35.81  ? 87  LEU B N   1 
ATOM   2942 C CA  . LEU B 2 88  ? 30.420 22.171  8.589   1.00 44.90  ? 87  LEU B CA  1 
ATOM   2943 C C   . LEU B 2 88  ? 31.053 21.325  9.686   1.00 43.06  ? 87  LEU B C   1 
ATOM   2944 O O   . LEU B 2 88  ? 30.967 20.091  9.654   1.00 45.29  ? 87  LEU B O   1 
ATOM   2945 C CB  . LEU B 2 88  ? 28.897 22.129  8.722   1.00 41.99  ? 87  LEU B CB  1 
ATOM   2946 C CG  . LEU B 2 88  ? 28.195 22.977  7.667   1.00 38.85  ? 87  LEU B CG  1 
ATOM   2947 C CD1 . LEU B 2 88  ? 26.681 22.823  7.774   1.00 33.01  ? 87  LEU B CD1 1 
ATOM   2948 C CD2 . LEU B 2 88  ? 28.635 24.433  7.826   1.00 38.69  ? 87  LEU B CD2 1 
ATOM   2949 N N   . SER B 2 89  ? 31.675 22.003  10.658  1.00 44.35  ? 88  SER B N   1 
ATOM   2950 C CA  . SER B 2 89  ? 32.267 21.320  11.807  1.00 44.88  ? 88  SER B CA  1 
ATOM   2951 C C   . SER B 2 89  ? 31.206 20.637  12.654  1.00 48.40  ? 88  SER B C   1 
ATOM   2952 O O   . SER B 2 89  ? 31.422 19.540  13.176  1.00 50.01  ? 88  SER B O   1 
ATOM   2953 C CB  . SER B 2 89  ? 33.038 22.324  12.656  1.00 41.26  ? 88  SER B CB  1 
ATOM   2954 O OG  . SER B 2 89  ? 34.384 22.361  12.240  1.00 51.81  ? 88  SER B OG  1 
ATOM   2955 N N   . GLN B 2 90  ? 30.065 21.285  12.816  1.00 48.76  ? 89  GLN B N   1 
ATOM   2956 C CA  . GLN B 2 90  ? 28.952 20.802  13.613  1.00 51.11  ? 89  GLN B CA  1 
ATOM   2957 C C   . GLN B 2 90  ? 27.673 21.146  12.869  1.00 42.88  ? 89  GLN B C   1 
ATOM   2958 O O   . GLN B 2 90  ? 27.690 21.985  11.965  1.00 40.44  ? 89  GLN B O   1 
ATOM   2959 C CB  . GLN B 2 90  ? 28.964 21.453  15.002  1.00 50.40  ? 89  GLN B CB  1 
ATOM   2960 C CG  . GLN B 2 90  ? 29.328 22.928  14.956  1.00 50.83  ? 89  GLN B CG  1 
ATOM   2961 C CD  . GLN B 2 90  ? 29.302 23.578  16.324  1.00 67.00  ? 89  GLN B CD  1 
ATOM   2962 O OE1 . GLN B 2 90  ? 29.244 22.896  17.349  1.00 67.00  ? 89  GLN B OE1 1 
ATOM   2963 N NE2 . GLN B 2 90  ? 29.345 24.906  16.348  1.00 69.21  ? 89  GLN B NE2 1 
ATOM   2964 N N   . PRO B 2 91  ? 26.552 20.519  13.224  1.00 48.42  ? 90  PRO B N   1 
ATOM   2965 C CA  . PRO B 2 91  ? 25.272 20.926  12.629  1.00 40.89  ? 90  PRO B CA  1 
ATOM   2966 C C   . PRO B 2 91  ? 25.057 22.429  12.772  1.00 45.33  ? 90  PRO B C   1 
ATOM   2967 O O   . PRO B 2 91  ? 25.478 23.049  13.756  1.00 43.17  ? 90  PRO B O   1 
ATOM   2968 C CB  . PRO B 2 91  ? 24.239 20.127  13.430  1.00 39.23  ? 90  PRO B CB  1 
ATOM   2969 C CG  . PRO B 2 91  ? 24.990 18.911  13.899  1.00 43.01  ? 90  PRO B CG  1 
ATOM   2970 C CD  . PRO B 2 91  ? 26.384 19.408  14.183  1.00 48.17  ? 90  PRO B CD  1 
ATOM   2971 N N   . LYS B 2 92  ? 24.447 23.027  11.753  1.00 36.12  ? 91  LYS B N   1 
ATOM   2972 C CA  . LYS B 2 92  ? 24.121 24.442  11.767  1.00 39.10  ? 91  LYS B CA  1 
ATOM   2973 C C   . LYS B 2 92  ? 22.611 24.599  11.863  1.00 44.55  ? 91  LYS B C   1 
ATOM   2974 O O   . LYS B 2 92  ? 21.862 23.989  11.087  1.00 36.32  ? 91  LYS B O   1 
ATOM   2975 C CB  . LYS B 2 92  ? 24.652 25.165  10.529  1.00 42.48  ? 91  LYS B CB  1 
ATOM   2976 C CG  . LYS B 2 92  ? 24.634 26.687  10.687  1.00 47.60  ? 91  LYS B CG  1 
ATOM   2977 C CD  . LYS B 2 92  ? 25.176 27.399  9.455   1.00 47.79  ? 91  LYS B CD  1 
ATOM   2978 C CE  . LYS B 2 92  ? 26.704 27.329  9.403   1.00 52.83  ? 91  LYS B CE  1 
ATOM   2979 N NZ  . LYS B 2 92  ? 27.382 28.430  10.154  1.00 62.29  ? 91  LYS B NZ  1 
ATOM   2980 N N   . ILE B 2 93  ? 22.178 25.408  12.823  1.00 42.10  ? 92  ILE B N   1 
ATOM   2981 C CA  . ILE B 2 93  ? 20.772 25.616  13.130  1.00 39.43  ? 92  ILE B CA  1 
ATOM   2982 C C   . ILE B 2 93  ? 20.429 27.057  12.774  1.00 41.90  ? 92  ILE B C   1 
ATOM   2983 O O   . ILE B 2 93  ? 21.043 27.994  13.297  1.00 48.53  ? 92  ILE B O   1 
ATOM   2984 C CB  . ILE B 2 93  ? 20.481 25.315  14.606  1.00 40.42  ? 92  ILE B CB  1 
ATOM   2985 C CG1 . ILE B 2 93  ? 20.798 23.840  14.892  1.00 41.54  ? 92  ILE B CG1 1 
ATOM   2986 C CG2 . ILE B 2 93  ? 19.037 25.688  14.970  1.00 38.24  ? 92  ILE B CG2 1 
ATOM   2987 C CD1 . ILE B 2 93  ? 20.019 23.239  16.058  1.00 42.63  ? 92  ILE B CD1 1 
ATOM   2988 N N   . VAL B 2 94  ? 19.482 27.233  11.859  1.00 36.18  ? 93  VAL B N   1 
ATOM   2989 C CA  . VAL B 2 94  ? 18.946 28.544  11.508  1.00 38.87  ? 93  VAL B CA  1 
ATOM   2990 C C   . VAL B 2 94  ? 17.491 28.576  11.941  1.00 35.59  ? 93  VAL B C   1 
ATOM   2991 O O   . VAL B 2 94  ? 16.685 27.754  11.483  1.00 38.16  ? 93  VAL B O   1 
ATOM   2992 C CB  . VAL B 2 94  ? 19.076 28.839  10.005  1.00 35.42  ? 93  VAL B CB  1 
ATOM   2993 C CG1 . VAL B 2 94  ? 18.951 30.343  9.739   1.00 33.31  ? 93  VAL B CG1 1 
ATOM   2994 C CG2 . VAL B 2 94  ? 20.406 28.316  9.488   1.00 37.69  ? 93  VAL B CG2 1 
ATOM   2995 N N   . LYS B 2 95  ? 17.153 29.532  12.804  1.00 33.45  ? 94  LYS B N   1 
ATOM   2996 C CA  . LYS B 2 95  ? 15.808 29.637  13.345  1.00 34.91  ? 94  LYS B CA  1 
ATOM   2997 C C   . LYS B 2 95  ? 14.874 30.307  12.342  1.00 36.43  ? 94  LYS B C   1 
ATOM   2998 O O   . LYS B 2 95  ? 15.284 31.164  11.552  1.00 29.73  ? 94  LYS B O   1 
ATOM   2999 C CB  . LYS B 2 95  ? 15.828 30.419  14.664  1.00 40.60  ? 94  LYS B CB  1 
ATOM   3000 C CG  . LYS B 2 95  ? 16.454 29.633  15.825  1.00 41.90  ? 94  LYS B CG  1 
ATOM   3001 C CD  . LYS B 2 95  ? 17.308 30.503  16.741  1.00 52.43  ? 94  LYS B CD  1 
ATOM   3002 C CE  . LYS B 2 95  ? 18.576 29.756  17.196  1.00 59.24  ? 94  LYS B CE  1 
ATOM   3003 N NZ  . LYS B 2 95  ? 19.527 29.480  16.056  1.00 56.39  ? 94  LYS B NZ  1 
ATOM   3004 N N   . TRP B 2 96  ? 13.609 29.893  12.362  1.00 32.44  ? 95  TRP B N   1 
ATOM   3005 C CA  . TRP B 2 96  ? 12.595 30.564  11.558  1.00 35.02  ? 95  TRP B CA  1 
ATOM   3006 C C   . TRP B 2 96  ? 12.269 31.925  12.170  1.00 36.65  ? 95  TRP B C   1 
ATOM   3007 O O   . TRP B 2 96  ? 11.860 32.002  13.332  1.00 37.04  ? 95  TRP B O   1 
ATOM   3008 C CB  . TRP B 2 96  ? 11.328 29.715  11.464  1.00 35.15  ? 95  TRP B CB  1 
ATOM   3009 C CG  . TRP B 2 96  ? 10.251 30.392  10.646  1.00 36.32  ? 95  TRP B CG  1 
ATOM   3010 C CD1 . TRP B 2 96  ? 10.431 31.069  9.480   1.00 36.64  ? 95  TRP B CD1 1 
ATOM   3011 C CD2 . TRP B 2 96  ? 8.847  30.472  10.945  1.00 37.60  ? 95  TRP B CD2 1 
ATOM   3012 N NE1 . TRP B 2 96  ? 9.232  31.563  9.027   1.00 36.28  ? 95  TRP B NE1 1 
ATOM   3013 C CE2 . TRP B 2 96  ? 8.242  31.210  9.905   1.00 37.29  ? 95  TRP B CE2 1 
ATOM   3014 C CE3 . TRP B 2 96  ? 8.043  29.995  11.991  1.00 39.73  ? 95  TRP B CE3 1 
ATOM   3015 C CZ2 . TRP B 2 96  ? 6.870  31.478  9.870   1.00 36.30  ? 95  TRP B CZ2 1 
ATOM   3016 C CZ3 . TRP B 2 96  ? 6.673  30.269  11.958  1.00 43.47  ? 95  TRP B CZ3 1 
ATOM   3017 C CH2 . TRP B 2 96  ? 6.105  31.005  10.899  1.00 39.13  ? 95  TRP B CH2 1 
ATOM   3018 N N   . ASP B 2 97  ? 12.434 32.991  11.388  1.00 41.79  ? 96  ASP B N   1 
ATOM   3019 C CA  . ASP B 2 97  ? 12.150 34.365  11.817  1.00 41.62  ? 96  ASP B CA  1 
ATOM   3020 C C   . ASP B 2 97  ? 11.073 34.926  10.894  1.00 40.86  ? 96  ASP B C   1 
ATOM   3021 O O   . ASP B 2 97  ? 11.376 35.396  9.795   1.00 45.74  ? 96  ASP B O   1 
ATOM   3022 C CB  . ASP B 2 97  ? 13.423 35.211  11.790  1.00 41.40  ? 96  ASP B CB  1 
ATOM   3023 C CG  . ASP B 2 97  ? 13.159 36.712  11.999  1.00 49.55  ? 96  ASP B CG  1 
ATOM   3024 O OD1 . ASP B 2 97  ? 12.050 37.098  12.428  1.00 45.90  ? 96  ASP B OD1 1 
ATOM   3025 O OD2 . ASP B 2 97  ? 14.087 37.512  11.738  1.00 49.71  ? 96  ASP B OD2 1 
ATOM   3026 N N   . ARG B 2 98  ? 9.819  34.914  11.350  1.00 39.57  ? 97  ARG B N   1 
ATOM   3027 C CA  . ARG B 2 98  ? 8.713  35.247  10.454  1.00 46.84  ? 97  ARG B CA  1 
ATOM   3028 C C   . ARG B 2 98  ? 8.663  36.734  10.084  1.00 51.38  ? 97  ARG B C   1 
ATOM   3029 O O   . ARG B 2 98  ? 8.105  37.088  9.038   1.00 49.14  ? 97  ARG B O   1 
ATOM   3030 C CB  . ARG B 2 98  ? 7.394  34.822  11.088  1.00 49.35  ? 97  ARG B CB  1 
ATOM   3031 C CG  . ARG B 2 98  ? 7.071  35.578  12.367  1.00 52.99  ? 97  ARG B CG  1 
ATOM   3032 C CD  . ARG B 2 98  ? 5.606  35.446  12.711  1.00 47.81  ? 97  ARG B CD  1 
ATOM   3033 N NE  . ARG B 2 98  ? 5.361  34.269  13.531  1.00 45.47  ? 97  ARG B NE  1 
ATOM   3034 C CZ  . ARG B 2 98  ? 4.172  33.687  13.662  1.00 52.39  ? 97  ARG B CZ  1 
ATOM   3035 N NH1 . ARG B 2 98  ? 3.119  34.168  13.005  1.00 51.32  ? 97  ARG B NH1 1 
ATOM   3036 N NH2 . ARG B 2 98  ? 4.034  32.618  14.440  1.00 43.72  ? 97  ARG B NH2 1 
ATOM   3037 N N   . ASP B 2 99  ? 9.210  37.619  10.918  1.00 49.05  ? 98  ASP B N   1 
ATOM   3038 C CA  . ASP B 2 99  ? 9.137  39.052  10.659  1.00 54.66  ? 98  ASP B CA  1 
ATOM   3039 C C   . ASP B 2 99  ? 10.352 39.590  9.904   1.00 57.04  ? 98  ASP B C   1 
ATOM   3040 O O   . ASP B 2 99  ? 10.615 40.798  9.956   1.00 56.55  ? 98  ASP B O   1 
ATOM   3041 C CB  . ASP B 2 99  ? 8.954  39.828  11.971  1.00 54.59  ? 98  ASP B CB  1 
ATOM   3042 C CG  . ASP B 2 99  ? 7.560  39.650  12.565  1.00 64.24  ? 98  ASP B CG  1 
ATOM   3043 O OD1 . ASP B 2 99  ? 6.561  39.794  11.813  1.00 61.96  ? 98  ASP B OD1 1 
ATOM   3044 O OD2 . ASP B 2 99  ? 7.466  39.361  13.782  1.00 62.03  ? 98  ASP B OD2 1 
ATOM   3045 N N   . MET B 2 100 ? 11.081 38.736  9.188   1.00 51.48  ? 99  MET B N   1 
ATOM   3046 C CA  . MET B 2 100 ? 12.320 39.164  8.551   1.00 49.77  ? 99  MET B CA  1 
ATOM   3047 C C   . MET B 2 100 ? 12.129 40.288  7.514   1.00 46.92  ? 99  MET B C   1 
ATOM   3048 O O   . MET B 2 100 ? 11.127 40.341  6.797   1.00 43.94  ? 99  MET B O   1 
ATOM   3049 C CB  . MET B 2 100 ? 13.010 37.968  7.896   1.00 49.45  ? 99  MET B CB  1 
ATOM   3050 C CG  . MET B 2 100 ? 14.411 38.304  7.427   1.00 53.47  ? 99  MET B CG  1 
ATOM   3051 S SD  . MET B 2 100 ? 15.258 36.911  6.691   1.00 58.17  ? 99  MET B SD  1 
ATOM   3052 C CE  . MET B 2 100 ? 15.503 35.921  8.163   1.00 49.93  ? 99  MET B CE  1 
ATOM   3053 N N   . ILE C 3 1   ? 12.157 15.229  -23.232 1.00 22.37  ? 1   ILE C N   1 
ATOM   3054 C CA  . ILE C 3 1   ? 12.611 13.945  -23.769 1.00 24.51  ? 1   ILE C CA  1 
ATOM   3055 C C   . ILE C 3 1   ? 14.135 13.923  -23.833 1.00 22.05  ? 1   ILE C C   1 
ATOM   3056 O O   . ILE C 3 1   ? 14.777 14.875  -24.276 1.00 23.99  ? 1   ILE C O   1 
ATOM   3057 C CB  . ILE C 3 1   ? 11.974 13.643  -25.161 1.00 23.02  ? 1   ILE C CB  1 
ATOM   3058 C CG1 . ILE C 3 1   ? 12.422 12.259  -25.665 1.00 28.38  ? 1   ILE C CG1 1 
ATOM   3059 C CG2 . ILE C 3 1   ? 12.318 14.730  -26.162 1.00 18.72  ? 1   ILE C CG2 1 
ATOM   3060 C CD1 . ILE C 3 1   ? 11.627 11.729  -26.860 1.00 27.24  ? 1   ILE C CD1 1 
ATOM   3061 N N   . LEU C 3 2   ? 14.702 12.816  -23.369 1.00 24.49  ? 2   LEU C N   1 
ATOM   3062 C CA  . LEU C 3 2   ? 16.144 12.684  -23.236 1.00 24.06  ? 2   LEU C CA  1 
ATOM   3063 C C   . LEU C 3 2   ? 16.821 12.605  -24.593 1.00 27.27  ? 2   LEU C C   1 
ATOM   3064 O O   . LEU C 3 2   ? 16.234 12.149  -25.578 1.00 27.56  ? 2   LEU C O   1 
ATOM   3065 C CB  . LEU C 3 2   ? 16.490 11.426  -22.437 1.00 23.39  ? 2   LEU C CB  1 
ATOM   3066 C CG  . LEU C 3 2   ? 16.318 11.539  -20.913 1.00 24.94  ? 2   LEU C CG  1 
ATOM   3067 C CD1 . LEU C 3 2   ? 16.462 10.167  -20.245 1.00 26.03  ? 2   LEU C CD1 1 
ATOM   3068 C CD2 . LEU C 3 2   ? 17.363 12.506  -20.389 1.00 19.78  ? 2   LEU C CD2 1 
ATOM   3069 N N   . ASP C 3 3   ? 18.070 13.070  -24.633 1.00 25.05  ? 3   ASP C N   1 
ATOM   3070 C CA  . ASP C 3 3   ? 18.973 12.733  -25.718 1.00 22.50  ? 3   ASP C CA  1 
ATOM   3071 C C   . ASP C 3 3   ? 19.378 11.259  -25.617 1.00 25.34  ? 3   ASP C C   1 
ATOM   3072 O O   . ASP C 3 3   ? 19.294 10.632  -24.562 1.00 22.33  ? 3   ASP C O   1 
ATOM   3073 C CB  . ASP C 3 3   ? 20.198 13.649  -25.681 1.00 22.96  ? 3   ASP C CB  1 
ATOM   3074 C CG  . ASP C 3 3   ? 21.092 13.500  -26.886 1.00 25.67  ? 3   ASP C CG  1 
ATOM   3075 O OD1 . ASP C 3 3   ? 20.707 12.778  -27.830 1.00 30.14  ? 3   ASP C OD1 1 
ATOM   3076 O OD2 . ASP C 3 3   ? 22.197 14.101  -26.898 1.00 26.99  ? 3   ASP C OD2 1 
ATOM   3077 N N   . THR C 3 4   ? 19.792 10.702  -26.748 1.00 26.56  ? 4   THR C N   1 
ATOM   3078 C CA  . THR C 3 4   ? 20.209 9.311   -26.800 1.00 26.59  ? 4   THR C CA  1 
ATOM   3079 C C   . THR C 3 4   ? 21.652 9.212   -26.348 1.00 24.79  ? 4   THR C C   1 
ATOM   3080 O O   . THR C 3 4   ? 22.496 9.993   -26.793 1.00 25.09  ? 4   THR C O   1 
ATOM   3081 C CB  . THR C 3 4   ? 20.052 8.763   -28.221 1.00 28.89  ? 4   THR C CB  1 
ATOM   3082 O OG1 . THR C 3 4   ? 18.674 8.861   -28.607 1.00 28.64  ? 4   THR C OG1 1 
ATOM   3083 C CG2 . THR C 3 4   ? 20.481 7.306   -28.279 1.00 28.12  ? 4   THR C CG2 1 
ATOM   3084 N N   . ALA C 3 5   ? 21.925 8.283   -25.432 1.00 25.36  ? 5   ALA C N   1 
ATOM   3085 C CA  . ALA C 3 5   ? 23.298 8.062   -24.982 1.00 25.13  ? 5   ALA C CA  1 
ATOM   3086 C C   . ALA C 3 5   ? 24.179 7.678   -26.165 1.00 29.63  ? 5   ALA C C   1 
ATOM   3087 O O   . ALA C 3 5   ? 23.803 6.831   -26.981 1.00 31.83  ? 5   ALA C O   1 
ATOM   3088 C CB  . ALA C 3 5   ? 23.338 6.968   -23.918 1.00 23.67  ? 5   ALA C CB  1 
ATOM   3089 N N   . GLY C 3 6   ? 25.341 8.318   -26.277 1.00 26.06  ? 6   GLY C N   1 
ATOM   3090 C CA  . GLY C 3 6   ? 26.233 8.023   -27.383 1.00 25.40  ? 6   GLY C CA  1 
ATOM   3091 C C   . GLY C 3 6   ? 27.221 9.128   -27.704 1.00 29.90  ? 6   GLY C C   1 
ATOM   3092 O O   . GLY C 3 6   ? 26.897 10.315  -27.595 1.00 29.82  ? 6   GLY C O   1 
ATOM   3093 N N   . ARG C 3 7   ? 28.433 8.743   -28.095 1.00 24.48  ? 7   ARG C N   1 
ATOM   3094 C CA  . ARG C 3 7   ? 29.486 9.693   -28.439 1.00 26.83  ? 7   ARG C CA  1 
ATOM   3095 C C   . ARG C 3 7   ? 29.730 10.681  -27.295 1.00 30.26  ? 7   ARG C C   1 
ATOM   3096 O O   . ARG C 3 7   ? 29.811 11.899  -27.489 1.00 26.50  ? 7   ARG C O   1 
ATOM   3097 C CB  . ARG C 3 7   ? 29.151 10.414  -29.753 1.00 27.95  ? 7   ARG C CB  1 
ATOM   3098 C CG  . ARG C 3 7   ? 29.342 9.524   -30.988 1.00 30.32  ? 7   ARG C CG  1 
ATOM   3099 C CD  . ARG C 3 7   ? 28.781 10.116  -32.305 1.00 28.33  ? 7   ARG C CD  1 
ATOM   3100 N NE  . ARG C 3 7   ? 29.469 9.567   -33.481 1.00 28.85  ? 7   ARG C NE  1 
ATOM   3101 C CZ  . ARG C 3 7   ? 28.880 9.266   -34.646 1.00 32.80  ? 7   ARG C CZ  1 
ATOM   3102 N NH1 . ARG C 3 7   ? 27.574 9.455   -34.819 1.00 26.16  ? 7   ARG C NH1 1 
ATOM   3103 N NH2 . ARG C 3 7   ? 29.601 8.768   -35.647 1.00 27.82  ? 7   ARG C NH2 1 
ATOM   3104 N N   . GLU C 3 8   ? 29.844 10.145  -26.070 1.00 32.91  ? 8   GLU C N   1 
ATOM   3105 C CA  . GLU C 3 8   ? 30.111 11.018  -24.936 1.00 29.06  ? 8   GLU C CA  1 
ATOM   3106 C C   . GLU C 3 8   ? 31.067 10.382  -23.932 1.00 31.31  ? 8   GLU C C   1 
ATOM   3107 O O   . GLU C 3 8   ? 31.034 10.718  -22.739 1.00 25.26  ? 8   GLU C O   1 
ATOM   3108 C CB  . GLU C 3 8   ? 28.809 11.446  -24.249 1.00 28.59  ? 8   GLU C CB  1 
ATOM   3109 C CG  . GLU C 3 8   ? 27.883 10.334  -23.824 1.00 27.75  ? 8   GLU C CG  1 
ATOM   3110 C CD  . GLU C 3 8   ? 26.417 10.803  -23.700 1.00 33.58  ? 8   GLU C CD  1 
ATOM   3111 O OE1 . GLU C 3 8   ? 26.149 11.816  -23.010 1.00 31.00  ? 8   GLU C OE1 1 
ATOM   3112 O OE2 . GLU C 3 8   ? 25.529 10.155  -24.304 1.00 39.89  ? 8   GLU C OE2 1 
ATOM   3113 N N   . GLU C 3 9   ? 31.944 9.495   -24.393 1.00 24.57  ? 9   GLU C N   1 
ATOM   3114 C CA  . GLU C 3 9   ? 32.949 8.931   -23.505 1.00 30.50  ? 9   GLU C CA  1 
ATOM   3115 C C   . GLU C 3 9   ? 34.116 9.899   -23.362 1.00 26.39  ? 9   GLU C C   1 
ATOM   3116 O O   . GLU C 3 9   ? 34.585 10.474  -24.352 1.00 24.13  ? 9   GLU C O   1 
ATOM   3117 C CB  . GLU C 3 9   ? 33.427 7.580   -24.033 1.00 30.04  ? 9   GLU C CB  1 
ATOM   3118 C CG  . GLU C 3 9   ? 32.329 6.527   -23.993 1.00 34.51  ? 9   GLU C CG  1 
ATOM   3119 C CD  . GLU C 3 9   ? 32.768 5.189   -24.541 1.00 39.68  ? 9   GLU C CD  1 
ATOM   3120 O OE1 . GLU C 3 9   ? 31.881 4.363   -24.843 1.00 49.45  ? 9   GLU C OE1 1 
ATOM   3121 O OE2 . GLU C 3 9   ? 33.994 4.962   -24.672 1.00 46.24  ? 9   GLU C OE2 1 
ATOM   3122 N N   . TYR C 3 10  ? 34.573 10.096  -22.124 1.00 21.57  ? 10  TYR C N   1 
ATOM   3123 C CA  . TYR C 3 10  ? 35.688 11.024  -21.873 1.00 24.20  ? 10  TYR C CA  1 
ATOM   3124 C C   . TYR C 3 10  ? 37.022 10.374  -22.258 1.00 29.15  ? 10  TYR C C   1 
ATOM   3125 O O   . TYR C 3 10  ? 38.039 11.045  -22.428 1.00 27.07  ? 10  TYR C O   1 
ATOM   3126 C CB  . TYR C 3 10  ? 35.735 11.477  -20.396 1.00 26.07  ? 10  TYR C CB  1 
ATOM   3127 C CG  . TYR C 3 10  ? 34.528 12.283  -19.936 1.00 23.39  ? 10  TYR C CG  1 
ATOM   3128 C CD1 . TYR C 3 10  ? 33.670 12.878  -20.858 1.00 25.53  ? 10  TYR C CD1 1 
ATOM   3129 C CD2 . TYR C 3 10  ? 34.258 12.454  -18.598 1.00 22.34  ? 10  TYR C CD2 1 
ATOM   3130 C CE1 . TYR C 3 10  ? 32.574 13.603  -20.457 1.00 21.96  ? 10  TYR C CE1 1 
ATOM   3131 C CE2 . TYR C 3 10  ? 33.158 13.191  -18.175 1.00 23.37  ? 10  TYR C CE2 1 
ATOM   3132 C CZ  . TYR C 3 10  ? 32.317 13.759  -19.113 1.00 25.71  ? 10  TYR C CZ  1 
ATOM   3133 O OH  . TYR C 3 10  ? 31.216 14.478  -18.705 1.00 21.92  ? 10  TYR C OH  1 
ATOM   3134 O OXT . TYR C 3 10  ? 37.129 9.146   -22.391 1.00 31.49  ? 10  TYR C OXT 1 
ATOM   3135 N N   . ALA D 4 3   ? 35.479 -2.841  -43.126 1.00 56.27  ? 2   ALA E N   1 
ATOM   3136 C CA  . ALA D 4 3   ? 34.322 -2.436  -42.339 1.00 48.78  ? 2   ALA E CA  1 
ATOM   3137 C C   . ALA D 4 3   ? 33.184 -3.448  -42.495 1.00 48.86  ? 2   ALA E C   1 
ATOM   3138 O O   . ALA D 4 3   ? 32.419 -3.372  -43.459 1.00 46.56  ? 2   ALA E O   1 
ATOM   3139 C CB  . ALA D 4 3   ? 33.861 -1.055  -42.758 1.00 45.21  ? 2   ALA E CB  1 
ATOM   3140 N N   . GLN D 4 4   ? 33.053 -4.380  -41.547 1.00 42.93  ? 3   GLN E N   1 
ATOM   3141 C CA  . GLN D 4 4   ? 32.108 -5.475  -41.715 1.00 42.33  ? 3   GLN E CA  1 
ATOM   3142 C C   . GLN D 4 4   ? 31.635 -6.027  -40.375 1.00 31.77  ? 3   GLN E C   1 
ATOM   3143 O O   . GLN D 4 4   ? 32.347 -5.966  -39.371 1.00 28.96  ? 3   GLN E O   1 
ATOM   3144 C CB  . GLN D 4 4   ? 32.740 -6.604  -42.521 1.00 46.09  ? 3   GLN E CB  1 
ATOM   3145 C CG  . GLN D 4 4   ? 32.167 -6.797  -43.896 1.00 54.34  ? 3   GLN E CG  1 
ATOM   3146 C CD  . GLN D 4 4   ? 32.829 -7.971  -44.583 1.00 61.33  ? 3   GLN E CD  1 
ATOM   3147 O OE1 . GLN D 4 4   ? 33.859 -8.467  -44.110 1.00 57.42  ? 3   GLN E OE1 1 
ATOM   3148 N NE2 . GLN D 4 4   ? 32.240 -8.435  -45.686 1.00 57.49  ? 3   GLN E NE2 1 
ATOM   3149 N N   . VAL D 4 5   ? 30.436 -6.610  -40.393 1.00 32.85  ? 4   VAL E N   1 
ATOM   3150 C CA  . VAL D 4 5   ? 29.884 -7.377  -39.277 1.00 30.92  ? 4   VAL E CA  1 
ATOM   3151 C C   . VAL D 4 5   ? 30.040 -8.860  -39.595 1.00 26.60  ? 4   VAL E C   1 
ATOM   3152 O O   . VAL D 4 5   ? 29.564 -9.327  -40.628 1.00 22.28  ? 4   VAL E O   1 
ATOM   3153 C CB  . VAL D 4 5   ? 28.399 -7.035  -39.052 1.00 28.28  ? 4   VAL E CB  1 
ATOM   3154 C CG1 . VAL D 4 5   ? 27.792 -7.937  -37.972 1.00 21.97  ? 4   VAL E CG1 1 
ATOM   3155 C CG2 . VAL D 4 5   ? 28.213 -5.555  -38.737 1.00 27.45  ? 4   VAL E CG2 1 
ATOM   3156 N N   . THR D 4 6   ? 30.648 -9.614  -38.692 1.00 23.75  ? 5   THR E N   1 
ATOM   3157 C CA  . THR D 4 6   ? 30.874 -11.039 -38.906 1.00 28.62  ? 5   THR E CA  1 
ATOM   3158 C C   . THR D 4 6   ? 29.986 -11.857 -37.970 1.00 28.04  ? 5   THR E C   1 
ATOM   3159 O O   . THR D 4 6   ? 29.875 -11.540 -36.783 1.00 27.05  ? 5   THR E O   1 
ATOM   3160 C CB  . THR D 4 6   ? 32.355 -11.386 -38.670 1.00 30.36  ? 5   THR E CB  1 
ATOM   3161 O OG1 . THR D 4 6   ? 33.179 -10.625 -39.568 1.00 30.45  ? 5   THR E OG1 1 
ATOM   3162 C CG2 . THR D 4 6   ? 32.617 -12.889 -38.845 1.00 28.82  ? 5   THR E CG2 1 
ATOM   3163 N N   . GLN D 4 7   ? 29.356 -12.904 -38.504 1.00 21.48  ? 6   GLN E N   1 
ATOM   3164 C CA  . GLN D 4 7   ? 28.611 -13.872 -37.708 1.00 24.05  ? 6   GLN E CA  1 
ATOM   3165 C C   . GLN D 4 7   ? 29.238 -15.254 -37.878 1.00 24.39  ? 6   GLN E C   1 
ATOM   3166 O O   . GLN D 4 7   ? 29.660 -15.620 -38.973 1.00 29.91  ? 6   GLN E O   1 
ATOM   3167 C CB  . GLN D 4 7   ? 27.122 -13.906 -38.110 1.00 23.69  ? 6   GLN E CB  1 
ATOM   3168 C CG  . GLN D 4 7   ? 26.442 -12.511 -38.126 1.00 22.36  ? 6   GLN E CG  1 
ATOM   3169 C CD  . GLN D 4 7   ? 24.953 -12.530 -38.453 1.00 20.45  ? 6   GLN E CD  1 
ATOM   3170 O OE1 . GLN D 4 7   ? 24.403 -11.502 -38.811 1.00 22.74  ? 6   GLN E OE1 1 
ATOM   3171 N NE2 . GLN D 4 7   ? 24.298 -13.692 -38.332 1.00 20.87  ? 6   GLN E NE2 1 
ATOM   3172 N N   . ASN D 4 8   ? 29.318 -16.014 -36.798 1.00 24.29  ? 7   ASN E N   1 
ATOM   3173 C CA  . ASN D 4 8   ? 29.867 -17.363 -36.883 1.00 28.43  ? 7   ASN E CA  1 
ATOM   3174 C C   . ASN D 4 8   ? 29.031 -18.249 -35.969 1.00 27.17  ? 7   ASN E C   1 
ATOM   3175 O O   . ASN D 4 8   ? 28.967 -18.001 -34.763 1.00 23.99  ? 7   ASN E O   1 
ATOM   3176 C CB  . ASN D 4 8   ? 31.359 -17.381 -36.492 1.00 24.96  ? 7   ASN E CB  1 
ATOM   3177 C CG  . ASN D 4 8   ? 32.014 -18.771 -36.632 1.00 29.23  ? 7   ASN E CG  1 
ATOM   3178 O OD1 . ASN D 4 8   ? 31.372 -19.812 -36.458 1.00 37.53  ? 7   ASN E OD1 1 
ATOM   3179 N ND2 . ASN D 4 8   ? 33.307 -18.782 -36.908 1.00 24.77  ? 7   ASN E ND2 1 
ATOM   3180 N N   . PRO D 4 9   ? 28.393 -19.305 -36.490 1.00 27.85  ? 8   PRO E N   1 
ATOM   3181 C CA  . PRO D 4 9   ? 28.464 -19.804 -37.863 1.00 25.22  ? 8   PRO E CA  1 
ATOM   3182 C C   . PRO D 4 9   ? 27.444 -19.168 -38.793 1.00 27.77  ? 8   PRO E C   1 
ATOM   3183 O O   . PRO D 4 9   ? 26.438 -18.634 -38.324 1.00 26.76  ? 8   PRO E O   1 
ATOM   3184 C CB  . PRO D 4 9   ? 28.164 -21.292 -37.692 1.00 24.48  ? 8   PRO E CB  1 
ATOM   3185 C CG  . PRO D 4 9   ? 27.196 -21.307 -36.589 1.00 28.78  ? 8   PRO E CG  1 
ATOM   3186 C CD  . PRO D 4 9   ? 27.603 -20.205 -35.634 1.00 21.95  ? 8   PRO E CD  1 
ATOM   3187 N N   . ARG D 4 10  ? 27.707 -19.212 -40.099 1.00 22.55  ? 9   ARG E N   1 
ATOM   3188 C CA  . ARG D 4 10  ? 26.708 -18.780 -41.058 1.00 23.50  ? 9   ARG E CA  1 
ATOM   3189 C C   . ARG D 4 10  ? 25.609 -19.822 -41.241 1.00 24.72  ? 9   ARG E C   1 
ATOM   3190 O O   . ARG D 4 10  ? 24.476 -19.455 -41.578 1.00 25.40  ? 9   ARG E O   1 
ATOM   3191 C CB  . ARG D 4 10  ? 27.374 -18.453 -42.397 1.00 26.07  ? 9   ARG E CB  1 
ATOM   3192 C CG  . ARG D 4 10  ? 28.174 -17.123 -42.438 1.00 29.69  ? 9   ARG E CG  1 
ATOM   3193 C CD  . ARG D 4 10  ? 28.444 -16.665 -43.920 1.00 26.94  ? 9   ARG E CD  1 
ATOM   3194 N NE  . ARG D 4 10  ? 28.976 -17.787 -44.704 1.00 36.10  ? 9   ARG E NE  1 
ATOM   3195 C CZ  . ARG D 4 10  ? 28.481 -18.224 -45.867 1.00 37.25  ? 9   ARG E CZ  1 
ATOM   3196 N NH1 . ARG D 4 10  ? 27.420 -17.644 -46.436 1.00 33.49  ? 9   ARG E NH1 1 
ATOM   3197 N NH2 . ARG D 4 10  ? 29.044 -19.268 -46.461 1.00 39.71  ? 9   ARG E NH2 1 
ATOM   3198 N N   . TYR D 4 11  ? 25.909 -21.100 -40.996 1.00 22.56  ? 10  TYR E N   1 
ATOM   3199 C CA  . TYR D 4 11  ? 24.942 -22.188 -41.096 1.00 22.52  ? 10  TYR E CA  1 
ATOM   3200 C C   . TYR D 4 11  ? 25.152 -23.134 -39.928 1.00 23.84  ? 10  TYR E C   1 
ATOM   3201 O O   . TYR D 4 11  ? 26.289 -23.426 -39.560 1.00 25.68  ? 10  TYR E O   1 
ATOM   3202 C CB  . TYR D 4 11  ? 25.083 -22.982 -42.417 1.00 23.65  ? 10  TYR E CB  1 
ATOM   3203 C CG  . TYR D 4 11  ? 24.788 -22.175 -43.667 1.00 22.34  ? 10  TYR E CG  1 
ATOM   3204 C CD1 . TYR D 4 11  ? 25.800 -21.458 -44.300 1.00 22.57  ? 10  TYR E CD1 1 
ATOM   3205 C CD2 . TYR D 4 11  ? 23.502 -22.138 -44.216 1.00 23.67  ? 10  TYR E CD2 1 
ATOM   3206 C CE1 . TYR D 4 11  ? 25.556 -20.713 -45.432 1.00 25.41  ? 10  TYR E CE1 1 
ATOM   3207 C CE2 . TYR D 4 11  ? 23.242 -21.407 -45.390 1.00 31.35  ? 10  TYR E CE2 1 
ATOM   3208 C CZ  . TYR D 4 11  ? 24.275 -20.673 -45.976 1.00 31.67  ? 10  TYR E CZ  1 
ATOM   3209 O OH  . TYR D 4 11  ? 24.057 -19.925 -47.119 1.00 37.34  ? 10  TYR E OH  1 
ATOM   3210 N N   . LEU D 4 12  ? 24.062 -23.609 -39.342 1.00 25.06  ? 11  LEU E N   1 
ATOM   3211 C CA  . LEU D 4 12  ? 24.195 -24.502 -38.205 1.00 27.59  ? 11  LEU E CA  1 
ATOM   3212 C C   . LEU D 4 12  ? 22.982 -25.408 -38.143 1.00 25.11  ? 11  LEU E C   1 
ATOM   3213 O O   . LEU D 4 12  ? 21.844 -24.931 -38.141 1.00 28.44  ? 11  LEU E O   1 
ATOM   3214 C CB  . LEU D 4 12  ? 24.357 -23.712 -36.901 1.00 26.88  ? 11  LEU E CB  1 
ATOM   3215 C CG  . LEU D 4 12  ? 24.394 -24.487 -35.576 1.00 29.32  ? 11  LEU E CG  1 
ATOM   3216 C CD1 . LEU D 4 12  ? 25.349 -25.677 -35.605 1.00 31.41  ? 11  LEU E CD1 1 
ATOM   3217 C CD2 . LEU D 4 12  ? 24.756 -23.531 -34.439 1.00 31.44  ? 11  LEU E CD2 1 
ATOM   3218 N N   . ILE D 4 13  ? 23.239 -26.710 -38.102 1.00 25.94  ? 12  ILE E N   1 
ATOM   3219 C CA  . ILE D 4 13  ? 22.224 -27.727 -37.872 1.00 28.74  ? 12  ILE E CA  1 
ATOM   3220 C C   . ILE D 4 13  ? 22.514 -28.360 -36.522 1.00 26.01  ? 12  ILE E C   1 
ATOM   3221 O O   . ILE D 4 13  ? 23.590 -28.937 -36.318 1.00 23.56  ? 12  ILE E O   1 
ATOM   3222 C CB  . ILE D 4 13  ? 22.223 -28.804 -38.964 1.00 26.62  ? 12  ILE E CB  1 
ATOM   3223 C CG1 . ILE D 4 13  ? 22.142 -28.182 -40.351 1.00 23.51  ? 12  ILE E CG1 1 
ATOM   3224 C CG2 . ILE D 4 13  ? 21.069 -29.764 -38.735 1.00 24.35  ? 12  ILE E CG2 1 
ATOM   3225 C CD1 . ILE D 4 13  ? 22.514 -29.175 -41.436 1.00 24.25  ? 12  ILE E CD1 1 
ATOM   3226 N N   . THR D 4 14  ? 21.549 -28.299 -35.616 1.00 25.82  ? 13  THR E N   1 
ATOM   3227 C CA  . THR D 4 14  ? 21.792 -28.803 -34.280 1.00 23.41  ? 13  THR E CA  1 
ATOM   3228 C C   . THR D 4 14  ? 20.543 -29.497 -33.754 1.00 29.49  ? 13  THR E C   1 
ATOM   3229 O O   . THR D 4 14  ? 19.433 -29.329 -34.274 1.00 28.28  ? 13  THR E O   1 
ATOM   3230 C CB  . THR D 4 14  ? 22.239 -27.669 -33.356 1.00 27.67  ? 13  THR E CB  1 
ATOM   3231 O OG1 . THR D 4 14  ? 22.685 -28.209 -32.112 1.00 38.68  ? 13  THR E OG1 1 
ATOM   3232 C CG2 . THR D 4 14  ? 21.077 -26.707 -33.106 1.00 25.46  ? 13  THR E CG2 1 
ATOM   3233 N N   . VAL D 4 15  ? 20.741 -30.297 -32.717 1.00 25.63  ? 14  VAL E N   1 
ATOM   3234 C CA  . VAL D 4 15  ? 19.664 -31.085 -32.163 1.00 27.87  ? 14  VAL E CA  1 
ATOM   3235 C C   . VAL D 4 15  ? 19.062 -30.321 -30.993 1.00 31.18  ? 14  VAL E C   1 
ATOM   3236 O O   . VAL D 4 15  ? 19.748 -29.578 -30.273 1.00 32.90  ? 14  VAL E O   1 
ATOM   3237 C CB  . VAL D 4 15  ? 20.140 -32.497 -31.741 1.00 36.77  ? 14  VAL E CB  1 
ATOM   3238 C CG1 . VAL D 4 15  ? 20.983 -33.130 -32.839 1.00 27.32  ? 14  VAL E CG1 1 
ATOM   3239 C CG2 . VAL D 4 15  ? 20.899 -32.446 -30.429 1.00 32.09  ? 14  VAL E CG2 1 
ATOM   3240 N N   . THR D 4 16  ? 17.754 -30.494 -30.828 1.00 28.78  ? 15  THR E N   1 
ATOM   3241 C CA  . THR D 4 16  ? 16.991 -29.941 -29.720 1.00 29.53  ? 15  THR E CA  1 
ATOM   3242 C C   . THR D 4 16  ? 17.729 -30.078 -28.396 1.00 34.20  ? 15  THR E C   1 
ATOM   3243 O O   . THR D 4 16  ? 18.183 -31.168 -28.030 1.00 30.38  ? 15  THR E O   1 
ATOM   3244 C CB  . THR D 4 16  ? 15.651 -30.662 -29.643 1.00 27.95  ? 15  THR E CB  1 
ATOM   3245 O OG1 . THR D 4 16  ? 14.968 -30.488 -30.887 1.00 32.18  ? 15  THR E OG1 1 
ATOM   3246 C CG2 . THR D 4 16  ? 14.803 -30.121 -28.487 1.00 28.31  ? 15  THR E CG2 1 
ATOM   3247 N N   . GLY D 4 17  ? 17.863 -28.952 -27.693 1.00 27.93  ? 16  GLY E N   1 
ATOM   3248 C CA  . GLY D 4 17  ? 18.324 -28.944 -26.328 1.00 28.75  ? 16  GLY E CA  1 
ATOM   3249 C C   . GLY D 4 17  ? 19.818 -28.862 -26.137 1.00 28.73  ? 16  GLY E C   1 
ATOM   3250 O O   . GLY D 4 17  ? 20.273 -28.858 -24.989 1.00 30.27  ? 16  GLY E O   1 
ATOM   3251 N N   . LYS D 4 18  ? 20.603 -28.803 -27.204 1.00 26.51  ? 17  LYS E N   1 
ATOM   3252 C CA  . LYS D 4 18  ? 22.055 -28.741 -27.080 1.00 27.77  ? 17  LYS E CA  1 
ATOM   3253 C C   . LYS D 4 18  ? 22.499 -27.281 -27.132 1.00 29.60  ? 17  LYS E C   1 
ATOM   3254 O O   . LYS D 4 18  ? 22.313 -26.604 -28.153 1.00 24.10  ? 17  LYS E O   1 
ATOM   3255 C CB  . LYS D 4 18  ? 22.733 -29.565 -28.171 1.00 30.15  ? 17  LYS E CB  1 
ATOM   3256 C CG  . LYS D 4 18  ? 24.247 -29.438 -28.154 1.00 40.74  ? 17  LYS E CG  1 
ATOM   3257 C CD  . LYS D 4 18  ? 24.929 -30.654 -28.761 1.00 48.84  ? 17  LYS E CD  1 
ATOM   3258 C CE  . LYS D 4 18  ? 26.061 -30.235 -29.703 1.00 44.87  ? 17  LYS E CE  1 
ATOM   3259 N NZ  . LYS D 4 18  ? 27.398 -30.325 -29.037 1.00 53.36  ? 17  LYS E NZ  1 
ATOM   3260 N N   . LYS D 4 19  ? 23.077 -26.799 -26.031 1.00 26.39  ? 18  LYS E N   1 
ATOM   3261 C CA  . LYS D 4 19  ? 23.385 -25.381 -25.906 1.00 27.63  ? 18  LYS E CA  1 
ATOM   3262 C C   . LYS D 4 19  ? 24.237 -24.906 -27.076 1.00 27.99  ? 18  LYS E C   1 
ATOM   3263 O O   . LYS D 4 19  ? 25.113 -25.627 -27.560 1.00 30.14  ? 18  LYS E O   1 
ATOM   3264 C CB  . LYS D 4 19  ? 24.115 -25.107 -24.588 1.00 25.99  ? 18  LYS E CB  1 
ATOM   3265 C CG  . LYS D 4 19  ? 24.608 -23.671 -24.447 1.00 29.55  ? 18  LYS E CG  1 
ATOM   3266 C CD  . LYS D 4 19  ? 24.448 -23.179 -23.023 1.00 34.46  ? 18  LYS E CD  1 
ATOM   3267 C CE  . LYS D 4 19  ? 25.437 -22.097 -22.687 1.00 30.31  ? 18  LYS E CE  1 
ATOM   3268 N NZ  . LYS D 4 19  ? 25.642 -22.025 -21.212 1.00 49.45  ? 18  LYS E NZ  1 
ATOM   3269 N N   . LEU D 4 20  ? 23.981 -23.687 -27.542 1.00 24.44  ? 19  LEU E N   1 
ATOM   3270 C CA  . LEU D 4 20  ? 24.851 -23.141 -28.572 1.00 25.36  ? 19  LEU E CA  1 
ATOM   3271 C C   . LEU D 4 20  ? 24.950 -21.631 -28.428 1.00 23.54  ? 19  LEU E C   1 
ATOM   3272 O O   . LEU D 4 20  ? 24.082 -20.982 -27.846 1.00 27.35  ? 19  LEU E O   1 
ATOM   3273 C CB  . LEU D 4 20  ? 24.370 -23.520 -29.975 1.00 25.02  ? 19  LEU E CB  1 
ATOM   3274 C CG  . LEU D 4 20  ? 23.047 -22.927 -30.459 1.00 26.31  ? 19  LEU E CG  1 
ATOM   3275 C CD1 . LEU D 4 20  ? 23.246 -21.591 -31.175 1.00 23.17  ? 19  LEU E CD1 1 
ATOM   3276 C CD2 . LEU D 4 20  ? 22.389 -23.944 -31.398 1.00 25.57  ? 19  LEU E CD2 1 
ATOM   3277 N N   . THR D 4 21  ? 26.015 -21.080 -29.002 1.00 26.33  ? 20  THR E N   1 
ATOM   3278 C CA  . THR D 4 21  ? 26.241 -19.643 -29.073 1.00 25.04  ? 20  THR E CA  1 
ATOM   3279 C C   . THR D 4 21  ? 26.567 -19.273 -30.511 1.00 23.89  ? 20  THR E C   1 
ATOM   3280 O O   . THR D 4 21  ? 27.350 -19.967 -31.166 1.00 25.07  ? 20  THR E O   1 
ATOM   3281 C CB  . THR D 4 21  ? 27.386 -19.227 -28.140 1.00 24.21  ? 20  THR E CB  1 
ATOM   3282 O OG1 . THR D 4 21  ? 26.987 -19.448 -26.777 1.00 28.04  ? 20  THR E OG1 1 
ATOM   3283 C CG2 . THR D 4 21  ? 27.746 -17.759 -28.351 1.00 24.43  ? 20  THR E CG2 1 
ATOM   3284 N N   . VAL D 4 22  ? 25.956 -18.197 -31.003 1.00 22.12  ? 21  VAL E N   1 
ATOM   3285 C CA  . VAL D 4 22  ? 26.280 -17.617 -32.301 1.00 21.71  ? 21  VAL E CA  1 
ATOM   3286 C C   . VAL D 4 22  ? 27.000 -16.298 -32.031 1.00 25.41  ? 21  VAL E C   1 
ATOM   3287 O O   . VAL D 4 22  ? 26.474 -15.442 -31.305 1.00 24.54  ? 21  VAL E O   1 
ATOM   3288 C CB  . VAL D 4 22  ? 25.016 -17.412 -33.157 1.00 26.78  ? 21  VAL E CB  1 
ATOM   3289 C CG1 . VAL D 4 22  ? 25.376 -16.896 -34.542 1.00 24.31  ? 21  VAL E CG1 1 
ATOM   3290 C CG2 . VAL D 4 22  ? 24.236 -18.720 -33.280 1.00 23.16  ? 21  VAL E CG2 1 
ATOM   3291 N N   . THR D 4 23  ? 28.226 -16.149 -32.553 1.00 21.19  ? 22  THR E N   1 
ATOM   3292 C CA  . THR D 4 23  ? 28.994 -14.946 -32.283 1.00 17.80  ? 22  THR E CA  1 
ATOM   3293 C C   . THR D 4 23  ? 28.730 -13.901 -33.346 1.00 23.71  ? 22  THR E C   1 
ATOM   3294 O O   . THR D 4 23  ? 28.420 -14.218 -34.501 1.00 25.20  ? 22  THR E O   1 
ATOM   3295 C CB  . THR D 4 23  ? 30.507 -15.192 -32.202 1.00 22.94  ? 22  THR E CB  1 
ATOM   3296 O OG1 . THR D 4 23  ? 30.997 -15.725 -33.432 1.00 24.89  ? 22  THR E OG1 1 
ATOM   3297 C CG2 . THR D 4 23  ? 30.879 -16.109 -31.023 1.00 17.64  ? 22  THR E CG2 1 
ATOM   3298 N N   . CYS D 4 24  ? 28.855 -12.644 -32.928 1.00 21.78  ? 23  CYS E N   1 
ATOM   3299 C CA  . CYS D 4 24  ? 28.724 -11.488 -33.787 1.00 24.94  ? 23  CYS E CA  1 
ATOM   3300 C C   . CYS D 4 24  ? 29.834 -10.531 -33.404 1.00 26.08  ? 23  CYS E C   1 
ATOM   3301 O O   . CYS D 4 24  ? 29.977 -10.196 -32.228 1.00 22.88  ? 23  CYS E O   1 
ATOM   3302 C CB  . CYS D 4 24  ? 27.376 -10.781 -33.611 1.00 21.50  ? 23  CYS E CB  1 
ATOM   3303 S SG  . CYS D 4 24  ? 27.305 -9.348  -34.704 1.00 25.06  ? 23  CYS E SG  1 
ATOM   3304 N N   . SER D 4 25  ? 30.592 -10.060 -34.382 1.00 25.11  ? 24  SER E N   1 
ATOM   3305 C CA  . SER D 4 25  ? 31.630 -9.109  -34.044 1.00 26.69  ? 24  SER E CA  1 
ATOM   3306 C C   . SER D 4 25  ? 31.762 -8.085  -35.157 1.00 27.16  ? 24  SER E C   1 
ATOM   3307 O O   . SER D 4 25  ? 31.360 -8.323  -36.298 1.00 28.13  ? 24  SER E O   1 
ATOM   3308 C CB  . SER D 4 25  ? 32.960 -9.820  -33.776 1.00 30.99  ? 24  SER E CB  1 
ATOM   3309 O OG  . SER D 4 25  ? 33.457 -10.408 -34.956 1.00 32.70  ? 24  SER E OG  1 
ATOM   3310 N N   . GLN D 4 26  ? 32.300 -6.921  -34.792 1.00 25.13  ? 25  GLN E N   1 
ATOM   3311 C CA  . GLN D 4 26  ? 32.646 -5.868  -35.734 1.00 28.07  ? 25  GLN E CA  1 
ATOM   3312 C C   . GLN D 4 26  ? 33.837 -5.135  -35.149 1.00 29.79  ? 25  GLN E C   1 
ATOM   3313 O O   . GLN D 4 26  ? 33.954 -5.000  -33.929 1.00 26.16  ? 25  GLN E O   1 
ATOM   3314 C CB  . GLN D 4 26  ? 31.488 -4.896  -35.985 1.00 22.52  ? 25  GLN E CB  1 
ATOM   3315 C CG  . GLN D 4 26  ? 30.759 -4.436  -34.711 1.00 23.01  ? 25  GLN E CG  1 
ATOM   3316 C CD  . GLN D 4 26  ? 31.488 -3.318  -33.972 1.00 25.55  ? 25  GLN E CD  1 
ATOM   3317 O OE1 . GLN D 4 26  ? 32.223 -2.524  -34.579 1.00 24.58  ? 25  GLN E OE1 1 
ATOM   3318 N NE2 . GLN D 4 26  ? 31.308 -3.269  -32.650 1.00 20.79  ? 25  GLN E NE2 1 
ATOM   3319 N N   . ASN D 4 27  ? 34.732 -4.682  -36.014 1.00 29.42  ? 26  ASN E N   1 
ATOM   3320 C CA  . ASN D 4 27  ? 35.922 -3.974  -35.567 1.00 33.32  ? 26  ASN E CA  1 
ATOM   3321 C C   . ASN D 4 27  ? 35.865 -2.512  -35.984 1.00 35.31  ? 26  ASN E C   1 
ATOM   3322 O O   . ASN D 4 27  ? 36.865 -1.925  -36.389 1.00 39.73  ? 26  ASN E O   1 
ATOM   3323 C CB  . ASN D 4 27  ? 37.188 -4.646  -36.091 1.00 38.01  ? 26  ASN E CB  1 
ATOM   3324 C CG  . ASN D 4 27  ? 37.376 -6.061  -35.532 1.00 43.72  ? 26  ASN E CG  1 
ATOM   3325 O OD1 . ASN D 4 27  ? 37.635 -6.244  -34.342 1.00 46.77  ? 26  ASN E OD1 1 
ATOM   3326 N ND2 . ASN D 4 27  ? 37.251 -7.061  -36.396 1.00 44.41  ? 26  ASN E ND2 1 
ATOM   3327 N N   . MET D 4 28  ? 34.683 -1.906  -35.901 1.00 32.06  ? 27  MET E N   1 
ATOM   3328 C CA  . MET D 4 28  ? 34.529 -0.504  -36.252 1.00 32.98  ? 27  MET E CA  1 
ATOM   3329 C C   . MET D 4 28  ? 34.226 0.350   -35.035 1.00 31.18  ? 27  MET E C   1 
ATOM   3330 O O   . MET D 4 28  ? 33.825 1.505   -35.184 1.00 35.92  ? 27  MET E O   1 
ATOM   3331 C CB  . MET D 4 28  ? 33.447 -0.343  -37.323 1.00 32.86  ? 27  MET E CB  1 
ATOM   3332 C CG  . MET D 4 28  ? 33.712 -1.182  -38.570 1.00 34.36  ? 27  MET E CG  1 
ATOM   3333 S SD  . MET D 4 28  ? 32.323 -1.206  -39.743 1.00 49.20  ? 27  MET E SD  1 
ATOM   3334 C CE  . MET D 4 28  ? 31.374 -2.604  -39.120 1.00 37.48  ? 27  MET E CE  1 
ATOM   3335 N N   . ASN D 4 29  ? 34.416 -0.202  -33.836 1.00 30.24  ? 28  ASN E N   1 
ATOM   3336 C CA  . ASN D 4 29  ? 34.132 0.466   -32.570 1.00 31.45  ? 28  ASN E CA  1 
ATOM   3337 C C   . ASN D 4 29  ? 32.695 0.994   -32.490 1.00 31.62  ? 28  ASN E C   1 
ATOM   3338 O O   . ASN D 4 29  ? 32.435 2.092   -31.992 1.00 29.31  ? 28  ASN E O   1 
ATOM   3339 C CB  . ASN D 4 29  ? 35.139 1.585   -32.305 1.00 35.42  ? 28  ASN E CB  1 
ATOM   3340 C CG  . ASN D 4 29  ? 35.521 1.661   -30.848 1.00 40.92  ? 28  ASN E CG  1 
ATOM   3341 O OD1 . ASN D 4 29  ? 36.129 0.728   -30.293 1.00 48.92  ? 28  ASN E OD1 1 
ATOM   3342 N ND2 . ASN D 4 29  ? 35.140 2.748   -30.204 1.00 42.26  ? 28  ASN E ND2 1 
ATOM   3343 N N   . HIS D 4 30  ? 31.746 0.179   -32.945 1.00 26.44  ? 29  HIS E N   1 
ATOM   3344 C CA  . HIS D 4 30  ? 30.343 0.573   -32.934 1.00 23.79  ? 29  HIS E CA  1 
ATOM   3345 C C   . HIS D 4 30  ? 29.744 0.411   -31.549 1.00 24.45  ? 29  HIS E C   1 
ATOM   3346 O O   . HIS D 4 30  ? 29.888 -0.639  -30.914 1.00 23.22  ? 29  HIS E O   1 
ATOM   3347 C CB  . HIS D 4 30  ? 29.550 -0.254  -33.942 1.00 26.70  ? 29  HIS E CB  1 
ATOM   3348 C CG  . HIS D 4 30  ? 29.786 0.162   -35.359 1.00 25.41  ? 29  HIS E CG  1 
ATOM   3349 N ND1 . HIS D 4 30  ? 29.200 -0.468  -36.430 1.00 27.38  ? 29  HIS E ND1 1 
ATOM   3350 C CD2 . HIS D 4 30  ? 30.553 1.150   -35.876 1.00 29.01  ? 29  HIS E CD2 1 
ATOM   3351 C CE1 . HIS D 4 30  ? 29.580 0.123   -37.549 1.00 32.56  ? 29  HIS E CE1 1 
ATOM   3352 N NE2 . HIS D 4 30  ? 30.397 1.112   -37.240 1.00 28.63  ? 29  HIS E NE2 1 
ATOM   3353 N N   . GLU D 4 31  ? 29.032 1.441   -31.095 1.00 24.25  ? 30  GLU E N   1 
ATOM   3354 C CA  . GLU D 4 31  ? 28.380 1.343   -29.793 1.00 25.15  ? 30  GLU E CA  1 
ATOM   3355 C C   . GLU D 4 31  ? 27.166 0.418   -29.849 1.00 22.66  ? 30  GLU E C   1 
ATOM   3356 O O   . GLU D 4 31  ? 26.880 -0.312  -28.889 1.00 23.64  ? 30  GLU E O   1 
ATOM   3357 C CB  . GLU D 4 31  ? 27.965 2.738   -29.306 1.00 24.19  ? 30  GLU E CB  1 
ATOM   3358 C CG  . GLU D 4 31  ? 29.122 3.708   -29.082 1.00 25.34  ? 30  GLU E CG  1 
ATOM   3359 C CD  . GLU D 4 31  ? 28.661 5.040   -28.475 1.00 35.98  ? 30  GLU E CD  1 
ATOM   3360 O OE1 . GLU D 4 31  ? 27.458 5.150   -28.146 1.00 34.81  ? 30  GLU E OE1 1 
ATOM   3361 O OE2 . GLU D 4 31  ? 29.498 5.971   -28.308 1.00 34.97  ? 30  GLU E OE2 1 
ATOM   3362 N N   . TYR D 4 32  ? 26.429 0.445   -30.951 1.00 19.64  ? 31  TYR E N   1 
ATOM   3363 C CA  . TYR D 4 32  ? 25.117 -0.187  -31.008 1.00 24.33  ? 31  TYR E CA  1 
ATOM   3364 C C   . TYR D 4 32  ? 25.197 -1.495  -31.782 1.00 20.36  ? 31  TYR E C   1 
ATOM   3365 O O   . TYR D 4 32  ? 25.767 -1.542  -32.873 1.00 23.22  ? 31  TYR E O   1 
ATOM   3366 C CB  . TYR D 4 32  ? 24.087 0.747   -31.649 1.00 23.55  ? 31  TYR E CB  1 
ATOM   3367 C CG  . TYR D 4 32  ? 22.730 0.103   -31.796 1.00 24.51  ? 31  TYR E CG  1 
ATOM   3368 C CD1 . TYR D 4 32  ? 21.835 0.101   -30.735 1.00 22.44  ? 31  TYR E CD1 1 
ATOM   3369 C CD2 . TYR D 4 32  ? 22.360 -0.542  -32.977 1.00 24.80  ? 31  TYR E CD2 1 
ATOM   3370 C CE1 . TYR D 4 32  ? 20.601 -0.483  -30.841 1.00 22.06  ? 31  TYR E CE1 1 
ATOM   3371 C CE2 . TYR D 4 32  ? 21.101 -1.148  -33.102 1.00 25.37  ? 31  TYR E CE2 1 
ATOM   3372 C CZ  . TYR D 4 32  ? 20.231 -1.115  -32.022 1.00 25.32  ? 31  TYR E CZ  1 
ATOM   3373 O OH  . TYR D 4 32  ? 18.981 -1.686  -32.095 1.00 23.61  ? 31  TYR E OH  1 
ATOM   3374 N N   . MET D 4 33  ? 24.617 -2.547  -31.219 1.00 21.93  ? 32  MET E N   1 
ATOM   3375 C CA  . MET D 4 33  ? 24.550 -3.842  -31.884 1.00 21.76  ? 32  MET E CA  1 
ATOM   3376 C C   . MET D 4 33  ? 23.207 -4.453  -31.516 1.00 24.29  ? 32  MET E C   1 
ATOM   3377 O O   . MET D 4 33  ? 22.702 -4.213  -30.420 1.00 23.14  ? 32  MET E O   1 
ATOM   3378 C CB  . MET D 4 33  ? 25.712 -4.763  -31.471 1.00 19.90  ? 32  MET E CB  1 
ATOM   3379 C CG  . MET D 4 33  ? 27.131 -4.248  -31.855 1.00 22.23  ? 32  MET E CG  1 
ATOM   3380 S SD  . MET D 4 33  ? 28.497 -5.357  -31.367 1.00 22.08  ? 32  MET E SD  1 
ATOM   3381 C CE  . MET D 4 33  ? 28.299 -6.629  -32.647 1.00 19.07  ? 32  MET E CE  1 
ATOM   3382 N N   . SER D 4 34  ? 22.627 -5.242  -32.428 1.00 20.82  ? 33  SER E N   1 
ATOM   3383 C CA  . SER D 4 34  ? 21.285 -5.765  -32.214 1.00 18.38  ? 33  SER E CA  1 
ATOM   3384 C C   . SER D 4 34  ? 21.132 -7.099  -32.954 1.00 25.57  ? 33  SER E C   1 
ATOM   3385 O O   . SER D 4 34  ? 21.651 -7.261  -34.061 1.00 23.48  ? 33  SER E O   1 
ATOM   3386 C CB  . SER D 4 34  ? 20.243 -4.749  -32.710 1.00 21.49  ? 33  SER E CB  1 
ATOM   3387 O OG  . SER D 4 34  ? 18.918 -5.277  -32.784 1.00 24.92  ? 33  SER E OG  1 
ATOM   3388 N N   . TRP D 4 35  ? 20.392 -8.031  -32.352 1.00 22.79  ? 34  TRP E N   1 
ATOM   3389 C CA  . TRP D 4 35  ? 20.071 -9.324  -32.947 1.00 19.21  ? 34  TRP E CA  1 
ATOM   3390 C C   . TRP D 4 35  ? 18.599 -9.374  -33.353 1.00 24.09  ? 34  TRP E C   1 
ATOM   3391 O O   . TRP D 4 35  ? 17.720 -8.898  -32.618 1.00 21.45  ? 34  TRP E O   1 
ATOM   3392 C CB  . TRP D 4 35  ? 20.355 -10.466 -31.965 1.00 20.76  ? 34  TRP E CB  1 
ATOM   3393 C CG  . TRP D 4 35  ? 21.782 -10.973 -31.983 1.00 22.87  ? 34  TRP E CG  1 
ATOM   3394 C CD1 . TRP D 4 35  ? 22.749 -10.749 -31.042 1.00 22.43  ? 34  TRP E CD1 1 
ATOM   3395 C CD2 . TRP D 4 35  ? 22.386 -11.788 -32.992 1.00 20.56  ? 34  TRP E CD2 1 
ATOM   3396 N NE1 . TRP D 4 35  ? 23.916 -11.385 -31.397 1.00 21.99  ? 34  TRP E NE1 1 
ATOM   3397 C CE2 . TRP D 4 35  ? 23.716 -12.034 -32.589 1.00 22.73  ? 34  TRP E CE2 1 
ATOM   3398 C CE3 . TRP D 4 35  ? 21.924 -12.351 -34.191 1.00 21.18  ? 34  TRP E CE3 1 
ATOM   3399 C CZ2 . TRP D 4 35  ? 24.595 -12.806 -33.349 1.00 26.61  ? 34  TRP E CZ2 1 
ATOM   3400 C CZ3 . TRP D 4 35  ? 22.798 -13.127 -34.949 1.00 21.27  ? 34  TRP E CZ3 1 
ATOM   3401 C CH2 . TRP D 4 35  ? 24.119 -13.341 -34.530 1.00 24.10  ? 34  TRP E CH2 1 
ATOM   3402 N N   . TYR D 4 36  ? 18.337 -9.959  -34.527 1.00 22.16  ? 35  TYR E N   1 
ATOM   3403 C CA  . TYR D 4 36  ? 16.987 -10.206 -35.010 1.00 23.05  ? 35  TYR E CA  1 
ATOM   3404 C C   . TYR D 4 36  ? 16.879 -11.625 -35.552 1.00 23.60  ? 35  TYR E C   1 
ATOM   3405 O O   . TYR D 4 36  ? 17.874 -12.241 -35.941 1.00 21.20  ? 35  TYR E O   1 
ATOM   3406 C CB  . TYR D 4 36  ? 16.570 -9.253  -36.144 1.00 22.98  ? 35  TYR E CB  1 
ATOM   3407 C CG  . TYR D 4 36  ? 16.908 -7.796  -35.957 1.00 23.25  ? 35  TYR E CG  1 
ATOM   3408 C CD1 . TYR D 4 36  ? 18.177 -7.310  -36.245 1.00 25.14  ? 35  TYR E CD1 1 
ATOM   3409 C CD2 . TYR D 4 36  ? 15.946 -6.897  -35.539 1.00 24.77  ? 35  TYR E CD2 1 
ATOM   3410 C CE1 . TYR D 4 36  ? 18.471 -5.959  -36.111 1.00 25.05  ? 35  TYR E CE1 1 
ATOM   3411 C CE2 . TYR D 4 36  ? 16.239 -5.542  -35.395 1.00 26.71  ? 35  TYR E CE2 1 
ATOM   3412 C CZ  . TYR D 4 36  ? 17.498 -5.089  -35.685 1.00 26.27  ? 35  TYR E CZ  1 
ATOM   3413 O OH  . TYR D 4 36  ? 17.784 -3.746  -35.547 1.00 34.54  ? 35  TYR E OH  1 
ATOM   3414 N N   . ARG D 4 37  ? 15.647 -12.124 -35.610 1.00 21.85  ? 36  ARG E N   1 
ATOM   3415 C CA  . ARG D 4 37  ? 15.345 -13.349 -36.338 1.00 22.37  ? 36  ARG E CA  1 
ATOM   3416 C C   . ARG D 4 37  ? 14.286 -13.059 -37.392 1.00 22.45  ? 36  ARG E C   1 
ATOM   3417 O O   . ARG D 4 37  ? 13.379 -12.255 -37.164 1.00 23.66  ? 36  ARG E O   1 
ATOM   3418 C CB  . ARG D 4 37  ? 14.886 -14.481 -35.388 1.00 21.58  ? 36  ARG E CB  1 
ATOM   3419 C CG  . ARG D 4 37  ? 13.616 -14.198 -34.581 1.00 21.03  ? 36  ARG E CG  1 
ATOM   3420 C CD  . ARG D 4 37  ? 13.260 -15.407 -33.713 1.00 22.42  ? 36  ARG E CD  1 
ATOM   3421 N NE  . ARG D 4 37  ? 12.630 -16.465 -34.511 1.00 19.24  ? 36  ARG E NE  1 
ATOM   3422 C CZ  . ARG D 4 37  ? 12.236 -17.635 -34.020 1.00 25.17  ? 36  ARG E CZ  1 
ATOM   3423 N NH1 . ARG D 4 37  ? 12.420 -17.919 -32.731 1.00 21.38  ? 36  ARG E NH1 1 
ATOM   3424 N NH2 . ARG D 4 37  ? 11.660 -18.530 -34.818 1.00 25.48  ? 36  ARG E NH2 1 
ATOM   3425 N N   . GLN D 4 38  ? 14.435 -13.690 -38.556 1.00 23.11  ? 37  GLN E N   1 
ATOM   3426 C CA  . GLN D 4 38  ? 13.525 -13.542 -39.695 1.00 26.38  ? 37  GLN E CA  1 
ATOM   3427 C C   . GLN D 4 38  ? 13.000 -14.916 -40.093 1.00 21.24  ? 37  GLN E C   1 
ATOM   3428 O O   . GLN D 4 38  ? 13.755 -15.727 -40.630 1.00 21.10  ? 37  GLN E O   1 
ATOM   3429 C CB  . GLN D 4 38  ? 14.226 -12.893 -40.895 1.00 23.60  ? 37  GLN E CB  1 
ATOM   3430 C CG  . GLN D 4 38  ? 13.309 -12.710 -42.105 1.00 21.18  ? 37  GLN E CG  1 
ATOM   3431 C CD  . GLN D 4 38  ? 14.049 -12.246 -43.345 1.00 23.97  ? 37  GLN E CD  1 
ATOM   3432 O OE1 . GLN D 4 38  ? 15.160 -12.688 -43.617 1.00 27.86  ? 37  GLN E OE1 1 
ATOM   3433 N NE2 . GLN D 4 38  ? 13.431 -11.355 -44.108 1.00 21.88  ? 37  GLN E NE2 1 
ATOM   3434 N N   . ASP D 4 39  ? 11.724 -15.183 -39.823 1.00 22.23  ? 38  ASP E N   1 
ATOM   3435 C CA  . ASP D 4 39  ? 11.102 -16.413 -40.295 1.00 24.67  ? 38  ASP E CA  1 
ATOM   3436 C C   . ASP D 4 39  ? 10.812 -16.271 -41.797 1.00 27.59  ? 38  ASP E C   1 
ATOM   3437 O O   . ASP D 4 39  ? 10.810 -15.158 -42.327 1.00 27.70  ? 38  ASP E O   1 
ATOM   3438 C CB  . ASP D 4 39  ? 9.824  -16.704 -39.499 1.00 25.49  ? 38  ASP E CB  1 
ATOM   3439 C CG  . ASP D 4 39  ? 10.099 -17.380 -38.125 1.00 31.17  ? 38  ASP E CG  1 
ATOM   3440 O OD1 . ASP D 4 39  ? 11.271 -17.584 -37.727 1.00 29.05  ? 38  ASP E OD1 1 
ATOM   3441 O OD2 . ASP D 4 39  ? 9.118  -17.723 -37.427 1.00 39.92  ? 38  ASP E OD2 1 
ATOM   3442 N N   . PRO D 4 40  ? 10.614 -17.377 -42.521 1.00 26.47  ? 39  PRO E N   1 
ATOM   3443 C CA  . PRO D 4 40  ? 10.427 -17.259 -43.981 1.00 25.82  ? 39  PRO E CA  1 
ATOM   3444 C C   . PRO D 4 40  ? 9.207  -16.409 -44.320 1.00 24.67  ? 39  PRO E C   1 
ATOM   3445 O O   . PRO D 4 40  ? 8.129  -16.588 -43.753 1.00 29.01  ? 39  PRO E O   1 
ATOM   3446 C CB  . PRO D 4 40  ? 10.259 -18.718 -44.447 1.00 23.68  ? 39  PRO E CB  1 
ATOM   3447 C CG  . PRO D 4 40  ? 10.929 -19.559 -43.341 1.00 27.84  ? 39  PRO E CG  1 
ATOM   3448 C CD  . PRO D 4 40  ? 10.640 -18.786 -42.069 1.00 20.35  ? 39  PRO E CD  1 
ATOM   3449 N N   . GLY D 4 41  ? 9.396  -15.453 -45.227 1.00 24.52  ? 40  GLY E N   1 
ATOM   3450 C CA  . GLY D 4 41  ? 8.318  -14.596 -45.669 1.00 31.80  ? 40  GLY E CA  1 
ATOM   3451 C C   . GLY D 4 41  ? 7.957  -13.443 -44.751 1.00 31.54  ? 40  GLY E C   1 
ATOM   3452 O O   . GLY D 4 41  ? 7.154  -12.588 -45.149 1.00 32.69  ? 40  GLY E O   1 
ATOM   3453 N N   . LEU D 4 42  ? 8.525  -13.365 -43.554 1.00 27.11  ? 41  LEU E N   1 
ATOM   3454 C CA  . LEU D 4 42  ? 8.169  -12.304 -42.621 1.00 28.85  ? 41  LEU E CA  1 
ATOM   3455 C C   . LEU D 4 42  ? 9.317  -11.300 -42.507 1.00 27.80  ? 41  LEU E C   1 
ATOM   3456 O O   . LEU D 4 42  ? 10.297 -11.352 -43.258 1.00 28.48  ? 41  LEU E O   1 
ATOM   3457 C CB  . LEU D 4 42  ? 7.799  -12.900 -41.263 1.00 26.25  ? 41  LEU E CB  1 
ATOM   3458 C CG  . LEU D 4 42  ? 6.615  -13.873 -41.214 1.00 35.53  ? 41  LEU E CG  1 
ATOM   3459 C CD1 . LEU D 4 42  ? 6.519  -14.502 -39.836 1.00 36.44  ? 41  LEU E CD1 1 
ATOM   3460 C CD2 . LEU D 4 42  ? 5.315  -13.170 -41.555 1.00 31.20  ? 41  LEU E CD2 1 
ATOM   3461 N N   . GLY D 4 43  ? 9.180  -10.360 -41.573 1.00 30.07  ? 42  GLY E N   1 
ATOM   3462 C CA  . GLY D 4 43  ? 10.192 -9.357  -41.328 1.00 28.07  ? 42  GLY E CA  1 
ATOM   3463 C C   . GLY D 4 43  ? 11.113 -9.744  -40.181 1.00 27.62  ? 42  GLY E C   1 
ATOM   3464 O O   . GLY D 4 43  ? 11.116 -10.878 -39.701 1.00 24.77  ? 42  GLY E O   1 
ATOM   3465 N N   . LEU D 4 44  ? 11.911 -8.770  -39.741 1.00 29.32  ? 43  LEU E N   1 
ATOM   3466 C CA  . LEU D 4 44  ? 12.927 -8.999  -38.715 1.00 27.24  ? 43  LEU E CA  1 
ATOM   3467 C C   . LEU D 4 44  ? 12.328 -8.733  -37.342 1.00 23.49  ? 43  LEU E C   1 
ATOM   3468 O O   . LEU D 4 44  ? 11.795 -7.649  -37.094 1.00 27.48  ? 43  LEU E O   1 
ATOM   3469 C CB  . LEU D 4 44  ? 14.152 -8.113  -38.961 1.00 24.39  ? 43  LEU E CB  1 
ATOM   3470 C CG  . LEU D 4 44  ? 15.237 -8.783  -39.821 1.00 22.49  ? 43  LEU E CG  1 
ATOM   3471 C CD1 . LEU D 4 44  ? 14.710 -9.138  -41.234 1.00 25.09  ? 43  LEU E CD1 1 
ATOM   3472 C CD2 . LEU D 4 44  ? 16.473 -7.917  -39.912 1.00 22.39  ? 43  LEU E CD2 1 
ATOM   3473 N N   . ARG D 4 45  ? 12.380 -9.726  -36.465 1.00 25.00  ? 44  ARG E N   1 
ATOM   3474 C CA  . ARG D 4 45  ? 11.900 -9.575  -35.098 1.00 27.02  ? 44  ARG E CA  1 
ATOM   3475 C C   . ARG D 4 45  ? 13.096 -9.388  -34.164 1.00 25.63  ? 44  ARG E C   1 
ATOM   3476 O O   . ARG D 4 45  ? 13.999 -10.232 -34.125 1.00 23.05  ? 44  ARG E O   1 
ATOM   3477 C CB  . ARG D 4 45  ? 11.057 -10.779 -34.677 1.00 26.19  ? 44  ARG E CB  1 
ATOM   3478 C CG  . ARG D 4 45  ? 9.976  -11.143 -35.666 1.00 29.44  ? 44  ARG E CG  1 
ATOM   3479 C CD  . ARG D 4 45  ? 8.691  -10.359 -35.421 1.00 36.49  ? 44  ARG E CD  1 
ATOM   3480 N NE  . ARG D 4 45  ? 8.492  -9.277  -36.391 1.00 36.06  ? 44  ARG E NE  1 
ATOM   3481 C CZ  . ARG D 4 45  ? 7.800  -9.400  -37.531 1.00 42.65  ? 44  ARG E CZ  1 
ATOM   3482 N NH1 . ARG D 4 45  ? 7.239  -10.564 -37.868 1.00 39.31  ? 44  ARG E NH1 1 
ATOM   3483 N NH2 . ARG D 4 45  ? 7.677  -8.355  -38.349 1.00 39.44  ? 44  ARG E NH2 1 
ATOM   3484 N N   . GLN D 4 46  ? 13.089 -8.295  -33.408 1.00 22.35  ? 45  GLN E N   1 
ATOM   3485 C CA  . GLN D 4 46  ? 14.217 -7.960  -32.549 1.00 25.07  ? 45  GLN E CA  1 
ATOM   3486 C C   . GLN D 4 46  ? 14.251 -8.858  -31.315 1.00 22.51  ? 45  GLN E C   1 
ATOM   3487 O O   . GLN D 4 46  ? 13.254 -9.003  -30.605 1.00 26.27  ? 45  GLN E O   1 
ATOM   3488 C CB  . GLN D 4 46  ? 14.141 -6.489  -32.132 1.00 21.49  ? 45  GLN E CB  1 
ATOM   3489 C CG  . GLN D 4 46  ? 15.474 -5.898  -31.675 1.00 21.07  ? 45  GLN E CG  1 
ATOM   3490 C CD  . GLN D 4 46  ? 15.353 -4.417  -31.305 1.00 20.48  ? 45  GLN E CD  1 
ATOM   3491 O OE1 . GLN D 4 46  ? 14.312 -3.966  -30.819 1.00 21.59  ? 45  GLN E OE1 1 
ATOM   3492 N NE2 . GLN D 4 46  ? 16.412 -3.653  -31.555 1.00 19.54  ? 45  GLN E NE2 1 
ATOM   3493 N N   . ILE D 4 47  ? 15.414 -9.445  -31.049 1.00 23.85  ? 46  ILE E N   1 
ATOM   3494 C CA  . ILE D 4 47  ? 15.587 -10.363 -29.927 1.00 23.28  ? 46  ILE E CA  1 
ATOM   3495 C C   . ILE D 4 47  ? 16.120 -9.618  -28.700 1.00 24.70  ? 46  ILE E C   1 
ATOM   3496 O O   . ILE D 4 47  ? 15.454 -9.556  -27.661 1.00 21.01  ? 46  ILE E O   1 
ATOM   3497 C CB  . ILE D 4 47  ? 16.520 -11.518 -30.335 1.00 25.09  ? 46  ILE E CB  1 
ATOM   3498 C CG1 . ILE D 4 47  ? 15.994 -12.180 -31.628 1.00 22.53  ? 46  ILE E CG1 1 
ATOM   3499 C CG2 . ILE D 4 47  ? 16.654 -12.530 -29.198 1.00 21.18  ? 46  ILE E CG2 1 
ATOM   3500 C CD1 . ILE D 4 47  ? 16.938 -13.214 -32.209 1.00 19.58  ? 46  ILE E CD1 1 
ATOM   3501 N N   . TYR D 4 48  ? 17.328 -9.064  -28.825 1.00 24.23  ? 47  TYR E N   1 
ATOM   3502 C CA  . TYR D 4 48  ? 18.005 -8.252  -27.821 1.00 25.15  ? 47  TYR E CA  1 
ATOM   3503 C C   . TYR D 4 48  ? 18.828 -7.229  -28.586 1.00 19.38  ? 47  TYR E C   1 
ATOM   3504 O O   . TYR D 4 48  ? 19.187 -7.454  -29.740 1.00 22.30  ? 47  TYR E O   1 
ATOM   3505 C CB  . TYR D 4 48  ? 18.974 -9.053  -26.904 1.00 23.19  ? 47  TYR E CB  1 
ATOM   3506 C CG  . TYR D 4 48  ? 18.406 -9.770  -25.688 1.00 24.28  ? 47  TYR E CG  1 
ATOM   3507 C CD1 . TYR D 4 48  ? 18.342 -9.152  -24.440 1.00 28.09  ? 47  TYR E CD1 1 
ATOM   3508 C CD2 . TYR D 4 48  ? 18.014 -11.096 -25.775 1.00 24.31  ? 47  TYR E CD2 1 
ATOM   3509 C CE1 . TYR D 4 48  ? 17.840 -9.843  -23.308 1.00 26.91  ? 47  TYR E CE1 1 
ATOM   3510 C CE2 . TYR D 4 48  ? 17.515 -11.778 -24.691 1.00 26.93  ? 47  TYR E CE2 1 
ATOM   3511 C CZ  . TYR D 4 48  ? 17.424 -11.154 -23.457 1.00 29.13  ? 47  TYR E CZ  1 
ATOM   3512 O OH  . TYR D 4 48  ? 16.922 -11.886 -22.401 1.00 31.50  ? 47  TYR E OH  1 
ATOM   3513 N N   . TYR D 4 49  ? 19.146 -6.111  -27.941 1.00 17.95  ? 48  TYR E N   1 
ATOM   3514 C CA  . TYR D 4 49  ? 20.074 -5.162  -28.541 1.00 17.80  ? 48  TYR E CA  1 
ATOM   3515 C C   . TYR D 4 49  ? 20.887 -4.534  -27.425 1.00 22.08  ? 48  TYR E C   1 
ATOM   3516 O O   . TYR D 4 49  ? 20.522 -4.596  -26.254 1.00 20.17  ? 48  TYR E O   1 
ATOM   3517 C CB  . TYR D 4 49  ? 19.367 -4.079  -29.379 1.00 19.43  ? 48  TYR E CB  1 
ATOM   3518 C CG  . TYR D 4 49  ? 18.318 -3.325  -28.606 1.00 19.73  ? 48  TYR E CG  1 
ATOM   3519 C CD1 . TYR D 4 49  ? 17.032 -3.819  -28.497 1.00 21.71  ? 48  TYR E CD1 1 
ATOM   3520 C CD2 . TYR D 4 49  ? 18.629 -2.142  -27.947 1.00 21.68  ? 48  TYR E CD2 1 
ATOM   3521 C CE1 . TYR D 4 49  ? 16.066 -3.154  -27.780 1.00 20.75  ? 48  TYR E CE1 1 
ATOM   3522 C CE2 . TYR D 4 49  ? 17.662 -1.457  -27.228 1.00 24.00  ? 48  TYR E CE2 1 
ATOM   3523 C CZ  . TYR D 4 49  ? 16.390 -1.977  -27.144 1.00 22.95  ? 48  TYR E CZ  1 
ATOM   3524 O OH  . TYR D 4 49  ? 15.422 -1.316  -26.436 1.00 26.68  ? 48  TYR E OH  1 
ATOM   3525 N N   . SER D 4 50  ? 22.004 -3.929  -27.803 1.00 23.27  ? 49  SER E N   1 
ATOM   3526 C CA  . SER D 4 50  ? 22.941 -3.407  -26.830 1.00 21.35  ? 49  SER E CA  1 
ATOM   3527 C C   . SER D 4 50  ? 23.356 -2.023  -27.280 1.00 22.21  ? 49  SER E C   1 
ATOM   3528 O O   . SER D 4 50  ? 23.915 -1.872  -28.369 1.00 22.26  ? 49  SER E O   1 
ATOM   3529 C CB  . SER D 4 50  ? 24.163 -4.312  -26.686 1.00 21.67  ? 49  SER E CB  1 
ATOM   3530 O OG  . SER D 4 50  ? 25.205 -3.601  -26.056 1.00 20.51  ? 49  SER E OG  1 
ATOM   3531 N N   . MET D 4 51  ? 23.103 -1.019  -26.426 1.00 24.98  ? 50  MET E N   1 
ATOM   3532 C CA  . MET D 4 51  ? 23.361 0.365   -26.798 1.00 22.95  ? 50  MET E CA  1 
ATOM   3533 C C   . MET D 4 51  ? 24.822 0.750   -26.639 1.00 24.42  ? 50  MET E C   1 
ATOM   3534 O O   . MET D 4 51  ? 25.259 1.736   -27.249 1.00 26.10  ? 50  MET E O   1 
ATOM   3535 C CB  . MET D 4 51  ? 22.463 1.298   -25.989 1.00 21.51  ? 50  MET E CB  1 
ATOM   3536 C CG  . MET D 4 51  ? 21.035 1.434   -26.549 1.00 24.99  ? 50  MET E CG  1 
ATOM   3537 S SD  . MET D 4 51  ? 19.962 2.459   -25.495 1.00 36.06  ? 50  MET E SD  1 
ATOM   3538 C CE  . MET D 4 51  ? 20.656 4.077   -25.825 1.00 30.79  ? 50  MET E CE  1 
ATOM   3539 N N   . ASN D 4 52  ? 25.590 -0.026  -25.878 1.00 22.70  ? 51  ASN E N   1 
ATOM   3540 C CA  . ASN D 4 52  ? 27.007 0.226   -25.652 1.00 24.33  ? 51  ASN E CA  1 
ATOM   3541 C C   . ASN D 4 52  ? 27.519 -0.910  -24.775 1.00 23.71  ? 51  ASN E C   1 
ATOM   3542 O O   . ASN D 4 52  ? 26.749 -1.784  -24.365 1.00 24.35  ? 51  ASN E O   1 
ATOM   3543 C CB  . ASN D 4 52  ? 27.256 1.589   -25.006 1.00 23.83  ? 51  ASN E CB  1 
ATOM   3544 C CG  . ASN D 4 52  ? 28.618 2.131   -25.325 1.00 27.76  ? 51  ASN E CG  1 
ATOM   3545 O OD1 . ASN D 4 52  ? 29.534 1.366   -25.636 1.00 29.20  ? 51  ASN E OD1 1 
ATOM   3546 N ND2 . ASN D 4 52  ? 28.772 3.453   -25.251 1.00 31.06  ? 51  ASN E ND2 1 
ATOM   3547 N N   . VAL D 4 53  ? 28.831 -0.908  -24.516 1.00 25.32  ? 52  VAL E N   1 
ATOM   3548 C CA  . VAL D 4 53  ? 29.438 -1.852  -23.572 1.00 25.06  ? 52  VAL E CA  1 
ATOM   3549 C C   . VAL D 4 53  ? 28.603 -1.935  -22.301 1.00 25.47  ? 52  VAL E C   1 
ATOM   3550 O O   . VAL D 4 53  ? 28.237 -0.905  -21.722 1.00 26.43  ? 52  VAL E O   1 
ATOM   3551 C CB  . VAL D 4 53  ? 30.890 -1.455  -23.259 1.00 28.09  ? 52  VAL E CB  1 
ATOM   3552 C CG1 . VAL D 4 53  ? 31.510 -2.383  -22.198 1.00 28.79  ? 52  VAL E CG1 1 
ATOM   3553 C CG2 . VAL D 4 53  ? 31.711 -1.495  -24.541 1.00 32.27  ? 52  VAL E CG2 1 
ATOM   3554 N N   . GLU D 4 54  ? 28.236 -3.163  -21.900 1.00 22.90  ? 53  GLU E N   1 
ATOM   3555 C CA  . GLU D 4 54  ? 27.555 -3.462  -20.638 1.00 25.51  ? 53  GLU E CA  1 
ATOM   3556 C C   . GLU D 4 54  ? 26.136 -2.902  -20.559 1.00 27.95  ? 53  GLU E C   1 
ATOM   3557 O O   . GLU D 4 54  ? 25.615 -2.674  -19.457 1.00 32.21  ? 53  GLU E O   1 
ATOM   3558 C CB  . GLU D 4 54  ? 28.365 -2.960  -19.434 1.00 27.81  ? 53  GLU E CB  1 
ATOM   3559 C CG  . GLU D 4 54  ? 29.661 -3.707  -19.233 1.00 28.24  ? 53  GLU E CG  1 
ATOM   3560 C CD  . GLU D 4 54  ? 29.474 -5.143  -18.737 1.00 36.49  ? 53  GLU E CD  1 
ATOM   3561 O OE1 . GLU D 4 54  ? 28.359 -5.568  -18.357 1.00 39.13  ? 53  GLU E OE1 1 
ATOM   3562 O OE2 . GLU D 4 54  ? 30.477 -5.863  -18.715 1.00 39.95  ? 53  GLU E OE2 1 
ATOM   3563 N N   . VAL D 4 55  ? 25.497 -2.664  -21.694 1.00 26.04  ? 54  VAL E N   1 
ATOM   3564 C CA  . VAL D 4 55  ? 24.109 -2.218  -21.759 1.00 26.78  ? 54  VAL E CA  1 
ATOM   3565 C C   . VAL D 4 55  ? 23.372 -3.182  -22.680 1.00 22.67  ? 54  VAL E C   1 
ATOM   3566 O O   . VAL D 4 55  ? 23.708 -3.282  -23.862 1.00 24.40  ? 54  VAL E O   1 
ATOM   3567 C CB  . VAL D 4 55  ? 23.993 -0.771  -22.283 1.00 25.17  ? 54  VAL E CB  1 
ATOM   3568 C CG1 . VAL D 4 55  ? 22.523 -0.362  -22.453 1.00 21.40  ? 54  VAL E CG1 1 
ATOM   3569 C CG2 . VAL D 4 55  ? 24.752 0.213   -21.368 1.00 22.89  ? 54  VAL E CG2 1 
ATOM   3570 N N   . THR D 4 56  ? 22.393 -3.901  -22.150 1.00 22.95  ? 55  THR E N   1 
ATOM   3571 C CA  . THR D 4 56  ? 21.551 -4.745  -22.986 1.00 26.27  ? 55  THR E CA  1 
ATOM   3572 C C   . THR D 4 56  ? 20.091 -4.472  -22.648 1.00 28.39  ? 55  THR E C   1 
ATOM   3573 O O   . THR D 4 56  ? 19.763 -3.980  -21.562 1.00 21.91  ? 55  THR E O   1 
ATOM   3574 C CB  . THR D 4 56  ? 21.882 -6.246  -22.834 1.00 26.28  ? 55  THR E CB  1 
ATOM   3575 O OG1 . THR D 4 56  ? 21.540 -6.693  -21.522 1.00 26.65  ? 55  THR E OG1 1 
ATOM   3576 C CG2 . THR D 4 56  ? 23.391 -6.518  -23.083 1.00 21.73  ? 55  THR E CG2 1 
ATOM   3577 N N   . ASP D 4 57  ? 19.217 -4.749  -23.619 1.00 25.48  ? 56  ASP E N   1 
ATOM   3578 C CA  . ASP D 4 57  ? 17.789 -4.503  -23.468 1.00 23.74  ? 56  ASP E CA  1 
ATOM   3579 C C   . ASP D 4 57  ? 17.043 -5.521  -24.315 1.00 27.06  ? 56  ASP E C   1 
ATOM   3580 O O   . ASP D 4 57  ? 17.478 -5.859  -25.422 1.00 24.60  ? 56  ASP E O   1 
ATOM   3581 C CB  . ASP D 4 57  ? 17.403 -3.079  -23.904 1.00 22.63  ? 56  ASP E CB  1 
ATOM   3582 C CG  . ASP D 4 57  ? 17.848 -2.018  -22.908 1.00 27.92  ? 56  ASP E CG  1 
ATOM   3583 O OD1 . ASP D 4 57  ? 17.353 -2.054  -21.756 1.00 26.80  ? 56  ASP E OD1 1 
ATOM   3584 O OD2 . ASP D 4 57  ? 18.691 -1.156  -23.279 1.00 25.10  ? 56  ASP E OD2 1 
ATOM   3585 N N   . LYS D 4 58  ? 15.921 -5.997  -23.789 1.00 26.36  ? 57  LYS E N   1 
ATOM   3586 C CA  . LYS D 4 58  ? 15.124 -6.991  -24.484 1.00 27.20  ? 57  LYS E CA  1 
ATOM   3587 C C   . LYS D 4 58  ? 14.394 -6.370  -25.673 1.00 27.98  ? 57  LYS E C   1 
ATOM   3588 O O   . LYS D 4 58  ? 13.929 -5.225  -25.620 1.00 25.72  ? 57  LYS E O   1 
ATOM   3589 C CB  . LYS D 4 58  ? 14.118 -7.617  -23.523 1.00 28.15  ? 57  LYS E CB  1 
ATOM   3590 C CG  . LYS D 4 58  ? 14.738 -8.596  -22.530 1.00 26.71  ? 57  LYS E CG  1 
ATOM   3591 C CD  . LYS D 4 58  ? 13.804 -8.798  -21.339 1.00 39.53  ? 57  LYS E CD  1 
ATOM   3592 C CE  . LYS D 4 58  ? 14.239 -9.959  -20.453 1.00 34.75  ? 57  LYS E CE  1 
ATOM   3593 N NZ  . LYS D 4 58  ? 13.145 -10.293 -19.504 1.00 42.40  ? 57  LYS E NZ  1 
ATOM   3594 N N   . GLY D 4 59  ? 14.314 -7.125  -26.758 1.00 26.17  ? 58  GLY E N   1 
ATOM   3595 C CA  . GLY D 4 59  ? 13.438 -6.801  -27.867 1.00 29.61  ? 58  GLY E CA  1 
ATOM   3596 C C   . GLY D 4 59  ? 12.072 -7.433  -27.686 1.00 28.59  ? 58  GLY E C   1 
ATOM   3597 O O   . GLY D 4 59  ? 11.650 -7.753  -26.571 1.00 28.07  ? 58  GLY E O   1 
ATOM   3598 N N   . ASP D 4 60  ? 11.390 -7.663  -28.808 1.00 27.70  ? 59  ASP E N   1 
ATOM   3599 C CA  . ASP D 4 60  ? 10.040 -8.204  -28.759 1.00 28.07  ? 59  ASP E CA  1 
ATOM   3600 C C   . ASP D 4 60  ? 10.027 -9.701  -28.458 1.00 29.37  ? 59  ASP E C   1 
ATOM   3601 O O   . ASP D 4 60  ? 9.069  -10.197 -27.849 1.00 31.73  ? 59  ASP E O   1 
ATOM   3602 C CB  . ASP D 4 60  ? 9.329  -7.901  -30.081 1.00 32.62  ? 59  ASP E CB  1 
ATOM   3603 C CG  . ASP D 4 60  ? 8.912  -6.436  -30.189 1.00 39.55  ? 59  ASP E CG  1 
ATOM   3604 O OD1 . ASP D 4 60  ? 8.389  -5.903  -29.185 1.00 43.18  ? 59  ASP E OD1 1 
ATOM   3605 O OD2 . ASP D 4 60  ? 9.120  -5.813  -31.259 1.00 40.73  ? 59  ASP E OD2 1 
ATOM   3606 N N   . VAL D 4 61  ? 11.068 -10.436 -28.848 1.00 27.00  ? 60  VAL E N   1 
ATOM   3607 C CA  . VAL D 4 61  ? 11.056 -11.888 -28.672 1.00 27.31  ? 60  VAL E CA  1 
ATOM   3608 C C   . VAL D 4 61  ? 12.339 -12.351 -27.977 1.00 28.51  ? 60  VAL E C   1 
ATOM   3609 O O   . VAL D 4 61  ? 13.188 -13.010 -28.597 1.00 25.79  ? 60  VAL E O   1 
ATOM   3610 C CB  . VAL D 4 61  ? 10.799 -12.601 -30.022 1.00 34.69  ? 60  VAL E CB  1 
ATOM   3611 C CG1 . VAL D 4 61  ? 9.387  -12.279 -30.513 1.00 34.98  ? 60  VAL E CG1 1 
ATOM   3612 C CG2 . VAL D 4 61  ? 11.794 -12.197 -31.124 1.00 25.29  ? 60  VAL E CG2 1 
ATOM   3613 N N   . PRO D 4 62  ? 12.503 -12.065 -26.663 1.00 27.82  ? 61  PRO E N   1 
ATOM   3614 C CA  . PRO D 4 62  ? 13.746 -12.439 -25.969 1.00 24.46  ? 61  PRO E CA  1 
ATOM   3615 C C   . PRO D 4 62  ? 13.783 -13.852 -25.409 1.00 26.52  ? 61  PRO E C   1 
ATOM   3616 O O   . PRO D 4 62  ? 14.868 -14.340 -25.072 1.00 24.85  ? 61  PRO E O   1 
ATOM   3617 C CB  . PRO D 4 62  ? 13.818 -11.421 -24.823 1.00 25.49  ? 61  PRO E CB  1 
ATOM   3618 C CG  . PRO D 4 62  ? 12.366 -11.140 -24.509 1.00 28.85  ? 61  PRO E CG  1 
ATOM   3619 C CD  . PRO D 4 62  ? 11.658 -11.168 -25.842 1.00 26.86  ? 61  PRO E CD  1 
ATOM   3620 N N   . GLU D 4 63  ? 12.625 -14.501 -25.278 1.00 28.26  ? 62  GLU E N   1 
ATOM   3621 C CA  . GLU D 4 63  ? 12.535 -15.774 -24.566 1.00 30.89  ? 62  GLU E CA  1 
ATOM   3622 C C   . GLU D 4 63  ? 13.318 -16.863 -25.294 1.00 27.26  ? 62  GLU E C   1 
ATOM   3623 O O   . GLU D 4 63  ? 13.260 -16.979 -26.521 1.00 29.41  ? 62  GLU E O   1 
ATOM   3624 C CB  . GLU D 4 63  ? 11.067 -16.205 -24.410 1.00 30.24  ? 62  GLU E CB  1 
ATOM   3625 C CG  . GLU D 4 63  ? 10.135 -15.163 -23.800 1.00 32.43  ? 62  GLU E CG  1 
ATOM   3626 C CD  . GLU D 4 63  ? 9.838  -14.000 -24.750 1.00 40.09  ? 62  GLU E CD  1 
ATOM   3627 O OE1 . GLU D 4 63  ? 9.449  -12.921 -24.249 1.00 46.58  ? 62  GLU E OE1 1 
ATOM   3628 O OE2 . GLU D 4 63  ? 10.014 -14.152 -25.993 1.00 34.39  ? 62  GLU E OE2 1 
ATOM   3629 N N   . GLY D 4 64  ? 14.051 -17.667 -24.531 1.00 28.32  ? 63  GLY E N   1 
ATOM   3630 C CA  . GLY D 4 64  ? 14.928 -18.685 -25.097 1.00 24.59  ? 63  GLY E CA  1 
ATOM   3631 C C   . GLY D 4 64  ? 16.277 -18.168 -25.547 1.00 25.68  ? 63  GLY E C   1 
ATOM   3632 O O   . GLY D 4 64  ? 17.067 -18.947 -26.098 1.00 25.84  ? 63  GLY E O   1 
ATOM   3633 N N   . TYR D 4 65  ? 16.566 -16.882 -25.324 1.00 21.36  ? 64  TYR E N   1 
ATOM   3634 C CA  . TYR D 4 65  ? 17.797 -16.239 -25.756 1.00 23.24  ? 64  TYR E CA  1 
ATOM   3635 C C   . TYR D 4 65  ? 18.441 -15.476 -24.600 1.00 21.47  ? 64  TYR E C   1 
ATOM   3636 O O   . TYR D 4 65  ? 17.759 -14.961 -23.716 1.00 25.31  ? 64  TYR E O   1 
ATOM   3637 C CB  . TYR D 4 65  ? 17.551 -15.248 -26.915 1.00 20.94  ? 64  TYR E CB  1 
ATOM   3638 C CG  . TYR D 4 65  ? 16.883 -15.846 -28.129 1.00 23.11  ? 64  TYR E CG  1 
ATOM   3639 C CD1 . TYR D 4 65  ? 17.604 -16.570 -29.070 1.00 19.59  ? 64  TYR E CD1 1 
ATOM   3640 C CD2 . TYR D 4 65  ? 15.525 -15.689 -28.326 1.00 22.79  ? 64  TYR E CD2 1 
ATOM   3641 C CE1 . TYR D 4 65  ? 16.970 -17.121 -30.175 1.00 22.50  ? 64  TYR E CE1 1 
ATOM   3642 C CE2 . TYR D 4 65  ? 14.892 -16.226 -29.421 1.00 21.75  ? 64  TYR E CE2 1 
ATOM   3643 C CZ  . TYR D 4 65  ? 15.601 -16.948 -30.333 1.00 22.48  ? 64  TYR E CZ  1 
ATOM   3644 O OH  . TYR D 4 65  ? 14.917 -17.461 -31.417 1.00 21.67  ? 64  TYR E OH  1 
ATOM   3645 N N   . LYS D 4 66  ? 19.767 -15.384 -24.640 1.00 23.83  ? 65  LYS E N   1 
ATOM   3646 C CA  . LYS D 4 66  ? 20.533 -14.467 -23.805 1.00 25.10  ? 65  LYS E CA  1 
ATOM   3647 C C   . LYS D 4 66  ? 21.620 -13.828 -24.656 1.00 23.55  ? 65  LYS E C   1 
ATOM   3648 O O   . LYS D 4 66  ? 22.038 -14.378 -25.675 1.00 23.22  ? 65  LYS E O   1 
ATOM   3649 C CB  . LYS D 4 66  ? 21.176 -15.172 -22.600 1.00 21.19  ? 65  LYS E CB  1 
ATOM   3650 C CG  . LYS D 4 66  ? 20.175 -15.746 -21.589 1.00 26.13  ? 65  LYS E CG  1 
ATOM   3651 C CD  . LYS D 4 66  ? 19.224 -14.658 -21.066 1.00 35.55  ? 65  LYS E CD  1 
ATOM   3652 C CE  . LYS D 4 66  ? 18.139 -15.231 -20.143 1.00 33.53  ? 65  LYS E CE  1 
ATOM   3653 N NZ  . LYS D 4 66  ? 18.744 -15.670 -18.858 1.00 42.34  ? 65  LYS E NZ  1 
ATOM   3654 N N   . VAL D 4 67  ? 22.091 -12.661 -24.218 1.00 27.30  ? 66  VAL E N   1 
ATOM   3655 C CA  . VAL D 4 67  ? 23.202 -11.969 -24.858 1.00 24.15  ? 66  VAL E CA  1 
ATOM   3656 C C   . VAL D 4 67  ? 24.140 -11.456 -23.771 1.00 25.99  ? 66  VAL E C   1 
ATOM   3657 O O   . VAL D 4 67  ? 23.823 -11.470 -22.581 1.00 26.16  ? 66  VAL E O   1 
ATOM   3658 C CB  . VAL D 4 67  ? 22.731 -10.794 -25.747 1.00 22.23  ? 66  VAL E CB  1 
ATOM   3659 C CG1 . VAL D 4 67  ? 21.882 -11.283 -26.877 1.00 18.22  ? 66  VAL E CG1 1 
ATOM   3660 C CG2 . VAL D 4 67  ? 21.971 -9.750  -24.889 1.00 23.71  ? 66  VAL E CG2 1 
ATOM   3661 N N   . SER D 4 68  ? 25.305 -10.989 -24.200 1.00 24.45  ? 67  SER E N   1 
ATOM   3662 C CA  . SER D 4 68  ? 26.206 -10.276 -23.309 1.00 27.53  ? 67  SER E CA  1 
ATOM   3663 C C   . SER D 4 68  ? 26.933 -9.219  -24.127 1.00 22.88  ? 67  SER E C   1 
ATOM   3664 O O   . SER D 4 68  ? 27.013 -9.303  -25.356 1.00 22.05  ? 67  SER E O   1 
ATOM   3665 C CB  . SER D 4 68  ? 27.197 -11.231 -22.617 1.00 27.05  ? 67  SER E CB  1 
ATOM   3666 O OG  . SER D 4 68  ? 28.279 -11.556 -23.478 1.00 29.14  ? 67  SER E OG  1 
ATOM   3667 N N   . ARG D 4 69  ? 27.453 -8.208  -23.432 1.00 21.82  ? 68  ARG E N   1 
ATOM   3668 C CA  . ARG D 4 69  ? 28.209 -7.146  -24.089 1.00 24.78  ? 68  ARG E CA  1 
ATOM   3669 C C   . ARG D 4 69  ? 29.325 -6.693  -23.139 1.00 28.88  ? 68  ARG E C   1 
ATOM   3670 O O   . ARG D 4 69  ? 29.266 -5.632  -22.511 1.00 28.12  ? 68  ARG E O   1 
ATOM   3671 C CB  . ARG D 4 69  ? 27.303 -5.981  -24.500 1.00 21.16  ? 68  ARG E CB  1 
ATOM   3672 C CG  . ARG D 4 69  ? 27.979 -5.014  -25.448 1.00 22.68  ? 68  ARG E CG  1 
ATOM   3673 C CD  . ARG D 4 69  ? 27.940 -5.536  -26.887 1.00 20.77  ? 68  ARG E CD  1 
ATOM   3674 N NE  . ARG D 4 69  ? 28.698 -4.699  -27.808 1.00 19.79  ? 68  ARG E NE  1 
ATOM   3675 C CZ  . ARG D 4 69  ? 28.292 -3.503  -28.217 1.00 21.83  ? 68  ARG E CZ  1 
ATOM   3676 N NH1 . ARG D 4 69  ? 27.140 -3.003  -27.766 1.00 22.14  ? 68  ARG E NH1 1 
ATOM   3677 N NH2 . ARG D 4 69  ? 29.030 -2.807  -29.064 1.00 18.13  ? 68  ARG E NH2 1 
ATOM   3678 N N   . LYS D 4 70  ? 30.351 -7.529  -23.012 1.00 31.61  ? 69  LYS E N   1 
ATOM   3679 C CA  . LYS D 4 70  ? 31.552 -7.305  -22.172 1.00 33.61  ? 69  LYS E CA  1 
ATOM   3680 C C   . LYS D 4 70  ? 32.512 -6.318  -22.835 1.00 30.76  ? 69  LYS E C   1 
ATOM   3681 O O   . LYS D 4 70  ? 33.135 -5.601  -22.136 1.00 35.32  ? 69  LYS E O   1 
ATOM   3682 C CB  . LYS D 4 70  ? 32.269 -8.610  -21.829 1.00 31.73  ? 69  LYS E CB  1 
ATOM   3683 C CG  . LYS D 4 70  ? 31.613 -9.458  -20.760 1.00 39.80  ? 69  LYS E CG  1 
ATOM   3684 C CD  . LYS D 4 70  ? 32.543 -10.465 -20.118 1.00 48.95  ? 69  LYS E CD  1 
ATOM   3685 C CE  . LYS D 4 70  ? 32.202 -11.911 -20.384 1.00 51.10  ? 69  LYS E CE  1 
ATOM   3686 N NZ  . LYS D 4 70  ? 31.554 -12.591 -19.235 1.00 55.53  ? 69  LYS E NZ  1 
ATOM   3687 N N   . GLU D 4 71  ? 32.588 -6.299  -24.144 1.00 24.73  ? 70  GLU E N   1 
ATOM   3688 C CA  . GLU D 4 71  ? 33.450 -5.371  -24.876 1.00 30.11  ? 70  GLU E CA  1 
ATOM   3689 C C   . GLU D 4 71  ? 32.735 -4.902  -26.141 1.00 25.50  ? 70  GLU E C   1 
ATOM   3690 O O   . GLU D 4 71  ? 31.759 -5.508  -26.585 1.00 28.18  ? 70  GLU E O   1 
ATOM   3691 C CB  . GLU D 4 71  ? 34.807 -6.010  -25.232 1.00 32.57  ? 70  GLU E CB  1 
ATOM   3692 C CG  . GLU D 4 71  ? 34.701 -7.320  -25.998 1.00 33.23  ? 70  GLU E CG  1 
ATOM   3693 C CD  . GLU D 4 71  ? 34.729 -8.534  -25.093 1.00 44.67  ? 70  GLU E CD  1 
ATOM   3694 O OE1 . GLU D 4 71  ? 35.256 -8.401  -23.966 1.00 49.14  ? 70  GLU E OE1 1 
ATOM   3695 O OE2 . GLU D 4 71  ? 34.222 -9.616  -25.502 1.00 42.69  ? 70  GLU E OE2 1 
ATOM   3696 N N   . LYS D 4 72  ? 33.196 -3.821  -26.711 1.00 26.99  ? 71  LYS E N   1 
ATOM   3697 C CA  . LYS D 4 72  ? 32.493 -3.195  -27.839 1.00 27.56  ? 71  LYS E CA  1 
ATOM   3698 C C   . LYS D 4 72  ? 32.415 -4.111  -29.053 1.00 30.22  ? 71  LYS E C   1 
ATOM   3699 O O   . LYS D 4 72  ? 31.431 -4.114  -29.709 1.00 24.81  ? 71  LYS E O   1 
ATOM   3700 C CB  . LYS D 4 72  ? 33.189 -1.883  -28.192 1.00 34.76  ? 71  LYS E CB  1 
ATOM   3701 C CG  . LYS D 4 72  ? 32.257 -0.695  -28.355 1.00 36.25  ? 71  LYS E CG  1 
ATOM   3702 C CD  . LYS D 4 72  ? 32.939 0.586   -28.601 1.00 31.14  ? 71  LYS E CD  1 
ATOM   3703 C CE  . LYS D 4 72  ? 32.147 1.775   -28.150 1.00 37.36  ? 71  LYS E CE  1 
ATOM   3704 N NZ  . LYS D 4 72  ? 32.546 2.208   -26.791 1.00 44.63  ? 71  LYS E NZ  1 
ATOM   3705 N N   . ARG D 4 73  ? 33.384 -4.982  -29.185 1.00 27.89  ? 72  ARG E N   1 
ATOM   3706 C CA  . ARG D 4 73  ? 33.574 -5.697  -30.428 1.00 29.37  ? 72  ARG E CA  1 
ATOM   3707 C C   . ARG D 4 73  ? 32.607 -6.863  -30.589 1.00 27.47  ? 72  ARG E C   1 
ATOM   3708 O O   . ARG D 4 73  ? 32.247 -7.178  -31.721 1.00 24.56  ? 72  ARG E O   1 
ATOM   3709 C CB  . ARG D 4 73  ? 35.033 -6.161  -30.512 1.00 35.02  ? 72  ARG E CB  1 
ATOM   3710 C CG  . ARG D 4 73  ? 35.256 -7.402  -31.341 1.00 37.35  ? 72  ARG E CG  1 
ATOM   3711 C CD  . ARG D 4 73  ? 36.692 -7.910  -31.243 1.00 39.60  ? 72  ARG E CD  1 
ATOM   3712 N NE  . ARG D 4 73  ? 37.074 -8.556  -32.499 1.00 40.33  ? 72  ARG E NE  1 
ATOM   3713 C CZ  . ARG D 4 73  ? 36.826 -9.832  -32.782 1.00 43.47  ? 72  ARG E CZ  1 
ATOM   3714 N NH1 . ARG D 4 73  ? 36.211 -10.601 -31.889 1.00 37.14  ? 72  ARG E NH1 1 
ATOM   3715 N NH2 . ARG D 4 73  ? 37.192 -10.340 -33.956 1.00 42.49  ? 72  ARG E NH2 1 
ATOM   3716 N N   . ASN D 4 74  ? 32.141 -7.481  -29.490 1.00 25.18  ? 73  ASN E N   1 
ATOM   3717 C CA  . ASN D 4 74  ? 31.416 -8.749  -29.547 1.00 25.64  ? 73  ASN E CA  1 
ATOM   3718 C C   . ASN D 4 74  ? 30.010 -8.629  -28.963 1.00 27.79  ? 73  ASN E C   1 
ATOM   3719 O O   . ASN D 4 74  ? 29.791 -7.931  -27.963 1.00 23.86  ? 73  ASN E O   1 
ATOM   3720 C CB  . ASN D 4 74  ? 32.160 -9.874  -28.774 1.00 27.91  ? 73  ASN E CB  1 
ATOM   3721 C CG  . ASN D 4 74  ? 33.585 -10.107 -29.285 1.00 32.47  ? 73  ASN E CG  1 
ATOM   3722 O OD1 . ASN D 4 74  ? 33.794 -10.447 -30.447 1.00 31.77  ? 73  ASN E OD1 1 
ATOM   3723 N ND2 . ASN D 4 74  ? 34.565 -9.926  -28.407 1.00 36.36  ? 73  ASN E ND2 1 
ATOM   3724 N N   . PHE D 4 75  ? 29.072 -9.372  -29.562 1.00 21.53  ? 74  PHE E N   1 
ATOM   3725 C CA  . PHE D 4 75  ? 27.681 -9.407  -29.103 1.00 20.47  ? 74  PHE E CA  1 
ATOM   3726 C C   . PHE D 4 75  ? 27.120 -10.800 -29.360 1.00 23.74  ? 74  PHE E C   1 
ATOM   3727 O O   . PHE D 4 75  ? 26.346 -11.015 -30.302 1.00 23.46  ? 74  PHE E O   1 
ATOM   3728 C CB  . PHE D 4 75  ? 26.840 -8.336  -29.812 1.00 22.21  ? 74  PHE E CB  1 
ATOM   3729 C CG  . PHE D 4 75  ? 25.465 -8.121  -29.215 1.00 19.39  ? 74  PHE E CG  1 
ATOM   3730 C CD1 . PHE D 4 75  ? 25.295 -8.044  -27.839 1.00 21.95  ? 74  PHE E CD1 1 
ATOM   3731 C CD2 . PHE D 4 75  ? 24.351 -7.958  -30.037 1.00 19.84  ? 74  PHE E CD2 1 
ATOM   3732 C CE1 . PHE D 4 75  ? 24.040 -7.832  -27.276 1.00 20.78  ? 74  PHE E CE1 1 
ATOM   3733 C CE2 . PHE D 4 75  ? 23.083 -7.748  -29.493 1.00 21.19  ? 74  PHE E CE2 1 
ATOM   3734 C CZ  . PHE D 4 75  ? 22.928 -7.689  -28.089 1.00 21.09  ? 74  PHE E CZ  1 
ATOM   3735 N N   . PRO D 4 76  ? 27.477 -11.777 -28.527 1.00 21.72  ? 75  PRO E N   1 
ATOM   3736 C CA  . PRO D 4 76  ? 27.057 -13.156 -28.793 1.00 22.86  ? 75  PRO E CA  1 
ATOM   3737 C C   . PRO D 4 76  ? 25.590 -13.403 -28.472 1.00 25.05  ? 75  PRO E C   1 
ATOM   3738 O O   . PRO D 4 76  ? 25.007 -12.799 -27.567 1.00 20.76  ? 75  PRO E O   1 
ATOM   3739 C CB  . PRO D 4 76  ? 27.959 -13.981 -27.870 1.00 21.71  ? 75  PRO E CB  1 
ATOM   3740 C CG  . PRO D 4 76  ? 28.229 -13.041 -26.701 1.00 23.13  ? 75  PRO E CG  1 
ATOM   3741 C CD  . PRO D 4 76  ? 28.366 -11.684 -27.350 1.00 22.62  ? 75  PRO E CD  1 
ATOM   3742 N N   . LEU D 4 77  ? 24.997 -14.314 -29.249 1.00 23.45  ? 76  LEU E N   1 
ATOM   3743 C CA  . LEU D 4 77  ? 23.635 -14.790 -29.034 1.00 24.87  ? 76  LEU E CA  1 
ATOM   3744 C C   . LEU D 4 77  ? 23.706 -16.202 -28.461 1.00 23.51  ? 76  LEU E C   1 
ATOM   3745 O O   . LEU D 4 77  ? 24.289 -17.096 -29.075 1.00 22.81  ? 76  LEU E O   1 
ATOM   3746 C CB  . LEU D 4 77  ? 22.832 -14.770 -30.343 1.00 22.26  ? 76  LEU E CB  1 
ATOM   3747 C CG  . LEU D 4 77  ? 21.352 -15.160 -30.237 1.00 24.51  ? 76  LEU E CG  1 
ATOM   3748 C CD1 . LEU D 4 77  ? 20.620 -14.182 -29.321 1.00 18.91  ? 76  LEU E CD1 1 
ATOM   3749 C CD2 . LEU D 4 77  ? 20.687 -15.193 -31.612 1.00 25.37  ? 76  LEU E CD2 1 
ATOM   3750 N N   . ILE D 4 78  ? 23.103 -16.409 -27.302 1.00 22.53  ? 77  ILE E N   1 
ATOM   3751 C CA  . ILE D 4 78  ? 23.215 -17.669 -26.582 1.00 24.35  ? 77  ILE E CA  1 
ATOM   3752 C C   . ILE D 4 78  ? 21.841 -18.318 -26.540 1.00 24.39  ? 77  ILE E C   1 
ATOM   3753 O O   . ILE D 4 78  ? 20.865 -17.683 -26.128 1.00 23.88  ? 77  ILE E O   1 
ATOM   3754 C CB  . ILE D 4 78  ? 23.770 -17.438 -25.167 1.00 22.39  ? 77  ILE E CB  1 
ATOM   3755 C CG1 . ILE D 4 78  ? 25.109 -16.692 -25.255 1.00 28.90  ? 77  ILE E CG1 1 
ATOM   3756 C CG2 . ILE D 4 78  ? 23.907 -18.724 -24.421 1.00 22.40  ? 77  ILE E CG2 1 
ATOM   3757 C CD1 . ILE D 4 78  ? 25.447 -15.889 -23.999 1.00 30.98  ? 77  ILE E CD1 1 
ATOM   3758 N N   . LEU D 4 79  ? 21.768 -19.578 -26.962 1.00 24.65  ? 78  LEU E N   1 
ATOM   3759 C CA  . LEU D 4 79  ? 20.539 -20.373 -26.888 1.00 23.86  ? 78  LEU E CA  1 
ATOM   3760 C C   . LEU D 4 79  ? 20.778 -21.502 -25.891 1.00 27.60  ? 78  LEU E C   1 
ATOM   3761 O O   . LEU D 4 79  ? 21.402 -22.518 -26.225 1.00 27.37  ? 78  LEU E O   1 
ATOM   3762 C CB  . LEU D 4 79  ? 20.155 -20.915 -28.257 1.00 24.14  ? 78  LEU E CB  1 
ATOM   3763 C CG  . LEU D 4 79  ? 19.541 -19.916 -29.239 1.00 23.46  ? 78  LEU E CG  1 
ATOM   3764 C CD1 . LEU D 4 79  ? 20.599 -19.030 -29.858 1.00 18.28  ? 78  LEU E CD1 1 
ATOM   3765 C CD2 . LEU D 4 79  ? 18.771 -20.685 -30.312 1.00 17.68  ? 78  LEU E CD2 1 
ATOM   3766 N N   . GLU D 4 80  ? 20.269 -21.324 -24.668 1.00 28.75  ? 79  GLU E N   1 
ATOM   3767 C CA  . GLU D 4 80  ? 20.543 -22.279 -23.594 1.00 31.27  ? 79  GLU E CA  1 
ATOM   3768 C C   . GLU D 4 80  ? 20.056 -23.679 -23.942 1.00 29.67  ? 79  GLU E C   1 
ATOM   3769 O O   . GLU D 4 80  ? 20.733 -24.675 -23.652 1.00 32.62  ? 79  GLU E O   1 
ATOM   3770 C CB  . GLU D 4 80  ? 19.893 -21.809 -22.293 1.00 32.61  ? 79  GLU E CB  1 
ATOM   3771 C CG  . GLU D 4 80  ? 20.880 -21.262 -21.282 1.00 45.81  ? 79  GLU E CG  1 
ATOM   3772 C CD  . GLU D 4 80  ? 21.709 -22.355 -20.639 1.00 42.94  ? 79  GLU E CD  1 
ATOM   3773 O OE1 . GLU D 4 80  ? 22.942 -22.199 -20.569 1.00 49.93  ? 79  GLU E OE1 1 
ATOM   3774 O OE2 . GLU D 4 80  ? 21.131 -23.377 -20.213 1.00 47.45  ? 79  GLU E OE2 1 
ATOM   3775 N N   . SER D 4 81  ? 18.871 -23.781 -24.529 1.00 26.44  ? 80  SER E N   1 
ATOM   3776 C CA  . SER D 4 81  ? 18.275 -25.074 -24.864 1.00 30.77  ? 80  SER E CA  1 
ATOM   3777 C C   . SER D 4 81  ? 17.493 -24.912 -26.157 1.00 28.46  ? 80  SER E C   1 
ATOM   3778 O O   . SER D 4 81  ? 16.273 -24.700 -26.147 1.00 28.22  ? 80  SER E O   1 
ATOM   3779 C CB  . SER D 4 81  ? 17.377 -25.585 -23.734 1.00 28.70  ? 80  SER E CB  1 
ATOM   3780 O OG  . SER D 4 81  ? 17.129 -26.970 -23.869 1.00 32.24  ? 80  SER E OG  1 
ATOM   3781 N N   . PRO D 4 82  ? 18.171 -24.988 -27.303 1.00 28.30  ? 81  PRO E N   1 
ATOM   3782 C CA  . PRO D 4 82  ? 17.483 -24.758 -28.584 1.00 30.34  ? 81  PRO E CA  1 
ATOM   3783 C C   . PRO D 4 82  ? 16.296 -25.692 -28.786 1.00 29.80  ? 81  PRO E C   1 
ATOM   3784 O O   . PRO D 4 82  ? 16.349 -26.889 -28.485 1.00 27.93  ? 81  PRO E O   1 
ATOM   3785 C CB  . PRO D 4 82  ? 18.575 -25.009 -29.630 1.00 26.75  ? 81  PRO E CB  1 
ATOM   3786 C CG  . PRO D 4 82  ? 19.875 -24.773 -28.876 1.00 27.57  ? 81  PRO E CG  1 
ATOM   3787 C CD  . PRO D 4 82  ? 19.615 -25.249 -27.476 1.00 23.74  ? 81  PRO E CD  1 
ATOM   3788 N N   . SER D 4 83  ? 15.218 -25.130 -29.300 1.00 27.83  ? 82  SER E N   1 
ATOM   3789 C CA  . SER D 4 83  ? 14.016 -25.882 -29.610 1.00 30.24  ? 82  SER E CA  1 
ATOM   3790 C C   . SER D 4 83  ? 13.661 -25.651 -31.071 1.00 28.09  ? 82  SER E C   1 
ATOM   3791 O O   . SER D 4 83  ? 14.102 -24.661 -31.670 1.00 24.96  ? 82  SER E O   1 
ATOM   3792 C CB  . SER D 4 83  ? 12.870 -25.451 -28.686 1.00 29.62  ? 82  SER E CB  1 
ATOM   3793 O OG  . SER D 4 83  ? 12.542 -24.096 -28.923 1.00 39.99  ? 82  SER E OG  1 
ATOM   3794 N N   . PRO D 4 84  ? 12.868 -26.551 -31.677 1.00 25.64  ? 83  PRO E N   1 
ATOM   3795 C CA  . PRO D 4 84  ? 12.579 -26.424 -33.120 1.00 27.14  ? 83  PRO E CA  1 
ATOM   3796 C C   . PRO D 4 84  ? 12.026 -25.070 -33.548 1.00 28.99  ? 83  PRO E C   1 
ATOM   3797 O O   . PRO D 4 84  ? 12.349 -24.609 -34.655 1.00 29.12  ? 83  PRO E O   1 
ATOM   3798 C CB  . PRO D 4 84  ? 11.565 -27.556 -33.380 1.00 29.44  ? 83  PRO E CB  1 
ATOM   3799 C CG  . PRO D 4 84  ? 11.843 -28.571 -32.288 1.00 30.54  ? 83  PRO E CG  1 
ATOM   3800 C CD  . PRO D 4 84  ? 12.261 -27.763 -31.087 1.00 29.47  ? 83  PRO E CD  1 
ATOM   3801 N N   . ASN D 4 85  ? 11.216 -24.404 -32.720 1.00 25.76  ? 84  ASN E N   1 
ATOM   3802 C CA  . ASN D 4 85  ? 10.681 -23.123 -33.177 1.00 25.46  ? 84  ASN E CA  1 
ATOM   3803 C C   . ASN D 4 85  ? 11.708 -21.981 -33.106 1.00 25.83  ? 84  ASN E C   1 
ATOM   3804 O O   . ASN D 4 85  ? 11.356 -20.836 -33.413 1.00 26.71  ? 84  ASN E O   1 
ATOM   3805 C CB  . ASN D 4 85  ? 9.402  -22.765 -32.403 1.00 25.67  ? 84  ASN E CB  1 
ATOM   3806 C CG  . ASN D 4 85  ? 9.650  -22.524 -30.904 1.00 33.42  ? 84  ASN E CG  1 
ATOM   3807 O OD1 . ASN D 4 85  ? 10.790 -22.432 -30.445 1.00 32.18  ? 84  ASN E OD1 1 
ATOM   3808 N ND2 . ASN D 4 85  ? 8.567  -22.421 -30.141 1.00 42.05  ? 84  ASN E ND2 1 
ATOM   3809 N N   . GLN D 4 86  ? 12.960 -22.260 -32.745 1.00 22.40  ? 85  GLN E N   1 
ATOM   3810 C CA  . GLN D 4 86  ? 14.044 -21.299 -32.903 1.00 22.21  ? 85  GLN E CA  1 
ATOM   3811 C C   . GLN D 4 86  ? 14.779 -21.468 -34.237 1.00 24.68  ? 85  GLN E C   1 
ATOM   3812 O O   . GLN D 4 86  ? 15.713 -20.701 -34.539 1.00 22.10  ? 85  GLN E O   1 
ATOM   3813 C CB  . GLN D 4 86  ? 15.004 -21.401 -31.708 1.00 23.04  ? 85  GLN E CB  1 
ATOM   3814 C CG  . GLN D 4 86  ? 14.346 -20.956 -30.373 1.00 21.56  ? 85  GLN E CG  1 
ATOM   3815 C CD  . GLN D 4 86  ? 15.263 -21.076 -29.173 1.00 23.18  ? 85  GLN E CD  1 
ATOM   3816 O OE1 . GLN D 4 86  ? 15.690 -22.167 -28.810 1.00 28.61  ? 85  GLN E OE1 1 
ATOM   3817 N NE2 . GLN D 4 86  ? 15.575 -19.948 -28.554 1.00 21.40  ? 85  GLN E NE2 1 
ATOM   3818 N N   . THR D 4 87  ? 14.366 -22.437 -35.046 1.00 21.30  ? 86  THR E N   1 
ATOM   3819 C CA  . THR D 4 87  ? 14.769 -22.486 -36.448 1.00 22.06  ? 86  THR E CA  1 
ATOM   3820 C C   . THR D 4 87  ? 14.427 -21.172 -37.136 1.00 19.33  ? 86  THR E C   1 
ATOM   3821 O O   . THR D 4 87  ? 13.254 -20.789 -37.212 1.00 21.80  ? 86  THR E O   1 
ATOM   3822 C CB  . THR D 4 87  ? 14.052 -23.647 -37.144 1.00 21.00  ? 86  THR E CB  1 
ATOM   3823 O OG1 . THR D 4 87  ? 14.535 -24.887 -36.616 1.00 23.89  ? 86  THR E OG1 1 
ATOM   3824 C CG2 . THR D 4 87  ? 14.274 -23.601 -38.658 1.00 20.96  ? 86  THR E CG2 1 
ATOM   3825 N N   . SER D 4 88  ? 15.436 -20.468 -37.631 1.00 20.19  ? 87  SER E N   1 
ATOM   3826 C CA  . SER D 4 88  ? 15.172 -19.158 -38.207 1.00 21.22  ? 87  SER E CA  1 
ATOM   3827 C C   . SER D 4 88  ? 16.454 -18.683 -38.876 1.00 21.60  ? 87  SER E C   1 
ATOM   3828 O O   . SER D 4 88  ? 17.490 -19.355 -38.819 1.00 22.78  ? 87  SER E O   1 
ATOM   3829 C CB  . SER D 4 88  ? 14.676 -18.174 -37.128 1.00 21.35  ? 87  SER E CB  1 
ATOM   3830 O OG  . SER D 4 88  ? 14.279 -16.920 -37.672 1.00 25.96  ? 87  SER E OG  1 
ATOM   3831 N N   . LEU D 4 89  ? 16.362 -17.528 -39.532 1.00 18.85  ? 88  LEU E N   1 
ATOM   3832 C CA  . LEU D 4 89  ? 17.507 -16.801 -40.065 1.00 24.47  ? 88  LEU E CA  1 
ATOM   3833 C C   . LEU D 4 89  ? 17.833 -15.626 -39.140 1.00 23.29  ? 88  LEU E C   1 
ATOM   3834 O O   . LEU D 4 89  ? 17.019 -14.708 -38.993 1.00 21.59  ? 88  LEU E O   1 
ATOM   3835 C CB  . LEU D 4 89  ? 17.195 -16.290 -41.471 1.00 17.24  ? 88  LEU E CB  1 
ATOM   3836 C CG  . LEU D 4 89  ? 18.273 -15.503 -42.222 1.00 23.85  ? 88  LEU E CG  1 
ATOM   3837 C CD1 . LEU D 4 89  ? 19.526 -16.337 -42.402 1.00 24.59  ? 88  LEU E CD1 1 
ATOM   3838 C CD2 . LEU D 4 89  ? 17.712 -15.101 -43.598 1.00 27.22  ? 88  LEU E CD2 1 
ATOM   3839 N N   . TYR D 4 90  ? 19.033 -15.626 -38.565 1.00 20.28  ? 89  TYR E N   1 
ATOM   3840 C CA  . TYR D 4 90  ? 19.409 -14.641 -37.552 1.00 18.79  ? 89  TYR E CA  1 
ATOM   3841 C C   . TYR D 4 90  ? 20.345 -13.590 -38.134 1.00 22.25  ? 89  TYR E C   1 
ATOM   3842 O O   . TYR D 4 90  ? 21.339 -13.927 -38.789 1.00 23.81  ? 89  TYR E O   1 
ATOM   3843 C CB  . TYR D 4 90  ? 20.064 -15.325 -36.352 1.00 18.32  ? 89  TYR E CB  1 
ATOM   3844 C CG  . TYR D 4 90  ? 19.098 -16.206 -35.580 1.00 21.75  ? 89  TYR E CG  1 
ATOM   3845 C CD1 . TYR D 4 90  ? 18.781 -17.483 -36.029 1.00 19.64  ? 89  TYR E CD1 1 
ATOM   3846 C CD2 . TYR D 4 90  ? 18.488 -15.752 -34.412 1.00 21.68  ? 89  TYR E CD2 1 
ATOM   3847 C CE1 . TYR D 4 90  ? 17.907 -18.284 -35.337 1.00 20.72  ? 89  TYR E CE1 1 
ATOM   3848 C CE2 . TYR D 4 90  ? 17.604 -16.555 -33.703 1.00 19.74  ? 89  TYR E CE2 1 
ATOM   3849 C CZ  . TYR D 4 90  ? 17.315 -17.819 -34.170 1.00 20.50  ? 89  TYR E CZ  1 
ATOM   3850 O OH  . TYR D 4 90  ? 16.425 -18.619 -33.490 1.00 17.21  ? 89  TYR E OH  1 
ATOM   3851 N N   . PHE D 4 91  ? 20.036 -12.319 -37.878 1.00 19.37  ? 90  PHE E N   1 
ATOM   3852 C CA  . PHE D 4 91  ? 20.839 -11.188 -38.333 1.00 19.50  ? 90  PHE E CA  1 
ATOM   3853 C C   . PHE D 4 91  ? 21.364 -10.411 -37.133 1.00 22.43  ? 90  PHE E C   1 
ATOM   3854 O O   . PHE D 4 91  ? 20.606 -10.082 -36.213 1.00 23.05  ? 90  PHE E O   1 
ATOM   3855 C CB  . PHE D 4 91  ? 20.028 -10.224 -39.212 1.00 22.22  ? 90  PHE E CB  1 
ATOM   3856 C CG  . PHE D 4 91  ? 19.771 -10.726 -40.598 1.00 20.79  ? 90  PHE E CG  1 
ATOM   3857 C CD1 . PHE D 4 91  ? 20.764 -10.674 -41.569 1.00 21.82  ? 90  PHE E CD1 1 
ATOM   3858 C CD2 . PHE D 4 91  ? 18.531 -11.232 -40.941 1.00 22.23  ? 90  PHE E CD2 1 
ATOM   3859 C CE1 . PHE D 4 91  ? 20.531 -11.136 -42.852 1.00 23.76  ? 90  PHE E CE1 1 
ATOM   3860 C CE2 . PHE D 4 91  ? 18.295 -11.707 -42.240 1.00 22.56  ? 90  PHE E CE2 1 
ATOM   3861 C CZ  . PHE D 4 91  ? 19.295 -11.656 -43.182 1.00 19.77  ? 90  PHE E CZ  1 
ATOM   3862 N N   . CYS D 4 92  ? 22.651 -10.112 -37.152 1.00 22.05  ? 91  CYS E N   1 
ATOM   3863 C CA  . CYS D 4 92  ? 23.247 -9.142  -36.253 1.00 22.61  ? 91  CYS E CA  1 
ATOM   3864 C C   . CYS D 4 92  ? 23.428 -7.835  -37.022 1.00 25.67  ? 91  CYS E C   1 
ATOM   3865 O O   . CYS D 4 92  ? 23.865 -7.850  -38.178 1.00 26.51  ? 91  CYS E O   1 
ATOM   3866 C CB  . CYS D 4 92  ? 24.588 -9.670  -35.743 1.00 20.51  ? 91  CYS E CB  1 
ATOM   3867 S SG  . CYS D 4 92  ? 25.410 -8.648  -34.495 1.00 25.61  ? 91  CYS E SG  1 
ATOM   3868 N N   . ALA D 4 93  ? 23.075 -6.719  -36.396 1.00 24.72  ? 92  ALA E N   1 
ATOM   3869 C CA  . ALA D 4 93  ? 23.252 -5.405  -37.001 1.00 26.25  ? 92  ALA E CA  1 
ATOM   3870 C C   . ALA D 4 93  ? 24.061 -4.529  -36.063 1.00 25.43  ? 92  ALA E C   1 
ATOM   3871 O O   . ALA D 4 93  ? 24.047 -4.730  -34.845 1.00 27.04  ? 92  ALA E O   1 
ATOM   3872 C CB  . ALA D 4 93  ? 21.911 -4.721  -37.316 1.00 23.05  ? 92  ALA E CB  1 
ATOM   3873 N N   . SER D 4 94  ? 24.769 -3.554  -36.632 1.00 22.00  ? 93  SER E N   1 
ATOM   3874 C CA  . SER D 4 94  ? 25.517 -2.624  -35.801 1.00 25.85  ? 93  SER E CA  1 
ATOM   3875 C C   . SER D 4 94  ? 25.560 -1.257  -36.466 1.00 25.23  ? 93  SER E C   1 
ATOM   3876 O O   . SER D 4 94  ? 25.368 -1.125  -37.682 1.00 24.35  ? 93  SER E O   1 
ATOM   3877 C CB  . SER D 4 94  ? 26.948 -3.110  -35.517 1.00 24.95  ? 93  SER E CB  1 
ATOM   3878 O OG  . SER D 4 94  ? 27.818 -2.782  -36.591 1.00 30.22  ? 93  SER E OG  1 
ATOM   3879 N N   . SER D 4 95  ? 25.813 -0.240  -35.633 1.00 22.80  ? 94  SER E N   1 
ATOM   3880 C CA  . SER D 4 95  ? 26.032 1.130   -36.082 1.00 24.45  ? 94  SER E CA  1 
ATOM   3881 C C   . SER D 4 95  ? 26.837 1.880   -35.024 1.00 25.43  ? 94  SER E C   1 
ATOM   3882 O O   . SER D 4 95  ? 26.842 1.512   -33.843 1.00 22.65  ? 94  SER E O   1 
ATOM   3883 C CB  . SER D 4 95  ? 24.714 1.856   -36.370 1.00 22.67  ? 94  SER E CB  1 
ATOM   3884 O OG  . SER D 4 95  ? 23.814 1.743   -35.282 1.00 28.19  ? 94  SER E OG  1 
ATOM   3885 N N   . LEU D 4 96  ? 27.517 2.944   -35.475 1.00 25.65  ? 95  LEU E N   1 
ATOM   3886 C CA  . LEU D 4 96  ? 28.397 3.721   -34.603 1.00 26.48  ? 95  LEU E CA  1 
ATOM   3887 C C   . LEU D 4 96  ? 27.675 4.162   -33.339 1.00 26.58  ? 95  LEU E C   1 
ATOM   3888 O O   . LEU D 4 96  ? 28.189 3.993   -32.230 1.00 26.70  ? 95  LEU E O   1 
ATOM   3889 C CB  . LEU D 4 96  ? 28.956 4.933   -35.354 1.00 27.95  ? 95  LEU E CB  1 
ATOM   3890 C CG  . LEU D 4 96  ? 30.114 4.644   -36.313 1.00 33.77  ? 95  LEU E CG  1 
ATOM   3891 C CD1 . LEU D 4 96  ? 30.116 5.607   -37.508 1.00 30.77  ? 95  LEU E CD1 1 
ATOM   3892 C CD2 . LEU D 4 96  ? 31.445 4.700   -35.572 1.00 30.62  ? 95  LEU E CD2 1 
ATOM   3893 N N   . VAL D 4 97  ? 26.458 4.692   -33.483 1.00 26.42  ? 96  VAL E N   1 
ATOM   3894 C CA  . VAL D 4 97  ? 25.637 5.087   -32.347 1.00 24.74  ? 96  VAL E CA  1 
ATOM   3895 C C   . VAL D 4 97  ? 24.237 4.523   -32.544 1.00 26.44  ? 96  VAL E C   1 
ATOM   3896 O O   . VAL D 4 97  ? 23.861 4.115   -33.644 1.00 25.62  ? 96  VAL E O   1 
ATOM   3897 C CB  . VAL D 4 97  ? 25.593 6.621   -32.182 1.00 30.43  ? 96  VAL E CB  1 
ATOM   3898 C CG1 . VAL D 4 97  ? 26.911 7.097   -31.672 1.00 30.20  ? 96  VAL E CG1 1 
ATOM   3899 C CG2 . VAL D 4 97  ? 25.269 7.317   -33.535 1.00 24.73  ? 96  VAL E CG2 1 
ATOM   3900 N N   . SER D 4 98  ? 23.460 4.507   -31.452 1.00 25.85  ? 97  SER E N   1 
ATOM   3901 C CA  . SER D 4 98  ? 22.119 3.926   -31.489 1.00 27.09  ? 97  SER E CA  1 
ATOM   3902 C C   . SER D 4 98  ? 21.103 4.773   -32.256 1.00 24.73  ? 97  SER E C   1 
ATOM   3903 O O   . SER D 4 98  ? 20.023 4.266   -32.558 1.00 27.19  ? 97  SER E O   1 
ATOM   3904 C CB  . SER D 4 98  ? 21.607 3.686   -30.060 1.00 25.84  ? 97  SER E CB  1 
ATOM   3905 O OG  . SER D 4 98  ? 22.631 3.115   -29.263 1.00 30.54  ? 97  SER E OG  1 
ATOM   3906 N N   . THR D 4 99  ? 21.386 6.054   -32.515 1.00 20.65  ? 98  THR E N   1 
ATOM   3907 C CA  . THR D 4 99  ? 20.575 6.892   -33.413 1.00 30.92  ? 98  THR E CA  1 
ATOM   3908 C C   . THR D 4 99  ? 21.520 7.545   -34.415 1.00 25.93  ? 98  THR E C   1 
ATOM   3909 O O   . THR D 4 99  ? 22.004 8.662   -34.194 1.00 26.73  ? 98  THR E O   1 
ATOM   3910 C CB  . THR D 4 99  ? 19.770 7.959   -32.658 1.00 33.65  ? 98  THR E CB  1 
ATOM   3911 O OG1 . THR D 4 99  ? 20.647 8.715   -31.811 1.00 31.69  ? 98  THR E OG1 1 
ATOM   3912 C CG2 . THR D 4 99  ? 18.656 7.324   -31.798 1.00 31.88  ? 98  THR E CG2 1 
ATOM   3913 N N   . PRO D 4 100 ? 21.846 6.853   -35.503 1.00 26.19  ? 99  PRO E N   1 
ATOM   3914 C CA  . PRO D 4 100 ? 22.834 7.380   -36.456 1.00 27.36  ? 99  PRO E CA  1 
ATOM   3915 C C   . PRO D 4 100 ? 22.466 8.752   -37.012 1.00 29.81  ? 99  PRO E C   1 
ATOM   3916 O O   . PRO D 4 100 ? 21.294 9.103   -37.163 1.00 31.02  ? 99  PRO E O   1 
ATOM   3917 C CB  . PRO D 4 100 ? 22.842 6.324   -37.570 1.00 32.43  ? 99  PRO E CB  1 
ATOM   3918 C CG  . PRO D 4 100 ? 22.427 5.045   -36.874 1.00 25.36  ? 99  PRO E CG  1 
ATOM   3919 C CD  . PRO D 4 100 ? 21.433 5.473   -35.818 1.00 27.25  ? 99  PRO E CD  1 
ATOM   3920 N N   . LEU D 4 101 ? 23.507 9.425   -37.437 1.00 31.51  ? 100 LEU E N   1 
ATOM   3921 C CA  . LEU D 4 101 ? 23.437 10.708  -38.152 1.00 37.23  ? 100 LEU E CA  1 
ATOM   3922 C C   . LEU D 4 101 ? 22.925 10.468  -39.577 1.00 43.18  ? 100 LEU E C   1 
ATOM   3923 O O   . LEU D 4 101 ? 22.976 9.348   -40.075 1.00 37.95  ? 100 LEU E O   1 
ATOM   3924 C CB  . LEU D 4 101 ? 24.840 11.292  -38.188 1.00 31.59  ? 100 LEU E CB  1 
ATOM   3925 C CG  . LEU D 4 101 ? 25.401 11.721  -36.846 1.00 33.80  ? 100 LEU E CG  1 
ATOM   3926 C CD1 . LEU D 4 101 ? 26.847 12.078  -36.978 1.00 32.55  ? 100 LEU E CD1 1 
ATOM   3927 C CD2 . LEU D 4 101 ? 24.629 12.876  -36.278 1.00 29.02  ? 100 LEU E CD2 1 
ATOM   3928 N N   . PRO D 4 102 ? 22.540 11.543  -40.278 1.00 49.56  ? 101 PRO E N   1 
ATOM   3929 C CA  . PRO D 4 102 ? 21.951 11.488  -41.604 1.00 48.50  ? 101 PRO E CA  1 
ATOM   3930 C C   . PRO D 4 102 ? 22.551 10.509  -42.611 1.00 42.01  ? 101 PRO E C   1 
ATOM   3931 O O   . PRO D 4 102 ? 21.857 9.705   -43.103 1.00 45.44  ? 101 PRO E O   1 
ATOM   3932 C CB  . PRO D 4 102 ? 22.222 12.900  -42.114 1.00 51.01  ? 101 PRO E CB  1 
ATOM   3933 C CG  . PRO D 4 102 ? 22.050 13.733  -40.905 1.00 45.91  ? 101 PRO E CG  1 
ATOM   3934 C CD  . PRO D 4 102 ? 22.724 12.917  -39.837 1.00 48.92  ? 101 PRO E CD  1 
ATOM   3935 N N   . LYS D 4 103 ? 23.842 10.602  -42.817 1.00 48.02  ? 102 LYS E N   1 
ATOM   3936 C CA  . LYS D 4 103 ? 24.532 9.774   -43.817 1.00 49.59  ? 102 LYS E CA  1 
ATOM   3937 C C   . LYS D 4 103 ? 25.214 8.577   -43.164 1.00 45.21  ? 102 LYS E C   1 
ATOM   3938 O O   . LYS D 4 103 ? 26.183 8.114   -43.708 1.00 41.91  ? 102 LYS E O   1 
ATOM   3939 C CB  . LYS D 4 103 ? 25.681 10.627  -44.339 1.00 54.32  ? 102 LYS E CB  1 
ATOM   3940 C CG  . LYS D 4 103 ? 26.811 10.794  -43.331 1.00 45.98  ? 102 LYS E CG  1 
ATOM   3941 C CD  . LYS D 4 103 ? 26.347 11.198  -41.961 1.00 53.63  ? 102 LYS E CD  1 
ATOM   3942 C CE  . LYS D 4 103 ? 27.062 12.400  -41.403 1.00 48.33  ? 102 LYS E CE  1 
ATOM   3943 N NZ  . LYS D 4 103 ? 26.086 13.443  -41.039 1.00 50.48  ? 102 LYS E NZ  1 
ATOM   3944 N N   . GLU D 4 104 ? 24.728 8.131   -42.022 1.00 40.06  ? 103 GLU E N   1 
ATOM   3945 C CA  . GLU D 4 104 ? 25.383 7.005   -41.336 1.00 36.31  ? 103 GLU E CA  1 
ATOM   3946 C C   . GLU D 4 104 ? 24.572 5.755   -41.620 1.00 31.75  ? 103 GLU E C   1 
ATOM   3947 O O   . GLU D 4 104 ? 23.395 5.845   -41.708 1.00 31.75  ? 103 GLU E O   1 
ATOM   3948 C CB  . GLU D 4 104 ? 25.680 7.315   -39.878 1.00 33.50  ? 103 GLU E CB  1 
ATOM   3949 C CG  . GLU D 4 104 ? 26.904 8.168   -39.738 1.00 33.43  ? 103 GLU E CG  1 
ATOM   3950 C CD  . GLU D 4 104 ? 27.320 8.479   -38.327 1.00 33.59  ? 103 GLU E CD  1 
ATOM   3951 O OE1 . GLU D 4 104 ? 28.427 8.803   -38.138 1.00 37.95  ? 103 GLU E OE1 1 
ATOM   3952 O OE2 . GLU D 4 104 ? 26.523 8.372   -37.470 1.00 33.99  ? 103 GLU E OE2 1 
ATOM   3953 N N   . THR D 4 105 ? 25.282 4.659   -41.731 1.00 26.56  ? 104 THR E N   1 
ATOM   3954 C CA  . THR D 4 105 ? 24.771 3.370   -42.161 1.00 32.99  ? 104 THR E CA  1 
ATOM   3955 C C   . THR D 4 105 ? 24.460 2.482   -40.958 1.00 35.10  ? 104 THR E C   1 
ATOM   3956 O O   . THR D 4 105 ? 25.150 2.543   -39.940 1.00 32.23  ? 104 THR E O   1 
ATOM   3957 C CB  . THR D 4 105 ? 25.844 2.703   -43.035 1.00 29.37  ? 104 THR E CB  1 
ATOM   3958 O OG1 . THR D 4 105 ? 25.865 3.323   -44.317 1.00 44.54  ? 104 THR E OG1 1 
ATOM   3959 C CG2 . THR D 4 105 ? 25.637 1.192   -43.182 1.00 30.14  ? 104 THR E CG2 1 
ATOM   3960 N N   . GLN D 4 106 ? 23.411 1.658   -41.078 1.00 30.92  ? 105 GLN E N   1 
ATOM   3961 C CA  . GLN D 4 106 ? 23.297 0.445   -40.276 1.00 27.85  ? 105 GLN E CA  1 
ATOM   3962 C C   . GLN D 4 106 ? 23.916 -0.712  -41.047 1.00 28.36  ? 105 GLN E C   1 
ATOM   3963 O O   . GLN D 4 106 ? 23.533 -0.968  -42.194 1.00 29.58  ? 105 GLN E O   1 
ATOM   3964 C CB  . GLN D 4 106 ? 21.847 0.092   -39.953 1.00 30.53  ? 105 GLN E CB  1 
ATOM   3965 C CG  . GLN D 4 106 ? 21.067 1.128   -39.220 1.00 37.71  ? 105 GLN E CG  1 
ATOM   3966 C CD  . GLN D 4 106 ? 19.650 0.656   -38.938 1.00 45.28  ? 105 GLN E CD  1 
ATOM   3967 O OE1 . GLN D 4 106 ? 19.366 -0.549  -38.936 1.00 40.11  ? 105 GLN E OE1 1 
ATOM   3968 N NE2 . GLN D 4 106 ? 18.752 1.608   -38.689 1.00 47.51  ? 105 GLN E NE2 1 
ATOM   3969 N N   . TYR D 4 107 ? 24.852 -1.415  -40.416 1.00 25.61  ? 106 TYR E N   1 
ATOM   3970 C CA  . TYR D 4 107 ? 25.545 -2.539  -41.025 1.00 24.69  ? 106 TYR E CA  1 
ATOM   3971 C C   . TYR D 4 107 ? 24.871 -3.830  -40.594 1.00 26.61  ? 106 TYR E C   1 
ATOM   3972 O O   . TYR D 4 107 ? 24.505 -3.967  -39.428 1.00 24.17  ? 106 TYR E O   1 
ATOM   3973 C CB  . TYR D 4 107 ? 27.014 -2.572  -40.600 1.00 25.42  ? 106 TYR E CB  1 
ATOM   3974 C CG  . TYR D 4 107 ? 27.810 -1.399  -41.084 1.00 27.27  ? 106 TYR E CG  1 
ATOM   3975 C CD1 . TYR D 4 107 ? 27.751 -0.180  -40.426 1.00 29.35  ? 106 TYR E CD1 1 
ATOM   3976 C CD2 . TYR D 4 107 ? 28.622 -1.505  -42.207 1.00 30.00  ? 106 TYR E CD2 1 
ATOM   3977 C CE1 . TYR D 4 107 ? 28.482 0.912   -40.874 1.00 32.12  ? 106 TYR E CE1 1 
ATOM   3978 C CE2 . TYR D 4 107 ? 29.353 -0.427  -42.664 1.00 33.52  ? 106 TYR E CE2 1 
ATOM   3979 C CZ  . TYR D 4 107 ? 29.281 0.780   -41.993 1.00 36.00  ? 106 TYR E CZ  1 
ATOM   3980 O OH  . TYR D 4 107 ? 29.999 1.863   -42.448 1.00 41.98  ? 106 TYR E OH  1 
ATOM   3981 N N   . PHE D 4 108 ? 24.734 -4.786  -41.526 1.00 23.95  ? 107 PHE E N   1 
ATOM   3982 C CA  . PHE D 4 108 ? 24.198 -6.107  -41.208 1.00 25.28  ? 107 PHE E CA  1 
ATOM   3983 C C   . PHE D 4 108 ? 25.228 -7.198  -41.470 1.00 25.89  ? 107 PHE E C   1 
ATOM   3984 O O   . PHE D 4 108 ? 25.999 -7.127  -42.436 1.00 25.25  ? 107 PHE E O   1 
ATOM   3985 C CB  . PHE D 4 108 ? 22.926 -6.421  -42.016 1.00 27.06  ? 107 PHE E CB  1 
ATOM   3986 C CG  . PHE D 4 108 ? 21.697 -5.729  -41.493 1.00 25.79  ? 107 PHE E CG  1 
ATOM   3987 C CD1 . PHE D 4 108 ? 21.428 -4.411  -41.844 1.00 28.35  ? 107 PHE E CD1 1 
ATOM   3988 C CD2 . PHE D 4 108 ? 20.813 -6.389  -40.673 1.00 22.88  ? 107 PHE E CD2 1 
ATOM   3989 C CE1 . PHE D 4 108 ? 20.296 -3.763  -41.373 1.00 27.68  ? 107 PHE E CE1 1 
ATOM   3990 C CE2 . PHE D 4 108 ? 19.686 -5.751  -40.187 1.00 25.76  ? 107 PHE E CE2 1 
ATOM   3991 C CZ  . PHE D 4 108 ? 19.423 -4.436  -40.540 1.00 28.88  ? 107 PHE E CZ  1 
ATOM   3992 N N   . GLY D 4 109 ? 25.229 -8.210  -40.604 1.00 22.62  ? 108 GLY E N   1 
ATOM   3993 C CA  . GLY D 4 109 ? 25.963 -9.424  -40.864 1.00 21.48  ? 108 GLY E CA  1 
ATOM   3994 C C   . GLY D 4 109 ? 25.257 -10.265 -41.905 1.00 22.80  ? 108 GLY E C   1 
ATOM   3995 O O   . GLY D 4 109 ? 24.100 -10.026 -42.270 1.00 20.02  ? 108 GLY E O   1 
ATOM   3996 N N   . PRO D 4 110 ? 25.963 -11.280 -42.411 1.00 23.11  ? 109 PRO E N   1 
ATOM   3997 C CA  . PRO D 4 110 ? 25.445 -12.038 -43.568 1.00 23.69  ? 109 PRO E CA  1 
ATOM   3998 C C   . PRO D 4 110 ? 24.241 -12.918 -43.254 1.00 24.11  ? 109 PRO E C   1 
ATOM   3999 O O   . PRO D 4 110 ? 23.606 -13.408 -44.196 1.00 31.07  ? 109 PRO E O   1 
ATOM   4000 C CB  . PRO D 4 110 ? 26.651 -12.892 -43.994 1.00 22.06  ? 109 PRO E CB  1 
ATOM   4001 C CG  . PRO D 4 110 ? 27.386 -13.129 -42.679 1.00 27.17  ? 109 PRO E CG  1 
ATOM   4002 C CD  . PRO D 4 110 ? 27.251 -11.811 -41.919 1.00 22.81  ? 109 PRO E CD  1 
ATOM   4003 N N   . GLY D 4 111 ? 23.907 -13.126 -41.990 1.00 23.02  ? 110 GLY E N   1 
ATOM   4004 C CA  . GLY D 4 111 ? 22.868 -14.058 -41.596 1.00 24.03  ? 110 GLY E CA  1 
ATOM   4005 C C   . GLY D 4 111 ? 23.434 -15.367 -41.054 1.00 22.64  ? 110 GLY E C   1 
ATOM   4006 O O   . GLY D 4 111 ? 24.508 -15.824 -41.448 1.00 25.60  ? 110 GLY E O   1 
ATOM   4007 N N   . THR D 4 112 ? 22.708 -15.969 -40.110 1.00 22.15  ? 111 THR E N   1 
ATOM   4008 C CA  . THR D 4 112 ? 22.992 -17.312 -39.609 1.00 23.55  ? 111 THR E CA  1 
ATOM   4009 C C   . THR D 4 112 ? 21.730 -18.141 -39.814 1.00 25.30  ? 111 THR E C   1 
ATOM   4010 O O   . THR D 4 112 ? 20.695 -17.860 -39.204 1.00 26.09  ? 111 THR E O   1 
ATOM   4011 C CB  . THR D 4 112 ? 23.384 -17.304 -38.127 1.00 22.36  ? 111 THR E CB  1 
ATOM   4012 O OG1 . THR D 4 112 ? 24.687 -16.738 -37.976 1.00 27.61  ? 111 THR E OG1 1 
ATOM   4013 C CG2 . THR D 4 112 ? 23.386 -18.742 -37.544 1.00 20.49  ? 111 THR E CG2 1 
ATOM   4014 N N   . ARG D 4 113 ? 21.815 -19.154 -40.654 1.00 25.31  ? 112 ARG E N   1 
ATOM   4015 C CA  . ARG D 4 113 ? 20.699 -20.088 -40.888 1.00 22.15  ? 112 ARG E CA  1 
ATOM   4016 C C   . ARG D 4 113 ? 20.781 -21.136 -39.780 1.00 24.01  ? 112 ARG E C   1 
ATOM   4017 O O   . ARG D 4 113 ? 21.691 -21.875 -39.756 1.00 22.18  ? 112 ARG E O   1 
ATOM   4018 C CB  . ARG D 4 113 ? 20.768 -20.656 -42.308 1.00 24.69  ? 112 ARG E CB  1 
ATOM   4019 C CG  . ARG D 4 113 ? 19.693 -20.174 -43.264 1.00 27.12  ? 112 ARG E CG  1 
ATOM   4020 C CD  . ARG D 4 113 ? 18.336 -20.894 -43.324 1.00 38.38  ? 112 ARG E CD  1 
ATOM   4021 N NE  . ARG D 4 113 ? 17.563 -20.905 -42.083 1.00 47.50  ? 112 ARG E NE  1 
ATOM   4022 C CZ  . ARG D 4 113 ? 17.040 -21.972 -41.486 1.00 48.70  ? 112 ARG E CZ  1 
ATOM   4023 N NH1 . ARG D 4 113 ? 17.062 -23.186 -42.035 1.00 47.60  ? 112 ARG E NH1 1 
ATOM   4024 N NH2 . ARG D 4 113 ? 16.430 -21.791 -40.355 1.00 45.59  ? 112 ARG E NH2 1 
ATOM   4025 N N   . LEU D 4 114 ? 19.869 -21.101 -38.841 1.00 22.97  ? 113 LEU E N   1 
ATOM   4026 C CA  . LEU D 4 114 ? 19.893 -22.053 -37.742 1.00 23.97  ? 113 LEU E CA  1 
ATOM   4027 C C   . LEU D 4 114 ? 18.722 -23.000 -37.922 1.00 27.15  ? 113 LEU E C   1 
ATOM   4028 O O   . LEU D 4 114 ? 17.586 -22.553 -38.126 1.00 24.94  ? 113 LEU E O   1 
ATOM   4029 C CB  . LEU D 4 114 ? 19.809 -21.341 -36.391 1.00 21.03  ? 113 LEU E CB  1 
ATOM   4030 C CG  . LEU D 4 114 ? 19.673 -22.268 -35.180 1.00 24.59  ? 113 LEU E CG  1 
ATOM   4031 C CD1 . LEU D 4 114 ? 20.889 -23.196 -35.042 1.00 26.61  ? 113 LEU E CD1 1 
ATOM   4032 C CD2 . LEU D 4 114 ? 19.468 -21.452 -33.896 1.00 22.21  ? 113 LEU E CD2 1 
ATOM   4033 N N   . LEU D 4 115 ? 19.005 -24.294 -37.903 1.00 23.00  ? 114 LEU E N   1 
ATOM   4034 C CA  . LEU D 4 115 ? 17.972 -25.316 -37.979 1.00 23.70  ? 114 LEU E CA  1 
ATOM   4035 C C   . LEU D 4 115 ? 18.095 -26.219 -36.757 1.00 23.19  ? 114 LEU E C   1 
ATOM   4036 O O   . LEU D 4 115 ? 19.141 -26.839 -36.539 1.00 21.84  ? 114 LEU E O   1 
ATOM   4037 C CB  . LEU D 4 115 ? 18.103 -26.116 -39.278 1.00 21.44  ? 114 LEU E CB  1 
ATOM   4038 C CG  . LEU D 4 115 ? 17.173 -27.317 -39.406 1.00 23.70  ? 114 LEU E CG  1 
ATOM   4039 C CD1 . LEU D 4 115 ? 15.724 -26.868 -39.306 1.00 19.80  ? 114 LEU E CD1 1 
ATOM   4040 C CD2 . LEU D 4 115 ? 17.437 -28.097 -40.708 1.00 20.99  ? 114 LEU E CD2 1 
ATOM   4041 N N   . VAL D 4 116 ? 17.033 -26.296 -35.963 1.00 22.58  ? 115 VAL E N   1 
ATOM   4042 C CA  . VAL D 4 116 ? 17.003 -27.147 -34.779 1.00 22.38  ? 115 VAL E CA  1 
ATOM   4043 C C   . VAL D 4 116 ? 16.104 -28.347 -35.069 1.00 26.07  ? 115 VAL E C   1 
ATOM   4044 O O   . VAL D 4 116 ? 14.924 -28.181 -35.405 1.00 22.68  ? 115 VAL E O   1 
ATOM   4045 C CB  . VAL D 4 116 ? 16.517 -26.380 -33.542 1.00 21.95  ? 115 VAL E CB  1 
ATOM   4046 C CG1 . VAL D 4 116 ? 16.662 -27.242 -32.296 1.00 21.37  ? 115 VAL E CG1 1 
ATOM   4047 C CG2 . VAL D 4 116 ? 17.296 -25.097 -33.391 1.00 22.20  ? 115 VAL E CG2 1 
ATOM   4048 N N   . LEU D 4 117 ? 16.656 -29.552 -34.906 1.00 25.71  ? 116 LEU E N   1 
ATOM   4049 C CA  . LEU D 4 117 ? 15.989 -30.794 -35.276 1.00 26.57  ? 116 LEU E CA  1 
ATOM   4050 C C   . LEU D 4 117 ? 16.030 -31.806 -34.134 1.00 31.42  ? 116 LEU E C   1 
ATOM   4051 O O   . LEU D 4 117 ? 16.963 -31.830 -33.324 1.00 28.92  ? 116 LEU E O   1 
ATOM   4052 C CB  . LEU D 4 117 ? 16.643 -31.440 -36.506 1.00 26.36  ? 116 LEU E CB  1 
ATOM   4053 C CG  . LEU D 4 117 ? 16.672 -30.704 -37.839 1.00 26.92  ? 116 LEU E CG  1 
ATOM   4054 C CD1 . LEU D 4 117 ? 17.518 -31.498 -38.826 1.00 25.41  ? 116 LEU E CD1 1 
ATOM   4055 C CD2 . LEU D 4 117 ? 15.257 -30.442 -38.392 1.00 29.14  ? 116 LEU E CD2 1 
ATOM   4056 N N   . GLU D 4 118 ? 15.023 -32.684 -34.116 1.00 33.55  ? 117 GLU E N   1 
ATOM   4057 C CA  . GLU D 4 118 ? 15.014 -33.794 -33.165 1.00 34.30  ? 117 GLU E CA  1 
ATOM   4058 C C   . GLU D 4 118 ? 16.243 -34.693 -33.337 1.00 34.11  ? 117 GLU E C   1 
ATOM   4059 O O   . GLU D 4 118 ? 16.830 -35.160 -32.351 1.00 37.53  ? 117 GLU E O   1 
ATOM   4060 C CB  . GLU D 4 118 ? 13.715 -34.581 -33.323 1.00 31.45  ? 117 GLU E CB  1 
ATOM   4061 C CG  . GLU D 4 118 ? 13.710 -35.929 -32.608 1.00 48.79  ? 117 GLU E CG  1 
ATOM   4062 C CD  . GLU D 4 118 ? 12.332 -36.571 -32.571 1.00 50.24  ? 117 GLU E CD  1 
ATOM   4063 O OE1 . GLU D 4 118 ? 11.884 -36.943 -31.463 1.00 58.79  ? 117 GLU E OE1 1 
ATOM   4064 O OE2 . GLU D 4 118 ? 11.701 -36.695 -33.646 1.00 55.37  ? 117 GLU E OE2 1 
ATOM   4065 N N   . ASP D 4 119 ? 16.658 -34.936 -34.574 1.00 30.45  ? 118 ASP E N   1 
ATOM   4066 C CA  . ASP D 4 119 ? 17.913 -35.634 -34.830 1.00 31.31  ? 118 ASP E CA  1 
ATOM   4067 C C   . ASP D 4 119 ? 18.362 -35.277 -36.238 1.00 35.28  ? 118 ASP E C   1 
ATOM   4068 O O   . ASP D 4 119 ? 17.613 -34.669 -37.009 1.00 31.89  ? 118 ASP E O   1 
ATOM   4069 C CB  . ASP D 4 119 ? 17.763 -37.152 -34.646 1.00 35.60  ? 118 ASP E CB  1 
ATOM   4070 C CG  . ASP D 4 119 ? 16.738 -37.751 -35.584 1.00 38.79  ? 118 ASP E CG  1 
ATOM   4071 O OD1 . ASP D 4 119 ? 16.923 -37.651 -36.815 1.00 41.46  ? 118 ASP E OD1 1 
ATOM   4072 O OD2 . ASP D 4 119 ? 15.737 -38.315 -35.097 1.00 49.27  ? 118 ASP E OD2 1 
ATOM   4073 N N   . LEU D 4 120 ? 19.590 -35.687 -36.577 1.00 33.71  ? 119 LEU E N   1 
ATOM   4074 C CA  . LEU D 4 120 ? 20.226 -35.309 -37.834 1.00 32.26  ? 119 LEU E CA  1 
ATOM   4075 C C   . LEU D 4 120 ? 20.062 -36.365 -38.923 1.00 35.44  ? 119 LEU E C   1 
ATOM   4076 O O   . LEU D 4 120 ? 20.792 -36.334 -39.922 1.00 33.31  ? 119 LEU E O   1 
ATOM   4077 C CB  . LEU D 4 120 ? 21.711 -35.027 -37.609 1.00 34.29  ? 119 LEU E CB  1 
ATOM   4078 C CG  . LEU D 4 120 ? 22.076 -34.001 -36.529 1.00 39.40  ? 119 LEU E CG  1 
ATOM   4079 C CD1 . LEU D 4 120 ? 23.583 -33.813 -36.455 1.00 35.44  ? 119 LEU E CD1 1 
ATOM   4080 C CD2 . LEU D 4 120 ? 21.401 -32.676 -36.795 1.00 29.08  ? 119 LEU E CD2 1 
ATOM   4081 N N   . LYS D 4 121 ? 19.110 -37.284 -38.761 1.00 32.19  ? 120 LYS E N   1 
ATOM   4082 C CA  . LYS D 4 121 ? 19.003 -38.435 -39.649 1.00 34.69  ? 120 LYS E CA  1 
ATOM   4083 C C   . LYS D 4 121 ? 18.536 -38.080 -41.055 1.00 34.40  ? 120 LYS E C   1 
ATOM   4084 O O   . LYS D 4 121 ? 18.785 -38.861 -41.975 1.00 30.98  ? 120 LYS E O   1 
ATOM   4085 C CB  . LYS D 4 121 ? 18.059 -39.478 -39.044 1.00 37.48  ? 120 LYS E CB  1 
ATOM   4086 C CG  . LYS D 4 121 ? 18.796 -40.566 -38.240 1.00 50.96  ? 120 LYS E CG  1 
ATOM   4087 C CD  . LYS D 4 121 ? 17.926 -41.215 -37.143 1.00 52.24  ? 120 LYS E CD  1 
ATOM   4088 C CE  . LYS D 4 121 ? 18.801 -41.920 -36.096 1.00 50.52  ? 120 LYS E CE  1 
ATOM   4089 N NZ  . LYS D 4 121 ? 18.972 -41.106 -34.842 1.00 56.42  ? 120 LYS E NZ  1 
ATOM   4090 N N   . ASN D 4 122 ? 17.892 -36.931 -41.255 1.00 29.79  ? 121 ASN E N   1 
ATOM   4091 C CA  . ASN D 4 122 ? 17.397 -36.556 -42.572 1.00 34.50  ? 121 ASN E CA  1 
ATOM   4092 C C   . ASN D 4 122 ? 18.352 -35.669 -43.364 1.00 31.52  ? 121 ASN E C   1 
ATOM   4093 O O   . ASN D 4 122 ? 18.002 -35.260 -44.471 1.00 31.39  ? 121 ASN E O   1 
ATOM   4094 C CB  . ASN D 4 122 ? 16.042 -35.850 -42.443 1.00 36.06  ? 121 ASN E CB  1 
ATOM   4095 C CG  . ASN D 4 122 ? 14.895 -36.827 -42.265 1.00 42.87  ? 121 ASN E CG  1 
ATOM   4096 O OD1 . ASN D 4 122 ? 14.957 -37.970 -42.725 1.00 44.90  ? 121 ASN E OD1 1 
ATOM   4097 N ND2 . ASN D 4 122 ? 13.836 -36.380 -41.598 1.00 43.88  ? 121 ASN E ND2 1 
ATOM   4098 N N   . VAL D 4 123 ? 19.543 -35.373 -42.847 1.00 31.98  ? 122 VAL E N   1 
ATOM   4099 C CA  . VAL D 4 123 ? 20.472 -34.476 -43.537 1.00 29.40  ? 122 VAL E CA  1 
ATOM   4100 C C   . VAL D 4 123 ? 21.117 -35.213 -44.705 1.00 30.65  ? 122 VAL E C   1 
ATOM   4101 O O   . VAL D 4 123 ? 21.692 -36.297 -44.530 1.00 30.28  ? 122 VAL E O   1 
ATOM   4102 C CB  . VAL D 4 123 ? 21.526 -33.929 -42.559 1.00 27.63  ? 122 VAL E CB  1 
ATOM   4103 C CG1 . VAL D 4 123 ? 22.568 -33.069 -43.296 1.00 23.72  ? 122 VAL E CG1 1 
ATOM   4104 C CG2 . VAL D 4 123 ? 20.836 -33.123 -41.464 1.00 23.17  ? 122 VAL E CG2 1 
ATOM   4105 N N   . PHE D 4 124 ? 21.044 -34.608 -45.900 1.00 28.25  ? 123 PHE E N   1 
ATOM   4106 C CA  . PHE D 4 124 ? 21.443 -35.227 -47.178 1.00 27.13  ? 123 PHE E CA  1 
ATOM   4107 C C   . PHE D 4 124 ? 22.203 -34.237 -48.062 1.00 25.58  ? 123 PHE E C   1 
ATOM   4108 O O   . PHE D 4 124 ? 21.670 -33.162 -48.369 1.00 24.34  ? 123 PHE E O   1 
ATOM   4109 C CB  . PHE D 4 124 ? 20.208 -35.721 -47.945 1.00 30.36  ? 123 PHE E CB  1 
ATOM   4110 C CG  . PHE D 4 124 ? 19.727 -37.067 -47.540 1.00 35.24  ? 123 PHE E CG  1 
ATOM   4111 C CD1 . PHE D 4 124 ? 20.322 -38.212 -48.048 1.00 40.21  ? 123 PHE E CD1 1 
ATOM   4112 C CD2 . PHE D 4 124 ? 18.637 -37.192 -46.682 1.00 39.03  ? 123 PHE E CD2 1 
ATOM   4113 C CE1 . PHE D 4 124 ? 19.851 -39.470 -47.680 1.00 44.10  ? 123 PHE E CE1 1 
ATOM   4114 C CE2 . PHE D 4 124 ? 18.163 -38.436 -46.307 1.00 40.41  ? 123 PHE E CE2 1 
ATOM   4115 C CZ  . PHE D 4 124 ? 18.769 -39.578 -46.806 1.00 45.11  ? 123 PHE E CZ  1 
ATOM   4116 N N   . PRO D 4 125 ? 23.399 -34.578 -48.535 1.00 22.71  ? 124 PRO E N   1 
ATOM   4117 C CA  . PRO D 4 125 ? 24.102 -33.699 -49.488 1.00 23.65  ? 124 PRO E CA  1 
ATOM   4118 C C   . PRO D 4 125 ? 23.423 -33.744 -50.849 1.00 29.03  ? 124 PRO E C   1 
ATOM   4119 O O   . PRO D 4 125 ? 22.669 -34.681 -51.143 1.00 24.25  ? 124 PRO E O   1 
ATOM   4120 C CB  . PRO D 4 125 ? 25.506 -34.307 -49.548 1.00 23.30  ? 124 PRO E CB  1 
ATOM   4121 C CG  . PRO D 4 125 ? 25.243 -35.827 -49.343 1.00 18.90  ? 124 PRO E CG  1 
ATOM   4122 C CD  . PRO D 4 125 ? 24.068 -35.885 -48.370 1.00 22.42  ? 124 PRO E CD  1 
ATOM   4123 N N   . PRO D 4 126 ? 23.642 -32.753 -51.705 1.00 28.68  ? 125 PRO E N   1 
ATOM   4124 C CA  . PRO D 4 126 ? 23.005 -32.774 -53.023 1.00 26.80  ? 125 PRO E CA  1 
ATOM   4125 C C   . PRO D 4 126 ? 23.764 -33.636 -54.021 1.00 28.66  ? 125 PRO E C   1 
ATOM   4126 O O   . PRO D 4 126 ? 24.960 -33.917 -53.879 1.00 25.20  ? 125 PRO E O   1 
ATOM   4127 C CB  . PRO D 4 126 ? 23.041 -31.302 -53.454 1.00 25.46  ? 125 PRO E CB  1 
ATOM   4128 C CG  . PRO D 4 126 ? 24.299 -30.793 -52.842 1.00 25.64  ? 125 PRO E CG  1 
ATOM   4129 C CD  . PRO D 4 126 ? 24.421 -31.516 -51.497 1.00 25.22  ? 125 PRO E CD  1 
ATOM   4130 N N   . GLU D 4 127 ? 23.031 -34.051 -55.050 1.00 25.56  ? 126 GLU E N   1 
ATOM   4131 C CA  . GLU D 4 127 ? 23.624 -34.523 -56.290 1.00 32.15  ? 126 GLU E CA  1 
ATOM   4132 C C   . GLU D 4 127 ? 23.534 -33.399 -57.306 1.00 23.95  ? 126 GLU E C   1 
ATOM   4133 O O   . GLU D 4 127 ? 22.564 -32.637 -57.308 1.00 24.97  ? 126 GLU E O   1 
ATOM   4134 C CB  . GLU D 4 127 ? 22.916 -35.777 -56.808 1.00 29.19  ? 126 GLU E CB  1 
ATOM   4135 C CG  . GLU D 4 127 ? 23.188 -37.001 -55.953 1.00 35.38  ? 126 GLU E CG  1 
ATOM   4136 C CD  . GLU D 4 127 ? 22.297 -38.173 -56.335 1.00 46.60  ? 126 GLU E CD  1 
ATOM   4137 O OE1 . GLU D 4 127 ? 21.751 -38.159 -57.459 1.00 43.42  ? 126 GLU E OE1 1 
ATOM   4138 O OE2 . GLU D 4 127 ? 22.150 -39.106 -55.518 1.00 53.57  ? 126 GLU E OE2 1 
ATOM   4139 N N   . VAL D 4 128 ? 24.555 -33.275 -58.151 1.00 23.82  ? 127 VAL E N   1 
ATOM   4140 C CA  . VAL D 4 128 ? 24.650 -32.146 -59.069 1.00 24.11  ? 127 VAL E CA  1 
ATOM   4141 C C   . VAL D 4 128 ? 24.829 -32.676 -60.485 1.00 23.92  ? 127 VAL E C   1 
ATOM   4142 O O   . VAL D 4 128 ? 25.645 -33.572 -60.719 1.00 24.97  ? 127 VAL E O   1 
ATOM   4143 C CB  . VAL D 4 128 ? 25.805 -31.198 -58.686 1.00 22.64  ? 127 VAL E CB  1 
ATOM   4144 C CG1 . VAL D 4 128 ? 25.920 -30.046 -59.696 1.00 19.02  ? 127 VAL E CG1 1 
ATOM   4145 C CG2 . VAL D 4 128 ? 25.590 -30.666 -57.278 1.00 24.25  ? 127 VAL E CG2 1 
ATOM   4146 N N   . ALA D 4 129 ? 24.074 -32.123 -61.431 1.00 24.06  ? 128 ALA E N   1 
ATOM   4147 C CA  . ALA D 4 129 ? 24.193 -32.544 -62.819 1.00 26.20  ? 128 ALA E CA  1 
ATOM   4148 C C   . ALA D 4 129 ? 24.116 -31.320 -63.717 1.00 25.47  ? 128 ALA E C   1 
ATOM   4149 O O   . ALA D 4 129 ? 23.372 -30.374 -63.434 1.00 24.19  ? 128 ALA E O   1 
ATOM   4150 C CB  . ALA D 4 129 ? 23.114 -33.569 -63.200 1.00 22.57  ? 128 ALA E CB  1 
ATOM   4151 N N   . VAL D 4 130 ? 24.922 -31.331 -64.776 1.00 23.85  ? 129 VAL E N   1 
ATOM   4152 C CA  . VAL D 4 130 ? 24.960 -30.253 -65.759 1.00 26.60  ? 129 VAL E CA  1 
ATOM   4153 C C   . VAL D 4 130 ? 24.370 -30.775 -67.057 1.00 30.52  ? 129 VAL E C   1 
ATOM   4154 O O   . VAL D 4 130 ? 24.724 -31.870 -67.520 1.00 28.98  ? 129 VAL E O   1 
ATOM   4155 C CB  . VAL D 4 130 ? 26.386 -29.723 -65.982 1.00 29.47  ? 129 VAL E CB  1 
ATOM   4156 C CG1 . VAL D 4 130 ? 26.432 -28.869 -67.240 1.00 28.61  ? 129 VAL E CG1 1 
ATOM   4157 C CG2 . VAL D 4 130 ? 26.825 -28.911 -64.788 1.00 29.90  ? 129 VAL E CG2 1 
ATOM   4158 N N   . PHE D 4 131 ? 23.464 -30.003 -67.630 1.00 28.24  ? 130 PHE E N   1 
ATOM   4159 C CA  . PHE D 4 131 ? 22.765 -30.383 -68.846 1.00 29.59  ? 130 PHE E CA  1 
ATOM   4160 C C   . PHE D 4 131 ? 23.250 -29.476 -69.968 1.00 32.05  ? 130 PHE E C   1 
ATOM   4161 O O   . PHE D 4 131 ? 23.136 -28.248 -69.868 1.00 26.26  ? 130 PHE E O   1 
ATOM   4162 C CB  . PHE D 4 131 ? 21.253 -30.291 -68.636 1.00 28.95  ? 130 PHE E CB  1 
ATOM   4163 C CG  . PHE D 4 131 ? 20.736 -31.263 -67.602 1.00 29.18  ? 130 PHE E CG  1 
ATOM   4164 C CD1 . PHE D 4 131 ? 20.823 -30.972 -66.243 1.00 27.21  ? 130 PHE E CD1 1 
ATOM   4165 C CD2 . PHE D 4 131 ? 20.187 -32.483 -67.990 1.00 35.28  ? 130 PHE E CD2 1 
ATOM   4166 C CE1 . PHE D 4 131 ? 20.363 -31.879 -65.295 1.00 30.44  ? 130 PHE E CE1 1 
ATOM   4167 C CE2 . PHE D 4 131 ? 19.723 -33.398 -67.048 1.00 32.63  ? 130 PHE E CE2 1 
ATOM   4168 C CZ  . PHE D 4 131 ? 19.816 -33.096 -65.695 1.00 31.77  ? 130 PHE E CZ  1 
ATOM   4169 N N   . GLU D 4 132 ? 23.810 -30.091 -71.013 1.00 30.92  ? 131 GLU E N   1 
ATOM   4170 C CA  . GLU D 4 132 ? 24.433 -29.394 -72.127 1.00 30.71  ? 131 GLU E CA  1 
ATOM   4171 C C   . GLU D 4 132 ? 23.400 -28.677 -73.008 1.00 30.28  ? 131 GLU E C   1 
ATOM   4172 O O   . GLU D 4 132 ? 22.228 -29.052 -73.043 1.00 29.52  ? 131 GLU E O   1 
ATOM   4173 C CB  . GLU D 4 132 ? 25.233 -30.391 -72.963 1.00 26.30  ? 131 GLU E CB  1 
ATOM   4174 C CG  . GLU D 4 132 ? 26.161 -31.245 -72.138 1.00 33.09  ? 131 GLU E CG  1 
ATOM   4175 C CD  . GLU D 4 132 ? 27.286 -31.857 -72.957 1.00 37.80  ? 131 GLU E CD  1 
ATOM   4176 O OE1 . GLU D 4 132 ? 28.353 -32.130 -72.380 1.00 38.61  ? 131 GLU E OE1 1 
ATOM   4177 O OE2 . GLU D 4 132 ? 27.111 -32.065 -74.176 1.00 47.71  ? 131 GLU E OE2 1 
ATOM   4178 N N   . PRO D 4 133 ? 23.823 -27.648 -73.744 1.00 25.93  ? 132 PRO E N   1 
ATOM   4179 C CA  . PRO D 4 133 ? 22.874 -26.910 -74.591 1.00 30.26  ? 132 PRO E CA  1 
ATOM   4180 C C   . PRO D 4 133 ? 22.306 -27.791 -75.695 1.00 29.36  ? 132 PRO E C   1 
ATOM   4181 O O   . PRO D 4 133 ? 22.981 -28.680 -76.217 1.00 31.03  ? 132 PRO E O   1 
ATOM   4182 C CB  . PRO D 4 133 ? 23.720 -25.768 -75.179 1.00 27.84  ? 132 PRO E CB  1 
ATOM   4183 C CG  . PRO D 4 133 ? 24.997 -25.746 -74.376 1.00 31.44  ? 132 PRO E CG  1 
ATOM   4184 C CD  . PRO D 4 133 ? 25.205 -27.155 -73.890 1.00 27.21  ? 132 PRO E CD  1 
ATOM   4185 N N   . SER D 4 134 ? 21.048 -27.543 -76.043 1.00 30.70  ? 133 SER E N   1 
ATOM   4186 C CA  . SER D 4 134 ? 20.456 -28.226 -77.188 1.00 39.34  ? 133 SER E CA  1 
ATOM   4187 C C   . SER D 4 134 ? 20.981 -27.622 -78.480 1.00 30.86  ? 133 SER E C   1 
ATOM   4188 O O   . SER D 4 134 ? 21.168 -26.406 -78.580 1.00 27.10  ? 133 SER E O   1 
ATOM   4189 C CB  . SER D 4 134 ? 18.931 -28.127 -77.165 1.00 35.40  ? 133 SER E CB  1 
ATOM   4190 O OG  . SER D 4 134 ? 18.488 -26.913 -77.741 1.00 38.33  ? 133 SER E OG  1 
ATOM   4191 N N   . GLU D 4 135 ? 21.219 -28.481 -79.476 1.00 31.49  ? 134 GLU E N   1 
ATOM   4192 C CA  . GLU D 4 135 ? 21.655 -27.979 -80.771 1.00 34.44  ? 134 GLU E CA  1 
ATOM   4193 C C   . GLU D 4 135 ? 20.570 -27.152 -81.452 1.00 31.57  ? 134 GLU E C   1 
ATOM   4194 O O   . GLU D 4 135 ? 20.885 -26.291 -82.275 1.00 28.93  ? 134 GLU E O   1 
ATOM   4195 C CB  . GLU D 4 135 ? 22.109 -29.141 -81.674 1.00 40.82  ? 134 GLU E CB  1 
ATOM   4196 C CG  . GLU D 4 135 ? 23.430 -29.799 -81.227 1.00 44.55  ? 134 GLU E CG  1 
ATOM   4197 C CD  . GLU D 4 135 ? 24.561 -28.782 -80.961 1.00 45.74  ? 134 GLU E CD  1 
ATOM   4198 O OE1 . GLU D 4 135 ? 25.143 -28.821 -79.846 1.00 49.77  ? 134 GLU E OE1 1 
ATOM   4199 O OE2 . GLU D 4 135 ? 24.872 -27.967 -81.863 1.00 41.27  ? 134 GLU E OE2 1 
ATOM   4200 N N   . ALA D 4 136 ? 19.304 -27.356 -81.088 1.00 27.77  ? 135 ALA E N   1 
ATOM   4201 C CA  . ALA D 4 136 ? 18.242 -26.552 -81.672 1.00 29.80  ? 135 ALA E CA  1 
ATOM   4202 C C   . ALA D 4 136 ? 18.298 -25.102 -81.180 1.00 30.79  ? 135 ALA E C   1 
ATOM   4203 O O   . ALA D 4 136 ? 18.128 -24.171 -81.976 1.00 32.99  ? 135 ALA E O   1 
ATOM   4204 C CB  . ALA D 4 136 ? 16.887 -27.200 -81.381 1.00 24.22  ? 135 ALA E CB  1 
ATOM   4205 N N   . GLU D 4 137 ? 18.544 -24.880 -79.877 1.00 29.22  ? 136 GLU E N   1 
ATOM   4206 C CA  . GLU D 4 137 ? 18.744 -23.509 -79.409 1.00 26.89  ? 136 GLU E CA  1 
ATOM   4207 C C   . GLU D 4 137 ? 19.952 -22.871 -80.085 1.00 24.86  ? 136 GLU E C   1 
ATOM   4208 O O   . GLU D 4 137 ? 19.911 -21.696 -80.466 1.00 28.11  ? 136 GLU E O   1 
ATOM   4209 C CB  . GLU D 4 137 ? 18.909 -23.459 -77.881 1.00 26.03  ? 136 GLU E CB  1 
ATOM   4210 C CG  . GLU D 4 137 ? 19.105 -22.011 -77.353 1.00 28.81  ? 136 GLU E CG  1 
ATOM   4211 C CD  . GLU D 4 137 ? 19.723 -21.913 -75.934 1.00 29.21  ? 136 GLU E CD  1 
ATOM   4212 O OE1 . GLU D 4 137 ? 20.120 -22.954 -75.381 1.00 25.73  ? 136 GLU E OE1 1 
ATOM   4213 O OE2 . GLU D 4 137 ? 19.808 -20.784 -75.379 1.00 23.72  ? 136 GLU E OE2 1 
ATOM   4214 N N   . ILE D 4 138 ? 21.031 -23.638 -80.255 1.00 26.14  ? 137 ILE E N   1 
ATOM   4215 C CA  . ILE D 4 138 ? 22.237 -23.114 -80.887 1.00 29.04  ? 137 ILE E CA  1 
ATOM   4216 C C   . ILE D 4 138 ? 21.947 -22.655 -82.315 1.00 31.71  ? 137 ILE E C   1 
ATOM   4217 O O   . ILE D 4 138 ? 22.311 -21.546 -82.714 1.00 30.25  ? 137 ILE E O   1 
ATOM   4218 C CB  . ILE D 4 138 ? 23.362 -24.165 -80.842 1.00 32.17  ? 137 ILE E CB  1 
ATOM   4219 C CG1 . ILE D 4 138 ? 23.879 -24.312 -79.398 1.00 29.91  ? 137 ILE E CG1 1 
ATOM   4220 C CG2 . ILE D 4 138 ? 24.498 -23.762 -81.791 1.00 25.28  ? 137 ILE E CG2 1 
ATOM   4221 C CD1 . ILE D 4 138 ? 24.995 -25.336 -79.231 1.00 32.81  ? 137 ILE E CD1 1 
ATOM   4222 N N   . SER D 4 139 ? 21.283 -23.486 -83.111 1.00 30.83  ? 138 SER E N   1 
ATOM   4223 C CA  . SER D 4 139 ? 21.071 -23.043 -84.486 1.00 35.85  ? 138 SER E CA  1 
ATOM   4224 C C   . SER D 4 139 ? 19.919 -22.056 -84.606 1.00 34.84  ? 138 SER E C   1 
ATOM   4225 O O   . SER D 4 139 ? 19.890 -21.276 -85.565 1.00 30.15  ? 138 SER E O   1 
ATOM   4226 C CB  . SER D 4 139 ? 20.868 -24.237 -85.422 1.00 32.44  ? 138 SER E CB  1 
ATOM   4227 O OG  . SER D 4 139 ? 19.734 -24.994 -85.064 1.00 40.05  ? 138 SER E OG  1 
ATOM   4228 N N   . HIS D 4 140 ? 19.015 -22.012 -83.626 1.00 31.59  ? 139 HIS E N   1 
ATOM   4229 C CA  . HIS D 4 140 ? 17.923 -21.047 -83.684 1.00 34.22  ? 139 HIS E CA  1 
ATOM   4230 C C   . HIS D 4 140 ? 18.298 -19.658 -83.159 1.00 35.67  ? 139 HIS E C   1 
ATOM   4231 O O   . HIS D 4 140 ? 17.739 -18.659 -83.627 1.00 35.53  ? 139 HIS E O   1 
ATOM   4232 C CB  . HIS D 4 140 ? 16.713 -21.581 -82.910 1.00 33.79  ? 139 HIS E CB  1 
ATOM   4233 C CG  . HIS D 4 140 ? 15.470 -20.764 -83.099 1.00 39.59  ? 139 HIS E CG  1 
ATOM   4234 N ND1 . HIS D 4 140 ? 14.650 -20.898 -84.202 1.00 41.36  ? 139 HIS E ND1 1 
ATOM   4235 C CD2 . HIS D 4 140 ? 14.905 -19.808 -82.324 1.00 37.36  ? 139 HIS E CD2 1 
ATOM   4236 C CE1 . HIS D 4 140 ? 13.635 -20.057 -84.096 1.00 40.13  ? 139 HIS E CE1 1 
ATOM   4237 N NE2 . HIS D 4 140 ? 13.765 -19.386 -82.966 1.00 39.98  ? 139 HIS E NE2 1 
ATOM   4238 N N   . THR D 4 141 ? 19.227 -19.559 -82.201 1.00 32.57  ? 140 THR E N   1 
ATOM   4239 C CA  . THR D 4 141 ? 19.551 -18.288 -81.570 1.00 28.97  ? 140 THR E CA  1 
ATOM   4240 C C   . THR D 4 141 ? 21.016 -17.898 -81.660 1.00 28.70  ? 140 THR E C   1 
ATOM   4241 O O   . THR D 4 141 ? 21.349 -16.768 -81.285 1.00 34.47  ? 140 THR E O   1 
ATOM   4242 C CB  . THR D 4 141 ? 19.196 -18.313 -80.070 1.00 34.97  ? 140 THR E CB  1 
ATOM   4243 O OG1 . THR D 4 141 ? 20.058 -19.253 -79.412 1.00 26.86  ? 140 THR E OG1 1 
ATOM   4244 C CG2 . THR D 4 141 ? 17.733 -18.691 -79.829 1.00 31.03  ? 140 THR E CG2 1 
ATOM   4245 N N   . GLN D 4 142 ? 21.905 -18.805 -82.064 1.00 26.18  ? 141 GLN E N   1 
ATOM   4246 C CA  . GLN D 4 142 ? 23.348 -18.619 -81.918 1.00 30.18  ? 141 GLN E CA  1 
ATOM   4247 C C   . GLN D 4 142 ? 23.776 -18.392 -80.454 1.00 34.61  ? 141 GLN E C   1 
ATOM   4248 O O   . GLN D 4 142 ? 24.828 -17.797 -80.206 1.00 29.99  ? 141 GLN E O   1 
ATOM   4249 C CB  . GLN D 4 142 ? 23.858 -17.466 -82.802 1.00 30.09  ? 141 GLN E CB  1 
ATOM   4250 C CG  . GLN D 4 142 ? 23.638 -17.707 -84.329 1.00 38.31  ? 141 GLN E CG  1 
ATOM   4251 C CD  . GLN D 4 142 ? 24.114 -19.094 -84.783 1.00 40.02  ? 141 GLN E CD  1 
ATOM   4252 O OE1 . GLN D 4 142 ? 25.153 -19.595 -84.329 1.00 48.11  ? 141 GLN E OE1 1 
ATOM   4253 N NE2 . GLN D 4 142 ? 23.352 -19.719 -85.678 1.00 47.16  ? 141 GLN E NE2 1 
ATOM   4254 N N   . LYS D 4 143 ? 22.979 -18.846 -79.476 1.00 28.30  ? 142 LYS E N   1 
ATOM   4255 C CA  . LYS D 4 143 ? 23.355 -18.841 -78.067 1.00 28.34  ? 142 LYS E CA  1 
ATOM   4256 C C   . LYS D 4 143 ? 23.180 -20.246 -77.497 1.00 29.81  ? 142 LYS E C   1 
ATOM   4257 O O   . LYS D 4 143 ? 22.483 -21.081 -78.075 1.00 31.36  ? 142 LYS E O   1 
ATOM   4258 C CB  . LYS D 4 143 ? 22.530 -17.826 -77.259 1.00 27.84  ? 142 LYS E CB  1 
ATOM   4259 C CG  . LYS D 4 143 ? 22.780 -16.374 -77.689 1.00 30.39  ? 142 LYS E CG  1 
ATOM   4260 C CD  . LYS D 4 143 ? 21.927 -15.399 -76.910 1.00 35.50  ? 142 LYS E CD  1 
ATOM   4261 C CE  . LYS D 4 143 ? 22.373 -13.960 -77.162 1.00 39.25  ? 142 LYS E CE  1 
ATOM   4262 N NZ  . LYS D 4 143 ? 21.498 -13.334 -78.188 1.00 39.02  ? 142 LYS E NZ  1 
ATOM   4263 N N   . ALA D 4 144 ? 23.829 -20.510 -76.359 1.00 26.04  ? 143 ALA E N   1 
ATOM   4264 C CA  . ALA D 4 144 ? 23.844 -21.839 -75.754 1.00 25.67  ? 143 ALA E CA  1 
ATOM   4265 C C   . ALA D 4 144 ? 23.658 -21.720 -74.246 1.00 27.19  ? 143 ALA E C   1 
ATOM   4266 O O   . ALA D 4 144 ? 24.482 -21.104 -73.564 1.00 23.98  ? 143 ALA E O   1 
ATOM   4267 C CB  . ALA D 4 144 ? 25.148 -22.566 -76.078 1.00 21.11  ? 143 ALA E CB  1 
ATOM   4268 N N   . THR D 4 145 ? 22.586 -22.321 -73.733 1.00 25.68  ? 144 THR E N   1 
ATOM   4269 C CA  . THR D 4 145 ? 22.224 -22.283 -72.319 1.00 24.95  ? 144 THR E CA  1 
ATOM   4270 C C   . THR D 4 145 ? 22.560 -23.627 -71.683 1.00 27.36  ? 144 THR E C   1 
ATOM   4271 O O   . THR D 4 145 ? 22.076 -24.665 -72.144 1.00 24.24  ? 144 THR E O   1 
ATOM   4272 C CB  . THR D 4 145 ? 20.730 -22.005 -72.141 1.00 24.44  ? 144 THR E CB  1 
ATOM   4273 O OG1 . THR D 4 145 ? 20.357 -20.847 -72.893 1.00 22.60  ? 144 THR E OG1 1 
ATOM   4274 C CG2 . THR D 4 145 ? 20.374 -21.794 -70.631 1.00 21.66  ? 144 THR E CG2 1 
ATOM   4275 N N   . LEU D 4 146 ? 23.398 -23.606 -70.649 1.00 24.99  ? 145 LEU E N   1 
ATOM   4276 C CA  . LEU D 4 146 ? 23.625 -24.763 -69.793 1.00 26.03  ? 145 LEU E CA  1 
ATOM   4277 C C   . LEU D 4 146 ? 22.724 -24.658 -68.576 1.00 26.67  ? 145 LEU E C   1 
ATOM   4278 O O   . LEU D 4 146 ? 22.420 -23.556 -68.097 1.00 24.80  ? 145 LEU E O   1 
ATOM   4279 C CB  . LEU D 4 146 ? 25.081 -24.868 -69.324 1.00 23.23  ? 145 LEU E CB  1 
ATOM   4280 C CG  . LEU D 4 146 ? 26.204 -24.996 -70.358 1.00 28.92  ? 145 LEU E CG  1 
ATOM   4281 C CD1 . LEU D 4 146 ? 26.531 -23.641 -71.033 1.00 25.92  ? 145 LEU E CD1 1 
ATOM   4282 C CD2 . LEU D 4 146 ? 27.415 -25.564 -69.669 1.00 22.92  ? 145 LEU E CD2 1 
ATOM   4283 N N   . VAL D 4 147 ? 22.292 -25.813 -68.083 1.00 21.82  ? 146 VAL E N   1 
ATOM   4284 C CA  . VAL D 4 147 ? 21.458 -25.875 -66.895 1.00 25.36  ? 146 VAL E CA  1 
ATOM   4285 C C   . VAL D 4 147 ? 22.129 -26.793 -65.891 1.00 28.25  ? 146 VAL E C   1 
ATOM   4286 O O   . VAL D 4 147 ? 22.603 -27.884 -66.237 1.00 21.00  ? 146 VAL E O   1 
ATOM   4287 C CB  . VAL D 4 147 ? 20.023 -26.354 -67.187 1.00 28.17  ? 146 VAL E CB  1 
ATOM   4288 C CG1 . VAL D 4 147 ? 19.297 -26.622 -65.867 1.00 26.37  ? 146 VAL E CG1 1 
ATOM   4289 C CG2 . VAL D 4 147 ? 19.271 -25.312 -68.032 1.00 26.04  ? 146 VAL E CG2 1 
ATOM   4290 N N   . CYS D 4 148 ? 22.187 -26.332 -64.659 1.00 24.85  ? 147 CYS E N   1 
ATOM   4291 C CA  . CYS D 4 148 ? 22.676 -27.101 -63.542 1.00 25.99  ? 147 CYS E CA  1 
ATOM   4292 C C   . CYS D 4 148 ? 21.501 -27.428 -62.637 1.00 26.51  ? 147 CYS E C   1 
ATOM   4293 O O   . CYS D 4 148 ? 20.619 -26.586 -62.425 1.00 23.05  ? 147 CYS E O   1 
ATOM   4294 C CB  . CYS D 4 148 ? 23.732 -26.307 -62.775 1.00 22.81  ? 147 CYS E CB  1 
ATOM   4295 S SG  . CYS D 4 148 ? 24.405 -27.189 -61.350 1.00 30.62  ? 147 CYS E SG  1 
ATOM   4296 N N   . LEU D 4 149 ? 21.497 -28.649 -62.114 1.00 23.04  ? 148 LEU E N   1 
ATOM   4297 C CA  . LEU D 4 149 ? 20.436 -29.134 -61.244 1.00 26.76  ? 148 LEU E CA  1 
ATOM   4298 C C   . LEU D 4 149 ? 21.065 -29.755 -60.013 1.00 25.10  ? 148 LEU E C   1 
ATOM   4299 O O   . LEU D 4 149 ? 21.835 -30.713 -60.129 1.00 24.75  ? 148 LEU E O   1 
ATOM   4300 C CB  . LEU D 4 149 ? 19.571 -30.169 -61.962 1.00 27.37  ? 148 LEU E CB  1 
ATOM   4301 C CG  . LEU D 4 149 ? 18.061 -30.053 -61.948 1.00 33.38  ? 148 LEU E CG  1 
ATOM   4302 C CD1 . LEU D 4 149 ? 17.595 -28.728 -62.530 1.00 28.66  ? 148 LEU E CD1 1 
ATOM   4303 C CD2 . LEU D 4 149 ? 17.534 -31.210 -62.780 1.00 37.11  ? 148 LEU E CD2 1 
ATOM   4304 N N   . ALA D 4 150 ? 20.724 -29.227 -58.843 1.00 24.83  ? 149 ALA E N   1 
ATOM   4305 C CA  . ALA D 4 150 ? 21.096 -29.827 -57.574 1.00 24.89  ? 149 ALA E CA  1 
ATOM   4306 C C   . ALA D 4 150 ? 19.846 -30.433 -56.953 1.00 23.85  ? 149 ALA E C   1 
ATOM   4307 O O   . ALA D 4 150 ? 18.829 -29.752 -56.822 1.00 26.84  ? 149 ALA E O   1 
ATOM   4308 C CB  . ALA D 4 150 ? 21.726 -28.790 -56.638 1.00 24.68  ? 149 ALA E CB  1 
ATOM   4309 N N   . THR D 4 151 ? 19.919 -31.698 -56.564 1.00 20.83  ? 150 THR E N   1 
ATOM   4310 C CA  . THR D 4 151 ? 18.725 -32.421 -56.164 1.00 25.57  ? 150 THR E CA  1 
ATOM   4311 C C   . THR D 4 151 ? 19.004 -33.240 -54.914 1.00 26.54  ? 150 THR E C   1 
ATOM   4312 O O   . THR D 4 151 ? 20.154 -33.581 -54.612 1.00 25.35  ? 150 THR E O   1 
ATOM   4313 C CB  . THR D 4 151 ? 18.226 -33.386 -57.278 1.00 26.42  ? 150 THR E CB  1 
ATOM   4314 O OG1 . THR D 4 151 ? 19.299 -34.255 -57.668 1.00 25.06  ? 150 THR E OG1 1 
ATOM   4315 C CG2 . THR D 4 151 ? 17.730 -32.623 -58.513 1.00 22.82  ? 150 THR E CG2 1 
ATOM   4316 N N   . GLY D 4 152 ? 17.919 -33.575 -54.212 1.00 22.36  ? 151 GLY E N   1 
ATOM   4317 C CA  . GLY D 4 152 ? 17.964 -34.546 -53.141 1.00 27.04  ? 151 GLY E CA  1 
ATOM   4318 C C   . GLY D 4 152 ? 18.636 -34.080 -51.871 1.00 27.23  ? 151 GLY E C   1 
ATOM   4319 O O   . GLY D 4 152 ? 19.017 -34.913 -51.046 1.00 28.16  ? 151 GLY E O   1 
ATOM   4320 N N   . PHE D 4 153 ? 18.792 -32.777 -51.675 1.00 26.79  ? 152 PHE E N   1 
ATOM   4321 C CA  . PHE D 4 153 ? 19.531 -32.300 -50.519 1.00 25.29  ? 152 PHE E CA  1 
ATOM   4322 C C   . PHE D 4 153 ? 18.595 -31.804 -49.424 1.00 26.80  ? 152 PHE E C   1 
ATOM   4323 O O   . PHE D 4 153 ? 17.472 -31.364 -49.678 1.00 25.06  ? 152 PHE E O   1 
ATOM   4324 C CB  . PHE D 4 153 ? 20.532 -31.204 -50.905 1.00 23.20  ? 152 PHE E CB  1 
ATOM   4325 C CG  . PHE D 4 153 ? 19.920 -29.986 -51.554 1.00 28.11  ? 152 PHE E CG  1 
ATOM   4326 C CD1 . PHE D 4 153 ? 19.508 -28.911 -50.783 1.00 26.45  ? 152 PHE E CD1 1 
ATOM   4327 C CD2 . PHE D 4 153 ? 19.804 -29.896 -52.945 1.00 22.88  ? 152 PHE E CD2 1 
ATOM   4328 C CE1 . PHE D 4 153 ? 18.963 -27.769 -51.370 1.00 25.01  ? 152 PHE E CE1 1 
ATOM   4329 C CE2 . PHE D 4 153 ? 19.259 -28.753 -53.542 1.00 24.73  ? 152 PHE E CE2 1 
ATOM   4330 C CZ  . PHE D 4 153 ? 18.842 -27.690 -52.760 1.00 26.78  ? 152 PHE E CZ  1 
ATOM   4331 N N   . TYR D 4 154 ? 19.087 -31.875 -48.192 1.00 27.14  ? 153 TYR E N   1 
ATOM   4332 C CA  . TYR D 4 154 ? 18.358 -31.367 -47.043 1.00 27.04  ? 153 TYR E CA  1 
ATOM   4333 C C   . TYR D 4 154 ? 19.378 -31.085 -45.958 1.00 25.16  ? 153 TYR E C   1 
ATOM   4334 O O   . TYR D 4 154 ? 20.278 -31.908 -45.755 1.00 25.57  ? 153 TYR E O   1 
ATOM   4335 C CB  . TYR D 4 154 ? 17.316 -32.367 -46.533 1.00 28.26  ? 153 TYR E CB  1 
ATOM   4336 C CG  . TYR D 4 154 ? 16.617 -31.901 -45.274 1.00 29.97  ? 153 TYR E CG  1 
ATOM   4337 C CD1 . TYR D 4 154 ? 17.195 -32.077 -44.021 1.00 27.97  ? 153 TYR E CD1 1 
ATOM   4338 C CD2 . TYR D 4 154 ? 15.386 -31.271 -45.344 1.00 28.92  ? 153 TYR E CD2 1 
ATOM   4339 C CE1 . TYR D 4 154 ? 16.553 -31.633 -42.874 1.00 33.06  ? 153 TYR E CE1 1 
ATOM   4340 C CE2 . TYR D 4 154 ? 14.739 -30.834 -44.217 1.00 31.95  ? 153 TYR E CE2 1 
ATOM   4341 C CZ  . TYR D 4 154 ? 15.321 -31.018 -42.985 1.00 33.36  ? 153 TYR E CZ  1 
ATOM   4342 O OH  . TYR D 4 154 ? 14.668 -30.588 -41.864 1.00 33.55  ? 153 TYR E OH  1 
ATOM   4343 N N   . PRO D 4 155 ? 19.283 -29.950 -45.247 1.00 27.16  ? 154 PRO E N   1 
ATOM   4344 C CA  . PRO D 4 155 ? 18.288 -28.897 -45.477 1.00 26.91  ? 154 PRO E CA  1 
ATOM   4345 C C   . PRO D 4 155 ? 18.673 -28.063 -46.690 1.00 26.01  ? 154 PRO E C   1 
ATOM   4346 O O   . PRO D 4 155 ? 19.617 -28.429 -47.392 1.00 28.20  ? 154 PRO E O   1 
ATOM   4347 C CB  . PRO D 4 155 ? 18.353 -28.075 -44.187 1.00 27.68  ? 154 PRO E CB  1 
ATOM   4348 C CG  . PRO D 4 155 ? 19.784 -28.185 -43.784 1.00 24.80  ? 154 PRO E CG  1 
ATOM   4349 C CD  . PRO D 4 155 ? 20.183 -29.613 -44.127 1.00 24.24  ? 154 PRO E CD  1 
ATOM   4350 N N   . ASP D 4 156 ? 17.970 -26.965 -46.946 1.00 26.16  ? 155 ASP E N   1 
ATOM   4351 C CA  . ASP D 4 156 ? 18.291 -26.143 -48.109 1.00 30.23  ? 155 ASP E CA  1 
ATOM   4352 C C   . ASP D 4 156 ? 19.440 -25.182 -47.816 1.00 30.95  ? 155 ASP E C   1 
ATOM   4353 O O   . ASP D 4 156 ? 19.315 -23.976 -48.047 1.00 36.78  ? 155 ASP E O   1 
ATOM   4354 C CB  . ASP D 4 156 ? 17.052 -25.372 -48.579 1.00 32.33  ? 155 ASP E CB  1 
ATOM   4355 C CG  . ASP D 4 156 ? 16.534 -24.402 -47.538 1.00 35.10  ? 155 ASP E CG  1 
ATOM   4356 O OD1 . ASP D 4 156 ? 16.887 -24.563 -46.347 1.00 39.16  ? 155 ASP E OD1 1 
ATOM   4357 O OD2 . ASP D 4 156 ? 15.773 -23.482 -47.908 1.00 37.67  ? 155 ASP E OD2 1 
ATOM   4358 N N   . HIS D 4 157 ? 20.559 -25.694 -47.297 1.00 26.73  ? 156 HIS E N   1 
ATOM   4359 C CA  . HIS D 4 157 ? 21.706 -24.848 -46.952 1.00 26.86  ? 156 HIS E CA  1 
ATOM   4360 C C   . HIS D 4 157 ? 22.768 -25.021 -48.032 1.00 25.18  ? 156 HIS E C   1 
ATOM   4361 O O   . HIS D 4 157 ? 23.749 -25.741 -47.860 1.00 24.45  ? 156 HIS E O   1 
ATOM   4362 C CB  . HIS D 4 157 ? 22.264 -25.204 -45.577 1.00 20.95  ? 156 HIS E CB  1 
ATOM   4363 C CG  . HIS D 4 157 ? 21.314 -24.976 -44.442 1.00 25.85  ? 156 HIS E CG  1 
ATOM   4364 N ND1 . HIS D 4 157 ? 21.662 -25.216 -43.129 1.00 25.14  ? 156 HIS E ND1 1 
ATOM   4365 C CD2 . HIS D 4 157 ? 20.037 -24.524 -44.416 1.00 23.98  ? 156 HIS E CD2 1 
ATOM   4366 C CE1 . HIS D 4 157 ? 20.641 -24.921 -42.345 1.00 23.47  ? 156 HIS E CE1 1 
ATOM   4367 N NE2 . HIS D 4 157 ? 19.644 -24.498 -43.101 1.00 21.19  ? 156 HIS E NE2 1 
ATOM   4368 N N   . VAL D 4 158 ? 22.567 -24.349 -49.171 1.00 27.72  ? 157 VAL E N   1 
ATOM   4369 C CA  . VAL D 4 158 ? 23.437 -24.541 -50.327 1.00 22.57  ? 157 VAL E CA  1 
ATOM   4370 C C   . VAL D 4 158 ? 23.763 -23.201 -50.960 1.00 26.07  ? 157 VAL E C   1 
ATOM   4371 O O   . VAL D 4 158 ? 22.982 -22.248 -50.879 1.00 27.09  ? 157 VAL E O   1 
ATOM   4372 C CB  . VAL D 4 158 ? 22.815 -25.481 -51.391 1.00 25.94  ? 157 VAL E CB  1 
ATOM   4373 C CG1 . VAL D 4 158 ? 22.624 -26.886 -50.826 1.00 20.47  ? 157 VAL E CG1 1 
ATOM   4374 C CG2 . VAL D 4 158 ? 21.486 -24.894 -51.957 1.00 20.28  ? 157 VAL E CG2 1 
ATOM   4375 N N   . GLU D 4 159 ? 24.930 -23.138 -51.611 1.00 21.53  ? 158 GLU E N   1 
ATOM   4376 C CA  . GLU D 4 159 ? 25.281 -22.017 -52.469 1.00 21.74  ? 158 GLU E CA  1 
ATOM   4377 C C   . GLU D 4 159 ? 25.752 -22.588 -53.796 1.00 25.38  ? 158 GLU E C   1 
ATOM   4378 O O   . GLU D 4 159 ? 26.618 -23.469 -53.824 1.00 24.01  ? 158 GLU E O   1 
ATOM   4379 C CB  . GLU D 4 159 ? 26.367 -21.127 -51.844 1.00 22.25  ? 158 GLU E CB  1 
ATOM   4380 C CG  . GLU D 4 159 ? 25.954 -20.454 -50.524 1.00 29.98  ? 158 GLU E CG  1 
ATOM   4381 C CD  . GLU D 4 159 ? 27.162 -19.978 -49.683 1.00 29.38  ? 158 GLU E CD  1 
ATOM   4382 O OE1 . GLU D 4 159 ? 28.315 -20.385 -49.984 1.00 27.97  ? 158 GLU E OE1 1 
ATOM   4383 O OE2 . GLU D 4 159 ? 26.951 -19.216 -48.709 1.00 34.48  ? 158 GLU E OE2 1 
ATOM   4384 N N   . LEU D 4 160 ? 25.181 -22.089 -54.887 1.00 23.29  ? 159 LEU E N   1 
ATOM   4385 C CA  . LEU D 4 160 ? 25.485 -22.569 -56.228 1.00 24.40  ? 159 LEU E CA  1 
ATOM   4386 C C   . LEU D 4 160 ? 26.251 -21.487 -56.975 1.00 21.89  ? 159 LEU E C   1 
ATOM   4387 O O   . LEU D 4 160 ? 25.849 -20.317 -56.974 1.00 21.38  ? 159 LEU E O   1 
ATOM   4388 C CB  . LEU D 4 160 ? 24.201 -22.944 -56.979 1.00 20.78  ? 159 LEU E CB  1 
ATOM   4389 C CG  . LEU D 4 160 ? 24.346 -23.643 -58.339 1.00 22.30  ? 159 LEU E CG  1 
ATOM   4390 C CD1 . LEU D 4 160 ? 23.041 -24.371 -58.665 1.00 20.57  ? 159 LEU E CD1 1 
ATOM   4391 C CD2 . LEU D 4 160 ? 24.722 -22.679 -59.464 1.00 17.87  ? 159 LEU E CD2 1 
ATOM   4392 N N   . SER D 4 161 ? 27.347 -21.879 -57.617 1.00 19.26  ? 160 SER E N   1 
ATOM   4393 C CA  . SER D 4 161 ? 28.149 -20.949 -58.394 1.00 22.28  ? 160 SER E CA  1 
ATOM   4394 C C   . SER D 4 161 ? 28.571 -21.614 -59.700 1.00 23.10  ? 160 SER E C   1 
ATOM   4395 O O   . SER D 4 161 ? 28.661 -22.842 -59.799 1.00 21.42  ? 160 SER E O   1 
ATOM   4396 C CB  . SER D 4 161 ? 29.378 -20.478 -57.598 1.00 27.11  ? 160 SER E CB  1 
ATOM   4397 O OG  . SER D 4 161 ? 30.121 -21.588 -57.111 1.00 28.54  ? 160 SER E OG  1 
ATOM   4398 N N   . TRP D 4 162 ? 28.827 -20.781 -60.705 1.00 25.57  ? 161 TRP E N   1 
ATOM   4399 C CA  . TRP D 4 162 ? 29.333 -21.218 -61.999 1.00 22.51  ? 161 TRP E CA  1 
ATOM   4400 C C   . TRP D 4 162 ? 30.794 -20.808 -62.180 1.00 22.30  ? 161 TRP E C   1 
ATOM   4401 O O   . TRP D 4 162 ? 31.172 -19.668 -61.881 1.00 22.87  ? 161 TRP E O   1 
ATOM   4402 C CB  . TRP D 4 162 ? 28.505 -20.615 -63.130 1.00 20.68  ? 161 TRP E CB  1 
ATOM   4403 C CG  . TRP D 4 162 ? 27.155 -21.234 -63.341 1.00 22.28  ? 161 TRP E CG  1 
ATOM   4404 C CD1 . TRP D 4 162 ? 25.952 -20.797 -62.835 1.00 20.55  ? 161 TRP E CD1 1 
ATOM   4405 C CD2 . TRP D 4 162 ? 26.862 -22.384 -64.134 1.00 17.44  ? 161 TRP E CD2 1 
ATOM   4406 N NE1 . TRP D 4 162 ? 24.933 -21.610 -63.273 1.00 22.78  ? 161 TRP E NE1 1 
ATOM   4407 C CE2 . TRP D 4 162 ? 25.464 -22.591 -64.075 1.00 24.56  ? 161 TRP E CE2 1 
ATOM   4408 C CE3 . TRP D 4 162 ? 27.645 -23.268 -64.883 1.00 22.76  ? 161 TRP E CE3 1 
ATOM   4409 C CZ2 . TRP D 4 162 ? 24.827 -23.653 -64.754 1.00 27.10  ? 161 TRP E CZ2 1 
ATOM   4410 C CZ3 . TRP D 4 162 ? 27.009 -24.335 -65.570 1.00 25.16  ? 161 TRP E CZ3 1 
ATOM   4411 C CH2 . TRP D 4 162 ? 25.616 -24.506 -65.503 1.00 22.58  ? 161 TRP E CH2 1 
ATOM   4412 N N   . TRP D 4 163 ? 31.595 -21.727 -62.728 1.00 19.38  ? 162 TRP E N   1 
ATOM   4413 C CA  . TRP D 4 163 ? 33.033 -21.551 -62.901 1.00 21.71  ? 162 TRP E CA  1 
ATOM   4414 C C   . TRP D 4 163 ? 33.399 -21.896 -64.344 1.00 27.19  ? 162 TRP E C   1 
ATOM   4415 O O   . TRP D 4 163 ? 33.295 -23.058 -64.764 1.00 26.33  ? 162 TRP E O   1 
ATOM   4416 C CB  . TRP D 4 163 ? 33.810 -22.414 -61.904 1.00 20.92  ? 162 TRP E CB  1 
ATOM   4417 C CG  . TRP D 4 163 ? 33.544 -22.015 -60.479 1.00 26.50  ? 162 TRP E CG  1 
ATOM   4418 C CD1 . TRP D 4 163 ? 32.445 -22.327 -59.740 1.00 23.29  ? 162 TRP E CD1 1 
ATOM   4419 C CD2 . TRP D 4 163 ? 34.373 -21.188 -59.640 1.00 24.83  ? 162 TRP E CD2 1 
ATOM   4420 N NE1 . TRP D 4 163 ? 32.545 -21.776 -58.480 1.00 26.74  ? 162 TRP E NE1 1 
ATOM   4421 C CE2 . TRP D 4 163 ? 33.713 -21.063 -58.396 1.00 28.27  ? 162 TRP E CE2 1 
ATOM   4422 C CE3 . TRP D 4 163 ? 35.609 -20.555 -59.816 1.00 21.90  ? 162 TRP E CE3 1 
ATOM   4423 C CZ2 . TRP D 4 163 ? 34.245 -20.320 -57.332 1.00 29.66  ? 162 TRP E CZ2 1 
ATOM   4424 C CZ3 . TRP D 4 163 ? 36.143 -19.822 -58.756 1.00 25.19  ? 162 TRP E CZ3 1 
ATOM   4425 C CH2 . TRP D 4 163 ? 35.458 -19.710 -57.531 1.00 31.04  ? 162 TRP E CH2 1 
ATOM   4426 N N   . VAL D 4 164 ? 33.789 -20.882 -65.112 1.00 24.99  ? 163 VAL E N   1 
ATOM   4427 C CA  . VAL D 4 164 ? 34.127 -21.045 -66.517 1.00 21.88  ? 163 VAL E CA  1 
ATOM   4428 C C   . VAL D 4 164 ? 35.624 -20.854 -66.626 1.00 24.00  ? 163 VAL E C   1 
ATOM   4429 O O   . VAL D 4 164 ? 36.150 -19.807 -66.232 1.00 26.70  ? 163 VAL E O   1 
ATOM   4430 C CB  . VAL D 4 164 ? 33.369 -20.058 -67.415 1.00 25.49  ? 163 VAL E CB  1 
ATOM   4431 C CG1 . VAL D 4 164 ? 33.839 -20.211 -68.853 1.00 22.81  ? 163 VAL E CG1 1 
ATOM   4432 C CG2 . VAL D 4 164 ? 31.863 -20.284 -67.320 1.00 15.65  ? 163 VAL E CG2 1 
ATOM   4433 N N   . ASN D 4 165 ? 36.314 -21.886 -67.106 1.00 21.96  ? 164 ASN E N   1 
ATOM   4434 C CA  . ASN D 4 165 ? 37.763 -21.860 -67.268 1.00 25.76  ? 164 ASN E CA  1 
ATOM   4435 C C   . ASN D 4 165 ? 38.485 -21.487 -65.969 1.00 25.91  ? 164 ASN E C   1 
ATOM   4436 O O   . ASN D 4 165 ? 39.529 -20.834 -65.993 1.00 25.15  ? 164 ASN E O   1 
ATOM   4437 C CB  . ASN D 4 165 ? 38.149 -20.931 -68.429 1.00 23.99  ? 164 ASN E CB  1 
ATOM   4438 C CG  . ASN D 4 165 ? 37.829 -21.566 -69.778 1.00 28.60  ? 164 ASN E CG  1 
ATOM   4439 O OD1 . ASN D 4 165 ? 38.035 -22.767 -69.947 1.00 24.82  ? 164 ASN E OD1 1 
ATOM   4440 N ND2 . ASN D 4 165 ? 37.290 -20.784 -70.723 1.00 25.37  ? 164 ASN E ND2 1 
ATOM   4441 N N   . GLY D 4 166 ? 37.938 -21.913 -64.823 1.00 25.57  ? 165 GLY E N   1 
ATOM   4442 C CA  . GLY D 4 166 ? 38.572 -21.692 -63.542 1.00 23.12  ? 165 GLY E CA  1 
ATOM   4443 C C   . GLY D 4 166 ? 38.125 -20.455 -62.785 1.00 23.87  ? 165 GLY E C   1 
ATOM   4444 O O   . GLY D 4 166 ? 38.522 -20.297 -61.633 1.00 29.14  ? 165 GLY E O   1 
ATOM   4445 N N   . LYS D 4 167 ? 37.298 -19.596 -63.379 1.00 24.19  ? 166 LYS E N   1 
ATOM   4446 C CA  . LYS D 4 167 ? 36.861 -18.343 -62.782 1.00 25.76  ? 166 LYS E CA  1 
ATOM   4447 C C   . LYS D 4 167 ? 35.359 -18.318 -62.573 1.00 26.21  ? 166 LYS E C   1 
ATOM   4448 O O   . LYS D 4 167 ? 34.593 -18.704 -63.460 1.00 23.88  ? 166 LYS E O   1 
ATOM   4449 C CB  . LYS D 4 167 ? 37.221 -17.154 -63.653 1.00 29.55  ? 166 LYS E CB  1 
ATOM   4450 C CG  . LYS D 4 167 ? 38.564 -17.253 -64.285 1.00 36.69  ? 166 LYS E CG  1 
ATOM   4451 C CD  . LYS D 4 167 ? 39.536 -16.714 -63.287 1.00 38.11  ? 166 LYS E CD  1 
ATOM   4452 C CE  . LYS D 4 167 ? 40.530 -15.829 -63.996 1.00 47.49  ? 166 LYS E CE  1 
ATOM   4453 N NZ  . LYS D 4 167 ? 39.769 -14.785 -64.761 1.00 57.87  ? 166 LYS E NZ  1 
ATOM   4454 N N   . GLU D 4 168 ? 34.945 -17.845 -61.401 1.00 25.83  ? 167 GLU E N   1 
ATOM   4455 C CA  . GLU D 4 168 ? 33.523 -17.655 -61.163 1.00 29.00  ? 167 GLU E CA  1 
ATOM   4456 C C   . GLU D 4 168 ? 32.986 -16.638 -62.152 1.00 25.38  ? 167 GLU E C   1 
ATOM   4457 O O   . GLU D 4 168 ? 33.646 -15.650 -62.472 1.00 25.47  ? 167 GLU E O   1 
ATOM   4458 C CB  . GLU D 4 168 ? 33.257 -17.190 -59.733 1.00 24.95  ? 167 GLU E CB  1 
ATOM   4459 C CG  . GLU D 4 168 ? 31.797 -17.309 -59.316 1.00 28.28  ? 167 GLU E CG  1 
ATOM   4460 C CD  . GLU D 4 168 ? 31.577 -16.930 -57.861 1.00 31.69  ? 167 GLU E CD  1 
ATOM   4461 O OE1 . GLU D 4 168 ? 32.556 -16.537 -57.200 1.00 36.46  ? 167 GLU E OE1 1 
ATOM   4462 O OE2 . GLU D 4 168 ? 30.428 -17.010 -57.379 1.00 41.01  ? 167 GLU E OE2 1 
ATOM   4463 N N   . VAL D 4 169 ? 31.795 -16.905 -62.667 1.00 26.47  ? 168 VAL E N   1 
ATOM   4464 C CA  . VAL D 4 169 ? 31.119 -15.954 -63.533 1.00 22.87  ? 168 VAL E CA  1 
ATOM   4465 C C   . VAL D 4 169 ? 29.751 -15.663 -62.947 1.00 22.86  ? 168 VAL E C   1 
ATOM   4466 O O   . VAL D 4 169 ? 29.142 -16.508 -62.284 1.00 24.66  ? 168 VAL E O   1 
ATOM   4467 C CB  . VAL D 4 169 ? 30.996 -16.483 -64.978 1.00 24.92  ? 168 VAL E CB  1 
ATOM   4468 C CG1 . VAL D 4 169 ? 32.386 -16.716 -65.552 1.00 23.51  ? 168 VAL E CG1 1 
ATOM   4469 C CG2 . VAL D 4 169 ? 30.151 -17.780 -65.011 1.00 22.20  ? 168 VAL E CG2 1 
ATOM   4470 N N   . HIS D 4 170 ? 29.278 -14.448 -63.192 1.00 25.25  ? 169 HIS E N   1 
ATOM   4471 C CA  . HIS D 4 170 ? 27.912 -14.045 -62.905 1.00 26.11  ? 169 HIS E CA  1 
ATOM   4472 C C   . HIS D 4 170 ? 27.189 -13.508 -64.133 1.00 27.11  ? 169 HIS E C   1 
ATOM   4473 O O   . HIS D 4 170 ? 25.963 -13.597 -64.200 1.00 26.65  ? 169 HIS E O   1 
ATOM   4474 C CB  . HIS D 4 170 ? 27.900 -12.991 -61.783 1.00 22.45  ? 169 HIS E CB  1 
ATOM   4475 C CG  . HIS D 4 170 ? 28.827 -13.316 -60.660 1.00 29.00  ? 169 HIS E CG  1 
ATOM   4476 N ND1 . HIS D 4 170 ? 28.381 -13.780 -59.441 1.00 35.14  ? 169 HIS E ND1 1 
ATOM   4477 C CD2 . HIS D 4 170 ? 30.180 -13.292 -60.580 1.00 34.94  ? 169 HIS E CD2 1 
ATOM   4478 C CE1 . HIS D 4 170 ? 29.415 -14.007 -58.651 1.00 30.84  ? 169 HIS E CE1 1 
ATOM   4479 N NE2 . HIS D 4 170 ? 30.519 -13.722 -59.319 1.00 35.08  ? 169 HIS E NE2 1 
ATOM   4480 N N   . SER D 4 171 ? 27.919 -12.964 -65.105 1.00 24.33  ? 170 SER E N   1 
ATOM   4481 C CA  . SER D 4 171 ? 27.316 -12.574 -66.371 1.00 27.47  ? 170 SER E CA  1 
ATOM   4482 C C   . SER D 4 171 ? 26.708 -13.795 -67.043 1.00 27.84  ? 170 SER E C   1 
ATOM   4483 O O   . SER D 4 171 ? 27.355 -14.843 -67.148 1.00 28.05  ? 170 SER E O   1 
ATOM   4484 C CB  . SER D 4 171 ? 28.366 -11.932 -67.279 1.00 28.78  ? 170 SER E CB  1 
ATOM   4485 O OG  . SER D 4 171 ? 27.757 -11.365 -68.426 1.00 29.38  ? 170 SER E OG  1 
ATOM   4486 N N   . GLY D 4 172 ? 25.455 -13.671 -67.474 1.00 25.33  ? 171 GLY E N   1 
ATOM   4487 C CA  . GLY D 4 172 ? 24.791 -14.778 -68.143 1.00 25.92  ? 171 GLY E CA  1 
ATOM   4488 C C   . GLY D 4 172 ? 24.216 -15.839 -67.224 1.00 29.92  ? 171 GLY E C   1 
ATOM   4489 O O   . GLY D 4 172 ? 23.704 -16.853 -67.718 1.00 27.82  ? 171 GLY E O   1 
ATOM   4490 N N   . VAL D 4 173 ? 24.254 -15.625 -65.896 1.00 23.56  ? 172 VAL E N   1 
ATOM   4491 C CA  . VAL D 4 173 ? 23.791 -16.606 -64.929 1.00 24.57  ? 172 VAL E CA  1 
ATOM   4492 C C   . VAL D 4 173 ? 22.446 -16.172 -64.372 1.00 26.21  ? 172 VAL E C   1 
ATOM   4493 O O   . VAL D 4 173 ? 22.226 -14.987 -64.106 1.00 29.87  ? 172 VAL E O   1 
ATOM   4494 C CB  . VAL D 4 173 ? 24.823 -16.786 -63.798 1.00 27.06  ? 172 VAL E CB  1 
ATOM   4495 C CG1 . VAL D 4 173 ? 24.249 -17.636 -62.670 1.00 18.30  ? 172 VAL E CG1 1 
ATOM   4496 C CG2 . VAL D 4 173 ? 26.101 -17.386 -64.362 1.00 23.20  ? 172 VAL E CG2 1 
ATOM   4497 N N   . CYS D 4 174 ? 21.548 -17.136 -64.182 1.00 22.69  ? 173 CYS E N   1 
ATOM   4498 C CA  . CYS D 4 174 ? 20.360 -16.951 -63.365 1.00 26.13  ? 173 CYS E CA  1 
ATOM   4499 C C   . CYS D 4 174 ? 20.166 -18.192 -62.505 1.00 24.91  ? 173 CYS E C   1 
ATOM   4500 O O   . CYS D 4 174 ? 20.144 -19.309 -63.026 1.00 27.86  ? 173 CYS E O   1 
ATOM   4501 C CB  . CYS D 4 174 ? 19.103 -16.707 -64.218 1.00 30.58  ? 173 CYS E CB  1 
ATOM   4502 S SG  . CYS D 4 174 ? 17.911 -15.749 -63.268 1.00 50.82  ? 173 CYS E SG  1 
ATOM   4503 N N   . THR D 4 175 ? 20.005 -17.998 -61.203 1.00 24.72  ? 174 THR E N   1 
ATOM   4504 C CA  . THR D 4 175 ? 19.766 -19.085 -60.262 1.00 26.38  ? 174 THR E CA  1 
ATOM   4505 C C   . THR D 4 175 ? 18.409 -18.865 -59.607 1.00 30.15  ? 174 THR E C   1 
ATOM   4506 O O   . THR D 4 175 ? 18.041 -17.725 -59.310 1.00 28.63  ? 174 THR E O   1 
ATOM   4507 C CB  . THR D 4 175 ? 20.893 -19.145 -59.205 1.00 28.10  ? 174 THR E CB  1 
ATOM   4508 O OG1 . THR D 4 175 ? 22.149 -19.388 -59.860 1.00 26.63  ? 174 THR E OG1 1 
ATOM   4509 C CG2 . THR D 4 175 ? 20.635 -20.248 -58.162 1.00 24.25  ? 174 THR E CG2 1 
ATOM   4510 N N   . ASP D 4 176 ? 17.645 -19.942 -59.421 1.00 26.06  ? 175 ASP E N   1 
ATOM   4511 C CA  . ASP D 4 176 ? 16.382 -19.823 -58.701 1.00 33.59  ? 175 ASP E CA  1 
ATOM   4512 C C   . ASP D 4 176 ? 16.613 -19.131 -57.347 1.00 31.16  ? 175 ASP E C   1 
ATOM   4513 O O   . ASP D 4 176 ? 17.570 -19.473 -56.637 1.00 27.40  ? 175 ASP E O   1 
ATOM   4514 C CB  . ASP D 4 176 ? 15.739 -21.199 -58.481 1.00 22.56  ? 175 ASP E CB  1 
ATOM   4515 C CG  . ASP D 4 176 ? 15.604 -22.004 -59.764 1.00 35.12  ? 175 ASP E CG  1 
ATOM   4516 O OD1 . ASP D 4 176 ? 15.551 -21.409 -60.866 1.00 40.14  ? 175 ASP E OD1 1 
ATOM   4517 O OD2 . ASP D 4 176 ? 15.545 -23.252 -59.675 1.00 32.68  ? 175 ASP E OD2 1 
ATOM   4518 N N   . PRO D 4 177 ? 15.789 -18.149 -56.972 1.00 32.72  ? 176 PRO E N   1 
ATOM   4519 C CA  . PRO D 4 177 ? 15.996 -17.494 -55.665 1.00 35.39  ? 176 PRO E CA  1 
ATOM   4520 C C   . PRO D 4 177 ? 15.843 -18.445 -54.490 1.00 40.98  ? 176 PRO E C   1 
ATOM   4521 O O   . PRO D 4 177 ? 16.557 -18.298 -53.492 1.00 40.49  ? 176 PRO E O   1 
ATOM   4522 C CB  . PRO D 4 177 ? 14.927 -16.390 -55.642 1.00 35.81  ? 176 PRO E CB  1 
ATOM   4523 C CG  . PRO D 4 177 ? 13.900 -16.811 -56.698 1.00 36.84  ? 176 PRO E CG  1 
ATOM   4524 C CD  . PRO D 4 177 ? 14.695 -17.526 -57.748 1.00 33.45  ? 176 PRO E CD  1 
ATOM   4525 N N   . GLN D 4 178 ? 14.957 -19.437 -54.590 1.00 35.75  ? 177 GLN E N   1 
ATOM   4526 C CA  . GLN D 4 178 ? 14.727 -20.400 -53.521 1.00 41.56  ? 177 GLN E CA  1 
ATOM   4527 C C   . GLN D 4 178 ? 14.658 -21.833 -54.050 1.00 37.95  ? 177 GLN E C   1 
ATOM   4528 O O   . GLN D 4 178 ? 13.992 -22.087 -55.070 1.00 33.87  ? 177 GLN E O   1 
ATOM   4529 C CB  . GLN D 4 178 ? 13.425 -20.043 -52.800 1.00 48.62  ? 177 GLN E CB  1 
ATOM   4530 C CG  . GLN D 4 178 ? 12.273 -19.791 -53.783 1.00 53.13  ? 177 GLN E CG  1 
ATOM   4531 C CD  . GLN D 4 178 ? 11.145 -18.977 -53.189 1.00 63.00  ? 177 GLN E CD  1 
ATOM   4532 O OE1 . GLN D 4 178 ? 11.360 -17.864 -52.696 1.00 66.18  ? 177 GLN E OE1 1 
ATOM   4533 N NE2 . GLN D 4 178 ? 9.930  -19.528 -53.229 1.00 61.19  ? 177 GLN E NE2 1 
ATOM   4534 N N   . PRO D 4 179 ? 15.315 -22.785 -53.395 1.00 36.50  ? 178 PRO E N   1 
ATOM   4535 C CA  . PRO D 4 179 ? 15.098 -24.190 -53.741 1.00 33.80  ? 178 PRO E CA  1 
ATOM   4536 C C   . PRO D 4 179 ? 13.617 -24.534 -53.653 1.00 40.12  ? 178 PRO E C   1 
ATOM   4537 O O   . PRO D 4 179 ? 12.818 -23.821 -53.044 1.00 46.20  ? 178 PRO E O   1 
ATOM   4538 C CB  . PRO D 4 179 ? 15.914 -24.944 -52.685 1.00 38.48  ? 178 PRO E CB  1 
ATOM   4539 C CG  . PRO D 4 179 ? 17.005 -23.953 -52.289 1.00 36.32  ? 178 PRO E CG  1 
ATOM   4540 C CD  . PRO D 4 179 ? 16.351 -22.607 -52.359 1.00 35.91  ? 178 PRO E CD  1 
ATOM   4541 N N   . LEU D 4 180 ? 13.232 -25.619 -54.306 1.00 35.92  ? 179 LEU E N   1 
ATOM   4542 C CA  . LEU D 4 180 ? 11.865 -26.085 -54.166 1.00 35.70  ? 179 LEU E CA  1 
ATOM   4543 C C   . LEU D 4 180 ? 11.858 -27.497 -53.593 1.00 36.54  ? 179 LEU E C   1 
ATOM   4544 O O   . LEU D 4 180 ? 12.828 -28.254 -53.729 1.00 32.30  ? 179 LEU E O   1 
ATOM   4545 C CB  . LEU D 4 180 ? 11.116 -26.027 -55.494 1.00 33.50  ? 179 LEU E CB  1 
ATOM   4546 C CG  . LEU D 4 180 ? 11.657 -26.741 -56.718 1.00 35.17  ? 179 LEU E CG  1 
ATOM   4547 C CD1 . LEU D 4 180 ? 11.359 -28.235 -56.645 1.00 34.95  ? 179 LEU E CD1 1 
ATOM   4548 C CD2 . LEU D 4 180 ? 10.992 -26.117 -57.935 1.00 36.44  ? 179 LEU E CD2 1 
ATOM   4549 N N   . LYS D 4 181 ? 10.735 -27.845 -52.967 1.00 31.17  ? 180 LYS E N   1 
ATOM   4550 C CA  . LYS D 4 181 ? 10.612 -29.128 -52.293 1.00 32.54  ? 180 LYS E CA  1 
ATOM   4551 C C   . LYS D 4 181 ? 10.352 -30.222 -53.313 1.00 29.08  ? 180 LYS E C   1 
ATOM   4552 O O   . LYS D 4 181 ? 9.539  -30.054 -54.225 1.00 32.99  ? 180 LYS E O   1 
ATOM   4553 C CB  . LYS D 4 181 ? 9.493  -29.087 -51.252 1.00 31.78  ? 180 LYS E CB  1 
ATOM   4554 C CG  . LYS D 4 181 ? 9.792  -28.157 -50.081 1.00 36.84  ? 180 LYS E CG  1 
ATOM   4555 C CD  . LYS D 4 181 ? 8.711  -28.195 -49.013 1.00 38.61  ? 180 LYS E CD  1 
ATOM   4556 C CE  . LYS D 4 181 ? 9.115  -27.321 -47.821 1.00 42.56  ? 180 LYS E CE  1 
ATOM   4557 N NZ  . LYS D 4 181 ? 8.653  -27.875 -46.513 1.00 43.20  ? 180 LYS E NZ  1 
ATOM   4558 N N   . GLU D 4 182 ? 11.055 -31.340 -53.167 1.00 28.30  ? 181 GLU E N   1 
ATOM   4559 C CA  . GLU D 4 182 ? 10.793 -32.472 -54.043 1.00 34.57  ? 181 GLU E CA  1 
ATOM   4560 C C   . GLU D 4 182 ? 9.517  -33.207 -53.647 1.00 36.21  ? 181 GLU E C   1 
ATOM   4561 O O   . GLU D 4 182 ? 8.815  -33.719 -54.517 1.00 38.02  ? 181 GLU E O   1 
ATOM   4562 C CB  . GLU D 4 182 ? 11.992 -33.407 -54.045 1.00 32.03  ? 181 GLU E CB  1 
ATOM   4563 C CG  . GLU D 4 182 ? 13.242 -32.777 -54.668 1.00 33.48  ? 181 GLU E CG  1 
ATOM   4564 C CD  . GLU D 4 182 ? 14.396 -33.756 -54.731 1.00 35.49  ? 181 GLU E CD  1 
ATOM   4565 O OE1 . GLU D 4 182 ? 14.370 -34.724 -53.938 1.00 36.52  ? 181 GLU E OE1 1 
ATOM   4566 O OE2 . GLU D 4 182 ? 15.311 -33.580 -55.578 1.00 32.92  ? 181 GLU E OE2 1 
ATOM   4567 N N   . GLN D 4 183 ? 9.179  -33.224 -52.355 1.00 40.07  ? 182 GLN E N   1 
ATOM   4568 C CA  . GLN D 4 183 ? 7.928  -33.800 -51.847 1.00 41.70  ? 182 GLN E CA  1 
ATOM   4569 C C   . GLN D 4 183 ? 7.221  -32.762 -50.987 1.00 37.40  ? 182 GLN E C   1 
ATOM   4570 O O   . GLN D 4 183 ? 7.319  -32.793 -49.753 1.00 38.13  ? 182 GLN E O   1 
ATOM   4571 C CB  . GLN D 4 183 ? 8.184  -35.066 -51.027 1.00 42.24  ? 182 GLN E CB  1 
ATOM   4572 C CG  . GLN D 4 183 ? 9.050  -36.099 -51.711 1.00 41.96  ? 182 GLN E CG  1 
ATOM   4573 C CD  . GLN D 4 183 ? 8.385  -36.676 -52.936 1.00 53.63  ? 182 GLN E CD  1 
ATOM   4574 O OE1 . GLN D 4 183 ? 7.158  -36.809 -52.981 1.00 57.92  ? 182 GLN E OE1 1 
ATOM   4575 N NE2 . GLN D 4 183 ? 9.190  -37.045 -53.936 1.00 52.91  ? 182 GLN E NE2 1 
ATOM   4576 N N   . PRO D 4 184 ? 6.469  -31.842 -51.601 1.00 39.51  ? 183 PRO E N   1 
ATOM   4577 C CA  . PRO D 4 184 ? 5.897  -30.723 -50.826 1.00 41.23  ? 183 PRO E CA  1 
ATOM   4578 C C   . PRO D 4 184 ? 4.914  -31.153 -49.744 1.00 46.73  ? 183 PRO E C   1 
ATOM   4579 O O   . PRO D 4 184 ? 4.534  -30.314 -48.919 1.00 43.52  ? 183 PRO E O   1 
ATOM   4580 C CB  . PRO D 4 184 ? 5.198  -29.862 -51.890 1.00 43.25  ? 183 PRO E CB  1 
ATOM   4581 C CG  . PRO D 4 184 ? 5.557  -30.472 -53.233 1.00 37.81  ? 183 PRO E CG  1 
ATOM   4582 C CD  . PRO D 4 184 ? 5.964  -31.884 -52.982 1.00 38.30  ? 183 PRO E CD  1 
ATOM   4583 N N   . ALA D 4 185 ? 4.493  -32.419 -49.714 1.00 45.68  ? 184 ALA E N   1 
ATOM   4584 C CA  . ALA D 4 185 ? 3.571  -32.868 -48.679 1.00 51.43  ? 184 ALA E CA  1 
ATOM   4585 C C   . ALA D 4 185 ? 4.266  -33.123 -47.347 1.00 52.48  ? 184 ALA E C   1 
ATOM   4586 O O   . ALA D 4 185 ? 3.621  -33.011 -46.297 1.00 57.74  ? 184 ALA E O   1 
ATOM   4587 C CB  . ALA D 4 185 ? 2.839  -34.134 -49.136 1.00 54.26  ? 184 ALA E CB  1 
ATOM   4588 N N   . LEU D 4 186 ? 5.560  -33.437 -47.357 1.00 50.18  ? 185 LEU E N   1 
ATOM   4589 C CA  . LEU D 4 186 ? 6.301  -33.753 -46.143 1.00 52.25  ? 185 LEU E CA  1 
ATOM   4590 C C   . LEU D 4 186 ? 7.036  -32.525 -45.610 1.00 52.65  ? 185 LEU E C   1 
ATOM   4591 O O   . LEU D 4 186 ? 7.554  -31.710 -46.380 1.00 49.19  ? 185 LEU E O   1 
ATOM   4592 C CB  . LEU D 4 186 ? 7.287  -34.889 -46.410 1.00 50.42  ? 185 LEU E CB  1 
ATOM   4593 C CG  . LEU D 4 186 ? 6.742  -35.905 -47.415 1.00 52.87  ? 185 LEU E CG  1 
ATOM   4594 C CD1 . LEU D 4 186 ? 7.819  -36.882 -47.851 1.00 48.37  ? 185 LEU E CD1 1 
ATOM   4595 C CD2 . LEU D 4 186 ? 5.556  -36.645 -46.810 1.00 57.67  ? 185 LEU E CD2 1 
ATOM   4596 N N   . ASN D 4 187 ? 7.073  -32.390 -44.280 1.00 52.29  ? 186 ASN E N   1 
ATOM   4597 C CA  . ASN D 4 187 ? 7.840  -31.296 -43.688 1.00 58.44  ? 186 ASN E CA  1 
ATOM   4598 C C   . ASN D 4 187 ? 9.344  -31.517 -43.834 1.00 52.62  ? 186 ASN E C   1 
ATOM   4599 O O   . ASN D 4 187 ? 10.094 -30.547 -43.981 1.00 53.00  ? 186 ASN E O   1 
ATOM   4600 C CB  . ASN D 4 187 ? 7.473  -31.115 -42.213 1.00 61.96  ? 186 ASN E CB  1 
ATOM   4601 C CG  . ASN D 4 187 ? 5.974  -31.062 -41.988 1.00 68.55  ? 186 ASN E CG  1 
ATOM   4602 O OD1 . ASN D 4 187 ? 5.346  -30.004 -42.119 1.00 66.18  ? 186 ASN E OD1 1 
ATOM   4603 N ND2 . ASN D 4 187 ? 5.386  -32.214 -41.660 1.00 68.57  ? 186 ASN E ND2 1 
ATOM   4604 N N   . ASP D 4 188 ? 9.796  -32.774 -43.806 1.00 49.30  ? 187 ASP E N   1 
ATOM   4605 C CA  . ASP D 4 188 ? 11.201 -33.128 -43.977 1.00 46.59  ? 187 ASP E CA  1 
ATOM   4606 C C   . ASP D 4 188 ? 11.580 -33.332 -45.447 1.00 45.61  ? 187 ASP E C   1 
ATOM   4607 O O   . ASP D 4 188 ? 12.564 -34.025 -45.745 1.00 42.76  ? 187 ASP E O   1 
ATOM   4608 C CB  . ASP D 4 188 ? 11.535 -34.384 -43.151 1.00 52.48  ? 187 ASP E CB  1 
ATOM   4609 C CG  . ASP D 4 188 ? 10.702 -35.618 -43.555 1.00 59.48  ? 187 ASP E CG  1 
ATOM   4610 O OD1 . ASP D 4 188 ? 9.763  -35.493 -44.371 1.00 59.39  ? 187 ASP E OD1 1 
ATOM   4611 O OD2 . ASP D 4 188 ? 10.989 -36.725 -43.040 1.00 68.56  ? 187 ASP E OD2 1 
ATOM   4612 N N   . SER D 4 189 ? 10.825 -32.743 -46.369 1.00 41.22  ? 188 SER E N   1 
ATOM   4613 C CA  . SER D 4 189 ? 11.093 -32.938 -47.784 1.00 38.71  ? 188 SER E CA  1 
ATOM   4614 C C   . SER D 4 189 ? 12.494 -32.466 -48.154 1.00 32.43  ? 188 SER E C   1 
ATOM   4615 O O   . SER D 4 189 ? 12.969 -31.428 -47.681 1.00 32.86  ? 188 SER E O   1 
ATOM   4616 C CB  . SER D 4 189 ? 10.070 -32.177 -48.617 1.00 35.31  ? 188 SER E CB  1 
ATOM   4617 O OG  . SER D 4 189 ? 10.572 -31.952 -49.913 1.00 30.17  ? 188 SER E OG  1 
ATOM   4618 N N   . ARG D 4 190 ? 13.151 -33.229 -49.015 1.00 26.75  ? 189 ARG E N   1 
ATOM   4619 C CA  . ARG D 4 190 ? 14.379 -32.754 -49.630 1.00 30.31  ? 189 ARG E CA  1 
ATOM   4620 C C   . ARG D 4 190 ? 14.073 -31.754 -50.747 1.00 28.84  ? 189 ARG E C   1 
ATOM   4621 O O   . ARG D 4 190 ? 12.925 -31.564 -51.157 1.00 25.19  ? 189 ARG E O   1 
ATOM   4622 C CB  . ARG D 4 190 ? 15.185 -33.921 -50.170 1.00 30.93  ? 189 ARG E CB  1 
ATOM   4623 C CG  . ARG D 4 190 ? 15.434 -35.012 -49.141 1.00 33.01  ? 189 ARG E CG  1 
ATOM   4624 C CD  . ARG D 4 190 ? 16.493 -35.907 -49.711 1.00 34.56  ? 189 ARG E CD  1 
ATOM   4625 N NE  . ARG D 4 190 ? 16.311 -37.315 -49.438 1.00 43.09  ? 189 ARG E NE  1 
ATOM   4626 C CZ  . ARG D 4 190 ? 17.048 -38.251 -50.023 1.00 44.21  ? 189 ARG E CZ  1 
ATOM   4627 N NH1 . ARG D 4 190 ? 16.852 -39.526 -49.734 1.00 42.00  ? 189 ARG E NH1 1 
ATOM   4628 N NH2 . ARG D 4 190 ? 17.992 -37.893 -50.901 1.00 38.03  ? 189 ARG E NH2 1 
ATOM   4629 N N   . TYR D 4 191 ? 15.133 -31.117 -51.247 1.00 25.09  ? 190 TYR E N   1 
ATOM   4630 C CA  . TYR D 4 191 ? 15.017 -29.934 -52.084 1.00 27.25  ? 190 TYR E CA  1 
ATOM   4631 C C   . TYR D 4 191 ? 15.736 -30.129 -53.410 1.00 27.06  ? 190 TYR E C   1 
ATOM   4632 O O   . TYR D 4 191 ? 16.603 -30.993 -53.555 1.00 21.74  ? 190 TYR E O   1 
ATOM   4633 C CB  . TYR D 4 191 ? 15.612 -28.702 -51.398 1.00 26.92  ? 190 TYR E CB  1 
ATOM   4634 C CG  . TYR D 4 191 ? 14.878 -28.257 -50.148 1.00 29.39  ? 190 TYR E CG  1 
ATOM   4635 C CD1 . TYR D 4 191 ? 15.228 -28.753 -48.898 1.00 27.04  ? 190 TYR E CD1 1 
ATOM   4636 C CD2 . TYR D 4 191 ? 13.847 -27.329 -50.224 1.00 25.12  ? 190 TYR E CD2 1 
ATOM   4637 C CE1 . TYR D 4 191 ? 14.557 -28.334 -47.744 1.00 32.96  ? 190 TYR E CE1 1 
ATOM   4638 C CE2 . TYR D 4 191 ? 13.175 -26.906 -49.093 1.00 34.30  ? 190 TYR E CE2 1 
ATOM   4639 C CZ  . TYR D 4 191 ? 13.534 -27.401 -47.855 1.00 34.61  ? 190 TYR E CZ  1 
ATOM   4640 O OH  . TYR D 4 191 ? 12.843 -26.978 -46.747 1.00 38.05  ? 190 TYR E OH  1 
ATOM   4641 N N   . ALA D 4 192 ? 15.387 -29.266 -54.361 1.00 24.70  ? 191 ALA E N   1 
ATOM   4642 C CA  . ALA D 4 192 ? 16.076 -29.180 -55.634 1.00 28.03  ? 191 ALA E CA  1 
ATOM   4643 C C   . ALA D 4 192 ? 16.270 -27.712 -55.978 1.00 28.36  ? 191 ALA E C   1 
ATOM   4644 O O   . ALA D 4 192 ? 15.471 -26.856 -55.591 1.00 29.45  ? 191 ALA E O   1 
ATOM   4645 C CB  . ALA D 4 192 ? 15.308 -29.899 -56.767 1.00 22.78  ? 191 ALA E CB  1 
ATOM   4646 N N   . LEU D 4 193 ? 17.339 -27.433 -56.714 1.00 28.94  ? 192 LEU E N   1 
ATOM   4647 C CA  . LEU D 4 193 ? 17.684 -26.081 -57.119 1.00 24.67  ? 192 LEU E CA  1 
ATOM   4648 C C   . LEU D 4 193 ? 18.213 -26.144 -58.543 1.00 26.31  ? 192 LEU E C   1 
ATOM   4649 O O   . LEU D 4 193 ? 18.946 -27.074 -58.885 1.00 26.85  ? 192 LEU E O   1 
ATOM   4650 C CB  . LEU D 4 193 ? 18.739 -25.476 -56.179 1.00 23.64  ? 192 LEU E CB  1 
ATOM   4651 C CG  . LEU D 4 193 ? 19.090 -24.007 -56.451 1.00 30.48  ? 192 LEU E CG  1 
ATOM   4652 C CD1 . LEU D 4 193 ? 17.907 -23.134 -56.120 1.00 30.01  ? 192 LEU E CD1 1 
ATOM   4653 C CD2 . LEU D 4 193 ? 20.288 -23.572 -55.641 1.00 25.03  ? 192 LEU E CD2 1 
ATOM   4654 N N   . SER D 4 194 ? 17.839 -25.169 -59.372 1.00 23.70  ? 193 SER E N   1 
ATOM   4655 C CA  . SER D 4 194 ? 18.358 -25.089 -60.731 1.00 27.48  ? 193 SER E CA  1 
ATOM   4656 C C   . SER D 4 194 ? 18.988 -23.728 -61.007 1.00 24.99  ? 193 SER E C   1 
ATOM   4657 O O   . SER D 4 194 ? 18.698 -22.731 -60.349 1.00 26.11  ? 193 SER E O   1 
ATOM   4658 C CB  . SER D 4 194 ? 17.271 -25.354 -61.780 1.00 24.28  ? 193 SER E CB  1 
ATOM   4659 O OG  . SER D 4 194 ? 16.437 -24.232 -61.940 1.00 26.80  ? 193 SER E OG  1 
ATOM   4660 N N   . SER D 4 195 ? 19.841 -23.706 -62.024 1.00 26.27  ? 194 SER E N   1 
ATOM   4661 C CA  . SER D 4 195 ? 20.553 -22.510 -62.438 1.00 25.30  ? 194 SER E CA  1 
ATOM   4662 C C   . SER D 4 195 ? 20.879 -22.650 -63.919 1.00 26.78  ? 194 SER E C   1 
ATOM   4663 O O   . SER D 4 195 ? 21.117 -23.760 -64.402 1.00 27.68  ? 194 SER E O   1 
ATOM   4664 C CB  . SER D 4 195 ? 21.828 -22.332 -61.605 1.00 22.90  ? 194 SER E CB  1 
ATOM   4665 O OG  . SER D 4 195 ? 22.539 -21.166 -61.939 1.00 21.38  ? 194 SER E OG  1 
ATOM   4666 N N   . ARG D 4 196 ? 20.881 -21.521 -64.633 1.00 22.76  ? 195 ARG E N   1 
ATOM   4667 C CA  . ARG D 4 196 ? 21.246 -21.463 -66.040 1.00 26.50  ? 195 ARG E CA  1 
ATOM   4668 C C   . ARG D 4 196 ? 22.488 -20.603 -66.238 1.00 28.50  ? 195 ARG E C   1 
ATOM   4669 O O   . ARG D 4 196 ? 22.667 -19.580 -65.567 1.00 27.02  ? 195 ARG E O   1 
ATOM   4670 C CB  . ARG D 4 196 ? 20.105 -20.887 -66.910 1.00 29.78  ? 195 ARG E CB  1 
ATOM   4671 C CG  . ARG D 4 196 ? 18.692 -21.311 -66.474 1.00 32.08  ? 195 ARG E CG  1 
ATOM   4672 C CD  . ARG D 4 196 ? 18.063 -20.225 -65.632 1.00 29.55  ? 195 ARG E CD  1 
ATOM   4673 N NE  . ARG D 4 196 ? 16.650 -20.481 -65.384 1.00 38.87  ? 195 ARG E NE  1 
ATOM   4674 C CZ  . ARG D 4 196 ? 16.172 -20.966 -64.242 1.00 42.03  ? 195 ARG E CZ  1 
ATOM   4675 N NH1 . ARG D 4 196 ? 14.866 -21.160 -64.097 1.00 39.10  ? 195 ARG E NH1 1 
ATOM   4676 N NH2 . ARG D 4 196 ? 16.999 -21.238 -63.237 1.00 36.80  ? 195 ARG E NH2 1 
ATOM   4677 N N   . LEU D 4 197 ? 23.332 -21.016 -67.179 1.00 23.97  ? 196 LEU E N   1 
ATOM   4678 C CA  . LEU D 4 197 ? 24.420 -20.194 -67.690 1.00 25.33  ? 196 LEU E CA  1 
ATOM   4679 C C   . LEU D 4 197 ? 24.274 -20.104 -69.204 1.00 26.55  ? 196 LEU E C   1 
ATOM   4680 O O   . LEU D 4 197 ? 24.325 -21.126 -69.905 1.00 26.03  ? 196 LEU E O   1 
ATOM   4681 C CB  . LEU D 4 197 ? 25.788 -20.780 -67.329 1.00 21.26  ? 196 LEU E CB  1 
ATOM   4682 C CG  . LEU D 4 197 ? 26.943 -20.149 -68.117 1.00 23.16  ? 196 LEU E CG  1 
ATOM   4683 C CD1 . LEU D 4 197 ? 27.094 -18.686 -67.729 1.00 26.78  ? 196 LEU E CD1 1 
ATOM   4684 C CD2 . LEU D 4 197 ? 28.256 -20.907 -67.919 1.00 22.16  ? 196 LEU E CD2 1 
ATOM   4685 N N   . ARG D 4 198 ? 24.122 -18.901 -69.720 1.00 21.54  ? 197 ARG E N   1 
ATOM   4686 C CA  . ARG D 4 198 ? 23.998 -18.738 -71.157 1.00 25.23  ? 197 ARG E CA  1 
ATOM   4687 C C   . ARG D 4 198 ? 25.274 -18.132 -71.710 1.00 24.66  ? 197 ARG E C   1 
ATOM   4688 O O   . ARG D 4 198 ? 25.755 -17.115 -71.198 1.00 24.51  ? 197 ARG E O   1 
ATOM   4689 C CB  . ARG D 4 198 ? 22.788 -17.873 -71.510 1.00 29.50  ? 197 ARG E CB  1 
ATOM   4690 C CG  . ARG D 4 198 ? 22.284 -18.094 -72.913 1.00 25.90  ? 197 ARG E CG  1 
ATOM   4691 C CD  . ARG D 4 198 ? 20.890 -17.513 -73.108 1.00 25.21  ? 197 ARG E CD  1 
ATOM   4692 N NE  . ARG D 4 198 ? 20.272 -18.054 -74.319 1.00 29.20  ? 197 ARG E NE  1 
ATOM   4693 C CZ  . ARG D 4 198 ? 19.125 -17.622 -74.839 1.00 32.57  ? 197 ARG E CZ  1 
ATOM   4694 N NH1 . ARG D 4 198 ? 18.464 -16.614 -74.270 1.00 24.45  ? 197 ARG E NH1 1 
ATOM   4695 N NH2 . ARG D 4 198 ? 18.647 -18.195 -75.940 1.00 32.18  ? 197 ARG E NH2 1 
ATOM   4696 N N   . VAL D 4 199 ? 25.819 -18.758 -72.754 1.00 25.27  ? 198 VAL E N   1 
ATOM   4697 C CA  . VAL D 4 199 ? 26.979 -18.243 -73.467 1.00 24.05  ? 198 VAL E CA  1 
ATOM   4698 C C   . VAL D 4 199 ? 26.658 -18.211 -74.959 1.00 29.93  ? 198 VAL E C   1 
ATOM   4699 O O   . VAL D 4 199 ? 25.653 -18.751 -75.414 1.00 23.16  ? 198 VAL E O   1 
ATOM   4700 C CB  . VAL D 4 199 ? 28.250 -19.087 -73.217 1.00 24.34  ? 198 VAL E CB  1 
ATOM   4701 C CG1 . VAL D 4 199 ? 28.620 -19.077 -71.746 1.00 20.66  ? 198 VAL E CG1 1 
ATOM   4702 C CG2 . VAL D 4 199 ? 28.045 -20.536 -73.723 1.00 23.02  ? 198 VAL E CG2 1 
ATOM   4703 N N   . SER D 4 200 ? 27.557 -17.588 -75.719 1.00 31.83  ? 199 SER E N   1 
ATOM   4704 C CA  . SER D 4 200 ? 27.441 -17.572 -77.161 1.00 32.11  ? 199 SER E CA  1 
ATOM   4705 C C   . SER D 4 200 ? 27.717 -18.967 -77.709 1.00 30.10  ? 199 SER E C   1 
ATOM   4706 O O   . SER D 4 200 ? 28.414 -19.779 -77.086 1.00 27.37  ? 199 SER E O   1 
ATOM   4707 C CB  . SER D 4 200 ? 28.419 -16.566 -77.759 1.00 32.55  ? 199 SER E CB  1 
ATOM   4708 O OG  . SER D 4 200 ? 29.606 -17.237 -78.167 1.00 33.73  ? 199 SER E OG  1 
ATOM   4709 N N   . ALA D 4 201 ? 27.139 -19.245 -78.879 1.00 24.47  ? 200 ALA E N   1 
ATOM   4710 C CA  . ALA D 4 201 ? 27.390 -20.517 -79.560 1.00 31.82  ? 200 ALA E CA  1 
ATOM   4711 C C   . ALA D 4 201 ? 28.877 -20.723 -79.843 1.00 27.20  ? 200 ALA E C   1 
ATOM   4712 O O   . ALA D 4 201 ? 29.398 -21.826 -79.650 1.00 30.33  ? 200 ALA E O   1 
ATOM   4713 C CB  . ALA D 4 201 ? 26.593 -20.592 -80.866 1.00 31.61  ? 200 ALA E CB  1 
ATOM   4714 N N   . THR D 4 202 ? 29.580 -19.678 -80.294 1.00 26.27  ? 201 THR E N   1 
ATOM   4715 C CA  . THR D 4 202 ? 31.006 -19.832 -80.581 1.00 28.35  ? 201 THR E CA  1 
ATOM   4716 C C   . THR D 4 202 ? 31.804 -20.158 -79.322 1.00 29.75  ? 201 THR E C   1 
ATOM   4717 O O   . THR D 4 202 ? 32.768 -20.930 -79.382 1.00 31.13  ? 201 THR E O   1 
ATOM   4718 C CB  . THR D 4 202 ? 31.569 -18.579 -81.256 1.00 31.12  ? 201 THR E CB  1 
ATOM   4719 O OG1 . THR D 4 202 ? 30.935 -17.406 -80.725 1.00 37.48  ? 201 THR E OG1 1 
ATOM   4720 C CG2 . THR D 4 202 ? 31.313 -18.636 -82.756 1.00 36.75  ? 201 THR E CG2 1 
ATOM   4721 N N   . PHE D 4 203 ? 31.418 -19.594 -78.179 1.00 30.69  ? 202 PHE E N   1 
ATOM   4722 C CA  . PHE D 4 203 ? 32.069 -19.963 -76.925 1.00 28.89  ? 202 PHE E CA  1 
ATOM   4723 C C   . PHE D 4 203 ? 31.757 -21.405 -76.555 1.00 25.88  ? 202 PHE E C   1 
ATOM   4724 O O   . PHE D 4 203 ? 32.651 -22.147 -76.137 1.00 23.11  ? 202 PHE E O   1 
ATOM   4725 C CB  . PHE D 4 203 ? 31.635 -19.016 -75.805 1.00 23.67  ? 202 PHE E CB  1 
ATOM   4726 C CG  . PHE D 4 203 ? 32.533 -19.043 -74.584 1.00 27.99  ? 202 PHE E CG  1 
ATOM   4727 C CD1 . PHE D 4 203 ? 33.651 -18.222 -74.507 1.00 26.96  ? 202 PHE E CD1 1 
ATOM   4728 C CD2 . PHE D 4 203 ? 32.236 -19.862 -73.498 1.00 25.64  ? 202 PHE E CD2 1 
ATOM   4729 C CE1 . PHE D 4 203 ? 34.456 -18.229 -73.385 1.00 27.39  ? 202 PHE E CE1 1 
ATOM   4730 C CE2 . PHE D 4 203 ? 33.040 -19.865 -72.369 1.00 24.51  ? 202 PHE E CE2 1 
ATOM   4731 C CZ  . PHE D 4 203 ? 34.145 -19.046 -72.312 1.00 22.74  ? 202 PHE E CZ  1 
ATOM   4732 N N   . TRP D 4 204 ? 30.496 -21.834 -76.709 1.00 25.82  ? 203 TRP E N   1 
ATOM   4733 C CA  . TRP D 4 204 ? 30.203 -23.226 -76.385 1.00 24.74  ? 203 TRP E CA  1 
ATOM   4734 C C   . TRP D 4 204 ? 30.898 -24.175 -77.355 1.00 27.73  ? 203 TRP E C   1 
ATOM   4735 O O   . TRP D 4 204 ? 31.205 -25.313 -76.986 1.00 26.79  ? 203 TRP E O   1 
ATOM   4736 C CB  . TRP D 4 204 ? 28.696 -23.503 -76.368 1.00 22.19  ? 203 TRP E CB  1 
ATOM   4737 C CG  . TRP D 4 204 ? 28.420 -24.981 -76.403 1.00 24.14  ? 203 TRP E CG  1 
ATOM   4738 C CD1 . TRP D 4 204 ? 28.036 -25.728 -77.498 1.00 29.04  ? 203 TRP E CD1 1 
ATOM   4739 C CD2 . TRP D 4 204 ? 28.590 -25.914 -75.329 1.00 26.57  ? 203 TRP E CD2 1 
ATOM   4740 N NE1 . TRP D 4 204 ? 27.935 -27.051 -77.155 1.00 26.74  ? 203 TRP E NE1 1 
ATOM   4741 C CE2 . TRP D 4 204 ? 28.268 -27.197 -75.834 1.00 25.56  ? 203 TRP E CE2 1 
ATOM   4742 C CE3 . TRP D 4 204 ? 28.976 -25.793 -73.985 1.00 27.06  ? 203 TRP E CE3 1 
ATOM   4743 C CZ2 . TRP D 4 204 ? 28.312 -28.343 -75.044 1.00 21.92  ? 203 TRP E CZ2 1 
ATOM   4744 C CZ3 . TRP D 4 204 ? 29.020 -26.943 -73.199 1.00 24.27  ? 203 TRP E CZ3 1 
ATOM   4745 C CH2 . TRP D 4 204 ? 28.690 -28.198 -73.736 1.00 25.98  ? 203 TRP E CH2 1 
ATOM   4746 N N   . GLN D 4 205 ? 31.194 -23.721 -78.572 1.00 27.72  ? 204 GLN E N   1 
ATOM   4747 C CA  . GLN D 4 205 ? 31.748 -24.602 -79.594 1.00 32.36  ? 204 GLN E CA  1 
ATOM   4748 C C   . GLN D 4 205 ? 33.269 -24.731 -79.515 1.00 31.03  ? 204 GLN E C   1 
ATOM   4749 O O   . GLN D 4 205 ? 33.857 -25.493 -80.288 1.00 32.06  ? 204 GLN E O   1 
ATOM   4750 C CB  . GLN D 4 205 ? 31.309 -24.120 -80.986 1.00 32.01  ? 204 GLN E CB  1 
ATOM   4751 C CG  . GLN D 4 205 ? 29.844 -24.466 -81.291 1.00 32.74  ? 204 GLN E CG  1 
ATOM   4752 C CD  . GLN D 4 205 ? 29.239 -23.654 -82.436 1.00 39.29  ? 204 GLN E CD  1 
ATOM   4753 O OE1 . GLN D 4 205 ? 29.742 -22.591 -82.800 1.00 37.24  ? 204 GLN E OE1 1 
ATOM   4754 N NE2 . GLN D 4 205 ? 28.139 -24.148 -82.991 1.00 40.86  ? 204 GLN E NE2 1 
ATOM   4755 N N   . ASN D 4 206 ? 33.916 -24.021 -78.601 1.00 28.41  ? 205 ASN E N   1 
ATOM   4756 C CA  . ASN D 4 206 ? 35.354 -24.152 -78.424 1.00 24.42  ? 205 ASN E CA  1 
ATOM   4757 C C   . ASN D 4 206 ? 35.619 -25.269 -77.422 1.00 27.05  ? 205 ASN E C   1 
ATOM   4758 O O   . ASN D 4 206 ? 35.169 -25.170 -76.271 1.00 26.75  ? 205 ASN E O   1 
ATOM   4759 C CB  . ASN D 4 206 ? 35.939 -22.835 -77.947 1.00 28.87  ? 205 ASN E CB  1 
ATOM   4760 C CG  . ASN D 4 206 ? 37.428 -22.898 -77.722 1.00 24.77  ? 205 ASN E CG  1 
ATOM   4761 O OD1 . ASN D 4 206 ? 38.055 -23.945 -77.880 1.00 27.30  ? 205 ASN E OD1 1 
ATOM   4762 N ND2 . ASN D 4 206 ? 38.014 -21.757 -77.364 1.00 24.57  ? 205 ASN E ND2 1 
ATOM   4763 N N   . PRO D 4 207 ? 36.289 -26.358 -77.816 1.00 29.28  ? 206 PRO E N   1 
ATOM   4764 C CA  . PRO D 4 207 ? 36.462 -27.489 -76.886 1.00 28.17  ? 206 PRO E CA  1 
ATOM   4765 C C   . PRO D 4 207 ? 37.461 -27.222 -75.763 1.00 27.92  ? 206 PRO E C   1 
ATOM   4766 O O   . PRO D 4 207 ? 37.516 -28.008 -74.813 1.00 25.03  ? 206 PRO E O   1 
ATOM   4767 C CB  . PRO D 4 207 ? 36.937 -28.634 -77.803 1.00 27.64  ? 206 PRO E CB  1 
ATOM   4768 C CG  . PRO D 4 207 ? 37.570 -27.937 -78.977 1.00 30.14  ? 206 PRO E CG  1 
ATOM   4769 C CD  . PRO D 4 207 ? 36.758 -26.680 -79.181 1.00 29.73  ? 206 PRO E CD  1 
ATOM   4770 N N   . ARG D 4 208 ? 38.187 -26.126 -75.794 1.00 27.04  ? 207 ARG E N   1 
ATOM   4771 C CA  . ARG D 4 208 ? 39.098 -25.815 -74.679 1.00 27.70  ? 207 ARG E CA  1 
ATOM   4772 C C   . ARG D 4 208 ? 38.360 -25.084 -73.572 1.00 26.74  ? 207 ARG E C   1 
ATOM   4773 O O   . ARG D 4 208 ? 38.908 -24.859 -72.576 1.00 32.48  ? 207 ARG E O   1 
ATOM   4774 C CB  . ARG D 4 208 ? 40.220 -24.903 -75.132 1.00 29.68  ? 207 ARG E CB  1 
ATOM   4775 C CG  . ARG D 4 208 ? 41.292 -25.649 -75.879 1.00 36.00  ? 207 ARG E CG  1 
ATOM   4776 C CD  . ARG D 4 208 ? 42.069 -24.491 -76.388 1.00 42.74  ? 207 ARG E CD  1 
ATOM   4777 N NE  . ARG D 4 208 ? 42.906 -24.996 -77.431 1.00 44.62  ? 207 ARG E NE  1 
ATOM   4778 C CZ  . ARG D 4 208 ? 43.443 -24.254 -78.361 1.00 45.60  ? 207 ARG E CZ  1 
ATOM   4779 N NH1 . ARG D 4 208 ? 44.183 -24.845 -79.259 1.00 40.65  ? 207 ARG E NH1 1 
ATOM   4780 N NH2 . ARG D 4 208 ? 43.264 -22.952 -78.380 1.00 37.38  ? 207 ARG E NH2 1 
ATOM   4781 N N   . ASN D 4 209 ? 37.143 -24.698 -73.801 1.00 27.77  ? 208 ASN E N   1 
ATOM   4782 C CA  . ASN D 4 209 ? 36.402 -24.034 -72.736 1.00 26.22  ? 208 ASN E CA  1 
ATOM   4783 C C   . ASN D 4 209 ? 35.805 -25.072 -71.801 1.00 25.06  ? 208 ASN E C   1 
ATOM   4784 O O   . ASN D 4 209 ? 35.263 -26.092 -72.243 1.00 23.43  ? 208 ASN E O   1 
ATOM   4785 C CB  . ASN D 4 209 ? 35.297 -23.143 -73.295 1.00 25.95  ? 208 ASN E CB  1 
ATOM   4786 C CG  . ASN D 4 209 ? 35.837 -21.881 -73.889 1.00 29.49  ? 208 ASN E CG  1 
ATOM   4787 O OD1 . ASN D 4 209 ? 36.943 -21.463 -73.557 1.00 28.22  ? 208 ASN E OD1 1 
ATOM   4788 N ND2 . ASN D 4 209 ? 35.075 -21.270 -74.792 1.00 29.83  ? 208 ASN E ND2 1 
ATOM   4789 N N   . HIS D 4 210 ? 35.921 -24.811 -70.506 1.00 24.48  ? 209 HIS E N   1 
ATOM   4790 C CA  . HIS D 4 210 ? 35.533 -25.753 -69.464 1.00 26.17  ? 209 HIS E CA  1 
ATOM   4791 C C   . HIS D 4 210 ? 34.467 -25.106 -68.585 1.00 24.21  ? 209 HIS E C   1 
ATOM   4792 O O   . HIS D 4 210 ? 34.572 -23.924 -68.244 1.00 24.32  ? 209 HIS E O   1 
ATOM   4793 C CB  . HIS D 4 210 ? 36.775 -26.163 -68.663 1.00 27.36  ? 209 HIS E CB  1 
ATOM   4794 C CG  . HIS D 4 210 ? 36.479 -26.942 -67.419 1.00 31.75  ? 209 HIS E CG  1 
ATOM   4795 N ND1 . HIS D 4 210 ? 36.411 -26.353 -66.176 1.00 28.90  ? 209 HIS E ND1 1 
ATOM   4796 C CD2 . HIS D 4 210 ? 36.260 -28.266 -67.223 1.00 32.26  ? 209 HIS E CD2 1 
ATOM   4797 C CE1 . HIS D 4 210 ? 36.157 -27.279 -65.266 1.00 29.74  ? 209 HIS E CE1 1 
ATOM   4798 N NE2 . HIS D 4 210 ? 36.053 -28.447 -65.876 1.00 30.41  ? 209 HIS E NE2 1 
ATOM   4799 N N   . PHE D 4 211 ? 33.425 -25.861 -68.246 1.00 23.57  ? 210 PHE E N   1 
ATOM   4800 C CA  . PHE D 4 211 ? 32.281 -25.323 -67.515 1.00 23.78  ? 210 PHE E CA  1 
ATOM   4801 C C   . PHE D 4 211 ? 32.059 -26.164 -66.268 1.00 25.02  ? 210 PHE E C   1 
ATOM   4802 O O   . PHE D 4 211 ? 31.972 -27.386 -66.357 1.00 25.59  ? 210 PHE E O   1 
ATOM   4803 C CB  . PHE D 4 211 ? 31.004 -25.328 -68.370 1.00 22.59  ? 210 PHE E CB  1 
ATOM   4804 C CG  . PHE D 4 211 ? 31.137 -24.600 -69.675 1.00 23.03  ? 210 PHE E CG  1 
ATOM   4805 C CD1 . PHE D 4 211 ? 31.685 -25.229 -70.787 1.00 23.55  ? 210 PHE E CD1 1 
ATOM   4806 C CD2 . PHE D 4 211 ? 30.722 -23.281 -69.790 1.00 22.94  ? 210 PHE E CD2 1 
ATOM   4807 C CE1 . PHE D 4 211 ? 31.805 -24.559 -71.994 1.00 23.66  ? 210 PHE E CE1 1 
ATOM   4808 C CE2 . PHE D 4 211 ? 30.836 -22.605 -70.997 1.00 20.04  ? 210 PHE E CE2 1 
ATOM   4809 C CZ  . PHE D 4 211 ? 31.382 -23.245 -72.098 1.00 24.43  ? 210 PHE E CZ  1 
ATOM   4810 N N   . ARG D 4 212 ? 31.979 -25.527 -65.111 1.00 20.72  ? 211 ARG E N   1 
ATOM   4811 C CA  . ARG D 4 212 ? 31.749 -26.261 -63.876 1.00 26.38  ? 211 ARG E CA  1 
ATOM   4812 C C   . ARG D 4 212 ? 30.596 -25.611 -63.124 1.00 23.47  ? 211 ARG E C   1 
ATOM   4813 O O   . ARG D 4 212 ? 30.607 -24.396 -62.888 1.00 22.04  ? 211 ARG E O   1 
ATOM   4814 C CB  . ARG D 4 212 ? 33.021 -26.304 -63.010 1.00 24.90  ? 211 ARG E CB  1 
ATOM   4815 C CG  . ARG D 4 212 ? 32.919 -27.177 -61.769 1.00 24.78  ? 211 ARG E CG  1 
ATOM   4816 C CD  . ARG D 4 212 ? 34.303 -27.507 -61.230 1.00 23.79  ? 211 ARG E CD  1 
ATOM   4817 N NE  . ARG D 4 212 ? 34.921 -26.280 -60.753 1.00 27.56  ? 211 ARG E NE  1 
ATOM   4818 C CZ  . ARG D 4 212 ? 34.735 -25.785 -59.536 1.00 29.13  ? 211 ARG E CZ  1 
ATOM   4819 N NH1 . ARG D 4 212 ? 33.991 -26.457 -58.655 1.00 27.23  ? 211 ARG E NH1 1 
ATOM   4820 N NH2 . ARG D 4 212 ? 35.313 -24.634 -59.194 1.00 27.80  ? 211 ARG E NH2 1 
ATOM   4821 N N   . CYS D 4 213 ? 29.587 -26.405 -62.787 1.00 22.14  ? 212 CYS E N   1 
ATOM   4822 C CA  . CYS D 4 213 ? 28.582 -26.007 -61.812 1.00 22.98  ? 212 CYS E CA  1 
ATOM   4823 C C   . CYS D 4 213 ? 28.978 -26.573 -60.444 1.00 21.87  ? 212 CYS E C   1 
ATOM   4824 O O   . CYS D 4 213 ? 29.226 -27.773 -60.313 1.00 22.36  ? 212 CYS E O   1 
ATOM   4825 C CB  . CYS D 4 213 ? 27.186 -26.497 -62.211 1.00 19.90  ? 212 CYS E CB  1 
ATOM   4826 S SG  . CYS D 4 213 ? 26.005 -26.061 -60.962 1.00 37.29  ? 212 CYS E SG  1 
ATOM   4827 N N   . GLN D 4 214 ? 29.034 -25.713 -59.435 1.00 21.36  ? 213 GLN E N   1 
ATOM   4828 C CA  . GLN D 4 214 ? 29.518 -26.084 -58.109 1.00 20.87  ? 213 GLN E CA  1 
ATOM   4829 C C   . GLN D 4 214 ? 28.451 -25.764 -57.072 1.00 21.44  ? 213 GLN E C   1 
ATOM   4830 O O   . GLN D 4 214 ? 27.903 -24.657 -57.058 1.00 21.88  ? 213 GLN E O   1 
ATOM   4831 C CB  . GLN D 4 214 ? 30.820 -25.356 -57.764 1.00 22.83  ? 213 GLN E CB  1 
ATOM   4832 C CG  . GLN D 4 214 ? 31.055 -25.267 -56.261 1.00 29.09  ? 213 GLN E CG  1 
ATOM   4833 C CD  . GLN D 4 214 ? 32.375 -24.619 -55.872 1.00 26.66  ? 213 GLN E CD  1 
ATOM   4834 O OE1 . GLN D 4 214 ? 33.450 -25.033 -56.310 1.00 28.58  ? 213 GLN E OE1 1 
ATOM   4835 N NE2 . GLN D 4 214 ? 32.292 -23.611 -55.022 1.00 26.09  ? 213 GLN E NE2 1 
ATOM   4836 N N   . VAL D 4 215 ? 28.147 -26.731 -56.214 1.00 19.71  ? 214 VAL E N   1 
ATOM   4837 C CA  . VAL D 4 215 ? 27.232 -26.513 -55.103 1.00 23.27  ? 214 VAL E CA  1 
ATOM   4838 C C   . VAL D 4 215 ? 27.984 -26.733 -53.790 1.00 22.14  ? 214 VAL E C   1 
ATOM   4839 O O   . VAL D 4 215 ? 28.468 -27.842 -53.505 1.00 20.30  ? 214 VAL E O   1 
ATOM   4840 C CB  . VAL D 4 215 ? 25.994 -27.416 -55.194 1.00 26.78  ? 214 VAL E CB  1 
ATOM   4841 C CG1 . VAL D 4 215 ? 25.182 -27.299 -53.919 1.00 22.73  ? 214 VAL E CG1 1 
ATOM   4842 C CG2 . VAL D 4 215 ? 25.158 -27.019 -56.399 1.00 21.85  ? 214 VAL E CG2 1 
ATOM   4843 N N   . GLN D 4 216 ? 28.088 -25.677 -52.998 1.00 21.57  ? 215 GLN E N   1 
ATOM   4844 C CA  . GLN D 4 216 ? 28.608 -25.781 -51.641 1.00 20.33  ? 215 GLN E CA  1 
ATOM   4845 C C   . GLN D 4 216 ? 27.454 -26.166 -50.715 1.00 20.67  ? 215 GLN E C   1 
ATOM   4846 O O   . GLN D 4 216 ? 26.463 -25.440 -50.621 1.00 20.21  ? 215 GLN E O   1 
ATOM   4847 C CB  . GLN D 4 216 ? 29.248 -24.460 -51.215 1.00 21.30  ? 215 GLN E CB  1 
ATOM   4848 C CG  . GLN D 4 216 ? 29.543 -24.381 -49.698 1.00 25.89  ? 215 GLN E CG  1 
ATOM   4849 C CD  . GLN D 4 216 ? 30.781 -25.170 -49.314 1.00 25.17  ? 215 GLN E CD  1 
ATOM   4850 O OE1 . GLN D 4 216 ? 31.900 -24.751 -49.633 1.00 24.73  ? 215 GLN E OE1 1 
ATOM   4851 N NE2 . GLN D 4 216 ? 30.593 -26.326 -48.643 1.00 18.32  ? 215 GLN E NE2 1 
ATOM   4852 N N   . PHE D 4 217 ? 27.563 -27.320 -50.063 1.00 23.77  ? 216 PHE E N   1 
ATOM   4853 C CA  . PHE D 4 217 ? 26.551 -27.785 -49.116 1.00 21.08  ? 216 PHE E CA  1 
ATOM   4854 C C   . PHE D 4 217 ? 27.074 -27.583 -47.697 1.00 21.87  ? 216 PHE E C   1 
ATOM   4855 O O   . PHE D 4 217 ? 28.195 -27.989 -47.379 1.00 23.10  ? 216 PHE E O   1 
ATOM   4856 C CB  . PHE D 4 217 ? 26.216 -29.260 -49.369 1.00 21.37  ? 216 PHE E CB  1 
ATOM   4857 C CG  . PHE D 4 217 ? 25.278 -29.886 -48.341 1.00 22.00  ? 216 PHE E CG  1 
ATOM   4858 C CD1 . PHE D 4 217 ? 23.950 -29.496 -48.250 1.00 22.49  ? 216 PHE E CD1 1 
ATOM   4859 C CD2 . PHE D 4 217 ? 25.729 -30.886 -47.486 1.00 24.62  ? 216 PHE E CD2 1 
ATOM   4860 C CE1 . PHE D 4 217 ? 23.094 -30.077 -47.327 1.00 21.68  ? 216 PHE E CE1 1 
ATOM   4861 C CE2 . PHE D 4 217 ? 24.878 -31.482 -46.552 1.00 21.42  ? 216 PHE E CE2 1 
ATOM   4862 C CZ  . PHE D 4 217 ? 23.563 -31.071 -46.468 1.00 22.82  ? 216 PHE E CZ  1 
ATOM   4863 N N   . TYR D 4 218 ? 26.270 -26.961 -46.848 1.00 23.48  ? 217 TYR E N   1 
ATOM   4864 C CA  . TYR D 4 218 ? 26.622 -26.788 -45.442 1.00 25.42  ? 217 TYR E CA  1 
ATOM   4865 C C   . TYR D 4 218 ? 25.868 -27.830 -44.628 1.00 26.23  ? 217 TYR E C   1 
ATOM   4866 O O   . TYR D 4 218 ? 24.641 -27.765 -44.507 1.00 27.68  ? 217 TYR E O   1 
ATOM   4867 C CB  . TYR D 4 218 ? 26.301 -25.379 -44.973 1.00 20.69  ? 217 TYR E CB  1 
ATOM   4868 C CG  . TYR D 4 218 ? 27.084 -24.332 -45.725 1.00 22.46  ? 217 TYR E CG  1 
ATOM   4869 C CD1 . TYR D 4 218 ? 28.344 -23.936 -45.287 1.00 21.49  ? 217 TYR E CD1 1 
ATOM   4870 C CD2 . TYR D 4 218 ? 26.576 -23.750 -46.887 1.00 22.86  ? 217 TYR E CD2 1 
ATOM   4871 C CE1 . TYR D 4 218 ? 29.080 -22.981 -45.970 1.00 22.44  ? 217 TYR E CE1 1 
ATOM   4872 C CE2 . TYR D 4 218 ? 27.310 -22.788 -47.586 1.00 23.40  ? 217 TYR E CE2 1 
ATOM   4873 C CZ  . TYR D 4 218 ? 28.556 -22.399 -47.115 1.00 25.04  ? 217 TYR E CZ  1 
ATOM   4874 O OH  . TYR D 4 218 ? 29.296 -21.443 -47.791 1.00 21.68  ? 217 TYR E OH  1 
ATOM   4875 N N   . GLY D 4 219 ? 26.597 -28.789 -44.079 1.00 25.44  ? 218 GLY E N   1 
ATOM   4876 C CA  . GLY D 4 219 ? 25.984 -29.923 -43.414 1.00 27.62  ? 218 GLY E CA  1 
ATOM   4877 C C   . GLY D 4 219 ? 26.603 -30.159 -42.050 1.00 26.73  ? 218 GLY E C   1 
ATOM   4878 O O   . GLY D 4 219 ? 26.912 -29.231 -41.312 1.00 28.12  ? 218 GLY E O   1 
ATOM   4879 N N   . LEU D 4 220 ? 26.759 -31.434 -41.715 1.00 26.20  ? 219 LEU E N   1 
ATOM   4880 C CA  . LEU D 4 220 ? 27.284 -31.803 -40.413 1.00 30.18  ? 219 LEU E CA  1 
ATOM   4881 C C   . LEU D 4 220 ? 28.766 -31.440 -40.317 1.00 32.22  ? 219 LEU E C   1 
ATOM   4882 O O   . LEU D 4 220 ? 29.476 -31.317 -41.323 1.00 29.67  ? 219 LEU E O   1 
ATOM   4883 C CB  . LEU D 4 220 ? 27.089 -33.300 -40.161 1.00 27.91  ? 219 LEU E CB  1 
ATOM   4884 C CG  . LEU D 4 220 ? 25.662 -33.871 -40.281 1.00 34.00  ? 219 LEU E CG  1 
ATOM   4885 C CD1 . LEU D 4 220 ? 25.562 -35.238 -39.600 1.00 26.74  ? 219 LEU E CD1 1 
ATOM   4886 C CD2 . LEU D 4 220 ? 24.610 -32.931 -39.730 1.00 26.25  ? 219 LEU E CD2 1 
ATOM   4887 N N   . SER D 4 221 ? 29.225 -31.238 -39.090 1.00 31.32  ? 220 SER E N   1 
ATOM   4888 C CA  . SER D 4 221 ? 30.654 -31.107 -38.846 1.00 33.98  ? 220 SER E CA  1 
ATOM   4889 C C   . SER D 4 221 ? 31.257 -32.480 -38.560 1.00 36.07  ? 220 SER E C   1 
ATOM   4890 O O   . SER D 4 221 ? 30.549 -33.476 -38.386 1.00 32.54  ? 220 SER E O   1 
ATOM   4891 C CB  . SER D 4 221 ? 30.925 -30.170 -37.667 1.00 35.21  ? 220 SER E CB  1 
ATOM   4892 O OG  . SER D 4 221 ? 29.999 -29.096 -37.607 1.00 39.94  ? 220 SER E OG  1 
ATOM   4893 N N   . GLU D 4 222 ? 32.589 -32.519 -38.479 1.00 32.24  ? 221 GLU E N   1 
ATOM   4894 C CA  . GLU D 4 222 ? 33.253 -33.762 -38.107 1.00 35.51  ? 221 GLU E CA  1 
ATOM   4895 C C   . GLU D 4 222 ? 32.775 -34.276 -36.759 1.00 37.88  ? 221 GLU E C   1 
ATOM   4896 O O   . GLU D 4 222 ? 32.503 -35.470 -36.618 1.00 39.97  ? 221 GLU E O   1 
ATOM   4897 C CB  . GLU D 4 222 ? 34.764 -33.573 -38.085 1.00 39.07  ? 221 GLU E CB  1 
ATOM   4898 C CG  . GLU D 4 222 ? 35.417 -33.998 -39.371 1.00 47.50  ? 221 GLU E CG  1 
ATOM   4899 C CD  . GLU D 4 222 ? 36.745 -34.683 -39.161 1.00 54.00  ? 221 GLU E CD  1 
ATOM   4900 O OE1 . GLU D 4 222 ? 37.546 -34.696 -40.124 1.00 50.82  ? 221 GLU E OE1 1 
ATOM   4901 O OE2 . GLU D 4 222 ? 36.976 -35.211 -38.044 1.00 57.01  ? 221 GLU E OE2 1 
ATOM   4902 N N   . ASN D 4 223 ? 32.662 -33.394 -35.755 1.00 32.11  ? 222 ASN E N   1 
ATOM   4903 C CA  . ASN D 4 223 ? 32.328 -33.842 -34.408 1.00 38.09  ? 222 ASN E CA  1 
ATOM   4904 C C   . ASN D 4 223 ? 30.836 -34.111 -34.201 1.00 35.41  ? 222 ASN E C   1 
ATOM   4905 O O   . ASN D 4 223 ? 30.437 -34.381 -33.070 1.00 33.56  ? 222 ASN E O   1 
ATOM   4906 C CB  . ASN D 4 223 ? 32.835 -32.834 -33.366 1.00 40.72  ? 222 ASN E CB  1 
ATOM   4907 C CG  . ASN D 4 223 ? 31.912 -31.654 -33.191 1.00 41.24  ? 222 ASN E CG  1 
ATOM   4908 O OD1 . ASN D 4 223 ? 31.205 -31.265 -34.115 1.00 39.98  ? 222 ASN E OD1 1 
ATOM   4909 N ND2 . ASN D 4 223 ? 31.911 -31.072 -31.989 1.00 38.74  ? 222 ASN E ND2 1 
ATOM   4910 N N   . ASP D 4 224 ? 30.008 -34.058 -35.243 1.00 36.18  ? 223 ASP E N   1 
ATOM   4911 C CA  . ASP D 4 224 ? 28.621 -34.479 -35.105 1.00 34.92  ? 223 ASP E CA  1 
ATOM   4912 C C   . ASP D 4 224 ? 28.538 -36.003 -35.073 1.00 38.50  ? 223 ASP E C   1 
ATOM   4913 O O   . ASP D 4 224 ? 29.256 -36.700 -35.796 1.00 38.50  ? 223 ASP E O   1 
ATOM   4914 C CB  . ASP D 4 224 ? 27.777 -33.932 -36.252 1.00 33.01  ? 223 ASP E CB  1 
ATOM   4915 C CG  . ASP D 4 224 ? 27.385 -32.481 -36.050 1.00 35.43  ? 223 ASP E CG  1 
ATOM   4916 O OD1 . ASP D 4 224 ? 26.904 -32.139 -34.940 1.00 29.48  ? 223 ASP E OD1 1 
ATOM   4917 O OD2 . ASP D 4 224 ? 27.561 -31.687 -37.007 1.00 31.77  ? 223 ASP E OD2 1 
ATOM   4918 N N   . GLU D 4 225 ? 27.671 -36.527 -34.218 1.00 39.14  ? 224 GLU E N   1 
ATOM   4919 C CA  . GLU D 4 225 ? 27.524 -37.970 -34.127 1.00 43.15  ? 224 GLU E CA  1 
ATOM   4920 C C   . GLU D 4 225 ? 26.781 -38.493 -35.351 1.00 40.73  ? 224 GLU E C   1 
ATOM   4921 O O   . GLU D 4 225 ? 25.847 -37.858 -35.846 1.00 39.53  ? 224 GLU E O   1 
ATOM   4922 C CB  . GLU D 4 225 ? 26.789 -38.352 -32.838 1.00 41.27  ? 224 GLU E CB  1 
ATOM   4923 C CG  . GLU D 4 225 ? 27.710 -38.607 -31.632 1.00 54.01  ? 224 GLU E CG  1 
ATOM   4924 C CD  . GLU D 4 225 ? 27.872 -37.385 -30.720 1.00 68.09  ? 224 GLU E CD  1 
ATOM   4925 O OE1 . GLU D 4 225 ? 27.451 -36.270 -31.123 1.00 64.68  ? 224 GLU E OE1 1 
ATOM   4926 O OE2 . GLU D 4 225 ? 28.421 -37.541 -29.599 1.00 65.88  ? 224 GLU E OE2 1 
ATOM   4927 N N   . TRP D 4 226 ? 27.222 -39.649 -35.853 1.00 38.97  ? 225 TRP E N   1 
ATOM   4928 C CA  . TRP D 4 226 ? 26.611 -40.302 -37.005 1.00 37.81  ? 225 TRP E CA  1 
ATOM   4929 C C   . TRP D 4 226 ? 26.672 -41.808 -36.793 1.00 43.58  ? 225 TRP E C   1 
ATOM   4930 O O   . TRP D 4 226 ? 27.761 -42.371 -36.646 1.00 42.83  ? 225 TRP E O   1 
ATOM   4931 C CB  . TRP D 4 226 ? 27.322 -39.916 -38.310 1.00 37.08  ? 225 TRP E CB  1 
ATOM   4932 C CG  . TRP D 4 226 ? 26.548 -40.268 -39.558 1.00 34.26  ? 225 TRP E CG  1 
ATOM   4933 C CD1 . TRP D 4 226 ? 26.884 -41.202 -40.501 1.00 33.64  ? 225 TRP E CD1 1 
ATOM   4934 C CD2 . TRP D 4 226 ? 25.319 -39.672 -40.003 1.00 31.91  ? 225 TRP E CD2 1 
ATOM   4935 N NE1 . TRP D 4 226 ? 25.930 -41.227 -41.504 1.00 34.43  ? 225 TRP E NE1 1 
ATOM   4936 C CE2 . TRP D 4 226 ? 24.961 -40.303 -41.216 1.00 30.43  ? 225 TRP E CE2 1 
ATOM   4937 C CE3 . TRP D 4 226 ? 24.490 -38.668 -39.494 1.00 30.34  ? 225 TRP E CE3 1 
ATOM   4938 C CZ2 . TRP D 4 226 ? 23.818 -39.958 -41.926 1.00 33.95  ? 225 TRP E CZ2 1 
ATOM   4939 C CZ3 . TRP D 4 226 ? 23.348 -38.332 -40.196 1.00 32.33  ? 225 TRP E CZ3 1 
ATOM   4940 C CH2 . TRP D 4 226 ? 23.022 -38.976 -41.404 1.00 35.09  ? 225 TRP E CH2 1 
ATOM   4941 N N   . THR D 4 227 ? 25.510 -42.459 -36.789 1.00 46.91  ? 226 THR E N   1 
ATOM   4942 C CA  . THR D 4 227 ? 25.429 -43.905 -36.603 1.00 48.10  ? 226 THR E CA  1 
ATOM   4943 C C   . THR D 4 227 ? 24.802 -44.626 -37.789 1.00 50.43  ? 226 THR E C   1 
ATOM   4944 O O   . THR D 4 227 ? 24.457 -45.803 -37.659 1.00 54.43  ? 226 THR E O   1 
ATOM   4945 C CB  . THR D 4 227 ? 24.620 -44.247 -35.346 1.00 48.39  ? 226 THR E CB  1 
ATOM   4946 O OG1 . THR D 4 227 ? 23.258 -43.808 -35.519 1.00 57.64  ? 226 THR E OG1 1 
ATOM   4947 C CG2 . THR D 4 227 ? 25.228 -43.593 -34.111 1.00 39.50  ? 226 THR E CG2 1 
ATOM   4948 N N   . GLN D 4 228 ? 24.621 -43.964 -38.925 1.00 43.12  ? 227 GLN E N   1 
ATOM   4949 C CA  . GLN D 4 228 ? 23.881 -44.568 -40.019 1.00 45.12  ? 227 GLN E CA  1 
ATOM   4950 C C   . GLN D 4 228 ? 24.819 -45.179 -41.051 1.00 51.08  ? 227 GLN E C   1 
ATOM   4951 O O   . GLN D 4 228 ? 26.023 -44.908 -41.086 1.00 50.06  ? 227 GLN E O   1 
ATOM   4952 C CB  . GLN D 4 228 ? 22.958 -43.546 -40.679 1.00 44.55  ? 227 GLN E CB  1 
ATOM   4953 C CG  . GLN D 4 228 ? 21.599 -43.424 -40.000 1.00 52.62  ? 227 GLN E CG  1 
ATOM   4954 C CD  . GLN D 4 228 ? 20.555 -42.857 -40.948 1.00 57.63  ? 227 GLN E CD  1 
ATOM   4955 O OE1 . GLN D 4 228 ? 19.826 -43.598 -41.609 1.00 60.59  ? 227 GLN E OE1 1 
ATOM   4956 N NE2 . GLN D 4 228 ? 20.503 -41.532 -41.044 1.00 49.26  ? 227 GLN E NE2 1 
ATOM   4957 N N   . ASP D 4 229 ? 24.228 -46.011 -41.912 1.00 51.33  ? 228 ASP E N   1 
ATOM   4958 C CA  . ASP D 4 229 ? 24.997 -46.771 -42.894 1.00 55.30  ? 228 ASP E CA  1 
ATOM   4959 C C   . ASP D 4 229 ? 25.596 -45.864 -43.962 1.00 52.89  ? 228 ASP E C   1 
ATOM   4960 O O   . ASP D 4 229 ? 26.779 -45.986 -44.302 1.00 57.94  ? 228 ASP E O   1 
ATOM   4961 C CB  . ASP D 4 229 ? 24.106 -47.838 -43.540 1.00 59.79  ? 228 ASP E CB  1 
ATOM   4962 C CG  . ASP D 4 229 ? 24.059 -49.134 -42.738 1.00 62.55  ? 228 ASP E CG  1 
ATOM   4963 O OD1 . ASP D 4 229 ? 24.651 -49.174 -41.635 1.00 66.42  ? 228 ASP E OD1 1 
ATOM   4964 O OD2 . ASP D 4 229 ? 23.420 -50.107 -43.209 1.00 67.03  ? 228 ASP E OD2 1 
ATOM   4965 N N   . ARG D 4 230 ? 24.797 -44.963 -44.521 1.00 41.95  ? 229 ARG E N   1 
ATOM   4966 C CA  . ARG D 4 230 ? 25.321 -44.092 -45.559 1.00 46.36  ? 229 ARG E CA  1 
ATOM   4967 C C   . ARG D 4 230 ? 26.369 -43.135 -44.985 1.00 41.34  ? 229 ARG E C   1 
ATOM   4968 O O   . ARG D 4 230 ? 26.529 -42.980 -43.763 1.00 37.31  ? 229 ARG E O   1 
ATOM   4969 C CB  . ARG D 4 230 ? 24.190 -43.316 -46.238 1.00 42.69  ? 229 ARG E CB  1 
ATOM   4970 C CG  . ARG D 4 230 ? 23.403 -42.417 -45.303 1.00 41.17  ? 229 ARG E CG  1 
ATOM   4971 C CD  . ARG D 4 230 ? 22.386 -41.597 -46.086 1.00 43.59  ? 229 ARG E CD  1 
ATOM   4972 N NE  . ARG D 4 230 ? 21.416 -40.970 -45.198 1.00 41.71  ? 229 ARG E NE  1 
ATOM   4973 C CZ  . ARG D 4 230 ? 21.470 -39.699 -44.820 1.00 39.35  ? 229 ARG E CZ  1 
ATOM   4974 N NH1 . ARG D 4 230 ? 22.438 -38.912 -45.269 1.00 36.09  ? 229 ARG E NH1 1 
ATOM   4975 N NH2 . ARG D 4 230 ? 20.545 -39.206 -44.012 1.00 37.82  ? 229 ARG E NH2 1 
ATOM   4976 N N   . ALA D 4 231 ? 27.105 -42.508 -45.899 1.00 35.83  ? 230 ALA E N   1 
ATOM   4977 C CA  . ALA D 4 231 ? 28.204 -41.628 -45.524 1.00 35.62  ? 230 ALA E CA  1 
ATOM   4978 C C   . ALA D 4 231 ? 27.686 -40.432 -44.739 1.00 35.39  ? 230 ALA E C   1 
ATOM   4979 O O   . ALA D 4 231 ? 26.594 -39.920 -45.001 1.00 36.68  ? 230 ALA E O   1 
ATOM   4980 C CB  . ALA D 4 231 ? 28.949 -41.151 -46.775 1.00 37.17  ? 230 ALA E CB  1 
ATOM   4981 N N   . LYS D 4 232 ? 28.469 -40.003 -43.761 1.00 37.22  ? 231 LYS E N   1 
ATOM   4982 C CA  . LYS D 4 232 ? 28.080 -38.870 -42.938 1.00 33.98  ? 231 LYS E CA  1 
ATOM   4983 C C   . LYS D 4 232 ? 27.951 -37.622 -43.816 1.00 34.36  ? 231 LYS E C   1 
ATOM   4984 O O   . LYS D 4 232 ? 28.882 -37.300 -44.567 1.00 29.12  ? 231 LYS E O   1 
ATOM   4985 C CB  . LYS D 4 232 ? 29.109 -38.663 -41.834 1.00 32.66  ? 231 LYS E CB  1 
ATOM   4986 C CG  . LYS D 4 232 ? 28.779 -37.596 -40.781 1.00 30.63  ? 231 LYS E CG  1 
ATOM   4987 C CD  . LYS D 4 232 ? 30.086 -37.258 -40.075 1.00 33.35  ? 231 LYS E CD  1 
ATOM   4988 C CE  . LYS D 4 232 ? 29.912 -36.911 -38.631 1.00 38.56  ? 231 LYS E CE  1 
ATOM   4989 N NZ  . LYS D 4 232 ? 31.210 -37.027 -37.879 1.00 38.82  ? 231 LYS E NZ  1 
ATOM   4990 N N   . PRO D 4 233 ? 26.803 -36.920 -43.780 1.00 31.15  ? 232 PRO E N   1 
ATOM   4991 C CA  . PRO D 4 233 ? 26.530 -35.773 -44.687 1.00 31.80  ? 232 PRO E CA  1 
ATOM   4992 C C   . PRO D 4 233 ? 27.172 -34.479 -44.198 1.00 27.15  ? 232 PRO E C   1 
ATOM   4993 O O   . PRO D 4 233 ? 26.522 -33.514 -43.789 1.00 26.16  ? 232 PRO E O   1 
ATOM   4994 C CB  . PRO D 4 233 ? 24.997 -35.712 -44.683 1.00 31.61  ? 232 PRO E CB  1 
ATOM   4995 C CG  . PRO D 4 233 ? 24.622 -36.158 -43.284 1.00 31.59  ? 232 PRO E CG  1 
ATOM   4996 C CD  . PRO D 4 233 ? 25.652 -37.232 -42.915 1.00 31.08  ? 232 PRO E CD  1 
ATOM   4997 N N   . VAL D 4 234 ? 28.498 -34.451 -44.243 1.00 26.16  ? 233 VAL E N   1 
ATOM   4998 C CA  . VAL D 4 234 ? 29.251 -33.300 -43.775 1.00 25.21  ? 233 VAL E CA  1 
ATOM   4999 C C   . VAL D 4 234 ? 29.142 -32.189 -44.807 1.00 25.01  ? 233 VAL E C   1 
ATOM   5000 O O   . VAL D 4 234 ? 28.734 -32.414 -45.954 1.00 21.11  ? 233 VAL E O   1 
ATOM   5001 C CB  . VAL D 4 234 ? 30.731 -33.652 -43.519 1.00 28.30  ? 233 VAL E CB  1 
ATOM   5002 C CG1 . VAL D 4 234 ? 30.860 -34.685 -42.408 1.00 30.95  ? 233 VAL E CG1 1 
ATOM   5003 C CG2 . VAL D 4 234 ? 31.397 -34.159 -44.827 1.00 25.87  ? 233 VAL E CG2 1 
ATOM   5004 N N   . THR D 4 235 ? 29.509 -30.989 -44.385 1.00 24.05  ? 234 THR E N   1 
ATOM   5005 C CA  . THR D 4 235 ? 29.769 -29.890 -45.295 1.00 21.37  ? 234 THR E CA  1 
ATOM   5006 C C   . THR D 4 235 ? 30.746 -30.323 -46.381 1.00 26.58  ? 234 THR E C   1 
ATOM   5007 O O   . THR D 4 235 ? 31.772 -30.955 -46.103 1.00 25.05  ? 234 THR E O   1 
ATOM   5008 C CB  . THR D 4 235 ? 30.320 -28.710 -44.492 1.00 23.75  ? 234 THR E CB  1 
ATOM   5009 O OG1 . THR D 4 235 ? 29.266 -28.185 -43.667 1.00 24.61  ? 234 THR E OG1 1 
ATOM   5010 C CG2 . THR D 4 235 ? 30.858 -27.608 -45.418 1.00 21.28  ? 234 THR E CG2 1 
ATOM   5011 N N   . GLN D 4 236 ? 30.410 -29.998 -47.624 1.00 24.32  ? 235 GLN E N   1 
ATOM   5012 C CA  . GLN D 4 236 ? 31.161 -30.505 -48.760 1.00 24.15  ? 235 GLN E CA  1 
ATOM   5013 C C   . GLN D 4 236 ? 30.734 -29.751 -50.012 1.00 25.19  ? 235 GLN E C   1 
ATOM   5014 O O   . GLN D 4 236 ? 29.717 -29.048 -50.041 1.00 23.79  ? 235 GLN E O   1 
ATOM   5015 C CB  . GLN D 4 236 ? 30.942 -32.009 -48.941 1.00 27.29  ? 235 GLN E CB  1 
ATOM   5016 C CG  . GLN D 4 236 ? 29.519 -32.366 -49.356 1.00 26.47  ? 235 GLN E CG  1 
ATOM   5017 C CD  . GLN D 4 236 ? 29.220 -33.858 -49.228 1.00 27.16  ? 235 GLN E CD  1 
ATOM   5018 O OE1 . GLN D 4 236 ? 29.375 -34.611 -50.177 1.00 24.90  ? 235 GLN E OE1 1 
ATOM   5019 N NE2 . GLN D 4 236 ? 28.783 -34.284 -48.044 1.00 25.86  ? 235 GLN E NE2 1 
ATOM   5020 N N   . ILE D 4 237 ? 31.535 -29.915 -51.051 1.00 24.93  ? 236 ILE E N   1 
ATOM   5021 C CA  . ILE D 4 237 ? 31.265 -29.360 -52.364 1.00 26.85  ? 236 ILE E CA  1 
ATOM   5022 C C   . ILE D 4 237 ? 30.956 -30.517 -53.298 1.00 26.22  ? 236 ILE E C   1 
ATOM   5023 O O   . ILE D 4 237 ? 31.649 -31.540 -53.283 1.00 24.49  ? 236 ILE E O   1 
ATOM   5024 C CB  . ILE D 4 237 ? 32.455 -28.527 -52.865 1.00 28.60  ? 236 ILE E CB  1 
ATOM   5025 C CG1 . ILE D 4 237 ? 32.361 -27.123 -52.281 1.00 28.12  ? 236 ILE E CG1 1 
ATOM   5026 C CG2 . ILE D 4 237 ? 32.507 -28.490 -54.398 1.00 29.30  ? 236 ILE E CG2 1 
ATOM   5027 C CD1 . ILE D 4 237 ? 33.664 -26.433 -52.249 1.00 27.72  ? 236 ILE E CD1 1 
ATOM   5028 N N   . VAL D 4 238 ? 29.897 -30.358 -54.085 1.00 27.22  ? 237 VAL E N   1 
ATOM   5029 C CA  . VAL D 4 238 ? 29.507 -31.299 -55.119 1.00 24.30  ? 237 VAL E CA  1 
ATOM   5030 C C   . VAL D 4 238 ? 29.446 -30.522 -56.418 1.00 26.60  ? 237 VAL E C   1 
ATOM   5031 O O   . VAL D 4 238 ? 28.862 -29.432 -56.467 1.00 23.64  ? 237 VAL E O   1 
ATOM   5032 C CB  . VAL D 4 238 ? 28.162 -31.972 -54.798 1.00 25.22  ? 237 VAL E CB  1 
ATOM   5033 C CG1 . VAL D 4 238 ? 27.820 -33.058 -55.859 1.00 22.20  ? 237 VAL E CG1 1 
ATOM   5034 C CG2 . VAL D 4 238 ? 28.212 -32.568 -53.388 1.00 19.72  ? 237 VAL E CG2 1 
ATOM   5035 N N   . SER D 4 239 ? 30.084 -31.061 -57.453 1.00 24.08  ? 238 SER E N   1 
ATOM   5036 C CA  . SER D 4 239 ? 30.218 -30.382 -58.728 1.00 24.72  ? 238 SER E CA  1 
ATOM   5037 C C   . SER D 4 239 ? 29.878 -31.317 -59.871 1.00 27.44  ? 238 SER E C   1 
ATOM   5038 O O   . SER D 4 239 ? 29.959 -32.541 -59.755 1.00 23.84  ? 238 SER E O   1 
ATOM   5039 C CB  . SER D 4 239 ? 31.634 -29.831 -58.957 1.00 23.65  ? 238 SER E CB  1 
ATOM   5040 O OG  . SER D 4 239 ? 31.907 -28.765 -58.069 1.00 25.72  ? 238 SER E OG  1 
ATOM   5041 N N   . ALA D 4 240 ? 29.497 -30.701 -60.988 1.00 27.52  ? 239 ALA E N   1 
ATOM   5042 C CA  . ALA D 4 240 ? 29.393 -31.375 -62.269 1.00 28.10  ? 239 ALA E CA  1 
ATOM   5043 C C   . ALA D 4 240 ? 29.960 -30.428 -63.305 1.00 28.16  ? 239 ALA E C   1 
ATOM   5044 O O   . ALA D 4 240 ? 29.895 -29.206 -63.140 1.00 28.15  ? 239 ALA E O   1 
ATOM   5045 C CB  . ALA D 4 240 ? 27.944 -31.761 -62.624 1.00 24.58  ? 239 ALA E CB  1 
ATOM   5046 N N   . GLU D 4 241 ? 30.516 -30.992 -64.370 1.00 26.68  ? 240 GLU E N   1 
ATOM   5047 C CA  . GLU D 4 241 ? 31.177 -30.174 -65.369 1.00 30.08  ? 240 GLU E CA  1 
ATOM   5048 C C   . GLU D 4 241 ? 30.796 -30.617 -66.769 1.00 33.33  ? 240 GLU E C   1 
ATOM   5049 O O   . GLU D 4 241 ? 30.202 -31.676 -66.984 1.00 27.50  ? 240 GLU E O   1 
ATOM   5050 C CB  . GLU D 4 241 ? 32.701 -30.220 -65.246 1.00 29.57  ? 240 GLU E CB  1 
ATOM   5051 C CG  . GLU D 4 241 ? 33.249 -31.512 -64.729 1.00 36.22  ? 240 GLU E CG  1 
ATOM   5052 C CD  . GLU D 4 241 ? 34.713 -31.378 -64.361 1.00 48.28  ? 240 GLU E CD  1 
ATOM   5053 O OE1 . GLU D 4 241 ? 35.549 -31.794 -65.198 1.00 47.40  ? 240 GLU E OE1 1 
ATOM   5054 O OE2 . GLU D 4 241 ? 35.024 -30.831 -63.263 1.00 48.81  ? 240 GLU E OE2 1 
ATOM   5055 N N   . ALA D 4 242 ? 31.184 -29.775 -67.723 1.00 28.72  ? 241 ALA E N   1 
ATOM   5056 C CA  . ALA D 4 242 ? 31.092 -30.071 -69.137 1.00 31.53  ? 241 ALA E CA  1 
ATOM   5057 C C   . ALA D 4 242 ? 32.211 -29.327 -69.848 1.00 29.55  ? 241 ALA E C   1 
ATOM   5058 O O   . ALA D 4 242 ? 32.693 -28.296 -69.373 1.00 28.93  ? 241 ALA E O   1 
ATOM   5059 C CB  . ALA D 4 242 ? 29.730 -29.666 -69.709 1.00 28.20  ? 241 ALA E CB  1 
ATOM   5060 N N   . TRP D 4 243 ? 32.629 -29.871 -70.977 1.00 27.61  ? 242 TRP E N   1 
ATOM   5061 C CA  . TRP D 4 243 ? 33.510 -29.189 -71.906 1.00 30.73  ? 242 TRP E CA  1 
ATOM   5062 C C   . TRP D 4 243 ? 32.725 -28.743 -73.130 1.00 23.67  ? 242 TRP E C   1 
ATOM   5063 O O   . TRP D 4 243 ? 31.750 -29.378 -73.523 1.00 26.15  ? 242 TRP E O   1 
ATOM   5064 C CB  . TRP D 4 243 ? 34.657 -30.103 -72.333 1.00 31.23  ? 242 TRP E CB  1 
ATOM   5065 C CG  . TRP D 4 243 ? 35.595 -30.405 -71.199 1.00 35.63  ? 242 TRP E CG  1 
ATOM   5066 C CD1 . TRP D 4 243 ? 35.417 -31.326 -70.209 1.00 29.63  ? 242 TRP E CD1 1 
ATOM   5067 C CD2 . TRP D 4 243 ? 36.853 -29.770 -70.937 1.00 26.77  ? 242 TRP E CD2 1 
ATOM   5068 N NE1 . TRP D 4 243 ? 36.496 -31.321 -69.364 1.00 35.75  ? 242 TRP E NE1 1 
ATOM   5069 C CE2 . TRP D 4 243 ? 37.389 -30.370 -69.785 1.00 30.76  ? 242 TRP E CE2 1 
ATOM   5070 C CE3 . TRP D 4 243 ? 37.577 -28.759 -71.572 1.00 25.93  ? 242 TRP E CE3 1 
ATOM   5071 C CZ2 . TRP D 4 243 ? 38.615 -29.989 -69.247 1.00 30.87  ? 242 TRP E CZ2 1 
ATOM   5072 C CZ3 . TRP D 4 243 ? 38.797 -28.373 -71.036 1.00 33.20  ? 242 TRP E CZ3 1 
ATOM   5073 C CH2 . TRP D 4 243 ? 39.306 -28.989 -69.886 1.00 31.16  ? 242 TRP E CH2 1 
ATOM   5074 N N   . GLY D 4 244 ? 33.157 -27.643 -73.734 1.00 27.56  ? 243 GLY E N   1 
ATOM   5075 C CA  . GLY D 4 244 ? 32.609 -27.258 -75.023 1.00 27.59  ? 243 GLY E CA  1 
ATOM   5076 C C   . GLY D 4 244 ? 32.861 -28.318 -76.080 1.00 28.87  ? 243 GLY E C   1 
ATOM   5077 O O   . GLY D 4 244 ? 33.690 -29.213 -75.919 1.00 30.26  ? 243 GLY E O   1 
ATOM   5078 N N   . ARG D 4 245 ? 32.112 -28.238 -77.176 1.00 31.64  ? 244 ARG E N   1 
ATOM   5079 C CA  . ARG D 4 245 ? 32.258 -29.233 -78.231 1.00 39.66  ? 244 ARG E CA  1 
ATOM   5080 C C   . ARG D 4 245 ? 32.129 -28.579 -79.591 1.00 35.35  ? 244 ARG E C   1 
ATOM   5081 O O   . ARG D 4 245 ? 31.183 -27.821 -79.827 1.00 36.01  ? 244 ARG E O   1 
ATOM   5082 C CB  . ARG D 4 245 ? 31.225 -30.351 -78.098 1.00 42.74  ? 244 ARG E CB  1 
ATOM   5083 C CG  . ARG D 4 245 ? 31.459 -31.472 -79.088 1.00 51.76  ? 244 ARG E CG  1 
ATOM   5084 C CD  . ARG D 4 245 ? 30.628 -32.707 -78.766 1.00 61.02  ? 244 ARG E CD  1 
ATOM   5085 N NE  . ARG D 4 245 ? 29.255 -32.370 -78.405 1.00 60.04  ? 244 ARG E NE  1 
ATOM   5086 C CZ  . ARG D 4 245 ? 28.769 -32.448 -77.169 1.00 54.17  ? 244 ARG E CZ  1 
ATOM   5087 N NH1 . ARG D 4 245 ? 29.548 -32.829 -76.161 1.00 50.48  ? 244 ARG E NH1 1 
ATOM   5088 N NH2 . ARG D 4 245 ? 27.506 -32.120 -76.934 1.00 54.11  ? 244 ARG E NH2 1 
ATOM   5089 N N   . ALA D 4 246 ? 33.085 -28.872 -80.472 1.00 37.61  ? 245 ALA E N   1 
ATOM   5090 C CA  . ALA D 4 246 ? 33.030 -28.376 -81.844 1.00 48.78  ? 245 ALA E CA  1 
ATOM   5091 C C   . ALA D 4 246 ? 31.734 -28.811 -82.525 1.00 47.17  ? 245 ALA E C   1 
ATOM   5092 O O   . ALA D 4 246 ? 31.193 -29.889 -82.256 1.00 48.37  ? 245 ALA E O   1 
ATOM   5093 C CB  . ALA D 4 246 ? 34.238 -28.877 -82.645 1.00 41.59  ? 245 ALA E CB  1 
ATOM   5094 N N   . ASP D 4 247 ? 31.228 -27.947 -83.403 1.00 49.14  ? 246 ASP E N   1 
ATOM   5095 C CA  . ASP D 4 247 ? 29.985 -28.223 -84.113 1.00 60.99  ? 246 ASP E CA  1 
ATOM   5096 C C   . ASP D 4 247 ? 30.120 -29.543 -84.860 1.00 63.92  ? 246 ASP E C   1 
ATOM   5097 O O   . ASP D 4 247 ? 31.151 -29.840 -85.471 1.00 59.60  ? 246 ASP E O   1 
ATOM   5098 C CB  . ASP D 4 247 ? 29.627 -27.083 -85.081 1.00 66.07  ? 246 ASP E CB  1 
ATOM   5099 C CG  . ASP D 4 247 ? 28.123 -26.779 -85.113 1.00 65.02  ? 246 ASP E CG  1 
ATOM   5100 O OD1 . ASP D 4 247 ? 27.372 -27.340 -84.283 1.00 67.10  ? 246 ASP E OD1 1 
ATOM   5101 O OD2 . ASP D 4 247 ? 27.694 -25.969 -85.966 1.00 63.96  ? 246 ASP E OD2 1 
ATOM   5102 O OXT . ASP D 4 247 ? 29.197 -30.348 -84.830 1.00 65.58  ? 246 ASP E OXT 1 
ATOM   5103 N N   . ALA E 5 2   ? -1.555 0.311   -30.694 1.00 50.92  ? 1   ALA D N   1 
ATOM   5104 C CA  . ALA E 5 2   ? -0.695 -0.841  -30.945 1.00 48.66  ? 1   ALA D CA  1 
ATOM   5105 C C   . ALA E 5 2   ? 0.629  -0.391  -31.549 1.00 39.58  ? 1   ALA D C   1 
ATOM   5106 O O   . ALA E 5 2   ? 0.835  0.799   -31.807 1.00 43.17  ? 1   ALA D O   1 
ATOM   5107 C CB  . ALA E 5 2   ? -1.390 -1.842  -31.858 1.00 53.84  ? 1   ALA D CB  1 
ATOM   5108 N N   . GLN E 5 3   ? 1.540  -1.343  -31.724 1.00 39.26  ? 2   GLN D N   1 
ATOM   5109 C CA  . GLN E 5 3   ? 2.864  -1.108  -32.298 1.00 35.94  ? 2   GLN D CA  1 
ATOM   5110 C C   . GLN E 5 3   ? 2.981  -2.028  -33.513 1.00 32.80  ? 2   GLN D C   1 
ATOM   5111 O O   . GLN E 5 3   ? 3.294  -3.213  -33.376 1.00 35.51  ? 2   GLN D O   1 
ATOM   5112 C CB  . GLN E 5 3   ? 3.962  -1.374  -31.271 1.00 33.93  ? 2   GLN D CB  1 
ATOM   5113 C CG  . GLN E 5 3   ? 5.370  -1.100  -31.766 1.00 32.33  ? 2   GLN D CG  1 
ATOM   5114 C CD  . GLN E 5 3   ? 5.662  0.381   -31.919 1.00 33.90  ? 2   GLN D CD  1 
ATOM   5115 O OE1 . GLN E 5 3   ? 5.011  1.223   -31.286 1.00 34.50  ? 2   GLN D OE1 1 
ATOM   5116 N NE2 . GLN E 5 3   ? 6.661  0.709   -32.746 1.00 27.23  ? 2   GLN D NE2 1 
ATOM   5117 N N   . LYS E 5 4   ? 2.719  -1.493  -34.699 1.00 33.02  ? 3   LYS D N   1 
ATOM   5118 C CA  . LYS E 5 4   ? 2.589  -2.338  -35.874 1.00 35.38  ? 3   LYS D CA  1 
ATOM   5119 C C   . LYS E 5 4   ? 2.999  -1.552  -37.111 1.00 30.27  ? 3   LYS D C   1 
ATOM   5120 O O   . LYS E 5 4   ? 2.692  -0.363  -37.229 1.00 30.58  ? 3   LYS D O   1 
ATOM   5121 C CB  . LYS E 5 4   ? 1.148  -2.860  -35.978 1.00 36.73  ? 3   LYS D CB  1 
ATOM   5122 C CG  . LYS E 5 4   ? 0.776  -3.447  -37.318 1.00 44.15  ? 3   LYS D CG  1 
ATOM   5123 C CD  . LYS E 5 4   ? -0.004 -4.746  -37.155 1.00 53.38  ? 3   LYS D CD  1 
ATOM   5124 C CE  . LYS E 5 4   ? 0.006  -5.601  -38.434 1.00 52.12  ? 3   LYS D CE  1 
ATOM   5125 N NZ  . LYS E 5 4   ? 1.341  -5.697  -39.099 1.00 52.23  ? 3   LYS D NZ  1 
ATOM   5126 N N   . VAL E 5 5   ? 3.748  -2.207  -37.996 1.00 37.27  ? 4   VAL D N   1 
ATOM   5127 C CA  . VAL E 5 5   ? 4.154  -1.668  -39.295 1.00 28.90  ? 4   VAL D CA  1 
ATOM   5128 C C   . VAL E 5 5   ? 3.554  -2.561  -40.371 1.00 34.08  ? 4   VAL D C   1 
ATOM   5129 O O   . VAL E 5 5   ? 3.805  -3.774  -40.382 1.00 32.86  ? 4   VAL D O   1 
ATOM   5130 C CB  . VAL E 5 5   ? 5.680  -1.618  -39.444 1.00 31.58  ? 4   VAL D CB  1 
ATOM   5131 C CG1 . VAL E 5 5   ? 6.071  -0.938  -40.746 1.00 23.66  ? 4   VAL D CG1 1 
ATOM   5132 C CG2 . VAL E 5 5   ? 6.319  -0.941  -38.245 1.00 28.65  ? 4   VAL D CG2 1 
ATOM   5133 N N   . THR E 5 6   ? 2.779  -1.969  -41.281 1.00 32.74  ? 5   THR D N   1 
ATOM   5134 C CA  . THR E 5 6   ? 2.031  -2.725  -42.282 1.00 32.76  ? 5   THR D CA  1 
ATOM   5135 C C   . THR E 5 6   ? 2.476  -2.320  -43.673 1.00 29.42  ? 5   THR D C   1 
ATOM   5136 O O   . THR E 5 6   ? 2.369  -1.147  -44.050 1.00 27.90  ? 5   THR D O   1 
ATOM   5137 C CB  . THR E 5 6   ? 0.529  -2.494  -42.154 1.00 34.21  ? 5   THR D CB  1 
ATOM   5138 O OG1 . THR E 5 6   ? 0.234  -1.148  -42.543 1.00 43.25  ? 5   THR D OG1 1 
ATOM   5139 C CG2 . THR E 5 6   ? 0.070  -2.722  -40.746 1.00 23.54  ? 5   THR D CG2 1 
ATOM   5140 N N   . GLN E 5 7   ? 2.955  -3.288  -44.436 1.00 34.17  ? 6   GLN D N   1 
ATOM   5141 C CA  . GLN E 5 7   ? 3.187  -3.127  -45.865 1.00 31.45  ? 6   GLN D CA  1 
ATOM   5142 C C   . GLN E 5 7   ? 2.102  -3.951  -46.563 1.00 35.65  ? 6   GLN D C   1 
ATOM   5143 O O   . GLN E 5 7   ? 2.149  -5.187  -46.565 1.00 36.02  ? 6   GLN D O   1 
ATOM   5144 C CB  . GLN E 5 7   ? 4.609  -3.553  -46.229 1.00 27.50  ? 6   GLN D CB  1 
ATOM   5145 C CG  . GLN E 5 7   ? 5.670  -2.616  -45.599 1.00 30.85  ? 6   GLN D CG  1 
ATOM   5146 C CD  . GLN E 5 7   ? 7.106  -3.117  -45.719 1.00 29.25  ? 6   GLN D CD  1 
ATOM   5147 O OE1 . GLN E 5 7   ? 7.674  -3.651  -44.761 1.00 28.60  ? 6   GLN D OE1 1 
ATOM   5148 N NE2 . GLN E 5 7   ? 7.703  -2.927  -46.889 1.00 26.39  ? 6   GLN D NE2 1 
ATOM   5149 N N   . ALA E 5 8   ? 1.105  -3.261  -47.121 1.00 38.36  ? 7   ALA D N   1 
ATOM   5150 C CA  . ALA E 5 8   ? -0.118 -3.937  -47.555 1.00 39.29  ? 7   ALA D CA  1 
ATOM   5151 C C   . ALA E 5 8   ? 0.083  -4.719  -48.852 1.00 32.44  ? 7   ALA D C   1 
ATOM   5152 O O   . ALA E 5 8   ? -0.529 -5.772  -49.036 1.00 34.16  ? 7   ALA D O   1 
ATOM   5153 C CB  . ALA E 5 8   ? -1.254 -2.921  -47.703 1.00 30.51  ? 7   ALA D CB  1 
ATOM   5154 N N   . GLN E 5 9   ? 0.914  -4.221  -49.766 1.00 34.68  ? 8   GLN D N   1 
ATOM   5155 C CA  . GLN E 5 9   ? 1.225  -4.945  -50.997 1.00 36.35  ? 8   GLN D CA  1 
ATOM   5156 C C   . GLN E 5 9   ? 2.270  -6.012  -50.695 1.00 40.06  ? 8   GLN D C   1 
ATOM   5157 O O   . GLN E 5 9   ? 3.362  -5.693  -50.211 1.00 43.43  ? 8   GLN D O   1 
ATOM   5158 C CB  . GLN E 5 9   ? 1.768  -3.999  -52.070 1.00 35.09  ? 8   GLN D CB  1 
ATOM   5159 C CG  . GLN E 5 9   ? 1.232  -2.563  -52.053 1.00 39.03  ? 8   GLN D CG  1 
ATOM   5160 C CD  . GLN E 5 9   ? 2.281  -1.528  -52.536 1.00 45.83  ? 8   GLN D CD  1 
ATOM   5161 O OE1 . GLN E 5 9   ? 3.265  -1.234  -51.833 1.00 40.69  ? 8   GLN D OE1 1 
ATOM   5162 N NE2 . GLN E 5 9   ? 2.070  -0.983  -53.733 1.00 33.56  ? 8   GLN D NE2 1 
ATOM   5163 N N   . SER E 5 10  ? 1.965  -7.276  -50.987 1.00 38.06  ? 9   SER D N   1 
ATOM   5164 C CA  . SER E 5 10  ? 2.983  -8.297  -50.761 1.00 37.39  ? 9   SER D CA  1 
ATOM   5165 C C   . SER E 5 10  ? 3.966  -8.376  -51.920 1.00 35.86  ? 9   SER D C   1 
ATOM   5166 O O   . SER E 5 10  ? 5.149  -8.677  -51.713 1.00 34.96  ? 9   SER D O   1 
ATOM   5167 C CB  . SER E 5 10  ? 2.327  -9.653  -50.511 1.00 36.07  ? 9   SER D CB  1 
ATOM   5168 O OG  . SER E 5 10  ? 1.155  -9.766  -51.283 1.00 45.72  ? 9   SER D OG  1 
ATOM   5169 N N   . SER E 5 11  ? 3.515  -8.091  -53.136 1.00 39.02  ? 10  SER D N   1 
ATOM   5170 C CA  . SER E 5 11  ? 4.403  -8.086  -54.288 1.00 39.14  ? 10  SER D CA  1 
ATOM   5171 C C   . SER E 5 11  ? 3.974  -6.988  -55.242 1.00 38.79  ? 10  SER D C   1 
ATOM   5172 O O   . SER E 5 11  ? 2.783  -6.694  -55.381 1.00 41.91  ? 10  SER D O   1 
ATOM   5173 C CB  . SER E 5 11  ? 4.408  -9.433  -55.025 1.00 38.32  ? 10  SER D CB  1 
ATOM   5174 O OG  . SER E 5 11  ? 3.122  -10.019 -54.986 1.00 48.97  ? 10  SER D OG  1 
ATOM   5175 N N   . VAL E 5 12  ? 4.960  -6.373  -55.873 1.00 32.98  ? 11  VAL D N   1 
ATOM   5176 C CA  . VAL E 5 12  ? 4.747  -5.357  -56.889 1.00 40.78  ? 11  VAL D CA  1 
ATOM   5177 C C   . VAL E 5 12  ? 5.686  -5.673  -58.038 1.00 36.01  ? 11  VAL D C   1 
ATOM   5178 O O   . VAL E 5 12  ? 6.822  -6.116  -57.826 1.00 30.43  ? 11  VAL D O   1 
ATOM   5179 C CB  . VAL E 5 12  ? 4.991  -3.925  -56.352 1.00 37.11  ? 11  VAL D CB  1 
ATOM   5180 C CG1 . VAL E 5 12  ? 4.403  -2.891  -57.304 1.00 38.59  ? 11  VAL D CG1 1 
ATOM   5181 C CG2 . VAL E 5 12  ? 4.374  -3.769  -54.991 1.00 34.33  ? 11  VAL D CG2 1 
ATOM   5182 N N   . SER E 5 13  ? 5.215  -5.450  -59.256 1.00 35.57  ? 12  SER D N   1 
ATOM   5183 C CA  . SER E 5 13  ? 6.070  -5.625  -60.417 1.00 37.69  ? 12  SER D CA  1 
ATOM   5184 C C   . SER E 5 13  ? 5.967  -4.378  -61.282 1.00 35.28  ? 12  SER D C   1 
ATOM   5185 O O   . SER E 5 13  ? 4.873  -3.841  -61.475 1.00 36.14  ? 12  SER D O   1 
ATOM   5186 C CB  . SER E 5 13  ? 5.684  -6.885  -61.201 1.00 38.58  ? 12  SER D CB  1 
ATOM   5187 O OG  . SER E 5 13  ? 6.680  -7.187  -62.162 1.00 50.49  ? 12  SER D OG  1 
ATOM   5188 N N   . MET E 5 14  ? 7.109  -3.928  -61.797 1.00 33.79  ? 13  MET D N   1 
ATOM   5189 C CA  . MET E 5 14  ? 7.243  -2.658  -62.492 1.00 32.94  ? 13  MET D CA  1 
ATOM   5190 C C   . MET E 5 14  ? 8.339  -2.807  -63.541 1.00 37.54  ? 13  MET D C   1 
ATOM   5191 O O   . MET E 5 14  ? 9.305  -3.549  -63.314 1.00 31.40  ? 13  MET D O   1 
ATOM   5192 C CB  . MET E 5 14  ? 7.572  -1.529  -61.495 1.00 30.31  ? 13  MET D CB  1 
ATOM   5193 C CG  . MET E 5 14  ? 7.108  -0.117  -61.852 1.00 41.35  ? 13  MET D CG  1 
ATOM   5194 S SD  . MET E 5 14  ? 5.346  0.203   -62.181 1.00 52.43  ? 13  MET D SD  1 
ATOM   5195 C CE  . MET E 5 14  ? 4.504  -0.811  -60.999 1.00 28.51  ? 13  MET D CE  1 
ATOM   5196 N N   . PRO E 5 15  ? 8.212  -2.142  -64.698 1.00 34.28  ? 14  PRO D N   1 
ATOM   5197 C CA  . PRO E 5 15  ? 9.200  -2.316  -65.769 1.00 34.34  ? 14  PRO D CA  1 
ATOM   5198 C C   . PRO E 5 15  ? 10.464 -1.540  -65.481 1.00 34.35  ? 14  PRO D C   1 
ATOM   5199 O O   . PRO E 5 15  ? 10.445 -0.512  -64.803 1.00 35.71  ? 14  PRO D O   1 
ATOM   5200 C CB  . PRO E 5 15  ? 8.499  -1.740  -67.011 1.00 34.90  ? 14  PRO D CB  1 
ATOM   5201 C CG  . PRO E 5 15  ? 7.094  -1.427  -66.597 1.00 40.03  ? 14  PRO D CG  1 
ATOM   5202 C CD  . PRO E 5 15  ? 7.125  -1.244  -65.111 1.00 36.93  ? 14  PRO D CD  1 
ATOM   5203 N N   . VAL E 5 16  ? 11.571 -2.029  -66.043 1.00 33.98  ? 15  VAL D N   1 
ATOM   5204 C CA  . VAL E 5 16  ? 12.857 -1.344  -65.919 1.00 34.25  ? 15  VAL D CA  1 
ATOM   5205 C C   . VAL E 5 16  ? 12.680 0.101   -66.378 1.00 35.84  ? 15  VAL D C   1 
ATOM   5206 O O   . VAL E 5 16  ? 11.766 0.404   -67.149 1.00 38.20  ? 15  VAL D O   1 
ATOM   5207 C CB  . VAL E 5 16  ? 13.960 -2.083  -66.710 1.00 35.44  ? 15  VAL D CB  1 
ATOM   5208 C CG1 . VAL E 5 16  ? 13.549 -2.291  -68.172 1.00 40.17  ? 15  VAL D CG1 1 
ATOM   5209 C CG2 . VAL E 5 16  ? 15.322 -1.383  -66.611 1.00 35.59  ? 15  VAL D CG2 1 
ATOM   5210 N N   . ARG E 5 17  ? 13.505 1.010   -65.854 1.00 37.31  ? 16  ARG D N   1 
ATOM   5211 C CA  . ARG E 5 17  ? 13.562 2.434   -66.182 1.00 33.73  ? 16  ARG D CA  1 
ATOM   5212 C C   . ARG E 5 17  ? 12.373 3.234   -65.651 1.00 37.48  ? 16  ARG D C   1 
ATOM   5213 O O   . ARG E 5 17  ? 12.378 4.467   -65.762 1.00 33.86  ? 16  ARG D O   1 
ATOM   5214 C CB  . ARG E 5 17  ? 13.696 2.680   -67.693 1.00 39.07  ? 16  ARG D CB  1 
ATOM   5215 C CG  . ARG E 5 17  ? 15.118 2.574   -68.211 1.00 38.30  ? 16  ARG D CG  1 
ATOM   5216 C CD  . ARG E 5 17  ? 15.154 2.425   -69.733 1.00 53.17  ? 16  ARG D CD  1 
ATOM   5217 N NE  . ARG E 5 17  ? 15.516 1.063   -70.144 1.00 58.74  ? 16  ARG D NE  1 
ATOM   5218 C CZ  . ARG E 5 17  ? 14.761 0.267   -70.907 1.00 56.99  ? 16  ARG D CZ  1 
ATOM   5219 N NH1 . ARG E 5 17  ? 13.582 0.690   -71.356 1.00 54.17  ? 16  ARG D NH1 1 
ATOM   5220 N NH2 . ARG E 5 17  ? 15.184 -0.962  -71.215 1.00 48.53  ? 16  ARG D NH2 1 
ATOM   5221 N N   . LYS E 5 18  ? 11.369 2.597   -65.059 1.00 36.91  ? 17  LYS D N   1 
ATOM   5222 C CA  . LYS E 5 18  ? 10.244 3.332   -64.510 1.00 33.91  ? 17  LYS D CA  1 
ATOM   5223 C C   . LYS E 5 18  ? 10.470 3.612   -63.022 1.00 41.12  ? 17  LYS D C   1 
ATOM   5224 O O   . LYS E 5 18  ? 11.569 3.421   -62.488 1.00 38.91  ? 17  LYS D O   1 
ATOM   5225 C CB  . LYS E 5 18  ? 8.940  2.570   -64.766 1.00 36.88  ? 17  LYS D CB  1 
ATOM   5226 C CG  . LYS E 5 18  ? 8.671  2.252   -66.239 1.00 38.97  ? 17  LYS D CG  1 
ATOM   5227 C CD  . LYS E 5 18  ? 9.070  3.418   -67.145 1.00 35.76  ? 17  LYS D CD  1 
ATOM   5228 C CE  . LYS E 5 18  ? 8.202  4.642   -66.887 1.00 41.18  ? 17  LYS D CE  1 
ATOM   5229 N NZ  . LYS E 5 18  ? 6.828  4.253   -66.491 1.00 41.96  ? 17  LYS D NZ  1 
ATOM   5230 N N   . ALA E 5 19  ? 9.425  4.088   -62.346 1.00 38.24  ? 18  ALA D N   1 
ATOM   5231 C CA  . ALA E 5 19  ? 9.473  4.401   -60.926 1.00 37.96  ? 18  ALA D CA  1 
ATOM   5232 C C   . ALA E 5 19  ? 8.454  3.548   -60.185 1.00 35.52  ? 18  ALA D C   1 
ATOM   5233 O O   . ALA E 5 19  ? 7.406  3.193   -60.729 1.00 37.31  ? 18  ALA D O   1 
ATOM   5234 C CB  . ALA E 5 19  ? 9.200  5.890   -60.672 1.00 32.66  ? 18  ALA D CB  1 
ATOM   5235 N N   . VAL E 5 20  ? 8.777  3.193   -58.948 1.00 33.17  ? 19  VAL D N   1 
ATOM   5236 C CA  . VAL E 5 20  ? 7.868  2.416   -58.116 1.00 34.66  ? 19  VAL D CA  1 
ATOM   5237 C C   . VAL E 5 20  ? 7.742  3.105   -56.763 1.00 35.79  ? 19  VAL D C   1 
ATOM   5238 O O   . VAL E 5 20  ? 8.674  3.762   -56.287 1.00 34.55  ? 19  VAL D O   1 
ATOM   5239 C CB  . VAL E 5 20  ? 8.323  0.943   -57.950 1.00 34.30  ? 19  VAL D CB  1 
ATOM   5240 C CG1 . VAL E 5 20  ? 9.405  0.801   -56.862 1.00 27.95  ? 19  VAL D CG1 1 
ATOM   5241 C CG2 . VAL E 5 20  ? 7.125  0.060   -57.634 1.00 29.57  ? 19  VAL D CG2 1 
ATOM   5242 N N   . THR E 5 21  ? 6.566  2.973   -56.157 1.00 30.65  ? 20  THR D N   1 
ATOM   5243 C CA  . THR E 5 21  ? 6.315  3.474   -54.814 1.00 33.94  ? 20  THR D CA  1 
ATOM   5244 C C   . THR E 5 21  ? 5.846  2.313   -53.947 1.00 34.87  ? 20  THR D C   1 
ATOM   5245 O O   . THR E 5 21  ? 4.853  1.652   -54.271 1.00 31.75  ? 20  THR D O   1 
ATOM   5246 C CB  . THR E 5 21  ? 5.279  4.609   -54.824 1.00 34.05  ? 20  THR D CB  1 
ATOM   5247 O OG1 . THR E 5 21  ? 5.825  5.749   -55.497 1.00 37.39  ? 20  THR D OG1 1 
ATOM   5248 C CG2 . THR E 5 21  ? 4.924  5.013   -53.403 1.00 32.90  ? 20  THR D CG2 1 
ATOM   5249 N N   . LEU E 5 22  ? 6.570  2.049   -52.861 1.00 31.83  ? 21  LEU D N   1 
ATOM   5250 C CA  . LEU E 5 22  ? 6.237  0.962   -51.952 1.00 30.54  ? 21  LEU D CA  1 
ATOM   5251 C C   . LEU E 5 22  ? 5.666  1.579   -50.681 1.00 33.89  ? 21  LEU D C   1 
ATOM   5252 O O   . LEU E 5 22  ? 6.334  2.386   -50.025 1.00 29.63  ? 21  LEU D O   1 
ATOM   5253 C CB  . LEU E 5 22  ? 7.459  0.095   -51.660 1.00 28.36  ? 21  LEU D CB  1 
ATOM   5254 C CG  . LEU E 5 22  ? 8.235  -0.358  -52.905 1.00 33.01  ? 21  LEU D CG  1 
ATOM   5255 C CD1 . LEU E 5 22  ? 9.579  -0.955  -52.501 1.00 25.45  ? 21  LEU D CD1 1 
ATOM   5256 C CD2 . LEU E 5 22  ? 7.414  -1.374  -53.726 1.00 30.07  ? 21  LEU D CD2 1 
ATOM   5257 N N   . ASN E 5 23  ? 4.427  1.221   -50.358 1.00 30.99  ? 22  ASN D N   1 
ATOM   5258 C CA  . ASN E 5 23  ? 3.719  1.886   -49.277 1.00 32.08  ? 22  ASN D CA  1 
ATOM   5259 C C   . ASN E 5 23  ? 4.080  1.292   -47.926 1.00 30.97  ? 22  ASN D C   1 
ATOM   5260 O O   . ASN E 5 23  ? 4.491  0.133   -47.806 1.00 29.94  ? 22  ASN D O   1 
ATOM   5261 C CB  . ASN E 5 23  ? 2.207  1.797   -49.461 1.00 31.92  ? 22  ASN D CB  1 
ATOM   5262 C CG  . ASN E 5 23  ? 1.735  2.520   -50.696 1.00 36.87  ? 22  ASN D CG  1 
ATOM   5263 O OD1 . ASN E 5 23  ? 2.272  3.565   -51.064 1.00 41.95  ? 22  ASN D OD1 1 
ATOM   5264 N ND2 . ASN E 5 23  ? 0.742  1.959   -51.354 1.00 36.12  ? 22  ASN D ND2 1 
ATOM   5265 N N   . CYS E 5 24  ? 3.888  2.111   -46.898 1.00 29.89  ? 23  CYS D N   1 
ATOM   5266 C CA  . CYS E 5 24  ? 4.147  1.706   -45.527 1.00 30.84  ? 23  CYS D CA  1 
ATOM   5267 C C   . CYS E 5 24  ? 3.249  2.529   -44.623 1.00 26.77  ? 23  CYS D C   1 
ATOM   5268 O O   . CYS E 5 24  ? 3.328  3.759   -44.626 1.00 27.29  ? 23  CYS D O   1 
ATOM   5269 C CB  . CYS E 5 24  ? 5.619  1.903   -45.151 1.00 24.87  ? 23  CYS D CB  1 
ATOM   5270 S SG  . CYS E 5 24  ? 5.965  1.324   -43.455 1.00 31.27  ? 23  CYS D SG  1 
ATOM   5271 N N   . LEU E 5 25  ? 2.394  1.852   -43.875 1.00 26.93  ? 24  LEU D N   1 
ATOM   5272 C CA  . LEU E 5 25  ? 1.574  2.472   -42.850 1.00 35.60  ? 24  LEU D CA  1 
ATOM   5273 C C   . LEU E 5 25  ? 1.989  1.894   -41.503 1.00 35.46  ? 24  LEU D C   1 
ATOM   5274 O O   . LEU E 5 25  ? 2.386  0.727   -41.417 1.00 31.84  ? 24  LEU D O   1 
ATOM   5275 C CB  . LEU E 5 25  ? 0.075  2.225   -43.107 1.00 33.34  ? 24  LEU D CB  1 
ATOM   5276 C CG  . LEU E 5 25  ? -0.430 2.676   -44.483 1.00 39.48  ? 24  LEU D CG  1 
ATOM   5277 C CD1 . LEU E 5 25  ? -1.908 2.302   -44.714 1.00 33.59  ? 24  LEU D CD1 1 
ATOM   5278 C CD2 . LEU E 5 25  ? -0.244 4.166   -44.589 1.00 38.37  ? 24  LEU D CD2 1 
ATOM   5279 N N   . TYR E 5 26  ? 1.910  2.709   -40.448 1.00 31.78  ? 25  TYR D N   1 
ATOM   5280 C CA  . TYR E 5 26  ? 2.320  2.243   -39.131 1.00 30.16  ? 25  TYR D CA  1 
ATOM   5281 C C   . TYR E 5 26  ? 1.374  2.787   -38.079 1.00 32.50  ? 25  TYR D C   1 
ATOM   5282 O O   . TYR E 5 26  ? 0.790  3.862   -38.238 1.00 32.53  ? 25  TYR D O   1 
ATOM   5283 C CB  . TYR E 5 26  ? 3.773  2.643   -38.797 1.00 31.45  ? 25  TYR D CB  1 
ATOM   5284 C CG  . TYR E 5 26  ? 4.046  4.126   -38.872 1.00 30.61  ? 25  TYR D CG  1 
ATOM   5285 C CD1 . TYR E 5 26  ? 4.415  4.720   -40.063 1.00 25.93  ? 25  TYR D CD1 1 
ATOM   5286 C CD2 . TYR E 5 26  ? 3.937  4.927   -37.747 1.00 31.92  ? 25  TYR D CD2 1 
ATOM   5287 C CE1 . TYR E 5 26  ? 4.660  6.070   -40.135 1.00 32.39  ? 25  TYR D CE1 1 
ATOM   5288 C CE2 . TYR E 5 26  ? 4.177  6.275   -37.809 1.00 25.57  ? 25  TYR D CE2 1 
ATOM   5289 C CZ  . TYR E 5 26  ? 4.532  6.848   -38.995 1.00 29.47  ? 25  TYR D CZ  1 
ATOM   5290 O OH  . TYR E 5 26  ? 4.778  8.203   -39.050 1.00 30.25  ? 25  TYR D OH  1 
ATOM   5291 N N   . GLU E 5 27  ? 1.214  2.016   -37.008 1.00 32.83  ? 26  GLU D N   1 
ATOM   5292 C CA  . GLU E 5 27  ? 0.527  2.459   -35.807 1.00 34.63  ? 26  GLU D CA  1 
ATOM   5293 C C   . GLU E 5 27  ? 1.512  2.450   -34.653 1.00 35.09  ? 26  GLU D C   1 
ATOM   5294 O O   . GLU E 5 27  ? 2.228  1.460   -34.447 1.00 31.45  ? 26  GLU D O   1 
ATOM   5295 C CB  . GLU E 5 27  ? -0.663 1.564   -35.465 1.00 39.16  ? 26  GLU D CB  1 
ATOM   5296 C CG  . GLU E 5 27  ? -1.489 1.115   -36.655 1.00 44.44  ? 26  GLU D CG  1 
ATOM   5297 C CD  . GLU E 5 27  ? -2.243 -0.174  -36.371 1.00 55.10  ? 26  GLU D CD  1 
ATOM   5298 O OE1 . GLU E 5 27  ? -2.309 -1.043  -37.276 1.00 58.88  ? 26  GLU D OE1 1 
ATOM   5299 O OE2 . GLU E 5 27  ? -2.750 -0.322  -35.234 1.00 58.29  ? 26  GLU D OE2 1 
ATOM   5300 N N   . THR E 5 28  ? 1.530  3.535   -33.888 1.00 30.59  ? 27  THR D N   1 
ATOM   5301 C CA  . THR E 5 28  ? 2.452  3.592   -32.771 1.00 34.55  ? 27  THR D CA  1 
ATOM   5302 C C   . THR E 5 28  ? 2.000  4.660   -31.779 1.00 36.71  ? 27  THR D C   1 
ATOM   5303 O O   . THR E 5 28  ? 1.387  5.663   -32.157 1.00 33.46  ? 27  THR D O   1 
ATOM   5304 C CB  . THR E 5 28  ? 3.873  3.861   -33.282 1.00 30.82  ? 27  THR D CB  1 
ATOM   5305 O OG1 . THR E 5 28  ? 4.801  3.774   -32.198 1.00 31.78  ? 27  THR D OG1 1 
ATOM   5306 C CG2 . THR E 5 28  ? 3.967  5.231   -33.949 1.00 28.00  ? 27  THR D CG2 1 
ATOM   5307 N N   . SER E 5 29  ? 2.301  4.428   -30.502 1.00 33.43  ? 28  SER D N   1 
ATOM   5308 C CA  . SER E 5 29  ? 2.203  5.492   -29.516 1.00 35.75  ? 28  SER D CA  1 
ATOM   5309 C C   . SER E 5 29  ? 3.488  6.306   -29.401 1.00 34.90  ? 28  SER D C   1 
ATOM   5310 O O   . SER E 5 29  ? 3.509  7.285   -28.652 1.00 30.63  ? 28  SER D O   1 
ATOM   5311 C CB  . SER E 5 29  ? 1.826  4.921   -28.149 1.00 34.64  ? 28  SER D CB  1 
ATOM   5312 O OG  . SER E 5 29  ? 2.827  4.029   -27.683 1.00 47.62  ? 28  SER D OG  1 
ATOM   5313 N N   . TRP E 5 30  ? 4.555  5.931   -30.120 1.00 36.29  ? 29  TRP D N   1 
ATOM   5314 C CA  . TRP E 5 30  ? 5.792  6.707   -30.089 1.00 32.75  ? 29  TRP D CA  1 
ATOM   5315 C C   . TRP E 5 30  ? 5.582  8.016   -30.840 1.00 34.37  ? 29  TRP D C   1 
ATOM   5316 O O   . TRP E 5 30  ? 5.078  8.011   -31.967 1.00 39.50  ? 29  TRP D O   1 
ATOM   5317 C CB  . TRP E 5 30  ? 6.960  5.938   -30.729 1.00 29.63  ? 29  TRP D CB  1 
ATOM   5318 C CG  . TRP E 5 30  ? 7.263  4.563   -30.198 1.00 26.67  ? 29  TRP D CG  1 
ATOM   5319 C CD1 . TRP E 5 30  ? 6.749  3.975   -29.073 1.00 30.05  ? 29  TRP D CD1 1 
ATOM   5320 C CD2 . TRP E 5 30  ? 8.145  3.591   -30.789 1.00 26.28  ? 29  TRP D CD2 1 
ATOM   5321 N NE1 . TRP E 5 30  ? 7.264  2.703   -28.920 1.00 24.83  ? 29  TRP D NE1 1 
ATOM   5322 C CE2 . TRP E 5 30  ? 8.114  2.439   -29.964 1.00 29.28  ? 29  TRP D CE2 1 
ATOM   5323 C CE3 . TRP E 5 30  ? 8.936  3.574   -31.944 1.00 25.47  ? 29  TRP D CE3 1 
ATOM   5324 C CZ2 . TRP E 5 30  ? 8.859  1.288   -30.253 1.00 26.62  ? 29  TRP D CZ2 1 
ATOM   5325 C CZ3 . TRP E 5 30  ? 9.677  2.438   -32.230 1.00 27.41  ? 29  TRP D CZ3 1 
ATOM   5326 C CH2 . TRP E 5 30  ? 9.631  1.308   -31.389 1.00 29.94  ? 29  TRP D CH2 1 
ATOM   5327 N N   . TRP E 5 31  ? 5.989  9.137   -30.237 1.00 33.82  ? 30  TRP D N   1 
ATOM   5328 C CA  . TRP E 5 31  ? 5.826  10.445  -30.858 1.00 26.29  ? 30  TRP D CA  1 
ATOM   5329 C C   . TRP E 5 31  ? 7.150  11.068  -31.271 1.00 32.50  ? 30  TRP D C   1 
ATOM   5330 O O   . TRP E 5 31  ? 7.159  12.145  -31.886 1.00 31.51  ? 30  TRP D O   1 
ATOM   5331 C CB  . TRP E 5 31  ? 5.045  11.392  -29.936 1.00 27.90  ? 30  TRP D CB  1 
ATOM   5332 C CG  . TRP E 5 31  ? 5.575  11.573  -28.521 1.00 30.79  ? 30  TRP D CG  1 
ATOM   5333 C CD1 . TRP E 5 31  ? 5.131  10.953  -27.395 1.00 27.62  ? 30  TRP D CD1 1 
ATOM   5334 C CD2 . TRP E 5 31  ? 6.609  12.484  -28.102 1.00 26.54  ? 30  TRP D CD2 1 
ATOM   5335 N NE1 . TRP E 5 31  ? 5.840  11.409  -26.297 1.00 32.96  ? 30  TRP D NE1 1 
ATOM   5336 C CE2 . TRP E 5 31  ? 6.755  12.341  -26.714 1.00 27.56  ? 30  TRP D CE2 1 
ATOM   5337 C CE3 . TRP E 5 31  ? 7.437  13.392  -28.779 1.00 27.82  ? 30  TRP D CE3 1 
ATOM   5338 C CZ2 . TRP E 5 31  ? 7.685  13.087  -25.980 1.00 28.07  ? 30  TRP D CZ2 1 
ATOM   5339 C CZ3 . TRP E 5 31  ? 8.363  14.127  -28.050 1.00 29.53  ? 30  TRP D CZ3 1 
ATOM   5340 C CH2 . TRP E 5 31  ? 8.473  13.974  -26.668 1.00 23.25  ? 30  TRP D CH2 1 
ATOM   5341 N N   . SER E 5 32  ? 8.229  10.392  -30.969 1.00 30.92  ? 31  SER D N   1 
ATOM   5342 C CA  . SER E 5 32  ? 9.570  10.791  -31.433 1.00 34.55  ? 31  SER D CA  1 
ATOM   5343 C C   . SER E 5 32  ? 10.194 9.509   -31.970 1.00 30.26  ? 31  SER D C   1 
ATOM   5344 O O   . SER E 5 32  ? 10.350 8.641   -31.198 1.00 33.61  ? 31  SER D O   1 
ATOM   5345 C CB  . SER E 5 32  ? 10.366 11.402  -30.330 1.00 29.10  ? 31  SER D CB  1 
ATOM   5346 O OG  . SER E 5 32  ? 11.560 11.910  -30.828 1.00 31.03  ? 31  SER D OG  1 
ATOM   5347 N N   . TYR E 5 33  ? 10.528 9.443   -33.250 1.00 31.55  ? 32  TYR D N   1 
ATOM   5348 C CA  . TYR E 5 33  ? 10.956 8.164   -33.846 1.00 31.08  ? 32  TYR D CA  1 
ATOM   5349 C C   . TYR E 5 33  ? 11.622 8.316   -35.208 1.00 29.97  ? 32  TYR D C   1 
ATOM   5350 O O   . TYR E 5 33  ? 11.809 9.378   -35.702 1.00 29.91  ? 32  TYR D O   1 
ATOM   5351 C CB  . TYR E 5 33  ? 9.736  7.262   -34.020 1.00 30.02  ? 32  TYR D CB  1 
ATOM   5352 C CG  . TYR E 5 33  ? 8.563  7.875   -34.735 1.00 34.01  ? 32  TYR D CG  1 
ATOM   5353 C CD1 . TYR E 5 33  ? 8.500  7.891   -36.107 1.00 31.31  ? 32  TYR D CD1 1 
ATOM   5354 C CD2 . TYR E 5 33  ? 7.522  8.451   -34.040 1.00 34.43  ? 32  TYR D CD2 1 
ATOM   5355 C CE1 . TYR E 5 33  ? 7.425  8.428   -36.779 1.00 31.68  ? 32  TYR D CE1 1 
ATOM   5356 C CE2 . TYR E 5 33  ? 6.430  8.979   -34.696 1.00 39.48  ? 32  TYR D CE2 1 
ATOM   5357 C CZ  . TYR E 5 33  ? 6.384  8.966   -36.072 1.00 33.95  ? 32  TYR D CZ  1 
ATOM   5358 O OH  . TYR E 5 33  ? 5.339  9.501   -36.727 1.00 39.15  ? 32  TYR D OH  1 
ATOM   5359 N N   . TYR E 5 34  ? 11.969 7.171   -35.770 1.00 30.51  ? 33  TYR D N   1 
ATOM   5360 C CA  . TYR E 5 34  ? 12.621 7.050   -37.085 1.00 27.34  ? 33  TYR D CA  1 
ATOM   5361 C C   . TYR E 5 34  ? 11.947 5.939   -37.877 1.00 29.71  ? 33  TYR D C   1 
ATOM   5362 O O   . TYR E 5 34  ? 11.422 5.024   -37.321 1.00 29.88  ? 33  TYR D O   1 
ATOM   5363 C CB  . TYR E 5 34  ? 14.091 6.660   -36.936 1.00 31.29  ? 33  TYR D CB  1 
ATOM   5364 C CG  . TYR E 5 34  ? 14.973 7.724   -36.370 1.00 33.97  ? 33  TYR D CG  1 
ATOM   5365 C CD1 . TYR E 5 34  ? 15.279 7.801   -35.026 1.00 37.95  ? 33  TYR D CD1 1 
ATOM   5366 C CD2 . TYR E 5 34  ? 15.461 8.690   -37.204 1.00 36.26  ? 33  TYR D CD2 1 
ATOM   5367 C CE1 . TYR E 5 34  ? 16.066 8.819   -34.532 1.00 38.70  ? 33  TYR D CE1 1 
ATOM   5368 C CE2 . TYR E 5 34  ? 16.237 9.716   -36.728 1.00 36.88  ? 33  TYR D CE2 1 
ATOM   5369 C CZ  . TYR E 5 34  ? 16.541 9.780   -35.393 1.00 37.47  ? 33  TYR D CZ  1 
ATOM   5370 O OH  . TYR E 5 34  ? 17.318 10.820  -35.016 1.00 52.36  ? 33  TYR D OH  1 
ATOM   5371 N N   . ILE E 5 35  ? 11.954 6.093   -39.182 1.00 31.26  ? 34  ILE D N   1 
ATOM   5372 C CA  . ILE E 5 35  ? 11.467 5.055   -40.112 1.00 25.89  ? 34  ILE D CA  1 
ATOM   5373 C C   . ILE E 5 35  ? 12.673 4.643   -40.923 1.00 25.57  ? 34  ILE D C   1 
ATOM   5374 O O   . ILE E 5 35  ? 13.376 5.490   -41.360 1.00 26.10  ? 34  ILE D O   1 
ATOM   5375 C CB  . ILE E 5 35  ? 10.344 5.578   -41.013 1.00 33.11  ? 34  ILE D CB  1 
ATOM   5376 C CG1 . ILE E 5 35  ? 9.050  5.706   -40.238 1.00 28.60  ? 34  ILE D CG1 1 
ATOM   5377 C CG2 . ILE E 5 35  ? 10.161 4.727   -42.244 1.00 26.27  ? 34  ILE D CG2 1 
ATOM   5378 C CD1 . ILE E 5 35  ? 8.712  7.124   -40.030 1.00 36.56  ? 34  ILE D CD1 1 
ATOM   5379 N N   . PHE E 5 36  ? 12.881 3.352   -41.064 1.00 25.00  ? 35  PHE D N   1 
ATOM   5380 C CA  . PHE E 5 36  ? 13.994 2.849   -41.854 1.00 27.56  ? 35  PHE D CA  1 
ATOM   5381 C C   . PHE E 5 36  ? 13.468 2.080   -43.062 1.00 30.35  ? 35  PHE D C   1 
ATOM   5382 O O   . PHE E 5 36  ? 12.413 1.444   -43.002 1.00 31.02  ? 35  PHE D O   1 
ATOM   5383 C CB  . PHE E 5 36  ? 14.919 1.947   -41.024 1.00 25.88  ? 35  PHE D CB  1 
ATOM   5384 C CG  . PHE E 5 36  ? 15.246 2.490   -39.647 1.00 34.68  ? 35  PHE D CG  1 
ATOM   5385 C CD1 . PHE E 5 36  ? 16.191 3.493   -39.481 1.00 31.54  ? 35  PHE D CD1 1 
ATOM   5386 C CD2 . PHE E 5 36  ? 14.623 1.974   -38.517 1.00 31.22  ? 35  PHE D CD2 1 
ATOM   5387 C CE1 . PHE E 5 36  ? 16.500 3.977   -38.208 1.00 30.18  ? 35  PHE D CE1 1 
ATOM   5388 C CE2 . PHE E 5 36  ? 14.930 2.446   -37.247 1.00 34.51  ? 35  PHE D CE2 1 
ATOM   5389 C CZ  . PHE E 5 36  ? 15.871 3.448   -37.093 1.00 34.12  ? 35  PHE D CZ  1 
ATOM   5390 N N   . TRP E 5 37  ? 14.214 2.129   -44.159 1.00 27.23  ? 36  TRP D N   1 
ATOM   5391 C CA  . TRP E 5 37  ? 13.927 1.299   -45.320 1.00 26.57  ? 36  TRP D CA  1 
ATOM   5392 C C   . TRP E 5 37  ? 15.112 0.389   -45.580 1.00 27.42  ? 36  TRP D C   1 
ATOM   5393 O O   . TRP E 5 37  ? 16.262 0.843   -45.598 1.00 29.27  ? 36  TRP D O   1 
ATOM   5394 C CB  . TRP E 5 37  ? 13.611 2.147   -46.554 1.00 26.39  ? 36  TRP D CB  1 
ATOM   5395 C CG  . TRP E 5 37  ? 12.181 2.559   -46.573 1.00 31.04  ? 36  TRP D CG  1 
ATOM   5396 C CD1 . TRP E 5 37  ? 11.668 3.767   -46.184 1.00 31.00  ? 36  TRP D CD1 1 
ATOM   5397 C CD2 . TRP E 5 37  ? 11.063 1.755   -46.971 1.00 27.70  ? 36  TRP D CD2 1 
ATOM   5398 N NE1 . TRP E 5 37  ? 10.298 3.764   -46.316 1.00 29.76  ? 36  TRP D NE1 1 
ATOM   5399 C CE2 . TRP E 5 37  ? 9.904  2.542   -46.806 1.00 31.84  ? 36  TRP D CE2 1 
ATOM   5400 C CE3 . TRP E 5 37  ? 10.931 0.451   -47.457 1.00 28.97  ? 36  TRP D CE3 1 
ATOM   5401 C CZ2 . TRP E 5 37  ? 8.630  2.067   -47.118 1.00 27.26  ? 36  TRP D CZ2 1 
ATOM   5402 C CZ3 . TRP E 5 37  ? 9.669  -0.021  -47.761 1.00 31.80  ? 36  TRP D CZ3 1 
ATOM   5403 C CH2 . TRP E 5 37  ? 8.532  0.784   -47.590 1.00 29.47  ? 36  TRP D CH2 1 
ATOM   5404 N N   . TYR E 5 38  ? 14.827 -0.893  -45.784 1.00 27.83  ? 37  TYR D N   1 
ATOM   5405 C CA  . TYR E 5 38  ? 15.855 -1.885  -46.038 1.00 30.59  ? 37  TYR D CA  1 
ATOM   5406 C C   . TYR E 5 38  ? 15.566 -2.620  -47.337 1.00 29.37  ? 37  TYR D C   1 
ATOM   5407 O O   . TYR E 5 38  ? 14.417 -2.745  -47.768 1.00 28.67  ? 37  TYR D O   1 
ATOM   5408 C CB  . TYR E 5 38  ? 15.953 -2.912  -44.894 1.00 30.05  ? 37  TYR D CB  1 
ATOM   5409 C CG  . TYR E 5 38  ? 16.175 -2.314  -43.526 1.00 26.78  ? 37  TYR D CG  1 
ATOM   5410 C CD1 . TYR E 5 38  ? 17.453 -2.029  -43.068 1.00 30.18  ? 37  TYR D CD1 1 
ATOM   5411 C CD2 . TYR E 5 38  ? 15.104 -2.052  -42.686 1.00 28.80  ? 37  TYR D CD2 1 
ATOM   5412 C CE1 . TYR E 5 38  ? 17.658 -1.489  -41.789 1.00 33.39  ? 37  TYR D CE1 1 
ATOM   5413 C CE2 . TYR E 5 38  ? 15.293 -1.510  -41.421 1.00 31.73  ? 37  TYR D CE2 1 
ATOM   5414 C CZ  . TYR E 5 38  ? 16.566 -1.229  -40.979 1.00 29.33  ? 37  TYR D CZ  1 
ATOM   5415 O OH  . TYR E 5 38  ? 16.731 -0.693  -39.727 1.00 32.80  ? 37  TYR D OH  1 
ATOM   5416 N N   . LYS E 5 39  ? 16.632 -3.136  -47.926 1.00 28.23  ? 38  LYS D N   1 
ATOM   5417 C CA  . LYS E 5 39  ? 16.593 -3.926  -49.144 1.00 28.55  ? 38  LYS D CA  1 
ATOM   5418 C C   . LYS E 5 39  ? 17.178 -5.295  -48.816 1.00 30.63  ? 38  LYS D C   1 
ATOM   5419 O O   . LYS E 5 39  ? 18.302 -5.375  -48.315 1.00 31.19  ? 38  LYS D O   1 
ATOM   5420 C CB  . LYS E 5 39  ? 17.406 -3.216  -50.232 1.00 32.99  ? 38  LYS D CB  1 
ATOM   5421 C CG  . LYS E 5 39  ? 17.324 -3.788  -51.625 1.00 31.79  ? 38  LYS D CG  1 
ATOM   5422 C CD  . LYS E 5 39  ? 18.478 -3.264  -52.496 1.00 27.33  ? 38  LYS D CD  1 
ATOM   5423 C CE  . LYS E 5 39  ? 18.418 -3.904  -53.885 1.00 29.84  ? 38  LYS D CE  1 
ATOM   5424 N NZ  . LYS E 5 39  ? 19.630 -3.686  -54.732 1.00 41.78  ? 38  LYS D NZ  1 
ATOM   5425 N N   . GLN E 5 40  ? 16.422 -6.368  -49.064 1.00 25.86  ? 39  GLN D N   1 
ATOM   5426 C CA  . GLN E 5 40  ? 16.943 -7.721  -48.893 1.00 27.27  ? 39  GLN D CA  1 
ATOM   5427 C C   . GLN E 5 40  ? 17.080 -8.400  -50.250 1.00 30.53  ? 39  GLN D C   1 
ATOM   5428 O O   . GLN E 5 40  ? 16.082 -8.635  -50.941 1.00 31.33  ? 39  GLN D O   1 
ATOM   5429 C CB  . GLN E 5 40  ? 16.071 -8.568  -47.968 1.00 28.73  ? 39  GLN D CB  1 
ATOM   5430 C CG  . GLN E 5 40  ? 16.689 -9.953  -47.670 1.00 27.51  ? 39  GLN D CG  1 
ATOM   5431 C CD  . GLN E 5 40  ? 15.929 -10.724 -46.602 1.00 26.85  ? 39  GLN D CD  1 
ATOM   5432 O OE1 . GLN E 5 40  ? 14.696 -10.718 -46.575 1.00 30.07  ? 39  GLN D OE1 1 
ATOM   5433 N NE2 . GLN E 5 40  ? 16.665 -11.371 -45.693 1.00 25.98  ? 39  GLN D NE2 1 
ATOM   5434 N N   . LEU E 5 41  ? 18.318 -8.733  -50.604 1.00 30.76  ? 40  LEU D N   1 
ATOM   5435 C CA  . LEU E 5 41  ? 18.630 -9.392  -51.852 1.00 32.30  ? 40  LEU D CA  1 
ATOM   5436 C C   . LEU E 5 41  ? 18.138 -10.835 -51.841 1.00 33.65  ? 40  LEU D C   1 
ATOM   5437 O O   . LEU E 5 41  ? 17.884 -11.406 -50.775 1.00 30.16  ? 40  LEU D O   1 
ATOM   5438 C CB  . LEU E 5 41  ? 20.139 -9.371  -52.099 1.00 26.76  ? 40  LEU D CB  1 
ATOM   5439 C CG  . LEU E 5 41  ? 20.768 -7.984  -52.142 1.00 34.61  ? 40  LEU D CG  1 
ATOM   5440 C CD1 . LEU E 5 41  ? 22.171 -8.063  -52.720 1.00 33.61  ? 40  LEU D CD1 1 
ATOM   5441 C CD2 . LEU E 5 41  ? 19.889 -7.040  -52.948 1.00 40.71  ? 40  LEU D CD2 1 
ATOM   5442 N N   . PRO E 5 42  ? 17.989 -11.439 -53.033 1.00 37.11  ? 41  PRO D N   1 
ATOM   5443 C CA  . PRO E 5 42  ? 17.715 -12.887 -53.110 1.00 30.99  ? 41  PRO D CA  1 
ATOM   5444 C C   . PRO E 5 42  ? 18.687 -13.738 -52.300 1.00 32.61  ? 41  PRO D C   1 
ATOM   5445 O O   . PRO E 5 42  ? 18.286 -14.773 -51.758 1.00 35.04  ? 41  PRO D O   1 
ATOM   5446 C CB  . PRO E 5 42  ? 17.833 -13.179 -54.618 1.00 35.61  ? 41  PRO D CB  1 
ATOM   5447 C CG  . PRO E 5 42  ? 17.511 -11.883 -55.292 1.00 30.70  ? 41  PRO D CG  1 
ATOM   5448 C CD  . PRO E 5 42  ? 17.888 -10.769 -54.350 1.00 33.62  ? 41  PRO D CD  1 
ATOM   5449 N N   . SER E 5 43  ? 19.955 -13.339 -52.201 1.00 33.28  ? 42  SER D N   1 
ATOM   5450 C CA  . SER E 5 43  ? 20.920 -13.996 -51.325 1.00 35.72  ? 42  SER D CA  1 
ATOM   5451 C C   . SER E 5 43  ? 20.572 -13.894 -49.839 1.00 35.79  ? 42  SER D C   1 
ATOM   5452 O O   . SER E 5 43  ? 21.340 -14.412 -49.022 1.00 40.54  ? 42  SER D O   1 
ATOM   5453 C CB  . SER E 5 43  ? 22.292 -13.372 -51.530 1.00 34.79  ? 42  SER D CB  1 
ATOM   5454 O OG  . SER E 5 43  ? 22.311 -12.128 -50.849 1.00 32.82  ? 42  SER D OG  1 
ATOM   5455 N N   . LYS E 5 44  ? 19.483 -13.202 -49.482 1.00 32.84  ? 43  LYS D N   1 
ATOM   5456 C CA  . LYS E 5 44  ? 19.031 -12.796 -48.145 1.00 30.66  ? 43  LYS D CA  1 
ATOM   5457 C C   . LYS E 5 44  ? 19.952 -11.763 -47.475 1.00 31.92  ? 43  LYS D C   1 
ATOM   5458 O O   . LYS E 5 44  ? 19.708 -11.395 -46.321 1.00 35.53  ? 43  LYS D O   1 
ATOM   5459 C CB  . LYS E 5 44  ? 18.866 -13.972 -47.169 1.00 36.11  ? 43  LYS D CB  1 
ATOM   5460 C CG  . LYS E 5 44  ? 18.025 -15.114 -47.613 1.00 33.01  ? 43  LYS D CG  1 
ATOM   5461 C CD  . LYS E 5 44  ? 16.665 -14.659 -48.120 1.00 38.54  ? 43  LYS D CD  1 
ATOM   5462 C CE  . LYS E 5 44  ? 15.761 -15.855 -48.023 1.00 44.92  ? 43  LYS D CE  1 
ATOM   5463 N NZ  . LYS E 5 44  ? 14.814 -15.716 -49.139 1.00 48.68  ? 43  LYS D NZ  1 
ATOM   5464 N N   . GLU E 5 45  ? 21.007 -11.299 -48.135 1.00 31.40  ? 44  GLU D N   1 
ATOM   5465 C CA  . GLU E 5 45  ? 21.760 -10.170 -47.610 1.00 33.32  ? 44  GLU D CA  1 
ATOM   5466 C C   . GLU E 5 45  ? 20.832 -8.987  -47.361 1.00 34.75  ? 44  GLU D C   1 
ATOM   5467 O O   . GLU E 5 45  ? 19.972 -8.665  -48.190 1.00 32.83  ? 44  GLU D O   1 
ATOM   5468 C CB  . GLU E 5 45  ? 22.853 -9.763  -48.586 1.00 32.60  ? 44  GLU D CB  1 
ATOM   5469 C CG  . GLU E 5 45  ? 23.659 -8.586  -48.094 1.00 32.44  ? 44  GLU D CG  1 
ATOM   5470 C CD  . GLU E 5 45  ? 24.646 -8.085  -49.127 1.00 41.82  ? 44  GLU D CD  1 
ATOM   5471 O OE1 . GLU E 5 45  ? 25.131 -6.942  -48.970 1.00 46.26  ? 44  GLU D OE1 1 
ATOM   5472 O OE2 . GLU E 5 45  ? 24.934 -8.827  -50.099 1.00 45.47  ? 44  GLU D OE2 1 
ATOM   5473 N N   . MET E 5 46  ? 21.008 -8.344  -46.211 1.00 30.12  ? 45  MET D N   1 
ATOM   5474 C CA  . MET E 5 46  ? 20.187 -7.222  -45.782 1.00 29.10  ? 45  MET D CA  1 
ATOM   5475 C C   . MET E 5 46  ? 20.989 -5.932  -45.919 1.00 28.59  ? 45  MET D C   1 
ATOM   5476 O O   . MET E 5 46  ? 22.168 -5.882  -45.550 1.00 30.36  ? 45  MET D O   1 
ATOM   5477 C CB  . MET E 5 46  ? 19.714 -7.425  -44.341 1.00 28.42  ? 45  MET D CB  1 
ATOM   5478 C CG  . MET E 5 46  ? 18.674 -6.416  -43.897 1.00 37.14  ? 45  MET D CG  1 
ATOM   5479 S SD  . MET E 5 46  ? 17.048 -6.836  -44.557 1.00 37.96  ? 45  MET D SD  1 
ATOM   5480 C CE  . MET E 5 46  ? 17.085 -8.582  -44.304 1.00 26.43  ? 45  MET D CE  1 
ATOM   5481 N N   . ILE E 5 47  ? 20.360 -4.897  -46.470 1.00 28.25  ? 46  ILE D N   1 
ATOM   5482 C CA  . ILE E 5 47  ? 21.065 -3.681  -46.861 1.00 30.81  ? 46  ILE D CA  1 
ATOM   5483 C C   . ILE E 5 47  ? 20.218 -2.492  -46.452 1.00 30.76  ? 46  ILE D C   1 
ATOM   5484 O O   . ILE E 5 47  ? 19.062 -2.379  -46.880 1.00 29.45  ? 46  ILE D O   1 
ATOM   5485 C CB  . ILE E 5 47  ? 21.354 -3.635  -48.374 1.00 33.32  ? 46  ILE D CB  1 
ATOM   5486 C CG1 . ILE E 5 47  ? 22.365 -4.717  -48.755 1.00 34.63  ? 46  ILE D CG1 1 
ATOM   5487 C CG2 . ILE E 5 47  ? 21.836 -2.246  -48.808 1.00 30.23  ? 46  ILE D CG2 1 
ATOM   5488 C CD1 . ILE E 5 47  ? 22.234 -5.175  -50.177 1.00 34.65  ? 46  ILE D CD1 1 
ATOM   5489 N N   . PHE E 5 48  ? 20.785 -1.615  -45.624 1.00 28.08  ? 47  PHE D N   1 
ATOM   5490 C CA  . PHE E 5 48  ? 20.098 -0.398  -45.213 1.00 27.22  ? 47  PHE D CA  1 
ATOM   5491 C C   . PHE E 5 48  ? 20.086 0.600   -46.357 1.00 28.94  ? 47  PHE D C   1 
ATOM   5492 O O   . PHE E 5 48  ? 21.104 0.814   -47.023 1.00 27.59  ? 47  PHE D O   1 
ATOM   5493 C CB  . PHE E 5 48  ? 20.783 0.221   -43.985 1.00 29.69  ? 47  PHE D CB  1 
ATOM   5494 C CG  . PHE E 5 48  ? 20.416 1.667   -43.731 1.00 27.32  ? 47  PHE D CG  1 
ATOM   5495 C CD1 . PHE E 5 48  ? 19.347 1.989   -42.909 1.00 30.22  ? 47  PHE D CD1 1 
ATOM   5496 C CD2 . PHE E 5 48  ? 21.158 2.700   -44.288 1.00 29.35  ? 47  PHE D CD2 1 
ATOM   5497 C CE1 . PHE E 5 48  ? 19.017 3.312   -42.644 1.00 31.69  ? 47  PHE D CE1 1 
ATOM   5498 C CE2 . PHE E 5 48  ? 20.825 4.035   -44.037 1.00 31.47  ? 47  PHE D CE2 1 
ATOM   5499 C CZ  . PHE E 5 48  ? 19.752 4.337   -43.217 1.00 29.71  ? 47  PHE D CZ  1 
ATOM   5500 N N   . LEU E 5 49  ? 18.936 1.245   -46.558 1.00 29.65  ? 48  LEU D N   1 
ATOM   5501 C CA  . LEU E 5 49  ? 18.754 2.165   -47.676 1.00 29.01  ? 48  LEU D CA  1 
ATOM   5502 C C   . LEU E 5 49  ? 18.674 3.619   -47.229 1.00 28.74  ? 48  LEU D C   1 
ATOM   5503 O O   . LEU E 5 49  ? 19.447 4.452   -47.706 1.00 30.58  ? 48  LEU D O   1 
ATOM   5504 C CB  . LEU E 5 49  ? 17.490 1.790   -48.468 1.00 29.87  ? 48  LEU D CB  1 
ATOM   5505 C CG  . LEU E 5 49  ? 17.439 0.424   -49.162 1.00 29.79  ? 48  LEU D CG  1 
ATOM   5506 C CD1 . LEU E 5 49  ? 16.130 0.290   -49.915 1.00 23.73  ? 48  LEU D CD1 1 
ATOM   5507 C CD2 . LEU E 5 49  ? 18.630 0.220   -50.093 1.00 25.74  ? 48  LEU D CD2 1 
ATOM   5508 N N   . ILE E 5 50  ? 17.741 3.960   -46.339 1.00 28.68  ? 49  ILE D N   1 
ATOM   5509 C CA  . ILE E 5 50  ? 17.464 5.360   -46.033 1.00 32.23  ? 49  ILE D CA  1 
ATOM   5510 C C   . ILE E 5 50  ? 16.665 5.442   -44.740 1.00 27.75  ? 49  ILE D C   1 
ATOM   5511 O O   . ILE E 5 50  ? 15.936 4.516   -44.371 1.00 26.36  ? 49  ILE D O   1 
ATOM   5512 C CB  . ILE E 5 50  ? 16.732 6.060   -47.211 1.00 33.16  ? 49  ILE D CB  1 
ATOM   5513 C CG1 . ILE E 5 50  ? 16.693 7.581   -47.021 1.00 34.74  ? 49  ILE D CG1 1 
ATOM   5514 C CG2 . ILE E 5 50  ? 15.317 5.515   -47.406 1.00 29.03  ? 49  ILE D CG2 1 
ATOM   5515 C CD1 . ILE E 5 50  ? 16.291 8.351   -48.284 1.00 33.04  ? 49  ILE D CD1 1 
ATOM   5516 N N   . ARG E 5 51  ? 16.795 6.566   -44.053 1.00 32.41  ? 50  ARG D N   1 
ATOM   5517 C CA  . ARG E 5 51  ? 16.189 6.768   -42.751 1.00 30.65  ? 50  ARG D CA  1 
ATOM   5518 C C   . ARG E 5 51  ? 15.424 8.085   -42.763 1.00 29.05  ? 50  ARG D C   1 
ATOM   5519 O O   . ARG E 5 51  ? 15.885 9.076   -43.338 1.00 22.63  ? 50  ARG D O   1 
ATOM   5520 C CB  . ARG E 5 51  ? 17.279 6.741   -41.681 1.00 33.38  ? 50  ARG D CB  1 
ATOM   5521 C CG  . ARG E 5 51  ? 16.877 7.240   -40.313 1.00 33.95  ? 50  ARG D CG  1 
ATOM   5522 C CD  . ARG E 5 51  ? 18.099 7.343   -39.406 1.00 34.21  ? 50  ARG D CD  1 
ATOM   5523 N NE  . ARG E 5 51  ? 19.015 8.419   -39.782 1.00 36.03  ? 50  ARG D NE  1 
ATOM   5524 C CZ  . ARG E 5 51  ? 19.011 9.637   -39.236 1.00 44.36  ? 50  ARG D CZ  1 
ATOM   5525 N NH1 . ARG E 5 51  ? 18.120 9.957   -38.310 1.00 48.71  ? 50  ARG D NH1 1 
ATOM   5526 N NH2 . ARG E 5 51  ? 19.883 10.552  -39.629 1.00 45.51  ? 50  ARG D NH2 1 
ATOM   5527 N N   . GLN E 5 52  ? 14.240 8.083   -42.160 1.00 26.76  ? 51  GLN D N   1 
ATOM   5528 C CA  . GLN E 5 52  ? 13.358 9.244   -42.161 1.00 30.31  ? 51  GLN D CA  1 
ATOM   5529 C C   . GLN E 5 52  ? 13.040 9.609   -40.719 1.00 32.11  ? 51  GLN D C   1 
ATOM   5530 O O   . GLN E 5 52  ? 12.439 8.810   -39.989 1.00 29.31  ? 51  GLN D O   1 
ATOM   5531 C CB  . GLN E 5 52  ? 12.081 8.957   -42.956 1.00 30.27  ? 51  GLN D CB  1 
ATOM   5532 C CG  . GLN E 5 52  ? 10.994 10.017  -42.830 1.00 37.26  ? 51  GLN D CG  1 
ATOM   5533 C CD  . GLN E 5 52  ? 11.357 11.315  -43.520 1.00 33.62  ? 51  GLN D CD  1 
ATOM   5534 O OE1 . GLN E 5 52  ? 11.590 11.342  -44.725 1.00 35.46  ? 51  GLN D OE1 1 
ATOM   5535 N NE2 . GLN E 5 52  ? 11.429 12.408  -42.745 1.00 37.63  ? 51  GLN D NE2 1 
ATOM   5536 N N   . GLY E 5 53  ? 13.472 10.796  -40.300 1.00 30.40  ? 52  GLY D N   1 
ATOM   5537 C CA  . GLY E 5 53  ? 13.226 11.233  -38.932 1.00 29.19  ? 52  GLY D CA  1 
ATOM   5538 C C   . GLY E 5 53  ? 11.831 11.819  -38.772 1.00 31.19  ? 52  GLY D C   1 
ATOM   5539 O O   . GLY E 5 53  ? 11.296 12.473  -39.670 1.00 34.53  ? 52  GLY D O   1 
ATOM   5540 N N   . SER E 5 54  ? 11.242 11.574  -37.604 1.00 28.33  ? 53  SER D N   1 
ATOM   5541 C CA  . SER E 5 54  ? 9.888  12.033  -37.335 1.00 31.92  ? 53  SER D CA  1 
ATOM   5542 C C   . SER E 5 54  ? 9.749  13.564  -37.337 1.00 36.60  ? 53  SER D C   1 
ATOM   5543 O O   . SER E 5 54  ? 8.629  14.064  -37.486 1.00 37.82  ? 53  SER D O   1 
ATOM   5544 C CB  . SER E 5 54  ? 9.419  11.449  -36.001 1.00 30.33  ? 53  SER D CB  1 
ATOM   5545 O OG  . SER E 5 54  ? 10.067 12.088  -34.916 1.00 35.97  ? 53  SER D OG  1 
ATOM   5546 N N   . ASP E 5 55  ? 10.843 14.319  -37.178 1.00 36.89  ? 54  ASP D N   1 
ATOM   5547 C CA  . ASP E 5 55  ? 10.815 15.783  -37.169 1.00 40.08  ? 54  ASP D CA  1 
ATOM   5548 C C   . ASP E 5 55  ? 11.572 16.385  -38.338 1.00 37.69  ? 54  ASP D C   1 
ATOM   5549 O O   . ASP E 5 55  ? 11.966 17.552  -38.276 1.00 40.32  ? 54  ASP D O   1 
ATOM   5550 C CB  . ASP E 5 55  ? 11.428 16.362  -35.890 1.00 35.66  ? 54  ASP D CB  1 
ATOM   5551 C CG  . ASP E 5 55  ? 10.897 15.731  -34.645 1.00 42.22  ? 54  ASP D CG  1 
ATOM   5552 O OD1 . ASP E 5 55  ? 9.670  15.477  -34.592 1.00 47.28  ? 54  ASP D OD1 1 
ATOM   5553 O OD2 . ASP E 5 55  ? 11.717 15.494  -33.719 1.00 37.70  ? 54  ASP D OD2 1 
ATOM   5554 N N   . GLU E 5 56  ? 11.848 15.602  -39.366 1.00 37.53  ? 55  GLU D N   1 
ATOM   5555 C CA  . GLU E 5 56  ? 12.703 16.041  -40.455 1.00 39.83  ? 55  GLU D CA  1 
ATOM   5556 C C   . GLU E 5 56  ? 11.889 16.239  -41.725 1.00 35.75  ? 55  GLU D C   1 
ATOM   5557 O O   . GLU E 5 56  ? 10.737 15.814  -41.825 1.00 36.15  ? 55  GLU D O   1 
ATOM   5558 C CB  . GLU E 5 56  ? 13.833 15.034  -40.694 1.00 38.01  ? 55  GLU D CB  1 
ATOM   5559 C CG  . GLU E 5 56  ? 14.743 14.876  -39.478 1.00 38.20  ? 55  GLU D CG  1 
ATOM   5560 C CD  . GLU E 5 56  ? 15.670 13.682  -39.598 1.00 44.68  ? 55  GLU D CD  1 
ATOM   5561 O OE1 . GLU E 5 56  ? 15.856 13.169  -40.723 1.00 43.41  ? 55  GLU D OE1 1 
ATOM   5562 O OE2 . GLU E 5 56  ? 16.213 13.251  -38.560 1.00 51.59  ? 55  GLU D OE2 1 
ATOM   5563 N N   . GLN E 5 57  ? 12.496 16.929  -42.685 1.00 39.76  ? 56  GLN D N   1 
ATOM   5564 C CA  . GLN E 5 57  ? 11.902 17.028  -44.001 1.00 39.45  ? 56  GLN D CA  1 
ATOM   5565 C C   . GLN E 5 57  ? 11.990 15.672  -44.687 1.00 41.58  ? 56  GLN D C   1 
ATOM   5566 O O   . GLN E 5 57  ? 12.646 14.745  -44.204 1.00 40.80  ? 56  GLN D O   1 
ATOM   5567 C CB  . GLN E 5 57  ? 12.599 18.109  -44.832 1.00 43.43  ? 56  GLN D CB  1 
ATOM   5568 C CG  . GLN E 5 57  ? 12.342 19.547  -44.344 1.00 47.04  ? 56  GLN D CG  1 
ATOM   5569 C CD  . GLN E 5 57  ? 10.866 19.854  -44.129 1.00 49.75  ? 56  GLN D CD  1 
ATOM   5570 O OE1 . GLN E 5 57  ? 10.115 20.075  -45.082 1.00 57.80  ? 56  GLN D OE1 1 
ATOM   5571 N NE2 . GLN E 5 57  ? 10.448 19.883  -42.871 1.00 53.06  ? 56  GLN D NE2 1 
ATOM   5572 N N   . ASN E 5 58  ? 11.308 15.554  -45.821 1.00 38.80  ? 57  ASN D N   1 
ATOM   5573 C CA  . ASN E 5 58  ? 11.271 14.289  -46.531 1.00 35.13  ? 57  ASN D CA  1 
ATOM   5574 C C   . ASN E 5 58  ? 12.687 13.859  -46.886 1.00 35.90  ? 57  ASN D C   1 
ATOM   5575 O O   . ASN E 5 58  ? 13.428 14.610  -47.528 1.00 31.25  ? 57  ASN D O   1 
ATOM   5576 C CB  . ASN E 5 58  ? 10.403 14.418  -47.785 1.00 30.13  ? 57  ASN D CB  1 
ATOM   5577 C CG  . ASN E 5 58  ? 8.925  14.346  -47.474 1.00 31.11  ? 57  ASN D CG  1 
ATOM   5578 O OD1 . ASN E 5 58  ? 8.521  13.893  -46.399 1.00 30.48  ? 57  ASN D OD1 1 
ATOM   5579 N ND2 . ASN E 5 58  ? 8.105  14.797  -48.410 1.00 33.80  ? 57  ASN D ND2 1 
ATOM   5580 N N   . ALA E 5 59  ? 13.064 12.659  -46.439 1.00 30.80  ? 58  ALA D N   1 
ATOM   5581 C CA  . ALA E 5 59  ? 14.401 12.145  -46.696 1.00 32.01  ? 58  ALA D CA  1 
ATOM   5582 C C   . ALA E 5 59  ? 14.586 11.824  -48.171 1.00 32.55  ? 58  ALA D C   1 
ATOM   5583 O O   . ALA E 5 59  ? 13.657 11.405  -48.864 1.00 34.91  ? 58  ALA D O   1 
ATOM   5584 C CB  . ALA E 5 59  ? 14.665 10.890  -45.860 1.00 33.91  ? 58  ALA D CB  1 
ATOM   5585 N N   . LYS E 5 60  ? 15.809 12.014  -48.651 1.00 35.04  ? 59  LYS D N   1 
ATOM   5586 C CA  . LYS E 5 60  ? 16.117 11.770  -50.051 1.00 36.15  ? 59  LYS D CA  1 
ATOM   5587 C C   . LYS E 5 60  ? 17.573 11.353  -50.144 1.00 38.07  ? 59  LYS D C   1 
ATOM   5588 O O   . LYS E 5 60  ? 18.434 11.942  -49.485 1.00 38.61  ? 59  LYS D O   1 
ATOM   5589 C CB  . LYS E 5 60  ? 15.853 13.011  -50.913 1.00 41.46  ? 59  LYS D CB  1 
ATOM   5590 C CG  . LYS E 5 60  ? 16.087 12.796  -52.407 1.00 42.59  ? 59  LYS D CG  1 
ATOM   5591 C CD  . LYS E 5 60  ? 15.133 13.622  -53.269 1.00 43.89  ? 59  LYS D CD  1 
ATOM   5592 C CE  . LYS E 5 60  ? 15.210 13.195  -54.738 1.00 50.16  ? 59  LYS D CE  1 
ATOM   5593 N NZ  . LYS E 5 60  ? 13.932 13.418  -55.477 1.00 52.73  ? 59  LYS D NZ  1 
ATOM   5594 N N   . SER E 5 61  ? 17.837 10.322  -50.940 1.00 38.34  ? 60  SER D N   1 
ATOM   5595 C CA  . SER E 5 61  ? 19.201 9.828   -51.110 1.00 41.05  ? 60  SER D CA  1 
ATOM   5596 C C   . SER E 5 61  ? 19.273 9.034   -52.411 1.00 38.88  ? 60  SER D C   1 
ATOM   5597 O O   . SER E 5 61  ? 18.660 7.965   -52.519 1.00 37.94  ? 60  SER D O   1 
ATOM   5598 C CB  . SER E 5 61  ? 19.615 8.974   -49.920 1.00 41.00  ? 60  SER D CB  1 
ATOM   5599 O OG  . SER E 5 61  ? 20.911 8.429   -50.126 1.00 47.32  ? 60  SER D OG  1 
ATOM   5600 N N   . GLY E 5 62  ? 20.029 9.546   -53.378 1.00 36.53  ? 61  GLY D N   1 
ATOM   5601 C CA  . GLY E 5 62  ? 20.135 8.882   -54.670 1.00 39.02  ? 61  GLY D CA  1 
ATOM   5602 C C   . GLY E 5 62  ? 18.773 8.724   -55.324 1.00 37.18  ? 61  GLY D C   1 
ATOM   5603 O O   . GLY E 5 62  ? 17.965 9.658   -55.372 1.00 37.95  ? 61  GLY D O   1 
ATOM   5604 N N   . ARG E 5 63  ? 18.494 7.519   -55.813 1.00 35.89  ? 62  ARG D N   1 
ATOM   5605 C CA  . ARG E 5 63  ? 17.202 7.250   -56.432 1.00 35.94  ? 62  ARG D CA  1 
ATOM   5606 C C   . ARG E 5 63  ? 16.114 6.939   -55.413 1.00 36.18  ? 62  ARG D C   1 
ATOM   5607 O O   . ARG E 5 63  ? 14.969 6.685   -55.805 1.00 36.36  ? 62  ARG D O   1 
ATOM   5608 C CB  . ARG E 5 63  ? 17.333 6.099   -57.430 1.00 37.90  ? 62  ARG D CB  1 
ATOM   5609 C CG  . ARG E 5 63  ? 18.287 6.397   -58.565 1.00 34.94  ? 62  ARG D CG  1 
ATOM   5610 C CD  . ARG E 5 63  ? 18.456 5.176   -59.461 1.00 41.33  ? 62  ARG D CD  1 
ATOM   5611 N NE  . ARG E 5 63  ? 18.996 4.029   -58.730 1.00 41.45  ? 62  ARG D NE  1 
ATOM   5612 C CZ  . ARG E 5 63  ? 18.414 2.837   -58.633 1.00 35.78  ? 62  ARG D CZ  1 
ATOM   5613 N NH1 . ARG E 5 63  ? 17.243 2.597   -59.209 1.00 32.77  ? 62  ARG D NH1 1 
ATOM   5614 N NH2 . ARG E 5 63  ? 19.010 1.876   -57.950 1.00 36.43  ? 62  ARG D NH2 1 
ATOM   5615 N N   . TYR E 5 64  ? 16.435 6.960   -54.123 1.00 33.64  ? 63  TYR D N   1 
ATOM   5616 C CA  . TYR E 5 64  ? 15.460 6.736   -53.069 1.00 35.63  ? 63  TYR D CA  1 
ATOM   5617 C C   . TYR E 5 64  ? 14.942 8.059   -52.522 1.00 35.05  ? 63  TYR D C   1 
ATOM   5618 O O   . TYR E 5 64  ? 15.701 9.020   -52.357 1.00 30.26  ? 63  TYR D O   1 
ATOM   5619 C CB  . TYR E 5 64  ? 16.075 5.919   -51.930 1.00 36.20  ? 63  TYR D CB  1 
ATOM   5620 C CG  . TYR E 5 64  ? 16.808 4.672   -52.395 1.00 38.22  ? 63  TYR D CG  1 
ATOM   5621 C CD1 . TYR E 5 64  ? 16.108 3.574   -52.893 1.00 35.14  ? 63  TYR D CD1 1 
ATOM   5622 C CD2 . TYR E 5 64  ? 18.189 4.587   -52.320 1.00 33.66  ? 63  TYR D CD2 1 
ATOM   5623 C CE1 . TYR E 5 64  ? 16.767 2.431   -53.307 1.00 32.96  ? 63  TYR D CE1 1 
ATOM   5624 C CE2 . TYR E 5 64  ? 18.861 3.447   -52.731 1.00 41.72  ? 63  TYR D CE2 1 
ATOM   5625 C CZ  . TYR E 5 64  ? 18.144 2.372   -53.230 1.00 38.64  ? 63  TYR D CZ  1 
ATOM   5626 O OH  . TYR E 5 64  ? 18.805 1.240   -53.645 1.00 37.26  ? 63  TYR D OH  1 
ATOM   5627 N N   . SER E 5 65  ? 13.647 8.096   -52.222 1.00 32.69  ? 64  SER D N   1 
ATOM   5628 C CA  . SER E 5 65  ? 13.074 9.218   -51.501 1.00 35.55  ? 64  SER D CA  1 
ATOM   5629 C C   . SER E 5 65  ? 11.893 8.711   -50.693 1.00 33.42  ? 64  SER D C   1 
ATOM   5630 O O   . SER E 5 65  ? 11.281 7.694   -51.028 1.00 35.43  ? 64  SER D O   1 
ATOM   5631 C CB  . SER E 5 65  ? 12.637 10.349  -52.434 1.00 33.05  ? 64  SER D CB  1 
ATOM   5632 O OG  . SER E 5 65  ? 11.937 9.829   -53.544 1.00 42.14  ? 64  SER D OG  1 
ATOM   5633 N N   . VAL E 5 66  ? 11.588 9.425   -49.621 1.00 28.95  ? 65  VAL D N   1 
ATOM   5634 C CA  . VAL E 5 66  ? 10.485 9.094   -48.734 1.00 32.94  ? 65  VAL D CA  1 
ATOM   5635 C C   . VAL E 5 66  ? 9.465  10.226  -48.785 1.00 36.22  ? 65  VAL D C   1 
ATOM   5636 O O   . VAL E 5 66  ? 9.834  11.404  -48.764 1.00 33.94  ? 65  VAL D O   1 
ATOM   5637 C CB  . VAL E 5 66  ? 10.987 8.862   -47.298 1.00 32.38  ? 65  VAL D CB  1 
ATOM   5638 C CG1 . VAL E 5 66  ? 9.822  8.722   -46.341 1.00 28.78  ? 65  VAL D CG1 1 
ATOM   5639 C CG2 . VAL E 5 66  ? 11.869 7.623   -47.262 1.00 27.42  ? 65  VAL D CG2 1 
ATOM   5640 N N   . ASN E 5 67  ? 8.189  9.869   -48.877 1.00 35.73  ? 66  ASN D N   1 
ATOM   5641 C CA  . ASN E 5 67  ? 7.101  10.838  -48.796 1.00 35.10  ? 66  ASN D CA  1 
ATOM   5642 C C   . ASN E 5 67  ? 6.492  10.651  -47.413 1.00 30.49  ? 66  ASN D C   1 
ATOM   5643 O O   . ASN E 5 67  ? 5.634  9.798   -47.202 1.00 32.57  ? 66  ASN D O   1 
ATOM   5644 C CB  . ASN E 5 67  ? 6.085  10.636  -49.916 1.00 34.10  ? 66  ASN D CB  1 
ATOM   5645 C CG  . ASN E 5 67  ? 4.940  11.662  -49.867 1.00 42.28  ? 66  ASN D CG  1 
ATOM   5646 O OD1 . ASN E 5 67  ? 4.946  12.597  -49.058 1.00 35.64  ? 66  ASN D OD1 1 
ATOM   5647 N ND2 . ASN E 5 67  ? 3.957  11.483  -50.739 1.00 42.56  ? 66  ASN D ND2 1 
ATOM   5648 N N   . PHE E 5 68  ? 6.971  11.441  -46.456 1.00 33.29  ? 67  PHE D N   1 
ATOM   5649 C CA  . PHE E 5 68  ? 6.610  11.271  -45.054 1.00 32.65  ? 67  PHE D CA  1 
ATOM   5650 C C   . PHE E 5 68  ? 5.364  12.104  -44.763 1.00 34.03  ? 67  PHE D C   1 
ATOM   5651 O O   . PHE E 5 68  ? 5.412  13.335  -44.807 1.00 35.60  ? 67  PHE D O   1 
ATOM   5652 C CB  . PHE E 5 68  ? 7.778  11.677  -44.158 1.00 31.31  ? 67  PHE D CB  1 
ATOM   5653 C CG  . PHE E 5 68  ? 7.503  11.537  -42.674 1.00 34.39  ? 67  PHE D CG  1 
ATOM   5654 C CD1 . PHE E 5 68  ? 6.909  10.392  -42.162 1.00 34.27  ? 67  PHE D CD1 1 
ATOM   5655 C CD2 . PHE E 5 68  ? 7.857  12.547  -41.793 1.00 34.26  ? 67  PHE D CD2 1 
ATOM   5656 C CE1 . PHE E 5 68  ? 6.672  10.259  -40.791 1.00 35.44  ? 67  PHE D CE1 1 
ATOM   5657 C CE2 . PHE E 5 68  ? 7.625  12.419  -40.422 1.00 34.71  ? 67  PHE D CE2 1 
ATOM   5658 C CZ  . PHE E 5 68  ? 7.027  11.280  -39.923 1.00 34.90  ? 67  PHE D CZ  1 
ATOM   5659 N N   . LYS E 5 69  ? 4.260  11.439  -44.441 1.00 36.06  ? 68  LYS D N   1 
ATOM   5660 C CA  . LYS E 5 69  ? 3.006  12.097  -44.077 1.00 33.29  ? 68  LYS D CA  1 
ATOM   5661 C C   . LYS E 5 69  ? 2.719  11.760  -42.619 1.00 37.93  ? 68  LYS D C   1 
ATOM   5662 O O   . LYS E 5 69  ? 2.132  10.721  -42.308 1.00 38.10  ? 68  LYS D O   1 
ATOM   5663 C CB  . LYS E 5 69  ? 1.882  11.661  -45.001 1.00 38.75  ? 68  LYS D CB  1 
ATOM   5664 C CG  . LYS E 5 69  ? 2.150  12.033  -46.454 1.00 38.75  ? 68  LYS D CG  1 
ATOM   5665 C CD  . LYS E 5 69  ? 0.904  11.881  -47.314 1.00 48.18  ? 68  LYS D CD  1 
ATOM   5666 C CE  . LYS E 5 69  ? 1.135  10.913  -48.457 1.00 41.79  ? 68  LYS D CE  1 
ATOM   5667 N NZ  . LYS E 5 69  ? -0.125 10.537  -49.172 1.00 50.30  ? 68  LYS D NZ  1 
ATOM   5668 N N   . LYS E 5 70  ? 3.135  12.660  -41.721 1.00 39.97  ? 69  LYS D N   1 
ATOM   5669 C CA  . LYS E 5 70  ? 3.170  12.318  -40.306 1.00 35.91  ? 69  LYS D CA  1 
ATOM   5670 C C   . LYS E 5 70  ? 1.777  12.080  -39.754 1.00 39.06  ? 69  LYS D C   1 
ATOM   5671 O O   . LYS E 5 70  ? 1.555  11.108  -39.016 1.00 34.85  ? 69  LYS D O   1 
ATOM   5672 C CB  . LYS E 5 70  ? 3.868  13.409  -39.505 1.00 36.37  ? 69  LYS D CB  1 
ATOM   5673 C CG  . LYS E 5 70  ? 3.860  13.102  -38.017 1.00 43.42  ? 69  LYS D CG  1 
ATOM   5674 C CD  . LYS E 5 70  ? 4.531  14.187  -37.197 1.00 40.31  ? 69  LYS D CD  1 
ATOM   5675 C CE  . LYS E 5 70  ? 5.623  13.613  -36.319 1.00 35.78  ? 69  LYS D CE  1 
ATOM   5676 N NZ  . LYS E 5 70  ? 6.621  14.668  -35.978 1.00 44.89  ? 69  LYS D NZ  1 
ATOM   5677 N N   . ALA E 5 71  ? 0.831  12.959  -40.082 1.00 36.73  ? 70  ALA D N   1 
ATOM   5678 C CA  . ALA E 5 71  ? -0.506 12.808  -39.526 1.00 37.15  ? 70  ALA D CA  1 
ATOM   5679 C C   . ALA E 5 71  ? -1.157 11.521  -40.013 1.00 34.47  ? 70  ALA D C   1 
ATOM   5680 O O   . ALA E 5 71  ? -1.911 10.889  -39.269 1.00 39.12  ? 70  ALA D O   1 
ATOM   5681 C CB  . ALA E 5 71  ? -1.367 14.027  -39.879 1.00 38.46  ? 70  ALA D CB  1 
ATOM   5682 N N   . ALA E 5 72  ? -0.867 11.114  -41.249 1.00 37.19  ? 71  ALA D N   1 
ATOM   5683 C CA  . ALA E 5 72  ? -1.403 9.869   -41.783 1.00 36.74  ? 71  ALA D CA  1 
ATOM   5684 C C   . ALA E 5 72  ? -0.647 8.642   -41.282 1.00 38.60  ? 71  ALA D C   1 
ATOM   5685 O O   . ALA E 5 72  ? -1.168 7.523   -41.390 1.00 36.63  ? 71  ALA D O   1 
ATOM   5686 C CB  . ALA E 5 72  ? -1.376 9.904   -43.316 1.00 31.32  ? 71  ALA D CB  1 
ATOM   5687 N N   . LYS E 5 73  ? 0.552  8.826   -40.723 1.00 36.83  ? 72  LYS D N   1 
ATOM   5688 C CA  . LYS E 5 73  ? 1.442  7.713   -40.380 1.00 34.62  ? 72  LYS D CA  1 
ATOM   5689 C C   . LYS E 5 73  ? 1.658  6.818   -41.608 1.00 34.04  ? 72  LYS D C   1 
ATOM   5690 O O   . LYS E 5 73  ? 1.469  5.600   -41.583 1.00 31.58  ? 72  LYS D O   1 
ATOM   5691 C CB  . LYS E 5 73  ? 0.904  6.936   -39.175 1.00 29.80  ? 72  LYS D CB  1 
ATOM   5692 C CG  . LYS E 5 73  ? 0.883  7.785   -37.879 1.00 29.36  ? 72  LYS D CG  1 
ATOM   5693 C CD  . LYS E 5 73  ? 0.709  6.924   -36.616 1.00 31.98  ? 72  LYS D CD  1 
ATOM   5694 C CE  . LYS E 5 73  ? 1.001  7.722   -35.349 1.00 32.65  ? 72  LYS D CE  1 
ATOM   5695 N NZ  . LYS E 5 73  ? -0.153 8.558   -34.897 1.00 32.03  ? 72  LYS D NZ  1 
ATOM   5696 N N   . SER E 5 74  ? 2.131  7.472   -42.669 1.00 29.33  ? 73  SER D N   1 
ATOM   5697 C CA  . SER E 5 74  ? 2.482  6.806   -43.946 1.00 31.56  ? 73  SER D CA  1 
ATOM   5698 C C   . SER E 5 74  ? 3.846  7.345   -44.387 1.00 28.66  ? 73  SER D C   1 
ATOM   5699 O O   . SER E 5 74  ? 4.000  8.581   -44.439 1.00 32.92  ? 73  SER D O   1 
ATOM   5700 C CB  . SER E 5 74  ? 1.425  7.050   -44.991 1.00 29.02  ? 73  SER D CB  1 
ATOM   5701 O OG  . SER E 5 74  ? 1.961  6.890   -46.297 1.00 28.66  ? 73  SER D OG  1 
ATOM   5702 N N   . VAL E 5 75  ? 4.791  6.454   -44.691 1.00 26.66  ? 74  VAL D N   1 
ATOM   5703 C CA  . VAL E 5 75  ? 6.147  6.883   -45.146 1.00 27.25  ? 74  VAL D CA  1 
ATOM   5704 C C   . VAL E 5 75  ? 6.526  6.039   -46.367 1.00 31.97  ? 74  VAL D C   1 
ATOM   5705 O O   . VAL E 5 75  ? 7.450  5.210   -46.244 1.00 30.71  ? 74  VAL D O   1 
ATOM   5706 C CB  . VAL E 5 75  ? 7.190  6.746   -44.021 1.00 32.47  ? 74  VAL D CB  1 
ATOM   5707 C CG1 . VAL E 5 75  ? 7.118  5.384   -43.347 1.00 25.48  ? 74  VAL D CG1 1 
ATOM   5708 C CG2 . VAL E 5 75  ? 8.599  7.024   -44.521 1.00 31.62  ? 74  VAL D CG2 1 
ATOM   5709 N N   . ALA E 5 76  ? 5.838  6.245   -47.495 1.00 27.87  ? 75  ALA D N   1 
ATOM   5710 C CA  . ALA E 5 76  ? 6.133  5.457   -48.682 1.00 28.49  ? 75  ALA D CA  1 
ATOM   5711 C C   . ALA E 5 76  ? 7.541  5.731   -49.191 1.00 31.64  ? 75  ALA D C   1 
ATOM   5712 O O   . ALA E 5 76  ? 8.023  6.864   -49.155 1.00 30.29  ? 75  ALA D O   1 
ATOM   5713 C CB  . ALA E 5 76  ? 5.117  5.757   -49.791 1.00 29.69  ? 75  ALA D CB  1 
ATOM   5714 N N   . LEU E 5 77  ? 8.193  4.679   -49.679 1.00 31.17  ? 76  LEU D N   1 
ATOM   5715 C CA  . LEU E 5 77  ? 9.492  4.776   -50.329 1.00 28.84  ? 76  LEU D CA  1 
ATOM   5716 C C   . LEU E 5 77  ? 9.291  4.779   -51.839 1.00 32.89  ? 76  LEU D C   1 
ATOM   5717 O O   . LEU E 5 77  ? 8.532  3.957   -52.374 1.00 29.69  ? 76  LEU D O   1 
ATOM   5718 C CB  . LEU E 5 77  ? 10.394 3.610   -49.930 1.00 27.15  ? 76  LEU D CB  1 
ATOM   5719 C CG  . LEU E 5 77  ? 11.586 3.325   -50.858 1.00 30.35  ? 76  LEU D CG  1 
ATOM   5720 C CD1 . LEU E 5 77  ? 12.599 4.445   -50.783 1.00 32.11  ? 76  LEU D CD1 1 
ATOM   5721 C CD2 . LEU E 5 77  ? 12.263 1.969   -50.605 1.00 29.03  ? 76  LEU D CD2 1 
ATOM   5722 N N   . THR E 5 78  ? 9.986  5.683   -52.524 1.00 30.29  ? 77  THR D N   1 
ATOM   5723 C CA  . THR E 5 78  ? 9.944  5.770   -53.977 1.00 33.33  ? 77  THR D CA  1 
ATOM   5724 C C   . THR E 5 78  ? 11.328 5.499   -54.537 1.00 32.88  ? 77  THR D C   1 
ATOM   5725 O O   . THR E 5 78  ? 12.297 6.151   -54.137 1.00 33.55  ? 77  THR D O   1 
ATOM   5726 C CB  . THR E 5 78  ? 9.471  7.147   -54.442 1.00 33.58  ? 77  THR D CB  1 
ATOM   5727 O OG1 . THR E 5 78  ? 8.134  7.371   -53.984 1.00 32.51  ? 77  THR D OG1 1 
ATOM   5728 C CG2 . THR E 5 78  ? 9.527  7.228   -55.965 1.00 33.51  ? 77  THR D CG2 1 
ATOM   5729 N N   . ILE E 5 79  ? 11.420 4.532   -55.447 1.00 31.15  ? 78  ILE D N   1 
ATOM   5730 C CA  . ILE E 5 79  ? 12.650 4.239   -56.176 1.00 32.21  ? 78  ILE D CA  1 
ATOM   5731 C C   . ILE E 5 79  ? 12.477 4.718   -57.611 1.00 35.01  ? 78  ILE D C   1 
ATOM   5732 O O   . ILE E 5 79  ? 11.518 4.329   -58.289 1.00 34.21  ? 78  ILE D O   1 
ATOM   5733 C CB  . ILE E 5 79  ? 12.994 2.741   -56.146 1.00 33.70  ? 78  ILE D CB  1 
ATOM   5734 C CG1 . ILE E 5 79  ? 12.789 2.168   -54.739 1.00 30.42  ? 78  ILE D CG1 1 
ATOM   5735 C CG2 . ILE E 5 79  ? 14.410 2.522   -56.651 1.00 30.45  ? 78  ILE D CG2 1 
ATOM   5736 C CD1 . ILE E 5 79  ? 12.876 0.636   -54.664 1.00 26.88  ? 78  ILE D CD1 1 
ATOM   5737 N N   . SER E 5 80  ? 13.406 5.555   -58.064 1.00 35.65  ? 79  SER D N   1 
ATOM   5738 C CA  . SER E 5 80  ? 13.413 6.155   -59.393 1.00 43.09  ? 79  SER D CA  1 
ATOM   5739 C C   . SER E 5 80  ? 14.269 5.338   -60.351 1.00 38.22  ? 79  SER D C   1 
ATOM   5740 O O   . SER E 5 80  ? 15.252 4.713   -59.946 1.00 39.24  ? 79  SER D O   1 
ATOM   5741 C CB  . SER E 5 80  ? 13.969 7.580   -59.330 1.00 35.71  ? 79  SER D CB  1 
ATOM   5742 O OG  . SER E 5 80  ? 12.923 8.515   -59.177 1.00 51.48  ? 79  SER D OG  1 
ATOM   5743 N N   . ALA E 5 81  ? 13.914 5.391   -61.634 1.00 41.29  ? 80  ALA D N   1 
ATOM   5744 C CA  . ALA E 5 81  ? 14.739 4.843   -62.721 1.00 41.74  ? 80  ALA D CA  1 
ATOM   5745 C C   . ALA E 5 81  ? 15.195 3.419   -62.401 1.00 38.38  ? 80  ALA D C   1 
ATOM   5746 O O   . ALA E 5 81  ? 16.386 3.123   -62.273 1.00 37.25  ? 80  ALA D O   1 
ATOM   5747 C CB  . ALA E 5 81  ? 15.939 5.749   -63.011 1.00 32.28  ? 80  ALA D CB  1 
ATOM   5748 N N   . LEU E 5 82  ? 14.205 2.542   -62.268 1.00 34.47  ? 81  LEU D N   1 
ATOM   5749 C CA  . LEU E 5 82  ? 14.448 1.177   -61.832 1.00 35.39  ? 81  LEU D CA  1 
ATOM   5750 C C   . LEU E 5 82  ? 15.482 0.480   -62.698 1.00 33.77  ? 81  LEU D C   1 
ATOM   5751 O O   . LEU E 5 82  ? 15.463 0.578   -63.929 1.00 36.78  ? 81  LEU D O   1 
ATOM   5752 C CB  . LEU E 5 82  ? 13.149 0.382   -61.852 1.00 32.61  ? 81  LEU D CB  1 
ATOM   5753 C CG  . LEU E 5 82  ? 12.187 0.738   -60.734 1.00 37.53  ? 81  LEU D CG  1 
ATOM   5754 C CD1 . LEU E 5 82  ? 10.858 0.072   -61.033 1.00 37.48  ? 81  LEU D CD1 1 
ATOM   5755 C CD2 . LEU E 5 82  ? 12.759 0.313   -59.353 1.00 33.08  ? 81  LEU D CD2 1 
ATOM   5756 N N   . GLN E 5 83  ? 16.390 -0.227  -62.033 1.00 37.23  ? 82  GLN D N   1 
ATOM   5757 C CA  . GLN E 5 83  ? 17.324 -1.157  -62.648 1.00 36.27  ? 82  GLN D CA  1 
ATOM   5758 C C   . GLN E 5 83  ? 16.960 -2.574  -62.225 1.00 36.00  ? 82  GLN D C   1 
ATOM   5759 O O   . GLN E 5 83  ? 16.257 -2.785  -61.229 1.00 33.65  ? 82  GLN D O   1 
ATOM   5760 C CB  . GLN E 5 83  ? 18.765 -0.835  -62.241 1.00 35.62  ? 82  GLN D CB  1 
ATOM   5761 C CG  . GLN E 5 83  ? 19.173 0.607   -62.481 1.00 39.79  ? 82  GLN D CG  1 
ATOM   5762 C CD  . GLN E 5 83  ? 20.234 1.068   -61.494 1.00 45.20  ? 82  GLN D CD  1 
ATOM   5763 O OE1 . GLN E 5 83  ? 20.932 0.251   -60.907 1.00 43.78  ? 82  GLN D OE1 1 
ATOM   5764 N NE2 . GLN E 5 83  ? 20.358 2.379   -61.310 1.00 43.16  ? 82  GLN D NE2 1 
ATOM   5765 N N   . LEU E 5 84  ? 17.435 -3.550  -63.002 1.00 36.98  ? 83  LEU D N   1 
ATOM   5766 C CA  . LEU E 5 84  ? 17.166 -4.950  -62.677 1.00 38.99  ? 83  LEU D CA  1 
ATOM   5767 C C   . LEU E 5 84  ? 17.672 -5.319  -61.284 1.00 36.53  ? 83  LEU D C   1 
ATOM   5768 O O   . LEU E 5 84  ? 17.065 -6.162  -60.608 1.00 37.80  ? 83  LEU D O   1 
ATOM   5769 C CB  . LEU E 5 84  ? 17.807 -5.867  -63.715 1.00 36.59  ? 83  LEU D CB  1 
ATOM   5770 C CG  . LEU E 5 84  ? 17.196 -5.912  -65.113 1.00 38.27  ? 83  LEU D CG  1 
ATOM   5771 C CD1 . LEU E 5 84  ? 17.937 -6.941  -65.968 1.00 34.10  ? 83  LEU D CD1 1 
ATOM   5772 C CD2 . LEU E 5 84  ? 15.701 -6.202  -65.038 1.00 32.43  ? 83  LEU D CD2 1 
ATOM   5773 N N   . GLU E 5 85  ? 18.779 -4.712  -60.845 1.00 35.28  ? 84  GLU D N   1 
ATOM   5774 C CA  . GLU E 5 85  ? 19.334 -4.986  -59.524 1.00 40.15  ? 84  GLU D CA  1 
ATOM   5775 C C   . GLU E 5 85  ? 18.466 -4.442  -58.395 1.00 35.92  ? 84  GLU D C   1 
ATOM   5776 O O   . GLU E 5 85  ? 18.761 -4.704  -57.226 1.00 38.12  ? 84  GLU D O   1 
ATOM   5777 C CB  . GLU E 5 85  ? 20.752 -4.407  -59.410 1.00 39.12  ? 84  GLU D CB  1 
ATOM   5778 C CG  . GLU E 5 85  ? 21.816 -5.130  -60.239 1.00 45.89  ? 84  GLU D CG  1 
ATOM   5779 C CD  . GLU E 5 85  ? 21.630 -4.949  -61.755 1.00 57.48  ? 84  GLU D CD  1 
ATOM   5780 O OE1 . GLU E 5 85  ? 21.287 -3.821  -62.198 1.00 51.21  ? 84  GLU D OE1 1 
ATOM   5781 O OE2 . GLU E 5 85  ? 21.821 -5.938  -62.502 1.00 55.37  ? 84  GLU D OE2 1 
ATOM   5782 N N   . ASP E 5 86  ? 17.421 -3.681  -58.704 1.00 36.33  ? 85  ASP D N   1 
ATOM   5783 C CA  . ASP E 5 86  ? 16.502 -3.251  -57.659 1.00 33.07  ? 85  ASP D CA  1 
ATOM   5784 C C   . ASP E 5 86  ? 15.514 -4.341  -57.262 1.00 32.28  ? 85  ASP D C   1 
ATOM   5785 O O   . ASP E 5 86  ? 14.791 -4.157  -56.280 1.00 36.80  ? 85  ASP D O   1 
ATOM   5786 C CB  . ASP E 5 86  ? 15.741 -1.987  -58.101 1.00 34.39  ? 85  ASP D CB  1 
ATOM   5787 C CG  . ASP E 5 86  ? 16.652 -0.771  -58.278 1.00 33.89  ? 85  ASP D CG  1 
ATOM   5788 O OD1 . ASP E 5 86  ? 17.663 -0.651  -57.561 1.00 36.23  ? 85  ASP D OD1 1 
ATOM   5789 O OD2 . ASP E 5 86  ? 16.356 0.076   -59.145 1.00 35.80  ? 85  ASP D OD2 1 
ATOM   5790 N N   . SER E 5 87  ? 15.444 -5.458  -57.995 1.00 34.37  ? 86  SER D N   1 
ATOM   5791 C CA  . SER E 5 87  ? 14.571 -6.559  -57.588 1.00 32.96  ? 86  SER D CA  1 
ATOM   5792 C C   . SER E 5 87  ? 15.045 -7.117  -56.252 1.00 32.36  ? 86  SER D C   1 
ATOM   5793 O O   . SER E 5 87  ? 16.159 -7.639  -56.147 1.00 30.29  ? 86  SER D O   1 
ATOM   5794 C CB  . SER E 5 87  ? 14.542 -7.677  -58.646 1.00 35.69  ? 86  SER D CB  1 
ATOM   5795 O OG  . SER E 5 87  ? 13.991 -7.260  -59.896 1.00 34.16  ? 86  SER D OG  1 
ATOM   5796 N N   . ALA E 5 88  ? 14.193 -7.009  -55.239 1.00 32.54  ? 87  ALA D N   1 
ATOM   5797 C CA  . ALA E 5 88  ? 14.497 -7.443  -53.879 1.00 33.29  ? 87  ALA D CA  1 
ATOM   5798 C C   . ALA E 5 88  ? 13.192 -7.437  -53.097 1.00 30.44  ? 87  ALA D C   1 
ATOM   5799 O O   . ALA E 5 88  ? 12.122 -7.138  -53.635 1.00 29.14  ? 87  ALA D O   1 
ATOM   5800 C CB  . ALA E 5 88  ? 15.545 -6.540  -53.218 1.00 30.83  ? 87  ALA D CB  1 
ATOM   5801 N N   . LYS E 5 89  ? 13.281 -7.771  -51.819 1.00 29.46  ? 88  LYS D N   1 
ATOM   5802 C CA  . LYS E 5 89  ? 12.170 -7.568  -50.902 1.00 29.07  ? 88  LYS D CA  1 
ATOM   5803 C C   . LYS E 5 89  ? 12.526 -6.374  -50.021 1.00 30.21  ? 88  LYS D C   1 
ATOM   5804 O O   . LYS E 5 89  ? 13.591 -6.355  -49.393 1.00 26.84  ? 88  LYS D O   1 
ATOM   5805 C CB  . LYS E 5 89  ? 11.890 -8.824  -50.080 1.00 26.78  ? 88  LYS D CB  1 
ATOM   5806 C CG  . LYS E 5 89  ? 10.602 -8.773  -49.291 1.00 29.63  ? 88  LYS D CG  1 
ATOM   5807 C CD  . LYS E 5 89  ? 10.228 -10.140 -48.740 1.00 27.40  ? 88  LYS D CD  1 
ATOM   5808 C CE  . LYS E 5 89  ? 8.953  -10.051 -47.935 1.00 27.00  ? 88  LYS D CE  1 
ATOM   5809 N NZ  . LYS E 5 89  ? 8.505  -11.366 -47.414 1.00 26.78  ? 88  LYS D NZ  1 
ATOM   5810 N N   . TYR E 5 90  ? 11.657 -5.368  -50.006 1.00 28.89  ? 89  TYR D N   1 
ATOM   5811 C CA  . TYR E 5 90  ? 11.922 -4.120  -49.303 1.00 27.86  ? 89  TYR D CA  1 
ATOM   5812 C C   . TYR E 5 90  ? 11.149 -4.113  -47.994 1.00 27.70  ? 89  TYR D C   1 
ATOM   5813 O O   . TYR E 5 90  ? 9.956  -4.433  -47.964 1.00 27.63  ? 89  TYR D O   1 
ATOM   5814 C CB  . TYR E 5 90  ? 11.551 -2.905  -50.171 1.00 25.56  ? 89  TYR D CB  1 
ATOM   5815 C CG  . TYR E 5 90  ? 12.495 -2.738  -51.345 1.00 27.62  ? 89  TYR D CG  1 
ATOM   5816 C CD1 . TYR E 5 90  ? 12.391 -3.558  -52.469 1.00 24.99  ? 89  TYR D CD1 1 
ATOM   5817 C CD2 . TYR E 5 90  ? 13.523 -1.808  -51.303 1.00 24.30  ? 89  TYR D CD2 1 
ATOM   5818 C CE1 . TYR E 5 90  ? 13.271 -3.425  -53.538 1.00 28.22  ? 89  TYR D CE1 1 
ATOM   5819 C CE2 . TYR E 5 90  ? 14.407 -1.672  -52.354 1.00 23.67  ? 89  TYR D CE2 1 
ATOM   5820 C CZ  . TYR E 5 90  ? 14.281 -2.481  -53.480 1.00 31.54  ? 89  TYR D CZ  1 
ATOM   5821 O OH  . TYR E 5 90  ? 15.174 -2.342  -54.539 1.00 24.99  ? 89  TYR D OH  1 
ATOM   5822 N N   . PHE E 5 91  ? 11.830 -3.754  -46.918 1.00 26.17  ? 90  PHE D N   1 
ATOM   5823 C CA  . PHE E 5 91  ? 11.246 -3.762  -45.587 1.00 24.85  ? 90  PHE D CA  1 
ATOM   5824 C C   . PHE E 5 91  ? 11.180 -2.349  -45.042 1.00 26.45  ? 90  PHE D C   1 
ATOM   5825 O O   . PHE E 5 91  ? 12.132 -1.571  -45.188 1.00 24.73  ? 90  PHE D O   1 
ATOM   5826 C CB  . PHE E 5 91  ? 12.063 -4.628  -44.634 1.00 24.92  ? 90  PHE D CB  1 
ATOM   5827 C CG  . PHE E 5 91  ? 11.999 -6.086  -44.949 1.00 26.73  ? 90  PHE D CG  1 
ATOM   5828 C CD1 . PHE E 5 91  ? 10.968 -6.867  -44.444 1.00 23.95  ? 90  PHE D CD1 1 
ATOM   5829 C CD2 . PHE E 5 91  ? 12.974 -6.682  -45.746 1.00 24.32  ? 90  PHE D CD2 1 
ATOM   5830 C CE1 . PHE E 5 91  ? 10.898 -8.221  -44.739 1.00 25.75  ? 90  PHE D CE1 1 
ATOM   5831 C CE2 . PHE E 5 91  ? 12.913 -8.034  -46.039 1.00 24.30  ? 90  PHE D CE2 1 
ATOM   5832 C CZ  . PHE E 5 91  ? 11.873 -8.802  -45.543 1.00 20.95  ? 90  PHE D CZ  1 
ATOM   5833 N N   . CYS E 5 92  ? 10.053 -2.040  -44.404 1.00 27.30  ? 91  CYS D N   1 
ATOM   5834 C CA  . CYS E 5 92  ? 9.825  -0.789  -43.707 1.00 26.95  ? 91  CYS D CA  1 
ATOM   5835 C C   . CYS E 5 92  ? 9.891  -1.041  -42.203 1.00 27.56  ? 91  CYS D C   1 
ATOM   5836 O O   . CYS E 5 92  ? 9.351  -2.038  -41.715 1.00 27.28  ? 91  CYS D O   1 
ATOM   5837 C CB  . CYS E 5 92  ? 8.457  -0.222  -44.101 1.00 27.58  ? 91  CYS D CB  1 
ATOM   5838 S SG  . CYS E 5 92  ? 8.016  1.346   -43.357 1.00 32.98  ? 91  CYS D SG  1 
ATOM   5839 N N   . ALA E 5 93  ? 10.540 -0.140  -41.460 1.00 24.74  ? 92  ALA D N   1 
ATOM   5840 C CA  . ALA E 5 93  ? 10.701 -0.360  -40.030 1.00 27.27  ? 92  ALA D CA  1 
ATOM   5841 C C   . ALA E 5 93  ? 10.624 0.943   -39.237 1.00 25.85  ? 92  ALA D C   1 
ATOM   5842 O O   . ALA E 5 93  ? 10.947 2.027   -39.724 1.00 26.81  ? 92  ALA D O   1 
ATOM   5843 C CB  . ALA E 5 93  ? 12.029 -1.074  -39.728 1.00 26.06  ? 92  ALA D CB  1 
ATOM   5844 N N   . LEU E 5 94  ? 10.229 0.797   -37.986 1.00 27.64  ? 93  LEU D N   1 
ATOM   5845 C CA  . LEU E 5 94  ? 10.054 1.882   -37.039 1.00 27.84  ? 93  LEU D CA  1 
ATOM   5846 C C   . LEU E 5 94  ? 11.075 1.716   -35.917 1.00 29.82  ? 93  LEU D C   1 
ATOM   5847 O O   . LEU E 5 94  ? 11.319 0.593   -35.461 1.00 27.77  ? 93  LEU D O   1 
ATOM   5848 C CB  . LEU E 5 94  ? 8.628  1.835   -36.491 1.00 27.27  ? 93  LEU D CB  1 
ATOM   5849 C CG  . LEU E 5 94  ? 7.920  3.035   -35.884 1.00 33.30  ? 93  LEU D CG  1 
ATOM   5850 C CD1 . LEU E 5 94  ? 8.320  4.317   -36.581 1.00 32.29  ? 93  LEU D CD1 1 
ATOM   5851 C CD2 . LEU E 5 94  ? 6.442  2.799   -36.000 1.00 29.50  ? 93  LEU D CD2 1 
ATOM   5852 N N   . GLY E 5 95  ? 11.695 2.815   -35.501 1.00 27.61  ? 94  GLY D N   1 
ATOM   5853 C CA  . GLY E 5 95  ? 12.662 2.780   -34.413 1.00 26.26  ? 94  GLY D CA  1 
ATOM   5854 C C   . GLY E 5 95  ? 12.481 3.963   -33.479 1.00 30.88  ? 94  GLY D C   1 
ATOM   5855 O O   . GLY E 5 95  ? 12.149 5.072   -33.909 1.00 29.39  ? 94  GLY D O   1 
ATOM   5856 N N   . ASP E 5 96  ? 12.709 3.719   -32.178 1.00 27.60  ? 95  ASP D N   1 
ATOM   5857 C CA  . ASP E 5 96  ? 12.524 4.750   -31.163 1.00 26.76  ? 95  ASP D CA  1 
ATOM   5858 C C   . ASP E 5 96  ? 13.867 5.441   -30.853 1.00 27.28  ? 95  ASP D C   1 
ATOM   5859 O O   . ASP E 5 96  ? 14.835 5.334   -31.611 1.00 24.86  ? 95  ASP D O   1 
ATOM   5860 C CB  . ASP E 5 96  ? 11.828 4.138   -29.936 1.00 23.82  ? 95  ASP D CB  1 
ATOM   5861 C CG  . ASP E 5 96  ? 12.751 3.248   -29.084 1.00 26.93  ? 95  ASP D CG  1 
ATOM   5862 O OD1 . ASP E 5 96  ? 13.931 3.033   -29.440 1.00 24.75  ? 95  ASP D OD1 1 
ATOM   5863 O OD2 . ASP E 5 96  ? 12.276 2.744   -28.042 1.00 26.94  ? 95  ASP D OD2 1 
ATOM   5864 N N   . THR E 5 97  ? 13.945 6.162   -29.731 1.00 24.94  ? 96  THR D N   1 
ATOM   5865 C CA  . THR E 5 97  ? 15.155 6.930   -29.434 1.00 26.95  ? 96  THR D CA  1 
ATOM   5866 C C   . THR E 5 97  ? 16.137 6.167   -28.560 1.00 26.64  ? 96  THR D C   1 
ATOM   5867 O O   . THR E 5 97  ? 17.063 6.775   -28.011 1.00 30.62  ? 96  THR D O   1 
ATOM   5868 C CB  . THR E 5 97  ? 14.805 8.266   -28.763 1.00 30.18  ? 96  THR D CB  1 
ATOM   5869 O OG1 . THR E 5 97  ? 14.252 8.029   -27.463 1.00 25.87  ? 96  THR D OG1 1 
ATOM   5870 C CG2 . THR E 5 97  ? 13.811 9.067   -29.621 1.00 31.74  ? 96  THR D CG2 1 
ATOM   5871 N N   . ALA E 5 98  ? 15.954 4.856   -28.415 1.00 25.70  ? 97  ALA D N   1 
ATOM   5872 C CA  . ALA E 5 98  ? 16.757 4.072   -27.487 1.00 32.48  ? 97  ALA D CA  1 
ATOM   5873 C C   . ALA E 5 98  ? 16.896 2.642   -27.989 1.00 27.30  ? 97  ALA D C   1 
ATOM   5874 O O   . ALA E 5 98  ? 16.738 1.686   -27.225 1.00 27.92  ? 97  ALA D O   1 
ATOM   5875 C CB  . ALA E 5 98  ? 16.161 4.087   -26.075 1.00 26.86  ? 97  ALA D CB  1 
ATOM   5876 N N   . GLY E 5 99  ? 17.154 2.484   -29.286 1.00 26.59  ? 98  GLY D N   1 
ATOM   5877 C CA  . GLY E 5 99  ? 17.593 1.222   -29.856 1.00 23.67  ? 98  GLY D CA  1 
ATOM   5878 C C   . GLY E 5 99  ? 16.515 0.224   -30.232 1.00 22.89  ? 98  GLY D C   1 
ATOM   5879 O O   . GLY E 5 99  ? 16.835 -0.796  -30.855 1.00 24.80  ? 98  GLY D O   1 
ATOM   5880 N N   . LYS E 5 100 ? 15.262 0.457   -29.875 1.00 25.03  ? 99  LYS D N   1 
ATOM   5881 C CA  . LYS E 5 100 ? 14.216 -0.510  -30.163 1.00 25.10  ? 99  LYS D CA  1 
ATOM   5882 C C   . LYS E 5 100 ? 13.709 -0.315  -31.589 1.00 27.04  ? 99  LYS D C   1 
ATOM   5883 O O   . LYS E 5 100 ? 13.724 0.800   -32.120 1.00 27.18  ? 99  LYS D O   1 
ATOM   5884 C CB  . LYS E 5 100 ? 13.075 -0.374  -29.153 1.00 25.67  ? 99  LYS D CB  1 
ATOM   5885 C CG  . LYS E 5 100 ? 12.187 -1.605  -29.026 1.00 28.84  ? 99  LYS D CG  1 
ATOM   5886 C CD  . LYS E 5 100 ? 10.980 -1.360  -28.107 1.00 34.38  ? 99  LYS D CD  1 
ATOM   5887 C CE  . LYS E 5 100 ? 10.278 -2.681  -27.715 1.00 35.02  ? 99  LYS D CE  1 
ATOM   5888 N NZ  . LYS E 5 100 ? 10.855 -3.882  -28.409 1.00 36.16  ? 99  LYS D NZ  1 
ATOM   5889 N N   . SER E 5 101 ? 13.290 -1.416  -32.222 1.00 25.30  ? 100 SER D N   1 
ATOM   5890 C CA  . SER E 5 101 ? 12.759 -1.352  -33.583 1.00 26.09  ? 100 SER D CA  1 
ATOM   5891 C C   . SER E 5 101 ? 11.647 -2.374  -33.810 1.00 26.49  ? 100 SER D C   1 
ATOM   5892 O O   . SER E 5 101 ? 11.602 -3.427  -33.169 1.00 27.45  ? 100 SER D O   1 
ATOM   5893 C CB  . SER E 5 101 ? 13.851 -1.571  -34.633 1.00 29.24  ? 100 SER D CB  1 
ATOM   5894 O OG  . SER E 5 101 ? 14.208 -2.932  -34.696 1.00 34.60  ? 100 SER D OG  1 
ATOM   5895 N N   . THR E 5 102 ? 10.752 -2.035  -34.747 1.00 25.75  ? 101 THR D N   1 
ATOM   5896 C CA  . THR E 5 102 ? 9.612  -2.852  -35.162 1.00 29.97  ? 101 THR D CA  1 
ATOM   5897 C C   . THR E 5 102 ? 9.616  -2.909  -36.687 1.00 27.86  ? 101 THR D C   1 
ATOM   5898 O O   . THR E 5 102 ? 9.565  -1.862  -37.334 1.00 26.17  ? 101 THR D O   1 
ATOM   5899 C CB  . THR E 5 102 ? 8.273  -2.254  -34.678 1.00 31.46  ? 101 THR D CB  1 
ATOM   5900 O OG1 . THR E 5 102 ? 8.275  -2.067  -33.259 1.00 29.82  ? 101 THR D OG1 1 
ATOM   5901 C CG2 . THR E 5 102 ? 7.098  -3.169  -35.048 1.00 31.61  ? 101 THR D CG2 1 
ATOM   5902 N N   . PHE E 5 103 ? 9.667  -4.120  -37.262 1.00 27.88  ? 102 PHE D N   1 
ATOM   5903 C CA  . PHE E 5 103 ? 9.690  -4.307  -38.716 1.00 27.60  ? 102 PHE D CA  1 
ATOM   5904 C C   . PHE E 5 103 ? 8.303  -4.605  -39.272 1.00 27.24  ? 102 PHE D C   1 
ATOM   5905 O O   . PHE E 5 103 ? 7.505  -5.320  -38.649 1.00 25.80  ? 102 PHE D O   1 
ATOM   5906 C CB  . PHE E 5 103 ? 10.611 -5.461  -39.134 1.00 27.08  ? 102 PHE D CB  1 
ATOM   5907 C CG  . PHE E 5 103 ? 12.031 -5.052  -39.438 1.00 25.19  ? 102 PHE D CG  1 
ATOM   5908 C CD1 . PHE E 5 103 ? 12.850 -4.558  -38.442 1.00 22.79  ? 102 PHE D CD1 1 
ATOM   5909 C CD2 . PHE E 5 103 ? 12.556 -5.209  -40.712 1.00 27.53  ? 102 PHE D CD2 1 
ATOM   5910 C CE1 . PHE E 5 103 ? 14.159 -4.195  -38.704 1.00 22.03  ? 102 PHE D CE1 1 
ATOM   5911 C CE2 . PHE E 5 103 ? 13.875 -4.861  -40.986 1.00 25.23  ? 102 PHE D CE2 1 
ATOM   5912 C CZ  . PHE E 5 103 ? 14.677 -4.351  -39.968 1.00 27.65  ? 102 PHE D CZ  1 
ATOM   5913 N N   . GLY E 5 104 ? 8.040  -4.090  -40.474 1.00 27.46  ? 103 GLY D N   1 
ATOM   5914 C CA  . GLY E 5 104 ? 6.977  -4.623  -41.298 1.00 28.73  ? 103 GLY D CA  1 
ATOM   5915 C C   . GLY E 5 104 ? 7.401  -5.933  -41.938 1.00 28.44  ? 103 GLY D C   1 
ATOM   5916 O O   . GLY E 5 104 ? 8.551  -6.364  -41.842 1.00 25.99  ? 103 GLY D O   1 
ATOM   5917 N N   . ASP E 5 105 ? 6.458  -6.574  -42.625 1.00 28.09  ? 104 ASP D N   1 
ATOM   5918 C CA  . ASP E 5 105 ? 6.714  -7.896  -43.177 1.00 28.03  ? 104 ASP D CA  1 
ATOM   5919 C C   . ASP E 5 105 ? 7.132  -7.872  -44.644 1.00 29.39  ? 104 ASP D C   1 
ATOM   5920 O O   . ASP E 5 105 ? 7.347  -8.940  -45.224 1.00 30.77  ? 104 ASP D O   1 
ATOM   5921 C CB  . ASP E 5 105 ? 5.502  -8.804  -42.955 1.00 27.18  ? 104 ASP D CB  1 
ATOM   5922 C CG  . ASP E 5 105 ? 5.418  -9.314  -41.505 1.00 35.83  ? 104 ASP D CG  1 
ATOM   5923 O OD1 . ASP E 5 105 ? 6.478  -9.519  -40.847 1.00 30.71  ? 104 ASP D OD1 1 
ATOM   5924 O OD2 . ASP E 5 105 ? 4.289  -9.508  -41.014 1.00 38.49  ? 104 ASP D OD2 1 
ATOM   5925 N N   . GLY E 5 106 ? 7.299  -6.699  -45.242 1.00 26.41  ? 105 GLY D N   1 
ATOM   5926 C CA  . GLY E 5 106 ? 8.047  -6.623  -46.489 1.00 25.81  ? 105 GLY D CA  1 
ATOM   5927 C C   . GLY E 5 106 ? 7.177  -6.574  -47.742 1.00 28.41  ? 105 GLY D C   1 
ATOM   5928 O O   . GLY E 5 106 ? 6.030  -7.041  -47.765 1.00 26.75  ? 105 GLY D O   1 
ATOM   5929 N N   . THR E 5 107 ? 7.741  -6.006  -48.811 1.00 25.52  ? 106 THR D N   1 
ATOM   5930 C CA  . THR E 5 107 ? 7.138  -6.014  -50.143 1.00 28.09  ? 106 THR D CA  1 
ATOM   5931 C C   . THR E 5 107 ? 8.156  -6.528  -51.146 1.00 29.75  ? 106 THR D C   1 
ATOM   5932 O O   . THR E 5 107 ? 9.275  -6.011  -51.214 1.00 29.04  ? 106 THR D O   1 
ATOM   5933 C CB  . THR E 5 107 ? 6.671  -4.622  -50.589 1.00 28.39  ? 106 THR D CB  1 
ATOM   5934 O OG1 . THR E 5 107 ? 5.632  -4.161  -49.724 1.00 30.15  ? 106 THR D OG1 1 
ATOM   5935 C CG2 . THR E 5 107 ? 6.150  -4.666  -52.046 1.00 31.49  ? 106 THR D CG2 1 
ATOM   5936 N N   . THR E 5 108 ? 7.761  -7.520  -51.939 1.00 30.71  ? 107 THR D N   1 
ATOM   5937 C CA  . THR E 5 108 ? 8.637  -8.088  -52.958 1.00 33.48  ? 107 THR D CA  1 
ATOM   5938 C C   . THR E 5 108 ? 8.488  -7.305  -54.258 1.00 30.12  ? 107 THR D C   1 
ATOM   5939 O O   . THR E 5 108 ? 7.385  -7.186  -54.797 1.00 27.65  ? 107 THR D O   1 
ATOM   5940 C CB  . THR E 5 108 ? 8.332  -9.566  -53.181 1.00 35.19  ? 107 THR D CB  1 
ATOM   5941 O OG1 . THR E 5 108 ? 8.641  -10.305 -51.982 1.00 30.36  ? 107 THR D OG1 1 
ATOM   5942 C CG2 . THR E 5 108 ? 9.145  -10.098 -54.359 1.00 30.68  ? 107 THR D CG2 1 
ATOM   5943 N N   . LEU E 5 109 ? 9.601  -6.768  -54.751 1.00 27.44  ? 108 LEU D N   1 
ATOM   5944 C CA  . LEU E 5 109 ? 9.623  -5.952  -55.952 1.00 28.98  ? 108 LEU D CA  1 
ATOM   5945 C C   . LEU E 5 109 ? 10.300 -6.738  -57.070 1.00 33.34  ? 108 LEU D C   1 
ATOM   5946 O O   . LEU E 5 109 ? 11.458 -7.150  -56.931 1.00 33.33  ? 108 LEU D O   1 
ATOM   5947 C CB  . LEU E 5 109 ? 10.354 -4.628  -55.706 1.00 27.17  ? 108 LEU D CB  1 
ATOM   5948 C CG  . LEU E 5 109 ? 10.618 -3.848  -57.002 1.00 33.34  ? 108 LEU D CG  1 
ATOM   5949 C CD1 . LEU E 5 109 ? 9.295  -3.363  -57.601 1.00 28.11  ? 108 LEU D CD1 1 
ATOM   5950 C CD2 . LEU E 5 109 ? 11.627 -2.685  -56.836 1.00 31.47  ? 108 LEU D CD2 1 
ATOM   5951 N N   . THR E 5 110 ? 9.591  -6.931  -58.183 1.00 32.22  ? 109 THR D N   1 
ATOM   5952 C CA  . THR E 5 110 ? 10.173 -7.560  -59.366 1.00 30.45  ? 109 THR D CA  1 
ATOM   5953 C C   . THR E 5 110 ? 10.294 -6.505  -60.459 1.00 33.02  ? 109 THR D C   1 
ATOM   5954 O O   . THR E 5 110 ? 9.295  -5.901  -60.865 1.00 34.22  ? 109 THR D O   1 
ATOM   5955 C CB  . THR E 5 110 ? 9.339  -8.754  -59.843 1.00 36.33  ? 109 THR D CB  1 
ATOM   5956 O OG1 . THR E 5 110 ? 9.058  -9.630  -58.737 1.00 37.72  ? 109 THR D OG1 1 
ATOM   5957 C CG2 . THR E 5 110 ? 10.101 -9.543  -60.926 1.00 36.23  ? 109 THR D CG2 1 
ATOM   5958 N N   . VAL E 5 111 ? 11.512 -6.274  -60.919 1.00 32.96  ? 110 VAL D N   1 
ATOM   5959 C CA  . VAL E 5 111 ? 11.778 -5.333  -61.993 1.00 32.88  ? 110 VAL D CA  1 
ATOM   5960 C C   . VAL E 5 111 ? 11.869 -6.132  -63.285 1.00 36.45  ? 110 VAL D C   1 
ATOM   5961 O O   . VAL E 5 111 ? 12.758 -6.976  -63.455 1.00 36.87  ? 110 VAL D O   1 
ATOM   5962 C CB  . VAL E 5 111 ? 13.047 -4.524  -61.726 1.00 35.93  ? 110 VAL D CB  1 
ATOM   5963 C CG1 . VAL E 5 111 ? 13.391 -3.653  -62.938 1.00 31.25  ? 110 VAL D CG1 1 
ATOM   5964 C CG2 . VAL E 5 111 ? 12.849 -3.666  -60.455 1.00 33.07  ? 110 VAL D CG2 1 
ATOM   5965 N N   . LYS E 5 112 ? 10.954 -5.876  -64.182 1.00 36.36  ? 111 LYS D N   1 
ATOM   5966 C CA  . LYS E 5 112 ? 10.818 -6.706  -65.375 1.00 37.89  ? 111 LYS D CA  1 
ATOM   5967 C C   . LYS E 5 112 ? 11.628 -6.112  -66.517 1.00 35.45  ? 111 LYS D C   1 
ATOM   5968 O O   . LYS E 5 112 ? 11.501 -4.916  -66.804 1.00 34.47  ? 111 LYS D O   1 
ATOM   5969 C CB  . LYS E 5 112 ? 9.358  -6.833  -65.786 1.00 38.75  ? 111 LYS D CB  1 
ATOM   5970 C CG  . LYS E 5 112 ? 8.601  -7.911  -65.026 1.00 44.91  ? 111 LYS D CG  1 
ATOM   5971 C CD  . LYS E 5 112 ? 7.168  -8.025  -65.529 1.00 48.13  ? 111 LYS D CD  1 
ATOM   5972 C CE  . LYS E 5 112 ? 6.369  -6.787  -65.157 1.00 47.34  ? 111 LYS D CE  1 
ATOM   5973 N NZ  . LYS E 5 112 ? 5.489  -6.306  -66.236 1.00 47.57  ? 111 LYS D NZ  1 
ATOM   5974 N N   . PRO E 5 113 ? 12.453 -6.911  -67.180 1.00 31.76  ? 112 PRO D N   1 
ATOM   5975 C CA  . PRO E 5 113 ? 13.312 -6.378  -68.231 1.00 34.49  ? 112 PRO D CA  1 
ATOM   5976 C C   . PRO E 5 113 ? 12.522 -6.108  -69.505 1.00 36.50  ? 112 PRO D C   1 
ATOM   5977 O O   . PRO E 5 113 ? 11.432 -6.641  -69.732 1.00 32.75  ? 112 PRO D O   1 
ATOM   5978 C CB  . PRO E 5 113 ? 14.324 -7.503  -68.442 1.00 33.30  ? 112 PRO D CB  1 
ATOM   5979 C CG  . PRO E 5 113 ? 13.506 -8.738  -68.220 1.00 30.14  ? 112 PRO D CG  1 
ATOM   5980 C CD  . PRO E 5 113 ? 12.472 -8.386  -67.156 1.00 32.16  ? 112 PRO D CD  1 
ATOM   5981 N N   . ASN E 5 114 ? 13.110 -5.265  -70.343 1.00 33.78  ? 113 ASN D N   1 
ATOM   5982 C CA  . ASN E 5 114 ? 12.503 -4.857  -71.613 1.00 48.24  ? 113 ASN D CA  1 
ATOM   5983 C C   . ASN E 5 114 ? 12.992 -5.801  -72.712 1.00 40.16  ? 113 ASN D C   1 
ATOM   5984 O O   . ASN E 5 114 ? 14.050 -5.600  -73.306 1.00 42.85  ? 113 ASN D O   1 
ATOM   5985 C CB  . ASN E 5 114 ? 12.855 -3.403  -71.904 1.00 47.95  ? 113 ASN D CB  1 
ATOM   5986 C CG  . ASN E 5 114 ? 12.212 -2.889  -73.162 1.00 56.41  ? 113 ASN D CG  1 
ATOM   5987 O OD1 . ASN E 5 114 ? 11.072 -3.230  -73.474 1.00 54.77  ? 113 ASN D OD1 1 
ATOM   5988 N ND2 . ASN E 5 114 ? 12.944 -2.054  -73.899 1.00 56.63  ? 113 ASN D ND2 1 
ATOM   5989 N N   . ILE E 5 115 ? 12.236 -6.870  -72.957 1.00 35.78  ? 114 ILE D N   1 
ATOM   5990 C CA  . ILE E 5 115 ? 12.630 -7.890  -73.935 1.00 42.92  ? 114 ILE D CA  1 
ATOM   5991 C C   . ILE E 5 115 ? 12.175 -7.401  -75.307 1.00 43.24  ? 114 ILE D C   1 
ATOM   5992 O O   . ILE E 5 115 ? 10.991 -7.496  -75.646 1.00 41.02  ? 114 ILE D O   1 
ATOM   5993 C CB  . ILE E 5 115 ? 12.035 -9.262  -73.608 1.00 38.22  ? 114 ILE D CB  1 
ATOM   5994 C CG1 . ILE E 5 115 ? 12.453 -9.724  -72.210 1.00 37.86  ? 114 ILE D CG1 1 
ATOM   5995 C CG2 . ILE E 5 115 ? 12.430 -10.272 -74.682 1.00 39.34  ? 114 ILE D CG2 1 
ATOM   5996 C CD1 . ILE E 5 115 ? 13.877 -10.236 -72.109 1.00 32.93  ? 114 ILE D CD1 1 
ATOM   5997 N N   . GLN E 5 116 ? 13.096 -6.872  -76.106 1.00 44.22  ? 115 GLN D N   1 
ATOM   5998 C CA  . GLN E 5 116 ? 12.652 -6.200  -77.324 1.00 56.29  ? 115 GLN D CA  1 
ATOM   5999 C C   . GLN E 5 116 ? 12.744 -7.065  -78.575 1.00 52.06  ? 115 GLN D C   1 
ATOM   6000 O O   . GLN E 5 116 ? 12.203 -6.673  -79.612 1.00 51.39  ? 115 GLN D O   1 
ATOM   6001 C CB  . GLN E 5 116 ? 13.419 -4.886  -77.542 1.00 59.17  ? 115 GLN D CB  1 
ATOM   6002 C CG  . GLN E 5 116 ? 12.565 -3.811  -78.237 1.00 62.48  ? 115 GLN D CG  1 
ATOM   6003 C CD  . GLN E 5 116 ? 11.659 -3.054  -77.274 1.00 67.37  ? 115 GLN D CD  1 
ATOM   6004 O OE1 . GLN E 5 116 ? 12.037 -2.003  -76.748 1.00 71.43  ? 115 GLN D OE1 1 
ATOM   6005 N NE2 . GLN E 5 116 ? 10.459 -3.590  -77.034 1.00 61.91  ? 115 GLN D NE2 1 
ATOM   6006 N N   . ASN E 5 117 ? 13.367 -8.242  -78.505 1.00 45.64  ? 116 ASN D N   1 
ATOM   6007 C CA  . ASN E 5 117 ? 13.343 -9.197  -79.611 1.00 48.48  ? 116 ASN D CA  1 
ATOM   6008 C C   . ASN E 5 117 ? 12.925 -10.572 -79.108 1.00 41.97  ? 116 ASN D C   1 
ATOM   6009 O O   . ASN E 5 117 ? 13.718 -11.519 -79.135 1.00 40.80  ? 116 ASN D O   1 
ATOM   6010 C CB  . ASN E 5 117 ? 14.703 -9.261  -80.307 1.00 52.15  ? 116 ASN D CB  1 
ATOM   6011 C CG  . ASN E 5 117 ? 15.080 -7.949  -80.945 1.00 54.36  ? 116 ASN D CG  1 
ATOM   6012 O OD1 . ASN E 5 117 ? 14.301 -7.376  -81.709 1.00 50.91  ? 116 ASN D OD1 1 
ATOM   6013 N ND2 . ASN E 5 117 ? 16.271 -7.451  -80.621 1.00 53.42  ? 116 ASN D ND2 1 
ATOM   6014 N N   . PRO E 5 118 ? 11.674 -10.726 -78.665 1.00 39.27  ? 117 PRO D N   1 
ATOM   6015 C CA  . PRO E 5 118 ? 11.262 -12.014 -78.098 1.00 37.82  ? 117 PRO D CA  1 
ATOM   6016 C C   . PRO E 5 118 ? 11.308 -13.138 -79.124 1.00 43.45  ? 117 PRO D C   1 
ATOM   6017 O O   . PRO E 5 118 ? 11.142 -12.933 -80.333 1.00 43.94  ? 117 PRO D O   1 
ATOM   6018 C CB  . PRO E 5 118 ? 9.831  -11.750 -77.605 1.00 40.44  ? 117 PRO D CB  1 
ATOM   6019 C CG  . PRO E 5 118 ? 9.403  -10.508 -78.287 1.00 39.11  ? 117 PRO D CG  1 
ATOM   6020 C CD  . PRO E 5 118 ? 10.626 -9.704  -78.511 1.00 37.10  ? 117 PRO D CD  1 
ATOM   6021 N N   . ASP E 5 119 ? 11.545 -14.341 -78.620 1.00 37.07  ? 118 ASP D N   1 
ATOM   6022 C CA  . ASP E 5 119 ? 11.686 -15.515 -79.462 1.00 34.78  ? 118 ASP D CA  1 
ATOM   6023 C C   . ASP E 5 119 ? 11.307 -16.743 -78.652 1.00 33.63  ? 118 ASP D C   1 
ATOM   6024 O O   . ASP E 5 119 ? 12.120 -17.666 -78.527 1.00 34.61  ? 118 ASP D O   1 
ATOM   6025 C CB  . ASP E 5 119 ? 13.119 -15.623 -79.984 1.00 36.42  ? 118 ASP D CB  1 
ATOM   6026 C CG  . ASP E 5 119 ? 13.247 -16.560 -81.173 1.00 44.99  ? 118 ASP D CG  1 
ATOM   6027 O OD1 . ASP E 5 119 ? 12.252 -17.242 -81.532 1.00 42.52  ? 118 ASP D OD1 1 
ATOM   6028 O OD2 . ASP E 5 119 ? 14.358 -16.617 -81.748 1.00 43.43  ? 118 ASP D OD2 1 
ATOM   6029 N N   . PRO E 5 120 ? 10.084 -16.800 -78.113 1.00 34.68  ? 119 PRO D N   1 
ATOM   6030 C CA  . PRO E 5 120 ? 9.728  -17.880 -77.185 1.00 32.19  ? 119 PRO D CA  1 
ATOM   6031 C C   . PRO E 5 120 ? 10.010 -19.260 -77.770 1.00 35.87  ? 119 PRO D C   1 
ATOM   6032 O O   . PRO E 5 120 ? 9.701  -19.538 -78.929 1.00 36.69  ? 119 PRO D O   1 
ATOM   6033 C CB  . PRO E 5 120 ? 8.226  -17.668 -76.955 1.00 37.64  ? 119 PRO D CB  1 
ATOM   6034 C CG  . PRO E 5 120 ? 7.762  -16.836 -78.142 1.00 37.28  ? 119 PRO D CG  1 
ATOM   6035 C CD  . PRO E 5 120 ? 8.919  -15.965 -78.474 1.00 35.23  ? 119 PRO D CD  1 
ATOM   6036 N N   . ALA E 5 121 ? 10.591 -20.135 -76.951 1.00 36.13  ? 120 ALA D N   1 
ATOM   6037 C CA  . ALA E 5 121 ? 10.914 -21.474 -77.418 1.00 32.81  ? 120 ALA D CA  1 
ATOM   6038 C C   . ALA E 5 121 ? 11.071 -22.409 -76.232 1.00 34.09  ? 120 ALA D C   1 
ATOM   6039 O O   . ALA E 5 121 ? 11.374 -21.983 -75.111 1.00 34.64  ? 120 ALA D O   1 
ATOM   6040 C CB  . ALA E 5 121 ? 12.181 -21.471 -78.269 1.00 31.38  ? 120 ALA D CB  1 
ATOM   6041 N N   . VAL E 5 122 ? 10.873 -23.697 -76.506 1.00 29.15  ? 121 VAL D N   1 
ATOM   6042 C CA  . VAL E 5 122 ? 11.053 -24.771 -75.536 1.00 32.63  ? 121 VAL D CA  1 
ATOM   6043 C C   . VAL E 5 122 ? 12.103 -25.734 -76.075 1.00 33.27  ? 121 VAL D C   1 
ATOM   6044 O O   . VAL E 5 122 ? 11.959 -26.263 -77.186 1.00 35.28  ? 121 VAL D O   1 
ATOM   6045 C CB  . VAL E 5 122 ? 9.740  -25.501 -75.248 1.00 34.09  ? 121 VAL D CB  1 
ATOM   6046 C CG1 . VAL E 5 122 ? 10.018 -26.794 -74.518 1.00 35.64  ? 121 VAL D CG1 1 
ATOM   6047 C CG2 . VAL E 5 122 ? 8.824  -24.601 -74.445 1.00 34.86  ? 121 VAL D CG2 1 
ATOM   6048 N N   . TYR E 5 123 ? 13.150 -25.967 -75.288 1.00 30.40  ? 122 TYR D N   1 
ATOM   6049 C CA  . TYR E 5 123 ? 14.290 -26.760 -75.711 1.00 28.30  ? 122 TYR D CA  1 
ATOM   6050 C C   . TYR E 5 123 ? 14.503 -27.916 -74.750 1.00 30.65  ? 122 TYR D C   1 
ATOM   6051 O O   . TYR E 5 123 ? 14.251 -27.795 -73.547 1.00 30.58  ? 122 TYR D O   1 
ATOM   6052 C CB  . TYR E 5 123 ? 15.563 -25.913 -75.774 1.00 25.32  ? 122 TYR D CB  1 
ATOM   6053 C CG  . TYR E 5 123 ? 15.494 -24.768 -76.752 1.00 31.33  ? 122 TYR D CG  1 
ATOM   6054 C CD1 . TYR E 5 123 ? 15.429 -25.006 -78.127 1.00 30.53  ? 122 TYR D CD1 1 
ATOM   6055 C CD2 . TYR E 5 123 ? 15.498 -23.441 -76.311 1.00 27.51  ? 122 TYR D CD2 1 
ATOM   6056 C CE1 . TYR E 5 123 ? 15.367 -23.944 -79.041 1.00 30.43  ? 122 TYR D CE1 1 
ATOM   6057 C CE2 . TYR E 5 123 ? 15.445 -22.370 -77.221 1.00 27.31  ? 122 TYR D CE2 1 
ATOM   6058 C CZ  . TYR E 5 123 ? 15.386 -22.634 -78.586 1.00 30.59  ? 122 TYR D CZ  1 
ATOM   6059 O OH  . TYR E 5 123 ? 15.339 -21.596 -79.503 1.00 30.41  ? 122 TYR D OH  1 
ATOM   6060 N N   . GLN E 5 124 ? 14.987 -29.035 -75.287 1.00 29.83  ? 123 GLN D N   1 
ATOM   6061 C CA  . GLN E 5 124 ? 15.388 -30.178 -74.477 1.00 34.32  ? 123 GLN D CA  1 
ATOM   6062 C C   . GLN E 5 124 ? 16.906 -30.187 -74.351 1.00 32.57  ? 123 GLN D C   1 
ATOM   6063 O O   . GLN E 5 124 ? 17.609 -30.034 -75.351 1.00 31.59  ? 123 GLN D O   1 
ATOM   6064 C CB  . GLN E 5 124 ? 14.893 -31.489 -75.094 1.00 32.00  ? 123 GLN D CB  1 
ATOM   6065 C CG  . GLN E 5 124 ? 15.383 -32.732 -74.384 1.00 39.47  ? 123 GLN D CG  1 
ATOM   6066 C CD  . GLN E 5 124 ? 14.516 -33.957 -74.658 1.00 53.72  ? 123 GLN D CD  1 
ATOM   6067 O OE1 . GLN E 5 124 ? 13.647 -33.946 -75.543 1.00 57.25  ? 123 GLN D OE1 1 
ATOM   6068 N NE2 . GLN E 5 124 ? 14.758 -35.028 -73.903 1.00 52.80  ? 123 GLN D NE2 1 
ATOM   6069 N N   . LEU E 5 125 ? 17.401 -30.379 -73.131 1.00 30.70  ? 124 LEU D N   1 
ATOM   6070 C CA  . LEU E 5 125 ? 18.827 -30.418 -72.823 1.00 30.30  ? 124 LEU D CA  1 
ATOM   6071 C C   . LEU E 5 125 ? 19.148 -31.745 -72.156 1.00 38.52  ? 124 LEU D C   1 
ATOM   6072 O O   . LEU E 5 125 ? 18.519 -32.101 -71.152 1.00 43.00  ? 124 LEU D O   1 
ATOM   6073 C CB  . LEU E 5 125 ? 19.232 -29.296 -71.858 1.00 27.20  ? 124 LEU D CB  1 
ATOM   6074 C CG  . LEU E 5 125 ? 19.275 -27.814 -72.211 1.00 31.85  ? 124 LEU D CG  1 
ATOM   6075 C CD1 . LEU E 5 125 ? 17.894 -27.254 -72.501 1.00 30.02  ? 124 LEU D CD1 1 
ATOM   6076 C CD2 . LEU E 5 125 ? 19.928 -27.085 -71.062 1.00 24.62  ? 124 LEU D CD2 1 
ATOM   6077 N N   . ARG E 5 126 ? 20.163 -32.441 -72.651 1.00 35.26  ? 125 ARG D N   1 
ATOM   6078 C CA  . ARG E 5 126 ? 20.465 -33.761 -72.120 1.00 41.30  ? 125 ARG D CA  1 
ATOM   6079 C C   . ARG E 5 126 ? 21.668 -33.707 -71.174 1.00 42.76  ? 125 ARG D C   1 
ATOM   6080 O O   . ARG E 5 126 ? 22.491 -32.784 -71.221 1.00 31.96  ? 125 ARG D O   1 
ATOM   6081 C CB  . ARG E 5 126 ? 20.676 -34.758 -73.273 1.00 44.12  ? 125 ARG D CB  1 
ATOM   6082 C CG  . ARG E 5 126 ? 19.365 -34.978 -74.104 1.00 48.83  ? 125 ARG D CG  1 
ATOM   6083 C CD  . ARG E 5 126 ? 19.310 -36.298 -74.881 1.00 47.30  ? 125 ARG D CD  1 
ATOM   6084 N NE  . ARG E 5 126 ? 17.983 -36.924 -74.835 1.00 57.64  ? 125 ARG D NE  1 
ATOM   6085 C CZ  . ARG E 5 126 ? 17.056 -36.823 -75.792 1.00 57.78  ? 125 ARG D CZ  1 
ATOM   6086 N NH1 . ARG E 5 126 ? 17.296 -36.105 -76.885 1.00 54.35  ? 125 ARG D NH1 1 
ATOM   6087 N NH2 . ARG E 5 126 ? 15.880 -37.435 -75.656 1.00 57.33  ? 125 ARG D NH2 1 
ATOM   6088 N N   . ASP E 5 127 ? 21.742 -34.706 -70.285 1.00 45.28  ? 126 ASP D N   1 
ATOM   6089 C CA  . ASP E 5 127 ? 22.753 -34.709 -69.230 1.00 42.44  ? 126 ASP D CA  1 
ATOM   6090 C C   . ASP E 5 127 ? 24.147 -34.735 -69.836 1.00 47.40  ? 126 ASP D C   1 
ATOM   6091 O O   . ASP E 5 127 ? 24.370 -35.321 -70.900 1.00 50.16  ? 126 ASP D O   1 
ATOM   6092 C CB  . ASP E 5 127 ? 22.563 -35.913 -68.303 1.00 44.53  ? 126 ASP D CB  1 
ATOM   6093 C CG  . ASP E 5 127 ? 23.429 -35.845 -67.036 1.00 42.97  ? 126 ASP D CG  1 
ATOM   6094 O OD1 . ASP E 5 127 ? 24.496 -35.207 -67.037 1.00 38.24  ? 126 ASP D OD1 1 
ATOM   6095 O OD2 . ASP E 5 127 ? 23.039 -36.457 -66.019 1.00 50.43  ? 126 ASP D OD2 1 
ATOM   6096 N N   . SER E 5 128 ? 25.105 -34.060 -69.213 1.00 40.93  ? 127 SER D N   1 
ATOM   6097 C CA  . SER E 5 128 ? 26.502 -34.020 -69.700 1.00 44.51  ? 127 SER D CA  1 
ATOM   6098 C C   . SER E 5 128 ? 27.124 -35.411 -69.609 1.00 46.66  ? 127 SER D C   1 
ATOM   6099 O O   . SER E 5 128 ? 28.048 -35.696 -70.325 1.00 44.05  ? 127 SER D O   1 
ATOM   6100 C CB  . SER E 5 128 ? 27.295 -33.058 -68.899 1.00 38.89  ? 127 SER D CB  1 
ATOM   6101 O OG  . SER E 5 128 ? 28.519 -32.790 -69.523 1.00 39.22  ? 127 SER D OG  1 
ATOM   6102 N N   . LYS E 5 129 ? 26.564 -36.242 -68.754 1.00 43.16  ? 128 LYS D N   1 
ATOM   6103 C CA  . LYS E 5 129 ? 27.119 -37.579 -68.546 1.00 50.79  ? 128 LYS D CA  1 
ATOM   6104 C C   . LYS E 5 129 ? 26.108 -38.717 -68.762 1.00 51.95  ? 128 LYS D C   1 
ATOM   6105 O O   . LYS E 5 129 ? 26.523 -39.732 -69.289 1.00 52.06  ? 128 LYS D O   1 
ATOM   6106 C CB  . LYS E 5 129 ? 27.803 -37.586 -67.175 1.00 46.05  ? 128 LYS D CB  1 
ATOM   6107 C CG  . LYS E 5 129 ? 26.918 -37.753 -65.956 1.00 52.67  ? 128 LYS D CG  1 
ATOM   6108 C CD  . LYS E 5 129 ? 27.619 -38.519 -64.862 1.00 55.22  ? 128 LYS D CD  1 
ATOM   6109 C CE  . LYS E 5 129 ? 26.857 -38.590 -63.556 1.00 53.63  ? 128 LYS D CE  1 
ATOM   6110 N NZ  . LYS E 5 129 ? 25.741 -39.564 -63.614 1.00 39.00  ? 128 LYS D NZ  1 
ATOM   6111 N N   . SER E 5 130 ? 24.821 -38.502 -68.518 1.00 52.50  ? 129 SER D N   1 
ATOM   6112 C CA  . SER E 5 130 ? 23.903 -39.671 -68.422 1.00 62.07  ? 129 SER D CA  1 
ATOM   6113 C C   . SER E 5 130 ? 23.174 -40.110 -69.695 1.00 70.48  ? 129 SER D C   1 
ATOM   6114 O O   . SER E 5 130 ? 23.248 -39.417 -70.742 1.00 65.61  ? 129 SER D O   1 
ATOM   6115 C CB  . SER E 5 130 ? 22.928 -39.501 -67.291 1.00 60.30  ? 129 SER D CB  1 
ATOM   6116 O OG  . SER E 5 130 ? 23.319 -40.311 -66.201 1.00 59.94  ? 129 SER D OG  1 
ATOM   6117 N N   . SER E 5 131 ? 22.486 -41.250 -69.575 1.00 71.88  ? 130 SER D N   1 
ATOM   6118 C CA  . SER E 5 131 ? 21.724 -41.724 -70.722 1.00 74.66  ? 130 SER D CA  1 
ATOM   6119 C C   . SER E 5 131 ? 20.252 -41.351 -70.647 1.00 78.91  ? 130 SER D C   1 
ATOM   6120 O O   . SER E 5 131 ? 19.610 -41.200 -71.693 1.00 74.67  ? 130 SER D O   1 
ATOM   6121 C CB  . SER E 5 131 ? 21.845 -43.250 -70.862 1.00 73.77  ? 130 SER D CB  1 
ATOM   6122 O OG  . SER E 5 131 ? 21.869 -43.883 -69.591 1.00 74.48  ? 130 SER D OG  1 
ATOM   6123 N N   . ASP E 5 132 ? 19.707 -41.190 -69.438 1.00 75.21  ? 131 ASP D N   1 
ATOM   6124 C CA  . ASP E 5 132 ? 18.278 -40.962 -69.262 1.00 70.01  ? 131 ASP D CA  1 
ATOM   6125 C C   . ASP E 5 132 ? 17.928 -39.506 -69.000 1.00 62.07  ? 131 ASP D C   1 
ATOM   6126 O O   . ASP E 5 132 ? 16.913 -39.022 -69.508 1.00 68.61  ? 131 ASP D O   1 
ATOM   6127 C CB  . ASP E 5 132 ? 17.732 -41.818 -68.107 1.00 68.35  ? 131 ASP D CB  1 
ATOM   6128 C CG  . ASP E 5 132 ? 16.239 -41.578 -67.847 1.00 76.57  ? 131 ASP D CG  1 
ATOM   6129 O OD1 . ASP E 5 132 ? 15.415 -42.284 -68.471 1.00 75.08  ? 131 ASP D OD1 1 
ATOM   6130 O OD2 . ASP E 5 132 ? 15.889 -40.694 -67.023 1.00 69.37  ? 131 ASP D OD2 1 
ATOM   6131 N N   . LYS E 5 133 ? 18.752 -38.792 -68.238 1.00 60.17  ? 132 LYS D N   1 
ATOM   6132 C CA  . LYS E 5 133 ? 18.296 -37.565 -67.599 1.00 51.36  ? 132 LYS D CA  1 
ATOM   6133 C C   . LYS E 5 133 ? 18.227 -36.414 -68.594 1.00 48.87  ? 132 LYS D C   1 
ATOM   6134 O O   . LYS E 5 133 ? 19.134 -36.221 -69.413 1.00 44.06  ? 132 LYS D O   1 
ATOM   6135 C CB  . LYS E 5 133 ? 19.203 -37.230 -66.423 1.00 44.50  ? 132 LYS D CB  1 
ATOM   6136 C CG  . LYS E 5 133 ? 19.001 -38.209 -65.253 1.00 58.38  ? 132 LYS D CG  1 
ATOM   6137 C CD  . LYS E 5 133 ? 20.204 -38.269 -64.325 1.00 53.94  ? 132 LYS D CD  1 
ATOM   6138 C CE  . LYS E 5 133 ? 20.451 -36.928 -63.685 1.00 43.53  ? 132 LYS D CE  1 
ATOM   6139 N NZ  . LYS E 5 133 ? 21.530 -37.037 -62.666 1.00 52.37  ? 132 LYS D NZ  1 
ATOM   6140 N N   . SER E 5 134 ? 17.132 -35.657 -68.528 1.00 43.01  ? 133 SER D N   1 
ATOM   6141 C CA  . SER E 5 134 ? 16.915 -34.548 -69.444 1.00 42.62  ? 133 SER D CA  1 
ATOM   6142 C C   . SER E 5 134 ? 16.127 -33.464 -68.726 1.00 37.02  ? 133 SER D C   1 
ATOM   6143 O O   . SER E 5 134 ? 15.446 -33.713 -67.731 1.00 39.53  ? 133 SER D O   1 
ATOM   6144 C CB  . SER E 5 134 ? 16.168 -34.977 -70.722 1.00 47.12  ? 133 SER D CB  1 
ATOM   6145 O OG  . SER E 5 134 ? 16.736 -36.132 -71.322 1.00 52.14  ? 133 SER D OG  1 
ATOM   6146 N N   . VAL E 5 135 ? 16.213 -32.262 -69.275 1.00 32.30  ? 134 VAL D N   1 
ATOM   6147 C CA  . VAL E 5 135 ? 15.622 -31.057 -68.714 1.00 32.67  ? 134 VAL D CA  1 
ATOM   6148 C C   . VAL E 5 135 ? 14.983 -30.281 -69.863 1.00 30.64  ? 134 VAL D C   1 
ATOM   6149 O O   . VAL E 5 135 ? 15.537 -30.240 -70.964 1.00 29.03  ? 134 VAL D O   1 
ATOM   6150 C CB  . VAL E 5 135 ? 16.708 -30.217 -68.002 1.00 30.52  ? 134 VAL D CB  1 
ATOM   6151 C CG1 . VAL E 5 135 ? 16.246 -28.831 -67.777 1.00 37.10  ? 134 VAL D CG1 1 
ATOM   6152 C CG2 . VAL E 5 135 ? 17.103 -30.863 -66.683 1.00 34.46  ? 134 VAL D CG2 1 
ATOM   6153 N N   . CYS E 5 136 ? 13.826 -29.668 -69.617 1.00 28.41  ? 135 CYS D N   1 
ATOM   6154 C CA  . CYS E 5 136 ? 13.188 -28.792 -70.596 1.00 31.50  ? 135 CYS D CA  1 
ATOM   6155 C C   . CYS E 5 136 ? 13.352 -27.333 -70.188 1.00 32.93  ? 135 CYS D C   1 
ATOM   6156 O O   . CYS E 5 136 ? 13.146 -26.970 -69.024 1.00 30.56  ? 135 CYS D O   1 
ATOM   6157 C CB  . CYS E 5 136 ? 11.695 -29.117 -70.776 1.00 27.73  ? 135 CYS D CB  1 
ATOM   6158 S SG  . CYS E 5 136 ? 11.356 -30.869 -71.162 1.00 44.55  ? 135 CYS D SG  1 
ATOM   6159 N N   . LEU E 5 137 ? 13.690 -26.497 -71.166 1.00 31.36  ? 136 LEU D N   1 
ATOM   6160 C CA  . LEU E 5 137 ? 14.000 -25.093 -70.947 1.00 30.17  ? 136 LEU D CA  1 
ATOM   6161 C C   . LEU E 5 137 ? 13.032 -24.241 -71.755 1.00 35.26  ? 136 LEU D C   1 
ATOM   6162 O O   . LEU E 5 137 ? 13.032 -24.299 -72.994 1.00 30.50  ? 136 LEU D O   1 
ATOM   6163 C CB  . LEU E 5 137 ? 15.443 -24.793 -71.345 1.00 25.67  ? 136 LEU D CB  1 
ATOM   6164 C CG  . LEU E 5 137 ? 15.848 -23.325 -71.211 1.00 31.62  ? 136 LEU D CG  1 
ATOM   6165 C CD1 . LEU E 5 137 ? 15.989 -22.938 -69.726 1.00 29.20  ? 136 LEU D CD1 1 
ATOM   6166 C CD2 . LEU E 5 137 ? 17.148 -23.078 -71.974 1.00 22.46  ? 136 LEU D CD2 1 
ATOM   6167 N N   . PHE E 5 138 ? 12.207 -23.465 -71.054 1.00 28.86  ? 137 PHE D N   1 
ATOM   6168 C CA  . PHE E 5 138 ? 11.341 -22.465 -71.662 1.00 30.98  ? 137 PHE D CA  1 
ATOM   6169 C C   . PHE E 5 138 ? 12.044 -21.116 -71.566 1.00 32.05  ? 137 PHE D C   1 
ATOM   6170 O O   . PHE E 5 138 ? 12.294 -20.621 -70.461 1.00 30.24  ? 137 PHE D O   1 
ATOM   6171 C CB  . PHE E 5 138 ? 9.981  -22.437 -70.958 1.00 34.76  ? 137 PHE D CB  1 
ATOM   6172 C CG  . PHE E 5 138 ? 9.015  -21.429 -71.516 1.00 35.29  ? 137 PHE D CG  1 
ATOM   6173 C CD1 . PHE E 5 138 ? 9.028  -21.099 -72.862 1.00 33.04  ? 137 PHE D CD1 1 
ATOM   6174 C CD2 . PHE E 5 138 ? 8.079  -20.820 -70.686 1.00 35.74  ? 137 PHE D CD2 1 
ATOM   6175 C CE1 . PHE E 5 138 ? 8.127  -20.170 -73.369 1.00 35.96  ? 137 PHE D CE1 1 
ATOM   6176 C CE2 . PHE E 5 138 ? 7.187  -19.892 -71.183 1.00 34.16  ? 137 PHE D CE2 1 
ATOM   6177 C CZ  . PHE E 5 138 ? 7.207  -19.566 -72.522 1.00 36.34  ? 137 PHE D CZ  1 
ATOM   6178 N N   . THR E 5 139 ? 12.354 -20.519 -72.716 1.00 29.98  ? 138 THR D N   1 
ATOM   6179 C CA  . THR E 5 139 ? 13.250 -19.377 -72.745 1.00 28.48  ? 138 THR D CA  1 
ATOM   6180 C C   . THR E 5 139 ? 12.840 -18.396 -73.833 1.00 29.75  ? 138 THR D C   1 
ATOM   6181 O O   . THR E 5 139 ? 12.159 -18.744 -74.802 1.00 33.88  ? 138 THR D O   1 
ATOM   6182 C CB  . THR E 5 139 ? 14.708 -19.836 -72.948 1.00 28.71  ? 138 THR D CB  1 
ATOM   6183 O OG1 . THR E 5 139 ? 15.600 -18.778 -72.596 1.00 30.08  ? 138 THR D OG1 1 
ATOM   6184 C CG2 . THR E 5 139 ? 14.969 -20.236 -74.393 1.00 31.25  ? 138 THR D CG2 1 
ATOM   6185 N N   . ASP E 5 140 ? 13.267 -17.151 -73.640 1.00 30.21  ? 139 ASP D N   1 
ATOM   6186 C CA  . ASP E 5 140 ? 13.186 -16.025 -74.572 1.00 33.76  ? 139 ASP D CA  1 
ATOM   6187 C C   . ASP E 5 140 ? 11.778 -15.476 -74.756 1.00 35.31  ? 139 ASP D C   1 
ATOM   6188 O O   . ASP E 5 140 ? 11.559 -14.670 -75.662 1.00 35.47  ? 139 ASP D O   1 
ATOM   6189 C CB  . ASP E 5 140 ? 13.798 -16.373 -75.931 1.00 31.49  ? 139 ASP D CB  1 
ATOM   6190 C CG  . ASP E 5 140 ? 15.299 -16.599 -75.834 1.00 34.46  ? 139 ASP D CG  1 
ATOM   6191 O OD1 . ASP E 5 140 ? 15.899 -16.113 -74.852 1.00 34.93  ? 139 ASP D OD1 1 
ATOM   6192 O OD2 . ASP E 5 140 ? 15.876 -17.282 -76.703 1.00 35.18  ? 139 ASP D OD2 1 
ATOM   6193 N N   . PHE E 5 141 ? 10.831 -15.859 -73.903 1.00 31.88  ? 140 PHE D N   1 
ATOM   6194 C CA  . PHE E 5 141 ? 9.530  -15.219 -73.885 1.00 34.50  ? 140 PHE D CA  1 
ATOM   6195 C C   . PHE E 5 141 ? 9.650  -13.804 -73.329 1.00 37.77  ? 140 PHE D C   1 
ATOM   6196 O O   . PHE E 5 141 ? 10.594 -13.470 -72.608 1.00 34.76  ? 140 PHE D O   1 
ATOM   6197 C CB  . PHE E 5 141 ? 8.538  -16.033 -73.054 1.00 33.22  ? 140 PHE D CB  1 
ATOM   6198 C CG  . PHE E 5 141 ? 9.069  -16.480 -71.721 1.00 36.38  ? 140 PHE D CG  1 
ATOM   6199 C CD1 . PHE E 5 141 ? 9.797  -17.650 -71.600 1.00 34.49  ? 140 PHE D CD1 1 
ATOM   6200 C CD2 . PHE E 5 141 ? 8.818  -15.736 -70.575 1.00 35.72  ? 140 PHE D CD2 1 
ATOM   6201 C CE1 . PHE E 5 141 ? 10.260 -18.070 -70.350 1.00 36.27  ? 140 PHE D CE1 1 
ATOM   6202 C CE2 . PHE E 5 141 ? 9.280  -16.151 -69.338 1.00 33.09  ? 140 PHE D CE2 1 
ATOM   6203 C CZ  . PHE E 5 141 ? 10.005 -17.307 -69.221 1.00 29.18  ? 140 PHE D CZ  1 
ATOM   6204 N N   . ASP E 5 142 ? 8.684  -12.959 -73.674 1.00 38.11  ? 141 ASP D N   1 
ATOM   6205 C CA  . ASP E 5 142 ? 8.776  -11.593 -73.186 1.00 42.25  ? 141 ASP D CA  1 
ATOM   6206 C C   . ASP E 5 142 ? 8.158  -11.501 -71.790 1.00 42.67  ? 141 ASP D C   1 
ATOM   6207 O O   . ASP E 5 142 ? 7.554  -12.449 -71.279 1.00 42.02  ? 141 ASP D O   1 
ATOM   6208 C CB  . ASP E 5 142 ? 8.162  -10.604 -74.193 1.00 47.78  ? 141 ASP D CB  1 
ATOM   6209 C CG  . ASP E 5 142 ? 6.663  -10.371 -74.003 1.00 52.30  ? 141 ASP D CG  1 
ATOM   6210 O OD1 . ASP E 5 142 ? 5.943  -11.218 -73.424 1.00 51.53  ? 141 ASP D OD1 1 
ATOM   6211 O OD2 . ASP E 5 142 ? 6.201  -9.305  -74.466 1.00 59.01  ? 141 ASP D OD2 1 
ATOM   6212 N N   . SER E 5 143 ? 8.330  -10.342 -71.161 1.00 44.23  ? 142 SER D N   1 
ATOM   6213 C CA  . SER E 5 143 ? 8.093  -10.271 -69.725 1.00 47.32  ? 142 SER D CA  1 
ATOM   6214 C C   . SER E 5 143 ? 6.635  -10.520 -69.349 1.00 50.62  ? 142 SER D C   1 
ATOM   6215 O O   . SER E 5 143 ? 6.359  -10.868 -68.196 1.00 52.84  ? 142 SER D O   1 
ATOM   6216 C CB  . SER E 5 143 ? 8.568  -8.915  -69.204 1.00 45.03  ? 142 SER D CB  1 
ATOM   6217 O OG  . SER E 5 143 ? 9.969  -8.941  -68.987 1.00 40.86  ? 142 SER D OG  1 
ATOM   6218 N N   . GLN E 5 144 ? 5.702  -10.376 -70.291 1.00 52.84  ? 143 GLN D N   1 
ATOM   6219 C CA  . GLN E 5 144 ? 4.287  -10.555 -69.983 1.00 50.83  ? 143 GLN D CA  1 
ATOM   6220 C C   . GLN E 5 144 ? 3.864  -12.017 -69.888 1.00 48.27  ? 143 GLN D C   1 
ATOM   6221 O O   . GLN E 5 144 ? 2.710  -12.283 -69.533 1.00 52.45  ? 143 GLN D O   1 
ATOM   6222 C CB  . GLN E 5 144 ? 3.425  -9.842  -71.031 1.00 52.49  ? 143 GLN D CB  1 
ATOM   6223 C CG  . GLN E 5 144 ? 2.165  -9.204  -70.457 1.00 62.39  ? 143 GLN D CG  1 
ATOM   6224 C CD  . GLN E 5 144 ? 1.054  -9.049  -71.495 1.00 65.44  ? 143 GLN D CD  1 
ATOM   6225 O OE1 . GLN E 5 144 ? 1.316  -8.998  -72.700 1.00 64.58  ? 143 GLN D OE1 1 
ATOM   6226 N NE2 . GLN E 5 144 ? -0.193 -8.989  -71.027 1.00 54.03  ? 143 GLN D NE2 1 
ATOM   6227 N N   . THR E 5 145 ? 4.738  -12.969 -70.210 1.00 44.13  ? 144 THR D N   1 
ATOM   6228 C CA  . THR E 5 145 ? 4.426  -14.378 -69.993 1.00 44.33  ? 144 THR D CA  1 
ATOM   6229 C C   . THR E 5 145 ? 4.600  -14.725 -68.520 1.00 46.29  ? 144 THR D C   1 
ATOM   6230 O O   . THR E 5 145 ? 5.596  -14.341 -67.898 1.00 44.79  ? 144 THR D O   1 
ATOM   6231 C CB  . THR E 5 145 ? 5.322  -15.288 -70.832 1.00 42.42  ? 144 THR D CB  1 
ATOM   6232 O OG1 . THR E 5 145 ? 5.077  -15.075 -72.223 1.00 43.91  ? 144 THR D OG1 1 
ATOM   6233 C CG2 . THR E 5 145 ? 5.064  -16.755 -70.491 1.00 40.42  ? 144 THR D CG2 1 
ATOM   6234 N N   . ASN E 5 146 ? 3.624  -15.445 -67.966 1.00 48.02  ? 145 ASN D N   1 
ATOM   6235 C CA  . ASN E 5 146 ? 3.666  -15.958 -66.604 1.00 45.12  ? 145 ASN D CA  1 
ATOM   6236 C C   . ASN E 5 146 ? 3.778  -17.470 -66.673 1.00 47.36  ? 145 ASN D C   1 
ATOM   6237 O O   . ASN E 5 146 ? 2.918  -18.133 -67.262 1.00 50.20  ? 145 ASN D O   1 
ATOM   6238 C CB  . ASN E 5 146 ? 2.418  -15.566 -65.808 1.00 44.01  ? 145 ASN D CB  1 
ATOM   6239 C CG  . ASN E 5 146 ? 2.290  -14.066 -65.602 1.00 49.72  ? 145 ASN D CG  1 
ATOM   6240 O OD1 . ASN E 5 146 ? 3.284  -13.331 -65.594 1.00 52.91  ? 145 ASN D OD1 1 
ATOM   6241 N ND2 . ASN E 5 146 ? 1.057  -13.604 -65.427 1.00 49.31  ? 145 ASN D ND2 1 
ATOM   6242 N N   . VAL E 5 147 ? 4.829  -18.012 -66.074 1.00 46.43  ? 146 VAL D N   1 
ATOM   6243 C CA  . VAL E 5 147 ? 4.960  -19.454 -65.944 1.00 47.18  ? 146 VAL D CA  1 
ATOM   6244 C C   . VAL E 5 147 ? 4.158  -19.896 -64.730 1.00 51.17  ? 146 VAL D C   1 
ATOM   6245 O O   . VAL E 5 147 ? 4.302  -19.335 -63.639 1.00 50.92  ? 146 VAL D O   1 
ATOM   6246 C CB  . VAL E 5 147 ? 6.434  -19.860 -65.810 1.00 42.95  ? 146 VAL D CB  1 
ATOM   6247 C CG1 . VAL E 5 147 ? 6.552  -21.359 -65.582 1.00 41.45  ? 146 VAL D CG1 1 
ATOM   6248 C CG2 . VAL E 5 147 ? 7.202  -19.447 -67.034 1.00 40.92  ? 146 VAL D CG2 1 
ATOM   6249 N N   . SER E 5 148 ? 3.303  -20.891 -64.914 1.00 51.33  ? 147 SER D N   1 
ATOM   6250 C CA  . SER E 5 148 ? 2.450  -21.354 -63.833 1.00 53.43  ? 147 SER D CA  1 
ATOM   6251 C C   . SER E 5 148 ? 3.118  -22.524 -63.120 1.00 55.01  ? 147 SER D C   1 
ATOM   6252 O O   . SER E 5 148 ? 3.728  -23.392 -63.754 1.00 49.12  ? 147 SER D O   1 
ATOM   6253 C CB  . SER E 5 148 ? 1.068  -21.748 -64.370 1.00 49.44  ? 147 SER D CB  1 
ATOM   6254 O OG  . SER E 5 148 ? 0.977  -23.147 -64.593 1.00 55.27  ? 147 SER D OG  1 
ATOM   6255 N N   . GLN E 5 149 ? 3.022  -22.526 -61.793 1.00 56.26  ? 148 GLN D N   1 
ATOM   6256 C CA  . GLN E 5 149 ? 3.594  -23.613 -61.013 1.00 59.64  ? 148 GLN D CA  1 
ATOM   6257 C C   . GLN E 5 149 ? 3.003  -24.944 -61.463 1.00 59.60  ? 148 GLN D C   1 
ATOM   6258 O O   . GLN E 5 149 ? 1.865  -25.016 -61.930 1.00 65.48  ? 148 GLN D O   1 
ATOM   6259 C CB  . GLN E 5 149 ? 3.341  -23.377 -59.520 1.00 60.89  ? 148 GLN D CB  1 
ATOM   6260 C CG  . GLN E 5 149 ? 4.132  -24.287 -58.591 1.00 67.30  ? 148 GLN D CG  1 
ATOM   6261 C CD  . GLN E 5 149 ? 5.506  -24.642 -59.142 1.00 66.59  ? 148 GLN D CD  1 
ATOM   6262 O OE1 . GLN E 5 149 ? 6.338  -23.765 -59.380 1.00 66.21  ? 148 GLN D OE1 1 
ATOM   6263 N NE2 . GLN E 5 149 ? 5.747  -25.931 -59.347 1.00 59.46  ? 148 GLN D NE2 1 
ATOM   6264 N N   . SER E 5 150 ? 3.795  -25.999 -61.352 1.00 59.06  ? 149 SER D N   1 
ATOM   6265 C CA  . SER E 5 150 ? 3.294  -27.319 -61.696 1.00 59.19  ? 149 SER D CA  1 
ATOM   6266 C C   . SER E 5 150 ? 2.107  -27.681 -60.814 1.00 64.75  ? 149 SER D C   1 
ATOM   6267 O O   . SER E 5 150 ? 2.143  -27.503 -59.593 1.00 65.23  ? 149 SER D O   1 
ATOM   6268 C CB  . SER E 5 150 ? 4.401  -28.362 -61.547 1.00 52.45  ? 149 SER D CB  1 
ATOM   6269 O OG  . SER E 5 150 ? 3.883  -29.674 -61.727 1.00 56.01  ? 149 SER D OG  1 
ATOM   6270 N N   . LYS E 5 151 ? 1.117  -28.337 -61.407 1.00 65.05  ? 150 LYS D N   1 
ATOM   6271 C CA  . LYS E 5 151 ? -0.057 -28.829 -60.636 1.00 65.96  ? 150 LYS D CA  1 
ATOM   6272 C C   . LYS E 5 151 ? -0.064 -30.361 -60.706 1.00 64.38  ? 150 LYS D C   1 
ATOM   6273 O O   . LYS E 5 151 ? -1.118 -30.959 -60.482 1.00 56.56  ? 150 LYS D O   1 
ATOM   6274 C CB  . LYS E 5 151 ? -1.351 -28.166 -61.111 1.00 60.20  ? 150 LYS D CB  1 
ATOM   6275 N N   . ASP E 5 152 ? 1.129  -30.916 -60.949 1.00 65.13  ? 151 ASP D N   1 
ATOM   6276 C CA  . ASP E 5 152 ? 1.476  -32.352 -61.086 1.00 64.17  ? 151 ASP D CA  1 
ATOM   6277 C C   . ASP E 5 152 ? 2.735  -32.638 -60.259 1.00 61.89  ? 151 ASP D C   1 
ATOM   6278 O O   . ASP E 5 152 ? 3.840  -32.287 -60.677 1.00 55.61  ? 151 ASP D O   1 
ATOM   6279 C CB  . ASP E 5 152 ? 1.701  -32.702 -62.552 1.00 62.91  ? 151 ASP D CB  1 
ATOM   6280 C CG  . ASP E 5 152 ? 2.025  -34.158 -62.760 1.00 63.82  ? 151 ASP D CG  1 
ATOM   6281 O OD1 . ASP E 5 152 ? 2.367  -34.815 -61.785 1.00 62.30  ? 151 ASP D OD1 1 
ATOM   6282 O OD2 . ASP E 5 152 ? 1.881  -34.613 -63.891 1.00 67.99  ? 151 ASP D OD2 1 
ATOM   6283 N N   . SER E 5 153 ? 2.543  -33.369 -59.173 1.00 63.35  ? 152 SER D N   1 
ATOM   6284 C CA  . SER E 5 153 ? 3.572  -33.671 -58.154 1.00 58.29  ? 152 SER D CA  1 
ATOM   6285 C C   . SER E 5 153 ? 4.890  -34.261 -58.669 1.00 62.56  ? 152 SER D C   1 
ATOM   6286 O O   . SER E 5 153 ? 5.869  -34.084 -57.964 1.00 60.74  ? 152 SER D O   1 
ATOM   6287 C CB  . SER E 5 153 ? 2.970  -34.512 -57.120 1.00 62.80  ? 152 SER D CB  1 
ATOM   6288 O OG  . SER E 5 153 ? 2.066  -33.734 -56.370 1.00 68.20  ? 152 SER D OG  1 
ATOM   6289 N N   . ASP E 5 154 ? 4.935  -34.972 -59.789 1.00 57.14  ? 153 ASP D N   1 
ATOM   6290 C CA  . ASP E 5 154 ? 6.264  -35.507 -60.173 1.00 56.08  ? 153 ASP D CA  1 
ATOM   6291 C C   . ASP E 5 154 ? 6.885  -34.705 -61.314 1.00 50.13  ? 153 ASP D C   1 
ATOM   6292 O O   . ASP E 5 154 ? 7.798  -35.182 -61.889 1.00 46.20  ? 153 ASP D O   1 
ATOM   6293 C CB  . ASP E 5 154 ? 6.291  -37.024 -60.342 1.00 61.33  ? 153 ASP D CB  1 
ATOM   6294 C CG  . ASP E 5 154 ? 5.105  -37.520 -61.117 1.00 69.84  ? 153 ASP D CG  1 
ATOM   6295 O OD1 . ASP E 5 154 ? 4.651  -36.788 -61.974 1.00 72.56  ? 153 ASP D OD1 1 
ATOM   6296 O OD2 . ASP E 5 154 ? 4.642  -38.619 -60.834 1.00 73.40  ? 153 ASP D OD2 1 
ATOM   6297 N N   . VAL E 5 155 ? 6.366  -33.524 -61.588 1.00 48.78  ? 154 VAL D N   1 
ATOM   6298 C CA  . VAL E 5 155 ? 6.990  -32.610 -62.575 1.00 47.38  ? 154 VAL D CA  1 
ATOM   6299 C C   . VAL E 5 155 ? 7.402  -31.346 -61.826 1.00 45.41  ? 154 VAL D C   1 
ATOM   6300 O O   . VAL E 5 155 ? 6.566  -30.751 -61.191 1.00 45.75  ? 154 VAL D O   1 
ATOM   6301 C CB  . VAL E 5 155 ? 6.057  -32.269 -63.738 1.00 47.66  ? 154 VAL D CB  1 
ATOM   6302 C CG1 . VAL E 5 155 ? 6.675  -31.211 -64.614 1.00 54.24  ? 154 VAL D CG1 1 
ATOM   6303 C CG2 . VAL E 5 155 ? 5.744  -33.498 -64.544 1.00 51.65  ? 154 VAL D CG2 1 
ATOM   6304 N N   . TYR E 5 156 ? 8.655  -30.950 -61.962 1.00 39.57  ? 155 TYR D N   1 
ATOM   6305 C CA  . TYR E 5 156 ? 9.169  -29.776 -61.271 1.00 38.21  ? 155 TYR D CA  1 
ATOM   6306 C C   . TYR E 5 156 ? 9.367  -28.653 -62.270 1.00 34.27  ? 155 TYR D C   1 
ATOM   6307 O O   . TYR E 5 156 ? 9.963  -28.866 -63.328 1.00 36.34  ? 155 TYR D O   1 
ATOM   6308 C CB  . TYR E 5 156 ? 10.481 -30.108 -60.578 1.00 34.71  ? 155 TYR D CB  1 
ATOM   6309 C CG  . TYR E 5 156 ? 10.332 -31.282 -59.665 1.00 34.94  ? 155 TYR D CG  1 
ATOM   6310 C CD1 . TYR E 5 156 ? 9.701  -31.136 -58.441 1.00 33.78  ? 155 TYR D CD1 1 
ATOM   6311 C CD2 . TYR E 5 156 ? 10.784 -32.544 -60.035 1.00 37.49  ? 155 TYR D CD2 1 
ATOM   6312 C CE1 . TYR E 5 156 ? 9.551  -32.195 -57.589 1.00 37.80  ? 155 TYR D CE1 1 
ATOM   6313 C CE2 . TYR E 5 156 ? 10.634 -33.627 -59.188 1.00 43.85  ? 155 TYR D CE2 1 
ATOM   6314 C CZ  . TYR E 5 156 ? 10.019 -33.439 -57.958 1.00 43.85  ? 155 TYR D CZ  1 
ATOM   6315 O OH  . TYR E 5 156 ? 9.855  -34.486 -57.091 1.00 43.87  ? 155 TYR D OH  1 
ATOM   6316 N N   . ILE E 5 157 ? 8.851  -27.477 -61.941 1.00 32.42  ? 156 ILE D N   1 
ATOM   6317 C CA  . ILE E 5 157 ? 8.973  -26.291 -62.777 1.00 35.55  ? 156 ILE D CA  1 
ATOM   6318 C C   . ILE E 5 157 ? 9.373  -25.128 -61.885 1.00 38.79  ? 156 ILE D C   1 
ATOM   6319 O O   . ILE E 5 157 ? 8.693  -24.849 -60.891 1.00 37.83  ? 156 ILE D O   1 
ATOM   6320 C CB  . ILE E 5 157 ? 7.658  -25.960 -63.506 1.00 39.31  ? 156 ILE D CB  1 
ATOM   6321 C CG1 . ILE E 5 157 ? 7.120  -27.172 -64.259 1.00 37.66  ? 156 ILE D CG1 1 
ATOM   6322 C CG2 . ILE E 5 157 ? 7.864  -24.790 -64.453 1.00 34.12  ? 156 ILE D CG2 1 
ATOM   6323 C CD1 . ILE E 5 157 ? 5.885  -26.855 -65.101 1.00 35.72  ? 156 ILE D CD1 1 
ATOM   6324 N N   . THR E 5 158 ? 10.454 -24.439 -62.248 1.00 35.82  ? 157 THR D N   1 
ATOM   6325 C CA  . THR E 5 158 ? 10.888 -23.272 -61.491 1.00 38.41  ? 157 THR D CA  1 
ATOM   6326 C C   . THR E 5 158 ? 10.112 -22.030 -61.918 1.00 38.96  ? 157 THR D C   1 
ATOM   6327 O O   . THR E 5 158 ? 9.525  -21.973 -63.004 1.00 41.27  ? 157 THR D O   1 
ATOM   6328 C CB  . THR E 5 158 ? 12.387 -23.013 -61.689 1.00 39.30  ? 157 THR D CB  1 
ATOM   6329 O OG1 . THR E 5 158 ? 12.613 -22.454 -62.999 1.00 35.49  ? 157 THR D OG1 1 
ATOM   6330 C CG2 . THR E 5 158 ? 13.177 -24.293 -61.551 1.00 35.67  ? 157 THR D CG2 1 
ATOM   6331 N N   . ASP E 5 159 ? 10.128 -21.015 -61.056 1.00 41.10  ? 158 ASP D N   1 
ATOM   6332 C CA  . ASP E 5 159 ? 9.661  -19.715 -61.505 1.00 43.01  ? 158 ASP D CA  1 
ATOM   6333 C C   . ASP E 5 159 ? 10.591 -19.182 -62.598 1.00 39.37  ? 158 ASP D C   1 
ATOM   6334 O O   . ASP E 5 159 ? 11.698 -19.689 -62.819 1.00 35.08  ? 158 ASP D O   1 
ATOM   6335 C CB  . ASP E 5 159 ? 9.589  -18.698 -60.359 1.00 47.52  ? 158 ASP D CB  1 
ATOM   6336 C CG  . ASP E 5 159 ? 9.038  -19.278 -59.063 1.00 61.07  ? 158 ASP D CG  1 
ATOM   6337 O OD1 . ASP E 5 159 ? 8.116  -20.130 -59.107 1.00 65.85  ? 158 ASP D OD1 1 
ATOM   6338 O OD2 . ASP E 5 159 ? 9.502  -18.829 -57.986 1.00 65.42  ? 158 ASP D OD2 1 
ATOM   6339 N N   . LYS E 5 160 ? 10.133 -18.131 -63.276 1.00 35.31  ? 159 LYS D N   1 
ATOM   6340 C CA  . LYS E 5 160 ? 10.928 -17.543 -64.340 1.00 39.25  ? 159 LYS D CA  1 
ATOM   6341 C C   . LYS E 5 160 ? 12.112 -16.772 -63.764 1.00 41.08  ? 159 LYS D C   1 
ATOM   6342 O O   . LYS E 5 160 ? 12.128 -16.361 -62.600 1.00 37.55  ? 159 LYS D O   1 
ATOM   6343 C CB  . LYS E 5 160 ? 10.076 -16.642 -65.240 1.00 36.67  ? 159 LYS D CB  1 
ATOM   6344 C CG  . LYS E 5 160 ? 9.608  -15.342 -64.627 1.00 45.30  ? 159 LYS D CG  1 
ATOM   6345 C CD  . LYS E 5 160 ? 8.513  -14.748 -65.508 1.00 49.36  ? 159 LYS D CD  1 
ATOM   6346 C CE  . LYS E 5 160 ? 8.567  -13.233 -65.540 1.00 50.95  ? 159 LYS D CE  1 
ATOM   6347 N NZ  . LYS E 5 160 ? 7.243  -12.667 -65.912 1.00 50.77  ? 159 LYS D NZ  1 
ATOM   6348 N N   . CYS E 5 161 ? 13.122 -16.591 -64.605 1.00 38.26  ? 160 CYS D N   1 
ATOM   6349 C CA  . CYS E 5 161 ? 14.415 -16.129 -64.134 1.00 35.41  ? 160 CYS D CA  1 
ATOM   6350 C C   . CYS E 5 161 ? 15.054 -15.287 -65.222 1.00 31.84  ? 160 CYS D C   1 
ATOM   6351 O O   . CYS E 5 161 ? 15.127 -15.727 -66.376 1.00 34.70  ? 160 CYS D O   1 
ATOM   6352 C CB  . CYS E 5 161 ? 15.304 -17.327 -63.795 1.00 42.72  ? 160 CYS D CB  1 
ATOM   6353 S SG  . CYS E 5 161 ? 16.525 -17.056 -62.514 1.00 46.80  ? 160 CYS D SG  1 
ATOM   6354 N N   . VAL E 5 162 ? 15.537 -14.105 -64.853 1.00 26.96  ? 161 VAL D N   1 
ATOM   6355 C CA  . VAL E 5 162 ? 16.154 -13.175 -65.792 1.00 32.48  ? 161 VAL D CA  1 
ATOM   6356 C C   . VAL E 5 162 ? 17.667 -13.302 -65.677 1.00 31.40  ? 161 VAL D C   1 
ATOM   6357 O O   . VAL E 5 162 ? 18.226 -13.080 -64.598 1.00 28.46  ? 161 VAL D O   1 
ATOM   6358 C CB  . VAL E 5 162 ? 15.723 -11.728 -65.518 1.00 31.55  ? 161 VAL D CB  1 
ATOM   6359 C CG1 . VAL E 5 162 ? 16.101 -10.845 -66.693 1.00 32.34  ? 161 VAL D CG1 1 
ATOM   6360 C CG2 . VAL E 5 162 ? 14.244 -11.654 -65.201 1.00 31.87  ? 161 VAL D CG2 1 
ATOM   6361 N N   . LEU E 5 163 ? 18.335 -13.637 -66.785 1.00 28.03  ? 162 LEU D N   1 
ATOM   6362 C CA  . LEU E 5 163 ? 19.784 -13.563 -66.867 1.00 27.88  ? 162 LEU D CA  1 
ATOM   6363 C C   . LEU E 5 163 ? 20.178 -12.419 -67.794 1.00 29.76  ? 162 LEU D C   1 
ATOM   6364 O O   . LEU E 5 163 ? 19.406 -11.992 -68.650 1.00 30.28  ? 162 LEU D O   1 
ATOM   6365 C CB  . LEU E 5 163 ? 20.398 -14.895 -67.338 1.00 27.79  ? 162 LEU D CB  1 
ATOM   6366 C CG  . LEU E 5 163 ? 20.092 -15.465 -68.736 1.00 32.26  ? 162 LEU D CG  1 
ATOM   6367 C CD1 . LEU E 5 163 ? 21.016 -14.863 -69.810 1.00 27.82  ? 162 LEU D CD1 1 
ATOM   6368 C CD2 . LEU E 5 163 ? 20.155 -17.020 -68.765 1.00 31.06  ? 162 LEU D CD2 1 
ATOM   6369 N N   . ASP E 5 164 ? 21.393 -11.912 -67.601 1.00 29.19  ? 163 ASP D N   1 
ATOM   6370 C CA  . ASP E 5 164 ? 21.864 -10.700 -68.265 1.00 29.62  ? 163 ASP D CA  1 
ATOM   6371 C C   . ASP E 5 164 ? 23.248 -11.011 -68.818 1.00 28.77  ? 163 ASP D C   1 
ATOM   6372 O O   . ASP E 5 164 ? 24.229 -11.051 -68.070 1.00 28.75  ? 163 ASP D O   1 
ATOM   6373 C CB  . ASP E 5 164 ? 21.881 -9.514  -67.282 1.00 29.74  ? 163 ASP D CB  1 
ATOM   6374 C CG  . ASP E 5 164 ? 22.531 -8.247  -67.863 1.00 32.35  ? 163 ASP D CG  1 
ATOM   6375 O OD1 . ASP E 5 164 ? 22.765 -8.167  -69.088 1.00 37.25  ? 163 ASP D OD1 1 
ATOM   6376 O OD2 . ASP E 5 164 ? 22.791 -7.301  -67.081 1.00 38.76  ? 163 ASP D OD2 1 
ATOM   6377 N N   . MET E 5 165 ? 23.327 -11.223 -70.123 1.00 26.10  ? 164 MET D N   1 
ATOM   6378 C CA  . MET E 5 165 ? 24.613 -11.314 -70.804 1.00 31.09  ? 164 MET D CA  1 
ATOM   6379 C C   . MET E 5 165 ? 25.111 -9.881  -70.978 1.00 34.63  ? 164 MET D C   1 
ATOM   6380 O O   . MET E 5 165 ? 24.723 -9.186  -71.918 1.00 39.34  ? 164 MET D O   1 
ATOM   6381 C CB  . MET E 5 165 ? 24.463 -12.068 -72.124 1.00 32.19  ? 164 MET D CB  1 
ATOM   6382 C CG  . MET E 5 165 ? 23.771 -13.445 -71.969 1.00 27.05  ? 164 MET D CG  1 
ATOM   6383 S SD  . MET E 5 165 ? 23.528 -14.407 -73.499 1.00 30.31  ? 164 MET D SD  1 
ATOM   6384 C CE  . MET E 5 165 ? 25.214 -14.803 -73.959 1.00 25.52  ? 164 MET D CE  1 
ATOM   6385 N N   . ARG E 5 166 ? 25.956 -9.440  -70.038 1.00 30.13  ? 165 ARG D N   1 
ATOM   6386 C CA  . ARG E 5 166 ? 26.309 -8.029  -69.892 1.00 34.56  ? 165 ARG D CA  1 
ATOM   6387 C C   . ARG E 5 166 ? 27.079 -7.501  -71.099 1.00 37.58  ? 165 ARG D C   1 
ATOM   6388 O O   . ARG E 5 166 ? 26.736 -6.450  -71.648 1.00 41.72  ? 165 ARG D O   1 
ATOM   6389 C CB  . ARG E 5 166 ? 27.132 -7.825  -68.612 1.00 35.13  ? 165 ARG D CB  1 
ATOM   6390 C CG  . ARG E 5 166 ? 26.360 -8.055  -67.317 1.00 36.70  ? 165 ARG D CG  1 
ATOM   6391 C CD  . ARG E 5 166 ? 27.325 -8.237  -66.147 1.00 42.27  ? 165 ARG D CD  1 
ATOM   6392 N NE  . ARG E 5 166 ? 26.693 -8.785  -64.951 1.00 42.57  ? 165 ARG D NE  1 
ATOM   6393 C CZ  . ARG E 5 166 ? 27.368 -9.263  -63.903 1.00 43.48  ? 165 ARG D CZ  1 
ATOM   6394 N NH1 . ARG E 5 166 ? 28.697 -9.258  -63.909 1.00 41.18  ? 165 ARG D NH1 1 
ATOM   6395 N NH2 . ARG E 5 166 ? 26.718 -9.760  -62.850 1.00 36.01  ? 165 ARG D NH2 1 
ATOM   6396 N N   . SER E 5 167 ? 28.136 -8.205  -71.514 1.00 37.03  ? 166 SER D N   1 
ATOM   6397 C CA  . SER E 5 167 ? 28.959 -7.775  -72.643 1.00 37.36  ? 166 SER D CA  1 
ATOM   6398 C C   . SER E 5 167 ? 28.171 -7.626  -73.942 1.00 45.23  ? 166 SER D C   1 
ATOM   6399 O O   . SER E 5 167 ? 28.625 -6.918  -74.848 1.00 45.64  ? 166 SER D O   1 
ATOM   6400 C CB  . SER E 5 167 ? 30.090 -8.773  -72.879 1.00 39.36  ? 166 SER D CB  1 
ATOM   6401 O OG  . SER E 5 167 ? 29.548 -10.044 -73.195 1.00 43.57  ? 166 SER D OG  1 
ATOM   6402 N N   . MET E 5 168 ? 27.027 -8.293  -74.070 1.00 43.27  ? 167 MET D N   1 
ATOM   6403 C CA  . MET E 5 168 ? 26.204 -8.209  -75.268 1.00 44.24  ? 167 MET D CA  1 
ATOM   6404 C C   . MET E 5 168 ? 24.978 -7.322  -75.077 1.00 44.70  ? 167 MET D C   1 
ATOM   6405 O O   . MET E 5 168 ? 24.224 -7.118  -76.033 1.00 43.54  ? 167 MET D O   1 
ATOM   6406 C CB  . MET E 5 168 ? 25.764 -9.612  -75.708 1.00 41.68  ? 167 MET D CB  1 
ATOM   6407 C CG  . MET E 5 168 ? 26.760 -10.336 -76.616 1.00 53.74  ? 167 MET D CG  1 
ATOM   6408 S SD  . MET E 5 168 ? 26.585 -12.142 -76.534 1.00 68.14  ? 167 MET D SD  1 
ATOM   6409 C CE  . MET E 5 168 ? 25.747 -12.530 -78.081 1.00 55.55  ? 167 MET D CE  1 
ATOM   6410 N N   . ASP E 5 169 ? 24.769 -6.785  -73.873 1.00 45.91  ? 168 ASP D N   1 
ATOM   6411 C CA  . ASP E 5 169 ? 23.589 -5.978  -73.573 1.00 44.75  ? 168 ASP D CA  1 
ATOM   6412 C C   . ASP E 5 169 ? 22.318 -6.743  -73.955 1.00 43.39  ? 168 ASP D C   1 
ATOM   6413 O O   . ASP E 5 169 ? 21.436 -6.242  -74.657 1.00 49.65  ? 168 ASP D O   1 
ATOM   6414 C CB  . ASP E 5 169 ? 23.678 -4.623  -74.283 1.00 47.49  ? 168 ASP D CB  1 
ATOM   6415 C CG  . ASP E 5 169 ? 22.500 -3.712  -73.976 1.00 55.24  ? 168 ASP D CG  1 
ATOM   6416 O OD1 . ASP E 5 169 ? 21.909 -3.834  -72.879 1.00 51.62  ? 168 ASP D OD1 1 
ATOM   6417 O OD2 . ASP E 5 169 ? 22.160 -2.883  -74.853 1.00 62.76  ? 168 ASP D OD2 1 
ATOM   6418 N N   . PHE E 5 170 ? 22.243 -7.994  -73.502 1.00 37.26  ? 169 PHE D N   1 
ATOM   6419 C CA  . PHE E 5 170 ? 21.187 -8.915  -73.900 1.00 37.71  ? 169 PHE D CA  1 
ATOM   6420 C C   . PHE E 5 170 ? 20.566 -9.572  -72.674 1.00 33.96  ? 169 PHE D C   1 
ATOM   6421 O O   . PHE E 5 170 ? 21.268 -10.230 -71.900 1.00 32.61  ? 169 PHE D O   1 
ATOM   6422 C CB  . PHE E 5 170 ? 21.732 -9.998  -74.850 1.00 32.60  ? 169 PHE D CB  1 
ATOM   6423 C CG  . PHE E 5 170 ? 20.726 -11.050 -75.200 1.00 33.03  ? 169 PHE D CG  1 
ATOM   6424 C CD1 . PHE E 5 170 ? 20.560 -12.182 -74.391 1.00 32.79  ? 169 PHE D CD1 1 
ATOM   6425 C CD2 . PHE E 5 170 ? 19.933 -10.917 -76.336 1.00 35.70  ? 169 PHE D CD2 1 
ATOM   6426 C CE1 . PHE E 5 170 ? 19.612 -13.153 -74.698 1.00 29.02  ? 169 PHE D CE1 1 
ATOM   6427 C CE2 . PHE E 5 170 ? 18.990 -11.892 -76.658 1.00 32.70  ? 169 PHE D CE2 1 
ATOM   6428 C CZ  . PHE E 5 170 ? 18.832 -13.010 -75.831 1.00 33.17  ? 169 PHE D CZ  1 
ATOM   6429 N N   . LYS E 5 171 ? 19.246 -9.446  -72.531 1.00 31.55  ? 170 LYS D N   1 
ATOM   6430 C CA  . LYS E 5 171 ? 18.519 -10.050 -71.421 1.00 31.13  ? 170 LYS D CA  1 
ATOM   6431 C C   . LYS E 5 171 ? 17.484 -11.043 -71.943 1.00 33.19  ? 170 LYS D C   1 
ATOM   6432 O O   . LYS E 5 171 ? 16.926 -10.870 -73.031 1.00 34.34  ? 170 LYS D O   1 
ATOM   6433 C CB  . LYS E 5 171 ? 17.851 -8.974  -70.565 1.00 32.30  ? 170 LYS D CB  1 
ATOM   6434 C CG  . LYS E 5 171 ? 18.861 -8.189  -69.699 1.00 37.15  ? 170 LYS D CG  1 
ATOM   6435 C CD  . LYS E 5 171 ? 18.762 -6.690  -69.913 1.00 39.39  ? 170 LYS D CD  1 
ATOM   6436 C CE  . LYS E 5 171 ? 20.121 -6.022  -69.873 1.00 44.49  ? 170 LYS D CE  1 
ATOM   6437 N NZ  . LYS E 5 171 ? 20.138 -4.786  -70.728 1.00 50.96  ? 170 LYS D NZ  1 
ATOM   6438 N N   . SER E 5 172 ? 17.248 -12.097 -71.164 1.00 29.46  ? 171 SER D N   1 
ATOM   6439 C CA  . SER E 5 172 ? 16.283 -13.122 -71.521 1.00 29.14  ? 171 SER D CA  1 
ATOM   6440 C C   . SER E 5 172 ? 15.760 -13.793 -70.257 1.00 33.32  ? 171 SER D C   1 
ATOM   6441 O O   . SER E 5 172 ? 16.482 -13.937 -69.264 1.00 30.78  ? 171 SER D O   1 
ATOM   6442 C CB  . SER E 5 172 ? 16.889 -14.169 -72.473 1.00 28.06  ? 171 SER D CB  1 
ATOM   6443 O OG  . SER E 5 172 ? 17.968 -14.874 -71.881 1.00 34.38  ? 171 SER D OG  1 
ATOM   6444 N N   . ASN E 5 173 ? 14.483 -14.175 -70.307 1.00 33.66  ? 172 ASN D N   1 
ATOM   6445 C CA  . ASN E 5 173 ? 13.792 -14.937 -69.279 1.00 26.53  ? 172 ASN D CA  1 
ATOM   6446 C C   . ASN E 5 173 ? 13.875 -16.432 -69.568 1.00 31.40  ? 172 ASN D C   1 
ATOM   6447 O O   . ASN E 5 173 ? 14.092 -16.861 -70.703 1.00 29.64  ? 172 ASN D O   1 
ATOM   6448 C CB  . ASN E 5 173 ? 12.327 -14.525 -69.194 1.00 31.30  ? 172 ASN D CB  1 
ATOM   6449 C CG  . ASN E 5 173 ? 12.149 -13.075 -68.823 1.00 35.06  ? 172 ASN D CG  1 
ATOM   6450 O OD1 . ASN E 5 173 ? 12.694 -12.601 -67.815 1.00 35.58  ? 172 ASN D OD1 1 
ATOM   6451 N ND2 . ASN E 5 173 ? 11.378 -12.355 -69.627 1.00 30.94  ? 172 ASN D ND2 1 
ATOM   6452 N N   . SER E 5 174 ? 13.697 -17.227 -68.517 1.00 27.89  ? 173 SER D N   1 
ATOM   6453 C CA  . SER E 5 174 ? 13.699 -18.672 -68.670 1.00 28.24  ? 173 SER D CA  1 
ATOM   6454 C C   . SER E 5 174 ? 13.078 -19.322 -67.441 1.00 33.45  ? 173 SER D C   1 
ATOM   6455 O O   . SER E 5 174 ? 13.052 -18.748 -66.345 1.00 33.19  ? 173 SER D O   1 
ATOM   6456 C CB  . SER E 5 174 ? 15.115 -19.235 -68.920 1.00 31.09  ? 173 SER D CB  1 
ATOM   6457 O OG  . SER E 5 174 ? 15.916 -19.282 -67.746 1.00 33.17  ? 173 SER D OG  1 
ATOM   6458 N N   . ALA E 5 175 ? 12.549 -20.518 -67.662 1.00 31.52  ? 174 ALA D N   1 
ATOM   6459 C CA  . ALA E 5 175 ? 12.098 -21.404 -66.610 1.00 31.39  ? 174 ALA D CA  1 
ATOM   6460 C C   . ALA E 5 175 ? 12.579 -22.792 -66.982 1.00 29.22  ? 174 ALA D C   1 
ATOM   6461 O O   . ALA E 5 175 ? 12.848 -23.078 -68.152 1.00 30.63  ? 174 ALA D O   1 
ATOM   6462 C CB  . ALA E 5 175 ? 10.572 -21.372 -66.439 1.00 33.97  ? 174 ALA D CB  1 
ATOM   6463 N N   . VAL E 5 176 ? 12.699 -23.650 -65.981 1.00 28.27  ? 175 VAL D N   1 
ATOM   6464 C CA  . VAL E 5 176 ? 13.222 -24.995 -66.161 1.00 28.29  ? 175 VAL D CA  1 
ATOM   6465 C C   . VAL E 5 176 ? 12.176 -25.976 -65.665 1.00 31.81  ? 175 VAL D C   1 
ATOM   6466 O O   . VAL E 5 176 ? 11.557 -25.748 -64.622 1.00 33.10  ? 175 VAL D O   1 
ATOM   6467 C CB  . VAL E 5 176 ? 14.557 -25.177 -65.403 1.00 34.15  ? 175 VAL D CB  1 
ATOM   6468 C CG1 . VAL E 5 176 ? 15.000 -26.637 -65.424 1.00 32.98  ? 175 VAL D CG1 1 
ATOM   6469 C CG2 . VAL E 5 176 ? 15.626 -24.271 -65.988 1.00 27.48  ? 175 VAL D CG2 1 
ATOM   6470 N N   . ALA E 5 177 ? 11.976 -27.069 -66.409 1.00 32.56  ? 176 ALA D N   1 
ATOM   6471 C CA  . ALA E 5 177 ? 11.116 -28.150 -65.950 1.00 30.50  ? 176 ALA D CA  1 
ATOM   6472 C C   . ALA E 5 177 ? 11.816 -29.488 -66.126 1.00 30.91  ? 176 ALA D C   1 
ATOM   6473 O O   . ALA E 5 177 ? 12.571 -29.688 -67.081 1.00 34.06  ? 176 ALA D O   1 
ATOM   6474 C CB  . ALA E 5 177 ? 9.779  -28.174 -66.686 1.00 33.86  ? 176 ALA D CB  1 
ATOM   6475 N N   . TRP E 5 178 ? 11.556 -30.410 -65.201 1.00 31.37  ? 177 TRP D N   1 
ATOM   6476 C CA  . TRP E 5 178 ? 12.145 -31.736 -65.308 1.00 36.45  ? 177 TRP D CA  1 
ATOM   6477 C C   . TRP E 5 178 ? 11.272 -32.752 -64.582 1.00 41.08  ? 177 TRP D C   1 
ATOM   6478 O O   . TRP E 5 178 ? 10.347 -32.399 -63.844 1.00 40.85  ? 177 TRP D O   1 
ATOM   6479 C CB  . TRP E 5 178 ? 13.581 -31.746 -64.775 1.00 32.79  ? 177 TRP D CB  1 
ATOM   6480 C CG  . TRP E 5 178 ? 13.703 -31.587 -63.295 1.00 32.91  ? 177 TRP D CG  1 
ATOM   6481 C CD1 . TRP E 5 178 ? 13.784 -32.586 -62.369 1.00 32.45  ? 177 TRP D CD1 1 
ATOM   6482 C CD2 . TRP E 5 178 ? 13.783 -30.355 -62.565 1.00 30.87  ? 177 TRP D CD2 1 
ATOM   6483 N NE1 . TRP E 5 178 ? 13.907 -32.056 -61.110 1.00 37.85  ? 177 TRP D NE1 1 
ATOM   6484 C CE2 . TRP E 5 178 ? 13.913 -30.687 -61.202 1.00 36.79  ? 177 TRP D CE2 1 
ATOM   6485 C CE3 . TRP E 5 178 ? 13.761 -29.010 -62.932 1.00 28.49  ? 177 TRP D CE3 1 
ATOM   6486 C CZ2 . TRP E 5 178 ? 14.010 -29.714 -60.198 1.00 33.57  ? 177 TRP D CZ2 1 
ATOM   6487 C CZ3 . TRP E 5 178 ? 13.860 -28.042 -61.937 1.00 29.70  ? 177 TRP D CZ3 1 
ATOM   6488 C CH2 . TRP E 5 178 ? 13.982 -28.400 -60.589 1.00 30.04  ? 177 TRP D CH2 1 
ATOM   6489 N N   . SER E 5 179 ? 11.583 -34.031 -64.804 1.00 41.01  ? 178 SER D N   1 
ATOM   6490 C CA  . SER E 5 179 ? 10.799 -35.126 -64.253 1.00 42.65  ? 178 SER D CA  1 
ATOM   6491 C C   . SER E 5 179 ? 11.574 -36.429 -64.388 1.00 53.42  ? 178 SER D C   1 
ATOM   6492 O O   . SER E 5 179 ? 12.503 -36.547 -65.196 1.00 56.91  ? 178 SER D O   1 
ATOM   6493 C CB  . SER E 5 179 ? 9.436  -35.250 -64.948 1.00 45.86  ? 178 SER D CB  1 
ATOM   6494 O OG  . SER E 5 179 ? 8.703  -36.359 -64.434 1.00 46.94  ? 178 SER D OG  1 
ATOM   6495 N N   . ASN E 5 180 ? 11.173 -37.409 -63.571 1.00 51.70  ? 179 ASN D N   1 
ATOM   6496 C CA  . ASN E 5 180 ? 11.651 -38.781 -63.674 1.00 57.22  ? 179 ASN D CA  1 
ATOM   6497 C C   . ASN E 5 180 ? 10.755 -39.644 -64.547 1.00 52.99  ? 179 ASN D C   1 
ATOM   6498 O O   . ASN E 5 180 ? 11.190 -40.708 -64.995 1.00 59.41  ? 179 ASN D O   1 
ATOM   6499 C CB  . ASN E 5 180 ? 11.736 -39.423 -62.284 1.00 52.03  ? 179 ASN D CB  1 
ATOM   6500 C CG  . ASN E 5 180 ? 12.811 -38.801 -61.418 1.00 63.09  ? 179 ASN D CG  1 
ATOM   6501 O OD1 . ASN E 5 180 ? 13.914 -38.527 -61.888 1.00 68.56  ? 179 ASN D OD1 1 
ATOM   6502 N ND2 . ASN E 5 180 ? 12.496 -38.573 -60.142 1.00 64.73  ? 179 ASN D ND2 1 
ATOM   6503 N N   . LYS E 5 181 ? 9.521  -39.197 -64.781 1.00 56.49  ? 180 LYS D N   1 
ATOM   6504 C CA  . LYS E 5 181 ? 8.516  -39.961 -65.508 1.00 57.83  ? 180 LYS D CA  1 
ATOM   6505 C C   . LYS E 5 181 ? 9.067  -40.487 -66.829 1.00 63.44  ? 180 LYS D C   1 
ATOM   6506 O O   . LYS E 5 181 ? 9.978  -39.901 -67.428 1.00 61.76  ? 180 LYS D O   1 
ATOM   6507 C CB  . LYS E 5 181 ? 7.293  -39.077 -65.781 1.00 62.33  ? 180 LYS D CB  1 
ATOM   6508 C CG  . LYS E 5 181 ? 6.152  -39.147 -64.765 1.00 58.54  ? 180 LYS D CG  1 
ATOM   6509 C CD  . LYS E 5 181 ? 5.132  -38.046 -65.079 1.00 65.25  ? 180 LYS D CD  1 
ATOM   6510 C CE  . LYS E 5 181 ? 3.688  -38.511 -64.913 1.00 72.03  ? 180 LYS D CE  1 
ATOM   6511 N NZ  . LYS E 5 181 ? 3.291  -39.531 -65.932 1.00 68.61  ? 180 LYS D NZ  1 
ATOM   6512 N N   . SER E 5 182 ? 8.492  -41.606 -67.285 1.00 66.93  ? 181 SER D N   1 
ATOM   6513 C CA  . SER E 5 182 ? 8.838  -42.148 -68.598 1.00 64.70  ? 181 SER D CA  1 
ATOM   6514 C C   . SER E 5 182 ? 8.214  -41.327 -69.722 1.00 60.15  ? 181 SER D C   1 
ATOM   6515 O O   . SER E 5 182 ? 8.862  -41.066 -70.743 1.00 58.78  ? 181 SER D O   1 
ATOM   6516 C CB  . SER E 5 182 ? 8.390  -43.606 -68.698 1.00 59.25  ? 181 SER D CB  1 
ATOM   6517 O OG  . SER E 5 182 ? 8.991  -44.401 -67.690 1.00 66.70  ? 181 SER D OG  1 
ATOM   6518 N N   . ASP E 5 183 ? 6.958  -40.921 -69.548 1.00 60.06  ? 182 ASP D N   1 
ATOM   6519 C CA  . ASP E 5 183 ? 6.171  -40.216 -70.551 1.00 60.03  ? 182 ASP D CA  1 
ATOM   6520 C C   . ASP E 5 183 ? 6.460  -38.723 -70.615 1.00 58.09  ? 182 ASP D C   1 
ATOM   6521 O O   . ASP E 5 183 ? 5.722  -38.005 -71.300 1.00 61.08  ? 182 ASP D O   1 
ATOM   6522 C CB  . ASP E 5 183 ? 4.685  -40.417 -70.254 1.00 60.87  ? 182 ASP D CB  1 
ATOM   6523 C CG  . ASP E 5 183 ? 4.330  -40.021 -68.830 1.00 68.72  ? 182 ASP D CG  1 
ATOM   6524 O OD1 . ASP E 5 183 ? 5.219  -39.482 -68.133 1.00 66.99  ? 182 ASP D OD1 1 
ATOM   6525 O OD2 . ASP E 5 183 ? 3.178  -40.253 -68.400 1.00 70.32  ? 182 ASP D OD2 1 
ATOM   6526 N N   . PHE E 5 184 ? 7.469  -38.228 -69.902 1.00 55.26  ? 183 PHE D N   1 
ATOM   6527 C CA  . PHE E 5 184 ? 7.663  -36.788 -69.798 1.00 52.01  ? 183 PHE D CA  1 
ATOM   6528 C C   . PHE E 5 184 ? 8.322  -36.247 -71.057 1.00 41.83  ? 183 PHE D C   1 
ATOM   6529 O O   . PHE E 5 184 ? 9.392  -36.708 -71.459 1.00 42.07  ? 183 PHE D O   1 
ATOM   6530 C CB  . PHE E 5 184 ? 8.504  -36.429 -68.572 1.00 52.30  ? 183 PHE D CB  1 
ATOM   6531 C CG  . PHE E 5 184 ? 8.651  -34.945 -68.367 1.00 47.10  ? 183 PHE D CG  1 
ATOM   6532 C CD1 . PHE E 5 184 ? 7.540  -34.164 -68.082 1.00 42.53  ? 183 PHE D CD1 1 
ATOM   6533 C CD2 . PHE E 5 184 ? 9.890  -34.329 -68.480 1.00 47.90  ? 183 PHE D CD2 1 
ATOM   6534 C CE1 . PHE E 5 184 ? 7.657  -32.802 -67.898 1.00 42.09  ? 183 PHE D CE1 1 
ATOM   6535 C CE2 . PHE E 5 184 ? 10.016 -32.955 -68.292 1.00 46.45  ? 183 PHE D CE2 1 
ATOM   6536 C CZ  . PHE E 5 184 ? 8.898  -32.194 -68.001 1.00 38.31  ? 183 PHE D CZ  1 
ATOM   6537 N N   . ALA E 5 185 ? 7.693  -35.248 -71.662 1.00 43.04  ? 184 ALA D N   1 
ATOM   6538 C CA  . ALA E 5 185 ? 8.197  -34.671 -72.895 1.00 42.85  ? 184 ALA D CA  1 
ATOM   6539 C C   . ALA E 5 185 ? 8.057  -33.163 -72.831 1.00 41.72  ? 184 ALA D C   1 
ATOM   6540 O O   . ALA E 5 185 ? 7.168  -32.635 -72.159 1.00 40.09  ? 184 ALA D O   1 
ATOM   6541 C CB  . ALA E 5 185 ? 7.462  -35.218 -74.115 1.00 39.34  ? 184 ALA D CB  1 
ATOM   6542 N N   . CYS E 5 186 ? 8.951  -32.473 -73.541 1.00 42.79  ? 185 CYS D N   1 
ATOM   6543 C CA  . CYS E 5 186 ? 8.984  -31.017 -73.474 1.00 41.10  ? 185 CYS D CA  1 
ATOM   6544 C C   . CYS E 5 186 ? 7.789  -30.376 -74.168 1.00 42.50  ? 185 CYS D C   1 
ATOM   6545 O O   . CYS E 5 186 ? 7.432  -29.243 -73.832 1.00 41.59  ? 185 CYS D O   1 
ATOM   6546 C CB  . CYS E 5 186 ? 10.305 -30.502 -74.063 1.00 40.44  ? 185 CYS D CB  1 
ATOM   6547 S SG  . CYS E 5 186 ? 11.786 -31.091 -73.155 1.00 51.54  ? 185 CYS D SG  1 
ATOM   6548 N N   . ALA E 5 187 ? 7.146  -31.076 -75.108 1.00 43.41  ? 186 ALA D N   1 
ATOM   6549 C CA  . ALA E 5 187 ? 5.916  -30.547 -75.699 1.00 42.51  ? 186 ALA D CA  1 
ATOM   6550 C C   . ALA E 5 187 ? 4.817  -30.379 -74.657 1.00 45.91  ? 186 ALA D C   1 
ATOM   6551 O O   . ALA E 5 187 ? 4.007  -29.447 -74.747 1.00 48.52  ? 186 ALA D O   1 
ATOM   6552 C CB  . ALA E 5 187 ? 5.438  -31.465 -76.825 1.00 47.41  ? 186 ALA D CB  1 
ATOM   6553 N N   . ASN E 5 188 ? 4.781  -31.257 -73.653 1.00 46.08  ? 187 ASN D N   1 
ATOM   6554 C CA  . ASN E 5 188 ? 3.776  -31.207 -72.601 1.00 47.93  ? 187 ASN D CA  1 
ATOM   6555 C C   . ASN E 5 188 ? 4.246  -30.467 -71.355 1.00 46.62  ? 187 ASN D C   1 
ATOM   6556 O O   . ASN E 5 188 ? 3.408  -30.123 -70.516 1.00 49.89  ? 187 ASN D O   1 
ATOM   6557 C CB  . ASN E 5 188 ? 3.352  -32.632 -72.197 1.00 51.93  ? 187 ASN D CB  1 
ATOM   6558 C CG  . ASN E 5 188 ? 2.662  -33.395 -73.328 1.00 56.70  ? 187 ASN D CG  1 
ATOM   6559 O OD1 . ASN E 5 188 ? 2.040  -32.802 -74.217 1.00 53.35  ? 187 ASN D OD1 1 
ATOM   6560 N ND2 . ASN E 5 188 ? 2.761  -34.723 -73.286 1.00 52.27  ? 187 ASN D ND2 1 
ATOM   6561 N N   . ALA E 5 189 ? 5.552  -30.213 -71.224 1.00 45.64  ? 188 ALA D N   1 
ATOM   6562 C CA  . ALA E 5 189 ? 6.126  -29.756 -69.957 1.00 42.11  ? 188 ALA D CA  1 
ATOM   6563 C C   . ALA E 5 189 ? 5.404  -28.528 -69.405 1.00 35.69  ? 188 ALA D C   1 
ATOM   6564 O O   . ALA E 5 189 ? 4.982  -28.516 -68.245 1.00 41.80  ? 188 ALA D O   1 
ATOM   6565 C CB  . ALA E 5 189 ? 7.626  -29.475 -70.130 1.00 34.59  ? 188 ALA D CB  1 
ATOM   6566 N N   . PHE E 5 190 ? 5.239  -27.490 -70.221 1.00 36.99  ? 189 PHE D N   1 
ATOM   6567 C CA  . PHE E 5 190 ? 4.628  -26.241 -69.776 1.00 40.84  ? 189 PHE D CA  1 
ATOM   6568 C C   . PHE E 5 190 ? 3.143  -26.147 -70.151 1.00 48.56  ? 189 PHE D C   1 
ATOM   6569 O O   . PHE E 5 190 ? 2.627  -25.050 -70.397 1.00 47.72  ? 189 PHE D O   1 
ATOM   6570 C CB  . PHE E 5 190 ? 5.438  -25.062 -70.327 1.00 44.26  ? 189 PHE D CB  1 
ATOM   6571 C CG  . PHE E 5 190 ? 6.897  -25.095 -69.902 1.00 41.73  ? 189 PHE D CG  1 
ATOM   6572 C CD1 . PHE E 5 190 ? 7.304  -24.499 -68.712 1.00 34.49  ? 189 PHE D CD1 1 
ATOM   6573 C CD2 . PHE E 5 190 ? 7.847  -25.770 -70.662 1.00 33.97  ? 189 PHE D CD2 1 
ATOM   6574 C CE1 . PHE E 5 190 ? 8.635  -24.544 -68.306 1.00 35.61  ? 189 PHE D CE1 1 
ATOM   6575 C CE2 . PHE E 5 190 ? 9.182  -25.830 -70.250 1.00 34.48  ? 189 PHE D CE2 1 
ATOM   6576 C CZ  . PHE E 5 190 ? 9.571  -25.212 -69.064 1.00 35.35  ? 189 PHE D CZ  1 
ATOM   6577 N N   . ASN E 5 191 ? 2.437  -27.290 -70.152 1.00 51.76  ? 190 ASN D N   1 
ATOM   6578 C CA  . ASN E 5 191 ? 1.042  -27.336 -70.591 1.00 52.51  ? 190 ASN D CA  1 
ATOM   6579 C C   . ASN E 5 191 ? 0.137  -26.459 -69.741 1.00 53.72  ? 190 ASN D C   1 
ATOM   6580 O O   . ASN E 5 191 ? -0.841 -25.905 -70.254 1.00 62.33  ? 190 ASN D O   1 
ATOM   6581 C CB  . ASN E 5 191 ? 0.529  -28.777 -70.564 1.00 50.24  ? 190 ASN D CB  1 
ATOM   6582 C CG  . ASN E 5 191 ? 0.602  -29.453 -71.928 1.00 57.71  ? 190 ASN D CG  1 
ATOM   6583 O OD1 . ASN E 5 191 ? 1.104  -28.873 -72.897 1.00 56.55  ? 190 ASN D OD1 1 
ATOM   6584 N ND2 . ASN E 5 191 ? 0.119  -30.697 -72.003 1.00 58.87  ? 190 ASN D ND2 1 
ATOM   6585 N N   . ASN E 5 192 ? 0.435  -26.315 -68.453 1.00 52.72  ? 191 ASN D N   1 
ATOM   6586 C CA  . ASN E 5 192 ? -0.436 -25.587 -67.543 1.00 49.15  ? 191 ASN D CA  1 
ATOM   6587 C C   . ASN E 5 192 ? -0.134 -24.092 -67.482 1.00 52.48  ? 191 ASN D C   1 
ATOM   6588 O O   . ASN E 5 192 ? -0.699 -23.393 -66.630 1.00 52.82  ? 191 ASN D O   1 
ATOM   6589 C CB  . ASN E 5 192 ? -0.351 -26.199 -66.151 1.00 54.23  ? 191 ASN D CB  1 
ATOM   6590 C CG  . ASN E 5 192 ? -1.686 -26.208 -65.435 1.00 61.37  ? 191 ASN D CG  1 
ATOM   6591 O OD1 . ASN E 5 192 ? -2.702 -25.771 -65.983 1.00 64.00  ? 191 ASN D OD1 1 
ATOM   6592 N ND2 . ASN E 5 192 ? -1.691 -26.696 -64.200 1.00 66.20  ? 191 ASN D ND2 1 
ATOM   6593 N N   . SER E 5 193 ? 0.724  -23.585 -68.363 1.00 50.70  ? 192 SER D N   1 
ATOM   6594 C CA  . SER E 5 193 ? 0.982  -22.158 -68.480 1.00 51.51  ? 192 SER D CA  1 
ATOM   6595 C C   . SER E 5 193 ? 0.410  -21.647 -69.796 1.00 50.21  ? 192 SER D C   1 
ATOM   6596 O O   . SER E 5 193 ? 0.337  -22.385 -70.782 1.00 52.21  ? 192 SER D O   1 
ATOM   6597 C CB  . SER E 5 193 ? 2.485  -21.849 -68.426 1.00 47.45  ? 192 SER D CB  1 
ATOM   6598 O OG  . SER E 5 193 ? 3.118  -22.446 -67.313 1.00 46.98  ? 192 SER D OG  1 
ATOM   6599 N N   . ILE E 5 194 ? 0.001  -20.380 -69.807 1.00 50.57  ? 193 ILE D N   1 
ATOM   6600 C CA  . ILE E 5 194 ? -0.389 -19.713 -71.048 1.00 52.58  ? 193 ILE D CA  1 
ATOM   6601 C C   . ILE E 5 194 ? 0.875  -19.157 -71.696 1.00 51.88  ? 193 ILE D C   1 
ATOM   6602 O O   . ILE E 5 194 ? 1.435  -18.157 -71.238 1.00 46.31  ? 193 ILE D O   1 
ATOM   6603 C CB  . ILE E 5 194 ? -1.426 -18.606 -70.814 1.00 52.55  ? 193 ILE D CB  1 
ATOM   6604 C CG1 . ILE E 5 194 ? -2.728 -19.199 -70.271 1.00 54.03  ? 193 ILE D CG1 1 
ATOM   6605 C CG2 . ILE E 5 194 ? -1.716 -17.856 -72.120 1.00 49.09  ? 193 ILE D CG2 1 
ATOM   6606 C CD1 . ILE E 5 194 ? -3.345 -18.400 -69.108 1.00 59.70  ? 193 ILE D CD1 1 
ATOM   6607 N N   . ILE E 5 195 ? 1.321  -19.806 -72.768 1.00 46.94  ? 194 ILE D N   1 
ATOM   6608 C CA  . ILE E 5 195 ? 2.574  -19.456 -73.433 1.00 47.13  ? 194 ILE D CA  1 
ATOM   6609 C C   . ILE E 5 195 ? 2.246  -18.885 -74.810 1.00 50.47  ? 194 ILE D C   1 
ATOM   6610 O O   . ILE E 5 195 ? 1.158  -19.153 -75.337 1.00 48.12  ? 194 ILE D O   1 
ATOM   6611 C CB  . ILE E 5 195 ? 3.500  -20.678 -73.506 1.00 48.15  ? 194 ILE D CB  1 
ATOM   6612 C CG1 . ILE E 5 195 ? 2.877  -21.757 -74.386 1.00 49.21  ? 194 ILE D CG1 1 
ATOM   6613 C CG2 . ILE E 5 195 ? 3.704  -21.259 -72.105 1.00 47.34  ? 194 ILE D CG2 1 
ATOM   6614 C CD1 . ILE E 5 195 ? 3.730  -22.994 -74.513 1.00 43.09  ? 194 ILE D CD1 1 
ATOM   6615 N N   . PRO E 5 196 ? 3.123  -18.086 -75.421 1.00 49.97  ? 195 PRO D N   1 
ATOM   6616 C CA  . PRO E 5 196 ? 2.788  -17.480 -76.716 1.00 50.03  ? 195 PRO D CA  1 
ATOM   6617 C C   . PRO E 5 196 ? 2.375  -18.527 -77.748 1.00 52.27  ? 195 PRO D C   1 
ATOM   6618 O O   . PRO E 5 196 ? 2.752  -19.699 -77.666 1.00 48.76  ? 195 PRO D O   1 
ATOM   6619 C CB  . PRO E 5 196 ? 4.087  -16.774 -77.118 1.00 49.64  ? 195 PRO D CB  1 
ATOM   6620 C CG  . PRO E 5 196 ? 4.766  -16.469 -75.816 1.00 44.84  ? 195 PRO D CG  1 
ATOM   6621 C CD  . PRO E 5 196 ? 4.414  -17.601 -74.897 1.00 46.64  ? 195 PRO D CD  1 
ATOM   6622 N N   . GLU E 5 197 ? 1.570  -18.093 -78.721 1.00 55.48  ? 196 GLU D N   1 
ATOM   6623 C CA  . GLU E 5 197 ? 1.106  -19.013 -79.760 1.00 52.08  ? 196 GLU D CA  1 
ATOM   6624 C C   . GLU E 5 197 ? 2.230  -19.404 -80.713 1.00 47.13  ? 196 GLU D C   1 
ATOM   6625 O O   . GLU E 5 197 ? 2.252  -20.533 -81.210 1.00 47.19  ? 196 GLU D O   1 
ATOM   6626 C CB  . GLU E 5 197 ? -0.058 -18.388 -80.531 1.00 60.45  ? 196 GLU D CB  1 
ATOM   6627 C CG  . GLU E 5 197 ? -1.274 -18.044 -79.665 1.00 62.90  ? 196 GLU D CG  1 
ATOM   6628 C CD  . GLU E 5 197 ? -1.301 -16.579 -79.228 1.00 72.70  ? 196 GLU D CD  1 
ATOM   6629 O OE1 . GLU E 5 197 ? -0.478 -16.189 -78.364 1.00 66.36  ? 196 GLU D OE1 1 
ATOM   6630 O OE2 . GLU E 5 197 ? -2.143 -15.815 -79.756 1.00 73.24  ? 196 GLU D OE2 1 
ATOM   6631 N N   . ASP E 5 198 ? 3.180  -18.500 -80.957 1.00 45.76  ? 197 ASP D N   1 
ATOM   6632 C CA  . ASP E 5 198 ? 4.320  -18.736 -81.837 1.00 49.20  ? 197 ASP D CA  1 
ATOM   6633 C C   . ASP E 5 198 ? 5.537  -19.324 -81.111 1.00 50.28  ? 197 ASP D C   1 
ATOM   6634 O O   . ASP E 5 198 ? 6.677  -19.060 -81.528 1.00 52.66  ? 197 ASP D O   1 
ATOM   6635 C CB  . ASP E 5 198 ? 4.705  -17.425 -82.532 1.00 47.94  ? 197 ASP D CB  1 
ATOM   6636 C CG  . ASP E 5 198 ? 4.668  -16.226 -81.575 1.00 59.28  ? 197 ASP D CG  1 
ATOM   6637 O OD1 . ASP E 5 198 ? 3.946  -16.299 -80.551 1.00 53.23  ? 197 ASP D OD1 1 
ATOM   6638 O OD2 . ASP E 5 198 ? 5.359  -15.213 -81.838 1.00 59.56  ? 197 ASP D OD2 1 
ATOM   6639 N N   . THR E 5 199 ? 5.337  -20.109 -80.045 1.00 41.56  ? 198 THR D N   1 
ATOM   6640 C CA  . THR E 5 199 ? 6.457  -20.701 -79.314 1.00 38.78  ? 198 THR D CA  1 
ATOM   6641 C C   . THR E 5 199 ? 7.106  -21.808 -80.145 1.00 43.20  ? 198 THR D C   1 
ATOM   6642 O O   . THR E 5 199 ? 6.450  -22.787 -80.523 1.00 41.18  ? 198 THR D O   1 
ATOM   6643 C CB  . THR E 5 199 ? 5.999  -21.254 -77.959 1.00 41.36  ? 198 THR D CB  1 
ATOM   6644 O OG1 . THR E 5 199 ? 5.696  -20.179 -77.056 1.00 41.32  ? 198 THR D OG1 1 
ATOM   6645 C CG2 . THR E 5 199 ? 7.083  -22.110 -77.339 1.00 36.64  ? 198 THR D CG2 1 
ATOM   6646 N N   . PHE E 5 200 ? 8.405  -21.666 -80.395 1.00 40.00  ? 199 PHE D N   1 
ATOM   6647 C CA  . PHE E 5 200 ? 9.144  -22.608 -81.227 1.00 37.32  ? 199 PHE D CA  1 
ATOM   6648 C C   . PHE E 5 200 ? 9.333  -23.935 -80.501 1.00 38.58  ? 199 PHE D C   1 
ATOM   6649 O O   . PHE E 5 200 ? 9.942  -23.984 -79.428 1.00 42.43  ? 199 PHE D O   1 
ATOM   6650 C CB  . PHE E 5 200 ? 10.496 -22.001 -81.595 1.00 37.13  ? 199 PHE D CB  1 
ATOM   6651 C CG  . PHE E 5 200 ? 11.376 -22.906 -82.408 1.00 40.94  ? 199 PHE D CG  1 
ATOM   6652 C CD1 . PHE E 5 200 ? 10.916 -23.469 -83.594 1.00 45.19  ? 199 PHE D CD1 1 
ATOM   6653 C CD2 . PHE E 5 200 ? 12.672 -23.170 -82.006 1.00 38.61  ? 199 PHE D CD2 1 
ATOM   6654 C CE1 . PHE E 5 200 ? 11.733 -24.297 -84.362 1.00 43.83  ? 199 PHE D CE1 1 
ATOM   6655 C CE2 . PHE E 5 200 ? 13.500 -23.990 -82.763 1.00 43.80  ? 199 PHE D CE2 1 
ATOM   6656 C CZ  . PHE E 5 200 ? 13.028 -24.555 -83.949 1.00 47.28  ? 199 PHE D CZ  1 
ATOM   6657 N N   . PHE E 5 201 ? 8.822  -25.013 -81.086 1.00 41.82  ? 200 PHE D N   1 
ATOM   6658 C CA  . PHE E 5 201 ? 9.113  -26.365 -80.619 1.00 39.43  ? 200 PHE D CA  1 
ATOM   6659 C C   . PHE E 5 201 ? 9.915  -27.081 -81.695 1.00 45.05  ? 200 PHE D C   1 
ATOM   6660 O O   . PHE E 5 201 ? 9.376  -27.357 -82.779 1.00 53.42  ? 200 PHE D O   1 
ATOM   6661 C CB  . PHE E 5 201 ? 7.825  -27.133 -80.299 1.00 38.67  ? 200 PHE D CB  1 
ATOM   6662 C CG  . PHE E 5 201 ? 7.130  -26.655 -79.049 1.00 40.79  ? 200 PHE D CG  1 
ATOM   6663 C CD1 . PHE E 5 201 ? 6.303  -25.537 -79.078 1.00 40.90  ? 200 PHE D CD1 1 
ATOM   6664 C CD2 . PHE E 5 201 ? 7.305  -27.322 -77.839 1.00 42.38  ? 200 PHE D CD2 1 
ATOM   6665 C CE1 . PHE E 5 201 ? 5.659  -25.088 -77.918 1.00 39.85  ? 200 PHE D CE1 1 
ATOM   6666 C CE2 . PHE E 5 201 ? 6.671  -26.878 -76.677 1.00 43.13  ? 200 PHE D CE2 1 
ATOM   6667 C CZ  . PHE E 5 201 ? 5.850  -25.755 -76.720 1.00 40.53  ? 200 PHE D CZ  1 
ATOM   6668 N N   . PRO E 5 202 ? 11.190 -27.386 -81.453 1.00 45.96  ? 201 PRO D N   1 
ATOM   6669 C CA  . PRO E 5 202 ? 12.046 -27.945 -82.513 1.00 46.12  ? 201 PRO D CA  1 
ATOM   6670 C C   . PRO E 5 202 ? 11.504 -29.231 -83.122 1.00 48.42  ? 201 PRO D C   1 
ATOM   6671 O O   . PRO E 5 202 ? 11.035 -30.130 -82.420 1.00 51.46  ? 201 PRO D O   1 
ATOM   6672 C CB  . PRO E 5 202 ? 13.370 -28.205 -81.790 1.00 44.16  ? 201 PRO D CB  1 
ATOM   6673 C CG  . PRO E 5 202 ? 13.382 -27.209 -80.677 1.00 46.98  ? 201 PRO D CG  1 
ATOM   6674 C CD  . PRO E 5 202 ? 11.955 -26.995 -80.259 1.00 42.17  ? 201 PRO D CD  1 
ATOM   6675 N N   . SER E 5 203 ? 11.630 -29.326 -84.445 1.00 53.79  ? 202 SER D N   1 
ATOM   6676 C CA  . SER E 5 203 ? 11.267 -30.523 -85.202 1.00 55.75  ? 202 SER D CA  1 
ATOM   6677 C C   . SER E 5 203 ? 12.429 -31.511 -85.258 1.00 58.31  ? 202 SER D C   1 
ATOM   6678 O O   . SER E 5 203 ? 12.408 -32.457 -86.050 1.00 56.55  ? 202 SER D O   1 
ATOM   6679 C CB  . SER E 5 203 ? 10.844 -30.153 -86.625 1.00 53.97  ? 202 SER D CB  1 
ATOM   6680 O OG  . SER E 5 203 ? 10.154 -28.916 -86.646 1.00 64.00  ? 202 SER D OG  1 
HETATM 6681 O O   . HOH F 6 .   ? -4.320 24.919  -26.707 1.00 61.16  ? 301 HOH A O   1 
HETATM 6682 O O   . HOH F 6 .   ? -0.992 14.682  -17.631 1.00 41.93  ? 302 HOH A O   1 
HETATM 6683 O O   . HOH F 6 .   ? 35.508 5.539   -9.886  1.00 36.79  ? 303 HOH A O   1 
HETATM 6684 O O   . HOH F 6 .   ? 15.400 34.914  -9.845  1.00 35.58  ? 304 HOH A O   1 
HETATM 6685 O O   . HOH F 6 .   ? 0.295  36.683  -8.280  1.00 48.47  ? 305 HOH A O   1 
HETATM 6686 O O   . HOH F 6 .   ? 14.607 9.598   -24.916 1.00 26.74  ? 306 HOH A O   1 
HETATM 6687 O O   . HOH F 6 .   ? 11.631 17.973  -7.173  1.00 32.58  ? 307 HOH A O   1 
HETATM 6688 O O   . HOH F 6 .   ? 4.018  31.309  -24.930 1.00 48.12  ? 308 HOH A O   1 
HETATM 6689 O O   . HOH F 6 .   ? 14.794 19.681  -8.990  1.00 34.63  ? 309 HOH A O   1 
HETATM 6690 O O   . HOH F 6 .   ? 20.531 0.872   -9.493  1.00 46.67  ? 310 HOH A O   1 
HETATM 6691 O O   . HOH F 6 .   ? 6.826  27.837  -18.092 1.00 34.24  ? 311 HOH A O   1 
HETATM 6692 O O   . HOH F 6 .   ? 38.052 6.430   -25.341 1.00 41.83  ? 312 HOH A O   1 
HETATM 6693 O O   . HOH F 6 .   ? 13.283 -0.081  -19.381 1.00 45.69  ? 313 HOH A O   1 
HETATM 6694 O O   . HOH F 6 .   ? 26.254 1.647   -14.432 1.00 38.58  ? 314 HOH A O   1 
HETATM 6695 O O   . HOH F 6 .   ? 28.760 14.983  -5.005  1.00 32.07  ? 315 HOH A O   1 
HETATM 6696 O O   . HOH F 6 .   ? 27.612 20.076  -35.284 1.00 34.60  ? 316 HOH A O   1 
HETATM 6697 O O   . HOH F 6 .   ? 23.661 25.530  -34.929 1.00 43.58  ? 317 HOH A O   1 
HETATM 6698 O O   . HOH F 6 .   ? 22.183 12.817  -30.366 1.00 33.19  ? 318 HOH A O   1 
HETATM 6699 O O   . HOH F 6 .   ? 46.804 7.794   -13.636 1.00 44.23  ? 319 HOH A O   1 
HETATM 6700 O O   . HOH F 6 .   ? 30.031 11.692  -18.328 1.00 25.55  ? 320 HOH A O   1 
HETATM 6701 O O   . HOH F 6 .   ? 12.346 53.711  1.554   1.00 40.34  ? 321 HOH A O   1 
HETATM 6702 O O   . HOH F 6 .   ? 23.376 10.732  -13.543 1.00 24.33  ? 322 HOH A O   1 
HETATM 6703 O O   . HOH F 6 .   ? 3.135  8.851   -24.418 1.00 35.63  ? 323 HOH A O   1 
HETATM 6704 O O   . HOH F 6 .   ? 32.887 15.838  -5.808  1.00 34.60  ? 324 HOH A O   1 
HETATM 6705 O O   . HOH F 6 .   ? 5.624  51.921  5.730   1.00 36.24  ? 325 HOH A O   1 
HETATM 6706 O O   . HOH F 6 .   ? 33.011 17.030  -32.033 1.00 27.09  ? 326 HOH A O   1 
HETATM 6707 O O   . HOH F 6 .   ? 12.682 58.615  8.468   1.00 40.37  ? 327 HOH A O   1 
HETATM 6708 O O   . HOH F 6 .   ? 26.621 3.611   -22.183 1.00 31.03  ? 328 HOH A O   1 
HETATM 6709 O O   . HOH F 6 .   ? 26.011 25.998  -26.361 1.00 38.95  ? 329 HOH A O   1 
HETATM 6710 O O   . HOH F 6 .   ? 23.522 1.085   -16.710 1.00 33.45  ? 330 HOH A O   1 
HETATM 6711 O O   . HOH F 6 .   ? 30.994 13.160  -3.139  1.00 37.31  ? 331 HOH A O   1 
HETATM 6712 O O   . HOH F 6 .   ? 7.832  26.862  -6.008  1.00 32.57  ? 332 HOH A O   1 
HETATM 6713 O O   . HOH F 6 .   ? 3.530  14.212  -11.236 1.00 48.07  ? 333 HOH A O   1 
HETATM 6714 O O   . HOH F 6 .   ? 3.213  15.686  -21.915 1.00 31.69  ? 334 HOH A O   1 
HETATM 6715 O O   . HOH F 6 .   ? 12.136 12.527  -19.826 1.00 23.95  ? 335 HOH A O   1 
HETATM 6716 O O   . HOH F 6 .   ? 14.044 6.619   -10.259 1.00 25.98  ? 336 HOH A O   1 
HETATM 6717 O O   . HOH F 6 .   ? 14.909 29.371  -6.779  1.00 35.33  ? 337 HOH A O   1 
HETATM 6718 O O   . HOH F 6 .   ? 22.281 3.351   -6.875  1.00 36.52  ? 338 HOH A O   1 
HETATM 6719 O O   . HOH F 6 .   ? 26.521 24.662  -24.121 1.00 25.99  ? 339 HOH A O   1 
HETATM 6720 O O   . HOH F 6 .   ? 6.468  20.487  -11.104 1.00 45.82  ? 340 HOH A O   1 
HETATM 6721 O O   . HOH F 6 .   ? 27.029 10.071  -19.986 1.00 32.15  ? 341 HOH A O   1 
HETATM 6722 O O   . HOH F 6 .   ? 24.096 11.458  -7.949  1.00 31.86  ? 342 HOH A O   1 
HETATM 6723 O O   . HOH F 6 .   ? 36.024 9.801   -10.594 1.00 25.40  ? 343 HOH A O   1 
HETATM 6724 O O   . HOH F 6 .   ? 41.412 7.480   -22.487 1.00 34.61  ? 344 HOH A O   1 
HETATM 6725 O O   . HOH F 6 .   ? 26.426 13.531  -14.896 1.00 34.69  ? 345 HOH A O   1 
HETATM 6726 O O   . HOH F 6 .   ? 23.706 29.268  -5.275  1.00 35.31  ? 346 HOH A O   1 
HETATM 6727 O O   . HOH F 6 .   ? 3.602  15.641  -29.930 1.00 38.67  ? 347 HOH A O   1 
HETATM 6728 O O   . HOH F 6 .   ? 23.026 27.602  -29.549 1.00 30.42  ? 348 HOH A O   1 
HETATM 6729 O O   . HOH F 6 .   ? 29.412 14.572  -26.599 1.00 25.49  ? 349 HOH A O   1 
HETATM 6730 O O   . HOH F 6 .   ? 30.866 17.948  -11.080 1.00 24.39  ? 350 HOH A O   1 
HETATM 6731 O O   . HOH F 6 .   ? 39.028 16.827  -9.251  1.00 28.59  ? 351 HOH A O   1 
HETATM 6732 O O   . HOH F 6 .   ? 4.251  -1.558  -27.113 1.00 48.81  ? 352 HOH A O   1 
HETATM 6733 O O   . HOH F 6 .   ? 41.081 14.842  -32.792 1.00 35.47  ? 353 HOH A O   1 
HETATM 6734 O O   . HOH F 6 .   ? 15.159 26.724  -12.974 1.00 47.14  ? 354 HOH A O   1 
HETATM 6735 O O   . HOH F 6 .   ? 16.762 14.958  -33.324 1.00 31.98  ? 355 HOH A O   1 
HETATM 6736 O O   . HOH F 6 .   ? 13.592 32.356  -15.084 1.00 39.38  ? 356 HOH A O   1 
HETATM 6737 O O   . HOH F 6 .   ? 35.509 6.940   -20.934 1.00 33.28  ? 357 HOH A O   1 
HETATM 6738 O O   . HOH F 6 .   ? 32.353 20.544  -36.223 1.00 46.12  ? 358 HOH A O   1 
HETATM 6739 O O   . HOH F 6 .   ? 6.765  1.422   -18.551 1.00 39.36  ? 359 HOH A O   1 
HETATM 6740 O O   . HOH F 6 .   ? 42.338 7.370   -17.461 1.00 34.49  ? 360 HOH A O   1 
HETATM 6741 O O   . HOH F 6 .   ? 7.346  5.696   -14.083 1.00 38.54  ? 361 HOH A O   1 
HETATM 6742 O O   . HOH F 6 .   ? 36.299 3.236   -17.417 1.00 36.52  ? 362 HOH A O   1 
HETATM 6743 O O   . HOH F 6 .   ? 39.335 4.653   -19.765 1.00 35.75  ? 363 HOH A O   1 
HETATM 6744 O O   . HOH F 6 .   ? 10.723 -2.574  -24.039 1.00 52.51  ? 364 HOH A O   1 
HETATM 6745 O O   . HOH F 6 .   ? 14.602 24.959  -18.320 1.00 31.75  ? 365 HOH A O   1 
HETATM 6746 O O   . HOH F 6 .   ? 32.094 22.995  -18.926 1.00 26.12  ? 366 HOH A O   1 
HETATM 6747 O O   . HOH F 6 .   ? 30.994 4.093   -6.562  1.00 39.88  ? 367 HOH A O   1 
HETATM 6748 O O   . HOH F 6 .   ? 20.713 16.350  -10.904 1.00 25.34  ? 368 HOH A O   1 
HETATM 6749 O O   . HOH F 6 .   ? 6.001  52.043  -1.990  1.00 45.97  ? 369 HOH A O   1 
HETATM 6750 O O   . HOH F 6 .   ? 13.948 60.381  5.045   1.00 45.59  ? 370 HOH A O   1 
HETATM 6751 O O   . HOH F 6 .   ? 30.914 16.095  -37.832 1.00 39.34  ? 371 HOH A O   1 
HETATM 6752 O O   . HOH F 6 .   ? 34.076 26.104  -13.174 1.00 33.92  ? 372 HOH A O   1 
HETATM 6753 O O   . HOH F 6 .   ? 12.775 34.866  5.159   1.00 40.13  ? 373 HOH A O   1 
HETATM 6754 O O   . HOH F 6 .   ? 44.389 6.709   -10.930 1.00 40.57  ? 374 HOH A O   1 
HETATM 6755 O O   . HOH F 6 .   ? 11.963 19.576  -34.174 1.00 44.20  ? 375 HOH A O   1 
HETATM 6756 O O   . HOH F 6 .   ? 21.697 11.765  -22.318 1.00 28.79  ? 376 HOH A O   1 
HETATM 6757 O O   . HOH F 6 .   ? 30.603 29.227  -30.813 1.00 37.37  ? 377 HOH A O   1 
HETATM 6758 O O   . HOH F 6 .   ? 30.638 29.696  -27.225 1.00 34.41  ? 378 HOH A O   1 
HETATM 6759 O O   . HOH F 6 .   ? 6.166  31.975  -18.764 1.00 46.10  ? 379 HOH A O   1 
HETATM 6760 O O   . HOH F 6 .   ? 31.006 16.935  -34.970 1.00 31.73  ? 380 HOH A O   1 
HETATM 6761 O O   . HOH F 6 .   ? 9.193  22.514  -9.979  1.00 29.09  ? 381 HOH A O   1 
HETATM 6762 O O   . HOH F 6 .   ? 33.049 3.913   -11.547 1.00 40.91  ? 382 HOH A O   1 
HETATM 6763 O O   . HOH F 6 .   ? 8.377  45.857  9.253   1.00 38.40  ? 383 HOH A O   1 
HETATM 6764 O O   . HOH F 6 .   ? 33.438 28.866  -32.018 1.00 51.96  ? 384 HOH A O   1 
HETATM 6765 O O   . HOH F 6 .   ? 35.785 7.733   -8.861  1.00 36.57  ? 385 HOH A O   1 
HETATM 6766 O O   . HOH F 6 .   ? 34.608 23.734  -20.062 1.00 31.16  ? 386 HOH A O   1 
HETATM 6767 O O   . HOH F 6 .   ? 13.136 24.495  -35.053 1.00 38.14  ? 387 HOH A O   1 
HETATM 6768 O O   . HOH F 6 .   ? 21.230 47.748  -5.306  1.00 56.19  ? 388 HOH A O   1 
HETATM 6769 O O   . HOH F 6 .   ? 6.150  11.619  -7.510  1.00 48.40  ? 389 HOH A O   1 
HETATM 6770 O O   . HOH F 6 .   ? 30.897 28.444  -36.636 1.00 48.24  ? 390 HOH A O   1 
HETATM 6771 O O   . HOH F 6 .   ? 3.921  24.557  -28.474 1.00 38.37  ? 391 HOH A O   1 
HETATM 6772 O O   . HOH F 6 .   ? 33.015 14.558  -3.750  1.00 33.15  ? 392 HOH A O   1 
HETATM 6773 O O   . HOH F 6 .   ? 21.212 28.817  -19.679 1.00 40.11  ? 393 HOH A O   1 
HETATM 6774 O O   . HOH F 6 .   ? 13.293 29.577  -17.236 1.00 41.00  ? 394 HOH A O   1 
HETATM 6775 O O   . HOH F 6 .   ? 22.569 30.360  -20.715 1.00 49.65  ? 395 HOH A O   1 
HETATM 6776 O O   . HOH F 6 .   ? 4.638  6.620   -15.153 1.00 37.91  ? 396 HOH A O   1 
HETATM 6777 O O   . HOH F 6 .   ? 3.886  6.176   -25.146 1.00 45.04  ? 397 HOH A O   1 
HETATM 6778 O O   . HOH F 6 .   ? 12.919 30.724  -20.001 1.00 43.58  ? 398 HOH A O   1 
HETATM 6779 O O   . HOH F 6 .   ? 23.861 29.170  -26.925 1.00 47.51  ? 399 HOH A O   1 
HETATM 6780 O O   . HOH F 6 .   ? 8.983  2.127   -17.287 1.00 44.63  ? 400 HOH A O   1 
HETATM 6781 O O   . HOH F 6 .   ? 0.810  41.725  -8.214  1.00 42.40  ? 401 HOH A O   1 
HETATM 6782 O O   . HOH F 6 .   ? 14.283 27.571  -10.549 1.00 50.69  ? 402 HOH A O   1 
HETATM 6783 O O   . HOH F 6 .   ? 30.098 19.462  -36.269 1.00 37.44  ? 403 HOH A O   1 
HETATM 6784 O O   . HOH F 6 .   ? 11.311 31.294  -18.220 1.00 51.14  ? 404 HOH A O   1 
HETATM 6785 O O   . HOH F 6 .   ? 7.591  48.003  11.257  1.00 39.06  ? 405 HOH A O   1 
HETATM 6786 O O   . HOH F 6 .   ? 41.606 6.434   -19.939 1.00 41.54  ? 406 HOH A O   1 
HETATM 6787 O O   . HOH F 6 .   ? 14.137 62.568  3.719   1.00 53.45  ? 407 HOH A O   1 
HETATM 6788 O O   . HOH F 6 .   ? 36.252 2.413   -20.226 1.00 39.74  ? 408 HOH A O   1 
HETATM 6789 O O   . HOH F 6 .   ? 26.881 52.616  4.329   1.00 56.96  ? 409 HOH A O   1 
HETATM 6790 O O   . HOH F 6 .   ? 6.304  2.971   -15.322 1.00 44.72  ? 410 HOH A O   1 
HETATM 6791 O O   . HOH G 6 .   ? 29.846 18.058  8.527   1.00 38.37  ? 101 HOH B O   1 
HETATM 6792 O O   . HOH G 6 .   ? 1.715  23.723  17.491  1.00 46.11  ? 102 HOH B O   1 
HETATM 6793 O O   . HOH G 6 .   ? 13.557 20.001  22.064  1.00 29.07  ? 103 HOH B O   1 
HETATM 6794 O O   . HOH G 6 .   ? 32.477 24.164  10.083  1.00 49.33  ? 104 HOH B O   1 
HETATM 6795 O O   . HOH G 6 .   ? 13.689 13.815  21.497  1.00 32.11  ? 105 HOH B O   1 
HETATM 6796 O O   . HOH G 6 .   ? 2.768  25.738  15.157  1.00 49.79  ? 106 HOH B O   1 
HETATM 6797 O O   . HOH G 6 .   ? 37.267 23.890  -2.196  1.00 44.62  ? 107 HOH B O   1 
HETATM 6798 O O   . HOH G 6 .   ? 6.819  23.644  0.137   1.00 32.79  ? 108 HOH B O   1 
HETATM 6799 O O   . HOH G 6 .   ? 16.341 17.234  17.772  1.00 36.86  ? 109 HOH B O   1 
HETATM 6800 O O   . HOH G 6 .   ? 1.069  22.362  12.509  1.00 64.20  ? 110 HOH B O   1 
HETATM 6801 O O   . HOH G 6 .   ? 15.748 16.522  21.724  1.00 31.67  ? 111 HOH B O   1 
HETATM 6802 O O   . HOH G 6 .   ? 22.855 26.327  -6.010  1.00 29.12  ? 112 HOH B O   1 
HETATM 6803 O O   . HOH G 6 .   ? 40.936 18.998  -2.447  1.00 38.78  ? 113 HOH B O   1 
HETATM 6804 O O   . HOH G 6 .   ? 16.305 20.619  -5.860  1.00 30.67  ? 114 HOH B O   1 
HETATM 6805 O O   . HOH G 6 .   ? 34.892 24.197  6.583   1.00 39.56  ? 115 HOH B O   1 
HETATM 6806 O O   . HOH G 6 .   ? 28.745 16.711  2.862   1.00 30.24  ? 116 HOH B O   1 
HETATM 6807 O O   . HOH G 6 .   ? 10.367 30.066  15.017  1.00 38.96  ? 117 HOH B O   1 
HETATM 6808 O O   . HOH G 6 .   ? -0.078 30.538  8.083   1.00 44.31  ? 118 HOH B O   1 
HETATM 6809 O O   . HOH G 6 .   ? 19.728 29.189  0.456   1.00 33.01  ? 119 HOH B O   1 
HETATM 6810 O O   . HOH G 6 .   ? 12.357 40.144  12.056  1.00 49.81  ? 120 HOH B O   1 
HETATM 6811 O O   . HOH G 6 .   ? 14.583 15.562  18.032  1.00 36.48  ? 121 HOH B O   1 
HETATM 6812 O O   . HOH G 6 .   ? 13.130 16.759  9.542   1.00 33.64  ? 122 HOH B O   1 
HETATM 6813 O O   . HOH G 6 .   ? 4.850  29.117  14.916  1.00 46.33  ? 123 HOH B O   1 
HETATM 6814 O O   . HOH G 6 .   ? 6.372  20.620  20.393  1.00 44.79  ? 124 HOH B O   1 
HETATM 6815 O O   . HOH G 6 .   ? 16.157 34.503  3.984   1.00 38.94  ? 125 HOH B O   1 
HETATM 6816 O O   . HOH G 6 .   ? 13.774 33.322  8.828   1.00 38.24  ? 126 HOH B O   1 
HETATM 6817 O O   . HOH G 6 .   ? 11.022 34.036  7.224   1.00 56.02  ? 127 HOH B O   1 
HETATM 6818 O O   . HOH G 6 .   ? 19.230 31.541  13.424  1.00 41.32  ? 128 HOH B O   1 
HETATM 6819 O O   . HOH G 6 .   ? 18.477 14.700  5.484   1.00 38.27  ? 129 HOH B O   1 
HETATM 6820 O O   . HOH G 6 .   ? 3.364  21.539  13.884  1.00 47.96  ? 130 HOH B O   1 
HETATM 6821 O O   . HOH G 6 .   ? 15.929 32.973  9.250   1.00 37.77  ? 131 HOH B O   1 
HETATM 6822 O O   . HOH G 6 .   ? 21.469 25.483  -13.696 1.00 37.66  ? 132 HOH B O   1 
HETATM 6823 O O   . HOH G 6 .   ? 8.953  33.557  6.754   1.00 35.15  ? 133 HOH B O   1 
HETATM 6824 O O   . HOH G 6 .   ? 13.010 24.695  16.814  1.00 38.00  ? 134 HOH B O   1 
HETATM 6825 O O   . HOH G 6 .   ? 32.371 26.470  -10.414 1.00 37.55  ? 135 HOH B O   1 
HETATM 6826 O O   . HOH G 6 .   ? 23.176 30.697  5.505   1.00 42.35  ? 136 HOH B O   1 
HETATM 6827 O O   . HOH G 6 .   ? 21.484 29.310  -12.157 1.00 39.49  ? 137 HOH B O   1 
HETATM 6828 O O   . HOH G 6 .   ? 10.898 13.281  0.068   1.00 40.36  ? 138 HOH B O   1 
HETATM 6829 O O   . HOH G 6 .   ? 28.526 16.227  7.927   1.00 42.42  ? 139 HOH B O   1 
HETATM 6830 O O   . HOH G 6 .   ? 16.218 32.181  7.431   1.00 36.35  ? 140 HOH B O   1 
HETATM 6831 O O   . HOH G 6 .   ? 7.067  15.165  14.132  1.00 44.01  ? 141 HOH B O   1 
HETATM 6832 O O   . HOH G 6 .   ? 15.088 33.336  5.572   1.00 32.88  ? 142 HOH B O   1 
HETATM 6833 O O   . HOH G 6 .   ? 25.001 30.042  -10.083 1.00 36.19  ? 143 HOH B O   1 
HETATM 6834 O O   . HOH G 6 .   ? 17.087 27.221  -10.276 1.00 51.27  ? 144 HOH B O   1 
HETATM 6835 O O   . HOH G 6 .   ? 30.298 14.499  1.704   1.00 31.65  ? 145 HOH B O   1 
HETATM 6836 O O   . HOH G 6 .   ? 16.539 25.418  -13.530 1.00 48.96  ? 146 HOH B O   1 
HETATM 6837 O O   . HOH G 6 .   ? 22.890 31.251  -8.705  1.00 53.60  ? 147 HOH B O   1 
HETATM 6838 O O   . HOH G 6 .   ? 23.870 32.501  4.270   1.00 53.82  ? 148 HOH B O   1 
HETATM 6839 O O   . HOH H 6 .   ? 23.373 10.011  -29.092 1.00 45.24  ? 101 HOH C O   1 
HETATM 6840 O O   . HOH H 6 .   ? 24.780 5.033   -28.696 1.00 26.05  ? 102 HOH C O   1 
HETATM 6841 O O   . HOH H 6 .   ? 29.295 7.347   -25.530 1.00 28.96  ? 103 HOH C O   1 
HETATM 6842 O O   . HOH H 6 .   ? 34.924 9.246   -26.979 1.00 32.41  ? 104 HOH C O   1 
HETATM 6843 O O   . HOH H 6 .   ? 28.982 11.903  -21.018 1.00 26.25  ? 105 HOH C O   1 
HETATM 6844 O O   . HOH H 6 .   ? 23.359 15.847  -24.734 1.00 42.73  ? 106 HOH C O   1 
HETATM 6845 O O   . HOH H 6 .   ? 32.520 8.398   -27.295 1.00 30.10  ? 107 HOH C O   1 
HETATM 6846 O O   . HOH H 6 .   ? 23.112 12.196  -24.488 1.00 34.36  ? 108 HOH C O   1 
HETATM 6847 O O   . HOH H 6 .   ? 35.461 4.134   -21.587 1.00 37.92  ? 109 HOH C O   1 
HETATM 6848 O O   . HOH I 6 .   ? 30.627 -34.128 -75.517 1.00 51.05  ? 301 HOH E O   1 
HETATM 6849 O O   . HOH I 6 .   ? 12.299 -25.180 -46.524 1.00 38.19  ? 302 HOH E O   1 
HETATM 6850 O O   . HOH I 6 .   ? 17.973 -1.970  -34.504 1.00 33.78  ? 303 HOH E O   1 
HETATM 6851 O O   . HOH I 6 .   ? 15.447 -2.782  -20.945 1.00 35.17  ? 304 HOH E O   1 
HETATM 6852 O O   . HOH I 6 .   ? 15.866 -13.923 -22.633 1.00 27.89  ? 305 HOH E O   1 
HETATM 6853 O O   . HOH I 6 .   ? 37.673 -32.500 -64.420 1.00 40.91  ? 306 HOH E O   1 
HETATM 6854 O O   . HOH I 6 .   ? 21.305 6.829   -40.995 1.00 34.82  ? 307 HOH E O   1 
HETATM 6855 O O   . HOH I 6 .   ? 35.159 -8.291  -36.306 1.00 42.39  ? 308 HOH E O   1 
HETATM 6856 O O   . HOH I 6 .   ? 30.261 -10.400 -24.292 1.00 28.24  ? 309 HOH E O   1 
HETATM 6857 O O   . HOH I 6 .   ? 16.994 -34.954 -39.360 1.00 32.87  ? 310 HOH E O   1 
HETATM 6858 O O   . HOH I 6 .   ? 7.537  -4.031  -31.861 1.00 40.96  ? 311 HOH E O   1 
HETATM 6859 O O   . HOH I 6 .   ? 44.611 -26.263 -81.237 1.00 41.47  ? 312 HOH E O   1 
HETATM 6860 O O   . HOH I 6 .   ? 19.847 -25.177 -74.269 1.00 29.86  ? 313 HOH E O   1 
HETATM 6861 O O   . HOH I 6 .   ? 31.505 -13.922 -35.102 1.00 33.27  ? 314 HOH E O   1 
HETATM 6862 O O   . HOH I 6 .   ? 30.636 -21.095 -34.424 1.00 30.09  ? 315 HOH E O   1 
HETATM 6863 O O   . HOH I 6 .   ? 40.093 -24.136 -79.392 1.00 36.15  ? 316 HOH E O   1 
HETATM 6864 O O   . HOH I 6 .   ? 12.900 -27.880 -36.919 1.00 41.23  ? 317 HOH E O   1 
HETATM 6865 O O   . HOH I 6 .   ? 21.902 -9.118  -20.822 1.00 39.61  ? 318 HOH E O   1 
HETATM 6866 O O   . HOH I 6 .   ? 37.558 -30.557 -74.612 1.00 31.41  ? 319 HOH E O   1 
HETATM 6867 O O   . HOH I 6 .   ? 28.434 -18.900 -24.718 1.00 28.50  ? 320 HOH E O   1 
HETATM 6868 O O   . HOH I 6 .   ? 23.276 -9.078  -44.528 1.00 30.64  ? 321 HOH E O   1 
HETATM 6869 O O   . HOH I 6 .   ? 18.625 -36.360 -56.291 1.00 43.53  ? 322 HOH E O   1 
HETATM 6870 O O   . HOH I 6 .   ? 17.905 -29.158 -22.646 1.00 46.46  ? 323 HOH E O   1 
HETATM 6871 O O   . HOH I 6 .   ? 7.265  -12.953 -36.732 1.00 43.88  ? 324 HOH E O   1 
HETATM 6872 O O   . HOH I 6 .   ? 23.423 -2.085  -44.590 1.00 22.85  ? 325 HOH E O   1 
HETATM 6873 O O   . HOH I 6 .   ? 31.384 -33.929 -52.141 1.00 30.28  ? 326 HOH E O   1 
HETATM 6874 O O   . HOH I 6 .   ? 35.762 -26.098 -55.532 0.50 34.38  ? 327 HOH E O   1 
HETATM 6875 O O   . HOH I 6 .   ? 25.785 -27.339 -38.591 1.00 39.89  ? 328 HOH E O   1 
HETATM 6876 O O   . HOH I 6 .   ? 22.801 7.717   -30.590 1.00 36.41  ? 329 HOH E O   1 
HETATM 6877 O O   . HOH I 6 .   ? 15.502 -22.854 -85.818 1.00 39.48  ? 330 HOH E O   1 
HETATM 6878 O O   . HOH I 6 .   ? 28.841 -34.977 -59.763 1.00 28.79  ? 331 HOH E O   1 
HETATM 6879 O O   . HOH I 6 .   ? 26.525 -18.269 -55.379 1.00 44.29  ? 332 HOH E O   1 
HETATM 6880 O O   . HOH I 6 .   ? 22.711 -12.552 -65.122 1.00 25.86  ? 333 HOH E O   1 
HETATM 6881 O O   . HOH I 6 .   ? 26.450 -36.089 -53.348 1.00 25.36  ? 334 HOH E O   1 
HETATM 6882 O O   . HOH I 6 .   ? 24.093 -18.471 -58.239 1.00 28.06  ? 335 HOH E O   1 
HETATM 6883 O O   . HOH I 6 .   ? 29.053 1.663   -21.871 1.00 30.14  ? 336 HOH E O   1 
HETATM 6884 O O   . HOH I 6 .   ? 31.543 -17.240 -40.032 1.00 48.04  ? 337 HOH E O   1 
HETATM 6885 O O   . HOH I 6 .   ? 12.891 -32.242 -35.715 1.00 44.60  ? 338 HOH E O   1 
HETATM 6886 O O   . HOH I 6 .   ? 25.098 -30.210 -34.374 1.00 31.31  ? 339 HOH E O   1 
HETATM 6887 O O   . HOH I 6 .   ? 11.894 -29.418 -46.064 1.00 39.85  ? 340 HOH E O   1 
HETATM 6888 O O   . HOH I 6 .   ? 20.839 -26.901 -22.116 1.00 36.57  ? 341 HOH E O   1 
HETATM 6889 O O   . HOH I 6 .   ? 15.341 -26.184 -44.822 1.00 38.90  ? 342 HOH E O   1 
HETATM 6890 O O   . HOH I 6 .   ? 13.240 -36.854 -52.693 1.00 43.60  ? 343 HOH E O   1 
HETATM 6891 O O   . HOH I 6 .   ? 36.086 -23.898 -64.759 1.00 23.57  ? 344 HOH E O   1 
HETATM 6892 O O   . HOH I 6 .   ? 26.979 3.858   -38.410 1.00 29.63  ? 345 HOH E O   1 
HETATM 6893 O O   . HOH I 6 .   ? 33.027 -5.139  -19.356 1.00 36.46  ? 346 HOH E O   1 
HETATM 6894 O O   . HOH I 6 .   ? 29.593 -15.869 -68.328 1.00 28.06  ? 347 HOH E O   1 
HETATM 6895 O O   . HOH I 6 .   ? 28.345 -5.746  -42.646 1.00 29.81  ? 348 HOH E O   1 
HETATM 6896 O O   . HOH I 6 .   ? 14.101 -20.675 -41.282 1.00 28.29  ? 349 HOH E O   1 
HETATM 6897 O O   . HOH I 6 .   ? 34.074 -8.255  -38.513 1.00 35.81  ? 350 HOH E O   1 
HETATM 6898 O O   . HOH I 6 .   ? 21.183 1.489   -36.021 1.00 32.88  ? 351 HOH E O   1 
HETATM 6899 O O   . HOH I 6 .   ? 7.739  -12.589 -27.485 1.00 48.53  ? 352 HOH E O   1 
HETATM 6900 O O   . HOH I 6 .   ? 36.898 -25.176 -62.333 1.00 29.68  ? 353 HOH E O   1 
HETATM 6901 O O   . HOH I 6 .   ? 28.431 -18.012 -60.075 1.00 29.42  ? 354 HOH E O   1 
HETATM 6902 O O   . HOH I 6 .   ? 28.064 -15.680 -70.683 1.00 26.99  ? 355 HOH E O   1 
HETATM 6903 O O   . HOH I 6 .   ? 26.328 -8.329  -44.908 1.00 45.45  ? 356 HOH E O   1 
HETATM 6904 O O   . HOH I 6 .   ? 29.662 -10.202 -70.065 1.00 46.24  ? 357 HOH E O   1 
HETATM 6905 O O   . HOH I 6 .   ? 23.655 -1.380  -17.989 1.00 28.38  ? 358 HOH E O   1 
HETATM 6906 O O   . HOH I 6 .   ? 10.279 -13.175 -38.399 1.00 29.20  ? 359 HOH E O   1 
HETATM 6907 O O   . HOH I 6 .   ? 27.447 -28.983 -36.394 1.00 43.17  ? 360 HOH E O   1 
HETATM 6908 O O   . HOH I 6 .   ? 31.095 -8.875  -25.701 1.00 29.36  ? 361 HOH E O   1 
HETATM 6909 O O   . HOH I 6 .   ? 28.079 -25.010 -38.144 1.00 30.82  ? 362 HOH E O   1 
HETATM 6910 O O   . HOH I 6 .   ? 19.681 0.857   -21.638 1.00 20.81  ? 363 HOH E O   1 
HETATM 6911 O O   . HOH I 6 .   ? 24.419 -26.233 -42.196 1.00 33.65  ? 364 HOH E O   1 
HETATM 6912 O O   . HOH I 6 .   ? 20.853 -1.875  -24.896 1.00 22.51  ? 365 HOH E O   1 
HETATM 6913 O O   . HOH I 6 .   ? 31.497 -21.782 -38.437 1.00 41.61  ? 366 HOH E O   1 
HETATM 6914 O O   . HOH I 6 .   ? 19.951 -18.755 -23.604 1.00 24.13  ? 367 HOH E O   1 
HETATM 6915 O O   . HOH I 6 .   ? 30.356 -19.996 -40.553 1.00 30.52  ? 368 HOH E O   1 
HETATM 6916 O O   . HOH I 6 .   ? 34.050 -31.069 -50.617 1.00 27.44  ? 369 HOH E O   1 
HETATM 6917 O O   . HOH I 6 .   ? 29.191 -22.638 -54.683 1.00 22.73  ? 370 HOH E O   1 
HETATM 6918 O O   . HOH I 6 .   ? 27.356 -7.797  -20.656 1.00 30.79  ? 371 HOH E O   1 
HETATM 6919 O O   . HOH I 6 .   ? 41.230 -25.059 -71.009 1.00 43.50  ? 372 HOH E O   1 
HETATM 6920 O O   . HOH I 6 .   ? 28.076 -36.702 -51.529 1.00 28.87  ? 373 HOH E O   1 
HETATM 6921 O O   . HOH I 6 .   ? 39.381 -22.310 -59.851 1.00 28.38  ? 374 HOH E O   1 
HETATM 6922 O O   . HOH I 6 .   ? 9.787  -25.759 -30.680 1.00 35.24  ? 375 HOH E O   1 
HETATM 6923 O O   . HOH I 6 .   ? 19.131 -14.234 -79.472 1.00 43.52  ? 376 HOH E O   1 
HETATM 6924 O O   . HOH I 6 .   ? 26.686 -22.685 -84.944 1.00 37.11  ? 377 HOH E O   1 
HETATM 6925 O O   . HOH I 6 .   ? 27.406 -13.057 -70.696 1.00 32.72  ? 378 HOH E O   1 
HETATM 6926 O O   . HOH I 6 .   ? 34.471 -21.774 -81.522 1.00 32.74  ? 379 HOH E O   1 
HETATM 6927 O O   . HOH I 6 .   ? 14.350 -33.482 -58.275 1.00 40.11  ? 380 HOH E O   1 
HETATM 6928 O O   . HOH I 6 .   ? 31.946 6.662   -29.629 1.00 40.33  ? 381 HOH E O   1 
HETATM 6929 O O   . HOH I 6 .   ? 34.772 -2.663  -32.406 1.00 30.55  ? 382 HOH E O   1 
HETATM 6930 O O   . HOH I 6 .   ? 36.129 -23.020 -56.966 1.00 34.28  ? 383 HOH E O   1 
HETATM 6931 O O   . HOH I 6 .   ? 20.516 11.527  -32.370 1.00 37.03  ? 384 HOH E O   1 
HETATM 6932 O O   . HOH I 6 .   ? 22.926 -20.317 -54.595 1.00 25.03  ? 385 HOH E O   1 
HETATM 6933 O O   . HOH I 6 .   ? 31.849 -33.286 -56.957 1.00 31.98  ? 386 HOH E O   1 
HETATM 6934 O O   . HOH I 6 .   ? 12.012 -18.590 -28.565 1.00 44.16  ? 387 HOH E O   1 
HETATM 6935 O O   . HOH I 6 .   ? 12.052 -15.081 -46.296 1.00 33.06  ? 388 HOH E O   1 
HETATM 6936 O O   . HOH I 6 .   ? 10.824 -6.372  -33.531 1.00 30.11  ? 389 HOH E O   1 
HETATM 6937 O O   . HOH I 6 .   ? 16.860 -21.740 -25.361 1.00 30.84  ? 390 HOH E O   1 
HETATM 6938 O O   . HOH I 6 .   ? 14.373 -22.338 -26.234 1.00 37.32  ? 391 HOH E O   1 
HETATM 6939 O O   . HOH I 6 .   ? 21.048 -15.790 -59.634 1.00 30.73  ? 392 HOH E O   1 
HETATM 6940 O O   . HOH I 6 .   ? 26.248 4.815   -24.781 1.00 37.14  ? 393 HOH E O   1 
HETATM 6941 O O   . HOH I 6 .   ? 31.429 -38.618 -45.041 1.00 35.85  ? 394 HOH E O   1 
HETATM 6942 O O   . HOH I 6 .   ? 21.100 -33.511 -59.826 1.00 24.35  ? 395 HOH E O   1 
HETATM 6943 O O   . HOH I 6 .   ? 30.031 -12.343 -30.262 1.00 29.90  ? 396 HOH E O   1 
HETATM 6944 O O   . HOH I 6 .   ? 25.231 -4.247  -44.346 1.00 26.58  ? 397 HOH E O   1 
HETATM 6945 O O   . HOH I 6 .   ? 27.367 -22.312 -26.343 1.00 36.25  ? 398 HOH E O   1 
HETATM 6946 O O   . HOH I 6 .   ? 35.181 3.442   -27.140 1.00 46.24  ? 399 HOH E O   1 
HETATM 6947 O O   . HOH I 6 .   ? 28.762 -33.866 -65.660 1.00 43.09  ? 400 HOH E O   1 
HETATM 6948 O O   . HOH I 6 .   ? 26.317 -33.899 -65.068 1.00 30.45  ? 401 HOH E O   1 
HETATM 6949 O O   . HOH I 6 .   ? 26.531 -26.300 -41.434 1.00 32.73  ? 402 HOH E O   1 
HETATM 6950 O O   . HOH I 6 .   ? 38.871 -4.582  -32.220 1.00 47.53  ? 403 HOH E O   1 
HETATM 6951 O O   . HOH I 6 .   ? 21.211 -37.257 -34.649 1.00 34.26  ? 404 HOH E O   1 
HETATM 6952 O O   . HOH I 6 .   ? 36.040 -4.468  -27.958 1.00 31.47  ? 405 HOH E O   1 
HETATM 6953 O O   . HOH I 6 .   ? 7.268  -18.323 -41.479 1.00 36.26  ? 406 HOH E O   1 
HETATM 6954 O O   . HOH I 6 .   ? 30.276 -13.750 -41.226 1.00 33.95  ? 407 HOH E O   1 
HETATM 6955 O O   . HOH I 6 .   ? 20.319 -27.931 -85.191 1.00 41.84  ? 408 HOH E O   1 
HETATM 6956 O O   . HOH I 6 .   ? 25.645 -34.360 -32.569 1.00 50.34  ? 409 HOH E O   1 
HETATM 6957 O O   . HOH I 6 .   ? 31.567 2.786   -39.450 1.00 34.55  ? 410 HOH E O   1 
HETATM 6958 O O   . HOH I 6 .   ? 26.565 -35.520 -58.015 1.00 26.67  ? 411 HOH E O   1 
HETATM 6959 O O   . HOH I 6 .   ? 11.946 -35.717 -50.226 1.00 34.41  ? 412 HOH E O   1 
HETATM 6960 O O   . HOH I 6 .   ? 29.802 -20.832 -52.572 1.00 28.15  ? 413 HOH E O   1 
HETATM 6961 O O   . HOH I 6 .   ? 25.733 5.610   -36.513 1.00 28.84  ? 414 HOH E O   1 
HETATM 6962 O O   . HOH I 6 .   ? 18.969 -7.887  -20.456 1.00 39.63  ? 415 HOH E O   1 
HETATM 6963 O O   . HOH I 6 .   ? 35.236 -3.414  -21.968 1.00 41.75  ? 416 HOH E O   1 
HETATM 6964 O O   . HOH I 6 .   ? 28.311 -22.995 -29.551 1.00 29.52  ? 417 HOH E O   1 
HETATM 6965 O O   . HOH I 6 .   ? 10.797 -19.227 -30.509 1.00 34.54  ? 418 HOH E O   1 
HETATM 6966 O O   . HOH I 6 .   ? 31.495 -32.414 -72.240 1.00 38.46  ? 419 HOH E O   1 
HETATM 6967 O O   . HOH I 6 .   ? 36.066 -19.306 -76.917 1.00 31.87  ? 420 HOH E O   1 
HETATM 6968 O O   . HOH I 6 .   ? 26.951 -27.407 -25.859 1.00 36.20  ? 421 HOH E O   1 
HETATM 6969 O O   . HOH I 6 .   ? 21.953 -3.005  -19.242 1.00 27.09  ? 422 HOH E O   1 
HETATM 6970 O O   . HOH I 6 .   ? 40.327 -7.293  -33.185 1.00 49.67  ? 423 HOH E O   1 
HETATM 6971 O O   . HOH I 6 .   ? 33.875 -32.868 -55.011 1.00 46.60  ? 424 HOH E O   1 
HETATM 6972 O O   . HOH I 6 .   ? 31.084 5.094   -31.896 1.00 42.02  ? 425 HOH E O   1 
HETATM 6973 O O   . HOH I 6 .   ? 14.696 -5.334  -20.995 1.00 46.91  ? 426 HOH E O   1 
HETATM 6974 O O   . HOH I 6 .   ? 36.985 -0.558  -27.571 1.00 47.17  ? 427 HOH E O   1 
HETATM 6975 O O   . HOH I 6 .   ? 30.460 -25.864 -41.929 1.00 32.21  ? 428 HOH E O   1 
HETATM 6976 O O   . HOH I 6 .   ? 20.873 -11.572 -21.507 1.00 32.98  ? 429 HOH E O   1 
HETATM 6977 O O   . HOH I 6 .   ? 28.785 -22.311 -41.477 1.00 33.98  ? 430 HOH E O   1 
HETATM 6978 O O   . HOH I 6 .   ? 19.756 -18.610 -19.419 1.00 40.81  ? 431 HOH E O   1 
HETATM 6979 O O   . HOH I 6 .   ? 24.428 -13.254 -47.245 1.00 43.18  ? 432 HOH E O   1 
HETATM 6980 O O   . HOH I 6 .   ? 14.523 -33.544 -40.381 1.00 38.09  ? 433 HOH E O   1 
HETATM 6981 O O   . HOH I 6 .   ? 10.415 -21.943 -36.427 1.00 29.75  ? 434 HOH E O   1 
HETATM 6982 O O   . HOH I 6 .   ? 10.936 -11.786 -21.214 1.00 38.48  ? 435 HOH E O   1 
HETATM 6983 O O   . HOH I 6 .   ? 7.053  -7.263  -33.174 1.00 42.35  ? 436 HOH E O   1 
HETATM 6984 O O   . HOH I 6 .   ? 36.819 -17.651 -70.530 1.00 32.83  ? 437 HOH E O   1 
HETATM 6985 O O   . HOH I 6 .   ? 37.024 -17.207 -67.830 1.00 32.80  ? 438 HOH E O   1 
HETATM 6986 O O   . HOH I 6 .   ? 37.270 -16.366 -59.816 1.00 31.90  ? 439 HOH E O   1 
HETATM 6987 O O   . HOH I 6 .   ? 33.362 -27.896 -48.535 1.00 35.51  ? 440 HOH E O   1 
HETATM 6988 O O   . HOH I 6 .   ? 16.344 -25.192 -84.427 1.00 39.98  ? 441 HOH E O   1 
HETATM 6989 O O   . HOH I 6 .   ? 29.866 -15.882 -74.307 1.00 30.65  ? 442 HOH E O   1 
HETATM 6990 O O   . HOH I 6 .   ? 31.893 -17.726 -43.333 1.00 42.10  ? 443 HOH E O   1 
HETATM 6991 O O   . HOH I 6 .   ? 34.520 0.904   -24.539 1.00 38.25  ? 444 HOH E O   1 
HETATM 6992 O O   . HOH I 6 .   ? 41.277 -23.203 -70.843 1.00 51.04  ? 445 HOH E O   1 
HETATM 6993 O O   . HOH I 6 .   ? 17.226 -27.269 -20.507 1.00 44.75  ? 446 HOH E O   1 
HETATM 6994 O O   . HOH I 6 .   ? 36.042 -16.310 -57.318 1.00 36.51  ? 447 HOH E O   1 
HETATM 6995 O O   . HOH I 6 .   ? 25.229 -37.047 -60.032 1.00 40.62  ? 448 HOH E O   1 
HETATM 6996 O O   . HOH I 6 .   ? 17.277 -18.534 -22.242 1.00 30.55  ? 449 HOH E O   1 
HETATM 6997 O O   . HOH I 6 .   ? 33.492 -16.683 -77.849 1.00 46.00  ? 450 HOH E O   1 
HETATM 6998 O O   . HOH I 6 .   ? 32.586 -15.647 -76.683 1.00 50.39  ? 451 HOH E O   1 
HETATM 6999 O O   . HOH I 6 .   ? 37.141 -2.837  -30.544 1.00 44.69  ? 452 HOH E O   1 
HETATM 7000 O O   . HOH I 6 .   ? 26.138 -17.016 -59.244 1.00 25.49  ? 453 HOH E O   1 
HETATM 7001 O O   . HOH I 6 .   ? 33.896 -14.460 -29.536 1.00 47.09  ? 454 HOH E O   1 
HETATM 7002 O O   . HOH I 6 .   ? 31.312 -13.785 -68.059 1.00 35.61  ? 455 HOH E O   1 
HETATM 7003 O O   . HOH I 6 .   ? 22.378 -17.772 -55.989 1.00 35.16  ? 456 HOH E O   1 
HETATM 7004 O O   . HOH I 6 .   ? 12.714 -33.777 -38.433 1.00 43.56  ? 457 HOH E O   1 
HETATM 7005 O O   . HOH I 6 .   ? 11.052 -30.556 -29.205 1.00 35.57  ? 458 HOH E O   1 
HETATM 7006 O O   . HOH I 6 .   ? 29.079 -16.103 -25.074 1.00 36.09  ? 459 HOH E O   1 
HETATM 7007 O O   . HOH I 6 .   ? 31.726 -13.465 -28.069 1.00 32.10  ? 460 HOH E O   1 
HETATM 7008 O O   . HOH I 6 .   ? 27.476 -37.082 -55.819 1.00 31.99  ? 461 HOH E O   1 
HETATM 7009 O O   . HOH I 6 .   ? 11.584 -28.422 -27.239 1.00 39.59  ? 462 HOH E O   1 
HETATM 7010 O O   . HOH I 6 .   ? 31.080 -16.147 -27.178 1.00 29.12  ? 463 HOH E O   1 
HETATM 7011 O O   . HOH J 6 .   ? 6.918  -27.380 -59.304 1.00 49.98  ? 301 HOH D O   1 
HETATM 7012 O O   . HOH J 6 .   ? 13.623 -34.483 -67.515 1.00 52.98  ? 302 HOH D O   1 
HETATM 7013 O O   . HOH J 6 .   ? 3.268  7.912   -47.486 1.00 29.88  ? 303 HOH D O   1 
HETATM 7014 O O   . HOH J 6 .   ? 12.595 -34.132 -87.246 1.00 51.95  ? 304 HOH D O   1 
HETATM 7015 O O   . HOH J 6 .   ? 11.783 -4.704  -30.109 1.00 30.33  ? 305 HOH D O   1 
HETATM 7016 O O   . HOH J 6 .   ? 1.046  -16.475 -69.964 1.00 43.74  ? 306 HOH D O   1 
HETATM 7017 O O   . HOH J 6 .   ? 7.010  -10.730 -50.582 1.00 45.23  ? 307 HOH D O   1 
HETATM 7018 O O   . HOH J 6 .   ? 17.998 12.101  -33.346 1.00 40.01  ? 308 HOH D O   1 
HETATM 7019 O O   . HOH J 6 .   ? 15.179 12.335  -42.672 1.00 54.89  ? 309 HOH D O   1 
HETATM 7020 O O   . HOH J 6 .   ? 8.472  13.754  -33.695 1.00 37.14  ? 310 HOH D O   1 
HETATM 7021 O O   . HOH J 6 .   ? 3.526  1.992   -29.569 1.00 33.50  ? 311 HOH D O   1 
HETATM 7022 O O   . HOH J 6 .   ? 27.895 -11.753 -72.677 1.00 33.28  ? 312 HOH D O   1 
HETATM 7023 O O   . HOH J 6 .   ? 9.960  8.330   -28.808 1.00 45.42  ? 313 HOH D O   1 
HETATM 7024 O O   . HOH J 6 .   ? 4.202  -7.298  -46.103 1.00 35.64  ? 314 HOH D O   1 
HETATM 7025 O O   . HOH J 6 .   ? 20.377 -37.253 -71.340 1.00 52.35  ? 315 HOH D O   1 
HETATM 7026 O O   . HOH J 6 .   ? 17.288 -0.777  -55.075 1.00 32.81  ? 316 HOH D O   1 
HETATM 7027 O O   . HOH J 6 .   ? 7.877  -13.012 -49.216 1.00 32.49  ? 317 HOH D O   1 
HETATM 7028 O O   . HOH J 6 .   ? 7.498  8.177   -51.675 1.00 31.22  ? 318 HOH D O   1 
HETATM 7029 O O   . HOH J 6 .   ? 25.088 -5.960  -46.637 1.00 41.48  ? 319 HOH D O   1 
HETATM 7030 O O   . HOH J 6 .   ? 22.554 -35.897 -60.643 1.00 38.12  ? 320 HOH D O   1 
HETATM 7031 O O   . HOH J 6 .   ? 3.517  10.394  -35.180 1.00 35.61  ? 321 HOH D O   1 
HETATM 7032 O O   . HOH J 6 .   ? 16.952 -16.822 -67.805 1.00 24.34  ? 322 HOH D O   1 
HETATM 7033 O O   . HOH J 6 .   ? 11.061 14.364  -31.506 1.00 37.04  ? 323 HOH D O   1 
HETATM 7034 O O   . HOH J 6 .   ? 19.096 4.057   -62.796 1.00 39.32  ? 324 HOH D O   1 
HETATM 7035 O O   . HOH J 6 .   ? 12.977 8.644   -55.596 1.00 40.40  ? 325 HOH D O   1 
HETATM 7036 O O   . HOH J 6 .   ? 17.433 4.243   -31.164 1.00 37.33  ? 326 HOH D O   1 
HETATM 7037 O O   . HOH J 6 .   ? 9.540  -36.937 -61.095 1.00 52.32  ? 327 HOH D O   1 
HETATM 7038 O O   . HOH J 6 .   ? 9.189  -26.632 -85.846 1.00 52.15  ? 328 HOH D O   1 
HETATM 7039 O O   . HOH J 6 .   ? 10.484 -12.071 -45.873 1.00 25.48  ? 329 HOH D O   1 
HETATM 7040 O O   . HOH J 6 .   ? 6.114  -1.680  -48.993 1.00 25.10  ? 330 HOH D O   1 
HETATM 7041 O O   . HOH J 6 .   ? 18.083 -19.257 -71.837 1.00 27.78  ? 331 HOH D O   1 
HETATM 7042 O O   . HOH J 6 .   ? 14.652 -19.283 -78.383 1.00 35.40  ? 332 HOH D O   1 
HETATM 7043 O O   . HOH J 6 .   ? 5.092  -4.933  -37.534 1.00 31.11  ? 333 HOH D O   1 
HETATM 7044 O O   . HOH J 6 .   ? 13.274 -13.300 -72.810 1.00 32.39  ? 334 HOH D O   1 
HETATM 7045 O O   . HOH J 6 .   ? 2.371  4.559   -47.583 1.00 28.26  ? 335 HOH D O   1 
HETATM 7046 O O   . HOH J 6 .   ? 18.021 -12.025 -62.127 1.00 39.33  ? 336 HOH D O   1 
HETATM 7047 O O   . HOH J 6 .   ? 9.508  -18.161 -81.272 1.00 35.86  ? 337 HOH D O   1 
HETATM 7048 O O   . HOH J 6 .   ? 7.570  -17.561 -62.541 1.00 47.16  ? 338 HOH D O   1 
HETATM 7049 O O   . HOH J 6 .   ? 2.536  -5.021  -59.569 1.00 36.01  ? 339 HOH D O   1 
HETATM 7050 O O   . HOH J 6 .   ? 6.855  -13.933 -75.456 1.00 41.52  ? 340 HOH D O   1 
HETATM 7051 O O   . HOH J 6 .   ? 16.689 -15.390 -80.965 1.00 41.37  ? 341 HOH D O   1 
HETATM 7052 O O   . HOH J 6 .   ? 2.794  -2.222  -49.234 1.00 37.07  ? 342 HOH D O   1 
HETATM 7053 O O   . HOH J 6 .   ? 16.035 1.893   -33.253 1.00 28.88  ? 343 HOH D O   1 
HETATM 7054 O O   . HOH J 6 .   ? 22.265 -4.528  -54.269 1.00 48.08  ? 344 HOH D O   1 
HETATM 7055 O O   . HOH J 6 .   ? 23.841 0.431   -46.524 1.00 39.50  ? 345 HOH D O   1 
HETATM 7056 O O   . HOH J 6 .   ? 15.840 -4.665  -70.059 1.00 45.72  ? 346 HOH D O   1 
HETATM 7057 O O   . HOH J 6 .   ? 1.120  -0.505  -46.552 1.00 31.05  ? 347 HOH D O   1 
HETATM 7058 O O   . HOH J 6 .   ? 13.998 -19.059 -61.324 1.00 40.65  ? 348 HOH D O   1 
HETATM 7059 O O   . HOH J 6 .   ? 3.806  -5.685  -43.220 1.00 43.48  ? 349 HOH D O   1 
HETATM 7060 O O   . HOH J 6 .   ? 9.350  10.421  -52.545 1.00 37.19  ? 350 HOH D O   1 
HETATM 7061 O O   . HOH J 6 .   ? 15.051 -11.076 -51.998 1.00 38.36  ? 351 HOH D O   1 
HETATM 7062 O O   . HOH J 6 .   ? 12.183 7.357   -62.773 1.00 46.13  ? 352 HOH D O   1 
HETATM 7063 O O   . HOH J 6 .   ? 20.513 7.024   -47.051 1.00 36.50  ? 353 HOH D O   1 
HETATM 7064 O O   . HOH J 6 .   ? -0.224 13.270  -43.025 1.00 40.56  ? 354 HOH D O   1 
HETATM 7065 O O   . HOH J 6 .   ? 9.212  -6.533  -35.780 1.00 30.94  ? 355 HOH D O   1 
HETATM 7066 O O   . HOH J 6 .   ? 14.523 -8.897  -62.193 1.00 40.82  ? 356 HOH D O   1 
HETATM 7067 O O   . HOH J 6 .   ? 0.012  8.491   -32.029 1.00 49.72  ? 357 HOH D O   1 
HETATM 7068 O O   . HOH J 6 .   ? 9.512  -7.278  -72.110 1.00 44.09  ? 358 HOH D O   1 
HETATM 7069 O O   . HOH J 6 .   ? 5.510  -27.159 -73.291 1.00 42.79  ? 359 HOH D O   1 
HETATM 7070 O O   . HOH J 6 .   ? 0.554  -8.818  -54.434 1.00 49.34  ? 360 HOH D O   1 
HETATM 7071 O O   . HOH J 6 .   ? 17.993 -7.630  -74.407 1.00 37.44  ? 361 HOH D O   1 
HETATM 7072 O O   . HOH J 6 .   ? 15.639 -29.343 -78.112 1.00 37.73  ? 362 HOH D O   1 
HETATM 7073 O O   . HOH J 6 .   ? 2.693  -26.534 -73.629 1.00 44.73  ? 363 HOH D O   1 
HETATM 7074 O O   . HOH J 6 .   ? 17.057 -17.068 -70.175 1.00 31.11  ? 364 HOH D O   1 
HETATM 7075 O O   . HOH J 6 .   ? 17.035 -15.140 -78.333 1.00 37.95  ? 365 HOH D O   1 
HETATM 7076 O O   . HOH J 6 .   ? 19.135 -2.956  -65.320 1.00 40.81  ? 366 HOH D O   1 
HETATM 7077 O O   . HOH J 6 .   ? 5.474  -9.861  -48.384 1.00 37.80  ? 367 HOH D O   1 
HETATM 7078 O O   . HOH J 6 .   ? 15.249 -13.231 -62.048 1.00 32.24  ? 368 HOH D O   1 
HETATM 7079 O O   . HOH J 6 .   ? 9.254  12.686  -51.360 1.00 41.39  ? 369 HOH D O   1 
HETATM 7080 O O   . HOH J 6 .   ? -2.119 11.902  -36.486 1.00 45.09  ? 370 HOH D O   1 
HETATM 7081 O O   . HOH J 6 .   ? 11.193 -11.802 -52.351 1.00 37.41  ? 371 HOH D O   1 
HETATM 7082 O O   . HOH J 6 .   ? -1.143 4.555   -40.585 1.00 37.37  ? 372 HOH D O   1 
HETATM 7083 O O   . HOH J 6 .   ? -0.896 -11.929 -50.884 1.00 48.63  ? 373 HOH D O   1 
HETATM 7084 O O   . HOH J 6 .   ? 21.193 4.252   -50.158 1.00 32.35  ? 374 HOH D O   1 
HETATM 7085 O O   . HOH J 6 .   ? -1.055 5.081   -34.180 1.00 35.41  ? 375 HOH D O   1 
HETATM 7086 O O   . HOH J 6 .   ? 22.243 -31.739 -74.766 1.00 43.79  ? 376 HOH D O   1 
HETATM 7087 O O   . HOH J 6 .   ? 6.271  4.900   -63.026 1.00 40.32  ? 377 HOH D O   1 
HETATM 7088 O O   . HOH J 6 .   ? -0.623 -0.440  -49.942 1.00 42.24  ? 378 HOH D O   1 
HETATM 7089 O O   . HOH J 6 .   ? 5.594  -30.142 -58.308 1.00 48.95  ? 379 HOH D O   1 
HETATM 7090 O O   . HOH J 6 .   ? 12.795 -9.895  -56.353 1.00 35.43  ? 380 HOH D O   1 
HETATM 7091 O O   . HOH J 6 .   ? 9.230  -4.584  -68.937 1.00 40.72  ? 381 HOH D O   1 
HETATM 7092 O O   . HOH J 6 .   ? 20.761 5.368   -55.225 1.00 38.87  ? 382 HOH D O   1 
HETATM 7093 O O   . HOH J 6 .   ? 21.972 6.119   -52.038 1.00 49.71  ? 383 HOH D O   1 
HETATM 7094 O O   . HOH J 6 .   ? 12.132 -37.860 -68.597 1.00 51.34  ? 384 HOH D O   1 
HETATM 7095 O O   . HOH J 6 .   ? 11.255 10.419  -57.213 1.00 44.54  ? 385 HOH D O   1 
HETATM 7096 O O   . HOH J 6 .   ? 16.282 -8.979  -75.630 1.00 42.92  ? 386 HOH D O   1 
HETATM 7097 O O   . HOH J 6 .   ? 15.832 15.529  -36.121 1.00 45.17  ? 387 HOH D O   1 
HETATM 7098 O O   . HOH J 6 .   ? 8.363  9.186   -27.765 1.00 44.63  ? 388 HOH D O   1 
HETATM 7099 O O   . HOH J 6 .   ? 4.671  8.504   -52.293 1.00 35.30  ? 389 HOH D O   1 
HETATM 7100 O O   . HOH J 6 .   ? 12.692 -10.880 -53.445 1.00 51.23  ? 390 HOH D O   1 
HETATM 7101 O O   . HOH J 6 .   ? 16.295 -35.402 -64.697 1.00 48.22  ? 391 HOH D O   1 
HETATM 7102 O O   . HOH J 6 .   ? 2.487  8.000   -50.615 1.00 39.29  ? 392 HOH D O   1 
HETATM 7103 O O   . HOH J 6 .   ? 28.600 -13.499 -74.601 1.00 43.86  ? 393 HOH D O   1 
HETATM 7104 O O   . HOH J 6 .   ? 2.719  -9.181  -45.837 1.00 43.20  ? 394 HOH D O   1 
HETATM 7105 O O   . HOH J 6 .   ? -1.390 0.745   -47.770 1.00 39.93  ? 395 HOH D O   1 
HETATM 7106 O O   . HOH J 6 .   ? 17.137 -35.239 -61.903 1.00 42.22  ? 396 HOH D O   1 
# 
