data_8YIV
# 
_entry.id   8YIV 
# 
_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   8YIV         pdb_00008yiv 10.2210/pdb8yiv/pdb 
WWPDB D_1300045748 ?            ?                   
# 
_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                        8YIV 
_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 'MHC class I antigen'                   31897.266 1   ? ? ? ? 
2 polymer     syn ILE-LEU-ASP-THR-ALA-GLY-LYS-GLU-GLU-TYR 1139.233  1   ? ? ? ? 
3 polymer     man Beta-2-microglobulin                    11879.356 1   ? ? ? ? 
4 polymer     man 'TCR ALPHA'                             23074.811 1   ? ? ? ? 
5 polymer     man 'TCR beta'                              28186.664 1   ? ? ? ? 
6 non-polymer syn GLYCEROL                                92.094    8   ? ? ? ? 
7 non-polymer syn 1,2-ETHANEDIOL                          62.068    2   ? ? ? ? 
8 water       nat water                                   18.015    547 ? ? ? ? 
# 
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 ILDTAGKEEY ILDTAGKEEY C ? 
3 'polypeptide(L)' no no 
;MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
;
;MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
;
B ? 
4 'polypeptide(L)' no no 
;MAQKVTQAQSSVSMPVRKAVTLNCLYETSWWSYYIFWYKQLPSKEMIFLIRQGSDEQNAKSGRYSVNFKKAAKSVALTIS
ALQLEDSAKYFCALGDTAGKSTFGDGTTLTVKPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDK
CVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS
;
;MAQKVTQAQSSVSMPVRKAVTLNCLYETSWWSYYIFWYKQLPSKEMIFLIRQGSDEQNAKSGRYSVNFKKAAKSVALTIS
ALQLEDSAKYFCALGDTAGKSTFGDGTTLTVKPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDK
CVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS
;
D ? 
5 'polypeptide(L)' no no 
;MEAQVTQNPRYLITVTGKKLTVTCSQNMNHEYMSWYRQDPGLGLRQIYYSMNVEVTDKGDVPEGYKVSRKEKRNFPLILE
SPSPNQTSLYFCASSLVSTPLPKETQYFGPGTRLLVLEDLKNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVEL
SWWVNGKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSA
EAWGRAD
;
;MEAQVTQNPRYLITVTGKKLTVTCSQNMNHEYMSWYRQDPGLGLRQIYYSMNVEVTDKGDVPEGYKVSRKEKRNFPLILE
SPSPNQTSLYFCASSLVSTPLPKETQYFGPGTRLLVLEDLKNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVEL
SWWVNGKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSA
EAWGRAD
;
E ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
6 GLYCEROL       GOL 
7 1,2-ETHANEDIOL EDO 
8 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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   ILE n 
2 2   LEU n 
2 3   ASP n 
2 4   THR n 
2 5   ALA n 
2 6   GLY n 
2 7   LYS n 
2 8   GLU n 
2 9   GLU n 
2 10  TYR n 
3 1   MET n 
3 2   ILE n 
3 3   GLN n 
3 4   ARG n 
3 5   THR n 
3 6   PRO n 
3 7   LYS n 
3 8   ILE n 
3 9   GLN n 
3 10  VAL n 
3 11  TYR n 
3 12  SER n 
3 13  ARG n 
3 14  HIS n 
3 15  PRO n 
3 16  ALA n 
3 17  GLU n 
3 18  ASN n 
3 19  GLY n 
3 20  LYS n 
3 21  SER n 
3 22  ASN n 
3 23  PHE n 
3 24  LEU n 
3 25  ASN n 
3 26  CYS n 
3 27  TYR n 
3 28  VAL n 
3 29  SER n 
3 30  GLY n 
3 31  PHE n 
3 32  HIS n 
3 33  PRO n 
3 34  SER n 
3 35  ASP n 
3 36  ILE n 
3 37  GLU n 
3 38  VAL n 
3 39  ASP n 
3 40  LEU n 
3 41  LEU n 
3 42  LYS n 
3 43  ASN n 
3 44  GLY n 
3 45  GLU n 
3 46  ARG n 
3 47  ILE n 
3 48  GLU n 
3 49  LYS n 
3 50  VAL n 
3 51  GLU n 
3 52  HIS n 
3 53  SER n 
3 54  ASP n 
3 55  LEU n 
3 56  SER n 
3 57  PHE n 
3 58  SER n 
3 59  LYS n 
3 60  ASP n 
3 61  TRP n 
3 62  SER n 
3 63  PHE n 
3 64  TYR n 
3 65  LEU n 
3 66  LEU n 
3 67  TYR n 
3 68  TYR n 
3 69  THR n 
3 70  GLU n 
3 71  PHE n 
3 72  THR n 
3 73  PRO n 
3 74  THR n 
3 75  GLU n 
3 76  LYS n 
3 77  ASP n 
3 78  GLU n 
3 79  TYR n 
3 80  ALA n 
3 81  CYS n 
3 82  ARG n 
3 83  VAL n 
3 84  ASN n 
3 85  HIS n 
3 86  VAL n 
3 87  THR n 
3 88  LEU n 
3 89  SER n 
3 90  GLN n 
3 91  PRO n 
3 92  LYS n 
3 93  ILE n 
3 94  VAL n 
3 95  LYS n 
3 96  TRP n 
3 97  ASP n 
3 98  ARG n 
3 99  ASP n 
3 100 MET n 
4 1   MET n 
4 2   ALA n 
4 3   GLN n 
4 4   LYS n 
4 5   VAL n 
4 6   THR n 
4 7   GLN n 
4 8   ALA n 
4 9   GLN n 
4 10  SER n 
4 11  SER n 
4 12  VAL n 
4 13  SER n 
4 14  MET n 
4 15  PRO n 
4 16  VAL n 
4 17  ARG n 
4 18  LYS n 
4 19  ALA n 
4 20  VAL n 
4 21  THR n 
4 22  LEU n 
4 23  ASN n 
4 24  CYS n 
4 25  LEU n 
4 26  TYR n 
4 27  GLU n 
4 28  THR n 
4 29  SER n 
4 30  TRP n 
4 31  TRP n 
4 32  SER n 
4 33  TYR n 
4 34  TYR n 
4 35  ILE n 
4 36  PHE n 
4 37  TRP n 
4 38  TYR n 
4 39  LYS n 
4 40  GLN n 
4 41  LEU n 
4 42  PRO n 
4 43  SER n 
4 44  LYS n 
4 45  GLU n 
4 46  MET n 
4 47  ILE n 
4 48  PHE n 
4 49  LEU n 
4 50  ILE n 
4 51  ARG n 
4 52  GLN n 
4 53  GLY n 
4 54  SER n 
4 55  ASP n 
4 56  GLU n 
4 57  GLN n 
4 58  ASN n 
4 59  ALA n 
4 60  LYS n 
4 61  SER n 
4 62  GLY n 
4 63  ARG n 
4 64  TYR n 
4 65  SER n 
4 66  VAL n 
4 67  ASN n 
4 68  PHE n 
4 69  LYS n 
4 70  LYS n 
4 71  ALA n 
4 72  ALA n 
4 73  LYS n 
4 74  SER n 
4 75  VAL n 
4 76  ALA n 
4 77  LEU n 
4 78  THR n 
4 79  ILE n 
4 80  SER n 
4 81  ALA n 
4 82  LEU n 
4 83  GLN n 
4 84  LEU n 
4 85  GLU n 
4 86  ASP n 
4 87  SER n 
4 88  ALA n 
4 89  LYS n 
4 90  TYR n 
4 91  PHE n 
4 92  CYS n 
4 93  ALA n 
4 94  LEU n 
4 95  GLY n 
4 96  ASP n 
4 97  THR n 
4 98  ALA n 
4 99  GLY n 
4 100 LYS n 
4 101 SER n 
4 102 THR n 
4 103 PHE n 
4 104 GLY n 
4 105 ASP n 
4 106 GLY n 
4 107 THR n 
4 108 THR n 
4 109 LEU n 
4 110 THR n 
4 111 VAL n 
4 112 LYS n 
4 113 PRO n 
4 114 ASN n 
4 115 ILE n 
4 116 GLN n 
4 117 ASN n 
4 118 PRO n 
4 119 ASP n 
4 120 PRO n 
4 121 ALA n 
4 122 VAL n 
4 123 TYR n 
4 124 GLN n 
4 125 LEU n 
4 126 ARG n 
4 127 ASP n 
4 128 SER n 
4 129 LYS n 
4 130 SER n 
4 131 SER n 
4 132 ASP n 
4 133 LYS n 
4 134 SER n 
4 135 VAL n 
4 136 CYS n 
4 137 LEU n 
4 138 PHE n 
4 139 THR n 
4 140 ASP n 
4 141 PHE n 
4 142 ASP n 
4 143 SER n 
4 144 GLN n 
4 145 THR n 
4 146 ASN n 
4 147 VAL n 
4 148 SER n 
4 149 GLN n 
4 150 SER n 
4 151 LYS n 
4 152 ASP n 
4 153 SER n 
4 154 ASP n 
4 155 VAL n 
4 156 TYR n 
4 157 ILE n 
4 158 THR n 
4 159 ASP n 
4 160 LYS n 
4 161 CYS n 
4 162 VAL n 
4 163 LEU n 
4 164 ASP n 
4 165 MET n 
4 166 ARG n 
4 167 SER n 
4 168 MET n 
4 169 ASP n 
4 170 PHE n 
4 171 LYS n 
4 172 SER n 
4 173 ASN n 
4 174 SER n 
4 175 ALA n 
4 176 VAL n 
4 177 ALA n 
4 178 TRP n 
4 179 SER n 
4 180 ASN n 
4 181 LYS n 
4 182 SER n 
4 183 ASP n 
4 184 PHE n 
4 185 ALA n 
4 186 CYS n 
4 187 ALA n 
4 188 ASN n 
4 189 ALA n 
4 190 PHE n 
4 191 ASN n 
4 192 ASN n 
4 193 SER n 
4 194 ILE n 
4 195 ILE n 
4 196 PRO n 
4 197 GLU n 
4 198 ASP n 
4 199 THR n 
4 200 PHE n 
4 201 PHE n 
4 202 PRO n 
4 203 SER n 
4 204 PRO n 
4 205 GLU n 
4 206 SER n 
4 207 SER n 
5 1   MET n 
5 2   GLU n 
5 3   ALA n 
5 4   GLN n 
5 5   VAL n 
5 6   THR n 
5 7   GLN n 
5 8   ASN n 
5 9   PRO n 
5 10  ARG n 
5 11  TYR n 
5 12  LEU n 
5 13  ILE n 
5 14  THR n 
5 15  VAL n 
5 16  THR n 
5 17  GLY n 
5 18  LYS n 
5 19  LYS n 
5 20  LEU n 
5 21  THR n 
5 22  VAL n 
5 23  THR n 
5 24  CYS n 
5 25  SER n 
5 26  GLN n 
5 27  ASN n 
5 28  MET n 
5 29  ASN n 
5 30  HIS n 
5 31  GLU n 
5 32  TYR n 
5 33  MET n 
5 34  SER n 
5 35  TRP n 
5 36  TYR n 
5 37  ARG n 
5 38  GLN n 
5 39  ASP n 
5 40  PRO n 
5 41  GLY n 
5 42  LEU n 
5 43  GLY n 
5 44  LEU n 
5 45  ARG n 
5 46  GLN n 
5 47  ILE n 
5 48  TYR n 
5 49  TYR n 
5 50  SER n 
5 51  MET n 
5 52  ASN n 
5 53  VAL n 
5 54  GLU n 
5 55  VAL n 
5 56  THR n 
5 57  ASP n 
5 58  LYS n 
5 59  GLY n 
5 60  ASP n 
5 61  VAL n 
5 62  PRO n 
5 63  GLU n 
5 64  GLY n 
5 65  TYR n 
5 66  LYS n 
5 67  VAL n 
5 68  SER n 
5 69  ARG n 
5 70  LYS n 
5 71  GLU n 
5 72  LYS n 
5 73  ARG n 
5 74  ASN n 
5 75  PHE n 
5 76  PRO n 
5 77  LEU n 
5 78  ILE n 
5 79  LEU n 
5 80  GLU n 
5 81  SER n 
5 82  PRO n 
5 83  SER n 
5 84  PRO n 
5 85  ASN n 
5 86  GLN n 
5 87  THR n 
5 88  SER n 
5 89  LEU n 
5 90  TYR n 
5 91  PHE n 
5 92  CYS n 
5 93  ALA n 
5 94  SER n 
5 95  SER n 
5 96  LEU n 
5 97  VAL n 
5 98  SER n 
5 99  THR n 
5 100 PRO n 
5 101 LEU n 
5 102 PRO n 
5 103 LYS n 
5 104 GLU n 
5 105 THR n 
5 106 GLN n 
5 107 TYR n 
5 108 PHE n 
5 109 GLY n 
5 110 PRO n 
5 111 GLY n 
5 112 THR n 
5 113 ARG n 
5 114 LEU n 
5 115 LEU n 
5 116 VAL n 
5 117 LEU n 
5 118 GLU n 
5 119 ASP n 
5 120 LEU n 
5 121 LYS n 
5 122 ASN n 
5 123 VAL n 
5 124 PHE n 
5 125 PRO n 
5 126 PRO n 
5 127 GLU n 
5 128 VAL n 
5 129 ALA n 
5 130 VAL n 
5 131 PHE n 
5 132 GLU n 
5 133 PRO n 
5 134 SER n 
5 135 GLU n 
5 136 ALA n 
5 137 GLU n 
5 138 ILE n 
5 139 SER n 
5 140 HIS n 
5 141 THR n 
5 142 GLN n 
5 143 LYS n 
5 144 ALA n 
5 145 THR n 
5 146 LEU n 
5 147 VAL n 
5 148 CYS n 
5 149 LEU n 
5 150 ALA n 
5 151 THR n 
5 152 GLY n 
5 153 PHE n 
5 154 TYR n 
5 155 PRO n 
5 156 ASP n 
5 157 HIS n 
5 158 VAL n 
5 159 GLU n 
5 160 LEU n 
5 161 SER n 
5 162 TRP n 
5 163 TRP n 
5 164 VAL n 
5 165 ASN n 
5 166 GLY n 
5 167 LYS n 
5 168 GLU n 
5 169 VAL n 
5 170 HIS n 
5 171 SER n 
5 172 GLY n 
5 173 VAL n 
5 174 CYS n 
5 175 THR n 
5 176 ASP n 
5 177 PRO n 
5 178 GLN n 
5 179 PRO n 
5 180 LEU n 
5 181 LYS n 
5 182 GLU n 
5 183 GLN n 
5 184 PRO n 
5 185 ALA n 
5 186 LEU n 
5 187 ASN n 
5 188 ASP n 
5 189 SER n 
5 190 ARG n 
5 191 TYR n 
5 192 ALA n 
5 193 LEU n 
5 194 SER n 
5 195 SER n 
5 196 ARG n 
5 197 LEU n 
5 198 ARG n 
5 199 VAL n 
5 200 SER n 
5 201 ALA n 
5 202 THR n 
5 203 PHE n 
5 204 TRP n 
5 205 GLN n 
5 206 ASN n 
5 207 PRO n 
5 208 ARG n 
5 209 ASN n 
5 210 HIS n 
5 211 PHE n 
5 212 ARG n 
5 213 CYS n 
5 214 GLN n 
5 215 VAL n 
5 216 GLN n 
5 217 PHE n 
5 218 TYR n 
5 219 GLY n 
5 220 LEU n 
5 221 SER n 
5 222 GLU n 
5 223 ASN n 
5 224 ASP n 
5 225 GLU n 
5 226 TRP n 
5 227 THR n 
5 228 GLN n 
5 229 ASP n 
5 230 ARG n 
5 231 ALA n 
5 232 LYS n 
5 233 PRO n 
5 234 VAL n 
5 235 THR n 
5 236 GLN n 
5 237 ILE n 
5 238 VAL n 
5 239 SER n 
5 240 ALA n 
5 241 GLU n 
5 242 ALA n 
5 243 TRP n 
5 244 GLY n 
5 245 ARG n 
5 246 ALA n 
5 247 ASP 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 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 100 human ? B2M   ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 207 ?     ? ?     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5 1 sample 'Biological sequence' 1 247 ?     ? ?     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_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 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL'               'C2 H6 O2'       62.068  
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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   ILE 1   1   1   ILE ILE C . n 
B 2 2   LEU 2   2   2   LEU LEU C . n 
B 2 3   ASP 3   3   3   ASP ASP C . n 
B 2 4   THR 4   4   4   THR THR C . n 
B 2 5   ALA 5   5   5   ALA ALA C . n 
B 2 6   GLY 6   6   6   GLY GLY C . n 
B 2 7   LYS 7   7   7   LYS LYS C . n 
B 2 8   GLU 8   8   8   GLU GLU C . n 
B 2 9   GLU 9   9   9   GLU GLU C . n 
B 2 10  TYR 10  10  10  TYR TYR C . n 
C 3 1   MET 1   0   0   MET MET B . n 
C 3 2   ILE 2   1   1   ILE ILE B . n 
C 3 3   GLN 3   2   2   GLN GLN B . n 
C 3 4   ARG 4   3   3   ARG ARG B . n 
C 3 5   THR 5   4   4   THR THR B . n 
C 3 6   PRO 6   5   5   PRO PRO B . n 
C 3 7   LYS 7   6   6   LYS LYS B . n 
C 3 8   ILE 8   7   7   ILE ILE B . n 
C 3 9   GLN 9   8   8   GLN GLN B . n 
C 3 10  VAL 10  9   9   VAL VAL B . n 
C 3 11  TYR 11  10  10  TYR TYR B . n 
C 3 12  SER 12  11  11  SER SER B . n 
C 3 13  ARG 13  12  12  ARG ARG B . n 
C 3 14  HIS 14  13  13  HIS HIS B . n 
C 3 15  PRO 15  14  14  PRO PRO B . n 
C 3 16  ALA 16  15  15  ALA ALA B . n 
C 3 17  GLU 17  16  16  GLU GLU B . n 
C 3 18  ASN 18  17  17  ASN ASN B . n 
C 3 19  GLY 19  18  18  GLY GLY B . n 
C 3 20  LYS 20  19  19  LYS LYS B . n 
C 3 21  SER 21  20  20  SER SER B . n 
C 3 22  ASN 22  21  21  ASN ASN B . n 
C 3 23  PHE 23  22  22  PHE PHE B . n 
C 3 24  LEU 24  23  23  LEU LEU B . n 
C 3 25  ASN 25  24  24  ASN ASN B . n 
C 3 26  CYS 26  25  25  CYS CYS B . n 
C 3 27  TYR 27  26  26  TYR TYR B . n 
C 3 28  VAL 28  27  27  VAL VAL B . n 
C 3 29  SER 29  28  28  SER SER B . n 
C 3 30  GLY 30  29  29  GLY GLY B . n 
C 3 31  PHE 31  30  30  PHE PHE B . n 
C 3 32  HIS 32  31  31  HIS HIS B . n 
C 3 33  PRO 33  32  32  PRO PRO B . n 
C 3 34  SER 34  33  33  SER SER B . n 
C 3 35  ASP 35  34  34  ASP ASP B . n 
C 3 36  ILE 36  35  35  ILE ILE B . n 
C 3 37  GLU 37  36  36  GLU GLU B . n 
C 3 38  VAL 38  37  37  VAL VAL B . n 
C 3 39  ASP 39  38  38  ASP ASP B . n 
C 3 40  LEU 40  39  39  LEU LEU B . n 
C 3 41  LEU 41  40  40  LEU LEU B . n 
C 3 42  LYS 42  41  41  LYS LYS B . n 
C 3 43  ASN 43  42  42  ASN ASN B . n 
C 3 44  GLY 44  43  43  GLY GLY B . n 
C 3 45  GLU 45  44  44  GLU GLU B . n 
C 3 46  ARG 46  45  45  ARG ARG B . n 
C 3 47  ILE 47  46  46  ILE ILE B . n 
C 3 48  GLU 48  47  47  GLU GLU B . n 
C 3 49  LYS 49  48  48  LYS LYS B . n 
C 3 50  VAL 50  49  49  VAL VAL B . n 
C 3 51  GLU 51  50  50  GLU GLU B . n 
C 3 52  HIS 52  51  51  HIS HIS B . n 
C 3 53  SER 53  52  52  SER SER B . n 
C 3 54  ASP 54  53  53  ASP ASP B . n 
C 3 55  LEU 55  54  54  LEU LEU B . n 
C 3 56  SER 56  55  55  SER SER B . n 
C 3 57  PHE 57  56  56  PHE PHE B . n 
C 3 58  SER 58  57  57  SER SER B . n 
C 3 59  LYS 59  58  58  LYS LYS B . n 
C 3 60  ASP 60  59  59  ASP ASP B . n 
C 3 61  TRP 61  60  60  TRP TRP B . n 
C 3 62  SER 62  61  61  SER SER B . n 
C 3 63  PHE 63  62  62  PHE PHE B . n 
C 3 64  TYR 64  63  63  TYR TYR B . n 
C 3 65  LEU 65  64  64  LEU LEU B . n 
C 3 66  LEU 66  65  65  LEU LEU B . n 
C 3 67  TYR 67  66  66  TYR TYR B . n 
C 3 68  TYR 68  67  67  TYR TYR B . n 
C 3 69  THR 69  68  68  THR THR B . n 
C 3 70  GLU 70  69  69  GLU GLU B . n 
C 3 71  PHE 71  70  70  PHE PHE B . n 
C 3 72  THR 72  71  71  THR THR B . n 
C 3 73  PRO 73  72  72  PRO PRO B . n 
C 3 74  THR 74  73  73  THR THR B . n 
C 3 75  GLU 75  74  74  GLU GLU B . n 
C 3 76  LYS 76  75  75  LYS LYS B . n 
C 3 77  ASP 77  76  76  ASP ASP B . n 
C 3 78  GLU 78  77  77  GLU GLU B . n 
C 3 79  TYR 79  78  78  TYR TYR B . n 
C 3 80  ALA 80  79  79  ALA ALA B . n 
C 3 81  CYS 81  80  80  CYS CYS B . n 
C 3 82  ARG 82  81  81  ARG ARG B . n 
C 3 83  VAL 83  82  82  VAL VAL B . n 
C 3 84  ASN 84  83  83  ASN ASN B . n 
C 3 85  HIS 85  84  84  HIS HIS B . n 
C 3 86  VAL 86  85  85  VAL VAL B . n 
C 3 87  THR 87  86  86  THR THR B . n 
C 3 88  LEU 88  87  87  LEU LEU B . n 
C 3 89  SER 89  88  88  SER SER B . n 
C 3 90  GLN 90  89  89  GLN GLN B . n 
C 3 91  PRO 91  90  90  PRO PRO B . n 
C 3 92  LYS 92  91  91  LYS LYS B . n 
C 3 93  ILE 93  92  92  ILE ILE B . n 
C 3 94  VAL 94  93  93  VAL VAL B . n 
C 3 95  LYS 95  94  94  LYS LYS B . n 
C 3 96  TRP 96  95  95  TRP TRP B . n 
C 3 97  ASP 97  96  96  ASP ASP B . n 
C 3 98  ARG 98  97  97  ARG ARG B . n 
C 3 99  ASP 99  98  98  ASP ASP B . n 
C 3 100 MET 100 99  99  MET MET B . n 
D 4 1   MET 1   0   ?   ?   ?   D . n 
D 4 2   ALA 2   1   1   ALA ALA D . n 
D 4 3   GLN 3   2   2   GLN GLN D . n 
D 4 4   LYS 4   3   3   LYS LYS D . n 
D 4 5   VAL 5   4   4   VAL VAL D . n 
D 4 6   THR 6   5   5   THR THR D . n 
D 4 7   GLN 7   6   6   GLN GLN D . n 
D 4 8   ALA 8   7   7   ALA ALA D . n 
D 4 9   GLN 9   8   8   GLN GLN D . n 
D 4 10  SER 10  9   9   SER SER D . n 
D 4 11  SER 11  10  10  SER SER D . n 
D 4 12  VAL 12  11  11  VAL VAL D . n 
D 4 13  SER 13  12  12  SER SER D . n 
D 4 14  MET 14  13  13  MET MET D . n 
D 4 15  PRO 15  14  14  PRO PRO D . n 
D 4 16  VAL 16  15  15  VAL VAL D . n 
D 4 17  ARG 17  16  16  ARG ARG D . n 
D 4 18  LYS 18  17  17  LYS LYS D . n 
D 4 19  ALA 19  18  18  ALA ALA D . n 
D 4 20  VAL 20  19  19  VAL VAL D . n 
D 4 21  THR 21  20  20  THR THR D . n 
D 4 22  LEU 22  21  21  LEU LEU D . n 
D 4 23  ASN 23  22  22  ASN ASN D . n 
D 4 24  CYS 24  23  23  CYS CYS D . n 
D 4 25  LEU 25  24  24  LEU LEU D . n 
D 4 26  TYR 26  25  25  TYR TYR D . n 
D 4 27  GLU 27  26  26  GLU GLU D . n 
D 4 28  THR 28  27  27  THR THR D . n 
D 4 29  SER 29  28  28  SER SER D . n 
D 4 30  TRP 30  29  29  TRP TRP D . n 
D 4 31  TRP 31  30  30  TRP TRP D . n 
D 4 32  SER 32  31  31  SER SER D . n 
D 4 33  TYR 33  32  32  TYR TYR D . n 
D 4 34  TYR 34  33  33  TYR TYR D . n 
D 4 35  ILE 35  34  34  ILE ILE D . n 
D 4 36  PHE 36  35  35  PHE PHE D . n 
D 4 37  TRP 37  36  36  TRP TRP D . n 
D 4 38  TYR 38  37  37  TYR TYR D . n 
D 4 39  LYS 39  38  38  LYS LYS D . n 
D 4 40  GLN 40  39  39  GLN GLN D . n 
D 4 41  LEU 41  40  40  LEU LEU D . n 
D 4 42  PRO 42  41  41  PRO PRO D . n 
D 4 43  SER 43  42  42  SER SER D . n 
D 4 44  LYS 44  43  43  LYS LYS D . n 
D 4 45  GLU 45  44  44  GLU GLU D . n 
D 4 46  MET 46  45  45  MET MET D . n 
D 4 47  ILE 47  46  46  ILE ILE D . n 
D 4 48  PHE 48  47  47  PHE PHE D . n 
D 4 49  LEU 49  48  48  LEU LEU D . n 
D 4 50  ILE 50  49  49  ILE ILE D . n 
D 4 51  ARG 51  50  50  ARG ARG D . n 
D 4 52  GLN 52  51  51  GLN GLN D . n 
D 4 53  GLY 53  52  52  GLY GLY D . n 
D 4 54  SER 54  53  53  SER SER D . n 
D 4 55  ASP 55  54  54  ASP ASP D . n 
D 4 56  GLU 56  55  55  GLU GLU D . n 
D 4 57  GLN 57  56  56  GLN GLN D . n 
D 4 58  ASN 58  57  57  ASN ASN D . n 
D 4 59  ALA 59  58  58  ALA ALA D . n 
D 4 60  LYS 60  59  59  LYS LYS D . n 
D 4 61  SER 61  60  60  SER SER D . n 
D 4 62  GLY 62  61  61  GLY GLY D . n 
D 4 63  ARG 63  62  62  ARG ARG D . n 
D 4 64  TYR 64  63  63  TYR TYR D . n 
D 4 65  SER 65  64  64  SER SER D . n 
D 4 66  VAL 66  65  65  VAL VAL D . n 
D 4 67  ASN 67  66  66  ASN ASN D . n 
D 4 68  PHE 68  67  67  PHE PHE D . n 
D 4 69  LYS 69  68  68  LYS LYS D . n 
D 4 70  LYS 70  69  69  LYS LYS D . n 
D 4 71  ALA 71  70  70  ALA ALA D . n 
D 4 72  ALA 72  71  71  ALA ALA D . n 
D 4 73  LYS 73  72  72  LYS LYS D . n 
D 4 74  SER 74  73  73  SER SER D . n 
D 4 75  VAL 75  74  74  VAL VAL D . n 
D 4 76  ALA 76  75  75  ALA ALA D . n 
D 4 77  LEU 77  76  76  LEU LEU D . n 
D 4 78  THR 78  77  77  THR THR D . n 
D 4 79  ILE 79  78  78  ILE ILE D . n 
D 4 80  SER 80  79  79  SER SER D . n 
D 4 81  ALA 81  80  80  ALA ALA D . n 
D 4 82  LEU 82  81  81  LEU LEU D . n 
D 4 83  GLN 83  82  82  GLN GLN D . n 
D 4 84  LEU 84  83  83  LEU LEU D . n 
D 4 85  GLU 85  84  84  GLU GLU D . n 
D 4 86  ASP 86  85  85  ASP ASP D . n 
D 4 87  SER 87  86  86  SER SER D . n 
D 4 88  ALA 88  87  87  ALA ALA D . n 
D 4 89  LYS 89  88  88  LYS LYS D . n 
D 4 90  TYR 90  89  89  TYR TYR D . n 
D 4 91  PHE 91  90  90  PHE PHE D . n 
D 4 92  CYS 92  91  91  CYS CYS D . n 
D 4 93  ALA 93  92  92  ALA ALA D . n 
D 4 94  LEU 94  93  93  LEU LEU D . n 
D 4 95  GLY 95  94  94  GLY GLY D . n 
D 4 96  ASP 96  95  95  ASP ASP D . n 
D 4 97  THR 97  96  96  THR THR D . n 
D 4 98  ALA 98  97  97  ALA ALA D . n 
D 4 99  GLY 99  98  98  GLY GLY D . n 
D 4 100 LYS 100 99  99  LYS LYS D . n 
D 4 101 SER 101 100 100 SER SER D . n 
D 4 102 THR 102 101 101 THR THR D . n 
D 4 103 PHE 103 102 102 PHE PHE D . n 
D 4 104 GLY 104 103 103 GLY GLY D . n 
D 4 105 ASP 105 104 104 ASP ASP D . n 
D 4 106 GLY 106 105 105 GLY GLY D . n 
D 4 107 THR 107 106 106 THR THR D . n 
D 4 108 THR 108 107 107 THR THR D . n 
D 4 109 LEU 109 108 108 LEU LEU D . n 
D 4 110 THR 110 109 109 THR THR D . n 
D 4 111 VAL 111 110 110 VAL VAL D . n 
D 4 112 LYS 112 111 111 LYS LYS D . n 
D 4 113 PRO 113 112 112 PRO PRO D . n 
D 4 114 ASN 114 113 113 ASN ASN D . n 
D 4 115 ILE 115 114 114 ILE ILE D . n 
D 4 116 GLN 116 115 115 GLN GLN D . n 
D 4 117 ASN 117 116 116 ASN ASN D . n 
D 4 118 PRO 118 117 117 PRO PRO D . n 
D 4 119 ASP 119 118 118 ASP ASP D . n 
D 4 120 PRO 120 119 119 PRO PRO D . n 
D 4 121 ALA 121 120 120 ALA ALA D . n 
D 4 122 VAL 122 121 121 VAL VAL D . n 
D 4 123 TYR 123 122 122 TYR TYR D . n 
D 4 124 GLN 124 123 123 GLN GLN D . n 
D 4 125 LEU 125 124 124 LEU LEU D . n 
D 4 126 ARG 126 125 125 ARG ARG D . n 
D 4 127 ASP 127 126 126 ASP ASP D . n 
D 4 128 SER 128 127 127 SER SER D . n 
D 4 129 LYS 129 128 128 LYS LYS D . n 
D 4 130 SER 130 129 129 SER SER D . n 
D 4 131 SER 131 130 130 SER SER D . n 
D 4 132 ASP 132 131 131 ASP ASP D . n 
D 4 133 LYS 133 132 132 LYS LYS D . n 
D 4 134 SER 134 133 133 SER SER D . n 
D 4 135 VAL 135 134 134 VAL VAL D . n 
D 4 136 CYS 136 135 135 CYS CYS D . n 
D 4 137 LEU 137 136 136 LEU LEU D . n 
D 4 138 PHE 138 137 137 PHE PHE D . n 
D 4 139 THR 139 138 138 THR THR D . n 
D 4 140 ASP 140 139 139 ASP ASP D . n 
D 4 141 PHE 141 140 140 PHE PHE D . n 
D 4 142 ASP 142 141 141 ASP ASP D . n 
D 4 143 SER 143 142 142 SER SER D . n 
D 4 144 GLN 144 143 143 GLN GLN D . n 
D 4 145 THR 145 144 144 THR THR D . n 
D 4 146 ASN 146 145 145 ASN ASN D . n 
D 4 147 VAL 147 146 146 VAL VAL D . n 
D 4 148 SER 148 147 147 SER SER D . n 
D 4 149 GLN 149 148 148 GLN GLN D . n 
D 4 150 SER 150 149 149 SER SER D . n 
D 4 151 LYS 151 150 150 LYS LYS D . n 
D 4 152 ASP 152 151 151 ASP ASP D . n 
D 4 153 SER 153 152 152 SER SER D . n 
D 4 154 ASP 154 153 153 ASP ASP D . n 
D 4 155 VAL 155 154 154 VAL VAL D . n 
D 4 156 TYR 156 155 155 TYR TYR D . n 
D 4 157 ILE 157 156 156 ILE ILE D . n 
D 4 158 THR 158 157 157 THR THR D . n 
D 4 159 ASP 159 158 158 ASP ASP D . n 
D 4 160 LYS 160 159 159 LYS LYS D . n 
D 4 161 CYS 161 160 160 CYS CYS D . n 
D 4 162 VAL 162 161 161 VAL VAL D . n 
D 4 163 LEU 163 162 162 LEU LEU D . n 
D 4 164 ASP 164 163 163 ASP ASP D . n 
D 4 165 MET 165 164 164 MET MET D . n 
D 4 166 ARG 166 165 165 ARG ARG D . n 
D 4 167 SER 167 166 166 SER SER D . n 
D 4 168 MET 168 167 167 MET MET D . n 
D 4 169 ASP 169 168 168 ASP ASP D . n 
D 4 170 PHE 170 169 169 PHE PHE D . n 
D 4 171 LYS 171 170 170 LYS LYS D . n 
D 4 172 SER 172 171 171 SER SER D . n 
D 4 173 ASN 173 172 172 ASN ASN D . n 
D 4 174 SER 174 173 173 SER SER D . n 
D 4 175 ALA 175 174 174 ALA ALA D . n 
D 4 176 VAL 176 175 175 VAL VAL D . n 
D 4 177 ALA 177 176 176 ALA ALA D . n 
D 4 178 TRP 178 177 177 TRP TRP D . n 
D 4 179 SER 179 178 178 SER SER D . n 
D 4 180 ASN 180 179 179 ASN ASN D . n 
D 4 181 LYS 181 180 180 LYS LYS D . n 
D 4 182 SER 182 181 181 SER SER D . n 
D 4 183 ASP 183 182 182 ASP ASP D . n 
D 4 184 PHE 184 183 183 PHE PHE D . n 
D 4 185 ALA 185 184 184 ALA ALA D . n 
D 4 186 CYS 186 185 185 CYS CYS D . n 
D 4 187 ALA 187 186 186 ALA ALA D . n 
D 4 188 ASN 188 187 187 ASN ASN D . n 
D 4 189 ALA 189 188 188 ALA ALA D . n 
D 4 190 PHE 190 189 189 PHE PHE D . n 
D 4 191 ASN 191 190 190 ASN ASN D . n 
D 4 192 ASN 192 191 191 ASN ASN D . n 
D 4 193 SER 193 192 192 SER SER D . n 
D 4 194 ILE 194 193 193 ILE ILE D . n 
D 4 195 ILE 195 194 194 ILE ILE D . n 
D 4 196 PRO 196 195 195 PRO PRO D . n 
D 4 197 GLU 197 196 196 GLU GLU D . n 
D 4 198 ASP 198 197 197 ASP ASP D . n 
D 4 199 THR 199 198 198 THR THR D . n 
D 4 200 PHE 200 199 199 PHE PHE D . n 
D 4 201 PHE 201 200 200 PHE PHE D . n 
D 4 202 PRO 202 201 201 PRO PRO D . n 
D 4 203 SER 203 202 202 SER SER D . n 
D 4 204 PRO 204 203 ?   ?   ?   D . n 
D 4 205 GLU 205 204 ?   ?   ?   D . n 
D 4 206 SER 206 205 ?   ?   ?   D . n 
D 4 207 SER 207 206 ?   ?   ?   D . n 
E 5 1   MET 1   0   0   MET MET E . n 
E 5 2   GLU 2   1   1   GLU GLU E . n 
E 5 3   ALA 3   2   2   ALA ALA E . n 
E 5 4   GLN 4   3   3   GLN GLN E . n 
E 5 5   VAL 5   4   4   VAL VAL E . n 
E 5 6   THR 6   5   5   THR THR E . n 
E 5 7   GLN 7   6   6   GLN GLN E . n 
E 5 8   ASN 8   7   7   ASN ASN E . n 
E 5 9   PRO 9   8   8   PRO PRO E . n 
E 5 10  ARG 10  9   9   ARG ARG E . n 
E 5 11  TYR 11  10  10  TYR TYR E . n 
E 5 12  LEU 12  11  11  LEU LEU E . n 
E 5 13  ILE 13  12  12  ILE ILE E . n 
E 5 14  THR 14  13  13  THR THR E . n 
E 5 15  VAL 15  14  14  VAL VAL E . n 
E 5 16  THR 16  15  15  THR THR E . n 
E 5 17  GLY 17  16  16  GLY GLY E . n 
E 5 18  LYS 18  17  17  LYS LYS E . n 
E 5 19  LYS 19  18  18  LYS LYS E . n 
E 5 20  LEU 20  19  19  LEU LEU E . n 
E 5 21  THR 21  20  20  THR THR E . n 
E 5 22  VAL 22  21  21  VAL VAL E . n 
E 5 23  THR 23  22  22  THR THR E . n 
E 5 24  CYS 24  23  23  CYS CYS E . n 
E 5 25  SER 25  24  24  SER SER E . n 
E 5 26  GLN 26  25  25  GLN GLN E . n 
E 5 27  ASN 27  26  26  ASN ASN E . n 
E 5 28  MET 28  27  27  MET MET E . n 
E 5 29  ASN 29  28  28  ASN ASN E . n 
E 5 30  HIS 30  29  29  HIS HIS E . n 
E 5 31  GLU 31  30  30  GLU GLU E . n 
E 5 32  TYR 32  31  31  TYR TYR E . n 
E 5 33  MET 33  32  32  MET MET E . n 
E 5 34  SER 34  33  33  SER SER E . n 
E 5 35  TRP 35  34  34  TRP TRP E . n 
E 5 36  TYR 36  35  35  TYR TYR E . n 
E 5 37  ARG 37  36  36  ARG ARG E . n 
E 5 38  GLN 38  37  37  GLN GLN E . n 
E 5 39  ASP 39  38  38  ASP ASP E . n 
E 5 40  PRO 40  39  39  PRO PRO E . n 
E 5 41  GLY 41  40  40  GLY GLY E . n 
E 5 42  LEU 42  41  41  LEU LEU E . n 
E 5 43  GLY 43  42  42  GLY GLY E . n 
E 5 44  LEU 44  43  43  LEU LEU E . n 
E 5 45  ARG 45  44  44  ARG ARG E . n 
E 5 46  GLN 46  45  45  GLN GLN E . n 
E 5 47  ILE 47  46  46  ILE ILE E . n 
E 5 48  TYR 48  47  47  TYR TYR E . n 
E 5 49  TYR 49  48  48  TYR TYR E . n 
E 5 50  SER 50  49  49  SER SER E . n 
E 5 51  MET 51  50  50  MET MET E . n 
E 5 52  ASN 52  51  51  ASN ASN E . n 
E 5 53  VAL 53  52  52  VAL VAL E . n 
E 5 54  GLU 54  53  53  GLU GLU E . n 
E 5 55  VAL 55  54  54  VAL VAL E . n 
E 5 56  THR 56  55  55  THR THR E . n 
E 5 57  ASP 57  56  56  ASP ASP E . n 
E 5 58  LYS 58  57  57  LYS LYS E . n 
E 5 59  GLY 59  58  58  GLY GLY E . n 
E 5 60  ASP 60  59  59  ASP ASP E . n 
E 5 61  VAL 61  60  60  VAL VAL E . n 
E 5 62  PRO 62  61  61  PRO PRO E . n 
E 5 63  GLU 63  62  62  GLU GLU E . n 
E 5 64  GLY 64  63  63  GLY GLY E . n 
E 5 65  TYR 65  64  64  TYR TYR E . n 
E 5 66  LYS 66  65  65  LYS LYS E . n 
E 5 67  VAL 67  66  66  VAL VAL E . n 
E 5 68  SER 68  67  67  SER SER E . n 
E 5 69  ARG 69  68  68  ARG ARG E . n 
E 5 70  LYS 70  69  69  LYS LYS E . n 
E 5 71  GLU 71  70  70  GLU GLU E . n 
E 5 72  LYS 72  71  71  LYS LYS E . n 
E 5 73  ARG 73  72  72  ARG ARG E . n 
E 5 74  ASN 74  73  73  ASN ASN E . n 
E 5 75  PHE 75  74  74  PHE PHE E . n 
E 5 76  PRO 76  75  75  PRO PRO E . n 
E 5 77  LEU 77  76  76  LEU LEU E . n 
E 5 78  ILE 78  77  77  ILE ILE E . n 
E 5 79  LEU 79  78  78  LEU LEU E . n 
E 5 80  GLU 80  79  79  GLU GLU E . n 
E 5 81  SER 81  80  80  SER SER E . n 
E 5 82  PRO 82  81  81  PRO PRO E . n 
E 5 83  SER 83  82  82  SER SER E . n 
E 5 84  PRO 84  83  83  PRO PRO E . n 
E 5 85  ASN 85  84  84  ASN ASN E . n 
E 5 86  GLN 86  85  85  GLN GLN E . n 
E 5 87  THR 87  86  86  THR THR E . n 
E 5 88  SER 88  87  87  SER SER E . n 
E 5 89  LEU 89  88  88  LEU LEU E . n 
E 5 90  TYR 90  89  89  TYR TYR E . n 
E 5 91  PHE 91  90  90  PHE PHE E . n 
E 5 92  CYS 92  91  91  CYS CYS E . n 
E 5 93  ALA 93  92  92  ALA ALA E . n 
E 5 94  SER 94  93  93  SER SER E . n 
E 5 95  SER 95  94  94  SER SER E . n 
E 5 96  LEU 96  95  95  LEU LEU E . n 
E 5 97  VAL 97  96  96  VAL VAL E . n 
E 5 98  SER 98  97  97  SER SER E . n 
E 5 99  THR 99  98  98  THR THR E . n 
E 5 100 PRO 100 99  99  PRO PRO E . n 
E 5 101 LEU 101 100 100 LEU LEU E . n 
E 5 102 PRO 102 101 101 PRO PRO E . n 
E 5 103 LYS 103 102 102 LYS LYS E . n 
E 5 104 GLU 104 103 103 GLU GLU E . n 
E 5 105 THR 105 104 104 THR THR E . n 
E 5 106 GLN 106 105 105 GLN GLN E . n 
E 5 107 TYR 107 106 106 TYR TYR E . n 
E 5 108 PHE 108 107 107 PHE PHE E . n 
E 5 109 GLY 109 108 108 GLY GLY E . n 
E 5 110 PRO 110 109 109 PRO PRO E . n 
E 5 111 GLY 111 110 110 GLY GLY E . n 
E 5 112 THR 112 111 111 THR THR E . n 
E 5 113 ARG 113 112 112 ARG ARG E . n 
E 5 114 LEU 114 113 113 LEU LEU E . n 
E 5 115 LEU 115 114 114 LEU LEU E . n 
E 5 116 VAL 116 115 115 VAL VAL E . n 
E 5 117 LEU 117 116 116 LEU LEU E . n 
E 5 118 GLU 118 117 117 GLU GLU E . n 
E 5 119 ASP 119 118 118 ASP ASP E . n 
E 5 120 LEU 120 119 119 LEU LEU E . n 
E 5 121 LYS 121 120 120 LYS LYS E . n 
E 5 122 ASN 122 121 121 ASN ASN E . n 
E 5 123 VAL 123 122 122 VAL VAL E . n 
E 5 124 PHE 124 123 123 PHE PHE E . n 
E 5 125 PRO 125 124 124 PRO PRO E . n 
E 5 126 PRO 126 125 125 PRO PRO E . n 
E 5 127 GLU 127 126 126 GLU GLU E . n 
E 5 128 VAL 128 127 127 VAL VAL E . n 
E 5 129 ALA 129 128 128 ALA ALA E . n 
E 5 130 VAL 130 129 129 VAL VAL E . n 
E 5 131 PHE 131 130 130 PHE PHE E . n 
E 5 132 GLU 132 131 131 GLU GLU E . n 
E 5 133 PRO 133 132 132 PRO PRO E . n 
E 5 134 SER 134 133 133 SER SER E . n 
E 5 135 GLU 135 134 134 GLU GLU E . n 
E 5 136 ALA 136 135 135 ALA ALA E . n 
E 5 137 GLU 137 136 136 GLU GLU E . n 
E 5 138 ILE 138 137 137 ILE ILE E . n 
E 5 139 SER 139 138 138 SER SER E . n 
E 5 140 HIS 140 139 139 HIS HIS E . n 
E 5 141 THR 141 140 140 THR THR E . n 
E 5 142 GLN 142 141 141 GLN GLN E . n 
E 5 143 LYS 143 142 142 LYS LYS E . n 
E 5 144 ALA 144 143 143 ALA ALA E . n 
E 5 145 THR 145 144 144 THR THR E . n 
E 5 146 LEU 146 145 145 LEU LEU E . n 
E 5 147 VAL 147 146 146 VAL VAL E . n 
E 5 148 CYS 148 147 147 CYS CYS E . n 
E 5 149 LEU 149 148 148 LEU LEU E . n 
E 5 150 ALA 150 149 149 ALA ALA E . n 
E 5 151 THR 151 150 150 THR THR E . n 
E 5 152 GLY 152 151 151 GLY GLY E . n 
E 5 153 PHE 153 152 152 PHE PHE E . n 
E 5 154 TYR 154 153 153 TYR TYR E . n 
E 5 155 PRO 155 154 154 PRO PRO E . n 
E 5 156 ASP 156 155 155 ASP ASP E . n 
E 5 157 HIS 157 156 156 HIS HIS E . n 
E 5 158 VAL 158 157 157 VAL VAL E . n 
E 5 159 GLU 159 158 158 GLU GLU E . n 
E 5 160 LEU 160 159 159 LEU LEU E . n 
E 5 161 SER 161 160 160 SER SER E . n 
E 5 162 TRP 162 161 161 TRP TRP E . n 
E 5 163 TRP 163 162 162 TRP TRP E . n 
E 5 164 VAL 164 163 163 VAL VAL E . n 
E 5 165 ASN 165 164 164 ASN ASN E . n 
E 5 166 GLY 166 165 165 GLY GLY E . n 
E 5 167 LYS 167 166 166 LYS LYS E . n 
E 5 168 GLU 168 167 167 GLU GLU E . n 
E 5 169 VAL 169 168 168 VAL VAL E . n 
E 5 170 HIS 170 169 169 HIS HIS E . n 
E 5 171 SER 171 170 170 SER SER E . n 
E 5 172 GLY 172 171 171 GLY GLY E . n 
E 5 173 VAL 173 172 172 VAL VAL E . n 
E 5 174 CYS 174 173 173 CYS CYS E . n 
E 5 175 THR 175 174 174 THR THR E . n 
E 5 176 ASP 176 175 175 ASP ASP E . n 
E 5 177 PRO 177 176 176 PRO PRO E . n 
E 5 178 GLN 178 177 177 GLN GLN E . n 
E 5 179 PRO 179 178 178 PRO PRO E . n 
E 5 180 LEU 180 179 179 LEU LEU E . n 
E 5 181 LYS 181 180 180 LYS LYS E . n 
E 5 182 GLU 182 181 181 GLU GLU E . n 
E 5 183 GLN 183 182 182 GLN GLN E . n 
E 5 184 PRO 184 183 183 PRO PRO E . n 
E 5 185 ALA 185 184 184 ALA ALA E . n 
E 5 186 LEU 186 185 185 LEU LEU E . n 
E 5 187 ASN 187 186 186 ASN ASN E . n 
E 5 188 ASP 188 187 187 ASP ASP E . n 
E 5 189 SER 189 188 188 SER SER E . n 
E 5 190 ARG 190 189 189 ARG ARG E . n 
E 5 191 TYR 191 190 190 TYR TYR E . n 
E 5 192 ALA 192 191 191 ALA ALA E . n 
E 5 193 LEU 193 192 192 LEU LEU E . n 
E 5 194 SER 194 193 193 SER SER E . n 
E 5 195 SER 195 194 194 SER SER E . n 
E 5 196 ARG 196 195 195 ARG ARG E . n 
E 5 197 LEU 197 196 196 LEU LEU E . n 
E 5 198 ARG 198 197 197 ARG ARG E . n 
E 5 199 VAL 199 198 198 VAL VAL E . n 
E 5 200 SER 200 199 199 SER SER E . n 
E 5 201 ALA 201 200 200 ALA ALA E . n 
E 5 202 THR 202 201 201 THR THR E . n 
E 5 203 PHE 203 202 202 PHE PHE E . n 
E 5 204 TRP 204 203 203 TRP TRP E . n 
E 5 205 GLN 205 204 204 GLN GLN E . n 
E 5 206 ASN 206 205 205 ASN ASN E . n 
E 5 207 PRO 207 206 206 PRO PRO E . n 
E 5 208 ARG 208 207 207 ARG ARG E . n 
E 5 209 ASN 209 208 208 ASN ASN E . n 
E 5 210 HIS 210 209 209 HIS HIS E . n 
E 5 211 PHE 211 210 210 PHE PHE E . n 
E 5 212 ARG 212 211 211 ARG ARG E . n 
E 5 213 CYS 213 212 212 CYS CYS E . n 
E 5 214 GLN 214 213 213 GLN GLN E . n 
E 5 215 VAL 215 214 214 VAL VAL E . n 
E 5 216 GLN 216 215 215 GLN GLN E . n 
E 5 217 PHE 217 216 216 PHE PHE E . n 
E 5 218 TYR 218 217 217 TYR TYR E . n 
E 5 219 GLY 219 218 218 GLY GLY E . n 
E 5 220 LEU 220 219 219 LEU LEU E . n 
E 5 221 SER 221 220 220 SER SER E . n 
E 5 222 GLU 222 221 221 GLU GLU E . n 
E 5 223 ASN 223 222 222 ASN ASN E . n 
E 5 224 ASP 224 223 223 ASP ASP E . n 
E 5 225 GLU 225 224 224 GLU GLU E . n 
E 5 226 TRP 226 225 225 TRP TRP E . n 
E 5 227 THR 227 226 226 THR THR E . n 
E 5 228 GLN 228 227 227 GLN GLN E . n 
E 5 229 ASP 229 228 228 ASP ASP E . n 
E 5 230 ARG 230 229 229 ARG ARG E . n 
E 5 231 ALA 231 230 230 ALA ALA E . n 
E 5 232 LYS 232 231 231 LYS LYS E . n 
E 5 233 PRO 233 232 232 PRO PRO E . n 
E 5 234 VAL 234 233 233 VAL VAL E . n 
E 5 235 THR 235 234 234 THR THR E . n 
E 5 236 GLN 236 235 235 GLN GLN E . n 
E 5 237 ILE 237 236 236 ILE ILE E . n 
E 5 238 VAL 238 237 237 VAL VAL E . n 
E 5 239 SER 239 238 238 SER SER E . n 
E 5 240 ALA 240 239 239 ALA ALA E . n 
E 5 241 GLU 241 240 240 GLU GLU E . n 
E 5 242 ALA 242 241 241 ALA ALA E . n 
E 5 243 TRP 243 242 242 TRP TRP E . n 
E 5 244 GLY 244 243 243 GLY GLY E . n 
E 5 245 ARG 245 244 244 ARG ARG E . n 
E 5 246 ALA 246 245 245 ALA ALA E . n 
E 5 247 ASP 247 246 246 ASP ASP E . 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 GOL 1   301 301 GOL GOL A . 
G 6 GOL 1   302 401 GOL GOL A . 
H 6 GOL 1   303 501 GOL GOL A . 
I 7 EDO 1   304 101 EDO EDO A . 
J 6 GOL 1   301 204 GOL GOL D . 
K 7 EDO 1   301 301 EDO EDO E . 
L 6 GOL 1   302 401 GOL GOL E . 
M 6 GOL 1   303 501 GOL GOL E . 
N 6 GOL 1   304 601 GOL GOL E . 
O 6 GOL 1   305 801 GOL GOL E . 
P 8 HOH 1   401 424 HOH HOH A . 
P 8 HOH 2   402 364 HOH HOH A . 
P 8 HOH 3   403 233 HOH HOH A . 
P 8 HOH 4   404 388 HOH HOH A . 
P 8 HOH 5   405 46  HOH HOH A . 
P 8 HOH 6   406 160 HOH HOH A . 
P 8 HOH 7   407 93  HOH HOH A . 
P 8 HOH 8   408 64  HOH HOH A . 
P 8 HOH 9   409 40  HOH HOH A . 
P 8 HOH 10  410 39  HOH HOH A . 
P 8 HOH 11  411 385 HOH HOH A . 
P 8 HOH 12  412 60  HOH HOH A . 
P 8 HOH 13  413 122 HOH HOH A . 
P 8 HOH 14  414 111 HOH HOH A . 
P 8 HOH 15  415 141 HOH HOH A . 
P 8 HOH 16  416 10  HOH HOH A . 
P 8 HOH 17  417 77  HOH HOH A . 
P 8 HOH 18  418 351 HOH HOH A . 
P 8 HOH 19  419 333 HOH HOH A . 
P 8 HOH 20  420 150 HOH HOH A . 
P 8 HOH 21  421 330 HOH HOH A . 
P 8 HOH 22  422 235 HOH HOH A . 
P 8 HOH 23  423 396 HOH HOH A . 
P 8 HOH 24  424 36  HOH HOH A . 
P 8 HOH 25  425 28  HOH HOH A . 
P 8 HOH 26  426 61  HOH HOH A . 
P 8 HOH 27  427 210 HOH HOH A . 
P 8 HOH 28  428 136 HOH HOH A . 
P 8 HOH 29  429 161 HOH HOH A . 
P 8 HOH 30  430 13  HOH HOH A . 
P 8 HOH 31  431 438 HOH HOH A . 
P 8 HOH 32  432 69  HOH HOH A . 
P 8 HOH 33  433 458 HOH HOH A . 
P 8 HOH 34  434 386 HOH HOH A . 
P 8 HOH 35  435 177 HOH HOH A . 
P 8 HOH 36  436 135 HOH HOH A . 
P 8 HOH 37  437 45  HOH HOH A . 
P 8 HOH 38  438 370 HOH HOH A . 
P 8 HOH 39  439 24  HOH HOH A . 
P 8 HOH 40  440 37  HOH HOH A . 
P 8 HOH 41  441 168 HOH HOH A . 
P 8 HOH 42  442 48  HOH HOH A . 
P 8 HOH 43  443 73  HOH HOH A . 
P 8 HOH 44  444 56  HOH HOH A . 
P 8 HOH 45  445 58  HOH HOH A . 
P 8 HOH 46  446 474 HOH HOH A . 
P 8 HOH 47  447 146 HOH HOH A . 
P 8 HOH 48  448 153 HOH HOH A . 
P 8 HOH 49  449 391 HOH HOH A . 
P 8 HOH 50  450 273 HOH HOH A . 
P 8 HOH 51  451 335 HOH HOH A . 
P 8 HOH 52  452 190 HOH HOH A . 
P 8 HOH 53  453 66  HOH HOH A . 
P 8 HOH 54  454 198 HOH HOH A . 
P 8 HOH 55  455 209 HOH HOH A . 
P 8 HOH 56  456 206 HOH HOH A . 
P 8 HOH 57  457 224 HOH HOH A . 
P 8 HOH 58  458 518 HOH HOH A . 
P 8 HOH 59  459 41  HOH HOH A . 
P 8 HOH 60  460 171 HOH HOH A . 
P 8 HOH 61  461 106 HOH HOH A . 
P 8 HOH 62  462 158 HOH HOH A . 
P 8 HOH 63  463 460 HOH HOH A . 
P 8 HOH 64  464 528 HOH HOH A . 
P 8 HOH 65  465 456 HOH HOH A . 
P 8 HOH 66  466 50  HOH HOH A . 
P 8 HOH 67  467 368 HOH HOH A . 
P 8 HOH 68  468 350 HOH HOH A . 
P 8 HOH 69  469 547 HOH HOH A . 
P 8 HOH 70  470 410 HOH HOH A . 
P 8 HOH 71  471 373 HOH HOH A . 
P 8 HOH 72  472 403 HOH HOH A . 
P 8 HOH 73  473 317 HOH HOH A . 
P 8 HOH 74  474 96  HOH HOH A . 
P 8 HOH 75  475 174 HOH HOH A . 
P 8 HOH 76  476 332 HOH HOH A . 
P 8 HOH 77  477 408 HOH HOH A . 
P 8 HOH 78  478 117 HOH HOH A . 
P 8 HOH 79  479 430 HOH HOH A . 
P 8 HOH 80  480 365 HOH HOH A . 
P 8 HOH 81  481 288 HOH HOH A . 
P 8 HOH 82  482 363 HOH HOH A . 
P 8 HOH 83  483 466 HOH HOH A . 
P 8 HOH 84  484 381 HOH HOH A . 
P 8 HOH 85  485 382 HOH HOH A . 
P 8 HOH 86  486 417 HOH HOH A . 
P 8 HOH 87  487 525 HOH HOH A . 
P 8 HOH 88  488 265 HOH HOH A . 
P 8 HOH 89  489 437 HOH HOH A . 
P 8 HOH 90  490 175 HOH HOH A . 
P 8 HOH 91  491 320 HOH HOH A . 
P 8 HOH 92  492 278 HOH HOH A . 
P 8 HOH 93  493 241 HOH HOH A . 
P 8 HOH 94  494 119 HOH HOH A . 
P 8 HOH 95  495 218 HOH HOH A . 
P 8 HOH 96  496 172 HOH HOH A . 
P 8 HOH 97  497 334 HOH HOH A . 
P 8 HOH 98  498 500 HOH HOH A . 
P 8 HOH 99  499 537 HOH HOH A . 
P 8 HOH 100 500 207 HOH HOH A . 
P 8 HOH 101 501 427 HOH HOH A . 
P 8 HOH 102 502 219 HOH HOH A . 
P 8 HOH 103 503 82  HOH HOH A . 
P 8 HOH 104 504 201 HOH HOH A . 
P 8 HOH 105 505 407 HOH HOH A . 
P 8 HOH 106 506 520 HOH HOH A . 
P 8 HOH 107 507 521 HOH HOH A . 
P 8 HOH 108 508 314 HOH HOH A . 
P 8 HOH 109 509 272 HOH HOH A . 
P 8 HOH 110 510 343 HOH HOH A . 
P 8 HOH 111 511 308 HOH HOH A . 
P 8 HOH 112 512 289 HOH HOH A . 
P 8 HOH 113 513 360 HOH HOH A . 
P 8 HOH 114 514 418 HOH HOH A . 
P 8 HOH 115 515 358 HOH HOH A . 
P 8 HOH 116 516 527 HOH HOH A . 
P 8 HOH 117 517 324 HOH HOH A . 
P 8 HOH 118 518 504 HOH HOH A . 
P 8 HOH 119 519 355 HOH HOH A . 
P 8 HOH 120 520 338 HOH HOH A . 
P 8 HOH 121 521 512 HOH HOH A . 
P 8 HOH 122 522 342 HOH HOH A . 
P 8 HOH 123 523 467 HOH HOH A . 
P 8 HOH 124 524 455 HOH HOH A . 
P 8 HOH 125 525 451 HOH HOH A . 
P 8 HOH 126 526 501 HOH HOH A . 
P 8 HOH 127 527 302 HOH HOH A . 
P 8 HOH 128 528 531 HOH HOH A . 
P 8 HOH 129 529 471 HOH HOH A . 
P 8 HOH 130 530 470 HOH HOH A . 
P 8 HOH 131 531 535 HOH HOH A . 
P 8 HOH 132 532 253 HOH HOH A . 
P 8 HOH 133 533 526 HOH HOH A . 
P 8 HOH 134 534 286 HOH HOH A . 
P 8 HOH 135 535 280 HOH HOH A . 
P 8 HOH 136 536 260 HOH HOH A . 
P 8 HOH 137 537 443 HOH HOH A . 
P 8 HOH 138 538 457 HOH HOH A . 
P 8 HOH 139 539 354 HOH HOH A . 
Q 8 HOH 1   101 33  HOH HOH C . 
Q 8 HOH 2   102 8   HOH HOH C . 
Q 8 HOH 3   103 271 HOH HOH C . 
Q 8 HOH 4   104 20  HOH HOH C . 
Q 8 HOH 5   105 4   HOH HOH C . 
Q 8 HOH 6   106 31  HOH HOH C . 
Q 8 HOH 7   107 116 HOH HOH C . 
Q 8 HOH 8   108 52  HOH HOH C . 
Q 8 HOH 9   109 55  HOH HOH C . 
Q 8 HOH 10  110 211 HOH HOH C . 
R 8 HOH 1   101 204 HOH HOH B . 
R 8 HOH 2   102 349 HOH HOH B . 
R 8 HOH 3   103 445 HOH HOH B . 
R 8 HOH 4   104 68  HOH HOH B . 
R 8 HOH 5   105 67  HOH HOH B . 
R 8 HOH 6   106 304 HOH HOH B . 
R 8 HOH 7   107 284 HOH HOH B . 
R 8 HOH 8   108 208 HOH HOH B . 
R 8 HOH 9   109 326 HOH HOH B . 
R 8 HOH 10  110 264 HOH HOH B . 
R 8 HOH 11  111 62  HOH HOH B . 
R 8 HOH 12  112 312 HOH HOH B . 
R 8 HOH 13  113 139 HOH HOH B . 
R 8 HOH 14  114 230 HOH HOH B . 
R 8 HOH 15  115 187 HOH HOH B . 
R 8 HOH 16  116 79  HOH HOH B . 
R 8 HOH 17  117 478 HOH HOH B . 
R 8 HOH 18  118 53  HOH HOH B . 
R 8 HOH 19  119 442 HOH HOH B . 
R 8 HOH 20  120 250 HOH HOH B . 
R 8 HOH 21  121 371 HOH HOH B . 
R 8 HOH 22  122 480 HOH HOH B . 
R 8 HOH 23  123 49  HOH HOH B . 
R 8 HOH 24  124 259 HOH HOH B . 
R 8 HOH 25  125 59  HOH HOH B . 
R 8 HOH 26  126 181 HOH HOH B . 
R 8 HOH 27  127 63  HOH HOH B . 
R 8 HOH 28  128 446 HOH HOH B . 
R 8 HOH 29  129 379 HOH HOH B . 
R 8 HOH 30  130 415 HOH HOH B . 
R 8 HOH 31  131 468 HOH HOH B . 
R 8 HOH 32  132 497 HOH HOH B . 
R 8 HOH 33  133 532 HOH HOH B . 
R 8 HOH 34  134 453 HOH HOH B . 
R 8 HOH 35  135 469 HOH HOH B . 
R 8 HOH 36  136 294 HOH HOH B . 
R 8 HOH 37  137 319 HOH HOH B . 
R 8 HOH 38  138 236 HOH HOH B . 
R 8 HOH 39  139 539 HOH HOH B . 
R 8 HOH 40  140 481 HOH HOH B . 
R 8 HOH 41  141 231 HOH HOH B . 
R 8 HOH 42  142 398 HOH HOH B . 
R 8 HOH 43  143 517 HOH HOH B . 
R 8 HOH 44  144 529 HOH HOH B . 
R 8 HOH 45  145 432 HOH HOH B . 
S 8 HOH 1   401 248 HOH HOH D . 
S 8 HOH 2   402 463 HOH HOH D . 
S 8 HOH 3   403 487 HOH HOH D . 
S 8 HOH 4   404 494 HOH HOH D . 
S 8 HOH 5   405 510 HOH HOH D . 
S 8 HOH 6   406 328 HOH HOH D . 
S 8 HOH 7   407 23  HOH HOH D . 
S 8 HOH 8   408 402 HOH HOH D . 
S 8 HOH 9   409 125 HOH HOH D . 
S 8 HOH 10  410 97  HOH HOH D . 
S 8 HOH 11  411 12  HOH HOH D . 
S 8 HOH 12  412 176 HOH HOH D . 
S 8 HOH 13  413 75  HOH HOH D . 
S 8 HOH 14  414 186 HOH HOH D . 
S 8 HOH 15  415 390 HOH HOH D . 
S 8 HOH 16  416 245 HOH HOH D . 
S 8 HOH 17  417 98  HOH HOH D . 
S 8 HOH 18  418 143 HOH HOH D . 
S 8 HOH 19  419 16  HOH HOH D . 
S 8 HOH 20  420 178 HOH HOH D . 
S 8 HOH 21  421 123 HOH HOH D . 
S 8 HOH 22  422 179 HOH HOH D . 
S 8 HOH 23  423 120 HOH HOH D . 
S 8 HOH 24  424 311 HOH HOH D . 
S 8 HOH 25  425 94  HOH HOH D . 
S 8 HOH 26  426 118 HOH HOH D . 
S 8 HOH 27  427 428 HOH HOH D . 
S 8 HOH 28  428 229 HOH HOH D . 
S 8 HOH 29  429 191 HOH HOH D . 
S 8 HOH 30  430 155 HOH HOH D . 
S 8 HOH 31  431 182 HOH HOH D . 
S 8 HOH 32  432 321 HOH HOH D . 
S 8 HOH 33  433 27  HOH HOH D . 
S 8 HOH 34  434 227 HOH HOH D . 
S 8 HOH 35  435 543 HOH HOH D . 
S 8 HOH 36  436 112 HOH HOH D . 
S 8 HOH 37  437 251 HOH HOH D . 
S 8 HOH 38  438 184 HOH HOH D . 
S 8 HOH 39  439 76  HOH HOH D . 
S 8 HOH 40  440 393 HOH HOH D . 
S 8 HOH 41  441 287 HOH HOH D . 
S 8 HOH 42  442 367 HOH HOH D . 
S 8 HOH 43  443 276 HOH HOH D . 
S 8 HOH 44  444 283 HOH HOH D . 
S 8 HOH 45  445 121 HOH HOH D . 
S 8 HOH 46  446 274 HOH HOH D . 
S 8 HOH 47  447 19  HOH HOH D . 
S 8 HOH 48  448 300 HOH HOH D . 
S 8 HOH 49  449 183 HOH HOH D . 
S 8 HOH 50  450 81  HOH HOH D . 
S 8 HOH 51  451 242 HOH HOH D . 
S 8 HOH 52  452 214 HOH HOH D . 
S 8 HOH 53  453 101 HOH HOH D . 
S 8 HOH 54  454 25  HOH HOH D . 
S 8 HOH 55  455 530 HOH HOH D . 
S 8 HOH 56  456 222 HOH HOH D . 
S 8 HOH 57  457 202 HOH HOH D . 
S 8 HOH 58  458 447 HOH HOH D . 
S 8 HOH 59  459 220 HOH HOH D . 
S 8 HOH 60  460 246 HOH HOH D . 
S 8 HOH 61  461 498 HOH HOH D . 
S 8 HOH 62  462 129 HOH HOH D . 
S 8 HOH 63  463 162 HOH HOH D . 
S 8 HOH 64  464 257 HOH HOH D . 
S 8 HOH 65  465 477 HOH HOH D . 
S 8 HOH 66  466 134 HOH HOH D . 
S 8 HOH 67  467 199 HOH HOH D . 
S 8 HOH 68  468 102 HOH HOH D . 
S 8 HOH 69  469 124 HOH HOH D . 
S 8 HOH 70  470 399 HOH HOH D . 
S 8 HOH 71  471 126 HOH HOH D . 
S 8 HOH 72  472 366 HOH HOH D . 
S 8 HOH 73  473 127 HOH HOH D . 
S 8 HOH 74  474 189 HOH HOH D . 
S 8 HOH 75  475 17  HOH HOH D . 
S 8 HOH 76  476 269 HOH HOH D . 
S 8 HOH 77  477 483 HOH HOH D . 
S 8 HOH 78  478 515 HOH HOH D . 
S 8 HOH 79  479 380 HOH HOH D . 
S 8 HOH 80  480 503 HOH HOH D . 
S 8 HOH 81  481 293 HOH HOH D . 
S 8 HOH 82  482 387 HOH HOH D . 
S 8 HOH 83  483 256 HOH HOH D . 
S 8 HOH 84  484 323 HOH HOH D . 
S 8 HOH 85  485 78  HOH HOH D . 
S 8 HOH 86  486 514 HOH HOH D . 
S 8 HOH 87  487 261 HOH HOH D . 
S 8 HOH 88  488 540 HOH HOH D . 
S 8 HOH 89  489 100 HOH HOH D . 
S 8 HOH 90  490 180 HOH HOH D . 
S 8 HOH 91  491 493 HOH HOH D . 
S 8 HOH 92  492 472 HOH HOH D . 
S 8 HOH 93  493 228 HOH HOH D . 
S 8 HOH 94  494 508 HOH HOH D . 
S 8 HOH 95  495 419 HOH HOH D . 
S 8 HOH 96  496 263 HOH HOH D . 
S 8 HOH 97  497 270 HOH HOH D . 
S 8 HOH 98  498 357 HOH HOH D . 
S 8 HOH 99  499 243 HOH HOH D . 
S 8 HOH 100 500 331 HOH HOH D . 
S 8 HOH 101 501 267 HOH HOH D . 
S 8 HOH 102 502 462 HOH HOH D . 
S 8 HOH 103 503 405 HOH HOH D . 
S 8 HOH 104 504 196 HOH HOH D . 
S 8 HOH 105 505 188 HOH HOH D . 
S 8 HOH 106 506 297 HOH HOH D . 
S 8 HOH 107 507 310 HOH HOH D . 
S 8 HOH 108 508 341 HOH HOH D . 
S 8 HOH 109 509 546 HOH HOH D . 
S 8 HOH 110 510 400 HOH HOH D . 
S 8 HOH 111 511 392 HOH HOH D . 
S 8 HOH 112 512 339 HOH HOH D . 
S 8 HOH 113 513 340 HOH HOH D . 
S 8 HOH 114 514 482 HOH HOH D . 
S 8 HOH 115 515 541 HOH HOH D . 
S 8 HOH 116 516 291 HOH HOH D . 
S 8 HOH 117 517 375 HOH HOH D . 
S 8 HOH 118 518 542 HOH HOH D . 
S 8 HOH 119 519 409 HOH HOH D . 
S 8 HOH 120 520 336 HOH HOH D . 
S 8 HOH 121 521 479 HOH HOH D . 
S 8 HOH 122 522 156 HOH HOH D . 
S 8 HOH 123 523 524 HOH HOH D . 
S 8 HOH 124 524 444 HOH HOH D . 
S 8 HOH 125 525 459 HOH HOH D . 
S 8 HOH 126 526 406 HOH HOH D . 
S 8 HOH 127 527 492 HOH HOH D . 
S 8 HOH 128 528 522 HOH HOH D . 
S 8 HOH 129 529 389 HOH HOH D . 
T 8 HOH 1   401 507 HOH HOH E . 
T 8 HOH 2   402 348 HOH HOH E . 
T 8 HOH 3   403 489 HOH HOH E . 
T 8 HOH 4   404 6   HOH HOH E . 
T 8 HOH 5   405 290 HOH HOH E . 
T 8 HOH 6   406 440 HOH HOH E . 
T 8 HOH 7   407 18  HOH HOH E . 
T 8 HOH 8   408 523 HOH HOH E . 
T 8 HOH 9   409 21  HOH HOH E . 
T 8 HOH 10  410 509 HOH HOH E . 
T 8 HOH 11  411 441 HOH HOH E . 
T 8 HOH 12  412 325 HOH HOH E . 
T 8 HOH 13  413 421 HOH HOH E . 
T 8 HOH 14  414 30  HOH HOH E . 
T 8 HOH 15  415 327 HOH HOH E . 
T 8 HOH 16  416 516 HOH HOH E . 
T 8 HOH 17  417 491 HOH HOH E . 
T 8 HOH 18  418 88  HOH HOH E . 
T 8 HOH 19  419 29  HOH HOH E . 
T 8 HOH 20  420 315 HOH HOH E . 
T 8 HOH 21  421 404 HOH HOH E . 
T 8 HOH 22  422 249 HOH HOH E . 
T 8 HOH 23  423 148 HOH HOH E . 
T 8 HOH 24  424 110 HOH HOH E . 
T 8 HOH 25  425 329 HOH HOH E . 
T 8 HOH 26  426 157 HOH HOH E . 
T 8 HOH 27  427 173 HOH HOH E . 
T 8 HOH 28  428 164 HOH HOH E . 
T 8 HOH 29  429 7   HOH HOH E . 
T 8 HOH 30  430 226 HOH HOH E . 
T 8 HOH 31  431 42  HOH HOH E . 
T 8 HOH 32  432 131 HOH HOH E . 
T 8 HOH 33  433 165 HOH HOH E . 
T 8 HOH 34  434 352 HOH HOH E . 
T 8 HOH 35  435 145 HOH HOH E . 
T 8 HOH 36  436 9   HOH HOH E . 
T 8 HOH 37  437 262 HOH HOH E . 
T 8 HOH 38  438 132 HOH HOH E . 
T 8 HOH 39  439 282 HOH HOH E . 
T 8 HOH 40  440 65  HOH HOH E . 
T 8 HOH 41  441 369 HOH HOH E . 
T 8 HOH 42  442 44  HOH HOH E . 
T 8 HOH 43  443 2   HOH HOH E . 
T 8 HOH 44  444 114 HOH HOH E . 
T 8 HOH 45  445 372 HOH HOH E . 
T 8 HOH 46  446 275 HOH HOH E . 
T 8 HOH 47  447 99  HOH HOH E . 
T 8 HOH 48  448 90  HOH HOH E . 
T 8 HOH 49  449 87  HOH HOH E . 
T 8 HOH 50  450 11  HOH HOH E . 
T 8 HOH 51  451 84  HOH HOH E . 
T 8 HOH 52  452 205 HOH HOH E . 
T 8 HOH 53  453 22  HOH HOH E . 
T 8 HOH 54  454 154 HOH HOH E . 
T 8 HOH 55  455 465 HOH HOH E . 
T 8 HOH 56  456 142 HOH HOH E . 
T 8 HOH 57  457 86  HOH HOH E . 
T 8 HOH 58  458 14  HOH HOH E . 
T 8 HOH 59  459 47  HOH HOH E . 
T 8 HOH 60  460 193 HOH HOH E . 
T 8 HOH 61  461 239 HOH HOH E . 
T 8 HOH 62  462 473 HOH HOH E . 
T 8 HOH 63  463 138 HOH HOH E . 
T 8 HOH 64  464 108 HOH HOH E . 
T 8 HOH 65  465 281 HOH HOH E . 
T 8 HOH 66  466 255 HOH HOH E . 
T 8 HOH 67  467 103 HOH HOH E . 
T 8 HOH 68  468 216 HOH HOH E . 
T 8 HOH 69  469 185 HOH HOH E . 
T 8 HOH 70  470 35  HOH HOH E . 
T 8 HOH 71  471 137 HOH HOH E . 
T 8 HOH 72  472 296 HOH HOH E . 
T 8 HOH 73  473 5   HOH HOH E . 
T 8 HOH 74  474 92  HOH HOH E . 
T 8 HOH 75  475 254 HOH HOH E . 
T 8 HOH 76  476 83  HOH HOH E . 
T 8 HOH 77  477 266 HOH HOH E . 
T 8 HOH 78  478 51  HOH HOH E . 
T 8 HOH 79  479 91  HOH HOH E . 
T 8 HOH 80  480 197 HOH HOH E . 
T 8 HOH 81  481 506 HOH HOH E . 
T 8 HOH 82  482 3   HOH HOH E . 
T 8 HOH 83  483 221 HOH HOH E . 
T 8 HOH 84  484 347 HOH HOH E . 
T 8 HOH 85  485 152 HOH HOH E . 
T 8 HOH 86  486 89  HOH HOH E . 
T 8 HOH 87  487 544 HOH HOH E . 
T 8 HOH 88  488 163 HOH HOH E . 
T 8 HOH 89  489 238 HOH HOH E . 
T 8 HOH 90  490 72  HOH HOH E . 
T 8 HOH 91  491 70  HOH HOH E . 
T 8 HOH 92  492 488 HOH HOH E . 
T 8 HOH 93  493 105 HOH HOH E . 
T 8 HOH 94  494 133 HOH HOH E . 
T 8 HOH 95  495 412 HOH HOH E . 
T 8 HOH 96  496 422 HOH HOH E . 
T 8 HOH 97  497 309 HOH HOH E . 
T 8 HOH 98  498 113 HOH HOH E . 
T 8 HOH 99  499 361 HOH HOH E . 
T 8 HOH 100 500 475 HOH HOH E . 
T 8 HOH 101 501 345 HOH HOH E . 
T 8 HOH 102 502 95  HOH HOH E . 
T 8 HOH 103 503 429 HOH HOH E . 
T 8 HOH 104 504 298 HOH HOH E . 
T 8 HOH 105 505 115 HOH HOH E . 
T 8 HOH 106 506 32  HOH HOH E . 
T 8 HOH 107 507 1   HOH HOH E . 
T 8 HOH 108 508 411 HOH HOH E . 
T 8 HOH 109 509 285 HOH HOH E . 
T 8 HOH 110 510 192 HOH HOH E . 
T 8 HOH 111 511 74  HOH HOH E . 
T 8 HOH 112 512 353 HOH HOH E . 
T 8 HOH 113 513 34  HOH HOH E . 
T 8 HOH 114 514 149 HOH HOH E . 
T 8 HOH 115 515 54  HOH HOH E . 
T 8 HOH 116 516 307 HOH HOH E . 
T 8 HOH 117 517 109 HOH HOH E . 
T 8 HOH 118 518 439 HOH HOH E . 
T 8 HOH 119 519 144 HOH HOH E . 
T 8 HOH 120 520 169 HOH HOH E . 
T 8 HOH 121 521 303 HOH HOH E . 
T 8 HOH 122 522 346 HOH HOH E . 
T 8 HOH 123 523 166 HOH HOH E . 
T 8 HOH 124 524 107 HOH HOH E . 
T 8 HOH 125 525 213 HOH HOH E . 
T 8 HOH 126 526 128 HOH HOH E . 
T 8 HOH 127 527 433 HOH HOH E . 
T 8 HOH 128 528 395 HOH HOH E . 
T 8 HOH 129 529 344 HOH HOH E . 
T 8 HOH 130 530 234 HOH HOH E . 
T 8 HOH 131 531 376 HOH HOH E . 
T 8 HOH 132 532 426 HOH HOH E . 
T 8 HOH 133 533 57  HOH HOH E . 
T 8 HOH 134 534 43  HOH HOH E . 
T 8 HOH 135 535 85  HOH HOH E . 
T 8 HOH 136 536 26  HOH HOH E . 
T 8 HOH 137 537 337 HOH HOH E . 
T 8 HOH 138 538 130 HOH HOH E . 
T 8 HOH 139 539 448 HOH HOH E . 
T 8 HOH 140 540 450 HOH HOH E . 
T 8 HOH 141 541 538 HOH HOH E . 
T 8 HOH 142 542 140 HOH HOH E . 
T 8 HOH 143 543 268 HOH HOH E . 
T 8 HOH 144 544 258 HOH HOH E . 
T 8 HOH 145 545 195 HOH HOH E . 
T 8 HOH 146 546 434 HOH HOH E . 
T 8 HOH 147 547 225 HOH HOH E . 
T 8 HOH 148 548 533 HOH HOH E . 
T 8 HOH 149 549 194 HOH HOH E . 
T 8 HOH 150 550 449 HOH HOH E . 
T 8 HOH 151 551 203 HOH HOH E . 
T 8 HOH 152 552 496 HOH HOH E . 
T 8 HOH 153 553 170 HOH HOH E . 
T 8 HOH 154 554 401 HOH HOH E . 
T 8 HOH 155 555 397 HOH HOH E . 
T 8 HOH 156 556 159 HOH HOH E . 
T 8 HOH 157 557 104 HOH HOH E . 
T 8 HOH 158 558 232 HOH HOH E . 
T 8 HOH 159 559 80  HOH HOH E . 
T 8 HOH 160 560 244 HOH HOH E . 
T 8 HOH 161 561 545 HOH HOH E . 
T 8 HOH 162 562 359 HOH HOH E . 
T 8 HOH 163 563 423 HOH HOH E . 
T 8 HOH 164 564 476 HOH HOH E . 
T 8 HOH 165 565 416 HOH HOH E . 
T 8 HOH 166 566 502 HOH HOH E . 
T 8 HOH 167 567 299 HOH HOH E . 
T 8 HOH 168 568 38  HOH HOH E . 
T 8 HOH 169 569 490 HOH HOH E . 
T 8 HOH 170 570 383 HOH HOH E . 
T 8 HOH 171 571 313 HOH HOH E . 
T 8 HOH 172 572 362 HOH HOH E . 
T 8 HOH 173 573 212 HOH HOH E . 
T 8 HOH 174 574 485 HOH HOH E . 
T 8 HOH 175 575 167 HOH HOH E . 
T 8 HOH 176 576 240 HOH HOH E . 
T 8 HOH 177 577 420 HOH HOH E . 
T 8 HOH 178 578 277 HOH HOH E . 
T 8 HOH 179 579 425 HOH HOH E . 
T 8 HOH 180 580 431 HOH HOH E . 
T 8 HOH 181 581 454 HOH HOH E . 
T 8 HOH 182 582 223 HOH HOH E . 
T 8 HOH 183 583 435 HOH HOH E . 
T 8 HOH 184 584 292 HOH HOH E . 
T 8 HOH 185 585 534 HOH HOH E . 
T 8 HOH 186 586 436 HOH HOH E . 
T 8 HOH 187 587 511 HOH HOH E . 
T 8 HOH 188 588 374 HOH HOH E . 
T 8 HOH 189 589 71  HOH HOH E . 
T 8 HOH 190 590 316 HOH HOH E . 
T 8 HOH 191 591 413 HOH HOH E . 
T 8 HOH 192 592 464 HOH HOH E . 
T 8 HOH 193 593 200 HOH HOH E . 
T 8 HOH 194 594 147 HOH HOH E . 
T 8 HOH 195 595 505 HOH HOH E . 
T 8 HOH 196 596 217 HOH HOH E . 
T 8 HOH 197 597 461 HOH HOH E . 
T 8 HOH 198 598 15  HOH HOH E . 
T 8 HOH 199 599 301 HOH HOH E . 
T 8 HOH 200 600 252 HOH HOH E . 
T 8 HOH 201 601 378 HOH HOH E . 
T 8 HOH 202 602 384 HOH HOH E . 
T 8 HOH 203 603 295 HOH HOH E . 
T 8 HOH 204 604 452 HOH HOH E . 
T 8 HOH 205 605 513 HOH HOH E . 
T 8 HOH 206 606 279 HOH HOH E . 
T 8 HOH 207 607 536 HOH HOH E . 
T 8 HOH 208 608 306 HOH HOH E . 
T 8 HOH 209 609 394 HOH HOH E . 
T 8 HOH 210 610 151 HOH HOH E . 
T 8 HOH 211 611 247 HOH HOH E . 
T 8 HOH 212 612 237 HOH HOH E . 
T 8 HOH 213 613 322 HOH HOH E . 
T 8 HOH 214 614 484 HOH HOH E . 
T 8 HOH 215 615 414 HOH HOH E . 
T 8 HOH 216 616 305 HOH HOH E . 
T 8 HOH 217 617 377 HOH HOH E . 
T 8 HOH 218 618 499 HOH HOH E . 
T 8 HOH 219 619 356 HOH HOH E . 
T 8 HOH 220 620 215 HOH HOH E . 
T 8 HOH 221 621 519 HOH HOH E . 
T 8 HOH 222 622 318 HOH HOH E . 
T 8 HOH 223 623 486 HOH HOH E . 
T 8 HOH 224 624 495 HOH HOH E . 
# 
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 GLN 226 ? CG  ? A GLN 227 CG  
2  1 Y 1 A GLN 226 ? CD  ? A GLN 227 CD  
3  1 Y 1 A GLN 226 ? OE1 ? A GLN 227 OE1 
4  1 Y 1 A GLN 226 ? NE2 ? A GLN 227 NE2 
5  1 Y 1 A ASP 227 ? CG  ? A ASP 228 CG  
6  1 Y 1 A ASP 227 ? OD1 ? A ASP 228 OD1 
7  1 Y 1 A ASP 227 ? OD2 ? A ASP 228 OD2 
8  1 Y 1 A GLU 232 ? CD  ? A GLU 233 CD  
9  1 Y 1 A GLU 232 ? OE1 ? A GLU 233 OE1 
10 1 Y 1 A GLU 232 ? OE2 ? A GLU 233 OE2 
11 1 Y 1 B LYS 58  ? CG  ? C LYS 59  CG  
12 1 Y 1 B LYS 58  ? CD  ? C LYS 59  CD  
13 1 Y 1 B LYS 58  ? CE  ? C LYS 59  CE  
14 1 Y 1 B LYS 58  ? NZ  ? C LYS 59  NZ  
15 1 Y 1 B LYS 75  ? CG  ? C LYS 76  CG  
16 1 Y 1 B LYS 75  ? CD  ? C LYS 76  CD  
17 1 Y 1 B LYS 75  ? CE  ? C LYS 76  CE  
18 1 Y 1 B LYS 75  ? NZ  ? C LYS 76  NZ  
19 1 Y 1 B GLU 77  ? CG  ? C GLU 78  CG  
20 1 Y 1 B GLU 77  ? CD  ? C GLU 78  CD  
21 1 Y 1 B GLU 77  ? OE1 ? C GLU 78  OE1 
22 1 Y 1 B GLU 77  ? OE2 ? C GLU 78  OE2 
23 1 Y 1 D LYS 3   ? CG  ? D LYS 4   CG  
24 1 Y 1 D LYS 3   ? CD  ? D LYS 4   CD  
25 1 Y 1 D LYS 3   ? CE  ? D LYS 4   CE  
26 1 Y 1 D LYS 3   ? NZ  ? D LYS 4   NZ  
27 1 Y 1 D SER 130 ? OG  ? D SER 131 OG  
28 1 Y 1 D ASP 131 ? CG  ? D ASP 132 CG  
29 1 Y 1 D ASP 131 ? OD1 ? D ASP 132 OD1 
30 1 Y 1 D ASP 131 ? OD2 ? D ASP 132 OD2 
31 1 Y 1 D LYS 150 ? CG  ? D LYS 151 CG  
32 1 Y 1 D LYS 150 ? CD  ? D LYS 151 CD  
33 1 Y 1 D LYS 150 ? CE  ? D LYS 151 CE  
34 1 Y 1 D LYS 150 ? NZ  ? D LYS 151 NZ  
35 1 Y 1 D ASP 182 ? CG  ? D ASP 183 CG  
36 1 Y 1 D ASP 182 ? OD1 ? D ASP 183 OD1 
37 1 Y 1 D ASP 182 ? OD2 ? D ASP 183 OD2 
# 
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                     8YIV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.144 
_cell.length_a_esd                 ? 
_cell.length_b                     133.223 
_cell.length_b_esd                 ? 
_cell.length_c                     222.468 
_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                         8YIV 
_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                   8YIV 
_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             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.12 
_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, 8% TacsimateTM pH7.0, 20% PEG4K' 
_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                                       8YIV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               42.7 
_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                                     387710 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_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                                    2.10 
_reflns_shell.d_res_low                                     2.18 
_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                                  0.857 
_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                                 8YIV 
_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                            2.101 
_refine.ls_d_res_low                             42.692 
_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                     61738 
_refine.ls_number_reflns_R_free                  3116 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.73 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1925 
_refine.ls_R_factor_R_free                       0.2259 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1907 
_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                          1.36 
_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                 23.74 
_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                            0.23 
_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        6683 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             547 
_refine_hist.number_atoms_total               7286 
_refine_hist.d_res_high                       2.101 
_refine_hist.d_res_low                        42.692 
# 
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' ? 0.011 ? 6919 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.131 ? 9374 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.867 ? 4124 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.061 ? 985  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 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' 2.1012 2.1340 . . 145 2576 99.00  . . . . 0.2204 . . . . . . . . . . . 0.2706 
'X-RAY DIFFRACTION' 2.1340 2.1690 . . 134 2636 99.00  . . . . 0.2316 . . . . . . . . . . . 0.3148 
'X-RAY DIFFRACTION' 2.1690 2.2064 . . 138 2609 100.00 . . . . 0.2283 . . . . . . . . . . . 0.3154 
'X-RAY DIFFRACTION' 2.2064 2.2465 . . 154 2634 100.00 . . . . 0.2293 . . . . . . . . . . . 0.2942 
'X-RAY DIFFRACTION' 2.2465 2.2897 . . 147 2672 100.00 . . . . 0.2322 . . . . . . . . . . . 0.2953 
'X-RAY DIFFRACTION' 2.2897 2.3364 . . 137 2610 100.00 . . . . 0.2248 . . . . . . . . . . . 0.2799 
'X-RAY DIFFRACTION' 2.3364 2.3872 . . 137 2635 100.00 . . . . 0.2214 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 2.3872 2.4428 . . 142 2679 100.00 . . . . 0.2170 . . . . . . . . . . . 0.2705 
'X-RAY DIFFRACTION' 2.4428 2.5039 . . 134 2648 100.00 . . . . 0.2136 . . . . . . . . . . . 0.3114 
'X-RAY DIFFRACTION' 2.5039 2.5715 . . 145 2642 100.00 . . . . 0.2234 . . . . . . . . . . . 0.2929 
'X-RAY DIFFRACTION' 2.5715 2.6472 . . 136 2636 100.00 . . . . 0.2087 . . . . . . . . . . . 0.2673 
'X-RAY DIFFRACTION' 2.6472 2.7326 . . 128 2691 100.00 . . . . 0.2125 . . . . . . . . . . . 0.2241 
'X-RAY DIFFRACTION' 2.7326 2.8303 . . 133 2658 100.00 . . . . 0.2107 . . . . . . . . . . . 0.2698 
'X-RAY DIFFRACTION' 2.8303 2.9436 . . 120 2674 100.00 . . . . 0.2154 . . . . . . . . . . . 0.2760 
'X-RAY DIFFRACTION' 2.9436 3.0775 . . 140 2678 100.00 . . . . 0.2143 . . . . . . . . . . . 0.2553 
'X-RAY DIFFRACTION' 3.0775 3.2397 . . 150 2669 100.00 . . . . 0.2022 . . . . . . . . . . . 0.2355 
'X-RAY DIFFRACTION' 3.2397 3.4426 . . 148 2680 100.00 . . . . 0.1883 . . . . . . . . . . . 0.2149 
'X-RAY DIFFRACTION' 3.4426 3.7083 . . 161 2659 100.00 . . . . 0.1810 . . . . . . . . . . . 0.1964 
'X-RAY DIFFRACTION' 3.7083 4.0812 . . 157 2652 100.00 . . . . 0.1663 . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 4.0812 4.6711 . . 139 2735 100.00 . . . . 0.1429 . . . . . . . . . . . 0.1622 
'X-RAY DIFFRACTION' 4.6711 5.8827 . . 152 2728 100.00 . . . . 0.1535 . . . . . . . . . . . 0.1647 
'X-RAY DIFFRACTION' 5.8827 42.692 . . 139 2821 98.00  . . . . 0.1930 . . . . . . . . . . . 0.2173 
# 
_struct.entry_id                     8YIV 
_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        8YIV 
_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 7 ? 
J N N 6 ? 
K N N 7 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 6 ? 
P N N 8 ? 
Q N N 8 ? 
R N N 8 ? 
S N N 8 ? 
T N N 8 ? 
# 
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 PDB 8YIV         8YIV   ? 2 ? 1  
3 UNP B2MG_HUMAN   P61769 ? 3 
;IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDRDM
;
21 
4 PDB 8YIV         8YIV   ? 4 ? 1  
5 PDB 8YIV         8YIV   ? 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 8YIV A 2 ? 276 ? F6IQR9 25 ? 299 ? 1 275 
2 2 8YIV C 1 ? 10  ? 8YIV   1  ? 10  ? 1 10  
3 3 8YIV B 2 ? 100 ? P61769 21 ? 119 ? 1 99  
4 4 8YIV D 1 ? 207 ? 8YIV   0  ? 206 ? 0 206 
5 5 8YIV E 1 ? 247 ? 8YIV   0  ? 246 ? 0 246 
# 
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 8YIV MET A 1 ? UNP F6IQR9 ? ? 'initiating methionine' 0 1 
3 8YIV MET B 1 ? UNP P61769 ? ? 'expression tag'        0 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   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)' 13960 ? 
1 MORE         -39   ? 
1 'SSA (A^2)'  37590 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T 
# 
_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 GLN D 83  ? SER D 87  ? GLN D 82  SER D 86  5 ? 5  
HELX_P HELX_P9  AA9 ARG D 166 ? ASP D 169 ? ARG D 165 ASP D 168 5 ? 4  
HELX_P HELX_P10 AB1 ALA D 185 ? PHE D 190 ? ALA D 184 PHE D 189 1 ? 6  
HELX_P HELX_P11 AB2 SER E 83  ? THR E 87  ? SER E 82  THR E 86  5 ? 5  
HELX_P HELX_P12 AB3 SER E 134 ? GLN E 142 ? SER E 133 GLN E 141 1 ? 9  
HELX_P HELX_P13 AB4 ALA E 201 ? ASN E 206 ? ALA E 200 ASN E 205 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 ? ? ? ? ? ? ? 2.080 ? ? 
disulf2 disulf ? ? A CYS 204 SG ? ? ? 1_555 A CYS 260 SG ? ? A CYS 203 A CYS 259 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
disulf3 disulf ? ? C CYS 26  SG ? ? ? 1_555 C CYS 81  SG ? ? B CYS 25  B CYS 80  1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf4 disulf ? ? D CYS 24  SG ? ? ? 1_555 D CYS 92  SG ? ? D CYS 23  D CYS 91  1_555 ? ? ? ? ? ? ? 2.149 ? ? 
disulf5 disulf ? ? D CYS 136 SG ? ? ? 1_555 D CYS 186 SG ? ? D CYS 135 D CYS 185 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf6 disulf ? ? D CYS 161 SG ? ? ? 1_555 E CYS 174 SG ? ? D CYS 160 E CYS 173 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf7 disulf ? ? E CYS 24  SG ? ? ? 1_555 E CYS 92  SG ? ? E CYS 23  E CYS 91  1_555 ? ? ? ? ? ? ? 2.010 ? ? 
disulf8 disulf ? ? E CYS 148 SG ? ? ? 1_555 E CYS 213 SG ? ? E CYS 147 E CYS 212 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
# 
_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 C 26  ? CYS C 81  ? CYS B 25  ? 1_555 CYS B 80  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 24  ? CYS D 92  ? CYS D 23  ? 1_555 CYS D 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS D 136 ? CYS D 186 ? CYS D 135 ? 1_555 CYS D 185 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6 CYS D 161 ? CYS E 174 ? CYS D 160 ? 1_555 CYS E 173 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7 CYS E 24  ? CYS E 92  ? CYS E 23  ? 1_555 CYS E 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
8 CYS E 148 ? CYS E 213 ? CYS E 147 ? 1_555 CYS E 212 ? 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 0.63  
2 HIS 32  C . ? HIS 31  B PRO 33  C ? PRO 32  B 1 2.33  
3 ASN 8   E . ? ASN 7   E PRO 9   E ? PRO 8   E 1 4.13  
4 TYR 154 E . ? TYR 153 E PRO 155 E ? PRO 154 E 1 -2.14 
# 
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 ? 2 ? 
AA9 ? 5 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 6 ? 
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 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? 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 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB6 5 6 ? 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 C 7   ? SER C 12  ? LYS B 6   SER B 11  
AA5 2 ASN C 22  ? PHE C 31  ? ASN B 21  PHE B 30  
AA5 3 PHE C 63  ? PHE C 71  ? PHE B 62  PHE B 70  
AA5 4 GLU C 51  ? HIS C 52  ? GLU B 50  HIS B 51  
AA6 1 LYS C 7   ? SER C 12  ? LYS B 6   SER B 11  
AA6 2 ASN C 22  ? PHE C 31  ? ASN B 21  PHE B 30  
AA6 3 PHE C 63  ? PHE C 71  ? PHE B 62  PHE B 70  
AA6 4 SER C 56  ? PHE C 57  ? SER B 55  PHE B 56  
AA7 1 GLU C 45  ? ARG C 46  ? GLU B 44  ARG B 45  
AA7 2 GLU C 37  ? LYS C 42  ? GLU B 36  LYS B 41  
AA7 3 TYR C 79  ? ASN C 84  ? TYR B 78  ASN B 83  
AA7 4 LYS C 92  ? LYS C 95  ? LYS B 91  LYS B 94  
AA8 1 LYS D 4   ? THR D 6   ? LYS D 3   THR D 5   
AA8 2 LEU D 25  ? GLU D 27  ? LEU D 24  GLU D 26  
AA9 1 SER D 11  ? PRO D 15  ? SER D 10  PRO D 14  
AA9 2 THR D 107 ? LYS D 112 ? THR D 106 LYS D 111 
AA9 3 ALA D 88  ? GLY D 95  ? ALA D 87  GLY D 94  
AA9 4 TYR D 34  ? GLN D 40  ? TYR D 33  GLN D 39  
AA9 5 MET D 46  ? GLY D 53  ? MET D 45  GLY D 52  
AB1 1 SER D 11  ? PRO D 15  ? SER D 10  PRO D 14  
AB1 2 THR D 107 ? LYS D 112 ? THR D 106 LYS D 111 
AB1 3 ALA D 88  ? GLY D 95  ? ALA D 87  GLY D 94  
AB1 4 SER D 101 ? PHE D 103 ? SER D 100 PHE D 102 
AB2 1 VAL D 20  ? LEU D 22  ? VAL D 19  LEU D 21  
AB2 2 SER D 74  ? ILE D 79  ? SER D 73  ILE D 78  
AB2 3 TYR D 64  ? LYS D 69  ? TYR D 63  LYS D 68  
AB2 4 LYS D 60  ? SER D 61  ? LYS D 59  SER D 60  
AB3 1 ALA D 121 ? ARG D 126 ? ALA D 120 ARG D 125 
AB3 2 SER D 134 ? THR D 139 ? SER D 133 THR D 138 
AB3 3 PHE D 170 ? SER D 179 ? PHE D 169 SER D 178 
AB3 4 VAL D 155 ? ILE D 157 ? VAL D 154 ILE D 156 
AB4 1 ALA D 121 ? ARG D 126 ? ALA D 120 ARG D 125 
AB4 2 SER D 134 ? THR D 139 ? SER D 133 THR D 138 
AB4 3 PHE D 170 ? SER D 179 ? PHE D 169 SER D 178 
AB4 4 CYS D 161 ? MET D 165 ? CYS D 160 MET D 164 
AB5 1 VAL E 5   ? ASN E 8   ? VAL E 4   ASN E 7   
AB5 2 LEU E 20  ? GLN E 26  ? LEU E 19  GLN E 25  
AB5 3 LEU E 77  ? LEU E 79  ? LEU E 76  LEU E 78  
AB5 4 LYS E 66  ? VAL E 67  ? LYS E 65  VAL E 66  
AB6 1 TYR E 11  ? VAL E 15  ? TYR E 10  VAL E 14  
AB6 2 THR E 112 ? LEU E 117 ? THR E 111 LEU E 116 
AB6 3 SER E 88  ? SER E 95  ? SER E 87  SER E 94  
AB6 4 TYR E 32  ? GLN E 38  ? TYR E 31  GLN E 37  
AB6 5 LEU E 44  ? ASN E 52  ? LEU E 43  ASN E 51  
AB6 6 VAL E 55  ? LYS E 58  ? VAL E 54  LYS E 57  
AB7 1 TYR E 11  ? VAL E 15  ? TYR E 10  VAL E 14  
AB7 2 THR E 112 ? LEU E 117 ? THR E 111 LEU E 116 
AB7 3 SER E 88  ? SER E 95  ? SER E 87  SER E 94  
AB7 4 TYR E 107 ? PHE E 108 ? TYR E 106 PHE E 107 
AB8 1 GLU E 127 ? PHE E 131 ? GLU E 126 PHE E 130 
AB8 2 LYS E 143 ? PHE E 153 ? LYS E 142 PHE E 152 
AB8 3 TYR E 191 ? SER E 200 ? TYR E 190 SER E 199 
AB8 4 VAL E 173 ? THR E 175 ? VAL E 172 THR E 174 
AB9 1 GLU E 127 ? PHE E 131 ? GLU E 126 PHE E 130 
AB9 2 LYS E 143 ? PHE E 153 ? LYS E 142 PHE E 152 
AB9 3 TYR E 191 ? SER E 200 ? TYR E 190 SER E 199 
AB9 4 LEU E 180 ? LYS E 181 ? LEU E 179 LYS E 180 
AC1 1 LYS E 167 ? VAL E 169 ? LYS E 166 VAL E 168 
AC1 2 VAL E 158 ? VAL E 164 ? VAL E 157 VAL E 163 
AC1 3 HIS E 210 ? PHE E 217 ? HIS E 209 PHE E 216 
AC1 4 GLN E 236 ? TRP E 243 ? GLN E 235 TRP E 242 
# 
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 VAL A 26  ? O VAL A 25  N PHE A 9   ? N PHE A 8   
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 ARG A 115 ? N ARG A 114 O LEU A 127 ? O LEU A 126 
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 LYS C 7   ? N LYS B 6   O SER C 29  ? O SER B 28  
AA5 2 3 N CYS C 26  ? N CYS B 25  O TYR C 67  ? O TYR B 66  
AA5 3 4 O TYR C 68  ? O TYR B 67  N GLU C 51  ? N GLU B 50  
AA6 1 2 N LYS C 7   ? N LYS B 6   O SER C 29  ? O SER B 28  
AA6 2 3 N CYS C 26  ? N CYS B 25  O TYR C 67  ? O TYR B 66  
AA6 3 4 O TYR C 64  ? O TYR B 63  N SER C 56  ? N SER B 55  
AA7 1 2 O GLU C 45  ? O GLU B 44  N LYS C 42  ? N LYS B 41  
AA7 2 3 N LEU C 41  ? N LEU B 40  O ALA C 80  ? O ALA B 79  
AA7 3 4 N VAL C 83  ? N VAL B 82  O LYS C 92  ? O LYS B 91  
AA8 1 2 N THR D 6   ? N THR D 5   O LEU D 25  ? O LEU D 24  
AA9 1 2 N VAL D 12  ? N VAL D 11  O THR D 108 ? O THR D 107 
AA9 2 3 O LEU D 109 ? O LEU D 108 N ALA D 88  ? N ALA D 87  
AA9 3 4 O LYS D 89  ? O LYS D 88  N GLN D 40  ? N GLN D 39  
AA9 4 5 N LYS D 39  ? N LYS D 38  O ILE D 47  ? O ILE D 46  
AB1 1 2 N VAL D 12  ? N VAL D 11  O THR D 108 ? O THR D 107 
AB1 2 3 O LEU D 109 ? O LEU D 108 N ALA D 88  ? N ALA D 87  
AB1 3 4 N LEU D 94  ? N LEU D 93  O THR D 102 ? O THR D 101 
AB2 1 2 N LEU D 22  ? N LEU D 21  O LEU D 77  ? O LEU D 76  
AB2 2 3 O THR D 78  ? O THR D 77  N SER D 65  ? N SER D 64  
AB2 3 4 O TYR D 64  ? O TYR D 63  N SER D 61  ? N SER D 60  
AB3 1 2 N TYR D 123 ? N TYR D 122 O LEU D 137 ? O LEU D 136 
AB3 2 3 N CYS D 136 ? N CYS D 135 O ALA D 177 ? O ALA D 176 
AB3 3 4 O TRP D 178 ? O TRP D 177 N TYR D 156 ? N TYR D 155 
AB4 1 2 N TYR D 123 ? N TYR D 122 O LEU D 137 ? O LEU D 136 
AB4 2 3 N CYS D 136 ? N CYS D 135 O ALA D 177 ? O ALA D 176 
AB4 3 4 O PHE D 170 ? O PHE D 169 N MET D 165 ? N MET D 164 
AB5 1 2 N THR E 6   ? N THR E 5   O SER E 25  ? O SER E 24  
AB5 2 3 N LEU E 20  ? N LEU E 19  O LEU E 79  ? O LEU E 78  
AB5 3 4 O ILE E 78  ? O ILE E 77  N LYS E 66  ? N LYS E 65  
AB6 1 2 N THR E 14  ? N THR E 13  O LEU E 117 ? O LEU E 116 
AB6 2 3 O THR E 112 ? O THR E 111 N TYR E 90  ? N TYR E 89  
AB6 3 4 O LEU E 89  ? O LEU E 88  N GLN E 38  ? N GLN E 37  
AB6 4 5 N MET E 33  ? N MET E 32  O SER E 50  ? O SER E 49  
AB6 5 6 N TYR E 49  ? N TYR E 48  O ASP E 57  ? O ASP E 56  
AB7 1 2 N THR E 14  ? N THR E 13  O LEU E 117 ? O LEU E 116 
AB7 2 3 O THR E 112 ? O THR E 111 N TYR E 90  ? N TYR E 89  
AB7 3 4 N SER E 94  ? N SER E 93  O TYR E 107 ? O TYR E 106 
AB8 1 2 N PHE E 131 ? N PHE E 130 O VAL E 147 ? O VAL E 146 
AB8 2 3 N LEU E 146 ? N LEU E 145 O LEU E 197 ? O LEU E 196 
AB8 3 4 O ARG E 196 ? O ARG E 195 N CYS E 174 ? N CYS E 173 
AB9 1 2 N PHE E 131 ? N PHE E 130 O VAL E 147 ? O VAL E 146 
AB9 2 3 N LEU E 146 ? N LEU E 145 O LEU E 197 ? O LEU E 196 
AB9 3 4 O ALA E 192 ? O ALA E 191 N LEU E 180 ? N LEU E 179 
AC1 1 2 O LYS E 167 ? O LYS E 166 N VAL E 164 ? N VAL E 163 
AC1 2 3 N SER E 161 ? N SER E 160 O GLN E 214 ? O GLN E 213 
AC1 3 4 N PHE E 217 ? N PHE E 216 O GLN E 236 ? O GLN E 235 
# 
_pdbx_entry_details.entry_id                   8YIV 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 O   B HOH 114 ? ? O   B HOH 128 ? ? 1.86 
2  1 O   B HOH 139 ? ? O   B HOH 143 ? ? 1.89 
3  1 NZ  D LYS 132 ? ? O   D HOH 401 ? ? 1.96 
4  1 O   D HOH 414 ? ? O   D HOH 509 ? ? 1.98 
5  1 O   E HOH 565 ? ? O   E HOH 581 ? ? 1.99 
6  1 OG  D SER 73  ? ? O   D HOH 402 ? ? 2.02 
7  1 OE2 E GLU 134 ? ? O   E HOH 401 ? ? 2.04 
8  1 O   E HOH 520 ? ? O   E HOH 596 ? ? 2.04 
9  1 OE1 A GLU 264 ? ? O   A HOH 401 ? ? 2.05 
10 1 OE1 B GLU 44  ? ? O   B HOH 101 ? ? 2.06 
11 1 O   A VAL 231 ? ? NZ  A LYS 243 ? ? 2.09 
12 1 O   E HOH 410 ? ? O   E HOH 462 ? ? 2.09 
13 1 O   D LEU 81  ? ? O   D HOH 403 ? ? 2.10 
14 1 OG  A SER 4   ? ? OD1 A ASP 102 ? ? 2.10 
15 1 OG  A SER 195 ? ? N   A GLU 198 ? ? 2.11 
16 1 O   D HOH 405 ? ? O   D HOH 482 ? ? 2.11 
17 1 O   A HOH 538 ? ? O   C HOH 109 ? ? 2.11 
18 1 O   D ASP 153 ? ? O   D HOH 404 ? ? 2.12 
19 1 O   A HOH 523 ? ? O   A HOH 533 ? ? 2.12 
20 1 OD1 D ASP 141 ? ? O   D HOH 405 ? ? 2.14 
21 1 O   D HOH 422 ? ? O   E HOH 521 ? ? 2.15 
22 1 OH  E TYR 190 ? ? O   E HOH 402 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    N 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLY 
_pdbx_validate_symm_contact.auth_seq_id_1     1 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OXT 
_pdbx_validate_symm_contact.auth_asym_id_2    E 
_pdbx_validate_symm_contact.auth_comp_id_2    ASP 
_pdbx_validate_symm_contact.auth_seq_id_2     246 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   7_554 
_pdbx_validate_symm_contact.dist              2.05 
# 
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 NE A ARG 108 ? ? CZ  A ARG 108 ? ? 1.243 1.326 -0.083 0.013 N 
2 1 CZ A ARG 108 ? ? NH2 A ARG 108 ? ? 1.414 1.326 0.088  0.013 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 108 ? ? CZ A ARG 108 ? ? NH1 A ARG 108 ? ? 115.77 120.30 -4.53  0.50 N 
2 1 NE A ARG 108 ? ? CZ A ARG 108 ? ? NH2 A ARG 108 ? ? 112.66 120.30 -7.64  0.50 N 
3 1 CB A GLN 226 ? ? CA A GLN 226 ? ? C   A GLN 226 ? ? 86.73  110.40 -23.67 2.00 N 
4 1 N  A GLN 226 ? ? CA A GLN 226 ? ? C   A GLN 226 ? ? 141.30 111.00 30.30  2.70 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  ? ? -155.91 55.08   
2  1 ASP A 29  ? ? 56.79   -127.21 
3  1 SER A 195 ? ? -120.50 -155.91 
4  1 LEU A 230 ? ? -163.70 114.32  
5  1 GLU C 8   ? ? -144.38 28.73   
6  1 TRP B 60  ? ? 85.73   -3.59   
7  1 ARG D 16  ? ? 74.87   -11.36  
8  1 LYS D 43  ? ? 81.00   -1.17   
9  1 SER D 60  ? ? -161.45 118.82  
10 1 ALA D 97  ? ? -144.13 41.40   
11 1 ASP D 118 ? ? -156.09 55.32   
12 1 ILE E 46  ? ? -99.59  -61.50  
13 1 ASP E 155 ? ? -85.03  47.64   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     108 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.124 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_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     518 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   T 
_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 D MET 0   ? D MET 1   
3 1 Y 1 D PRO 203 ? D PRO 204 
4 1 Y 1 D GLU 204 ? D GLU 205 
5 1 Y 1 D SER 205 ? D SER 206 
6 1 Y 1 D SER 206 ? D 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  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
GOL C1   C N N 147 
GOL O1   O N N 148 
GOL C2   C N N 149 
GOL O2   O N N 150 
GOL C3   C N N 151 
GOL O3   O N N 152 
GOL H11  H N N 153 
GOL H12  H N N 154 
GOL HO1  H N N 155 
GOL H2   H N N 156 
GOL HO2  H N N 157 
GOL H31  H N N 158 
GOL H32  H N N 159 
GOL HO3  H N N 160 
HIS N    N N N 161 
HIS CA   C N S 162 
HIS C    C N N 163 
HIS O    O N N 164 
HIS CB   C N N 165 
HIS CG   C Y N 166 
HIS ND1  N Y N 167 
HIS CD2  C Y N 168 
HIS CE1  C Y N 169 
HIS NE2  N Y N 170 
HIS OXT  O N N 171 
HIS H    H N N 172 
HIS H2   H N N 173 
HIS HA   H N N 174 
HIS HB2  H N N 175 
HIS HB3  H N N 176 
HIS HD1  H N N 177 
HIS HD2  H N N 178 
HIS HE1  H N N 179 
HIS HE2  H N N 180 
HIS HXT  H N N 181 
HOH O    O N N 182 
HOH H1   H N N 183 
HOH H2   H N N 184 
ILE N    N N N 185 
ILE CA   C N S 186 
ILE C    C N N 187 
ILE O    O N N 188 
ILE CB   C N S 189 
ILE CG1  C N N 190 
ILE CG2  C N N 191 
ILE CD1  C N N 192 
ILE OXT  O N N 193 
ILE H    H N N 194 
ILE H2   H N N 195 
ILE HA   H N N 196 
ILE HB   H N N 197 
ILE HG12 H N N 198 
ILE HG13 H N N 199 
ILE HG21 H N N 200 
ILE HG22 H N N 201 
ILE HG23 H N N 202 
ILE HD11 H N N 203 
ILE HD12 H N N 204 
ILE HD13 H N N 205 
ILE HXT  H N N 206 
LEU N    N N N 207 
LEU CA   C N S 208 
LEU C    C N N 209 
LEU O    O N N 210 
LEU CB   C N N 211 
LEU CG   C N N 212 
LEU CD1  C N N 213 
LEU CD2  C N N 214 
LEU OXT  O N N 215 
LEU H    H N N 216 
LEU H2   H N N 217 
LEU HA   H N N 218 
LEU HB2  H N N 219 
LEU HB3  H N N 220 
LEU HG   H N N 221 
LEU HD11 H N N 222 
LEU HD12 H N N 223 
LEU HD13 H N N 224 
LEU HD21 H N N 225 
LEU HD22 H N N 226 
LEU HD23 H N N 227 
LEU HXT  H N N 228 
LYS N    N N N 229 
LYS CA   C N S 230 
LYS C    C N N 231 
LYS O    O N N 232 
LYS CB   C N N 233 
LYS CG   C N N 234 
LYS CD   C N N 235 
LYS CE   C N N 236 
LYS NZ   N N N 237 
LYS OXT  O N N 238 
LYS H    H N N 239 
LYS H2   H N N 240 
LYS HA   H N N 241 
LYS HB2  H N N 242 
LYS HB3  H N N 243 
LYS HG2  H N N 244 
LYS HG3  H N N 245 
LYS HD2  H N N 246 
LYS HD3  H N N 247 
LYS HE2  H N N 248 
LYS HE3  H N N 249 
LYS HZ1  H N N 250 
LYS HZ2  H N N 251 
LYS HZ3  H N N 252 
LYS HXT  H N N 253 
MET N    N N N 254 
MET CA   C N S 255 
MET C    C N N 256 
MET O    O N N 257 
MET CB   C N N 258 
MET CG   C N N 259 
MET SD   S N N 260 
MET CE   C N N 261 
MET OXT  O N N 262 
MET H    H N N 263 
MET H2   H N N 264 
MET HA   H N N 265 
MET HB2  H N N 266 
MET HB3  H N N 267 
MET HG2  H N N 268 
MET HG3  H N N 269 
MET HE1  H N N 270 
MET HE2  H N N 271 
MET HE3  H N N 272 
MET HXT  H N N 273 
PHE N    N N N 274 
PHE CA   C N S 275 
PHE C    C N N 276 
PHE O    O N N 277 
PHE CB   C N N 278 
PHE CG   C Y N 279 
PHE CD1  C Y N 280 
PHE CD2  C Y N 281 
PHE CE1  C Y N 282 
PHE CE2  C Y N 283 
PHE CZ   C Y N 284 
PHE OXT  O N N 285 
PHE H    H N N 286 
PHE H2   H N N 287 
PHE HA   H N N 288 
PHE HB2  H N N 289 
PHE HB3  H N N 290 
PHE HD1  H N N 291 
PHE HD2  H N N 292 
PHE HE1  H N N 293 
PHE HE2  H N N 294 
PHE HZ   H N N 295 
PHE HXT  H N N 296 
PRO N    N N N 297 
PRO CA   C N S 298 
PRO C    C N N 299 
PRO O    O N N 300 
PRO CB   C N N 301 
PRO CG   C N N 302 
PRO CD   C N N 303 
PRO OXT  O N N 304 
PRO H    H N N 305 
PRO HA   H N N 306 
PRO HB2  H N N 307 
PRO HB3  H N N 308 
PRO HG2  H N N 309 
PRO HG3  H N N 310 
PRO HD2  H N N 311 
PRO HD3  H N N 312 
PRO HXT  H N N 313 
SER N    N N N 314 
SER CA   C N S 315 
SER C    C N N 316 
SER O    O N N 317 
SER CB   C N N 318 
SER OG   O N N 319 
SER OXT  O N N 320 
SER H    H N N 321 
SER H2   H N N 322 
SER HA   H N N 323 
SER HB2  H N N 324 
SER HB3  H N N 325 
SER HG   H N N 326 
SER HXT  H N N 327 
THR N    N N N 328 
THR CA   C N S 329 
THR C    C N N 330 
THR O    O N N 331 
THR CB   C N R 332 
THR OG1  O N N 333 
THR CG2  C N N 334 
THR OXT  O N N 335 
THR H    H N N 336 
THR H2   H N N 337 
THR HA   H N N 338 
THR HB   H N N 339 
THR HG1  H N N 340 
THR HG21 H N N 341 
THR HG22 H N N 342 
THR HG23 H N N 343 
THR HXT  H N N 344 
TRP N    N N N 345 
TRP CA   C N S 346 
TRP C    C N N 347 
TRP O    O N N 348 
TRP CB   C N N 349 
TRP CG   C Y N 350 
TRP CD1  C Y N 351 
TRP CD2  C Y N 352 
TRP NE1  N Y N 353 
TRP CE2  C Y N 354 
TRP CE3  C Y N 355 
TRP CZ2  C Y N 356 
TRP CZ3  C Y N 357 
TRP CH2  C Y N 358 
TRP OXT  O N N 359 
TRP H    H N N 360 
TRP H2   H N N 361 
TRP HA   H N N 362 
TRP HB2  H N N 363 
TRP HB3  H N N 364 
TRP HD1  H N N 365 
TRP HE1  H N N 366 
TRP HE3  H N N 367 
TRP HZ2  H N N 368 
TRP HZ3  H N N 369 
TRP HH2  H N N 370 
TRP HXT  H N N 371 
TYR N    N N N 372 
TYR CA   C N S 373 
TYR C    C N N 374 
TYR O    O N N 375 
TYR CB   C N N 376 
TYR CG   C Y N 377 
TYR CD1  C Y N 378 
TYR CD2  C Y N 379 
TYR CE1  C Y N 380 
TYR CE2  C Y N 381 
TYR CZ   C Y N 382 
TYR OH   O N N 383 
TYR OXT  O N N 384 
TYR H    H N N 385 
TYR H2   H N N 386 
TYR HA   H N N 387 
TYR HB2  H N N 388 
TYR HB3  H N N 389 
TYR HD1  H N N 390 
TYR HD2  H N N 391 
TYR HE1  H N N 392 
TYR HE2  H N N 393 
TYR HH   H N N 394 
TYR HXT  H N N 395 
VAL N    N N N 396 
VAL CA   C N S 397 
VAL C    C N N 398 
VAL O    O N N 399 
VAL CB   C N N 400 
VAL CG1  C N N 401 
VAL CG2  C N N 402 
VAL OXT  O N N 403 
VAL H    H N N 404 
VAL H2   H N N 405 
VAL HA   H N N 406 
VAL HB   H N N 407 
VAL HG11 H N N 408 
VAL HG12 H N N 409 
VAL HG13 H N N 410 
VAL HG21 H N N 411 
VAL HG22 H N N 412 
VAL HG23 H N N 413 
VAL HXT  H N N 414 
# 
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  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
GOL C1  O1   sing N N 138 
GOL C1  C2   sing N N 139 
GOL C1  H11  sing N N 140 
GOL C1  H12  sing N N 141 
GOL O1  HO1  sing N N 142 
GOL C2  O2   sing N N 143 
GOL C2  C3   sing N N 144 
GOL C2  H2   sing N N 145 
GOL O2  HO2  sing N N 146 
GOL C3  O3   sing N N 147 
GOL C3  H31  sing N N 148 
GOL C3  H32  sing N N 149 
GOL O3  HO3  sing N N 150 
HIS N   CA   sing N N 151 
HIS N   H    sing N N 152 
HIS N   H2   sing N N 153 
HIS CA  C    sing N N 154 
HIS CA  CB   sing N N 155 
HIS CA  HA   sing N N 156 
HIS C   O    doub N N 157 
HIS C   OXT  sing N N 158 
HIS CB  CG   sing N N 159 
HIS CB  HB2  sing N N 160 
HIS CB  HB3  sing N N 161 
HIS CG  ND1  sing Y N 162 
HIS CG  CD2  doub Y N 163 
HIS ND1 CE1  doub Y N 164 
HIS ND1 HD1  sing N N 165 
HIS CD2 NE2  sing Y N 166 
HIS CD2 HD2  sing N N 167 
HIS CE1 NE2  sing Y N 168 
HIS CE1 HE1  sing N N 169 
HIS NE2 HE2  sing N N 170 
HIS OXT HXT  sing N N 171 
HOH O   H1   sing N N 172 
HOH O   H2   sing N N 173 
ILE N   CA   sing N N 174 
ILE N   H    sing N N 175 
ILE N   H2   sing N N 176 
ILE CA  C    sing N N 177 
ILE CA  CB   sing N N 178 
ILE CA  HA   sing N N 179 
ILE C   O    doub N N 180 
ILE C   OXT  sing N N 181 
ILE CB  CG1  sing N N 182 
ILE CB  CG2  sing N N 183 
ILE CB  HB   sing N N 184 
ILE CG1 CD1  sing N N 185 
ILE CG1 HG12 sing N N 186 
ILE CG1 HG13 sing N N 187 
ILE CG2 HG21 sing N N 188 
ILE CG2 HG22 sing N N 189 
ILE CG2 HG23 sing N N 190 
ILE CD1 HD11 sing N N 191 
ILE CD1 HD12 sing N N 192 
ILE CD1 HD13 sing N N 193 
ILE OXT HXT  sing N N 194 
LEU N   CA   sing N N 195 
LEU N   H    sing N N 196 
LEU N   H2   sing N N 197 
LEU CA  C    sing N N 198 
LEU CA  CB   sing N N 199 
LEU CA  HA   sing N N 200 
LEU C   O    doub N N 201 
LEU C   OXT  sing N N 202 
LEU CB  CG   sing N N 203 
LEU CB  HB2  sing N N 204 
LEU CB  HB3  sing N N 205 
LEU CG  CD1  sing N N 206 
LEU CG  CD2  sing N N 207 
LEU CG  HG   sing N N 208 
LEU CD1 HD11 sing N N 209 
LEU CD1 HD12 sing N N 210 
LEU CD1 HD13 sing N N 211 
LEU CD2 HD21 sing N N 212 
LEU CD2 HD22 sing N N 213 
LEU CD2 HD23 sing N N 214 
LEU OXT HXT  sing N N 215 
LYS N   CA   sing N N 216 
LYS N   H    sing N N 217 
LYS N   H2   sing N N 218 
LYS CA  C    sing N N 219 
LYS CA  CB   sing N N 220 
LYS CA  HA   sing N N 221 
LYS C   O    doub N N 222 
LYS C   OXT  sing N N 223 
LYS CB  CG   sing N N 224 
LYS CB  HB2  sing N N 225 
LYS CB  HB3  sing N N 226 
LYS CG  CD   sing N N 227 
LYS CG  HG2  sing N N 228 
LYS CG  HG3  sing N N 229 
LYS CD  CE   sing N N 230 
LYS CD  HD2  sing N N 231 
LYS CD  HD3  sing N N 232 
LYS CE  NZ   sing N N 233 
LYS CE  HE2  sing N N 234 
LYS CE  HE3  sing N N 235 
LYS NZ  HZ1  sing N N 236 
LYS NZ  HZ2  sing N N 237 
LYS NZ  HZ3  sing N N 238 
LYS OXT HXT  sing N N 239 
MET N   CA   sing N N 240 
MET N   H    sing N N 241 
MET N   H2   sing N N 242 
MET CA  C    sing N N 243 
MET CA  CB   sing N N 244 
MET CA  HA   sing N N 245 
MET C   O    doub N N 246 
MET C   OXT  sing N N 247 
MET CB  CG   sing N N 248 
MET CB  HB2  sing N N 249 
MET CB  HB3  sing N N 250 
MET CG  SD   sing N N 251 
MET CG  HG2  sing N N 252 
MET CG  HG3  sing N N 253 
MET SD  CE   sing N N 254 
MET CE  HE1  sing N N 255 
MET CE  HE2  sing N N 256 
MET CE  HE3  sing N N 257 
MET OXT HXT  sing N N 258 
PHE N   CA   sing N N 259 
PHE N   H    sing N N 260 
PHE N   H2   sing N N 261 
PHE CA  C    sing N N 262 
PHE CA  CB   sing N N 263 
PHE CA  HA   sing N N 264 
PHE C   O    doub N N 265 
PHE C   OXT  sing N N 266 
PHE CB  CG   sing N N 267 
PHE CB  HB2  sing N N 268 
PHE CB  HB3  sing N N 269 
PHE CG  CD1  doub Y N 270 
PHE CG  CD2  sing Y N 271 
PHE CD1 CE1  sing Y N 272 
PHE CD1 HD1  sing N N 273 
PHE CD2 CE2  doub Y N 274 
PHE CD2 HD2  sing N N 275 
PHE CE1 CZ   doub Y N 276 
PHE CE1 HE1  sing N N 277 
PHE CE2 CZ   sing Y N 278 
PHE CE2 HE2  sing N N 279 
PHE CZ  HZ   sing N N 280 
PHE OXT HXT  sing N N 281 
PRO N   CA   sing N N 282 
PRO N   CD   sing N N 283 
PRO N   H    sing N N 284 
PRO CA  C    sing N N 285 
PRO CA  CB   sing N N 286 
PRO CA  HA   sing N N 287 
PRO C   O    doub N N 288 
PRO C   OXT  sing N N 289 
PRO CB  CG   sing N N 290 
PRO CB  HB2  sing N N 291 
PRO CB  HB3  sing N N 292 
PRO CG  CD   sing N N 293 
PRO CG  HG2  sing N N 294 
PRO CG  HG3  sing N N 295 
PRO CD  HD2  sing N N 296 
PRO CD  HD3  sing N N 297 
PRO OXT HXT  sing N N 298 
SER N   CA   sing N N 299 
SER N   H    sing N N 300 
SER N   H2   sing N N 301 
SER CA  C    sing N N 302 
SER CA  CB   sing N N 303 
SER CA  HA   sing N N 304 
SER C   O    doub N N 305 
SER C   OXT  sing N N 306 
SER CB  OG   sing N N 307 
SER CB  HB2  sing N N 308 
SER CB  HB3  sing N N 309 
SER OG  HG   sing N N 310 
SER OXT HXT  sing N N 311 
THR N   CA   sing N N 312 
THR N   H    sing N N 313 
THR N   H2   sing N N 314 
THR CA  C    sing N N 315 
THR CA  CB   sing N N 316 
THR CA  HA   sing N N 317 
THR C   O    doub N N 318 
THR C   OXT  sing N N 319 
THR CB  OG1  sing N N 320 
THR CB  CG2  sing N N 321 
THR CB  HB   sing N N 322 
THR OG1 HG1  sing N N 323 
THR CG2 HG21 sing N N 324 
THR CG2 HG22 sing N N 325 
THR CG2 HG23 sing N N 326 
THR OXT HXT  sing N N 327 
TRP N   CA   sing N N 328 
TRP N   H    sing N N 329 
TRP N   H2   sing N N 330 
TRP CA  C    sing N N 331 
TRP CA  CB   sing N N 332 
TRP CA  HA   sing N N 333 
TRP C   O    doub N N 334 
TRP C   OXT  sing N N 335 
TRP CB  CG   sing N N 336 
TRP CB  HB2  sing N N 337 
TRP CB  HB3  sing N N 338 
TRP CG  CD1  doub Y N 339 
TRP CG  CD2  sing Y N 340 
TRP CD1 NE1  sing Y N 341 
TRP CD1 HD1  sing N N 342 
TRP CD2 CE2  doub Y N 343 
TRP CD2 CE3  sing Y N 344 
TRP NE1 CE2  sing Y N 345 
TRP NE1 HE1  sing N N 346 
TRP CE2 CZ2  sing Y N 347 
TRP CE3 CZ3  doub Y N 348 
TRP CE3 HE3  sing N N 349 
TRP CZ2 CH2  doub Y N 350 
TRP CZ2 HZ2  sing N N 351 
TRP CZ3 CH2  sing Y N 352 
TRP CZ3 HZ3  sing N N 353 
TRP CH2 HH2  sing N N 354 
TRP OXT HXT  sing N N 355 
TYR N   CA   sing N N 356 
TYR N   H    sing N N 357 
TYR N   H2   sing N N 358 
TYR CA  C    sing N N 359 
TYR CA  CB   sing N N 360 
TYR CA  HA   sing N N 361 
TYR C   O    doub N N 362 
TYR C   OXT  sing N N 363 
TYR CB  CG   sing N N 364 
TYR CB  HB2  sing N N 365 
TYR CB  HB3  sing N N 366 
TYR CG  CD1  doub Y N 367 
TYR CG  CD2  sing Y N 368 
TYR CD1 CE1  sing Y N 369 
TYR CD1 HD1  sing N N 370 
TYR CD2 CE2  doub Y N 371 
TYR CD2 HD2  sing N N 372 
TYR CE1 CZ   doub Y N 373 
TYR CE1 HE1  sing N N 374 
TYR CE2 CZ   sing Y N 375 
TYR CE2 HE2  sing N N 376 
TYR CZ  OH   sing N N 377 
TYR OH  HH   sing N N 378 
TYR OXT HXT  sing N N 379 
VAL N   CA   sing N N 380 
VAL N   H    sing N N 381 
VAL N   H2   sing N N 382 
VAL CA  C    sing N N 383 
VAL CA  CB   sing N N 384 
VAL CA  HA   sing N N 385 
VAL C   O    doub N N 386 
VAL C   OXT  sing N N 387 
VAL CB  CG1  sing N N 388 
VAL CB  CG2  sing N N 389 
VAL CB  HB   sing N N 390 
VAL CG1 HG11 sing N N 391 
VAL CG1 HG12 sing N N 392 
VAL CG1 HG13 sing N N 393 
VAL CG2 HG21 sing N N 394 
VAL CG2 HG22 sing N N 395 
VAL CG2 HG23 sing N N 396 
VAL OXT HXT  sing N N 397 
# 
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   '4NDM, 6VQO, 6MPP' 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YIV 
_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]   0.014056 
_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]   0.007506 
_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]   0.004495 
_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   ? 8.274  35.791  -25.394 1.00 76.45  ?  1   GLY A N   1 
ATOM   2    C CA  . GLY A 1 2   ? 7.787  34.924  -24.333 1.00 75.09  ?  1   GLY A CA  1 
ATOM   3    C C   . GLY A 1 2   ? 8.318  33.521  -24.510 1.00 62.99  ?  1   GLY A C   1 
ATOM   4    O O   . GLY A 1 2   ? 7.548  32.573  -24.652 1.00 61.53  ?  1   GLY A O   1 
ATOM   5    N N   . SER A 1 3   ? 9.645  33.405  -24.511 1.00 58.08  ?  2   SER A N   1 
ATOM   6    C CA  . SER A 1 3   ? 10.319 32.156  -24.810 1.00 49.91  ?  2   SER A CA  1 
ATOM   7    C C   . SER A 1 3   ? 10.085 31.128  -23.699 1.00 44.26  ?  2   SER A C   1 
ATOM   8    O O   . SER A 1 3   ? 9.585  31.434  -22.609 1.00 47.93  ?  2   SER A O   1 
ATOM   9    C CB  . SER A 1 3   ? 11.813 32.401  -25.011 1.00 50.32  ?  2   SER A CB  1 
ATOM   10   O OG  . SER A 1 3   ? 12.408 32.881  -23.813 1.00 56.34  ?  2   SER A OG  1 
ATOM   11   N N   . HIS A 1 4   ? 10.435 29.879  -24.003 1.00 41.14  ?  3   HIS A N   1 
ATOM   12   C CA  . HIS A 1 4   ? 10.333 28.801  -23.035 1.00 40.55  ?  3   HIS A CA  1 
ATOM   13   C C   . HIS A 1 4   ? 11.541 27.883  -23.166 1.00 36.25  ?  3   HIS A C   1 
ATOM   14   O O   . HIS A 1 4   ? 12.324 27.969  -24.120 1.00 43.28  ?  3   HIS A O   1 
ATOM   15   C CB  . HIS A 1 4   ? 9.045  27.997  -23.197 1.00 35.91  ?  3   HIS A CB  1 
ATOM   16   C CG  . HIS A 1 4   ? 7.797  28.816  -23.122 1.00 44.54  ?  3   HIS A CG  1 
ATOM   17   N ND1 . HIS A 1 4   ? 6.978  28.825  -22.016 1.00 47.74  ?  3   HIS A ND1 1 
ATOM   18   C CD2 . HIS A 1 4   ? 7.212  29.633  -24.031 1.00 48.66  ?  3   HIS A CD2 1 
ATOM   19   C CE1 . HIS A 1 4   ? 5.942  29.612  -22.245 1.00 49.54  ?  3   HIS A CE1 1 
ATOM   20   N NE2 . HIS A 1 4   ? 6.066  30.122  -23.457 1.00 48.76  ?  3   HIS A NE2 1 
ATOM   21   N N   . SER A 1 5   ? 11.673 26.987  -22.185 1.00 39.91  ?  4   SER A N   1 
ATOM   22   C CA  . SER A 1 5   ? 12.863 26.169  -22.061 1.00 37.73  ?  4   SER A CA  1 
ATOM   23   C C   . SER A 1 5   ? 12.511 24.761  -21.634 1.00 32.10  ?  4   SER A C   1 
ATOM   24   O O   . SER A 1 5   ? 11.572 24.541  -20.867 1.00 35.00  ?  4   SER A O   1 
ATOM   25   C CB  . SER A 1 5   ? 13.843 26.747  -21.028 1.00 37.49  ?  4   SER A CB  1 
ATOM   26   O OG  . SER A 1 5   ? 14.790 27.564  -21.672 1.00 44.95  ?  4   SER A OG  1 
ATOM   27   N N   . MET A 1 6   ? 13.319 23.809  -22.118 1.00 36.37  ?  5   MET A N   1 
ATOM   28   C CA  . MET A 1 6   ? 13.369 22.464  -21.564 1.00 39.26  ?  5   MET A CA  1 
ATOM   29   C C   . MET A 1 6   ? 14.803 22.158  -21.139 1.00 30.96  ?  5   MET A C   1 
ATOM   30   O O   . MET A 1 6   ? 15.759 22.485  -21.850 1.00 29.56  ?  5   MET A O   1 
ATOM   31   C CB  . MET A 1 6   ? 12.880 21.378  -22.550 1.00 31.82  ?  5   MET A CB  1 
ATOM   32   C CG  . MET A 1 6   ? 12.639 20.059  -21.817 1.00 32.32  ?  5   MET A CG  1 
ATOM   33   S SD  . MET A 1 6   ? 11.696 18.764  -22.653 1.00 36.47  ?  5   MET A SD  1 
ATOM   34   C CE  . MET A 1 6   ? 12.753 18.501  -24.057 1.00 27.42  ?  5   MET A CE  1 
ATOM   35   N N   . ARG A 1 7   ? 14.986 21.629  -19.944 1.00 31.85  ?  6   ARG A N   1 
ATOM   36   C CA  . ARG A 1 7   ? 16.332 21.373  -19.415 1.00 30.70  ?  6   ARG A CA  1 
ATOM   37   C C   . ARG A 1 7   ? 16.314 20.054  -18.634 1.00 28.76  ?  6   ARG A C   1 
ATOM   38   O O   . ARG A 1 7   ? 15.358 19.780  -18.007 1.00 28.15  ?  6   ARG A O   1 
ATOM   39   C CB  . ARG A 1 7   ? 16.806 22.457  -18.448 1.00 31.45  ?  6   ARG A CB  1 
ATOM   40   C CG  . ARG A 1 7   ? 16.839 23.912  -18.901 1.00 38.32  ?  6   ARG A CG  1 
ATOM   41   C CD  . ARG A 1 7   ? 18.134 24.466  -19.431 1.00 38.78  ?  6   ARG A CD  1 
ATOM   42   N NE  . ARG A 1 7   ? 18.256 24.568  -20.855 1.00 54.11  ?  6   ARG A NE  1 
ATOM   43   C CZ  . ARG A 1 7   ? 17.879 25.609  -21.550 1.00 42.63  ?  6   ARG A CZ  1 
ATOM   44   N NH1 . ARG A 1 7   ? 17.465 26.691  -20.938 1.00 54.39  ?  6   ARG A NH1 1 
ATOM   45   N NH2 . ARG A 1 7   ? 17.982 25.585  -22.844 1.00 54.42  ?  6   ARG A NH2 1 
ATOM   46   N N   . TYR A 1 8   ? 17.332 19.237  -18.765 1.00 27.64  ?  7   TYR A N   1 
ATOM   47   C CA  . TYR A 1 8   ? 17.544 18.049  -17.957 1.00 24.93  ?  7   TYR A CA  1 
ATOM   48   C C   . TYR A 1 8   ? 18.816 18.247  -17.132 1.00 24.00  ?  7   TYR A C   1 
ATOM   49   O O   . TYR A 1 8   ? 19.800 18.775  -17.635 1.00 25.64  ?  7   TYR A O   1 
ATOM   50   C CB  . TYR A 1 8   ? 17.657 16.812  -18.847 1.00 26.91  ?  7   TYR A CB  1 
ATOM   51   C CG  . TYR A 1 8   ? 16.321 16.251  -19.270 1.00 26.73  ?  7   TYR A CG  1 
ATOM   52   C CD1 . TYR A 1 8   ? 15.630 15.396  -18.448 1.00 26.63  ?  7   TYR A CD1 1 
ATOM   53   C CD2 . TYR A 1 8   ? 15.767 16.563  -20.499 1.00 28.32  ?  7   TYR A CD2 1 
ATOM   54   C CE1 . TYR A 1 8   ? 14.418 14.882  -18.815 1.00 27.87  ?  7   TYR A CE1 1 
ATOM   55   C CE2 . TYR A 1 8   ? 14.562 16.029  -20.885 1.00 29.86  ?  7   TYR A CE2 1 
ATOM   56   C CZ  . TYR A 1 8   ? 13.886 15.200  -20.047 1.00 31.30  ?  7   TYR A CZ  1 
ATOM   57   O OH  . TYR A 1 8   ? 12.658 14.654  -20.426 1.00 30.19  ?  7   TYR A OH  1 
ATOM   58   N N   . PHE A 1 9   ? 18.783 17.841  -15.866 1.00 28.04  ?  8   PHE A N   1 
ATOM   59   C CA  . PHE A 1 9   ? 19.907 17.990  -14.940 1.00 28.65  ?  8   PHE A CA  1 
ATOM   60   C C   . PHE A 1 9   ? 20.282 16.613  -14.399 1.00 21.08  ?  8   PHE A C   1 
ATOM   61   O O   . PHE A 1 9   ? 19.476 15.978  -13.728 1.00 25.67  ?  8   PHE A O   1 
ATOM   62   C CB  . PHE A 1 9   ? 19.536 18.944  -13.789 1.00 24.69  ?  8   PHE A CB  1 
ATOM   63   C CG  . PHE A 1 9   ? 19.150 20.340  -14.248 1.00 26.05  ?  8   PHE A CG  1 
ATOM   64   C CD1 . PHE A 1 9   ? 17.862 20.623  -14.634 1.00 30.14  ?  8   PHE A CD1 1 
ATOM   65   C CD2 . PHE A 1 9   ? 20.085 21.367  -14.272 1.00 34.24  ?  8   PHE A CD2 1 
ATOM   66   C CE1 . PHE A 1 9   ? 17.500 21.906  -15.068 1.00 33.94  ?  8   PHE A CE1 1 
ATOM   67   C CE2 . PHE A 1 9   ? 19.738 22.647  -14.695 1.00 32.48  ?  8   PHE A CE2 1 
ATOM   68   C CZ  . PHE A 1 9   ? 18.438 22.910  -15.106 1.00 36.71  ?  8   PHE A CZ  1 
ATOM   69   N N   . PHE A 1 10  ? 21.488 16.158  -14.693 1.00 21.30  ?  9   PHE A N   1 
ATOM   70   C CA  . PHE A 1 10  ? 21.949 14.844  -14.274 1.00 24.99  ?  9   PHE A CA  1 
ATOM   71   C C   . PHE A 1 10  ? 23.040 14.979  -13.220 1.00 25.31  ?  9   PHE A C   1 
ATOM   72   O O   . PHE A 1 10  ? 23.965 15.786  -13.377 1.00 23.24  ?  9   PHE A O   1 
ATOM   73   C CB  . PHE A 1 10  ? 22.522 14.034  -15.456 1.00 24.60  ?  9   PHE A CB  1 
ATOM   74   C CG  . PHE A 1 10  ? 21.519 13.732  -16.535 1.00 26.96  ?  9   PHE A CG  1 
ATOM   75   C CD1 . PHE A 1 10  ? 21.259 14.653  -17.535 1.00 29.91  ?  9   PHE A CD1 1 
ATOM   76   C CD2 . PHE A 1 10  ? 20.824 12.542  -16.534 1.00 30.71  ?  9   PHE A CD2 1 
ATOM   77   C CE1 . PHE A 1 10  ? 20.320 14.378  -18.528 1.00 30.52  ?  9   PHE A CE1 1 
ATOM   78   C CE2 . PHE A 1 10  ? 19.888 12.264  -17.524 1.00 31.37  ?  9   PHE A CE2 1 
ATOM   79   C CZ  . PHE A 1 10  ? 19.637 13.180  -18.509 1.00 24.09  ?  9   PHE A CZ  1 
ATOM   80   N N   . THR A 1 11  ? 22.951 14.145  -12.183 1.00 24.03  ?  10  THR A N   1 
ATOM   81   C CA  . THR A 1 11  ? 23.953 14.069  -11.120 1.00 24.57  ?  10  THR A CA  1 
ATOM   82   C C   . THR A 1 11  ? 24.299 12.607  -10.862 1.00 24.30  ?  10  THR A C   1 
ATOM   83   O O   . THR A 1 11  ? 23.437 11.835  -10.424 1.00 25.93  ?  10  THR A O   1 
ATOM   84   C CB  . THR A 1 11  ? 23.457 14.703  -9.805  1.00 25.84  ?  10  THR A CB  1 
ATOM   85   O OG1 . THR A 1 11  ? 22.981 16.036  -10.012 1.00 25.42  ?  10  THR A OG1 1 
ATOM   86   C CG2 . THR A 1 11  ? 24.606 14.739  -8.752  1.00 25.84  ?  10  THR A CG2 1 
ATOM   87   N N   . SER A 1 12  ? 25.565 12.246  -11.096 1.00 27.29  ?  11  SER A N   1 
ATOM   88   C CA  . SER A 1 12  ? 26.098 10.917  -10.825 1.00 26.71  ?  11  SER A CA  1 
ATOM   89   C C   . SER A 1 12  ? 27.260 10.998  -9.838  1.00 26.33  ?  11  SER A C   1 
ATOM   90   O O   . SER A 1 12  ? 28.259 11.681  -10.094 1.00 23.00  ?  11  SER A O   1 
ATOM   91   C CB  . SER A 1 12  ? 26.572 10.245  -12.121 1.00 30.41  ?  11  SER A CB  1 
ATOM   92   O OG  . SER A 1 12  ? 25.484 10.080  -13.036 1.00 29.37  ?  11  SER A OG  1 
ATOM   93   N N   . VAL A 1 13  ? 27.160 10.234  -8.755  1.00 20.06  ?  12  VAL A N   1 
ATOM   94   C CA  . VAL A 1 13  ? 28.064 10.358  -7.618  1.00 31.58  ?  12  VAL A CA  1 
ATOM   95   C C   . VAL A 1 13  ? 28.576 8.975   -7.255  1.00 29.29  ?  12  VAL A C   1 
ATOM   96   O O   . VAL A 1 13  ? 27.783 8.090   -6.930  1.00 30.59  ?  12  VAL A O   1 
ATOM   97   C CB  . VAL A 1 13  ? 27.355 10.999  -6.413  1.00 29.72  ?  12  VAL A CB  1 
ATOM   98   C CG1 . VAL A 1 13  ? 28.303 11.169  -5.186  1.00 32.31  ?  12  VAL A CG1 1 
ATOM   99   C CG2 . VAL A 1 13  ? 26.724 12.335  -6.818  1.00 29.34  ?  12  VAL A CG2 1 
ATOM   100  N N   . SER A 1 14  ? 29.897 8.801   -7.272  1.00 32.40  ?  13  SER A N   1 
ATOM   101  C CA  . SER A 1 14  ? 30.494 7.571   -6.771  1.00 34.01  ?  13  SER A CA  1 
ATOM   102  C C   . SER A 1 14  ? 30.505 7.556   -5.241  1.00 35.14  ?  13  SER A C   1 
ATOM   103  O O   . SER A 1 14  ? 30.632 8.584   -4.570  1.00 29.73  ?  13  SER A O   1 
ATOM   104  C CB  . SER A 1 14  ? 31.911 7.387   -7.318  1.00 30.42  ?  13  SER A CB  1 
ATOM   105  O OG  . SER A 1 14  ? 32.807 8.396   -6.911  1.00 31.58  ?  13  SER A OG  1 
ATOM   106  N N   . ARG A 1 15  ? 30.344 6.365   -4.693  1.00 36.90  ?  14  ARG A N   1 
ATOM   107  C CA  . ARG A 1 15  ? 30.218 6.161   -3.253  1.00 49.27  ?  14  ARG A CA  1 
ATOM   108  C C   . ARG A 1 15  ? 31.163 5.028   -2.896  1.00 57.34  ?  14  ARG A C   1 
ATOM   109  O O   . ARG A 1 15  ? 30.742 3.873   -2.772  1.00 65.30  ?  14  ARG A O   1 
ATOM   110  C CB  . ARG A 1 15  ? 28.778 5.845   -2.857  1.00 49.73  ?  14  ARG A CB  1 
ATOM   111  C CG  . ARG A 1 15  ? 27.807 6.975   -3.144  1.00 49.37  ?  14  ARG A CG  1 
ATOM   112  C CD  . ARG A 1 15  ? 26.388 6.587   -2.764  1.00 53.97  ?  14  ARG A CD  1 
ATOM   113  N NE  . ARG A 1 15  ? 25.848 5.567   -3.656  1.00 48.70  ?  14  ARG A NE  1 
ATOM   114  C CZ  . ARG A 1 15  ? 24.579 5.175   -3.655  1.00 50.89  ?  14  ARG A CZ  1 
ATOM   115  N NH1 . ARG A 1 15  ? 23.715 5.716   -2.797  1.00 53.96  ?  14  ARG A NH1 1 
ATOM   116  N NH2 . ARG A 1 15  ? 24.171 4.249   -4.522  1.00 52.95  ?  14  ARG A NH2 1 
ATOM   117  N N   . PRO A 1 16  ? 32.458 5.315   -2.765  1.00 54.12  ?  15  PRO A N   1 
ATOM   118  C CA  . PRO A 1 16  ? 33.417 4.265   -2.385  1.00 64.50  ?  15  PRO A CA  1 
ATOM   119  C C   . PRO A 1 16  ? 33.135 3.808   -0.960  1.00 64.66  ?  15  PRO A C   1 
ATOM   120  O O   . PRO A 1 16  ? 33.234 4.590   -0.017  1.00 60.10  ?  15  PRO A O   1 
ATOM   121  C CB  . PRO A 1 16  ? 34.775 4.964   -2.506  1.00 59.71  ?  15  PRO A CB  1 
ATOM   122  C CG  . PRO A 1 16  ? 34.463 6.423   -2.237  1.00 53.57  ?  15  PRO A CG  1 
ATOM   123  C CD  . PRO A 1 16  ? 33.063 6.657   -2.772  1.00 50.08  ?  15  PRO A CD  1 
ATOM   124  N N   . GLY A 1 17  ? 32.771 2.545   -0.811  1.00 77.62  ?  16  GLY A N   1 
ATOM   125  C CA  . GLY A 1 17  ? 32.319 2.030   0.457   1.00 98.72  ?  16  GLY A CA  1 
ATOM   126  C C   . GLY A 1 17  ? 30.848 1.717   0.591   1.00 124.45 ?  16  GLY A C   1 
ATOM   127  O O   . GLY A 1 17  ? 30.390 1.439   1.704   1.00 128.72 ?  16  GLY A O   1 
ATOM   128  N N   . ARG A 1 18  ? 30.077 1.876   -0.499  1.00 189.03 ?  17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 18  ? 28.582 1.884   -0.479  1.00 194.14 ?  17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 18  ? 28.030 1.488   -1.856  1.00 155.95 ?  17  ARG A C   1 
ATOM   131  O O   . ARG A 1 18  ? 27.291 2.264   -2.452  1.00 107.10 ?  17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 18  ? 28.036 3.285   -0.163  1.00 30.00  ?  17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 18  ? 27.509 3.542   1.244   1.00 30.00  ?  17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 18  ? 28.150 4.783   1.838   1.00 30.00  ?  17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 18  ? 29.556 4.565   2.119   1.00 30.00  ?  17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 18  ? 30.218 5.012   3.192   1.00 30.00  ?  17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 18  ? 29.597 5.727   4.116   1.00 30.00  ?  17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 18  ? 31.507 4.729   3.335   1.00 30.00  ?  17  ARG A NH2 1 
ATOM   139  N N   . GLY A 1 19  ? 28.415 0.343   -2.400  1.00 114.77 ?  18  GLY A N   1 
ATOM   140  C CA  . GLY A 1 19  ? 27.840 -0.088  -3.656  1.00 100.19 ?  18  GLY A CA  1 
ATOM   141  C C   . GLY A 1 19  ? 28.107 0.824   -4.854  1.00 81.04  ?  18  GLY A C   1 
ATOM   142  O O   . GLY A 1 19  ? 29.035 1.644   -4.884  1.00 68.70  ?  18  GLY A O   1 
ATOM   143  N N   . GLU A 1 20  ? 27.259 0.648   -5.870  1.00 66.98  ?  19  GLU A N   1 
ATOM   144  C CA  . GLU A 1 20  ? 27.390 1.403   -7.108  1.00 62.97  ?  19  GLU A CA  1 
ATOM   145  C C   . GLU A 1 20  ? 27.164 2.894   -6.859  1.00 50.24  ?  19  GLU A C   1 
ATOM   146  O O   . GLU A 1 20  ? 26.749 3.316   -5.772  1.00 46.85  ?  19  GLU A O   1 
ATOM   147  C CB  . GLU A 1 20  ? 26.407 0.901   -8.177  1.00 61.11  ?  19  GLU A CB  1 
ATOM   148  C CG  . GLU A 1 20  ? 26.285 -0.622  -8.331  1.00 68.94  ?  19  GLU A CG  1 
ATOM   149  C CD  . GLU A 1 20  ? 27.624 -1.331  -8.492  1.00 81.11  ?  19  GLU A CD  1 
ATOM   150  O OE1 . GLU A 1 20  ? 27.919 -2.219  -7.658  1.00 86.69  ?  19  GLU A OE1 1 
ATOM   151  O OE2 . GLU A 1 20  ? 28.371 -1.011  -9.452  1.00 77.10  ?  19  GLU A OE2 1 
ATOM   152  N N   . PRO A 1 21  ? 27.440 3.725   -7.845  1.00 42.30  ?  20  PRO A N   1 
ATOM   153  C CA  . PRO A 1 21  ? 27.122 5.151   -7.717  1.00 35.53  ?  20  PRO A CA  1 
ATOM   154  C C   . PRO A 1 21  ? 25.623 5.385   -7.608  1.00 36.92  ?  20  PRO A C   1 
ATOM   155  O O   . PRO A 1 21  ? 24.791 4.519   -7.881  1.00 37.15  ?  20  PRO A O   1 
ATOM   156  C CB  . PRO A 1 21  ? 27.700 5.758   -8.995  1.00 36.38  ?  20  PRO A CB  1 
ATOM   157  C CG  . PRO A 1 21  ? 28.699 4.753   -9.485  1.00 36.12  ?  20  PRO A CG  1 
ATOM   158  C CD  . PRO A 1 21  ? 28.258 3.414   -9.024  1.00 40.07  ?  20  PRO A CD  1 
ATOM   159  N N   . ARG A 1 22  ? 25.267 6.588   -7.191  1.00 27.60  ?  21  ARG A N   1 
ATOM   160  C CA  . ARG A 1 22  ? 23.883 7.035   -7.281  1.00 34.68  ?  21  ARG A CA  1 
ATOM   161  C C   . ARG A 1 22  ? 23.708 7.914   -8.516  1.00 29.75  ?  21  ARG A C   1 
ATOM   162  O O   . ARG A 1 22  ? 24.509 8.819   -8.748  1.00 29.43  ?  21  ARG A O   1 
ATOM   163  C CB  . ARG A 1 22  ? 23.464 7.807   -6.035  1.00 34.64  ?  21  ARG A CB  1 
ATOM   164  C CG  . ARG A 1 22  ? 21.984 8.118   -5.990  1.00 38.00  ?  21  ARG A CG  1 
ATOM   165  C CD  . ARG A 1 22  ? 21.685 8.760   -4.668  1.00 37.15  ?  21  ARG A CD  1 
ATOM   166  N NE  . ARG A 1 22  ? 20.289 9.109   -4.472  1.00 42.19  ?  21  ARG A NE  1 
ATOM   167  C CZ  . ARG A 1 22  ? 19.800 9.540   -3.317  1.00 42.28  ?  21  ARG A CZ  1 
ATOM   168  N NH1 . ARG A 1 22  ? 20.597 9.652   -2.257  1.00 48.12  ?  21  ARG A NH1 1 
ATOM   169  N NH2 . ARG A 1 22  ? 18.521 9.840   -3.215  1.00 36.64  ?  21  ARG A NH2 1 
ATOM   170  N N   . PHE A 1 23  ? 22.666 7.630   -9.308  1.00 30.41  ?  22  PHE A N   1 
ATOM   171  C CA  . PHE A 1 23  ? 22.354 8.357   -10.540 1.00 29.54  ?  22  PHE A CA  1 
ATOM   172  C C   . PHE A 1 23  ? 21.014 9.049   -10.350 1.00 29.00  ?  22  PHE A C   1 
ATOM   173  O O   . PHE A 1 23  ? 20.014 8.395   -10.035 1.00 29.85  ?  22  PHE A O   1 
ATOM   174  C CB  . PHE A 1 23  ? 22.313 7.418   -11.749 1.00 31.38  ?  22  PHE A CB  1 
ATOM   175  C CG  . PHE A 1 23  ? 23.551 6.549   -11.876 1.00 28.33  ?  22  PHE A CG  1 
ATOM   176  C CD1 . PHE A 1 23  ? 24.711 7.043   -12.472 1.00 26.67  ?  22  PHE A CD1 1 
ATOM   177  C CD2 . PHE A 1 23  ? 23.550 5.240   -11.387 1.00 30.64  ?  22  PHE A CD2 1 
ATOM   178  C CE1 . PHE A 1 23  ? 25.863 6.242   -12.573 1.00 27.12  ?  22  PHE A CE1 1 
ATOM   179  C CE2 . PHE A 1 23  ? 24.683 4.436   -11.485 1.00 29.69  ?  22  PHE A CE2 1 
ATOM   180  C CZ  . PHE A 1 23  ? 25.840 4.938   -12.072 1.00 32.78  ?  22  PHE A CZ  1 
ATOM   181  N N   . ILE A 1 24  ? 21.001 10.366  -10.512 1.00 27.99  ?  23  ILE A N   1 
ATOM   182  C CA  . ILE A 1 24  ? 19.780 11.151  -10.382 1.00 28.23  ?  23  ILE A CA  1 
ATOM   183  C C   . ILE A 1 24  ? 19.656 12.018  -11.621 1.00 26.85  ?  23  ILE A C   1 
ATOM   184  O O   . ILE A 1 24  ? 20.648 12.504  -12.170 1.00 25.77  ?  23  ILE A O   1 
ATOM   185  C CB  . ILE A 1 24  ? 19.784 12.037  -9.119  1.00 28.69  ?  23  ILE A CB  1 
ATOM   186  C CG1 . ILE A 1 24  ? 19.845 11.191  -7.849  1.00 35.82  ?  23  ILE A CG1 1 
ATOM   187  C CG2 . ILE A 1 24  ? 18.547 12.938  -9.065  1.00 29.48  ?  23  ILE A CG2 1 
ATOM   188  C CD1 . ILE A 1 24  ? 20.183 11.997  -6.583  1.00 30.02  ?  23  ILE A CD1 1 
ATOM   189  N N   . ALA A 1 25  ? 18.424 12.226  -12.056 1.00 27.24  ?  24  ALA A N   1 
ATOM   190  C CA  . ALA A 1 25  ? 18.175 13.118  -13.179 1.00 31.94  ?  24  ALA A CA  1 
ATOM   191  C C   . ALA A 1 25  ? 16.834 13.788  -12.924 1.00 25.17  ?  24  ALA A C   1 
ATOM   192  O O   . ALA A 1 25  ? 15.910 13.159  -12.405 1.00 22.67  ?  24  ALA A O   1 
ATOM   193  C CB  . ALA A 1 25  ? 18.176 12.359  -14.520 1.00 33.46  ?  24  ALA A CB  1 
ATOM   194  N N   . VAL A 1 26  ? 16.734 15.063  -13.267 1.00 23.80  ?  25  VAL A N   1 
ATOM   195  C CA  . VAL A 1 26  ? 15.445 15.732  -13.212 1.00 27.32  ?  25  VAL A CA  1 
ATOM   196  C C   . VAL A 1 26  ? 15.276 16.518  -14.508 1.00 26.22  ?  25  VAL A C   1 
ATOM   197  O O   . VAL A 1 26  ? 16.245 17.010  -15.088 1.00 32.86  ?  25  VAL A O   1 
ATOM   198  C CB  . VAL A 1 26  ? 15.293 16.660  -11.989 1.00 27.44  ?  25  VAL A CB  1 
ATOM   199  C CG1 . VAL A 1 26  ? 15.225 15.861  -10.650 1.00 30.06  ?  25  VAL A CG1 1 
ATOM   200  C CG2 . VAL A 1 26  ? 16.417 17.680  -11.980 1.00 24.55  ?  25  VAL A CG2 1 
ATOM   201  N N   . GLY A 1 27  ? 14.033 16.625  -14.952 1.00 27.67  ?  26  GLY A N   1 
ATOM   202  C CA  . GLY A 1 27  ? 13.704 17.391  -16.143 1.00 30.13  ?  26  GLY A CA  1 
ATOM   203  C C   . GLY A 1 27  ? 12.760 18.556  -15.780 1.00 26.75  ?  26  GLY A C   1 
ATOM   204  O O   . GLY A 1 27  ? 11.876 18.381  -14.964 1.00 27.76  ?  26  GLY A O   1 
ATOM   205  N N   . TYR A 1 28  ? 13.006 19.701  -16.409 1.00 29.47  ?  27  TYR A N   1 
ATOM   206  C CA  . TYR A 1 28  ? 12.205 20.901  -16.201 1.00 33.83  ?  27  TYR A CA  1 
ATOM   207  C C   . TYR A 1 28  ? 11.671 21.430  -17.525 1.00 33.22  ?  27  TYR A C   1 
ATOM   208  O O   . TYR A 1 28  ? 12.350 21.382  -18.550 1.00 28.15  ?  27  TYR A O   1 
ATOM   209  C CB  . TYR A 1 28  ? 13.029 22.051  -15.568 1.00 34.76  ?  27  TYR A CB  1 
ATOM   210  C CG  . TYR A 1 28  ? 13.246 21.960  -14.080 1.00 27.88  ?  27  TYR A CG  1 
ATOM   211  C CD1 . TYR A 1 28  ? 14.216 21.119  -13.555 1.00 31.29  ?  27  TYR A CD1 1 
ATOM   212  C CD2 . TYR A 1 28  ? 12.485 22.724  -13.196 1.00 36.63  ?  27  TYR A CD2 1 
ATOM   213  C CE1 . TYR A 1 28  ? 14.416 21.024  -12.178 1.00 31.23  ?  27  TYR A CE1 1 
ATOM   214  C CE2 . TYR A 1 28  ? 12.677 22.637  -11.836 1.00 31.67  ?  27  TYR A CE2 1 
ATOM   215  C CZ  . TYR A 1 28  ? 13.651 21.790  -11.333 1.00 37.89  ?  27  TYR A CZ  1 
ATOM   216  O OH  . TYR A 1 28  ? 13.850 21.707  -9.972  1.00 44.47  ?  27  TYR A OH  1 
ATOM   217  N N   . VAL A 1 29  ? 10.478 22.015  -17.473 1.00 34.56  ?  28  VAL A N   1 
ATOM   218  C CA  . VAL A 1 29  ? 10.019 22.945  -18.498 1.00 33.89  ?  28  VAL A CA  1 
ATOM   219  C C   . VAL A 1 29  ? 9.914  24.315  -17.836 1.00 31.42  ?  28  VAL A C   1 
ATOM   220  O O   . VAL A 1 29  ? 9.122  24.502  -16.908 1.00 33.46  ?  28  VAL A O   1 
ATOM   221  C CB  . VAL A 1 29  ? 8.675  22.522  -19.106 1.00 33.49  ?  28  VAL A CB  1 
ATOM   222  C CG1 . VAL A 1 29  ? 8.148  23.632  -20.020 1.00 37.69  ?  28  VAL A CG1 1 
ATOM   223  C CG2 . VAL A 1 29  ? 8.816  21.211  -19.870 1.00 42.00  ?  28  VAL A CG2 1 
ATOM   224  N N   . ASP A 1 30  ? 10.696 25.270  -18.315 1.00 32.73  ?  29  ASP A N   1 
ATOM   225  C CA  . ASP A 1 30  ? 10.796 26.568  -17.649 1.00 38.11  ?  29  ASP A CA  1 
ATOM   226  C C   . ASP A 1 30  ? 11.235 26.311  -16.207 1.00 38.10  ?  29  ASP A C   1 
ATOM   227  O O   . ASP A 1 30  ? 12.243 25.617  -15.986 1.00 37.85  ?  29  ASP A O   1 
ATOM   228  C CB  . ASP A 1 30  ? 9.465  27.296  -17.812 1.00 35.29  ?  29  ASP A CB  1 
ATOM   229  C CG  . ASP A 1 30  ? 9.153  27.639  -19.256 1.00 37.02  ?  29  ASP A CG  1 
ATOM   230  O OD1 . ASP A 1 30  ? 10.088 27.710  -20.090 1.00 40.29  ?  29  ASP A OD1 1 
ATOM   231  O OD2 . ASP A 1 30  ? 7.954  27.859  -19.536 1.00 43.43  -1 29  ASP A OD2 1 
ATOM   232  N N   . ASP A 1 31  ? 10.523 26.828  -15.204 1.00 34.53  ?  30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31  ? 10.864 26.620  -13.804 1.00 38.14  ?  30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31  ? 9.942  25.611  -13.138 1.00 37.83  ?  30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31  ? 9.742  25.660  -11.919 1.00 41.61  ?  30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31  ? 10.838 27.960  -13.063 1.00 42.16  ?  30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31  ? 11.854 28.937  -13.613 1.00 40.52  ?  30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31  ? 12.998 28.501  -13.865 1.00 45.25  ?  30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31  ? 11.525 30.131  -13.814 1.00 41.55  -1 30  ASP A OD2 1 
ATOM   240  N N   . THR A 1 32  ? 9.375  24.698  -13.925 1.00 33.14  ?  31  THR A N   1 
ATOM   241  C CA  . THR A 1 32  ? 8.483  23.652  -13.441 1.00 28.18  ?  31  THR A CA  1 
ATOM   242  C C   . THR A 1 32  ? 9.136  22.313  -13.742 1.00 34.89  ?  31  THR A C   1 
ATOM   243  O O   . THR A 1 32  ? 9.454  22.022  -14.903 1.00 38.54  ?  31  THR A O   1 
ATOM   244  C CB  . THR A 1 32  ? 7.114  23.757  -14.123 1.00 40.18  ?  31  THR A CB  1 
ATOM   245  O OG1 . THR A 1 32  ? 6.478  24.989  -13.751 1.00 46.67  ?  31  THR A OG1 1 
ATOM   246  C CG2 . THR A 1 32  ? 6.222  22.614  -13.746 1.00 35.32  ?  31  THR A CG2 1 
ATOM   247  N N   . GLN A 1 33  ? 9.356  21.515  -12.702 1.00 36.33  ?  32  GLN A N   1 
ATOM   248  C CA  . GLN A 1 33  ? 9.882  20.170  -12.874 1.00 37.51  ?  32  GLN A CA  1 
ATOM   249  C C   . GLN A 1 33  ? 8.763  19.226  -13.285 1.00 41.29  ?  32  GLN A C   1 
ATOM   250  O O   . GLN A 1 33  ? 7.624  19.355  -12.825 1.00 34.90  ?  32  GLN A O   1 
ATOM   251  C CB  . GLN A 1 33  ? 10.496 19.656  -11.580 1.00 35.46  ?  32  GLN A CB  1 
ATOM   252  C CG  . GLN A 1 33  ? 11.253 18.362  -11.734 1.00 36.02  ?  32  GLN A CG  1 
ATOM   253  C CD  . GLN A 1 33  ? 11.530 17.693  -10.401 1.00 37.56  ?  32  GLN A CD  1 
ATOM   254  O OE1 . GLN A 1 33  ? 11.486 18.337  -9.355  1.00 39.42  ?  32  GLN A OE1 1 
ATOM   255  N NE2 . GLN A 1 33  ? 11.803 16.388  -10.431 1.00 39.39  ?  32  GLN A NE2 1 
ATOM   256  N N   . PHE A 1 34  ? 9.097  18.238  -14.118 1.00 37.46  ?  33  PHE A N   1 
ATOM   257  C CA  . PHE A 1 34  ? 8.073  17.297  -14.567 1.00 35.19  ?  33  PHE A CA  1 
ATOM   258  C C   . PHE A 1 34  ? 8.460  15.835  -14.509 1.00 33.41  ?  33  PHE A C   1 
ATOM   259  O O   . PHE A 1 34  ? 7.552  14.999  -14.406 1.00 36.59  ?  33  PHE A O   1 
ATOM   260  C CB  . PHE A 1 34  ? 7.593  17.649  -15.991 1.00 35.18  ?  33  PHE A CB  1 
ATOM   261  C CG  . PHE A 1 34  ? 8.609  17.451  -17.095 1.00 31.70  ?  33  PHE A CG  1 
ATOM   262  C CD1 . PHE A 1 34  ? 9.619  18.351  -17.294 1.00 30.09  ?  33  PHE A CD1 1 
ATOM   263  C CD2 . PHE A 1 34  ? 8.500  16.377  -17.970 1.00 32.29  ?  33  PHE A CD2 1 
ATOM   264  C CE1 . PHE A 1 34  ? 10.511 18.193  -18.326 1.00 32.35  ?  33  PHE A CE1 1 
ATOM   265  C CE2 . PHE A 1 34  ? 9.408  16.202  -19.007 1.00 28.77  ?  33  PHE A CE2 1 
ATOM   266  C CZ  . PHE A 1 34  ? 10.395 17.106  -19.194 1.00 31.60  ?  33  PHE A CZ  1 
ATOM   267  N N   . VAL A 1 35  ? 9.753  15.485  -14.508 1.00 32.02  ?  34  VAL A N   1 
ATOM   268  C CA  . VAL A 1 35  ? 10.170 14.097  -14.332 1.00 32.08  ?  34  VAL A CA  1 
ATOM   269  C C   . VAL A 1 35  ? 11.364 14.003  -13.394 1.00 33.67  ?  34  VAL A C   1 
ATOM   270  O O   . VAL A 1 35  ? 12.085 14.976  -13.164 1.00 31.12  ?  34  VAL A O   1 
ATOM   271  C CB  . VAL A 1 35  ? 10.535 13.415  -15.669 1.00 34.45  ?  34  VAL A CB  1 
ATOM   272  C CG1 . VAL A 1 35  ? 9.275  13.248  -16.533 1.00 35.82  ?  34  VAL A CG1 1 
ATOM   273  C CG2 . VAL A 1 35  ? 11.619 14.213  -16.409 1.00 30.36  ?  34  VAL A CG2 1 
ATOM   274  N N   . ARG A 1 36  ? 11.574 12.789  -12.884 1.00 31.45  ?  35  ARG A N   1 
ATOM   275  C CA  . ARG A 1 36  ? 12.685 12.497  -11.995 1.00 35.96  ?  35  ARG A CA  1 
ATOM   276  C C   . ARG A 1 36  ? 13.103 11.042  -12.153 1.00 36.09  ?  35  ARG A C   1 
ATOM   277  O O   . ARG A 1 36  ? 12.276 10.163  -12.414 1.00 32.75  ?  35  ARG A O   1 
ATOM   278  C CB  . ARG A 1 36  ? 12.319 12.770  -10.519 1.00 37.41  ?  35  ARG A CB  1 
ATOM   279  C CG  . ARG A 1 36  ? 11.474 11.686  -9.848  1.00 38.04  ?  35  ARG A CG  1 
ATOM   280  C CD  . ARG A 1 36  ? 11.814 11.536  -8.344  1.00 47.95  ?  35  ARG A CD  1 
ATOM   281  N NE  . ARG A 1 36  ? 11.070 10.428  -7.735  1.00 52.36  ?  35  ARG A NE  1 
ATOM   282  C CZ  . ARG A 1 36  ? 10.080 10.564  -6.846  1.00 53.75  ?  35  ARG A CZ  1 
ATOM   283  N NH1 . ARG A 1 36  ? 9.709  11.763  -6.414  1.00 53.94  ?  35  ARG A NH1 1 
ATOM   284  N NH2 . ARG A 1 36  ? 9.452  9.492   -6.375  1.00 55.52  ?  35  ARG A NH2 1 
ATOM   285  N N   . PHE A 1 37  ? 14.389 10.793  -11.932 1.00 35.27  ?  36  PHE A N   1 
ATOM   286  C CA  . PHE A 1 37  ? 14.914 9.443   -11.819 1.00 33.24  ?  36  PHE A CA  1 
ATOM   287  C C   . PHE A 1 37  ? 15.916 9.426   -10.674 1.00 34.17  ?  36  PHE A C   1 
ATOM   288  O O   . PHE A 1 37  ? 16.730 10.349  -10.558 1.00 30.35  ?  36  PHE A O   1 
ATOM   289  C CB  . PHE A 1 37  ? 15.591 8.995   -13.114 1.00 31.31  ?  36  PHE A CB  1 
ATOM   290  C CG  . PHE A 1 37  ? 16.088 7.591   -13.063 1.00 35.09  ?  36  PHE A CG  1 
ATOM   291  C CD1 . PHE A 1 37  ? 17.330 7.300   -12.508 1.00 35.52  ?  36  PHE A CD1 1 
ATOM   292  C CD2 . PHE A 1 37  ? 15.300 6.556   -13.531 1.00 35.76  ?  36  PHE A CD2 1 
ATOM   293  C CE1 . PHE A 1 37  ? 17.791 5.987   -12.439 1.00 42.69  ?  36  PHE A CE1 1 
ATOM   294  C CE2 . PHE A 1 37  ? 15.737 5.244   -13.478 1.00 35.90  ?  36  PHE A CE2 1 
ATOM   295  C CZ  . PHE A 1 37  ? 16.984 4.943   -12.931 1.00 39.89  ?  36  PHE A CZ  1 
ATOM   296  N N   . ASP A 1 38  ? 15.847 8.385   -9.836  1.00 31.69  ?  37  ASP A N   1 
ATOM   297  C CA  . ASP A 1 38  ? 16.762 8.190   -8.706  1.00 37.18  ?  37  ASP A CA  1 
ATOM   298  C C   . ASP A 1 38  ? 17.030 6.695   -8.592  1.00 35.34  ?  37  ASP A C   1 
ATOM   299  O O   . ASP A 1 38  ? 16.137 5.928   -8.220  1.00 38.42  ?  37  ASP A O   1 
ATOM   300  C CB  . ASP A 1 38  ? 16.174 8.738   -7.403  1.00 34.02  ?  37  ASP A CB  1 
ATOM   301  C CG  . ASP A 1 38  ? 17.156 8.693   -6.222  1.00 37.93  ?  37  ASP A CG  1 
ATOM   302  O OD1 . ASP A 1 38  ? 18.292 8.177   -6.347  1.00 35.78  ?  37  ASP A OD1 1 
ATOM   303  O OD2 . ASP A 1 38  ? 16.767 9.185   -5.143  1.00 39.76  -1 37  ASP A OD2 1 
ATOM   304  N N   . SER A 1 39  ? 18.249 6.282   -8.940  1.00 33.98  ?  38  SER A N   1 
ATOM   305  C CA  . SER A 1 39  ? 18.642 4.879   -8.867  1.00 39.62  ?  38  SER A CA  1 
ATOM   306  C C   . SER A 1 39  ? 18.578 4.312   -7.447  1.00 39.49  ?  38  SER A C   1 
ATOM   307  O O   . SER A 1 39  ? 18.616 3.090   -7.286  1.00 40.65  ?  38  SER A O   1 
ATOM   308  C CB  . SER A 1 39  ? 20.058 4.723   -9.452  1.00 37.42  ?  38  SER A CB  1 
ATOM   309  O OG  . SER A 1 39  ? 21.050 5.386   -8.674  1.00 32.29  ?  38  SER A OG  1 
ATOM   310  N N   . ASP A 1 40  ? 18.465 5.150   -6.419  1.00 39.29  ?  39  ASP A N   1 
ATOM   311  C CA  . ASP A 1 40  ? 18.291 4.604   -5.078  1.00 45.49  ?  39  ASP A CA  1 
ATOM   312  C C   . ASP A 1 40  ? 16.849 4.198   -4.812  1.00 47.40  ?  39  ASP A C   1 
ATOM   313  O O   . ASP A 1 40  ? 16.607 3.334   -3.965  1.00 53.93  ?  39  ASP A O   1 
ATOM   314  C CB  . ASP A 1 40  ? 18.723 5.615   -4.014  1.00 44.47  ?  39  ASP A CB  1 
ATOM   315  C CG  . ASP A 1 40  ? 20.190 5.493   -3.641  1.00 42.20  ?  39  ASP A CG  1 
ATOM   316  O OD1 . ASP A 1 40  ? 20.902 4.620   -4.195  1.00 43.44  ?  39  ASP A OD1 1 
ATOM   317  O OD2 . ASP A 1 40  ? 20.626 6.285   -2.784  1.00 49.86  -1 39  ASP A OD2 1 
ATOM   318  N N   . ALA A 1 41  ? 15.890 4.814   -5.505  1.00 47.81  ?  40  ALA A N   1 
ATOM   319  C CA  . ALA A 1 41  ? 14.478 4.566   -5.255  1.00 49.08  ?  40  ALA A CA  1 
ATOM   320  C C   . ALA A 1 41  ? 14.102 3.163   -5.706  1.00 42.91  ?  40  ALA A C   1 
ATOM   321  O O   . ALA A 1 41  ? 14.828 2.507   -6.454  1.00 45.95  ?  40  ALA A O   1 
ATOM   322  C CB  . ALA A 1 41  ? 13.607 5.592   -5.982  1.00 52.21  ?  40  ALA A CB  1 
ATOM   323  N N   . ALA A 1 42  ? 12.946 2.697   -5.238  1.00 51.74  ?  41  ALA A N   1 
ATOM   324  C CA  . ALA A 1 42  ? 12.558 1.320   -5.531  1.00 53.42  ?  41  ALA A CA  1 
ATOM   325  C C   . ALA A 1 42  ? 12.065 1.158   -6.962  1.00 45.08  ?  41  ALA A C   1 
ATOM   326  O O   . ALA A 1 42  ? 12.248 0.092   -7.560  1.00 53.23  ?  41  ALA A O   1 
ATOM   327  C CB  . ALA A 1 42  ? 11.483 0.857   -4.556  1.00 50.22  ?  41  ALA A CB  1 
ATOM   328  N N   . SER A 1 43  ? 11.465 2.205   -7.526  1.00 50.06  ?  42  SER A N   1 
ATOM   329  C CA  . SER A 1 43  ? 10.905 2.126   -8.872  1.00 47.14  ?  42  SER A CA  1 
ATOM   330  C C   . SER A 1 43  ? 11.918 1.610   -9.885  1.00 47.48  ?  42  SER A C   1 
ATOM   331  O O   . SER A 1 43  ? 11.618 0.701   -10.668 1.00 50.08  ?  42  SER A O   1 
ATOM   332  C CB  . SER A 1 43  ? 10.400 3.509   -9.296  1.00 48.78  ?  42  SER A CB  1 
ATOM   333  O OG  . SER A 1 43  ? 11.379 4.195   -10.059 1.00 54.05  ?  42  SER A OG  1 
ATOM   334  N N   . GLN A 1 44  ? 13.118 2.201   -9.896  1.00 46.08  ?  43  GLN A N   1 
ATOM   335  C CA  . GLN A 1 44  ? 14.092 2.054   -10.978 1.00 44.49  ?  43  GLN A CA  1 
ATOM   336  C C   . GLN A 1 44  ? 13.547 2.574   -12.308 1.00 40.78  ?  43  GLN A C   1 
ATOM   337  O O   . GLN A 1 44  ? 14.054 2.208   -13.378 1.00 36.00  ?  43  GLN A O   1 
ATOM   338  C CB  . GLN A 1 44  ? 14.548 0.599   -11.121 1.00 45.01  ?  43  GLN A CB  1 
ATOM   339  C CG  . GLN A 1 44  ? 15.291 0.065   -9.897  1.00 44.21  ?  43  GLN A CG  1 
ATOM   340  C CD  . GLN A 1 44  ? 16.596 0.801   -9.629  1.00 43.05  ?  43  GLN A CD  1 
ATOM   341  O OE1 . GLN A 1 44  ? 17.523 0.785   -10.451 1.00 47.90  ?  43  GLN A OE1 1 
ATOM   342  N NE2 . GLN A 1 44  ? 16.676 1.444   -8.469  1.00 40.76  ?  43  GLN A NE2 1 
ATOM   343  N N   . LYS A 1 45  ? 12.547 3.459   -12.242 1.00 38.69  ?  44  LYS A N   1 
ATOM   344  C CA  . LYS A 1 45  ? 11.843 3.990   -13.402 1.00 33.20  ?  44  LYS A CA  1 
ATOM   345  C C   . LYS A 1 45  ? 11.881 5.511   -13.392 1.00 37.80  ?  44  LYS A C   1 
ATOM   346  O O   . LYS A 1 45  ? 11.908 6.140   -12.332 1.00 32.72  ?  44  LYS A O   1 
ATOM   347  C CB  . LYS A 1 45  ? 10.369 3.538   -13.413 1.00 39.56  ?  44  LYS A CB  1 
ATOM   348  C CG  . LYS A 1 45  ? 10.139 2.190   -14.105 1.00 44.86  ?  44  LYS A CG  1 
ATOM   349  C CD  . LYS A 1 45  ? 9.853  1.108   -13.093 1.00 48.35  ?  44  LYS A CD  1 
ATOM   350  C CE  . LYS A 1 45  ? 9.737  -0.263  -13.751 1.00 48.62  ?  44  LYS A CE  1 
ATOM   351  N NZ  . LYS A 1 45  ? 10.977 -0.578  -14.541 1.00 55.08  ?  44  LYS A NZ  1 
ATOM   352  N N   . MET A 1 46  ? 11.883 6.106   -14.580 1.00 29.42  ?  45  MET A N   1 
ATOM   353  C CA  . MET A 1 46  ? 11.547 7.519   -14.685 1.00 32.66  ?  45  MET A CA  1 
ATOM   354  C C   . MET A 1 46  ? 10.128 7.714   -14.167 1.00 35.79  ?  45  MET A C   1 
ATOM   355  O O   . MET A 1 46  ? 9.245  6.897   -14.428 1.00 38.19  ?  45  MET A O   1 
ATOM   356  C CB  . MET A 1 46  ? 11.664 7.981   -16.127 1.00 26.13  ?  45  MET A CB  1 
ATOM   357  C CG  . MET A 1 46  ? 11.512 9.457   -16.305 1.00 36.31  ?  45  MET A CG  1 
ATOM   358  S SD  . MET A 1 46  ? 12.999 10.329  -15.746 1.00 39.97  ?  45  MET A SD  1 
ATOM   359  C CE  . MET A 1 46  ? 13.847 10.659  -17.303 1.00 33.11  ?  45  MET A CE  1 
ATOM   360  N N   . GLU A 1 47  ? 9.910  8.781   -13.400 1.00 37.57  ?  46  GLU A N   1 
ATOM   361  C CA  . GLU A 1 47  ? 8.628  8.974   -12.742 1.00 36.52  ?  46  GLU A CA  1 
ATOM   362  C C   . GLU A 1 47  ? 8.111  10.379  -13.017 1.00 34.96  ?  46  GLU A C   1 
ATOM   363  O O   . GLU A 1 47  ? 8.897  11.314  -13.194 1.00 34.71  ?  46  GLU A O   1 
ATOM   364  C CB  . GLU A 1 47  ? 8.706  8.776   -11.220 1.00 36.92  ?  46  GLU A CB  1 
ATOM   365  C CG  . GLU A 1 47  ? 9.319  7.470   -10.710 1.00 41.03  ?  46  GLU A CG  1 
ATOM   366  C CD  . GLU A 1 47  ? 9.803  7.586   -9.239  1.00 52.60  ?  46  GLU A CD  1 
ATOM   367  O OE1 . GLU A 1 47  ? 8.955  7.803   -8.347  1.00 53.04  ?  46  GLU A OE1 1 
ATOM   368  O OE2 . GLU A 1 47  ? 11.026 7.486   -8.968  1.00 54.04  -1 46  GLU A OE2 1 
ATOM   369  N N   . PRO A 1 48  ? 6.794  10.557  -13.044 1.00 34.57  ?  47  PRO A N   1 
ATOM   370  C CA  . PRO A 1 48  ? 6.233  11.883  -13.304 1.00 40.06  ?  47  PRO A CA  1 
ATOM   371  C C   . PRO A 1 48  ? 6.238  12.736  -12.052 1.00 34.68  ?  47  PRO A C   1 
ATOM   372  O O   . PRO A 1 48  ? 6.082  12.239  -10.938 1.00 32.44  ?  47  PRO A O   1 
ATOM   373  C CB  . PRO A 1 48  ? 4.799  11.583  -13.755 1.00 39.39  ?  47  PRO A CB  1 
ATOM   374  C CG  . PRO A 1 48  ? 4.456  10.321  -13.096 1.00 34.82  ?  47  PRO A CG  1 
ATOM   375  C CD  . PRO A 1 48  ? 5.741  9.543   -12.873 1.00 36.05  ?  47  PRO A CD  1 
ATOM   376  N N   . ARG A 1 49  ? 6.423  14.041  -12.262 1.00 38.60  ?  48  ARG A N   1 
ATOM   377  C CA  . ARG A 1 49  ? 6.410  15.021  -11.179 1.00 43.27  ?  48  ARG A CA  1 
ATOM   378  C C   . ARG A 1 49  ? 5.550  16.245  -11.507 1.00 42.85  ?  48  ARG A C   1 
ATOM   379  O O   . ARG A 1 49  ? 5.574  17.225  -10.752 1.00 42.89  ?  48  ARG A O   1 
ATOM   380  C CB  . ARG A 1 49  ? 7.845  15.452  -10.841 1.00 35.36  ?  48  ARG A CB  1 
ATOM   381  C CG  . ARG A 1 49  ? 8.716  14.282  -10.365 1.00 39.06  ?  48  ARG A CG  1 
ATOM   382  C CD  . ARG A 1 49  ? 8.371  13.833  -8.947  1.00 43.30  ?  48  ARG A CD  1 
ATOM   383  N NE  . ARG A 1 49  ? 8.882  14.787  -7.957  1.00 45.34  ?  48  ARG A NE  1 
ATOM   384  C CZ  . ARG A 1 49  ? 8.528  14.806  -6.669  1.00 56.84  ?  48  ARG A CZ  1 
ATOM   385  N NH1 . ARG A 1 49  ? 7.663  13.913  -6.199  1.00 56.95  ?  48  ARG A NH1 1 
ATOM   386  N NH2 . ARG A 1 49  ? 9.035  15.721  -5.847  1.00 47.84  ?  48  ARG A NH2 1 
ATOM   387  N N   . ALA A 1 50  ? 4.812  16.223  -12.614 1.00 42.16  ?  49  ALA A N   1 
ATOM   388  C CA  . ALA A 1 50  ? 3.794  17.216  -12.931 1.00 44.97  ?  49  ALA A CA  1 
ATOM   389  C C   . ALA A 1 50  ? 2.562  16.499  -13.460 1.00 51.35  ?  49  ALA A C   1 
ATOM   390  O O   . ALA A 1 50  ? 2.671  15.434  -14.086 1.00 45.63  ?  49  ALA A O   1 
ATOM   391  C CB  . ALA A 1 50  ? 4.292  18.248  -13.954 1.00 42.34  ?  49  ALA A CB  1 
ATOM   392  N N   . PRO A 1 51  ? 1.368  17.039  -13.205 1.00 53.03  ?  50  PRO A N   1 
ATOM   393  C CA  . PRO A 1 51  ? 0.153  16.324  -13.625 1.00 48.91  ?  50  PRO A CA  1 
ATOM   394  C C   . PRO A 1 51  ? 0.006  16.224  -15.138 1.00 43.74  ?  50  PRO A C   1 
ATOM   395  O O   . PRO A 1 51  ? -0.564 15.244  -15.623 1.00 43.98  ?  50  PRO A O   1 
ATOM   396  C CB  . PRO A 1 51  ? -0.978 17.147  -12.985 1.00 54.24  ?  50  PRO A CB  1 
ATOM   397  C CG  . PRO A 1 51  ? -0.423 18.546  -12.896 1.00 51.48  ?  50  PRO A CG  1 
ATOM   398  C CD  . PRO A 1 51  ? 1.080  18.391  -12.680 1.00 50.83  ?  50  PRO A CD  1 
ATOM   399  N N   . TRP A 1 52  ? 0.525  17.186  -15.903 1.00 43.38  ?  51  TRP A N   1 
ATOM   400  C CA  . TRP A 1 52  ? 0.341  17.170  -17.347 1.00 42.60  ?  51  TRP A CA  1 
ATOM   401  C C   . TRP A 1 52  ? 1.285  16.220  -18.079 1.00 48.79  ?  51  TRP A C   1 
ATOM   402  O O   . TRP A 1 52  ? 1.153  16.063  -19.299 1.00 47.64  ?  51  TRP A O   1 
ATOM   403  C CB  . TRP A 1 52  ? 0.516  18.571  -17.907 1.00 44.88  ?  51  TRP A CB  1 
ATOM   404  C CG  . TRP A 1 52  ? 1.735  19.315  -17.441 1.00 52.06  ?  51  TRP A CG  1 
ATOM   405  C CD1 . TRP A 1 52  ? 1.784  20.300  -16.484 1.00 48.00  ?  51  TRP A CD1 1 
ATOM   406  C CD2 . TRP A 1 52  ? 3.079  19.156  -17.920 1.00 46.56  ?  51  TRP A CD2 1 
ATOM   407  N NE1 . TRP A 1 52  ? 3.072  20.758  -16.349 1.00 48.61  ?  51  TRP A NE1 1 
ATOM   408  C CE2 . TRP A 1 52  ? 3.886  20.071  -17.214 1.00 48.30  ?  51  TRP A CE2 1 
ATOM   409  C CE3 . TRP A 1 52  ? 3.680  18.316  -18.866 1.00 45.69  ?  51  TRP A CE3 1 
ATOM   410  C CZ2 . TRP A 1 52  ? 5.258  20.176  -17.433 1.00 44.70  ?  51  TRP A CZ2 1 
ATOM   411  C CZ3 . TRP A 1 52  ? 5.039  18.421  -19.078 1.00 39.23  ?  51  TRP A CZ3 1 
ATOM   412  C CH2 . TRP A 1 52  ? 5.814  19.348  -18.374 1.00 42.50  ?  51  TRP A CH2 1 
ATOM   413  N N   . ILE A 1 53  ? 2.239  15.595  -17.386 1.00 41.84  ?  52  ILE A N   1 
ATOM   414  C CA  . ILE A 1 53  ? 3.022  14.524  -17.991 1.00 43.79  ?  52  ILE A CA  1 
ATOM   415  C C   . ILE A 1 53  ? 2.471  13.151  -17.649 1.00 39.62  ?  52  ILE A C   1 
ATOM   416  O O   . ILE A 1 53  ? 2.881  12.166  -18.277 1.00 40.10  ?  52  ILE A O   1 
ATOM   417  C CB  . ILE A 1 53  ? 4.501  14.580  -17.566 1.00 36.66  ?  52  ILE A CB  1 
ATOM   418  C CG1 . ILE A 1 53  ? 5.370  13.741  -18.509 1.00 36.42  ?  52  ILE A CG1 1 
ATOM   419  C CG2 . ILE A 1 53  ? 4.648  14.012  -16.183 1.00 36.22  ?  52  ILE A CG2 1 
ATOM   420  C CD1 . ILE A 1 53  ? 5.986  14.514  -19.629 1.00 32.55  ?  52  ILE A CD1 1 
ATOM   421  N N   . GLU A 1 54  ? 1.585  13.047  -16.647 1.00 39.91  ?  53  GLU A N   1 
ATOM   422  C CA  . GLU A 1 54  ? 0.985  11.765  -16.290 1.00 43.22  ?  53  GLU A CA  1 
ATOM   423  C C   . GLU A 1 54  ? 0.169  11.190  -17.437 1.00 40.71  ?  53  GLU A C   1 
ATOM   424  O O   . GLU A 1 54  ? -0.151 9.997   -17.423 1.00 43.62  ?  53  GLU A O   1 
ATOM   425  C CB  . GLU A 1 54  ? 0.098  11.922  -15.052 1.00 45.08  ?  53  GLU A CB  1 
ATOM   426  C CG  . GLU A 1 54  ? 0.854  11.957  -13.734 1.00 50.70  ?  53  GLU A CG  1 
ATOM   427  C CD  . GLU A 1 54  ? 0.101  12.710  -12.654 1.00 58.60  ?  53  GLU A CD  1 
ATOM   428  O OE1 . GLU A 1 54  ? 0.724  13.078  -11.637 1.00 63.98  ?  53  GLU A OE1 1 
ATOM   429  O OE2 . GLU A 1 54  ? -1.118 12.936  -12.814 1.00 61.14  -1 53  GLU A OE2 1 
ATOM   430  N N   . GLN A 1 55  ? -0.162 12.028  -18.426 1.00 42.57  ?  54  GLN A N   1 
ATOM   431  C CA  . GLN A 1 55  ? -0.853 11.570  -19.621 1.00 45.41  ?  54  GLN A CA  1 
ATOM   432  C C   . GLN A 1 55  ? -0.034 10.531  -20.365 1.00 44.38  ?  54  GLN A C   1 
ATOM   433  O O   . GLN A 1 55  ? -0.582 9.555   -20.882 1.00 44.14  ?  54  GLN A O   1 
ATOM   434  C CB  . GLN A 1 55  ? -1.101 12.733  -20.575 1.00 43.62  ?  54  GLN A CB  1 
ATOM   435  C CG  . GLN A 1 55  ? -1.858 13.932  -20.070 1.00 56.29  ?  54  GLN A CG  1 
ATOM   436  C CD  . GLN A 1 55  ? -1.871 15.050  -21.119 1.00 51.54  ?  54  GLN A CD  1 
ATOM   437  O OE1 . GLN A 1 55  ? -1.775 16.226  -20.781 1.00 53.64  ?  54  GLN A OE1 1 
ATOM   438  N NE2 . GLN A 1 55  ? -1.977 14.676  -22.399 1.00 52.20  ?  54  GLN A NE2 1 
ATOM   439  N N   . GLU A 1 56  ? 1.273  10.773  -20.484 1.00 42.44  ?  55  GLU A N   1 
ATOM   440  C CA  . GLU A 1 56  ? 2.162  9.910   -21.250 1.00 37.60  ?  55  GLU A CA  1 
ATOM   441  C C   . GLU A 1 56  ? 1.903  8.450   -20.930 1.00 33.23  ?  55  GLU A C   1 
ATOM   442  O O   . GLU A 1 56  ? 1.724  8.078   -19.769 1.00 39.39  ?  55  GLU A O   1 
ATOM   443  C CB  . GLU A 1 56  ? 3.614  10.292  -20.944 1.00 37.51  ?  55  GLU A CB  1 
ATOM   444  C CG  . GLU A 1 56  ? 3.909  11.762  -21.250 1.00 39.14  ?  55  GLU A CG  1 
ATOM   445  C CD  . GLU A 1 56  ? 3.641  12.108  -22.720 1.00 35.72  ?  55  GLU A CD  1 
ATOM   446  O OE1 . GLU A 1 56  ? 3.671  13.304  -23.103 1.00 36.85  ?  55  GLU A OE1 1 
ATOM   447  O OE2 . GLU A 1 56  ? 3.429  11.164  -23.504 1.00 38.63  -1 55  GLU A OE2 1 
ATOM   448  N N   . GLY A 1 57  ? 1.844  7.620   -21.986 1.00 35.05  ?  56  GLY A N   1 
ATOM   449  C CA  . GLY A 1 57  ? 1.532  6.221   -21.829 1.00 34.71  ?  56  GLY A CA  1 
ATOM   450  C C   . GLY A 1 57  ? 2.719  5.393   -21.373 1.00 37.44  ?  56  GLY A C   1 
ATOM   451  O O   . GLY A 1 57  ? 3.838  5.889   -21.187 1.00 37.45  ?  56  GLY A O   1 
ATOM   452  N N   . PRO A 1 58  ? 2.475  4.085   -21.201 1.00 37.28  ?  57  PRO A N   1 
ATOM   453  C CA  . PRO A 1 58  ? 3.498  3.220   -20.596 1.00 39.08  ?  57  PRO A CA  1 
ATOM   454  C C   . PRO A 1 58  ? 4.742  3.102   -21.427 1.00 39.30  ?  57  PRO A C   1 
ATOM   455  O O   . PRO A 1 58  ? 5.800  2.776   -20.877 1.00 34.85  ?  57  PRO A O   1 
ATOM   456  C CB  . PRO A 1 58  ? 2.793  1.858   -20.460 1.00 39.60  ?  57  PRO A CB  1 
ATOM   457  C CG  . PRO A 1 58  ? 1.336  2.165   -20.567 1.00 38.68  ?  57  PRO A CG  1 
ATOM   458  C CD  . PRO A 1 58  ? 1.240  3.342   -21.491 1.00 40.51  ?  57  PRO A CD  1 
ATOM   459  N N   . GLU A 1 59  ? 4.631  3.356   -22.718 1.00 34.05  ?  58  GLU A N   1 
ATOM   460  C CA  . GLU A 1 59  ? 5.809  3.248   -23.598 1.00 36.83  ?  58  GLU A CA  1 
ATOM   461  C C   . GLU A 1 59  ? 6.732  4.444   -23.427 1.00 34.61  ?  58  GLU A C   1 
ATOM   462  O O   . GLU A 1 59  ? 7.879  4.292   -23.612 1.00 31.30  ?  58  GLU A O   1 
ATOM   463  C CB  . GLU A 1 59  ? 5.407  3.073   -25.039 1.00 36.07  ?  58  GLU A CB  1 
ATOM   464  C CG  . GLU A 1 59  ? 5.021  1.659   -25.287 1.00 45.27  ?  58  GLU A CG  1 
ATOM   465  C CD  . GLU A 1 59  ? 3.803  1.562   -26.140 1.00 52.95  ?  58  GLU A CD  1 
ATOM   466  O OE1 . GLU A 1 59  ? 2.738  1.899   -25.648 1.00 58.70  ?  58  GLU A OE1 1 
ATOM   467  O OE2 . GLU A 1 59  ? 3.953  1.147   -27.266 1.00 56.86  -1 58  GLU A OE2 1 
ATOM   468  N N   . TYR A 1 60  ? 6.181  5.610   -23.202 1.00 33.77  ?  59  TYR A N   1 
ATOM   469  C CA  . TYR A 1 60  ? 7.027  6.751   -22.896 1.00 37.05  ?  59  TYR A CA  1 
ATOM   470  C C   . TYR A 1 60  ? 7.868  6.461   -21.662 1.00 32.07  ?  59  TYR A C   1 
ATOM   471  O O   . TYR A 1 60  ? 9.098  6.594   -21.687 1.00 36.14  ?  59  TYR A O   1 
ATOM   472  C CB  . TYR A 1 60  ? 6.164  7.987   -22.681 1.00 35.30  ?  59  TYR A CB  1 
ATOM   473  C CG  . TYR A 1 60  ? 6.895  9.217   -22.228 1.00 27.84  ?  59  TYR A CG  1 
ATOM   474  C CD1 . TYR A 1 60  ? 7.404  10.097  -23.148 1.00 31.36  ?  59  TYR A CD1 1 
ATOM   475  C CD2 . TYR A 1 60  ? 7.042  9.517   -20.879 1.00 32.47  ?  59  TYR A CD2 1 
ATOM   476  C CE1 . TYR A 1 60  ? 8.048  11.222  -22.769 1.00 32.47  ?  59  TYR A CE1 1 
ATOM   477  C CE2 . TYR A 1 60  ? 7.689  10.669  -20.485 1.00 29.78  ?  59  TYR A CE2 1 
ATOM   478  C CZ  . TYR A 1 60  ? 8.190  11.510  -21.437 1.00 30.45  ?  59  TYR A CZ  1 
ATOM   479  O OH  . TYR A 1 60  ? 8.845  12.665  -21.094 1.00 31.29  ?  59  TYR A OH  1 
ATOM   480  N N   . TRP A 1 61  ? 7.214  6.044   -20.576 1.00 30.88  ?  60  TRP A N   1 
ATOM   481  C CA  . TRP A 1 61  ? 7.940  5.763   -19.342 1.00 38.32  ?  60  TRP A CA  1 
ATOM   482  C C   . TRP A 1 61  ? 8.974  4.671   -19.558 1.00 37.67  ?  60  TRP A C   1 
ATOM   483  O O   . TRP A 1 61  ? 10.104 4.773   -19.066 1.00 31.39  ?  60  TRP A O   1 
ATOM   484  C CB  . TRP A 1 61  ? 6.954  5.399   -18.229 1.00 37.28  ?  60  TRP A CB  1 
ATOM   485  C CG  . TRP A 1 61  ? 6.031  6.547   -17.984 1.00 41.38  ?  60  TRP A CG  1 
ATOM   486  C CD1 . TRP A 1 61  ? 4.681  6.608   -18.250 1.00 39.35  ?  60  TRP A CD1 1 
ATOM   487  C CD2 . TRP A 1 61  ? 6.401  7.834   -17.481 1.00 39.42  ?  60  TRP A CD2 1 
ATOM   488  N NE1 . TRP A 1 61  ? 4.198  7.860   -17.939 1.00 40.31  ?  60  TRP A NE1 1 
ATOM   489  C CE2 . TRP A 1 61  ? 5.229  8.624   -17.450 1.00 41.78  ?  60  TRP A CE2 1 
ATOM   490  C CE3 . TRP A 1 61  ? 7.604  8.390   -17.034 1.00 38.51  ?  60  TRP A CE3 1 
ATOM   491  C CZ2 . TRP A 1 61  ? 5.230  9.939   -16.985 1.00 38.58  ?  60  TRP A CZ2 1 
ATOM   492  C CZ3 . TRP A 1 61  ? 7.603  9.706   -16.587 1.00 42.88  ?  60  TRP A CZ3 1 
ATOM   493  C CH2 . TRP A 1 61  ? 6.423  10.463  -16.573 1.00 41.36  ?  60  TRP A CH2 1 
ATOM   494  N N   . ASP A 1 62  ? 8.629  3.629   -20.316 1.00 34.90  ?  61  ASP A N   1 
ATOM   495  C CA  . ASP A 1 62  ? 9.615  2.574   -20.538 1.00 32.33  ?  61  ASP A CA  1 
ATOM   496  C C   . ASP A 1 62  ? 10.802 3.090   -21.339 1.00 29.33  ?  61  ASP A C   1 
ATOM   497  O O   . ASP A 1 62  ? 11.957 2.809   -21.009 1.00 32.72  ?  61  ASP A O   1 
ATOM   498  C CB  . ASP A 1 62  ? 8.994  1.375   -21.242 1.00 33.84  ?  61  ASP A CB  1 
ATOM   499  C CG  . ASP A 1 62  ? 9.966  0.214   -21.327 1.00 35.26  ?  61  ASP A CG  1 
ATOM   500  O OD1 . ASP A 1 62  ? 10.513 -0.220  -20.283 1.00 45.18  ?  61  ASP A OD1 1 
ATOM   501  O OD2 . ASP A 1 62  ? 10.214 -0.233  -22.439 1.00 38.86  -1 61  ASP A OD2 1 
ATOM   502  N N   . GLN A 1 63  ? 10.537 3.852   -22.395 1.00 31.21  ?  62  GLN A N   1 
ATOM   503  C CA  . GLN A 1 63  ? 11.607 4.426   -23.199 1.00 30.95  ?  62  GLN A CA  1 
ATOM   504  C C   . GLN A 1 63  ? 12.477 5.409   -22.408 1.00 35.58  ?  62  GLN A C   1 
ATOM   505  O O   . GLN A 1 63  ? 13.700 5.456   -22.606 1.00 28.74  ?  62  GLN A O   1 
ATOM   506  C CB  . GLN A 1 63  ? 10.984 5.112   -24.410 1.00 32.04  ?  62  GLN A CB  1 
ATOM   507  C CG  . GLN A 1 63  ? 11.896 5.915   -25.243 1.00 31.27  ?  62  GLN A CG  1 
ATOM   508  C CD  . GLN A 1 63  ? 11.128 6.811   -26.193 1.00 40.71  ?  62  GLN A CD  1 
ATOM   509  O OE1 . GLN A 1 63  ? 10.855 6.440   -27.345 1.00 30.80  ?  62  GLN A OE1 1 
ATOM   510  N NE2 . GLN A 1 63  ? 10.751 7.999   -25.708 1.00 35.09  ?  62  GLN A NE2 1 
ATOM   511  N N   . GLU A 1 64  ? 11.872 6.253   -21.563 1.00 32.98  ?  63  GLU A N   1 
ATOM   512  C CA  . GLU A 1 64  ? 12.685 7.195   -20.789 1.00 31.83  ?  63  GLU A CA  1 
ATOM   513  C C   . GLU A 1 64  ? 13.551 6.443   -19.790 1.00 24.88  ?  63  GLU A C   1 
ATOM   514  O O   . GLU A 1 64  ? 14.719 6.780   -19.589 1.00 27.47  ?  63  GLU A O   1 
ATOM   515  C CB  . GLU A 1 64  ? 11.797 8.226   -20.082 1.00 27.25  ?  63  GLU A CB  1 
ATOM   516  C CG  . GLU A 1 64  ? 11.029 9.146   -21.075 1.00 32.14  ?  63  GLU A CG  1 
ATOM   517  C CD  . GLU A 1 64  ? 11.947 9.763   -22.127 1.00 30.23  ?  63  GLU A CD  1 
ATOM   518  O OE1 . GLU A 1 64  ? 12.549 10.820  -21.840 1.00 31.69  ?  63  GLU A OE1 1 
ATOM   519  O OE2 . GLU A 1 64  ? 12.089 9.201   -23.249 1.00 32.63  -1 63  GLU A OE2 1 
ATOM   520  N N   . THR A 1 65  ? 13.002 5.396   -19.195 1.00 24.71  ?  64  THR A N   1 
ATOM   521  C CA  . THR A 1 65  ? 13.759 4.575   -18.262 1.00 28.23  ?  64  THR A CA  1 
ATOM   522  C C   . THR A 1 65  ? 14.953 3.922   -18.943 1.00 33.02  ?  64  THR A C   1 
ATOM   523  O O   . THR A 1 65  ? 16.056 3.900   -18.382 1.00 29.22  ?  64  THR A O   1 
ATOM   524  C CB  . THR A 1 65  ? 12.825 3.542   -17.643 1.00 27.46  ?  64  THR A CB  1 
ATOM   525  O OG1 . THR A 1 65  ? 11.826 4.239   -16.895 1.00 37.40  ?  64  THR A OG1 1 
ATOM   526  C CG2 . THR A 1 65  ? 13.576 2.586   -16.702 1.00 31.88  ?  64  THR A CG2 1 
ATOM   527  N N   . ARG A 1 66  ? 14.766 3.431   -20.179 1.00 25.55  ?  65  ARG A N   1 
ATOM   528  C CA  . ARG A 1 66  ? 15.859 2.781   -20.891 1.00 25.15  ?  65  ARG A CA  1 
ATOM   529  C C   . ARG A 1 66  ? 16.956 3.773   -21.248 1.00 23.20  ?  65  ARG A C   1 
ATOM   530  O O   . ARG A 1 66  ? 18.141 3.452   -21.128 1.00 27.36  ?  65  ARG A O   1 
ATOM   531  C CB  . ARG A 1 66  ? 15.352 2.095   -22.172 1.00 24.05  ?  65  ARG A CB  1 
ATOM   532  C CG  . ARG A 1 66  ? 14.732 0.731   -21.964 1.00 28.17  ?  65  ARG A CG  1 
ATOM   533  C CD  . ARG A 1 66  ? 14.327 0.097   -23.287 1.00 34.75  ?  65  ARG A CD  1 
ATOM   534  N NE  . ARG A 1 66  ? 12.936 0.398   -23.558 1.00 35.69  ?  65  ARG A NE  1 
ATOM   535  C CZ  . ARG A 1 66  ? 12.499 1.005   -24.652 1.00 34.32  ?  65  ARG A CZ  1 
ATOM   536  N NH1 . ARG A 1 66  ? 13.348 1.365   -25.612 1.00 27.78  ?  65  ARG A NH1 1 
ATOM   537  N NH2 . ARG A 1 66  ? 11.194 1.231   -24.783 1.00 35.75  ?  65  ARG A NH2 1 
ATOM   538  N N   . ASN A 1 67  ? 16.592 4.967   -21.722 1.00 22.48  ?  66  ASN A N   1 
ATOM   539  C CA  . ASN A 1 67  ? 17.607 5.985   -21.962 1.00 26.15  ?  66  ASN A CA  1 
ATOM   540  C C   . ASN A 1 67  ? 18.306 6.422   -20.669 1.00 26.72  ?  66  ASN A C   1 
ATOM   541  O O   . ASN A 1 67  ? 19.504 6.714   -20.699 1.00 28.71  ?  66  ASN A O   1 
ATOM   542  C CB  . ASN A 1 67  ? 16.996 7.178   -22.694 1.00 25.57  ?  66  ASN A CB  1 
ATOM   543  C CG  . ASN A 1 67  ? 17.297 7.143   -24.214 1.00 26.35  ?  66  ASN A CG  1 
ATOM   544  O OD1 . ASN A 1 67  ? 18.363 6.683   -24.645 1.00 27.00  ?  66  ASN A OD1 1 
ATOM   545  N ND2 . ASN A 1 67  ? 16.346 7.610   -25.020 1.00 26.93  ?  66  ASN A ND2 1 
ATOM   546  N N   . MET A 1 68  ? 17.603 6.435   -19.524 1.00 27.51  ?  67  MET A N   1 
ATOM   547  C CA  . MET A 1 68  ? 18.263 6.764   -18.255 1.00 31.21  ?  67  MET A CA  1 
ATOM   548  C C   . MET A 1 68  ? 19.243 5.678   -17.833 1.00 27.99  ?  67  MET A C   1 
ATOM   549  O O   . MET A 1 68  ? 20.320 5.979   -17.299 1.00 27.55  ?  67  MET A O   1 
ATOM   550  C CB  . MET A 1 68  ? 17.252 6.918   -17.112 1.00 29.32  ?  67  MET A CB  1 
ATOM   551  C CG  . MET A 1 68  ? 16.705 8.296   -16.944 1.00 38.82  ?  67  MET A CG  1 
ATOM   552  S SD  . MET A 1 68  ? 17.937 9.571   -16.688 1.00 44.98  ?  67  MET A SD  1 
ATOM   553  C CE  . MET A 1 68  ? 18.970 8.781   -15.463 1.00 31.12  ?  67  MET A CE  1 
ATOM   554  N N   . LYS A 1 69  ? 18.824 4.412   -17.969 1.00 28.02  ?  68  LYS A N   1 
ATOM   555  C CA  . LYS A 1 69  ? 19.671 3.263   -17.630 1.00 29.07  ?  68  LYS A CA  1 
ATOM   556  C C   . LYS A 1 69  ? 20.943 3.270   -18.452 1.00 29.02  ?  68  LYS A C   1 
ATOM   557  O O   . LYS A 1 69  ? 22.028 2.958   -17.946 1.00 26.20  ?  68  LYS A O   1 
ATOM   558  C CB  . LYS A 1 69  ? 18.897 1.960   -17.872 1.00 30.21  ?  68  LYS A CB  1 
ATOM   559  C CG  . LYS A 1 69  ? 19.703 0.658   -17.762 1.00 32.12  ?  68  LYS A CG  1 
ATOM   560  C CD  . LYS A 1 69  ? 18.799 -0.568  -17.424 1.00 33.26  ?  68  LYS A CD  1 
ATOM   561  C CE  . LYS A 1 69  ? 17.819 -0.990  -18.578 1.00 36.20  ?  68  LYS A CE  1 
ATOM   562  N NZ  . LYS A 1 69  ? 18.528 -1.375  -19.824 1.00 28.72  ?  68  LYS A NZ  1 
ATOM   563  N N   . ALA A 1 70  ? 20.829 3.632   -19.732 1.00 25.42  ?  69  ALA A N   1 
ATOM   564  C CA  . ALA A 1 70  ? 22.006 3.675   -20.594 1.00 28.47  ?  69  ALA A CA  1 
ATOM   565  C C   . ALA A 1 70  ? 22.901 4.849   -20.230 1.00 25.70  ?  69  ALA A C   1 
ATOM   566  O O   . ALA A 1 70  ? 24.132 4.708   -20.167 1.00 27.60  ?  69  ALA A O   1 
ATOM   567  C CB  . ALA A 1 70  ? 21.591 3.761   -22.064 1.00 23.85  ?  69  ALA A CB  1 
ATOM   568  N N   . HIS A 1 71  ? 22.298 6.020   -20.005 1.00 26.78  ?  70  HIS A N   1 
ATOM   569  C CA  . HIS A 1 71  ? 23.060 7.177   -19.526 1.00 30.27  ?  70  HIS A CA  1 
ATOM   570  C C   . HIS A 1 71  ? 23.848 6.851   -18.250 1.00 27.01  ?  70  HIS A C   1 
ATOM   571  O O   . HIS A 1 71  ? 25.027 7.207   -18.125 1.00 27.15  ?  70  HIS A O   1 
ATOM   572  C CB  . HIS A 1 71  ? 22.111 8.350   -19.272 1.00 26.22  ?  70  HIS A CB  1 
ATOM   573  C CG  . HIS A 1 71  ? 22.783 9.498   -18.606 1.00 28.85  ?  70  HIS A CG  1 
ATOM   574  N ND1 . HIS A 1 71  ? 22.892 9.599   -17.237 1.00 38.09  ?  70  HIS A ND1 1 
ATOM   575  C CD2 . HIS A 1 71  ? 23.474 10.540  -19.121 1.00 38.73  ?  70  HIS A CD2 1 
ATOM   576  C CE1 . HIS A 1 71  ? 23.578 10.685  -16.935 1.00 38.33  ?  70  HIS A CE1 1 
ATOM   577  N NE2 . HIS A 1 71  ? 23.957 11.263  -18.059 1.00 40.91  ?  70  HIS A NE2 1 
ATOM   578  N N   . SER A 1 72  ? 23.215 6.161   -17.303 1.00 23.64  ?  71  SER A N   1 
ATOM   579  C CA  . SER A 1 72  ? 23.869 5.861   -16.026 1.00 28.15  ?  71  SER A CA  1 
ATOM   580  C C   . SER A 1 72  ? 25.064 4.938   -16.195 1.00 32.42  ?  71  SER A C   1 
ATOM   581  O O   . SER A 1 72  ? 26.049 5.045   -15.447 1.00 27.45  ?  71  SER A O   1 
ATOM   582  C CB  . SER A 1 72  ? 22.889 5.193   -15.067 1.00 25.81  ?  71  SER A CB  1 
ATOM   583  O OG  . SER A 1 72  ? 21.769 6.006   -14.848 1.00 33.53  ?  71  SER A OG  1 
ATOM   584  N N   . GLN A 1 73  ? 24.958 3.964   -17.106 1.00 27.40  ?  72  GLN A N   1 
ATOM   585  C CA  . GLN A 1 73  ? 26.079 3.065   -17.354 1.00 26.87  ?  72  GLN A CA  1 
ATOM   586  C C   . GLN A 1 73  ? 27.267 3.827   -17.923 1.00 27.35  ?  72  GLN A C   1 
ATOM   587  O O   . GLN A 1 73  ? 28.413 3.561   -17.564 1.00 27.37  ?  72  GLN A O   1 
ATOM   588  C CB  . GLN A 1 73  ? 25.657 1.948   -18.301 1.00 31.14  ?  72  GLN A CB  1 
ATOM   589  C CG  . GLN A 1 73  ? 26.676 0.840   -18.394 1.00 32.49  ?  72  GLN A CG  1 
ATOM   590  C CD  . GLN A 1 73  ? 26.925 0.175   -17.039 1.00 34.54  ?  72  GLN A CD  1 
ATOM   591  O OE1 . GLN A 1 73  ? 26.013 0.008   -16.220 1.00 32.07  ?  72  GLN A OE1 1 
ATOM   592  N NE2 . GLN A 1 73  ? 28.165 -0.208  -16.807 1.00 33.76  ?  72  GLN A NE2 1 
ATOM   593  N N   . THR A 1 74  ? 27.006 4.786   -18.817 1.00 23.43  ?  73  THR A N   1 
ATOM   594  C CA  . THR A 1 74  ? 28.064 5.639   -19.352 1.00 32.20  ?  73  THR A CA  1 
ATOM   595  C C   . THR A 1 74  ? 28.630 6.572   -18.287 1.00 29.20  ?  73  THR A C   1 
ATOM   596  O O   . THR A 1 74  ? 29.817 6.906   -18.316 1.00 24.38  ?  73  THR A O   1 
ATOM   597  C CB  . THR A 1 74  ? 27.519 6.466   -20.520 1.00 31.14  ?  73  THR A CB  1 
ATOM   598  O OG1 . THR A 1 74  ? 27.110 5.574   -21.552 1.00 40.25  ?  73  THR A OG1 1 
ATOM   599  C CG2 . THR A 1 74  ? 28.574 7.421   -21.034 1.00 32.23  ?  73  THR A CG2 1 
ATOM   600  N N   . ASP A 1 75  ? 27.790 7.044   -17.372 1.00 28.11  ?  74  ASP A N   1 
ATOM   601  C CA  . ASP A 1 75  ? 28.314 7.873   -16.299 1.00 29.70  ?  74  ASP A CA  1 
ATOM   602  C C   . ASP A 1 75  ? 29.198 7.037   -15.383 1.00 29.38  ?  74  ASP A C   1 
ATOM   603  O O   . ASP A 1 75  ? 30.256 7.502   -14.930 1.00 26.27  ?  74  ASP A O   1 
ATOM   604  C CB  . ASP A 1 75  ? 27.168 8.513   -15.533 1.00 26.29  ?  74  ASP A CB  1 
ATOM   605  C CG  . ASP A 1 75  ? 26.721 9.841   -16.144 1.00 36.62  ?  74  ASP A CG  1 
ATOM   606  O OD1 . ASP A 1 75  ? 27.133 10.169  -17.291 1.00 31.00  ?  74  ASP A OD1 1 
ATOM   607  O OD2 . ASP A 1 75  ? 25.956 10.563  -15.456 1.00 33.92  -1 74  ASP A OD2 1 
ATOM   608  N N   . ARG A 1 76  ? 28.781 5.797   -15.118 1.00 24.69  ?  75  ARG A N   1 
ATOM   609  C CA  . ARG A 1 76  ? 29.601 4.874   -14.333 1.00 29.05  ?  75  ARG A CA  1 
ATOM   610  C C   . ARG A 1 76  ? 30.980 4.701   -14.966 1.00 27.47  ?  75  ARG A C   1 
ATOM   611  O O   . ARG A 1 76  ? 32.013 4.910   -14.320 1.00 25.76  ?  75  ARG A O   1 
ATOM   612  C CB  . ARG A 1 76  ? 28.893 3.517   -14.179 1.00 32.01  ?  75  ARG A CB  1 
ATOM   613  C CG  . ARG A 1 76  ? 29.679 2.522   -13.304 1.00 31.38  ?  75  ARG A CG  1 
ATOM   614  C CD  . ARG A 1 76  ? 29.131 1.095   -13.338 1.00 34.95  ?  75  ARG A CD  1 
ATOM   615  N NE  . ARG A 1 76  ? 27.678 1.084   -13.231 1.00 47.48  ?  75  ARG A NE  1 
ATOM   616  C CZ  . ARG A 1 76  ? 27.001 0.810   -12.113 1.00 54.37  ?  75  ARG A CZ  1 
ATOM   617  N NH1 . ARG A 1 76  ? 27.654 0.513   -10.989 1.00 58.27  ?  75  ARG A NH1 1 
ATOM   618  N NH2 . ARG A 1 76  ? 25.670 0.828   -12.113 1.00 53.08  ?  75  ARG A NH2 1 
ATOM   619  N N   . ALA A 1 77  ? 31.017 4.377   -16.251 1.00 25.64  ?  76  ALA A N   1 
ATOM   620  C CA  . ALA A 1 77  ? 32.294 4.263   -16.941 1.00 24.58  ?  76  ALA A CA  1 
ATOM   621  C C   . ALA A 1 77  ? 33.060 5.575   -16.907 1.00 26.30  ?  76  ALA A C   1 
ATOM   622  O O   . ALA A 1 77  ? 34.291 5.583   -16.809 1.00 27.40  ?  76  ALA A O   1 
ATOM   623  C CB  . ALA A 1 77  ? 32.072 3.826   -18.385 1.00 29.06  ?  76  ALA A CB  1 
ATOM   624  N N   . ASN A 1 78  ? 32.343 6.694   -16.998 1.00 28.39  ?  77  ASN A N   1 
ATOM   625  C CA  . ASN A 1 78  ? 32.999 7.996   -17.087 1.00 28.83  ?  77  ASN A CA  1 
ATOM   626  C C   . ASN A 1 78  ? 33.644 8.375   -15.757 1.00 20.92  ?  77  ASN A C   1 
ATOM   627  O O   . ASN A 1 78  ? 34.690 9.019   -15.743 1.00 23.43  ?  77  ASN A O   1 
ATOM   628  C CB  . ASN A 1 78  ? 31.992 9.059   -17.548 1.00 24.69  ?  77  ASN A CB  1 
ATOM   629  C CG  . ASN A 1 78  ? 31.831 9.074   -19.068 1.00 26.32  ?  77  ASN A CG  1 
ATOM   630  O OD1 . ASN A 1 78  ? 32.589 8.431   -19.771 1.00 22.90  ?  77  ASN A OD1 1 
ATOM   631  N ND2 . ASN A 1 78  ? 30.871 9.842   -19.568 1.00 26.58  ?  77  ASN A ND2 1 
ATOM   632  N N   . LEU A 1 79  ? 33.051 7.965   -14.651 1.00 23.64  ?  78  LEU A N   1 
ATOM   633  C CA  . LEU A 1 79  ? 33.675 8.184   -13.351 1.00 28.00  ?  78  LEU A CA  1 
ATOM   634  C C   . LEU A 1 79  ? 35.001 7.443   -13.256 1.00 27.22  ?  78  LEU A C   1 
ATOM   635  O O   . LEU A 1 79  ? 35.987 7.984   -12.748 1.00 27.51  ?  78  LEU A O   1 
ATOM   636  C CB  . LEU A 1 79  ? 32.731 7.731   -12.240 1.00 24.11  ?  78  LEU A CB  1 
ATOM   637  C CG  . LEU A 1 79  ? 31.609 8.727   -11.910 1.00 29.48  ?  78  LEU A CG  1 
ATOM   638  C CD1 . LEU A 1 79  ? 30.451 7.990   -11.224 1.00 27.11  ?  78  LEU A CD1 1 
ATOM   639  C CD2 . LEU A 1 79  ? 32.085 9.883   -11.015 1.00 27.56  ?  78  LEU A CD2 1 
ATOM   640  N N   . GLY A 1 80  ? 35.058 6.216   -13.778 1.00 30.50  ?  79  GLY A N   1 
ATOM   641  C CA  . GLY A 1 80  ? 36.319 5.488   -13.791 1.00 31.66  ?  79  GLY A CA  1 
ATOM   642  C C   . GLY A 1 80  ? 37.362 6.150   -14.669 1.00 33.75  ?  79  GLY A C   1 
ATOM   643  O O   . GLY A 1 80  ? 38.517 6.328   -14.260 1.00 31.04  ?  79  GLY A O   1 
ATOM   644  N N   . THR A 1 81  ? 36.965 6.563   -15.869 1.00 26.94  ?  80  THR A N   1 
ATOM   645  C CA  . THR A 1 81  ? 37.907 7.182   -16.793 1.00 29.36  ?  80  THR A CA  1 
ATOM   646  C C   . THR A 1 81  ? 38.508 8.443   -16.192 1.00 26.70  ?  80  THR A C   1 
ATOM   647  O O   . THR A 1 81  ? 39.720 8.668   -16.267 1.00 28.00  ?  80  THR A O   1 
ATOM   648  C CB  . THR A 1 81  ? 37.208 7.510   -18.118 1.00 32.71  ?  80  THR A CB  1 
ATOM   649  O OG1 . THR A 1 81  ? 36.698 6.303   -18.703 1.00 34.30  ?  80  THR A OG1 1 
ATOM   650  C CG2 . THR A 1 81  ? 38.162 8.211   -19.086 1.00 30.99  ?  80  THR A CG2 1 
ATOM   651  N N   . LEU A 1 82  ? 37.671 9.294   -15.604 1.00 25.62  ?  81  LEU A N   1 
ATOM   652  C CA  . LEU A 1 82  ? 38.191 10.551  -15.073 1.00 27.53  ?  81  LEU A CA  1 
ATOM   653  C C   . LEU A 1 82  ? 39.098 10.305  -13.876 1.00 29.49  ?  81  LEU A C   1 
ATOM   654  O O   . LEU A 1 82  ? 40.118 10.985  -13.711 1.00 28.61  ?  81  LEU A O   1 
ATOM   655  C CB  . LEU A 1 82  ? 37.043 11.482  -14.698 1.00 25.59  ?  81  LEU A CB  1 
ATOM   656  C CG  . LEU A 1 82  ? 36.265 11.996  -15.921 1.00 28.79  ?  81  LEU A CG  1 
ATOM   657  C CD1 . LEU A 1 82  ? 35.087 12.840  -15.418 1.00 26.88  ?  81  LEU A CD1 1 
ATOM   658  C CD2 . LEU A 1 82  ? 37.129 12.750  -16.902 1.00 29.79  ?  81  LEU A CD2 1 
ATOM   659  N N   . ARG A 1 83  ? 38.723 9.360   -13.014 1.00 28.55  ?  82  ARG A N   1 
ATOM   660  C CA  . ARG A 1 83  ? 39.607 8.946   -11.933 1.00 32.44  ?  82  ARG A CA  1 
ATOM   661  C C   . ARG A 1 83  ? 41.003 8.680   -12.479 1.00 32.32  ?  82  ARG A C   1 
ATOM   662  O O   . ARG A 1 83  ? 41.995 9.208   -11.962 1.00 33.58  ?  82  ARG A O   1 
ATOM   663  C CB  . ARG A 1 83  ? 39.037 7.710   -11.235 1.00 33.98  ?  82  ARG A CB  1 
ATOM   664  C CG  . ARG A 1 83  ? 39.768 7.296   -9.947  1.00 41.48  ?  82  ARG A CG  1 
ATOM   665  C CD  . ARG A 1 83  ? 39.097 6.060   -9.326  1.00 39.30  ?  82  ARG A CD  1 
ATOM   666  N NE  . ARG A 1 83  ? 39.101 4.939   -10.265 1.00 46.82  ?  82  ARG A NE  1 
ATOM   667  C CZ  . ARG A 1 83  ? 38.072 4.116   -10.464 1.00 51.82  ?  82  ARG A CZ  1 
ATOM   668  N NH1 . ARG A 1 83  ? 36.943 4.267   -9.772  1.00 49.74  ?  82  ARG A NH1 1 
ATOM   669  N NH2 . ARG A 1 83  ? 38.173 3.139   -11.359 1.00 50.51  ?  82  ARG A NH2 1 
ATOM   670  N N   . GLY A 1 84  ? 41.090 7.928   -13.576 1.00 29.71  ?  83  GLY A N   1 
ATOM   671  C CA  . GLY A 1 84  ? 42.388 7.670   -14.178 1.00 31.52  ?  83  GLY A CA  1 
ATOM   672  C C   . GLY A 1 84  ? 43.031 8.915   -14.761 1.00 33.62  ?  83  GLY A C   1 
ATOM   673  O O   . GLY A 1 84  ? 44.233 9.146   -14.600 1.00 35.80  ?  83  GLY A O   1 
ATOM   674  N N   . TYR A 1 85  ? 42.246 9.726   -15.463 1.00 30.20  ?  84  TYR A N   1 
ATOM   675  C CA  . TYR A 1 85  ? 42.776 10.965  -16.024 1.00 35.32  ?  84  TYR A CA  1 
ATOM   676  C C   . TYR A 1 85  ? 43.465 11.833  -14.959 1.00 34.90  ?  84  TYR A C   1 
ATOM   677  O O   . TYR A 1 85  ? 44.496 12.458  -15.229 1.00 29.93  ?  84  TYR A O   1 
ATOM   678  C CB  . TYR A 1 85  ? 41.640 11.751  -16.686 1.00 30.90  ?  84  TYR A CB  1 
ATOM   679  C CG  . TYR A 1 85  ? 41.158 11.261  -18.043 1.00 32.98  ?  84  TYR A CG  1 
ATOM   680  C CD1 . TYR A 1 85  ? 41.777 10.206  -18.697 1.00 37.71  ?  84  TYR A CD1 1 
ATOM   681  C CD2 . TYR A 1 85  ? 40.096 11.888  -18.688 1.00 31.55  ?  84  TYR A CD2 1 
ATOM   682  C CE1 . TYR A 1 85  ? 41.346 9.780   -19.951 1.00 36.44  ?  84  TYR A CE1 1 
ATOM   683  C CE2 . TYR A 1 85  ? 39.671 11.474  -19.954 1.00 32.35  ?  84  TYR A CE2 1 
ATOM   684  C CZ  . TYR A 1 85  ? 40.294 10.413  -20.563 1.00 35.15  ?  84  TYR A CZ  1 
ATOM   685  O OH  . TYR A 1 85  ? 39.866 9.972   -21.790 1.00 38.11  ?  84  TYR A OH  1 
ATOM   686  N N   . TYR A 1 86  ? 42.882 11.930  -13.766 1.00 31.85  ?  85  TYR A N   1 
ATOM   687  C CA  . TYR A 1 86  ? 43.344 12.860  -12.747 1.00 34.24  ?  85  TYR A CA  1 
ATOM   688  C C   . TYR A 1 86  ? 44.111 12.171  -11.629 1.00 34.18  ?  85  TYR A C   1 
ATOM   689  O O   . TYR A 1 86  ? 44.370 12.795  -10.590 1.00 32.48  ?  85  TYR A O   1 
ATOM   690  C CB  . TYR A 1 86  ? 42.152 13.608  -12.161 1.00 36.56  ?  85  TYR A CB  1 
ATOM   691  C CG  . TYR A 1 86  ? 41.425 14.541  -13.117 1.00 36.09  ?  85  TYR A CG  1 
ATOM   692  C CD1 . TYR A 1 86  ? 42.029 15.695  -13.600 1.00 36.12  ?  85  TYR A CD1 1 
ATOM   693  C CD2 . TYR A 1 86  ? 40.130 14.260  -13.532 1.00 32.25  ?  85  TYR A CD2 1 
ATOM   694  C CE1 . TYR A 1 86  ? 41.351 16.550  -14.458 1.00 38.06  ?  85  TYR A CE1 1 
ATOM   695  C CE2 . TYR A 1 86  ? 39.454 15.105  -14.389 1.00 32.04  ?  85  TYR A CE2 1 
ATOM   696  C CZ  . TYR A 1 86  ? 40.061 16.245  -14.844 1.00 35.36  ?  85  TYR A CZ  1 
ATOM   697  O OH  . TYR A 1 86  ? 39.354 17.078  -15.688 1.00 33.07  ?  85  TYR A OH  1 
ATOM   698  N N   . ASN A 1 87  ? 44.428 10.884  -11.802 1.00 35.57  ?  86  ASN A N   1 
ATOM   699  C CA  . ASN A 1 87  ? 45.241 10.109  -10.852 1.00 35.35  ?  86  ASN A CA  1 
ATOM   700  C C   . ASN A 1 87  ? 44.661 10.150  -9.441  1.00 37.25  ?  86  ASN A C   1 
ATOM   701  O O   . ASN A 1 87  ? 45.376 10.254  -8.439  1.00 35.95  ?  86  ASN A O   1 
ATOM   702  C CB  . ASN A 1 87  ? 46.695 10.583  -10.888 1.00 40.74  ?  86  ASN A CB  1 
ATOM   703  C CG  . ASN A 1 87  ? 47.386 10.205  -12.193 1.00 43.20  ?  86  ASN A CG  1 
ATOM   704  O OD1 . ASN A 1 87  ? 47.057 9.196   -12.818 1.00 47.37  ?  86  ASN A OD1 1 
ATOM   705  N ND2 . ASN A 1 87  ? 48.350 11.014  -12.603 1.00 55.36  ?  86  ASN A ND2 1 
ATOM   706  N N   . GLN A 1 88  ? 43.340 10.022  -9.381  1.00 37.36  ?  87  GLN A N   1 
ATOM   707  C CA  . GLN A 1 88  ? 42.561 9.914   -8.166  1.00 33.48  ?  87  GLN A CA  1 
ATOM   708  C C   . GLN A 1 88  ? 42.435 8.447   -7.769  1.00 36.63  ?  87  GLN A C   1 
ATOM   709  O O   . GLN A 1 88  ? 42.988 7.557   -8.413  1.00 35.03  ?  87  GLN A O   1 
ATOM   710  C CB  . GLN A 1 88  ? 41.221 10.602  -8.390  1.00 30.38  ?  87  GLN A CB  1 
ATOM   711  C CG  . GLN A 1 88  ? 41.400 12.121  -8.404  1.00 32.86  ?  87  GLN A CG  1 
ATOM   712  C CD  . GLN A 1 88  ? 40.272 12.867  -9.090  1.00 36.94  ?  87  GLN A CD  1 
ATOM   713  O OE1 . GLN A 1 88  ? 39.486 12.290  -9.842  1.00 32.71  ?  87  GLN A OE1 1 
ATOM   714  N NE2 . GLN A 1 88  ? 40.186 14.162  -8.822  1.00 33.56  ?  87  GLN A NE2 1 
ATOM   715  N N   . SER A 1 89  ? 41.734 8.179   -6.676  1.00 33.36  ?  88  SER A N   1 
ATOM   716  C CA  . SER A 1 89  ? 41.666 6.815   -6.186  1.00 43.37  ?  88  SER A CA  1 
ATOM   717  C C   . SER A 1 89  ? 40.230 6.320   -6.122  1.00 39.29  ?  88  SER A C   1 
ATOM   718  O O   . SER A 1 89  ? 39.268 7.097   -6.107  1.00 37.38  ?  88  SER A O   1 
ATOM   719  C CB  . SER A 1 89  ? 42.301 6.681   -4.796  1.00 37.06  ?  88  SER A CB  1 
ATOM   720  O OG  . SER A 1 89  ? 41.291 6.682   -3.809  1.00 46.61  ?  88  SER A OG  1 
ATOM   721  N N   . GLU A 1 90  ? 40.098 4.998   -6.073  1.00 41.69  ?  89  GLU A N   1 
ATOM   722  C CA  . GLU A 1 90  ? 38.785 4.395   -5.900  1.00 39.72  ?  89  GLU A CA  1 
ATOM   723  C C   . GLU A 1 90  ? 38.216 4.629   -4.517  1.00 40.63  ?  89  GLU A C   1 
ATOM   724  O O   . GLU A 1 90  ? 37.061 4.273   -4.278  1.00 46.14  ?  89  GLU A O   1 
ATOM   725  C CB  . GLU A 1 90  ? 38.845 2.893   -6.155  1.00 58.42  ?  89  GLU A CB  1 
ATOM   726  C CG  . GLU A 1 90  ? 39.648 2.495   -7.378  1.00 57.36  ?  89  GLU A CG  1 
ATOM   727  C CD  . GLU A 1 90  ? 39.627 0.993   -7.597  1.00 79.69  ?  89  GLU A CD  1 
ATOM   728  O OE1 . GLU A 1 90  ? 38.757 0.313   -6.993  1.00 81.34  ?  89  GLU A OE1 1 
ATOM   729  O OE2 . GLU A 1 90  ? 40.481 0.499   -8.369  1.00 87.46  -1 89  GLU A OE2 1 
ATOM   730  N N   . ASP A 1 91  ? 38.998 5.192   -3.599  1.00 38.69  ?  90  ASP A N   1 
ATOM   731  C CA  . ASP A 1 91  ? 38.492 5.513   -2.272  1.00 41.76  ?  90  ASP A CA  1 
ATOM   732  C C   . ASP A 1 91  ? 37.792 6.863   -2.229  1.00 42.02  ?  90  ASP A C   1 
ATOM   733  O O   . ASP A 1 91  ? 37.081 7.139   -1.267  1.00 38.33  ?  90  ASP A O   1 
ATOM   734  C CB  . ASP A 1 91  ? 39.635 5.514   -1.248  1.00 49.47  ?  90  ASP A CB  1 
ATOM   735  C CG  . ASP A 1 91  ? 40.250 4.137   -1.057  1.00 56.87  ?  90  ASP A CG  1 
ATOM   736  O OD1 . ASP A 1 91  ? 39.501 3.140   -1.234  1.00 54.38  -1 90  ASP A OD1 1 
ATOM   737  O OD2 . ASP A 1 91  ? 41.470 4.062   -0.744  1.00 55.51  ?  90  ASP A OD2 1 
ATOM   738  N N   . GLY A 1 92  ? 38.005 7.720   -3.224  1.00 43.67  ?  91  GLY A N   1 
ATOM   739  C CA  . GLY A 1 92  ? 37.364 9.018   -3.244  1.00 36.62  ?  91  GLY A CA  1 
ATOM   740  C C   . GLY A 1 92  ? 35.969 8.990   -3.852  1.00 33.88  ?  91  GLY A C   1 
ATOM   741  O O   . GLY A 1 92  ? 35.657 8.200   -4.735  1.00 39.78  ?  91  GLY A O   1 
ATOM   742  N N   . SER A 1 93  ? 35.123 9.867   -3.340  1.00 35.60  ?  92  SER A N   1 
ATOM   743  C CA  . SER A 1 93  ? 33.810 10.094  -3.909  1.00 38.18  ?  92  SER A CA  1 
ATOM   744  C C   . SER A 1 93  ? 33.896 11.237  -4.922  1.00 35.40  ?  92  SER A C   1 
ATOM   745  O O   . SER A 1 93  ? 34.463 12.297  -4.631  1.00 30.11  ?  92  SER A O   1 
ATOM   746  C CB  . SER A 1 93  ? 32.811 10.415  -2.807  1.00 34.89  ?  92  SER A CB  1 
ATOM   747  O OG  . SER A 1 93  ? 31.627 10.924  -3.391  1.00 38.35  ?  92  SER A OG  1 
ATOM   748  N N   . HIS A 1 94  ? 33.359 11.017  -6.117  1.00 33.04  ?  93  HIS A N   1 
ATOM   749  C CA  . HIS A 1 94  ? 33.394 12.048  -7.151  1.00 31.10  ?  93  HIS A CA  1 
ATOM   750  C C   . HIS A 1 94  ? 32.029 12.220  -7.806  1.00 29.77  ?  93  HIS A C   1 
ATOM   751  O O   . HIS A 1 94  ? 31.141 11.379  -7.683  1.00 24.97  ?  93  HIS A O   1 
ATOM   752  C CB  . HIS A 1 94  ? 34.470 11.733  -8.204  1.00 28.40  ?  93  HIS A CB  1 
ATOM   753  C CG  . HIS A 1 94  ? 35.848 11.692  -7.631  1.00 31.65  ?  93  HIS A CG  1 
ATOM   754  N ND1 . HIS A 1 94  ? 36.659 12.806  -7.563  1.00 33.08  ?  93  HIS A ND1 1 
ATOM   755  C CD2 . HIS A 1 94  ? 36.523 10.696  -7.008  1.00 33.46  ?  93  HIS A CD2 1 
ATOM   756  C CE1 . HIS A 1 94  ? 37.793 12.486  -6.963  1.00 31.34  ?  93  HIS A CE1 1 
ATOM   757  N NE2 . HIS A 1 94  ? 37.731 11.214  -6.609  1.00 29.04  ?  93  HIS A NE2 1 
ATOM   758  N N   . THR A 1 95  ? 31.889 13.336  -8.515  1.00 26.98  ?  94  THR A N   1 
ATOM   759  C CA  . THR A 1 95  ? 30.598 13.793  -9.000  1.00 28.93  ?  94  THR A CA  1 
ATOM   760  C C   . THR A 1 95  ? 30.712 14.206  -10.461 1.00 23.69  ?  94  THR A C   1 
ATOM   761  O O   . THR A 1 95  ? 31.571 15.009  -10.822 1.00 26.13  ?  94  THR A O   1 
ATOM   762  C CB  . THR A 1 95  ? 30.075 14.978  -8.177  1.00 27.11  ?  94  THR A CB  1 
ATOM   763  O OG1 . THR A 1 95  ? 29.983 14.626  -6.788  1.00 27.91  ?  94  THR A OG1 1 
ATOM   764  C CG2 . THR A 1 95  ? 28.699 15.386  -8.700  1.00 26.00  ?  94  THR A CG2 1 
ATOM   765  N N   . ILE A 1 96  ? 29.837 13.662  -11.293 1.00 28.85  ?  95  ILE A N   1 
ATOM   766  C CA  . ILE A 1 96  ? 29.665 14.122  -12.661 1.00 23.43  ?  95  ILE A CA  1 
ATOM   767  C C   . ILE A 1 96  ? 28.286 14.750  -12.754 1.00 25.15  ?  95  ILE A C   1 
ATOM   768  O O   . ILE A 1 96  ? 27.298 14.146  -12.328 1.00 24.67  ?  95  ILE A O   1 
ATOM   769  C CB  . ILE A 1 96  ? 29.791 12.974  -13.671 1.00 24.97  ?  95  ILE A CB  1 
ATOM   770  C CG1 . ILE A 1 96  ? 31.236 12.488  -13.814 1.00 24.12  ?  95  ILE A CG1 1 
ATOM   771  C CG2 . ILE A 1 96  ? 29.293 13.436  -15.044 1.00 24.73  ?  95  ILE A CG2 1 
ATOM   772  C CD1 . ILE A 1 96  ? 31.332 11.177  -14.648 1.00 27.56  ?  95  ILE A CD1 1 
ATOM   773  N N   . GLN A 1 97  ? 28.220 15.938  -13.334 1.00 26.30  ?  96  GLN A N   1 
ATOM   774  C CA  . GLN A 1 97  ? 26.964 16.638  -13.526 1.00 26.20  ?  96  GLN A CA  1 
ATOM   775  C C   . GLN A 1 97  ? 26.842 16.989  -14.993 1.00 25.68  ?  96  GLN A C   1 
ATOM   776  O O   . GLN A 1 97  ? 27.822 17.386  -15.634 1.00 25.56  ?  96  GLN A O   1 
ATOM   777  C CB  . GLN A 1 97  ? 26.858 17.931  -12.709 1.00 23.78  ?  96  GLN A CB  1 
ATOM   778  C CG  . GLN A 1 97  ? 26.648 17.724  -11.210 1.00 27.74  ?  96  GLN A CG  1 
ATOM   779  C CD  . GLN A 1 97  ? 27.057 18.977  -10.426 1.00 29.47  ?  96  GLN A CD  1 
ATOM   780  O OE1 . GLN A 1 97  ? 28.209 19.123  -10.020 1.00 22.86  ?  96  GLN A OE1 1 
ATOM   781  N NE2 . GLN A 1 97  ? 26.119 19.892  -10.259 1.00 25.54  ?  96  GLN A NE2 1 
ATOM   782  N N   . ILE A 1 98  ? 25.627 16.875  -15.504 1.00 25.10  ?  97  ILE A N   1 
ATOM   783  C CA  . ILE A 1 98  ? 25.329 17.205  -16.889 1.00 22.33  ?  97  ILE A CA  1 
ATOM   784  C C   . ILE A 1 98  ? 24.053 18.027  -16.931 1.00 19.98  ?  97  ILE A C   1 
ATOM   785  O O   . ILE A 1 98  ? 23.075 17.702  -16.243 1.00 27.05  ?  97  ILE A O   1 
ATOM   786  C CB  . ILE A 1 98  ? 25.179 15.933  -17.754 1.00 24.36  ?  97  ILE A CB  1 
ATOM   787  C CG1 . ILE A 1 98  ? 26.531 15.206  -17.885 1.00 29.11  ?  97  ILE A CG1 1 
ATOM   788  C CG2 . ILE A 1 98  ? 24.684 16.307  -19.137 1.00 27.20  ?  97  ILE A CG2 1 
ATOM   789  C CD1 . ILE A 1 98  ? 26.439 13.815  -18.464 1.00 24.19  ?  97  ILE A CD1 1 
ATOM   790  N N   . MET A 1 99  ? 24.062 19.099  -17.726 1.00 24.97  ?  98  MET A N   1 
ATOM   791  C CA  . MET A 1 99  ? 22.858 19.849  -18.076 1.00 30.44  ?  98  MET A CA  1 
ATOM   792  C C   . MET A 1 99  ? 22.799 19.981  -19.593 1.00 21.71  ?  98  MET A C   1 
ATOM   793  O O   . MET A 1 99  ? 23.817 20.280  -20.230 1.00 27.00  ?  98  MET A O   1 
ATOM   794  C CB  . MET A 1 99  ? 22.836 21.228  -17.392 1.00 30.46  ?  98  MET A CB  1 
ATOM   795  C CG  . MET A 1 99  ? 21.470 21.903  -17.401 1.00 33.56  ?  98  MET A CG  1 
ATOM   796  S SD  . MET A 1 99  ? 21.098 22.776  -18.956 1.00 44.78  ?  98  MET A SD  1 
ATOM   797  C CE  . MET A 1 99  ? 22.627 23.516  -19.431 1.00 26.77  ?  98  MET A CE  1 
ATOM   798  N N   . TYR A 1 100 ? 21.642 19.680  -20.184 1.00 25.63  ?  99  TYR A N   1 
ATOM   799  C CA  . TYR A 1 100 ? 21.409 20.006  -21.584 1.00 26.84  ?  99  TYR A CA  1 
ATOM   800  C C   . TYR A 1 100 ? 19.953 20.405  -21.735 1.00 26.58  ?  99  TYR A C   1 
ATOM   801  O O   . TYR A 1 100 ? 19.127 20.093  -20.882 1.00 27.90  ?  99  TYR A O   1 
ATOM   802  C CB  . TYR A 1 100 ? 21.761 18.863  -22.554 1.00 25.71  ?  99  TYR A CB  1 
ATOM   803  C CG  . TYR A 1 100 ? 20.985 17.567  -22.395 1.00 27.55  ?  99  TYR A CG  1 
ATOM   804  C CD1 . TYR A 1 100 ? 19.648 17.479  -22.747 1.00 26.38  ?  99  TYR A CD1 1 
ATOM   805  C CD2 . TYR A 1 100 ? 21.625 16.401  -21.956 1.00 24.61  ?  99  TYR A CD2 1 
ATOM   806  C CE1 . TYR A 1 100 ? 18.956 16.296  -22.618 1.00 24.75  ?  99  TYR A CE1 1 
ATOM   807  C CE2 . TYR A 1 100 ? 20.946 15.212  -21.838 1.00 23.89  ?  99  TYR A CE2 1 
ATOM   808  C CZ  . TYR A 1 100 ? 19.615 15.154  -22.176 1.00 27.46  ?  99  TYR A CZ  1 
ATOM   809  O OH  . TYR A 1 100 ? 18.937 13.961  -22.029 1.00 27.87  ?  99  TYR A OH  1 
ATOM   810  N N   . GLY A 1 101 ? 19.652 21.082  -22.839 1.00 27.62  ?  100 GLY A N   1 
ATOM   811  C CA  . GLY A 1 101 ? 18.277 21.429  -23.155 1.00 31.04  ?  100 GLY A CA  1 
ATOM   812  C C   . GLY A 1 101 ? 18.216 22.479  -24.248 1.00 28.12  ?  100 GLY A C   1 
ATOM   813  O O   . GLY A 1 101 ? 19.238 22.924  -24.786 1.00 28.03  ?  100 GLY A O   1 
ATOM   814  N N   . CYS A 1 102 ? 16.986 22.912  -24.526 1.00 31.55  ?  101 CYS A N   1 
ATOM   815  C CA  . CYS A 1 102 ? 16.737 23.820  -25.632 1.00 31.87  ?  101 CYS A CA  1 
ATOM   816  C C   . CYS A 1 102 ? 15.779 24.928  -25.219 1.00 30.97  ?  101 CYS A C   1 
ATOM   817  O O   . CYS A 1 102 ? 14.950 24.749  -24.333 1.00 30.78  ?  101 CYS A O   1 
ATOM   818  C CB  . CYS A 1 102 ? 16.137 23.075  -26.840 1.00 30.65  ?  101 CYS A CB  1 
ATOM   819  S SG  . CYS A 1 102 ? 14.620 22.189  -26.476 1.00 32.20  ?  101 CYS A SG  1 
ATOM   820  N N   . ASP A 1 103 ? 15.891 26.074  -25.903 1.00 33.14  ?  102 ASP A N   1 
ATOM   821  C CA  . ASP A 1 103 ? 14.946 27.180  -25.785 1.00 39.56  ?  102 ASP A CA  1 
ATOM   822  C C   . ASP A 1 103 ? 14.181 27.355  -27.091 1.00 37.40  ?  102 ASP A C   1 
ATOM   823  O O   . ASP A 1 103 ? 14.769 27.243  -28.167 1.00 35.30  ?  102 ASP A O   1 
ATOM   824  C CB  . ASP A 1 103 ? 15.636 28.517  -25.511 1.00 36.94  ?  102 ASP A CB  1 
ATOM   825  C CG  . ASP A 1 103 ? 16.428 28.518  -24.259 1.00 40.05  ?  102 ASP A CG  1 
ATOM   826  O OD1 . ASP A 1 103 ? 16.043 27.777  -23.341 1.00 29.29  ?  102 ASP A OD1 1 
ATOM   827  O OD2 . ASP A 1 103 ? 17.451 29.223  -24.199 1.00 42.54  -1 102 ASP A OD2 1 
ATOM   828  N N   . VAL A 1 104 ? 12.890 27.686  -26.987 1.00 37.63  ?  103 VAL A N   1 
ATOM   829  C CA  . VAL A 1 104 ? 12.066 28.035  -28.142 1.00 44.60  ?  103 VAL A CA  1 
ATOM   830  C C   . VAL A 1 104 ? 11.389 29.391  -27.928 1.00 47.02  ?  103 VAL A C   1 
ATOM   831  O O   . VAL A 1 104 ? 10.930 29.702  -26.818 1.00 42.99  ?  103 VAL A O   1 
ATOM   832  C CB  . VAL A 1 104 ? 10.980 26.973  -28.416 1.00 42.35  ?  103 VAL A CB  1 
ATOM   833  C CG1 . VAL A 1 104 ? 11.594 25.635  -28.691 1.00 40.03  ?  103 VAL A CG1 1 
ATOM   834  C CG2 . VAL A 1 104 ? 9.998  26.920  -27.241 1.00 41.79  ?  103 VAL A CG2 1 
ATOM   835  N N   . GLY A 1 105 ? 11.266 30.166  -29.013 1.00 56.32  ?  104 GLY A N   1 
ATOM   836  C CA  . GLY A 1 105 ? 10.472 31.381  -29.034 1.00 52.38  ?  104 GLY A CA  1 
ATOM   837  C C   . GLY A 1 105 ? 9.001  31.161  -28.716 1.00 60.78  ?  104 GLY A C   1 
ATOM   838  O O   . GLY A 1 105 ? 8.551  30.038  -28.455 1.00 57.07  ?  104 GLY A O   1 
ATOM   839  N N   . PRO A 1 106 ? 8.210  32.240  -28.738 1.00 66.77  ?  105 PRO A N   1 
ATOM   840  C CA  . PRO A 1 106 ? 6.773  32.096  -28.420 1.00 67.69  ?  105 PRO A CA  1 
ATOM   841  C C   . PRO A 1 106 ? 5.994  31.326  -29.483 1.00 67.79  ?  105 PRO A C   1 
ATOM   842  O O   . PRO A 1 106 ? 4.942  30.749  -29.166 1.00 61.84  ?  105 PRO A O   1 
ATOM   843  C CB  . PRO A 1 106 ? 6.287  33.548  -28.300 1.00 67.03  ?  105 PRO A CB  1 
ATOM   844  C CG  . PRO A 1 106 ? 7.228  34.336  -29.196 1.00 67.24  ?  105 PRO A CG  1 
ATOM   845  C CD  . PRO A 1 106 ? 8.558  33.586  -29.230 1.00 61.83  ?  105 PRO A CD  1 
ATOM   846  N N   . ASP A 1 107 ? 6.488  31.295  -30.727 1.00 63.09  ?  106 ASP A N   1 
ATOM   847  C CA  . ASP A 1 107 ? 5.895  30.505  -31.801 1.00 69.15  ?  106 ASP A CA  1 
ATOM   848  C C   . ASP A 1 107 ? 6.201  29.014  -31.687 1.00 68.43  ?  106 ASP A C   1 
ATOM   849  O O   . ASP A 1 107 ? 5.659  28.223  -32.468 1.00 70.78  ?  106 ASP A O   1 
ATOM   850  C CB  . ASP A 1 107 ? 6.393  31.021  -33.161 1.00 62.36  ?  106 ASP A CB  1 
ATOM   851  C CG  . ASP A 1 107 ? 7.913  31.215  -33.202 1.00 61.44  ?  106 ASP A CG  1 
ATOM   852  O OD1 . ASP A 1 107 ? 8.514  31.446  -32.130 1.00 67.72  ?  106 ASP A OD1 1 
ATOM   853  O OD2 . ASP A 1 107 ? 8.510  31.148  -34.299 1.00 62.79  -1 106 ASP A OD2 1 
ATOM   854  N N   . GLY A 1 108 ? 7.045  28.611  -30.739 1.00 66.73  ?  107 GLY A N   1 
ATOM   855  C CA  . GLY A 1 108 ? 7.467  27.234  -30.634 1.00 52.21  ?  107 GLY A CA  1 
ATOM   856  C C   . GLY A 1 108 ? 8.705  26.879  -31.423 1.00 44.72  ?  107 GLY A C   1 
ATOM   857  O O   . GLY A 1 108 ? 9.026  25.693  -31.525 1.00 52.76  ?  107 GLY A O   1 
ATOM   858  N N   . ARG A 1 109 ? 9.432  27.851  -31.953 1.00 48.21  ?  108 ARG A N   1 
ATOM   859  C CA  . ARG A 1 109 ? 10.545 27.575  -32.844 1.00 47.83  ?  108 ARG A CA  1 
ATOM   860  C C   . ARG A 1 109 ? 11.880 27.686  -32.120 1.00 44.87  ?  108 ARG A C   1 
ATOM   861  O O   . ARG A 1 109 ? 12.053 28.535  -31.245 1.00 45.07  ?  108 ARG A O   1 
ATOM   862  C CB  . ARG A 1 109 ? 10.487 28.525  -34.028 1.00 54.50  ?  108 ARG A CB  1 
ATOM   863  C CG  . ARG A 1 109 ? 9.224  28.295  -34.808 1.00 60.88  ?  108 ARG A CG  1 
ATOM   864  C CD  . ARG A 1 109 ? 9.619  28.020  -36.217 1.00 58.36  ?  108 ARG A CD  1 
ATOM   865  N NE  . ARG A 1 109 ? 10.252 29.274  -36.687 1.00 71.36  ?  108 ARG A NE  1 
ATOM   866  C CZ  . ARG A 1 109 ? 10.400 29.568  -37.886 1.00 69.84  ?  108 ARG A CZ  1 
ATOM   867  N NH1 . ARG A 1 109 ? 10.587 28.569  -38.693 1.00 68.90  ?  108 ARG A NH1 1 
ATOM   868  N NH2 . ARG A 1 109 ? 11.269 30.667  -38.074 1.00 66.65  ?  108 ARG A NH2 1 
ATOM   869  N N   . PHE A 1 110 ? 12.817 26.820  -32.504 1.00 39.74  ?  109 PHE A N   1 
ATOM   870  C CA  . PHE A 1 110 ? 14.117 26.728  -31.853 1.00 42.92  ?  109 PHE A CA  1 
ATOM   871  C C   . PHE A 1 110 ? 14.857 28.056  -31.849 1.00 43.55  ?  109 PHE A C   1 
ATOM   872  O O   . PHE A 1 110 ? 15.063 28.675  -32.896 1.00 37.41  ?  109 PHE A O   1 
ATOM   873  C CB  . PHE A 1 110 ? 14.954 25.673  -32.572 1.00 38.26  ?  109 PHE A CB  1 
ATOM   874  C CG  . PHE A 1 110 ? 16.427 25.671  -32.203 1.00 36.03  ?  109 PHE A CG  1 
ATOM   875  C CD1 . PHE A 1 110 ? 16.874 24.954  -31.097 1.00 38.17  ?  109 PHE A CD1 1 
ATOM   876  C CD2 . PHE A 1 110 ? 17.368 26.330  -32.993 1.00 40.95  ?  109 PHE A CD2 1 
ATOM   877  C CE1 . PHE A 1 110 ? 18.224 24.915  -30.767 1.00 36.84  ?  109 PHE A CE1 1 
ATOM   878  C CE2 . PHE A 1 110 ? 18.714 26.310  -32.664 1.00 40.91  ?  109 PHE A CE2 1 
ATOM   879  C CZ  . PHE A 1 110 ? 19.146 25.588  -31.547 1.00 34.84  ?  109 PHE A CZ  1 
ATOM   880  N N   . LEU A 1 111 ? 15.289 28.473  -30.658 1.00 42.15  ?  110 LEU A N   1 
ATOM   881  C CA  . LEU A 1 111 ? 16.174 29.618  -30.504 1.00 36.23  ?  110 LEU A CA  1 
ATOM   882  C C   . LEU A 1 111 ? 17.616 29.200  -30.250 1.00 40.11  ?  110 LEU A C   1 
ATOM   883  O O   . LEU A 1 111 ? 18.535 29.696  -30.913 1.00 32.15  ?  110 LEU A O   1 
ATOM   884  C CB  . LEU A 1 111 ? 15.696 30.509  -29.355 1.00 44.58  ?  110 LEU A CB  1 
ATOM   885  C CG  . LEU A 1 111 ? 14.238 30.959  -29.341 1.00 53.07  ?  110 LEU A CG  1 
ATOM   886  C CD1 . LEU A 1 111 ? 13.978 31.809  -28.083 1.00 51.11  ?  110 LEU A CD1 1 
ATOM   887  C CD2 . LEU A 1 111 ? 13.901 31.742  -30.581 1.00 49.42  ?  110 LEU A CD2 1 
ATOM   888  N N   . ARG A 1 112 ? 17.832 28.287  -29.303 1.00 38.17  ?  111 ARG A N   1 
ATOM   889  C CA  . ARG A 1 112 ? 19.186 27.924  -28.912 1.00 39.41  ?  111 ARG A CA  1 
ATOM   890  C C   . ARG A 1 112 ? 19.172 26.592  -28.177 1.00 29.49  ?  111 ARG A C   1 
ATOM   891  O O   . ARG A 1 112 ? 18.144 26.163  -27.642 1.00 33.25  ?  111 ARG A O   1 
ATOM   892  C CB  . ARG A 1 112 ? 19.804 29.005  -28.020 1.00 45.97  ?  111 ARG A CB  1 
ATOM   893  C CG  . ARG A 1 112 ? 18.900 29.408  -26.856 1.00 46.98  ?  111 ARG A CG  1 
ATOM   894  C CD  . ARG A 1 112 ? 19.365 30.722  -26.208 1.00 56.26  ?  111 ARG A CD  1 
ATOM   895  N NE  . ARG A 1 112 ? 18.240 31.589  -25.844 1.00 55.29  ?  111 ARG A NE  1 
ATOM   896  C CZ  . ARG A 1 112 ? 17.838 32.639  -26.551 1.00 52.77  ?  111 ARG A CZ  1 
ATOM   897  N NH1 . ARG A 1 112 ? 18.472 32.980  -27.663 1.00 57.09  ?  111 ARG A NH1 1 
ATOM   898  N NH2 . ARG A 1 112 ? 16.808 33.362  -26.135 1.00 65.77  ?  111 ARG A NH2 1 
ATOM   899  N N   . GLY A 1 113 ? 20.340 25.954  -28.146 1.00 35.17  ?  112 GLY A N   1 
ATOM   900  C CA  . GLY A 1 113 ? 20.500 24.697  -27.447 1.00 37.30  ?  112 GLY A CA  1 
ATOM   901  C C   . GLY A 1 113 ? 21.725 24.702  -26.578 1.00 32.90  ?  112 GLY A C   1 
ATOM   902  O O   . GLY A 1 113 ? 22.654 25.507  -26.746 1.00 32.05  ?  112 GLY A O   1 
ATOM   903  N N   . TYR A 1 114 ? 21.815 23.808  -25.595 1.00 30.07  ?  113 TYR A N   1 
ATOM   904  C CA  . TYR A 1 114 ? 22.940 23.783  -24.683 1.00 32.66  ?  113 TYR A CA  1 
ATOM   905  C C   . TYR A 1 114 ? 23.213 22.346  -24.288 1.00 25.63  ?  113 TYR A C   1 
ATOM   906  O O   . TYR A 1 114 ? 22.336 21.573  -24.266 1.00 28.49  ?  113 TYR A O   1 
ATOM   907  C CB  . TYR A 1 114 ? 22.645 24.511  -23.386 1.00 35.07  ?  113 TYR A CB  1 
ATOM   908  C CG  . TYR A 1 114 ? 22.377 25.974  -23.528 1.00 41.71  ?  113 TYR A CG  1 
ATOM   909  C CD1 . TYR A 1 114 ? 23.359 26.926  -23.480 1.00 48.95  ?  113 TYR A CD1 1 
ATOM   910  C CD2 . TYR A 1 114 ? 21.099 26.385  -23.740 1.00 44.95  ?  113 TYR A CD2 1 
ATOM   911  C CE1 . TYR A 1 114 ? 23.058 28.266  -23.627 1.00 58.66  ?  113 TYR A CE1 1 
ATOM   912  C CE2 . TYR A 1 114 ? 20.770 27.710  -23.941 1.00 54.85  ?  113 TYR A CE2 1 
ATOM   913  C CZ  . TYR A 1 114 ? 21.761 28.660  -23.863 1.00 56.12  ?  113 TYR A CZ  1 
ATOM   914  O OH  . TYR A 1 114 ? 21.509 29.968  -24.010 1.00 58.42  ?  113 TYR A OH  1 
ATOM   915  N N   . ARG A 1 115 ? 24.454 22.076  -24.001 1.00 35.79  ?  114 ARG A N   1 
ATOM   916  C CA  . ARG A 1 115 ? 24.955 20.868  -23.348 1.00 32.39  ?  114 ARG A CA  1 
ATOM   917  C C   . ARG A 1 115 ? 26.277 21.201  -22.656 1.00 30.25  ?  114 ARG A C   1 
ATOM   918  O O   . ARG A 1 115 ? 27.201 21.724  -23.288 1.00 29.11  ?  114 ARG A O   1 
ATOM   919  C CB  . ARG A 1 115 ? 25.139 19.733  -24.358 1.00 36.82  ?  114 ARG A CB  1 
ATOM   920  C CG  . ARG A 1 115 ? 26.159 18.664  -23.936 1.00 38.24  ?  114 ARG A CG  1 
ATOM   921  C CD  . ARG A 1 115 ? 25.498 17.416  -23.418 1.00 34.43  ?  114 ARG A CD  1 
ATOM   922  N NE  . ARG A 1 115 ? 26.391 16.539  -22.646 1.00 31.72  ?  114 ARG A NE  1 
ATOM   923  C CZ  . ARG A 1 115 ? 26.328 15.206  -22.669 1.00 35.17  ?  114 ARG A CZ  1 
ATOM   924  N NH1 . ARG A 1 115 ? 25.433 14.590  -23.439 1.00 29.86  ?  114 ARG A NH1 1 
ATOM   925  N NH2 . ARG A 1 115 ? 27.165 14.485  -21.927 1.00 27.80  ?  114 ARG A NH2 1 
ATOM   926  N N   . GLN A 1 116 ? 26.365 20.879  -21.365 1.00 31.19  ?  115 GLN A N   1 
ATOM   927  C CA  . GLN A 1 116 ? 27.544 21.195  -20.572 1.00 28.47  ?  115 GLN A CA  1 
ATOM   928  C C   . GLN A 1 116 ? 27.742 20.123  -19.515 1.00 27.68  ?  115 GLN A C   1 
ATOM   929  O O   . GLN A 1 116 ? 26.776 19.683  -18.892 1.00 25.02  ?  115 GLN A O   1 
ATOM   930  C CB  . GLN A 1 116 ? 27.411 22.546  -19.853 1.00 34.72  ?  115 GLN A CB  1 
ATOM   931  C CG  . GLN A 1 116 ? 27.876 23.724  -20.646 1.00 42.97  ?  115 GLN A CG  1 
ATOM   932  C CD  . GLN A 1 116 ? 27.098 24.992  -20.308 1.00 50.49  ?  115 GLN A CD  1 
ATOM   933  O OE1 . GLN A 1 116 ? 26.765 25.785  -21.197 1.00 54.24  ?  115 GLN A OE1 1 
ATOM   934  N NE2 . GLN A 1 116 ? 26.803 25.184  -19.025 1.00 41.13  ?  115 GLN A NE2 1 
ATOM   935  N N   . ASP A 1 117 ? 29.000 19.752  -19.288 1.00 27.09  ?  116 ASP A N   1 
ATOM   936  C CA  . ASP A 1 117 ? 29.372 18.650  -18.413 1.00 25.45  ?  116 ASP A CA  1 
ATOM   937  C C   . ASP A 1 117 ? 30.358 19.157  -17.370 1.00 23.75  ?  116 ASP A C   1 
ATOM   938  O O   . ASP A 1 117 ? 31.266 19.920  -17.702 1.00 24.81  ?  116 ASP A O   1 
ATOM   939  C CB  . ASP A 1 117 ? 30.054 17.520  -19.188 1.00 23.00  ?  116 ASP A CB  1 
ATOM   940  C CG  . ASP A 1 117 ? 29.104 16.785  -20.133 1.00 26.76  ?  116 ASP A CG  1 
ATOM   941  O OD1 . ASP A 1 117 ? 28.192 17.454  -20.672 1.00 26.17  ?  116 ASP A OD1 1 
ATOM   942  O OD2 . ASP A 1 117 ? 29.270 15.548  -20.314 1.00 27.52  -1 116 ASP A OD2 1 
ATOM   943  N N   . ALA A 1 118 ? 30.223 18.671  -16.130 1.00 30.77  ?  117 ALA A N   1 
ATOM   944  C CA  . ALA A 1 118 ? 31.105 19.105  -15.057 1.00 27.86  ?  117 ALA A CA  1 
ATOM   945  C C   . ALA A 1 118 ? 31.573 17.924  -14.223 1.00 29.87  ?  117 ALA A C   1 
ATOM   946  O O   . ALA A 1 118 ? 30.846 16.944  -14.037 1.00 29.34  ?  117 ALA A O   1 
ATOM   947  C CB  . ALA A 1 118 ? 30.402 20.127  -14.163 1.00 27.93  ?  117 ALA A CB  1 
ATOM   948  N N   . TYR A 1 119 ? 32.788 18.059  -13.683 1.00 28.07  ?  118 TYR A N   1 
ATOM   949  C CA  . TYR A 1 119 ? 33.403 17.062  -12.818 1.00 27.80  ?  118 TYR A CA  1 
ATOM   950  C C   . TYR A 1 119 ? 33.778 17.726  -11.506 1.00 28.02  ?  118 TYR A C   1 
ATOM   951  O O   . TYR A 1 119 ? 34.510 18.723  -11.510 1.00 26.47  ?  118 TYR A O   1 
ATOM   952  C CB  . TYR A 1 119 ? 34.651 16.466  -13.452 1.00 26.24  ?  118 TYR A CB  1 
ATOM   953  C CG  . TYR A 1 119 ? 35.274 15.329  -12.643 1.00 28.11  ?  118 TYR A CG  1 
ATOM   954  C CD1 . TYR A 1 119 ? 34.522 14.222  -12.292 1.00 24.78  ?  118 TYR A CD1 1 
ATOM   955  C CD2 . TYR A 1 119 ? 36.618 15.368  -12.248 1.00 30.99  ?  118 TYR A CD2 1 
ATOM   956  C CE1 . TYR A 1 119 ? 35.073 13.165  -11.588 1.00 30.06  ?  118 TYR A CE1 1 
ATOM   957  C CE2 . TYR A 1 119 ? 37.193 14.293  -11.507 1.00 31.76  ?  118 TYR A CE2 1 
ATOM   958  C CZ  . TYR A 1 119 ? 36.404 13.193  -11.213 1.00 29.69  ?  118 TYR A CZ  1 
ATOM   959  O OH  . TYR A 1 119 ? 36.887 12.109  -10.524 1.00 32.96  ?  118 TYR A OH  1 
ATOM   960  N N   . ASP A 1 120 ? 33.260 17.173  -10.404 1.00 27.46  ?  119 ASP A N   1 
ATOM   961  C CA  . ASP A 1 120 ? 33.464 17.693  -9.045  1.00 30.94  ?  119 ASP A CA  1 
ATOM   962  C C   . ASP A 1 120 ? 33.145 19.187  -8.948  1.00 31.77  ?  119 ASP A C   1 
ATOM   963  O O   . ASP A 1 120 ? 33.887 19.966  -8.347  1.00 27.40  ?  119 ASP A O   1 
ATOM   964  C CB  . ASP A 1 120 ? 34.889 17.412  -8.567  1.00 25.07  ?  119 ASP A CB  1 
ATOM   965  C CG  . ASP A 1 120 ? 35.103 15.948  -8.198  1.00 28.68  ?  119 ASP A CG  1 
ATOM   966  O OD1 . ASP A 1 120 ? 34.132 15.268  -7.813  1.00 28.95  ?  119 ASP A OD1 1 
ATOM   967  O OD2 . ASP A 1 120 ? 36.246 15.476  -8.307  1.00 34.71  -1 119 ASP A OD2 1 
ATOM   968  N N   . GLY A 1 121 ? 32.040 19.589  -9.559  1.00 27.79  ?  120 GLY A N   1 
ATOM   969  C CA  . GLY A 1 121 ? 31.550 20.941  -9.419  1.00 32.68  ?  120 GLY A CA  1 
ATOM   970  C C   . GLY A 1 121 ? 32.206 21.961  -10.320 1.00 33.57  ?  120 GLY A C   1 
ATOM   971  O O   . GLY A 1 121 ? 31.946 23.160  -10.161 1.00 34.59  ?  120 GLY A O   1 
ATOM   972  N N   . LYS A 1 122 ? 33.042 21.538  -11.263 1.00 29.91  ?  121 LYS A N   1 
ATOM   973  C CA  . LYS A 1 122 ? 33.706 22.471  -12.159 1.00 31.45  ?  121 LYS A CA  1 
ATOM   974  C C   . LYS A 1 122 ? 33.526 22.045  -13.615 1.00 32.04  ?  121 LYS A C   1 
ATOM   975  O O   . LYS A 1 122 ? 33.493 20.852  -13.943 1.00 31.57  ?  121 LYS A O   1 
ATOM   976  C CB  . LYS A 1 122 ? 35.218 22.594  -11.829 1.00 37.88  ?  121 LYS A CB  1 
ATOM   977  C CG  . LYS A 1 122 ? 35.521 23.374  -10.543 1.00 49.34  ?  121 LYS A CG  1 
ATOM   978  C CD  . LYS A 1 122 ? 37.006 23.706  -10.403 1.00 56.87  ?  121 LYS A CD  1 
ATOM   979  C CE  . LYS A 1 122 ? 37.275 25.229  -10.390 1.00 66.55  ?  121 LYS A CE  1 
ATOM   980  N NZ  . LYS A 1 122 ? 36.184 26.121  -9.857  1.00 67.63  ?  121 LYS A NZ  1 
ATOM   981  N N   . ASP A 1 123 ? 33.424 23.041  -14.489 1.00 29.63  ?  122 ASP A N   1 
ATOM   982  C CA  . ASP A 1 123 ? 33.356 22.798  -15.923 1.00 28.61  ?  122 ASP A CA  1 
ATOM   983  C C   . ASP A 1 123 ? 34.340 21.715  -16.351 1.00 33.51  ?  122 ASP A C   1 
ATOM   984  O O   . ASP A 1 123 ? 35.525 21.768  -16.009 1.00 31.33  ?  122 ASP A O   1 
ATOM   985  C CB  . ASP A 1 123 ? 33.697 24.071  -16.691 1.00 32.28  ?  122 ASP A CB  1 
ATOM   986  C CG  . ASP A 1 123 ? 32.607 25.130  -16.632 1.00 32.50  ?  122 ASP A CG  1 
ATOM   987  O OD1 . ASP A 1 123 ? 31.514 24.925  -16.059 1.00 32.54  ?  122 ASP A OD1 1 
ATOM   988  O OD2 . ASP A 1 123 ? 32.884 26.200  -17.186 1.00 42.88  -1 122 ASP A OD2 1 
ATOM   989  N N   . TYR A 1 124 ? 33.862 20.766  -17.156 1.00 28.57  ?  123 TYR A N   1 
ATOM   990  C CA  . TYR A 1 124 ? 34.735 19.789  -17.804 1.00 29.37  ?  123 TYR A CA  1 
ATOM   991  C C   . TYR A 1 124 ? 34.741 19.963  -19.322 1.00 28.45  ?  123 TYR A C   1 
ATOM   992  O O   . TYR A 1 124 ? 35.762 20.321  -19.926 1.00 25.13  ?  123 TYR A O   1 
ATOM   993  C CB  . TYR A 1 124 ? 34.305 18.364  -17.401 1.00 25.18  ?  123 TYR A CB  1 
ATOM   994  C CG  . TYR A 1 124 ? 35.206 17.282  -17.980 1.00 30.89  ?  123 TYR A CG  1 
ATOM   995  C CD1 . TYR A 1 124 ? 36.484 17.082  -17.475 1.00 31.21  ?  123 TYR A CD1 1 
ATOM   996  C CD2 . TYR A 1 124 ? 34.782 16.479  -19.028 1.00 27.36  ?  123 TYR A CD2 1 
ATOM   997  C CE1 . TYR A 1 124 ? 37.315 16.127  -17.993 1.00 29.76  ?  123 TYR A CE1 1 
ATOM   998  C CE2 . TYR A 1 124 ? 35.602 15.500  -19.543 1.00 29.39  ?  123 TYR A CE2 1 
ATOM   999  C CZ  . TYR A 1 124 ? 36.873 15.336  -19.026 1.00 30.67  ?  123 TYR A CZ  1 
ATOM   1000 O OH  . TYR A 1 124 ? 37.720 14.391  -19.542 1.00 31.26  ?  123 TYR A OH  1 
ATOM   1001 N N   . ILE A 1 125 ? 33.604 19.767  -19.975 1.00 28.26  ?  124 ILE A N   1 
ATOM   1002 C CA  . ILE A 1 125 ? 33.509 20.037  -21.401 1.00 28.00  ?  124 ILE A CA  1 
ATOM   1003 C C   . ILE A 1 125 ? 32.134 20.624  -21.671 1.00 29.39  ?  124 ILE A C   1 
ATOM   1004 O O   . ILE A 1 125 ? 31.162 20.314  -20.974 1.00 26.41  ?  124 ILE A O   1 
ATOM   1005 C CB  . ILE A 1 125 ? 33.771 18.747  -22.218 1.00 29.87  ?  124 ILE A CB  1 
ATOM   1006 C CG1 . ILE A 1 125 ? 34.022 19.074  -23.692 1.00 27.51  ?  124 ILE A CG1 1 
ATOM   1007 C CG2 . ILE A 1 125 ? 32.606 17.797  -22.048 1.00 28.30  ?  124 ILE A CG2 1 
ATOM   1008 C CD1 . ILE A 1 125 ? 34.530 17.902  -24.489 1.00 27.52  ?  124 ILE A CD1 1 
ATOM   1009 N N   . ALA A 1 126 ? 32.057 21.481  -22.692 1.00 29.35  ?  125 ALA A N   1 
ATOM   1010 C CA  . ALA A 1 126 ? 30.801 22.136  -23.022 1.00 30.89  ?  125 ALA A CA  1 
ATOM   1011 C C   . ALA A 1 126 ? 30.603 22.221  -24.531 1.00 25.28  ?  125 ALA A C   1 
ATOM   1012 O O   . ALA A 1 126 ? 31.544 22.430  -25.294 1.00 27.67  ?  125 ALA A O   1 
ATOM   1013 C CB  . ALA A 1 126 ? 30.725 23.548  -22.399 1.00 33.60  ?  125 ALA A CB  1 
ATOM   1014 N N   . LEU A 1 127 ? 29.367 22.052  -24.958 1.00 34.39  ?  126 LEU A N   1 
ATOM   1015 C CA  . LEU A 1 127 ? 29.030 22.318  -26.350 1.00 33.35  ?  126 LEU A CA  1 
ATOM   1016 C C   . LEU A 1 127 ? 28.924 23.821  -26.535 1.00 35.28  ?  126 LEU A C   1 
ATOM   1017 O O   . LEU A 1 127 ? 28.252 24.494  -25.753 1.00 31.96  ?  126 LEU A O   1 
ATOM   1018 C CB  . LEU A 1 127 ? 27.713 21.660  -26.721 1.00 28.12  ?  126 LEU A CB  1 
ATOM   1019 C CG  . LEU A 1 127 ? 27.212 21.755  -28.157 1.00 34.76  ?  126 LEU A CG  1 
ATOM   1020 C CD1 . LEU A 1 127 ? 28.129 21.027  -29.085 1.00 33.35  ?  126 LEU A CD1 1 
ATOM   1021 C CD2 . LEU A 1 127 ? 25.805 21.158  -28.146 1.00 31.13  ?  126 LEU A CD2 1 
ATOM   1022 N N   . ASN A 1 128 ? 29.574 24.340  -27.574 1.00 35.51  ?  127 ASN A N   1 
ATOM   1023 C CA  . ASN A 1 128 ? 29.555 25.769  -27.837 1.00 35.15  ?  127 ASN A CA  1 
ATOM   1024 C C   . ASN A 1 128 ? 28.217 26.194  -28.434 1.00 38.26  ?  127 ASN A C   1 
ATOM   1025 O O   . ASN A 1 128 ? 27.415 25.373  -28.905 1.00 33.17  ?  127 ASN A O   1 
ATOM   1026 C CB  . ASN A 1 128 ? 30.694 26.162  -28.779 1.00 33.41  ?  127 ASN A CB  1 
ATOM   1027 C CG  . ASN A 1 128 ? 32.059 26.028  -28.133 1.00 35.65  ?  127 ASN A CG  1 
ATOM   1028 O OD1 . ASN A 1 128 ? 32.204 26.220  -26.930 1.00 35.54  ?  127 ASN A OD1 1 
ATOM   1029 N ND2 . ASN A 1 128 ? 33.061 25.666  -28.925 1.00 34.93  ?  127 ASN A ND2 1 
ATOM   1030 N N   . GLU A 1 129 ? 27.996 27.513  -28.428 1.00 37.70  ?  128 GLU A N   1 
ATOM   1031 C CA  . GLU A 1 129 ? 26.722 28.069  -28.875 1.00 39.37  ?  128 GLU A CA  1 
ATOM   1032 C C   . GLU A 1 129 ? 26.347 27.600  -30.275 1.00 29.57  ?  128 GLU A C   1 
ATOM   1033 O O   . GLU A 1 129 ? 25.165 27.422  -30.573 1.00 33.17  ?  128 GLU A O   1 
ATOM   1034 C CB  . GLU A 1 129 ? 26.782 29.600  -28.839 1.00 38.65  ?  128 GLU A CB  1 
ATOM   1035 C CG  . GLU A 1 129 ? 25.477 30.288  -29.271 1.00 52.22  ?  128 GLU A CG  1 
ATOM   1036 C CD  . GLU A 1 129 ? 24.298 30.080  -28.294 1.00 65.79  ?  128 GLU A CD  1 
ATOM   1037 O OE1 . GLU A 1 129 ? 24.379 29.225  -27.370 1.00 63.39  ?  128 GLU A OE1 1 
ATOM   1038 O OE2 . GLU A 1 129 ? 23.282 30.799  -28.450 1.00 66.97  -1 128 GLU A OE2 1 
ATOM   1039 N N   . ASP A 1 130 ? 27.330 27.419  -31.154 1.00 34.58  ?  129 ASP A N   1 
ATOM   1040 C CA  . ASP A 1 130 ? 27.032 27.020  -32.525 1.00 40.91  ?  129 ASP A CA  1 
ATOM   1041 C C   . ASP A 1 130 ? 26.613 25.562  -32.648 1.00 39.13  ?  129 ASP A C   1 
ATOM   1042 O O   . ASP A 1 130 ? 26.233 25.144  -33.747 1.00 40.35  ?  129 ASP A O   1 
ATOM   1043 C CB  . ASP A 1 130 ? 28.240 27.263  -33.438 1.00 40.64  ?  129 ASP A CB  1 
ATOM   1044 C CG  . ASP A 1 130 ? 29.461 26.452  -33.030 1.00 45.18  ?  129 ASP A CG  1 
ATOM   1045 O OD1 . ASP A 1 130 ? 29.329 25.521  -32.201 1.00 44.94  ?  129 ASP A OD1 1 
ATOM   1046 O OD2 . ASP A 1 130 ? 30.560 26.751  -33.547 1.00 45.04  -1 129 ASP A OD2 1 
ATOM   1047 N N   . LEU A 1 131 ? 26.680 24.784  -31.566 1.00 37.55  ?  130 LEU A N   1 
ATOM   1048 C CA  . LEU A 1 131 ? 26.260 23.385  -31.566 1.00 33.28  ?  130 LEU A CA  1 
ATOM   1049 C C   . LEU A 1 131 ? 27.054 22.555  -32.565 1.00 32.47  ?  130 LEU A C   1 
ATOM   1050 O O   . LEU A 1 131 ? 26.576 21.538  -33.065 1.00 34.56  ?  130 LEU A O   1 
ATOM   1051 C CB  . LEU A 1 131 ? 24.764 23.267  -31.842 1.00 34.42  ?  130 LEU A CB  1 
ATOM   1052 C CG  . LEU A 1 131 ? 23.939 24.259  -31.039 1.00 35.91  ?  130 LEU A CG  1 
ATOM   1053 C CD1 . LEU A 1 131 ? 22.482 23.942  -31.284 1.00 35.29  ?  130 LEU A CD1 1 
ATOM   1054 C CD2 . LEU A 1 131 ? 24.215 24.209  -29.547 1.00 36.54  ?  130 LEU A CD2 1 
ATOM   1055 N N   . ARG A 1 132 ? 28.286 22.974  -32.814 1.00 30.37  ?  131 ARG A N   1 
ATOM   1056 C CA  . ARG A 1 132 ? 29.157 22.375  -33.801 1.00 37.10  ?  131 ARG A CA  1 
ATOM   1057 C C   . ARG A 1 132 ? 30.561 22.121  -33.274 1.00 37.86  ?  131 ARG A C   1 
ATOM   1058 O O   . ARG A 1 132 ? 31.352 21.485  -33.974 1.00 37.76  ?  131 ARG A O   1 
ATOM   1059 C CB  . ARG A 1 132 ? 29.256 23.283  -35.043 1.00 42.15  ?  131 ARG A CB  1 
ATOM   1060 C CG  . ARG A 1 132 ? 28.199 23.012  -36.097 1.00 47.28  ?  131 ARG A CG  1 
ATOM   1061 C CD  . ARG A 1 132 ? 27.951 24.202  -37.070 1.00 43.19  ?  131 ARG A CD  1 
ATOM   1062 N NE  . ARG A 1 132 ? 26.512 24.275  -37.316 1.00 46.36  ?  131 ARG A NE  1 
ATOM   1063 C CZ  . ARG A 1 132 ? 25.846 23.454  -38.123 1.00 49.41  ?  131 ARG A CZ  1 
ATOM   1064 N NH1 . ARG A 1 132 ? 26.496 22.516  -38.803 1.00 58.87  ?  131 ARG A NH1 1 
ATOM   1065 N NH2 . ARG A 1 132 ? 24.527 23.566  -38.252 1.00 52.21  ?  131 ARG A NH2 1 
ATOM   1066 N N   . SER A 1 133 ? 31.006 22.539  -32.094 1.00 36.74  ?  132 SER A N   1 
ATOM   1067 C CA  . SER A 1 133 ? 32.384 22.532  -31.609 1.00 34.42  ?  132 SER A CA  1 
ATOM   1068 C C   . SER A 1 133 ? 32.299 22.557  -30.094 1.00 33.68  ?  132 SER A C   1 
ATOM   1069 O O   . SER A 1 133 ? 31.317 22.966  -29.528 1.00 31.46  ?  132 SER A O   1 
ATOM   1070 C CB  . SER A 1 133 ? 33.191 23.674  -32.120 1.00 37.33  ?  132 SER A CB  1 
ATOM   1071 O OG  . SER A 1 133 ? 32.660 24.889  -31.699 1.00 51.37  ?  132 SER A OG  1 
ATOM   1072 N N   . TRP A 1 134 ? 33.381 22.183  -29.488 1.00 35.74  ?  133 TRP A N   1 
ATOM   1073 C CA  . TRP A 1 134 ? 33.468 21.960  -28.051 1.00 35.11  ?  133 TRP A CA  1 
ATOM   1074 C C   . TRP A 1 134 ? 34.543 22.837  -27.426 1.00 35.51  ?  133 TRP A C   1 
ATOM   1075 O O   . TRP A 1 134 ? 35.572 23.114  -28.048 1.00 37.23  ?  133 TRP A O   1 
ATOM   1076 C CB  . TRP A 1 134 ? 33.795 20.488  -27.714 1.00 33.46  ?  133 TRP A CB  1 
ATOM   1077 C CG  . TRP A 1 134 ? 32.823 19.501  -28.271 1.00 31.41  ?  133 TRP A CG  1 
ATOM   1078 C CD1 . TRP A 1 134 ? 32.932 18.829  -29.455 1.00 30.58  ?  133 TRP A CD1 1 
ATOM   1079 C CD2 . TRP A 1 134 ? 31.602 19.063  -27.669 1.00 29.18  ?  133 TRP A CD2 1 
ATOM   1080 N NE1 . TRP A 1 134 ? 31.849 18.007  -29.630 1.00 32.66  ?  133 TRP A NE1 1 
ATOM   1081 C CE2 . TRP A 1 134 ? 31.014 18.127  -28.549 1.00 27.39  ?  133 TRP A CE2 1 
ATOM   1082 C CE3 . TRP A 1 134 ? 30.957 19.359  -26.476 1.00 28.77  ?  133 TRP A CE3 1 
ATOM   1083 C CZ2 . TRP A 1 134 ? 29.800 17.497  -28.274 1.00 26.13  ?  133 TRP A CZ2 1 
ATOM   1084 C CZ3 . TRP A 1 134 ? 29.748 18.745  -26.204 1.00 31.77  ?  133 TRP A CZ3 1 
ATOM   1085 C CH2 . TRP A 1 134 ? 29.176 17.822  -27.109 1.00 33.53  ?  133 TRP A CH2 1 
ATOM   1086 N N   . THR A 1 135 ? 34.302 23.225  -26.165 1.00 35.67  ?  134 THR A N   1 
ATOM   1087 C CA  . THR A 1 135 ? 35.273 23.883  -25.292 1.00 33.14  ?  134 THR A CA  1 
ATOM   1088 C C   . THR A 1 135 ? 35.658 22.928  -24.174 1.00 31.35  ?  134 THR A C   1 
ATOM   1089 O O   . THR A 1 135 ? 34.804 22.537  -23.364 1.00 32.25  ?  134 THR A O   1 
ATOM   1090 C CB  . THR A 1 135 ? 34.696 25.164  -24.670 1.00 38.88  ?  134 THR A CB  1 
ATOM   1091 O OG1 . THR A 1 135 ? 34.289 26.066  -25.698 1.00 37.36  ?  134 THR A OG1 1 
ATOM   1092 C CG2 . THR A 1 135 ? 35.714 25.859  -23.765 1.00 36.38  ?  134 THR A CG2 1 
ATOM   1093 N N   . ALA A 1 136 ? 36.935 22.572  -24.115 1.00 37.69  ?  135 ALA A N   1 
ATOM   1094 C CA  . ALA A 1 136 ? 37.456 21.675  -23.088 1.00 36.12  ?  135 ALA A CA  1 
ATOM   1095 C C   . ALA A 1 136 ? 38.112 22.503  -21.987 1.00 35.99  ?  135 ALA A C   1 
ATOM   1096 O O   . ALA A 1 136 ? 38.921 23.388  -22.276 1.00 37.45  ?  135 ALA A O   1 
ATOM   1097 C CB  . ALA A 1 136 ? 38.457 20.690  -23.697 1.00 35.87  ?  135 ALA A CB  1 
ATOM   1098 N N   . ALA A 1 137 ? 37.764 22.215  -20.727 1.00 36.33  ?  136 ALA A N   1 
ATOM   1099 C CA  . ALA A 1 137 ? 38.178 23.089  -19.636 1.00 41.11  ?  136 ALA A CA  1 
ATOM   1100 C C   . ALA A 1 137 ? 39.630 22.879  -19.210 1.00 41.58  ?  136 ALA A C   1 
ATOM   1101 O O   . ALA A 1 137 ? 40.196 23.768  -18.570 1.00 37.22  ?  136 ALA A O   1 
ATOM   1102 C CB  . ALA A 1 137 ? 37.244 22.908  -18.432 1.00 33.61  ?  136 ALA A CB  1 
ATOM   1103 N N   . ASP A 1 138 ? 40.245 21.751  -19.550 1.00 38.53  ?  137 ASP A N   1 
ATOM   1104 C CA  . ASP A 1 138 ? 41.597 21.418  -19.098 1.00 38.79  ?  137 ASP A CA  1 
ATOM   1105 C C   . ASP A 1 138 ? 42.115 20.287  -19.983 1.00 39.77  ?  137 ASP A C   1 
ATOM   1106 O O   . ASP A 1 138 ? 41.461 19.898  -20.957 1.00 41.29  ?  137 ASP A O   1 
ATOM   1107 C CB  . ASP A 1 138 ? 41.616 21.047  -17.612 1.00 36.94  ?  137 ASP A CB  1 
ATOM   1108 C CG  . ASP A 1 138 ? 40.897 19.726  -17.318 1.00 38.41  ?  137 ASP A CG  1 
ATOM   1109 O OD1 . ASP A 1 138 ? 40.716 18.911  -18.247 1.00 42.48  ?  137 ASP A OD1 1 
ATOM   1110 O OD2 . ASP A 1 138 ? 40.505 19.499  -16.151 1.00 43.07  -1 137 ASP A OD2 1 
ATOM   1111 N N   . MET A 1 139 ? 43.281 19.735  -19.634 1.00 42.32  ?  138 MET A N   1 
ATOM   1112 C CA  . MET A 1 139 ? 43.978 18.834  -20.557 1.00 47.54  ?  138 MET A CA  1 
ATOM   1113 C C   . MET A 1 139 ? 43.286 17.475  -20.655 1.00 37.87  ?  138 MET A C   1 
ATOM   1114 O O   . MET A 1 139 ? 43.234 16.877  -21.732 1.00 41.65  ?  138 MET A O   1 
ATOM   1115 C CB  . MET A 1 139 ? 45.434 18.655  -20.119 1.00 47.63  ?  138 MET A CB  1 
ATOM   1116 C CG  . MET A 1 139 ? 46.349 19.846  -20.427 1.00 48.02  ?  138 MET A CG  1 
ATOM   1117 S SD  . MET A 1 139 ? 46.330 20.395  -22.151 1.00 67.34  ?  138 MET A SD  1 
ATOM   1118 C CE  . MET A 1 139 ? 47.076 18.988  -22.987 1.00 53.16  ?  138 MET A CE  1 
ATOM   1119 N N   . ALA A 1 140 ? 42.763 16.971  -19.542 1.00 39.66  ?  139 ALA A N   1 
ATOM   1120 C CA  . ALA A 1 140 ? 41.977 15.740  -19.576 1.00 39.96  ?  139 ALA A CA  1 
ATOM   1121 C C   . ALA A 1 140 ? 40.776 15.892  -20.501 1.00 38.17  ?  139 ALA A C   1 
ATOM   1122 O O   . ALA A 1 140 ? 40.519 15.039  -21.361 1.00 34.35  ?  139 ALA A O   1 
ATOM   1123 C CB  . ALA A 1 140 ? 41.517 15.381  -18.162 1.00 32.48  ?  139 ALA A CB  1 
ATOM   1124 N N   . ALA A 1 141 ? 40.040 16.993  -20.348 1.00 33.99  ?  140 ALA A N   1 
ATOM   1125 C CA  . ALA A 1 141 ? 38.855 17.205  -21.166 1.00 35.72  ?  140 ALA A CA  1 
ATOM   1126 C C   . ALA A 1 141 ? 39.213 17.319  -22.640 1.00 33.27  ?  140 ALA A C   1 
ATOM   1127 O O   . ALA A 1 141 ? 38.399 16.990  -23.503 1.00 32.74  ?  140 ALA A O   1 
ATOM   1128 C CB  . ALA A 1 141 ? 38.115 18.447  -20.677 1.00 33.02  ?  140 ALA A CB  1 
ATOM   1129 N N   . GLN A 1 142 ? 40.432 17.757  -22.950 1.00 38.56  ?  141 GLN A N   1 
ATOM   1130 C CA  . GLN A 1 142 ? 40.868 17.791  -24.347 1.00 39.32  ?  141 GLN A CA  1 
ATOM   1131 C C   . GLN A 1 142 ? 40.970 16.384  -24.946 1.00 40.97  ?  141 GLN A C   1 
ATOM   1132 O O   . GLN A 1 142 ? 40.769 16.211  -26.156 1.00 38.45  ?  141 GLN A O   1 
ATOM   1133 C CB  . GLN A 1 142 ? 42.201 18.548  -24.452 1.00 42.22  ?  141 GLN A CB  1 
ATOM   1134 C CG  . GLN A 1 142 ? 42.091 20.065  -24.139 1.00 46.25  ?  141 GLN A CG  1 
ATOM   1135 C CD  . GLN A 1 142 ? 41.830 20.969  -25.372 1.00 57.96  ?  141 GLN A CD  1 
ATOM   1136 O OE1 . GLN A 1 142 ? 41.694 22.190  -25.217 1.00 65.94  ?  141 GLN A OE1 1 
ATOM   1137 N NE2 . GLN A 1 142 ? 41.757 20.380  -26.583 1.00 57.57  ?  141 GLN A NE2 1 
ATOM   1138 N N   . ILE A 1 143 ? 41.272 15.371  -24.127 1.00 36.38  ?  142 ILE A N   1 
ATOM   1139 C CA  . ILE A 1 143 ? 41.210 13.986  -24.606 1.00 38.41  ?  142 ILE A CA  1 
ATOM   1140 C C   . ILE A 1 143 ? 39.788 13.653  -25.031 1.00 38.14  ?  142 ILE A C   1 
ATOM   1141 O O   . ILE A 1 143 ? 39.544 13.118  -26.125 1.00 35.04  ?  142 ILE A O   1 
ATOM   1142 C CB  . ILE A 1 143 ? 41.695 13.013  -23.516 1.00 36.56  ?  142 ILE A CB  1 
ATOM   1143 C CG1 . ILE A 1 143 ? 43.109 13.380  -23.080 1.00 39.65  ?  142 ILE A CG1 1 
ATOM   1144 C CG2 . ILE A 1 143 ? 41.621 11.565  -24.010 1.00 34.95  ?  142 ILE A CG2 1 
ATOM   1145 C CD1 . ILE A 1 143 ? 43.553 12.668  -21.817 1.00 43.32  ?  142 ILE A CD1 1 
ATOM   1146 N N   . THR A 1 144 ? 38.829 13.959  -24.155 1.00 34.01  ?  143 THR A N   1 
ATOM   1147 C CA  . THR A 1 144 ? 37.421 13.789  -24.484 1.00 33.88  ?  143 THR A CA  1 
ATOM   1148 C C   . THR A 1 144 ? 37.040 14.563  -25.739 1.00 34.36  ?  143 THR A C   1 
ATOM   1149 O O   . THR A 1 144 ? 36.277 14.058  -26.576 1.00 34.17  ?  143 THR A O   1 
ATOM   1150 C CB  . THR A 1 144 ? 36.558 14.224  -23.295 1.00 35.04  ?  143 THR A CB  1 
ATOM   1151 O OG1 . THR A 1 144 ? 36.937 13.458  -22.132 1.00 30.01  ?  143 THR A OG1 1 
ATOM   1152 C CG2 . THR A 1 144 ? 35.065 14.026  -23.604 1.00 31.20  ?  143 THR A CG2 1 
ATOM   1153 N N   . LYS A 1 145 ? 37.552 15.789  -25.894 1.00 30.68  ?  144 LYS A N   1 
ATOM   1154 C CA  . LYS A 1 145 ? 37.207 16.585  -27.075 1.00 33.70  ?  144 LYS A CA  1 
ATOM   1155 C C   . LYS A 1 145 ? 37.582 15.859  -28.360 1.00 30.93  ?  144 LYS A C   1 
ATOM   1156 O O   . LYS A 1 145 ? 36.808 15.829  -29.322 1.00 31.40  ?  144 LYS A O   1 
ATOM   1157 C CB  . LYS A 1 145 ? 37.902 17.943  -27.021 1.00 36.57  ?  144 LYS A CB  1 
ATOM   1158 C CG  . LYS A 1 145 ? 37.584 18.887  -28.188 1.00 39.71  ?  144 LYS A CG  1 
ATOM   1159 C CD  . LYS A 1 145 ? 37.765 20.345  -27.756 1.00 40.30  ?  144 LYS A CD  1 
ATOM   1160 C CE  . LYS A 1 145 ? 39.000 21.018  -28.363 1.00 52.43  ?  144 LYS A CE  1 
ATOM   1161 N NZ  . LYS A 1 145 ? 38.881 21.155  -29.844 1.00 52.72  ?  144 LYS A NZ  1 
ATOM   1162 N N   . ARG A 1 146 ? 38.781 15.283  -28.398 1.00 36.83  ?  145 ARG A N   1 
ATOM   1163 C CA  . ARG A 1 146 ? 39.235 14.602  -29.604 1.00 39.52  ?  145 ARG A CA  1 
ATOM   1164 C C   . ARG A 1 146 ? 38.378 13.381  -29.892 1.00 38.68  ?  145 ARG A C   1 
ATOM   1165 O O   . ARG A 1 146 ? 38.047 13.103  -31.051 1.00 35.43  ?  145 ARG A O   1 
ATOM   1166 C CB  . ARG A 1 146 ? 40.707 14.206  -29.456 1.00 42.03  ?  145 ARG A CB  1 
ATOM   1167 C CG  . ARG A 1 146 ? 41.697 15.268  -29.969 1.00 45.03  ?  145 ARG A CG  1 
ATOM   1168 C CD  . ARG A 1 146 ? 42.878 15.519  -29.010 1.00 57.27  ?  145 ARG A CD  1 
ATOM   1169 N NE  . ARG A 1 146 ? 43.463 14.274  -28.503 1.00 58.73  ?  145 ARG A NE  1 
ATOM   1170 C CZ  . ARG A 1 146 ? 44.115 14.147  -27.343 1.00 58.62  ?  145 ARG A CZ  1 
ATOM   1171 N NH1 . ARG A 1 146 ? 44.304 15.202  -26.550 1.00 46.55  ?  145 ARG A NH1 1 
ATOM   1172 N NH2 . ARG A 1 146 ? 44.581 12.950  -26.974 1.00 56.99  ?  145 ARG A NH2 1 
ATOM   1173 N N   . LYS A 1 147 ? 38.024 12.626  -28.850 1.00 36.65  ?  146 LYS A N   1 
ATOM   1174 C CA  . LYS A 1 147 ? 37.129 11.497  -29.050 1.00 33.04  ?  146 LYS A CA  1 
ATOM   1175 C C   . LYS A 1 147 ? 35.802 11.964  -29.617 1.00 35.28  ?  146 LYS A C   1 
ATOM   1176 O O   . LYS A 1 147 ? 35.246 11.334  -30.521 1.00 34.07  ?  146 LYS A O   1 
ATOM   1177 C CB  . LYS A 1 147 ? 36.872 10.768  -27.738 1.00 33.33  ?  146 LYS A CB  1 
ATOM   1178 C CG  . LYS A 1 147 ? 38.046 10.115  -27.072 1.00 42.11  ?  146 LYS A CG  1 
ATOM   1179 C CD  . LYS A 1 147 ? 37.499 9.231   -25.952 1.00 42.64  ?  146 LYS A CD  1 
ATOM   1180 C CE  . LYS A 1 147 ? 38.580 8.635   -25.111 1.00 36.01  ?  146 LYS A CE  1 
ATOM   1181 N NZ  . LYS A 1 147 ? 37.975 7.729   -24.107 1.00 42.20  ?  146 LYS A NZ  1 
ATOM   1182 N N   . TRP A 1 148 ? 35.270 13.063  -29.074 1.00 35.07  ?  147 TRP A N   1 
ATOM   1183 C CA  . TRP A 1 148 ? 33.913 13.474  -29.416 1.00 35.80  ?  147 TRP A CA  1 
ATOM   1184 C C   . TRP A 1 148 ? 33.856 14.018  -30.836 1.00 34.57  ?  147 TRP A C   1 
ATOM   1185 O O   . TRP A 1 148 ? 32.890 13.760  -31.570 1.00 34.92  ?  147 TRP A O   1 
ATOM   1186 C CB  . TRP A 1 148 ? 33.415 14.490  -28.390 1.00 29.20  ?  147 TRP A CB  1 
ATOM   1187 C CG  . TRP A 1 148 ? 32.929 13.807  -27.114 1.00 29.14  ?  147 TRP A CG  1 
ATOM   1188 C CD1 . TRP A 1 148 ? 33.155 12.506  -26.752 1.00 32.00  ?  147 TRP A CD1 1 
ATOM   1189 C CD2 . TRP A 1 148 ? 32.160 14.390  -26.045 1.00 29.78  ?  147 TRP A CD2 1 
ATOM   1190 N NE1 . TRP A 1 148 ? 32.563 12.245  -25.542 1.00 30.31  ?  147 TRP A NE1 1 
ATOM   1191 C CE2 . TRP A 1 148 ? 31.942 13.380  -25.088 1.00 24.40  ?  147 TRP A CE2 1 
ATOM   1192 C CE3 . TRP A 1 148 ? 31.618 15.658  -25.819 1.00 30.84  ?  147 TRP A CE3 1 
ATOM   1193 C CZ2 . TRP A 1 148 ? 31.227 13.601  -23.910 1.00 25.21  ?  147 TRP A CZ2 1 
ATOM   1194 C CZ3 . TRP A 1 148 ? 30.892 15.879  -24.643 1.00 29.66  ?  147 TRP A CZ3 1 
ATOM   1195 C CH2 . TRP A 1 148 ? 30.712 14.853  -23.703 1.00 31.72  ?  147 TRP A CH2 1 
ATOM   1196 N N   . GLU A 1 149 ? 34.896 14.742  -31.246 1.00 34.14  ?  148 GLU A N   1 
ATOM   1197 C CA  . GLU A 1 149 ? 35.012 15.166  -32.638 1.00 37.42  ?  148 GLU A CA  1 
ATOM   1198 C C   . GLU A 1 149 ? 35.050 13.957  -33.560 1.00 39.46  ?  148 GLU A C   1 
ATOM   1199 O O   . GLU A 1 149 ? 34.321 13.899  -34.561 1.00 40.14  ?  148 GLU A O   1 
ATOM   1200 C CB  . GLU A 1 149 ? 36.268 16.030  -32.809 1.00 35.41  ?  148 GLU A CB  1 
ATOM   1201 C CG  . GLU A 1 149 ? 36.177 17.389  -32.130 1.00 36.05  ?  148 GLU A CG  1 
ATOM   1202 C CD  . GLU A 1 149 ? 37.538 18.045  -31.899 1.00 41.92  ?  148 GLU A CD  1 
ATOM   1203 O OE1 . GLU A 1 149 ? 38.570 17.352  -31.988 1.00 45.76  ?  148 GLU A OE1 1 
ATOM   1204 O OE2 . GLU A 1 149 ? 37.572 19.258  -31.601 1.00 46.28  -1 148 GLU A OE2 1 
ATOM   1205 N N   . ALA A 1 150 ? 35.855 12.949  -33.200 1.00 35.25  ?  149 ALA A N   1 
ATOM   1206 C CA  . ALA A 1 150 ? 36.023 11.794  -34.074 1.00 39.37  ?  149 ALA A CA  1 
ATOM   1207 C C   . ALA A 1 150 ? 34.718 11.041  -34.308 1.00 41.37  ?  149 ALA A C   1 
ATOM   1208 O O   . ALA A 1 150 ? 34.583 10.383  -35.340 1.00 43.29  ?  149 ALA A O   1 
ATOM   1209 C CB  . ALA A 1 150 ? 37.063 10.835  -33.508 1.00 39.17  ?  149 ALA A CB  1 
ATOM   1210 N N   . VAL A 1 151 ? 33.751 11.100  -33.385 1.00 37.24  ?  150 VAL A N   1 
ATOM   1211 C CA  . VAL A 1 151 ? 32.482 10.390  -33.581 1.00 35.64  ?  150 VAL A CA  1 
ATOM   1212 C C   . VAL A 1 151 ? 31.346 11.343  -33.921 1.00 33.53  ?  150 VAL A C   1 
ATOM   1213 O O   . VAL A 1 151 ? 30.172 10.933  -33.914 1.00 30.86  ?  150 VAL A O   1 
ATOM   1214 C CB  . VAL A 1 151 ? 32.097 9.520   -32.372 1.00 34.86  ?  150 VAL A CB  1 
ATOM   1215 C CG1 . VAL A 1 151 ? 33.105 8.407   -32.158 1.00 37.46  ?  150 VAL A CG1 1 
ATOM   1216 C CG2 . VAL A 1 151 ? 31.898 10.396  -31.115 1.00 33.65  ?  150 VAL A CG2 1 
ATOM   1217 N N   . HIS A 1 152 ? 31.663 12.611  -34.194 1.00 37.35  ?  151 HIS A N   1 
ATOM   1218 C CA  . HIS A 1 152 ? 30.668 13.649  -34.492 1.00 37.32  ?  151 HIS A CA  1 
ATOM   1219 C C   . HIS A 1 152 ? 29.567 13.692  -33.441 1.00 32.38  ?  151 HIS A C   1 
ATOM   1220 O O   . HIS A 1 152 ? 28.371 13.734  -33.747 1.00 34.57  ?  151 HIS A O   1 
ATOM   1221 C CB  . HIS A 1 152 ? 30.101 13.437  -35.893 1.00 40.22  ?  151 HIS A CB  1 
ATOM   1222 C CG  . HIS A 1 152 ? 31.165 13.395  -36.939 1.00 47.53  ?  151 HIS A CG  1 
ATOM   1223 N ND1 . HIS A 1 152 ? 31.682 14.537  -37.513 1.00 54.26  ?  151 HIS A ND1 1 
ATOM   1224 C CD2 . HIS A 1 152 ? 31.852 12.358  -37.475 1.00 47.08  ?  151 HIS A CD2 1 
ATOM   1225 C CE1 . HIS A 1 152 ? 32.622 14.205  -38.378 1.00 56.06  ?  151 HIS A CE1 1 
ATOM   1226 N NE2 . HIS A 1 152 ? 32.748 12.889  -38.370 1.00 58.73  ?  151 HIS A NE2 1 
ATOM   1227 N N   . ALA A 1 153 ? 29.991 13.718  -32.178 1.00 31.27  ?  152 ALA A N   1 
ATOM   1228 C CA  . ALA A 1 153 ? 29.052 13.929  -31.083 1.00 29.57  ?  152 ALA A CA  1 
ATOM   1229 C C   . ALA A 1 153 ? 28.316 15.260  -31.212 1.00 25.28  ?  152 ALA A C   1 
ATOM   1230 O O   . ALA A 1 153 ? 27.137 15.363  -30.846 1.00 29.89  ?  152 ALA A O   1 
ATOM   1231 C CB  . ALA A 1 153 ? 29.803 13.873  -29.748 1.00 32.85  ?  152 ALA A CB  1 
ATOM   1232 N N   . ALA A 1 154 ? 29.000 16.302  -31.685 1.00 29.21  ?  153 ALA A N   1 
ATOM   1233 C CA  . ALA A 1 154 ? 28.370 17.626  -31.721 1.00 30.82  ?  153 ALA A CA  1 
ATOM   1234 C C   . ALA A 1 154 ? 27.093 17.596  -32.545 1.00 26.98  ?  153 ALA A C   1 
ATOM   1235 O O   . ALA A 1 154 ? 26.020 17.997  -32.078 1.00 29.25  ?  153 ALA A O   1 
ATOM   1236 C CB  . ALA A 1 154 ? 29.353 18.650  -32.279 1.00 32.38  ?  153 ALA A CB  1 
ATOM   1237 N N   . GLU A 1 155 ? 27.176 17.054  -33.759 1.00 30.02  ?  154 GLU A N   1 
ATOM   1238 C CA  . GLU A 1 155 ? 25.987 16.904  -34.588 1.00 29.34  ?  154 GLU A CA  1 
ATOM   1239 C C   . GLU A 1 155 ? 24.962 16.015  -33.912 1.00 28.33  ?  154 GLU A C   1 
ATOM   1240 O O   . GLU A 1 155 ? 23.747 16.228  -34.057 1.00 27.55  ?  154 GLU A O   1 
ATOM   1241 C CB  . GLU A 1 155 ? 26.389 16.325  -35.954 1.00 38.32  ?  154 GLU A CB  1 
ATOM   1242 C CG  . GLU A 1 155 ? 25.223 16.169  -36.912 1.00 45.58  ?  154 GLU A CG  1 
ATOM   1243 C CD  . GLU A 1 155 ? 25.633 15.781  -38.335 1.00 47.21  ?  154 GLU A CD  1 
ATOM   1244 O OE1 . GLU A 1 155 ? 26.845 15.867  -38.691 1.00 43.91  ?  154 GLU A OE1 1 
ATOM   1245 O OE2 . GLU A 1 155 ? 24.700 15.384  -39.078 1.00 45.11  -1 154 GLU A OE2 1 
ATOM   1246 N N   . GLN A 1 156 ? 25.433 15.011  -33.166 1.00 29.40  ?  155 GLN A N   1 
ATOM   1247 C CA  . GLN A 1 156 ? 24.512 14.125  -32.467 1.00 26.42  ?  155 GLN A CA  1 
ATOM   1248 C C   . GLN A 1 156 ? 23.697 14.887  -31.441 1.00 29.79  ?  155 GLN A C   1 
ATOM   1249 O O   . GLN A 1 156 ? 22.486 14.664  -31.317 1.00 27.88  ?  155 GLN A O   1 
ATOM   1250 C CB  . GLN A 1 156 ? 25.264 12.979  -31.787 1.00 27.71  ?  155 GLN A CB  1 
ATOM   1251 C CG  . GLN A 1 156 ? 24.341 11.836  -31.365 1.00 27.58  ?  155 GLN A CG  1 
ATOM   1252 C CD  . GLN A 1 156 ? 23.906 10.979  -32.561 1.00 27.42  ?  155 GLN A CD  1 
ATOM   1253 O OE1 . GLN A 1 156 ? 24.674 10.778  -33.491 1.00 26.39  ?  155 GLN A OE1 1 
ATOM   1254 N NE2 . GLN A 1 156 ? 22.674 10.486  -32.536 1.00 30.50  ?  155 GLN A NE2 1 
ATOM   1255 N N   . ARG A 1 157 ? 24.348 15.777  -30.672 1.00 28.76  ?  156 ARG A N   1 
ATOM   1256 C CA  . ARG A 1 157 ? 23.610 16.638  -29.746 1.00 29.47  ?  156 ARG A CA  1 
ATOM   1257 C C   . ARG A 1 157 ? 22.735 17.641  -30.498 1.00 23.94  ?  156 ARG A C   1 
ATOM   1258 O O   . ARG A 1 157 ? 21.566 17.850  -30.151 1.00 25.58  ?  156 ARG A O   1 
ATOM   1259 C CB  . ARG A 1 157 ? 24.594 17.374  -28.830 1.00 26.91  ?  156 ARG A CB  1 
ATOM   1260 C CG  . ARG A 1 157 ? 25.621 16.435  -28.150 1.00 29.68  ?  156 ARG A CG  1 
ATOM   1261 C CD  . ARG A 1 157 ? 25.006 15.693  -26.989 1.00 28.75  ?  156 ARG A CD  1 
ATOM   1262 N NE  . ARG A 1 157 ? 24.184 14.511  -27.304 1.00 32.27  ?  156 ARG A NE  1 
ATOM   1263 C CZ  . ARG A 1 157 ? 24.652 13.262  -27.406 1.00 28.21  ?  156 ARG A CZ  1 
ATOM   1264 N NH1 . ARG A 1 157 ? 25.944 13.010  -27.271 1.00 27.87  ?  156 ARG A NH1 1 
ATOM   1265 N NH2 . ARG A 1 157 ? 23.820 12.264  -27.662 1.00 32.20  ?  156 ARG A NH2 1 
ATOM   1266 N N   . ARG A 1 158 ? 23.293 18.279  -31.523 1.00 26.60  ?  157 ARG A N   1 
ATOM   1267 C CA  . ARG A 1 158 ? 22.552 19.309  -32.249 1.00 30.46  ?  157 ARG A CA  1 
ATOM   1268 C C   . ARG A 1 158 ? 21.258 18.747  -32.825 1.00 32.13  ?  157 ARG A C   1 
ATOM   1269 O O   . ARG A 1 158 ? 20.198 19.384  -32.751 1.00 35.36  ?  157 ARG A O   1 
ATOM   1270 C CB  . ARG A 1 158 ? 23.430 19.902  -33.355 1.00 30.26  ?  157 ARG A CB  1 
ATOM   1271 C CG  . ARG A 1 158 ? 22.628 20.708  -34.368 1.00 34.86  ?  157 ARG A CG  1 
ATOM   1272 C CD  . ARG A 1 158 ? 23.471 21.637  -35.223 1.00 40.14  ?  157 ARG A CD  1 
ATOM   1273 N NE  . ARG A 1 158 ? 24.469 20.965  -36.057 1.00 47.78  ?  157 ARG A NE  1 
ATOM   1274 C CZ  . ARG A 1 158 ? 24.197 20.305  -37.177 1.00 53.18  ?  157 ARG A CZ  1 
ATOM   1275 N NH1 . ARG A 1 158 ? 22.942 20.201  -37.600 1.00 55.72  ?  157 ARG A NH1 1 
ATOM   1276 N NH2 . ARG A 1 158 ? 25.183 19.735  -37.869 1.00 56.29  ?  157 ARG A NH2 1 
ATOM   1277 N N   . VAL A 1 159 ? 21.303 17.530  -33.360 1.00 32.19  ?  158 VAL A N   1 
ATOM   1278 C CA  . VAL A 1 159 ? 20.093 16.961  -33.932 1.00 27.52  ?  158 VAL A CA  1 
ATOM   1279 C C   . VAL A 1 159 ? 19.035 16.791  -32.863 1.00 31.02  ?  158 VAL A C   1 
ATOM   1280 O O   . VAL A 1 159 ? 17.839 16.966  -33.113 1.00 32.56  ?  158 VAL A O   1 
ATOM   1281 C CB  . VAL A 1 159 ? 20.422 15.636  -34.640 1.00 36.57  ?  158 VAL A CB  1 
ATOM   1282 C CG1 . VAL A 1 159 ? 19.200 14.784  -34.753 1.00 39.13  ?  158 VAL A CG1 1 
ATOM   1283 C CG2 . VAL A 1 159 ? 21.025 15.943  -36.022 1.00 36.29  ?  158 VAL A CG2 1 
ATOM   1284 N N   . TYR A 1 160 ? 19.447 16.413  -31.659 1.00 27.79  ?  159 TYR A N   1 
ATOM   1285 C CA  . TYR A 1 160 ? 18.480 16.328  -30.571 1.00 25.71  ?  159 TYR A CA  1 
ATOM   1286 C C   . TYR A 1 160 ? 17.954 17.706  -30.183 1.00 25.50  ?  159 TYR A C   1 
ATOM   1287 O O   . TYR A 1 160 ? 16.745 17.887  -29.962 1.00 29.06  ?  159 TYR A O   1 
ATOM   1288 C CB  . TYR A 1 160 ? 19.122 15.651  -29.345 1.00 27.36  ?  159 TYR A CB  1 
ATOM   1289 C CG  . TYR A 1 160 ? 18.352 15.882  -28.071 1.00 21.36  ?  159 TYR A CG  1 
ATOM   1290 C CD1 . TYR A 1 160 ? 17.221 15.136  -27.789 1.00 24.63  ?  159 TYR A CD1 1 
ATOM   1291 C CD2 . TYR A 1 160 ? 18.730 16.860  -27.165 1.00 25.62  ?  159 TYR A CD2 1 
ATOM   1292 C CE1 . TYR A 1 160 ? 16.505 15.327  -26.652 1.00 24.17  ?  159 TYR A CE1 1 
ATOM   1293 C CE2 . TYR A 1 160 ? 17.999 17.065  -25.993 1.00 29.26  ?  159 TYR A CE2 1 
ATOM   1294 C CZ  . TYR A 1 160 ? 16.897 16.291  -25.754 1.00 27.57  ?  159 TYR A CZ  1 
ATOM   1295 O OH  . TYR A 1 160 ? 16.151 16.456  -24.629 1.00 25.36  ?  159 TYR A OH  1 
ATOM   1296 N N   . LEU A 1 161 ? 18.864 18.674  -30.035 1.00 26.18  ?  160 LEU A N   1 
ATOM   1297 C CA  . LEU A 1 161 ? 18.519 19.981  -29.473 1.00 33.44  ?  160 LEU A CA  1 
ATOM   1298 C C   . LEU A 1 161 ? 17.623 20.790  -30.412 1.00 35.65  ?  160 LEU A C   1 
ATOM   1299 O O   . LEU A 1 161 ? 16.652 21.422  -29.965 1.00 36.20  ?  160 LEU A O   1 
ATOM   1300 C CB  . LEU A 1 161 ? 19.806 20.754  -29.188 1.00 25.73  ?  160 LEU A CB  1 
ATOM   1301 C CG  . LEU A 1 161 ? 20.788 20.153  -28.173 1.00 32.03  ?  160 LEU A CG  1 
ATOM   1302 C CD1 . LEU A 1 161 ? 22.125 20.882  -28.304 1.00 26.41  ?  160 LEU A CD1 1 
ATOM   1303 C CD2 . LEU A 1 161 ? 20.210 20.257  -26.787 1.00 30.31  ?  160 LEU A CD2 1 
ATOM   1304 N N   . GLU A 1 162 ? 17.955 20.801  -31.707 1.00 34.46  ?  161 GLU A N   1 
ATOM   1305 C CA  . GLU A 1 162 ? 17.159 21.451  -32.743 1.00 38.26  ?  161 GLU A CA  1 
ATOM   1306 C C   . GLU A 1 162 ? 15.913 20.658  -33.124 1.00 43.82  ?  161 GLU A C   1 
ATOM   1307 O O   . GLU A 1 162 ? 15.050 21.211  -33.818 1.00 40.79  ?  161 GLU A O   1 
ATOM   1308 C CB  . GLU A 1 162 ? 18.016 21.677  -34.002 1.00 39.57  ?  161 GLU A CB  1 
ATOM   1309 C CG  . GLU A 1 162 ? 19.102 22.737  -33.856 1.00 40.55  ?  161 GLU A CG  1 
ATOM   1310 C CD  . GLU A 1 162 ? 20.035 22.817  -35.058 1.00 41.12  ?  161 GLU A CD  1 
ATOM   1311 O OE1 . GLU A 1 162 ? 20.869 23.743  -35.107 1.00 41.79  ?  161 GLU A OE1 1 
ATOM   1312 O OE2 . GLU A 1 162 ? 19.954 21.953  -35.949 1.00 49.59  -1 161 GLU A OE2 1 
ATOM   1313 N N   . GLY A 1 163 ? 15.782 19.401  -32.671 1.00 39.97  ?  162 GLY A N   1 
ATOM   1314 C CA  . GLY A 1 163 ? 14.744 18.511  -33.169 1.00 31.61  ?  162 GLY A CA  1 
ATOM   1315 C C   . GLY A 1 163 ? 13.839 17.888  -32.127 1.00 34.05  ?  162 GLY A C   1 
ATOM   1316 O O   . GLY A 1 163 ? 12.763 18.417  -31.831 1.00 36.98  ?  162 GLY A O   1 
ATOM   1317 N N   . ARG A 1 164 ? 14.245 16.745  -31.574 1.00 29.84  ?  163 ARG A N   1 
ATOM   1318 C CA  . ARG A 1 164 ? 13.434 16.089  -30.554 1.00 28.39  ?  163 ARG A CA  1 
ATOM   1319 C C   . ARG A 1 164 ? 13.160 17.013  -29.357 1.00 24.81  ?  163 ARG A C   1 
ATOM   1320 O O   . ARG A 1 164 ? 12.064 16.996  -28.786 1.00 27.83  ?  163 ARG A O   1 
ATOM   1321 C CB  . ARG A 1 164 ? 14.140 14.805  -30.100 1.00 29.36  ?  163 ARG A CB  1 
ATOM   1322 C CG  . ARG A 1 164 ? 13.319 13.930  -29.169 1.00 30.29  ?  163 ARG A CG  1 
ATOM   1323 C CD  . ARG A 1 164 ? 14.176 12.810  -28.528 1.00 30.52  ?  163 ARG A CD  1 
ATOM   1324 N NE  . ARG A 1 164 ? 14.839 11.950  -29.513 1.00 32.25  ?  163 ARG A NE  1 
ATOM   1325 C CZ  . ARG A 1 164 ? 15.853 11.127  -29.249 1.00 31.76  ?  163 ARG A CZ  1 
ATOM   1326 N NH1 . ARG A 1 164 ? 16.372 11.030  -28.016 1.00 26.04  ?  163 ARG A NH1 1 
ATOM   1327 N NH2 . ARG A 1 164 ? 16.348 10.378  -30.225 1.00 36.20  ?  163 ARG A NH2 1 
ATOM   1328 N N   . CYS A 1 165 ? 14.147 17.790  -28.932 1.00 29.88  ?  164 CYS A N   1 
ATOM   1329 C CA  . CYS A 1 165 ? 13.957 18.648  -27.762 1.00 28.12  ?  164 CYS A CA  1 
ATOM   1330 C C   . CYS A 1 165 ? 12.855 19.683  -28.024 1.00 28.73  ?  164 CYS A C   1 
ATOM   1331 O O   . CYS A 1 165 ? 11.938 19.854  -27.209 1.00 33.58  ?  164 CYS A O   1 
ATOM   1332 C CB  . CYS A 1 165 ? 15.280 19.329  -27.420 1.00 29.37  ?  164 CYS A CB  1 
ATOM   1333 S SG  . CYS A 1 165 ? 15.361 20.329  -25.913 1.00 35.37  ?  164 CYS A SG  1 
ATOM   1334 N N   . VAL A 1 166 ? 12.936 20.354  -29.178 1.00 34.58  ?  165 VAL A N   1 
ATOM   1335 C CA  . VAL A 1 166 ? 11.911 21.328  -29.556 1.00 34.52  ?  165 VAL A CA  1 
ATOM   1336 C C   . VAL A 1 166 ? 10.556 20.648  -29.633 1.00 37.06  ?  165 VAL A C   1 
ATOM   1337 O O   . VAL A 1 166 ? 9.551  21.169  -29.129 1.00 31.58  ?  165 VAL A O   1 
ATOM   1338 C CB  . VAL A 1 166 ? 12.268 21.998  -30.898 1.00 38.31  ?  165 VAL A CB  1 
ATOM   1339 C CG1 . VAL A 1 166 ? 11.064 22.821  -31.417 1.00 42.50  ?  165 VAL A CG1 1 
ATOM   1340 C CG2 . VAL A 1 166 ? 13.486 22.862  -30.774 1.00 36.20  ?  165 VAL A CG2 1 
ATOM   1341 N N   . ASP A 1 167 ? 10.507 19.452  -30.228 1.00 34.10  ?  166 ASP A N   1 
ATOM   1342 C CA  . ASP A 1 167 ? 9.219  18.805  -30.424 1.00 27.94  ?  166 ASP A CA  1 
ATOM   1343 C C   . ASP A 1 167 ? 8.603  18.406  -29.099 1.00 32.08  ?  166 ASP A C   1 
ATOM   1344 O O   . ASP A 1 167 ? 7.399  18.581  -28.883 1.00 36.54  ?  166 ASP A O   1 
ATOM   1345 C CB  . ASP A 1 167 ? 9.360  17.587  -31.340 1.00 37.30  ?  166 ASP A CB  1 
ATOM   1346 C CG  . ASP A 1 167 ? 8.018  17.032  -31.757 1.00 41.65  ?  166 ASP A CG  1 
ATOM   1347 O OD1 . ASP A 1 167 ? 7.300  17.717  -32.529 1.00 42.21  ?  166 ASP A OD1 1 
ATOM   1348 O OD2 . ASP A 1 167 ? 7.665  15.929  -31.292 1.00 42.70  -1 166 ASP A OD2 1 
ATOM   1349 N N   . GLY A 1 168 ? 9.401  17.868  -28.183 1.00 30.38  ?  167 GLY A N   1 
ATOM   1350 C CA  . GLY A 1 168 ? 8.842  17.515  -26.890 1.00 32.65  ?  167 GLY A CA  1 
ATOM   1351 C C   . GLY A 1 168 ? 8.393  18.746  -26.122 1.00 28.65  ?  167 GLY A C   1 
ATOM   1352 O O   . GLY A 1 168 ? 7.322  18.755  -25.512 1.00 29.79  ?  167 GLY A O   1 
ATOM   1353 N N   . LEU A 1 169 ? 9.209  19.795  -26.146 1.00 28.58  ?  168 LEU A N   1 
ATOM   1354 C CA  . LEU A 1 169 ? 8.856  21.035  -25.452 1.00 35.62  ?  168 LEU A CA  1 
ATOM   1355 C C   . LEU A 1 169 ? 7.517  21.575  -25.944 1.00 35.97  ?  168 LEU A C   1 
ATOM   1356 O O   . LEU A 1 169 ? 6.663  21.962  -25.136 1.00 34.93  ?  168 LEU A O   1 
ATOM   1357 C CB  . LEU A 1 169 ? 9.965  22.066  -25.659 1.00 29.88  ?  168 LEU A CB  1 
ATOM   1358 C CG  . LEU A 1 169 ? 9.792  23.434  -24.983 1.00 33.07  ?  168 LEU A CG  1 
ATOM   1359 C CD1 . LEU A 1 169 ? 9.359  23.305  -23.563 1.00 32.76  ?  168 LEU A CD1 1 
ATOM   1360 C CD2 . LEU A 1 169 ? 11.088 24.210  -25.090 1.00 31.57  ?  168 LEU A CD2 1 
ATOM   1361 N N   . ARG A 1 170 ? 7.303  21.571  -27.270 1.00 37.76  ?  169 ARG A N   1 
ATOM   1362 C CA  . ARG A 1 170 ? 6.006  21.969  -27.819 1.00 38.68  ?  169 ARG A CA  1 
ATOM   1363 C C   . ARG A 1 170 ? 4.884  21.131  -27.227 1.00 44.96  ?  169 ARG A C   1 
ATOM   1364 O O   . ARG A 1 170 ? 3.890  21.666  -26.713 1.00 39.18  ?  169 ARG A O   1 
ATOM   1365 C CB  . ARG A 1 170 ? 6.004  21.832  -29.340 1.00 41.09  ?  169 ARG A CB  1 
ATOM   1366 C CG  . ARG A 1 170 ? 7.095  22.582  -30.053 1.00 40.82  ?  169 ARG A CG  1 
ATOM   1367 C CD  . ARG A 1 170 ? 6.592  23.148  -31.378 1.00 50.96  ?  169 ARG A CD  1 
ATOM   1368 N NE  . ARG A 1 170 ? 7.645  23.230  -32.390 1.00 56.23  ?  169 ARG A NE  1 
ATOM   1369 C CZ  . ARG A 1 170 ? 7.492  23.793  -33.590 1.00 69.04  ?  169 ARG A CZ  1 
ATOM   1370 N NH1 . ARG A 1 170 ? 6.317  24.333  -33.933 1.00 65.80  ?  169 ARG A NH1 1 
ATOM   1371 N NH2 . ARG A 1 170 ? 8.517  23.827  -34.446 1.00 61.24  ?  169 ARG A NH2 1 
ATOM   1372 N N   . ARG A 1 171 ? 5.027  19.805  -27.290 1.00 36.03  ?  170 ARG A N   1 
ATOM   1373 C CA  . ARG A 1 171 ? 3.970  18.934  -26.801 1.00 34.74  ?  170 ARG A CA  1 
ATOM   1374 C C   . ARG A 1 171 ? 3.669  19.199  -25.330 1.00 41.96  ?  170 ARG A C   1 
ATOM   1375 O O   . ARG A 1 171 ? 2.500  19.245  -24.923 1.00 36.13  ?  170 ARG A O   1 
ATOM   1376 C CB  . ARG A 1 171 ? 4.366  17.475  -27.023 1.00 32.31  ?  170 ARG A CB  1 
ATOM   1377 C CG  . ARG A 1 171 ? 3.524  16.448  -26.308 1.00 35.46  ?  170 ARG A CG  1 
ATOM   1378 C CD  . ARG A 1 171 ? 4.178  15.061  -26.444 1.00 35.36  ?  170 ARG A CD  1 
ATOM   1379 N NE  . ARG A 1 171 ? 3.386  14.018  -25.807 1.00 32.13  ?  170 ARG A NE  1 
ATOM   1380 C CZ  . ARG A 1 171 ? 2.436  13.346  -26.444 1.00 36.18  ?  170 ARG A CZ  1 
ATOM   1381 N NH1 . ARG A 1 171 ? 1.755  12.397  -25.831 1.00 32.97  ?  170 ARG A NH1 1 
ATOM   1382 N NH2 . ARG A 1 171 ? 2.173  13.641  -27.712 1.00 38.56  ?  170 ARG A NH2 1 
ATOM   1383 N N   . TYR A 1 172 ? 4.708  19.333  -24.501 1.00 39.46  ?  171 TYR A N   1 
ATOM   1384 C CA  . TYR A 1 172 ? 4.456  19.512  -23.069 1.00 32.87  ?  171 TYR A CA  1 
ATOM   1385 C C   . TYR A 1 172 ? 3.777  20.853  -22.798 1.00 31.63  ?  171 TYR A C   1 
ATOM   1386 O O   . TYR A 1 172 ? 2.880  20.936  -21.957 1.00 36.56  ?  171 TYR A O   1 
ATOM   1387 C CB  . TYR A 1 172 ? 5.759  19.421  -22.263 1.00 37.60  ?  171 TYR A CB  1 
ATOM   1388 C CG  . TYR A 1 172 ? 6.568  18.141  -22.415 1.00 34.46  ?  171 TYR A CG  1 
ATOM   1389 C CD1 . TYR A 1 172 ? 5.949  16.905  -22.520 1.00 33.36  ?  171 TYR A CD1 1 
ATOM   1390 C CD2 . TYR A 1 172 ? 7.968  18.181  -22.443 1.00 35.81  ?  171 TYR A CD2 1 
ATOM   1391 C CE1 . TYR A 1 172 ? 6.682  15.745  -22.660 1.00 32.79  ?  171 TYR A CE1 1 
ATOM   1392 C CE2 . TYR A 1 172 ? 8.719  17.017  -22.586 1.00 31.44  ?  171 TYR A CE2 1 
ATOM   1393 C CZ  . TYR A 1 172 ? 8.068  15.807  -22.699 1.00 32.63  ?  171 TYR A CZ  1 
ATOM   1394 O OH  . TYR A 1 172 ? 8.803  14.654  -22.844 1.00 35.00  ?  171 TYR A OH  1 
ATOM   1395 N N   . LEU A 1 173 ? 4.191  21.912  -23.505 1.00 33.06  ?  172 LEU A N   1 
ATOM   1396 C CA  . LEU A 1 173 ? 3.553  23.216  -23.330 1.00 43.30  ?  172 LEU A CA  1 
ATOM   1397 C C   . LEU A 1 173 ? 2.072  23.155  -23.674 1.00 48.09  ?  172 LEU A C   1 
ATOM   1398 O O   . LEU A 1 173 ? 1.236  23.692  -22.940 1.00 44.53  ?  172 LEU A O   1 
ATOM   1399 C CB  . LEU A 1 173 ? 4.239  24.267  -24.196 1.00 38.29  ?  172 LEU A CB  1 
ATOM   1400 C CG  . LEU A 1 173 ? 5.615  24.709  -23.719 1.00 40.51  ?  172 LEU A CG  1 
ATOM   1401 C CD1 . LEU A 1 173 ? 6.320  25.535  -24.771 1.00 31.58  ?  172 LEU A CD1 1 
ATOM   1402 C CD2 . LEU A 1 173 ? 5.467  25.465  -22.388 1.00 42.11  ?  172 LEU A CD2 1 
ATOM   1403 N N   . GLU A 1 174 ? 1.723  22.499  -24.787 1.00 47.10  ?  173 GLU A N   1 
ATOM   1404 C CA  . GLU A 1 174 ? 0.313  22.281  -25.103 1.00 41.46  ?  173 GLU A CA  1 
ATOM   1405 C C   . GLU A 1 174 ? -0.379 21.501  -23.995 1.00 46.19  ?  173 GLU A C   1 
ATOM   1406 O O   . GLU A 1 174 ? -1.386 21.947  -23.433 1.00 45.84  ?  173 GLU A O   1 
ATOM   1407 C CB  . GLU A 1 174 ? 0.179  21.534  -26.432 1.00 46.72  ?  173 GLU A CB  1 
ATOM   1408 C CG  . GLU A 1 174 ? 0.011  22.422  -27.651 1.00 52.54  ?  173 GLU A CG  1 
ATOM   1409 C CD  . GLU A 1 174 ? -1.219 23.323  -27.572 1.00 53.99  ?  173 GLU A CD  1 
ATOM   1410 O OE1 . GLU A 1 174 ? -2.331 22.849  -27.212 1.00 52.74  ?  173 GLU A OE1 1 
ATOM   1411 O OE2 . GLU A 1 174 ? -1.051 24.524  -27.866 1.00 66.43  -1 173 GLU A OE2 1 
ATOM   1412 N N   . ASN A 1 175 ? 0.150  20.317  -23.666 1.00 42.01  ?  174 ASN A N   1 
ATOM   1413 C CA  . ASN A 1 175 ? -0.562 19.431  -22.754 1.00 40.82  ?  174 ASN A CA  1 
ATOM   1414 C C   . ASN A 1 175 ? -0.695 20.045  -21.364 1.00 45.61  ?  174 ASN A C   1 
ATOM   1415 O O   . ASN A 1 175 ? -1.649 19.735  -20.629 1.00 44.02  ?  174 ASN A O   1 
ATOM   1416 C CB  . ASN A 1 175 ? 0.144  18.074  -22.675 1.00 48.23  ?  174 ASN A CB  1 
ATOM   1417 C CG  . ASN A 1 175 ? -0.095 17.204  -23.923 1.00 52.78  ?  174 ASN A CG  1 
ATOM   1418 O OD1 . ASN A 1 175 ? -1.056 17.403  -24.659 1.00 49.78  ?  174 ASN A OD1 1 
ATOM   1419 N ND2 . ASN A 1 175 ? 0.788  16.236  -24.150 1.00 44.23  ?  174 ASN A ND2 1 
ATOM   1420 N N   . GLY A 1 176 ? 0.252  20.894  -20.976 1.00 40.63  ?  175 GLY A N   1 
ATOM   1421 C CA  . GLY A 1 176 ? 0.154  21.578  -19.699 1.00 48.27  ?  175 GLY A CA  1 
ATOM   1422 C C   . GLY A 1 176 ? -0.144 23.062  -19.831 1.00 51.42  ?  175 GLY A C   1 
ATOM   1423 O O   . GLY A 1 176 ? 0.205  23.848  -18.944 1.00 45.55  ?  175 GLY A O   1 
ATOM   1424 N N   . LYS A 1 177 ? -0.820 23.442  -20.923 1.00 53.00  ?  176 LYS A N   1 
ATOM   1425 C CA  . LYS A 1 177 ? -0.938 24.852  -21.303 1.00 56.20  ?  176 LYS A CA  1 
ATOM   1426 C C   . LYS A 1 177 ? -1.451 25.711  -20.152 1.00 58.06  ?  176 LYS A C   1 
ATOM   1427 O O   . LYS A 1 177 ? -1.008 26.853  -19.970 1.00 59.27  ?  176 LYS A O   1 
ATOM   1428 C CB  . LYS A 1 177 ? -1.873 24.985  -22.510 1.00 49.96  ?  176 LYS A CB  1 
ATOM   1429 C CG  . LYS A 1 177 ? -3.175 24.189  -22.334 1.00 57.85  ?  176 LYS A CG  1 
ATOM   1430 C CD  . LYS A 1 177 ? -4.001 24.072  -23.624 1.00 61.75  ?  176 LYS A CD  1 
ATOM   1431 C CE  . LYS A 1 177 ? -5.488 23.864  -23.307 1.00 69.54  ?  176 LYS A CE  1 
ATOM   1432 N NZ  . LYS A 1 177 ? -6.391 24.461  -24.338 1.00 69.90  ?  176 LYS A NZ  1 
ATOM   1433 N N   . GLU A 1 178 ? -2.387 25.184  -19.367 1.00 52.06  ?  177 GLU A N   1 
ATOM   1434 C CA  . GLU A 1 178 ? -3.009 26.004  -18.339 1.00 61.33  ?  177 GLU A CA  1 
ATOM   1435 C C   . GLU A 1 178 ? -1.968 26.567  -17.379 1.00 64.89  ?  177 GLU A C   1 
ATOM   1436 O O   . GLU A 1 178 ? -1.984 27.761  -17.054 1.00 67.30  ?  177 GLU A O   1 
ATOM   1437 C CB  . GLU A 1 178 ? -4.059 25.192  -17.582 1.00 64.00  ?  177 GLU A CB  1 
ATOM   1438 C CG  . GLU A 1 178 ? -4.771 26.006  -16.510 1.00 76.86  ?  177 GLU A CG  1 
ATOM   1439 C CD  . GLU A 1 178 ? -4.885 25.271  -15.187 1.00 84.29  ?  177 GLU A CD  1 
ATOM   1440 O OE1 . GLU A 1 178 ? -4.719 25.912  -14.121 1.00 88.43  ?  177 GLU A OE1 1 
ATOM   1441 O OE2 . GLU A 1 178 ? -5.147 24.049  -15.217 1.00 88.50  -1 177 GLU A OE2 1 
ATOM   1442 N N   . THR A 1 179 ? -1.045 25.726  -16.925 1.00 59.52  ?  178 THR A N   1 
ATOM   1443 C CA  . THR A 1 179 ? -0.131 26.100  -15.855 1.00 54.08  ?  178 THR A CA  1 
ATOM   1444 C C   . THR A 1 179 ? 1.210  26.605  -16.366 1.00 57.24  ?  178 THR A C   1 
ATOM   1445 O O   . THR A 1 179 ? 1.806  27.501  -15.753 1.00 54.30  ?  178 THR A O   1 
ATOM   1446 C CB  . THR A 1 179 ? 0.067  24.896  -14.944 1.00 52.12  ?  178 THR A CB  1 
ATOM   1447 O OG1 . THR A 1 179 ? 0.756  23.871  -15.665 1.00 52.13  ?  178 THR A OG1 1 
ATOM   1448 C CG2 . THR A 1 179 ? -1.285 24.362  -14.501 1.00 54.49  ?  178 THR A CG2 1 
ATOM   1449 N N   . LEU A 1 180 ? 1.683  26.079  -17.492 1.00 48.06  ?  179 LEU A N   1 
ATOM   1450 C CA  . LEU A 1 180 ? 2.983  26.482  -18.004 1.00 53.39  ?  179 LEU A CA  1 
ATOM   1451 C C   . LEU A 1 180 ? 2.937  27.846  -18.683 1.00 46.64  ?  179 LEU A C   1 
ATOM   1452 O O   . LEU A 1 180 ? 3.952  28.544  -18.732 1.00 40.92  ?  179 LEU A O   1 
ATOM   1453 C CB  . LEU A 1 180 ? 3.513  25.416  -18.977 1.00 47.53  ?  179 LEU A CB  1 
ATOM   1454 C CG  . LEU A 1 180 ? 3.589  23.998  -18.383 1.00 45.46  ?  179 LEU A CG  1 
ATOM   1455 C CD1 . LEU A 1 180 ? 3.837  22.915  -19.418 1.00 46.30  ?  179 LEU A CD1 1 
ATOM   1456 C CD2 . LEU A 1 180 ? 4.686  23.959  -17.310 1.00 46.50  ?  179 LEU A CD2 1 
ATOM   1457 N N   . GLN A 1 181 ? 1.795  28.257  -19.209 1.00 50.23  ?  180 GLN A N   1 
ATOM   1458 C CA  . GLN A 1 181 ? 1.737  29.522  -19.929 1.00 56.91  ?  180 GLN A CA  1 
ATOM   1459 C C   . GLN A 1 181 ? 1.362  30.710  -19.033 1.00 58.00  ?  180 GLN A C   1 
ATOM   1460 O O   . GLN A 1 181 ? 1.124  31.807  -19.545 1.00 63.84  ?  180 GLN A O   1 
ATOM   1461 C CB  . GLN A 1 181 ? 0.773  29.387  -21.106 1.00 60.33  ?  180 GLN A CB  1 
ATOM   1462 C CG  . GLN A 1 181 ? 1.357  28.571  -22.279 1.00 57.77  ?  180 GLN A CG  1 
ATOM   1463 C CD  . GLN A 1 181 ? 2.419  29.341  -23.070 1.00 61.05  ?  180 GLN A CD  1 
ATOM   1464 O OE1 . GLN A 1 181 ? 2.962  30.346  -22.597 1.00 60.93  ?  180 GLN A OE1 1 
ATOM   1465 N NE2 . GLN A 1 181 ? 2.707  28.876  -24.288 1.00 62.75  ?  180 GLN A NE2 1 
ATOM   1466 N N   . ARG A 1 182 ? 1.365  30.532  -17.716 1.00 54.88  ?  181 ARG A N   1 
ATOM   1467 C CA  . ARG A 1 182 ? 0.996  31.575  -16.773 1.00 53.95  ?  181 ARG A CA  1 
ATOM   1468 C C   . ARG A 1 182 ? 2.200  32.440  -16.402 1.00 59.27  ?  181 ARG A C   1 
ATOM   1469 O O   . ARG A 1 182 ? 3.340  31.970  -16.367 1.00 58.20  ?  181 ARG A O   1 
ATOM   1470 C CB  . ARG A 1 182 ? 0.410  30.947  -15.505 1.00 60.55  ?  181 ARG A CB  1 
ATOM   1471 C CG  . ARG A 1 182 ? 1.482  30.591  -14.475 1.00 59.17  ?  181 ARG A CG  1 
ATOM   1472 C CD  . ARG A 1 182 ? 1.041  29.551  -13.443 1.00 58.29  ?  181 ARG A CD  1 
ATOM   1473 N NE  . ARG A 1 182 ? 2.212  28.806  -12.977 1.00 60.47  ?  181 ARG A NE  1 
ATOM   1474 C CZ  . ARG A 1 182 ? 2.532  28.622  -11.703 1.00 60.89  ?  181 ARG A CZ  1 
ATOM   1475 N NH1 . ARG A 1 182 ? 1.758  29.116  -10.739 1.00 65.41  ?  181 ARG A NH1 1 
ATOM   1476 N NH2 . ARG A 1 182 ? 3.624  27.933  -11.400 1.00 58.80  ?  181 ARG A NH2 1 
ATOM   1477 N N   . THR A 1 183 ? 1.935  33.723  -16.138 1.00 57.29  ?  182 THR A N   1 
ATOM   1478 C CA  . THR A 1 183 ? 2.902  34.632  -15.521 1.00 57.09  ?  182 THR A CA  1 
ATOM   1479 C C   . THR A 1 183 ? 2.226  35.237  -14.298 1.00 55.01  ?  182 THR A C   1 
ATOM   1480 O O   . THR A 1 183 ? 1.250  35.978  -14.437 1.00 58.34  ?  182 THR A O   1 
ATOM   1481 C CB  . THR A 1 183 ? 3.363  35.734  -16.477 1.00 55.29  ?  182 THR A CB  1 
ATOM   1482 O OG1 . THR A 1 183 ? 2.238  36.251  -17.198 1.00 67.88  ?  182 THR A OG1 1 
ATOM   1483 C CG2 . THR A 1 183 ? 4.385  35.205  -17.470 1.00 54.78  ?  182 THR A CG2 1 
ATOM   1484 N N   . ASP A 1 184 ? 2.722  34.902  -13.100 1.00 52.32  ?  183 ASP A N   1 
ATOM   1485 C CA  . ASP A 1 184 ? 2.172  35.437  -11.860 1.00 46.21  ?  183 ASP A CA  1 
ATOM   1486 C C   . ASP A 1 184 ? 3.046  36.592  -11.405 1.00 43.85  ?  183 ASP A C   1 
ATOM   1487 O O   . ASP A 1 184 ? 4.206  36.356  -11.035 1.00 37.31  ?  183 ASP A O   1 
ATOM   1488 C CB  . ASP A 1 184 ? 2.120  34.362  -10.774 1.00 47.77  ?  183 ASP A CB  1 
ATOM   1489 C CG  . ASP A 1 184 ? 1.120  33.250  -11.076 1.00 55.85  ?  183 ASP A CG  1 
ATOM   1490 O OD1 . ASP A 1 184 ? -0.079 33.555  -11.290 1.00 54.59  ?  183 ASP A OD1 1 
ATOM   1491 O OD2 . ASP A 1 184 ? 1.540  32.065  -11.060 1.00 50.24  -1 183 ASP A OD2 1 
ATOM   1492 N N   . PRO A 1 185 ? 2.564  37.843  -11.415 1.00 43.51  ?  184 PRO A N   1 
ATOM   1493 C CA  . PRO A 1 185 ? 3.415  38.968  -10.999 1.00 42.47  ?  184 PRO A CA  1 
ATOM   1494 C C   . PRO A 1 185 ? 3.665  38.929  -9.502  1.00 36.66  ?  184 PRO A C   1 
ATOM   1495 O O   . PRO A 1 185 ? 2.904  38.309  -8.741  1.00 35.15  ?  184 PRO A O   1 
ATOM   1496 C CB  . PRO A 1 185 ? 2.590  40.205  -11.399 1.00 43.20  ?  184 PRO A CB  1 
ATOM   1497 C CG  . PRO A 1 185 ? 1.170  39.751  -11.275 1.00 32.99  ?  184 PRO A CG  1 
ATOM   1498 C CD  . PRO A 1 185 ? 1.182  38.283  -11.697 1.00 43.11  ?  184 PRO A CD  1 
ATOM   1499 N N   . PRO A 1 186 ? 4.728  39.576  -9.034  1.00 42.58  ?  185 PRO A N   1 
ATOM   1500 C CA  . PRO A 1 186 ? 5.064  39.497  -7.608  1.00 36.57  ?  185 PRO A CA  1 
ATOM   1501 C C   . PRO A 1 186 ? 4.169  40.395  -6.774  1.00 37.66  ?  185 PRO A C   1 
ATOM   1502 O O   . PRO A 1 186 ? 3.922  41.549  -7.129  1.00 44.24  ?  185 PRO A O   1 
ATOM   1503 C CB  . PRO A 1 186 ? 6.509  40.000  -7.564  1.00 38.88  ?  185 PRO A CB  1 
ATOM   1504 C CG  . PRO A 1 186 ? 6.589  40.944  -8.733  1.00 38.70  ?  185 PRO A CG  1 
ATOM   1505 C CD  . PRO A 1 186 ? 5.730  40.334  -9.799  1.00 35.39  ?  185 PRO A CD  1 
ATOM   1506 N N   . LYS A 1 187 ? 3.705  39.862  -5.647  1.00 33.80  ?  186 LYS A N   1 
ATOM   1507 C CA  . LYS A 1 187 ? 3.090  40.686  -4.611  1.00 39.82  ?  186 LYS A CA  1 
ATOM   1508 C C   . LYS A 1 187 ? 4.201  41.239  -3.720  1.00 35.45  ?  186 LYS A C   1 
ATOM   1509 O O   . LYS A 1 187 ? 4.996  40.469  -3.174  1.00 33.83  ?  186 LYS A O   1 
ATOM   1510 C CB  . LYS A 1 187 ? 2.094  39.872  -3.788  1.00 37.25  ?  186 LYS A CB  1 
ATOM   1511 C CG  . LYS A 1 187 ? 1.035  39.099  -4.566  1.00 47.74  ?  186 LYS A CG  1 
ATOM   1512 C CD  . LYS A 1 187 ? 0.173  38.248  -3.594  1.00 50.06  ?  186 LYS A CD  1 
ATOM   1513 C CE  . LYS A 1 187 ? -0.862 37.381  -4.318  1.00 56.48  ?  186 LYS A CE  1 
ATOM   1514 N NZ  . LYS A 1 187 ? -1.950 38.219  -4.947  1.00 63.17  ?  186 LYS A NZ  1 
ATOM   1515 N N   . THR A 1 188 ? 4.279  42.556  -3.590  1.00 31.81  ?  187 THR A N   1 
ATOM   1516 C CA  . THR A 1 188 ? 5.434  43.204  -2.980  1.00 33.42  ?  187 THR A CA  1 
ATOM   1517 C C   . THR A 1 188 ? 5.040  43.966  -1.715  1.00 36.74  ?  187 THR A C   1 
ATOM   1518 O O   . THR A 1 188 ? 3.902  44.405  -1.560  1.00 34.12  ?  187 THR A O   1 
ATOM   1519 C CB  . THR A 1 188 ? 6.134  44.159  -3.970  1.00 41.11  ?  187 THR A CB  1 
ATOM   1520 O OG1 . THR A 1 188 ? 5.290  45.279  -4.256  1.00 41.91  ?  187 THR A OG1 1 
ATOM   1521 C CG2 . THR A 1 188 ? 6.490  43.451  -5.285  1.00 37.42  ?  187 THR A CG2 1 
ATOM   1522 N N   . HIS A 1 189 ? 5.992  44.090  -0.797  1.00 33.74  ?  188 HIS A N   1 
ATOM   1523 C CA  . HIS A 1 189 ? 5.841  44.902  0.410   1.00 39.35  ?  188 HIS A CA  1 
ATOM   1524 C C   . HIS A 1 189 ? 7.228  45.169  0.977   1.00 40.18  ?  188 HIS A C   1 
ATOM   1525 O O   . HIS A 1 189 ? 8.242  44.668  0.474   1.00 36.11  ?  188 HIS A O   1 
ATOM   1526 C CB  . HIS A 1 189 ? 4.933  44.246  1.463   1.00 34.60  ?  188 HIS A CB  1 
ATOM   1527 C CG  . HIS A 1 189 ? 5.471  42.975  2.055   1.00 35.42  ?  188 HIS A CG  1 
ATOM   1528 N ND1 . HIS A 1 189 ? 5.991  42.902  3.334   1.00 40.83  ?  188 HIS A ND1 1 
ATOM   1529 C CD2 . HIS A 1 189 ? 5.519  41.715  1.563   1.00 30.78  ?  188 HIS A CD2 1 
ATOM   1530 C CE1 . HIS A 1 189 ? 6.364  41.659  3.587   1.00 37.38  ?  188 HIS A CE1 1 
ATOM   1531 N NE2 . HIS A 1 189 ? 6.084  40.918  2.530   1.00 37.92  ?  188 HIS A NE2 1 
ATOM   1532 N N   . MET A 1 190 ? 7.264  45.945  2.054   1.00 38.75  ?  189 MET A N   1 
ATOM   1533 C CA  . MET A 1 190 ? 8.529  46.387  2.617   1.00 38.76  ?  189 MET A CA  1 
ATOM   1534 C C   . MET A 1 190 ? 8.457  46.358  4.136   1.00 40.77  ?  189 MET A C   1 
ATOM   1535 O O   . MET A 1 190 ? 7.458  46.790  4.713   1.00 42.81  ?  189 MET A O   1 
ATOM   1536 C CB  . MET A 1 190 ? 8.837  47.788  2.093   1.00 41.67  ?  189 MET A CB  1 
ATOM   1537 C CG  . MET A 1 190 ? 10.059 48.427  2.640   1.00 46.38  ?  189 MET A CG  1 
ATOM   1538 S SD  . MET A 1 190 ? 10.363 49.911  1.696   1.00 69.12  ?  189 MET A SD  1 
ATOM   1539 C CE  . MET A 1 190 ? 11.874 50.396  2.481   1.00 45.56  ?  189 MET A CE  1 
ATOM   1540 N N   . THR A 1 191 ? 9.487  45.823  4.782   1.00 36.06  ?  190 THR A N   1 
ATOM   1541 C CA  . THR A 1 191 ? 9.555  45.803  6.234   1.00 36.80  ?  190 THR A CA  1 
ATOM   1542 C C   . THR A 1 191 ? 10.667 46.727  6.711   1.00 39.83  ?  190 THR A C   1 
ATOM   1543 O O   . THR A 1 191 ? 11.536 47.137  5.936   1.00 36.87  ?  190 THR A O   1 
ATOM   1544 C CB  . THR A 1 191 ? 9.785  44.391  6.776   1.00 37.95  ?  190 THR A CB  1 
ATOM   1545 O OG1 . THR A 1 191 ? 11.035 43.897  6.288   1.00 40.55  ?  190 THR A OG1 1 
ATOM   1546 C CG2 . THR A 1 191 ? 8.645  43.455  6.371   1.00 41.18  ?  190 THR A CG2 1 
ATOM   1547 N N   . HIS A 1 192 ? 10.623 47.055  8.006   1.00 37.12  ?  191 HIS A N   1 
ATOM   1548 C CA  . HIS A 1 192 ? 11.513 48.045  8.614   1.00 37.10  ?  191 HIS A CA  1 
ATOM   1549 C C   . HIS A 1 192 ? 11.910 47.539  9.990   1.00 39.86  ?  191 HIS A C   1 
ATOM   1550 O O   . HIS A 1 192 ? 11.039 47.311  10.833  1.00 35.65  ?  191 HIS A O   1 
ATOM   1551 C CB  . HIS A 1 192 ? 10.823 49.415  8.723   1.00 34.42  ?  191 HIS A CB  1 
ATOM   1552 C CG  . HIS A 1 192 ? 11.630 50.456  9.443   1.00 38.04  ?  191 HIS A CG  1 
ATOM   1553 N ND1 . HIS A 1 192 ? 11.558 50.647  10.807  1.00 41.68  ?  191 HIS A ND1 1 
ATOM   1554 C CD2 . HIS A 1 192 ? 12.507 51.382  8.983   1.00 38.52  ?  191 HIS A CD2 1 
ATOM   1555 C CE1 . HIS A 1 192 ? 12.366 51.630  11.160  1.00 39.08  ?  191 HIS A CE1 1 
ATOM   1556 N NE2 . HIS A 1 192 ? 12.950 52.099  10.072  1.00 40.19  ?  191 HIS A NE2 1 
ATOM   1557 N N   . HIS A 1 193 ? 13.208 47.370  10.223  1.00 37.87  ?  192 HIS A N   1 
ATOM   1558 C CA  . HIS A 1 193 ? 13.697 46.804  11.480  1.00 43.05  ?  192 HIS A CA  1 
ATOM   1559 C C   . HIS A 1 193 ? 14.822 47.656  12.047  1.00 44.36  ?  192 HIS A C   1 
ATOM   1560 O O   . HIS A 1 193 ? 15.951 47.617  11.513  1.00 42.80  ?  192 HIS A O   1 
ATOM   1561 C CB  . HIS A 1 193 ? 14.166 45.363  11.286  1.00 46.48  ?  192 HIS A CB  1 
ATOM   1562 C CG  . HIS A 1 193 ? 13.087 44.432  10.824  1.00 46.76  ?  192 HIS A CG  1 
ATOM   1563 N ND1 . HIS A 1 193 ? 12.146 43.900  11.678  1.00 54.55  ?  192 HIS A ND1 1 
ATOM   1564 C CD2 . HIS A 1 193 ? 12.796 43.944  9.592   1.00 50.98  ?  192 HIS A CD2 1 
ATOM   1565 C CE1 . HIS A 1 193 ? 11.321 43.126  10.995  1.00 55.69  ?  192 HIS A CE1 1 
ATOM   1566 N NE2 . HIS A 1 193 ? 11.698 43.129  9.729   1.00 52.41  ?  192 HIS A NE2 1 
ATOM   1567 N N   . PRO A 1 194 ? 14.580 48.408  13.124  1.00 49.77  ?  193 PRO A N   1 
ATOM   1568 C CA  . PRO A 1 194 ? 15.676 49.137  13.774  1.00 50.62  ?  193 PRO A CA  1 
ATOM   1569 C C   . PRO A 1 194 ? 16.770 48.183  14.247  1.00 52.05  ?  193 PRO A C   1 
ATOM   1570 O O   . PRO A 1 194 ? 16.494 47.166  14.886  1.00 50.48  ?  193 PRO A O   1 
ATOM   1571 C CB  . PRO A 1 194 ? 14.979 49.838  14.950  1.00 51.76  ?  193 PRO A CB  1 
ATOM   1572 C CG  . PRO A 1 194 ? 13.495 49.855  14.582  1.00 42.42  ?  193 PRO A CG  1 
ATOM   1573 C CD  . PRO A 1 194 ? 13.305 48.564  13.850  1.00 43.71  ?  193 PRO A CD  1 
ATOM   1574 N N   . ILE A 1 195 ? 18.014 48.503  13.882  1.00 59.03  ?  194 ILE A N   1 
ATOM   1575 C CA  . ILE A 1 195 ? 19.219 47.843  14.401  1.00 57.49  ?  194 ILE A CA  1 
ATOM   1576 C C   . ILE A 1 195 ? 19.718 48.556  15.643  1.00 64.67  ?  194 ILE A C   1 
ATOM   1577 O O   . ILE A 1 195 ? 20.055 47.948  16.663  1.00 65.01  ?  194 ILE A O   1 
ATOM   1578 C CB  . ILE A 1 195 ? 20.340 47.862  13.333  1.00 61.84  ?  194 ILE A CB  1 
ATOM   1579 C CG1 . ILE A 1 195 ? 19.882 47.337  11.978  1.00 57.16  ?  194 ILE A CG1 1 
ATOM   1580 C CG2 . ILE A 1 195 ? 21.596 47.163  13.841  1.00 63.38  ?  194 ILE A CG2 1 
ATOM   1581 C CD1 . ILE A 1 195 ? 20.525 48.092  10.830  1.00 54.44  ?  194 ILE A CD1 1 
ATOM   1582 N N   . SER A 1 196 ? 19.799 49.869  15.526  1.00 65.73  ?  195 SER A N   1 
ATOM   1583 C CA  . SER A 1 196 ? 20.449 50.724  16.508  1.00 70.53  ?  195 SER A CA  1 
ATOM   1584 C C   . SER A 1 196 ? 19.394 51.700  17.012  1.00 73.79  ?  195 SER A C   1 
ATOM   1585 O O   . SER A 1 196 ? 18.181 51.469  16.908  1.00 75.71  ?  195 SER A O   1 
ATOM   1586 C CB  . SER A 1 196 ? 21.621 51.432  15.819  1.00 70.58  ?  195 SER A CB  1 
ATOM   1587 O OG  . SER A 1 196 ? 21.214 51.912  14.544  1.00 71.70  ?  195 SER A OG  1 
ATOM   1588 N N   . ASP A 1 197 ? 19.837 52.847  17.513  1.00 77.90  ?  196 ASP A N   1 
ATOM   1589 C CA  . ASP A 1 197 ? 19.000 54.037  17.446  1.00 77.40  ?  196 ASP A CA  1 
ATOM   1590 C C   . ASP A 1 197 ? 19.398 54.926  16.275  1.00 75.45  ?  196 ASP A C   1 
ATOM   1591 O O   . ASP A 1 197 ? 18.726 55.930  16.005  1.00 79.66  ?  196 ASP A O   1 
ATOM   1592 C CB  . ASP A 1 197 ? 19.045 54.832  18.760  1.00 80.86  ?  196 ASP A CB  1 
ATOM   1593 C CG  . ASP A 1 197 ? 20.445 54.916  19.355  1.00 93.42  ?  196 ASP A CG  1 
ATOM   1594 O OD1 . ASP A 1 197 ? 21.022 53.856  19.693  1.00 93.05  ?  196 ASP A OD1 1 
ATOM   1595 O OD2 . ASP A 1 197 ? 20.974 56.043  19.484  1.00 101.88 -1 196 ASP A OD2 1 
ATOM   1596 N N   . HIS A 1 198 ? 20.468 54.558  15.565  1.00 72.25  ?  197 HIS A N   1 
ATOM   1597 C CA  . HIS A 1 198 ? 20.939 55.294  14.403  1.00 70.89  ?  197 HIS A CA  1 
ATOM   1598 C C   . HIS A 1 198 ? 20.741 54.563  13.078  1.00 61.53  ?  197 HIS A C   1 
ATOM   1599 O O   . HIS A 1 198 ? 20.815 55.210  12.028  1.00 60.88  ?  197 HIS A O   1 
ATOM   1600 C CB  . HIS A 1 198 ? 22.432 55.655  14.559  1.00 75.26  ?  197 HIS A CB  1 
ATOM   1601 C CG  . HIS A 1 198 ? 23.260 54.607  15.250  1.00 79.75  ?  197 HIS A CG  1 
ATOM   1602 N ND1 . HIS A 1 198 ? 23.156 54.338  16.601  1.00 84.73  ?  197 HIS A ND1 1 
ATOM   1603 C CD2 . HIS A 1 198 ? 24.227 53.781  14.779  1.00 80.11  ?  197 HIS A CD2 1 
ATOM   1604 C CE1 . HIS A 1 198 ? 24.008 53.381  16.926  1.00 81.97  ?  197 HIS A CE1 1 
ATOM   1605 N NE2 . HIS A 1 198 ? 24.671 53.025  15.839  1.00 80.96  ?  197 HIS A NE2 1 
ATOM   1606 N N   . GLU A 1 199 ? 20.478 53.250  13.095  1.00 62.83  ?  198 GLU A N   1 
ATOM   1607 C CA  . GLU A 1 199 ? 20.391 52.438  11.882  1.00 61.68  ?  198 GLU A CA  1 
ATOM   1608 C C   . GLU A 1 199 ? 19.114 51.607  11.878  1.00 57.00  ?  198 GLU A C   1 
ATOM   1609 O O   . GLU A 1 199 ? 18.619 51.187  12.929  1.00 55.57  ?  198 GLU A O   1 
ATOM   1610 C CB  . GLU A 1 199 ? 21.590 51.462  11.734  1.00 58.30  ?  198 GLU A CB  1 
ATOM   1611 C CG  . GLU A 1 199 ? 22.950 52.108  11.645  1.00 61.66  ?  198 GLU A CG  1 
ATOM   1612 C CD  . GLU A 1 199 ? 24.069 51.139  11.964  1.00 68.11  ?  198 GLU A CD  1 
ATOM   1613 O OE1 . GLU A 1 199 ? 24.145 50.641  13.114  1.00 68.48  ?  198 GLU A OE1 1 
ATOM   1614 O OE2 . GLU A 1 199 ? 24.871 50.870  11.051  1.00 70.90  -1 198 GLU A OE2 1 
ATOM   1615 N N   . ALA A 1 200 ? 18.611 51.333  10.676  1.00 47.67  ?  199 ALA A N   1 
ATOM   1616 C CA  . ALA A 1 200 ? 17.491 50.419  10.519  1.00 51.53  ?  199 ALA A CA  1 
ATOM   1617 C C   . ALA A 1 200 ? 17.653 49.643  9.213   1.00 47.85  ?  199 ALA A C   1 
ATOM   1618 O O   . ALA A 1 200 ? 18.193 50.160  8.231   1.00 43.84  ?  199 ALA A O   1 
ATOM   1619 C CB  . ALA A 1 200 ? 16.154 51.178  10.548  1.00 43.85  ?  199 ALA A CB  1 
ATOM   1620 N N   . THR A 1 201 ? 17.180 48.398  9.219   1.00 38.63  ?  200 THR A N   1 
ATOM   1621 C CA  . THR A 1 201 ? 17.113 47.562  8.023   1.00 39.82  ?  200 THR A CA  1 
ATOM   1622 C C   . THR A 1 201 ? 15.796 47.825  7.300   1.00 40.71  ?  200 THR A C   1 
ATOM   1623 O O   . THR A 1 201 ? 14.727 47.686  7.902   1.00 39.41  ?  200 THR A O   1 
ATOM   1624 C CB  . THR A 1 201 ? 17.200 46.075  8.392   1.00 48.07  ?  200 THR A CB  1 
ATOM   1625 O OG1 . THR A 1 201 ? 18.493 45.762  8.923   1.00 43.82  ?  200 THR A OG1 1 
ATOM   1626 C CG2 . THR A 1 201 ? 16.915 45.174  7.167   1.00 46.03  ?  200 THR A CG2 1 
ATOM   1627 N N   . LEU A 1 202 ? 15.874 48.238  6.031   1.00 36.19  ?  201 LEU A N   1 
ATOM   1628 C CA  . LEU A 1 202 ? 14.750 48.215  5.102   1.00 31.84  ?  201 LEU A CA  1 
ATOM   1629 C C   . LEU A 1 202 ? 14.836 46.947  4.254   1.00 40.05  ?  201 LEU A C   1 
ATOM   1630 O O   . LEU A 1 202 ? 15.864 46.692  3.618   1.00 39.34  ?  201 LEU A O   1 
ATOM   1631 C CB  . LEU A 1 202 ? 14.751 49.440  4.182   1.00 34.99  ?  201 LEU A CB  1 
ATOM   1632 C CG  . LEU A 1 202 ? 14.286 50.788  4.739   1.00 45.81  ?  201 LEU A CG  1 
ATOM   1633 C CD1 . LEU A 1 202 ? 14.293 51.855  3.633   1.00 40.68  ?  201 LEU A CD1 1 
ATOM   1634 C CD2 . LEU A 1 202 ? 12.905 50.688  5.444   1.00 40.17  ?  201 LEU A CD2 1 
ATOM   1635 N N   . ARG A 1 203 ? 13.764 46.157  4.228   1.00 37.90  ?  202 ARG A N   1 
ATOM   1636 C CA  . ARG A 1 203 ? 13.742 44.925  3.446   1.00 41.83  ?  202 ARG A CA  1 
ATOM   1637 C C   . ARG A 1 203 ? 12.588 44.972  2.451   1.00 37.53  ?  202 ARG A C   1 
ATOM   1638 O O   . ARG A 1 203 ? 11.435 45.189  2.838   1.00 35.95  ?  202 ARG A O   1 
ATOM   1639 C CB  . ARG A 1 203 ? 13.644 43.693  4.362   1.00 31.95  ?  202 ARG A CB  1 
ATOM   1640 C CG  . ARG A 1 203 ? 13.625 42.384  3.592   1.00 39.06  ?  202 ARG A CG  1 
ATOM   1641 C CD  . ARG A 1 203 ? 13.823 41.161  4.496   1.00 40.76  ?  202 ARG A CD  1 
ATOM   1642 N NE  . ARG A 1 203 ? 15.200 41.089  4.972   1.00 41.49  ?  202 ARG A NE  1 
ATOM   1643 C CZ  . ARG A 1 203 ? 15.573 41.299  6.231   1.00 46.75  ?  202 ARG A CZ  1 
ATOM   1644 N NH1 . ARG A 1 203 ? 14.660 41.581  7.160   1.00 44.82  ?  202 ARG A NH1 1 
ATOM   1645 N NH2 . ARG A 1 203 ? 16.861 41.232  6.551   1.00 42.12  ?  202 ARG A NH2 1 
ATOM   1646 N N   . CYS A 1 204 ? 12.907 44.773  1.176   1.00 34.59  ?  203 CYS A N   1 
ATOM   1647 C CA  . CYS A 1 204 ? 11.967 44.820  0.062   1.00 37.87  ?  203 CYS A CA  1 
ATOM   1648 C C   . CYS A 1 204 ? 11.628 43.398  -0.379  1.00 39.75  ?  203 CYS A C   1 
ATOM   1649 O O   . CYS A 1 204 ? 12.522 42.657  -0.812  1.00 38.66  ?  203 CYS A O   1 
ATOM   1650 C CB  . CYS A 1 204 ? 12.589 45.606  -1.089  1.00 37.00  ?  203 CYS A CB  1 
ATOM   1651 S SG  . CYS A 1 204 ? 11.515 45.763  -2.502  1.00 47.78  ?  203 CYS A SG  1 
ATOM   1652 N N   . TRP A 1 205 ? 10.348 43.020  -0.298  1.00 37.78  ?  204 TRP A N   1 
ATOM   1653 C CA  . TRP A 1 205 ? 9.903  41.639  -0.456  1.00 31.67  ?  204 TRP A CA  1 
ATOM   1654 C C   . TRP A 1 205 ? 9.133  41.454  -1.762  1.00 37.31  ?  204 TRP A C   1 
ATOM   1655 O O   . TRP A 1 205 ? 8.324  42.304  -2.148  1.00 32.47  ?  204 TRP A O   1 
ATOM   1656 C CB  . TRP A 1 205 ? 8.993  41.208  0.697   1.00 28.09  ?  204 TRP A CB  1 
ATOM   1657 C CG  . TRP A 1 205 ? 9.651  40.822  1.980   1.00 39.27  ?  204 TRP A CG  1 
ATOM   1658 C CD1 . TRP A 1 205 ? 9.913  41.632  3.054   1.00 36.36  ?  204 TRP A CD1 1 
ATOM   1659 C CD2 . TRP A 1 205 ? 10.056 39.510  2.362   1.00 38.78  ?  204 TRP A CD2 1 
ATOM   1660 N NE1 . TRP A 1 205 ? 10.491 40.905  4.056   1.00 38.31  ?  204 TRP A NE1 1 
ATOM   1661 C CE2 . TRP A 1 205 ? 10.580 39.597  3.663   1.00 38.70  ?  204 TRP A CE2 1 
ATOM   1662 C CE3 . TRP A 1 205 ? 10.034 38.264  1.723   1.00 43.46  ?  204 TRP A CE3 1 
ATOM   1663 C CZ2 . TRP A 1 205 ? 11.094 38.493  4.330   1.00 42.73  ?  204 TRP A CZ2 1 
ATOM   1664 C CZ3 . TRP A 1 205 ? 10.526 37.164  2.395   1.00 42.12  ?  204 TRP A CZ3 1 
ATOM   1665 C CH2 . TRP A 1 205 ? 11.053 37.286  3.683   1.00 47.03  ?  204 TRP A CH2 1 
ATOM   1666 N N   . ALA A 1 206 ? 9.361  40.325  -2.424  1.00 35.59  ?  205 ALA A N   1 
ATOM   1667 C CA  . ALA A 1 206 ? 8.653  39.958  -3.646  1.00 38.41  ?  205 ALA A CA  1 
ATOM   1668 C C   . ALA A 1 206 ? 8.159  38.541  -3.426  1.00 35.70  ?  205 ALA A C   1 
ATOM   1669 O O   . ALA A 1 206 ? 8.957  37.653  -3.127  1.00 34.81  ?  205 ALA A O   1 
ATOM   1670 C CB  . ALA A 1 206 ? 9.563  40.052  -4.875  1.00 36.55  ?  205 ALA A CB  1 
ATOM   1671 N N   . LEU A 1 207 ? 6.859  38.329  -3.536  1.00 36.50  ?  206 LEU A N   1 
ATOM   1672 C CA  . LEU A 1 207 ? 6.281  37.033  -3.231  1.00 33.23  ?  206 LEU A CA  1 
ATOM   1673 C C   . LEU A 1 207 ? 5.345  36.570  -4.341  1.00 36.93  ?  206 LEU A C   1 
ATOM   1674 O O   . LEU A 1 207 ? 4.790  37.375  -5.093  1.00 39.22  ?  206 LEU A O   1 
ATOM   1675 C CB  . LEU A 1 207 ? 5.489  37.066  -1.920  1.00 39.34  ?  206 LEU A CB  1 
ATOM   1676 C CG  . LEU A 1 207 ? 6.208  37.445  -0.626  1.00 44.56  ?  206 LEU A CG  1 
ATOM   1677 C CD1 . LEU A 1 207 ? 5.225  37.539  0.577   1.00 44.94  ?  206 LEU A CD1 1 
ATOM   1678 C CD2 . LEU A 1 207 ? 7.330  36.443  -0.330  1.00 35.92  ?  206 LEU A CD2 1 
ATOM   1679 N N   . GLY A 1 208 ? 5.185  35.253  -4.428  1.00 31.96  ?  207 GLY A N   1 
ATOM   1680 C CA  . GLY A 1 208 ? 4.164  34.640  -5.249  1.00 38.51  ?  207 GLY A CA  1 
ATOM   1681 C C   . GLY A 1 208 ? 4.339  34.801  -6.738  1.00 42.34  ?  207 GLY A C   1 
ATOM   1682 O O   . GLY A 1 208 ? 3.338  34.805  -7.466  1.00 40.71  ?  207 GLY A O   1 
ATOM   1683 N N   . PHE A 1 209 ? 5.572  34.940  -7.225  1.00 37.13  ?  208 PHE A N   1 
ATOM   1684 C CA  . PHE A 1 209 ? 5.785  35.231  -8.635  1.00 37.45  ?  208 PHE A CA  1 
ATOM   1685 C C   . PHE A 1 209 ? 6.280  33.978  -9.375  1.00 42.66  ?  208 PHE A C   1 
ATOM   1686 O O   . PHE A 1 209 ? 6.885  33.072  -8.789  1.00 37.69  ?  208 PHE A O   1 
ATOM   1687 C CB  . PHE A 1 209 ? 6.722  36.446  -8.817  1.00 37.77  ?  208 PHE A CB  1 
ATOM   1688 C CG  . PHE A 1 209 ? 8.079  36.286  -8.198  1.00 40.99  ?  208 PHE A CG  1 
ATOM   1689 C CD1 . PHE A 1 209 ? 8.292  36.604  -6.867  1.00 37.41  ?  208 PHE A CD1 1 
ATOM   1690 C CD2 . PHE A 1 209 ? 9.153  35.826  -8.955  1.00 38.09  ?  208 PHE A CD2 1 
ATOM   1691 C CE1 . PHE A 1 209 ? 9.556  36.448  -6.285  1.00 37.71  ?  208 PHE A CE1 1 
ATOM   1692 C CE2 . PHE A 1 209 ? 10.416 35.654  -8.382  1.00 40.04  ?  208 PHE A CE2 1 
ATOM   1693 C CZ  . PHE A 1 209 ? 10.615 35.970  -7.040  1.00 37.79  ?  208 PHE A CZ  1 
ATOM   1694 N N   . TYR A 1 210 ? 5.914  33.896  -10.659 1.00 42.28  ?  209 TYR A N   1 
ATOM   1695 C CA  . TYR A 1 210 ? 6.265  32.789  -11.565 1.00 44.27  ?  209 TYR A CA  1 
ATOM   1696 C C   . TYR A 1 210 ? 6.308  33.456  -12.933 1.00 44.99  ?  209 TYR A C   1 
ATOM   1697 O O   . TYR A 1 210 ? 5.335  34.135  -13.290 1.00 38.51  ?  209 TYR A O   1 
ATOM   1698 C CB  . TYR A 1 210 ? 5.276  31.629  -11.601 1.00 48.80  ?  209 TYR A CB  1 
ATOM   1699 C CG  . TYR A 1 210 ? 5.749  30.501  -12.508 1.00 50.55  ?  209 TYR A CG  1 
ATOM   1700 C CD1 . TYR A 1 210 ? 5.574  30.554  -13.895 1.00 42.53  ?  209 TYR A CD1 1 
ATOM   1701 C CD2 . TYR A 1 210 ? 6.397  29.396  -11.971 1.00 50.86  ?  209 TYR A CD2 1 
ATOM   1702 C CE1 . TYR A 1 210 ? 6.026  29.517  -14.715 1.00 47.73  ?  209 TYR A CE1 1 
ATOM   1703 C CE2 . TYR A 1 210 ? 6.841  28.359  -12.773 1.00 52.03  ?  209 TYR A CE2 1 
ATOM   1704 C CZ  . TYR A 1 210 ? 6.666  28.425  -14.145 1.00 50.51  ?  209 TYR A CZ  1 
ATOM   1705 O OH  . TYR A 1 210 ? 7.130  27.374  -14.914 1.00 52.20  ?  209 TYR A OH  1 
ATOM   1706 N N   . PRO A 1 211 ? 7.383  33.280  -13.726 1.00 45.79  ?  210 PRO A N   1 
ATOM   1707 C CA  . PRO A 1 211 ? 8.568  32.473  -13.417 1.00 46.76  ?  210 PRO A CA  1 
ATOM   1708 C C   . PRO A 1 211 ? 9.570  33.180  -12.484 1.00 48.09  ?  210 PRO A C   1 
ATOM   1709 O O   . PRO A 1 211 ? 9.378  34.345  -12.073 1.00 39.23  ?  210 PRO A O   1 
ATOM   1710 C CB  . PRO A 1 211 ? 9.183  32.244  -14.794 1.00 48.83  ?  210 PRO A CB  1 
ATOM   1711 C CG  . PRO A 1 211 ? 8.918  33.549  -15.500 1.00 50.76  ?  210 PRO A CG  1 
ATOM   1712 C CD  . PRO A 1 211 ? 7.529  33.970  -15.021 1.00 48.46  ?  210 PRO A CD  1 
ATOM   1713 N N   . ALA A 1 212 ? 10.652 32.452  -12.176 1.00 42.30  ?  211 ALA A N   1 
ATOM   1714 C CA  . ALA A 1 212 ? 11.527 32.830  -11.074 1.00 41.60  ?  211 ALA A CA  1 
ATOM   1715 C C   . ALA A 1 212 ? 12.339 34.068  -11.402 1.00 43.50  ?  211 ALA A C   1 
ATOM   1716 O O   . ALA A 1 212 ? 12.735 34.807  -10.493 1.00 44.70  ?  211 ALA A O   1 
ATOM   1717 C CB  . ALA A 1 212 ? 12.454 31.661  -10.719 1.00 40.39  ?  211 ALA A CB  1 
ATOM   1718 N N   . GLU A 1 213 ? 12.594 34.321  -12.680 1.00 39.33  ?  212 GLU A N   1 
ATOM   1719 C CA  . GLU A 1 213 ? 13.464 35.433  -13.040 1.00 47.62  ?  212 GLU A CA  1 
ATOM   1720 C C   . GLU A 1 213 ? 12.879 36.738  -12.501 1.00 45.18  ?  212 GLU A C   1 
ATOM   1721 O O   . GLU A 1 213 ? 11.678 36.986  -12.621 1.00 42.83  ?  212 GLU A O   1 
ATOM   1722 C CB  . GLU A 1 213 ? 13.636 35.494  -14.555 1.00 38.28  ?  212 GLU A CB  1 
ATOM   1723 C CG  . GLU A 1 213 ? 14.420 36.720  -15.033 1.00 51.01  ?  212 GLU A CG  1 
ATOM   1724 C CD  . GLU A 1 213 ? 15.864 36.755  -14.530 1.00 65.20  ?  212 GLU A CD  1 
ATOM   1725 O OE1 . GLU A 1 213 ? 16.343 35.732  -13.972 1.00 67.31  ?  212 GLU A OE1 1 
ATOM   1726 O OE2 . GLU A 1 213 ? 16.515 37.818  -14.694 1.00 68.59  -1 212 GLU A OE2 1 
ATOM   1727 N N   . ILE A 1 214 ? 13.730 37.578  -11.902 1.00 47.71  ?  213 ILE A N   1 
ATOM   1728 C CA  . ILE A 1 214 ? 13.274 38.788  -11.217 1.00 49.40  ?  213 ILE A CA  1 
ATOM   1729 C C   . ILE A 1 214 ? 14.471 39.673  -10.878 1.00 50.34  ?  213 ILE A C   1 
ATOM   1730 O O   . ILE A 1 214 ? 15.601 39.193  -10.731 1.00 52.41  ?  213 ILE A O   1 
ATOM   1731 C CB  . ILE A 1 214 ? 12.449 38.435  -9.952  1.00 36.75  ?  213 ILE A CB  1 
ATOM   1732 C CG1 . ILE A 1 214 ? 11.567 39.621  -9.520  1.00 49.27  ?  213 ILE A CG1 1 
ATOM   1733 C CG2 . ILE A 1 214 ? 13.353 38.013  -8.817  1.00 43.95  ?  213 ILE A CG2 1 
ATOM   1734 C CD1 . ILE A 1 214 ? 10.398 39.256  -8.552  1.00 37.62  ?  213 ILE A CD1 1 
ATOM   1735 N N   . THR A 1 215 ? 14.244 40.980  -10.786 1.00 49.25  ?  214 THR A N   1 
ATOM   1736 C CA  . THR A 1 215 ? 15.293 41.905  -10.386 1.00 50.94  ?  214 THR A CA  1 
ATOM   1737 C C   . THR A 1 215 ? 14.768 42.828  -9.289  1.00 52.52  ?  214 THR A C   1 
ATOM   1738 O O   . THR A 1 215 ? 13.699 43.430  -9.432  1.00 46.89  ?  214 THR A O   1 
ATOM   1739 C CB  . THR A 1 215 ? 15.796 42.682  -11.606 1.00 52.64  ?  214 THR A CB  1 
ATOM   1740 O OG1 . THR A 1 215 ? 16.244 41.745  -12.601 1.00 57.88  ?  214 THR A OG1 1 
ATOM   1741 C CG2 . THR A 1 215 ? 16.955 43.596  -11.238 1.00 46.06  ?  214 THR A CG2 1 
ATOM   1742 N N   . LEU A 1 216 ? 15.510 42.905  -8.184  1.00 48.74  ?  215 LEU A N   1 
ATOM   1743 C CA  . LEU A 1 216 ? 15.200 43.765  -7.043  1.00 52.43  ?  215 LEU A CA  1 
ATOM   1744 C C   . LEU A 1 216 ? 16.391 44.679  -6.813  1.00 54.10  ?  215 LEU A C   1 
ATOM   1745 O O   . LEU A 1 216 ? 17.455 44.216  -6.385  1.00 49.45  ?  215 LEU A O   1 
ATOM   1746 C CB  . LEU A 1 216 ? 14.927 42.951  -5.778  1.00 46.56  ?  215 LEU A CB  1 
ATOM   1747 C CG  . LEU A 1 216 ? 13.754 41.981  -5.743  1.00 47.74  ?  215 LEU A CG  1 
ATOM   1748 C CD1 . LEU A 1 216 ? 13.470 41.560  -4.307  1.00 44.17  ?  215 LEU A CD1 1 
ATOM   1749 C CD2 . LEU A 1 216 ? 12.530 42.598  -6.379  1.00 39.00  ?  215 LEU A CD2 1 
ATOM   1750 N N   . THR A 1 217 ? 16.210 45.973  -7.058  1.00 50.72  ?  216 THR A N   1 
ATOM   1751 C CA  . THR A 1 217 ? 17.282 46.944  -6.901  1.00 53.72  ?  216 THR A CA  1 
ATOM   1752 C C   . THR A 1 217 ? 16.876 48.045  -5.922  1.00 52.72  ?  216 THR A C   1 
ATOM   1753 O O   . THR A 1 217 ? 15.702 48.427  -5.845  1.00 51.36  ?  216 THR A O   1 
ATOM   1754 C CB  . THR A 1 217 ? 17.677 47.537  -8.273  1.00 54.46  ?  216 THR A CB  1 
ATOM   1755 O OG1 . THR A 1 217 ? 18.474 48.716  -8.090  1.00 63.48  ?  216 THR A OG1 1 
ATOM   1756 C CG2 . THR A 1 217 ? 16.444 47.877  -9.106  1.00 57.30  ?  216 THR A CG2 1 
ATOM   1757 N N   . TRP A 1 218 ? 17.850 48.524  -5.153  1.00 51.70  ?  217 TRP A N   1 
ATOM   1758 C CA  . TRP A 1 218 ? 17.696 49.692  -4.300  1.00 56.96  ?  217 TRP A CA  1 
ATOM   1759 C C   . TRP A 1 218 ? 18.277 50.932  -4.972  1.00 62.23  ?  217 TRP A C   1 
ATOM   1760 O O   . TRP A 1 218 ? 19.235 50.853  -5.742  1.00 68.46  ?  217 TRP A O   1 
ATOM   1761 C CB  . TRP A 1 218 ? 18.389 49.483  -2.954  1.00 55.83  ?  217 TRP A CB  1 
ATOM   1762 C CG  . TRP A 1 218 ? 17.599 48.640  -2.011  1.00 58.61  ?  217 TRP A CG  1 
ATOM   1763 C CD1 . TRP A 1 218 ? 17.861 47.353  -1.648  1.00 53.58  ?  217 TRP A CD1 1 
ATOM   1764 C CD2 . TRP A 1 218 ? 16.402 49.018  -1.314  1.00 57.43  ?  217 TRP A CD2 1 
ATOM   1765 N NE1 . TRP A 1 218 ? 16.907 46.908  -0.767  1.00 51.01  ?  217 TRP A NE1 1 
ATOM   1766 C CE2 . TRP A 1 218 ? 15.999 47.909  -0.548  1.00 51.38  ?  217 TRP A CE2 1 
ATOM   1767 C CE3 . TRP A 1 218 ? 15.635 50.189  -1.265  1.00 54.89  ?  217 TRP A CE3 1 
ATOM   1768 C CZ2 . TRP A 1 218 ? 14.863 47.933  0.268   1.00 50.91  ?  217 TRP A CZ2 1 
ATOM   1769 C CZ3 . TRP A 1 218 ? 14.508 50.212  -0.461  1.00 54.54  ?  217 TRP A CZ3 1 
ATOM   1770 C CH2 . TRP A 1 218 ? 14.134 49.088  0.299   1.00 49.57  ?  217 TRP A CH2 1 
ATOM   1771 N N   . GLN A 1 219 ? 17.688 52.082  -4.669  1.00 58.74  ?  218 GLN A N   1 
ATOM   1772 C CA  . GLN A 1 219 ? 18.229 53.374  -5.064  1.00 63.94  ?  218 GLN A CA  1 
ATOM   1773 C C   . GLN A 1 219 ? 18.268 54.272  -3.843  1.00 62.83  ?  218 GLN A C   1 
ATOM   1774 O O   . GLN A 1 219 ? 17.439 54.142  -2.939  1.00 61.86  ?  218 GLN A O   1 
ATOM   1775 C CB  . GLN A 1 219 ? 17.396 54.050  -6.166  1.00 61.74  ?  218 GLN A CB  1 
ATOM   1776 C CG  . GLN A 1 219 ? 17.279 53.220  -7.434  1.00 67.58  ?  218 GLN A CG  1 
ATOM   1777 C CD  . GLN A 1 219 ? 16.703 53.998  -8.609  1.00 72.14  ?  218 GLN A CD  1 
ATOM   1778 O OE1 . GLN A 1 219 ? 16.832 53.584  -9.760  1.00 75.01  ?  218 GLN A OE1 1 
ATOM   1779 N NE2 . GLN A 1 219 ? 16.054 55.124  -8.321  1.00 72.00  ?  218 GLN A NE2 1 
ATOM   1780 N N   . ARG A 1 220 ? 19.248 55.172  -3.813  1.00 64.18  ?  219 ARG A N   1 
ATOM   1781 C CA  . ARG A 1 220 ? 19.314 56.226  -2.807  1.00 62.03  ?  219 ARG A CA  1 
ATOM   1782 C C   . ARG A 1 220 ? 19.264 57.571  -3.518  1.00 66.38  ?  219 ARG A C   1 
ATOM   1783 O O   . ARG A 1 220 ? 20.183 57.920  -4.269  1.00 62.30  ?  219 ARG A O   1 
ATOM   1784 C CB  . ARG A 1 220 ? 20.563 56.128  -1.941  1.00 61.51  ?  219 ARG A CB  1 
ATOM   1785 C CG  . ARG A 1 220 ? 20.628 57.266  -0.943  1.00 60.28  ?  219 ARG A CG  1 
ATOM   1786 C CD  . ARG A 1 220 ? 22.000 57.407  -0.343  1.00 63.39  ?  219 ARG A CD  1 
ATOM   1787 N NE  . ARG A 1 220 ? 21.932 57.349  1.109   1.00 73.36  ?  219 ARG A NE  1 
ATOM   1788 C CZ  . ARG A 1 220 ? 21.564 58.364  1.886   1.00 74.98  ?  219 ARG A CZ  1 
ATOM   1789 N NH1 . ARG A 1 220 ? 21.533 58.199  3.204   1.00 69.78  ?  219 ARG A NH1 1 
ATOM   1790 N NH2 . ARG A 1 220 ? 21.226 59.538  1.352   1.00 72.62  ?  219 ARG A NH2 1 
ATOM   1791 N N   . ASP A 1 221 ? 18.199 58.324  -3.300  1.00 61.20  ?  220 ASP A N   1 
ATOM   1792 C CA  . ASP A 1 221 ? 18.025 59.635  -3.972  1.00 66.74  ?  220 ASP A CA  1 
ATOM   1793 C C   . ASP A 1 221 ? 18.082 59.422  -5.484  1.00 70.41  ?  220 ASP A C   1 
ATOM   1794 O O   . ASP A 1 221 ? 18.694 60.214  -6.146  1.00 77.37  ?  220 ASP A O   1 
ATOM   1795 C CB  . ASP A 1 221 ? 18.931 60.733  -3.414  1.00 60.94  ?  220 ASP A CB  1 
ATOM   1796 C CG  . ASP A 1 221 ? 18.577 61.102  -1.989  1.00 72.24  ?  220 ASP A CG  1 
ATOM   1797 O OD1 . ASP A 1 221 ? 17.397 61.331  -1.743  1.00 72.65  -1 220 ASP A OD1 1 
ATOM   1798 O OD2 . ASP A 1 221 ? 19.483 61.150  -1.139  1.00 72.47  ?  220 ASP A OD2 1 
ATOM   1799 N N   . GLY A 1 222 ? 17.515 58.322  -5.982  1.00 70.75  ?  221 GLY A N   1 
ATOM   1800 C CA  . GLY A 1 222 ? 17.425 58.039  -7.428  1.00 73.23  ?  221 GLY A CA  1 
ATOM   1801 C C   . GLY A 1 222 ? 18.684 57.444  -8.041  1.00 77.25  ?  221 GLY A C   1 
ATOM   1802 O O   . GLY A 1 222 ? 18.650 57.145  -9.227  1.00 80.33  ?  221 GLY A O   1 
ATOM   1803 N N   . GLU A 1 223 ? 19.739 57.292  -7.245  1.00 75.40  ?  222 GLU A N   1 
ATOM   1804 C CA  . GLU A 1 223 ? 21.061 56.755  -7.622  1.00 76.03  ?  222 GLU A CA  1 
ATOM   1805 C C   . GLU A 1 223 ? 21.117 55.317  -7.145  1.00 74.70  ?  222 GLU A C   1 
ATOM   1806 O O   . GLU A 1 223 ? 20.908 55.110  -5.965  1.00 75.64  ?  222 GLU A O   1 
ATOM   1807 C CB  . GLU A 1 223 ? 22.102 57.515  -6.801  1.00 30.00  ?  222 GLU A CB  1 
ATOM   1808 C CG  . GLU A 1 223 ? 23.547 57.210  -7.114  1.00 30.00  ?  222 GLU A CG  1 
ATOM   1809 C CD  . GLU A 1 223 ? 24.319 58.421  -7.604  1.00 30.00  ?  222 GLU A CD  1 
ATOM   1810 O OE1 . GLU A 1 223 ? 24.751 58.398  -8.765  1.00 30.00  ?  222 GLU A OE1 1 
ATOM   1811 O OE2 . GLU A 1 223 ? 24.446 59.398  -6.828  1.00 30.00  ?  222 GLU A OE2 1 
ATOM   1812 N N   . ASP A 1 224 ? 21.489 54.387  -8.021  1.00 89.97  ?  223 ASP A N   1 
ATOM   1813 C CA  . ASP A 1 224 ? 21.581 52.940  -7.676  1.00 82.25  ?  223 ASP A CA  1 
ATOM   1814 C C   . ASP A 1 224 ? 22.407 52.740  -6.409  1.00 76.27  ?  223 ASP A C   1 
ATOM   1815 O O   . ASP A 1 224 ? 23.471 53.310  -6.314  1.00 77.27  ?  223 ASP A O   1 
ATOM   1816 C CB  . ASP A 1 224 ? 22.083 52.123  -8.863  1.00 82.58  ?  223 ASP A CB  1 
ATOM   1817 C CG  . ASP A 1 224 ? 21.108 52.127  -10.024 1.00 89.36  ?  223 ASP A CG  1 
ATOM   1818 O OD1 . ASP A 1 224 ? 20.183 51.302  -9.992  1.00 89.12  ?  223 ASP A OD1 1 
ATOM   1819 O OD2 . ASP A 1 224 ? 21.288 52.946  -10.950 1.00 89.22  ?  223 ASP A OD2 1 
ATOM   1820 N N   . GLN A 1 225 ? 21.912 51.927  -5.485  1.00 76.56  ?  224 GLN A N   1 
ATOM   1821 C CA  . GLN A 1 225 ? 22.590 51.703  -4.182  1.00 79.89  ?  224 GLN A CA  1 
ATOM   1822 C C   . GLN A 1 225 ? 23.305 50.368  -4.228  1.00 81.24  ?  224 GLN A C   1 
ATOM   1823 O O   . GLN A 1 225 ? 22.699 49.329  -4.025  1.00 77.84  ?  224 GLN A O   1 
ATOM   1824 C CB  . GLN A 1 225 ? 21.628 51.753  -2.996  1.00 74.33  ?  224 GLN A CB  1 
ATOM   1825 C CG  . GLN A 1 225 ? 22.322 51.755  -1.652  1.00 73.79  ?  224 GLN A CG  1 
ATOM   1826 C CD  . GLN A 1 225 ? 23.248 52.936  -1.535  1.00 78.43  ?  224 GLN A CD  1 
ATOM   1827 O OE1 . GLN A 1 225 ? 23.539 53.595  -2.512  1.00 79.80  ?  224 GLN A OE1 1 
ATOM   1828 N NE2 . GLN A 1 225 ? 23.724 53.207  -0.339  1.00 73.74  ?  224 GLN A NE2 1 
ATOM   1829 N N   . THR A 1 226 ? 24.591 50.432  -4.517  1.00 88.18  ?  225 THR A N   1 
ATOM   1830 C CA  . THR A 1 226 ? 25.424 49.224  -4.655  1.00 86.59  ?  225 THR A CA  1 
ATOM   1831 C C   . THR A 1 226 ? 26.312 49.058  -3.433  1.00 89.96  ?  225 THR A C   1 
ATOM   1832 O O   . THR A 1 226 ? 27.203 48.205  -3.509  1.00 89.52  ?  225 THR A O   1 
ATOM   1833 C CB  . THR A 1 226 ? 26.352 49.408  -5.846  1.00 86.93  ?  225 THR A CB  1 
ATOM   1834 O OG1 . THR A 1 226 ? 26.461 48.092  -6.374  1.00 93.24  ?  225 THR A OG1 1 
ATOM   1835 C CG2 . THR A 1 226 ? 27.692 49.995  -5.468  1.00 81.32  ?  225 THR A CG2 1 
ATOM   1836 N N   . GLN A 1 227 ? 26.072 49.856  -2.387  1.00 88.36  ?  226 GLN A N   1 
ATOM   1837 C CA  . GLN A 1 227 ? 26.842 49.796  -1.122  1.00 90.96  ?  226 GLN A CA  1 
ATOM   1838 C C   . GLN A 1 227 ? 26.879 49.064  0.215   1.00 93.64  ?  226 GLN A C   1 
ATOM   1839 O O   . GLN A 1 227 ? 27.955 48.575  0.615   1.00 87.38  ?  226 GLN A O   1 
ATOM   1840 C CB  . GLN A 1 227 ? 26.725 51.083  -0.315  1.00 88.17  ?  226 GLN A CB  1 
ATOM   1841 N N   . ASP A 1 228 ? 25.726 48.929  0.872   1.00 93.42  ?  227 ASP A N   1 
ATOM   1842 C CA  . ASP A 1 228 ? 25.313 47.848  1.812   1.00 88.07  ?  227 ASP A CA  1 
ATOM   1843 C C   . ASP A 1 228 ? 23.980 47.189  1.417   1.00 76.28  ?  227 ASP A C   1 
ATOM   1844 O O   . ASP A 1 228 ? 23.122 47.087  2.291   1.00 70.67  ?  227 ASP A O   1 
ATOM   1845 C CB  . ASP A 1 228 ? 25.333 48.371  3.249   1.00 88.83  ?  227 ASP A CB  1 
ATOM   1846 N N   . THR A 1 229 ? 23.885 46.649  0.200   1.00 73.91  ?  228 THR A N   1 
ATOM   1847 C CA  . THR A 1 229 ? 22.669 46.035  -0.377  1.00 65.12  ?  228 THR A CA  1 
ATOM   1848 C C   . THR A 1 229 ? 22.742 44.511  -0.351  1.00 65.45  ?  228 THR A C   1 
ATOM   1849 O O   . THR A 1 229 ? 23.267 43.938  -1.305  1.00 62.93  ?  228 THR A O   1 
ATOM   1850 C CB  . THR A 1 229 ? 22.538 46.409  -1.848  1.00 67.12  ?  228 THR A CB  1 
ATOM   1851 O OG1 . THR A 1 229 ? 22.698 47.814  -1.955  1.00 78.26  ?  228 THR A OG1 1 
ATOM   1852 C CG2 . THR A 1 229 ? 21.218 46.007  -2.447  1.00 58.60  ?  228 THR A CG2 1 
ATOM   1853 N N   . GLU A 1 230 ? 22.263 43.900  0.726   1.00 58.06  ?  229 GLU A N   1 
ATOM   1854 C CA  . GLU A 1 230 ? 22.134 42.451  0.810   1.00 51.45  ?  229 GLU A CA  1 
ATOM   1855 C C   . GLU A 1 230 ? 21.003 41.959  -0.101  1.00 56.93  ?  229 GLU A C   1 
ATOM   1856 O O   . GLU A 1 230 ? 20.078 42.701  -0.459  1.00 51.77  ?  229 GLU A O   1 
ATOM   1857 C CB  . GLU A 1 230 ? 21.893 42.013  2.255   1.00 47.76  ?  229 GLU A CB  1 
ATOM   1858 C CG  . GLU A 1 230 ? 21.563 40.544  2.397   1.00 44.82  ?  229 GLU A CG  1 
ATOM   1859 C CD  . GLU A 1 230 ? 21.674 40.032  3.824   1.00 54.02  ?  229 GLU A CD  1 
ATOM   1860 O OE1 . GLU A 1 230 ? 22.019 38.842  3.995   1.00 58.06  ?  229 GLU A OE1 1 
ATOM   1861 O OE2 . GLU A 1 230 ? 21.408 40.803  4.775   1.00 54.99  ?  229 GLU A OE2 1 
ATOM   1862 N N   . LEU A 1 231 ? 21.095 40.680  -0.481  1.00 55.25  ?  230 LEU A N   1 
ATOM   1863 C CA  . LEU A 1 231 ? 20.244 40.111  -1.516  1.00 49.06  ?  230 LEU A CA  1 
ATOM   1864 C C   . LEU A 1 231 ? 20.284 38.593  -1.458  1.00 52.41  ?  230 LEU A C   1 
ATOM   1865 O O   . LEU A 1 231 ? 21.337 38.005  -1.715  1.00 53.37  ?  230 LEU A O   1 
ATOM   1866 C CB  . LEU A 1 231 ? 20.707 40.601  -2.889  1.00 50.62  ?  230 LEU A CB  1 
ATOM   1867 C CG  . LEU A 1 231 ? 20.002 40.126  -4.145  1.00 52.90  ?  230 LEU A CG  1 
ATOM   1868 C CD1 . LEU A 1 231 ? 19.488 41.341  -4.901  1.00 57.10  ?  230 LEU A CD1 1 
ATOM   1869 C CD2 . LEU A 1 231 ? 20.956 39.317  -5.008  1.00 56.77  ?  230 LEU A CD2 1 
ATOM   1870 N N   . VAL A 1 232 ? 19.163 37.939  -1.128  1.00 49.23  ?  231 VAL A N   1 
ATOM   1871 C CA  . VAL A 1 232 ? 19.192 36.490  -0.934  1.00 45.27  ?  231 VAL A CA  1 
ATOM   1872 C C   . VAL A 1 232 ? 18.883 35.782  -2.244  1.00 42.25  ?  231 VAL A C   1 
ATOM   1873 O O   . VAL A 1 232 ? 18.512 36.411  -3.239  1.00 41.02  ?  231 VAL A O   1 
ATOM   1874 C CB  . VAL A 1 232 ? 18.216 36.003  0.159   1.00 41.75  ?  231 VAL A CB  1 
ATOM   1875 C CG1 . VAL A 1 232 ? 18.643 36.489  1.544   1.00 47.71  ?  231 VAL A CG1 1 
ATOM   1876 C CG2 . VAL A 1 232 ? 16.760 36.389  -0.175  1.00 39.72  ?  231 VAL A CG2 1 
ATOM   1877 N N   . GLU A 1 233 ? 19.000 34.463  -2.235  1.00 45.69  ?  232 GLU A N   1 
ATOM   1878 C CA  . GLU A 1 233 ? 18.777 33.670  -3.430  1.00 46.73  ?  232 GLU A CA  1 
ATOM   1879 C C   . GLU A 1 233 ? 17.282 33.466  -3.637  1.00 45.39  ?  232 GLU A C   1 
ATOM   1880 O O   . GLU A 1 233 ? 16.560 33.109  -2.697  1.00 36.30  ?  232 GLU A O   1 
ATOM   1881 C CB  . GLU A 1 233 ? 19.495 32.323  -3.313  1.00 47.56  ?  232 GLU A CB  1 
ATOM   1882 C CG  . GLU A 1 233 ? 20.082 31.865  -4.644  1.00 53.10  ?  232 GLU A CG  1 
ATOM   1883 N N   . THR A 1 234 ? 16.813 33.708  -4.866  1.00 34.93  ?  233 THR A N   1 
ATOM   1884 C CA  . THR A 1 234 ? 15.419 33.437  -5.171  1.00 34.26  ?  233 THR A CA  1 
ATOM   1885 C C   . THR A 1 234 ? 15.080 32.038  -4.704  1.00 33.23  ?  233 THR A C   1 
ATOM   1886 O O   . THR A 1 234 ? 15.848 31.098  -4.915  1.00 42.00  ?  233 THR A O   1 
ATOM   1887 C CB  . THR A 1 234 ? 15.158 33.582  -6.666  1.00 37.28  ?  233 THR A CB  1 
ATOM   1888 O OG1 . THR A 1 234 ? 15.590 34.880  -7.064  1.00 39.04  ?  233 THR A OG1 1 
ATOM   1889 C CG2 . THR A 1 234 ? 13.685 33.377  -6.961  1.00 36.13  ?  233 THR A CG2 1 
ATOM   1890 N N   . ARG A 1 235 ? 13.945 31.900  -4.045  1.00 33.26  ?  234 ARG A N   1 
ATOM   1891 C CA  . ARG A 1 235 ? 13.636 30.653  -3.377  1.00 31.31  ?  234 ARG A CA  1 
ATOM   1892 C C   . ARG A 1 235 ? 12.247 30.195  -3.772  1.00 34.83  ?  234 ARG A C   1 
ATOM   1893 O O   . ARG A 1 235 ? 11.411 31.014  -4.167  1.00 40.92  ?  234 ARG A O   1 
ATOM   1894 C CB  . ARG A 1 235 ? 13.719 30.805  -1.850  1.00 37.00  ?  234 ARG A CB  1 
ATOM   1895 C CG  . ARG A 1 235 ? 12.679 31.769  -1.259  1.00 38.27  ?  234 ARG A CG  1 
ATOM   1896 C CD  . ARG A 1 235 ? 13.087 32.226  0.140   1.00 36.57  ?  234 ARG A CD  1 
ATOM   1897 N NE  . ARG A 1 235 ? 11.954 32.788  0.875   1.00 41.21  ?  234 ARG A NE  1 
ATOM   1898 C CZ  . ARG A 1 235 ? 12.067 33.497  2.004   1.00 42.04  ?  234 ARG A CZ  1 
ATOM   1899 N NH1 . ARG A 1 235 ? 13.261 33.742  2.536   1.00 34.55  ?  234 ARG A NH1 1 
ATOM   1900 N NH2 . ARG A 1 235 ? 10.980 33.954  2.611   1.00 34.20  ?  234 ARG A NH2 1 
ATOM   1901 N N   . PRO A 1 236 ? 11.986 28.890  -3.714  1.00 43.18  ?  235 PRO A N   1 
ATOM   1902 C CA  . PRO A 1 236 ? 10.645 28.396  -4.055  1.00 40.68  ?  235 PRO A CA  1 
ATOM   1903 C C   . PRO A 1 236 ? 9.680  28.472  -2.887  1.00 42.12  ?  235 PRO A C   1 
ATOM   1904 O O   . PRO A 1 236 ? 10.022 28.165  -1.739  1.00 36.95  ?  235 PRO A O   1 
ATOM   1905 C CB  . PRO A 1 236 ? 10.894 26.934  -4.454  1.00 44.15  ?  235 PRO A CB  1 
ATOM   1906 C CG  . PRO A 1 236 ? 12.121 26.525  -3.578  1.00 41.66  ?  235 PRO A CG  1 
ATOM   1907 C CD  . PRO A 1 236 ? 12.980 27.794  -3.578  1.00 37.08  ?  235 PRO A CD  1 
ATOM   1908 N N   . ALA A 1 237 ? 8.444  28.855  -3.203  1.00 41.06  ?  236 ALA A N   1 
ATOM   1909 C CA  . ALA A 1 237 ? 7.370  28.758  -2.227  1.00 43.36  ?  236 ALA A CA  1 
ATOM   1910 C C   . ALA A 1 237 ? 6.880  27.326  -2.053  1.00 38.65  ?  236 ALA A C   1 
ATOM   1911 O O   . ALA A 1 237 ? 6.303  26.998  -1.012  1.00 39.29  ?  236 ALA A O   1 
ATOM   1912 C CB  . ALA A 1 237 ? 6.209  29.667  -2.647  1.00 45.20  ?  236 ALA A CB  1 
ATOM   1913 N N   . GLY A 1 238 ? 7.107  26.458  -3.037  1.00 42.83  ?  237 GLY A N   1 
ATOM   1914 C CA  . GLY A 1 238 ? 6.619  25.093  -2.974  1.00 42.95  ?  237 GLY A CA  1 
ATOM   1915 C C   . GLY A 1 238 ? 5.263  24.867  -3.607  1.00 43.62  ?  237 GLY A C   1 
ATOM   1916 O O   . GLY A 1 238 ? 4.843  23.715  -3.737  1.00 43.58  ?  237 GLY A O   1 
ATOM   1917 N N   . ASP A 1 239 ? 4.559  25.934  -3.974  1.00 41.60  ?  238 ASP A N   1 
ATOM   1918 C CA  . ASP A 1 239 ? 3.290  25.866  -4.679  1.00 44.95  ?  238 ASP A CA  1 
ATOM   1919 C C   . ASP A 1 239 ? 3.457  26.280  -6.136  1.00 39.62  ?  238 ASP A C   1 
ATOM   1920 O O   . ASP A 1 239 ? 2.489  26.677  -6.785  1.00 44.25  ?  238 ASP A O   1 
ATOM   1921 C CB  . ASP A 1 239 ? 2.242  26.751  -3.983  1.00 43.21  ?  238 ASP A CB  1 
ATOM   1922 C CG  . ASP A 1 239 ? 2.609  28.241  -3.993  1.00 43.45  ?  238 ASP A CG  1 
ATOM   1923 O OD1 . ASP A 1 239 ? 3.602  28.620  -4.653  1.00 43.44  ?  238 ASP A OD1 1 
ATOM   1924 O OD2 . ASP A 1 239 ? 1.894  29.039  -3.343  1.00 46.74  -1 238 ASP A OD2 1 
ATOM   1925 N N   . GLY A 1 240 ? 4.681  26.238  -6.644  1.00 42.43  ?  239 GLY A N   1 
ATOM   1926 C CA  . GLY A 1 240 ? 4.953  26.657  -7.993  1.00 41.77  ?  239 GLY A CA  1 
ATOM   1927 C C   . GLY A 1 240 ? 5.304  28.117  -8.163  1.00 45.58  ?  239 GLY A C   1 
ATOM   1928 O O   . GLY A 1 240 ? 5.509  28.549  -9.305  1.00 42.89  ?  239 GLY A O   1 
ATOM   1929 N N   . THR A 1 241 ? 5.366  28.896  -7.084  1.00 36.62  ?  240 THR A N   1 
ATOM   1930 C CA  . THR A 1 241 ? 5.802  30.287  -7.158  1.00 41.12  ?  240 THR A CA  1 
ATOM   1931 C C   . THR A 1 241 ? 7.121  30.464  -6.409  1.00 39.94  ?  240 THR A C   1 
ATOM   1932 O O   . THR A 1 241 ? 7.613  29.548  -5.750  1.00 39.90  ?  240 THR A O   1 
ATOM   1933 C CB  . THR A 1 241 ? 4.735  31.233  -6.589  1.00 42.04  ?  240 THR A CB  1 
ATOM   1934 O OG1 . THR A 1 241 ? 4.418  30.840  -5.256  1.00 38.27  ?  240 THR A OG1 1 
ATOM   1935 C CG2 . THR A 1 241 ? 3.450  31.198  -7.442  1.00 44.97  ?  240 THR A CG2 1 
ATOM   1936 N N   . PHE A 1 242 ? 7.695  31.663  -6.534  1.00 35.09  ?  241 PHE A N   1 
ATOM   1937 C CA  . PHE A 1 242 ? 8.988  31.987  -5.954  1.00 39.89  ?  241 PHE A CA  1 
ATOM   1938 C C   . PHE A 1 242 ? 8.912  33.262  -5.113  1.00 39.89  ?  241 PHE A C   1 
ATOM   1939 O O   . PHE A 1 242 ? 7.927  34.006  -5.139  1.00 34.76  ?  241 PHE A O   1 
ATOM   1940 C CB  . PHE A 1 242 ? 10.036 32.096  -7.063  1.00 38.10  ?  241 PHE A CB  1 
ATOM   1941 C CG  . PHE A 1 242 ? 10.196 30.814  -7.840  1.00 41.36  ?  241 PHE A CG  1 
ATOM   1942 C CD1 . PHE A 1 242 ? 9.332  30.504  -8.863  1.00 38.07  ?  241 PHE A CD1 1 
ATOM   1943 C CD2 . PHE A 1 242 ? 11.160 29.889  -7.492  1.00 45.30  ?  241 PHE A CD2 1 
ATOM   1944 C CE1 . PHE A 1 242 ? 9.448  29.330  -9.542  1.00 45.48  ?  241 PHE A CE1 1 
ATOM   1945 C CE2 . PHE A 1 242 ? 11.278 28.701  -8.182  1.00 44.03  ?  241 PHE A CE2 1 
ATOM   1946 C CZ  . PHE A 1 242 ? 10.425 28.429  -9.204  1.00 43.06  ?  241 PHE A CZ  1 
ATOM   1947 N N   . GLN A 1 243 ? 9.974  33.473  -4.335  1.00 36.80  ?  242 GLN A N   1 
ATOM   1948 C CA  . GLN A 1 243 ? 10.098 34.582  -3.397  1.00 36.59  ?  242 GLN A CA  1 
ATOM   1949 C C   . GLN A 1 243 ? 11.527 35.087  -3.458  1.00 38.70  ?  242 GLN A C   1 
ATOM   1950 O O   . GLN A 1 243 ? 12.440 34.327  -3.778  1.00 42.66  ?  242 GLN A O   1 
ATOM   1951 C CB  . GLN A 1 243 ? 9.774  34.172  -1.962  1.00 31.79  ?  242 GLN A CB  1 
ATOM   1952 C CG  . GLN A 1 243 ? 8.586  33.260  -1.831  1.00 30.00  ?  242 GLN A CG  1 
ATOM   1953 C CD  . GLN A 1 243 ? 8.313  32.808  -0.396  1.00 34.06  ?  242 GLN A CD  1 
ATOM   1954 O OE1 . GLN A 1 243 ? 9.199  32.857  0.458   1.00 35.39  ?  242 GLN A OE1 1 
ATOM   1955 N NE2 . GLN A 1 243 ? 7.082  32.352  -0.135  1.00 34.31  ?  242 GLN A NE2 1 
ATOM   1956 N N   . LYS A 1 244 ? 11.713 36.375  -3.190  1.00 31.38  ?  243 LYS A N   1 
ATOM   1957 C CA  . LYS A 1 244 ? 13.044 36.954  -3.077  1.00 32.57  ?  243 LYS A CA  1 
ATOM   1958 C C   . LYS A 1 244 ? 12.934 38.230  -2.249  1.00 40.45  ?  243 LYS A C   1 
ATOM   1959 O O   . LYS A 1 244 ? 11.892 38.893  -2.244  1.00 38.72  ?  243 LYS A O   1 
ATOM   1960 C CB  . LYS A 1 244 ? 13.660 37.252  -4.450  1.00 44.41  ?  243 LYS A CB  1 
ATOM   1961 C CG  . LYS A 1 244 ? 15.174 37.543  -4.415  1.00 40.43  ?  243 LYS A CG  1 
ATOM   1962 C CD  . LYS A 1 244 ? 15.657 38.149  -5.738  1.00 43.00  ?  243 LYS A CD  1 
ATOM   1963 C CE  . LYS A 1 244 ? 16.974 37.528  -6.219  1.00 46.77  ?  243 LYS A CE  1 
ATOM   1964 N NZ  . LYS A 1 244 ? 17.855 36.991  -5.133  1.00 53.62  ?  243 LYS A NZ  1 
ATOM   1965 N N   . TRP A 1 245 ? 14.001 38.564  -1.530  1.00 37.57  ?  244 TRP A N   1 
ATOM   1966 C CA  . TRP A 1 245 ? 14.049 39.885  -0.922  1.00 39.64  ?  244 TRP A CA  1 
ATOM   1967 C C   . TRP A 1 245 ? 15.431 40.509  -1.051  1.00 44.17  ?  244 TRP A C   1 
ATOM   1968 O O   . TRP A 1 245 ? 16.449 39.815  -1.171  1.00 41.72  ?  244 TRP A O   1 
ATOM   1969 C CB  . TRP A 1 245 ? 13.608 39.860  0.543   1.00 33.84  ?  244 TRP A CB  1 
ATOM   1970 C CG  . TRP A 1 245 ? 14.419 39.019  1.481   1.00 38.64  ?  244 TRP A CG  1 
ATOM   1971 C CD1 . TRP A 1 245 ? 14.067 37.811  2.022   1.00 37.12  ?  244 TRP A CD1 1 
ATOM   1972 C CD2 . TRP A 1 245 ? 15.685 39.361  2.050   1.00 40.23  ?  244 TRP A CD2 1 
ATOM   1973 N NE1 . TRP A 1 245 ? 15.049 37.370  2.879   1.00 36.52  ?  244 TRP A NE1 1 
ATOM   1974 C CE2 . TRP A 1 245 ? 16.049 38.307  2.923   1.00 41.30  ?  244 TRP A CE2 1 
ATOM   1975 C CE3 . TRP A 1 245 ? 16.543 40.461  1.913   1.00 38.69  ?  244 TRP A CE3 1 
ATOM   1976 C CZ2 . TRP A 1 245 ? 17.240 38.316  3.649   1.00 43.34  ?  244 TRP A CZ2 1 
ATOM   1977 C CZ3 . TRP A 1 245 ? 17.728 40.468  2.631   1.00 44.24  ?  244 TRP A CZ3 1 
ATOM   1978 C CH2 . TRP A 1 245 ? 18.066 39.397  3.491   1.00 47.05  ?  244 TRP A CH2 1 
ATOM   1979 N N   . ALA A 1 246 ? 15.433 41.843  -1.063  1.00 39.07  ?  245 ALA A N   1 
ATOM   1980 C CA  . ALA A 1 246 ? 16.630 42.670  -1.036  1.00 37.34  ?  245 ALA A CA  1 
ATOM   1981 C C   . ALA A 1 246 ? 16.533 43.610  0.162   1.00 47.91  ?  245 ALA A C   1 
ATOM   1982 O O   . ALA A 1 246 ? 15.474 44.205  0.402   1.00 37.66  ?  245 ALA A O   1 
ATOM   1983 C CB  . ALA A 1 246 ? 16.765 43.465  -2.343  1.00 36.44  ?  245 ALA A CB  1 
ATOM   1984 N N   . ALA A 1 247 ? 17.624 43.736  0.924   1.00 42.51  ?  246 ALA A N   1 
ATOM   1985 C CA  . ALA A 1 247 ? 17.656 44.613  2.090   1.00 42.73  ?  246 ALA A CA  1 
ATOM   1986 C C   . ALA A 1 247 ? 18.794 45.617  1.979   1.00 50.65  ?  246 ALA A C   1 
ATOM   1987 O O   . ALA A 1 247 ? 19.827 45.354  1.357   1.00 50.37  ?  246 ALA A O   1 
ATOM   1988 C CB  . ALA A 1 247 ? 17.807 43.824  3.396   1.00 37.48  ?  246 ALA A CB  1 
ATOM   1989 N N   . VAL A 1 248 ? 18.587 46.781  2.587   1.00 50.84  ?  247 VAL A N   1 
ATOM   1990 C CA  . VAL A 1 248 ? 19.647 47.758  2.786   1.00 52.97  ?  247 VAL A CA  1 
ATOM   1991 C C   . VAL A 1 248 ? 19.611 48.251  4.230   1.00 53.30  ?  247 VAL A C   1 
ATOM   1992 O O   . VAL A 1 248 ? 18.571 48.221  4.902   1.00 50.70  ?  247 VAL A O   1 
ATOM   1993 C CB  . VAL A 1 248 ? 19.536 48.933  1.794   1.00 50.93  ?  247 VAL A CB  1 
ATOM   1994 C CG1 . VAL A 1 248 ? 18.214 49.665  1.974   1.00 49.05  ?  247 VAL A CG1 1 
ATOM   1995 C CG2 . VAL A 1 248 ? 20.715 49.870  1.969   1.00 58.15  ?  247 VAL A CG2 1 
ATOM   1996 N N   . VAL A 1 249 ? 20.771 48.679  4.718   1.00 54.95  ?  248 VAL A N   1 
ATOM   1997 C CA  . VAL A 1 249 ? 20.879 49.332  6.017   1.00 54.19  ?  248 VAL A CA  1 
ATOM   1998 C C   . VAL A 1 249 ? 20.909 50.831  5.774   1.00 56.67  ?  248 VAL A C   1 
ATOM   1999 O O   . VAL A 1 249 ? 21.703 51.320  4.960   1.00 56.44  ?  248 VAL A O   1 
ATOM   2000 C CB  . VAL A 1 249 ? 22.127 48.871  6.782   1.00 51.06  ?  248 VAL A CB  1 
ATOM   2001 C CG1 . VAL A 1 249 ? 22.176 49.547  8.142   1.00 53.31  ?  248 VAL A CG1 1 
ATOM   2002 C CG2 . VAL A 1 249 ? 22.127 47.361  6.931   1.00 55.22  ?  248 VAL A CG2 1 
ATOM   2003 N N   . VAL A 1 250 ? 20.030 51.558  6.452   1.00 53.61  ?  249 VAL A N   1 
ATOM   2004 C CA  . VAL A 1 250 ? 19.903 52.988  6.204   1.00 52.46  ?  249 VAL A CA  1 
ATOM   2005 C C   . VAL A 1 250 ? 20.068 53.755  7.509   1.00 53.77  ?  249 VAL A C   1 
ATOM   2006 O O   . VAL A 1 250 ? 19.779 53.219  8.592   1.00 47.46  ?  249 VAL A O   1 
ATOM   2007 C CB  . VAL A 1 250 ? 18.558 53.315  5.542   1.00 52.56  ?  249 VAL A CB  1 
ATOM   2008 C CG1 . VAL A 1 250 ? 18.396 52.511  4.253   1.00 51.92  ?  249 VAL A CG1 1 
ATOM   2009 C CG2 . VAL A 1 250 ? 17.407 53.044  6.524   1.00 45.50  ?  249 VAL A CG2 1 
ATOM   2010 N N   . PRO A 1 251 ? 20.512 55.012  7.448   1.00 56.65  ?  250 PRO A N   1 
ATOM   2011 C CA  . PRO A 1 251 ? 20.573 55.838  8.663   1.00 61.41  ?  250 PRO A CA  1 
ATOM   2012 C C   . PRO A 1 251 ? 19.169 56.157  9.169   1.00 54.15  ?  250 PRO A C   1 
ATOM   2013 O O   . PRO A 1 251 ? 18.315 56.639  8.417   1.00 51.41  ?  250 PRO A O   1 
ATOM   2014 C CB  . PRO A 1 251 ? 21.311 57.106  8.197   1.00 57.05  ?  250 PRO A CB  1 
ATOM   2015 C CG  . PRO A 1 251 ? 21.603 56.924  6.711   1.00 52.58  ?  250 PRO A CG  1 
ATOM   2016 C CD  . PRO A 1 251 ? 20.764 55.792  6.226   1.00 53.99  ?  250 PRO A CD  1 
ATOM   2017 N N   . SER A 1 252 ? 18.930 55.879  10.449  1.00 51.79  ?  251 SER A N   1 
ATOM   2018 C CA  . SER A 1 252 ? 17.609 56.124  11.025  1.00 56.37  ?  251 SER A CA  1 
ATOM   2019 C C   . SER A 1 252 ? 17.194 57.583  10.819  1.00 56.23  ?  251 SER A C   1 
ATOM   2020 O O   . SER A 1 252 ? 17.925 58.503  11.194  1.00 56.74  ?  251 SER A O   1 
ATOM   2021 C CB  . SER A 1 252 ? 17.619 55.765  12.507  1.00 56.84  ?  251 SER A CB  1 
ATOM   2022 O OG  . SER A 1 252 ? 16.299 55.628  12.990  1.00 64.33  ?  251 SER A OG  1 
ATOM   2023 N N   . GLY A 1 253 ? 16.027 57.801  10.210  1.00 51.23  ?  252 GLY A N   1 
ATOM   2024 C CA  . GLY A 1 253 ? 15.585 59.124  9.811   1.00 47.99  ?  252 GLY A CA  1 
ATOM   2025 C C   . GLY A 1 253 ? 15.679 59.390  8.318   1.00 49.31  ?  252 GLY A C   1 
ATOM   2026 O O   . GLY A 1 253 ? 15.019 60.309  7.817   1.00 48.44  ?  252 GLY A O   1 
ATOM   2027 N N   . GLU A 1 254 ? 16.459 58.602  7.583   1.00 52.17  ?  253 GLU A N   1 
ATOM   2028 C CA  . GLU A 1 254 ? 16.598 58.803  6.146   1.00 52.59  ?  253 GLU A CA  1 
ATOM   2029 C C   . GLU A 1 254 ? 15.847 57.751  5.344   1.00 51.12  ?  253 GLU A C   1 
ATOM   2030 O O   . GLU A 1 254 ? 16.102 57.591  4.141   1.00 53.02  ?  253 GLU A O   1 
ATOM   2031 C CB  . GLU A 1 254 ? 18.077 58.825  5.764   1.00 56.61  ?  253 GLU A CB  1 
ATOM   2032 C CG  . GLU A 1 254 ? 18.909 59.752  6.649   1.00 62.36  ?  253 GLU A CG  1 
ATOM   2033 C CD  . GLU A 1 254 ? 20.347 59.889  6.179   1.00 69.42  ?  253 GLU A CD  1 
ATOM   2034 O OE1 . GLU A 1 254 ? 21.234 60.116  7.033   1.00 68.12  ?  253 GLU A OE1 1 
ATOM   2035 O OE2 . GLU A 1 254 ? 20.587 59.770  4.958   1.00 73.56  -1 253 GLU A OE2 1 
ATOM   2036 N N   . GLU A 1 255 ? 14.907 57.049  5.985   1.00 43.00  ?  254 GLU A N   1 
ATOM   2037 C CA  . GLU A 1 255 ? 14.199 55.961  5.316   1.00 42.10  ?  254 GLU A CA  1 
ATOM   2038 C C   . GLU A 1 255 ? 13.561 56.402  4.001   1.00 44.28  ?  254 GLU A C   1 
ATOM   2039 O O   . GLU A 1 255 ? 13.469 55.607  3.055   1.00 42.68  ?  254 GLU A O   1 
ATOM   2040 C CB  . GLU A 1 255 ? 13.140 55.380  6.255   1.00 39.91  ?  254 GLU A CB  1 
ATOM   2041 C CG  . GLU A 1 255 ? 13.693 54.413  7.309   1.00 39.44  ?  254 GLU A CG  1 
ATOM   2042 C CD  . GLU A 1 255 ? 14.010 55.093  8.645   1.00 43.80  ?  254 GLU A CD  1 
ATOM   2043 O OE1 . GLU A 1 255 ? 14.126 54.375  9.673   1.00 43.03  ?  254 GLU A OE1 1 
ATOM   2044 O OE2 . GLU A 1 255 ? 14.149 56.343  8.660   1.00 42.84  -1 254 GLU A OE2 1 
ATOM   2045 N N   . GLN A 1 256 ? 13.123 57.657  3.910   1.00 39.89  ?  255 GLN A N   1 
ATOM   2046 C CA  . GLN A 1 256 ? 12.411 58.090  2.715   1.00 45.44  ?  255 GLN A CA  1 
ATOM   2047 C C   . GLN A 1 256 ? 13.332 58.440  1.547   1.00 48.38  ?  255 GLN A C   1 
ATOM   2048 O O   . GLN A 1 256 ? 12.835 58.592  0.423   1.00 42.46  ?  255 GLN A O   1 
ATOM   2049 C CB  . GLN A 1 256 ? 11.501 59.282  3.034   1.00 43.20  ?  255 GLN A CB  1 
ATOM   2050 C CG  . GLN A 1 256 ? 10.154 58.882  3.668   1.00 44.82  ?  255 GLN A CG  1 
ATOM   2051 C CD  . GLN A 1 256 ? 10.270 58.502  5.153   1.00 39.72  ?  255 GLN A CD  1 
ATOM   2052 O OE1 . GLN A 1 256 ? 10.898 59.206  5.958   1.00 37.01  ?  255 GLN A OE1 1 
ATOM   2053 N NE2 . GLN A 1 256 ? 9.647  57.398  5.519   1.00 37.72  ?  255 GLN A NE2 1 
ATOM   2054 N N   . ARG A 1 257 ? 14.647 58.561  1.772   1.00 47.34  ?  256 ARG A N   1 
ATOM   2055 C CA  . ARG A 1 257 ? 15.570 58.735  0.648   1.00 49.30  ?  256 ARG A CA  1 
ATOM   2056 C C   . ARG A 1 257 ? 15.727 57.472  -0.192  1.00 56.82  ?  256 ARG A C   1 
ATOM   2057 O O   . ARG A 1 257 ? 16.414 57.525  -1.219  1.00 57.40  ?  256 ARG A O   1 
ATOM   2058 C CB  . ARG A 1 257 ? 16.953 59.176  1.141   1.00 53.78  ?  256 ARG A CB  1 
ATOM   2059 C CG  . ARG A 1 257 ? 16.959 60.411  2.035   1.00 58.52  ?  256 ARG A CG  1 
ATOM   2060 C CD  . ARG A 1 257 ? 18.178 61.326  1.771   1.00 73.80  ?  256 ARG A CD  1 
ATOM   2061 N NE  . ARG A 1 257 ? 18.049 62.629  2.439   1.00 78.38  ?  256 ARG A NE  1 
ATOM   2062 C CZ  . ARG A 1 257 ? 17.538 63.725  1.873   1.00 75.20  ?  256 ARG A CZ  1 
ATOM   2063 N NH1 . ARG A 1 257 ? 17.111 63.695  0.612   1.00 74.55  ?  256 ARG A NH1 1 
ATOM   2064 N NH2 . ARG A 1 257 ? 17.457 64.856  2.567   1.00 66.96  ?  256 ARG A NH2 1 
ATOM   2065 N N   . TYR A 1 258 ? 15.117 56.350  0.196   1.00 48.47  ?  257 TYR A N   1 
ATOM   2066 C CA  . TYR A 1 258 ? 15.358 55.062  -0.444  1.00 48.98  ?  257 TYR A CA  1 
ATOM   2067 C C   . TYR A 1 258 ? 14.142 54.583  -1.231  1.00 50.64  ?  257 TYR A C   1 
ATOM   2068 O O   . TYR A 1 258 ? 12.996 54.774  -0.812  1.00 46.77  ?  257 TYR A O   1 
ATOM   2069 C CB  . TYR A 1 258 ? 15.744 54.009  0.591   1.00 46.03  ?  257 TYR A CB  1 
ATOM   2070 C CG  . TYR A 1 258 ? 17.116 54.228  1.172   1.00 52.51  ?  257 TYR A CG  1 
ATOM   2071 C CD1 . TYR A 1 258 ? 17.318 55.139  2.200   1.00 54.40  ?  257 TYR A CD1 1 
ATOM   2072 C CD2 . TYR A 1 258 ? 18.216 53.539  0.683   1.00 54.79  ?  257 TYR A CD2 1 
ATOM   2073 C CE1 . TYR A 1 258 ? 18.579 55.345  2.735   1.00 58.99  ?  257 TYR A CE1 1 
ATOM   2074 C CE2 . TYR A 1 258 ? 19.479 53.740  1.205   1.00 54.06  ?  257 TYR A CE2 1 
ATOM   2075 C CZ  . TYR A 1 258 ? 19.658 54.641  2.232   1.00 60.82  ?  257 TYR A CZ  1 
ATOM   2076 O OH  . TYR A 1 258 ? 20.917 54.838  2.765   1.00 64.06  ?  257 TYR A OH  1 
ATOM   2077 N N   . THR A 1 259 ? 14.395 53.952  -2.372  1.00 40.33  ?  258 THR A N   1 
ATOM   2078 C CA  . THR A 1 259 ? 13.348 53.312  -3.146  1.00 42.70  ?  258 THR A CA  1 
ATOM   2079 C C   . THR A 1 259 ? 13.809 51.908  -3.512  1.00 53.92  ?  258 THR A C   1 
ATOM   2080 O O   . THR A 1 259 ? 15.007 51.651  -3.668  1.00 50.71  ?  258 THR A O   1 
ATOM   2081 C CB  . THR A 1 259 ? 12.993 54.097  -4.434  1.00 46.82  ?  258 THR A CB  1 
ATOM   2082 O OG1 . THR A 1 259 ? 14.197 54.469  -5.115  1.00 48.77  ?  258 THR A OG1 1 
ATOM   2083 C CG2 . THR A 1 259 ? 12.198 55.344  -4.110  1.00 48.94  ?  258 THR A CG2 1 
ATOM   2084 N N   . CYS A 1 260 ? 12.846 51.000  -3.624  1.00 48.53  ?  259 CYS A N   1 
ATOM   2085 C CA  . CYS A 1 260 ? 13.079 49.644  -4.080  1.00 48.58  ?  259 CYS A CA  1 
ATOM   2086 C C   . CYS A 1 260 ? 12.364 49.481  -5.414  1.00 48.99  ?  259 CYS A C   1 
ATOM   2087 O O   . CYS A 1 260 ? 11.195 49.869  -5.545  1.00 45.09  ?  259 CYS A O   1 
ATOM   2088 C CB  . CYS A 1 260 ? 12.590 48.625  -3.052  1.00 46.04  ?  259 CYS A CB  1 
ATOM   2089 S SG  . CYS A 1 260 ? 12.653 46.980  -3.762  1.00 49.35  ?  259 CYS A SG  1 
ATOM   2090 N N   . HIS A 1 261 ? 13.077 48.962  -6.417  1.00 46.69  ?  260 HIS A N   1 
ATOM   2091 C CA  . HIS A 1 261 ? 12.549 48.823  -7.768  1.00 46.92  ?  260 HIS A CA  1 
ATOM   2092 C C   . HIS A 1 261 ? 12.463 47.348  -8.109  1.00 49.19  ?  260 HIS A C   1 
ATOM   2093 O O   . HIS A 1 261 ? 13.449 46.615  -7.965  1.00 47.34  ?  260 HIS A O   1 
ATOM   2094 C CB  . HIS A 1 261 ? 13.425 49.575  -8.764  1.00 52.71  ?  260 HIS A CB  1 
ATOM   2095 C CG  . HIS A 1 261 ? 13.693 50.987  -8.353  1.00 51.89  ?  260 HIS A CG  1 
ATOM   2096 N ND1 . HIS A 1 261 ? 12.983 52.053  -8.860  1.00 52.02  ?  260 HIS A ND1 1 
ATOM   2097 C CD2 . HIS A 1 261 ? 14.556 51.504  -7.445  1.00 54.71  ?  260 HIS A CD2 1 
ATOM   2098 C CE1 . HIS A 1 261 ? 13.418 53.171  -8.304  1.00 55.11  ?  260 HIS A CE1 1 
ATOM   2099 N NE2 . HIS A 1 261 ? 14.368 52.866  -7.438  1.00 53.47  ?  260 HIS A NE2 1 
ATOM   2100 N N   . VAL A 1 262 ? 11.283 46.919  -8.540  1.00 45.28  ?  261 VAL A N   1 
ATOM   2101 C CA  . VAL A 1 262 ? 10.995 45.520  -8.811  1.00 46.75  ?  261 VAL A CA  1 
ATOM   2102 C C   . VAL A 1 262 ? 10.682 45.375  -10.290 1.00 50.40  ?  261 VAL A C   1 
ATOM   2103 O O   . VAL A 1 262 ? 9.724  45.987  -10.791 1.00 47.46  ?  261 VAL A O   1 
ATOM   2104 C CB  . VAL A 1 262 ? 9.825  45.006  -7.966  1.00 41.12  ?  261 VAL A CB  1 
ATOM   2105 C CG1 . VAL A 1 262 ? 9.700  43.481  -8.120  1.00 41.73  ?  261 VAL A CG1 1 
ATOM   2106 C CG2 . VAL A 1 262 ? 9.999  45.439  -6.511  1.00 43.03  ?  261 VAL A CG2 1 
ATOM   2107 N N   . GLN A 1 263 ? 11.469 44.547  -10.978 1.00 51.76  ?  262 GLN A N   1 
ATOM   2108 C CA  . GLN A 1 263 ? 11.263 44.234  -12.389 1.00 51.56  ?  262 GLN A CA  1 
ATOM   2109 C C   . GLN A 1 263 ? 10.943 42.754  -12.508 1.00 48.60  ?  262 GLN A C   1 
ATOM   2110 O O   . GLN A 1 263 ? 11.736 41.911  -12.075 1.00 49.58  ?  262 GLN A O   1 
ATOM   2111 C CB  . GLN A 1 263 ? 12.497 44.569  -13.227 1.00 49.51  ?  262 GLN A CB  1 
ATOM   2112 C CG  . GLN A 1 263 ? 12.880 46.023  -13.250 1.00 56.09  ?  262 GLN A CG  1 
ATOM   2113 C CD  . GLN A 1 263 ? 14.341 46.221  -12.895 1.00 64.85  ?  262 GLN A CD  1 
ATOM   2114 O OE1 . GLN A 1 263 ? 15.206 46.228  -13.776 1.00 62.12  ?  262 GLN A OE1 1 
ATOM   2115 N NE2 . GLN A 1 263 ? 14.628 46.377  -11.590 1.00 61.93  ?  262 GLN A NE2 1 
ATOM   2116 N N   . HIS A 1 264 ? 9.790  42.443  -13.093 1.00 46.31  ?  263 HIS A N   1 
ATOM   2117 C CA  . HIS A 1 264 ? 9.393  41.062  -13.329 1.00 45.86  ?  263 HIS A CA  1 
ATOM   2118 C C   . HIS A 1 264 ? 8.617  40.996  -14.636 1.00 51.39  ?  263 HIS A C   1 
ATOM   2119 O O   . HIS A 1 264 ? 8.041  41.986  -15.095 1.00 55.14  ?  263 HIS A O   1 
ATOM   2120 C CB  . HIS A 1 264 ? 8.556  40.514  -12.171 1.00 44.29  ?  263 HIS A CB  1 
ATOM   2121 C CG  . HIS A 1 264 ? 8.149  39.080  -12.326 1.00 46.67  ?  263 HIS A CG  1 
ATOM   2122 N ND1 . HIS A 1 264 ? 6.920  38.705  -12.828 1.00 45.59  ?  263 HIS A ND1 1 
ATOM   2123 C CD2 . HIS A 1 264 ? 8.788  37.928  -12.004 1.00 45.63  ?  263 HIS A CD2 1 
ATOM   2124 C CE1 . HIS A 1 264 ? 6.828  37.387  -12.832 1.00 45.79  ?  263 HIS A CE1 1 
ATOM   2125 N NE2 . HIS A 1 264 ? 7.945  36.891  -12.330 1.00 42.43  ?  263 HIS A NE2 1 
ATOM   2126 N N   . GLU A 1 265 ? 8.613  39.806  -15.228 1.00 49.55  ?  264 GLU A N   1 
ATOM   2127 C CA  . GLU A 1 265 ? 7.924  39.598  -16.491 1.00 54.66  ?  264 GLU A CA  1 
ATOM   2128 C C   . GLU A 1 265 ? 6.433  39.893  -16.371 1.00 56.75  ?  264 GLU A C   1 
ATOM   2129 O O   . GLU A 1 265 ? 5.817  40.374  -17.329 1.00 58.77  ?  264 GLU A O   1 
ATOM   2130 C CB  . GLU A 1 265 ? 8.171  38.160  -16.959 1.00 59.37  ?  264 GLU A CB  1 
ATOM   2131 C CG  . GLU A 1 265 ? 7.271  37.659  -18.070 1.00 60.18  ?  264 GLU A CG  1 
ATOM   2132 C CD  . GLU A 1 265 ? 7.724  36.300  -18.606 1.00 66.25  ?  264 GLU A CD  1 
ATOM   2133 O OE1 . GLU A 1 265 ? 6.847  35.467  -18.947 1.00 67.68  ?  264 GLU A OE1 1 
ATOM   2134 O OE2 . GLU A 1 265 ? 8.955  36.070  -18.693 1.00 66.14  -1 264 GLU A OE2 1 
ATOM   2135 N N   . GLY A 1 266 ? 5.839  39.623  -15.213 1.00 52.15  ?  265 GLY A N   1 
ATOM   2136 C CA  . GLY A 1 266 ? 4.426  39.870  -15.009 1.00 49.84  ?  265 GLY A CA  1 
ATOM   2137 C C   . GLY A 1 266 ? 4.037  41.305  -14.712 1.00 50.28  ?  265 GLY A C   1 
ATOM   2138 O O   . GLY A 1 266 ? 2.876  41.560  -14.382 1.00 50.54  ?  265 GLY A O   1 
ATOM   2139 N N   . LEU A 1 267 ? 4.964  42.254  -14.827 1.00 51.47  ?  266 LEU A N   1 
ATOM   2140 C CA  . LEU A 1 267 ? 4.715  43.635  -14.421 1.00 57.83  ?  266 LEU A CA  1 
ATOM   2141 C C   . LEU A 1 267 ? 4.711  44.548  -15.641 1.00 60.95  ?  266 LEU A C   1 
ATOM   2142 O O   . LEU A 1 267 ? 5.781  44.788  -16.233 1.00 52.88  ?  266 LEU A O   1 
ATOM   2143 C CB  . LEU A 1 267 ? 5.766  44.107  -13.410 1.00 48.24  ?  266 LEU A CB  1 
ATOM   2144 C CG  . LEU A 1 267 ? 5.780  43.437  -12.028 1.00 49.17  ?  266 LEU A CG  1 
ATOM   2145 C CD1 . LEU A 1 267 ? 6.825  44.081  -11.137 1.00 42.20  ?  266 LEU A CD1 1 
ATOM   2146 C CD2 . LEU A 1 267 ? 4.398  43.435  -11.351 1.00 42.03  ?  266 LEU A CD2 1 
ATOM   2147 N N   . PRO A 1 268 ? 3.534  45.086  -16.044 1.00 59.46  ?  267 PRO A N   1 
ATOM   2148 C CA  . PRO A 1 268 ? 3.473  46.021  -17.180 1.00 59.04  ?  267 PRO A CA  1 
ATOM   2149 C C   . PRO A 1 268 ? 4.638  47.000  -17.222 1.00 61.68  ?  267 PRO A C   1 
ATOM   2150 O O   . PRO A 1 268 ? 5.282  47.146  -18.268 1.00 59.46  ?  267 PRO A O   1 
ATOM   2151 C CB  . PRO A 1 268 ? 2.133  46.729  -16.957 1.00 61.50  ?  267 PRO A CB  1 
ATOM   2152 C CG  . PRO A 1 268 ? 1.266  45.653  -16.313 1.00 55.05  ?  267 PRO A CG  1 
ATOM   2153 C CD  . PRO A 1 268 ? 2.194  44.760  -15.519 1.00 56.04  ?  267 PRO A CD  1 
ATOM   2154 N N   . LYS A 1 269 ? 4.936  47.663  -16.108 1.00 63.15  ?  268 LYS A N   1 
ATOM   2155 C CA  . LYS A 1 269 ? 6.168  48.430  -15.984 1.00 57.81  ?  268 LYS A CA  1 
ATOM   2156 C C   . LYS A 1 269 ? 6.692  48.295  -14.535 1.00 56.54  ?  268 LYS A C   1 
ATOM   2157 O O   . LYS A 1 269 ? 5.977  47.859  -13.664 1.00 54.05  ?  268 LYS A O   1 
ATOM   2158 C CB  . LYS A 1 269 ? 5.985  49.906  -16.361 1.00 64.49  ?  268 LYS A CB  1 
ATOM   2159 C CG  . LYS A 1 269 ? 6.167  50.183  -17.879 1.00 68.60  ?  268 LYS A CG  1 
ATOM   2160 C CD  . LYS A 1 269 ? 7.598  49.901  -18.384 1.00 64.80  ?  268 LYS A CD  1 
ATOM   2161 C CE  . LYS A 1 269 ? 7.822  48.411  -18.659 1.00 58.98  ?  268 LYS A CE  1 
ATOM   2162 N NZ  . LYS A 1 269 ? 9.042  48.179  -19.488 1.00 63.53  ?  268 LYS A NZ  1 
ATOM   2163 N N   . PRO A 1 270 ? 7.953  48.674  -14.339 1.00 56.39  ?  269 PRO A N   1 
ATOM   2164 C CA  . PRO A 1 270 ? 8.593  48.329  -13.051 1.00 54.69  ?  269 PRO A CA  1 
ATOM   2165 C C   . PRO A 1 270 ? 7.941  49.029  -11.868 1.00 52.28  ?  269 PRO A C   1 
ATOM   2166 O O   . PRO A 1 270 ? 7.433  50.149  -11.969 1.00 51.66  ?  269 PRO A O   1 
ATOM   2167 C CB  . PRO A 1 270 ? 10.043 48.808  -13.251 1.00 54.09  ?  269 PRO A CB  1 
ATOM   2168 C CG  . PRO A 1 270 ? 10.151 49.177  -14.728 1.00 57.59  ?  269 PRO A CG  1 
ATOM   2169 C CD  . PRO A 1 270 ? 8.789  49.538  -15.164 1.00 56.89  ?  269 PRO A CD  1 
ATOM   2170 N N   . LEU A 1 271 ? 7.954  48.336  -10.728 1.00 53.09  ?  270 LEU A N   1 
ATOM   2171 C CA  . LEU A 1 271 ? 7.396  48.855  -9.487  1.00 41.37  ?  270 LEU A CA  1 
ATOM   2172 C C   . LEU A 1 271 ? 8.453  49.616  -8.710  1.00 48.32  ?  270 LEU A C   1 
ATOM   2173 O O   . LEU A 1 271 ? 9.620  49.209  -8.656  1.00 47.49  ?  270 LEU A O   1 
ATOM   2174 C CB  . LEU A 1 271 ? 6.866  47.721  -8.619  1.00 46.24  ?  270 LEU A CB  1 
ATOM   2175 C CG  . LEU A 1 271 ? 5.620  47.019  -9.117  1.00 52.52  ?  270 LEU A CG  1 
ATOM   2176 C CD1 . LEU A 1 271 ? 5.284  45.836  -8.207  1.00 47.05  ?  270 LEU A CD1 1 
ATOM   2177 C CD2 . LEU A 1 271 ? 4.486  48.021  -9.196  1.00 49.81  ?  270 LEU A CD2 1 
ATOM   2178 N N   . THR A 1 272 ? 8.031  50.716  -8.093  1.00 48.78  ?  271 THR A N   1 
ATOM   2179 C CA  . THR A 1 272 ? 8.861  51.472  -7.166  1.00 42.44  ?  271 THR A CA  1 
ATOM   2180 C C   . THR A 1 272 ? 8.190  51.441  -5.802  1.00 48.79  ?  271 THR A C   1 
ATOM   2181 O O   . THR A 1 272 ? 7.021  51.824  -5.675  1.00 47.07  ?  271 THR A O   1 
ATOM   2182 C CB  . THR A 1 272 ? 9.057  52.908  -7.645  1.00 45.63  ?  271 THR A CB  1 
ATOM   2183 O OG1 . THR A 1 272 ? 9.603  52.879  -8.965  1.00 57.61  ?  271 THR A OG1 1 
ATOM   2184 C CG2 . THR A 1 272 ? 10.030 53.659  -6.715  1.00 45.07  ?  271 THR A CG2 1 
ATOM   2185 N N   . LEU A 1 273 ? 8.910  50.957  -4.796  1.00 45.62  ?  272 LEU A N   1 
ATOM   2186 C CA  . LEU A 1 273 ? 8.403  50.893  -3.437  1.00 43.32  ?  272 LEU A CA  1 
ATOM   2187 C C   . LEU A 1 273 ? 9.208  51.824  -2.548  1.00 46.44  ?  272 LEU A C   1 
ATOM   2188 O O   . LEU A 1 273 ? 10.414 51.999  -2.737  1.00 36.80  ?  272 LEU A O   1 
ATOM   2189 C CB  . LEU A 1 273 ? 8.458  49.470  -2.870  1.00 41.44  ?  272 LEU A CB  1 
ATOM   2190 C CG  . LEU A 1 273 ? 7.323  48.575  -3.369  1.00 51.48  ?  272 LEU A CG  1 
ATOM   2191 C CD1 . LEU A 1 273 ? 7.597  48.192  -4.811  1.00 47.15  ?  272 LEU A CD1 1 
ATOM   2192 C CD2 . LEU A 1 273 ? 7.132  47.333  -2.482  1.00 41.56  ?  272 LEU A CD2 1 
ATOM   2193 N N   . ARG A 1 274 ? 8.523  52.400  -1.557  1.00 41.96  ?  273 ARG A N   1 
ATOM   2194 C CA  . ARG A 1 274 ? 9.130  53.332  -0.626  1.00 41.04  ?  273 ARG A CA  1 
ATOM   2195 C C   . ARG A 1 274 ? 8.562  53.069  0.764   1.00 44.89  ?  273 ARG A C   1 
ATOM   2196 O O   . ARG A 1 274 ? 7.387  52.713  0.911   1.00 42.48  ?  273 ARG A O   1 
ATOM   2197 C CB  . ARG A 1 274 ? 8.871  54.790  -1.067  1.00 39.80  ?  273 ARG A CB  1 
ATOM   2198 C CG  . ARG A 1 274 ? 9.391  55.829  -0.087  1.00 50.39  ?  273 ARG A CG  1 
ATOM   2199 C CD  . ARG A 1 274 ? 9.207  57.263  -0.595  1.00 56.60  ?  273 ARG A CD  1 
ATOM   2200 N NE  . ARG A 1 274 ? 10.450 57.745  -1.183  1.00 61.93  ?  273 ARG A NE  1 
ATOM   2201 C CZ  . ARG A 1 274 ? 10.590 58.090  -2.457  1.00 57.02  ?  273 ARG A CZ  1 
ATOM   2202 N NH1 . ARG A 1 274 ? 9.554  58.029  -3.286  1.00 62.34  ?  273 ARG A NH1 1 
ATOM   2203 N NH2 . ARG A 1 274 ? 11.769 58.501  -2.898  1.00 53.84  ?  273 ARG A NH2 1 
ATOM   2204 N N   . TRP A 1 275 ? 9.403  53.217  1.779   1.00 39.26  ?  274 TRP A N   1 
ATOM   2205 C CA  . TRP A 1 275 ? 8.943  53.126  3.157   1.00 43.65  ?  274 TRP A CA  1 
ATOM   2206 C C   . TRP A 1 275 ? 8.256  54.435  3.522   1.00 42.43  ?  274 TRP A C   1 
ATOM   2207 O O   . TRP A 1 275 ? 8.911  55.473  3.663   1.00 41.54  ?  274 TRP A O   1 
ATOM   2208 C CB  . TRP A 1 275 ? 10.095 52.854  4.111   1.00 39.00  ?  274 TRP A CB  1 
ATOM   2209 C CG  . TRP A 1 275 ? 9.632  52.767  5.554   1.00 35.88  ?  274 TRP A CG  1 
ATOM   2210 C CD1 . TRP A 1 275 ? 9.813  53.703  6.538   1.00 36.14  ?  274 TRP A CD1 1 
ATOM   2211 C CD2 . TRP A 1 275 ? 8.898  51.684  6.160   1.00 38.74  ?  274 TRP A CD2 1 
ATOM   2212 N NE1 . TRP A 1 275 ? 9.238  53.263  7.720   1.00 35.25  ?  274 TRP A NE1 1 
ATOM   2213 C CE2 . TRP A 1 275 ? 8.674  52.030  7.515   1.00 32.70  ?  274 TRP A CE2 1 
ATOM   2214 C CE3 . TRP A 1 275 ? 8.408  50.460  5.689   1.00 34.55  ?  274 TRP A CE3 1 
ATOM   2215 C CZ2 . TRP A 1 275 ? 7.986  51.189  8.401   1.00 33.68  ?  274 TRP A CZ2 1 
ATOM   2216 C CZ3 . TRP A 1 275 ? 7.725  49.622  6.578   1.00 36.69  ?  274 TRP A CZ3 1 
ATOM   2217 C CH2 . TRP A 1 275 ? 7.519  49.993  7.911   1.00 32.65  ?  274 TRP A CH2 1 
ATOM   2218 N N   . GLU A 1 276 ? 6.945  54.400  3.667   1.00 38.04  ?  275 GLU A N   1 
ATOM   2219 C CA  . GLU A 1 276 ? 6.246  55.613  4.069   1.00 41.73  ?  275 GLU A CA  1 
ATOM   2220 C C   . GLU A 1 276 ? 4.975  55.280  4.841   1.00 41.01  ?  275 GLU A C   1 
ATOM   2221 O O   . GLU A 1 276 ? 4.594  54.104  4.966   1.00 33.54  ?  275 GLU A O   1 
ATOM   2222 C CB  . GLU A 1 276 ? 5.915  56.481  2.852   1.00 41.30  ?  275 GLU A CB  1 
ATOM   2223 C CG  . GLU A 1 276 ? 5.030  55.808  1.836   1.00 45.84  ?  275 GLU A CG  1 
ATOM   2224 C CD  . GLU A 1 276 ? 5.274  56.327  0.415   1.00 51.29  ?  275 GLU A CD  1 
ATOM   2225 O OE1 . GLU A 1 276 ? 4.752  55.706  -0.537  1.00 51.83  ?  275 GLU A OE1 1 
ATOM   2226 O OE2 . GLU A 1 276 ? 5.989  57.341  0.255   1.00 50.67  -1 275 GLU A OE2 1 
ATOM   2227 O OXT . GLU A 1 276 ? 4.327  56.209  5.332   1.00 36.43  -1 275 GLU A OXT 1 
ATOM   2228 N N   . ILE B 2 1   ? 11.472 15.140  -23.036 1.00 26.11  ?  1   ILE C N   1 
ATOM   2229 C CA  . ILE B 2 1   ? 11.912 13.841  -23.547 1.00 29.57  ?  1   ILE C CA  1 
ATOM   2230 C C   . ILE B 2 1   ? 13.434 13.821  -23.653 1.00 23.49  ?  1   ILE C C   1 
ATOM   2231 O O   . ILE B 2 1   ? 14.031 14.761  -24.173 1.00 23.97  ?  1   ILE C O   1 
ATOM   2232 C CB  . ILE B 2 1   ? 11.239 13.508  -24.919 1.00 26.75  ?  1   ILE C CB  1 
ATOM   2233 C CG1 . ILE B 2 1   ? 11.558 12.072  -25.361 1.00 30.09  ?  1   ILE C CG1 1 
ATOM   2234 C CG2 . ILE B 2 1   ? 11.640 14.541  -26.020 1.00 26.33  ?  1   ILE C CG2 1 
ATOM   2235 C CD1 . ILE B 2 1   ? 10.729 11.622  -26.620 1.00 29.03  ?  1   ILE C CD1 1 
ATOM   2236 N N   . LEU B 2 2   ? 14.044 12.733  -23.157 1.00 26.25  ?  2   LEU C N   1 
ATOM   2237 C CA  . LEU B 2 2   ? 15.495 12.620  -23.061 1.00 26.20  ?  2   LEU C CA  1 
ATOM   2238 C C   . LEU B 2 2   ? 16.190 12.543  -24.420 1.00 26.58  ?  2   LEU C C   1 
ATOM   2239 O O   . LEU B 2 2   ? 15.688 11.948  -25.378 1.00 25.85  ?  2   LEU C O   1 
ATOM   2240 C CB  . LEU B 2 2   ? 15.872 11.363  -22.286 1.00 23.76  ?  2   LEU C CB  1 
ATOM   2241 C CG  . LEU B 2 2   ? 15.617 11.368  -20.793 1.00 26.47  ?  2   LEU C CG  1 
ATOM   2242 C CD1 . LEU B 2 2   ? 15.666 9.918   -20.232 1.00 23.17  ?  2   LEU C CD1 1 
ATOM   2243 C CD2 . LEU B 2 2   ? 16.679 12.273  -20.151 1.00 31.63  ?  2   LEU C CD2 1 
ATOM   2244 N N   . ASP B 2 3   ? 17.398 13.083  -24.469 1.00 21.41  ?  3   ASP C N   1 
ATOM   2245 C CA  . ASP B 2 3   ? 18.299 12.740  -25.557 1.00 25.50  ?  3   ASP C CA  1 
ATOM   2246 C C   . ASP B 2 3   ? 18.677 11.255  -25.451 1.00 28.31  ?  3   ASP C C   1 
ATOM   2247 O O   . ASP B 2 3   ? 18.562 10.635  -24.390 1.00 25.53  ?  3   ASP C O   1 
ATOM   2248 C CB  . ASP B 2 3   ? 19.540 13.631  -25.528 1.00 27.64  ?  3   ASP C CB  1 
ATOM   2249 C CG  . ASP B 2 3   ? 20.371 13.543  -26.800 1.00 31.13  ?  3   ASP C CG  1 
ATOM   2250 O OD1 . ASP B 2 3   ? 20.028 12.748  -27.715 1.00 31.04  ?  3   ASP C OD1 1 
ATOM   2251 O OD2 . ASP B 2 3   ? 21.398 14.258  -26.878 1.00 28.48  -1 3   ASP C OD2 1 
ATOM   2252 N N   . THR B 2 4   ? 19.090 10.683  -26.584 1.00 25.90  ?  4   THR C N   1 
ATOM   2253 C CA  . THR B 2 4   ? 19.520 9.283   -26.655 1.00 25.37  ?  4   THR C CA  1 
ATOM   2254 C C   . THR B 2 4   ? 20.927 9.118   -26.101 1.00 24.29  ?  4   THR C C   1 
ATOM   2255 O O   . THR B 2 4   ? 21.851 9.814   -26.523 1.00 29.33  ?  4   THR C O   1 
ATOM   2256 C CB  . THR B 2 4   ? 19.476 8.780   -28.108 1.00 28.33  ?  4   THR C CB  1 
ATOM   2257 O OG1 . THR B 2 4   ? 18.103 8.689   -28.506 1.00 28.59  ?  4   THR C OG1 1 
ATOM   2258 C CG2 . THR B 2 4   ? 20.125 7.376   -28.204 1.00 21.70  ?  4   THR C CG2 1 
ATOM   2259 N N   . ALA B 2 5   ? 21.086 8.217   -25.128 1.00 24.89  ?  5   ALA C N   1 
ATOM   2260 C CA  . ALA B 2 5   ? 22.409 7.954   -24.570 1.00 28.82  ?  5   ALA C CA  1 
ATOM   2261 C C   . ALA B 2 5   ? 23.331 7.463   -25.669 1.00 31.94  ?  5   ALA C C   1 
ATOM   2262 O O   . ALA B 2 5   ? 23.046 6.446   -26.309 1.00 33.43  ?  5   ALA C O   1 
ATOM   2263 C CB  . ALA B 2 5   ? 22.317 6.900   -23.456 1.00 31.81  ?  5   ALA C CB  1 
ATOM   2264 N N   . GLY B 2 6   ? 24.422 8.179   -25.907 1.00 31.31  ?  6   GLY C N   1 
ATOM   2265 C CA  . GLY B 2 6   ? 25.288 7.798   -27.007 1.00 28.19  ?  6   GLY C CA  1 
ATOM   2266 C C   . GLY B 2 6   ? 26.289 8.869   -27.364 1.00 29.57  ?  6   GLY C C   1 
ATOM   2267 O O   . GLY B 2 6   ? 26.001 10.067  -27.223 1.00 29.58  ?  6   GLY C O   1 
ATOM   2268 N N   . LYS B 2 7   ? 27.473 8.449   -27.811 1.00 21.68  ?  7   LYS C N   1 
ATOM   2269 C CA  . LYS B 2 7   ? 28.567 9.359   -28.164 1.00 27.06  ?  7   LYS C CA  1 
ATOM   2270 C C   . LYS B 2 7   ? 28.925 10.310  -27.019 1.00 29.48  ?  7   LYS C C   1 
ATOM   2271 O O   . LYS B 2 7   ? 29.159 11.514  -27.219 1.00 25.99  ?  7   LYS C O   1 
ATOM   2272 C CB  . LYS B 2 7   ? 28.236 10.144  -29.435 1.00 30.86  ?  7   LYS C CB  1 
ATOM   2273 C CG  . LYS B 2 7   ? 28.229 9.274   -30.689 1.00 30.65  ?  7   LYS C CG  1 
ATOM   2274 C CD  . LYS B 2 7   ? 27.839 10.104  -31.932 1.00 29.66  ?  7   LYS C CD  1 
ATOM   2275 C CE  . LYS B 2 7   ? 27.672 9.254   -33.210 1.00 29.28  ?  7   LYS C CE  1 
ATOM   2276 N NZ  . LYS B 2 7   ? 27.222 10.092  -34.404 1.00 28.28  ?  7   LYS C NZ  1 
ATOM   2277 N N   . GLU B 2 8   ? 29.026 9.757   -25.798 1.00 26.29  ?  8   GLU C N   1 
ATOM   2278 C CA  . GLU B 2 8   ? 29.347 10.651  -24.690 1.00 27.60  ?  8   GLU C CA  1 
ATOM   2279 C C   . GLU B 2 8   ? 30.245 9.992   -23.645 1.00 28.58  ?  8   GLU C C   1 
ATOM   2280 O O   . GLU B 2 8   ? 30.216 10.375  -22.467 1.00 24.89  ?  8   GLU C O   1 
ATOM   2281 C CB  . GLU B 2 8   ? 28.069 11.209  -24.041 1.00 25.21  ?  8   GLU C CB  1 
ATOM   2282 C CG  . GLU B 2 8   ? 27.068 10.178  -23.559 1.00 29.76  ?  8   GLU C CG  1 
ATOM   2283 C CD  . GLU B 2 8   ? 25.647 10.758  -23.377 1.00 36.39  ?  8   GLU C CD  1 
ATOM   2284 O OE1 . GLU B 2 8   ? 25.484 11.879  -22.829 1.00 31.62  ?  8   GLU C OE1 1 
ATOM   2285 O OE2 . GLU B 2 8   ? 24.671 10.071  -23.756 1.00 37.16  -1 8   GLU C OE2 1 
ATOM   2286 N N   . GLU B 2 9   ? 31.073 9.035   -24.060 1.00 25.47  ?  9   GLU C N   1 
ATOM   2287 C CA  . GLU B 2 9   ? 32.109 8.511   -23.180 1.00 27.05  ?  9   GLU C CA  1 
ATOM   2288 C C   . GLU B 2 9   ? 33.281 9.481   -23.124 1.00 27.69  ?  9   GLU C C   1 
ATOM   2289 O O   . GLU B 2 9   ? 33.706 10.023  -24.153 1.00 26.60  ?  9   GLU C O   1 
ATOM   2290 C CB  . GLU B 2 9   ? 32.581 7.144   -23.678 1.00 28.88  ?  9   GLU C CB  1 
ATOM   2291 C CG  . GLU B 2 9   ? 31.450 6.140   -23.882 1.00 31.16  ?  9   GLU C CG  1 
ATOM   2292 C CD  . GLU B 2 9   ? 31.961 4.752   -24.250 1.00 38.36  ?  9   GLU C CD  1 
ATOM   2293 O OE1 . GLU B 2 9   ? 33.168 4.476   -24.093 1.00 38.55  ?  9   GLU C OE1 1 
ATOM   2294 O OE2 . GLU B 2 9   ? 31.148 3.940   -24.706 1.00 36.71  -1 9   GLU C OE2 1 
ATOM   2295 N N   . TYR B 2 10  ? 33.818 9.693   -21.919 1.00 25.61  ?  10  TYR C N   1 
ATOM   2296 C CA  . TYR B 2 10  ? 34.900 10.675  -21.742 1.00 27.61  ?  10  TYR C CA  1 
ATOM   2297 C C   . TYR B 2 10  ? 36.250 10.111  -22.155 1.00 30.72  ?  10  TYR C C   1 
ATOM   2298 O O   . TYR B 2 10  ? 37.208 10.804  -22.520 1.00 29.90  ?  10  TYR C O   1 
ATOM   2299 C CB  . TYR B 2 10  ? 34.976 11.137  -20.284 1.00 28.62  ?  10  TYR C CB  1 
ATOM   2300 C CG  . TYR B 2 10  ? 33.808 11.973  -19.852 1.00 26.14  ?  10  TYR C CG  1 
ATOM   2301 C CD1 . TYR B 2 10  ? 32.969 12.558  -20.790 1.00 26.07  ?  10  TYR C CD1 1 
ATOM   2302 C CD2 . TYR B 2 10  ? 33.554 12.195  -18.496 1.00 24.90  ?  10  TYR C CD2 1 
ATOM   2303 C CE1 . TYR B 2 10  ? 31.898 13.344  -20.380 1.00 24.68  ?  10  TYR C CE1 1 
ATOM   2304 C CE2 . TYR B 2 10  ? 32.493 12.970  -18.075 1.00 24.15  ?  10  TYR C CE2 1 
ATOM   2305 C CZ  . TYR B 2 10  ? 31.660 13.537  -19.016 1.00 29.04  ?  10  TYR C CZ  1 
ATOM   2306 O OH  . TYR B 2 10  ? 30.591 14.296  -18.602 1.00 22.88  ?  10  TYR C OH  1 
ATOM   2307 O OXT . TYR B 2 10  ? 36.416 8.895   -22.118 1.00 37.31  -1 10  TYR C OXT 1 
ATOM   2308 N N   . MET C 3 1   ? 39.344 19.446  -4.659  1.00 64.91  ?  0   MET B N   1 
ATOM   2309 C CA  . MET C 3 1   ? 37.887 19.605  -4.942  1.00 64.53  ?  0   MET B CA  1 
ATOM   2310 C C   . MET C 3 1   ? 37.378 20.913  -4.347  1.00 62.76  ?  0   MET B C   1 
ATOM   2311 O O   . MET C 3 1   ? 37.876 21.374  -3.317  1.00 59.64  ?  0   MET B O   1 
ATOM   2312 C CB  . MET C 3 1   ? 37.090 18.420  -4.382  1.00 60.70  ?  0   MET B CB  1 
ATOM   2313 C CG  . MET C 3 1   ? 36.857 17.315  -5.401  1.00 54.74  ?  0   MET B CG  1 
ATOM   2314 S SD  . MET C 3 1   ? 35.967 15.889  -4.751  1.00 68.39  ?  0   MET B SD  1 
ATOM   2315 C CE  . MET C 3 1   ? 37.355 14.886  -4.203  1.00 54.99  ?  0   MET B CE  1 
ATOM   2316 N N   . ILE C 3 2   ? 36.383 21.504  -5.002  1.00 64.62  ?  1   ILE B N   1 
ATOM   2317 C CA  . ILE C 3 2   ? 35.745 22.726  -4.519  1.00 65.48  ?  1   ILE B CA  1 
ATOM   2318 C C   . ILE C 3 2   ? 34.595 22.338  -3.598  1.00 54.41  ?  1   ILE B C   1 
ATOM   2319 O O   . ILE C 3 2   ? 33.638 21.681  -4.024  1.00 62.55  ?  1   ILE B O   1 
ATOM   2320 C CB  . ILE C 3 2   ? 35.241 23.590  -5.688  1.00 63.77  ?  1   ILE B CB  1 
ATOM   2321 C CG1 . ILE C 3 2   ? 34.309 22.769  -6.591  1.00 58.07  ?  1   ILE B CG1 1 
ATOM   2322 C CG2 . ILE C 3 2   ? 36.416 24.136  -6.499  1.00 64.36  ?  1   ILE B CG2 1 
ATOM   2323 C CD1 . ILE C 3 2   ? 33.008 23.467  -6.962  1.00 55.73  ?  1   ILE B CD1 1 
ATOM   2324 N N   . GLN C 3 3   ? 34.681 22.730  -2.336  1.00 52.57  ?  2   GLN B N   1 
ATOM   2325 C CA  . GLN C 3 3   ? 33.591 22.514  -1.398  1.00 46.52  ?  2   GLN B CA  1 
ATOM   2326 C C   . GLN C 3 3   ? 32.912 23.846  -1.119  1.00 47.05  ?  2   GLN B C   1 
ATOM   2327 O O   . GLN C 3 3   ? 33.577 24.848  -0.827  1.00 48.60  ?  2   GLN B O   1 
ATOM   2328 C CB  . GLN C 3 3   ? 34.085 21.862  -0.111  1.00 44.74  ?  2   GLN B CB  1 
ATOM   2329 C CG  . GLN C 3 3   ? 34.792 20.527  -0.357  1.00 53.99  ?  2   GLN B CG  1 
ATOM   2330 C CD  . GLN C 3 3   ? 34.544 19.505  0.744   1.00 51.54  ?  2   GLN B CD  1 
ATOM   2331 O OE1 . GLN C 3 3   ? 34.182 18.346  0.477   1.00 58.95  ?  2   GLN B OE1 1 
ATOM   2332 N NE2 . GLN C 3 3   ? 34.733 19.926  1.982   1.00 44.39  ?  2   GLN B NE2 1 
ATOM   2333 N N   . ARG C 3 4   ? 31.588 23.848  -1.227  1.00 44.81  ?  3   ARG B N   1 
ATOM   2334 C CA  . ARG C 3 4   ? 30.763 25.018  -0.993  1.00 41.18  ?  3   ARG B CA  1 
ATOM   2335 C C   . ARG C 3 4   ? 29.786 24.703  0.122   1.00 38.45  ?  3   ARG B C   1 
ATOM   2336 O O   . ARG C 3 4   ? 29.137 23.653  0.102   1.00 31.49  ?  3   ARG B O   1 
ATOM   2337 C CB  . ARG C 3 4   ? 30.046 25.412  -2.276  1.00 39.54  ?  3   ARG B CB  1 
ATOM   2338 C CG  . ARG C 3 4   ? 31.038 25.541  -3.401  1.00 41.89  ?  3   ARG B CG  1 
ATOM   2339 C CD  . ARG C 3 4   ? 30.424 26.182  -4.613  1.00 49.51  ?  3   ARG B CD  1 
ATOM   2340 N NE  . ARG C 3 4   ? 30.364 25.194  -5.668  1.00 53.65  ?  3   ARG B NE  1 
ATOM   2341 C CZ  . ARG C 3 4   ? 30.386 25.465  -6.963  1.00 49.69  ?  3   ARG B CZ  1 
ATOM   2342 N NH1 . ARG C 3 4   ? 30.469 26.730  -7.393  1.00 54.34  ?  3   ARG B NH1 1 
ATOM   2343 N NH2 . ARG C 3 4   ? 30.325 24.449  -7.821  1.00 46.23  ?  3   ARG B NH2 1 
ATOM   2344 N N   . THR C 3 5   ? 29.717 25.612  1.111   1.00 33.67  ?  4   THR B N   1 
ATOM   2345 C CA  . THR C 3 5   ? 28.826 25.493  2.249   1.00 35.54  ?  4   THR B CA  1 
ATOM   2346 C C   . THR C 3 5   ? 27.399 25.819  1.829   1.00 31.06  ?  4   THR B C   1 
ATOM   2347 O O   . THR C 3 5   ? 27.191 26.709  1.000   1.00 33.88  ?  4   THR B O   1 
ATOM   2348 C CB  . THR C 3 5   ? 29.237 26.466  3.363   1.00 43.03  ?  4   THR B CB  1 
ATOM   2349 O OG1 . THR C 3 5   ? 30.658 26.590  3.409   1.00 49.73  ?  4   THR B OG1 1 
ATOM   2350 C CG2 . THR C 3 5   ? 28.718 25.965  4.686   1.00 42.86  ?  4   THR B CG2 1 
ATOM   2351 N N   . PRO C 3 6   ? 26.404 25.150  2.402   1.00 29.29  ?  5   PRO B N   1 
ATOM   2352 C CA  . PRO C 3 6   ? 25.017 25.492  2.069   1.00 30.22  ?  5   PRO B CA  1 
ATOM   2353 C C   . PRO C 3 6   ? 24.598 26.839  2.633   1.00 37.38  ?  5   PRO B C   1 
ATOM   2354 O O   . PRO C 3 6   ? 24.864 27.171  3.791   1.00 35.51  ?  5   PRO B O   1 
ATOM   2355 C CB  . PRO C 3 6   ? 24.205 24.363  2.705   1.00 32.00  ?  5   PRO B CB  1 
ATOM   2356 C CG  . PRO C 3 6   ? 25.064 23.897  3.857   1.00 39.90  ?  5   PRO B CG  1 
ATOM   2357 C CD  . PRO C 3 6   ? 26.485 24.031  3.354   1.00 33.68  ?  5   PRO B CD  1 
ATOM   2358 N N   . LYS C 3 7   ? 23.932 27.614  1.796   1.00 34.94  ?  6   LYS B N   1 
ATOM   2359 C CA  . LYS C 3 7   ? 23.113 28.725  2.250   1.00 29.44  ?  6   LYS B CA  1 
ATOM   2360 C C   . LYS C 3 7   ? 21.735 28.204  2.636   1.00 34.53  ?  6   LYS B C   1 
ATOM   2361 O O   . LYS C 3 7   ? 21.161 27.365  1.938   1.00 38.20  ?  6   LYS B O   1 
ATOM   2362 C CB  . LYS C 3 7   ? 23.035 29.770  1.147   1.00 37.96  ?  6   LYS B CB  1 
ATOM   2363 C CG  . LYS C 3 7   ? 24.385 30.432  0.897   1.00 41.51  ?  6   LYS B CG  1 
ATOM   2364 C CD  . LYS C 3 7   ? 25.164 29.712  -0.201  1.00 52.09  ?  6   LYS B CD  1 
ATOM   2365 C CE  . LYS C 3 7   ? 26.522 30.358  -0.487  1.00 57.47  ?  6   LYS B CE  1 
ATOM   2366 N NZ  . LYS C 3 7   ? 27.577 29.299  -0.704  1.00 56.88  ?  6   LYS B NZ  1 
ATOM   2367 N N   . ILE C 3 8   ? 21.216 28.678  3.767   1.00 32.09  ?  7   ILE B N   1 
ATOM   2368 C CA  . ILE C 3 8   ? 20.010 28.122  4.372   1.00 34.11  ?  7   ILE B CA  1 
ATOM   2369 C C   . ILE C 3 8   ? 18.984 29.228  4.554   1.00 36.83  ?  7   ILE B C   1 
ATOM   2370 O O   . ILE C 3 8   ? 19.308 30.295  5.080   1.00 34.05  ?  7   ILE B O   1 
ATOM   2371 C CB  . ILE C 3 8   ? 20.308 27.461  5.731   1.00 31.79  ?  7   ILE B CB  1 
ATOM   2372 C CG1 . ILE C 3 8   ? 21.302 26.308  5.549   1.00 33.62  ?  7   ILE B CG1 1 
ATOM   2373 C CG2 . ILE C 3 8   ? 18.998 27.015  6.378   1.00 37.35  ?  7   ILE B CG2 1 
ATOM   2374 C CD1 . ILE C 3 8   ? 22.275 26.136  6.712   1.00 37.56  ?  7   ILE B CD1 1 
ATOM   2375 N N   . GLN C 3 9   ? 17.743 28.957  4.164   1.00 33.75  ?  8   GLN B N   1 
ATOM   2376 C CA  . GLN C 3 9   ? 16.644 29.891  4.377   1.00 34.92  ?  8   GLN B CA  1 
ATOM   2377 C C   . GLN C 3 9   ? 15.462 29.120  4.924   1.00 36.43  ?  8   GLN B C   1 
ATOM   2378 O O   . GLN C 3 9   ? 15.092 28.085  4.362   1.00 34.78  ?  8   GLN B O   1 
ATOM   2379 C CB  . GLN C 3 9   ? 16.221 30.590  3.088   1.00 34.13  ?  8   GLN B CB  1 
ATOM   2380 C CG  . GLN C 3 9   ? 17.265 31.484  2.487   1.00 34.79  ?  8   GLN B CG  1 
ATOM   2381 C CD  . GLN C 3 9   ? 16.711 32.319  1.351   1.00 40.90  ?  8   GLN B CD  1 
ATOM   2382 O OE1 . GLN C 3 9   ? 16.063 33.341  1.570   1.00 38.17  ?  8   GLN B OE1 1 
ATOM   2383 N NE2 . GLN C 3 9   ? 16.966 31.884  0.125   1.00 39.16  ?  8   GLN B NE2 1 
ATOM   2384 N N   . VAL C 3 10  ? 14.870 29.615  6.009   1.00 33.00  ?  9   VAL B N   1 
ATOM   2385 C CA  . VAL C 3 10  ? 13.695 29.011  6.615   1.00 33.03  ?  9   VAL B CA  1 
ATOM   2386 C C   . VAL C 3 10  ? 12.583 30.046  6.570   1.00 39.31  ?  9   VAL B C   1 
ATOM   2387 O O   . VAL C 3 10  ? 12.788 31.197  6.967   1.00 41.29  ?  9   VAL B O   1 
ATOM   2388 C CB  . VAL C 3 10  ? 13.967 28.554  8.060   1.00 37.38  ?  9   VAL B CB  1 
ATOM   2389 C CG1 . VAL C 3 10  ? 12.817 27.707  8.573   1.00 36.25  ?  9   VAL B CG1 1 
ATOM   2390 C CG2 . VAL C 3 10  ? 15.278 27.774  8.120   1.00 42.41  ?  9   VAL B CG2 1 
ATOM   2391 N N   . TYR C 3 11  ? 11.413 29.640  6.089   1.00 37.92  ?  10  TYR B N   1 
ATOM   2392 C CA  . TYR C 3 11  ? 10.354 30.587  5.772   1.00 36.35  ?  10  TYR B CA  1 
ATOM   2393 C C   . TYR C 3 11  ? 9.066  29.804  5.576   1.00 39.21  ?  10  TYR B C   1 
ATOM   2394 O O   . TYR C 3 11  ? 9.071  28.574  5.501   1.00 39.94  ?  10  TYR B O   1 
ATOM   2395 C CB  . TYR C 3 11  ? 10.701 31.420  4.527   1.00 39.28  ?  10  TYR B CB  1 
ATOM   2396 C CG  . TYR C 3 11  ? 11.043 30.593  3.300   1.00 36.91  ?  10  TYR B CG  1 
ATOM   2397 C CD1 . TYR C 3 11  ? 12.242 29.888  3.220   1.00 37.59  ?  10  TYR B CD1 1 
ATOM   2398 C CD2 . TYR C 3 11  ? 10.175 30.523  2.236   1.00 33.59  ?  10  TYR B CD2 1 
ATOM   2399 C CE1 . TYR C 3 11  ? 12.559 29.136  2.099   1.00 39.14  ?  10  TYR B CE1 1 
ATOM   2400 C CE2 . TYR C 3 11  ? 10.475 29.765  1.109   1.00 38.65  ?  10  TYR B CE2 1 
ATOM   2401 C CZ  . TYR C 3 11  ? 11.669 29.081  1.045   1.00 35.09  ?  10  TYR B CZ  1 
ATOM   2402 O OH  . TYR C 3 11  ? 11.970 28.346  -0.077  1.00 34.61  ?  10  TYR B OH  1 
ATOM   2403 N N   . SER C 3 12  ? 7.957  30.533  5.504   1.00 40.51  ?  11  SER B N   1 
ATOM   2404 C CA  . SER C 3 12  ? 6.653  29.943  5.243   1.00 39.70  ?  11  SER B CA  1 
ATOM   2405 C C   . SER C 3 12  ? 6.288  30.158  3.781   1.00 43.04  ?  11  SER B C   1 
ATOM   2406 O O   . SER C 3 12  ? 6.741  31.113  3.134   1.00 38.43  ?  11  SER B O   1 
ATOM   2407 C CB  . SER C 3 12  ? 5.557  30.537  6.143   1.00 41.80  ?  11  SER B CB  1 
ATOM   2408 O OG  . SER C 3 12  ? 5.553  31.954  6.098   1.00 45.34  ?  11  SER B OG  1 
ATOM   2409 N N   . ARG C 3 13  ? 5.468  29.247  3.259   1.00 43.13  ?  12  ARG B N   1 
ATOM   2410 C CA  . ARG C 3 13  ? 5.013  29.380  1.882   1.00 44.20  ?  12  ARG B CA  1 
ATOM   2411 C C   . ARG C 3 13  ? 4.163  30.633  1.715   1.00 43.66  ?  12  ARG B C   1 
ATOM   2412 O O   . ARG C 3 13  ? 4.344  31.398  0.764   1.00 46.60  ?  12  ARG B O   1 
ATOM   2413 C CB  . ARG C 3 13  ? 4.233  28.135  1.468   1.00 44.16  ?  12  ARG B CB  1 
ATOM   2414 C CG  . ARG C 3 13  ? 3.685  28.229  0.046   1.00 45.40  ?  12  ARG B CG  1 
ATOM   2415 C CD  . ARG C 3 13  ? 2.859  27.005  -0.350  1.00 44.78  ?  12  ARG B CD  1 
ATOM   2416 N NE  . ARG C 3 13  ? 3.635  25.766  -0.341  1.00 48.54  ?  12  ARG B NE  1 
ATOM   2417 C CZ  . ARG C 3 13  ? 3.100  24.563  -0.490  1.00 45.72  ?  12  ARG B CZ  1 
ATOM   2418 N NH1 . ARG C 3 13  ? 1.796  24.454  -0.668  1.00 51.20  ?  12  ARG B NH1 1 
ATOM   2419 N NH2 . ARG C 3 13  ? 3.854  23.475  -0.465  1.00 45.58  ?  12  ARG B NH2 1 
ATOM   2420 N N   . HIS C 3 14  ? 3.247  30.865  2.640   1.00 46.25  ?  13  HIS B N   1 
ATOM   2421 C CA  . HIS C 3 14  ? 2.376  32.019  2.648   1.00 45.65  ?  13  HIS B CA  1 
ATOM   2422 C C   . HIS C 3 14  ? 2.726  32.930  3.813   1.00 51.65  ?  13  HIS B C   1 
ATOM   2423 O O   . HIS C 3 14  ? 3.380  32.509  4.774   1.00 47.06  ?  13  HIS B O   1 
ATOM   2424 C CB  . HIS C 3 14  ? 0.904  31.600  2.769   1.00 47.87  ?  13  HIS B CB  1 
ATOM   2425 C CG  . HIS C 3 14  ? 0.481  30.583  1.759   1.00 46.01  ?  13  HIS B CG  1 
ATOM   2426 N ND1 . HIS C 3 14  ? 0.651  30.767  0.406   1.00 48.25  ?  13  HIS B ND1 1 
ATOM   2427 C CD2 . HIS C 3 14  ? -0.099 29.368  1.905   1.00 49.12  ?  13  HIS B CD2 1 
ATOM   2428 C CE1 . HIS C 3 14  ? 0.195  29.708  -0.240  1.00 48.12  ?  13  HIS B CE1 1 
ATOM   2429 N NE2 . HIS C 3 14  ? -0.265 28.845  0.646   1.00 47.75  ?  13  HIS B NE2 1 
ATOM   2430 N N   . PRO C 3 15  ? 2.299  34.191  3.764   1.00 53.70  ?  14  PRO B N   1 
ATOM   2431 C CA  . PRO C 3 15  ? 2.427  35.051  4.947   1.00 53.99  ?  14  PRO B CA  1 
ATOM   2432 C C   . PRO C 3 15  ? 1.800  34.375  6.164   1.00 48.40  ?  14  PRO B C   1 
ATOM   2433 O O   . PRO C 3 15  ? 0.706  33.811  6.095   1.00 51.89  ?  14  PRO B O   1 
ATOM   2434 C CB  . PRO C 3 15  ? 1.681  36.330  4.547   1.00 58.06  ?  14  PRO B CB  1 
ATOM   2435 C CG  . PRO C 3 15  ? 1.587  36.285  3.024   1.00 55.35  ?  14  PRO B CG  1 
ATOM   2436 C CD  . PRO C 3 15  ? 1.564  34.836  2.660   1.00 53.00  ?  14  PRO B CD  1 
ATOM   2437 N N   . ALA C 3 16  ? 2.508  34.429  7.286   1.00 46.01  ?  15  ALA B N   1 
ATOM   2438 C CA  . ALA C 3 16  ? 2.129  33.638  8.446   1.00 49.84  ?  15  ALA B CA  1 
ATOM   2439 C C   . ALA C 3 16  ? 0.976  34.283  9.196   1.00 54.27  ?  15  ALA B C   1 
ATOM   2440 O O   . ALA C 3 16  ? 0.966  35.495  9.427   1.00 58.89  ?  15  ALA B O   1 
ATOM   2441 C CB  . ALA C 3 16  ? 3.317  33.468  9.392   1.00 50.35  ?  15  ALA B CB  1 
ATOM   2442 N N   . GLU C 3 17  ? 0.007  33.456  9.582   1.00 53.80  ?  16  GLU B N   1 
ATOM   2443 C CA  . GLU C 3 17  ? -1.146 33.887  10.362  1.00 59.40  ?  16  GLU B CA  1 
ATOM   2444 C C   . GLU C 3 17  ? -1.484 32.754  11.317  1.00 60.78  ?  16  GLU B C   1 
ATOM   2445 O O   . GLU C 3 17  ? -1.734 31.625  10.879  1.00 57.46  ?  16  GLU B O   1 
ATOM   2446 C CB  . GLU C 3 17  ? -2.341 34.238  9.468   1.00 60.47  ?  16  GLU B CB  1 
ATOM   2447 C CG  . GLU C 3 17  ? -2.138 35.529  8.678   1.00 57.57  ?  16  GLU B CG  1 
ATOM   2448 C CD  . GLU C 3 17  ? -3.443 36.180  8.262   1.00 64.07  ?  16  GLU B CD  1 
ATOM   2449 O OE1 . GLU C 3 17  ? -4.155 36.705  9.151   1.00 59.22  ?  16  GLU B OE1 1 
ATOM   2450 O OE2 . GLU C 3 17  ? -3.753 36.163  7.046   1.00 70.36  -1 16  GLU B OE2 1 
ATOM   2451 N N   . ASN C 3 18  ? -1.457 33.056  12.615  1.00 61.86  ?  17  ASN B N   1 
ATOM   2452 C CA  . ASN C 3 18  ? -1.655 32.046  13.645  1.00 66.08  ?  17  ASN B CA  1 
ATOM   2453 C C   . ASN C 3 18  ? -2.946 31.276  13.415  1.00 64.33  ?  17  ASN B C   1 
ATOM   2454 O O   . ASN C 3 18  ? -3.969 31.839  13.017  1.00 67.04  ?  17  ASN B O   1 
ATOM   2455 C CB  . ASN C 3 18  ? -1.670 32.710  15.023  1.00 60.56  ?  17  ASN B CB  1 
ATOM   2456 C CG  . ASN C 3 18  ? -0.276 33.046  15.522  1.00 65.25  ?  17  ASN B CG  1 
ATOM   2457 O OD1 . ASN C 3 18  ? 0.658  33.172  14.739  1.00 63.65  ?  17  ASN B OD1 1 
ATOM   2458 N ND2 . ASN C 3 18  ? -0.127 33.176  16.832  1.00 69.52  ?  17  ASN B ND2 1 
ATOM   2459 N N   . GLY C 3 19  ? -2.880 29.968  13.645  1.00 61.56  ?  18  GLY B N   1 
ATOM   2460 C CA  . GLY C 3 19  ? -4.040 29.112  13.548  1.00 65.46  ?  18  GLY B CA  1 
ATOM   2461 C C   . GLY C 3 19  ? -4.451 28.692  12.154  1.00 64.74  ?  18  GLY B C   1 
ATOM   2462 O O   . GLY C 3 19  ? -5.299 27.801  12.026  1.00 66.78  ?  18  GLY B O   1 
ATOM   2463 N N   . LYS C 3 20  ? -3.909 29.297  11.103  1.00 63.42  ?  19  LYS B N   1 
ATOM   2464 C CA  . LYS C 3 20  ? -4.275 28.936  9.740   1.00 65.82  ?  19  LYS B CA  1 
ATOM   2465 C C   . LYS C 3 20  ? -3.160 28.124  9.091   1.00 66.43  ?  19  LYS B C   1 
ATOM   2466 O O   . LYS C 3 20  ? -1.973 28.404  9.292   1.00 61.89  ?  19  LYS B O   1 
ATOM   2467 C CB  . LYS C 3 20  ? -4.601 30.182  8.911   1.00 64.52  ?  19  LYS B CB  1 
ATOM   2468 C CG  . LYS C 3 20  ? -5.896 30.911  9.346   1.00 72.75  ?  19  LYS B CG  1 
ATOM   2469 C CD  . LYS C 3 20  ? -6.973 29.998  9.999   1.00 76.13  ?  19  LYS B CD  1 
ATOM   2470 C CE  . LYS C 3 20  ? -7.783 29.186  8.974   1.00 74.22  ?  19  LYS B CE  1 
ATOM   2471 N NZ  . LYS C 3 20  ? -9.247 29.097  9.272   1.00 70.88  ?  19  LYS B NZ  1 
ATOM   2472 N N   . SER C 3 21  ? -3.555 27.110  8.316   1.00 69.82  ?  20  SER B N   1 
ATOM   2473 C CA  . SER C 3 21  ? -2.612 26.141  7.772   1.00 64.31  ?  20  SER B CA  1 
ATOM   2474 C C   . SER C 3 21  ? -1.659 26.796  6.778   1.00 57.09  ?  20  SER B C   1 
ATOM   2475 O O   . SER C 3 21  ? -2.029 27.711  6.038   1.00 55.61  ?  20  SER B O   1 
ATOM   2476 C CB  . SER C 3 21  ? -3.368 24.990  7.104   1.00 62.12  ?  20  SER B CB  1 
ATOM   2477 O OG  . SER C 3 21  ? -2.622 23.778  7.158   1.00 68.47  ?  20  SER B OG  1 
ATOM   2478 N N   . ASN C 3 22  ? -0.416 26.322  6.784   1.00 55.12  ?  21  ASN B N   1 
ATOM   2479 C CA  . ASN C 3 22  ? 0.667  26.868  5.975   1.00 56.42  ?  21  ASN B CA  1 
ATOM   2480 C C   . ASN C 3 22  ? 1.656  25.729  5.748   1.00 54.26  ?  21  ASN B C   1 
ATOM   2481 O O   . ASN C 3 22  ? 1.452  24.600  6.214   1.00 50.43  ?  21  ASN B O   1 
ATOM   2482 C CB  . ASN C 3 22  ? 1.316  28.085  6.664   1.00 45.79  ?  21  ASN B CB  1 
ATOM   2483 C CG  . ASN C 3 22  ? 1.901  29.103  5.682   1.00 51.00  ?  21  ASN B CG  1 
ATOM   2484 O OD1 . ASN C 3 22  ? 2.452  28.752  4.631   1.00 50.98  ?  21  ASN B OD1 1 
ATOM   2485 N ND2 . ASN C 3 22  ? 1.802  30.379  6.038   1.00 46.84  ?  21  ASN B ND2 1 
ATOM   2486 N N   . PHE C 3 23  ? 2.721  26.028  5.011   1.00 50.42  ?  22  PHE B N   1 
ATOM   2487 C CA  . PHE C 3 23  ? 3.844  25.123  4.829   1.00 50.42  ?  22  PHE B CA  1 
ATOM   2488 C C   . PHE C 3 23  ? 5.104  25.802  5.359   1.00 44.23  ?  22  PHE B C   1 
ATOM   2489 O O   . PHE C 3 23  ? 5.336  26.989  5.102   1.00 42.16  ?  22  PHE B O   1 
ATOM   2490 C CB  . PHE C 3 23  ? 4.017  24.746  3.345   1.00 48.31  ?  22  PHE B CB  1 
ATOM   2491 C CG  . PHE C 3 23  ? 3.131  23.597  2.888   1.00 54.93  ?  22  PHE B CG  1 
ATOM   2492 C CD1 . PHE C 3 23  ? 3.551  22.278  3.031   1.00 51.96  ?  22  PHE B CD1 1 
ATOM   2493 C CD2 . PHE C 3 23  ? 1.893  23.840  2.300   1.00 53.05  ?  22  PHE B CD2 1 
ATOM   2494 C CE1 . PHE C 3 23  ? 2.752  21.229  2.608   1.00 52.33  ?  22  PHE B CE1 1 
ATOM   2495 C CE2 . PHE C 3 23  ? 1.090  22.789  1.872   1.00 53.04  ?  22  PHE B CE2 1 
ATOM   2496 C CZ  . PHE C 3 23  ? 1.522  21.484  2.030   1.00 51.46  ?  22  PHE B CZ  1 
ATOM   2497 N N   . LEU C 3 24  ? 5.894  25.048  6.121   1.00 42.69  ?  23  LEU B N   1 
ATOM   2498 C CA  . LEU C 3 24  ? 7.208  25.477  6.581   1.00 38.65  ?  23  LEU B CA  1 
ATOM   2499 C C   . LEU C 3 24  ? 8.271  24.905  5.654   1.00 38.54  ?  23  LEU B C   1 
ATOM   2500 O O   . LEU C 3 24  ? 8.330  23.690  5.447   1.00 36.83  ?  23  LEU B O   1 
ATOM   2501 C CB  . LEU C 3 24  ? 7.459  25.012  8.015   1.00 46.42  ?  23  LEU B CB  1 
ATOM   2502 C CG  . LEU C 3 24  ? 8.819  25.330  8.650   1.00 40.04  ?  23  LEU B CG  1 
ATOM   2503 C CD1 . LEU C 3 24  ? 8.951  26.793  9.009   1.00 42.25  ?  23  LEU B CD1 1 
ATOM   2504 C CD2 . LEU C 3 24  ? 9.016  24.439  9.888   1.00 38.15  ?  23  LEU B CD2 1 
ATOM   2505 N N   . ASN C 3 25  ? 9.112  25.779  5.111   1.00 37.97  ?  24  ASN B N   1 
ATOM   2506 C CA  . ASN C 3 25  ? 10.095 25.414  4.105   1.00 38.48  ?  24  ASN B CA  1 
ATOM   2507 C C   . ASN C 3 25  ? 11.499 25.649  4.646   1.00 38.17  ?  24  ASN B C   1 
ATOM   2508 O O   . ASN C 3 25  ? 11.744 26.633  5.348   1.00 35.81  ?  24  ASN B O   1 
ATOM   2509 C CB  . ASN C 3 25  ? 9.915  26.239  2.822   1.00 34.37  ?  24  ASN B CB  1 
ATOM   2510 C CG  . ASN C 3 25  ? 8.632  25.917  2.078   1.00 37.31  ?  24  ASN B CG  1 
ATOM   2511 O OD1 . ASN C 3 25  ? 8.099  24.805  2.161   1.00 36.14  ?  24  ASN B OD1 1 
ATOM   2512 N ND2 . ASN C 3 25  ? 8.140  26.898  1.317   1.00 41.55  ?  24  ASN B ND2 1 
ATOM   2513 N N   . CYS C 3 26  ? 12.426 24.762  4.294   1.00 35.36  ?  25  CYS B N   1 
ATOM   2514 C CA  . CYS C 3 26  ? 13.852 25.006  4.488   1.00 29.30  ?  25  CYS B CA  1 
ATOM   2515 C C   . CYS C 3 26  ? 14.539 24.789  3.151   1.00 31.01  ?  25  CYS B C   1 
ATOM   2516 O O   . CYS C 3 26  ? 14.567 23.666  2.642   1.00 29.91  ?  25  CYS B O   1 
ATOM   2517 C CB  . CYS C 3 26  ? 14.436 24.101  5.567   1.00 30.39  ?  25  CYS B CB  1 
ATOM   2518 S SG  . CYS C 3 26  ? 16.163 24.401  5.819   1.00 38.22  ?  25  CYS B SG  1 
ATOM   2519 N N   . TYR C 3 27  ? 15.070 25.869  2.583   1.00 30.80  ?  26  TYR B N   1 
ATOM   2520 C CA  . TYR C 3 27  ? 15.698 25.863  1.272   1.00 35.72  ?  26  TYR B CA  1 
ATOM   2521 C C   . TYR C 3 27  ? 17.200 25.926  1.490   1.00 37.31  ?  26  TYR B C   1 
ATOM   2522 O O   . TYR C 3 27  ? 17.695 26.842  2.156   1.00 31.19  ?  26  TYR B O   1 
ATOM   2523 C CB  . TYR C 3 27  ? 15.223 27.047  0.426   1.00 31.85  ?  26  TYR B CB  1 
ATOM   2524 C CG  . TYR C 3 27  ? 15.735 27.070  -0.995  1.00 34.39  ?  26  TYR B CG  1 
ATOM   2525 C CD1 . TYR C 3 27  ? 15.375 26.067  -1.908  1.00 34.73  ?  26  TYR B CD1 1 
ATOM   2526 C CD2 . TYR C 3 27  ? 16.553 28.103  -1.443  1.00 36.09  ?  26  TYR B CD2 1 
ATOM   2527 C CE1 . TYR C 3 27  ? 15.834 26.093  -3.239  1.00 34.59  ?  26  TYR B CE1 1 
ATOM   2528 C CE2 . TYR C 3 27  ? 17.019 28.139  -2.757  1.00 34.91  ?  26  TYR B CE2 1 
ATOM   2529 C CZ  . TYR C 3 27  ? 16.647 27.127  -3.652  1.00 37.83  ?  26  TYR B CZ  1 
ATOM   2530 O OH  . TYR C 3 27  ? 17.101 27.169  -4.947  1.00 38.72  ?  26  TYR B OH  1 
ATOM   2531 N N   . VAL C 3 28  ? 17.915 24.941  0.965   1.00 28.98  ?  27  VAL B N   1 
ATOM   2532 C CA  . VAL C 3 28  ? 19.364 24.892  1.063   1.00 26.92  ?  27  VAL B CA  1 
ATOM   2533 C C   . VAL C 3 28  ? 19.907 24.932  -0.347  1.00 29.97  ?  27  VAL B C   1 
ATOM   2534 O O   . VAL C 3 28  ? 19.491 24.135  -1.200  1.00 29.08  ?  27  VAL B O   1 
ATOM   2535 C CB  . VAL C 3 28  ? 19.850 23.632  1.805   1.00 28.64  ?  27  VAL B CB  1 
ATOM   2536 C CG1 . VAL C 3 28  ? 19.490 23.707  3.245   1.00 32.52  ?  27  VAL B CG1 1 
ATOM   2537 C CG2 . VAL C 3 28  ? 19.216 22.357  1.168   1.00 35.22  ?  27  VAL B CG2 1 
ATOM   2538 N N   . SER C 3 29  ? 20.837 25.839  -0.589  1.00 30.28  ?  28  SER B N   1 
ATOM   2539 C CA  . SER C 3 29  ? 21.376 26.009  -1.923  1.00 34.11  ?  28  SER B CA  1 
ATOM   2540 C C   . SER C 3 29  ? 22.842 26.386  -1.844  1.00 32.33  ?  28  SER B C   1 
ATOM   2541 O O   . SER C 3 29  ? 23.384 26.673  -0.773  1.00 32.85  ?  28  SER B O   1 
ATOM   2542 C CB  . SER C 3 29  ? 20.595 27.083  -2.698  1.00 34.75  ?  28  SER B CB  1 
ATOM   2543 O OG  . SER C 3 29  ? 20.417 28.234  -1.891  1.00 35.89  ?  28  SER B OG  1 
ATOM   2544 N N   . GLY C 3 30  ? 23.465 26.419  -3.019  1.00 25.45  ?  29  GLY B N   1 
ATOM   2545 C CA  . GLY C 3 30  ? 24.850 26.769  -3.186  1.00 27.79  ?  29  GLY B CA  1 
ATOM   2546 C C   . GLY C 3 30  ? 25.851 25.816  -2.570  1.00 27.44  ?  29  GLY B C   1 
ATOM   2547 O O   . GLY C 3 30  ? 26.982 26.219  -2.302  1.00 34.38  ?  29  GLY B O   1 
ATOM   2548 N N   . PHE C 3 31  ? 25.484 24.574  -2.328  1.00 30.43  ?  30  PHE B N   1 
ATOM   2549 C CA  . PHE C 3 31  ? 26.396 23.643  -1.683  1.00 30.78  ?  30  PHE B CA  1 
ATOM   2550 C C   . PHE C 3 31  ? 26.909 22.593  -2.663  1.00 35.02  ?  30  PHE B C   1 
ATOM   2551 O O   . PHE C 3 31  ? 26.245 22.249  -3.653  1.00 27.51  ?  30  PHE B O   1 
ATOM   2552 C CB  . PHE C 3 31  ? 25.740 22.961  -0.485  1.00 26.13  ?  30  PHE B CB  1 
ATOM   2553 C CG  . PHE C 3 31  ? 24.527 22.122  -0.811  1.00 31.28  ?  30  PHE B CG  1 
ATOM   2554 C CD1 . PHE C 3 31  ? 23.264 22.695  -0.871  1.00 32.97  ?  30  PHE B CD1 1 
ATOM   2555 C CD2 . PHE C 3 31  ? 24.643 20.754  -1.001  1.00 27.50  ?  30  PHE B CD2 1 
ATOM   2556 C CE1 . PHE C 3 31  ? 22.147 21.934  -1.146  1.00 30.84  ?  30  PHE B CE1 1 
ATOM   2557 C CE2 . PHE C 3 31  ? 23.540 19.989  -1.270  1.00 27.51  ?  30  PHE B CE2 1 
ATOM   2558 C CZ  . PHE C 3 31  ? 22.277 20.578  -1.339  1.00 30.89  ?  30  PHE B CZ  1 
ATOM   2559 N N   . HIS C 3 32  ? 28.107 22.080  -2.351  1.00 32.76  ?  31  HIS B N   1 
ATOM   2560 C CA  . HIS C 3 32  ? 28.798 21.038  -3.113  1.00 34.98  ?  31  HIS B CA  1 
ATOM   2561 C C   . HIS C 3 32  ? 29.801 20.395  -2.169  1.00 34.69  ?  31  HIS B C   1 
ATOM   2562 O O   . HIS C 3 32  ? 30.544 21.129  -1.502  1.00 34.84  ?  31  HIS B O   1 
ATOM   2563 C CB  . HIS C 3 32  ? 29.521 21.613  -4.332  1.00 32.18  ?  31  HIS B CB  1 
ATOM   2564 C CG  . HIS C 3 32  ? 29.432 20.745  -5.551  1.00 34.81  ?  31  HIS B CG  1 
ATOM   2565 N ND1 . HIS C 3 32  ? 30.137 19.569  -5.678  1.00 32.93  ?  31  HIS B ND1 1 
ATOM   2566 C CD2 . HIS C 3 32  ? 28.737 20.893  -6.711  1.00 30.90  ?  31  HIS B CD2 1 
ATOM   2567 C CE1 . HIS C 3 32  ? 29.865 19.012  -6.844  1.00 31.15  ?  31  HIS B CE1 1 
ATOM   2568 N NE2 . HIS C 3 32  ? 29.014 19.793  -7.489  1.00 32.75  ?  31  HIS B NE2 1 
ATOM   2569 N N   . PRO C 3 33  ? 29.897 19.053  -2.097  1.00 31.17  ?  32  PRO B N   1 
ATOM   2570 C CA  . PRO C 3 33  ? 29.173 18.021  -2.864  1.00 30.67  ?  32  PRO B CA  1 
ATOM   2571 C C   . PRO C 3 33  ? 27.739 17.839  -2.351  1.00 34.63  ?  32  PRO B C   1 
ATOM   2572 O O   . PRO C 3 33  ? 27.272 18.594  -1.476  1.00 26.61  ?  32  PRO B O   1 
ATOM   2573 C CB  . PRO C 3 33  ? 30.021 16.750  -2.656  1.00 31.58  ?  32  PRO B CB  1 
ATOM   2574 C CG  . PRO C 3 33  ? 30.708 16.954  -1.319  1.00 38.71  ?  32  PRO B CG  1 
ATOM   2575 C CD  . PRO C 3 33  ? 30.843 18.467  -1.120  1.00 32.26  ?  32  PRO B CD  1 
ATOM   2576 N N   . SER C 3 34  ? 27.063 16.810  -2.870  1.00 32.32  ?  33  SER B N   1 
ATOM   2577 C CA  . SER C 3 34  ? 25.607 16.772  -2.853  1.00 27.83  ?  33  SER B CA  1 
ATOM   2578 C C   . SER C 3 34  ? 25.016 16.165  -1.596  1.00 29.53  ?  33  SER B C   1 
ATOM   2579 O O   . SER C 3 34  ? 23.861 16.453  -1.295  1.00 28.37  ?  33  SER B O   1 
ATOM   2580 C CB  . SER C 3 34  ? 25.061 15.984  -4.051  1.00 26.88  ?  33  SER B CB  1 
ATOM   2581 O OG  . SER C 3 34  ? 25.557 14.664  -4.059  1.00 30.06  ?  33  SER B OG  1 
ATOM   2582 N N   . ASP C 3 35  ? 25.760 15.335  -0.872  1.00 31.56  ?  34  ASP B N   1 
ATOM   2583 C CA  . ASP C 3 35  ? 25.261 14.773  0.378   1.00 36.55  ?  34  ASP B CA  1 
ATOM   2584 C C   . ASP C 3 35  ? 25.002 15.867  1.424   1.00 30.03  ?  34  ASP B C   1 
ATOM   2585 O O   . ASP C 3 35  ? 25.811 16.775  1.631   1.00 31.09  ?  34  ASP B O   1 
ATOM   2586 C CB  . ASP C 3 35  ? 26.249 13.730  0.908   1.00 40.92  ?  34  ASP B CB  1 
ATOM   2587 C CG  . ASP C 3 35  ? 26.295 12.457  0.043   1.00 57.47  ?  34  ASP B CG  1 
ATOM   2588 O OD1 . ASP C 3 35  ? 25.217 11.997  -0.422  1.00 60.79  ?  34  ASP B OD1 1 
ATOM   2589 O OD2 . ASP C 3 35  ? 27.410 11.914  -0.163  1.00 62.19  -1 34  ASP B OD2 1 
ATOM   2590 N N   . ILE C 3 36  ? 23.865 15.770  2.099   1.00 30.59  ?  35  ILE B N   1 
ATOM   2591 C CA  . ILE C 3 36  ? 23.452 16.803  3.039   1.00 36.37  ?  35  ILE B CA  1 
ATOM   2592 C C   . ILE C 3 36  ? 22.359 16.194  3.898   1.00 37.72  ?  35  ILE B C   1 
ATOM   2593 O O   . ILE C 3 36  ? 21.637 15.296  3.462   1.00 41.53  ?  35  ILE B O   1 
ATOM   2594 C CB  . ILE C 3 36  ? 22.992 18.076  2.281   1.00 37.91  ?  35  ILE B CB  1 
ATOM   2595 C CG1 . ILE C 3 36  ? 22.747 19.247  3.242   1.00 33.70  ?  35  ILE B CG1 1 
ATOM   2596 C CG2 . ILE C 3 36  ? 21.782 17.766  1.360   1.00 35.65  ?  35  ILE B CG2 1 
ATOM   2597 C CD1 . ILE C 3 36  ? 23.119 20.622  2.589   1.00 36.82  ?  35  ILE B CD1 1 
ATOM   2598 N N   . GLU C 3 37  ? 22.285 16.625  5.145   1.00 39.74  ?  36  GLU B N   1 
ATOM   2599 C CA  . GLU C 3 37  ? 21.221 16.191  6.038   1.00 37.52  ?  36  GLU B CA  1 
ATOM   2600 C C   . GLU C 3 37  ? 20.426 17.419  6.446   1.00 36.00  ?  36  GLU B C   1 
ATOM   2601 O O   . GLU C 3 37  ? 21.007 18.450  6.805   1.00 34.31  ?  36  GLU B O   1 
ATOM   2602 C CB  . GLU C 3 37  ? 21.790 15.463  7.255   1.00 43.23  ?  36  GLU B CB  1 
ATOM   2603 C CG  . GLU C 3 37  ? 20.716 14.779  8.083   1.00 47.90  ?  36  GLU B CG  1 
ATOM   2604 C CD  . GLU C 3 37  ? 21.288 14.062  9.300   1.00 60.84  ?  36  GLU B CD  1 
ATOM   2605 O OE1 . GLU C 3 37  ? 20.515 13.803  10.258  1.00 60.80  ?  36  GLU B OE1 1 
ATOM   2606 O OE2 . GLU C 3 37  ? 22.509 13.755  9.283   1.00 57.27  -1 36  GLU B OE2 1 
ATOM   2607 N N   . VAL C 3 38  ? 19.106 17.334  6.347   1.00 36.92  ?  37  VAL B N   1 
ATOM   2608 C CA  . VAL C 3 38  ? 18.255 18.470  6.682   1.00 38.95  ?  37  VAL B CA  1 
ATOM   2609 C C   . VAL C 3 38  ? 17.081 17.973  7.494   1.00 37.92  ?  37  VAL B C   1 
ATOM   2610 O O   . VAL C 3 38  ? 16.431 16.996  7.109   1.00 36.54  ?  37  VAL B O   1 
ATOM   2611 C CB  . VAL C 3 38  ? 17.770 19.205  5.423   1.00 33.95  ?  37  VAL B CB  1 
ATOM   2612 C CG1 . VAL C 3 38  ? 16.821 20.323  5.780   1.00 35.38  ?  37  VAL B CG1 1 
ATOM   2613 C CG2 . VAL C 3 38  ? 18.970 19.749  4.681   1.00 32.28  ?  37  VAL B CG2 1 
ATOM   2614 N N   . ASP C 3 39  ? 16.817 18.641  8.620   1.00 35.32  ?  38  ASP B N   1 
ATOM   2615 C CA  . ASP C 3 39  ? 15.671 18.350  9.475   1.00 39.91  ?  38  ASP B CA  1 
ATOM   2616 C C   . ASP C 3 39  ? 14.911 19.636  9.759   1.00 37.60  ?  38  ASP B C   1 
ATOM   2617 O O   . ASP C 3 39  ? 15.518 20.699  9.915   1.00 39.26  ?  38  ASP B O   1 
ATOM   2618 C CB  . ASP C 3 39  ? 16.085 17.729  10.817  1.00 45.73  ?  38  ASP B CB  1 
ATOM   2619 C CG  . ASP C 3 39  ? 16.746 16.393  10.655  1.00 46.75  ?  38  ASP B CG  1 
ATOM   2620 O OD1 . ASP C 3 39  ? 16.018 15.404  10.400  1.00 50.22  ?  38  ASP B OD1 1 
ATOM   2621 O OD2 . ASP C 3 39  ? 17.994 16.348  10.778  1.00 54.46  -1 38  ASP B OD2 1 
ATOM   2622 N N   . LEU C 3 40  ? 13.587 19.538  9.815   1.00 37.27  ?  39  LEU B N   1 
ATOM   2623 C CA  . LEU C 3 40  ? 12.748 20.627  10.291  1.00 38.00  ?  39  LEU B CA  1 
ATOM   2624 C C   . LEU C 3 40  ? 12.399 20.362  11.748  1.00 42.92  ?  39  LEU B C   1 
ATOM   2625 O O   . LEU C 3 40  ? 12.135 19.217  12.135  1.00 40.77  ?  39  LEU B O   1 
ATOM   2626 C CB  . LEU C 3 40  ? 11.480 20.776  9.452   1.00 39.09  ?  39  LEU B CB  1 
ATOM   2627 C CG  . LEU C 3 40  ? 11.750 21.077  7.973   1.00 39.76  ?  39  LEU B CG  1 
ATOM   2628 C CD1 . LEU C 3 40  ? 10.469 21.341  7.202   1.00 41.14  ?  39  LEU B CD1 1 
ATOM   2629 C CD2 . LEU C 3 40  ? 12.720 22.245  7.786   1.00 41.42  ?  39  LEU B CD2 1 
ATOM   2630 N N   . LEU C 3 41  ? 12.432 21.417  12.561  1.00 39.74  ?  40  LEU B N   1 
ATOM   2631 C CA  . LEU C 3 41  ? 12.265 21.297  14.001  1.00 41.60  ?  40  LEU B CA  1 
ATOM   2632 C C   . LEU C 3 41  ? 11.065 22.097  14.492  1.00 44.39  ?  40  LEU B C   1 
ATOM   2633 O O   . LEU C 3 41  ? 10.858 23.249  14.088  1.00 43.78  ?  40  LEU B O   1 
ATOM   2634 C CB  . LEU C 3 41  ? 13.522 21.781  14.734  1.00 43.17  ?  40  LEU B CB  1 
ATOM   2635 C CG  . LEU C 3 41  ? 14.848 21.058  14.481  1.00 47.52  ?  40  LEU B CG  1 
ATOM   2636 C CD1 . LEU C 3 41  ? 15.949 21.587  15.399  1.00 45.05  ?  40  LEU B CD1 1 
ATOM   2637 C CD2 . LEU C 3 41  ? 14.640 19.561  14.655  1.00 40.28  ?  40  LEU B CD2 1 
ATOM   2638 N N   . LYS C 3 42  ? 10.285 21.480  15.380  1.00 45.42  ?  41  LYS B N   1 
ATOM   2639 C CA  . LYS C 3 42  ? 9.213  22.151  16.110  1.00 48.80  ?  41  LYS B CA  1 
ATOM   2640 C C   . LYS C 3 42  ? 9.602  22.145  17.585  1.00 46.82  ?  41  LYS B C   1 
ATOM   2641 O O   . LYS C 3 42  ? 9.689  21.076  18.200  1.00 42.85  ?  41  LYS B O   1 
ATOM   2642 C CB  . LYS C 3 42  ? 7.858  21.469  15.892  1.00 47.05  ?  41  LYS B CB  1 
ATOM   2643 C CG  . LYS C 3 42  ? 6.721  22.199  16.599  1.00 49.08  ?  41  LYS B CG  1 
ATOM   2644 C CD  . LYS C 3 42  ? 5.344  21.646  16.263  1.00 55.03  ?  41  LYS B CD  1 
ATOM   2645 C CE  . LYS C 3 42  ? 4.270  22.282  17.159  1.00 53.28  ?  41  LYS B CE  1 
ATOM   2646 N NZ  . LYS C 3 42  ? 2.953  21.589  17.072  1.00 52.16  ?  41  LYS B NZ  1 
ATOM   2647 N N   . ASN C 3 43  ? 9.851  23.334  18.139  1.00 44.78  ?  42  ASN B N   1 
ATOM   2648 C CA  . ASN C 3 43  ? 10.275 23.499  19.538  1.00 46.78  ?  42  ASN B CA  1 
ATOM   2649 C C   . ASN C 3 43  ? 11.446 22.577  19.871  1.00 43.50  ?  42  ASN B C   1 
ATOM   2650 O O   . ASN C 3 43  ? 11.467 21.884  20.891  1.00 41.34  ?  42  ASN B O   1 
ATOM   2651 C CB  . ASN C 3 43  ? 9.098  23.287  20.487  1.00 41.67  ?  42  ASN B CB  1 
ATOM   2652 C CG  . ASN C 3 43  ? 7.979  24.278  20.236  1.00 49.65  ?  42  ASN B CG  1 
ATOM   2653 O OD1 . ASN C 3 43  ? 8.204  25.488  20.202  1.00 40.47  ?  42  ASN B OD1 1 
ATOM   2654 N ND2 . ASN C 3 43  ? 6.775  23.767  20.013  1.00 53.46  ?  42  ASN B ND2 1 
ATOM   2655 N N   . GLY C 3 44  ? 12.448 22.598  18.990  1.00 42.57  ?  43  GLY B N   1 
ATOM   2656 C CA  . GLY C 3 44  ? 13.658 21.836  19.179  1.00 39.81  ?  43  GLY B CA  1 
ATOM   2657 C C   . GLY C 3 44  ? 13.572 20.385  18.773  1.00 37.18  ?  43  GLY B C   1 
ATOM   2658 O O   . GLY C 3 44  ? 14.608 19.714  18.743  1.00 37.37  ?  43  GLY B O   1 
ATOM   2659 N N   . GLU C 3 45  ? 12.382 19.879  18.456  1.00 42.06  ?  44  GLU B N   1 
ATOM   2660 C CA  . GLU C 3 45  ? 12.164 18.456  18.215  1.00 41.45  ?  44  GLU B CA  1 
ATOM   2661 C C   . GLU C 3 45  ? 12.016 18.192  16.721  1.00 45.76  ?  44  GLU B C   1 
ATOM   2662 O O   . GLU C 3 45  ? 11.418 18.989  15.986  1.00 44.38  ?  44  GLU B O   1 
ATOM   2663 C CB  . GLU C 3 45  ? 10.917 17.956  18.959  1.00 42.69  ?  44  GLU B CB  1 
ATOM   2664 C CG  . GLU C 3 45  ? 11.035 17.953  20.497  1.00 36.18  ?  44  GLU B CG  1 
ATOM   2665 C CD  . GLU C 3 45  ? 12.178 17.097  20.997  1.00 40.40  ?  44  GLU B CD  1 
ATOM   2666 O OE1 . GLU C 3 45  ? 12.180 15.876  20.699  1.00 43.17  ?  44  GLU B OE1 1 
ATOM   2667 O OE2 . GLU C 3 45  ? 13.084 17.643  21.676  1.00 37.64  -1 44  GLU B OE2 1 
ATOM   2668 N N   . ARG C 3 46  ? 12.567 17.075  16.268  1.00 44.31  ?  45  ARG B N   1 
ATOM   2669 C CA  . ARG C 3 46  ? 12.501 16.760  14.848  1.00 44.68  ?  45  ARG B CA  1 
ATOM   2670 C C   . ARG C 3 46  ? 11.057 16.538  14.427  1.00 39.33  ?  45  ARG B C   1 
ATOM   2671 O O   . ARG C 3 46  ? 10.333 15.779  15.071  1.00 43.82  ?  45  ARG B O   1 
ATOM   2672 C CB  . ARG C 3 46  ? 13.328 15.519  14.540  1.00 47.13  ?  45  ARG B CB  1 
ATOM   2673 C CG  . ARG C 3 46  ? 13.312 15.129  13.059  1.00 59.34  ?  45  ARG B CG  1 
ATOM   2674 C CD  . ARG C 3 46  ? 14.406 14.100  12.728  1.00 63.60  ?  45  ARG B CD  1 
ATOM   2675 N NE  . ARG C 3 46  ? 14.469 13.049  13.745  1.00 75.97  ?  45  ARG B NE  1 
ATOM   2676 C CZ  . ARG C 3 46  ? 13.553 12.096  13.893  1.00 81.39  ?  45  ARG B CZ  1 
ATOM   2677 N NH1 . ARG C 3 46  ? 12.507 12.053  13.079  1.00 78.11  ?  45  ARG B NH1 1 
ATOM   2678 N NH2 . ARG C 3 46  ? 13.681 11.185  14.853  1.00 90.55  ?  45  ARG B NH2 1 
ATOM   2679 N N   . ILE C 3 47  ? 10.638 17.178  13.333  1.00 41.09  ?  46  ILE B N   1 
ATOM   2680 C CA  . ILE C 3 47  ? 9.322  16.898  12.760  1.00 45.05  ?  46  ILE B CA  1 
ATOM   2681 C C   . ILE C 3 47  ? 9.413  15.636  11.911  1.00 52.86  ?  46  ILE B C   1 
ATOM   2682 O O   . ILE C 3 47  ? 10.373 15.444  11.155  1.00 49.86  ?  46  ILE B O   1 
ATOM   2683 C CB  . ILE C 3 47  ? 8.803  18.089  11.931  1.00 45.63  ?  46  ILE B CB  1 
ATOM   2684 C CG1 . ILE C 3 47  ? 8.650  19.311  12.841  1.00 45.79  ?  46  ILE B CG1 1 
ATOM   2685 C CG2 . ILE C 3 47  ? 7.480  17.712  11.243  1.00 42.44  ?  46  ILE B CG2 1 
ATOM   2686 C CD1 . ILE C 3 47  ? 8.453  20.602  12.138  1.00 44.49  ?  46  ILE B CD1 1 
ATOM   2687 N N   . GLU C 3 48  ? 8.386  14.792  12.001  1.00 52.03  ?  47  GLU B N   1 
ATOM   2688 C CA  . GLU C 3 48  ? 8.463  13.428  11.475  1.00 60.26  ?  47  GLU B CA  1 
ATOM   2689 C C   . GLU C 3 48  ? 8.290  13.359  9.958   1.00 63.69  ?  47  GLU B C   1 
ATOM   2690 O O   . GLU C 3 48  ? 9.219  12.988  9.231   1.00 72.24  ?  47  GLU B O   1 
ATOM   2691 C CB  . GLU C 3 48  ? 7.405  12.580  12.186  1.00 65.02  ?  47  GLU B CB  1 
ATOM   2692 C CG  . GLU C 3 48  ? 7.501  11.082  11.999  1.00 77.59  ?  47  GLU B CG  1 
ATOM   2693 C CD  . GLU C 3 48  ? 6.454  10.341  12.838  1.00 76.68  ?  47  GLU B CD  1 
ATOM   2694 O OE1 . GLU C 3 48  ? 5.287  10.800  12.881  1.00 74.38  ?  47  GLU B OE1 1 
ATOM   2695 O OE2 . GLU C 3 48  ? 6.806  9.311   13.461  1.00 82.38  -1 47  GLU B OE2 1 
ATOM   2696 N N   . LYS C 3 49  ? 7.101  13.679  9.457   1.00 59.88  ?  48  LYS B N   1 
ATOM   2697 C CA  . LYS C 3 49  ? 6.801  13.487  8.035   1.00 64.84  ?  48  LYS B CA  1 
ATOM   2698 C C   . LYS C 3 49  ? 7.233  14.741  7.286   1.00 57.92  ?  48  LYS B C   1 
ATOM   2699 O O   . LYS C 3 49  ? 6.461  15.683  7.096   1.00 59.16  ?  48  LYS B O   1 
ATOM   2700 C CB  . LYS C 3 49  ? 5.325  13.165  7.823   1.00 62.13  ?  48  LYS B CB  1 
ATOM   2701 C CG  . LYS C 3 49  ? 4.915  11.784  8.349   1.00 64.06  ?  48  LYS B CG  1 
ATOM   2702 C CD  . LYS C 3 49  ? 3.433  11.758  8.744   1.00 73.96  ?  48  LYS B CD  1 
ATOM   2703 C CE  . LYS C 3 49  ? 3.134  12.658  9.952   1.00 69.51  ?  48  LYS B CE  1 
ATOM   2704 N NZ  . LYS C 3 49  ? 3.935  12.290  11.172  1.00 69.60  ?  48  LYS B NZ  1 
ATOM   2705 N N   . VAL C 3 50  ? 8.498  14.760  6.878   1.00 49.56  ?  49  VAL B N   1 
ATOM   2706 C CA  . VAL C 3 50  ? 9.069  15.867  6.127   1.00 48.59  ?  49  VAL B CA  1 
ATOM   2707 C C   . VAL C 3 50  ? 9.420  15.374  4.731   1.00 50.77  ?  49  VAL B C   1 
ATOM   2708 O O   . VAL C 3 50  ? 9.963  14.277  4.560   1.00 55.57  ?  49  VAL B O   1 
ATOM   2709 C CB  . VAL C 3 50  ? 10.306 16.458  6.826   1.00 48.12  ?  49  VAL B CB  1 
ATOM   2710 C CG1 . VAL C 3 50  ? 11.072 17.405  5.888   1.00 42.16  ?  49  VAL B CG1 1 
ATOM   2711 C CG2 . VAL C 3 50  ? 9.887  17.180  8.095   1.00 50.83  ?  49  VAL B CG2 1 
ATOM   2712 N N   . GLU C 3 51  ? 9.122  16.194  3.737   1.00 48.13  ?  50  GLU B N   1 
ATOM   2713 C CA  . GLU C 3 51  ? 9.372  15.865  2.347   1.00 43.24  ?  50  GLU B CA  1 
ATOM   2714 C C   . GLU C 3 51  ? 10.412 16.810  1.780   1.00 43.83  ?  50  GLU B C   1 
ATOM   2715 O O   . GLU C 3 51  ? 10.696 17.865  2.357   1.00 40.59  ?  50  GLU B O   1 
ATOM   2716 C CB  . GLU C 3 51  ? 8.077  15.951  1.553   1.00 40.81  ?  50  GLU B CB  1 
ATOM   2717 C CG  . GLU C 3 51  ? 7.066  14.957  2.030   1.00 48.82  ?  50  GLU B CG  1 
ATOM   2718 C CD  . GLU C 3 51  ? 6.289  14.365  0.900   1.00 58.10  ?  50  GLU B CD  1 
ATOM   2719 O OE1 . GLU C 3 51  ? 6.674  13.268  0.421   1.00 63.48  ?  50  GLU B OE1 1 
ATOM   2720 O OE2 . GLU C 3 51  ? 5.308  15.016  0.483   1.00 62.34  -1 50  GLU B OE2 1 
ATOM   2721 N N   . HIS C 3 52  ? 10.979 16.417  0.634   1.00 34.21  ?  51  HIS B N   1 
ATOM   2722 C CA  . HIS C 3 52  ? 11.983 17.235  -0.026  1.00 37.09  ?  51  HIS B CA  1 
ATOM   2723 C C   . HIS C 3 52  ? 11.944 17.013  -1.531  1.00 33.82  ?  51  HIS B C   1 
ATOM   2724 O O   . HIS C 3 52  ? 11.492 15.980  -2.026  1.00 34.47  ?  51  HIS B O   1 
ATOM   2725 C CB  . HIS C 3 52  ? 13.393 16.956  0.513   1.00 38.56  ?  51  HIS B CB  1 
ATOM   2726 C CG  . HIS C 3 52  ? 13.849 15.543  0.330   1.00 40.28  ?  51  HIS B CG  1 
ATOM   2727 N ND1 . HIS C 3 52  ? 14.364 15.075  -0.861  1.00 42.77  ?  51  HIS B ND1 1 
ATOM   2728 C CD2 . HIS C 3 52  ? 13.884 14.499  1.193   1.00 41.36  ?  51  HIS B CD2 1 
ATOM   2729 C CE1 . HIS C 3 52  ? 14.689 13.800  -0.727  1.00 45.55  ?  51  HIS B CE1 1 
ATOM   2730 N NE2 . HIS C 3 52  ? 14.415 13.429  0.511   1.00 48.74  ?  51  HIS B NE2 1 
ATOM   2731 N N   . SER C 3 53  ? 12.406 18.031  -2.235  1.00 34.97  ?  52  SER B N   1 
ATOM   2732 C CA  . SER C 3 53  ? 12.450 18.063  -3.681  1.00 35.35  ?  52  SER B CA  1 
ATOM   2733 C C   . SER C 3 53  ? 13.559 17.155  -4.205  1.00 34.10  ?  52  SER B C   1 
ATOM   2734 O O   . SER C 3 53  ? 14.460 16.734  -3.476  1.00 30.73  ?  52  SER B O   1 
ATOM   2735 C CB  . SER C 3 53  ? 12.691 19.495  -4.155  1.00 30.54  ?  52  SER B CB  1 
ATOM   2736 O OG  . SER C 3 53  ? 13.995 19.929  -3.786  1.00 33.18  ?  52  SER B OG  1 
ATOM   2737 N N   . ASP C 3 54  ? 13.481 16.857  -5.492  1.00 31.76  ?  53  ASP B N   1 
ATOM   2738 C CA  . ASP C 3 54  ? 14.519 16.089  -6.150  1.00 29.02  ?  53  ASP B CA  1 
ATOM   2739 C C   . ASP C 3 54  ? 15.731 16.968  -6.392  1.00 31.43  ?  53  ASP B C   1 
ATOM   2740 O O   . ASP C 3 54  ? 15.606 18.155  -6.727  1.00 31.71  ?  53  ASP B O   1 
ATOM   2741 C CB  . ASP C 3 54  ? 14.017 15.527  -7.477  1.00 34.64  ?  53  ASP B CB  1 
ATOM   2742 C CG  . ASP C 3 54  ? 12.710 14.805  -7.342  1.00 39.87  ?  53  ASP B CG  1 
ATOM   2743 O OD1 . ASP C 3 54  ? 12.605 13.871  -6.504  1.00 42.67  ?  53  ASP B OD1 1 
ATOM   2744 O OD2 . ASP C 3 54  ? 11.788 15.183  -8.088  1.00 41.47  -1 53  ASP B OD2 1 
ATOM   2745 N N   . LEU C 3 55  ? 16.906 16.359  -6.268  1.00 36.55  ?  54  LEU B N   1 
ATOM   2746 C CA  . LEU C 3 55  ? 18.162 17.088  -6.350  1.00 26.11  ?  54  LEU B CA  1 
ATOM   2747 C C   . LEU C 3 55  ? 18.369 17.700  -7.719  1.00 29.55  ?  54  LEU B C   1 
ATOM   2748 O O   . LEU C 3 55  ? 18.334 17.012  -8.750  1.00 27.03  ?  54  LEU B O   1 
ATOM   2749 C CB  . LEU C 3 55  ? 19.330 16.159  -6.021  1.00 24.50  ?  54  LEU B CB  1 
ATOM   2750 C CG  . LEU C 3 55  ? 20.734 16.776  -6.048  1.00 26.87  ?  54  LEU B CG  1 
ATOM   2751 C CD1 . LEU C 3 55  ? 20.889 17.713  -4.831  1.00 31.01  ?  54  LEU B CD1 1 
ATOM   2752 C CD2 . LEU C 3 55  ? 21.812 15.710  -6.030  1.00 26.92  ?  54  LEU B CD2 1 
ATOM   2753 N N   . SER C 3 56  ? 18.653 18.995  -7.720  1.00 27.07  ?  55  SER B N   1 
ATOM   2754 C CA  . SER C 3 56  ? 19.028 19.688  -8.938  1.00 30.40  ?  55  SER B CA  1 
ATOM   2755 C C   . SER C 3 56  ? 20.147 20.649  -8.603  1.00 28.67  ?  55  SER B C   1 
ATOM   2756 O O   . SER C 3 56  ? 20.614 20.724  -7.458  1.00 27.79  ?  55  SER B O   1 
ATOM   2757 C CB  . SER C 3 56  ? 17.836 20.427  -9.558  1.00 30.09  ?  55  SER B CB  1 
ATOM   2758 O OG  . SER C 3 56  ? 18.173 20.896  -10.850 1.00 35.92  ?  55  SER B OG  1 
ATOM   2759 N N   . PHE C 3 57  ? 20.565 21.414  -9.597  1.00 25.08  ?  56  PHE B N   1 
ATOM   2760 C CA  . PHE C 3 57  ? 21.639 22.355  -9.365  1.00 26.73  ?  56  PHE B CA  1 
ATOM   2761 C C   . PHE C 3 57  ? 21.521 23.582  -10.252 1.00 31.08  ?  56  PHE B C   1 
ATOM   2762 O O   . PHE C 3 57  ? 20.794 23.587  -11.249 1.00 29.40  ?  56  PHE B O   1 
ATOM   2763 C CB  . PHE C 3 57  ? 22.984 21.713  -9.604  1.00 29.22  ?  56  PHE B CB  1 
ATOM   2764 C CG  . PHE C 3 57  ? 23.129 21.024  -10.943 1.00 24.89  ?  56  PHE B CG  1 
ATOM   2765 C CD1 . PHE C 3 57  ? 23.598 21.722  -12.049 1.00 29.91  ?  56  PHE B CD1 1 
ATOM   2766 C CD2 . PHE C 3 57  ? 22.877 19.664  -11.067 1.00 25.22  ?  56  PHE B CD2 1 
ATOM   2767 C CE1 . PHE C 3 57  ? 23.801 21.086  -13.256 1.00 27.35  ?  56  PHE B CE1 1 
ATOM   2768 C CE2 . PHE C 3 57  ? 23.090 18.993  -12.285 1.00 26.94  ?  56  PHE B CE2 1 
ATOM   2769 C CZ  . PHE C 3 57  ? 23.536 19.709  -13.380 1.00 28.81  ?  56  PHE B CZ  1 
ATOM   2770 N N   . SER C 3 58  ? 22.332 24.587  -9.917  1.00 26.20  ?  57  SER B N   1 
ATOM   2771 C CA  . SER C 3 58  ? 22.313 25.897  -10.548 1.00 32.49  ?  57  SER B CA  1 
ATOM   2772 C C   . SER C 3 58  ? 23.408 26.013  -11.609 1.00 34.85  ?  57  SER B C   1 
ATOM   2773 O O   . SER C 3 58  ? 24.185 25.081  -11.851 1.00 34.50  ?  57  SER B O   1 
ATOM   2774 C CB  . SER C 3 58  ? 22.482 27.001  -9.490  1.00 29.82  ?  57  SER B CB  1 
ATOM   2775 O OG  . SER C 3 58  ? 21.481 26.923  -8.495  1.00 30.20  ?  57  SER B OG  1 
ATOM   2776 N N   . LYS C 3 59  ? 23.475 27.195  -12.244 1.00 36.80  ?  58  LYS B N   1 
ATOM   2777 C CA  . LYS C 3 59  ? 24.404 27.404  -13.358 1.00 37.00  ?  58  LYS B CA  1 
ATOM   2778 C C   . LYS C 3 59  ? 25.843 27.188  -12.920 1.00 36.41  ?  58  LYS B C   1 
ATOM   2779 O O   . LYS C 3 59  ? 26.671 26.696  -13.703 1.00 34.03  ?  58  LYS B O   1 
ATOM   2780 C CB  . LYS C 3 59  ? 24.244 28.818  -13.945 1.00 33.00  ?  58  LYS B CB  1 
ATOM   2781 N N   . ASP C 3 60  ? 26.175 27.577  -11.683 1.00 30.10  ?  59  ASP B N   1 
ATOM   2782 C CA  . ASP C 3 60  ? 27.528 27.391  -11.175 1.00 33.32  ?  59  ASP B CA  1 
ATOM   2783 C C   . ASP C 3 60  ? 27.788 25.964  -10.697 1.00 32.51  ?  59  ASP B C   1 
ATOM   2784 O O   . ASP C 3 60  ? 28.879 25.689  -10.191 1.00 32.92  ?  59  ASP B O   1 
ATOM   2785 C CB  . ASP C 3 60  ? 27.830 28.389  -10.034 1.00 33.27  ?  59  ASP B CB  1 
ATOM   2786 C CG  . ASP C 3 60  ? 27.033 28.130  -8.772  1.00 33.96  ?  59  ASP B CG  1 
ATOM   2787 O OD1 . ASP C 3 60  ? 26.200 27.187  -8.709  1.00 35.51  ?  59  ASP B OD1 1 
ATOM   2788 O OD2 . ASP C 3 60  ? 27.249 28.878  -7.792  1.00 43.21  -1 59  ASP B OD2 1 
ATOM   2789 N N   . TRP C 3 61  ? 26.808 25.068  -10.826 1.00 29.54  ?  60  TRP B N   1 
ATOM   2790 C CA  . TRP C 3 61  ? 26.877 23.625  -10.531 1.00 30.48  ?  60  TRP B CA  1 
ATOM   2791 C C   . TRP C 3 61  ? 26.605 23.298  -9.075  1.00 33.93  ?  60  TRP B C   1 
ATOM   2792 O O   . TRP C 3 61  ? 26.575 22.092  -8.724  1.00 29.72  ?  60  TRP B O   1 
ATOM   2793 C CB  . TRP C 3 61  ? 28.229 22.998  -10.904 1.00 24.84  ?  60  TRP B CB  1 
ATOM   2794 C CG  . TRP C 3 61  ? 28.640 23.204  -12.328 1.00 30.19  ?  60  TRP B CG  1 
ATOM   2795 C CD1 . TRP C 3 61  ? 29.618 24.045  -12.786 1.00 32.40  ?  60  TRP B CD1 1 
ATOM   2796 C CD2 . TRP C 3 61  ? 28.107 22.545  -13.488 1.00 25.97  ?  60  TRP B CD2 1 
ATOM   2797 N NE1 . TRP C 3 61  ? 29.751 23.919  -14.157 1.00 28.46  ?  60  TRP B NE1 1 
ATOM   2798 C CE2 . TRP C 3 61  ? 28.814 23.028  -14.609 1.00 25.64  ?  60  TRP B CE2 1 
ATOM   2799 C CE3 . TRP C 3 61  ? 27.112 21.583  -13.684 1.00 27.83  ?  60  TRP B CE3 1 
ATOM   2800 C CZ2 . TRP C 3 61  ? 28.551 22.585  -15.903 1.00 33.18  ?  60  TRP B CZ2 1 
ATOM   2801 C CZ3 . TRP C 3 61  ? 26.856 21.149  -14.966 1.00 28.12  ?  60  TRP B CZ3 1 
ATOM   2802 C CH2 . TRP C 3 61  ? 27.573 21.640  -16.056 1.00 27.48  ?  60  TRP B CH2 1 
ATOM   2803 N N   . SER C 3 62  ? 26.412 24.303  -8.217  1.00 29.36  ?  61  SER B N   1 
ATOM   2804 C CA  . SER C 3 62  ? 26.045 24.056  -6.834  1.00 30.69  ?  61  SER B CA  1 
ATOM   2805 C C   . SER C 3 62  ? 24.610 23.547  -6.763  1.00 27.28  ?  61  SER B C   1 
ATOM   2806 O O   . SER C 3 62  ? 23.740 23.930  -7.554  1.00 25.95  ?  61  SER B O   1 
ATOM   2807 C CB  . SER C 3 62  ? 26.238 25.344  -6.001  1.00 29.12  ?  61  SER B CB  1 
ATOM   2808 O OG  . SER C 3 62  ? 25.331 26.359  -6.367  1.00 36.29  ?  61  SER B OG  1 
ATOM   2809 N N   . PHE C 3 63  ? 24.365 22.685  -5.790  1.00 24.95  ?  62  PHE B N   1 
ATOM   2810 C CA  . PHE C 3 63  ? 23.086 22.021  -5.637  1.00 26.60  ?  62  PHE B CA  1 
ATOM   2811 C C   . PHE C 3 63  ? 22.092 22.842  -4.827  1.00 30.89  ?  62  PHE B C   1 
ATOM   2812 O O   . PHE C 3 63  ? 22.455 23.781  -4.108  1.00 32.30  ?  62  PHE B O   1 
ATOM   2813 C CB  . PHE C 3 63  ? 23.294 20.686  -4.952  1.00 29.01  ?  62  PHE B CB  1 
ATOM   2814 C CG  . PHE C 3 63  ? 24.164 19.748  -5.727  1.00 27.61  ?  62  PHE B CG  1 
ATOM   2815 C CD1 . PHE C 3 63  ? 23.662 19.089  -6.842  1.00 25.50  ?  62  PHE B CD1 1 
ATOM   2816 C CD2 . PHE C 3 63  ? 25.484 19.549  -5.356  1.00 28.27  ?  62  PHE B CD2 1 
ATOM   2817 C CE1 . PHE C 3 63  ? 24.465 18.215  -7.589  1.00 23.91  ?  62  PHE B CE1 1 
ATOM   2818 C CE2 . PHE C 3 63  ? 26.299 18.683  -6.067  1.00 29.68  ?  62  PHE B CE2 1 
ATOM   2819 C CZ  . PHE C 3 63  ? 25.791 17.997  -7.188  1.00 30.27  ?  62  PHE B CZ  1 
ATOM   2820 N N   . TYR C 3 64  ? 20.821 22.460  -4.943  1.00 24.61  ?  63  TYR B N   1 
ATOM   2821 C CA  . TYR C 3 64  ? 19.767 23.045  -4.123  1.00 30.53  ?  63  TYR B CA  1 
ATOM   2822 C C   . TYR C 3 64  ? 18.692 22.005  -3.862  1.00 31.94  ?  63  TYR B C   1 
ATOM   2823 O O   . TYR C 3 64  ? 18.387 21.155  -4.714  1.00 31.73  ?  63  TYR B O   1 
ATOM   2824 C CB  . TYR C 3 64  ? 19.155 24.323  -4.757  1.00 32.14  ?  63  TYR B CB  1 
ATOM   2825 C CG  . TYR C 3 64  ? 18.477 24.153  -6.102  1.00 31.24  ?  63  TYR B CG  1 
ATOM   2826 C CD1 . TYR C 3 64  ? 17.167 23.683  -6.181  1.00 35.47  ?  63  TYR B CD1 1 
ATOM   2827 C CD2 . TYR C 3 64  ? 19.140 24.468  -7.293  1.00 31.97  ?  63  TYR B CD2 1 
ATOM   2828 C CE1 . TYR C 3 64  ? 16.521 23.511  -7.419  1.00 37.08  ?  63  TYR B CE1 1 
ATOM   2829 C CE2 . TYR C 3 64  ? 18.505 24.283  -8.550  1.00 36.10  ?  63  TYR B CE2 1 
ATOM   2830 C CZ  . TYR C 3 64  ? 17.191 23.811  -8.595  1.00 32.51  ?  63  TYR B CZ  1 
ATOM   2831 O OH  . TYR C 3 64  ? 16.543 23.621  -9.799  1.00 37.16  ?  63  TYR B OH  1 
ATOM   2832 N N   . LEU C 3 65  ? 18.129 22.078  -2.660  1.00 25.87  ?  64  LEU B N   1 
ATOM   2833 C CA  . LEU C 3 65  ? 17.000 21.262  -2.264  1.00 28.26  ?  64  LEU B CA  1 
ATOM   2834 C C   . LEU C 3 65  ? 16.025 22.067  -1.417  1.00 31.51  ?  64  LEU B C   1 
ATOM   2835 O O   . LEU C 3 65  ? 16.422 22.965  -0.674  1.00 33.48  ?  64  LEU B O   1 
ATOM   2836 C CB  . LEU C 3 65  ? 17.430 20.051  -1.430  1.00 29.28  ?  64  LEU B CB  1 
ATOM   2837 C CG  . LEU C 3 65  ? 18.388 19.038  -2.058  1.00 30.26  ?  64  LEU B CG  1 
ATOM   2838 C CD1 . LEU C 3 65  ? 18.946 18.137  -0.933  1.00 32.62  ?  64  LEU B CD1 1 
ATOM   2839 C CD2 . LEU C 3 65  ? 17.671 18.217  -3.100  1.00 33.72  ?  64  LEU B CD2 1 
ATOM   2840 N N   . LEU C 3 66  ? 14.747 21.707  -1.504  1.00 26.83  ?  65  LEU B N   1 
ATOM   2841 C CA  . LEU C 3 66  ? 13.699 22.261  -0.661  1.00 28.20  ?  65  LEU B CA  1 
ATOM   2842 C C   . LEU C 3 66  ? 13.137 21.168  0.231   1.00 33.73  ?  65  LEU B C   1 
ATOM   2843 O O   . LEU C 3 66  ? 12.639 20.162  -0.273  1.00 35.36  ?  65  LEU B O   1 
ATOM   2844 C CB  . LEU C 3 66  ? 12.580 22.865  -1.505  1.00 34.07  ?  65  LEU B CB  1 
ATOM   2845 C CG  . LEU C 3 66  ? 11.351 23.396  -0.776  1.00 38.01  ?  65  LEU B CG  1 
ATOM   2846 C CD1 . LEU C 3 66  ? 11.772 24.633  0.031   1.00 35.22  ?  65  LEU B CD1 1 
ATOM   2847 C CD2 . LEU C 3 66  ? 10.229 23.723  -1.761  1.00 38.21  ?  65  LEU B CD2 1 
ATOM   2848 N N   . TYR C 3 67  ? 13.212 21.366  1.552   1.00 31.58  ?  66  TYR B N   1 
ATOM   2849 C CA  . TYR C 3 67  ? 12.541 20.511  2.524   1.00 35.22  ?  66  TYR B CA  1 
ATOM   2850 C C   . TYR C 3 67  ? 11.328 21.257  3.063   1.00 34.15  ?  66  TYR B C   1 
ATOM   2851 O O   . TYR C 3 67  ? 11.387 22.471  3.279   1.00 38.81  ?  66  TYR B O   1 
ATOM   2852 C CB  . TYR C 3 67  ? 13.474 20.124  3.671   1.00 39.07  ?  66  TYR B CB  1 
ATOM   2853 C CG  . TYR C 3 67  ? 14.513 19.104  3.293   1.00 36.35  ?  66  TYR B CG  1 
ATOM   2854 C CD1 . TYR C 3 67  ? 15.546 19.430  2.422   1.00 35.67  ?  66  TYR B CD1 1 
ATOM   2855 C CD2 . TYR C 3 67  ? 14.458 17.810  3.803   1.00 36.54  ?  66  TYR B CD2 1 
ATOM   2856 C CE1 . TYR C 3 67  ? 16.502 18.496  2.075   1.00 42.68  ?  66  TYR B CE1 1 
ATOM   2857 C CE2 . TYR C 3 67  ? 15.398 16.873  3.455   1.00 38.61  ?  66  TYR B CE2 1 
ATOM   2858 C CZ  . TYR C 3 67  ? 16.423 17.215  2.598   1.00 37.30  ?  66  TYR B CZ  1 
ATOM   2859 O OH  . TYR C 3 67  ? 17.372 16.269  2.253   1.00 36.39  ?  66  TYR B OH  1 
ATOM   2860 N N   . TYR C 3 68  ? 10.230 20.535  3.271   1.00 31.63  ?  67  TYR B N   1 
ATOM   2861 C CA  . TYR C 3 68  ? 8.961  21.190  3.565   1.00 40.71  ?  67  TYR B CA  1 
ATOM   2862 C C   . TYR C 3 68  ? 8.010  20.243  4.279   1.00 41.98  ?  67  TYR B C   1 
ATOM   2863 O O   . TYR C 3 68  ? 8.082  19.025  4.120   1.00 40.39  ?  67  TYR B O   1 
ATOM   2864 C CB  . TYR C 3 68  ? 8.294  21.728  2.285   1.00 40.37  ?  67  TYR B CB  1 
ATOM   2865 C CG  . TYR C 3 68  ? 8.016  20.687  1.216   1.00 38.33  ?  67  TYR B CG  1 
ATOM   2866 C CD1 . TYR C 3 68  ? 8.996  20.328  0.283   1.00 42.48  ?  67  TYR B CD1 1 
ATOM   2867 C CD2 . TYR C 3 68  ? 6.765  20.087  1.110   1.00 41.26  ?  67  TYR B CD2 1 
ATOM   2868 C CE1 . TYR C 3 68  ? 8.737  19.384  -0.713  1.00 41.50  ?  67  TYR B CE1 1 
ATOM   2869 C CE2 . TYR C 3 68  ? 6.499  19.141  0.129   1.00 44.82  ?  67  TYR B CE2 1 
ATOM   2870 C CZ  . TYR C 3 68  ? 7.488  18.792  -0.782  1.00 49.45  ?  67  TYR B CZ  1 
ATOM   2871 O OH  . TYR C 3 68  ? 7.224  17.848  -1.753  1.00 48.67  ?  67  TYR B OH  1 
ATOM   2872 N N   . THR C 3 69  ? 7.106  20.834  5.061   1.00 41.79  ?  68  THR B N   1 
ATOM   2873 C CA  . THR C 3 69  ? 6.107  20.098  5.820   1.00 47.35  ?  68  THR B CA  1 
ATOM   2874 C C   . THR C 3 69  ? 4.929  21.026  6.085   1.00 49.58  ?  68  THR B C   1 
ATOM   2875 O O   . THR C 3 69  ? 5.087  22.250  6.183   1.00 46.06  ?  68  THR B O   1 
ATOM   2876 C CB  . THR C 3 69  ? 6.674  19.570  7.146   1.00 49.34  ?  68  THR B CB  1 
ATOM   2877 O OG1 . THR C 3 69  ? 5.831  18.526  7.650   1.00 57.85  ?  68  THR B OG1 1 
ATOM   2878 C CG2 . THR C 3 69  ? 6.757  20.678  8.176   1.00 47.31  ?  68  THR B CG2 1 
ATOM   2879 N N   . GLU C 3 70  ? 3.752  20.434  6.207   1.00 51.36  ?  69  GLU B N   1 
ATOM   2880 C CA  . GLU C 3 70  ? 2.571  21.197  6.578   1.00 55.58  ?  69  GLU B CA  1 
ATOM   2881 C C   . GLU C 3 70  ? 2.631  21.548  8.057   1.00 54.01  ?  69  GLU B C   1 
ATOM   2882 O O   . GLU C 3 70  ? 3.130  20.765  8.874   1.00 51.26  ?  69  GLU B O   1 
ATOM   2883 C CB  . GLU C 3 70  ? 1.310  20.393  6.276   1.00 56.30  ?  69  GLU B CB  1 
ATOM   2884 C CG  . GLU C 3 70  ? 0.091  21.245  5.993   1.00 62.37  ?  69  GLU B CG  1 
ATOM   2885 C CD  . GLU C 3 70  ? -1.017 20.466  5.298   1.00 74.18  ?  69  GLU B CD  1 
ATOM   2886 O OE1 . GLU C 3 70  ? -0.709 19.467  4.595   1.00 74.26  ?  69  GLU B OE1 1 
ATOM   2887 O OE2 . GLU C 3 70  ? -2.194 20.858  5.463   1.00 77.02  -1 69  GLU B OE2 1 
ATOM   2888 N N   . PHE C 3 71  ? 2.142  22.738  8.402   1.00 53.93  ?  70  PHE B N   1 
ATOM   2889 C CA  . PHE C 3 71  ? 2.027  23.104  9.815   1.00 60.99  ?  70  PHE B CA  1 
ATOM   2890 C C   . PHE C 3 71  ? 1.056  24.272  9.961   1.00 59.10  ?  70  PHE B C   1 
ATOM   2891 O O   . PHE C 3 71  ? 0.812  25.028  9.014   1.00 54.47  ?  70  PHE B O   1 
ATOM   2892 C CB  . PHE C 3 71  ? 3.405  23.437  10.431  1.00 53.18  ?  70  PHE B CB  1 
ATOM   2893 C CG  . PHE C 3 71  ? 3.905  24.837  10.127  1.00 54.48  ?  70  PHE B CG  1 
ATOM   2894 C CD1 . PHE C 3 71  ? 3.865  25.342  8.841   1.00 50.53  ?  70  PHE B CD1 1 
ATOM   2895 C CD2 . PHE C 3 71  ? 4.416  25.640  11.134  1.00 55.07  ?  70  PHE B CD2 1 
ATOM   2896 C CE1 . PHE C 3 71  ? 4.310  26.631  8.566   1.00 54.14  ?  70  PHE B CE1 1 
ATOM   2897 C CE2 . PHE C 3 71  ? 4.862  26.921  10.866  1.00 48.89  ?  70  PHE B CE2 1 
ATOM   2898 C CZ  . PHE C 3 71  ? 4.812  27.418  9.578   1.00 55.32  ?  70  PHE B CZ  1 
ATOM   2899 N N   . THR C 3 72  ? 0.480  24.389  11.159  1.00 63.14  ?  71  THR B N   1 
ATOM   2900 C CA  . THR C 3 72  ? -0.316 25.560  11.524  1.00 64.46  ?  71  THR B CA  1 
ATOM   2901 C C   . THR C 3 72  ? 0.443  26.307  12.611  1.00 60.87  ?  71  THR B C   1 
ATOM   2902 O O   . THR C 3 72  ? 0.580  25.789  13.732  1.00 59.87  ?  71  THR B O   1 
ATOM   2903 C CB  . THR C 3 72  ? -1.722 25.180  12.007  1.00 65.43  ?  71  THR B CB  1 
ATOM   2904 O OG1 . THR C 3 72  ? -1.639 24.391  13.201  1.00 75.22  ?  71  THR B OG1 1 
ATOM   2905 C CG2 . THR C 3 72  ? -2.470 24.402  10.922  1.00 60.54  ?  71  THR B CG2 1 
ATOM   2906 N N   . PRO C 3 73  ? 0.980  27.490  12.337  1.00 59.29  ?  72  PRO B N   1 
ATOM   2907 C CA  . PRO C 3 73  ? 1.782  28.177  13.353  1.00 57.14  ?  72  PRO B CA  1 
ATOM   2908 C C   . PRO C 3 73  ? 0.924  28.792  14.447  1.00 62.71  ?  72  PRO B C   1 
ATOM   2909 O O   . PRO C 3 73  ? -0.241 29.144  14.240  1.00 61.10  ?  72  PRO B O   1 
ATOM   2910 C CB  . PRO C 3 73  ? 2.513  29.266  12.554  1.00 54.59  ?  72  PRO B CB  1 
ATOM   2911 C CG  . PRO C 3 73  ? 1.593  29.582  11.416  1.00 59.81  ?  72  PRO B CG  1 
ATOM   2912 C CD  . PRO C 3 73  ? 0.837  28.286  11.101  1.00 57.77  ?  72  PRO B CD  1 
ATOM   2913 N N   . THR C 3 74  ? 1.532  28.915  15.631  1.00 59.05  ?  73  THR B N   1 
ATOM   2914 C CA  . THR C 3 74  ? 0.941  29.659  16.734  1.00 62.05  ?  73  THR B CA  1 
ATOM   2915 C C   . THR C 3 74  ? 1.896  30.743  17.221  1.00 63.57  ?  73  THR B C   1 
ATOM   2916 O O   . THR C 3 74  ? 2.938  30.992  16.606  1.00 59.74  ?  73  THR B O   1 
ATOM   2917 C CB  . THR C 3 74  ? 0.596  28.731  17.899  1.00 57.97  ?  73  THR B CB  1 
ATOM   2918 O OG1 . THR C 3 74  ? 0.326  29.511  19.074  1.00 75.47  ?  73  THR B OG1 1 
ATOM   2919 C CG2 . THR C 3 74  ? 1.752  27.817  18.191  1.00 55.73  ?  73  THR B CG2 1 
ATOM   2920 N N   . GLU C 3 75  ? 1.569  31.363  18.355  1.00 64.01  ?  74  GLU B N   1 
ATOM   2921 C CA  . GLU C 3 75  ? 2.390  32.450  18.870  1.00 61.82  ?  74  GLU B CA  1 
ATOM   2922 C C   . GLU C 3 75  ? 3.671  31.949  19.524  1.00 56.93  ?  74  GLU B C   1 
ATOM   2923 O O   . GLU C 3 75  ? 4.727  32.559  19.351  1.00 56.07  ?  74  GLU B O   1 
ATOM   2924 C CB  . GLU C 3 75  ? 1.590  33.276  19.876  1.00 68.57  ?  74  GLU B CB  1 
ATOM   2925 C CG  . GLU C 3 75  ? 2.239  34.597  20.268  1.00 75.09  ?  74  GLU B CG  1 
ATOM   2926 C CD  . GLU C 3 75  ? 1.249  35.544  20.921  1.00 80.23  ?  74  GLU B CD  1 
ATOM   2927 O OE1 . GLU C 3 75  ? 0.671  35.163  21.969  1.00 75.35  ?  74  GLU B OE1 1 
ATOM   2928 O OE2 . GLU C 3 75  ? 1.039  36.655  20.373  1.00 83.60  -1 74  GLU B OE2 1 
ATOM   2929 N N   . LYS C 3 76  ? 3.610  30.863  20.290  1.00 54.19  ?  75  LYS B N   1 
ATOM   2930 C CA  . LYS C 3 76  ? 4.774  30.439  21.056  1.00 66.75  ?  75  LYS B CA  1 
ATOM   2931 C C   . LYS C 3 76  ? 5.492  29.223  20.476  1.00 61.51  ?  75  LYS B C   1 
ATOM   2932 O O   . LYS C 3 76  ? 6.526  28.820  21.025  1.00 64.17  ?  75  LYS B O   1 
ATOM   2933 C CB  . LYS C 3 76  ? 4.371  30.137  22.506  1.00 64.62  ?  75  LYS B CB  1 
ATOM   2934 N N   . ASP C 3 77  ? 4.970  28.609  19.413  1.00 59.18  ?  76  ASP B N   1 
ATOM   2935 C CA  . ASP C 3 77  ? 5.672  27.498  18.772  1.00 58.84  ?  76  ASP B CA  1 
ATOM   2936 C C   . ASP C 3 77  ? 6.827  28.031  17.927  1.00 53.11  ?  76  ASP B C   1 
ATOM   2937 O O   . ASP C 3 77  ? 6.625  28.841  17.012  1.00 51.11  ?  76  ASP B O   1 
ATOM   2938 C CB  . ASP C 3 77  ? 4.721  26.666  17.917  1.00 53.85  ?  76  ASP B CB  1 
ATOM   2939 C CG  . ASP C 3 77  ? 3.897  25.700  18.745  1.00 50.47  ?  76  ASP B CG  1 
ATOM   2940 O OD1 . ASP C 3 77  ? 4.320  25.364  19.865  1.00 53.13  ?  76  ASP B OD1 1 
ATOM   2941 O OD2 . ASP C 3 77  ? 2.826  25.281  18.270  1.00 56.15  -1 76  ASP B OD2 1 
ATOM   2942 N N   . GLU C 3 78  ? 8.031  27.569  18.240  1.00 50.43  ?  77  GLU B N   1 
ATOM   2943 C CA  . GLU C 3 78  ? 9.238  27.933  17.518  1.00 53.34  ?  77  GLU B CA  1 
ATOM   2944 C C   . GLU C 3 78  ? 9.641  26.836  16.532  1.00 52.98  ?  77  GLU B C   1 
ATOM   2945 O O   . GLU C 3 78  ? 9.649  25.645  16.865  1.00 46.64  ?  77  GLU B O   1 
ATOM   2946 C CB  . GLU C 3 78  ? 10.369 28.179  18.512  1.00 57.65  ?  77  GLU B CB  1 
ATOM   2947 N N   . TYR C 3 79  ? 10.004 27.254  15.325  1.00 49.72  ?  78  TYR B N   1 
ATOM   2948 C CA  . TYR C 3 79  ? 10.437 26.340  14.282  1.00 46.88  ?  78  TYR B CA  1 
ATOM   2949 C C   . TYR C 3 79  ? 11.829 26.715  13.805  1.00 44.94  ?  78  TYR B C   1 
ATOM   2950 O O   . TYR C 3 79  ? 12.281 27.852  13.959  1.00 41.53  ?  78  TYR B O   1 
ATOM   2951 C CB  . TYR C 3 79  ? 9.464  26.344  13.108  1.00 43.34  ?  78  TYR B CB  1 
ATOM   2952 C CG  . TYR C 3 79  ? 8.114  25.812  13.492  1.00 48.09  ?  78  TYR B CG  1 
ATOM   2953 C CD1 . TYR C 3 79  ? 7.825  24.456  13.390  1.00 43.38  ?  78  TYR B CD1 1 
ATOM   2954 C CD2 . TYR C 3 79  ? 7.124  26.668  13.984  1.00 49.25  ?  78  TYR B CD2 1 
ATOM   2955 C CE1 . TYR C 3 79  ? 6.583  23.963  13.742  1.00 44.97  ?  78  TYR B CE1 1 
ATOM   2956 C CE2 . TYR C 3 79  ? 5.885  26.185  14.354  1.00 46.97  ?  78  TYR B CE2 1 
ATOM   2957 C CZ  . TYR C 3 79  ? 5.619  24.830  14.227  1.00 49.28  ?  78  TYR B CZ  1 
ATOM   2958 O OH  . TYR C 3 79  ? 4.386  24.343  14.575  1.00 50.37  ?  78  TYR B OH  1 
ATOM   2959 N N   . ALA C 3 80  ? 12.517 25.728  13.238  1.00 43.16  ?  79  ALA B N   1 
ATOM   2960 C CA  . ALA C 3 80  ? 13.889 25.927  12.806  1.00 39.34  ?  79  ALA B CA  1 
ATOM   2961 C C   . ALA C 3 80  ? 14.258 24.834  11.817  1.00 35.04  ?  79  ALA B C   1 
ATOM   2962 O O   . ALA C 3 80  ? 13.531 23.855  11.637  1.00 37.98  ?  79  ALA B O   1 
ATOM   2963 C CB  . ALA C 3 80  ? 14.852 25.940  13.996  1.00 43.01  ?  79  ALA B CB  1 
ATOM   2964 N N   . CYS C 3 81  ? 15.391 25.039  11.156  1.00 41.63  ?  80  CYS B N   1 
ATOM   2965 C CA  . CYS C 3 81  ? 15.983 24.076  10.235  1.00 41.78  ?  80  CYS B CA  1 
ATOM   2966 C C   . CYS C 3 81  ? 17.390 23.736  10.715  1.00 37.36  ?  80  CYS B C   1 
ATOM   2967 O O   . CYS C 3 81  ? 18.196 24.633  10.980  1.00 43.80  ?  80  CYS B O   1 
ATOM   2968 C CB  . CYS C 3 81  ? 16.026 24.640  8.810   1.00 37.15  ?  80  CYS B CB  1 
ATOM   2969 S SG  . CYS C 3 81  ? 16.588 23.453  7.560   1.00 48.68  ?  80  CYS B SG  1 
ATOM   2970 N N   . ARG C 3 82  ? 17.676 22.450  10.821  1.00 37.56  ?  81  ARG B N   1 
ATOM   2971 C CA  . ARG C 3 82  ? 18.972 21.945  11.240  1.00 40.27  ?  81  ARG B CA  1 
ATOM   2972 C C   . ARG C 3 82  ? 19.599 21.221  10.060  1.00 35.77  ?  81  ARG B C   1 
ATOM   2973 O O   . ARG C 3 82  ? 18.999 20.296  9.504   1.00 36.40  ?  81  ARG B O   1 
ATOM   2974 C CB  . ARG C 3 82  ? 18.796 21.018  12.441  1.00 40.85  ?  81  ARG B CB  1 
ATOM   2975 C CG  . ARG C 3 82  ? 20.043 20.353  12.998  1.00 47.94  ?  81  ARG B CG  1 
ATOM   2976 C CD  . ARG C 3 82  ? 19.718 18.890  13.396  1.00 47.86  ?  81  ARG B CD  1 
ATOM   2977 N NE  . ARG C 3 82  ? 19.061 18.763  14.685  1.00 52.41  ?  81  ARG B NE  1 
ATOM   2978 C CZ  . ARG C 3 82  ? 18.169 17.820  15.007  1.00 56.13  ?  81  ARG B CZ  1 
ATOM   2979 N NH1 . ARG C 3 82  ? 17.786 16.895  14.133  1.00 45.09  ?  81  ARG B NH1 1 
ATOM   2980 N NH2 . ARG C 3 82  ? 17.654 17.809  16.230  1.00 56.23  ?  81  ARG B NH2 1 
ATOM   2981 N N   . VAL C 3 83  ? 20.806 21.636  9.694   1.00 37.45  ?  82  VAL B N   1 
ATOM   2982 C CA  . VAL C 3 83  ? 21.462 21.195  8.471   1.00 42.79  ?  82  VAL B CA  1 
ATOM   2983 C C   . VAL C 3 83  ? 22.869 20.723  8.811   1.00 40.39  ?  82  VAL B C   1 
ATOM   2984 O O   . VAL C 3 83  ? 23.597 21.404  9.539   1.00 40.67  ?  82  VAL B O   1 
ATOM   2985 C CB  . VAL C 3 83  ? 21.537 22.318  7.416   1.00 40.90  ?  82  VAL B CB  1 
ATOM   2986 C CG1 . VAL C 3 83  ? 22.310 21.823  6.190   1.00 41.09  ?  82  VAL B CG1 1 
ATOM   2987 C CG2 . VAL C 3 83  ? 20.141 22.817  7.023   1.00 37.74  ?  82  VAL B CG2 1 
ATOM   2988 N N   . ASN C 3 84  ? 23.261 19.576  8.260   1.00 37.72  ?  83  ASN B N   1 
ATOM   2989 C CA  . ASN C 3 84  ? 24.649 19.151  8.310   1.00 39.42  ?  83  ASN B CA  1 
ATOM   2990 C C   . ASN C 3 84  ? 25.186 18.828  6.918   1.00 40.27  ?  83  ASN B C   1 
ATOM   2991 O O   . ASN C 3 84  ? 24.495 18.246  6.076   1.00 38.97  ?  83  ASN B O   1 
ATOM   2992 C CB  . ASN C 3 84  ? 24.838 17.937  9.225   1.00 43.48  ?  83  ASN B CB  1 
ATOM   2993 C CG  . ASN C 3 84  ? 26.213 17.930  9.895   1.00 52.27  ?  83  ASN B CG  1 
ATOM   2994 O OD1 . ASN C 3 84  ? 27.238 18.281  9.282   1.00 46.89  ?  83  ASN B OD1 1 
ATOM   2995 N ND2 . ASN C 3 84  ? 26.237 17.549  11.163  1.00 55.08  ?  83  ASN B ND2 1 
ATOM   2996 N N   . HIS C 3 85  ? 26.444 19.184  6.713   1.00 36.55  ?  84  HIS B N   1 
ATOM   2997 C CA  . HIS C 3 85  ? 27.118 19.086  5.432   1.00 42.50  ?  84  HIS B CA  1 
ATOM   2998 C C   . HIS C 3 85  ? 28.581 18.877  5.771   1.00 44.26  ?  84  HIS B C   1 
ATOM   2999 O O   . HIS C 3 85  ? 29.019 19.203  6.878   1.00 43.36  ?  84  HIS B O   1 
ATOM   3000 C CB  . HIS C 3 85  ? 26.891 20.350  4.591   1.00 37.12  ?  84  HIS B CB  1 
ATOM   3001 C CG  . HIS C 3 85  ? 27.449 20.271  3.211   1.00 34.21  ?  84  HIS B CG  1 
ATOM   3002 N ND1 . HIS C 3 85  ? 28.564 20.978  2.827   1.00 33.48  ?  84  HIS B ND1 1 
ATOM   3003 C CD2 . HIS C 3 85  ? 27.040 19.583  2.119   1.00 34.14  ?  84  HIS B CD2 1 
ATOM   3004 C CE1 . HIS C 3 85  ? 28.828 20.721  1.559   1.00 37.45  ?  84  HIS B CE1 1 
ATOM   3005 N NE2 . HIS C 3 85  ? 27.922 19.871  1.109   1.00 29.81  ?  84  HIS B NE2 1 
ATOM   3006 N N   . VAL C 3 86  ? 29.339 18.309  4.828   1.00 37.94  ?  85  VAL B N   1 
ATOM   3007 C CA  . VAL C 3 86  ? 30.746 18.077  5.111   1.00 39.25  ?  85  VAL B CA  1 
ATOM   3008 C C   . VAL C 3 86  ? 31.470 19.391  5.356   1.00 42.24  ?  85  VAL B C   1 
ATOM   3009 O O   . VAL C 3 86  ? 32.483 19.407  6.056   1.00 49.80  ?  85  VAL B O   1 
ATOM   3010 C CB  . VAL C 3 86  ? 31.438 17.275  3.991   1.00 42.94  ?  85  VAL B CB  1 
ATOM   3011 C CG1 . VAL C 3 86  ? 31.570 18.102  2.725   1.00 42.68  ?  85  VAL B CG1 1 
ATOM   3012 C CG2 . VAL C 3 86  ? 32.817 16.788  4.461   1.00 47.20  ?  85  VAL B CG2 1 
ATOM   3013 N N   . THR C 3 87  ? 30.978 20.501  4.799   1.00 43.73  ?  86  THR B N   1 
ATOM   3014 C CA  . THR C 3 87  ? 31.609 21.796  5.032   1.00 41.45  ?  86  THR B CA  1 
ATOM   3015 C C   . THR C 3 87  ? 31.369 22.333  6.445   1.00 44.05  ?  86  THR B C   1 
ATOM   3016 O O   . THR C 3 87  ? 31.832 23.437  6.744   1.00 42.97  ?  86  THR B O   1 
ATOM   3017 C CB  . THR C 3 87  ? 31.080 22.853  4.060   1.00 39.32  ?  86  THR B CB  1 
ATOM   3018 O OG1 . THR C 3 87  ? 29.646 22.814  4.071   1.00 39.57  ?  86  THR B OG1 1 
ATOM   3019 C CG2 . THR C 3 87  ? 31.610 22.658  2.652   1.00 41.85  ?  86  THR B CG2 1 
ATOM   3020 N N   . LEU C 3 88  ? 30.609 21.635  7.284   1.00 44.35  ?  87  LEU B N   1 
ATOM   3021 C CA  . LEU C 3 88  ? 30.179 22.162  8.572   1.00 48.48  ?  87  LEU B CA  1 
ATOM   3022 C C   . LEU C 3 88  ? 30.614 21.229  9.693   1.00 48.33  ?  87  LEU B C   1 
ATOM   3023 O O   . LEU C 3 88  ? 30.394 20.013  9.617   1.00 44.03  ?  87  LEU B O   1 
ATOM   3024 C CB  . LEU C 3 88  ? 28.657 22.343  8.640   1.00 42.96  ?  87  LEU B CB  1 
ATOM   3025 C CG  . LEU C 3 88  ? 27.949 23.299  7.679   1.00 43.71  ?  87  LEU B CG  1 
ATOM   3026 C CD1 . LEU C 3 88  ? 26.437 22.991  7.720   1.00 43.55  ?  87  LEU B CD1 1 
ATOM   3027 C CD2 . LEU C 3 88  ? 28.192 24.758  7.995   1.00 48.93  ?  87  LEU B CD2 1 
ATOM   3028 N N   . SER C 3 89  ? 31.185 21.818  10.754  1.00 53.75  ?  88  SER B N   1 
ATOM   3029 C CA  . SER C 3 89  ? 31.729 21.030  11.862  1.00 51.79  ?  88  SER B CA  1 
ATOM   3030 C C   . SER C 3 89  ? 30.625 20.461  12.747  1.00 56.48  ?  88  SER B C   1 
ATOM   3031 O O   . SER C 3 89  ? 30.766 19.371  13.315  1.00 52.12  ?  88  SER B O   1 
ATOM   3032 C CB  . SER C 3 89  ? 32.655 21.912  12.692  1.00 52.95  ?  88  SER B CB  1 
ATOM   3033 O OG  . SER C 3 89  ? 32.028 23.166  12.916  1.00 63.40  ?  88  SER B OG  1 
ATOM   3034 N N   . GLN C 3 90  ? 29.536 21.200  12.896  1.00 58.24  ?  89  GLN B N   1 
ATOM   3035 C CA  . GLN C 3 90  ? 28.396 20.891  13.737  1.00 56.30  ?  89  GLN B CA  1 
ATOM   3036 C C   . GLN C 3 90  ? 27.148 21.123  12.923  1.00 45.70  ?  89  GLN B C   1 
ATOM   3037 O O   . GLN C 3 90  ? 27.150 21.953  12.003  1.00 43.90  ?  89  GLN B O   1 
ATOM   3038 C CB  . GLN C 3 90  ? 28.397 21.791  14.991  1.00 53.48  ?  89  GLN B CB  1 
ATOM   3039 C CG  . GLN C 3 90  ? 28.619 23.279  14.681  1.00 61.09  ?  89  GLN B CG  1 
ATOM   3040 C CD  . GLN C 3 90  ? 30.044 23.753  14.966  1.00 68.42  ?  89  GLN B CD  1 
ATOM   3041 O OE1 . GLN C 3 90  ? 30.891 22.984  15.433  1.00 71.14  ?  89  GLN B OE1 1 
ATOM   3042 N NE2 . GLN C 3 90  ? 30.316 25.024  14.668  1.00 76.25  ?  89  GLN B NE2 1 
ATOM   3043 N N   . PRO C 3 91  ? 26.056 20.414  13.201  1.00 49.51  ?  90  PRO B N   1 
ATOM   3044 C CA  . PRO C 3 91  ? 24.751 20.838  12.672  1.00 49.67  ?  90  PRO B CA  1 
ATOM   3045 C C   . PRO C 3 91  ? 24.542 22.343  12.825  1.00 53.69  ?  90  PRO B C   1 
ATOM   3046 O O   . PRO C 3 91  ? 24.841 22.910  13.885  1.00 53.98  ?  90  PRO B O   1 
ATOM   3047 C CB  . PRO C 3 91  ? 23.751 20.036  13.508  1.00 47.71  ?  90  PRO B CB  1 
ATOM   3048 C CG  . PRO C 3 91  ? 24.515 18.746  13.857  1.00 51.84  ?  90  PRO B CG  1 
ATOM   3049 C CD  . PRO C 3 91  ? 25.983 19.128  13.934  1.00 52.48  ?  90  PRO B CD  1 
ATOM   3050 N N   . LYS C 3 92  ? 24.076 23.011  11.771  1.00 48.51  ?  91  LYS B N   1 
ATOM   3051 C CA  . LYS C 3 92  ? 23.750 24.432  11.817  1.00 48.42  ?  91  LYS B CA  1 
ATOM   3052 C C   . LYS C 3 92  ? 22.238 24.579  11.883  1.00 50.93  ?  91  LYS B C   1 
ATOM   3053 O O   . LYS C 3 92  ? 21.515 23.958  11.091  1.00 40.24  ?  91  LYS B O   1 
ATOM   3054 C CB  . LYS C 3 92  ? 24.297 25.192  10.604  1.00 50.06  ?  91  LYS B CB  1 
ATOM   3055 C CG  . LYS C 3 92  ? 24.094 26.686  10.733  1.00 54.63  ?  91  LYS B CG  1 
ATOM   3056 C CD  . LYS C 3 92  ? 24.903 27.501  9.724   1.00 56.14  ?  91  LYS B CD  1 
ATOM   3057 C CE  . LYS C 3 92  ? 24.205 28.839  9.386   1.00 65.57  ?  91  LYS B CE  1 
ATOM   3058 N NZ  . LYS C 3 92  ? 24.257 29.887  10.463  1.00 63.83  ?  91  LYS B NZ  1 
ATOM   3059 N N   . ILE C 3 93  ? 21.771 25.393  12.829  1.00 44.71  ?  92  ILE B N   1 
ATOM   3060 C CA  . ILE C 3 93  ? 20.352 25.567  13.110  1.00 47.24  ?  92  ILE B CA  1 
ATOM   3061 C C   . ILE C 3 93  ? 19.983 27.007  12.782  1.00 49.59  ?  92  ILE B C   1 
ATOM   3062 O O   . ILE C 3 93  ? 20.599 27.946  13.304  1.00 47.44  ?  92  ILE B O   1 
ATOM   3063 C CB  . ILE C 3 93  ? 20.022 25.229  14.573  1.00 47.58  ?  92  ILE B CB  1 
ATOM   3064 C CG1 . ILE C 3 93  ? 20.440 23.790  14.874  1.00 46.44  ?  92  ILE B CG1 1 
ATOM   3065 C CG2 . ILE C 3 93  ? 18.535 25.457  14.866  1.00 52.97  ?  92  ILE B CG2 1 
ATOM   3066 C CD1 . ILE C 3 93  ? 19.636 23.117  15.952  1.00 50.32  ?  92  ILE B CD1 1 
ATOM   3067 N N   . VAL C 3 94  ? 19.003 27.180  11.898  1.00 39.11  ?  93  VAL B N   1 
ATOM   3068 C CA  . VAL C 3 94  ? 18.464 28.488  11.556  1.00 41.36  ?  93  VAL B CA  1 
ATOM   3069 C C   . VAL C 3 94  ? 17.012 28.505  11.994  1.00 44.73  ?  93  VAL B C   1 
ATOM   3070 O O   . VAL C 3 94  ? 16.207 27.680  11.544  1.00 43.07  ?  93  VAL B O   1 
ATOM   3071 C CB  . VAL C 3 94  ? 18.599 28.800  10.060  1.00 45.40  ?  93  VAL B CB  1 
ATOM   3072 C CG1 . VAL C 3 94  ? 18.342 30.279  9.805   1.00 46.97  ?  93  VAL B CG1 1 
ATOM   3073 C CG2 . VAL C 3 94  ? 19.986 28.397  9.580   1.00 45.78  ?  93  VAL B CG2 1 
ATOM   3074 N N   . LYS C 3 95  ? 16.687 29.427  12.887  1.00 45.90  ?  94  LYS B N   1 
ATOM   3075 C CA  . LYS C 3 95  ? 15.344 29.529  13.415  1.00 44.38  ?  94  LYS B CA  1 
ATOM   3076 C C   . LYS C 3 95  ? 14.447 30.280  12.442  1.00 41.50  ?  94  LYS B C   1 
ATOM   3077 O O   . LYS C 3 95  ? 14.893 31.142  11.682  1.00 40.54  ?  94  LYS B O   1 
ATOM   3078 C CB  . LYS C 3 95  ? 15.378 30.221  14.783  1.00 53.77  ?  94  LYS B CB  1 
ATOM   3079 C CG  . LYS C 3 95  ? 16.141 29.412  15.834  1.00 58.10  ?  94  LYS B CG  1 
ATOM   3080 C CD  . LYS C 3 95  ? 16.920 30.302  16.791  1.00 68.60  ?  94  LYS B CD  1 
ATOM   3081 C CE  . LYS C 3 95  ? 18.123 29.559  17.389  1.00 75.53  ?  94  LYS B CE  1 
ATOM   3082 N NZ  . LYS C 3 95  ? 19.204 29.284  16.372  1.00 65.99  ?  94  LYS B NZ  1 
ATOM   3083 N N   . TRP C 3 96  ? 13.171 29.913  12.450  1.00 41.41  ?  95  TRP B N   1 
ATOM   3084 C CA  . TRP C 3 96  ? 12.188 30.624  11.655  1.00 39.59  ?  95  TRP B CA  1 
ATOM   3085 C C   . TRP C 3 96  ? 11.864 31.964  12.300  1.00 44.83  ?  95  TRP B C   1 
ATOM   3086 O O   . TRP C 3 96  ? 11.488 32.019  13.472  1.00 43.23  ?  95  TRP B O   1 
ATOM   3087 C CB  . TRP C 3 96  ? 10.921 29.790  11.531  1.00 41.43  ?  95  TRP B CB  1 
ATOM   3088 C CG  . TRP C 3 96  ? 9.871  30.463  10.748  1.00 41.36  ?  95  TRP B CG  1 
ATOM   3089 C CD1 . TRP C 3 96  ? 10.041 31.156  9.591   1.00 40.88  ?  95  TRP B CD1 1 
ATOM   3090 C CD2 . TRP C 3 96  ? 8.473  30.521  11.056  1.00 42.47  ?  95  TRP B CD2 1 
ATOM   3091 N NE1 . TRP C 3 96  ? 8.833  31.641  9.151   1.00 48.35  ?  95  TRP B NE1 1 
ATOM   3092 C CE2 . TRP C 3 96  ? 7.853  31.258  10.032  1.00 48.68  ?  95  TRP B CE2 1 
ATOM   3093 C CE3 . TRP C 3 96  ? 7.686  30.019  12.099  1.00 46.79  ?  95  TRP B CE3 1 
ATOM   3094 C CZ2 . TRP C 3 96  ? 6.479  31.510  10.017  1.00 48.25  ?  95  TRP B CZ2 1 
ATOM   3095 C CZ3 . TRP C 3 96  ? 6.323  30.265  12.081  1.00 50.81  ?  95  TRP B CZ3 1 
ATOM   3096 C CH2 . TRP C 3 96  ? 5.735  31.005  11.043  1.00 45.61  ?  95  TRP B CH2 1 
ATOM   3097 N N   . ASP C 3 97  ? 11.976 33.036  11.521  1.00 46.28  ?  96  ASP B N   1 
ATOM   3098 C CA  . ASP C 3 97  ? 11.702 34.401  11.972  1.00 50.74  ?  96  ASP B CA  1 
ATOM   3099 C C   . ASP C 3 97  ? 10.638 34.991  11.046  1.00 48.72  ?  96  ASP B C   1 
ATOM   3100 O O   . ASP C 3 97  ? 10.945 35.469  9.948   1.00 48.79  ?  96  ASP B O   1 
ATOM   3101 C CB  . ASP C 3 97  ? 12.987 35.227  11.978  1.00 51.73  ?  96  ASP B CB  1 
ATOM   3102 C CG  . ASP C 3 97  ? 12.733 36.720  12.173  1.00 57.67  ?  96  ASP B CG  1 
ATOM   3103 O OD1 . ASP C 3 97  ? 11.675 37.073  12.745  1.00 55.02  ?  96  ASP B OD1 1 
ATOM   3104 O OD2 . ASP C 3 97  ? 13.592 37.528  11.738  1.00 52.05  -1 96  ASP B OD2 1 
ATOM   3105 N N   . ARG C 3 98  ? 9.381  34.973  11.487  1.00 48.35  ?  97  ARG B N   1 
ATOM   3106 C CA  . ARG C 3 98  ? 8.304  35.317  10.565  1.00 53.34  ?  97  ARG B CA  1 
ATOM   3107 C C   . ARG C 3 98  ? 8.298  36.799  10.201  1.00 57.85  ?  97  ARG B C   1 
ATOM   3108 O O   . ARG C 3 98  ? 7.826  37.166  9.116   1.00 56.20  ?  97  ARG B O   1 
ATOM   3109 C CB  . ARG C 3 98  ? 6.959  34.923  11.159  1.00 55.38  ?  97  ARG B CB  1 
ATOM   3110 C CG  . ARG C 3 98  ? 6.629  35.624  12.451  1.00 65.16  ?  97  ARG B CG  1 
ATOM   3111 C CD  . ARG C 3 98  ? 5.203  35.311  12.857  1.00 60.58  ?  97  ARG B CD  1 
ATOM   3112 N NE  . ARG C 3 98  ? 5.143  34.110  13.679  1.00 60.30  ?  97  ARG B NE  1 
ATOM   3113 C CZ  . ARG C 3 98  ? 4.040  33.398  13.870  1.00 61.78  ?  97  ARG B CZ  1 
ATOM   3114 N NH1 . ARG C 3 98  ? 2.904  33.775  13.293  1.00 60.33  ?  97  ARG B NH1 1 
ATOM   3115 N NH2 . ARG C 3 98  ? 4.072  32.315  14.634  1.00 63.47  ?  97  ARG B NH2 1 
ATOM   3116 N N   . ASP C 3 99  ? 8.812  37.662  11.072  1.00 56.13  ?  98  ASP B N   1 
ATOM   3117 C CA  . ASP C 3 99  ? 8.701  39.100  10.865  1.00 64.36  ?  98  ASP B CA  1 
ATOM   3118 C C   . ASP C 3 99  ? 9.825  39.686  10.015  1.00 62.50  ?  98  ASP B C   1 
ATOM   3119 O O   . ASP C 3 99  ? 9.914  40.915  9.902   1.00 58.21  ?  98  ASP B O   1 
ATOM   3120 C CB  . ASP C 3 99  ? 8.655  39.821  12.216  1.00 66.20  ?  98  ASP B CB  1 
ATOM   3121 C CG  . ASP C 3 99  ? 7.272  39.804  12.830  1.00 67.98  ?  98  ASP B CG  1 
ATOM   3122 O OD1 . ASP C 3 99  ? 6.293  40.047  12.086  1.00 67.26  ?  98  ASP B OD1 1 
ATOM   3123 O OD2 . ASP C 3 99  ? 7.169  39.532  14.046  1.00 74.81  -1 98  ASP B OD2 1 
ATOM   3124 N N   . MET C 3 100 ? 10.673 38.858  9.412   1.00 56.19  ?  99  MET B N   1 
ATOM   3125 C CA  . MET C 3 100 ? 11.779 39.397  8.630   1.00 58.09  ?  99  MET B CA  1 
ATOM   3126 C C   . MET C 3 100 ? 11.279 39.837  7.252   1.00 55.17  ?  99  MET B C   1 
ATOM   3127 O O   . MET C 3 100 ? 11.421 41.009  6.881   1.00 48.93  ?  99  MET B O   1 
ATOM   3128 C CB  . MET C 3 100 ? 12.921 38.376  8.530   1.00 57.96  ?  99  MET B CB  1 
ATOM   3129 C CG  . MET C 3 100 ? 12.742 37.236  7.570   1.00 59.28  ?  99  MET B CG  1 
ATOM   3130 S SD  . MET C 3 100 ? 14.371 36.463  7.345   1.00 64.65  ?  99  MET B SD  1 
ATOM   3131 C CE  . MET C 3 100 ? 15.479 37.831  7.697   1.00 51.01  ?  99  MET B CE  1 
ATOM   3132 N N   . ALA D 4 2   ? -1.868 0.240   -31.150 1.00 55.22  ?  1   ALA D N   1 
ATOM   3133 C CA  . ALA D 4 2   ? -0.890 -0.827  -30.943 1.00 55.28  ?  1   ALA D CA  1 
ATOM   3134 C C   . ALA D 4 2   ? 0.433  -0.458  -31.604 1.00 47.66  ?  1   ALA D C   1 
ATOM   3135 O O   . ALA D 4 2   ? 0.629  0.699   -31.981 1.00 46.75  ?  1   ALA D O   1 
ATOM   3136 C CB  . ALA D 4 2   ? -1.416 -2.148  -31.489 1.00 50.05  ?  1   ALA D CB  1 
ATOM   3137 N N   . GLN D 4 3   ? 1.334  -1.441  -31.734 1.00 41.29  ?  2   GLN D N   1 
ATOM   3138 C CA  . GLN D 4 3   ? 2.618  -1.297  -32.429 1.00 42.71  ?  2   GLN D CA  1 
ATOM   3139 C C   . GLN D 4 3   ? 2.570  -2.222  -33.630 1.00 37.13  ?  2   GLN D C   1 
ATOM   3140 O O   . GLN D 4 3   ? 2.832  -3.415  -33.488 1.00 37.26  ?  2   GLN D O   1 
ATOM   3141 C CB  . GLN D 4 3   ? 3.801  -1.702  -31.555 1.00 38.82  ?  2   GLN D CB  1 
ATOM   3142 C CG  . GLN D 4 3   ? 4.421  -0.626  -30.759 1.00 53.14  ?  2   GLN D CG  1 
ATOM   3143 C CD  . GLN D 4 3   ? 5.026  0.446   -31.612 1.00 43.62  ?  2   GLN D CD  1 
ATOM   3144 O OE1 . GLN D 4 3   ? 4.636  1.607   -31.498 1.00 45.44  ?  2   GLN D OE1 1 
ATOM   3145 N NE2 . GLN D 4 3   ? 6.006  0.082   -32.453 1.00 38.04  ?  2   GLN D NE2 1 
ATOM   3146 N N   . LYS D 4 4   ? 2.254  -1.685  -34.801 1.00 32.19  ?  3   LYS D N   1 
ATOM   3147 C CA  . LYS D 4 4   ? 2.165  -2.509  -35.999 1.00 42.30  ?  3   LYS D CA  1 
ATOM   3148 C C   . LYS D 4 4   ? 2.613  -1.670  -37.185 1.00 35.90  ?  3   LYS D C   1 
ATOM   3149 O O   . LYS D 4 4   ? 2.237  -0.499  -37.288 1.00 38.61  ?  3   LYS D O   1 
ATOM   3150 C CB  . LYS D 4 4   ? 0.737  -3.033  -36.207 1.00 40.91  ?  3   LYS D CB  1 
ATOM   3151 N N   . VAL D 4 5   ? 3.457  -2.247  -38.034 1.00 31.81  ?  4   VAL D N   1 
ATOM   3152 C CA  . VAL D 4 5   ? 3.849  -1.656  -39.313 1.00 31.54  ?  4   VAL D CA  1 
ATOM   3153 C C   . VAL D 4 5   ? 3.214  -2.502  -40.422 1.00 36.25  ?  4   VAL D C   1 
ATOM   3154 O O   . VAL D 4 5   ? 3.247  -3.738  -40.364 1.00 36.81  ?  4   VAL D O   1 
ATOM   3155 C CB  . VAL D 4 5   ? 5.380  -1.582  -39.454 1.00 25.17  ?  4   VAL D CB  1 
ATOM   3156 C CG1 . VAL D 4 5   ? 5.774  -1.034  -40.820 1.00 23.75  ?  4   VAL D CG1 1 
ATOM   3157 C CG2 . VAL D 4 5   ? 6.034  -0.735  -38.272 1.00 26.67  ?  4   VAL D CG2 1 
ATOM   3158 N N   . THR D 4 6   ? 2.607  -1.846  -41.413 1.00 36.26  ?  5   THR D N   1 
ATOM   3159 C CA  . THR D 4 6   ? 1.809  -2.552  -42.416 1.00 36.58  ?  5   THR D CA  1 
ATOM   3160 C C   . THR D 4 6   ? 2.299  -2.188  -43.799 1.00 30.67  ?  5   THR D C   1 
ATOM   3161 O O   . THR D 4 6   ? 2.214  -1.025  -44.204 1.00 32.97  ?  5   THR D O   1 
ATOM   3162 C CB  . THR D 4 6   ? 0.318  -2.218  -42.320 1.00 38.42  ?  5   THR D CB  1 
ATOM   3163 O OG1 . THR D 4 6   ? -0.204 -2.660  -41.072 1.00 38.91  ?  5   THR D OG1 1 
ATOM   3164 C CG2 . THR D 4 6   ? -0.453 -2.929  -43.448 1.00 40.71  ?  5   THR D CG2 1 
ATOM   3165 N N   . GLN D 4 7   ? 2.795  -3.179  -44.522 1.00 31.70  ?  6   GLN D N   1 
ATOM   3166 C CA  . GLN D 4 7   ? 3.094  -3.041  -45.946 1.00 33.48  ?  6   GLN D CA  1 
ATOM   3167 C C   . GLN D 4 7   ? 2.038  -3.886  -46.672 1.00 38.05  ?  6   GLN D C   1 
ATOM   3168 O O   . GLN D 4 7   ? 2.137  -5.118  -46.718 1.00 35.82  ?  6   GLN D O   1 
ATOM   3169 C CB  . GLN D 4 7   ? 4.529  -3.466  -46.244 1.00 31.10  ?  6   GLN D CB  1 
ATOM   3170 C CG  . GLN D 4 7   ? 5.556  -2.471  -45.649 1.00 32.85  ?  6   GLN D CG  1 
ATOM   3171 C CD  . GLN D 4 7   ? 6.959  -2.979  -45.718 1.00 29.87  ?  6   GLN D CD  1 
ATOM   3172 O OE1 . GLN D 4 7   ? 7.458  -3.630  -44.775 1.00 30.20  ?  6   GLN D OE1 1 
ATOM   3173 N NE2 . GLN D 4 7   ? 7.627  -2.690  -46.826 1.00 27.12  ?  6   GLN D NE2 1 
ATOM   3174 N N   . ALA D 4 8   ? 1.011  -3.214  -47.215 1.00 37.66  ?  7   ALA D N   1 
ATOM   3175 C CA  . ALA D 4 8   ? -0.198 -3.908  -47.671 1.00 38.21  ?  7   ALA D CA  1 
ATOM   3176 C C   . ALA D 4 8   ? -0.020 -4.648  -49.002 1.00 37.28  ?  7   ALA D C   1 
ATOM   3177 O O   . ALA D 4 8   ? -0.703 -5.651  -49.215 1.00 31.92  ?  7   ALA D O   1 
ATOM   3178 C CB  . ALA D 4 8   ? -1.362 -2.924  -47.785 1.00 33.77  ?  7   ALA D CB  1 
ATOM   3179 N N   . GLN D 4 9   ? 0.843  -4.159  -49.907 1.00 30.31  ?  8   GLN D N   1 
ATOM   3180 C CA  . GLN D 4 9   ? 1.189  -4.847  -51.153 1.00 39.51  ?  8   GLN D CA  1 
ATOM   3181 C C   . GLN D 4 9   ? 2.221  -5.934  -50.857 1.00 40.46  ?  8   GLN D C   1 
ATOM   3182 O O   . GLN D 4 9   ? 3.367  -5.630  -50.504 1.00 41.03  ?  8   GLN D O   1 
ATOM   3183 C CB  . GLN D 4 9   ? 1.761  -3.860  -52.171 1.00 40.97  ?  8   GLN D CB  1 
ATOM   3184 C CG  . GLN D 4 9   ? 1.162  -2.444  -52.099 1.00 43.81  ?  8   GLN D CG  1 
ATOM   3185 C CD  . GLN D 4 9   ? 2.154  -1.311  -52.434 1.00 45.84  ?  8   GLN D CD  1 
ATOM   3186 O OE1 . GLN D 4 9   ? 3.069  -1.022  -51.656 1.00 41.72  ?  8   GLN D OE1 1 
ATOM   3187 N NE2 . GLN D 4 9   ? 1.953  -0.650  -53.586 1.00 40.93  ?  8   GLN D NE2 1 
ATOM   3188 N N   . SER D 4 10  ? 1.840  -7.202  -51.007 1.00 39.71  ?  9   SER D N   1 
ATOM   3189 C CA  . SER D 4 10  ? 2.824  -8.256  -50.792 1.00 40.54  ?  9   SER D CA  1 
ATOM   3190 C C   . SER D 4 10  ? 3.892  -8.247  -51.875 1.00 38.39  ?  9   SER D C   1 
ATOM   3191 O O   . SER D 4 10  ? 5.030  -8.649  -51.627 1.00 41.52  ?  9   SER D O   1 
ATOM   3192 C CB  . SER D 4 10  ? 2.132  -9.617  -50.732 1.00 47.95  ?  9   SER D CB  1 
ATOM   3193 O OG  . SER D 4 10  ? 1.274  -9.772  -51.850 1.00 51.22  ?  9   SER D OG  1 
ATOM   3194 N N   . SER D 4 11  ? 3.555  -7.774  -53.072 1.00 38.60  ?  10  SER D N   1 
ATOM   3195 C CA  . SER D 4 11  ? 4.470  -7.838  -54.201 1.00 42.45  ?  10  SER D CA  1 
ATOM   3196 C C   . SER D 4 11  ? 4.032  -6.816  -55.241 1.00 43.68  ?  10  SER D C   1 
ATOM   3197 O O   . SER D 4 11  ? 2.852  -6.457  -55.319 1.00 44.08  ?  10  SER D O   1 
ATOM   3198 C CB  . SER D 4 11  ? 4.507  -9.246  -54.811 1.00 43.31  ?  10  SER D CB  1 
ATOM   3199 O OG  . SER D 4 11  ? 3.324  -9.500  -55.528 1.00 48.69  ?  10  SER D OG  1 
ATOM   3200 N N   . VAL D 4 12  ? 4.998  -6.363  -56.034 1.00 31.19  ?  11  VAL D N   1 
ATOM   3201 C CA  . VAL D 4 12  ? 4.812  -5.287  -56.994 1.00 39.99  ?  11  VAL D CA  1 
ATOM   3202 C C   . VAL D 4 12  ? 5.795  -5.530  -58.116 1.00 40.65  ?  11  VAL D C   1 
ATOM   3203 O O   . VAL D 4 12  ? 6.920  -5.969  -57.865 1.00 36.57  ?  11  VAL D O   1 
ATOM   3204 C CB  . VAL D 4 12  ? 5.069  -3.891  -56.380 1.00 38.38  ?  11  VAL D CB  1 
ATOM   3205 C CG1 . VAL D 4 12  ? 5.087  -2.834  -57.470 1.00 41.22  ?  11  VAL D CG1 1 
ATOM   3206 C CG2 . VAL D 4 12  ? 4.030  -3.572  -55.353 1.00 43.16  ?  11  VAL D CG2 1 
ATOM   3207 N N   . SER D 4 13  ? 5.374  -5.244  -59.354 1.00 35.46  ?  12  SER D N   1 
ATOM   3208 C CA  . SER D 4 13  ? 6.274  -5.284  -60.498 1.00 37.01  ?  12  SER D CA  1 
ATOM   3209 C C   . SER D 4 13  ? 6.148  -3.985  -61.266 1.00 33.77  ?  12  SER D C   1 
ATOM   3210 O O   . SER D 4 13  ? 5.058  -3.423  -61.364 1.00 40.61  ?  12  SER D O   1 
ATOM   3211 C CB  . SER D 4 13  ? 5.976  -6.470  -61.431 1.00 39.42  ?  12  SER D CB  1 
ATOM   3212 O OG  . SER D 4 13  ? 5.857  -7.662  -60.672 1.00 45.43  ?  12  SER D OG  1 
ATOM   3213 N N   . MET D 4 14  ? 7.263  -3.541  -61.834 1.00 34.33  ?  13  MET D N   1 
ATOM   3214 C CA  . MET D 4 14  ? 7.344  -2.296  -62.574 1.00 35.05  ?  13  MET D CA  1 
ATOM   3215 C C   . MET D 4 14  ? 8.470  -2.420  -63.600 1.00 40.03  ?  13  MET D C   1 
ATOM   3216 O O   . MET D 4 14  ? 9.436  -3.149  -63.362 1.00 36.65  ?  13  MET D O   1 
ATOM   3217 C CB  . MET D 4 14  ? 7.589  -1.115  -61.618 1.00 37.55  ?  13  MET D CB  1 
ATOM   3218 C CG  . MET D 4 14  ? 7.161  0.264   -62.154 1.00 54.89  ?  13  MET D CG  1 
ATOM   3219 S SD  . MET D 4 14  ? 5.403  0.731   -62.061 1.00 61.05  ?  13  MET D SD  1 
ATOM   3220 C CE  . MET D 4 14  ? 4.726  -0.415  -60.875 1.00 36.51  ?  13  MET D CE  1 
ATOM   3221 N N   . PRO D 4 15  ? 8.348  -1.746  -64.756 1.00 37.43  ?  14  PRO D N   1 
ATOM   3222 C CA  . PRO D 4 15  ? 9.404  -1.837  -65.778 1.00 35.19  ?  14  PRO D CA  1 
ATOM   3223 C C   . PRO D 4 15  ? 10.672 -1.099  -65.381 1.00 40.32  ?  14  PRO D C   1 
ATOM   3224 O O   . PRO D 4 15  ? 10.653 -0.120  -64.630 1.00 35.94  ?  14  PRO D O   1 
ATOM   3225 C CB  . PRO D 4 15  ? 8.767  -1.175  -67.010 1.00 37.71  ?  14  PRO D CB  1 
ATOM   3226 C CG  . PRO D 4 15  ? 7.285  -1.051  -66.682 1.00 42.53  ?  14  PRO D CG  1 
ATOM   3227 C CD  . PRO D 4 15  ? 7.218  -0.920  -65.201 1.00 41.60  ?  14  PRO D CD  1 
ATOM   3228 N N   . VAL D 4 16  ? 11.789 -1.590  -65.920 1.00 34.72  ?  15  VAL D N   1 
ATOM   3229 C CA  . VAL D 4 16  ? 13.057 -0.896  -65.771 1.00 33.26  ?  15  VAL D CA  1 
ATOM   3230 C C   . VAL D 4 16  ? 12.876 0.555   -66.203 1.00 41.50  ?  15  VAL D C   1 
ATOM   3231 O O   . VAL D 4 16  ? 11.999 0.879   -67.005 1.00 38.08  ?  15  VAL D O   1 
ATOM   3232 C CB  . VAL D 4 16  ? 14.118 -1.626  -66.611 1.00 35.12  ?  15  VAL D CB  1 
ATOM   3233 C CG1 . VAL D 4 16  ? 13.702 -1.582  -68.113 1.00 45.92  ?  15  VAL D CG1 1 
ATOM   3234 C CG2 . VAL D 4 16  ? 15.481 -1.062  -66.412 1.00 40.17  ?  15  VAL D CG2 1 
ATOM   3235 N N   . ARG D 4 17  ? 13.664 1.444   -65.611 1.00 40.20  ?  16  ARG D N   1 
ATOM   3236 C CA  . ARG D 4 17  ? 13.742 2.863   -65.933 1.00 41.63  ?  16  ARG D CA  1 
ATOM   3237 C C   . ARG D 4 17  ? 12.542 3.683   -65.421 1.00 39.55  ?  16  ARG D C   1 
ATOM   3238 O O   . ARG D 4 17  ? 12.612 4.905   -65.445 1.00 44.15  ?  16  ARG D O   1 
ATOM   3239 C CB  . ARG D 4 17  ? 13.915 3.115   -67.444 1.00 47.31  ?  16  ARG D CB  1 
ATOM   3240 C CG  . ARG D 4 17  ? 15.250 2.617   -67.986 1.00 50.63  ?  16  ARG D CG  1 
ATOM   3241 C CD  . ARG D 4 17  ? 15.307 2.640   -69.523 1.00 58.48  ?  16  ARG D CD  1 
ATOM   3242 N NE  . ARG D 4 17  ? 15.824 1.376   -70.074 1.00 66.94  ?  16  ARG D NE  1 
ATOM   3243 C CZ  . ARG D 4 17  ? 15.154 0.562   -70.900 1.00 64.40  ?  16  ARG D CZ  1 
ATOM   3244 N NH1 . ARG D 4 17  ? 13.922 0.869   -71.300 1.00 61.77  ?  16  ARG D NH1 1 
ATOM   3245 N NH2 . ARG D 4 17  ? 15.718 -0.568  -71.330 1.00 58.17  ?  16  ARG D NH2 1 
ATOM   3246 N N   . LYS D 4 18  ? 11.461 3.070   -64.957 1.00 37.35  ?  17  LYS D N   1 
ATOM   3247 C CA  . LYS D 4 18  ? 10.358 3.833   -64.384 1.00 35.45  ?  17  LYS D CA  1 
ATOM   3248 C C   . LYS D 4 18  ? 10.590 4.039   -62.883 1.00 42.19  ?  17  LYS D C   1 
ATOM   3249 O O   . LYS D 4 18  ? 11.646 3.697   -62.343 1.00 39.77  ?  17  LYS D O   1 
ATOM   3250 C CB  . LYS D 4 18  ? 9.030  3.129   -64.647 1.00 34.87  ?  17  LYS D CB  1 
ATOM   3251 C CG  . LYS D 4 18  ? 8.833  2.691   -66.109 1.00 43.03  ?  17  LYS D CG  1 
ATOM   3252 C CD  . LYS D 4 18  ? 8.845  3.896   -67.014 1.00 36.90  ?  17  LYS D CD  1 
ATOM   3253 C CE  . LYS D 4 18  ? 7.729  4.856   -66.619 1.00 45.71  ?  17  LYS D CE  1 
ATOM   3254 N NZ  . LYS D 4 18  ? 7.513  5.931   -67.639 1.00 59.63  ?  17  LYS D NZ  1 
ATOM   3255 N N   . ALA D 4 19  ? 9.583  4.569   -62.189 1.00 40.85  ?  18  ALA D N   1 
ATOM   3256 C CA  . ALA D 4 19  ? 9.621  4.804   -60.756 1.00 36.14  ?  18  ALA D CA  1 
ATOM   3257 C C   . ALA D 4 19  ? 8.638  3.883   -60.048 1.00 43.01  ?  18  ALA D C   1 
ATOM   3258 O O   . ALA D 4 19  ? 7.634  3.460   -60.629 1.00 42.30  ?  18  ALA D O   1 
ATOM   3259 C CB  . ALA D 4 19  ? 9.275  6.261   -60.448 1.00 41.95  ?  18  ALA D CB  1 
ATOM   3260 N N   . VAL D 4 20  ? 8.912  3.574   -58.781 1.00 33.19  ?  19  VAL D N   1 
ATOM   3261 C CA  . VAL D 4 20  ? 7.974  2.779   -58.003 1.00 34.07  ?  19  VAL D CA  1 
ATOM   3262 C C   . VAL D 4 20  ? 7.814  3.403   -56.623 1.00 36.25  ?  19  VAL D C   1 
ATOM   3263 O O   . VAL D 4 20  ? 8.751  3.990   -56.079 1.00 35.05  ?  19  VAL D O   1 
ATOM   3264 C CB  . VAL D 4 20  ? 8.417  1.287   -57.922 1.00 38.52  ?  19  VAL D CB  1 
ATOM   3265 C CG1 . VAL D 4 20  ? 9.615  1.067   -56.952 1.00 34.24  ?  19  VAL D CG1 1 
ATOM   3266 C CG2 . VAL D 4 20  ? 7.267  0.422   -57.519 1.00 36.05  ?  19  VAL D CG2 1 
ATOM   3267 N N   . THR D 4 21  ? 6.605  3.290   -56.068 1.00 32.28  ?  20  THR D N   1 
ATOM   3268 C CA  . THR D 4 21  ? 6.296  3.750   -54.723 1.00 38.93  ?  20  THR D CA  1 
ATOM   3269 C C   . THR D 4 21  ? 5.861  2.541   -53.901 1.00 43.66  ?  20  THR D C   1 
ATOM   3270 O O   . THR D 4 21  ? 4.926  1.826   -54.290 1.00 39.44  ?  20  THR D O   1 
ATOM   3271 C CB  . THR D 4 21  ? 5.205  4.832   -54.747 1.00 35.96  ?  20  THR D CB  1 
ATOM   3272 O OG1 . THR D 4 21  ? 5.704  6.016   -55.413 1.00 31.57  ?  20  THR D OG1 1 
ATOM   3273 C CG2 . THR D 4 21  ? 4.745  5.160   -53.326 1.00 36.97  ?  20  THR D CG2 1 
ATOM   3274 N N   . LEU D 4 22  ? 6.553  2.291   -52.786 1.00 38.91  ?  21  LEU D N   1 
ATOM   3275 C CA  . LEU D 4 22  ? 6.234  1.176   -51.892 1.00 33.60  ?  21  LEU D CA  1 
ATOM   3276 C C   . LEU D 4 22  ? 5.641  1.740   -50.612 1.00 38.16  ?  21  LEU D C   1 
ATOM   3277 O O   . LEU D 4 22  ? 6.305  2.504   -49.897 1.00 31.79  ?  21  LEU D O   1 
ATOM   3278 C CB  . LEU D 4 22  ? 7.472  0.335   -51.595 1.00 35.25  ?  21  LEU D CB  1 
ATOM   3279 C CG  . LEU D 4 22  ? 8.248  -0.013  -52.869 1.00 36.96  ?  21  LEU D CG  1 
ATOM   3280 C CD1 . LEU D 4 22  ? 9.661  -0.470  -52.533 1.00 37.69  ?  21  LEU D CD1 1 
ATOM   3281 C CD2 . LEU D 4 22  ? 7.489  -1.066  -53.723 1.00 36.81  ?  21  LEU D CD2 1 
ATOM   3282 N N   . ASN D 4 23  ? 4.401  1.363   -50.323 1.00 34.94  ?  22  ASN D N   1 
ATOM   3283 C CA  . ASN D 4 23  ? 3.652  2.018   -49.263 1.00 35.06  ?  22  ASN D CA  1 
ATOM   3284 C C   . ASN D 4 23  ? 3.947  1.410   -47.906 1.00 38.61  ?  22  ASN D C   1 
ATOM   3285 O O   . ASN D 4 23  ? 4.218  0.210   -47.775 1.00 32.52  ?  22  ASN D O   1 
ATOM   3286 C CB  . ASN D 4 23  ? 2.158  1.940   -49.505 1.00 34.63  ?  22  ASN D CB  1 
ATOM   3287 C CG  . ASN D 4 23  ? 1.732  2.721   -50.712 1.00 43.89  ?  22  ASN D CG  1 
ATOM   3288 O OD1 . ASN D 4 23  ? 2.161  3.865   -50.926 1.00 42.16  ?  22  ASN D OD1 1 
ATOM   3289 N ND2 . ASN D 4 23  ? 0.882  2.109   -51.517 1.00 40.52  ?  22  ASN D ND2 1 
ATOM   3290 N N   . CYS D 4 24  ? 3.851  2.248   -46.880 1.00 34.21  ?  23  CYS D N   1 
ATOM   3291 C CA  . CYS D 4 24  ? 4.023  1.757   -45.524 1.00 32.54  ?  23  CYS D CA  1 
ATOM   3292 C C   . CYS D 4 24  ? 3.145  2.612   -44.622 1.00 31.40  ?  23  CYS D C   1 
ATOM   3293 O O   . CYS D 4 24  ? 3.199  3.845   -44.688 1.00 32.02  ?  23  CYS D O   1 
ATOM   3294 C CB  . CYS D 4 24  ? 5.502  1.770   -45.132 1.00 29.72  ?  23  CYS D CB  1 
ATOM   3295 S SG  . CYS D 4 24  ? 5.662  1.645   -43.381 1.00 34.62  ?  23  CYS D SG  1 
ATOM   3296 N N   . LEU D 4 25  ? 2.249  1.965   -43.878 1.00 31.38  ?  24  LEU D N   1 
ATOM   3297 C CA  . LEU D 4 25  ? 1.400  2.604   -42.893 1.00 36.90  ?  24  LEU D CA  1 
ATOM   3298 C C   . LEU D 4 25  ? 1.730  1.992   -41.541 1.00 40.31  ?  24  LEU D C   1 
ATOM   3299 O O   . LEU D 4 25  ? 2.093  0.813   -41.463 1.00 33.04  ?  24  LEU D O   1 
ATOM   3300 C CB  . LEU D 4 25  ? -0.089 2.386   -43.209 1.00 41.94  ?  24  LEU D CB  1 
ATOM   3301 C CG  . LEU D 4 25  ? -0.566 2.831   -44.597 1.00 37.64  ?  24  LEU D CG  1 
ATOM   3302 C CD1 . LEU D 4 25  ? -2.052 2.464   -44.822 1.00 41.65  ?  24  LEU D CD1 1 
ATOM   3303 C CD2 . LEU D 4 25  ? -0.337 4.325   -44.766 1.00 39.98  ?  24  LEU D CD2 1 
ATOM   3304 N N   . TYR D 4 26  ? 1.588  2.773   -40.471 1.00 33.75  ?  25  TYR D N   1 
ATOM   3305 C CA  . TYR D 4 26  ? 1.981  2.281   -39.162 1.00 34.19  ?  25  TYR D CA  1 
ATOM   3306 C C   . TYR D 4 26  ? 1.018  2.790   -38.103 1.00 35.61  ?  25  TYR D C   1 
ATOM   3307 O O   . TYR D 4 26  ? 0.382  3.834   -38.267 1.00 35.96  ?  25  TYR D O   1 
ATOM   3308 C CB  . TYR D 4 26  ? 3.439  2.690   -38.839 1.00 33.59  ?  25  TYR D CB  1 
ATOM   3309 C CG  . TYR D 4 26  ? 3.734  4.177   -38.891 1.00 34.65  ?  25  TYR D CG  1 
ATOM   3310 C CD1 . TYR D 4 26  ? 4.029  4.793   -40.083 1.00 27.17  ?  25  TYR D CD1 1 
ATOM   3311 C CD2 . TYR D 4 26  ? 3.744  4.955   -37.728 1.00 37.92  ?  25  TYR D CD2 1 
ATOM   3312 C CE1 . TYR D 4 26  ? 4.311  6.142   -40.148 1.00 40.30  ?  25  TYR D CE1 1 
ATOM   3313 C CE2 . TYR D 4 26  ? 4.035  6.320   -37.781 1.00 31.10  ?  25  TYR D CE2 1 
ATOM   3314 C CZ  . TYR D 4 26  ? 4.314  6.902   -38.988 1.00 33.59  ?  25  TYR D CZ  1 
ATOM   3315 O OH  . TYR D 4 26  ? 4.605  8.238   -39.077 1.00 32.94  ?  25  TYR D OH  1 
ATOM   3316 N N   . GLU D 4 27  ? 0.901  2.021   -37.025 1.00 34.42  ?  26  GLU D N   1 
ATOM   3317 C CA  . GLU D 4 27  ? 0.180  2.419   -35.830 1.00 42.55  ?  26  GLU D CA  1 
ATOM   3318 C C   . GLU D 4 27  ? 1.138  2.364   -34.651 1.00 40.32  ?  26  GLU D C   1 
ATOM   3319 O O   . GLU D 4 27  ? 1.848  1.367   -34.470 1.00 37.70  ?  26  GLU D O   1 
ATOM   3320 C CB  . GLU D 4 27  ? -1.025 1.513   -35.549 1.00 39.40  ?  26  GLU D CB  1 
ATOM   3321 C CG  . GLU D 4 27  ? -1.854 1.109   -36.723 1.00 51.97  ?  26  GLU D CG  1 
ATOM   3322 C CD  . GLU D 4 27  ? -2.594 -0.175  -36.418 1.00 63.18  ?  26  GLU D CD  1 
ATOM   3323 O OE1 . GLU D 4 27  ? -3.095 -0.293  -35.268 1.00 58.92  ?  26  GLU D OE1 1 
ATOM   3324 O OE2 . GLU D 4 27  ? -2.632 -1.073  -37.299 1.00 58.42  -1 26  GLU D OE2 1 
ATOM   3325 N N   . THR D 4 28  ? 1.131  3.406   -33.834 1.00 38.87  ?  27  THR D N   1 
ATOM   3326 C CA  . THR D 4 28  ? 2.056  3.470   -32.716 1.00 40.20  ?  27  THR D CA  1 
ATOM   3327 C C   . THR D 4 28  ? 1.550  4.525   -31.760 1.00 37.09  ?  27  THR D C   1 
ATOM   3328 O O   . THR D 4 28  ? 0.984  5.533   -32.186 1.00 31.43  ?  27  THR D O   1 
ATOM   3329 C CB  . THR D 4 28  ? 3.464  3.844   -33.176 1.00 38.65  ?  27  THR D CB  1 
ATOM   3330 O OG1 . THR D 4 28  ? 4.342  3.868   -32.045 1.00 36.82  ?  27  THR D OG1 1 
ATOM   3331 C CG2 . THR D 4 28  ? 3.424  5.227   -33.811 1.00 36.18  ?  27  THR D CG2 1 
ATOM   3332 N N   . SER D 4 29  ? 1.744  4.277   -30.473 1.00 33.03  ?  28  SER D N   1 
ATOM   3333 C CA  . SER D 4 29  ? 1.561  5.325   -29.487 1.00 41.09  ?  28  SER D CA  1 
ATOM   3334 C C   . SER D 4 29  ? 2.825  6.155   -29.291 1.00 41.17  ?  28  SER D C   1 
ATOM   3335 O O   . SER D 4 29  ? 2.797  7.124   -28.523 1.00 42.80  ?  28  SER D O   1 
ATOM   3336 C CB  . SER D 4 29  ? 1.099  4.724   -28.167 1.00 40.01  ?  28  SER D CB  1 
ATOM   3337 O OG  . SER D 4 29  ? 2.137  3.957   -27.602 1.00 49.88  ?  28  SER D OG  1 
ATOM   3338 N N   . TRP D 4 30  ? 3.913  5.822   -29.994 1.00 38.67  ?  29  TRP D N   1 
ATOM   3339 C CA  . TRP D 4 30  ? 5.142  6.610   -29.931 1.00 35.61  ?  29  TRP D CA  1 
ATOM   3340 C C   . TRP D 4 30  ? 4.936  7.921   -30.670 1.00 43.65  ?  29  TRP D C   1 
ATOM   3341 O O   . TRP D 4 30  ? 4.464  7.923   -31.808 1.00 37.16  ?  29  TRP D O   1 
ATOM   3342 C CB  . TRP D 4 30  ? 6.323  5.866   -30.572 1.00 33.31  ?  29  TRP D CB  1 
ATOM   3343 C CG  . TRP D 4 30  ? 6.633  4.469   -30.042 1.00 31.59  ?  29  TRP D CG  1 
ATOM   3344 C CD1 . TRP D 4 30  ? 6.108  3.867   -28.936 1.00 35.86  ?  29  TRP D CD1 1 
ATOM   3345 C CD2 . TRP D 4 30  ? 7.555  3.527   -30.614 1.00 26.12  ?  29  TRP D CD2 1 
ATOM   3346 N NE1 . TRP D 4 30  ? 6.648  2.609   -28.784 1.00 34.37  ?  29  TRP D NE1 1 
ATOM   3347 C CE2 . TRP D 4 30  ? 7.528  2.374   -29.811 1.00 33.05  ?  29  TRP D CE2 1 
ATOM   3348 C CE3 . TRP D 4 30  ? 8.379  3.541   -31.749 1.00 28.78  ?  29  TRP D CE3 1 
ATOM   3349 C CZ2 . TRP D 4 30  ? 8.311  1.237   -30.101 1.00 31.27  ?  29  TRP D CZ2 1 
ATOM   3350 C CZ3 . TRP D 4 30  ? 9.146  2.418   -32.041 1.00 26.22  ?  29  TRP D CZ3 1 
ATOM   3351 C CH2 . TRP D 4 30  ? 9.107  1.285   -31.218 1.00 30.45  ?  29  TRP D CH2 1 
ATOM   3352 N N   . TRP D 4 31  ? 5.336  9.038   -30.052 1.00 42.51  ?  30  TRP D N   1 
ATOM   3353 C CA  . TRP D 4 31  ? 5.217  10.330  -30.704 1.00 29.97  ?  30  TRP D CA  1 
ATOM   3354 C C   . TRP D 4 31  ? 6.548  10.923  -31.134 1.00 31.21  ?  30  TRP D C   1 
ATOM   3355 O O   . TRP D 4 31  ? 6.568  11.970  -31.804 1.00 30.54  ?  30  TRP D O   1 
ATOM   3356 C CB  . TRP D 4 31  ? 4.464  11.305  -29.793 1.00 34.58  ?  30  TRP D CB  1 
ATOM   3357 C CG  . TRP D 4 31  ? 4.953  11.458  -28.340 1.00 30.04  ?  30  TRP D CG  1 
ATOM   3358 C CD1 . TRP D 4 31  ? 4.465  10.831  -27.228 1.00 27.16  ?  30  TRP D CD1 1 
ATOM   3359 C CD2 . TRP D 4 31  ? 5.967  12.352  -27.888 1.00 26.30  ?  30  TRP D CD2 1 
ATOM   3360 N NE1 . TRP D 4 31  ? 5.121  11.285  -26.106 1.00 35.36  ?  30  TRP D NE1 1 
ATOM   3361 C CE2 . TRP D 4 31  ? 6.051  12.220  -26.492 1.00 32.14  ?  30  TRP D CE2 1 
ATOM   3362 C CE3 . TRP D 4 31  ? 6.814  13.261  -28.538 1.00 30.02  ?  30  TRP D CE3 1 
ATOM   3363 C CZ2 . TRP D 4 31  ? 6.957  12.959  -25.726 1.00 34.27  ?  30  TRP D CZ2 1 
ATOM   3364 C CZ3 . TRP D 4 31  ? 7.710  13.997  -27.774 1.00 32.66  ?  30  TRP D CZ3 1 
ATOM   3365 C CH2 . TRP D 4 31  ? 7.780  13.832  -26.390 1.00 26.80  ?  30  TRP D CH2 1 
ATOM   3366 N N   . SER D 4 32  ? 7.655  10.278  -30.790 1.00 28.83  ?  31  SER D N   1 
ATOM   3367 C CA  . SER D 4 32  ? 8.978  10.630  -31.293 1.00 31.06  ?  31  SER D CA  1 
ATOM   3368 C C   . SER D 4 32  ? 9.590  9.321   -31.772 1.00 33.83  ?  31  SER D C   1 
ATOM   3369 O O   . SER D 4 32  ? 9.588  8.344   -31.014 1.00 33.39  ?  31  SER D O   1 
ATOM   3370 C CB  . SER D 4 32  ? 9.845  11.290  -30.184 1.00 29.98  ?  31  SER D CB  1 
ATOM   3371 O OG  . SER D 4 32  ? 10.998 11.931  -30.726 1.00 28.87  ?  31  SER D OG  1 
ATOM   3372 N N   . TYR D 4 33  ? 10.030 9.271   -33.036 1.00 33.84  ?  32  TYR D N   1 
ATOM   3373 C CA  . TYR D 4 33  ? 10.412 8.002   -33.650 1.00 31.56  ?  32  TYR D CA  1 
ATOM   3374 C C   . TYR D 4 33  ? 11.126 8.243   -34.978 1.00 33.83  ?  32  TYR D C   1 
ATOM   3375 O O   . TYR D 4 33  ? 11.259 9.378   -35.446 1.00 33.16  ?  32  TYR D O   1 
ATOM   3376 C CB  . TYR D 4 33  ? 9.194  7.091   -33.853 1.00 31.24  ?  32  TYR D CB  1 
ATOM   3377 C CG  . TYR D 4 33  ? 8.042  7.743   -34.616 1.00 35.07  ?  32  TYR D CG  1 
ATOM   3378 C CD1 . TYR D 4 33  ? 8.044  7.781   -36.009 1.00 34.66  ?  32  TYR D CD1 1 
ATOM   3379 C CD2 . TYR D 4 33  ? 6.970  8.339   -33.937 1.00 32.77  ?  32  TYR D CD2 1 
ATOM   3380 C CE1 . TYR D 4 33  ? 6.988  8.366   -36.726 1.00 39.31  ?  32  TYR D CE1 1 
ATOM   3381 C CE2 . TYR D 4 33  ? 5.905  8.940   -34.648 1.00 40.39  ?  32  TYR D CE2 1 
ATOM   3382 C CZ  . TYR D 4 33  ? 5.926  8.936   -36.040 1.00 37.56  ?  32  TYR D CZ  1 
ATOM   3383 O OH  . TYR D 4 33  ? 4.901  9.517   -36.749 1.00 39.97  ?  32  TYR D OH  1 
ATOM   3384 N N   . TYR D 4 34  ? 11.617 7.143   -35.561 1.00 29.67  ?  33  TYR D N   1 
ATOM   3385 C CA  . TYR D 4 34  ? 12.187 7.130   -36.901 1.00 29.55  ?  33  TYR D CA  1 
ATOM   3386 C C   . TYR D 4 34  ? 11.485 6.043   -37.704 1.00 29.37  ?  33  TYR D C   1 
ATOM   3387 O O   . TYR D 4 34  ? 10.887 5.127   -37.144 1.00 30.88  ?  33  TYR D O   1 
ATOM   3388 C CB  . TYR D 4 34  ? 13.704 6.859   -36.929 1.00 35.44  ?  33  TYR D CB  1 
ATOM   3389 C CG  . TYR D 4 34  ? 14.520 7.702   -35.978 1.00 36.22  ?  33  TYR D CG  1 
ATOM   3390 C CD1 . TYR D 4 34  ? 14.564 7.377   -34.638 1.00 39.49  ?  33  TYR D CD1 1 
ATOM   3391 C CD2 . TYR D 4 34  ? 15.227 8.826   -36.412 1.00 42.02  ?  33  TYR D CD2 1 
ATOM   3392 C CE1 . TYR D 4 34  ? 15.278 8.131   -33.733 1.00 46.36  ?  33  TYR D CE1 1 
ATOM   3393 C CE2 . TYR D 4 34  ? 15.968 9.611   -35.490 1.00 39.12  ?  33  TYR D CE2 1 
ATOM   3394 C CZ  . TYR D 4 34  ? 15.975 9.241   -34.152 1.00 38.12  ?  33  TYR D CZ  1 
ATOM   3395 O OH  . TYR D 4 34  ? 16.665 9.939   -33.179 1.00 43.92  ?  33  TYR D OH  1 
ATOM   3396 N N   . ILE D 4 35  ? 11.578 6.150   -39.025 1.00 28.92  ?  34  ILE D N   1 
ATOM   3397 C CA  . ILE D 4 35  ? 11.143 5.107   -39.944 1.00 29.82  ?  34  ILE D CA  1 
ATOM   3398 C C   . ILE D 4 35  ? 12.338 4.676   -40.768 1.00 26.87  ?  34  ILE D C   1 
ATOM   3399 O O   . ILE D 4 35  ? 12.962 5.513   -41.431 1.00 28.93  ?  34  ILE D O   1 
ATOM   3400 C CB  . ILE D 4 35  ? 10.034 5.587   -40.892 1.00 33.25  ?  34  ILE D CB  1 
ATOM   3401 C CG1 . ILE D 4 35  ? 8.754  5.856   -40.112 1.00 33.07  ?  34  ILE D CG1 1 
ATOM   3402 C CG2 . ILE D 4 35  ? 9.860  4.531   -42.004 1.00 29.50  ?  34  ILE D CG2 1 
ATOM   3403 C CD1 . ILE D 4 35  ? 7.941  4.592   -39.775 1.00 34.95  ?  34  ILE D CD1 1 
ATOM   3404 N N   . PHE D 4 36  ? 12.632 3.374   -40.773 1.00 25.47  ?  35  PHE D N   1 
ATOM   3405 C CA  . PHE D 4 36  ? 13.755 2.854   -41.548 1.00 28.72  ?  35  PHE D CA  1 
ATOM   3406 C C   . PHE D 4 36  ? 13.247 2.101   -42.772 1.00 28.73  ?  35  PHE D C   1 
ATOM   3407 O O   . PHE D 4 36  ? 12.267 1.359   -42.684 1.00 29.31  ?  35  PHE D O   1 
ATOM   3408 C CB  . PHE D 4 36  ? 14.643 1.901   -40.730 1.00 29.67  ?  35  PHE D CB  1 
ATOM   3409 C CG  . PHE D 4 36  ? 14.946 2.386   -39.350 1.00 30.14  ?  35  PHE D CG  1 
ATOM   3410 C CD1 . PHE D 4 36  ? 15.866 3.391   -39.145 1.00 30.75  ?  35  PHE D CD1 1 
ATOM   3411 C CD2 . PHE D 4 36  ? 14.292 1.835   -38.252 1.00 33.04  ?  35  PHE D CD2 1 
ATOM   3412 C CE1 . PHE D 4 36  ? 16.137 3.838   -37.862 1.00 30.06  ?  35  PHE D CE1 1 
ATOM   3413 C CE2 . PHE D 4 36  ? 14.564 2.277   -36.969 1.00 34.08  ?  35  PHE D CE2 1 
ATOM   3414 C CZ  . PHE D 4 36  ? 15.476 3.286   -36.783 1.00 28.18  ?  35  PHE D CZ  1 
ATOM   3415 N N   . TRP D 4 37  ? 13.951 2.258   -43.891 1.00 24.13  ?  36  TRP D N   1 
ATOM   3416 C CA  . TRP D 4 37  ? 13.724 1.446   -45.079 1.00 35.59  ?  36  TRP D CA  1 
ATOM   3417 C C   . TRP D 4 37  ? 14.957 0.597   -45.362 1.00 31.09  ?  36  TRP D C   1 
ATOM   3418 O O   . TRP D 4 37  ? 16.085 1.112   -45.392 1.00 30.55  ?  36  TRP D O   1 
ATOM   3419 C CB  . TRP D 4 37  ? 13.375 2.309   -46.312 1.00 28.18  ?  36  TRP D CB  1 
ATOM   3420 C CG  . TRP D 4 37  ? 11.940 2.715   -46.313 1.00 31.62  ?  36  TRP D CG  1 
ATOM   3421 C CD1 . TRP D 4 37  ? 11.416 3.883   -45.844 1.00 36.92  ?  36  TRP D CD1 1 
ATOM   3422 C CD2 . TRP D 4 37  ? 10.830 1.936   -46.786 1.00 34.96  ?  36  TRP D CD2 1 
ATOM   3423 N NE1 . TRP D 4 37  ? 10.041 3.882   -45.989 1.00 34.92  ?  36  TRP D NE1 1 
ATOM   3424 C CE2 . TRP D 4 37  ? 9.659  2.702   -46.578 1.00 35.83  ?  36  TRP D CE2 1 
ATOM   3425 C CE3 . TRP D 4 37  ? 10.715 0.669   -47.375 1.00 32.77  ?  36  TRP D CE3 1 
ATOM   3426 C CZ2 . TRP D 4 37  ? 8.382  2.245   -46.956 1.00 31.26  ?  36  TRP D CZ2 1 
ATOM   3427 C CZ3 . TRP D 4 37  ? 9.453  0.210   -47.750 1.00 36.67  ?  36  TRP D CZ3 1 
ATOM   3428 C CH2 . TRP D 4 37  ? 8.300  0.999   -47.535 1.00 35.55  ?  36  TRP D CH2 1 
ATOM   3429 N N   . TYR D 4 38  ? 14.720 -0.699  -45.592 1.00 34.05  ?  37  TYR D N   1 
ATOM   3430 C CA  . TYR D 4 38  ? 15.753 -1.682  -45.878 1.00 33.80  ?  37  TYR D CA  1 
ATOM   3431 C C   . TYR D 4 38  ? 15.450 -2.424  -47.179 1.00 30.74  ?  37  TYR D C   1 
ATOM   3432 O O   . TYR D 4 38  ? 14.293 -2.593  -47.576 1.00 30.82  ?  37  TYR D O   1 
ATOM   3433 C CB  . TYR D 4 38  ? 15.871 -2.728  -44.743 1.00 33.33  ?  37  TYR D CB  1 
ATOM   3434 C CG  . TYR D 4 38  ? 16.018 -2.162  -43.341 1.00 31.89  ?  37  TYR D CG  1 
ATOM   3435 C CD1 . TYR D 4 38  ? 14.897 -1.877  -42.560 1.00 28.55  ?  37  TYR D CD1 1 
ATOM   3436 C CD2 . TYR D 4 38  ? 17.290 -1.944  -42.786 1.00 33.46  ?  37  TYR D CD2 1 
ATOM   3437 C CE1 . TYR D 4 38  ? 15.030 -1.355  -41.270 1.00 32.79  ?  37  TYR D CE1 1 
ATOM   3438 C CE2 . TYR D 4 38  ? 17.437 -1.434  -41.494 1.00 32.16  ?  37  TYR D CE2 1 
ATOM   3439 C CZ  . TYR D 4 38  ? 16.309 -1.138  -40.744 1.00 35.45  ?  37  TYR D CZ  1 
ATOM   3440 O OH  . TYR D 4 38  ? 16.470 -0.636  -39.466 1.00 34.74  ?  37  TYR D OH  1 
ATOM   3441 N N   . LYS D 4 39  ? 16.520 -2.911  -47.800 1.00 32.32  ?  38  LYS D N   1 
ATOM   3442 C CA  . LYS D 4 39  ? 16.486 -3.696  -49.027 1.00 33.05  ?  38  LYS D CA  1 
ATOM   3443 C C   . LYS D 4 39  ? 17.096 -5.070  -48.740 1.00 36.56  ?  38  LYS D C   1 
ATOM   3444 O O   . LYS D 4 39  ? 18.254 -5.150  -48.320 1.00 31.15  ?  38  LYS D O   1 
ATOM   3445 C CB  . LYS D 4 39  ? 17.269 -2.949  -50.115 1.00 35.29  ?  38  LYS D CB  1 
ATOM   3446 C CG  . LYS D 4 39  ? 17.601 -3.705  -51.374 1.00 31.58  ?  38  LYS D CG  1 
ATOM   3447 C CD  . LYS D 4 39  ? 18.521 -2.899  -52.275 1.00 33.45  ?  38  LYS D CD  1 
ATOM   3448 C CE  . LYS D 4 39  ? 18.486 -3.482  -53.703 1.00 35.36  ?  38  LYS D CE  1 
ATOM   3449 N NZ  . LYS D 4 39  ? 19.739 -3.253  -54.485 1.00 40.70  ?  38  LYS D NZ  1 
ATOM   3450 N N   . GLN D 4 40  ? 16.323 -6.149  -48.933 1.00 27.14  ?  39  GLN D N   1 
ATOM   3451 C CA  . GLN D 4 40  ? 16.849 -7.506  -48.764 1.00 27.94  ?  39  GLN D CA  1 
ATOM   3452 C C   . GLN D 4 40  ? 17.024 -8.145  -50.137 1.00 32.81  ?  39  GLN D C   1 
ATOM   3453 O O   . GLN D 4 40  ? 16.043 -8.342  -50.862 1.00 31.37  ?  39  GLN D O   1 
ATOM   3454 C CB  . GLN D 4 40  ? 15.947 -8.366  -47.870 1.00 27.06  ?  39  GLN D CB  1 
ATOM   3455 C CG  . GLN D 4 40  ? 16.495 -9.785  -47.677 1.00 27.60  ?  39  GLN D CG  1 
ATOM   3456 C CD  . GLN D 4 40  ? 15.785 -10.581 -46.608 1.00 29.47  ?  39  GLN D CD  1 
ATOM   3457 O OE1 . GLN D 4 40  ? 14.556 -10.542 -46.497 1.00 29.07  ?  39  GLN D OE1 1 
ATOM   3458 N NE2 . GLN D 4 40  ? 16.565 -11.302 -45.773 1.00 30.78  ?  39  GLN D NE2 1 
ATOM   3459 N N   . LEU D 4 41  ? 18.267 -8.449  -50.498 1.00 28.82  ?  40  LEU D N   1 
ATOM   3460 C CA  . LEU D 4 41  ? 18.545 -9.066  -51.783 1.00 33.40  ?  40  LEU D CA  1 
ATOM   3461 C C   . LEU D 4 41  ? 18.064 -10.519 -51.827 1.00 34.23  ?  40  LEU D C   1 
ATOM   3462 O O   . LEU D 4 41  ? 17.763 -11.123 -50.792 1.00 31.52  ?  40  LEU D O   1 
ATOM   3463 C CB  . LEU D 4 41  ? 20.037 -9.028  -52.105 1.00 29.26  ?  40  LEU D CB  1 
ATOM   3464 C CG  . LEU D 4 41  ? 20.824 -7.724  -52.016 1.00 36.80  ?  40  LEU D CG  1 
ATOM   3465 C CD1 . LEU D 4 41  ? 22.279 -7.974  -52.429 1.00 32.87  ?  40  LEU D CD1 1 
ATOM   3466 C CD2 . LEU D 4 41  ? 20.192 -6.656  -52.883 1.00 37.72  ?  40  LEU D CD2 1 
ATOM   3467 N N   . PRO D 4 42  ? 17.957 -11.092 -53.040 1.00 36.96  ?  41  PRO D N   1 
ATOM   3468 C CA  . PRO D 4 42  ? 17.649 -12.533 -53.146 1.00 30.51  ?  41  PRO D CA  1 
ATOM   3469 C C   . PRO D 4 42  ? 18.645 -13.427 -52.428 1.00 35.58  ?  41  PRO D C   1 
ATOM   3470 O O   . PRO D 4 42  ? 18.263 -14.492 -51.930 1.00 37.12  ?  41  PRO D O   1 
ATOM   3471 C CB  . PRO D 4 42  ? 17.648 -12.775 -54.666 1.00 35.97  ?  41  PRO D CB  1 
ATOM   3472 C CG  . PRO D 4 42  ? 17.112 -11.448 -55.221 1.00 38.09  ?  41  PRO D CG  1 
ATOM   3473 C CD  . PRO D 4 42  ? 17.792 -10.392 -54.332 1.00 35.91  ?  41  PRO D CD  1 
ATOM   3474 N N   . SER D 4 43  ? 19.907 -13.021 -52.322 1.00 36.10  ?  42  SER D N   1 
ATOM   3475 C CA  . SER D 4 43  ? 20.836 -13.754 -51.467 1.00 37.63  ?  42  SER D CA  1 
ATOM   3476 C C   . SER D 4 43  ? 20.447 -13.749 -49.984 1.00 38.71  ?  42  SER D C   1 
ATOM   3477 O O   . SER D 4 43  ? 21.089 -14.456 -49.202 1.00 38.22  ?  42  SER D O   1 
ATOM   3478 C CB  . SER D 4 43  ? 22.237 -13.162 -51.611 1.00 40.64  ?  42  SER D CB  1 
ATOM   3479 O OG  . SER D 4 43  ? 22.360 -11.965 -50.856 1.00 41.91  ?  42  SER D OG  1 
ATOM   3480 N N   . LYS D 4 44  ? 19.437 -12.978 -49.577 1.00 34.84  ?  43  LYS D N   1 
ATOM   3481 C CA  . LYS D 4 44  ? 18.983 -12.756 -48.190 1.00 32.48  ?  43  LYS D CA  1 
ATOM   3482 C C   . LYS D 4 44  ? 19.861 -11.716 -47.498 1.00 28.61  ?  43  LYS D C   1 
ATOM   3483 O O   . LYS D 4 44  ? 19.599 -11.394 -46.348 1.00 34.22  ?  43  LYS D O   1 
ATOM   3484 C CB  . LYS D 4 44  ? 18.935 -14.026 -47.320 1.00 31.61  ?  43  LYS D CB  1 
ATOM   3485 C CG  . LYS D 4 44  ? 18.099 -15.180 -47.883 1.00 40.96  ?  43  LYS D CG  1 
ATOM   3486 C CD  . LYS D 4 44  ? 16.639 -14.782 -48.114 1.00 42.13  ?  43  LYS D CD  1 
ATOM   3487 C CE  . LYS D 4 44  ? 15.697 -15.960 -47.832 1.00 52.08  ?  43  LYS D CE  1 
ATOM   3488 N NZ  . LYS D 4 44  ? 14.494 -15.952 -48.722 1.00 57.86  ?  43  LYS D NZ  1 
ATOM   3489 N N   . GLU D 4 45  ? 20.879 -11.179 -48.157 1.00 27.53  ?  44  GLU D N   1 
ATOM   3490 C CA  . GLU D 4 45  ? 21.629 -10.074 -47.583 1.00 30.86  ?  44  GLU D CA  1 
ATOM   3491 C C   . GLU D 4 45  ? 20.710 -8.883  -47.328 1.00 37.25  ?  44  GLU D C   1 
ATOM   3492 O O   . GLU D 4 45  ? 19.918 -8.495  -48.195 1.00 35.12  ?  44  GLU D O   1 
ATOM   3493 C CB  . GLU D 4 45  ? 22.766 -9.649  -48.505 1.00 30.99  ?  44  GLU D CB  1 
ATOM   3494 C CG  . GLU D 4 45  ? 23.538 -8.455  -47.944 1.00 34.74  ?  44  GLU D CG  1 
ATOM   3495 C CD  . GLU D 4 45  ? 24.598 -7.895  -48.896 1.00 41.01  ?  44  GLU D CD  1 
ATOM   3496 O OE1 . GLU D 4 45  ? 25.165 -6.821  -48.576 1.00 44.30  ?  44  GLU D OE1 1 
ATOM   3497 O OE2 . GLU D 4 45  ? 24.878 -8.525  -49.946 1.00 45.30  -1 44  GLU D OE2 1 
ATOM   3498 N N   . MET D 4 46  ? 20.849 -8.286  -46.145 1.00 29.98  ?  45  MET D N   1 
ATOM   3499 C CA  . MET D 4 46  ? 20.060 -7.144  -45.706 1.00 25.53  ?  45  MET D CA  1 
ATOM   3500 C C   . MET D 4 46  ? 20.887 -5.869  -45.801 1.00 34.40  ?  45  MET D C   1 
ATOM   3501 O O   . MET D 4 46  ? 22.089 -5.866  -45.508 1.00 34.43  ?  45  MET D O   1 
ATOM   3502 C CB  . MET D 4 46  ? 19.576 -7.368  -44.266 1.00 29.03  ?  45  MET D CB  1 
ATOM   3503 C CG  . MET D 4 46  ? 18.659 -6.298  -43.766 1.00 42.11  ?  45  MET D CG  1 
ATOM   3504 S SD  . MET D 4 46  ? 16.971 -6.520  -44.425 1.00 44.05  ?  45  MET D SD  1 
ATOM   3505 C CE  . MET D 4 46  ? 16.813 -8.262  -44.321 1.00 27.63  ?  45  MET D CE  1 
ATOM   3506 N N   . ILE D 4 47  ? 20.249 -4.785  -46.239 1.00 31.93  ?  46  ILE D N   1 
ATOM   3507 C CA  . ILE D 4 47  ? 20.958 -3.546  -46.534 1.00 31.97  ?  46  ILE D CA  1 
ATOM   3508 C C   . ILE D 4 47  ? 20.091 -2.377  -46.100 1.00 32.83  ?  46  ILE D C   1 
ATOM   3509 O O   . ILE D 4 47  ? 18.917 -2.303  -46.474 1.00 30.73  ?  46  ILE D O   1 
ATOM   3510 C CB  . ILE D 4 47  ? 21.316 -3.407  -48.025 1.00 31.08  ?  46  ILE D CB  1 
ATOM   3511 C CG1 . ILE D 4 47  ? 22.168 -4.590  -48.486 1.00 35.57  ?  46  ILE D CG1 1 
ATOM   3512 C CG2 . ILE D 4 47  ? 22.069 -2.072  -48.303 1.00 29.39  ?  46  ILE D CG2 1 
ATOM   3513 C CD1 . ILE D 4 47  ? 22.198 -4.768  -49.981 1.00 34.17  ?  46  ILE D CD1 1 
ATOM   3514 N N   . PHE D 4 48  ? 20.677 -1.464  -45.324 1.00 34.85  ?  47  PHE D N   1 
ATOM   3515 C CA  . PHE D 4 48  ? 19.982 -0.263  -44.879 1.00 31.69  ?  47  PHE D CA  1 
ATOM   3516 C C   . PHE D 4 48  ? 19.964 0.755   -46.014 1.00 28.24  ?  47  PHE D C   1 
ATOM   3517 O O   . PHE D 4 48  ? 20.993 1.001   -46.648 1.00 28.41  ?  47  PHE D O   1 
ATOM   3518 C CB  . PHE D 4 48  ? 20.674 0.322   -43.636 1.00 31.86  ?  47  PHE D CB  1 
ATOM   3519 C CG  . PHE D 4 48  ? 20.172 1.707   -43.238 1.00 29.13  ?  47  PHE D CG  1 
ATOM   3520 C CD1 . PHE D 4 48  ? 18.957 1.865   -42.589 1.00 28.96  ?  47  PHE D CD1 1 
ATOM   3521 C CD2 . PHE D 4 48  ? 20.904 2.844   -43.555 1.00 33.36  ?  47  PHE D CD2 1 
ATOM   3522 C CE1 . PHE D 4 48  ? 18.497 3.150   -42.217 1.00 32.14  ?  47  PHE D CE1 1 
ATOM   3523 C CE2 . PHE D 4 48  ? 20.445 4.121   -43.193 1.00 35.07  ?  47  PHE D CE2 1 
ATOM   3524 C CZ  . PHE D 4 48  ? 19.243 4.266   -42.520 1.00 29.23  ?  47  PHE D CZ  1 
ATOM   3525 N N   . LEU D 4 49  ? 18.800 1.352   -46.276 1.00 34.14  ?  48  LEU D N   1 
ATOM   3526 C CA  . LEU D 4 49  ? 18.738 2.390   -47.311 1.00 32.20  ?  48  LEU D CA  1 
ATOM   3527 C C   . LEU D 4 49  ? 18.652 3.794   -46.731 1.00 29.67  ?  48  LEU D C   1 
ATOM   3528 O O   . LEU D 4 49  ? 19.464 4.651   -47.088 1.00 31.29  ?  48  LEU D O   1 
ATOM   3529 C CB  . LEU D 4 49  ? 17.544 2.174   -48.250 1.00 30.05  ?  48  LEU D CB  1 
ATOM   3530 C CG  . LEU D 4 49  ? 17.469 0.767   -48.838 1.00 33.18  ?  48  LEU D CG  1 
ATOM   3531 C CD1 . LEU D 4 49  ? 16.147 0.555   -49.583 1.00 31.79  ?  48  LEU D CD1 1 
ATOM   3532 C CD2 . LEU D 4 49  ? 18.683 0.498   -49.751 1.00 36.12  ?  48  LEU D CD2 1 
ATOM   3533 N N   . ILE D 4 50  ? 17.694 4.047   -45.841 1.00 30.03  ?  49  ILE D N   1 
ATOM   3534 C CA  . ILE D 4 50  ? 17.396 5.421   -45.437 1.00 33.61  ?  49  ILE D CA  1 
ATOM   3535 C C   . ILE D 4 50  ? 16.490 5.429   -44.214 1.00 31.20  ?  49  ILE D C   1 
ATOM   3536 O O   . ILE D 4 50  ? 15.720 4.484   -43.988 1.00 34.15  ?  49  ILE D O   1 
ATOM   3537 C CB  . ILE D 4 50  ? 16.753 6.193   -46.610 1.00 38.30  ?  49  ILE D CB  1 
ATOM   3538 C CG1 . ILE D 4 50  ? 16.788 7.707   -46.371 1.00 40.95  ?  49  ILE D CG1 1 
ATOM   3539 C CG2 . ILE D 4 50  ? 15.304 5.755   -46.816 1.00 36.17  ?  49  ILE D CG2 1 
ATOM   3540 C CD1 . ILE D 4 50  ? 16.327 8.510   -47.582 1.00 36.45  ?  49  ILE D CD1 1 
ATOM   3541 N N   . ARG D 4 51  ? 16.595 6.481   -43.394 1.00 31.44  ?  50  ARG D N   1 
ATOM   3542 C CA  . ARG D 4 51  ? 15.711 6.658   -42.250 1.00 32.45  ?  50  ARG D CA  1 
ATOM   3543 C C   . ARG D 4 51  ? 15.054 8.026   -42.327 1.00 29.89  ?  50  ARG D C   1 
ATOM   3544 O O   . ARG D 4 51  ? 15.661 9.013   -42.755 1.00 30.52  ?  50  ARG D O   1 
ATOM   3545 C CB  . ARG D 4 51  ? 16.457 6.549   -40.914 1.00 38.16  ?  50  ARG D CB  1 
ATOM   3546 C CG  . ARG D 4 51  ? 17.622 7.524   -40.876 1.00 42.02  ?  50  ARG D CG  1 
ATOM   3547 C CD  . ARG D 4 51  ? 18.009 7.879   -39.508 1.00 41.55  ?  50  ARG D CD  1 
ATOM   3548 N NE  . ARG D 4 51  ? 17.329 9.081   -39.066 1.00 54.34  ?  50  ARG D NE  1 
ATOM   3549 C CZ  . ARG D 4 51  ? 17.872 10.289  -39.110 1.00 48.45  ?  50  ARG D CZ  1 
ATOM   3550 N NH1 . ARG D 4 51  ? 17.195 11.353  -38.693 1.00 49.55  ?  50  ARG D NH1 1 
ATOM   3551 N NH2 . ARG D 4 51  ? 19.097 10.423  -39.578 1.00 51.06  ?  50  ARG D NH2 1 
ATOM   3552 N N   . GLN D 4 52  ? 13.824 8.071   -41.861 1.00 30.13  ?  51  GLN D N   1 
ATOM   3553 C CA  . GLN D 4 52  ? 13.007 9.271   -41.834 1.00 32.01  ?  51  GLN D CA  1 
ATOM   3554 C C   . GLN D 4 52  ? 12.752 9.627   -40.378 1.00 30.50  ?  51  GLN D C   1 
ATOM   3555 O O   . GLN D 4 52  ? 12.248 8.792   -39.615 1.00 30.97  ?  51  GLN D O   1 
ATOM   3556 C CB  . GLN D 4 52  ? 11.687 9.013   -42.558 1.00 30.32  ?  51  GLN D CB  1 
ATOM   3557 C CG  . GLN D 4 52  ? 10.630 10.060  -42.344 1.00 32.82  ?  51  GLN D CG  1 
ATOM   3558 C CD  . GLN D 4 52  ? 10.944 11.343  -43.073 1.00 36.34  ?  51  GLN D CD  1 
ATOM   3559 O OE1 . GLN D 4 52  ? 11.177 11.352  -44.291 1.00 33.27  ?  51  GLN D OE1 1 
ATOM   3560 N NE2 . GLN D 4 52  ? 10.960 12.451  -42.329 1.00 35.28  ?  51  GLN D NE2 1 
ATOM   3561 N N   . GLY D 4 53  ? 13.110 10.847  -39.989 1.00 33.67  ?  52  GLY D N   1 
ATOM   3562 C CA  . GLY D 4 53  ? 12.825 11.296  -38.626 1.00 32.41  ?  52  GLY D CA  1 
ATOM   3563 C C   . GLY D 4 53  ? 11.433 11.900  -38.513 1.00 29.44  ?  52  GLY D C   1 
ATOM   3564 O O   . GLY D 4 53  ? 10.955 12.595  -39.411 1.00 36.86  ?  52  GLY D O   1 
ATOM   3565 N N   . SER D 4 54  ? 10.781 11.627  -37.386 1.00 30.54  ?  53  SER D N   1 
ATOM   3566 C CA  . SER D 4 54  ? 9.412  12.074  -37.188 1.00 33.45  ?  53  SER D CA  1 
ATOM   3567 C C   . SER D 4 54  ? 9.297  13.592  -37.056 1.00 42.54  ?  53  SER D C   1 
ATOM   3568 O O   . SER D 4 54  ? 8.184  14.115  -37.169 1.00 36.06  ?  53  SER D O   1 
ATOM   3569 C CB  . SER D 4 54  ? 8.794  11.355  -35.978 1.00 34.77  ?  53  SER D CB  1 
ATOM   3570 O OG  . SER D 4 54  ? 9.252  11.833  -34.715 1.00 34.76  ?  53  SER D OG  1 
ATOM   3571 N N   . ASP D 4 55  ? 10.413 14.304  -36.867 1.00 37.69  ?  54  ASP D N   1 
ATOM   3572 C CA  . ASP D 4 55  ? 10.437 15.758  -36.768 1.00 42.38  ?  54  ASP D CA  1 
ATOM   3573 C C   . ASP D 4 55  ? 11.061 16.401  -37.984 1.00 40.75  ?  54  ASP D C   1 
ATOM   3574 O O   . ASP D 4 55  ? 11.258 17.616  -37.987 1.00 41.86  ?  54  ASP D O   1 
ATOM   3575 C CB  . ASP D 4 55  ? 11.208 16.215  -35.522 1.00 36.40  ?  54  ASP D CB  1 
ATOM   3576 C CG  . ASP D 4 55  ? 10.601 15.689  -34.273 1.00 43.97  ?  54  ASP D CG  1 
ATOM   3577 O OD1 . ASP D 4 55  ? 9.347  15.729  -34.222 1.00 46.91  ?  54  ASP D OD1 1 
ATOM   3578 O OD2 . ASP D 4 55  ? 11.346 15.208  -33.370 1.00 37.66  -1 54  ASP D OD2 1 
ATOM   3579 N N   . GLU D 4 56  ? 11.414 15.622  -38.999 1.00 34.06  ?  55  GLU D N   1 
ATOM   3580 C CA  . GLU D 4 56  ? 12.236 16.137  -40.078 1.00 38.29  ?  55  GLU D CA  1 
ATOM   3581 C C   . GLU D 4 56  ? 11.398 16.303  -41.336 1.00 38.36  ?  55  GLU D C   1 
ATOM   3582 O O   . GLU D 4 56  ? 10.270 15.813  -41.428 1.00 34.76  ?  55  GLU D O   1 
ATOM   3583 C CB  . GLU D 4 56  ? 13.435 15.211  -40.341 1.00 36.27  ?  55  GLU D CB  1 
ATOM   3584 C CG  . GLU D 4 56  ? 14.237 14.865  -39.073 1.00 40.64  ?  55  GLU D CG  1 
ATOM   3585 C CD  . GLU D 4 56  ? 15.331 13.817  -39.320 1.00 46.72  ?  55  GLU D CD  1 
ATOM   3586 O OE1 . GLU D 4 56  ? 15.303 13.139  -40.384 1.00 41.49  ?  55  GLU D OE1 1 
ATOM   3587 O OE2 . GLU D 4 56  ? 16.222 13.687  -38.439 1.00 45.56  -1 55  GLU D OE2 1 
ATOM   3588 N N   . GLN D 4 57  ? 11.972 17.016  -42.301 1.00 35.72  ?  56  GLN D N   1 
ATOM   3589 C CA  . GLN D 4 57  ? 11.379 17.095  -43.625 1.00 40.30  ?  56  GLN D CA  1 
ATOM   3590 C C   . GLN D 4 57  ? 11.564 15.754  -44.330 1.00 39.60  ?  56  GLN D C   1 
ATOM   3591 O O   . GLN D 4 57  ? 12.205 14.837  -43.815 1.00 35.20  ?  56  GLN D O   1 
ATOM   3592 C CB  . GLN D 4 57  ? 11.999 18.241  -44.425 1.00 41.85  ?  56  GLN D CB  1 
ATOM   3593 C CG  . GLN D 4 57  ? 11.592 19.641  -43.941 1.00 42.65  ?  56  GLN D CG  1 
ATOM   3594 C CD  . GLN D 4 57  ? 10.099 19.911  -44.128 1.00 55.50  ?  56  GLN D CD  1 
ATOM   3595 O OE1 . GLN D 4 57  ? 9.621  20.050  -45.254 1.00 60.12  ?  56  GLN D OE1 1 
ATOM   3596 N NE2 . GLN D 4 57  ? 9.356  19.977  -43.020 1.00 53.18  ?  56  GLN D NE2 1 
ATOM   3597 N N   . ASN D 4 58  ? 10.991 15.636  -45.523 1.00 41.03  ?  57  ASN D N   1 
ATOM   3598 C CA  . ASN D 4 58  ? 11.048 14.378  -46.259 1.00 36.46  ?  57  ASN D CA  1 
ATOM   3599 C C   . ASN D 4 58  ? 12.492 13.961  -46.510 1.00 32.53  ?  57  ASN D C   1 
ATOM   3600 O O   . ASN D 4 58  ? 13.259 14.706  -47.129 1.00 35.49  ?  57  ASN D O   1 
ATOM   3601 C CB  . ASN D 4 58  ? 10.282 14.523  -47.577 1.00 32.38  ?  57  ASN D CB  1 
ATOM   3602 C CG  . ASN D 4 58  ? 8.790  14.392  -47.382 1.00 32.06  ?  57  ASN D CG  1 
ATOM   3603 O OD1 . ASN D 4 58  ? 8.329  13.862  -46.365 1.00 34.01  ?  57  ASN D OD1 1 
ATOM   3604 N ND2 . ASN D 4 58  ? 8.018  14.872  -48.347 1.00 35.56  ?  57  ASN D ND2 1 
ATOM   3605 N N   . ALA D 4 59  ? 12.857 12.755  -46.051 1.00 32.65  ?  58  ALA D N   1 
ATOM   3606 C CA  . ALA D 4 59  ? 14.190 12.224  -46.309 1.00 35.05  ?  58  ALA D CA  1 
ATOM   3607 C C   . ALA D 4 59  ? 14.368 11.892  -47.780 1.00 37.21  ?  58  ALA D C   1 
ATOM   3608 O O   . ALA D 4 59  ? 13.449 11.420  -48.454 1.00 37.85  ?  58  ALA D O   1 
ATOM   3609 C CB  . ALA D 4 59  ? 14.467 10.960  -45.481 1.00 34.44  ?  58  ALA D CB  1 
ATOM   3610 N N   . LYS D 4 60  ? 15.583 12.117  -48.265 1.00 34.67  ?  59  LYS D N   1 
ATOM   3611 C CA  . LYS D 4 60  ? 15.929 11.897  -49.658 1.00 36.54  ?  59  LYS D CA  1 
ATOM   3612 C C   . LYS D 4 60  ? 17.391 11.505  -49.703 1.00 40.27  ?  59  LYS D C   1 
ATOM   3613 O O   . LYS D 4 60  ? 18.198 12.087  -48.970 1.00 34.69  ?  59  LYS D O   1 
ATOM   3614 C CB  . LYS D 4 60  ? 15.701 13.181  -50.479 1.00 42.68  ?  59  LYS D CB  1 
ATOM   3615 C CG  . LYS D 4 60  ? 15.702 13.039  -51.982 1.00 47.12  ?  59  LYS D CG  1 
ATOM   3616 C CD  . LYS D 4 60  ? 17.118 12.978  -52.551 1.00 54.47  ?  59  LYS D CD  1 
ATOM   3617 C CE  . LYS D 4 60  ? 17.115 13.048  -54.092 1.00 50.17  ?  59  LYS D CE  1 
ATOM   3618 N NZ  . LYS D 4 60  ? 18.468 13.349  -54.673 1.00 50.79  ?  59  LYS D NZ  1 
ATOM   3619 N N   . SER D 4 61  ? 17.733 10.543  -50.572 1.00 30.78  ?  60  SER D N   1 
ATOM   3620 C CA  . SER D 4 61  ? 19.133 10.180  -50.802 1.00 35.19  ?  60  SER D CA  1 
ATOM   3621 C C   . SER D 4 61  ? 19.274 9.422   -52.120 1.00 39.24  ?  60  SER D C   1 
ATOM   3622 O O   . SER D 4 61  ? 18.722 8.325   -52.274 1.00 41.14  ?  60  SER D O   1 
ATOM   3623 C CB  . SER D 4 61  ? 19.670 9.341   -49.634 1.00 41.46  ?  60  SER D CB  1 
ATOM   3624 O OG  . SER D 4 61  ? 20.973 8.840   -49.913 1.00 49.80  ?  60  SER D OG  1 
ATOM   3625 N N   . GLY D 4 62  ? 20.040 9.971   -53.051 1.00 40.97  ?  61  GLY D N   1 
ATOM   3626 C CA  . GLY D 4 62  ? 20.136 9.343   -54.360 1.00 45.83  ?  61  GLY D CA  1 
ATOM   3627 C C   . GLY D 4 62  ? 18.758 9.114   -54.956 1.00 45.58  ?  61  GLY D C   1 
ATOM   3628 O O   . GLY D 4 62  ? 17.893 10.004  -54.952 1.00 40.81  ?  61  GLY D O   1 
ATOM   3629 N N   . ARG D 4 63  ? 18.528 7.898   -55.450 1.00 42.01  ?  62  ARG D N   1 
ATOM   3630 C CA  . ARG D 4 63  ? 17.253 7.567   -56.064 1.00 38.31  ?  62  ARG D CA  1 
ATOM   3631 C C   . ARG D 4 63  ? 16.166 7.237   -55.053 1.00 37.68  ?  62  ARG D C   1 
ATOM   3632 O O   . ARG D 4 63  ? 15.059 6.864   -55.456 1.00 41.60  ?  62  ARG D O   1 
ATOM   3633 C CB  . ARG D 4 63  ? 17.431 6.401   -57.032 1.00 40.23  ?  62  ARG D CB  1 
ATOM   3634 C CG  . ARG D 4 63  ? 18.243 6.766   -58.246 1.00 35.56  ?  62  ARG D CG  1 
ATOM   3635 C CD  . ARG D 4 63  ? 18.444 5.546   -59.148 1.00 38.54  ?  62  ARG D CD  1 
ATOM   3636 N NE  . ARG D 4 63  ? 19.079 4.422   -58.454 1.00 35.49  ?  62  ARG D NE  1 
ATOM   3637 C CZ  . ARG D 4 63  ? 18.567 3.200   -58.400 1.00 33.19  ?  62  ARG D CZ  1 
ATOM   3638 N NH1 . ARG D 4 63  ? 17.402 2.940   -58.972 1.00 41.56  ?  62  ARG D NH1 1 
ATOM   3639 N NH2 . ARG D 4 63  ? 19.203 2.231   -57.752 1.00 34.94  ?  62  ARG D NH2 1 
ATOM   3640 N N   . TYR D 4 64  ? 16.435 7.352   -53.759 1.00 37.05  ?  63  TYR D N   1 
ATOM   3641 C CA  . TYR D 4 64  ? 15.430 7.073   -52.746 1.00 40.12  ?  63  TYR D CA  1 
ATOM   3642 C C   . TYR D 4 64  ? 14.867 8.386   -52.216 1.00 39.22  ?  63  TYR D C   1 
ATOM   3643 O O   . TYR D 4 64  ? 15.598 9.364   -52.046 1.00 37.87  ?  63  TYR D O   1 
ATOM   3644 C CB  . TYR D 4 64  ? 16.020 6.244   -51.591 1.00 36.78  ?  63  TYR D CB  1 
ATOM   3645 C CG  . TYR D 4 64  ? 16.747 4.983   -52.040 1.00 37.72  ?  63  TYR D CG  1 
ATOM   3646 C CD1 . TYR D 4 64  ? 16.041 3.875   -52.514 1.00 41.42  ?  63  TYR D CD1 1 
ATOM   3647 C CD2 . TYR D 4 64  ? 18.135 4.908   -52.002 1.00 42.16  ?  63  TYR D CD2 1 
ATOM   3648 C CE1 . TYR D 4 64  ? 16.706 2.712   -52.941 1.00 40.75  ?  63  TYR D CE1 1 
ATOM   3649 C CE2 . TYR D 4 64  ? 18.810 3.761   -52.413 1.00 42.74  ?  63  TYR D CE2 1 
ATOM   3650 C CZ  . TYR D 4 64  ? 18.093 2.669   -52.886 1.00 44.27  ?  63  TYR D CZ  1 
ATOM   3651 O OH  . TYR D 4 64  ? 18.776 1.551   -53.304 1.00 39.17  ?  63  TYR D OH  1 
ATOM   3652 N N   . SER D 4 65  ? 13.568 8.397   -51.940 1.00 37.98  ?  64  SER D N   1 
ATOM   3653 C CA  . SER D 4 65  ? 12.970 9.512   -51.227 1.00 37.71  ?  64  SER D CA  1 
ATOM   3654 C C   . SER D 4 65  ? 11.773 8.996   -50.447 1.00 39.01  ?  64  SER D C   1 
ATOM   3655 O O   . SER D 4 65  ? 11.143 8.007   -50.834 1.00 36.83  ?  64  SER D O   1 
ATOM   3656 C CB  . SER D 4 65  ? 12.578 10.647  -52.185 1.00 39.61  ?  64  SER D CB  1 
ATOM   3657 O OG  . SER D 4 65  ? 11.464 10.282  -52.961 1.00 42.78  ?  64  SER D OG  1 
ATOM   3658 N N   . VAL D 4 66  ? 11.486 9.649   -49.323 1.00 30.33  ?  65  VAL D N   1 
ATOM   3659 C CA  . VAL D 4 66  ? 10.378 9.271   -48.460 1.00 36.85  ?  65  VAL D CA  1 
ATOM   3660 C C   . VAL D 4 66  ? 9.322  10.364  -48.525 1.00 36.35  ?  65  VAL D C   1 
ATOM   3661 O O   . VAL D 4 66  ? 9.648  11.555  -48.510 1.00 39.19  ?  65  VAL D O   1 
ATOM   3662 C CB  . VAL D 4 66  ? 10.827 9.043   -47.002 1.00 34.28  ?  65  VAL D CB  1 
ATOM   3663 C CG1 . VAL D 4 66  ? 9.620  8.641   -46.136 1.00 35.74  ?  65  VAL D CG1 1 
ATOM   3664 C CG2 . VAL D 4 66  ? 11.920 7.984   -46.953 1.00 34.95  ?  65  VAL D CG2 1 
ATOM   3665 N N   . ASN D 4 67  ? 8.062  9.955   -48.592 1.00 36.16  ?  66  ASN D N   1 
ATOM   3666 C CA  . ASN D 4 67  ? 6.930  10.881  -48.564 1.00 39.43  ?  66  ASN D CA  1 
ATOM   3667 C C   . ASN D 4 67  ? 6.332  10.713  -47.181 1.00 35.05  ?  66  ASN D C   1 
ATOM   3668 O O   . ASN D 4 67  ? 5.430  9.904   -46.963 1.00 36.55  ?  66  ASN D O   1 
ATOM   3669 C CB  . ASN D 4 67  ? 5.925  10.600  -49.685 1.00 37.78  ?  66  ASN D CB  1 
ATOM   3670 C CG  . ASN D 4 67  ? 4.802  11.656  -49.755 1.00 43.24  ?  66  ASN D CG  1 
ATOM   3671 O OD1 . ASN D 4 67  ? 4.678  12.510  -48.876 1.00 37.40  ?  66  ASN D OD1 1 
ATOM   3672 N ND2 . ASN D 4 67  ? 3.984  11.588  -50.802 1.00 39.85  ?  66  ASN D ND2 1 
ATOM   3673 N N   . PHE D 4 68  ? 6.891  11.446  -46.220 1.00 37.53  ?  67  PHE D N   1 
ATOM   3674 C CA  . PHE D 4 68  ? 6.481  11.314  -44.832 1.00 36.29  ?  67  PHE D CA  1 
ATOM   3675 C C   . PHE D 4 68  ? 5.206  12.124  -44.618 1.00 34.23  ?  67  PHE D C   1 
ATOM   3676 O O   . PHE D 4 68  ? 5.215  13.347  -44.764 1.00 42.14  ?  67  PHE D O   1 
ATOM   3677 C CB  . PHE D 4 68  ? 7.606  11.778  -43.894 1.00 36.34  ?  67  PHE D CB  1 
ATOM   3678 C CG  . PHE D 4 68  ? 7.288  11.604  -42.429 1.00 36.23  ?  67  PHE D CG  1 
ATOM   3679 C CD1 . PHE D 4 68  ? 6.625  10.473  -41.983 1.00 34.63  ?  67  PHE D CD1 1 
ATOM   3680 C CD2 . PHE D 4 68  ? 7.647  12.580  -41.501 1.00 34.19  ?  67  PHE D CD2 1 
ATOM   3681 C CE1 . PHE D 4 68  ? 6.321  10.310  -40.633 1.00 38.08  ?  67  PHE D CE1 1 
ATOM   3682 C CE2 . PHE D 4 68  ? 7.350  12.432  -40.156 1.00 35.85  ?  67  PHE D CE2 1 
ATOM   3683 C CZ  . PHE D 4 68  ? 6.686  11.300  -39.716 1.00 34.56  ?  67  PHE D CZ  1 
ATOM   3684 N N   . LYS D 4 69  ? 4.113  11.443  -44.274 1.00 38.17  ?  68  LYS D N   1 
ATOM   3685 C CA  . LYS D 4 69  ? 2.810  12.064  -44.045 1.00 36.89  ?  68  LYS D CA  1 
ATOM   3686 C C   . LYS D 4 69  ? 2.396  11.710  -42.627 1.00 35.61  ?  68  LYS D C   1 
ATOM   3687 O O   . LYS D 4 69  ? 1.681  10.740  -42.372 1.00 35.67  ?  68  LYS D O   1 
ATOM   3688 C CB  . LYS D 4 69  ? 1.773  11.622  -45.085 1.00 40.85  ?  68  LYS D CB  1 
ATOM   3689 C CG  . LYS D 4 69  ? 2.131  12.092  -46.498 1.00 39.80  ?  68  LYS D CG  1 
ATOM   3690 C CD  . LYS D 4 69  ? 0.921  12.024  -47.431 1.00 45.08  ?  68  LYS D CD  1 
ATOM   3691 C CE  . LYS D 4 69  ? 1.114  11.051  -48.588 1.00 45.17  ?  68  LYS D CE  1 
ATOM   3692 N NZ  . LYS D 4 69  ? -0.170 10.839  -49.363 1.00 51.08  ?  68  LYS D NZ  1 
ATOM   3693 N N   . LYS D 4 70  ? 2.830  12.552  -41.696 1.00 38.31  ?  69  LYS D N   1 
ATOM   3694 C CA  . LYS D 4 70  ? 2.834  12.175  -40.296 1.00 37.10  ?  69  LYS D CA  1 
ATOM   3695 C C   . LYS D 4 70  ? 1.424  12.032  -39.744 1.00 37.91  ?  69  LYS D C   1 
ATOM   3696 O O   . LYS D 4 70  ? 1.153  11.115  -38.956 1.00 38.18  ?  69  LYS D O   1 
ATOM   3697 C CB  . LYS D 4 70  ? 3.641  13.209  -39.512 1.00 35.12  ?  69  LYS D CB  1 
ATOM   3698 C CG  . LYS D 4 70  ? 3.455  13.151  -38.031 1.00 41.47  ?  69  LYS D CG  1 
ATOM   3699 C CD  . LYS D 4 70  ? 4.216  14.304  -37.400 1.00 47.60  ?  69  LYS D CD  1 
ATOM   3700 C CE  . LYS D 4 70  ? 4.882  13.896  -36.101 1.00 43.66  ?  69  LYS D CE  1 
ATOM   3701 N NZ  . LYS D 4 70  ? 5.957  14.888  -35.825 1.00 47.99  ?  69  LYS D NZ  1 
ATOM   3702 N N   . ALA D 4 71  ? 0.515  12.936  -40.115 1.00 35.88  ?  70  ALA D N   1 
ATOM   3703 C CA  . ALA D 4 71  ? -0.841 12.833  -39.591 1.00 35.80  ?  70  ALA D CA  1 
ATOM   3704 C C   . ALA D 4 71  ? -1.494 11.535  -40.046 1.00 35.18  ?  70  ALA D C   1 
ATOM   3705 O O   . ALA D 4 71  ? -2.245 10.902  -39.290 1.00 42.41  ?  70  ALA D O   1 
ATOM   3706 C CB  . ALA D 4 71  ? -1.674 14.048  -40.027 1.00 38.16  ?  70  ALA D CB  1 
ATOM   3707 N N   . ALA D 4 72  ? -1.202 11.113  -41.271 1.00 36.17  ?  71  ALA D N   1 
ATOM   3708 C CA  . ALA D 4 72  ? -1.732 9.868   -41.807 1.00 40.64  ?  71  ALA D CA  1 
ATOM   3709 C C   . ALA D 4 72  ? -0.939 8.644   -41.354 1.00 46.07  ?  71  ALA D C   1 
ATOM   3710 O O   . ALA D 4 72  ? -1.368 7.508   -41.615 1.00 40.42  ?  71  ALA D O   1 
ATOM   3711 C CB  . ALA D 4 72  ? -1.755 9.952   -43.340 1.00 34.76  ?  71  ALA D CB  1 
ATOM   3712 N N   . LYS D 4 73  ? 0.189  8.837   -40.668 1.00 41.06  ?  72  LYS D N   1 
ATOM   3713 C CA  . LYS D 4 73  ? 1.099  7.732   -40.348 1.00 36.47  ?  72  LYS D CA  1 
ATOM   3714 C C   . LYS D 4 73  ? 1.309  6.858   -41.587 1.00 35.98  ?  72  LYS D C   1 
ATOM   3715 O O   . LYS D 4 73  ? 0.977  5.671   -41.632 1.00 32.12  ?  72  LYS D O   1 
ATOM   3716 C CB  . LYS D 4 73  ? 0.584  6.932   -39.154 1.00 32.86  ?  72  LYS D CB  1 
ATOM   3717 C CG  . LYS D 4 73  ? 0.760  7.684   -37.845 1.00 28.66  ?  72  LYS D CG  1 
ATOM   3718 C CD  . LYS D 4 73  ? 0.417  6.822   -36.636 1.00 39.45  ?  72  LYS D CD  1 
ATOM   3719 C CE  . LYS D 4 73  ? 0.634  7.614   -35.353 1.00 37.44  ?  72  LYS D CE  1 
ATOM   3720 N NZ  . LYS D 4 73  ? -0.532 8.479   -35.060 1.00 37.59  ?  72  LYS D NZ  1 
ATOM   3721 N N   . SER D 4 74  ? 1.850  7.522   -42.579 1.00 30.67  ?  73  SER D N   1 
ATOM   3722 C CA  . SER D 4 74  ? 2.177  6.943   -43.886 1.00 37.18  ?  73  SER D CA  1 
ATOM   3723 C C   . SER D 4 74  ? 3.512  7.466   -44.421 1.00 36.77  ?  73  SER D C   1 
ATOM   3724 O O   . SER D 4 74  ? 3.645  8.646   -44.590 1.00 33.67  ?  73  SER D O   1 
ATOM   3725 C CB  . SER D 4 74  ? 1.055  7.234   -44.855 1.00 36.96  ?  73  SER D CB  1 
ATOM   3726 O OG  . SER D 4 74  ? 1.468  7.122   -46.183 1.00 30.90  ?  73  SER D OG  1 
ATOM   3727 N N   . VAL D 4 75  ? 4.416  6.548   -44.746 1.00 34.16  ?  74  VAL D N   1 
ATOM   3728 C CA  . VAL D 4 75  ? 5.850  6.806   -45.030 1.00 33.77  ?  74  VAL D CA  1 
ATOM   3729 C C   . VAL D 4 75  ? 6.211  5.997   -46.263 1.00 36.55  ?  74  VAL D C   1 
ATOM   3730 O O   . VAL D 4 75  ? 7.091  5.186   -46.176 1.00 33.52  ?  74  VAL D O   1 
ATOM   3731 C CB  . VAL D 4 75  ? 6.720  6.299   -43.871 1.00 34.78  ?  74  VAL D CB  1 
ATOM   3732 C CG1 . VAL D 4 75  ? 7.750  7.262   -43.381 1.00 35.06  ?  74  VAL D CG1 1 
ATOM   3733 C CG2 . VAL D 4 75  ? 5.991  5.542   -42.807 1.00 34.55  ?  74  VAL D CG2 1 
ATOM   3734 N N   . ALA D 4 76  ? 5.586  6.269   -47.383 1.00 34.55  ?  75  ALA D N   1 
ATOM   3735 C CA  . ALA D 4 76  ? 5.924  5.541   -48.611 1.00 30.04  ?  75  ALA D CA  1 
ATOM   3736 C C   . ALA D 4 76  ? 7.333  5.857   -49.096 1.00 34.11  ?  75  ALA D C   1 
ATOM   3737 O O   . ALA D 4 76  ? 7.741  6.969   -49.035 1.00 34.40  ?  75  ALA D O   1 
ATOM   3738 C CB  . ALA D 4 76  ? 4.913  5.852   -49.667 1.00 31.54  ?  75  ALA D CB  1 
ATOM   3739 N N   . LEU D 4 77  ? 8.046  4.828   -49.513 1.00 34.64  ?  76  LEU D N   1 
ATOM   3740 C CA  . LEU D 4 77  ? 9.344  4.948   -50.167 1.00 28.40  ?  76  LEU D CA  1 
ATOM   3741 C C   . LEU D 4 77  ? 9.169  4.928   -51.682 1.00 32.28  ?  76  LEU D C   1 
ATOM   3742 O O   . LEU D 4 77  ? 8.495  4.044   -52.225 1.00 35.16  ?  76  LEU D O   1 
ATOM   3743 C CB  . LEU D 4 77  ? 10.247 3.784   -49.760 1.00 25.72  ?  76  LEU D CB  1 
ATOM   3744 C CG  . LEU D 4 77  ? 11.498 3.673   -50.625 1.00 30.65  ?  76  LEU D CG  1 
ATOM   3745 C CD1 . LEU D 4 77  ? 12.386 4.897   -50.443 1.00 34.96  ?  76  LEU D CD1 1 
ATOM   3746 C CD2 . LEU D 4 77  ? 12.286 2.342   -50.399 1.00 34.80  ?  76  LEU D CD2 1 
ATOM   3747 N N   . THR D 4 78  ? 9.819  5.856   -52.367 1.00 29.20  ?  77  THR D N   1 
ATOM   3748 C CA  . THR D 4 78  ? 9.776  5.913   -53.816 1.00 35.07  ?  77  THR D CA  1 
ATOM   3749 C C   . THR D 4 78  ? 11.187 5.740   -54.339 1.00 34.56  ?  77  THR D C   1 
ATOM   3750 O O   . THR D 4 78  ? 12.105 6.425   -53.881 1.00 36.32  ?  77  THR D O   1 
ATOM   3751 C CB  . THR D 4 78  ? 9.184  7.246   -54.290 1.00 36.91  ?  77  THR D CB  1 
ATOM   3752 O OG1 . THR D 4 78  ? 7.785  7.295   -53.952 1.00 35.17  ?  77  THR D OG1 1 
ATOM   3753 C CG2 . THR D 4 78  ? 9.400  7.425   -55.768 1.00 37.44  ?  77  THR D CG2 1 
ATOM   3754 N N   . ILE D 4 79  ? 11.355 4.803   -55.269 1.00 28.57  ?  78  ILE D N   1 
ATOM   3755 C CA  . ILE D 4 79  ? 12.605 4.593   -55.990 1.00 31.03  ?  78  ILE D CA  1 
ATOM   3756 C C   . ILE D 4 79  ? 12.414 5.048   -57.434 1.00 39.35  ?  78  ILE D C   1 
ATOM   3757 O O   . ILE D 4 79  ? 11.505 4.572   -58.126 1.00 36.99  ?  78  ILE D O   1 
ATOM   3758 C CB  . ILE D 4 79  ? 13.040 3.121   -55.958 1.00 31.87  ?  78  ILE D CB  1 
ATOM   3759 C CG1 . ILE D 4 79  ? 13.043 2.584   -54.521 1.00 33.62  ?  78  ILE D CG1 1 
ATOM   3760 C CG2 . ILE D 4 79  ? 14.394 2.986   -56.631 1.00 32.26  ?  78  ILE D CG2 1 
ATOM   3761 C CD1 . ILE D 4 79  ? 13.001 1.078   -54.404 1.00 32.51  ?  78  ILE D CD1 1 
ATOM   3762 N N   . SER D 4 80  ? 13.284 5.944   -57.884 1.00 33.71  ?  79  SER D N   1 
ATOM   3763 C CA  . SER D 4 80  ? 13.268 6.484   -59.236 1.00 42.82  ?  79  SER D CA  1 
ATOM   3764 C C   . SER D 4 80  ? 14.231 5.701   -60.126 1.00 43.83  ?  79  SER D C   1 
ATOM   3765 O O   . SER D 4 80  ? 15.132 5.010   -59.640 1.00 40.79  ?  79  SER D O   1 
ATOM   3766 C CB  . SER D 4 80  ? 13.649 7.975   -59.216 1.00 42.63  ?  79  SER D CB  1 
ATOM   3767 O OG  . SER D 4 80  ? 15.058 8.189   -59.211 1.00 44.88  ?  79  SER D OG  1 
ATOM   3768 N N   . ALA D 4 81  ? 14.034 5.829   -61.443 1.00 43.73  ?  80  ALA D N   1 
ATOM   3769 C CA  . ALA D 4 81  ? 14.955 5.299   -62.464 1.00 40.24  ?  80  ALA D CA  1 
ATOM   3770 C C   . ALA D 4 81  ? 15.333 3.840   -62.178 1.00 40.04  ?  80  ALA D C   1 
ATOM   3771 O O   . ALA D 4 81  ? 16.502 3.489   -62.034 1.00 38.98  ?  80  ALA D O   1 
ATOM   3772 C CB  . ALA D 4 81  ? 16.209 6.175   -62.577 1.00 39.84  ?  80  ALA D CB  1 
ATOM   3773 N N   . LEU D 4 82  ? 14.311 2.985   -62.130 1.00 36.92  ?  81  LEU D N   1 
ATOM   3774 C CA  . LEU D 4 82  ? 14.488 1.607   -61.697 1.00 40.22  ?  81  LEU D CA  1 
ATOM   3775 C C   . LEU D 4 82  ? 15.559 0.883   -62.504 1.00 43.38  ?  81  LEU D C   1 
ATOM   3776 O O   . LEU D 4 82  ? 15.629 1.001   -63.731 1.00 40.00  ?  81  LEU D O   1 
ATOM   3777 C CB  . LEU D 4 82  ? 13.167 0.856   -61.811 1.00 37.07  ?  81  LEU D CB  1 
ATOM   3778 C CG  . LEU D 4 82  ? 12.237 1.111   -60.640 1.00 39.74  ?  81  LEU D CG  1 
ATOM   3779 C CD1 . LEU D 4 82  ? 10.861 0.526   -60.925 1.00 42.63  ?  81  LEU D CD1 1 
ATOM   3780 C CD2 . LEU D 4 82  ? 12.827 0.527   -59.341 1.00 42.60  ?  81  LEU D CD2 1 
ATOM   3781 N N   . GLN D 4 83  ? 16.390 0.115   -61.797 1.00 39.66  ?  82  GLN D N   1 
ATOM   3782 C CA  . GLN D 4 83  ? 17.369 -0.767  -62.411 1.00 39.60  ?  82  GLN D CA  1 
ATOM   3783 C C   . GLN D 4 83  ? 17.034 -2.201  -62.032 1.00 33.80  ?  82  GLN D C   1 
ATOM   3784 O O   . GLN D 4 83  ? 16.305 -2.455  -61.067 1.00 38.05  ?  82  GLN D O   1 
ATOM   3785 C CB  . GLN D 4 83  ? 18.793 -0.418  -61.977 1.00 43.23  ?  82  GLN D CB  1 
ATOM   3786 C CG  . GLN D 4 83  ? 19.203 1.009   -62.255 1.00 42.97  ?  82  GLN D CG  1 
ATOM   3787 C CD  . GLN D 4 83  ? 20.459 1.403   -61.481 1.00 45.50  ?  82  GLN D CD  1 
ATOM   3788 O OE1 . GLN D 4 83  ? 21.294 0.560   -61.175 1.00 45.47  ?  82  GLN D OE1 1 
ATOM   3789 N NE2 . GLN D 4 83  ? 20.595 2.686   -61.175 1.00 45.71  ?  82  GLN D NE2 1 
ATOM   3790 N N   . LEU D 4 84  ? 17.537 -3.149  -62.820 1.00 35.67  ?  83  LEU D N   1 
ATOM   3791 C CA  . LEU D 4 84  ? 17.249 -4.542  -62.502 1.00 40.19  ?  83  LEU D CA  1 
ATOM   3792 C C   . LEU D 4 84  ? 17.789 -4.906  -61.123 1.00 34.92  ?  83  LEU D C   1 
ATOM   3793 O O   . LEU D 4 84  ? 17.177 -5.706  -60.412 1.00 41.49  ?  83  LEU D O   1 
ATOM   3794 C CB  . LEU D 4 84  ? 17.822 -5.473  -63.577 1.00 40.48  ?  83  LEU D CB  1 
ATOM   3795 C CG  . LEU D 4 84  ? 17.065 -5.557  -64.914 1.00 43.04  ?  83  LEU D CG  1 
ATOM   3796 C CD1 . LEU D 4 84  ? 17.669 -6.646  -65.790 1.00 40.05  ?  83  LEU D CD1 1 
ATOM   3797 C CD2 . LEU D 4 84  ? 15.574 -5.783  -64.717 1.00 35.13  ?  83  LEU D CD2 1 
ATOM   3798 N N   . GLU D 4 85  ? 18.911 -4.300  -60.725 1.00 39.69  ?  84  GLU D N   1 
ATOM   3799 C CA  . GLU D 4 85  ? 19.503 -4.508  -59.406 1.00 40.59  ?  84  GLU D CA  1 
ATOM   3800 C C   . GLU D 4 85  ? 18.573 -4.093  -58.270 1.00 41.04  ?  84  GLU D C   1 
ATOM   3801 O O   . GLU D 4 85  ? 18.808 -4.480  -57.126 1.00 39.06  ?  84  GLU D O   1 
ATOM   3802 C CB  . GLU D 4 85  ? 20.820 -3.734  -59.306 1.00 46.24  ?  84  GLU D CB  1 
ATOM   3803 C CG  . GLU D 4 85  ? 21.933 -4.235  -60.238 1.00 54.39  ?  84  GLU D CG  1 
ATOM   3804 C CD  . GLU D 4 85  ? 21.758 -3.822  -61.711 1.00 58.60  ?  84  GLU D CD  1 
ATOM   3805 O OE1 . GLU D 4 85  ? 20.609 -3.552  -62.144 1.00 47.19  ?  84  GLU D OE1 1 
ATOM   3806 O OE2 . GLU D 4 85  ? 22.788 -3.769  -62.433 1.00 66.25  -1 84  GLU D OE2 1 
ATOM   3807 N N   . ASP D 4 86  ? 17.526 -3.313  -58.543 1.00 40.09  ?  85  ASP D N   1 
ATOM   3808 C CA  . ASP D 4 86  ? 16.598 -2.970  -57.473 1.00 37.21  ?  85  ASP D CA  1 
ATOM   3809 C C   . ASP D 4 86  ? 15.628 -4.090  -57.130 1.00 35.75  ?  85  ASP D C   1 
ATOM   3810 O O   . ASP D 4 86  ? 14.943 -3.988  -56.106 1.00 36.92  ?  85  ASP D O   1 
ATOM   3811 C CB  . ASP D 4 86  ? 15.814 -1.709  -57.830 1.00 34.56  ?  85  ASP D CB  1 
ATOM   3812 C CG  . ASP D 4 86  ? 16.710 -0.520  -58.013 1.00 37.01  ?  85  ASP D CG  1 
ATOM   3813 O OD1 . ASP D 4 86  ? 17.667 -0.366  -57.228 1.00 45.76  ?  85  ASP D OD1 1 
ATOM   3814 O OD2 . ASP D 4 86  ? 16.490 0.245   -58.959 1.00 39.63  -1 85  ASP D OD2 1 
ATOM   3815 N N   . SER D 4 87  ? 15.538 -5.156  -57.934 1.00 35.87  ?  86  SER D N   1 
ATOM   3816 C CA  . SER D 4 87  ? 14.645 -6.253  -57.561 1.00 39.07  ?  86  SER D CA  1 
ATOM   3817 C C   . SER D 4 87  ? 15.122 -6.884  -56.253 1.00 36.30  ?  86  SER D C   1 
ATOM   3818 O O   . SER D 4 87  ? 16.244 -7.388  -56.176 1.00 33.32  ?  86  SER D O   1 
ATOM   3819 C CB  . SER D 4 87  ? 14.571 -7.307  -58.680 1.00 39.56  ?  86  SER D CB  1 
ATOM   3820 O OG  . SER D 4 87  ? 14.221 -6.747  -59.960 1.00 36.01  ?  86  SER D OG  1 
ATOM   3821 N N   . ALA D 4 88  ? 14.248 -6.891  -55.245 1.00 31.40  ?  87  ALA D N   1 
ATOM   3822 C CA  . ALA D 4 88  ? 14.605 -7.217  -53.868 1.00 31.51  ?  87  ALA D CA  1 
ATOM   3823 C C   . ALA D 4 88  ? 13.332 -7.115  -53.048 1.00 35.45  ?  87  ALA D C   1 
ATOM   3824 O O   . ALA D 4 88  ? 12.286 -6.679  -53.543 1.00 33.95  ?  87  ALA D O   1 
ATOM   3825 C CB  . ALA D 4 88  ? 15.682 -6.278  -53.316 1.00 34.40  ?  87  ALA D CB  1 
ATOM   3826 N N   . LYS D 4 89  ? 13.413 -7.543  -51.798 1.00 31.76  ?  88  LYS D N   1 
ATOM   3827 C CA  . LYS D 4 89  ? 12.293 -7.355  -50.896 1.00 28.14  ?  88  LYS D CA  1 
ATOM   3828 C C   . LYS D 4 89  ? 12.605 -6.170  -49.978 1.00 35.71  ?  88  LYS D C   1 
ATOM   3829 O O   . LYS D 4 89  ? 13.707 -6.070  -49.410 1.00 34.98  ?  88  LYS D O   1 
ATOM   3830 C CB  . LYS D 4 89  ? 11.972 -8.631  -50.119 1.00 27.13  ?  88  LYS D CB  1 
ATOM   3831 C CG  . LYS D 4 89  ? 10.615 -8.558  -49.430 1.00 30.76  ?  88  LYS D CG  1 
ATOM   3832 C CD  . LYS D 4 89  ? 10.164 -9.897  -48.868 1.00 34.22  ?  88  LYS D CD  1 
ATOM   3833 C CE  . LYS D 4 89  ? 8.879  -9.763  -48.042 1.00 33.12  ?  88  LYS D CE  1 
ATOM   3834 N NZ  . LYS D 4 89  ? 8.417  -11.043 -47.435 1.00 32.40  ?  88  LYS D NZ  1 
ATOM   3835 N N   . TYR D 4 90  ? 11.647 -5.260  -49.862 1.00 30.78  ?  89  TYR D N   1 
ATOM   3836 C CA  . TYR D 4 90  ? 11.847 -3.976  -49.202 1.00 29.42  ?  89  TYR D CA  1 
ATOM   3837 C C   . TYR D 4 90  ? 11.030 -3.957  -47.927 1.00 30.89  ?  89  TYR D C   1 
ATOM   3838 O O   . TYR D 4 90  ? 9.849  -4.336  -47.928 1.00 31.92  ?  89  TYR D O   1 
ATOM   3839 C CB  . TYR D 4 90  ? 11.446 -2.805  -50.111 1.00 29.53  ?  89  TYR D CB  1 
ATOM   3840 C CG  . TYR D 4 90  ? 12.438 -2.563  -51.233 1.00 29.82  ?  89  TYR D CG  1 
ATOM   3841 C CD1 . TYR D 4 90  ? 12.392 -3.328  -52.401 1.00 33.10  ?  89  TYR D CD1 1 
ATOM   3842 C CD2 . TYR D 4 90  ? 13.427 -1.592  -51.129 1.00 25.06  ?  89  TYR D CD2 1 
ATOM   3843 C CE1 . TYR D 4 90  ? 13.293 -3.131  -53.420 1.00 26.69  ?  89  TYR D CE1 1 
ATOM   3844 C CE2 . TYR D 4 90  ? 14.354 -1.393  -52.169 1.00 30.17  ?  89  TYR D CE2 1 
ATOM   3845 C CZ  . TYR D 4 90  ? 14.266 -2.177  -53.317 1.00 31.07  ?  89  TYR D CZ  1 
ATOM   3846 O OH  . TYR D 4 90  ? 15.162 -1.997  -54.366 1.00 30.75  ?  89  TYR D OH  1 
ATOM   3847 N N   . PHE D 4 91  ? 11.664 -3.541  -46.840 1.00 28.72  ?  90  PHE D N   1 
ATOM   3848 C CA  . PHE D 4 91  ? 11.057 -3.618  -45.528 1.00 28.58  ?  90  PHE D CA  1 
ATOM   3849 C C   . PHE D 4 91  ? 10.979 -2.216  -44.948 1.00 28.72  ?  90  PHE D C   1 
ATOM   3850 O O   . PHE D 4 91  ? 11.919 -1.418  -45.086 1.00 30.91  ?  90  PHE D O   1 
ATOM   3851 C CB  . PHE D 4 91  ? 11.866 -4.539  -44.579 1.00 30.34  ?  90  PHE D CB  1 
ATOM   3852 C CG  . PHE D 4 91  ? 11.783 -6.007  -44.917 1.00 28.69  ?  90  PHE D CG  1 
ATOM   3853 C CD1 . PHE D 4 91  ? 10.745 -6.786  -44.432 1.00 26.46  ?  90  PHE D CD1 1 
ATOM   3854 C CD2 . PHE D 4 91  ? 12.759 -6.610  -45.702 1.00 31.58  ?  90  PHE D CD2 1 
ATOM   3855 C CE1 . PHE D 4 91  ? 10.669 -8.148  -44.717 1.00 25.90  ?  90  PHE D CE1 1 
ATOM   3856 C CE2 . PHE D 4 91  ? 12.685 -7.980  -46.010 1.00 26.91  ?  90  PHE D CE2 1 
ATOM   3857 C CZ  . PHE D 4 91  ? 11.643 -8.745  -45.509 1.00 23.24  ?  90  PHE D CZ  1 
ATOM   3858 N N   . CYS D 4 92  ? 9.847  -1.947  -44.307 1.00 32.04  ?  91  CYS D N   1 
ATOM   3859 C CA  . CYS D 4 92  ? 9.548  -0.720  -43.600 1.00 33.67  ?  91  CYS D CA  1 
ATOM   3860 C C   . CYS D 4 92  ? 9.589  -1.051  -42.103 1.00 27.52  ?  91  CYS D C   1 
ATOM   3861 O O   . CYS D 4 92  ? 9.115  -2.122  -41.691 1.00 33.09  ?  91  CYS D O   1 
ATOM   3862 C CB  . CYS D 4 92  ? 8.184  -0.177  -44.071 1.00 32.04  ?  91  CYS D CB  1 
ATOM   3863 S SG  . CYS D 4 92  ? 7.796  1.432   -43.247 1.00 36.56  ?  91  CYS D SG  1 
ATOM   3864 N N   . ALA D 4 93  ? 10.233 -0.184  -41.297 1.00 31.09  ?  92  ALA D N   1 
ATOM   3865 C CA  . ALA D 4 93  ? 10.452 -0.431  -39.872 1.00 29.07  ?  92  ALA D CA  1 
ATOM   3866 C C   . ALA D 4 93  ? 10.389 0.886   -39.102 1.00 30.11  ?  92  ALA D C   1 
ATOM   3867 O O   . ALA D 4 93  ? 10.802 1.940   -39.591 1.00 30.24  ?  92  ALA D O   1 
ATOM   3868 C CB  . ALA D 4 93  ? 11.797 -1.130  -39.624 1.00 28.40  ?  92  ALA D CB  1 
ATOM   3869 N N   . LEU D 4 94  ? 9.878  0.787   -37.885 1.00 26.34  ?  93  LEU D N   1 
ATOM   3870 C CA  . LEU D 4 94  ? 9.700  1.880   -36.947 1.00 34.81  ?  93  LEU D CA  1 
ATOM   3871 C C   . LEU D 4 94  ? 10.655 1.685   -35.772 1.00 33.51  ?  93  LEU D C   1 
ATOM   3872 O O   . LEU D 4 94  ? 10.815 0.559   -35.284 1.00 33.71  ?  93  LEU D O   1 
ATOM   3873 C CB  . LEU D 4 94  ? 8.255  1.863   -36.471 1.00 31.91  ?  93  LEU D CB  1 
ATOM   3874 C CG  . LEU D 4 94  ? 7.531  2.892   -35.635 1.00 36.77  ?  93  LEU D CG  1 
ATOM   3875 C CD1 . LEU D 4 94  ? 7.622  4.282   -36.249 1.00 36.49  ?  93  LEU D CD1 1 
ATOM   3876 C CD2 . LEU D 4 94  ? 6.092  2.429   -35.553 1.00 35.64  ?  93  LEU D CD2 1 
ATOM   3877 N N   . GLY D 4 95  ? 11.293 2.762   -35.325 1.00 29.10  ?  94  GLY D N   1 
ATOM   3878 C CA  . GLY D 4 95  ? 12.162 2.687   -34.154 1.00 37.84  ?  94  GLY D CA  1 
ATOM   3879 C C   . GLY D 4 95  ? 11.928 3.840   -33.194 1.00 36.24  ?  94  GLY D C   1 
ATOM   3880 O O   . GLY D 4 95  ? 11.529 4.933   -33.596 1.00 29.02  ?  94  GLY D O   1 
ATOM   3881 N N   . ASP D 4 96  ? 12.206 3.596   -31.907 1.00 29.40  ?  95  ASP D N   1 
ATOM   3882 C CA  . ASP D 4 96  ? 11.955 4.615   -30.890 1.00 30.51  ?  95  ASP D CA  1 
ATOM   3883 C C   . ASP D 4 96  ? 13.227 5.434   -30.626 1.00 30.69  ?  95  ASP D C   1 
ATOM   3884 O O   . ASP D 4 96  ? 14.132 5.484   -31.464 1.00 25.74  ?  95  ASP D O   1 
ATOM   3885 C CB  . ASP D 4 96  ? 11.363 3.956   -29.638 1.00 27.54  ?  95  ASP D CB  1 
ATOM   3886 C CG  . ASP D 4 96  ? 12.396 3.118   -28.835 1.00 26.70  ?  95  ASP D CG  1 
ATOM   3887 O OD1 . ASP D 4 96  ? 13.561 2.982   -29.226 1.00 26.79  ?  95  ASP D OD1 1 
ATOM   3888 O OD2 . ASP D 4 96  ? 12.004 2.603   -27.788 1.00 31.54  -1 95  ASP D OD2 1 
ATOM   3889 N N   . THR D 4 97  ? 13.309 6.153   -29.500 1.00 28.81  ?  96  THR D N   1 
ATOM   3890 C CA  . THR D 4 97  ? 14.498 6.960   -29.226 1.00 28.71  ?  96  THR D CA  1 
ATOM   3891 C C   . THR D 4 97  ? 15.588 6.166   -28.512 1.00 28.11  ?  96  THR D C   1 
ATOM   3892 O O   . THR D 4 97  ? 16.603 6.745   -28.093 1.00 29.61  ?  96  THR D O   1 
ATOM   3893 C CB  . THR D 4 97  ? 14.144 8.190   -28.368 1.00 26.11  ?  96  THR D CB  1 
ATOM   3894 O OG1 . THR D 4 97  ? 13.768 7.717   -27.082 1.00 23.73  ?  96  THR D OG1 1 
ATOM   3895 C CG2 . THR D 4 97  ? 12.964 8.985   -28.986 1.00 26.42  ?  96  THR D CG2 1 
ATOM   3896 N N   . ALA D 4 98  ? 15.397 4.863   -28.332 1.00 27.37  ?  97  ALA D N   1 
ATOM   3897 C CA  . ALA D 4 98  ? 16.350 4.097   -27.548 1.00 30.58  ?  97  ALA D CA  1 
ATOM   3898 C C   . ALA D 4 98  ? 16.534 2.685   -28.113 1.00 33.29  ?  97  ALA D C   1 
ATOM   3899 O O   . ALA D 4 98  ? 16.621 1.712   -27.361 1.00 33.87  ?  97  ALA D O   1 
ATOM   3900 C CB  . ALA D 4 98  ? 15.924 4.046   -26.073 1.00 25.58  ?  97  ALA D CB  1 
ATOM   3901 N N   . GLY D 4 99  ? 16.607 2.550   -29.445 1.00 32.32  ?  98  GLY D N   1 
ATOM   3902 C CA  . GLY D 4 99  ? 17.091 1.323   -30.061 1.00 29.35  ?  98  GLY D CA  1 
ATOM   3903 C C   . GLY D 4 99  ? 16.058 0.236   -30.310 1.00 28.80  ?  98  GLY D C   1 
ATOM   3904 O O   . GLY D 4 99  ? 16.392 -0.777  -30.958 1.00 26.19  ?  98  GLY D O   1 
ATOM   3905 N N   . LYS D 4 100 ? 14.826 0.392   -29.819 1.00 24.60  ?  99  LYS D N   1 
ATOM   3906 C CA  . LYS D 4 100 ? 13.786 -0.593  -30.103 1.00 26.08  ?  99  LYS D CA  1 
ATOM   3907 C C   . LYS D 4 100 ? 13.273 -0.447  -31.532 1.00 31.79  ?  99  LYS D C   1 
ATOM   3908 O O   . LYS D 4 100 ? 13.296 0.645   -32.113 1.00 30.90  ?  99  LYS D O   1 
ATOM   3909 C CB  . LYS D 4 100 ? 12.624 -0.460  -29.129 1.00 27.59  ?  99  LYS D CB  1 
ATOM   3910 C CG  . LYS D 4 100 ? 11.948 -1.775  -28.840 1.00 31.03  ?  99  LYS D CG  1 
ATOM   3911 C CD  . LYS D 4 100 ? 10.935 -1.631  -27.732 1.00 33.98  ?  99  LYS D CD  1 
ATOM   3912 C CE  . LYS D 4 100 ? 9.877  -2.718  -27.824 1.00 43.25  ?  99  LYS D CE  1 
ATOM   3913 N NZ  . LYS D 4 100 ? 10.043 -3.705  -26.686 1.00 51.45  ?  99  LYS D NZ  1 
ATOM   3914 N N   . SER D 4 101 ? 12.830 -1.562  -32.117 1.00 26.46  ?  100 SER D N   1 
ATOM   3915 C CA  . SER D 4 101 ? 12.307 -1.453  -33.477 1.00 34.82  ?  100 SER D CA  1 
ATOM   3916 C C   . SER D 4 101 ? 11.218 -2.479  -33.746 1.00 31.62  ?  100 SER D C   1 
ATOM   3917 O O   . SER D 4 101 ? 11.124 -3.528  -33.098 1.00 30.73  ?  100 SER D O   1 
ATOM   3918 C CB  . SER D 4 101 ? 13.400 -1.585  -34.536 1.00 33.33  ?  100 SER D CB  1 
ATOM   3919 O OG  . SER D 4 101 ? 13.593 -2.938  -34.873 1.00 37.78  ?  100 SER D OG  1 
ATOM   3920 N N   . THR D 4 102 ? 10.389 -2.127  -34.720 1.00 30.28  ?  101 THR D N   1 
ATOM   3921 C CA  . THR D 4 102 ? 9.224  -2.889  -35.149 1.00 29.00  ?  101 THR D CA  1 
ATOM   3922 C C   . THR D 4 102 ? 9.290  -2.979  -36.672 1.00 31.61  ?  101 THR D C   1 
ATOM   3923 O O   . THR D 4 102 ? 9.423  -1.957  -37.340 1.00 32.80  ?  101 THR D O   1 
ATOM   3924 C CB  . THR D 4 102 ? 7.902  -2.206  -34.710 1.00 38.06  ?  101 THR D CB  1 
ATOM   3925 O OG1 . THR D 4 102 ? 7.888  -2.008  -33.292 1.00 31.91  ?  101 THR D OG1 1 
ATOM   3926 C CG2 . THR D 4 102 ? 6.690  -3.078  -35.031 1.00 37.76  ?  101 THR D CG2 1 
ATOM   3927 N N   . PHE D 4 103 ? 9.235  -4.195  -37.217 1.00 31.66  ?  102 PHE D N   1 
ATOM   3928 C CA  . PHE D 4 103 ? 9.332  -4.361  -38.668 1.00 31.86  ?  102 PHE D CA  1 
ATOM   3929 C C   . PHE D 4 103 ? 7.967  -4.672  -39.271 1.00 26.62  ?  102 PHE D C   1 
ATOM   3930 O O   . PHE D 4 103 ? 7.177  -5.436  -38.699 1.00 29.22  ?  102 PHE D O   1 
ATOM   3931 C CB  . PHE D 4 103 ? 10.294 -5.497  -39.057 1.00 28.18  ?  102 PHE D CB  1 
ATOM   3932 C CG  . PHE D 4 103 ? 11.693 -5.051  -39.408 1.00 28.80  ?  102 PHE D CG  1 
ATOM   3933 C CD1 . PHE D 4 103 ? 12.533 -4.537  -38.420 1.00 26.60  ?  102 PHE D CD1 1 
ATOM   3934 C CD2 . PHE D 4 103 ? 12.198 -5.209  -40.710 1.00 26.56  ?  102 PHE D CD2 1 
ATOM   3935 C CE1 . PHE D 4 103 ? 13.830 -4.155  -38.724 1.00 28.26  ?  102 PHE D CE1 1 
ATOM   3936 C CE2 . PHE D 4 103 ? 13.505 -4.828  -41.024 1.00 30.25  ?  102 PHE D CE2 1 
ATOM   3937 C CZ  . PHE D 4 103 ? 14.326 -4.300  -40.029 1.00 31.69  ?  102 PHE D CZ  1 
ATOM   3938 N N   . GLY D 4 104 ? 7.716  -4.107  -40.445 1.00 28.62  ?  103 GLY D N   1 
ATOM   3939 C CA  . GLY D 4 104 ? 6.641  -4.616  -41.274 1.00 31.34  ?  103 GLY D CA  1 
ATOM   3940 C C   . GLY D 4 104 ? 7.104  -5.892  -41.944 1.00 35.21  ?  103 GLY D C   1 
ATOM   3941 O O   . GLY D 4 104 ? 8.272  -6.278  -41.814 1.00 34.39  ?  103 GLY D O   1 
ATOM   3942 N N   . ASP D 4 105 ? 6.197  -6.546  -42.673 1.00 35.59  ?  104 ASP D N   1 
ATOM   3943 C CA  . ASP D 4 105 ? 6.512  -7.839  -43.270 1.00 28.63  ?  104 ASP D CA  1 
ATOM   3944 C C   . ASP D 4 105 ? 6.959  -7.727  -44.724 1.00 30.79  ?  104 ASP D C   1 
ATOM   3945 O O   . ASP D 4 105 ? 7.171  -8.751  -45.378 1.00 33.53  ?  104 ASP D O   1 
ATOM   3946 C CB  . ASP D 4 105 ? 5.329  -8.794  -43.104 1.00 30.85  ?  104 ASP D CB  1 
ATOM   3947 C CG  . ASP D 4 105 ? 5.234  -9.345  -41.682 1.00 37.81  ?  104 ASP D CG  1 
ATOM   3948 O OD1 . ASP D 4 105 ? 6.281  -9.418  -40.979 1.00 41.25  ?  104 ASP D OD1 1 
ATOM   3949 O OD2 . ASP D 4 105 ? 4.126  -9.715  -41.246 1.00 42.98  -1 104 ASP D OD2 1 
ATOM   3950 N N   . GLY D 4 106 ? 7.164  -6.514  -45.229 1.00 26.09  ?  105 GLY D N   1 
ATOM   3951 C CA  . GLY D 4 106 ? 7.910  -6.313  -46.455 1.00 30.41  ?  105 GLY D CA  1 
ATOM   3952 C C   . GLY D 4 106 ? 7.075  -6.411  -47.741 1.00 33.31  ?  105 GLY D C   1 
ATOM   3953 O O   . GLY D 4 106 ? 5.941  -6.896  -47.762 1.00 32.08  ?  105 GLY D O   1 
ATOM   3954 N N   . THR D 4 107 ? 7.683  -5.941  -48.830 1.00 33.66  ?  106 THR D N   1 
ATOM   3955 C CA  . THR D 4 107 ? 7.070  -5.894  -50.161 1.00 36.56  ?  106 THR D CA  1 
ATOM   3956 C C   . THR D 4 107 ? 8.099  -6.329  -51.188 1.00 32.61  ?  106 THR D C   1 
ATOM   3957 O O   . THR D 4 107 ? 9.171  -5.715  -51.277 1.00 32.68  ?  106 THR D O   1 
ATOM   3958 C CB  . THR D 4 107 ? 6.579  -4.483  -50.545 1.00 34.11  ?  106 THR D CB  1 
ATOM   3959 O OG1 . THR D 4 107 ? 5.492  -4.086  -49.699 1.00 34.38  ?  106 THR D OG1 1 
ATOM   3960 C CG2 . THR D 4 107 ? 6.120  -4.509  -51.995 1.00 35.26  ?  106 THR D CG2 1 
ATOM   3961 N N   . THR D 4 108 ? 7.773  -7.352  -51.987 1.00 34.55  ?  107 THR D N   1 
ATOM   3962 C CA  . THR D 4 108 ? 8.712  -7.866  -52.978 1.00 26.49  ?  107 THR D CA  1 
ATOM   3963 C C   . THR D 4 108 ? 8.562  -7.059  -54.255 1.00 30.75  ?  107 THR D C   1 
ATOM   3964 O O   . THR D 4 108 ? 7.456  -6.940  -54.790 1.00 32.09  ?  107 THR D O   1 
ATOM   3965 C CB  . THR D 4 108 ? 8.493  -9.353  -53.259 1.00 36.65  ?  107 THR D CB  1 
ATOM   3966 O OG1 . THR D 4 108 ? 8.738  -10.114 -52.067 1.00 32.35  ?  107 THR D OG1 1 
ATOM   3967 C CG2 . THR D 4 108 ? 9.454  -9.828  -54.373 1.00 28.00  ?  107 THR D CG2 1 
ATOM   3968 N N   . LEU D 4 109 ? 9.668  -6.494  -54.724 1.00 32.59  ?  108 LEU D N   1 
ATOM   3969 C CA  . LEU D 4 109 ? 9.716  -5.691  -55.933 1.00 30.10  ?  108 LEU D CA  1 
ATOM   3970 C C   . LEU D 4 109 ? 10.443 -6.459  -57.028 1.00 40.88  ?  108 LEU D C   1 
ATOM   3971 O O   . LEU D 4 109 ? 11.642 -6.757  -56.888 1.00 34.41  ?  108 LEU D O   1 
ATOM   3972 C CB  . LEU D 4 109 ? 10.439 -4.367  -55.695 1.00 36.12  ?  108 LEU D CB  1 
ATOM   3973 C CG  . LEU D 4 109 ? 10.746 -3.666  -57.022 1.00 33.89  ?  108 LEU D CG  1 
ATOM   3974 C CD1 . LEU D 4 109 ? 9.450  -3.050  -57.540 1.00 37.70  ?  108 LEU D CD1 1 
ATOM   3975 C CD2 . LEU D 4 109 ? 11.836 -2.606  -56.932 1.00 29.69  ?  108 LEU D CD2 1 
ATOM   3976 N N   . THR D 4 110 ? 9.741  -6.715  -58.139 1.00 34.62  ?  109 THR D N   1 
ATOM   3977 C CA  . THR D 4 110 ? 10.344 -7.277  -59.347 1.00 39.21  ?  109 THR D CA  1 
ATOM   3978 C C   . THR D 4 110 ? 10.417 -6.201  -60.429 1.00 36.94  ?  109 THR D C   1 
ATOM   3979 O O   . THR D 4 110 ? 9.390  -5.677  -60.871 1.00 35.58  ?  109 THR D O   1 
ATOM   3980 C CB  . THR D 4 110 ? 9.557  -8.492  -59.847 1.00 37.48  ?  109 THR D CB  1 
ATOM   3981 O OG1 . THR D 4 110 ? 9.089  -9.262  -58.729 1.00 42.36  ?  109 THR D OG1 1 
ATOM   3982 C CG2 . THR D 4 110 ? 10.434 -9.371  -60.720 1.00 42.13  ?  109 THR D CG2 1 
ATOM   3983 N N   . VAL D 4 111 ? 11.623 -5.849  -60.824 1.00 33.70  ?  110 VAL D N   1 
ATOM   3984 C CA  . VAL D 4 111 ? 11.840 -4.956  -61.948 1.00 34.10  ?  110 VAL D CA  1 
ATOM   3985 C C   . VAL D 4 111 ? 11.917 -5.826  -63.194 1.00 41.62  ?  110 VAL D C   1 
ATOM   3986 O O   . VAL D 4 111 ? 12.733 -6.749  -63.253 1.00 37.96  ?  110 VAL D O   1 
ATOM   3987 C CB  . VAL D 4 111 ? 13.127 -4.146  -61.765 1.00 33.10  ?  110 VAL D CB  1 
ATOM   3988 C CG1 . VAL D 4 111 ? 13.305 -3.092  -62.892 1.00 36.02  ?  110 VAL D CG1 1 
ATOM   3989 C CG2 . VAL D 4 111 ? 13.152 -3.491  -60.365 1.00 37.27  ?  110 VAL D CG2 1 
ATOM   3990 N N   . LYS D 4 112 ? 11.088 -5.525  -64.188 1.00 38.80  ?  111 LYS D N   1 
ATOM   3991 C CA  . LYS D 4 112 ? 11.001 -6.339  -65.404 1.00 36.83  ?  111 LYS D CA  1 
ATOM   3992 C C   . LYS D 4 112 ? 11.833 -5.721  -66.510 1.00 36.76  ?  111 LYS D C   1 
ATOM   3993 O O   . LYS D 4 112 ? 11.617 -4.549  -66.831 1.00 35.62  ?  111 LYS D O   1 
ATOM   3994 C CB  . LYS D 4 112 ? 9.549  -6.450  -65.856 1.00 36.22  ?  111 LYS D CB  1 
ATOM   3995 C CG  . LYS D 4 112 ? 8.685  -7.261  -64.912 1.00 46.44  ?  111 LYS D CG  1 
ATOM   3996 C CD  . LYS D 4 112 ? 7.363  -6.573  -64.658 1.00 52.60  ?  111 LYS D CD  1 
ATOM   3997 C CE  . LYS D 4 112 ? 6.364  -6.848  -65.770 1.00 58.40  ?  111 LYS D CE  1 
ATOM   3998 N NZ  . LYS D 4 112 ? 5.029  -7.236  -65.235 1.00 57.55  ?  111 LYS D NZ  1 
ATOM   3999 N N   . PRO D 4 113 ? 12.764 -6.453  -67.129 1.00 32.36  ?  112 PRO D N   1 
ATOM   4000 C CA  . PRO D 4 113 ? 13.566 -5.875  -68.213 1.00 39.36  ?  112 PRO D CA  1 
ATOM   4001 C C   . PRO D 4 113 ? 12.709 -5.628  -69.448 1.00 36.86  ?  112 PRO D C   1 
ATOM   4002 O O   . PRO D 4 113 ? 11.643 -6.225  -69.627 1.00 38.57  ?  112 PRO D O   1 
ATOM   4003 C CB  . PRO D 4 113 ? 14.612 -6.958  -68.491 1.00 34.70  ?  112 PRO D CB  1 
ATOM   4004 C CG  . PRO D 4 113 ? 13.804 -8.233  -68.304 1.00 33.66  ?  112 PRO D CG  1 
ATOM   4005 C CD  . PRO D 4 113 ? 12.871 -7.926  -67.108 1.00 36.79  ?  112 PRO D CD  1 
ATOM   4006 N N   . ASN D 4 114 ? 13.199 -4.756  -70.320 1.00 37.65  ?  113 ASN D N   1 
ATOM   4007 C CA  . ASN D 4 114 ? 12.512 -4.482  -71.586 1.00 48.59  ?  113 ASN D CA  1 
ATOM   4008 C C   . ASN D 4 114 ? 13.061 -5.425  -72.661 1.00 42.29  ?  113 ASN D C   1 
ATOM   4009 O O   . ASN D 4 114 ? 14.137 -5.199  -73.224 1.00 44.28  ?  113 ASN D O   1 
ATOM   4010 C CB  . ASN D 4 114 ? 12.666 -3.016  -71.975 1.00 53.02  ?  113 ASN D CB  1 
ATOM   4011 C CG  . ASN D 4 114 ? 11.879 -2.679  -73.211 1.00 55.03  ?  113 ASN D CG  1 
ATOM   4012 O OD1 . ASN D 4 114 ? 10.721 -3.080  -73.339 1.00 62.85  ?  113 ASN D OD1 1 
ATOM   4013 N ND2 . ASN D 4 114 ? 12.510 -1.986  -74.150 1.00 59.26  ?  113 ASN D ND2 1 
ATOM   4014 N N   . ILE D 4 115 ? 12.350 -6.516  -72.923 1.00 35.75  ?  114 ILE D N   1 
ATOM   4015 C CA  . ILE D 4 115 ? 12.787 -7.481  -73.929 1.00 40.86  ?  114 ILE D CA  1 
ATOM   4016 C C   . ILE D 4 115 ? 12.455 -6.919  -75.313 1.00 44.96  ?  114 ILE D C   1 
ATOM   4017 O O   . ILE D 4 115 ? 11.289 -6.884  -75.707 1.00 44.67  ?  114 ILE D O   1 
ATOM   4018 C CB  . ILE D 4 115 ? 12.127 -8.844  -73.716 1.00 40.02  ?  114 ILE D CB  1 
ATOM   4019 C CG1 . ILE D 4 115 ? 12.273 -9.271  -72.255 1.00 38.31  ?  114 ILE D CG1 1 
ATOM   4020 C CG2 . ILE D 4 115 ? 12.724 -9.858  -74.668 1.00 40.41  ?  114 ILE D CG2 1 
ATOM   4021 C CD1 . ILE D 4 115 ? 13.697 -9.624  -71.873 1.00 31.59  ?  114 ILE D CD1 1 
ATOM   4022 N N   . GLN D 4 116 ? 13.470 -6.490  -76.060 1.00 42.04  ?  115 GLN D N   1 
ATOM   4023 C CA  . GLN D 4 116 ? 13.192 -5.810  -77.324 1.00 54.98  ?  115 GLN D CA  1 
ATOM   4024 C C   . GLN D 4 116 ? 12.993 -6.752  -78.504 1.00 55.82  ?  115 GLN D C   1 
ATOM   4025 O O   . GLN D 4 116 ? 12.414 -6.337  -79.516 1.00 57.58  ?  115 GLN D O   1 
ATOM   4026 C CB  . GLN D 4 116 ? 14.310 -4.819  -77.671 1.00 64.10  ?  115 GLN D CB  1 
ATOM   4027 C CG  . GLN D 4 116 ? 15.738 -5.312  -77.404 1.00 65.71  ?  115 GLN D CG  1 
ATOM   4028 C CD  . GLN D 4 116 ? 16.375 -4.598  -76.215 1.00 68.56  ?  115 GLN D CD  1 
ATOM   4029 O OE1 . GLN D 4 116 ? 15.945 -4.773  -75.073 1.00 69.49  ?  115 GLN D OE1 1 
ATOM   4030 N NE2 . GLN D 4 116 ? 17.388 -3.773  -76.484 1.00 68.93  ?  115 GLN D NE2 1 
ATOM   4031 N N   . ASN D 4 117 ? 13.460 -7.996  -78.419 1.00 45.41  ?  116 ASN D N   1 
ATOM   4032 C CA  . ASN D 4 117 ? 13.311 -8.955  -79.514 1.00 43.41  ?  116 ASN D CA  1 
ATOM   4033 C C   . ASN D 4 117 ? 12.891 -10.294 -78.945 1.00 39.23  ?  116 ASN D C   1 
ATOM   4034 O O   . ASN D 4 117 ? 13.657 -11.260 -78.965 1.00 40.43  ?  116 ASN D O   1 
ATOM   4035 C CB  . ASN D 4 117 ? 14.610 -9.079  -80.314 1.00 44.95  ?  116 ASN D CB  1 
ATOM   4036 C CG  . ASN D 4 117 ? 14.999 -7.780  -81.008 1.00 53.35  ?  116 ASN D CG  1 
ATOM   4037 O OD1 . ASN D 4 117 ? 14.253 -7.264  -81.836 1.00 58.88  ?  116 ASN D OD1 1 
ATOM   4038 N ND2 . ASN D 4 117 ? 16.167 -7.245  -80.663 1.00 49.84  ?  116 ASN D ND2 1 
ATOM   4039 N N   . PRO D 4 118 ? 11.673 -10.390 -78.421 1.00 36.60  ?  117 PRO D N   1 
ATOM   4040 C CA  . PRO D 4 118 ? 11.210 -11.673 -77.893 1.00 38.92  ?  117 PRO D CA  1 
ATOM   4041 C C   . PRO D 4 118 ? 11.288 -12.756 -78.950 1.00 38.50  ?  117 PRO D C   1 
ATOM   4042 O O   . PRO D 4 118 ? 11.164 -12.501 -80.152 1.00 39.17  ?  117 PRO D O   1 
ATOM   4043 C CB  . PRO D 4 118 ? 9.760  -11.400 -77.475 1.00 37.49  ?  117 PRO D CB  1 
ATOM   4044 C CG  . PRO D 4 118 ? 9.439  -10.058 -78.004 1.00 39.20  ?  117 PRO D CG  1 
ATOM   4045 C CD  . PRO D 4 118 ? 10.699 -9.314  -78.200 1.00 40.07  ?  117 PRO D CD  1 
ATOM   4046 N N   . ASP D 4 119 ? 11.483 -13.978 -78.478 1.00 34.29  ?  118 ASP D N   1 
ATOM   4047 C CA  . ASP D 4 119 ? 11.678 -15.135 -79.327 1.00 34.12  ?  118 ASP D CA  1 
ATOM   4048 C C   . ASP D 4 119 ? 11.283 -16.375 -78.549 1.00 34.66  ?  118 ASP D C   1 
ATOM   4049 O O   . ASP D 4 119 ? 12.065 -17.324 -78.442 1.00 36.20  ?  118 ASP D O   1 
ATOM   4050 C CB  . ASP D 4 119 ? 13.122 -15.202 -79.784 1.00 38.80  ?  118 ASP D CB  1 
ATOM   4051 C CG  . ASP D 4 119 ? 13.298 -16.001 -81.050 1.00 41.75  ?  118 ASP D CG  1 
ATOM   4052 O OD1 . ASP D 4 119 ? 12.354 -16.698 -81.497 1.00 42.95  ?  118 ASP D OD1 1 
ATOM   4053 O OD2 . ASP D 4 119 ? 14.416 -15.943 -81.591 1.00 39.98  -1 118 ASP D OD2 1 
ATOM   4054 N N   . PRO D 4 120 ? 10.064 -16.410 -78.031 1.00 36.05  ?  119 PRO D N   1 
ATOM   4055 C CA  . PRO D 4 120 ? 9.666  -17.494 -77.124 1.00 32.34  ?  119 PRO D CA  1 
ATOM   4056 C C   . PRO D 4 120 ? 9.938  -18.861 -77.722 1.00 41.22  ?  119 PRO D C   1 
ATOM   4057 O O   . PRO D 4 120 ? 9.693  -19.109 -78.907 1.00 40.47  ?  119 PRO D O   1 
ATOM   4058 C CB  . PRO D 4 120 ? 8.163  -17.255 -76.917 1.00 41.26  ?  119 PRO D CB  1 
ATOM   4059 C CG  . PRO D 4 120 ? 7.755  -16.287 -78.046 1.00 38.85  ?  119 PRO D CG  1 
ATOM   4060 C CD  . PRO D 4 120 ? 8.972  -15.471 -78.322 1.00 33.92  ?  119 PRO D CD  1 
ATOM   4061 N N   . ALA D 4 121 ? 10.456 -19.757 -76.886 1.00 38.18  ?  120 ALA D N   1 
ATOM   4062 C CA  . ALA D 4 121 ? 10.849 -21.073 -77.352 1.00 32.73  ?  120 ALA D CA  1 
ATOM   4063 C C   . ALA D 4 121 ? 10.982 -22.002 -76.155 1.00 34.37  ?  120 ALA D C   1 
ATOM   4064 O O   . ALA D 4 121 ? 11.320 -21.572 -75.047 1.00 31.54  ?  120 ALA D O   1 
ATOM   4065 C CB  . ALA D 4 121 ? 12.158 -21.002 -78.134 1.00 34.37  ?  120 ALA D CB  1 
ATOM   4066 N N   . VAL D 4 122 ? 10.715 -23.274 -76.402 1.00 29.94  ?  121 VAL D N   1 
ATOM   4067 C CA  . VAL D 4 122 ? 10.898 -24.358 -75.436 1.00 38.73  ?  121 VAL D CA  1 
ATOM   4068 C C   . VAL D 4 122 ? 11.926 -25.332 -76.006 1.00 36.86  ?  121 VAL D C   1 
ATOM   4069 O O   . VAL D 4 122 ? 11.675 -25.981 -77.031 1.00 35.78  ?  121 VAL D O   1 
ATOM   4070 C CB  . VAL D 4 122 ? 9.574  -25.074 -75.134 1.00 35.11  ?  121 VAL D CB  1 
ATOM   4071 C CG1 . VAL D 4 122 ? 9.797  -26.199 -74.162 1.00 39.44  ?  121 VAL D CG1 1 
ATOM   4072 C CG2 . VAL D 4 122 ? 8.578  -24.092 -74.579 1.00 32.89  ?  121 VAL D CG2 1 
ATOM   4073 N N   . TYR D 4 123 ? 13.075 -25.437 -75.333 1.00 31.04  ?  122 TYR D N   1 
ATOM   4074 C CA  . TYR D 4 123 ? 14.170 -26.302 -75.736 1.00 32.30  ?  122 TYR D CA  1 
ATOM   4075 C C   . TYR D 4 123 ? 14.336 -27.464 -74.775 1.00 35.33  ?  122 TYR D C   1 
ATOM   4076 O O   . TYR D 4 123 ? 14.030 -27.364 -73.582 1.00 34.64  ?  122 TYR D O   1 
ATOM   4077 C CB  . TYR D 4 123 ? 15.496 -25.536 -75.791 1.00 34.40  ?  122 TYR D CB  1 
ATOM   4078 C CG  . TYR D 4 123 ? 15.462 -24.370 -76.740 1.00 33.55  ?  122 TYR D CG  1 
ATOM   4079 C CD1 . TYR D 4 123 ? 15.418 -24.569 -78.108 1.00 33.34  ?  122 TYR D CD1 1 
ATOM   4080 C CD2 . TYR D 4 123 ? 15.452 -23.057 -76.267 1.00 29.86  ?  122 TYR D CD2 1 
ATOM   4081 C CE1 . TYR D 4 123 ? 15.397 -23.489 -78.985 1.00 31.11  ?  122 TYR D CE1 1 
ATOM   4082 C CE2 . TYR D 4 123 ? 15.404 -21.981 -77.131 1.00 30.01  ?  122 TYR D CE2 1 
ATOM   4083 C CZ  . TYR D 4 123 ? 15.385 -22.201 -78.490 1.00 32.43  ?  122 TYR D CZ  1 
ATOM   4084 O OH  . TYR D 4 123 ? 15.342 -21.138 -79.359 1.00 33.10  ?  122 TYR D OH  1 
ATOM   4085 N N   . GLN D 4 124 ? 14.846 -28.567 -75.306 1.00 33.71  ?  123 GLN D N   1 
ATOM   4086 C CA  . GLN D 4 124 ? 15.225 -29.710 -74.498 1.00 34.36  ?  123 GLN D CA  1 
ATOM   4087 C C   . GLN D 4 124 ? 16.744 -29.764 -74.401 1.00 32.33  ?  123 GLN D C   1 
ATOM   4088 O O   . GLN D 4 124 ? 17.438 -29.592 -75.407 1.00 34.07  ?  123 GLN D O   1 
ATOM   4089 C CB  . GLN D 4 124 ? 14.679 -31.018 -75.079 1.00 36.00  ?  123 GLN D CB  1 
ATOM   4090 C CG  . GLN D 4 124 ? 14.730 -32.159 -74.056 1.00 41.94  ?  123 GLN D CG  1 
ATOM   4091 C CD  . GLN D 4 124 ? 14.364 -33.529 -74.629 1.00 51.88  ?  123 GLN D CD  1 
ATOM   4092 O OE1 . GLN D 4 124 ? 14.170 -33.678 -75.833 1.00 55.11  ?  123 GLN D OE1 1 
ATOM   4093 N NE2 . GLN D 4 124 ? 14.287 -34.541 -73.753 1.00 52.28  ?  123 GLN D NE2 1 
ATOM   4094 N N   . LEU D 4 125 ? 17.250 -29.993 -73.189 1.00 34.19  ?  124 LEU D N   1 
ATOM   4095 C CA  . LEU D 4 125 ? 18.678 -30.055 -72.899 1.00 35.01  ?  124 LEU D CA  1 
ATOM   4096 C C   . LEU D 4 125 ? 19.006 -31.400 -72.269 1.00 40.13  ?  124 LEU D C   1 
ATOM   4097 O O   . LEU D 4 125 ? 18.318 -31.832 -71.335 1.00 39.00  ?  124 LEU D O   1 
ATOM   4098 C CB  . LEU D 4 125 ? 19.100 -28.939 -71.930 1.00 32.63  ?  124 LEU D CB  1 
ATOM   4099 C CG  . LEU D 4 125 ? 19.114 -27.452 -72.294 1.00 36.03  ?  124 LEU D CG  1 
ATOM   4100 C CD1 . LEU D 4 125 ? 17.703 -26.927 -72.535 1.00 36.57  ?  124 LEU D CD1 1 
ATOM   4101 C CD2 . LEU D 4 125 ? 19.799 -26.666 -71.161 1.00 31.59  ?  124 LEU D CD2 1 
ATOM   4102 N N   . ARG D 4 126 ? 20.069 -32.043 -72.740 1.00 34.87  ?  125 ARG D N   1 
ATOM   4103 C CA  . ARG D 4 126 ? 20.410 -33.369 -72.249 1.00 40.05  ?  125 ARG D CA  1 
ATOM   4104 C C   . ARG D 4 126 ? 21.580 -33.305 -71.271 1.00 42.06  ?  125 ARG D C   1 
ATOM   4105 O O   . ARG D 4 126 ? 22.469 -32.455 -71.390 1.00 33.29  ?  125 ARG D O   1 
ATOM   4106 C CB  . ARG D 4 126 ? 20.735 -34.312 -73.413 1.00 42.10  ?  125 ARG D CB  1 
ATOM   4107 C CG  . ARG D 4 126 ? 19.645 -34.317 -74.514 1.00 54.30  ?  125 ARG D CG  1 
ATOM   4108 C CD  . ARG D 4 126 ? 19.380 -35.704 -75.095 1.00 54.66  ?  125 ARG D CD  1 
ATOM   4109 N NE  . ARG D 4 126 ? 18.540 -36.521 -74.218 1.00 66.66  ?  125 ARG D NE  1 
ATOM   4110 C CZ  . ARG D 4 126 ? 17.474 -37.219 -74.617 1.00 72.20  ?  125 ARG D CZ  1 
ATOM   4111 N NH1 . ARG D 4 126 ? 17.089 -37.209 -75.895 1.00 60.07  ?  125 ARG D NH1 1 
ATOM   4112 N NH2 . ARG D 4 126 ? 16.791 -37.936 -73.730 1.00 77.50  ?  125 ARG D NH2 1 
ATOM   4113 N N   . ASP D 4 127 ? 21.569 -34.235 -70.311 1.00 43.78  ?  126 ASP D N   1 
ATOM   4114 C CA  . ASP D 4 127 ? 22.603 -34.315 -69.283 1.00 42.22  ?  126 ASP D CA  1 
ATOM   4115 C C   . ASP D 4 127 ? 23.979 -34.479 -69.914 1.00 45.88  ?  126 ASP D C   1 
ATOM   4116 O O   . ASP D 4 127 ? 24.177 -35.318 -70.800 1.00 44.05  ?  126 ASP D O   1 
ATOM   4117 C CB  . ASP D 4 127 ? 22.311 -35.483 -68.336 1.00 40.14  ?  126 ASP D CB  1 
ATOM   4118 C CG  . ASP D 4 127 ? 23.265 -35.544 -67.124 1.00 39.53  ?  126 ASP D CG  1 
ATOM   4119 O OD1 . ASP D 4 127 ? 24.364 -34.971 -67.154 1.00 36.31  ?  126 ASP D OD1 1 
ATOM   4120 O OD2 . ASP D 4 127 ? 22.923 -36.223 -66.135 1.00 39.21  -1 126 ASP D OD2 1 
ATOM   4121 N N   . SER D 4 128 ? 24.926 -33.662 -69.436 1.00 41.27  ?  127 SER D N   1 
ATOM   4122 C CA  . SER D 4 128 ? 26.329 -33.770 -69.816 1.00 43.80  ?  127 SER D CA  1 
ATOM   4123 C C   . SER D 4 128 ? 26.917 -35.152 -69.551 1.00 49.58  ?  127 SER D C   1 
ATOM   4124 O O   . SER D 4 128 ? 27.849 -35.564 -70.274 1.00 48.23  ?  127 SER D O   1 
ATOM   4125 C CB  . SER D 4 128 ? 27.173 -32.770 -69.041 1.00 39.46  ?  127 SER D CB  1 
ATOM   4126 O OG  . SER D 4 128 ? 28.511 -32.734 -69.510 1.00 45.55  ?  127 SER D OG  1 
ATOM   4127 N N   . LYS D 4 129 ? 26.303 -35.965 -68.715 1.00 50.53  ?  128 LYS D N   1 
ATOM   4128 C CA  . LYS D 4 129 ? 26.792 -37.309 -68.425 1.00 52.35  ?  128 LYS D CA  1 
ATOM   4129 C C   . LYS D 4 129 ? 25.843 -38.403 -68.913 1.00 51.05  ?  128 LYS D C   1 
ATOM   4130 O O   . LYS D 4 129 ? 26.235 -39.264 -69.705 1.00 58.07  ?  128 LYS D O   1 
ATOM   4131 C CB  . LYS D 4 129 ? 26.990 -37.445 -66.905 1.00 48.62  ?  128 LYS D CB  1 
ATOM   4132 C CG  . LYS D 4 129 ? 28.343 -37.034 -66.396 1.00 56.31  ?  128 LYS D CG  1 
ATOM   4133 C CD  . LYS D 4 129 ? 28.946 -35.931 -67.261 1.00 54.41  ?  128 LYS D CD  1 
ATOM   4134 C CE  . LYS D 4 129 ? 30.478 -35.923 -67.216 1.00 56.41  ?  128 LYS D CE  1 
ATOM   4135 N NZ  . LYS D 4 129 ? 31.060 -34.732 -67.933 1.00 56.14  ?  128 LYS D NZ  1 
ATOM   4136 N N   . SER D 4 130 ? 24.610 -38.408 -68.417 1.00 56.87  ?  129 SER D N   1 
ATOM   4137 C CA  . SER D 4 130 ? 23.760 -39.590 -68.494 1.00 62.95  ?  129 SER D CA  1 
ATOM   4138 C C   . SER D 4 130 ? 22.916 -39.566 -69.756 1.00 65.47  ?  129 SER D C   1 
ATOM   4139 O O   . SER D 4 130 ? 22.915 -38.600 -70.522 1.00 70.10  ?  129 SER D O   1 
ATOM   4140 C CB  . SER D 4 130 ? 22.858 -39.694 -67.259 1.00 59.46  ?  129 SER D CB  1 
ATOM   4141 O OG  . SER D 4 130 ? 21.744 -38.819 -67.359 1.00 48.97  ?  129 SER D OG  1 
ATOM   4142 N N   . SER D 4 131 ? 22.192 -40.657 -69.977 1.00 67.41  ?  130 SER D N   1 
ATOM   4143 C CA  . SER D 4 131 ? 21.314 -40.751 -71.138 1.00 77.24  ?  130 SER D CA  1 
ATOM   4144 C C   . SER D 4 131 ? 19.856 -40.568 -70.757 1.00 75.92  ?  130 SER D C   1 
ATOM   4145 O O   . SER D 4 131 ? 19.085 -39.960 -71.513 1.00 74.98  ?  130 SER D O   1 
ATOM   4146 C CB  . SER D 4 131 ? 21.494 -42.102 -71.851 1.00 72.13  ?  130 SER D CB  1 
ATOM   4147 N N   . ASP D 4 132 ? 19.482 -41.077 -69.582 1.00 73.78  ?  131 ASP D N   1 
ATOM   4148 C CA  . ASP D 4 132 ? 18.134 -40.886 -69.070 1.00 71.29  ?  131 ASP D CA  1 
ATOM   4149 C C   . ASP D 4 132 ? 17.740 -39.409 -69.101 1.00 61.90  ?  131 ASP D C   1 
ATOM   4150 O O   . ASP D 4 132 ? 16.740 -39.039 -69.723 1.00 56.33  ?  131 ASP D O   1 
ATOM   4151 C CB  . ASP D 4 132 ? 18.061 -41.479 -67.651 1.00 71.94  ?  131 ASP D CB  1 
ATOM   4152 N N   . LYS D 4 133 ? 18.567 -38.542 -68.511 1.00 58.63  ?  132 LYS D N   1 
ATOM   4153 C CA  . LYS D 4 133 ? 18.091 -37.290 -67.928 1.00 51.01  ?  132 LYS D CA  1 
ATOM   4154 C C   . LYS D 4 133 ? 18.054 -36.128 -68.918 1.00 40.28  ?  132 LYS D C   1 
ATOM   4155 O O   . LYS D 4 133 ? 19.017 -35.878 -69.648 1.00 41.39  ?  132 LYS D O   1 
ATOM   4156 C CB  . LYS D 4 133 ? 18.957 -36.930 -66.723 1.00 44.29  ?  132 LYS D CB  1 
ATOM   4157 C CG  . LYS D 4 133 ? 19.190 -38.109 -65.789 1.00 53.52  ?  132 LYS D CG  1 
ATOM   4158 C CD  . LYS D 4 133 ? 19.738 -37.644 -64.449 1.00 53.31  ?  132 LYS D CD  1 
ATOM   4159 C CE  . LYS D 4 133 ? 20.745 -36.525 -64.642 1.00 47.41  ?  132 LYS D CE  1 
ATOM   4160 N NZ  . LYS D 4 133 ? 21.798 -36.592 -63.591 1.00 55.46  ?  132 LYS D NZ  1 
ATOM   4161 N N   . SER D 4 134 ? 16.944 -35.393 -68.909 1.00 41.04  ?  133 SER D N   1 
ATOM   4162 C CA  . SER D 4 134 ? 16.863 -34.138 -69.637 1.00 43.29  ?  133 SER D CA  1 
ATOM   4163 C C   . SER D 4 134 ? 16.066 -33.110 -68.836 1.00 38.64  ?  133 SER D C   1 
ATOM   4164 O O   . SER D 4 134 ? 15.468 -33.403 -67.801 1.00 42.32  ?  133 SER D O   1 
ATOM   4165 C CB  . SER D 4 134 ? 16.248 -34.337 -71.029 1.00 47.38  ?  133 SER D CB  1 
ATOM   4166 O OG  . SER D 4 134 ? 14.933 -34.844 -70.906 1.00 56.96  ?  133 SER D OG  1 
ATOM   4167 N N   . VAL D 4 135 ? 16.033 -31.902 -69.372 1.00 36.35  ?  134 VAL D N   1 
ATOM   4168 C CA  . VAL D 4 135 ? 15.430 -30.733 -68.760 1.00 34.47  ?  134 VAL D CA  1 
ATOM   4169 C C   . VAL D 4 135 ? 14.806 -29.924 -69.891 1.00 35.05  ?  134 VAL D C   1 
ATOM   4170 O O   . VAL D 4 135 ? 15.299 -29.963 -71.022 1.00 31.66  ?  134 VAL D O   1 
ATOM   4171 C CB  . VAL D 4 135 ? 16.540 -29.962 -68.007 1.00 35.60  ?  134 VAL D CB  1 
ATOM   4172 C CG1 . VAL D 4 135 ? 16.248 -28.497 -67.932 1.00 38.92  ?  134 VAL D CG1 1 
ATOM   4173 C CG2 . VAL D 4 135 ? 16.766 -30.569 -66.649 1.00 34.54  ?  134 VAL D CG2 1 
ATOM   4174 N N   . CYS D 4 136 ? 13.704 -29.216 -69.609 1.00 30.98  ?  135 CYS D N   1 
ATOM   4175 C CA  . CYS D 4 136 ? 13.076 -28.333 -70.594 1.00 35.73  ?  135 CYS D CA  1 
ATOM   4176 C C   . CYS D 4 136 ? 13.253 -26.877 -70.181 1.00 34.01  ?  135 CYS D C   1 
ATOM   4177 O O   . CYS D 4 136 ? 13.062 -26.523 -69.012 1.00 33.30  ?  135 CYS D O   1 
ATOM   4178 C CB  . CYS D 4 136 ? 11.576 -28.637 -70.784 1.00 35.45  ?  135 CYS D CB  1 
ATOM   4179 S SG  . CYS D 4 136 ? 11.232 -30.361 -71.328 1.00 44.22  ?  135 CYS D SG  1 
ATOM   4180 N N   . LEU D 4 137 ? 13.599 -26.040 -71.149 1.00 29.40  ?  136 LEU D N   1 
ATOM   4181 C CA  . LEU D 4 137 ? 13.909 -24.634 -70.926 1.00 30.73  ?  136 LEU D CA  1 
ATOM   4182 C C   . LEU D 4 137 ? 12.957 -23.773 -71.739 1.00 33.16  ?  136 LEU D C   1 
ATOM   4183 O O   . LEU D 4 137 ? 13.002 -23.810 -72.976 1.00 30.49  ?  136 LEU D O   1 
ATOM   4184 C CB  . LEU D 4 137 ? 15.351 -24.327 -71.342 1.00 27.64  ?  136 LEU D CB  1 
ATOM   4185 C CG  . LEU D 4 137 ? 15.764 -22.858 -71.326 1.00 28.98  ?  136 LEU D CG  1 
ATOM   4186 C CD1 . LEU D 4 137 ? 15.862 -22.375 -69.861 1.00 32.18  ?  136 LEU D CD1 1 
ATOM   4187 C CD2 . LEU D 4 137 ? 17.089 -22.670 -72.091 1.00 24.36  ?  136 LEU D CD2 1 
ATOM   4188 N N   . PHE D 4 138 ? 12.110 -22.998 -71.050 1.00 26.82  ?  137 PHE D N   1 
ATOM   4189 C CA  . PHE D 4 138 ? 11.262 -21.979 -71.664 1.00 30.02  ?  137 PHE D CA  1 
ATOM   4190 C C   . PHE D 4 138 ? 11.995 -20.644 -71.573 1.00 32.52  ?  137 PHE D C   1 
ATOM   4191 O O   . PHE D 4 138 ? 12.315 -20.183 -70.468 1.00 32.57  ?  137 PHE D O   1 
ATOM   4192 C CB  . PHE D 4 138 ? 9.907  -21.907 -70.951 1.00 34.15  ?  137 PHE D CB  1 
ATOM   4193 C CG  . PHE D 4 138 ? 8.945  -20.907 -71.547 1.00 37.83  ?  137 PHE D CG  1 
ATOM   4194 C CD1 . PHE D 4 138 ? 8.905  -20.690 -72.916 1.00 32.23  ?  137 PHE D CD1 1 
ATOM   4195 C CD2 . PHE D 4 138 ? 8.088  -20.175 -70.728 1.00 31.38  ?  137 PHE D CD2 1 
ATOM   4196 C CE1 . PHE D 4 138 ? 8.013  -19.760 -73.462 1.00 35.53  ?  137 PHE D CE1 1 
ATOM   4197 C CE2 . PHE D 4 138 ? 7.205  -19.249 -71.257 1.00 37.66  ?  137 PHE D CE2 1 
ATOM   4198 C CZ  . PHE D 4 138 ? 7.158  -19.037 -72.628 1.00 33.59  ?  137 PHE D CZ  1 
ATOM   4199 N N   . THR D 4 139 ? 12.272 -20.029 -72.716 1.00 30.78  ?  138 THR D N   1 
ATOM   4200 C CA  . THR D 4 139 ? 13.175 -18.889 -72.704 1.00 28.64  ?  138 THR D CA  1 
ATOM   4201 C C   . THR D 4 139 ? 12.819 -17.903 -73.811 1.00 33.04  ?  138 THR D C   1 
ATOM   4202 O O   . THR D 4 139 ? 12.133 -18.236 -74.783 1.00 32.79  ?  138 THR D O   1 
ATOM   4203 C CB  . THR D 4 139 ? 14.629 -19.377 -72.834 1.00 29.75  ?  138 THR D CB  1 
ATOM   4204 O OG1 . THR D 4 139 ? 15.536 -18.280 -72.689 1.00 30.47  ?  138 THR D OG1 1 
ATOM   4205 C CG2 . THR D 4 139 ? 14.849 -20.048 -74.188 1.00 31.61  ?  138 THR D CG2 1 
ATOM   4206 N N   . ASP D 4 140 ? 13.300 -16.670 -73.635 1.00 29.43  ?  139 ASP D N   1 
ATOM   4207 C CA  . ASP D 4 140 ? 13.238 -15.556 -74.583 1.00 35.15  ?  139 ASP D CA  1 
ATOM   4208 C C   . ASP D 4 140 ? 11.834 -14.966 -74.741 1.00 35.91  ?  139 ASP D C   1 
ATOM   4209 O O   . ASP D 4 140 ? 11.603 -14.166 -75.655 1.00 34.03  ?  139 ASP D O   1 
ATOM   4210 C CB  . ASP D 4 140 ? 13.836 -15.964 -75.939 1.00 30.83  ?  139 ASP D CB  1 
ATOM   4211 C CG  . ASP D 4 140 ? 15.357 -16.258 -75.840 1.00 39.39  ?  139 ASP D CG  1 
ATOM   4212 O OD1 . ASP D 4 140 ? 15.953 -15.994 -74.759 1.00 37.21  ?  139 ASP D OD1 1 
ATOM   4213 O OD2 . ASP D 4 140 ? 15.976 -16.750 -76.816 1.00 31.93  -1 139 ASP D OD2 1 
ATOM   4214 N N   . PHE D 4 141 ? 10.903 -15.300 -73.853 1.00 31.75  ?  140 PHE D N   1 
ATOM   4215 C CA  . PHE D 4 141 ? 9.611  -14.638 -73.829 1.00 32.60  ?  140 PHE D CA  1 
ATOM   4216 C C   . PHE D 4 141 ? 9.731  -13.233 -73.224 1.00 43.27  ?  140 PHE D C   1 
ATOM   4217 O O   . PHE D 4 141 ? 10.650 -12.922 -72.455 1.00 33.73  ?  140 PHE D O   1 
ATOM   4218 C CB  . PHE D 4 141 ? 8.591  -15.480 -73.053 1.00 38.83  ?  140 PHE D CB  1 
ATOM   4219 C CG  . PHE D 4 141 ? 9.070  -15.950 -71.699 1.00 34.45  ?  140 PHE D CG  1 
ATOM   4220 C CD1 . PHE D 4 141 ? 9.739  -17.153 -71.565 1.00 31.19  ?  140 PHE D CD1 1 
ATOM   4221 C CD2 . PHE D 4 141 ? 8.852  -15.186 -70.573 1.00 34.44  ?  140 PHE D CD2 1 
ATOM   4222 C CE1 . PHE D 4 141 ? 10.196 -17.598 -70.326 1.00 34.96  ?  140 PHE D CE1 1 
ATOM   4223 C CE2 . PHE D 4 141 ? 9.295  -15.628 -69.317 1.00 34.74  ?  140 PHE D CE2 1 
ATOM   4224 C CZ  . PHE D 4 141 ? 9.974  -16.840 -69.201 1.00 29.08  ?  140 PHE D CZ  1 
ATOM   4225 N N   . ASP D 4 142 ? 8.793  -12.359 -73.579 1.00 41.67  ?  141 ASP D N   1 
ATOM   4226 C CA  . ASP D 4 142 ? 8.925  -11.045 -72.970 1.00 44.04  ?  141 ASP D CA  1 
ATOM   4227 C C   . ASP D 4 142 ? 8.189  -10.991 -71.631 1.00 40.61  ?  141 ASP D C   1 
ATOM   4228 O O   . ASP D 4 142 ? 7.524  -11.938 -71.201 1.00 38.94  ?  141 ASP D O   1 
ATOM   4229 C CB  . ASP D 4 142 ? 8.479  -9.939  -73.931 1.00 45.37  ?  141 ASP D CB  1 
ATOM   4230 C CG  . ASP D 4 142 ? 6.980  -9.874  -74.111 1.00 50.80  ?  141 ASP D CG  1 
ATOM   4231 O OD1 . ASP D 4 142 ? 6.243  -10.688 -73.515 1.00 50.39  ?  141 ASP D OD1 1 
ATOM   4232 O OD2 . ASP D 4 142 ? 6.540  -8.999  -74.885 1.00 59.01  -1 141 ASP D OD2 1 
ATOM   4233 N N   . SER D 4 143 ? 8.339  -9.861  -70.952 1.00 44.32  ?  142 SER D N   1 
ATOM   4234 C CA  . SER D 4 143 ? 8.042  -9.864  -69.530 1.00 48.97  ?  142 SER D CA  1 
ATOM   4235 C C   . SER D 4 143 ? 6.550  -9.884  -69.236 1.00 53.24  ?  142 SER D C   1 
ATOM   4236 O O   . SER D 4 143 ? 6.171  -9.986  -68.066 1.00 54.10  ?  142 SER D O   1 
ATOM   4237 C CB  . SER D 4 143 ? 8.724  -8.667  -68.880 1.00 44.68  ?  142 SER D CB  1 
ATOM   4238 O OG  . SER D 4 143 ? 10.127 -8.782  -69.041 1.00 44.88  ?  142 SER D OG  1 
ATOM   4239 N N   . GLN D 4 144 ? 5.701  -9.784  -70.262 1.00 51.11  ?  143 GLN D N   1 
ATOM   4240 C CA  . GLN D 4 144 ? 4.265  -9.946  -70.046 1.00 54.80  ?  143 GLN D CA  1 
ATOM   4241 C C   . GLN D 4 144 ? 3.911  -11.386 -69.690 1.00 52.37  ?  143 GLN D C   1 
ATOM   4242 O O   . GLN D 4 144 ? 2.965  -11.615 -68.929 1.00 50.40  ?  143 GLN D O   1 
ATOM   4243 C CB  . GLN D 4 144 ? 3.481  -9.501  -71.286 1.00 55.82  ?  143 GLN D CB  1 
ATOM   4244 C CG  . GLN D 4 144 ? 3.710  -8.042  -71.702 1.00 64.18  ?  143 GLN D CG  1 
ATOM   4245 C CD  . GLN D 4 144 ? 4.399  -7.185  -70.629 1.00 65.52  ?  143 GLN D CD  1 
ATOM   4246 O OE1 . GLN D 4 144 ? 4.093  -7.272  -69.432 1.00 68.81  ?  143 GLN D OE1 1 
ATOM   4247 N NE2 . GLN D 4 144 ? 5.340  -6.349  -71.067 1.00 66.76  ?  143 GLN D NE2 1 
ATOM   4248 N N   . THR D 4 145 ? 4.665  -12.358 -70.208 1.00 46.45  ?  144 THR D N   1 
ATOM   4249 C CA  . THR D 4 145 ? 4.351  -13.760 -69.975 1.00 45.42  ?  144 THR D CA  1 
ATOM   4250 C C   . THR D 4 145 ? 4.511  -14.125 -68.501 1.00 50.56  ?  144 THR D C   1 
ATOM   4251 O O   . THR D 4 145 ? 5.468  -13.709 -67.838 1.00 50.12  ?  144 THR D O   1 
ATOM   4252 C CB  . THR D 4 145 ? 5.245  -14.662 -70.830 1.00 48.35  ?  144 THR D CB  1 
ATOM   4253 O OG1 . THR D 4 145 ? 4.888  -14.541 -72.215 1.00 50.41  ?  144 THR D OG1 1 
ATOM   4254 C CG2 . THR D 4 145 ? 5.088  -16.103 -70.398 1.00 39.42  ?  144 THR D CG2 1 
ATOM   4255 N N   . ASN D 4 146 ? 3.567  -14.914 -67.989 1.00 51.39  ?  145 ASN D N   1 
ATOM   4256 C CA  . ASN D 4 146 ? 3.589  -15.397 -66.612 1.00 47.93  ?  145 ASN D CA  1 
ATOM   4257 C C   . ASN D 4 146 ? 3.747  -16.907 -66.617 1.00 44.61  ?  145 ASN D C   1 
ATOM   4258 O O   . ASN D 4 146 ? 2.945  -17.611 -67.235 1.00 50.04  ?  145 ASN D O   1 
ATOM   4259 C CB  . ASN D 4 146 ? 2.311  -15.020 -65.867 1.00 51.23  ?  145 ASN D CB  1 
ATOM   4260 C CG  . ASN D 4 146 ? 2.254  -13.550 -65.502 1.00 61.58  ?  145 ASN D CG  1 
ATOM   4261 O OD1 . ASN D 4 146 ? 3.278  -12.862 -65.386 1.00 61.72  ?  145 ASN D OD1 1 
ATOM   4262 N ND2 . ASN D 4 146 ? 1.040  -13.062 -65.306 1.00 62.30  ?  145 ASN D ND2 1 
ATOM   4263 N N   . VAL D 4 147 ? 4.748  -17.407 -65.922 1.00 47.05  ?  146 VAL D N   1 
ATOM   4264 C CA  . VAL D 4 147 ? 4.971  -18.870 -65.867 1.00 43.48  ?  146 VAL D CA  1 
ATOM   4265 C C   . VAL D 4 147 ? 4.174  -19.396 -64.690 1.00 48.27  ?  146 VAL D C   1 
ATOM   4266 O O   . VAL D 4 147 ? 4.293  -18.860 -63.624 1.00 49.22  ?  146 VAL D O   1 
ATOM   4267 C CB  . VAL D 4 147 ? 6.457  -19.242 -65.783 1.00 46.43  ?  146 VAL D CB  1 
ATOM   4268 C CG1 . VAL D 4 147 ? 6.649  -20.656 -65.302 1.00 40.11  ?  146 VAL D CG1 1 
ATOM   4269 C CG2 . VAL D 4 147 ? 7.139  -19.061 -67.117 1.00 41.17  ?  146 VAL D CG2 1 
ATOM   4270 N N   . SER D 4 148 ? 3.391  -20.423 -64.918 1.00 48.27  ?  147 SER D N   1 
ATOM   4271 C CA  . SER D 4 148 ? 2.529  -20.933 -63.839 1.00 51.09  ?  147 SER D CA  1 
ATOM   4272 C C   . SER D 4 148 ? 3.188  -22.083 -63.097 1.00 51.61  ?  147 SER D C   1 
ATOM   4273 O O   . SER D 4 148 ? 3.821  -22.896 -63.716 1.00 48.11  ?  147 SER D O   1 
ATOM   4274 C CB  . SER D 4 148 ? 1.199  -21.342 -64.383 1.00 48.45  ?  147 SER D CB  1 
ATOM   4275 O OG  . SER D 4 148 ? 0.612  -20.292 -65.120 1.00 58.70  ?  147 SER D OG  1 
ATOM   4276 N N   . GLN D 4 149 ? 2.865  -22.205 -61.814 1.00 54.83  ?  148 GLN D N   1 
ATOM   4277 C CA  . GLN D 4 149 ? 3.393  -23.290 -60.959 1.00 60.03  ?  148 GLN D CA  1 
ATOM   4278 C C   . GLN D 4 149 ? 2.927  -24.634 -61.494 1.00 55.30  ?  148 GLN D C   1 
ATOM   4279 O O   . GLN D 4 149 ? 1.843  -24.733 -61.990 1.00 61.26  ?  148 GLN D O   1 
ATOM   4280 C CB  . GLN D 4 149 ? 2.817  -23.252 -59.542 1.00 60.15  ?  148 GLN D CB  1 
ATOM   4281 C CG  . GLN D 4 149 ? 2.449  -21.879 -59.023 1.00 67.95  ?  148 GLN D CG  1 
ATOM   4282 C CD  . GLN D 4 149 ? 3.549  -21.293 -58.179 1.00 73.64  ?  148 GLN D CD  1 
ATOM   4283 O OE1 . GLN D 4 149 ? 4.719  -21.602 -58.364 1.00 78.34  ?  148 GLN D OE1 1 
ATOM   4284 N NE2 . GLN D 4 149 ? 3.189  -20.410 -57.264 1.00 72.28  ?  148 GLN D NE2 1 
ATOM   4285 N N   . SER D 4 150 ? 3.725  -25.656 -61.318 1.00 50.66  ?  149 SER D N   1 
ATOM   4286 C CA  . SER D 4 150 ? 3.260  -26.984 -61.737 1.00 51.44  ?  149 SER D CA  1 
ATOM   4287 C C   . SER D 4 150 ? 2.075  -27.346 -60.840 1.00 60.16  ?  149 SER D C   1 
ATOM   4288 O O   . SER D 4 150 ? 2.165  -27.140 -59.635 1.00 54.42  ?  149 SER D O   1 
ATOM   4289 C CB  . SER D 4 150 ? 4.347  -27.973 -61.612 1.00 46.73  ?  149 SER D CB  1 
ATOM   4290 O OG  . SER D 4 150 ? 3.849  -29.270 -61.706 1.00 44.32  ?  149 SER D OG  1 
ATOM   4291 N N   . LYS D 4 151 ? 1.005  -27.844 -61.444 1.00 55.24  ?  150 LYS D N   1 
ATOM   4292 C CA  . LYS D 4 151 ? -0.179 -28.322 -60.695 1.00 59.07  ?  150 LYS D CA  1 
ATOM   4293 C C   . LYS D 4 151 ? -0.085 -29.847 -60.628 1.00 57.94  ?  150 LYS D C   1 
ATOM   4294 O O   . LYS D 4 151 ? -1.058 -30.480 -60.229 1.00 57.03  ?  150 LYS D O   1 
ATOM   4295 C CB  . LYS D 4 151 ? -1.454 -27.836 -61.381 1.00 53.03  ?  150 LYS D CB  1 
ATOM   4296 N N   . ASP D 4 152 ? 1.062  -30.394 -61.027 1.00 56.61  ?  151 ASP D N   1 
ATOM   4297 C CA  . ASP D 4 152 ? 1.312  -31.830 -61.013 1.00 53.27  ?  151 ASP D CA  1 
ATOM   4298 C C   . ASP D 4 152 ? 2.592  -32.072 -60.226 1.00 54.05  ?  151 ASP D C   1 
ATOM   4299 O O   . ASP D 4 152 ? 3.664  -31.581 -60.605 1.00 53.03  ?  151 ASP D O   1 
ATOM   4300 C CB  . ASP D 4 152 ? 1.432  -32.370 -62.438 1.00 49.09  ?  151 ASP D CB  1 
ATOM   4301 C CG  . ASP D 4 152 ? 1.663  -33.858 -62.479 1.00 55.05  ?  151 ASP D CG  1 
ATOM   4302 O OD1 . ASP D 4 152 ? 2.195  -34.416 -61.482 1.00 57.57  ?  151 ASP D OD1 1 
ATOM   4303 O OD2 . ASP D 4 152 ? 1.302  -34.461 -63.518 1.00 57.16  -1 151 ASP D OD2 1 
ATOM   4304 N N   . SER D 4 153 ? 2.485  -32.834 -59.147 1.00 55.81  ?  152 SER D N   1 
ATOM   4305 C CA  . SER D 4 153 ? 3.551  -32.856 -58.157 1.00 53.81  ?  152 SER D CA  1 
ATOM   4306 C C   . SER D 4 153 ? 4.761  -33.693 -58.572 1.00 52.58  ?  152 SER D C   1 
ATOM   4307 O O   . SER D 4 153 ? 5.772  -33.679 -57.860 1.00 58.64  ?  152 SER D O   1 
ATOM   4308 C CB  . SER D 4 153 ? 2.994  -33.341 -56.816 1.00 56.98  ?  152 SER D CB  1 
ATOM   4309 O OG  . SER D 4 153 ? 3.057  -34.757 -56.711 1.00 68.20  ?  152 SER D OG  1 
ATOM   4310 N N   . ASP D 4 154 ? 4.707  -34.405 -59.695 1.00 56.42  ?  153 ASP D N   1 
ATOM   4311 C CA  . ASP D 4 154 ? 5.884  -35.079 -60.226 1.00 55.48  ?  153 ASP D CA  1 
ATOM   4312 C C   . ASP D 4 154 ? 6.513  -34.322 -61.384 1.00 48.65  ?  153 ASP D C   1 
ATOM   4313 O O   . ASP D 4 154 ? 7.398  -34.857 -62.060 1.00 47.46  ?  153 ASP D O   1 
ATOM   4314 C CB  . ASP D 4 154 ? 5.541  -36.503 -60.650 1.00 58.98  ?  153 ASP D CB  1 
ATOM   4315 C CG  . ASP D 4 154 ? 5.519  -37.446 -59.478 1.00 64.39  ?  153 ASP D CG  1 
ATOM   4316 O OD1 . ASP D 4 154 ? 6.582  -37.615 -58.833 1.00 64.33  ?  153 ASP D OD1 1 
ATOM   4317 O OD2 . ASP D 4 154 ? 4.433  -37.991 -59.186 1.00 68.36  -1 153 ASP D OD2 1 
ATOM   4318 N N   . VAL D 4 155 ? 6.073  -33.094 -61.626 1.00 44.65  ?  154 VAL D N   1 
ATOM   4319 C CA  . VAL D 4 155 ? 6.683  -32.205 -62.605 1.00 46.37  ?  154 VAL D CA  1 
ATOM   4320 C C   . VAL D 4 155 ? 7.150  -30.968 -61.852 1.00 40.25  ?  154 VAL D C   1 
ATOM   4321 O O   . VAL D 4 155 ? 6.372  -30.363 -61.106 1.00 45.80  ?  154 VAL D O   1 
ATOM   4322 C CB  . VAL D 4 155 ? 5.696  -31.828 -63.730 1.00 46.76  ?  154 VAL D CB  1 
ATOM   4323 C CG1 . VAL D 4 155 ? 6.279  -30.753 -64.629 1.00 40.43  ?  154 VAL D CG1 1 
ATOM   4324 C CG2 . VAL D 4 155 ? 5.311  -33.062 -64.542 1.00 47.41  ?  154 VAL D CG2 1 
ATOM   4325 N N   . TYR D 4 156 ? 8.405  -30.587 -62.048 1.00 39.03  ?  155 TYR D N   1 
ATOM   4326 C CA  . TYR D 4 156 ? 8.982  -29.450 -61.339 1.00 38.77  ?  155 TYR D CA  1 
ATOM   4327 C C   . TYR D 4 156 ? 9.170  -28.292 -62.306 1.00 32.85  ?  155 TYR D C   1 
ATOM   4328 O O   . TYR D 4 156 ? 9.756  -28.466 -63.380 1.00 34.15  ?  155 TYR D O   1 
ATOM   4329 C CB  . TYR D 4 156 ? 10.312 -29.842 -60.685 1.00 34.78  ?  155 TYR D CB  1 
ATOM   4330 C CG  . TYR D 4 156 ? 10.159 -31.043 -59.778 1.00 37.15  ?  155 TYR D CG  1 
ATOM   4331 C CD1 . TYR D 4 156 ? 9.525  -30.923 -58.553 1.00 36.32  ?  155 TYR D CD1 1 
ATOM   4332 C CD2 . TYR D 4 156 ? 10.617 -32.301 -60.167 1.00 43.05  ?  155 TYR D CD2 1 
ATOM   4333 C CE1 . TYR D 4 156 ? 9.370  -32.009 -57.719 1.00 43.53  ?  155 TYR D CE1 1 
ATOM   4334 C CE2 . TYR D 4 156 ? 10.456 -33.407 -59.340 1.00 45.42  ?  155 TYR D CE2 1 
ATOM   4335 C CZ  . TYR D 4 156 ? 9.827  -33.246 -58.123 1.00 44.92  ?  155 TYR D CZ  1 
ATOM   4336 O OH  . TYR D 4 156 ? 9.652  -34.304 -57.286 1.00 46.93  ?  155 TYR D OH  1 
ATOM   4337 N N   . ILE D 4 157 ? 8.679  -27.115 -61.920 1.00 33.31  ?  156 ILE D N   1 
ATOM   4338 C CA  . ILE D 4 157 ? 8.760  -25.925 -62.753 1.00 33.60  ?  156 ILE D CA  1 
ATOM   4339 C C   . ILE D 4 157 ? 9.190  -24.757 -61.877 1.00 38.33  ?  156 ILE D C   1 
ATOM   4340 O O   . ILE D 4 157 ? 8.499  -24.423 -60.909 1.00 34.96  ?  156 ILE D O   1 
ATOM   4341 C CB  . ILE D 4 157 ? 7.420  -25.597 -63.432 1.00 40.18  ?  156 ILE D CB  1 
ATOM   4342 C CG1 . ILE D 4 157 ? 6.903  -26.793 -64.224 1.00 41.88  ?  156 ILE D CG1 1 
ATOM   4343 C CG2 . ILE D 4 157 ? 7.570  -24.388 -64.330 1.00 30.56  ?  156 ILE D CG2 1 
ATOM   4344 C CD1 . ILE D 4 157 ? 5.573  -26.511 -64.939 1.00 40.06  ?  156 ILE D CD1 1 
ATOM   4345 N N   . THR D 4 158 ? 10.305 -24.119 -62.232 1.00 37.98  ?  157 THR D N   1 
ATOM   4346 C CA  . THR D 4 158 ? 10.819 -22.971 -61.500 1.00 37.99  ?  157 THR D CA  1 
ATOM   4347 C C   . THR D 4 158 ? 10.075 -21.691 -61.880 1.00 37.68  ?  157 THR D C   1 
ATOM   4348 O O   . THR D 4 158 ? 9.384  -21.619 -62.895 1.00 41.31  ?  157 THR D O   1 
ATOM   4349 C CB  . THR D 4 158 ? 12.303 -22.764 -61.792 1.00 35.15  ?  157 THR D CB  1 
ATOM   4350 O OG1 . THR D 4 158 ? 12.445 -22.224 -63.113 1.00 34.46  ?  157 THR D OG1 1 
ATOM   4351 C CG2 . THR D 4 158 ? 13.082 -24.069 -61.703 1.00 34.16  ?  157 THR D CG2 1 
ATOM   4352 N N   . ASP D 4 159 ? 10.251 -20.655 -61.060 1.00 38.64  ?  158 ASP D N   1 
ATOM   4353 C CA  . ASP D 4 159 ? 9.860  -19.307 -61.458 1.00 39.32  ?  158 ASP D CA  1 
ATOM   4354 C C   . ASP D 4 159 ? 10.721 -18.835 -62.629 1.00 36.66  ?  158 ASP D C   1 
ATOM   4355 O O   . ASP D 4 159 ? 11.794 -19.389 -62.902 1.00 33.95  ?  158 ASP D O   1 
ATOM   4356 C CB  . ASP D 4 159 ? 10.029 -18.314 -60.298 1.00 47.50  ?  158 ASP D CB  1 
ATOM   4357 C CG  . ASP D 4 159 ? 9.293  -18.729 -59.026 1.00 58.60  ?  158 ASP D CG  1 
ATOM   4358 O OD1 . ASP D 4 159 ? 8.451  -19.661 -59.081 1.00 58.98  -1 158 ASP D OD1 1 
ATOM   4359 O OD2 . ASP D 4 159 ? 9.557  -18.099 -57.966 1.00 56.46  ?  158 ASP D OD2 1 
ATOM   4360 N N   . LYS D 4 160 ? 10.249 -17.793 -63.322 1.00 39.77  ?  159 LYS D N   1 
ATOM   4361 C CA  . LYS D 4 160 ? 11.071 -17.189 -64.365 1.00 38.47  ?  159 LYS D CA  1 
ATOM   4362 C C   . LYS D 4 160 ? 12.228 -16.432 -63.730 1.00 38.67  ?  159 LYS D C   1 
ATOM   4363 O O   . LYS D 4 160 ? 12.173 -16.025 -62.568 1.00 37.79  ?  159 LYS D O   1 
ATOM   4364 C CB  . LYS D 4 160 ? 10.279 -16.235 -65.262 1.00 32.01  ?  159 LYS D CB  1 
ATOM   4365 C CG  . LYS D 4 160 ? 9.543  -15.176 -64.523 1.00 43.32  ?  159 LYS D CG  1 
ATOM   4366 C CD  . LYS D 4 160 ? 8.411  -14.623 -65.372 1.00 50.80  ?  159 LYS D CD  1 
ATOM   4367 C CE  . LYS D 4 160 ? 8.579  -13.137 -65.553 1.00 51.56  ?  159 LYS D CE  1 
ATOM   4368 N NZ  . LYS D 4 160 ? 7.292  -12.454 -65.810 1.00 54.76  ?  159 LYS D NZ  1 
ATOM   4369 N N   . CYS D 4 161 ? 13.275 -16.239 -64.527 1.00 33.87  ?  160 CYS D N   1 
ATOM   4370 C CA  . CYS D 4 161 ? 14.575 -15.763 -64.080 1.00 34.00  ?  160 CYS D CA  1 
ATOM   4371 C C   . CYS D 4 161 ? 15.136 -14.894 -65.191 1.00 31.30  ?  160 CYS D C   1 
ATOM   4372 O O   . CYS D 4 161 ? 15.241 -15.350 -66.337 1.00 32.19  ?  160 CYS D O   1 
ATOM   4373 C CB  . CYS D 4 161 ? 15.506 -16.966 -63.854 1.00 38.25  ?  160 CYS D CB  1 
ATOM   4374 S SG  . CYS D 4 161 ? 16.664 -16.958 -62.563 1.00 46.94  ?  160 CYS D SG  1 
ATOM   4375 N N   . VAL D 4 162 ? 15.561 -13.696 -64.849 1.00 27.57  ?  161 VAL D N   1 
ATOM   4376 C CA  . VAL D 4 162 ? 16.199 -12.797 -65.803 1.00 27.21  ?  161 VAL D CA  1 
ATOM   4377 C C   . VAL D 4 162 ? 17.705 -12.979 -65.710 1.00 31.29  ?  161 VAL D C   1 
ATOM   4378 O O   . VAL D 4 162 ? 18.286 -12.804 -64.631 1.00 31.14  ?  161 VAL D O   1 
ATOM   4379 C CB  . VAL D 4 162 ? 15.823 -11.336 -65.516 1.00 29.55  ?  161 VAL D CB  1 
ATOM   4380 C CG1 . VAL D 4 162 ? 16.368 -10.463 -66.613 1.00 31.92  ?  161 VAL D CG1 1 
ATOM   4381 C CG2 . VAL D 4 162 ? 14.318 -11.207 -65.379 1.00 33.24  ?  161 VAL D CG2 1 
ATOM   4382 N N   . LEU D 4 163 ? 18.341 -13.310 -66.831 1.00 25.53  ?  162 LEU D N   1 
ATOM   4383 C CA  . LEU D 4 163 ? 19.791 -13.283 -66.915 1.00 27.34  ?  162 LEU D CA  1 
ATOM   4384 C C   . LEU D 4 163 ? 20.200 -12.114 -67.788 1.00 29.31  ?  162 LEU D C   1 
ATOM   4385 O O   . LEU D 4 163 ? 19.418 -11.638 -68.612 1.00 30.95  ?  162 LEU D O   1 
ATOM   4386 C CB  . LEU D 4 163 ? 20.369 -14.601 -67.446 1.00 28.43  ?  162 LEU D CB  1 
ATOM   4387 C CG  . LEU D 4 163 ? 20.151 -15.132 -68.880 1.00 26.26  ?  162 LEU D CG  1 
ATOM   4388 C CD1 . LEU D 4 163 ? 21.093 -14.477 -69.856 1.00 23.14  ?  162 LEU D CD1 1 
ATOM   4389 C CD2 . LEU D 4 163 ? 20.391 -16.627 -68.885 1.00 29.99  ?  162 LEU D CD2 1 
ATOM   4390 N N   . ASP D 4 164 ? 21.413 -11.617 -67.570 1.00 29.45  ?  163 ASP D N   1 
ATOM   4391 C CA  . ASP D 4 164 ? 21.888 -10.411 -68.242 1.00 29.12  ?  163 ASP D CA  1 
ATOM   4392 C C   . ASP D 4 164 ? 23.274 -10.709 -68.787 1.00 31.97  ?  163 ASP D C   1 
ATOM   4393 O O   . ASP D 4 164 ? 24.231 -10.830 -68.012 1.00 31.35  ?  163 ASP D O   1 
ATOM   4394 C CB  . ASP D 4 164 ? 21.896 -9.221  -67.261 1.00 29.00  ?  163 ASP D CB  1 
ATOM   4395 C CG  . ASP D 4 164 ? 22.599 -7.967  -67.818 1.00 37.99  ?  163 ASP D CG  1 
ATOM   4396 O OD1 . ASP D 4 164 ? 23.004 -7.955  -69.005 1.00 35.33  ?  163 ASP D OD1 1 
ATOM   4397 O OD2 . ASP D 4 164 ? 22.756 -6.988  -67.045 1.00 38.30  -1 163 ASP D OD2 1 
ATOM   4398 N N   . MET D 4 165 ? 23.379 -10.855 -70.112 1.00 27.96  ?  164 MET D N   1 
ATOM   4399 C CA  . MET D 4 165 ? 24.670 -11.036 -70.777 1.00 31.28  ?  164 MET D CA  1 
ATOM   4400 C C   . MET D 4 165 ? 25.280 -9.652  -70.948 1.00 37.79  ?  164 MET D C   1 
ATOM   4401 O O   . MET D 4 165 ? 24.977 -8.934  -71.904 1.00 37.58  ?  164 MET D O   1 
ATOM   4402 C CB  . MET D 4 165 ? 24.504 -11.783 -72.100 1.00 32.57  ?  164 MET D CB  1 
ATOM   4403 C CG  . MET D 4 165 ? 23.805 -13.153 -71.915 1.00 32.30  ?  164 MET D CG  1 
ATOM   4404 S SD  . MET D 4 165 ? 23.536 -14.079 -73.443 1.00 31.24  ?  164 MET D SD  1 
ATOM   4405 C CE  . MET D 4 165 ? 25.245 -14.406 -73.910 1.00 27.26  ?  164 MET D CE  1 
ATOM   4406 N N   . ARG D 4 166 ? 26.137 -9.267  -69.996 1.00 33.35  ?  165 ARG D N   1 
ATOM   4407 C CA  . ARG D 4 166 ? 26.471 -7.856  -69.829 1.00 36.66  ?  165 ARG D CA  1 
ATOM   4408 C C   . ARG D 4 166 ? 27.226 -7.315  -71.032 1.00 37.81  ?  165 ARG D C   1 
ATOM   4409 O O   . ARG D 4 166 ? 26.897 -6.237  -71.534 1.00 41.86  ?  165 ARG D O   1 
ATOM   4410 C CB  . ARG D 4 166 ? 27.277 -7.663  -68.546 1.00 37.46  ?  165 ARG D CB  1 
ATOM   4411 C CG  . ARG D 4 166 ? 26.462 -7.806  -67.298 1.00 41.55  ?  165 ARG D CG  1 
ATOM   4412 C CD  . ARG D 4 166 ? 27.349 -7.753  -66.058 1.00 46.38  ?  165 ARG D CD  1 
ATOM   4413 N NE  . ARG D 4 166 ? 26.813 -8.623  -65.017 1.00 47.08  ?  165 ARG D NE  1 
ATOM   4414 C CZ  . ARG D 4 166 ? 27.458 -8.982  -63.907 1.00 47.70  ?  165 ARG D CZ  1 
ATOM   4415 N NH1 . ARG D 4 166 ? 28.686 -8.540  -63.671 1.00 50.75  ?  165 ARG D NH1 1 
ATOM   4416 N NH2 . ARG D 4 166 ? 26.865 -9.784  -63.021 1.00 44.33  ?  165 ARG D NH2 1 
ATOM   4417 N N   . SER D 4 167 ? 28.216 -8.069  -71.528 1.00 36.87  ?  166 SER D N   1 
ATOM   4418 C CA  . SER D 4 167 ? 29.018 -7.627  -72.668 1.00 41.30  ?  166 SER D CA  1 
ATOM   4419 C C   . SER D 4 167 ? 28.176 -7.341  -73.896 1.00 42.99  ?  166 SER D C   1 
ATOM   4420 O O   . SER D 4 167 ? 28.572 -6.520  -74.731 1.00 42.68  ?  166 SER D O   1 
ATOM   4421 C CB  . SER D 4 167 ? 30.056 -8.673  -73.053 1.00 39.82  ?  166 SER D CB  1 
ATOM   4422 O OG  . SER D 4 167 ? 30.577 -9.321  -71.921 1.00 60.74  ?  166 SER D OG  1 
ATOM   4423 N N   . MET D 4 168 ? 27.051 -8.031  -74.053 1.00 43.57  ?  167 MET D N   1 
ATOM   4424 C CA  . MET D 4 168 ? 26.191 -7.883  -75.220 1.00 48.09  ?  167 MET D CA  1 
ATOM   4425 C C   . MET D 4 168 ? 24.961 -7.019  -74.950 1.00 41.86  ?  167 MET D C   1 
ATOM   4426 O O   . MET D 4 168 ? 24.162 -6.794  -75.864 1.00 44.94  ?  167 MET D O   1 
ATOM   4427 C CB  . MET D 4 168 ? 25.758 -9.266  -75.722 1.00 45.67  ?  167 MET D CB  1 
ATOM   4428 C CG  . MET D 4 168 ? 26.901 -10.124 -76.228 1.00 49.25  ?  167 MET D CG  1 
ATOM   4429 S SD  . MET D 4 168 ? 26.400 -11.799 -76.726 1.00 61.47  ?  167 MET D SD  1 
ATOM   4430 C CE  . MET D 4 168 ? 25.879 -11.477 -78.425 1.00 53.71  ?  167 MET D CE  1 
ATOM   4431 N N   . ASP D 4 169 ? 24.784 -6.530  -73.728 1.00 39.26  ?  168 ASP D N   1 
ATOM   4432 C CA  . ASP D 4 169 ? 23.605 -5.724  -73.395 1.00 46.06  ?  168 ASP D CA  1 
ATOM   4433 C C   . ASP D 4 169 ? 22.310 -6.466  -73.739 1.00 45.36  ?  168 ASP D C   1 
ATOM   4434 O O   . ASP D 4 169 ? 21.353 -5.883  -74.254 1.00 40.70  ?  168 ASP D O   1 
ATOM   4435 C CB  . ASP D 4 169 ? 23.650 -4.369  -74.105 1.00 48.22  ?  168 ASP D CB  1 
ATOM   4436 C CG  . ASP D 4 169 ? 22.493 -3.465  -73.709 1.00 57.23  ?  168 ASP D CG  1 
ATOM   4437 O OD1 . ASP D 4 169 ? 21.953 -3.671  -72.596 1.00 55.97  -1 168 ASP D OD1 1 
ATOM   4438 O OD2 . ASP D 4 169 ? 22.121 -2.574  -74.519 1.00 61.68  ?  168 ASP D OD2 1 
ATOM   4439 N N   . PHE D 4 170 ? 22.270 -7.756  -73.423 1.00 39.24  ?  169 PHE D N   1 
ATOM   4440 C CA  . PHE D 4 170 ? 21.184 -8.640  -73.813 1.00 32.64  ?  169 PHE D CA  1 
ATOM   4441 C C   . PHE D 4 170 ? 20.625 -9.304  -72.562 1.00 34.15  ?  169 PHE D C   1 
ATOM   4442 O O   . PHE D 4 170 ? 21.365 -9.972  -71.833 1.00 32.94  ?  169 PHE D O   1 
ATOM   4443 C CB  . PHE D 4 170 ? 21.695 -9.689  -74.803 1.00 32.32  ?  169 PHE D CB  1 
ATOM   4444 C CG  . PHE D 4 170 ? 20.684 -10.722 -75.163 1.00 31.49  ?  169 PHE D CG  1 
ATOM   4445 C CD1 . PHE D 4 170 ? 20.548 -11.874 -74.398 1.00 28.98  ?  169 PHE D CD1 1 
ATOM   4446 C CD2 . PHE D 4 170 ? 19.860 -10.548 -76.278 1.00 33.89  ?  169 PHE D CD2 1 
ATOM   4447 C CE1 . PHE D 4 170 ? 19.608 -12.846 -74.721 1.00 33.85  ?  169 PHE D CE1 1 
ATOM   4448 C CE2 . PHE D 4 170 ? 18.915 -11.521 -76.626 1.00 35.32  ?  169 PHE D CE2 1 
ATOM   4449 C CZ  . PHE D 4 170 ? 18.795 -12.687 -75.846 1.00 33.28  ?  169 PHE D CZ  1 
ATOM   4450 N N   . LYS D 4 171 ? 19.332 -9.124  -72.324 1.00 28.17  ?  170 LYS D N   1 
ATOM   4451 C CA  . LYS D 4 171 ? 18.610 -9.715  -71.207 1.00 30.79  ?  170 LYS D CA  1 
ATOM   4452 C C   . LYS D 4 171 ? 17.646 -10.776 -71.722 1.00 31.63  ?  170 LYS D C   1 
ATOM   4453 O O   . LYS D 4 171 ? 17.062 -10.620 -72.795 1.00 32.49  ?  170 LYS D O   1 
ATOM   4454 C CB  . LYS D 4 171 ? 17.811 -8.649  -70.448 1.00 32.73  ?  170 LYS D CB  1 
ATOM   4455 C CG  . LYS D 4 171 ? 18.647 -7.725  -69.537 1.00 42.46  ?  170 LYS D CG  1 
ATOM   4456 C CD  . LYS D 4 171 ? 19.547 -6.811  -70.351 1.00 37.50  ?  170 LYS D CD  1 
ATOM   4457 C CE  . LYS D 4 171 ? 20.132 -5.713  -69.465 1.00 47.07  ?  170 LYS D CE  1 
ATOM   4458 N NZ  . LYS D 4 171 ? 21.579 -5.500  -69.769 1.00 48.13  ?  170 LYS D NZ  1 
ATOM   4459 N N   . SER D 4 172 ? 17.443 -11.846 -70.962 1.00 30.14  ?  171 SER D N   1 
ATOM   4460 C CA  . SER D 4 172 ? 16.391 -12.756 -71.376 1.00 30.71  ?  171 SER D CA  1 
ATOM   4461 C C   . SER D 4 172 ? 15.801 -13.450 -70.166 1.00 36.42  ?  171 SER D C   1 
ATOM   4462 O O   . SER D 4 172 ? 16.483 -13.666 -69.154 1.00 31.09  ?  171 SER D O   1 
ATOM   4463 C CB  . SER D 4 172 ? 16.895 -13.775 -72.416 1.00 25.92  ?  171 SER D CB  1 
ATOM   4464 O OG  . SER D 4 172 ? 18.038 -14.500 -71.966 1.00 30.76  ?  171 SER D OG  1 
ATOM   4465 N N   . ASN D 4 173 ? 14.510 -13.775 -70.281 1.00 32.50  ?  172 ASN D N   1 
ATOM   4466 C CA  . ASN D 4 173 ? 13.770 -14.506 -69.260 1.00 30.44  ?  172 ASN D CA  1 
ATOM   4467 C C   . ASN D 4 173 ? 13.812 -16.000 -69.541 1.00 31.49  ?  172 ASN D C   1 
ATOM   4468 O O   . ASN D 4 173 ? 13.876 -16.427 -70.695 1.00 31.20  ?  172 ASN D O   1 
ATOM   4469 C CB  . ASN D 4 173 ? 12.305 -14.054 -69.208 1.00 32.09  ?  172 ASN D CB  1 
ATOM   4470 C CG  . ASN D 4 173 ? 12.156 -12.602 -68.874 1.00 37.43  ?  172 ASN D CG  1 
ATOM   4471 O OD1 . ASN D 4 173 ? 12.614 -12.126 -67.815 1.00 34.32  ?  172 ASN D OD1 1 
ATOM   4472 N ND2 . ASN D 4 173 ? 11.500 -11.871 -69.766 1.00 34.01  ?  172 ASN D ND2 1 
ATOM   4473 N N   . SER D 4 174 ? 13.745 -16.805 -68.480 1.00 28.91  ?  173 SER D N   1 
ATOM   4474 C CA  . SER D 4 174 ? 13.665 -18.248 -68.683 1.00 25.81  ?  173 SER D CA  1 
ATOM   4475 C C   . SER D 4 174 ? 13.055 -18.910 -67.455 1.00 34.63  ?  173 SER D C   1 
ATOM   4476 O O   . SER D 4 174 ? 12.989 -18.331 -66.367 1.00 29.06  ?  173 SER D O   1 
ATOM   4477 C CB  . SER D 4 174 ? 15.036 -18.882 -68.989 1.00 29.68  ?  173 SER D CB  1 
ATOM   4478 O OG  . SER D 4 174 ? 15.803 -19.035 -67.806 1.00 34.01  ?  173 SER D OG  1 
ATOM   4479 N N   . ALA D 4 175 ? 12.581 -20.133 -67.669 1.00 31.20  ?  174 ALA D N   1 
ATOM   4480 C CA  . ALA D 4 175 ? 12.080 -20.990 -66.614 1.00 32.36  ?  174 ALA D CA  1 
ATOM   4481 C C   . ALA D 4 175 ? 12.473 -22.400 -66.997 1.00 31.50  ?  174 ALA D C   1 
ATOM   4482 O O   . ALA D 4 175 ? 12.697 -22.696 -68.175 1.00 31.33  ?  174 ALA D O   1 
ATOM   4483 C CB  . ALA D 4 175 ? 10.563 -20.855 -66.438 1.00 37.55  ?  174 ALA D CB  1 
ATOM   4484 N N   . VAL D 4 176 ? 12.572 -23.269 -66.002 1.00 27.54  ?  175 VAL D N   1 
ATOM   4485 C CA  . VAL D 4 176 ? 13.083 -24.615 -66.226 1.00 31.94  ?  175 VAL D CA  1 
ATOM   4486 C C   . VAL D 4 176 ? 12.040 -25.609 -65.746 1.00 33.65  ?  175 VAL D C   1 
ATOM   4487 O O   . VAL D 4 176 ? 11.352 -25.373 -64.752 1.00 34.42  ?  175 VAL D O   1 
ATOM   4488 C CB  . VAL D 4 176 ? 14.438 -24.843 -65.510 1.00 34.77  ?  175 VAL D CB  1 
ATOM   4489 C CG1 . VAL D 4 176 ? 14.912 -26.282 -65.688 1.00 34.36  ?  175 VAL D CG1 1 
ATOM   4490 C CG2 . VAL D 4 176 ? 15.481 -23.854 -66.026 1.00 30.63  ?  175 VAL D CG2 1 
ATOM   4491 N N   . ALA D 4 177 ? 11.931 -26.734 -66.445 1.00 27.26  ?  176 ALA D N   1 
ATOM   4492 C CA  . ALA D 4 177 ? 11.002 -27.769 -66.016 1.00 33.78  ?  176 ALA D CA  1 
ATOM   4493 C C   . ALA D 4 177 ? 11.635 -29.123 -66.218 1.00 31.13  ?  176 ALA D C   1 
ATOM   4494 O O   . ALA D 4 177 ? 12.353 -29.331 -67.197 1.00 33.19  ?  176 ALA D O   1 
ATOM   4495 C CB  . ALA D 4 177 ? 9.683  -27.695 -66.784 1.00 34.91  ?  176 ALA D CB  1 
ATOM   4496 N N   . TRP D 4 178 ? 11.384 -30.040 -65.287 1.00 32.90  ?  177 TRP D N   1 
ATOM   4497 C CA  . TRP D 4 178 ? 11.902 -31.394 -65.421 1.00 33.50  ?  177 TRP D CA  1 
ATOM   4498 C C   . TRP D 4 178 ? 11.011 -32.377 -64.666 1.00 41.43  ?  177 TRP D C   1 
ATOM   4499 O O   . TRP D 4 178 ? 10.103 -31.992 -63.921 1.00 36.85  ?  177 TRP D O   1 
ATOM   4500 C CB  . TRP D 4 178 ? 13.353 -31.500 -64.939 1.00 37.10  ?  177 TRP D CB  1 
ATOM   4501 C CG  . TRP D 4 178 ? 13.520 -31.373 -63.452 1.00 37.09  ?  177 TRP D CG  1 
ATOM   4502 C CD1 . TRP D 4 178 ? 13.605 -32.390 -62.541 1.00 36.71  ?  177 TRP D CD1 1 
ATOM   4503 C CD2 . TRP D 4 178 ? 13.635 -30.164 -62.717 1.00 31.23  ?  177 TRP D CD2 1 
ATOM   4504 N NE1 . TRP D 4 178 ? 13.758 -31.879 -61.277 1.00 40.86  ?  177 TRP D NE1 1 
ATOM   4505 C CE2 . TRP D 4 178 ? 13.787 -30.513 -61.359 1.00 38.38  ?  177 TRP D CE2 1 
ATOM   4506 C CE3 . TRP D 4 178 ? 13.642 -28.818 -63.071 1.00 34.63  ?  177 TRP D CE3 1 
ATOM   4507 C CZ2 . TRP D 4 178 ? 13.931 -29.560 -60.360 1.00 32.64  ?  177 TRP D CZ2 1 
ATOM   4508 C CZ3 . TRP D 4 178 ? 13.785 -27.873 -62.071 1.00 32.66  ?  177 TRP D CZ3 1 
ATOM   4509 C CH2 . TRP D 4 178 ? 13.924 -28.251 -60.738 1.00 29.95  ?  177 TRP D CH2 1 
ATOM   4510 N N   . SER D 4 179 ? 11.284 -33.665 -64.871 1.00 43.01  ?  178 SER D N   1 
ATOM   4511 C CA  . SER D 4 179 ? 10.437 -34.682 -64.270 1.00 45.99  ?  178 SER D CA  1 
ATOM   4512 C C   . SER D 4 179 ? 11.082 -36.043 -64.457 1.00 44.15  ?  178 SER D C   1 
ATOM   4513 O O   . SER D 4 179 ? 11.909 -36.242 -65.348 1.00 54.85  ?  178 SER D O   1 
ATOM   4514 C CB  . SER D 4 179 ? 9.030  -34.658 -64.877 1.00 45.20  ?  178 SER D CB  1 
ATOM   4515 O OG  . SER D 4 179 ? 8.222  -35.696 -64.339 1.00 53.86  ?  178 SER D OG  1 
ATOM   4516 N N   . ASN D 4 180 ? 10.678 -37.002 -63.653 1.00 55.30  ?  179 ASN D N   1 
ATOM   4517 C CA  . ASN D 4 180 ? 11.208 -38.374 -63.811 1.00 61.15  ?  179 ASN D CA  1 
ATOM   4518 C C   . ASN D 4 180 ? 10.144 -39.228 -64.511 1.00 63.51  ?  179 ASN D C   1 
ATOM   4519 O O   . ASN D 4 180 ? 10.455 -40.329 -64.918 1.00 65.86  ?  179 ASN D O   1 
ATOM   4520 C CB  . ASN D 4 180 ? 11.579 -38.979 -62.458 1.00 61.82  ?  179 ASN D CB  1 
ATOM   4521 C CG  . ASN D 4 180 ? 12.524 -38.127 -61.630 1.00 75.70  ?  179 ASN D CG  1 
ATOM   4522 O OD1 . ASN D 4 180 ? 12.201 -37.747 -60.507 1.00 75.74  ?  179 ASN D OD1 1 
ATOM   4523 N ND2 . ASN D 4 180 ? 13.692 -37.822 -62.160 1.00 71.56  ?  179 ASN D ND2 1 
ATOM   4524 N N   . LYS D 4 181 ? 8.941  -38.694 -64.703 1.00 66.13  ?  180 LYS D N   1 
ATOM   4525 C CA  . LYS D 4 181 ? 7.841  -39.527 -65.248 1.00 63.60  ?  180 LYS D CA  1 
ATOM   4526 C C   . LYS D 4 181 ? 7.964  -39.846 -66.741 1.00 75.05  ?  180 LYS D C   1 
ATOM   4527 O O   . LYS D 4 181 ? 8.375  -39.000 -67.509 1.00 69.63  ?  180 LYS D O   1 
ATOM   4528 C CB  . LYS D 4 181 ? 6.457  -39.176 -64.699 1.00 56.60  ?  180 LYS D CB  1 
ATOM   4529 C CG  . LYS D 4 181 ? 5.895  -37.812 -65.004 1.00 62.68  ?  180 LYS D CG  1 
ATOM   4530 C CD  . LYS D 4 181 ? 4.413  -37.863 -65.170 1.00 63.99  ?  180 LYS D CD  1 
ATOM   4531 C CE  . LYS D 4 181 ? 3.636  -37.260 -64.025 1.00 64.01  ?  180 LYS D CE  1 
ATOM   4532 N NZ  . LYS D 4 181 ? 3.204  -35.891 -64.364 1.00 64.26  ?  180 LYS D NZ  1 
ATOM   4533 N N   . SER D 4 182 ? 7.558  -41.079 -67.060 1.00 80.95  ?  181 SER D N   1 
ATOM   4534 C CA  . SER D 4 182 ? 7.561  -41.787 -68.367 1.00 75.82  ?  181 SER D CA  1 
ATOM   4535 C C   . SER D 4 182 ? 7.245  -40.904 -69.566 1.00 68.79  ?  181 SER D C   1 
ATOM   4536 O O   . SER D 4 182 ? 8.065  -40.877 -70.461 1.00 64.29  ?  181 SER D O   1 
ATOM   4537 C CB  . SER D 4 182 ? 6.646  -42.981 -68.338 1.00 77.91  ?  181 SER D CB  1 
ATOM   4538 O OG  . SER D 4 182 ? 5.509  -42.742 -67.523 1.00 81.19  ?  181 SER D OG  1 
ATOM   4539 N N   . ASP D 4 183 ? 6.104  -40.231 -69.562 1.00 66.65  ?  182 ASP D N   1 
ATOM   4540 C CA  . ASP D 4 183 ? 5.674  -39.476 -70.760 1.00 64.80  ?  182 ASP D CA  1 
ATOM   4541 C C   . ASP D 4 183 ? 5.901  -37.977 -70.617 1.00 66.34  ?  182 ASP D C   1 
ATOM   4542 O O   . ASP D 4 183 ? 5.167  -37.211 -71.259 1.00 61.50  ?  182 ASP D O   1 
ATOM   4543 C CB  . ASP D 4 183 ? 4.174  -39.656 -70.968 1.00 77.71  ?  182 ASP D CB  1 
ATOM   4544 N N   . PHE D 4 184 ? 6.831  -37.564 -69.768 1.00 61.51  ?  183 PHE D N   1 
ATOM   4545 C CA  . PHE D 4 184 ? 7.075  -36.108 -69.675 1.00 55.05  ?  183 PHE D CA  1 
ATOM   4546 C C   . PHE D 4 184 ? 7.779  -35.669 -70.963 1.00 49.53  ?  183 PHE D C   1 
ATOM   4547 O O   . PHE D 4 184 ? 8.725  -36.299 -71.334 1.00 49.50  ?  183 PHE D O   1 
ATOM   4548 C CB  . PHE D 4 184 ? 7.823  -35.754 -68.387 1.00 52.75  ?  183 PHE D CB  1 
ATOM   4549 C CG  . PHE D 4 184 ? 8.123  -34.293 -68.263 1.00 43.24  ?  183 PHE D CG  1 
ATOM   4550 C CD1 . PHE D 4 184 ? 7.145  -33.410 -67.888 1.00 39.95  ?  183 PHE D CD1 1 
ATOM   4551 C CD2 . PHE D 4 184 ? 9.372  -33.801 -68.570 1.00 45.12  ?  183 PHE D CD2 1 
ATOM   4552 C CE1 . PHE D 4 184 ? 7.417  -32.065 -67.803 1.00 36.64  ?  183 PHE D CE1 1 
ATOM   4553 C CE2 . PHE D 4 184 ? 9.644  -32.456 -68.469 1.00 39.77  ?  183 PHE D CE2 1 
ATOM   4554 C CZ  . PHE D 4 184 ? 8.659  -31.594 -68.099 1.00 34.39  ?  183 PHE D CZ  1 
ATOM   4555 N N   . ALA D 4 185 ? 7.260  -34.651 -71.631 1.00 46.02  ?  184 ALA D N   1 
ATOM   4556 C CA  . ALA D 4 185 ? 7.881  -34.132 -72.840 1.00 43.06  ?  184 ALA D CA  1 
ATOM   4557 C C   . ALA D 4 185 ? 7.813  -32.614 -72.838 1.00 43.56  ?  184 ALA D C   1 
ATOM   4558 O O   . ALA D 4 185 ? 6.877  -32.025 -72.288 1.00 44.39  ?  184 ALA D O   1 
ATOM   4559 C CB  . ALA D 4 185 ? 7.194  -34.670 -74.103 1.00 53.92  ?  184 ALA D CB  1 
ATOM   4560 N N   . CYS D 4 186 ? 8.804  -31.982 -73.479 1.00 41.62  ?  185 CYS D N   1 
ATOM   4561 C CA  . CYS D 4 186 ? 8.871  -30.522 -73.489 1.00 41.55  ?  185 CYS D CA  1 
ATOM   4562 C C   . CYS D 4 186 ? 7.621  -29.903 -74.082 1.00 44.78  ?  185 CYS D C   1 
ATOM   4563 O O   . CYS D 4 186 ? 7.209  -28.810 -73.667 1.00 43.79  ?  185 CYS D O   1 
ATOM   4564 C CB  . CYS D 4 186 ? 10.118 -30.071 -74.244 1.00 40.71  ?  185 CYS D CB  1 
ATOM   4565 S SG  . CYS D 4 186 ? 11.637 -30.563 -73.311 1.00 51.46  ?  185 CYS D SG  1 
ATOM   4566 N N   . ALA D 4 187 ? 7.012  -30.585 -75.057 1.00 52.49  ?  186 ALA D N   1 
ATOM   4567 C CA  . ALA D 4 187 ? 5.802  -30.072 -75.688 1.00 45.73  ?  186 ALA D CA  1 
ATOM   4568 C C   . ALA D 4 187 ? 4.708  -29.835 -74.659 1.00 45.75  ?  186 ALA D C   1 
ATOM   4569 O O   . ALA D 4 187 ? 3.937  -28.875 -74.772 1.00 51.03  ?  186 ALA D O   1 
ATOM   4570 C CB  . ALA D 4 187 ? 5.333  -31.044 -76.776 1.00 49.47  ?  186 ALA D CB  1 
ATOM   4571 N N   . ASN D 4 188 ? 4.638  -30.684 -73.632 1.00 44.39  ?  187 ASN D N   1 
ATOM   4572 C CA  . ASN D 4 188 ? 3.631  -30.535 -72.584 1.00 48.30  ?  187 ASN D CA  1 
ATOM   4573 C C   . ASN D 4 188 ? 4.120  -29.784 -71.351 1.00 50.10  ?  187 ASN D C   1 
ATOM   4574 O O   . ASN D 4 188 ? 3.286  -29.332 -70.557 1.00 48.54  ?  187 ASN D O   1 
ATOM   4575 C CB  . ASN D 4 188 ? 3.131  -31.909 -72.118 1.00 49.87  ?  187 ASN D CB  1 
ATOM   4576 C CG  . ASN D 4 188 ? 2.602  -32.745 -73.245 1.00 54.88  ?  187 ASN D CG  1 
ATOM   4577 O OD1 . ASN D 4 188 ? 2.751  -33.972 -73.248 1.00 59.22  ?  187 ASN D OD1 1 
ATOM   4578 N ND2 . ASN D 4 188 ? 1.964  -32.095 -74.211 1.00 54.20  ?  187 ASN D ND2 1 
ATOM   4579 N N   . ALA D 4 189 ? 5.438  -29.662 -71.160 1.00 52.57  ?  188 ALA D N   1 
ATOM   4580 C CA  . ALA D 4 189 ? 5.991  -29.157 -69.903 1.00 45.97  ?  188 ALA D CA  1 
ATOM   4581 C C   . ALA D 4 189 ? 5.208  -27.968 -69.373 1.00 41.70  ?  188 ALA D C   1 
ATOM   4582 O O   . ALA D 4 189 ? 4.719  -27.985 -68.236 1.00 45.28  ?  188 ALA D O   1 
ATOM   4583 C CB  . ALA D 4 189 ? 7.469  -28.785 -70.096 1.00 40.20  ?  188 ALA D CB  1 
ATOM   4584 N N   . PHE D 4 190 ? 5.040  -26.936 -70.199 1.00 39.38  ?  189 PHE D N   1 
ATOM   4585 C CA  . PHE D 4 190 ? 4.490  -25.663 -69.747 1.00 44.03  ?  189 PHE D CA  1 
ATOM   4586 C C   . PHE D 4 190 ? 3.019  -25.483 -70.112 1.00 49.40  ?  189 PHE D C   1 
ATOM   4587 O O   . PHE D 4 190 ? 2.524  -24.348 -70.156 1.00 46.70  ?  189 PHE D O   1 
ATOM   4588 C CB  . PHE D 4 190 ? 5.340  -24.515 -70.290 1.00 41.62  ?  189 PHE D CB  1 
ATOM   4589 C CG  . PHE D 4 190 ? 6.792  -24.627 -69.895 1.00 45.02  ?  189 PHE D CG  1 
ATOM   4590 C CD1 . PHE D 4 190 ? 7.239  -24.132 -68.669 1.00 39.31  ?  189 PHE D CD1 1 
ATOM   4591 C CD2 . PHE D 4 190 ? 7.694  -25.299 -70.710 1.00 38.32  ?  189 PHE D CD2 1 
ATOM   4592 C CE1 . PHE D 4 190 ? 8.577  -24.258 -68.289 1.00 36.80  ?  189 PHE D CE1 1 
ATOM   4593 C CE2 . PHE D 4 190 ? 9.026  -25.435 -70.335 1.00 38.37  ?  189 PHE D CE2 1 
ATOM   4594 C CZ  . PHE D 4 190 ? 9.469  -24.909 -69.123 1.00 38.65  ?  189 PHE D CZ  1 
ATOM   4595 N N   . ASN D 4 191 ? 2.291  -26.590 -70.302 1.00 53.18  ?  190 ASN D N   1 
ATOM   4596 C CA  . ASN D 4 191 ? 0.879  -26.528 -70.683 1.00 56.80  ?  190 ASN D CA  1 
ATOM   4597 C C   . ASN D 4 191 ? -0.014 -25.924 -69.608 1.00 56.65  ?  190 ASN D C   1 
ATOM   4598 O O   . ASN D 4 191 ? -1.161 -25.581 -69.911 1.00 63.04  ?  190 ASN D O   1 
ATOM   4599 C CB  . ASN D 4 191 ? 0.367  -27.925 -71.045 1.00 52.90  ?  190 ASN D CB  1 
ATOM   4600 C CG  . ASN D 4 191 ? 0.633  -28.279 -72.506 1.00 53.69  ?  190 ASN D CG  1 
ATOM   4601 O OD1 . ASN D 4 191 ? 0.659  -27.406 -73.373 1.00 57.73  ?  190 ASN D OD1 1 
ATOM   4602 N ND2 . ASN D 4 191 ? 0.831  -29.566 -72.780 1.00 57.24  ?  190 ASN D ND2 1 
ATOM   4603 N N   . ASN D 4 192 ? 0.463  -25.790 -68.373 1.00 54.63  ?  191 ASN D N   1 
ATOM   4604 C CA  . ASN D 4 192 ? -0.307 -25.129 -67.333 1.00 52.31  ?  191 ASN D CA  1 
ATOM   4605 C C   . ASN D 4 192 ? -0.093 -23.618 -67.308 1.00 54.91  ?  191 ASN D C   1 
ATOM   4606 O O   . ASN D 4 192 ? -0.680 -22.933 -66.466 1.00 54.89  ?  191 ASN D O   1 
ATOM   4607 C CB  . ASN D 4 192 ? 0.024  -25.738 -65.966 1.00 60.98  ?  191 ASN D CB  1 
ATOM   4608 C CG  . ASN D 4 192 ? -1.178 -25.795 -65.063 1.00 65.54  ?  191 ASN D CG  1 
ATOM   4609 O OD1 . ASN D 4 192 ? -2.060 -26.641 -65.234 1.00 70.32  ?  191 ASN D OD1 1 
ATOM   4610 N ND2 . ASN D 4 192 ? -1.242 -24.872 -64.110 1.00 69.64  ?  191 ASN D ND2 1 
ATOM   4611 N N   . SER D 4 193 ? 0.715  -23.081 -68.214 1.00 52.38  ?  192 SER D N   1 
ATOM   4612 C CA  . SER D 4 193 ? 0.881  -21.646 -68.377 1.00 51.81  ?  192 SER D CA  1 
ATOM   4613 C C   . SER D 4 193 ? 0.251  -21.232 -69.699 1.00 50.18  ?  192 SER D C   1 
ATOM   4614 O O   . SER D 4 193 ? 0.005  -22.069 -70.568 1.00 54.35  ?  192 SER D O   1 
ATOM   4615 C CB  . SER D 4 193 ? 2.369  -21.252 -68.355 1.00 51.83  ?  192 SER D CB  1 
ATOM   4616 O OG  . SER D 4 193 ? 3.034  -21.754 -67.195 1.00 45.11  ?  192 SER D OG  1 
ATOM   4617 N N   . ILE D 4 194 ? -0.004 -19.934 -69.856 1.00 54.67  ?  193 ILE D N   1 
ATOM   4618 C CA  . ILE D 4 194 ? -0.430 -19.387 -71.145 1.00 53.06  ?  193 ILE D CA  1 
ATOM   4619 C C   . ILE D 4 194 ? 0.747  -18.620 -71.741 1.00 51.84  ?  193 ILE D C   1 
ATOM   4620 O O   . ILE D 4 194 ? 1.143  -17.555 -71.247 1.00 49.74  ?  193 ILE D O   1 
ATOM   4621 C CB  . ILE D 4 194 ? -1.704 -18.531 -71.043 1.00 56.91  ?  193 ILE D CB  1 
ATOM   4622 C CG1 . ILE D 4 194 ? -1.584 -17.385 -70.043 1.00 61.35  ?  193 ILE D CG1 1 
ATOM   4623 C CG2 . ILE D 4 194 ? -2.899 -19.398 -70.645 1.00 57.55  ?  193 ILE D CG2 1 
ATOM   4624 C CD1 . ILE D 4 194 ? -2.954 -16.864 -69.601 1.00 54.18  ?  193 ILE D CD1 1 
ATOM   4625 N N   . ILE D 4 195 ? 1.300  -19.182 -72.811 1.00 50.18  ?  194 ILE D N   1 
ATOM   4626 C CA  . ILE D 4 195 ? 2.550  -18.756 -73.430 1.00 50.12  ?  194 ILE D CA  1 
ATOM   4627 C C   . ILE D 4 195 ? 2.244  -18.251 -74.838 1.00 55.31  ?  194 ILE D C   1 
ATOM   4628 O O   . ILE D 4 195 ? 1.270  -18.711 -75.453 1.00 54.72  ?  194 ILE D O   1 
ATOM   4629 C CB  . ILE D 4 195 ? 3.550  -19.921 -73.469 1.00 44.01  ?  194 ILE D CB  1 
ATOM   4630 C CG1 . ILE D 4 195 ? 3.018  -21.031 -74.375 1.00 47.27  ?  194 ILE D CG1 1 
ATOM   4631 C CG2 . ILE D 4 195 ? 3.753  -20.504 -72.074 1.00 47.89  ?  194 ILE D CG2 1 
ATOM   4632 C CD1 . ILE D 4 195 ? 3.899  -22.264 -74.423 1.00 40.00  ?  194 ILE D CD1 1 
ATOM   4633 N N   . PRO D 4 196 ? 3.045  -17.345 -75.399 1.00 53.76  ?  195 PRO D N   1 
ATOM   4634 C CA  . PRO D 4 196 ? 2.717  -16.787 -76.719 1.00 53.99  ?  195 PRO D CA  1 
ATOM   4635 C C   . PRO D 4 196 ? 2.380  -17.897 -77.703 1.00 51.97  ?  195 PRO D C   1 
ATOM   4636 O O   . PRO D 4 196 ? 2.874  -19.019 -77.591 1.00 54.23  ?  195 PRO D O   1 
ATOM   4637 C CB  . PRO D 4 196 ? 3.999  -16.046 -77.124 1.00 51.70  ?  195 PRO D CB  1 
ATOM   4638 C CG  . PRO D 4 196 ? 4.744  -15.821 -75.854 1.00 51.15  ?  195 PRO D CG  1 
ATOM   4639 C CD  . PRO D 4 196 ? 4.398  -16.970 -74.952 1.00 51.23  ?  195 PRO D CD  1 
ATOM   4640 N N   . GLU D 4 197 ? 1.510  -17.598 -78.666 1.00 56.04  ?  196 GLU D N   1 
ATOM   4641 C CA  . GLU D 4 197 ? 1.112  -18.688 -79.548 1.00 60.71  ?  196 GLU D CA  1 
ATOM   4642 C C   . GLU D 4 197 ? 2.126  -18.951 -80.657 1.00 54.71  ?  196 GLU D C   1 
ATOM   4643 O O   . GLU D 4 197 ? 2.056  -20.003 -81.297 1.00 50.73  ?  196 GLU D O   1 
ATOM   4644 C CB  . GLU D 4 197 ? -0.285 -18.439 -80.132 1.00 65.25  ?  196 GLU D CB  1 
ATOM   4645 C CG  . GLU D 4 197 ? -1.012 -19.747 -80.527 1.00 75.85  ?  196 GLU D CG  1 
ATOM   4646 C CD  . GLU D 4 197 ? -1.825 -20.398 -79.390 1.00 85.20  ?  196 GLU D CD  1 
ATOM   4647 O OE1 . GLU D 4 197 ? -1.600 -20.071 -78.202 1.00 79.21  ?  196 GLU D OE1 1 
ATOM   4648 O OE2 . GLU D 4 197 ? -2.685 -21.260 -79.695 1.00 91.88  -1 196 GLU D OE2 1 
ATOM   4649 N N   . ASP D 4 198 ? 3.091  -18.050 -80.869 1.00 51.74  ?  197 ASP D N   1 
ATOM   4650 C CA  . ASP D 4 198 ? 4.225  -18.292 -81.756 1.00 56.22  ?  197 ASP D CA  1 
ATOM   4651 C C   . ASP D 4 198 ? 5.449  -18.874 -81.021 1.00 51.85  ?  197 ASP D C   1 
ATOM   4652 O O   . ASP D 4 198 ? 6.589  -18.707 -81.486 1.00 48.13  ?  197 ASP D O   1 
ATOM   4653 C CB  . ASP D 4 198 ? 4.600  -16.992 -82.471 1.00 49.94  ?  197 ASP D CB  1 
ATOM   4654 C CG  . ASP D 4 198 ? 4.792  -15.845 -81.496 1.00 64.47  ?  197 ASP D CG  1 
ATOM   4655 O OD1 . ASP D 4 198 ? 4.056  -15.814 -80.475 1.00 62.18  ?  197 ASP D OD1 1 
ATOM   4656 O OD2 . ASP D 4 198 ? 5.686  -14.996 -81.728 1.00 69.68  -1 197 ASP D OD2 1 
ATOM   4657 N N   . THR D 4 199 ? 5.253  -19.539 -79.885 1.00 45.94  ?  198 THR D N   1 
ATOM   4658 C CA  . THR D 4 199 ? 6.373  -20.178 -79.196 1.00 45.92  ?  198 THR D CA  1 
ATOM   4659 C C   . THR D 4 199 ? 7.005  -21.247 -80.082 1.00 46.09  ?  198 THR D C   1 
ATOM   4660 O O   . THR D 4 199 ? 6.337  -22.189 -80.532 1.00 47.01  ?  198 THR D O   1 
ATOM   4661 C CB  . THR D 4 199 ? 5.919  -20.798 -77.862 1.00 46.17  ?  198 THR D CB  1 
ATOM   4662 O OG1 . THR D 4 199 ? 5.462  -19.766 -76.970 1.00 42.01  ?  198 THR D OG1 1 
ATOM   4663 C CG2 . THR D 4 199 ? 7.078  -21.564 -77.188 1.00 41.27  ?  198 THR D CG2 1 
ATOM   4664 N N   . PHE D 4 200 ? 8.308  -21.109 -80.309 1.00 45.27  ?  199 PHE D N   1 
ATOM   4665 C CA  . PHE D 4 200 ? 9.050  -22.054 -81.131 1.00 39.56  ?  199 PHE D CA  1 
ATOM   4666 C C   . PHE D 4 200 ? 9.233  -23.386 -80.398 1.00 46.94  ?  199 PHE D C   1 
ATOM   4667 O O   . PHE D 4 200 ? 9.805  -23.434 -79.297 1.00 43.73  ?  199 PHE D O   1 
ATOM   4668 C CB  . PHE D 4 200 ? 10.398 -21.439 -81.513 1.00 46.27  ?  199 PHE D CB  1 
ATOM   4669 C CG  . PHE D 4 200 ? 11.279 -22.354 -82.299 1.00 45.26  ?  199 PHE D CG  1 
ATOM   4670 C CD1 . PHE D 4 200 ? 10.873 -22.837 -83.537 1.00 48.00  ?  199 PHE D CD1 1 
ATOM   4671 C CD2 . PHE D 4 200 ? 12.519 -22.730 -81.809 1.00 41.95  ?  199 PHE D CD2 1 
ATOM   4672 C CE1 . PHE D 4 200 ? 11.688 -23.704 -84.268 1.00 46.87  ?  199 PHE D CE1 1 
ATOM   4673 C CE2 . PHE D 4 200 ? 13.333 -23.587 -82.522 1.00 42.18  ?  199 PHE D CE2 1 
ATOM   4674 C CZ  . PHE D 4 200 ? 12.923 -24.073 -83.763 1.00 49.40  ?  199 PHE D CZ  1 
ATOM   4675 N N   . PHE D 4 201 ? 8.727  -24.462 -81.000 1.00 34.26  ?  200 PHE D N   1 
ATOM   4676 C CA  . PHE D 4 201 ? 9.006  -25.825 -80.573 1.00 41.88  ?  200 PHE D CA  1 
ATOM   4677 C C   . PHE D 4 201 ? 9.763  -26.519 -81.701 1.00 49.06  ?  200 PHE D C   1 
ATOM   4678 O O   . PHE D 4 201 ? 9.198  -26.706 -82.795 1.00 54.33  ?  200 PHE D O   1 
ATOM   4679 C CB  . PHE D 4 201 ? 7.716  -26.595 -80.229 1.00 45.96  ?  200 PHE D CB  1 
ATOM   4680 C CG  . PHE D 4 201 ? 7.023  -26.124 -78.962 1.00 44.20  ?  200 PHE D CG  1 
ATOM   4681 C CD1 . PHE D 4 201 ? 6.087  -25.103 -79.009 1.00 45.60  ?  200 PHE D CD1 1 
ATOM   4682 C CD2 . PHE D 4 201 ? 7.282  -26.731 -77.737 1.00 45.33  ?  200 PHE D CD2 1 
ATOM   4683 C CE1 . PHE D 4 201 ? 5.438  -24.667 -77.849 1.00 49.86  ?  200 PHE D CE1 1 
ATOM   4684 C CE2 . PHE D 4 201 ? 6.639  -26.311 -76.581 1.00 42.87  ?  200 PHE D CE2 1 
ATOM   4685 C CZ  . PHE D 4 201 ? 5.715  -25.264 -76.636 1.00 42.07  ?  200 PHE D CZ  1 
ATOM   4686 N N   . PRO D 4 202 ? 11.024 -26.902 -81.505 1.00 46.96  ?  201 PRO D N   1 
ATOM   4687 C CA  . PRO D 4 202 ? 11.807 -27.464 -82.616 1.00 50.16  ?  201 PRO D CA  1 
ATOM   4688 C C   . PRO D 4 202 ? 11.247 -28.790 -83.112 1.00 51.26  ?  201 PRO D C   1 
ATOM   4689 O O   . PRO D 4 202 ? 10.753 -29.607 -82.334 1.00 56.26  ?  201 PRO D O   1 
ATOM   4690 C CB  . PRO D 4 202 ? 13.206 -27.644 -82.011 1.00 46.43  ?  201 PRO D CB  1 
ATOM   4691 C CG  . PRO D 4 202 ? 13.244 -26.667 -80.861 1.00 47.23  ?  201 PRO D CG  1 
ATOM   4692 C CD  . PRO D 4 202 ? 11.846 -26.652 -80.309 1.00 44.39  ?  201 PRO D CD  1 
ATOM   4693 N N   . SER D 4 203 ? 11.358 -29.000 -84.423 1.00 54.94  ?  202 SER D N   1 
ATOM   4694 C CA  . SER D 4 203 ? 10.898 -30.224 -85.082 1.00 62.56  ?  202 SER D CA  1 
ATOM   4695 C C   . SER D 4 203 ? 11.987 -31.289 -85.117 1.00 59.86  ?  202 SER D C   1 
ATOM   4696 O O   . SER D 4 203 ? 12.009 -32.127 -86.023 1.00 63.99  ?  202 SER D O   1 
ATOM   4697 C CB  . SER D 4 203 ? 10.434 -29.921 -86.514 1.00 60.41  ?  202 SER D CB  1 
ATOM   4698 O OG  . SER D 4 203 ? 9.295  -29.076 -86.520 1.00 65.14  ?  202 SER D OG  1 
ATOM   4699 N N   . MET E 5 1   ? 40.478 -1.480  -42.546 1.00 131.92 ?  0   MET E N   1 
ATOM   4700 C CA  . MET E 5 1   ? 39.366 -0.763  -41.929 1.00 128.22 ?  0   MET E CA  1 
ATOM   4701 C C   . MET E 5 1   ? 38.044 -0.861  -42.668 1.00 101.68 ?  0   MET E C   1 
ATOM   4702 O O   . MET E 5 1   ? 37.227 0.064   -42.583 1.00 97.38  ?  0   MET E O   1 
ATOM   4703 C CB  . MET E 5 1   ? 39.703 0.727   -41.760 1.00 140.90 ?  0   MET E CB  1 
ATOM   4704 C CG  . MET E 5 1   ? 38.887 1.488   -40.687 1.00 137.28 ?  0   MET E CG  1 
ATOM   4705 S SD  . MET E 5 1   ? 39.792 2.884   -39.956 1.00 116.35 ?  0   MET E SD  1 
ATOM   4706 C CE  . MET E 5 1   ? 40.588 2.096   -38.556 1.00 100.08 ?  0   MET E CE  1 
ATOM   4707 N N   . GLU E 5 2   ? 37.766 -2.015  -43.262 1.00 89.68  ?  1   GLU E N   1 
ATOM   4708 C CA  . GLU E 5 2   ? 36.486 -2.156  -43.945 1.00 80.09  ?  1   GLU E CA  1 
ATOM   4709 C C   . GLU E 5 2   ? 35.411 -2.558  -42.932 1.00 70.19  ?  1   GLU E C   1 
ATOM   4710 O O   . GLU E 5 2   ? 35.525 -3.580  -42.241 1.00 65.66  ?  1   GLU E O   1 
ATOM   4711 C CB  . GLU E 5 2   ? 36.563 -3.129  -45.124 1.00 73.96  ?  1   GLU E CB  1 
ATOM   4712 C CG  . GLU E 5 2   ? 35.367 -2.947  -46.090 1.00 74.18  ?  1   GLU E CG  1 
ATOM   4713 C CD  . GLU E 5 2   ? 35.533 -1.808  -47.114 1.00 79.85  ?  1   GLU E CD  1 
ATOM   4714 O OE1 . GLU E 5 2   ? 34.775 -1.780  -48.115 1.00 68.41  ?  1   GLU E OE1 1 
ATOM   4715 O OE2 . GLU E 5 2   ? 36.413 -0.945  -46.915 1.00 80.80  -1 1   GLU E OE2 1 
ATOM   4716 N N   . ALA E 5 3   ? 34.385 -1.721  -42.827 1.00 60.82  ?  2   ALA E N   1 
ATOM   4717 C CA  . ALA E 5 3   ? 33.322 -1.935  -41.860 1.00 57.78  ?  2   ALA E CA  1 
ATOM   4718 C C   . ALA E 5 3   ? 32.560 -3.210  -42.178 1.00 46.91  ?  2   ALA E C   1 
ATOM   4719 O O   . ALA E 5 3   ? 32.164 -3.432  -43.324 1.00 48.29  ?  2   ALA E O   1 
ATOM   4720 C CB  . ALA E 5 3   ? 32.360 -0.750  -41.870 1.00 54.60  ?  2   ALA E CB  1 
ATOM   4721 N N   . GLN E 5 4   ? 32.340 -4.042  -41.162 1.00 46.52  ?  3   GLN E N   1 
ATOM   4722 C CA  . GLN E 5 4   ? 31.546 -5.249  -41.361 1.00 40.91  ?  3   GLN E CA  1 
ATOM   4723 C C   . GLN E 5 4   ? 31.173 -5.847  -40.016 1.00 31.89  ?  3   GLN E C   1 
ATOM   4724 O O   . GLN E 5 4   ? 31.876 -5.676  -39.016 1.00 30.03  ?  3   GLN E O   1 
ATOM   4725 C CB  . GLN E 5 4   ? 32.283 -6.291  -42.213 1.00 34.37  ?  3   GLN E CB  1 
ATOM   4726 C CG  . GLN E 5 4   ? 33.578 -6.799  -41.580 1.00 46.69  ?  3   GLN E CG  1 
ATOM   4727 C CD  . GLN E 5 4   ? 34.691 -7.033  -42.609 1.00 60.56  ?  3   GLN E CD  1 
ATOM   4728 O OE1 . GLN E 5 4   ? 34.558 -7.883  -43.501 1.00 59.54  ?  3   GLN E OE1 1 
ATOM   4729 N NE2 . GLN E 5 4   ? 35.786 -6.265  -42.496 1.00 57.46  ?  3   GLN E NE2 1 
ATOM   4730 N N   . VAL E 5 5   ? 30.041 -6.538  -40.017 1.00 31.37  ?  4   VAL E N   1 
ATOM   4731 C CA  . VAL E 5 5   ? 29.557 -7.334  -38.900 1.00 24.50  ?  4   VAL E CA  1 
ATOM   4732 C C   . VAL E 5 5   ? 29.741 -8.797  -39.265 1.00 30.30  ?  4   VAL E C   1 
ATOM   4733 O O   . VAL E 5 5   ? 29.350 -9.212  -40.362 1.00 24.50  ?  4   VAL E O   1 
ATOM   4734 C CB  . VAL E 5 5   ? 28.081 -7.024  -38.637 1.00 28.21  ?  4   VAL E CB  1 
ATOM   4735 C CG1 . VAL E 5 5   ? 27.536 -7.957  -37.549 1.00 23.04  ?  4   VAL E CG1 1 
ATOM   4736 C CG2 . VAL E 5 5   ? 27.926 -5.505  -38.313 1.00 24.65  ?  4   VAL E CG2 1 
ATOM   4737 N N   . THR E 5 6   ? 30.312 -9.581  -38.353 1.00 28.14  ?  5   THR E N   1 
ATOM   4738 C CA  . THR E 5 6   ? 30.614 -10.986 -38.612 1.00 24.81  ?  5   THR E CA  1 
ATOM   4739 C C   . THR E 5 6   ? 29.751 -11.868 -37.728 1.00 25.23  ?  5   THR E C   1 
ATOM   4740 O O   . THR E 5 6   ? 29.648 -11.632 -36.521 1.00 30.02  ?  5   THR E O   1 
ATOM   4741 C CB  . THR E 5 6   ? 32.083 -11.303 -38.346 1.00 27.57  ?  5   THR E CB  1 
ATOM   4742 O OG1 . THR E 5 6   ? 32.892 -10.566 -39.249 1.00 36.78  ?  5   THR E OG1 1 
ATOM   4743 C CG2 . THR E 5 6   ? 32.336 -12.806 -38.551 1.00 34.90  ?  5   THR E CG2 1 
ATOM   4744 N N   . GLN E 5 7   ? 29.130 -12.871 -38.318 1.00 25.56  ?  6   GLN E N   1 
ATOM   4745 C CA  . GLN E 5 7   ? 28.348 -13.827 -37.561 1.00 28.19  ?  6   GLN E CA  1 
ATOM   4746 C C   . GLN E 5 7   ? 28.991 -15.186 -37.750 1.00 27.78  ?  6   GLN E C   1 
ATOM   4747 O O   . GLN E 5 7   ? 29.420 -15.520 -38.849 1.00 32.27  ?  6   GLN E O   1 
ATOM   4748 C CB  . GLN E 5 7   ? 26.878 -13.862 -38.014 1.00 25.75  ?  6   GLN E CB  1 
ATOM   4749 C CG  . GLN E 5 7   ? 26.134 -12.524 -37.793 1.00 31.39  ?  6   GLN E CG  1 
ATOM   4750 C CD  . GLN E 5 7   ? 24.681 -12.522 -38.291 1.00 25.09  ?  6   GLN E CD  1 
ATOM   4751 O OE1 . GLN E 5 7   ? 24.187 -11.497 -38.736 1.00 28.15  ?  6   GLN E OE1 1 
ATOM   4752 N NE2 . GLN E 5 7   ? 24.008 -13.666 -38.219 1.00 21.86  ?  6   GLN E NE2 1 
ATOM   4753 N N   . ASN E 5 8   ? 29.042 -15.962 -36.684 1.00 29.35  ?  7   ASN E N   1 
ATOM   4754 C CA  . ASN E 5 8   ? 29.579 -17.311 -36.740 1.00 26.34  ?  7   ASN E CA  1 
ATOM   4755 C C   . ASN E 5 8   ? 28.708 -18.167 -35.833 1.00 30.52  ?  7   ASN E C   1 
ATOM   4756 O O   . ASN E 5 8   ? 28.595 -17.887 -34.633 1.00 28.70  ?  7   ASN E O   1 
ATOM   4757 C CB  . ASN E 5 8   ? 31.053 -17.347 -36.289 1.00 25.82  ?  7   ASN E CB  1 
ATOM   4758 C CG  . ASN E 5 8   ? 31.726 -18.701 -36.555 1.00 27.61  ?  7   ASN E CG  1 
ATOM   4759 O OD1 . ASN E 5 8   ? 31.125 -19.759 -36.348 1.00 32.07  ?  7   ASN E OD1 1 
ATOM   4760 N ND2 . ASN E 5 8   ? 32.970 -18.669 -36.995 1.00 24.73  ?  7   ASN E ND2 1 
ATOM   4761 N N   . PRO E 5 9   ? 28.074 -19.220 -36.357 1.00 26.11  ?  8   PRO E N   1 
ATOM   4762 C CA  . PRO E 5 9   ? 28.198 -19.701 -37.739 1.00 23.83  ?  8   PRO E CA  1 
ATOM   4763 C C   . PRO E 5 9   ? 27.193 -19.046 -38.702 1.00 28.54  ?  8   PRO E C   1 
ATOM   4764 O O   . PRO E 5 9   ? 26.227 -18.466 -38.259 1.00 25.43  ?  8   PRO E O   1 
ATOM   4765 C CB  . PRO E 5 9   ? 27.914 -21.185 -37.596 1.00 25.31  ?  8   PRO E CB  1 
ATOM   4766 C CG  . PRO E 5 9   ? 26.883 -21.236 -36.441 1.00 27.93  ?  8   PRO E CG  1 
ATOM   4767 C CD  . PRO E 5 9   ? 27.270 -20.117 -35.506 1.00 23.86  ?  8   PRO E CD  1 
ATOM   4768 N N   . ARG E 5 10  ? 27.449 -19.108 -40.004 1.00 24.87  ?  9   ARG E N   1 
ATOM   4769 C CA  . ARG E 5 10  ? 26.456 -18.651 -40.969 1.00 28.85  ?  9   ARG E CA  1 
ATOM   4770 C C   . ARG E 5 10  ? 25.380 -19.702 -41.208 1.00 27.31  ?  9   ARG E C   1 
ATOM   4771 O O   . ARG E 5 10  ? 24.248 -19.341 -41.543 1.00 23.05  ?  9   ARG E O   1 
ATOM   4772 C CB  . ARG E 5 10  ? 27.140 -18.284 -42.289 1.00 29.68  ?  9   ARG E CB  1 
ATOM   4773 C CG  . ARG E 5 10  ? 28.023 -17.015 -42.226 1.00 32.15  ?  9   ARG E CG  1 
ATOM   4774 C CD  . ARG E 5 10  ? 28.381 -16.512 -43.656 1.00 39.51  ?  9   ARG E CD  1 
ATOM   4775 N NE  . ARG E 5 10  ? 29.166 -17.497 -44.406 1.00 39.45  ?  9   ARG E NE  1 
ATOM   4776 C CZ  . ARG E 5 10  ? 28.776 -18.089 -45.534 1.00 40.48  ?  9   ARG E CZ  1 
ATOM   4777 N NH1 . ARG E 5 10  ? 27.598 -17.802 -46.090 1.00 44.16  ?  9   ARG E NH1 1 
ATOM   4778 N NH2 . ARG E 5 10  ? 29.576 -18.974 -46.117 1.00 33.14  ?  9   ARG E NH2 1 
ATOM   4779 N N   . TYR E 5 11  ? 25.712 -20.998 -41.026 1.00 23.78  ?  10  TYR E N   1 
ATOM   4780 C CA  . TYR E 5 11  ? 24.770 -22.109 -41.174 1.00 25.39  ?  10  TYR E CA  1 
ATOM   4781 C C   . TYR E 5 11  ? 24.950 -23.098 -40.034 1.00 28.97  ?  10  TYR E C   1 
ATOM   4782 O O   . TYR E 5 11  ? 26.077 -23.459 -39.693 1.00 25.84  ?  10  TYR E O   1 
ATOM   4783 C CB  . TYR E 5 11  ? 24.964 -22.871 -42.497 1.00 25.07  ?  10  TYR E CB  1 
ATOM   4784 C CG  . TYR E 5 11  ? 24.716 -22.050 -43.753 1.00 29.30  ?  10  TYR E CG  1 
ATOM   4785 C CD1 . TYR E 5 11  ? 25.744 -21.330 -44.332 1.00 27.81  ?  10  TYR E CD1 1 
ATOM   4786 C CD2 . TYR E 5 11  ? 23.464 -22.028 -44.371 1.00 29.08  ?  10  TYR E CD2 1 
ATOM   4787 C CE1 . TYR E 5 11  ? 25.547 -20.604 -45.469 1.00 31.04  ?  10  TYR E CE1 1 
ATOM   4788 C CE2 . TYR E 5 11  ? 23.259 -21.295 -45.532 1.00 30.92  ?  10  TYR E CE2 1 
ATOM   4789 C CZ  . TYR E 5 11  ? 24.314 -20.587 -46.071 1.00 30.69  ?  10  TYR E CZ  1 
ATOM   4790 O OH  . TYR E 5 11  ? 24.151 -19.844 -47.212 1.00 42.67  ?  10  TYR E OH  1 
ATOM   4791 N N   . LEU E 5 12  ? 23.844 -23.554 -39.455 1.00 27.56  ?  11  LEU E N   1 
ATOM   4792 C CA  . LEU E 5 12  ? 23.966 -24.505 -38.356 1.00 27.64  ?  11  LEU E CA  1 
ATOM   4793 C C   . LEU E 5 12  ? 22.734 -25.401 -38.302 1.00 30.43  ?  11  LEU E C   1 
ATOM   4794 O O   . LEU E 5 12  ? 21.604 -24.909 -38.259 1.00 27.81  ?  11  LEU E O   1 
ATOM   4795 C CB  . LEU E 5 12  ? 24.152 -23.769 -37.016 1.00 25.37  ?  11  LEU E CB  1 
ATOM   4796 C CG  . LEU E 5 12  ? 24.264 -24.599 -35.725 1.00 29.97  ?  11  LEU E CG  1 
ATOM   4797 C CD1 . LEU E 5 12  ? 25.474 -25.584 -35.701 1.00 28.87  ?  11  LEU E CD1 1 
ATOM   4798 C CD2 . LEU E 5 12  ? 24.298 -23.624 -34.518 1.00 30.68  ?  11  LEU E CD2 1 
ATOM   4799 N N   . ILE E 5 13  ? 22.960 -26.712 -38.308 1.00 30.20  ?  12  ILE E N   1 
ATOM   4800 C CA  . ILE E 5 13  ? 21.919 -27.700 -38.045 1.00 27.45  ?  12  ILE E CA  1 
ATOM   4801 C C   . ILE E 5 13  ? 22.218 -28.304 -36.687 1.00 26.00  ?  12  ILE E C   1 
ATOM   4802 O O   . ILE E 5 13  ? 23.338 -28.765 -36.439 1.00 27.91  ?  12  ILE E O   1 
ATOM   4803 C CB  . ILE E 5 13  ? 21.867 -28.794 -39.125 1.00 29.01  ?  12  ILE E CB  1 
ATOM   4804 C CG1 . ILE E 5 13  ? 21.786 -28.181 -40.522 1.00 23.73  ?  12  ILE E CG1 1 
ATOM   4805 C CG2 . ILE E 5 13  ? 20.650 -29.692 -38.908 1.00 26.54  ?  12  ILE E CG2 1 
ATOM   4806 C CD1 . ILE E 5 13  ? 22.108 -29.226 -41.636 1.00 23.87  ?  12  ILE E CD1 1 
ATOM   4807 N N   . THR E 5 14  ? 21.234 -28.289 -35.805 1.00 26.69  ?  13  THR E N   1 
ATOM   4808 C CA  . THR E 5 14  ? 21.481 -28.715 -34.445 1.00 30.33  ?  13  THR E CA  1 
ATOM   4809 C C   . THR E 5 14  ? 20.278 -29.498 -33.955 1.00 29.18  ?  13  THR E C   1 
ATOM   4810 O O   . THR E 5 14  ? 19.174 -29.391 -34.496 1.00 30.04  ?  13  THR E O   1 
ATOM   4811 C CB  . THR E 5 14  ? 21.767 -27.519 -33.529 1.00 29.34  ?  13  THR E CB  1 
ATOM   4812 O OG1 . THR E 5 14  ? 22.256 -27.995 -32.267 1.00 37.33  ?  13  THR E OG1 1 
ATOM   4813 C CG2 . THR E 5 14  ? 20.473 -26.708 -33.320 1.00 27.21  ?  13  THR E CG2 1 
ATOM   4814 N N   . VAL E 5 15  ? 20.516 -30.279 -32.916 1.00 32.44  ?  14  VAL E N   1 
ATOM   4815 C CA  . VAL E 5 15  ? 19.512 -31.121 -32.269 1.00 28.60  ?  14  VAL E CA  1 
ATOM   4816 C C   . VAL E 5 15  ? 18.855 -30.381 -31.106 1.00 31.62  ?  14  VAL E C   1 
ATOM   4817 O O   . VAL E 5 15  ? 19.531 -29.709 -30.305 1.00 29.16  ?  14  VAL E O   1 
ATOM   4818 C CB  . VAL E 5 15  ? 20.173 -32.419 -31.785 1.00 32.67  ?  14  VAL E CB  1 
ATOM   4819 C CG1 . VAL E 5 15  ? 19.211 -33.228 -30.937 1.00 35.21  ?  14  VAL E CG1 1 
ATOM   4820 C CG2 . VAL E 5 15  ? 20.700 -33.213 -32.974 1.00 34.53  ?  14  VAL E CG2 1 
ATOM   4821 N N   . THR E 5 16  ? 17.535 -30.563 -30.987 1.00 29.44  ?  15  THR E N   1 
ATOM   4822 C CA  . THR E 5 16  ? 16.728 -29.952 -29.937 1.00 29.83  ?  15  THR E CA  1 
ATOM   4823 C C   . THR E 5 16  ? 17.388 -30.069 -28.571 1.00 33.13  ?  15  THR E C   1 
ATOM   4824 O O   . THR E 5 16  ? 17.862 -31.138 -28.186 1.00 29.39  ?  15  THR E O   1 
ATOM   4825 C CB  . THR E 5 16  ? 15.344 -30.609 -29.902 1.00 31.37  ?  15  THR E CB  1 
ATOM   4826 O OG1 . THR E 5 16  ? 14.638 -30.265 -31.087 1.00 33.81  ?  15  THR E OG1 1 
ATOM   4827 C CG2 . THR E 5 16  ? 14.537 -30.112 -28.705 1.00 32.02  ?  15  THR E CG2 1 
ATOM   4828 N N   . GLY E 5 17  ? 17.413 -28.962 -27.833 1.00 30.21  ?  16  GLY E N   1 
ATOM   4829 C CA  . GLY E 5 17  ? 17.854 -29.022 -26.450 1.00 33.04  ?  16  GLY E CA  1 
ATOM   4830 C C   . GLY E 5 17  ? 19.352 -28.959 -26.217 1.00 29.56  ?  16  GLY E C   1 
ATOM   4831 O O   . GLY E 5 17  ? 19.774 -28.921 -25.057 1.00 34.46  ?  16  GLY E O   1 
ATOM   4832 N N   . LYS E 5 18  ? 20.174 -28.942 -27.261 1.00 25.89  ?  17  LYS E N   1 
ATOM   4833 C CA  . LYS E 5 18  ? 21.613 -28.819 -27.082 1.00 28.78  ?  17  LYS E CA  1 
ATOM   4834 C C   . LYS E 5 18  ? 21.992 -27.342 -27.111 1.00 33.94  ?  17  LYS E C   1 
ATOM   4835 O O   . LYS E 5 18  ? 21.817 -26.677 -28.142 1.00 30.68  ?  17  LYS E O   1 
ATOM   4836 C CB  . LYS E 5 18  ? 22.377 -29.582 -28.168 1.00 36.51  ?  17  LYS E CB  1 
ATOM   4837 C CG  . LYS E 5 18  ? 23.875 -29.398 -28.046 1.00 41.49  ?  17  LYS E CG  1 
ATOM   4838 C CD  . LYS E 5 18  ? 24.673 -30.229 -29.047 1.00 48.07  ?  17  LYS E CD  1 
ATOM   4839 C CE  . LYS E 5 18  ? 26.149 -30.248 -28.656 1.00 52.77  ?  17  LYS E CE  1 
ATOM   4840 N NZ  . LYS E 5 18  ? 26.506 -31.384 -27.742 1.00 69.21  ?  17  LYS E NZ  1 
ATOM   4841 N N   . LYS E 5 19  ? 22.543 -26.844 -25.998 1.00 31.19  ?  18  LYS E N   1 
ATOM   4842 C CA  . LYS E 5 19  ? 22.849 -25.422 -25.879 1.00 32.47  ?  18  LYS E CA  1 
ATOM   4843 C C   . LYS E 5 19  ? 23.757 -24.959 -27.010 1.00 32.45  ?  18  LYS E C   1 
ATOM   4844 O O   . LYS E 5 19  ? 24.678 -25.673 -27.416 1.00 27.56  ?  18  LYS E O   1 
ATOM   4845 C CB  . LYS E 5 19  ? 23.511 -25.131 -24.525 1.00 35.99  ?  18  LYS E CB  1 
ATOM   4846 C CG  . LYS E 5 19  ? 23.938 -23.673 -24.350 1.00 34.65  ?  18  LYS E CG  1 
ATOM   4847 C CD  . LYS E 5 19  ? 24.084 -23.343 -22.863 1.00 41.12  ?  18  LYS E CD  1 
ATOM   4848 C CE  . LYS E 5 19  ? 24.913 -22.086 -22.644 1.00 35.13  ?  18  LYS E CE  1 
ATOM   4849 N NZ  . LYS E 5 19  ? 25.216 -21.981 -21.194 1.00 41.90  ?  18  LYS E NZ  1 
ATOM   4850 N N   . LEU E 5 20  ? 23.506 -23.747 -27.524 1.00 31.17  ?  19  LEU E N   1 
ATOM   4851 C CA  . LEU E 5 20  ? 24.395 -23.199 -28.546 1.00 28.69  ?  19  LEU E CA  1 
ATOM   4852 C C   . LEU E 5 20  ? 24.482 -21.688 -28.424 1.00 26.98  ?  19  LEU E C   1 
ATOM   4853 O O   . LEU E 5 20  ? 23.616 -21.039 -27.831 1.00 28.59  ?  19  LEU E O   1 
ATOM   4854 C CB  . LEU E 5 20  ? 23.948 -23.585 -29.964 1.00 28.78  ?  19  LEU E CB  1 
ATOM   4855 C CG  . LEU E 5 20  ? 22.662 -22.910 -30.429 1.00 25.46  ?  19  LEU E CG  1 
ATOM   4856 C CD1 . LEU E 5 20  ? 22.921 -21.508 -30.988 1.00 29.00  ?  19  LEU E CD1 1 
ATOM   4857 C CD2 . LEU E 5 20  ? 21.959 -23.814 -31.468 1.00 32.47  ?  19  LEU E CD2 1 
ATOM   4858 N N   . THR E 5 21  ? 25.555 -21.140 -28.997 1.00 25.55  ?  20  THR E N   1 
ATOM   4859 C CA  . THR E 5 21  ? 25.813 -19.704 -29.040 1.00 27.06  ?  20  THR E CA  1 
ATOM   4860 C C   . THR E 5 21  ? 26.186 -19.291 -30.455 1.00 27.41  ?  20  THR E C   1 
ATOM   4861 O O   . THR E 5 21  ? 27.029 -19.936 -31.092 1.00 29.79  ?  20  THR E O   1 
ATOM   4862 C CB  . THR E 5 21  ? 26.947 -19.324 -28.093 1.00 25.94  ?  20  THR E CB  1 
ATOM   4863 O OG1 . THR E 5 21  ? 26.540 -19.627 -26.762 1.00 32.58  ?  20  THR E OG1 1 
ATOM   4864 C CG2 . THR E 5 21  ? 27.259 -17.834 -28.205 1.00 26.43  ?  20  THR E CG2 1 
ATOM   4865 N N   . VAL E 5 22  ? 25.575 -18.212 -30.938 1.00 23.23  ?  21  VAL E N   1 
ATOM   4866 C CA  . VAL E 5 22  ? 25.943 -17.596 -32.206 1.00 23.57  ?  21  VAL E CA  1 
ATOM   4867 C C   . VAL E 5 22  ? 26.710 -16.314 -31.865 1.00 24.80  ?  21  VAL E C   1 
ATOM   4868 O O   . VAL E 5 22  ? 26.234 -15.491 -31.072 1.00 25.73  ?  21  VAL E O   1 
ATOM   4869 C CB  . VAL E 5 22  ? 24.698 -17.324 -33.070 1.00 23.50  ?  21  VAL E CB  1 
ATOM   4870 C CG1 . VAL E 5 22  ? 25.086 -16.769 -34.462 1.00 25.22  ?  21  VAL E CG1 1 
ATOM   4871 C CG2 . VAL E 5 22  ? 23.836 -18.626 -33.209 1.00 21.44  ?  21  VAL E CG2 1 
ATOM   4872 N N   . THR E 5 23  ? 27.920 -16.160 -32.404 1.00 23.42  ?  22  THR E N   1 
ATOM   4873 C CA  . THR E 5 23  ? 28.689 -14.960 -32.087 1.00 25.78  ?  22  THR E CA  1 
ATOM   4874 C C   . THR E 5 23  ? 28.413 -13.881 -33.117 1.00 27.90  ?  22  THR E C   1 
ATOM   4875 O O   . THR E 5 23  ? 28.049 -14.163 -34.268 1.00 25.08  ?  22  THR E O   1 
ATOM   4876 C CB  . THR E 5 23  ? 30.200 -15.222 -32.008 1.00 30.80  ?  22  THR E CB  1 
ATOM   4877 O OG1 . THR E 5 23  ? 30.649 -15.857 -33.206 1.00 29.43  ?  22  THR E OG1 1 
ATOM   4878 C CG2 . THR E 5 23  ? 30.551 -16.087 -30.779 1.00 32.02  ?  22  THR E CG2 1 
ATOM   4879 N N   . CYS E 5 24  ? 28.547 -12.632 -32.672 1.00 23.86  ?  23  CYS E N   1 
ATOM   4880 C CA  . CYS E 5 24  ? 28.406 -11.469 -33.539 1.00 26.52  ?  23  CYS E CA  1 
ATOM   4881 C C   . CYS E 5 24  ? 29.478 -10.487 -33.144 1.00 23.75  ?  23  CYS E C   1 
ATOM   4882 O O   . CYS E 5 24  ? 29.632 -10.186 -31.955 1.00 24.78  ?  23  CYS E O   1 
ATOM   4883 C CB  . CYS E 5 24  ? 27.039 -10.766 -33.429 1.00 19.55  ?  23  CYS E CB  1 
ATOM   4884 S SG  . CYS E 5 24  ? 27.043 -9.262  -34.482 1.00 26.22  ?  23  CYS E SG  1 
ATOM   4885 N N   . SER E 5 25  ? 30.238 -10.005 -34.113 1.00 23.60  ?  24  SER E N   1 
ATOM   4886 C CA  . SER E 5 25  ? 31.256 -9.056  -33.713 1.00 28.06  ?  24  SER E CA  1 
ATOM   4887 C C   . SER E 5 25  ? 31.431 -8.018  -34.797 1.00 25.14  ?  24  SER E C   1 
ATOM   4888 O O   . SER E 5 25  ? 31.076 -8.235  -35.960 1.00 27.99  ?  24  SER E O   1 
ATOM   4889 C CB  . SER E 5 25  ? 32.573 -9.766  -33.391 1.00 32.45  ?  24  SER E CB  1 
ATOM   4890 O OG  . SER E 5 25  ? 33.090 -10.323 -34.561 1.00 33.45  ?  24  SER E OG  1 
ATOM   4891 N N   . GLN E 5 26  ? 31.947 -6.861  -34.382 1.00 23.27  ?  25  GLN E N   1 
ATOM   4892 C CA  . GLN E 5 26  ? 32.269 -5.761  -35.270 1.00 24.58  ?  25  GLN E CA  1 
ATOM   4893 C C   . GLN E 5 26  ? 33.462 -5.036  -34.678 1.00 29.49  ?  25  GLN E C   1 
ATOM   4894 O O   . GLN E 5 26  ? 33.563 -4.882  -33.457 1.00 26.94  ?  25  GLN E O   1 
ATOM   4895 C CB  . GLN E 5 26  ? 31.099 -4.783  -35.465 1.00 27.21  ?  25  GLN E CB  1 
ATOM   4896 C CG  . GLN E 5 26  ? 30.351 -4.399  -34.190 1.00 24.85  ?  25  GLN E CG  1 
ATOM   4897 C CD  . GLN E 5 26  ? 31.030 -3.265  -33.453 1.00 26.55  ?  25  GLN E CD  1 
ATOM   4898 O OE1 . GLN E 5 26  ? 31.817 -2.498  -34.039 1.00 25.68  ?  25  GLN E OE1 1 
ATOM   4899 N NE2 . GLN E 5 26  ? 30.743 -3.155  -32.158 1.00 24.62  ?  25  GLN E NE2 1 
ATOM   4900 N N   . ASN E 5 27  ? 34.367 -4.597  -35.547 1.00 29.69  ?  26  ASN E N   1 
ATOM   4901 C CA  . ASN E 5 27  ? 35.564 -3.934  -35.073 1.00 33.69  ?  26  ASN E CA  1 
ATOM   4902 C C   . ASN E 5 27  ? 35.500 -2.426  -35.265 1.00 34.84  ?  26  ASN E C   1 
ATOM   4903 O O   . ASN E 5 27  ? 36.543 -1.769  -35.218 1.00 34.14  ?  26  ASN E O   1 
ATOM   4904 C CB  . ASN E 5 27  ? 36.805 -4.530  -35.756 1.00 38.14  ?  26  ASN E CB  1 
ATOM   4905 C CG  . ASN E 5 27  ? 37.076 -5.981  -35.328 1.00 35.52  ?  26  ASN E CG  1 
ATOM   4906 O OD1 . ASN E 5 27  ? 36.984 -6.333  -34.146 1.00 31.40  ?  26  ASN E OD1 1 
ATOM   4907 N ND2 . ASN E 5 27  ? 37.405 -6.827  -36.296 1.00 35.71  ?  26  ASN E ND2 1 
ATOM   4908 N N   . MET E 5 28  ? 34.298 -1.851  -35.416 1.00 32.49  ?  27  MET E N   1 
ATOM   4909 C CA  . MET E 5 28  ? 34.176 -0.406  -35.636 1.00 31.27  ?  27  MET E CA  1 
ATOM   4910 C C   . MET E 5 28  ? 33.949 0.379   -34.350 1.00 32.29  ?  27  MET E C   1 
ATOM   4911 O O   . MET E 5 28  ? 33.646 1.572   -34.409 1.00 32.47  ?  27  MET E O   1 
ATOM   4912 C CB  . MET E 5 28  ? 33.052 -0.109  -36.630 1.00 31.42  ?  27  MET E CB  1 
ATOM   4913 C CG  . MET E 5 28  ? 33.339 -0.601  -38.054 1.00 37.49  ?  27  MET E CG  1 
ATOM   4914 S SD  . MET E 5 28  ? 31.795 -1.061  -38.880 1.00 59.52  ?  27  MET E SD  1 
ATOM   4915 C CE  . MET E 5 28  ? 31.726 -2.768  -38.316 1.00 33.07  ?  27  MET E CE  1 
ATOM   4916 N N   . ASN E 5 29  ? 34.082 -0.261  -33.193 1.00 30.61  ?  28  ASN E N   1 
ATOM   4917 C CA  . ASN E 5 29  ? 33.834 0.403   -31.929 1.00 33.93  ?  28  ASN E CA  1 
ATOM   4918 C C   . ASN E 5 29  ? 32.414 0.956   -31.848 1.00 35.12  ?  28  ASN E C   1 
ATOM   4919 O O   . ASN E 5 29  ? 32.189 1.993   -31.231 1.00 30.26  ?  28  ASN E O   1 
ATOM   4920 C CB  . ASN E 5 29  ? 34.852 1.522   -31.688 1.00 37.12  ?  28  ASN E CB  1 
ATOM   4921 C CG  . ASN E 5 29  ? 35.290 1.588   -30.244 1.00 46.51  ?  28  ASN E CG  1 
ATOM   4922 O OD1 . ASN E 5 29  ? 35.649 0.558   -29.643 1.00 52.43  ?  28  ASN E OD1 1 
ATOM   4923 N ND2 . ASN E 5 29  ? 35.263 2.797   -29.665 1.00 48.73  ?  28  ASN E ND2 1 
ATOM   4924 N N   . HIS E 5 30  ? 31.458 0.265   -32.469 1.00 29.77  ?  29  HIS E N   1 
ATOM   4925 C CA  . HIS E 5 30  ? 30.067 0.690   -32.445 1.00 24.74  ?  29  HIS E CA  1 
ATOM   4926 C C   . HIS E 5 30  ? 29.459 0.460   -31.069 1.00 26.99  ?  29  HIS E C   1 
ATOM   4927 O O   . HIS E 5 30  ? 29.683 -0.579  -30.441 1.00 29.21  ?  29  HIS E O   1 
ATOM   4928 C CB  . HIS E 5 30  ? 29.252 -0.089  -33.489 1.00 23.69  ?  29  HIS E CB  1 
ATOM   4929 C CG  . HIS E 5 30  ? 29.427 0.410   -34.895 1.00 27.75  ?  29  HIS E CG  1 
ATOM   4930 N ND1 . HIS E 5 30  ? 28.774 -0.156  -35.971 1.00 26.91  ?  29  HIS E ND1 1 
ATOM   4931 C CD2 . HIS E 5 30  ? 30.182 1.416   -35.402 1.00 26.87  ?  29  HIS E CD2 1 
ATOM   4932 C CE1 . HIS E 5 30  ? 29.118 0.482   -37.080 1.00 26.74  ?  29  HIS E CE1 1 
ATOM   4933 N NE2 . HIS E 5 30  ? 29.973 1.438   -36.761 1.00 30.48  ?  29  HIS E NE2 1 
ATOM   4934 N N   . GLU E 5 31  ? 28.637 1.414   -30.629 1.00 20.21  ?  30  GLU E N   1 
ATOM   4935 C CA  . GLU E 5 31  ? 27.888 1.256   -29.379 1.00 30.11  ?  30  GLU E CA  1 
ATOM   4936 C C   . GLU E 5 31  ? 26.704 0.306   -29.524 1.00 23.10  ?  30  GLU E C   1 
ATOM   4937 O O   . GLU E 5 31  ? 26.405 -0.470  -28.612 1.00 23.44  ?  30  GLU E O   1 
ATOM   4938 C CB  . GLU E 5 31  ? 27.393 2.628   -28.895 1.00 23.59  ?  30  GLU E CB  1 
ATOM   4939 C CG  . GLU E 5 31  ? 28.530 3.623   -28.640 1.00 23.72  ?  30  GLU E CG  1 
ATOM   4940 C CD  . GLU E 5 31  ? 28.022 4.995   -28.166 1.00 28.07  ?  30  GLU E CD  1 
ATOM   4941 O OE1 . GLU E 5 31  ? 26.820 5.102   -27.890 1.00 32.74  ?  30  GLU E OE1 1 
ATOM   4942 O OE2 . GLU E 5 31  ? 28.807 5.961   -28.053 1.00 29.26  -1 30  GLU E OE2 1 
ATOM   4943 N N   . TYR E 5 32  ? 26.000 0.375   -30.649 1.00 22.77  ?  31  TYR E N   1 
ATOM   4944 C CA  . TYR E 5 32  ? 24.694 -0.242  -30.774 1.00 23.58  ?  31  TYR E CA  1 
ATOM   4945 C C   . TYR E 5 32  ? 24.798 -1.555  -31.544 1.00 23.04  ?  31  TYR E C   1 
ATOM   4946 O O   . TYR E 5 32  ? 25.358 -1.588  -32.647 1.00 24.28  ?  31  TYR E O   1 
ATOM   4947 C CB  . TYR E 5 32  ? 23.736 0.710   -31.474 1.00 24.18  ?  31  TYR E CB  1 
ATOM   4948 C CG  . TYR E 5 32  ? 22.390 0.083   -31.650 1.00 26.55  ?  31  TYR E CG  1 
ATOM   4949 C CD1 . TYR E 5 32  ? 21.489 0.063   -30.604 1.00 23.81  ?  31  TYR E CD1 1 
ATOM   4950 C CD2 . TYR E 5 32  ? 22.035 -0.555  -32.849 1.00 26.49  ?  31  TYR E CD2 1 
ATOM   4951 C CE1 . TYR E 5 32  ? 20.246 -0.528  -30.751 1.00 24.59  ?  31  TYR E CE1 1 
ATOM   4952 C CE2 . TYR E 5 32  ? 20.778 -1.133  -33.014 1.00 24.22  ?  31  TYR E CE2 1 
ATOM   4953 C CZ  . TYR E 5 32  ? 19.891 -1.125  -31.951 1.00 27.09  ?  31  TYR E CZ  1 
ATOM   4954 O OH  . TYR E 5 32  ? 18.642 -1.691  -32.053 1.00 23.22  ?  31  TYR E OH  1 
ATOM   4955 N N   . MET E 5 33  ? 24.289 -2.641  -30.947 1.00 24.57  ?  32  MET E N   1 
ATOM   4956 C CA  . MET E 5 33  ? 24.186 -3.920  -31.652 1.00 25.44  ?  32  MET E CA  1 
ATOM   4957 C C   . MET E 5 33  ? 22.838 -4.535  -31.341 1.00 24.60  ?  32  MET E C   1 
ATOM   4958 O O   . MET E 5 33  ? 22.342 -4.413  -30.220 1.00 23.09  ?  32  MET E O   1 
ATOM   4959 C CB  . MET E 5 33  ? 25.322 -4.903  -31.267 1.00 20.41  ?  32  MET E CB  1 
ATOM   4960 C CG  . MET E 5 33  ? 26.733 -4.336  -31.595 1.00 20.19  ?  32  MET E CG  1 
ATOM   4961 S SD  . MET E 5 33  ? 28.092 -5.446  -31.120 1.00 23.79  ?  32  MET E SD  1 
ATOM   4962 C CE  . MET E 5 33  ? 27.843 -6.777  -32.344 1.00 20.18  ?  32  MET E CE  1 
ATOM   4963 N N   . SER E 5 34  ? 22.252 -5.211  -32.331 1.00 22.64  ?  33  SER E N   1 
ATOM   4964 C CA  . SER E 5 34  ? 20.931 -5.777  -32.164 1.00 22.10  ?  33  SER E CA  1 
ATOM   4965 C C   . SER E 5 34  ? 20.834 -7.153  -32.823 1.00 24.41  ?  33  SER E C   1 
ATOM   4966 O O   . SER E 5 34  ? 21.397 -7.380  -33.893 1.00 25.19  ?  33  SER E O   1 
ATOM   4967 C CB  . SER E 5 34  ? 19.872 -4.850  -32.796 1.00 25.30  ?  33  SER E CB  1 
ATOM   4968 O OG  . SER E 5 34  ? 18.566 -5.386  -32.625 1.00 27.01  ?  33  SER E OG  1 
ATOM   4969 N N   . TRP E 5 35  ? 20.043 -8.035  -32.218 1.00 24.47  ?  34  TRP E N   1 
ATOM   4970 C CA  . TRP E 5 35  ? 19.719 -9.333  -32.808 1.00 25.91  ?  34  TRP E CA  1 
ATOM   4971 C C   . TRP E 5 35  ? 18.255 -9.366  -33.246 1.00 25.31  ?  34  TRP E C   1 
ATOM   4972 O O   . TRP E 5 35  ? 17.365 -8.854  -32.546 1.00 24.67  ?  34  TRP E O   1 
ATOM   4973 C CB  . TRP E 5 35  ? 19.981 -10.489 -31.840 1.00 23.76  ?  34  TRP E CB  1 
ATOM   4974 C CG  . TRP E 5 35  ? 21.410 -11.036 -31.865 1.00 25.33  ?  34  TRP E CG  1 
ATOM   4975 C CD1 . TRP E 5 35  ? 22.374 -10.847 -30.906 1.00 24.01  ?  34  TRP E CD1 1 
ATOM   4976 C CD2 . TRP E 5 35  ? 22.033 -11.818 -32.912 1.00 24.58  ?  34  TRP E CD2 1 
ATOM   4977 N NE1 . TRP E 5 35  ? 23.555 -11.471 -31.282 1.00 28.23  ?  34  TRP E NE1 1 
ATOM   4978 C CE2 . TRP E 5 35  ? 23.371 -12.082 -32.498 1.00 25.86  ?  34  TRP E CE2 1 
ATOM   4979 C CE3 . TRP E 5 35  ? 21.590 -12.329 -34.149 1.00 22.87  ?  34  TRP E CE3 1 
ATOM   4980 C CZ2 . TRP E 5 35  ? 24.258 -12.845 -33.264 1.00 23.24  ?  34  TRP E CZ2 1 
ATOM   4981 C CZ3 . TRP E 5 35  ? 22.484 -13.070 -34.928 1.00 22.45  ?  34  TRP E CZ3 1 
ATOM   4982 C CH2 . TRP E 5 35  ? 23.806 -13.323 -34.478 1.00 25.39  ?  34  TRP E CH2 1 
ATOM   4983 N N   . TYR E 5 36  ? 18.021 -9.982  -34.407 1.00 26.24  ?  35  TYR E N   1 
ATOM   4984 C CA  . TYR E 5 36  ? 16.689 -10.180 -34.971 1.00 22.70  ?  35  TYR E CA  1 
ATOM   4985 C C   . TYR E 5 36  ? 16.541 -11.599 -35.507 1.00 24.37  ?  35  TYR E C   1 
ATOM   4986 O O   . TYR E 5 36  ? 17.518 -12.228 -35.931 1.00 25.88  ?  35  TYR E O   1 
ATOM   4987 C CB  . TYR E 5 36  ? 16.432 -9.238  -36.163 1.00 27.15  ?  35  TYR E CB  1 
ATOM   4988 C CG  . TYR E 5 36  ? 16.684 -7.781  -35.951 1.00 28.97  ?  35  TYR E CG  1 
ATOM   4989 C CD1 . TYR E 5 36  ? 17.941 -7.233  -36.185 1.00 25.93  ?  35  TYR E CD1 1 
ATOM   4990 C CD2 . TYR E 5 36  ? 15.634 -6.920  -35.601 1.00 29.22  ?  35  TYR E CD2 1 
ATOM   4991 C CE1 . TYR E 5 36  ? 18.158 -5.870  -36.040 1.00 30.67  ?  35  TYR E CE1 1 
ATOM   4992 C CE2 . TYR E 5 36  ? 15.851 -5.536  -35.439 1.00 29.95  ?  35  TYR E CE2 1 
ATOM   4993 C CZ  . TYR E 5 36  ? 17.110 -5.031  -35.661 1.00 30.64  ?  35  TYR E CZ  1 
ATOM   4994 O OH  . TYR E 5 36  ? 17.323 -3.682  -35.510 1.00 44.31  ?  35  TYR E OH  1 
ATOM   4995 N N   . ARG E 5 37  ? 15.303 -12.081 -35.580 1.00 24.18  ?  36  ARG E N   1 
ATOM   4996 C CA  . ARG E 5 37  ? 15.039 -13.310 -36.324 1.00 24.84  ?  36  ARG E CA  1 
ATOM   4997 C C   . ARG E 5 37  ? 14.010 -13.051 -37.417 1.00 29.27  ?  36  ARG E C   1 
ATOM   4998 O O   . ARG E 5 37  ? 13.019 -12.331 -37.200 1.00 28.67  ?  36  ARG E O   1 
ATOM   4999 C CB  . ARG E 5 37  ? 14.581 -14.454 -35.400 1.00 26.19  ?  36  ARG E CB  1 
ATOM   5000 C CG  . ARG E 5 37  ? 13.393 -14.141 -34.509 1.00 26.22  ?  36  ARG E CG  1 
ATOM   5001 C CD  . ARG E 5 37  ? 13.003 -15.367 -33.761 1.00 32.27  ?  36  ARG E CD  1 
ATOM   5002 N NE  . ARG E 5 37  ? 12.362 -16.340 -34.637 1.00 28.92  ?  36  ARG E NE  1 
ATOM   5003 C CZ  . ARG E 5 37  ? 11.957 -17.544 -34.238 1.00 30.72  ?  36  ARG E CZ  1 
ATOM   5004 N NH1 . ARG E 5 37  ? 12.133 -17.932 -32.971 1.00 23.89  ?  36  ARG E NH1 1 
ATOM   5005 N NH2 . ARG E 5 37  ? 11.384 -18.365 -35.112 1.00 27.27  ?  36  ARG E NH2 1 
ATOM   5006 N N   . GLN E 5 38  ? 14.257 -13.631 -38.597 1.00 27.32  ?  37  GLN E N   1 
ATOM   5007 C CA  . GLN E 5 38  ? 13.350 -13.530 -39.742 1.00 25.59  ?  37  GLN E CA  1 
ATOM   5008 C C   . GLN E 5 38  ? 12.840 -14.914 -40.149 1.00 29.04  ?  37  GLN E C   1 
ATOM   5009 O O   . GLN E 5 38  ? 13.600 -15.723 -40.691 1.00 24.56  ?  37  GLN E O   1 
ATOM   5010 C CB  . GLN E 5 38  ? 14.044 -12.859 -40.933 1.00 25.38  ?  37  GLN E CB  1 
ATOM   5011 C CG  . GLN E 5 38  ? 13.098 -12.667 -42.135 1.00 26.77  ?  37  GLN E CG  1 
ATOM   5012 C CD  . GLN E 5 38  ? 13.786 -12.061 -43.344 1.00 27.49  ?  37  GLN E CD  1 
ATOM   5013 O OE1 . GLN E 5 38  ? 14.875 -12.484 -43.723 1.00 31.51  ?  37  GLN E OE1 1 
ATOM   5014 N NE2 . GLN E 5 38  ? 13.163 -11.052 -43.945 1.00 29.81  ?  37  GLN E NE2 1 
ATOM   5015 N N   . ASP E 5 39  ? 11.569 -15.168 -39.916 1.00 25.30  ?  38  ASP E N   1 
ATOM   5016 C CA  . ASP E 5 39  ? 10.899 -16.365 -40.398 1.00 29.98  ?  38  ASP E CA  1 
ATOM   5017 C C   . ASP E 5 39  ? 10.545 -16.200 -41.890 1.00 31.16  ?  38  ASP E C   1 
ATOM   5018 O O   . ASP E 5 39  ? 10.398 -15.079 -42.382 1.00 31.03  ?  38  ASP E O   1 
ATOM   5019 C CB  . ASP E 5 39  ? 9.630  -16.638 -39.565 1.00 28.99  ?  38  ASP E CB  1 
ATOM   5020 C CG  . ASP E 5 39  ? 9.925  -17.288 -38.196 1.00 34.65  ?  38  ASP E CG  1 
ATOM   5021 O OD1 . ASP E 5 39  ? 11.075 -17.691 -37.904 1.00 35.09  ?  38  ASP E OD1 1 
ATOM   5022 O OD2 . ASP E 5 39  ? 8.985  -17.411 -37.388 1.00 41.60  -1 38  ASP E OD2 1 
ATOM   5023 N N   . PRO E 5 40  ? 10.445 -17.292 -42.654 1.00 31.19  ?  39  PRO E N   1 
ATOM   5024 C CA  . PRO E 5 40  ? 10.271 -17.143 -44.108 1.00 28.34  ?  39  PRO E CA  1 
ATOM   5025 C C   . PRO E 5 40  ? 9.039  -16.302 -44.444 1.00 26.44  ?  39  PRO E C   1 
ATOM   5026 O O   . PRO E 5 40  ? 7.970  -16.443 -43.840 1.00 34.31  ?  39  PRO E O   1 
ATOM   5027 C CB  . PRO E 5 40  ? 10.134 -18.590 -44.611 1.00 34.30  ?  39  PRO E CB  1 
ATOM   5028 C CG  . PRO E 5 40  ? 10.710 -19.451 -43.485 1.00 38.47  ?  39  PRO E CG  1 
ATOM   5029 C CD  . PRO E 5 40  ? 10.348 -18.703 -42.220 1.00 28.65  ?  39  PRO E CD  1 
ATOM   5030 N N   . GLY E 5 41  ? 9.210  -15.395 -45.388 1.00 31.39  ?  40  GLY E N   1 
ATOM   5031 C CA  . GLY E 5 41  ? 8.128  -14.538 -45.810 1.00 34.35  ?  40  GLY E CA  1 
ATOM   5032 C C   . GLY E 5 41  ? 7.878  -13.308 -44.959 1.00 38.98  ?  40  GLY E C   1 
ATOM   5033 O O   . GLY E 5 41  ? 7.179  -12.393 -45.425 1.00 34.04  ?  40  GLY E O   1 
ATOM   5034 N N   . LEU E 5 42  ? 8.444  -13.221 -43.750 1.00 32.02  ?  41  LEU E N   1 
ATOM   5035 C CA  . LEU E 5 42  ? 8.093  -12.159 -42.809 1.00 30.18  ?  41  LEU E CA  1 
ATOM   5036 C C   . LEU E 5 42  ? 9.254  -11.180 -42.622 1.00 32.73  ?  41  LEU E C   1 
ATOM   5037 O O   . LEU E 5 42  ? 10.338 -11.307 -43.228 1.00 29.24  ?  41  LEU E O   1 
ATOM   5038 C CB  . LEU E 5 42  ? 7.656  -12.763 -41.470 1.00 30.06  ?  41  LEU E CB  1 
ATOM   5039 C CG  . LEU E 5 42  ? 6.563  -13.825 -41.588 1.00 34.59  ?  41  LEU E CG  1 
ATOM   5040 C CD1 . LEU E 5 42  ? 6.359  -14.498 -40.259 1.00 38.71  ?  41  LEU E CD1 1 
ATOM   5041 C CD2 . LEU E 5 42  ? 5.264  -13.200 -42.025 1.00 34.66  ?  41  LEU E CD2 1 
ATOM   5042 N N   . GLY E 5 43  ? 9.005  -10.174 -41.769 1.00 34.63  ?  42  GLY E N   1 
ATOM   5043 C CA  . GLY E 5 43  ? 10.003 -9.179  -41.431 1.00 30.65  ?  42  GLY E CA  1 
ATOM   5044 C C   . GLY E 5 43  ? 10.861 -9.640  -40.259 1.00 32.93  ?  42  GLY E C   1 
ATOM   5045 O O   . GLY E 5 43  ? 10.725 -10.758 -39.764 1.00 27.51  ?  42  GLY E O   1 
ATOM   5046 N N   . LEU E 5 44  ? 11.761 -8.748  -39.821 1.00 31.73  ?  43  LEU E N   1 
ATOM   5047 C CA  . LEU E 5 44  ? 12.713 -9.051  -38.754 1.00 26.65  ?  43  LEU E CA  1 
ATOM   5048 C C   . LEU E 5 44  ? 12.083 -8.766  -37.397 1.00 28.58  ?  43  LEU E C   1 
ATOM   5049 O O   . LEU E 5 44  ? 11.561 -7.678  -37.174 1.00 34.41  ?  43  LEU E O   1 
ATOM   5050 C CB  . LEU E 5 44  ? 13.981 -8.216  -38.940 1.00 30.16  ?  43  LEU E CB  1 
ATOM   5051 C CG  . LEU E 5 44  ? 15.033 -8.775  -39.905 1.00 29.37  ?  43  LEU E CG  1 
ATOM   5052 C CD1 . LEU E 5 44  ? 14.495 -8.960  -41.335 1.00 27.84  ?  43  LEU E CD1 1 
ATOM   5053 C CD2 . LEU E 5 44  ? 16.254 -7.884  -39.910 1.00 27.18  ?  43  LEU E CD2 1 
ATOM   5054 N N   . ARG E 5 45  ? 12.103 -9.745  -36.504 1.00 27.96  ?  44  ARG E N   1 
ATOM   5055 C CA  . ARG E 5 45  ? 11.585 -9.574  -35.162 1.00 26.99  ?  44  ARG E CA  1 
ATOM   5056 C C   . ARG E 5 45  ? 12.763 -9.389  -34.206 1.00 29.64  ?  44  ARG E C   1 
ATOM   5057 O O   . ARG E 5 45  ? 13.659 -10.240 -34.140 1.00 25.99  ?  44  ARG E O   1 
ATOM   5058 C CB  . ARG E 5 45  ? 10.727 -10.765 -34.756 1.00 27.57  ?  44  ARG E CB  1 
ATOM   5059 C CG  . ARG E 5 45  ? 9.607  -11.111 -35.768 1.00 36.00  ?  44  ARG E CG  1 
ATOM   5060 C CD  . ARG E 5 45  ? 8.365  -10.223 -35.579 1.00 36.90  ?  44  ARG E CD  1 
ATOM   5061 N NE  . ARG E 5 45  ? 8.351  -9.165  -36.592 1.00 42.23  ?  44  ARG E NE  1 
ATOM   5062 C CZ  . ARG E 5 45  ? 7.765  -9.290  -37.785 1.00 39.58  ?  44  ARG E CZ  1 
ATOM   5063 N NH1 . ARG E 5 45  ? 7.130  -10.420 -38.098 1.00 41.12  ?  44  ARG E NH1 1 
ATOM   5064 N NH2 . ARG E 5 45  ? 7.802  -8.286  -38.658 1.00 38.03  ?  44  ARG E NH2 1 
ATOM   5065 N N   . GLN E 5 46  ? 12.747 -8.293  -33.450 1.00 25.63  ?  45  GLN E N   1 
ATOM   5066 C CA  . GLN E 5 46  ? 13.885 -7.976  -32.594 1.00 28.26  ?  45  GLN E CA  1 
ATOM   5067 C C   . GLN E 5 46  ? 13.894 -8.899  -31.376 1.00 23.42  ?  45  GLN E C   1 
ATOM   5068 O O   . GLN E 5 46  ? 12.862 -9.119  -30.741 1.00 27.65  ?  45  GLN E O   1 
ATOM   5069 C CB  . GLN E 5 46  ? 13.834 -6.501  -32.169 1.00 29.54  ?  45  GLN E CB  1 
ATOM   5070 C CG  . GLN E 5 46  ? 15.170 -5.960  -31.594 1.00 25.21  ?  45  GLN E CG  1 
ATOM   5071 C CD  . GLN E 5 46  ? 15.100 -4.450  -31.337 1.00 25.32  ?  45  GLN E CD  1 
ATOM   5072 O OE1 . GLN E 5 46  ? 14.097 -3.942  -30.829 1.00 25.33  ?  45  GLN E OE1 1 
ATOM   5073 N NE2 . GLN E 5 46  ? 16.148 -3.738  -31.711 1.00 21.23  ?  45  GLN E NE2 1 
ATOM   5074 N N   . ILE E 5 47  ? 15.066 -9.445  -31.055 1.00 24.94  ?  46  ILE E N   1 
ATOM   5075 C CA  . ILE E 5 47  ? 15.204 -10.402 -29.956 1.00 26.01  ?  46  ILE E CA  1 
ATOM   5076 C C   . ILE E 5 47  ? 15.741 -9.693  -28.705 1.00 27.56  ?  46  ILE E C   1 
ATOM   5077 O O   . ILE E 5 47  ? 15.095 -9.690  -27.652 1.00 28.22  ?  46  ILE E O   1 
ATOM   5078 C CB  . ILE E 5 47  ? 16.125 -11.570 -30.377 1.00 24.92  ?  46  ILE E CB  1 
ATOM   5079 C CG1 . ILE E 5 47  ? 15.574 -12.264 -31.643 1.00 23.61  ?  46  ILE E CG1 1 
ATOM   5080 C CG2 . ILE E 5 47  ? 16.359 -12.560 -29.199 1.00 23.40  ?  46  ILE E CG2 1 
ATOM   5081 C CD1 . ILE E 5 47  ? 16.579 -13.194 -32.266 1.00 27.76  ?  46  ILE E CD1 1 
ATOM   5082 N N   . TYR E 5 48  ? 16.946 -9.132  -28.805 1.00 27.61  ?  47  TYR E N   1 
ATOM   5083 C CA  . TYR E 5 48  ? 17.587 -8.334  -27.764 1.00 27.71  ?  47  TYR E CA  1 
ATOM   5084 C C   . TYR E 5 48  ? 18.422 -7.283  -28.469 1.00 23.75  ?  47  TYR E C   1 
ATOM   5085 O O   . TYR E 5 48  ? 18.908 -7.518  -29.573 1.00 22.19  ?  47  TYR E O   1 
ATOM   5086 C CB  . TYR E 5 48  ? 18.533 -9.159  -26.856 1.00 26.96  ?  47  TYR E CB  1 
ATOM   5087 C CG  . TYR E 5 48  ? 17.931 -9.858  -25.671 1.00 26.04  ?  47  TYR E CG  1 
ATOM   5088 C CD1 . TYR E 5 48  ? 17.821 -9.231  -24.427 1.00 27.97  ?  47  TYR E CD1 1 
ATOM   5089 C CD2 . TYR E 5 48  ? 17.517 -11.169 -25.781 1.00 30.08  ?  47  TYR E CD2 1 
ATOM   5090 C CE1 . TYR E 5 48  ? 17.272 -9.910  -23.323 1.00 30.56  ?  47  TYR E CE1 1 
ATOM   5091 C CE2 . TYR E 5 48  ? 16.980 -11.836 -24.729 1.00 27.63  ?  47  TYR E CE2 1 
ATOM   5092 C CZ  . TYR E 5 48  ? 16.863 -11.216 -23.498 1.00 30.40  ?  47  TYR E CZ  1 
ATOM   5093 O OH  . TYR E 5 48  ? 16.329 -11.954 -22.489 1.00 30.88  ?  47  TYR E OH  1 
ATOM   5094 N N   . TYR E 5 49  ? 18.635 -6.139  -27.818 1.00 23.75  ?  48  TYR E N   1 
ATOM   5095 C CA  . TYR E 5 49  ? 19.564 -5.183  -28.380 1.00 21.70  ?  48  TYR E CA  1 
ATOM   5096 C C   . TYR E 5 49  ? 20.369 -4.572  -27.251 1.00 22.61  ?  48  TYR E C   1 
ATOM   5097 O O   . TYR E 5 49  ? 19.989 -4.642  -26.089 1.00 24.17  ?  48  TYR E O   1 
ATOM   5098 C CB  . TYR E 5 49  ? 18.863 -4.086  -29.212 1.00 23.49  ?  48  TYR E CB  1 
ATOM   5099 C CG  . TYR E 5 49  ? 17.815 -3.321  -28.446 1.00 25.64  ?  48  TYR E CG  1 
ATOM   5100 C CD1 . TYR E 5 49  ? 16.549 -3.861  -28.257 1.00 26.65  ?  48  TYR E CD1 1 
ATOM   5101 C CD2 . TYR E 5 49  ? 18.094 -2.082  -27.888 1.00 26.30  ?  48  TYR E CD2 1 
ATOM   5102 C CE1 . TYR E 5 49  ? 15.593 -3.188  -27.544 1.00 26.13  ?  48  TYR E CE1 1 
ATOM   5103 C CE2 . TYR E 5 49  ? 17.121 -1.391  -27.165 1.00 26.08  ?  48  TYR E CE2 1 
ATOM   5104 C CZ  . TYR E 5 49  ? 15.886 -1.951  -26.997 1.00 30.14  ?  48  TYR E CZ  1 
ATOM   5105 O OH  . TYR E 5 49  ? 14.904 -1.295  -26.297 1.00 29.43  ?  48  TYR E OH  1 
ATOM   5106 N N   . SER E 5 50  ? 21.486 -3.958  -27.621 1.00 22.72  ?  49  SER E N   1 
ATOM   5107 C CA  . SER E 5 50  ? 22.459 -3.424  -26.669 1.00 21.81  ?  49  SER E CA  1 
ATOM   5108 C C   . SER E 5 50  ? 22.863 -2.016  -27.079 1.00 22.72  ?  49  SER E C   1 
ATOM   5109 O O   . SER E 5 50  ? 23.558 -1.834  -28.077 1.00 20.62  ?  49  SER E O   1 
ATOM   5110 C CB  . SER E 5 50  ? 23.707 -4.306  -26.580 1.00 23.58  ?  49  SER E CB  1 
ATOM   5111 O OG  . SER E 5 50  ? 24.700 -3.669  -25.756 1.00 22.59  ?  49  SER E OG  1 
ATOM   5112 N N   . MET E 5 51  ? 22.482 -1.027  -26.265 1.00 26.71  ?  50  MET E N   1 
ATOM   5113 C CA  . MET E 5 51  ? 22.826 0.354   -26.588 1.00 26.24  ?  50  MET E CA  1 
ATOM   5114 C C   . MET E 5 51  ? 24.304 0.646   -26.373 1.00 28.78  ?  50  MET E C   1 
ATOM   5115 O O   . MET E 5 51  ? 24.806 1.630   -26.930 1.00 26.20  ?  50  MET E O   1 
ATOM   5116 C CB  . MET E 5 51  ? 21.961 1.326   -25.779 1.00 21.87  ?  50  MET E CB  1 
ATOM   5117 C CG  . MET E 5 51  ? 20.462 1.142   -26.003 1.00 29.12  ?  50  MET E CG  1 
ATOM   5118 S SD  . MET E 5 51  ? 19.474 2.363   -25.076 1.00 32.82  ?  50  MET E SD  1 
ATOM   5119 C CE  . MET E 5 51  ? 19.913 3.851   -25.953 1.00 21.92  ?  50  MET E CE  1 
ATOM   5120 N N   . ASN E 5 52  ? 25.015 -0.150  -25.592 1.00 23.20  ?  51  ASN E N   1 
ATOM   5121 C CA  . ASN E 5 52  ? 26.467 0.020   -25.321 1.00 25.73  ?  51  ASN E CA  1 
ATOM   5122 C C   . ASN E 5 52  ? 26.914 -1.097  -24.387 1.00 25.40  ?  51  ASN E C   1 
ATOM   5123 O O   . ASN E 5 52  ? 26.098 -1.837  -23.923 1.00 24.38  ?  51  ASN E O   1 
ATOM   5124 C CB  . ASN E 5 52  ? 26.842 1.273   -24.511 1.00 28.62  ?  51  ASN E CB  1 
ATOM   5125 C CG  . ASN E 5 52  ? 28.113 1.967   -24.961 1.00 31.25  ?  51  ASN E CG  1 
ATOM   5126 O OD1 . ASN E 5 52  ? 29.067 1.322   -25.337 1.00 26.48  ?  51  ASN E OD1 1 
ATOM   5127 N ND2 . ASN E 5 52  ? 28.151 3.269   -24.845 1.00 28.68  ?  51  ASN E ND2 1 
ATOM   5128 N N   . VAL E 5 53  ? 28.194 -1.104  -24.056 1.00 26.84  ?  52  VAL E N   1 
ATOM   5129 C CA  . VAL E 5 53  ? 28.806 -2.058  -23.111 1.00 23.91  ?  52  VAL E CA  1 
ATOM   5130 C C   . VAL E 5 53  ? 27.973 -2.113  -21.840 1.00 24.41  ?  52  VAL E C   1 
ATOM   5131 O O   . VAL E 5 53  ? 27.676 -1.058  -21.305 1.00 27.35  ?  52  VAL E O   1 
ATOM   5132 C CB  . VAL E 5 53  ? 30.267 -1.703  -22.803 1.00 31.36  ?  52  VAL E CB  1 
ATOM   5133 C CG1 . VAL E 5 53  ? 30.836 -2.673  -21.800 1.00 28.95  ?  52  VAL E CG1 1 
ATOM   5134 C CG2 . VAL E 5 53  ? 31.112 -1.663  -24.056 1.00 31.38  ?  52  VAL E CG2 1 
ATOM   5135 N N   . GLU E 5 54  ? 27.558 -3.324  -21.512 1.00 22.52  ?  53  GLU E N   1 
ATOM   5136 C CA  . GLU E 5 54  ? 26.884 -3.687  -20.272 1.00 27.80  ?  53  GLU E CA  1 
ATOM   5137 C C   . GLU E 5 54  ? 25.454 -3.157  -20.219 1.00 28.16  ?  53  GLU E C   1 
ATOM   5138 O O   . GLU E 5 54  ? 24.846 -3.099  -19.146 1.00 30.81  ?  53  GLU E O   1 
ATOM   5139 C CB  . GLU E 5 54  ? 27.692 -3.218  -19.036 1.00 28.74  ?  53  GLU E CB  1 
ATOM   5140 C CG  . GLU E 5 54  ? 28.985 -4.007  -18.779 1.00 31.59  ?  53  GLU E CG  1 
ATOM   5141 C CD  . GLU E 5 54  ? 28.771 -5.503  -18.495 1.00 35.90  ?  53  GLU E CD  1 
ATOM   5142 O OE1 . GLU E 5 54  ? 27.644 -5.935  -18.203 1.00 37.42  ?  53  GLU E OE1 1 
ATOM   5143 O OE2 . GLU E 5 54  ? 29.751 -6.269  -18.568 1.00 40.19  -1 53  GLU E OE2 1 
ATOM   5144 N N   . VAL E 5 55  ? 24.905 -2.761  -21.360 1.00 23.54  ?  54  VAL E N   1 
ATOM   5145 C CA  . VAL E 5 55  ? 23.511 -2.335  -21.468 1.00 25.47  ?  54  VAL E CA  1 
ATOM   5146 C C   . VAL E 5 55  ? 22.807 -3.286  -22.432 1.00 26.81  ?  54  VAL E C   1 
ATOM   5147 O O   . VAL E 5 55  ? 23.187 -3.374  -23.603 1.00 23.27  ?  54  VAL E O   1 
ATOM   5148 C CB  . VAL E 5 55  ? 23.389 -0.885  -21.976 1.00 29.88  ?  54  VAL E CB  1 
ATOM   5149 C CG1 . VAL E 5 55  ? 21.912 -0.466  -22.028 1.00 26.35  ?  54  VAL E CG1 1 
ATOM   5150 C CG2 . VAL E 5 55  ? 24.240 0.078   -21.113 1.00 28.55  ?  54  VAL E CG2 1 
ATOM   5151 N N   . THR E 5 56  ? 21.794 -3.993  -21.947 1.00 26.07  ?  55  THR E N   1 
ATOM   5152 C CA  . THR E 5 56  ? 20.970 -4.815  -22.815 1.00 28.54  ?  55  THR E CA  1 
ATOM   5153 C C   . THR E 5 56  ? 19.499 -4.550  -22.521 1.00 29.69  ?  55  THR E C   1 
ATOM   5154 O O   . THR E 5 56  ? 19.137 -4.151  -21.413 1.00 24.95  ?  55  THR E O   1 
ATOM   5155 C CB  . THR E 5 56  ? 21.288 -6.317  -22.648 1.00 26.43  ?  55  THR E CB  1 
ATOM   5156 O OG1 . THR E 5 56  ? 20.856 -6.745  -21.356 1.00 29.50  ?  55  THR E OG1 1 
ATOM   5157 C CG2 . THR E 5 56  ? 22.799 -6.587  -22.834 1.00 22.42  ?  55  THR E CG2 1 
ATOM   5158 N N   . ASP E 5 57  ? 18.656 -4.754  -23.541 1.00 24.69  ?  56  ASP E N   1 
ATOM   5159 C CA  . ASP E 5 57  ? 17.215 -4.601  -23.417 1.00 27.19  ?  56  ASP E CA  1 
ATOM   5160 C C   . ASP E 5 57  ? 16.514 -5.663  -24.273 1.00 28.78  ?  56  ASP E C   1 
ATOM   5161 O O   . ASP E 5 57  ? 16.983 -6.019  -25.354 1.00 24.86  ?  56  ASP E O   1 
ATOM   5162 C CB  . ASP E 5 57  ? 16.771 -3.184  -23.851 1.00 26.03  ?  56  ASP E CB  1 
ATOM   5163 C CG  . ASP E 5 57  ? 17.204 -2.066  -22.857 1.00 30.92  ?  56  ASP E CG  1 
ATOM   5164 O OD1 . ASP E 5 57  ? 16.702 -2.063  -21.718 1.00 29.82  ?  56  ASP E OD1 1 
ATOM   5165 O OD2 . ASP E 5 57  ? 18.009 -1.167  -23.239 1.00 29.79  -1 56  ASP E OD2 1 
ATOM   5166 N N   . LYS E 5 58  ? 15.371 -6.134  -23.790 1.00 25.83  ?  57  LYS E N   1 
ATOM   5167 C CA  . LYS E 5 58  ? 14.557 -7.094  -24.526 1.00 33.72  ?  57  LYS E CA  1 
ATOM   5168 C C   . LYS E 5 58  ? 13.894 -6.466  -25.748 1.00 28.35  ?  57  LYS E C   1 
ATOM   5169 O O   . LYS E 5 58  ? 13.424 -5.328  -25.714 1.00 26.87  ?  57  LYS E O   1 
ATOM   5170 C CB  . LYS E 5 58  ? 13.486 -7.666  -23.607 1.00 29.17  ?  57  LYS E CB  1 
ATOM   5171 C CG  . LYS E 5 58  ? 14.045 -8.550  -22.540 1.00 30.82  ?  57  LYS E CG  1 
ATOM   5172 C CD  . LYS E 5 58  ? 12.968 -8.829  -21.507 1.00 42.45  ?  57  LYS E CD  1 
ATOM   5173 C CE  . LYS E 5 58  ? 13.365 -9.933  -20.555 1.00 41.09  ?  57  LYS E CE  1 
ATOM   5174 N NZ  . LYS E 5 58  ? 12.211 -10.308 -19.670 1.00 44.90  ?  57  LYS E NZ  1 
ATOM   5175 N N   . GLY E 5 59  ? 13.883 -7.204  -26.846 1.00 32.73  ?  58  GLY E N   1 
ATOM   5176 C CA  . GLY E 5 59  ? 13.060 -6.849  -27.988 1.00 30.97  ?  58  GLY E CA  1 
ATOM   5177 C C   . GLY E 5 59  ? 11.688 -7.479  -27.822 1.00 30.22  ?  58  GLY E C   1 
ATOM   5178 O O   . GLY E 5 59  ? 11.254 -7.787  -26.713 1.00 28.26  ?  58  GLY E O   1 
ATOM   5179 N N   . ASP E 5 60  ? 11.022 -7.717  -28.955 1.00 33.84  ?  59  ASP E N   1 
ATOM   5180 C CA  . ASP E 5 60  ? 9.689  -8.309  -28.935 1.00 29.46  ?  59  ASP E CA  1 
ATOM   5181 C C   . ASP E 5 60  ? 9.698  -9.806  -28.627 1.00 30.73  ?  59  ASP E C   1 
ATOM   5182 O O   . ASP E 5 60  ? 8.730  -10.311 -28.056 1.00 29.76  ?  59  ASP E O   1 
ATOM   5183 C CB  . ASP E 5 60  ? 8.993  -8.062  -30.276 1.00 32.21  ?  59  ASP E CB  1 
ATOM   5184 C CG  . ASP E 5 60  ? 8.646  -6.598  -30.486 1.00 37.40  ?  59  ASP E CG  1 
ATOM   5185 O OD1 . ASP E 5 60  ? 8.161  -5.984  -29.528 1.00 36.80  ?  59  ASP E OD1 1 
ATOM   5186 O OD2 . ASP E 5 60  ? 8.869  -6.056  -31.599 1.00 42.91  -1 59  ASP E OD2 1 
ATOM   5187 N N   . VAL E 5 61  ? 10.749 -10.542 -28.989 1.00 30.07  ?  60  VAL E N   1 
ATOM   5188 C CA  . VAL E 5 61  ? 10.704 -11.998 -28.811 1.00 29.38  ?  60  VAL E CA  1 
ATOM   5189 C C   . VAL E 5 61  ? 11.945 -12.487 -28.070 1.00 30.67  ?  60  VAL E C   1 
ATOM   5190 O O   . VAL E 5 61  ? 12.762 -13.228 -28.642 1.00 30.78  ?  60  VAL E O   1 
ATOM   5191 C CB  . VAL E 5 61  ? 10.503 -12.710 -30.170 1.00 31.88  ?  60  VAL E CB  1 
ATOM   5192 C CG1 . VAL E 5 61  ? 9.226  -12.179 -30.815 1.00 38.45  ?  60  VAL E CG1 1 
ATOM   5193 C CG2 . VAL E 5 61  ? 11.654 -12.479 -31.140 1.00 25.49  ?  60  VAL E CG2 1 
ATOM   5194 N N   . PRO E 5 62  ? 12.116 -12.116 -26.794 1.00 31.15  ?  61  PRO E N   1 
ATOM   5195 C CA  . PRO E 5 62  ? 13.316 -12.535 -26.051 1.00 31.48  ?  61  PRO E CA  1 
ATOM   5196 C C   . PRO E 5 62  ? 13.280 -13.970 -25.529 1.00 33.34  ?  61  PRO E C   1 
ATOM   5197 O O   . PRO E 5 62  ? 14.354 -14.531 -25.257 1.00 34.11  ?  61  PRO E O   1 
ATOM   5198 C CB  . PRO E 5 62  ? 13.368 -11.534 -24.875 1.00 28.56  ?  61  PRO E CB  1 
ATOM   5199 C CG  . PRO E 5 62  ? 11.911 -11.234 -24.611 1.00 33.98  ?  61  PRO E CG  1 
ATOM   5200 C CD  . PRO E 5 62  ? 11.272 -11.189 -26.011 1.00 31.42  ?  61  PRO E CD  1 
ATOM   5201 N N   . GLU E 5 63  ? 12.106 -14.581 -25.387 1.00 30.16  ?  62  GLU E N   1 
ATOM   5202 C CA  . GLU E 5 63  ? 11.996 -15.890 -24.745 1.00 35.98  ?  62  GLU E CA  1 
ATOM   5203 C C   . GLU E 5 63  ? 12.857 -16.937 -25.449 1.00 33.34  ?  62  GLU E C   1 
ATOM   5204 O O   . GLU E 5 63  ? 12.855 -17.050 -26.678 1.00 26.93  ?  62  GLU E O   1 
ATOM   5205 C CB  . GLU E 5 63  ? 10.530 -16.334 -24.705 1.00 36.83  ?  62  GLU E CB  1 
ATOM   5206 C CG  . GLU E 5 63  ? 9.590  -15.336 -23.998 1.00 36.49  ?  62  GLU E CG  1 
ATOM   5207 C CD  . GLU E 5 63  ? 9.138  -14.174 -24.903 1.00 47.32  ?  62  GLU E CD  1 
ATOM   5208 O OE1 . GLU E 5 63  ? 8.439  -13.275 -24.391 1.00 47.32  ?  62  GLU E OE1 1 
ATOM   5209 O OE2 . GLU E 5 63  ? 9.478  -14.154 -26.118 1.00 35.38  -1 62  GLU E OE2 1 
ATOM   5210 N N   . GLY E 5 64  ? 13.615 -17.688 -24.653 1.00 35.37  ?  63  GLY E N   1 
ATOM   5211 C CA  . GLY E 5 64  ? 14.500 -18.726 -25.149 1.00 28.56  ?  63  GLY E CA  1 
ATOM   5212 C C   . GLY E 5 64  ? 15.845 -18.225 -25.609 1.00 33.40  ?  63  GLY E C   1 
ATOM   5213 O O   . GLY E 5 64  ? 16.619 -19.012 -26.172 1.00 28.30  ?  63  GLY E O   1 
ATOM   5214 N N   . TYR E 5 65  ? 16.138 -16.928 -25.403 1.00 30.36  ?  64  TYR E N   1 
ATOM   5215 C CA  . TYR E 5 65  ? 17.390 -16.309 -25.811 1.00 28.06  ?  64  TYR E CA  1 
ATOM   5216 C C   . TYR E 5 65  ? 17.988 -15.509 -24.657 1.00 29.20  ?  64  TYR E C   1 
ATOM   5217 O O   . TYR E 5 65  ? 17.271 -14.970 -23.805 1.00 27.03  ?  64  TYR E O   1 
ATOM   5218 C CB  . TYR E 5 65  ? 17.200 -15.356 -26.993 1.00 25.28  ?  64  TYR E CB  1 
ATOM   5219 C CG  . TYR E 5 65  ? 16.538 -15.950 -28.233 1.00 27.82  ?  64  TYR E CG  1 
ATOM   5220 C CD1 . TYR E 5 65  ? 17.274 -16.657 -29.172 1.00 25.58  ?  64  TYR E CD1 1 
ATOM   5221 C CD2 . TYR E 5 65  ? 15.185 -15.776 -28.464 1.00 28.82  ?  64  TYR E CD2 1 
ATOM   5222 C CE1 . TYR E 5 65  ? 16.663 -17.199 -30.315 1.00 27.41  ?  64  TYR E CE1 1 
ATOM   5223 C CE2 . TYR E 5 65  ? 14.566 -16.303 -29.580 1.00 27.43  ?  64  TYR E CE2 1 
ATOM   5224 C CZ  . TYR E 5 65  ? 15.304 -17.009 -30.505 1.00 30.94  ?  64  TYR E CZ  1 
ATOM   5225 O OH  . TYR E 5 65  ? 14.667 -17.504 -31.615 1.00 25.64  ?  64  TYR E OH  1 
ATOM   5226 N N   . LYS E 5 66  ? 19.313 -15.397 -24.668 1.00 26.46  ?  65  LYS E N   1 
ATOM   5227 C CA  . LYS E 5 66  ? 20.026 -14.473 -23.792 1.00 31.36  ?  65  LYS E CA  1 
ATOM   5228 C C   . LYS E 5 66  ? 21.184 -13.887 -24.576 1.00 25.52  ?  65  LYS E C   1 
ATOM   5229 O O   . LYS E 5 66  ? 21.648 -14.478 -25.547 1.00 28.47  ?  65  LYS E O   1 
ATOM   5230 C CB  . LYS E 5 66  ? 20.555 -15.145 -22.509 1.00 28.84  ?  65  LYS E CB  1 
ATOM   5231 C CG  . LYS E 5 66  ? 19.538 -15.962 -21.731 1.00 33.45  ?  65  LYS E CG  1 
ATOM   5232 C CD  . LYS E 5 66  ? 18.892 -15.189 -20.591 1.00 45.62  ?  65  LYS E CD  1 
ATOM   5233 C CE  . LYS E 5 66  ? 17.442 -15.644 -20.395 1.00 46.00  ?  65  LYS E CE  1 
ATOM   5234 N NZ  . LYS E 5 66  ? 16.504 -14.535 -19.947 1.00 49.54  ?  65  LYS E NZ  1 
ATOM   5235 N N   . VAL E 5 67  ? 21.646 -12.709 -24.151 1.00 26.19  ?  66  VAL E N   1 
ATOM   5236 C CA  . VAL E 5 67  ? 22.770 -12.029 -24.784 1.00 23.74  ?  66  VAL E CA  1 
ATOM   5237 C C   . VAL E 5 67  ? 23.688 -11.549 -23.672 1.00 29.06  ?  66  VAL E C   1 
ATOM   5238 O O   . VAL E 5 67  ? 23.357 -11.627 -22.489 1.00 25.91  ?  66  VAL E O   1 
ATOM   5239 C CB  . VAL E 5 67  ? 22.327 -10.850 -25.688 1.00 27.59  ?  66  VAL E CB  1 
ATOM   5240 C CG1 . VAL E 5 67  ? 21.409 -11.326 -26.817 1.00 22.38  ?  66  VAL E CG1 1 
ATOM   5241 C CG2 . VAL E 5 67  ? 21.590 -9.833  -24.862 1.00 27.21  ?  66  VAL E CG2 1 
ATOM   5242 N N   . SER E 5 68  ? 24.858 -11.053 -24.059 1.00 23.05  ?  67  SER E N   1 
ATOM   5243 C CA  . SER E 5 68  ? 25.666 -10.299 -23.109 1.00 28.34  ?  67  SER E CA  1 
ATOM   5244 C C   . SER E 5 68  ? 26.452 -9.259  -23.876 1.00 25.09  ?  67  SER E C   1 
ATOM   5245 O O   . SER E 5 68  ? 26.607 -9.345  -25.098 1.00 26.04  ?  67  SER E O   1 
ATOM   5246 C CB  . SER E 5 68  ? 26.617 -11.204 -22.300 1.00 30.85  ?  67  SER E CB  1 
ATOM   5247 O OG  . SER E 5 68  ? 27.506 -11.867 -23.175 1.00 31.64  ?  67  SER E OG  1 
ATOM   5248 N N   . ARG E 5 69  ? 26.942 -8.262  -23.157 1.00 24.34  ?  68  ARG E N   1 
ATOM   5249 C CA  . ARG E 5 69  ? 27.701 -7.229  -23.827 1.00 23.54  ?  68  ARG E CA  1 
ATOM   5250 C C   . ARG E 5 69  ? 28.789 -6.777  -22.853 1.00 29.78  ?  68  ARG E C   1 
ATOM   5251 O O   . ARG E 5 69  ? 28.712 -5.703  -22.228 1.00 25.98  ?  68  ARG E O   1 
ATOM   5252 C CB  . ARG E 5 69  ? 26.807 -6.066  -24.269 1.00 22.51  ?  68  ARG E CB  1 
ATOM   5253 C CG  . ARG E 5 69  ? 27.518 -5.071  -25.199 1.00 20.69  ?  68  ARG E CG  1 
ATOM   5254 C CD  . ARG E 5 69  ? 27.473 -5.569  -26.616 1.00 21.97  ?  68  ARG E CD  1 
ATOM   5255 N NE  . ARG E 5 69  ? 28.280 -4.766  -27.515 1.00 20.64  ?  68  ARG E NE  1 
ATOM   5256 C CZ  . ARG E 5 69  ? 27.918 -3.555  -27.941 1.00 25.86  ?  68  ARG E CZ  1 
ATOM   5257 N NH1 . ARG E 5 69  ? 26.767 -3.031  -27.517 1.00 22.42  ?  68  ARG E NH1 1 
ATOM   5258 N NH2 . ARG E 5 69  ? 28.688 -2.885  -28.804 1.00 22.61  ?  68  ARG E NH2 1 
ATOM   5259 N N   . LYS E 5 70  ? 29.805 -7.615  -22.722 1.00 30.36  ?  69  LYS E N   1 
ATOM   5260 C CA  . LYS E 5 70  ? 30.974 -7.373  -21.855 1.00 33.17  ?  69  LYS E CA  1 
ATOM   5261 C C   . LYS E 5 70  ? 31.936 -6.384  -22.507 1.00 33.83  ?  69  LYS E C   1 
ATOM   5262 O O   . LYS E 5 70  ? 32.648 -5.775  -21.812 1.00 30.58  ?  69  LYS E O   1 
ATOM   5263 C CB  . LYS E 5 70  ? 31.678 -8.683  -21.511 1.00 38.87  ?  69  LYS E CB  1 
ATOM   5264 C CG  . LYS E 5 70  ? 30.864 -9.670  -20.698 1.00 40.90  ?  69  LYS E CG  1 
ATOM   5265 C CD  . LYS E 5 70  ? 29.960 -9.036  -19.676 1.00 45.32  ?  69  LYS E CD  1 
ATOM   5266 C CE  . LYS E 5 70  ? 30.478 -9.089  -18.252 1.00 49.37  ?  69  LYS E CE  1 
ATOM   5267 N NZ  . LYS E 5 70  ? 29.378 -8.903  -17.289 1.00 44.33  ?  69  LYS E NZ  1 
ATOM   5268 N N   . GLU E 5 71  ? 31.953 -6.303  -23.818 1.00 25.52  ?  70  GLU E N   1 
ATOM   5269 C CA  . GLU E 5 71  ? 32.827 -5.342  -24.514 1.00 28.18  ?  70  GLU E CA  1 
ATOM   5270 C C   . GLU E 5 71  ? 32.158 -4.894  -25.805 1.00 27.60  ?  70  GLU E C   1 
ATOM   5271 O O   . GLU E 5 71  ? 31.257 -5.536  -26.234 1.00 27.35  ?  70  GLU E O   1 
ATOM   5272 C CB  . GLU E 5 71  ? 34.194 -5.930  -24.784 1.00 28.83  ?  70  GLU E CB  1 
ATOM   5273 C CG  . GLU E 5 71  ? 34.137 -6.907  -25.907 1.00 32.09  ?  70  GLU E CG  1 
ATOM   5274 C CD  . GLU E 5 71  ? 34.648 -8.279  -25.589 1.00 45.65  ?  70  GLU E CD  1 
ATOM   5275 O OE1 . GLU E 5 71  ? 35.843 -8.465  -25.800 1.00 51.93  ?  70  GLU E OE1 1 
ATOM   5276 O OE2 . GLU E 5 71  ? 33.857 -9.149  -25.235 1.00 49.99  -1 70  GLU E OE2 1 
ATOM   5277 N N   . LYS E 5 72  ? 32.655 -3.832  -26.395 1.00 25.23  ?  71  LYS E N   1 
ATOM   5278 C CA  . LYS E 5 72  ? 32.010 -3.255  -27.586 1.00 29.85  ?  71  LYS E CA  1 
ATOM   5279 C C   . LYS E 5 72  ? 32.038 -4.200  -28.780 1.00 28.55  ?  71  LYS E C   1 
ATOM   5280 O O   . LYS E 5 72  ? 31.102 -4.212  -29.479 1.00 26.31  ?  71  LYS E O   1 
ATOM   5281 C CB  . LYS E 5 72  ? 32.708 -1.955  -27.963 1.00 32.73  ?  71  LYS E CB  1 
ATOM   5282 C CG  . LYS E 5 72  ? 31.915 -0.697  -27.674 1.00 36.59  ?  71  LYS E CG  1 
ATOM   5283 C CD  . LYS E 5 72  ? 32.642 0.533   -28.027 1.00 37.68  ?  71  LYS E CD  1 
ATOM   5284 C CE  . LYS E 5 72  ? 31.986 1.767   -27.474 1.00 32.77  ?  71  LYS E CE  1 
ATOM   5285 N NZ  . LYS E 5 72  ? 31.955 1.760   -26.005 1.00 46.71  ?  71  LYS E NZ  1 
ATOM   5286 N N   . ARG E 5 73  ? 33.048 -5.036  -28.872 1.00 25.63  ?  72  ARG E N   1 
ATOM   5287 C CA  . ARG E 5 73  ? 33.251 -5.824  -30.081 1.00 29.58  ?  72  ARG E CA  1 
ATOM   5288 C C   . ARG E 5 73  ? 32.206 -6.931  -30.258 1.00 27.85  ?  72  ARG E C   1 
ATOM   5289 O O   . ARG E 5 73  ? 31.815 -7.226  -31.395 1.00 27.54  ?  72  ARG E O   1 
ATOM   5290 C CB  . ARG E 5 73  ? 34.664 -6.426  -30.062 1.00 32.67  ?  72  ARG E CB  1 
ATOM   5291 C CG  . ARG E 5 73  ? 34.842 -7.668  -30.907 1.00 40.69  ?  72  ARG E CG  1 
ATOM   5292 C CD  . ARG E 5 73  ? 36.336 -8.021  -31.088 1.00 38.33  ?  72  ARG E CD  1 
ATOM   5293 N NE  . ARG E 5 73  ? 36.598 -8.736  -32.342 1.00 41.66  ?  72  ARG E NE  1 
ATOM   5294 C CZ  . ARG E 5 73  ? 36.381 -10.040 -32.517 1.00 45.65  ?  72  ARG E CZ  1 
ATOM   5295 N NH1 . ARG E 5 73  ? 35.893 -10.783 -31.521 1.00 43.17  ?  72  ARG E NH1 1 
ATOM   5296 N NH2 . ARG E 5 73  ? 36.643 -10.603 -33.692 1.00 49.85  ?  72  ARG E NH2 1 
ATOM   5297 N N   . ASN E 5 74  ? 31.730 -7.535  -29.170 1.00 27.91  ?  73  ASN E N   1 
ATOM   5298 C CA  . ASN E 5 74  ? 31.028 -8.814  -29.208 1.00 24.50  ?  73  ASN E CA  1 
ATOM   5299 C C   . ASN E 5 74  ? 29.623 -8.717  -28.623 1.00 29.73  ?  73  ASN E C   1 
ATOM   5300 O O   . ASN E 5 74  ? 29.415 -8.097  -27.567 1.00 22.73  ?  73  ASN E O   1 
ATOM   5301 C CB  . ASN E 5 74  ? 31.822 -9.874  -28.423 1.00 27.60  ?  73  ASN E CB  1 
ATOM   5302 C CG  . ASN E 5 74  ? 33.161 -10.188 -29.075 1.00 36.48  ?  73  ASN E CG  1 
ATOM   5303 O OD1 . ASN E 5 74  ? 33.216 -10.604 -30.230 1.00 36.36  ?  73  ASN E OD1 1 
ATOM   5304 N ND2 . ASN E 5 74  ? 34.243 -9.990  -28.333 1.00 41.44  ?  73  ASN E ND2 1 
ATOM   5305 N N   . PHE E 5 75  ? 28.673 -9.402  -29.273 1.00 24.61  ?  74  PHE E N   1 
ATOM   5306 C CA  . PHE E 5 75  ? 27.277 -9.428  -28.822 1.00 22.53  ?  74  PHE E CA  1 
ATOM   5307 C C   . PHE E 5 75  ? 26.713 -10.800 -29.124 1.00 25.33  ?  74  PHE E C   1 
ATOM   5308 O O   . PHE E 5 75  ? 26.028 -10.998 -30.133 1.00 24.27  ?  74  PHE E O   1 
ATOM   5309 C CB  . PHE E 5 75  ? 26.455 -8.343  -29.524 1.00 19.57  ?  74  PHE E CB  1 
ATOM   5310 C CG  . PHE E 5 75  ? 25.082 -8.128  -28.957 1.00 22.65  ?  74  PHE E CG  1 
ATOM   5311 C CD1 . PHE E 5 75  ? 24.885 -8.037  -27.583 1.00 24.53  ?  74  PHE E CD1 1 
ATOM   5312 C CD2 . PHE E 5 75  ? 23.991 -7.949  -29.808 1.00 21.60  ?  74  PHE E CD2 1 
ATOM   5313 C CE1 . PHE E 5 75  ? 23.612 -7.802  -27.053 1.00 26.05  ?  74  PHE E CE1 1 
ATOM   5314 C CE2 . PHE E 5 75  ? 22.725 -7.699  -29.299 1.00 24.01  ?  74  PHE E CE2 1 
ATOM   5315 C CZ  . PHE E 5 75  ? 22.524 -7.630  -27.923 1.00 24.67  ?  74  PHE E CZ  1 
ATOM   5316 N N   . PRO E 5 76  ? 27.014 -11.792 -28.293 1.00 25.46  ?  75  PRO E N   1 
ATOM   5317 C CA  . PRO E 5 76  ? 26.608 -13.165 -28.622 1.00 21.15  ?  75  PRO E CA  1 
ATOM   5318 C C   . PRO E 5 76  ? 25.140 -13.425 -28.317 1.00 24.91  ?  75  PRO E C   1 
ATOM   5319 O O   . PRO E 5 76  ? 24.543 -12.836 -27.409 1.00 23.87  ?  75  PRO E O   1 
ATOM   5320 C CB  . PRO E 5 76  ? 27.522 -14.025 -27.739 1.00 24.94  ?  75  PRO E CB  1 
ATOM   5321 C CG  . PRO E 5 76  ? 27.858 -13.118 -26.543 1.00 25.38  ?  75  PRO E CG  1 
ATOM   5322 C CD  . PRO E 5 76  ? 27.920 -11.722 -27.121 1.00 22.14  ?  75  PRO E CD  1 
ATOM   5323 N N   . LEU E 5 77  ? 24.555 -14.316 -29.111 1.00 23.80  ?  76  LEU E N   1 
ATOM   5324 C CA  . LEU E 5 77  ? 23.185 -14.782 -28.912 1.00 23.07  ?  76  LEU E CA  1 
ATOM   5325 C C   . LEU E 5 77  ? 23.225 -16.198 -28.342 1.00 26.13  ?  76  LEU E C   1 
ATOM   5326 O O   . LEU E 5 77  ? 23.745 -17.116 -28.984 1.00 24.16  ?  76  LEU E O   1 
ATOM   5327 C CB  . LEU E 5 77  ? 22.413 -14.765 -30.236 1.00 23.39  ?  76  LEU E CB  1 
ATOM   5328 C CG  . LEU E 5 77  ? 20.930 -15.153 -30.165 1.00 27.29  ?  76  LEU E CG  1 
ATOM   5329 C CD1 . LEU E 5 77  ? 20.234 -14.122 -29.309 1.00 24.59  ?  76  LEU E CD1 1 
ATOM   5330 C CD2 . LEU E 5 77  ? 20.288 -15.205 -31.580 1.00 26.99  ?  76  LEU E CD2 1 
ATOM   5331 N N   . ILE E 5 78  ? 22.653 -16.396 -27.163 1.00 23.93  ?  77  ILE E N   1 
ATOM   5332 C CA  . ILE E 5 78  ? 22.756 -17.684 -26.489 1.00 26.31  ?  77  ILE E CA  1 
ATOM   5333 C C   . ILE E 5 78  ? 21.395 -18.359 -26.489 1.00 28.18  ?  77  ILE E C   1 
ATOM   5334 O O   . ILE E 5 78  ? 20.396 -17.753 -26.086 1.00 30.70  ?  77  ILE E O   1 
ATOM   5335 C CB  . ILE E 5 78  ? 23.295 -17.517 -25.060 1.00 25.35  ?  77  ILE E CB  1 
ATOM   5336 C CG1 . ILE E 5 78  ? 24.613 -16.731 -25.108 1.00 24.50  ?  77  ILE E CG1 1 
ATOM   5337 C CG2 . ILE E 5 78  ? 23.451 -18.876 -24.399 1.00 26.23  ?  77  ILE E CG2 1 
ATOM   5338 C CD1 . ILE E 5 78  ? 24.919 -15.974 -23.853 1.00 33.77  ?  77  ILE E CD1 1 
ATOM   5339 N N   . LEU E 5 79  ? 21.355 -19.614 -26.921 1.00 27.41  ?  78  LEU E N   1 
ATOM   5340 C CA  . LEU E 5 79  ? 20.124 -20.409 -26.887 1.00 26.79  ?  78  LEU E CA  1 
ATOM   5341 C C   . LEU E 5 79  ? 20.347 -21.546 -25.894 1.00 29.61  ?  78  LEU E C   1 
ATOM   5342 O O   . LEU E 5 79  ? 20.979 -22.555 -26.227 1.00 27.67  ?  78  LEU E O   1 
ATOM   5343 C CB  . LEU E 5 79  ? 19.757 -20.937 -28.273 1.00 23.18  ?  78  LEU E CB  1 
ATOM   5344 C CG  . LEU E 5 79  ? 19.052 -20.015 -29.269 1.00 25.62  ?  78  LEU E CG  1 
ATOM   5345 C CD1 . LEU E 5 79  ? 20.028 -18.926 -29.722 1.00 24.90  ?  78  LEU E CD1 1 
ATOM   5346 C CD2 . LEU E 5 79  ? 18.510 -20.805 -30.507 1.00 21.32  ?  78  LEU E CD2 1 
ATOM   5347 N N   . GLU E 5 80  ? 19.839 -21.363 -24.666 1.00 33.74  ?  79  GLU E N   1 
ATOM   5348 C CA  . GLU E 5 80  ? 20.108 -22.317 -23.593 1.00 34.09  ?  79  GLU E CA  1 
ATOM   5349 C C   . GLU E 5 80  ? 19.618 -23.705 -23.962 1.00 33.57  ?  79  GLU E C   1 
ATOM   5350 O O   . GLU E 5 80  ? 20.290 -24.703 -23.692 1.00 32.43  ?  79  GLU E O   1 
ATOM   5351 C CB  . GLU E 5 80  ? 19.448 -21.865 -22.285 1.00 38.22  ?  79  GLU E CB  1 
ATOM   5352 C CG  . GLU E 5 80  ? 20.416 -21.354 -21.219 1.00 48.44  ?  79  GLU E CG  1 
ATOM   5353 C CD  . GLU E 5 80  ? 21.342 -22.426 -20.686 1.00 47.31  ?  79  GLU E CD  1 
ATOM   5354 O OE1 . GLU E 5 80  ? 22.571 -22.236 -20.780 1.00 56.61  ?  79  GLU E OE1 1 
ATOM   5355 O OE2 . GLU E 5 80  ? 20.851 -23.453 -20.172 1.00 52.87  -1 79  GLU E OE2 1 
ATOM   5356 N N   . SER E 5 81  ? 18.454 -23.791 -24.584 1.00 29.50  ?  80  SER E N   1 
ATOM   5357 C CA  . SER E 5 81  ? 17.836 -25.080 -24.884 1.00 31.86  ?  80  SER E CA  1 
ATOM   5358 C C   . SER E 5 81  ? 17.040 -24.952 -26.182 1.00 31.58  ?  80  SER E C   1 
ATOM   5359 O O   . SER E 5 81  ? 15.806 -24.876 -26.176 1.00 33.23  ?  80  SER E O   1 
ATOM   5360 C CB  . SER E 5 81  ? 16.956 -25.550 -23.721 1.00 32.75  ?  80  SER E CB  1 
ATOM   5361 O OG  . SER E 5 81  ? 16.461 -26.857 -23.958 1.00 35.94  ?  80  SER E OG  1 
ATOM   5362 N N   . PRO E 5 82  ? 17.727 -24.986 -27.324 1.00 28.56  ?  81  PRO E N   1 
ATOM   5363 C CA  . PRO E 5 82  ? 17.060 -24.716 -28.610 1.00 33.66  ?  81  PRO E CA  1 
ATOM   5364 C C   . PRO E 5 82  ? 15.863 -25.621 -28.854 1.00 30.60  ?  81  PRO E C   1 
ATOM   5365 O O   . PRO E 5 82  ? 15.889 -26.817 -28.569 1.00 34.65  ?  81  PRO E O   1 
ATOM   5366 C CB  . PRO E 5 82  ? 18.167 -24.982 -29.646 1.00 29.45  ?  81  PRO E CB  1 
ATOM   5367 C CG  . PRO E 5 82  ? 19.520 -24.914 -28.804 1.00 25.87  ?  81  PRO E CG  1 
ATOM   5368 C CD  . PRO E 5 82  ? 19.106 -25.472 -27.487 1.00 25.27  ?  81  PRO E CD  1 
ATOM   5369 N N   . SER E 5 83  ? 14.832 -25.058 -29.458 1.00 30.17  ?  82  SER E N   1 
ATOM   5370 C CA  . SER E 5 83  ? 13.671 -25.849 -29.821 1.00 34.05  ?  82  SER E CA  1 
ATOM   5371 C C   . SER E 5 83  ? 13.337 -25.640 -31.287 1.00 29.70  ?  82  SER E C   1 
ATOM   5372 O O   . SER E 5 83  ? 13.783 -24.662 -31.899 1.00 29.94  ?  82  SER E O   1 
ATOM   5373 C CB  . SER E 5 83  ? 12.461 -25.478 -28.958 1.00 34.23  ?  82  SER E CB  1 
ATOM   5374 O OG  . SER E 5 83  ? 12.356 -24.073 -28.889 1.00 48.31  ?  82  SER E OG  1 
ATOM   5375 N N   . PRO E 5 84  ? 12.531 -26.539 -31.879 1.00 30.50  ?  83  PRO E N   1 
ATOM   5376 C CA  . PRO E 5 84  ? 12.257 -26.445 -33.326 1.00 30.89  ?  83  PRO E CA  1 
ATOM   5377 C C   . PRO E 5 84  ? 11.723 -25.093 -33.777 1.00 30.61  ?  83  PRO E C   1 
ATOM   5378 O O   . PRO E 5 84  ? 12.072 -24.644 -34.882 1.00 28.73  ?  83  PRO E O   1 
ATOM   5379 C CB  . PRO E 5 84  ? 11.234 -27.570 -33.563 1.00 32.40  ?  83  PRO E CB  1 
ATOM   5380 C CG  . PRO E 5 84  ? 11.591 -28.630 -32.514 1.00 35.76  ?  83  PRO E CG  1 
ATOM   5381 C CD  . PRO E 5 84  ? 12.013 -27.796 -31.288 1.00 36.85  ?  83  PRO E CD  1 
ATOM   5382 N N   . ASN E 5 85  ? 10.903 -24.423 -32.969 1.00 29.61  ?  84  ASN E N   1 
ATOM   5383 C CA  . ASN E 5 85  ? 10.359 -23.143 -33.403 1.00 29.88  ?  84  ASN E CA  1 
ATOM   5384 C C   . ASN E 5 85  ? 11.370 -21.997 -33.279 1.00 31.56  ?  84  ASN E C   1 
ATOM   5385 O O   . ASN E 5 85  ? 11.033 -20.851 -33.613 1.00 32.07  ?  84  ASN E O   1 
ATOM   5386 C CB  . ASN E 5 85  ? 9.035  -22.845 -32.668 1.00 29.70  ?  84  ASN E CB  1 
ATOM   5387 C CG  . ASN E 5 85  ? 9.202  -22.536 -31.183 1.00 33.49  ?  84  ASN E CG  1 
ATOM   5388 O OD1 . ASN E 5 85  ? 10.309 -22.430 -30.646 1.00 32.48  ?  84  ASN E OD1 1 
ATOM   5389 N ND2 . ASN E 5 85  ? 8.074  -22.389 -30.511 1.00 37.20  ?  84  ASN E ND2 1 
ATOM   5390 N N   . GLN E 5 86  ? 12.613 -22.282 -32.871 1.00 29.35  ?  85  GLN E N   1 
ATOM   5391 C CA  . GLN E 5 86  ? 13.703 -21.325 -33.043 1.00 28.45  ?  85  GLN E CA  1 
ATOM   5392 C C   . GLN E 5 86  ? 14.443 -21.489 -34.376 1.00 30.79  ?  85  GLN E C   1 
ATOM   5393 O O   . GLN E 5 86  ? 15.387 -20.731 -34.647 1.00 28.62  ?  85  GLN E O   1 
ATOM   5394 C CB  . GLN E 5 86  ? 14.671 -21.420 -31.863 1.00 27.12  ?  85  GLN E CB  1 
ATOM   5395 C CG  . GLN E 5 86  ? 14.018 -20.935 -30.567 1.00 22.29  ?  85  GLN E CG  1 
ATOM   5396 C CD  . GLN E 5 86  ? 14.898 -21.080 -29.348 1.00 30.84  ?  85  GLN E CD  1 
ATOM   5397 O OE1 . GLN E 5 86  ? 15.260 -22.190 -28.952 1.00 33.11  ?  85  GLN E OE1 1 
ATOM   5398 N NE2 . GLN E 5 86  ? 15.217 -19.949 -28.710 1.00 29.14  ?  85  GLN E NE2 1 
ATOM   5399 N N   . THR E 5 87  ? 14.017 -22.422 -35.233 1.00 27.43  ?  86  THR E N   1 
ATOM   5400 C CA  . THR E 5 87  ? 14.484 -22.444 -36.620 1.00 26.27  ?  86  THR E CA  1 
ATOM   5401 C C   . THR E 5 87  ? 14.153 -21.117 -37.297 1.00 27.93  ?  86  THR E C   1 
ATOM   5402 O O   . THR E 5 87  ? 12.990 -20.716 -37.354 1.00 28.47  ?  86  THR E O   1 
ATOM   5403 C CB  . THR E 5 87  ? 13.832 -23.612 -37.379 1.00 27.21  ?  86  THR E CB  1 
ATOM   5404 O OG1 . THR E 5 87  ? 14.216 -24.854 -36.769 1.00 29.65  ?  86  THR E OG1 1 
ATOM   5405 C CG2 . THR E 5 87  ? 14.285 -23.652 -38.838 1.00 24.10  ?  86  THR E CG2 1 
ATOM   5406 N N   . SER E 5 88  ? 15.166 -20.422 -37.808 1.00 25.69  ?  87  SER E N   1 
ATOM   5407 C CA  . SER E 5 88  ? 14.912 -19.087 -38.341 1.00 26.29  ?  87  SER E CA  1 
ATOM   5408 C C   . SER E 5 88  ? 16.197 -18.613 -39.002 1.00 24.93  ?  87  SER E C   1 
ATOM   5409 O O   . SER E 5 88  ? 17.229 -19.281 -38.923 1.00 27.20  ?  87  SER E O   1 
ATOM   5410 C CB  . SER E 5 88  ? 14.449 -18.091 -37.243 1.00 24.46  ?  87  SER E CB  1 
ATOM   5411 O OG  . SER E 5 88  ? 13.921 -16.892 -37.844 1.00 27.19  ?  87  SER E OG  1 
ATOM   5412 N N   . LEU E 5 89  ? 16.116 -17.460 -39.669 1.00 22.05  ?  88  LEU E N   1 
ATOM   5413 C CA  . LEU E 5 89  ? 17.287 -16.738 -40.164 1.00 22.75  ?  88  LEU E CA  1 
ATOM   5414 C C   . LEU E 5 89  ? 17.606 -15.587 -39.210 1.00 25.21  ?  88  LEU E C   1 
ATOM   5415 O O   . LEU E 5 89  ? 16.782 -14.684 -39.049 1.00 27.49  ?  88  LEU E O   1 
ATOM   5416 C CB  . LEU E 5 89  ? 17.021 -16.181 -41.563 1.00 22.70  ?  88  LEU E CB  1 
ATOM   5417 C CG  . LEU E 5 89  ? 18.164 -15.453 -42.263 1.00 27.05  ?  88  LEU E CG  1 
ATOM   5418 C CD1 . LEU E 5 89  ? 19.387 -16.356 -42.299 1.00 27.57  ?  88  LEU E CD1 1 
ATOM   5419 C CD2 . LEU E 5 89  ? 17.764 -15.017 -43.694 1.00 29.49  ?  88  LEU E CD2 1 
ATOM   5420 N N   . TYR E 5 90  ? 18.799 -15.591 -38.603 1.00 25.55  ?  89  TYR E N   1 
ATOM   5421 C CA  . TYR E 5 90  ? 19.145 -14.626 -37.554 1.00 25.27  ?  89  TYR E CA  1 
ATOM   5422 C C   . TYR E 5 90  ? 20.098 -13.568 -38.097 1.00 26.43  ?  89  TYR E C   1 
ATOM   5423 O O   . TYR E 5 90  ? 21.107 -13.905 -38.728 1.00 24.19  ?  89  TYR E O   1 
ATOM   5424 C CB  . TYR E 5 90  ? 19.773 -15.321 -36.346 1.00 22.83  ?  89  TYR E CB  1 
ATOM   5425 C CG  . TYR E 5 90  ? 18.800 -16.163 -35.576 1.00 26.18  ?  89  TYR E CG  1 
ATOM   5426 C CD1 . TYR E 5 90  ? 18.478 -17.440 -36.004 1.00 25.87  ?  89  TYR E CD1 1 
ATOM   5427 C CD2 . TYR E 5 90  ? 18.209 -15.688 -34.419 1.00 21.31  ?  89  TYR E CD2 1 
ATOM   5428 C CE1 . TYR E 5 90  ? 17.602 -18.215 -35.319 1.00 22.15  ?  89  TYR E CE1 1 
ATOM   5429 C CE2 . TYR E 5 90  ? 17.292 -16.467 -33.701 1.00 23.62  ?  89  TYR E CE2 1 
ATOM   5430 C CZ  . TYR E 5 90  ? 16.989 -17.726 -34.156 1.00 24.50  ?  89  TYR E CZ  1 
ATOM   5431 O OH  . TYR E 5 90  ? 16.084 -18.503 -33.446 1.00 24.57  ?  89  TYR E OH  1 
ATOM   5432 N N   . PHE E 5 91  ? 19.781 -12.291 -37.843 1.00 22.93  ?  90  PHE E N   1 
ATOM   5433 C CA  . PHE E 5 91  ? 20.613 -11.169 -38.254 1.00 23.77  ?  90  PHE E CA  1 
ATOM   5434 C C   . PHE E 5 91  ? 21.100 -10.409 -37.030 1.00 23.62  ?  90  PHE E C   1 
ATOM   5435 O O   . PHE E 5 91  ? 20.313 -10.091 -36.126 1.00 23.94  ?  90  PHE E O   1 
ATOM   5436 C CB  . PHE E 5 91  ? 19.852 -10.173 -39.169 1.00 23.85  ?  90  PHE E CB  1 
ATOM   5437 C CG  . PHE E 5 91  ? 19.554 -10.699 -40.541 1.00 25.82  ?  90  PHE E CG  1 
ATOM   5438 C CD1 . PHE E 5 91  ? 20.510 -10.608 -41.566 1.00 24.38  ?  90  PHE E CD1 1 
ATOM   5439 C CD2 . PHE E 5 91  ? 18.317 -11.272 -40.821 1.00 24.54  ?  90  PHE E CD2 1 
ATOM   5440 C CE1 . PHE E 5 91  ? 20.234 -11.091 -42.864 1.00 26.39  ?  90  PHE E CE1 1 
ATOM   5441 C CE2 . PHE E 5 91  ? 18.030 -11.773 -42.126 1.00 23.73  ?  90  PHE E CE2 1 
ATOM   5442 C CZ  . PHE E 5 91  ? 18.984 -11.667 -43.142 1.00 21.33  ?  90  PHE E CZ  1 
ATOM   5443 N N   . CYS E 5 92  ? 22.390 -10.074 -37.042 1.00 27.02  ?  91  CYS E N   1 
ATOM   5444 C CA  . CYS E 5 92  ? 22.991 -9.128  -36.105 1.00 25.25  ?  91  CYS E CA  1 
ATOM   5445 C C   . CYS E 5 92  ? 23.277 -7.826  -36.845 1.00 25.76  ?  91  CYS E C   1 
ATOM   5446 O O   . CYS E 5 92  ? 23.838 -7.836  -37.951 1.00 26.42  ?  91  CYS E O   1 
ATOM   5447 C CB  . CYS E 5 92  ? 24.284 -9.705  -35.492 1.00 22.82  ?  91  CYS E CB  1 
ATOM   5448 S SG  . CYS E 5 92  ? 25.144 -8.619  -34.343 1.00 28.04  ?  91  CYS E SG  1 
ATOM   5449 N N   . ALA E 5 93  ? 22.876 -6.714  -36.251 1.00 25.98  ?  92  ALA E N   1 
ATOM   5450 C CA  . ALA E 5 93  ? 23.071 -5.390  -36.835 1.00 26.89  ?  92  ALA E CA  1 
ATOM   5451 C C   . ALA E 5 93  ? 23.869 -4.518  -35.876 1.00 23.52  ?  92  ALA E C   1 
ATOM   5452 O O   . ALA E 5 93  ? 23.824 -4.717  -34.656 1.00 27.52  ?  92  ALA E O   1 
ATOM   5453 C CB  . ALA E 5 93  ? 21.720 -4.698  -37.137 1.00 22.64  ?  92  ALA E CB  1 
ATOM   5454 N N   . SER E 5 94  ? 24.596 -3.538  -36.420 1.00 26.50  ?  93  SER E N   1 
ATOM   5455 C CA  . SER E 5 94  ? 25.263 -2.568  -35.559 1.00 27.51  ?  93  SER E CA  1 
ATOM   5456 C C   . SER E 5 94  ? 25.276 -1.198  -36.212 1.00 29.23  ?  93  SER E C   1 
ATOM   5457 O O   . SER E 5 94  ? 25.216 -1.064  -37.437 1.00 23.86  ?  93  SER E O   1 
ATOM   5458 C CB  . SER E 5 94  ? 26.693 -3.014  -35.197 1.00 24.23  ?  93  SER E CB  1 
ATOM   5459 O OG  . SER E 5 94  ? 27.657 -2.576  -36.139 1.00 28.38  ?  93  SER E OG  1 
ATOM   5460 N N   . SER E 5 95  ? 25.360 -0.175  -35.356 1.00 26.65  ?  94  SER E N   1 
ATOM   5461 C CA  . SER E 5 95  ? 25.546 1.209   -35.771 1.00 24.97  ?  94  SER E CA  1 
ATOM   5462 C C   . SER E 5 95  ? 26.346 1.945   -34.685 1.00 28.31  ?  94  SER E C   1 
ATOM   5463 O O   . SER E 5 95  ? 26.264 1.605   -33.500 1.00 23.99  ?  94  SER E O   1 
ATOM   5464 C CB  . SER E 5 95  ? 24.195 1.922   -35.982 1.00 20.65  ?  94  SER E CB  1 
ATOM   5465 O OG  . SER E 5 95  ? 23.406 1.834   -34.801 1.00 27.61  ?  94  SER E OG  1 
ATOM   5466 N N   . LEU E 5 96  ? 27.073 2.994   -35.106 1.00 27.00  ?  95  LEU E N   1 
ATOM   5467 C CA  . LEU E 5 96  ? 27.932 3.752   -34.197 1.00 27.56  ?  95  LEU E CA  1 
ATOM   5468 C C   . LEU E 5 96  ? 27.184 4.197   -32.943 1.00 28.16  ?  95  LEU E C   1 
ATOM   5469 O O   . LEU E 5 96  ? 27.712 4.116   -31.825 1.00 24.32  ?  95  LEU E O   1 
ATOM   5470 C CB  . LEU E 5 96  ? 28.524 4.959   -34.936 1.00 26.27  ?  95  LEU E CB  1 
ATOM   5471 C CG  . LEU E 5 96  ? 29.656 5.796   -34.313 1.00 30.09  ?  95  LEU E CG  1 
ATOM   5472 C CD1 . LEU E 5 96  ? 30.888 4.955   -34.005 1.00 32.58  ?  95  LEU E CD1 1 
ATOM   5473 C CD2 . LEU E 5 96  ? 30.041 6.945   -35.279 1.00 30.12  ?  95  LEU E CD2 1 
ATOM   5474 N N   . VAL E 5 97  ? 25.944 4.641   -33.100 1.00 28.46  ?  96  VAL E N   1 
ATOM   5475 C CA  . VAL E 5 97  ? 25.135 5.101   -31.986 1.00 24.62  ?  96  VAL E CA  1 
ATOM   5476 C C   . VAL E 5 97  ? 23.741 4.541   -32.196 1.00 33.68  ?  96  VAL E C   1 
ATOM   5477 O O   . VAL E 5 97  ? 23.355 4.190   -33.312 1.00 29.25  ?  96  VAL E O   1 
ATOM   5478 C CB  . VAL E 5 97  ? 25.147 6.642   -31.916 1.00 30.99  ?  96  VAL E CB  1 
ATOM   5479 C CG1 . VAL E 5 97  ? 24.386 7.271   -33.149 1.00 27.20  ?  96  VAL E CG1 1 
ATOM   5480 C CG2 . VAL E 5 97  ? 24.600 7.134   -30.593 1.00 30.11  ?  96  VAL E CG2 1 
ATOM   5481 N N   . SER E 5 98  ? 22.977 4.456   -31.111 1.00 27.69  ?  97  SER E N   1 
ATOM   5482 C CA  . SER E 5 98  ? 21.675 3.812   -31.176 1.00 26.03  ?  97  SER E CA  1 
ATOM   5483 C C   . SER E 5 98  ? 20.653 4.508   -32.085 1.00 32.76  ?  97  SER E C   1 
ATOM   5484 O O   . SER E 5 98  ? 19.669 3.865   -32.460 1.00 30.27  ?  97  SER E O   1 
ATOM   5485 C CB  . SER E 5 98  ? 21.085 3.691   -29.768 1.00 32.52  ?  97  SER E CB  1 
ATOM   5486 O OG  . SER E 5 98  ? 21.975 2.983   -28.902 1.00 35.61  ?  97  SER E OG  1 
ATOM   5487 N N   . THR E 5 99  ? 20.787 5.807   -32.372 1.00 29.39  ?  98  THR E N   1 
ATOM   5488 C CA  . THR E 5 99  ? 19.891 6.524   -33.296 1.00 32.50  ?  98  THR E CA  1 
ATOM   5489 C C   . THR E 5 99  ? 20.799 7.239   -34.290 1.00 31.96  ?  98  THR E C   1 
ATOM   5490 O O   . THR E 5 99  ? 21.217 8.388   -34.066 1.00 30.40  ?  98  THR E O   1 
ATOM   5491 C CB  . THR E 5 99  ? 18.966 7.537   -32.606 1.00 35.85  ?  98  THR E CB  1 
ATOM   5492 O OG1 . THR E 5 99  ? 19.734 8.404   -31.765 1.00 31.64  ?  98  THR E OG1 1 
ATOM   5493 C CG2 . THR E 5 99  ? 17.852 6.866   -31.796 1.00 33.52  ?  98  THR E CG2 1 
ATOM   5494 N N   . PRO E 5 100 ? 21.168 6.569   -35.373 1.00 27.48  ?  99  PRO E N   1 
ATOM   5495 C CA  . PRO E 5 100 ? 22.172 7.128   -36.277 1.00 30.27  ?  99  PRO E CA  1 
ATOM   5496 C C   . PRO E 5 100 ? 21.739 8.462   -36.871 1.00 31.92  ?  99  PRO E C   1 
ATOM   5497 O O   . PRO E 5 100 ? 20.548 8.735   -37.060 1.00 32.01  ?  99  PRO E O   1 
ATOM   5498 C CB  . PRO E 5 100 ? 22.299 6.046   -37.364 1.00 33.67  ?  99  PRO E CB  1 
ATOM   5499 C CG  . PRO E 5 100 ? 22.000 4.769   -36.631 1.00 33.90  ?  99  PRO E CG  1 
ATOM   5500 C CD  . PRO E 5 100 ? 20.960 5.126   -35.590 1.00 32.19  ?  99  PRO E CD  1 
ATOM   5501 N N   . LEU E 5 101 ? 22.742 9.291   -37.164 1.00 28.38  ?  100 LEU E N   1 
ATOM   5502 C CA  . LEU E 5 101 ? 22.569 10.493  -37.966 1.00 30.93  ?  100 LEU E CA  1 
ATOM   5503 C C   . LEU E 5 101 ? 22.130 10.131  -39.391 1.00 37.64  ?  100 LEU E C   1 
ATOM   5504 O O   . LEU E 5 101 ? 22.331 8.999   -39.837 1.00 33.20  ?  100 LEU E O   1 
ATOM   5505 C CB  . LEU E 5 101 ? 23.890 11.250  -38.026 1.00 31.25  ?  100 LEU E CB  1 
ATOM   5506 C CG  . LEU E 5 101 ? 24.456 11.672  -36.662 1.00 35.82  ?  100 LEU E CG  1 
ATOM   5507 C CD1 . LEU E 5 101 ? 25.880 12.118  -36.802 1.00 32.13  ?  100 LEU E CD1 1 
ATOM   5508 C CD2 . LEU E 5 101 ? 23.596 12.789  -36.062 1.00 34.71  ?  100 LEU E CD2 1 
ATOM   5509 N N   . PRO E 5 102 ? 21.576 11.102  -40.140 1.00 34.87  ?  101 PRO E N   1 
ATOM   5510 C CA  . PRO E 5 102 ? 21.170 10.813  -41.535 1.00 37.63  ?  101 PRO E CA  1 
ATOM   5511 C C   . PRO E 5 102 ? 22.265 10.164  -42.368 1.00 30.80  ?  101 PRO E C   1 
ATOM   5512 O O   . PRO E 5 102 ? 21.987 9.205   -43.093 1.00 37.02  ?  101 PRO E O   1 
ATOM   5513 C CB  . PRO E 5 102 ? 20.780 12.207  -42.083 1.00 37.88  ?  101 PRO E CB  1 
ATOM   5514 C CG  . PRO E 5 102 ? 20.372 13.008  -40.861 1.00 39.96  ?  101 PRO E CG  1 
ATOM   5515 C CD  . PRO E 5 102 ? 21.304 12.502  -39.755 1.00 40.08  ?  101 PRO E CD  1 
ATOM   5516 N N   . LYS E 5 103 ? 23.489 10.603  -42.237 1.00 36.57  ?  102 LYS E N   1 
ATOM   5517 C CA  . LYS E 5 103 ? 24.542 10.046  -43.099 1.00 35.02  ?  102 LYS E CA  1 
ATOM   5518 C C   . LYS E 5 103 ? 25.185 8.772   -42.547 1.00 41.07  ?  102 LYS E C   1 
ATOM   5519 O O   . LYS E 5 103 ? 26.060 8.289   -43.179 1.00 40.43  ?  102 LYS E O   1 
ATOM   5520 C CB  . LYS E 5 103 ? 25.590 11.134  -43.272 1.00 40.62  ?  102 LYS E CB  1 
ATOM   5521 C CG  . LYS E 5 103 ? 26.801 11.022  -42.375 1.00 46.93  ?  102 LYS E CG  1 
ATOM   5522 C CD  . LYS E 5 103 ? 26.610 11.505  -40.985 1.00 48.32  ?  102 LYS E CD  1 
ATOM   5523 C CE  . LYS E 5 103 ? 27.554 12.619  -40.619 1.00 55.17  ?  102 LYS E CE  1 
ATOM   5524 N NZ  . LYS E 5 103 ? 26.817 13.895  -40.587 1.00 55.28  ?  102 LYS E NZ  1 
ATOM   5525 N N   . GLU E 5 104 ? 24.754 8.277   -41.398 1.00 39.36  ?  103 GLU E N   1 
ATOM   5526 C CA  . GLU E 5 104 ? 25.345 7.085   -40.797 1.00 36.07  ?  103 GLU E CA  1 
ATOM   5527 C C   . GLU E 5 104 ? 24.567 5.838   -41.198 1.00 32.69  ?  103 GLU E C   1 
ATOM   5528 O O   . GLU E 5 104 ? 23.354 5.894   -41.413 1.00 32.65  ?  103 GLU E O   1 
ATOM   5529 C CB  . GLU E 5 104 ? 25.370 7.229   -39.271 1.00 35.40  ?  103 GLU E CB  1 
ATOM   5530 C CG  . GLU E 5 104 ? 26.502 8.148   -38.769 1.00 31.77  ?  103 GLU E CG  1 
ATOM   5531 C CD  . GLU E 5 104 ? 26.435 8.455   -37.277 1.00 30.14  ?  103 GLU E CD  1 
ATOM   5532 O OE1 . GLU E 5 104 ? 27.432 8.990   -36.762 1.00 28.57  ?  103 GLU E OE1 1 
ATOM   5533 O OE2 . GLU E 5 104 ? 25.397 8.207   -36.620 1.00 29.49  -1 103 GLU E OE2 1 
ATOM   5534 N N   . THR E 5 105 ? 25.277 4.707   -41.264 1.00 31.96  ?  104 THR E N   1 
ATOM   5535 C CA  . THR E 5 105 ? 24.763 3.438   -41.783 1.00 33.86  ?  104 THR E CA  1 
ATOM   5536 C C   . THR E 5 105 ? 24.412 2.457   -40.659 1.00 28.83  ?  104 THR E C   1 
ATOM   5537 O O   . THR E 5 105 ? 25.098 2.400   -39.639 1.00 30.48  ?  104 THR E O   1 
ATOM   5538 C CB  . THR E 5 105 ? 25.818 2.801   -42.701 1.00 31.74  ?  104 THR E CB  1 
ATOM   5539 O OG1 . THR E 5 105 ? 26.009 3.622   -43.852 1.00 31.84  ?  104 THR E OG1 1 
ATOM   5540 C CG2 . THR E 5 105 ? 25.439 1.375   -43.119 1.00 31.61  ?  104 THR E CG2 1 
ATOM   5541 N N   . GLN E 5 106 ? 23.345 1.673   -40.851 1.00 32.91  ?  105 GLN E N   1 
ATOM   5542 C CA  . GLN E 5 106 ? 23.104 0.486   -40.032 1.00 29.67  ?  105 GLN E CA  1 
ATOM   5543 C C   . GLN E 5 106 ? 23.714 -0.711  -40.748 1.00 30.45  ?  105 GLN E C   1 
ATOM   5544 O O   . GLN E 5 106 ? 23.301 -1.027  -41.868 1.00 29.06  ?  105 GLN E O   1 
ATOM   5545 C CB  . GLN E 5 106 ? 21.618 0.226   -39.833 1.00 32.44  ?  105 GLN E CB  1 
ATOM   5546 C CG  . GLN E 5 106 ? 20.926 1.079   -38.846 1.00 38.42  ?  105 GLN E CG  1 
ATOM   5547 C CD  . GLN E 5 106 ? 19.424 0.837   -38.886 1.00 38.62  ?  105 GLN E CD  1 
ATOM   5548 O OE1 . GLN E 5 106 ? 18.977 -0.293  -39.074 1.00 32.57  ?  105 GLN E OE1 1 
ATOM   5549 N NE2 . GLN E 5 106 ? 18.640 1.902   -38.699 1.00 39.34  ?  105 GLN E NE2 1 
ATOM   5550 N N   . TYR E 5 107 ? 24.688 -1.376  -40.117 1.00 26.55  ?  106 TYR E N   1 
ATOM   5551 C CA  . TYR E 5 107 ? 25.375 -2.497  -40.757 1.00 28.02  ?  106 TYR E CA  1 
ATOM   5552 C C   . TYR E 5 107 ? 24.729 -3.803  -40.347 1.00 29.74  ?  106 TYR E C   1 
ATOM   5553 O O   . TYR E 5 107 ? 24.361 -3.983  -39.186 1.00 29.32  ?  106 TYR E O   1 
ATOM   5554 C CB  . TYR E 5 107 ? 26.862 -2.529  -40.395 1.00 27.13  ?  106 TYR E CB  1 
ATOM   5555 C CG  . TYR E 5 107 ? 27.595 -1.297  -40.872 1.00 30.31  ?  106 TYR E CG  1 
ATOM   5556 C CD1 . TYR E 5 107 ? 27.553 -0.116  -40.128 1.00 30.70  ?  106 TYR E CD1 1 
ATOM   5557 C CD2 . TYR E 5 107 ? 28.301 -1.302  -42.078 1.00 31.64  ?  106 TYR E CD2 1 
ATOM   5558 C CE1 . TYR E 5 107 ? 28.200 1.032   -40.563 1.00 32.66  ?  106 TYR E CE1 1 
ATOM   5559 C CE2 . TYR E 5 107 ? 28.960 -0.165  -42.525 1.00 34.07  ?  106 TYR E CE2 1 
ATOM   5560 C CZ  . TYR E 5 107 ? 28.907 1.000   -41.758 1.00 38.17  ?  106 TYR E CZ  1 
ATOM   5561 O OH  . TYR E 5 107 ? 29.540 2.146   -42.178 1.00 43.35  ?  106 TYR E OH  1 
ATOM   5562 N N   . PHE E 5 108 ? 24.645 -4.739  -41.288 1.00 26.34  ?  107 PHE E N   1 
ATOM   5563 C CA  . PHE E 5 108 ? 24.089 -6.056  -41.005 1.00 28.15  ?  107 PHE E CA  1 
ATOM   5564 C C   . PHE E 5 108 ? 25.118 -7.153  -41.236 1.00 24.33  ?  107 PHE E C   1 
ATOM   5565 O O   . PHE E 5 108 ? 25.906 -7.096  -42.184 1.00 25.77  ?  107 PHE E O   1 
ATOM   5566 C CB  . PHE E 5 108 ? 22.842 -6.332  -41.865 1.00 28.86  ?  107 PHE E CB  1 
ATOM   5567 C CG  . PHE E 5 108 ? 21.607 -5.669  -41.343 1.00 25.27  ?  107 PHE E CG  1 
ATOM   5568 C CD1 . PHE E 5 108 ? 21.349 -4.348  -41.642 1.00 30.29  ?  107 PHE E CD1 1 
ATOM   5569 C CD2 . PHE E 5 108 ? 20.723 -6.354  -40.544 1.00 25.92  ?  107 PHE E CD2 1 
ATOM   5570 C CE1 . PHE E 5 108 ? 20.227 -3.737  -41.168 1.00 32.60  ?  107 PHE E CE1 1 
ATOM   5571 C CE2 . PHE E 5 108 ? 19.608 -5.750  -40.049 1.00 32.11  ?  107 PHE E CE2 1 
ATOM   5572 C CZ  . PHE E 5 108 ? 19.356 -4.434  -40.360 1.00 30.82  ?  107 PHE E CZ  1 
ATOM   5573 N N   . GLY E 5 109 ? 25.108 -8.159  -40.365 1.00 24.94  ?  108 GLY E N   1 
ATOM   5574 C CA  . GLY E 5 109 ? 25.853 -9.362  -40.632 1.00 25.15  ?  108 GLY E CA  1 
ATOM   5575 C C   . GLY E 5 109 ? 25.150 -10.181 -41.712 1.00 28.87  ?  108 GLY E C   1 
ATOM   5576 O O   . GLY E 5 109 ? 24.023 -9.861  -42.131 1.00 25.32  ?  108 GLY E O   1 
ATOM   5577 N N   . PRO E 5 110 ? 25.800 -11.254 -42.191 1.00 26.56  ?  109 PRO E N   1 
ATOM   5578 C CA  . PRO E 5 110 ? 25.273 -11.969 -43.376 1.00 24.79  ?  109 PRO E CA  1 
ATOM   5579 C C   . PRO E 5 110 ? 24.074 -12.835 -43.075 1.00 24.61  ?  109 PRO E C   1 
ATOM   5580 O O   . PRO E 5 110 ? 23.472 -13.359 -44.009 1.00 30.74  ?  109 PRO E O   1 
ATOM   5581 C CB  . PRO E 5 110 ? 26.458 -12.823 -43.826 1.00 25.16  ?  109 PRO E CB  1 
ATOM   5582 C CG  . PRO E 5 110 ? 27.227 -13.089 -42.552 1.00 29.28  ?  109 PRO E CG  1 
ATOM   5583 C CD  . PRO E 5 110 ? 27.125 -11.754 -41.795 1.00 28.28  ?  109 PRO E CD  1 
ATOM   5584 N N   . GLY E 5 111 ? 23.724 -13.018 -41.814 1.00 24.03  ?  110 GLY E N   1 
ATOM   5585 C CA  . GLY E 5 111 ? 22.656 -13.913 -41.427 1.00 26.77  ?  110 GLY E CA  1 
ATOM   5586 C C   . GLY E 5 111 ? 23.195 -15.267 -40.994 1.00 25.64  ?  110 GLY E C   1 
ATOM   5587 O O   . GLY E 5 111 ? 24.232 -15.731 -41.449 1.00 23.61  ?  110 GLY E O   1 
ATOM   5588 N N   . THR E 5 112 ? 22.494 -15.887 -40.042 1.00 22.56  ?  111 THR E N   1 
ATOM   5589 C CA  . THR E 5 112 ? 22.764 -17.245 -39.568 1.00 23.97  ?  111 THR E CA  1 
ATOM   5590 C C   . THR E 5 112 ? 21.501 -18.060 -39.828 1.00 23.67  ?  111 THR E C   1 
ATOM   5591 O O   . THR E 5 112 ? 20.443 -17.743 -39.276 1.00 25.41  ?  111 THR E O   1 
ATOM   5592 C CB  . THR E 5 112 ? 23.107 -17.259 -38.058 1.00 25.84  ?  111 THR E CB  1 
ATOM   5593 O OG1 . THR E 5 112 ? 24.332 -16.547 -37.809 1.00 23.85  ?  111 THR E OG1 1 
ATOM   5594 C CG2 . THR E 5 112 ? 23.246 -18.692 -37.496 1.00 23.28  ?  111 THR E CG2 1 
ATOM   5595 N N   . ARG E 5 113 ? 21.600 -19.092 -40.678 1.00 22.34  ?  112 ARG E N   1 
ATOM   5596 C CA  . ARG E 5 113 ? 20.498 -20.029 -40.888 1.00 23.30  ?  112 ARG E CA  1 
ATOM   5597 C C   . ARG E 5 113 ? 20.598 -21.098 -39.808 1.00 23.54  ?  112 ARG E C   1 
ATOM   5598 O O   . ARG E 5 113 ? 21.486 -21.943 -39.853 1.00 27.57  ?  112 ARG E O   1 
ATOM   5599 C CB  . ARG E 5 113 ? 20.548 -20.687 -42.271 1.00 30.85  ?  112 ARG E CB  1 
ATOM   5600 C CG  . ARG E 5 113 ? 20.319 -19.793 -43.450 1.00 34.03  ?  112 ARG E CG  1 
ATOM   5601 C CD  . ARG E 5 113 ? 18.851 -19.449 -43.562 1.00 42.73  ?  112 ARG E CD  1 
ATOM   5602 N NE  . ARG E 5 113 ? 17.967 -20.601 -43.805 1.00 48.88  ?  112 ARG E NE  1 
ATOM   5603 C CZ  . ARG E 5 113 ? 17.728 -21.149 -45.002 1.00 45.00  ?  112 ARG E CZ  1 
ATOM   5604 N NH1 . ARG E 5 113 ? 16.883 -22.171 -45.101 1.00 44.51  ?  112 ARG E NH1 1 
ATOM   5605 N NH2 . ARG E 5 113 ? 18.337 -20.696 -46.095 1.00 43.43  ?  112 ARG E NH2 1 
ATOM   5606 N N   . LEU E 5 114 ? 19.689 -21.074 -38.847 1.00 25.45  ?  113 LEU E N   1 
ATOM   5607 C CA  . LEU E 5 114 ? 19.668 -22.054 -37.778 1.00 27.37  ?  113 LEU E CA  1 
ATOM   5608 C C   . LEU E 5 114 ? 18.504 -22.998 -38.032 1.00 25.80  ?  113 LEU E C   1 
ATOM   5609 O O   . LEU E 5 114 ? 17.387 -22.540 -38.280 1.00 23.54  ?  113 LEU E O   1 
ATOM   5610 C CB  . LEU E 5 114 ? 19.503 -21.375 -36.407 1.00 26.33  ?  113 LEU E CB  1 
ATOM   5611 C CG  . LEU E 5 114 ? 19.268 -22.357 -35.259 1.00 28.70  ?  113 LEU E CG  1 
ATOM   5612 C CD1 . LEU E 5 114 ? 20.519 -23.233 -35.143 1.00 28.98  ?  113 LEU E CD1 1 
ATOM   5613 C CD2 . LEU E 5 114 ? 18.958 -21.649 -33.914 1.00 25.99  ?  113 LEU E CD2 1 
ATOM   5614 N N   . LEU E 5 115 ? 18.765 -24.303 -37.957 1.00 24.43  ?  114 LEU E N   1 
ATOM   5615 C CA  . LEU E 5 115 ? 17.737 -25.332 -38.058 1.00 25.07  ?  114 LEU E CA  1 
ATOM   5616 C C   . LEU E 5 115 ? 17.867 -26.264 -36.858 1.00 29.50  ?  114 LEU E C   1 
ATOM   5617 O O   . LEU E 5 115 ? 18.907 -26.913 -36.679 1.00 25.58  ?  114 LEU E O   1 
ATOM   5618 C CB  . LEU E 5 115 ? 17.884 -26.123 -39.369 1.00 29.06  ?  114 LEU E CB  1 
ATOM   5619 C CG  . LEU E 5 115 ? 16.950 -27.315 -39.606 1.00 30.12  ?  114 LEU E CG  1 
ATOM   5620 C CD1 . LEU E 5 115 ? 15.452 -26.925 -39.579 1.00 21.77  ?  114 LEU E CD1 1 
ATOM   5621 C CD2 . LEU E 5 115 ? 17.304 -28.017 -40.938 1.00 26.97  ?  114 LEU E CD2 1 
ATOM   5622 N N   . VAL E 5 116 ? 16.821 -26.328 -36.041 1.00 27.55  ?  115 VAL E N   1 
ATOM   5623 C CA  . VAL E 5 116 ? 16.779 -27.171 -34.852 1.00 28.14  ?  115 VAL E CA  1 
ATOM   5624 C C   . VAL E 5 116 ? 15.907 -28.378 -35.176 1.00 27.49  ?  115 VAL E C   1 
ATOM   5625 O O   . VAL E 5 116 ? 14.735 -28.219 -35.529 1.00 29.17  ?  115 VAL E O   1 
ATOM   5626 C CB  . VAL E 5 116 ? 16.211 -26.401 -33.646 1.00 26.80  ?  115 VAL E CB  1 
ATOM   5627 C CG1 . VAL E 5 116 ? 16.297 -27.236 -32.367 1.00 26.52  ?  115 VAL E CG1 1 
ATOM   5628 C CG2 . VAL E 5 116 ? 16.918 -25.076 -33.473 1.00 26.28  ?  115 VAL E CG2 1 
ATOM   5629 N N   . LEU E 5 117 ? 16.451 -29.582 -35.013 1.00 27.54  ?  116 LEU E N   1 
ATOM   5630 C CA  . LEU E 5 117 ? 15.765 -30.807 -35.415 1.00 30.67  ?  116 LEU E CA  1 
ATOM   5631 C C   . LEU E 5 117 ? 15.812 -31.833 -34.292 1.00 33.12  ?  116 LEU E C   1 
ATOM   5632 O O   . LEU E 5 117 ? 16.709 -31.820 -33.449 1.00 31.44  ?  116 LEU E O   1 
ATOM   5633 C CB  . LEU E 5 117 ? 16.402 -31.429 -36.658 1.00 29.99  ?  116 LEU E CB  1 
ATOM   5634 C CG  . LEU E 5 117 ? 16.463 -30.615 -37.940 1.00 27.65  ?  116 LEU E CG  1 
ATOM   5635 C CD1 . LEU E 5 117 ? 17.275 -31.413 -38.994 1.00 23.97  ?  116 LEU E CD1 1 
ATOM   5636 C CD2 . LEU E 5 117 ? 15.052 -30.318 -38.419 1.00 34.55  ?  116 LEU E CD2 1 
ATOM   5637 N N   . GLU E 5 118 ? 14.878 -32.757 -34.351 1.00 37.44  ?  117 GLU E N   1 
ATOM   5638 C CA  . GLU E 5 118 ? 14.746 -33.871 -33.399 1.00 42.27  ?  117 GLU E CA  1 
ATOM   5639 C C   . GLU E 5 118 ? 15.994 -34.744 -33.530 1.00 41.48  ?  117 GLU E C   1 
ATOM   5640 O O   . GLU E 5 118 ? 16.506 -35.133 -32.511 1.00 44.76  ?  117 GLU E O   1 
ATOM   5641 C CB  . GLU E 5 118 ? 13.380 -34.520 -33.597 1.00 41.68  ?  117 GLU E CB  1 
ATOM   5642 C CG  . GLU E 5 118 ? 13.334 -35.994 -33.294 1.00 57.47  ?  117 GLU E CG  1 
ATOM   5643 C CD  . GLU E 5 118 ? 11.972 -36.684 -33.218 1.00 64.33  ?  117 GLU E CD  1 
ATOM   5644 O OE1 . GLU E 5 118 ? 11.189 -36.596 -34.168 1.00 57.43  ?  117 GLU E OE1 1 
ATOM   5645 O OE2 . GLU E 5 118 ? 11.722 -37.331 -32.210 1.00 67.90  ?  117 GLU E OE2 1 
ATOM   5646 N N   . ASP E 5 119 ? 16.451 -34.992 -34.756 1.00 35.55  ?  118 ASP E N   1 
ATOM   5647 C CA  . ASP E 5 119 ? 17.679 -35.718 -35.037 1.00 33.88  ?  118 ASP E CA  1 
ATOM   5648 C C   . ASP E 5 119 ? 18.109 -35.340 -36.450 1.00 36.75  ?  118 ASP E C   1 
ATOM   5649 O O   . ASP E 5 119 ? 17.361 -34.698 -37.198 1.00 33.58  ?  118 ASP E O   1 
ATOM   5650 C CB  . ASP E 5 119 ? 17.482 -37.227 -34.866 1.00 38.13  ?  118 ASP E CB  1 
ATOM   5651 C CG  . ASP E 5 119 ? 16.478 -37.799 -35.850 1.00 48.00  ?  118 ASP E CG  1 
ATOM   5652 O OD1 . ASP E 5 119 ? 16.615 -37.549 -37.062 1.00 46.15  ?  118 ASP E OD1 1 
ATOM   5653 O OD2 . ASP E 5 119 ? 15.543 -38.501 -35.417 1.00 57.53  -1 118 ASP E OD2 1 
ATOM   5654 N N   . LEU E 5 120 ? 19.332 -35.730 -36.799 1.00 28.98  ?  119 LEU E N   1 
ATOM   5655 C CA  . LEU E 5 120 ? 19.969 -35.311 -38.042 1.00 33.78  ?  119 LEU E CA  1 
ATOM   5656 C C   . LEU E 5 120 ? 19.831 -36.333 -39.150 1.00 34.50  ?  119 LEU E C   1 
ATOM   5657 O O   . LEU E 5 120 ? 20.557 -36.236 -40.140 1.00 32.73  ?  119 LEU E O   1 
ATOM   5658 C CB  . LEU E 5 120 ? 21.453 -35.037 -37.808 1.00 32.85  ?  119 LEU E CB  1 
ATOM   5659 C CG  . LEU E 5 120 ? 21.782 -34.121 -36.632 1.00 37.96  ?  119 LEU E CG  1 
ATOM   5660 C CD1 . LEU E 5 120 ? 23.277 -34.051 -36.409 1.00 35.24  ?  119 LEU E CD1 1 
ATOM   5661 C CD2 . LEU E 5 120 ? 21.229 -32.739 -36.882 1.00 33.44  ?  119 LEU E CD2 1 
ATOM   5662 N N   . LYS E 5 121 ? 18.926 -37.312 -38.996 1.00 31.79  ?  120 LYS E N   1 
ATOM   5663 C CA  . LYS E 5 121 ? 18.833 -38.440 -39.918 1.00 36.35  ?  120 LYS E CA  1 
ATOM   5664 C C   . LYS E 5 121 ? 18.372 -38.041 -41.310 1.00 35.48  ?  120 LYS E C   1 
ATOM   5665 O O   . LYS E 5 121 ? 18.635 -38.777 -42.260 1.00 35.87  ?  120 LYS E O   1 
ATOM   5666 C CB  . LYS E 5 121 ? 17.883 -39.507 -39.372 1.00 33.32  ?  120 LYS E CB  1 
ATOM   5667 C CG  . LYS E 5 121 ? 18.286 -40.026 -37.983 1.00 51.18  ?  120 LYS E CG  1 
ATOM   5668 C CD  . LYS E 5 121 ? 17.544 -41.312 -37.597 1.00 52.25  ?  120 LYS E CD  1 
ATOM   5669 C CE  . LYS E 5 121 ? 16.501 -41.071 -36.514 1.00 55.15  ?  120 LYS E CE  1 
ATOM   5670 N NZ  . LYS E 5 121 ? 15.805 -42.343 -36.155 1.00 57.54  ?  120 LYS E NZ  1 
ATOM   5671 N N   . ASN E 5 122 ? 17.695 -36.909 -41.470 1.00 36.55  ?  121 ASN E N   1 
ATOM   5672 C CA  . ASN E 5 122 ? 17.200 -36.527 -42.786 1.00 35.69  ?  121 ASN E CA  1 
ATOM   5673 C C   . ASN E 5 122 ? 18.162 -35.649 -43.581 1.00 35.87  ?  121 ASN E C   1 
ATOM   5674 O O   . ASN E 5 122 ? 17.831 -35.276 -44.717 1.00 31.98  ?  121 ASN E O   1 
ATOM   5675 C CB  . ASN E 5 122 ? 15.856 -35.818 -42.648 1.00 32.86  ?  121 ASN E CB  1 
ATOM   5676 C CG  . ASN E 5 122 ? 14.758 -36.753 -42.183 1.00 49.69  ?  121 ASN E CG  1 
ATOM   5677 O OD1 . ASN E 5 122 ? 14.681 -37.917 -42.606 1.00 47.63  ?  121 ASN E OD1 1 
ATOM   5678 N ND2 . ASN E 5 122 ? 13.897 -36.248 -41.305 1.00 51.49  ?  121 ASN E ND2 1 
ATOM   5679 N N   . VAL E 5 123 ? 19.330 -35.302 -43.032 1.00 31.30  ?  122 VAL E N   1 
ATOM   5680 C CA  . VAL E 5 123 ? 20.257 -34.418 -43.743 1.00 27.27  ?  122 VAL E CA  1 
ATOM   5681 C C   . VAL E 5 123 ? 20.882 -35.175 -44.908 1.00 28.51  ?  122 VAL E C   1 
ATOM   5682 O O   . VAL E 5 123 ? 21.447 -36.269 -44.733 1.00 27.96  ?  122 VAL E O   1 
ATOM   5683 C CB  . VAL E 5 123 ? 21.314 -33.851 -42.774 1.00 26.09  ?  122 VAL E CB  1 
ATOM   5684 C CG1 . VAL E 5 123 ? 22.265 -32.885 -43.507 1.00 25.94  ?  122 VAL E CG1 1 
ATOM   5685 C CG2 . VAL E 5 123 ? 20.616 -33.133 -41.611 1.00 24.34  ?  122 VAL E CG2 1 
ATOM   5686 N N   . PHE E 5 124 ? 20.767 -34.617 -46.124 1.00 30.11  ?  123 PHE E N   1 
ATOM   5687 C CA  . PHE E 5 124 ? 21.245 -35.230 -47.375 1.00 32.32  ?  123 PHE E CA  1 
ATOM   5688 C C   . PHE E 5 124 ? 21.938 -34.147 -48.197 1.00 26.94  ?  123 PHE E C   1 
ATOM   5689 O O   . PHE E 5 124 ? 21.355 -33.067 -48.389 1.00 25.23  ?  123 PHE E O   1 
ATOM   5690 C CB  . PHE E 5 124 ? 20.107 -35.830 -48.221 1.00 34.35  ?  123 PHE E CB  1 
ATOM   5691 C CG  . PHE E 5 124 ? 19.535 -37.096 -47.689 1.00 37.10  ?  123 PHE E CG  1 
ATOM   5692 C CD1 . PHE E 5 124 ? 20.143 -38.299 -47.953 1.00 40.21  ?  123 PHE E CD1 1 
ATOM   5693 C CD2 . PHE E 5 124 ? 18.351 -37.081 -46.947 1.00 44.58  ?  123 PHE E CD2 1 
ATOM   5694 C CE1 . PHE E 5 124 ? 19.603 -39.479 -47.470 1.00 45.86  ?  123 PHE E CE1 1 
ATOM   5695 C CE2 . PHE E 5 124 ? 17.797 -38.256 -46.457 1.00 44.42  ?  123 PHE E CE2 1 
ATOM   5696 C CZ  . PHE E 5 124 ? 18.421 -39.457 -46.722 1.00 47.10  ?  123 PHE E CZ  1 
ATOM   5697 N N   . PRO E 5 125 ? 23.137 -34.407 -48.725 1.00 23.96  ?  124 PRO E N   1 
ATOM   5698 C CA  . PRO E 5 125 ? 23.785 -33.454 -49.636 1.00 26.01  ?  124 PRO E CA  1 
ATOM   5699 C C   . PRO E 5 125 ? 23.157 -33.526 -51.017 1.00 31.88  ?  124 PRO E C   1 
ATOM   5700 O O   . PRO E 5 125 ? 22.451 -34.498 -51.326 1.00 23.92  ?  124 PRO E O   1 
ATOM   5701 C CB  . PRO E 5 125 ? 25.241 -33.943 -49.679 1.00 23.39  ?  124 PRO E CB  1 
ATOM   5702 C CG  . PRO E 5 125 ? 25.143 -35.424 -49.441 1.00 25.80  ?  124 PRO E CG  1 
ATOM   5703 C CD  . PRO E 5 125 ? 23.869 -35.689 -48.663 1.00 23.47  ?  124 PRO E CD  1 
ATOM   5704 N N   . PRO E 5 126 ? 23.406 -32.540 -51.876 1.00 25.41  ?  125 PRO E N   1 
ATOM   5705 C CA  . PRO E 5 126 ? 22.841 -32.566 -53.231 1.00 25.95  ?  125 PRO E CA  1 
ATOM   5706 C C   . PRO E 5 126 ? 23.573 -33.518 -54.163 1.00 30.74  ?  125 PRO E C   1 
ATOM   5707 O O   . PRO E 5 126 ? 24.754 -33.828 -53.988 1.00 24.85  ?  125 PRO E O   1 
ATOM   5708 C CB  . PRO E 5 126 ? 23.026 -31.123 -53.722 1.00 24.31  ?  125 PRO E CB  1 
ATOM   5709 C CG  . PRO E 5 126 ? 24.305 -30.663 -53.043 1.00 23.73  ?  125 PRO E CG  1 
ATOM   5710 C CD  . PRO E 5 126 ? 24.228 -31.335 -51.639 1.00 28.17  ?  125 PRO E CD  1 
ATOM   5711 N N   . GLU E 5 127 ? 22.849 -33.937 -55.199 1.00 26.28  ?  126 GLU E N   1 
ATOM   5712 C CA  . GLU E 5 127 ? 23.461 -34.365 -56.452 1.00 32.14  ?  126 GLU E CA  1 
ATOM   5713 C C   . GLU E 5 127 ? 23.350 -33.231 -57.463 1.00 24.13  ?  126 GLU E C   1 
ATOM   5714 O O   . GLU E 5 127 ? 22.395 -32.449 -57.440 1.00 25.51  ?  126 GLU E O   1 
ATOM   5715 C CB  . GLU E 5 127 ? 22.787 -35.623 -57.001 1.00 29.09  ?  126 GLU E CB  1 
ATOM   5716 C CG  . GLU E 5 127 ? 22.711 -36.763 -56.013 1.00 37.67  ?  126 GLU E CG  1 
ATOM   5717 C CD  . GLU E 5 127 ? 22.285 -38.058 -56.699 1.00 54.03  ?  126 GLU E CD  1 
ATOM   5718 O OE1 . GLU E 5 127 ? 22.366 -38.126 -57.953 1.00 57.26  ?  126 GLU E OE1 1 
ATOM   5719 O OE2 . GLU E 5 127 ? 21.879 -39.004 -55.993 1.00 55.10  -1 126 GLU E OE2 1 
ATOM   5720 N N   . VAL E 5 128 ? 24.354 -33.103 -58.322 1.00 22.91  ?  127 VAL E N   1 
ATOM   5721 C CA  . VAL E 5 128 ? 24.433 -31.948 -59.218 1.00 26.38  ?  127 VAL E CA  1 
ATOM   5722 C C   . VAL E 5 128 ? 24.627 -32.458 -60.637 1.00 28.14  ?  127 VAL E C   1 
ATOM   5723 O O   . VAL E 5 128 ? 25.386 -33.407 -60.859 1.00 26.36  ?  127 VAL E O   1 
ATOM   5724 C CB  . VAL E 5 128 ? 25.577 -30.982 -58.831 1.00 23.23  ?  127 VAL E CB  1 
ATOM   5725 C CG1 . VAL E 5 128 ? 25.715 -29.841 -59.874 1.00 18.45  ?  127 VAL E CG1 1 
ATOM   5726 C CG2 . VAL E 5 128 ? 25.343 -30.411 -57.425 1.00 22.32  ?  127 VAL E CG2 1 
ATOM   5727 N N   . ALA E 5 129 ? 23.955 -31.822 -61.603 1.00 22.45  ?  128 ALA E N   1 
ATOM   5728 C CA  . ALA E 5 129 ? 24.119 -32.235 -62.993 1.00 28.77  ?  128 ALA E CA  1 
ATOM   5729 C C   . ALA E 5 129 ? 24.055 -31.002 -63.885 1.00 27.36  ?  128 ALA E C   1 
ATOM   5730 O O   . ALA E 5 129 ? 23.323 -30.049 -63.591 1.00 26.77  ?  128 ALA E O   1 
ATOM   5731 C CB  . ALA E 5 129 ? 23.036 -33.259 -63.415 1.00 24.69  ?  128 ALA E CB  1 
ATOM   5732 N N   . VAL E 5 130 ? 24.823 -31.015 -64.963 1.00 21.79  ?  129 VAL E N   1 
ATOM   5733 C CA  . VAL E 5 130 ? 24.848 -29.914 -65.922 1.00 23.08  ?  129 VAL E CA  1 
ATOM   5734 C C   . VAL E 5 130 ? 24.257 -30.423 -67.225 1.00 28.44  ?  129 VAL E C   1 
ATOM   5735 O O   . VAL E 5 130 ? 24.662 -31.476 -67.724 1.00 26.51  ?  129 VAL E O   1 
ATOM   5736 C CB  . VAL E 5 130 ? 26.266 -29.376 -66.167 1.00 24.24  ?  129 VAL E CB  1 
ATOM   5737 C CG1 . VAL E 5 130 ? 26.235 -28.425 -67.347 1.00 25.25  ?  129 VAL E CG1 1 
ATOM   5738 C CG2 . VAL E 5 130 ? 26.773 -28.627 -64.930 1.00 31.09  ?  129 VAL E CG2 1 
ATOM   5739 N N   . PHE E 5 131 ? 23.328 -29.662 -67.782 1.00 28.21  ?  130 PHE E N   1 
ATOM   5740 C CA  . PHE E 5 131 ? 22.617 -30.059 -68.986 1.00 28.96  ?  130 PHE E CA  1 
ATOM   5741 C C   . PHE E 5 131 ? 23.105 -29.159 -70.110 1.00 29.05  ?  130 PHE E C   1 
ATOM   5742 O O   . PHE E 5 131 ? 23.082 -27.928 -69.979 1.00 27.81  ?  130 PHE E O   1 
ATOM   5743 C CB  . PHE E 5 131 ? 21.103 -29.957 -68.769 1.00 28.82  ?  130 PHE E CB  1 
ATOM   5744 C CG  . PHE E 5 131 ? 20.572 -30.933 -67.749 1.00 33.41  ?  130 PHE E CG  1 
ATOM   5745 C CD1 . PHE E 5 131 ? 20.662 -30.653 -66.373 1.00 29.39  ?  130 PHE E CD1 1 
ATOM   5746 C CD2 . PHE E 5 131 ? 20.013 -32.140 -68.154 1.00 28.97  ?  130 PHE E CD2 1 
ATOM   5747 C CE1 . PHE E 5 131 ? 20.192 -31.560 -65.425 1.00 30.67  ?  130 PHE E CE1 1 
ATOM   5748 C CE2 . PHE E 5 131 ? 19.553 -33.067 -67.220 1.00 31.21  ?  130 PHE E CE2 1 
ATOM   5749 C CZ  . PHE E 5 131 ? 19.641 -32.768 -65.832 1.00 34.15  ?  130 PHE E CZ  1 
ATOM   5750 N N   . GLU E 5 132 ? 23.586 -29.767 -71.185 1.00 28.78  ?  131 GLU E N   1 
ATOM   5751 C CA  . GLU E 5 132 ? 24.241 -29.036 -72.262 1.00 28.84  ?  131 GLU E CA  1 
ATOM   5752 C C   . GLU E 5 132 ? 23.235 -28.325 -73.162 1.00 31.51  ?  131 GLU E C   1 
ATOM   5753 O O   . GLU E 5 132 ? 22.050 -28.665 -73.197 1.00 28.65  ?  131 GLU E O   1 
ATOM   5754 C CB  . GLU E 5 132 ? 25.119 -29.986 -73.080 1.00 29.02  ?  131 GLU E CB  1 
ATOM   5755 C CG  . GLU E 5 132 ? 26.087 -30.711 -72.164 1.00 31.15  ?  131 GLU E CG  1 
ATOM   5756 C CD  . GLU E 5 132 ? 27.179 -31.502 -72.870 1.00 37.68  ?  131 GLU E CD  1 
ATOM   5757 O OE1 . GLU E 5 132 ? 28.106 -31.994 -72.183 1.00 45.68  ?  131 GLU E OE1 1 
ATOM   5758 O OE2 . GLU E 5 132 ? 27.106 -31.666 -74.100 1.00 51.76  -1 131 GLU E OE2 1 
ATOM   5759 N N   . PRO E 5 133 ? 23.693 -27.294 -73.863 1.00 32.37  ?  132 PRO E N   1 
ATOM   5760 C CA  . PRO E 5 133 ? 22.807 -26.506 -74.723 1.00 31.87  ?  132 PRO E CA  1 
ATOM   5761 C C   . PRO E 5 133 ? 22.195 -27.351 -75.831 1.00 31.48  ?  132 PRO E C   1 
ATOM   5762 O O   . PRO E 5 133 ? 22.851 -28.216 -76.407 1.00 29.00  ?  132 PRO E O   1 
ATOM   5763 C CB  . PRO E 5 133 ? 23.748 -25.447 -75.311 1.00 29.37  ?  132 PRO E CB  1 
ATOM   5764 C CG  . PRO E 5 133 ? 24.913 -25.376 -74.335 1.00 31.39  ?  132 PRO E CG  1 
ATOM   5765 C CD  . PRO E 5 133 ? 25.072 -26.769 -73.819 1.00 29.95  ?  132 PRO E CD  1 
ATOM   5766 N N   . SER E 5 134 ? 20.951 -27.054 -76.176 1.00 29.30  ?  133 SER E N   1 
ATOM   5767 C CA  . SER E 5 134 ? 20.328 -27.763 -77.286 1.00 38.22  ?  133 SER E CA  1 
ATOM   5768 C C   . SER E 5 134 ? 20.803 -27.191 -78.616 1.00 32.62  ?  133 SER E C   1 
ATOM   5769 O O   . SER E 5 134 ? 21.041 -25.989 -78.743 1.00 26.41  ?  133 SER E O   1 
ATOM   5770 C CB  . SER E 5 134 ? 18.807 -27.682 -77.194 1.00 35.95  ?  133 SER E CB  1 
ATOM   5771 O OG  . SER E 5 134 ? 18.314 -26.680 -78.038 1.00 39.45  ?  133 SER E OG  1 
ATOM   5772 N N   . GLU E 5 135 ? 20.959 -28.072 -79.609 1.00 32.08  ?  134 GLU E N   1 
ATOM   5773 C CA  . GLU E 5 135 ? 21.386 -27.613 -80.922 1.00 33.52  ?  134 GLU E CA  1 
ATOM   5774 C C   . GLU E 5 135 ? 20.332 -26.704 -81.534 1.00 29.25  ?  134 GLU E C   1 
ATOM   5775 O O   . GLU E 5 135 ? 20.655 -25.815 -82.323 1.00 32.85  ?  134 GLU E O   1 
ATOM   5776 C CB  . GLU E 5 135 ? 21.690 -28.817 -81.829 1.00 45.78  ?  134 GLU E CB  1 
ATOM   5777 C CG  . GLU E 5 135 ? 22.987 -29.592 -81.465 1.00 47.71  ?  134 GLU E CG  1 
ATOM   5778 C CD  . GLU E 5 135 ? 24.236 -28.681 -81.281 1.00 56.12  ?  134 GLU E CD  1 
ATOM   5779 O OE1 . GLU E 5 135 ? 24.583 -27.895 -82.206 1.00 53.53  ?  134 GLU E OE1 1 
ATOM   5780 O OE2 . GLU E 5 135 ? 24.878 -28.751 -80.197 1.00 59.50  -1 134 GLU E OE2 1 
ATOM   5781 N N   . ALA E 5 136 ? 19.078 -26.861 -81.130 1.00 29.26  ?  135 ALA E N   1 
ATOM   5782 C CA  . ALA E 5 136 ? 18.038 -26.003 -81.674 1.00 34.54  ?  135 ALA E CA  1 
ATOM   5783 C C   . ALA E 5 136 ? 18.181 -24.577 -81.160 1.00 36.59  ?  135 ALA E C   1 
ATOM   5784 O O   . ALA E 5 136 ? 18.020 -23.620 -81.932 1.00 29.00  ?  135 ALA E O   1 
ATOM   5785 C CB  . ALA E 5 136 ? 16.660 -26.580 -81.350 1.00 34.96  ?  135 ALA E CB  1 
ATOM   5786 N N   . GLU E 5 137 ? 18.515 -24.390 -79.872 1.00 25.97  ?  136 GLU E N   1 
ATOM   5787 C CA  . GLU E 5 137 ? 18.713 -23.008 -79.441 1.00 28.86  ?  136 GLU E CA  1 
ATOM   5788 C C   . GLU E 5 137 ? 19.894 -22.391 -80.183 1.00 27.73  ?  136 GLU E C   1 
ATOM   5789 O O   . GLU E 5 137 ? 19.814 -21.250 -80.664 1.00 29.69  ?  136 GLU E O   1 
ATOM   5790 C CB  . GLU E 5 137 ? 18.886 -22.908 -77.903 1.00 26.90  ?  136 GLU E CB  1 
ATOM   5791 C CG  . GLU E 5 137 ? 19.330 -21.493 -77.412 1.00 26.49  ?  136 GLU E CG  1 
ATOM   5792 C CD  . GLU E 5 137 ? 19.807 -21.474 -75.933 1.00 30.01  ?  136 GLU E CD  1 
ATOM   5793 O OE1 . GLU E 5 137 ? 20.230 -22.541 -75.458 1.00 22.64  ?  136 GLU E OE1 1 
ATOM   5794 O OE2 . GLU E 5 137 ? 19.748 -20.393 -75.271 1.00 26.95  -1 136 GLU E OE2 1 
ATOM   5795 N N   . ILE E 5 138 ? 20.984 -23.151 -80.333 1.00 29.21  ?  137 ILE E N   1 
ATOM   5796 C CA  . ILE E 5 138 ? 22.160 -22.647 -81.038 1.00 30.91  ?  137 ILE E CA  1 
ATOM   5797 C C   . ILE E 5 138 ? 21.785 -22.233 -82.468 1.00 33.44  ?  137 ILE E C   1 
ATOM   5798 O O   . ILE E 5 138 ? 22.069 -21.117 -82.903 1.00 32.30  ?  137 ILE E O   1 
ATOM   5799 C CB  . ILE E 5 138 ? 23.280 -23.708 -81.001 1.00 33.11  ?  137 ILE E CB  1 
ATOM   5800 C CG1 . ILE E 5 138 ? 23.796 -23.860 -79.561 1.00 33.31  ?  137 ILE E CG1 1 
ATOM   5801 C CG2 . ILE E 5 138 ? 24.424 -23.344 -81.959 1.00 30.11  ?  137 ILE E CG2 1 
ATOM   5802 C CD1 . ILE E 5 138 ? 24.716 -25.054 -79.308 1.00 32.07  ?  137 ILE E CD1 1 
ATOM   5803 N N   . SER E 5 139 ? 21.075 -23.110 -83.180 1.00 29.66  ?  138 SER E N   1 
ATOM   5804 C CA  . SER E 5 139 ? 20.589 -22.788 -84.524 1.00 38.61  ?  138 SER E CA  1 
ATOM   5805 C C   . SER E 5 139 ? 19.683 -21.572 -84.506 1.00 34.58  ?  138 SER E C   1 
ATOM   5806 O O   . SER E 5 139 ? 19.831 -20.661 -85.325 1.00 31.51  ?  138 SER E O   1 
ATOM   5807 C CB  . SER E 5 139 ? 19.832 -23.992 -85.097 1.00 39.71  ?  138 SER E CB  1 
ATOM   5808 O OG  . SER E 5 139 ? 20.741 -25.029 -85.418 1.00 46.91  ?  138 SER E OG  1 
ATOM   5809 N N   . HIS E 5 140 ? 18.738 -21.523 -83.576 1.00 35.34  ?  139 HIS E N   1 
ATOM   5810 C CA  . HIS E 5 140 ? 17.720 -20.481 -83.617 1.00 33.94  ?  139 HIS E CA  1 
ATOM   5811 C C   . HIS E 5 140 ? 18.236 -19.124 -83.127 1.00 39.38  ?  139 HIS E C   1 
ATOM   5812 O O   . HIS E 5 140 ? 17.808 -18.074 -83.621 1.00 39.84  ?  139 HIS E O   1 
ATOM   5813 C CB  . HIS E 5 140 ? 16.531 -20.939 -82.783 1.00 37.49  ?  139 HIS E CB  1 
ATOM   5814 C CG  . HIS E 5 140 ? 15.266 -20.192 -83.058 1.00 42.25  ?  139 HIS E CG  1 
ATOM   5815 N ND1 . HIS E 5 140 ? 14.477 -20.439 -84.167 1.00 39.87  ?  139 HIS E ND1 1 
ATOM   5816 C CD2 . HIS E 5 140 ? 14.641 -19.219 -82.355 1.00 39.63  ?  139 HIS E CD2 1 
ATOM   5817 C CE1 . HIS E 5 140 ? 13.423 -19.646 -84.132 1.00 35.75  ?  139 HIS E CE1 1 
ATOM   5818 N NE2 . HIS E 5 140 ? 13.498 -18.896 -83.045 1.00 42.92  ?  139 HIS E NE2 1 
ATOM   5819 N N   . THR E 5 141 ? 19.112 -19.110 -82.114 1.00 35.25  ?  140 THR E N   1 
ATOM   5820 C CA  . THR E 5 141 ? 19.495 -17.848 -81.498 1.00 33.79  ?  140 THR E CA  1 
ATOM   5821 C C   . THR E 5 141 ? 20.965 -17.505 -81.605 1.00 31.01  ?  140 THR E C   1 
ATOM   5822 O O   . THR E 5 141 ? 21.329 -16.384 -81.243 1.00 29.97  ?  140 THR E O   1 
ATOM   5823 C CB  . THR E 5 141 ? 19.151 -17.830 -79.996 1.00 34.94  ?  140 THR E CB  1 
ATOM   5824 O OG1 . THR E 5 141 ? 19.992 -18.778 -79.318 1.00 30.10  ?  140 THR E OG1 1 
ATOM   5825 C CG2 . THR E 5 141 ? 17.695 -18.192 -79.754 1.00 33.42  ?  140 THR E CG2 1 
ATOM   5826 N N   . GLN E 5 142 ? 21.825 -18.428 -82.035 1.00 29.91  ?  141 GLN E N   1 
ATOM   5827 C CA  . GLN E 5 142 ? 23.277 -18.264 -81.889 1.00 31.72  ?  141 GLN E CA  1 
ATOM   5828 C C   . GLN E 5 142 ? 23.692 -17.993 -80.430 1.00 33.69  ?  141 GLN E C   1 
ATOM   5829 O O   . GLN E 5 142 ? 24.699 -17.339 -80.173 1.00 30.31  ?  141 GLN E O   1 
ATOM   5830 C CB  . GLN E 5 142 ? 23.813 -17.160 -82.808 1.00 34.44  ?  141 GLN E CB  1 
ATOM   5831 C CG  . GLN E 5 142 ? 23.712 -17.504 -84.314 1.00 40.28  ?  141 GLN E CG  1 
ATOM   5832 C CD  . GLN E 5 142 ? 24.550 -18.725 -84.715 1.00 47.95  ?  141 GLN E CD  1 
ATOM   5833 O OE1 . GLN E 5 142 ? 25.740 -18.815 -84.393 1.00 55.92  ?  141 GLN E OE1 1 
ATOM   5834 N NE2 . GLN E 5 142 ? 23.929 -19.667 -85.429 1.00 49.65  ?  141 GLN E NE2 1 
ATOM   5835 N N   . LYS E 5 143 ? 22.900 -18.453 -79.460 1.00 30.17  ?  142 LYS E N   1 
ATOM   5836 C CA  . LYS E 5 143 ? 23.281 -18.474 -78.056 1.00 29.80  ?  142 LYS E CA  1 
ATOM   5837 C C   . LYS E 5 143 ? 23.083 -19.896 -77.541 1.00 32.09  ?  142 LYS E C   1 
ATOM   5838 O O   . LYS E 5 143 ? 22.392 -20.708 -78.169 1.00 29.81  ?  142 LYS E O   1 
ATOM   5839 C CB  . LYS E 5 143 ? 22.463 -17.474 -77.228 1.00 25.74  ?  142 LYS E CB  1 
ATOM   5840 C CG  . LYS E 5 143 ? 22.591 -16.000 -77.716 1.00 27.40  ?  142 LYS E CG  1 
ATOM   5841 C CD  . LYS E 5 143 ? 21.879 -15.031 -76.766 1.00 31.77  ?  142 LYS E CD  1 
ATOM   5842 C CE  . LYS E 5 143 ? 22.320 -13.588 -77.004 1.00 38.65  ?  142 LYS E CE  1 
ATOM   5843 N NZ  . LYS E 5 143 ? 21.845 -13.127 -78.345 1.00 39.53  ?  142 LYS E NZ  1 
ATOM   5844 N N   . ALA E 5 144 ? 23.711 -20.205 -76.401 1.00 27.44  ?  143 ALA E N   1 
ATOM   5845 C CA  . ALA E 5 144 ? 23.667 -21.547 -75.821 1.00 26.52  ?  143 ALA E CA  1 
ATOM   5846 C C   . ALA E 5 144 ? 23.490 -21.435 -74.313 1.00 27.46  ?  143 ALA E C   1 
ATOM   5847 O O   . ALA E 5 144 ? 24.335 -20.854 -73.632 1.00 25.29  ?  143 ALA E O   1 
ATOM   5848 C CB  . ALA E 5 144 ? 24.938 -22.330 -76.149 1.00 26.92  ?  143 ALA E CB  1 
ATOM   5849 N N   . THR E 5 145 ? 22.396 -21.993 -73.802 1.00 25.45  ?  144 THR E N   1 
ATOM   5850 C CA  . THR E 5 145 ? 22.058 -21.939 -72.391 1.00 30.76  ?  144 THR E CA  1 
ATOM   5851 C C   . THR E 5 145 ? 22.420 -23.268 -71.743 1.00 31.48  ?  144 THR E C   1 
ATOM   5852 O O   . THR E 5 145 ? 21.910 -24.321 -72.153 1.00 25.29  ?  144 THR E O   1 
ATOM   5853 C CB  . THR E 5 145 ? 20.567 -21.648 -72.194 1.00 26.04  ?  144 THR E CB  1 
ATOM   5854 O OG1 . THR E 5 145 ? 20.243 -20.419 -72.831 1.00 26.43  ?  144 THR E OG1 1 
ATOM   5855 C CG2 . THR E 5 145 ? 20.241 -21.521 -70.701 1.00 25.96  ?  144 THR E CG2 1 
ATOM   5856 N N   . LEU E 5 146 ? 23.284 -23.221 -70.725 1.00 26.26  ?  145 LEU E N   1 
ATOM   5857 C CA  . LEU E 5 146 ? 23.503 -24.382 -69.876 1.00 25.77  ?  145 LEU E CA  1 
ATOM   5858 C C   . LEU E 5 146 ? 22.612 -24.293 -68.645 1.00 25.18  ?  145 LEU E C   1 
ATOM   5859 O O   . LEU E 5 146 ? 22.330 -23.203 -68.132 1.00 25.31  ?  145 LEU E O   1 
ATOM   5860 C CB  . LEU E 5 146 ? 24.960 -24.499 -69.431 1.00 26.99  ?  145 LEU E CB  1 
ATOM   5861 C CG  . LEU E 5 146 ? 26.057 -24.754 -70.470 1.00 26.17  ?  145 LEU E CG  1 
ATOM   5862 C CD1 . LEU E 5 146 ? 26.455 -23.448 -71.148 1.00 26.62  ?  145 LEU E CD1 1 
ATOM   5863 C CD2 . LEU E 5 146 ? 27.238 -25.356 -69.719 1.00 26.06  ?  145 LEU E CD2 1 
ATOM   5864 N N   . VAL E 5 147 ? 22.179 -25.452 -68.156 1.00 23.73  ?  146 VAL E N   1 
ATOM   5865 C CA  . VAL E 5 147 ? 21.337 -25.500 -66.972 1.00 24.57  ?  146 VAL E CA  1 
ATOM   5866 C C   . VAL E 5 147 ? 22.012 -26.400 -65.958 1.00 27.14  ?  146 VAL E C   1 
ATOM   5867 O O   . VAL E 5 147 ? 22.494 -27.487 -66.303 1.00 24.44  ?  146 VAL E O   1 
ATOM   5868 C CB  . VAL E 5 147 ? 19.912 -25.986 -67.290 1.00 26.17  ?  146 VAL E CB  1 
ATOM   5869 C CG1 . VAL E 5 147 ? 19.206 -26.418 -65.996 1.00 28.50  ?  146 VAL E CG1 1 
ATOM   5870 C CG2 . VAL E 5 147 ? 19.115 -24.873 -68.038 1.00 24.52  ?  146 VAL E CG2 1 
ATOM   5871 N N   . CYS E 5 148 ? 22.064 -25.934 -64.721 1.00 24.68  ?  147 CYS E N   1 
ATOM   5872 C CA  . CYS E 5 148 ? 22.562 -26.710 -63.599 1.00 26.30  ?  147 CYS E CA  1 
ATOM   5873 C C   . CYS E 5 148 ? 21.370 -27.090 -62.729 1.00 24.99  ?  147 CYS E C   1 
ATOM   5874 O O   . CYS E 5 148 ? 20.460 -26.275 -62.524 1.00 26.37  ?  147 CYS E O   1 
ATOM   5875 C CB  . CYS E 5 148 ? 23.606 -25.904 -62.796 1.00 22.66  ?  147 CYS E CB  1 
ATOM   5876 S SG  . CYS E 5 148 ? 24.269 -26.897 -61.407 1.00 30.44  ?  147 CYS E SG  1 
ATOM   5877 N N   . LEU E 5 149 ? 21.350 -28.339 -62.256 1.00 26.27  ?  148 LEU E N   1 
ATOM   5878 C CA  . LEU E 5 149 ? 20.297 -28.836 -61.373 1.00 25.62  ?  148 LEU E CA  1 
ATOM   5879 C C   . LEU E 5 149 ? 20.921 -29.457 -60.133 1.00 28.31  ?  148 LEU E C   1 
ATOM   5880 O O   . LEU E 5 149 ? 21.662 -30.436 -60.239 1.00 24.92  ?  148 LEU E O   1 
ATOM   5881 C CB  . LEU E 5 149 ? 19.432 -29.885 -62.085 1.00 28.73  ?  148 LEU E CB  1 
ATOM   5882 C CG  . LEU E 5 149 ? 17.928 -29.826 -61.920 1.00 35.04  ?  148 LEU E CG  1 
ATOM   5883 C CD1 . LEU E 5 149 ? 17.425 -28.481 -62.458 1.00 33.91  ?  148 LEU E CD1 1 
ATOM   5884 C CD2 . LEU E 5 149 ? 17.333 -30.975 -62.698 1.00 38.32  ?  148 LEU E CD2 1 
ATOM   5885 N N   . ALA E 5 150 ? 20.574 -28.943 -58.963 1.00 25.99  ?  149 ALA E N   1 
ATOM   5886 C CA  . ALA E 5 150 ? 20.945 -29.576 -57.708 1.00 24.01  ?  149 ALA E CA  1 
ATOM   5887 C C   . ALA E 5 150 ? 19.698 -30.231 -57.137 1.00 22.65  ?  149 ALA E C   1 
ATOM   5888 O O   . ALA E 5 150 ? 18.645 -29.599 -57.081 1.00 25.90  ?  149 ALA E O   1 
ATOM   5889 C CB  . ALA E 5 150 ? 21.520 -28.548 -56.734 1.00 24.50  ?  149 ALA E CB  1 
ATOM   5890 N N   . THR E 5 151 ? 19.800 -31.498 -56.745 1.00 23.24  ?  150 THR E N   1 
ATOM   5891 C CA  . THR E 5 151 ? 18.601 -32.214 -56.348 1.00 26.05  ?  150 THR E CA  1 
ATOM   5892 C C   . THR E 5 151 ? 18.854 -33.030 -55.091 1.00 30.51  ?  150 THR E C   1 
ATOM   5893 O O   . THR E 5 151 ? 19.997 -33.378 -54.758 1.00 26.24  ?  150 THR E O   1 
ATOM   5894 C CB  . THR E 5 151 ? 18.089 -33.153 -57.462 1.00 25.95  ?  150 THR E CB  1 
ATOM   5895 O OG1 . THR E 5 151 ? 19.144 -34.025 -57.898 1.00 27.99  ?  150 THR E OG1 1 
ATOM   5896 C CG2 . THR E 5 151 ? 17.594 -32.335 -58.631 1.00 23.42  ?  150 THR E CG2 1 
ATOM   5897 N N   . GLY E 5 152 ? 17.752 -33.358 -54.415 1.00 25.17  ?  151 GLY E N   1 
ATOM   5898 C CA  . GLY E 5 152 ? 17.803 -34.352 -53.366 1.00 28.75  ?  151 GLY E CA  1 
ATOM   5899 C C   . GLY E 5 152 ? 18.463 -33.897 -52.084 1.00 32.62  ?  151 GLY E C   1 
ATOM   5900 O O   . GLY E 5 152 ? 18.843 -34.744 -51.267 1.00 26.49  ?  151 GLY E O   1 
ATOM   5901 N N   . PHE E 5 153 ? 18.619 -32.589 -51.870 1.00 27.82  ?  152 PHE E N   1 
ATOM   5902 C CA  . PHE E 5 153 ? 19.336 -32.146 -50.680 1.00 26.40  ?  152 PHE E CA  1 
ATOM   5903 C C   . PHE E 5 153 ? 18.370 -31.669 -49.599 1.00 30.30  ?  152 PHE E C   1 
ATOM   5904 O O   . PHE E 5 153 ? 17.273 -31.182 -49.888 1.00 28.02  ?  152 PHE E O   1 
ATOM   5905 C CB  . PHE E 5 153 ? 20.361 -31.049 -51.013 1.00 23.06  ?  152 PHE E CB  1 
ATOM   5906 C CG  . PHE E 5 153 ? 19.777 -29.799 -51.683 1.00 24.13  ?  152 PHE E CG  1 
ATOM   5907 C CD1 . PHE E 5 153 ? 19.658 -29.724 -53.063 1.00 26.50  ?  152 PHE E CD1 1 
ATOM   5908 C CD2 . PHE E 5 153 ? 19.386 -28.699 -50.932 1.00 27.24  ?  152 PHE E CD2 1 
ATOM   5909 C CE1 . PHE E 5 153 ? 19.153 -28.572 -53.692 1.00 27.16  ?  152 PHE E CE1 1 
ATOM   5910 C CE2 . PHE E 5 153 ? 18.879 -27.551 -51.549 1.00 22.84  ?  152 PHE E CE2 1 
ATOM   5911 C CZ  . PHE E 5 153 ? 18.770 -27.495 -52.937 1.00 28.19  ?  152 PHE E CZ  1 
ATOM   5912 N N   . TYR E 5 154 ? 18.804 -31.809 -48.340 1.00 27.11  ?  153 TYR E N   1 
ATOM   5913 C CA  . TYR E 5 154 ? 18.097 -31.329 -47.163 1.00 27.67  ?  153 TYR E CA  1 
ATOM   5914 C C   . TYR E 5 154 ? 19.135 -31.006 -46.090 1.00 26.72  ?  153 TYR E C   1 
ATOM   5915 O O   . TYR E 5 154 ? 20.010 -31.839 -45.824 1.00 26.26  ?  153 TYR E O   1 
ATOM   5916 C CB  . TYR E 5 154 ? 17.102 -32.352 -46.603 1.00 26.92  ?  153 TYR E CB  1 
ATOM   5917 C CG  . TYR E 5 154 ? 16.392 -31.836 -45.356 1.00 32.02  ?  153 TYR E CG  1 
ATOM   5918 C CD1 . TYR E 5 154 ? 16.957 -31.996 -44.097 1.00 29.05  ?  153 TYR E CD1 1 
ATOM   5919 C CD2 . TYR E 5 154 ? 15.177 -31.161 -45.446 1.00 32.25  ?  153 TYR E CD2 1 
ATOM   5920 C CE1 . TYR E 5 154 ? 16.317 -31.516 -42.954 1.00 35.93  ?  153 TYR E CE1 1 
ATOM   5921 C CE2 . TYR E 5 154 ? 14.533 -30.687 -44.314 1.00 35.94  ?  153 TYR E CE2 1 
ATOM   5922 C CZ  . TYR E 5 154 ? 15.116 -30.862 -43.069 1.00 36.00  ?  153 TYR E CZ  1 
ATOM   5923 O OH  . TYR E 5 154 ? 14.481 -30.382 -41.945 1.00 40.44  ?  153 TYR E OH  1 
ATOM   5924 N N   . PRO E 5 155 ? 19.043 -29.850 -45.436 1.00 29.43  ?  154 PRO E N   1 
ATOM   5925 C CA  . PRO E 5 155 ? 18.039 -28.822 -45.691 1.00 26.01  ?  154 PRO E CA  1 
ATOM   5926 C C   . PRO E 5 155 ? 18.494 -27.959 -46.857 1.00 27.75  ?  154 PRO E C   1 
ATOM   5927 O O   . PRO E 5 155 ? 19.489 -28.299 -47.524 1.00 27.17  ?  154 PRO E O   1 
ATOM   5928 C CB  . PRO E 5 155 ? 18.046 -28.027 -44.392 1.00 32.56  ?  154 PRO E CB  1 
ATOM   5929 C CG  . PRO E 5 155 ? 19.499 -28.016 -44.051 1.00 27.10  ?  154 PRO E CG  1 
ATOM   5930 C CD  . PRO E 5 155 ? 19.984 -29.421 -44.386 1.00 27.88  ?  154 PRO E CD  1 
ATOM   5931 N N   . ASP E 5 156 ? 17.809 -26.849 -47.105 1.00 25.18  ?  155 ASP E N   1 
ATOM   5932 C CA  . ASP E 5 156 ? 18.149 -26.024 -48.264 1.00 29.35  ?  155 ASP E CA  1 
ATOM   5933 C C   . ASP E 5 156 ? 19.279 -25.044 -47.954 1.00 33.24  ?  155 ASP E C   1 
ATOM   5934 O O   . ASP E 5 156 ? 19.169 -23.853 -48.221 1.00 36.16  ?  155 ASP E O   1 
ATOM   5935 C CB  . ASP E 5 156 ? 16.900 -25.301 -48.758 1.00 34.96  ?  155 ASP E CB  1 
ATOM   5936 C CG  . ASP E 5 156 ? 16.400 -24.244 -47.783 1.00 42.53  ?  155 ASP E CG  1 
ATOM   5937 O OD1 . ASP E 5 156 ? 16.628 -24.359 -46.556 1.00 39.40  ?  155 ASP E OD1 1 
ATOM   5938 O OD2 . ASP E 5 156 ? 15.753 -23.295 -48.255 1.00 43.96  -1 155 ASP E OD2 1 
ATOM   5939 N N   . HIS E 5 157 ? 20.368 -25.527 -47.331 1.00 28.87  ?  156 HIS E N   1 
ATOM   5940 C CA  . HIS E 5 157 ? 21.523 -24.678 -47.004 1.00 29.79  ?  156 HIS E CA  1 
ATOM   5941 C C   . HIS E 5 157 ? 22.573 -24.889 -48.090 1.00 22.96  ?  156 HIS E C   1 
ATOM   5942 O O   . HIS E 5 157 ? 23.491 -25.683 -47.925 1.00 24.93  ?  156 HIS E O   1 
ATOM   5943 C CB  . HIS E 5 157 ? 22.099 -25.001 -45.624 1.00 24.15  ?  156 HIS E CB  1 
ATOM   5944 C CG  . HIS E 5 157 ? 21.141 -24.759 -44.510 1.00 27.61  ?  156 HIS E CG  1 
ATOM   5945 N ND1 . HIS E 5 157 ? 21.425 -25.062 -43.193 1.00 26.14  ?  156 HIS E ND1 1 
ATOM   5946 C CD2 . HIS E 5 157 ? 19.880 -24.272 -44.523 1.00 27.59  ?  156 HIS E CD2 1 
ATOM   5947 C CE1 . HIS E 5 157 ? 20.379 -24.768 -42.449 1.00 23.29  ?  156 HIS E CE1 1 
ATOM   5948 N NE2 . HIS E 5 157 ? 19.435 -24.278 -43.229 1.00 25.70  ?  156 HIS E NE2 1 
ATOM   5949 N N   . VAL E 5 158 ? 22.448 -24.157 -49.198 1.00 23.48  ?  157 VAL E N   1 
ATOM   5950 C CA  . VAL E 5 158 ? 23.287 -24.375 -50.373 1.00 23.72  ?  157 VAL E CA  1 
ATOM   5951 C C   . VAL E 5 158 ? 23.611 -23.038 -50.999 1.00 25.07  ?  157 VAL E C   1 
ATOM   5952 O O   . VAL E 5 158 ? 22.834 -22.086 -50.903 1.00 24.90  ?  157 VAL E O   1 
ATOM   5953 C CB  . VAL E 5 158 ? 22.621 -25.284 -51.441 1.00 23.80  ?  157 VAL E CB  1 
ATOM   5954 C CG1 . VAL E 5 158 ? 22.345 -26.650 -50.879 1.00 21.70  ?  157 VAL E CG1 1 
ATOM   5955 C CG2 . VAL E 5 158 ? 21.313 -24.645 -51.971 1.00 20.31  ?  157 VAL E CG2 1 
ATOM   5956 N N   . GLU E 5 159 ? 24.762 -22.982 -51.667 1.00 21.34  ?  158 GLU E N   1 
ATOM   5957 C CA  . GLU E 5 159 ? 25.124 -21.863 -52.521 1.00 21.44  ?  158 GLU E CA  1 
ATOM   5958 C C   . GLU E 5 159 ? 25.633 -22.442 -53.825 1.00 24.24  ?  158 GLU E C   1 
ATOM   5959 O O   . GLU E 5 159 ? 26.507 -23.312 -53.816 1.00 22.05  ?  158 GLU E O   1 
ATOM   5960 C CB  . GLU E 5 159 ? 26.201 -20.982 -51.886 1.00 21.26  ?  158 GLU E CB  1 
ATOM   5961 C CG  . GLU E 5 159 ? 25.796 -20.449 -50.532 1.00 26.36  ?  158 GLU E CG  1 
ATOM   5962 C CD  . GLU E 5 159 ? 26.993 -19.921 -49.708 1.00 28.26  ?  158 GLU E CD  1 
ATOM   5963 O OE1 . GLU E 5 159 ? 28.124 -20.403 -49.924 1.00 30.51  ?  158 GLU E OE1 1 
ATOM   5964 O OE2 . GLU E 5 159 ? 26.769 -19.070 -48.816 1.00 37.77  -1 158 GLU E OE2 1 
ATOM   5965 N N   . LEU E 5 160 ? 25.104 -21.959 -54.930 1.00 21.88  ?  159 LEU E N   1 
ATOM   5966 C CA  . LEU E 5 160 ? 25.455 -22.468 -56.244 1.00 24.18  ?  159 LEU E CA  1 
ATOM   5967 C C   . LEU E 5 160 ? 26.248 -21.406 -56.985 1.00 24.05  ?  159 LEU E C   1 
ATOM   5968 O O   . LEU E 5 160 ? 25.866 -20.235 -56.965 1.00 24.12  ?  159 LEU E O   1 
ATOM   5969 C CB  . LEU E 5 160 ? 24.177 -22.804 -57.023 1.00 24.22  ?  159 LEU E CB  1 
ATOM   5970 C CG  . LEU E 5 160 ? 24.352 -23.438 -58.389 1.00 24.77  ?  159 LEU E CG  1 
ATOM   5971 C CD1 . LEU E 5 160 ? 23.101 -24.269 -58.690 1.00 24.62  ?  159 LEU E CD1 1 
ATOM   5972 C CD2 . LEU E 5 160 ? 24.647 -22.390 -59.491 1.00 24.01  ?  159 LEU E CD2 1 
ATOM   5973 N N   . SER E 5 161 ? 27.333 -21.802 -57.659 1.00 20.22  ?  160 SER E N   1 
ATOM   5974 C CA  . SER E 5 161 ? 28.108 -20.854 -58.447 1.00 22.55  ?  160 SER E CA  1 
ATOM   5975 C C   . SER E 5 161 ? 28.549 -21.508 -59.753 1.00 23.43  ?  160 SER E C   1 
ATOM   5976 O O   . SER E 5 161 ? 28.652 -22.728 -59.853 1.00 20.39  ?  160 SER E O   1 
ATOM   5977 C CB  . SER E 5 161 ? 29.340 -20.319 -57.681 1.00 26.14  ?  160 SER E CB  1 
ATOM   5978 O OG  . SER E 5 161 ? 30.080 -21.361 -57.078 1.00 25.79  ?  160 SER E OG  1 
ATOM   5979 N N   . TRP E 5 162 ? 28.813 -20.671 -60.761 1.00 22.42  ?  161 TRP E N   1 
ATOM   5980 C CA  . TRP E 5 162 ? 29.354 -21.110 -62.041 1.00 25.53  ?  161 TRP E CA  1 
ATOM   5981 C C   . TRP E 5 162 ? 30.813 -20.710 -62.215 1.00 24.77  ?  161 TRP E C   1 
ATOM   5982 O O   . TRP E 5 162 ? 31.207 -19.592 -61.878 1.00 26.79  ?  161 TRP E O   1 
ATOM   5983 C CB  . TRP E 5 162 ? 28.567 -20.526 -63.211 1.00 19.51  ?  161 TRP E CB  1 
ATOM   5984 C CG  . TRP E 5 162 ? 27.183 -21.102 -63.383 1.00 24.90  ?  161 TRP E CG  1 
ATOM   5985 C CD1 . TRP E 5 162 ? 26.021 -20.612 -62.859 1.00 20.56  ?  161 TRP E CD1 1 
ATOM   5986 C CD2 . TRP E 5 162 ? 26.818 -22.227 -64.193 1.00 21.52  ?  161 TRP E CD2 1 
ATOM   5987 N NE1 . TRP E 5 162 ? 24.954 -21.385 -63.270 1.00 22.55  ?  161 TRP E NE1 1 
ATOM   5988 C CE2 . TRP E 5 162 ? 25.414 -22.371 -64.103 1.00 23.78  ?  161 TRP E CE2 1 
ATOM   5989 C CE3 . TRP E 5 162 ? 27.540 -23.133 -64.979 1.00 20.96  ?  161 TRP E CE3 1 
ATOM   5990 C CZ2 . TRP E 5 162 ? 24.714 -23.384 -64.789 1.00 25.24  ?  161 TRP E CZ2 1 
ATOM   5991 C CZ3 . TRP E 5 162 ? 26.837 -24.153 -65.667 1.00 26.44  ?  161 TRP E CZ3 1 
ATOM   5992 C CH2 . TRP E 5 162 ? 25.444 -24.259 -65.568 1.00 23.64  ?  161 TRP E CH2 1 
ATOM   5993 N N   . TRP E 5 163 ? 31.587 -21.614 -62.808 1.00 19.12  ?  162 TRP E N   1 
ATOM   5994 C CA  . TRP E 5 163 ? 33.011 -21.432 -62.998 1.00 21.19  ?  162 TRP E CA  1 
ATOM   5995 C C   . TRP E 5 163 ? 33.324 -21.779 -64.445 1.00 26.64  ?  162 TRP E C   1 
ATOM   5996 O O   . TRP E 5 163 ? 33.098 -22.920 -64.875 1.00 23.61  ?  162 TRP E O   1 
ATOM   5997 C CB  . TRP E 5 163 ? 33.800 -22.314 -62.014 1.00 23.04  ?  162 TRP E CB  1 
ATOM   5998 C CG  . TRP E 5 163 ? 33.477 -21.978 -60.594 1.00 26.52  ?  162 TRP E CG  1 
ATOM   5999 C CD1 . TRP E 5 163 ? 32.375 -22.371 -59.883 1.00 23.31  ?  162 TRP E CD1 1 
ATOM   6000 C CD2 . TRP E 5 163 ? 34.233 -21.121 -59.722 1.00 28.63  ?  162 TRP E CD2 1 
ATOM   6001 N NE1 . TRP E 5 163 ? 32.420 -21.840 -58.600 1.00 25.37  ?  162 TRP E NE1 1 
ATOM   6002 C CE2 . TRP E 5 163 ? 33.551 -21.070 -58.482 1.00 27.64  ?  162 TRP E CE2 1 
ATOM   6003 C CE3 . TRP E 5 163 ? 35.438 -20.423 -59.860 1.00 28.43  ?  162 TRP E CE3 1 
ATOM   6004 C CZ2 . TRP E 5 163 ? 34.016 -20.316 -57.398 1.00 29.76  ?  162 TRP E CZ2 1 
ATOM   6005 C CZ3 . TRP E 5 163 ? 35.911 -19.686 -58.772 1.00 31.21  ?  162 TRP E CZ3 1 
ATOM   6006 C CH2 . TRP E 5 163 ? 35.200 -19.640 -57.561 1.00 29.29  ?  162 TRP E CH2 1 
ATOM   6007 N N   . VAL E 5 164 ? 33.796 -20.789 -65.200 1.00 22.30  ?  163 VAL E N   1 
ATOM   6008 C CA  . VAL E 5 164 ? 34.133 -20.949 -66.608 1.00 21.31  ?  163 VAL E CA  1 
ATOM   6009 C C   . VAL E 5 164 ? 35.641 -20.795 -66.730 1.00 23.37  ?  163 VAL E C   1 
ATOM   6010 O O   . VAL E 5 164 ? 36.204 -19.784 -66.296 1.00 22.90  ?  163 VAL E O   1 
ATOM   6011 C CB  . VAL E 5 164 ? 33.396 -19.922 -67.488 1.00 29.05  ?  163 VAL E CB  1 
ATOM   6012 C CG1 . VAL E 5 164 ? 33.828 -20.056 -68.954 1.00 22.07  ?  163 VAL E CG1 1 
ATOM   6013 C CG2 . VAL E 5 164 ? 31.865 -20.056 -67.361 1.00 24.49  ?  163 VAL E CG2 1 
ATOM   6014 N N   . ASN E 5 165 ? 36.302 -21.805 -67.283 1.00 21.68  ?  164 ASN E N   1 
ATOM   6015 C CA  . ASN E 5 165 ? 37.759 -21.764 -67.428 1.00 27.11  ?  164 ASN E CA  1 
ATOM   6016 C C   . ASN E 5 165 ? 38.460 -21.434 -66.102 1.00 28.53  ?  164 ASN E C   1 
ATOM   6017 O O   . ASN E 5 165 ? 39.508 -20.779 -66.070 1.00 29.45  ?  164 ASN E O   1 
ATOM   6018 C CB  . ASN E 5 165 ? 38.139 -20.778 -68.539 1.00 29.93  ?  164 ASN E CB  1 
ATOM   6019 C CG  . ASN E 5 165 ? 37.653 -21.257 -69.909 1.00 31.24  ?  164 ASN E CG  1 
ATOM   6020 O OD1 . ASN E 5 165 ? 37.495 -22.464 -70.126 1.00 27.91  ?  164 ASN E OD1 1 
ATOM   6021 N ND2 . ASN E 5 165 ? 37.368 -20.337 -70.810 1.00 24.00  ?  164 ASN E ND2 1 
ATOM   6022 N N   . GLY E 5 166 ? 37.860 -21.865 -64.996 1.00 27.28  ?  165 GLY E N   1 
ATOM   6023 C CA  . GLY E 5 166 ? 38.441 -21.711 -63.670 1.00 30.15  ?  165 GLY E CA  1 
ATOM   6024 C C   . GLY E 5 166 ? 38.084 -20.440 -62.928 1.00 29.88  ?  165 GLY E C   1 
ATOM   6025 O O   . GLY E 5 166 ? 38.492 -20.290 -61.769 1.00 26.20  ?  165 GLY E O   1 
ATOM   6026 N N   . LYS E 5 167 ? 37.319 -19.533 -63.533 1.00 27.62  ?  166 LYS E N   1 
ATOM   6027 C CA  . LYS E 5 167 ? 36.975 -18.263 -62.914 1.00 26.24  ?  166 LYS E CA  1 
ATOM   6028 C C   . LYS E 5 167 ? 35.473 -18.205 -62.665 1.00 33.12  ?  166 LYS E C   1 
ATOM   6029 O O   . LYS E 5 167 ? 34.675 -18.582 -63.538 1.00 22.88  ?  166 LYS E O   1 
ATOM   6030 C CB  . LYS E 5 167 ? 37.403 -17.077 -63.796 1.00 29.91  ?  166 LYS E CB  1 
ATOM   6031 C CG  . LYS E 5 167 ? 38.876 -16.674 -63.630 1.00 41.54  ?  166 LYS E CG  1 
ATOM   6032 C CD  . LYS E 5 167 ? 39.091 -15.167 -63.827 1.00 51.48  ?  166 LYS E CD  1 
ATOM   6033 C CE  . LYS E 5 167 ? 38.466 -14.712 -65.131 1.00 53.91  ?  166 LYS E CE  1 
ATOM   6034 N NZ  . LYS E 5 167 ? 39.152 -13.520 -65.690 1.00 58.65  ?  166 LYS E NZ  1 
ATOM   6035 N N   . GLU E 5 168 ? 35.085 -17.726 -61.480 1.00 25.41  ?  167 GLU E N   1 
ATOM   6036 C CA  . GLU E 5 168 ? 33.664 -17.618 -61.190 1.00 28.41  ?  167 GLU E CA  1 
ATOM   6037 C C   . GLU E 5 168 ? 33.029 -16.602 -62.141 1.00 28.68  ?  167 GLU E C   1 
ATOM   6038 O O   . GLU E 5 168 ? 33.639 -15.596 -62.496 1.00 29.12  ?  167 GLU E O   1 
ATOM   6039 C CB  . GLU E 5 168 ? 33.422 -17.218 -59.729 1.00 22.51  ?  167 GLU E CB  1 
ATOM   6040 C CG  . GLU E 5 168 ? 31.928 -17.290 -59.401 1.00 26.42  ?  167 GLU E CG  1 
ATOM   6041 C CD  . GLU E 5 168 ? 31.570 -16.920 -57.968 1.00 36.67  ?  167 GLU E CD  1 
ATOM   6042 O OE1 . GLU E 5 168 ? 32.479 -16.630 -57.138 1.00 37.04  ?  167 GLU E OE1 1 
ATOM   6043 O OE2 . GLU E 5 168 ? 30.349 -16.921 -57.687 1.00 39.90  -1 167 GLU E OE2 1 
ATOM   6044 N N   . VAL E 5 169 ? 31.821 -16.888 -62.614 1.00 27.68  ?  168 VAL E N   1 
ATOM   6045 C CA  . VAL E 5 169 ? 31.157 -15.923 -63.484 1.00 26.27  ?  168 VAL E CA  1 
ATOM   6046 C C   . VAL E 5 169 ? 29.809 -15.542 -62.889 1.00 23.42  ?  168 VAL E C   1 
ATOM   6047 O O   . VAL E 5 169 ? 29.129 -16.351 -62.247 1.00 24.25  ?  168 VAL E O   1 
ATOM   6048 C CB  . VAL E 5 169 ? 31.002 -16.433 -64.938 1.00 26.44  ?  168 VAL E CB  1 
ATOM   6049 C CG1 . VAL E 5 169 ? 32.361 -16.610 -65.564 1.00 31.68  ?  168 VAL E CG1 1 
ATOM   6050 C CG2 . VAL E 5 169 ? 30.206 -17.737 -65.004 1.00 21.65  ?  168 VAL E CG2 1 
ATOM   6051 N N   . HIS E 5 170 ? 29.415 -14.288 -63.126 1.00 26.28  ?  169 HIS E N   1 
ATOM   6052 C CA  . HIS E 5 170 ? 28.054 -13.819 -62.866 1.00 29.17  ?  169 HIS E CA  1 
ATOM   6053 C C   . HIS E 5 170 ? 27.335 -13.266 -64.097 1.00 31.01  ?  169 HIS E C   1 
ATOM   6054 O O   . HIS E 5 170 ? 26.097 -13.309 -64.139 1.00 28.26  ?  169 HIS E O   1 
ATOM   6055 C CB  . HIS E 5 170 ? 28.057 -12.743 -61.765 1.00 30.42  ?  169 HIS E CB  1 
ATOM   6056 C CG  . HIS E 5 170 ? 28.802 -13.158 -60.532 1.00 33.20  ?  169 HIS E CG  1 
ATOM   6057 N ND1 . HIS E 5 170 ? 28.192 -13.781 -59.465 1.00 37.60  ?  169 HIS E ND1 1 
ATOM   6058 C CD2 . HIS E 5 170 ? 30.116 -13.067 -60.212 1.00 37.49  ?  169 HIS E CD2 1 
ATOM   6059 C CE1 . HIS E 5 170 ? 29.092 -14.038 -58.530 1.00 36.71  ?  169 HIS E CE1 1 
ATOM   6060 N NE2 . HIS E 5 170 ? 30.266 -13.610 -58.958 1.00 40.82  ?  169 HIS E NE2 1 
ATOM   6061 N N   . SER E 5 171 ? 28.060 -12.740 -65.088 1.00 30.77  ?  170 SER E N   1 
ATOM   6062 C CA  . SER E 5 171 ? 27.418 -12.345 -66.333 1.00 31.85  ?  170 SER E CA  1 
ATOM   6063 C C   . SER E 5 171 ? 26.751 -13.564 -66.968 1.00 28.73  ?  170 SER E C   1 
ATOM   6064 O O   . SER E 5 171 ? 27.355 -14.635 -67.059 1.00 26.17  ?  170 SER E O   1 
ATOM   6065 C CB  . SER E 5 171 ? 28.453 -11.741 -67.283 1.00 33.04  ?  170 SER E CB  1 
ATOM   6066 O OG  . SER E 5 171 ? 27.829 -11.188 -68.424 1.00 29.80  ?  170 SER E OG  1 
ATOM   6067 N N   . GLY E 5 172 ? 25.502 -13.408 -67.404 1.00 28.46  ?  171 GLY E N   1 
ATOM   6068 C CA  . GLY E 5 172 ? 24.824 -14.475 -68.114 1.00 25.64  ?  171 GLY E CA  1 
ATOM   6069 C C   . GLY E 5 172 ? 24.264 -15.566 -67.228 1.00 32.28  ?  171 GLY E C   1 
ATOM   6070 O O   . GLY E 5 172 ? 23.828 -16.607 -67.750 1.00 25.35  ?  171 GLY E O   1 
ATOM   6071 N N   . VAL E 5 173 ? 24.263 -15.367 -65.907 1.00 24.17  ?  172 VAL E N   1 
ATOM   6072 C CA  . VAL E 5 173 ? 23.764 -16.348 -64.954 1.00 26.24  ?  172 VAL E CA  1 
ATOM   6073 C C   . VAL E 5 173 ? 22.447 -15.866 -64.386 1.00 26.45  ?  172 VAL E C   1 
ATOM   6074 O O   . VAL E 5 173 ? 22.288 -14.670 -64.106 1.00 29.47  ?  172 VAL E O   1 
ATOM   6075 C CB  . VAL E 5 173 ? 24.763 -16.597 -63.814 1.00 26.03  ?  172 VAL E CB  1 
ATOM   6076 C CG1 . VAL E 5 173 ? 24.114 -17.507 -62.746 1.00 24.32  ?  172 VAL E CG1 1 
ATOM   6077 C CG2 . VAL E 5 173 ? 26.055 -17.159 -64.384 1.00 24.86  ?  172 VAL E CG2 1 
ATOM   6078 N N   . CYS E 5 174 ? 21.521 -16.798 -64.168 1.00 25.13  ?  173 CYS E N   1 
ATOM   6079 C CA  . CYS E 5 174 ? 20.360 -16.579 -63.316 1.00 28.68  ?  173 CYS E CA  1 
ATOM   6080 C C   . CYS E 5 174 ? 20.110 -17.854 -62.527 1.00 29.24  ?  173 CYS E C   1 
ATOM   6081 O O   . CYS E 5 174 ? 19.996 -18.935 -63.118 1.00 30.76  ?  173 CYS E O   1 
ATOM   6082 C CB  . CYS E 5 174 ? 19.132 -16.189 -64.163 1.00 35.08  ?  173 CYS E CB  1 
ATOM   6083 S SG  . CYS E 5 174 ? 17.859 -15.406 -63.210 1.00 49.88  ?  173 CYS E SG  1 
ATOM   6084 N N   . THR E 5 175 ? 20.031 -17.751 -61.203 1.00 27.71  ?  174 THR E N   1 
ATOM   6085 C CA  . THR E 5 175 ? 19.792 -18.894 -60.327 1.00 25.67  ?  174 THR E CA  1 
ATOM   6086 C C   . THR E 5 175 ? 18.448 -18.694 -59.636 1.00 29.71  ?  174 THR E C   1 
ATOM   6087 O O   . THR E 5 175 ? 18.123 -17.571 -59.260 1.00 30.54  ?  174 THR E O   1 
ATOM   6088 C CB  . THR E 5 175 ? 20.913 -18.988 -59.282 1.00 24.71  ?  174 THR E CB  1 
ATOM   6089 O OG1 . THR E 5 175 ? 22.155 -19.272 -59.932 1.00 24.38  ?  174 THR E OG1 1 
ATOM   6090 C CG2 . THR E 5 175 ? 20.609 -20.024 -58.184 1.00 26.93  ?  174 THR E CG2 1 
ATOM   6091 N N   . ASP E 5 176 ? 17.672 -19.761 -59.442 1.00 26.56  ?  175 ASP E N   1 
ATOM   6092 C CA  . ASP E 5 176 ? 16.404 -19.603 -58.728 1.00 30.77  ?  175 ASP E CA  1 
ATOM   6093 C C   . ASP E 5 176 ? 16.637 -18.915 -57.383 1.00 34.43  ?  175 ASP E C   1 
ATOM   6094 O O   . ASP E 5 176 ? 17.543 -19.303 -56.642 1.00 31.11  ?  175 ASP E O   1 
ATOM   6095 C CB  . ASP E 5 176 ? 15.734 -20.948 -58.456 1.00 32.08  ?  175 ASP E CB  1 
ATOM   6096 C CG  . ASP E 5 176 ? 15.530 -21.768 -59.697 1.00 29.49  ?  175 ASP E CG  1 
ATOM   6097 O OD1 . ASP E 5 176 ? 15.375 -21.192 -60.794 1.00 33.27  ?  175 ASP E OD1 1 
ATOM   6098 O OD2 . ASP E 5 176 ? 15.515 -23.003 -59.554 1.00 28.57  -1 175 ASP E OD2 1 
ATOM   6099 N N   . PRO E 5 177 ? 15.806 -17.941 -57.001 1.00 36.99  ?  176 PRO E N   1 
ATOM   6100 C CA  . PRO E 5 177 ? 16.020 -17.272 -55.698 1.00 38.42  ?  176 PRO E CA  1 
ATOM   6101 C C   . PRO E 5 177 ? 15.759 -18.167 -54.492 1.00 41.57  ?  176 PRO E C   1 
ATOM   6102 O O   . PRO E 5 177 ? 16.283 -17.869 -53.413 1.00 48.33  ?  176 PRO E O   1 
ATOM   6103 C CB  . PRO E 5 177 ? 15.057 -16.078 -55.743 1.00 35.87  ?  176 PRO E CB  1 
ATOM   6104 C CG  . PRO E 5 177 ? 14.004 -16.468 -56.740 1.00 42.17  ?  176 PRO E CG  1 
ATOM   6105 C CD  . PRO E 5 177 ? 14.617 -17.444 -57.716 1.00 35.72  ?  176 PRO E CD  1 
ATOM   6106 N N   . GLN E 5 178 ? 15.000 -19.261 -54.636 1.00 40.41  ?  177 GLN E N   1 
ATOM   6107 C CA  . GLN E 5 178 ? 14.787 -20.246 -53.559 1.00 44.83  ?  177 GLN E CA  1 
ATOM   6108 C C   . GLN E 5 178 ? 14.660 -21.668 -54.099 1.00 37.21  ?  177 GLN E C   1 
ATOM   6109 O O   . GLN E 5 178 ? 14.071 -21.866 -55.169 1.00 34.49  ?  177 GLN E O   1 
ATOM   6110 C CB  . GLN E 5 178 ? 13.537 -19.910 -52.741 1.00 48.28  ?  177 GLN E CB  1 
ATOM   6111 C CG  . GLN E 5 178 ? 13.725 -18.776 -51.733 1.00 53.59  ?  177 GLN E CG  1 
ATOM   6112 C CD  . GLN E 5 178 ? 12.453 -17.978 -51.536 1.00 69.22  ?  177 GLN E CD  1 
ATOM   6113 O OE1 . GLN E 5 178 ? 11.350 -18.517 -51.669 1.00 75.77  ?  177 GLN E OE1 1 
ATOM   6114 N NE2 . GLN E 5 178 ? 12.594 -16.685 -51.227 1.00 68.31  ?  177 GLN E NE2 1 
ATOM   6115 N N   . PRO E 5 179 ? 15.197 -22.660 -53.407 1.00 42.57  ?  178 PRO E N   1 
ATOM   6116 C CA  . PRO E 5 179 ? 15.007 -24.047 -53.845 1.00 39.11  ?  178 PRO E CA  1 
ATOM   6117 C C   . PRO E 5 179 ? 13.556 -24.447 -53.694 1.00 42.01  ?  178 PRO E C   1 
ATOM   6118 O O   . PRO E 5 179 ? 12.839 -23.919 -52.847 1.00 48.84  ?  178 PRO E O   1 
ATOM   6119 C CB  . PRO E 5 179 ? 15.896 -24.844 -52.887 1.00 34.92  ?  178 PRO E CB  1 
ATOM   6120 C CG  . PRO E 5 179 ? 16.927 -23.822 -52.397 1.00 41.95  ?  178 PRO E CG  1 
ATOM   6121 C CD  . PRO E 5 179 ? 16.134 -22.562 -52.274 1.00 43.40  ?  178 PRO E CD  1 
ATOM   6122 N N   . LEU E 5 180 ? 13.117 -25.396 -54.511 1.00 38.05  ?  179 LEU E N   1 
ATOM   6123 C CA  . LEU E 5 180 ? 11.753 -25.877 -54.378 1.00 33.88  ?  179 LEU E CA  1 
ATOM   6124 C C   . LEU E 5 180 ? 11.724 -27.259 -53.733 1.00 33.29  ?  179 LEU E C   1 
ATOM   6125 O O   . LEU E 5 180 ? 12.708 -28.012 -53.758 1.00 31.38  ?  179 LEU E O   1 
ATOM   6126 C CB  . LEU E 5 180 ? 11.030 -25.875 -55.728 1.00 37.35  ?  179 LEU E CB  1 
ATOM   6127 C CG  . LEU E 5 180 ? 11.599 -26.615 -56.925 1.00 38.51  ?  179 LEU E CG  1 
ATOM   6128 C CD1 . LEU E 5 180 ? 11.215 -28.072 -56.783 1.00 39.51  ?  179 LEU E CD1 1 
ATOM   6129 C CD2 . LEU E 5 180 ? 11.062 -26.028 -58.229 1.00 32.03  ?  179 LEU E CD2 1 
ATOM   6130 N N   . LYS E 5 181 ? 10.596 -27.566 -53.097 1.00 30.98  ?  180 LYS E N   1 
ATOM   6131 C CA  . LYS E 5 181 ? 10.466 -28.837 -52.401 1.00 32.94  ?  180 LYS E CA  1 
ATOM   6132 C C   . LYS E 5 181 ? 10.172 -29.925 -53.411 1.00 33.55  ?  180 LYS E C   1 
ATOM   6133 O O   . LYS E 5 181 ? 9.350  -29.741 -54.310 1.00 31.06  ?  180 LYS E O   1 
ATOM   6134 C CB  . LYS E 5 181 ? 9.367  -28.772 -51.340 1.00 37.81  ?  180 LYS E CB  1 
ATOM   6135 C CG  . LYS E 5 181 ? 9.766  -27.937 -50.147 1.00 36.94  ?  180 LYS E CG  1 
ATOM   6136 C CD  . LYS E 5 181 ? 8.619  -27.789 -49.179 1.00 39.34  ?  180 LYS E CD  1 
ATOM   6137 C CE  . LYS E 5 181 ? 9.087  -27.104 -47.900 1.00 43.83  ?  180 LYS E CE  1 
ATOM   6138 N NZ  . LYS E 5 181 ? 8.789  -27.994 -46.746 1.00 44.79  ?  180 LYS E NZ  1 
ATOM   6139 N N   . GLU E 5 182 ? 10.886 -31.035 -53.296 1.00 29.11  ?  181 GLU E N   1 
ATOM   6140 C CA  . GLU E 5 182 ? 10.617 -32.167 -54.169 1.00 31.85  ?  181 GLU E CA  1 
ATOM   6141 C C   . GLU E 5 182 ? 9.344  -32.908 -53.755 1.00 37.90  ?  181 GLU E C   1 
ATOM   6142 O O   . GLU E 5 182 ? 8.703  -33.550 -54.593 1.00 39.53  ?  181 GLU E O   1 
ATOM   6143 C CB  . GLU E 5 182 ? 11.835 -33.090 -54.170 1.00 29.85  ?  181 GLU E CB  1 
ATOM   6144 C CG  . GLU E 5 182 ? 13.035 -32.457 -54.892 1.00 32.77  ?  181 GLU E CG  1 
ATOM   6145 C CD  . GLU E 5 182 ? 14.231 -33.382 -55.007 1.00 31.57  ?  181 GLU E CD  1 
ATOM   6146 O OE1 . GLU E 5 182 ? 14.342 -34.332 -54.189 1.00 33.15  ?  181 GLU E OE1 1 
ATOM   6147 O OE2 . GLU E 5 182 ? 15.063 -33.158 -55.925 1.00 32.01  -1 181 GLU E OE2 1 
ATOM   6148 N N   . GLN E 5 183 ? 8.957  -32.834 -52.478 1.00 37.08  ?  182 GLN E N   1 
ATOM   6149 C CA  . GLN E 5 183 ? 7.701  -33.414 -51.993 1.00 34.94  ?  182 GLN E CA  1 
ATOM   6150 C C   . GLN E 5 183 ? 7.006  -32.379 -51.121 1.00 35.79  ?  182 GLN E C   1 
ATOM   6151 O O   . GLN E 5 183 ? 7.088  -32.426 -49.887 1.00 39.43  ?  182 GLN E O   1 
ATOM   6152 C CB  . GLN E 5 183 ? 7.943  -34.720 -51.235 1.00 37.76  ?  182 GLN E CB  1 
ATOM   6153 C CG  . GLN E 5 183 ? 8.891  -35.690 -51.933 1.00 38.85  ?  182 GLN E CG  1 
ATOM   6154 C CD  . GLN E 5 183 ? 8.247  -36.440 -53.087 1.00 54.30  ?  182 GLN E CD  1 
ATOM   6155 O OE1 . GLN E 5 183 ? 7.091  -36.869 -52.995 1.00 58.09  ?  182 GLN E OE1 1 
ATOM   6156 N NE2 . GLN E 5 183 ? 8.998  -36.618 -54.183 1.00 55.94  ?  182 GLN E NE2 1 
ATOM   6157 N N   . PRO E 5 184 ? 6.288  -31.433 -51.735 1.00 37.08  ?  183 PRO E N   1 
ATOM   6158 C CA  . PRO E 5 184 ? 5.752  -30.291 -50.969 1.00 36.50  ?  183 PRO E CA  1 
ATOM   6159 C C   . PRO E 5 184 ? 4.817  -30.676 -49.847 1.00 41.80  ?  183 PRO E C   1 
ATOM   6160 O O   . PRO E 5 184 ? 4.496  -29.819 -49.020 1.00 42.63  ?  183 PRO E O   1 
ATOM   6161 C CB  . PRO E 5 184 ? 5.007  -29.465 -52.034 1.00 37.79  ?  183 PRO E CB  1 
ATOM   6162 C CG  . PRO E 5 184 ? 5.578  -29.925 -53.374 1.00 33.72  ?  183 PRO E CG  1 
ATOM   6163 C CD  . PRO E 5 184 ? 5.922  -31.376 -53.164 1.00 34.87  ?  183 PRO E CD  1 
ATOM   6164 N N   . ALA E 5 185 ? 4.334  -31.909 -49.810 1.00 42.37  ?  184 ALA E N   1 
ATOM   6165 C CA  . ALA E 5 185 ? 3.415  -32.299 -48.757 1.00 47.46  ?  184 ALA E CA  1 
ATOM   6166 C C   . ALA E 5 185 ? 4.143  -32.721 -47.494 1.00 50.47  ?  184 ALA E C   1 
ATOM   6167 O O   . ALA E 5 185 ? 3.525  -32.766 -46.424 1.00 51.52  ?  184 ALA E O   1 
ATOM   6168 C CB  . ALA E 5 185 ? 2.511  -33.431 -49.248 1.00 46.83  ?  184 ALA E CB  1 
ATOM   6169 N N   . LEU E 5 186 ? 5.438  -33.013 -47.586 1.00 50.31  ?  185 LEU E N   1 
ATOM   6170 C CA  . LEU E 5 186 ? 6.230  -33.461 -46.447 1.00 49.09  ?  185 LEU E CA  1 
ATOM   6171 C C   . LEU E 5 186 ? 6.968  -32.294 -45.797 1.00 50.67  ?  185 LEU E C   1 
ATOM   6172 O O   . LEU E 5 186 ? 7.526  -31.427 -46.478 1.00 50.21  ?  185 LEU E O   1 
ATOM   6173 C CB  . LEU E 5 186 ? 7.210  -34.545 -46.893 1.00 45.73  ?  185 LEU E CB  1 
ATOM   6174 C CG  . LEU E 5 186 ? 6.449  -35.543 -47.761 1.00 45.36  ?  185 LEU E CG  1 
ATOM   6175 C CD1 . LEU E 5 186 ? 7.346  -36.644 -48.320 1.00 47.63  ?  185 LEU E CD1 1 
ATOM   6176 C CD2 . LEU E 5 186 ? 5.330  -36.114 -46.904 1.00 47.65  ?  185 LEU E CD2 1 
ATOM   6177 N N   . ASN E 5 187 ? 6.953  -32.260 -44.466 1.00 54.60  ?  186 ASN E N   1 
ATOM   6178 C CA  . ASN E 5 187 ? 7.655  -31.180 -43.788 1.00 49.99  ?  186 ASN E CA  1 
ATOM   6179 C C   . ASN E 5 187 ? 9.164  -31.318 -43.950 1.00 50.31  ?  186 ASN E C   1 
ATOM   6180 O O   . ASN E 5 187 ? 9.875  -30.309 -43.989 1.00 50.26  ?  186 ASN E O   1 
ATOM   6181 C CB  . ASN E 5 187 ? 7.264  -31.141 -42.311 1.00 60.86  ?  186 ASN E CB  1 
ATOM   6182 C CG  . ASN E 5 187 ? 5.891  -30.524 -42.089 1.00 61.60  ?  186 ASN E CG  1 
ATOM   6183 O OD1 . ASN E 5 187 ? 4.918  -31.230 -41.801 1.00 64.55  ?  186 ASN E OD1 1 
ATOM   6184 N ND2 . ASN E 5 187 ? 5.802  -29.202 -42.237 1.00 60.26  ?  186 ASN E ND2 1 
ATOM   6185 N N   . ASP E 5 188 ? 9.667  -32.546 -44.068 1.00 44.48  ?  187 ASP E N   1 
ATOM   6186 C CA  . ASP E 5 188 ? 11.084 -32.798 -44.313 1.00 46.79  ?  187 ASP E CA  1 
ATOM   6187 C C   . ASP E 5 188 ? 11.370 -33.136 -45.780 1.00 44.49  ?  187 ASP E C   1 
ATOM   6188 O O   . ASP E 5 188 ? 12.265 -33.938 -46.096 1.00 32.92  ?  187 ASP E O   1 
ATOM   6189 C CB  . ASP E 5 188 ? 11.564 -33.900 -43.377 1.00 50.18  ?  187 ASP E CB  1 
ATOM   6190 C CG  . ASP E 5 188 ? 11.246 -33.587 -41.927 1.00 59.60  ?  187 ASP E CG  1 
ATOM   6191 O OD1 . ASP E 5 188 ? 11.128 -32.381 -41.587 1.00 59.30  -1 187 ASP E OD1 1 
ATOM   6192 O OD2 . ASP E 5 188 ? 11.105 -34.538 -41.130 1.00 72.06  ?  187 ASP E OD2 1 
ATOM   6193 N N   . SER E 5 189 ? 10.609 -32.539 -46.688 1.00 36.04  ?  188 SER E N   1 
ATOM   6194 C CA  . SER E 5 189 ? 10.887 -32.692 -48.105 1.00 41.29  ?  188 SER E CA  1 
ATOM   6195 C C   . SER E 5 189 ? 12.312 -32.256 -48.424 1.00 33.47  ?  188 SER E C   1 
ATOM   6196 O O   . SER E 5 189 ? 12.773 -31.198 -47.990 1.00 32.42  ?  188 SER E O   1 
ATOM   6197 C CB  . SER E 5 189 ? 9.890  -31.863 -48.919 1.00 37.31  ?  188 SER E CB  1 
ATOM   6198 O OG  . SER E 5 189 ? 10.270 -31.799 -50.274 1.00 34.50  ?  188 SER E OG  1 
ATOM   6199 N N   . ARG E 5 190 ? 12.995 -33.071 -49.203 1.00 31.82  ?  189 ARG E N   1 
ATOM   6200 C CA  . ARG E 5 190 ? 14.212 -32.612 -49.848 1.00 30.72  ?  189 ARG E CA  1 
ATOM   6201 C C   . ARG E 5 190 ? 13.891 -31.529 -50.870 1.00 28.10  ?  189 ARG E C   1 
ATOM   6202 O O   . ARG E 5 190 ? 12.736 -31.291 -51.230 1.00 27.00  ?  189 ARG E O   1 
ATOM   6203 C CB  . ARG E 5 190 ? 14.914 -33.782 -50.512 1.00 26.41  ?  189 ARG E CB  1 
ATOM   6204 C CG  . ARG E 5 190 ? 15.162 -34.911 -49.533 1.00 35.11  ?  189 ARG E CG  1 
ATOM   6205 C CD  . ARG E 5 190 ? 16.207 -35.768 -50.147 1.00 39.34  ?  189 ARG E CD  1 
ATOM   6206 N NE  . ARG E 5 190 ? 16.217 -37.111 -49.630 1.00 46.23  ?  189 ARG E NE  1 
ATOM   6207 C CZ  . ARG E 5 190 ? 17.038 -38.043 -50.099 1.00 48.97  ?  189 ARG E CZ  1 
ATOM   6208 N NH1 . ARG E 5 190 ? 16.998 -39.249 -49.578 1.00 46.62  ?  189 ARG E NH1 1 
ATOM   6209 N NH2 . ARG E 5 190 ? 17.916 -37.748 -51.076 1.00 42.20  ?  189 ARG E NH2 1 
ATOM   6210 N N   . TYR E 5 191 ? 14.952 -30.894 -51.367 1.00 28.17  ?  190 TYR E N   1 
ATOM   6211 C CA  . TYR E 5 191 ? 14.859 -29.707 -52.198 1.00 26.14  ?  190 TYR E CA  1 
ATOM   6212 C C   . TYR E 5 191 ? 15.579 -29.930 -53.520 1.00 25.99  ?  190 TYR E C   1 
ATOM   6213 O O   . TYR E 5 191 ? 16.371 -30.869 -53.667 1.00 26.00  ?  190 TYR E O   1 
ATOM   6214 C CB  . TYR E 5 191 ? 15.468 -28.496 -51.494 1.00 28.76  ?  190 TYR E CB  1 
ATOM   6215 C CG  . TYR E 5 191 ? 14.724 -28.065 -50.245 1.00 28.36  ?  190 TYR E CG  1 
ATOM   6216 C CD1 . TYR E 5 191 ? 15.056 -28.589 -48.991 1.00 31.42  ?  190 TYR E CD1 1 
ATOM   6217 C CD2 . TYR E 5 191 ? 13.713 -27.119 -50.313 1.00 25.58  ?  190 TYR E CD2 1 
ATOM   6218 C CE1 . TYR E 5 191 ? 14.382 -28.178 -47.844 1.00 32.40  ?  190 TYR E CE1 1 
ATOM   6219 C CE2 . TYR E 5 191 ? 13.045 -26.703 -49.176 1.00 34.22  ?  190 TYR E CE2 1 
ATOM   6220 C CZ  . TYR E 5 191 ? 13.380 -27.235 -47.955 1.00 34.11  ?  190 TYR E CZ  1 
ATOM   6221 O OH  . TYR E 5 191 ? 12.697 -26.821 -46.846 1.00 36.59  ?  190 TYR E OH  1 
ATOM   6222 N N   . ALA E 5 192 ? 15.296 -29.041 -54.472 1.00 23.35  ?  191 ALA E N   1 
ATOM   6223 C CA  . ALA E 5 192 ? 16.014 -28.973 -55.737 1.00 24.45  ?  191 ALA E CA  1 
ATOM   6224 C C   . ALA E 5 192 ? 16.198 -27.506 -56.102 1.00 27.12  ?  191 ALA E C   1 
ATOM   6225 O O   . ALA E 5 192 ? 15.399 -26.652 -55.706 1.00 27.30  ?  191 ALA E O   1 
ATOM   6226 C CB  . ALA E 5 192 ? 15.273 -29.728 -56.858 1.00 25.37  ?  191 ALA E CB  1 
ATOM   6227 N N   . LEU E 5 193 ? 17.254 -27.221 -56.861 1.00 25.25  ?  192 LEU E N   1 
ATOM   6228 C CA  . LEU E 5 193 ? 17.606 -25.862 -57.253 1.00 26.78  ?  192 LEU E CA  1 
ATOM   6229 C C   . LEU E 5 193 ? 18.147 -25.885 -58.679 1.00 25.05  ?  192 LEU E C   1 
ATOM   6230 O O   . LEU E 5 193 ? 18.930 -26.774 -59.021 1.00 27.89  ?  192 LEU E O   1 
ATOM   6231 C CB  . LEU E 5 193 ? 18.667 -25.273 -56.274 1.00 27.14  ?  192 LEU E CB  1 
ATOM   6232 C CG  . LEU E 5 193 ? 19.101 -23.829 -56.575 1.00 33.83  ?  192 LEU E CG  1 
ATOM   6233 C CD1 . LEU E 5 193 ? 17.923 -22.873 -56.350 1.00 29.86  ?  192 LEU E CD1 1 
ATOM   6234 C CD2 . LEU E 5 193 ? 20.342 -23.388 -55.774 1.00 30.65  ?  192 LEU E CD2 1 
ATOM   6235 N N   . SER E 5 194 ? 17.738 -24.916 -59.514 1.00 25.64  ?  193 SER E N   1 
ATOM   6236 C CA  . SER E 5 194 ? 18.223 -24.839 -60.887 1.00 28.84  ?  193 SER E CA  1 
ATOM   6237 C C   . SER E 5 194 ? 18.884 -23.498 -61.149 1.00 26.41  ?  193 SER E C   1 
ATOM   6238 O O   . SER E 5 194 ? 18.588 -22.496 -60.497 1.00 27.75  ?  193 SER E O   1 
ATOM   6239 C CB  . SER E 5 194 ? 17.096 -25.052 -61.947 1.00 30.84  ?  193 SER E CB  1 
ATOM   6240 O OG  . SER E 5 194 ? 16.224 -23.941 -61.996 1.00 29.82  ?  193 SER E OG  1 
ATOM   6241 N N   . SER E 5 195 ? 19.793 -23.509 -62.118 1.00 25.97  ?  194 SER E N   1 
ATOM   6242 C CA  . SER E 5 195 ? 20.506 -22.315 -62.536 1.00 24.98  ?  194 SER E CA  1 
ATOM   6243 C C   . SER E 5 195 ? 20.799 -22.377 -64.020 1.00 25.21  ?  194 SER E C   1 
ATOM   6244 O O   . SER E 5 195 ? 21.103 -23.447 -64.560 1.00 28.07  ?  194 SER E O   1 
ATOM   6245 C CB  . SER E 5 195 ? 21.861 -22.135 -61.828 1.00 24.54  ?  194 SER E CB  1 
ATOM   6246 O OG  . SER E 5 195 ? 22.384 -20.844 -62.177 1.00 25.16  ?  194 SER E OG  1 
ATOM   6247 N N   . ARG E 5 196 ? 20.812 -21.203 -64.652 1.00 24.74  ?  195 ARG E N   1 
ATOM   6248 C CA  . ARG E 5 196 ? 21.179 -21.099 -66.064 1.00 26.67  ?  195 ARG E CA  1 
ATOM   6249 C C   . ARG E 5 196 ? 22.413 -20.228 -66.239 1.00 26.51  ?  195 ARG E C   1 
ATOM   6250 O O   . ARG E 5 196 ? 22.609 -19.227 -65.531 1.00 23.62  ?  195 ARG E O   1 
ATOM   6251 C CB  . ARG E 5 196 ? 20.048 -20.514 -66.945 1.00 24.63  ?  195 ARG E CB  1 
ATOM   6252 C CG  . ARG E 5 196 ? 18.659 -20.974 -66.543 1.00 30.95  ?  195 ARG E CG  1 
ATOM   6253 C CD  . ARG E 5 196 ? 18.037 -19.871 -65.714 1.00 31.33  ?  195 ARG E CD  1 
ATOM   6254 N NE  . ARG E 5 196 ? 16.653 -20.168 -65.392 1.00 36.10  ?  195 ARG E NE  1 
ATOM   6255 C CZ  . ARG E 5 196 ? 16.241 -20.565 -64.200 1.00 36.40  ?  195 ARG E CZ  1 
ATOM   6256 N NH1 . ARG E 5 196 ? 14.947 -20.817 -64.001 1.00 37.79  ?  195 ARG E NH1 1 
ATOM   6257 N NH2 . ARG E 5 196 ? 17.114 -20.688 -63.203 1.00 34.62  ?  195 ARG E NH2 1 
ATOM   6258 N N   . LEU E 5 197 ? 23.236 -20.623 -67.199 1.00 22.22  ?  196 LEU E N   1 
ATOM   6259 C CA  . LEU E 5 197 ? 24.357 -19.829 -67.657 1.00 24.28  ?  196 LEU E CA  1 
ATOM   6260 C C   . LEU E 5 197 ? 24.215 -19.767 -69.163 1.00 24.88  ?  196 LEU E C   1 
ATOM   6261 O O   . LEU E 5 197 ? 24.137 -20.810 -69.816 1.00 26.38  ?  196 LEU E O   1 
ATOM   6262 C CB  . LEU E 5 197 ? 25.704 -20.463 -67.268 1.00 20.45  ?  196 LEU E CB  1 
ATOM   6263 C CG  . LEU E 5 197 ? 26.853 -19.875 -68.096 1.00 24.54  ?  196 LEU E CG  1 
ATOM   6264 C CD1 . LEU E 5 197 ? 27.050 -18.359 -67.739 1.00 23.36  ?  196 LEU E CD1 1 
ATOM   6265 C CD2 . LEU E 5 197 ? 28.103 -20.672 -67.775 1.00 23.40  ?  196 LEU E CD2 1 
ATOM   6266 N N   . ARG E 5 198 ? 24.175 -18.572 -69.729 1.00 21.75  ?  197 ARG E N   1 
ATOM   6267 C CA  . ARG E 5 198 ? 24.038 -18.477 -71.172 1.00 24.22  ?  197 ARG E CA  1 
ATOM   6268 C C   . ARG E 5 198 ? 25.272 -17.822 -71.756 1.00 26.90  ?  197 ARG E C   1 
ATOM   6269 O O   . ARG E 5 198 ? 25.727 -16.780 -71.258 1.00 24.13  ?  197 ARG E O   1 
ATOM   6270 C CB  . ARG E 5 198 ? 22.776 -17.692 -71.554 1.00 29.07  ?  197 ARG E CB  1 
ATOM   6271 C CG  . ARG E 5 198 ? 22.393 -17.774 -73.007 1.00 23.78  ?  197 ARG E CG  1 
ATOM   6272 C CD  . ARG E 5 198 ? 21.019 -17.097 -73.232 1.00 27.79  ?  197 ARG E CD  1 
ATOM   6273 N NE  . ARG E 5 198 ? 20.306 -17.665 -74.383 1.00 27.59  ?  197 ARG E NE  1 
ATOM   6274 C CZ  . ARG E 5 198 ? 19.151 -17.207 -74.864 1.00 30.63  ?  197 ARG E CZ  1 
ATOM   6275 N NH1 . ARG E 5 198 ? 18.570 -16.138 -74.321 1.00 25.57  ?  197 ARG E NH1 1 
ATOM   6276 N NH2 . ARG E 5 198 ? 18.582 -17.827 -75.902 1.00 29.67  ?  197 ARG E NH2 1 
ATOM   6277 N N   . VAL E 5 199 ? 25.798 -18.422 -72.827 1.00 22.74  ?  198 VAL E N   1 
ATOM   6278 C CA  . VAL E 5 199 ? 26.963 -17.903 -73.525 1.00 24.69  ?  198 VAL E CA  1 
ATOM   6279 C C   . VAL E 5 199 ? 26.628 -17.838 -75.005 1.00 29.09  ?  198 VAL E C   1 
ATOM   6280 O O   . VAL E 5 199 ? 25.598 -18.341 -75.448 1.00 25.31  ?  198 VAL E O   1 
ATOM   6281 C CB  . VAL E 5 199 ? 28.231 -18.766 -73.288 1.00 27.95  ?  198 VAL E CB  1 
ATOM   6282 C CG1 . VAL E 5 199 ? 28.523 -18.871 -71.789 1.00 23.35  ?  198 VAL E CG1 1 
ATOM   6283 C CG2 . VAL E 5 199 ? 28.085 -20.180 -73.899 1.00 25.97  ?  198 VAL E CG2 1 
ATOM   6284 N N   . SER E 5 200 ? 27.516 -17.209 -75.771 1.00 25.31  ?  199 SER E N   1 
ATOM   6285 C CA  . SER E 5 200 ? 27.358 -17.184 -77.209 1.00 28.18  ?  199 SER E CA  1 
ATOM   6286 C C   . SER E 5 200 ? 27.610 -18.580 -77.780 1.00 32.38  ?  199 SER E C   1 
ATOM   6287 O O   . SER E 5 200 ? 28.324 -19.398 -77.186 1.00 25.36  ?  199 SER E O   1 
ATOM   6288 C CB  . SER E 5 200 ? 28.319 -16.160 -77.809 1.00 31.24  ?  199 SER E CB  1 
ATOM   6289 O OG  . SER E 5 200 ? 29.646 -16.667 -77.855 1.00 34.40  ?  199 SER E OG  1 
ATOM   6290 N N   . ALA E 5 201 ? 26.999 -18.866 -78.937 1.00 28.22  ?  200 ALA E N   1 
ATOM   6291 C CA  . ALA E 5 201 ? 27.183 -20.192 -79.532 1.00 31.36  ?  200 ALA E CA  1 
ATOM   6292 C C   . ALA E 5 201 ? 28.652 -20.448 -79.831 1.00 27.18  ?  200 ALA E C   1 
ATOM   6293 O O   . ALA E 5 201 ? 29.137 -21.571 -79.651 1.00 28.59  ?  200 ALA E O   1 
ATOM   6294 C CB  . ALA E 5 201 ? 26.344 -20.356 -80.808 1.00 32.66  ?  200 ALA E CB  1 
ATOM   6295 N N   . THR E 5 202 ? 29.376 -19.415 -80.288 1.00 27.52  ?  201 THR E N   1 
ATOM   6296 C CA  . THR E 5 202 ? 30.797 -19.586 -80.595 1.00 29.62  ?  201 THR E CA  1 
ATOM   6297 C C   . THR E 5 202 ? 31.594 -19.898 -79.337 1.00 26.81  ?  201 THR E C   1 
ATOM   6298 O O   . THR E 5 202 ? 32.531 -20.703 -79.380 1.00 28.15  ?  201 THR E O   1 
ATOM   6299 C CB  . THR E 5 202 ? 31.371 -18.348 -81.299 1.00 31.40  ?  201 THR E CB  1 
ATOM   6300 O OG1 . THR E 5 202 ? 31.112 -17.170 -80.530 1.00 38.92  ?  201 THR E OG1 1 
ATOM   6301 C CG2 . THR E 5 202 ? 30.727 -18.176 -82.663 1.00 40.94  ?  201 THR E CG2 1 
ATOM   6302 N N   . PHE E 5 203 ? 31.235 -19.292 -78.202 1.00 29.64  ?  202 PHE E N   1 
ATOM   6303 C CA  . PHE E 5 203 ? 31.920 -19.662 -76.965 1.00 29.21  ?  202 PHE E CA  1 
ATOM   6304 C C   . PHE E 5 203 ? 31.634 -21.118 -76.611 1.00 24.69  ?  202 PHE E C   1 
ATOM   6305 O O   . PHE E 5 203 ? 32.551 -21.879 -76.276 1.00 26.18  ?  202 PHE E O   1 
ATOM   6306 C CB  . PHE E 5 203 ? 31.506 -18.732 -75.816 1.00 24.47  ?  202 PHE E CB  1 
ATOM   6307 C CG  . PHE E 5 203 ? 32.411 -18.821 -74.602 1.00 26.03  ?  202 PHE E CG  1 
ATOM   6308 C CD1 . PHE E 5 203 ? 33.544 -18.012 -74.504 1.00 27.93  ?  202 PHE E CD1 1 
ATOM   6309 C CD2 . PHE E 5 203 ? 32.108 -19.691 -73.534 1.00 23.08  ?  202 PHE E CD2 1 
ATOM   6310 C CE1 . PHE E 5 203 ? 34.380 -18.063 -73.371 1.00 27.86  ?  202 PHE E CE1 1 
ATOM   6311 C CE2 . PHE E 5 203 ? 32.943 -19.765 -72.392 1.00 20.66  ?  202 PHE E CE2 1 
ATOM   6312 C CZ  . PHE E 5 203 ? 34.073 -18.953 -72.302 1.00 26.98  ?  202 PHE E CZ  1 
ATOM   6313 N N   . TRP E 5 204 ? 30.376 -21.545 -76.726 1.00 28.66  ?  203 TRP E N   1 
ATOM   6314 C CA  . TRP E 5 204 ? 30.081 -22.954 -76.465 1.00 30.72  ?  203 TRP E CA  1 
ATOM   6315 C C   . TRP E 5 204 ? 30.802 -23.879 -77.445 1.00 28.85  ?  203 TRP E C   1 
ATOM   6316 O O   . TRP E 5 204 ? 31.112 -25.022 -77.098 1.00 31.17  ?  203 TRP E O   1 
ATOM   6317 C CB  . TRP E 5 204 ? 28.558 -23.226 -76.494 1.00 25.94  ?  203 TRP E CB  1 
ATOM   6318 C CG  . TRP E 5 204 ? 28.280 -24.717 -76.462 1.00 32.01  ?  203 TRP E CG  1 
ATOM   6319 C CD1 . TRP E 5 204 ? 27.868 -25.487 -77.518 1.00 33.04  ?  203 TRP E CD1 1 
ATOM   6320 C CD2 . TRP E 5 204 ? 28.457 -25.626 -75.352 1.00 29.46  ?  203 TRP E CD2 1 
ATOM   6321 N NE1 . TRP E 5 204 ? 27.771 -26.806 -77.138 1.00 30.11  ?  203 TRP E NE1 1 
ATOM   6322 C CE2 . TRP E 5 204 ? 28.121 -26.922 -75.815 1.00 32.96  ?  203 TRP E CE2 1 
ATOM   6323 C CE3 . TRP E 5 204 ? 28.879 -25.474 -74.027 1.00 28.08  ?  203 TRP E CE3 1 
ATOM   6324 C CZ2 . TRP E 5 204 ? 28.178 -28.056 -74.990 1.00 32.30  ?  203 TRP E CZ2 1 
ATOM   6325 C CZ3 . TRP E 5 204 ? 28.941 -26.597 -73.210 1.00 26.24  ?  203 TRP E CZ3 1 
ATOM   6326 C CH2 . TRP E 5 204 ? 28.589 -27.872 -73.690 1.00 29.28  ?  203 TRP E CH2 1 
ATOM   6327 N N   . GLN E 5 205 ? 31.125 -23.412 -78.635 1.00 26.69  ?  204 GLN E N   1 
ATOM   6328 C CA  . GLN E 5 205 ? 31.632 -24.311 -79.666 1.00 33.49  ?  204 GLN E CA  1 
ATOM   6329 C C   . GLN E 5 205 ? 33.142 -24.479 -79.611 1.00 31.10  ?  204 GLN E C   1 
ATOM   6330 O O   . GLN E 5 205 ? 33.690 -25.274 -80.384 1.00 26.37  ?  204 GLN E O   1 
ATOM   6331 C CB  . GLN E 5 205 ? 31.202 -23.810 -81.057 1.00 34.23  ?  204 GLN E CB  1 
ATOM   6332 C CG  . GLN E 5 205 ? 29.719 -23.996 -81.314 1.00 33.43  ?  204 GLN E CG  1 
ATOM   6333 C CD  . GLN E 5 205 ? 29.203 -23.165 -82.498 1.00 43.40  ?  204 GLN E CD  1 
ATOM   6334 O OE1 . GLN E 5 205 ? 29.892 -22.272 -83.019 1.00 32.73  ?  204 GLN E OE1 1 
ATOM   6335 N NE2 . GLN E 5 205 ? 27.984 -23.462 -82.922 1.00 39.33  ?  204 GLN E NE2 1 
ATOM   6336 N N   . ASN E 5 206 ? 33.824 -23.747 -78.715 1.00 27.61  ?  205 ASN E N   1 
ATOM   6337 C CA  . ASN E 5 206 ? 35.252 -23.905 -78.481 1.00 25.53  ?  205 ASN E CA  1 
ATOM   6338 C C   . ASN E 5 206 ? 35.474 -25.040 -77.483 1.00 31.51  ?  205 ASN E C   1 
ATOM   6339 O O   . ASN E 5 206 ? 35.090 -24.917 -76.311 1.00 30.71  ?  205 ASN E O   1 
ATOM   6340 C CB  . ASN E 5 206 ? 35.830 -22.590 -77.970 1.00 30.69  ?  205 ASN E CB  1 
ATOM   6341 C CG  . ASN E 5 206 ? 37.319 -22.636 -77.751 1.00 27.48  ?  205 ASN E CG  1 
ATOM   6342 O OD1 . ASN E 5 206 ? 37.970 -23.683 -77.871 1.00 23.91  ?  205 ASN E OD1 1 
ATOM   6343 N ND2 . ASN E 5 206 ? 37.878 -21.473 -77.419 1.00 27.96  ?  205 ASN E ND2 1 
ATOM   6344 N N   . PRO E 5 207 ? 36.062 -26.169 -77.905 1.00 31.88  ?  206 PRO E N   1 
ATOM   6345 C CA  . PRO E 5 207 ? 36.239 -27.290 -76.974 1.00 30.49  ?  206 PRO E CA  1 
ATOM   6346 C C   . PRO E 5 207 ? 37.282 -27.033 -75.895 1.00 28.94  ?  206 PRO E C   1 
ATOM   6347 O O   . PRO E 5 207 ? 37.410 -27.869 -75.000 1.00 33.05  ?  206 PRO E O   1 
ATOM   6348 C CB  . PRO E 5 207 ? 36.674 -28.437 -77.891 1.00 29.79  ?  206 PRO E CB  1 
ATOM   6349 C CG  . PRO E 5 207 ? 37.445 -27.758 -78.944 1.00 35.03  ?  206 PRO E CG  1 
ATOM   6350 C CD  . PRO E 5 207 ? 36.624 -26.491 -79.230 1.00 34.15  ?  206 PRO E CD  1 
ATOM   6351 N N   . ARG E 5 208 ? 38.046 -25.941 -75.968 1.00 28.08  ?  207 ARG E N   1 
ATOM   6352 C CA  . ARG E 5 208 ? 38.950 -25.585 -74.884 1.00 33.72  ?  207 ARG E CA  1 
ATOM   6353 C C   . ARG E 5 208 ? 38.220 -24.913 -73.721 1.00 33.37  ?  207 ARG E C   1 
ATOM   6354 O O   . ARG E 5 208 ? 38.813 -24.715 -72.657 1.00 30.90  ?  207 ARG E O   1 
ATOM   6355 C CB  . ARG E 5 208 ? 40.054 -24.660 -75.404 1.00 35.94  ?  207 ARG E CB  1 
ATOM   6356 C CG  . ARG E 5 208 ? 41.313 -25.356 -75.865 1.00 41.00  ?  207 ARG E CG  1 
ATOM   6357 C CD  . ARG E 5 208 ? 42.339 -24.307 -76.277 1.00 35.84  ?  207 ARG E CD  1 
ATOM   6358 N NE  . ARG E 5 208 ? 42.976 -24.657 -77.531 1.00 44.98  ?  207 ARG E NE  1 
ATOM   6359 C CZ  . ARG E 5 208 ? 43.251 -23.782 -78.499 1.00 45.07  ?  207 ARG E CZ  1 
ATOM   6360 N NH1 . ARG E 5 208 ? 42.945 -22.486 -78.361 1.00 41.43  ?  207 ARG E NH1 1 
ATOM   6361 N NH2 . ARG E 5 208 ? 43.835 -24.207 -79.610 1.00 47.68  ?  207 ARG E NH2 1 
ATOM   6362 N N   . ASN E 5 209 ? 36.950 -24.562 -73.880 1.00 29.74  ?  208 ASN E N   1 
ATOM   6363 C CA  . ASN E 5 209 ? 36.231 -23.909 -72.804 1.00 25.81  ?  208 ASN E CA  1 
ATOM   6364 C C   . ASN E 5 209 ? 35.636 -24.942 -71.866 1.00 25.83  ?  208 ASN E C   1 
ATOM   6365 O O   . ASN E 5 209 ? 34.998 -25.911 -72.313 1.00 21.50  ?  208 ASN E O   1 
ATOM   6366 C CB  . ASN E 5 209 ? 35.142 -22.999 -73.361 1.00 24.02  ?  208 ASN E CB  1 
ATOM   6367 C CG  . ASN E 5 209 ? 35.724 -21.739 -73.949 1.00 31.54  ?  208 ASN E CG  1 
ATOM   6368 O OD1 . ASN E 5 209 ? 36.743 -21.221 -73.441 1.00 23.79  ?  208 ASN E OD1 1 
ATOM   6369 N ND2 . ASN E 5 209 ? 35.117 -21.250 -75.048 1.00 24.18  ?  208 ASN E ND2 1 
ATOM   6370 N N   . HIS E 5 210 ? 35.809 -24.698 -70.566 1.00 26.58  ?  209 HIS E N   1 
ATOM   6371 C CA  . HIS E 5 210 ? 35.417 -25.605 -69.497 1.00 26.68  ?  209 HIS E CA  1 
ATOM   6372 C C   . HIS E 5 210 ? 34.346 -24.948 -68.636 1.00 23.25  ?  209 HIS E C   1 
ATOM   6373 O O   . HIS E 5 210 ? 34.480 -23.781 -68.246 1.00 23.82  ?  209 HIS E O   1 
ATOM   6374 C CB  . HIS E 5 210 ? 36.644 -25.988 -68.660 1.00 24.27  ?  209 HIS E CB  1 
ATOM   6375 C CG  . HIS E 5 210 ? 36.333 -26.912 -67.523 1.00 29.30  ?  209 HIS E CG  1 
ATOM   6376 N ND1 . HIS E 5 210 ? 36.227 -26.477 -66.217 1.00 26.96  ?  209 HIS E ND1 1 
ATOM   6377 C CD2 . HIS E 5 210 ? 36.110 -28.247 -67.495 1.00 30.23  ?  209 HIS E CD2 1 
ATOM   6378 C CE1 . HIS E 5 210 ? 35.939 -27.505 -65.436 1.00 29.81  ?  209 HIS E CE1 1 
ATOM   6379 N NE2 . HIS E 5 210 ? 35.860 -28.591 -66.186 1.00 31.79  ?  209 HIS E NE2 1 
ATOM   6380 N N   . PHE E 5 211 ? 33.275 -25.681 -68.353 1.00 21.96  ?  210 PHE E N   1 
ATOM   6381 C CA  . PHE E 5 211 ? 32.144 -25.163 -67.588 1.00 27.91  ?  210 PHE E CA  1 
ATOM   6382 C C   . PHE E 5 211 ? 31.962 -26.024 -66.347 1.00 25.51  ?  210 PHE E C   1 
ATOM   6383 O O   . PHE E 5 211 ? 31.980 -27.252 -66.436 1.00 25.27  ?  210 PHE E O   1 
ATOM   6384 C CB  . PHE E 5 211 ? 30.846 -25.139 -68.434 1.00 24.99  ?  210 PHE E CB  1 
ATOM   6385 C CG  . PHE E 5 211 ? 30.975 -24.364 -69.718 1.00 25.13  ?  210 PHE E CG  1 
ATOM   6386 C CD1 . PHE E 5 211 ? 31.530 -24.957 -70.851 1.00 23.11  ?  210 PHE E CD1 1 
ATOM   6387 C CD2 . PHE E 5 211 ? 30.554 -23.042 -69.795 1.00 24.96  ?  210 PHE E CD2 1 
ATOM   6388 C CE1 . PHE E 5 211 ? 31.645 -24.263 -72.042 1.00 20.97  ?  210 PHE E CE1 1 
ATOM   6389 C CE2 . PHE E 5 211 ? 30.687 -22.321 -70.982 1.00 24.66  ?  210 PHE E CE2 1 
ATOM   6390 C CZ  . PHE E 5 211 ? 31.225 -22.948 -72.112 1.00 22.91  ?  210 PHE E CZ  1 
ATOM   6391 N N   . ARG E 5 212 ? 31.834 -25.390 -65.186 1.00 24.77  ?  211 ARG E N   1 
ATOM   6392 C CA  . ARG E 5 212 ? 31.591 -26.156 -63.972 1.00 23.82  ?  211 ARG E CA  1 
ATOM   6393 C C   . ARG E 5 212 ? 30.510 -25.459 -63.162 1.00 23.23  ?  211 ARG E C   1 
ATOM   6394 O O   . ARG E 5 212 ? 30.559 -24.246 -62.949 1.00 23.47  ?  211 ARG E O   1 
ATOM   6395 C CB  . ARG E 5 212 ? 32.879 -26.338 -63.138 1.00 25.74  ?  211 ARG E CB  1 
ATOM   6396 C CG  . ARG E 5 212 ? 32.710 -27.143 -61.832 1.00 26.72  ?  211 ARG E CG  1 
ATOM   6397 C CD  . ARG E 5 212 ? 34.092 -27.547 -61.255 1.00 30.64  ?  211 ARG E CD  1 
ATOM   6398 N NE  . ARG E 5 212 ? 34.831 -26.350 -60.850 1.00 30.09  ?  211 ARG E NE  1 
ATOM   6399 C CZ  . ARG E 5 212 ? 34.660 -25.757 -59.677 1.00 32.52  ?  211 ARG E CZ  1 
ATOM   6400 N NH1 . ARG E 5 212 ? 33.794 -26.272 -58.808 1.00 30.02  ?  211 ARG E NH1 1 
ATOM   6401 N NH2 . ARG E 5 212 ? 35.341 -24.651 -59.373 1.00 34.96  ?  211 ARG E NH2 1 
ATOM   6402 N N   . CYS E 5 213 ? 29.510 -26.232 -62.767 1.00 23.66  ?  212 CYS E N   1 
ATOM   6403 C CA  . CYS E 5 213 ? 28.501 -25.809 -61.812 1.00 23.58  ?  212 CYS E CA  1 
ATOM   6404 C C   . CYS E 5 213 ? 28.871 -26.391 -60.449 1.00 25.22  ?  212 CYS E C   1 
ATOM   6405 O O   . CYS E 5 213 ? 29.048 -27.606 -60.325 1.00 23.78  ?  212 CYS E O   1 
ATOM   6406 C CB  . CYS E 5 213 ? 27.110 -26.321 -62.210 1.00 24.19  ?  212 CYS E CB  1 
ATOM   6407 S SG  . CYS E 5 213 ? 25.974 -25.901 -60.912 1.00 35.08  ?  212 CYS E SG  1 
ATOM   6408 N N   . GLN E 5 214 ? 28.985 -25.531 -59.436 1.00 23.55  ?  213 GLN E N   1 
ATOM   6409 C CA  . GLN E 5 214 ? 29.462 -25.908 -58.110 1.00 22.05  ?  213 GLN E CA  1 
ATOM   6410 C C   . GLN E 5 214 ? 28.361 -25.643 -57.101 1.00 25.85  ?  213 GLN E C   1 
ATOM   6411 O O   . GLN E 5 214 ? 27.810 -24.541 -57.066 1.00 22.87  ?  213 GLN E O   1 
ATOM   6412 C CB  . GLN E 5 214 ? 30.702 -25.101 -57.698 1.00 20.74  ?  213 GLN E CB  1 
ATOM   6413 C CG  . GLN E 5 214 ? 31.087 -25.358 -56.242 1.00 28.00  ?  213 GLN E CG  1 
ATOM   6414 C CD  . GLN E 5 214 ? 32.361 -24.634 -55.861 1.00 31.66  ?  213 GLN E CD  1 
ATOM   6415 O OE1 . GLN E 5 214 ? 33.435 -24.969 -56.355 1.00 36.16  ?  213 GLN E OE1 1 
ATOM   6416 N NE2 . GLN E 5 214 ? 32.240 -23.612 -55.010 1.00 26.38  ?  213 GLN E NE2 1 
ATOM   6417 N N   . VAL E 5 215 ? 28.061 -26.625 -56.262 1.00 22.21  ?  214 VAL E N   1 
ATOM   6418 C CA  . VAL E 5 215 ? 27.151 -26.406 -55.145 1.00 19.49  ?  214 VAL E CA  1 
ATOM   6419 C C   . VAL E 5 215 ? 27.917 -26.647 -53.840 1.00 24.07  ?  214 VAL E C   1 
ATOM   6420 O O   . VAL E 5 215 ? 28.339 -27.779 -53.553 1.00 21.49  ?  214 VAL E O   1 
ATOM   6421 C CB  . VAL E 5 215 ? 25.895 -27.290 -55.227 1.00 24.72  ?  214 VAL E CB  1 
ATOM   6422 C CG1 . VAL E 5 215 ? 24.929 -26.938 -54.069 1.00 21.42  ?  214 VAL E CG1 1 
ATOM   6423 C CG2 . VAL E 5 215 ? 25.171 -27.084 -56.610 1.00 25.39  ?  214 VAL E CG2 1 
ATOM   6424 N N   . GLN E 5 216 ? 28.074 -25.585 -53.048 1.00 22.38  ?  215 GLN E N   1 
ATOM   6425 C CA  . GLN E 5 216 ? 28.513 -25.710 -51.659 1.00 22.25  ?  215 GLN E CA  1 
ATOM   6426 C C   . GLN E 5 216 ? 27.322 -26.094 -50.796 1.00 25.16  ?  215 GLN E C   1 
ATOM   6427 O O   . GLN E 5 216 ? 26.333 -25.356 -50.714 1.00 24.12  ?  215 GLN E O   1 
ATOM   6428 C CB  . GLN E 5 216 ? 29.131 -24.402 -51.172 1.00 24.69  ?  215 GLN E CB  1 
ATOM   6429 C CG  . GLN E 5 216 ? 29.469 -24.421 -49.678 1.00 24.79  ?  215 GLN E CG  1 
ATOM   6430 C CD  . GLN E 5 216 ? 30.769 -25.172 -49.416 1.00 24.53  ?  215 GLN E CD  1 
ATOM   6431 O OE1 . GLN E 5 216 ? 31.846 -24.684 -49.748 1.00 23.90  ?  215 GLN E OE1 1 
ATOM   6432 N NE2 . GLN E 5 216 ? 30.668 -26.369 -48.854 1.00 21.33  ?  215 GLN E NE2 1 
ATOM   6433 N N   . PHE E 5 217 ? 27.410 -27.250 -50.162 1.00 25.90  ?  216 PHE E N   1 
ATOM   6434 C CA  . PHE E 5 217 ? 26.382 -27.722 -49.251 1.00 22.96  ?  216 PHE E CA  1 
ATOM   6435 C C   . PHE E 5 217 ? 26.906 -27.539 -47.837 1.00 23.48  ?  216 PHE E C   1 
ATOM   6436 O O   . PHE E 5 217 ? 28.033 -27.951 -47.534 1.00 25.06  ?  216 PHE E O   1 
ATOM   6437 C CB  . PHE E 5 217 ? 26.048 -29.199 -49.494 1.00 20.75  ?  216 PHE E CB  1 
ATOM   6438 C CG  . PHE E 5 217 ? 25.110 -29.816 -48.455 1.00 28.01  ?  216 PHE E CG  1 
ATOM   6439 C CD1 . PHE E 5 217 ? 23.764 -29.462 -48.414 1.00 23.75  ?  216 PHE E CD1 1 
ATOM   6440 C CD2 . PHE E 5 217 ? 25.575 -30.777 -47.547 1.00 26.90  ?  216 PHE E CD2 1 
ATOM   6441 C CE1 . PHE E 5 217 ? 22.896 -30.032 -47.487 1.00 22.63  ?  216 PHE E CE1 1 
ATOM   6442 C CE2 . PHE E 5 217 ? 24.705 -31.387 -46.618 1.00 26.80  ?  216 PHE E CE2 1 
ATOM   6443 C CZ  . PHE E 5 217 ? 23.364 -31.007 -46.578 1.00 25.03  ?  216 PHE E CZ  1 
ATOM   6444 N N   . TYR E 5 218 ? 26.086 -26.953 -46.977 1.00 21.79  ?  217 TYR E N   1 
ATOM   6445 C CA  . TYR E 5 218 ? 26.435 -26.737 -45.571 1.00 27.78  ?  217 TYR E CA  1 
ATOM   6446 C C   . TYR E 5 218 ? 25.680 -27.799 -44.771 1.00 26.63  ?  217 TYR E C   1 
ATOM   6447 O O   . TYR E 5 218 ? 24.445 -27.774 -44.701 1.00 26.14  ?  217 TYR E O   1 
ATOM   6448 C CB  . TYR E 5 218 ? 26.091 -25.311 -45.121 1.00 25.54  ?  217 TYR E CB  1 
ATOM   6449 C CG  . TYR E 5 218 ? 26.879 -24.241 -45.854 1.00 28.26  ?  217 TYR E CG  1 
ATOM   6450 C CD1 . TYR E 5 218 ? 28.172 -23.900 -45.454 1.00 30.40  ?  217 TYR E CD1 1 
ATOM   6451 C CD2 . TYR E 5 218 ? 26.340 -23.569 -46.957 1.00 25.65  ?  217 TYR E CD2 1 
ATOM   6452 C CE1 . TYR E 5 218 ? 28.916 -22.936 -46.116 1.00 30.61  ?  217 TYR E CE1 1 
ATOM   6453 C CE2 . TYR E 5 218 ? 27.071 -22.613 -47.610 1.00 25.66  ?  217 TYR E CE2 1 
ATOM   6454 C CZ  . TYR E 5 218 ? 28.361 -22.292 -47.185 1.00 25.40  ?  217 TYR E CZ  1 
ATOM   6455 O OH  . TYR E 5 218 ? 29.129 -21.340 -47.838 1.00 27.18  ?  217 TYR E OH  1 
ATOM   6456 N N   . GLY E 5 219 ? 26.405 -28.783 -44.252 1.00 23.48  ?  218 GLY E N   1 
ATOM   6457 C CA  . GLY E 5 219 ? 25.766 -29.904 -43.583 1.00 24.97  ?  218 GLY E CA  1 
ATOM   6458 C C   . GLY E 5 219 ? 26.379 -30.135 -42.216 1.00 27.88  ?  218 GLY E C   1 
ATOM   6459 O O   . GLY E 5 219 ? 26.675 -29.198 -41.480 1.00 28.61  ?  218 GLY E O   1 
ATOM   6460 N N   . LEU E 5 220 ? 26.562 -31.410 -41.871 1.00 30.34  ?  219 LEU E N   1 
ATOM   6461 C CA  . LEU E 5 220 ? 27.068 -31.719 -40.534 1.00 29.91  ?  219 LEU E CA  1 
ATOM   6462 C C   . LEU E 5 220 ? 28.547 -31.363 -40.424 1.00 31.93  ?  219 LEU E C   1 
ATOM   6463 O O   . LEU E 5 220 ? 29.255 -31.119 -41.414 1.00 28.30  ?  219 LEU E O   1 
ATOM   6464 C CB  . LEU E 5 220 ? 26.868 -33.194 -40.186 1.00 29.01  ?  219 LEU E CB  1 
ATOM   6465 C CG  . LEU E 5 220 ? 25.460 -33.795 -40.302 1.00 37.88  ?  219 LEU E CG  1 
ATOM   6466 C CD1 . LEU E 5 220 ? 25.378 -35.011 -39.411 1.00 30.58  ?  219 LEU E CD1 1 
ATOM   6467 C CD2 . LEU E 5 220 ? 24.331 -32.814 -39.984 1.00 29.32  ?  219 LEU E CD2 1 
ATOM   6468 N N   . SER E 5 221 ? 29.014 -31.294 -39.196 1.00 29.95  ?  220 SER E N   1 
ATOM   6469 C CA  . SER E 5 221 ? 30.430 -31.075 -38.994 1.00 32.70  ?  220 SER E CA  1 
ATOM   6470 C C   . SER E 5 221 ? 31.095 -32.390 -38.613 1.00 35.28  ?  220 SER E C   1 
ATOM   6471 O O   . SER E 5 221 ? 30.442 -33.399 -38.328 1.00 29.61  ?  220 SER E O   1 
ATOM   6472 C CB  . SER E 5 221 ? 30.659 -30.008 -37.925 1.00 34.66  ?  220 SER E CB  1 
ATOM   6473 O OG  . SER E 5 221 ? 30.435 -30.598 -36.663 1.00 37.32  ?  220 SER E OG  1 
ATOM   6474 N N   . GLU E 5 222 ? 32.426 -32.365 -38.617 1.00 33.61  ?  221 GLU E N   1 
ATOM   6475 C CA  . GLU E 5 222 ? 33.182 -33.539 -38.207 1.00 34.85  ?  221 GLU E CA  1 
ATOM   6476 C C   . GLU E 5 222 ? 32.734 -34.053 -36.838 1.00 39.89  ?  221 GLU E C   1 
ATOM   6477 O O   . GLU E 5 222 ? 32.693 -35.264 -36.608 1.00 39.91  ?  221 GLU E O   1 
ATOM   6478 C CB  . GLU E 5 222 ? 34.676 -33.219 -38.199 1.00 38.34  ?  221 GLU E CB  1 
ATOM   6479 C CG  . GLU E 5 222 ? 35.569 -34.437 -37.986 1.00 46.44  ?  221 GLU E CG  1 
ATOM   6480 C CD  . GLU E 5 222 ? 37.048 -34.125 -38.246 1.00 52.76  ?  221 GLU E CD  1 
ATOM   6481 O OE1 . GLU E 5 222 ? 37.782 -33.791 -37.274 1.00 50.97  ?  221 GLU E OE1 1 
ATOM   6482 O OE2 . GLU E 5 222 ? 37.458 -34.186 -39.429 1.00 48.65  -1 221 GLU E OE2 1 
ATOM   6483 N N   . ASN E 5 223 ? 32.390 -33.163 -35.916 1.00 31.93  ?  222 ASN E N   1 
ATOM   6484 C CA  . ASN E 5 223 ? 32.119 -33.634 -34.567 1.00 41.65  ?  222 ASN E CA  1 
ATOM   6485 C C   . ASN E 5 223 ? 30.649 -33.965 -34.330 1.00 39.05  ?  222 ASN E C   1 
ATOM   6486 O O   . ASN E 5 223 ? 30.302 -34.373 -33.230 1.00 36.47  ?  222 ASN E O   1 
ATOM   6487 C CB  . ASN E 5 223 ? 32.625 -32.614 -33.531 1.00 39.30  ?  222 ASN E CB  1 
ATOM   6488 C CG  . ASN E 5 223 ? 31.724 -31.424 -33.404 1.00 43.12  ?  222 ASN E CG  1 
ATOM   6489 O OD1 . ASN E 5 223 ? 30.998 -31.102 -34.339 1.00 45.81  ?  222 ASN E OD1 1 
ATOM   6490 N ND2 . ASN E 5 223 ? 31.751 -30.757 -32.245 1.00 43.46  ?  222 ASN E ND2 1 
ATOM   6491 N N   . ASP E 5 224 ? 29.785 -33.840 -35.332 1.00 36.98  ?  223 ASP E N   1 
ATOM   6492 C CA  . ASP E 5 224 ? 28.426 -34.345 -35.191 1.00 34.83  ?  223 ASP E CA  1 
ATOM   6493 C C   . ASP E 5 224 ? 28.405 -35.873 -35.137 1.00 39.59  ?  223 ASP E C   1 
ATOM   6494 O O   . ASP E 5 224 ? 29.117 -36.559 -35.885 1.00 39.73  ?  223 ASP E O   1 
ATOM   6495 C CB  . ASP E 5 224 ? 27.554 -33.868 -36.356 1.00 33.03  ?  223 ASP E CB  1 
ATOM   6496 C CG  . ASP E 5 224 ? 27.106 -32.405 -36.201 1.00 36.92  ?  223 ASP E CG  1 
ATOM   6497 O OD1 . ASP E 5 224 ? 26.671 -32.031 -35.096 1.00 31.78  ?  223 ASP E OD1 1 
ATOM   6498 O OD2 . ASP E 5 224 ? 27.203 -31.632 -37.187 1.00 32.47  -1 223 ASP E OD2 1 
ATOM   6499 N N   . GLU E 5 225 ? 27.545 -36.405 -34.280 1.00 39.75  ?  224 GLU E N   1 
ATOM   6500 C CA  . GLU E 5 225 ? 27.338 -37.847 -34.238 1.00 42.90  ?  224 GLU E CA  1 
ATOM   6501 C C   . GLU E 5 225 ? 26.653 -38.324 -35.511 1.00 37.87  ?  224 GLU E C   1 
ATOM   6502 O O   . GLU E 5 225 ? 25.759 -37.659 -36.031 1.00 41.69  ?  224 GLU E O   1 
ATOM   6503 C CB  . GLU E 5 225 ? 26.468 -38.221 -33.037 1.00 45.35  ?  224 GLU E CB  1 
ATOM   6504 C CG  . GLU E 5 225 ? 27.066 -37.959 -31.674 1.00 59.82  ?  224 GLU E CG  1 
ATOM   6505 C CD  . GLU E 5 225 ? 25.991 -37.682 -30.586 1.00 73.99  ?  224 GLU E CD  1 
ATOM   6506 O OE1 . GLU E 5 225 ? 24.771 -37.659 -30.897 1.00 72.44  ?  224 GLU E OE1 1 
ATOM   6507 O OE2 . GLU E 5 225 ? 26.371 -37.478 -29.409 1.00 73.87  -1 224 GLU E OE2 1 
ATOM   6508 N N   . TRP E 5 226 ? 27.050 -39.504 -35.987 1.00 35.56  ?  225 TRP E N   1 
ATOM   6509 C CA  . TRP E 5 226 ? 26.429 -40.132 -37.148 1.00 43.47  ?  225 TRP E CA  1 
ATOM   6510 C C   . TRP E 5 226 ? 26.549 -41.644 -37.015 1.00 49.40  ?  225 TRP E C   1 
ATOM   6511 O O   . TRP E 5 226 ? 27.663 -42.170 -36.910 1.00 45.40  ?  225 TRP E O   1 
ATOM   6512 C CB  . TRP E 5 226 ? 27.088 -39.664 -38.449 1.00 40.78  ?  225 TRP E CB  1 
ATOM   6513 C CG  . TRP E 5 226 ? 26.317 -40.057 -39.675 1.00 35.62  ?  225 TRP E CG  1 
ATOM   6514 C CD1 . TRP E 5 226 ? 26.663 -41.010 -40.592 1.00 39.75  ?  225 TRP E CD1 1 
ATOM   6515 C CD2 . TRP E 5 226 ? 25.072 -39.502 -40.126 1.00 34.62  ?  225 TRP E CD2 1 
ATOM   6516 N NE1 . TRP E 5 226 ? 25.713 -41.083 -41.583 1.00 38.11  ?  225 TRP E NE1 1 
ATOM   6517 C CE2 . TRP E 5 226 ? 24.721 -40.175 -41.314 1.00 33.50  ?  225 TRP E CE2 1 
ATOM   6518 C CE3 . TRP E 5 226 ? 24.212 -38.515 -39.629 1.00 34.43  ?  225 TRP E CE3 1 
ATOM   6519 C CZ2 . TRP E 5 226 ? 23.555 -39.874 -42.030 1.00 40.92  ?  225 TRP E CZ2 1 
ATOM   6520 C CZ3 . TRP E 5 226 ? 23.058 -38.218 -40.329 1.00 34.68  ?  225 TRP E CZ3 1 
ATOM   6521 C CH2 . TRP E 5 226 ? 22.736 -38.898 -41.520 1.00 37.30  ?  225 TRP E CH2 1 
ATOM   6522 N N   . THR E 5 227 ? 25.412 -42.344 -37.054 1.00 49.53  ?  226 THR E N   1 
ATOM   6523 C CA  . THR E 5 227 ? 25.393 -43.795 -36.939 1.00 46.94  ?  226 THR E CA  1 
ATOM   6524 C C   . THR E 5 227 ? 24.791 -44.502 -38.144 1.00 55.84  ?  226 THR E C   1 
ATOM   6525 O O   . THR E 5 227 ? 24.879 -45.734 -38.220 1.00 60.28  ?  226 THR E O   1 
ATOM   6526 C CB  . THR E 5 227 ? 24.616 -44.226 -35.684 1.00 49.41  ?  226 THR E CB  1 
ATOM   6527 O OG1 . THR E 5 227 ? 23.248 -43.815 -35.815 1.00 51.20  ?  226 THR E OG1 1 
ATOM   6528 C CG2 . THR E 5 227 ? 25.225 -43.611 -34.413 1.00 41.39  ?  226 THR E CG2 1 
ATOM   6529 N N   . GLN E 5 228 ? 24.185 -43.781 -39.080 1.00 48.65  ?  227 GLN E N   1 
ATOM   6530 C CA  . GLN E 5 228 ? 23.580 -44.456 -40.214 1.00 52.73  ?  227 GLN E CA  1 
ATOM   6531 C C   . GLN E 5 228 ? 24.654 -45.034 -41.133 1.00 48.75  ?  227 GLN E C   1 
ATOM   6532 O O   . GLN E 5 228 ? 25.810 -44.602 -41.149 1.00 51.49  ?  227 GLN E O   1 
ATOM   6533 C CB  . GLN E 5 228 ? 22.661 -43.505 -40.991 1.00 46.48  ?  227 GLN E CB  1 
ATOM   6534 C CG  . GLN E 5 228 ? 21.859 -42.524 -40.125 1.00 55.18  ?  227 GLN E CG  1 
ATOM   6535 C CD  . GLN E 5 228 ? 20.740 -43.191 -39.339 1.00 56.84  ?  227 GLN E CD  1 
ATOM   6536 O OE1 . GLN E 5 228 ? 19.999 -44.013 -39.880 1.00 58.61  ?  227 GLN E OE1 1 
ATOM   6537 N NE2 . GLN E 5 228 ? 20.611 -42.832 -38.053 1.00 46.17  ?  227 GLN E NE2 1 
ATOM   6538 N N   . ASP E 5 229 ? 24.245 -46.045 -41.899 1.00 54.95  ?  228 ASP E N   1 
ATOM   6539 C CA  . ASP E 5 229 ? 25.130 -46.693 -42.864 1.00 51.01  ?  228 ASP E CA  1 
ATOM   6540 C C   . ASP E 5 229 ? 25.630 -45.713 -43.921 1.00 53.16  ?  228 ASP E C   1 
ATOM   6541 O O   . ASP E 5 229 ? 26.809 -45.744 -44.299 1.00 54.58  ?  228 ASP E O   1 
ATOM   6542 C CB  . ASP E 5 229 ? 24.399 -47.848 -43.567 1.00 58.24  ?  228 ASP E CB  1 
ATOM   6543 C CG  . ASP E 5 229 ? 24.057 -49.017 -42.642 1.00 59.03  ?  228 ASP E CG  1 
ATOM   6544 O OD1 . ASP E 5 229 ? 24.322 -48.951 -41.415 1.00 60.81  ?  228 ASP E OD1 1 
ATOM   6545 O OD2 . ASP E 5 229 ? 23.502 -50.015 -43.170 1.00 62.60  -1 228 ASP E OD2 1 
ATOM   6546 N N   . ARG E 5 230 ? 24.744 -44.879 -44.461 1.00 45.37  ?  229 ARG E N   1 
ATOM   6547 C CA  . ARG E 5 230 ? 25.161 -44.050 -45.581 1.00 44.60  ?  229 ARG E CA  1 
ATOM   6548 C C   . ARG E 5 230 ? 26.195 -43.022 -45.127 1.00 44.37  ?  229 ARG E C   1 
ATOM   6549 O O   . ARG E 5 230 ? 26.375 -42.761 -43.931 1.00 39.12  ?  229 ARG E O   1 
ATOM   6550 C CB  . ARG E 5 230 ? 23.961 -43.360 -46.235 1.00 42.48  ?  229 ARG E CB  1 
ATOM   6551 C CG  . ARG E 5 230 ? 23.306 -42.312 -45.366 1.00 44.70  ?  229 ARG E CG  1 
ATOM   6552 C CD  . ARG E 5 230 ? 22.235 -41.576 -46.141 1.00 46.76  ?  229 ARG E CD  1 
ATOM   6553 N NE  . ARG E 5 230 ? 21.291 -40.866 -45.278 1.00 51.27  ?  229 ARG E NE  1 
ATOM   6554 C CZ  . ARG E 5 230 ? 21.399 -39.578 -44.975 1.00 45.34  ?  229 ARG E CZ  1 
ATOM   6555 N NH1 . ARG E 5 230 ? 22.422 -38.892 -45.474 1.00 39.42  ?  229 ARG E NH1 1 
ATOM   6556 N NH2 . ARG E 5 230 ? 20.491 -38.980 -44.197 1.00 33.77  ?  229 ARG E NH2 1 
ATOM   6557 N N   . ALA E 5 231 ? 26.906 -42.461 -46.110 1.00 39.69  ?  230 ALA E N   1 
ATOM   6558 C CA  . ALA E 5 231 ? 27.974 -41.515 -45.818 1.00 38.79  ?  230 ALA E CA  1 
ATOM   6559 C C   . ALA E 5 231 ? 27.457 -40.359 -44.961 1.00 38.78  ?  230 ALA E C   1 
ATOM   6560 O O   . ALA E 5 231 ? 26.344 -39.863 -45.159 1.00 36.66  ?  230 ALA E O   1 
ATOM   6561 C CB  . ALA E 5 231 ? 28.572 -40.993 -47.126 1.00 34.44  ?  230 ALA E CB  1 
ATOM   6562 N N   . LYS E 5 232 ? 28.254 -39.954 -43.975 1.00 37.11  ?  231 LYS E N   1 
ATOM   6563 C CA  . LYS E 5 232 ? 27.869 -38.837 -43.121 1.00 35.98  ?  231 LYS E CA  1 
ATOM   6564 C C   . LYS E 5 232 ? 27.721 -37.559 -43.960 1.00 33.64  ?  231 LYS E C   1 
ATOM   6565 O O   . LYS E 5 232 ? 28.679 -37.156 -44.633 1.00 30.42  ?  231 LYS E O   1 
ATOM   6566 C CB  . LYS E 5 232 ? 28.910 -38.663 -42.031 1.00 33.46  ?  231 LYS E CB  1 
ATOM   6567 C CG  . LYS E 5 232 ? 28.642 -37.585 -40.978 1.00 32.73  ?  231 LYS E CG  1 
ATOM   6568 C CD  . LYS E 5 232 ? 29.888 -37.577 -40.040 1.00 32.60  ?  231 LYS E CD  1 
ATOM   6569 C CE  . LYS E 5 232 ? 29.760 -36.663 -38.828 1.00 38.85  ?  231 LYS E CE  1 
ATOM   6570 N NZ  . LYS E 5 232 ? 31.020 -36.683 -38.005 1.00 37.82  ?  231 LYS E NZ  1 
ATOM   6571 N N   . PRO E 5 233 ? 26.551 -36.916 -43.970 1.00 35.50  ?  232 PRO E N   1 
ATOM   6572 C CA  . PRO E 5 233 ? 26.312 -35.744 -44.879 1.00 27.54  ?  232 PRO E CA  1 
ATOM   6573 C C   . PRO E 5 233 ? 26.932 -34.457 -44.339 1.00 28.65  ?  232 PRO E C   1 
ATOM   6574 O O   . PRO E 5 233 ? 26.263 -33.515 -43.904 1.00 25.49  ?  232 PRO E O   1 
ATOM   6575 C CB  . PRO E 5 233 ? 24.783 -35.677 -44.939 1.00 29.91  ?  232 PRO E CB  1 
ATOM   6576 C CG  . PRO E 5 233 ? 24.333 -36.211 -43.550 1.00 33.24  ?  232 PRO E CG  1 
ATOM   6577 C CD  . PRO E 5 233 ? 25.357 -37.310 -43.194 1.00 29.44  ?  232 PRO E CD  1 
ATOM   6578 N N   . VAL E 5 234 ? 28.259 -34.424 -44.329 1.00 25.99  ?  233 VAL E N   1 
ATOM   6579 C CA  . VAL E 5 234 ? 29.022 -33.256 -43.908 1.00 26.10  ?  233 VAL E CA  1 
ATOM   6580 C C   . VAL E 5 234 ? 28.919 -32.109 -44.911 1.00 27.55  ?  233 VAL E C   1 
ATOM   6581 O O   . VAL E 5 234 ? 28.573 -32.290 -46.090 1.00 22.47  ?  233 VAL E O   1 
ATOM   6582 C CB  . VAL E 5 234 ? 30.503 -33.633 -43.718 1.00 33.88  ?  233 VAL E CB  1 
ATOM   6583 C CG1 . VAL E 5 234 ? 30.653 -34.740 -42.658 1.00 29.83  ?  233 VAL E CG1 1 
ATOM   6584 C CG2 . VAL E 5 234 ? 31.094 -34.094 -45.066 1.00 25.09  ?  233 VAL E CG2 1 
ATOM   6585 N N   . THR E 5 235 ? 29.275 -30.928 -44.446 1.00 25.01  ?  234 THR E N   1 
ATOM   6586 C CA  . THR E 5 235 ? 29.575 -29.811 -45.316 1.00 26.02  ?  234 THR E CA  1 
ATOM   6587 C C   . THR E 5 235 ? 30.556 -30.235 -46.409 1.00 28.88  ?  234 THR E C   1 
ATOM   6588 O O   . THR E 5 235 ? 31.581 -30.866 -46.132 1.00 27.81  ?  234 THR E O   1 
ATOM   6589 C CB  . THR E 5 235 ? 30.136 -28.689 -44.447 1.00 23.34  ?  234 THR E CB  1 
ATOM   6590 O OG1 . THR E 5 235 ? 29.063 -28.160 -43.663 1.00 23.20  ?  234 THR E OG1 1 
ATOM   6591 C CG2 . THR E 5 235 ? 30.758 -27.600 -45.275 1.00 20.55  ?  234 THR E CG2 1 
ATOM   6592 N N   . GLN E 5 236 ? 30.229 -29.904 -47.661 1.00 26.45  ?  235 GLN E N   1 
ATOM   6593 C CA  . GLN E 5 236 ? 30.984 -30.436 -48.789 1.00 27.47  ?  235 GLN E CA  1 
ATOM   6594 C C   . GLN E 5 236 ? 30.558 -29.704 -50.052 1.00 25.96  ?  235 GLN E C   1 
ATOM   6595 O O   . GLN E 5 236 ? 29.480 -29.110 -50.116 1.00 22.70  ?  235 GLN E O   1 
ATOM   6596 C CB  . GLN E 5 236 ? 30.748 -31.953 -48.947 1.00 25.01  ?  235 GLN E CB  1 
ATOM   6597 C CG  . GLN E 5 236 ? 29.307 -32.294 -49.364 1.00 21.49  ?  235 GLN E CG  1 
ATOM   6598 C CD  . GLN E 5 236 ? 29.030 -33.790 -49.387 1.00 26.22  ?  235 GLN E CD  1 
ATOM   6599 O OE1 . GLN E 5 236 ? 29.135 -34.448 -50.430 1.00 26.00  ?  235 GLN E OE1 1 
ATOM   6600 N NE2 . GLN E 5 236 ? 28.681 -34.338 -48.231 1.00 28.54  ?  235 GLN E NE2 1 
ATOM   6601 N N   . ILE E 5 237 ? 31.409 -29.779 -51.051 1.00 23.66  ?  236 ILE E N   1 
ATOM   6602 C CA  . ILE E 5 237 ? 31.114 -29.286 -52.388 1.00 28.50  ?  236 ILE E CA  1 
ATOM   6603 C C   . ILE E 5 237 ? 30.761 -30.455 -53.291 1.00 30.28  ?  236 ILE E C   1 
ATOM   6604 O O   . ILE E 5 237 ? 31.340 -31.548 -53.184 1.00 28.51  ?  236 ILE E O   1 
ATOM   6605 C CB  . ILE E 5 237 ? 32.304 -28.482 -52.950 1.00 33.10  ?  236 ILE E CB  1 
ATOM   6606 C CG1 . ILE E 5 237 ? 32.312 -27.086 -52.307 1.00 33.58  ?  236 ILE E CG1 1 
ATOM   6607 C CG2 . ILE E 5 237 ? 32.201 -28.377 -54.479 1.00 32.29  ?  236 ILE E CG2 1 
ATOM   6608 C CD1 . ILE E 5 237 ? 33.537 -26.342 -52.541 1.00 37.46  ?  236 ILE E CD1 1 
ATOM   6609 N N   . VAL E 5 238 ? 29.787 -30.222 -54.178 1.00 29.77  ?  237 VAL E N   1 
ATOM   6610 C CA  . VAL E 5 238 ? 29.371 -31.155 -55.212 1.00 24.84  ?  237 VAL E CA  1 
ATOM   6611 C C   . VAL E 5 238 ? 29.269 -30.365 -56.510 1.00 29.44  ?  237 VAL E C   1 
ATOM   6612 O O   . VAL E 5 238 ? 28.616 -29.319 -56.555 1.00 24.23  ?  237 VAL E O   1 
ATOM   6613 C CB  . VAL E 5 238 ? 28.034 -31.852 -54.876 1.00 29.20  ?  237 VAL E CB  1 
ATOM   6614 C CG1 . VAL E 5 238 ? 27.682 -32.909 -55.961 1.00 26.66  ?  237 VAL E CG1 1 
ATOM   6615 C CG2 . VAL E 5 238 ? 28.093 -32.512 -53.478 1.00 21.74  ?  237 VAL E CG2 1 
ATOM   6616 N N   . SER E 5 239 ? 29.941 -30.856 -57.551 1.00 26.46  ?  238 SER E N   1 
ATOM   6617 C CA  . SER E 5 239 ? 30.125 -30.166 -58.814 1.00 23.79  ?  238 SER E CA  1 
ATOM   6618 C C   . SER E 5 239 ? 29.727 -31.104 -59.934 1.00 24.09  ?  238 SER E C   1 
ATOM   6619 O O   . SER E 5 239 ? 29.765 -32.325 -59.788 1.00 25.16  ?  238 SER E O   1 
ATOM   6620 C CB  . SER E 5 239 ? 31.593 -29.754 -59.034 1.00 21.84  ?  238 SER E CB  1 
ATOM   6621 O OG  . SER E 5 239 ? 31.911 -28.594 -58.300 1.00 29.48  ?  238 SER E OG  1 
ATOM   6622 N N   . ALA E 5 240 ? 29.362 -30.516 -61.060 1.00 26.17  ?  239 ALA E N   1 
ATOM   6623 C CA  . ALA E 5 240 ? 29.289 -31.217 -62.332 1.00 30.05  ?  239 ALA E CA  1 
ATOM   6624 C C   . ALA E 5 240 ? 29.849 -30.271 -63.372 1.00 29.79  ?  239 ALA E C   1 
ATOM   6625 O O   . ALA E 5 240 ? 29.843 -29.050 -63.178 1.00 26.75  ?  239 ALA E O   1 
ATOM   6626 C CB  . ALA E 5 240 ? 27.857 -31.634 -62.706 1.00 26.43  ?  239 ALA E CB  1 
ATOM   6627 N N   . GLU E 5 241 ? 30.341 -30.825 -64.469 1.00 28.05  ?  240 GLU E N   1 
ATOM   6628 C CA  . GLU E 5 241 ? 31.030 -29.999 -65.443 1.00 31.08  ?  240 GLU E CA  1 
ATOM   6629 C C   . GLU E 5 241 ? 30.693 -30.427 -66.864 1.00 36.45  ?  240 GLU E C   1 
ATOM   6630 O O   . GLU E 5 241 ? 30.133 -31.501 -67.108 1.00 29.92  ?  240 GLU E O   1 
ATOM   6631 C CB  . GLU E 5 241 ? 32.536 -30.047 -65.212 1.00 32.38  ?  240 GLU E CB  1 
ATOM   6632 C CG  . GLU E 5 241 ? 33.078 -31.420 -64.988 1.00 42.13  ?  240 GLU E CG  1 
ATOM   6633 C CD  . GLU E 5 241 ? 34.579 -31.382 -64.731 1.00 51.37  ?  240 GLU E CD  1 
ATOM   6634 O OE1 . GLU E 5 241 ? 35.315 -31.849 -65.634 1.00 46.83  ?  240 GLU E OE1 1 
ATOM   6635 O OE2 . GLU E 5 241 ? 35.004 -30.863 -63.647 1.00 51.55  -1 240 GLU E OE2 1 
ATOM   6636 N N   . ALA E 5 242 ? 31.049 -29.558 -67.812 1.00 27.24  ?  241 ALA E N   1 
ATOM   6637 C CA  . ALA E 5 242 ? 30.912 -29.850 -69.230 1.00 26.97  ?  241 ALA E CA  1 
ATOM   6638 C C   . ALA E 5 242 ? 32.029 -29.130 -69.976 1.00 29.97  ?  241 ALA E C   1 
ATOM   6639 O O   . ALA E 5 242 ? 32.532 -28.094 -69.524 1.00 28.19  ?  241 ALA E O   1 
ATOM   6640 C CB  . ALA E 5 242 ? 29.543 -29.401 -69.757 1.00 29.21  ?  241 ALA E CB  1 
ATOM   6641 N N   . TRP E 5 243 ? 32.418 -29.679 -71.116 1.00 23.18  ?  242 TRP E N   1 
ATOM   6642 C CA  . TRP E 5 243 ? 33.323 -28.994 -72.029 1.00 24.73  ?  242 TRP E CA  1 
ATOM   6643 C C   . TRP E 5 243 ? 32.577 -28.483 -73.262 1.00 28.92  ?  242 TRP E C   1 
ATOM   6644 O O   . TRP E 5 243 ? 31.562 -29.050 -73.676 1.00 26.93  ?  242 TRP E O   1 
ATOM   6645 C CB  . TRP E 5 243 ? 34.439 -29.929 -72.471 1.00 27.49  ?  242 TRP E CB  1 
ATOM   6646 C CG  . TRP E 5 243 ? 35.389 -30.263 -71.365 1.00 35.77  ?  242 TRP E CG  1 
ATOM   6647 C CD1 . TRP E 5 243 ? 35.235 -31.214 -70.386 1.00 33.28  ?  242 TRP E CD1 1 
ATOM   6648 C CD2 . TRP E 5 243 ? 36.643 -29.639 -71.121 1.00 28.51  ?  242 TRP E CD2 1 
ATOM   6649 N NE1 . TRP E 5 243 ? 36.329 -31.219 -69.563 1.00 32.90  ?  242 TRP E NE1 1 
ATOM   6650 C CE2 . TRP E 5 243 ? 37.206 -30.260 -69.992 1.00 33.29  ?  242 TRP E CE2 1 
ATOM   6651 C CE3 . TRP E 5 243 ? 37.343 -28.612 -71.746 1.00 27.67  ?  242 TRP E CE3 1 
ATOM   6652 C CZ2 . TRP E 5 243 ? 38.443 -29.895 -69.492 1.00 33.92  ?  242 TRP E CZ2 1 
ATOM   6653 C CZ3 . TRP E 5 243 ? 38.569 -28.241 -71.235 1.00 34.37  ?  242 TRP E CZ3 1 
ATOM   6654 C CH2 . TRP E 5 243 ? 39.109 -28.877 -70.132 1.00 30.63  ?  242 TRP E CH2 1 
ATOM   6655 N N   . GLY E 5 244 ? 33.100 -27.418 -73.868 1.00 26.97  ?  243 GLY E N   1 
ATOM   6656 C CA  . GLY E 5 244 ? 32.559 -26.972 -75.133 1.00 28.68  ?  243 GLY E CA  1 
ATOM   6657 C C   . GLY E 5 244 ? 32.773 -28.021 -76.203 1.00 32.03  ?  243 GLY E C   1 
ATOM   6658 O O   . GLY E 5 244 ? 33.606 -28.916 -76.064 1.00 29.08  ?  243 GLY E O   1 
ATOM   6659 N N   . ARG E 5 245 ? 32.000 -27.923 -77.283 1.00 36.35  ?  244 ARG E N   1 
ATOM   6660 C CA  . ARG E 5 245 ? 31.979 -28.984 -78.285 1.00 38.90  ?  244 ARG E CA  1 
ATOM   6661 C C   . ARG E 5 245 ? 31.850 -28.353 -79.656 1.00 36.59  ?  244 ARG E C   1 
ATOM   6662 O O   . ARG E 5 245 ? 30.915 -27.585 -79.898 1.00 29.57  ?  244 ARG E O   1 
ATOM   6663 C CB  . ARG E 5 245 ? 30.835 -29.960 -78.023 1.00 43.85  ?  244 ARG E CB  1 
ATOM   6664 C CG  . ARG E 5 245 ? 30.682 -31.024 -79.102 1.00 54.80  ?  244 ARG E CG  1 
ATOM   6665 C CD  . ARG E 5 245 ? 29.950 -32.250 -78.564 1.00 60.77  ?  244 ARG E CD  1 
ATOM   6666 N NE  . ARG E 5 245 ? 28.586 -31.939 -78.138 1.00 63.89  ?  244 ARG E NE  1 
ATOM   6667 C CZ  . ARG E 5 245 ? 28.220 -31.705 -76.876 1.00 61.57  ?  244 ARG E CZ  1 
ATOM   6668 N NH1 . ARG E 5 245 ? 29.125 -31.741 -75.894 1.00 56.63  ?  244 ARG E NH1 1 
ATOM   6669 N NH2 . ARG E 5 245 ? 26.945 -31.410 -76.604 1.00 50.66  ?  244 ARG E NH2 1 
ATOM   6670 N N   . ALA E 5 246 ? 32.815 -28.643 -80.522 1.00 34.44  ?  245 ALA E N   1 
ATOM   6671 C CA  . ALA E 5 246 ? 32.791 -28.134 -81.885 1.00 47.35  ?  245 ALA E CA  1 
ATOM   6672 C C   . ALA E 5 246 ? 31.498 -28.537 -82.590 1.00 52.33  ?  245 ALA E C   1 
ATOM   6673 O O   . ALA E 5 246 ? 30.945 -29.621 -82.358 1.00 47.68  ?  245 ALA E O   1 
ATOM   6674 C CB  . ALA E 5 246 ? 34.000 -28.653 -82.666 1.00 45.21  ?  245 ALA E CB  1 
ATOM   6675 N N   . ASP E 5 247 ? 31.011 -27.641 -83.442 1.00 49.90  ?  246 ASP E N   1 
ATOM   6676 C CA  . ASP E 5 247 ? 29.799 -27.881 -84.208 1.00 62.62  ?  246 ASP E CA  1 
ATOM   6677 C C   . ASP E 5 247 ? 29.979 -29.142 -85.028 1.00 68.35  ?  246 ASP E C   1 
ATOM   6678 O O   . ASP E 5 247 ? 31.088 -29.470 -85.465 1.00 63.08  ?  246 ASP E O   1 
ATOM   6679 C CB  . ASP E 5 247 ? 29.468 -26.689 -85.121 1.00 64.33  ?  246 ASP E CB  1 
ATOM   6680 C CG  . ASP E 5 247 ? 27.960 -26.472 -85.293 1.00 67.70  ?  246 ASP E CG  1 
ATOM   6681 O OD1 . ASP E 5 247 ? 27.156 -27.034 -84.508 1.00 71.10  ?  246 ASP E OD1 1 
ATOM   6682 O OD2 . ASP E 5 247 ? 27.577 -25.718 -86.212 1.00 64.08  -1 246 ASP E OD2 1 
ATOM   6683 O OXT . ASP E 5 247 ? 29.007 -29.857 -85.250 1.00 74.35  -1 246 ASP E OXT 1 
HETATM 6684 C C1  . GOL F 6 .   ? 15.917 24.788  -13.001 1.00 45.72  ?  301 GOL A C1  1 
HETATM 6685 O O1  . GOL F 6 .   ? 17.124 25.408  -12.561 1.00 59.97  ?  301 GOL A O1  1 
HETATM 6686 C C2  . GOL F 6 .   ? 15.030 25.929  -13.619 1.00 50.61  ?  301 GOL A C2  1 
HETATM 6687 O O2  . GOL F 6 .   ? 14.917 27.025  -12.767 1.00 54.16  ?  301 GOL A O2  1 
HETATM 6688 C C3  . GOL F 6 .   ? 15.706 26.227  -14.980 1.00 54.88  ?  301 GOL A C3  1 
HETATM 6689 O O3  . GOL F 6 .   ? 15.488 25.095  -15.814 1.00 51.02  ?  301 GOL A O3  1 
HETATM 6690 C C1  . GOL G 6 .   ? 45.267 10.684  -18.003 1.00 44.51  ?  302 GOL A C1  1 
HETATM 6691 O O1  . GOL G 6 .   ? 45.999 9.584   -18.482 1.00 61.29  ?  302 GOL A O1  1 
HETATM 6692 C C2  . GOL G 6 .   ? 45.463 11.881  -18.965 1.00 52.04  ?  302 GOL A C2  1 
HETATM 6693 O O2  . GOL G 6 .   ? 46.774 11.949  -19.410 1.00 59.43  ?  302 GOL A O2  1 
HETATM 6694 C C3  . GOL G 6 .   ? 45.055 13.127  -18.135 1.00 45.93  ?  302 GOL A C3  1 
HETATM 6695 O O3  . GOL G 6 .   ? 45.214 14.274  -18.982 1.00 57.27  ?  302 GOL A O3  1 
HETATM 6696 C C1  . GOL H 6 .   ? 34.412 1.059   -4.568  1.00 61.02  ?  303 GOL A C1  1 
HETATM 6697 O O1  . GOL H 6 .   ? 35.487 1.445   -3.705  1.00 60.68  ?  303 GOL A O1  1 
HETATM 6698 C C2  . GOL H 6 .   ? 33.465 0.061   -3.930  1.00 65.50  ?  303 GOL A C2  1 
HETATM 6699 O O2  . GOL H 6 .   ? 33.829 -0.228  -2.586  1.00 77.14  ?  303 GOL A O2  1 
HETATM 6700 C C3  . GOL H 6 .   ? 32.022 0.501   -3.919  1.00 73.22  ?  303 GOL A C3  1 
HETATM 6701 O O3  . GOL H 6 .   ? 31.148 -0.618  -3.911  1.00 77.00  ?  303 GOL A O3  1 
HETATM 6702 C C1  . EDO I 7 .   ? 6.847  34.636  3.488   1.00 50.86  ?  304 EDO A C1  1 
HETATM 6703 O O1  . EDO I 7 .   ? 7.797  33.594  3.810   1.00 49.03  ?  304 EDO A O1  1 
HETATM 6704 C C2  . EDO I 7 .   ? 7.240  35.954  4.158   1.00 50.73  ?  304 EDO A C2  1 
HETATM 6705 O O2  . EDO I 7 .   ? 7.175  35.845  5.594   1.00 54.05  ?  304 EDO A O2  1 
HETATM 6706 C C1  . GOL J 6 .   ? 13.337 11.119  -33.130 1.00 32.49  ?  301 GOL D C1  1 
HETATM 6707 O O1  . GOL J 6 .   ? 13.156 11.207  -31.749 1.00 32.39  ?  301 GOL D O1  1 
HETATM 6708 C C2  . GOL J 6 .   ? 12.876 12.429  -33.839 1.00 34.97  ?  301 GOL D C2  1 
HETATM 6709 O O2  . GOL J 6 .   ? 13.406 13.590  -33.217 1.00 37.51  ?  301 GOL D O2  1 
HETATM 6710 C C3  . GOL J 6 .   ? 13.422 12.215  -35.306 1.00 37.29  ?  301 GOL D C3  1 
HETATM 6711 O O3  . GOL J 6 .   ? 13.084 13.288  -36.105 1.00 36.57  ?  301 GOL D O3  1 
HETATM 6712 C C1  . EDO K 7 .   ? 29.975 -34.052 -63.972 1.00 43.49  ?  301 EDO E C1  1 
HETATM 6713 O O1  . EDO K 7 .   ? 31.291 -34.605 -63.826 1.00 53.00  ?  301 EDO E O1  1 
HETATM 6714 C C2  . EDO K 7 .   ? 29.780 -33.596 -65.417 1.00 44.10  ?  301 EDO E C2  1 
HETATM 6715 O O2  . EDO K 7 .   ? 28.390 -33.562 -65.817 1.00 48.82  ?  301 EDO E O2  1 
HETATM 6716 C C1  . GOL L 6 .   ? 40.717 -23.448 -68.981 1.00 54.16  ?  302 GOL E C1  1 
HETATM 6717 O O1  . GOL L 6 .   ? 41.484 -22.249 -68.863 1.00 57.29  ?  302 GOL E O1  1 
HETATM 6718 C C2  . GOL L 6 .   ? 41.547 -24.542 -69.617 1.00 52.19  ?  302 GOL E C2  1 
HETATM 6719 O O2  . GOL L 6 .   ? 41.092 -25.833 -69.226 1.00 46.78  ?  302 GOL E O2  1 
HETATM 6720 C C3  . GOL L 6 .   ? 41.589 -24.436 -71.125 1.00 46.55  ?  302 GOL E C3  1 
HETATM 6721 O O3  . GOL L 6 .   ? 41.116 -23.170 -71.572 1.00 49.02  ?  302 GOL E O3  1 
HETATM 6722 C C1  . GOL M 6 .   ? 30.885 -17.738 -54.537 1.00 52.90  ?  303 GOL E C1  1 
HETATM 6723 O O1  . GOL M 6 .   ? 31.811 -18.845 -54.285 1.00 44.59  ?  303 GOL E O1  1 
HETATM 6724 C C2  . GOL M 6 .   ? 29.463 -18.179 -54.061 1.00 49.71  ?  303 GOL E C2  1 
HETATM 6725 O O2  . GOL M 6 .   ? 29.099 -17.614 -52.820 1.00 57.02  ?  303 GOL E O2  1 
HETATM 6726 C C3  . GOL M 6 .   ? 28.455 -17.723 -55.185 1.00 44.07  ?  303 GOL E C3  1 
HETATM 6727 O O3  . GOL M 6 .   ? 27.159 -18.397 -54.957 1.00 44.35  ?  303 GOL E O3  1 
HETATM 6728 C C1  . GOL N 6 .   ? 32.415 -11.853 -65.727 1.00 55.55  ?  304 GOL E C1  1 
HETATM 6729 O O1  . GOL N 6 .   ? 33.362 -10.970 -65.142 1.00 49.39  ?  304 GOL E O1  1 
HETATM 6730 C C2  . GOL N 6 .   ? 31.341 -12.286 -64.747 1.00 38.70  ?  304 GOL E C2  1 
HETATM 6731 O O2  . GOL N 6 .   ? 30.356 -12.961 -65.491 1.00 42.36  ?  304 GOL E O2  1 
HETATM 6732 C C3  . GOL N 6 .   ? 30.670 -11.180 -63.969 1.00 47.49  ?  304 GOL E C3  1 
HETATM 6733 O O3  . GOL N 6 .   ? 31.236 -10.976 -62.680 1.00 56.15  ?  304 GOL E O3  1 
HETATM 6734 C C1  . GOL O 6 .   ? 20.335 -44.653 -43.402 1.00 56.79  ?  305 GOL E C1  1 
HETATM 6735 O O1  . GOL O 6 .   ? 19.409 -44.731 -42.347 1.00 59.54  ?  305 GOL E O1  1 
HETATM 6736 C C2  . GOL O 6 .   ? 20.763 -46.052 -43.868 1.00 59.18  ?  305 GOL E C2  1 
HETATM 6737 O O2  . GOL O 6 .   ? 21.398 -45.985 -45.143 1.00 59.09  ?  305 GOL E O2  1 
HETATM 6738 C C3  . GOL O 6 .   ? 21.704 -46.571 -42.723 1.00 55.83  ?  305 GOL E C3  1 
HETATM 6739 O O3  . GOL O 6 .   ? 20.962 -46.753 -41.529 1.00 56.16  ?  305 GOL E O3  1 
HETATM 6740 O O   . HOH P 8 .   ? 5.957  36.606  -20.405 1.00 56.41  ?  401 HOH A O   1 
HETATM 6741 O O   . HOH P 8 .   ? 1.178  34.417  -6.983  1.00 46.51  ?  402 HOH A O   1 
HETATM 6742 O O   . HOH P 8 .   ? 17.589 44.221  10.422  1.00 46.22  ?  403 HOH A O   1 
HETATM 6743 O O   . HOH P 8 .   ? 30.008 -0.114  -18.271 1.00 46.63  ?  404 HOH A O   1 
HETATM 6744 O O   . HOH P 8 .   ? 11.674 12.496  -20.017 1.00 30.95  ?  405 HOH A O   1 
HETATM 6745 O O   . HOH P 8 .   ? 6.122  1.578   -18.783 1.00 41.90  ?  406 HOH A O   1 
HETATM 6746 O O   . HOH P 8 .   ? 26.638 19.881  -35.517 1.00 42.95  ?  407 HOH A O   1 
HETATM 6747 O O   . HOH P 8 .   ? 5.342  51.876  5.790   1.00 36.47  ?  408 HOH A O   1 
HETATM 6748 O O   . HOH P 8 .   ? 26.135 24.425  -24.397 1.00 32.11  ?  409 HOH A O   1 
HETATM 6749 O O   . HOH P 8 .   ? 2.901  1.854   -29.449 1.00 42.19  ?  410 HOH A O   1 
HETATM 6750 O O   . HOH P 8 .   ? 10.689 0.478   -17.859 1.00 43.03  ?  411 HOH A O   1 
HETATM 6751 O O   . HOH P 8 .   ? 15.138 34.905  -9.563  1.00 34.31  ?  412 HOH A O   1 
HETATM 6752 O O   . HOH P 8 .   ? 6.337  20.156  -10.786 1.00 37.96  ?  413 HOH A O   1 
HETATM 6753 O O   . HOH P 8 .   ? 25.152 25.903  -26.424 1.00 38.86  ?  414 HOH A O   1 
HETATM 6754 O O   . HOH P 8 .   ? 14.136 4.437   -8.773  1.00 44.32  ?  415 HOH A O   1 
HETATM 6755 O O   . HOH P 8 .   ? 29.143 11.489  -18.175 1.00 29.03  ?  416 HOH A O   1 
HETATM 6756 O O   . HOH P 8 .   ? 2.582  8.693   -24.211 1.00 35.81  ?  417 HOH A O   1 
HETATM 6757 O O   . HOH P 8 .   ? 39.606 13.514  -33.076 1.00 43.10  ?  418 HOH A O   1 
HETATM 6758 O O   . HOH P 8 .   ? 32.151 28.020  -31.944 1.00 46.84  ?  419 HOH A O   1 
HETATM 6759 O O   . HOH P 8 .   ? 10.843 -2.449  -23.656 1.00 34.70  ?  420 HOH A O   1 
HETATM 6760 O O   . HOH P 8 .   ? 16.117 1.178   -14.594 1.00 40.06  ?  421 HOH A O   1 
HETATM 6761 O O   . HOH P 8 .   ? 22.722 27.455  -29.649 1.00 39.17  ?  422 HOH A O   1 
HETATM 6762 O O   . HOH P 8 .   ? 38.450 16.646  -9.083  1.00 29.03  ?  423 HOH A O   1 
HETATM 6763 O O   . HOH P 8 .   ? 35.749 9.759   -10.661 1.00 27.94  ?  424 HOH A O   1 
HETATM 6764 O O   . HOH P 8 .   ? 13.267 6.619   -10.013 1.00 33.35  ?  425 HOH A O   1 
HETATM 6765 O O   . HOH P 8 .   ? 28.198 15.092  -4.927  1.00 32.57  ?  426 HOH A O   1 
HETATM 6766 O O   . HOH P 8 .   ? 30.269 13.124  -2.908  1.00 38.43  ?  427 HOH A O   1 
HETATM 6767 O O   . HOH P 8 .   ? 21.125 29.341  -31.239 1.00 41.72  ?  428 HOH A O   1 
HETATM 6768 O O   . HOH P 8 .   ? 6.001  27.519  -17.428 1.00 44.97  ?  429 HOH A O   1 
HETATM 6769 O O   . HOH P 8 .   ? 14.124 9.588   -24.881 1.00 30.67  ?  430 HOH A O   1 
HETATM 6770 O O   . HOH P 8 .   ? 2.407  4.178   -24.363 1.00 44.74  ?  431 HOH A O   1 
HETATM 6771 O O   . HOH P 8 .   ? 26.494 9.937   -19.857 1.00 32.71  ?  432 HOH A O   1 
HETATM 6772 O O   . HOH P 8 .   ? 5.153  15.095  -31.621 1.00 49.13  ?  433 HOH A O   1 
HETATM 6773 O O   . HOH P 8 .   ? 13.766 60.142  5.468   1.00 52.06  ?  434 HOH A O   1 
HETATM 6774 O O   . HOH P 8 .   ? 40.561 7.596   -22.814 1.00 41.28  ?  435 HOH A O   1 
HETATM 6775 O O   . HOH P 8 .   ? 18.633 33.834  -6.828  1.00 36.49  ?  436 HOH A O   1 
HETATM 6776 O O   . HOH P 8 .   ? 34.801 7.102   -20.521 1.00 32.72  ?  437 HOH A O   1 
HETATM 6777 O O   . HOH P 8 .   ? 14.031 19.296  -8.776  1.00 37.05  ?  438 HOH A O   1 
HETATM 6778 O O   . HOH P 8 .   ? 30.353 17.888  -11.118 1.00 27.82  ?  439 HOH A O   1 
HETATM 6779 O O   . HOH P 8 .   ? 18.863 0.866   -21.582 1.00 25.62  ?  440 HOH A O   1 
HETATM 6780 O O   . HOH P 8 .   ? 33.643 19.997  -33.893 1.00 47.20  ?  441 HOH A O   1 
HETATM 6781 O O   . HOH P 8 .   ? 7.379  26.821  -5.800  1.00 39.72  ?  442 HOH A O   1 
HETATM 6782 O O   . HOH P 8 .   ? 12.160 53.648  1.540   1.00 43.67  ?  443 HOH A O   1 
HETATM 6783 O O   . HOH P 8 .   ? 20.345 16.298  -10.707 1.00 26.95  ?  444 HOH A O   1 
HETATM 6784 O O   . HOH P 8 .   ? 32.263 15.912  -5.917  1.00 29.40  ?  445 HOH A O   1 
HETATM 6785 O O   . HOH P 8 .   ? 23.441 11.268  -7.743  1.00 35.68  ?  446 HOH A O   1 
HETATM 6786 O O   . HOH P 8 .   ? 34.367 5.209   -9.704  1.00 38.38  ?  447 HOH A O   1 
HETATM 6787 O O   . HOH P 8 .   ? 10.509 37.831  -15.004 1.00 46.20  ?  448 HOH A O   1 
HETATM 6788 O O   . HOH P 8 .   ? 22.741 0.994   -16.160 1.00 43.78  ?  449 HOH A O   1 
HETATM 6789 O O   . HOH P 8 .   ? 25.779 13.250  -14.889 1.00 33.74  ?  450 HOH A O   1 
HETATM 6790 O O   . HOH P 8 .   ? 6.852  5.673   -13.826 1.00 44.25  ?  451 HOH A O   1 
HETATM 6791 O O   . HOH P 8 .   ? 13.869 24.823  -18.074 1.00 40.52  ?  452 HOH A O   1 
HETATM 6792 O O   . HOH P 8 .   ? 2.420  15.553  -21.703 1.00 41.36  ?  453 HOH A O   1 
HETATM 6793 O O   . HOH P 8 .   ? 35.263 21.022  -31.150 1.00 41.10  ?  454 HOH A O   1 
HETATM 6794 O O   . HOH P 8 .   ? 14.292 23.379  -35.361 1.00 43.41  ?  455 HOH A O   1 
HETATM 6795 O O   . HOH P 8 .   ? 9.748  49.710  12.708  1.00 37.92  ?  456 HOH A O   1 
HETATM 6796 O O   . HOH P 8 .   ? 2.858  15.346  -29.812 1.00 39.61  ?  457 HOH A O   1 
HETATM 6797 O O   . HOH P 8 .   ? 47.320 8.649   -15.551 1.00 53.81  ?  458 HOH A O   1 
HETATM 6798 O O   . HOH P 8 .   ? 35.684 3.229   -17.412 1.00 37.87  ?  459 HOH A O   1 
HETATM 6799 O O   . HOH P 8 .   ? 41.477 6.904   -17.556 1.00 39.75  ?  460 HOH A O   1 
HETATM 6800 O O   . HOH P 8 .   ? 31.767 16.433  -32.134 1.00 30.06  ?  461 HOH A O   1 
HETATM 6801 O O   . HOH P 8 .   ? 5.379  51.830  2.676   1.00 40.77  ?  462 HOH A O   1 
HETATM 6802 O O   . HOH P 8 .   ? 18.970 67.239  2.481   1.00 57.04  ?  463 HOH A O   1 
HETATM 6803 O O   . HOH P 8 .   ? 44.329 7.433   -17.700 1.00 53.23  ?  464 HOH A O   1 
HETATM 6804 O O   . HOH P 8 .   ? 22.654 52.578  2.600   1.00 63.00  ?  465 HOH A O   1 
HETATM 6805 O O   . HOH P 8 .   ? 22.699 10.589  -13.287 1.00 30.78  ?  466 HOH A O   1 
HETATM 6806 O O   . HOH P 8 .   ? 0.555  11.660  -28.963 1.00 49.64  ?  467 HOH A O   1 
HETATM 6807 O O   . HOH P 8 .   ? 25.414 3.098   -22.136 1.00 35.52  ?  468 HOH A O   1 
HETATM 6808 O O   . HOH P 8 .   ? 29.422 26.671  -16.931 1.00 52.43  ?  469 HOH A O   1 
HETATM 6809 O O   . HOH P 8 .   ? 6.107  28.856  -27.354 1.00 56.64  ?  470 HOH A O   1 
HETATM 6810 O O   . HOH P 8 .   ? 11.878 22.303  -7.975  1.00 47.07  ?  471 HOH A O   1 
HETATM 6811 O O   . HOH P 8 .   ? 30.214 3.878   -6.266  1.00 44.56  ?  472 HOH A O   1 
HETATM 6812 O O   . HOH P 8 .   ? 12.510 58.717  8.509   1.00 44.39  ?  473 HOH A O   1 
HETATM 6813 O O   . HOH P 8 .   ? 33.744 25.757  -13.558 1.00 39.00  ?  474 HOH A O   1 
HETATM 6814 O O   . HOH P 8 .   ? 30.064 29.265  -27.358 1.00 36.65  ?  475 HOH A O   1 
HETATM 6815 O O   . HOH P 8 .   ? 0.298  6.234   -18.016 1.00 49.90  ?  476 HOH A O   1 
HETATM 6816 O O   . HOH P 8 .   ? 3.591  25.465  -13.790 1.00 45.98  ?  477 HOH A O   1 
HETATM 6817 O O   . HOH P 8 .   ? 8.162  46.245  9.389   1.00 38.67  ?  478 HOH A O   1 
HETATM 6818 O O   . HOH P 8 .   ? 17.792 41.074  -7.904  1.00 50.13  ?  479 HOH A O   1 
HETATM 6819 O O   . HOH P 8 .   ? 11.036 19.677  -33.854 1.00 41.55  ?  480 HOH A O   1 
HETATM 6820 O O   . HOH P 8 .   ? 8.350  4.990   -26.793 1.00 39.78  ?  481 HOH A O   1 
HETATM 6821 O O   . HOH P 8 .   ? 5.546  51.829  -1.225  1.00 49.23  ?  482 HOH A O   1 
HETATM 6822 O O   . HOH P 8 .   ? 4.006  47.701  -3.139  1.00 49.91  ?  483 HOH A O   1 
HETATM 6823 O O   . HOH P 8 .   ? 38.699 24.022  -26.019 1.00 43.76  ?  484 HOH A O   1 
HETATM 6824 O O   . HOH P 8 .   ? 41.496 11.233  -27.342 1.00 44.34  ?  485 HOH A O   1 
HETATM 6825 O O   . HOH P 8 .   ? 27.601 18.403  -40.064 1.00 62.21  ?  486 HOH A O   1 
HETATM 6826 O O   . HOH P 8 .   ? 13.958 31.344  -33.654 1.00 52.69  ?  487 HOH A O   1 
HETATM 6827 O O   . HOH P 8 .   ? 11.931 24.951  -34.688 1.00 41.74  ?  488 HOH A O   1 
HETATM 6828 O O   . HOH P 8 .   ? 13.050 34.606  5.415   1.00 42.43  ?  489 HOH A O   1 
HETATM 6829 O O   . HOH P 8 .   ? 37.252 23.984  -14.914 1.00 37.17  ?  490 HOH A O   1 
HETATM 6830 O O   . HOH P 8 .   ? 32.860 14.518  -3.359  1.00 39.89  ?  491 HOH A O   1 
HETATM 6831 O O   . HOH P 8 .   ? 5.119  32.848  -2.574  1.00 38.44  ?  492 HOH A O   1 
HETATM 6832 O O   . HOH P 8 .   ? 31.669 22.635  -19.061 1.00 36.04  ?  493 HOH A O   1 
HETATM 6833 O O   . HOH P 8 .   ? 20.873 -3.181  -19.084 1.00 31.32  ?  494 HOH A O   1 
HETATM 6834 O O   . HOH P 8 .   ? 35.146 7.829   -8.799  1.00 30.67  ?  495 HOH A O   1 
HETATM 6835 O O   . HOH P 8 .   ? 8.667  22.319  -9.828  1.00 37.45  ?  496 HOH A O   1 
HETATM 6836 O O   . HOH P 8 .   ? 41.988 23.340  -22.107 1.00 51.43  ?  497 HOH A O   1 
HETATM 6837 O O   . HOH P 8 .   ? 45.229 20.972  -17.601 1.00 45.89  ?  498 HOH A O   1 
HETATM 6838 O O   . HOH P 8 .   ? 20.930 44.173  7.892   1.00 57.97  ?  499 HOH A O   1 
HETATM 6839 O O   . HOH P 8 .   ? 38.870 4.444   -19.881 1.00 41.16  ?  500 HOH A O   1 
HETATM 6840 O O   . HOH P 8 .   ? 32.262 26.231  -10.345 1.00 50.22  ?  501 HOH A O   1 
HETATM 6841 O O   . HOH P 8 .   ? 20.815 11.504  -22.158 1.00 35.51  ?  502 HOH A O   1 
HETATM 6842 O O   . HOH P 8 .   ? 29.837 16.730  -35.336 1.00 34.50  ?  503 HOH A O   1 
HETATM 6843 O O   . HOH P 8 .   ? 3.292  24.328  -28.213 1.00 43.29  ?  504 HOH A O   1 
HETATM 6844 O O   . HOH P 8 .   ? 21.052 1.257   -6.557  1.00 48.40  ?  505 HOH A O   1 
HETATM 6845 O O   . HOH P 8 .   ? 20.541 3.738   -13.049 1.00 47.39  ?  506 HOH A O   1 
HETATM 6846 O O   . HOH P 8 .   ? 37.041 19.285  -13.300 1.00 48.97  ?  507 HOH A O   1 
HETATM 6847 O O   . HOH P 8 .   ? 33.855 23.391  -20.475 1.00 37.17  ?  508 HOH A O   1 
HETATM 6848 O O   . HOH P 8 .   ? 5.457  -0.070  -22.238 1.00 45.16  ?  509 HOH A O   1 
HETATM 6849 O O   . HOH P 8 .   ? 7.533  -0.386  -24.154 1.00 41.96  ?  510 HOH A O   1 
HETATM 6850 O O   . HOH P 8 .   ? 30.142 28.900  -30.887 1.00 41.04  ?  511 HOH A O   1 
HETATM 6851 O O   . HOH P 8 .   ? -4.065 18.438  -24.888 1.00 50.79  ?  512 HOH A O   1 
HETATM 6852 O O   . HOH P 8 .   ? 6.460  6.859   -26.162 1.00 38.06  ?  513 HOH A O   1 
HETATM 6853 O O   . HOH P 8 .   ? 26.240 20.267  -41.116 1.00 58.05  ?  514 HOH A O   1 
HETATM 6854 O O   . HOH P 8 .   ? 2.736  46.850  0.243   1.00 46.61  ?  515 HOH A O   1 
HETATM 6855 O O   . HOH P 8 .   ? 13.576 10.582  -5.476  1.00 50.97  ?  516 HOH A O   1 
HETATM 6856 O O   . HOH P 8 .   ? 8.594  2.445   -17.103 1.00 41.48  ?  517 HOH A O   1 
HETATM 6857 O O   . HOH P 8 .   ? 32.868 17.046  -35.477 1.00 45.35  ?  518 HOH A O   1 
HETATM 6858 O O   . HOH P 8 .   ? 31.266 27.586  -13.875 1.00 48.24  ?  519 HOH A O   1 
HETATM 6859 O O   . HOH P 8 .   ? 31.652 0.945   -15.938 1.00 45.50  ?  520 HOH A O   1 
HETATM 6860 O O   . HOH P 8 .   ? 40.652 4.206   -16.297 1.00 51.66  ?  521 HOH A O   1 
HETATM 6861 O O   . HOH P 8 .   ? 4.074  6.391   -14.611 1.00 44.68  ?  522 HOH A O   1 
HETATM 6862 O O   . HOH P 8 .   ? 40.656 10.627  -30.376 1.00 43.48  ?  523 HOH A O   1 
HETATM 6863 O O   . HOH P 8 .   ? 38.075 4.331   -22.661 1.00 53.14  ?  524 HOH A O   1 
HETATM 6864 O O   . HOH P 8 .   ? 38.518 3.240   -16.539 1.00 48.91  ?  525 HOH A O   1 
HETATM 6865 O O   . HOH P 8 .   ? 22.114 1.630   -11.277 1.00 52.04  ?  526 HOH A O   1 
HETATM 6866 O O   . HOH P 8 .   ? 7.442  48.265  11.227  1.00 44.73  ?  527 HOH A O   1 
HETATM 6867 O O   . HOH P 8 .   ? 23.064 62.939  -6.589  1.00 64.61  ?  528 HOH A O   1 
HETATM 6868 O O   . HOH P 8 .   ? 4.576  26.501  -28.734 1.00 51.17  ?  529 HOH A O   1 
HETATM 6869 O O   . HOH P 8 .   ? 28.771 19.417  -36.393 1.00 48.33  ?  530 HOH A O   1 
HETATM 6870 O O   . HOH P 8 .   ? 34.075 17.706  -38.157 1.00 61.06  ?  531 HOH A O   1 
HETATM 6871 O O   . HOH P 8 .   ? 15.304 -0.554  -16.051 1.00 46.23  ?  532 HOH A O   1 
HETATM 6872 O O   . HOH P 8 .   ? 39.321 9.001   -30.675 1.00 47.68  ?  533 HOH A O   1 
HETATM 6873 O O   . HOH P 8 .   ? 34.023 1.127   -16.387 1.00 46.64  ?  534 HOH A O   1 
HETATM 6874 O O   . HOH P 8 .   ? 35.682 2.264   -20.229 1.00 44.03  ?  535 HOH A O   1 
HETATM 6875 O O   . HOH P 8 .   ? 41.078 5.859   -20.403 1.00 41.66  ?  536 HOH A O   1 
HETATM 6876 O O   . HOH P 8 .   ? 33.009 3.254   -7.077  1.00 51.59  ?  537 HOH A O   1 
HETATM 6877 O O   . HOH P 8 .   ? 35.015 7.319   -28.144 1.00 45.41  ?  538 HOH A O   1 
HETATM 6878 O O   . HOH P 8 .   ? 6.349  3.097   -15.201 1.00 42.88  ?  539 HOH A O   1 
HETATM 6879 O O   . HOH Q 8 .   ? 25.036 8.481   -22.013 1.00 37.22  ?  101 HOH C O   1 
HETATM 6880 O O   . HOH Q 8 .   ? 28.411 11.716  -20.930 1.00 23.08  ?  102 HOH C O   1 
HETATM 6881 O O   . HOH Q 8 .   ? 21.270 12.500  -30.140 1.00 35.76  ?  103 HOH C O   1 
HETATM 6882 O O   . HOH Q 8 .   ? 22.737 11.945  -24.273 1.00 29.56  ?  104 HOH C O   1 
HETATM 6883 O O   . HOH Q 8 .   ? 28.672 14.230  -26.636 1.00 27.33  ?  105 HOH C O   1 
HETATM 6884 O O   . HOH Q 8 .   ? 28.521 6.982   -25.289 1.00 25.29  ?  106 HOH C O   1 
HETATM 6885 O O   . HOH Q 8 .   ? 34.958 4.655   -21.793 1.00 35.52  ?  107 HOH C O   1 
HETATM 6886 O O   . HOH Q 8 .   ? 31.508 7.971   -26.761 1.00 32.32  ?  108 HOH C O   1 
HETATM 6887 O O   . HOH Q 8 .   ? 33.790 8.729   -27.163 1.00 39.23  ?  109 HOH C O   1 
HETATM 6888 O O   . HOH Q 8 .   ? 32.839 0.913   -21.192 1.00 50.34  ?  110 HOH C O   1 
HETATM 6889 O O   . HOH R 8 .   ? 13.047 14.132  21.366  1.00 36.13  ?  101 HOH B O   1 
HETATM 6890 O O   . HOH R 8 .   ? 0.745  22.593  12.466  1.00 55.27  ?  102 HOH B O   1 
HETATM 6891 O O   . HOH R 8 .   ? 9.161  37.680  7.365   1.00 56.56  ?  103 HOH B O   1 
HETATM 6892 O O   . HOH R 8 .   ? 15.228 16.700  21.872  1.00 36.56  ?  104 HOH B O   1 
HETATM 6893 O O   . HOH R 8 .   ? 6.112  23.794  0.354   1.00 42.14  ?  105 HOH B O   1 
HETATM 6894 O O   . HOH R 8 .   ? 2.264  25.784  15.483  1.00 54.31  ?  106 HOH B O   1 
HETATM 6895 O O   . HOH R 8 .   ? 27.262 24.412  12.217  1.00 46.86  ?  107 HOH B O   1 
HETATM 6896 O O   . HOH R 8 .   ? 27.974 28.721  -3.091  1.00 49.86  ?  108 HOH B O   1 
HETATM 6897 O O   . HOH R 8 .   ? 15.878 17.318  17.940  1.00 44.54  ?  109 HOH B O   1 
HETATM 6898 O O   . HOH R 8 .   ? 12.969 20.295  22.139  1.00 40.21  ?  110 HOH B O   1 
HETATM 6899 O O   . HOH R 8 .   ? 15.718 20.527  -5.590  1.00 24.78  ?  111 HOH B O   1 
HETATM 6900 O O   . HOH R 8 .   ? 16.949 20.490  19.767  1.00 52.49  ?  112 HOH B O   1 
HETATM 6901 O O   . HOH R 8 .   ? 12.471 24.434  17.044  1.00 43.48  ?  113 HOH B O   1 
HETATM 6902 O O   . HOH R 8 .   ? 13.647 33.215  8.560   1.00 44.54  ?  114 HOH B O   1 
HETATM 6903 O O   . HOH R 8 .   ? 10.163 30.261  15.087  1.00 44.08  ?  115 HOH B O   1 
HETATM 6904 O O   . HOH R 8 .   ? 28.315 16.802  2.722   1.00 32.11  ?  116 HOH B O   1 
HETATM 6905 O O   . HOH R 8 .   ? 13.821 16.076  7.138   1.00 45.95  ?  117 HOH B O   1 
HETATM 6906 O O   . HOH R 8 .   ? 22.488 26.326  -5.966  1.00 31.25  ?  118 HOH B O   1 
HETATM 6907 O O   . HOH R 8 .   ? 15.840 34.597  4.073   1.00 48.33  ?  119 HOH B O   1 
HETATM 6908 O O   . HOH R 8 .   ? 4.491  29.179  15.100  1.00 46.58  ?  120 HOH B O   1 
HETATM 6909 O O   . HOH R 8 .   ? 13.786 15.200  18.008  1.00 46.13  ?  121 HOH B O   1 
HETATM 6910 O O   . HOH R 8 .   ? -0.317 30.855  8.494   1.00 49.44  ?  122 HOH B O   1 
HETATM 6911 O O   . HOH R 8 .   ? 40.503 18.619  -2.188  1.00 39.57  ?  123 HOH B O   1 
HETATM 6912 O O   . HOH R 8 .   ? 34.607 23.964  6.340   1.00 49.55  ?  124 HOH B O   1 
HETATM 6913 O O   . HOH R 8 .   ? 8.390  33.238  6.823   1.00 39.18  ?  125 HOH B O   1 
HETATM 6914 O O   . HOH R 8 .   ? 16.096 31.865  7.299   1.00 37.16  ?  126 HOH B O   1 
HETATM 6915 O O   . HOH R 8 .   ? 19.145 29.421  0.403   1.00 39.17  ?  127 HOH B O   1 
HETATM 6916 O O   . HOH R 8 .   ? 15.316 32.785  9.269   1.00 49.47  ?  128 HOH B O   1 
HETATM 6917 O O   . HOH R 8 .   ? 10.575 13.501  0.086   1.00 41.67  ?  129 HOH B O   1 
HETATM 6918 O O   . HOH R 8 .   ? 18.196 32.660  6.688   1.00 46.76  ?  130 HOH B O   1 
HETATM 6919 O O   . HOH R 8 .   ? 25.678 29.963  -5.355  1.00 46.35  ?  131 HOH B O   1 
HETATM 6920 O O   . HOH R 8 .   ? 18.059 14.467  5.702   1.00 48.59  ?  132 HOH B O   1 
HETATM 6921 O O   . HOH R 8 .   ? -6.577 26.292  8.189   1.00 57.61  ?  133 HOH B O   1 
HETATM 6922 O O   . HOH R 8 .   ? 29.261 9.823   -1.593  1.00 46.76  ?  134 HOH B O   1 
HETATM 6923 O O   . HOH R 8 .   ? 24.555 29.835  -10.137 1.00 38.67  ?  135 HOH B O   1 
HETATM 6924 O O   . HOH R 8 .   ? 15.583 12.525  -6.183  1.00 44.57  ?  136 HOH B O   1 
HETATM 6925 O O   . HOH R 8 .   ? 10.413 34.291  6.893   1.00 50.47  ?  137 HOH B O   1 
HETATM 6926 O O   . HOH R 8 .   ? 16.882 13.694  -4.185  1.00 45.13  ?  138 HOH B O   1 
HETATM 6927 O O   . HOH R 8 .   ? 26.413 15.666  7.160   1.00 53.42  ?  139 HOH B O   1 
HETATM 6928 O O   . HOH R 8 .   ? 20.037 20.460  17.552  1.00 49.16  ?  140 HOH B O   1 
HETATM 6929 O O   . HOH R 8 .   ? 23.426 29.140  -5.214  1.00 36.57  ?  141 HOH B O   1 
HETATM 6930 O O   . HOH R 8 .   ? 18.966 18.905  19.515  1.00 41.33  ?  142 HOH B O   1 
HETATM 6931 O O   . HOH R 8 .   ? 27.079 15.089  5.489   1.00 45.46  ?  143 HOH B O   1 
HETATM 6932 O O   . HOH R 8 .   ? 14.663 26.053  17.984  1.00 57.24  ?  144 HOH B O   1 
HETATM 6933 O O   . HOH R 8 .   ? 18.848 34.683  4.989   1.00 43.05  ?  145 HOH B O   1 
HETATM 6934 O O   . HOH S 8 .   ? 23.705 -37.006 -63.813 1.00 44.56  ?  401 HOH D O   1 
HETATM 6935 O O   . HOH S 8 .   ? 2.896  7.989   -47.321 1.00 35.36  ?  402 HOH D O   1 
HETATM 6936 O O   . HOH S 8 .   ? 17.292 1.544   -64.885 1.00 53.83  ?  403 HOH D O   1 
HETATM 6937 O O   . HOH S 8 .   ? 8.529  -36.459 -61.250 1.00 50.53  ?  404 HOH D O   1 
HETATM 6938 O O   . HOH S 8 .   ? 5.110  -12.395 -74.131 1.00 51.84  ?  405 HOH D O   1 
HETATM 6939 O O   . HOH S 8 .   ? 3.731  -23.757 -66.400 1.00 51.66  ?  406 HOH D O   1 
HETATM 6940 O O   . HOH S 8 .   ? 10.282 14.373  -31.542 1.00 37.60  ?  407 HOH D O   1 
HETATM 6941 O O   . HOH S 8 .   ? 16.377 -14.888 -80.983 1.00 40.37  ?  408 HOH D O   1 
HETATM 6942 O O   . HOH S 8 .   ? 29.560 -10.098 -69.992 1.00 39.08  ?  409 HOH D O   1 
HETATM 6943 O O   . HOH S 8 .   ? 3.258  10.598  -35.370 1.00 35.07  ?  410 HOH D O   1 
HETATM 6944 O O   . HOH S 8 .   ? 16.932 -16.536 -67.623 1.00 30.55  ?  411 HOH D O   1 
HETATM 6945 O O   . HOH S 8 .   ? 15.269 1.556   -33.230 1.00 32.24  ?  412 HOH D O   1 
HETATM 6946 O O   . HOH S 8 .   ? 7.496  8.271   -51.691 1.00 35.38  ?  413 HOH D O   1 
HETATM 6947 O O   . HOH S 8 .   ? 24.653 -11.038 -51.142 1.00 43.51  ?  414 HOH D O   1 
HETATM 6948 O O   . HOH S 8 .   ? 5.492  -24.784 -59.791 1.00 50.10  ?  415 HOH D O   1 
HETATM 6949 O O   . HOH S 8 .   ? 11.511 -28.460 -77.308 1.00 44.81  ?  416 HOH D O   1 
HETATM 6950 O O   . HOH S 8 .   ? 3.025  -26.717 -66.878 1.00 44.46  ?  417 HOH D O   1 
HETATM 6951 O O   . HOH S 8 .   ? 13.015 -33.716 -67.345 1.00 40.98  ?  418 HOH D O   1 
HETATM 6952 O O   . HOH S 8 .   ? 7.885  13.758  -33.663 1.00 34.16  ?  419 HOH D O   1 
HETATM 6953 O O   . HOH S 8 .   ? 0.424  10.839  -36.545 1.00 40.40  ?  420 HOH D O   1 
HETATM 6954 O O   . HOH S 8 .   ? 17.449 -0.307  -54.695 1.00 33.31  ?  421 HOH D O   1 
HETATM 6955 O O   . HOH S 8 .   ? 24.610 -5.954  -45.912 1.00 39.62  ?  422 HOH D O   1 
HETATM 6956 O O   . HOH S 8 .   ? 9.505  17.464  -46.557 1.00 44.56  ?  423 HOH D O   1 
HETATM 6957 O O   . HOH S 8 .   ? 6.672  -11.045 -50.833 1.00 40.06  ?  424 HOH D O   1 
HETATM 6958 O O   . HOH S 8 .   ? 15.762 -1.405  -37.095 1.00 34.66  ?  425 HOH D O   1 
HETATM 6959 O O   . HOH S 8 .   ? 7.012  -4.181  -32.182 1.00 40.38  ?  426 HOH D O   1 
HETATM 6960 O O   . HOH S 8 .   ? 24.525 -5.128  -67.431 1.00 51.33  ?  427 HOH D O   1 
HETATM 6961 O O   . HOH S 8 .   ? 2.754  -2.038  -49.288 1.00 38.29  ?  428 HOH D O   1 
HETATM 6962 O O   . HOH S 8 .   ? 8.967  8.083   -28.490 1.00 38.59  ?  429 HOH D O   1 
HETATM 6963 O O   . HOH S 8 .   ? 20.088 -37.642 -72.188 1.00 51.22  ?  430 HOH D O   1 
HETATM 6964 O O   . HOH S 8 .   ? 14.782 12.924  -42.949 1.00 40.11  ?  431 HOH D O   1 
HETATM 6965 O O   . HOH S 8 .   ? 8.903  10.330  -52.247 1.00 36.71  ?  432 HOH D O   1 
HETATM 6966 O O   . HOH S 8 .   ? 18.936 4.446   -62.539 1.00 36.73  ?  433 HOH D O   1 
HETATM 6967 O O   . HOH S 8 .   ? 6.312  5.967   -58.011 1.00 42.39  ?  434 HOH D O   1 
HETATM 6968 O O   . HOH S 8 .   ? 0.864  8.922   -28.092 1.00 48.41  ?  435 HOH D O   1 
HETATM 6969 O O   . HOH S 8 .   ? 3.862  -7.280  -46.092 1.00 40.80  ?  436 HOH D O   1 
HETATM 6970 O O   . HOH S 8 .   ? -0.235 -0.787  -39.125 1.00 39.97  ?  437 HOH D O   1 
HETATM 6971 O O   . HOH S 8 .   ? 0.845  -0.388  -46.458 1.00 34.02  ?  438 HOH D O   1 
HETATM 6972 O O   . HOH S 8 .   ? 14.641 -18.725 -78.320 1.00 39.38  ?  439 HOH D O   1 
HETATM 6973 O O   . HOH S 8 .   ? 7.788  17.664  -35.359 1.00 48.66  ?  440 HOH D O   1 
HETATM 6974 O O   . HOH S 8 .   ? 8.288  -32.324 -76.737 1.00 49.31  ?  441 HOH D O   1 
HETATM 6975 O O   . HOH S 8 .   ? 15.328 -12.439 -77.145 1.00 38.03  ?  442 HOH D O   1 
HETATM 6976 O O   . HOH S 8 .   ? 3.380  -22.265 -80.450 1.00 48.27  ?  443 HOH D O   1 
HETATM 6977 O O   . HOH S 8 .   ? 6.591  4.922   -62.743 1.00 38.85  ?  444 HOH D O   1 
HETATM 6978 O O   . HOH S 8 .   ? 16.055 14.422  -33.186 1.00 34.92  ?  445 HOH D O   1 
HETATM 6979 O O   . HOH S 8 .   ? 4.183  14.852  -42.467 1.00 45.20  ?  446 HOH D O   1 
HETATM 6980 O O   . HOH S 8 .   ? 13.413 -13.057 -72.785 1.00 28.16  ?  447 HOH D O   1 
HETATM 6981 O O   . HOH S 8 .   ? 10.513 -12.083 -45.911 1.00 35.39  ?  448 HOH D O   1 
HETATM 6982 O O   . HOH S 8 .   ? 14.690 -8.424  -62.172 1.00 40.24  ?  449 HOH D O   1 
HETATM 6983 O O   . HOH S 8 .   ? 18.116 -18.861 -71.766 1.00 29.66  ?  450 HOH D O   1 
HETATM 6984 O O   . HOH S 8 .   ? 12.571 8.872   -55.170 1.00 38.17  ?  451 HOH D O   1 
HETATM 6985 O O   . HOH S 8 .   ? 1.208  -15.395 -69.451 1.00 48.54  ?  452 HOH D O   1 
HETATM 6986 O O   . HOH S 8 .   ? 12.726 -9.301  -56.350 1.00 39.95  ?  453 HOH D O   1 
HETATM 6987 O O   . HOH S 8 .   ? 6.254  -1.429  -49.153 1.00 31.17  ?  454 HOH D O   1 
HETATM 6988 O O   . HOH S 8 .   ? 14.680 -36.445 -67.592 1.00 55.34  ?  455 HOH D O   1 
HETATM 6989 O O   . HOH S 8 .   ? 11.687 -21.206 -58.688 1.00 42.69  ?  456 HOH D O   1 
HETATM 6990 O O   . HOH S 8 .   ? 4.645  -4.877  -37.561 1.00 37.53  ?  457 HOH D O   1 
HETATM 6991 O O   . HOH S 8 .   ? 2.220  -15.402 -72.739 1.00 51.64  ?  458 HOH D O   1 
HETATM 6992 O O   . HOH S 8 .   ? 3.424  -30.048 -66.771 1.00 50.65  ?  459 HOH D O   1 
HETATM 6993 O O   . HOH S 8 .   ? 18.034 13.431  -46.469 1.00 40.49  ?  460 HOH D O   1 
HETATM 6994 O O   . HOH S 8 .   ? 9.756  -4.040  -68.938 1.00 45.79  ?  461 HOH D O   1 
HETATM 6995 O O   . HOH S 8 .   ? 15.252 -12.162 -74.389 1.00 33.99  ?  462 HOH D O   1 
HETATM 6996 O O   . HOH S 8 .   ? 15.433 15.215  -36.143 1.00 40.01  ?  463 HOH D O   1 
HETATM 6997 O O   . HOH S 8 .   ? 17.857 -11.890 -61.939 1.00 47.46  ?  464 HOH D O   1 
HETATM 6998 O O   . HOH S 8 .   ? 6.966  -24.343 -83.275 1.00 51.75  ?  465 HOH D O   1 
HETATM 6999 O O   . HOH S 8 .   ? 5.419  -26.632 -73.077 1.00 44.56  ?  466 HOH D O   1 
HETATM 7000 O O   . HOH S 8 .   ? 9.320  -17.528 -81.295 1.00 42.55  ?  467 HOH D O   1 
HETATM 7001 O O   . HOH S 8 .   ? 20.713 7.218   -46.576 1.00 43.71  ?  468 HOH D O   1 
HETATM 7002 O O   . HOH S 8 .   ? 7.710  -12.920 -49.556 1.00 33.76  ?  469 HOH D O   1 
HETATM 7003 O O   . HOH S 8 .   ? 3.392  -5.719  -42.789 1.00 49.89  ?  470 HOH D O   1 
HETATM 7004 O O   . HOH S 8 .   ? 9.278  2.400   -26.740 1.00 34.30  ?  471 HOH D O   1 
HETATM 7005 O O   . HOH S 8 .   ? 17.124 -14.580 -78.450 1.00 41.37  ?  472 HOH D O   1 
HETATM 7006 O O   . HOH S 8 .   ? 2.330  4.671   -47.609 1.00 35.29  ?  473 HOH D O   1 
HETATM 7007 O O   . HOH S 8 .   ? 2.459  -4.873  -59.640 1.00 38.02  ?  474 HOH D O   1 
HETATM 7008 O O   . HOH S 8 .   ? 17.032 -16.777 -70.366 1.00 28.92  ?  475 HOH D O   1 
HETATM 7009 O O   . HOH S 8 .   ? 5.866  -19.907 -60.526 1.00 52.85  ?  476 HOH D O   1 
HETATM 7010 O O   . HOH S 8 .   ? 0.546  -5.288  -39.891 1.00 45.66  ?  477 HOH D O   1 
HETATM 7011 O O   . HOH S 8 .   ? 14.657 18.207  -41.747 1.00 44.12  ?  478 HOH D O   1 
HETATM 7012 O O   . HOH S 8 .   ? 21.185 4.538   -49.530 1.00 48.84  ?  479 HOH D O   1 
HETATM 7013 O O   . HOH S 8 .   ? 14.742 -10.776 -52.018 1.00 36.79  ?  480 HOH D O   1 
HETATM 7014 O O   . HOH S 8 .   ? 3.917  6.800   -25.756 1.00 45.45  ?  481 HOH D O   1 
HETATM 7015 O O   . HOH S 8 .   ? 6.554  -13.353 -75.334 1.00 43.75  ?  482 HOH D O   1 
HETATM 7016 O O   . HOH S 8 .   ? -1.592 4.432   -40.647 1.00 39.93  ?  483 HOH D O   1 
HETATM 7017 O O   . HOH S 8 .   ? -0.464 -0.343  -50.337 1.00 43.07  ?  484 HOH D O   1 
HETATM 7018 O O   . HOH S 8 .   ? 4.680  8.885   -52.045 1.00 37.44  ?  485 HOH D O   1 
HETATM 7019 O O   . HOH S 8 .   ? 5.538  -9.899  -48.267 1.00 43.84  ?  486 HOH D O   1 
HETATM 7020 O O   . HOH S 8 .   ? 21.307 -11.211 -54.393 1.00 33.00  ?  487 HOH D O   1 
HETATM 7021 O O   . HOH S 8 .   ? 10.876 -33.794 -74.882 1.00 50.34  ?  488 HOH D O   1 
HETATM 7022 O O   . HOH S 8 .   ? 15.307 -12.929 -61.866 1.00 32.29  ?  489 HOH D O   1 
HETATM 7023 O O   . HOH S 8 .   ? 22.321 -35.936 -60.615 1.00 37.54  ?  490 HOH D O   1 
HETATM 7024 O O   . HOH S 8 .   ? 7.442  -27.356 -59.054 1.00 44.69  ?  491 HOH D O   1 
HETATM 7025 O O   . HOH S 8 .   ? 9.278  -7.003  -71.893 1.00 45.23  ?  492 HOH D O   1 
HETATM 7026 O O   . HOH S 8 .   ? 15.441 -28.790 -78.394 1.00 37.18  ?  493 HOH D O   1 
HETATM 7027 O O   . HOH S 8 .   ? 3.532  2.051   -57.109 1.00 43.50  ?  494 HOH D O   1 
HETATM 7028 O O   . HOH S 8 .   ? 16.294 -4.171  -69.939 1.00 45.91  ?  495 HOH D O   1 
HETATM 7029 O O   . HOH S 8 .   ? 31.394 -12.087 -70.597 1.00 47.52  ?  496 HOH D O   1 
HETATM 7030 O O   . HOH S 8 .   ? 22.311 -3.044  -67.878 1.00 56.55  ?  497 HOH D O   1 
HETATM 7031 O O   . HOH S 8 .   ? 21.329 6.158   -51.754 1.00 51.38  ?  498 HOH D O   1 
HETATM 7032 O O   . HOH S 8 .   ? 7.927  7.141   -63.403 1.00 49.27  ?  499 HOH D O   1 
HETATM 7033 O O   . HOH S 8 .   ? 18.495 10.366  -43.785 1.00 42.11  ?  500 HOH D O   1 
HETATM 7034 O O   . HOH S 8 .   ? 19.702 -34.391 -62.167 1.00 35.63  ?  501 HOH D O   1 
HETATM 7035 O O   . HOH S 8 .   ? 2.726  -6.841  -39.175 1.00 51.45  ?  502 HOH D O   1 
HETATM 7036 O O   . HOH S 8 .   ? 16.925 12.999  -43.428 1.00 44.48  ?  503 HOH D O   1 
HETATM 7037 O O   . HOH S 8 .   ? 22.130 1.215   -52.476 1.00 54.58  ?  504 HOH D O   1 
HETATM 7038 O O   . HOH S 8 .   ? 7.862  0.160   -26.612 1.00 41.94  ?  505 HOH D O   1 
HETATM 7039 O O   . HOH S 8 .   ? 27.865 -11.336 -72.965 1.00 38.84  ?  506 HOH D O   1 
HETATM 7040 O O   . HOH S 8 .   ? 2.629  8.334   -50.472 1.00 37.40  ?  507 HOH D O   1 
HETATM 7041 O O   . HOH S 8 .   ? 17.154 -9.095  -61.823 1.00 44.46  ?  508 HOH D O   1 
HETATM 7042 O O   . HOH S 8 .   ? 26.205 -12.182 -50.681 1.00 52.11  ?  509 HOH D O   1 
HETATM 7043 O O   . HOH S 8 .   ? 1.023  15.998  -37.713 1.00 46.36  ?  510 HOH D O   1 
HETATM 7044 O O   . HOH S 8 .   ? 11.175 10.700  -56.990 1.00 55.65  ?  511 HOH D O   1 
HETATM 7045 O O   . HOH S 8 .   ? 0.275  13.648  -35.824 1.00 50.16  ?  512 HOH D O   1 
HETATM 7046 O O   . HOH S 8 .   ? 6.191  16.781  -41.346 1.00 51.68  ?  513 HOH D O   1 
HETATM 7047 O O   . HOH S 8 .   ? 18.173 15.404  -42.460 1.00 51.11  ?  514 HOH D O   1 
HETATM 7048 O O   . HOH S 8 .   ? 5.267  -2.394  -69.574 1.00 49.86  ?  515 HOH D O   1 
HETATM 7049 O O   . HOH S 8 .   ? 23.219 -1.540  -52.642 1.00 52.51  ?  516 HOH D O   1 
HETATM 7050 O O   . HOH S 8 .   ? 0.761  -30.306 -67.179 1.00 55.22  ?  517 HOH D O   1 
HETATM 7051 O O   . HOH S 8 .   ? 13.506 12.210  -58.453 1.00 60.06  ?  518 HOH D O   1 
HETATM 7052 O O   . HOH S 8 .   ? 17.097 -35.009 -61.986 1.00 41.49  ?  519 HOH D O   1 
HETATM 7053 O O   . HOH S 8 .   ? 7.124  8.617   -58.771 1.00 46.45  ?  520 HOH D O   1 
HETATM 7054 O O   . HOH S 8 .   ? -4.078 -0.604  -42.442 1.00 43.38  ?  521 HOH D O   1 
HETATM 7055 O O   . HOH S 8 .   ? -1.272 0.810   -47.653 1.00 38.39  ?  522 HOH D O   1 
HETATM 7056 O O   . HOH S 8 .   ? 3.547  -0.425  -64.638 1.00 48.91  ?  523 HOH D O   1 
HETATM 7057 O O   . HOH S 8 .   ? 5.415  1.781   -65.798 1.00 38.86  ?  524 HOH D O   1 
HETATM 7058 O O   . HOH S 8 .   ? 4.596  4.096   -64.382 1.00 47.35  ?  525 HOH D O   1 
HETATM 7059 O O   . HOH S 8 .   ? 13.943 -13.060 -55.119 1.00 37.03  ?  526 HOH D O   1 
HETATM 7060 O O   . HOH S 8 .   ? 5.268  1.567   -68.297 1.00 48.27  ?  527 HOH D O   1 
HETATM 7061 O O   . HOH S 8 .   ? 14.826 -12.055 -57.479 1.00 50.77  ?  528 HOH D O   1 
HETATM 7062 O O   . HOH S 8 .   ? 9.643  9.729   -59.327 1.00 49.68  ?  529 HOH D O   1 
HETATM 7063 O O   . HOH T 8 .   ? 26.376 -29.023 -78.841 1.00 54.99  ?  401 HOH E O   1 
HETATM 7064 O O   . HOH T 8 .   ? 11.455 -25.030 -46.853 1.00 47.33  ?  402 HOH E O   1 
HETATM 7065 O O   . HOH T 8 .   ? 35.389 2.884   -27.465 1.00 52.94  ?  403 HOH E O   1 
HETATM 7066 O O   . HOH T 8 .   ? 15.438 -14.180 -22.650 1.00 30.52  ?  404 HOH E O   1 
HETATM 7067 O O   . HOH T 8 .   ? 27.060 -25.839 -82.491 1.00 47.51  ?  405 HOH E O   1 
HETATM 7068 O O   . HOH T 8 .   ? 36.024 -3.944  -39.921 1.00 50.61  ?  406 HOH E O   1 
HETATM 7069 O O   . HOH T 8 .   ? 26.050 -33.761 -65.307 1.00 29.83  ?  407 HOH E O   1 
HETATM 7070 O O   . HOH T 8 .   ? 34.202 -33.820 -66.480 1.00 53.93  ?  408 HOH E O   1 
HETATM 7071 O O   . HOH T 8 .   ? 20.900 -27.322 -30.365 1.00 33.81  ?  409 HOH E O   1 
HETATM 7072 O O   . HOH T 8 .   ? 19.587 -42.295 -44.204 1.00 51.59  ?  410 HOH E O   1 
HETATM 7073 O O   . HOH T 8 .   ? 13.227 -2.668  -25.092 1.00 41.82  ?  411 HOH E O   1 
HETATM 7074 O O   . HOH T 8 .   ? 28.295 1.342   -21.498 1.00 41.89  ?  412 HOH E O   1 
HETATM 7075 O O   . HOH T 8 .   ? 23.253 -26.440 -83.750 1.00 42.91  ?  413 HOH E O   1 
HETATM 7076 O O   . HOH T 8 .   ? 16.831 -34.917 -39.646 1.00 32.32  ?  414 HOH E O   1 
HETATM 7077 O O   . HOH T 8 .   ? 32.215 -21.693 -83.788 1.00 38.58  ?  415 HOH E O   1 
HETATM 7078 O O   . HOH T 8 .   ? 28.948 -34.321 -72.727 1.00 49.91  ?  416 HOH E O   1 
HETATM 7079 O O   . HOH T 8 .   ? 18.807 -36.071 -56.426 1.00 42.59  ?  417 HOH E O   1 
HETATM 7080 O O   . HOH T 8 .   ? 30.714 -8.639  -25.442 1.00 27.17  ?  418 HOH E O   1 
HETATM 7081 O O   . HOH T 8 .   ? 23.463 -1.957  -44.256 1.00 23.42  ?  419 HOH E O   1 
HETATM 7082 O O   . HOH T 8 .   ? 18.601 -7.835  -20.780 1.00 45.51  ?  420 HOH E O   1 
HETATM 7083 O O   . HOH T 8 .   ? 12.591 -28.730 -42.523 1.00 49.48  ?  421 HOH E O   1 
HETATM 7084 O O   . HOH T 8 .   ? 37.327 -32.401 -64.120 1.00 40.53  ?  422 HOH E O   1 
HETATM 7085 O O   . HOH T 8 .   ? 26.130 -35.134 -62.624 1.00 32.13  ?  423 HOH E O   1 
HETATM 7086 O O   . HOH T 8 .   ? 26.022 -35.995 -53.380 1.00 28.78  ?  424 HOH E O   1 
HETATM 7087 O O   . HOH T 8 .   ? 35.180 -25.022 -82.481 1.00 34.61  ?  425 HOH E O   1 
HETATM 7088 O O   . HOH T 8 .   ? 23.183 -8.968  -44.411 1.00 34.41  ?  426 HOH E O   1 
HETATM 7089 O O   . HOH T 8 .   ? 31.069 -33.972 -52.094 1.00 29.17  ?  427 HOH E O   1 
HETATM 7090 O O   . HOH T 8 .   ? 32.142 -5.321  -18.953 1.00 40.00  ?  428 HOH E O   1 
HETATM 7091 O O   . HOH T 8 .   ? 36.615 -25.135 -62.310 1.00 25.49  ?  429 HOH E O   1 
HETATM 7092 O O   . HOH T 8 .   ? 28.192 -5.857  -42.380 1.00 36.88  ?  430 HOH E O   1 
HETATM 7093 O O   . HOH T 8 .   ? 24.069 -18.563 -58.304 1.00 32.18  ?  431 HOH E O   1 
HETATM 7094 O O   . HOH T 8 .   ? 11.791 -29.617 -46.151 1.00 41.49  ?  432 HOH E O   1 
HETATM 7095 O O   . HOH T 8 .   ? 31.548 1.370   -23.446 1.00 52.31  ?  433 HOH E O   1 
HETATM 7096 O O   . HOH T 8 .   ? 15.483 -35.052 -30.097 1.00 49.68  ?  434 HOH E O   1 
HETATM 7097 O O   . HOH T 8 .   ? 27.562 5.701   -43.458 1.00 42.65  ?  435 HOH E O   1 
HETATM 7098 O O   . HOH T 8 .   ? 10.607 -6.420  -33.557 1.00 25.52  ?  436 HOH E O   1 
HETATM 7099 O O   . HOH T 8 .   ? 34.613 -31.350 -75.827 1.00 35.88  ?  437 HOH E O   1 
HETATM 7100 O O   . HOH T 8 .   ? 36.190 -23.262 -57.288 1.00 36.24  ?  438 HOH E O   1 
HETATM 7101 O O   . HOH T 8 .   ? 24.806 -30.124 -34.708 1.00 38.97  ?  439 HOH E O   1 
HETATM 7102 O O   . HOH T 8 .   ? 30.299 -21.040 -34.170 1.00 31.86  ?  440 HOH E O   1 
HETATM 7103 O O   . HOH T 8 .   ? 14.022 -32.919 -58.379 1.00 35.72  ?  441 HOH E O   1 
HETATM 7104 O O   . HOH T 8 .   ? 20.996 1.250   -35.809 1.00 31.89  ?  442 HOH E O   1 
HETATM 7105 O O   . HOH T 8 .   ? 29.129 -22.448 -54.818 1.00 19.91  ?  443 HOH E O   1 
HETATM 7106 O O   . HOH T 8 .   ? 14.084 -22.826 -26.351 1.00 39.67  ?  444 HOH E O   1 
HETATM 7107 O O   . HOH T 8 .   ? 22.801 7.260   -44.753 1.00 51.77  ?  445 HOH E O   1 
HETATM 7108 O O   . HOH T 8 .   ? 21.139 -9.345  -20.746 1.00 38.27  ?  446 HOH E O   1 
HETATM 7109 O O   . HOH T 8 .   ? 10.045 -13.131 -38.699 1.00 33.54  ?  447 HOH E O   1 
HETATM 7110 O O   . HOH T 8 .   ? 34.358 -4.971  -38.258 1.00 38.64  ?  448 HOH E O   1 
HETATM 7111 O O   . HOH T 8 .   ? 14.073 -18.879 -61.232 1.00 39.27  ?  449 HOH E O   1 
HETATM 7112 O O   . HOH T 8 .   ? 23.875 -26.209 -42.577 1.00 28.13  ?  450 HOH E O   1 
HETATM 7113 O O   . HOH T 8 .   ? 38.921 -22.375 -60.108 1.00 34.69  ?  451 HOH E O   1 
HETATM 7114 O O   . HOH T 8 .   ? 28.156 -36.569 -51.794 1.00 33.81  ?  452 HOH E O   1 
HETATM 7115 O O   . HOH T 8 .   ? 20.811 6.378   -40.624 1.00 34.13  ?  453 HOH E O   1 
HETATM 7116 O O   . HOH T 8 .   ? 32.436 4.600   -30.528 1.00 34.32  ?  454 HOH E O   1 
HETATM 7117 O O   . HOH T 8 .   ? 37.186 -30.571 -74.904 1.00 32.05  ?  455 HOH E O   1 
HETATM 7118 O O   . HOH T 8 .   ? 28.315 -14.410 -22.682 1.00 33.27  ?  456 HOH E O   1 
HETATM 7119 O O   . HOH T 8 .   ? 40.003 -23.711 -79.672 1.00 38.97  ?  457 HOH E O   1 
HETATM 7120 O O   . HOH T 8 .   ? 34.294 -2.775  -31.900 1.00 29.85  ?  458 HOH E O   1 
HETATM 7121 O O   . HOH T 8 .   ? 28.383 -17.914 -60.149 1.00 29.39  ?  459 HOH E O   1 
HETATM 7122 O O   . HOH T 8 .   ? 27.761 -24.927 -38.133 1.00 37.20  ?  460 HOH E O   1 
HETATM 7123 O O   . HOH T 8 .   ? 10.901 -12.157 -21.192 1.00 44.55  ?  461 HOH E O   1 
HETATM 7124 O O   . HOH T 8 .   ? 19.772 -42.031 -42.141 1.00 60.30  ?  462 HOH E O   1 
HETATM 7125 O O   . HOH T 8 .   ? 19.276 -18.793 -23.821 1.00 29.19  ?  463 HOH E O   1 
HETATM 7126 O O   . HOH T 8 .   ? 43.283 -23.092 -82.043 1.00 36.98  ?  464 HOH E O   1 
HETATM 7127 O O   . HOH T 8 .   ? 29.759 5.989   -30.623 1.00 36.79  ?  465 HOH E O   1 
HETATM 7128 O O   . HOH T 8 .   ? 28.531 -34.780 -59.690 1.00 33.94  ?  466 HOH E O   1 
HETATM 7129 O O   . HOH T 8 .   ? 8.801  -6.563  -35.823 1.00 33.01  ?  467 HOH E O   1 
HETATM 7130 O O   . HOH T 8 .   ? 36.913 -17.639 -70.515 1.00 35.35  ?  468 HOH E O   1 
HETATM 7131 O O   . HOH T 8 .   ? 26.333 -26.258 -29.536 1.00 42.44  ?  469 HOH E O   1 
HETATM 7132 O O   . HOH T 8 .   ? 22.829 -12.203 -65.202 1.00 26.49  ?  470 HOH E O   1 
HETATM 7133 O O   . HOH T 8 .   ? 19.675 -25.082 -74.554 1.00 39.45  ?  471 HOH E O   1 
HETATM 7134 O O   . HOH T 8 .   ? 27.636 -12.845 -70.623 1.00 36.40  ?  472 HOH E O   1 
HETATM 7135 O O   . HOH T 8 .   ? 20.895 -33.095 -60.046 1.00 20.35  ?  473 HOH E O   1 
HETATM 7136 O O   . HOH T 8 .   ? 24.070 4.677   -28.233 1.00 31.14  ?  474 HOH E O   1 
HETATM 7137 O O   . HOH T 8 .   ? 27.157 -22.313 -26.412 1.00 36.26  ?  475 HOH E O   1 
HETATM 7138 O O   . HOH T 8 .   ? 27.815 -18.756 -24.451 1.00 30.46  ?  476 HOH E O   1 
HETATM 7139 O O   . HOH T 8 .   ? 19.331 11.024  -36.042 1.00 38.78  ?  477 HOH E O   1 
HETATM 7140 O O   . HOH T 8 .   ? 26.660 3.799   -37.798 1.00 28.10  ?  478 HOH E O   1 
HETATM 7141 O O   . HOH T 8 .   ? 29.578 -15.612 -68.438 1.00 27.64  ?  479 HOH E O   1 
HETATM 7142 O O   . HOH T 8 .   ? 26.250 -22.166 -84.688 1.00 44.63  ?  480 HOH E O   1 
HETATM 7143 O O   . HOH T 8 .   ? 15.566 -22.272 -85.984 1.00 40.30  ?  481 HOH E O   1 
HETATM 7144 O O   . HOH T 8 .   ? 20.199 -1.932  -24.823 1.00 24.47  ?  482 HOH E O   1 
HETATM 7145 O O   . HOH T 8 .   ? 39.616 -32.381 -39.299 1.00 38.64  ?  483 HOH E O   1 
HETATM 7146 O O   . HOH T 8 .   ? 19.563 7.786   -43.323 1.00 40.05  ?  484 HOH E O   1 
HETATM 7147 O O   . HOH T 8 .   ? 28.048 -15.286 -70.670 1.00 32.22  ?  485 HOH E O   1 
HETATM 7148 O O   . HOH T 8 .   ? 18.336 7.002   -36.793 1.00 40.20  ?  486 HOH E O   1 
HETATM 7149 O O   . HOH T 8 .   ? 19.454 -27.505 -84.985 1.00 49.20  ?  487 HOH E O   1 
HETATM 7150 O O   . HOH T 8 .   ? 16.639 -21.778 -25.383 1.00 36.07  ?  488 HOH E O   1 
HETATM 7151 O O   . HOH T 8 .   ? 12.930 -36.347 -52.799 1.00 40.34  ?  489 HOH E O   1 
HETATM 7152 O O   . HOH T 8 .   ? 20.808 -15.340 -59.928 1.00 32.05  ?  490 HOH E O   1 
HETATM 7153 O O   . HOH T 8 .   ? 22.862 -20.242 -54.651 1.00 26.53  ?  491 HOH E O   1 
HETATM 7154 O O   . HOH T 8 .   ? 15.902 -17.991 -85.722 1.00 50.95  ?  492 HOH E O   1 
HETATM 7155 O O   . HOH T 8 .   ? 29.954 -13.363 -40.992 1.00 36.55  ?  493 HOH E O   1 
HETATM 7156 O O   . HOH T 8 .   ? 31.000 -13.735 -35.065 1.00 35.47  ?  494 HOH E O   1 
HETATM 7157 O O   . HOH T 8 .   ? 34.822 -8.923  -36.330 1.00 46.48  ?  495 HOH E O   1 
HETATM 7158 O O   . HOH T 8 .   ? 31.732 -17.145 -43.227 1.00 47.63  ?  496 HOH E O   1 
HETATM 7159 O O   . HOH T 8 .   ? 13.674 -23.634 -57.477 1.00 37.07  ?  497 HOH E O   1 
HETATM 7160 O O   . HOH T 8 .   ? 9.391  -25.617 -30.872 1.00 36.32  ?  498 HOH E O   1 
HETATM 7161 O O   . HOH T 8 .   ? 8.312  -25.897 -53.448 1.00 43.83  ?  499 HOH E O   1 
HETATM 7162 O O   . HOH T 8 .   ? 24.507 -39.557 -47.318 1.00 46.08  ?  500 HOH E O   1 
HETATM 7163 O O   . HOH T 8 .   ? 19.362 11.234  -31.859 1.00 37.05  ?  501 HOH E O   1 
HETATM 7164 O O   . HOH T 8 .   ? 11.748 -35.321 -50.450 1.00 34.72  ?  502 HOH E O   1 
HETATM 7165 O O   . HOH T 8 .   ? 15.920 -36.544 -55.095 1.00 45.85  ?  503 HOH E O   1 
HETATM 7166 O O   . HOH T 8 .   ? 16.774 -23.742 -42.314 1.00 31.43  ?  504 HOH E O   1 
HETATM 7167 O O   . HOH T 8 .   ? 20.330 -27.298 -22.476 1.00 40.72  ?  505 HOH E O   1 
HETATM 7168 O O   . HOH T 8 .   ? 35.863 -23.930 -64.905 1.00 24.59  ?  506 HOH E O   1 
HETATM 7169 O O   . HOH T 8 .   ? 29.650 -12.544 -30.015 1.00 20.96  ?  507 HOH E O   1 
HETATM 7170 O O   . HOH T 8 .   ? 11.683 -20.417 -39.904 1.00 43.20  ?  508 HOH E O   1 
HETATM 7171 O O   . HOH T 8 .   ? 33.315 -36.867 -39.750 1.00 45.62  ?  509 HOH E O   1 
HETATM 7172 O O   . HOH T 8 .   ? 6.871  -18.249 -41.870 1.00 41.34  ?  510 HOH E O   1 
HETATM 7173 O O   . HOH T 8 .   ? 25.135 -3.952  -44.026 1.00 31.35  ?  511 HOH E O   1 
HETATM 7174 O O   . HOH T 8 .   ? 33.929 -8.033  -38.315 1.00 40.66  ?  512 HOH E O   1 
HETATM 7175 O O   . HOH T 8 .   ? 25.183 5.433   -35.828 1.00 27.50  ?  513 HOH E O   1 
HETATM 7176 O O   . HOH T 8 .   ? 29.760 -20.892 -52.260 1.00 36.19  ?  514 HOH E O   1 
HETATM 7177 O O   . HOH T 8 .   ? 37.019 -16.388 -59.794 1.00 32.04  ?  515 HOH E O   1 
HETATM 7178 O O   . HOH T 8 .   ? 14.144 -14.902 -45.150 1.00 41.10  ?  516 HOH E O   1 
HETATM 7179 O O   . HOH T 8 .   ? 33.245 -27.673 -48.539 1.00 30.43  ?  517 HOH E O   1 
HETATM 7180 O O   . HOH T 8 .   ? 35.572 -26.799 -55.617 0.50 40.59  ?  518 HOH E O   1 
HETATM 7181 O O   . HOH T 8 .   ? 16.575 -21.568 -40.900 1.00 32.02  ?  519 HOH E O   1 
HETATM 7182 O O   . HOH T 8 .   ? 32.705 -31.932 -82.092 1.00 51.17  ?  520 HOH E O   1 
HETATM 7183 O O   . HOH T 8 .   ? 25.382 -7.730  -44.985 1.00 36.57  ?  521 HOH E O   1 
HETATM 7184 O O   . HOH T 8 .   ? 14.405 -33.537 -40.346 1.00 38.54  ?  522 HOH E O   1 
HETATM 7185 O O   . HOH T 8 .   ? 31.287 3.505   -38.352 1.00 43.38  ?  523 HOH E O   1 
HETATM 7186 O O   . HOH T 8 .   ? 35.714 -4.248  -27.957 1.00 36.08  ?  524 HOH E O   1 
HETATM 7187 O O   . HOH T 8 .   ? 34.283 -21.465 -81.601 1.00 38.39  ?  525 HOH E O   1 
HETATM 7188 O O   . HOH T 8 .   ? 26.398 -26.277 -41.523 1.00 36.19  ?  526 HOH E O   1 
HETATM 7189 O O   . HOH T 8 .   ? 24.989 -4.733  -16.710 1.00 51.34  ?  527 HOH E O   1 
HETATM 7190 O O   . HOH T 8 .   ? 33.889 -31.310 -50.671 1.00 34.32  ?  528 HOH E O   1 
HETATM 7191 O O   . HOH T 8 .   ? 23.322 -30.984 -32.393 1.00 36.17  ?  529 HOH E O   1 
HETATM 7192 O O   . HOH T 8 .   ? 4.426  -34.077 -51.798 1.00 42.46  ?  530 HOH E O   1 
HETATM 7193 O O   . HOH T 8 .   ? 12.582 -32.271 -36.129 1.00 40.35  ?  531 HOH E O   1 
HETATM 7194 O O   . HOH T 8 .   ? 30.051 -28.363 -32.004 1.00 40.22  ?  532 HOH E O   1 
HETATM 7195 O O   . HOH T 8 .   ? 11.405 -4.722  -29.920 1.00 34.28  ?  533 HOH E O   1 
HETATM 7196 O O   . HOH T 8 .   ? 30.234 -19.935 -40.509 1.00 27.68  ?  534 HOH E O   1 
HETATM 7197 O O   . HOH T 8 .   ? 36.155 -19.132 -76.906 1.00 29.30  ?  535 HOH E O   1 
HETATM 7198 O O   . HOH T 8 .   ? 26.395 -35.242 -58.234 1.00 23.47  ?  536 HOH E O   1 
HETATM 7199 O O   . HOH T 8 .   ? 25.704 -27.657 -38.915 1.00 32.17  ?  537 HOH E O   1 
HETATM 7200 O O   . HOH T 8 .   ? 10.946 -19.444 -30.712 1.00 35.77  ?  538 HOH E O   1 
HETATM 7201 O O   . HOH T 8 .   ? 26.208 -7.938  -20.294 1.00 40.80  ?  539 HOH E O   1 
HETATM 7202 O O   . HOH T 8 .   ? 27.779 -28.093 -80.294 1.00 50.98  ?  540 HOH E O   1 
HETATM 7203 O O   . HOH T 8 .   ? 18.537 2.130   -34.609 1.00 52.37  ?  541 HOH E O   1 
HETATM 7204 O O   . HOH T 8 .   ? 29.811 -10.327 -24.283 1.00 31.62  ?  542 HOH E O   1 
HETATM 7205 O O   . HOH T 8 .   ? 31.048 -41.029 -43.849 1.00 50.08  ?  543 HOH E O   1 
HETATM 7206 O O   . HOH T 8 .   ? 33.811 3.781   -36.432 1.00 50.38  ?  544 HOH E O   1 
HETATM 7207 O O   . HOH T 8 .   ? 28.340 -37.290 -47.805 1.00 33.67  ?  545 HOH E O   1 
HETATM 7208 O O   . HOH T 8 .   ? 23.936 -50.898 -39.150 1.00 57.49  ?  546 HOH E O   1 
HETATM 7209 O O   . HOH T 8 .   ? 7.057  -13.173 -36.873 1.00 46.90  ?  547 HOH E O   1 
HETATM 7210 O O   . HOH T 8 .   ? 14.547 -5.038  -21.101 1.00 43.39  ?  548 HOH E O   1 
HETATM 7211 O O   . HOH T 8 .   ? 30.007 -19.937 -30.590 1.00 37.08  ?  549 HOH E O   1 
HETATM 7212 O O   . HOH T 8 .   ? 36.005 -16.980 -67.401 1.00 44.39  ?  550 HOH E O   1 
HETATM 7213 O O   . HOH T 8 .   ? 35.426 -15.937 -57.231 1.00 39.20  ?  551 HOH E O   1 
HETATM 7214 O O   . HOH T 8 .   ? 22.825 -40.753 -36.948 1.00 55.01  ?  552 HOH E O   1 
HETATM 7215 O O   . HOH T 8 .   ? 31.705 -33.310 -57.120 1.00 31.06  ?  553 HOH E O   1 
HETATM 7216 O O   . HOH T 8 .   ? 31.600 -13.768 -68.160 1.00 44.14  ?  554 HOH E O   1 
HETATM 7217 O O   . HOH T 8 .   ? 10.249 -21.907 -36.704 1.00 38.80  ?  555 HOH E O   1 
HETATM 7218 O O   . HOH T 8 .   ? 12.019 -15.038 -46.548 1.00 43.70  ?  556 HOH E O   1 
HETATM 7219 O O   . HOH T 8 .   ? 22.843 -28.634 -23.528 1.00 38.34  ?  557 HOH E O   1 
HETATM 7220 O O   . HOH T 8 .   ? 19.245 4.871   -39.182 1.00 40.54  ?  558 HOH E O   1 
HETATM 7221 O O   . HOH T 8 .   ? 34.811 -3.596  -21.904 1.00 39.71  ?  559 HOH E O   1 
HETATM 7222 O O   . HOH T 8 .   ? 14.081 -27.441 -26.165 1.00 41.52  ?  560 HOH E O   1 
HETATM 7223 O O   . HOH T 8 .   ? 32.256 2.648   -40.832 1.00 54.35  ?  561 HOH E O   1 
HETATM 7224 O O   . HOH T 8 .   ? 21.022 -37.398 -34.845 1.00 45.40  ?  562 HOH E O   1 
HETATM 7225 O O   . HOH T 8 .   ? 20.645 -31.089 -79.090 1.00 46.42  ?  563 HOH E O   1 
HETATM 7226 O O   . HOH T 8 .   ? 25.699 -34.292 -32.987 1.00 55.90  ?  564 HOH E O   1 
HETATM 7227 O O   . HOH T 8 .   ? 12.339 -27.692 -37.411 1.00 48.03  ?  565 HOH E O   1 
HETATM 7228 O O   . HOH T 8 .   ? 28.292 5.063   -40.631 1.00 43.57  ?  566 HOH E O   1 
HETATM 7229 O O   . HOH T 8 .   ? 20.148 -11.631 -21.654 1.00 30.53  ?  567 HOH E O   1 
HETATM 7230 O O   . HOH T 8 .   ? 29.799 -15.585 -74.419 1.00 30.83  ?  568 HOH E O   1 
HETATM 7231 O O   . HOH T 8 .   ? 13.335 -40.163 -36.862 1.00 55.67  ?  569 HOH E O   1 
HETATM 7232 O O   . HOH T 8 .   ? 35.383 -14.364 -64.769 1.00 45.16  ?  570 HOH E O   1 
HETATM 7233 O O   . HOH T 8 .   ? 22.773 -1.564  -17.379 1.00 39.00  ?  571 HOH E O   1 
HETATM 7234 O O   . HOH T 8 .   ? 31.530 -38.312 -45.220 1.00 39.32  ?  572 HOH E O   1 
HETATM 7235 O O   . HOH T 8 .   ? 27.708 -17.028 -81.460 1.00 36.11  ?  573 HOH E O   1 
HETATM 7236 O O   . HOH T 8 .   ? 23.782 4.473   -45.897 1.00 49.97  ?  574 HOH E O   1 
HETATM 7237 O O   . HOH T 8 .   ? 34.194 0.532   -24.103 1.00 44.75  ?  575 HOH E O   1 
HETATM 7238 O O   . HOH T 8 .   ? 31.453 -18.897 -32.690 1.00 39.21  ?  576 HOH E O   1 
HETATM 7239 O O   . HOH T 8 .   ? 6.422  -18.110 -39.227 1.00 50.21  ?  577 HOH E O   1 
HETATM 7240 O O   . HOH T 8 .   ? 16.219 -24.538 -84.470 1.00 48.02  ?  578 HOH E O   1 
HETATM 7241 O O   . HOH T 8 .   ? 24.501 -24.881 -85.122 1.00 42.18  ?  579 HOH E O   1 
HETATM 7242 O O   . HOH T 8 .   ? 37.632 -10.078 -28.445 1.00 50.56  ?  580 HOH E O   1 
HETATM 7243 O O   . HOH T 8 .   ? 11.756 -29.472 -36.747 1.00 44.83  ?  581 HOH E O   1 
HETATM 7244 O O   . HOH T 8 .   ? 16.887 -18.612 -22.479 1.00 35.29  ?  582 HOH E O   1 
HETATM 7245 O O   . HOH T 8 .   ? 39.114 -9.985  -30.282 1.00 49.57  ?  583 HOH E O   1 
HETATM 7246 O O   . HOH T 8 .   ? 34.435 5.538   -31.662 1.00 45.73  ?  584 HOH E O   1 
HETATM 7247 O O   . HOH T 8 .   ? 9.635  -24.136 -37.352 1.00 55.54  ?  585 HOH E O   1 
HETATM 7248 O O   . HOH T 8 .   ? 34.514 -15.563 -36.386 1.00 52.18  ?  586 HOH E O   1 
HETATM 7249 O O   . HOH T 8 .   ? 12.575 -24.653 -24.740 1.00 53.03  ?  587 HOH E O   1 
HETATM 7250 O O   . HOH T 8 .   ? 31.744 -12.010 -25.479 1.00 49.26  ?  588 HOH E O   1 
HETATM 7251 O O   . HOH T 8 .   ? 17.328 5.160   -34.823 1.00 35.56  ?  589 HOH E O   1 
HETATM 7252 O O   . HOH T 8 .   ? 25.054 -36.951 -60.257 1.00 43.75  ?  590 HOH E O   1 
HETATM 7253 O O   . HOH T 8 .   ? 33.849 -15.920 -39.218 1.00 42.09  ?  591 HOH E O   1 
HETATM 7254 O O   . HOH T 8 .   ? 8.425  -18.685 -32.272 1.00 46.00  ?  592 HOH E O   1 
HETATM 7255 O O   . HOH T 8 .   ? 36.529 -3.065  -30.113 1.00 38.81  ?  593 HOH E O   1 
HETATM 7256 O O   . HOH T 8 .   ? 15.843 -14.583 -59.718 1.00 40.06  ?  594 HOH E O   1 
HETATM 7257 O O   . HOH T 8 .   ? 17.064 0.184   -34.955 1.00 39.60  ?  595 HOH E O   1 
HETATM 7258 O O   . HOH T 8 .   ? 33.483 -32.207 -83.962 1.00 54.31  ?  596 HOH E O   1 
HETATM 7259 O O   . HOH T 8 .   ? 31.747 -36.821 -47.979 1.00 47.03  ?  597 HOH E O   1 
HETATM 7260 O O   . HOH T 8 .   ? 25.883 -17.029 -59.292 1.00 32.36  ?  598 HOH E O   1 
HETATM 7261 O O   . HOH T 8 .   ? 40.733 -22.100 -81.695 1.00 39.26  ?  599 HOH E O   1 
HETATM 7262 O O   . HOH T 8 .   ? 22.549 -17.696 -56.223 1.00 34.99  ?  600 HOH E O   1 
HETATM 7263 O O   . HOH T 8 .   ? 24.257 -38.268 -52.771 1.00 36.62  ?  601 HOH E O   1 
HETATM 7264 O O   . HOH T 8 .   ? 29.469 5.143   -45.594 1.00 52.80  ?  602 HOH E O   1 
HETATM 7265 O O   . HOH T 8 .   ? 33.625 -14.602 -29.027 1.00 39.55  ?  603 HOH E O   1 
HETATM 7266 O O   . HOH T 8 .   ? 13.654 -20.678 -41.745 1.00 41.56  ?  604 HOH E O   1 
HETATM 7267 O O   . HOH T 8 .   ? 5.065  -15.811 -37.526 1.00 54.19  ?  605 HOH E O   1 
HETATM 7268 O O   . HOH T 8 .   ? 28.528 -16.296 -25.029 1.00 38.72  ?  606 HOH E O   1 
HETATM 7269 O O   . HOH T 8 .   ? 34.612 5.683   -34.910 1.00 54.64  ?  607 HOH E O   1 
HETATM 7270 O O   . HOH T 8 .   ? 15.378 -21.483 -22.751 1.00 44.50  ?  608 HOH E O   1 
HETATM 7271 O O   . HOH T 8 .   ? 28.398 -13.113 -74.820 1.00 43.29  ?  609 HOH E O   1 
HETATM 7272 O O   . HOH T 8 .   ? 27.141 -36.896 -55.926 1.00 31.11  ?  610 HOH E O   1 
HETATM 7273 O O   . HOH T 8 .   ? 33.484 -34.376 -50.678 1.00 45.32  ?  611 HOH E O   1 
HETATM 7274 O O   . HOH T 8 .   ? 14.375 -0.644  -18.330 1.00 43.04  ?  612 HOH E O   1 
HETATM 7275 O O   . HOH T 8 .   ? 31.251 -13.594 -27.727 1.00 37.27  ?  613 HOH E O   1 
HETATM 7276 O O   . HOH T 8 .   ? 12.956 -22.516 -43.221 1.00 46.89  ?  614 HOH E O   1 
HETATM 7277 O O   . HOH T 8 .   ? 37.613 -34.964 -63.340 1.00 45.77  ?  615 HOH E O   1 
HETATM 7278 O O   . HOH T 8 .   ? 27.477 -38.650 -49.966 1.00 38.08  ?  616 HOH E O   1 
HETATM 7279 O O   . HOH T 8 .   ? 32.347 -2.543  -18.226 1.00 46.73  ?  617 HOH E O   1 
HETATM 7280 O O   . HOH T 8 .   ? 24.832 -27.162 -22.060 1.00 49.55  ?  618 HOH E O   1 
HETATM 7281 O O   . HOH T 8 .   ? 30.883 -18.422 -28.290 1.00 35.79  ?  619 HOH E O   1 
HETATM 7282 O O   . HOH T 8 .   ? 34.368 -1.865  -19.631 1.00 50.60  ?  620 HOH E O   1 
HETATM 7283 O O   . HOH T 8 .   ? 31.059 -16.290 -72.056 1.00 48.74  ?  621 HOH E O   1 
HETATM 7284 O O   . HOH T 8 .   ? 30.407 -16.124 -26.815 1.00 34.95  ?  622 HOH E O   1 
HETATM 7285 O O   . HOH T 8 .   ? 33.927 -16.109 -69.322 1.00 45.54  ?  623 HOH E O   1 
HETATM 7286 O O   . HOH T 8 .   ? 26.897 -38.926 -60.883 1.00 60.84  ?  624 HOH E O   1 
# 
