data_9MER
# 
_entry.id   9MER 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MER         pdb_00009mer 10.2210/pdb9mer/pdb 
WWPDB D_1000290837 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MER 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bruno.correia@epfl.ch 
_pdbx_contact_author.name_first         Bruno 
_pdbx_contact_author.name_last          Correia 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7377-8636 
# 
_audit_author.name               'Seraj, N.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-3292-377X 
# 
_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            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure-based Design of Chimeric Influenza Hemagglutinins to Elicit Cross-group Immunity.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.12.17.628867 
_citation.pdbx_database_id_PubMed   40027756 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Castro, K.M.'    1  0000-0002-7753-6060 
primary 'Ayardulabi, R.'  2  ?                   
primary 'Wehrle, S.'      3  ?                   
primary 'Cui, H.'         4  ?                   
primary 'Georgeon, S.'    5  ?                   
primary 'Schmidt, J.'     6  ?                   
primary 'Xiao, S.'        7  ?                   
primary 'Seraj, N.'       8  ?                   
primary 'Harshbarger, W.' 9  ?                   
primary 'Mallett, C.P.'   10 ?                   
primary 'Vassilev, V.'    11 ?                   
primary 'Saelens, X.'     12 0000-0002-3861-6965 
primary 'Correia, B.E.'   13 ?                   
# 
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 'H1H5 HA'                                25574.566 1   ? ? ? ? 
2 polymer     man 'FluA20 Heavy Chain Fab'                 25154.039 1   ? ? ? ? 
3 polymer     man 'FluA20 Light Chain Fab'                 23508.186 1   ? ? ? ? 
4 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   1   ? ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                           62.068    23  ? ? ? ? 
6 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                  106.120   3   ? ? ? ? 
7 non-polymer syn 'POTASSIUM ION'                          39.098    7   ? ? ? ? 
8 water       nat water                                    18.015    477 ? ? ? ? 
# 
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 
;APLQLGNCSVAGWILGNPECELLISRESWSYIVEKPNPENGTCFPGHFADYEELREQLSSVSSFERFEIFPKESSWPNHE
ASLGVSSCSHNGESSFYKNLLWLIGKNSTYPNLSKSYANNKEKEVLVLWGVHHPPDAAEQTKLYHKPTAYVSVVSSHYSR
KFTPRIATRSKVRGQSGRINYYWTLLEPGDTIIFEANGNLIAPRYAFALSRGSGLVPRGSGHHHHHH
;
;APLQLGNCSVAGWILGNPECELLISRESWSYIVEKPNPENGTCFPGHFADYEELREQLSSVSSFERFEIFPKESSWPNHE
ASLGVSSCSHNGESSFYKNLLWLIGKNSTYPNLSKSYANNKEKEVLVLWGVHHPPDAAEQTKLYHKPTAYVSVVSSHYSR
KFTPRIATRSKVRGQSGRINYYWTLLEPGDTIIFEANGNLIAPRYAFALSRGSGLVPRGSGHHHHHH
;
B ? 
2 'polypeptide(L)' no no 
;QVQLEESGPGLVKPSETLSLTCSVSGVSVTSDIYYWTWIRQPPGKGLEWIGYIFYNGDTNYNPSLKSRVTMSIDTSKNEF
SLRLTSVTAADTAVYFCARGTEDLGYCSSGSCPNHWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFP
EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCHHHHHH
;
;QVQLEESGPGLVKPSETLSLTCSVSGVSVTSDIYYWTWIRQPPGKGLEWIGYIFYNGDTNYNPSLKSRVTMSIDTSKNEF
SLRLTSVTAADTAVYFCARGTEDLGYCSSGSCPNHWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFP
EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCHHHHHH
;
H ? 
3 'polypeptide(L)' no no 
;DIVMTQSPSSLSASIGDRVTITCRPSQNIRSFLNWFQHKPGKAPKLLIYAASNLQSGVPSRFSGSGSGTEFTLTIRSLQP
EDFATYYCQQSYNTPPTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;DIVMTQSPSSLSASIGDRVTITCRPSQNIRSFLNWFQHKPGKAPKLLIYAASNLQSGVPSRFSGSGSGTEFTLTIRSLQP
EDFATYYCQQSYNTPPTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
L ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
5 1,2-ETHANEDIOL                           EDO 
6 'DI(HYDROXYETHYL)ETHER'                  PEG 
7 'POTASSIUM ION'                          K   
8 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   PRO n 
1 3   LEU n 
1 4   GLN n 
1 5   LEU n 
1 6   GLY n 
1 7   ASN n 
1 8   CYS n 
1 9   SER n 
1 10  VAL n 
1 11  ALA n 
1 12  GLY n 
1 13  TRP n 
1 14  ILE n 
1 15  LEU n 
1 16  GLY n 
1 17  ASN n 
1 18  PRO n 
1 19  GLU n 
1 20  CYS n 
1 21  GLU n 
1 22  LEU n 
1 23  LEU n 
1 24  ILE n 
1 25  SER n 
1 26  ARG n 
1 27  GLU n 
1 28  SER n 
1 29  TRP n 
1 30  SER n 
1 31  TYR n 
1 32  ILE n 
1 33  VAL n 
1 34  GLU n 
1 35  LYS n 
1 36  PRO n 
1 37  ASN n 
1 38  PRO n 
1 39  GLU n 
1 40  ASN n 
1 41  GLY n 
1 42  THR n 
1 43  CYS n 
1 44  PHE n 
1 45  PRO n 
1 46  GLY n 
1 47  HIS n 
1 48  PHE n 
1 49  ALA n 
1 50  ASP n 
1 51  TYR n 
1 52  GLU n 
1 53  GLU n 
1 54  LEU n 
1 55  ARG n 
1 56  GLU n 
1 57  GLN n 
1 58  LEU n 
1 59  SER n 
1 60  SER n 
1 61  VAL n 
1 62  SER n 
1 63  SER n 
1 64  PHE n 
1 65  GLU n 
1 66  ARG n 
1 67  PHE n 
1 68  GLU n 
1 69  ILE n 
1 70  PHE n 
1 71  PRO n 
1 72  LYS n 
1 73  GLU n 
1 74  SER n 
1 75  SER n 
1 76  TRP n 
1 77  PRO n 
1 78  ASN n 
1 79  HIS n 
1 80  GLU n 
1 81  ALA n 
1 82  SER n 
1 83  LEU n 
1 84  GLY n 
1 85  VAL n 
1 86  SER n 
1 87  SER n 
1 88  CYS n 
1 89  SER n 
1 90  HIS n 
1 91  ASN n 
1 92  GLY n 
1 93  GLU n 
1 94  SER n 
1 95  SER n 
1 96  PHE n 
1 97  TYR n 
1 98  LYS n 
1 99  ASN n 
1 100 LEU n 
1 101 LEU n 
1 102 TRP n 
1 103 LEU n 
1 104 ILE n 
1 105 GLY n 
1 106 LYS n 
1 107 ASN n 
1 108 SER n 
1 109 THR n 
1 110 TYR n 
1 111 PRO n 
1 112 ASN n 
1 113 LEU n 
1 114 SER n 
1 115 LYS n 
1 116 SER n 
1 117 TYR n 
1 118 ALA n 
1 119 ASN n 
1 120 ASN n 
1 121 LYS n 
1 122 GLU n 
1 123 LYS n 
1 124 GLU n 
1 125 VAL n 
1 126 LEU n 
1 127 VAL n 
1 128 LEU n 
1 129 TRP n 
1 130 GLY n 
1 131 VAL n 
1 132 HIS n 
1 133 HIS n 
1 134 PRO n 
1 135 PRO n 
1 136 ASP n 
1 137 ALA n 
1 138 ALA n 
1 139 GLU n 
1 140 GLN n 
1 141 THR n 
1 142 LYS n 
1 143 LEU n 
1 144 TYR n 
1 145 HIS n 
1 146 LYS n 
1 147 PRO n 
1 148 THR n 
1 149 ALA n 
1 150 TYR n 
1 151 VAL n 
1 152 SER n 
1 153 VAL n 
1 154 VAL n 
1 155 SER n 
1 156 SER n 
1 157 HIS n 
1 158 TYR n 
1 159 SER n 
1 160 ARG n 
1 161 LYS n 
1 162 PHE n 
1 163 THR n 
1 164 PRO n 
1 165 ARG n 
1 166 ILE n 
1 167 ALA n 
1 168 THR n 
1 169 ARG n 
1 170 SER n 
1 171 LYS n 
1 172 VAL n 
1 173 ARG n 
1 174 GLY n 
1 175 GLN n 
1 176 SER n 
1 177 GLY n 
1 178 ARG n 
1 179 ILE n 
1 180 ASN n 
1 181 TYR n 
1 182 TYR n 
1 183 TRP n 
1 184 THR n 
1 185 LEU n 
1 186 LEU n 
1 187 GLU n 
1 188 PRO n 
1 189 GLY n 
1 190 ASP n 
1 191 THR n 
1 192 ILE n 
1 193 ILE n 
1 194 PHE n 
1 195 GLU n 
1 196 ALA n 
1 197 ASN n 
1 198 GLY n 
1 199 ASN n 
1 200 LEU n 
1 201 ILE n 
1 202 ALA n 
1 203 PRO n 
1 204 ARG n 
1 205 TYR n 
1 206 ALA n 
1 207 PHE n 
1 208 ALA n 
1 209 LEU n 
1 210 SER n 
1 211 ARG n 
1 212 GLY n 
1 213 SER n 
1 214 GLY n 
1 215 LEU n 
1 216 VAL n 
1 217 PRO n 
1 218 ARG n 
1 219 GLY n 
1 220 SER n 
1 221 GLY n 
1 222 HIS n 
1 223 HIS n 
1 224 HIS n 
1 225 HIS n 
1 226 HIS n 
1 227 HIS n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   GLU n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   PRO n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  LYS n 
2 14  PRO n 
2 15  SER n 
2 16  GLU n 
2 17  THR n 
2 18  LEU n 
2 19  SER n 
2 20  LEU n 
2 21  THR n 
2 22  CYS n 
2 23  SER n 
2 24  VAL n 
2 25  SER n 
2 26  GLY n 
2 27  VAL n 
2 28  SER n 
2 29  VAL n 
2 30  THR n 
2 31  SER n 
2 32  ASP n 
2 33  ILE n 
2 34  TYR n 
2 35  TYR n 
2 36  TRP n 
2 37  THR n 
2 38  TRP n 
2 39  ILE n 
2 40  ARG n 
2 41  GLN n 
2 42  PRO n 
2 43  PRO n 
2 44  GLY n 
2 45  LYS n 
2 46  GLY n 
2 47  LEU n 
2 48  GLU n 
2 49  TRP n 
2 50  ILE n 
2 51  GLY n 
2 52  TYR n 
2 53  ILE n 
2 54  PHE n 
2 55  TYR n 
2 56  ASN n 
2 57  GLY n 
2 58  ASP n 
2 59  THR n 
2 60  ASN n 
2 61  TYR n 
2 62  ASN n 
2 63  PRO n 
2 64  SER n 
2 65  LEU n 
2 66  LYS n 
2 67  SER n 
2 68  ARG n 
2 69  VAL n 
2 70  THR n 
2 71  MET n 
2 72  SER n 
2 73  ILE n 
2 74  ASP n 
2 75  THR n 
2 76  SER n 
2 77  LYS n 
2 78  ASN n 
2 79  GLU n 
2 80  PHE n 
2 81  SER n 
2 82  LEU n 
2 83  ARG n 
2 84  LEU n 
2 85  THR n 
2 86  SER n 
2 87  VAL n 
2 88  THR n 
2 89  ALA n 
2 90  ALA n 
2 91  ASP n 
2 92  THR n 
2 93  ALA n 
2 94  VAL n 
2 95  TYR n 
2 96  PHE n 
2 97  CYS n 
2 98  ALA n 
2 99  ARG n 
2 100 GLY n 
2 101 THR n 
2 102 GLU n 
2 103 ASP n 
2 104 LEU n 
2 105 GLY n 
2 106 TYR n 
2 107 CYS n 
2 108 SER n 
2 109 SER n 
2 110 GLY n 
2 111 SER n 
2 112 CYS n 
2 113 PRO n 
2 114 ASN n 
2 115 HIS n 
2 116 TRP n 
2 117 GLY n 
2 118 GLN n 
2 119 GLY n 
2 120 THR n 
2 121 LEU n 
2 122 VAL n 
2 123 THR n 
2 124 VAL n 
2 125 SER n 
2 126 SER n 
2 127 ALA n 
2 128 SER n 
2 129 THR n 
2 130 LYS n 
2 131 GLY n 
2 132 PRO n 
2 133 SER n 
2 134 VAL n 
2 135 PHE n 
2 136 PRO n 
2 137 LEU n 
2 138 ALA n 
2 139 PRO n 
2 140 SER n 
2 141 SER n 
2 142 LYS n 
2 143 SER n 
2 144 THR n 
2 145 SER n 
2 146 GLY n 
2 147 GLY n 
2 148 THR n 
2 149 ALA n 
2 150 ALA n 
2 151 LEU n 
2 152 GLY n 
2 153 CYS n 
2 154 LEU n 
2 155 VAL n 
2 156 LYS n 
2 157 ASP n 
2 158 TYR n 
2 159 PHE n 
2 160 PRO n 
2 161 GLU n 
2 162 PRO n 
2 163 VAL n 
2 164 THR n 
2 165 VAL n 
2 166 SER n 
2 167 TRP n 
2 168 ASN n 
2 169 SER n 
2 170 GLY n 
2 171 ALA n 
2 172 LEU n 
2 173 THR n 
2 174 SER n 
2 175 GLY n 
2 176 VAL n 
2 177 HIS n 
2 178 THR n 
2 179 PHE n 
2 180 PRO n 
2 181 ALA n 
2 182 VAL n 
2 183 LEU n 
2 184 GLN n 
2 185 SER n 
2 186 SER n 
2 187 GLY n 
2 188 LEU n 
2 189 TYR n 
2 190 SER n 
2 191 LEU n 
2 192 SER n 
2 193 SER n 
2 194 VAL n 
2 195 VAL n 
2 196 THR n 
2 197 VAL n 
2 198 PRO n 
2 199 SER n 
2 200 SER n 
2 201 SER n 
2 202 LEU n 
2 203 GLY n 
2 204 THR n 
2 205 GLN n 
2 206 THR n 
2 207 TYR n 
2 208 ILE n 
2 209 CYS n 
2 210 ASN n 
2 211 VAL n 
2 212 ASN n 
2 213 HIS n 
2 214 LYS n 
2 215 PRO n 
2 216 SER n 
2 217 ASN n 
2 218 THR n 
2 219 LYS n 
2 220 VAL n 
2 221 ASP n 
2 222 LYS n 
2 223 ARG n 
2 224 VAL n 
2 225 GLU n 
2 226 PRO n 
2 227 LYS n 
2 228 SER n 
2 229 CYS n 
2 230 HIS n 
2 231 HIS n 
2 232 HIS n 
2 233 HIS n 
2 234 HIS n 
2 235 HIS n 
3 1   ASP n 
3 2   ILE n 
3 3   VAL n 
3 4   MET n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   SER n 
3 10  SER n 
3 11  LEU n 
3 12  SER n 
3 13  ALA n 
3 14  SER n 
3 15  ILE n 
3 16  GLY n 
3 17  ASP n 
3 18  ARG n 
3 19  VAL n 
3 20  THR n 
3 21  ILE n 
3 22  THR n 
3 23  CYS n 
3 24  ARG n 
3 25  PRO n 
3 26  SER n 
3 27  GLN n 
3 28  ASN n 
3 29  ILE n 
3 30  ARG n 
3 31  SER n 
3 32  PHE n 
3 33  LEU n 
3 34  ASN n 
3 35  TRP n 
3 36  PHE n 
3 37  GLN n 
3 38  HIS n 
3 39  LYS n 
3 40  PRO n 
3 41  GLY n 
3 42  LYS n 
3 43  ALA n 
3 44  PRO n 
3 45  LYS n 
3 46  LEU n 
3 47  LEU n 
3 48  ILE n 
3 49  TYR n 
3 50  ALA n 
3 51  ALA n 
3 52  SER n 
3 53  ASN n 
3 54  LEU n 
3 55  GLN n 
3 56  SER n 
3 57  GLY n 
3 58  VAL n 
3 59  PRO n 
3 60  SER n 
3 61  ARG n 
3 62  PHE n 
3 63  SER n 
3 64  GLY n 
3 65  SER n 
3 66  GLY n 
3 67  SER n 
3 68  GLY n 
3 69  THR n 
3 70  GLU n 
3 71  PHE n 
3 72  THR n 
3 73  LEU n 
3 74  THR n 
3 75  ILE n 
3 76  ARG n 
3 77  SER n 
3 78  LEU n 
3 79  GLN n 
3 80  PRO n 
3 81  GLU n 
3 82  ASP n 
3 83  PHE n 
3 84  ALA n 
3 85  THR n 
3 86  TYR n 
3 87  TYR n 
3 88  CYS n 
3 89  GLN n 
3 90  GLN n 
3 91  SER n 
3 92  TYR n 
3 93  ASN n 
3 94  THR n 
3 95  PRO n 
3 96  PRO n 
3 97  THR n 
3 98  PHE n 
3 99  GLY n 
3 100 GLN n 
3 101 GLY n 
3 102 THR n 
3 103 LYS n 
3 104 VAL n 
3 105 GLU n 
3 106 ILE n 
3 107 LYS n 
3 108 ARG n 
3 109 THR n 
3 110 VAL n 
3 111 ALA n 
3 112 ALA n 
3 113 PRO n 
3 114 SER n 
3 115 VAL n 
3 116 PHE n 
3 117 ILE n 
3 118 PHE n 
3 119 PRO n 
3 120 PRO n 
3 121 SER n 
3 122 ASP n 
3 123 GLU n 
3 124 GLN n 
3 125 LEU n 
3 126 LYS n 
3 127 SER n 
3 128 GLY n 
3 129 THR n 
3 130 ALA n 
3 131 SER n 
3 132 VAL n 
3 133 VAL n 
3 134 CYS n 
3 135 LEU n 
3 136 LEU n 
3 137 ASN n 
3 138 ASN n 
3 139 PHE n 
3 140 TYR n 
3 141 PRO n 
3 142 ARG n 
3 143 GLU n 
3 144 ALA n 
3 145 LYS n 
3 146 VAL n 
3 147 GLN n 
3 148 TRP n 
3 149 LYS n 
3 150 VAL n 
3 151 ASP n 
3 152 ASN n 
3 153 ALA n 
3 154 LEU n 
3 155 GLN n 
3 156 SER n 
3 157 GLY n 
3 158 ASN n 
3 159 SER n 
3 160 GLN n 
3 161 GLU n 
3 162 SER n 
3 163 VAL n 
3 164 THR n 
3 165 GLU n 
3 166 GLN n 
3 167 ASP n 
3 168 SER n 
3 169 LYS n 
3 170 ASP n 
3 171 SER n 
3 172 THR n 
3 173 TYR n 
3 174 SER n 
3 175 LEU n 
3 176 SER n 
3 177 SER n 
3 178 THR n 
3 179 LEU n 
3 180 THR n 
3 181 LEU n 
3 182 SER n 
3 183 LYS n 
3 184 ALA n 
3 185 ASP n 
3 186 TYR n 
3 187 GLU n 
3 188 LYS n 
3 189 HIS n 
3 190 LYS n 
3 191 VAL n 
3 192 TYR n 
3 193 ALA n 
3 194 CYS n 
3 195 GLU n 
3 196 VAL n 
3 197 THR n 
3 198 HIS n 
3 199 GLN n 
3 200 GLY n 
3 201 LEU n 
3 202 SER n 
3 203 SER n 
3 204 PRO n 
3 205 VAL n 
3 206 THR n 
3 207 LYS n 
3 208 SER n 
3 209 PHE n 
3 210 ASN n 
3 211 ARG n 
3 212 GLY n 
3 213 GLU n 
3 214 CYS 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' 1 227 ?     ? ? ? ? ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 235 human ? ? ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 214 human ? ? ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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  
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 
K   non-polymer                  . 'POTASSIUM ION'                          ? 'K 1'            39.098  
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PEG non-polymer                  . 'DI(HYDROXYETHYL)ETHER'                  ? 'C4 H10 O3'      106.120 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   ALA 1   52  52  ALA ALA B . n 
A 1 2   PRO 2   53  53  PRO PRO B . n 
A 1 3   LEU 3   54  54  LEU LEU B . n 
A 1 4   GLN 4   55  55  GLN GLN B . n 
A 1 5   LEU 5   56  56  LEU LEU B . n 
A 1 6   GLY 6   57  57  GLY GLY B . n 
A 1 7   ASN 7   58  58  ASN ASN B . n 
A 1 8   CYS 8   59  59  CYS CYS B . n 
A 1 9   SER 9   60  60  SER SER B . n 
A 1 10  VAL 10  61  61  VAL VAL B . n 
A 1 11  ALA 11  62  62  ALA ALA B . n 
A 1 12  GLY 12  63  63  GLY GLY B . n 
A 1 13  TRP 13  64  64  TRP TRP B . n 
A 1 14  ILE 14  65  65  ILE ILE B . n 
A 1 15  LEU 15  66  66  LEU LEU B . n 
A 1 16  GLY 16  67  67  GLY GLY B . n 
A 1 17  ASN 17  68  68  ASN ASN B . n 
A 1 18  PRO 18  69  69  PRO PRO B . n 
A 1 19  GLU 19  70  70  GLU GLU B . n 
A 1 20  CYS 20  71  71  CYS CYS B . n 
A 1 21  GLU 21  72  72  GLU GLU B . n 
A 1 22  LEU 22  73  73  LEU LEU B . n 
A 1 23  LEU 23  74  74  LEU LEU B . n 
A 1 24  ILE 24  75  75  ILE ILE B . n 
A 1 25  SER 25  76  76  SER SER B . n 
A 1 26  ARG 26  77  77  ARG ARG B . n 
A 1 27  GLU 27  78  78  GLU GLU B . n 
A 1 28  SER 28  79  79  SER SER B . n 
A 1 29  TRP 29  80  80  TRP TRP B . n 
A 1 30  SER 30  81  81  SER SER B . n 
A 1 31  TYR 31  82  82  TYR TYR B . n 
A 1 32  ILE 32  83  83  ILE ILE B . n 
A 1 33  VAL 33  84  84  VAL VAL B . n 
A 1 34  GLU 34  85  85  GLU GLU B . n 
A 1 35  LYS 35  86  86  LYS LYS B . n 
A 1 36  PRO 36  87  87  PRO PRO B . n 
A 1 37  ASN 37  88  88  ASN ASN B . n 
A 1 38  PRO 38  89  89  PRO PRO B . n 
A 1 39  GLU 39  90  90  GLU GLU B . n 
A 1 40  ASN 40  91  91  ASN ASN B . n 
A 1 41  GLY 41  92  92  GLY GLY B . n 
A 1 42  THR 42  93  93  THR THR B . n 
A 1 43  CYS 43  94  94  CYS CYS B . n 
A 1 44  PHE 44  95  95  PHE PHE B . n 
A 1 45  PRO 45  96  96  PRO PRO B . n 
A 1 46  GLY 46  97  97  GLY GLY B . n 
A 1 47  HIS 47  98  98  HIS HIS B . n 
A 1 48  PHE 48  99  99  PHE PHE B . n 
A 1 49  ALA 49  100 100 ALA ALA B . n 
A 1 50  ASP 50  101 101 ASP ASP B . n 
A 1 51  TYR 51  102 102 TYR TYR B . n 
A 1 52  GLU 52  103 103 GLU GLU B . n 
A 1 53  GLU 53  104 104 GLU GLU B . n 
A 1 54  LEU 54  105 105 LEU LEU B . n 
A 1 55  ARG 55  106 106 ARG ARG B . n 
A 1 56  GLU 56  107 107 GLU GLU B . n 
A 1 57  GLN 57  108 108 GLN GLN B . n 
A 1 58  LEU 58  109 109 LEU LEU B . n 
A 1 59  SER 59  110 110 SER SER B . n 
A 1 60  SER 60  111 111 SER SER B . n 
A 1 61  VAL 61  112 112 VAL VAL B . n 
A 1 62  SER 62  113 113 SER SER B . n 
A 1 63  SER 63  114 114 SER SER B . n 
A 1 64  PHE 64  115 115 PHE PHE B . n 
A 1 65  GLU 65  116 116 GLU GLU B . n 
A 1 66  ARG 66  117 117 ARG ARG B . n 
A 1 67  PHE 67  118 118 PHE PHE B . n 
A 1 68  GLU 68  119 119 GLU GLU B . n 
A 1 69  ILE 69  120 120 ILE ILE B . n 
A 1 70  PHE 70  121 121 PHE PHE B . n 
A 1 71  PRO 71  122 122 PRO PRO B . n 
A 1 72  LYS 72  123 123 LYS LYS B . n 
A 1 73  GLU 73  124 124 GLU GLU B . n 
A 1 74  SER 74  125 125 SER SER B . n 
A 1 75  SER 75  126 126 SER SER B . n 
A 1 76  TRP 76  127 127 TRP TRP B . n 
A 1 77  PRO 77  128 128 PRO PRO B . n 
A 1 78  ASN 78  129 129 ASN ASN B . n 
A 1 79  HIS 79  130 130 HIS HIS B . n 
A 1 80  GLU 80  131 131 GLU GLU B . n 
A 1 81  ALA 81  132 132 ALA ALA B . n 
A 1 82  SER 82  133 133 SER SER B . n 
A 1 83  LEU 83  134 134 LEU LEU B . n 
A 1 84  GLY 84  135 135 GLY GLY B . n 
A 1 85  VAL 85  136 136 VAL VAL B . n 
A 1 86  SER 86  137 137 SER SER B . n 
A 1 87  SER 87  138 138 SER SER B . n 
A 1 88  CYS 88  139 139 CYS CYS B . n 
A 1 89  SER 89  140 140 SER SER B . n 
A 1 90  HIS 90  141 141 HIS HIS B . n 
A 1 91  ASN 91  142 142 ASN ASN B . n 
A 1 92  GLY 92  143 143 GLY GLY B . n 
A 1 93  GLU 93  144 144 GLU GLU B . n 
A 1 94  SER 94  145 145 SER SER B . n 
A 1 95  SER 95  146 146 SER SER B . n 
A 1 96  PHE 96  147 147 PHE PHE B . n 
A 1 97  TYR 97  148 148 TYR TYR B . n 
A 1 98  LYS 98  149 149 LYS LYS B . n 
A 1 99  ASN 99  150 150 ASN ASN B . n 
A 1 100 LEU 100 151 151 LEU LEU B . n 
A 1 101 LEU 101 152 152 LEU LEU B . n 
A 1 102 TRP 102 153 153 TRP TRP B . n 
A 1 103 LEU 103 154 154 LEU LEU B . n 
A 1 104 ILE 104 155 155 ILE ILE B . n 
A 1 105 GLY 105 156 156 GLY GLY B . n 
A 1 106 LYS 106 157 157 LYS LYS B . n 
A 1 107 ASN 107 158 158 ASN ASN B . n 
A 1 108 SER 108 159 159 SER SER B . n 
A 1 109 THR 109 160 160 THR THR B . n 
A 1 110 TYR 110 161 161 TYR TYR B . n 
A 1 111 PRO 111 162 162 PRO PRO B . n 
A 1 112 ASN 112 163 163 ASN ASN B . n 
A 1 113 LEU 113 164 164 LEU LEU B . n 
A 1 114 SER 114 165 165 SER SER B . n 
A 1 115 LYS 115 166 166 LYS LYS B . n 
A 1 116 SER 116 167 167 SER SER B . n 
A 1 117 TYR 117 168 168 TYR TYR B . n 
A 1 118 ALA 118 169 169 ALA ALA B . n 
A 1 119 ASN 119 170 170 ASN ASN B . n 
A 1 120 ASN 120 171 171 ASN ASN B . n 
A 1 121 LYS 121 172 172 LYS LYS B . n 
A 1 122 GLU 122 173 173 GLU GLU B . n 
A 1 123 LYS 123 174 174 LYS LYS B . n 
A 1 124 GLU 124 175 175 GLU GLU B . n 
A 1 125 VAL 125 176 176 VAL VAL B . n 
A 1 126 LEU 126 177 177 LEU LEU B . n 
A 1 127 VAL 127 178 178 VAL VAL B . n 
A 1 128 LEU 128 179 179 LEU LEU B . n 
A 1 129 TRP 129 180 180 TRP TRP B . n 
A 1 130 GLY 130 181 181 GLY GLY B . n 
A 1 131 VAL 131 182 182 VAL VAL B . n 
A 1 132 HIS 132 183 183 HIS HIS B . n 
A 1 133 HIS 133 184 184 HIS HIS B . n 
A 1 134 PRO 134 185 185 PRO PRO B . n 
A 1 135 PRO 135 186 186 PRO PRO B . n 
A 1 136 ASP 136 187 187 ASP ASP B . n 
A 1 137 ALA 137 188 188 ALA ALA B . n 
A 1 138 ALA 138 189 189 ALA ALA B . n 
A 1 139 GLU 139 190 190 GLU GLU B . n 
A 1 140 GLN 140 191 191 GLN GLN B . n 
A 1 141 THR 141 192 192 THR THR B . n 
A 1 142 LYS 142 193 193 LYS LYS B . n 
A 1 143 LEU 143 194 194 LEU LEU B . n 
A 1 144 TYR 144 195 195 TYR TYR B . n 
A 1 145 HIS 145 196 196 HIS HIS B . n 
A 1 146 LYS 146 197 197 LYS LYS B . n 
A 1 147 PRO 147 198 198 PRO PRO B . n 
A 1 148 THR 148 199 199 THR THR B . n 
A 1 149 ALA 149 200 200 ALA ALA B . n 
A 1 150 TYR 150 201 201 TYR TYR B . n 
A 1 151 VAL 151 202 202 VAL VAL B . n 
A 1 152 SER 152 203 203 SER SER B . n 
A 1 153 VAL 153 204 204 VAL VAL B . n 
A 1 154 VAL 154 205 205 VAL VAL B . n 
A 1 155 SER 155 206 206 SER SER B . n 
A 1 156 SER 156 207 207 SER SER B . n 
A 1 157 HIS 157 208 208 HIS HIS B . n 
A 1 158 TYR 158 209 209 TYR TYR B . n 
A 1 159 SER 159 210 210 SER SER B . n 
A 1 160 ARG 160 211 211 ARG ARG B . n 
A 1 161 LYS 161 212 212 LYS LYS B . n 
A 1 162 PHE 162 213 213 PHE PHE B . n 
A 1 163 THR 163 214 214 THR THR B . n 
A 1 164 PRO 164 215 215 PRO PRO B . n 
A 1 165 ARG 165 216 216 ARG ARG B . n 
A 1 166 ILE 166 217 217 ILE ILE B . n 
A 1 167 ALA 167 218 218 ALA ALA B . n 
A 1 168 THR 168 219 219 THR THR B . n 
A 1 169 ARG 169 220 220 ARG ARG B . n 
A 1 170 SER 170 221 221 SER SER B . n 
A 1 171 LYS 171 222 222 LYS LYS B . n 
A 1 172 VAL 172 223 223 VAL VAL B . n 
A 1 173 ARG 173 224 224 ARG ARG B . n 
A 1 174 GLY 174 225 225 GLY GLY B . n 
A 1 175 GLN 175 226 226 GLN GLN B . n 
A 1 176 SER 176 227 227 SER SER B . n 
A 1 177 GLY 177 228 228 GLY GLY B . n 
A 1 178 ARG 178 229 229 ARG ARG B . n 
A 1 179 ILE 179 230 230 ILE ILE B . n 
A 1 180 ASN 180 231 231 ASN ASN B . n 
A 1 181 TYR 181 232 232 TYR TYR B . n 
A 1 182 TYR 182 233 233 TYR TYR B . n 
A 1 183 TRP 183 234 234 TRP TRP B . n 
A 1 184 THR 184 235 235 THR THR B . n 
A 1 185 LEU 185 236 236 LEU LEU B . n 
A 1 186 LEU 186 237 237 LEU LEU B . n 
A 1 187 GLU 187 238 238 GLU GLU B . n 
A 1 188 PRO 188 239 239 PRO PRO B . n 
A 1 189 GLY 189 240 240 GLY GLY B . n 
A 1 190 ASP 190 241 241 ASP ASP B . n 
A 1 191 THR 191 242 242 THR THR B . n 
A 1 192 ILE 192 243 243 ILE ILE B . n 
A 1 193 ILE 193 244 244 ILE ILE B . n 
A 1 194 PHE 194 245 245 PHE PHE B . n 
A 1 195 GLU 195 246 246 GLU GLU B . n 
A 1 196 ALA 196 247 247 ALA ALA B . n 
A 1 197 ASN 197 248 248 ASN ASN B . n 
A 1 198 GLY 198 249 249 GLY GLY B . n 
A 1 199 ASN 199 250 250 ASN ASN B . n 
A 1 200 LEU 200 251 251 LEU LEU B . n 
A 1 201 ILE 201 252 252 ILE ILE B . n 
A 1 202 ALA 202 253 253 ALA ALA B . n 
A 1 203 PRO 203 254 254 PRO PRO B . n 
A 1 204 ARG 204 255 255 ARG ARG B . n 
A 1 205 TYR 205 256 256 TYR TYR B . n 
A 1 206 ALA 206 257 257 ALA ALA B . n 
A 1 207 PHE 207 258 258 PHE PHE B . n 
A 1 208 ALA 208 259 259 ALA ALA B . n 
A 1 209 LEU 209 260 260 LEU LEU B . n 
A 1 210 SER 210 261 261 SER SER B . n 
A 1 211 ARG 211 262 262 ARG ARG B . n 
A 1 212 GLY 212 263 263 GLY GLY B . n 
A 1 213 SER 213 264 264 SER SER B . n 
A 1 214 GLY 214 265 265 GLY GLY B . n 
A 1 215 LEU 215 266 ?   ?   ?   B . n 
A 1 216 VAL 216 267 ?   ?   ?   B . n 
A 1 217 PRO 217 268 ?   ?   ?   B . n 
A 1 218 ARG 218 269 ?   ?   ?   B . n 
A 1 219 GLY 219 270 ?   ?   ?   B . n 
A 1 220 SER 220 271 ?   ?   ?   B . n 
A 1 221 GLY 221 272 ?   ?   ?   B . n 
A 1 222 HIS 222 273 ?   ?   ?   B . n 
A 1 223 HIS 223 274 ?   ?   ?   B . n 
A 1 224 HIS 224 275 ?   ?   ?   B . n 
A 1 225 HIS 225 276 ?   ?   ?   B . n 
A 1 226 HIS 226 277 ?   ?   ?   B . n 
A 1 227 HIS 227 278 ?   ?   ?   B . n 
B 2 1   GLN 1   1   1   GLN GLN H . n 
B 2 2   VAL 2   2   2   VAL VAL H . n 
B 2 3   GLN 3   3   3   GLN GLN H . n 
B 2 4   LEU 4   4   4   LEU LEU H . n 
B 2 5   GLU 5   5   5   GLU GLU H . n 
B 2 6   GLU 6   6   6   GLU GLU H . n 
B 2 7   SER 7   7   7   SER SER H . n 
B 2 8   GLY 8   8   8   GLY GLY H . n 
B 2 9   PRO 9   9   9   PRO PRO H . n 
B 2 10  GLY 10  10  10  GLY GLY H . n 
B 2 11  LEU 11  11  11  LEU LEU H . n 
B 2 12  VAL 12  12  12  VAL VAL H . n 
B 2 13  LYS 13  13  13  LYS LYS H . n 
B 2 14  PRO 14  14  14  PRO PRO H . n 
B 2 15  SER 15  15  15  SER SER H . n 
B 2 16  GLU 16  16  16  GLU GLU H . n 
B 2 17  THR 17  17  17  THR THR H . n 
B 2 18  LEU 18  18  18  LEU LEU H . n 
B 2 19  SER 19  19  19  SER SER H . n 
B 2 20  LEU 20  20  20  LEU LEU H . n 
B 2 21  THR 21  21  21  THR THR H . n 
B 2 22  CYS 22  22  22  CYS CYS H . n 
B 2 23  SER 23  23  23  SER SER H . n 
B 2 24  VAL 24  24  24  VAL VAL H . n 
B 2 25  SER 25  25  25  SER SER H . n 
B 2 26  GLY 26  26  26  GLY GLY H . n 
B 2 27  VAL 27  27  27  VAL VAL H . n 
B 2 28  SER 28  28  28  SER SER H . n 
B 2 29  VAL 29  29  29  VAL VAL H . n 
B 2 30  THR 30  30  30  THR THR H . n 
B 2 31  SER 31  31  31  SER SER H . n 
B 2 32  ASP 32  32  32  ASP ASP H . n 
B 2 33  ILE 33  33  33  ILE ILE H . n 
B 2 34  TYR 34  34  34  TYR TYR H . n 
B 2 35  TYR 35  35  35  TYR TYR H . n 
B 2 36  TRP 36  35  35  TRP TRP H A n 
B 2 37  THR 37  35  35  THR THR H B n 
B 2 38  TRP 38  36  36  TRP TRP H . n 
B 2 39  ILE 39  37  37  ILE ILE H . n 
B 2 40  ARG 40  38  38  ARG ARG H . n 
B 2 41  GLN 41  39  39  GLN GLN H . n 
B 2 42  PRO 42  40  40  PRO PRO H . n 
B 2 43  PRO 43  41  41  PRO PRO H . n 
B 2 44  GLY 44  42  42  GLY GLY H . n 
B 2 45  LYS 45  43  43  LYS LYS H . n 
B 2 46  GLY 46  44  44  GLY GLY H . n 
B 2 47  LEU 47  45  45  LEU LEU H . n 
B 2 48  GLU 48  46  46  GLU GLU H . n 
B 2 49  TRP 49  47  47  TRP TRP H . n 
B 2 50  ILE 50  48  48  ILE ILE H . n 
B 2 51  GLY 51  49  49  GLY GLY H . n 
B 2 52  TYR 52  50  50  TYR TYR H . n 
B 2 53  ILE 53  51  51  ILE ILE H . n 
B 2 54  PHE 54  52  52  PHE PHE H . n 
B 2 55  TYR 55  53  53  TYR TYR H . n 
B 2 56  ASN 56  54  54  ASN ASN H . n 
B 2 57  GLY 57  55  55  GLY GLY H . n 
B 2 58  ASP 58  56  56  ASP ASP H . n 
B 2 59  THR 59  57  57  THR THR H . n 
B 2 60  ASN 60  58  58  ASN ASN H . n 
B 2 61  TYR 61  59  59  TYR TYR H . n 
B 2 62  ASN 62  60  60  ASN ASN H . n 
B 2 63  PRO 63  61  61  PRO PRO H . n 
B 2 64  SER 64  62  62  SER SER H . n 
B 2 65  LEU 65  63  63  LEU LEU H . n 
B 2 66  LYS 66  64  64  LYS LYS H . n 
B 2 67  SER 67  65  65  SER SER H . n 
B 2 68  ARG 68  66  66  ARG ARG H . n 
B 2 69  VAL 69  67  67  VAL VAL H . n 
B 2 70  THR 70  68  68  THR THR H . n 
B 2 71  MET 71  69  69  MET MET H . n 
B 2 72  SER 72  70  70  SER SER H . n 
B 2 73  ILE 73  71  71  ILE ILE H . n 
B 2 74  ASP 74  72  72  ASP ASP H . n 
B 2 75  THR 75  73  73  THR THR H . n 
B 2 76  SER 76  74  74  SER SER H . n 
B 2 77  LYS 77  75  75  LYS LYS H . n 
B 2 78  ASN 78  76  76  ASN ASN H . n 
B 2 79  GLU 79  77  77  GLU GLU H . n 
B 2 80  PHE 80  78  78  PHE PHE H . n 
B 2 81  SER 81  79  79  SER SER H . n 
B 2 82  LEU 82  80  80  LEU LEU H . n 
B 2 83  ARG 83  81  81  ARG ARG H . n 
B 2 84  LEU 84  82  82  LEU LEU H . n 
B 2 85  THR 85  82  82  THR THR H A n 
B 2 86  SER 86  82  82  SER SER H B n 
B 2 87  VAL 87  82  82  VAL VAL H C n 
B 2 88  THR 88  83  83  THR THR H . n 
B 2 89  ALA 89  84  84  ALA ALA H . n 
B 2 90  ALA 90  85  85  ALA ALA H . n 
B 2 91  ASP 91  86  86  ASP ASP H . n 
B 2 92  THR 92  87  87  THR THR H . n 
B 2 93  ALA 93  88  88  ALA ALA H . n 
B 2 94  VAL 94  89  89  VAL VAL H . n 
B 2 95  TYR 95  90  90  TYR TYR H . n 
B 2 96  PHE 96  91  91  PHE PHE H . n 
B 2 97  CYS 97  92  92  CYS CYS H . n 
B 2 98  ALA 98  93  93  ALA ALA H . n 
B 2 99  ARG 99  94  94  ARG ARG H . n 
B 2 100 GLY 100 95  95  GLY GLY H . n 
B 2 101 THR 101 96  96  THR THR H . n 
B 2 102 GLU 102 97  97  GLU GLU H . n 
B 2 103 ASP 103 98  98  ASP ASP H . n 
B 2 104 LEU 104 99  99  LEU LEU H . n 
B 2 105 GLY 105 100 100 GLY GLY H . n 
B 2 106 TYR 106 100 100 TYR TYR H A n 
B 2 107 CYS 107 100 100 CYS CYS H B n 
B 2 108 SER 108 100 100 SER SER H C n 
B 2 109 SER 109 100 100 SER SER H D n 
B 2 110 GLY 110 100 100 GLY GLY H E n 
B 2 111 SER 111 100 100 SER SER H F n 
B 2 112 CYS 112 100 100 CYS CYS H G n 
B 2 113 PRO 113 100 100 PRO PRO H H n 
B 2 114 ASN 114 101 101 ASN ASN H . n 
B 2 115 HIS 115 102 102 HIS HIS H . n 
B 2 116 TRP 116 103 103 TRP TRP H . n 
B 2 117 GLY 117 104 104 GLY GLY H . n 
B 2 118 GLN 118 105 105 GLN GLN H . n 
B 2 119 GLY 119 106 106 GLY GLY H . n 
B 2 120 THR 120 107 107 THR THR H . n 
B 2 121 LEU 121 108 108 LEU LEU H . n 
B 2 122 VAL 122 109 109 VAL VAL H . n 
B 2 123 THR 123 110 110 THR THR H . n 
B 2 124 VAL 124 111 111 VAL VAL H . n 
B 2 125 SER 125 112 112 SER SER H . n 
B 2 126 SER 126 113 113 SER SER H . n 
B 2 127 ALA 127 114 114 ALA ALA H . n 
B 2 128 SER 128 115 115 SER SER H . n 
B 2 129 THR 129 116 116 THR THR H . n 
B 2 130 LYS 130 117 117 LYS LYS H . n 
B 2 131 GLY 131 118 118 GLY GLY H . n 
B 2 132 PRO 132 119 119 PRO PRO H . n 
B 2 133 SER 133 120 120 SER SER H . n 
B 2 134 VAL 134 121 121 VAL VAL H . n 
B 2 135 PHE 135 122 122 PHE PHE H . n 
B 2 136 PRO 136 123 123 PRO PRO H . n 
B 2 137 LEU 137 124 124 LEU LEU H . n 
B 2 138 ALA 138 125 125 ALA ALA H . n 
B 2 139 PRO 139 126 126 PRO PRO H . n 
B 2 140 SER 140 127 127 SER SER H . n 
B 2 141 SER 141 128 128 SER SER H . n 
B 2 142 LYS 142 129 129 LYS LYS H . n 
B 2 143 SER 143 130 130 SER SER H . n 
B 2 144 THR 144 131 131 THR THR H . n 
B 2 145 SER 145 132 132 SER SER H . n 
B 2 146 GLY 146 133 133 GLY GLY H . n 
B 2 147 GLY 147 134 134 GLY GLY H . n 
B 2 148 THR 148 135 135 THR THR H . n 
B 2 149 ALA 149 136 136 ALA ALA H . n 
B 2 150 ALA 150 137 137 ALA ALA H . n 
B 2 151 LEU 151 138 138 LEU LEU H . n 
B 2 152 GLY 152 139 139 GLY GLY H . n 
B 2 153 CYS 153 140 140 CYS CYS H . n 
B 2 154 LEU 154 141 141 LEU LEU H . n 
B 2 155 VAL 155 142 142 VAL VAL H . n 
B 2 156 LYS 156 143 143 LYS LYS H . n 
B 2 157 ASP 157 144 144 ASP ASP H . n 
B 2 158 TYR 158 145 145 TYR TYR H . n 
B 2 159 PHE 159 146 146 PHE PHE H . n 
B 2 160 PRO 160 147 147 PRO PRO H . n 
B 2 161 GLU 161 148 148 GLU GLU H . n 
B 2 162 PRO 162 149 149 PRO PRO H . n 
B 2 163 VAL 163 150 150 VAL VAL H . n 
B 2 164 THR 164 151 151 THR THR H . n 
B 2 165 VAL 165 152 152 VAL VAL H . n 
B 2 166 SER 166 153 153 SER SER H . n 
B 2 167 TRP 167 154 154 TRP TRP H . n 
B 2 168 ASN 168 155 155 ASN ASN H . n 
B 2 169 SER 169 156 156 SER SER H . n 
B 2 170 GLY 170 157 157 GLY GLY H . n 
B 2 171 ALA 171 158 158 ALA ALA H . n 
B 2 172 LEU 172 159 159 LEU LEU H . n 
B 2 173 THR 173 160 160 THR THR H . n 
B 2 174 SER 174 161 161 SER SER H . n 
B 2 175 GLY 175 162 162 GLY GLY H . n 
B 2 176 VAL 176 163 163 VAL VAL H . n 
B 2 177 HIS 177 164 164 HIS HIS H . n 
B 2 178 THR 178 165 165 THR THR H . n 
B 2 179 PHE 179 166 166 PHE PHE H . n 
B 2 180 PRO 180 167 167 PRO PRO H . n 
B 2 181 ALA 181 168 168 ALA ALA H . n 
B 2 182 VAL 182 169 169 VAL VAL H . n 
B 2 183 LEU 183 170 170 LEU LEU H . n 
B 2 184 GLN 184 171 171 GLN GLN H . n 
B 2 185 SER 185 172 172 SER SER H . n 
B 2 186 SER 186 173 173 SER SER H . n 
B 2 187 GLY 187 174 174 GLY GLY H . n 
B 2 188 LEU 188 175 175 LEU LEU H . n 
B 2 189 TYR 189 176 176 TYR TYR H . n 
B 2 190 SER 190 177 177 SER SER H . n 
B 2 191 LEU 191 178 178 LEU LEU H . n 
B 2 192 SER 192 179 179 SER SER H . n 
B 2 193 SER 193 180 180 SER SER H . n 
B 2 194 VAL 194 181 181 VAL VAL H . n 
B 2 195 VAL 195 182 182 VAL VAL H . n 
B 2 196 THR 196 183 183 THR THR H . n 
B 2 197 VAL 197 184 184 VAL VAL H . n 
B 2 198 PRO 198 185 185 PRO PRO H . n 
B 2 199 SER 199 186 186 SER SER H . n 
B 2 200 SER 200 187 187 SER SER H . n 
B 2 201 SER 201 188 188 SER SER H . n 
B 2 202 LEU 202 189 189 LEU LEU H . n 
B 2 203 GLY 203 190 190 GLY GLY H . n 
B 2 204 THR 204 191 191 THR THR H . n 
B 2 205 GLN 205 192 192 GLN GLN H . n 
B 2 206 THR 206 193 193 THR THR H . n 
B 2 207 TYR 207 194 194 TYR TYR H . n 
B 2 208 ILE 208 195 195 ILE ILE H . n 
B 2 209 CYS 209 196 196 CYS CYS H . n 
B 2 210 ASN 210 197 197 ASN ASN H . n 
B 2 211 VAL 211 198 198 VAL VAL H . n 
B 2 212 ASN 212 199 199 ASN ASN H . n 
B 2 213 HIS 213 200 200 HIS HIS H . n 
B 2 214 LYS 214 201 201 LYS LYS H . n 
B 2 215 PRO 215 202 202 PRO PRO H . n 
B 2 216 SER 216 203 203 SER SER H . n 
B 2 217 ASN 217 204 204 ASN ASN H . n 
B 2 218 THR 218 205 205 THR THR H . n 
B 2 219 LYS 219 206 206 LYS LYS H . n 
B 2 220 VAL 220 207 207 VAL VAL H . n 
B 2 221 ASP 221 208 208 ASP ASP H . n 
B 2 222 LYS 222 209 209 LYS LYS H . n 
B 2 223 ARG 223 210 210 ARG ARG H . n 
B 2 224 VAL 224 211 211 VAL VAL H . n 
B 2 225 GLU 225 212 212 GLU GLU H . n 
B 2 226 PRO 226 213 213 PRO PRO H . n 
B 2 227 LYS 227 214 214 LYS LYS H . n 
B 2 228 SER 228 215 ?   ?   ?   H . n 
B 2 229 CYS 229 216 ?   ?   ?   H . n 
B 2 230 HIS 230 217 ?   ?   ?   H . n 
B 2 231 HIS 231 218 ?   ?   ?   H . n 
B 2 232 HIS 232 219 ?   ?   ?   H . n 
B 2 233 HIS 233 220 ?   ?   ?   H . n 
B 2 234 HIS 234 221 ?   ?   ?   H . n 
B 2 235 HIS 235 222 ?   ?   ?   H . n 
C 3 1   ASP 1   1   1   ASP ASP L . n 
C 3 2   ILE 2   2   2   ILE ILE L . n 
C 3 3   VAL 3   3   3   VAL VAL L . n 
C 3 4   MET 4   4   4   MET MET L . n 
C 3 5   THR 5   5   5   THR THR L . n 
C 3 6   GLN 6   6   6   GLN GLN L . n 
C 3 7   SER 7   7   7   SER SER L . n 
C 3 8   PRO 8   8   8   PRO PRO L . n 
C 3 9   SER 9   9   9   SER SER L . n 
C 3 10  SER 10  10  10  SER SER L . n 
C 3 11  LEU 11  11  11  LEU LEU L . n 
C 3 12  SER 12  12  12  SER SER L . n 
C 3 13  ALA 13  13  13  ALA ALA L . n 
C 3 14  SER 14  14  14  SER SER L . n 
C 3 15  ILE 15  15  15  ILE ILE L . n 
C 3 16  GLY 16  16  16  GLY GLY L . n 
C 3 17  ASP 17  17  17  ASP ASP L . n 
C 3 18  ARG 18  18  18  ARG ARG L . n 
C 3 19  VAL 19  19  19  VAL VAL L . n 
C 3 20  THR 20  20  20  THR THR L . n 
C 3 21  ILE 21  21  21  ILE ILE L . n 
C 3 22  THR 22  22  22  THR THR L . n 
C 3 23  CYS 23  23  23  CYS CYS L . n 
C 3 24  ARG 24  24  24  ARG ARG L . n 
C 3 25  PRO 25  25  25  PRO PRO L . n 
C 3 26  SER 26  26  26  SER SER L . n 
C 3 27  GLN 27  27  27  GLN GLN L . n 
C 3 28  ASN 28  28  28  ASN ASN L . n 
C 3 29  ILE 29  29  29  ILE ILE L . n 
C 3 30  ARG 30  30  30  ARG ARG L . n 
C 3 31  SER 31  31  31  SER SER L . n 
C 3 32  PHE 32  32  32  PHE PHE L . n 
C 3 33  LEU 33  33  33  LEU LEU L . n 
C 3 34  ASN 34  34  34  ASN ASN L . n 
C 3 35  TRP 35  35  35  TRP TRP L . n 
C 3 36  PHE 36  36  36  PHE PHE L . n 
C 3 37  GLN 37  37  37  GLN GLN L . n 
C 3 38  HIS 38  38  38  HIS HIS L . n 
C 3 39  LYS 39  39  39  LYS LYS L . n 
C 3 40  PRO 40  40  40  PRO PRO L . n 
C 3 41  GLY 41  41  41  GLY GLY L . n 
C 3 42  LYS 42  42  42  LYS LYS L . n 
C 3 43  ALA 43  43  43  ALA ALA L . n 
C 3 44  PRO 44  44  44  PRO PRO L . n 
C 3 45  LYS 45  45  45  LYS LYS L . n 
C 3 46  LEU 46  46  46  LEU LEU L . n 
C 3 47  LEU 47  47  47  LEU LEU L . n 
C 3 48  ILE 48  48  48  ILE ILE L . n 
C 3 49  TYR 49  49  49  TYR TYR L . n 
C 3 50  ALA 50  50  50  ALA ALA L . n 
C 3 51  ALA 51  51  51  ALA ALA L . n 
C 3 52  SER 52  52  52  SER SER L . n 
C 3 53  ASN 53  53  53  ASN ASN L . n 
C 3 54  LEU 54  54  54  LEU LEU L . n 
C 3 55  GLN 55  55  55  GLN GLN L . n 
C 3 56  SER 56  56  56  SER SER L . n 
C 3 57  GLY 57  57  57  GLY GLY L . n 
C 3 58  VAL 58  58  58  VAL VAL L . n 
C 3 59  PRO 59  59  59  PRO PRO L . n 
C 3 60  SER 60  60  60  SER SER L . n 
C 3 61  ARG 61  61  61  ARG ARG L . n 
C 3 62  PHE 62  62  62  PHE PHE L . n 
C 3 63  SER 63  63  63  SER SER L . n 
C 3 64  GLY 64  64  64  GLY GLY L . n 
C 3 65  SER 65  65  65  SER SER L . n 
C 3 66  GLY 66  66  66  GLY GLY L . n 
C 3 67  SER 67  67  67  SER SER L . n 
C 3 68  GLY 68  68  68  GLY GLY L . n 
C 3 69  THR 69  69  69  THR THR L . n 
C 3 70  GLU 70  70  70  GLU GLU L . n 
C 3 71  PHE 71  71  71  PHE PHE L . n 
C 3 72  THR 72  72  72  THR THR L . n 
C 3 73  LEU 73  73  73  LEU LEU L . n 
C 3 74  THR 74  74  74  THR THR L . n 
C 3 75  ILE 75  75  75  ILE ILE L . n 
C 3 76  ARG 76  76  76  ARG ARG L . n 
C 3 77  SER 77  77  77  SER SER L . n 
C 3 78  LEU 78  78  78  LEU LEU L . n 
C 3 79  GLN 79  79  79  GLN GLN L . n 
C 3 80  PRO 80  80  80  PRO PRO L . n 
C 3 81  GLU 81  81  81  GLU GLU L . n 
C 3 82  ASP 82  82  82  ASP ASP L . n 
C 3 83  PHE 83  83  83  PHE PHE L . n 
C 3 84  ALA 84  84  84  ALA ALA L . n 
C 3 85  THR 85  85  85  THR THR L . n 
C 3 86  TYR 86  86  86  TYR TYR L . n 
C 3 87  TYR 87  87  87  TYR TYR L . n 
C 3 88  CYS 88  88  88  CYS CYS L . n 
C 3 89  GLN 89  89  89  GLN GLN L . n 
C 3 90  GLN 90  90  90  GLN GLN L . n 
C 3 91  SER 91  91  91  SER SER L . n 
C 3 92  TYR 92  92  92  TYR TYR L . n 
C 3 93  ASN 93  93  93  ASN ASN L . n 
C 3 94  THR 94  94  94  THR THR L . n 
C 3 95  PRO 95  95  95  PRO PRO L . n 
C 3 96  PRO 96  96  96  PRO PRO L . n 
C 3 97  THR 97  97  97  THR THR L . n 
C 3 98  PHE 98  98  98  PHE PHE L . n 
C 3 99  GLY 99  99  99  GLY GLY L . n 
C 3 100 GLN 100 100 100 GLN GLN L . n 
C 3 101 GLY 101 101 101 GLY GLY L . n 
C 3 102 THR 102 102 102 THR THR L . n 
C 3 103 LYS 103 103 103 LYS LYS L . n 
C 3 104 VAL 104 104 104 VAL VAL L . n 
C 3 105 GLU 105 105 105 GLU GLU L . n 
C 3 106 ILE 106 106 106 ILE ILE L . n 
C 3 107 LYS 107 107 107 LYS LYS L . n 
C 3 108 ARG 108 108 108 ARG ARG L . n 
C 3 109 THR 109 109 109 THR THR L . n 
C 3 110 VAL 110 110 110 VAL VAL L . n 
C 3 111 ALA 111 111 111 ALA ALA L . n 
C 3 112 ALA 112 112 112 ALA ALA L . n 
C 3 113 PRO 113 113 113 PRO PRO L . n 
C 3 114 SER 114 114 114 SER SER L . n 
C 3 115 VAL 115 115 115 VAL VAL L . n 
C 3 116 PHE 116 116 116 PHE PHE L . n 
C 3 117 ILE 117 117 117 ILE ILE L . n 
C 3 118 PHE 118 118 118 PHE PHE L . n 
C 3 119 PRO 119 119 119 PRO PRO L . n 
C 3 120 PRO 120 120 120 PRO PRO L . n 
C 3 121 SER 121 121 121 SER SER L . n 
C 3 122 ASP 122 122 122 ASP ASP L . n 
C 3 123 GLU 123 123 123 GLU GLU L . n 
C 3 124 GLN 124 124 124 GLN GLN L . n 
C 3 125 LEU 125 125 125 LEU LEU L . n 
C 3 126 LYS 126 126 126 LYS LYS L . n 
C 3 127 SER 127 127 127 SER SER L . n 
C 3 128 GLY 128 128 128 GLY GLY L . n 
C 3 129 THR 129 129 129 THR THR L . n 
C 3 130 ALA 130 130 130 ALA ALA L . n 
C 3 131 SER 131 131 131 SER SER L . n 
C 3 132 VAL 132 132 132 VAL VAL L . n 
C 3 133 VAL 133 133 133 VAL VAL L . n 
C 3 134 CYS 134 134 134 CYS CYS L . n 
C 3 135 LEU 135 135 135 LEU LEU L . n 
C 3 136 LEU 136 136 136 LEU LEU L . n 
C 3 137 ASN 137 137 137 ASN ASN L . n 
C 3 138 ASN 138 138 138 ASN ASN L . n 
C 3 139 PHE 139 139 139 PHE PHE L . n 
C 3 140 TYR 140 140 140 TYR TYR L . n 
C 3 141 PRO 141 141 141 PRO PRO L . n 
C 3 142 ARG 142 142 142 ARG ARG L . n 
C 3 143 GLU 143 143 143 GLU GLU L . n 
C 3 144 ALA 144 144 144 ALA ALA L . n 
C 3 145 LYS 145 145 145 LYS LYS L . n 
C 3 146 VAL 146 146 146 VAL VAL L . n 
C 3 147 GLN 147 147 147 GLN GLN L . n 
C 3 148 TRP 148 148 148 TRP TRP L . n 
C 3 149 LYS 149 149 149 LYS LYS L . n 
C 3 150 VAL 150 150 150 VAL VAL L . n 
C 3 151 ASP 151 151 151 ASP ASP L . n 
C 3 152 ASN 152 152 152 ASN ASN L . n 
C 3 153 ALA 153 153 153 ALA ALA L . n 
C 3 154 LEU 154 154 154 LEU LEU L . n 
C 3 155 GLN 155 155 155 GLN GLN L . n 
C 3 156 SER 156 156 156 SER SER L . n 
C 3 157 GLY 157 157 157 GLY GLY L . n 
C 3 158 ASN 158 158 158 ASN ASN L . n 
C 3 159 SER 159 159 159 SER SER L . n 
C 3 160 GLN 160 160 160 GLN GLN L . n 
C 3 161 GLU 161 161 161 GLU GLU L . n 
C 3 162 SER 162 162 162 SER SER L . n 
C 3 163 VAL 163 163 163 VAL VAL L . n 
C 3 164 THR 164 164 164 THR THR L . n 
C 3 165 GLU 165 165 165 GLU GLU L . n 
C 3 166 GLN 166 166 166 GLN GLN L . n 
C 3 167 ASP 167 167 167 ASP ASP L . n 
C 3 168 SER 168 168 168 SER SER L . n 
C 3 169 LYS 169 169 169 LYS LYS L . n 
C 3 170 ASP 170 170 170 ASP ASP L . n 
C 3 171 SER 171 171 171 SER SER L . n 
C 3 172 THR 172 172 172 THR THR L . n 
C 3 173 TYR 173 173 173 TYR TYR L . n 
C 3 174 SER 174 174 174 SER SER L . n 
C 3 175 LEU 175 175 175 LEU LEU L . n 
C 3 176 SER 176 176 176 SER SER L . n 
C 3 177 SER 177 177 177 SER SER L . n 
C 3 178 THR 178 178 178 THR THR L . n 
C 3 179 LEU 179 179 179 LEU LEU L . n 
C 3 180 THR 180 180 180 THR THR L . n 
C 3 181 LEU 181 181 181 LEU LEU L . n 
C 3 182 SER 182 182 182 SER SER L . n 
C 3 183 LYS 183 183 183 LYS LYS L . n 
C 3 184 ALA 184 184 184 ALA ALA L . n 
C 3 185 ASP 185 185 185 ASP ASP L . n 
C 3 186 TYR 186 186 186 TYR TYR L . n 
C 3 187 GLU 187 187 187 GLU GLU L . n 
C 3 188 LYS 188 188 188 LYS LYS L . n 
C 3 189 HIS 189 189 189 HIS HIS L . n 
C 3 190 LYS 190 190 190 LYS LYS L . n 
C 3 191 VAL 191 191 191 VAL VAL L . n 
C 3 192 TYR 192 192 192 TYR TYR L . n 
C 3 193 ALA 193 193 193 ALA ALA L . n 
C 3 194 CYS 194 194 194 CYS CYS L . n 
C 3 195 GLU 195 195 195 GLU GLU L . n 
C 3 196 VAL 196 196 196 VAL VAL L . n 
C 3 197 THR 197 197 197 THR THR L . n 
C 3 198 HIS 198 198 198 HIS HIS L . n 
C 3 199 GLN 199 199 199 GLN GLN L . n 
C 3 200 GLY 200 200 200 GLY GLY L . n 
C 3 201 LEU 201 201 201 LEU LEU L . n 
C 3 202 SER 202 202 202 SER SER L . n 
C 3 203 SER 203 203 203 SER SER L . n 
C 3 204 PRO 204 204 204 PRO PRO L . n 
C 3 205 VAL 205 205 205 VAL VAL L . n 
C 3 206 THR 206 206 206 THR THR L . n 
C 3 207 LYS 207 207 207 LYS LYS L . n 
C 3 208 SER 208 208 208 SER SER L . n 
C 3 209 PHE 209 209 209 PHE PHE L . n 
C 3 210 ASN 210 210 210 ASN ASN L . n 
C 3 211 ARG 211 211 211 ARG ARG L . n 
C 3 212 GLY 212 212 212 GLY GLY L . n 
C 3 213 GLU 213 213 213 GLU GLU L . n 
C 3 214 CYS 214 214 214 CYS CYS L . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PEG ? ? PEG ? ? 'SUBJECT OF INVESTIGATION' ? 
3 K   ? ? K   ? ? 'SUBJECT OF INVESTIGATION' ? 
4 EDO ? ? EDO ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
D  4 NAG 1   301 300 NAG NAG B . 
E  5 EDO 1   302 301 EDO EDO B . 
F  5 EDO 1   303 302 EDO EDO B . 
G  5 EDO 1   304 303 EDO EDO B . 
H  5 EDO 1   305 304 EDO EDO B . 
I  5 EDO 1   306 305 EDO EDO B . 
J  5 EDO 1   307 306 EDO EDO B . 
K  5 EDO 1   308 307 EDO EDO B . 
L  5 EDO 1   309 308 EDO EDO B . 
M  5 EDO 1   310 309 EDO EDO B . 
N  5 EDO 1   311 310 EDO EDO B . 
O  6 PEG 1   312 311 PEG PEG B . 
P  6 PEG 1   313 312 PEG PEG B . 
Q  5 EDO 1   314 313 EDO EDO B . 
R  5 EDO 1   315 314 EDO EDO B . 
S  5 EDO 1   316 315 EDO EDO B . 
T  7 K   1   317 4   K   K   B . 
U  7 K   1   318 5   K   K   B . 
V  7 K   1   319 6   K   K   B . 
W  7 K   1   320 7   K   K   B . 
X  7 K   1   321 8   K   K   B . 
Y  5 EDO 1   301 301 EDO EDO H . 
Z  5 EDO 1   302 302 EDO EDO H . 
AA 5 EDO 1   303 303 EDO EDO H . 
BA 6 PEG 1   304 304 PEG PEG H . 
CA 5 EDO 1   305 679 EDO EDO H . 
DA 5 EDO 1   301 301 EDO EDO L . 
EA 5 EDO 1   302 302 EDO EDO L . 
FA 5 EDO 1   303 303 EDO EDO L . 
GA 5 EDO 1   304 304 EDO EDO L . 
HA 5 EDO 1   305 305 EDO EDO L . 
IA 5 EDO 1   306 306 EDO EDO L . 
JA 7 K   1   307 3   K   K   L . 
KA 7 K   1   308 9   K   K   L . 
LA 8 HOH 1   401 489 HOH HOH B . 
LA 8 HOH 2   402 166 HOH HOH B . 
LA 8 HOH 3   403 420 HOH HOH B . 
LA 8 HOH 4   404 370 HOH HOH B . 
LA 8 HOH 5   405 270 HOH HOH B . 
LA 8 HOH 6   406 358 HOH HOH B . 
LA 8 HOH 7   407 156 HOH HOH B . 
LA 8 HOH 8   408 168 HOH HOH B . 
LA 8 HOH 9   409 10  HOH HOH B . 
LA 8 HOH 10  410 71  HOH HOH B . 
LA 8 HOH 11  411 466 HOH HOH B . 
LA 8 HOH 12  412 30  HOH HOH B . 
LA 8 HOH 13  413 21  HOH HOH B . 
LA 8 HOH 14  414 157 HOH HOH B . 
LA 8 HOH 15  415 153 HOH HOH B . 
LA 8 HOH 16  416 203 HOH HOH B . 
LA 8 HOH 17  417 253 HOH HOH B . 
LA 8 HOH 18  418 498 HOH HOH B . 
LA 8 HOH 19  419 6   HOH HOH B . 
LA 8 HOH 20  420 278 HOH HOH B . 
LA 8 HOH 21  421 206 HOH HOH B . 
LA 8 HOH 22  422 27  HOH HOH B . 
LA 8 HOH 23  423 11  HOH HOH B . 
LA 8 HOH 24  424 131 HOH HOH B . 
LA 8 HOH 25  425 165 HOH HOH B . 
LA 8 HOH 26  426 94  HOH HOH B . 
LA 8 HOH 27  427 34  HOH HOH B . 
LA 8 HOH 28  428 297 HOH HOH B . 
LA 8 HOH 29  429 17  HOH HOH B . 
LA 8 HOH 30  430 76  HOH HOH B . 
LA 8 HOH 31  431 78  HOH HOH B . 
LA 8 HOH 32  432 61  HOH HOH B . 
LA 8 HOH 33  433 316 HOH HOH B . 
LA 8 HOH 34  434 485 HOH HOH B . 
LA 8 HOH 35  435 151 HOH HOH B . 
LA 8 HOH 36  436 144 HOH HOH B . 
LA 8 HOH 37  437 42  HOH HOH B . 
LA 8 HOH 38  438 33  HOH HOH B . 
LA 8 HOH 39  439 140 HOH HOH B . 
LA 8 HOH 40  440 145 HOH HOH B . 
LA 8 HOH 41  441 252 HOH HOH B . 
LA 8 HOH 42  442 287 HOH HOH B . 
LA 8 HOH 43  443 112 HOH HOH B . 
LA 8 HOH 44  444 64  HOH HOH B . 
LA 8 HOH 45  445 483 HOH HOH B . 
LA 8 HOH 46  446 208 HOH HOH B . 
LA 8 HOH 47  447 196 HOH HOH B . 
LA 8 HOH 48  448 291 HOH HOH B . 
LA 8 HOH 49  449 40  HOH HOH B . 
LA 8 HOH 50  450 351 HOH HOH B . 
LA 8 HOH 51  451 452 HOH HOH B . 
LA 8 HOH 52  452 102 HOH HOH B . 
LA 8 HOH 53  453 254 HOH HOH B . 
LA 8 HOH 54  454 46  HOH HOH B . 
LA 8 HOH 55  455 22  HOH HOH B . 
LA 8 HOH 56  456 501 HOH HOH B . 
LA 8 HOH 57  457 80  HOH HOH B . 
LA 8 HOH 58  458 12  HOH HOH B . 
LA 8 HOH 59  459 217 HOH HOH B . 
LA 8 HOH 60  460 38  HOH HOH B . 
LA 8 HOH 61  461 462 HOH HOH B . 
LA 8 HOH 62  462 104 HOH HOH B . 
LA 8 HOH 63  463 65  HOH HOH B . 
LA 8 HOH 64  464 4   HOH HOH B . 
LA 8 HOH 65  465 47  HOH HOH B . 
LA 8 HOH 66  466 28  HOH HOH B . 
LA 8 HOH 67  467 223 HOH HOH B . 
LA 8 HOH 68  468 123 HOH HOH B . 
LA 8 HOH 69  469 273 HOH HOH B . 
LA 8 HOH 70  470 44  HOH HOH B . 
LA 8 HOH 71  471 53  HOH HOH B . 
LA 8 HOH 72  472 15  HOH HOH B . 
LA 8 HOH 73  473 82  HOH HOH B . 
LA 8 HOH 74  474 212 HOH HOH B . 
LA 8 HOH 75  475 108 HOH HOH B . 
LA 8 HOH 76  476 1   HOH HOH B . 
LA 8 HOH 77  477 158 HOH HOH B . 
LA 8 HOH 78  478 304 HOH HOH B . 
LA 8 HOH 79  479 302 HOH HOH B . 
LA 8 HOH 80  480 442 HOH HOH B . 
LA 8 HOH 81  481 244 HOH HOH B . 
LA 8 HOH 82  482 26  HOH HOH B . 
LA 8 HOH 83  483 444 HOH HOH B . 
LA 8 HOH 84  484 69  HOH HOH B . 
LA 8 HOH 85  485 125 HOH HOH B . 
LA 8 HOH 86  486 137 HOH HOH B . 
LA 8 HOH 87  487 463 HOH HOH B . 
LA 8 HOH 88  488 41  HOH HOH B . 
LA 8 HOH 89  489 23  HOH HOH B . 
LA 8 HOH 90  490 189 HOH HOH B . 
LA 8 HOH 91  491 184 HOH HOH B . 
LA 8 HOH 92  492 436 HOH HOH B . 
LA 8 HOH 93  493 183 HOH HOH B . 
LA 8 HOH 94  494 215 HOH HOH B . 
LA 8 HOH 95  495 176 HOH HOH B . 
LA 8 HOH 96  496 221 HOH HOH B . 
LA 8 HOH 97  497 18  HOH HOH B . 
LA 8 HOH 98  498 209 HOH HOH B . 
LA 8 HOH 99  499 240 HOH HOH B . 
LA 8 HOH 100 500 314 HOH HOH B . 
LA 8 HOH 101 501 234 HOH HOH B . 
LA 8 HOH 102 502 440 HOH HOH B . 
LA 8 HOH 103 503 185 HOH HOH B . 
LA 8 HOH 104 504 450 HOH HOH B . 
LA 8 HOH 105 505 327 HOH HOH B . 
LA 8 HOH 106 506 410 HOH HOH B . 
LA 8 HOH 107 507 218 HOH HOH B . 
LA 8 HOH 108 508 86  HOH HOH B . 
LA 8 HOH 109 509 325 HOH HOH B . 
LA 8 HOH 110 510 36  HOH HOH B . 
LA 8 HOH 111 511 211 HOH HOH B . 
LA 8 HOH 112 512 177 HOH HOH B . 
LA 8 HOH 113 513 313 HOH HOH B . 
LA 8 HOH 114 514 312 HOH HOH B . 
LA 8 HOH 115 515 353 HOH HOH B . 
LA 8 HOH 116 516 481 HOH HOH B . 
LA 8 HOH 117 517 425 HOH HOH B . 
LA 8 HOH 118 518 469 HOH HOH B . 
LA 8 HOH 119 519 401 HOH HOH B . 
LA 8 HOH 120 520 318 HOH HOH B . 
LA 8 HOH 121 521 443 HOH HOH B . 
LA 8 HOH 122 522 477 HOH HOH B . 
LA 8 HOH 123 523 311 HOH HOH B . 
LA 8 HOH 124 524 441 HOH HOH B . 
LA 8 HOH 125 525 449 HOH HOH B . 
LA 8 HOH 126 526 412 HOH HOH B . 
LA 8 HOH 127 527 389 HOH HOH B . 
LA 8 HOH 128 528 279 HOH HOH B . 
LA 8 HOH 129 529 378 HOH HOH B . 
LA 8 HOH 130 530 363 HOH HOH B . 
LA 8 HOH 131 531 161 HOH HOH B . 
LA 8 HOH 132 532 486 HOH HOH B . 
LA 8 HOH 133 533 332 HOH HOH B . 
LA 8 HOH 134 534 132 HOH HOH B . 
LA 8 HOH 135 535 330 HOH HOH B . 
LA 8 HOH 136 536 306 HOH HOH B . 
LA 8 HOH 137 537 180 HOH HOH B . 
LA 8 HOH 138 538 470 HOH HOH B . 
LA 8 HOH 139 539 111 HOH HOH B . 
LA 8 HOH 140 540 406 HOH HOH B . 
LA 8 HOH 141 541 267 HOH HOH B . 
LA 8 HOH 142 542 274 HOH HOH B . 
LA 8 HOH 143 543 232 HOH HOH B . 
LA 8 HOH 144 544 175 HOH HOH B . 
LA 8 HOH 145 545 321 HOH HOH B . 
LA 8 HOH 146 546 366 HOH HOH B . 
LA 8 HOH 147 547 413 HOH HOH B . 
LA 8 HOH 148 548 382 HOH HOH B . 
LA 8 HOH 149 549 239 HOH HOH B . 
LA 8 HOH 150 550 372 HOH HOH B . 
LA 8 HOH 151 551 100 HOH HOH B . 
LA 8 HOH 152 552 225 HOH HOH B . 
LA 8 HOH 153 553 301 HOH HOH B . 
LA 8 HOH 154 554 90  HOH HOH B . 
LA 8 HOH 155 555 376 HOH HOH B . 
LA 8 HOH 156 556 453 HOH HOH B . 
LA 8 HOH 157 557 416 HOH HOH B . 
LA 8 HOH 158 558 421 HOH HOH B . 
MA 8 HOH 1   401 295 HOH HOH H . 
MA 8 HOH 2   402 352 HOH HOH H . 
MA 8 HOH 3   403 247 HOH HOH H . 
MA 8 HOH 4   404 385 HOH HOH H . 
MA 8 HOH 5   405 66  HOH HOH H . 
MA 8 HOH 6   406 235 HOH HOH H . 
MA 8 HOH 7   407 361 HOH HOH H . 
MA 8 HOH 8   408 32  HOH HOH H . 
MA 8 HOH 9   409 407 HOH HOH H . 
MA 8 HOH 10  410 194 HOH HOH H . 
MA 8 HOH 11  411 495 HOH HOH H . 
MA 8 HOH 12  412 198 HOH HOH H . 
MA 8 HOH 13  413 169 HOH HOH H . 
MA 8 HOH 14  414 143 HOH HOH H . 
MA 8 HOH 15  415 116 HOH HOH H . 
MA 8 HOH 16  416 222 HOH HOH H . 
MA 8 HOH 17  417 280 HOH HOH H . 
MA 8 HOH 18  418 101 HOH HOH H . 
MA 8 HOH 19  419 85  HOH HOH H . 
MA 8 HOH 20  420 95  HOH HOH H . 
MA 8 HOH 21  421 167 HOH HOH H . 
MA 8 HOH 22  422 119 HOH HOH H . 
MA 8 HOH 23  423 115 HOH HOH H . 
MA 8 HOH 24  424 187 HOH HOH H . 
MA 8 HOH 25  425 263 HOH HOH H . 
MA 8 HOH 26  426 250 HOH HOH H . 
MA 8 HOH 27  427 488 HOH HOH H . 
MA 8 HOH 28  428 92  HOH HOH H . 
MA 8 HOH 29  429 37  HOH HOH H . 
MA 8 HOH 30  430 290 HOH HOH H . 
MA 8 HOH 31  431 56  HOH HOH H . 
MA 8 HOH 32  432 147 HOH HOH H . 
MA 8 HOH 33  433 98  HOH HOH H . 
MA 8 HOH 34  434 210 HOH HOH H . 
MA 8 HOH 35  435 68  HOH HOH H . 
MA 8 HOH 36  436 159 HOH HOH H . 
MA 8 HOH 37  437 127 HOH HOH H . 
MA 8 HOH 38  438 400 HOH HOH H . 
MA 8 HOH 39  439 192 HOH HOH H . 
MA 8 HOH 40  440 238 HOH HOH H . 
MA 8 HOH 41  441 377 HOH HOH H . 
MA 8 HOH 42  442 236 HOH HOH H . 
MA 8 HOH 43  443 308 HOH HOH H . 
MA 8 HOH 44  444 317 HOH HOH H . 
MA 8 HOH 45  445 109 HOH HOH H . 
MA 8 HOH 46  446 87  HOH HOH H . 
MA 8 HOH 47  447 246 HOH HOH H . 
MA 8 HOH 48  448 231 HOH HOH H . 
MA 8 HOH 49  449 497 HOH HOH H . 
MA 8 HOH 50  450 315 HOH HOH H . 
MA 8 HOH 51  451 63  HOH HOH H . 
MA 8 HOH 52  452 257 HOH HOH H . 
MA 8 HOH 53  453 393 HOH HOH H . 
MA 8 HOH 54  454 19  HOH HOH H . 
MA 8 HOH 55  455 199 HOH HOH H . 
MA 8 HOH 56  456 422 HOH HOH H . 
MA 8 HOH 57  457 105 HOH HOH H . 
MA 8 HOH 58  458 89  HOH HOH H . 
MA 8 HOH 59  459 114 HOH HOH H . 
MA 8 HOH 60  460 283 HOH HOH H . 
MA 8 HOH 61  461 379 HOH HOH H . 
MA 8 HOH 62  462 117 HOH HOH H . 
MA 8 HOH 63  463 276 HOH HOH H . 
MA 8 HOH 64  464 195 HOH HOH H . 
MA 8 HOH 65  465 43  HOH HOH H . 
MA 8 HOH 66  466 62  HOH HOH H . 
MA 8 HOH 67  467 336 HOH HOH H . 
MA 8 HOH 68  468 220 HOH HOH H . 
MA 8 HOH 69  469 228 HOH HOH H . 
MA 8 HOH 70  470 51  HOH HOH H . 
MA 8 HOH 71  471 339 HOH HOH H . 
MA 8 HOH 72  472 473 HOH HOH H . 
MA 8 HOH 73  473 265 HOH HOH H . 
MA 8 HOH 74  474 305 HOH HOH H . 
MA 8 HOH 75  475 45  HOH HOH H . 
MA 8 HOH 76  476 164 HOH HOH H . 
MA 8 HOH 77  477 124 HOH HOH H . 
MA 8 HOH 78  478 58  HOH HOH H . 
MA 8 HOH 79  479 373 HOH HOH H . 
MA 8 HOH 80  480 133 HOH HOH H . 
MA 8 HOH 81  481 266 HOH HOH H . 
MA 8 HOH 82  482 296 HOH HOH H . 
MA 8 HOH 83  483 455 HOH HOH H . 
MA 8 HOH 84  484 171 HOH HOH H . 
MA 8 HOH 85  485 16  HOH HOH H . 
MA 8 HOH 86  486 360 HOH HOH H . 
MA 8 HOH 87  487 120 HOH HOH H . 
MA 8 HOH 88  488 191 HOH HOH H . 
MA 8 HOH 89  489 73  HOH HOH H . 
MA 8 HOH 90  490 190 HOH HOH H . 
MA 8 HOH 91  491 300 HOH HOH H . 
MA 8 HOH 92  492 396 HOH HOH H . 
MA 8 HOH 93  493 356 HOH HOH H . 
MA 8 HOH 94  494 245 HOH HOH H . 
MA 8 HOH 95  495 326 HOH HOH H . 
MA 8 HOH 96  496 359 HOH HOH H . 
MA 8 HOH 97  497 110 HOH HOH H . 
MA 8 HOH 98  498 309 HOH HOH H . 
MA 8 HOH 99  499 237 HOH HOH H . 
MA 8 HOH 100 500 354 HOH HOH H . 
MA 8 HOH 101 501 173 HOH HOH H . 
MA 8 HOH 102 502 415 HOH HOH H . 
MA 8 HOH 103 503 323 HOH HOH H . 
MA 8 HOH 104 504 186 HOH HOH H . 
MA 8 HOH 105 505 374 HOH HOH H . 
MA 8 HOH 106 506 408 HOH HOH H . 
MA 8 HOH 107 507 369 HOH HOH H . 
MA 8 HOH 108 508 345 HOH HOH H . 
MA 8 HOH 109 509 233 HOH HOH H . 
MA 8 HOH 110 510 284 HOH HOH H . 
MA 8 HOH 111 511 468 HOH HOH H . 
MA 8 HOH 112 512 154 HOH HOH H . 
MA 8 HOH 113 513 350 HOH HOH H . 
MA 8 HOH 114 514 2   HOH HOH H . 
MA 8 HOH 115 515 182 HOH HOH H . 
MA 8 HOH 116 516 242 HOH HOH H . 
MA 8 HOH 117 517 333 HOH HOH H . 
MA 8 HOH 118 518 456 HOH HOH H . 
MA 8 HOH 119 519 251 HOH HOH H . 
MA 8 HOH 120 520 446 HOH HOH H . 
MA 8 HOH 121 521 249 HOH HOH H . 
MA 8 HOH 122 522 414 HOH HOH H . 
MA 8 HOH 123 523 357 HOH HOH H . 
MA 8 HOH 124 524 496 HOH HOH H . 
MA 8 HOH 125 525 399 HOH HOH H . 
MA 8 HOH 126 526 492 HOH HOH H . 
MA 8 HOH 127 527 179 HOH HOH H . 
MA 8 HOH 128 528 99  HOH HOH H . 
MA 8 HOH 129 529 310 HOH HOH H . 
MA 8 HOH 130 530 499 HOH HOH H . 
MA 8 HOH 131 531 349 HOH HOH H . 
MA 8 HOH 132 532 331 HOH HOH H . 
MA 8 HOH 133 533 128 HOH HOH H . 
MA 8 HOH 134 534 107 HOH HOH H . 
MA 8 HOH 135 535 241 HOH HOH H . 
MA 8 HOH 136 536 419 HOH HOH H . 
MA 8 HOH 137 537 172 HOH HOH H . 
MA 8 HOH 138 538 122 HOH HOH H . 
NA 8 HOH 1   401 362 HOH HOH L . 
NA 8 HOH 2   402 365 HOH HOH L . 
NA 8 HOH 3   403 482 HOH HOH L . 
NA 8 HOH 4   404 134 HOH HOH L . 
NA 8 HOH 5   405 341 HOH HOH L . 
NA 8 HOH 6   406 226 HOH HOH L . 
NA 8 HOH 7   407 83  HOH HOH L . 
NA 8 HOH 8   408 35  HOH HOH L . 
NA 8 HOH 9   409 193 HOH HOH L . 
NA 8 HOH 10  410 118 HOH HOH L . 
NA 8 HOH 11  411 96  HOH HOH L . 
NA 8 HOH 12  412 126 HOH HOH L . 
NA 8 HOH 13  413 149 HOH HOH L . 
NA 8 HOH 14  414 346 HOH HOH L . 
NA 8 HOH 15  415 320 HOH HOH L . 
NA 8 HOH 16  416 97  HOH HOH L . 
NA 8 HOH 17  417 152 HOH HOH L . 
NA 8 HOH 18  418 3   HOH HOH L . 
NA 8 HOH 19  419 142 HOH HOH L . 
NA 8 HOH 20  420 141 HOH HOH L . 
NA 8 HOH 21  421 72  HOH HOH L . 
NA 8 HOH 22  422 394 HOH HOH L . 
NA 8 HOH 23  423 54  HOH HOH L . 
NA 8 HOH 24  424 319 HOH HOH L . 
NA 8 HOH 25  425 48  HOH HOH L . 
NA 8 HOH 26  426 367 HOH HOH L . 
NA 8 HOH 27  427 31  HOH HOH L . 
NA 8 HOH 28  428 207 HOH HOH L . 
NA 8 HOH 29  429 256 HOH HOH L . 
NA 8 HOH 30  430 139 HOH HOH L . 
NA 8 HOH 31  431 286 HOH HOH L . 
NA 8 HOH 32  432 24  HOH HOH L . 
NA 8 HOH 33  433 491 HOH HOH L . 
NA 8 HOH 34  434 74  HOH HOH L . 
NA 8 HOH 35  435 52  HOH HOH L . 
NA 8 HOH 36  436 433 HOH HOH L . 
NA 8 HOH 37  437 381 HOH HOH L . 
NA 8 HOH 38  438 103 HOH HOH L . 
NA 8 HOH 39  439 7   HOH HOH L . 
NA 8 HOH 40  440 129 HOH HOH L . 
NA 8 HOH 41  441 368 HOH HOH L . 
NA 8 HOH 42  442 70  HOH HOH L . 
NA 8 HOH 43  443 77  HOH HOH L . 
NA 8 HOH 44  444 429 HOH HOH L . 
NA 8 HOH 45  445 403 HOH HOH L . 
NA 8 HOH 46  446 229 HOH HOH L . 
NA 8 HOH 47  447 135 HOH HOH L . 
NA 8 HOH 48  448 29  HOH HOH L . 
NA 8 HOH 49  449 59  HOH HOH L . 
NA 8 HOH 50  450 136 HOH HOH L . 
NA 8 HOH 51  451 39  HOH HOH L . 
NA 8 HOH 52  452 347 HOH HOH L . 
NA 8 HOH 53  453 1   HOH HOH L . 
NA 8 HOH 54  454 60  HOH HOH L . 
NA 8 HOH 55  455 467 HOH HOH L . 
NA 8 HOH 56  456 248 HOH HOH L . 
NA 8 HOH 57  457 163 HOH HOH L . 
NA 8 HOH 58  458 383 HOH HOH L . 
NA 8 HOH 59  459 75  HOH HOH L . 
NA 8 HOH 60  460 384 HOH HOH L . 
NA 8 HOH 61  461 480 HOH HOH L . 
NA 8 HOH 62  462 8   HOH HOH L . 
NA 8 HOH 63  463 205 HOH HOH L . 
NA 8 HOH 64  464 338 HOH HOH L . 
NA 8 HOH 65  465 260 HOH HOH L . 
NA 8 HOH 66  466 25  HOH HOH L . 
NA 8 HOH 67  467 5   HOH HOH L . 
NA 8 HOH 68  468 342 HOH HOH L . 
NA 8 HOH 69  469 170 HOH HOH L . 
NA 8 HOH 70  470 474 HOH HOH L . 
NA 8 HOH 71  471 294 HOH HOH L . 
NA 8 HOH 72  472 91  HOH HOH L . 
NA 8 HOH 73  473 50  HOH HOH L . 
NA 8 HOH 74  474 155 HOH HOH L . 
NA 8 HOH 75  475 230 HOH HOH L . 
NA 8 HOH 76  476 130 HOH HOH L . 
NA 8 HOH 77  477 13  HOH HOH L . 
NA 8 HOH 78  478 322 HOH HOH L . 
NA 8 HOH 79  479 299 HOH HOH L . 
NA 8 HOH 80  480 213 HOH HOH L . 
NA 8 HOH 81  481 335 HOH HOH L . 
NA 8 HOH 82  482 343 HOH HOH L . 
NA 8 HOH 83  483 285 HOH HOH L . 
NA 8 HOH 84  484 269 HOH HOH L . 
NA 8 HOH 85  485 93  HOH HOH L . 
NA 8 HOH 86  486 181 HOH HOH L . 
NA 8 HOH 87  487 292 HOH HOH L . 
NA 8 HOH 88  488 188 HOH HOH L . 
NA 8 HOH 89  489 431 HOH HOH L . 
NA 8 HOH 90  490 255 HOH HOH L . 
NA 8 HOH 91  491 148 HOH HOH L . 
NA 8 HOH 92  492 121 HOH HOH L . 
NA 8 HOH 93  493 424 HOH HOH L . 
NA 8 HOH 94  494 67  HOH HOH L . 
NA 8 HOH 95  495 202 HOH HOH L . 
NA 8 HOH 96  496 9   HOH HOH L . 
NA 8 HOH 97  497 303 HOH HOH L . 
NA 8 HOH 98  498 334 HOH HOH L . 
NA 8 HOH 99  499 178 HOH HOH L . 
NA 8 HOH 100 500 426 HOH HOH L . 
NA 8 HOH 101 501 395 HOH HOH L . 
NA 8 HOH 102 502 162 HOH HOH L . 
NA 8 HOH 103 503 201 HOH HOH L . 
NA 8 HOH 104 504 49  HOH HOH L . 
NA 8 HOH 105 505 174 HOH HOH L . 
NA 8 HOH 106 506 337 HOH HOH L . 
NA 8 HOH 107 507 282 HOH HOH L . 
NA 8 HOH 108 508 494 HOH HOH L . 
NA 8 HOH 109 509 57  HOH HOH L . 
NA 8 HOH 110 510 268 HOH HOH L . 
NA 8 HOH 111 511 55  HOH HOH L . 
NA 8 HOH 112 512 204 HOH HOH L . 
NA 8 HOH 113 513 459 HOH HOH L . 
NA 8 HOH 114 514 329 HOH HOH L . 
NA 8 HOH 115 515 106 HOH HOH L . 
NA 8 HOH 116 516 20  HOH HOH L . 
NA 8 HOH 117 517 307 HOH HOH L . 
NA 8 HOH 118 518 138 HOH HOH L . 
NA 8 HOH 119 519 150 HOH HOH L . 
NA 8 HOH 120 520 478 HOH HOH L . 
NA 8 HOH 121 521 355 HOH HOH L . 
NA 8 HOH 122 522 293 HOH HOH L . 
NA 8 HOH 123 523 262 HOH HOH L . 
NA 8 HOH 124 524 197 HOH HOH L . 
NA 8 HOH 125 525 272 HOH HOH L . 
NA 8 HOH 126 526 200 HOH HOH L . 
NA 8 HOH 127 527 214 HOH HOH L . 
NA 8 HOH 128 528 227 HOH HOH L . 
NA 8 HOH 129 529 160 HOH HOH L . 
NA 8 HOH 130 530 476 HOH HOH L . 
NA 8 HOH 131 531 445 HOH HOH L . 
NA 8 HOH 132 532 388 HOH HOH L . 
NA 8 HOH 133 533 264 HOH HOH L . 
NA 8 HOH 134 534 298 HOH HOH L . 
NA 8 HOH 135 535 348 HOH HOH L . 
NA 8 HOH 136 536 344 HOH HOH L . 
NA 8 HOH 137 537 390 HOH HOH L . 
NA 8 HOH 138 538 428 HOH HOH L . 
NA 8 HOH 139 539 216 HOH HOH L . 
NA 8 HOH 140 540 328 HOH HOH L . 
NA 8 HOH 141 541 88  HOH HOH L . 
NA 8 HOH 142 542 411 HOH HOH L . 
NA 8 HOH 143 543 146 HOH HOH L . 
NA 8 HOH 144 544 219 HOH HOH L . 
NA 8 HOH 145 545 84  HOH HOH L . 
NA 8 HOH 146 546 364 HOH HOH L . 
NA 8 HOH 147 547 454 HOH HOH L . 
NA 8 HOH 148 548 479 HOH HOH L . 
NA 8 HOH 149 549 375 HOH HOH L . 
NA 8 HOH 150 550 397 HOH HOH L . 
NA 8 HOH 151 551 261 HOH HOH L . 
NA 8 HOH 152 552 243 HOH HOH L . 
NA 8 HOH 153 553 113 HOH HOH L . 
NA 8 HOH 154 554 447 HOH HOH L . 
NA 8 HOH 155 555 398 HOH HOH L . 
NA 8 HOH 156 556 448 HOH HOH L . 
NA 8 HOH 157 557 81  HOH HOH L . 
NA 8 HOH 158 558 271 HOH HOH L . 
NA 8 HOH 159 559 409 HOH HOH L . 
NA 8 HOH 160 560 2   HOH HOH L . 
NA 8 HOH 161 561 458 HOH HOH L . 
NA 8 HOH 162 562 259 HOH HOH L . 
NA 8 HOH 163 563 490 HOH HOH L . 
NA 8 HOH 164 564 392 HOH HOH L . 
NA 8 HOH 165 565 386 HOH HOH L . 
NA 8 HOH 166 566 275 HOH HOH L . 
NA 8 HOH 167 567 281 HOH HOH L . 
NA 8 HOH 168 568 324 HOH HOH L . 
NA 8 HOH 169 569 472 HOH HOH L . 
NA 8 HOH 170 570 288 HOH HOH L . 
NA 8 HOH 171 571 405 HOH HOH L . 
NA 8 HOH 172 572 464 HOH HOH L . 
NA 8 HOH 173 573 402 HOH HOH L . 
NA 8 HOH 174 574 289 HOH HOH L . 
NA 8 HOH 175 575 418 HOH HOH L . 
NA 8 HOH 176 576 380 HOH HOH L . 
NA 8 HOH 177 577 277 HOH HOH L . 
NA 8 HOH 178 578 387 HOH HOH L . 
NA 8 HOH 179 579 475 HOH HOH L . 
NA 8 HOH 180 580 224 HOH HOH L . 
NA 8 HOH 181 581 500 HOH HOH L . 
# 
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   ? ? ? 1-21.2-5419 1 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MER 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     79.533 
_cell.length_a_esd                 ? 
_cell.length_b                     79.533 
_cell.length_b_esd                 ? 
_cell.length_c                     256.452 
_cell.length_c_esd                 ? 
_cell.volume                       1622186.636 
_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                         9MER 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            'P 4nw 2abw' 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MER 
_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             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.97 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M ammonium nitrate, 20% w/v PEG3350' 
_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         2023-02-02 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 22-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          23.83 
_reflns.entry_id                                       9MER 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               46.98 
_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                                     92614 
_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                           97.16 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.6 
_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                                0.031 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.091 
_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                                    2.00 
_reflns_shell.d_res_low                                     2.072 
_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                             4365 
_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                                  0.791 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          78.83 
_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                               30.63 
_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                                 9MER 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             46.98 
_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                     92614 
_refine.ls_number_reflns_R_free                  3357 
_refine.ls_number_reflns_R_work                  89257 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.85 
_refine.ls_percent_reflns_R_free                 3.62 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2062 
_refine.ls_R_factor_R_free                       0.2151 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2059 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.6818 
_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                            0.2179 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        46.98 
_refine_hist.number_atoms_solvent             477 
_refine_hist.number_atoms_total               5661 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5050 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         134 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0142  ? 5339 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.6572  ? 7229 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0930  ? 797  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0092  ? 922  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.7235 ? 1962 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.03  . . 59  1624 38.14 . . . . 0.2864 . . . . . . . . . . . 0.2844 
'X-RAY DIFFRACTION' 2.03 2.06  . . 74  1979 46.38 . . . . 0.2700 . . . . . . . . . . . 0.3127 
'X-RAY DIFFRACTION' 2.06 2.09  . . 87  2264 52.12 . . . . 0.2603 . . . . . . . . . . . 0.3309 
'X-RAY DIFFRACTION' 2.09 2.12  . . 96  2574 60.20 . . . . 0.2373 . . . . . . . . . . . 0.2384 
'X-RAY DIFFRACTION' 2.12 2.16  . . 110 2758 64.96 . . . . 0.2484 . . . . . . . . . . . 0.2788 
'X-RAY DIFFRACTION' 2.16 2.20  . . 110 3015 69.97 . . . . 0.2396 . . . . . . . . . . . 0.3323 
'X-RAY DIFFRACTION' 2.20 2.24  . . 128 3318 78.46 . . . . 0.2435 . . . . . . . . . . . 0.2535 
'X-RAY DIFFRACTION' 2.24 2.29  . . 147 3725 86.08 . . . . 0.2381 . . . . . . . . . . . 0.2484 
'X-RAY DIFFRACTION' 2.29 2.34  . . 156 4013 93.50 . . . . 0.2372 . . . . . . . . . . . 0.2618 
'X-RAY DIFFRACTION' 2.34 2.39  . . 157 4152 97.80 . . . . 0.2420 . . . . . . . . . . . 0.2925 
'X-RAY DIFFRACTION' 2.39 2.45  . . 155 4246 99.73 . . . . 0.2410 . . . . . . . . . . . 0.2722 
'X-RAY DIFFRACTION' 2.45 2.52  . . 166 4275 99.71 . . . . 0.2356 . . . . . . . . . . . 0.2327 
'X-RAY DIFFRACTION' 2.52 2.59  . . 158 4260 99.64 . . . . 0.2274 . . . . . . . . . . . 0.3119 
'X-RAY DIFFRACTION' 2.59 2.67  . . 163 4287 99.75 . . . . 0.2291 . . . . . . . . . . . 0.2377 
'X-RAY DIFFRACTION' 2.67 2.77  . . 158 4265 99.86 . . . . 0.2222 . . . . . . . . . . . 0.2643 
'X-RAY DIFFRACTION' 2.77 2.88  . . 159 4294 99.80 . . . . 0.2220 . . . . . . . . . . . 0.2438 
'X-RAY DIFFRACTION' 2.88 3.01  . . 157 4272 99.86 . . . . 0.2137 . . . . . . . . . . . 0.2339 
'X-RAY DIFFRACTION' 3.01 3.17  . . 163 4286 99.82 . . . . 0.2065 . . . . . . . . . . . 0.2038 
'X-RAY DIFFRACTION' 3.17 3.37  . . 157 4266 99.95 . . . . 0.2010 . . . . . . . . . . . 0.2297 
'X-RAY DIFFRACTION' 3.37 3.63  . . 160 4331 99.93 . . . . 0.1889 . . . . . . . . . . . 0.1758 
'X-RAY DIFFRACTION' 3.63 3.99  . . 157 4261 99.95 . . . . 0.1769 . . . . . . . . . . . 0.1745 
'X-RAY DIFFRACTION' 3.99 4.57  . . 160 4265 99.91 . . . . 0.1633 . . . . . . . . . . . 0.1754 
'X-RAY DIFFRACTION' 4.57 5.76  . . 166 4269 99.69 . . . . 0.1685 . . . . . . . . . . . 0.1375 
'X-RAY DIFFRACTION' 5.76 46.98 . . 154 4258 99.28 . . . . 0.2047 . . . . . . . . . . . 0.1849 
# 
_struct.entry_id                     9MER 
_struct.title                        'Structure of H1H5:FluA20 Chimeric Influenza HA Complex' 
_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        9MER 
_struct_keywords.text            'Influenza, Hemagglutinins, HA, Chimera H1, H5, VIRAL PROTEIN-IMMUNE SYSTEM complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/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 5 ? 
G  N N 5 ? 
H  N N 5 ? 
I  N N 5 ? 
J  N N 5 ? 
K  N N 5 ? 
L  N N 5 ? 
M  N N 5 ? 
N  N N 5 ? 
O  N N 6 ? 
P  N N 6 ? 
Q  N N 5 ? 
R  N N 5 ? 
S  N N 5 ? 
T  N N 7 ? 
U  N N 7 ? 
V  N N 7 ? 
W  N N 7 ? 
X  N N 7 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 5 ? 
BA N N 6 ? 
CA N N 5 ? 
DA N N 5 ? 
EA N N 5 ? 
FA N N 5 ? 
GA N N 5 ? 
HA N N 5 ? 
IA N N 5 ? 
JA N N 7 ? 
KA N N 7 ? 
LA N N 8 ? 
MA N N 8 ? 
NA 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 PDB 9MER 9MER ? 1 ? 1 
2 PDB 9MER 9MER ? 2 ? 1 
3 PDB 9MER 9MER ? 3 ? 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 9MER B 1 ? 227 ? 9MER 52 ? 278 ? 52 278 
2 2 9MER H 1 ? 235 ? 9MER 1  ? 222 ? 1  222 
3 3 9MER L 1 ? 214 ? 9MER 1  ? 214 ? 1  214 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_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,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 9   ? GLY A 16  ? SER B 60  GLY B 67  1 ? 8  
HELX_P HELX_P2  AA2 ASP A 50  ? LEU A 58  ? ASP B 101 LEU B 109 1 ? 9  
HELX_P HELX_P3  AA3 PRO A 71  ? TRP A 76  ? PRO B 122 TRP B 127 1 ? 6  
HELX_P HELX_P4  AA4 ASP A 136 ? HIS A 145 ? ASP B 187 HIS B 196 1 ? 10 
HELX_P HELX_P5  AA5 PRO B 63  ? LYS B 66  ? PRO H 61  LYS H 64  5 ? 4  
HELX_P HELX_P6  AA6 THR B 88  ? THR B 92  ? THR H 83  THR H 87  5 ? 5  
HELX_P HELX_P7  AA7 SER B 169 ? ALA B 171 ? SER H 156 ALA H 158 5 ? 3  
HELX_P HELX_P8  AA8 SER B 200 ? LEU B 202 ? SER H 187 LEU H 189 5 ? 3  
HELX_P HELX_P9  AA9 LYS B 214 ? ASN B 217 ? LYS H 201 ASN H 204 5 ? 4  
HELX_P HELX_P10 AB1 GLN C 79  ? PHE C 83  ? GLN L 79  PHE L 83  5 ? 5  
HELX_P HELX_P11 AB2 SER C 121 ? LYS C 126 ? SER L 121 LYS L 126 1 ? 6  
HELX_P HELX_P12 AB3 LYS C 183 ? GLU C 187 ? LYS L 183 GLU L 187 1 ? 5  
# 
_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 8   SG  ? ? ? 1_555 A  CYS 20  SG ? ? B CYS 59  B CYS 71  1_555 ? ? ? ? ? ? ? 2.022 ? ?               
disulf2 disulf ?   ? A CYS 43  SG  ? ? ? 1_555 A  CYS 88  SG ? ? B CYS 94  B CYS 139 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf3 disulf ?   ? B CYS 22  SG  ? ? ? 1_555 B  CYS 97  SG ? ? H CYS 22  H CYS 92  1_555 ? ? ? ? ? ? ? 2.077 ? ?               
disulf4 disulf ?   ? B CYS 107 SG  ? B ? 1_555 B  CYS 112 SG ? G H CYS 100 H CYS 100 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf5 disulf ?   ? B CYS 153 SG  ? ? ? 1_555 B  CYS 209 SG ? ? H CYS 140 H CYS 196 1_555 ? ? ? ? ? ? ? 2.040 ? ?               
disulf6 disulf ?   ? C CYS 23  SG  ? ? ? 1_555 C  CYS 88  SG ? ? L CYS 23  L CYS 88  1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf7 disulf ?   ? C CYS 134 SG  ? ? ? 1_555 C  CYS 194 SG ? ? L CYS 134 L CYS 194 1_555 ? ? ? ? ? ? ? 2.018 ? ?               
covale1 covale one ? A ASN 40  ND2 ? ? ? 1_555 D  NAG .   C1 ? ? B ASN 91  B NAG 301 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
metalc1 metalc ?   ? A GLN 175 OE1 ? ? ? 1_555 V  K   .   K  ? ? B GLN 226 B K   319 1_555 ? ? ? ? ? ? ? 3.499 ? ?               
metalc2 metalc ?   ? T K   .   K   ? ? ? 1_555 MA HOH .   O  ? ? B K   317 H HOH 468 1_555 ? ? ? ? ? ? ? 3.200 ? ?               
metalc3 metalc ?   ? W K   .   K   ? ? ? 1_555 LA HOH .   O  ? ? B K   320 B HOH 487 1_555 ? ? ? ? ? ? ? 2.842 ? ?               
metalc4 metalc ?   ? C SER 121 OG  ? ? ? 1_555 KA K   .   K  ? ? L SER 121 L K   308 1_555 ? ? ? ? ? ? ? 3.144 ? ?               
metalc5 metalc ?   ? C GLN 124 OE1 ? ? ? 1_555 KA K   .   K  ? ? L GLN 124 L K   308 1_555 ? ? ? ? ? ? ? 2.798 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OG 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   C 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   SER 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    121 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    L 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    SER 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     121 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   K 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   KA 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   K 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    L 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    K 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     308 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   OE1 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   C 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   GLN 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    124 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    L 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    GLN 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     124 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 105.4 
_pdbx_struct_conn_angle.value_esd             ? 
# 
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 NAG D .   ? ASN A 40  ? NAG B 301 ? 1_555 ASN B 91  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 CYS A 8   ? CYS A 20  ? CYS B 59  ? 1_555 CYS B 71  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
3 CYS A 43  ? CYS A 88  ? CYS B 94  ? 1_555 CYS B 139 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS B 22  ? CYS B 97  ? CYS H 22  ? 1_555 CYS H 92  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5 CYS B 107 ? CYS B 112 ? CYS H 100 B 1_555 CYS H 100 G 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6 CYS B 153 ? CYS B 209 ? CYS H 140 ? 1_555 CYS H 196 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7 CYS C 23  ? CYS C 88  ? CYS L 23  ? 1_555 CYS L 88  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS C 134 ? CYS C 194 ? CYS L 134 ? 1_555 CYS L 194 ? 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 PHE 159 B . ? PHE 146 H PRO 160 B ? PRO 147 H 1 -19.11 
2 GLU 161 B . ? GLU 148 H PRO 162 B ? PRO 149 H 1 9.59   
3 SER 7   C . ? SER 7   L PRO 8   C ? PRO 8   L 1 -4.64  
4 TYR 140 C . ? TYR 140 L PRO 141 C ? PRO 141 L 1 2.51   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 6 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 3 ? 
AB3 ? 4 ? 
AB4 ? 6 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 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 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 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 PRO A 2   ? GLN A 4   ? PRO B 53  GLN B 55  
AA1 2 TYR A 31  ? VAL A 33  ? TYR B 82  VAL B 84  
AA2 1 VAL A 61  ? GLU A 68  ? VAL B 112 GLU B 119 
AA2 2 TYR A 205 ? ARG A 211 ? TYR B 256 ARG B 262 
AA2 3 GLU A 124 ? HIS A 133 ? GLU B 175 HIS B 184 
AA2 4 LEU A 200 ? PRO A 203 ? LEU B 251 PRO B 254 
AA2 5 LEU A 100 ? ILE A 104 ? LEU B 151 ILE B 155 
AA2 6 GLU A 80  ? ALA A 81  ? GLU B 131 ALA B 132 
AA3 1 VAL A 61  ? GLU A 68  ? VAL B 112 GLU B 119 
AA3 2 TYR A 205 ? ARG A 211 ? TYR B 256 ARG B 262 
AA3 3 GLU A 124 ? HIS A 133 ? GLU B 175 HIS B 184 
AA3 4 ARG A 178 ? LEU A 186 ? ARG B 229 LEU B 237 
AA4 1 VAL A 85  ? HIS A 90  ? VAL B 136 HIS B 141 
AA4 2 GLU A 93  ? SER A 95  ? GLU B 144 SER B 146 
AA5 1 LEU A 113 ? ALA A 118 ? LEU B 164 ALA B 169 
AA5 2 THR A 191 ? ALA A 196 ? THR B 242 ALA B 247 
AA5 3 VAL A 151 ? VAL A 154 ? VAL B 202 VAL B 205 
AA5 4 SER A 159 ? PHE A 162 ? SER B 210 PHE B 213 
AA6 1 GLN B 3   ? SER B 7   ? GLN H 3   SER H 7   
AA6 2 LEU B 18  ? SER B 25  ? LEU H 18  SER H 25  
AA6 3 GLU B 79  ? LEU B 84  ? GLU H 77  LEU H 82  
AA6 4 VAL B 69  ? ASP B 74  ? VAL H 67  ASP H 72  
AA7 1 LEU B 11  ? VAL B 12  ? LEU H 11  VAL H 12  
AA7 2 THR B 120 ? VAL B 124 ? THR H 107 VAL H 111 
AA7 3 ALA B 93  ? THR B 101 ? ALA H 88  THR H 96  
AA7 4 TYR B 34  ? GLN B 41  ? TYR H 34  GLN H 39  
AA7 5 GLU B 48  ? ILE B 53  ? GLU H 46  ILE H 51  
AA7 6 THR B 59  ? TYR B 61  ? THR H 57  TYR H 59  
AA8 1 LEU B 11  ? VAL B 12  ? LEU H 11  VAL H 12  
AA8 2 THR B 120 ? VAL B 124 ? THR H 107 VAL H 111 
AA8 3 ALA B 93  ? THR B 101 ? ALA H 88  THR H 96  
AA8 4 HIS B 115 ? TRP B 116 ? HIS H 102 TRP H 103 
AA9 1 SER B 133 ? LEU B 137 ? SER H 120 LEU H 124 
AA9 2 THR B 148 ? TYR B 158 ? THR H 135 TYR H 145 
AA9 3 TYR B 189 ? PRO B 198 ? TYR H 176 PRO H 185 
AA9 4 VAL B 176 ? THR B 178 ? VAL H 163 THR H 165 
AB1 1 SER B 133 ? LEU B 137 ? SER H 120 LEU H 124 
AB1 2 THR B 148 ? TYR B 158 ? THR H 135 TYR H 145 
AB1 3 TYR B 189 ? PRO B 198 ? TYR H 176 PRO H 185 
AB1 4 VAL B 182 ? LEU B 183 ? VAL H 169 LEU H 170 
AB2 1 THR B 164 ? TRP B 167 ? THR H 151 TRP H 154 
AB2 2 ILE B 208 ? HIS B 213 ? ILE H 195 HIS H 200 
AB2 3 THR B 218 ? ARG B 223 ? THR H 205 ARG H 210 
AB3 1 MET C 4   ? SER C 7   ? MET L 4   SER L 7   
AB3 2 VAL C 19  ? PRO C 25  ? VAL L 19  PRO L 25  
AB3 3 GLU C 70  ? ILE C 75  ? GLU L 70  ILE L 75  
AB3 4 PHE C 62  ? SER C 67  ? PHE L 62  SER L 67  
AB4 1 SER C 10  ? ALA C 13  ? SER L 10  ALA L 13  
AB4 2 THR C 102 ? ILE C 106 ? THR L 102 ILE L 106 
AB4 3 ALA C 84  ? GLN C 90  ? ALA L 84  GLN L 90  
AB4 4 LEU C 33  ? HIS C 38  ? LEU L 33  HIS L 38  
AB4 5 LYS C 45  ? TYR C 49  ? LYS L 45  TYR L 49  
AB4 6 ASN C 53  ? LEU C 54  ? ASN L 53  LEU L 54  
AB5 1 SER C 10  ? ALA C 13  ? SER L 10  ALA L 13  
AB5 2 THR C 102 ? ILE C 106 ? THR L 102 ILE L 106 
AB5 3 ALA C 84  ? GLN C 90  ? ALA L 84  GLN L 90  
AB5 4 THR C 97  ? PHE C 98  ? THR L 97  PHE L 98  
AB6 1 SER C 114 ? PHE C 118 ? SER L 114 PHE L 118 
AB6 2 THR C 129 ? PHE C 139 ? THR L 129 PHE L 139 
AB6 3 TYR C 173 ? SER C 182 ? TYR L 173 SER L 182 
AB6 4 SER C 159 ? VAL C 163 ? SER L 159 VAL L 163 
AB7 1 ALA C 153 ? LEU C 154 ? ALA L 153 LEU L 154 
AB7 2 LYS C 145 ? VAL C 150 ? LYS L 145 VAL L 150 
AB7 3 VAL C 191 ? THR C 197 ? VAL L 191 THR L 197 
AB7 4 VAL C 205 ? ASN C 210 ? VAL L 205 ASN L 210 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 3   ? N LEU B 54  O TYR A 31  ? O TYR B 82  
AA2 1 2 N GLU A 65  ? N GLU B 116 O ALA A 208 ? O ALA B 259 
AA2 2 3 O PHE A 207 ? O PHE B 258 N LEU A 126 ? N LEU B 177 
AA2 3 4 N GLY A 130 ? N GLY B 181 O ILE A 201 ? O ILE B 252 
AA2 4 5 O ALA A 202 ? O ALA B 253 N LEU A 101 ? N LEU B 152 
AA2 5 6 O ILE A 104 ? O ILE B 155 N GLU A 80  ? N GLU B 131 
AA3 1 2 N GLU A 65  ? N GLU B 116 O ALA A 208 ? O ALA B 259 
AA3 2 3 O PHE A 207 ? O PHE B 258 N LEU A 126 ? N LEU B 177 
AA3 3 4 N HIS A 133 ? N HIS B 184 O ARG A 178 ? O ARG B 229 
AA4 1 2 N VAL A 85  ? N VAL B 136 O SER A 95  ? O SER B 146 
AA5 1 2 N LYS A 115 ? N LYS B 166 O PHE A 194 ? O PHE B 245 
AA5 2 3 O GLU A 195 ? O GLU B 246 N SER A 152 ? N SER B 203 
AA5 3 4 N VAL A 151 ? N VAL B 202 O PHE A 162 ? O PHE B 213 
AA6 1 2 N GLU B 5   ? N GLU H 5   O SER B 23  ? O SER H 23  
AA6 2 3 N LEU B 18  ? N LEU H 18  O LEU B 84  ? O LEU H 82  
AA6 3 4 O ARG B 83  ? O ARG H 81  N THR B 70  ? N THR H 68  
AA7 1 2 N VAL B 12  ? N VAL H 12  O THR B 123 ? O THR H 110 
AA7 2 3 O VAL B 122 ? O VAL H 109 N ALA B 93  ? N ALA H 88  
AA7 3 4 O PHE B 96  ? O PHE H 91  N ILE B 39  ? N ILE H 37  
AA7 4 5 N ARG B 40  ? N ARG H 38  O GLU B 48  ? O GLU H 46  
AA7 5 6 N TYR B 52  ? N TYR H 50  O ASN B 60  ? O ASN H 58  
AA8 1 2 N VAL B 12  ? N VAL H 12  O THR B 123 ? O THR H 110 
AA8 2 3 O VAL B 122 ? O VAL H 109 N ALA B 93  ? N ALA H 88  
AA8 3 4 N ARG B 99  ? N ARG H 94  O HIS B 115 ? O HIS H 102 
AA9 1 2 N LEU B 137 ? N LEU H 124 O GLY B 152 ? O GLY H 139 
AA9 2 3 N VAL B 155 ? N VAL H 142 O LEU B 191 ? O LEU H 178 
AA9 3 4 O VAL B 194 ? O VAL H 181 N HIS B 177 ? N HIS H 164 
AB1 1 2 N LEU B 137 ? N LEU H 124 O GLY B 152 ? O GLY H 139 
AB1 2 3 N VAL B 155 ? N VAL H 142 O LEU B 191 ? O LEU H 178 
AB1 3 4 O SER B 190 ? O SER H 177 N VAL B 182 ? N VAL H 169 
AB2 1 2 N SER B 166 ? N SER H 153 O ASN B 210 ? O ASN H 197 
AB2 2 3 N VAL B 211 ? N VAL H 198 O VAL B 220 ? O VAL H 207 
AB3 1 2 N SER C 7   ? N SER L 7   O THR C 22  ? O THR L 22  
AB3 2 3 N VAL C 19  ? N VAL L 19  O ILE C 75  ? O ILE L 75  
AB3 3 4 O THR C 74  ? O THR L 74  N SER C 63  ? N SER L 63  
AB4 1 2 N LEU C 11  ? N LEU L 11  O GLU C 105 ? O GLU L 105 
AB4 2 3 O VAL C 104 ? O VAL L 104 N ALA C 84  ? N ALA L 84  
AB4 3 4 O TYR C 87  ? O TYR L 87  N PHE C 36  ? N PHE L 36  
AB4 4 5 N GLN C 37  ? N GLN L 37  O LYS C 45  ? O LYS L 45  
AB4 5 6 N TYR C 49  ? N TYR L 49  O ASN C 53  ? O ASN L 53  
AB5 1 2 N LEU C 11  ? N LEU L 11  O GLU C 105 ? O GLU L 105 
AB5 2 3 O VAL C 104 ? O VAL L 104 N ALA C 84  ? N ALA L 84  
AB5 3 4 N GLN C 90  ? N GLN L 90  O THR C 97  ? O THR L 97  
AB6 1 2 N PHE C 116 ? N PHE L 116 O LEU C 135 ? O LEU L 135 
AB6 2 3 N LEU C 136 ? N LEU L 136 O LEU C 175 ? O LEU L 175 
AB6 3 4 O SER C 176 ? O SER L 176 N SER C 162 ? N SER L 162 
AB7 1 2 O ALA C 153 ? O ALA L 153 N VAL C 150 ? N VAL L 150 
AB7 2 3 N LYS C 149 ? N LYS L 149 O ALA C 193 ? O ALA L 193 
AB7 3 4 N VAL C 196 ? N VAL L 196 O VAL C 205 ? O VAL L 205 
# 
_pdbx_entry_details.entry_id                   9MER 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 492 ? ? O B HOH 524 ? ? 1.44 
2  1 O  L HOH 522 ? ? O L HOH 571 ? ? 1.80 
3  1 O  L HOH 564 ? ? O L HOH 569 ? ? 1.82 
4  1 O  L HOH 563 ? ? O L HOH 572 ? ? 1.84 
5  1 O  L HOH 414 ? ? O L HOH 555 ? ? 1.88 
6  1 O  H HOH 522 ? ? O H HOH 536 ? ? 2.04 
7  1 O  B SER 133 ? ? O B HOH 401 ? ? 2.04 
8  1 O  L HOH 422 ? ? O L HOH 562 ? ? 2.07 
9  1 NZ L LYS 145 ? ? O L HOH 401 ? ? 2.11 
10 1 O  L HOH 552 ? ? O L HOH 559 ? ? 2.13 
11 1 NZ L LYS 169 ? ? O L HOH 402 ? ? 2.16 
12 1 O  L HOH 436 ? ? O L HOH 444 ? ? 2.16 
13 1 O  H HOH 492 ? ? O H HOH 523 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     540 
_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    O 
_pdbx_validate_symm_contact.auth_asym_id_2    H 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     471 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_455 
_pdbx_validate_symm_contact.dist              1.92 
# 
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 SER B 146 ? ? -141.44 -157.89 
2  1 ARG B 255 ? ? -120.75 -58.52  
3  1 SER H 15  ? ? 66.26   -4.30   
4  1 LYS H 43  ? ? -124.23 -169.97 
5  1 LYS H 64  ? ? 50.78   -122.80 
6  1 ASP H 98  ? ? -155.41 69.77   
7  1 SER H 130 ? ? -100.27 -160.69 
8  1 ASP H 144 ? ? 61.32   69.97   
9  1 THR H 160 ? ? -130.53 -31.73  
10 1 ARG L 30  ? ? 57.71   -124.61 
11 1 ALA L 51  ? ? 73.35   -43.54  
12 1 ALA L 84  ? ? 179.09  176.03  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+3/4  
3 y+1/2,-x+1/2,z+1/4  
4 x+1/2,-y+1/2,-z+1/4 
5 -x+1/2,y+1/2,-z+3/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
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 B LEU 266 ? A LEU 215 
2  1 Y 1 B VAL 267 ? A VAL 216 
3  1 Y 1 B PRO 268 ? A PRO 217 
4  1 Y 1 B ARG 269 ? A ARG 218 
5  1 Y 1 B GLY 270 ? A GLY 219 
6  1 Y 1 B SER 271 ? A SER 220 
7  1 Y 1 B GLY 272 ? A GLY 221 
8  1 Y 1 B HIS 273 ? A HIS 222 
9  1 Y 1 B HIS 274 ? A HIS 223 
10 1 Y 1 B HIS 275 ? A HIS 224 
11 1 Y 1 B HIS 276 ? A HIS 225 
12 1 Y 1 B HIS 277 ? A HIS 226 
13 1 Y 1 B HIS 278 ? A HIS 227 
14 1 Y 1 H SER 215 ? B SER 228 
15 1 Y 1 H CYS 216 ? B CYS 229 
16 1 Y 1 H HIS 217 ? B HIS 230 
17 1 Y 1 H HIS 218 ? B HIS 231 
18 1 Y 1 H HIS 219 ? B HIS 232 
19 1 Y 1 H HIS 220 ? B HIS 233 
20 1 Y 1 H HIS 221 ? B HIS 234 
21 1 Y 1 H HIS 222 ? B HIS 235 
# 
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 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
K   K    K N N 193 
LEU N    N N N 194 
LEU CA   C N S 195 
LEU C    C N N 196 
LEU O    O N N 197 
LEU CB   C N N 198 
LEU CG   C N N 199 
LEU CD1  C N N 200 
LEU CD2  C N N 201 
LEU OXT  O N N 202 
LEU H    H N N 203 
LEU H2   H N N 204 
LEU HA   H N N 205 
LEU HB2  H N N 206 
LEU HB3  H N N 207 
LEU HG   H N N 208 
LEU HD11 H N N 209 
LEU HD12 H N N 210 
LEU HD13 H N N 211 
LEU HD21 H N N 212 
LEU HD22 H N N 213 
LEU HD23 H N N 214 
LEU HXT  H N N 215 
LYS N    N N N 216 
LYS CA   C N S 217 
LYS C    C N N 218 
LYS O    O N N 219 
LYS CB   C N N 220 
LYS CG   C N N 221 
LYS CD   C N N 222 
LYS CE   C N N 223 
LYS NZ   N N N 224 
LYS OXT  O N N 225 
LYS H    H N N 226 
LYS H2   H N N 227 
LYS HA   H N N 228 
LYS HB2  H N N 229 
LYS HB3  H N N 230 
LYS HG2  H N N 231 
LYS HG3  H N N 232 
LYS HD2  H N N 233 
LYS HD3  H N N 234 
LYS HE2  H N N 235 
LYS HE3  H N N 236 
LYS HZ1  H N N 237 
LYS HZ2  H N N 238 
LYS HZ3  H N N 239 
LYS HXT  H N N 240 
MET N    N N N 241 
MET CA   C N S 242 
MET C    C N N 243 
MET O    O N N 244 
MET CB   C N N 245 
MET CG   C N N 246 
MET SD   S N N 247 
MET CE   C N N 248 
MET OXT  O N N 249 
MET H    H N N 250 
MET H2   H N N 251 
MET HA   H N N 252 
MET HB2  H N N 253 
MET HB3  H N N 254 
MET HG2  H N N 255 
MET HG3  H N N 256 
MET HE1  H N N 257 
MET HE2  H N N 258 
MET HE3  H N N 259 
MET HXT  H N N 260 
NAG C1   C N R 261 
NAG C2   C N R 262 
NAG C3   C N R 263 
NAG C4   C N S 264 
NAG C5   C N R 265 
NAG C6   C N N 266 
NAG C7   C N N 267 
NAG C8   C N N 268 
NAG N2   N N N 269 
NAG O1   O N N 270 
NAG O3   O N N 271 
NAG O4   O N N 272 
NAG O5   O N N 273 
NAG O6   O N N 274 
NAG O7   O N N 275 
NAG H1   H N N 276 
NAG H2   H N N 277 
NAG H3   H N N 278 
NAG H4   H N N 279 
NAG H5   H N N 280 
NAG H61  H N N 281 
NAG H62  H N N 282 
NAG H81  H N N 283 
NAG H82  H N N 284 
NAG H83  H N N 285 
NAG HN2  H N N 286 
NAG HO1  H N N 287 
NAG HO3  H N N 288 
NAG HO4  H N N 289 
NAG HO6  H N N 290 
PEG C1   C N N 291 
PEG O1   O N N 292 
PEG C2   C N N 293 
PEG O2   O N N 294 
PEG C3   C N N 295 
PEG C4   C N N 296 
PEG O4   O N N 297 
PEG H11  H N N 298 
PEG H12  H N N 299 
PEG HO1  H N N 300 
PEG H21  H N N 301 
PEG H22  H N N 302 
PEG H31  H N N 303 
PEG H32  H N N 304 
PEG H41  H N N 305 
PEG H42  H N N 306 
PEG HO4  H N N 307 
PHE N    N N N 308 
PHE CA   C N S 309 
PHE C    C N N 310 
PHE O    O N N 311 
PHE CB   C N N 312 
PHE CG   C Y N 313 
PHE CD1  C Y N 314 
PHE CD2  C Y N 315 
PHE CE1  C Y N 316 
PHE CE2  C Y N 317 
PHE CZ   C Y N 318 
PHE OXT  O N N 319 
PHE H    H N N 320 
PHE H2   H N N 321 
PHE HA   H N N 322 
PHE HB2  H N N 323 
PHE HB3  H N N 324 
PHE HD1  H N N 325 
PHE HD2  H N N 326 
PHE HE1  H N N 327 
PHE HE2  H N N 328 
PHE HZ   H N N 329 
PHE HXT  H N N 330 
PRO N    N N N 331 
PRO CA   C N S 332 
PRO C    C N N 333 
PRO O    O N N 334 
PRO CB   C N N 335 
PRO CG   C N N 336 
PRO CD   C N N 337 
PRO OXT  O N N 338 
PRO H    H N N 339 
PRO HA   H N N 340 
PRO HB2  H N N 341 
PRO HB3  H N N 342 
PRO HG2  H N N 343 
PRO HG3  H N N 344 
PRO HD2  H N N 345 
PRO HD3  H N N 346 
PRO HXT  H N N 347 
SER N    N N N 348 
SER CA   C N S 349 
SER C    C N N 350 
SER O    O N N 351 
SER CB   C N N 352 
SER OG   O N N 353 
SER OXT  O N N 354 
SER H    H N N 355 
SER H2   H N N 356 
SER HA   H N N 357 
SER HB2  H N N 358 
SER HB3  H N N 359 
SER HG   H N N 360 
SER HXT  H N N 361 
THR N    N N N 362 
THR CA   C N S 363 
THR C    C N N 364 
THR O    O N N 365 
THR CB   C N R 366 
THR OG1  O N N 367 
THR CG2  C N N 368 
THR OXT  O N N 369 
THR H    H N N 370 
THR H2   H N N 371 
THR HA   H N N 372 
THR HB   H N N 373 
THR HG1  H N N 374 
THR HG21 H N N 375 
THR HG22 H N N 376 
THR HG23 H N N 377 
THR HXT  H N N 378 
TRP N    N N N 379 
TRP CA   C N S 380 
TRP C    C N N 381 
TRP O    O N N 382 
TRP CB   C N N 383 
TRP CG   C Y N 384 
TRP CD1  C Y N 385 
TRP CD2  C Y N 386 
TRP NE1  N Y N 387 
TRP CE2  C Y N 388 
TRP CE3  C Y N 389 
TRP CZ2  C Y N 390 
TRP CZ3  C Y N 391 
TRP CH2  C Y N 392 
TRP OXT  O N N 393 
TRP H    H N N 394 
TRP H2   H N N 395 
TRP HA   H N N 396 
TRP HB2  H N N 397 
TRP HB3  H N N 398 
TRP HD1  H N N 399 
TRP HE1  H N N 400 
TRP HE3  H N N 401 
TRP HZ2  H N N 402 
TRP HZ3  H N N 403 
TRP HH2  H N N 404 
TRP HXT  H N N 405 
TYR N    N N N 406 
TYR CA   C N S 407 
TYR C    C N N 408 
TYR O    O N N 409 
TYR CB   C N N 410 
TYR CG   C Y N 411 
TYR CD1  C Y N 412 
TYR CD2  C Y N 413 
TYR CE1  C Y N 414 
TYR CE2  C Y N 415 
TYR CZ   C Y N 416 
TYR OH   O N N 417 
TYR OXT  O N N 418 
TYR H    H N N 419 
TYR H2   H N N 420 
TYR HA   H N N 421 
TYR HB2  H N N 422 
TYR HB3  H N N 423 
TYR HD1  H N N 424 
TYR HD2  H N N 425 
TYR HE1  H N N 426 
TYR HE2  H N N 427 
TYR HH   H N N 428 
TYR HXT  H N N 429 
VAL N    N N N 430 
VAL CA   C N S 431 
VAL C    C N N 432 
VAL O    O N N 433 
VAL CB   C N N 434 
VAL CG1  C N N 435 
VAL CG2  C N N 436 
VAL OXT  O N N 437 
VAL H    H N N 438 
VAL H2   H N N 439 
VAL HA   H N N 440 
VAL HB   H N N 441 
VAL HG11 H N N 442 
VAL HG12 H N N 443 
VAL HG13 H N N 444 
VAL HG21 H N N 445 
VAL HG22 H N N 446 
VAL HG23 H N N 447 
VAL HXT  H N N 448 
# 
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 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
NAG C1  C2   sing N N 246 
NAG C1  O1   sing N N 247 
NAG C1  O5   sing N N 248 
NAG C1  H1   sing N N 249 
NAG C2  C3   sing N N 250 
NAG C2  N2   sing N N 251 
NAG C2  H2   sing N N 252 
NAG C3  C4   sing N N 253 
NAG C3  O3   sing N N 254 
NAG C3  H3   sing N N 255 
NAG C4  C5   sing N N 256 
NAG C4  O4   sing N N 257 
NAG C4  H4   sing N N 258 
NAG C5  C6   sing N N 259 
NAG C5  O5   sing N N 260 
NAG C5  H5   sing N N 261 
NAG C6  O6   sing N N 262 
NAG C6  H61  sing N N 263 
NAG C6  H62  sing N N 264 
NAG C7  C8   sing N N 265 
NAG C7  N2   sing N N 266 
NAG C7  O7   doub N N 267 
NAG C8  H81  sing N N 268 
NAG C8  H82  sing N N 269 
NAG C8  H83  sing N N 270 
NAG N2  HN2  sing N N 271 
NAG O1  HO1  sing N N 272 
NAG O3  HO3  sing N N 273 
NAG O4  HO4  sing N N 274 
NAG O6  HO6  sing N N 275 
PEG C1  O1   sing N N 276 
PEG C1  C2   sing N N 277 
PEG C1  H11  sing N N 278 
PEG C1  H12  sing N N 279 
PEG O1  HO1  sing N N 280 
PEG C2  O2   sing N N 281 
PEG C2  H21  sing N N 282 
PEG C2  H22  sing N N 283 
PEG O2  C3   sing N N 284 
PEG C3  C4   sing N N 285 
PEG C3  H31  sing N N 286 
PEG C3  H32  sing N N 287 
PEG C4  O4   sing N N 288 
PEG C4  H41  sing N N 289 
PEG C4  H42  sing N N 290 
PEG O4  HO4  sing N N 291 
PHE N   CA   sing N N 292 
PHE N   H    sing N N 293 
PHE N   H2   sing N N 294 
PHE CA  C    sing N N 295 
PHE CA  CB   sing N N 296 
PHE CA  HA   sing N N 297 
PHE C   O    doub N N 298 
PHE C   OXT  sing N N 299 
PHE CB  CG   sing N N 300 
PHE CB  HB2  sing N N 301 
PHE CB  HB3  sing N N 302 
PHE CG  CD1  doub Y N 303 
PHE CG  CD2  sing Y N 304 
PHE CD1 CE1  sing Y N 305 
PHE CD1 HD1  sing N N 306 
PHE CD2 CE2  doub Y N 307 
PHE CD2 HD2  sing N N 308 
PHE CE1 CZ   doub Y N 309 
PHE CE1 HE1  sing N N 310 
PHE CE2 CZ   sing Y N 311 
PHE CE2 HE2  sing N N 312 
PHE CZ  HZ   sing N N 313 
PHE OXT HXT  sing N N 314 
PRO N   CA   sing N N 315 
PRO N   CD   sing N N 316 
PRO N   H    sing N N 317 
PRO CA  C    sing N N 318 
PRO CA  CB   sing N N 319 
PRO CA  HA   sing N N 320 
PRO C   O    doub N N 321 
PRO C   OXT  sing N N 322 
PRO CB  CG   sing N N 323 
PRO CB  HB2  sing N N 324 
PRO CB  HB3  sing N N 325 
PRO CG  CD   sing N N 326 
PRO CG  HG2  sing N N 327 
PRO CG  HG3  sing N N 328 
PRO CD  HD2  sing N N 329 
PRO CD  HD3  sing N N 330 
PRO OXT HXT  sing N N 331 
SER N   CA   sing N N 332 
SER N   H    sing N N 333 
SER N   H2   sing N N 334 
SER CA  C    sing N N 335 
SER CA  CB   sing N N 336 
SER CA  HA   sing N N 337 
SER C   O    doub N N 338 
SER C   OXT  sing N N 339 
SER CB  OG   sing N N 340 
SER CB  HB2  sing N N 341 
SER CB  HB3  sing N N 342 
SER OG  HG   sing N N 343 
SER OXT HXT  sing N N 344 
THR N   CA   sing N N 345 
THR N   H    sing N N 346 
THR N   H2   sing N N 347 
THR CA  C    sing N N 348 
THR CA  CB   sing N N 349 
THR CA  HA   sing N N 350 
THR C   O    doub N N 351 
THR C   OXT  sing N N 352 
THR CB  OG1  sing N N 353 
THR CB  CG2  sing N N 354 
THR CB  HB   sing N N 355 
THR OG1 HG1  sing N N 356 
THR CG2 HG21 sing N N 357 
THR CG2 HG22 sing N N 358 
THR CG2 HG23 sing N N 359 
THR OXT HXT  sing N N 360 
TRP N   CA   sing N N 361 
TRP N   H    sing N N 362 
TRP N   H2   sing N N 363 
TRP CA  C    sing N N 364 
TRP CA  CB   sing N N 365 
TRP CA  HA   sing N N 366 
TRP C   O    doub N N 367 
TRP C   OXT  sing N N 368 
TRP CB  CG   sing N N 369 
TRP CB  HB2  sing N N 370 
TRP CB  HB3  sing N N 371 
TRP CG  CD1  doub Y N 372 
TRP CG  CD2  sing Y N 373 
TRP CD1 NE1  sing Y N 374 
TRP CD1 HD1  sing N N 375 
TRP CD2 CE2  doub Y N 376 
TRP CD2 CE3  sing Y N 377 
TRP NE1 CE2  sing Y N 378 
TRP NE1 HE1  sing N N 379 
TRP CE2 CZ2  sing Y N 380 
TRP CE3 CZ3  doub Y N 381 
TRP CE3 HE3  sing N N 382 
TRP CZ2 CH2  doub Y N 383 
TRP CZ2 HZ2  sing N N 384 
TRP CZ3 CH2  sing Y N 385 
TRP CZ3 HZ3  sing N N 386 
TRP CH2 HH2  sing N N 387 
TRP OXT HXT  sing N N 388 
TYR N   CA   sing N N 389 
TYR N   H    sing N N 390 
TYR N   H2   sing N N 391 
TYR CA  C    sing N N 392 
TYR CA  CB   sing N N 393 
TYR CA  HA   sing N N 394 
TYR C   O    doub N N 395 
TYR C   OXT  sing N N 396 
TYR CB  CG   sing N N 397 
TYR CB  HB2  sing N N 398 
TYR CB  HB3  sing N N 399 
TYR CG  CD1  doub Y N 400 
TYR CG  CD2  sing Y N 401 
TYR CD1 CE1  sing Y N 402 
TYR CD1 HD1  sing N N 403 
TYR CD2 CE2  doub Y N 404 
TYR CD2 HD2  sing N N 405 
TYR CE1 CZ   doub Y N 406 
TYR CE1 HE1  sing N N 407 
TYR CE2 CZ   sing Y N 408 
TYR CE2 HE2  sing N N 409 
TYR CZ  OH   sing N N 410 
TYR OH  HH   sing N N 411 
TYR OXT HXT  sing N N 412 
VAL N   CA   sing N N 413 
VAL N   H    sing N N 414 
VAL N   H2   sing N N 415 
VAL CA  C    sing N N 416 
VAL CA  CB   sing N N 417 
VAL CA  HA   sing N N 418 
VAL C   O    doub N N 419 
VAL C   OXT  sing N N 420 
VAL CB  CG1  sing N N 421 
VAL CB  CG2  sing N N 422 
VAL CB  HB   sing N N 423 
VAL CG1 HG11 sing N N 424 
VAL CG1 HG12 sing N N 425 
VAL CG1 HG13 sing N N 426 
VAL CG2 HG21 sing N N 427 
VAL CG2 HG22 sing N N 428 
VAL CG2 HG23 sing N N 429 
VAL OXT HXT  sing N N 430 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 4BGW ? 
2 ? 'experimental model' PDB 6OBZ ? 
# 
_space_group.name_H-M_alt     'P 43 21 2' 
_space_group.name_Hall        'P 4nw 2abw' 
_space_group.IT_number        96 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9MER 
_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]   0.012573 
_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]   0.012573 
_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]   0.003899 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
K ? ? 16.37977 2.54835 ? ? 4.54127  84.28225 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A  1 1   ? -61.16400 19.27300  -8.00800  1.000 49.59631  ? 52  ALA B N   1 
ATOM   2    C CA  . ALA A  1 1   ? -60.24600 20.39200  -7.90300  1.000 54.36373  ? 52  ALA B CA  1 
ATOM   3    C C   . ALA A  1 1   ? -58.83700 20.06200  -8.41600  1.000 55.57484  ? 52  ALA B C   1 
ATOM   4    O O   . ALA A  1 1   ? -58.60200 18.99700  -8.92800  1.000 62.23545  ? 52  ALA B O   1 
ATOM   5    C CB  . ALA A  1 1   ? -60.19700 20.89300  -6.46400  1.000 47.90420  ? 52  ALA B CB  1 
ATOM   6    N N   . PRO A  1 2   ? -57.92500 21.01200  -8.32700  1.000 56.58853  ? 53  PRO B N   1 
ATOM   7    C CA  . PRO A  1 2   ? -56.57200 20.68700  -8.74900  1.000 50.55404  ? 53  PRO B CA  1 
ATOM   8    C C   . PRO A  1 2   ? -55.61700 20.36600  -7.60200  1.000 61.86953  ? 53  PRO B C   1 
ATOM   9    O O   . PRO A  1 2   ? -55.78600 20.90600  -6.51900  1.000 58.67711  ? 53  PRO B O   1 
ATOM   10   C CB  . PRO A  1 2   ? -56.13000 21.95800  -9.44900  1.000 40.77373  ? 53  PRO B CB  1 
ATOM   11   C CG  . PRO A  1 2   ? -56.83400 23.03700  -8.72500  1.000 57.99525  ? 53  PRO B CG  1 
ATOM   12   C CD  . PRO A  1 2   ? -58.15600 22.46500  -8.29400  1.000 59.37129  ? 53  PRO B CD  1 
ATOM   13   N N   . LEU A  1 3   ? -54.63700 19.49300  -7.84000  1.000 51.03137  ? 54  LEU B N   1 
ATOM   14   C CA  . LEU A  1 3   ? -53.65200 19.15800  -6.84500  1.000 37.85678  ? 54  LEU B CA  1 
ATOM   15   C C   . LEU A  1 3   ? -52.37600 19.84300  -7.20300  1.000 41.11440  ? 54  LEU B C   1 
ATOM   16   O O   . LEU A  1 3   ? -51.81200 19.60000  -8.25500  1.000 42.73349  ? 54  LEU B O   1 
ATOM   17   C CB  . LEU A  1 3   ? -53.44400 17.65900  -6.78700  1.000 38.16134  ? 54  LEU B CB  1 
ATOM   18   C CG  . LEU A  1 3   ? -52.28400 17.14200  -5.93300  1.000 41.73098  ? 54  LEU B CG  1 
ATOM   19   C CD1 . LEU A  1 3   ? -52.71200 17.00200  -4.48300  1.000 33.83498  ? 54  LEU B CD1 1 
ATOM   20   C CD2 . LEU A  1 3   ? -51.75400 15.82300  -6.45900  1.000 39.48581  ? 54  LEU B CD2 1 
ATOM   21   N N   . GLN A  1 4   ? -51.90500 20.70500  -6.32300  1.000 41.65505  ? 55  GLN B N   1 
ATOM   22   C CA  . GLN A  1 4   ? -50.69100 21.45200  -6.57900  1.000 41.09611  ? 55  GLN B CA  1 
ATOM   23   C C   . GLN A  1 4   ? -49.49300 20.81700  -5.89500  1.000 41.11884  ? 55  GLN B C   1 
ATOM   24   O O   . GLN A  1 4   ? -49.54400 20.55200  -4.70700  1.000 39.41430  ? 55  GLN B O   1 
ATOM   25   C CB  . GLN A  1 4   ? -50.86600 22.92900  -6.18100  1.000 51.19118  ? 55  GLN B CB  1 
ATOM   26   C CG  . GLN A  1 4   ? -49.55100 23.68400  -6.06600  1.000 59.81551  ? 55  GLN B CG  1 
ATOM   27   C CD  . GLN A  1 4   ? -49.03300 24.17000  -7.40100  1.000 54.01599  ? 55  GLN B CD  1 
ATOM   28   O OE1 . GLN A  1 4   ? -47.85800 24.02200  -7.71700  1.000 55.17293  ? 55  GLN B OE1 1 
ATOM   29   N NE2 . GLN A  1 4   ? -49.91100 24.76200  -8.18900  1.000 65.08800  ? 55  GLN B NE2 1 
ATOM   30   N N   . LEU A  1 5   ? -48.41000 20.64000  -6.62500  1.000 35.65970  ? 56  LEU B N   1 
ATOM   31   C CA  . LEU A  1 5   ? -47.20400 19.91400  -6.14800  1.000 43.39906  ? 56  LEU B CA  1 
ATOM   32   C C   . LEU A  1 5   ? -46.04900 20.88900  -5.95700  1.000 37.94684  ? 56  LEU B C   1 
ATOM   33   O O   . LEU A  1 5   ? -44.93700 20.44000  -5.71400  1.000 32.48128  ? 56  LEU B O   1 
ATOM   34   C CB  . LEU A  1 5   ? -46.84200 18.83200  -7.17600  1.000 37.65146  ? 56  LEU B CB  1 
ATOM   35   C CG  . LEU A  1 5   ? -47.86200 17.71300  -7.35800  1.000 34.41723  ? 56  LEU B CG  1 
ATOM   36   C CD1 . LEU A  1 5   ? -47.38300 16.72700  -8.40900  1.000 45.20910  ? 56  LEU B CD1 1 
ATOM   37   C CD2 . LEU A  1 5   ? -48.12200 17.00200  -6.04200  1.000 28.46845  ? 56  LEU B CD2 1 
ATOM   38   N N   . GLY A  1 6   ? -46.31300 22.17300  -6.08300  1.000 40.32265  ? 57  GLY B N   1 
ATOM   39   C CA  . GLY A  1 6   ? -45.27500 23.14300  -5.86200  1.000 31.78947  ? 57  GLY B CA  1 
ATOM   40   C C   . GLY A  1 6   ? -44.02400 22.82600  -6.61600  1.000 37.92512  ? 57  GLY B C   1 
ATOM   41   O O   . GLY A  1 6   ? -44.06400 22.64900  -7.81600  1.000 45.31553  ? 57  GLY B O   1 
ATOM   42   N N   . ASN A  1 7   ? -42.91600 22.74300  -5.91600  1.000 26.19246  ? 58  ASN B N   1 
ATOM   43   C CA  . ASN A  1 7   ? -41.65800 22.49300  -6.57100  1.000 40.73526  ? 58  ASN B CA  1 
ATOM   44   C C   . ASN A  1 7   ? -41.40500 20.99600  -6.77000  1.000 34.95072  ? 58  ASN B C   1 
ATOM   45   O O   . ASN A  1 7   ? -40.31400 20.60500  -7.12900  1.000 37.90019  ? 58  ASN B O   1 
ATOM   46   C CB  . ASN A  1 7   ? -40.51900 23.12900  -5.77800  1.000 41.92734  ? 58  ASN B CB  1 
ATOM   47   C CG  . ASN A  1 7   ? -40.41000 24.62500  -6.01500  1.000 58.85095  ? 58  ASN B CG  1 
ATOM   48   O OD1 . ASN A  1 7   ? -41.14400 25.18900  -6.82000  1.000 49.66485  ? 58  ASN B OD1 1 
ATOM   49   N ND2 . ASN A  1 7   ? -39.49500 25.27200  -5.30800  1.000 59.63513  ? 58  ASN B ND2 1 
ATOM   50   N N   . CYS A  1 8   ? -42.41000 20.17800  -6.54300  1.000 25.94509  ? 59  CYS B N   1 
ATOM   51   C CA  . CYS A  1 8   ? -42.23500 18.74000  -6.61300  1.000 29.81995  ? 59  CYS B CA  1 
ATOM   52   C C   . CYS A  1 8   ? -42.82500 17.98300  -7.81400  1.000 33.40174  ? 59  CYS B C   1 
ATOM   53   O O   . CYS A  1 8   ? -43.85200 18.37300  -8.32900  1.000 30.07915  ? 59  CYS B O   1 
ATOM   54   C CB  . CYS A  1 8   ? -42.81400 18.12200  -5.32200  1.000 24.10038  ? 59  CYS B CB  1 
ATOM   55   S SG  . CYS A  1 8   ? -42.07800 18.59200  -3.75500  1.000 28.58697  ? 59  CYS B SG  1 
ATOM   56   N N   . SER A  1 9   ? -42.15900 16.91700  -8.26400  1.000 30.26037  ? 60  SER B N   1 
ATOM   57   C CA  . SER A  1 9   ? -42.70800 16.01000  -9.26700  1.000 28.81698  ? 60  SER B CA  1 
ATOM   58   C C   . SER A  1 9   ? -43.70300 15.02900  -8.63100  1.000 26.53566  ? 60  SER B C   1 
ATOM   59   O O   . SER A  1 9   ? -43.74700 14.85300  -7.40600  1.000 25.55034  ? 60  SER B O   1 
ATOM   60   C CB  . SER A  1 9   ? -41.57000 15.23800  -9.95900  1.000 27.58682  ? 60  SER B CB  1 
ATOM   61   O OG  . SER A  1 9   ? -40.91900 14.33200  -9.07300  1.000 26.30615  ? 60  SER B OG  1 
ATOM   62   N N   . VAL A  1 10  ? -44.50700 14.38000  -9.48200  1.000 25.94764  ? 61  VAL B N   1 
ATOM   63   C CA  . VAL A  1 10  ? -45.36700 13.30600  -8.99100  1.000 19.67790  ? 61  VAL B CA  1 
ATOM   64   C C   . VAL A  1 10  ? -44.53700 12.27800  -8.22800  1.000 18.93205  ? 61  VAL B C   1 
ATOM   65   O O   . VAL A  1 10  ? -44.96200 11.77500  -7.17500  1.000 25.04852  ? 61  VAL B O   1 
ATOM   66   C CB  . VAL A  1 10  ? -46.15000 12.66000  -10.14900 1.000 25.32905  ? 61  VAL B CB  1 
ATOM   67   C CG1 . VAL A  1 10  ? -46.83800 11.30900  -9.70500  1.000 23.83241  ? 61  VAL B CG1 1 
ATOM   68   C CG2 . VAL A  1 10  ? -47.15700 13.65800  -10.79300 1.000 22.73786  ? 61  VAL B CG2 1 
ATOM   69   N N   . ALA A  1 11  ? -43.32700 11.98000  -8.71000  1.000 19.08296  ? 62  ALA B N   1 
ATOM   70   C CA  . ALA A  1 11  ? -42.47700 11.02000  -8.00800  1.000 21.64906  ? 62  ALA B CA  1 
ATOM   71   C C   . ALA A  1 11  ? -42.10900 11.52000  -6.61000  1.000 25.69921  ? 62  ALA B C   1 
ATOM   72   O O   . ALA A  1 11  ? -42.29200 10.80900  -5.61300  1.000 18.58126  ? 62  ALA B O   1 
ATOM   73   C CB  . ALA A  1 11  ? -41.22200 10.71900  -8.82000  1.000 18.32157  ? 62  ALA B CB  1 
ATOM   74   N N   . GLY A  1 12  ? -41.58200 12.73900  -6.50800  1.000 22.39948  ? 63  GLY B N   1 
ATOM   75   C CA  . GLY A  1 12  ? -41.24500 13.26800  -5.18600  1.000 21.58809  ? 63  GLY B CA  1 
ATOM   76   C C   . GLY A  1 12  ? -42.43100 13.29500  -4.23100  1.000 21.87188  ? 63  GLY B C   1 
ATOM   77   O O   . GLY A  1 12  ? -42.31200 12.93200  -3.04900  1.000 23.88850  ? 63  GLY B O   1 
ATOM   78   N N   . TRP A  1 13  ? -43.59900 13.70400  -4.73000  1.000 24.97386  ? 64  TRP B N   1 
ATOM   79   C CA  . TRP A  1 13  ? -44.78100 13.75200  -3.87500  1.000 20.99282  ? 64  TRP B CA  1 
ATOM   80   C C   . TRP A  1 13  ? -45.18200 12.34400  -3.42200  1.000 23.10436  ? 64  TRP B C   1 
ATOM   81   O O   . TRP A  1 13  ? -45.34200 12.08500  -2.21800  1.000 16.54526  ? 64  TRP B O   1 
ATOM   82   C CB  . TRP A  1 13  ? -45.92100 14.46400  -4.63000  1.000 20.65668  ? 64  TRP B CB  1 
ATOM   83   C CG  . TRP A  1 13  ? -47.32600 14.24900  -4.11100  1.000 18.56567  ? 64  TRP B CG  1 
ATOM   84   C CD1 . TRP A  1 13  ? -47.83100 14.69700  -2.94800  1.000 25.25891  ? 64  TRP B CD1 1 
ATOM   85   C CD2 . TRP A  1 13  ? -48.37400 13.49200  -4.74100  1.000 25.45222  ? 64  TRP B CD2 1 
ATOM   86   N NE1 . TRP A  1 13  ? -49.13700 14.28300  -2.80200  1.000 25.19678  ? 64  TRP B NE1 1 
ATOM   87   C CE2 . TRP A  1 13  ? -49.49100 13.53900  -3.89500  1.000 24.87586  ? 64  TRP B CE2 1 
ATOM   88   C CE3 . TRP A  1 13  ? -48.46800 12.78400  -5.95100  1.000 25.43715  ? 64  TRP B CE3 1 
ATOM   89   C CZ2 . TRP A  1 13  ? -50.70200 12.90500  -4.19700  1.000 22.86541  ? 64  TRP B CZ2 1 
ATOM   90   C CZ3 . TRP A  1 13  ? -49.66700 12.16300  -6.26200  1.000 24.37681  ? 64  TRP B CZ3 1 
ATOM   91   C CH2 . TRP A  1 13  ? -50.77400 12.22400  -5.38100  1.000 25.48482  ? 64  TRP B CH2 1 
ATOM   92   N N   . ILE A  1 14  ? -45.36000 11.41800  -4.37500  1.000 16.43258  ? 65  ILE B N   1 
ATOM   93   C CA  . ILE A  1 14  ? -45.93500 10.12600  -4.01100  1.000 16.33242  ? 65  ILE B CA  1 
ATOM   94   C C   . ILE A  1 14  ? -44.95600 9.26200   -3.25200  1.000 14.52821  ? 65  ILE B C   1 
ATOM   95   O O   . ILE A  1 14  ? -45.36400 8.47700   -2.37400  1.000 20.05753  ? 65  ILE B O   1 
ATOM   96   C CB  . ILE A  1 14  ? -46.57600 9.41200   -5.22500  1.000 20.32763  ? 65  ILE B CB  1 
ATOM   97   C CG1 . ILE A  1 14  ? -47.53500 8.35600   -4.66300  1.000 19.02809  ? 65  ILE B CG1 1 
ATOM   98   C CG2 . ILE A  1 14  ? -45.50600 8.73700   -6.13500  1.000 15.95305  ? 65  ILE B CG2 1 
ATOM   99   C CD1 . ILE A  1 14  ? -48.89200 8.89200   -4.24200  1.000 16.65825  ? 65  ILE B CD1 1 
ATOM   100  N N   . LEU A  1 15  ? -43.65900 9.43500   -3.48000  1.000 16.21248  ? 66  LEU B N   1 
ATOM   101  C CA  . LEU A  1 15  ? -42.71000 8.73500   -2.63100  1.000 15.74332  ? 66  LEU B CA  1 
ATOM   102  C C   . LEU A  1 15  ? -42.55600 9.42400   -1.27000  1.000 20.94643  ? 66  LEU B C   1 
ATOM   103  O O   . LEU A  1 15  ? -42.10200 8.78100   -0.31000  1.000 19.96492  ? 66  LEU B O   1 
ATOM   104  C CB  . LEU A  1 15  ? -41.34500 8.64900   -3.32400  1.000 16.26600  ? 66  LEU B CB  1 
ATOM   105  C CG  . LEU A  1 15  ? -41.32500 7.66100   -4.50000  1.000 15.32429  ? 66  LEU B CG  1 
ATOM   106  C CD1 . LEU A  1 15  ? -40.04700 7.95400   -5.27700  1.000 18.28891  ? 66  LEU B CD1 1 
ATOM   107  C CD2 . LEU A  1 15  ? -41.47400 6.20100   -4.06100  1.000 15.53053  ? 66  LEU B CD2 1 
ATOM   108  N N   . GLY A  1 16  ? -42.91800 10.68900  -1.15500  1.000 20.03971  ? 67  GLY B N   1 
ATOM   109  C CA  . GLY A  1 16  ? -42.69900 11.39700  0.11200   1.000 19.17440  ? 67  GLY B CA  1 
ATOM   110  C C   . GLY A  1 16  ? -41.31700 12.00100  0.24600   1.000 21.43174  ? 67  GLY B C   1 
ATOM   111  O O   . GLY A  1 16  ? -40.75200 11.89900  1.33300   1.000 24.35911  ? 67  GLY B O   1 
ATOM   112  N N   . ASN A  1 17  ? -40.78600 12.57300  -0.83000  1.000 22.35374  ? 68  ASN B N   1 
ATOM   113  C CA  . ASN A  1 17  ? -39.52000 13.32800  -0.73500  1.000 22.69342  ? 68  ASN B CA  1 
ATOM   114  C C   . ASN A  1 17  ? -39.67400 14.25100  0.47500   1.000 19.00233  ? 68  ASN B C   1 
ATOM   115  O O   . ASN A  1 17  ? -40.70900 14.90100  0.59300   1.000 22.71377  ? 68  ASN B O   1 
ATOM   116  C CB  . ASN A  1 17  ? -39.20100 14.07500  -2.03700  1.000 17.26031  ? 68  ASN B CB  1 
ATOM   117  C CG  . ASN A  1 17  ? -37.98300 14.97000  -1.98000  1.000 22.38938  ? 68  ASN B CG  1 
ATOM   118  O OD1 . ASN A  1 17  ? -37.85200 15.79600  -1.08600  1.000 21.94390  ? 68  ASN B OD1 1 
ATOM   119  N ND2 . ASN A  1 17  ? -37.10100 14.83000  -2.95300  1.000 18.27999  ? 68  ASN B ND2 1 
ATOM   120  N N   . PRO A  1 18  ? -38.67000 14.31400  1.35700   1.000 22.82405  ? 69  PRO B N   1 
ATOM   121  C CA  . PRO A  1 18  ? -38.78400 15.09300  2.59600   1.000 24.21730  ? 69  PRO B CA  1 
ATOM   122  C C   . PRO A  1 18  ? -39.11900 16.57400  2.35700   1.000 31.56882  ? 69  PRO B C   1 
ATOM   123  O O   . PRO A  1 18  ? -39.66300 17.18100  3.23400   1.000 31.24119  ? 69  PRO B O   1 
ATOM   124  C CB  . PRO A  1 18  ? -37.40300 14.89700  3.22800   1.000 24.73389  ? 69  PRO B CB  1 
ATOM   125  C CG  . PRO A  1 18  ? -36.50400 14.44500  2.10900   1.000 32.05132  ? 69  PRO B CG  1 
ATOM   126  C CD  . PRO A  1 18  ? -37.40000 13.61700  1.22100   1.000 27.77365  ? 69  PRO B CD  1 
ATOM   127  N N   . GLU A  1 19  ? -38.82500 17.08400  1.16800   1.000 26.20240  ? 70  GLU B N   1 
ATOM   128  C CA  . GLU A  1 19  ? -39.12300 18.49200  0.80600   1.000 30.71311  ? 70  GLU B CA  1 
ATOM   129  C C   . GLU A  1 19  ? -40.51300 18.62300  0.18600   1.000 29.47814  ? 70  GLU B C   1 
ATOM   130  O O   . GLU A  1 19  ? -40.86200 19.73700  -0.19000  1.000 35.11632  ? 70  GLU B O   1 
ATOM   131  C CB  . GLU A  1 19  ? -38.07300 19.01500  -0.17100  1.000 25.17238  ? 70  GLU B CB  1 
ATOM   132  C CG  . GLU A  1 19  ? -36.66200 18.98400  0.37700   1.000 30.97618  ? 70  GLU B CG  1 
ATOM   133  C CD  . GLU A  1 19  ? -36.44500 19.87300  1.58700   1.000 48.16699  ? 70  GLU B CD  1 
ATOM   134  O OE1 . GLU A  1 19  ? -37.18200 20.86300  1.73300   1.000 43.47642  ? 70  GLU B OE1 1 
ATOM   135  O OE2 . GLU A  1 19  ? -35.54300 19.57000  2.37800   1.000 50.43502  ? 70  GLU B OE2 1 
ATOM   136  N N   . CYS A  1 20  ? -41.27500 17.55200  0.09300   1.000 29.52103  ? 71  CYS B N   1 
ATOM   137  C CA  . CYS A  1 20  ? -42.55900 17.57300  -0.55900  1.000 26.85563  ? 71  CYS B CA  1 
ATOM   138  C C   . CYS A  1 20  ? -43.66500 17.28800  0.41700   1.000 36.80922  ? 71  CYS B C   1 
ATOM   139  O O   . CYS A  1 20  ? -44.69300 16.73400  0.04800   1.000 44.66564  ? 71  CYS B O   1 
ATOM   140  C CB  . CYS A  1 20  ? -42.54400 16.52800  -1.68100  1.000 25.63427  ? 71  CYS B CB  1 
ATOM   141  S SG  . CYS A  1 20  ? -41.38200 16.85000  -3.00000  1.000 27.32889  ? 71  CYS B SG  1 
ATOM   142  N N   . GLU A  1 21  ? -43.49200 17.70000  1.64900   1.000 41.01834  ? 72  GLU B N   1 
ATOM   143  C CA  . GLU A  1 21  ? -44.44600 17.37500  2.69700   1.000 55.54850  ? 72  GLU B CA  1 
ATOM   144  C C   . GLU A  1 21  ? -45.33600 18.52200  3.10700   1.000 68.09684  ? 72  GLU B C   1 
ATOM   145  O O   . GLU A  1 21  ? -46.36100 18.29600  3.72600   1.000 78.08868  ? 72  GLU B O   1 
ATOM   146  C CB  . GLU A  1 21  ? -43.65900 16.89100  3.91800   1.000 54.10494  ? 72  GLU B CB  1 
ATOM   147  C CG  . GLU A  1 21  ? -44.33000 17.04800  5.27500   1.000 69.48739  ? 72  GLU B CG  1 
ATOM   148  C CD  . GLU A  1 21  ? -43.45000 16.57300  6.42100   1.000 84.60817  ? 72  GLU B CD  1 
ATOM   149  O OE1 . GLU A  1 21  ? -42.57800 17.35000  6.87300   1.000 79.06357  ? 72  GLU B OE1 1 
ATOM   150  O OE2 . GLU A  1 21  ? -43.62300 15.42000  6.87300   1.000 70.89325  ? 72  GLU B OE2 1 
ATOM   151  N N   . LEU A  1 22  ? -44.96400 19.75200  2.77200   1.000 69.85649  ? 73  LEU B N   1 
ATOM   152  C CA  . LEU A  1 22  ? -45.73300 20.90400  3.21800   1.000 77.57454  ? 73  LEU B CA  1 
ATOM   153  C C   . LEU A  1 22  ? -46.89800 21.09500  2.29500   1.000 79.24268  ? 73  LEU B C   1 
ATOM   154  O O   . LEU A  1 22  ? -47.66100 22.04100  2.42800   1.000 81.24253  ? 73  LEU B O   1 
ATOM   155  C CB  . LEU A  1 22  ? -44.87900 22.16200  3.23100   1.000 69.41411  ? 73  LEU B CB  1 
ATOM   156  C CG  . LEU A  1 22  ? -43.85800 22.28000  4.35500   1.000 81.02341  ? 73  LEU B CG  1 
ATOM   157  C CD1 . LEU A  1 22  ? -42.90900 23.42900  4.05900   1.000 78.63700  ? 73  LEU B CD1 1 
ATOM   158  C CD2 . LEU A  1 22  ? -44.55600 22.48200  5.68900   1.000 71.13049  ? 73  LEU B CD2 1 
ATOM   159  N N   . LEU A  1 23  ? -47.02700 20.19400  1.33900   1.000 69.79354  ? 74  LEU B N   1 
ATOM   160  C CA  . LEU A  1 23  ? -48.09700 20.29700  0.39900   1.000 65.22967  ? 74  LEU B CA  1 
ATOM   161  C C   . LEU A  1 23  ? -49.43600 20.41800  1.09600   1.000 70.46096  ? 74  LEU B C   1 
ATOM   162  O O   . LEU A  1 23  ? -49.62400 19.82700  2.14900   1.000 65.99201  ? 74  LEU B O   1 
ATOM   163  C CB  . LEU A  1 23  ? -48.05200 19.07700  -0.51600  1.000 60.77029  ? 74  LEU B CB  1 
ATOM   164  C CG  . LEU A  1 23  ? -47.34200 19.32500  -1.85000  1.000 54.69996  ? 74  LEU B CG  1 
ATOM   165  C CD1 . LEU A  1 23  ? -46.05100 20.10100  -1.66500  1.000 45.16001  ? 74  LEU B CD1 1 
ATOM   166  C CD2 . LEU A  1 23  ? -47.08500 18.03200  -2.59500  1.000 53.40967  ? 74  LEU B CD2 1 
ATOM   167  N N   . ILE A  1 24  ? -50.34500 21.22000  0.53600   1.000 77.49987  ? 75  ILE B N   1 
ATOM   168  C CA  . ILE A  1 24  ? -51.69300 21.38200  1.07400   1.000 72.83470  ? 75  ILE B CA  1 
ATOM   169  C C   . ILE A  1 24  ? -52.38200 20.08900  0.78800   1.000 79.26448  ? 75  ILE B C   1 
ATOM   170  O O   . ILE A  1 24  ? -52.40900 19.67200  -0.36600  1.000 74.86539  ? 75  ILE B O   1 
ATOM   171  C CB  . ILE A  1 24  ? -52.42200 22.47900  0.33600   1.000 78.68432  ? 75  ILE B CB  1 
ATOM   172  C CG1 . ILE A  1 24  ? -51.59400 23.76800  0.35300   1.000 83.25835  ? 75  ILE B CG1 1 
ATOM   173  C CG2 . ILE A  1 24  ? -53.79800 22.69600  0.95100   1.000 84.78981  ? 75  ILE B CG2 1 
ATOM   174  C CD1 . ILE A  1 24  ? -50.83900 24.00800  1.64300   1.000 71.75665  ? 75  ILE B CD1 1 
ATOM   175  N N   . SER A  1 25  ? -52.97100 19.45000  1.79500   1.000 71.10681  ? 76  SER B N   1 
ATOM   176  C CA  . SER A  1 25  ? -53.49700 18.08000  1.57100   1.000 63.17498  ? 76  SER B CA  1 
ATOM   177  C C   . SER A  1 25  ? -54.77200 18.08700  0.73000   1.000 68.66138  ? 76  SER B C   1 
ATOM   178  O O   . SER A  1 25  ? -55.47600 19.10300  0.74600   1.000 72.00652  ? 76  SER B O   1 
ATOM   179  C CB  . SER A  1 25  ? -53.68800 17.34100  2.86800   1.000 57.68682  ? 76  SER B CB  1 
ATOM   180  O OG  . SER A  1 25  ? -54.23800 16.05400  2.64800   1.000 62.57227  ? 76  SER B OG  1 
ATOM   181  N N   . ARG A  1 26  ? -55.05300 16.96700  0.05300   1.000 60.09415  ? 77  ARG B N   1 
ATOM   182  C CA  . ARG A  1 26  ? -56.28800 16.84900  -0.75500  1.000 42.07983  ? 77  ARG B CA  1 
ATOM   183  C C   . ARG A  1 26  ? -56.73800 15.38600  -0.81200  1.000 37.01111  ? 77  ARG B C   1 
ATOM   184  O O   . ARG A  1 26  ? -55.90200 14.52800  -1.07400  1.000 44.25123  ? 77  ARG B O   1 
ATOM   185  C CB  . ARG A  1 26  ? -56.02300 17.42800  -2.14300  1.000 51.54233  ? 77  ARG B CB  1 
ATOM   186  C CG  . ARG A  1 26  ? -57.10900 18.37400  -2.63300  1.000 62.77790  ? 77  ARG B CG  1 
ATOM   187  C CD  . ARG A  1 26  ? -56.57800 19.38300  -3.62800  1.000 59.55573  ? 77  ARG B CD  1 
ATOM   188  N NE  . ARG A  1 26  ? -56.48600 20.69100  -3.00500  1.000 79.07100  ? 77  ARG B NE  1 
ATOM   189  C CZ  . ARG A  1 26  ? -55.65100 21.65100  -3.37400  1.000 76.54437  ? 77  ARG B CZ  1 
ATOM   190  N NH1 . ARG A  1 26  ? -54.81900 21.45600  -4.38100  1.000 63.39472  ? 77  ARG B NH1 1 
ATOM   191  N NH2 . ARG A  1 26  ? -55.65300 22.80400  -2.73100  1.000 72.94641  ? 77  ARG B NH2 1 
ATOM   192  N N   . GLU A  1 27  ? -58.01800 15.13200  -0.58600  1.000 29.70233  ? 78  GLU B N   1 
ATOM   193  C CA  . GLU A  1 27  ? -58.58600 13.76500  -0.65700  1.000 36.66627  ? 78  GLU B CA  1 
ATOM   194  C C   . GLU A  1 27  ? -59.22100 13.52900  -2.03600  1.000 33.49742  ? 78  GLU B C   1 
ATOM   195  O O   . GLU A  1 27  ? -59.73700 12.43000  -2.24700  1.000 31.72184  ? 78  GLU B O   1 
ATOM   196  C CB  . GLU A  1 27  ? -59.63800 13.62700  0.43700   1.000 38.76052  ? 78  GLU B CB  1 
ATOM   197  C CG  . GLU A  1 27  ? -59.66700 12.27300  1.11600   1.000 58.11114  ? 78  GLU B CG  1 
ATOM   198  C CD  . GLU A  1 27  ? -60.71400 12.17600  2.21300   1.000 71.06328  ? 78  GLU B CD  1 
ATOM   199  O OE1 . GLU A  1 27  ? -61.45400 13.16100  2.41600   1.000 61.21797  ? 78  GLU B OE1 1 
ATOM   200  O OE2 . GLU A  1 27  ? -60.78900 11.11600  2.85700   1.000 75.47724  ? 78  GLU B OE2 1 
ATOM   201  N N   . SER A  1 28  ? -59.16400 14.52200  -2.92800  1.000 27.72636  ? 79  SER B N   1 
ATOM   202  C CA  . SER A  1 28  ? -59.76900 14.40500  -4.24700  1.000 31.34597  ? 79  SER B CA  1 
ATOM   203  C C   . SER A  1 28  ? -59.16900 15.47600  -5.13500  1.000 30.41662  ? 79  SER B C   1 
ATOM   204  O O   . SER A  1 28  ? -58.75400 16.52600  -4.64400  1.000 37.15976  ? 79  SER B O   1 
ATOM   205  C CB  . SER A  1 28  ? -61.28200 14.57400  -4.18900  1.000 34.01984  ? 79  SER B CB  1 
ATOM   206  O OG  . SER A  1 28  ? -61.82600 13.47100  -3.51800  1.000 52.97738  ? 79  SER B OG  1 
ATOM   207  N N   . TRP A  1 29  ? -59.09900 15.19900  -6.43600  1.000 31.51643  ? 80  TRP B N   1 
ATOM   208  C CA  . TRP A  1 29  ? -58.62900 16.20700  -7.38400  1.000 34.97287  ? 80  TRP B CA  1 
ATOM   209  C C   . TRP A  1 29  ? -58.91500 15.74500  -8.80800  1.000 42.74367  ? 80  TRP B C   1 
ATOM   210  O O   . TRP A  1 29  ? -59.11400 14.55200  -9.07300  1.000 38.90626  ? 80  TRP B O   1 
ATOM   211  C CB  . TRP A  1 29  ? -57.13800 16.52500  -7.23100  1.000 35.23046  ? 80  TRP B CB  1 
ATOM   212  C CG  . TRP A  1 29  ? -56.25800 15.33300  -7.41700  1.000 42.50438  ? 80  TRP B CG  1 
ATOM   213  C CD1 . TRP A  1 29  ? -55.74100 14.87900  -8.59300  1.000 38.63117  ? 80  TRP B CD1 1 
ATOM   214  C CD2 . TRP A  1 29  ? -55.71600 14.48500  -6.39000  1.000 38.89388  ? 80  TRP B CD2 1 
ATOM   215  N NE1 . TRP A  1 29  ? -54.96800 13.76400  -8.37200  1.000 31.74549  ? 80  TRP B NE1 1 
ATOM   216  C CE2 . TRP A  1 29  ? -54.92700 13.50700  -7.02900  1.000 37.92189  ? 80  TRP B CE2 1 
ATOM   217  C CE3 . TRP A  1 29  ? -55.85200 14.43600  -5.00500  1.000 29.78879  ? 80  TRP B CE3 1 
ATOM   218  C CZ2 . TRP A  1 29  ? -54.27300 12.49100  -6.32100  1.000 32.32075  ? 80  TRP B CZ2 1 
ATOM   219  C CZ3 . TRP A  1 29  ? -55.19600 13.44500  -4.30800  1.000 30.69514  ? 80  TRP B CZ3 1 
ATOM   220  C CH2 . TRP A  1 29  ? -54.41800 12.48500  -4.96500  1.000 34.55187  ? 80  TRP B CH2 1 
ATOM   221  N N   . SER A  1 30  ? -58.93800 16.72700  -9.72500  1.000 42.03112  ? 81  SER B N   1 
ATOM   222  C CA  . SER A  1 30  ? -59.28900 16.49800  -11.12000 1.000 40.94031  ? 81  SER B CA  1 
ATOM   223  C C   . SER A  1 30  ? -58.09700 16.56400  -12.04900 1.000 36.95465  ? 81  SER B C   1 
ATOM   224  O O   . SER A  1 30  ? -58.17000 16.01300  -13.15300 1.000 44.93166  ? 81  SER B O   1 
ATOM   225  C CB  . SER A  1 30  ? -60.34300 17.51500  -11.60800 1.000 46.44419  ? 81  SER B CB  1 
ATOM   226  O OG  . SER A  1 30  ? -61.58000 17.39600  -10.91400 1.000 44.97637  ? 81  SER B OG  1 
ATOM   227  N N   . TYR A  1 31  ? -57.04400 17.20300  -11.58300 1.000 33.16348  ? 82  TYR B N   1 
ATOM   228  C CA  . TYR A  1 31  ? -55.82200 17.23400  -12.40200 1.000 36.18170  ? 82  TYR B CA  1 
ATOM   229  C C   . TYR A  1 31  ? -54.62800 17.48300  -11.49900 1.000 34.85099  ? 82  TYR B C   1 
ATOM   230  O O   . TYR A  1 31  ? -54.80200 17.76500  -10.31500 1.000 42.71088  ? 82  TYR B O   1 
ATOM   231  C CB  . TYR A  1 31  ? -55.94100 18.26600  -13.52700 1.000 49.22471  ? 82  TYR B CB  1 
ATOM   232  C CG  . TYR A  1 31  ? -56.37400 19.64800  -13.11600 1.000 48.64967  ? 82  TYR B CG  1 
ATOM   233  C CD1 . TYR A  1 31  ? -57.65400 19.89200  -12.64900 1.000 48.31105  ? 82  TYR B CD1 1 
ATOM   234  C CD2 . TYR A  1 31  ? -55.50900 20.72200  -13.22600 1.000 48.11285  ? 82  TYR B CD2 1 
ATOM   235  C CE1 . TYR A  1 31  ? -58.05700 21.16400  -12.28100 1.000 53.56008  ? 82  TYR B CE1 1 
ATOM   236  C CE2 . TYR A  1 31  ? -55.89700 22.00000  -12.86600 1.000 53.05000  ? 82  TYR B CE2 1 
ATOM   237  C CZ  . TYR A  1 31  ? -57.17700 22.22400  -12.39300 1.000 55.16132  ? 82  TYR B CZ  1 
ATOM   238  O OH  . TYR A  1 31  ? -57.55900 23.48300  -12.03200 1.000 62.28830  ? 82  TYR B OH  1 
ATOM   239  N N   . ILE A  1 32  ? -53.45200 17.41400  -12.08000 1.000 33.33932  ? 83  ILE B N   1 
ATOM   240  C CA  . ILE A  1 32  ? -52.23600 17.56700  -11.31600 1.000 45.01476  ? 83  ILE B CA  1 
ATOM   241  C C   . ILE A  1 32  ? -51.50000 18.70000  -12.00700 1.000 47.07909  ? 83  ILE B C   1 
ATOM   242  O O   . ILE A  1 32  ? -51.10700 18.55700  -13.16900 1.000 52.02549  ? 83  ILE B O   1 
ATOM   243  C CB  . ILE A  1 32  ? -51.39700 16.28400  -11.32900 1.000 38.41152  ? 83  ILE B CB  1 
ATOM   244  C CG1 . ILE A  1 32  ? -52.17700 15.12800  -10.65300 1.000 40.24201  ? 83  ILE B CG1 1 
ATOM   245  C CG2 . ILE A  1 32  ? -50.05800 16.57400  -10.64300 1.000 36.51860  ? 83  ILE B CG2 1 
ATOM   246  C CD1 . ILE A  1 32  ? -51.36100 13.99000  -9.98500  1.000 27.84502  ? 83  ILE B CD1 1 
ATOM   247  N N   . VAL A  1 33  ? -51.35700 19.84200  -11.33900 1.000 48.01901  ? 84  VAL B N   1 
ATOM   248  C CA  . VAL A  1 33  ? -50.51500 20.91700  -11.86800 1.000 54.29096  ? 84  VAL B CA  1 
ATOM   249  C C   . VAL A  1 33  ? -49.11500 20.71900  -11.31000 1.000 50.07604  ? 84  VAL B C   1 
ATOM   250  O O   . VAL A  1 33  ? -48.89900 20.63700  -10.09100 1.000 49.85206  ? 84  VAL B O   1 
ATOM   251  C CB  . VAL A  1 33  ? -51.07300 22.32900  -11.57500 1.000 55.52783  ? 84  VAL B CB  1 
ATOM   252  C CG1 . VAL A  1 33  ? -52.56300 22.38700  -11.84200 1.000 54.87019  ? 84  VAL B CG1 1 
ATOM   253  C CG2 . VAL A  1 33  ? -50.82500 22.76500  -10.18700 1.000 55.91120  ? 84  VAL B CG2 1 
ATOM   254  N N   . GLU A  1 34  ? -48.19500 20.54500  -12.22400 1.000 46.44835  ? 85  GLU B N   1 
ATOM   255  C CA  . GLU A  1 34  ? -46.85800 20.28400  -11.83800 1.000 43.16258  ? 85  GLU B CA  1 
ATOM   256  C C   . GLU A  1 34  ? -45.97800 21.06000  -12.77400 1.000 45.46533  ? 85  GLU B C   1 
ATOM   257  O O   . GLU A  1 34  ? -46.31000 21.23500  -13.93600 1.000 52.44160  ? 85  GLU B O   1 
ATOM   258  C CB  . GLU A  1 34  ? -46.62100 18.79100  -11.98800 1.000 42.97532  ? 85  GLU B CB  1 
ATOM   259  C CG  . GLU A  1 34  ? -45.16500 18.37200  -12.05400 1.000 47.64901  ? 85  GLU B CG  1 
ATOM   260  C CD  . GLU A  1 34  ? -44.99000 16.88500  -12.27900 1.000 44.35961  ? 85  GLU B CD  1 
ATOM   261  O OE1 . GLU A  1 34  ? -45.96200 16.21400  -12.66400 1.000 41.55951  ? 85  GLU B OE1 1 
ATOM   262  O OE2 . GLU A  1 34  ? -43.87300 16.39100  -12.07100 1.000 41.41111  ? 85  GLU B OE2 1 
ATOM   263  N N   . LYS A  1 35  ? -44.86800 21.52500  -12.25700 1.000 42.28845  ? 86  LYS B N   1 
ATOM   264  C CA  . LYS A  1 35  ? -43.96300 22.31600  -13.03600 1.000 47.93871  ? 86  LYS B CA  1 
ATOM   265  C C   . LYS A  1 35  ? -43.31100 21.54400  -14.15100 1.000 61.81960  ? 86  LYS B C   1 
ATOM   266  O O   . LYS A  1 35  ? -43.09100 20.34900  -14.05500 1.000 55.90105  ? 86  LYS B O   1 
ATOM   267  C CB  . LYS A  1 35  ? -42.88000 22.88500  -12.12500 1.000 48.57564  ? 86  LYS B CB  1 
ATOM   268  C CG  . LYS A  1 35  ? -43.28000 24.13700  -11.37500 1.000 47.00185  ? 86  LYS B CG  1 
ATOM   269  C CD  . LYS A  1 35  ? -42.49200 24.26100  -10.08700 1.000 54.82834  ? 86  LYS B CD  1 
ATOM   270  C CE  . LYS A  1 35  ? -41.84500 25.62500  -9.95600  1.000 50.99709  ? 86  LYS B CE  1 
ATOM   271  N NZ  . LYS A  1 35  ? -40.50200 25.52500  -9.32600  1.000 52.39953  ? 86  LYS B NZ  1 
ATOM   272  N N   . PRO A  1 36  ? -42.99200 22.24800  -15.23200 1.000 70.19839  ? 87  PRO B N   1 
ATOM   273  C CA  . PRO A  1 36  ? -42.35000 21.60100  -16.36400 1.000 66.07851  ? 87  PRO B CA  1 
ATOM   274  C C   . PRO A  1 36  ? -41.05300 20.96400  -15.91500 1.000 65.89951  ? 87  PRO B C   1 
ATOM   275  O O   . PRO A  1 36  ? -40.65300 19.92200  -16.43200 1.000 60.81456  ? 87  PRO B O   1 
ATOM   276  C CB  . PRO A  1 36  ? -42.12400 22.76600  -17.33800 1.000 67.02163  ? 87  PRO B CB  1 
ATOM   277  C CG  . PRO A  1 36  ? -42.22400 24.00400  -16.51700 1.000 67.43478  ? 87  PRO B CG  1 
ATOM   278  C CD  . PRO A  1 36  ? -43.22100 23.68100  -15.45800 1.000 60.65477  ? 87  PRO B CD  1 
ATOM   279  N N   . ASN A  1 37  ? -40.39900 21.56100  -14.93900 1.000 60.28913  ? 88  ASN B N   1 
ATOM   280  C CA  . ASN A  1 37  ? -39.20500 20.94800  -14.41300 1.000 56.32775  ? 88  ASN B CA  1 
ATOM   281  C C   . ASN A  1 37  ? -39.17100 20.96300  -12.87700 1.000 60.00590  ? 88  ASN B C   1 
ATOM   282  O O   . ASN A  1 37  ? -38.53400 21.81600  -12.29100 1.000 62.68527  ? 88  ASN B O   1 
ATOM   283  C CB  . ASN A  1 37  ? -38.00200 21.67400  -14.95400 1.000 68.28139  ? 88  ASN B CB  1 
ATOM   284  C CG  . ASN A  1 37  ? -36.85800 20.74100  -15.29200 1.000 75.43779  ? 88  ASN B CG  1 
ATOM   285  O OD1 . ASN A  1 37  ? -37.02700 19.77700  -16.03500 1.000 78.26249  ? 88  ASN B OD1 1 
ATOM   286  N ND2 . ASN A  1 37  ? -35.68100 21.03100  -14.75500 1.000 66.60359  ? 88  ASN B ND2 1 
ATOM   287  N N   . PRO A  1 38  ? -39.85700 20.01200  -12.22300 1.000 51.35246  ? 89  PRO B N   1 
ATOM   288  C CA  . PRO A  1 38  ? -39.78100 20.07100  -10.76500 1.000 43.50537  ? 89  PRO B CA  1 
ATOM   289  C C   . PRO A  1 38  ? -38.38100 19.84100  -10.20100 1.000 43.69426  ? 89  PRO B C   1 
ATOM   290  O O   . PRO A  1 38  ? -37.59900 19.11300  -10.76800 1.000 42.78668  ? 89  PRO B O   1 
ATOM   291  C CB  . PRO A  1 38  ? -40.75600 18.98200  -10.32600 1.000 43.35818  ? 89  PRO B CB  1 
ATOM   292  C CG  . PRO A  1 38  ? -41.65000 18.75900  -11.48900 1.000 43.17269  ? 89  PRO B CG  1 
ATOM   293  C CD  . PRO A  1 38  ? -40.79800 18.99000  -12.69200 1.000 43.68482  ? 89  PRO B CD  1 
ATOM   294  N N   . GLU A  1 39  ? -38.07400 20.48300  -9.08500  1.000 38.51343  ? 90  GLU B N   1 
ATOM   295  C CA  . GLU A  1 39  ? -36.75300 20.36100  -8.49400  1.000 40.93530  ? 90  GLU B CA  1 
ATOM   296  C C   . GLU A  1 39  ? -36.64200 19.25400  -7.46000  1.000 39.26709  ? 90  GLU B C   1 
ATOM   297  O O   . GLU A  1 39  ? -35.55900 18.78000  -7.14800  1.000 36.01787  ? 90  GLU B O   1 
ATOM   298  C CB  . GLU A  1 39  ? -36.37400 21.67600  -7.81400  1.000 54.57989  ? 90  GLU B CB  1 
ATOM   299  C CG  . GLU A  1 39  ? -36.31700 22.89400  -8.73500  1.000 63.76151  ? 90  GLU B CG  1 
ATOM   300  C CD  . GLU A  1 39  ? -37.65500 23.60000  -8.91000  1.000 62.29430  ? 90  GLU B CD  1 
ATOM   301  O OE1 . GLU A  1 39  ? -38.68200 23.10400  -8.41100  1.000 54.81304  ? 90  GLU B OE1 1 
ATOM   302  O OE2 . GLU A  1 39  ? -37.68200 24.66100  -9.56400  1.000 68.89051  ? 90  GLU B OE2 1 
ATOM   303  N N   . ASN A  1 40  ? -37.76100 18.88900  -6.88000  1.000 30.01524  ? 91  ASN B N   1 
ATOM   304  C CA  . ASN A  1 40  ? -37.74300 17.80700  -5.92500  1.000 30.45469  ? 91  ASN B CA  1 
ATOM   305  C C   . ASN A  1 40  ? -38.51200 16.54000  -6.35500  1.000 29.80577  ? 91  ASN B C   1 
ATOM   306  O O   . ASN A  1 40  ? -39.71800 16.55600  -6.46900  1.000 25.45519  ? 91  ASN B O   1 
ATOM   307  C CB  . ASN A  1 40  ? -38.23200 18.33000  -4.57400  1.000 35.11408  ? 91  ASN B CB  1 
ATOM   308  C CG  . ASN A  1 40  ? -37.31400 19.39200  -3.99600  1.000 30.80148  ? 91  ASN B CG  1 
ATOM   309  O OD1 . ASN A  1 40  ? -37.76000 20.45400  -3.59500  1.000 30.37198  ? 91  ASN B OD1 1 
ATOM   310  N ND2 . ASN A  1 40  ? -36.02500 19.10100  -3.96700  1.000 36.46101  ? 91  ASN B ND2 1 
ATOM   311  N N   . GLY A  1 41  ? -37.77900 15.45200  -6.58700  1.000 34.80172  ? 92  GLY B N   1 
ATOM   312  C CA  . GLY A  1 41  ? -38.40200 14.17100  -6.93500  1.000 31.81092  ? 92  GLY B CA  1 
ATOM   313  C C   . GLY A  1 41  ? -37.68000 12.98600  -6.32200  1.000 26.24155  ? 92  GLY B C   1 
ATOM   314  O O   . GLY A  1 41  ? -37.74600 12.78600  -5.14300  1.000 22.06925  ? 92  GLY B O   1 
ATOM   315  N N   . THR A  1 42  ? -36.99200 12.22400  -7.14800  1.000 21.05078  ? 93  THR B N   1 
ATOM   316  C CA  . THR A  1 42  ? -36.22100 11.10400  -6.68600  1.000 21.62376  ? 93  THR B CA  1 
ATOM   317  C C   . THR A  1 42  ? -34.90900 11.59800  -6.07800  1.000 26.07400  ? 93  THR B C   1 
ATOM   318  O O   . THR A  1 42  ? -33.89300 11.59300  -6.74100  1.000 25.39247  ? 93  THR B O   1 
ATOM   319  C CB  . THR A  1 42  ? -36.01200 10.09100  -7.83100  1.000 24.44449  ? 93  THR B CB  1 
ATOM   320  O OG1 . THR A  1 42  ? -35.43500 10.73200  -8.96600  1.000 26.37896  ? 93  THR B OG1 1 
ATOM   321  C CG2 . THR A  1 42  ? -37.34700 9.49200   -8.21700  1.000 26.30558  ? 93  THR B CG2 1 
ATOM   322  N N   . CYS A  1 43  ? -34.94600 12.01200  -4.81400  1.000 17.32216  ? 94  CYS B N   1 
ATOM   323  C CA  . CYS A  1 43  ? -33.76300 12.54800  -4.08800  1.000 18.76605  ? 94  CYS B CA  1 
ATOM   324  C C   . CYS A  1 43  ? -32.68100 11.46500  -4.01400  1.000 26.47837  ? 94  CYS B C   1 
ATOM   325  O O   . CYS A  1 43  ? -31.50600 11.83300  -3.95300  1.000 23.18832  ? 94  CYS B O   1 
ATOM   326  C CB  . CYS A  1 43  ? -34.17300 13.12600  -2.73500  1.000 18.70985  ? 94  CYS B CB  1 
ATOM   327  S SG  . CYS A  1 43  ? -34.89300 11.94900  -1.57100  1.000 24.33673  ? 94  CYS B SG  1 
ATOM   328  N N   . PHE A  1 44  ? -33.06600 10.18500  -3.97700  1.000 22.53325  ? 95  PHE B N   1 
ATOM   329  C CA  . PHE A  1 44  ? -32.06500 9.09500   -4.12400  1.000 15.75596  ? 95  PHE B CA  1 
ATOM   330  C C   . PHE A  1 44  ? -32.19000 8.60000   -5.56400  1.000 19.71559  ? 95  PHE B C   1 
ATOM   331  O O   . PHE A  1 44  ? -33.28200 8.25500   -5.99500  1.000 18.58703  ? 95  PHE B O   1 
ATOM   332  C CB  . PHE A  1 44  ? -32.18700 7.94100   -3.13400  1.000 14.43666  ? 95  PHE B CB  1 
ATOM   333  C CG  . PHE A  1 44  ? -30.94400 7.09500   -3.06500  1.000 15.80738  ? 95  PHE B CG  1 
ATOM   334  C CD1 . PHE A  1 44  ? -30.69400 6.12500   -4.02000  1.000 15.85719  ? 95  PHE B CD1 1 
ATOM   335  C CD2 . PHE A  1 44  ? -30.00400 7.29400   -2.07000  1.000 17.66651  ? 95  PHE B CD2 1 
ATOM   336  C CE1 . PHE A  1 44  ? -29.54000 5.36400   -3.97100  1.000 16.65624  ? 95  PHE B CE1 1 
ATOM   337  C CE2 . PHE A  1 44  ? -28.84800 6.53100   -2.02200  1.000 18.64580  ? 95  PHE B CE2 1 
ATOM   338  C CZ  . PHE A  1 44  ? -28.62000 5.56800   -2.97200  1.000 19.87778  ? 95  PHE B CZ  1 
ATOM   339  N N   . PRO A  1 45  ? -31.08400 8.57500   -6.32700  1.000 18.86543  ? 96  PRO B N   1 
ATOM   340  C CA  . PRO A  1 45  ? -31.15800 8.24400   -7.73900  1.000 18.90330  ? 96  PRO B CA  1 
ATOM   341  C C   . PRO A  1 45  ? -31.60200 6.82300   -8.10400  1.000 13.90296  ? 96  PRO B C   1 
ATOM   342  O O   . PRO A  1 45  ? -31.23100 5.91600   -7.45200  1.000 14.08525  ? 96  PRO B O   1 
ATOM   343  C CB  . PRO A  1 45  ? -29.71600 8.45800   -8.21400  1.000 13.11398  ? 96  PRO B CB  1 
ATOM   344  C CG  . PRO A  1 45  ? -28.88100 8.25500   -6.98300  1.000 17.51660  ? 96  PRO B CG  1 
ATOM   345  C CD  . PRO A  1 45  ? -29.72100 8.83500   -5.87000  1.000 17.78452  ? 96  PRO B CD  1 
ATOM   346  N N   . GLY A  1 46  ? -32.38500 6.73900   -9.17100  1.000 16.18040  ? 97  GLY B N   1 
ATOM   347  C CA  . GLY A  1 46  ? -32.81700 5.43600   -9.69000  1.000 15.38775  ? 97  GLY B CA  1 
ATOM   348  C C   . GLY A  1 46  ? -33.85000 5.55400   -10.79000 1.000 19.85324  ? 97  GLY B C   1 
ATOM   349  O O   . GLY A  1 46  ? -34.23100 6.67000   -11.13800 1.000 18.72284  ? 97  GLY B O   1 
ATOM   350  N N   . HIS A  1 47  ? -34.24600 4.41900   -11.34600 1.000 15.37959  ? 98  HIS B N   1 
ATOM   351  C CA  . HIS A  1 47  ? -35.26900 4.39900   -12.38900 1.000 18.43826  ? 98  HIS B CA  1 
ATOM   352  C C   . HIS A  1 47  ? -36.63300 4.16600   -11.76000 1.000 14.35113  ? 98  HIS B C   1 
ATOM   353  O O   . HIS A  1 47  ? -36.78200 3.26600   -10.93600 1.000 15.52831  ? 98  HIS B O   1 
ATOM   354  C CB  . HIS A  1 47  ? -35.00300 3.27500   -13.37700 1.000 15.67410  ? 98  HIS B CB  1 
ATOM   355  C CG  . HIS A  1 47  ? -35.93400 3.26400   -14.53400 1.000 23.31852  ? 98  HIS B CG  1 
ATOM   356  N ND1 . HIS A  1 47  ? -36.83000 2.24000   -14.74500 1.000 32.07183  ? 98  HIS B ND1 1 
ATOM   357  C CD2 . HIS A  1 47  ? -36.04000 4.08700   -15.60300 1.000 29.16887  ? 98  HIS B CD2 1 
ATOM   358  C CE1 . HIS A  1 47  ? -37.50100 2.47400   -15.86200 1.000 28.70689  ? 98  HIS B CE1 1 
ATOM   359  N NE2 . HIS A  1 47  ? -37.04000 3.58600   -16.40400 1.000 25.77466  ? 98  HIS B NE2 1 
ATOM   360  N N   . PHE A  1 48  ? -37.61800 4.94200   -12.15600 1.000 14.40941  ? 99  PHE B N   1 
ATOM   361  C CA  . PHE A  1 48  ? -38.97800 4.81500   -11.63200 1.000 21.68402  ? 99  PHE B CA  1 
ATOM   362  C C   . PHE A  1 48  ? -39.83400 4.07600   -12.65200 1.000 18.77135  ? 99  PHE B C   1 
ATOM   363  O O   . PHE A  1 48  ? -40.20600 4.65600   -13.66700 1.000 18.64989  ? 99  PHE B O   1 
ATOM   364  C CB  . PHE A  1 48  ? -39.56300 6.19300   -11.34900 1.000 18.85069  ? 99  PHE B CB  1 
ATOM   365  C CG  . PHE A  1 48  ? -40.71300 6.20500   -10.37900 1.000 21.99137  ? 99  PHE B CG  1 
ATOM   366  C CD1 . PHE A  1 48  ? -41.90000 5.54200   -10.68400 1.000 17.22393  ? 99  PHE B CD1 1 
ATOM   367  C CD2 . PHE A  1 48  ? -40.66800 6.96600   -9.21700  1.000 22.82003  ? 99  PHE B CD2 1 
ATOM   368  C CE1 . PHE A  1 48  ? -42.98600 5.59100   -9.84800  1.000 19.57967  ? 99  PHE B CE1 1 
ATOM   369  C CE2 . PHE A  1 48  ? -41.76600 7.01800   -8.35800  1.000 18.34789  ? 99  PHE B CE2 1 
ATOM   370  C CZ  . PHE A  1 48  ? -42.92500 6.32200   -8.65700  1.000 16.44134  ? 99  PHE B CZ  1 
ATOM   371  N N   . ALA A  1 49  ? -40.17000 2.82300   -12.35600 1.000 18.37033  ? 100 ALA B N   1 
ATOM   372  C CA  . ALA A  1 49  ? -40.95000 1.97100   -13.26100 1.000 13.46784  ? 100 ALA B CA  1 
ATOM   373  C C   . ALA A  1 49  ? -42.34100 2.52800   -13.57000 1.000 17.96052  ? 100 ALA B C   1 
ATOM   374  O O   . ALA A  1 49  ? -43.05300 3.01900   -12.68200 1.000 20.10419  ? 100 ALA B O   1 
ATOM   375  C CB  . ALA A  1 49  ? -41.10300 0.57900   -12.65100 1.000 15.20261  ? 100 ALA B CB  1 
ATOM   376  N N   . ASP A  1 50  ? -42.73900 2.42400   -14.85300 1.000 15.07073  ? 101 ASP B N   1 
ATOM   377  C CA  . ASP A  1 50  ? -44.10300 2.71800   -15.28900 1.000 18.16502  ? 101 ASP B CA  1 
ATOM   378  C C   . ASP A  1 50  ? -44.54100 4.10700   -14.86200 1.000 19.95227  ? 101 ASP B C   1 
ATOM   379  O O   . ASP A  1 50  ? -45.67200 4.31900   -14.40100 1.000 18.98556  ? 101 ASP B O   1 
ATOM   380  C CB  . ASP A  1 50  ? -45.06600 1.66400   -14.75300 1.000 19.40129  ? 101 ASP B CB  1 
ATOM   381  C CG  . ASP A  1 50  ? -44.70200 0.28000   -15.24900 1.000 25.24336  ? 101 ASP B CG  1 
ATOM   382  O OD1 . ASP A  1 50  ? -44.50500 0.10800   -16.47800 1.000 22.32367  ? 101 ASP B OD1 1 
ATOM   383  O OD2 . ASP A  1 50  ? -44.54300 -0.60800  -14.39400 1.000 27.14025  ? 101 ASP B OD2 1 
ATOM   384  N N   . TYR A  1 51  ? -43.62600 5.05700   -14.96900 1.000 17.81382  ? 102 TYR B N   1 
ATOM   385  C CA  . TYR A  1 51  ? -43.85900 6.32200   -14.30000 1.000 17.83794  ? 102 TYR B CA  1 
ATOM   386  C C   . TYR A  1 51  ? -44.96900 7.11900   -14.98600 1.000 18.69269  ? 102 TYR B C   1 
ATOM   387  O O   . TYR A  1 51  ? -45.90500 7.59600   -14.32700 1.000 19.57749  ? 102 TYR B O   1 
ATOM   388  C CB  . TYR A  1 51  ? -42.55900 7.09600   -14.23900 1.000 16.20639  ? 102 TYR B CB  1 
ATOM   389  C CG  . TYR A  1 51  ? -42.70100 8.46200   -13.58900 1.000 23.45716  ? 102 TYR B CG  1 
ATOM   390  C CD1 . TYR A  1 51  ? -43.16500 8.58200   -12.27200 1.000 19.78932  ? 102 TYR B CD1 1 
ATOM   391  C CD2 . TYR A  1 51  ? -42.35500 9.62900   -14.28400 1.000 24.91651  ? 102 TYR B CD2 1 
ATOM   392  C CE1 . TYR A  1 51  ? -43.29200 9.83200   -11.68300 1.000 23.51503  ? 102 TYR B CE1 1 
ATOM   393  C CE2 . TYR A  1 51  ? -42.46100 10.87000  -13.69400 1.000 27.79316  ? 102 TYR B CE2 1 
ATOM   394  C CZ  . TYR A  1 51  ? -42.92600 10.97700  -12.40200 1.000 24.75421  ? 102 TYR B CZ  1 
ATOM   395  O OH  . TYR A  1 51  ? -43.02600 12.23200  -11.81900 1.000 27.84399  ? 102 TYR B OH  1 
ATOM   396  N N   . GLU A  1 52  ? -44.90900 7.25600   -16.31900 1.000 20.17197  ? 103 GLU B N   1 
ATOM   397  C CA  . GLU A  1 52  ? -45.96700 8.01200   -16.97600 1.000 19.08318  ? 103 GLU B CA  1 
ATOM   398  C C   . GLU A  1 52  ? -47.31600 7.37100   -16.74900 1.000 21.00285  ? 103 GLU B C   1 
ATOM   399  O O   . GLU A  1 52  ? -48.32200 8.07600   -16.57700 1.000 21.70655  ? 103 GLU B O   1 
ATOM   400  C CB  . GLU A  1 52  ? -45.66900 8.17600   -18.46300 1.000 22.68597  ? 103 GLU B CB  1 
ATOM   401  C CG  . GLU A  1 52  ? -44.41500 9.02000   -18.58900 1.000 27.78768  ? 103 GLU B CG  1 
ATOM   402  C CD  . GLU A  1 52  ? -44.70000 10.48800  -18.29200 1.000 33.14055  ? 103 GLU B CD  1 
ATOM   403  O OE1 . GLU A  1 52  ? -45.78200 10.96800  -18.67000 1.000 38.73593  ? 103 GLU B OE1 1 
ATOM   404  O OE2 . GLU A  1 52  ? -43.85000 11.16800  -17.68700 1.000 43.52124  ? 103 GLU B OE2 1 
ATOM   405  N N   . GLU A  1 53  ? -47.37500 6.06400   -16.69000 1.000 18.88360  ? 104 GLU B N   1 
ATOM   406  C CA  A GLU A  1 53  ? -48.61300 5.41600   -16.35500 0.503 22.41104  ? 104 GLU B CA  1 
ATOM   407  C CA  B GLU A  1 53  ? -48.62100 5.41900   -16.34800 0.497 22.41210  ? 104 GLU B CA  1 
ATOM   408  C C   . GLU A  1 53  ? -49.15900 5.86900   -14.93100 1.000 19.92474  ? 104 GLU B C   1 
ATOM   409  O O   . GLU A  1 53  ? -50.34700 6.12500   -14.68900 1.000 20.43690  ? 104 GLU B O   1 
ATOM   410  C CB  A GLU A  1 53  ? -48.43400 3.90800   -16.44300 0.503 18.91704  ? 104 GLU B CB  1 
ATOM   411  C CB  B GLU A  1 53  ? -48.46200 3.90900   -16.39600 0.497 18.82968  ? 104 GLU B CB  1 
ATOM   412  C CG  A GLU A  1 53  ? -48.01100 3.41800   -17.82300 0.503 22.37188  ? 104 GLU B CG  1 
ATOM   413  C CG  B GLU A  1 53  ? -48.64000 3.31000   -17.77700 0.497 23.79576  ? 104 GLU B CG  1 
ATOM   414  C CD  A GLU A  1 53  ? -46.50000 3.37400   -18.02200 0.503 25.26541  ? 104 GLU B CD  1 
ATOM   415  C CD  B GLU A  1 53  ? -50.08200 3.35400   -18.24800 0.497 24.20665  ? 104 GLU B CD  1 
ATOM   416  O OE1 A GLU A  1 53  ? -45.82300 4.39700   -17.79100 0.503 15.37371  ? 104 GLU B OE1 1 
ATOM   417  O OE1 B GLU A  1 53  ? -50.99100 3.40200   -17.39700 0.497 24.45289  ? 104 GLU B OE1 1 
ATOM   418  O OE2 A GLU A  1 53  ? -45.98400 2.30900   -18.42400 0.503 28.35090  ? 104 GLU B OE2 1 
ATOM   419  O OE2 B GLU A  1 53  ? -50.30400 3.34200   -19.47300 0.497 30.65606  ? 104 GLU B OE2 1 
ATOM   420  N N   . LEU A  1 54  ? -48.22500 5.92300   -13.99000 1.000 16.84041  ? 105 LEU B N   1 
ATOM   421  C CA  . LEU A  1 54  ? -48.65900 6.31400   -12.63700 1.000 17.99004  ? 105 LEU B CA  1 
ATOM   422  C C   . LEU A  1 54  ? -49.18100 7.74700   -12.61100 1.000 20.49579  ? 105 LEU B C   1 
ATOM   423  O O   . LEU A  1 54  ? -50.22500 8.03000   -12.00400 1.000 21.43471  ? 105 LEU B O   1 
ATOM   424  C CB  . LEU A  1 54  ? -47.52000 6.12300   -11.62500 1.000 19.58329  ? 105 LEU B CB  1 
ATOM   425  C CG  . LEU A  1 54  ? -47.88700 6.39300   -10.15800 1.000 18.68447  ? 105 LEU B CG  1 
ATOM   426  C CD1 . LEU A  1 54  ? -48.80100 5.31600   -9.62900  1.000 24.75354  ? 105 LEU B CD1 1 
ATOM   427  C CD2 . LEU A  1 54  ? -46.65000 6.45500   -9.28900  1.000 17.55362  ? 105 LEU B CD2 1 
ATOM   428  N N   . ARG A  1 55  ? -48.50900 8.63400   -13.33500 1.000 17.68343  ? 106 ARG B N   1 
ATOM   429  C CA  . ARG A  1 55  ? -48.95700 10.04500  -13.40500 1.000 22.52645  ? 106 ARG B CA  1 
ATOM   430  C C   . ARG A  1 55  ? -50.36100 10.08400  -13.99900 1.000 25.73592  ? 106 ARG B C   1 
ATOM   431  O O   . ARG A  1 55  ? -51.19700 10.83700  -13.50700 1.000 25.17476  ? 106 ARG B O   1 
ATOM   432  C CB  . ARG A  1 55  ? -48.03400 10.89200  -14.27400 1.000 21.65518  ? 106 ARG B CB  1 
ATOM   433  C CG  . ARG A  1 55  ? -46.61400 10.99100  -13.73700 1.000 33.78265  ? 106 ARG B CG  1 
ATOM   434  C CD  . ARG A  1 55  ? -45.60300 11.35600  -14.80500 1.000 35.89039  ? 106 ARG B CD  1 
ATOM   435  N NE  . ARG A  1 55  ? -46.03100 12.46400  -15.64000 1.000 46.06836  ? 106 ARG B NE  1 
ATOM   436  C CZ  . ARG A  1 55  ? -46.17500 13.70500  -15.20800 1.000 42.49726  ? 106 ARG B CZ  1 
ATOM   437  N NH1 . ARG A  1 55  ? -45.93000 13.98600  -13.94300 1.000 44.06091  ? 106 ARG B NH1 1 
ATOM   438  N NH2 . ARG A  1 55  ? -46.56300 14.65900  -16.03400 1.000 40.56673  ? 106 ARG B NH2 1 
ATOM   439  N N   . GLU A  1 56  ? -50.56300 9.30200   -15.04500 1.000 26.51411  ? 107 GLU B N   1 
ATOM   440  C CA  . GLU A  1 56  ? -51.88300 9.35100   -15.66400 1.000 25.39733  ? 107 GLU B CA  1 
ATOM   441  C C   . GLU A  1 56  ? -52.92300 8.71300   -14.74400 1.000 29.01840  ? 107 GLU B C   1 
ATOM   442  O O   . GLU A  1 56  ? -54.01800 9.25400   -14.55700 1.000 29.60709  ? 107 GLU B O   1 
ATOM   443  C CB  . GLU A  1 56  ? -51.84900 8.67300   -17.03800 1.000 27.99027  ? 107 GLU B CB  1 
ATOM   444  C CG  . GLU A  1 56  ? -53.22500 8.38400   -17.70500 1.000 36.21557  ? 107 GLU B CG  1 
ATOM   445  C CD  . GLU A  1 56  ? -54.09800 9.64700   -17.95200 1.000 49.28968  ? 107 GLU B CD  1 
ATOM   446  O OE1 . GLU A  1 56  ? -53.59400 10.79900  -17.80500 1.000 47.19101  ? 107 GLU B OE1 1 
ATOM   447  O OE2 . GLU A  1 56  ? -55.30300 9.48100   -18.28900 1.000 59.38936  ? 107 GLU B OE2 1 
ATOM   448  N N   . GLN A  1 57  ? -52.58600 7.60200   -14.10200 1.000 22.01114  ? 108 GLN B N   1 
ATOM   449  C CA  . GLN A  1 57  ? -53.60500 6.95300   -13.28300 1.000 26.34631  ? 108 GLN B CA  1 
ATOM   450  C C   . GLN A  1 57  ? -53.92500 7.74300   -12.01400 1.000 24.45916  ? 108 GLN B C   1 
ATOM   451  O O   . GLN A  1 57  ? -55.01400 7.56900   -11.45700 1.000 24.56796  ? 108 GLN B O   1 
ATOM   452  C CB  . GLN A  1 57  ? -53.17000 5.53700   -12.95200 1.000 19.18164  ? 108 GLN B CB  1 
ATOM   453  C CG  . GLN A  1 57  ? -53.45700 4.61100   -14.11500 1.000 28.52332  ? 108 GLN B CG  1 
ATOM   454  C CD  . GLN A  1 57  ? -53.01600 3.19000   -13.85800 1.000 39.23314  ? 108 GLN B CD  1 
ATOM   455  O OE1 . GLN A  1 57  ? -53.13000 2.70300   -12.73800 1.000 36.08275  ? 108 GLN B OE1 1 
ATOM   456  N NE2 . GLN A  1 57  ? -52.39300 2.54700   -14.86800 1.000 35.49212  ? 108 GLN B NE2 1 
ATOM   457  N N   . LEU A  1 58  ? -53.02000 8.62200   -11.56000 1.000 20.81349  ? 109 LEU B N   1 
ATOM   458  C CA  . LEU A  1 58  ? -53.26500 9.50000   -10.41700 1.000 26.69509  ? 109 LEU B CA  1 
ATOM   459  C C   . LEU A  1 58  ? -53.72300 10.92200  -10.80700 1.000 31.44821  ? 109 LEU B C   1 
ATOM   460  O O   . LEU A  1 58  ? -53.94200 11.75000  -9.91500  1.000 27.00044  ? 109 LEU B O   1 
ATOM   461  C CB  . LEU A  1 58  ? -52.00300 9.61000   -9.54100  1.000 20.53468  ? 109 LEU B CB  1 
ATOM   462  C CG  . LEU A  1 58  ? -51.52600 8.35700   -8.80200  1.000 23.11760  ? 109 LEU B CG  1 
ATOM   463  C CD1 . LEU A  1 58  ? -50.21800 8.57900   -8.04700  1.000 18.71049  ? 109 LEU B CD1 1 
ATOM   464  C CD2 . LEU A  1 58  ? -52.60200 7.76400   -7.94800  1.000 23.36593  ? 109 LEU B CD2 1 
ATOM   465  N N   . SER A  1 59  ? -53.89800 11.22200  -12.10800 1.000 23.80899  ? 110 SER B N   1 
ATOM   466  C CA  . SER A  1 59  ? -54.21600 12.59100  -12.52100 1.000 32.22918  ? 110 SER B CA  1 
ATOM   467  C C   . SER A  1 59  ? -55.57900 13.02400  -11.98700 1.000 31.44793  ? 110 SER B C   1 
ATOM   468  O O   . SER A  1 59  ? -55.76500 14.18600  -11.60200 1.000 30.97249  ? 110 SER B O   1 
ATOM   469  C CB  . SER A  1 59  ? -54.19300 12.72200  -14.05100 1.000 26.25675  ? 110 SER B CB  1 
ATOM   470  O OG  . SER A  1 59  ? -54.96400 11.72000  -14.68400 1.000 32.39388  ? 110 SER B OG  1 
ATOM   471  N N   . SER A  1 60  ? -56.54300 12.10700  -11.97200 1.000 26.18935  ? 111 SER B N   1 
ATOM   472  C CA  . SER A  1 60  ? -57.87200 12.38400  -11.46200 1.000 31.50552  ? 111 SER B CA  1 
ATOM   473  C C   . SER A  1 60  ? -58.22400 11.30100  -10.44300 1.000 37.05815  ? 111 SER B C   1 
ATOM   474  O O   . SER A  1 60  ? -58.10800 10.10500  -10.73000 1.000 31.64979  ? 111 SER B O   1 
ATOM   475  C CB  . SER A  1 60  ? -58.88200 12.47400  -12.62000 1.000 37.88005  ? 111 SER B CB  1 
ATOM   476  O OG  . SER A  1 60  ? -60.14600 12.00100  -12.22600 1.000 48.37130  ? 111 SER B OG  1 
ATOM   477  N N   . VAL A  1 61  ? -58.60800 11.73700  -9.23700  1.000 30.64958  ? 112 VAL B N   1 
ATOM   478  C CA  . VAL A  1 61  ? -58.80600 10.86200  -8.08800  1.000 35.24121  ? 112 VAL B CA  1 
ATOM   479  C C   . VAL A  1 61  ? -59.98400 11.34300  -7.24300  1.000 33.12324  ? 112 VAL B C   1 
ATOM   480  O O   . VAL A  1 61  ? -60.05800 12.50900  -6.84800  1.000 36.46463  ? 112 VAL B O   1 
ATOM   481  C CB  . VAL A  1 61  ? -57.49900 10.76800  -7.27700  1.000 40.73049  ? 112 VAL B CB  1 
ATOM   482  C CG1 . VAL A  1 61  ? -57.75600 10.45800  -5.81100  1.000 34.67042  ? 112 VAL B CG1 1 
ATOM   483  C CG2 . VAL A  1 61  ? -56.58400 9.69100   -7.91100  1.000 27.30707  ? 112 VAL B CG2 1 
ATOM   484  N N   . SER A  1 62  ? -60.92200 10.45400  -6.99000  1.000 35.53364  ? 113 SER B N   1 
ATOM   485  C CA  . SER A  1 62  ? -62.12600 10.77600  -6.24100  1.000 35.00567  ? 113 SER B CA  1 
ATOM   486  C C   . SER A  1 62  ? -62.00700 10.52400  -4.72900  1.000 40.81288  ? 113 SER B C   1 
ATOM   487  O O   . SER A  1 62  ? -62.87300 10.98700  -3.97200  1.000 41.57309  ? 113 SER B O   1 
ATOM   488  C CB  . SER A  1 62  ? -63.28700 9.98900   -6.85800  1.000 37.27450  ? 113 SER B CB  1 
ATOM   489  O OG  . SER A  1 62  ? -63.54800 8.79500   -6.16100  1.000 41.01473  ? 113 SER B OG  1 
ATOM   490  N N   . SER A  1 63  ? -60.99000 9.78000   -4.28900  1.000 35.16417  ? 114 SER B N   1 
ATOM   491  C CA  . SER A  1 63  ? -60.74200 9.48100   -2.84900  1.000 33.27836  ? 114 SER B CA  1 
ATOM   492  C C   . SER A  1 63  ? -59.27400 9.06600   -2.70000  1.000 34.01831  ? 114 SER B C   1 
ATOM   493  O O   . SER A  1 63  ? -58.79600 8.30700   -3.54500  1.000 29.76632  ? 114 SER B O   1 
ATOM   494  C CB  . SER A  1 63  ? -61.66300 8.42600   -2.29600  1.000 27.35424  ? 114 SER B CB  1 
ATOM   495  O OG  . SER A  1 63  ? -61.26400 8.00300   -1.01000  1.000 49.55397  ? 114 SER B OG  1 
ATOM   496  N N   . PHE A  1 64  ? -58.61200 9.53600   -1.65200  1.000 28.25003  ? 115 PHE B N   1 
ATOM   497  C CA  . PHE A  1 64  ? -57.16200 9.27600   -1.49500  1.000 32.16751  ? 115 PHE B CA  1 
ATOM   498  C C   . PHE A  1 64  ? -56.81900 9.26400   -0.00900  1.000 30.63013  ? 115 PHE B C   1 
ATOM   499  O O   . PHE A  1 64  ? -56.76600 10.33000  0.59100   1.000 37.99043  ? 115 PHE B O   1 
ATOM   500  C CB  . PHE A  1 64  ? -56.35200 10.32300  -2.25500  1.000 25.97498  ? 115 PHE B CB  1 
ATOM   501  C CG  . PHE A  1 64  ? -54.88600 10.03400  -2.42400  1.000 31.43226  ? 115 PHE B CG  1 
ATOM   502  C CD1 . PHE A  1 64  ? -54.45600 8.96300   -3.18600  1.000 28.46034  ? 115 PHE B CD1 1 
ATOM   503  C CD2 . PHE A  1 64  ? -53.93400 10.85800  -1.85100  1.000 25.35256  ? 115 PHE B CD2 1 
ATOM   504  C CE1 . PHE A  1 64  ? -53.10500 8.71200   -3.35000  1.000 29.13609  ? 115 PHE B CE1 1 
ATOM   505  C CE2 . PHE A  1 64  ? -52.58300 10.60400  -2.01800  1.000 31.88372  ? 115 PHE B CE2 1 
ATOM   506  C CZ  . PHE A  1 64  ? -52.17000 9.53100   -2.76700  1.000 25.33341  ? 115 PHE B CZ  1 
ATOM   507  N N   . GLU A  1 65  ? -56.57000 8.08600   0.53900   1.000 34.72183  ? 116 GLU B N   1 
ATOM   508  C CA  . GLU A  1 65  ? -56.30500 7.97600   1.99100   1.000 28.91591  ? 116 GLU B CA  1 
ATOM   509  C C   . GLU A  1 65  ? -54.98700 7.24900   2.28500   1.000 27.42469  ? 116 GLU B C   1 
ATOM   510  O O   . GLU A  1 65  ? -54.87700 6.07100   1.94500   1.000 27.60644  ? 116 GLU B O   1 
ATOM   511  C CB  . GLU A  1 65  ? -57.45700 7.23600   2.66000   1.000 34.19070  ? 116 GLU B CB  1 
ATOM   512  C CG  . GLU A  1 65  ? -58.66700 8.09600   2.96300   1.000 55.66637  ? 116 GLU B CG  1 
ATOM   513  C CD  . GLU A  1 65  ? -59.73600 7.38200   3.77300   1.000 64.85838  ? 116 GLU B CD  1 
ATOM   514  O OE1 . GLU A  1 65  ? -59.40700 6.86000   4.85000   1.000 62.58957  ? 116 GLU B OE1 1 
ATOM   515  O OE2 . GLU A  1 65  ? -60.89100 7.34200   3.31800   1.000 71.22301  ? 116 GLU B OE2 1 
ATOM   516  N N   . ARG A  1 66  ? -54.04700 7.94600   2.89400   1.000 18.62014  ? 117 ARG B N   1 
ATOM   517  C CA  . ARG A  1 66  ? -52.81000 7.33100   3.32300   1.000 18.81610  ? 117 ARG B CA  1 
ATOM   518  C C   . ARG A  1 66  ? -53.04200 6.48700   4.56400   1.000 27.75174  ? 117 ARG B C   1 
ATOM   519  O O   . ARG A  1 66  ? -53.87700 6.81300   5.41500   1.000 27.76172  ? 117 ARG B O   1 
ATOM   520  C CB  . ARG A  1 66  ? -51.75800 8.40000   3.60100   1.000 23.80550  ? 117 ARG B CB  1 
ATOM   521  C CG  . ARG A  1 66  ? -50.37700 7.81300   3.82300   1.000 23.15584  ? 117 ARG B CG  1 
ATOM   522  C CD  . ARG A  1 66  ? -49.29900 8.86400   4.18300   1.000 26.34217  ? 117 ARG B CD  1 
ATOM   523  N NE  . ARG A  1 66  ? -49.41200 9.30900   5.57500   1.000 24.58537  ? 117 ARG B NE  1 
ATOM   524  C CZ  . ARG A  1 66  ? -48.70000 10.30400  6.08100   1.000 31.77885  ? 117 ARG B CZ  1 
ATOM   525  N NH1 . ARG A  1 66  ? -47.77700 10.92700  5.36500   1.000 30.84508  ? 117 ARG B NH1 1 
ATOM   526  N NH2 . ARG A  1 66  ? -48.86100 10.63400  7.35800   1.000 39.22334  ? 117 ARG B NH2 1 
ATOM   527  N N   . PHE A  1 67  ? -52.31500 5.37400   4.64700   1.000 23.48066  ? 118 PHE B N   1 
ATOM   528  C CA  . PHE A  1 67  ? -52.34400 4.49800   5.80900   1.000 17.66107  ? 118 PHE B CA  1 
ATOM   529  C C   . PHE A  1 67  ? -51.03300 3.73700   5.90300   1.000 21.56637  ? 118 PHE B C   1 
ATOM   530  O O   . PHE A  1 67  ? -50.35200 3.48200   4.89700   1.000 16.57640  ? 118 PHE B O   1 
ATOM   531  C CB  . PHE A  1 67  ? -53.58200 3.58400   5.78600   1.000 21.63602  ? 118 PHE B CB  1 
ATOM   532  C CG  . PHE A  1 67  ? -53.45300 2.42800   4.87500   1.000 19.30010  ? 118 PHE B CG  1 
ATOM   533  C CD1 . PHE A  1 67  ? -53.79300 2.58300   3.53700   1.000 16.69720  ? 118 PHE B CD1 1 
ATOM   534  C CD2 . PHE A  1 67  ? -52.99000 1.21500   5.31700   1.000 20.02671  ? 118 PHE B CD2 1 
ATOM   535  C CE1 . PHE A  1 67  ? -53.66500 1.52800   2.62100   1.000 18.07645  ? 118 PHE B CE1 1 
ATOM   536  C CE2 . PHE A  1 67  ? -52.86800 0.09600   4.42100   1.000 17.68176  ? 118 PHE B CE2 1 
ATOM   537  C CZ  . PHE A  1 67  ? -53.21500 0.26300   3.05600   1.000 17.49720  ? 118 PHE B CZ  1 
ATOM   538  N N   . GLU A  1 68  ? -50.64900 3.43100   7.13400   1.000 16.41104  ? 119 GLU B N   1 
ATOM   539  C CA  . GLU A  1 68  ? -49.38800 2.75600   7.37900   1.000 16.19250  ? 119 GLU B CA  1 
ATOM   540  C C   . GLU A  1 68  ? -49.52600 1.25400   7.08000   1.000 22.44740  ? 119 GLU B C   1 
ATOM   541  O O   . GLU A  1 68  ? -49.84400 0.44500   7.96300   1.000 22.90277  ? 119 GLU B O   1 
ATOM   542  C CB  . GLU A  1 68  ? -48.93900 3.00300   8.81500   1.000 16.44315  ? 119 GLU B CB  1 
ATOM   543  C CG  . GLU A  1 68  ? -47.44600 2.87400   8.93400   1.000 21.08260  ? 119 GLU B CG  1 
ATOM   544  C CD  . GLU A  1 68  ? -46.84200 3.46500   10.21400  1.000 24.28342  ? 119 GLU B CD  1 
ATOM   545  O OE1 . GLU A  1 68  ? -47.57600 3.69100   11.21100  1.000 25.17117  ? 119 GLU B OE1 1 
ATOM   546  O OE2 . GLU A  1 68  ? -45.59300 3.56500   10.23100  1.000 18.98197  ? 119 GLU B OE2 1 
ATOM   547  N N   . ILE A  1 69  ? -49.22000 0.84300   5.83900   1.000 22.63878  ? 120 ILE B N   1 
ATOM   548  C CA  . ILE A  1 69  ? -49.38300 -0.57400  5.47700   1.000 17.63054  ? 120 ILE B CA  1 
ATOM   549  C C   . ILE A  1 69  ? -48.50700 -1.48700  6.34500   1.000 17.20597  ? 120 ILE B C   1 
ATOM   550  O O   . ILE A  1 69  ? -48.94600 -2.56500  6.77400   1.000 14.49924  ? 120 ILE B O   1 
ATOM   551  C CB  . ILE A  1 69  ? -49.11700 -0.78500  3.96300   1.000 13.79798  ? 120 ILE B CB  1 
ATOM   552  C CG1 . ILE A  1 69  ? -49.37000 -2.25300  3.58400   1.000 17.87462  ? 120 ILE B CG1 1 
ATOM   553  C CG2 . ILE A  1 69  ? -47.71500 -0.33600  3.57300   1.000 15.91218  ? 120 ILE B CG2 1 
ATOM   554  C CD1 . ILE A  1 69  ? -49.54500 -2.49400  2.08200   1.000 15.29892  ? 120 ILE B CD1 1 
ATOM   555  N N   . PHE A  1 70  ? -47.25200 -1.10100  6.59400   1.000 13.99965  ? 121 PHE B N   1 
ATOM   556  C CA  . PHE A  1 70  ? -46.32300 -1.89100  7.40100   1.000 15.46352  ? 121 PHE B CA  1 
ATOM   557  C C   . PHE A  1 70  ? -45.83600 -0.91800  8.47200   1.000 17.52575  ? 121 PHE B C   1 
ATOM   558  O O   . PHE A  1 70  ? -44.90600 -0.13100  8.23200   1.000 15.56043  ? 121 PHE B O   1 
ATOM   559  C CB  . PHE A  1 70  ? -45.17200 -2.43000  6.55700   1.000 17.18152  ? 121 PHE B CB  1 
ATOM   560  C CG  . PHE A  1 70  ? -45.59300 -3.43200  5.52100   1.000 16.92586  ? 121 PHE B CG  1 
ATOM   561  C CD1 . PHE A  1 70  ? -46.56800 -4.41700  5.82500   1.000 17.16357  ? 121 PHE B CD1 1 
ATOM   562  C CD2 . PHE A  1 70  ? -45.06400 -3.36400  4.23800   1.000 12.92897  ? 121 PHE B CD2 1 
ATOM   563  C CE1 . PHE A  1 70  ? -46.95600 -5.34100  4.85600   1.000 18.36133  ? 121 PHE B CE1 1 
ATOM   564  C CE2 . PHE A  1 70  ? -45.43800 -4.29200  3.24900   1.000 18.56671  ? 121 PHE B CE2 1 
ATOM   565  C CZ  . PHE A  1 70  ? -46.37700 -5.28800  3.55700   1.000 17.29828  ? 121 PHE B CZ  1 
ATOM   566  N N   . PRO A  1 71  ? -46.50800 -0.87600  9.63700   1.000 15.03164  ? 122 PRO B N   1 
ATOM   567  C CA  . PRO A  1 71  ? -46.17600 0.12800   10.68000  1.000 14.90510  ? 122 PRO B CA  1 
ATOM   568  C C   . PRO A  1 71  ? -44.70100 0.14000   11.07200  1.000 13.02812  ? 122 PRO B C   1 
ATOM   569  O O   . PRO A  1 71  ? -44.15300 -0.90000  11.47700  1.000 16.38779  ? 122 PRO B O   1 
ATOM   570  C CB  . PRO A  1 71  ? -47.07800 -0.29500  11.86200  1.000 20.35238  ? 122 PRO B CB  1 
ATOM   571  C CG  . PRO A  1 71  ? -48.28000 -0.81900  11.17500  1.000 20.61098  ? 122 PRO B CG  1 
ATOM   572  C CD  . PRO A  1 71  ? -47.72400 -1.62900  9.97700   1.000 14.94443  ? 122 PRO B CD  1 
ATOM   573  N N   . LYS A  1 72  ? -44.04100 1.22700   10.80300  1.000 14.39762  ? 123 LYS B N   1 
ATOM   574  C CA  A LYS A  1 72  ? -42.61000 1.27300   11.06400  0.564 16.56556  ? 123 LYS B CA  1 
ATOM   575  C CA  B LYS A  1 72  ? -42.61100 1.26900   11.06400  0.436 16.51777  ? 123 LYS B CA  1 
ATOM   576  C C   . LYS A  1 72  ? -42.08600 0.81900   12.46400  1.000 11.51844  ? 123 LYS B C   1 
ATOM   577  O O   . LYS A  1 72  ? -41.19700 -0.02400  12.60200  1.000 15.51525  ? 123 LYS B O   1 
ATOM   578  C CB  A LYS A  1 72  ? -42.08200 2.68400   10.77600  0.564 17.24632  ? 123 LYS B CB  1 
ATOM   579  C CB  B LYS A  1 72  ? -42.07200 2.67400   10.77500  0.436 17.27913  ? 123 LYS B CB  1 
ATOM   580  C CG  A LYS A  1 72  ? -40.64000 2.92400   11.18300  0.564 20.21100  ? 123 LYS B CG  1 
ATOM   581  C CG  B LYS A  1 72  ? -40.59600 2.84300   11.08100  0.436 20.26817  ? 123 LYS B CG  1 
ATOM   582  C CD  A LYS A  1 72  ? -40.11900 4.21000   10.56500  0.564 25.79441  ? 123 LYS B CD  1 
ATOM   583  C CD  B LYS A  1 72  ? -40.14100 4.26700   10.81500  0.436 25.69461  ? 123 LYS B CD  1 
ATOM   584  C CE  A LYS A  1 72  ? -39.26600 5.00900   11.53400  0.564 27.67784  ? 123 LYS B CE  1 
ATOM   585  C CE  B LYS A  1 72  ? -38.86300 4.58400   11.57000  0.436 26.97407  ? 123 LYS B CE  1 
ATOM   586  N NZ  A LYS A  1 72  ? -38.10800 4.23100   12.04600  0.564 25.26317  ? 123 LYS B NZ  1 
ATOM   587  N NZ  B LYS A  1 72  ? -38.40300 5.96600   11.27600  0.436 25.52786  ? 123 LYS B NZ  1 
ATOM   588  N N   . GLU A  1 73  ? -42.76800 1.29100   13.50200  1.000 14.53977  ? 124 GLU B N   1 
ATOM   589  C CA  . GLU A  1 73  ? -42.25800 1.03300   14.84400  1.000 13.40307  ? 124 GLU B CA  1 
ATOM   590  C C   . GLU A  1 73  ? -42.60500 -0.35600  15.37800  1.000 16.29733  ? 124 GLU B C   1 
ATOM   591  O O   . GLU A  1 73  ? -42.09300 -0.75200  16.44200  1.000 16.23953  ? 124 GLU B O   1 
ATOM   592  C CB  . GLU A  1 73  ? -42.76100 2.10700   15.81400  1.000 17.23826  ? 124 GLU B CB  1 
ATOM   593  C CG  . GLU A  1 73  ? -42.53400 3.56500   15.32100  1.000 13.87384  ? 124 GLU B CG  1 
ATOM   594  C CD  . GLU A  1 73  ? -41.03400 3.92900   15.15500  1.000 18.35226  ? 124 GLU B CD  1 
ATOM   595  O OE1 . GLU A  1 73  ? -40.18000 3.21600   15.74500  1.000 22.08663  ? 124 GLU B OE1 1 
ATOM   596  O OE2 . GLU A  1 73  ? -40.70300 4.89100   14.41000  1.000 25.28194  ? 124 GLU B OE2 1 
ATOM   597  N N   . SER A  1 74  ? -43.37500 -1.12700  14.64500  1.000 12.73083  ? 125 SER B N   1 
ATOM   598  C CA  . SER A  1 74  ? -43.83400 -2.41200  15.14200  1.000 17.94139  ? 125 SER B CA  1 
ATOM   599  C C   . SER A  1 74  ? -43.71600 -3.61200  14.21700  1.000 16.04497  ? 125 SER B C   1 
ATOM   600  O O   . SER A  1 74  ? -44.00200 -4.71600  14.63800  1.000 16.59434  ? 125 SER B O   1 
ATOM   601  C CB  . SER A  1 74  ? -45.31900 -2.24700  15.48600  1.000 15.62851  ? 125 SER B CB  1 
ATOM   602  O OG  . SER A  1 74  ? -46.08700 -1.78200  14.40300  1.000 18.75786  ? 125 SER B OG  1 
ATOM   603  N N   . SER A  1 75  ? -43.35900 -3.39600  12.97100  1.000 15.88241  ? 126 SER B N   1 
ATOM   604  C CA  . SER A  1 75  ? -43.38600 -4.47600  11.97800  1.000 14.71010  ? 126 SER B CA  1 
ATOM   605  C C   . SER A  1 75  ? -42.01700 -5.09100  11.65600  1.000 20.46720  ? 126 SER B C   1 
ATOM   606  O O   . SER A  1 75  ? -41.94600 -6.09400  10.98700  1.000 18.20249  ? 126 SER B O   1 
ATOM   607  C CB  . SER A  1 75  ? -44.05800 -3.94300  10.69900  1.000 13.02480  ? 126 SER B CB  1 
ATOM   608  O OG  . SER A  1 75  ? -45.30700 -3.34700  10.90400  1.000 23.77105  ? 126 SER B OG  1 
ATOM   609  N N   . TRP A  1 76  ? -40.94800 -4.49400  12.14600  1.000 17.80966  ? 127 TRP B N   1 
ATOM   610  C CA  . TRP A  1 76  ? -39.61500 -4.95500  11.79500  1.000 19.30832  ? 127 TRP B CA  1 
ATOM   611  C C   . TRP A  1 76  ? -38.73000 -5.25600  13.00800  1.000 19.80475  ? 127 TRP B C   1 
ATOM   612  O O   . TRP A  1 76  ? -37.75300 -4.57600  13.25000  1.000 23.45700  ? 127 TRP B O   1 
ATOM   613  C CB  . TRP A  1 76  ? -38.96300 -3.91900  10.89100  1.000 20.94710  ? 127 TRP B CB  1 
ATOM   614  C CG  . TRP A  1 76  ? -39.79400 -3.46900  9.76500   1.000 15.92449  ? 127 TRP B CG  1 
ATOM   615  C CD1 . TRP A  1 76  ? -40.48300 -2.30800  9.67300   1.000 15.03236  ? 127 TRP B CD1 1 
ATOM   616  C CD2 . TRP A  1 76  ? -40.01400 -4.16600  8.54500   1.000 17.30752  ? 127 TRP B CD2 1 
ATOM   617  N NE1 . TRP A  1 76  ? -41.13000 -2.23700  8.47400   1.000 14.36152  ? 127 TRP B NE1 1 
ATOM   618  C CE2 . TRP A  1 76  ? -40.85900 -3.37000  7.76100   1.000 12.85484  ? 127 TRP B CE2 1 
ATOM   619  C CE3 . TRP A  1 76  ? -39.58500 -5.39200  8.04200   1.000 17.22545  ? 127 TRP B CE3 1 
ATOM   620  C CZ2 . TRP A  1 76  ? -41.28000 -3.75900  6.50600   1.000 17.70648  ? 127 TRP B CZ2 1 
ATOM   621  C CZ3 . TRP A  1 76  ? -40.00300 -5.77000  6.79800   1.000 16.13716  ? 127 TRP B CZ3 1 
ATOM   622  C CH2 . TRP A  1 76  ? -40.84200 -4.96200  6.04400   1.000 12.52337  ? 127 TRP B CH2 1 
ATOM   623  N N   . PRO A  1 77  ? -39.07500 -6.30300  13.73800  1.000 17.24240  ? 128 PRO B N   1 
ATOM   624  C CA  . PRO A  1 77  ? -38.30800 -6.68200  14.92900  1.000 20.45146  ? 128 PRO B CA  1 
ATOM   625  C C   . PRO A  1 77  ? -36.85600 -7.11600  14.68800  1.000 25.58289  ? 128 PRO B C   1 
ATOM   626  O O   . PRO A  1 77  ? -36.04400 -6.94200  15.56300  1.000 24.03771  ? 128 PRO B O   1 
ATOM   627  C CB  . PRO A  1 77  ? -39.10500 -7.87300  15.46900  1.000 19.00026  ? 128 PRO B CB  1 
ATOM   628  C CG  . PRO A  1 77  ? -39.88900 -8.38500  14.33000  1.000 19.77001  ? 128 PRO B CG  1 
ATOM   629  C CD  . PRO A  1 77  ? -40.21600 -7.19400  13.49800  1.000 17.17081  ? 128 PRO B CD  1 
ATOM   630  N N   . ASN A  1 78  ? -36.54800 -7.64200  13.51700  1.000 22.67360  ? 129 ASN B N   1 
ATOM   631  C CA  . ASN A  1 78  ? -35.21800 -8.17400  13.25100  1.000 26.72442  ? 129 ASN B CA  1 
ATOM   632  C C   . ASN A  1 78  ? -34.38300 -7.38500  12.23400  1.000 22.63533  ? 129 ASN B C   1 
ATOM   633  O O   . ASN A  1 78  ? -33.42600 -7.89500  11.71400  1.000 26.91646  ? 129 ASN B O   1 
ATOM   634  C CB  . ASN A  1 78  ? -35.36000 -9.61000  12.78700  1.000 22.45655  ? 129 ASN B CB  1 
ATOM   635  C CG  . ASN A  1 78  ? -36.19600 -10.44500 13.73300  1.000 27.84959  ? 129 ASN B CG  1 
ATOM   636  O OD1 . ASN A  1 78  ? -36.03900 -10.37300 14.94200  1.000 27.34487  ? 129 ASN B OD1 1 
ATOM   637  N ND2 . ASN A  1 78  ? -37.09400 -11.23100 13.18000  1.000 28.83094  ? 129 ASN B ND2 1 
ATOM   638  N N   . HIS A  1 79  ? -34.77500 -6.15400  11.96900  1.000 18.83081  ? 130 HIS B N   1 
ATOM   639  C CA  . HIS A  1 79  ? -34.03000 -5.33600  11.01700  1.000 22.22933  ? 130 HIS B CA  1 
ATOM   640  C C   . HIS A  1 79  ? -33.99200 -3.93300  11.58100  1.000 27.25073  ? 130 HIS B C   1 
ATOM   641  O O   . HIS A  1 79  ? -34.85000 -3.58000  12.39800  1.000 26.93524  ? 130 HIS B O   1 
ATOM   642  C CB  . HIS A  1 79  ? -34.70800 -5.33400  9.64100   1.000 17.64572  ? 130 HIS B CB  1 
ATOM   643  C CG  . HIS A  1 79  ? -34.74500 -6.68900  8.99700   1.000 20.96591  ? 130 HIS B CG  1 
ATOM   644  N ND1 . HIS A  1 79  ? -35.70400 -7.63500  9.30900   1.000 21.62870  ? 130 HIS B ND1 1 
ATOM   645  C CD2 . HIS A  1 79  ? -33.91300 -7.28100  8.10200   1.000 20.68856  ? 130 HIS B CD2 1 
ATOM   646  C CE1 . HIS A  1 79  ? -35.48300 -8.73800  8.60500   1.000 27.12191  ? 130 HIS B CE1 1 
ATOM   647  N NE2 . HIS A  1 79  ? -34.40700 -8.54500  7.85800   1.000 23.02516  ? 130 HIS B NE2 1 
ATOM   648  N N   . GLU A  1 80  ? -33.03500 -3.11500  11.13100  1.000 21.00095  ? 131 GLU B N   1 
ATOM   649  C CA  . GLU A  1 80  ? -33.06200 -1.71500  11.51900  1.000 20.24860  ? 131 GLU B CA  1 
ATOM   650  C C   . GLU A  1 80  ? -33.34600 -0.88700  10.28200  1.000 23.25015  ? 131 GLU B C   1 
ATOM   651  O O   . GLU A  1 80  ? -33.39700 -1.42200  9.18900   1.000 21.97279  ? 131 GLU B O   1 
ATOM   652  C CB  . GLU A  1 80  ? -31.75000 -1.29400  12.18000  1.000 30.69450  ? 131 GLU B CB  1 
ATOM   653  C CG  . GLU A  1 80  ? -31.58000 -2.09800  13.46200  1.000 30.65243  ? 131 GLU B CG  1 
ATOM   654  C CD  . GLU A  1 80  ? -32.01700 -1.39400  14.73100  1.000 41.80246  ? 131 GLU B CD  1 
ATOM   655  O OE1 . GLU A  1 80  ? -32.69300 -0.35000  14.63800  1.000 43.05113  ? 131 GLU B OE1 1 
ATOM   656  O OE2 . GLU A  1 80  ? -31.78300 -1.95500  15.82900  1.000 47.74755  ? 131 GLU B OE2 1 
ATOM   657  N N   . ALA A  1 81  ? -33.55700 0.40600   10.46200  1.000 23.83427  ? 132 ALA B N   1 
ATOM   658  C CA  . ALA A  1 81  ? -33.77700 1.30300   9.31200   1.000 28.42096  ? 132 ALA B CA  1 
ATOM   659  C C   . ALA A  1 81  ? -32.64300 2.32600   9.20900   1.000 29.78786  ? 132 ALA B C   1 
ATOM   660  O O   . ALA A  1 81  ? -32.14300 2.74300   10.25400  1.000 27.35635  ? 132 ALA B O   1 
ATOM   661  C CB  . ALA A  1 81  ? -35.08700 1.99700   9.48100   1.000 26.94115  ? 132 ALA B CB  1 
ATOM   662  N N   . SER A  1 82  ? -32.27400 2.72100   7.99300   1.000 24.34685  ? 133 SER B N   1 
ATOM   663  C CA  . SER A  1 82  ? -31.27600 3.80100   7.84900   1.000 31.76275  ? 133 SER B CA  1 
ATOM   664  C C   . SER A  1 82  ? -31.82600 5.03100   8.55300   1.000 33.01487  ? 133 SER B C   1 
ATOM   665  O O   . SER A  1 82  ? -33.03900 5.23600   8.53500   1.000 39.86157  ? 133 SER B O   1 
ATOM   666  C CB  . SER A  1 82  ? -30.96300 4.12800   6.41200   1.000 31.53635  ? 133 SER B CB  1 
ATOM   667  O OG  . SER A  1 82  ? -30.43100 5.43400   6.27300   1.000 32.52143  ? 133 SER B OG  1 
ATOM   668  N N   . LEU A  1 83  ? -30.94200 5.81300   9.13300   1.000 36.14975  ? 134 LEU B N   1 
ATOM   669  C CA  . LEU A  1 83  ? -31.37900 7.07600   9.76200   1.000 44.79822  ? 134 LEU B CA  1 
ATOM   670  C C   . LEU A  1 83  ? -31.49500 8.14700   8.67800   1.000 52.32991  ? 134 LEU B C   1 
ATOM   671  O O   . LEU A  1 83  ? -32.12200 9.18500   8.94000   1.000 55.30769  ? 134 LEU B O   1 
ATOM   672  C CB  . LEU A  1 83  ? -30.35200 7.46100   10.82200  1.000 57.47838  ? 134 LEU B CB  1 
ATOM   673  C CG  . LEU A  1 83  ? -30.53000 6.76200   12.16800  1.000 63.61984  ? 134 LEU B CG  1 
ATOM   674  C CD1 . LEU A  1 83  ? -29.46600 7.20900   13.15500  1.000 63.96344  ? 134 LEU B CD1 1 
ATOM   675  C CD2 . LEU A  1 83  ? -31.92000 7.02100   12.72600  1.000 52.34942  ? 134 LEU B CD2 1 
ATOM   676  N N   . GLY A  1 84  ? -30.92100 7.89100   7.50800   1.000 34.43216  ? 135 GLY B N   1 
ATOM   677  C CA  . GLY A  1 84  ? -31.10000 8.86000   6.42000   1.000 36.68547  ? 135 GLY B CA  1 
ATOM   678  C C   . GLY A  1 84  ? -29.92000 8.92500   5.48700   1.000 28.38293  ? 135 GLY B C   1 
ATOM   679  O O   . GLY A  1 84  ? -28.88000 8.35900   5.81900   1.000 35.19536  ? 135 GLY B O   1 
ATOM   680  N N   . VAL A  1 85  ? -30.09700 9.62100   4.37200   1.000 27.15562  ? 136 VAL B N   1 
ATOM   681  C CA  . VAL A  1 85  ? -29.00300 9.76800   3.38200   1.000 30.03134  ? 136 VAL B CA  1 
ATOM   682  C C   . VAL A  1 85  ? -28.88500 11.25800  3.03600   1.000 27.14889  ? 136 VAL B C   1 
ATOM   683  O O   . VAL A  1 85  ? -29.88600 11.95900  3.08500   1.000 26.77358  ? 136 VAL B O   1 
ATOM   684  C CB  . VAL A  1 85  ? -29.23800 8.87600   2.14600   1.000 30.01413  ? 136 VAL B CB  1 
ATOM   685  C CG1 . VAL A  1 85  ? -30.29300 9.44500   1.21700   1.000 27.85743  ? 136 VAL B CG1 1 
ATOM   686  C CG2 . VAL A  1 85  ? -27.95200 8.58000   1.39400   1.000 41.31048  ? 136 VAL B CG2 1 
ATOM   687  N N   . SER A  1 86  ? -27.69200 11.73100  2.67400   1.000 30.48169  ? 137 SER B N   1 
ATOM   688  C CA  . SER A  1 86  ? -27.43500 13.17700  2.39300   1.000 33.65909  ? 137 SER B CA  1 
ATOM   689  C C   . SER A  1 86  ? -28.19400 13.70800  1.17300   1.000 26.49483  ? 137 SER B C   1 
ATOM   690  O O   . SER A  1 86  ? -28.56100 14.87800  1.19400   1.000 29.03253  ? 137 SER B O   1 
ATOM   691  C CB  . SER A  1 86  ? -25.96000 13.41000  2.21300   1.000 41.84257  ? 137 SER B CB  1 
ATOM   692  O OG  . SER A  1 86  ? -25.43200 12.59400  1.18000   1.000 48.33510  ? 137 SER B OG  1 
ATOM   693  N N   . SER A  1 87  ? -28.37400 12.91200  0.15100   1.000 21.78326  ? 138 SER B N   1 
ATOM   694  C CA  . SER A  1 87  ? -29.09700 13.30500  -1.04300  1.000 20.44605  ? 138 SER B CA  1 
ATOM   695  C C   . SER A  1 87  ? -30.57900 13.57000  -0.78700  1.000 23.54089  ? 138 SER B C   1 
ATOM   696  O O   . SER A  1 87  ? -31.25000 14.10900  -1.63000  1.000 25.55069  ? 138 SER B O   1 
ATOM   697  C CB  . SER A  1 87  ? -28.89600 12.18400  -2.07200  1.000 22.82434  ? 138 SER B CB  1 
ATOM   698  O OG  . SER A  1 87  ? -29.45200 10.98100  -1.60500  1.000 38.02207  ? 138 SER B OG  1 
ATOM   699  N N   . CYS A  1 88  ? -31.07000 13.17500  0.38100   1.000 20.27887  ? 139 CYS B N   1 
ATOM   700  C CA  . CYS A  1 88  ? -32.49600 13.34300  0.75200   1.000 20.70174  ? 139 CYS B CA  1 
ATOM   701  C C   . CYS A  1 88  ? -32.57100 14.15600  2.05600   1.000 31.53517  ? 139 CYS B C   1 
ATOM   702  O O   . CYS A  1 88  ? -33.24200 13.73300  3.00100   1.000 29.33728  ? 139 CYS B O   1 
ATOM   703  C CB  . CYS A  1 88  ? -33.15800 11.98000  0.90100   1.000 22.72172  ? 139 CYS B CB  1 
ATOM   704  S SG  . CYS A  1 88  ? -33.29200 11.07600  -0.66100  1.000 23.85640  ? 139 CYS B SG  1 
ATOM   705  N N   . SER A  1 89  ? -31.94200 15.32000  2.06900   1.000 28.59697  ? 140 SER B N   1 
ATOM   706  C CA  . SER A  1 89  ? -31.84400 16.10800  3.32100   1.000 24.86932  ? 140 SER B CA  1 
ATOM   707  C C   . SER A  1 89  ? -33.03700 17.04300  3.53300   1.000 28.23773  ? 140 SER B C   1 
ATOM   708  O O   . SER A  1 89  ? -33.68800 17.40400  2.55800   1.000 25.57805  ? 140 SER B O   1 
ATOM   709  C CB  . SER A  1 89  ? -30.50700 16.83100  3.37500   1.000 27.45536  ? 140 SER B CB  1 
ATOM   710  O OG  . SER A  1 89  ? -29.45300 15.95000  3.72700   1.000 34.71309  ? 140 SER B OG  1 
ATOM   711  N N   . HIS A  1 90  ? -33.32000 17.36100  4.79600   1.000 29.23521  ? 141 HIS B N   1 
ATOM   712  C CA  . HIS A  1 90  ? -34.41000 18.26300  5.17000   1.000 41.06665  ? 141 HIS B CA  1 
ATOM   713  C C   . HIS A  1 90  ? -33.93100 19.05900  6.37500   1.000 43.20707  ? 141 HIS B C   1 
ATOM   714  O O   . HIS A  1 90  ? -33.51100 18.45900  7.37200   1.000 33.42885  ? 141 HIS B O   1 
ATOM   715  C CB  . HIS A  1 90  ? -35.69800 17.51900  5.54000   1.000 33.48922  ? 141 HIS B CB  1 
ATOM   716  C CG  . HIS A  1 90  ? -36.90200 18.41200  5.61300   1.000 40.16301  ? 141 HIS B CG  1 
ATOM   717  N ND1 . HIS A  1 90  ? -37.29000 19.23300  4.57600   1.000 38.12344  ? 141 HIS B ND1 1 
ATOM   718  C CD2 . HIS A  1 90  ? -37.75300 18.67700  6.63700   1.000 42.21272  ? 141 HIS B CD2 1 
ATOM   719  C CE1 . HIS A  1 90  ? -38.36200 19.92300  4.93700   1.000 51.97982  ? 141 HIS B CE1 1 
ATOM   720  N NE2 . HIS A  1 90  ? -38.65700 19.61400  6.18600   1.000 39.57146  ? 141 HIS B NE2 1 
ATOM   721  N N   . ASN A  1 91  ? -33.98700 20.38600  6.29800   1.000 42.47961  ? 142 ASN B N   1 
ATOM   722  C CA  . ASN A  1 91  ? -33.48700 21.25400  7.40400   1.000 43.53150  ? 142 ASN B CA  1 
ATOM   723  C C   . ASN A  1 91  ? -32.03900 20.88800  7.74100   1.000 42.12580  ? 142 ASN B C   1 
ATOM   724  O O   . ASN A  1 91  ? -31.75400 20.63900  8.90700   1.000 43.89914  ? 142 ASN B O   1 
ATOM   725  C CB  . ASN A  1 91  ? -34.39800 21.17900  8.62500   1.000 42.57609  ? 142 ASN B CB  1 
ATOM   726  C CG  . ASN A  1 91  ? -35.80200 21.65800  8.33200   1.000 46.69603  ? 142 ASN B CG  1 
ATOM   727  O OD1 . ASN A  1 91  ? -36.00800 22.45600  7.42300   1.000 55.97722  ? 142 ASN B OD1 1 
ATOM   728  N ND2 . ASN A  1 91  ? -36.77000 21.17600  9.09200   1.000 49.37994  ? 142 ASN B ND2 1 
ATOM   729  N N   . GLY A  1 92  ? -31.17700 20.80200  6.73500   1.000 41.81976  ? 143 GLY B N   1 
ATOM   730  C CA  . GLY A  1 92  ? -29.74400 20.53800  6.96200   1.000 37.03243  ? 143 GLY B CA  1 
ATOM   731  C C   . GLY A  1 92  ? -29.42500 19.18700  7.57900   1.000 48.75183  ? 143 GLY B C   1 
ATOM   732  O O   . GLY A  1 92  ? -28.30400 19.03100  8.07600   1.000 45.28246  ? 143 GLY B O   1 
ATOM   733  N N   . GLU A  1 93  ? -30.36800 18.23600  7.52700   1.000 46.22702  ? 144 GLU B N   1 
ATOM   734  C CA  . GLU A  1 93  ? -30.05700 16.88500  8.05400   1.000 41.92712  ? 144 GLU B CA  1 
ATOM   735  C C   . GLU A  1 93  ? -30.42100 15.76600  7.06500   1.000 32.99321  ? 144 GLU B C   1 
ATOM   736  O O   . GLU A  1 93  ? -31.42400 15.90300  6.36900   1.000 28.90548  ? 144 GLU B O   1 
ATOM   737  C CB  . GLU A  1 93  ? -30.78100 16.63900  9.37200   1.000 43.11884  ? 144 GLU B CB  1 
ATOM   738  C CG  . GLU A  1 93  ? -30.52800 17.68800  10.43200  1.000 53.84536  ? 144 GLU B CG  1 
ATOM   739  C CD  . GLU A  1 93  ? -30.76600 17.16100  11.83500  1.000 63.70058  ? 144 GLU B CD  1 
ATOM   740  O OE1 . GLU A  1 93  ? -31.57900 16.23200  11.98100  1.000 57.37476  ? 144 GLU B OE1 1 
ATOM   741  O OE2 . GLU A  1 93  ? -30.13200 17.67400  12.77300  1.000 85.81347  ? 144 GLU B OE2 1 
ATOM   742  N N   . SER A  1 94  ? -29.61700 14.70100  7.06300   1.000 28.17839  ? 145 SER B N   1 
ATOM   743  C CA  . SER A  1 94  ? -29.88100 13.51800  6.21900   1.000 31.43720  ? 145 SER B CA  1 
ATOM   744  C C   . SER A  1 94  ? -31.24900 12.91000  6.54900   1.000 26.56239  ? 145 SER B C   1 
ATOM   745  O O   . SER A  1 94  ? -31.55000 12.71000  7.71500   1.000 31.07719  ? 145 SER B O   1 
ATOM   746  C CB  . SER A  1 94  ? -28.76600 12.53200  6.39300   1.000 28.25709  ? 145 SER B CB  1 
ATOM   747  O OG  . SER A  1 94  ? -27.58300 12.97100  5.75300   1.000 41.25165  ? 145 SER B OG  1 
ATOM   748  N N   . SER A  1 95  ? -32.05800 12.67300  5.53500   1.000 29.24712  ? 146 SER B N   1 
ATOM   749  C CA  . SER A  1 95  ? -33.36200 12.05500  5.71700   1.000 32.27426  ? 146 SER B CA  1 
ATOM   750  C C   . SER A  1 95  ? -33.64600 11.07600  4.56000   1.000 26.97767  ? 146 SER B C   1 
ATOM   751  O O   . SER A  1 95  ? -32.72100 10.61400  3.91700   1.000 24.29713  ? 146 SER B O   1 
ATOM   752  C CB  . SER A  1 95  ? -34.48800 13.09200  5.86500   1.000 18.23007  ? 146 SER B CB  1 
ATOM   753  O OG  . SER A  1 95  ? -35.67500 12.54600  6.38300   1.000 22.14019  ? 146 SER B OG  1 
ATOM   754  N N   . PHE A  1 96  ? -34.92300 10.79500  4.33800   1.000 23.79307  ? 147 PHE B N   1 
ATOM   755  C CA  . PHE A  1 96  ? -35.33100 9.80500   3.31100   1.000 22.57946  ? 147 PHE B CA  1 
ATOM   756  C C   . PHE A  1 96  ? -36.80800 9.99200   3.01000   1.000 20.43772  ? 147 PHE B C   1 
ATOM   757  O O   . PHE A  1 96  ? -37.43900 10.86000  3.59900   1.000 22.90476  ? 147 PHE B O   1 
ATOM   758  C CB  . PHE A  1 96  ? -35.05600 8.37000   3.77100   1.000 16.23307  ? 147 PHE B CB  1 
ATOM   759  C CG  . PHE A  1 96  ? -35.03000 7.32100   2.68600   1.000 23.13526  ? 147 PHE B CG  1 
ATOM   760  C CD1 . PHE A  1 96  ? -34.12500 7.39300   1.64200   1.000 21.42622  ? 147 PHE B CD1 1 
ATOM   761  C CD2 . PHE A  1 96  ? -35.91200 6.25400   2.71000   1.000 25.02223  ? 147 PHE B CD2 1 
ATOM   762  C CE1 . PHE A  1 96  ? -34.10400 6.43000   0.64700   1.000 23.19975  ? 147 PHE B CE1 1 
ATOM   763  C CE2 . PHE A  1 96  ? -35.89100 5.29000   1.71500   1.000 18.83745  ? 147 PHE B CE2 1 
ATOM   764  C CZ  . PHE A  1 96  ? -34.98700 5.37900   0.68500   1.000 23.59000  ? 147 PHE B CZ  1 
ATOM   765  N N   . TYR A  1 97  ? -37.31400 9.17100   2.10600   1.000 20.60404  ? 148 TYR B N   1 
ATOM   766  C CA  . TYR A  1 97  ? -38.73300 9.23600   1.71100   1.000 15.51651  ? 148 TYR B CA  1 
ATOM   767  C C   . TYR A  1 97  ? -39.61400 8.86400   2.90500   1.000 13.85633  ? 148 TYR B C   1 
ATOM   768  O O   . TYR A  1 97  ? -39.28000 7.94800   3.64500   1.000 18.45455  ? 148 TYR B O   1 
ATOM   769  C CB  . TYR A  1 97  ? -38.96600 8.28700   0.53800   1.000 18.29319  ? 148 TYR B CB  1 
ATOM   770  C CG  . TYR A  1 97  ? -38.11500 8.50700   -0.68500  1.000 14.73955  ? 148 TYR B CG  1 
ATOM   771  C CD1 . TYR A  1 97  ? -38.39100 9.53200   -1.57300  1.000 16.27284  ? 148 TYR B CD1 1 
ATOM   772  C CD2 . TYR A  1 97  ? -37.06100 7.66300   -0.98200  1.000 14.72466  ? 148 TYR B CD2 1 
ATOM   773  C CE1 . TYR A  1 97  ? -37.63200 9.72500   -2.71300  1.000 13.91256  ? 148 TYR B CE1 1 
ATOM   774  C CE2 . TYR A  1 97  ? -36.29400 7.83800   -2.11900  1.000 12.65029  ? 148 TYR B CE2 1 
ATOM   775  C CZ  . TYR A  1 97  ? -36.57900 8.87400   -2.99000  1.000 19.84511  ? 148 TYR B CZ  1 
ATOM   776  O OH  . TYR A  1 97  ? -35.82900 9.05800   -4.11200  1.000 15.22336  ? 148 TYR B OH  1 
ATOM   777  N N   . LYS A  1 98  ? -40.71800 9.57100   3.05100   1.000 19.67247  ? 149 LYS B N   1 
ATOM   778  C CA  . LYS A  1 98  ? -41.66800 9.30200   4.15200   1.000 23.13419  ? 149 LYS B CA  1 
ATOM   779  C C   . LYS A  1 98  ? -42.43800 8.00300   3.90300   1.000 17.90345  ? 149 LYS B C   1 
ATOM   780  O O   . LYS A  1 98  ? -42.80500 7.35200   4.87000   1.000 17.73718  ? 149 LYS B O   1 
ATOM   781  C CB  . LYS A  1 98  ? -42.65300 10.46200  4.23200   1.000 16.80735  ? 149 LYS B CB  1 
ATOM   782  C CG  . LYS A  1 98  ? -43.70800 10.34200  5.32000   1.000 31.68480  ? 149 LYS B CG  1 
ATOM   783  C CD  . LYS A  1 98  ? -43.10900 10.34100  6.70600   1.000 46.67310  ? 149 LYS B CD  1 
ATOM   784  C CE  . LYS A  1 98  ? -43.54700 11.53100  7.53100   1.000 54.79721  ? 149 LYS B CE  1 
ATOM   785  N NZ  . LYS A  1 98  ? -45.00800 11.74600  7.42700   1.000 57.67899  ? 149 LYS B NZ  1 
ATOM   786  N N   . ASN A  1 99  ? -42.61200 7.63100   2.63700   1.000 18.64868  ? 150 ASN B N   1 
ATOM   787  C CA  . ASN A  1 99  ? -43.48600 6.49200   2.37700   1.000 15.90929  ? 150 ASN B CA  1 
ATOM   788  C C   . ASN A  1 99  ? -42.75300 5.15600   2.26400   1.000 20.03337  ? 150 ASN B C   1 
ATOM   789  O O   . ASN A  1 99  ? -43.41200 4.10100   2.17400   1.000 16.22349  ? 150 ASN B O   1 
ATOM   790  C CB  . ASN A  1 99  ? -44.31100 6.79400   1.13400   1.000 12.92464  ? 150 ASN B CB  1 
ATOM   791  C CG  . ASN A  1 99  ? -45.22200 8.00700   1.32900   1.000 20.34759  ? 150 ASN B CG  1 
ATOM   792  O OD1 . ASN A  1 99  ? -45.50400 8.42200   2.46000   1.000 19.57069  ? 150 ASN B OD1 1 
ATOM   793  N ND2 . ASN A  1 99  ? -45.63900 8.59900   0.24100   1.000 15.76929  ? 150 ASN B ND2 1 
ATOM   794  N N   . LEU A  1 100 ? -41.41800 5.15300   2.30600   1.000 16.70710  ? 151 LEU B N   1 
ATOM   795  C CA  . LEU A  1 100 ? -40.62300 3.92700   2.25300   1.000 14.54690  ? 151 LEU B CA  1 
ATOM   796  C C   . LEU A  1 100 ? -39.71600 3.84000   3.45400   1.000 18.16970  ? 151 LEU B C   1 
ATOM   797  O O   . LEU A  1 100 ? -39.49100 4.82000   4.15600   1.000 20.94561  ? 151 LEU B O   1 
ATOM   798  C CB  . LEU A  1 100 ? -39.76200 3.84800   0.98600   1.000 17.99183  ? 151 LEU B CB  1 
ATOM   799  C CG  . LEU A  1 100 ? -40.45900 4.22400   -0.31100  1.000 18.77312  ? 151 LEU B CG  1 
ATOM   800  C CD1 . LEU A  1 100 ? -39.45000 4.17600   -1.46600  1.000 16.12726  ? 151 LEU B CD1 1 
ATOM   801  C CD2 . LEU A  1 100 ? -41.63200 3.28600   -0.52900  1.000 12.82595  ? 151 LEU B CD2 1 
ATOM   802  N N   . LEU A  1 101 ? -39.18200 2.64400   3.68200   1.000 14.45620  ? 152 LEU B N   1 
ATOM   803  C CA  . LEU A  1 101 ? -38.31300 2.38700   4.81200   1.000 15.78847  ? 152 LEU B CA  1 
ATOM   804  C C   . LEU A  1 101 ? -37.08600 1.67100   4.29900   1.000 18.46548  ? 152 LEU B C   1 
ATOM   805  O O   . LEU A  1 101 ? -37.19700 0.60900   3.67500   1.000 16.90554  ? 152 LEU B O   1 
ATOM   806  C CB  . LEU A  1 101 ? -39.03000 1.56700   5.89700   1.000 17.69780  ? 152 LEU B CB  1 
ATOM   807  C CG  . LEU A  1 101 ? -38.28800 1.39700   7.23100   1.000 19.16634  ? 152 LEU B CG  1 
ATOM   808  C CD1 . LEU A  1 101 ? -38.17900 2.69000   7.96500   1.000 19.14457  ? 152 LEU B CD1 1 
ATOM   809  C CD2 . LEU A  1 101 ? -39.11000 0.39600   8.07400   1.000 14.59735  ? 152 LEU B CD2 1 
ATOM   810  N N   . TRP A  1 102 ? -35.92500 2.24700   4.54300   1.000 14.47821  ? 153 TRP B N   1 
ATOM   811  C CA  . TRP A  1 102 ? -34.67000 1.62000   4.10900   1.000 16.68431  ? 153 TRP B CA  1 
ATOM   812  C C   . TRP A  1 102 ? -34.19800 0.62600   5.15900   1.000 15.46510  ? 153 TRP B C   1 
ATOM   813  O O   . TRP A  1 102 ? -33.42400 0.96100   6.06000   1.000 17.45381  ? 153 TRP B O   1 
ATOM   814  C CB  . TRP A  1 102 ? -33.60300 2.67700   3.85800   1.000 17.58381  ? 153 TRP B CB  1 
ATOM   815  C CG  . TRP A  1 102 ? -32.43900 2.17200   3.07000   1.000 16.72351  ? 153 TRP B CG  1 
ATOM   816  C CD1 . TRP A  1 102 ? -31.92000 0.87700   3.04500   1.000 17.21031  ? 153 TRP B CD1 1 
ATOM   817  C CD2 . TRP A  1 102 ? -31.61500 2.94600   2.20600   1.000 14.51356  ? 153 TRP B CD2 1 
ATOM   818  N NE1 . TRP A  1 102 ? -30.82400 0.82300   2.19700   1.000 19.49828  ? 153 TRP B NE1 1 
ATOM   819  C CE2 . TRP A  1 102 ? -30.63300 2.07300   1.65800   1.000 15.97956  ? 153 TRP B CE2 1 
ATOM   820  C CE3 . TRP A  1 102 ? -31.61900 4.28600   1.82600   1.000 20.28492  ? 153 TRP B CE3 1 
ATOM   821  C CZ2 . TRP A  1 102 ? -29.68400 2.50500   0.75300   1.000 17.92034  ? 153 TRP B CZ2 1 
ATOM   822  C CZ3 . TRP A  1 102 ? -30.67600 4.71400   0.91400   1.000 19.29182  ? 153 TRP B CZ3 1 
ATOM   823  C CH2 . TRP A  1 102 ? -29.70900 3.83100   0.39500   1.000 16.31546  ? 153 TRP B CH2 1 
ATOM   824  N N   . LEU A  1 103 ? -34.58200 -0.63800  4.98400   1.000 16.99863  ? 154 LEU B N   1 
ATOM   825  C CA  . LEU A  1 103 ? -34.22100 -1.69400  5.91400   1.000 15.58843  ? 154 LEU B CA  1 
ATOM   826  C C   . LEU A  1 103 ? -32.76200 -2.08700  5.74200   1.000 19.70250  ? 154 LEU B C   1 
ATOM   827  O O   . LEU A  1 103 ? -32.28500 -2.25300  4.62400   1.000 16.44237  ? 154 LEU B O   1 
ATOM   828  C CB  . LEU A  1 103 ? -35.08000 -2.91700  5.68500   1.000 13.45163  ? 154 LEU B CB  1 
ATOM   829  C CG  . LEU A  1 103 ? -36.58000 -2.78700  6.00600   1.000 17.43496  ? 154 LEU B CG  1 
ATOM   830  C CD1 . LEU A  1 103 ? -37.26300 -4.04400  5.39400   1.000 20.27556  ? 154 LEU B CD1 1 
ATOM   831  C CD2 . LEU A  1 103 ? -36.86000 -2.67500  7.54400   1.000 15.77200  ? 154 LEU B CD2 1 
ATOM   832  N N   . ILE A  1 104 ? -32.07300 -2.23800  6.86900   1.000 14.80530  ? 155 ILE B N   1 
ATOM   833  C CA  . ILE A  1 104 ? -30.66900 -2.58500  6.92300   1.000 23.04514  ? 155 ILE B CA  1 
ATOM   834  C C   . ILE A  1 104 ? -30.50400 -3.62500  8.02200   1.000 18.82048  ? 155 ILE B C   1 
ATOM   835  O O   . ILE A  1 104 ? -31.41900 -3.89200  8.80600   1.000 20.12279  ? 155 ILE B O   1 
ATOM   836  C CB  . ILE A  1 104 ? -29.77500 -1.31800  7.11600   1.000 20.53578  ? 155 ILE B CB  1 
ATOM   837  C CG1 . ILE A  1 104 ? -29.89900 -0.72700  8.52600   1.000 26.26102  ? 155 ILE B CG1 1 
ATOM   838  C CG2 . ILE A  1 104 ? -29.98300 -0.26500  6.02200   1.000 16.34422  ? 155 ILE B CG2 1 
ATOM   839  C CD1 . ILE A  1 104 ? -28.85000 0.32300   8.81300   1.000 28.80425  ? 155 ILE B CD1 1 
ATOM   840  N N   . GLY A  1 105 ? -29.33500 -4.24000  8.05000   1.000 22.58683  ? 156 GLY B N   1 
ATOM   841  C CA  . GLY A  1 105 ? -29.07800 -5.29800  9.00600   1.000 20.00563  ? 156 GLY B CA  1 
ATOM   842  C C   . GLY A  1 105 ? -29.17200 -4.83500  10.45100  1.000 19.92374  ? 156 GLY B C   1 
ATOM   843  O O   . GLY A  1 105 ? -29.17600 -3.63600  10.77200  1.000 22.02583  ? 156 GLY B O   1 
ATOM   844  N N   . LYS A  1 106 ? -29.28000 -5.82700  11.32700  1.000 22.52864  ? 157 LYS B N   1 
ATOM   845  C CA  . LYS A  1 106 ? -29.35700 -5.58300  12.75000  1.000 24.28035  ? 157 LYS B CA  1 
ATOM   846  C C   . LYS A  1 106 ? -28.49000 -6.61100  13.46400  1.000 27.50635  ? 157 LYS B C   1 
ATOM   847  O O   . LYS A  1 106 ? -28.57000 -7.79800  13.20500  1.000 28.97840  ? 157 LYS B O   1 
ATOM   848  C CB  . LYS A  1 106 ? -30.80100 -5.64700  13.26200  1.000 27.66410  ? 157 LYS B CB  1 
ATOM   849  C CG  . LYS A  1 106 ? -30.96600 -5.48600  14.75700  1.000 31.46446  ? 157 LYS B CG  1 
ATOM   850  C CD  . LYS A  1 106 ? -32.38600 -5.07800  15.08700  1.000 28.47561  ? 157 LYS B CD  1 
ATOM   851  C CE  . LYS A  1 106 ? -32.79100 -5.56700  16.46200  1.000 39.88958  ? 157 LYS B CE  1 
ATOM   852  N NZ  . LYS A  1 106 ? -34.13300 -5.08000  16.86200  1.000 31.86591  ? 157 LYS B NZ  1 
ATOM   853  N N   . ASN A  1 107 ? -27.64800 -6.16100  14.35500  1.000 30.43007  ? 158 ASN B N   1 
ATOM   854  C CA  . ASN A  1 107 ? -26.74700 -7.06400  15.02600  1.000 33.77403  ? 158 ASN B CA  1 
ATOM   855  C C   . ASN A  1 107 ? -25.93800 -7.85300  13.99900  1.000 34.13777  ? 158 ASN B C   1 
ATOM   856  O O   . ASN A  1 107 ? -25.87400 -9.06900  14.05600  1.000 29.27775  ? 158 ASN B O   1 
ATOM   857  C CB  . ASN A  1 107 ? -27.52100 -7.94100  16.00800  1.000 35.54637  ? 158 ASN B CB  1 
ATOM   858  C CG  . ASN A  1 107 ? -28.17800 -7.13500  17.10000  1.000 51.88805  ? 158 ASN B CG  1 
ATOM   859  O OD1 . ASN A  1 107 ? -27.56100 -6.25000  17.69300  1.000 56.55979  ? 158 ASN B OD1 1 
ATOM   860  N ND2 . ASN A  1 107 ? -29.43900 -7.42700  17.36800  1.000 60.78204  ? 158 ASN B ND2 1 
ATOM   861  N N   . SER A  1 108 ? -25.38600 -7.14800  13.02200  1.000 34.08436  ? 159 SER B N   1 
ATOM   862  C CA  . SER A  1 108 ? -24.46700 -7.79600  12.04800  1.000 33.64417  ? 159 SER B CA  1 
ATOM   863  C C   . SER A  1 108 ? -25.11500 -8.88600  11.18600  1.000 32.91857  ? 159 SER B C   1 
ATOM   864  O O   . SER A  1 108 ? -24.37400 -9.71000  10.65100  1.000 28.29737  ? 159 SER B O   1 
ATOM   865  C CB  . SER A  1 108 ? -23.24000 -8.28200  12.77800  1.000 36.27059  ? 159 SER B CB  1 
ATOM   866  O OG  . SER A  1 108 ? -22.76200 -7.27800  13.65700  1.000 44.72672  ? 159 SER B OG  1 
ATOM   867  N N   . THR A  1 109 ? -26.43700 -8.86800  11.04000  1.000 32.55218  ? 160 THR B N   1 
ATOM   868  C CA  . THR A  1 109 ? -27.12900 -9.79200  10.15500  1.000 31.59688  ? 160 THR B CA  1 
ATOM   869  C C   . THR A  1 109 ? -28.41500 -9.19600  9.55600   1.000 26.52202  ? 160 THR B C   1 
ATOM   870  O O   . THR A  1 109 ? -28.92800 -8.22300  10.06300  1.000 27.35600  ? 160 THR B O   1 
ATOM   871  C CB  . THR A  1 109 ? -27.44900 -11.13100 10.84300  1.000 36.54206  ? 160 THR B CB  1 
ATOM   872  O OG1 . THR A  1 109 ? -27.68600 -12.13000 9.84800   1.000 42.58018  ? 160 THR B OG1 1 
ATOM   873  C CG2 . THR A  1 109 ? -28.67300 -11.00400 11.72900  1.000 29.77839  ? 160 THR B CG2 1 
ATOM   874  N N   . TYR A  1 110 ? -28.89200 -9.78100  8.47300   1.000 29.13047  ? 161 TYR B N   1 
ATOM   875  C CA  . TYR A  1 110 ? -30.09600 -9.31800  7.79800   1.000 26.45915  ? 161 TYR B CA  1 
ATOM   876  C C   . TYR A  1 110 ? -30.92900 -10.52300 7.51000   1.000 24.96886  ? 161 TYR B C   1 
ATOM   877  O O   . TYR A  1 110 ? -30.79600 -11.15700 6.48500   1.000 25.38195  ? 161 TYR B O   1 
ATOM   878  C CB  . TYR A  1 110 ? -29.77200 -8.58300  6.50200   1.000 26.62357  ? 161 TYR B CB  1 
ATOM   879  C CG  . TYR A  1 110 ? -30.95000 -7.94200  5.78800   1.000 21.60660  ? 161 TYR B CG  1 
ATOM   880  C CD1 . TYR A  1 110 ? -31.97400 -8.71100  5.25400   1.000 16.84690  ? 161 TYR B CD1 1 
ATOM   881  C CD2 . TYR A  1 110 ? -31.01300 -6.56900  5.61800   1.000 17.33752  ? 161 TYR B CD2 1 
ATOM   882  C CE1 . TYR A  1 110 ? -33.03300 -8.12900  4.59100   1.000 19.35563  ? 161 TYR B CE1 1 
ATOM   883  C CE2 . TYR A  1 110 ? -32.06900 -5.97800  4.95300   1.000 21.26867  ? 161 TYR B CE2 1 
ATOM   884  C CZ  . TYR A  1 110 ? -33.07800 -6.76000  4.44200   1.000 19.50072  ? 161 TYR B CZ  1 
ATOM   885  O OH  . TYR A  1 110 ? -34.12400 -6.17400  3.78100   1.000 15.96687  ? 161 TYR B OH  1 
ATOM   886  N N   . PRO A  1 111 ? -31.80700 -10.84100 8.43900   1.000 22.79703  ? 162 PRO B N   1 
ATOM   887  C CA  . PRO A  1 111 ? -32.58200 -12.04700 8.27300   1.000 18.02443  ? 162 PRO B CA  1 
ATOM   888  C C   . PRO A  1 111 ? -33.57100 -12.02200 7.12500   1.000 23.15199  ? 162 PRO B C   1 
ATOM   889  O O   . PRO A  1 111 ? -33.98700 -10.97600 6.69000   1.000 21.16806  ? 162 PRO B O   1 
ATOM   890  C CB  . PRO A  1 111 ? -33.32400 -12.15100 9.61000   1.000 17.71683  ? 162 PRO B CB  1 
ATOM   891  C CG  . PRO A  1 111 ? -32.62000 -11.25200 10.55100  1.000 24.34941  ? 162 PRO B CG  1 
ATOM   892  C CD  . PRO A  1 111 ? -32.08700 -10.15400 9.70400   1.000 23.87847  ? 162 PRO B CD  1 
ATOM   893  N N   . ASN A  1 112 ? -33.89000 -13.19300 6.61300   1.000 19.67349  ? 163 ASN B N   1 
ATOM   894  C CA  . ASN A  1 112 ? -34.92300 -13.29400 5.62500   1.000 21.22531  ? 163 ASN B CA  1 
ATOM   895  C C   . ASN A  1 112 ? -36.20200 -12.67800 6.17600   1.000 21.90071  ? 163 ASN B C   1 
ATOM   896  O O   . ASN A  1 112 ? -36.50600 -12.80000 7.34100   1.000 22.04664  ? 163 ASN B O   1 
ATOM   897  C CB  . ASN A  1 112 ? -35.21500 -14.74800 5.28600   1.000 28.16929  ? 163 ASN B CB  1 
ATOM   898  C CG  . ASN A  1 112 ? -34.06400 -15.45300 4.60200   1.000 35.39211  ? 163 ASN B CG  1 
ATOM   899  O OD1 . ASN A  1 112 ? -33.03900 -14.86400 4.31100   1.000 32.86324  ? 163 ASN B OD1 1 
ATOM   900  N ND2 . ASN A  1 112 ? -34.24800 -16.73500 4.32800   1.000 39.77000  ? 163 ASN B ND2 1 
ATOM   901  N N   . LEU A  1 113 ? -36.93200 -12.02000 5.32500   1.000 18.04386  ? 164 LEU B N   1 
ATOM   902  C CA  . LEU A  1 113 ? -38.17600 -11.38900 5.74100   1.000 22.25087  ? 164 LEU B CA  1 
ATOM   903  C C   . LEU A  1 113 ? -39.30800 -11.79700 4.81400   1.000 21.01254  ? 164 LEU B C   1 
ATOM   904  O O   . LEU A  1 113 ? -39.10900 -12.12300 3.63200   1.000 16.94682  ? 164 LEU B O   1 
ATOM   905  C CB  . LEU A  1 113 ? -38.04900 -9.86200  5.81200   1.000 20.57140  ? 164 LEU B CB  1 
ATOM   906  C CG  . LEU A  1 113 ? -37.89300 -9.08500  4.49100   1.000 20.82307  ? 164 LEU B CG  1 
ATOM   907  C CD1 . LEU A  1 113 ? -39.22800 -8.77000  3.73900   1.000 22.57779  ? 164 LEU B CD1 1 
ATOM   908  C CD2 . LEU A  1 113 ? -37.13700 -7.76100  4.86900   1.000 21.15663  ? 164 LEU B CD2 1 
ATOM   909  N N   . SER A  1 114 ? -40.51100 -11.81400 5.37500   1.000 16.42109  ? 165 SER B N   1 
ATOM   910  C CA  . SER A  1 114 ? -41.65400 -12.15400 4.55900   1.000 22.75445  ? 165 SER B CA  1 
ATOM   911  C C   . SER A  1 114 ? -42.82600 -11.39100 5.13600   1.000 23.00858  ? 165 SER B C   1 
ATOM   912  O O   . SER A  1 114 ? -43.04700 -11.39400 6.36100   1.000 27.25861  ? 165 SER B O   1 
ATOM   913  C CB  . SER A  1 114 ? -41.88500 -13.66400 4.53300   1.000 21.28919  ? 165 SER B CB  1 
ATOM   914  O OG  . SER A  1 114 ? -43.20300 -13.92500 4.09200   1.000 25.54752  ? 165 SER B OG  1 
ATOM   915  N N   . LYS A  1 115 ? -43.51100 -10.65300 4.28100   1.000 15.98274  ? 166 LYS B N   1 
ATOM   916  C CA  . LYS A  1 115 ? -44.48000 -9.70700  4.79700   1.000 20.13112  ? 166 LYS B CA  1 
ATOM   917  C C   . LYS A  1 115 ? -45.64300 -9.70500  3.82300   1.000 24.58063  ? 166 LYS B C   1 
ATOM   918  O O   . LYS A  1 115 ? -45.40800 -9.71700  2.61200   1.000 20.76398  ? 166 LYS B O   1 
ATOM   919  C CB  . LYS A  1 115 ? -43.79900 -8.33400  4.96400   1.000 27.48419  ? 166 LYS B CB  1 
ATOM   920  C CG  . LYS A  1 115 ? -44.55000 -7.28500  5.69200   1.000 31.55100  ? 166 LYS B CG  1 
ATOM   921  C CD  . LYS A  1 115 ? -44.56800 -7.60200  7.15100   1.000 30.88513  ? 166 LYS B CD  1 
ATOM   922  C CE  . LYS A  1 115 ? -43.27200 -7.34300  7.88400   1.000 22.97400  ? 166 LYS B CE  1 
ATOM   923  N NZ  . LYS A  1 115 ? -43.65600 -7.29200  9.38800   1.000 22.51948  ? 166 LYS B NZ  1 
ATOM   924  N N   . SER A  1 116 ? -46.84900 -9.84300  4.33000   1.000 15.37313  ? 167 SER B N   1 
ATOM   925  C CA  A SER A  1 116 ? -48.03800 -9.78700  3.49700   0.585 20.85750  ? 167 SER B CA  1 
ATOM   926  C CA  B SER A  1 116 ? -48.05200 -9.80700  3.51200   0.415 20.83107  ? 167 SER B CA  1 
ATOM   927  C C   . SER A  1 116 ? -49.12100 -8.75000  3.94900   1.000 19.05011  ? 167 SER B C   1 
ATOM   928  O O   . SER A  1 116 ? -49.21000 -8.27700  5.10000   1.000 21.28545  ? 167 SER B O   1 
ATOM   929  C CB  A SER A  1 116 ? -48.66400 -11.18700 3.40500   0.585 19.30507  ? 167 SER B CB  1 
ATOM   930  C CB  B SER A  1 116 ? -48.68800 -11.20500 3.51900   0.415 19.35988  ? 167 SER B CB  1 
ATOM   931  O OG  A SER A  1 116 ? -49.09400 -11.64000 4.67100   0.585 17.04867  ? 167 SER B OG  1 
ATOM   932  O OG  B SER A  1 116 ? -47.86400 -12.14500 2.86200   0.415 17.73414  ? 167 SER B OG  1 
ATOM   933  N N   . TYR A  1 117 ? -49.85300 -8.26200  2.98600   1.000 14.41141  ? 168 TYR B N   1 
ATOM   934  C CA  . TYR A  1 117 ? -50.94800 -7.37000  3.31800   1.000 19.05661  ? 168 TYR B CA  1 
ATOM   935  C C   . TYR A  1 117 ? -52.19100 -7.72000  2.49800   1.000 24.76070  ? 168 TYR B C   1 
ATOM   936  O O   . TYR A  1 117 ? -52.13500 -7.74100  1.27900   1.000 18.54965  ? 168 TYR B O   1 
ATOM   937  C CB  . TYR A  1 117 ? -50.65100 -5.89100  3.11000   1.000 14.01838  ? 168 TYR B CB  1 
ATOM   938  C CG  . TYR A  1 117 ? -51.87500 -5.02900  3.19200   1.000 19.09045  ? 168 TYR B CG  1 
ATOM   939  C CD1 . TYR A  1 117 ? -52.48300 -4.77700  4.40700   1.000 21.65463  ? 168 TYR B CD1 1 
ATOM   940  C CD2 . TYR A  1 117 ? -52.43500 -4.47800  2.05500   1.000 19.40811  ? 168 TYR B CD2 1 
ATOM   941  C CE1 . TYR A  1 117 ? -53.60900 -3.99100  4.49100   1.000 19.69683  ? 168 TYR B CE1 1 
ATOM   942  C CE2 . TYR A  1 117 ? -53.56200 -3.69400  2.12700   1.000 18.79625  ? 168 TYR B CE2 1 
ATOM   943  C CZ  . TYR A  1 117 ? -54.14500 -3.45300  3.35000   1.000 26.28618  ? 168 TYR B CZ  1 
ATOM   944  O OH  . TYR A  1 117 ? -55.26700 -2.67800  3.42900   1.000 23.47350  ? 168 TYR B OH  1 
ATOM   945  N N   . ALA A  1 118 ? -53.27600 -8.00900  3.18500   1.000 18.17411  ? 169 ALA B N   1 
ATOM   946  C CA  . ALA A  1 118 ? -54.53000 -8.28600  2.52600   1.000 20.75941  ? 169 ALA B CA  1 
ATOM   947  C C   . ALA A  1 118 ? -55.37500 -7.02400  2.46300   1.000 19.34365  ? 169 ALA B C   1 
ATOM   948  O O   . ALA A  1 118 ? -55.64800 -6.40500  3.45800   1.000 20.67055  ? 169 ALA B O   1 
ATOM   949  C CB  . ALA A  1 118 ? -55.25600 -9.39200  3.23700   1.000 21.13954  ? 169 ALA B CB  1 
ATOM   950  N N   . ASN A  1 119 ? -55.79500 -6.66900  1.27600   1.000 17.71475  ? 170 ASN B N   1 
ATOM   951  C CA  . ASN A  1 119 ? -56.58300 -5.48000  1.08600   1.000 21.93769  ? 170 ASN B CA  1 
ATOM   952  C C   . ASN A  1 119 ? -58.01900 -5.74400  1.49500   1.000 28.24087  ? 170 ASN B C   1 
ATOM   953  O O   . ASN A  1 119 ? -58.81700 -6.21600  0.71300   1.000 22.59017  ? 170 ASN B O   1 
ATOM   954  C CB  . ASN A  1 119 ? -56.49800 -4.97000  -0.36400  1.000 15.73215  ? 170 ASN B CB  1 
ATOM   955  C CG  . ASN A  1 119 ? -57.26900 -3.69800  -0.58200  1.000 19.84929  ? 170 ASN B CG  1 
ATOM   956  O OD1 . ASN A  1 119 ? -57.96100 -3.21800  0.30500   1.000 24.04298  ? 170 ASN B OD1 1 
ATOM   957  N ND2 . ASN A  1 119 ? -57.14500 -3.14000  -1.76800  1.000 14.44210  ? 170 ASN B ND2 1 
ATOM   958  N N   . ASN A  1 120 ? -58.33700 -5.40500  2.73200   1.000 30.86101  ? 171 ASN B N   1 
ATOM   959  C CA  . ASN A  1 120 ? -59.68300 -5.57000  3.26700   1.000 31.78931  ? 171 ASN B CA  1 
ATOM   960  C C   . ASN A  1 120 ? -60.42700 -4.28400  3.11700   1.000 35.98054  ? 171 ASN B C   1 
ATOM   961  O O   . ASN A  1 120 ? -61.56900 -4.16600  3.51800   1.000 38.40630  ? 171 ASN B O   1 
ATOM   962  C CB  . ASN A  1 120 ? -59.62700 -5.94400  4.74300   1.000 24.09741  ? 171 ASN B CB  1 
ATOM   963  C CG  . ASN A  1 120 ? -59.10000 -4.82900  5.60600   1.000 35.33179  ? 171 ASN B CG  1 
ATOM   964  O OD1 . ASN A  1 120 ? -58.68400 -3.79100  5.11300   1.000 37.65900  ? 171 ASN B OD1 1 
ATOM   965  N ND2 . ASN A  1 120 ? -59.11100 -5.04300  6.91100   1.000 39.47579  ? 171 ASN B ND2 1 
ATOM   966  N N   . LYS A  1 121 ? -59.76300 -3.29500  2.57100   1.000 26.72119  ? 172 LYS B N   1 
ATOM   967  C CA  . LYS A  1 121 ? -60.43800 -2.08100  2.30000   1.000 27.06438  ? 172 LYS B CA  1 
ATOM   968  C C   . LYS A  1 121 ? -61.32300 -2.38900  1.08200   1.000 31.49511  ? 172 LYS B C   1 
ATOM   969  O O   . LYS A  1 121 ? -61.31300 -3.48400  0.53500   1.000 35.26983  ? 172 LYS B O   1 
ATOM   970  C CB  . LYS A  1 121 ? -59.46200 -0.94800  2.08800   1.000 23.60521  ? 172 LYS B CB  1 
ATOM   971  C CG  . LYS A  1 121 ? -58.21100 -1.04400  2.92800   1.000 34.42367  ? 172 LYS B CG  1 
ATOM   972  C CD  . LYS A  1 121 ? -57.91500 0.26500   3.62500   1.000 33.13956  ? 172 LYS B CD  1 
ATOM   973  C CE  . LYS A  1 121 ? -56.68100 0.14700   4.49400   1.000 31.22239  ? 172 LYS B CE  1 
ATOM   974  N NZ  . LYS A  1 121 ? -57.01100 0.38400   5.92000   1.000 37.38763  ? 172 LYS B NZ  1 
ATOM   975  N N   . GLU A  1 122 ? -62.12400 -1.45700  0.69100   1.000 27.07771  ? 173 GLU B N   1 
ATOM   976  C CA  . GLU A  1 122 ? -63.03400 -1.74800  -0.39800  1.000 33.48807  ? 173 GLU B CA  1 
ATOM   977  C C   . GLU A  1 122 ? -62.68800 -0.85600  -1.53900  1.000 25.31391  ? 173 GLU B C   1 
ATOM   978  O O   . GLU A  1 122 ? -63.53000 -0.53900  -2.34900  1.000 27.32904  ? 173 GLU B O   1 
ATOM   979  C CB  . GLU A  1 122 ? -64.47500 -1.59200  0.07400   1.000 40.28755  ? 173 GLU B CB  1 
ATOM   980  C CG  . GLU A  1 122 ? -64.91200 -2.71500  0.99200   1.000 43.11906  ? 173 GLU B CG  1 
ATOM   981  C CD  . GLU A  1 122 ? -66.16100 -2.37500  1.77200   1.000 64.04605  ? 173 GLU B CD  1 
ATOM   982  O OE1 . GLU A  1 122 ? -66.97600 -1.57100  1.27300   1.000 62.70782  ? 173 GLU B OE1 1 
ATOM   983  O OE2 . GLU A  1 122 ? -66.32100 -2.91300  2.88400   1.000 63.30052  ? 173 GLU B OE2 1 
ATOM   984  N N   . LYS A  1 123 ? -61.43900 -0.43800  -1.56300  1.000 27.53424  ? 174 LYS B N   1 
ATOM   985  C CA  . LYS A  1 123 ? -60.93100 0.37800   -2.63500  1.000 24.75621  ? 174 LYS B CA  1 
ATOM   986  C C   . LYS A  1 123 ? -59.55300 -0.14200  -3.02700  1.000 27.15609  ? 174 LYS B C   1 
ATOM   987  O O   . LYS A  1 123 ? -58.95500 -0.89300  -2.28700  1.000 23.79543  ? 174 LYS B O   1 
ATOM   988  C CB  . LYS A  1 123 ? -60.78900 1.81300   -2.18900  1.000 26.78801  ? 174 LYS B CB  1 
ATOM   989  C CG  . LYS A  1 123 ? -62.01700 2.50300   -1.64700  1.000 37.07633  ? 174 LYS B CG  1 
ATOM   990  C CD  . LYS A  1 123 ? -61.59400 3.50000   -0.58600  1.000 38.50271  ? 174 LYS B CD  1 
ATOM   991  C CE  . LYS A  1 123 ? -62.51500 4.70300   -0.52100  1.000 45.35674  ? 174 LYS B CE  1 
ATOM   992  N NZ  . LYS A  1 123 ? -62.58000 5.44000   -1.80600  1.000 43.92885  ? 174 LYS B NZ  1 
ATOM   993  N N   . GLU A  1 124 ? -59.06000 0.25800   -4.18500  1.000 20.04295  ? 175 GLU B N   1 
ATOM   994  C CA  . GLU A  1 124 ? -57.71900 -0.11400  -4.59300  1.000 25.26013  ? 175 GLU B CA  1 
ATOM   995  C C   . GLU A  1 124 ? -56.69300 0.45100   -3.63100  1.000 20.88908  ? 175 GLU B C   1 
ATOM   996  O O   . GLU A  1 124 ? -56.89400 1.53200   -3.11300  1.000 19.79359  ? 175 GLU B O   1 
ATOM   997  C CB  . GLU A  1 124 ? -57.42500 0.40500   -5.99900  1.000 16.65912  ? 175 GLU B CB  1 
ATOM   998  C CG  . GLU A  1 124 ? -58.03900 -0.38300  -7.13700  1.000 22.24350  ? 175 GLU B CG  1 
ATOM   999  C CD  . GLU A  1 124 ? -57.70900 0.21200   -8.49600  1.000 32.94709  ? 175 GLU B CD  1 
ATOM   1000 O OE1 . GLU A  1 124 ? -57.73300 1.44700   -8.63200  1.000 32.03952  ? 175 GLU B OE1 1 
ATOM   1001 O OE2 . GLU A  1 124 ? -57.42900 -0.55400  -9.43200  1.000 27.12203  ? 175 GLU B OE2 1 
ATOM   1002 N N   . VAL A  1 125 ? -55.60900 -0.27400  -3.38800  1.000 17.67463  ? 176 VAL B N   1 
ATOM   1003 C CA  . VAL A  1 125 ? -54.53000 0.28300   -2.57400  1.000 17.96880  ? 176 VAL B CA  1 
ATOM   1004 C C   . VAL A  1 125 ? -53.26700 0.38800   -3.44300  1.000 21.60567  ? 176 VAL B C   1 
ATOM   1005 O O   . VAL A  1 125 ? -52.75300 -0.62700  -3.93400  1.000 19.70431  ? 176 VAL B O   1 
ATOM   1006 C CB  . VAL A  1 125 ? -54.28300 -0.54500  -1.31100  1.000 15.94384  ? 176 VAL B CB  1 
ATOM   1007 C CG1 . VAL A  1 125 ? -52.93800 -0.15600  -0.65700  1.000 17.77988  ? 176 VAL B CG1 1 
ATOM   1008 C CG2 . VAL A  1 125 ? -55.47600 -0.36100  -0.30600  1.000 18.41781  ? 176 VAL B CG2 1 
ATOM   1009 N N   . LEU A  1 126 ? -52.74200 1.59000   -3.54300  1.000 17.85396  ? 177 LEU B N   1 
ATOM   1010 C CA  . LEU A  1 126 ? -51.50400 1.80700   -4.23700  1.000 17.90904  ? 177 LEU B CA  1 
ATOM   1011 C C   . LEU A  1 126 ? -50.32400 1.49300   -3.32000  1.000 19.27884  ? 177 LEU B C   1 
ATOM   1012 O O   . LEU A  1 126 ? -50.19300 2.09200   -2.26300  1.000 16.73917  ? 177 LEU B O   1 
ATOM   1013 C CB  . LEU A  1 126 ? -51.38800 3.22600   -4.75300  1.000 15.36271  ? 177 LEU B CB  1 
ATOM   1014 C CG  . LEU A  1 126 ? -50.02200 3.64300   -5.29700  1.000 16.37432  ? 177 LEU B CG  1 
ATOM   1015 C CD1 . LEU A  1 126 ? -49.74400 2.93300   -6.60700  1.000 11.32460  ? 177 LEU B CD1 1 
ATOM   1016 C CD2 . LEU A  1 126 ? -49.92200 5.15100   -5.46000  1.000 18.00862  ? 177 LEU B CD2 1 
ATOM   1017 N N   . VAL A  1 127 ? -49.51300 0.53000   -3.72600  1.000 14.53625  ? 178 VAL B N   1 
ATOM   1018 C CA  . VAL A  1 127 ? -48.32200 0.16700   -2.97000  1.000 10.85318  ? 178 VAL B CA  1 
ATOM   1019 C C   . VAL A  1 127 ? -47.04600 0.50300   -3.74000  1.000 14.94915  ? 178 VAL B C   1 
ATOM   1020 O O   . VAL A  1 127 ? -46.93300 0.17500   -4.89300  1.000 14.42527  ? 178 VAL B O   1 
ATOM   1021 C CB  . VAL A  1 127 ? -48.28600 -1.32300  -2.54400  1.000 13.00999  ? 178 VAL B CB  1 
ATOM   1022 C CG1 . VAL A  1 127 ? -47.13200 -1.57900  -1.59700  1.000 10.94447  ? 178 VAL B CG1 1 
ATOM   1023 C CG2 . VAL A  1 127 ? -49.61500 -1.75500  -1.95200  1.000 13.94749  ? 178 VAL B CG2 1 
ATOM   1024 N N   . LEU A  1 128 ? -46.10900 1.13300   -3.06900  1.000 11.84753  ? 179 LEU B N   1 
ATOM   1025 C CA  . LEU A  1 128 ? -44.85600 1.49900   -3.67000  1.000 14.01549  ? 179 LEU B CA  1 
ATOM   1026 C C   . LEU A  1 128 ? -43.66400 0.96600   -2.88700  1.000 15.53152  ? 179 LEU B C   1 
ATOM   1027 O O   . LEU A  1 128 ? -43.68200 0.93300   -1.66300  1.000 12.97772  ? 179 LEU B O   1 
ATOM   1028 C CB  . LEU A  1 128 ? -44.74000 2.99600   -3.77900  1.000 12.05549  ? 179 LEU B CB  1 
ATOM   1029 C CG  . LEU A  1 128 ? -45.86300 3.78200   -4.45100  1.000 17.11307  ? 179 LEU B CG  1 
ATOM   1030 C CD1 . LEU A  1 128 ? -46.67600 4.53400   -3.41500  1.000 12.75288  ? 179 LEU B CD1 1 
ATOM   1031 C CD2 . LEU A  1 128 ? -45.29400 4.73900   -5.48200  1.000 13.85869  ? 179 LEU B CD2 1 
ATOM   1032 N N   . TRP A  1 129 ? -42.63500 0.56300   -3.60300  1.000 10.00697  ? 180 TRP B N   1 
ATOM   1033 C CA  . TRP A  1 129 ? -41.42100 0.09000   -2.97900  1.000 7.35884   ? 180 TRP B CA  1 
ATOM   1034 C C   . TRP A  1 129 ? -40.18400 0.35300   -3.85300  1.000 10.67028  ? 180 TRP B C   1 
ATOM   1035 O O   . TRP A  1 129 ? -40.27600 0.88000   -4.92600  1.000 13.64180  ? 180 TRP B O   1 
ATOM   1036 C CB  . TRP A  1 129 ? -41.52600 -1.39400  -2.66400  1.000 10.82308  ? 180 TRP B CB  1 
ATOM   1037 C CG  . TRP A  1 129 ? -41.57700 -2.27000  -3.86400  1.000 12.11880  ? 180 TRP B CG  1 
ATOM   1038 C CD1 . TRP A  1 129 ? -40.54400 -2.95500  -4.41100  1.000 12.73555  ? 180 TRP B CD1 1 
ATOM   1039 C CD2 . TRP A  1 129 ? -42.72700 -2.57800  -4.65500  1.000 9.66835   ? 180 TRP B CD2 1 
ATOM   1040 N NE1 . TRP A  1 129 ? -40.96900 -3.67300  -5.49400  1.000 13.85899  ? 180 TRP B NE1 1 
ATOM   1041 C CE2 . TRP A  1 129 ? -42.30800 -3.46000  -5.66700  1.000 13.46567  ? 180 TRP B CE2 1 
ATOM   1042 C CE3 . TRP A  1 129 ? -44.06900 -2.19500  -4.60800  1.000 10.80974  ? 180 TRP B CE3 1 
ATOM   1043 C CZ2 . TRP A  1 129 ? -43.18100 -3.96000  -6.62600  1.000 10.35154  ? 180 TRP B CZ2 1 
ATOM   1044 C CZ3 . TRP A  1 129 ? -44.93200 -2.69300  -5.55500  1.000 11.42348  ? 180 TRP B CZ3 1 
ATOM   1045 C CH2 . TRP A  1 129 ? -44.48500 -3.56700  -6.55400  1.000 14.19041  ? 180 TRP B CH2 1 
ATOM   1046 N N   . GLY A  1 130 ? -39.05400 -0.06200  -3.36000  1.000 10.94277  ? 181 GLY B N   1 
ATOM   1047 C CA  . GLY A  1 130 ? -37.84300 0.06700   -4.11100  1.000 16.03342  ? 181 GLY B CA  1 
ATOM   1048 C C   . GLY A  1 130 ? -36.85800 -1.04800  -3.88900  1.000 13.38570  ? 181 GLY B C   1 
ATOM   1049 O O   . GLY A  1 130 ? -37.00000 -1.81000  -2.95300  1.000 13.17311  ? 181 GLY B O   1 
ATOM   1050 N N   . VAL A  1 131 ? -35.86800 -1.12500  -4.77000  1.000 13.30184  ? 182 VAL B N   1 
ATOM   1051 C CA  . VAL A  1 131 ? -34.79200 -2.14800  -4.64300  1.000 12.35482  ? 182 VAL B CA  1 
ATOM   1052 C C   . VAL A  1 131 ? -33.44600 -1.41600  -4.71800  1.000 13.67984  ? 182 VAL B C   1 
ATOM   1053 O O   . VAL A  1 131 ? -33.25900 -0.64200  -5.66200  1.000 11.91576  ? 182 VAL B O   1 
ATOM   1054 C CB  . VAL A  1 131 ? -34.92700 -3.25500  -5.70400  1.000 15.29213  ? 182 VAL B CB  1 
ATOM   1055 C CG1 . VAL A  1 131 ? -33.82400 -4.29500  -5.59500  1.000 12.66147  ? 182 VAL B CG1 1 
ATOM   1056 C CG2 . VAL A  1 131 ? -36.30400 -3.90000  -5.68900  1.000 15.95099  ? 182 VAL B CG2 1 
ATOM   1057 N N   . HIS A  1 132 ? -32.57900 -1.66100  -3.74800  1.000 13.65014  ? 183 HIS B N   1 
ATOM   1058 C CA  . HIS A  1 132 ? -31.27800 -0.95600  -3.66700  1.000 15.97142  ? 183 HIS B CA  1 
ATOM   1059 C C   . HIS A  1 132 ? -30.19000 -1.68600  -4.44500  1.000 16.66362  ? 183 HIS B C   1 
ATOM   1060 O O   . HIS A  1 132 ? -30.01700 -2.88600  -4.25000  1.000 16.50849  ? 183 HIS B O   1 
ATOM   1061 C CB  . HIS A  1 132 ? -30.84700 -0.75800  -2.21500  1.000 15.21385  ? 183 HIS B CB  1 
ATOM   1062 C CG  . HIS A  1 132 ? -29.57200 -0.00800  -2.06600  1.000 18.36774  ? 183 HIS B CG  1 
ATOM   1063 N ND1 . HIS A  1 132 ? -28.61700 -0.36800  -1.14700  1.000 15.75862  ? 183 HIS B ND1 1 
ATOM   1064 C CD2 . HIS A  1 132 ? -29.09300 1.07100   -2.71500  1.000 17.67509  ? 183 HIS B CD2 1 
ATOM   1065 C CE1 . HIS A  1 132 ? -27.60100 0.45900   -1.23400  1.000 22.03651  ? 183 HIS B CE1 1 
ATOM   1066 N NE2 . HIS A  1 132 ? -27.87000 1.34700   -2.18500  1.000 17.95652  ? 183 HIS B NE2 1 
ATOM   1067 N N   . HIS A  1 133 ? -29.49300 -0.94900  -5.28200  1.000 15.56729  ? 184 HIS B N   1 
ATOM   1068 C CA  . HIS A  1 133 ? -28.35000 -1.49500  -6.03800  1.000 13.90951  ? 184 HIS B CA  1 
ATOM   1069 C C   . HIS A  1 133 ? -27.10100 -0.76400  -5.54700  1.000 19.21614  ? 184 HIS B C   1 
ATOM   1070 O O   . HIS A  1 133 ? -26.88100 0.37000   -5.97500  1.000 20.10464  ? 184 HIS B O   1 
ATOM   1071 C CB  . HIS A  1 133 ? -28.60600 -1.29900  -7.51900  1.000 14.33794  ? 184 HIS B CB  1 
ATOM   1072 C CG  . HIS A  1 133 ? -29.91300 -1.85000  -7.97300  1.000 22.97888  ? 184 HIS B CG  1 
ATOM   1073 N ND1 . HIS A  1 133 ? -30.06100 -3.16200  -8.36600  1.000 22.15820  ? 184 HIS B ND1 1 
ATOM   1074 C CD2 . HIS A  1 133 ? -31.12800 -1.27900  -8.08700  1.000 17.62721  ? 184 HIS B CD2 1 
ATOM   1075 C CE1 . HIS A  1 133 ? -31.31000 -3.37100  -8.71400  1.000 21.96985  ? 184 HIS B CE1 1 
ATOM   1076 N NE2 . HIS A  1 133 ? -31.98500 -2.23400  -8.55000  1.000 19.01966  ? 184 HIS B NE2 1 
ATOM   1077 N N   . PRO A  1 134 ? -26.34100 -1.35100  -4.60900  1.000 18.14519  ? 185 PRO B N   1 
ATOM   1078 C CA  . PRO A  1 134 ? -25.18000 -0.69100  -4.02800  1.000 18.76584  ? 185 PRO B CA  1 
ATOM   1079 C C   . PRO A  1 134 ? -24.02900 -0.53900  -5.03600  1.000 21.90446  ? 185 PRO B C   1 
ATOM   1080 O O   . PRO A  1 134 ? -23.99100 -1.27900  -5.97600  1.000 21.45070  ? 185 PRO B O   1 
ATOM   1081 C CB  . PRO A  1 134 ? -24.81700 -1.61100  -2.85900  1.000 26.84170  ? 185 PRO B CB  1 
ATOM   1082 C CG  . PRO A  1 134 ? -26.04300 -2.45300  -2.63000  1.000 20.62279  ? 185 PRO B CG  1 
ATOM   1083 C CD  . PRO A  1 134 ? -26.59200 -2.66000  -4.02100  1.000 21.06678  ? 185 PRO B CD  1 
ATOM   1084 N N   . PRO A  1 135 ? -23.10700 0.43700   -4.86600  1.000 25.43622  ? 186 PRO B N   1 
ATOM   1085 C CA  . PRO A  1 135 ? -22.07100 0.64900   -5.90400  1.000 25.97926  ? 186 PRO B CA  1 
ATOM   1086 C C   . PRO A  1 135 ? -20.94900 -0.37600  -5.86300  1.000 24.99296  ? 186 PRO B C   1 
ATOM   1087 O O   . PRO A  1 135 ? -20.25000 -0.56200  -6.86700  1.000 30.86263  ? 186 PRO B O   1 
ATOM   1088 C CB  . PRO A  1 135 ? -21.54600 2.05000   -5.58900  1.000 25.31591  ? 186 PRO B CB  1 
ATOM   1089 C CG  . PRO A  1 135 ? -21.73700 2.18800   -4.06300  1.000 23.73672  ? 186 PRO B CG  1 
ATOM   1090 C CD  . PRO A  1 135 ? -23.01900 1.42800   -3.76900  1.000 20.46572  ? 186 PRO B CD  1 
ATOM   1091 N N   . ASP A  1 136 ? -20.76100 -1.05700  -4.74800  1.000 24.08104  ? 187 ASP B N   1 
ATOM   1092 C CA  . ASP A  1 136 ? -19.67100 -1.99700  -4.62000  1.000 23.44981  ? 187 ASP B CA  1 
ATOM   1093 C C   . ASP A  1 136 ? -20.04100 -3.06200  -3.59700  1.000 31.41059  ? 187 ASP B C   1 
ATOM   1094 O O   . ASP A  1 136 ? -21.01400 -2.93400  -2.83900  1.000 28.04219  ? 187 ASP B O   1 
ATOM   1095 C CB  . ASP A  1 136 ? -18.38000 -1.26400  -4.27200  1.000 25.99188  ? 187 ASP B CB  1 
ATOM   1096 C CG  . ASP A  1 136 ? -18.51100 -0.37900  -3.05100  1.000 37.23765  ? 187 ASP B CG  1 
ATOM   1097 O OD1 . ASP A  1 136 ? -18.93900 -0.85000  -1.96900  1.000 40.49610  ? 187 ASP B OD1 1 
ATOM   1098 O OD2 . ASP A  1 136 ? -18.19800 0.82200   -3.19000  1.000 43.18928  ? 187 ASP B OD2 1 
ATOM   1099 N N   . ALA A  1 137 ? -19.26200 -4.14500  -3.62600  1.000 28.25656  ? 188 ALA B N   1 
ATOM   1100 C CA  . ALA A  1 137 ? -19.51200 -5.29400  -2.76900  1.000 27.02835  ? 188 ALA B CA  1 
ATOM   1101 C C   . ALA A  1 137 ? -19.30200 -4.97000  -1.29100  1.000 34.14061  ? 188 ALA B C   1 
ATOM   1102 O O   . ALA A  1 137 ? -19.91900 -5.60900  -0.42200  1.000 28.94814  ? 188 ALA B O   1 
ATOM   1103 C CB  . ALA A  1 137 ? -18.62700 -6.45000  -3.24200  1.000 27.72729  ? 188 ALA B CB  1 
ATOM   1104 N N   . ALA A  1 138 ? -18.50500 -3.94800  -0.97500  1.000 32.08936  ? 189 ALA B N   1 
ATOM   1105 C CA  . ALA A  1 138 ? -18.30300 -3.61000  0.42900   1.000 30.54133  ? 189 ALA B CA  1 
ATOM   1106 C C   . ALA A  1 138 ? -19.55500 -2.99600  1.04700   1.000 36.21536  ? 189 ALA B C   1 
ATOM   1107 O O   . ALA A  1 138 ? -19.88600 -3.30600  2.20200   1.000 26.79517  ? 189 ALA B O   1 
ATOM   1108 C CB  . ALA A  1 138 ? -17.11100 -2.66600  0.57400   1.000 37.24617  ? 189 ALA B CB  1 
ATOM   1109 N N   . GLU A  1 139 ? -20.26300 -2.15700  0.29900   1.000 32.38084  ? 190 GLU B N   1 
ATOM   1110 C CA  . GLU A  1 139 ? -21.53600 -1.58300  0.80900   1.000 30.74322  ? 190 GLU B CA  1 
ATOM   1111 C C   . GLU A  1 139 ? -22.60200 -2.69500  0.92300   1.000 24.25454  ? 190 GLU B C   1 
ATOM   1112 O O   . GLU A  1 139 ? -23.35300 -2.68100  1.88400   1.000 28.43934  ? 190 GLU B O   1 
ATOM   1113 C CB  . GLU A  1 139 ? -21.96900 -0.41200  -0.06700  1.000 26.16818  ? 190 GLU B CB  1 
ATOM   1114 C CG  . GLU A  1 139 ? -23.18700 0.31100   0.46800   1.000 27.89904  ? 190 GLU B CG  1 
ATOM   1115 C CD  . GLU A  1 139 ? -23.57200 1.55900   -0.30400  1.000 28.73209  ? 190 GLU B CD  1 
ATOM   1116 O OE1 . GLU A  1 139 ? -22.69200 2.39500   -0.54000  1.000 29.93408  ? 190 GLU B OE1 1 
ATOM   1117 O OE2 . GLU A  1 139 ? -24.74800 1.68200   -0.66300  1.000 27.57601  ? 190 GLU B OE2 1 
ATOM   1118 N N   . GLN A  1 140 ? -22.62600 -3.61900  -0.03000  1.000 28.94972  ? 191 GLN B N   1 
ATOM   1119 C CA  . GLN A  1 140 ? -23.59600 -4.74400  -0.02400  1.000 29.90226  ? 191 GLN B CA  1 
ATOM   1120 C C   . GLN A  1 140 ? -23.42700 -5.53500  1.26800   1.000 30.92235  ? 191 GLN B C   1 
ATOM   1121 O O   . GLN A  1 140 ? -24.43500 -5.79100  1.93800   1.000 22.49998  ? 191 GLN B O   1 
ATOM   1122 C CB  . GLN A  1 140 ? -23.39300 -5.63800  -1.24300  1.000 21.11776  ? 191 GLN B CB  1 
ATOM   1123 C CG  . GLN A  1 140 ? -24.26900 -6.87700  -1.25700  1.000 25.70505  ? 191 GLN B CG  1 
ATOM   1124 C CD  . GLN A  1 140 ? -25.73200 -6.57800  -1.47500  1.000 27.22199  ? 191 GLN B CD  1 
ATOM   1125 O OE1 . GLN A  1 140 ? -26.10500 -5.54700  -2.02800  1.000 20.65699  ? 191 GLN B OE1 1 
ATOM   1126 N NE2 . GLN A  1 140 ? -26.57500 -7.49600  -1.04100  1.000 21.49289  ? 191 GLN B NE2 1 
ATOM   1127 N N   . THR A  1 141 ? -22.19300 -5.93000  1.56500   1.000 25.15520  ? 192 THR B N   1 
ATOM   1128 C CA  A THR A  1 141 ? -21.92100 -6.66700  2.82800   0.608 27.26395  ? 192 THR B CA  1 
ATOM   1129 C CA  B THR A  1 141 ? -21.93000 -6.67600  2.82600   0.392 27.28441  ? 192 THR B CA  1 
ATOM   1130 C C   . THR A  1 141 ? -22.19900 -5.81700  4.08400   1.000 23.57675  ? 192 THR B C   1 
ATOM   1131 O O   . THR A  1 141 ? -22.77800 -6.17100  5.19900   1.000 32.18376  ? 192 THR B O   1 
ATOM   1132 C CB  A THR A  1 141 ? -20.47300 -7.17300  2.88400   0.608 31.50124  ? 192 THR B CB  1 
ATOM   1133 C CB  B THR A  1 141 ? -20.51700 -7.28000  2.83100   0.392 31.42847  ? 192 THR B CB  1 
ATOM   1134 O OG1 A THR A  1 141 ? -19.61000 -6.03700  2.84800   0.608 42.28710  ? 192 THR B OG1 1 
ATOM   1135 O OG1 B THR A  1 141 ? -20.34000 -7.95900  4.07400   0.392 30.23344  ? 192 THR B OG1 1 
ATOM   1136 C CG2 A THR A  1 141 ? -20.13200 -8.11800  1.75500   0.608 21.46449  ? 192 THR B CG2 1 
ATOM   1137 C CG2 B THR A  1 141 ? -19.42200 -6.25300  2.66000   0.392 40.34416  ? 192 THR B CG2 1 
ATOM   1138 N N   . LYS A  1 142 ? -21.90900 -4.53000  3.91700   1.000 27.99783  ? 193 LYS B N   1 
ATOM   1139 C CA  . LYS A  1 142 ? -22.06100 -3.66700  5.09100   1.000 28.50754  ? 193 LYS B CA  1 
ATOM   1140 C C   . LYS A  1 142 ? -23.52100 -3.55700  5.51400   1.000 27.17871  ? 193 LYS B C   1 
ATOM   1141 O O   . LYS A  1 142 ? -23.82500 -3.47700  6.70900   1.000 24.49033  ? 193 LYS B O   1 
ATOM   1142 C CB  . LYS A  1 142 ? -21.49700 -2.26900  4.83100   1.000 25.49960  ? 193 LYS B CB  1 
ATOM   1143 C CG  . LYS A  1 142 ? -21.72300 -1.31300  5.99600   1.000 29.47356  ? 193 LYS B CG  1 
ATOM   1144 C CD  . LYS A  1 142 ? -20.74200 -0.17300  5.95300   1.000 38.06025  ? 193 LYS B CD  1 
ATOM   1145 C CE  . LYS A  1 142 ? -21.34100 1.13400   6.46400   1.000 47.95855  ? 193 LYS B CE  1 
ATOM   1146 N NZ  . LYS A  1 142 ? -22.21800 1.75600   5.43100   1.000 44.14323  ? 193 LYS B NZ  1 
ATOM   1147 N N   . LEU A  1 143 ? -24.43400 -3.53300  4.55500   1.000 21.29767  ? 194 LEU B N   1 
ATOM   1148 C CA  . LEU A  1 143 ? -25.83300 -3.27700  4.87900   1.000 24.29680  ? 194 LEU B CA  1 
ATOM   1149 C C   . LEU A  1 143 ? -26.62000 -4.55600  5.01000   1.000 21.78977  ? 194 LEU B C   1 
ATOM   1150 O O   . LEU A  1 143 ? -27.50600 -4.66000  5.86700   1.000 29.00582  ? 194 LEU B O   1 
ATOM   1151 C CB  . LEU A  1 143 ? -26.48300 -2.38200  3.81300   1.000 17.74203  ? 194 LEU B CB  1 
ATOM   1152 C CG  . LEU A  1 143 ? -25.86200 -1.00200  3.51500   1.000 19.05812  ? 194 LEU B CG  1 
ATOM   1153 C CD1 . LEU A  1 143 ? -26.61400 -0.28200  2.40000   1.000 21.19665  ? 194 LEU B CD1 1 
ATOM   1154 C CD2 . LEU A  1 143 ? -25.97300 -0.14900  4.75000   1.000 16.65853  ? 194 LEU B CD2 1 
ATOM   1155 N N   . TYR A  1 144 ? -26.28200 -5.53800  4.20200   1.000 21.11644  ? 195 TYR B N   1 
ATOM   1156 C CA  . TYR A  1 144 ? -27.11400 -6.70600  4.00600   1.000 25.50073  ? 195 TYR B CA  1 
ATOM   1157 C C   . TYR A  1 144 ? -26.40300 -8.00700  4.34500   1.000 22.39406  ? 195 TYR B C   1 
ATOM   1158 O O   . TYR A  1 144 ? -27.07000 -9.04500  4.39400   1.000 25.46316  ? 195 TYR B O   1 
ATOM   1159 C CB  . TYR A  1 144 ? -27.62200 -6.72000  2.55200   1.000 21.40664  ? 195 TYR B CB  1 
ATOM   1160 C CG  . TYR A  1 144 ? -28.21200 -5.38400  2.13200   1.000 17.81662  ? 195 TYR B CG  1 
ATOM   1161 C CD1 . TYR A  1 144 ? -29.19800 -4.73400  2.91000   1.000 18.96260  ? 195 TYR B CD1 1 
ATOM   1162 C CD2 . TYR A  1 144 ? -27.70000 -4.70800  1.03000   1.000 17.72604  ? 195 TYR B CD2 1 
ATOM   1163 C CE1 . TYR A  1 144 ? -29.70700 -3.49900  2.54100   1.000 17.69812  ? 195 TYR B CE1 1 
ATOM   1164 C CE2 . TYR A  1 144 ? -28.19500 -3.45300  0.65900   1.000 15.62259  ? 195 TYR B CE2 1 
ATOM   1165 C CZ  . TYR A  1 144 ? -29.19000 -2.87700  1.40800   1.000 14.24898  ? 195 TYR B CZ  1 
ATOM   1166 O OH  . TYR A  1 144 ? -29.68500 -1.66500  1.04900   1.000 15.76858  ? 195 TYR B OH  1 
ATOM   1167 N N   . HIS A  1 145 ? -25.07800 -7.98100  4.59100   1.000 27.87578  ? 196 HIS B N   1 
ATOM   1168 C CA  . HIS A  1 145 ? -24.34400 -9.10700  5.17900   1.000 27.04015  ? 196 HIS B CA  1 
ATOM   1169 C C   . HIS A  1 145 ? -24.33900 -10.33800 4.28500   1.000 25.77175  ? 196 HIS B C   1 
ATOM   1170 O O   . HIS A  1 145 ? -24.33500 -11.46500 4.78300   1.000 26.62010  ? 196 HIS B O   1 
ATOM   1171 C CB  . HIS A  1 145 ? -24.90800 -9.43200  6.56500   1.000 26.97536  ? 196 HIS B CB  1 
ATOM   1172 C CG  . HIS A  1 145 ? -24.79200 -8.29100  7.52100   1.000 27.20710  ? 196 HIS B CG  1 
ATOM   1173 N ND1 . HIS A  1 145 ? -23.57200 -7.80300  7.93300   1.000 32.37200  ? 196 HIS B ND1 1 
ATOM   1174 C CD2 . HIS A  1 145 ? -25.71000 -7.38200  7.93900   1.000 30.20002  ? 196 HIS B CD2 1 
ATOM   1175 C CE1 . HIS A  1 145 ? -23.75100 -6.73800  8.69400   1.000 30.03429  ? 196 HIS B CE1 1 
ATOM   1176 N NE2 . HIS A  1 145 ? -25.04300 -6.45500  8.70900   1.000 33.53018  ? 196 HIS B NE2 1 
ATOM   1177 N N   . LYS A  1 146 ? -24.35400 -10.14300 2.96800   1.000 25.05752  ? 197 LYS B N   1 
ATOM   1178 C CA  . LYS A  1 146 ? -24.31400 -11.24200 2.00000   1.000 23.84040  ? 197 LYS B CA  1 
ATOM   1179 C C   . LYS A  1 146 ? -24.04100 -10.62200 0.63500   1.000 22.76964  ? 197 LYS B C   1 
ATOM   1180 O O   . LYS A  1 146 ? -24.46800 -9.48700  0.39300   1.000 24.79608  ? 197 LYS B O   1 
ATOM   1181 C CB  . LYS A  1 146 ? -25.61200 -12.07300 1.96700   1.000 26.82171  ? 197 LYS B CB  1 
ATOM   1182 C CG  . LYS A  1 146 ? -26.89800 -11.26400 1.72600   1.000 24.52754  ? 197 LYS B CG  1 
ATOM   1183 C CD  . LYS A  1 146 ? -28.21400 -12.02500 2.06400   1.000 24.13218  ? 197 LYS B CD  1 
ATOM   1184 C CE  . LYS A  1 146 ? -28.32500 -12.33900 3.55900   1.000 21.34686  ? 197 LYS B CE  1 
ATOM   1185 N NZ  . LYS A  1 146 ? -29.06300 -11.24300 4.24700   1.000 20.26436  ? 197 LYS B NZ  1 
ATOM   1186 N N   . PRO A  1 147 ? -23.31200 -11.33800 -0.29500  1.000 26.77454  ? 198 PRO B N   1 
ATOM   1187 C CA  . PRO A  1 147 ? -22.86600 -10.71600 -1.54600  1.000 28.67040  ? 198 PRO B CA  1 
ATOM   1188 C C   . PRO A  1 147 ? -23.99700 -10.54600 -2.56000  1.000 25.71868  ? 198 PRO B C   1 
ATOM   1189 O O   . PRO A  1 147 ? -23.95500 -9.66100  -3.42400  1.000 26.35839  ? 198 PRO B O   1 
ATOM   1190 C CB  . PRO A  1 147 ? -21.80300 -11.71000 -2.05400  1.000 28.13623  ? 198 PRO B CB  1 
ATOM   1191 C CG  . PRO A  1 147 ? -22.27000 -13.01000 -1.53200  1.000 25.70023  ? 198 PRO B CG  1 
ATOM   1192 C CD  . PRO A  1 147 ? -22.80600 -12.72100 -0.16900  1.000 29.11166  ? 198 PRO B CD  1 
ATOM   1193 N N   . THR A  1 148 ? -24.97600 -11.43500 -2.48500  1.000 23.51294  ? 199 THR B N   1 
ATOM   1194 C CA  . THR A  1 148 ? -26.12800 -11.35700 -3.40200  1.000 21.27670  ? 199 THR B CA  1 
ATOM   1195 C C   . THR A  1 148 ? -27.41700 -11.45200 -2.58700  1.000 29.06758  ? 199 THR B C   1 
ATOM   1196 O O   . THR A  1 148 ? -27.37800 -11.90500 -1.43700  1.000 27.77202  ? 199 THR B O   1 
ATOM   1197 C CB  . THR A  1 148 ? -26.10300 -12.45500 -4.46600  1.000 25.43041  ? 199 THR B CB  1 
ATOM   1198 O OG1 . THR A  1 148 ? -27.17000 -12.20200 -5.37800  1.000 41.27903  ? 199 THR B OG1 1 
ATOM   1199 C CG2 . THR A  1 148 ? -26.24600 -13.84100 -3.88200  1.000 34.37103  ? 199 THR B CG2 1 
ATOM   1200 N N   . ALA A  1 149 ? -28.51000 -11.03900 -3.19900  1.000 26.14034  ? 200 ALA B N   1 
ATOM   1201 C CA  . ALA A  1 149 ? -29.77600 -11.04900 -2.46300  1.000 24.09515  ? 200 ALA B CA  1 
ATOM   1202 C C   . ALA A  1 149 ? -30.94100 -11.16900 -3.43100  1.000 25.37460  ? 200 ALA B C   1 
ATOM   1203 O O   . ALA A  1 149 ? -30.73800 -11.07800 -4.63300  1.000 23.14671  ? 200 ALA B O   1 
ATOM   1204 C CB  . ALA A  1 149 ? -29.87100 -9.81000  -1.61900  1.000 21.90470  ? 200 ALA B CB  1 
ATOM   1205 N N   . TYR A  1 150 ? -32.10800 -11.41400 -2.86900  1.000 22.03076  ? 201 TYR B N   1 
ATOM   1206 C CA  . TYR A  1 150 ? -33.31800 -11.48800 -3.69500  1.000 22.21476  ? 201 TYR B CA  1 
ATOM   1207 C C   . TYR A  1 150 ? -34.43200 -10.63800 -3.09900  1.000 21.42566  ? 201 TYR B C   1 
ATOM   1208 O O   . TYR A  1 150 ? -34.50700 -10.50800 -1.87400  1.000 17.41024  ? 201 TYR B O   1 
ATOM   1209 C CB  . TYR A  1 150 ? -33.82700 -12.92800 -3.78000  1.000 25.85447  ? 201 TYR B CB  1 
ATOM   1210 C CG  . TYR A  1 150 ? -34.43000 -13.46600 -2.50700  1.000 31.60899  ? 201 TYR B CG  1 
ATOM   1211 C CD1 . TYR A  1 150 ? -35.76200 -13.25900 -2.19000  1.000 28.53938  ? 201 TYR B CD1 1 
ATOM   1212 C CD2 . TYR A  1 150 ? -33.65900 -14.18800 -1.61600  1.000 35.43235  ? 201 TYR B CD2 1 
ATOM   1213 C CE1 . TYR A  1 150 ? -36.31000 -13.74700 -1.01600  1.000 25.18487  ? 201 TYR B CE1 1 
ATOM   1214 C CE2 . TYR A  1 150 ? -34.19000 -14.68700 -0.44100  1.000 29.32354  ? 201 TYR B CE2 1 
ATOM   1215 C CZ  . TYR A  1 150 ? -35.51900 -14.46700 -0.14000  1.000 33.60905  ? 201 TYR B CZ  1 
ATOM   1216 O OH  . TYR A  1 150 ? -36.02400 -14.96700 1.02200   1.000 40.37735  ? 201 TYR B OH  1 
ATOM   1217 N N   . VAL A  1 151 ? -35.21200 -10.03000 -3.97000  1.000 16.60597  ? 202 VAL B N   1 
ATOM   1218 C CA  . VAL A  1 151 ? -36.44900 -9.38900  -3.54600  1.000 15.33628  ? 202 VAL B CA  1 
ATOM   1219 C C   . VAL A  1 151 ? -37.54300 -9.93500  -4.43800  1.000 17.19533  ? 202 VAL B C   1 
ATOM   1220 O O   . VAL A  1 151 ? -37.37100 -10.01400 -5.65800  1.000 18.14974  ? 202 VAL B O   1 
ATOM   1221 C CB  . VAL A  1 151 ? -36.38000 -7.85200  -3.62600  1.000 16.69384  ? 202 VAL B CB  1 
ATOM   1222 C CG1 . VAL A  1 151 ? -37.73500 -7.24700  -3.28600  1.000 22.50288  ? 202 VAL B CG1 1 
ATOM   1223 C CG2 . VAL A  1 151 ? -35.34200 -7.31900  -2.64400  1.000 14.96625  ? 202 VAL B CG2 1 
ATOM   1224 N N   . SER A  1 152 ? -38.64100 -10.34300 -3.83200  1.000 14.83434  ? 203 SER B N   1 
ATOM   1225 C CA  A SER A  1 152 ? -39.80600 -10.81200 -4.56100  0.502 13.77578  ? 203 SER B CA  1 
ATOM   1226 C CA  B SER A  1 152 ? -39.80600 -10.79500 -4.58300  0.498 13.68187  ? 203 SER B CA  1 
ATOM   1227 C C   . SER A  1 152 ? -41.10800 -10.10100 -4.11200  1.000 17.08529  ? 203 SER B C   1 
ATOM   1228 O O   . SER A  1 152 ? -41.43800 -9.91100  -2.92500  1.000 17.85466  ? 203 SER B O   1 
ATOM   1229 C CB  A SER A  1 152 ? -40.01200 -12.31200 -4.37300  0.502 18.99451  ? 203 SER B CB  1 
ATOM   1230 C CB  B SER A  1 152 ? -40.01700 -12.30800 -4.50100  0.498 18.98190  ? 203 SER B CB  1 
ATOM   1231 O OG  A SER A  1 152 ? -41.28100 -12.72200 -4.82600  0.502 19.39940  ? 203 SER B OG  1 
ATOM   1232 O OG  B SER A  1 152 ? -40.89500 -12.66000 -3.45900  0.498 17.65469  ? 203 SER B OG  1 
ATOM   1233 N N   . VAL A  1 153 ? -41.89700 -9.76100  -5.09300  1.000 14.20042  ? 204 VAL B N   1 
ATOM   1234 C CA  . VAL A  1 153 ? -43.17400 -9.13300  -4.80500  1.000 13.17269  ? 204 VAL B CA  1 
ATOM   1235 C C   . VAL A  1 153 ? -44.23700 -9.80000  -5.65900  1.000 18.64817  ? 204 VAL B C   1 
ATOM   1236 O O   . VAL A  1 153 ? -44.10500 -9.85000  -6.88600  1.000 16.20152  ? 204 VAL B O   1 
ATOM   1237 C CB  . VAL A  1 153 ? -43.16200 -7.62900  -5.10100  1.000 15.24679  ? 204 VAL B CB  1 
ATOM   1238 C CG1 . VAL A  1 153 ? -44.59100 -7.01600  -4.87500  1.000 13.38772  ? 204 VAL B CG1 1 
ATOM   1239 C CG2 . VAL A  1 153 ? -42.11800 -6.94700  -4.30800  1.000 12.55968  ? 204 VAL B CG2 1 
ATOM   1240 N N   . VAL A  1 154 ? -45.30800 -10.24900 -5.00900  1.000 15.74338  ? 205 VAL B N   1 
ATOM   1241 C CA  . VAL A  1 154 ? -46.37800 -10.96300 -5.68800  1.000 18.11625  ? 205 VAL B CA  1 
ATOM   1242 C C   . VAL A  1 154 ? -47.81400 -10.68500 -5.23500  1.000 17.89228  ? 205 VAL B C   1 
ATOM   1243 O O   . VAL A  1 154 ? -48.08400 -10.68100 -4.04600  1.000 17.11157  ? 205 VAL B O   1 
ATOM   1244 C CB  . VAL A  1 154 ? -46.15700 -12.49600 -5.57700  1.000 18.79833  ? 205 VAL B CB  1 
ATOM   1245 C CG1 . VAL A  1 154 ? -47.27200 -13.25500 -6.27200  1.000 26.17454  ? 205 VAL B CG1 1 
ATOM   1246 C CG2 . VAL A  1 154 ? -44.79600 -12.89600 -6.11200  1.000 25.97001  ? 205 VAL B CG2 1 
ATOM   1247 N N   . SER A  1 155 ? -48.69000 -10.46100 -6.18000  1.000 15.30087  ? 206 SER B N   1 
ATOM   1248 C CA  . SER A  1 155 ? -50.09500 -10.27900 -5.93300  1.000 15.56701  ? 206 SER B CA  1 
ATOM   1249 C C   . SER A  1 155 ? -50.81200 -11.18100 -6.94900  1.000 22.42463  ? 206 SER B C   1 
ATOM   1250 O O   . SER A  1 155 ? -50.18800 -11.95500 -7.61800  1.000 18.61134  ? 206 SER B O   1 
ATOM   1251 C CB  . SER A  1 155 ? -50.49700 -8.84600  -6.18500  1.000 12.43988  ? 206 SER B CB  1 
ATOM   1252 O OG  . SER A  1 155 ? -50.82800 -8.60600  -7.52700  1.000 21.10646  ? 206 SER B OG  1 
ATOM   1253 N N   . SER A  1 156 ? -52.11500 -11.05100 -7.06600  1.000 19.66686  ? 207 SER B N   1 
ATOM   1254 C CA  . SER A  1 156 ? -52.84600 -11.78800 -8.10400  1.000 24.28629  ? 207 SER B CA  1 
ATOM   1255 C C   . SER A  1 156 ? -52.74200 -11.07000 -9.47900  1.000 22.70503  ? 207 SER B C   1 
ATOM   1256 O O   . SER A  1 156 ? -53.14400 -11.62400 -10.47300 1.000 27.11647  ? 207 SER B O   1 
ATOM   1257 C CB  . SER A  1 156 ? -54.30500 -12.03300 -7.65900  1.000 16.99453  ? 207 SER B CB  1 
ATOM   1258 O OG  . SER A  1 156 ? -54.39400 -12.74000 -6.45000  1.000 22.18013  ? 207 SER B OG  1 
ATOM   1259 N N   . HIS A  1 157 ? -52.20800 -9.85800  -9.51700  1.000 20.57747  ? 208 HIS B N   1 
ATOM   1260 C CA  . HIS A  1 157 ? -52.10000 -9.09700  -10.74400 1.000 18.52985  ? 208 HIS B CA  1 
ATOM   1261 C C   . HIS A  1 157 ? -50.69800 -8.50200  -10.92600 1.000 19.62346  ? 208 HIS B C   1 
ATOM   1262 O O   . HIS A  1 157 ? -50.45500 -7.77300  -11.86200 1.000 17.65418  ? 208 HIS B O   1 
ATOM   1263 C CB  . HIS A  1 157 ? -53.17200 -8.03600  -10.71000 1.000 19.17405  ? 208 HIS B CB  1 
ATOM   1264 C CG  . HIS A  1 157 ? -54.55900 -8.57600  -10.84100 1.000 29.50998  ? 208 HIS B CG  1 
ATOM   1265 N ND1 . HIS A  1 157 ? -55.11500 -8.90800  -12.05500 1.000 20.52557  ? 208 HIS B ND1 1 
ATOM   1266 C CD2 . HIS A  1 157 ? -55.50400 -8.84000  -9.91000  1.000 18.33910  ? 208 HIS B CD2 1 
ATOM   1267 C CE1 . HIS A  1 157 ? -56.33900 -9.35800  -11.86800 1.000 17.72645  ? 208 HIS B CE1 1 
ATOM   1268 N NE2 . HIS A  1 157 ? -56.60100 -9.32600  -10.57500 1.000 34.60310  ? 208 HIS B NE2 1 
ATOM   1269 N N   . TYR A  1 158 ? -49.79400 -8.83400  -10.01800 1.000 15.14187  ? 209 TYR B N   1 
ATOM   1270 C CA  . TYR A  1 158 ? -48.42600 -8.35800  -10.07800 1.000 12.87898  ? 209 TYR B CA  1 
ATOM   1271 C C   . TYR A  1 158 ? -47.52700 -9.49100  -9.63300  1.000 15.82313  ? 209 TYR B C   1 
ATOM   1272 O O   . TYR A  1 158 ? -47.76400 -10.07700 -8.57100  1.000 18.70829  ? 209 TYR B O   1 
ATOM   1273 C CB  . TYR A  1 158 ? -48.20700 -7.14800  -9.15600  1.000 15.75640  ? 209 TYR B CB  1 
ATOM   1274 C CG  . TYR A  1 158 ? -46.84900 -6.53800  -9.34800  1.000 14.50485  ? 209 TYR B CG  1 
ATOM   1275 C CD1 . TYR A  1 158 ? -45.71700 -7.06700  -8.69700  1.000 14.60313  ? 209 TYR B CD1 1 
ATOM   1276 C CD2 . TYR A  1 158 ? -46.67900 -5.46300  -10.19700 1.000 12.67144  ? 209 TYR B CD2 1 
ATOM   1277 C CE1 . TYR A  1 158 ? -44.47800 -6.51800  -8.88800  1.000 15.65924  ? 209 TYR B CE1 1 
ATOM   1278 C CE2 . TYR A  1 158 ? -45.40200 -4.89300  -10.39800 1.000 14.46691  ? 209 TYR B CE2 1 
ATOM   1279 C CZ  . TYR A  1 158 ? -44.33200 -5.43600  -9.73300  1.000 15.01963  ? 209 TYR B CZ  1 
ATOM   1280 O OH  . TYR A  1 158 ? -43.11600 -4.90900  -9.91700  1.000 16.70742  ? 209 TYR B OH  1 
ATOM   1281 N N   . SER A  1 159 ? -46.45300 -9.73700  -10.37900 1.000 15.52973  ? 210 SER B N   1 
ATOM   1282 C CA  . SER A  1 159 ? -45.47500 -10.72600 -9.92600  1.000 17.74000  ? 210 SER B CA  1 
ATOM   1283 C C   . SER A  1 159 ? -44.10200 -10.39900 -10.50700 1.000 20.51225  ? 210 SER B C   1 
ATOM   1284 O O   . SER A  1 159 ? -43.93900 -10.38500 -11.73400 1.000 17.59424  ? 210 SER B O   1 
ATOM   1285 C CB  . SER A  1 159 ? -45.91600 -12.12900 -10.35000 1.000 22.51770  ? 210 SER B CB  1 
ATOM   1286 O OG  . SER A  1 159 ? -44.79700 -12.96200 -10.41800 1.000 39.99469  ? 210 SER B OG  1 
ATOM   1287 N N   . ARG A  1 160 ? -43.10700 -10.14100 -9.65500  1.000 16.58904  ? 211 ARG B N   1 
ATOM   1288 C CA  . ARG A  1 160 ? -41.77700 -9.81800  -10.17500 1.000 15.39479  ? 211 ARG B CA  1 
ATOM   1289 C C   . ARG A  1 160 ? -40.70400 -10.17700 -9.16200  1.000 15.91730  ? 211 ARG B C   1 
ATOM   1290 O O   . ARG A  1 160 ? -40.90700 -10.04500 -7.95000  1.000 16.23602  ? 211 ARG B O   1 
ATOM   1291 C CB  . ARG A  1 160 ? -41.70100 -8.33200  -10.53600 1.000 19.00307  ? 211 ARG B CB  1 
ATOM   1292 C CG  . ARG A  1 160 ? -40.39500 -7.86800  -11.24900 1.000 24.08596  ? 211 ARG B CG  1 
ATOM   1293 C CD  . ARG A  1 160 ? -40.69300 -6.52100  -11.91500 1.000 26.56203  ? 211 ARG B CD  1 
ATOM   1294 N NE  . ARG A  1 160 ? -39.74800 -6.17500  -12.96000 1.000 32.92379  ? 211 ARG B NE  1 
ATOM   1295 C CZ  . ARG A  1 160 ? -39.80100 -5.05200  -13.67300 1.000 46.29291  ? 211 ARG B CZ  1 
ATOM   1296 N NH1 . ARG A  1 160 ? -40.74300 -4.12600  -13.46100 1.000 37.94574  ? 211 ARG B NH1 1 
ATOM   1297 N NH2 . ARG A  1 160 ? -38.89700 -4.84600  -14.63500 1.000 50.52127  ? 211 ARG B NH2 1 
ATOM   1298 N N   . LYS A  1 161 ? -39.56900 -10.62400 -9.68000  1.000 17.00520  ? 212 LYS B N   1 
ATOM   1299 C CA  . LYS A  1 161 ? -38.43400 -10.94600 -8.84400  1.000 19.37643  ? 212 LYS B CA  1 
ATOM   1300 C C   . LYS A  1 161 ? -37.27900 -10.00600 -9.15900  1.000 20.91206  ? 212 LYS B C   1 
ATOM   1301 O O   . LYS A  1 161 ? -37.03400 -9.70200  -10.30100 1.000 22.73215  ? 212 LYS B O   1 
ATOM   1302 C CB  . LYS A  1 161 ? -38.02600 -12.39300 -9.00000  1.000 26.00858  ? 212 LYS B CB  1 
ATOM   1303 C CG  . LYS A  1 161 ? -37.12800 -12.91100 -7.89600  1.000 38.64877  ? 212 LYS B CG  1 
ATOM   1304 C CD  . LYS A  1 161 ? -36.68800 -14.33900 -8.16400  1.000 53.68518  ? 212 LYS B CD  1 
ATOM   1305 C CE  . LYS A  1 161 ? -35.18000 -14.48800 -8.05200  1.000 59.58420  ? 212 LYS B CE  1 
ATOM   1306 N NZ  . LYS A  1 161 ? -34.76200 -15.91600 -8.11800  1.000 65.68864  ? 212 LYS B NZ  1 
ATOM   1307 N N   . PHE A  1 162 ? -36.57400 -9.57200  -8.12900  1.000 19.06662  ? 213 PHE B N   1 
ATOM   1308 C CA  . PHE A  1 162 ? -35.52200 -8.56200  -8.33200  1.000 22.56803  ? 213 PHE B CA  1 
ATOM   1309 C C   . PHE A  1 162 ? -34.19400 -9.07200  -7.78300  1.000 28.85904  ? 213 PHE B C   1 
ATOM   1310 O O   . PHE A  1 162 ? -34.17700 -9.73600  -6.74200  1.000 20.18289  ? 213 PHE B O   1 
ATOM   1311 C CB  . PHE A  1 162 ? -35.90900 -7.22800  -7.69200  1.000 17.12731  ? 213 PHE B CB  1 
ATOM   1312 C CG  . PHE A  1 162 ? -37.31300 -6.75000  -7.95300  1.000 16.29296  ? 213 PHE B CG  1 
ATOM   1313 C CD1 . PHE A  1 162 ? -38.36600 -7.18000  -7.16500  1.000 15.19459  ? 213 PHE B CD1 1 
ATOM   1314 C CD2 . PHE A  1 162 ? -37.57800 -5.85000  -8.96900  1.000 15.64044  ? 213 PHE B CD2 1 
ATOM   1315 C CE1 . PHE A  1 162 ? -39.65500 -6.73100  -7.39600  1.000 13.49641  ? 213 PHE B CE1 1 
ATOM   1316 C CE2 . PHE A  1 162 ? -38.86800 -5.39900  -9.19500  1.000 20.62125  ? 213 PHE B CE2 1 
ATOM   1317 C CZ  . PHE A  1 162 ? -39.90400 -5.84100  -8.40900  1.000 14.99388  ? 213 PHE B CZ  1 
ATOM   1318 N N   . THR A  1 163 ? -33.12300 -8.70400  -8.47400  1.000 27.74930  ? 214 THR B N   1 
ATOM   1319 C CA  . THR A  1 163 ? -31.77700 -9.05200  -8.06700  1.000 27.41623  ? 214 THR B CA  1 
ATOM   1320 C C   . THR A  1 163 ? -30.93200 -7.78900  -8.07500  1.000 20.89698  ? 214 THR B C   1 
ATOM   1321 O O   . THR A  1 163 ? -30.85600 -7.12300  -9.07600  1.000 23.54993  ? 214 THR B O   1 
ATOM   1322 C CB  . THR A  1 163 ? -31.17000 -10.10700 -9.03100  1.000 35.03160  ? 214 THR B CB  1 
ATOM   1323 O OG1 . THR A  1 163 ? -32.06900 -11.21100 -9.17100  1.000 32.37688  ? 214 THR B OG1 1 
ATOM   1324 C CG2 . THR A  1 163 ? -29.84000 -10.59400 -8.50600  1.000 35.84540  ? 214 THR B CG2 1 
ATOM   1325 N N   . PRO A  1 164 ? -30.32800 -7.44000  -6.93800  1.000 27.42857  ? 215 PRO B N   1 
ATOM   1326 C CA  . PRO A  1 164 ? -29.41500 -6.30400  -6.93700  1.000 24.06440  ? 215 PRO B CA  1 
ATOM   1327 C C   . PRO A  1 164 ? -28.27200 -6.47600  -7.94500  1.000 22.88562  ? 215 PRO B C   1 
ATOM   1328 O O   . PRO A  1 164 ? -27.69500 -7.52900  -7.99700  1.000 24.12024  ? 215 PRO B O   1 
ATOM   1329 C CB  . PRO A  1 164 ? -28.78900 -6.32300  -5.55200  1.000 21.09683  ? 215 PRO B CB  1 
ATOM   1330 C CG  . PRO A  1 164 ? -29.19800 -7.65500  -4.95300  1.000 37.09429  ? 215 PRO B CG  1 
ATOM   1331 C CD  . PRO A  1 164 ? -30.50500 -8.01900  -5.61900  1.000 25.52441  ? 215 PRO B CD  1 
ATOM   1332 N N   . ARG A  1 165 ? -28.02100 -5.44200  -8.72900  1.000 25.69592  ? 216 ARG B N   1 
ATOM   1333 C CA  . ARG A  1 165 ? -26.89300 -5.45000  -9.69200  1.000 24.21400  ? 216 ARG B CA  1 
ATOM   1334 C C   . ARG A  1 165 ? -25.83400 -4.51100  -9.11400  1.000 23.52934  ? 216 ARG B C   1 
ATOM   1335 O O   . ARG A  1 165 ? -26.01900 -3.29600  -9.17600  1.000 19.69801  ? 216 ARG B O   1 
ATOM   1336 C CB  . ARG A  1 165 ? -27.39800 -5.02700  -11.06600 1.000 27.18639  ? 216 ARG B CB  1 
ATOM   1337 C CG  . ARG A  1 165 ? -28.45900 -5.95300  -11.63800 1.000 33.26905  ? 216 ARG B CG  1 
ATOM   1338 C CD  . ARG A  1 165 ? -29.11700 -5.31100  -12.83900 1.000 50.97740  ? 216 ARG B CD  1 
ATOM   1339 N NE  . ARG A  1 165 ? -28.51400 -5.70900  -14.09900 1.000 62.49818  ? 216 ARG B NE  1 
ATOM   1340 C CZ  . ARG A  1 165 ? -28.62800 -5.03200  -15.23600 1.000 55.85871  ? 216 ARG B CZ  1 
ATOM   1341 N NH1 . ARG A  1 165 ? -29.32100 -3.90800  -15.27800 1.000 52.56807  ? 216 ARG B NH1 1 
ATOM   1342 N NH2 . ARG A  1 165 ? -28.04800 -5.48200  -16.32900 1.000 51.85332  ? 216 ARG B NH2 1 
ATOM   1343 N N   . ILE A  1 166 ? -24.80700 -5.08300  -8.51200  1.000 21.02044  ? 217 ILE B N   1 
ATOM   1344 C CA  . ILE A  1 166 ? -23.79400 -4.24200  -7.82400  1.000 22.78155  ? 217 ILE B CA  1 
ATOM   1345 C C   . ILE A  1 166 ? -22.80400 -3.71200  -8.86800  1.000 28.22278  ? 217 ILE B C   1 
ATOM   1346 O O   . ILE A  1 166 ? -22.17100 -4.50700  -9.55300  1.000 24.22379  ? 217 ILE B O   1 
ATOM   1347 C CB  . ILE A  1 166 ? -23.11400 -4.97700  -6.65800  1.000 30.08897  ? 217 ILE B CB  1 
ATOM   1348 C CG1 . ILE A  1 166 ? -24.02600 -5.07500  -5.43200  1.000 30.89310  ? 217 ILE B CG1 1 
ATOM   1349 C CG2 . ILE A  1 166 ? -21.78400 -4.32900  -6.31200  1.000 23.40333  ? 217 ILE B CG2 1 
ATOM   1350 C CD1 . ILE A  1 166 ? -25.23200 -5.95600  -5.63000  1.000 30.69205  ? 217 ILE B CD1 1 
ATOM   1351 N N   . ALA A  1 167 ? -22.76700 -2.39200  -8.98600  1.000 27.72583  ? 218 ALA B N   1 
ATOM   1352 C CA  . ALA A  1 167 ? -21.84600 -1.74000  -9.93300  1.000 24.55763  ? 218 ALA B CA  1 
ATOM   1353 C C   . ALA A  1 167 ? -21.80600 -0.24500  -9.64500  1.000 25.74418  ? 218 ALA B C   1 
ATOM   1354 O O   . ALA A  1 167 ? -22.80100 0.30200   -9.16600  1.000 24.04882  ? 218 ALA B O   1 
ATOM   1355 C CB  . ALA A  1 167 ? -22.24400 -2.02400  -11.34900 1.000 21.83387  ? 218 ALA B CB  1 
ATOM   1356 N N   . THR A  1 168 ? -20.65000 0.34800   -9.87600  1.000 24.97573  ? 219 THR B N   1 
ATOM   1357 C CA  . THR A  1 168 ? -20.46400 1.78700   -9.67700  1.000 24.40677  ? 219 THR B CA  1 
ATOM   1358 C C   . THR A  1 168 ? -21.08900 2.54100   -10.85900 1.000 21.25871  ? 219 THR B C   1 
ATOM   1359 O O   . THR A  1 168 ? -20.67900 2.35700   -12.01700 1.000 26.08016  ? 219 THR B O   1 
ATOM   1360 C CB  . THR A  1 168 ? -18.97600 2.09800   -9.54400  1.000 24.43519  ? 219 THR B CB  1 
ATOM   1361 O OG1 . THR A  1 168 ? -18.43500 1.34700   -8.44500  1.000 36.64360  ? 219 THR B OG1 1 
ATOM   1362 C CG2 . THR A  1 168 ? -18.79100 3.55700   -9.24700  1.000 27.47157  ? 219 THR B CG2 1 
ATOM   1363 N N   . ARG A  1 169 ? -22.11900 3.35000   -10.58500 1.000 16.76455  ? 220 ARG B N   1 
ATOM   1364 C CA  . ARG A  1 169 ? -22.69000 4.27200   -11.56300 1.000 21.82982  ? 220 ARG B CA  1 
ATOM   1365 C C   . ARG A  1 169 ? -22.02000 5.64200   -11.39300 1.000 20.09062  ? 220 ARG B C   1 
ATOM   1366 O O   . ARG A  1 169 ? -21.37400 5.91800   -10.37900 1.000 23.10304  ? 220 ARG B O   1 
ATOM   1367 C CB  . ARG A  1 169 ? -24.20900 4.37200   -11.38100 1.000 22.06892  ? 220 ARG B CB  1 
ATOM   1368 C CG  . ARG A  1 169 ? -24.91300 3.10000   -11.83500 1.000 25.06319  ? 220 ARG B CG  1 
ATOM   1369 C CD  . ARG A  1 169 ? -25.17900 2.20100   -10.63000 1.000 19.75884  ? 220 ARG B CD  1 
ATOM   1370 N NE  . ARG A  1 169 ? -26.26000 1.25600   -10.88300 1.000 24.87869  ? 220 ARG B NE  1 
ATOM   1371 C CZ  . ARG A  1 169 ? -26.35200 0.04800   -10.33800 1.000 24.71608  ? 220 ARG B CZ  1 
ATOM   1372 N NH1 . ARG A  1 169 ? -25.43600 -0.40100  -9.49000  1.000 20.03623  ? 220 ARG B NH1 1 
ATOM   1373 N NH2 . ARG A  1 169 ? -27.41400 -0.70900  -10.63100 1.000 19.60476  ? 220 ARG B NH2 1 
ATOM   1374 N N   . SER A  1 170 ? -22.14200 6.47200   -12.42200 1.000 17.26637  ? 221 SER B N   1 
ATOM   1375 C CA  . SER A  1 170 ? -21.80800 7.87800   -12.25500 1.000 21.21681  ? 221 SER B CA  1 
ATOM   1376 C C   . SER A  1 170 ? -22.61400 8.43800   -11.09700 1.000 24.93093  ? 221 SER B C   1 
ATOM   1377 O O   . SER A  1 170 ? -23.74800 8.01800   -10.84200 1.000 21.60941  ? 221 SER B O   1 
ATOM   1378 C CB  . SER A  1 170 ? -22.12400 8.67000   -13.52300 1.000 21.57960  ? 221 SER B CB  1 
ATOM   1379 O OG  . SER A  1 170 ? -21.35700 8.20300   -14.59100 1.000 24.11446  ? 221 SER B OG  1 
ATOM   1380 N N   . LYS A  1 171 ? -22.01000 9.38600   -10.37900 1.000 20.57202  ? 222 LYS B N   1 
ATOM   1381 C CA  . LYS A  1 171 ? -22.71500 9.98300   -9.25700  1.000 20.29490  ? 222 LYS B CA  1 
ATOM   1382 C C   . LYS A  1 171 ? -23.90600 10.80300  -9.72800  1.000 20.49351  ? 222 LYS B C   1 
ATOM   1383 O O   . LYS A  1 171 ? -23.84800 11.51600  -10.73800 1.000 19.72169  ? 222 LYS B O   1 
ATOM   1384 C CB  . LYS A  1 171 ? -21.76700 10.84000  -8.42500  1.000 21.54827  ? 222 LYS B CB  1 
ATOM   1385 C CG  . LYS A  1 171 ? -21.28300 10.02200  -7.23300  1.000 28.75229  ? 222 LYS B CG  1 
ATOM   1386 C CD  . LYS A  1 171 ? -20.10100 10.53200  -6.45600  1.000 22.39077  ? 222 LYS B CD  1 
ATOM   1387 C CE  . LYS A  1 171 ? -19.56600 9.32800   -5.70300  1.000 26.47804  ? 222 LYS B CE  1 
ATOM   1388 N NZ  . LYS A  1 171 ? -18.89700 9.73600   -4.51400  1.000 40.35030  ? 222 LYS B NZ  1 
ATOM   1389 N N   . VAL A  1 172 ? -24.99100 10.65900  -8.97800  1.000 17.61310  ? 223 VAL B N   1 
ATOM   1390 C CA  . VAL A  1 172 ? -26.16200 11.55800  -9.13400  1.000 18.51828  ? 223 VAL B CA  1 
ATOM   1391 C C   . VAL A  1 172 ? -26.49000 11.96900  -7.69400  1.000 19.03112  ? 223 VAL B C   1 
ATOM   1392 O O   . VAL A  1 172 ? -26.60400 11.08300  -6.85000  1.000 16.46410  ? 223 VAL B O   1 
ATOM   1393 C CB  . VAL A  1 172 ? -27.37600 10.93200  -9.83600  1.000 18.84633  ? 223 VAL B CB  1 
ATOM   1394 C CG1 . VAL A  1 172 ? -28.59600 11.83400  -9.75200  1.000 15.83145  ? 223 VAL B CG1 1 
ATOM   1395 C CG2 . VAL A  1 172 ? -27.07400 10.55800  -11.27900 1.000 18.03933  ? 223 VAL B CG2 1 
ATOM   1396 N N   . ARG A  1 173 ? -26.56000 13.25100  -7.43200  1.000 18.13208  ? 224 ARG B N   1 
ATOM   1397 C CA  . ARG A  1 173 ? -26.73400 13.74400  -6.07700  1.000 12.87449  ? 224 ARG B CA  1 
ATOM   1398 C C   . ARG A  1 173 ? -25.70100 13.10200  -5.15200  1.000 18.15242  ? 224 ARG B C   1 
ATOM   1399 O O   . ARG A  1 173 ? -26.00000 12.76800  -4.02600  1.000 20.67679  ? 224 ARG B O   1 
ATOM   1400 C CB  . ARG A  1 173 ? -28.17200 13.55800  -5.63000  1.000 18.60478  ? 224 ARG B CB  1 
ATOM   1401 C CG  . ARG A  1 173 ? -29.13000 14.44200  -6.41200  1.000 22.47207  ? 224 ARG B CG  1 
ATOM   1402 C CD  . ARG A  1 173 ? -30.57600 14.29800  -5.98200  1.000 16.46437  ? 224 ARG B CD  1 
ATOM   1403 N NE  . ARG A  1 173 ? -30.84100 14.87100  -4.67200  1.000 18.86125  ? 224 ARG B NE  1 
ATOM   1404 C CZ  . ARG A  1 173 ? -31.02600 16.16300  -4.43700  1.000 29.45761  ? 224 ARG B CZ  1 
ATOM   1405 N NH1 . ARG A  1 173 ? -30.97300 17.04100  -5.42100  1.000 23.61329  ? 224 ARG B NH1 1 
ATOM   1406 N NH2 . ARG A  1 173 ? -31.26900 16.57900  -3.21000  1.000 24.79663  ? 224 ARG B NH2 1 
ATOM   1407 N N   . GLY A  1 174 ? -24.49500 12.90600  -5.65300  1.000 18.41379  ? 225 GLY B N   1 
ATOM   1408 C CA  . GLY A  1 174 ? -23.39800 12.30600  -4.88000  1.000 15.32832  ? 225 GLY B CA  1 
ATOM   1409 C C   . GLY A  1 174 ? -23.52000 10.81000  -4.68900  1.000 20.56039  ? 225 GLY B C   1 
ATOM   1410 O O   . GLY A  1 174 ? -22.71700 10.27100  -3.94300  1.000 17.13046  ? 225 GLY B O   1 
ATOM   1411 N N   . GLN A  1 175 ? -24.45100 10.16100  -5.39000  1.000 20.41699  ? 226 GLN B N   1 
ATOM   1412 C CA  . GLN A  1 175 ? -24.61700 8.73600   -5.09700  1.000 21.18056  ? 226 GLN B CA  1 
ATOM   1413 C C   . GLN A  1 175 ? -24.24100 7.88300   -6.29200  1.000 16.03443  ? 226 GLN B C   1 
ATOM   1414 O O   . GLN A  1 175 ? -24.78000 8.07300   -7.38900  1.000 21.04201  ? 226 GLN B O   1 
ATOM   1415 C CB  . GLN A  1 175 ? -26.05800 8.37700   -4.66600  1.000 24.92964  ? 226 GLN B CB  1 
ATOM   1416 C CG  . GLN A  1 175 ? -26.49000 9.21100   -3.47700  1.000 22.01119  ? 226 GLN B CG  1 
ATOM   1417 C CD  . GLN A  1 175 ? -25.87200 8.74000   -2.17400  1.000 25.87717  ? 226 GLN B CD  1 
ATOM   1418 O OE1 . GLN A  1 175 ? -25.49000 7.59300   -2.02000  1.000 22.70067  ? 226 GLN B OE1 1 
ATOM   1419 N NE2 . GLN A  1 175 ? -25.69000 9.67900   -1.25600  1.000 40.19954  ? 226 GLN B NE2 1 
ATOM   1420 N N   . SER A  1 176 ? -23.35200 6.92000   -6.04600  1.000 18.00622  ? 227 SER B N   1 
ATOM   1421 C CA  . SER A  1 176 ? -22.87300 5.93700   -7.01500  1.000 22.52110  ? 227 SER B CA  1 
ATOM   1422 C C   . SER A  1 176 ? -23.73700 4.68800   -7.11600  1.000 24.88353  ? 227 SER B C   1 
ATOM   1423 O O   . SER A  1 176 ? -23.62600 3.97100   -8.10900  1.000 21.21061  ? 227 SER B O   1 
ATOM   1424 C CB  . SER A  1 176 ? -21.47000 5.49400   -6.63300  1.000 20.03353  ? 227 SER B CB  1 
ATOM   1425 O OG  . SER A  1 176 ? -20.59400 6.53400   -6.99000  1.000 39.28299  ? 227 SER B OG  1 
ATOM   1426 N N   . GLY A  1 177 ? -24.55100 4.38600   -6.09900  1.000 20.33930  ? 228 GLY B N   1 
ATOM   1427 C CA  . GLY A  1 177 ? -25.52000 3.31300   -6.17000  1.000 15.48577  ? 228 GLY B CA  1 
ATOM   1428 C C   . GLY A  1 177 ? -26.87300 3.85400   -6.61000  1.000 17.56016  ? 228 GLY B C   1 
ATOM   1429 O O   . GLY A  1 177 ? -27.01400 5.03300   -6.94000  1.000 19.87796  ? 228 GLY B O   1 
ATOM   1430 N N   . ARG A  1 178 ? -27.88700 2.97100   -6.60300  1.000 17.49947  ? 229 ARG B N   1 
ATOM   1431 C CA  . ARG A  1 178 ? -29.18600 3.31700   -7.17000  1.000 13.76375  ? 229 ARG B CA  1 
ATOM   1432 C C   . ARG A  1 178 ? -30.27400 2.63600   -6.35600  1.000 19.18878  ? 229 ARG B C   1 
ATOM   1433 O O   . ARG A  1 178 ? -30.04300 1.59700   -5.72600  1.000 18.33272  ? 229 ARG B O   1 
ATOM   1434 C CB  . ARG A  1 178 ? -29.30300 2.91200   -8.64800  1.000 15.01931  ? 229 ARG B CB  1 
ATOM   1435 C CG  . ARG A  1 178 ? -28.32000 3.69500   -9.56400  1.000 20.14364  ? 229 ARG B CG  1 
ATOM   1436 C CD  . ARG A  1 178 ? -28.81200 5.12500   -9.76000  1.000 19.57091  ? 229 ARG B CD  1 
ATOM   1437 N NE  . ARG A  1 178 ? -28.06500 5.85300   -10.78300 1.000 21.25411  ? 229 ARG B NE  1 
ATOM   1438 C CZ  . ARG A  1 178 ? -26.93500 6.53000   -10.59100 1.000 25.85001  ? 229 ARG B CZ  1 
ATOM   1439 N NH1 . ARG A  1 178 ? -26.37600 6.62500   -9.39100  1.000 16.44677  ? 229 ARG B NH1 1 
ATOM   1440 N NH2 . ARG A  1 178 ? -26.36800 7.15000   -11.63300 1.000 19.64765  ? 229 ARG B NH2 1 
ATOM   1441 N N   . ILE A  1 179 ? -31.47200 3.24200   -6.38500  1.000 15.38965  ? 230 ILE B N   1 
ATOM   1442 C CA  . ILE A  1 179 ? -32.70300 2.62900   -5.89700  1.000 14.45738  ? 230 ILE B CA  1 
ATOM   1443 C C   . ILE A  1 179 ? -33.71000 2.72200   -7.01000  1.000 14.75853  ? 230 ILE B C   1 
ATOM   1444 O O   . ILE A  1 179 ? -34.08900 3.83400   -7.40700  1.000 17.83903  ? 230 ILE B O   1 
ATOM   1445 C CB  . ILE A  1 179 ? -33.26200 3.32700   -4.64200  1.000 18.61338  ? 230 ILE B CB  1 
ATOM   1446 C CG1 . ILE A  1 179 ? -32.34400 3.06000   -3.44500  1.000 17.32512  ? 230 ILE B CG1 1 
ATOM   1447 C CG2 . ILE A  1 179 ? -34.65200 2.73100   -4.32800  1.000 11.87360  ? 230 ILE B CG2 1 
ATOM   1448 C CD1 . ILE A  1 179 ? -32.83000 3.73300   -2.07600  1.000 16.59761  ? 230 ILE B CD1 1 
ATOM   1449 N N   . ASN A  1 180 ? -34.18000 1.56500   -7.50200  1.000 11.87547  ? 231 ASN B N   1 
ATOM   1450 C CA  . ASN A  1 180 ? -35.21800 1.53400   -8.52600  1.000 11.07470  ? 231 ASN B CA  1 
ATOM   1451 C C   . ASN A  1 180 ? -36.56600 1.43700   -7.83300  1.000 13.28248  ? 231 ASN B C   1 
ATOM   1452 O O   . ASN A  1 180 ? -36.72000 0.65500   -6.90100  1.000 15.90486  ? 231 ASN B O   1 
ATOM   1453 C CB  . ASN A  1 180 ? -34.99200 0.32000   -9.42700  1.000 14.11170  ? 231 ASN B CB  1 
ATOM   1454 C CG  . ASN A  1 180 ? -33.93300 0.58500   -10.46400 1.000 18.71515  ? 231 ASN B CG  1 
ATOM   1455 O OD1 . ASN A  1 180 ? -33.43300 1.72600   -10.57300 1.000 17.59638  ? 231 ASN B OD1 1 
ATOM   1456 N ND2 . ASN A  1 180 ? -33.36200 -0.50200  -10.98200 1.000 19.54965  ? 231 ASN B ND2 1 
ATOM   1457 N N   . TYR A  1 181 ? -37.53800 2.20600   -8.30300  1.000 12.58417  ? 232 TYR B N   1 
ATOM   1458 C CA  . TYR A  1 181 ? -38.85700 2.31000   -7.67800  1.000 18.22491  ? 232 TYR B CA  1 
ATOM   1459 C C   . TYR A  1 181 ? -39.89300 1.55000   -8.50300  1.000 18.30649  ? 232 TYR B C   1 
ATOM   1460 O O   . TYR A  1 181 ? -39.85300 1.56500   -9.74100  1.000 13.57510  ? 232 TYR B O   1 
ATOM   1461 C CB  . TYR A  1 181 ? -39.28900 3.77100   -7.54800  1.000 10.86340  ? 232 TYR B CB  1 
ATOM   1462 C CG  . TYR A  1 181 ? -38.23600 4.56100   -6.85400  1.000 15.06340  ? 232 TYR B CG  1 
ATOM   1463 C CD1 . TYR A  1 181 ? -38.14100 4.54300   -5.46000  1.000 15.96813  ? 232 TYR B CD1 1 
ATOM   1464 C CD2 . TYR A  1 181 ? -37.23800 5.21700   -7.59000  1.000 14.00835  ? 232 TYR B CD2 1 
ATOM   1465 C CE1 . TYR A  1 181 ? -37.13400 5.21900   -4.79700  1.000 13.50576  ? 232 TYR B CE1 1 
ATOM   1466 C CE2 . TYR A  1 181 ? -36.22600 5.90000   -6.94300  1.000 17.68485  ? 232 TYR B CE2 1 
ATOM   1467 C CZ  . TYR A  1 181 ? -36.17100 5.88600   -5.54700  1.000 10.89725  ? 232 TYR B CZ  1 
ATOM   1468 O OH  . TYR A  1 181 ? -35.15400 6.54000   -4.89700  1.000 19.73349  ? 232 TYR B OH  1 
ATOM   1469 N N   . TYR A  1 182 ? -40.80400 0.87200   -7.79800  1.000 13.66207  ? 233 TYR B N   1 
ATOM   1470 C CA  . TYR A  1 182 ? -41.83600 0.02900   -8.36500  1.000 13.22413  ? 233 TYR B CA  1 
ATOM   1471 C C   . TYR A  1 182 ? -43.12400 0.30000   -7.62400  1.000 15.07436  ? 233 TYR B C   1 
ATOM   1472 O O   . TYR A  1 182 ? -43.10500 0.68800   -6.45600  1.000 14.82706  ? 233 TYR B O   1 
ATOM   1473 C CB  . TYR A  1 182 ? -41.45600 -1.44300  -8.22500  1.000 14.03583  ? 233 TYR B CB  1 
ATOM   1474 C CG  . TYR A  1 182 ? -40.15000 -1.75600  -8.88900  1.000 14.04768  ? 233 TYR B CG  1 
ATOM   1475 C CD1 . TYR A  1 182 ? -40.08100 -1.91800  -10.26000 1.000 14.25103  ? 233 TYR B CD1 1 
ATOM   1476 C CD2 . TYR A  1 182 ? -38.97000 -1.82500  -8.14700  1.000 18.65254  ? 233 TYR B CD2 1 
ATOM   1477 C CE1 . TYR A  1 182 ? -38.86500 -2.18500  -10.90900 1.000 14.37589  ? 233 TYR B CE1 1 
ATOM   1478 C CE2 . TYR A  1 182 ? -37.75300 -2.09800  -8.76400  1.000 18.83104  ? 233 TYR B CE2 1 
ATOM   1479 C CZ  . TYR A  1 182 ? -37.71600 -2.26300  -10.16000 1.000 21.76185  ? 233 TYR B CZ  1 
ATOM   1480 O OH  . TYR A  1 182 ? -36.49900 -2.53500  -10.76900 1.000 20.90428  ? 233 TYR B OH  1 
ATOM   1481 N N   . TRP A  1 183 ? -44.24300 -0.01100  -8.26500  1.000 11.92639  ? 234 TRP B N   1 
ATOM   1482 C CA  . TRP A  1 183 ? -45.54900 0.18700   -7.63800  1.000 15.00617  ? 234 TRP B CA  1 
ATOM   1483 C C   . TRP A  1 183 ? -46.57400 -0.74900  -8.26000  1.000 17.67566  ? 234 TRP B C   1 
ATOM   1484 O O   . TRP A  1 183 ? -46.42500 -1.19600  -9.41200  1.000 15.68748  ? 234 TRP B O   1 
ATOM   1485 C CB  . TRP A  1 183 ? -46.03100 1.64500   -7.78600  1.000 13.63900  ? 234 TRP B CB  1 
ATOM   1486 C CG  . TRP A  1 183 ? -46.18100 2.03000   -9.18700  1.000 13.34288  ? 234 TRP B CG  1 
ATOM   1487 C CD1 . TRP A  1 183 ? -45.18100 2.47400   -9.99800  1.000 20.13834  ? 234 TRP B CD1 1 
ATOM   1488 C CD2 . TRP A  1 183 ? -47.36800 2.00900   -9.98100  1.000 16.65587  ? 234 TRP B CD2 1 
ATOM   1489 N NE1 . TRP A  1 183 ? -45.67100 2.73400   -11.25300 1.000 18.75847  ? 234 TRP B NE1 1 
ATOM   1490 C CE2 . TRP A  1 183 ? -47.01300 2.45900   -11.26500 1.000 18.03437  ? 234 TRP B CE2 1 
ATOM   1491 C CE3 . TRP A  1 183 ? -48.70000 1.65800   -9.73200  1.000 17.18605  ? 234 TRP B CE3 1 
ATOM   1492 C CZ2 . TRP A  1 183 ? -47.93600 2.58700   -12.29600 1.000 19.05959  ? 234 TRP B CZ2 1 
ATOM   1493 C CZ3 . TRP A  1 183 ? -49.62200 1.78800   -10.76000 1.000 21.31752  ? 234 TRP B CZ3 1 
ATOM   1494 C CH2 . TRP A  1 183 ? -49.23000 2.24900   -12.03500 1.000 15.25896  ? 234 TRP B CH2 1 
ATOM   1495 N N   . THR A  1 184 ? -47.65800 -0.98100  -7.51800  1.000 13.98548  ? 235 THR B N   1 
ATOM   1496 C CA  . THR A  1 184 ? -48.77800 -1.66600  -8.13900  1.000 11.74236  ? 235 THR B CA  1 
ATOM   1497 C C   . THR A  1 184 ? -50.05500 -1.27300  -7.39600  1.000 20.16783  ? 235 THR B C   1 
ATOM   1498 O O   . THR A  1 184 ? -50.01300 -0.84300  -6.23100  1.000 17.39792  ? 235 THR B O   1 
ATOM   1499 C CB  . THR A  1 184 ? -48.57600 -3.18400  -8.09200  1.000 14.46990  ? 235 THR B CB  1 
ATOM   1500 O OG1 . THR A  1 184 ? -49.63700 -3.85100  -8.79300  1.000 16.15934  ? 235 THR B OG1 1 
ATOM   1501 C CG2 . THR A  1 184 ? -48.62200 -3.68600  -6.61100  1.000 9.86188   ? 235 THR B CG2 1 
ATOM   1502 N N   . LEU A  1 185 ? -51.19800 -1.45000  -8.07100  1.000 18.79467  ? 236 LEU B N   1 
ATOM   1503 C CA  . LEU A  1 185 ? -52.50900 -1.28100  -7.45700  1.000 21.08089  ? 236 LEU B CA  1 
ATOM   1504 C C   . LEU A  1 185 ? -52.98400 -2.64600  -6.98800  1.000 21.56443  ? 236 LEU B C   1 
ATOM   1505 O O   . LEU A  1 185 ? -53.14500 -3.56600  -7.79900  1.000 20.66464  ? 236 LEU B O   1 
ATOM   1506 C CB  . LEU A  1 185 ? -53.51700 -0.71100  -8.44700  1.000 18.18193  ? 236 LEU B CB  1 
ATOM   1507 C CG  . LEU A  1 185 ? -53.16700 0.71200   -8.86400  1.000 18.03417  ? 236 LEU B CG  1 
ATOM   1508 C CD1 . LEU A  1 185 ? -53.92100 1.08300   -10.12600 1.000 22.41172  ? 236 LEU B CD1 1 
ATOM   1509 C CD2 . LEU A  1 185 ? -53.38900 1.64400   -7.73100  1.000 20.84137  ? 236 LEU B CD2 1 
ATOM   1510 N N   . LEU A  1 186 ? -53.20700 -2.78200  -5.69200  1.000 16.88828  ? 237 LEU B N   1 
ATOM   1511 C CA  . LEU A  1 186 ? -53.71000 -4.01500  -5.09600  1.000 15.28997  ? 237 LEU B CA  1 
ATOM   1512 C C   . LEU A  1 186 ? -55.22400 -3.90900  -4.98400  1.000 25.56593  ? 237 LEU B C   1 
ATOM   1513 O O   . LEU A  1 186 ? -55.73400 -2.99200  -4.32100  1.000 20.26494  ? 237 LEU B O   1 
ATOM   1514 C CB  . LEU A  1 186 ? -53.08600 -4.23000  -3.72100  1.000 16.99089  ? 237 LEU B CB  1 
ATOM   1515 C CG  . LEU A  1 186 ? -53.45900 -5.50000  -2.97400  1.000 15.89078  ? 237 LEU B CG  1 
ATOM   1516 C CD1 . LEU A  1 186 ? -52.84300 -6.68000  -3.70500  1.000 17.76262  ? 237 LEU B CD1 1 
ATOM   1517 C CD2 . LEU A  1 186 ? -52.83200 -5.41800  -1.58300  1.000 12.95590  ? 237 LEU B CD2 1 
ATOM   1518 N N   . GLU A  1 187 ? -55.91500 -4.78900  -5.65900  1.000 17.76914  ? 238 GLU B N   1 
ATOM   1519 C CA  . GLU A  1 187 ? -57.35600 -4.72400  -5.66400  1.000 22.42847  ? 238 GLU B CA  1 
ATOM   1520 C C   . GLU A  1 187 ? -58.03900 -5.19800  -4.37500  1.000 15.26082  ? 238 GLU B C   1 
ATOM   1521 O O   . GLU A  1 187 ? -57.51900 -6.04300  -3.67400  1.000 14.14038  ? 238 GLU B O   1 
ATOM   1522 C CB  . GLU A  1 187 ? -57.90500 -5.53000  -6.86300  1.000 20.64597  ? 238 GLU B CB  1 
ATOM   1523 C CG  . GLU A  1 187 ? -57.92200 -7.03300  -6.69200  1.000 20.07560  ? 238 GLU B CG  1 
ATOM   1524 C CD  . GLU A  1 187 ? -58.16200 -7.74000  -8.01000  1.000 18.23715  ? 238 GLU B CD  1 
ATOM   1525 O OE1 . GLU A  1 187 ? -58.00500 -7.09400  -9.05500  1.000 27.60845  ? 238 GLU B OE1 1 
ATOM   1526 O OE2 . GLU A  1 187 ? -58.50800 -8.92900  -8.01000  1.000 33.68788  ? 238 GLU B OE2 1 
ATOM   1527 N N   . PRO A  1 188 ? -59.22100 -4.63400  -4.10700  1.000 18.55142  ? 239 PRO B N   1 
ATOM   1528 C CA  . PRO A  1 188 ? -59.98100 -5.13700  -2.96000  1.000 16.03434  ? 239 PRO B CA  1 
ATOM   1529 C C   . PRO A  1 188 ? -59.96800 -6.65700  -2.91500  1.000 21.01425  ? 239 PRO B C   1 
ATOM   1530 O O   . PRO A  1 188 ? -60.15800 -7.33100  -3.94300  1.000 21.86716  ? 239 PRO B O   1 
ATOM   1531 C CB  . PRO A  1 188 ? -61.38000 -4.57400  -3.21100  1.000 21.42845  ? 239 PRO B CB  1 
ATOM   1532 C CG  . PRO A  1 188 ? -61.14500 -3.28200  -3.97000  1.000 17.98407  ? 239 PRO B CG  1 
ATOM   1533 C CD  . PRO A  1 188 ? -59.93400 -3.56100  -4.84900  1.000 18.81756  ? 239 PRO B CD  1 
ATOM   1534 N N   . GLY A  1 189 ? -59.62600 -7.20000  -1.74100  1.000 17.62980  ? 240 GLY B N   1 
ATOM   1535 C CA  . GLY A  1 189 ? -59.58900 -8.65300  -1.50800  1.000 22.68188  ? 240 GLY B CA  1 
ATOM   1536 C C   . GLY A  1 189 ? -58.33100 -9.39100  -1.94100  1.000 27.04335  ? 240 GLY B C   1 
ATOM   1537 O O   . GLY A  1 189 ? -58.17500 -10.59000 -1.62300  1.000 24.57203  ? 240 GLY B O   1 
ATOM   1538 N N   . ASP A  1 190 ? -57.44400 -8.74500  -2.67500  1.000 24.02743  ? 241 ASP B N   1 
ATOM   1539 C CA  . ASP A  1 190 ? -56.18500 -9.37800  -3.03900  1.000 21.12526  ? 241 ASP B CA  1 
ATOM   1540 C C   . ASP A  1 190 ? -55.18700 -9.16200  -1.90200  1.000 13.73133  ? 241 ASP B C   1 
ATOM   1541 O O   . ASP A  1 190 ? -55.36700 -8.28000  -1.04900  1.000 19.81635  ? 241 ASP B O   1 
ATOM   1542 C CB  . ASP A  1 190 ? -55.66500 -8.76700  -4.34200  1.000 21.22770  ? 241 ASP B CB  1 
ATOM   1543 C CG  . ASP A  1 190 ? -54.72300 -9.67200  -5.11600  1.000 19.03758  ? 241 ASP B CG  1 
ATOM   1544 O OD1 . ASP A  1 190 ? -54.38600 -10.79000 -4.68800  1.000 21.31690  ? 241 ASP B OD1 1 
ATOM   1545 O OD2 . ASP A  1 190 ? -54.24300 -9.18300  -6.14400  1.000 21.24191  ? 241 ASP B OD2 1 
ATOM   1546 N N   . THR A  1 191 ? -54.12100 -9.96500  -1.90600  1.000 16.86512  ? 242 THR B N   1 
ATOM   1547 C CA  . THR A  1 191 ? -53.01100 -9.88600  -0.96200  1.000 14.05608  ? 242 THR B CA  1 
ATOM   1548 C C   . THR A  1 191 ? -51.70000 -9.67300  -1.70400  1.000 17.15045  ? 242 THR B C   1 
ATOM   1549 O O   . THR A  1 191 ? -51.42500 -10.35300 -2.70200  1.000 19.10690  ? 242 THR B O   1 
ATOM   1550 C CB  . THR A  1 191 ? -52.93900 -11.14900 -0.10100  1.000 19.02571  ? 242 THR B CB  1 
ATOM   1551 O OG1 . THR A  1 191 ? -54.20900 -11.37100 0.53800   1.000 24.46819  ? 242 THR B OG1 1 
ATOM   1552 C CG2 . THR A  1 191 ? -51.72100 -11.16600 0.89000   1.000 23.44510  ? 242 THR B CG2 1 
ATOM   1553 N N   . ILE A  1 192 ? -50.89300 -8.73100  -1.22900  1.000 12.48851  ? 243 ILE B N   1 
ATOM   1554 C CA  . ILE A  1 192 ? -49.54900 -8.53100  -1.76400  1.000 12.14519  ? 243 ILE B CA  1 
ATOM   1555 C C   . ILE A  1 192 ? -48.55700 -9.14900  -0.78600  1.000 16.25340  ? 243 ILE B C   1 
ATOM   1556 O O   . ILE A  1 192 ? -48.70700 -9.03800  0.44900   1.000 15.87120  ? 243 ILE B O   1 
ATOM   1557 C CB  . ILE A  1 192 ? -49.27500 -7.03600  -2.02300  1.000 10.74600  ? 243 ILE B CB  1 
ATOM   1558 C CG1 . ILE A  1 192 ? -47.94300 -6.84700  -2.76700  1.000 13.07318  ? 243 ILE B CG1 1 
ATOM   1559 C CG2 . ILE A  1 192 ? -49.35200 -6.25400  -0.69800  1.000 8.39074   ? 243 ILE B CG2 1 
ATOM   1560 C CD1 . ILE A  1 192 ? -47.86500 -5.48900  -3.55000  1.000 11.64491  ? 243 ILE B CD1 1 
ATOM   1561 N N   . ILE A  1 193 ? -47.55300 -9.83100  -1.32000  1.000 11.58673  ? 244 ILE B N   1 
ATOM   1562 C CA  . ILE A  1 193 ? -46.54400 -10.48800 -0.50600  1.000 12.71566  ? 244 ILE B CA  1 
ATOM   1563 C C   . ILE A  1 193 ? -45.15200 -9.99200  -0.88500  1.000 13.79723  ? 244 ILE B C   1 
ATOM   1564 O O   . ILE A  1 193 ? -44.75300 -10.08300 -2.06300  1.000 13.71715  ? 244 ILE B O   1 
ATOM   1565 C CB  . ILE A  1 193 ? -46.59400 -12.00900 -0.68900  1.000 23.12495  ? 244 ILE B CB  1 
ATOM   1566 C CG1 . ILE A  1 193 ? -48.03700 -12.50600 -0.43800  1.000 24.64071  ? 244 ILE B CG1 1 
ATOM   1567 C CG2 . ILE A  1 193 ? -45.53900 -12.67000 0.22200   1.000 19.06149  ? 244 ILE B CG2 1 
ATOM   1568 C CD1 . ILE A  1 193 ? -48.13300 -13.96800 0.00200   1.000 31.23316  ? 244 ILE B CD1 1 
ATOM   1569 N N   . PHE A  1 194 ? -44.40600 -9.52800  0.12400   1.000 12.50823  ? 245 PHE B N   1 
ATOM   1570 C CA  . PHE A  1 194 ? -42.99500 -9.15300  0.01200   1.000 14.59714  ? 245 PHE B CA  1 
ATOM   1571 C C   . PHE A  1 194 ? -42.09700 -10.21700 0.63900   1.000 18.56008  ? 245 PHE B C   1 
ATOM   1572 O O   . PHE A  1 194 ? -42.27400 -10.59600 1.80800   1.000 16.84636  ? 245 PHE B O   1 
ATOM   1573 C CB  . PHE A  1 194 ? -42.72500 -7.79200  0.68400   1.000 10.81836  ? 245 PHE B CB  1 
ATOM   1574 C CG  . PHE A  1 194 ? -43.35200 -6.63700  -0.03500  1.000 14.08344  ? 245 PHE B CG  1 
ATOM   1575 C CD1 . PHE A  1 194 ? -44.70700 -6.42500  0.04500   1.000 12.61219  ? 245 PHE B CD1 1 
ATOM   1576 C CD2 . PHE A  1 194 ? -42.57200 -5.78400  -0.85000  1.000 13.08733  ? 245 PHE B CD2 1 
ATOM   1577 C CE1 . PHE A  1 194 ? -45.29800 -5.40800  -0.65800  1.000 13.92136  ? 245 PHE B CE1 1 
ATOM   1578 C CE2 . PHE A  1 194 ? -43.14200 -4.75100  -1.56100  1.000 12.26011  ? 245 PHE B CE2 1 
ATOM   1579 C CZ  . PHE A  1 194 ? -44.52100 -4.55900  -1.48300  1.000 16.56400  ? 245 PHE B CZ  1 
ATOM   1580 N N   . GLU A  1 195 ? -41.07600 -10.63500 -0.10200  1.000 14.47512  ? 246 GLU B N   1 
ATOM   1581 C CA  . GLU A  1 195 ? -40.05300 -11.53000 0.43400   1.000 18.00563  ? 246 GLU B CA  1 
ATOM   1582 C C   . GLU A  1 195 ? -38.69700 -10.99900 0.01200   1.000 17.47560  ? 246 GLU B C   1 
ATOM   1583 O O   . GLU A  1 195 ? -38.52400 -10.57800 -1.13200  1.000 15.01735  ? 246 GLU B O   1 
ATOM   1584 C CB  . GLU A  1 195 ? -40.25200 -12.96800 -0.07800  1.000 18.96126  ? 246 GLU B CB  1 
ATOM   1585 C CG  . GLU A  1 195 ? -41.63400 -13.49700 0.34200   1.000 20.96201  ? 246 GLU B CG  1 
ATOM   1586 C CD  . GLU A  1 195 ? -41.65400 -14.98000 0.56600   1.000 33.09222  ? 246 GLU B CD  1 
ATOM   1587 O OE1 . GLU A  1 195 ? -40.97700 -15.68500 -0.21500  1.000 39.77251  ? 246 GLU B OE1 1 
ATOM   1588 O OE2 . GLU A  1 195 ? -42.33600 -15.43400 1.51300   1.000 45.41014  ? 246 GLU B OE2 1 
ATOM   1589 N N   . ALA A  1 196 ? -37.74800 -11.00500 0.93700   1.000 17.31191  ? 247 ALA B N   1 
ATOM   1590 C CA  . ALA A  1 196 ? -36.43400 -10.49300 0.64400   1.000 16.31845  ? 247 ALA B CA  1 
ATOM   1591 C C   . ALA A  1 196 ? -35.45000 -11.07400 1.63400   1.000 20.49016  ? 247 ALA B C   1 
ATOM   1592 O O   . ALA A  1 196 ? -35.78100 -11.34600 2.80500   1.000 15.95527  ? 247 ALA B O   1 
ATOM   1593 C CB  . ALA A  1 196 ? -36.42400 -8.96100  0.70200   1.000 14.80738  ? 247 ALA B CB  1 
ATOM   1594 N N   . ASN A  1 197 ? -34.19600 -11.17300 1.18600   1.000 13.96803  ? 248 ASN B N   1 
ATOM   1595 C CA  . ASN A  1 197 ? -33.11100 -11.36000 2.14500   1.000 24.61954  ? 248 ASN B CA  1 
ATOM   1596 C C   . ASN A  1 197 ? -32.11700 -10.20000 2.10200   1.000 19.35093  ? 248 ASN B C   1 
ATOM   1597 O O   . ASN A  1 197 ? -31.03600 -10.30700 2.69100   1.000 20.55694  ? 248 ASN B O   1 
ATOM   1598 C CB  . ASN A  1 197 ? -32.39500 -12.69400 1.89600   1.000 20.16981  ? 248 ASN B CB  1 
ATOM   1599 C CG  . ASN A  1 197 ? -31.72100 -12.73900 0.54200   1.000 26.50357  ? 248 ASN B CG  1 
ATOM   1600 O OD1 . ASN A  1 197 ? -31.91100 -11.85600 -0.31200  1.000 23.75125  ? 248 ASN B OD1 1 
ATOM   1601 N ND2 . ASN A  1 197 ? -30.99700 -13.81900 0.30300   1.000 27.21193  ? 248 ASN B ND2 1 
ATOM   1602 N N   . GLY A  1 198 ? -32.52700 -9.10700  1.46900   1.000 18.88142  ? 249 GLY B N   1 
ATOM   1603 C CA  . GLY A  1 198 ? -31.69900 -7.90000  1.42800   1.000 15.29857  ? 249 GLY B CA  1 
ATOM   1604 C C   . GLY A  1 198 ? -32.11800 -6.91200  0.36100   1.000 15.58038  ? 249 GLY B C   1 
ATOM   1605 O O   . GLY A  1 198 ? -32.92300 -7.28200  -0.48500  1.000 16.83284  ? 249 GLY B O   1 
ATOM   1606 N N   . ASN A  1 199 ? -31.67800 -5.65900  0.48100   1.000 17.38532  ? 250 ASN B N   1 
ATOM   1607 C CA  . ASN A  1 199 ? -31.85400 -4.68100  -0.62500  1.000 12.53549  ? 250 ASN B CA  1 
ATOM   1608 C C   . ASN A  1 199 ? -33.29700 -4.16700  -0.81200  1.000 16.48751  ? 250 ASN B C   1 
ATOM   1609 O O   . ASN A  1 199 ? -33.54600 -3.48400  -1.80000  1.000 17.43881  ? 250 ASN B O   1 
ATOM   1610 C CB  . ASN A  1 199 ? -31.25600 -5.25900  -1.91200  1.000 11.81228  ? 250 ASN B CB  1 
ATOM   1611 C CG  . ASN A  1 199 ? -29.80200 -5.66100  -1.76500  1.000 20.13119  ? 250 ASN B CG  1 
ATOM   1612 O OD1 . ASN A  1 199 ? -29.47400 -6.59200  -1.03700  1.000 17.05804  ? 250 ASN B OD1 1 
ATOM   1613 N ND2 . ASN A  1 199 ? -28.91500 -4.96000  -2.45000  1.000 18.13340  ? 250 ASN B ND2 1 
ATOM   1614 N N   . LEU A  1 200 ? -34.19100 -4.46100  0.11800   1.000 14.46475  ? 251 LEU B N   1 
ATOM   1615 C CA  . LEU A  1 200 ? -35.58500 -3.98800  -0.00700  1.000 17.09913  ? 251 LEU B CA  1 
ATOM   1616 C C   . LEU A  1 200 ? -35.80900 -2.61500  0.63100   1.000 16.10832  ? 251 LEU B C   1 
ATOM   1617 O O   . LEU A  1 200 ? -35.45600 -2.42600  1.78500   1.000 16.24445  ? 251 LEU B O   1 
ATOM   1618 C CB  . LEU A  1 200 ? -36.54500 -5.00700  0.61600   1.000 18.66161  ? 251 LEU B CB  1 
ATOM   1619 C CG  . LEU A  1 200 ? -38.00500 -4.56900  0.71400   1.000 14.85744  ? 251 LEU B CG  1 
ATOM   1620 C CD1 . LEU A  1 200 ? -38.60500 -4.34900  -0.66400  1.000 10.53411  ? 251 LEU B CD1 1 
ATOM   1621 C CD2 . LEU A  1 200 ? -38.82200 -5.58400  1.49700   1.000 12.83318  ? 251 LEU B CD2 1 
ATOM   1622 N N   . ILE A  1 201 ? -36.28600 -1.67600  -0.15800  1.000 11.21608  ? 252 ILE B N   1 
ATOM   1623 C CA  . ILE A  1 201 ? -36.78900 -0.42900  0.41900   1.000 12.59406  ? 252 ILE B CA  1 
ATOM   1624 C C   . ILE A  1 201 ? -38.29100 -0.64500  0.56400   1.000 16.68377  ? 252 ILE B C   1 
ATOM   1625 O O   . ILE A  1 201 ? -39.05300 -0.53900  -0.41000  1.000 14.03501  ? 252 ILE B O   1 
ATOM   1626 C CB  . ILE A  1 201 ? -36.42000 0.78100   -0.43700  1.000 11.52550  ? 252 ILE B CB  1 
ATOM   1627 C CG1 . ILE A  1 201 ? -34.97500 0.56100   -0.95200  1.000 15.24591  ? 252 ILE B CG1 1 
ATOM   1628 C CG2 . ILE A  1 201 ? -36.59700 2.09400   0.27200   1.000 16.28152  ? 252 ILE B CG2 1 
ATOM   1629 C CD1 . ILE A  1 201 ? -33.90700 0.68500   0.15800   1.000 11.33470  ? 252 ILE B CD1 1 
ATOM   1630 N N   . ALA A  1 202 ? -38.67500 -1.03900  1.76100   1.000 14.16108  ? 253 ALA B N   1 
ATOM   1631 C CA  . ALA A  1 202 ? -40.05100 -1.42300  2.00100   1.000 12.76881  ? 253 ALA B CA  1 
ATOM   1632 C C   . ALA A  1 202 ? -41.06400 -0.34300  2.07300   1.000 11.64269  ? 253 ALA B C   1 
ATOM   1633 O O   . ALA A  1 202 ? -40.78000 0.77500   2.37800   1.000 18.20953  ? 253 ALA B O   1 
ATOM   1634 C CB  . ALA A  1 202 ? -40.14900 -2.24500  3.27200   1.000 12.10739  ? 253 ALA B CB  1 
ATOM   1635 N N   . PRO A  1 203 ? -42.26200 -0.73200  1.75600   1.000 15.70059  ? 254 PRO B N   1 
ATOM   1636 C CA  . PRO A  1 203 ? -43.34200 0.20300   1.89700   1.000 11.98810  ? 254 PRO B CA  1 
ATOM   1637 C C   . PRO A  1 203 ? -43.58800 0.54100   3.36900   1.000 15.23041  ? 254 PRO B C   1 
ATOM   1638 O O   . PRO A  1 203 ? -43.44300 -0.32200  4.20600   1.000 15.30245  ? 254 PRO B O   1 
ATOM   1639 C CB  . PRO A  1 203 ? -44.53700 -0.57300  1.33700   1.000 11.93498  ? 254 PRO B CB  1 
ATOM   1640 C CG  . PRO A  1 203 ? -43.97800 -1.66700  0.51500   1.000 13.07323  ? 254 PRO B CG  1 
ATOM   1641 C CD  . PRO A  1 203 ? -42.69400 -2.01500  1.18100   1.000 11.72213  ? 254 PRO B CD  1 
ATOM   1642 N N   . ARG A  1 204 ? -43.91500 1.78000   3.65200   1.000 14.86538  ? 255 ARG B N   1 
ATOM   1643 C CA  . ARG A  1 204 ? -44.30600 2.17800   4.99700   1.000 19.44338  ? 255 ARG B CA  1 
ATOM   1644 C C   . ARG A  1 204 ? -45.71200 2.73700   4.85400   1.000 15.70154  ? 255 ARG B C   1 
ATOM   1645 O O   . ARG A  1 204 ? -46.61300 2.23400   5.46300   1.000 16.25138  ? 255 ARG B O   1 
ATOM   1646 C CB  . ARG A  1 204 ? -43.35600 3.16600   5.64600   1.000 15.34565  ? 255 ARG B CB  1 
ATOM   1647 C CG  . ARG A  1 204 ? -43.69100 3.47400   7.08400   1.000 21.15944  ? 255 ARG B CG  1 
ATOM   1648 C CD  . ARG A  1 204 ? -43.62100 4.95500   7.37200   1.000 26.69912  ? 255 ARG B CD  1 
ATOM   1649 N NE  . ARG A  1 204 ? -44.07900 5.24900   8.72000   1.000 26.53978  ? 255 ARG B NE  1 
ATOM   1650 C CZ  . ARG A  1 204 ? -43.53400 6.16200   9.51200   1.000 34.28448  ? 255 ARG B CZ  1 
ATOM   1651 N NH1 . ARG A  1 204 ? -42.51100 6.88300   9.08800   1.000 32.76875  ? 255 ARG B NH1 1 
ATOM   1652 N NH2 . ARG A  1 204 ? -44.01300 6.35300   10.72700  1.000 31.43788  ? 255 ARG B NH2 1 
ATOM   1653 N N   . TYR A  1 205 ? -45.87400 3.75800   4.03600   1.000 15.12416  ? 256 TYR B N   1 
ATOM   1654 C CA  . TYR A  1 205 ? -47.20300 4.24300   3.75100   1.000 15.75082  ? 256 TYR B CA  1 
ATOM   1655 C C   . TYR A  1 205 ? -47.74200 3.84400   2.36200   1.000 20.99955  ? 256 TYR B C   1 
ATOM   1656 O O   . TYR A  1 205 ? -47.01300 3.92500   1.38600   1.000 16.69223  ? 256 TYR B O   1 
ATOM   1657 C CB  . TYR A  1 205 ? -47.33000 5.75700   3.91900   1.000 15.55116  ? 256 TYR B CB  1 
ATOM   1658 C CG  . TYR A  1 205 ? -47.16600 6.27700   5.31700   1.000 18.32131  ? 256 TYR B CG  1 
ATOM   1659 C CD1 . TYR A  1 205 ? -48.14700 6.08000   6.27500   1.000 21.76180  ? 256 TYR B CD1 1 
ATOM   1660 C CD2 . TYR A  1 205 ? -46.04200 6.99100   5.67200   1.000 21.42649  ? 256 TYR B CD2 1 
ATOM   1661 C CE1 . TYR A  1 205 ? -47.99500 6.57000   7.55400   1.000 20.62651  ? 256 TYR B CE1 1 
ATOM   1662 C CE2 . TYR A  1 205 ? -45.88100 7.48100   6.94400   1.000 26.69255  ? 256 TYR B CE2 1 
ATOM   1663 C CZ  . TYR A  1 205 ? -46.85800 7.26800   7.88100   1.000 30.93046  ? 256 TYR B CZ  1 
ATOM   1664 O OH  . TYR A  1 205 ? -46.68200 7.75900   9.14200   1.000 30.43608  ? 256 TYR B OH  1 
ATOM   1665 N N   . ALA A  1 206 ? -48.95900 3.34100   2.32100   1.000 12.01123  ? 257 ALA B N   1 
ATOM   1666 C CA  . ALA A  1 206 ? -49.66100 3.02800   1.08300   1.000 14.11012  ? 257 ALA B CA  1 
ATOM   1667 C C   . ALA A  1 206 ? -50.91900 3.88700   1.02300   1.000 21.87628  ? 257 ALA B C   1 
ATOM   1668 O O   . ALA A  1 206 ? -51.18400 4.67500   1.93000   1.000 17.82480  ? 257 ALA B O   1 
ATOM   1669 C CB  . ALA A  1 206 ? -49.99300 1.53600   1.00900   1.000 15.29385  ? 257 ALA B CB  1 
ATOM   1670 N N   . PHE A  1 207 ? -51.70100 3.76200   -0.05400  1.000 16.57119  ? 258 PHE B N   1 
ATOM   1671 C CA  . PHE A  1 207 ? -52.80200 4.69300   -0.29400  1.000 15.60001  ? 258 PHE B CA  1 
ATOM   1672 C C   . PHE A  1 207 ? -54.05200 3.96600   -0.77000  1.000 20.80133  ? 258 PHE B C   1 
ATOM   1673 O O   . PHE A  1 207 ? -54.05900 3.34700   -1.84100  1.000 22.08045  ? 258 PHE B O   1 
ATOM   1674 C CB  . PHE A  1 207 ? -52.38300 5.75200   -1.30500  1.000 12.53394  ? 258 PHE B CB  1 
ATOM   1675 C CG  . PHE A  1 207 ? -51.16000 6.53100   -0.88900  1.000 21.23763  ? 258 PHE B CG  1 
ATOM   1676 C CD1 . PHE A  1 207 ? -51.29300 7.67800   -0.09800  1.000 24.10234  ? 258 PHE B CD1 1 
ATOM   1677 C CD2 . PHE A  1 207 ? -49.87800 6.12800   -1.26900  1.000 16.22975  ? 258 PHE B CD2 1 
ATOM   1678 C CE1 . PHE A  1 207 ? -50.17600 8.41600   0.31300   1.000 21.91460  ? 258 PHE B CE1 1 
ATOM   1679 C CE2 . PHE A  1 207 ? -48.72400 6.87900   -0.87100  1.000 23.38732  ? 258 PHE B CE2 1 
ATOM   1680 C CZ  . PHE A  1 207 ? -48.87900 8.02700   -0.06000  1.000 26.57348  ? 258 PHE B CZ  1 
ATOM   1681 N N   . ALA A  1 208 ? -55.12600 4.04700   0.00900   1.000 17.44240  ? 259 ALA B N   1 
ATOM   1682 C CA  . ALA A  1 208 ? -56.40800 3.56300   -0.47900  1.000 17.29973  ? 259 ALA B CA  1 
ATOM   1683 C C   . ALA A  1 208 ? -57.02200 4.65300   -1.34000  1.000 21.48989  ? 259 ALA B C   1 
ATOM   1684 O O   . ALA A  1 208 ? -57.00300 5.83300   -0.97000  1.000 25.17842  ? 259 ALA B O   1 
ATOM   1685 C CB  . ALA A  1 208 ? -57.32900 3.20000   0.68000   1.000 28.40097  ? 259 ALA B CB  1 
ATOM   1686 N N   . LEU A  1 209 ? -57.48900 4.29800   -2.52600  1.000 19.28806  ? 260 LEU B N   1 
ATOM   1687 C CA  . LEU A  1 209 ? -57.83200 5.39300   -3.42000  1.000 22.14058  ? 260 LEU B CA  1 
ATOM   1688 C C   . LEU A  1 209 ? -58.85400 4.90500   -4.42600  1.000 29.90858  ? 260 LEU B C   1 
ATOM   1689 O O   . LEU A  1 209 ? -59.05200 3.69600   -4.62300  1.000 23.46183  ? 260 LEU B O   1 
ATOM   1690 C CB  . LEU A  1 209 ? -56.59900 5.98500   -4.13000  1.000 23.31427  ? 260 LEU B CB  1 
ATOM   1691 C CG  . LEU A  1 209 ? -56.19600 5.30400   -5.47400  1.000 27.64897  ? 260 LEU B CG  1 
ATOM   1692 C CD1 . LEU A  1 209 ? -55.08100 6.04400   -6.15700  1.000 23.94629  ? 260 LEU B CD1 1 
ATOM   1693 C CD2 . LEU A  1 209 ? -55.83300 3.85800   -5.29100  1.000 20.46292  ? 260 LEU B CD2 1 
ATOM   1694 N N   . SER A  1 210 ? -59.52400 5.89000   -5.02600  1.000 28.08934  ? 261 SER B N   1 
ATOM   1695 C CA  . SER A  1 210 ? -60.63000 5.70500   -5.96200  1.000 33.82631  ? 261 SER B CA  1 
ATOM   1696 C C   . SER A  1 210 ? -60.22600 6.48100   -7.20400  1.000 34.23716  ? 261 SER B C   1 
ATOM   1697 O O   . SER A  1 210 ? -60.33800 7.71000   -7.23100  1.000 33.26917  ? 261 SER B O   1 
ATOM   1698 C CB  . SER A  1 210 ? -61.94300 6.24200   -5.39700  1.000 33.46355  ? 261 SER B CB  1 
ATOM   1699 O OG  . SER A  1 210 ? -62.47300 5.34300   -4.42200  1.000 51.72608  ? 261 SER B OG  1 
ATOM   1700 N N   . ARG A  1 211 ? -59.74200 5.76500   -8.19900  1.000 28.89516  ? 262 ARG B N   1 
ATOM   1701 C CA  . ARG A  1 211 ? -59.30000 6.46400   -9.41800  1.000 34.37440  ? 262 ARG B CA  1 
ATOM   1702 C C   . ARG A  1 211 ? -60.55100 6.93300   -10.15700 1.000 36.36448  ? 262 ARG B C   1 
ATOM   1703 O O   . ARG A  1 211 ? -61.58500 6.27900   -10.07300 1.000 32.63045  ? 262 ARG B O   1 
ATOM   1704 C CB  . ARG A  1 211 ? -58.40400 5.56600   -10.27700 1.000 30.77373  ? 262 ARG B CB  1 
ATOM   1705 C CG  . ARG A  1 211 ? -57.03000 5.30200   -9.68100  1.000 27.65245  ? 262 ARG B CG  1 
ATOM   1706 C CD  . ARG A  1 211 ? -56.24500 4.37500   -10.58400 1.000 29.85289  ? 262 ARG B CD  1 
ATOM   1707 N NE  . ARG A  1 211 ? -56.83700 3.05400   -10.72300 1.000 21.31926  ? 262 ARG B NE  1 
ATOM   1708 C CZ  . ARG A  1 211 ? -56.85600 2.35900   -11.85200 1.000 25.47324  ? 262 ARG B CZ  1 
ATOM   1709 N NH1 . ARG A  1 211 ? -56.33000 2.86700   -12.95100 1.000 28.75866  ? 262 ARG B NH1 1 
ATOM   1710 N NH2 . ARG A  1 211 ? -57.40500 1.16000   -11.88300 1.000 29.95614  ? 262 ARG B NH2 1 
ATOM   1711 N N   . GLY A  1 212 ? -60.41200 8.02600   -10.87900 1.000 35.38948  ? 263 GLY B N   1 
ATOM   1712 C CA  . GLY A  1 212 ? -61.55700 8.54400   -11.63200 1.000 46.04979  ? 263 GLY B CA  1 
ATOM   1713 C C   . GLY A  1 212 ? -62.27000 9.63200   -10.87700 1.000 45.90538  ? 263 GLY B C   1 
ATOM   1714 O O   . GLY A  1 212 ? -62.39400 9.51400   -9.66500  1.000 52.10635  ? 263 GLY B O   1 
ATOM   1715 N N   . SER A  1 213 ? -62.70200 10.66600  -11.58600 1.000 63.09539  ? 264 SER B N   1 
ATOM   1716 C CA  . SER A  1 213 ? -63.49000 11.76100  -10.97300 1.000 61.81482  ? 264 SER B CA  1 
ATOM   1717 C C   . SER A  1 213 ? -64.87200 11.18600  -10.66900 1.000 72.63092  ? 264 SER B C   1 
ATOM   1718 O O   . SER A  1 213 ? -65.48100 11.56500  -9.65300  1.000 75.94691  ? 264 SER B O   1 
ATOM   1719 C CB  . SER A  1 213 ? -63.56900 12.93600  -11.90200 1.000 58.72327  ? 264 SER B CB  1 
ATOM   1720 O OG  . SER A  1 213 ? -63.68900 12.49500  -13.24300 1.000 64.38432  ? 264 SER B OG  1 
ATOM   1721 N N   . GLY A  1 214 ? -65.32700 10.27200  -11.51300 1.000 71.83342  ? 265 GLY B N   1 
ATOM   1722 C CA  . GLY A  1 214 ? -66.60700 9.60500   -11.22500 1.000 69.07613  ? 265 GLY B CA  1 
ATOM   1723 C C   . GLY A  1 214 ? -66.57200 9.00000   -9.84000  1.000 61.03082  ? 265 GLY B C   1 
ATOM   1724 O O   . GLY A  1 214 ? -65.48100 8.58700   -9.43800  1.000 69.05226  ? 265 GLY B O   1 
ATOM   1725 N N   . GLN B  2 1   ? -8.32900  0.40300   -9.61500  1.000 55.44991  ? 1   GLN H N   1 
ATOM   1726 C CA  . GLN B  2 1   ? -9.69500  0.22000   -10.09100 1.000 64.33241  ? 1   GLN H CA  1 
ATOM   1727 C C   . GLN B  2 1   ? -9.73000  -0.26500  -11.54100 1.000 51.04468  ? 1   GLN H C   1 
ATOM   1728 O O   . GLN B  2 1   ? -8.87700  -1.03600  -11.95700 1.000 48.77603  ? 1   GLN H O   1 
ATOM   1729 C CB  . GLN B  2 1   ? -10.48900 1.52000   -9.93000  1.000 57.58568  ? 1   GLN H CB  1 
ATOM   1730 C CG  . GLN B  2 1   ? -10.64600 1.98500   -8.49400  1.000 77.40273  ? 1   GLN H CG  1 
ATOM   1731 C CD  . GLN B  2 1   ? -11.41600 0.99700   -7.64100  1.000 86.91678  ? 1   GLN H CD  1 
ATOM   1732 O OE1 . GLN B  2 1   ? -12.63600 1.09600   -7.50400  1.000 83.58599  ? 1   GLN H OE1 1 
ATOM   1733 N NE2 . GLN B  2 1   ? -10.70400 0.03800   -7.05900  1.000 86.88986  ? 1   GLN H NE2 1 
ATOM   1734 N N   . VAL B  2 2   ? -10.71900 0.17900   -12.29100 1.000 50.21621  ? 2   VAL H N   1 
ATOM   1735 C CA  . VAL B  2 2   ? -10.78900 -0.18800  -13.67200 1.000 44.79433  ? 2   VAL H CA  1 
ATOM   1736 C C   . VAL B  2 2   ? -9.73300  0.48700   -14.49500 1.000 44.64132  ? 2   VAL H C   1 
ATOM   1737 O O   . VAL B  2 2   ? -9.50100  1.67400   -14.36400 1.000 40.90602  ? 2   VAL H O   1 
ATOM   1738 C CB  . VAL B  2 2   ? -12.15700 0.14700   -14.26100 1.000 40.55677  ? 2   VAL H CB  1 
ATOM   1739 C CG1 . VAL B  2 2   ? -12.56200 1.55800   -13.90700 1.000 45.97981  ? 2   VAL H CG1 1 
ATOM   1740 C CG2 . VAL B  2 2   ? -12.18100 -0.08200  -15.75600 1.000 42.79304  ? 2   VAL H CG2 1 
ATOM   1741 N N   . GLN B  2 3   ? -9.05200  -0.29100  -15.31200 1.000 45.93891  ? 3   GLN H N   1 
ATOM   1742 C CA  . GLN B  2 3   ? -8.09100  0.26600   -16.23000 1.000 40.72537  ? 3   GLN H CA  1 
ATOM   1743 C C   . GLN B  2 3   ? -8.45200  -0.22300  -17.61000 1.000 38.95431  ? 3   GLN H C   1 
ATOM   1744 O O   . GLN B  2 3   ? -8.64400  -1.40800  -17.78700 1.000 33.70467  ? 3   GLN H O   1 
ATOM   1745 C CB  . GLN B  2 3   ? -6.67300  -0.15700  -15.91800 1.000 41.58456  ? 3   GLN H CB  1 
ATOM   1746 C CG  . GLN B  2 3   ? -6.03200  0.56000   -14.74900 1.000 54.90776  ? 3   GLN H CG  1 
ATOM   1747 C CD  . GLN B  2 3   ? -4.63700  0.04500   -14.46600 1.000 71.68630  ? 3   GLN H CD  1 
ATOM   1748 O OE1 . GLN B  2 3   ? -3.68400  0.81600   -14.37100 1.000 75.51521  ? 3   GLN H OE1 1 
ATOM   1749 N NE2 . GLN B  2 3   ? -4.50800  -1.26900  -14.34300 1.000 76.60182  ? 3   GLN H NE2 1 
ATOM   1750 N N   . LEU B  2 4   ? -8.59100  0.69200   -18.56800 1.000 29.41287  ? 4   LEU H N   1 
ATOM   1751 C CA  . LEU B  2 4   ? -8.82900  0.29700   -19.97700 1.000 34.00242  ? 4   LEU H CA  1 
ATOM   1752 C C   . LEU B  2 4   ? -7.63600  0.80600   -20.79500 1.000 38.19920  ? 4   LEU H C   1 
ATOM   1753 O O   . LEU B  2 4   ? -7.19000  1.92700   -20.53600 1.000 31.39750  ? 4   LEU H O   1 
ATOM   1754 C CB  . LEU B  2 4   ? -10.15700 0.86600   -20.48300 1.000 30.06300  ? 4   LEU H CB  1 
ATOM   1755 C CG  . LEU B  2 4   ? -11.37900 -0.03400  -20.33000 1.000 33.68708  ? 4   LEU H CG  1 
ATOM   1756 C CD1 . LEU B  2 4   ? -11.54800 -0.47300  -18.89000 1.000 38.34825  ? 4   LEU H CD1 1 
ATOM   1757 C CD2 . LEU B  2 4   ? -12.62700 0.67300   -20.81800 1.000 38.93448  ? 4   LEU H CD2 1 
ATOM   1758 N N   . GLU B  2 5   ? -7.12200  -0.00700  -21.70200 1.000 38.78567  ? 5   GLU H N   1 
ATOM   1759 C CA  . GLU B  2 5   ? -5.91900  0.34100   -22.50400 1.000 36.63449  ? 5   GLU H CA  1 
ATOM   1760 C C   . GLU B  2 5   ? -6.10700  -0.16400  -23.93200 1.000 39.04462  ? 5   GLU H C   1 
ATOM   1761 O O   . GLU B  2 5   ? -6.31300  -1.36800  -24.09900 1.000 31.81523  ? 5   GLU H O   1 
ATOM   1762 C CB  . GLU B  2 5   ? -4.66400  -0.26200  -21.87900 1.000 37.45015  ? 5   GLU H CB  1 
ATOM   1763 C CG  . GLU B  2 5   ? -3.41900  -0.05900  -22.71900 1.000 52.76815  ? 5   GLU H CG  1 
ATOM   1764 C CD  . GLU B  2 5   ? -2.19100  0.31400   -21.91200 1.000 68.70211  ? 5   GLU H CD  1 
ATOM   1765 O OE1 . GLU B  2 5   ? -2.29800  0.35200   -20.67400 1.000 75.70281  ? 5   GLU H OE1 1 
ATOM   1766 O OE2 . GLU B  2 5   ? -1.13300  0.56200   -22.52100 1.000 70.50327  ? 5   GLU H OE2 1 
ATOM   1767 N N   . GLU B  2 6   ? -6.05400  0.71800   -24.90300 1.000 32.10532  ? 6   GLU H N   1 
ATOM   1768 C CA  . GLU B  2 6   ? -6.26200  0.34200   -26.27800 1.000 29.17597  ? 6   GLU H CA  1 
ATOM   1769 C C   . GLU B  2 6   ? -4.96600  -0.10200  -26.94200 1.000 34.04782  ? 6   GLU H C   1 
ATOM   1770 O O   . GLU B  2 6   ? -3.89800  0.40500   -26.63400 1.000 30.33895  ? 6   GLU H O   1 
ATOM   1771 C CB  . GLU B  2 6   ? -6.90800  1.48000   -27.06400 1.000 28.77348  ? 6   GLU H CB  1 
ATOM   1772 C CG  . GLU B  2 6   ? -8.13100  2.10600   -26.42700 1.000 34.03987  ? 6   GLU H CG  1 
ATOM   1773 C CD  . GLU B  2 6   ? -7.79400  3.25400   -25.49700 1.000 28.65395  ? 6   GLU H CD  1 
ATOM   1774 O OE1 . GLU B  2 6   ? -6.63200  3.36500   -25.07700 1.000 25.40001  ? 6   GLU H OE1 1 
ATOM   1775 O OE2 . GLU B  2 6   ? -8.70200  4.03700   -25.18200 1.000 26.22912  ? 6   GLU H OE2 1 
ATOM   1776 N N   . SER B  2 7   ? -5.06500  -1.07400  -27.83100 1.000 34.62348  ? 7   SER H N   1 
ATOM   1777 C CA  . SER B  2 7   ? -3.90000  -1.52200  -28.57100 1.000 35.79390  ? 7   SER H CA  1 
ATOM   1778 C C   . SER B  2 7   ? -4.34500  -1.79800  -29.97800 1.000 38.94884  ? 7   SER H C   1 
ATOM   1779 O O   . SER B  2 7   ? -5.47200  -2.19400  -30.22300 1.000 35.90387  ? 7   SER H O   1 
ATOM   1780 C CB  . SER B  2 7   ? -3.23800  -2.75100  -27.95700 1.000 32.63286  ? 7   SER H CB  1 
ATOM   1781 O OG  . SER B  2 7   ? -4.11300  -3.85300  -27.90700 1.000 49.53923  ? 7   SER H OG  1 
ATOM   1782 N N   . GLY B  2 8   ? -3.44100  -1.58200  -30.91500 1.000 45.34121  ? 8   GLY H N   1 
ATOM   1783 C CA  . GLY B  2 8   ? -3.81100  -1.74800  -32.29800 1.000 42.19760  ? 8   GLY H CA  1 
ATOM   1784 C C   . GLY B  2 8   ? -2.72000  -1.43800  -33.26400 1.000 45.72658  ? 8   GLY H C   1 
ATOM   1785 O O   . GLY B  2 8   ? -1.61100  -1.16100  -32.88000 1.000 43.60933  ? 8   GLY H O   1 
ATOM   1786 N N   . PRO B  2 9   ? -3.05000  -1.49800  -34.54000 1.000 49.70860  ? 9   PRO H N   1 
ATOM   1787 C CA  . PRO B  2 9   ? -2.08300  -1.17200  -35.55300 1.000 44.38339  ? 9   PRO H CA  1 
ATOM   1788 C C   . PRO B  2 9   ? -2.00000  0.32600   -35.67700 1.000 45.39569  ? 9   PRO H C   1 
ATOM   1789 O O   . PRO B  2 9   ? -3.01400  0.96800   -35.89800 1.000 54.56502  ? 9   PRO H O   1 
ATOM   1790 C CB  . PRO B  2 9   ? -2.73700  -1.72700  -36.78700 1.000 47.52191  ? 9   PRO H CB  1 
ATOM   1791 C CG  . PRO B  2 9   ? -4.19000  -1.49700  -36.56900 1.000 45.92752  ? 9   PRO H CG  1 
ATOM   1792 C CD  . PRO B  2 9   ? -4.40300  -1.64700  -35.09600 1.000 46.86646  ? 9   PRO H CD  1 
ATOM   1793 N N   . GLY B  2 10  ? -0.82400  0.88700   -35.51700 1.000 44.43470  ? 10  GLY H N   1 
ATOM   1794 C CA  . GLY B  2 10  ? -0.67200  2.30800   -35.74100 1.000 45.84812  ? 10  GLY H CA  1 
ATOM   1795 C C   . GLY B  2 10  ? -0.84600  2.71400   -37.18600 1.000 32.66696  ? 10  GLY H C   1 
ATOM   1796 O O   . GLY B  2 10  ? -1.21400  3.83000   -37.47500 1.000 34.62819  ? 10  GLY H O   1 
ATOM   1797 N N   . LEU B  2 11  ? -0.57100  1.79900   -38.08700 1.000 36.85432  ? 11  LEU H N   1 
ATOM   1798 C CA  . LEU B  2 11  ? -0.70100  2.07800   -39.50000 1.000 38.35855  ? 11  LEU H CA  1 
ATOM   1799 C C   . LEU B  2 11  ? -1.50200  1.02500   -40.25100 1.000 40.65001  ? 11  LEU H C   1 
ATOM   1800 O O   . LEU B  2 11  ? -1.27500  -0.15700  -40.09600 1.000 33.87092  ? 11  LEU H O   1 
ATOM   1801 C CB  . LEU B  2 11  ? 0.68600   2.21700   -40.11900 1.000 35.63329  ? 11  LEU H CB  1 
ATOM   1802 C CG  . LEU B  2 11  ? 0.79400   2.59100   -41.59700 1.000 35.50740  ? 11  LEU H CG  1 
ATOM   1803 C CD1 . LEU B  2 11  ? 0.19200   3.95800   -41.85900 1.000 30.81165  ? 11  LEU H CD1 1 
ATOM   1804 C CD2 . LEU B  2 11  ? 2.24700   2.55300   -42.03200 1.000 32.89350  ? 11  LEU H CD2 1 
ATOM   1805 N N   . VAL B  2 12  ? -2.43600  1.47900   -41.05800 1.000 33.88219  ? 12  VAL H N   1 
ATOM   1806 C CA  . VAL B  2 12  ? -3.24100  0.57700   -41.83000 1.000 38.37285  ? 12  VAL H CA  1 
ATOM   1807 C C   . VAL B  2 12  ? -3.37500  1.11500   -43.25900 1.000 45.35419  ? 12  VAL H C   1 
ATOM   1808 O O   . VAL B  2 12  ? -3.49000  2.31000   -43.45400 1.000 42.46775  ? 12  VAL H O   1 
ATOM   1809 C CB  . VAL B  2 12  ? -4.60900  0.35300   -41.17000 1.000 38.35461  ? 12  VAL H CB  1 
ATOM   1810 C CG1 . VAL B  2 12  ? -5.62100  -0.15600  -42.17700 1.000 44.20555  ? 12  VAL H CG1 1 
ATOM   1811 C CG2 . VAL B  2 12  ? -4.48400  -0.60100  -40.00200 1.000 39.91075  ? 12  VAL H CG2 1 
ATOM   1812 N N   . LYS B  2 13  ? -3.31400  0.23400   -44.25300 1.000 39.03240  ? 13  LYS H N   1 
ATOM   1813 C CA  . LYS B  2 13  ? -3.45700  0.64300   -45.63900 1.000 33.81522  ? 13  LYS H CA  1 
ATOM   1814 C C   . LYS B  2 13  ? -4.92800  0.75100   -46.02800 1.000 39.86716  ? 13  LYS H C   1 
ATOM   1815 O O   . LYS B  2 13  ? -5.75400  0.04400   -45.49000 1.000 40.61446  ? 13  LYS H O   1 
ATOM   1816 C CB  . LYS B  2 13  ? -2.73000  -0.32800  -46.54700 1.000 37.98048  ? 13  LYS H CB  1 
ATOM   1817 C CG  . LYS B  2 13  ? -1.50700  -0.96900  -45.91500 1.000 51.21953  ? 13  LYS H CG  1 
ATOM   1818 C CD  . LYS B  2 13  ? -0.70800  -1.77400  -46.92600 0.803 44.90425  ? 13  LYS H CD  1 
ATOM   1819 C CE  . LYS B  2 13  ? 0.02500   -0.87100  -47.90400 1.000 49.44282  ? 13  LYS H CE  1 
ATOM   1820 N NZ  . LYS B  2 13  ? 1.39400   -0.51500  -47.43700 1.000 43.00700  ? 13  LYS H NZ  1 
ATOM   1821 N N   . PRO B  2 14  ? -5.25900  1.66100   -46.95400 1.000 41.43781  ? 14  PRO H N   1 
ATOM   1822 C CA  . PRO B  2 14  ? -6.65300  1.84200   -47.37900 1.000 42.60587  ? 14  PRO H CA  1 
ATOM   1823 C C   . PRO B  2 14  ? -7.30200  0.58300   -47.97200 1.000 43.71151  ? 14  PRO H C   1 
ATOM   1824 O O   . PRO B  2 14  ? -6.57800  -0.27100  -48.41400 1.000 47.12280  ? 14  PRO H O   1 
ATOM   1825 C CB  . PRO B  2 14  ? -6.55900  2.97500   -48.40400 1.000 39.10333  ? 14  PRO H CB  1 
ATOM   1826 C CG  . PRO B  2 14  ? -5.30900  3.71600   -48.01100 1.000 43.22758  ? 14  PRO H CG  1 
ATOM   1827 C CD  . PRO B  2 14  ? -4.35700  2.62600   -47.57600 1.000 39.82818  ? 14  PRO H CD  1 
ATOM   1828 N N   . SER B  2 15  ? -8.68000  0.53600   -47.90500 1.000 39.90519  ? 15  SER H N   1 
ATOM   1829 C CA  . SER B  2 15  ? -9.44800  -0.65900  -48.35400 1.000 47.00234  ? 15  SER H CA  1 
ATOM   1830 C C   . SER B  2 15  ? -9.17000  -1.87500  -47.45800 1.000 44.49532  ? 15  SER H C   1 
ATOM   1831 O O   . SER B  2 15  ? -9.76900  -2.93300  -47.69600 1.000 61.37051  ? 15  SER H O   1 
ATOM   1832 C CB  . SER B  2 15  ? -9.18700  -0.97200  -49.80100 1.000 44.74335  ? 15  SER H CB  1 
ATOM   1833 O OG  . SER B  2 15  ? -8.11300  -1.88900  -49.92900 1.000 51.39257  ? 15  SER H OG  1 
ATOM   1834 N N   . GLU B  2 16  ? -8.26500  -1.75200  -46.50400 1.000 40.65310  ? 16  GLU H N   1 
ATOM   1835 C CA  . GLU B  2 16  ? -7.97100  -2.86000  -45.57100 1.000 37.57714  ? 16  GLU H CA  1 
ATOM   1836 C C   . GLU B  2 16  ? -8.85300  -2.74600  -44.31500 1.000 49.73192  ? 16  GLU H C   1 
ATOM   1837 O O   . GLU B  2 16  ? -9.66600  -1.81600  -44.25100 1.000 44.75938  ? 16  GLU H O   1 
ATOM   1838 C CB  . GLU B  2 16  ? -6.48400  -2.86700  -45.23000 1.000 43.41686  ? 16  GLU H CB  1 
ATOM   1839 C CG  . GLU B  2 16  ? -5.59500  -3.65100  -46.17100 1.000 45.81767  ? 16  GLU H CG  1 
ATOM   1840 C CD  . GLU B  2 16  ? -4.16100  -3.66700  -45.66900 1.000 54.99247  ? 16  GLU H CD  1 
ATOM   1841 O OE1 . GLU B  2 16  ? -3.91100  -3.08600  -44.59500 1.000 56.46185  ? 16  GLU H OE1 1 
ATOM   1842 O OE2 . GLU B  2 16  ? -3.29900  -4.24800  -46.34700 1.000 65.76478  ? 16  GLU H OE2 1 
ATOM   1843 N N   . THR B  2 17  ? -8.68800  -3.66300  -43.37000 1.000 48.48176  ? 17  THR H N   1 
ATOM   1844 C CA  . THR B  2 17  ? -9.51000  -3.73600  -42.17100 1.000 41.76958  ? 17  THR H CA  1 
ATOM   1845 C C   . THR B  2 17  ? -8.72000  -3.26500  -40.95900 1.000 42.85125  ? 17  THR H C   1 
ATOM   1846 O O   . THR B  2 17  ? -7.57600  -3.68400  -40.74700 1.000 37.95312  ? 17  THR H O   1 
ATOM   1847 C CB  . THR B  2 17  ? -10.04300 -5.14800  -41.93800 1.000 40.40238  ? 17  THR H CB  1 
ATOM   1848 O OG1 . THR B  2 17  ? -10.48200 -5.69000  -43.19100 1.000 48.18431  ? 17  THR H OG1 1 
ATOM   1849 C CG2 . THR B  2 17  ? -11.21800 -5.09900  -40.98000 1.000 48.16088  ? 17  THR H CG2 1 
ATOM   1850 N N   . LEU B  2 18  ? -9.34400  -2.37600  -40.19100 1.000 33.42130  ? 18  LEU H N   1 
ATOM   1851 C CA  . LEU B  2 18  ? -8.84300  -1.90500  -38.91000 1.000 39.46935  ? 18  LEU H CA  1 
ATOM   1852 C C   . LEU B  2 18  ? -9.31400  -2.79600  -37.77100 1.000 35.33150  ? 18  LEU H C   1 
ATOM   1853 O O   . LEU B  2 18  ? -10.52000 -2.97300  -37.55600 1.000 35.16797  ? 18  LEU H O   1 
ATOM   1854 C CB  . LEU B  2 18  ? -9.29700  -0.46400  -38.64600 1.000 37.69336  ? 18  LEU H CB  1 
ATOM   1855 C CG  . LEU B  2 18  ? -8.70600  0.28600   -37.42700 1.000 30.26053  ? 18  LEU H CG  1 
ATOM   1856 C CD1 . LEU B  2 18  ? -7.25500  -0.04700  -37.13500 1.000 39.83716  ? 18  LEU H CD1 1 
ATOM   1857 C CD2 . LEU B  2 18  ? -8.89800  1.80600   -37.53400 1.000 38.47836  ? 18  LEU H CD2 1 
ATOM   1858 N N   . SER B  2 19  ? -8.36100  -3.31100  -37.02700 1.000 31.58412  ? 19  SER H N   1 
ATOM   1859 C CA  . SER B  2 19  ? -8.65200  -4.08700  -35.84000 1.000 36.92680  ? 19  SER H CA  1 
ATOM   1860 C C   . SER B  2 19  ? -8.05200  -3.39900  -34.62100 1.000 43.79968  ? 19  SER H C   1 
ATOM   1861 O O   . SER B  2 19  ? -6.91100  -2.91700  -34.66100 1.000 33.40870  ? 19  SER H O   1 
ATOM   1862 C CB  . SER B  2 19  ? -8.10900  -5.49600  -35.99600 1.000 41.32911  ? 19  SER H CB  1 
ATOM   1863 O OG  . SER B  2 19  ? -9.14700  -6.31600  -36.50200 1.000 53.36223  ? 19  SER H OG  1 
ATOM   1864 N N   . LEU B  2 20  ? -8.82900  -3.36800  -33.53300 1.000 39.70456  ? 20  LEU H N   1 
ATOM   1865 C CA  . LEU B  2 20  ? -8.43700  -2.65700  -32.32500 1.000 37.26030  ? 20  LEU H CA  1 
ATOM   1866 C C   . LEU B  2 20  ? -8.95900  -3.39600  -31.09700 1.000 32.94544  ? 20  LEU H C   1 
ATOM   1867 O O   . LEU B  2 20  ? -10.10200 -3.87200  -31.08000 1.000 30.48016  ? 20  LEU H O   1 
ATOM   1868 C CB  . LEU B  2 20  ? -9.00800  -1.23800  -32.35400 1.000 39.99419  ? 20  LEU H CB  1 
ATOM   1869 C CG  . LEU B  2 20  ? -8.23300  -0.11800  -33.05800 1.000 36.32349  ? 20  LEU H CG  1 
ATOM   1870 C CD1 . LEU B  2 20  ? -9.15700  1.06600   -33.05900 1.000 35.48711  ? 20  LEU H CD1 1 
ATOM   1871 C CD2 . LEU B  2 20  ? -6.95200  0.24200   -32.37400 1.000 33.99934  ? 20  LEU H CD2 1 
ATOM   1872 N N   . THR B  2 21  ? -8.14500  -3.40700  -30.04800 1.000 34.57691  ? 21  THR H N   1 
ATOM   1873 C CA  . THR B  2 21  ? -8.37800  -4.24100  -28.87800 1.000 38.17562  ? 21  THR H CA  1 
ATOM   1874 C C   . THR B  2 21  ? -8.26300  -3.40400  -27.60000 1.000 37.28812  ? 21  THR H C   1 
ATOM   1875 O O   . THR B  2 21  ? -7.24700  -2.73300  -27.38000 1.000 39.48097  ? 21  THR H O   1 
ATOM   1876 C CB  . THR B  2 21  ? -7.37700  -5.39600  -28.90700 1.000 35.09556  ? 21  THR H CB  1 
ATOM   1877 O OG1 . THR B  2 21  ? -7.88700  -6.39700  -29.79200 1.000 50.04263  ? 21  THR H OG1 1 
ATOM   1878 C CG2 . THR B  2 21  ? -7.18100  -5.99800  -27.53500 1.000 36.69597  ? 21  THR H CG2 1 
ATOM   1879 N N   . CYS B  2 22  ? -9.30700  -3.43800  -26.76200 1.000 36.60302  ? 22  CYS H N   1 
ATOM   1880 C CA  . CYS B  2 22  ? -9.30000  -2.76700  -25.46000 1.000 34.09196  ? 22  CYS H CA  1 
ATOM   1881 C C   . CYS B  2 22  ? -9.04500  -3.82000  -24.38700 1.000 34.04481  ? 22  CYS H C   1 
ATOM   1882 O O   . CYS B  2 22  ? -9.86400  -4.72900  -24.20800 1.000 37.30512  ? 22  CYS H O   1 
ATOM   1883 C CB  . CYS B  2 22  ? -10.62900 -2.05000  -25.21700 1.000 31.25775  ? 22  CYS H CB  1 
ATOM   1884 S SG  . CYS B  2 22  ? -10.74000 -1.07300  -23.68100 1.000 29.67808  ? 22  CYS H SG  1 
ATOM   1885 N N   . SER B  2 23  ? -7.91800  -3.70900  -23.68400 1.000 29.37281  ? 23  SER H N   1 
ATOM   1886 C CA  . SER B  2 23  ? -7.62200  -4.57700  -22.55300 1.000 34.64197  ? 23  SER H CA  1 
ATOM   1887 C C   . SER B  2 23  ? -8.21400  -3.98700  -21.26800 1.000 41.62949  ? 23  SER H C   1 
ATOM   1888 O O   . SER B  2 23  ? -7.81200  -2.90100  -20.84400 1.000 38.02538  ? 23  SER H O   1 
ATOM   1889 C CB  . SER B  2 23  ? -6.11300  -4.74300  -22.40800 1.000 33.14503  ? 23  SER H CB  1 
ATOM   1890 O OG  . SER B  2 23  ? -5.63000  -5.56800  -23.45700 1.000 48.51731  ? 23  SER H OG  1 
ATOM   1891 N N   . VAL B  2 24  ? -9.18800  -4.68700  -20.69800 1.000 31.49723  ? 24  VAL H N   1 
ATOM   1892 C CA  . VAL B  2 24  ? -9.84400  -4.24900  -19.48500 1.000 35.96692  ? 24  VAL H CA  1 
ATOM   1893 C C   . VAL B  2 24  ? -9.30300  -4.92400  -18.25200 1.000 38.49568  ? 24  VAL H C   1 
ATOM   1894 O O   . VAL B  2 24  ? -9.22100  -6.13600  -18.19600 1.000 43.93407  ? 24  VAL H O   1 
ATOM   1895 C CB  . VAL B  2 24  ? -11.33500 -4.57800  -19.56600 1.000 30.07704  ? 24  VAL H CB  1 
ATOM   1896 C CG1 . VAL B  2 24  ? -12.03900 -4.26400  -18.25800 1.000 31.43744  ? 24  VAL H CG1 1 
ATOM   1897 C CG2 . VAL B  2 24  ? -11.98400 -3.88100  -20.74500 1.000 35.28952  ? 24  VAL H CG2 1 
ATOM   1898 N N   . SER B  2 25  ? -8.93200  -4.15400  -17.25700 1.000 40.53893  ? 25  SER H N   1 
ATOM   1899 C CA  . SER B  2 25  ? -8.47000  -4.71300  -16.00400 1.000 42.92864  ? 25  SER H CA  1 
ATOM   1900 C C   . SER B  2 25  ? -9.27500  -4.16300  -14.84600 1.000 45.81126  ? 25  SER H C   1 
ATOM   1901 O O   . SER B  2 25  ? -9.73500  -3.03700  -14.89500 1.000 43.33248  ? 25  SER H O   1 
ATOM   1902 C CB  . SER B  2 25  ? -7.01600  -4.38100  -15.77400 1.000 45.19488  ? 25  SER H CB  1 
ATOM   1903 O OG  . SER B  2 25  ? -6.17300  -5.18800  -16.57200 1.000 65.92444  ? 25  SER H OG  1 
ATOM   1904 N N   . GLY B  2 26  ? -9.46000  -4.97700  -13.80000 1.000 51.97169  ? 26  GLY H N   1 
ATOM   1905 C CA  . GLY B  2 26  ? -10.18300 -4.53400  -12.58800 1.000 44.28271  ? 26  GLY H CA  1 
ATOM   1906 C C   . GLY B  2 26  ? -11.63500 -4.95700  -12.56500 1.000 37.97991  ? 26  GLY H C   1 
ATOM   1907 O O   . GLY B  2 26  ? -12.21300 -4.99900  -11.47900 1.000 51.23381  ? 26  GLY H O   1 
ATOM   1908 N N   . VAL B  2 27  ? -12.20000 -5.24800  -13.72200 1.000 37.19933  ? 27  VAL H N   1 
ATOM   1909 C CA  . VAL B  2 27  ? -13.63100 -5.63000  -13.81400 1.000 38.82816  ? 27  VAL H CA  1 
ATOM   1910 C C   . VAL B  2 27  ? -13.78100 -6.68800  -14.90900 1.000 39.35484  ? 27  VAL H C   1 
ATOM   1911 O O   . VAL B  2 27  ? -12.93700 -6.73800  -15.80100 1.000 42.28021  ? 27  VAL H O   1 
ATOM   1912 C CB  . VAL B  2 27  ? -14.52600 -4.41300  -14.09800 1.000 43.69026  ? 27  VAL H CB  1 
ATOM   1913 C CG1 . VAL B  2 27  ? -14.69900 -3.52900  -12.87500 1.000 43.32127  ? 27  VAL H CG1 1 
ATOM   1914 C CG2 . VAL B  2 27  ? -14.01100 -3.61000  -15.28100 1.000 34.97856  ? 27  VAL H CG2 1 
ATOM   1915 N N   . SER B  2 28  ? -14.83400 -7.48900  -14.82700 1.000 33.98219  ? 28  SER H N   1 
ATOM   1916 C CA  . SER B  2 28  ? -15.04600 -8.57400  -15.80500 1.000 37.27493  ? 28  SER H CA  1 
ATOM   1917 C C   . SER B  2 28  ? -15.91400 -8.09400  -16.95600 1.000 34.91802  ? 28  SER H C   1 
ATOM   1918 O O   . SER B  2 28  ? -16.92600 -7.45100  -16.70500 1.000 30.35147  ? 28  SER H O   1 
ATOM   1919 C CB  . SER B  2 28  ? -15.65300 -9.79700  -15.16200 1.000 41.18088  ? 28  SER H CB  1 
ATOM   1920 O OG  . SER B  2 28  ? -15.64300 -10.88700 -16.06700 1.000 43.74476  ? 28  SER H OG  1 
ATOM   1921 N N   . VAL B  2 29  ? -15.51200 -8.44500  -18.16700 1.000 34.99941  ? 29  VAL H N   1 
ATOM   1922 C CA  . VAL B  2 29  ? -16.31600 -8.10300  -19.37200 1.000 36.53661  ? 29  VAL H CA  1 
ATOM   1923 C C   . VAL B  2 29  ? -17.58200 -8.94900  -19.35500 1.000 37.43261  ? 29  VAL H C   1 
ATOM   1924 O O   . VAL B  2 29  ? -18.43800 -8.72100  -20.20900 1.000 38.90026  ? 29  VAL H O   1 
ATOM   1925 C CB  . VAL B  2 29  ? -15.48900 -8.34100  -20.65200 1.000 41.18744  ? 29  VAL H CB  1 
ATOM   1926 C CG1 . VAL B  2 29  ? -15.37100 -9.81900  -20.98600 1.000 37.15318  ? 29  VAL H CG1 1 
ATOM   1927 C CG2 . VAL B  2 29  ? -16.03800 -7.55700  -21.82700 1.000 54.29349  ? 29  VAL H CG2 1 
ATOM   1928 N N   . THR B  2 30  ? -17.69400 -9.89500  -18.44400 1.000 33.67137  ? 30  THR H N   1 
ATOM   1929 C CA  . THR B  2 30  ? -18.85800 -10.75700 -18.39500 1.000 41.60575  ? 30  THR H CA  1 
ATOM   1930 C C   . THR B  2 30  ? -20.07200 -10.08400 -17.72600 1.000 40.60498  ? 30  THR H C   1 
ATOM   1931 O O   . THR B  2 30  ? -21.16200 -10.61800 -17.76500 1.000 42.45314  ? 30  THR H O   1 
ATOM   1932 C CB  . THR B  2 30  ? -18.52200 -12.11000 -17.70000 1.000 37.48991  ? 30  THR H CB  1 
ATOM   1933 O OG1 . THR B  2 30  ? -18.18400 -11.88700 -16.33000 1.000 39.70151  ? 30  THR H OG1 1 
ATOM   1934 C CG2 . THR B  2 30  ? -17.36400 -12.78400 -18.39700 1.000 25.91305  ? 30  THR H CG2 1 
ATOM   1935 N N   . SER B  2 31  ? -19.88200 -8.91300  -17.15200 1.000 37.37007  ? 31  SER H N   1 
ATOM   1936 C CA  . SER B  2 31  ? -20.96800 -8.18700  -16.44400 1.000 33.39056  ? 31  SER H CA  1 
ATOM   1937 C C   . SER B  2 31  ? -22.22500 -8.04200  -17.28100 1.000 37.36237  ? 31  SER H C   1 
ATOM   1938 O O   . SER B  2 31  ? -22.11300 -7.88400  -18.49000 1.000 36.86087  ? 31  SER H O   1 
ATOM   1939 C CB  . SER B  2 31  ? -20.52000 -6.81800  -16.01400 1.000 38.61025  ? 31  SER H CB  1 
ATOM   1940 O OG  . SER B  2 31  ? -21.63400 -6.02000  -15.65200 1.000 45.63921  ? 31  SER H OG  1 
ATOM   1941 N N   . ASP B  2 32  ? -23.35900 -7.96900  -16.61800 1.000 35.26946  ? 32  ASP H N   1 
ATOM   1942 C CA  . ASP B  2 32  ? -24.61400 -7.75200  -17.29000 1.000 37.46011  ? 32  ASP H CA  1 
ATOM   1943 C C   . ASP B  2 32  ? -25.06300 -6.30000  -17.18200 1.000 36.07580  ? 32  ASP H C   1 
ATOM   1944 O O   . ASP B  2 32  ? -26.04800 -5.93800  -17.78200 1.000 43.17592  ? 32  ASP H O   1 
ATOM   1945 C CB  . ASP B  2 32  ? -25.67100 -8.64600  -16.65700 1.000 38.97906  ? 32  ASP H CB  1 
ATOM   1946 C CG  . ASP B  2 32  ? -25.97000 -8.27400  -15.21200 1.000 58.60337  ? 32  ASP H CG  1 
ATOM   1947 O OD1 . ASP B  2 32  ? -26.53800 -7.19600  -14.97500 1.000 58.57369  ? 32  ASP H OD1 1 
ATOM   1948 O OD2 . ASP B  2 32  ? -25.64900 -9.06600  -14.30700 1.000 58.91789  ? 32  ASP H OD2 1 
ATOM   1949 N N   . ILE B  2 33  ? -24.33100 -5.48300  -16.44300 1.000 28.91210  ? 33  ILE H N   1 
ATOM   1950 C CA  . ILE B  2 33  ? -24.71900 -4.08500  -16.22100 1.000 37.47160  ? 33  ILE H CA  1 
ATOM   1951 C C   . ILE B  2 33  ? -23.81000 -3.11400  -16.98400 1.000 28.65231  ? 33  ILE H C   1 
ATOM   1952 O O   . ILE B  2 33  ? -24.26800 -2.15700  -17.56900 1.000 27.20184  ? 33  ILE H O   1 
ATOM   1953 C CB  . ILE B  2 33  ? -24.73600 -3.74700  -14.71700 1.000 27.59535  ? 33  ILE H CB  1 
ATOM   1954 C CG1 . ILE B  2 33  ? -25.28400 -2.33800  -14.50100 1.000 34.15416  ? 33  ILE H CG1 1 
ATOM   1955 C CG2 . ILE B  2 33  ? -23.36200 -3.91000  -14.09600 1.000 26.15812  ? 33  ILE H CG2 1 
ATOM   1956 C CD1 . ILE B  2 33  ? -25.62700 -2.03600  -13.06400 1.000 39.80429  ? 33  ILE H CD1 1 
ATOM   1957 N N   . TYR B  2 34  ? -22.53700 -3.40900  -16.98200 1.000 27.93021  ? 34  TYR H N   1 
ATOM   1958 C CA  . TYR B  2 34  ? -21.54500 -2.57000  -17.69200 1.000 28.22711  ? 34  TYR H CA  1 
ATOM   1959 C C   . TYR B  2 34  ? -21.63600 -2.77700  -19.20100 1.000 36.64415  ? 34  TYR H C   1 
ATOM   1960 O O   . TYR B  2 34  ? -21.94800 -3.89100  -19.63600 1.000 32.20311  ? 34  TYR H O   1 
ATOM   1961 C CB  . TYR B  2 34  ? -20.12800 -2.86400  -17.18800 1.000 23.75542  ? 34  TYR H CB  1 
ATOM   1962 C CG  . TYR B  2 34  ? -19.82700 -2.52700  -15.75000 1.000 27.50424  ? 34  TYR H CG  1 
ATOM   1963 C CD1 . TYR B  2 34  ? -20.05000 -1.25800  -15.24600 1.000 24.18671  ? 34  TYR H CD1 1 
ATOM   1964 C CD2 . TYR B  2 34  ? -19.27500 -3.47000  -14.90100 1.000 20.82080  ? 34  TYR H CD2 1 
ATOM   1965 C CE1 . TYR B  2 34  ? -19.75800 -0.94600  -13.93000 1.000 30.63527  ? 34  TYR H CE1 1 
ATOM   1966 C CE2 . TYR B  2 34  ? -18.97400 -3.17500  -13.58300 1.000 25.51878  ? 34  TYR H CE2 1 
ATOM   1967 C CZ  . TYR B  2 34  ? -19.22000 -1.90700  -13.09300 1.000 24.17983  ? 34  TYR H CZ  1 
ATOM   1968 O OH  . TYR B  2 34  ? -18.92800 -1.60000  -11.79800 1.000 26.09014  ? 34  TYR H OH  1 
ATOM   1969 N N   . TYR B  2 35  ? -21.42100 -1.70500  -19.96200 1.000 31.22443  ? 35  TYR H N   1 
ATOM   1970 C CA  . TYR B  2 35  ? -21.36500 -1.79800  -21.44100 1.000 34.34263  ? 35  TYR H CA  1 
ATOM   1971 C C   . TYR B  2 35  ? -20.00500 -1.26300  -21.91200 1.000 38.22261  ? 35  TYR H C   1 
ATOM   1972 O O   . TYR B  2 35  ? -19.34000 -0.57500  -21.12700 1.000 32.55552  ? 35  TYR H O   1 
ATOM   1973 C CB  . TYR B  2 35  ? -22.54300 -1.10300  -22.12600 1.000 31.46008  ? 35  TYR H CB  1 
ATOM   1974 C CG  . TYR B  2 35  ? -22.77700 0.32800   -21.73200 1.000 34.50354  ? 35  TYR H CG  1 
ATOM   1975 C CD1 . TYR B  2 35  ? -22.13600 1.36200   -22.39100 1.000 24.70599  ? 35  TYR H CD1 1 
ATOM   1976 C CD2 . TYR B  2 35  ? -23.64900 0.64600   -20.70700 1.000 25.12416  ? 35  TYR H CD2 1 
ATOM   1977 C CE1 . TYR B  2 35  ? -22.35300 2.68000   -22.03600 1.000 28.51472  ? 35  TYR H CE1 1 
ATOM   1978 C CE2 . TYR B  2 35  ? -23.87400 1.95900   -20.33700 1.000 24.78092  ? 35  TYR H CE2 1 
ATOM   1979 C CZ  . TYR B  2 35  ? -23.22300 2.97800   -21.00500 1.000 28.50658  ? 35  TYR H CZ  1 
ATOM   1980 O OH  . TYR B  2 35  ? -23.43900 4.27200   -20.64900 1.000 26.24696  ? 35  TYR H OH  1 
ATOM   1981 N N   . TRP B  2 36  A -19.62900 -1.56900  -23.14500 1.000 27.46349  ? 35  TRP H N   1 
ATOM   1982 C CA  . TRP B  2 36  A -18.33100 -1.23200  -23.71200 1.000 28.16102  ? 35  TRP H CA  1 
ATOM   1983 C C   . TRP B  2 36  A -18.49800 -0.44300  -24.99800 1.000 28.26740  ? 35  TRP H C   1 
ATOM   1984 O O   . TRP B  2 36  A -19.42700 -0.68000  -25.78000 1.000 27.01755  ? 35  TRP H O   1 
ATOM   1985 C CB  . TRP B  2 36  A -17.49900 -2.47900  -23.89400 1.000 29.51944  ? 35  TRP H CB  1 
ATOM   1986 C CG  . TRP B  2 36  A -17.75300 -3.35800  -22.72800 1.000 31.53316  ? 35  TRP H CG  1 
ATOM   1987 C CD1 . TRP B  2 36  A -18.70900 -4.33400  -22.61500 1.000 35.36117  ? 35  TRP H CD1 1 
ATOM   1988 C CD2 . TRP B  2 36  A -17.04100 -3.34700  -21.47800 1.000 29.13095  ? 35  TRP H CD2 1 
ATOM   1989 N NE1 . TRP B  2 36  A -18.63500 -4.91900  -21.36000 1.000 31.01057  ? 35  TRP H NE1 1 
ATOM   1990 C CE2 . TRP B  2 36  A -17.62600 -4.33100  -20.64900 1.000 26.05644  ? 35  TRP H CE2 1 
ATOM   1991 C CE3 . TRP B  2 36  A -15.97600 -2.59400  -20.97700 1.000 28.37698  ? 35  TRP H CE3 1 
ATOM   1992 C CZ2 . TRP B  2 36  A -17.18300 -4.58400  -19.36100 1.000 31.59373  ? 35  TRP H CZ2 1 
ATOM   1993 C CZ3 . TRP B  2 36  A -15.52800 -2.85800  -19.67700 1.000 28.69135  ? 35  TRP H CZ3 1 
ATOM   1994 C CH2 . TRP B  2 36  A -16.13200 -3.84500  -18.89400 1.000 30.61577  ? 35  TRP H CH2 1 
ATOM   1995 N N   . THR B  2 37  B -17.61800 0.53300   -25.17200 1.000 21.56679  ? 35  THR H N   1 
ATOM   1996 C CA  . THR B  2 37  B -17.81400 1.58000   -26.16000 1.000 28.52696  ? 35  THR H CA  1 
ATOM   1997 C C   . THR B  2 37  B -16.51300 1.87400   -26.87600 1.000 18.67541  ? 35  THR H C   1 
ATOM   1998 O O   . THR B  2 37  B -15.42600 1.71000   -26.31400 1.000 23.45600  ? 35  THR H O   1 
ATOM   1999 C CB  . THR B  2 37  B -18.32600 2.83100   -25.47800 1.000 31.05368  ? 35  THR H CB  1 
ATOM   2000 O OG1 . THR B  2 37  B -19.61000 2.52700   -24.90300 1.000 27.74574  ? 35  THR H OG1 1 
ATOM   2001 C CG2 . THR B  2 37  B -18.46700 3.96800   -26.47400 1.000 27.27365  ? 35  THR H CG2 1 
ATOM   2002 N N   . TRP B  2 38  ? -16.63200 2.25800   -28.14400 1.000 21.95677  ? 36  TRP H N   1 
ATOM   2003 C CA  . TRP B  2 38  ? -15.52100 2.81400   -28.90000 1.000 21.74344  ? 36  TRP H CA  1 
ATOM   2004 C C   . TRP B  2 38  ? -15.89300 4.22100   -29.31400 1.000 21.93406  ? 36  TRP H C   1 
ATOM   2005 O O   . TRP B  2 38  ? -17.03100 4.48300   -29.70500 1.000 23.04308  ? 36  TRP H O   1 
ATOM   2006 C CB  . TRP B  2 38  ? -15.16300 1.98000   -30.15900 1.000 23.28372  ? 36  TRP H CB  1 
ATOM   2007 C CG  . TRP B  2 38  ? -14.48200 0.74300   -29.78300 1.000 22.93146  ? 36  TRP H CG  1 
ATOM   2008 C CD1 . TRP B  2 38  ? -15.06000 -0.49300  -29.58900 1.000 24.50592  ? 36  TRP H CD1 1 
ATOM   2009 C CD2 . TRP B  2 38  ? -13.08800 0.58300   -29.50100 1.000 22.88460  ? 36  TRP H CD2 1 
ATOM   2010 N NE1 . TRP B  2 38  ? -14.10200 -1.41000  -29.17900 1.000 25.68144  ? 36  TRP H NE1 1 
ATOM   2011 C CE2 . TRP B  2 38  ? -12.88400 -0.78300  -29.13700 1.000 30.43607  ? 36  TRP H CE2 1 
ATOM   2012 C CE3 . TRP B  2 38  ? -11.98900 1.44900   -29.52600 1.000 23.78846  ? 36  TRP H CE3 1 
ATOM   2013 C CZ2 . TRP B  2 38  ? -11.63000 -1.29200  -28.81900 1.000 24.94000  ? 36  TRP H CZ2 1 
ATOM   2014 C CZ3 . TRP B  2 38  ? -10.75000 0.95200   -29.19200 1.000 27.51907  ? 36  TRP H CZ3 1 
ATOM   2015 C CH2 . TRP B  2 38  ? -10.57500 -0.42000  -28.84200 1.000 28.44278  ? 36  TRP H CH2 1 
ATOM   2016 N N   . ILE B  2 39  ? -14.92900 5.13000   -29.22500 1.000 20.65662  ? 37  ILE H N   1 
ATOM   2017 C CA  . ILE B  2 39  ? -15.13800 6.52800   -29.69600 1.000 21.42590  ? 37  ILE H CA  1 
ATOM   2018 C C   . ILE B  2 39  ? -13.89700 6.92700   -30.49200 1.000 20.82176  ? 37  ILE H C   1 
ATOM   2019 O O   . ILE B  2 39  ? -12.83300 6.36500   -30.23200 1.000 20.10769  ? 37  ILE H O   1 
ATOM   2020 C CB  . ILE B  2 39  ? -15.42500 7.50900   -28.54400 1.000 17.75501  ? 37  ILE H CB  1 
ATOM   2021 C CG1 . ILE B  2 39  ? -16.55100 7.00800   -27.63500 1.000 21.62137  ? 37  ILE H CG1 1 
ATOM   2022 C CG2 . ILE B  2 39  ? -15.70400 8.90700   -29.06800 1.000 23.16581  ? 37  ILE H CG2 1 
ATOM   2023 C CD1 . ILE B  2 39  ? -16.06600 6.41500   -26.33600 1.000 22.75873  ? 37  ILE H CD1 1 
ATOM   2024 N N   . ARG B  2 40  ? -13.93100 7.83500   -31.34200 1.000 18.28577  ? 38  ARG H N   1 
ATOM   2025 C CA  . ARG B  2 40  ? -12.76800 8.24400   -32.17300 1.000 25.58821  ? 38  ARG H CA  1 
ATOM   2026 C C   . ARG B  2 40  ? -12.68500 9.76100   -32.33100 1.000 23.87474  ? 38  ARG H C   1 
ATOM   2027 O O   . ARG B  2 40  ? -13.73200 10.40800  -32.38500 1.000 23.89144  ? 38  ARG H O   1 
ATOM   2028 C CB  . ARG B  2 40  ? -12.83700 7.59400   -33.56400 1.000 24.33200  ? 38  ARG H CB  1 
ATOM   2029 C CG  . ARG B  2 40  ? -13.64700 8.31500   -34.62800 1.000 32.03702  ? 38  ARG H CG  1 
ATOM   2030 C CD  . ARG B  2 40  ? -13.37300 7.58300   -35.93200 1.000 26.65753  ? 38  ARG H CD  1 
ATOM   2031 N NE  . ARG B  2 40  ? -14.32400 7.82600   -37.00100 1.000 24.92463  ? 38  ARG H NE  1 
ATOM   2032 C CZ  . ARG B  2 40  ? -14.40600 7.11500   -38.12000 1.000 29.39132  ? 38  ARG H CZ  1 
ATOM   2033 N NH1 . ARG B  2 40  ? -13.59600 6.09300   -38.32300 1.000 21.02881  ? 38  ARG H NH1 1 
ATOM   2034 N NH2 . ARG B  2 40  ? -15.30500 7.42800   -39.03200 1.000 24.48268  ? 38  ARG H NH2 1 
ATOM   2035 N N   . GLN B  2 41  ? -11.55200 10.27500  -32.45100 1.000 23.37743  ? 39  GLN H N   1 
ATOM   2036 C CA  . GLN B  2 41  ? -11.27900 11.71700  -32.66000 1.000 25.56454  ? 39  GLN H CA  1 
ATOM   2037 C C   . GLN B  2 41  ? -10.42400 11.86000  -33.92100 1.000 19.19249  ? 39  GLN H C   1 
ATOM   2038 O O   . GLN B  2 41  ? -9.22300  11.61200  -33.86900 1.000 16.43493  ? 39  GLN H O   1 
ATOM   2039 C CB  . GLN B  2 41  ? -10.57700 12.38800  -31.48400 1.000 26.77000  ? 39  GLN H CB  1 
ATOM   2040 C CG  . GLN B  2 41  ? -10.25700 13.85100  -31.75400 1.000 27.02820  ? 39  GLN H CG  1 
ATOM   2041 C CD  . GLN B  2 41  ? -9.98900  14.65400  -30.50500 1.000 22.65644  ? 39  GLN H CD  1 
ATOM   2042 O OE1 . GLN B  2 41  ? -9.23400  14.24700  -29.63000 1.000 23.30905  ? 39  GLN H OE1 1 
ATOM   2043 N NE2 . GLN B  2 41  ? -10.60200 15.82000  -30.42400 1.000 25.15661  ? 39  GLN H NE2 1 
ATOM   2044 N N   . PRO B  2 42  ? -11.05400 12.21900  -35.04500 1.000 22.65834  ? 40  PRO H N   1 
ATOM   2045 C CA  . PRO B  2 42  ? -10.31000 12.46700  -36.26600 1.000 32.64885  ? 40  PRO H CA  1 
ATOM   2046 C C   . PRO B  2 42  ? -9.36200  13.65800  -36.04400 1.000 36.50296  ? 40  PRO H C   1 
ATOM   2047 O O   . PRO B  2 42  ? -9.66600  14.51300  -35.25900 1.000 25.55460  ? 40  PRO H O   1 
ATOM   2048 C CB  . PRO B  2 42  ? -11.40300 12.80500  -37.27600 1.000 26.60227  ? 40  PRO H CB  1 
ATOM   2049 C CG  . PRO B  2 42  ? -12.68000 12.28400  -36.67300 1.000 26.44271  ? 40  PRO H CG  1 
ATOM   2050 C CD  . PRO B  2 42  ? -12.48700 12.42900  -35.18400 1.000 22.06345  ? 40  PRO H CD  1 
ATOM   2051 N N   . PRO B  2 43  ? -8.21100  13.69500  -36.73700 1.000 34.51993  ? 41  PRO H N   1 
ATOM   2052 C CA  . PRO B  2 43  ? -7.26700  14.79100  -36.60300 1.000 31.24546  ? 41  PRO H CA  1 
ATOM   2053 C C   . PRO B  2 43  ? -7.95200  16.13100  -36.88200 1.000 25.38018  ? 41  PRO H C   1 
ATOM   2054 O O   . PRO B  2 43  ? -8.63800  16.25400  -37.85300 1.000 31.55059  ? 41  PRO H O   1 
ATOM   2055 C CB  . PRO B  2 43  ? -6.18500  14.48900  -37.64700 1.000 41.59002  ? 41  PRO H CB  1 
ATOM   2056 C CG  . PRO B  2 43  ? -6.29700  13.00100  -37.87700 1.000 42.32574  ? 41  PRO H CG  1 
ATOM   2057 C CD  . PRO B  2 43  ? -7.76700  12.69300  -37.70400 1.000 32.97382  ? 41  PRO H CD  1 
ATOM   2058 N N   . GLY B  2 44  ? -7.76800  17.07600  -35.97100 1.000 27.35851  ? 42  GLY H N   1 
ATOM   2059 C CA  . GLY B  2 44  ? -8.40300  18.35500  -36.14200 1.000 31.51192  ? 42  GLY H CA  1 
ATOM   2060 C C   . GLY B  2 44  ? -9.86900  18.43200  -35.80300 1.000 31.80756  ? 42  GLY H C   1 
ATOM   2061 O O   . GLY B  2 44  ? -10.48100 19.46900  -35.95100 1.000 37.64070  ? 42  GLY H O   1 
ATOM   2062 N N   . LYS B  2 45  ? -10.43400 17.34500  -35.34300 1.000 25.76624  ? 43  LYS H N   1 
ATOM   2063 C CA  . LYS B  2 45  ? -11.85700 17.36500  -35.10100 1.000 26.36746  ? 43  LYS H CA  1 
ATOM   2064 C C   . LYS B  2 45  ? -12.24700 16.99500  -33.70400 1.000 19.62529  ? 43  LYS H C   1 
ATOM   2065 O O   . LYS B  2 45  ? -11.43500 16.92800  -32.82500 1.000 23.76119  ? 43  LYS H O   1 
ATOM   2066 C CB  . LYS B  2 45  ? -12.56600 16.50200  -36.12800 1.000 34.46501  ? 43  LYS H CB  1 
ATOM   2067 C CG  . LYS B  2 45  ? -12.59000 17.14900  -37.49700 1.000 40.52438  ? 43  LYS H CG  1 
ATOM   2068 C CD  . LYS B  2 45  ? -12.36200 16.12700  -38.58700 1.000 49.55580  ? 43  LYS H CD  1 
ATOM   2069 C CE  . LYS B  2 45  ? -13.56100 15.20900  -38.71900 1.000 55.12850  ? 43  LYS H CE  1 
ATOM   2070 N NZ  . LYS B  2 45  ? -13.24000 14.05500  -39.59700 1.000 62.36761  ? 43  LYS H NZ  1 
ATOM   2071 N N   . GLY B  2 46  ? -13.52000 16.80900  -33.52200 1.000 24.15020  ? 44  GLY H N   1 
ATOM   2072 C CA  . GLY B  2 46  ? -14.00800 16.48500  -32.21800 1.000 25.27259  ? 44  GLY H CA  1 
ATOM   2073 C C   . GLY B  2 46  ? -14.20900 15.01500  -31.94700 1.000 33.46180  ? 44  GLY H C   1 
ATOM   2074 O O   . GLY B  2 46  ? -13.43200 14.19200  -32.39300 1.000 36.15873  ? 44  GLY H O   1 
ATOM   2075 N N   . LEU B  2 47  ? -15.25800 14.69300  -31.21400 1.000 34.52921  ? 45  LEU H N   1 
ATOM   2076 C CA  . LEU B  2 47  ? -15.43600 13.31700  -30.79600 1.000 32.24073  ? 45  LEU H CA  1 
ATOM   2077 C C   . LEU B  2 47  ? -16.60800 12.64500  -31.50100 1.000 29.55224  ? 45  LEU H C   1 
ATOM   2078 O O   . LEU B  2 47  ? -17.70600 13.14700  -31.44900 1.000 34.43893  ? 45  LEU H O   1 
ATOM   2079 C CB  . LEU B  2 47  ? -15.51100 13.20700  -29.26400 1.000 25.32092  ? 45  LEU H CB  1 
ATOM   2080 C CG  . LEU B  2 47  ? -14.30700 13.46000  -28.36500 1.000 26.09950  ? 45  LEU H CG  1 
ATOM   2081 C CD1 . LEU B  2 47  ? -14.73600 13.48700  -26.91100 1.000 25.93703  ? 45  LEU H CD1 1 
ATOM   2082 C CD2 . LEU B  2 47  ? -13.22600 12.42300  -28.57300 1.000 30.76049  ? 45  LEU H CD2 1 
ATOM   2083 N N   . GLU B  2 48  ? -16.32000 11.51500  -32.11500 1.000 28.02425  ? 46  GLU H N   1 
ATOM   2084 C CA  . GLU B  2 48  ? -17.34000 10.79300  -32.83100 1.000 34.87371  ? 46  GLU H CA  1 
ATOM   2085 C C   . GLU B  2 48  ? -17.58600 9.41200   -32.22800 1.000 28.37472  ? 46  GLU H C   1 
ATOM   2086 O O   . GLU B  2 48  ? -16.67300 8.63400   -32.07000 1.000 25.37389  ? 46  GLU H O   1 
ATOM   2087 C CB  . GLU B  2 48  ? -16.98900 10.65800  -34.30400 1.000 33.60612  ? 46  GLU H CB  1 
ATOM   2088 C CG  . GLU B  2 48  ? -17.99900 9.80300   -35.07100 1.000 39.47797  ? 46  GLU H CG  1 
ATOM   2089 C CD  . GLU B  2 48  ? -17.58800 9.44700   -36.49200 1.000 44.10722  ? 46  GLU H CD  1 
ATOM   2090 O OE1 . GLU B  2 48  ? -16.38600 9.30400   -36.76300 1.000 40.55639  ? 46  GLU H OE1 1 
ATOM   2091 O OE2 . GLU B  2 48  ? -18.48400 9.28800   -37.34300 1.000 42.61630  ? 46  GLU H OE2 1 
ATOM   2092 N N   . TRP B  2 49  ? -18.83200 9.14100   -31.90600 1.000 29.15217  ? 47  TRP H N   1 
ATOM   2093 C CA  . TRP B  2 49  ? -19.19700 7.86700   -31.33200 1.000 32.55010  ? 47  TRP H CA  1 
ATOM   2094 C C   . TRP B  2 49  ? -19.22300 6.75800   -32.38000 1.000 27.13943  ? 47  TRP H C   1 
ATOM   2095 O O   . TRP B  2 49  ? -19.74200 6.94300   -33.45500 1.000 32.40942  ? 47  TRP H O   1 
ATOM   2096 C CB  . TRP B  2 49  ? -20.53800 8.00500   -30.67800 1.000 26.62466  ? 47  TRP H CB  1 
ATOM   2097 C CG  . TRP B  2 49  ? -20.99800 6.84400   -29.88100 1.000 35.46523  ? 47  TRP H CG  1 
ATOM   2098 C CD1 . TRP B  2 49  ? -20.59500 6.49700   -28.63400 1.000 26.18141  ? 47  TRP H CD1 1 
ATOM   2099 C CD2 . TRP B  2 49  ? -21.99500 5.89800   -30.26100 1.000 35.20566  ? 47  TRP H CD2 1 
ATOM   2100 N NE1 . TRP B  2 49  ? -21.26900 5.38200   -28.21200 1.000 33.29534  ? 47  TRP H NE1 1 
ATOM   2101 C CE2 . TRP B  2 49  ? -22.13800 4.99400   -29.19700 1.000 35.99908  ? 47  TRP H CE2 1 
ATOM   2102 C CE3 . TRP B  2 49  ? -22.78000 5.72600   -31.40200 1.000 29.39084  ? 47  TRP H CE3 1 
ATOM   2103 C CZ2 . TRP B  2 49  ? -23.02900 3.93000   -29.24100 1.000 37.38856  ? 47  TRP H CZ2 1 
ATOM   2104 C CZ3 . TRP B  2 49  ? -23.66300 4.67300   -31.44300 1.000 40.91871  ? 47  TRP H CZ3 1 
ATOM   2105 C CH2 . TRP B  2 49  ? -23.78200 3.78700   -30.37000 1.000 36.45005  ? 47  TRP H CH2 1 
ATOM   2106 N N   . ILE B  2 50  ? -18.63300 5.62700   -32.05200 1.000 23.61133  ? 48  ILE H N   1 
ATOM   2107 C CA  . ILE B  2 50  ? -18.59700 4.50300   -32.97700 1.000 26.81470  ? 48  ILE H CA  1 
ATOM   2108 C C   . ILE B  2 50  ? -19.70500 3.53400   -32.61300 1.000 33.36108  ? 48  ILE H C   1 
ATOM   2109 O O   . ILE B  2 50  ? -20.55500 3.26700   -33.43400 1.000 38.75304  ? 48  ILE H O   1 
ATOM   2110 C CB  . ILE B  2 50  ? -17.21600 3.84200   -33.00500 1.000 25.34486  ? 48  ILE H CB  1 
ATOM   2111 C CG1 . ILE B  2 50  ? -16.20900 4.79400   -33.65600 1.000 24.67165  ? 48  ILE H CG1 1 
ATOM   2112 C CG2 . ILE B  2 50  ? -17.26000 2.51600   -33.73800 1.000 27.14491  ? 48  ILE H CG2 1 
ATOM   2113 C CD1 . ILE B  2 50  ? -14.77600 4.33600   -33.55900 1.000 21.58824  ? 48  ILE H CD1 1 
ATOM   2114 N N   . GLY B  2 51  ? -19.70600 3.03600   -31.39100 1.000 32.48911  ? 49  GLY H N   1 
ATOM   2115 C CA  . GLY B  2 51  ? -20.78300 2.19900   -30.92400 1.000 28.64106  ? 49  GLY H CA  1 
ATOM   2116 C C   . GLY B  2 51  ? -20.61700 1.53200   -29.57500 1.000 34.41844  ? 49  GLY H C   1 
ATOM   2117 O O   . GLY B  2 51  ? -19.61500 1.72400   -28.90300 1.000 29.11748  ? 49  GLY H O   1 
ATOM   2118 N N   . TYR B  2 52  ? -21.59000 0.72900   -29.19800 1.000 28.44527  ? 50  TYR H N   1 
ATOM   2119 C CA  . TYR B  2 52  ? -21.52700 -0.01800  -27.93600 1.000 32.48768  ? 50  TYR H CA  1 
ATOM   2120 C C   . TYR B  2 52  ? -21.84100 -1.50400  -28.13500 1.000 29.92142  ? 50  TYR H C   1 
ATOM   2121 O O   . TYR B  2 52  ? -22.54800 -1.90000  -29.06400 1.000 31.28376  ? 50  TYR H O   1 
ATOM   2122 C CB  . TYR B  2 52  ? -22.48600 0.59300   -26.89500 1.000 29.29233  ? 50  TYR H CB  1 
ATOM   2123 C CG  . TYR B  2 52  ? -23.97800 0.32200   -27.07800 1.000 25.54454  ? 50  TYR H CG  1 
ATOM   2124 C CD1 . TYR B  2 52  ? -24.53100 -0.93800  -26.83500 1.000 35.46063  ? 50  TYR H CD1 1 
ATOM   2125 C CD2 . TYR B  2 52  ? -24.84500 1.33300   -27.47500 1.000 30.34012  ? 50  TYR H CD2 1 
ATOM   2126 C CE1 . TYR B  2 52  ? -25.90800 -1.16700  -26.98500 1.000 30.35309  ? 50  TYR H CE1 1 
ATOM   2127 C CE2 . TYR B  2 52  ? -26.20100 1.10800   -27.61900 1.000 30.44401  ? 50  TYR H CE2 1 
ATOM   2128 C CZ  . TYR B  2 52  ? -26.71800 -0.14800  -27.36700 1.000 32.16101  ? 50  TYR H CZ  1 
ATOM   2129 O OH  . TYR B  2 52  ? -28.06300 -0.37200  -27.50600 1.000 34.11728  ? 50  TYR H OH  1 
ATOM   2130 N N   . ILE B  2 53  ? -21.39900 -2.27900  -27.16500 1.000 30.58439  ? 51  ILE H N   1 
ATOM   2131 C CA  . ILE B  2 53  ? -21.68600 -3.69200  -27.13900 1.000 34.18775  ? 51  ILE H CA  1 
ATOM   2132 C C   . ILE B  2 53  ? -21.92400 -4.11500  -25.67400 1.000 44.49513  ? 51  ILE H C   1 
ATOM   2133 O O   . ILE B  2 53  ? -21.25900 -3.60100  -24.77800 1.000 32.83660  ? 51  ILE H O   1 
ATOM   2134 C CB  . ILE B  2 53  ? -20.55900 -4.52800  -27.74300 1.000 32.85853  ? 51  ILE H CB  1 
ATOM   2135 C CG1 . ILE B  2 53  ? -20.96200 -6.00400  -27.75800 1.000 34.08209  ? 51  ILE H CG1 1 
ATOM   2136 C CG2 . ILE B  2 53  ? -19.26200 -4.34100  -26.97600 1.000 28.49073  ? 51  ILE H CG2 1 
ATOM   2137 C CD1 . ILE B  2 53  ? -20.09400 -6.86700  -28.64000 1.000 38.24629  ? 51  ILE H CD1 1 
ATOM   2138 N N   . PHE B  2 54  ? -22.85300 -5.03400  -25.42300 1.000 45.42909  ? 52  PHE H N   1 
ATOM   2139 C CA  . PHE B  2 54  ? -23.16100 -5.56900  -24.09200 1.000 39.93345  ? 52  PHE H CA  1 
ATOM   2140 C C   . PHE B  2 54  ? -22.83600 -7.07200  -24.15000 1.000 43.91900  ? 52  PHE H C   1 
ATOM   2141 O O   . PHE B  2 54  ? -22.92900 -7.66600  -25.20700 1.000 35.49086  ? 52  PHE H O   1 
ATOM   2142 C CB  . PHE B  2 54  ? -24.63100 -5.43200  -23.78700 1.000 35.11629  ? 52  PHE H CB  1 
ATOM   2143 C CG  . PHE B  2 54  ? -25.05500 -4.10300  -23.24200 1.000 38.91850  ? 52  PHE H CG  1 
ATOM   2144 C CD1 . PHE B  2 54  ? -25.09700 -3.88400  -21.88100 1.000 33.87394  ? 52  PHE H CD1 1 
ATOM   2145 C CD2 . PHE B  2 54  ? -25.49700 -3.10700  -24.08500 1.000 37.42038  ? 52  PHE H CD2 1 
ATOM   2146 C CE1 . PHE B  2 54  ? -25.52300 -2.67600  -21.37200 1.000 37.52896  ? 52  PHE H CE1 1 
ATOM   2147 C CE2 . PHE B  2 54  ? -25.92600 -1.89300  -23.58500 1.000 40.56768  ? 52  PHE H CE2 1 
ATOM   2148 C CZ  . PHE B  2 54  ? -25.93900 -1.67600  -22.22500 1.000 34.27673  ? 52  PHE H CZ  1 
ATOM   2149 N N   . TYR B  2 55  ? -22.48800 -7.70000  -23.03000 1.000 36.94635  ? 53  TYR H N   1 
ATOM   2150 C CA  . TYR B  2 55  ? -22.16600 -9.12000  -23.03800 1.000 47.67226  ? 53  TYR H CA  1 
ATOM   2151 C C   . TYR B  2 55  ? -23.36500 -9.96600  -23.48800 1.000 43.71174  ? 53  TYR H C   1 
ATOM   2152 O O   . TYR B  2 55  ? -23.19100 -11.03900 -24.02400 1.000 40.31390  ? 53  TYR H O   1 
ATOM   2153 C CB  . TYR B  2 55  ? -21.63200 -9.56100  -21.68300 1.000 47.45792  ? 53  TYR H CB  1 
ATOM   2154 C CG  . TYR B  2 55  ? -21.30800 -11.01600 -21.57100 1.000 47.41311  ? 53  TYR H CG  1 
ATOM   2155 C CD1 . TYR B  2 55  ? -20.10500 -11.51300 -22.03300 1.000 44.49570  ? 53  TYR H CD1 1 
ATOM   2156 C CD2 . TYR B  2 55  ? -22.19800 -11.89400 -20.97900 1.000 50.48684  ? 53  TYR H CD2 1 
ATOM   2157 C CE1 . TYR B  2 55  ? -19.80400 -12.84900 -21.92200 1.000 53.73751  ? 53  TYR H CE1 1 
ATOM   2158 C CE2 . TYR B  2 55  ? -21.90600 -13.23000 -20.86300 1.000 50.94141  ? 53  TYR H CE2 1 
ATOM   2159 C CZ  . TYR B  2 55  ? -20.70700 -13.70200 -21.33600 1.000 54.40154  ? 53  TYR H CZ  1 
ATOM   2160 O OH  . TYR B  2 55  ? -20.41600 -15.03600 -21.21900 1.000 65.74890  ? 53  TYR H OH  1 
ATOM   2161 N N   . ASN B  2 56  ? -24.56700 -9.44600  -23.30900 1.000 40.70025  ? 54  ASN H N   1 
ATOM   2162 C CA  . ASN B  2 56  ? -25.75800 -10.14500 -23.75600 1.000 39.09301  ? 54  ASN H CA  1 
ATOM   2163 C C   . ASN B  2 56  ? -25.79100 -10.14900 -25.26700 1.000 41.01299  ? 54  ASN H C   1 
ATOM   2164 O O   . ASN B  2 56  ? -26.66500 -10.74500 -25.85900 1.000 47.30097  ? 54  ASN H O   1 
ATOM   2165 C CB  . ASN B  2 56  ? -27.01600 -9.53900  -23.13300 1.000 40.72987  ? 54  ASN H CB  1 
ATOM   2166 C CG  . ASN B  2 56  ? -27.53900 -8.34200  -23.88600 1.000 46.67837  ? 54  ASN H CG  1 
ATOM   2167 O OD1 . ASN B  2 56  ? -26.83700 -7.74200  -24.68400 1.000 44.62457  ? 54  ASN H OD1 1 
ATOM   2168 N ND2 . ASN B  2 56  ? -28.78800 -7.97900  -23.61500 1.000 48.67720  ? 54  ASN H ND2 1 
ATOM   2169 N N   . GLY B  2 57  ? -24.84600 -9.46800  -25.89200 1.000 46.36369  ? 55  GLY H N   1 
ATOM   2170 C CA  . GLY B  2 57  ? -24.72600 -9.50500  -27.35500 1.000 45.38343  ? 55  GLY H CA  1 
ATOM   2171 C C   . GLY B  2 57  ? -25.46300 -8.34300  -27.96800 1.000 45.09337  ? 55  GLY H C   1 
ATOM   2172 O O   . GLY B  2 57  ? -25.33400 -8.12600  -29.17200 1.000 43.00844  ? 55  GLY H O   1 
ATOM   2173 N N   . ASP B  2 58  ? -26.18300 -7.60600  -27.13400 1.000 36.50488  ? 56  ASP H N   1 
ATOM   2174 C CA  . ASP B  2 58  ? -26.86400 -6.43700  -27.68100 1.000 41.65763  ? 56  ASP H CA  1 
ATOM   2175 C C   . ASP B  2 58  ? -25.84800 -5.35900  -28.06100 1.000 41.89439  ? 56  ASP H C   1 
ATOM   2176 O O   . ASP B  2 58  ? -24.96700 -5.00600  -27.27000 1.000 34.76746  ? 56  ASP H O   1 
ATOM   2177 C CB  . ASP B  2 58  ? -27.85100 -5.90700  -26.65300 1.000 38.73425  ? 56  ASP H CB  1 
ATOM   2178 C CG  . ASP B  2 58  ? -29.16800 -6.65700  -26.68000 1.000 47.75484  ? 56  ASP H CG  1 
ATOM   2179 O OD1 . ASP B  2 58  ? -29.42900 -7.42000  -27.63200 1.000 52.81183  ? 56  ASP H OD1 1 
ATOM   2180 O OD2 . ASP B  2 58  ? -29.93300 -6.51900  -25.72000 1.000 57.37891  ? 56  ASP H OD2 1 
ATOM   2181 N N   . THR B  2 59  ? -25.97900 -4.87100  -29.28900 1.000 38.29771  ? 57  THR H N   1 
ATOM   2182 C CA  . THR B  2 59  ? -25.04600 -3.89500  -29.81200 1.000 38.98518  ? 57  THR H CA  1 
ATOM   2183 C C   . THR B  2 59  ? -25.73800 -2.79700  -30.59400 1.000 36.17240  ? 57  THR H C   1 
ATOM   2184 O O   . THR B  2 59  ? -26.87600 -2.93600  -31.00600 1.000 32.45442  ? 57  THR H O   1 
ATOM   2185 C CB  . THR B  2 59  ? -24.00800 -4.57400  -30.75000 1.000 42.06335  ? 57  THR H CB  1 
ATOM   2186 O OG1 . THR B  2 59  ? -24.61300 -4.86000  -32.01600 1.000 36.48483  ? 57  THR H OG1 1 
ATOM   2187 C CG2 . THR B  2 59  ? -23.45900 -5.84400  -30.13700 1.000 36.53991  ? 57  THR H CG2 1 
ATOM   2188 N N   . ASN B  2 60  ? -25.06400 -1.67500  -30.74900 1.000 29.53911  ? 58  ASN H N   1 
ATOM   2189 C CA  . ASN B  2 60  ? -25.61900 -0.61900  -31.58700 1.000 32.04389  ? 58  ASN H CA  1 
ATOM   2190 C C   . ASN B  2 60  ? -24.43900 0.18600   -32.11200 1.000 42.46672  ? 58  ASN H C   1 
ATOM   2191 O O   . ASN B  2 60  ? -23.50900 0.47800   -31.34700 1.000 32.99008  ? 58  ASN H O   1 
ATOM   2192 C CB  . ASN B  2 60  ? -26.58700 0.27200   -30.79600 1.000 32.28688  ? 58  ASN H CB  1 
ATOM   2193 C CG  . ASN B  2 60  ? -27.22800 1.36400   -31.64300 1.000 40.63031  ? 58  ASN H CG  1 
ATOM   2194 O OD1 . ASN B  2 60  ? -26.80000 2.52200   -31.65200 1.000 41.72155  ? 58  ASN H OD1 1 
ATOM   2195 N ND2 . ASN B  2 60  ? -28.30500 0.99700   -32.33100 1.000 49.40858  ? 58  ASN H ND2 1 
ATOM   2196 N N   . TYR B  2 61  ? -24.47200 0.52200   -33.40500 1.000 37.09393  ? 59  TYR H N   1 
ATOM   2197 C CA  . TYR B  2 61  ? -23.34700 1.11700   -34.10200 1.000 33.20631  ? 59  TYR H CA  1 
ATOM   2198 C C   . TYR B  2 61  ? -23.80000 2.41700   -34.75200 1.000 36.27478  ? 59  TYR H C   1 
ATOM   2199 O O   . TYR B  2 61  ? -24.97000 2.57100   -35.11100 1.000 32.48371  ? 59  TYR H O   1 
ATOM   2200 C CB  . TYR B  2 61  ? -22.80500 0.16800   -35.18200 1.000 42.03827  ? 59  TYR H CB  1 
ATOM   2201 C CG  . TYR B  2 61  ? -22.27900 -1.16100  -34.67100 1.000 35.67028  ? 59  TYR H CG  1 
ATOM   2202 C CD1 . TYR B  2 61  ? -21.45000 -1.23500  -33.55200 1.000 38.36271  ? 59  TYR H CD1 1 
ATOM   2203 C CD2 . TYR B  2 61  ? -22.62300 -2.36100  -35.30900 1.000 35.53452  ? 59  TYR H CD2 1 
ATOM   2204 C CE1 . TYR B  2 61  ? -20.95600 -2.46200  -33.08700 1.000 34.59818  ? 59  TYR H CE1 1 
ATOM   2205 C CE2 . TYR B  2 61  ? -22.13800 -3.59800  -34.84400 1.000 34.92642  ? 59  TYR H CE2 1 
ATOM   2206 C CZ  . TYR B  2 61  ? -21.30700 -3.65200  -33.74600 1.000 35.76747  ? 59  TYR H CZ  1 
ATOM   2207 O OH  . TYR B  2 61  ? -20.81700 -4.88100  -33.30700 1.000 46.86804  ? 59  TYR H OH  1 
ATOM   2208 N N   . ASN B  2 62  ? -22.86600 3.35900   -34.91100 1.000 36.66284  ? 60  ASN H N   1 
ATOM   2209 C CA  . ASN B  2 62  ? -23.20800 4.66100   -35.50900 1.000 31.53416  ? 60  ASN H CA  1 
ATOM   2210 C C   . ASN B  2 62  ? -23.63900 4.50500   -36.96900 1.000 32.62347  ? 60  ASN H C   1 
ATOM   2211 O O   . ASN B  2 62  ? -22.87300 3.95900   -37.78800 1.000 31.65487  ? 60  ASN H O   1 
ATOM   2212 C CB  . ASN B  2 62  ? -22.02900 5.61800   -35.43700 1.000 33.98353  ? 60  ASN H CB  1 
ATOM   2213 C CG  . ASN B  2 62  ? -22.43300 7.07800   -35.68500 1.000 36.77386  ? 60  ASN H CG  1 
ATOM   2214 O OD1 . ASN B  2 62  ? -23.32100 7.36500   -36.50600 1.000 32.78230  ? 60  ASN H OD1 1 
ATOM   2215 N ND2 . ASN B  2 62  ? -21.73600 8.01500   -35.00800 1.000 28.31308  ? 60  ASN H ND2 1 
ATOM   2216 N N   . PRO B  2 63  ? -24.83600 4.96700   -37.37500 1.000 30.65847  ? 61  PRO H N   1 
ATOM   2217 C CA  . PRO B  2 63  ? -25.25100 4.85800   -38.76600 1.000 37.30092  ? 61  PRO H CA  1 
ATOM   2218 C C   . PRO B  2 63  ? -24.22700 5.41000   -39.76600 1.000 45.11665  ? 61  PRO H C   1 
ATOM   2219 O O   . PRO B  2 63  ? -24.09300 4.85700   -40.82300 1.000 45.88716  ? 61  PRO H O   1 
ATOM   2220 C CB  . PRO B  2 63  ? -26.52200 5.70700   -38.81400 1.000 35.37791  ? 61  PRO H CB  1 
ATOM   2221 C CG  . PRO B  2 63  ? -27.08000 5.61500   -37.42100 1.000 36.18659  ? 61  PRO H CG  1 
ATOM   2222 C CD  . PRO B  2 63  ? -25.85600 5.60000   -36.53500 1.000 36.52263  ? 61  PRO H CD  1 
ATOM   2223 N N   . SER B  2 64  ? -23.54000 6.48200   -39.40000 1.000 39.52398  ? 62  SER H N   1 
ATOM   2224 C CA  . SER B  2 64  ? -22.50300 7.08200   -40.26600 1.000 42.40240  ? 62  SER H CA  1 
ATOM   2225 C C   . SER B  2 64  ? -21.51700 6.01600   -40.73400 1.000 39.43972  ? 62  SER H C   1 
ATOM   2226 O O   . SER B  2 64  ? -20.95700 6.17300   -41.81100 1.000 41.12928  ? 62  SER H O   1 
ATOM   2227 C CB  . SER B  2 64  ? -21.77500 8.14900   -39.50700 1.000 37.61363  ? 62  SER H CB  1 
ATOM   2228 O OG  . SER B  2 64  ? -20.99800 7.59400   -38.46100 1.000 41.48946  ? 62  SER H OG  1 
ATOM   2229 N N   . LEU B  2 65  ? -21.28400 4.99900   -39.91400 1.000 32.31583  ? 63  LEU H N   1 
ATOM   2230 C CA  . LEU B  2 65  ? -20.23400 4.02700   -40.28600 1.000 42.74969  ? 63  LEU H CA  1 
ATOM   2231 C C   . LEU B  2 65  ? -20.86100 2.92200   -41.13000 1.000 53.20406  ? 63  LEU H C   1 
ATOM   2232 O O   . LEU B  2 65  ? -20.18400 1.92300   -41.40700 1.000 55.93778  ? 63  LEU H O   1 
ATOM   2233 C CB  . LEU B  2 65  ? -19.56700 3.50600   -39.01700 1.000 46.22807  ? 63  LEU H CB  1 
ATOM   2234 C CG  . LEU B  2 65  ? -18.72900 4.53300   -38.26000 1.000 44.69316  ? 63  LEU H CG  1 
ATOM   2235 C CD1 . LEU B  2 65  ? -18.33800 4.00700   -36.89000 1.000 40.27663  ? 63  LEU H CD1 1 
ATOM   2236 C CD2 . LEU B  2 65  ? -17.49500 4.91700   -39.05900 1.000 35.86218  ? 63  LEU H CD2 1 
ATOM   2237 N N   . LYS B  2 66  ? -22.10500 3.13800   -41.53300 1.000 43.83121  ? 64  LYS H N   1 
ATOM   2238 C CA  . LYS B  2 66  ? -22.77200 2.16200   -42.40900 1.000 53.46036  ? 64  LYS H CA  1 
ATOM   2239 C C   . LYS B  2 66  ? -22.61300 0.79000   -41.77100 1.000 60.35941  ? 64  LYS H C   1 
ATOM   2240 O O   . LYS B  2 66  ? -22.99400 0.61600   -40.60500 1.000 68.74061  ? 64  LYS H O   1 
ATOM   2241 C CB  . LYS B  2 66  ? -22.15900 2.23300   -43.80500 1.000 47.28605  ? 64  LYS H CB  1 
ATOM   2242 C CG  . LYS B  2 66  ? -22.07800 3.62900   -44.40100 1.000 49.75170  ? 64  LYS H CG  1 
ATOM   2243 C CD  . LYS B  2 66  ? -23.41600 4.33600   -44.45800 1.000 56.68407  ? 64  LYS H CD  1 
ATOM   2244 C CE  . LYS B  2 66  ? -23.94200 4.50100   -45.86800 1.000 63.20050  ? 64  LYS H CE  1 
ATOM   2245 N NZ  . LYS B  2 66  ? -25.41900 4.40000   -45.92300 1.000 56.50587  ? 64  LYS H NZ  1 
ATOM   2246 N N   . SER B  2 67  ? -22.03000 -0.12600  -42.51000 1.000 53.87404  ? 65  SER H N   1 
ATOM   2247 C CA  . SER B  2 67  ? -21.92500 -1.49500  -41.99000 1.000 43.79734  ? 65  SER H CA  1 
ATOM   2248 C C   . SER B  2 67  ? -20.47100 -1.92000  -42.08700 1.000 49.45670  ? 65  SER H C   1 
ATOM   2249 O O   . SER B  2 67  ? -20.22400 -3.05800  -42.50700 1.000 53.42116  ? 65  SER H O   1 
ATOM   2250 C CB  . SER B  2 67  ? -22.83100 -2.39100  -42.75000 1.000 53.45188  ? 65  SER H CB  1 
ATOM   2251 O OG  . SER B  2 67  ? -24.18700 -2.06200  -42.49600 1.000 57.70046  ? 65  SER H OG  1 
ATOM   2252 N N   . ARG B  2 68  ? -19.55500 -1.04200  -41.67200 1.000 45.22434  ? 66  ARG H N   1 
ATOM   2253 C CA  . ARG B  2 68  ? -18.14400 -1.49800  -41.65200 1.000 32.22606  ? 66  ARG H CA  1 
ATOM   2254 C C   . ARG B  2 68  ? -17.75400 -1.79500  -40.20400 1.000 37.83813  ? 66  ARG H C   1 
ATOM   2255 O O   . ARG B  2 68  ? -16.61600 -2.19700  -39.99500 1.000 36.27522  ? 66  ARG H O   1 
ATOM   2256 C CB  . ARG B  2 68  ? -17.23200 -0.48500  -42.34700 1.000 43.57705  ? 66  ARG H CB  1 
ATOM   2257 C CG  . ARG B  2 68  ? -17.89300 0.33900   -43.44100 1.000 41.07980  ? 66  ARG H CG  1 
ATOM   2258 C CD  . ARG B  2 68  ? -16.87500 1.23200   -44.12900 1.000 44.72051  ? 66  ARG H CD  1 
ATOM   2259 N NE  . ARG B  2 68  ? -16.69100 2.51600   -43.46600 1.000 38.07177  ? 66  ARG H NE  1 
ATOM   2260 C CZ  . ARG B  2 68  ? -15.53200 2.96900   -43.00500 1.000 37.68425  ? 66  ARG H CZ  1 
ATOM   2261 N NH1 . ARG B  2 68  ? -14.43600 2.24400   -43.12000 1.000 37.01388  ? 66  ARG H NH1 1 
ATOM   2262 N NH2 . ARG B  2 68  ? -15.47000 4.14600   -42.41600 1.000 42.47263  ? 66  ARG H NH2 1 
ATOM   2263 N N   . VAL B  2 69  ? -18.70000 -1.81600  -39.27400 1.000 41.11472  ? 67  VAL H N   1 
ATOM   2264 C CA  . VAL B  2 69  ? -18.41100 -1.81300  -37.83900 1.000 41.25954  ? 67  VAL H CA  1 
ATOM   2265 C C   . VAL B  2 69  ? -18.80400 -3.15300  -37.22200 1.000 39.93497  ? 67  VAL H C   1 
ATOM   2266 O O   . VAL B  2 69  ? -19.94400 -3.60700  -37.38100 1.000 43.64387  ? 67  VAL H O   1 
ATOM   2267 C CB  . VAL B  2 69  ? -19.15400 -0.66800  -37.12100 1.000 48.07801  ? 67  VAL H CB  1 
ATOM   2268 C CG1 . VAL B  2 69  ? -18.40500 0.59300   -37.25800 1.000 42.63027  ? 67  VAL H CG1 1 
ATOM   2269 C CG2 . VAL B  2 69  ? -20.59400 -0.50400  -37.69000 1.000 44.46927  ? 67  VAL H CG2 1 
ATOM   2270 N N   . THR B  2 70  ? -17.87700 -3.73200  -36.46200 1.000 38.35440  ? 68  THR H N   1 
ATOM   2271 C CA  . THR B  2 70  ? -18.02000 -4.95700  -35.69000 1.000 44.49082  ? 68  THR H CA  1 
ATOM   2272 C C   . THR B  2 70  ? -17.35000 -4.74100  -34.35000 1.000 34.43262  ? 68  THR H C   1 
ATOM   2273 O O   . THR B  2 70  ? -16.24900 -4.19100  -34.30400 1.000 39.02810  ? 68  THR H O   1 
ATOM   2274 C CB  . THR B  2 70  ? -17.36100 -6.14200  -36.44200 1.000 38.15619  ? 68  THR H CB  1 
ATOM   2275 O OG1 . THR B  2 70  ? -18.21200 -6.54400  -37.51400 1.000 47.63928  ? 68  THR H OG1 1 
ATOM   2276 C CG2 . THR B  2 70  ? -16.91500 -7.33100  -35.53500 1.000 48.42475  ? 68  THR H CG2 1 
ATOM   2277 N N   . MET B  2 71  ? -18.01000 -5.16000  -33.26400 1.000 39.84339  ? 69  MET H N   1 
ATOM   2278 C CA  . MET B  2 71  ? -17.35000 -5.29200  -31.96400 1.000 44.00384  ? 69  MET H CA  1 
ATOM   2279 C C   . MET B  2 71  ? -17.59000 -6.68900  -31.41600 1.000 43.40184  ? 69  MET H C   1 
ATOM   2280 O O   . MET B  2 71  ? -18.65700 -7.27100  -31.63800 1.000 36.43031  ? 69  MET H O   1 
ATOM   2281 C CB  . MET B  2 71  ? -17.84300 -4.23200  -30.96200 1.000 36.08594  ? 69  MET H CB  1 
ATOM   2282 C CG  . MET B  2 71  ? -17.60200 -2.80900  -31.44600 1.000 31.41628  ? 69  MET H CG  1 
ATOM   2283 S SD  . MET B  2 71  ? -18.41300 -1.48400  -30.50800 1.000 32.26522  ? 69  MET H SD  1 
ATOM   2284 C CE  . MET B  2 71  ? -17.99600 -0.09300  -31.50100 1.000 34.00543  ? 69  MET H CE  1 
ATOM   2285 N N   . SER B  2 72  ? -16.65100 -7.13800  -30.61700 1.000 37.82566  ? 70  SER H N   1 
ATOM   2286 C CA  . SER B  2 72  ? -16.78100 -8.41500  -30.01800 1.000 44.50022  ? 70  SER H CA  1 
ATOM   2287 C C   . SER B  2 72  ? -16.20200 -8.31700  -28.63500 1.000 46.58308  ? 70  SER H C   1 
ATOM   2288 O O   . SER B  2 72  ? -15.61100 -7.29800  -28.29600 1.000 42.06700  ? 70  SER H O   1 
ATOM   2289 C CB  . SER B  2 72  ? -16.00700 -9.42600  -30.84100 1.000 48.11030  ? 70  SER H CB  1 
ATOM   2290 O OG  . SER B  2 72  ? -14.64200 -9.41300  -30.47100 1.000 53.69994  ? 70  SER H OG  1 
ATOM   2291 N N   . ILE B  2 73  ? -16.30700 -9.38600  -27.85500 1.000 47.27298  ? 71  ILE H N   1 
ATOM   2292 C CA  . ILE B  2 73  ? -15.82300 -9.40400  -26.45300 1.000 35.33546  ? 71  ILE H CA  1 
ATOM   2293 C C   . ILE B  2 73  ? -15.16700 -10.76000 -26.25800 1.000 38.18802  ? 71  ILE H C   1 
ATOM   2294 O O   . ILE B  2 73  ? -15.77300 -11.75800 -26.65600 1.000 41.12440  ? 71  ILE H O   1 
ATOM   2295 C CB  . ILE B  2 73  ? -16.98300 -9.18500  -25.46300 1.000 37.77065  ? 71  ILE H CB  1 
ATOM   2296 C CG1 . ILE B  2 73  ? -17.46500 -7.73300  -25.44300 1.000 37.92291  ? 71  ILE H CG1 1 
ATOM   2297 C CG2 . ILE B  2 73  ? -16.59500 -9.67400  -24.07700 1.000 28.43426  ? 71  ILE H CG2 1 
ATOM   2298 C CD1 . ILE B  2 73  ? -18.85000 -7.55400  -24.87300 1.000 30.04709  ? 71  ILE H CD1 1 
ATOM   2299 N N   . ASP B  2 74  ? -13.95800 -10.77300 -25.72500 1.000 42.97564  ? 72  ASP H N   1 
ATOM   2300 C CA  . ASP B  2 74  ? -13.21600 -12.03600 -25.50200 1.000 44.92999  ? 72  ASP H CA  1 
ATOM   2301 C C   . ASP B  2 74  ? -13.17600 -12.30200 -23.99500 1.000 46.35568  ? 72  ASP H C   1 
ATOM   2302 O O   . ASP B  2 74  ? -12.30500 -11.73800 -23.32300 1.000 41.02340  ? 72  ASP H O   1 
ATOM   2303 C CB  . ASP B  2 74  ? -11.84200 -11.98300 -26.16200 1.000 43.30728  ? 72  ASP H CB  1 
ATOM   2304 C CG  . ASP B  2 74  ? -11.02400 -13.24200 -25.97500 1.000 50.38314  ? 72  ASP H CG  1 
ATOM   2305 O OD1 . ASP B  2 74  ? -10.79300 -13.61600 -24.81900 1.000 50.12260  ? 72  ASP H OD1 1 
ATOM   2306 O OD2 . ASP B  2 74  ? -10.62400 -13.82700 -26.99300 1.000 53.45950  ? 72  ASP H OD2 1 
ATOM   2307 N N   . THR B  2 75  ? -14.09800 -13.13400 -23.51200 1.000 36.66678  ? 73  THR H N   1 
ATOM   2308 C CA  . THR B  2 75  ? -14.18700 -13.45700 -22.07100 1.000 33.71126  ? 73  THR H CA  1 
ATOM   2309 C C   . THR B  2 75  ? -12.84900 -14.02100 -21.62300 1.000 32.14019  ? 73  THR H C   1 
ATOM   2310 O O   . THR B  2 75  ? -12.41500 -13.70000 -20.51300 1.000 39.43269  ? 73  THR H O   1 
ATOM   2311 C CB  . THR B  2 75  ? -15.35200 -14.43100 -21.86500 1.000 37.25033  ? 73  THR H CB  1 
ATOM   2312 O OG1 . THR B  2 75  ? -14.99400 -15.67400 -22.46400 1.000 56.15384  ? 73  THR H OG1 1 
ATOM   2313 C CG2 . THR B  2 75  ? -16.64600 -13.93600 -22.46800 1.000 33.93931  ? 73  THR H CG2 1 
ATOM   2314 N N   . SER B  2 76  ? -12.19200 -14.80900 -22.47000 1.000 39.67811  ? 74  SER H N   1 
ATOM   2315 C CA  . SER B  2 76  ? -10.91600 -15.47900 -22.09500 1.000 38.63847  ? 74  SER H CA  1 
ATOM   2316 C C   . SER B  2 76  ? -9.84000  -14.45200 -21.75400 1.000 45.30564  ? 74  SER H C   1 
ATOM   2317 O O   . SER B  2 76  ? -9.11200  -14.68300 -20.78900 1.000 41.71664  ? 74  SER H O   1 
ATOM   2318 C CB  . SER B  2 76  ? -10.45100 -16.42900 -23.17200 1.000 44.69994  ? 74  SER H CB  1 
ATOM   2319 O OG  . SER B  2 76  ? -10.02100 -15.74500 -24.33600 1.000 46.77474  ? 74  SER H OG  1 
ATOM   2320 N N   . LYS B  2 77  ? -9.74900  -13.36800 -22.53300 1.000 48.93296  ? 75  LYS H N   1 
ATOM   2321 C CA  . LYS B  2 77  ? -8.67300  -12.37200 -22.28700 1.000 45.75878  ? 75  LYS H CA  1 
ATOM   2322 C C   . LYS B  2 77  ? -9.19000  -11.12300 -21.54900 1.000 38.92663  ? 75  LYS H C   1 
ATOM   2323 O O   . LYS B  2 77  ? -8.37500  -10.24900 -21.26100 1.000 37.66961  ? 75  LYS H O   1 
ATOM   2324 C CB  . LYS B  2 77  ? -8.04400  -12.00100 -23.63400 1.000 45.65465  ? 75  LYS H CB  1 
ATOM   2325 C CG  . LYS B  2 77  ? -7.80800  -13.15400 -24.59700 1.000 47.41164  ? 75  LYS H CG  1 
ATOM   2326 C CD  . LYS B  2 77  ? -7.35400  -12.69800 -25.96600 1.000 47.99371  ? 75  LYS H CD  1 
ATOM   2327 C CE  . LYS B  2 77  ? -5.92500  -12.19800 -25.98100 1.000 52.89269  ? 75  LYS H CE  1 
ATOM   2328 N NZ  . LYS B  2 77  ? -4.99300  -13.20900 -26.53300 1.000 51.84966  ? 75  LYS H NZ  1 
ATOM   2329 N N   . ASN B  2 78  ? -10.48200 -11.07300 -21.26600 1.000 39.48122  ? 76  ASN H N   1 
ATOM   2330 C CA  . ASN B  2 78  ? -11.11300 -9.92000  -20.60300 1.000 45.95427  ? 76  ASN H CA  1 
ATOM   2331 C C   . ASN B  2 78  ? -10.86200 -8.72000  -21.45900 1.000 47.70936  ? 76  ASN H C   1 
ATOM   2332 O O   . ASN B  2 78  ? -10.39500 -7.70400  -20.99500 1.000 47.69251  ? 76  ASN H O   1 
ATOM   2333 C CB  . ASN B  2 78  ? -10.65200 -9.69300  -19.17500 1.000 35.23900  ? 76  ASN H CB  1 
ATOM   2334 C CG  . ASN B  2 78  ? -11.71500 -9.03100  -18.33100 1.000 40.96620  ? 76  ASN H CG  1 
ATOM   2335 O OD1 . ASN B  2 78  ? -12.78300 -9.58900  -18.11300 1.000 44.18435  ? 76  ASN H OD1 1 
ATOM   2336 N ND2 . ASN B  2 78  ? -11.43500 -7.82500  -17.87000 1.000 43.10863  ? 76  ASN H ND2 1 
ATOM   2337 N N   . GLU B  2 79  ? -11.22400 -8.84700  -22.71600 1.000 35.33090  ? 77  GLU H N   1 
ATOM   2338 C CA  A GLU B  2 79  ? -11.04000 -7.75800  -23.63100 0.543 34.82087  ? 77  GLU H CA  1 
ATOM   2339 C CA  B GLU B  2 79  ? -11.03900 -7.74300  -23.61200 0.457 34.85252  ? 77  GLU H CA  1 
ATOM   2340 C C   . GLU B  2 79  ? -12.23700 -7.55300  -24.56100 1.000 36.22133  ? 77  GLU H C   1 
ATOM   2341 O O   . GLU B  2 79  ? -13.25700 -8.28800  -24.62600 1.000 36.27972  ? 77  GLU H O   1 
ATOM   2342 C CB  A GLU B  2 79  ? -9.83700  -8.02900  -24.52400 0.543 37.36655  ? 77  GLU H CB  1 
ATOM   2343 C CB  B GLU B  2 79  ? -9.75000  -7.93600  -24.40300 0.457 37.41146  ? 77  GLU H CB  1 
ATOM   2344 C CG  A GLU B  2 79  ? -8.53600  -8.35100  -23.81600 0.543 36.60883  ? 77  GLU H CG  1 
ATOM   2345 C CG  B GLU B  2 79  ? -9.76800  -9.06000  -25.41500 0.457 40.60775  ? 77  GLU H CG  1 
ATOM   2346 C CD  A GLU B  2 79  ? -7.44100  -8.75000  -24.78900 0.543 40.45594  ? 77  GLU H CD  1 
ATOM   2347 C CD  B GLU B  2 79  ? -8.40600  -9.27400  -26.04600 0.457 40.80015  ? 77  GLU H CD  1 
ATOM   2348 O OE1 A GLU B  2 79  ? -7.76700  -9.33200  -25.84400 0.543 41.63543  ? 77  GLU H OE1 1 
ATOM   2349 O OE1 B GLU B  2 79  ? -7.39300  -9.19800  -25.31700 0.457 40.80025  ? 77  GLU H OE1 1 
ATOM   2350 O OE2 A GLU B  2 79  ? -6.25800  -8.47800  -24.50200 0.543 33.62274  ? 77  GLU H OE2 1 
ATOM   2351 O OE2 B GLU B  2 79  ? -8.34800  -9.50900  -27.26800 0.457 35.36863  ? 77  GLU H OE2 1 
ATOM   2352 N N   . PHE B  2 80  ? -12.25600 -6.37300  -25.11400 1.000 27.83237  ? 78  PHE H N   1 
ATOM   2353 C CA  . PHE B  2 80  ? -13.27500 -6.18800  -26.16600 1.000 34.88328  ? 78  PHE H CA  1 
ATOM   2354 C C   . PHE B  2 80  ? -12.51000 -5.64900  -27.37300 1.000 36.40435  ? 78  PHE H C   1 
ATOM   2355 O O   . PHE B  2 80  ? -11.33200 -5.31900  -27.23600 1.000 35.72669  ? 78  PHE H O   1 
ATOM   2356 C CB  . PHE B  2 80  ? -14.51300 -5.41100  -25.71000 1.000 31.87778  ? 78  PHE H CB  1 
ATOM   2357 C CG  . PHE B  2 80  ? -14.33800 -3.94800  -25.39400 1.000 31.70035  ? 78  PHE H CG  1 
ATOM   2358 C CD1 . PHE B  2 80  ? -13.90200 -3.54100  -24.14600 1.000 32.47350  ? 78  PHE H CD1 1 
ATOM   2359 C CD2 . PHE B  2 80  ? -14.67100 -2.97900  -26.32500 1.000 30.60393  ? 78  PHE H CD2 1 
ATOM   2360 C CE1 . PHE B  2 80  ? -13.77000 -2.19500  -23.84900 1.000 36.60000  ? 78  PHE H CE1 1 
ATOM   2361 C CE2 . PHE B  2 80  ? -14.53000 -1.63400  -26.02900 1.000 30.09670  ? 78  PHE H CE2 1 
ATOM   2362 C CZ  . PHE B  2 80  ? -14.08100 -1.24600  -24.79100 1.000 27.85942  ? 78  PHE H CZ  1 
ATOM   2363 N N   . SER B  2 81  ? -13.19000 -5.58500  -28.49200 1.000 35.55055  ? 79  SER H N   1 
ATOM   2364 C CA  A SER B  2 81  ? -12.56000 -5.19700  -29.73300 0.486 31.44232  ? 79  SER H CA  1 
ATOM   2365 C CA  B SER B  2 81  ? -12.55500 -5.19000  -29.72900 0.514 31.43902  ? 79  SER H CA  1 
ATOM   2366 C C   . SER B  2 81  ? -13.44700 -4.46600  -30.76300 1.000 32.72332  ? 79  SER H C   1 
ATOM   2367 O O   . SER B  2 81  ? -14.69400 -4.36400  -30.72600 1.000 29.25211  ? 79  SER H O   1 
ATOM   2368 C CB  A SER B  2 81  ? -11.99000 -6.45100  -30.40700 0.486 32.68479  ? 79  SER H CB  1 
ATOM   2369 C CB  B SER B  2 81  ? -11.96500 -6.43800  -30.39500 0.514 32.69003  ? 79  SER H CB  1 
ATOM   2370 O OG  A SER B  2 81  ? -10.76300 -6.83000  -29.81700 0.486 30.75496  ? 79  SER H OG  1 
ATOM   2371 O OG  B SER B  2 81  ? -12.98500 -7.20600  -31.00600 0.514 25.88333  ? 79  SER H OG  1 
ATOM   2372 N N   . LEU B  2 82  ? -12.76100 -3.93900  -31.74500 1.000 25.59348  ? 80  LEU H N   1 
ATOM   2373 C CA  . LEU B  2 82  ? -13.44900 -3.22000  -32.80000 1.000 26.85248  ? 80  LEU H CA  1 
ATOM   2374 C C   . LEU B  2 82  ? -12.82700 -3.62200  -34.12200 1.000 27.19017  ? 80  LEU H C   1 
ATOM   2375 O O   . LEU B  2 82  ? -11.61000 -3.80500  -34.21800 1.000 28.36688  ? 80  LEU H O   1 
ATOM   2376 C CB  . LEU B  2 82  ? -13.34500 -1.68900  -32.59700 1.000 32.19773  ? 80  LEU H CB  1 
ATOM   2377 C CG  . LEU B  2 82  ? -13.45100 -0.79400  -33.81400 1.000 21.39350  ? 80  LEU H CG  1 
ATOM   2378 C CD1 . LEU B  2 82  ? -14.90300 -0.61600  -34.19500 1.000 29.45174  ? 80  LEU H CD1 1 
ATOM   2379 C CD2 . LEU B  2 82  ? -12.81800 0.52900   -33.47300 1.000 30.02854  ? 80  LEU H CD2 1 
ATOM   2380 N N   . ARG B  2 83  ? -13.67400 -3.75700  -35.12700 1.000 25.78156  ? 81  ARG H N   1 
ATOM   2381 C CA  . ARG B  2 83  ? -13.23000 -4.06400  -36.46400 1.000 36.22152  ? 81  ARG H CA  1 
ATOM   2382 C C   . ARG B  2 83  ? -13.90100 -3.11400  -37.41100 1.000 39.79822  ? 81  ARG H C   1 
ATOM   2383 O O   . ARG B  2 83  ? -15.11800 -2.99400  -37.43500 1.000 36.37237  ? 81  ARG H O   1 
ATOM   2384 C CB  . ARG B  2 83  ? -13.61700 -5.45000  -36.91200 1.000 45.37770  ? 81  ARG H CB  1 
ATOM   2385 C CG  . ARG B  2 83  ? -13.29700 -6.57900  -35.96900 1.000 56.15548  ? 81  ARG H CG  1 
ATOM   2386 C CD  . ARG B  2 83  ? -13.64200 -7.88200  -36.66600 1.000 77.06934  ? 81  ARG H CD  1 
ATOM   2387 N NE  . ARG B  2 83  ? -12.58000 -8.30500  -37.58000 1.000 81.38167  ? 81  ARG H NE  1 
ATOM   2388 C CZ  . ARG B  2 83  ? -12.70000 -8.38500  -38.90000 1.000 65.34274  ? 81  ARG H CZ  1 
ATOM   2389 N NH1 . ARG B  2 83  ? -13.83900 -8.07000  -39.49400 1.000 46.44311  ? 81  ARG H NH1 1 
ATOM   2390 N NH2 . ARG B  2 83  ? -11.67100 -8.79000  -39.62400 1.000 63.00346  ? 81  ARG H NH2 1 
ATOM   2391 N N   . LEU B  2 84  ? -13.09200 -2.44800  -38.20300 1.000 36.85730  ? 82  LEU H N   1 
ATOM   2392 C CA  . LEU B  2 84  ? -13.62700 -1.50000  -39.16600 1.000 43.43443  ? 82  LEU H CA  1 
ATOM   2393 C C   . LEU B  2 84  ? -13.05400 -1.80400  -40.54100 1.000 34.36190  ? 82  LEU H C   1 
ATOM   2394 O O   . LEU B  2 84  ? -11.83200 -1.78100  -40.71900 1.000 39.04571  ? 82  LEU H O   1 
ATOM   2395 C CB  . LEU B  2 84  ? -13.32600 -0.06700  -38.74000 1.000 31.77939  ? 82  LEU H CB  1 
ATOM   2396 C CG  . LEU B  2 84  ? -14.07700 0.88400   -39.66600 1.000 38.47801  ? 82  LEU H CG  1 
ATOM   2397 C CD1 . LEU B  2 84  ? -15.47700 1.21400   -39.15400 1.000 32.77919  ? 82  LEU H CD1 1 
ATOM   2398 C CD2 . LEU B  2 84  ? -13.22300 2.12600   -39.72200 1.000 38.83995  ? 82  LEU H CD2 1 
ATOM   2399 N N   . THR B  2 85  A -13.94600 -2.01900  -41.50100 1.000 30.34332  ? 82  THR H N   1 
ATOM   2400 C CA  . THR B  2 85  A -13.53800 -2.49300  -42.84400 1.000 39.17604  ? 82  THR H CA  1 
ATOM   2401 C C   . THR B  2 85  A -13.54700 -1.38900  -43.90000 1.000 45.71534  ? 82  THR H C   1 
ATOM   2402 O O   . THR B  2 85  A -14.22000 -0.37000  -43.68900 1.000 35.61417  ? 82  THR H O   1 
ATOM   2403 C CB  . THR B  2 85  A -14.51400 -3.60300  -43.27300 1.000 32.38805  ? 82  THR H CB  1 
ATOM   2404 O OG1 . THR B  2 85  A -15.82100 -3.04400  -43.38300 1.000 36.11327  ? 82  THR H OG1 1 
ATOM   2405 C CG2 . THR B  2 85  A -14.54700 -4.76400  -42.30500 1.000 30.56615  ? 82  THR H CG2 1 
ATOM   2406 N N   . SER B  2 86  B -12.87500 -1.64000  -45.02800 1.000 39.97546  ? 82  SER H N   1 
ATOM   2407 C CA  . SER B  2 86  B -12.87900 -0.67500  -46.15500 1.000 43.14565  ? 82  SER H CA  1 
ATOM   2408 C C   . SER B  2 86  B -12.45100 0.68800   -45.62100 1.000 38.61610  ? 82  SER H C   1 
ATOM   2409 O O   . SER B  2 86  B -13.13600 1.67600   -45.90600 1.000 38.44897  ? 82  SER H O   1 
ATOM   2410 C CB  . SER B  2 86  B -14.22600 -0.66900  -46.81800 1.000 42.03364  ? 82  SER H CB  1 
ATOM   2411 O OG  . SER B  2 86  B -14.44300 -1.88400  -47.51900 1.000 47.56849  ? 82  SER H OG  1 
ATOM   2412 N N   . VAL B  2 87  C -11.34100 0.70400   -44.89000 1.000 39.65463  ? 82  VAL H N   1 
ATOM   2413 C CA  . VAL B  2 87  C -10.83000 1.94400   -44.23800 1.000 36.20835  ? 82  VAL H CA  1 
ATOM   2414 C C   . VAL B  2 87  C -10.29700 2.95500   -45.26100 1.000 42.71539  ? 82  VAL H C   1 
ATOM   2415 O O   . VAL B  2 87  C -9.65700  2.53100   -46.22400 1.000 42.80814  ? 82  VAL H O   1 
ATOM   2416 C CB  . VAL B  2 87  C -9.76400  1.57100   -43.19000 1.000 37.55128  ? 82  VAL H CB  1 
ATOM   2417 C CG1 . VAL B  2 87  C -8.41300  1.25500   -43.80700 1.000 35.53074  ? 82  VAL H CG1 1 
ATOM   2418 C CG2 . VAL B  2 87  C -9.64700  2.60300   -42.08800 1.000 49.30194  ? 82  VAL H CG2 1 
ATOM   2419 N N   . THR B  2 88  ? -10.61600 4.23000   -45.07800 1.000 37.39871  ? 83  THR H N   1 
ATOM   2420 C CA  . THR B  2 88  ? -10.09200 5.32900   -45.91700 1.000 33.04489  ? 83  THR H CA  1 
ATOM   2421 C C   . THR B  2 88  ? -9.28800  6.23800   -44.99800 1.000 44.84465  ? 83  THR H C   1 
ATOM   2422 O O   . THR B  2 88  ? -9.19500  5.92800   -43.80200 1.000 40.33825  ? 83  THR H O   1 
ATOM   2423 C CB  . THR B  2 88  ? -11.22400 6.17800   -46.49500 1.000 40.43920  ? 83  THR H CB  1 
ATOM   2424 O OG1 . THR B  2 88  ? -11.84200 6.89700   -45.43000 1.000 47.99918  ? 83  THR H OG1 1 
ATOM   2425 C CG2 . THR B  2 88  ? -12.26300 5.35000   -47.22100 1.000 40.04823  ? 83  THR H CG2 1 
ATOM   2426 N N   . ALA B  2 89  ? -8.75700  7.32900   -45.53000 1.000 32.90072  ? 84  ALA H N   1 
ATOM   2427 C CA  . ALA B  2 89  ? -7.98100  8.27300   -44.70500 1.000 40.05927  ? 84  ALA H CA  1 
ATOM   2428 C C   . ALA B  2 89  ? -8.91400  8.93100   -43.69500 1.000 33.08593  ? 84  ALA H C   1 
ATOM   2429 O O   . ALA B  2 89  ? -8.42300  9.39500   -42.67500 1.000 31.57903  ? 84  ALA H O   1 
ATOM   2430 C CB  . ALA B  2 89  ? -7.32900  9.29200   -45.59000 1.000 36.39074  ? 84  ALA H CB  1 
ATOM   2431 N N   . ALA B  2 90  ? -10.20700 8.95400   -44.00400 1.000 25.23785  ? 85  ALA H N   1 
ATOM   2432 C CA  . ALA B  2 90  ? -11.20400 9.56600   -43.11000 1.000 32.42480  ? 85  ALA H CA  1 
ATOM   2433 C C   . ALA B  2 90  ? -11.34900 8.74600   -41.81900 1.000 27.77010  ? 85  ALA H C   1 
ATOM   2434 O O   . ALA B  2 90  ? -12.03300 9.20800   -40.91600 1.000 29.93019  ? 85  ALA H O   1 
ATOM   2435 C CB  . ALA B  2 90  ? -12.50800 9.69000   -43.85200 1.000 29.32242  ? 85  ALA H CB  1 
ATOM   2436 N N   . ASP B  2 91  ? -10.72200 7.58000   -41.76700 1.000 24.63249  ? 86  ASP H N   1 
ATOM   2437 C CA  . ASP B  2 91  ? -10.76800 6.71500   -40.56200 1.000 32.52377  ? 86  ASP H CA  1 
ATOM   2438 C C   . ASP B  2 91  ? -9.48800  6.93500   -39.75000 1.000 36.31221  ? 86  ASP H C   1 
ATOM   2439 O O   . ASP B  2 91  ? -9.36800  6.34200   -38.67900 1.000 24.66591  ? 86  ASP H O   1 
ATOM   2440 C CB  . ASP B  2 91  ? -11.01100 5.25600   -40.95900 1.000 36.77613  ? 86  ASP H CB  1 
ATOM   2441 C CG  . ASP B  2 91  ? -12.32600 5.04300   -41.68800 1.000 34.28880  ? 86  ASP H CG  1 
ATOM   2442 O OD1 . ASP B  2 91  ? -13.35500 5.53000   -41.19500 1.000 32.50104  ? 86  ASP H OD1 1 
ATOM   2443 O OD2 . ASP B  2 91  ? -12.30500 4.40100   -42.74600 1.000 36.06407  ? 86  ASP H OD2 1 
ATOM   2444 N N   . THR B  2 92  ? -8.58500  7.78400   -40.24300 1.000 28.00123  ? 87  THR H N   1 
ATOM   2445 C CA  . THR B  2 92  ? -7.37400  8.11400   -39.44500 1.000 28.15314  ? 87  THR H CA  1 
ATOM   2446 C C   . THR B  2 92  ? -7.85100  8.83400   -38.18100 1.000 28.18622  ? 87  THR H C   1 
ATOM   2447 O O   . THR B  2 92  ? -8.62200  9.79100   -38.31700 1.000 21.63433  ? 87  THR H O   1 
ATOM   2448 C CB  . THR B  2 92  ? -6.32700  8.90000   -40.25100 1.000 34.94540  ? 87  THR H CB  1 
ATOM   2449 O OG1 . THR B  2 92  ? -5.67100  8.03300   -41.17500 1.000 36.26154  ? 87  THR H OG1 1 
ATOM   2450 C CG2 . THR B  2 92  ? -5.30000  9.57100   -39.36700 1.000 30.85340  ? 87  THR H CG2 1 
ATOM   2451 N N   . ALA B  2 93  ? -7.42200  8.36300   -37.01400 1.000 25.61741  ? 88  ALA H N   1 
ATOM   2452 C CA  . ALA B  2 93  ? -7.95300  8.94000   -35.78100 1.000 22.92674  ? 88  ALA H CA  1 
ATOM   2453 C C   . ALA B  2 93  ? -7.27300  8.34300   -34.55000 1.000 21.20284  ? 88  ALA H C   1 
ATOM   2454 O O   . ALA B  2 93  ? -6.58700  7.30900   -34.61300 1.000 23.82047  ? 88  ALA H O   1 
ATOM   2455 C CB  . ALA B  2 93  ? -9.48300  8.75000   -35.69400 1.000 23.95456  ? 88  ALA H CB  1 
ATOM   2456 N N   . VAL B  2 94  ? -7.44500  9.04700   -33.41800 1.000 26.22908  ? 89  VAL H N   1 
ATOM   2457 C CA  . VAL B  2 94  ? -7.20800  8.43900   -32.12000 1.000 22.48122  ? 89  VAL H CA  1 
ATOM   2458 C C   . VAL B  2 94  ? -8.47400  7.65000   -31.77500 1.000 23.79947  ? 89  VAL H C   1 
ATOM   2459 O O   . VAL B  2 94  ? -9.58600  8.17900   -31.89200 1.000 21.13586  ? 89  VAL H O   1 
ATOM   2460 C CB  . VAL B  2 94  ? -6.89800  9.51300   -31.05500 1.000 24.29602  ? 89  VAL H CB  1 
ATOM   2461 C CG1 . VAL B  2 94  ? -6.94400  8.90000   -29.67000 1.000 23.10780  ? 89  VAL H CG1 1 
ATOM   2462 C CG2 . VAL B  2 94  ? -5.53600  10.21500  -31.33400 1.000 20.77166  ? 89  VAL H CG2 1 
ATOM   2463 N N   . TYR B  2 95  ? -8.31600  6.37300   -31.38600 1.000 19.17262  ? 90  TYR H N   1 
ATOM   2464 C CA  . TYR B  2 95  ? -9.44600  5.51300   -31.03000 1.000 18.29842  ? 90  TYR H CA  1 
ATOM   2465 C C   . TYR B  2 95  ? -9.49700  5.31600   -29.52400 1.000 22.20131  ? 90  TYR H C   1 
ATOM   2466 O O   . TYR B  2 95  ? -8.48800  4.96000   -28.90300 1.000 27.02543  ? 90  TYR H O   1 
ATOM   2467 C CB  . TYR B  2 95  ? -9.36700  4.17000   -31.77900 1.000 29.70745  ? 90  TYR H CB  1 
ATOM   2468 C CG  . TYR B  2 95  ? -9.79600  4.34800   -33.23000 1.000 25.26007  ? 90  TYR H CG  1 
ATOM   2469 C CD1 . TYR B  2 95  ? -8.88400  4.76300   -34.21700 1.000 26.56495  ? 90  TYR H CD1 1 
ATOM   2470 C CD2 . TYR B  2 95  ? -11.12200 4.12100   -33.61800 1.000 25.38025  ? 90  TYR H CD2 1 
ATOM   2471 C CE1 . TYR B  2 95  ? -9.31000  4.96200   -35.54500 1.000 24.69373  ? 90  TYR H CE1 1 
ATOM   2472 C CE2 . TYR B  2 95  ? -11.54200 4.31000   -34.92800 1.000 25.19906  ? 90  TYR H CE2 1 
ATOM   2473 C CZ  . TYR B  2 95  ? -10.63600 4.72700   -35.88800 1.000 25.66534  ? 90  TYR H CZ  1 
ATOM   2474 O OH  . TYR B  2 95  ? -11.08600 4.91100   -37.19100 1.000 29.65259  ? 90  TYR H OH  1 
ATOM   2475 N N   . PHE B  2 96  ? -10.67300 5.56100   -28.93500 1.000 20.08027  ? 91  PHE H N   1 
ATOM   2476 C CA  . PHE B  2 96  ? -10.86000 5.47200   -27.48600 1.000 23.98172  ? 91  PHE H CA  1 
ATOM   2477 C C   . PHE B  2 96  ? -11.76000 4.27400   -27.18200 1.000 18.73618  ? 91  PHE H C   1 
ATOM   2478 O O   . PHE B  2 96  ? -12.84500 4.14400   -27.76900 1.000 22.42100  ? 91  PHE H O   1 
ATOM   2479 C CB  . PHE B  2 96  ? -11.54100 6.74900   -26.95200 1.000 21.54055  ? 91  PHE H CB  1 
ATOM   2480 C CG  . PHE B  2 96  ? -10.68600 7.97300   -27.01400 1.000 18.53597  ? 91  PHE H CG  1 
ATOM   2481 C CD1 . PHE B  2 96  ? -9.60000  8.15100   -26.16600 1.000 21.39324  ? 91  PHE H CD1 1 
ATOM   2482 C CD2 . PHE B  2 96  ? -10.89400 8.88700   -28.03700 1.000 21.29765  ? 91  PHE H CD2 1 
ATOM   2483 C CE1 . PHE B  2 96  ? -8.78100  9.30000   -26.25800 1.000 24.31350  ? 91  PHE H CE1 1 
ATOM   2484 C CE2 . PHE B  2 96  ? -10.07100 10.04500  -28.16800 1.000 23.43174  ? 91  PHE H CE2 1 
ATOM   2485 C CZ  . PHE B  2 96  ? -9.00400  10.24100  -27.28000 1.000 16.86279  ? 91  PHE H CZ  1 
ATOM   2486 N N   . CYS B  2 97  ? -11.36900 3.46100   -26.21300 1.000 21.35501  ? 92  CYS H N   1 
ATOM   2487 C CA  . CYS B  2 97  ? -12.31900 2.52300   -25.62900 1.000 30.32216  ? 92  CYS H CA  1 
ATOM   2488 C C   . CYS B  2 97  ? -12.78600 3.04800   -24.27200 1.000 26.56969  ? 92  CYS H C   1 
ATOM   2489 O O   . CYS B  2 97  ? -12.11700 3.87300   -23.63900 1.000 24.32004  ? 92  CYS H O   1 
ATOM   2490 C CB  . CYS B  2 97  ? -11.71400 1.12700   -25.50200 1.000 21.78334  ? 92  CYS H CB  1 
ATOM   2491 S SG  . CYS B  2 97  ? -10.35100 0.84700   -24.37200 1.000 32.04712  ? 92  CYS H SG  1 
ATOM   2492 N N   . ALA B  2 98  ? -13.96600 2.59700   -23.84900 1.000 32.61518  ? 93  ALA H N   1 
ATOM   2493 C CA  . ALA B  2 98  ? -14.57000 3.14900   -22.63300 1.000 28.79372  ? 93  ALA H CA  1 
ATOM   2494 C C   . ALA B  2 98  ? -15.59900 2.17200   -22.07500 1.000 30.01158  ? 93  ALA H C   1 
ATOM   2495 O O   . ALA B  2 98  ? -16.21600 1.39700   -22.81700 1.000 23.91310  ? 93  ALA H O   1 
ATOM   2496 C CB  . ALA B  2 98  ? -15.24000 4.50900   -22.88300 1.000 22.59468  ? 93  ALA H CB  1 
ATOM   2497 N N   . ARG B  2 99  ? -15.77100 2.22700   -20.76100 1.000 25.13523  ? 94  ARG H N   1 
ATOM   2498 C CA  . ARG B  2 99  ? -16.83600 1.52900   -20.05700 1.000 22.60679  ? 94  ARG H CA  1 
ATOM   2499 C C   . ARG B  2 99  ? -17.94300 2.49700   -19.64800 1.000 26.89849  ? 94  ARG H C   1 
ATOM   2500 O O   . ARG B  2 99  ? -17.69500 3.68000   -19.38600 1.000 24.49667  ? 94  ARG H O   1 
ATOM   2501 C CB  . ARG B  2 99  ? -16.26600 0.81600   -18.82600 1.000 25.21033  ? 94  ARG H CB  1 
ATOM   2502 C CG  . ARG B  2 99  ? -17.23700 -0.12300  -18.08800 1.000 24.44249  ? 94  ARG H CG  1 
ATOM   2503 C CD  . ARG B  2 99  ? -16.58800 -0.49400  -16.78900 1.000 21.04282  ? 94  ARG H CD  1 
ATOM   2504 N NE  . ARG B  2 99  ? -16.91800 0.43200   -15.70900 1.000 24.07404  ? 94  ARG H NE  1 
ATOM   2505 C CZ  . ARG B  2 99  ? -16.52200 0.26200   -14.45100 1.000 28.88845  ? 94  ARG H CZ  1 
ATOM   2506 N NH1 . ARG B  2 99  ? -15.82100 -0.80600  -14.08600 1.000 29.23135  ? 94  ARG H NH1 1 
ATOM   2507 N NH2 . ARG B  2 99  ? -16.78400 1.21300   -13.54600 1.000 24.37948  ? 94  ARG H NH2 1 
ATOM   2508 N N   . GLY B  2 100 ? -19.18400 1.99100   -19.63900 1.000 20.62061  ? 95  GLY H N   1 
ATOM   2509 C CA  . GLY B  2 100 ? -20.29800 2.68100   -19.01800 1.000 22.94714  ? 95  GLY H CA  1 
ATOM   2510 C C   . GLY B  2 100 ? -21.09000 1.69700   -18.17900 1.000 26.08025  ? 95  GLY H C   1 
ATOM   2511 O O   . GLY B  2 100 ? -20.81800 0.50500   -18.18800 1.000 24.78099  ? 95  GLY H O   1 
ATOM   2512 N N   . THR B  2 101 ? -22.07900 2.21900   -17.47000 1.000 19.85896  ? 96  THR H N   1 
ATOM   2513 C CA  . THR B  2 101 ? -22.90100 1.38500   -16.56400 1.000 21.73473  ? 96  THR H CA  1 
ATOM   2514 C C   . THR B  2 101 ? -24.38300 1.64200   -16.86200 1.000 26.83483  ? 96  THR H C   1 
ATOM   2515 O O   . THR B  2 101 ? -24.81500 2.77700   -16.64100 1.000 21.57890  ? 96  THR H O   1 
ATOM   2516 C CB  . THR B  2 101 ? -22.51900 1.64400   -15.09600 1.000 25.60545  ? 96  THR H CB  1 
ATOM   2517 O OG1 . THR B  2 101 ? -21.10000 1.63300   -14.93900 1.000 24.73077  ? 96  THR H OG1 1 
ATOM   2518 C CG2 . THR B  2 101 ? -23.15100 0.64500   -14.15100 1.000 22.49672  ? 96  THR H CG2 1 
ATOM   2519 N N   . GLU B  2 102 ? -25.12700 0.62800   -17.33000 1.000 20.08688  ? 97  GLU H N   1 
ATOM   2520 C CA  . GLU B  2 102 ? -26.56600 0.80800   -17.68000 1.000 23.95141  ? 97  GLU H CA  1 
ATOM   2521 C C   . GLU B  2 102 ? -27.27400 1.59400   -16.57000 1.000 21.56889  ? 97  GLU H C   1 
ATOM   2522 O O   . GLU B  2 102 ? -27.13100 1.20200   -15.42000 1.000 21.36577  ? 97  GLU H O   1 
ATOM   2523 C CB  . GLU B  2 102 ? -27.27900 -0.50800  -18.01400 1.000 29.16086  ? 97  GLU H CB  1 
ATOM   2524 C CG  . GLU B  2 102 ? -28.59400 -0.30600  -18.74100 1.000 24.24132  ? 97  GLU H CG  1 
ATOM   2525 C CD  . GLU B  2 102 ? -28.48300 -0.04500  -20.23400 1.000 40.26993  ? 97  GLU H CD  1 
ATOM   2526 O OE1 . GLU B  2 102 ? -27.54000 0.64900   -20.64700 1.000 37.71960  ? 97  GLU H OE1 1 
ATOM   2527 O OE2 . GLU B  2 102 ? -29.34400 -0.53700  -20.97700 1.000 29.52225  ? 97  GLU H OE2 1 
ATOM   2528 N N   . ASP B  2 103 ? -27.98400 2.65800   -16.93300 1.000 21.78054  ? 98  ASP H N   1 
ATOM   2529 C CA  . ASP B  2 103 ? -28.58800 3.57400   -15.93700 1.000 19.94857  ? 98  ASP H CA  1 
ATOM   2530 C C   . ASP B  2 103 ? -29.77400 4.26000   -16.60300 1.000 29.68944  ? 98  ASP H C   1 
ATOM   2531 O O   . ASP B  2 103 ? -29.70800 5.48400   -16.78300 1.000 25.68885  ? 98  ASP H O   1 
ATOM   2532 C CB  . ASP B  2 103 ? -27.49600 4.51600   -15.42600 1.000 25.77139  ? 98  ASP H CB  1 
ATOM   2533 C CG  . ASP B  2 103 ? -27.87100 5.34500   -14.21100 1.000 27.63611  ? 98  ASP H CG  1 
ATOM   2534 O OD1 . ASP B  2 103 ? -28.57600 4.82100   -13.34300 1.000 24.62837  ? 98  ASP H OD1 1 
ATOM   2535 O OD2 . ASP B  2 103 ? -27.43300 6.50200   -14.14700 1.000 20.74220  ? 98  ASP H OD2 1 
ATOM   2536 N N   . LEU B  2 104 ? -30.83700 3.51500   -16.86700 1.000 25.63631  ? 99  LEU H N   1 
ATOM   2537 C CA  . LEU B  2 104 ? -31.98000 4.02400   -17.62600 1.000 29.76358  ? 99  LEU H CA  1 
ATOM   2538 C C   . LEU B  2 104 ? -32.70500 5.22900   -17.08200 1.000 24.95150  ? 99  LEU H C   1 
ATOM   2539 O O   . LEU B  2 104 ? -33.44200 5.86700   -17.78900 1.000 28.60777  ? 99  LEU H O   1 
ATOM   2540 C CB  . LEU B  2 104 ? -32.95700 2.85200   -17.87400 1.000 30.33617  ? 99  LEU H CB  1 
ATOM   2541 C CG  . LEU B  2 104 ? -32.37600 1.61900   -18.55600 1.000 29.18228  ? 99  LEU H CG  1 
ATOM   2542 C CD1 . LEU B  2 104 ? -33.49400 0.73200   -19.06800 1.000 32.91673  ? 99  LEU H CD1 1 
ATOM   2543 C CD2 . LEU B  2 104 ? -31.45400 2.01500   -19.69500 1.000 38.42608  ? 99  LEU H CD2 1 
ATOM   2544 N N   . GLY B  2 105 ? -32.50500 5.53800   -15.83200 1.000 25.30406  ? 100 GLY H N   1 
ATOM   2545 C CA  . GLY B  2 105 ? -33.09700 6.73500   -15.29200 1.000 31.30268  ? 100 GLY H CA  1 
ATOM   2546 C C   . GLY B  2 105 ? -32.42700 8.03600   -15.68600 1.000 28.75173  ? 100 GLY H C   1 
ATOM   2547 O O   . GLY B  2 105 ? -33.00300 9.08900   -15.53100 1.000 31.46786  ? 100 GLY H O   1 
ATOM   2548 N N   . TYR B  2 106 A -31.21700 7.95500   -16.20200 1.000 26.71383  ? 100 TYR H N   1 
ATOM   2549 C CA  . TYR B  2 106 A -30.46100 9.15700   -16.52600 1.000 24.14659  ? 100 TYR H CA  1 
ATOM   2550 C C   . TYR B  2 106 A -29.69200 9.05200   -17.84800 1.000 29.48405  ? 100 TYR H C   1 
ATOM   2551 O O   . TYR B  2 106 A -28.96000 9.95400   -18.19500 1.000 28.94111  ? 100 TYR H O   1 
ATOM   2552 C CB  . TYR B  2 106 A -29.53000 9.42100   -15.35800 1.000 20.37157  ? 100 TYR H CB  1 
ATOM   2553 C CG  . TYR B  2 106 A -30.22600 9.42700   -14.01300 1.000 26.55450  ? 100 TYR H CG  1 
ATOM   2554 C CD1 . TYR B  2 106 A -30.82800 10.57300  -13.53700 1.000 22.08547  ? 100 TYR H CD1 1 
ATOM   2555 C CD2 . TYR B  2 106 A -30.29600 8.28200   -13.23500 1.000 25.92766  ? 100 TYR H CD2 1 
ATOM   2556 C CE1 . TYR B  2 106 A -31.47300 10.58600  -12.32600 1.000 24.22192  ? 100 TYR H CE1 1 
ATOM   2557 C CE2 . TYR B  2 106 A -30.94000 8.28600   -12.01600 1.000 16.76165  ? 100 TYR H CE2 1 
ATOM   2558 C CZ  . TYR B  2 106 A -31.52500 9.44200   -11.57100 1.000 19.56514  ? 100 TYR H CZ  1 
ATOM   2559 O OH  . TYR B  2 106 A -32.16700 9.46900   -10.37400 1.000 23.49876  ? 100 TYR H OH  1 
ATOM   2560 N N   . CYS B  2 107 B -29.85500 7.95500   -18.56400 1.000 27.76610  ? 100 CYS H N   1 
ATOM   2561 C CA  . CYS B  2 107 B -29.16800 7.71800   -19.81400 1.000 24.63461  ? 100 CYS H CA  1 
ATOM   2562 C C   . CYS B  2 107 B -29.91100 6.70100   -20.64200 1.000 35.56477  ? 100 CYS H C   1 
ATOM   2563 O O   . CYS B  2 107 B -30.45100 5.74700   -20.10300 1.000 31.33008  ? 100 CYS H O   1 
ATOM   2564 C CB  . CYS B  2 107 B -27.75800 7.17800   -19.59900 1.000 21.26521  ? 100 CYS H CB  1 
ATOM   2565 S SG  . CYS B  2 107 B -26.66700 7.12200   -21.02000 1.000 29.29453  ? 100 CYS H SG  1 
ATOM   2566 N N   . SER B  2 108 C -29.93800 6.91600   -21.94300 1.000 29.28744  ? 100 SER H N   1 
ATOM   2567 C CA  . SER B  2 108 C -30.52000 5.94200   -22.85300 1.000 30.24557  ? 100 SER H CA  1 
ATOM   2568 C C   . SER B  2 108 C -29.52600 4.75900   -22.81000 1.000 30.70004  ? 100 SER H C   1 
ATOM   2569 O O   . SER B  2 108 C -28.38700 4.93000   -22.41200 1.000 24.89422  ? 100 SER H O   1 
ATOM   2570 C CB  . SER B  2 108 C -30.75100 6.52900   -24.27100 1.000 26.70557  ? 100 SER H CB  1 
ATOM   2571 O OG  . SER B  2 108 C -29.57900 6.59200   -25.03400 1.000 42.78642  ? 100 SER H OG  1 
ATOM   2572 N N   . SER B  2 109 D -29.95200 3.57100   -23.20000 1.000 27.22941  ? 100 SER H N   1 
ATOM   2573 C CA  . SER B  2 109 D -29.09300 2.38400   -23.11700 1.000 22.82388  ? 100 SER H CA  1 
ATOM   2574 C C   . SER B  2 109 D -27.76500 2.50400   -23.81700 1.000 23.23030  ? 100 SER H C   1 
ATOM   2575 O O   . SER B  2 109 D -27.68600 3.04800   -24.89000 1.000 28.71885  ? 100 SER H O   1 
ATOM   2576 C CB  . SER B  2 109 D -29.84300 1.10400   -23.62400 1.000 29.79109  ? 100 SER H CB  1 
ATOM   2577 O OG  . SER B  2 109 D -29.04900 -0.05100  -23.50400 1.000 25.30602  ? 100 SER H OG  1 
ATOM   2578 N N   . GLY B  2 110 E -26.73100 1.97800   -23.19200 1.000 25.29621  ? 100 GLY H N   1 
ATOM   2579 C CA  . GLY B  2 110 E -25.39700 2.01300   -23.75100 1.000 25.92111  ? 100 GLY H CA  1 
ATOM   2580 C C   . GLY B  2 110 E -24.89600 3.33900   -24.27300 1.000 24.67737  ? 100 GLY H C   1 
ATOM   2581 O O   . GLY B  2 110 E -24.03200 3.35200   -25.11300 1.000 28.72449  ? 100 GLY H O   1 
ATOM   2582 N N   . SER B  2 111 F -25.41100 4.43300   -23.75300 1.000 23.93971  ? 100 SER H N   1 
ATOM   2583 C CA  . SER B  2 111 F -25.08200 5.73500   -24.29300 1.000 23.18017  ? 100 SER H CA  1 
ATOM   2584 C C   . SER B  2 111 F -24.28100 6.70600   -23.40200 1.000 32.66027  ? 100 SER H C   1 
ATOM   2585 O O   . SER B  2 111 F -24.31400 7.89000   -23.67600 1.000 28.87177  ? 100 SER H O   1 
ATOM   2586 C CB  . SER B  2 111 F -26.39700 6.41300   -24.70400 1.000 24.37264  ? 100 SER H CB  1 
ATOM   2587 O OG  . SER B  2 111 F -27.05100 5.73900   -25.75200 1.000 30.07496  ? 100 SER H OG  1 
ATOM   2588 N N   . CYS B  2 112 G -23.61000 6.25600   -22.34800 1.000 31.46350  ? 100 CYS H N   1 
ATOM   2589 C CA  . CYS B  2 112 G -22.91800 7.15500   -21.42700 1.000 18.47676  ? 100 CYS H CA  1 
ATOM   2590 C C   . CYS B  2 112 G -21.57500 6.57800   -20.96700 1.000 18.49395  ? 100 CYS H C   1 
ATOM   2591 O O   . CYS B  2 112 G -21.41700 6.28700   -19.80400 1.000 19.19877  ? 100 CYS H O   1 
ATOM   2592 C CB  . CYS B  2 112 G -23.81300 7.50800   -20.23100 1.000 17.57676  ? 100 CYS H CB  1 
ATOM   2593 S SG  . CYS B  2 112 G -25.26000 8.51400   -20.56000 1.000 24.73006  ? 100 CYS H SG  1 
ATOM   2594 N N   . PRO B  2 113 H -20.61600 6.42800   -21.90200 1.000 18.45969  ? 100 PRO H N   1 
ATOM   2595 C CA  . PRO B  2 113 H -19.29700 5.93500   -21.48100 1.000 21.67070  ? 100 PRO H CA  1 
ATOM   2596 C C   . PRO B  2 113 H -18.72200 6.88800   -20.44300 1.000 26.32463  ? 100 PRO H C   1 
ATOM   2597 O O   . PRO B  2 113 H -18.77000 8.10600   -20.61500 1.000 25.11119  ? 100 PRO H O   1 
ATOM   2598 C CB  . PRO B  2 113 H -18.48400 5.95100   -22.78000 1.000 16.55465  ? 100 PRO H CB  1 
ATOM   2599 C CG  . PRO B  2 113 H -19.12600 7.04100   -23.59700 1.000 18.92284  ? 100 PRO H CG  1 
ATOM   2600 C CD  . PRO B  2 113 H -20.61200 6.87100   -23.30200 1.000 18.65749  ? 100 PRO H CD  1 
ATOM   2601 N N   . ASN B  2 114 ? -18.23000 6.34100   -19.33900 1.000 18.72312  ? 101 ASN H N   1 
ATOM   2602 C CA  . ASN B  2 114 ? -17.80800 7.21000   -18.27000 1.000 21.01609  ? 101 ASN H CA  1 
ATOM   2603 C C   . ASN B  2 114 ? -16.43300 6.86500   -17.73600 1.000 20.39605  ? 101 ASN H C   1 
ATOM   2604 O O   . ASN B  2 114 ? -15.97900 7.49500   -16.78600 1.000 18.81026  ? 101 ASN H O   1 
ATOM   2605 C CB  . ASN B  2 114 ? -18.84400 7.20800   -17.12900 1.000 22.20489  ? 101 ASN H CB  1 
ATOM   2606 C CG  . ASN B  2 114 ? -18.88400 5.89200   -16.39000 1.000 20.54606  ? 101 ASN H CG  1 
ATOM   2607 O OD1 . ASN B  2 114 ? -18.36600 4.88100   -16.87000 1.000 24.22750  ? 101 ASN H OD1 1 
ATOM   2608 N ND2 . ASN B  2 114 ? -19.44400 5.90800   -15.18700 1.000 24.93470  ? 101 ASN H ND2 1 
ATOM   2609 N N   . HIS B  2 115 ? -15.78000 5.85900   -18.27400 1.000 20.06682  ? 102 HIS H N   1 
ATOM   2610 C CA  . HIS B  2 115 ? -14.41400 5.55700   -17.90600 1.000 18.62146  ? 102 HIS H CA  1 
ATOM   2611 C C   . HIS B  2 115 ? -13.72400 5.24200   -19.20000 1.000 29.21660  ? 102 HIS H C   1 
ATOM   2612 O O   . HIS B  2 115 ? -13.94600 4.19200   -19.77200 1.000 23.06407  ? 102 HIS H O   1 
ATOM   2613 C CB  . HIS B  2 115 ? -14.25600 4.41600   -16.91900 1.000 26.26166  ? 102 HIS H CB  1 
ATOM   2614 C CG  . HIS B  2 115 ? -12.85700 4.23800   -16.43700 1.000 32.16505  ? 102 HIS H CG  1 
ATOM   2615 N ND1 . HIS B  2 115 ? -11.86500 3.69900   -17.22300 1.000 43.56417  ? 102 HIS H ND1 1 
ATOM   2616 C CD2 . HIS B  2 115 ? -12.27400 4.55500   -15.26100 1.000 37.79601  ? 102 HIS H CD2 1 
ATOM   2617 C CE1 . HIS B  2 115 ? -10.73300 3.67800   -16.54600 1.000 36.19607  ? 102 HIS H CE1 1 
ATOM   2618 N NE2 . HIS B  2 115 ? -10.95500 4.19000   -15.35200 1.000 41.69602  ? 102 HIS H NE2 1 
ATOM   2619 N N   . TRP B  2 116 ? -12.89800 6.14500   -19.65100 1.000 22.12767  ? 103 TRP H N   1 
ATOM   2620 C CA  . TRP B  2 116 ? -12.23000 6.00700   -20.93300 1.000 19.07663  ? 103 TRP H CA  1 
ATOM   2621 C C   . TRP B  2 116 ? -10.75700 5.70200   -20.80300 1.000 18.92967  ? 103 TRP H C   1 
ATOM   2622 O O   . TRP B  2 116 ? -10.09000 6.09800   -19.83800 1.000 25.13913  ? 103 TRP H O   1 
ATOM   2623 C CB  . TRP B  2 116 ? -12.34400 7.24100   -21.82000 1.000 20.14900  ? 103 TRP H CB  1 
ATOM   2624 C CG  . TRP B  2 116 ? -13.68700 7.87500   -22.05600 1.000 16.89974  ? 103 TRP H CG  1 
ATOM   2625 C CD1 . TRP B  2 116 ? -14.81800 7.76300   -21.30900 1.000 21.01729  ? 103 TRP H CD1 1 
ATOM   2626 C CD2 . TRP B  2 116 ? -14.09500 8.45100   -23.30100 1.000 14.17537  ? 103 TRP H CD2 1 
ATOM   2627 N NE1 . TRP B  2 116 ? -15.86900 8.41000   -21.93700 1.000 18.60418  ? 103 TRP H NE1 1 
ATOM   2628 C CE2 . TRP B  2 116 ? -15.46500 8.79300   -23.18500 1.000 14.47995  ? 103 TRP H CE2 1 
ATOM   2629 C CE3 . TRP B  2 116 ? -13.41700 8.75000   -24.49800 1.000 16.80187  ? 103 TRP H CE3 1 
ATOM   2630 C CZ2 . TRP B  2 116 ? -16.16400 9.45600   -24.19700 1.000 18.65452  ? 103 TRP H CZ2 1 
ATOM   2631 C CZ3 . TRP B  2 116 ? -14.10300 9.39900   -25.51400 1.000 15.77280  ? 103 TRP H CZ3 1 
ATOM   2632 C CH2 . TRP B  2 116 ? -15.46500 9.75300   -25.35800 1.000 21.79537  ? 103 TRP H CH2 1 
ATOM   2633 N N   . GLY B  2 117 ? -10.23300 5.04100   -21.84800 1.000 21.28556  ? 104 GLY H N   1 
ATOM   2634 C CA  . GLY B  2 117 ? -8.78800  4.90300   -21.98000 1.000 31.57892  ? 104 GLY H CA  1 
ATOM   2635 C C   . GLY B  2 117 ? -8.11200  6.15500   -22.58500 1.000 22.21217  ? 104 GLY H C   1 
ATOM   2636 O O   . GLY B  2 117 ? -8.75500  7.07100   -23.06400 1.000 23.38110  ? 104 GLY H O   1 
ATOM   2637 N N   . GLN B  2 118 ? -6.80900  6.18100   -22.60500 1.000 30.93450  ? 105 GLN H N   1 
ATOM   2638 C CA  . GLN B  2 118 ? -6.09100  7.32800   -23.14300 1.000 28.95672  ? 105 GLN H CA  1 
ATOM   2639 C C   . GLN B  2 118 ? -6.17000  7.42700   -24.65400 1.000 30.82800  ? 105 GLN H C   1 
ATOM   2640 O O   . GLN B  2 118 ? -5.89200  8.46300   -25.20600 1.000 27.03279  ? 105 GLN H O   1 
ATOM   2641 C CB  . GLN B  2 118 ? -4.63400  7.25600   -22.74300 1.000 28.65886  ? 105 GLN H CB  1 
ATOM   2642 C CG  . GLN B  2 118 ? -4.39100  7.44000   -21.25800 1.000 48.90270  ? 105 GLN H CG  1 
ATOM   2643 C CD  . GLN B  2 118 ? -3.09200  8.16200   -20.95100 1.000 46.35172  ? 105 GLN H CD  1 
ATOM   2644 O OE1 . GLN B  2 118 ? -2.30500  8.44000   -21.84400 1.000 60.15483  ? 105 GLN H OE1 1 
ATOM   2645 N NE2 . GLN B  2 118 ? -2.86900  8.46900   -19.68500 1.000 45.79400  ? 105 GLN H NE2 1 
ATOM   2646 N N   . GLY B  2 119 ? -6.54700  6.33300   -25.30800 1.000 30.72223  ? 106 GLY H N   1 
ATOM   2647 C CA  . GLY B  2 119 ? -6.66800  6.34800   -26.75400 1.000 27.13436  ? 106 GLY H CA  1 
ATOM   2648 C C   . GLY B  2 119 ? -5.42500  5.81500   -27.45900 1.000 28.18386  ? 106 GLY H C   1 
ATOM   2649 O O   . GLY B  2 119 ? -4.34000  5.71300   -26.88200 1.000 30.24821  ? 106 GLY H O   1 
ATOM   2650 N N   . THR B  2 120 ? -5.59400  5.46500   -28.73100 1.000 27.85720  ? 107 THR H N   1 
ATOM   2651 C CA  . THR B  2 120 ? -4.46000  5.00000   -29.57300 1.000 27.55611  ? 107 THR H CA  1 
ATOM   2652 C C   . THR B  2 120 ? -4.62300  5.56100   -30.99600 1.000 23.06993  ? 107 THR H C   1 
ATOM   2653 O O   . THR B  2 120 ? -5.72800  5.47200   -31.54100 1.000 23.81646  ? 107 THR H O   1 
ATOM   2654 C CB  . THR B  2 120 ? -4.28900  3.47000   -29.58400 1.000 30.07639  ? 107 THR H CB  1 
ATOM   2655 O OG1 . THR B  2 120 ? -3.06900  3.11900   -30.23600 1.000 35.28921  ? 107 THR H OG1 1 
ATOM   2656 C CG2 . THR B  2 120 ? -5.44600  2.76300   -30.25000 1.000 24.08434  ? 107 THR H CG2 1 
ATOM   2657 N N   . LEU B  2 121 ? -3.52700  6.08700   -31.54500 1.000 24.37061  ? 108 LEU H N   1 
ATOM   2658 C CA  . LEU B  2 121 ? -3.55900  6.69100   -32.90100 1.000 27.69908  ? 108 LEU H CA  1 
ATOM   2659 C C   . LEU B  2 121 ? -3.56200  5.61600   -33.99100 1.000 28.64682  ? 108 LEU H C   1 
ATOM   2660 O O   . LEU B  2 121 ? -2.73900  4.70200   -33.91500 1.000 26.54184  ? 108 LEU H O   1 
ATOM   2661 C CB  . LEU B  2 121 ? -2.35800  7.62700   -33.08300 1.000 26.84463  ? 108 LEU H CB  1 
ATOM   2662 C CG  . LEU B  2 121 ? -2.15700  8.17700   -34.49200 1.000 27.84770  ? 108 LEU H CG  1 
ATOM   2663 C CD1 . LEU B  2 121 ? -3.39000  8.92200   -34.96800 1.000 26.15499  ? 108 LEU H CD1 1 
ATOM   2664 C CD2 . LEU B  2 121 ? -0.93400  9.07700   -34.55000 1.000 28.98796  ? 108 LEU H CD2 1 
ATOM   2665 N N   . VAL B  2 122 ? -4.46800  5.75400   -34.95200 1.000 27.13018  ? 109 VAL H N   1 
ATOM   2666 C CA  . VAL B  2 122 ? -4.46300  4.85600   -36.13500 1.000 29.15945  ? 109 VAL H CA  1 
ATOM   2667 C C   . VAL B  2 122 ? -4.39700  5.72300   -37.39900 1.000 28.92244  ? 109 VAL H C   1 
ATOM   2668 O O   . VAL B  2 122 ? -5.33000  6.49000   -37.65100 1.000 30.34695  ? 109 VAL H O   1 
ATOM   2669 C CB  . VAL B  2 122 ? -5.66400  3.90000   -36.15200 1.000 31.50293  ? 109 VAL H CB  1 
ATOM   2670 C CG1 . VAL B  2 122 ? -5.86500  3.26900   -37.51800 1.000 36.04093  ? 109 VAL H CG1 1 
ATOM   2671 C CG2 . VAL B  2 122 ? -5.54400  2.83600   -35.07500 1.000 33.28340  ? 109 VAL H CG2 1 
ATOM   2672 N N   . THR B  2 123 ? -3.32100  5.57200   -38.15800 1.000 25.57318  ? 110 THR H N   1 
ATOM   2673 C CA  . THR B  2 123 ? -3.15600  6.31400   -39.42400 1.000 29.13004  ? 110 THR H CA  1 
ATOM   2674 C C   . THR B  2 123 ? -3.52500  5.40700   -40.60100 1.000 33.96554  ? 110 THR H C   1 
ATOM   2675 O O   . THR B  2 123 ? -3.02000  4.28400   -40.65000 1.000 30.14127  ? 110 THR H O   1 
ATOM   2676 C CB  . THR B  2 123 ? -1.71700  6.84600   -39.52500 1.000 34.41810  ? 110 THR H CB  1 
ATOM   2677 O OG1 . THR B  2 123 ? -1.43200  7.69900   -38.41700 1.000 30.80458  ? 110 THR H OG1 1 
ATOM   2678 C CG2 . THR B  2 123 ? -1.45000  7.57200   -40.82600 1.000 33.55664  ? 110 THR H CG2 1 
ATOM   2679 N N   . VAL B  2 124 ? -4.39700  5.87300   -41.49200 1.000 29.76535  ? 111 VAL H N   1 
ATOM   2680 C CA  . VAL B  2 124 ? -4.68100  5.10800   -42.70100 1.000 33.36174  ? 111 VAL H CA  1 
ATOM   2681 C C   . VAL B  2 124 ? -3.95600  5.78400   -43.86000 1.000 34.16635  ? 111 VAL H C   1 
ATOM   2682 O O   . VAL B  2 124 ? -4.42300  6.81900   -44.35200 1.000 41.75137  ? 111 VAL H O   1 
ATOM   2683 C CB  . VAL B  2 124 ? -6.18300  5.01000   -42.97500 1.000 33.31718  ? 111 VAL H CB  1 
ATOM   2684 C CG1 . VAL B  2 124 ? -6.48200  3.98100   -44.06300 1.000 41.29009  ? 111 VAL H CG1 1 
ATOM   2685 C CG2 . VAL B  2 124 ? -6.90200  4.62200   -41.69800 1.000 41.12024  ? 111 VAL H CG2 1 
ATOM   2686 N N   . SER B  2 125 ? -2.83800  5.21300   -44.32800 1.000 37.95605  ? 112 SER H N   1 
ATOM   2687 C CA  . SER B  2 125 ? -2.39400  5.55700   -45.68500 1.000 39.72701  ? 112 SER H CA  1 
ATOM   2688 C C   . SER B  2 125 ? -1.59000  4.41000   -46.29500 1.000 51.06817  ? 112 SER H C   1 
ATOM   2689 O O   . SER B  2 125 ? -1.15100  3.48600   -45.60000 1.000 38.65419  ? 112 SER H O   1 
ATOM   2690 C CB  . SER B  2 125 ? -1.56000  6.84900   -45.74900 1.000 41.38203  ? 112 SER H CB  1 
ATOM   2691 O OG  . SER B  2 125 ? -0.17700  6.60800   -45.57300 1.000 34.00598  ? 112 SER H OG  1 
ATOM   2692 N N   . SER B  2 126 ? -1.33300  4.48900   -47.59400 1.000 43.19101  ? 113 SER H N   1 
ATOM   2693 C CA  . SER B  2 126 ? -0.56000  3.45500   -48.33900 1.000 50.31450  ? 113 SER H CA  1 
ATOM   2694 C C   . SER B  2 126 ? 0.93300   3.72000   -48.21400 1.000 43.14621  ? 113 SER H C   1 
ATOM   2695 O O   . SER B  2 126 ? 1.71700   2.94800   -48.75800 1.000 49.62700  ? 113 SER H O   1 
ATOM   2696 C CB  . SER B  2 126 ? -0.95600  3.43400   -49.80200 1.000 38.44581  ? 113 SER H CB  1 
ATOM   2697 O OG  . SER B  2 126 ? -0.63200  4.64900   -50.45100 1.000 51.41663  ? 113 SER H OG  1 
ATOM   2698 N N   . ALA B  2 127 ? 1.28800   4.81200   -47.54300 1.000 48.30826  ? 114 ALA H N   1 
ATOM   2699 C CA  . ALA B  2 127 ? 2.70400   5.18300   -47.38500 1.000 45.74837  ? 114 ALA H CA  1 
ATOM   2700 C C   . ALA B  2 127 ? 3.43900   4.15000   -46.53800 1.000 38.90548  ? 114 ALA H C   1 
ATOM   2701 O O   . ALA B  2 127 ? 2.80200   3.41700   -45.81200 1.000 47.43105  ? 114 ALA H O   1 
ATOM   2702 C CB  . ALA B  2 127 ? 2.82300   6.55400   -46.79400 1.000 42.84753  ? 114 ALA H CB  1 
ATOM   2703 N N   . SER B  2 128 ? 4.75700   4.17800   -46.60000 1.000 37.25819  ? 115 SER H N   1 
ATOM   2704 C CA  . SER B  2 128 ? 5.53100   3.12300   -45.92000 1.000 37.55600  ? 115 SER H CA  1 
ATOM   2705 C C   . SER B  2 128 ? 6.16400   3.62900   -44.63600 1.000 35.92022  ? 115 SER H C   1 
ATOM   2706 O O   . SER B  2 128 ? 6.55200   4.79700   -44.55000 1.000 38.90541  ? 115 SER H O   1 
ATOM   2707 C CB  . SER B  2 128 ? 6.59100   2.56000   -46.83300 1.000 42.72759  ? 115 SER H CB  1 
ATOM   2708 O OG  . SER B  2 128 ? 7.44500   1.67900   -46.12300 1.000 56.01939  ? 115 SER H OG  1 
ATOM   2709 N N   . THR B  2 129 ? 6.22900   2.74300   -43.67600 1.000 30.83950  ? 116 THR H N   1 
ATOM   2710 C CA  . THR B  2 129 ? 6.92900   3.08700   -42.45700 1.000 33.81609  ? 116 THR H CA  1 
ATOM   2711 C C   . THR B  2 129 ? 8.31100   3.59500   -42.80600 1.000 40.20765  ? 116 THR H C   1 
ATOM   2712 O O   . THR B  2 129 ? 8.88700   3.20800   -43.82400 1.000 39.85788  ? 116 THR H O   1 
ATOM   2713 C CB  . THR B  2 129 ? 6.98100   1.87300   -41.51800 1.000 39.37157  ? 116 THR H CB  1 
ATOM   2714 O OG1 . THR B  2 129 ? 5.63300   1.47900   -41.18000 1.000 43.26197  ? 116 THR H OG1 1 
ATOM   2715 C CG2 . THR B  2 129 ? 7.75800   2.17300   -40.26400 1.000 27.22133  ? 116 THR H CG2 1 
ATOM   2716 N N   . LYS B  2 130 ? 8.83000   4.52200   -42.01200 1.000 31.23707  ? 117 LYS H N   1 
ATOM   2717 C CA  . LYS B  2 130 ? 10.18100  5.01400   -42.18800 1.000 30.42737  ? 117 LYS H CA  1 
ATOM   2718 C C   . LYS B  2 130 ? 10.64600  5.69700   -40.92200 1.000 39.66824  ? 117 LYS H C   1 
ATOM   2719 O O   . LYS B  2 130 ? 9.94400   6.52600   -40.35600 1.000 38.39853  ? 117 LYS H O   1 
ATOM   2720 C CB  . LYS B  2 130 ? 10.33200  6.00900   -43.34400 1.000 34.49092  ? 117 LYS H CB  1 
ATOM   2721 C CG  . LYS B  2 130 ? 11.61000  6.83000   -43.24800 1.000 30.90217  ? 117 LYS H CG  1 
ATOM   2722 C CD  . LYS B  2 130 ? 11.86100  7.67000   -44.48300 1.000 40.89176  ? 117 LYS H CD  1 
ATOM   2723 C CE  . LYS B  2 130 ? 13.33300  8.02500   -44.63100 1.000 40.72460  ? 117 LYS H CE  1 
ATOM   2724 N NZ  . LYS B  2 130 ? 13.88600  8.78700   -43.47700 1.000 40.07785  ? 117 LYS H NZ  1 
ATOM   2725 N N   . GLY B  2 131 ? 11.84000  5.37700   -40.49700 1.000 33.69148  ? 118 GLY H N   1 
ATOM   2726 C CA  . GLY B  2 131 ? 12.38300  6.00700   -39.33000 1.000 34.79600  ? 118 GLY H CA  1 
ATOM   2727 C C   . GLY B  2 131 ? 13.08500  7.31600   -39.58600 1.000 38.01541  ? 118 GLY H C   1 
ATOM   2728 O O   . GLY B  2 131 ? 13.40000  7.65100   -40.70900 1.000 39.56691  ? 118 GLY H O   1 
ATOM   2729 N N   . PRO B  2 132 ? 13.34600  8.05700   -38.52400 1.000 39.95119  ? 119 PRO H N   1 
ATOM   2730 C CA  . PRO B  2 132 ? 13.91600  9.36900   -38.76100 1.000 29.32348  ? 119 PRO H CA  1 
ATOM   2731 C C   . PRO B  2 132 ? 15.38400  9.51300   -38.62800 1.000 29.95789  ? 119 PRO H C   1 
ATOM   2732 O O   . PRO B  2 132 ? 16.06000  8.69300   -38.05200 1.000 30.01934  ? 119 PRO H O   1 
ATOM   2733 C CB  . PRO B  2 132 ? 13.32600  10.18900  -37.61500 1.000 32.47924  ? 119 PRO H CB  1 
ATOM   2734 C CG  . PRO B  2 132 ? 13.14800  9.21100   -36.50700 1.000 36.23545  ? 119 PRO H CG  1 
ATOM   2735 C CD  . PRO B  2 132 ? 12.98500  7.84800   -37.11400 1.000 28.63430  ? 119 PRO H CD  1 
ATOM   2736 N N   . SER B  2 133 ? 15.87100  10.58500  -39.18700 1.000 25.86133  ? 120 SER H N   1 
ATOM   2737 C CA  . SER B  2 133 ? 17.22200  10.92300  -39.03400 1.000 26.21939  ? 120 SER H CA  1 
ATOM   2738 C C   . SER B  2 133 ? 17.18300  11.96100  -37.93000 1.000 34.74019  ? 120 SER H C   1 
ATOM   2739 O O   . SER B  2 133 ? 16.24000  12.73800  -37.84300 1.000 27.80735  ? 120 SER H O   1 
ATOM   2740 C CB  . SER B  2 133 ? 17.76000  11.49800  -40.35100 1.000 30.28878  ? 120 SER H CB  1 
ATOM   2741 O OG  . SER B  2 133 ? 17.26100  10.81500  -41.48000 1.000 39.30633  ? 120 SER H OG  1 
ATOM   2742 N N   . VAL B  2 134 ? 18.17800  11.96400  -37.07600 1.000 25.44225  ? 121 VAL H N   1 
ATOM   2743 C CA  . VAL B  2 134 ? 18.26400  12.96400  -36.03600 1.000 26.80458  ? 121 VAL H CA  1 
ATOM   2744 C C   . VAL B  2 134 ? 19.50800  13.82100  -36.18400 1.000 32.03815  ? 121 VAL H C   1 
ATOM   2745 O O   . VAL B  2 134 ? 20.60500  13.30300  -36.27400 1.000 37.96613  ? 121 VAL H O   1 
ATOM   2746 C CB  . VAL B  2 134 ? 18.23200  12.31800  -34.62700 1.000 28.06414  ? 121 VAL H CB  1 
ATOM   2747 C CG1 . VAL B  2 134 ? 18.40700  13.36700  -33.54800 1.000 28.01906  ? 121 VAL H CG1 1 
ATOM   2748 C CG2 . VAL B  2 134 ? 16.95900  11.52200  -34.43100 1.000 25.53903  ? 121 VAL H CG2 1 
ATOM   2749 N N   . PHE B  2 135 ? 19.34000  15.13000  -36.17900 1.000 30.70619  ? 122 PHE H N   1 
ATOM   2750 C CA  . PHE B  2 135 ? 20.44800  16.03300  -36.33800 1.000 22.58385  ? 122 PHE H CA  1 
ATOM   2751 C C   . PHE B  2 135 ? 20.52300  17.03900  -35.20200 1.000 31.97028  ? 122 PHE H C   1 
ATOM   2752 O O   . PHE B  2 135 ? 19.51700  17.47400  -34.68300 1.000 33.06547  ? 122 PHE H O   1 
ATOM   2753 C CB  . PHE B  2 135 ? 20.34100  16.79700  -37.66200 1.000 27.73574  ? 122 PHE H CB  1 
ATOM   2754 C CG  . PHE B  2 135 ? 20.09900  15.94500  -38.86300 1.000 28.62059  ? 122 PHE H CG  1 
ATOM   2755 C CD1 . PHE B  2 135 ? 21.10200  15.15600  -39.38200 1.000 39.73017  ? 122 PHE H CD1 1 
ATOM   2756 C CD2 . PHE B  2 135 ? 18.88200  15.97500  -39.50400 1.000 31.56997  ? 122 PHE H CD2 1 
ATOM   2757 C CE1 . PHE B  2 135 ? 20.88300  14.38900  -40.50400 1.000 33.82319  ? 122 PHE H CE1 1 
ATOM   2758 C CE2 . PHE B  2 135 ? 18.65700  15.21300  -40.62600 1.000 28.59670  ? 122 PHE H CE2 1 
ATOM   2759 C CZ  . PHE B  2 135 ? 19.66000  14.41700  -41.12700 1.000 30.27453  ? 122 PHE H CZ  1 
ATOM   2760 N N   . PRO B  2 136 ? 21.72400  17.41300  -34.82800 1.000 29.36167  ? 123 PRO H N   1 
ATOM   2761 C CA  . PRO B  2 136 ? 21.88700  18.35700  -33.73500 1.000 32.16119  ? 123 PRO H CA  1 
ATOM   2762 C C   . PRO B  2 136 ? 21.65700  19.81500  -34.06600 1.000 35.93010  ? 123 PRO H C   1 
ATOM   2763 O O   . PRO B  2 136 ? 22.05900  20.26500  -35.12000 1.000 35.66127  ? 123 PRO H O   1 
ATOM   2764 C CB  . PRO B  2 136 ? 23.35600  18.16600  -33.33600 1.000 32.77939  ? 123 PRO H CB  1 
ATOM   2765 C CG  . PRO B  2 136 ? 24.02000  17.73100  -34.59300 1.000 36.02880  ? 123 PRO H CG  1 
ATOM   2766 C CD  . PRO B  2 136 ? 23.01000  16.88900  -35.31300 1.000 34.54326  ? 123 PRO H CD  1 
ATOM   2767 N N   . LEU B  2 137 ? 21.02300  20.53300  -33.15800 1.000 28.60404  ? 124 LEU H N   1 
ATOM   2768 C CA  . LEU B  2 137 ? 20.84400  21.94400  -33.32300 1.000 29.94364  ? 124 LEU H CA  1 
ATOM   2769 C C   . LEU B  2 137 ? 21.80100  22.49800  -32.29400 1.000 29.66675  ? 124 LEU H C   1 
ATOM   2770 O O   . LEU B  2 137 ? 21.46900  22.64500  -31.13600 1.000 24.02497  ? 124 LEU H O   1 
ATOM   2771 C CB  . LEU B  2 137 ? 19.39400  22.32800  -33.12000 1.000 26.16942  ? 124 LEU H CB  1 
ATOM   2772 C CG  . LEU B  2 137 ? 18.43000  21.75100  -34.14700 1.000 29.10303  ? 124 LEU H CG  1 
ATOM   2773 C CD1 . LEU B  2 137 ? 16.99700  21.86300  -33.66600 1.000 25.37741  ? 124 LEU H CD1 1 
ATOM   2774 C CD2 . LEU B  2 137 ? 18.61200  22.46000  -35.47400 1.000 30.04446  ? 124 LEU H CD2 1 
ATOM   2775 N N   . ALA B  2 138 ? 23.01300  22.78300  -32.74100 1.000 29.89647  ? 125 ALA H N   1 
ATOM   2776 C CA  . ALA B  2 138 ? 24.06800  23.22400  -31.84100 1.000 34.60858  ? 125 ALA H CA  1 
ATOM   2777 C C   . ALA B  2 138 ? 23.92300  24.58700  -31.20700 1.000 36.44066  ? 125 ALA H C   1 
ATOM   2778 O O   . ALA B  2 138 ? 23.48600  25.52300  -31.83400 1.000 32.80000  ? 125 ALA H O   1 
ATOM   2779 C CB  . ALA B  2 138 ? 25.39200  23.18400  -32.56800 1.000 39.19330  ? 125 ALA H CB  1 
ATOM   2780 N N   . PRO B  2 139 ? 24.34600  24.67000  -29.94700 1.000 36.81392  ? 126 PRO H N   1 
ATOM   2781 C CA  . PRO B  2 139 ? 24.29600  25.97600  -29.32800 1.000 35.93473  ? 126 PRO H CA  1 
ATOM   2782 C C   . PRO B  2 139 ? 25.33700  26.86100  -30.02500 1.000 47.83578  ? 126 PRO H C   1 
ATOM   2783 O O   . PRO B  2 139 ? 26.46200  26.45800  -30.11100 1.000 50.92691  ? 126 PRO H O   1 
ATOM   2784 C CB  . PRO B  2 139 ? 24.63700  25.71700  -27.85600 1.000 36.03131  ? 126 PRO H CB  1 
ATOM   2785 C CG  . PRO B  2 139 ? 24.61600  24.21800  -27.69600 1.000 41.11900  ? 126 PRO H CG  1 
ATOM   2786 C CD  . PRO B  2 139 ? 24.96000  23.68000  -29.06400 1.000 33.69024  ? 126 PRO H CD  1 
ATOM   2787 N N   . SER B  2 140 ? 24.93200  28.04800  -30.47300 1.000 47.09723  ? 127 SER H N   1 
ATOM   2788 C CA  . SER B  2 140 ? 25.83200  28.91900  -31.27400 1.000 63.73297  ? 127 SER H CA  1 
ATOM   2789 C C   . SER B  2 140 ? 27.04000  29.41300  -30.48400 1.000 67.68639  ? 127 SER H C   1 
ATOM   2790 O O   . SER B  2 140 ? 26.92800  29.58800  -29.25800 1.000 55.02058  ? 127 SER H O   1 
ATOM   2791 C CB  . SER B  2 140 ? 25.07500  30.08000  -31.88200 1.000 68.14114  ? 127 SER H CB  1 
ATOM   2792 O OG  . SER B  2 140 ? 25.94400  30.93600  -32.60800 1.000 77.91232  ? 127 SER H OG  1 
ATOM   2793 N N   . SER B  2 141 ? 28.13200  29.67400  -31.20900 1.000 76.90875  ? 128 SER H N   1 
ATOM   2794 C CA  . SER B  2 141 ? 29.37400  30.19200  -30.59300 1.000 82.85108  ? 128 SER H CA  1 
ATOM   2795 C C   . SER B  2 141 ? 29.11100  31.57600  -30.00500 1.000 87.23449  ? 128 SER H C   1 
ATOM   2796 O O   . SER B  2 141 ? 29.90200  32.01600  -29.16300 1.000 91.80021  ? 128 SER H O   1 
ATOM   2797 C CB  . SER B  2 141 ? 30.47400  30.24000  -31.61300 1.000 75.20109  ? 128 SER H CB  1 
ATOM   2798 O OG  . SER B  2 141 ? 30.05800  30.93500  -32.77800 1.000 75.76910  ? 128 SER H OG  1 
ATOM   2799 N N   . LYS B  2 142 ? 27.93600  32.16800  -30.46800 1.000 90.67539  ? 129 LYS H N   1 
ATOM   2800 C CA  . LYS B  2 142 ? 27.52400  33.46300  -29.92300 1.000 93.62010  ? 129 LYS H CA  1 
ATOM   2801 C C   . LYS B  2 142 ? 26.81800  33.23500  -28.59000 1.000 97.49920  ? 129 LYS H C   1 
ATOM   2802 O O   . LYS B  2 142 ? 25.59800  33.12700  -28.56800 1.000 100.18830 ? 129 LYS H O   1 
ATOM   2803 C CB  . LYS B  2 142 ? 26.66200  34.21300  -30.93400 1.000 78.18036  ? 129 LYS H CB  1 
ATOM   2804 C CG  . LYS B  2 142 ? 27.27700  34.32300  -32.31700 1.000 73.04123  ? 129 LYS H CG  1 
ATOM   2805 C CD  . LYS B  2 142 ? 28.72600  34.76500  -32.25000 1.000 83.53007  ? 129 LYS H CD  1 
ATOM   2806 C CE  . LYS B  2 142 ? 29.14200  35.49400  -33.51700 1.000 78.25928  ? 129 LYS H CE  1 
ATOM   2807 N NZ  . LYS B  2 142 ? 30.38000  36.29400  -33.30100 1.000 67.09149  ? 129 LYS H NZ  1 
ATOM   2808 N N   . SER B  2 143 ? 27.62800  33.21500  -27.44300 1.000 94.57978  ? 130 SER H N   1 
ATOM   2809 C CA  . SER B  2 143 ? 27.00100  32.82300  -26.15100 1.000 87.17428  ? 130 SER H CA  1 
ATOM   2810 C C   . SER B  2 143 ? 26.64900  34.02300  -25.26300 1.000 93.07722  ? 130 SER H C   1 
ATOM   2811 O O   . SER B  2 143 ? 26.52700  35.14000  -25.78700 1.000 98.79622  ? 130 SER H O   1 
ATOM   2812 C CB  . SER B  2 143 ? 27.93100  31.87200  -25.43100 1.000 78.10165  ? 130 SER H CB  1 
ATOM   2813 O OG  . SER B  2 143 ? 29.15700  32.49600  -25.08300 1.000 83.98524  ? 130 SER H OG  1 
ATOM   2814 N N   . THR B  2 144 ? 26.46100  33.78100  -23.96000 1.000 89.86085  ? 131 THR H N   1 
ATOM   2815 C CA  . THR B  2 144 ? 26.16800  34.88700  -23.00800 1.000 88.99798  ? 131 THR H CA  1 
ATOM   2816 C C   . THR B  2 144 ? 25.01900  35.77300  -23.52500 1.000 94.87090  ? 131 THR H C   1 
ATOM   2817 O O   . THR B  2 144 ? 24.91900  36.92300  -23.05200 1.000 93.25828  ? 131 THR H O   1 
ATOM   2818 C CB  . THR B  2 144 ? 27.45600  35.64900  -22.65200 1.000 92.52224  ? 131 THR H CB  1 
ATOM   2819 O OG1 . THR B  2 144 ? 28.37400  34.75100  -22.02700 1.000 93.88886  ? 131 THR H OG1 1 
ATOM   2820 C CG2 . THR B  2 144 ? 27.20200  36.82400  -21.73400 1.000 85.02559  ? 131 THR H CG2 1 
ATOM   2821 N N   . SER B  2 145 ? 24.16500  35.26200  -24.41500 1.000 92.42327  ? 132 SER H N   1 
ATOM   2822 C CA  . SER B  2 145 ? 22.96500  36.01100  -24.87100 1.000 89.16164  ? 132 SER H CA  1 
ATOM   2823 C C   . SER B  2 145 ? 21.87000  35.92000  -23.80700 1.000 91.70664  ? 132 SER H C   1 
ATOM   2824 O O   . SER B  2 145 ? 21.17700  34.89200  -23.76700 1.000 88.06390  ? 132 SER H O   1 
ATOM   2825 C CB  . SER B  2 145 ? 22.46600  35.41800  -26.13600 1.000 83.76304  ? 132 SER H CB  1 
ATOM   2826 O OG  . SER B  2 145 ? 22.57900  34.00300  -26.08800 1.000 64.77365  ? 132 SER H OG  1 
ATOM   2827 N N   . GLY B  2 146 ? 21.68700  36.95600  -22.99100 1.000 82.41076  ? 133 GLY H N   1 
ATOM   2828 C CA  . GLY B  2 146 ? 20.72400  36.84600  -21.87900 1.000 73.96512  ? 133 GLY H CA  1 
ATOM   2829 C C   . GLY B  2 146 ? 21.23400  35.85700  -20.84000 1.000 83.42479  ? 133 GLY H C   1 
ATOM   2830 O O   . GLY B  2 146 ? 20.43500  35.48300  -19.95200 1.000 80.85213  ? 133 GLY H O   1 
ATOM   2831 N N   . GLY B  2 147 ? 22.51000  35.45800  -20.91700 1.000 74.29304  ? 134 GLY H N   1 
ATOM   2832 C CA  . GLY B  2 147 ? 23.03900  34.41000  -20.02400 1.000 63.36694  ? 134 GLY H CA  1 
ATOM   2833 C C   . GLY B  2 147 ? 22.44500  33.06500  -20.39200 1.000 58.15816  ? 134 GLY H C   1 
ATOM   2834 O O   . GLY B  2 147 ? 22.83800  32.05800  -19.79500 1.000 45.59933  ? 134 GLY H O   1 
ATOM   2835 N N   . THR B  2 148 ? 21.54900  33.05900  -21.37600 1.000 54.55266  ? 135 THR H N   1 
ATOM   2836 C CA  . THR B  2 148 ? 20.84200  31.80800  -21.73200 1.000 50.83180  ? 135 THR H CA  1 
ATOM   2837 C C   . THR B  2 148 ? 21.11500  31.41600  -23.18500 1.000 42.62566  ? 135 THR H C   1 
ATOM   2838 O O   . THR B  2 148 ? 21.08400  32.30000  -24.05000 1.000 38.78014  ? 135 THR H O   1 
ATOM   2839 C CB  . THR B  2 148 ? 19.33300  31.95600  -21.51200 1.000 43.37932  ? 135 THR H CB  1 
ATOM   2840 O OG1 . THR B  2 148 ? 19.10000  32.06500  -20.10800 1.000 50.20968  ? 135 THR H OG1 1 
ATOM   2841 C CG2 . THR B  2 148 ? 18.54100  30.80400  -22.09000 1.000 30.59579  ? 135 THR H CG2 1 
ATOM   2842 N N   . ALA B  2 149 ? 21.36200  30.13100  -23.41700 1.000 36.34927  ? 136 ALA H N   1 
ATOM   2843 C CA  . ALA B  2 149 ? 21.55600  29.64000  -24.79000 1.000 29.70817  ? 136 ALA H CA  1 
ATOM   2844 C C   . ALA B  2 149 ? 20.48300  28.60700  -25.10600 1.000 33.86064  ? 136 ALA H C   1 
ATOM   2845 O O   . ALA B  2 149 ? 19.87300  28.07900  -24.17000 1.000 27.27428  ? 136 ALA H O   1 
ATOM   2846 C CB  . ALA B  2 149 ? 22.90700  29.02500  -24.94200 1.000 34.87162  ? 136 ALA H CB  1 
ATOM   2847 N N   . ALA B  2 150 ? 20.30600  28.32600  -26.38900 1.000 27.47643  ? 137 ALA H N   1 
ATOM   2848 C CA  . ALA B  2 150 ? 19.31900  27.34100  -26.81200 1.000 22.27719  ? 137 ALA H CA  1 
ATOM   2849 C C   . ALA B  2 150 ? 19.97000  26.25300  -27.67300 1.000 23.84738  ? 137 ALA H C   1 
ATOM   2850 O O   . ALA B  2 150 ? 20.83000  26.54300  -28.51400 1.000 23.88751  ? 137 ALA H O   1 
ATOM   2851 C CB  . ALA B  2 150 ? 18.18200  28.04400  -27.58400 1.000 20.89962  ? 137 ALA H CB  1 
ATOM   2852 N N   . LEU B  2 151 ? 19.57300  24.99900  -27.46400 1.000 23.41169  ? 138 LEU H N   1 
ATOM   2853 C CA  . LEU B  2 151 ? 20.08400  23.91700  -28.28600 1.000 24.11805  ? 138 LEU H CA  1 
ATOM   2854 C C   . LEU B  2 151 ? 18.93600  22.94400  -28.48200 1.000 22.96689  ? 138 LEU H C   1 
ATOM   2855 O O   . LEU B  2 151 ? 17.90800  23.03700  -27.80900 1.000 24.36816  ? 138 LEU H O   1 
ATOM   2856 C CB  . LEU B  2 151 ? 21.27500  23.20400  -27.63600 1.000 24.36345  ? 138 LEU H CB  1 
ATOM   2857 C CG  . LEU B  2 151 ? 21.07700  22.64500  -26.21600 1.000 31.19543  ? 138 LEU H CG  1 
ATOM   2858 C CD1 . LEU B  2 151 ? 20.83800  21.12100  -26.31500 1.000 34.24071  ? 138 LEU H CD1 1 
ATOM   2859 C CD2 . LEU B  2 151 ? 22.22900  22.94200  -25.26100 1.000 39.56308  ? 138 LEU H CD2 1 
ATOM   2860 N N   . GLY B  2 152 ? 19.14700  21.99000  -29.36200 1.000 25.93391  ? 139 GLY H N   1 
ATOM   2861 C CA  . GLY B  2 152 ? 18.16000  20.97300  -29.58600 1.000 20.44709  ? 139 GLY H CA  1 
ATOM   2862 C C   . GLY B  2 152 ? 18.48600  19.92400  -30.61300 1.000 22.72689  ? 139 GLY H C   1 
ATOM   2863 O O   . GLY B  2 152 ? 19.62700  19.80000  -31.01000 1.000 24.85728  ? 139 GLY H O   1 
ATOM   2864 N N   . CYS B  2 153 ? 17.48800  19.16500  -31.01400 1.000 19.92890  ? 140 CYS H N   1 
ATOM   2865 C CA  . CYS B  2 153 ? 17.63000  18.12600  -31.99900 1.000 20.96400  ? 140 CYS H CA  1 
ATOM   2866 C C   . CYS B  2 153 ? 16.52500  18.18900  -33.05400 1.000 26.81568  ? 140 CYS H C   1 
ATOM   2867 O O   . CYS B  2 153 ? 15.38100  18.42800  -32.71200 1.000 23.75795  ? 140 CYS H O   1 
ATOM   2868 C CB  . CYS B  2 153 ? 17.57900  16.73200  -31.33800 1.000 24.58394  ? 140 CYS H CB  1 
ATOM   2869 S SG  . CYS B  2 153 ? 19.01200  16.24000  -30.38000 1.000 35.97163  ? 140 CYS H SG  1 
ATOM   2870 N N   . LEU B  2 154 ? 16.87600  18.00100  -34.31300 1.000 22.71423  ? 141 LEU H N   1 
ATOM   2871 C CA  . LEU B  2 154 ? 15.89000  17.92500  -35.38600 1.000 26.11955  ? 141 LEU H CA  1 
ATOM   2872 C C   . LEU B  2 154 ? 15.64000  16.47300  -35.74500 1.000 19.96195  ? 141 LEU H C   1 
ATOM   2873 O O   . LEU B  2 154 ? 16.56900  15.75700  -36.02200 1.000 23.40027  ? 141 LEU H O   1 
ATOM   2874 C CB  . LEU B  2 154 ? 16.32300  18.71100  -36.62400 1.000 26.66655  ? 141 LEU H CB  1 
ATOM   2875 C CG  . LEU B  2 154 ? 15.50700  18.63600  -37.91500 1.000 27.28614  ? 141 LEU H CG  1 
ATOM   2876 C CD1 . LEU B  2 154 ? 14.13600  19.26500  -37.75100 1.000 22.55701  ? 141 LEU H CD1 1 
ATOM   2877 C CD2 . LEU B  2 154 ? 16.26100  19.31400  -39.04300 1.000 22.28977  ? 141 LEU H CD2 1 
ATOM   2878 N N   . VAL B  2 155 ? 14.38900  16.05900  -35.73600 1.000 22.65952  ? 142 VAL H N   1 
ATOM   2879 C CA  . VAL B  2 155 ? 14.00400  14.68700  -36.00900 1.000 18.91468  ? 142 VAL H CA  1 
ATOM   2880 C C   . VAL B  2 155 ? 13.24800  14.71200  -37.31900 1.000 22.47417  ? 142 VAL H C   1 
ATOM   2881 O O   . VAL B  2 155 ? 12.07600  15.01600  -37.35100 1.000 26.01858  ? 142 VAL H O   1 
ATOM   2882 C CB  . VAL B  2 155 ? 13.18900  14.10800  -34.83700 1.000 19.67920  ? 142 VAL H CB  1 
ATOM   2883 C CG1 . VAL B  2 155 ? 12.91500  12.63600  -35.05600 1.000 26.11773  ? 142 VAL H CG1 1 
ATOM   2884 C CG2 . VAL B  2 155 ? 13.89000  14.34900  -33.51900 1.000 19.58456  ? 142 VAL H CG2 1 
ATOM   2885 N N   . LYS B  2 156 ? 13.90900  14.34800  -38.39500 1.000 22.60303  ? 143 LYS H N   1 
ATOM   2886 C CA  . LYS B  2 156 ? 13.33400  14.51100  -39.72600 1.000 22.67695  ? 143 LYS H CA  1 
ATOM   2887 C C   . LYS B  2 156 ? 13.02000  13.30000  -40.58100 1.000 28.47669  ? 143 LYS H C   1 
ATOM   2888 O O   . LYS B  2 156 ? 13.69100  12.28100  -40.49900 1.000 24.77488  ? 143 LYS H O   1 
ATOM   2889 C CB  . LYS B  2 156 ? 14.31300  15.36800  -40.53300 1.000 21.99040  ? 143 LYS H CB  1 
ATOM   2890 C CG  . LYS B  2 156 ? 13.79700  15.89800  -41.85600 1.000 32.99840  ? 143 LYS H CG  1 
ATOM   2891 C CD  . LYS B  2 156 ? 14.91100  16.58000  -42.63100 1.000 31.53661  ? 143 LYS H CD  1 
ATOM   2892 C CE  . LYS B  2 156 ? 14.37600  17.65000  -43.56300 1.000 25.90314  ? 143 LYS H CE  1 
ATOM   2893 N NZ  . LYS B  2 156 ? 13.29900  17.13200  -44.43700 1.000 32.10921  ? 143 LYS H NZ  1 
ATOM   2894 N N   . ASP B  2 157 ? 12.00900  13.44100  -41.41200 1.000 22.70167  ? 144 ASP H N   1 
ATOM   2895 C CA  . ASP B  2 157 ? 11.69200  12.42100  -42.38100 1.000 27.95467  ? 144 ASP H CA  1 
ATOM   2896 C C   . ASP B  2 157 ? 11.32600  11.07600  -41.79800 1.000 33.87666  ? 144 ASP H C   1 
ATOM   2897 O O   . ASP B  2 157 ? 12.07700  10.12800  -41.92800 1.000 31.94443  ? 144 ASP H O   1 
ATOM   2898 C CB  . ASP B  2 157 ? 12.86100  12.29800  -43.38700 1.000 23.40713  ? 144 ASP H CB  1 
ATOM   2899 C CG  . ASP B  2 157 ? 13.08300  13.56400  -44.17500 1.000 28.32487  ? 144 ASP H CG  1 
ATOM   2900 O OD1 . ASP B  2 157 ? 12.14000  14.36100  -44.30300 1.000 32.74158  ? 144 ASP H OD1 1 
ATOM   2901 O OD2 . ASP B  2 157 ? 14.20100  13.76500  -44.66000 1.000 30.02738  ? 144 ASP H OD2 1 
ATOM   2902 N N   . TYR B  2 158 ? 10.16500  11.01300  -41.16900 1.000 25.24275  ? 145 TYR H N   1 
ATOM   2903 C CA  . TYR B  2 158 ? 9.69100   9.77100   -40.60400 1.000 26.75311  ? 145 TYR H CA  1 
ATOM   2904 C C   . TYR B  2 158 ? 8.22000   9.51600   -40.84900 1.000 27.66793  ? 145 TYR H C   1 
ATOM   2905 O O   . TYR B  2 158 ? 7.48700   10.43100  -41.17100 1.000 27.97336  ? 145 TYR H O   1 
ATOM   2906 C CB  . TYR B  2 158 ? 9.98600   9.71300   -39.10600 1.000 29.10948  ? 145 TYR H CB  1 
ATOM   2907 C CG  . TYR B  2 158 ? 9.16200   10.64600  -38.24600 1.000 27.75737  ? 145 TYR H CG  1 
ATOM   2908 C CD1 . TYR B  2 158 ? 7.88300   10.30100  -37.84200 1.000 31.99588  ? 145 TYR H CD1 1 
ATOM   2909 C CD2 . TYR B  2 158 ? 9.67300   11.85400  -37.81700 1.000 26.17739  ? 145 TYR H CD2 1 
ATOM   2910 C CE1 . TYR B  2 158 ? 7.13500   11.14000  -37.04900 1.000 25.76220  ? 145 TYR H CE1 1 
ATOM   2911 C CE2 . TYR B  2 158 ? 8.93100   12.70100  -37.02400 1.000 27.19115  ? 145 TYR H CE2 1 
ATOM   2912 C CZ  . TYR B  2 158 ? 7.66300   12.33600  -36.64300 1.000 28.46046  ? 145 TYR H CZ  1 
ATOM   2913 O OH  . TYR B  2 158 ? 6.92000   13.17200  -35.85800 1.000 27.66044  ? 145 TYR H OH  1 
ATOM   2914 N N   . PHE B  2 159 ? 7.78700   8.28900   -40.66000 1.000 29.05175  ? 146 PHE H N   1 
ATOM   2915 C CA  . PHE B  2 159 ? 6.40700   7.89600   -40.84400 1.000 29.48164  ? 146 PHE H CA  1 
ATOM   2916 C C   . PHE B  2 159 ? 6.26800   6.54000   -40.16300 1.000 29.18400  ? 146 PHE H C   1 
ATOM   2917 O O   . PHE B  2 159 ? 7.20700   5.77200   -40.11900 1.000 33.02142  ? 146 PHE H O   1 
ATOM   2918 C CB  . PHE B  2 159 ? 6.05400   7.82200   -42.32900 1.000 30.92202  ? 146 PHE H CB  1 
ATOM   2919 C CG  . PHE B  2 159 ? 4.59200   7.77800   -42.62800 1.000 32.63518  ? 146 PHE H CG  1 
ATOM   2920 C CD1 . PHE B  2 159 ? 3.86000   8.94200   -42.72900 1.000 29.20606  ? 146 PHE H CD1 1 
ATOM   2921 C CD2 . PHE B  2 159 ? 3.96000   6.57400   -42.85900 1.000 33.87517  ? 146 PHE H CD2 1 
ATOM   2922 C CE1 . PHE B  2 159 ? 2.51400   8.90400   -43.01700 1.000 27.79442  ? 146 PHE H CE1 1 
ATOM   2923 C CE2 . PHE B  2 159 ? 2.61500   6.52700   -43.15800 1.000 28.65642  ? 146 PHE H CE2 1 
ATOM   2924 C CZ  . PHE B  2 159 ? 1.88900   7.69400   -43.23500 1.000 31.24656  ? 146 PHE H CZ  1 
ATOM   2925 N N   . PRO B  2 160 ? 5.08900   6.24400   -39.63400 1.000 35.78995  ? 147 PRO H N   1 
ATOM   2926 C CA  . PRO B  2 160 ? 4.05300   7.21500   -39.29500 1.000 32.85159  ? 147 PRO H CA  1 
ATOM   2927 C C   . PRO B  2 160 ? 4.28200   7.84600   -37.94900 1.000 25.23126  ? 147 PRO H C   1 
ATOM   2928 O O   . PRO B  2 160 ? 5.29600   7.61600   -37.33300 1.000 27.25534  ? 147 PRO H O   1 
ATOM   2929 C CB  . PRO B  2 160 ? 2.82500   6.34600   -39.18200 1.000 33.28768  ? 147 PRO H CB  1 
ATOM   2930 C CG  . PRO B  2 160 ? 3.34300   5.06900   -38.63600 1.000 33.91422  ? 147 PRO H CG  1 
ATOM   2931 C CD  . PRO B  2 160 ? 4.72100   4.88800   -39.20100 1.000 33.62153  ? 147 PRO H CD  1 
ATOM   2932 N N   . GLU B  2 161 ? 3.35600   8.68200   -37.51400 1.000 27.21989  ? 148 GLU H N   1 
ATOM   2933 C CA  . GLU B  2 161 ? 3.44000   9.19800   -36.17100 1.000 28.71753  ? 148 GLU H CA  1 
ATOM   2934 C C   . GLU B  2 161 ? 3.19900   7.99600   -35.24300 1.000 29.60668  ? 148 GLU H C   1 
ATOM   2935 O O   . GLU B  2 161 ? 2.53300   7.06500   -35.61700 1.000 26.62664  ? 148 GLU H O   1 
ATOM   2936 C CB  . GLU B  2 161 ? 2.40400   10.28800  -35.92700 1.000 25.51396  ? 148 GLU H CB  1 
ATOM   2937 C CG  . GLU B  2 161 ? 2.72700   11.60800  -36.59300 1.000 26.42218  ? 148 GLU H CG  1 
ATOM   2938 C CD  . GLU B  2 161 ? 3.47800   12.52800  -35.66600 1.000 31.41545  ? 148 GLU H CD  1 
ATOM   2939 O OE1 . GLU B  2 161 ? 4.59000   12.16900  -35.25300 1.000 27.62667  ? 148 GLU H OE1 1 
ATOM   2940 O OE2 . GLU B  2 161 ? 2.94000   13.59200  -35.33200 1.000 33.12339  ? 148 GLU H OE2 1 
ATOM   2941 N N   . PRO B  2 162 ? 3.73600   8.04800   -34.03000 1.000 30.87307  ? 149 PRO H N   1 
ATOM   2942 C CA  . PRO B  2 162 ? 4.37300   9.18400   -33.38500 1.000 22.92168  ? 149 PRO H CA  1 
ATOM   2943 C C   . PRO B  2 162 ? 5.81000   8.97100   -32.99500 1.000 31.80953  ? 149 PRO H C   1 
ATOM   2944 O O   . PRO B  2 162 ? 6.33200   7.88600   -33.12900 1.000 34.95763  ? 149 PRO H O   1 
ATOM   2945 C CB  . PRO B  2 162 ? 3.59500   9.27500   -32.08800 1.000 25.81646  ? 149 PRO H CB  1 
ATOM   2946 C CG  . PRO B  2 162 ? 3.31800   7.84700   -31.74200 1.000 30.91239  ? 149 PRO H CG  1 
ATOM   2947 C CD  . PRO B  2 162 ? 3.32800   7.05300   -33.02500 1.000 28.55358  ? 149 PRO H CD  1 
ATOM   2948 N N   . VAL B  2 163 ? 6.43400   10.01500  -32.49800 1.000 29.74753  ? 150 VAL H N   1 
ATOM   2949 C CA  . VAL B  2 163 ? 7.78200   9.91200   -32.02900 1.000 29.96234  ? 150 VAL H CA  1 
ATOM   2950 C C   . VAL B  2 163 ? 7.80200   10.49900  -30.63800 1.000 32.70039  ? 150 VAL H C   1 
ATOM   2951 O O   . VAL B  2 163 ? 6.97800   11.31800  -30.30800 1.000 29.53794  ? 150 VAL H O   1 
ATOM   2952 C CB  . VAL B  2 163 ? 8.75200   10.67000  -32.94600 1.000 31.21902  ? 150 VAL H CB  1 
ATOM   2953 C CG1 . VAL B  2 163 ? 10.06700  10.97500  -32.25600 1.000 37.93171  ? 150 VAL H CG1 1 
ATOM   2954 C CG2 . VAL B  2 163 ? 8.96700   9.91100   -34.23900 1.000 31.02534  ? 150 VAL H CG2 1 
ATOM   2955 N N   . THR B  2 164 ? 8.72700   10.03800  -29.82600 1.000 25.48904  ? 151 THR H N   1 
ATOM   2956 C CA  . THR B  2 164 ? 8.85700   10.59900  -28.51600 1.000 29.52387  ? 151 THR H CA  1 
ATOM   2957 C C   . THR B  2 164 ? 10.27900  11.04900  -28.31700 1.000 32.31821  ? 151 THR H C   1 
ATOM   2958 O O   . THR B  2 164 ? 11.19900  10.45300  -28.83200 1.000 27.81978  ? 151 THR H O   1 
ATOM   2959 C CB  . THR B  2 164 ? 8.38400   9.63400   -27.41900 1.000 29.89412  ? 151 THR H CB  1 
ATOM   2960 O OG1 . THR B  2 164 ? 7.07900   9.15500   -27.74700 1.000 44.90081  ? 151 THR H OG1 1 
ATOM   2961 C CG2 . THR B  2 164 ? 8.31300   10.34500  -26.10200 1.000 47.93752  ? 151 THR H CG2 1 
ATOM   2962 N N   . VAL B  2 165 ? 10.43100  12.15200  -27.62100 1.000 32.69007  ? 152 VAL H N   1 
ATOM   2963 C CA  . VAL B  2 165 ? 11.72600  12.69700  -27.36700 1.000 26.55998  ? 152 VAL H CA  1 
ATOM   2964 C C   . VAL B  2 165 ? 11.93600  13.05600  -25.90800 1.000 29.07090  ? 152 VAL H C   1 
ATOM   2965 O O   . VAL B  2 165 ? 11.06300  13.59900  -25.25900 1.000 27.06721  ? 152 VAL H O   1 
ATOM   2966 C CB  . VAL B  2 165 ? 11.99300  13.94100  -28.25700 1.000 23.13616  ? 152 VAL H CB  1 
ATOM   2967 C CG1 . VAL B  2 165 ? 13.41500  14.43600  -28.08400 1.000 23.21340  ? 152 VAL H CG1 1 
ATOM   2968 C CG2 . VAL B  2 165 ? 11.66300  13.67000  -29.70900 1.000 23.79498  ? 152 VAL H CG2 1 
ATOM   2969 N N   . SER B  2 166 ? 13.10900  12.73500  -25.41600 1.000 25.62911  ? 153 SER H N   1 
ATOM   2970 C CA  . SER B  2 166 ? 13.47400  13.05000  -24.04100 1.000 26.68758  ? 153 SER H CA  1 
ATOM   2971 C C   . SER B  2 166 ? 14.86400  13.66200  -24.02800 1.000 26.88332  ? 153 SER H C   1 
ATOM   2972 O O   . SER B  2 166 ? 15.59300  13.58300  -25.00200 1.000 34.57266  ? 153 SER H O   1 
ATOM   2973 C CB  . SER B  2 166 ? 13.47500  11.80300  -23.14400 1.000 35.05228  ? 153 SER H CB  1 
ATOM   2974 O OG  . SER B  2 166 ? 14.76700  11.26400  -22.99200 1.000 29.60355  ? 153 SER H OG  1 
ATOM   2975 N N   . TRP B  2 167 ? 15.26600  14.26000  -22.92800 1.000 22.64278  ? 154 TRP H N   1 
ATOM   2976 C CA  . TRP B  2 167 ? 16.61800  14.77600  -22.81000 1.000 25.91248  ? 154 TRP H CA  1 
ATOM   2977 C C   . TRP B  2 167 ? 17.40300  14.23700  -21.58200 1.000 31.62227  ? 154 TRP H C   1 
ATOM   2978 O O   . TRP B  2 167 ? 16.89400  14.23300  -20.48100 1.000 28.43584  ? 154 TRP H O   1 
ATOM   2979 C CB  . TRP B  2 167 ? 16.63900  16.29400  -22.80100 1.000 30.77441  ? 154 TRP H CB  1 
ATOM   2980 C CG  . TRP B  2 167 ? 16.37100  16.94600  -24.11900 1.000 30.13913  ? 154 TRP H CG  1 
ATOM   2981 C CD1 . TRP B  2 167 ? 15.15700  17.23200  -24.65300 1.000 27.02209  ? 154 TRP H CD1 1 
ATOM   2982 C CD2 . TRP B  2 167 ? 17.34100  17.41100  -25.06000 1.000 27.35417  ? 154 TRP H CD2 1 
ATOM   2983 N NE1 . TRP B  2 167 ? 15.30200  17.83300  -25.87000 1.000 23.65129  ? 154 TRP H NE1 1 
ATOM   2984 C CE2 . TRP B  2 167 ? 16.63500  17.95700  -26.14700 1.000 29.62432  ? 154 TRP H CE2 1 
ATOM   2985 C CE3 . TRP B  2 167 ? 18.73600  17.41100  -25.09400 1.000 26.14614  ? 154 TRP H CE3 1 
ATOM   2986 C CZ2 . TRP B  2 167 ? 17.27600  18.49800  -27.25400 1.000 23.72403  ? 154 TRP H CZ2 1 
ATOM   2987 C CZ3 . TRP B  2 167 ? 19.37000  17.95100  -26.19200 1.000 24.38874  ? 154 TRP H CZ3 1 
ATOM   2988 C CH2 . TRP B  2 167 ? 18.64100  18.48400  -27.25900 1.000 25.55449  ? 154 TRP H CH2 1 
ATOM   2989 N N   . ASN B  2 168 ? 18.64300  13.82100  -21.80600 1.000 28.25839  ? 155 ASN H N   1 
ATOM   2990 C CA  . ASN B  2 168 ? 19.50800  13.31000  -20.70900 1.000 31.43515  ? 155 ASN H CA  1 
ATOM   2991 C C   . ASN B  2 168 ? 18.78000  12.17600  -19.98300 1.000 28.46504  ? 155 ASN H C   1 
ATOM   2992 O O   . ASN B  2 168 ? 18.86700  12.12500  -18.75300 1.000 31.54986  ? 155 ASN H O   1 
ATOM   2993 C CB  . ASN B  2 168 ? 19.98200  14.45500  -19.81700 1.000 32.37259  ? 155 ASN H CB  1 
ATOM   2994 C CG  . ASN B  2 168 ? 21.04100  15.32000  -20.46300 1.000 33.24114  ? 155 ASN H CG  1 
ATOM   2995 O OD1 . ASN B  2 168 ? 21.45600  15.06200  -21.58800 1.000 35.85199  ? 155 ASN H OD1 1 
ATOM   2996 N ND2 . ASN B  2 168 ? 21.48400  16.34300  -19.75400 1.000 25.87052  ? 155 ASN H ND2 1 
ATOM   2997 N N   . SER B  2 169 ? 18.05900  11.35200  -20.72900 1.000 30.83792  ? 156 SER H N   1 
ATOM   2998 C CA  . SER B  2 169 ? 17.33800  10.17300  -20.18600 1.000 34.80842  ? 156 SER H CA  1 
ATOM   2999 C C   . SER B  2 169 ? 16.29500  10.56400  -19.12300 1.000 37.31921  ? 156 SER H C   1 
ATOM   3000 O O   . SER B  2 169 ? 15.94500  9.69700   -18.32900 1.000 43.01265  ? 156 SER H O   1 
ATOM   3001 C CB  . SER B  2 169 ? 18.32700  9.10400   -19.74400 1.000 35.81272  ? 156 SER H CB  1 
ATOM   3002 O OG  . SER B  2 169 ? 19.39500  8.98300   -20.66600 1.000 36.66024  ? 156 SER H OG  1 
ATOM   3003 N N   . GLY B  2 170 ? 15.76800  11.79300  -19.16800 1.000 33.61935  ? 157 GLY H N   1 
ATOM   3004 C CA  . GLY B  2 170 ? 14.68100  12.21600  -18.25600 1.000 29.85042  ? 157 GLY H CA  1 
ATOM   3005 C C   . GLY B  2 170 ? 15.16300  13.19000  -17.21200 1.000 32.94333  ? 157 GLY H C   1 
ATOM   3006 O O   . GLY B  2 170 ? 14.32400  13.76700  -16.52300 1.000 37.73632  ? 157 GLY H O   1 
ATOM   3007 N N   . ALA B  2 171 ? 16.45900  13.40800  -17.14400 1.000 30.10220  ? 158 ALA H N   1 
ATOM   3008 C CA  . ALA B  2 171 ? 17.03900  14.28800  -16.14100 1.000 34.66295  ? 158 ALA H CA  1 
ATOM   3009 C C   . ALA B  2 171 ? 16.96900  15.75400  -16.49200 1.000 35.93188  ? 158 ALA H C   1 
ATOM   3010 O O   . ALA B  2 171 ? 17.18300  16.58900  -15.64800 1.000 36.47075  ? 158 ALA H O   1 
ATOM   3011 C CB  . ALA B  2 171 ? 18.47300  13.89600  -15.91300 1.000 31.17209  ? 158 ALA H CB  1 
ATOM   3012 N N   . LEU B  2 172 ? 16.69100  16.05300  -17.74900 1.000 32.66664  ? 159 LEU H N   1 
ATOM   3013 C CA  . LEU B  2 172 ? 16.52400  17.43900  -18.15400 1.000 36.92802  ? 159 LEU H CA  1 
ATOM   3014 C C   . LEU B  2 172 ? 15.13000  17.62500  -18.69100 1.000 35.04671  ? 159 LEU H C   1 
ATOM   3015 O O   . LEU B  2 172 ? 14.79400  17.08000  -19.72600 1.000 35.86357  ? 159 LEU H O   1 
ATOM   3016 C CB  . LEU B  2 172 ? 17.58100  17.86000  -19.17700 1.000 33.51320  ? 159 LEU H CB  1 
ATOM   3017 C CG  . LEU B  2 172 ? 17.45100  19.23600  -19.81200 1.000 26.26518  ? 159 LEU H CG  1 
ATOM   3018 C CD1 . LEU B  2 172 ? 17.58300  20.31700  -18.75400 1.000 27.32645  ? 159 LEU H CD1 1 
ATOM   3019 C CD2 . LEU B  2 172 ? 18.53300  19.37300  -20.86400 1.000 31.38350  ? 159 LEU H CD2 1 
ATOM   3020 N N   . THR B  2 173 ? 14.32100  18.38900  -17.97300 1.000 30.20451  ? 160 THR H N   1 
ATOM   3021 C CA  . THR B  2 173 ? 12.95500  18.62900  -18.38500 1.000 21.88283  ? 160 THR H CA  1 
ATOM   3022 C C   . THR B  2 173 ? 12.63100  20.12700  -18.35400 1.000 32.88700  ? 160 THR H C   1 
ATOM   3023 O O   . THR B  2 173 ? 11.85200  20.62400  -19.14100 1.000 29.19039  ? 160 THR H O   1 
ATOM   3024 C CB  . THR B  2 173 ? 11.97900  17.83200  -17.50300 1.000 31.45678  ? 160 THR H CB  1 
ATOM   3025 O OG1 . THR B  2 173 ? 12.16300  18.21200  -16.13300 1.000 34.59953  ? 160 THR H OG1 1 
ATOM   3026 C CG2 . THR B  2 173 ? 12.20900  16.34000  -17.64600 1.000 28.66778  ? 160 THR H CG2 1 
ATOM   3027 N N   . SER B  2 174 ? 13.24500  20.84500  -17.44800 1.000 31.00878  ? 161 SER H N   1 
ATOM   3028 C CA  . SER B  2 174 ? 12.97200  22.24600  -17.35300 1.000 33.97121  ? 161 SER H CA  1 
ATOM   3029 C C   . SER B  2 174 ? 13.37500  22.90300  -18.64700 1.000 37.83872  ? 161 SER H C   1 
ATOM   3030 O O   . SER B  2 174 ? 14.45500  22.66100  -19.16000 1.000 30.22581  ? 161 SER H O   1 
ATOM   3031 C CB  . SER B  2 174 ? 13.71400  22.89900  -16.17000 1.000 26.83259  ? 161 SER H CB  1 
ATOM   3032 O OG  . SER B  2 174 ? 13.86000  24.28600  -16.34600 1.000 47.78992  ? 161 SER H OG  1 
ATOM   3033 N N   . GLY B  2 175 ? 12.48000  23.70400  -19.19300 1.000 29.90470  ? 162 GLY H N   1 
ATOM   3034 C CA  . GLY B  2 175 ? 12.88600  24.47700  -20.37800 1.000 25.53714  ? 162 GLY H CA  1 
ATOM   3035 C C   . GLY B  2 175 ? 12.90000  23.68500  -21.66600 1.000 25.08639  ? 162 GLY H C   1 
ATOM   3036 O O   . GLY B  2 175 ? 13.31700  24.27200  -22.66800 1.000 28.96857  ? 162 GLY H O   1 
ATOM   3037 N N   . VAL B  2 176 ? 12.43000  22.46400  -21.67600 1.000 24.00583  ? 163 VAL H N   1 
ATOM   3038 C CA  . VAL B  2 176 ? 12.34500  21.71400  -22.89300 1.000 21.57046  ? 163 VAL H CA  1 
ATOM   3039 C C   . VAL B  2 176 ? 11.06600  22.06000  -23.65200 1.000 24.33902  ? 163 VAL H C   1 
ATOM   3040 O O   . VAL B  2 176 ? 10.03300  22.23900  -23.04900 1.000 23.50516  ? 163 VAL H O   1 
ATOM   3041 C CB  . VAL B  2 176 ? 12.43700  20.17400  -22.62900 1.000 18.58059  ? 163 VAL H CB  1 
ATOM   3042 C CG1 . VAL B  2 176 ? 12.17400  19.38100  -23.89300 1.000 21.07079  ? 163 VAL H CG1 1 
ATOM   3043 C CG2 . VAL B  2 176 ? 13.77900  19.80900  -22.02100 1.000 23.58305  ? 163 VAL H CG2 1 
ATOM   3044 N N   . HIS B  2 177 ? 11.15200  22.17100  -24.96500 1.000 17.91748  ? 164 HIS H N   1 
ATOM   3045 C CA  . HIS B  2 177 ? 9.97500   22.36600  -25.78700 1.000 19.76908  ? 164 HIS H CA  1 
ATOM   3046 C C   . HIS B  2 177 ? 10.10900  21.39000  -26.95600 1.000 22.48814  ? 164 HIS H C   1 
ATOM   3047 O O   . HIS B  2 177 ? 10.96600  21.55100  -27.80200 1.000 24.94054  ? 164 HIS H O   1 
ATOM   3048 C CB  . HIS B  2 177 ? 9.79800   23.80200  -26.27600 1.000 15.84612  ? 164 HIS H CB  1 
ATOM   3049 C CG  . HIS B  2 177 ? 9.46700   24.80100  -25.21800 1.000 16.80152  ? 164 HIS H CG  1 
ATOM   3050 N ND1 . HIS B  2 177 ? 8.38000   24.68000  -24.38600 1.000 17.38205  ? 164 HIS H ND1 1 
ATOM   3051 C CD2 . HIS B  2 177 ? 10.05900  25.97200  -24.89500 1.000 20.39378  ? 164 HIS H CD2 1 
ATOM   3052 C CE1 . HIS B  2 177 ? 8.32800   25.72300  -23.58100 1.000 20.21070  ? 164 HIS H CE1 1 
ATOM   3053 N NE2 . HIS B  2 177 ? 9.33700   26.52200  -23.86900 1.000 27.27610  ? 164 HIS H NE2 1 
ATOM   3054 N N   . THR B  2 178 ? 9.31000   20.35500  -26.95100 1.000 24.39484  ? 165 THR H N   1 
ATOM   3055 C CA  . THR B  2 178 ? 9.30600   19.39100  -28.02300 1.000 23.33213  ? 165 THR H CA  1 
ATOM   3056 C C   . THR B  2 178 ? 8.07200   19.70500  -28.87500 1.000 26.85992  ? 165 THR H C   1 
ATOM   3057 O O   . THR B  2 178 ? 6.94800   19.55100  -28.43000 1.000 23.99888  ? 165 THR H O   1 
ATOM   3058 C CB  . THR B  2 178 ? 9.38000   17.91500  -27.49200 1.000 20.70547  ? 165 THR H CB  1 
ATOM   3059 O OG1 . THR B  2 178 ? 10.58900  17.71300  -26.76500 1.000 22.25164  ? 165 THR H OG1 1 
ATOM   3060 C CG2 . THR B  2 178 ? 9.29300   16.93600  -28.64500 1.000 22.97570  ? 165 THR H CG2 1 
ATOM   3061 N N   . PHE B  2 179 ? 8.29700   20.16200  -30.09500 1.000 20.21827  ? 166 PHE H N   1 
ATOM   3062 C CA  . PHE B  2 179 ? 7.18300   20.60300  -30.93300 1.000 17.77953  ? 166 PHE H CA  1 
ATOM   3063 C C   . PHE B  2 179 ? 6.37100   19.53100  -31.62200 1.000 17.19732  ? 166 PHE H C   1 
ATOM   3064 O O   . PHE B  2 179 ? 6.86300   18.49600  -31.94900 1.000 18.11903  ? 166 PHE H O   1 
ATOM   3065 C CB  . PHE B  2 179 ? 7.68300   21.59400  -32.01500 1.000 19.87241  ? 166 PHE H CB  1 
ATOM   3066 C CG  . PHE B  2 179 ? 8.21100   22.88300  -31.47800 1.000 16.94133  ? 166 PHE H CG  1 
ATOM   3067 C CD1 . PHE B  2 179 ? 7.37600   23.96500  -31.31300 1.000 14.09210  ? 166 PHE H CD1 1 
ATOM   3068 C CD2 . PHE B  2 179 ? 9.55000   23.01900  -31.16000 1.000 17.90866  ? 166 PHE H CD2 1 
ATOM   3069 C CE1 . PHE B  2 179 ? 7.86000   25.15900  -30.82500 1.000 15.83259  ? 166 PHE H CE1 1 
ATOM   3070 C CE2 . PHE B  2 179 ? 10.04000  24.21100  -30.66900 1.000 17.21083  ? 166 PHE H CE2 1 
ATOM   3071 C CZ  . PHE B  2 179 ? 9.19400   25.28300  -30.50000 1.000 15.08253  ? 166 PHE H CZ  1 
ATOM   3072 N N   . PRO B  2 180 ? 5.10300   19.84500  -31.86600 1.000 21.29238  ? 167 PRO H N   1 
ATOM   3073 C CA  . PRO B  2 180 ? 4.31800   18.91100  -32.64900 1.000 19.70582  ? 167 PRO H CA  1 
ATOM   3074 C C   . PRO B  2 180 ? 4.92500   18.75900  -34.05400 1.000 22.33609  ? 167 PRO H C   1 
ATOM   3075 O O   . PRO B  2 180 ? 5.41600   19.72200  -34.61200 1.000 16.66690  ? 167 PRO H O   1 
ATOM   3076 C CB  . PRO B  2 180 ? 2.94400   19.56700  -32.71500 1.000 18.26228  ? 167 PRO H CB  1 
ATOM   3077 C CG  . PRO B  2 180 ? 2.91400   20.55400  -31.60700 1.000 28.47054  ? 167 PRO H CG  1 
ATOM   3078 C CD  . PRO B  2 180 ? 4.32200   21.00000  -31.40600 1.000 20.66557  ? 167 PRO H CD  1 
ATOM   3079 N N   . ALA B  2 181 ? 4.89400   17.54900  -34.57700 1.000 20.27645  ? 168 ALA H N   1 
ATOM   3080 C CA  . ALA B  2 181 ? 5.43200   17.29700  -35.91800 1.000 20.80667  ? 168 ALA H CA  1 
ATOM   3081 C C   . ALA B  2 181 ? 4.63000   18.04800  -36.98500 1.000 21.62050  ? 168 ALA H C   1 
ATOM   3082 O O   . ALA B  2 181 ? 3.42600   18.28100  -36.83200 1.000 21.95149  ? 168 ALA H O   1 
ATOM   3083 C CB  . ALA B  2 181 ? 5.39300   15.79800  -36.22700 1.000 22.28112  ? 168 ALA H CB  1 
ATOM   3084 N N   . VAL B  2 182 ? 5.28900   18.38800  -38.10500 1.000 20.05699  ? 169 VAL H N   1 
ATOM   3085 C CA  . VAL B  2 182 ? 4.57500   18.89900  -39.27500 1.000 19.58088  ? 169 VAL H CA  1 
ATOM   3086 C C   . VAL B  2 182 ? 4.62600   17.81900  -40.33700 1.000 25.75340  ? 169 VAL H C   1 
ATOM   3087 O O   . VAL B  2 182 ? 5.51400   16.96000  -40.33800 1.000 21.38399  ? 169 VAL H O   1 
ATOM   3088 C CB  . VAL B  2 182 ? 5.16800   20.21800  -39.82500 1.000 21.44375  ? 169 VAL H CB  1 
ATOM   3089 C CG1 . VAL B  2 182 ? 5.07400   21.31300  -38.76200 1.000 24.09897  ? 169 VAL H CG1 1 
ATOM   3090 C CG2 . VAL B  2 182 ? 6.60500   20.05100  -40.31300 1.000 18.08762  ? 169 VAL H CG2 1 
ATOM   3091 N N   . LEU B  2 183 ? 3.66500   17.85300  -41.23400 1.000 24.94669  ? 170 LEU H N   1 
ATOM   3092 C CA  . LEU B  2 183 ? 3.65500   16.94900  -42.38300 1.000 22.32636  ? 170 LEU H CA  1 
ATOM   3093 C C   . LEU B  2 183 ? 4.35200   17.69100  -43.51700 1.000 25.28127  ? 170 LEU H C   1 
ATOM   3094 O O   . LEU B  2 183 ? 3.83800   18.70200  -44.00400 1.000 20.08342  ? 170 LEU H O   1 
ATOM   3095 C CB  . LEU B  2 183 ? 2.21900   16.54500  -42.75400 1.000 22.31377  ? 170 LEU H CB  1 
ATOM   3096 C CG  . LEU B  2 183 ? 2.03000   15.53500  -43.88800 1.000 31.60886  ? 170 LEU H CG  1 
ATOM   3097 C CD1 . LEU B  2 183 ? 2.76900   14.27100  -43.48700 1.000 29.91627  ? 170 LEU H CD1 1 
ATOM   3098 C CD2 . LEU B  2 183 ? 0.57100   15.21400  -44.18700 1.000 27.58311  ? 170 LEU H CD2 1 
ATOM   3099 N N   . GLN B  2 184 ? 5.54600   17.23400  -43.90200 1.000 25.97366  ? 171 GLN H N   1 
ATOM   3100 C CA  . GLN B  2 184 ? 6.24200   17.91600  -44.98500 1.000 27.83774  ? 171 GLN H CA  1 
ATOM   3101 C C   . GLN B  2 184 ? 5.59800   17.59300  -46.33400 1.000 26.72470  ? 171 GLN H C   1 
ATOM   3102 O O   . GLN B  2 184 ? 4.80900   16.66500  -46.46200 1.000 27.41691  ? 171 GLN H O   1 
ATOM   3103 C CB  . GLN B  2 184 ? 7.71000   17.52600  -45.00000 1.000 24.64496  ? 171 GLN H CB  1 
ATOM   3104 C CG  . GLN B  2 184 ? 8.41500   17.83300  -43.74000 1.000 18.94430  ? 171 GLN H CG  1 
ATOM   3105 C CD  . GLN B  2 184 ? 9.68800   17.10000  -43.67300 1.000 28.77067  ? 171 GLN H CD  1 
ATOM   3106 O OE1 . GLN B  2 184 ? 10.75800  17.68200  -43.77600 1.000 31.65987  ? 171 GLN H OE1 1 
ATOM   3107 N NE2 . GLN B  2 184 ? 9.59800   15.78400  -43.53300 1.000 27.72969  ? 171 GLN H NE2 1 
ATOM   3108 N N   . SER B  2 185 ? 5.95300   18.37900  -47.36600 1.000 32.04349  ? 172 SER H N   1 
ATOM   3109 C CA  . SER B  2 185 ? 5.40300   18.13900  -48.70300 1.000 31.77998  ? 172 SER H CA  1 
ATOM   3110 C C   . SER B  2 185 ? 5.82100   16.77700  -49.25400 1.000 27.38800  ? 172 SER H C   1 
ATOM   3111 O O   . SER B  2 185 ? 5.14300   16.25600  -50.14400 1.000 29.07500  ? 172 SER H O   1 
ATOM   3112 C CB  . SER B  2 185 ? 5.80400   19.28500  -49.65200 1.000 29.29753  ? 172 SER H CB  1 
ATOM   3113 O OG  . SER B  2 185 ? 7.21300   19.42400  -49.70000 1.000 34.21324  ? 172 SER H OG  1 
ATOM   3114 N N   . SER B  2 186 ? 6.84500   16.15200  -48.69100 1.000 29.73897  ? 173 SER H N   1 
ATOM   3115 C CA  . SER B  2 186 ? 7.24400   14.79800  -49.06400 1.000 28.24120  ? 173 SER H CA  1 
ATOM   3116 C C   . SER B  2 186 ? 6.30100   13.72200  -48.54600 1.000 32.28481  ? 173 SER H C   1 
ATOM   3117 O O   . SER B  2 186 ? 6.38100   12.59200  -48.97400 1.000 33.93550  ? 173 SER H O   1 
ATOM   3118 C CB  . SER B  2 186 ? 8.61300   14.50500  -48.46800 1.000 31.91190  ? 173 SER H CB  1 
ATOM   3119 O OG  . SER B  2 186 ? 8.60200   14.56600  -47.06100 1.000 32.21583  ? 173 SER H OG  1 
ATOM   3120 N N   . GLY B  2 187 ? 5.41800   14.06400  -47.63400 1.000 25.23857  ? 174 GLY H N   1 
ATOM   3121 C CA  . GLY B  2 187 ? 4.55000   13.08400  -47.00800 1.000 26.15116  ? 174 GLY H CA  1 
ATOM   3122 C C   . GLY B  2 187 ? 5.16900   12.56100  -45.74600 1.000 23.46572  ? 174 GLY H C   1 
ATOM   3123 O O   . GLY B  2 187 ? 4.57300   11.76900  -45.05600 1.000 35.96797  ? 174 GLY H O   1 
ATOM   3124 N N   . LEU B  2 188 ? 6.38200   12.99100  -45.45600 1.000 21.09531  ? 175 LEU H N   1 
ATOM   3125 C CA  . LEU B  2 188 ? 7.03500   12.60000  -44.23500 1.000 22.27947  ? 175 LEU H CA  1 
ATOM   3126 C C   . LEU B  2 188 ? 6.97600   13.66400  -43.13400 1.000 27.07268  ? 175 LEU H C   1 
ATOM   3127 O O   . LEU B  2 188 ? 6.91800   14.84300  -43.41100 1.000 25.15530  ? 175 LEU H O   1 
ATOM   3128 C CB  . LEU B  2 188 ? 8.47700   12.22700  -44.48800 1.000 26.79960  ? 175 LEU H CB  1 
ATOM   3129 C CG  . LEU B  2 188 ? 8.78800   11.15000  -45.52400 1.000 30.06789  ? 175 LEU H CG  1 
ATOM   3130 C CD1 . LEU B  2 188 ? 10.23500  11.26500  -45.94900 1.000 23.88113  ? 175 LEU H CD1 1 
ATOM   3131 C CD2 . LEU B  2 188 ? 8.50300   9.76800   -44.96700 1.000 28.40352  ? 175 LEU H CD2 1 
ATOM   3132 N N   . TYR B  2 189 ? 7.02500   13.21500  -41.89500 1.000 24.70771  ? 176 TYR H N   1 
ATOM   3133 C CA  . TYR B  2 189 ? 6.94300   14.09800  -40.76900 1.000 23.00603  ? 176 TYR H CA  1 
ATOM   3134 C C   . TYR B  2 189 ? 8.27500   14.59300  -40.29400 1.000 26.98152  ? 176 TYR H C   1 
ATOM   3135 O O   . TYR B  2 189 ? 9.27600   13.94400  -40.52000 1.000 24.07775  ? 176 TYR H O   1 
ATOM   3136 C CB  . TYR B  2 189 ? 6.29100   13.34800  -39.62700 1.000 26.84470  ? 176 TYR H CB  1 
ATOM   3137 C CG  . TYR B  2 189 ? 4.82300   13.02800  -39.79500 1.000 24.08377  ? 176 TYR H CG  1 
ATOM   3138 C CD1 . TYR B  2 189 ? 3.85300   13.99100  -39.58000 1.000 24.20144  ? 176 TYR H CD1 1 
ATOM   3139 C CD2 . TYR B  2 189 ? 4.41000   11.75300  -40.12400 1.000 25.52632  ? 176 TYR H CD2 1 
ATOM   3140 C CE1 . TYR B  2 189 ? 2.51300   13.69700  -39.71100 1.000 22.58555  ? 176 TYR H CE1 1 
ATOM   3141 C CE2 . TYR B  2 189 ? 3.07300   11.44500  -40.25800 1.000 24.54574  ? 176 TYR H CE2 1 
ATOM   3142 C CZ  . TYR B  2 189 ? 2.12900   12.41900  -40.05400 1.000 30.20816  ? 176 TYR H CZ  1 
ATOM   3143 O OH  . TYR B  2 189 ? 0.80300   12.11600  -40.19000 1.000 28.40245  ? 176 TYR H OH  1 
ATOM   3144 N N   . SER B  2 190 ? 8.27400   15.71300  -39.60500 1.000 22.44242  ? 177 SER H N   1 
ATOM   3145 C CA  . SER B  2 190 ? 9.47800   16.28100  -39.03100 1.000 22.78142  ? 177 SER H CA  1 
ATOM   3146 C C   . SER B  2 190 ? 9.14000   17.10100  -37.81100 1.000 20.63294  ? 177 SER H C   1 
ATOM   3147 O O   . SER B  2 190 ? 8.14900   17.78100  -37.79000 1.000 24.07216  ? 177 SER H O   1 
ATOM   3148 C CB  . SER B  2 190 ? 10.25000  17.15200  -40.03900 1.000 21.57774  ? 177 SER H CB  1 
ATOM   3149 O OG  . SER B  2 190 ? 11.43500  17.66300  -39.48600 1.000 34.63472  ? 177 SER H OG  1 
ATOM   3150 N N   . LEU B  2 191 ? 9.96900   17.01700  -36.81100 1.000 19.65116  ? 178 LEU H N   1 
ATOM   3151 C CA  . LEU B  2 191 ? 9.77800   17.78900  -35.61500 1.000 26.04772  ? 178 LEU H CA  1 
ATOM   3152 C C   . LEU B  2 191 ? 11.08300  18.16100  -34.99500 1.000 24.31110  ? 178 LEU H C   1 
ATOM   3153 O O   . LEU B  2 191 ? 12.11000  17.59600  -35.32600 1.000 24.23678  ? 178 LEU H O   1 
ATOM   3154 C CB  . LEU B  2 191 ? 8.94800   17.02500  -34.58000 1.000 24.27617  ? 178 LEU H CB  1 
ATOM   3155 C CG  . LEU B  2 191 ? 9.56900   15.90200  -33.75000 1.000 23.29486  ? 178 LEU H CG  1 
ATOM   3156 C CD1 . LEU B  2 191 ? 10.39200  16.43100  -32.59000 1.000 21.18277  ? 178 LEU H CD1 1 
ATOM   3157 C CD2 . LEU B  2 191 ? 8.47300   14.98400  -33.24400 1.000 25.40249  ? 178 LEU H CD2 1 
ATOM   3158 N N   . SER B  2 192 ? 11.04500  19.11400  -34.11200 1.000 18.90115  ? 179 SER H N   1 
ATOM   3159 C CA  A SER B  2 192 ? 12.24100  19.47900  -33.37300 0.480 23.17332  ? 179 SER H CA  1 
ATOM   3160 C CA  B SER B  2 192 ? 12.24400  19.46100  -33.37300 0.520 23.17350  ? 179 SER H CA  1 
ATOM   3161 C C   . SER B  2 192 ? 12.01400  19.54800  -31.82900 1.000 21.42746  ? 179 SER H C   1 
ATOM   3162 O O   . SER B  2 192 ? 10.88600  19.85200  -31.30200 1.000 23.92672  ? 179 SER H O   1 
ATOM   3163 C CB  A SER B  2 192 ? 12.76800  20.83200  -33.84200 0.480 25.75467  ? 179 SER H CB  1 
ATOM   3164 C CB  B SER B  2 192 ? 12.81600  20.78400  -33.87100 0.520 25.76411  ? 179 SER H CB  1 
ATOM   3165 O OG  A SER B  2 192 ? 13.75500  20.69000  -34.84400 0.480 27.37400  ? 179 SER H OG  1 
ATOM   3166 O OG  B SER B  2 192 ? 12.29200  21.86800  -33.12700 0.520 21.72755  ? 179 SER H OG  1 
ATOM   3167 N N   . SER B  2 193 ? 13.06500  19.29300  -31.06100 1.000 16.43141  ? 180 SER H N   1 
ATOM   3168 C CA  . SER B  2 193 ? 12.95700  19.46400  -29.61300 1.000 14.00576  ? 180 SER H CA  1 
ATOM   3169 C C   . SER B  2 193 ? 14.07200  20.41700  -29.25200 1.000 19.93039  ? 180 SER H C   1 
ATOM   3170 O O   . SER B  2 193 ? 15.17300  20.30700  -29.74700 1.000 18.79455  ? 180 SER H O   1 
ATOM   3171 C CB  . SER B  2 193 ? 13.03200  18.19800  -28.76100 1.000 24.10163  ? 180 SER H CB  1 
ATOM   3172 O OG  . SER B  2 193 ? 12.95100  18.48700  -27.38700 1.000 24.07193  ? 180 SER H OG  1 
ATOM   3173 N N   . VAL B  2 194 ? 13.75600  21.36500  -28.40300 1.000 17.34451  ? 181 VAL H N   1 
ATOM   3174 C CA  . VAL B  2 194 ? 14.73400  22.33800  -27.99800 1.000 19.78521  ? 181 VAL H CA  1 
ATOM   3175 C C   . VAL B  2 194 ? 14.73200  22.51700  -26.49600 1.000 20.06496  ? 181 VAL H C   1 
ATOM   3176 O O   . VAL B  2 194 ? 13.81400  22.09900  -25.82600 1.000 22.61569  ? 181 VAL H O   1 
ATOM   3177 C CB  . VAL B  2 194 ? 14.51600  23.71000  -28.68100 1.000 20.23353  ? 181 VAL H CB  1 
ATOM   3178 C CG1 . VAL B  2 194 ? 14.55200  23.57900  -30.19300 1.000 18.54380  ? 181 VAL H CG1 1 
ATOM   3179 C CG2 . VAL B  2 194 ? 13.21600  24.33700  -28.20800 1.000 17.31197  ? 181 VAL H CG2 1 
ATOM   3180 N N   . VAL B  2 195 ? 15.78400  23.11800  -25.99700 1.000 19.45537  ? 182 VAL H N   1 
ATOM   3181 C CA  . VAL B  2 195 ? 15.87900  23.36700  -24.59900 1.000 21.71879  ? 182 VAL H CA  1 
ATOM   3182 C C   . VAL B  2 195 ? 16.72800  24.61200  -24.34500 1.000 30.20294  ? 182 VAL H C   1 
ATOM   3183 O O   . VAL B  2 195 ? 17.71800  24.82400  -25.02800 1.000 25.79737  ? 182 VAL H O   1 
ATOM   3184 C CB  . VAL B  2 195 ? 16.45300  22.13900  -23.84800 1.000 26.15706  ? 182 VAL H CB  1 
ATOM   3185 C CG1 . VAL B  2 195 ? 17.78500  21.70600  -24.43000 1.000 28.40439  ? 182 VAL H CG1 1 
ATOM   3186 C CG2 . VAL B  2 195 ? 16.57400  22.44800  -22.36500 1.000 27.29379  ? 182 VAL H CG2 1 
ATOM   3187 N N   . THR B  2 196 ? 16.30100  25.46600  -23.42500 1.000 23.98111  ? 183 THR H N   1 
ATOM   3188 C CA  . THR B  2 196 ? 17.15500  26.58100  -23.05600 1.000 20.94956  ? 183 THR H CA  1 
ATOM   3189 C C   . THR B  2 196 ? 17.89800  26.23000  -21.76800 1.000 25.11617  ? 183 THR H C   1 
ATOM   3190 O O   . THR B  2 196 ? 17.33900  25.64300  -20.84200 1.000 22.70201  ? 183 THR H O   1 
ATOM   3191 C CB  . THR B  2 196 ? 16.37300  27.90500  -22.89700 1.000 25.32613  ? 183 THR H CB  1 
ATOM   3192 O OG1 . THR B  2 196 ? 15.25300  27.74800  -22.00200 1.000 26.62111  ? 183 THR H OG1 1 
ATOM   3193 C CG2 . THR B  2 196 ? 15.87500  28.43900  -24.27300 1.000 23.99600  ? 183 THR H CG2 1 
ATOM   3194 N N   . VAL B  2 197 ? 19.18000  26.56200  -21.73800 1.000 29.79377  ? 184 VAL H N   1 
ATOM   3195 C CA  . VAL B  2 197 ? 20.07100  26.21700  -20.63200 1.000 23.75239  ? 184 VAL H CA  1 
ATOM   3196 C C   . VAL B  2 197 ? 21.01900  27.38300  -20.39600 1.000 35.51816  ? 184 VAL H C   1 
ATOM   3197 O O   . VAL B  2 197 ? 21.20300  28.23800  -21.26700 1.000 38.35266  ? 184 VAL H O   1 
ATOM   3198 C CB  . VAL B  2 197 ? 20.87800  24.93400  -20.90500 1.000 25.97263  ? 184 VAL H CB  1 
ATOM   3199 C CG1 . VAL B  2 197 ? 19.97700  23.78200  -21.35400 1.000 28.02402  ? 184 VAL H CG1 1 
ATOM   3200 C CG2 . VAL B  2 197 ? 21.98100  25.21400  -21.91500 1.000 30.30202  ? 184 VAL H CG2 1 
ATOM   3201 N N   . PRO B  2 198 ? 21.61200  27.44500  -19.19700 1.000 36.37118  ? 185 PRO H N   1 
ATOM   3202 C CA  . PRO B  2 198 ? 22.63400  28.47700  -18.94500 1.000 39.06568  ? 185 PRO H CA  1 
ATOM   3203 C C   . PRO B  2 198 ? 23.81100  28.35000  -19.90100 1.000 38.16315  ? 185 PRO H C   1 
ATOM   3204 O O   . PRO B  2 198 ? 24.35600  27.26600  -20.12400 1.000 40.80072  ? 185 PRO H O   1 
ATOM   3205 C CB  . PRO B  2 198 ? 23.05300  28.23000  -17.48500 1.000 43.41205  ? 185 PRO H CB  1 
ATOM   3206 C CG  . PRO B  2 198 ? 21.98000  27.29600  -16.90100 1.000 35.04198  ? 185 PRO H CG  1 
ATOM   3207 C CD  . PRO B  2 198 ? 21.42000  26.53600  -18.04600 1.000 31.19735  ? 185 PRO H CD  1 
ATOM   3208 N N   . SER B  2 199 ? 24.18000  29.48400  -20.48900 1.000 44.18692  ? 186 SER H N   1 
ATOM   3209 C CA  . SER B  2 199 ? 25.37400  29.55500  -21.31900 1.000 45.30891  ? 186 SER H CA  1 
ATOM   3210 C C   . SER B  2 199 ? 26.60800  29.22100  -20.51700 1.000 50.62303  ? 186 SER H C   1 
ATOM   3211 O O   . SER B  2 199 ? 27.61100  28.75900  -21.07500 1.000 45.82949  ? 186 SER H O   1 
ATOM   3212 C CB  . SER B  2 199 ? 25.50700  30.95400  -21.88100 1.000 40.62625  ? 186 SER H CB  1 
ATOM   3213 O OG  . SER B  2 199 ? 24.25700  31.38500  -22.37800 1.000 60.71437  ? 186 SER H OG  1 
ATOM   3214 N N   . SER B  2 200 ? 26.54100  29.49500  -19.21400 1.000 48.37117  ? 187 SER H N   1 
ATOM   3215 C CA  . SER B  2 200 ? 27.60300  29.16500  -18.28200 1.000 53.18355  ? 187 SER H CA  1 
ATOM   3216 C C   . SER B  2 200 ? 27.93900  27.67700  -18.33700 1.000 47.72918  ? 187 SER H C   1 
ATOM   3217 O O   . SER B  2 200 ? 29.09000  27.28700  -18.10900 1.000 52.82976  ? 187 SER H O   1 
ATOM   3218 C CB  . SER B  2 200 ? 27.15000  29.60500  -16.88500 1.000 42.69397  ? 187 SER H CB  1 
ATOM   3219 O OG  . SER B  2 200 ? 28.23500  29.78400  -16.00400 1.000 73.27354  ? 187 SER H OG  1 
ATOM   3220 N N   . SER B  2 201 ? 26.96300  26.84500  -18.69900 1.000 42.96118  ? 188 SER H N   1 
ATOM   3221 C CA  . SER B  2 201 ? 27.06000  25.40100  -18.56800 1.000 39.53362  ? 188 SER H CA  1 
ATOM   3222 C C   . SER B  2 201 ? 27.45500  24.69700  -19.85500 1.000 46.45409  ? 188 SER H C   1 
ATOM   3223 O O   . SER B  2 201 ? 27.52100  23.46400  -19.86900 1.000 46.45459  ? 188 SER H O   1 
ATOM   3224 C CB  . SER B  2 201 ? 25.72500  24.83000  -18.09300 1.000 47.16663  ? 188 SER H CB  1 
ATOM   3225 O OG  . SER B  2 201 ? 24.82000  24.71300  -19.18200 1.000 46.66034  ? 188 SER H OG  1 
ATOM   3226 N N   . LEU B  2 202 ? 27.66400  25.42600  -20.94200 1.000 37.64500  ? 189 LEU H N   1 
ATOM   3227 C CA  . LEU B  2 202 ? 27.87900  24.73600  -22.24600 1.000 44.71277  ? 189 LEU H CA  1 
ATOM   3228 C C   . LEU B  2 202 ? 29.17700  23.90400  -22.27000 1.000 50.10581  ? 189 LEU H C   1 
ATOM   3229 O O   . LEU B  2 202 ? 29.20400  22.87000  -22.94100 1.000 51.13118  ? 189 LEU H O   1 
ATOM   3230 C CB  . LEU B  2 202 ? 27.82000  25.79300  -23.35300 1.000 39.54517  ? 189 LEU H CB  1 
ATOM   3231 C CG  . LEU B  2 202 ? 26.43900  26.38600  -23.62400 1.000 35.64326  ? 189 LEU H CG  1 
ATOM   3232 C CD1 . LEU B  2 202 ? 26.46900  27.27300  -24.85700 1.000 36.65083  ? 189 LEU H CD1 1 
ATOM   3233 C CD2 . LEU B  2 202 ? 25.39500  25.29300  -23.78700 1.000 44.18527  ? 189 LEU H CD2 1 
ATOM   3234 N N   . GLY B  2 203 ? 30.22300  24.34300  -21.57800 1.000 47.32503  ? 190 GLY H N   1 
ATOM   3235 C CA  . GLY B  2 203 ? 31.47500  23.57500  -21.66100 1.000 56.40828  ? 190 GLY H CA  1 
ATOM   3236 C C   . GLY B  2 203 ? 31.43900  22.35400  -20.77600 1.000 53.37076  ? 190 GLY H C   1 
ATOM   3237 O O   . GLY B  2 203 ? 31.96200  21.31100  -21.20000 1.000 60.77523  ? 190 GLY H O   1 
ATOM   3238 N N   . THR B  2 204 ? 30.82800  22.47900  -19.60600 1.000 53.24024  ? 191 THR H N   1 
ATOM   3239 C CA  . THR B  2 204 ? 30.82600  21.38200  -18.61200 1.000 53.99787  ? 191 THR H CA  1 
ATOM   3240 C C   . THR B  2 204 ? 29.70000  20.38800  -18.85100 1.000 46.20348  ? 191 THR H C   1 
ATOM   3241 O O   . THR B  2 204 ? 29.98700  19.19800  -18.93000 1.000 56.03743  ? 191 THR H O   1 
ATOM   3242 C CB  . THR B  2 204 ? 30.61800  21.96000  -17.21000 1.000 46.77966  ? 191 THR H CB  1 
ATOM   3243 O OG1 . THR B  2 204 ? 29.66400  23.01300  -17.32800 1.000 56.72384  ? 191 THR H OG1 1 
ATOM   3244 C CG2 . THR B  2 204 ? 31.89100  22.49700  -16.59600 1.000 53.07142  ? 191 THR H CG2 1 
ATOM   3245 N N   . GLN B  2 205 ? 28.47000  20.86400  -18.95900 1.000 53.97815  ? 192 GLN H N   1 
ATOM   3246 C CA  . GLN B  2 205 ? 27.31700  19.93300  -19.00900 1.000 42.01964  ? 192 GLN H CA  1 
ATOM   3247 C C   . GLN B  2 205 ? 27.20200  19.21200  -20.34400 1.000 40.66240  ? 192 GLN H C   1 
ATOM   3248 O O   . GLN B  2 205 ? 27.40000  19.85500  -21.37600 1.000 38.39774  ? 192 GLN H O   1 
ATOM   3249 C CB  . GLN B  2 205 ? 26.01400  20.68300  -18.72600 1.000 45.21745  ? 192 GLN H CB  1 
ATOM   3250 C CG  . GLN B  2 205 ? 24.78600  19.78700  -18.72900 1.000 45.71678  ? 192 GLN H CG  1 
ATOM   3251 C CD  . GLN B  2 205 ? 24.88300  18.70100  -17.68600 1.000 52.95357  ? 192 GLN H CD  1 
ATOM   3252 O OE1 . GLN B  2 205 ? 25.14500  18.96000  -16.51400 1.000 64.71545  ? 192 GLN H OE1 1 
ATOM   3253 N NE2 . GLN B  2 205 ? 24.68200  17.46600  -18.11000 1.000 45.14873  ? 192 GLN H NE2 1 
ATOM   3254 N N   . THR B  2 206 ? 26.81000  17.93700  -20.29500 1.000 40.72837  ? 193 THR H N   1 
ATOM   3255 C CA  . THR B  2 206 ? 26.54500  17.20200  -21.54900 1.000 38.94659  ? 193 THR H CA  1 
ATOM   3256 C C   . THR B  2 206 ? 25.03000  17.18300  -21.75600 1.000 36.02864  ? 193 THR H C   1 
ATOM   3257 O O   . THR B  2 206 ? 24.31300  17.13400  -20.75100 1.000 33.42257  ? 193 THR H O   1 
ATOM   3258 C CB  . THR B  2 206 ? 27.18200  15.80800  -21.51400 1.000 31.90360  ? 193 THR H CB  1 
ATOM   3259 O OG1 . THR B  2 206 ? 28.56300  15.94400  -21.84500 1.000 48.71820  ? 193 THR H OG1 1 
ATOM   3260 C CG2 . THR B  2 206 ? 26.51800  14.83100  -22.45900 1.000 35.72182  ? 193 THR H CG2 1 
ATOM   3261 N N   . TYR B  2 207 ? 24.58500  17.26500  -23.03400 1.000 32.53294  ? 194 TYR H N   1 
ATOM   3262 C CA  . TYR B  2 207 ? 23.17200  17.20400  -23.35300 1.000 35.80247  ? 194 TYR H CA  1 
ATOM   3263 C C   . TYR B  2 207 ? 22.95300  16.20500  -24.46500 1.000 23.08470  ? 194 TYR H C   1 
ATOM   3264 O O   . TYR B  2 207 ? 23.63600  16.25200  -25.48400 1.000 32.95328  ? 194 TYR H O   1 
ATOM   3265 C CB  . TYR B  2 207 ? 22.63100  18.56100  -23.79500 1.000 34.59768  ? 194 TYR H CB  1 
ATOM   3266 C CG  . TYR B  2 207 ? 22.80900  19.63900  -22.76800 1.000 34.94193  ? 194 TYR H CG  1 
ATOM   3267 C CD1 . TYR B  2 207 ? 21.85700  19.85000  -21.79400 1.000 30.13045  ? 194 TYR H CD1 1 
ATOM   3268 C CD2 . TYR B  2 207 ? 23.91100  20.46200  -22.79700 1.000 30.45819  ? 194 TYR H CD2 1 
ATOM   3269 C CE1 . TYR B  2 207 ? 22.00800  20.83900  -20.85000 1.000 27.09606  ? 194 TYR H CE1 1 
ATOM   3270 C CE2 . TYR B  2 207 ? 24.08300  21.44900  -21.86600 1.000 37.29316  ? 194 TYR H CE2 1 
ATOM   3271 C CZ  . TYR B  2 207 ? 23.12400  21.64100  -20.88200 1.000 34.20444  ? 194 TYR H CZ  1 
ATOM   3272 O OH  . TYR B  2 207 ? 23.28400  22.63000  -19.91800 1.000 27.74454  ? 194 TYR H OH  1 
ATOM   3273 N N   . ILE B  2 208 ? 21.97500  15.35700  -24.24800 1.000 24.84136  ? 195 ILE H N   1 
ATOM   3274 C CA  . ILE B  2 208 ? 21.66100  14.30300  -25.23200 1.000 29.33809  ? 195 ILE H CA  1 
ATOM   3275 C C   . ILE B  2 208 ? 20.14900  14.23500  -25.37800 1.000 29.07088  ? 195 ILE H C   1 
ATOM   3276 O O   . ILE B  2 208 ? 19.46700  14.33100  -24.36400 1.000 29.22748  ? 195 ILE H O   1 
ATOM   3277 C CB  . ILE B  2 208 ? 22.25800  12.96200  -24.75700 1.000 30.62285  ? 195 ILE H CB  1 
ATOM   3278 C CG1 . ILE B  2 208 ? 23.77800  13.04700  -24.60100 1.000 37.15933  ? 195 ILE H CG1 1 
ATOM   3279 C CG2 . ILE B  2 208 ? 21.84500  11.82900  -25.68300 1.000 29.51955  ? 195 ILE H CG2 1 
ATOM   3280 C CD1 . ILE B  2 208 ? 24.37000  11.97900  -23.71100 1.000 46.90508  ? 195 ILE H CD1 1 
ATOM   3281 N N   . CYS B  2 209 ? 19.65400  14.10100  -26.59900 1.000 28.03093  ? 196 CYS H N   1 
ATOM   3282 C CA  . CYS B  2 209 ? 18.23900  13.90000  -26.86000 1.000 30.96230  ? 196 CYS H CA  1 
ATOM   3283 C C   . CYS B  2 209 ? 18.01400  12.43400  -27.20200 1.000 31.56989  ? 196 CYS H C   1 
ATOM   3284 O O   . CYS B  2 209 ? 18.70800  11.87800  -28.05600 1.000 29.38111  ? 196 CYS H O   1 
ATOM   3285 C CB  . CYS B  2 209 ? 17.76500  14.82900  -27.98300 1.000 29.31428  ? 196 CYS H CB  1 
ATOM   3286 S SG  . CYS B  2 209 ? 18.45900  14.43500  -29.60700 1.000 32.70045  ? 196 CYS H SG  1 
ATOM   3287 N N   . ASN B  2 210 ? 17.05100  11.86700  -26.53900 1.000 31.51136  ? 197 ASN H N   1 
ATOM   3288 C CA  . ASN B  2 210 ? 16.71500  10.51600  -26.76400 1.000 31.44227  ? 197 ASN H CA  1 
ATOM   3289 C C   . ASN B  2 210 ? 15.44700  10.53000  -27.58500 1.000 32.77842  ? 197 ASN H C   1 
ATOM   3290 O O   . ASN B  2 210 ? 14.45400  11.07800  -27.15400 1.000 30.13887  ? 197 ASN H O   1 
ATOM   3291 C CB  . ASN B  2 210 ? 16.55700  9.86800   -25.39700 1.000 25.61946  ? 197 ASN H CB  1 
ATOM   3292 C CG  . ASN B  2 210 ? 17.52800  10.42100  -24.38200 1.000 30.63758  ? 197 ASN H CG  1 
ATOM   3293 O OD1 . ASN B  2 210 ? 17.15800  11.19700  -23.51400 1.000 35.45149  ? 197 ASN H OD1 1 
ATOM   3294 N ND2 . ASN B  2 210 ? 18.78400  10.03300  -24.50100 1.000 31.24379  ? 197 ASN H ND2 1 
ATOM   3295 N N   . VAL B  2 211 ? 15.52900  9.93600   -28.75200 1.000 26.75552  ? 198 VAL H N   1 
ATOM   3296 C CA  . VAL B  2 211 ? 14.40200  9.89500   -29.62800 1.000 28.54650  ? 198 VAL H CA  1 
ATOM   3297 C C   . VAL B  2 211 ? 13.97000  8.47400   -29.80900 1.000 30.54674  ? 198 VAL H C   1 
ATOM   3298 O O   . VAL B  2 211 ? 14.80200  7.59800   -29.87400 1.000 41.70101  ? 198 VAL H O   1 
ATOM   3299 C CB  . VAL B  2 211 ? 14.76500  10.50700  -31.00400 1.000 28.44948  ? 198 VAL H CB  1 
ATOM   3300 C CG1 . VAL B  2 211 ? 13.53800  10.60200  -31.88900 1.000 32.06376  ? 198 VAL H CG1 1 
ATOM   3301 C CG2 . VAL B  2 211 ? 15.44900  11.84900  -30.83500 1.000 30.06707  ? 198 VAL H CG2 1 
ATOM   3302 N N   . ASN B  2 212 ? 12.68200  8.24800   -29.91400 1.000 30.02869  ? 199 ASN H N   1 
ATOM   3303 C CA  . ASN B  2 212 ? 12.14700  6.91200   -30.10500 1.000 32.65891  ? 199 ASN H CA  1 
ATOM   3304 C C   . ASN B  2 212 ? 11.03300  6.86800   -31.10400 1.000 36.62564  ? 199 ASN H C   1 
ATOM   3305 O O   . ASN B  2 212 ? 10.01200  7.49400   -30.90600 1.000 37.28540  ? 199 ASN H O   1 
ATOM   3306 C CB  . ASN B  2 212 ? 11.63200  6.33600   -28.77300 1.000 40.22464  ? 199 ASN H CB  1 
ATOM   3307 C CG  . ASN B  2 212 ? 11.46900  4.83900   -28.80500 1.000 54.36301  ? 199 ASN H CG  1 
ATOM   3308 O OD1 . ASN B  2 212 ? 11.47600  4.21700   -29.86500 1.000 55.27051  ? 199 ASN H OD1 1 
ATOM   3309 N ND2 . ASN B  2 212 ? 11.31900  4.24700   -27.63300 1.000 55.26715  ? 199 ASN H ND2 1 
ATOM   3310 N N   . HIS B  2 213 ? 11.22900  6.14900   -32.19400 1.000 26.35083  ? 200 HIS H N   1 
ATOM   3311 C CA  . HIS B  2 213 ? 10.19000  5.97700   -33.17700 1.000 30.08502  ? 200 HIS H CA  1 
ATOM   3312 C C   . HIS B  2 213 ? 9.84600   4.51500   -33.15600 1.000 38.18706  ? 200 HIS H C   1 
ATOM   3313 O O   . HIS B  2 213 ? 10.46600  3.71700   -33.84100 1.000 31.83463  ? 200 HIS H O   1 
ATOM   3314 C CB  . HIS B  2 213 ? 10.60400  6.42200   -34.57000 1.000 28.04848  ? 200 HIS H CB  1 
ATOM   3315 C CG  . HIS B  2 213 ? 9.48800   6.43100   -35.56400 1.000 30.61282  ? 200 HIS H CG  1 
ATOM   3316 N ND1 . HIS B  2 213 ? 9.55800   5.76200   -36.76400 1.000 29.09510  ? 200 HIS H ND1 1 
ATOM   3317 C CD2 . HIS B  2 213 ? 8.27700   7.03300   -35.54200 1.000 30.77674  ? 200 HIS H CD2 1 
ATOM   3318 C CE1 . HIS B  2 213 ? 8.43800   5.94600   -37.43500 1.000 24.96323  ? 200 HIS H CE1 1 
ATOM   3319 N NE2 . HIS B  2 213 ? 7.64400   6.71400   -36.71500 1.000 30.14038  ? 200 HIS H NE2 1 
ATOM   3320 N N   . LYS B  2 214 ? 8.86100   4.17400   -32.36300 1.000 34.85470  ? 201 LYS H N   1 
ATOM   3321 C CA  . LYS B  2 214 ? 8.49000   2.78500   -32.19600 1.000 37.56698  ? 201 LYS H CA  1 
ATOM   3322 C C   . LYS B  2 214 ? 8.08600   2.04800   -33.47100 1.000 35.49889  ? 201 LYS H C   1 
ATOM   3323 O O   . LYS B  2 214 ? 8.42300   0.90400   -33.63100 1.000 45.49143  ? 201 LYS H O   1 
ATOM   3324 C CB  . LYS B  2 214 ? 7.38900   2.69400   -31.14700 1.000 37.65512  ? 201 LYS H CB  1 
ATOM   3325 C CG  . LYS B  2 214 ? 7.89900   2.82900   -29.72700 1.000 49.14284  ? 201 LYS H CG  1 
ATOM   3326 C CD  . LYS B  2 214 ? 6.82900   3.37900   -28.80800 1.000 51.49034  ? 201 LYS H CD  1 
ATOM   3327 C CE  . LYS B  2 214 ? 6.99500   2.85200   -27.39300 1.000 57.51025  ? 201 LYS H CE  1 
ATOM   3328 N NZ  . LYS B  2 214 ? 5.84300   3.23400   -26.53000 1.000 64.02548  ? 201 LYS H NZ  1 
ATOM   3329 N N   . PRO B  2 215 ? 7.38500   2.70700   -34.37200 1.000 32.06253  ? 202 PRO H N   1 
ATOM   3330 C CA  . PRO B  2 215 ? 6.94500   1.98100   -35.55100 1.000 31.05265  ? 202 PRO H CA  1 
ATOM   3331 C C   . PRO B  2 215 ? 8.07600   1.51700   -36.45800 1.000 42.05292  ? 202 PRO H C   1 
ATOM   3332 O O   . PRO B  2 215 ? 7.84400   0.62800   -37.25200 1.000 41.04557  ? 202 PRO H O   1 
ATOM   3333 C CB  . PRO B  2 215 ? 6.11000   3.00200   -36.28000 1.000 38.00214  ? 202 PRO H CB  1 
ATOM   3334 C CG  . PRO B  2 215 ? 5.67000   3.97700   -35.25300 1.000 35.23052  ? 202 PRO H CG  1 
ATOM   3335 C CD  . PRO B  2 215 ? 6.81800   4.06300   -34.31600 1.000 37.54656  ? 202 PRO H CD  1 
ATOM   3336 N N   . SER B  2 216 ? 9.25200   2.11000   -36.35700 1.000 42.34247  ? 203 SER H N   1 
ATOM   3337 C CA  . SER B  2 216 ? 10.40800  1.69900   -37.14400 1.000 37.57990  ? 203 SER H CA  1 
ATOM   3338 C C   . SER B  2 216 ? 11.43400  1.09300   -36.22800 1.000 40.89655  ? 203 SER H C   1 
ATOM   3339 O O   . SER B  2 216 ? 12.49300  0.69800   -36.65700 1.000 47.41491  ? 203 SER H O   1 
ATOM   3340 C CB  . SER B  2 216 ? 10.98000  2.90100   -37.86300 1.000 36.22709  ? 203 SER H CB  1 
ATOM   3341 O OG  . SER B  2 216 ? 11.24900  3.92500   -36.93500 1.000 44.60915  ? 203 SER H OG  1 
ATOM   3342 N N   . ASN B  2 217 ? 11.11800  1.02500   -34.95400 1.000 39.44691  ? 204 ASN H N   1 
ATOM   3343 C CA  . ASN B  2 217 ? 12.03300  0.50900   -33.96100 1.000 38.16913  ? 204 ASN H CA  1 
ATOM   3344 C C   . ASN B  2 217 ? 13.32300  1.29200   -33.88700 1.000 46.10949  ? 204 ASN H C   1 
ATOM   3345 O O   . ASN B  2 217 ? 14.36400  0.73300   -33.59500 1.000 52.82704  ? 204 ASN H O   1 
ATOM   3346 C CB  . ASN B  2 217 ? 12.32500  -0.96500  -34.19900 1.000 54.12067  ? 204 ASN H CB  1 
ATOM   3347 C CG  . ASN B  2 217 ? 12.53300  -1.71800  -32.90900 1.000 67.44335  ? 204 ASN H CG  1 
ATOM   3348 O OD1 . ASN B  2 217 ? 13.66200  -1.90700  -32.46300 1.000 71.58423  ? 204 ASN H OD1 1 
ATOM   3349 N ND2 . ASN B  2 217 ? 11.43800  -2.13400  -32.28500 1.000 70.69551  ? 204 ASN H ND2 1 
ATOM   3350 N N   . THR B  2 218 ? 13.25500  2.57500   -34.16300 1.000 33.15358  ? 205 THR H N   1 
ATOM   3351 C CA  . THR B  2 218 ? 14.42900  3.38600   -34.12500 1.000 37.68704  ? 205 THR H CA  1 
ATOM   3352 C C   . THR B  2 218 ? 14.58400  4.03900   -32.78000 1.000 37.30647  ? 205 THR H C   1 
ATOM   3353 O O   . THR B  2 218 ? 13.70000  4.71800   -32.31700 1.000 40.55112  ? 205 THR H O   1 
ATOM   3354 C CB  . THR B  2 218 ? 14.40000  4.47900   -35.22700 1.000 35.15935  ? 205 THR H CB  1 
ATOM   3355 O OG1 . THR B  2 218 ? 13.43400  5.47300   -34.88300 1.000 48.96843  ? 205 THR H OG1 1 
ATOM   3356 C CG2 . THR B  2 218 ? 14.05000  3.87500   -36.55800 1.000 31.17175  ? 205 THR H CG2 1 
ATOM   3357 N N   . LYS B  2 219 ? 15.70200  3.81200   -32.14000 1.000 36.75586  ? 206 LYS H N   1 
ATOM   3358 C CA  . LYS B  2 219 ? 15.97900  4.46400   -30.89400 1.000 38.13255  ? 206 LYS H CA  1 
ATOM   3359 C C   . LYS B  2 219 ? 17.30300  5.12300   -31.11500 1.000 45.49912  ? 206 LYS H C   1 
ATOM   3360 O O   . LYS B  2 219 ? 18.26700  4.48000   -31.48700 1.000 44.13250  ? 206 LYS H O   1 
ATOM   3361 C CB  . LYS B  2 219 ? 16.04900  3.50400   -29.72600 1.000 42.30002  ? 206 LYS H CB  1 
ATOM   3362 C CG  . LYS B  2 219 ? 14.74600  3.28500   -28.98200 1.000 52.79062  ? 206 LYS H CG  1 
ATOM   3363 C CD  . LYS B  2 219 ? 14.96600  2.42800   -27.74300 1.000 68.24093  ? 206 LYS H CD  1 
ATOM   3364 C CE  . LYS B  2 219 ? 13.90900  2.67900   -26.67500 1.000 69.81549  ? 206 LYS H CE  1 
ATOM   3365 N NZ  . LYS B  2 219 ? 14.35200  2.26700   -25.31500 1.000 56.64036  ? 206 LYS H NZ  1 
ATOM   3366 N N   . VAL B  2 220 ? 17.34500  6.41800   -30.91200 1.000 34.89935  ? 207 VAL H N   1 
ATOM   3367 C CA  . VAL B  2 220 ? 18.59900  7.16200   -31.20000 1.000 27.94314  ? 207 VAL H CA  1 
ATOM   3368 C C   . VAL B  2 220 ? 18.92800  8.11700   -30.06400 1.000 36.88593  ? 207 VAL H C   1 
ATOM   3369 O O   . VAL B  2 220 ? 18.01400  8.79200   -29.58200 1.000 35.67067  ? 207 VAL H O   1 
ATOM   3370 C CB  . VAL B  2 220 ? 18.50500  7.91500   -32.54100 1.000 35.03723  ? 207 VAL H CB  1 
ATOM   3371 C CG1 . VAL B  2 220 ? 19.60800  8.94700   -32.69600 1.000 28.58881  ? 207 VAL H CG1 1 
ATOM   3372 C CG2 . VAL B  2 220 ? 18.48500  6.96200   -33.72200 1.000 35.56174  ? 207 VAL H CG2 1 
ATOM   3373 N N   . ASP B  2 221 ? 20.19300  8.15100   -29.66000 1.000 32.37818  ? 208 ASP H N   1 
ATOM   3374 C CA  . ASP B  2 221 ? 20.66200  9.11500   -28.64500 1.000 37.76438  ? 208 ASP H CA  1 
ATOM   3375 C C   . ASP B  2 221 ? 21.65800  10.04200  -29.34500 1.000 41.09297  ? 208 ASP H C   1 
ATOM   3376 O O   . ASP B  2 221 ? 22.69100  9.54500   -29.79400 1.000 38.55349  ? 208 ASP H O   1 
ATOM   3377 C CB  . ASP B  2 221 ? 21.25100  8.41000   -27.42200 1.000 49.15647  ? 208 ASP H CB  1 
ATOM   3378 C CG  . ASP B  2 221 ? 20.27700  7.49100   -26.70800 1.000 45.27042  ? 208 ASP H CG  1 
ATOM   3379 O OD1 . ASP B  2 221 ? 19.06700  7.76300   -26.75400 1.000 45.64696  ? 208 ASP H OD1 1 
ATOM   3380 O OD2 . ASP B  2 221 ? 20.74500  6.51400   -26.10800 1.000 50.55243  ? 208 ASP H OD2 1 
ATOM   3381 N N   . LYS B  2 222 ? 21.33300  11.32600  -29.46900 1.000 35.75260  ? 209 LYS H N   1 
ATOM   3382 C CA  . LYS B  2 222 ? 22.20200  12.23500  -30.24800 1.000 34.72329  ? 209 LYS H CA  1 
ATOM   3383 C C   . LYS B  2 222 ? 22.87100  13.22900  -29.32000 1.000 33.60348  ? 209 LYS H C   1 
ATOM   3384 O O   . LYS B  2 222 ? 22.18500  14.02100  -28.66600 1.000 33.17843  ? 209 LYS H O   1 
ATOM   3385 C CB  . LYS B  2 222 ? 21.45600  12.94700  -31.38200 1.000 32.73572  ? 209 LYS H CB  1 
ATOM   3386 C CG  . LYS B  2 222 ? 22.25000  14.02300  -32.10400 1.000 35.79233  ? 209 LYS H CG  1 
ATOM   3387 C CD  . LYS B  2 222 ? 23.46300  13.49300  -32.82500 1.000 43.86031  ? 209 LYS H CD  1 
ATOM   3388 C CE  . LYS B  2 222 ? 23.14400  12.35000  -33.76200 1.000 45.08610  ? 209 LYS H CE  1 
ATOM   3389 N NZ  . LYS B  2 222 ? 24.23300  12.12400  -34.73800 1.000 49.14694  ? 209 LYS H NZ  1 
ATOM   3390 N N   . ARG B  2 223 ? 24.18000  13.14700  -29.28300 1.000 38.81289  ? 210 ARG H N   1 
ATOM   3391 C CA  . ARG B  2 223 ? 24.94900  14.07800  -28.47300 1.000 37.52029  ? 210 ARG H CA  1 
ATOM   3392 C C   . ARG B  2 223 ? 24.86100  15.45400  -29.10900 1.000 35.60252  ? 210 ARG H C   1 
ATOM   3393 O O   . ARG B  2 223 ? 25.53400  15.72400  -30.09800 1.000 46.58650  ? 210 ARG H O   1 
ATOM   3394 C CB  . ARG B  2 223 ? 26.39100  13.59300  -28.41800 1.000 47.11981  ? 210 ARG H CB  1 
ATOM   3395 C CG  . ARG B  2 223 ? 27.33700  14.28000  -27.48400 1.000 45.57474  ? 210 ARG H CG  1 
ATOM   3396 C CD  . ARG B  2 223 ? 26.91500  14.12900  -26.07200 1.000 61.01373  ? 210 ARG H CD  1 
ATOM   3397 N NE  . ARG B  2 223 ? 28.08000  14.14900  -25.19600 1.000 67.30752  ? 210 ARG H NE  1 
ATOM   3398 C CZ  . ARG B  2 223 ? 28.97500  13.17000  -25.11200 1.000 68.98546  ? 210 ARG H CZ  1 
ATOM   3399 N NH1 . ARG B  2 223 ? 28.80400  12.01500  -25.73700 1.000 63.91600  ? 210 ARG H NH1 1 
ATOM   3400 N NH2 . ARG B  2 223 ? 30.05200  13.34000  -24.35000 1.000 68.15887  ? 210 ARG H NH2 1 
ATOM   3401 N N   . VAL B  2 224 ? 24.35300  16.45800  -28.40700 1.000 37.33156  ? 211 VAL H N   1 
ATOM   3402 C CA  . VAL B  2 224 ? 24.36700  17.84200  -28.95800 1.000 33.65553  ? 211 VAL H CA  1 
ATOM   3403 C C   . VAL B  2 224 ? 25.46200  18.71100  -28.35300 1.000 41.00916  ? 211 VAL H C   1 
ATOM   3404 O O   . VAL B  2 224 ? 25.44200  18.99000  -27.17000 1.000 43.92338  ? 211 VAL H O   1 
ATOM   3405 C CB  . VAL B  2 224 ? 23.00800  18.54900  -28.83300 1.000 26.58776  ? 211 VAL H CB  1 
ATOM   3406 C CG1 . VAL B  2 224 ? 23.08800  19.96200  -29.38500 1.000 29.61408  ? 211 VAL H CG1 1 
ATOM   3407 C CG2 . VAL B  2 224 ? 21.92400  17.74700  -29.52100 1.000 26.95868  ? 211 VAL H CG2 1 
ATOM   3408 N N   . GLU B  2 225 ? 26.39200  19.19400  -29.17000 1.000 41.41405  ? 212 GLU H N   1 
ATOM   3409 C CA  . GLU B  2 225 ? 27.53900  19.92000  -28.63000 1.000 39.24164  ? 212 GLU H CA  1 
ATOM   3410 C C   . GLU B  2 225 ? 27.83700  21.31000  -29.14500 1.000 43.30357  ? 212 GLU H C   1 
ATOM   3411 O O   . GLU B  2 225 ? 27.58700  21.61900  -30.28700 1.000 40.99208  ? 212 GLU H O   1 
ATOM   3412 C CB  . GLU B  2 225 ? 28.79300  19.07700  -28.84800 1.000 53.90283  ? 212 GLU H CB  1 
ATOM   3413 C CG  . GLU B  2 225 ? 28.90000  17.88200  -27.91700 1.000 60.97028  ? 212 GLU H CG  1 
ATOM   3414 C CD  . GLU B  2 225 ? 30.29400  17.29400  -27.86700 1.000 69.54879  ? 212 GLU H CD  1 
ATOM   3415 O OE1 . GLU B  2 225 ? 30.66900  16.56500  -28.80700 1.000 62.13974  ? 212 GLU H OE1 1 
ATOM   3416 O OE2 . GLU B  2 225 ? 31.01400  17.55800  -26.88400 1.000 76.36306  ? 212 GLU H OE2 1 
ATOM   3417 N N   . PRO B  2 226 ? 28.44400  22.12400  -28.29600 1.000 45.15427  ? 213 PRO H N   1 
ATOM   3418 C CA  . PRO B  2 226 ? 28.71300  23.51500  -28.65200 1.000 52.12659  ? 213 PRO H CA  1 
ATOM   3419 C C   . PRO B  2 226 ? 29.54600  23.68200  -29.89500 1.000 52.87736  ? 213 PRO H C   1 
ATOM   3420 O O   . PRO B  2 226 ? 30.44600  22.90700  -30.13700 1.000 61.72220  ? 213 PRO H O   1 
ATOM   3421 C CB  . PRO B  2 226 ? 29.47400  24.05000  -27.43100 1.000 46.86674  ? 213 PRO H CB  1 
ATOM   3422 C CG  . PRO B  2 226 ? 29.92600  22.85200  -26.67400 1.000 51.94352  ? 213 PRO H CG  1 
ATOM   3423 C CD  . PRO B  2 226 ? 28.91900  21.78800  -26.94700 1.000 47.96925  ? 213 PRO H CD  1 
ATOM   3424 N N   . LYS B  2 227 ? 29.12000  24.67200  -30.66200 1.000 56.56554  ? 214 LYS H N   1 
ATOM   3425 C CA  . LYS B  2 227 ? 29.77500  25.00200  -31.88700 1.000 66.91684  ? 214 LYS H CA  1 
ATOM   3426 C C   . LYS B  2 227 ? 30.97400  25.86000  -31.55800 1.000 74.75215  ? 214 LYS H C   1 
ATOM   3427 O O   . LYS B  2 227 ? 31.77700  26.18300  -32.43300 1.000 76.88811  ? 214 LYS H O   1 
ATOM   3428 C CB  . LYS B  2 227 ? 28.80100  25.80900  -32.73500 1.000 57.01528  ? 214 LYS H CB  1 
ATOM   3429 C CG  . LYS B  2 227 ? 28.10800  25.07600  -33.85400 1.000 63.06529  ? 214 LYS H CG  1 
ATOM   3430 C CD  . LYS B  2 227 ? 27.01500  25.97500  -34.41000 1.000 64.11383  ? 214 LYS H CD  1 
ATOM   3431 C CE  . LYS B  2 227 ? 26.34100  25.36200  -35.61900 1.000 64.19046  ? 214 LYS H CE  1 
ATOM   3432 N NZ  . LYS B  2 227 ? 26.18000  26.35200  -36.71600 1.000 59.72925  ? 214 LYS H NZ  1 
ATOM   3433 N N   . ASP C  3 1   ? -27.76600 12.40100  -35.44000 1.000 47.96576  ? 1   ASP L N   1 
ATOM   3434 C CA  . ASP C  3 1   ? -28.86400 13.28000  -35.81000 1.000 55.00974  ? 1   ASP L CA  1 
ATOM   3435 C C   . ASP C  3 1   ? -29.09500 14.40800  -34.80300 1.000 52.34623  ? 1   ASP L C   1 
ATOM   3436 O O   . ASP C  3 1   ? -29.25200 15.54400  -35.21900 1.000 49.57709  ? 1   ASP L O   1 
ATOM   3437 C CB  . ASP C  3 1   ? -30.16100 12.48100  -36.06300 1.000 55.64824  ? 1   ASP L CB  1 
ATOM   3438 C CG  . ASP C  3 1   ? -31.25700 13.32000  -36.61600 1.000 66.94199  ? 1   ASP L CG  1 
ATOM   3439 O OD1 . ASP C  3 1   ? -30.98000 14.11000  -37.53500 1.000 84.75726  ? 1   ASP L OD1 1 
ATOM   3440 O OD2 . ASP C  3 1   ? -32.40200 13.18300  -36.14300 1.000 73.95851  ? 1   ASP L OD2 1 
ATOM   3441 N N   . ILE C  3 2   ? -29.13200 14.13100  -33.50400 1.000 43.16922  ? 2   ILE L N   1 
ATOM   3442 C CA  . ILE C  3 2   ? -29.26300 15.24200  -32.56600 1.000 39.88327  ? 2   ILE L CA  1 
ATOM   3443 C C   . ILE C  3 2   ? -27.97700 16.01000  -32.68100 1.000 43.84107  ? 2   ILE L C   1 
ATOM   3444 O O   . ILE C  3 2   ? -26.89800 15.49700  -32.43700 1.000 36.78695  ? 2   ILE L O   1 
ATOM   3445 C CB  . ILE C  3 2   ? -29.57500 14.86700  -31.11700 1.000 44.13583  ? 2   ILE L CB  1 
ATOM   3446 C CG1 . ILE C  3 2   ? -30.82200 13.98700  -31.04500 1.000 41.81739  ? 2   ILE L CG1 1 
ATOM   3447 C CG2 . ILE C  3 2   ? -29.77800 16.12500  -30.29200 1.000 35.91332  ? 2   ILE L CG2 1 
ATOM   3448 C CD1 . ILE C  3 2   ? -31.33000 13.76600  -29.64000 1.000 36.08355  ? 2   ILE L CD1 1 
ATOM   3449 N N   . VAL C  3 3   ? -28.11100 17.25800  -33.06400 1.000 44.30389  ? 3   VAL L N   1 
ATOM   3450 C CA  . VAL C  3 3   ? -26.92200 18.04600  -33.34700 1.000 39.57639  ? 3   VAL L CA  1 
ATOM   3451 C C   . VAL C  3 3   ? -26.62900 18.88700  -32.10400 1.000 30.62377  ? 3   VAL L C   1 
ATOM   3452 O O   . VAL C  3 3   ? -27.54200 19.50300  -31.53800 1.000 28.85861  ? 3   VAL L O   1 
ATOM   3453 C CB  . VAL C  3 3   ? -27.13100 18.91200  -34.60700 1.000 36.89569  ? 3   VAL L CB  1 
ATOM   3454 C CG1 . VAL C  3 3   ? -26.21400 20.15000  -34.60400 1.000 34.48329  ? 3   VAL L CG1 1 
ATOM   3455 C CG2 . VAL C  3 3   ? -26.99100 18.06400  -35.87800 1.000 31.62085  ? 3   VAL L CG2 1 
ATOM   3456 N N   . MET C  3 4   ? -25.37000 18.89400  -31.65100 1.000 29.38793  ? 4   MET L N   1 
ATOM   3457 C CA  . MET C  3 4   ? -25.01700 19.50600  -30.37400 1.000 25.40583  ? 4   MET L CA  1 
ATOM   3458 C C   . MET C  3 4   ? -24.17600 20.74800  -30.67900 1.000 29.65738  ? 4   MET L C   1 
ATOM   3459 O O   . MET C  3 4   ? -23.07300 20.62600  -31.22000 1.000 35.81966  ? 4   MET L O   1 
ATOM   3460 C CB  . MET C  3 4   ? -24.23200 18.51400  -29.50600 1.000 29.17836  ? 4   MET L CB  1 
ATOM   3461 C CG  . MET C  3 4   ? -25.12300 17.31100  -29.11600 1.000 29.94139  ? 4   MET L CG  1 
ATOM   3462 S SD  . MET C  3 4   ? -26.63500 17.74300  -28.27400 1.000 30.01545  ? 4   MET L SD  1 
ATOM   3463 C CE  . MET C  3 4   ? -26.10600 18.59600  -26.82700 1.000 27.06739  ? 4   MET L CE  1 
ATOM   3464 N N   . THR C  3 5   ? -24.69600 21.91300  -30.37400 1.000 29.54986  ? 5   THR L N   1 
ATOM   3465 C CA  . THR C  3 5   ? -24.01800 23.15500  -30.67100 1.000 29.82031  ? 5   THR L CA  1 
ATOM   3466 C C   . THR C  3 5   ? -23.49100 23.85500  -29.43400 1.000 27.39583  ? 5   THR L C   1 
ATOM   3467 O O   . THR C  3 5   ? -24.24800 24.35200  -28.62700 1.000 27.24366  ? 5   THR L O   1 
ATOM   3468 C CB  . THR C  3 5   ? -24.94000 24.11600  -31.45300 1.000 30.94161  ? 5   THR L CB  1 
ATOM   3469 O OG1 . THR C  3 5   ? -25.32900 23.52100  -32.69000 1.000 43.93119  ? 5   THR L OG1 1 
ATOM   3470 C CG2 . THR C  3 5   ? -24.22600 25.43100  -31.72100 1.000 38.22306  ? 5   THR L CG2 1 
ATOM   3471 N N   . GLN C  3 6   ? -22.18000 23.89100  -29.30700 1.000 28.00408  ? 6   GLN L N   1 
ATOM   3472 C CA  . GLN C  3 6   ? -21.55200 24.53800  -28.16400 1.000 26.92472  ? 6   GLN L CA  1 
ATOM   3473 C C   . GLN C  3 6   ? -21.07500 25.97000  -28.42700 1.000 32.55406  ? 6   GLN L C   1 
ATOM   3474 O O   . GLN C  3 6   ? -20.72500 26.30600  -29.54500 1.000 27.59727  ? 6   GLN L O   1 
ATOM   3475 C CB  . GLN C  3 6   ? -20.35700 23.73600  -27.68500 1.000 24.71177  ? 6   GLN L CB  1 
ATOM   3476 C CG  . GLN C  3 6   ? -20.58800 22.58800  -26.74900 1.000 28.01430  ? 6   GLN L CG  1 
ATOM   3477 C CD  . GLN C  3 6   ? -19.31900 21.78900  -26.56100 1.000 22.47183  ? 6   GLN L CD  1 
ATOM   3478 O OE1 . GLN C  3 6   ? -19.23800 20.64100  -26.96800 1.000 26.05261  ? 6   GLN L OE1 1 
ATOM   3479 N NE2 . GLN C  3 6   ? -18.31600 22.40600  -25.96000 1.000 17.16558  ? 6   GLN L NE2 1 
ATOM   3480 N N   . SER C  3 7   ? -21.05900 26.79800  -27.38900 1.000 27.78693  ? 7   SER L N   1 
ATOM   3481 C CA  . SER C  3 7   ? -20.56900 28.17300  -27.49200 1.000 31.29925  ? 7   SER L CA  1 
ATOM   3482 C C   . SER C  3 7   ? -19.93400 28.64600  -26.16500 1.000 28.50245  ? 7   SER L C   1 
ATOM   3483 O O   . SER C  3 7   ? -20.47500 28.39100  -25.10900 1.000 28.45023  ? 7   SER L O   1 
ATOM   3484 C CB  . SER C  3 7   ? -21.68900 29.12100  -27.89500 1.000 35.72087  ? 7   SER L CB  1 
ATOM   3485 O OG  . SER C  3 7   ? -22.69700 29.18000  -26.91100 1.000 47.31790  ? 7   SER L OG  1 
ATOM   3486 N N   . PRO C  3 8   ? -18.78200 29.30600  -26.24300 1.000 22.13066  ? 8   PRO L N   1 
ATOM   3487 C CA  . PRO C  3 8   ? -18.07300 29.50100  -27.49900 1.000 21.07363  ? 8   PRO L CA  1 
ATOM   3488 C C   . PRO C  3 8   ? -17.23900 28.29200  -27.94400 1.000 22.89353  ? 8   PRO L C   1 
ATOM   3489 O O   . PRO C  3 8   ? -17.22000 27.32400  -27.25500 1.000 23.62802  ? 8   PRO L O   1 
ATOM   3490 C CB  . PRO C  3 8   ? -17.12800 30.64400  -27.13300 1.000 23.03677  ? 8   PRO L CB  1 
ATOM   3491 C CG  . PRO C  3 8   ? -16.79000 30.38600  -25.68700 1.000 18.58141  ? 8   PRO L CG  1 
ATOM   3492 C CD  . PRO C  3 8   ? -18.07100 29.84700  -25.09000 1.000 21.19740  ? 8   PRO L CD  1 
ATOM   3493 N N   . SER C  3 9   ? -16.54700 28.39200  -29.07000 1.000 19.68529  ? 9   SER L N   1 
ATOM   3494 C CA  . SER C  3 9   ? -15.65900 27.34600  -29.53900 1.000 17.83726  ? 9   SER L CA  1 
ATOM   3495 C C   . SER C  3 9   ? -14.26500 27.45600  -28.92900 1.000 21.99115  ? 9   SER L C   1 
ATOM   3496 O O   . SER C  3 9   ? -13.55100 26.48800  -28.87700 1.000 24.01289  ? 9   SER L O   1 
ATOM   3497 C CB  . SER C  3 9   ? -15.55700 27.39100  -31.04200 1.000 23.86165  ? 9   SER L CB  1 
ATOM   3498 O OG  . SER C  3 9   ? -16.79000 27.06700  -31.64400 1.000 45.58147  ? 9   SER L OG  1 
ATOM   3499 N N   . SER C  3 10  ? -13.90300 28.63300  -28.46800 1.000 17.18103  ? 10  SER L N   1 
ATOM   3500 C CA  . SER C  3 10  ? -12.63700 28.84600  -27.81200 1.000 19.00666  ? 10  SER L CA  1 
ATOM   3501 C C   . SER C  3 10  ? -12.77700 30.03600  -26.91800 1.000 19.06221  ? 10  SER L C   1 
ATOM   3502 O O   . SER C  3 10  ? -13.57200 30.91100  -27.16500 1.000 22.35817  ? 10  SER L O   1 
ATOM   3503 C CB  . SER C  3 10  ? -11.49700 29.09000  -28.79500 1.000 20.92207  ? 10  SER L CB  1 
ATOM   3504 O OG  . SER C  3 10  ? -11.63900 30.32800  -29.44500 1.000 36.90230  ? 10  SER L OG  1 
ATOM   3505 N N   . LEU C  3 11  ? -11.97700 30.06400  -25.88800 1.000 19.72138  ? 11  LEU L N   1 
ATOM   3506 C CA  . LEU C  3 11  ? -11.97600 31.18600  -25.00800 1.000 17.56894  ? 11  LEU L CA  1 
ATOM   3507 C C   . LEU C  3 11  ? -10.71100 31.32100  -24.20600 1.000 22.37975  ? 11  LEU L C   1 
ATOM   3508 O O   . LEU C  3 11  ? -10.03000 30.35000  -23.94600 1.000 25.01960  ? 11  LEU L O   1 
ATOM   3509 C CB  . LEU C  3 11  ? -13.17100 31.14500  -24.05900 1.000 20.26166  ? 11  LEU L CB  1 
ATOM   3510 C CG  . LEU C  3 11  ? -13.21000 30.08100  -22.96700 1.000 23.43747  ? 11  LEU L CG  1 
ATOM   3511 C CD1 . LEU C  3 11  ? -12.47400 30.55300  -21.72800 1.000 17.81360  ? 11  LEU L CD1 1 
ATOM   3512 C CD2 . LEU C  3 11  ? -14.64900 29.72900  -22.63300 1.000 23.96102  ? 11  LEU L CD2 1 
ATOM   3513 N N   . SER C  3 12  ? -10.37900 32.53800  -23.86800 1.000 20.25054  ? 12  SER L N   1 
ATOM   3514 C CA  A SER C  3 12  ? -9.22000  32.78900  -23.02000 0.515 21.00367  ? 12  SER L CA  1 
ATOM   3515 C CA  B SER C  3 12  ? -9.22100  32.79200  -23.01400 0.485 21.00570  ? 12  SER L CA  1 
ATOM   3516 C C   . SER C  3 12  ? -9.67100  33.54400  -21.73400 1.000 18.46536  ? 12  SER L C   1 
ATOM   3517 O O   . SER C  3 12  ? -10.42500 34.57500  -21.70300 1.000 26.81905  ? 12  SER L O   1 
ATOM   3518 C CB  A SER C  3 12  ? -8.14100  33.56300  -23.78600 0.515 22.53356  ? 12  SER L CB  1 
ATOM   3519 C CB  B SER C  3 12  ? -8.14900  33.60100  -23.74000 0.485 22.51559  ? 12  SER L CB  1 
ATOM   3520 O OG  A SER C  3 12  ? -7.34400  34.35700  -22.93400 0.515 22.92538  ? 12  SER L OG  1 
ATOM   3521 O OG  B SER C  3 12  ? -7.44000  32.79600  -24.65800 0.485 20.95799  ? 12  SER L OG  1 
ATOM   3522 N N   . ALA C  3 13  ? -9.25700  33.01100  -20.60800 1.000 14.75469  ? 13  ALA L N   1 
ATOM   3523 C CA  . ALA C  3 13  ? -9.64300  33.63600  -19.35500 1.000 18.69256  ? 13  ALA L CA  1 
ATOM   3524 C C   . ALA C  3 13  ? -8.53300  33.68100  -18.31300 1.000 19.83560  ? 13  ALA L C   1 
ATOM   3525 O O   . ALA C  3 13  ? -7.62900  32.87900  -18.32700 1.000 16.99232  ? 13  ALA L O   1 
ATOM   3526 C CB  . ALA C  3 13  ? -10.86500 32.96500  -18.77700 1.000 16.68959  ? 13  ALA L CB  1 
ATOM   3527 N N   . SER C  3 14  ? -8.65500  34.63100  -17.40700 1.000 14.85301  ? 14  SER L N   1 
ATOM   3528 C CA  . SER C  3 14  ? -7.66000  34.78100  -16.38000 1.000 11.90817  ? 14  SER L CA  1 
ATOM   3529 C C   . SER C  3 14  ? -7.85400  33.78700  -15.23200 1.000 18.31555  ? 14  SER L C   1 
ATOM   3530 O O   . SER C  3 14  ? -8.96000  33.34400  -15.00500 1.000 19.01701  ? 14  SER L O   1 
ATOM   3531 C CB  . SER C  3 14  ? -7.68700  36.24000  -15.89600 1.000 20.89859  ? 14  SER L CB  1 
ATOM   3532 O OG  . SER C  3 14  ? -7.22300  37.14400  -16.86500 1.000 27.25249  ? 14  SER L OG  1 
ATOM   3533 N N   . ILE C  3 15  ? -6.78800  33.41800  -14.53300 1.000 15.57115  ? 15  ILE L N   1 
ATOM   3534 C CA  . ILE C  3 15  ? -6.92000  32.57000  -13.35500 1.000 14.46009  ? 15  ILE L CA  1 
ATOM   3535 C C   . ILE C  3 15  ? -7.78500  33.28000  -12.30300 1.000 20.59031  ? 15  ILE L C   1 
ATOM   3536 O O   . ILE C  3 15  ? -7.54800  34.42300  -11.99400 1.000 20.91143  ? 15  ILE L O   1 
ATOM   3537 C CB  . ILE C  3 15  ? -5.55500  32.11300  -12.75800 1.000 15.22295  ? 15  ILE L CB  1 
ATOM   3538 C CG1 . ILE C  3 15  ? -4.65800  31.50700  -13.84900 1.000 17.57675  ? 15  ILE L CG1 1 
ATOM   3539 C CG2 . ILE C  3 15  ? -5.73800  31.15600  -11.59900 1.000 16.45436  ? 15  ILE L CG2 1 
ATOM   3540 C CD1 . ILE C  3 15  ? -5.27000  30.35300  -14.60100 1.000 16.88398  ? 15  ILE L CD1 1 
ATOM   3541 N N   . GLY C  3 16  ? -8.77700  32.58800  -11.76300 1.000 21.26907  ? 16  GLY L N   1 
ATOM   3542 C CA  . GLY C  3 16  ? -9.72700  33.19000  -10.81000 1.000 17.49830  ? 16  GLY L CA  1 
ATOM   3543 C C   . GLY C  3 16  ? -11.02500 33.61300  -11.47500 1.000 19.06516  ? 16  GLY L C   1 
ATOM   3544 O O   . GLY C  3 16  ? -12.00300 33.85300  -10.76500 1.000 21.89948  ? 16  GLY L O   1 
ATOM   3545 N N   . ASP C  3 17  ? -11.04700 33.66700  -12.79000 1.000 15.55966  ? 17  ASP L N   1 
ATOM   3546 C CA  . ASP C  3 17  ? -12.23700 34.03800  -13.50100 1.000 16.50580  ? 17  ASP L CA  1 
ATOM   3547 C C   . ASP C  3 17  ? -13.32300 32.94800  -13.51300 1.000 27.01238  ? 17  ASP L C   1 
ATOM   3548 O O   . ASP C  3 17  ? -13.03300 31.77400  -13.36300 1.000 22.05171  ? 17  ASP L O   1 
ATOM   3549 C CB  . ASP C  3 17  ? -11.91800 34.34700  -14.94100 1.000 18.49076  ? 17  ASP L CB  1 
ATOM   3550 C CG  . ASP C  3 17  ? -11.38700 35.74400  -15.15900 1.000 33.12088  ? 17  ASP L CG  1 
ATOM   3551 O OD1 . ASP C  3 17  ? -11.23700 36.50200  -14.18700 1.000 25.43450  ? 17  ASP L OD1 1 
ATOM   3552 O OD2 . ASP C  3 17  ? -11.12200 36.07300  -16.33600 1.000 33.62406  ? 17  ASP L OD2 1 
ATOM   3553 N N   . ARG C  3 18  ? -14.55600 33.36300  -13.72500 1.000 25.50999  ? 18  ARG L N   1 
ATOM   3554 C CA  . ARG C  3 18  ? -15.68200 32.41200  -13.83100 1.000 25.98151  ? 18  ARG L CA  1 
ATOM   3555 C C   . ARG C  3 18  ? -15.94500 32.20400  -15.32000 1.000 28.37129  ? 18  ARG L C   1 
ATOM   3556 O O   . ARG C  3 18  ? -16.15900 33.19000  -16.02600 1.000 25.58819  ? 18  ARG L O   1 
ATOM   3557 C CB  . ARG C  3 18  ? -16.91100 32.95900  -13.10000 1.000 28.56923  ? 18  ARG L CB  1 
ATOM   3558 C CG  . ARG C  3 18  ? -18.21700 32.23200  -13.37600 1.000 33.58106  ? 18  ARG L CG  1 
ATOM   3559 C CD  . ARG C  3 18  ? -19.32600 33.06200  -12.76000 1.000 42.23428  ? 18  ARG L CD  1 
ATOM   3560 N NE  . ARG C  3 18  ? -20.55300 32.32500  -12.51600 1.000 47.87673  ? 18  ARG L NE  1 
ATOM   3561 C CZ  . ARG C  3 18  ? -20.89000 31.79000  -11.35000 1.000 62.24630  ? 18  ARG L CZ  1 
ATOM   3562 N NH1 . ARG C  3 18  ? -20.08100 31.90000  -10.31200 1.000 62.98479  ? 18  ARG L NH1 1 
ATOM   3563 N NH2 . ARG C  3 18  ? -22.03100 31.13600  -11.23100 1.000 62.54936  ? 18  ARG L NH2 1 
ATOM   3564 N N   . VAL C  3 19  ? -15.87000 30.95700  -15.76600 1.000 26.60521  ? 19  VAL L N   1 
ATOM   3565 C CA  . VAL C  3 19  ? -16.05000 30.64900  -17.20900 1.000 24.92080  ? 19  VAL L CA  1 
ATOM   3566 C C   . VAL C  3 19  ? -17.40100 29.98000  -17.39200 1.000 25.61423  ? 19  VAL L C   1 
ATOM   3567 O O   . VAL C  3 19  ? -17.77900 29.15800  -16.56000 1.000 22.05840  ? 19  VAL L O   1 
ATOM   3568 C CB  . VAL C  3 19  ? -14.93000 29.74800  -17.76200 1.000 24.33427  ? 19  VAL L CB  1 
ATOM   3569 C CG1 . VAL C  3 19  ? -15.24800 29.22800  -19.15100 1.000 25.50633  ? 19  VAL L CG1 1 
ATOM   3570 C CG2 . VAL C  3 19  ? -13.57500 30.43100  -17.72800 1.000 27.51490  ? 19  VAL L CG2 1 
ATOM   3571 N N   . THR C  3 20  ? -18.05200 30.30900  -18.47900 1.000 21.09242  ? 20  THR L N   1 
ATOM   3572 C CA  . THR C  3 20  ? -19.29800 29.71500  -18.79800 1.000 22.00402  ? 20  THR L CA  1 
ATOM   3573 C C   . THR C  3 20  ? -19.26500 29.15200  -20.22400 1.000 21.99580  ? 20  THR L C   1 
ATOM   3574 O O   . THR C  3 20  ? -18.94200 29.84100  -21.16200 1.000 19.81960  ? 20  THR L O   1 
ATOM   3575 C CB  . THR C  3 20  ? -20.42900 30.73200  -18.63000 1.000 26.76525  ? 20  THR L CB  1 
ATOM   3576 O OG1 . THR C  3 20  ? -20.73500 30.87000  -17.24100 1.000 38.00312  ? 20  THR L OG1 1 
ATOM   3577 C CG2 . THR C  3 20  ? -21.66000 30.28400  -19.37100 1.000 40.05897  ? 20  THR L CG2 1 
ATOM   3578 N N   . ILE C  3 21  ? -19.55600 27.87700  -20.34900 1.000 20.18052  ? 21  ILE L N   1 
ATOM   3579 C CA  . ILE C  3 21  ? -19.62100 27.24800  -21.64000 1.000 19.56415  ? 21  ILE L CA  1 
ATOM   3580 C C   . ILE C  3 21  ? -21.04400 26.75600  -21.85100 1.000 23.35220  ? 21  ILE L C   1 
ATOM   3581 O O   . ILE C  3 21  ? -21.59600 26.07600  -21.00000 1.000 21.71902  ? 21  ILE L O   1 
ATOM   3582 C CB  . ILE C  3 21  ? -18.66100 26.08200  -21.75900 1.000 20.19061  ? 21  ILE L CB  1 
ATOM   3583 C CG1 . ILE C  3 21  ? -17.22100 26.53800  -21.52400 1.000 20.73238  ? 21  ILE L CG1 1 
ATOM   3584 C CG2 . ILE C  3 21  ? -18.80400 25.40800  -23.11600 1.000 18.80845  ? 21  ILE L CG2 1 
ATOM   3585 C CD1 . ILE C  3 21  ? -16.26700 25.39400  -21.29400 1.000 16.65839  ? 21  ILE L CD1 1 
ATOM   3586 N N   . THR C  3 22  ? -21.61500 27.07700  -22.99100 1.000 22.86757  ? 22  THR L N   1 
ATOM   3587 C CA  . THR C  3 22  ? -23.00400 26.73500  -23.26400 1.000 20.89335  ? 22  THR L CA  1 
ATOM   3588 C C   . THR C  3 22  ? -23.18500 25.62600  -24.31500 1.000 26.56553  ? 22  THR L C   1 
ATOM   3589 O O   . THR C  3 22  ? -22.35200 25.45500  -25.18300 1.000 21.91328  ? 22  THR L O   1 
ATOM   3590 C CB  . THR C  3 22  ? -23.81500 28.02500  -23.59200 1.000 25.88659  ? 22  THR L CB  1 
ATOM   3591 O OG1 . THR C  3 22  ? -23.61500 29.00700  -22.57200 1.000 27.48960  ? 22  THR L OG1 1 
ATOM   3592 C CG2 . THR C  3 22  ? -25.29400 27.72600  -23.71800 1.000 33.69440  ? 22  THR L CG2 1 
ATOM   3593 N N   . CYS C  3 23  ? -24.26700 24.87100  -24.20800 1.000 27.50762  ? 23  CYS L N   1 
ATOM   3594 C CA  . CYS C  3 23  ? -24.55600 23.75900  -25.10300 1.000 25.93379  ? 23  CYS L CA  1 
ATOM   3595 C C   . CYS C  3 23  ? -26.03500 23.79100  -25.45900 1.000 28.00965  ? 23  CYS L C   1 
ATOM   3596 O O   . CYS C  3 23  ? -26.87700 23.80500  -24.55600 1.000 25.50300  ? 23  CYS L O   1 
ATOM   3597 C CB  . CYS C  3 23  ? -24.15600 22.44100  -24.43000 1.000 27.03177  ? 23  CYS L CB  1 
ATOM   3598 S SG  . CYS C  3 23  ? -24.35100 20.97000  -25.42800 1.000 39.43894  ? 23  CYS L SG  1 
ATOM   3599 N N   . ARG C  3 24  ? -26.35400 23.84800  -26.75700 1.000 27.45560  ? 24  ARG L N   1 
ATOM   3600 C CA  . ARG C  3 24  ? -27.74000 23.68800  -27.19400 1.000 27.23462  ? 24  ARG L CA  1 
ATOM   3601 C C   . ARG C  3 24  ? -27.91900 22.52500  -28.15400 1.000 30.52444  ? 24  ARG L C   1 
ATOM   3602 O O   . ARG C  3 24  ? -27.27600 22.50100  -29.21600 1.000 29.00830  ? 24  ARG L O   1 
ATOM   3603 C CB  . ARG C  3 24  ? -28.33100 24.94900  -27.81200 1.000 35.00038  ? 24  ARG L CB  1 
ATOM   3604 C CG  . ARG C  3 24  ? -28.25000 26.15200  -26.90400 1.000 49.39364  ? 24  ARG L CG  1 
ATOM   3605 C CD  . ARG C  3 24  ? -29.00500 27.33200  -27.50600 1.000 60.36056  ? 24  ARG L CD  1 
ATOM   3606 N NE  . ARG C  3 24  ? -30.41800 26.92800  -27.56500 1.000 72.10966  ? 24  ARG L NE  1 
ATOM   3607 C CZ  . ARG C  3 24  ? -31.43200 27.54100  -26.96100 1.000 68.92680  ? 24  ARG L CZ  1 
ATOM   3608 N NH1 . ARG C  3 24  ? -31.24900 28.62300  -26.21700 1.000 69.64223  ? 24  ARG L NH1 1 
ATOM   3609 N NH2 . ARG C  3 24  ? -32.66100 27.04100  -27.09300 1.000 63.96292  ? 24  ARG L NH2 1 
ATOM   3610 N N   . PRO C  3 25  ? -28.78100 21.55900  -27.83200 1.000 32.68333  ? 25  PRO L N   1 
ATOM   3611 C CA  . PRO C  3 25  ? -29.13600 20.49300  -28.77700 1.000 33.49112  ? 25  PRO L CA  1 
ATOM   3612 C C   . PRO C  3 25  ? -30.26600 20.92900  -29.71200 1.000 35.41105  ? 25  PRO L C   1 
ATOM   3613 O O   . PRO C  3 25  ? -30.94900 21.93200  -29.48100 1.000 28.98981  ? 25  PRO L O   1 
ATOM   3614 C CB  . PRO C  3 25  ? -29.63000 19.36700  -27.85200 1.000 28.62320  ? 25  PRO L CB  1 
ATOM   3615 C CG  . PRO C  3 25  ? -30.29800 20.13000  -26.70300 1.000 34.70812  ? 25  PRO L CG  1 
ATOM   3616 C CD  . PRO C  3 25  ? -29.65600 21.54000  -26.64200 1.000 30.88488  ? 25  PRO L CD  1 
ATOM   3617 N N   . SER C  3 26  ? -30.39400 20.18600  -30.81300 1.000 36.50817  ? 26  SER L N   1 
ATOM   3618 C CA  . SER C  3 26  ? -31.39700 20.45100  -31.87600 1.000 38.46738  ? 26  SER L CA  1 
ATOM   3619 C C   . SER C  3 26  ? -32.82600 20.14900  -31.42200 1.000 43.75860  ? 26  SER L C   1 
ATOM   3620 O O   . SER C  3 26  ? -33.75900 20.57000  -32.11900 1.000 38.96749  ? 26  SER L O   1 
ATOM   3621 C CB  . SER C  3 26  ? -31.03800 19.61900  -33.08300 1.000 33.40129  ? 26  SER L CB  1 
ATOM   3622 O OG  . SER C  3 26  ? -30.58200 18.33100  -32.71600 1.000 35.03011  ? 26  SER L OG  1 
ATOM   3623 N N   . GLN C  3 27  ? -32.99000 19.39900  -30.34000 1.000 39.38667  ? 27  GLN L N   1 
ATOM   3624 C CA  . GLN C  3 27  ? -34.33100 19.10600  -29.79100 1.000 39.39193  ? 27  GLN L CA  1 
ATOM   3625 C C   . GLN C  3 27  ? -34.24000 19.06700  -28.26700 1.000 40.83944  ? 27  GLN L C   1 
ATOM   3626 O O   . GLN C  3 27  ? -33.12700 19.11100  -27.75300 1.000 37.42253  ? 27  GLN L O   1 
ATOM   3627 C CB  . GLN C  3 27  ? -34.83900 17.76200  -30.31100 1.000 38.02867  ? 27  GLN L CB  1 
ATOM   3628 C CG  . GLN C  3 27  ? -33.87800 16.60200  -30.12800 1.000 37.48559  ? 27  GLN L CG  1 
ATOM   3629 C CD  . GLN C  3 27  ? -34.50400 15.32000  -30.61800 1.000 49.89743  ? 27  GLN L CD  1 
ATOM   3630 O OE1 . GLN C  3 27  ? -34.22200 14.84800  -31.71400 1.000 42.94415  ? 27  GLN L OE1 1 
ATOM   3631 N NE2 . GLN C  3 27  ? -35.37500 14.74900  -29.80400 1.000 50.23182  ? 27  GLN L NE2 1 
ATOM   3632 N N   . ASN C  3 28  ? -35.37700 18.98400  -27.58600 1.000 33.87969  ? 28  ASN L N   1 
ATOM   3633 C CA  . ASN C  3 28  ? -35.35600 18.83900  -26.11000 1.000 38.39216  ? 28  ASN L CA  1 
ATOM   3634 C C   . ASN C  3 28  ? -34.79900 17.46200  -25.75500 1.000 39.55944  ? 28  ASN L C   1 
ATOM   3635 O O   . ASN C  3 28  ? -35.18600 16.49100  -26.40100 1.000 36.42288  ? 28  ASN L O   1 
ATOM   3636 C CB  . ASN C  3 28  ? -36.71900 19.09600  -25.46400 1.000 30.77519  ? 28  ASN L CB  1 
ATOM   3637 C CG  . ASN C  3 28  ? -36.69900 19.04600  -23.95400 1.000 38.03339  ? 28  ASN L CG  1 
ATOM   3638 O OD1 . ASN C  3 28  ? -36.22000 18.08500  -23.36500 1.000 46.45227  ? 28  ASN L OD1 1 
ATOM   3639 N ND2 . ASN C  3 28  ? -37.23600 20.07400  -23.32400 1.000 46.07818  ? 28  ASN L ND2 1 
ATOM   3640 N N   . ILE C  3 29  ? -33.93200 17.41000  -24.75200 1.000 37.42235  ? 29  ILE L N   1 
ATOM   3641 C CA  . ILE C  3 29  ? -33.30200 16.16700  -24.32400 1.000 31.83644  ? 29  ILE L CA  1 
ATOM   3642 C C   . ILE C  3 29  ? -33.39000 15.97500  -22.80900 1.000 26.55327  ? 29  ILE L C   1 
ATOM   3643 O O   . ILE C  3 29  ? -32.66600 15.14900  -22.25000 1.000 26.99817  ? 29  ILE L O   1 
ATOM   3644 C CB  . ILE C  3 29  ? -31.84200 16.14100  -24.80500 1.000 33.87401  ? 29  ILE L CB  1 
ATOM   3645 C CG1 . ILE C  3 29  ? -31.09600 17.36400  -24.24500 1.000 30.60929  ? 29  ILE L CG1 1 
ATOM   3646 C CG2 . ILE C  3 29  ? -31.76500 16.08100  -26.35700 1.000 25.22094  ? 29  ILE L CG2 1 
ATOM   3647 C CD1 . ILE C  3 29  ? -29.59400 17.36300  -24.54500 1.000 26.25050  ? 29  ILE L CD1 1 
ATOM   3648 N N   . ARG C  3 30  ? -34.26000 16.73400  -22.19200 1.000 29.68900  ? 30  ARG L N   1 
ATOM   3649 C CA  . ARG C  3 30  ? -34.44700 16.64600  -20.76900 1.000 34.59762  ? 30  ARG L CA  1 
ATOM   3650 C C   . ARG C  3 30  ? -33.11800 16.91400  -20.06600 1.000 32.20652  ? 30  ARG L C   1 
ATOM   3651 O O   . ARG C  3 30  ? -32.51600 17.93900  -20.29500 1.000 34.70394  ? 30  ARG L O   1 
ATOM   3652 C CB  . ARG C  3 30  ? -35.07100 15.28800  -20.40700 1.000 36.97472  ? 30  ARG L CB  1 
ATOM   3653 C CG  . ARG C  3 30  ? -36.13000 14.81900  -21.37800 1.000 50.00538  ? 30  ARG L CG  1 
ATOM   3654 C CD  . ARG C  3 30  ? -37.33000 15.73800  -21.34000 1.000 54.02331  ? 30  ARG L CD  1 
ATOM   3655 N NE  . ARG C  3 30  ? -38.57400 14.99700  -21.48300 1.000 75.55598  ? 30  ARG L NE  1 
ATOM   3656 C CZ  . ARG C  3 30  ? -39.21400 14.81700  -22.63300 1.000 78.09844  ? 30  ARG L CZ  1 
ATOM   3657 N NH1 . ARG C  3 30  ? -38.73200 15.32600  -23.76100 1.000 53.85452  ? 30  ARG L NH1 1 
ATOM   3658 N NH2 . ARG C  3 30  ? -40.34100 14.12400  -22.65100 1.000 83.50576  ? 30  ARG L NH2 1 
ATOM   3659 N N   . SER C  3 31  ? -32.67600 15.99900  -19.22800 1.000 29.97867  ? 31  SER L N   1 
ATOM   3660 C CA  . SER C  3 31  ? -31.40100 16.14700  -18.53900 1.000 26.09033  ? 31  SER L CA  1 
ATOM   3661 C C   . SER C  3 31  ? -30.42100 15.07200  -18.98000 1.000 20.54839  ? 31  SER L C   1 
ATOM   3662 O O   . SER C  3 31  ? -29.53700 14.69300  -18.24000 1.000 26.34836  ? 31  SER L O   1 
ATOM   3663 C CB  . SER C  3 31  ? -31.63400 16.20100  -17.02500 1.000 20.44015  ? 31  SER L CB  1 
ATOM   3664 O OG  . SER C  3 31  ? -32.53800 17.22000  -16.67700 1.000 30.58502  ? 31  SER L OG  1 
ATOM   3665 N N   . PHE C  3 32  ? -30.57100 14.61600  -20.20600 1.000 24.04243  ? 32  PHE L N   1 
ATOM   3666 C CA  . PHE C  3 32  ? -29.72700 13.57700  -20.74000 1.000 25.93696  ? 32  PHE L CA  1 
ATOM   3667 C C   . PHE C  3 32  ? -28.56100 14.25300  -21.43900 1.000 26.32827  ? 32  PHE L C   1 
ATOM   3668 O O   . PHE C  3 32  ? -28.43200 14.17700  -22.64000 1.000 21.35347  ? 32  PHE L O   1 
ATOM   3669 C CB  . PHE C  3 32  ? -30.51900 12.67700  -21.67600 1.000 26.57702  ? 32  PHE L CB  1 
ATOM   3670 C CG  . PHE C  3 32  ? -31.59200 11.87700  -20.99400 1.000 35.13940  ? 32  PHE L CG  1 
ATOM   3671 C CD1 . PHE C  3 32  ? -32.78100 12.47000  -20.60800 1.000 35.78004  ? 32  PHE L CD1 1 
ATOM   3672 C CD2 . PHE C  3 32  ? -31.41600 10.53000  -20.74900 1.000 29.95682  ? 32  PHE L CD2 1 
ATOM   3673 C CE1 . PHE C  3 32  ? -33.76700 11.73800  -19.97800 1.000 34.58252  ? 32  PHE L CE1 1 
ATOM   3674 C CE2 . PHE C  3 32  ? -32.39900 9.79100   -20.12100 1.000 33.80191  ? 32  PHE L CE2 1 
ATOM   3675 C CZ  . PHE C  3 32  ? -33.57400 10.39600  -19.73700 1.000 32.33353  ? 32  PHE L CZ  1 
ATOM   3676 N N   . LEU C  3 33  ? -27.74100 14.92600  -20.65200 1.000 24.78923  ? 33  LEU L N   1 
ATOM   3677 C CA  . LEU C  3 33  ? -26.60100 15.63000  -21.17000 1.000 22.32878  ? 33  LEU L CA  1 
ATOM   3678 C C   . LEU C  3 33  ? -25.47700 15.55600  -20.15500 1.000 24.17079  ? 33  LEU L C   1 
ATOM   3679 O O   . LEU C  3 33  ? -25.69100 15.74200  -18.96500 1.000 19.06555  ? 33  LEU L O   1 
ATOM   3680 C CB  . LEU C  3 33  ? -26.95800 17.06800  -21.45400 1.000 23.39432  ? 33  LEU L CB  1 
ATOM   3681 C CG  . LEU C  3 33  ? -25.81400 17.90900  -22.01700 1.000 27.97521  ? 33  LEU L CG  1 
ATOM   3682 C CD1 . LEU C  3 33  ? -26.31900 18.79500  -23.13500 1.000 36.84118  ? 33  LEU L CD1 1 
ATOM   3683 C CD2 . LEU C  3 33  ? -25.12900 18.72400  -20.93400 1.000 19.59840  ? 33  LEU L CD2 1 
ATOM   3684 N N   . ASN C  3 34  ? -24.30000 15.27300  -20.63900 1.000 20.04702  ? 34  ASN L N   1 
ATOM   3685 C CA  . ASN C  3 34  ? -23.14100 15.15400  -19.79800 1.000 22.39865  ? 34  ASN L CA  1 
ATOM   3686 C C   . ASN C  3 34  ? -22.02100 16.06700  -20.31900 1.000 15.09942  ? 34  ASN L C   1 
ATOM   3687 O O   . ASN C  3 34  ? -22.04400 16.46600  -21.45600 1.000 16.02990  ? 34  ASN L O   1 
ATOM   3688 C CB  . ASN C  3 34  ? -22.66900 13.72100  -19.78400 1.000 14.89526  ? 34  ASN L CB  1 
ATOM   3689 C CG  . ASN C  3 34  ? -23.77500 12.74000  -19.43600 1.000 26.09299  ? 34  ASN L CG  1 
ATOM   3690 O OD1 . ASN C  3 34  ? -24.65400 13.03700  -18.64000 1.000 23.65242  ? 34  ASN L OD1 1 
ATOM   3691 N ND2 . ASN C  3 34  ? -23.72500 11.56400  -20.03600 1.000 25.47457  ? 34  ASN L ND2 1 
ATOM   3692 N N   . TRP C  3 35  ? -21.07300 16.38100  -19.46400 1.000 17.55376  ? 35  TRP L N   1 
ATOM   3693 C CA  . TRP C  3 35  ? -19.95400 17.22500  -19.84500 1.000 17.36261  ? 35  TRP L CA  1 
ATOM   3694 C C   . TRP C  3 35  ? -18.65000 16.52600  -19.59800 1.000 19.88475  ? 35  TRP L C   1 
ATOM   3695 O O   . TRP C  3 35  ? -18.43900 15.95000  -18.54000 1.000 21.09232  ? 35  TRP L O   1 
ATOM   3696 C CB  . TRP C  3 35  ? -19.96000 18.53200  -19.09400 1.000 14.21517  ? 35  TRP L CB  1 
ATOM   3697 C CG  . TRP C  3 35  ? -21.04200 19.47500  -19.40900 1.000 18.63342  ? 35  TRP L CG  1 
ATOM   3698 C CD1 . TRP C  3 35  ? -22.22900 19.59400  -18.76900 1.000 19.05583  ? 35  TRP L CD1 1 
ATOM   3699 C CD2 . TRP C  3 35  ? -21.02000 20.48700  -20.41100 1.000 19.66875  ? 35  TRP L CD2 1 
ATOM   3700 N NE1 . TRP C  3 35  ? -22.96700 20.60300  -19.32300 1.000 16.28006  ? 35  TRP L NE1 1 
ATOM   3701 C CE2 . TRP C  3 35  ? -22.24600 21.16800  -20.33900 1.000 22.38066  ? 35  TRP L CE2 1 
ATOM   3702 C CE3 . TRP C  3 35  ? -20.08500 20.87900  -21.37400 1.000 18.06379  ? 35  TRP L CE3 1 
ATOM   3703 C CZ2 . TRP C  3 35  ? -22.56100 22.22400  -21.18800 1.000 20.36960  ? 35  TRP L CZ2 1 
ATOM   3704 C CZ3 . TRP C  3 35  ? -20.40300 21.91900  -22.21600 1.000 18.65174  ? 35  TRP L CZ3 1 
ATOM   3705 C CH2 . TRP C  3 35  ? -21.62800 22.58300  -22.11500 1.000 18.14998  ? 35  TRP L CH2 1 
ATOM   3706 N N   . PHE C  3 36  ? -17.77600 16.59300  -20.56900 1.000 17.98736  ? 36  PHE L N   1 
ATOM   3707 C CA  . PHE C  3 36  ? -16.48200 15.99400  -20.45000 1.000 19.43114  ? 36  PHE L CA  1 
ATOM   3708 C C   . PHE C  3 36  ? -15.31300 16.98400  -20.49500 1.000 19.38041  ? 36  PHE L C   1 
ATOM   3709 O O   . PHE C  3 36  ? -15.44500 18.06000  -21.05100 1.000 19.76394  ? 36  PHE L O   1 
ATOM   3710 C CB  . PHE C  3 36  ? -16.27400 15.01400  -21.59000 1.000 18.72054  ? 36  PHE L CB  1 
ATOM   3711 C CG  . PHE C  3 36  ? -17.04500 13.73800  -21.48300 1.000 19.38943  ? 36  PHE L CG  1 
ATOM   3712 C CD1 . PHE C  3 36  ? -18.30800 13.64000  -22.01400 1.000 15.63231  ? 36  PHE L CD1 1 
ATOM   3713 C CD2 . PHE C  3 36  ? -16.47300 12.61900  -20.91400 1.000 18.26026  ? 36  PHE L CD2 1 
ATOM   3714 C CE1 . PHE C  3 36  ? -19.01200 12.46000  -21.94400 1.000 19.58587  ? 36  PHE L CE1 1 
ATOM   3715 C CE2 . PHE C  3 36  ? -17.16700 11.43000  -20.84300 1.000 21.90072  ? 36  PHE L CE2 1 
ATOM   3716 C CZ  . PHE C  3 36  ? -18.44100 11.35100  -21.35600 1.000 17.66039  ? 36  PHE L CZ  1 
ATOM   3717 N N   . GLN C  3 37  ? -14.19900 16.60900  -19.91700 1.000 15.39344  ? 37  GLN L N   1 
ATOM   3718 C CA  . GLN C  3 37  ? -12.99900 17.39500  -19.99200 1.000 17.65682  ? 37  GLN L CA  1 
ATOM   3719 C C   . GLN C  3 37  ? -11.95900 16.57100  -20.74300 1.000 21.08005  ? 37  GLN L C   1 
ATOM   3720 O O   . GLN C  3 37  ? -11.73500 15.41800  -20.42700 1.000 18.29204  ? 37  GLN L O   1 
ATOM   3721 C CB  . GLN C  3 37  ? -12.47200 17.76600  -18.60900 1.000 18.64367  ? 37  GLN L CB  1 
ATOM   3722 C CG  . GLN C  3 37  ? -11.07900 18.37100  -18.59900 1.000 14.97775  ? 37  GLN L CG  1 
ATOM   3723 C CD  . GLN C  3 37  ? -10.56100 18.64600  -17.19900 1.000 20.34088  ? 37  GLN L CD  1 
ATOM   3724 O OE1 . GLN C  3 37  ? -10.02700 17.76700  -16.54800 1.000 22.60986  ? 37  GLN L OE1 1 
ATOM   3725 N NE2 . GLN C  3 37  ? -10.72100 19.87300  -16.73700 1.000 18.95548  ? 37  GLN L NE2 1 
ATOM   3726 N N   . HIS C  3 38  ? -11.32000 17.17600  -21.70500 1.000 15.71092  ? 38  HIS L N   1 
ATOM   3727 C CA  . HIS C  3 38  ? -10.29200 16.49400  -22.46300 1.000 14.88974  ? 38  HIS L CA  1 
ATOM   3728 C C   . HIS C  3 38  ? -8.96600  17.26200  -22.62900 1.000 17.18060  ? 38  HIS L C   1 
ATOM   3729 O O   . HIS C  3 38  ? -8.93200  18.33600  -23.16700 1.000 21.69833  ? 38  HIS L O   1 
ATOM   3730 C CB  . HIS C  3 38  ? -10.81700 16.04800  -23.83600 1.000 16.01210  ? 38  HIS L CB  1 
ATOM   3731 C CG  . HIS C  3 38  ? -9.90300  15.11600  -24.56300 1.000 18.47740  ? 38  HIS L CG  1 
ATOM   3732 N ND1 . HIS C  3 38  ? -9.94100  14.95600  -25.92900 1.000 22.43579  ? 38  HIS L ND1 1 
ATOM   3733 C CD2 . HIS C  3 38  ? -8.93100  14.29100  -24.11500 1.000 19.37435  ? 38  HIS L CD2 1 
ATOM   3734 C CE1 . HIS C  3 38  ? -9.03000  14.07500  -26.29200 1.000 30.10553  ? 38  HIS L CE1 1 
ATOM   3735 N NE2 . HIS C  3 38  ? -8.40200  13.65600  -25.20900 1.000 26.89013  ? 38  HIS L NE2 1 
ATOM   3736 N N   . LYS C  3 39  ? -7.90900  16.68600  -22.12900 1.000 17.31044  ? 39  LYS L N   1 
ATOM   3737 C CA  . LYS C  3 39  ? -6.56800  17.26900  -22.30400 1.000 27.83393  ? 39  LYS L CA  1 
ATOM   3738 C C   . LYS C  3 39  ? -5.82900  16.42600  -23.35200 1.000 24.01672  ? 39  LYS L C   1 
ATOM   3739 O O   . LYS C  3 39  ? -5.92500  15.20000  -23.31400 1.000 23.94945  ? 39  LYS L O   1 
ATOM   3740 C CB  . LYS C  3 39  ? -5.83200  17.27200  -20.97000 1.000 24.60119  ? 39  LYS L CB  1 
ATOM   3741 C CG  . LYS C  3 39  ? -6.47800  18.09800  -19.87000 1.000 19.94035  ? 39  LYS L CG  1 
ATOM   3742 C CD  . LYS C  3 39  ? -5.70900  18.03700  -18.57600 1.000 20.24799  ? 39  LYS L CD  1 
ATOM   3743 C CE  . LYS C  3 39  ? -6.32400  18.87900  -17.48300 1.000 28.16313  ? 39  LYS L CE  1 
ATOM   3744 N NZ  . LYS C  3 39  ? -5.34800  19.16000  -16.40800 1.000 30.34207  ? 39  LYS L NZ  1 
ATOM   3745 N N   . PRO C  3 40  ? -5.06700  17.05800  -24.25800 1.000 30.46378  ? 40  PRO L N   1 
ATOM   3746 C CA  . PRO C  3 40  ? -4.33900  16.32600  -25.28500 1.000 36.60159  ? 40  PRO L CA  1 
ATOM   3747 C C   . PRO C  3 40  ? -3.54000  15.13300  -24.74400 1.000 25.16636  ? 40  PRO L C   1 
ATOM   3748 O O   . PRO C  3 40  ? -2.82600  15.29100  -23.80300 1.000 25.44090  ? 40  PRO L O   1 
ATOM   3749 C CB  . PRO C  3 40  ? -3.42000  17.41500  -25.87200 1.000 34.99111  ? 40  PRO L CB  1 
ATOM   3750 C CG  . PRO C  3 40  ? -4.20600  18.68800  -25.69600 1.000 36.82824  ? 40  PRO L CG  1 
ATOM   3751 C CD  . PRO C  3 40  ? -4.90500  18.50800  -24.36800 1.000 29.99614  ? 40  PRO L CD  1 
ATOM   3752 N N   . GLY C  3 41  ? -3.75700  13.95900  -25.33500 1.000 29.13119  ? 41  GLY L N   1 
ATOM   3753 C CA  . GLY C  3 41  ? -2.97100  12.76800  -24.97100 1.000 25.57799  ? 41  GLY L CA  1 
ATOM   3754 C C   . GLY C  3 41  ? -3.39100  12.14700  -23.66300 1.000 37.58689  ? 41  GLY L C   1 
ATOM   3755 O O   . GLY C  3 41  ? -2.66900  11.26300  -23.17300 1.000 31.22633  ? 41  GLY L O   1 
ATOM   3756 N N   . LYS C  3 42  ? -4.51400  12.59900  -23.11800 1.000 24.53058  ? 42  LYS L N   1 
ATOM   3757 C CA  . LYS C  3 42  ? -5.02800  12.01700  -21.86500 1.000 24.45727  ? 42  LYS L CA  1 
ATOM   3758 C C   . LYS C  3 42  ? -6.41900  11.43700  -22.11000 1.000 23.59598  ? 42  LYS L C   1 
ATOM   3759 O O   . LYS C  3 42  ? -7.01500  11.74700  -23.12100 1.000 24.89489  ? 42  LYS L O   1 
ATOM   3760 C CB  . LYS C  3 42  ? -5.07600  13.07500  -20.77000 1.000 24.09490  ? 42  LYS L CB  1 
ATOM   3761 C CG  . LYS C  3 42  ? -3.74200  13.72100  -20.43100 1.000 41.72386  ? 42  LYS L CG  1 
ATOM   3762 C CD  . LYS C  3 42  ? -2.95800  12.95900  -19.38600 1.000 42.86301  ? 42  LYS L CD  1 
ATOM   3763 C CE  . LYS C  3 42  ? -1.64200  13.62000  -19.03200 1.000 61.62841  ? 42  LYS L CE  1 
ATOM   3764 N NZ  . LYS C  3 42  ? -0.57400  12.62300  -18.78400 1.000 58.62540  ? 42  LYS L NZ  1 
ATOM   3765 N N   . ALA C  3 43  ? -6.88200  10.62200  -21.17200 1.000 26.24425  ? 43  ALA L N   1 
ATOM   3766 C CA  . ALA C  3 43  ? -8.23800  10.05100  -21.29000 1.000 23.81659  ? 43  ALA L CA  1 
ATOM   3767 C C   . ALA C  3 43  ? -9.30300  11.09700  -20.98100 1.000 22.47045  ? 43  ALA L C   1 
ATOM   3768 O O   . ALA C  3 43  ? -9.19700  11.77100  -19.96300 1.000 21.20631  ? 43  ALA L O   1 
ATOM   3769 C CB  . ALA C  3 43  ? -8.39000  8.88600   -20.35500 1.000 22.29004  ? 43  ALA L CB  1 
ATOM   3770 N N   . PRO C  3 44  ? -10.32100 11.25800  -21.84200 1.000 17.49829  ? 44  PRO L N   1 
ATOM   3771 C CA  . PRO C  3 44  ? -11.45500 12.11000  -21.45100 1.000 17.72236  ? 44  PRO L CA  1 
ATOM   3772 C C   . PRO C  3 44  ? -12.01600 11.74900  -20.06900 1.000 22.56074  ? 44  PRO L C   1 
ATOM   3773 O O   . PRO C  3 44  ? -11.91800 10.60700  -19.60700 1.000 23.55257  ? 44  PRO L O   1 
ATOM   3774 C CB  . PRO C  3 44  ? -12.45600 11.92200  -22.60000 1.000 16.83065  ? 44  PRO L CB  1 
ATOM   3775 C CG  . PRO C  3 44  ? -11.55800 11.50200  -23.81200 1.000 15.24329  ? 44  PRO L CG  1 
ATOM   3776 C CD  . PRO C  3 44  ? -10.47700 10.67400  -23.18800 1.000 16.54883  ? 44  PRO L CD  1 
ATOM   3777 N N   . LYS C  3 45  ? -12.47700 12.78900  -19.38300 1.000 17.18954  ? 45  LYS L N   1 
ATOM   3778 C CA  . LYS C  3 45  ? -13.02400 12.62800  -18.05800 1.000 18.58460  ? 45  LYS L CA  1 
ATOM   3779 C C   . LYS C  3 45  ? -14.40800 13.21800  -17.93700 1.000 24.18507  ? 45  LYS L C   1 
ATOM   3780 O O   . LYS C  3 45  ? -14.60600 14.37300  -18.25700 1.000 19.47815  ? 45  LYS L O   1 
ATOM   3781 C CB  . LYS C  3 45  ? -12.13300 13.27100  -17.01100 1.000 21.56653  ? 45  LYS L CB  1 
ATOM   3782 C CG  . LYS C  3 45  ? -12.84100 13.76400  -15.77100 1.000 31.36361  ? 45  LYS L CG  1 
ATOM   3783 C CD  . LYS C  3 45  ? -13.15600 12.62800  -14.81900 1.000 45.41004  ? 45  LYS L CD  1 
ATOM   3784 C CE  . LYS C  3 45  ? -13.10200 13.09600  -13.37600 1.000 42.93971  ? 45  LYS L CE  1 
ATOM   3785 N NZ  . LYS C  3 45  ? -13.71700 12.10400  -12.46100 1.000 43.06950  ? 45  LYS L NZ  1 
ATOM   3786 N N   . LEU C  3 46  ? -15.36100 12.45600  -17.47900 1.000 17.98537  ? 46  LEU L N   1 
ATOM   3787 C CA  . LEU C  3 46  ? -16.71100 12.93100  -17.26100 1.000 18.12523  ? 46  LEU L CA  1 
ATOM   3788 C C   . LEU C  3 46  ? -16.79300 13.81900  -15.99200 1.000 20.29433  ? 46  LEU L C   1 
ATOM   3789 O O   . LEU C  3 46  ? -16.60600 13.35100  -14.88800 1.000 19.24759  ? 46  LEU L O   1 
ATOM   3790 C CB  . LEU C  3 46  ? -17.69200 11.75800  -17.17200 1.000 18.96047  ? 46  LEU L CB  1 
ATOM   3791 C CG  . LEU C  3 46  ? -19.15800 12.04700  -16.87900 1.000 25.15419  ? 46  LEU L CG  1 
ATOM   3792 C CD1 . LEU C  3 46  ? -19.75900 12.87100  -17.99600 1.000 21.01019  ? 46  LEU L CD1 1 
ATOM   3793 C CD2 . LEU C  3 46  ? -19.91300 10.74000  -16.70400 1.000 38.22060  ? 46  LEU L CD2 1 
ATOM   3794 N N   . LEU C  3 47  ? -17.05500 15.06700  -16.17100 1.000 17.30520  ? 47  LEU L N   1 
ATOM   3795 C CA  . LEU C  3 47  ? -17.14500 15.98300  -15.03800 1.000 15.51835  ? 47  LEU L CA  1 
ATOM   3796 C C   . LEU C  3 47  ? -18.55800 16.10900  -14.48100 1.000 21.88077  ? 47  LEU L C   1 
ATOM   3797 O O   . LEU C  3 47  ? -18.74600 16.06400  -13.28800 1.000 18.39823  ? 47  LEU L O   1 
ATOM   3798 C CB  . LEU C  3 47  ? -16.65100 17.35800  -15.47600 1.000 19.60243  ? 47  LEU L CB  1 
ATOM   3799 C CG  . LEU C  3 47  ? -15.20800 17.55900  -15.92900 1.000 21.58318  ? 47  LEU L CG  1 
ATOM   3800 C CD1 . LEU C  3 47  ? -14.87900 19.04100  -15.95400 1.000 25.37132  ? 47  LEU L CD1 1 
ATOM   3801 C CD2 . LEU C  3 47  ? -14.25200 16.81400  -15.02500 1.000 16.96204  ? 47  LEU L CD2 1 
ATOM   3802 N N   . ILE C  3 48  ? -19.51500 16.32800  -15.36000 1.000 15.49895  ? 48  ILE L N   1 
ATOM   3803 C CA  . ILE C  3 48  ? -20.89400 16.47400  -14.95600 1.000 14.15183  ? 48  ILE L CA  1 
ATOM   3804 C C   . ILE C  3 48  ? -21.74600 15.42900  -15.65100 1.000 22.98016  ? 48  ILE L C   1 
ATOM   3805 O O   . ILE C  3 48  ? -21.60500 15.22200  -16.84000 1.000 18.17459  ? 48  ILE L O   1 
ATOM   3806 C CB  . ILE C  3 48  ? -21.46200 17.85200  -15.30600 1.000 18.85262  ? 48  ILE L CB  1 
ATOM   3807 C CG1 . ILE C  3 48  ? -20.54800 18.95900  -14.76200 1.000 17.67676  ? 48  ILE L CG1 1 
ATOM   3808 C CG2 . ILE C  3 48  ? -22.88700 17.99900  -14.79800 1.000 20.25588  ? 48  ILE L CG2 1 
ATOM   3809 C CD1 . ILE C  3 48  ? -20.51400 19.05300  -13.25900 1.000 17.90084  ? 48  ILE L CD1 1 
ATOM   3810 N N   . TYR C  3 49  ? -22.62800 14.79200  -14.89500 1.000 21.26308  ? 49  TYR L N   1 
ATOM   3811 C CA  . TYR C  3 49  ? -23.50700 13.76100  -15.42100 1.000 21.65935  ? 49  TYR L CA  1 
ATOM   3812 C C   . TYR C  3 49  ? -24.94600 14.17000  -15.25800 1.000 20.20366  ? 49  TYR L C   1 
ATOM   3813 O O   . TYR C  3 49  ? -25.35000 14.65300  -14.22900 1.000 20.89444  ? 49  TYR L O   1 
ATOM   3814 C CB  . TYR C  3 49  ? -23.25000 12.42900  -14.69900 1.000 20.11626  ? 49  TYR L CB  1 
ATOM   3815 C CG  . TYR C  3 49  ? -24.07000 11.23800  -15.12800 1.000 22.90065  ? 49  TYR L CG  1 
ATOM   3816 C CD1 . TYR C  3 49  ? -23.92800 10.69100  -16.38500 1.000 21.39291  ? 49  TYR L CD1 1 
ATOM   3817 C CD2 . TYR C  3 49  ? -24.95200 10.63000  -14.24600 1.000 24.77308  ? 49  TYR L CD2 1 
ATOM   3818 C CE1 . TYR C  3 49  ? -24.66100 9.58800   -16.76600 1.000 31.81973  ? 49  TYR L CE1 1 
ATOM   3819 C CE2 . TYR C  3 49  ? -25.69000 9.52700   -14.61200 1.000 19.81683  ? 49  TYR L CE2 1 
ATOM   3820 C CZ  . TYR C  3 49  ? -25.54200 9.00900   -15.87600 1.000 28.60816  ? 49  TYR L CZ  1 
ATOM   3821 O OH  . TYR C  3 49  ? -26.26500 7.91600   -16.25700 1.000 25.15771  ? 49  TYR L OH  1 
ATOM   3822 N N   . ALA C  3 50  ? -25.71600 13.95100  -16.29100 1.000 21.59119  ? 50  ALA L N   1 
ATOM   3823 C CA  . ALA C  3 50  ? -27.12400 14.25500  -16.24600 1.000 18.02352  ? 50  ALA L CA  1 
ATOM   3824 C C   . ALA C  3 50  ? -27.36200 15.70200  -15.89400 1.000 22.87879  ? 50  ALA L C   1 
ATOM   3825 O O   . ALA C  3 50  ? -28.08500 15.99600  -14.96400 1.000 19.95799  ? 50  ALA L O   1 
ATOM   3826 C CB  . ALA C  3 50  ? -27.83200 13.30900  -15.31400 1.000 19.98539  ? 50  ALA L CB  1 
ATOM   3827 N N   . ALA C  3 51  ? -26.70400 16.58000  -16.63100 1.000 22.18408  ? 51  ALA L N   1 
ATOM   3828 C CA  . ALA C  3 51  ? -26.87700 18.02400  -16.48400 1.000 24.04009  ? 51  ALA L CA  1 
ATOM   3829 C C   . ALA C  3 51  ? -26.29400 18.75700  -15.27500 1.000 19.49907  ? 51  ALA L C   1 
ATOM   3830 O O   . ALA C  3 51  ? -25.75300 19.82900  -15.43200 1.000 19.58929  ? 51  ALA L O   1 
ATOM   3831 C CB  . ALA C  3 51  ? -28.34500 18.36400  -16.57700 1.000 20.20956  ? 51  ALA L CB  1 
ATOM   3832 N N   . SER C  3 52  ? -26.44000 18.19400  -14.09600 1.000 17.66212  ? 52  SER L N   1 
ATOM   3833 C CA  . SER C  3 52  ? -26.02000 18.88800  -12.90100 1.000 19.94046  ? 52  SER L CA  1 
ATOM   3834 C C   . SER C  3 52  ? -25.21200 18.14000  -11.86500 1.000 19.44244  ? 52  SER L C   1 
ATOM   3835 O O   . SER C  3 52  ? -24.91000 18.68600  -10.82600 1.000 22.17412  ? 52  SER L O   1 
ATOM   3836 C CB  . SER C  3 52  ? -27.33500 19.29300  -12.24400 1.000 23.60624  ? 52  SER L CB  1 
ATOM   3837 O OG  . SER C  3 52  ? -28.11600 18.17500  -11.90000 1.000 25.50783  ? 52  SER L OG  1 
ATOM   3838 N N   . ASN C  3 53  ? -24.87700 16.89800  -12.12300 1.000 18.49528  ? 53  ASN L N   1 
ATOM   3839 C CA  . ASN C  3 53  ? -24.24800 16.09900  -11.10400 1.000 17.88136  ? 53  ASN L CA  1 
ATOM   3840 C C   . ASN C  3 53  ? -22.70600 16.02400  -11.09900 1.000 18.76018  ? 53  ASN L C   1 
ATOM   3841 O O   . ASN C  3 53  ? -22.12400 15.45000  -12.00100 1.000 21.37800  ? 53  ASN L O   1 
ATOM   3842 C CB  . ASN C  3 53  ? -24.87400 14.71300  -11.18500 1.000 19.02174  ? 53  ASN L CB  1 
ATOM   3843 C CG  . ASN C  3 53  ? -26.38000 14.74100  -10.99400 1.000 22.31665  ? 53  ASN L CG  1 
ATOM   3844 O OD1 . ASN C  3 53  ? -26.87200 14.95500  -9.89500  1.000 23.28555  ? 53  ASN L OD1 1 
ATOM   3845 N ND2 . ASN C  3 53  ? -27.11000 14.52700  -12.06900 1.000 16.58631  ? 53  ASN L ND2 1 
ATOM   3846 N N   . LEU C  3 54  ? -22.07400 16.57300  -10.05700 1.000 21.82446  ? 54  LEU L N   1 
ATOM   3847 C CA  . LEU C  3 54  ? -20.61600 16.45300  -9.98400  1.000 25.37482  ? 54  LEU L CA  1 
ATOM   3848 C C   . LEU C  3 54  ? -20.15800 15.01400  -9.84700  1.000 26.20934  ? 54  LEU L C   1 
ATOM   3849 O O   . LEU C  3 54  ? -20.66200 14.29100  -9.00000  1.000 19.45016  ? 54  LEU L O   1 
ATOM   3850 C CB  . LEU C  3 54  ? -19.96800 17.15900  -8.79100  1.000 22.40400  ? 54  LEU L CB  1 
ATOM   3851 C CG  . LEU C  3 54  ? -19.22400 18.43300  -8.96600  1.000 32.55803  ? 54  LEU L CG  1 
ATOM   3852 C CD1 . LEU C  3 54  ? -18.64600 18.87200  -7.60300  1.000 26.35331  ? 54  LEU L CD1 1 
ATOM   3853 C CD2 . LEU C  3 54  ? -18.20700 18.24300  -10.03000 1.000 23.76234  ? 54  LEU L CD2 1 
ATOM   3854 N N   . GLN C  3 55  ? -19.05300 14.67500  -10.51800 1.000 17.06941  ? 55  GLN L N   1 
ATOM   3855 C CA  . GLN C  3 55  ? -18.41800 13.37500  -10.36200 1.000 16.04635  ? 55  GLN L CA  1 
ATOM   3856 C C   . GLN C  3 55  ? -17.26000 13.37400  -9.36500  1.000 24.63048  ? 55  GLN L C   1 
ATOM   3857 O O   . GLN C  3 55  ? -16.69700 14.40900  -9.01800  1.000 21.82986  ? 55  GLN L O   1 
ATOM   3858 C CB  . GLN C  3 55  ? -17.96500 12.82400  -11.73400 1.000 18.54034  ? 55  GLN L CB  1 
ATOM   3859 C CG  . GLN C  3 55  ? -19.14200 12.93400  -12.70700 1.000 16.93079  ? 55  GLN L CG  1 
ATOM   3860 C CD  . GLN C  3 55  ? -20.29700 12.03200  -12.15400 1.000 23.35757  ? 55  GLN L CD  1 
ATOM   3861 O OE1 . GLN C  3 55  ? -20.13600 10.81300  -12.02100 1.000 18.22061  ? 55  GLN L OE1 1 
ATOM   3862 N NE2 . GLN C  3 55  ? -21.41800 12.65200  -11.78900 1.000 10.28644  ? 55  GLN L NE2 1 
ATOM   3863 N N   . SER C  3 56  ? -16.92300 12.17000  -8.89000  1.000 20.15535  ? 56  SER L N   1 
ATOM   3864 C CA  . SER C  3 56  ? -15.86300 12.01400  -7.89600  1.000 21.41190  ? 56  SER L CA  1 
ATOM   3865 C C   . SER C  3 56  ? -14.53300 12.50000  -8.45500  1.000 25.15406  ? 56  SER L C   1 
ATOM   3866 O O   . SER C  3 56  ? -14.20400 12.26900  -9.62400  1.000 24.25079  ? 56  SER L O   1 
ATOM   3867 C CB  . SER C  3 56  ? -15.72300 10.54700  -7.47500  1.000 33.68722  ? 56  SER L CB  1 
ATOM   3868 O OG  . SER C  3 56  ? -16.99900 9.94100   -7.44300  1.000 46.23768  ? 56  SER L OG  1 
ATOM   3869 N N   . GLY C  3 57  ? -13.77400 13.18900  -7.60500  1.000 22.14601  ? 57  GLY L N   1 
ATOM   3870 C CA  . GLY C  3 57  ? -12.50400 13.71200  -7.99800  1.000 28.33823  ? 57  GLY L CA  1 
ATOM   3871 C C   . GLY C  3 57  ? -12.58000 15.04100  -8.70200  1.000 32.44067  ? 57  GLY L C   1 
ATOM   3872 O O   . GLY C  3 57  ? -11.52700 15.60500  -9.03800  1.000 36.80269  ? 57  GLY L O   1 
ATOM   3873 N N   . VAL C  3 58  ? -13.77200 15.57200  -8.92300  1.000 19.87680  ? 58  VAL L N   1 
ATOM   3874 C CA  . VAL C  3 58  ? -13.94800 16.81300  -9.66600  1.000 19.69031  ? 58  VAL L CA  1 
ATOM   3875 C C   . VAL C  3 58  ? -14.16600 17.95200  -8.67300  1.000 24.58148  ? 58  VAL L C   1 
ATOM   3876 O O   . VAL C  3 58  ? -15.05200 17.84400  -7.81000  1.000 23.14430  ? 58  VAL L O   1 
ATOM   3877 C CB  . VAL C  3 58  ? -15.11000 16.69200  -10.67100 1.000 18.50405  ? 58  VAL L CB  1 
ATOM   3878 C CG1 . VAL C  3 58  ? -15.22600 17.92800  -11.51200 1.000 18.55421  ? 58  VAL L CG1 1 
ATOM   3879 C CG2 . VAL C  3 58  ? -14.86900 15.49000  -11.57400 1.000 17.55074  ? 58  VAL L CG2 1 
ATOM   3880 N N   . PRO C  3 59  ? -13.37300 19.02700  -8.72900  1.000 26.34665  ? 59  PRO L N   1 
ATOM   3881 C CA  . PRO C  3 59  ? -13.49600 20.09800  -7.72600  1.000 22.88296  ? 59  PRO L CA  1 
ATOM   3882 C C   . PRO C  3 59  ? -14.86000 20.77700  -7.76000  1.000 23.14127  ? 59  PRO L C   1 
ATOM   3883 O O   . PRO C  3 59  ? -15.49000 20.87600  -8.81100  1.000 17.33050  ? 59  PRO L O   1 
ATOM   3884 C CB  . PRO C  3 59  ? -12.37400 21.07700  -8.12100  1.000 22.91782  ? 59  PRO L CB  1 
ATOM   3885 C CG  . PRO C  3 59  ? -11.31800 20.20200  -8.78400  1.000 28.67079  ? 59  PRO L CG  1 
ATOM   3886 C CD  . PRO C  3 59  ? -12.18700 19.20900  -9.59700  1.000 27.75939  ? 59  PRO L CD  1 
ATOM   3887 N N   . SER C  3 60  ? -15.27600 21.30400  -6.60400  1.000 22.94825  ? 60  SER L N   1 
ATOM   3888 C CA  . SER C  3 60  ? -16.60400 21.95900  -6.47800  1.000 26.26497  ? 60  SER L CA  1 
ATOM   3889 C C   . SER C  3 60  ? -16.71200 23.22000  -7.34400  1.000 25.41928  ? 60  SER L C   1 
ATOM   3890 O O   . SER C  3 60  ? -17.83200 23.72200  -7.48800  1.000 22.11728  ? 60  SER L O   1 
ATOM   3891 C CB  . SER C  3 60  ? -16.90500 22.30500  -5.04100  1.000 25.69557  ? 60  SER L CB  1 
ATOM   3892 O OG  . SER C  3 60  ? -15.99400 23.26000  -4.53300  1.000 49.17909  ? 60  SER L OG  1 
ATOM   3893 N N   . ARG C  3 61  ? -15.61300 23.74000  -7.86700  1.000 24.38165  ? 61  ARG L N   1 
ATOM   3894 C CA  . ARG C  3 61  ? -15.72900 24.89000  -8.77000  1.000 28.21365  ? 61  ARG L CA  1 
ATOM   3895 C C   . ARG C  3 61  ? -16.50100 24.53900  -10.05100 1.000 24.19495  ? 61  ARG L C   1 
ATOM   3896 O O   . ARG C  3 61  ? -17.07900 25.40000  -10.68000 1.000 21.09392  ? 61  ARG L O   1 
ATOM   3897 C CB  . ARG C  3 61  ? -14.36500 25.50900  -9.08700  1.000 23.79444  ? 61  ARG L CB  1 
ATOM   3898 C CG  . ARG C  3 61  ? -13.37900 24.65900  -9.85500  1.000 30.04861  ? 61  ARG L CG  1 
ATOM   3899 C CD  . ARG C  3 61  ? -12.07700 25.42500  -10.03600 1.000 22.10050  ? 61  ARG L CD  1 
ATOM   3900 N NE  . ARG C  3 61  ? -11.03000 24.62500  -10.64700 1.000 17.64540  ? 61  ARG L NE  1 
ATOM   3901 C CZ  . ARG C  3 61  ? -10.22300 23.82500  -9.97000  1.000 20.59769  ? 61  ARG L CZ  1 
ATOM   3902 N NH1 . ARG C  3 61  ? -10.35000 23.71900  -8.65800  1.000 27.66465  ? 61  ARG L NH1 1 
ATOM   3903 N NH2 . ARG C  3 61  ? -9.29400  23.13300  -10.59800 1.000 22.14890  ? 61  ARG L NH2 1 
ATOM   3904 N N   . PHE C  3 62  ? -16.50900 23.26600  -10.39300 1.000 18.00577  ? 62  PHE L N   1 
ATOM   3905 C CA  . PHE C  3 62  ? -17.20900 22.82500  -11.59000 1.000 18.88315  ? 62  PHE L CA  1 
ATOM   3906 C C   . PHE C  3 62  ? -18.68700 22.62600  -11.30800 1.000 20.51876  ? 62  PHE L C   1 
ATOM   3907 O O   . PHE C  3 62  ? -19.05100 21.93500  -10.38200 1.000 20.51844  ? 62  PHE L O   1 
ATOM   3908 C CB  . PHE C  3 62  ? -16.57300 21.56400  -12.16600 1.000 18.06824  ? 62  PHE L CB  1 
ATOM   3909 C CG  . PHE C  3 62  ? -15.23600 21.78500  -12.79100 1.000 21.05564  ? 62  PHE L CG  1 
ATOM   3910 C CD1 . PHE C  3 62  ? -14.08800 21.70600  -12.03300 1.000 20.91140  ? 62  PHE L CD1 1 
ATOM   3911 C CD2 . PHE C  3 62  ? -15.12500 22.05900  -14.13800 1.000 18.47824  ? 62  PHE L CD2 1 
ATOM   3912 C CE1 . PHE C  3 62  ? -12.85000 21.90700  -12.60700 1.000 19.18941  ? 62  PHE L CE1 1 
ATOM   3913 C CE2 . PHE C  3 62  ? -13.89400 22.25500  -14.71800 1.000 19.90999  ? 62  PHE L CE2 1 
ATOM   3914 C CZ  . PHE C  3 62  ? -12.75400 22.17700  -13.95200 1.000 18.01307  ? 62  PHE L CZ  1 
ATOM   3915 N N   . SER C  3 63  ? -19.51100 23.25500  -12.10900 1.000 24.16654  ? 63  SER L N   1 
ATOM   3916 C CA  . SER C  3 63  ? -20.94800 23.12800  -11.96000 1.000 21.99462  ? 63  SER L CA  1 
ATOM   3917 C C   . SER C  3 63  ? -21.66900 22.99800  -13.29200 1.000 25.23277  ? 63  SER L C   1 
ATOM   3918 O O   . SER C  3 63  ? -21.24200 23.55800  -14.27700 1.000 22.90102  ? 63  SER L O   1 
ATOM   3919 C CB  . SER C  3 63  ? -21.53400 24.30700  -11.18600 1.000 24.03062  ? 63  SER L CB  1 
ATOM   3920 O OG  . SER C  3 63  ? -21.57100 25.47500  -11.96400 1.000 34.70892  ? 63  SER L OG  1 
ATOM   3921 N N   . GLY C  3 64  ? -22.75900 22.24400  -13.29500 1.000 21.39730  ? 64  GLY L N   1 
ATOM   3922 C CA  . GLY C  3 64  ? -23.55300 22.05200  -14.50100 1.000 26.89106  ? 64  GLY L CA  1 
ATOM   3923 C C   . GLY C  3 64  ? -24.98800 22.42000  -14.19800 1.000 28.44083  ? 64  GLY L C   1 
ATOM   3924 O O   . GLY C  3 64  ? -25.48400 22.18100  -13.09400 1.000 23.63209  ? 64  GLY L O   1 
ATOM   3925 N N   . SER C  3 65  ? -25.64800 23.01500  -15.18400 1.000 24.07636  ? 65  SER L N   1 
ATOM   3926 C CA  . SER C  3 65  ? -26.98500 23.54800  -14.98900 1.000 25.05279  ? 65  SER L CA  1 
ATOM   3927 C C   . SER C  3 65  ? -27.75100 23.47800  -16.30000 1.000 34.74427  ? 65  SER L C   1 
ATOM   3928 O O   . SER C  3 65  ? -27.16200 23.33100  -17.37700 1.000 29.04511  ? 65  SER L O   1 
ATOM   3929 C CB  . SER C  3 65  ? -26.90600 24.98900  -14.48500 1.000 34.58446  ? 65  SER L CB  1 
ATOM   3930 O OG  . SER C  3 65  ? -28.14800 25.63400  -14.60100 1.000 44.16197  ? 65  SER L OG  1 
ATOM   3931 N N   . GLY C  3 66  ? -29.07700 23.57200  -16.21400 1.000 30.35290  ? 66  GLY L N   1 
ATOM   3932 C CA  . GLY C  3 66  ? -29.90500 23.61900  -17.42700 1.000 29.55108  ? 66  GLY L CA  1 
ATOM   3933 C C   . GLY C  3 66  ? -30.68900 22.35200  -17.68600 1.000 36.55654  ? 66  GLY L C   1 
ATOM   3934 O O   . GLY C  3 66  ? -30.42400 21.35500  -17.02100 1.000 32.32332  ? 66  GLY L O   1 
ATOM   3935 N N   . SER C  3 67  ? -31.61500 22.40800  -18.63400 1.000 34.51938  ? 67  SER L N   1 
ATOM   3936 C CA  . SER C  3 67  ? -32.41900 21.23100  -19.02400 1.000 44.89694  ? 67  SER L CA  1 
ATOM   3937 C C   . SER C  3 67  ? -33.08300 21.50200  -20.37300 1.000 36.91947  ? 67  SER L C   1 
ATOM   3938 O O   . SER C  3 67  ? -33.17100 22.67400  -20.76000 1.000 38.67819  ? 67  SER L O   1 
ATOM   3939 C CB  . SER C  3 67  ? -33.47400 20.93800  -18.00100 1.000 44.42962  ? 67  SER L CB  1 
ATOM   3940 O OG  . SER C  3 67  ? -34.40700 21.99900  -17.93900 1.000 49.54983  ? 67  SER L OG  1 
ATOM   3941 N N   . GLY C  3 68  ? -33.50000 20.45300  -21.06000 1.000 36.90975  ? 68  GLY L N   1 
ATOM   3942 C CA  . GLY C  3 68  ? -34.27000 20.64400  -22.30300 1.000 33.85241  ? 68  GLY L CA  1 
ATOM   3943 C C   . GLY C  3 68  ? -33.44700 21.08300  -23.49200 1.000 35.92806  ? 68  GLY L C   1 
ATOM   3944 O O   . GLY C  3 68  ? -32.84300 20.22500  -24.11700 1.000 34.33797  ? 68  GLY L O   1 
ATOM   3945 N N   . THR C  3 69  ? -33.51400 22.37800  -23.82800 1.000 36.89472  ? 69  THR L N   1 
ATOM   3946 C CA  . THR C  3 69  ? -32.68300 22.90800  -24.93500 1.000 40.36598  ? 69  THR L CA  1 
ATOM   3947 C C   . THR C  3 69  ? -31.55000 23.89100  -24.61900 1.000 41.12335  ? 69  THR L C   1 
ATOM   3948 O O   . THR C  3 69  ? -31.01300 24.46300  -25.55200 1.000 35.55319  ? 69  THR L O   1 
ATOM   3949 C CB  . THR C  3 69  ? -33.74300 23.53600  -25.84900 1.000 44.89500  ? 69  THR L CB  1 
ATOM   3950 O OG1 . THR C  3 69  ? -34.04600 24.84700  -25.37200 1.000 48.25870  ? 69  THR L OG1 1 
ATOM   3951 C CG2 . THR C  3 69  ? -35.00600 22.70700  -25.93800 1.000 42.56095  ? 69  THR L CG2 1 
ATOM   3952 N N   . GLU C  3 70  ? -31.20000 24.01600  -23.33100 1.000 34.07848  ? 70  GLU L N   1 
ATOM   3953 C CA  . GLU C  3 70  ? -30.09800 24.92200  -22.93200 1.000 37.04208  ? 70  GLU L CA  1 
ATOM   3954 C C   . GLU C  3 70  ? -29.34600 24.35000  -21.74000 1.000 34.42821  ? 70  GLU L C   1 
ATOM   3955 O O   . GLU C  3 70  ? -29.97900 24.07800  -20.72700 1.000 32.49273  ? 70  GLU L O   1 
ATOM   3956 C CB  . GLU C  3 70  ? -30.60200 26.32300  -22.59100 1.000 44.78708  ? 70  GLU L CB  1 
ATOM   3957 C CG  . GLU C  3 70  ? -29.50300 27.26800  -22.14600 1.000 53.87365  ? 70  GLU L CG  1 
ATOM   3958 C CD  . GLU C  3 70  ? -29.88700 28.73400  -22.22300 1.000 71.54439  ? 70  GLU L CD  1 
ATOM   3959 O OE1 . GLU C  3 70  ? -30.76600 29.15400  -21.44800 1.000 82.45322  ? 70  GLU L OE1 1 
ATOM   3960 O OE2 . GLU C  3 70  ? -29.32200 29.44700  -23.06900 1.000 72.04409  ? 70  GLU L OE2 1 
ATOM   3961 N N   . PHE C  3 71  ? -28.01700 24.27300  -21.88000 1.000 28.83678  ? 71  PHE L N   1 
ATOM   3962 C CA  . PHE C  3 71  ? -27.18300 23.73200  -20.79000 1.000 26.07426  ? 71  PHE L CA  1 
ATOM   3963 C C   . PHE C  3 71  ? -25.94300 24.60500  -20.59700 1.000 21.07449  ? 71  PHE L C   1 
ATOM   3964 O O   . PHE C  3 71  ? -25.46600 25.18500  -21.56100 1.000 27.43845  ? 71  PHE L O   1 
ATOM   3965 C CB  . PHE C  3 71  ? -26.85000 22.26800  -21.05900 1.000 20.99053  ? 71  PHE L CB  1 
ATOM   3966 C CG  . PHE C  3 71  ? -28.05300 21.38800  -21.27400 1.000 29.24288  ? 71  PHE L CG  1 
ATOM   3967 C CD1 . PHE C  3 71  ? -28.68300 21.33700  -22.50600 1.000 27.58646  ? 71  PHE L CD1 1 
ATOM   3968 C CD2 . PHE C  3 71  ? -28.56000 20.61700  -20.24200 1.000 26.33940  ? 71  PHE L CD2 1 
ATOM   3969 C CE1 . PHE C  3 71  ? -29.79200 20.53300  -22.70300 1.000 31.31061  ? 71  PHE L CE1 1 
ATOM   3970 C CE2 . PHE C  3 71  ? -29.66700 19.81000  -20.44300 1.000 34.95872  ? 71  PHE L CE2 1 
ATOM   3971 C CZ  . PHE C  3 71  ? -30.28200 19.77000  -21.67100 1.000 29.00540  ? 71  PHE L CZ  1 
ATOM   3972 N N   . THR C  3 72  ? -25.47800 24.71600  -19.37600 1.000 22.87164  ? 72  THR L N   1 
ATOM   3973 C CA  . THR C  3 72  ? -24.31700 25.50900  -19.08600 1.000 20.63897  ? 72  THR L CA  1 
ATOM   3974 C C   . THR C  3 72  ? -23.32800 24.83700  -18.14700 1.000 26.14059  ? 72  THR L C   1 
ATOM   3975 O O   . THR C  3 72  ? -23.71300 24.33200  -17.10900 1.000 27.13704  ? 72  THR L O   1 
ATOM   3976 C CB  . THR C  3 72  ? -24.74200 26.87200  -18.50600 1.000 23.38011  ? 72  THR L CB  1 
ATOM   3977 O OG1 . THR C  3 72  ? -25.50000 27.59300  -19.47900 1.000 35.22303  ? 72  THR L OG1 1 
ATOM   3978 C CG2 . THR C  3 72  ? -23.53200 27.67800  -18.11800 1.000 27.92152  ? 72  THR L CG2 1 
ATOM   3979 N N   . LEU C  3 73  ? -22.08100 24.75900  -18.54900 1.000 17.77170  ? 73  LEU L N   1 
ATOM   3980 C CA  . LEU C  3 73  ? -21.05600 24.28100  -17.65600 1.000 18.60856  ? 73  LEU L CA  1 
ATOM   3981 C C   . LEU C  3 73  ? -20.43100 25.53500  -17.10600 1.000 21.58575  ? 73  LEU L C   1 
ATOM   3982 O O   . LEU C  3 73  ? -20.06900 26.42700  -17.85300 1.000 21.12723  ? 73  LEU L O   1 
ATOM   3983 C CB  . LEU C  3 73  ? -19.99000 23.43700  -18.34600 1.000 16.22031  ? 73  LEU L CB  1 
ATOM   3984 C CG  . LEU C  3 73  ? -18.74100 23.03700  -17.57300 1.000 16.48924  ? 73  LEU L CG  1 
ATOM   3985 C CD1 . LEU C  3 73  ? -19.07700 22.01800  -16.50200 1.000 17.76934  ? 73  LEU L CD1 1 
ATOM   3986 C CD2 . LEU C  3 73  ? -17.70300 22.47700  -18.52700 1.000 21.86864  ? 73  LEU L CD2 1 
ATOM   3987 N N   . THR C  3 74  ? -20.30100 25.60400  -15.80800 1.000 21.61023  ? 74  THR L N   1 
ATOM   3988 C CA  . THR C  3 74  ? -19.64600 26.73600  -15.19900 1.000 16.10019  ? 74  THR L CA  1 
ATOM   3989 C C   . THR C  3 74  ? -18.39200 26.32100  -14.43200 1.000 20.36354  ? 74  THR L C   1 
ATOM   3990 O O   . THR C  3 74  ? -18.41500 25.35000  -13.71000 1.000 22.47581  ? 74  THR L O   1 
ATOM   3991 C CB  . THR C  3 74  ? -20.63100 27.56900  -14.31000 1.000 22.13364  ? 74  THR L CB  1 
ATOM   3992 O OG1 . THR C  3 74  ? -21.75400 28.00300  -15.07500 1.000 22.59081  ? 74  THR L OG1 1 
ATOM   3993 C CG2 . THR C  3 74  ? -19.93200 28.77300  -13.71300 1.000 19.45357  ? 74  THR L CG2 1 
ATOM   3994 N N   . ILE C  3 75  ? -17.29200 27.04000  -14.63100 1.000 20.20505  ? 75  ILE L N   1 
ATOM   3995 C CA  . ILE C  3 75  ? -16.06400 26.81300  -13.88200 1.000 16.92941  ? 75  ILE L CA  1 
ATOM   3996 C C   . ILE C  3 75  ? -15.86500 28.12300  -13.15300 1.000 21.46334  ? 75  ILE L C   1 
ATOM   3997 O O   . ILE C  3 75  ? -15.50700 29.11400  -13.75800 1.000 20.94613  ? 75  ILE L O   1 
ATOM   3998 C CB  . ILE C  3 75  ? -14.87100 26.44200  -14.75600 1.000 20.31532  ? 75  ILE L CB  1 
ATOM   3999 C CG1 . ILE C  3 75  ? -15.27200 25.42700  -15.82600 1.000 20.06956  ? 75  ILE L CG1 1 
ATOM   4000 C CG2 . ILE C  3 75  ? -13.73700 25.91300  -13.89500 1.000 19.20136  ? 75  ILE L CG2 1 
ATOM   4001 C CD1 . ILE C  3 75  ? -14.26500 25.31700  -16.94600 1.000 23.56997  ? 75  ILE L CD1 1 
ATOM   4002 N N   . ARG C  3 76  ? -16.06900 28.11900  -11.85800 1.000 17.55782  ? 76  ARG L N   1 
ATOM   4003 C CA  . ARG C  3 76  ? -16.07400 29.36800  -11.11000 1.000 25.07482  ? 76  ARG L CA  1 
ATOM   4004 C C   . ARG C  3 76  ? -14.76800 30.12900  -10.80100 1.000 34.17466  ? 76  ARG L C   1 
ATOM   4005 O O   . ARG C  3 76  ? -14.79700 31.34200  -10.71800 1.000 42.48155  ? 76  ARG L O   1 
ATOM   4006 C CB  . ARG C  3 76  ? -16.90500 29.18600  -9.81300  1.000 28.95908  ? 76  ARG L CB  1 
ATOM   4007 C CG  . ARG C  3 76  ? -16.44300 28.09900  -8.88100  1.000 46.20747  ? 76  ARG L CG  1 
ATOM   4008 C CD  . ARG C  3 76  ? -17.33600 28.01600  -7.64600  1.000 59.22245  ? 76  ARG L CD  1 
ATOM   4009 N NE  . ARG C  3 76  ? -16.97300 26.86700  -6.81700  1.000 63.44715  ? 76  ARG L NE  1 
ATOM   4010 C CZ  . ARG C  3 76  ? -17.04800 26.83800  -5.49400  1.000 59.55500  ? 76  ARG L CZ  1 
ATOM   4011 N NH1 . ARG C  3 76  ? -17.47700 27.90300  -4.83300  1.000 67.45882  ? 76  ARG L NH1 1 
ATOM   4012 N NH2 . ARG C  3 76  ? -16.69000 25.74600  -4.83200  1.000 47.37010  ? 76  ARG L NH2 1 
ATOM   4013 N N   . SER C  3 77  ? -13.67100 29.45500  -10.60600 1.000 24.87731  ? 77  SER L N   1 
ATOM   4014 C CA  . SER C  3 77  ? -12.43400 30.13900  -10.22200 1.000 18.08735  ? 77  SER L CA  1 
ATOM   4015 C C   . SER C  3 77  ? -11.39900 29.41300  -11.03700 1.000 21.46699  ? 77  SER L C   1 
ATOM   4016 O O   . SER C  3 77  ? -10.72500 28.53900  -10.54400 1.000 27.21648  ? 77  SER L O   1 
ATOM   4017 C CB  . SER C  3 77  ? -12.16500 30.06700  -8.72100  1.000 23.73728  ? 77  SER L CB  1 
ATOM   4018 O OG  . SER C  3 77  ? -10.82300 30.34400  -8.41100  1.000 34.59882  ? 77  SER L OG  1 
ATOM   4019 N N   . LEU C  3 78  ? -11.30000 29.77400  -12.29400 1.000 19.84017  ? 78  LEU L N   1 
ATOM   4020 C CA  . LEU C  3 78  ? -10.44100 29.04600  -13.19600 1.000 18.43186  ? 78  LEU L CA  1 
ATOM   4021 C C   . LEU C  3 78  ? -9.03500  28.81000  -12.66100 1.000 21.55672  ? 78  LEU L C   1 
ATOM   4022 O O   . LEU C  3 78  ? -8.38000  29.72600  -12.18200 1.000 18.48856  ? 78  LEU L O   1 
ATOM   4023 C CB  . LEU C  3 78  ? -10.41700 29.77200  -14.52400 1.000 15.41837  ? 78  LEU L CB  1 
ATOM   4024 C CG  . LEU C  3 78  ? -9.98100  29.09000  -15.82500 1.000 28.42864  ? 78  LEU L CG  1 
ATOM   4025 C CD1 . LEU C  3 78  ? -9.99200  30.10100  -16.95300 1.000 21.69765  ? 78  LEU L CD1 1 
ATOM   4026 C CD2 . LEU C  3 78  ? -8.59500  28.49400  -15.70500 1.000 28.28433  ? 78  LEU L CD2 1 
ATOM   4027 N N   . GLN C  3 79  ? -8.58900  27.58300  -12.77100 1.000 15.19850  ? 79  GLN L N   1 
ATOM   4028 C CA  . GLN C  3 79  ? -7.25200  27.23500  -12.31800 1.000 19.15778  ? 79  GLN L CA  1 
ATOM   4029 C C   . GLN C  3 79  ? -6.41600  26.72800  -13.49200 1.000 20.44235  ? 79  GLN L C   1 
ATOM   4030 O O   . GLN C  3 79  ? -6.95800  26.34400  -14.50200 1.000 20.75475  ? 79  GLN L O   1 
ATOM   4031 C CB  . GLN C  3 79  ? -7.29200  26.23200  -11.16900 1.000 19.78904  ? 79  GLN L CB  1 
ATOM   4032 C CG  . GLN C  3 79  ? -8.09800  26.69100  -9.97900  1.000 23.34061  ? 79  GLN L CG  1 
ATOM   4033 C CD  . GLN C  3 79  ? -7.47100  27.90100  -9.32900  1.000 25.80711  ? 79  GLN L CD  1 
ATOM   4034 O OE1 . GLN C  3 79  ? -6.31000  27.86900  -8.93700  1.000 23.77153  ? 79  GLN L OE1 1 
ATOM   4035 N NE2 . GLN C  3 79  ? -8.22400  28.97700  -9.24000  1.000 17.80917  ? 79  GLN L NE2 1 
ATOM   4036 N N   . PRO C  3 80  ? -5.09000  26.69700  -13.31900 1.000 19.90363  ? 80  PRO L N   1 
ATOM   4037 C CA  . PRO C  3 80  ? -4.25100  26.37400  -14.49100 1.000 23.42312  ? 80  PRO L CA  1 
ATOM   4038 C C   . PRO C  3 80  ? -4.50000  24.97200  -15.03100 1.000 23.91908  ? 80  PRO L C   1 
ATOM   4039 O O   . PRO C  3 80  ? -4.51200  24.78100  -16.25200 1.000 16.06322  ? 80  PRO L O   1 
ATOM   4040 C CB  . PRO C  3 80  ? -2.82000  26.50900  -13.94500 1.000 26.18647  ? 80  PRO L CB  1 
ATOM   4041 C CG  . PRO C  3 80  ? -2.94900  27.60100  -12.88700 1.000 18.80242  ? 80  PRO L CG  1 
ATOM   4042 C CD  . PRO C  3 80  ? -4.28300  27.26300  -12.21300 1.000 15.87747  ? 80  PRO L CD  1 
ATOM   4043 N N   . GLU C  3 81  ? -4.81100  24.04100  -14.14900 1.000 14.99127  ? 81  GLU L N   1 
ATOM   4044 C CA  . GLU C  3 81  ? -5.12600  22.68000  -14.53400 1.000 19.15222  ? 81  GLU L CA  1 
ATOM   4045 C C   . GLU C  3 81  ? -6.43000  22.51800  -15.31600 1.000 18.31170  ? 81  GLU L C   1 
ATOM   4046 O O   . GLU C  3 81  ? -6.71100  21.45600  -15.77500 1.000 20.83782  ? 81  GLU L O   1 
ATOM   4047 C CB  . GLU C  3 81  ? -5.24300  21.80200  -13.28500 1.000 18.01515  ? 81  GLU L CB  1 
ATOM   4048 C CG  . GLU C  3 81  ? -6.17000  22.34200  -12.22800 1.000 21.17710  ? 81  GLU L CG  1 
ATOM   4049 C CD  . GLU C  3 81  ? -5.42300  23.10300  -11.15300 1.000 24.05319  ? 81  GLU L CD  1 
ATOM   4050 O OE1 . GLU C  3 81  ? -4.71600  24.06600  -11.47800 1.000 21.04418  ? 81  GLU L OE1 1 
ATOM   4051 O OE2 . GLU C  3 81  ? -5.54400  22.72600  -9.98300  1.000 28.51366  ? 81  GLU L OE2 1 
ATOM   4052 N N   . ASP C  3 82  ? -7.22300  23.56300  -15.39000 1.000 19.19226  ? 82  ASP L N   1 
ATOM   4053 C CA  . ASP C  3 82  ? -8.49200  23.51200  -16.08800 1.000 16.83058  ? 82  ASP L CA  1 
ATOM   4054 C C   . ASP C  3 82  ? -8.27500  23.74000  -17.58300 1.000 20.88647  ? 82  ASP L C   1 
ATOM   4055 O O   . ASP C  3 82  ? -9.22700  23.71700  -18.33500 1.000 19.51786  ? 82  ASP L O   1 
ATOM   4056 C CB  . ASP C  3 82  ? -9.45500  24.50100  -15.47600 1.000 16.60272  ? 82  ASP L CB  1 
ATOM   4057 C CG  . ASP C  3 82  ? -9.66300  24.28200  -13.97700 1.000 21.68050  ? 82  ASP L CG  1 
ATOM   4058 O OD1 . ASP C  3 82  ? -9.38900  23.18400  -13.46200 1.000 18.21875  ? 82  ASP L OD1 1 
ATOM   4059 O OD2 . ASP C  3 82  ? -10.10500 25.22500  -13.30900 1.000 23.22474  ? 82  ASP L OD2 1 
ATOM   4060 N N   . PHE C  3 83  ? -7.03600  24.00600  -17.98600 1.000 18.52919  ? 83  PHE L N   1 
ATOM   4061 C CA  . PHE C  3 83  ? -6.66600  24.12100  -19.38900 1.000 19.96694  ? 83  PHE L CA  1 
ATOM   4062 C C   . PHE C  3 83  ? -7.05600  22.84000  -20.06300 1.000 17.28510  ? 83  PHE L C   1 
ATOM   4063 O O   . PHE C  3 83  ? -6.56100  21.79600  -19.71500 1.000 27.53019  ? 83  PHE L O   1 
ATOM   4064 C CB  . PHE C  3 83  ? -5.15100  24.34600  -19.46300 1.000 31.19277  ? 83  PHE L CB  1 
ATOM   4065 C CG  . PHE C  3 83  ? -4.59000  24.51800  -20.82900 1.000 40.05411  ? 83  PHE L CG  1 
ATOM   4066 C CD1 . PHE C  3 83  ? -4.62200  25.74600  -21.45900 1.000 38.67461  ? 83  PHE L CD1 1 
ATOM   4067 C CD2 . PHE C  3 83  ? -3.93300  23.47500  -21.44100 1.000 40.76736  ? 83  PHE L CD2 1 
ATOM   4068 C CE1 . PHE C  3 83  ? -4.06300  25.90800  -22.70300 1.000 32.73123  ? 83  PHE L CE1 1 
ATOM   4069 C CE2 . PHE C  3 83  ? -3.37200  23.63200  -22.68500 1.000 35.97695  ? 83  PHE L CE2 1 
ATOM   4070 C CZ  . PHE C  3 83  ? -3.44200  24.84800  -23.31600 1.000 32.48310  ? 83  PHE L CZ  1 
ATOM   4071 N N   . ALA C  3 84  ? -7.97500  22.92300  -20.99600 1.000 18.23085  ? 84  ALA L N   1 
ATOM   4072 C CA  . ALA C  3 84  ? -8.46500  21.75400  -21.67500 1.000 16.84846  ? 84  ALA L CA  1 
ATOM   4073 C C   . ALA C  3 84  ? -9.53300  22.06700  -22.69500 1.000 18.98008  ? 84  ALA L C   1 
ATOM   4074 O O   . ALA C  3 84  ? -9.93100  23.20500  -22.84600 1.000 21.94742  ? 84  ALA L O   1 
ATOM   4075 C CB  . ALA C  3 84  ? -9.03700  20.81000  -20.65300 1.000 19.13660  ? 84  ALA L CB  1 
ATOM   4076 N N   . THR C  3 85  ? -9.97600  21.05900  -23.41700 1.000 14.50668  ? 85  THR L N   1 
ATOM   4077 C CA  . THR C  3 85  ? -11.08300 21.25000  -24.29900 1.000 13.36506  ? 85  THR L CA  1 
ATOM   4078 C C   . THR C  3 85  ? -12.28700 20.56100  -23.64500 1.000 17.77055  ? 85  THR L C   1 
ATOM   4079 O O   . THR C  3 85  ? -12.17400 19.44400  -23.17900 1.000 22.51193  ? 85  THR L O   1 
ATOM   4080 C CB  . THR C  3 85  ? -10.78900 20.78100  -25.73300 1.000 21.38564  ? 85  THR L CB  1 
ATOM   4081 O OG1 . THR C  3 85  ? -9.76500  21.58800  -26.31500 1.000 20.18578  ? 85  THR L OG1 1 
ATOM   4082 C CG2 . THR C  3 85  ? -12.05300 20.86300  -26.58500 1.000 20.27537  ? 85  THR L CG2 1 
ATOM   4083 N N   . TYR C  3 86  ? -13.39800 21.23800  -23.59300 1.000 13.54765  ? 86  TYR L N   1 
ATOM   4084 C CA  . TYR C  3 86  ? -14.60000 20.71500  -22.95900 1.000 13.18220  ? 86  TYR L CA  1 
ATOM   4085 C C   . TYR C  3 86  ? -15.68100 20.33400  -23.97900 1.000 21.26756  ? 86  TYR L C   1 
ATOM   4086 O O   . TYR C  3 86  ? -15.87800 21.03000  -24.95400 1.000 19.50259  ? 86  TYR L O   1 
ATOM   4087 C CB  . TYR C  3 86  ? -15.11700 21.70300  -21.91000 1.000 12.66269  ? 86  TYR L CB  1 
ATOM   4088 C CG  . TYR C  3 86  ? -14.15700 21.94700  -20.77500 1.000 17.03569  ? 86  TYR L CG  1 
ATOM   4089 C CD1 . TYR C  3 86  ? -13.13400 22.86800  -20.89300 1.000 13.35152  ? 86  TYR L CD1 1 
ATOM   4090 C CD2 . TYR C  3 86  ? -14.26900 21.24900  -19.58900 1.000 15.23149  ? 86  TYR L CD2 1 
ATOM   4091 C CE1 . TYR C  3 86  ? -12.24900 23.08900  -19.85800 1.000 16.78781  ? 86  TYR L CE1 1 
ATOM   4092 C CE2 . TYR C  3 86  ? -13.39200 21.46100  -18.55100 1.000 17.43169  ? 86  TYR L CE2 1 
ATOM   4093 C CZ  . TYR C  3 86  ? -12.37900 22.38200  -18.68900 1.000 15.85656  ? 86  TYR L CZ  1 
ATOM   4094 O OH  . TYR C  3 86  ? -11.51200 22.59300  -17.65400 1.000 13.80912  ? 86  TYR L OH  1 
ATOM   4095 N N   . TYR C  3 87  ? -16.35400 19.22800  -23.73800 1.000 12.23578  ? 87  TYR L N   1 
ATOM   4096 C CA  . TYR C  3 87  ? -17.38000 18.75000  -24.63700 1.000 16.42287  ? 87  TYR L CA  1 
ATOM   4097 C C   . TYR C  3 87  ? -18.69700 18.37900  -23.95500 1.000 18.67382  ? 87  TYR L C   1 
ATOM   4098 O O   . TYR C  3 87  ? -18.69100 17.74400  -22.92100 1.000 22.19368  ? 87  TYR L O   1 
ATOM   4099 C CB  . TYR C  3 87  ? -16.89700 17.48400  -25.37300 1.000 15.93621  ? 87  TYR L CB  1 
ATOM   4100 C CG  . TYR C  3 87  ? -15.72100 17.56500  -26.28900 1.000 14.90384  ? 87  TYR L CG  1 
ATOM   4101 C CD1 . TYR C  3 87  ? -14.45100 17.30200  -25.82700 1.000 15.87890  ? 87  TYR L CD1 1 
ATOM   4102 C CD2 . TYR C  3 87  ? -15.89000 17.81600  -27.63800 1.000 20.35506  ? 87  TYR L CD2 1 
ATOM   4103 C CE1 . TYR C  3 87  ? -13.36700 17.34800  -26.66800 1.000 19.23241  ? 87  TYR L CE1 1 
ATOM   4104 C CE2 . TYR C  3 87  ? -14.81100 17.85800  -28.49100 1.000 20.82982  ? 87  TYR L CE2 1 
ATOM   4105 C CZ  . TYR C  3 87  ? -13.55100 17.62500  -27.99500 1.000 23.84742  ? 87  TYR L CZ  1 
ATOM   4106 O OH  . TYR C  3 87  ? -12.47200 17.66100  -28.82200 1.000 21.62698  ? 87  TYR L OH  1 
ATOM   4107 N N   . CYS C  3 88  ? -19.81100 18.79600  -24.51800 1.000 15.80118  ? 88  CYS L N   1 
ATOM   4108 C CA  . CYS C  3 88  ? -21.08900 18.34700  -24.01500 1.000 16.59622  ? 88  CYS L CA  1 
ATOM   4109 C C   . CYS C  3 88  ? -21.48500 17.11700  -24.81000 1.000 22.51075  ? 88  CYS L C   1 
ATOM   4110 O O   . CYS C  3 88  ? -21.05600 16.95800  -25.93500 1.000 21.42006  ? 88  CYS L O   1 
ATOM   4111 C CB  . CYS C  3 88  ? -22.17300 19.39500  -24.11800 1.000 18.76230  ? 88  CYS L CB  1 
ATOM   4112 S SG  . CYS C  3 88  ? -22.55000 20.07900  -25.72900 1.000 24.28729  ? 88  CYS L SG  1 
ATOM   4113 N N   . GLN C  3 89  ? -22.25300 16.23600  -24.20100 1.000 17.82459  ? 89  GLN L N   1 
ATOM   4114 C CA  . GLN C  3 89  ? -22.70500 15.01900  -24.85400 1.000 17.40745  ? 89  GLN L CA  1 
ATOM   4115 C C   . GLN C  3 89  ? -24.14700 14.66200  -24.51300 1.000 25.21066  ? 89  GLN L C   1 
ATOM   4116 O O   . GLN C  3 89  ? -24.50600 14.57500  -23.36500 1.000 20.56799  ? 89  GLN L O   1 
ATOM   4117 C CB  . GLN C  3 89  ? -21.79900 13.82700  -24.56100 1.000 18.08614  ? 89  GLN L CB  1 
ATOM   4118 C CG  . GLN C  3 89  ? -22.24500 12.51500  -25.18100 1.000 19.84380  ? 89  GLN L CG  1 
ATOM   4119 C CD  . GLN C  3 89  ? -22.61600 11.46500  -24.14900 1.000 24.69762  ? 89  GLN L CD  1 
ATOM   4120 O OE1 . GLN C  3 89  ? -22.00900 11.38000  -23.09100 1.000 29.22115  ? 89  GLN L OE1 1 
ATOM   4121 N NE2 . GLN C  3 89  ? -23.61900 10.66400  -24.46000 1.000 19.75474  ? 89  GLN L NE2 1 
ATOM   4122 N N   . GLN C  3 90  ? -24.94000 14.47800  -25.54800 1.000 20.90153  ? 90  GLN L N   1 
ATOM   4123 C CA  . GLN C  3 90  ? -26.31100 14.10600  -25.36600 1.000 23.08619  ? 90  GLN L CA  1 
ATOM   4124 C C   . GLN C  3 90  ? -26.43800 12.58400  -25.30400 1.000 24.96373  ? 90  GLN L C   1 
ATOM   4125 O O   . GLN C  3 90  ? -25.79800 11.87600  -26.04300 1.000 25.16699  ? 90  GLN L O   1 
ATOM   4126 C CB  . GLN C  3 90  ? -27.16100 14.67800  -26.47500 1.000 22.87115  ? 90  GLN L CB  1 
ATOM   4127 C CG  . GLN C  3 90  ? -26.96400 14.05500  -27.83700 1.000 26.98908  ? 90  GLN L CG  1 
ATOM   4128 C CD  . GLN C  3 90  ? -27.83400 12.83500  -28.06600 1.000 32.24363  ? 90  GLN L CD  1 
ATOM   4129 O OE1 . GLN C  3 90  ? -28.75400 12.56300  -27.30300 1.000 30.30719  ? 90  GLN L OE1 1 
ATOM   4130 N NE2 . GLN C  3 90  ? -27.53300 12.09100  -29.11300 1.000 22.24087  ? 90  GLN L NE2 1 
ATOM   4131 N N   . SER C  3 91  ? -27.25300 12.11200  -24.39800 1.000 25.83096  ? 91  SER L N   1 
ATOM   4132 C CA  . SER C  3 91  ? -27.49900 10.67100  -24.22100 1.000 26.71034  ? 91  SER L CA  1 
ATOM   4133 C C   . SER C  3 91  ? -28.97400 10.31800  -24.40000 1.000 28.60341  ? 91  SER L C   1 
ATOM   4134 O O   . SER C  3 91  ? -29.44400 9.34200   -23.80800 1.000 30.45264  ? 91  SER L O   1 
ATOM   4135 C CB  . SER C  3 91  ? -27.06500 10.18600  -22.84300 1.000 21.67451  ? 91  SER L CB  1 
ATOM   4136 O OG  . SER C  3 91  ? -27.78400 10.90600  -21.87800 1.000 22.95908  ? 91  SER L OG  1 
ATOM   4137 N N   . TYR C  3 92  ? -29.71200 11.12700  -25.12800 1.000 23.65123  ? 92  TYR L N   1 
ATOM   4138 C CA  . TYR C  3 92  ? -31.14400 10.96000  -25.29400 1.000 35.06756  ? 92  TYR L CA  1 
ATOM   4139 C C   . TYR C  3 92  ? -31.57400 10.10300  -26.48800 1.000 34.79633  ? 92  TYR L C   1 
ATOM   4140 O O   . TYR C  3 92  ? -32.50300 9.33800   -26.35900 1.000 35.77484  ? 92  TYR L O   1 
ATOM   4141 C CB  . TYR C  3 92  ? -31.73900 12.35200  -25.40600 1.000 33.47643  ? 92  TYR L CB  1 
ATOM   4142 C CG  . TYR C  3 92  ? -33.23200 12.48400  -25.43100 1.000 39.31457  ? 92  TYR L CG  1 
ATOM   4143 C CD1 . TYR C  3 92  ? -33.96100 12.49600  -24.26000 1.000 40.59133  ? 92  TYR L CD1 1 
ATOM   4144 C CD2 . TYR C  3 92  ? -33.90800 12.66700  -26.62300 1.000 39.87372  ? 92  TYR L CD2 1 
ATOM   4145 C CE1 . TYR C  3 92  ? -35.32500 12.64700  -24.27200 1.000 39.47463  ? 92  TYR L CE1 1 
ATOM   4146 C CE2 . TYR C  3 92  ? -35.27700 12.81600  -26.64400 1.000 45.34033  ? 92  TYR L CE2 1 
ATOM   4147 C CZ  . TYR C  3 92  ? -35.97700 12.80300  -25.46200 1.000 43.77678  ? 92  TYR L CZ  1 
ATOM   4148 O OH  . TYR C  3 92  ? -37.33700 12.95200  -25.46200 1.000 54.92709  ? 92  TYR L OH  1 
ATOM   4149 N N   . ASN C  3 93  ? -30.91600 10.24800  -27.62800 1.000 29.14723  ? 93  ASN L N   1 
ATOM   4150 C CA  . ASN C  3 93  ? -31.21000 9.42600   -28.80600 1.000 38.44193  ? 93  ASN L CA  1 
ATOM   4151 C C   . ASN C  3 93  ? -30.06100 8.48300   -29.19200 1.000 42.19079  ? 93  ASN L C   1 
ATOM   4152 O O   . ASN C  3 93  ? -28.90400 8.84000   -29.01800 1.000 39.79937  ? 93  ASN L O   1 
ATOM   4153 C CB  . ASN C  3 93  ? -31.62200 10.30200  -29.96700 1.000 45.27650  ? 93  ASN L CB  1 
ATOM   4154 C CG  . ASN C  3 93  ? -33.10800 10.60000  -29.97900 1.000 52.95836  ? 93  ASN L CG  1 
ATOM   4155 O OD1 . ASN C  3 93  ? -33.81200 10.34900  -29.00900 1.000 54.77925  ? 93  ASN L OD1 1 
ATOM   4156 N ND2 . ASN C  3 93  ? -33.59000 11.14200  -31.08500 1.000 53.63848  ? 93  ASN L ND2 1 
ATOM   4157 N N   . THR C  3 94  ? -30.36600 7.34400   -29.79800 1.000 46.31908  ? 94  THR L N   1 
ATOM   4158 C CA  . THR C  3 94  ? -29.36600 6.27300   -30.05000 1.000 46.36128  ? 94  THR L CA  1 
ATOM   4159 C C   . THR C  3 94  ? -28.03200 6.58100   -30.61100 1.000 53.62557  ? 94  THR L C   1 
ATOM   4160 O O   . THR C  3 94  ? -27.08800 5.89800   -30.28600 1.000 64.07238  ? 94  THR L O   1 
ATOM   4161 C CB  . THR C  3 94  ? -29.90300 5.13700   -30.94900 1.000 47.48047  ? 94  THR L CB  1 
ATOM   4162 O OG1 . THR C  3 94  ? -28.96600 4.05900   -30.97000 1.000 60.36584  ? 94  THR L OG1 1 
ATOM   4163 C CG2 . THR C  3 94  ? -30.15100 5.62600   -32.37000 1.000 62.16206  ? 94  THR L CG2 1 
ATOM   4164 N N   . PRO C  3 95  ? -27.95900 7.49800   -31.54600 1.000 46.38420  ? 95  PRO L N   1 
ATOM   4165 C CA  . PRO C  3 95  ? -26.59100 7.79600   -31.91500 1.000 39.88745  ? 95  PRO L CA  1 
ATOM   4166 C C   . PRO C  3 95  ? -26.10100 8.87300   -30.91300 1.000 35.11918  ? 95  PRO L C   1 
ATOM   4167 O O   . PRO C  3 95  ? -26.43400 10.02500  -31.08800 1.000 36.10602  ? 95  PRO L O   1 
ATOM   4168 C CB  . PRO C  3 95  ? -26.71300 8.31300   -33.33300 1.000 41.26052  ? 95  PRO L CB  1 
ATOM   4169 C CG  . PRO C  3 95  ? -28.17000 8.43200   -33.63900 1.000 44.80869  ? 95  PRO L CG  1 
ATOM   4170 C CD  . PRO C  3 95  ? -28.93400 8.20700   -32.37900 1.000 44.36205  ? 95  PRO L CD  1 
ATOM   4171 N N   . PRO C  3 96  ? -25.37700 8.48400   -29.86000 1.000 29.43653  ? 96  PRO L N   1 
ATOM   4172 C CA  . PRO C  3 96  ? -24.86100 9.52400   -28.96800 1.000 30.70598  ? 96  PRO L CA  1 
ATOM   4173 C C   . PRO C  3 96  ? -24.01000 10.56900  -29.71900 1.000 27.23414  ? 96  PRO L C   1 
ATOM   4174 O O   . PRO C  3 96  ? -23.18800 10.17700  -30.51500 1.000 27.76274  ? 96  PRO L O   1 
ATOM   4175 C CB  . PRO C  3 96  ? -24.00300 8.74000   -27.96500 1.000 30.05400  ? 96  PRO L CB  1 
ATOM   4176 C CG  . PRO C  3 96  ? -24.47900 7.34200   -28.05100 1.000 33.43289  ? 96  PRO L CG  1 
ATOM   4177 C CD  . PRO C  3 96  ? -24.85900 7.16400   -29.48500 1.000 36.88960  ? 96  PRO L CD  1 
ATOM   4178 N N   . THR C  3 97  ? -24.21700 11.85500  -29.44400 1.000 29.41669  ? 97  THR L N   1 
ATOM   4179 C CA  . THR C  3 97  ? -23.50400 12.92800  -30.14600 1.000 28.15100  ? 97  THR L CA  1 
ATOM   4180 C C   . THR C  3 97  ? -22.82700 13.96700  -29.22400 1.000 27.17324  ? 97  THR L C   1 
ATOM   4181 O O   . THR C  3 97  ? -23.36000 14.27800  -28.17900 1.000 20.61404  ? 97  THR L O   1 
ATOM   4182 C CB  . THR C  3 97  ? -24.48000 13.68300  -31.06900 1.000 25.74885  ? 97  THR L CB  1 
ATOM   4183 O OG1 . THR C  3 97  ? -25.73900 13.83300  -30.42100 1.000 28.17633  ? 97  THR L OG1 1 
ATOM   4184 C CG2 . THR C  3 97  ? -24.66400 12.92900  -32.38000 1.000 28.35129  ? 97  THR L CG2 1 
ATOM   4185 N N   . PHE C  3 98  ? -21.69500 14.52000  -29.65000 1.000 20.31310  ? 98  PHE L N   1 
ATOM   4186 C CA  . PHE C  3 98  ? -20.95300 15.45100  -28.82200 1.000 19.56131  ? 98  PHE L CA  1 
ATOM   4187 C C   . PHE C  3 98  ? -21.00700 16.83800  -29.46000 1.000 26.39163  ? 98  PHE L C   1 
ATOM   4188 O O   . PHE C  3 98  ? -21.09100 16.96500  -30.69000 1.000 24.30241  ? 98  PHE L O   1 
ATOM   4189 C CB  . PHE C  3 98  ? -19.49100 15.04900  -28.68800 1.000 21.02885  ? 98  PHE L CB  1 
ATOM   4190 C CG  . PHE C  3 98  ? -19.27100 13.77600  -27.93800 1.000 22.11317  ? 98  PHE L CG  1 
ATOM   4191 C CD1 . PHE C  3 98  ? -19.52200 12.56400  -28.56000 1.000 24.35954  ? 98  PHE L CD1 1 
ATOM   4192 C CD2 . PHE C  3 98  ? -18.87500 13.78500  -26.62000 1.000 20.05027  ? 98  PHE L CD2 1 
ATOM   4193 C CE1 . PHE C  3 98  ? -19.30700 11.37200  -27.87900 1.000 30.01371  ? 98  PHE L CE1 1 
ATOM   4194 C CE2 . PHE C  3 98  ? -18.67500 12.61800  -25.93000 1.000 23.83650  ? 98  PHE L CE2 1 
ATOM   4195 C CZ  . PHE C  3 98  ? -18.89900 11.40200  -26.55200 1.000 23.88849  ? 98  PHE L CZ  1 
ATOM   4196 N N   . GLY C  3 99  ? -20.95800 17.88500  -28.63600 1.000 19.77381  ? 99  GLY L N   1 
ATOM   4197 C CA  . GLY C  3 99  ? -20.74100 19.21200  -29.18100 1.000 24.19121  ? 99  GLY L CA  1 
ATOM   4198 C C   . GLY C  3 99  ? -19.37100 19.29500  -29.83400 1.000 23.88581  ? 99  GLY L C   1 
ATOM   4199 O O   . GLY C  3 99  ? -18.53100 18.40900  -29.69600 1.000 19.95561  ? 99  GLY L O   1 
ATOM   4200 N N   . GLN C  3 100 ? -19.08100 20.37400  -30.55500 1.000 22.37334  ? 100 GLN L N   1 
ATOM   4201 C CA  . GLN C  3 100 ? -17.79800 20.50300  -31.26300 1.000 17.66999  ? 100 GLN L CA  1 
ATOM   4202 C C   . GLN C  3 100 ? -16.60000 20.76400  -30.37100 1.000 20.90490  ? 100 GLN L C   1 
ATOM   4203 O O   . GLN C  3 100 ? -15.47400 20.60100  -30.78800 1.000 25.05179  ? 100 GLN L O   1 
ATOM   4204 C CB  . GLN C  3 100 ? -17.83800 21.63300  -32.26800 1.000 25.38050  ? 100 GLN L CB  1 
ATOM   4205 C CG  . GLN C  3 100 ? -17.60000 23.00700  -31.67100 1.000 26.88895  ? 100 GLN L CG  1 
ATOM   4206 C CD  . GLN C  3 100 ? -18.85200 23.62900  -31.08900 1.000 39.39127  ? 100 GLN L CD  1 
ATOM   4207 O OE1 . GLN C  3 100 ? -19.89400 22.99000  -30.99400 1.000 35.32193  ? 100 GLN L OE1 1 
ATOM   4208 N NE2 . GLN C  3 100 ? -18.75100 24.88600  -30.70400 1.000 30.89511  ? 100 GLN L NE2 1 
ATOM   4209 N N   . GLY C  3 101 ? -16.85800 21.17100  -29.14800 1.000 24.88534  ? 101 GLY L N   1 
ATOM   4210 C CA  . GLY C  3 101 ? -15.80300 21.46000  -28.23600 1.000 17.01009  ? 101 GLY L CA  1 
ATOM   4211 C C   . GLY C  3 101 ? -15.56100 22.91100  -27.95500 1.000 31.30414  ? 101 GLY L C   1 
ATOM   4212 O O   . GLY C  3 101 ? -15.79900 23.74700  -28.80500 1.000 18.88538  ? 101 GLY L O   1 
ATOM   4213 N N   . THR C  3 102 ? -15.05800 23.17900  -26.75900 1.000 21.60824  ? 102 THR L N   1 
ATOM   4214 C CA  . THR C  3 102 ? -14.74700 24.50000  -26.34800 1.000 15.95080  ? 102 THR L CA  1 
ATOM   4215 C C   . THR C  3 102 ? -13.34500 24.45300  -25.70300 1.000 22.56564  ? 102 THR L C   1 
ATOM   4216 O O   . THR C  3 102 ? -13.16400 23.83800  -24.66500 1.000 17.49726  ? 102 THR L O   1 
ATOM   4217 C CB  . THR C  3 102 ? -15.84700 25.05300  -25.41400 1.000 17.48436  ? 102 THR L CB  1 
ATOM   4218 O OG1 . THR C  3 102 ? -17.09700 25.09700  -26.10300 1.000 19.49568  ? 102 THR L OG1 1 
ATOM   4219 C CG2 . THR C  3 102 ? -15.46300 26.43500  -24.92200 1.000 19.27330  ? 102 THR L CG2 1 
ATOM   4220 N N   . LYS C  3 103 ? -12.36700 25.06000  -26.36500 1.000 14.45360  ? 103 LYS L N   1 
ATOM   4221 C CA  . LYS C  3 103 ? -10.99500 25.08400  -25.86300 1.000 16.66421  ? 103 LYS L CA  1 
ATOM   4222 C C   . LYS C  3 103 ? -10.76600 26.20200  -24.88300 1.000 17.39470  ? 103 LYS L C   1 
ATOM   4223 O O   . LYS C  3 103 ? -11.00100 27.35000  -25.17300 1.000 21.98259  ? 103 LYS L O   1 
ATOM   4224 C CB  . LYS C  3 103 ? -9.96200  25.19200  -26.98600 1.000 19.52092  ? 103 LYS L CB  1 
ATOM   4225 C CG  . LYS C  3 103 ? -8.52400  25.05300  -26.51700 1.000 23.95769  ? 103 LYS L CG  1 
ATOM   4226 C CD  . LYS C  3 103 ? -7.66900  24.33000  -27.53900 1.000 29.10913  ? 103 LYS L CD  1 
ATOM   4227 C CE  . LYS C  3 103 ? -6.20600  24.33600  -27.13500 1.000 31.90787  ? 103 LYS L CE  1 
ATOM   4228 N NZ  . LYS C  3 103 ? -5.32000  24.08000  -28.29600 1.000 33.93270  ? 103 LYS L NZ  1 
ATOM   4229 N N   . VAL C  3 104 ? -10.28900 25.84400  -23.72900 1.000 17.13755  ? 104 VAL L N   1 
ATOM   4230 C CA  . VAL C  3 104 ? -10.02400 26.82800  -22.71700 1.000 18.00984  ? 104 VAL L CA  1 
ATOM   4231 C C   . VAL C  3 104 ? -8.54500  27.12300  -22.50100 1.000 19.13312  ? 104 VAL L C   1 
ATOM   4232 O O   . VAL C  3 104 ? -7.77600  26.26700  -22.12300 1.000 18.76601  ? 104 VAL L O   1 
ATOM   4233 C CB  . VAL C  3 104 ? -10.69800 26.48000  -21.37500 1.000 18.73448  ? 104 VAL L CB  1 
ATOM   4234 C CG1 . VAL C  3 104 ? -10.33400 27.50800  -20.31600 1.000 13.92823  ? 104 VAL L CG1 1 
ATOM   4235 C CG2 . VAL C  3 104 ? -12.20800 26.41400  -21.54500 1.000 13.68915  ? 104 VAL L CG2 1 
ATOM   4236 N N   . GLU C  3 105 ? -8.19300  28.34400  -22.77100 1.000 17.77101  ? 105 GLU L N   1 
ATOM   4237 C CA  . GLU C  3 105 ? -6.83300  28.77500  -22.57500 1.000 21.22469  ? 105 GLU L CA  1 
ATOM   4238 C C   . GLU C  3 105 ? -6.71400  29.88000  -21.53500 1.000 20.56818  ? 105 GLU L C   1 
ATOM   4239 O O   . GLU C  3 105 ? -7.69600  30.51800  -21.20200 1.000 16.83753  ? 105 GLU L O   1 
ATOM   4240 C CB  . GLU C  3 105 ? -6.19200  29.20300  -23.89200 1.000 27.81796  ? 105 GLU L CB  1 
ATOM   4241 C CG  . GLU C  3 105 ? -5.27400  28.14500  -24.48200 1.000 42.52310  ? 105 GLU L CG  1 
ATOM   4242 C CD  . GLU C  3 105 ? -5.27600  28.11000  -25.99900 1.000 39.12650  ? 105 GLU L CD  1 
ATOM   4243 O OE1 . GLU C  3 105 ? -6.35800  28.21500  -26.59800 1.000 40.83113  ? 105 GLU L OE1 1 
ATOM   4244 O OE2 . GLU C  3 105 ? -4.19200  27.97700  -26.58700 1.000 31.84075  ? 105 GLU L OE2 1 
ATOM   4245 N N   . ILE C  3 106 ? -5.50300  30.14600  -21.11000 1.000 17.61964  ? 106 ILE L N   1 
ATOM   4246 C CA  . ILE C  3 106 ? -5.25200  31.05600  -20.00700 1.000 14.79514  ? 106 ILE L CA  1 
ATOM   4247 C C   . ILE C  3 106 ? -4.79900  32.40000  -20.61000 1.000 20.02262  ? 106 ILE L C   1 
ATOM   4248 O O   . ILE C  3 106 ? -3.82900  32.46400  -21.39000 1.000 16.13643  ? 106 ILE L O   1 
ATOM   4249 C CB  . ILE C  3 106 ? -4.19200  30.47500  -19.05200 1.000 16.45599  ? 106 ILE L CB  1 
ATOM   4250 C CG1 . ILE C  3 106 ? -4.61400  29.09800  -18.46000 1.000 19.01152  ? 106 ILE L CG1 1 
ATOM   4251 C CG2 . ILE C  3 106 ? -3.98300  31.42500  -17.87500 1.000 14.34542  ? 106 ILE L CG2 1 
ATOM   4252 C CD1 . ILE C  3 106 ? -6.15500  28.83400  -18.32500 1.000 21.63901  ? 106 ILE L CD1 1 
ATOM   4253 N N   . LYS C  3 107 ? -5.50100  33.45800  -20.23700 1.000 20.63162  ? 107 LYS L N   1 
ATOM   4254 C CA  . LYS C  3 107 ? -5.09000  34.84500  -20.46900 1.000 20.58266  ? 107 LYS L CA  1 
ATOM   4255 C C   . LYS C  3 107 ? -4.00000  35.28000  -19.50000 1.000 20.24725  ? 107 LYS L C   1 
ATOM   4256 O O   . LYS C  3 107 ? -4.11100  35.06900  -18.29300 1.000 15.72226  ? 107 LYS L O   1 
ATOM   4257 C CB  . LYS C  3 107 ? -6.29500  35.76400  -20.32400 1.000 18.19545  ? 107 LYS L CB  1 
ATOM   4258 C CG  . LYS C  3 107 ? -6.29700  36.90200  -21.29800 1.000 28.37094  ? 107 LYS L CG  1 
ATOM   4259 C CD  . LYS C  3 107 ? -7.08400  38.11300  -20.82000 1.000 37.48042  ? 107 LYS L CD  1 
ATOM   4260 C CE  . LYS C  3 107 ? -8.56900  37.98000  -21.28200 1.000 56.61680  ? 107 LYS L CE  1 
ATOM   4261 N NZ  . LYS C  3 107 ? -9.63000  38.67700  -20.46000 1.000 57.76442  ? 107 LYS L NZ  1 
ATOM   4262 N N   . ARG C  3 108 ? -2.94600  35.87400  -20.05800 1.000 16.68606  ? 108 ARG L N   1 
ATOM   4263 C CA  . ARG C  3 108 ? -1.81200  36.35900  -19.24500 1.000 13.53657  ? 108 ARG L CA  1 
ATOM   4264 C C   . ARG C  3 108 ? -1.24800  37.65900  -19.85500 1.000 19.86068  ? 108 ARG L C   1 
ATOM   4265 O O   . ARG C  3 108 ? -1.73500  38.08800  -20.90300 1.000 15.15699  ? 108 ARG L O   1 
ATOM   4266 C CB  . ARG C  3 108 ? -0.74700  35.26700  -19.13900 1.000 17.18824  ? 108 ARG L CB  1 
ATOM   4267 C CG  . ARG C  3 108 ? 0.07000   35.01100  -20.39400 1.000 12.89430  ? 108 ARG L CG  1 
ATOM   4268 C CD  . ARG C  3 108 ? 1.49400   34.65600  -20.01000 1.000 16.55331  ? 108 ARG L CD  1 
ATOM   4269 N NE  . ARG C  3 108 ? 2.27200   35.85600  -19.75600 1.000 14.56198  ? 108 ARG L NE  1 
ATOM   4270 C CZ  . ARG C  3 108 ? 3.42800   35.90100  -19.11200 1.000 14.79304  ? 108 ARG L CZ  1 
ATOM   4271 N NH1 . ARG C  3 108 ? 3.97500   34.79600  -18.63900 1.000 14.59694  ? 108 ARG L NH1 1 
ATOM   4272 N NH2 . ARG C  3 108 ? 4.03800   37.05600  -18.94500 1.000 16.52368  ? 108 ARG L NH2 1 
ATOM   4273 N N   . THR C  3 109 ? -0.23200  38.22800  -19.20600 1.000 14.03722  ? 109 THR L N   1 
ATOM   4274 C CA  . THR C  3 109 ? 0.32500   39.47700  -19.71000 1.000 15.93652  ? 109 THR L CA  1 
ATOM   4275 C C   . THR C  3 109 ? 1.15200   39.19100  -20.97600 1.000 15.31355  ? 109 THR L C   1 
ATOM   4276 O O   . THR C  3 109 ? 1.67800   38.08400  -21.16800 1.000 13.19235  ? 109 THR L O   1 
ATOM   4277 C CB  . THR C  3 109 ? 1.26900   40.12800  -18.69100 1.000 12.99318  ? 109 THR L CB  1 
ATOM   4278 O OG1 . THR C  3 109 ? 2.16000   39.13800  -18.22100 1.000 16.73256  ? 109 THR L OG1 1 
ATOM   4279 C CG2 . THR C  3 109 ? 0.47800   40.65700  -17.44200 1.000 18.11301  ? 109 THR L CG2 1 
ATOM   4280 N N   . VAL C  3 110 ? 1.32900   40.23000  -21.80500 1.000 15.46833  ? 110 VAL L N   1 
ATOM   4281 C CA  . VAL C  3 110 ? 2.23200   40.13200  -22.94800 1.000 14.67683  ? 110 VAL L CA  1 
ATOM   4282 C C   . VAL C  3 110 ? 3.63600   39.74300  -22.52000 1.000 15.41781  ? 110 VAL L C   1 
ATOM   4283 O O   . VAL C  3 110 ? 4.18300   40.26000  -21.53900 1.000 17.79898  ? 110 VAL L O   1 
ATOM   4284 C CB  . VAL C  3 110 ? 2.24100   41.45700  -23.71800 1.000 21.30861  ? 110 VAL L CB  1 
ATOM   4285 C CG1 . VAL C  3 110 ? 3.14800   41.33800  -24.93000 1.000 19.22507  ? 110 VAL L CG1 1 
ATOM   4286 C CG2 . VAL C  3 110 ? 0.81600   41.77900  -24.20400 1.000 18.48839  ? 110 VAL L CG2 1 
ATOM   4287 N N   . ALA C  3 111 ? 4.22800   38.81000  -23.25500 1.000 14.37303  ? 111 ALA L N   1 
ATOM   4288 C CA  . ALA C  3 111 ? 5.60900   38.41300  -23.03800 1.000 16.45319  ? 111 ALA L CA  1 
ATOM   4289 C C   . ALA C  3 111 ? 6.28500   38.26900  -24.40000 1.000 21.30311  ? 111 ALA L C   1 
ATOM   4290 O O   . ALA C  3 111 ? 5.76800   37.55800  -25.26400 1.000 15.35081  ? 111 ALA L O   1 
ATOM   4291 C CB  . ALA C  3 111 ? 5.68000   37.08100  -22.25800 1.000 15.29936  ? 111 ALA L CB  1 
ATOM   4292 N N   . ALA C  3 112 ? 7.46500   38.93300  -24.58900 1.000 18.39400  ? 112 ALA L N   1 
ATOM   4293 C CA  . ALA C  3 112 ? 8.17800   38.87900  -25.86600 1.000 20.89322  ? 112 ALA L CA  1 
ATOM   4294 C C   . ALA C  3 112 ? 8.95200   37.56400  -26.00600 1.000 15.92519  ? 112 ALA L C   1 
ATOM   4295 O O   . ALA C  3 112 ? 9.46300   37.03300  -25.01500 1.000 19.32397  ? 112 ALA L O   1 
ATOM   4296 C CB  . ALA C  3 112 ? 9.14200   40.07000  -25.96700 1.000 22.07443  ? 112 ALA L CB  1 
ATOM   4297 N N   . PRO C  3 113 ? 9.06300   37.00400  -27.21600 1.000 14.11275  ? 113 PRO L N   1 
ATOM   4298 C CA  . PRO C  3 113 ? 9.87900   35.78900  -27.38900 1.000 13.36022  ? 113 PRO L CA  1 
ATOM   4299 C C   . PRO C  3 113 ? 11.35600  36.10400  -27.22100 1.000 19.92770  ? 113 PRO L C   1 
ATOM   4300 O O   . PRO C  3 113 ? 11.79000  37.22400  -27.46200 1.000 18.95904  ? 113 PRO L O   1 
ATOM   4301 C CB  . PRO C  3 113 ? 9.60000   35.35000  -28.83900 1.000 14.63102  ? 113 PRO L CB  1 
ATOM   4302 C CG  . PRO C  3 113 ? 9.21500   36.67300  -29.54600 1.000 16.75858  ? 113 PRO L CG  1 
ATOM   4303 C CD  . PRO C  3 113 ? 8.46000   37.46200  -28.49100 1.000 17.12400  ? 113 PRO L CD  1 
ATOM   4304 N N   . SER C  3 114 ? 12.10900  35.07300  -26.87100 1.000 18.43043  ? 114 SER L N   1 
ATOM   4305 C CA  A SER C  3 114 ? 13.56400  35.12100  -26.97700 0.450 21.76239  ? 114 SER L CA  1 
ATOM   4306 C CA  B SER C  3 114 ? 13.56700  35.14000  -26.97700 0.550 21.77701  ? 114 SER L CA  1 
ATOM   4307 C C   . SER C  3 114 ? 13.71500  34.39600  -28.40700 1.000 16.84424  ? 114 SER L C   1 
ATOM   4308 O O   . SER C  3 114 ? 13.00500  33.41900  -28.69600 1.000 19.25847  ? 114 SER L O   1 
ATOM   4309 C CB  A SER C  3 114 ? 14.24600  34.35800  -25.87100 0.450 21.31505  ? 114 SER L CB  1 
ATOM   4310 C CB  B SER C  3 114 ? 14.26800  34.42800  -25.84800 0.550 21.32309  ? 114 SER L CB  1 
ATOM   4311 O OG  A SER C  3 114 ? 14.14300  35.04200  -24.64100 0.450 19.40531  ? 114 SER L OG  1 
ATOM   4312 O OG  B SER C  3 114 ? 13.70900  33.15100  -25.63300 0.550 17.82055  ? 114 SER L OG  1 
ATOM   4313 N N   . VAL C  3 115 ? 14.60100  34.84700  -29.27000 1.000 15.48670  ? 115 VAL L N   1 
ATOM   4314 C CA  . VAL C  3 115 ? 14.68700  34.32200  -30.62900 1.000 17.65942  ? 115 VAL L CA  1 
ATOM   4315 C C   . VAL C  3 115 ? 16.05500  33.70800  -30.85800 1.000 20.13674  ? 115 VAL L C   1 
ATOM   4316 O O   . VAL C  3 115 ? 17.07900  34.31600  -30.51800 1.000 17.70912  ? 115 VAL L O   1 
ATOM   4317 C CB  . VAL C  3 115 ? 14.38400  35.39700  -31.69100 1.000 18.12441  ? 115 VAL L CB  1 
ATOM   4318 C CG1 . VAL C  3 115 ? 14.21700  34.72100  -33.03400 1.000 16.30653  ? 115 VAL L CG1 1 
ATOM   4319 C CG2 . VAL C  3 115 ? 13.08700  36.13700  -31.34800 1.000 13.99226  ? 115 VAL L CG2 1 
ATOM   4320 N N   . PHE C  3 116 ? 16.06600  32.52600  -31.48200 1.000 16.39984  ? 116 PHE L N   1 
ATOM   4321 C CA  . PHE C  3 116 ? 17.28800  31.77000  -31.74600 1.000 18.44338  ? 116 PHE L CA  1 
ATOM   4322 C C   . PHE C  3 116 ? 17.25100  31.20800  -33.17000 1.000 23.27501  ? 116 PHE L C   1 
ATOM   4323 O O   . PHE C  3 116 ? 16.20200  30.73400  -33.62300 1.000 20.34090  ? 116 PHE L O   1 
ATOM   4324 C CB  . PHE C  3 116 ? 17.42000  30.61200  -30.75200 1.000 21.05211  ? 116 PHE L CB  1 
ATOM   4325 C CG  . PHE C  3 116 ? 17.42200  31.04100  -29.32700 1.000 24.72318  ? 116 PHE L CG  1 
ATOM   4326 C CD1 . PHE C  3 116 ? 18.60100  31.47600  -28.71500 1.000 27.04585  ? 116 PHE L CD1 1 
ATOM   4327 C CD2 . PHE C  3 116 ? 16.24000  31.05500  -28.59800 1.000 19.06698  ? 116 PHE L CD2 1 
ATOM   4328 C CE1 . PHE C  3 116 ? 18.61200  31.85400  -27.38300 1.000 26.99698  ? 116 PHE L CE1 1 
ATOM   4329 C CE2 . PHE C  3 116 ? 16.27000  31.44500  -27.24500 1.000 20.79701  ? 116 PHE L CE2 1 
ATOM   4330 C CZ  . PHE C  3 116 ? 17.44100  31.83800  -26.65900 1.000 21.31004  ? 116 PHE L CZ  1 
ATOM   4331 N N   . ILE C  3 117 ? 18.38700  31.26500  -33.88400 1.000 19.66339  ? 117 ILE L N   1 
ATOM   4332 C CA  . ILE C  3 117 ? 18.49000  30.65400  -35.20600 1.000 21.50227  ? 117 ILE L CA  1 
ATOM   4333 C C   . ILE C  3 117 ? 19.50400  29.51000  -35.18600 1.000 21.43808  ? 117 ILE L C   1 
ATOM   4334 O O   . ILE C  3 117 ? 20.55400  29.58300  -34.53300 1.000 24.19752  ? 117 ILE L O   1 
ATOM   4335 C CB  . ILE C  3 117 ? 18.83600  31.68200  -36.30100 1.000 16.91425  ? 117 ILE L CB  1 
ATOM   4336 C CG1 . ILE C  3 117 ? 18.68600  31.03100  -37.69300 1.000 19.04480  ? 117 ILE L CG1 1 
ATOM   4337 C CG2 . ILE C  3 117 ? 20.25000  32.20500  -36.17800 1.000 24.32759  ? 117 ILE L CG2 1 
ATOM   4338 C CD1 . ILE C  3 117 ? 18.29700  32.02200  -38.74700 1.000 21.43544  ? 117 ILE L CD1 1 
ATOM   4339 N N   . PHE C  3 118 ? 19.18700  28.45600  -35.91800 1.000 22.28390  ? 118 PHE L N   1 
ATOM   4340 C CA  . PHE C  3 118 ? 20.00500  27.25600  -36.03400 1.000 18.84346  ? 118 PHE L CA  1 
ATOM   4341 C C   . PHE C  3 118 ? 20.33800  26.96000  -37.48400 1.000 27.37741  ? 118 PHE L C   1 
ATOM   4342 O O   . PHE C  3 118 ? 19.43000  26.61600  -38.26800 1.000 21.07857  ? 118 PHE L O   1 
ATOM   4343 C CB  . PHE C  3 118 ? 19.21900  26.09700  -35.44900 1.000 25.15934  ? 118 PHE L CB  1 
ATOM   4344 C CG  . PHE C  3 118 ? 19.05300  26.14900  -33.97100 1.000 28.04391  ? 118 PHE L CG  1 
ATOM   4345 C CD1 . PHE C  3 118 ? 20.14900  25.97400  -33.11000 1.000 23.68101  ? 118 PHE L CD1 1 
ATOM   4346 C CD2 . PHE C  3 118 ? 17.83400  26.52700  -33.43500 1.000 20.48364  ? 118 PHE L CD2 1 
ATOM   4347 C CE1 . PHE C  3 118 ? 19.98500  26.01200  -31.73700 1.000 24.79506  ? 118 PHE L CE1 1 
ATOM   4348 C CE2 . PHE C  3 118 ? 17.66500  26.61000  -32.08400 1.000 25.85154  ? 118 PHE L CE2 1 
ATOM   4349 C CZ  . PHE C  3 118 ? 18.75900  26.35600  -31.21800 1.000 25.19863  ? 118 PHE L CZ  1 
ATOM   4350 N N   . PRO C  3 119 ? 21.60800  27.04300  -37.87400 1.000 25.41497  ? 119 PRO L N   1 
ATOM   4351 C CA  . PRO C  3 119 ? 22.02500  26.59000  -39.20700 1.000 24.47542  ? 119 PRO L CA  1 
ATOM   4352 C C   . PRO C  3 119 ? 21.87600  25.08900  -39.36400 1.000 26.38688  ? 119 PRO L C   1 
ATOM   4353 O O   . PRO C  3 119 ? 21.79200  24.34500  -38.37300 1.000 25.26740  ? 119 PRO L O   1 
ATOM   4354 C CB  . PRO C  3 119 ? 23.50000  27.03900  -39.29700 1.000 24.83098  ? 119 PRO L CB  1 
ATOM   4355 C CG  . PRO C  3 119 ? 23.71500  27.90800  -38.13800 1.000 30.55431  ? 119 PRO L CG  1 
ATOM   4356 C CD  . PRO C  3 119 ? 22.74300  27.50100  -37.06600 1.000 23.77919  ? 119 PRO L CD  1 
ATOM   4357 N N   . PRO C  3 120 ? 21.74900  24.67900  -40.63400 1.000 24.90909  ? 120 PRO L N   1 
ATOM   4358 C CA  . PRO C  3 120 ? 21.71700  23.25400  -40.88100 1.000 28.35336  ? 120 PRO L CA  1 
ATOM   4359 C C   . PRO C  3 120 ? 22.96600  22.56700  -40.35300 1.000 32.97352  ? 120 PRO L C   1 
ATOM   4360 O O   . PRO C  3 120 ? 24.02300  23.16700  -40.26900 1.000 20.61159  ? 120 PRO L O   1 
ATOM   4361 C CB  . PRO C  3 120 ? 21.71200  23.16200  -42.40500 1.000 26.81027  ? 120 PRO L CB  1 
ATOM   4362 C CG  . PRO C  3 120 ? 22.20500  24.46300  -42.88800 1.000 26.58852  ? 120 PRO L CG  1 
ATOM   4363 C CD  . PRO C  3 120 ? 21.71600  25.44500  -41.89200 1.000 21.76657  ? 120 PRO L CD  1 
ATOM   4364 N N   . SER C  3 121 ? 22.79900  21.31200  -39.99700 1.000 35.10519  ? 121 SER L N   1 
ATOM   4365 C CA  . SER C  3 121 ? 23.90000  20.51000  -39.51900 1.000 39.28946  ? 121 SER L CA  1 
ATOM   4366 C C   . SER C  3 121 ? 24.79700  19.97500  -40.63900 1.000 29.05764  ? 121 SER L C   1 
ATOM   4367 O O   . SER C  3 121 ? 24.34000  19.67800  -41.71700 1.000 33.66065  ? 121 SER L O   1 
ATOM   4368 C CB  . SER C  3 121 ? 23.34000  19.32900  -38.71000 1.000 25.09367  ? 121 SER L CB  1 
ATOM   4369 O OG  . SER C  3 121 ? 23.03900  18.23200  -39.53600 1.000 40.08585  ? 121 SER L OG  1 
ATOM   4370 N N   . ASP C  3 122 ? 26.07700  19.84800  -40.34900 1.000 40.27282  ? 122 ASP L N   1 
ATOM   4371 C CA  . ASP C  3 122 ? 26.99800  19.25500  -41.32000 1.000 42.81176  ? 122 ASP L CA  1 
ATOM   4372 C C   . ASP C  3 122 ? 26.58400  17.83500  -41.63000 1.000 37.27357  ? 122 ASP L C   1 
ATOM   4373 O O   . ASP C  3 122 ? 26.70600  17.39100  -42.75200 1.000 44.67861  ? 122 ASP L O   1 
ATOM   4374 C CB  . ASP C  3 122 ? 28.43500  19.31000  -40.81300 1.000 46.24841  ? 122 ASP L CB  1 
ATOM   4375 C CG  . ASP C  3 122 ? 28.96700  20.73700  -40.68300 1.000 59.35011  ? 122 ASP L CG  1 
ATOM   4376 O OD1 . ASP C  3 122 ? 28.39700  21.66600  -41.29000 1.000 54.99950  ? 122 ASP L OD1 1 
ATOM   4377 O OD2 . ASP C  3 122 ? 29.96700  20.92800  -39.96600 1.000 68.42211  ? 122 ASP L OD2 1 
ATOM   4378 N N   . GLU C  3 123 ? 26.04900  17.14300  -40.63700 1.000 42.21637  ? 123 GLU L N   1 
ATOM   4379 C CA  . GLU C  3 123 ? 25.57100  15.79000  -40.86200 1.000 39.66006  ? 123 GLU L CA  1 
ATOM   4380 C C   . GLU C  3 123 ? 24.46300  15.82600  -41.86800 1.000 36.19968  ? 123 GLU L C   1 
ATOM   4381 O O   . GLU C  3 123 ? 24.45900  15.08300  -42.82500 1.000 36.44334  ? 123 GLU L O   1 
ATOM   4382 C CB  . GLU C  3 123 ? 25.11200  15.14500  -39.55200 1.000 37.26978  ? 123 GLU L CB  1 
ATOM   4383 C CG  . GLU C  3 123 ? 24.23700  13.91500  -39.74400 1.000 53.57188  ? 123 GLU L CG  1 
ATOM   4384 C CD  . GLU C  3 123 ? 23.90500  13.18900  -38.45100 1.000 59.38204  ? 123 GLU L CD  1 
ATOM   4385 O OE1 . GLU C  3 123 ? 24.31800  13.64900  -37.37200 1.000 54.43773  ? 123 GLU L OE1 1 
ATOM   4386 O OE2 . GLU C  3 123 ? 23.21900  12.15000  -38.51500 1.000 58.28313  ? 123 GLU L OE2 1 
ATOM   4387 N N   . GLN C  3 124 ? 23.51600  16.72300  -41.65900 1.000 38.23398  ? 124 GLN L N   1 
ATOM   4388 C CA  . GLN C  3 124 ? 22.42600  16.84200  -42.58800 1.000 30.41473  ? 124 GLN L CA  1 
ATOM   4389 C C   . GLN C  3 124 ? 22.92600  17.20800  -43.93900 1.000 29.32610  ? 124 GLN L C   1 
ATOM   4390 O O   . GLN C  3 124 ? 22.51500  16.65700  -44.94100 1.000 37.75550  ? 124 GLN L O   1 
ATOM   4391 C CB  . GLN C  3 124 ? 21.44900  17.94300  -42.15100 1.000 28.77973  ? 124 GLN L CB  1 
ATOM   4392 C CG  . GLN C  3 124 ? 20.32200  18.12500  -43.15700 1.000 30.68981  ? 124 GLN L CG  1 
ATOM   4393 C CD  . GLN C  3 124 ? 19.22900  19.08300  -42.72200 1.000 25.59211  ? 124 GLN L CD  1 
ATOM   4394 O OE1 . GLN C  3 124 ? 19.47800  20.07000  -42.05100 1.000 19.18610  ? 124 GLN L OE1 1 
ATOM   4395 N NE2 . GLN C  3 124 ? 18.01000  18.79000  -43.13000 1.000 18.00138  ? 124 GLN L NE2 1 
ATOM   4396 N N   . LEU C  3 125 ? 23.82400  18.15600  -43.96500 1.000 35.17771  ? 125 LEU L N   1 
ATOM   4397 C CA  . LEU C  3 125 ? 24.30800  18.66300  -45.23000 1.000 42.96537  ? 125 LEU L CA  1 
ATOM   4398 C C   . LEU C  3 125 ? 24.85500  17.53600  -46.12800 1.000 42.83941  ? 125 LEU L C   1 
ATOM   4399 O O   . LEU C  3 125 ? 24.70700  17.58700  -47.32500 1.000 46.12324  ? 125 LEU L O   1 
ATOM   4400 C CB  . LEU C  3 125 ? 25.31100  19.77800  -44.94900 1.000 31.86701  ? 125 LEU L CB  1 
ATOM   4401 C CG  . LEU C  3 125 ? 24.72600  21.08300  -44.42600 1.000 34.95415  ? 125 LEU L CG  1 
ATOM   4402 C CD1 . LEU C  3 125 ? 25.82900  22.03500  -43.99900 1.000 33.34411  ? 125 LEU L CD1 1 
ATOM   4403 C CD2 . LEU C  3 125 ? 23.82400  21.72700  -45.46300 1.000 30.97986  ? 125 LEU L CD2 1 
ATOM   4404 N N   . LYS C  3 126 ? 25.39700  16.49600  -45.53500 1.000 41.32276  ? 126 LYS L N   1 
ATOM   4405 C CA  . LYS C  3 126 ? 25.87900  15.35200  -46.30800 1.000 51.11859  ? 126 LYS L CA  1 
ATOM   4406 C C   . LYS C  3 126 ? 24.77000  14.64500  -47.06800 1.000 50.63012  ? 126 LYS L C   1 
ATOM   4407 O O   . LYS C  3 126 ? 25.05200  13.82000  -47.92100 1.000 62.36604  ? 126 LYS L O   1 
ATOM   4408 C CB  . LYS C  3 126 ? 26.58600  14.36000  -45.39800 1.000 47.27808  ? 126 LYS L CB  1 
ATOM   4409 C CG  . LYS C  3 126 ? 27.50400  15.00200  -44.37400 1.000 47.93859  ? 126 LYS L CG  1 
ATOM   4410 C CD  . LYS C  3 126 ? 28.28900  13.96700  -43.58600 1.000 54.54696  ? 126 LYS L CD  1 
ATOM   4411 C CE  . LYS C  3 126 ? 29.73200  14.40400  -43.39100 1.000 62.68099  ? 126 LYS L CE  1 
ATOM   4412 N NZ  . LYS C  3 126 ? 30.09400  14.62400  -41.96300 1.000 62.11538  ? 126 LYS L NZ  1 
ATOM   4413 N N   . SER C  3 127 ? 23.51600  14.96300  -46.78300 1.000 41.95303  ? 127 SER L N   1 
ATOM   4414 C CA  . SER C  3 127 ? 22.45100  14.23800  -47.43700 1.000 46.19979  ? 127 SER L CA  1 
ATOM   4415 C C   . SER C  3 127 ? 21.72500  15.04000  -48.47800 1.000 48.34910  ? 127 SER L C   1 
ATOM   4416 O O   . SER C  3 127 ? 20.72700  14.58200  -49.01600 1.000 62.85830  ? 127 SER L O   1 
ATOM   4417 C CB  . SER C  3 127 ? 21.44600  13.70500  -46.43500 1.000 50.94749  ? 127 SER L CB  1 
ATOM   4418 O OG  . SER C  3 127 ? 20.44000  12.96100  -47.08800 1.000 60.23975  ? 127 SER L OG  1 
ATOM   4419 N N   . GLY C  3 128 ? 22.19300  16.23000  -48.76700 1.000 40.69315  ? 128 GLY L N   1 
ATOM   4420 C CA  . GLY C  3 128 ? 21.57900  16.97500  -49.83800 1.000 47.63667  ? 128 GLY L CA  1 
ATOM   4421 C C   . GLY C  3 128 ? 20.44900  17.91300  -49.53600 1.000 49.25078  ? 128 GLY L C   1 
ATOM   4422 O O   . GLY C  3 128 ? 19.90700  18.55500  -50.43000 1.000 37.11025  ? 128 GLY L O   1 
ATOM   4423 N N   . THR C  3 129 ? 20.08900  17.99000  -48.26200 1.000 53.02828  ? 129 THR L N   1 
ATOM   4424 C CA  . THR C  3 129 ? 19.04700  18.89400  -47.86000 1.000 40.76081  ? 129 THR L CA  1 
ATOM   4425 C C   . THR C  3 129 ? 19.52200  19.70200  -46.69000 1.000 31.12636  ? 129 THR L C   1 
ATOM   4426 O O   . THR C  3 129 ? 20.36500  19.27600  -45.93600 1.000 29.01464  ? 129 THR L O   1 
ATOM   4427 C CB  . THR C  3 129 ? 17.73000  18.15500  -47.55600 1.000 45.56985  ? 129 THR L CB  1 
ATOM   4428 O OG1 . THR C  3 129 ? 17.43000  17.25900  -48.62400 1.000 51.84721  ? 129 THR L OG1 1 
ATOM   4429 C CG2 . THR C  3 129 ? 16.58700  19.15000  -47.39500 1.000 41.71312  ? 129 THR L CG2 1 
ATOM   4430 N N   . ALA C  3 130 ? 19.02900  20.91100  -46.61200 1.000 28.07834  ? 130 ALA L N   1 
ATOM   4431 C CA  . ALA C  3 130 ? 19.38000  21.78500  -45.54200 1.000 24.04617  ? 130 ALA L CA  1 
ATOM   4432 C C   . ALA C  3 130 ? 18.12700  22.27400  -44.84400 1.000 36.11342  ? 130 ALA L C   1 
ATOM   4433 O O   . ALA C  3 130 ? 17.18700  22.69900  -45.49300 1.000 28.65076  ? 130 ALA L O   1 
ATOM   4434 C CB  . ALA C  3 130 ? 20.17400  22.94800  -46.03400 1.000 17.71783  ? 130 ALA L CB  1 
ATOM   4435 N N   . SER C  3 131 ? 18.12700  22.20100  -43.52700 1.000 23.61896  ? 131 SER L N   1 
ATOM   4436 C CA  . SER C  3 131 ? 17.02300  22.72200  -42.74300 1.000 21.64818  ? 131 SER L CA  1 
ATOM   4437 C C   . SER C  3 131 ? 17.59900  23.83000  -41.88300 1.000 24.39620  ? 131 SER L C   1 
ATOM   4438 O O   . SER C  3 131 ? 18.63200  23.62600  -41.22900 1.000 19.79515  ? 131 SER L O   1 
ATOM   4439 C CB  . SER C  3 131 ? 16.39800  21.62300  -41.88800 1.000 22.26848  ? 131 SER L CB  1 
ATOM   4440 O OG  . SER C  3 131 ? 15.88900  20.61400  -42.72800 1.000 20.04830  ? 131 SER L OG  1 
ATOM   4441 N N   . VAL C  3 132 ? 16.99700  25.01200  -41.95400 1.000 16.10487  ? 132 VAL L N   1 
ATOM   4442 C CA  . VAL C  3 132 ? 17.37800  26.10900  -41.09000 1.000 10.70067  ? 132 VAL L CA  1 
ATOM   4443 C C   . VAL C  3 132 ? 16.21500  26.30000  -40.12900 1.000 17.99511  ? 132 VAL L C   1 
ATOM   4444 O O   . VAL C  3 132 ? 15.06800  26.32700  -40.53700 1.000 20.62695  ? 132 VAL L O   1 
ATOM   4445 C CB  . VAL C  3 132 ? 17.65800  27.40100  -41.84000 1.000 14.57719  ? 132 VAL L CB  1 
ATOM   4446 C CG1 . VAL C  3 132 ? 18.37500  28.40400  -40.96100 1.000 17.01034  ? 132 VAL L CG1 1 
ATOM   4447 C CG2 . VAL C  3 132 ? 18.41000  27.13000  -43.13000 1.000 19.77104  ? 132 VAL L CG2 1 
ATOM   4448 N N   . VAL C  3 133 ? 16.51200  26.42000  -38.85800 1.000 17.14866  ? 133 VAL L N   1 
ATOM   4449 C CA  . VAL C  3 133 ? 15.45400  26.50000  -37.87800 1.000 17.42591  ? 133 VAL L CA  1 
ATOM   4450 C C   . VAL C  3 133 ? 15.48000  27.75300  -37.03100 1.000 12.79424  ? 133 VAL L C   1 
ATOM   4451 O O   . VAL C  3 133 ? 16.51800  28.17300  -36.57000 1.000 20.70236  ? 133 VAL L O   1 
ATOM   4452 C CB  . VAL C  3 133 ? 15.43400  25.25100  -36.95700 1.000 18.48758  ? 133 VAL L CB  1 
ATOM   4453 C CG1 . VAL C  3 133 ? 14.40000  25.39800  -35.85300 1.000 15.33100  ? 133 VAL L CG1 1 
ATOM   4454 C CG2 . VAL C  3 133 ? 15.24400  23.97000  -37.75400 1.000 12.97374  ? 133 VAL L CG2 1 
ATOM   4455 N N   . CYS C  3 134 ? 14.32100  28.33700  -36.85300 1.000 15.59161  ? 134 CYS L N   1 
ATOM   4456 C CA  . CYS C  3 134 ? 14.19100  29.52500  -36.03600 1.000 13.84613  ? 134 CYS L CA  1 
ATOM   4457 C C   . CYS C  3 134 ? 13.28100  29.25800  -34.81900 1.000 18.93338  ? 134 CYS L C   1 
ATOM   4458 O O   . CYS C  3 134 ? 12.20400  28.71400  -34.98000 1.000 18.22535  ? 134 CYS L O   1 
ATOM   4459 C CB  . CYS C  3 134 ? 13.67200  30.67500  -36.85200 1.000 12.04206  ? 134 CYS L CB  1 
ATOM   4460 S SG  . CYS C  3 134 ? 13.53400  32.23900  -35.98900 1.000 23.61541  ? 134 CYS L SG  1 
ATOM   4461 N N   . LEU C  3 135 ? 13.72200  29.64600  -33.63500 1.000 18.19795  ? 135 LEU L N   1 
ATOM   4462 C CA  . LEU C  3 135 ? 12.97800  29.39500  -32.40100 1.000 17.60412  ? 135 LEU L CA  1 
ATOM   4463 C C   . LEU C  3 135 ? 12.47500  30.68900  -31.76600 1.000 15.92542  ? 135 LEU L C   1 
ATOM   4464 O O   . LEU C  3 135 ? 13.25700  31.61100  -31.53300 1.000 16.03527  ? 135 LEU L O   1 
ATOM   4465 C CB  . LEU C  3 135 ? 13.84200  28.58800  -31.42000 1.000 9.97094   ? 135 LEU L CB  1 
ATOM   4466 C CG  . LEU C  3 135 ? 13.25600  28.48600  -30.01700 1.000 17.25800  ? 135 LEU L CG  1 
ATOM   4467 C CD1 . LEU C  3 135 ? 11.95800  27.63800  -29.95300 1.000 18.08136  ? 135 LEU L CD1 1 
ATOM   4468 C CD2 . LEU C  3 135 ? 14.31200  27.86800  -29.09300 1.000 20.40326  ? 135 LEU L CD2 1 
ATOM   4469 N N   . LEU C  3 136 ? 11.16900  30.77600  -31.49600 1.000 16.63866  ? 136 LEU L N   1 
ATOM   4470 C CA  . LEU C  3 136 ? 10.58700  31.88100  -30.73700 1.000 12.43658  ? 136 LEU L CA  1 
ATOM   4471 C C   . LEU C  3 136 ? 10.22500  31.23200  -29.37700 1.000 13.77431  ? 136 LEU L C   1 
ATOM   4472 O O   . LEU C  3 136 ? 9.35500   30.38900  -29.31700 1.000 13.06578  ? 136 LEU L O   1 
ATOM   4473 C CB  . LEU C  3 136 ? 9.40100   32.50100  -31.42400 1.000 13.89437  ? 136 LEU L CB  1 
ATOM   4474 C CG  . LEU C  3 136 ? 9.60500   33.41800  -32.61400 1.000 14.71949  ? 136 LEU L CG  1 
ATOM   4475 C CD1 . LEU C  3 136 ? 10.25200  32.67000  -33.76400 1.000 14.07957  ? 136 LEU L CD1 1 
ATOM   4476 C CD2 . LEU C  3 136 ? 8.26100   33.99200  -33.01600 1.000 12.53203  ? 136 LEU L CD2 1 
ATOM   4477 N N   . ASN C  3 137 ? 10.91100  31.60700  -28.30700 1.000 15.09407  ? 137 ASN L N   1 
ATOM   4478 C CA  . ASN C  3 137 ? 10.75600  30.90100  -27.00800 1.000 18.32016  ? 137 ASN L CA  1 
ATOM   4479 C C   . ASN C  3 137 ? 9.94500   31.66400  -25.95800 1.000 17.27046  ? 137 ASN L C   1 
ATOM   4480 O O   . ASN C  3 137 ? 10.30400  32.80800  -25.67400 1.000 17.68412  ? 137 ASN L O   1 
ATOM   4481 C CB  . ASN C  3 137 ? 12.12900  30.54000  -26.43900 1.000 17.01398  ? 137 ASN L CB  1 
ATOM   4482 C CG  . ASN C  3 137 ? 12.08900  29.64700  -25.22100 1.000 23.03291  ? 137 ASN L CG  1 
ATOM   4483 O OD1 . ASN C  3 137 ? 11.72600  28.48100  -25.31600 1.000 29.35568  ? 137 ASN L OD1 1 
ATOM   4484 N ND2 . ASN C  3 137 ? 12.47800  30.18300  -24.07800 1.000 22.86295  ? 137 ASN L ND2 1 
ATOM   4485 N N   . ASN C  3 138 ? 8.89600   31.04000  -25.43700 1.000 16.36579  ? 138 ASN L N   1 
ATOM   4486 C CA  . ASN C  3 138 ? 8.14100   31.56300  -24.26600 1.000 17.89114  ? 138 ASN L CA  1 
ATOM   4487 C C   . ASN C  3 138 ? 7.56900   32.96900  -24.49200 1.000 18.18178  ? 138 ASN L C   1 
ATOM   4488 O O   . ASN C  3 138 ? 8.02500   33.89300  -23.83500 1.000 16.47502  ? 138 ASN L O   1 
ATOM   4489 C CB  . ASN C  3 138 ? 8.97000   31.39300  -22.99100 1.000 20.40231  ? 138 ASN L CB  1 
ATOM   4490 C CG  . ASN C  3 138 ? 9.17200   29.93300  -22.65200 1.000 22.27543  ? 138 ASN L CG  1 
ATOM   4491 O OD1 . ASN C  3 138 ? 9.76000   29.19100  -23.42700 1.000 21.93146  ? 138 ASN L OD1 1 
ATOM   4492 N ND2 . ASN C  3 138 ? 8.65800   29.50500  -21.51300 1.000 24.91057  ? 138 ASN L ND2 1 
ATOM   4493 N N   . PHE C  3 139 ? 6.58000   33.06100  -25.37000 1.000 13.82521  ? 139 PHE L N   1 
ATOM   4494 C CA  . PHE C  3 139 ? 5.92700   34.35300  -25.66700 1.000 14.33140  ? 139 PHE L CA  1 
ATOM   4495 C C   . PHE C  3 139 ? 4.40700   34.26800  -25.47500 1.000 17.83323  ? 139 PHE L C   1 
ATOM   4496 O O   . PHE C  3 139 ? 3.88100   33.15600  -25.39500 1.000 14.74628  ? 139 PHE L O   1 
ATOM   4497 C CB  . PHE C  3 139 ? 6.25000   34.78700  -27.09600 1.000 12.91350  ? 139 PHE L CB  1 
ATOM   4498 C CG  . PHE C  3 139 ? 5.82700   33.82100  -28.17200 1.000 15.09195  ? 139 PHE L CG  1 
ATOM   4499 C CD1 . PHE C  3 139 ? 6.63000   32.74600  -28.51600 1.000 11.25514  ? 139 PHE L CD1 1 
ATOM   4500 C CD2 . PHE C  3 139 ? 4.63500   33.99800  -28.85200 1.000 13.56026  ? 139 PHE L CD2 1 
ATOM   4501 C CE1 . PHE C  3 139 ? 6.24200   31.86100  -29.50700 1.000 11.98418  ? 139 PHE L CE1 1 
ATOM   4502 C CE2 . PHE C  3 139 ? 4.24800   33.11100  -29.84300 1.000 15.79630  ? 139 PHE L CE2 1 
ATOM   4503 C CZ  . PHE C  3 139 ? 5.05200   32.04700  -30.16900 1.000 13.28262  ? 139 PHE L CZ  1 
ATOM   4504 N N   . TYR C  3 140 ? 3.74000   35.41800  -25.42000 1.000 15.06579  ? 140 TYR L N   1 
ATOM   4505 C CA  . TYR C  3 140 ? 2.27900   35.53700  -25.28600 1.000 16.34344  ? 140 TYR L CA  1 
ATOM   4506 C C   . TYR C  3 140 ? 1.90000   36.94600  -25.77400 1.000 15.75450  ? 140 TYR L C   1 
ATOM   4507 O O   . TYR C  3 140 ? 2.56400   37.90600  -25.42600 1.000 15.09361  ? 140 TYR L O   1 
ATOM   4508 C CB  . TYR C  3 140 ? 1.73600   35.33300  -23.86500 1.000 14.08478  ? 140 TYR L CB  1 
ATOM   4509 C CG  . TYR C  3 140 ? 0.22900   35.33100  -23.82600 1.000 15.37823  ? 140 TYR L CG  1 
ATOM   4510 C CD1 . TYR C  3 140 ? -0.47900  36.51100  -23.70400 1.000 15.60240  ? 140 TYR L CD1 1 
ATOM   4511 C CD2 . TYR C  3 140 ? -0.48600  34.15100  -23.95700 1.000 16.41288  ? 140 TYR L CD2 1 
ATOM   4512 C CE1 . TYR C  3 140 ? -1.85300  36.51600  -23.68900 1.000 18.92456  ? 140 TYR L CE1 1 
ATOM   4513 C CE2 . TYR C  3 140 ? -1.86100  34.14700  -23.95000 1.000 16.78754  ? 140 TYR L CE2 1 
ATOM   4514 C CZ  . TYR C  3 140 ? -2.53900  35.33200  -23.81700 1.000 17.10637  ? 140 TYR L CZ  1 
ATOM   4515 O OH  . TYR C  3 140 ? -3.90000  35.33700  -23.80200 1.000 21.52050  ? 140 TYR L OH  1 
ATOM   4516 N N   . PRO C  3 141 ? 0.84400   37.05400  -26.58100 1.000 17.24068  ? 141 PRO L N   1 
ATOM   4517 C CA  . PRO C  3 141 ? -0.06600  36.00400  -27.04800 1.000 14.49587  ? 141 PRO L CA  1 
ATOM   4518 C C   . PRO C  3 141 ? 0.52600   35.15600  -28.16200 1.000 15.86477  ? 141 PRO L C   1 
ATOM   4519 O O   . PRO C  3 141 ? 1.68800   35.34400  -28.59100 1.000 15.76422  ? 141 PRO L O   1 
ATOM   4520 C CB  . PRO C  3 141 ? -1.28400  36.79000  -27.53800 1.000 17.60570  ? 141 PRO L CB  1 
ATOM   4521 C CG  . PRO C  3 141 ? -0.74600  38.10400  -27.97600 1.000 25.73665  ? 141 PRO L CG  1 
ATOM   4522 C CD  . PRO C  3 141 ? 0.44200   38.39600  -27.07100 1.000 24.17739  ? 141 PRO L CD  1 
ATOM   4523 N N   . ARG C  3 142 ? -0.23100  34.16500  -28.60600 1.000 16.19933  ? 142 ARG L N   1 
ATOM   4524 C CA  . ARG C  3 142 ? 0.26300   33.20500  -29.62100 1.000 20.87441  ? 142 ARG L CA  1 
ATOM   4525 C C   . ARG C  3 142 ? 0.59900   33.80100  -30.99000 1.000 18.71813  ? 142 ARG L C   1 
ATOM   4526 O O   . ARG C  3 142 ? 1.48400   33.34100  -31.66200 1.000 19.83850  ? 142 ARG L O   1 
ATOM   4527 C CB  . ARG C  3 142 ? -0.72500  32.05800  -29.80600 1.000 22.27457  ? 142 ARG L CB  1 
ATOM   4528 C CG  . ARG C  3 142 ? -0.24000  30.92500  -30.68000 1.000 28.85516  ? 142 ARG L CG  1 
ATOM   4529 C CD  . ARG C  3 142 ? -0.94600  29.63500  -30.31600 1.000 36.27652  ? 142 ARG L CD  1 
ATOM   4530 N NE  . ARG C  3 142 ? -2.21800  29.50600  -31.00300 1.000 40.45078  ? 142 ARG L NE  1 
ATOM   4531 C CZ  . ARG C  3 142 ? -3.40000  29.70900  -30.43500 1.000 45.22406  ? 142 ARG L CZ  1 
ATOM   4532 N NH1 . ARG C  3 142 ? -3.48200  30.04400  -29.15900 1.000 47.50224  ? 142 ARG L NH1 1 
ATOM   4533 N NH2 . ARG C  3 142 ? -4.50600  29.57000  -31.14700 1.000 65.50165  ? 142 ARG L NH2 1 
ATOM   4534 N N   . GLU C  3 143 ? -0.12500  34.82600  -31.36600 1.000 19.42631  ? 143 GLU L N   1 
ATOM   4535 C CA  . GLU C  3 143 ? 0.11200   35.45400  -32.66900 1.000 24.21546  ? 143 GLU L CA  1 
ATOM   4536 C C   . GLU C  3 143 ? 1.50700   36.06700  -32.80100 1.000 18.74891  ? 143 GLU L C   1 
ATOM   4537 O O   . GLU C  3 143 ? 1.93300   36.92400  -32.00100 1.000 17.70721  ? 143 GLU L O   1 
ATOM   4538 C CB  . GLU C  3 143 ? -0.99600  36.48700  -32.96200 1.000 24.83104  ? 143 GLU L CB  1 
ATOM   4539 C CG  . GLU C  3 143 ? -2.47900  35.86000  -32.84800 1.000 32.14823  ? 143 GLU L CG  1 
ATOM   4540 C CD  . GLU C  3 143 ? -2.97100  35.48700  -31.38500 1.000 40.23210  ? 143 GLU L CD  1 
ATOM   4541 O OE1 . GLU C  3 143 ? -2.77200  36.27900  -30.43800 1.000 35.00625  ? 143 GLU L OE1 1 
ATOM   4542 O OE2 . GLU C  3 143 ? -3.51600  34.36500  -31.17400 1.000 48.06853  ? 143 GLU L OE2 1 
ATOM   4543 N N   . ALA C  3 144 ? 2.19500   35.64900  -33.87300 1.000 16.43513  ? 144 ALA L N   1 
ATOM   4544 C CA  . ALA C  3 144 ? 3.53900   36.10100  -34.18800 1.000 17.78442  ? 144 ALA L CA  1 
ATOM   4545 C C   . ALA C  3 144 ? 3.72600   35.99800  -35.69000 1.000 18.10746  ? 144 ALA L C   1 
ATOM   4546 O O   . ALA C  3 144 ? 3.09900   35.16500  -36.35400 1.000 21.79522  ? 144 ALA L O   1 
ATOM   4547 C CB  . ALA C  3 144 ? 4.60500   35.26400  -33.44200 1.000 15.33177  ? 144 ALA L CB  1 
ATOM   4548 N N   . LYS C  3 145 ? 4.57900   36.85300  -36.23200 1.000 16.68947  ? 145 LYS L N   1 
ATOM   4549 C CA  . LYS C  3 145 ? 4.94400   36.77700  -37.63900 1.000 21.28992  ? 145 LYS L CA  1 
ATOM   4550 C C   . LYS C  3 145 ? 6.42500   36.47600  -37.72100 1.000 18.65167  ? 145 LYS L C   1 
ATOM   4551 O O   . LYS C  3 145 ? 7.23600   37.15500  -37.08900 1.000 21.58455  ? 145 LYS L O   1 
ATOM   4552 C CB  . LYS C  3 145 ? 4.61700   38.07700  -38.40500 1.000 21.33390  ? 145 LYS L CB  1 
ATOM   4553 C CG  . LYS C  3 145 ? 4.79100   37.91200  -39.93900 1.000 29.53748  ? 145 LYS L CG  1 
ATOM   4554 C CD  . LYS C  3 145 ? 4.16900   39.06400  -40.71400 1.000 37.29825  ? 145 LYS L CD  1 
ATOM   4555 C CE  . LYS C  3 145 ? 5.22300   40.17700  -40.93500 1.000 45.11306  ? 145 LYS L CE  1 
ATOM   4556 N NZ  . LYS C  3 145 ? 4.68600   41.56400  -40.95100 1.000 52.53077  ? 145 LYS L NZ  1 
ATOM   4557 N N   . VAL C  3 146 ? 6.76700   35.45200  -38.48600 1.000 22.51358  ? 146 VAL L N   1 
ATOM   4558 C CA  . VAL C  3 146 ? 8.13300   34.99600  -38.64200 1.000 18.24863  ? 146 VAL L CA  1 
ATOM   4559 C C   . VAL C  3 146 ? 8.38800   34.99400  -40.14300 1.000 24.00745  ? 146 VAL L C   1 
ATOM   4560 O O   . VAL C  3 146 ? 7.65400   34.33200  -40.88200 1.000 21.47458  ? 146 VAL L O   1 
ATOM   4561 C CB  . VAL C  3 146 ? 8.32100   33.58900  -38.04800 1.000 18.45530  ? 146 VAL L CB  1 
ATOM   4562 C CG1 . VAL C  3 146 ? 9.71800   33.04800  -38.40600 1.000 23.98900  ? 146 VAL L CG1 1 
ATOM   4563 C CG2 . VAL C  3 146 ? 8.00300   33.61300  -36.57200 1.000 20.39161  ? 146 VAL L CG2 1 
ATOM   4564 N N   . GLN C  3 147 ? 9.35900   35.79100  -40.60700 1.000 21.72255  ? 147 GLN L N   1 
ATOM   4565 C CA  . GLN C  3 147 ? 9.68700   35.86900  -42.02600 1.000 20.13526  ? 147 GLN L CA  1 
ATOM   4566 C C   . GLN C  3 147 ? 11.11200  35.37600  -42.19700 1.000 19.21021  ? 147 GLN L C   1 
ATOM   4567 O O   . GLN C  3 147 ? 11.99300  35.74400  -41.41700 1.000 19.82010  ? 147 GLN L O   1 
ATOM   4568 C CB  . GLN C  3 147 ? 9.55000   37.30000  -42.53600 1.000 17.89699  ? 147 GLN L CB  1 
ATOM   4569 C CG  . GLN C  3 147 ? 8.16200   37.89400  -42.39900 1.000 24.98719  ? 147 GLN L CG  1 
ATOM   4570 C CD  . GLN C  3 147 ? 7.88100   39.02200  -43.40900 1.000 45.65961  ? 147 GLN L CD  1 
ATOM   4571 O OE1 . GLN C  3 147 ? 7.00100   38.94100  -44.27500 1.000 42.52113  ? 147 GLN L OE1 1 
ATOM   4572 N NE2 . GLN C  3 147 ? 8.61700   40.12300  -43.24000 1.000 43.64181  ? 147 GLN L NE2 1 
ATOM   4573 N N   . TRP C  3 148 ? 11.33600  34.54300  -43.20300 1.000 11.69090  ? 148 TRP L N   1 
ATOM   4574 C CA  . TRP C  3 148 ? 12.68200  34.10200  -43.54400 1.000 14.57458  ? 148 TRP L CA  1 
ATOM   4575 C C   . TRP C  3 148 ? 13.25500  35.01100  -44.62300 1.000 24.12860  ? 148 TRP L C   1 
ATOM   4576 O O   . TRP C  3 148 ? 12.54300  35.36600  -45.57500 1.000 16.32548  ? 148 TRP L O   1 
ATOM   4577 C CB  . TRP C  3 148 ? 12.61000  32.68000  -44.06700 1.000 13.52884  ? 148 TRP L CB  1 
ATOM   4578 C CG  . TRP C  3 148 ? 12.53300  31.70500  -42.98600 1.000 16.17620  ? 148 TRP L CG  1 
ATOM   4579 C CD1 . TRP C  3 148 ? 11.44400  31.00200  -42.63500 1.000 17.25337  ? 148 TRP L CD1 1 
ATOM   4580 C CD2 . TRP C  3 148 ? 13.60100  31.26400  -42.13900 1.000 16.04235  ? 148 TRP L CD2 1 
ATOM   4581 N NE1 . TRP C  3 148 ? 11.74900  30.13700  -41.60800 1.000 16.26172  ? 148 TRP L NE1 1 
ATOM   4582 C CE2 . TRP C  3 148 ? 13.06100  30.28800  -41.26700 1.000 16.76331  ? 148 TRP L CE2 1 
ATOM   4583 C CE3 . TRP C  3 148 ? 14.96700  31.61100  -42.01700 1.000 17.08682  ? 148 TRP L CE3 1 
ATOM   4584 C CZ2 . TRP C  3 148 ? 13.83000  29.61900  -40.31000 1.000 16.48080  ? 148 TRP L CZ2 1 
ATOM   4585 C CZ3 . TRP C  3 148 ? 15.74600  30.94300  -41.03900 1.000 19.06974  ? 148 TRP L CZ3 1 
ATOM   4586 C CH2 . TRP C  3 148 ? 15.16300  29.97800  -40.19900 1.000 18.40382  ? 148 TRP L CH2 1 
ATOM   4587 N N   . LYS C  3 149 ? 14.54000  35.37500  -44.49000 1.000 17.85047  ? 149 LYS L N   1 
ATOM   4588 C CA  . LYS C  3 149 ? 15.21800  36.15900  -45.52400 1.000 19.19621  ? 149 LYS L CA  1 
ATOM   4589 C C   . LYS C  3 149 ? 16.54400  35.47200  -45.83000 1.000 24.52466  ? 149 LYS L C   1 
ATOM   4590 O O   . LYS C  3 149 ? 17.26400  35.08300  -44.91100 1.000 24.64636  ? 149 LYS L O   1 
ATOM   4591 C CB  . LYS C  3 149 ? 15.40500  37.61300  -45.05400 1.000 20.60468  ? 149 LYS L CB  1 
ATOM   4592 C CG  . LYS C  3 149 ? 14.17600  38.46800  -45.31900 1.000 27.12129  ? 149 LYS L CG  1 
ATOM   4593 C CD  . LYS C  3 149 ? 13.88800  39.50400  -44.24800 1.000 37.54429  ? 149 LYS L CD  1 
ATOM   4594 C CE  . LYS C  3 149 ? 14.40100  40.91700  -44.41800 1.000 47.72463  ? 149 LYS L CE  1 
ATOM   4595 N NZ  . LYS C  3 149 ? 13.22300  41.83100  -44.07000 1.000 43.88564  ? 149 LYS L NZ  1 
ATOM   4596 N N   . VAL C  3 150 ? 16.82300  35.23900  -47.10800 1.000 19.44660  ? 150 VAL L N   1 
ATOM   4597 C CA  . VAL C  3 150 ? 18.05800  34.59900  -47.57400 1.000 17.01356  ? 150 VAL L CA  1 
ATOM   4598 C C   . VAL C  3 150 ? 18.73200  35.59400  -48.48800 1.000 28.15211  ? 150 VAL L C   1 
ATOM   4599 O O   . VAL C  3 150 ? 18.13600  36.00100  -49.50200 1.000 20.97074  ? 150 VAL L O   1 
ATOM   4600 C CB  . VAL C  3 150 ? 17.78700  33.26400  -48.29900 1.000 20.02889  ? 150 VAL L CB  1 
ATOM   4601 C CG1 . VAL C  3 150 ? 19.08800  32.50600  -48.53900 1.000 22.67513  ? 150 VAL L CG1 1 
ATOM   4602 C CG2 . VAL C  3 150 ? 16.92800  32.35900  -47.40700 1.000 19.86861  ? 150 VAL L CG2 1 
ATOM   4603 N N   . ASP C  3 151 ? 19.94300  36.01400  -48.11500 1.000 24.72926  ? 151 ASP L N   1 
ATOM   4604 C CA  . ASP C  3 151 ? 20.62100  37.10600  -48.80500 1.000 26.68786  ? 151 ASP L CA  1 
ATOM   4605 C C   . ASP C  3 151 ? 19.65800  38.25100  -48.97600 1.000 28.71211  ? 151 ASP L C   1 
ATOM   4606 O O   . ASP C  3 151 ? 19.53800  38.83600  -50.06600 1.000 25.36154  ? 151 ASP L O   1 
ATOM   4607 C CB  . ASP C  3 151 ? 21.18600  36.69300  -50.16200 1.000 26.67451  ? 151 ASP L CB  1 
ATOM   4608 C CG  . ASP C  3 151 ? 22.38600  35.82600  -50.01900 1.000 23.90435  ? 151 ASP L CG  1 
ATOM   4609 O OD1 . ASP C  3 151 ? 23.06500  36.03800  -49.02300 1.000 30.27959  ? 151 ASP L OD1 1 
ATOM   4610 O OD2 . ASP C  3 151 ? 22.69600  35.01100  -50.91700 1.000 35.95553  ? 151 ASP L OD2 1 
ATOM   4611 N N   . ASN C  3 152 ? 18.94800  38.61500  -47.92900 1.000 21.92166  ? 152 ASN L N   1 
ATOM   4612 C CA  A ASN C  3 152 ? 18.01800  39.74300  -47.95700 0.522 20.59690  ? 152 ASN L CA  1 
ATOM   4613 C CA  B ASN C  3 152 ? 18.01800  39.74800  -47.96200 0.478 20.60907  ? 152 ASN L CA  1 
ATOM   4614 C C   . ASN C  3 152 ? 16.76900  39.62100  -48.89100 1.000 18.76900  ? 152 ASN L C   1 
ATOM   4615 O O   . ASN C  3 152 ? 15.99300  40.54200  -49.16500 1.000 26.20804  ? 152 ASN L O   1 
ATOM   4616 C CB  A ASN C  3 152 ? 18.77000  41.05500  -48.20900 0.522 23.24097  ? 152 ASN L CB  1 
ATOM   4617 C CB  B ASN C  3 152 ? 18.77400  41.05200  -48.23800 0.478 23.24880  ? 152 ASN L CB  1 
ATOM   4618 C CG  A ASN C  3 152 ? 18.30200  42.17100  -47.29900 0.522 24.99755  ? 152 ASN L CG  1 
ATOM   4619 C CG  B ASN C  3 152 ? 20.00700  41.19900  -47.37500 0.478 23.12475  ? 152 ASN L CG  1 
ATOM   4620 O OD1 A ASN C  3 152 ? 17.88900  41.93100  -46.16600 0.522 28.41205  ? 152 ASN L OD1 1 
ATOM   4621 O OD1 B ASN C  3 152 ? 19.91300  41.52000  -46.19300 0.478 26.82310  ? 152 ASN L OD1 1 
ATOM   4622 N ND2 A ASN C  3 152 ? 18.35800  43.40000  -47.79400 0.522 29.19260  ? 152 ASN L ND2 1 
ATOM   4623 N ND2 B ASN C  3 152 ? 21.17300  40.95500  -47.96000 0.478 20.90424  ? 152 ASN L ND2 1 
ATOM   4624 N N   . ALA C  3 153 ? 16.55300  38.39400  -49.34200 1.000 22.55630  ? 153 ALA L N   1 
ATOM   4625 C CA  . ALA C  3 153 ? 15.33600  38.18500  -50.11400 1.000 20.03442  ? 153 ALA L CA  1 
ATOM   4626 C C   . ALA C  3 153 ? 14.29500  37.43800  -49.27100 1.000 19.66467  ? 153 ALA L C   1 
ATOM   4627 O O   . ALA C  3 153 ? 14.57500  36.36100  -48.72500 1.000 15.84837  ? 153 ALA L O   1 
ATOM   4628 C CB  . ALA C  3 153 ? 15.64600  37.40500  -51.40600 1.000 18.47557  ? 153 ALA L CB  1 
ATOM   4629 N N   . LEU C  3 154 ? 13.07800  37.98200  -49.21500 1.000 18.59775  ? 154 LEU L N   1 
ATOM   4630 C CA  . LEU C  3 154 ? 11.96300  37.34200  -48.51400 1.000 17.96981  ? 154 LEU L CA  1 
ATOM   4631 C C   . LEU C  3 154 ? 11.59500  36.00500  -49.14600 1.000 20.80864  ? 154 LEU L C   1 
ATOM   4632 O O   . LEU C  3 154 ? 11.43000  35.91000  -50.35700 1.000 24.59264  ? 154 LEU L O   1 
ATOM   4633 C CB  . LEU C  3 154 ? 10.75700  38.29100  -48.50600 1.000 30.80168  ? 154 LEU L CB  1 
ATOM   4634 C CG  . LEU C  3 154 ? 10.24000  38.72400  -47.13400 1.000 36.80553  ? 154 LEU L CG  1 
ATOM   4635 C CD1 . LEU C  3 154 ? 8.90600   39.47100  -47.25900 1.000 39.21867  ? 154 LEU L CD1 1 
ATOM   4636 C CD2 . LEU C  3 154 ? 10.01200  37.48700  -46.29400 1.000 38.05771  ? 154 LEU L CD2 1 
ATOM   4637 N N   . GLN C  3 155 ? 11.49900  34.95300  -48.33600 1.000 16.10118  ? 155 GLN L N   1 
ATOM   4638 C CA  . GLN C  3 155 ? 11.09500  33.63200  -48.80300 1.000 16.60240  ? 155 GLN L CA  1 
ATOM   4639 C C   . GLN C  3 155 ? 9.58700   33.47200  -48.71900 1.000 22.90404  ? 155 GLN L C   1 
ATOM   4640 O O   . GLN C  3 155 ? 8.92200   34.12900  -47.93200 1.000 18.91113  ? 155 GLN L O   1 
ATOM   4641 C CB  . GLN C  3 155 ? 11.74800  32.52300  -47.96500 1.000 15.42892  ? 155 GLN L CB  1 
ATOM   4642 C CG  . GLN C  3 155 ? 13.24900  32.62700  -47.83700 1.000 14.56001  ? 155 GLN L CG  1 
ATOM   4643 C CD  . GLN C  3 155 ? 13.88100  32.47800  -49.19900 1.000 16.32829  ? 155 GLN L CD  1 
ATOM   4644 O OE1 . GLN C  3 155 ? 13.87800  31.36500  -49.77300 1.000 16.58349  ? 155 GLN L OE1 1 
ATOM   4645 N NE2 . GLN C  3 155 ? 14.42100  33.55900  -49.73000 1.000 10.12250  ? 155 GLN L NE2 1 
ATOM   4646 N N   . SER C  3 156 ? 9.05100   32.54000  -49.48600 1.000 16.64711  ? 156 SER L N   1 
ATOM   4647 C CA  . SER C  3 156 ? 7.69300   32.13100  -49.16500 1.000 19.64867  ? 156 SER L CA  1 
ATOM   4648 C C   . SER C  3 156 ? 7.38900   30.76200  -49.76800 1.000 19.90183  ? 156 SER L C   1 
ATOM   4649 O O   . SER C  3 156 ? 7.90800   30.38000  -50.82900 1.000 23.36251  ? 156 SER L O   1 
ATOM   4650 C CB  . SER C  3 156 ? 6.66400   33.18200  -49.61100 1.000 28.12638  ? 156 SER L CB  1 
ATOM   4651 O OG  . SER C  3 156 ? 6.16000   32.83300  -50.88600 1.000 38.12469  ? 156 SER L OG  1 
ATOM   4652 N N   . GLY C  3 157 ? 6.57900   30.00800  -49.04700 1.000 17.47695  ? 157 GLY L N   1 
ATOM   4653 C CA  . GLY C  3 157 ? 6.16900   28.67400  -49.43900 1.000 14.59102  ? 157 GLY L CA  1 
ATOM   4654 C C   . GLY C  3 157 ? 7.16000   27.56900  -49.15600 1.000 20.38460  ? 157 GLY L C   1 
ATOM   4655 O O   . GLY C  3 157 ? 6.88700   26.41400  -49.49800 1.000 21.84705  ? 157 GLY L O   1 
ATOM   4656 N N   . ASN C  3 158 ? 8.32100   27.88000  -48.57900 1.000 19.58724  ? 158 ASN L N   1 
ATOM   4657 C CA  . ASN C  3 158 ? 9.36200   26.89000  -48.30900 1.000 22.37120  ? 158 ASN L CA  1 
ATOM   4658 C C   . ASN C  3 158 ? 9.61000   26.74800  -46.80200 1.000 24.53685  ? 158 ASN L C   1 
ATOM   4659 O O   . ASN C  3 158 ? 10.67800  26.27100  -46.37200 1.000 18.03702  ? 158 ASN L O   1 
ATOM   4660 C CB  . ASN C  3 158 ? 10.66900  27.22900  -49.07600 1.000 16.82716  ? 158 ASN L CB  1 
ATOM   4661 C CG  . ASN C  3 158 ? 11.11700  28.70500  -48.91800 1.000 18.59540  ? 158 ASN L CG  1 
ATOM   4662 O OD1 . ASN C  3 158 ? 10.48600  29.49200  -48.21400 1.000 16.38286  ? 158 ASN L OD1 1 
ATOM   4663 N ND2 . ASN C  3 158 ? 12.22500  29.08000  -49.59200 1.000 17.66477  ? 158 ASN L ND2 1 
ATOM   4664 N N   . SER C  3 159 ? 8.64200   27.15100  -45.97700 1.000 20.18132  ? 159 SER L N   1 
ATOM   4665 C CA  . SER C  3 159 ? 8.80100   27.02800  -44.53500 1.000 20.37793  ? 159 SER L CA  1 
ATOM   4666 C C   . SER C  3 159 ? 7.50600   26.51500  -43.90900 1.000 17.27683  ? 159 SER L C   1 
ATOM   4667 O O   . SER C  3 159 ? 6.42700   26.58700  -44.50500 1.000 15.26813  ? 159 SER L O   1 
ATOM   4668 C CB  . SER C  3 159 ? 9.26000   28.35400  -43.91600 1.000 14.94841  ? 159 SER L CB  1 
ATOM   4669 O OG  . SER C  3 159 ? 8.24300   29.33900  -44.00300 1.000 19.10255  ? 159 SER L OG  1 
ATOM   4670 N N   . GLN C  3 160 ? 7.65400   25.92400  -42.71300 1.000 18.54833  ? 160 GLN L N   1 
ATOM   4671 C CA  . GLN C  3 160 ? 6.55800   25.32400  -41.95500 1.000 17.94094  ? 160 GLN L CA  1 
ATOM   4672 C C   . GLN C  3 160 ? 6.75800   25.67800  -40.48400 1.000 15.91446  ? 160 GLN L C   1 
ATOM   4673 O O   . GLN C  3 160 ? 7.88700   25.63000  -39.95300 1.000 18.01473  ? 160 GLN L O   1 
ATOM   4674 C CB  . GLN C  3 160 ? 6.53100   23.81300  -42.15700 1.000 17.35111  ? 160 GLN L CB  1 
ATOM   4675 C CG  . GLN C  3 160 ? 5.93500   23.38300  -43.49700 1.000 17.22802  ? 160 GLN L CG  1 
ATOM   4676 C CD  . GLN C  3 160 ? 5.85800   21.88100  -43.58500 1.000 23.34975  ? 160 GLN L CD  1 
ATOM   4677 O OE1 . GLN C  3 160 ? 6.87000   21.16900  -43.44300 1.000 21.79076  ? 160 GLN L OE1 1 
ATOM   4678 N NE2 . GLN C  3 160 ? 4.64300   21.38100  -43.64400 1.000 24.38974  ? 160 GLN L NE2 1 
ATOM   4679 N N   . GLU C  3 161 ? 5.66000   26.03500  -39.83200 1.000 16.54126  ? 161 GLU L N   1 
ATOM   4680 C CA  . GLU C  3 161 ? 5.66800   26.39600  -38.41800 1.000 18.40480  ? 161 GLU L CA  1 
ATOM   4681 C C   . GLU C  3 161 ? 4.99600   25.35600  -37.55800 1.000 15.09118  ? 161 GLU L C   1 
ATOM   4682 O O   . GLU C  3 161 ? 4.10100   24.64600  -38.00300 1.000 14.85248  ? 161 GLU L O   1 
ATOM   4683 C CB  . GLU C  3 161 ? 5.00000   27.76300  -38.15300 1.000 15.26211  ? 161 GLU L CB  1 
ATOM   4684 C CG  . GLU C  3 161 ? 5.76600   28.97200  -38.71300 1.000 20.54931  ? 161 GLU L CG  1 
ATOM   4685 C CD  . GLU C  3 161 ? 5.02100   30.29100  -38.48500 1.000 25.87330  ? 161 GLU L CD  1 
ATOM   4686 O OE1 . GLU C  3 161 ? 3.89900   30.23000  -37.90900 1.000 28.47205  ? 161 GLU L OE1 1 
ATOM   4687 O OE2 . GLU C  3 161 ? 5.42600   31.35400  -39.04000 1.000 28.23363  ? 161 GLU L OE2 1 
ATOM   4688 N N   . SER C  3 162 ? 5.41100   25.32500  -36.29100 1.000 16.57212  ? 162 SER L N   1 
ATOM   4689 C CA  . SER C  3 162 ? 4.72800   24.49300  -35.31700 1.000 17.05742  ? 162 SER L CA  1 
ATOM   4690 C C   . SER C  3 162 ? 4.78200   25.20600  -33.97600 1.000 15.87818  ? 162 SER L C   1 
ATOM   4691 O O   . SER C  3 162 ? 5.77500   25.89100  -33.65300 1.000 14.35369  ? 162 SER L O   1 
ATOM   4692 C CB  . SER C  3 162 ? 5.37500   23.09800  -35.27700 1.000 21.22915  ? 162 SER L CB  1 
ATOM   4693 O OG  . SER C  3 162 ? 5.31400   22.42000  -34.05600 1.000 21.89710  ? 162 SER L OG  1 
ATOM   4694 N N   . VAL C  3 163 ? 3.69500   25.06900  -33.24200 1.000 18.28037  ? 163 VAL L N   1 
ATOM   4695 C CA  . VAL C  3 163 ? 3.57100   25.74300  -31.96600 1.000 22.36790  ? 163 VAL L CA  1 
ATOM   4696 C C   . VAL C  3 163 ? 3.25700   24.78600  -30.84000 1.000 16.01310  ? 163 VAL L C   1 
ATOM   4697 O O   . VAL C  3 163 ? 2.47000   23.89200  -31.00100 1.000 16.49286  ? 163 VAL L O   1 
ATOM   4698 C CB  . VAL C  3 163 ? 2.46800   26.79800  -32.01800 1.000 23.09275  ? 163 VAL L CB  1 
ATOM   4699 C CG1 . VAL C  3 163 ? 2.57900   27.75400  -30.84500 1.000 24.46861  ? 163 VAL L CG1 1 
ATOM   4700 C CG2 . VAL C  3 163 ? 2.49800   27.54900  -33.33400 1.000 33.75178  ? 163 VAL L CG2 1 
ATOM   4701 N N   . THR C  3 164 ? 3.89500   24.99700  -29.70400 1.000 15.52052  ? 164 THR L N   1 
ATOM   4702 C CA  . THR C  3 164 ? 3.57500   24.16900  -28.55100 1.000 16.86335  ? 164 THR L CA  1 
ATOM   4703 C C   . THR C  3 164 ? 2.24500   24.59900  -27.94200 1.000 22.30076  ? 164 THR L C   1 
ATOM   4704 O O   . THR C  3 164 ? 1.67000   25.63900  -28.29300 1.000 23.19593  ? 164 THR L O   1 
ATOM   4705 C CB  . THR C  3 164 ? 4.67900   24.24800  -27.50800 1.000 18.94807  ? 164 THR L CB  1 
ATOM   4706 O OG1 . THR C  3 164 ? 4.80500   25.62700  -27.10100 1.000 24.60191  ? 164 THR L OG1 1 
ATOM   4707 C CG2 . THR C  3 164 ? 6.03000   23.68700  -28.06300 1.000 18.22796  ? 164 THR L CG2 1 
ATOM   4708 N N   . GLU C  3 165 ? 1.71700   23.74400  -27.07000 1.000 24.00462  ? 165 GLU L N   1 
ATOM   4709 C CA  . GLU C  3 165 ? 0.55300   24.10800  -26.27900 1.000 17.33851  ? 165 GLU L CA  1 
ATOM   4710 C C   . GLU C  3 165 ? 1.00300   25.00300  -25.13400 1.000 18.75555  ? 165 GLU L C   1 
ATOM   4711 O O   . GLU C  3 165 ? 2.19100   25.04000  -24.77600 1.000 20.47854  ? 165 GLU L O   1 
ATOM   4712 C CB  . GLU C  3 165 ? -0.13600  22.84300  -25.74600 1.000 24.68120  ? 165 GLU L CB  1 
ATOM   4713 C CG  . GLU C  3 165 ? -0.75300  22.05500  -26.90300 1.000 30.88826  ? 165 GLU L CG  1 
ATOM   4714 C CD  . GLU C  3 165 ? -1.83300  22.87200  -27.60300 1.000 42.61971  ? 165 GLU L CD  1 
ATOM   4715 O OE1 . GLU C  3 165 ? -2.64100  23.53300  -26.90900 1.000 33.82170  ? 165 GLU L OE1 1 
ATOM   4716 O OE2 . GLU C  3 165 ? -1.93000  22.78500  -28.85800 1.000 53.63401  ? 165 GLU L OE2 1 
ATOM   4717 N N   . GLN C  3 166 ? 0.05100   25.73200  -24.56100 1.000 18.78327  ? 166 GLN L N   1 
ATOM   4718 C CA  . GLN C  3 166 ? 0.37200   26.70300  -23.52200 1.000 20.58541  ? 166 GLN L CA  1 
ATOM   4719 C C   . GLN C  3 166 ? 1.12800   26.07300  -22.36700 1.000 19.82181  ? 166 GLN L C   1 
ATOM   4720 O O   . GLN C  3 166 ? 0.71600   25.04500  -21.83100 1.000 20.04094  ? 166 GLN L O   1 
ATOM   4721 C CB  . GLN C  3 166 ? -0.90600  27.34800  -23.00200 1.000 16.53207  ? 166 GLN L CB  1 
ATOM   4722 C CG  . GLN C  3 166 ? -0.75600  28.79900  -22.90400 1.000 27.84604  ? 166 GLN L CG  1 
ATOM   4723 C CD  . GLN C  3 166 ? -1.96600  29.51200  -22.36300 1.000 27.17909  ? 166 GLN L CD  1 
ATOM   4724 O OE1 . GLN C  3 166 ? -3.07100  28.93300  -22.22500 1.000 19.13539  ? 166 GLN L OE1 1 
ATOM   4725 N NE2 . GLN C  3 166 ? -1.80600  30.83400  -22.20000 1.000 19.24950  ? 166 GLN L NE2 1 
ATOM   4726 N N   . ASP C  3 167 ? 2.20700   26.72700  -21.94400 1.000 20.90847  ? 167 ASP L N   1 
ATOM   4727 C CA  . ASP C  3 167 ? 3.04300   26.17200  -20.85200 1.000 21.77148  ? 167 ASP L CA  1 
ATOM   4728 C C   . ASP C  3 167 ? 2.26000   26.12900  -19.53200 1.000 29.38867  ? 167 ASP L C   1 
ATOM   4729 O O   . ASP C  3 167 ? 1.49500   27.05300  -19.29000 1.000 24.02806  ? 167 ASP L O   1 
ATOM   4730 C CB  . ASP C  3 167 ? 4.37200   26.90500  -20.71600 1.000 20.83075  ? 167 ASP L CB  1 
ATOM   4731 C CG  . ASP C  3 167 ? 5.25700   26.35800  -19.61200 1.000 27.98695  ? 167 ASP L CG  1 
ATOM   4732 O OD1 . ASP C  3 167 ? 5.13500   26.84100  -18.48100 1.000 28.58881  ? 167 ASP L OD1 1 
ATOM   4733 O OD2 . ASP C  3 167 ? 6.05900   25.46100  -19.90100 1.000 24.93974  ? 167 ASP L OD2 1 
ATOM   4734 N N   . SER C  3 168 ? 2.50300   25.10000  -18.71300 1.000 25.21163  ? 168 SER L N   1 
ATOM   4735 C CA  . SER C  3 168 ? 1.78700   24.89800  -17.42600 1.000 35.41056  ? 168 SER L CA  1 
ATOM   4736 C C   . SER C  3 168 ? 2.19200   25.93700  -16.37300 1.000 30.56827  ? 168 SER L C   1 
ATOM   4737 O O   . SER C  3 168 ? 1.36000   26.26400  -15.52200 1.000 34.28009  ? 168 SER L O   1 
ATOM   4738 C CB  . SER C  3 168 ? 2.04300   23.47300  -16.91800 1.000 38.67189  ? 168 SER L CB  1 
ATOM   4739 O OG  . SER C  3 168 ? 3.42600   23.16600  -16.91500 1.000 37.14333  ? 168 SER L OG  1 
ATOM   4740 N N   . LYS C  3 169 ? 3.42300   26.38200  -16.41000 1.000 22.77439  ? 169 LYS L N   1 
ATOM   4741 C CA  . LYS C  3 169 ? 3.89700   27.29200  -15.39600 1.000 26.44154  ? 169 LYS L CA  1 
ATOM   4742 C C   . LYS C  3 169 ? 3.79800   28.75000  -15.76700 1.000 30.69867  ? 169 LYS L C   1 
ATOM   4743 O O   . LYS C  3 169 ? 3.43900   29.55100  -14.92700 1.000 24.64870  ? 169 LYS L O   1 
ATOM   4744 C CB  . LYS C  3 169 ? 5.35700   27.00400  -15.05900 1.000 32.10127  ? 169 LYS L CB  1 
ATOM   4745 C CG  . LYS C  3 169 ? 5.73300   25.53900  -14.98700 1.000 49.41715  ? 169 LYS L CG  1 
ATOM   4746 C CD  . LYS C  3 169 ? 7.24300   25.36700  -14.96800 1.000 55.58108  ? 169 LYS L CD  1 
ATOM   4747 C CE  . LYS C  3 169 ? 7.72400   24.57700  -16.17300 1.000 52.10467  ? 169 LYS L CE  1 
ATOM   4748 N NZ  . LYS C  3 169 ? 9.16500   24.79500  -16.46100 1.000 54.93677  ? 169 LYS L NZ  1 
ATOM   4749 N N   . ASP C  3 170 ? 4.09600   29.09300  -17.01900 1.000 23.16131  ? 170 ASP L N   1 
ATOM   4750 C CA  . ASP C  3 170 ? 4.14700   30.52900  -17.41100 1.000 19.73691  ? 170 ASP L CA  1 
ATOM   4751 C C   . ASP C  3 170 ? 3.03900   30.91400  -18.41000 1.000 18.92856  ? 170 ASP L C   1 
ATOM   4752 O O   . ASP C  3 170 ? 2.95300   32.08800  -18.72100 1.000 18.49257  ? 170 ASP L O   1 
ATOM   4753 C CB  . ASP C  3 170 ? 5.58000   30.91300  -17.79800 1.000 24.28031  ? 170 ASP L CB  1 
ATOM   4754 C CG  . ASP C  3 170 ? 6.03600   30.40600  -19.14700 1.000 25.84708  ? 170 ASP L CG  1 
ATOM   4755 O OD1 . ASP C  3 170 ? 5.26100   29.68800  -19.79100 1.000 22.42225  ? 170 ASP L OD1 1 
ATOM   4756 O OD2 . ASP C  3 170 ? 7.16200   30.75100  -19.53500 1.000 29.98209  ? 170 ASP L OD2 1 
ATOM   4757 N N   . SER C  3 171 ? 2.21700   29.95500  -18.83600 1.000 20.82784  ? 171 SER L N   1 
ATOM   4758 C CA  . SER C  3 171 ? 1.07000   30.22700  -19.74100 1.000 15.99143  ? 171 SER L CA  1 
ATOM   4759 C C   . SER C  3 171 ? 1.57600   30.82800  -21.06600 1.000 19.76830  ? 171 SER L C   1 
ATOM   4760 O O   . SER C  3 171 ? 0.80200   31.45400  -21.76000 1.000 16.46827  ? 171 SER L O   1 
ATOM   4761 C CB  . SER C  3 171 ? 0.01000   31.02200  -19.03400 1.000 15.18446  ? 171 SER L CB  1 
ATOM   4762 O OG  . SER C  3 171 ? -0.51700  30.30600  -17.93800 1.000 21.70644  ? 171 SER L OG  1 
ATOM   4763 N N   . THR C  3 172 ? 2.84600   30.58500  -21.38500 1.000 15.35859  ? 172 THR L N   1 
ATOM   4764 C CA  . THR C  3 172 ? 3.43700   31.04100  -22.67100 1.000 14.40222  ? 172 THR L CA  1 
ATOM   4765 C C   . THR C  3 172 ? 3.35800   29.99500  -23.78800 1.000 20.12482  ? 172 THR L C   1 
ATOM   4766 O O   . THR C  3 172 ? 3.01800   28.84600  -23.50000 1.000 13.72303  ? 172 THR L O   1 
ATOM   4767 C CB  . THR C  3 172 ? 4.93100   31.37200  -22.52700 1.000 18.99462  ? 172 THR L CB  1 
ATOM   4768 O OG1 . THR C  3 172 ? 5.68000   30.22200  -22.14300 1.000 18.31822  ? 172 THR L OG1 1 
ATOM   4769 C CG2 . THR C  3 172 ? 5.16500   32.50200  -21.54500 1.000 17.98726  ? 172 THR L CG2 1 
ATOM   4770 N N   . TYR C  3 173 ? 3.63700   30.42300  -25.01900 1.000 13.65875  ? 173 TYR L N   1 
ATOM   4771 C CA  . TYR C  3 173 ? 3.72500   29.54000  -26.17200 1.000 15.09060  ? 173 TYR L CA  1 
ATOM   4772 C C   . TYR C  3 173 ? 5.15600   29.56900  -26.67900 1.000 17.79548  ? 173 TYR L C   1 
ATOM   4773 O O   . TYR C  3 173 ? 5.88500   30.53900  -26.45200 1.000 12.09164  ? 173 TYR L O   1 
ATOM   4774 C CB  . TYR C  3 173 ? 2.80400   29.98300  -27.30100 1.000 13.87894  ? 173 TYR L CB  1 
ATOM   4775 C CG  . TYR C  3 173 ? 1.35400   29.94800  -26.94300 1.000 15.25872  ? 173 TYR L CG  1 
ATOM   4776 C CD1 . TYR C  3 173 ? 0.59900   28.78700  -27.07500 1.000 20.80332  ? 173 TYR L CD1 1 
ATOM   4777 C CD2 . TYR C  3 173 ? 0.72500   31.09000  -26.46400 1.000 17.06035  ? 173 TYR L CD2 1 
ATOM   4778 C CE1 . TYR C  3 173 ? -0.74400  28.77700  -26.72500 1.000 23.32908  ? 173 TYR L CE1 1 
ATOM   4779 C CE2 . TYR C  3 173 ? -0.58600  31.08400  -26.11600 1.000 19.40106  ? 173 TYR L CE2 1 
ATOM   4780 C CZ  . TYR C  3 173 ? -1.32400  29.93900  -26.24400 1.000 26.91813  ? 173 TYR L CZ  1 
ATOM   4781 O OH  . TYR C  3 173 ? -2.66800  29.98100  -25.87600 1.000 23.52211  ? 173 TYR L OH  1 
ATOM   4782 N N   . SER C  3 174 ? 5.57100   28.49700  -27.35200 1.000 13.19747  ? 174 SER L N   1 
ATOM   4783 C CA  . SER C  3 174 ? 6.85700   28.51100  -28.04500 1.000 13.43127  ? 174 SER L CA  1 
ATOM   4784 C C   . SER C  3 174 ? 6.58900   28.09200  -29.48800 1.000 16.44054  ? 174 SER L C   1 
ATOM   4785 O O   . SER C  3 174 ? 5.55800   27.46600  -29.79200 1.000 13.44394  ? 174 SER L O   1 
ATOM   4786 C CB  . SER C  3 174 ? 7.88300   27.61600  -27.32700 1.000 14.62487  ? 174 SER L CB  1 
ATOM   4787 O OG  . SER C  3 174 ? 8.40500   28.26700  -26.16200 1.000 16.55507  ? 174 SER L OG  1 
ATOM   4788 N N   . LEU C  3 175 ? 7.45300   28.51000  -30.38900 1.000 17.12027  ? 175 LEU L N   1 
ATOM   4789 C CA  . LEU C  3 175 ? 7.22300   28.25800  -31.80000 1.000 15.60470  ? 175 LEU L CA  1 
ATOM   4790 C C   . LEU C  3 175 ? 8.47400   28.06900  -32.61100 1.000 17.16381  ? 175 LEU L C   1 
ATOM   4791 O O   . LEU C  3 175 ? 9.47600   28.71000  -32.36800 1.000 13.43829  ? 175 LEU L O   1 
ATOM   4792 C CB  . LEU C  3 175 ? 6.42000   29.39700  -32.40700 1.000 16.09018  ? 175 LEU L CB  1 
ATOM   4793 C CG  . LEU C  3 175 ? 6.11600   29.39900  -33.91000 1.000 21.07419  ? 175 LEU L CG  1 
ATOM   4794 C CD1 . LEU C  3 175 ? 4.79400   30.09000  -34.17400 1.000 20.89433  ? 175 LEU L CD1 1 
ATOM   4795 C CD2 . LEU C  3 175 ? 7.21300   30.05700  -34.73000 1.000 19.13229  ? 175 LEU L CD2 1 
ATOM   4796 N N   . SER C  3 176 ? 8.37300   27.15500  -33.56100 1.000 19.04355  ? 176 SER L N   1 
ATOM   4797 C CA  . SER C  3 176 ? 9.48600   26.93300  -34.47900 1.000 17.04497  ? 176 SER L CA  1 
ATOM   4798 C C   . SER C  3 176 ? 9.04300   27.23000  -35.90400 1.000 17.17503  ? 176 SER L C   1 
ATOM   4799 O O   . SER C  3 176 ? 7.89300   26.98200  -36.26500 1.000 16.59764  ? 176 SER L O   1 
ATOM   4800 C CB  . SER C  3 176 ? 10.01000  25.49400  -34.34900 1.000 16.87198  ? 176 SER L CB  1 
ATOM   4801 O OG  . SER C  3 176 ? 9.18400   24.65500  -35.11400 1.000 18.09383  ? 176 SER L OG  1 
ATOM   4802 N N   . SER C  3 177 ? 9.96800   27.77600  -36.70600 1.000 16.33139  ? 177 SER L N   1 
ATOM   4803 C CA  . SER C  3 177 ? 9.83100   27.88900  -38.16700 1.000 13.84741  ? 177 SER L CA  1 
ATOM   4804 C C   . SER C  3 177 ? 11.02800  27.21200  -38.82400 1.000 18.53334  ? 177 SER L C   1 
ATOM   4805 O O   . SER C  3 177 ? 12.18100  27.58400  -38.55900 1.000 20.96777  ? 177 SER L O   1 
ATOM   4806 C CB  . SER C  3 177 ? 9.72900   29.35400  -38.62900 1.000 15.84574  ? 177 SER L CB  1 
ATOM   4807 O OG  . SER C  3 177 ? 9.34500   29.42100  -40.01400 1.000 17.28477  ? 177 SER L OG  1 
ATOM   4808 N N   . THR C  3 178 ? 10.75700  26.20300  -39.63900 1.000 14.93024  ? 178 THR L N   1 
ATOM   4809 C CA  . THR C  3 178 ? 11.77700  25.49700  -40.41600 1.000 14.54247  ? 178 THR L CA  1 
ATOM   4810 C C   . THR C  3 178 ? 11.75300  25.82500  -41.90500 1.000 23.08043  ? 178 THR L C   1 
ATOM   4811 O O   . THR C  3 178 ? 10.80100  25.46800  -42.60800 1.000 14.37800  ? 178 THR L O   1 
ATOM   4812 C CB  . THR C  3 178 ? 11.63100  24.00000  -40.20700 1.000 19.93771  ? 178 THR L CB  1 
ATOM   4813 O OG1 . THR C  3 178 ? 11.41300  23.79600  -38.82400 1.000 18.16166  ? 178 THR L OG1 1 
ATOM   4814 C CG2 . THR C  3 178 ? 12.81400  23.20300  -40.74100 1.000 17.59613  ? 178 THR L CG2 1 
ATOM   4815 N N   . LEU C  3 179 ? 12.87300  26.38300  -42.38600 1.000 19.13678  ? 179 LEU L N   1 
ATOM   4816 C CA  . LEU C  3 179 ? 13.10200  26.68400  -43.79900 1.000 16.19999  ? 179 LEU L CA  1 
ATOM   4817 C C   . LEU C  3 179 ? 13.82800  25.51700  -44.47000 1.000 21.90533  ? 179 LEU L C   1 
ATOM   4818 O O   . LEU C  3 179 ? 14.90000  25.09700  -44.00500 1.000 20.52964  ? 179 LEU L O   1 
ATOM   4819 C CB  . LEU C  3 179 ? 13.91700  27.97700  -43.91300 1.000 16.56261  ? 179 LEU L CB  1 
ATOM   4820 C CG  . LEU C  3 179 ? 14.29800  28.41000  -45.32200 1.000 17.35437  ? 179 LEU L CG  1 
ATOM   4821 C CD1 . LEU C  3 179 ? 13.06600  29.00500  -45.99200 1.000 16.12025  ? 179 LEU L CD1 1 
ATOM   4822 C CD2 . LEU C  3 179 ? 15.40100  29.45700  -45.14300 1.000 14.45142  ? 179 LEU L CD2 1 
ATOM   4823 N N   . THR C  3 180 ? 13.24900  25.02000  -45.53600 1.000 19.94807  ? 180 THR L N   1 
ATOM   4824 C CA  . THR C  3 180 ? 13.83400  23.87900  -46.20600 1.000 22.17466  ? 180 THR L CA  1 
ATOM   4825 C C   . THR C  3 180 ? 14.38800  24.24900  -47.58800 1.000 27.88282  ? 180 THR L C   1 
ATOM   4826 O O   . THR C  3 180 ? 13.70500  24.84900  -48.39100 1.000 21.69782  ? 180 THR L O   1 
ATOM   4827 C CB  . THR C  3 180 ? 12.83300  22.70800  -46.27900 1.000 22.88227  ? 180 THR L CB  1 
ATOM   4828 O OG1 . THR C  3 180 ? 12.66800  22.13500  -44.98700 1.000 28.12879  ? 180 THR L OG1 1 
ATOM   4829 C CG2 . THR C  3 180 ? 13.31800  21.64600  -47.25700 1.000 25.28240  ? 180 THR L CG2 1 
ATOM   4830 N N   . LEU C  3 181 ? 15.63200  23.89500  -47.82200 1.000 19.03247  ? 181 LEU L N   1 
ATOM   4831 C CA  . LEU C  3 181 ? 16.26100  24.16100  -49.09300 1.000 25.86184  ? 181 LEU L CA  1 
ATOM   4832 C C   . LEU C  3 181 ? 17.18500  23.05600  -49.52600 1.000 25.38238  ? 181 LEU L C   1 
ATOM   4833 O O   . LEU C  3 181 ? 17.68600  22.31700  -48.70600 1.000 22.26120  ? 181 LEU L O   1 
ATOM   4834 C CB  . LEU C  3 181 ? 17.11800  25.42600  -49.03200 1.000 23.99185  ? 181 LEU L CB  1 
ATOM   4835 C CG  . LEU C  3 181 ? 16.64100  26.87100  -49.09700 1.000 31.32367  ? 181 LEU L CG  1 
ATOM   4836 C CD1 . LEU C  3 181 ? 15.60200  27.17300  -48.04700 1.000 40.50473  ? 181 LEU L CD1 1 
ATOM   4837 C CD2 . LEU C  3 181 ? 17.82800  27.79900  -48.91700 1.000 26.26189  ? 181 LEU L CD2 1 
ATOM   4838 N N   . SER C  3 182 ? 17.39600  22.93600  -50.82300 1.000 22.48790  ? 182 SER L N   1 
ATOM   4839 C CA  . SER C  3 182 ? 18.39900  22.03000  -51.32700 1.000 23.04123  ? 182 SER L CA  1 
ATOM   4840 C C   . SER C  3 182 ? 19.76300  22.44300  -50.81300 1.000 19.79417  ? 182 SER L C   1 
ATOM   4841 O O   . SER C  3 182 ? 20.00200  23.60300  -50.58700 1.000 17.11138  ? 182 SER L O   1 
ATOM   4842 C CB  . SER C  3 182 ? 18.44500  22.08500  -52.86400 1.000 20.54602  ? 182 SER L CB  1 
ATOM   4843 O OG  . SER C  3 182 ? 19.25400  23.13100  -53.33800 1.000 23.65045  ? 182 SER L OG  1 
ATOM   4844 N N   . LYS C  3 183 ? 20.65000  21.48300  -50.68100 1.000 31.21478  ? 183 LYS L N   1 
ATOM   4845 C CA  . LYS C  3 183 ? 22.01100  21.78300  -50.31300 1.000 27.49313  ? 183 LYS L CA  1 
ATOM   4846 C C   . LYS C  3 183 ? 22.64500  22.69400  -51.36500 1.000 23.86756  ? 183 LYS L C   1 
ATOM   4847 O O   . LYS C  3 183 ? 23.23500  23.69000  -51.03000 1.000 25.70825  ? 183 LYS L O   1 
ATOM   4848 C CB  . LYS C  3 183 ? 22.78800  20.49000  -50.20800 1.000 26.89008  ? 183 LYS L CB  1 
ATOM   4849 C CG  . LYS C  3 183 ? 24.29000  20.66400  -50.26100 1.000 37.58831  ? 183 LYS L CG  1 
ATOM   4850 C CD  . LYS C  3 183 ? 24.97500  19.77600  -49.24700 1.000 43.02029  ? 183 LYS L CD  1 
ATOM   4851 C CE  . LYS C  3 183 ? 26.42800  19.54100  -49.61300 1.000 44.50065  ? 183 LYS L CE  1 
ATOM   4852 N NZ  . LYS C  3 183 ? 26.55800  18.69700  -50.82400 1.000 48.60343  ? 183 LYS L NZ  1 
ATOM   4853 N N   . ALA C  3 184 ? 22.48600  22.34000  -52.62400 1.000 27.39520  ? 184 ALA L N   1 
ATOM   4854 C CA  . ALA C  3 184 ? 23.07100  23.11600  -53.74400 1.000 25.02084  ? 184 ALA L CA  1 
ATOM   4855 C C   . ALA C  3 184 ? 22.70000  24.58200  -53.58600 1.000 24.25367  ? 184 ALA L C   1 
ATOM   4856 O O   . ALA C  3 184 ? 23.57600  25.44000  -53.65300 1.000 26.26603  ? 184 ALA L O   1 
ATOM   4857 C CB  . ALA C  3 184 ? 22.54800  22.56600  -55.03400 1.000 23.82570  ? 184 ALA L CB  1 
ATOM   4858 N N   . ASP C  3 185 ? 21.42200  24.85900  -53.33900 1.000 25.17188  ? 185 ASP L N   1 
ATOM   4859 C CA  . ASP C  3 185 ? 20.97600  26.24000  -53.20600 1.000 22.59011  ? 185 ASP L CA  1 
ATOM   4860 C C   . ASP C  3 185 ? 21.48900  26.85800  -51.90800 1.000 21.65321  ? 185 ASP L C   1 
ATOM   4861 O O   . ASP C  3 185 ? 21.95700  27.97400  -51.91900 1.000 22.14077  ? 185 ASP L O   1 
ATOM   4862 C CB  . ASP C  3 185 ? 19.45200  26.38300  -53.37100 1.000 25.68502  ? 185 ASP L CB  1 
ATOM   4863 C CG  . ASP C  3 185 ? 18.98500  27.82100  -53.24100 1.000 24.49091  ? 185 ASP L CG  1 
ATOM   4864 O OD1 . ASP C  3 185 ? 19.01300  28.60100  -54.22300 1.000 24.02151  ? 185 ASP L OD1 1 
ATOM   4865 O OD2 . ASP C  3 185 ? 18.59000  28.17500  -52.12900 1.000 18.69329  ? 185 ASP L OD2 1 
ATOM   4866 N N   . TYR C  3 186 ? 21.42900  26.10400  -50.80000 1.000 22.28164  ? 186 TYR L N   1 
ATOM   4867 C CA  . TYR C  3 186 ? 21.99100  26.60900  -49.52200 1.000 21.07750  ? 186 TYR L CA  1 
ATOM   4868 C C   . TYR C  3 186 ? 23.40800  27.12900  -49.76700 1.000 21.86020  ? 186 TYR L C   1 
ATOM   4869 O O   . TYR C  3 186 ? 23.73500  28.22000  -49.32500 1.000 23.67557  ? 186 TYR L O   1 
ATOM   4870 C CB  . TYR C  3 186 ? 21.98900  25.50200  -48.46800 1.000 22.55136  ? 186 TYR L CB  1 
ATOM   4871 C CG  . TYR C  3 186 ? 22.59600  25.89500  -47.14600 1.000 27.96025  ? 186 TYR L CG  1 
ATOM   4872 C CD1 . TYR C  3 186 ? 21.96500  26.80200  -46.31500 1.000 23.33126  ? 186 TYR L CD1 1 
ATOM   4873 C CD2 . TYR C  3 186 ? 23.80600  25.36800  -46.72800 1.000 29.81983  ? 186 TYR L CD2 1 
ATOM   4874 C CE1 . TYR C  3 186 ? 22.51500  27.17800  -45.10300 1.000 24.31217  ? 186 TYR L CE1 1 
ATOM   4875 C CE2 . TYR C  3 186 ? 24.36800  25.72800  -45.51500 1.000 26.55084  ? 186 TYR L CE2 1 
ATOM   4876 C CZ  . TYR C  3 186 ? 23.72200  26.63900  -44.70000 1.000 28.51375  ? 186 TYR L CZ  1 
ATOM   4877 O OH  . TYR C  3 186 ? 24.26600  27.00700  -43.50600 1.000 29.29241  ? 186 TYR L OH  1 
ATOM   4878 N N   . GLU C  3 187 ? 24.19400  26.35900  -50.51200 1.000 27.02511  ? 187 GLU L N   1 
ATOM   4879 C CA  . GLU C  3 187 ? 25.62400  26.70200  -50.75300 1.000 33.37254  ? 187 GLU L CA  1 
ATOM   4880 C C   . GLU C  3 187 ? 25.79800  27.87100  -51.73400 1.000 32.67591  ? 187 GLU L C   1 
ATOM   4881 O O   . GLU C  3 187 ? 26.94300  28.29300  -51.90400 1.000 32.50072  ? 187 GLU L O   1 
ATOM   4882 C CB  . GLU C  3 187 ? 26.33100  25.43800  -51.23200 1.000 32.22793  ? 187 GLU L CB  1 
ATOM   4883 C CG  . GLU C  3 187 ? 26.17800  24.27300  -50.27800 1.000 33.41714  ? 187 GLU L CG  1 
ATOM   4884 C CD  . GLU C  3 187 ? 27.12000  23.11300  -50.54000 1.000 47.48538  ? 187 GLU L CD  1 
ATOM   4885 O OE1 . GLU C  3 187 ? 27.17200  22.64400  -51.69000 1.000 44.46097  ? 187 GLU L OE1 1 
ATOM   4886 O OE2 . GLU C  3 187 ? 27.79400  22.68400  -49.59400 1.000 47.03240  ? 187 GLU L OE2 1 
ATOM   4887 N N   . LYS C  3 188 ? 24.71600  28.37900  -52.32700 1.000 25.53208  ? 188 LYS L N   1 
ATOM   4888 C CA  . LYS C  3 188 ? 24.80400  29.54300  -53.24000 1.000 21.70255  ? 188 LYS L CA  1 
ATOM   4889 C C   . LYS C  3 188 ? 24.53500  30.84000  -52.47500 1.000 27.16958  ? 188 LYS L C   1 
ATOM   4890 O O   . LYS C  3 188 ? 24.70200  31.90600  -53.07000 1.000 28.46531  ? 188 LYS L O   1 
ATOM   4891 C CB  . LYS C  3 188 ? 23.80200  29.41800  -54.38900 1.000 25.15102  ? 188 LYS L CB  1 
ATOM   4892 C CG  . LYS C  3 188 ? 23.77300  28.09700  -55.13600 1.000 30.22285  ? 188 LYS L CG  1 
ATOM   4893 C CD  . LYS C  3 188 ? 23.04700  28.22600  -56.45100 1.000 30.01097  ? 188 LYS L CD  1 
ATOM   4894 C CE  . LYS C  3 188 ? 22.75900  26.89700  -57.11000 1.000 31.96040  ? 188 LYS L CE  1 
ATOM   4895 N NZ  . LYS C  3 188 ? 21.88100  27.06000  -58.29100 1.000 41.87795  ? 188 LYS L NZ  1 
ATOM   4896 N N   . HIS C  3 189 ? 24.11900  30.76900  -51.22600 1.000 22.61631  ? 189 HIS L N   1 
ATOM   4897 C CA  . HIS C  3 189 ? 23.78400  31.95200  -50.46300 1.000 23.29746  ? 189 HIS L CA  1 
ATOM   4898 C C   . HIS C  3 189 ? 24.60200  32.08600  -49.16200 1.000 24.83060  ? 189 HIS L C   1 
ATOM   4899 O O   . HIS C  3 189 ? 25.04700  31.09300  -48.63400 1.000 25.38798  ? 189 HIS L O   1 
ATOM   4900 C CB  . HIS C  3 189 ? 22.25900  31.99500  -50.18300 1.000 25.77582  ? 189 HIS L CB  1 
ATOM   4901 C CG  . HIS C  3 189 ? 21.40100  31.76600  -51.39100 1.000 23.59263  ? 189 HIS L CG  1 
ATOM   4902 N ND1 . HIS C  3 189 ? 21.28100  32.69200  -52.40100 1.000 29.53229  ? 189 HIS L ND1 1 
ATOM   4903 C CD2 . HIS C  3 189 ? 20.61200  30.72400  -51.74400 1.000 15.16936  ? 189 HIS L CD2 1 
ATOM   4904 C CE1 . HIS C  3 189 ? 20.45800  32.23100  -53.32500 1.000 22.24993  ? 189 HIS L CE1 1 
ATOM   4905 N NE2 . HIS C  3 189 ? 20.04000  31.03700  -52.95200 1.000 25.91731  ? 189 HIS L NE2 1 
ATOM   4906 N N   . LYS C  3 190 ? 24.73100  33.28600  -48.63600 1.000 18.11292  ? 190 LYS L N   1 
ATOM   4907 C CA  . LYS C  3 190 ? 25.47400  33.48000  -47.41000 1.000 28.67968  ? 190 LYS L CA  1 
ATOM   4908 C C   . LYS C  3 190 ? 24.73000  33.90500  -46.16100 1.000 19.33520  ? 190 LYS L C   1 
ATOM   4909 O O   . LYS C  3 190 ? 24.99700  33.40600  -45.11500 1.000 26.99588  ? 190 LYS L O   1 
ATOM   4910 C CB  . LYS C  3 190 ? 26.52100  34.57400  -47.66300 1.000 31.53139  ? 190 LYS L CB  1 
ATOM   4911 C CG  . LYS C  3 190 ? 27.13500  35.20200  -46.42900 1.000 36.85581  ? 190 LYS L CG  1 
ATOM   4912 C CD  . LYS C  3 190 ? 28.48500  35.81300  -46.75900 1.000 41.45427  ? 190 LYS L CD  1 
ATOM   4913 C CE  . LYS C  3 190 ? 28.83400  36.96100  -45.82700 1.000 48.74548  ? 190 LYS L CE  1 
ATOM   4914 N NZ  . LYS C  3 190 ? 29.20800  38.20000  -46.55800 1.000 45.35498  ? 190 LYS L NZ  1 
ATOM   4915 N N   . VAL C  3 191 ? 23.74000  34.73600  -46.29100 1.000 20.35291  ? 191 VAL L N   1 
ATOM   4916 C CA  . VAL C  3 191 ? 23.12100  35.41800  -45.11500 1.000 20.03875  ? 191 VAL L CA  1 
ATOM   4917 C C   . VAL C  3 191 ? 21.73900  34.77800  -44.95600 1.000 28.36201  ? 191 VAL L C   1 
ATOM   4918 O O   . VAL C  3 191 ? 20.89600  34.95800  -45.83200 1.000 23.10288  ? 191 VAL L O   1 
ATOM   4919 C CB  . VAL C  3 191 ? 23.02900  36.95200  -45.12700 1.000 25.40621  ? 191 VAL L CB  1 
ATOM   4920 C CG1 . VAL C  3 191 ? 22.29300  37.48100  -43.90800 1.000 26.05446  ? 191 VAL L CG1 1 
ATOM   4921 C CG2 . VAL C  3 191 ? 24.40000  37.59300  -45.25400 1.000 25.27399  ? 191 VAL L CG2 1 
ATOM   4922 N N   . TYR C  3 192 ? 21.56700  34.04200  -43.86500 1.000 23.30286  ? 192 TYR L N   1 
ATOM   4923 C CA  . TYR C  3 192 ? 20.26700  33.41800  -43.54300 1.000 18.74624  ? 192 TYR L CA  1 
ATOM   4924 C C   . TYR C  3 192 ? 19.71800  34.15600  -42.31800 1.000 28.09832  ? 192 TYR L C   1 
ATOM   4925 O O   . TYR C  3 192 ? 20.42200  34.25900  -41.31000 1.000 18.13113  ? 192 TYR L O   1 
ATOM   4926 C CB  . TYR C  3 192 ? 20.43000  31.90700  -43.39500 1.000 16.31181  ? 192 TYR L CB  1 
ATOM   4927 C CG  . TYR C  3 192 ? 20.73800  31.19600  -44.68500 1.000 20.21564  ? 192 TYR L CG  1 
ATOM   4928 C CD1 . TYR C  3 192 ? 22.00200  31.24800  -45.24600 1.000 24.64546  ? 192 TYR L CD1 1 
ATOM   4929 C CD2 . TYR C  3 192 ? 19.75700  30.49400  -45.36100 1.000 18.79573  ? 192 TYR L CD2 1 
ATOM   4930 C CE1 . TYR C  3 192 ? 22.28900  30.60700  -46.43900 1.000 21.44609  ? 192 TYR L CE1 1 
ATOM   4931 C CE2 . TYR C  3 192 ? 20.02500  29.84700  -46.55400 1.000 22.62291  ? 192 TYR L CE2 1 
ATOM   4932 C CZ  . TYR C  3 192 ? 21.29500  29.90800  -47.09600 1.000 26.07006  ? 192 TYR L CZ  1 
ATOM   4933 O OH  . TYR C  3 192 ? 21.55500  29.28100  -48.27400 1.000 23.45361  ? 192 TYR L OH  1 
ATOM   4934 N N   . ALA C  3 193 ? 18.48700  34.64700  -42.43000 1.000 21.52310  ? 193 ALA L N   1 
ATOM   4935 C CA  . ALA C  3 193 ? 17.92100  35.47500  -41.34900 1.000 22.04338  ? 193 ALA L CA  1 
ATOM   4936 C C   . ALA C  3 193 ? 16.48100  35.09600  -40.99200 1.000 22.75764  ? 193 ALA L C   1 
ATOM   4937 O O   . ALA C  3 193 ? 15.70700  34.79300  -41.90800 1.000 20.51508  ? 193 ALA L O   1 
ATOM   4938 C CB  . ALA C  3 193 ? 18.00300  36.90900  -41.75000 1.000 16.08024  ? 193 ALA L CB  1 
ATOM   4939 N N   . CYS C  3 194 ? 16.15900  35.13800  -39.69900 1.000 22.24966  ? 194 CYS L N   1 
ATOM   4940 C CA  . CYS C  3 194 ? 14.78700  34.91800  -39.20700 1.000 17.27753  ? 194 CYS L CA  1 
ATOM   4941 C C   . CYS C  3 194 ? 14.38100  36.24900  -38.58800 1.000 18.02488  ? 194 CYS L C   1 
ATOM   4942 O O   . CYS C  3 194 ? 15.09900  36.73200  -37.72000 1.000 23.57363  ? 194 CYS L O   1 
ATOM   4943 C CB  . CYS C  3 194 ? 14.73400  33.85900  -38.11800 1.000 25.77866  ? 194 CYS L CB  1 
ATOM   4944 S SG  . CYS C  3 194 ? 13.08600  33.53800  -37.46700 1.000 48.05074  ? 194 CYS L SG  1 
ATOM   4945 N N   . GLU C  3 195 ? 13.30800  36.82900  -39.07700 1.000 16.06495  ? 195 GLU L N   1 
ATOM   4946 C CA  . GLU C  3 195 ? 12.81600  38.11900  -38.60700 1.000 21.88234  ? 195 GLU L CA  1 
ATOM   4947 C C   . GLU C  3 195 ? 11.46500  37.93100  -37.91700 1.000 20.42081  ? 195 GLU L C   1 
ATOM   4948 O O   . GLU C  3 195 ? 10.54400  37.34200  -38.50700 1.000 16.56362  ? 195 GLU L O   1 
ATOM   4949 C CB  . GLU C  3 195 ? 12.62800  39.09300  -39.77500 1.000 23.53225  ? 195 GLU L CB  1 
ATOM   4950 C CG  . GLU C  3 195 ? 12.32700  40.46100  -39.29900 1.000 25.33221  ? 195 GLU L CG  1 
ATOM   4951 C CD  . GLU C  3 195 ? 12.29900  41.51200  -40.44600 1.000 47.38625  ? 195 GLU L CD  1 
ATOM   4952 O OE1 . GLU C  3 195 ? 12.75200  41.19600  -41.59300 1.000 41.90562  ? 195 GLU L OE1 1 
ATOM   4953 O OE2 . GLU C  3 195 ? 11.80400  42.65200  -40.17600 1.000 35.98584  ? 195 GLU L OE2 1 
ATOM   4954 N N   . VAL C  3 196 ? 11.33100  38.47300  -36.70500 1.000 18.73610  ? 196 VAL L N   1 
ATOM   4955 C CA  . VAL C  3 196 ? 10.22500  38.15500  -35.80800 1.000 18.53400  ? 196 VAL L CA  1 
ATOM   4956 C C   . VAL C  3 196 ? 9.52600   39.44200  -35.42100 1.000 16.54614  ? 196 VAL L C   1 
ATOM   4957 O O   . VAL C  3 196 ? 10.16500  40.36400  -34.91600 1.000 22.03852  ? 196 VAL L O   1 
ATOM   4958 C CB  . VAL C  3 196 ? 10.69600  37.40400  -34.54800 1.000 21.43711  ? 196 VAL L CB  1 
ATOM   4959 C CG1 . VAL C  3 196 ? 9.54400   37.34400  -33.51000 1.000 17.05963  ? 196 VAL L CG1 1 
ATOM   4960 C CG2 . VAL C  3 196 ? 11.12300  35.97300  -34.90600 1.000 14.37731  ? 196 VAL L CG2 1 
ATOM   4961 N N   . THR C  3 197 ? 8.22200   39.48700  -35.64700 1.000 16.97874  ? 197 THR L N   1 
ATOM   4962 C CA  . THR C  3 197 ? 7.31700   40.54400  -35.20200 1.000 18.18986  ? 197 THR L CA  1 
ATOM   4963 C C   . THR C  3 197 ? 6.35600   39.96300  -34.16700 1.000 19.01358  ? 197 THR L C   1 
ATOM   4964 O O   . THR C  3 197 ? 5.74900   38.91500  -34.41000 1.000 17.68404  ? 197 THR L O   1 
ATOM   4965 C CB  . THR C  3 197 ? 6.51900   41.09400  -36.40300 1.000 26.01302  ? 197 THR L CB  1 
ATOM   4966 O OG1 . THR C  3 197 ? 7.45100   41.50200  -37.40800 1.000 25.09293  ? 197 THR L OG1 1 
ATOM   4967 C CG2 . THR C  3 197 ? 5.60200   42.25000  -36.00700 1.000 27.19328  ? 197 THR L CG2 1 
ATOM   4968 N N   . HIS C  3 198 ? 6.19100   40.64900  -33.03500 1.000 21.80508  ? 198 HIS L N   1 
ATOM   4969 C CA  . HIS C  3 198 ? 5.28800   40.18800  -31.97500 1.000 24.33043  ? 198 HIS L CA  1 
ATOM   4970 C C   . HIS C  3 198 ? 4.89700   41.37000  -31.12300 1.000 20.04968  ? 198 HIS L C   1 
ATOM   4971 O O   . HIS C  3 198 ? 5.69100   42.29100  -30.95800 1.000 21.28036  ? 198 HIS L O   1 
ATOM   4972 C CB  . HIS C  3 198 ? 5.95300   39.14100  -31.05900 1.000 16.89462  ? 198 HIS L CB  1 
ATOM   4973 C CG  . HIS C  3 198 ? 5.02900   38.58300  -30.01300 1.000 19.40861  ? 198 HIS L CG  1 
ATOM   4974 N ND1 . HIS C  3 198 ? 5.04800   39.02800  -28.70600 1.000 18.38530  ? 198 HIS L ND1 1 
ATOM   4975 C CD2 . HIS C  3 198 ? 4.10200   37.60100  -30.06700 1.000 15.65130  ? 198 HIS L CD2 1 
ATOM   4976 C CE1 . HIS C  3 198 ? 4.13400   38.37100  -28.01400 1.000 18.50992  ? 198 HIS L CE1 1 
ATOM   4977 N NE2 . HIS C  3 198 ? 3.54500   37.50100  -28.81700 1.000 20.59538  ? 198 HIS L NE2 1 
ATOM   4978 N N   . GLN C  3 199 ? 3.70100   41.29600  -30.51600 1.000 24.08179  ? 199 GLN L N   1 
ATOM   4979 C CA  . GLN C  3 199 ? 3.18000   42.42600  -29.73300 1.000 21.11807  ? 199 GLN L CA  1 
ATOM   4980 C C   . GLN C  3 199 ? 4.13100   42.86400  -28.63200 1.000 18.84774  ? 199 GLN L C   1 
ATOM   4981 O O   . GLN C  3 199 ? 4.15600   44.04700  -28.27400 1.000 24.89657  ? 199 GLN L O   1 
ATOM   4982 C CB  . GLN C  3 199 ? 1.82700   42.06400  -29.11500 1.000 28.31092  ? 199 GLN L CB  1 
ATOM   4983 C CG  . GLN C  3 199 ? 1.24000   43.12600  -28.10100 1.000 25.43360  ? 199 GLN L CG  1 
ATOM   4984 C CD  . GLN C  3 199 ? -0.19500  42.76400  -27.68400 1.000 28.56446  ? 199 GLN L CD  1 
ATOM   4985 O OE1 . GLN C  3 199 ? -0.76300  41.82100  -28.22600 1.000 32.75283  ? 199 GLN L OE1 1 
ATOM   4986 N NE2 . GLN C  3 199 ? -0.80900  43.56500  -26.80200 1.000 38.76599  ? 199 GLN L NE2 1 
ATOM   4987 N N   . GLY C  3 200 ? 4.90400   41.93100  -28.06400 1.000 19.44790  ? 200 GLY L N   1 
ATOM   4988 C CA  . GLY C  3 200 ? 5.85300   42.23700  -27.01000 1.000 21.07835  ? 200 GLY L CA  1 
ATOM   4989 C C   . GLY C  3 200 ? 7.16600   42.85800  -27.47000 1.000 24.74289  ? 200 GLY L C   1 
ATOM   4990 O O   . GLY C  3 200 ? 7.98000   43.24200  -26.62400 1.000 20.74194  ? 200 GLY L O   1 
ATOM   4991 N N   . LEU C  3 201 ? 7.39500   42.97800  -28.78000 1.000 25.16525  ? 201 LEU L N   1 
ATOM   4992 C CA  . LEU C  3 201 ? 8.63600   43.51700  -29.32800 1.000 22.32538  ? 201 LEU L CA  1 
ATOM   4993 C C   . LEU C  3 201 ? 8.34400   44.91300  -29.85600 1.000 26.72881  ? 201 LEU L C   1 
ATOM   4994 O O   . LEU C  3 201 ? 7.39800   45.09900  -30.63600 1.000 26.08633  ? 201 LEU L O   1 
ATOM   4995 C CB  . LEU C  3 201 ? 9.13000   42.62900  -30.46500 1.000 26.05802  ? 201 LEU L CB  1 
ATOM   4996 C CG  . LEU C  3 201 ? 9.58400   41.25300  -29.98600 1.000 20.44696  ? 201 LEU L CG  1 
ATOM   4997 C CD1 . LEU C  3 201 ? 9.92200   40.31400  -31.17400 1.000 22.06777  ? 201 LEU L CD1 1 
ATOM   4998 C CD2 . LEU C  3 201 ? 10.74400  41.34300  -29.02000 1.000 17.23335  ? 201 LEU L CD2 1 
ATOM   4999 N N   . SER C  3 202 ? 9.13400   45.90100  -29.44200 1.000 31.40049  ? 202 SER L N   1 
ATOM   5000 C CA  . SER C  3 202 ? 8.81900   47.25900  -29.88800 1.000 30.55173  ? 202 SER L CA  1 
ATOM   5001 C C   . SER C  3 202 ? 9.22100   47.49700  -31.34200 1.000 28.45660  ? 202 SER L C   1 
ATOM   5002 O O   . SER C  3 202 ? 8.65400   48.37800  -31.99500 1.000 36.07265  ? 202 SER L O   1 
ATOM   5003 C CB  . SER C  3 202 ? 9.44100   48.23700  -28.89000 1.000 27.92644  ? 202 SER L CB  1 
ATOM   5004 O OG  . SER C  3 202 ? 10.83500  48.37900  -29.12500 1.000 36.35159  ? 202 SER L OG  1 
ATOM   5005 N N   . SER C  3 203 ? 10.11500  46.67700  -31.88100 1.000 24.14072  ? 203 SER L N   1 
ATOM   5006 C CA  . SER C  3 203 ? 10.35200  46.59500  -33.31500 1.000 32.74940  ? 203 SER L CA  1 
ATOM   5007 C C   . SER C  3 203 ? 10.80200  45.16900  -33.61200 1.000 26.32696  ? 203 SER L C   1 
ATOM   5008 O O   . SER C  3 203 ? 11.14500  44.41700  -32.68800 1.000 27.64920  ? 203 SER L O   1 
ATOM   5009 C CB  . SER C  3 203 ? 11.39900  47.62400  -33.77500 1.000 34.13019  ? 203 SER L CB  1 
ATOM   5010 O OG  . SER C  3 203 ? 12.68500  47.39300  -33.22300 1.000 34.92636  ? 203 SER L OG  1 
ATOM   5011 N N   . PRO C  3 204 ? 10.82200  44.76300  -34.88800 1.000 24.81403  ? 204 PRO L N   1 
ATOM   5012 C CA  . PRO C  3 204 ? 11.13700  43.35400  -35.19400 1.000 22.26873  ? 204 PRO L CA  1 
ATOM   5013 C C   . PRO C  3 204 ? 12.53200  42.97200  -34.73400 1.000 29.55811  ? 204 PRO L C   1 
ATOM   5014 O O   . PRO C  3 204 ? 13.44100  43.80100  -34.65900 1.000 33.42704  ? 204 PRO L O   1 
ATOM   5015 C CB  . PRO C  3 204 ? 11.00700  43.26700  -36.71900 1.000 24.87754  ? 204 PRO L CB  1 
ATOM   5016 C CG  . PRO C  3 204 ? 10.09900  44.42500  -37.09600 1.000 27.81147  ? 204 PRO L CG  1 
ATOM   5017 C CD  . PRO C  3 204 ? 10.43500  45.51800  -36.09500 1.000 25.40444  ? 204 PRO L CD  1 
ATOM   5018 N N   . VAL C  3 205 ? 12.67200  41.71400  -34.32800 1.000 21.96168  ? 205 VAL L N   1 
ATOM   5019 C CA  . VAL C  3 205 ? 13.94300  41.15300  -33.89000 1.000 22.64227  ? 205 VAL L CA  1 
ATOM   5020 C C   . VAL C  3 205 ? 14.41100  40.24800  -35.01900 1.000 26.62555  ? 205 VAL L C   1 
ATOM   5021 O O   . VAL C  3 205 ? 13.61400  39.45300  -35.52900 1.000 18.68654  ? 205 VAL L O   1 
ATOM   5022 C CB  . VAL C  3 205 ? 13.77900  40.38000  -32.55800 1.000 22.91807  ? 205 VAL L CB  1 
ATOM   5023 C CG1 . VAL C  3 205 ? 14.96700  39.51700  -32.25800 1.000 24.57869  ? 205 VAL L CG1 1 
ATOM   5024 C CG2 . VAL C  3 205 ? 13.59200  41.33000  -31.39600 1.000 24.41983  ? 205 VAL L CG2 1 
ATOM   5025 N N   . THR C  3 206 ? 15.67800  40.40500  -35.45000 1.000 17.53428  ? 206 THR L N   1 
ATOM   5026 C CA  . THR C  3 206 ? 16.29500  39.56200  -36.47600 1.000 22.79612  ? 206 THR L CA  1 
ATOM   5027 C C   . THR C  3 206 ? 17.49100  38.79700  -35.90700 1.000 27.66128  ? 206 THR L C   1 
ATOM   5028 O O   . THR C  3 206 ? 18.38500  39.38400  -35.26900 1.000 26.53988  ? 206 THR L O   1 
ATOM   5029 C CB  . THR C  3 206 ? 16.71600  40.37800  -37.72400 1.000 22.68537  ? 206 THR L CB  1 
ATOM   5030 O OG1 . THR C  3 206 ? 15.62600  41.20700  -38.18000 1.000 23.93327  ? 206 THR L OG1 1 
ATOM   5031 C CG2 . THR C  3 206 ? 17.25600  39.47300  -38.87000 1.000 26.37749  ? 206 THR L CG2 1 
ATOM   5032 N N   . LYS C  3 207 ? 17.47800  37.47600  -36.10100 1.000 20.85456  ? 207 LYS L N   1 
ATOM   5033 C CA  . LYS C  3 207 ? 18.59900  36.60200  -35.79800 1.000 21.40869  ? 207 LYS L CA  1 
ATOM   5034 C C   . LYS C  3 207 ? 19.10300  36.05900  -37.12000 1.000 22.30589  ? 207 LYS L C   1 
ATOM   5035 O O   . LYS C  3 207 ? 18.30400  35.59900  -37.94700 1.000 18.43996  ? 207 LYS L O   1 
ATOM   5036 C CB  . LYS C  3 207 ? 18.18400  35.44900  -34.88600 1.000 20.33230  ? 207 LYS L CB  1 
ATOM   5037 C CG  . LYS C  3 207 ? 17.65600  35.82000  -33.47900 1.000 20.71237  ? 207 LYS L CG  1 
ATOM   5038 C CD  . LYS C  3 207 ? 18.26000  37.10300  -32.92100 1.000 26.90932  ? 207 LYS L CD  1 
ATOM   5039 C CE  . LYS C  3 207 ? 18.67100  36.86600  -31.50100 1.000 36.36631  ? 207 LYS L CE  1 
ATOM   5040 N NZ  . LYS C  3 207 ? 19.00700  38.09300  -30.69900 1.000 41.17049  ? 207 LYS L NZ  1 
ATOM   5041 N N   . SER C  3 208 ? 20.41700  36.10400  -37.33100 1.000 20.58767  ? 208 SER L N   1 
ATOM   5042 C CA  . SER C  3 208 ? 20.92700  35.71400  -38.63500 1.000 19.99179  ? 208 SER L CA  1 
ATOM   5043 C C   . SER C  3 208 ? 22.29600  35.08400  -38.45800 1.000 24.77030  ? 208 SER L C   1 
ATOM   5044 O O   . SER C  3 208 ? 22.93600  35.21900  -37.41100 1.000 24.99582  ? 208 SER L O   1 
ATOM   5045 C CB  . SER C  3 208 ? 20.98200  36.90600  -39.57600 1.000 22.99927  ? 208 SER L CB  1 
ATOM   5046 O OG  . SER C  3 208 ? 21.99200  37.79900  -39.14400 1.000 28.51087  ? 208 SER L OG  1 
ATOM   5047 N N   . PHE C  3 209 ? 22.71900  34.37300  -39.49700 1.000 23.38332  ? 209 PHE L N   1 
ATOM   5048 C CA  . PHE C  3 209 ? 24.03100  33.75500  -39.56100 1.000 24.43057  ? 209 PHE L CA  1 
ATOM   5049 C C   . PHE C  3 209 ? 24.57600  33.79100  -40.98700 1.000 33.40306  ? 209 PHE L C   1 
ATOM   5050 O O   . PHE C  3 209 ? 23.84000  33.94500  -41.97200 1.000 26.78335  ? 209 PHE L O   1 
ATOM   5051 C CB  . PHE C  3 209 ? 23.97600  32.33600  -38.97200 1.000 28.86339  ? 209 PHE L CB  1 
ATOM   5052 C CG  . PHE C  3 209 ? 23.32400  31.28900  -39.85300 1.000 26.42088  ? 209 PHE L CG  1 
ATOM   5053 C CD1 . PHE C  3 209 ? 24.00500  30.68100  -40.88200 1.000 27.13065  ? 209 PHE L CD1 1 
ATOM   5054 C CD2 . PHE C  3 209 ? 22.03800  30.85300  -39.57600 1.000 20.95556  ? 209 PHE L CD2 1 
ATOM   5055 C CE1 . PHE C  3 209 ? 23.40000  29.70500  -41.65000 1.000 25.70361  ? 209 PHE L CE1 1 
ATOM   5056 C CE2 . PHE C  3 209 ? 21.44200  29.87700  -40.34300 1.000 19.84227  ? 209 PHE L CE2 1 
ATOM   5057 C CZ  . PHE C  3 209 ? 22.12500  29.30300  -41.38000 1.000 22.95247  ? 209 PHE L CZ  1 
ATOM   5058 N N   . ASN C  3 210 ? 25.89400  33.66600  -41.07300 1.000 27.61357  ? 210 ASN L N   1 
ATOM   5059 C CA  . ASN C  3 210 ? 26.62000  33.71500  -42.33000 1.000 29.90995  ? 210 ASN L CA  1 
ATOM   5060 C C   . ASN C  3 210 ? 27.03000  32.26600  -42.58300 1.000 28.36866  ? 210 ASN L C   1 
ATOM   5061 O O   . ASN C  3 210 ? 27.73800  31.69200  -41.75900 1.000 35.24217  ? 210 ASN L O   1 
ATOM   5062 C CB  . ASN C  3 210 ? 27.82000  34.62900  -42.13500 1.000 37.77719  ? 210 ASN L CB  1 
ATOM   5063 C CG  . ASN C  3 210 ? 27.50600  36.09600  -42.44100 1.000 36.73795  ? 210 ASN L CG  1 
ATOM   5064 O OD1 . ASN C  3 210 ? 26.95700  36.43800  -43.48100 1.000 45.73733  ? 210 ASN L OD1 1 
ATOM   5065 N ND2 . ASN C  3 210 ? 27.83000  36.97100  -41.48800 1.000 49.18952  ? 210 ASN L ND2 1 
ATOM   5066 N N   . ARG C  3 211 ? 26.59000  31.67800  -43.69000 1.000 23.93465  ? 211 ARG L N   1 
ATOM   5067 C CA  . ARG C  3 211 ? 26.99500  30.29000  -44.02100 1.000 26.99801  ? 211 ARG L CA  1 
ATOM   5068 C C   . ARG C  3 211 ? 28.52000  30.16900  -43.96600 1.000 40.47604  ? 211 ARG L C   1 
ATOM   5069 O O   . ARG C  3 211 ? 29.20800  30.99200  -44.58000 1.000 34.48973  ? 211 ARG L O   1 
ATOM   5070 C CB  . ARG C  3 211 ? 26.48300  29.82300  -45.38300 1.000 24.45245  ? 211 ARG L CB  1 
ATOM   5071 C CG  . ARG C  3 211 ? 26.63600  28.33200  -45.63800 1.000 26.72458  ? 211 ARG L CG  1 
ATOM   5072 C CD  . ARG C  3 211 ? 26.26200  27.95700  -47.05900 1.000 26.65022  ? 211 ARG L CD  1 
ATOM   5073 N NE  . ARG C  3 211 ? 26.67100  29.00000  -47.97900 1.000 28.47025  ? 211 ARG L NE  1 
ATOM   5074 C CZ  . ARG C  3 211 ? 27.79100  28.97800  -48.68400 1.000 36.67231  ? 211 ARG L CZ  1 
ATOM   5075 N NH1 . ARG C  3 211 ? 28.60800  27.94500  -48.59300 1.000 36.09574  ? 211 ARG L NH1 1 
ATOM   5076 N NH2 . ARG C  3 211 ? 28.08800  29.98600  -49.48300 1.000 43.41650  ? 211 ARG L NH2 1 
ATOM   5077 N N   . GLY C  3 212 ? 29.00600  29.16400  -43.24000 1.000 47.00366  ? 212 GLY L N   1 
ATOM   5078 C CA  . GLY C  3 212 ? 30.45400  28.92700  -43.15000 1.000 45.60768  ? 212 GLY L CA  1 
ATOM   5079 C C   . GLY C  3 212 ? 31.07500  29.61700  -41.96100 1.000 54.99631  ? 212 GLY L C   1 
ATOM   5080 O O   . GLY C  3 212 ? 32.09200  29.11800  -41.47200 1.000 67.82178  ? 212 GLY L O   1 
ATOM   5081 N N   . GLU C  3 213 ? 30.52900  30.74300  -41.53800 1.000 49.96671  ? 213 GLU L N   1 
ATOM   5082 C CA  . GLU C  3 213 ? 31.07200  31.47600  -40.42900 1.000 50.05923  ? 213 GLU L CA  1 
ATOM   5083 C C   . GLU C  3 213 ? 30.37300  31.17200  -39.11400 1.000 61.98455  ? 213 GLU L C   1 
ATOM   5084 O O   . GLU C  3 213 ? 29.22000  31.54800  -38.93600 1.000 58.25521  ? 213 GLU L O   1 
ATOM   5085 C CB  . GLU C  3 213 ? 30.93500  32.96800  -40.68400 1.000 49.25405  ? 213 GLU L CB  1 
ATOM   5086 C CG  . GLU C  3 213 ? 31.46700  33.45900  -42.01800 1.000 61.15323  ? 213 GLU L CG  1 
ATOM   5087 C CD  . GLU C  3 213 ? 31.34600  34.96700  -42.15900 1.000 65.43645  ? 213 GLU L CD  1 
ATOM   5088 O OE1 . GLU C  3 213 ? 31.11200  35.64300  -41.13700 1.000 63.89378  ? 213 GLU L OE1 1 
ATOM   5089 O OE2 . GLU C  3 213 ? 31.48600  35.47800  -43.28600 1.000 69.19355  ? 213 GLU L OE2 1 
ATOM   5090 N N   . CYS C  3 214 ? 31.06700  30.53500  -38.17200 1.000 68.27037  ? 214 CYS L N   1 
ATOM   5091 C CA  . CYS C  3 214 ? 30.47400  30.30500  -36.82400 1.000 78.48043  ? 214 CYS L CA  1 
ATOM   5092 C C   . CYS C  3 214 ? 30.72400  31.52300  -35.92800 1.000 76.16282  ? 214 CYS L C   1 
ATOM   5093 O O   . CYS C  3 214 ? 31.67600  31.45300  -35.13700 1.000 86.33019  ? 214 CYS L O   1 
ATOM   5094 C CB  . CYS C  3 214 ? 31.07700  29.09500  -36.13700 1.000 71.35797  ? 214 CYS L CB  1 
ATOM   5095 S SG  . CYS C  3 214 ? 30.05900  28.46800  -34.77900 1.000 92.22231  ? 214 CYS L SG  1 
HETATM 5096 C C1  . NAG D  4 .   ? -34.96800 19.94800  -3.47800  1.000 32.67311  ? 301 NAG B C1  1 
HETATM 5097 C C2  . NAG D  4 .   ? -33.67700 19.17600  -3.23700  1.000 26.99590  ? 301 NAG B C2  1 
HETATM 5098 C C3  . NAG D  4 .   ? -32.50500 20.09200  -2.93200  1.000 33.30379  ? 301 NAG B C3  1 
HETATM 5099 C C4  . NAG D  4 .   ? -32.44800 21.28400  -3.87500  1.000 41.38866  ? 301 NAG B C4  1 
HETATM 5100 C C5  . NAG D  4 .   ? -33.80800 21.94800  -3.96200  1.000 42.49780  ? 301 NAG B C5  1 
HETATM 5101 C C6  . NAG D  4 .   ? -33.79500 23.10000  -4.95200  1.000 52.59095  ? 301 NAG B C6  1 
HETATM 5102 C C7  . NAG D  4 .   ? -34.47200 17.11300  -2.22900  1.000 33.20309  ? 301 NAG B C7  1 
HETATM 5103 C C8  . NAG D  4 .   ? -34.52800 16.29400  -0.97600  1.000 27.55043  ? 301 NAG B C8  1 
HETATM 5104 N N2  . NAG D  4 .   ? -33.83500 18.26800  -2.12100  1.000 29.04494  ? 301 NAG B N2  1 
HETATM 5105 O O3  . NAG D  4 .   ? -31.29900 19.34500  -3.05300  1.000 35.53101  ? 301 NAG B O3  1 
HETATM 5106 O O4  . NAG D  4 .   ? -31.48800 22.21900  -3.38600  1.000 38.34930  ? 301 NAG B O4  1 
HETATM 5107 O O5  . NAG D  4 .   ? -34.76000 21.00100  -4.40600  1.000 39.91652  ? 301 NAG B O5  1 
HETATM 5108 O O6  . NAG D  4 .   ? -35.00800 23.84500  -4.81600  1.000 50.24299  ? 301 NAG B O6  1 
HETATM 5109 O O7  . NAG D  4 .   ? -34.97600 16.74600  -3.27000  1.000 24.75750  ? 301 NAG B O7  1 
HETATM 5110 C C1  . EDO E  5 .   ? -49.13200 12.26900  0.22200   1.000 24.45279  ? 302 EDO B C1  1 
HETATM 5111 O O1  . EDO E  5 .   ? -49.17600 11.58600  1.45300   1.000 26.43187  ? 302 EDO B O1  1 
HETATM 5112 C C2  . EDO E  5 .   ? -48.54800 11.45700  -0.87200  1.000 27.83998  ? 302 EDO B C2  1 
HETATM 5113 O O2  . EDO E  5 .   ? -47.29900 10.89800  -0.54500  1.000 25.26186  ? 302 EDO B O2  1 
HETATM 5114 C C1  . EDO F  5 .   ? -33.27500 -6.07500  -10.85100 1.000 30.57383  ? 303 EDO B C1  1 
HETATM 5115 O O1  . EDO F  5 .   ? -33.35700 -5.92700  -9.45400  1.000 36.79774  ? 303 EDO B O1  1 
HETATM 5116 C C2  . EDO F  5 .   ? -33.35400 -7.48300  -11.28200 1.000 31.32645  ? 303 EDO B C2  1 
HETATM 5117 O O2  . EDO F  5 .   ? -34.14600 -7.65800  -12.43100 1.000 54.83081  ? 303 EDO B O2  1 
HETATM 5118 C C1  . EDO G  5 .   ? -31.29900 -1.94800  -12.79500 1.000 37.09458  ? 304 EDO B C1  1 
HETATM 5119 O O1  . EDO G  5 .   ? -31.52500 -3.33400  -12.71900 1.000 39.84416  ? 304 EDO B O1  1 
HETATM 5120 C C2  . EDO G  5 .   ? -30.37600 -1.45200  -11.75300 1.000 32.09131  ? 304 EDO B C2  1 
HETATM 5121 O O2  . EDO G  5 .   ? -29.84100 -0.19100  -12.07100 1.000 39.94185  ? 304 EDO B O2  1 
HETATM 5122 C C1  . EDO H  5 .   ? -51.12100 -13.29200 -3.16300  1.000 36.75003  ? 305 EDO B C1  1 
HETATM 5123 O O1  . EDO H  5 .   ? -52.30500 -12.81500 -3.79900  1.000 32.84729  ? 305 EDO B O1  1 
HETATM 5124 C C2  . EDO H  5 .   ? -50.89300 -14.74300 -3.54100  1.000 49.06109  ? 305 EDO B C2  1 
HETATM 5125 O O2  . EDO H  5 .   ? -50.40900 -14.82000 -4.88100  1.000 52.10882  ? 305 EDO B O2  1 
HETATM 5126 C C1  . EDO I  5 .   ? -48.42500 -1.59200  -12.43200 1.000 27.66280  ? 306 EDO B C1  1 
HETATM 5127 O O1  . EDO I  5 .   ? -48.24400 -2.51600  -11.36500 1.000 23.67174  ? 306 EDO B O1  1 
HETATM 5128 C C2  . EDO I  5 .   ? -47.09900 -0.94800  -12.80500 1.000 34.28967  ? 306 EDO B C2  1 
HETATM 5129 O O2  . EDO I  5 .   ? -46.05400 -1.91000  -12.64200 1.000 45.42759  ? 306 EDO B O2  1 
HETATM 5130 C C1  . EDO J  5 .   ? -50.01200 -12.84900 -10.31800 1.000 24.55821  ? 307 EDO B C1  1 
HETATM 5131 O O1  . EDO J  5 .   ? -49.08000 -13.75100 -9.71900  1.000 41.99070  ? 307 EDO B O1  1 
HETATM 5132 C C2  . EDO J  5 .   ? -49.26900 -11.73700 -11.04200 1.000 35.05906  ? 307 EDO B C2  1 
HETATM 5133 O O2  . EDO J  5 .   ? -48.69700 -12.21600 -12.26000 1.000 28.28792  ? 307 EDO B O2  1 
HETATM 5134 C C1  . EDO K  5 .   ? -51.46900 7.35500   8.98900   1.000 36.40524  ? 308 EDO B C1  1 
HETATM 5135 O O1  . EDO K  5 .   ? -51.46300 5.92800   8.97600   1.000 43.47845  ? 308 EDO B O1  1 
HETATM 5136 C C2  . EDO K  5 .   ? -51.23800 7.86500   7.58000   1.000 30.28366  ? 308 EDO B C2  1 
HETATM 5137 O O2  . EDO K  5 .   ? -51.77900 9.18400   7.47900   1.000 52.83652  ? 308 EDO B O2  1 
HETATM 5138 C C1  . EDO L  5 .   ? -56.66300 -5.85800  -11.81300 1.000 26.54700  ? 309 EDO B C1  1 
HETATM 5139 O O1  . EDO L  5 .   ? -57.63700 -4.92400  -11.33900 1.000 42.42606  ? 309 EDO B O1  1 
HETATM 5140 C C2  . EDO L  5 .   ? -55.26400 -5.39800  -11.42900 1.000 32.06003  ? 309 EDO B C2  1 
HETATM 5141 O O2  . EDO L  5 .   ? -55.14000 -5.22100  -10.01300 1.000 25.00806  ? 309 EDO B O2  1 
HETATM 5142 C C1  . EDO M  5 .   ? -34.43000 14.95700  10.28100  1.000 50.83667  ? 310 EDO B C1  1 
HETATM 5143 O O1  . EDO M  5 .   ? -34.85600 15.94100  9.33500   1.000 50.83430  ? 310 EDO B O1  1 
HETATM 5144 C C2  . EDO M  5 .   ? -35.00900 13.59400  9.91500   1.000 54.34873  ? 310 EDO B C2  1 
HETATM 5145 O O2  . EDO M  5 .   ? -34.01600 12.81200  9.24400   1.000 53.92097  ? 310 EDO B O2  1 
HETATM 5146 C C1  . EDO N  5 .   ? -40.66100 28.34000  -4.69000  1.000 63.98155  ? 311 EDO B C1  1 
HETATM 5147 O O1  . EDO N  5 .   ? -41.42600 27.19000  -4.32400  1.000 56.72548  ? 311 EDO B O1  1 
HETATM 5148 C C2  . EDO N  5 .   ? -39.43900 28.44500  -3.78500  1.000 61.50598  ? 311 EDO B C2  1 
HETATM 5149 O O2  . EDO N  5 .   ? -39.76900 29.26800  -2.66300  1.000 61.11641  ? 311 EDO B O2  1 
HETATM 5150 C C1  . PEG O  6 .   ? -37.80300 14.24500  -10.22100 1.000 47.29378  ? 312 PEG B C1  1 
HETATM 5151 O O1  . PEG O  6 .   ? -39.00100 13.56200  -10.57200 1.000 44.51450  ? 312 PEG B O1  1 
HETATM 5152 C C2  . PEG O  6 .   ? -36.65200 13.24700  -10.18000 1.000 39.14935  ? 312 PEG B C2  1 
HETATM 5153 O O2  . PEG O  6 .   ? -35.51300 13.80900  -9.53300  1.000 47.33595  ? 312 PEG B O2  1 
HETATM 5154 C C3  . PEG O  6 .   ? -35.75100 15.13200  -9.06300  1.000 43.21473  ? 312 PEG B C3  1 
HETATM 5155 C C4  . PEG O  6 .   ? -34.44700 15.91900  -9.05700  1.000 52.18715  ? 312 PEG B C4  1 
HETATM 5156 O O4  . PEG O  6 .   ? -33.60000 15.45400  -8.00200  1.000 47.75859  ? 312 PEG B O4  1 
HETATM 5157 C C1  . PEG P  6 .   ? -55.20000 -7.47800  6.20600   1.000 30.73477  ? 313 PEG B C1  1 
HETATM 5158 O O1  . PEG P  6 .   ? -55.86200 -6.23000  6.09400   1.000 33.80658  ? 313 PEG B O1  1 
HETATM 5159 C C2  . PEG P  6 .   ? -53.71000 -7.23100  6.35700   1.000 35.42995  ? 313 PEG B C2  1 
HETATM 5160 O O2  . PEG P  6 .   ? -53.01600 -8.29900  5.75700   1.000 26.59398  ? 313 PEG B O2  1 
HETATM 5161 C C3  . PEG P  6 .   ? -52.92100 -9.41200  6.61800   1.000 28.76041  ? 313 PEG B C3  1 
HETATM 5162 C C4  . PEG P  6 .   ? -51.57700 -10.07900 6.38300   1.000 27.66961  ? 313 PEG B C4  1 
HETATM 5163 O O4  . PEG P  6 .   ? -51.52500 -10.49200 5.01900   1.000 39.48495  ? 313 PEG B O4  1 
HETATM 5164 C C1  . EDO Q  5 .   ? -37.76200 0.17000   12.05900  1.000 29.16103  ? 314 EDO B C1  1 
HETATM 5165 O O1  . EDO Q  5 .   ? -37.39200 1.30000   12.84600  1.000 36.40380  ? 314 EDO B O1  1 
HETATM 5166 C C2  . EDO Q  5 .   ? -36.74400 -0.93400  12.26200  1.000 31.39923  ? 314 EDO B C2  1 
HETATM 5167 O O2  . EDO Q  5 .   ? -37.09900 -1.69200  13.41200  1.000 37.15237  ? 314 EDO B O2  1 
HETATM 5168 C C1  . EDO R  5 .   ? -30.46300 16.75200  -0.07900  1.000 30.27386  ? 315 EDO B C1  1 
HETATM 5169 O O1  . EDO R  5 .   ? -31.61600 17.59000  0.01000   1.000 44.89557  ? 315 EDO B O1  1 
HETATM 5170 C C2  . EDO R  5 .   ? -29.42800 17.36600  -1.00600  1.000 47.75107  ? 315 EDO B C2  1 
HETATM 5171 O O2  . EDO R  5 .   ? -28.53000 18.18900  -0.26200  1.000 50.57690  ? 315 EDO B O2  1 
HETATM 5172 C C1  . EDO S  5 .   ? -46.71100 2.07800   14.84200  1.000 30.45013  ? 316 EDO B C1  1 
HETATM 5173 O O1  . EDO S  5 .   ? -45.74300 1.04600   15.02400  1.000 32.56905  ? 316 EDO B O1  1 
HETATM 5174 C C2  . EDO S  5 .   ? -46.06900 3.30200   14.19700  1.000 26.96823  ? 316 EDO B C2  1 
HETATM 5175 O O2  . EDO S  5 .   ? -45.25700 2.91100   13.09800  1.000 23.61039  ? 316 EDO B O2  1 
HETATM 5176 K K   . K   T  7 .   ? -37.54100 7.13300   -14.37100 1.000 59.21601  ? 317 K   B K   1 
HETATM 5177 K K   . K   U  7 .   ? -30.36400 -8.22200  -12.69000 1.000 73.55261  ? 318 K   B K   1 
HETATM 5178 K K   . K   V  7 .   ? -25.35100 5.86000   1.01600   1.000 71.50609  ? 319 K   B K   1 
HETATM 5179 K K   . K   W  7 .   ? -38.65900 9.73000   -12.29200 1.000 74.62687  ? 320 K   B K   1 
HETATM 5180 K K   . K   X  7 .   ? -19.80600 14.14100  -5.39000  1.000 67.78107  ? 321 K   B K   1 
HETATM 5181 C C1  . EDO Y  5 .   ? -23.09000 5.56400   -15.44100 1.000 30.50019  ? 301 EDO H C1  1 
HETATM 5182 O O1  . EDO Y  5 .   ? -24.32800 5.91800   -14.84500 1.000 35.52959  ? 301 EDO H O1  1 
HETATM 5183 C C2  . EDO Y  5 .   ? -23.08300 6.03400   -16.88800 1.000 22.58674  ? 301 EDO H C2  1 
HETATM 5184 O O2  . EDO Y  5 .   ? -22.48200 5.01600   -17.67800 1.000 22.45052  ? 301 EDO H O2  1 
HETATM 5185 C C1  . EDO Z  5 .   ? 5.17000   13.73400  -31.79600 1.000 34.97862  ? 302 EDO H C1  1 
HETATM 5186 O O1  . EDO Z  5 .   ? 4.87600   12.55100  -32.53600 1.000 29.52473  ? 302 EDO H O1  1 
HETATM 5187 C C2  . EDO Z  5 .   ? 4.01100   14.71400  -31.91600 1.000 29.85207  ? 302 EDO H C2  1 
HETATM 5188 O O2  . EDO Z  5 .   ? 3.87700   15.15500  -33.26700 1.000 25.28631  ? 302 EDO H O2  1 
HETATM 5189 C C1  . EDO AA 5 .   ? 9.74700   21.09200  -38.85500 1.000 25.84064  ? 303 EDO H C1  1 
HETATM 5190 O O1  . EDO AA 5 .   ? 8.63700   21.51700  -38.06800 1.000 24.93509  ? 303 EDO H O1  1 
HETATM 5191 C C2  . EDO AA 5 .   ? 10.82800  20.51900  -37.95100 1.000 26.27105  ? 303 EDO H C2  1 
HETATM 5192 O O2  . EDO AA 5 .   ? 11.55700  21.56700  -37.32300 1.000 24.51525  ? 303 EDO H O2  1 
HETATM 5193 C C1  . PEG BA 6 .   ? -15.62300 13.58900  -36.25900 1.000 46.96767  ? 304 PEG H C1  1 
HETATM 5194 O O1  . PEG BA 6 .   ? -16.80200 14.38100  -36.11500 1.000 55.59943  ? 304 PEG H O1  1 
HETATM 5195 C C2  . PEG BA 6 .   ? -15.93700 12.27300  -36.96200 1.000 50.88257  ? 304 PEG H C2  1 
HETATM 5196 O O2  . PEG BA 6 .   ? -15.83700 12.39900  -38.38000 1.000 56.70442  ? 304 PEG H O2  1 
HETATM 5197 C C3  . PEG BA 6 .   ? -15.21300 11.27300  -38.97500 1.000 42.89384  ? 304 PEG H C3  1 
HETATM 5198 C C4  . PEG BA 6 .   ? -14.87600 11.57500  -40.42800 1.000 42.79315  ? 304 PEG H C4  1 
HETATM 5199 O O4  . PEG BA 6 .   ? -13.45900 11.55100  -40.60300 1.000 44.12394  ? 304 PEG H O4  1 
HETATM 5200 C C1  . EDO CA 5 .   ? 5.41500   23.13600  -22.52800 1.000 34.69971  ? 305 EDO H C1  1 
HETATM 5201 O O1  . EDO CA 5 .   ? 6.04100   24.41000  -22.38200 1.000 37.16195  ? 305 EDO H O1  1 
HETATM 5202 C C2  . EDO CA 5 .   ? 5.34000   22.74400  -23.99800 1.000 34.73056  ? 305 EDO H C2  1 
HETATM 5203 O O2  . EDO CA 5 .   ? 6.63900   22.76100  -24.58800 1.000 22.96556  ? 305 EDO H O2  1 
HETATM 5204 C C1  . EDO DA 5 .   ? 6.64600   38.78400  -17.13000 1.000 46.05576  ? 301 EDO L C1  1 
HETATM 5205 O O1  . EDO DA 5 .   ? 6.51600   37.63300  -17.96500 1.000 28.27852  ? 301 EDO L O1  1 
HETATM 5206 C C2  . EDO DA 5 .   ? 5.94300   40.00200  -17.72100 1.000 36.65296  ? 301 EDO L C2  1 
HETATM 5207 O O2  . EDO DA 5 .   ? 6.10800   40.03000  -19.13800 1.000 39.83800  ? 301 EDO L O2  1 
HETATM 5208 C C1  . EDO EA 5 .   ? 2.46600   21.78700  -21.53900 1.000 50.30425  ? 302 EDO L C1  1 
HETATM 5209 O O1  . EDO EA 5 .   ? 1.71500   22.58600  -22.45100 1.000 41.57850  ? 302 EDO L O1  1 
HETATM 5210 C C2  . EDO EA 5 .   ? 2.51700   22.45800  -20.17600 1.000 40.95648  ? 302 EDO L C2  1 
HETATM 5211 O O2  . EDO EA 5 .   ? 3.84500   22.34000  -19.65800 1.000 46.17633  ? 302 EDO L O2  1 
HETATM 5212 C C1  . EDO FA 5 .   ? 2.02100   22.43100  -34.75800 1.000 37.68229  ? 303 EDO L C1  1 
HETATM 5213 O O1  . EDO FA 5 .   ? 1.49000   23.75300  -34.74000 1.000 30.51270  ? 303 EDO L O1  1 
HETATM 5214 C C2  . EDO FA 5 .   ? 2.00000   21.80300  -36.15100 1.000 34.83727  ? 303 EDO L C2  1 
HETATM 5215 O O2  . EDO FA 5 .   ? 2.02400   22.81200  -37.16800 1.000 39.53308  ? 303 EDO L O2  1 
HETATM 5216 C C1  . EDO GA 5 .   ? -8.91400  17.93400  -27.40800 1.000 32.53455  ? 304 EDO L C1  1 
HETATM 5217 O O1  . EDO GA 5 .   ? -10.01000 17.09000  -27.76000 1.000 23.87568  ? 304 EDO L O1  1 
HETATM 5218 C C2  . EDO GA 5 .   ? -7.66100  17.11100  -27.12700 1.000 40.84609  ? 304 EDO L C2  1 
HETATM 5219 O O2  . EDO GA 5 .   ? -7.23300  16.42500  -28.31400 1.000 40.07863  ? 304 EDO L O2  1 
HETATM 5220 C C1  . EDO HA 5 .   ? -2.24800  25.82400  -18.69500 1.000 37.12381  ? 305 EDO L C1  1 
HETATM 5221 O O1  . EDO HA 5 .   ? -1.49800  24.79300  -19.34700 1.000 48.66186  ? 305 EDO L O1  1 
HETATM 5222 C C2  . EDO HA 5 .   ? -1.30800  26.72100  -17.91200 1.000 47.16074  ? 305 EDO L C2  1 
HETATM 5223 O O2  . EDO HA 5 .   ? -0.89300  27.80500  -18.73900 1.000 32.36505  ? 305 EDO L O2  1 
HETATM 5224 C C1  . EDO IA 5 .   ? 26.84800  27.63200  -41.82600 1.000 40.73569  ? 306 EDO L C1  1 
HETATM 5225 O O1  . EDO IA 5 .   ? 27.31800  28.10400  -40.56100 1.000 48.77069  ? 306 EDO L O1  1 
HETATM 5226 C C2  . EDO IA 5 .   ? 27.14100  26.14500  -41.99000 1.000 45.13098  ? 306 EDO L C2  1 
HETATM 5227 O O2  . EDO IA 5 .   ? 26.52800  25.62800  -43.17100 1.000 33.63390  ? 306 EDO L O2  1 
HETATM 5228 K K   . K   JA 7 .   ? 2.18400   40.21800  -34.93300 1.000 67.69050  ? 307 K   L K   1 
HETATM 5229 K K   . K   KA 7 .   ? 20.43300  19.98800  -39.42200 1.000 59.80962  ? 308 K   L K   1 
HETATM 5230 O O   . HOH LA 8 .   ? -33.87500 6.54200   7.20400   1.000 43.67674  ? 401 HOH B O   1 
HETATM 5231 O O   . HOH LA 8 .   ? -59.78700 6.51700   -0.07600  1.000 36.74788  ? 402 HOH B O   1 
HETATM 5232 O O   . HOH LA 8 .   ? -46.01300 24.89300  -8.76600  1.000 50.29499  ? 403 HOH B O   1 
HETATM 5233 O O   . HOH LA 8 .   ? -61.15100 10.16500  0.79400   1.000 48.87842  ? 404 HOH B O   1 
HETATM 5234 O O   . HOH LA 8 .   ? -52.88700 -14.49700 -6.26000  1.000 46.61908  ? 405 HOH B O   1 
HETATM 5235 O O   . HOH LA 8 .   ? -18.42700 0.71300   -0.21500  1.000 43.18562  ? 406 HOH B O   1 
HETATM 5236 O O   . HOH LA 8 .   ? -56.61000 -2.89300  6.02500   1.000 32.28342  ? 407 HOH B O   1 
HETATM 5237 O O   . HOH LA 8 .   ? -42.30500 6.62300   13.73600  1.000 30.23861  ? 408 HOH B O   1 
HETATM 5238 O O   . HOH LA 8 .   ? -24.88900 5.64200   -3.41000  1.000 16.38076  ? 409 HOH B O   1 
HETATM 5239 O O   . HOH LA 8 .   ? -37.94100 -14.26000 2.43000   1.000 26.06710  ? 410 HOH B O   1 
HETATM 5240 O O   . HOH LA 8 .   ? -33.27700 1.40200   12.97300  1.000 41.61778  ? 411 HOH B O   1 
HETATM 5241 O O   . HOH LA 8 .   ? -43.32400 -12.52400 -2.91600  1.000 17.48697  ? 412 HOH B O   1 
HETATM 5242 O O   . HOH LA 8 .   ? -57.52600 14.79800  -15.23500 1.000 32.22586  ? 413 HOH B O   1 
HETATM 5243 O O   . HOH LA 8 .   ? -56.59900 -2.86000  -8.93600  1.000 33.43150  ? 414 HOH B O   1 
HETATM 5244 O O   . HOH LA 8 .   ? -31.09000 -13.57000 5.19400   1.000 35.40766  ? 415 HOH B O   1 
HETATM 5245 O O   . HOH LA 8 .   ? -48.26700 10.76000  -18.29700 1.000 33.57099  ? 416 HOH B O   1 
HETATM 5246 O O   . HOH LA 8 .   ? -25.77400 3.12800   -2.45600  1.000 21.68685  ? 417 HOH B O   1 
HETATM 5247 O O   . HOH LA 8 .   ? -57.18700 7.83400   -18.72400 1.000 48.63410  ? 418 HOH B O   1 
HETATM 5248 O O   . HOH LA 8 .   ? -34.39800 -3.27300  -9.52900  1.000 14.62509  ? 419 HOH B O   1 
HETATM 5249 O O   . HOH LA 8 .   ? -37.09600 -4.86900  -12.82700 1.000 38.11150  ? 420 HOH B O   1 
HETATM 5250 O O   . HOH LA 8 .   ? -60.44800 5.16500   2.02700   1.000 42.21693  ? 421 HOH B O   1 
HETATM 5251 O O   . HOH LA 8 .   ? -44.31400 -0.50000  -11.35700 1.000 22.07485  ? 422 HOH B O   1 
HETATM 5252 O O   . HOH LA 8 .   ? -33.25900 -3.67700  2.68000   1.000 16.87070  ? 423 HOH B O   1 
HETATM 5253 O O   . HOH LA 8 .   ? -22.47800 4.68400   -1.76600  1.000 36.45168  ? 424 HOH B O   1 
HETATM 5254 O O   . HOH LA 8 .   ? -17.97000 -3.85800  3.90000   1.000 40.81977  ? 425 HOH B O   1 
HETATM 5255 O O   . HOH LA 8 .   ? -40.23900 -2.18200  13.74500  1.000 19.16706  ? 426 HOH B O   1 
HETATM 5256 O O   . HOH LA 8 .   ? -54.40600 -6.82300  -7.28500  1.000 20.42808  ? 427 HOH B O   1 
HETATM 5257 O O   . HOH LA 8 .   ? -48.64600 7.49900   10.86800  1.000 37.82202  ? 428 HOH B O   1 
HETATM 5258 O O   . HOH LA 8 .   ? -35.09600 15.17800  -5.85400  1.000 27.09302  ? 429 HOH B O   1 
HETATM 5259 O O   . HOH LA 8 .   ? -42.86400 14.37100  -13.43000 1.000 29.25347  ? 430 HOH B O   1 
HETATM 5260 O O   . HOH LA 8 .   ? -45.44800 13.89900  -0.29700  1.000 20.49106  ? 431 HOH B O   1 
HETATM 5261 O O   . HOH LA 8 .   ? -51.34200 -6.01000  -7.73000  1.000 15.31062  ? 432 HOH B O   1 
HETATM 5262 O O   . HOH LA 8 .   ? -52.79200 3.63900   9.22300   1.000 32.58379  ? 433 HOH B O   1 
HETATM 5263 O O   . HOH LA 8 .   ? -41.76000 13.98200  8.12300   1.000 54.05741  ? 434 HOH B O   1 
HETATM 5264 O O   . HOH LA 8 .   ? -43.99700 20.82500  -9.82800  1.000 39.75468  ? 435 HOH B O   1 
HETATM 5265 O O   . HOH LA 8 .   ? -28.30800 1.87300   -12.81300 1.000 24.84139  ? 436 HOH B O   1 
HETATM 5266 O O   . HOH LA 8 .   ? -36.81300 -7.32800  -12.38500 1.000 32.02216  ? 437 HOH B O   1 
HETATM 5267 O O   . HOH LA 8 .   ? -31.34100 2.09600   -12.22300 1.000 22.65858  ? 438 HOH B O   1 
HETATM 5268 O O   . HOH LA 8 .   ? -46.85000 10.73500  2.76400   1.000 23.04618  ? 439 HOH B O   1 
HETATM 5269 O O   . HOH LA 8 .   ? -54.792   13.193    -18.129   1.000 36.46172  ? 440 HOH B O   1 
HETATM 5270 O O   . HOH LA 8 .   ? -40.86400 17.27400  8.95400   1.000 44.31940  ? 441 HOH B O   1 
HETATM 5271 O O   . HOH LA 8 .   ? -43.36600 -4.32900  -14.09600 1.000 38.98104  ? 442 HOH B O   1 
HETATM 5272 O O   . HOH LA 8 .   ? -50.08400 3.32700   12.16600  1.000 33.95987  ? 443 HOH B O   1 
HETATM 5273 O O   . HOH LA 8 .   ? -30.59200 16.96300  -8.12000  1.000 27.16154  ? 444 HOH B O   1 
HETATM 5274 O O   . HOH LA 8 .   ? -27.74300 15.12500  9.00000   1.000 47.53056  ? 445 HOH B O   1 
HETATM 5275 O O   . HOH LA 8 .   ? -37.62300 -11.50300 9.47400   1.000 31.15937  ? 446 HOH B O   1 
HETATM 5276 O O   . HOH LA 8 .   ? -19.12700 7.23100   -9.52900  1.000 26.24471  ? 447 HOH B O   1 
HETATM 5277 O O   . HOH LA 8 .   ? -37.86800 -7.65900  11.11300  1.000 22.97924  ? 448 HOH B O   1 
HETATM 5278 O O   . HOH LA 8 .   ? -50.02800 -5.10400  -11.39200 1.000 23.49525  ? 449 HOH B O   1 
HETATM 5279 O O   . HOH LA 8 .   ? -38.11000 6.95100   5.91800   1.000 28.92673  ? 450 HOH B O   1 
HETATM 5280 O O   . HOH LA 8 .   ? -38.95700 22.83200  2.45000   1.000 43.18101  ? 451 HOH B O   1 
HETATM 5281 O O   . HOH LA 8 .   ? -59.98300 2.98300   -8.22200  1.000 31.56940  ? 452 HOH B O   1 
HETATM 5282 O O   . HOH LA 8 .   ? -45.89700 -5.69500  9.14700   1.000 26.31710  ? 453 HOH B O   1 
HETATM 5283 O O   . HOH LA 8 .   ? -52.17400 0.11100   -12.90500 1.000 21.93287  ? 454 HOH B O   1 
HETATM 5284 O O   . HOH LA 8 .   ? -21.57300 -8.24800  -3.37300  1.000 25.95792  ? 455 HOH B O   1 
HETATM 5285 O O   . HOH LA 8 .   ? -28.50900 20.34900  -2.00000  1.000 51.63017  ? 456 HOH B O   1 
HETATM 5286 O O   . HOH LA 8 .   ? -18.07900 -1.96900  -7.87100  1.000 37.27715  ? 457 HOH B O   1 
HETATM 5287 O O   . HOH LA 8 .   ? -42.33700 -0.17700  7.04400   1.000 16.05570  ? 458 HOH B O   1 
HETATM 5288 O O   . HOH LA 8 .   ? -35.64600 -0.95500  15.67000  1.000 36.25882  ? 459 HOH B O   1 
HETATM 5289 O O   . HOH LA 8 .   ? -23.42100 14.23600  -7.85300  1.000 22.39761  ? 460 HOH B O   1 
HETATM 5290 O O   . HOH LA 8 .   ? -40.66400 31.41200  -1.12300  1.000 52.52768  ? 461 HOH B O   1 
HETATM 5291 O O   . HOH LA 8 .   ? -40.83300 4.64300   -16.38800 1.000 24.39312  ? 462 HOH B O   1 
HETATM 5292 O O   . HOH LA 8 .   ? -41.13700 1.44400   -16.92200 1.000 27.95164  ? 463 HOH B O   1 
HETATM 5293 O O   . HOH LA 8 .   ? -45.96600 1.90400   -0.37300  1.000 16.16219  ? 464 HOH B O   1 
HETATM 5294 O O   . HOH LA 8 .   ? -18.60800 3.88400   -13.11400 1.000 23.96260  ? 465 HOH B O   1 
HETATM 5295 O O   . HOH LA 8 .   ? -35.82300 4.67100   5.96300   1.000 22.81973  ? 466 HOH B O   1 
HETATM 5296 O O   . HOH LA 8 .   ? -55.20600 0.75200   8.05000   1.000 39.34989  ? 467 HOH B O   1 
HETATM 5297 O O   . HOH LA 8 .   ? -56.08700 -12.59800 -1.17200  1.000 34.68440  ? 468 HOH B O   1 
HETATM 5298 O O   . HOH LA 8 .   ? -31.48600 14.44500  -9.57800  1.000 41.50582  ? 469 HOH B O   1 
HETATM 5299 O O   . HOH LA 8 .   ? -52.62000 -3.93300  -10.54900 1.000 19.02369  ? 470 HOH B O   1 
HETATM 5300 O O   . HOH LA 8 .   ? -42.99400 -3.09400  -12.10400 1.000 23.22481  ? 471 HOH B O   1 
HETATM 5301 O O   . HOH LA 8 .   ? -17.57900 -4.30400  -5.88900  1.000 31.69833  ? 472 HOH B O   1 
HETATM 5302 O O   . HOH LA 8 .   ? -20.82300 -8.15700  -1.24400  1.000 28.12141  ? 473 HOH B O   1 
HETATM 5303 O O   . HOH LA 8 .   ? -25.50800 -12.97100 6.86800   1.000 46.03371  ? 474 HOH B O   1 
HETATM 5304 O O   . HOH LA 8 .   ? -24.20200 -7.83600  -8.81800  1.000 31.24170  ? 475 HOH B O   1 
HETATM 5305 O O   . HOH LA 8 .   ? -44.71500 10.03300  9.69200   1.000 37.65691  ? 476 HOH B O   1 
HETATM 5306 O O   . HOH LA 8 .   ? -27.86900 -1.69500  12.41800  1.000 37.60071  ? 477 HOH B O   1 
HETATM 5307 O O   . HOH LA 8 .   ? -39.20700 -11.29600 -12.44300 1.000 31.64126  ? 478 HOH B O   1 
HETATM 5308 O O   . HOH LA 8 .   ? -20.93800 -8.60700  7.13000   1.000 42.42296  ? 479 HOH B O   1 
HETATM 5309 O O   . HOH LA 8 .   ? -39.62500 16.17500  5.92300   1.000 42.94466  ? 480 HOH B O   1 
HETATM 5310 O O   . HOH LA 8 .   ? -27.17000 -3.35000  14.77600  1.000 40.07114  ? 481 HOH B O   1 
HETATM 5311 O O   . HOH LA 8 .   ? -50.96700 -1.64300  -10.95300 1.000 21.29644  ? 482 HOH B O   1 
HETATM 5312 O O   . HOH LA 8 .   ? -41.14300 10.21300  -18.02200 1.000 44.03705  ? 483 HOH B O   1 
HETATM 5313 O O   . HOH LA 8 .   ? -42.90300 6.05300   -18.03100 1.000 27.50476  ? 484 HOH B O   1 
HETATM 5314 O O   . HOH LA 8 .   ? -61.04800 1.64200   -5.77900  1.000 29.85640  ? 485 HOH B O   1 
HETATM 5315 O O   . HOH LA 8 .   ? -21.90800 6.79400   -3.53200  1.000 30.11071  ? 486 HOH B O   1 
HETATM 5316 O O   . HOH LA 8 .   ? -36.10400 9.05100   -11.24800 1.000 39.17853  ? 487 HOH B O   1 
HETATM 5317 O O   . HOH LA 8 .   ? -27.85200 -11.95200 6.83300   1.000 27.30371  ? 488 HOH B O   1 
HETATM 5318 O O   . HOH LA 8 .   ? -40.60200 -11.20700 8.23200   1.000 33.76660  ? 489 HOH B O   1 
HETATM 5319 O O   . HOH LA 8 .   ? -54.96700 -13.84400 -3.15700  1.000 38.37118  ? 490 HOH B O   1 
HETATM 5320 O O   . HOH LA 8 .   ? -33.00500 -15.74900 7.73000   1.000 34.08574  ? 491 HOH B O   1 
HETATM 5321 O O   . HOH LA 8 .   ? -54.11800 -13.00600 2.96900   1.000 44.27997  ? 492 HOH B O   1 
HETATM 5322 O O   . HOH LA 8 .   ? -53.10700 15.97100  -14.61000 1.000 37.13963  ? 493 HOH B O   1 
HETATM 5323 O O   . HOH LA 8 .   ? -25.46500 -4.23600  12.63100  1.000 33.74184  ? 494 HOH B O   1 
HETATM 5324 O O   . HOH LA 8 .   ? -55.88200 6.18100   7.50100   1.000 38.55515  ? 495 HOH B O   1 
HETATM 5325 O O   . HOH LA 8 .   ? -31.46700 -12.98400 -6.78300  1.000 43.49867  ? 496 HOH B O   1 
HETATM 5326 O O   . HOH LA 8 .   ? -36.53800 -1.73300  -13.64400 1.000 41.26731  ? 497 HOH B O   1 
HETATM 5327 O O   . HOH LA 8 .   ? -39.60000 -15.48300 -2.88300  1.000 38.07898  ? 498 HOH B O   1 
HETATM 5328 O O   . HOH LA 8 .   ? -29.33700 -0.91300  -14.95900 1.000 37.33397  ? 499 HOH B O   1 
HETATM 5329 O O   . HOH LA 8 .   ? -43.03800 14.22900  2.42200   1.000 40.84234  ? 500 HOH B O   1 
HETATM 5330 O O   . HOH LA 8 .   ? -29.34400 -14.90000 -2.01200  1.000 32.47224  ? 501 HOH B O   1 
HETATM 5331 O O   . HOH LA 8 .   ? -25.43200 9.75100   3.16200   1.000 38.96459  ? 502 HOH B O   1 
HETATM 5332 O O   . HOH LA 8 .   ? -57.744   -8.431    7.063     1.000 28.75240  ? 503 HOH B O   1 
HETATM 5333 O O   . HOH LA 8 .   ? -38.07300 4.84300   -18.98900 1.000 45.83817  ? 504 HOH B O   1 
HETATM 5334 O O   . HOH LA 8 .   ? -60.30000 18.78200  -3.26100  1.000 50.22961  ? 505 HOH B O   1 
HETATM 5335 O O   . HOH LA 8 .   ? -37.107   -6.130    18.325    1.000 39.30994  ? 506 HOH B O   1 
HETATM 5336 O O   . HOH LA 8 .   ? -63.42900 2.69200   -5.64600  1.000 36.35940  ? 507 HOH B O   1 
HETATM 5337 O O   . HOH LA 8 .   ? -31.33600 -9.69100  13.08200  1.000 32.21581  ? 508 HOH B O   1 
HETATM 5338 O O   . HOH LA 8 .   ? -54.50800 10.94100  3.46400   1.000 37.37411  ? 509 HOH B O   1 
HETATM 5339 O O   . HOH LA 8 .   ? -37.78400 0.55200   -12.07000 1.000 25.26186  ? 510 HOH B O   1 
HETATM 5340 O O   . HOH LA 8 .   ? -51.630   -13.998   -11.797   1.000 36.18294  ? 511 HOH B O   1 
HETATM 5341 O O   . HOH LA 8 .   ? -57.70900 7.96500   -12.97600 1.000 42.08778  ? 512 HOH B O   1 
HETATM 5342 O O   . HOH LA 8 .   ? -56.88000 5.66900   -14.26000 1.000 37.17121  ? 513 HOH B O   1 
HETATM 5343 O O   . HOH LA 8 .   ? -26.76100 16.28300  5.33400   1.000 40.37522  ? 514 HOH B O   1 
HETATM 5344 O O   . HOH LA 8 .   ? -25.89200 -3.54600  9.58200   1.000 34.29706  ? 515 HOH B O   1 
HETATM 5345 O O   . HOH LA 8 .   ? -27.96800 4.77600   9.35600   1.000 46.16336  ? 516 HOH B O   1 
HETATM 5346 O O   . HOH LA 8 .   ? -38.54600 6.76400   8.22400   1.000 44.09733  ? 517 HOH B O   1 
HETATM 5347 O O   . HOH LA 8 .   ? -56.313   11.870    -20.105   1.000 40.25421  ? 518 HOH B O   1 
HETATM 5348 O O   . HOH LA 8 .   ? -33.82500 -8.84800  16.78900  1.000 37.20385  ? 519 HOH B O   1 
HETATM 5349 O O   . HOH LA 8 .   ? -15.80000 -3.04800  -2.36900  1.000 32.73145  ? 520 HOH B O   1 
HETATM 5350 O O   . HOH LA 8 .   ? -19.26400 -5.18300  -10.65200 1.000 41.65611  ? 521 HOH B O   1 
HETATM 5351 O O   . HOH LA 8 .   ? -49.53100 -14.85800 2.94600   1.000 43.59667  ? 522 HOH B O   1 
HETATM 5352 O O   . HOH LA 8 .   ? -34.27500 -11.44500 -11.47200 1.000 39.70343  ? 523 HOH B O   1 
HETATM 5353 O O   . HOH LA 8 .   ? -53.596   -12.835   4.304     1.000 44.07202  ? 524 HOH B O   1 
HETATM 5354 O O   . HOH LA 8 .   ? -31.02000 -16.55100 2.47100   1.000 48.25191  ? 525 HOH B O   1 
HETATM 5355 O O   . HOH LA 8 .   ? -30.44200 2.17300   12.94000  1.000 43.93585  ? 526 HOH B O   1 
HETATM 5356 O O   . HOH LA 8 .   ? -40.66200 8.22100   11.88600  1.000 43.67772  ? 527 HOH B O   1 
HETATM 5357 O O   . HOH LA 8 .   ? -24.60700 -12.59700 8.90000   1.000 44.57055  ? 528 HOH B O   1 
HETATM 5358 O O   . HOH LA 8 .   ? -19.37900 2.66100   -0.68700  1.000 40.26942  ? 529 HOH B O   1 
HETATM 5359 O O   . HOH LA 8 .   ? -45.765   -14.204   6.287     1.000 39.53074  ? 530 HOH B O   1 
HETATM 5360 O O   . HOH LA 8 .   ? -50.88000 14.09500  -14.42200 1.000 37.78074  ? 531 HOH B O   1 
HETATM 5361 O O   . HOH LA 8 .   ? -42.762   -13.151   9.293     1.000 48.37802  ? 532 HOH B O   1 
HETATM 5362 O O   . HOH LA 8 .   ? -47.18000 14.09400  4.13300   1.000 44.87752  ? 533 HOH B O   1 
HETATM 5363 O O   . HOH LA 8 .   ? -40.08900 -3.53700  16.05200  1.000 30.24132  ? 534 HOH B O   1 
HETATM 5364 O O   . HOH LA 8 .   ? -62.931   21.445    -10.058   1.000 51.66112  ? 535 HOH B O   1 
HETATM 5365 O O   . HOH LA 8 .   ? -24.36500 -7.07400  -11.37400 1.000 38.43909  ? 536 HOH B O   1 
HETATM 5366 O O   . HOH LA 8 .   ? -34.06900 -0.14900  -14.72000 1.000 34.79767  ? 537 HOH B O   1 
HETATM 5367 O O   . HOH LA 8 .   ? -27.96300 22.65900  -2.52100  1.000 48.89590  ? 538 HOH B O   1 
HETATM 5368 O O   . HOH LA 8 .   ? -29.53600 -14.54600 7.23700   1.000 36.70900  ? 539 HOH B O   1 
HETATM 5369 O O   . HOH LA 8 .   ? -65.056   15.880    -12.608   1.000 50.54853  ? 540 HOH B O   1 
HETATM 5370 O O   . HOH LA 8 .   ? -40.00500 3.05000   -18.58000 1.000 39.97496  ? 541 HOH B O   1 
HETATM 5371 O O   . HOH LA 8 .   ? -57.67300 9.26000   -15.43300 1.000 44.62911  ? 542 HOH B O   1 
HETATM 5372 O O   . HOH LA 8 .   ? -59.652   -9.532    2.317     1.000 37.00397  ? 543 HOH B O   1 
HETATM 5373 O O   . HOH LA 8 .   ? -19.06200 0.50500   2.73200   1.000 32.92443  ? 544 HOH B O   1 
HETATM 5374 O O   . HOH LA 8 .   ? -39.53000 -8.91300  10.08200  1.000 33.78073  ? 545 HOH B O   1 
HETATM 5375 O O   . HOH LA 8 .   ? -38.41000 -15.35200 -5.17800  1.000 38.57028  ? 546 HOH B O   1 
HETATM 5376 O O   . HOH LA 8 .   ? -62.026   -7.672    7.361     1.000 48.55386  ? 547 HOH B O   1 
HETATM 5377 O O   . HOH LA 8 .   ? -32.20200 -2.63400  -17.94700 1.000 40.49227  ? 548 HOH B O   1 
HETATM 5378 O O   . HOH LA 8 .   ? -17.24000 -1.23900  4.64100   1.000 38.77539  ? 549 HOH B O   1 
HETATM 5379 O O   . HOH LA 8 .   ? -55.21900 4.16200   9.32400   1.000 45.04408  ? 550 HOH B O   1 
HETATM 5380 O O   . HOH LA 8 .   ? -45.05000 13.08400  2.54000   1.000 32.26389  ? 551 HOH B O   1 
HETATM 5381 O O   . HOH LA 8 .   ? -61.69700 2.52600   2.83200   1.000 44.02970  ? 552 HOH B O   1 
HETATM 5382 O O   . HOH LA 8 .   ? -62.000   22.263    -12.534   1.000 49.13994  ? 553 HOH B O   1 
HETATM 5383 O O   . HOH LA 8 .   ? -18.49000 -6.80000  -7.47100  1.000 43.19763  ? 554 HOH B O   1 
HETATM 5384 O O   . HOH LA 8 .   ? -39.50400 14.81500  9.48400   1.000 49.20556  ? 555 HOH B O   1 
HETATM 5385 O O   . HOH LA 8 .   ? -61.88200 1.12700   5.11500   1.000 52.44458  ? 556 HOH B O   1 
HETATM 5386 O O   . HOH LA 8 .   ? -31.26500 -15.69600 10.25000  1.000 45.70317  ? 557 HOH B O   1 
HETATM 5387 O O   . HOH LA 8 .   ? -65.154   22.321    -8.877    1.000 51.58901  ? 558 HOH B O   1 
HETATM 5388 O O   . HOH MA 8 .   ? -0.66200  4.66000   -33.08700 1.000 34.51642  ? 401 HOH H O   1 
HETATM 5389 O O   . HOH MA 8 .   ? -18.45500 1.90700   -22.85200 1.000 34.33105  ? 402 HOH H O   1 
HETATM 5390 O O   . HOH MA 8 .   ? 1.05700   1.93300   -45.54100 1.000 36.65188  ? 403 HOH H O   1 
HETATM 5391 O O   . HOH MA 8 .   ? 0.68600   -0.71100  -38.97600 1.000 44.13452  ? 404 HOH H O   1 
HETATM 5392 O O   . HOH MA 8 .   ? 23.85600  25.95500  -34.11000 1.000 29.57673  ? 405 HOH H O   1 
HETATM 5393 O O   . HOH MA 8 .   ? -8.13600  -7.76300  -20.34600 1.000 40.72428  ? 406 HOH H O   1 
HETATM 5394 O O   . HOH MA 8 .   ? 21.78100  33.30500  -28.25300 1.000 47.42134  ? 407 HOH H O   1 
HETATM 5395 O O   . HOH MA 8 .   ? 11.43200  15.03600  -46.51900 1.000 28.47479  ? 408 HOH H O   1 
HETATM 5396 O O   . HOH MA 8 .   ? -13.91200 -11.62000 -29.69500 1.000 45.33599  ? 409 HOH H O   1 
HETATM 5397 O O   . HOH MA 8 .   ? 27.44300  21.34500  -23.71000 1.000 35.35175  ? 410 HOH H O   1 
HETATM 5398 O O   . HOH MA 8 .   ? -20.64000 -6.51500  -13.46000 1.000 44.30875  ? 411 HOH H O   1 
HETATM 5399 O O   . HOH MA 8 .   ? -5.27900  -3.50800  -25.75000 1.000 37.55249  ? 412 HOH H O   1 
HETATM 5400 O O   . HOH MA 8 .   ? 11.94200  12.92400  -16.61500 1.000 38.63720  ? 413 HOH H O   1 
HETATM 5401 O O   . HOH MA 8 .   ? 0.02100   6.48300   -36.73600 1.000 31.91537  ? 414 HOH H O   1 
HETATM 5402 O O   . HOH MA 8 .   ? -32.93700 11.81700  -9.75700  1.000 27.61308  ? 415 HOH H O   1 
HETATM 5403 O O   . HOH MA 8 .   ? 12.95900  17.74200  -46.89300 1.000 44.18864  ? 416 HOH H O   1 
HETATM 5404 O O   . HOH MA 8 .   ? 11.17800  19.35600  -45.65900 1.000 44.09724  ? 417 HOH H O   1 
HETATM 5405 O O   . HOH MA 8 .   ? -4.94800  9.76900   -18.96000 1.000 40.20357  ? 418 HOH H O   1 
HETATM 5406 O O   . HOH MA 8 .   ? -18.93300 2.31400   -16.13300 1.000 23.89380  ? 419 HOH H O   1 
HETATM 5407 O O   . HOH MA 8 .   ? -26.97700 4.38000   -33.45400 1.000 47.53070  ? 420 HOH H O   1 
HETATM 5408 O O   . HOH MA 8 .   ? -11.37600 -4.24600  -45.15400 1.000 41.34764  ? 421 HOH H O   1 
HETATM 5409 O O   . HOH MA 8 .   ? -21.82700 4.60100   -25.70900 1.000 25.55028  ? 422 HOH H O   1 
HETATM 5410 O O   . HOH MA 8 .   ? 16.76100  23.83500  -18.82000 1.000 32.42942  ? 423 HOH H O   1 
HETATM 5411 O O   . HOH MA 8 .   ? -23.12000 -9.23700  -13.64900 1.000 50.10907  ? 424 HOH H O   1 
HETATM 5412 O O   . HOH MA 8 .   ? 10.19600  18.73600  -19.91700 1.000 43.77651  ? 425 HOH H O   1 
HETATM 5413 O O   . HOH MA 8 .   ? 26.69400  18.31500  -24.94800 1.000 38.26246  ? 426 HOH H O   1 
HETATM 5414 O O   . HOH MA 8 .   ? 32.06100  23.60400  -32.92300 1.000 53.62488  ? 427 HOH H O   1 
HETATM 5415 O O   . HOH MA 8 .   ? 7.25800   5.98000   -31.26800 1.000 31.64978  ? 428 HOH H O   1 
HETATM 5416 O O   . HOH MA 8 .   ? -31.21900 4.72500   -13.10100 1.000 23.40196  ? 429 HOH H O   1 
HETATM 5417 O O   . HOH MA 8 .   ? 26.91000  24.39800  -38.36300 1.000 47.93984  ? 430 HOH H O   1 
HETATM 5418 O O   . HOH MA 8 .   ? -7.75400  5.71900   -18.62200 1.000 34.96810  ? 431 HOH H O   1 
HETATM 5419 O O   . HOH MA 8 .   ? -25.44800 4.43100   -18.90700 1.000 23.82752  ? 432 HOH H O   1 
HETATM 5420 O O   . HOH MA 8 .   ? 1.58200   19.49100  -40.95400 1.000 30.90544  ? 433 HOH H O   1 
HETATM 5421 O O   . HOH MA 8 .   ? -33.65300 5.58200   -20.43200 1.000 39.96933  ? 434 HOH H O   1 
HETATM 5422 O O   . HOH MA 8 .   ? 7.76600   20.34600  -35.73100 1.000 23.38942  ? 435 HOH H O   1 
HETATM 5423 O O   . HOH MA 8 .   ? 25.09200  31.54500  -18.27100 1.000 41.50319  ? 436 HOH H O   1 
HETATM 5424 O O   . HOH MA 8 .   ? 24.28800  15.50400  -16.32100 1.000 38.95775  ? 437 HOH H O   1 
HETATM 5425 O O   . HOH MA 8 .   ? -21.60900 -6.40200  -20.68200 1.000 39.25211  ? 438 HOH H O   1 
HETATM 5426 O O   . HOH MA 8 .   ? 24.37900  9.48800   -31.90100 1.000 41.09335  ? 439 HOH H O   1 
HETATM 5427 O O   . HOH MA 8 .   ? 25.86100  11.44700  -30.53900 1.000 38.94376  ? 440 HOH H O   1 
HETATM 5428 O O   . HOH MA 8 .   ? -31.43800 -2.18200  -20.37900 1.000 42.43779  ? 441 HOH H O   1 
HETATM 5429 O O   . HOH MA 8 .   ? 21.24400  10.47500  -22.01100 1.000 32.52517  ? 442 HOH H O   1 
HETATM 5430 O O   . HOH MA 8 .   ? 15.58600  25.85700  -17.78000 1.000 41.72315  ? 443 HOH H O   1 
HETATM 5431 O O   . HOH MA 8 .   ? -5.85200  -3.31900  -18.97100 1.000 44.28462  ? 444 HOH H O   1 
HETATM 5432 O O   . HOH MA 8 .   ? -16.87000 -4.91300  -39.26900 1.000 36.03889  ? 445 HOH H O   1 
HETATM 5433 O O   . HOH MA 8 .   ? -8.95400  11.31600  -40.59800 1.000 38.83715  ? 446 HOH H O   1 
HETATM 5434 O O   . HOH MA 8 .   ? -10.90500 13.36800  -40.91000 1.000 43.22583  ? 447 HOH H O   1 
HETATM 5435 O O   . HOH MA 8 .   ? 1.92900   4.46600   -34.86000 1.000 32.87493  ? 448 HOH H O   1 
HETATM 5436 O O   . HOH MA 8 .   ? -2.09500  5.90600   -23.01900 1.000 47.45866  ? 449 HOH H O   1 
HETATM 5437 O O   . HOH MA 8 .   ? 5.25200   -0.15000  -38.00000 1.000 49.33731  ? 450 HOH H O   1 
HETATM 5438 O O   . HOH MA 8 .   ? 12.80500  26.99100  -23.15200 1.000 26.27092  ? 451 HOH H O   1 
HETATM 5439 O O   . HOH MA 8 .   ? -27.85900 3.62400   -19.56900 1.000 30.02861  ? 452 HOH H O   1 
HETATM 5440 O O   . HOH MA 8 .   ? -32.66500 3.53000   -23.94300 1.000 33.23338  ? 453 HOH H O   1 
HETATM 5441 O O   . HOH MA 8 .   ? -29.32300 -4.24300  -24.17900 1.000 40.39509  ? 454 HOH H O   1 
HETATM 5442 O O   . HOH MA 8 .   ? 26.57400  18.62600  -31.92400 1.000 35.40706  ? 455 HOH H O   1 
HETATM 5443 O O   . HOH MA 8 .   ? 16.68900  6.25500   -26.64700 1.000 43.75600  ? 456 HOH H O   1 
HETATM 5444 O O   . HOH MA 8 .   ? 13.45500  14.87200  -20.85400 1.000 39.68347  ? 457 HOH H O   1 
HETATM 5445 O O   . HOH MA 8 .   ? 22.07200  28.73300  -29.80600 1.000 34.65207  ? 458 HOH H O   1 
HETATM 5446 O O   . HOH MA 8 .   ? -29.72600 -2.11700  -25.33800 1.000 41.05810  ? 459 HOH H O   1 
HETATM 5447 O O   . HOH MA 8 .   ? -17.34000 16.55800  -31.74600 1.000 28.33890  ? 460 HOH H O   1 
HETATM 5448 O O   . HOH MA 8 .   ? -6.74500  12.90300  -29.95100 1.000 37.25014  ? 461 HOH H O   1 
HETATM 5449 O O   . HOH MA 8 .   ? 22.35300  6.52200   -30.59500 1.000 40.21879  ? 462 HOH H O   1 
HETATM 5450 O O   . HOH MA 8 .   ? 21.60500  22.02400  -17.67600 1.000 41.62241  ? 463 HOH H O   1 
HETATM 5451 O O   . HOH MA 8 .   ? 7.47600   13.97600  -29.35400 1.000 39.68335  ? 464 HOH H O   1 
HETATM 5452 O O   . HOH MA 8 .   ? 11.24400  19.68200  -41.76900 1.000 22.54603  ? 465 HOH H O   1 
HETATM 5453 O O   . HOH MA 8 .   ? 9.99300   16.13700  -24.38100 1.000 31.40133  ? 466 HOH H O   1 
HETATM 5454 O O   . HOH MA 8 .   ? 7.53100   6.38600   -28.44900 1.000 48.84469  ? 467 HOH H O   1 
HETATM 5455 O O   . HOH MA 8 .   ? -35.23100 9.24000   -13.69000 1.000 37.03571  ? 468 HOH H O   1 
HETATM 5456 O O   . HOH MA 8 .   ? 0.91500   9.35200   -38.93700 1.000 27.66929  ? 469 HOH H O   1 
HETATM 5457 O O   . HOH MA 8 .   ? 7.70900   19.82600  -24.58500 1.000 24.70127  ? 470 HOH H O   1 
HETATM 5458 O O   . HOH MA 8 .   ? 13.41900  16.74300  -13.96300 1.000 48.60714  ? 471 HOH H O   1 
HETATM 5459 O O   . HOH MA 8 .   ? 0.73100   15.12400  -36.50200 1.000 45.91470  ? 472 HOH H O   1 
HETATM 5460 O O   . HOH MA 8 .   ? -2.90100  1.88200   -32.89600 1.000 39.71896  ? 473 HOH H O   1 
HETATM 5461 O O   . HOH MA 8 .   ? 20.63700  17.03000  -17.01100 1.000 31.42381  ? 474 HOH H O   1 
HETATM 5462 O O   . HOH MA 8 .   ? 9.45400   24.11200  -20.82500 1.000 28.17856  ? 475 HOH H O   1 
HETATM 5463 O O   . HOH MA 8 .   ? 8.17700   20.11200  -22.09400 1.000 34.64961  ? 476 HOH H O   1 
HETATM 5464 O O   . HOH MA 8 .   ? -17.91500 9.51500   -40.26300 1.000 37.81690  ? 477 HOH H O   1 
HETATM 5465 O O   . HOH MA 8 .   ? 7.91600   13.47900  -26.67200 1.000 29.89067  ? 478 HOH H O   1 
HETATM 5466 O O   . HOH MA 8 .   ? -2.29900  7.03100   -48.86400 1.000 44.29084  ? 479 HOH H O   1 
HETATM 5467 O O   . HOH MA 8 .   ? -16.38800 7.54200   -41.83100 1.000 36.22954  ? 480 HOH H O   1 
HETATM 5468 O O   . HOH MA 8 .   ? -18.58600 4.85600   -43.44500 1.000 44.85161  ? 481 HOH H O   1 
HETATM 5469 O O   . HOH MA 8 .   ? -1.36100  -2.78800  -42.99100 1.000 45.59510  ? 482 HOH H O   1 
HETATM 5470 O O   . HOH MA 8 .   ? -7.01400  -6.14200  -43.85300 1.000 46.49803  ? 483 HOH H O   1 
HETATM 5471 O O   . HOH MA 8 .   ? 5.88700   16.50600  -29.88300 1.000 39.20296  ? 484 HOH H O   1 
HETATM 5472 O O   . HOH MA 8 .   ? 15.53300  19.65000  -15.49700 1.000 24.91191  ? 485 HOH H O   1 
HETATM 5473 O O   . HOH MA 8 .   ? 15.47800  6.29900   -42.77600 1.000 43.50425  ? 486 HOH H O   1 
HETATM 5474 O O   . HOH MA 8 .   ? -20.61500 11.45400  -37.28300 1.000 41.17679  ? 487 HOH H O   1 
HETATM 5475 O O   . HOH MA 8 .   ? -3.18000  2.83200   -24.94900 1.000 47.22787  ? 488 HOH H O   1 
HETATM 5476 O O   . HOH MA 8 .   ? -31.29400 1.12200   -15.03600 1.000 28.49007  ? 489 HOH H O   1 
HETATM 5477 O O   . HOH MA 8 .   ? -4.82000  10.05100  -43.30900 1.000 45.44797  ? 490 HOH H O   1 
HETATM 5478 O O   . HOH MA 8 .   ? -17.11600 -2.76200  -46.13900 1.000 42.57170  ? 491 HOH H O   1 
HETATM 5479 O O   . HOH MA 8 .   ? -8.40600  17.19900  -32.48200 1.000 37.13172  ? 492 HOH H O   1 
HETATM 5480 O O   . HOH MA 8 .   ? 30.19000  29.94600  -13.64500 1.000 46.82623  ? 493 HOH H O   1 
HETATM 5481 O O   . HOH MA 8 .   ? -7.94200  3.51600   -17.54500 1.000 41.72285  ? 494 HOH H O   1 
HETATM 5482 O O   . HOH MA 8 .   ? -16.74100 -7.39800  -12.41900 1.000 38.68784  ? 495 HOH H O   1 
HETATM 5483 O O   . HOH MA 8 .   ? -3.64200  9.44000   -27.06200 1.000 39.26642  ? 496 HOH H O   1 
HETATM 5484 O O   . HOH MA 8 .   ? 0.91600   17.12600  -35.46200 1.000 39.02927  ? 497 HOH H O   1 
HETATM 5485 O O   . HOH MA 8 .   ? 1.93700   11.03400  -46.48800 1.000 41.94502  ? 498 HOH H O   1 
HETATM 5486 O O   . HOH MA 8 .   ? -8.03600  6.99300   -48.52100 1.000 40.23505  ? 499 HOH H O   1 
HETATM 5487 O O   . HOH MA 8 .   ? 28.80200  20.85600  -33.03000 1.000 46.56089  ? 500 HOH H O   1 
HETATM 5488 O O   . HOH MA 8 .   ? -1.04100  14.60400  -40.31300 1.000 41.68309  ? 501 HOH H O   1 
HETATM 5489 O O   . HOH MA 8 .   ? 4.39700   11.62900  -28.56600 1.000 39.59951  ? 502 HOH H O   1 
HETATM 5490 O O   . HOH MA 8 .   ? 20.48200  9.84300   -36.97100 1.000 35.10312  ? 503 HOH H O   1 
HETATM 5491 O O   . HOH MA 8 .   ? 7.77800   20.78700  -46.50300 1.000 31.99716  ? 504 HOH H O   1 
HETATM 5492 O O   . HOH MA 8 .   ? -23.274   -6.394    -34.553   1.000 35.90051  ? 505 HOH H O   1 
HETATM 5493 O O   . HOH MA 8 .   ? 14.25600  3.73700   -41.69100 1.000 49.03605  ? 506 HOH H O   1 
HETATM 5494 O O   . HOH MA 8 .   ? 22.02100  19.24000  -16.92200 1.000 47.02781  ? 507 HOH H O   1 
HETATM 5495 O O   . HOH MA 8 .   ? -26.81300 -0.69600  -35.20100 1.000 33.74785  ? 508 HOH H O   1 
HETATM 5496 O O   . HOH MA 8 .   ? 26.11300  21.96100  -26.09400 1.000 44.16087  ? 509 HOH H O   1 
HETATM 5497 O O   . HOH MA 8 .   ? -22.46000 11.16800  -35.07800 1.000 37.20227  ? 510 HOH H O   1 
HETATM 5498 O O   . HOH MA 8 .   ? 9.61000   17.98900  -48.01500 1.000 38.08029  ? 511 HOH H O   1 
HETATM 5499 O O   . HOH MA 8 .   ? 22.13700  30.62500  -27.83600 1.000 35.90538  ? 512 HOH H O   1 
HETATM 5500 O O   . HOH MA 8 .   ? -6.44200  13.17200  -32.94600 1.000 36.89180  ? 513 HOH H O   1 
HETATM 5501 O O   . HOH MA 8 .   ? -25.98300 -7.67700  -20.87300 1.000 37.54558  ? 514 HOH H O   1 
HETATM 5502 O O   . HOH MA 8 .   ? 19.58400  18.90000  -15.75000 1.000 42.01466  ? 515 HOH H O   1 
HETATM 5503 O O   . HOH MA 8 .   ? 23.39700  32.46700  -34.14700 1.000 45.83661  ? 516 HOH H O   1 
HETATM 5504 O O   . HOH MA 8 .   ? 15.57700  13.60200  -47.71900 1.000 46.25459  ? 517 HOH H O   1 
HETATM 5505 O O   . HOH MA 8 .   ? -11.69500 21.60000  -33.65000 1.000 46.06635  ? 518 HOH H O   1 
HETATM 5506 O O   . HOH MA 8 .   ? -19.16200 9.00300   -42.56400 1.000 43.52113  ? 519 HOH H O   1 
HETATM 5507 O O   . HOH MA 8 .   ? 20.678    3.944     -28.428   1.000 44.77556  ? 520 HOH H O   1 
HETATM 5508 O O   . HOH MA 8 .   ? 22.05500  8.33700   -23.09100 1.000 45.81587  ? 521 HOH H O   1 
HETATM 5509 O O   . HOH MA 8 .   ? -2.00200  11.21800  -42.41400 1.000 51.13578  ? 522 HOH H O   1 
HETATM 5510 O O   . HOH MA 8 .   ? -6.63700  15.95300  -32.61300 1.000 34.71250  ? 523 HOH H O   1 
HETATM 5511 O O   . HOH MA 8 .   ? 15.50400  23.84600  -13.01600 1.000 46.66716  ? 524 HOH H O   1 
HETATM 5512 O O   . HOH MA 8 .   ? 2.17600   -0.31400  -43.76600 1.000 48.54444  ? 525 HOH H O   1 
HETATM 5513 O O   . HOH MA 8 .   ? -4.02400  6.07400   -51.62000 1.000 43.46649  ? 526 HOH H O   1 
HETATM 5514 O O   . HOH MA 8 .   ? 3.71100   17.20900  -29.23800 1.000 32.39119  ? 527 HOH H O   1 
HETATM 5515 O O   . HOH MA 8 .   ? -14.31100 5.11900   -13.42700 1.000 41.09031  ? 528 HOH H O   1 
HETATM 5516 O O   . HOH MA 8 .   ? 1.09900   -1.95100  -42.77300 1.000 44.82401  ? 529 HOH H O   1 
HETATM 5517 O O   . HOH MA 8 .   ? -2.42200  5.51300   -54.02300 1.000 48.27992  ? 530 HOH H O   1 
HETATM 5518 O O   . HOH MA 8 .   ? -36.55100 10.12200  -17.45200 1.000 42.25804  ? 531 HOH H O   1 
HETATM 5519 O O   . HOH MA 8 .   ? 12.83500  12.88800  -48.52400 1.000 46.75779  ? 532 HOH H O   1 
HETATM 5520 O O   . HOH MA 8 .   ? 7.02300   16.13100  -24.98700 1.000 36.71599  ? 533 HOH H O   1 
HETATM 5521 O O   . HOH MA 8 .   ? 11.18700  16.72900  -22.02600 1.000 36.43201  ? 534 HOH H O   1 
HETATM 5522 O O   . HOH MA 8 .   ? -18.71800 6.21300   -45.64600 1.000 52.76047  ? 535 HOH H O   1 
HETATM 5523 O O   . HOH MA 8 .   ? -1.56800  12.32300  -44.07700 1.000 49.94225  ? 536 HOH H O   1 
HETATM 5524 O O   . HOH MA 8 .   ? 17.73000  21.15700  -15.11200 1.000 45.07094  ? 537 HOH H O   1 
HETATM 5525 O O   . HOH MA 8 .   ? 18.96100  22.99900  -16.85500 1.000 35.15171  ? 538 HOH H O   1 
HETATM 5526 O O   . HOH NA 8 .   ? 6.04800   43.06800  -41.53700 1.000 42.57632  ? 401 HOH L O   1 
HETATM 5527 O O   . HOH NA 8 .   ? 10.32300  23.92300  -14.86400 1.000 46.88744  ? 402 HOH L O   1 
HETATM 5528 O O   . HOH NA 8 .   ? -38.45900 14.38900  -19.29700 1.000 50.81345  ? 403 HOH L O   1 
HETATM 5529 O O   . HOH NA 8 .   ? 13.21500  20.77200  -43.21200 1.000 28.79517  ? 404 HOH L O   1 
HETATM 5530 O O   . HOH NA 8 .   ? -23.87600 25.69100  -12.30500 1.000 32.90804  ? 405 HOH L O   1 
HETATM 5531 O O   . HOH NA 8 .   ? -4.968    37.723    -17.204   1.000 18.96029  ? 406 HOH L O   1 
HETATM 5532 O O   . HOH NA 8 .   ? 10.42100  23.74800  -44.23000 1.000 20.49829  ? 407 HOH L O   1 
HETATM 5533 O O   . HOH NA 8 .   ? -23.55200 17.57800  -32.50000 1.000 30.17649  ? 408 HOH L O   1 
HETATM 5534 O O   . HOH NA 8 .   ? -5.00100  32.75000  -24.38300 1.000 31.92247  ? 409 HOH L O   1 
HETATM 5535 O O   . HOH NA 8 .   ? -3.16100  38.69400  -30.78500 1.000 38.61205  ? 410 HOH L O   1 
HETATM 5536 O O   . HOH NA 8 .   ? -19.33900 26.39400  -10.51000 1.000 23.39646  ? 411 HOH L O   1 
HETATM 5537 O O   . HOH NA 8 .   ? -7.53700  20.61000  -25.80500 1.000 30.04630  ? 412 HOH L O   1 
HETATM 5538 O O   . HOH NA 8 .   ? 15.18000  43.37900  -37.03900 1.000 31.92175  ? 413 HOH L O   1 
HETATM 5539 O O   . HOH NA 8 .   ? 4.56400   33.70000  -39.15100 1.000 22.52585  ? 414 HOH L O   1 
HETATM 5540 O O   . HOH NA 8 .   ? -4.87600  24.28200  -8.12600  1.000 26.75852  ? 415 HOH L O   1 
HETATM 5541 O O   . HOH NA 8 .   ? -23.68200 25.80400  -15.06300 1.000 25.73869  ? 416 HOH L O   1 
HETATM 5542 O O   . HOH NA 8 .   ? -19.47600 25.56700  -7.98800  1.000 39.82906  ? 417 HOH L O   1 
HETATM 5543 O O   . HOH NA 8 .   ? 7.38600   31.09000  -40.64800 1.000 19.60048  ? 418 HOH L O   1 
HETATM 5544 O O   . HOH NA 8 .   ? 12.58600  33.44800  -23.36400 1.000 30.11903  ? 419 HOH L O   1 
HETATM 5545 O O   . HOH NA 8 .   ? 6.17600   29.47600  -42.51100 1.000 26.87955  ? 420 HOH L O   1 
HETATM 5546 O O   . HOH NA 8 .   ? -10.000   32.440    -7.206    1.000 22.56731  ? 421 HOH L O   1 
HETATM 5547 O O   . HOH NA 8 .   ? 7.44700   32.60000  -42.76600 1.000 36.87329  ? 422 HOH L O   1 
HETATM 5548 O O   . HOH NA 8 .   ? 9.18300   21.64400  -42.43100 1.000 23.19116  ? 423 HOH L O   1 
HETATM 5549 O O   . HOH NA 8 .   ? -12.13500 8.41900   -18.25400 1.000 16.95805  ? 424 HOH L O   1 
HETATM 5550 O O   . HOH NA 8 .   ? -7.39600  21.01000  -9.44300  1.000 28.44442  ? 425 HOH L O   1 
HETATM 5551 O O   . HOH NA 8 .   ? -26.71900 23.06000  -10.99300 1.000 40.27719  ? 426 HOH L O   1 
HETATM 5552 O O   . HOH NA 8 .   ? 8.49600   39.72600  -38.99100 1.000 22.76186  ? 427 HOH L O   1 
HETATM 5553 O O   . HOH NA 8 .   ? -2.39300  17.21600  -22.09400 1.000 40.71891  ? 428 HOH L O   1 
HETATM 5554 O O   . HOH NA 8 .   ? -2.45700  25.86600  -25.71800 1.000 33.46656  ? 429 HOH L O   1 
HETATM 5555 O O   . HOH NA 8 .   ? 9.07700   24.41700  -37.73400 1.000 19.97599  ? 430 HOH L O   1 
HETATM 5556 O O   . HOH NA 8 .   ? -12.13800 34.56100  -8.21700  1.000 36.95710  ? 431 HOH L O   1 
HETATM 5557 O O   . HOH NA 8 .   ? 5.85100   28.28800  -46.45200 1.000 23.97924  ? 432 HOH L O   1 
HETATM 5558 O O   . HOH NA 8 .   ? 21.51100  40.11700  -37.94200 1.000 48.97148  ? 433 HOH L O   1 
HETATM 5559 O O   . HOH NA 8 .   ? -2.25400  24.39700  -10.52600 1.000 26.74866  ? 434 HOH L O   1 
HETATM 5560 O O   . HOH NA 8 .   ? 1.70700   39.51300  -31.35300 1.000 23.26436  ? 435 HOH L O   1 
HETATM 5561 O O   . HOH NA 8 .   ? -8.67900  29.56000  -26.65300 1.000 31.49297  ? 436 HOH L O   1 
HETATM 5562 O O   . HOH NA 8 .   ? -6.04600  11.44500  -25.61600 1.000 38.87355  ? 437 HOH L O   1 
HETATM 5563 O O   . HOH NA 8 .   ? -14.54500 10.11500  -16.42200 1.000 22.16262  ? 438 HOH L O   1 
HETATM 5564 O O   . HOH NA 8 .   ? -23.57900 21.03800  -10.68800 1.000 22.46389  ? 439 HOH L O   1 
HETATM 5565 O O   . HOH NA 8 .   ? -28.00500 17.46800  -9.28800  1.000 28.02341  ? 440 HOH L O   1 
HETATM 5566 O O   . HOH NA 8 .   ? 14.849    46.582    -34.652   1.000 45.35698  ? 441 HOH L O   1 
HETATM 5567 O O   . HOH NA 8 .   ? 9.76200   22.00600  -34.90800 1.000 21.57515  ? 442 HOH L O   1 
HETATM 5568 O O   . HOH NA 8 .   ? 4.70000   25.96800  -24.28800 1.000 20.62565  ? 443 HOH L O   1 
HETATM 5569 O O   . HOH NA 8 .   ? -8.40400  31.68500  -26.94800 1.000 35.45052  ? 444 HOH L O   1 
HETATM 5570 O O   . HOH NA 8 .   ? -32.50900 24.90100  -19.33700 1.000 46.17772  ? 445 HOH L O   1 
HETATM 5571 O O   . HOH NA 8 .   ? -14.88500 28.52200  -6.22300  1.000 36.72565  ? 446 HOH L O   1 
HETATM 5572 O O   . HOH NA 8 .   ? 9.05100   30.92300  -46.38200 1.000 17.61955  ? 447 HOH L O   1 
HETATM 5573 O O   . HOH NA 8 .   ? -25.39800 21.00400  -17.87300 1.000 21.33654  ? 448 HOH L O   1 
HETATM 5574 O O   . HOH NA 8 .   ? -15.71600 10.93100  -13.91200 1.000 26.34097  ? 449 HOH L O   1 
HETATM 5575 O O   . HOH NA 8 .   ? 16.06400  27.16100  -52.39900 1.000 31.60495  ? 450 HOH L O   1 
HETATM 5576 O O   . HOH NA 8 .   ? 6.32300   28.30700  -23.99400 1.000 17.84329  ? 451 HOH L O   1 
HETATM 5577 O O   . HOH NA 8 .   ? -9.65100  38.30800  -17.74300 1.000 29.10723  ? 452 HOH L O   1 
HETATM 5578 O O   . HOH NA 8 .   ? -6.44900  24.37000  -23.59800 1.000 23.76010  ? 453 HOH L O   1 
HETATM 5579 O O   . HOH NA 8 .   ? -21.23800 10.69400  -32.37700 1.000 22.85985  ? 454 HOH L O   1 
HETATM 5580 O O   . HOH NA 8 .   ? -3.63100  22.00000  -24.85600 1.000 45.67098  ? 455 HOH L O   1 
HETATM 5581 O O   . HOH NA 8 .   ? -5.28200  37.44000  -24.91800 1.000 43.37585  ? 456 HOH L O   1 
HETATM 5582 O O   . HOH NA 8 .   ? 18.98000  37.38400  -45.46100 1.000 27.44643  ? 457 HOH L O   1 
HETATM 5583 O O   . HOH NA 8 .   ? 2.62300   32.43100  -36.83300 1.000 36.46750  ? 458 HOH L O   1 
HETATM 5584 O O   . HOH NA 8 .   ? -27.00200 11.66800  -19.13600 1.000 23.18046  ? 459 HOH L O   1 
HETATM 5585 O O   . HOH NA 8 .   ? -8.63300  41.09300  -19.56200 1.000 45.04044  ? 460 HOH L O   1 
HETATM 5586 O O   . HOH NA 8 .   ? -28.58100 10.16300  -36.84600 1.000 51.83667  ? 461 HOH L O   1 
HETATM 5587 O O   . HOH NA 8 .   ? -9.30900  20.46700  -14.00800 1.000 19.11465  ? 462 HOH L O   1 
HETATM 5588 O O   . HOH NA 8 .   ? 0.24000   22.27000  -30.62700 1.000 36.65374  ? 463 HOH L O   1 
HETATM 5589 O O   . HOH NA 8 .   ? 2.49400   20.65100  -24.30000 1.000 40.87834  ? 464 HOH L O   1 
HETATM 5590 O O   . HOH NA 8 .   ? -28.47200 11.44300  -32.36400 1.000 42.70158  ? 465 HOH L O   1 
HETATM 5591 O O   . HOH NA 8 .   ? -16.26100 15.88400  -6.23200  1.000 33.88830  ? 466 HOH L O   1 
HETATM 5592 O O   . HOH NA 8 .   ? -9.34300  36.56400  -12.04800 1.000 24.89448  ? 467 HOH L O   1 
HETATM 5593 O O   . HOH NA 8 .   ? -15.25500 10.16100  -11.15000 1.000 41.96479  ? 468 HOH L O   1 
HETATM 5594 O O   . HOH NA 8 .   ? 15.53400  42.05700  -40.85400 1.000 36.26337  ? 469 HOH L O   1 
HETATM 5595 O O   . HOH NA 8 .   ? 2.84400   46.34400  -29.22300 1.000 41.37694  ? 470 HOH L O   1 
HETATM 5596 O O   . HOH NA 8 .   ? 25.68300  24.63600  -55.34000 1.000 35.55181  ? 471 HOH L O   1 
HETATM 5597 O O   . HOH NA 8 .   ? 9.30700   26.91700  -20.60700 1.000 34.86227  ? 472 HOH L O   1 
HETATM 5598 O O   . HOH NA 8 .   ? -8.02000  11.83000  -17.39700 1.000 41.61613  ? 473 HOH L O   1 
HETATM 5599 O O   . HOH NA 8 .   ? -2.77300  33.83200  -27.41600 1.000 23.90338  ? 474 HOH L O   1 
HETATM 5600 O O   . HOH NA 8 .   ? -8.71700  15.55500  -17.75000 1.000 29.98941  ? 475 HOH L O   1 
HETATM 5601 O O   . HOH NA 8 .   ? 10.52900  35.07700  -23.21400 1.000 27.24963  ? 476 HOH L O   1 
HETATM 5602 O O   . HOH NA 8 .   ? 16.01400  37.24700  -28.72100 1.000 24.22497  ? 477 HOH L O   1 
HETATM 5603 O O   . HOH NA 8 .   ? 8.37400   40.73700  -22.59200 1.000 27.06752  ? 478 HOH L O   1 
HETATM 5604 O O   . HOH NA 8 .   ? 7.58200   24.23900  -51.20000 1.000 42.56107  ? 479 HOH L O   1 
HETATM 5605 O O   . HOH NA 8 .   ? 17.59800  39.81800  -28.91800 1.000 48.54586  ? 480 HOH L O   1 
HETATM 5606 O O   . HOH NA 8 .   ? -24.28800 27.22300  -28.24600 1.000 38.11828  ? 481 HOH L O   1 
HETATM 5607 O O   . HOH NA 8 .   ? 8.15800   27.04000  -17.91200 1.000 38.49558  ? 482 HOH L O   1 
HETATM 5608 O O   . HOH NA 8 .   ? -10.35400 32.48000  -28.04800 1.000 38.10813  ? 483 HOH L O   1 
HETATM 5609 O O   . HOH NA 8 .   ? 13.92400  39.03600  -28.09200 1.000 42.90261  ? 484 HOH L O   1 
HETATM 5610 O O   . HOH NA 8 .   ? 3.17700   26.18400  -41.26800 1.000 23.28680  ? 485 HOH L O   1 
HETATM 5611 O O   . HOH NA 8 .   ? -6.81500  18.72100  -13.97800 1.000 34.63014  ? 486 HOH L O   1 
HETATM 5612 O O   . HOH NA 8 .   ? -12.09400 34.66200  -24.76500 1.000 30.60983  ? 487 HOH L O   1 
HETATM 5613 O O   . HOH NA 8 .   ? -14.54500 20.21100  -33.48000 1.000 36.93641  ? 488 HOH L O   1 
HETATM 5614 O O   . HOH NA 8 .   ? -14.92400 36.23300  -13.81400 1.000 30.84084  ? 489 HOH L O   1 
HETATM 5615 O O   . HOH NA 8 .   ? -20.56700 13.67300  -32.18100 1.000 23.30845  ? 490 HOH L O   1 
HETATM 5616 O O   . HOH NA 8 .   ? -21.37900 30.81700  -22.98100 1.000 34.53150  ? 491 HOH L O   1 
HETATM 5617 O O   . HOH NA 8 .   ? 6.36000   34.80400  -16.97700 1.000 24.59392  ? 492 HOH L O   1 
HETATM 5618 O O   . HOH NA 8 .   ? 9.30100   31.37900  -17.66300 1.000 45.48489  ? 493 HOH L O   1 
HETATM 5619 O O   . HOH NA 8 .   ? 13.67500  26.63000  -50.69400 1.000 25.26792  ? 494 HOH L O   1 
HETATM 5620 O O   . HOH NA 8 .   ? -0.56100  40.27000  -30.68600 1.000 37.25341  ? 495 HOH L O   1 
HETATM 5621 O O   . HOH NA 8 .   ? 27.57800  33.94300  -38.65800 1.000 42.74513  ? 496 HOH L O   1 
HETATM 5622 O O   . HOH NA 8 .   ? -8.42800  14.59400  -20.00600 1.000 21.57249  ? 497 HOH L O   1 
HETATM 5623 O O   . HOH NA 8 .   ? 11.36100  45.36400  -27.62000 1.000 40.42983  ? 498 HOH L O   1 
HETATM 5624 O O   . HOH NA 8 .   ? 3.92100   42.67300  -19.89300 1.000 35.70364  ? 499 HOH L O   1 
HETATM 5625 O O   . HOH NA 8 .   ? -21.27100 28.23000  -31.70000 1.000 46.50198  ? 500 HOH L O   1 
HETATM 5626 O O   . HOH NA 8 .   ? -20.40500 22.29500  -7.51300  1.000 35.91479  ? 501 HOH L O   1 
HETATM 5627 O O   . HOH NA 8 .   ? 15.97500  24.61800  -52.77800 1.000 25.99770  ? 502 HOH L O   1 
HETATM 5628 O O   . HOH NA 8 .   ? -10.16100 21.57600  -29.24600 1.000 40.69413  ? 503 HOH L O   1 
HETATM 5629 O O   . HOH NA 8 .   ? 6.94100   43.68900  -33.26700 1.000 27.65231  ? 504 HOH L O   1 
HETATM 5630 O O   . HOH NA 8 .   ? -7.467    31.531    -7.913    1.000 26.75092  ? 505 HOH L O   1 
HETATM 5631 O O   . HOH NA 8 .   ? 10.45500  44.56900  -25.63300 1.000 45.52344  ? 506 HOH L O   1 
HETATM 5632 O O   . HOH NA 8 .   ? -23.61000 17.39900  -7.63400  1.000 27.87409  ? 507 HOH L O   1 
HETATM 5633 O O   . HOH NA 8 .   ? 28.37700  25.30700  -45.49500 1.000 45.61588  ? 508 HOH L O   1 
HETATM 5634 O O   . HOH NA 8 .   ? -1.05600  26.29400  -29.33000 1.000 27.12309  ? 509 HOH L O   1 
HETATM 5635 O O   . HOH NA 8 .   ? 3.01800   21.06000  -26.76200 1.000 32.90882  ? 510 HOH L O   1 
HETATM 5636 O O   . HOH NA 8 .   ? 20.83100  32.37100  -32.54300 1.000 32.51054  ? 511 HOH L O   1 
HETATM 5637 O O   . HOH NA 8 .   ? 3.804     31.188    -50.001   1.000 43.14497  ? 512 HOH L O   1 
HETATM 5638 O O   . HOH NA 8 .   ? 29.84400  15.96200  -39.27900 1.000 48.52486  ? 513 HOH L O   1 
HETATM 5639 O O   . HOH NA 8 .   ? 6.95700   43.69200  -39.42100 1.000 39.12349  ? 514 HOH L O   1 
HETATM 5640 O O   . HOH NA 8 .   ? 5.50600   31.10100  -46.44400 1.000 26.54106  ? 515 HOH L O   1 
HETATM 5641 O O   . HOH NA 8 .   ? 0.14400   42.83900  -20.84700 1.000 20.49344  ? 516 HOH L O   1 
HETATM 5642 O O   . HOH NA 8 .   ? 23.29800  23.28300  -35.97200 1.000 45.18129  ? 517 HOH L O   1 
HETATM 5643 O O   . HOH NA 8 .   ? -2.43700  40.26300  -22.89600 1.000 32.95338  ? 518 HOH L O   1 
HETATM 5644 O O   . HOH NA 8 .   ? 20.08500  34.38800  -30.02500 1.000 32.47027  ? 519 HOH L O   1 
HETATM 5645 O O   . HOH NA 8 .   ? 1.49100   24.85400  -12.82300 1.000 50.34835  ? 520 HOH L O   1 
HETATM 5646 O O   . HOH NA 8 .   ? -18.26000 9.03200   -13.63600 1.000 31.84348  ? 521 HOH L O   1 
HETATM 5647 O O   . HOH NA 8 .   ? 1.37500   31.75800  -34.28500 1.000 27.73321  ? 522 HOH L O   1 
HETATM 5648 O O   . HOH NA 8 .   ? -28.20300 22.59100  -32.14900 1.000 37.40495  ? 523 HOH L O   1 
HETATM 5649 O O   . HOH NA 8 .   ? -16.84000 30.76800  -31.01700 1.000 33.56337  ? 524 HOH L O   1 
HETATM 5650 O O   . HOH NA 8 .   ? -21.91700 20.12800  -34.04100 1.000 42.43461  ? 525 HOH L O   1 
HETATM 5651 O O   . HOH NA 8 .   ? 17.33700  42.80000  -34.37700 1.000 35.90648  ? 526 HOH L O   1 
HETATM 5652 O O   . HOH NA 8 .   ? -5.72600  26.21300  -30.52000 1.000 37.35023  ? 527 HOH L O   1 
HETATM 5653 O O   . HOH NA 8 .   ? 21.98100  37.56100  -35.06400 1.000 27.88890  ? 528 HOH L O   1 
HETATM 5654 O O   . HOH NA 8 .   ? 21.20400  19.57200  -53.26600 1.000 34.01245  ? 529 HOH L O   1 
HETATM 5655 O O   . HOH NA 8 .   ? 25.51500  35.59900  -52.11400 1.000 40.89610  ? 530 HOH L O   1 
HETATM 5656 O O   . HOH NA 8 .   ? 3.31700   26.82800  -44.14700 1.000 42.34407  ? 531 HOH L O   1 
HETATM 5657 O O   . HOH NA 8 .   ? -37.83600 12.77300  -29.89400 1.000 47.27617  ? 532 HOH L O   1 
HETATM 5658 O O   . HOH NA 8 .   ? -2.39800  44.44500  -24.20500 1.000 37.71343  ? 533 HOH L O   1 
HETATM 5659 O O   . HOH NA 8 .   ? -34.50600 8.56300   -24.02100 1.000 39.17254  ? 534 HOH L O   1 
HETATM 5660 O O   . HOH NA 8 .   ? -13.27100 23.90500  -30.72000 1.000 37.16256  ? 535 HOH L O   1 
HETATM 5661 O O   . HOH NA 8 .   ? 27.35400  32.44300  -51.36100 1.000 39.21074  ? 536 HOH L O   1 
HETATM 5662 O O   . HOH NA 8 .   ? -12.80100 23.78500  -6.37800  1.000 37.74158  ? 537 HOH L O   1 
HETATM 5663 O O   . HOH NA 8 .   ? -5.89500  20.96800  -28.64600 1.000 37.70786  ? 538 HOH L O   1 
HETATM 5664 O O   . HOH NA 8 .   ? 5.64700   24.75300  -47.07100 1.000 38.15946  ? 539 HOH L O   1 
HETATM 5665 O O   . HOH NA 8 .   ? 7.51500   43.17300  -23.44300 1.000 41.74757  ? 540 HOH L O   1 
HETATM 5666 O O   . HOH NA 8 .   ? -0.46600  21.78100  -33.08600 1.000 42.59217  ? 541 HOH L O   1 
HETATM 5667 O O   . HOH NA 8 .   ? -5.58100  12.45200  -27.56800 1.000 43.78673  ? 542 HOH L O   1 
HETATM 5668 O O   . HOH NA 8 .   ? -10.48500 36.59400  -9.77000  1.000 32.73279  ? 543 HOH L O   1 
HETATM 5669 O O   . HOH NA 8 .   ? 2.63400   23.89500  -42.94900 1.000 34.65326  ? 544 HOH L O   1 
HETATM 5670 O O   . HOH NA 8 .   ? 8.61000   23.70700  -46.63600 1.000 27.82589  ? 545 HOH L O   1 
HETATM 5671 O O   . HOH NA 8 .   ? 18.96500  39.79100  -43.50200 1.000 38.89810  ? 546 HOH L O   1 
HETATM 5672 O O   . HOH NA 8 .   ? -30.35600 15.37100  -11.80200 1.000 46.31378  ? 547 HOH L O   1 
HETATM 5673 O O   . HOH NA 8 .   ? 11.91300  31.12800  -20.89300 1.000 42.96258  ? 548 HOH L O   1 
HETATM 5674 O O   . HOH NA 8 .   ? -30.87300 10.88800  -33.11600 1.000 48.08366  ? 549 HOH L O   1 
HETATM 5675 O O   . HOH NA 8 .   ? -30.40600 23.18400  -13.07600 1.000 41.75277  ? 550 HOH L O   1 
HETATM 5676 O O   . HOH NA 8 .   ? -0.83700  20.38300  -23.55600 1.000 35.51867  ? 551 HOH L O   1 
HETATM 5677 O O   . HOH NA 8 .   ? -12.39100 21.70800  -4.49100  1.000 44.53730  ? 552 HOH L O   1 
HETATM 5678 O O   . HOH NA 8 .   ? 11.82000  27.90600  -20.76100 1.000 33.58767  ? 553 HOH L O   1 
HETATM 5679 O O   . HOH NA 8 .   ? 13.45600  44.88200  -29.91700 1.000 40.01787  ? 554 HOH L O   1 
HETATM 5680 O O   . HOH NA 8 .   ? 3.89000   34.39900  -40.75500 1.000 41.20096  ? 555 HOH L O   1 
HETATM 5681 O O   . HOH NA 8 .   ? -32.12100 14.84500  -13.73300 1.000 41.46128  ? 556 HOH L O   1 
HETATM 5682 O O   . HOH NA 8 .   ? 7.12400   46.06200  -34.66900 1.000 35.66836  ? 557 HOH L O   1 
HETATM 5683 O O   . HOH NA 8 .   ? -8.65400  18.13400  -9.65700  1.000 40.33298  ? 558 HOH L O   1 
HETATM 5684 O O   . HOH NA 8 .   ? -12.98200 21.93500  -2.46100  1.000 49.52626  ? 559 HOH L O   1 
HETATM 5685 O O   . HOH NA 8 .   ? -5.78600  21.81100  -24.01700 1.000 28.58335  ? 560 HOH L O   1 
HETATM 5686 O O   . HOH NA 8 .   ? 20.84400  40.53200  -41.71400 1.000 48.02113  ? 561 HOH L O   1 
HETATM 5687 O O   . HOH NA 8 .   ? 6.66100   33.29200  -44.54900 1.000 36.46667  ? 562 HOH L O   1 
HETATM 5688 O O   . HOH NA 8 .   ? -4.73100  40.18400  -19.27500 1.000 44.76075  ? 563 HOH L O   1 
HETATM 5689 O O   . HOH NA 8 .   ? -4.17300  39.02400  -27.82500 1.000 50.01767  ? 564 HOH L O   1 
HETATM 5690 O O   . HOH NA 8 .   ? 3.42200   28.73300  -42.77800 1.000 46.04917  ? 565 HOH L O   1 
HETATM 5691 O O   . HOH NA 8 .   ? -0.81900  23.70100  -12.80300 1.000 46.08559  ? 566 HOH L O   1 
HETATM 5692 O O   . HOH NA 8 .   ? -19.53700 19.75800  -34.64800 1.000 44.96665  ? 567 HOH L O   1 
HETATM 5693 O O   . HOH NA 8 .   ? -11.65800 8.67700   -15.87000 1.000 37.59495  ? 568 HOH L O   1 
HETATM 5694 O O   . HOH NA 8 .   ? -3.77700  39.68400  -26.18100 1.000 50.92905  ? 569 HOH L O   1 
HETATM 5695 O O   . HOH NA 8 .   ? 0.18700   42.57800  -32.60900 1.000 46.03491  ? 570 HOH L O   1 
HETATM 5696 O O   . HOH NA 8 .   ? 0.27300   30.35100  -34.53700 1.000 46.67565  ? 571 HOH L O   1 
HETATM 5697 O O   . HOH NA 8 .   ? -3.604    40.786    -17.955   1.000 37.88072  ? 572 HOH L O   1 
HETATM 5698 O O   . HOH NA 8 .   ? -1.12100  21.86500  -15.25000 1.000 38.37988  ? 573 HOH L O   1 
HETATM 5699 O O   . HOH NA 8 .   ? 3.95300   22.69400  -47.95300 1.000 52.98685  ? 574 HOH L O   1 
HETATM 5700 O O   . HOH NA 8 .   ? 0.51100   18.37300  -24.74600 1.000 49.54880  ? 575 HOH L O   1 
HETATM 5701 O O   . HOH NA 8 .   ? -37.00100 12.84500  -17.66000 1.000 43.64075  ? 576 HOH L O   1 
HETATM 5702 O O   . HOH NA 8 .   ? -2.48300  19.83400  -21.11000 1.000 37.60938  ? 577 HOH L O   1 
HETATM 5703 O O   . HOH NA 8 .   ? -6.374    18.133    -10.994   1.000 54.18278  ? 578 HOH L O   1 
HETATM 5704 O O   . HOH NA 8 .   ? 1.30700   19.16000  -28.44100 1.000 41.31294  ? 579 HOH L O   1 
HETATM 5705 O O   . HOH NA 8 .   ? -9.81000  20.34800  -5.21500  1.000 34.13155  ? 580 HOH L O   1 
HETATM 5706 O O   . HOH NA 8 .   ? 12.28200  31.89000  -18.46600 1.000 50.86513  ? 581 HOH L O   1 
# 
