data_9CT1
# 
_entry.id   9CT1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CT1         pdb_00009ct1 10.2210/pdb9ct1/pdb 
WWPDB D_1000285311 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-14 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CT1 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-24 
_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              alexis.campuzano@ibt.unam.mx 
_pdbx_contact_author.name_first         Alexis 
_pdbx_contact_author.name_last          Campuzano-Gonzalez 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0006-9399-122X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Campuzano-Gonzalez, A.' 1 0009-0006-9399-122X 
'Rudino-Pinera, E.'      2 0000-0001-8170-6379 
# 
_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            Biochem.Biophys.Res.Commun. 
_citation.journal_id_ASTM           BBRCA9 
_citation.journal_id_CSD            0146 
_citation.journal_id_ISSN           1090-2104 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            768 
_citation.language                  ? 
_citation.page_first                151818 
_citation.page_last                 151818 
_citation.title                     
'Structural determination of a new non-canonical inhibition complex between porcine trypsin and M271 a potato Kunitz-STI inhibitor.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bbrc.2025.151818 
_citation.pdbx_database_id_PubMed   40345005 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Campuzano-Gonzalez, A.' 1 ? 
primary 'Gil-Rodriguez, P.'      2 ? 
primary 'Quintana-Armas, A.X.'   3 ? 
primary 'Guerra, Y.'             4 ? 
primary 'Perez, Y.'              5 ? 
primary 'Rudino-Pinera, E.'      6 ? 
# 
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     nat Trypsin         24428.424 2   3.4.21.4 ? ? ? 
2 polymer     man 'KTI-A protein' 21727.828 2   ?        ? ? ? 
3 non-polymer syn 'CALCIUM ION'   40.078    2   ?        ? ? ? 
4 water       nat water           18.015    198 ?        ? ? ? 
# 
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 
;FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIIT
HPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSY
PGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN
;
;FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIIT
HPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSY
PGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN
;
A,C ? 
2 'polypeptide(L)' no no 
;ESPLPKPVLDTNGKKLNPNSSYRIISTFWGALGGDVYLGKSPNSDAPCPDGVFRYNSDVGPSGTPVRFIPLSGANIFEDQ
LLNIQFNIPTVKLCVSYTIWKVGNINAHLRTMLLETGGTIGQADSSYFKIVKSSKFGYNLLYCPLTRHFLCPFCRDDNFC
AKVGVVIQNGKRRLALVNENPLDVLFQEVHHHHHH
;
;ESPLPKPVLDTNGKKLNPNSSYRIISTFWGALGGDVYLGKSPNSDAPCPDGVFRYNSDVGPSGTPVRFIPLSGANIFEDQ
LLNIQFNIPTVKLCVSYTIWKVGNINAHLRTMLLETGGTIGQADSSYFKIVKSSKFGYNLLYCPLTRHFLCPFCRDDNFC
AKVGVVIQNGKRRLALVNENPLDVLFQEVHHHHHH
;
B,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CALCIUM ION' CA  
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PHE n 
1 2   PRO n 
1 3   THR n 
1 4   ASP n 
1 5   ASP n 
1 6   ASP n 
1 7   ASP n 
1 8   LYS n 
1 9   ILE n 
1 10  VAL n 
1 11  GLY n 
1 12  GLY n 
1 13  TYR n 
1 14  THR n 
1 15  CYS n 
1 16  ALA n 
1 17  ALA n 
1 18  ASN n 
1 19  SER n 
1 20  ILE n 
1 21  PRO n 
1 22  TYR n 
1 23  GLN n 
1 24  VAL n 
1 25  SER n 
1 26  LEU n 
1 27  ASN n 
1 28  SER n 
1 29  GLY n 
1 30  SER n 
1 31  HIS n 
1 32  PHE n 
1 33  CYS n 
1 34  GLY n 
1 35  GLY n 
1 36  SER n 
1 37  LEU n 
1 38  ILE n 
1 39  ASN n 
1 40  SER n 
1 41  GLN n 
1 42  TRP n 
1 43  VAL n 
1 44  VAL n 
1 45  SER n 
1 46  ALA n 
1 47  ALA n 
1 48  HIS n 
1 49  CYS n 
1 50  TYR n 
1 51  LYS n 
1 52  SER n 
1 53  ARG n 
1 54  ILE n 
1 55  GLN n 
1 56  VAL n 
1 57  ARG n 
1 58  LEU n 
1 59  GLY n 
1 60  GLU n 
1 61  HIS n 
1 62  ASN n 
1 63  ILE n 
1 64  ASP n 
1 65  VAL n 
1 66  LEU n 
1 67  GLU n 
1 68  GLY n 
1 69  ASN n 
1 70  GLU n 
1 71  GLN n 
1 72  PHE n 
1 73  ILE n 
1 74  ASN n 
1 75  ALA n 
1 76  ALA n 
1 77  LYS n 
1 78  ILE n 
1 79  ILE n 
1 80  THR n 
1 81  HIS n 
1 82  PRO n 
1 83  ASN n 
1 84  PHE n 
1 85  ASN n 
1 86  GLY n 
1 87  ASN n 
1 88  THR n 
1 89  LEU n 
1 90  ASP n 
1 91  ASN n 
1 92  ASP n 
1 93  ILE n 
1 94  MET n 
1 95  LEU n 
1 96  ILE n 
1 97  LYS n 
1 98  LEU n 
1 99  SER n 
1 100 SER n 
1 101 PRO n 
1 102 ALA n 
1 103 THR n 
1 104 LEU n 
1 105 ASN n 
1 106 SER n 
1 107 ARG n 
1 108 VAL n 
1 109 ALA n 
1 110 THR n 
1 111 VAL n 
1 112 SER n 
1 113 LEU n 
1 114 PRO n 
1 115 ARG n 
1 116 SER n 
1 117 CYS n 
1 118 ALA n 
1 119 ALA n 
1 120 ALA n 
1 121 GLY n 
1 122 THR n 
1 123 GLU n 
1 124 CYS n 
1 125 LEU n 
1 126 ILE n 
1 127 SER n 
1 128 GLY n 
1 129 TRP n 
1 130 GLY n 
1 131 ASN n 
1 132 THR n 
1 133 LYS n 
1 134 SER n 
1 135 SER n 
1 136 GLY n 
1 137 SER n 
1 138 SER n 
1 139 TYR n 
1 140 PRO n 
1 141 SER n 
1 142 LEU n 
1 143 LEU n 
1 144 GLN n 
1 145 CYS n 
1 146 LEU n 
1 147 LYS n 
1 148 ALA n 
1 149 PRO n 
1 150 VAL n 
1 151 LEU n 
1 152 SER n 
1 153 ASP n 
1 154 SER n 
1 155 SER n 
1 156 CYS n 
1 157 LYS n 
1 158 SER n 
1 159 SER n 
1 160 TYR n 
1 161 PRO n 
1 162 GLY n 
1 163 GLN n 
1 164 ILE n 
1 165 THR n 
1 166 GLY n 
1 167 ASN n 
1 168 MET n 
1 169 ILE n 
1 170 CYS n 
1 171 VAL n 
1 172 GLY n 
1 173 PHE n 
1 174 LEU n 
1 175 GLU n 
1 176 GLY n 
1 177 GLY n 
1 178 LYS n 
1 179 ASP n 
1 180 SER n 
1 181 CYS n 
1 182 GLN n 
1 183 GLY n 
1 184 ASP n 
1 185 SER n 
1 186 GLY n 
1 187 GLY n 
1 188 PRO n 
1 189 VAL n 
1 190 VAL n 
1 191 CYS n 
1 192 ASN n 
1 193 GLY n 
1 194 GLN n 
1 195 LEU n 
1 196 GLN n 
1 197 GLY n 
1 198 ILE n 
1 199 VAL n 
1 200 SER n 
1 201 TRP n 
1 202 GLY n 
1 203 TYR n 
1 204 GLY n 
1 205 CYS n 
1 206 ALA n 
1 207 GLN n 
1 208 LYS n 
1 209 ASN n 
1 210 LYS n 
1 211 PRO n 
1 212 GLY n 
1 213 VAL n 
1 214 TYR n 
1 215 THR n 
1 216 LYS n 
1 217 VAL n 
1 218 CYS n 
1 219 ASN n 
1 220 TYR n 
1 221 VAL n 
1 222 ASN n 
1 223 TRP n 
1 224 ILE n 
1 225 GLN n 
1 226 GLN n 
1 227 THR n 
1 228 ILE n 
1 229 ALA n 
1 230 ALA n 
1 231 ASN n 
2 1   GLU n 
2 2   SER n 
2 3   PRO n 
2 4   LEU n 
2 5   PRO n 
2 6   LYS n 
2 7   PRO n 
2 8   VAL n 
2 9   LEU n 
2 10  ASP n 
2 11  THR n 
2 12  ASN n 
2 13  GLY n 
2 14  LYS n 
2 15  LYS n 
2 16  LEU n 
2 17  ASN n 
2 18  PRO n 
2 19  ASN n 
2 20  SER n 
2 21  SER n 
2 22  TYR n 
2 23  ARG n 
2 24  ILE n 
2 25  ILE n 
2 26  SER n 
2 27  THR n 
2 28  PHE n 
2 29  TRP n 
2 30  GLY n 
2 31  ALA n 
2 32  LEU n 
2 33  GLY n 
2 34  GLY n 
2 35  ASP n 
2 36  VAL n 
2 37  TYR n 
2 38  LEU n 
2 39  GLY n 
2 40  LYS n 
2 41  SER n 
2 42  PRO n 
2 43  ASN n 
2 44  SER n 
2 45  ASP n 
2 46  ALA n 
2 47  PRO n 
2 48  CYS n 
2 49  PRO n 
2 50  ASP n 
2 51  GLY n 
2 52  VAL n 
2 53  PHE n 
2 54  ARG n 
2 55  TYR n 
2 56  ASN n 
2 57  SER n 
2 58  ASP n 
2 59  VAL n 
2 60  GLY n 
2 61  PRO n 
2 62  SER n 
2 63  GLY n 
2 64  THR n 
2 65  PRO n 
2 66  VAL n 
2 67  ARG n 
2 68  PHE n 
2 69  ILE n 
2 70  PRO n 
2 71  LEU n 
2 72  SER n 
2 73  GLY n 
2 74  ALA n 
2 75  ASN n 
2 76  ILE n 
2 77  PHE n 
2 78  GLU n 
2 79  ASP n 
2 80  GLN n 
2 81  LEU n 
2 82  LEU n 
2 83  ASN n 
2 84  ILE n 
2 85  GLN n 
2 86  PHE n 
2 87  ASN n 
2 88  ILE n 
2 89  PRO n 
2 90  THR n 
2 91  VAL n 
2 92  LYS n 
2 93  LEU n 
2 94  CYS n 
2 95  VAL n 
2 96  SER n 
2 97  TYR n 
2 98  THR n 
2 99  ILE n 
2 100 TRP n 
2 101 LYS n 
2 102 VAL n 
2 103 GLY n 
2 104 ASN n 
2 105 ILE n 
2 106 ASN n 
2 107 ALA n 
2 108 HIS n 
2 109 LEU n 
2 110 ARG n 
2 111 THR n 
2 112 MET n 
2 113 LEU n 
2 114 LEU n 
2 115 GLU n 
2 116 THR n 
2 117 GLY n 
2 118 GLY n 
2 119 THR n 
2 120 ILE n 
2 121 GLY n 
2 122 GLN n 
2 123 ALA n 
2 124 ASP n 
2 125 SER n 
2 126 SER n 
2 127 TYR n 
2 128 PHE n 
2 129 LYS n 
2 130 ILE n 
2 131 VAL n 
2 132 LYS n 
2 133 SER n 
2 134 SER n 
2 135 LYS n 
2 136 PHE n 
2 137 GLY n 
2 138 TYR n 
2 139 ASN n 
2 140 LEU n 
2 141 LEU n 
2 142 TYR n 
2 143 CYS n 
2 144 PRO n 
2 145 LEU n 
2 146 THR n 
2 147 ARG n 
2 148 HIS n 
2 149 PHE n 
2 150 LEU n 
2 151 CYS n 
2 152 PRO n 
2 153 PHE n 
2 154 CYS n 
2 155 ARG n 
2 156 ASP n 
2 157 ASP n 
2 158 ASN n 
2 159 PHE n 
2 160 CYS n 
2 161 ALA n 
2 162 LYS n 
2 163 VAL n 
2 164 GLY n 
2 165 VAL n 
2 166 VAL n 
2 167 ILE n 
2 168 GLN n 
2 169 ASN n 
2 170 GLY n 
2 171 LYS n 
2 172 ARG n 
2 173 ARG n 
2 174 LEU n 
2 175 ALA n 
2 176 LEU n 
2 177 VAL n 
2 178 ASN n 
2 179 GLU n 
2 180 ASN n 
2 181 PRO n 
2 182 LEU n 
2 183 ASP n 
2 184 VAL n 
2 185 LEU n 
2 186 PHE n 
2 187 GLN n 
2 188 GLU n 
2 189 VAL n 
2 190 HIS n 
2 191 HIS n 
2 192 HIS n 
2 193 HIS n 
2 194 HIS n 
2 195 HIS n 
# 
_entity_src_gen.entity_id                          2 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   195 
_entity_src_gen.gene_src_common_name               potato 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 KTI-A 
_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                   
'obtained from genomic DNA sequencing from Solanum tuberosum (potato) samples isolated with the plant CTAB method' 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Solanum tuberosum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4113 
_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      'Komagataella pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_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               X33 
_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                       pPICZaC 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           231 
_entity_src_nat.common_name                pig 
_entity_src_nat.pdbx_organism_scientific   'Sus scrofa' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9823 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   PHE 1   -7  ?   ?   ?   A . n 
A 1 2   PRO 2   -6  ?   ?   ?   A . n 
A 1 3   THR 3   -5  ?   ?   ?   A . n 
A 1 4   ASP 4   -4  ?   ?   ?   A . n 
A 1 5   ASP 5   -3  ?   ?   ?   A . n 
A 1 6   ASP 6   -2  ?   ?   ?   A . n 
A 1 7   ASP 7   -1  ?   ?   ?   A . n 
A 1 8   LYS 8   0   ?   ?   ?   A . n 
A 1 9   ILE 9   1   1   ILE ILE A . n 
A 1 10  VAL 10  2   2   VAL VAL A . n 
A 1 11  GLY 11  3   3   GLY GLY A . n 
A 1 12  GLY 12  4   4   GLY GLY A . n 
A 1 13  TYR 13  5   5   TYR TYR A . n 
A 1 14  THR 14  6   6   THR THR A . n 
A 1 15  CYS 15  7   7   CYS CYS A . n 
A 1 16  ALA 16  8   8   ALA ALA A . n 
A 1 17  ALA 17  9   9   ALA ALA A . n 
A 1 18  ASN 18  10  10  ASN ASN A . n 
A 1 19  SER 19  11  11  SER SER A . n 
A 1 20  ILE 20  12  12  ILE ILE A . n 
A 1 21  PRO 21  13  13  PRO PRO A . n 
A 1 22  TYR 22  14  14  TYR TYR A . n 
A 1 23  GLN 23  15  15  GLN GLN A . n 
A 1 24  VAL 24  16  16  VAL VAL A . n 
A 1 25  SER 25  17  17  SER SER A . n 
A 1 26  LEU 26  18  18  LEU LEU A . n 
A 1 27  ASN 27  19  19  ASN ASN A . n 
A 1 28  SER 28  20  20  SER SER A . n 
A 1 29  GLY 29  21  21  GLY GLY A . n 
A 1 30  SER 30  22  22  SER SER A . n 
A 1 31  HIS 31  23  23  HIS HIS A . n 
A 1 32  PHE 32  24  24  PHE PHE A . n 
A 1 33  CYS 33  25  25  CYS CYS A . n 
A 1 34  GLY 34  26  26  GLY GLY A . n 
A 1 35  GLY 35  27  27  GLY GLY A . n 
A 1 36  SER 36  28  28  SER SER A . n 
A 1 37  LEU 37  29  29  LEU LEU A . n 
A 1 38  ILE 38  30  30  ILE ILE A . n 
A 1 39  ASN 39  31  31  ASN ASN A . n 
A 1 40  SER 40  32  32  SER SER A . n 
A 1 41  GLN 41  33  33  GLN GLN A . n 
A 1 42  TRP 42  34  34  TRP TRP A . n 
A 1 43  VAL 43  35  35  VAL VAL A . n 
A 1 44  VAL 44  36  36  VAL VAL A . n 
A 1 45  SER 45  37  37  SER SER A . n 
A 1 46  ALA 46  38  38  ALA ALA A . n 
A 1 47  ALA 47  39  39  ALA ALA A . n 
A 1 48  HIS 48  40  40  HIS HIS A . n 
A 1 49  CYS 49  41  41  CYS CYS A . n 
A 1 50  TYR 50  42  42  TYR TYR A . n 
A 1 51  LYS 51  43  43  LYS LYS A . n 
A 1 52  SER 52  44  44  SER SER A . n 
A 1 53  ARG 53  45  45  ARG ARG A . n 
A 1 54  ILE 54  46  46  ILE ILE A . n 
A 1 55  GLN 55  47  47  GLN GLN A . n 
A 1 56  VAL 56  48  48  VAL VAL A . n 
A 1 57  ARG 57  49  49  ARG ARG A . n 
A 1 58  LEU 58  50  50  LEU LEU A . n 
A 1 59  GLY 59  51  51  GLY GLY A . n 
A 1 60  GLU 60  52  52  GLU GLU A . n 
A 1 61  HIS 61  53  53  HIS HIS A . n 
A 1 62  ASN 62  54  54  ASN ASN A . n 
A 1 63  ILE 63  55  55  ILE ILE A . n 
A 1 64  ASP 64  56  56  ASP ASP A . n 
A 1 65  VAL 65  57  57  VAL VAL A . n 
A 1 66  LEU 66  58  58  LEU LEU A . n 
A 1 67  GLU 67  59  59  GLU GLU A . n 
A 1 68  GLY 68  60  60  GLY GLY A . n 
A 1 69  ASN 69  61  61  ASN ASN A . n 
A 1 70  GLU 70  62  62  GLU GLU A . n 
A 1 71  GLN 71  63  63  GLN GLN A . n 
A 1 72  PHE 72  64  64  PHE PHE A . n 
A 1 73  ILE 73  65  65  ILE ILE A . n 
A 1 74  ASN 74  66  66  ASN ASN A . n 
A 1 75  ALA 75  67  67  ALA ALA A . n 
A 1 76  ALA 76  68  68  ALA ALA A . n 
A 1 77  LYS 77  69  69  LYS LYS A . n 
A 1 78  ILE 78  70  70  ILE ILE A . n 
A 1 79  ILE 79  71  71  ILE ILE A . n 
A 1 80  THR 80  72  72  THR THR A . n 
A 1 81  HIS 81  73  73  HIS HIS A . n 
A 1 82  PRO 82  74  74  PRO PRO A . n 
A 1 83  ASN 83  75  75  ASN ASN A . n 
A 1 84  PHE 84  76  76  PHE PHE A . n 
A 1 85  ASN 85  77  77  ASN ASN A . n 
A 1 86  GLY 86  78  78  GLY GLY A . n 
A 1 87  ASN 87  79  79  ASN ASN A . n 
A 1 88  THR 88  80  80  THR THR A . n 
A 1 89  LEU 89  81  81  LEU LEU A . n 
A 1 90  ASP 90  82  82  ASP ASP A . n 
A 1 91  ASN 91  83  83  ASN ASN A . n 
A 1 92  ASP 92  84  84  ASP ASP A . n 
A 1 93  ILE 93  85  85  ILE ILE A . n 
A 1 94  MET 94  86  86  MET MET A . n 
A 1 95  LEU 95  87  87  LEU LEU A . n 
A 1 96  ILE 96  88  88  ILE ILE A . n 
A 1 97  LYS 97  89  89  LYS LYS A . n 
A 1 98  LEU 98  90  90  LEU LEU A . n 
A 1 99  SER 99  91  91  SER SER A . n 
A 1 100 SER 100 92  92  SER SER A . n 
A 1 101 PRO 101 93  93  PRO PRO A . n 
A 1 102 ALA 102 94  94  ALA ALA A . n 
A 1 103 THR 103 95  95  THR THR A . n 
A 1 104 LEU 104 96  96  LEU LEU A . n 
A 1 105 ASN 105 97  97  ASN ASN A . n 
A 1 106 SER 106 98  98  SER SER A . n 
A 1 107 ARG 107 99  99  ARG ARG A . n 
A 1 108 VAL 108 100 100 VAL VAL A . n 
A 1 109 ALA 109 101 101 ALA ALA A . n 
A 1 110 THR 110 102 102 THR THR A . n 
A 1 111 VAL 111 103 103 VAL VAL A . n 
A 1 112 SER 112 104 104 SER SER A . n 
A 1 113 LEU 113 105 105 LEU LEU A . n 
A 1 114 PRO 114 106 106 PRO PRO A . n 
A 1 115 ARG 115 107 107 ARG ARG A . n 
A 1 116 SER 116 108 108 SER SER A . n 
A 1 117 CYS 117 109 109 CYS CYS A . n 
A 1 118 ALA 118 110 110 ALA ALA A . n 
A 1 119 ALA 119 111 111 ALA ALA A . n 
A 1 120 ALA 120 112 112 ALA ALA A . n 
A 1 121 GLY 121 113 113 GLY GLY A . n 
A 1 122 THR 122 114 114 THR THR A . n 
A 1 123 GLU 123 115 115 GLU GLU A . n 
A 1 124 CYS 124 116 116 CYS CYS A . n 
A 1 125 LEU 125 117 117 LEU LEU A . n 
A 1 126 ILE 126 118 118 ILE ILE A . n 
A 1 127 SER 127 119 119 SER SER A . n 
A 1 128 GLY 128 120 120 GLY GLY A . n 
A 1 129 TRP 129 121 121 TRP TRP A . n 
A 1 130 GLY 130 122 122 GLY GLY A . n 
A 1 131 ASN 131 123 123 ASN ASN A . n 
A 1 132 THR 132 124 124 THR THR A . n 
A 1 133 LYS 133 125 125 LYS LYS A . n 
A 1 134 SER 134 126 126 SER SER A . n 
A 1 135 SER 135 127 127 SER SER A . n 
A 1 136 GLY 136 128 128 GLY GLY A . n 
A 1 137 SER 137 129 129 SER SER A . n 
A 1 138 SER 138 130 130 SER SER A . n 
A 1 139 TYR 139 131 131 TYR TYR A . n 
A 1 140 PRO 140 132 132 PRO PRO A . n 
A 1 141 SER 141 133 133 SER SER A . n 
A 1 142 LEU 142 134 134 LEU LEU A . n 
A 1 143 LEU 143 135 135 LEU LEU A . n 
A 1 144 GLN 144 136 136 GLN GLN A . n 
A 1 145 CYS 145 137 137 CYS CYS A . n 
A 1 146 LEU 146 138 138 LEU LEU A . n 
A 1 147 LYS 147 139 139 LYS LYS A . n 
A 1 148 ALA 148 140 140 ALA ALA A . n 
A 1 149 PRO 149 141 141 PRO PRO A . n 
A 1 150 VAL 150 142 142 VAL VAL A . n 
A 1 151 LEU 151 143 143 LEU LEU A . n 
A 1 152 SER 152 144 144 SER SER A . n 
A 1 153 ASP 153 145 145 ASP ASP A . n 
A 1 154 SER 154 146 146 SER SER A . n 
A 1 155 SER 155 147 147 SER SER A . n 
A 1 156 CYS 156 148 148 CYS CYS A . n 
A 1 157 LYS 157 149 149 LYS LYS A . n 
A 1 158 SER 158 150 150 SER SER A . n 
A 1 159 SER 159 151 151 SER SER A . n 
A 1 160 TYR 160 152 152 TYR TYR A . n 
A 1 161 PRO 161 153 153 PRO PRO A . n 
A 1 162 GLY 162 154 154 GLY GLY A . n 
A 1 163 GLN 163 155 155 GLN GLN A . n 
A 1 164 ILE 164 156 156 ILE ILE A . n 
A 1 165 THR 165 157 157 THR THR A . n 
A 1 166 GLY 166 158 158 GLY GLY A . n 
A 1 167 ASN 167 159 159 ASN ASN A . n 
A 1 168 MET 168 160 160 MET MET A . n 
A 1 169 ILE 169 161 161 ILE ILE A . n 
A 1 170 CYS 170 162 162 CYS CYS A . n 
A 1 171 VAL 171 163 163 VAL VAL A . n 
A 1 172 GLY 172 164 164 GLY GLY A . n 
A 1 173 PHE 173 165 165 PHE PHE A . n 
A 1 174 LEU 174 166 166 LEU LEU A . n 
A 1 175 GLU 175 167 167 GLU GLU A . n 
A 1 176 GLY 176 168 168 GLY GLY A . n 
A 1 177 GLY 177 169 169 GLY GLY A . n 
A 1 178 LYS 178 170 170 LYS LYS A . n 
A 1 179 ASP 179 171 171 ASP ASP A . n 
A 1 180 SER 180 172 172 SER SER A . n 
A 1 181 CYS 181 173 173 CYS CYS A . n 
A 1 182 GLN 182 174 174 GLN GLN A . n 
A 1 183 GLY 183 175 175 GLY GLY A . n 
A 1 184 ASP 184 176 176 ASP ASP A . n 
A 1 185 SER 185 177 177 SER SER A . n 
A 1 186 GLY 186 178 178 GLY GLY A . n 
A 1 187 GLY 187 179 179 GLY GLY A . n 
A 1 188 PRO 188 180 180 PRO PRO A . n 
A 1 189 VAL 189 181 181 VAL VAL A . n 
A 1 190 VAL 190 182 182 VAL VAL A . n 
A 1 191 CYS 191 183 183 CYS CYS A . n 
A 1 192 ASN 192 184 184 ASN ASN A . n 
A 1 193 GLY 193 185 185 GLY GLY A . n 
A 1 194 GLN 194 186 186 GLN GLN A . n 
A 1 195 LEU 195 187 187 LEU LEU A . n 
A 1 196 GLN 196 188 188 GLN GLN A . n 
A 1 197 GLY 197 189 189 GLY GLY A . n 
A 1 198 ILE 198 190 190 ILE ILE A . n 
A 1 199 VAL 199 191 191 VAL VAL A . n 
A 1 200 SER 200 192 192 SER SER A . n 
A 1 201 TRP 201 193 193 TRP TRP A . n 
A 1 202 GLY 202 194 194 GLY GLY A . n 
A 1 203 TYR 203 195 195 TYR TYR A . n 
A 1 204 GLY 204 196 196 GLY GLY A . n 
A 1 205 CYS 205 197 197 CYS CYS A . n 
A 1 206 ALA 206 198 198 ALA ALA A . n 
A 1 207 GLN 207 199 199 GLN GLN A . n 
A 1 208 LYS 208 200 200 LYS LYS A . n 
A 1 209 ASN 209 201 201 ASN ASN A . n 
A 1 210 LYS 210 202 202 LYS LYS A . n 
A 1 211 PRO 211 203 203 PRO PRO A . n 
A 1 212 GLY 212 204 204 GLY GLY A . n 
A 1 213 VAL 213 205 205 VAL VAL A . n 
A 1 214 TYR 214 206 206 TYR TYR A . n 
A 1 215 THR 215 207 207 THR THR A . n 
A 1 216 LYS 216 208 208 LYS LYS A . n 
A 1 217 VAL 217 209 209 VAL VAL A . n 
A 1 218 CYS 218 210 210 CYS CYS A . n 
A 1 219 ASN 219 211 211 ASN ASN A . n 
A 1 220 TYR 220 212 212 TYR TYR A . n 
A 1 221 VAL 221 213 213 VAL VAL A . n 
A 1 222 ASN 222 214 214 ASN ASN A . n 
A 1 223 TRP 223 215 215 TRP TRP A . n 
A 1 224 ILE 224 216 216 ILE ILE A . n 
A 1 225 GLN 225 217 217 GLN GLN A . n 
A 1 226 GLN 226 218 218 GLN GLN A . n 
A 1 227 THR 227 219 219 THR THR A . n 
A 1 228 ILE 228 220 220 ILE ILE A . n 
A 1 229 ALA 229 221 221 ALA ALA A . n 
A 1 230 ALA 230 222 222 ALA ALA A . n 
A 1 231 ASN 231 223 223 ASN ASN A . n 
B 2 1   GLU 1   1   ?   ?   ?   B . n 
B 2 2   SER 2   2   ?   ?   ?   B . n 
B 2 3   PRO 3   3   ?   ?   ?   B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   PRO 5   5   5   PRO PRO B . n 
B 2 6   LYS 6   6   6   LYS LYS B . n 
B 2 7   PRO 7   7   7   PRO PRO B . n 
B 2 8   VAL 8   8   8   VAL VAL B . n 
B 2 9   LEU 9   9   9   LEU LEU B . n 
B 2 10  ASP 10  10  10  ASP ASP B . n 
B 2 11  THR 11  11  11  THR THR B . n 
B 2 12  ASN 12  12  12  ASN ASN B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  LYS 14  14  14  LYS LYS B . n 
B 2 15  LYS 15  15  15  LYS LYS B . n 
B 2 16  LEU 16  16  16  LEU LEU B . n 
B 2 17  ASN 17  17  17  ASN ASN B . n 
B 2 18  PRO 18  18  18  PRO PRO B . n 
B 2 19  ASN 19  19  19  ASN ASN B . n 
B 2 20  SER 20  20  20  SER SER B . n 
B 2 21  SER 21  21  21  SER SER B . n 
B 2 22  TYR 22  22  22  TYR TYR B . n 
B 2 23  ARG 23  23  23  ARG ARG B . n 
B 2 24  ILE 24  24  24  ILE ILE B . n 
B 2 25  ILE 25  25  25  ILE ILE B . n 
B 2 26  SER 26  26  26  SER SER B . n 
B 2 27  THR 27  27  27  THR THR B . n 
B 2 28  PHE 28  28  28  PHE PHE B . n 
B 2 29  TRP 29  29  29  TRP TRP B . n 
B 2 30  GLY 30  30  30  GLY GLY B . n 
B 2 31  ALA 31  31  31  ALA ALA B . n 
B 2 32  LEU 32  32  32  LEU LEU B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  GLY 34  34  34  GLY GLY B . n 
B 2 35  ASP 35  35  35  ASP ASP B . n 
B 2 36  VAL 36  36  36  VAL VAL B . n 
B 2 37  TYR 37  37  37  TYR TYR B . n 
B 2 38  LEU 38  38  38  LEU LEU B . n 
B 2 39  GLY 39  39  39  GLY GLY B . n 
B 2 40  LYS 40  40  40  LYS LYS B . n 
B 2 41  SER 41  41  41  SER SER B . n 
B 2 42  PRO 42  42  42  PRO PRO B . n 
B 2 43  ASN 43  43  43  ASN ASN B . n 
B 2 44  SER 44  44  44  SER SER B . n 
B 2 45  ASP 45  45  45  ASP ASP B . n 
B 2 46  ALA 46  46  46  ALA ALA B . n 
B 2 47  PRO 47  47  47  PRO PRO B . n 
B 2 48  CYS 48  48  48  CYS CYS B . n 
B 2 49  PRO 49  49  49  PRO PRO B . n 
B 2 50  ASP 50  50  50  ASP ASP B . n 
B 2 51  GLY 51  51  51  GLY GLY B . n 
B 2 52  VAL 52  52  52  VAL VAL B . n 
B 2 53  PHE 53  53  53  PHE PHE B . n 
B 2 54  ARG 54  54  54  ARG ARG B . n 
B 2 55  TYR 55  55  55  TYR TYR B . n 
B 2 56  ASN 56  56  56  ASN ASN B . n 
B 2 57  SER 57  57  57  SER SER B . n 
B 2 58  ASP 58  58  58  ASP ASP B . n 
B 2 59  VAL 59  59  59  VAL VAL B . n 
B 2 60  GLY 60  60  60  GLY GLY B . n 
B 2 61  PRO 61  61  61  PRO PRO B . n 
B 2 62  SER 62  62  62  SER SER B . n 
B 2 63  GLY 63  63  63  GLY GLY B . n 
B 2 64  THR 64  64  64  THR THR B . n 
B 2 65  PRO 65  65  65  PRO PRO B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  ARG 67  67  67  ARG ARG B . n 
B 2 68  PHE 68  68  68  PHE PHE B . n 
B 2 69  ILE 69  69  69  ILE ILE B . n 
B 2 70  PRO 70  70  70  PRO PRO B . n 
B 2 71  LEU 71  71  71  LEU LEU B . n 
B 2 72  SER 72  72  72  SER SER B . n 
B 2 73  GLY 73  73  73  GLY GLY B . n 
B 2 74  ALA 74  74  74  ALA ALA B . n 
B 2 75  ASN 75  75  75  ASN ASN B . n 
B 2 76  ILE 76  76  76  ILE ILE B . n 
B 2 77  PHE 77  77  77  PHE PHE B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  ASP 79  79  79  ASP ASP B . n 
B 2 80  GLN 80  80  80  GLN GLN B . n 
B 2 81  LEU 81  81  81  LEU LEU B . n 
B 2 82  LEU 82  82  82  LEU LEU B . n 
B 2 83  ASN 83  83  83  ASN ASN B . n 
B 2 84  ILE 84  84  84  ILE ILE B . n 
B 2 85  GLN 85  85  85  GLN GLN B . n 
B 2 86  PHE 86  86  86  PHE PHE B . n 
B 2 87  ASN 87  87  87  ASN ASN B . n 
B 2 88  ILE 88  88  88  ILE ILE B . n 
B 2 89  PRO 89  89  89  PRO PRO B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  LYS 92  92  92  LYS LYS B . n 
B 2 93  LEU 93  93  93  LEU LEU B . n 
B 2 94  CYS 94  94  94  CYS CYS B . n 
B 2 95  VAL 95  95  95  VAL VAL B . n 
B 2 96  SER 96  96  96  SER SER B . n 
B 2 97  TYR 97  97  97  TYR TYR B . n 
B 2 98  THR 98  98  98  THR THR B . n 
B 2 99  ILE 99  99  99  ILE ILE B . n 
B 2 100 TRP 100 100 100 TRP TRP B . n 
B 2 101 LYS 101 101 101 LYS LYS B . n 
B 2 102 VAL 102 102 102 VAL VAL B . n 
B 2 103 GLY 103 103 103 GLY GLY B . n 
B 2 104 ASN 104 104 ?   ?   ?   B . n 
B 2 105 ILE 105 105 ?   ?   ?   B . n 
B 2 106 ASN 106 106 ?   ?   ?   B . n 
B 2 107 ALA 107 107 ?   ?   ?   B . n 
B 2 108 HIS 108 108 ?   ?   ?   B . n 
B 2 109 LEU 109 109 ?   ?   ?   B . n 
B 2 110 ARG 110 110 110 ARG ARG B . n 
B 2 111 THR 111 111 111 THR THR B . n 
B 2 112 MET 112 112 112 MET MET B . n 
B 2 113 LEU 113 113 113 LEU LEU B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 GLU 115 115 115 GLU GLU B . n 
B 2 116 THR 116 116 116 THR THR B . n 
B 2 117 GLY 117 117 117 GLY GLY B . n 
B 2 118 GLY 118 118 118 GLY GLY B . n 
B 2 119 THR 119 119 119 THR THR B . n 
B 2 120 ILE 120 120 120 ILE ILE B . n 
B 2 121 GLY 121 121 121 GLY GLY B . n 
B 2 122 GLN 122 122 122 GLN GLN B . n 
B 2 123 ALA 123 123 123 ALA ALA B . n 
B 2 124 ASP 124 124 124 ASP ASP B . n 
B 2 125 SER 125 125 125 SER SER B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 TYR 127 127 127 TYR TYR B . n 
B 2 128 PHE 128 128 128 PHE PHE B . n 
B 2 129 LYS 129 129 129 LYS LYS B . n 
B 2 130 ILE 130 130 130 ILE ILE B . n 
B 2 131 VAL 131 131 131 VAL VAL B . n 
B 2 132 LYS 132 132 132 LYS LYS B . n 
B 2 133 SER 133 133 133 SER SER B . n 
B 2 134 SER 134 134 134 SER SER B . n 
B 2 135 LYS 135 135 135 LYS LYS B . n 
B 2 136 PHE 136 136 136 PHE PHE B . n 
B 2 137 GLY 137 137 137 GLY GLY B . n 
B 2 138 TYR 138 138 138 TYR TYR B . n 
B 2 139 ASN 139 139 139 ASN ASN B . n 
B 2 140 LEU 140 140 140 LEU LEU B . n 
B 2 141 LEU 141 141 141 LEU LEU B . n 
B 2 142 TYR 142 142 142 TYR TYR B . n 
B 2 143 CYS 143 143 143 CYS CYS B . n 
B 2 144 PRO 144 144 144 PRO PRO B . n 
B 2 145 LEU 145 145 145 LEU LEU B . n 
B 2 146 THR 146 146 ?   ?   ?   B . n 
B 2 147 ARG 147 147 ?   ?   ?   B . n 
B 2 148 HIS 148 148 ?   ?   ?   B . n 
B 2 149 PHE 149 149 ?   ?   ?   B . n 
B 2 150 LEU 150 150 ?   ?   ?   B . n 
B 2 151 CYS 151 151 ?   ?   ?   B . n 
B 2 152 PRO 152 152 ?   ?   ?   B . n 
B 2 153 PHE 153 153 ?   ?   ?   B . n 
B 2 154 CYS 154 154 ?   ?   ?   B . n 
B 2 155 ARG 155 155 ?   ?   ?   B . n 
B 2 156 ASP 156 156 ?   ?   ?   B . n 
B 2 157 ASP 157 157 ?   ?   ?   B . n 
B 2 158 ASN 158 158 158 ASN ASN B . n 
B 2 159 PHE 159 159 159 PHE PHE B . n 
B 2 160 CYS 160 160 160 CYS CYS B . n 
B 2 161 ALA 161 161 161 ALA ALA B . n 
B 2 162 LYS 162 162 162 LYS LYS B . n 
B 2 163 VAL 163 163 163 VAL VAL B . n 
B 2 164 GLY 164 164 164 GLY GLY B . n 
B 2 165 VAL 165 165 165 VAL VAL B . n 
B 2 166 VAL 166 166 166 VAL VAL B . n 
B 2 167 ILE 167 167 167 ILE ILE B . n 
B 2 168 GLN 168 168 168 GLN GLN B . n 
B 2 169 ASN 169 169 169 ASN ASN B . n 
B 2 170 GLY 170 170 170 GLY GLY B . n 
B 2 171 LYS 171 171 171 LYS LYS B . n 
B 2 172 ARG 172 172 172 ARG ARG B . n 
B 2 173 ARG 173 173 173 ARG ARG B . n 
B 2 174 LEU 174 174 174 LEU LEU B . n 
B 2 175 ALA 175 175 175 ALA ALA B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 VAL 177 177 177 VAL VAL B . n 
B 2 178 ASN 178 178 178 ASN ASN B . n 
B 2 179 GLU 179 179 179 GLU GLU B . n 
B 2 180 ASN 180 180 180 ASN ASN B . n 
B 2 181 PRO 181 181 181 PRO PRO B . n 
B 2 182 LEU 182 182 182 LEU LEU B . n 
B 2 183 ASP 183 183 183 ASP ASP B . n 
B 2 184 VAL 184 184 184 VAL VAL B . n 
B 2 185 LEU 185 185 185 LEU LEU B . n 
B 2 186 PHE 186 186 186 PHE PHE B . n 
B 2 187 GLN 187 187 187 GLN GLN B . n 
B 2 188 GLU 188 188 188 GLU GLU B . n 
B 2 189 VAL 189 189 189 VAL VAL B . n 
B 2 190 HIS 190 190 ?   ?   ?   B . n 
B 2 191 HIS 191 191 ?   ?   ?   B . n 
B 2 192 HIS 192 192 ?   ?   ?   B . n 
B 2 193 HIS 193 193 ?   ?   ?   B . n 
B 2 194 HIS 194 194 ?   ?   ?   B . n 
B 2 195 HIS 195 195 ?   ?   ?   B . n 
C 1 1   PHE 1   -7  ?   ?   ?   C . n 
C 1 2   PRO 2   -6  ?   ?   ?   C . n 
C 1 3   THR 3   -5  ?   ?   ?   C . n 
C 1 4   ASP 4   -4  ?   ?   ?   C . n 
C 1 5   ASP 5   -3  ?   ?   ?   C . n 
C 1 6   ASP 6   -2  ?   ?   ?   C . n 
C 1 7   ASP 7   -1  ?   ?   ?   C . n 
C 1 8   LYS 8   0   ?   ?   ?   C . n 
C 1 9   ILE 9   1   1   ILE ILE C . n 
C 1 10  VAL 10  2   2   VAL VAL C . n 
C 1 11  GLY 11  3   3   GLY GLY C . n 
C 1 12  GLY 12  4   4   GLY GLY C . n 
C 1 13  TYR 13  5   5   TYR TYR C . n 
C 1 14  THR 14  6   6   THR THR C . n 
C 1 15  CYS 15  7   7   CYS CYS C . n 
C 1 16  ALA 16  8   8   ALA ALA C . n 
C 1 17  ALA 17  9   9   ALA ALA C . n 
C 1 18  ASN 18  10  10  ASN ASN C . n 
C 1 19  SER 19  11  11  SER SER C . n 
C 1 20  ILE 20  12  12  ILE ILE C . n 
C 1 21  PRO 21  13  13  PRO PRO C . n 
C 1 22  TYR 22  14  14  TYR TYR C . n 
C 1 23  GLN 23  15  15  GLN GLN C . n 
C 1 24  VAL 24  16  16  VAL VAL C . n 
C 1 25  SER 25  17  17  SER SER C . n 
C 1 26  LEU 26  18  18  LEU LEU C . n 
C 1 27  ASN 27  19  19  ASN ASN C . n 
C 1 28  SER 28  20  20  SER SER C . n 
C 1 29  GLY 29  21  21  GLY GLY C . n 
C 1 30  SER 30  22  22  SER SER C . n 
C 1 31  HIS 31  23  23  HIS HIS C . n 
C 1 32  PHE 32  24  24  PHE PHE C . n 
C 1 33  CYS 33  25  25  CYS CYS C . n 
C 1 34  GLY 34  26  26  GLY GLY C . n 
C 1 35  GLY 35  27  27  GLY GLY C . n 
C 1 36  SER 36  28  28  SER SER C . n 
C 1 37  LEU 37  29  29  LEU LEU C . n 
C 1 38  ILE 38  30  30  ILE ILE C . n 
C 1 39  ASN 39  31  31  ASN ASN C . n 
C 1 40  SER 40  32  32  SER SER C . n 
C 1 41  GLN 41  33  33  GLN GLN C . n 
C 1 42  TRP 42  34  34  TRP TRP C . n 
C 1 43  VAL 43  35  35  VAL VAL C . n 
C 1 44  VAL 44  36  36  VAL VAL C . n 
C 1 45  SER 45  37  37  SER SER C . n 
C 1 46  ALA 46  38  38  ALA ALA C . n 
C 1 47  ALA 47  39  39  ALA ALA C . n 
C 1 48  HIS 48  40  40  HIS HIS C . n 
C 1 49  CYS 49  41  41  CYS CYS C . n 
C 1 50  TYR 50  42  42  TYR TYR C . n 
C 1 51  LYS 51  43  43  LYS LYS C . n 
C 1 52  SER 52  44  44  SER SER C . n 
C 1 53  ARG 53  45  45  ARG ARG C . n 
C 1 54  ILE 54  46  46  ILE ILE C . n 
C 1 55  GLN 55  47  47  GLN GLN C . n 
C 1 56  VAL 56  48  48  VAL VAL C . n 
C 1 57  ARG 57  49  49  ARG ARG C . n 
C 1 58  LEU 58  50  50  LEU LEU C . n 
C 1 59  GLY 59  51  51  GLY GLY C . n 
C 1 60  GLU 60  52  52  GLU GLU C . n 
C 1 61  HIS 61  53  53  HIS HIS C . n 
C 1 62  ASN 62  54  54  ASN ASN C . n 
C 1 63  ILE 63  55  55  ILE ILE C . n 
C 1 64  ASP 64  56  56  ASP ASP C . n 
C 1 65  VAL 65  57  57  VAL VAL C . n 
C 1 66  LEU 66  58  58  LEU LEU C . n 
C 1 67  GLU 67  59  59  GLU GLU C . n 
C 1 68  GLY 68  60  60  GLY GLY C . n 
C 1 69  ASN 69  61  61  ASN ASN C . n 
C 1 70  GLU 70  62  62  GLU GLU C . n 
C 1 71  GLN 71  63  63  GLN GLN C . n 
C 1 72  PHE 72  64  64  PHE PHE C . n 
C 1 73  ILE 73  65  65  ILE ILE C . n 
C 1 74  ASN 74  66  66  ASN ASN C . n 
C 1 75  ALA 75  67  67  ALA ALA C . n 
C 1 76  ALA 76  68  68  ALA ALA C . n 
C 1 77  LYS 77  69  69  LYS LYS C . n 
C 1 78  ILE 78  70  70  ILE ILE C . n 
C 1 79  ILE 79  71  71  ILE ILE C . n 
C 1 80  THR 80  72  72  THR THR C . n 
C 1 81  HIS 81  73  73  HIS HIS C . n 
C 1 82  PRO 82  74  74  PRO PRO C . n 
C 1 83  ASN 83  75  75  ASN ASN C . n 
C 1 84  PHE 84  76  76  PHE PHE C . n 
C 1 85  ASN 85  77  77  ASN ASN C . n 
C 1 86  GLY 86  78  78  GLY GLY C . n 
C 1 87  ASN 87  79  79  ASN ASN C . n 
C 1 88  THR 88  80  80  THR THR C . n 
C 1 89  LEU 89  81  81  LEU LEU C . n 
C 1 90  ASP 90  82  82  ASP ASP C . n 
C 1 91  ASN 91  83  83  ASN ASN C . n 
C 1 92  ASP 92  84  84  ASP ASP C . n 
C 1 93  ILE 93  85  85  ILE ILE C . n 
C 1 94  MET 94  86  86  MET MET C . n 
C 1 95  LEU 95  87  87  LEU LEU C . n 
C 1 96  ILE 96  88  88  ILE ILE C . n 
C 1 97  LYS 97  89  89  LYS LYS C . n 
C 1 98  LEU 98  90  90  LEU LEU C . n 
C 1 99  SER 99  91  91  SER SER C . n 
C 1 100 SER 100 92  92  SER SER C . n 
C 1 101 PRO 101 93  93  PRO PRO C . n 
C 1 102 ALA 102 94  94  ALA ALA C . n 
C 1 103 THR 103 95  95  THR THR C . n 
C 1 104 LEU 104 96  96  LEU LEU C . n 
C 1 105 ASN 105 97  97  ASN ASN C . n 
C 1 106 SER 106 98  98  SER SER C . n 
C 1 107 ARG 107 99  99  ARG ARG C . n 
C 1 108 VAL 108 100 100 VAL VAL C . n 
C 1 109 ALA 109 101 101 ALA ALA C . n 
C 1 110 THR 110 102 102 THR THR C . n 
C 1 111 VAL 111 103 103 VAL VAL C . n 
C 1 112 SER 112 104 104 SER SER C . n 
C 1 113 LEU 113 105 105 LEU LEU C . n 
C 1 114 PRO 114 106 106 PRO PRO C . n 
C 1 115 ARG 115 107 107 ARG ARG C . n 
C 1 116 SER 116 108 108 SER SER C . n 
C 1 117 CYS 117 109 109 CYS CYS C . n 
C 1 118 ALA 118 110 110 ALA ALA C . n 
C 1 119 ALA 119 111 111 ALA ALA C . n 
C 1 120 ALA 120 112 112 ALA ALA C . n 
C 1 121 GLY 121 113 113 GLY GLY C . n 
C 1 122 THR 122 114 114 THR THR C . n 
C 1 123 GLU 123 115 115 GLU GLU C . n 
C 1 124 CYS 124 116 116 CYS CYS C . n 
C 1 125 LEU 125 117 117 LEU LEU C . n 
C 1 126 ILE 126 118 118 ILE ILE C . n 
C 1 127 SER 127 119 119 SER SER C . n 
C 1 128 GLY 128 120 120 GLY GLY C . n 
C 1 129 TRP 129 121 121 TRP TRP C . n 
C 1 130 GLY 130 122 122 GLY GLY C . n 
C 1 131 ASN 131 123 123 ASN ASN C . n 
C 1 132 THR 132 124 124 THR THR C . n 
C 1 133 LYS 133 125 125 LYS LYS C . n 
C 1 134 SER 134 126 126 SER SER C . n 
C 1 135 SER 135 127 127 SER SER C . n 
C 1 136 GLY 136 128 128 GLY GLY C . n 
C 1 137 SER 137 129 129 SER SER C . n 
C 1 138 SER 138 130 130 SER SER C . n 
C 1 139 TYR 139 131 131 TYR TYR C . n 
C 1 140 PRO 140 132 132 PRO PRO C . n 
C 1 141 SER 141 133 133 SER SER C . n 
C 1 142 LEU 142 134 134 LEU LEU C . n 
C 1 143 LEU 143 135 135 LEU LEU C . n 
C 1 144 GLN 144 136 136 GLN GLN C . n 
C 1 145 CYS 145 137 137 CYS CYS C . n 
C 1 146 LEU 146 138 138 LEU LEU C . n 
C 1 147 LYS 147 139 139 LYS LYS C . n 
C 1 148 ALA 148 140 140 ALA ALA C . n 
C 1 149 PRO 149 141 141 PRO PRO C . n 
C 1 150 VAL 150 142 142 VAL VAL C . n 
C 1 151 LEU 151 143 143 LEU LEU C . n 
C 1 152 SER 152 144 144 SER SER C . n 
C 1 153 ASP 153 145 145 ASP ASP C . n 
C 1 154 SER 154 146 146 SER SER C . n 
C 1 155 SER 155 147 147 SER SER C . n 
C 1 156 CYS 156 148 148 CYS CYS C . n 
C 1 157 LYS 157 149 149 LYS LYS C . n 
C 1 158 SER 158 150 150 SER SER C . n 
C 1 159 SER 159 151 151 SER SER C . n 
C 1 160 TYR 160 152 152 TYR TYR C . n 
C 1 161 PRO 161 153 153 PRO PRO C . n 
C 1 162 GLY 162 154 154 GLY GLY C . n 
C 1 163 GLN 163 155 155 GLN GLN C . n 
C 1 164 ILE 164 156 156 ILE ILE C . n 
C 1 165 THR 165 157 157 THR THR C . n 
C 1 166 GLY 166 158 158 GLY GLY C . n 
C 1 167 ASN 167 159 159 ASN ASN C . n 
C 1 168 MET 168 160 160 MET MET C . n 
C 1 169 ILE 169 161 161 ILE ILE C . n 
C 1 170 CYS 170 162 162 CYS CYS C . n 
C 1 171 VAL 171 163 163 VAL VAL C . n 
C 1 172 GLY 172 164 164 GLY GLY C . n 
C 1 173 PHE 173 165 165 PHE PHE C . n 
C 1 174 LEU 174 166 166 LEU LEU C . n 
C 1 175 GLU 175 167 167 GLU GLU C . n 
C 1 176 GLY 176 168 168 GLY GLY C . n 
C 1 177 GLY 177 169 169 GLY GLY C . n 
C 1 178 LYS 178 170 170 LYS LYS C . n 
C 1 179 ASP 179 171 171 ASP ASP C . n 
C 1 180 SER 180 172 172 SER SER C . n 
C 1 181 CYS 181 173 173 CYS CYS C . n 
C 1 182 GLN 182 174 174 GLN GLN C . n 
C 1 183 GLY 183 175 175 GLY GLY C . n 
C 1 184 ASP 184 176 176 ASP ASP C . n 
C 1 185 SER 185 177 177 SER SER C . n 
C 1 186 GLY 186 178 178 GLY GLY C . n 
C 1 187 GLY 187 179 179 GLY GLY C . n 
C 1 188 PRO 188 180 180 PRO PRO C . n 
C 1 189 VAL 189 181 181 VAL VAL C . n 
C 1 190 VAL 190 182 182 VAL VAL C . n 
C 1 191 CYS 191 183 183 CYS CYS C . n 
C 1 192 ASN 192 184 184 ASN ASN C . n 
C 1 193 GLY 193 185 185 GLY GLY C . n 
C 1 194 GLN 194 186 186 GLN GLN C . n 
C 1 195 LEU 195 187 187 LEU LEU C . n 
C 1 196 GLN 196 188 188 GLN GLN C . n 
C 1 197 GLY 197 189 189 GLY GLY C . n 
C 1 198 ILE 198 190 190 ILE ILE C . n 
C 1 199 VAL 199 191 191 VAL VAL C . n 
C 1 200 SER 200 192 192 SER SER C . n 
C 1 201 TRP 201 193 193 TRP TRP C . n 
C 1 202 GLY 202 194 194 GLY GLY C . n 
C 1 203 TYR 203 195 195 TYR TYR C . n 
C 1 204 GLY 204 196 196 GLY GLY C . n 
C 1 205 CYS 205 197 197 CYS CYS C . n 
C 1 206 ALA 206 198 198 ALA ALA C . n 
C 1 207 GLN 207 199 199 GLN GLN C . n 
C 1 208 LYS 208 200 200 LYS LYS C . n 
C 1 209 ASN 209 201 201 ASN ASN C . n 
C 1 210 LYS 210 202 202 LYS LYS C . n 
C 1 211 PRO 211 203 203 PRO PRO C . n 
C 1 212 GLY 212 204 204 GLY GLY C . n 
C 1 213 VAL 213 205 205 VAL VAL C . n 
C 1 214 TYR 214 206 206 TYR TYR C . n 
C 1 215 THR 215 207 207 THR THR C . n 
C 1 216 LYS 216 208 208 LYS LYS C . n 
C 1 217 VAL 217 209 209 VAL VAL C . n 
C 1 218 CYS 218 210 210 CYS CYS C . n 
C 1 219 ASN 219 211 211 ASN ASN C . n 
C 1 220 TYR 220 212 212 TYR TYR C . n 
C 1 221 VAL 221 213 213 VAL VAL C . n 
C 1 222 ASN 222 214 214 ASN ASN C . n 
C 1 223 TRP 223 215 215 TRP TRP C . n 
C 1 224 ILE 224 216 216 ILE ILE C . n 
C 1 225 GLN 225 217 217 GLN GLN C . n 
C 1 226 GLN 226 218 218 GLN GLN C . n 
C 1 227 THR 227 219 219 THR THR C . n 
C 1 228 ILE 228 220 220 ILE ILE C . n 
C 1 229 ALA 229 221 221 ALA ALA C . n 
C 1 230 ALA 230 222 222 ALA ALA C . n 
C 1 231 ASN 231 223 223 ASN ASN C . n 
D 2 1   GLU 1   1   ?   ?   ?   D . n 
D 2 2   SER 2   2   ?   ?   ?   D . n 
D 2 3   PRO 3   3   ?   ?   ?   D . n 
D 2 4   LEU 4   4   4   LEU LEU D . n 
D 2 5   PRO 5   5   5   PRO PRO D . n 
D 2 6   LYS 6   6   6   LYS LYS D . n 
D 2 7   PRO 7   7   7   PRO PRO D . n 
D 2 8   VAL 8   8   8   VAL VAL D . n 
D 2 9   LEU 9   9   9   LEU LEU D . n 
D 2 10  ASP 10  10  10  ASP ASP D . n 
D 2 11  THR 11  11  11  THR THR D . n 
D 2 12  ASN 12  12  12  ASN ASN D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  LYS 14  14  14  LYS LYS D . n 
D 2 15  LYS 15  15  15  LYS LYS D . n 
D 2 16  LEU 16  16  16  LEU LEU D . n 
D 2 17  ASN 17  17  17  ASN ASN D . n 
D 2 18  PRO 18  18  18  PRO PRO D . n 
D 2 19  ASN 19  19  19  ASN ASN D . n 
D 2 20  SER 20  20  20  SER SER D . n 
D 2 21  SER 21  21  21  SER SER D . n 
D 2 22  TYR 22  22  22  TYR TYR D . n 
D 2 23  ARG 23  23  23  ARG ARG D . n 
D 2 24  ILE 24  24  24  ILE ILE D . n 
D 2 25  ILE 25  25  25  ILE ILE D . n 
D 2 26  SER 26  26  26  SER SER D . n 
D 2 27  THR 27  27  27  THR THR D . n 
D 2 28  PHE 28  28  28  PHE PHE D . n 
D 2 29  TRP 29  29  29  TRP TRP D . n 
D 2 30  GLY 30  30  30  GLY GLY D . n 
D 2 31  ALA 31  31  31  ALA ALA D . n 
D 2 32  LEU 32  32  32  LEU LEU D . n 
D 2 33  GLY 33  33  33  GLY GLY D . n 
D 2 34  GLY 34  34  34  GLY GLY D . n 
D 2 35  ASP 35  35  35  ASP ASP D . n 
D 2 36  VAL 36  36  36  VAL VAL D . n 
D 2 37  TYR 37  37  37  TYR TYR D . n 
D 2 38  LEU 38  38  38  LEU LEU D . n 
D 2 39  GLY 39  39  39  GLY GLY D . n 
D 2 40  LYS 40  40  40  LYS LYS D . n 
D 2 41  SER 41  41  41  SER SER D . n 
D 2 42  PRO 42  42  42  PRO PRO D . n 
D 2 43  ASN 43  43  43  ASN ASN D . n 
D 2 44  SER 44  44  44  SER SER D . n 
D 2 45  ASP 45  45  45  ASP ASP D . n 
D 2 46  ALA 46  46  46  ALA ALA D . n 
D 2 47  PRO 47  47  47  PRO PRO D . n 
D 2 48  CYS 48  48  48  CYS CYS D . n 
D 2 49  PRO 49  49  49  PRO PRO D . n 
D 2 50  ASP 50  50  50  ASP ASP D . n 
D 2 51  GLY 51  51  51  GLY GLY D . n 
D 2 52  VAL 52  52  52  VAL VAL D . n 
D 2 53  PHE 53  53  53  PHE PHE D . n 
D 2 54  ARG 54  54  54  ARG ARG D . n 
D 2 55  TYR 55  55  55  TYR TYR D . n 
D 2 56  ASN 56  56  56  ASN ASN D . n 
D 2 57  SER 57  57  57  SER SER D . n 
D 2 58  ASP 58  58  58  ASP ASP D . n 
D 2 59  VAL 59  59  59  VAL VAL D . n 
D 2 60  GLY 60  60  60  GLY GLY D . n 
D 2 61  PRO 61  61  61  PRO PRO D . n 
D 2 62  SER 62  62  62  SER SER D . n 
D 2 63  GLY 63  63  63  GLY GLY D . n 
D 2 64  THR 64  64  64  THR THR D . n 
D 2 65  PRO 65  65  65  PRO PRO D . n 
D 2 66  VAL 66  66  66  VAL VAL D . n 
D 2 67  ARG 67  67  67  ARG ARG D . n 
D 2 68  PHE 68  68  68  PHE PHE D . n 
D 2 69  ILE 69  69  69  ILE ILE D . n 
D 2 70  PRO 70  70  70  PRO PRO D . n 
D 2 71  LEU 71  71  71  LEU LEU D . n 
D 2 72  SER 72  72  72  SER SER D . n 
D 2 73  GLY 73  73  73  GLY GLY D . n 
D 2 74  ALA 74  74  74  ALA ALA D . n 
D 2 75  ASN 75  75  75  ASN ASN D . n 
D 2 76  ILE 76  76  76  ILE ILE D . n 
D 2 77  PHE 77  77  77  PHE PHE D . n 
D 2 78  GLU 78  78  78  GLU GLU D . n 
D 2 79  ASP 79  79  79  ASP ASP D . n 
D 2 80  GLN 80  80  80  GLN GLN D . n 
D 2 81  LEU 81  81  81  LEU LEU D . n 
D 2 82  LEU 82  82  82  LEU LEU D . n 
D 2 83  ASN 83  83  83  ASN ASN D . n 
D 2 84  ILE 84  84  84  ILE ILE D . n 
D 2 85  GLN 85  85  85  GLN GLN D . n 
D 2 86  PHE 86  86  86  PHE PHE D . n 
D 2 87  ASN 87  87  87  ASN ASN D . n 
D 2 88  ILE 88  88  88  ILE ILE D . n 
D 2 89  PRO 89  89  89  PRO PRO D . n 
D 2 90  THR 90  90  90  THR THR D . n 
D 2 91  VAL 91  91  91  VAL VAL D . n 
D 2 92  LYS 92  92  92  LYS LYS D . n 
D 2 93  LEU 93  93  93  LEU LEU D . n 
D 2 94  CYS 94  94  94  CYS CYS D . n 
D 2 95  VAL 95  95  95  VAL VAL D . n 
D 2 96  SER 96  96  96  SER SER D . n 
D 2 97  TYR 97  97  97  TYR TYR D . n 
D 2 98  THR 98  98  98  THR THR D . n 
D 2 99  ILE 99  99  99  ILE ILE D . n 
D 2 100 TRP 100 100 100 TRP TRP D . n 
D 2 101 LYS 101 101 101 LYS LYS D . n 
D 2 102 VAL 102 102 102 VAL VAL D . n 
D 2 103 GLY 103 103 103 GLY GLY D . n 
D 2 104 ASN 104 104 ?   ?   ?   D . n 
D 2 105 ILE 105 105 ?   ?   ?   D . n 
D 2 106 ASN 106 106 ?   ?   ?   D . n 
D 2 107 ALA 107 107 ?   ?   ?   D . n 
D 2 108 HIS 108 108 ?   ?   ?   D . n 
D 2 109 LEU 109 109 109 LEU GLY D . n 
D 2 110 ARG 110 110 110 ARG ARG D . n 
D 2 111 THR 111 111 111 THR THR D . n 
D 2 112 MET 112 112 112 MET MET D . n 
D 2 113 LEU 113 113 113 LEU LEU D . n 
D 2 114 LEU 114 114 114 LEU LEU D . n 
D 2 115 GLU 115 115 115 GLU GLU D . n 
D 2 116 THR 116 116 116 THR THR D . n 
D 2 117 GLY 117 117 117 GLY GLY D . n 
D 2 118 GLY 118 118 118 GLY GLY D . n 
D 2 119 THR 119 119 119 THR THR D . n 
D 2 120 ILE 120 120 120 ILE ILE D . n 
D 2 121 GLY 121 121 121 GLY GLY D . n 
D 2 122 GLN 122 122 122 GLN GLN D . n 
D 2 123 ALA 123 123 123 ALA ALA D . n 
D 2 124 ASP 124 124 124 ASP ASP D . n 
D 2 125 SER 125 125 125 SER SER D . n 
D 2 126 SER 126 126 126 SER SER D . n 
D 2 127 TYR 127 127 127 TYR TYR D . n 
D 2 128 PHE 128 128 128 PHE PHE D . n 
D 2 129 LYS 129 129 129 LYS LYS D . n 
D 2 130 ILE 130 130 130 ILE ILE D . n 
D 2 131 VAL 131 131 131 VAL VAL D . n 
D 2 132 LYS 132 132 132 LYS LYS D . n 
D 2 133 SER 133 133 133 SER SER D . n 
D 2 134 SER 134 134 134 SER SER D . n 
D 2 135 LYS 135 135 135 LYS LYS D . n 
D 2 136 PHE 136 136 136 PHE PHE D . n 
D 2 137 GLY 137 137 137 GLY GLY D . n 
D 2 138 TYR 138 138 138 TYR TYR D . n 
D 2 139 ASN 139 139 139 ASN ASN D . n 
D 2 140 LEU 140 140 140 LEU LEU D . n 
D 2 141 LEU 141 141 141 LEU LEU D . n 
D 2 142 TYR 142 142 142 TYR TYR D . n 
D 2 143 CYS 143 143 143 CYS CYS D . n 
D 2 144 PRO 144 144 144 PRO PRO D . n 
D 2 145 LEU 145 145 145 LEU LEU D . n 
D 2 146 THR 146 146 ?   ?   ?   D . n 
D 2 147 ARG 147 147 ?   ?   ?   D . n 
D 2 148 HIS 148 148 ?   ?   ?   D . n 
D 2 149 PHE 149 149 ?   ?   ?   D . n 
D 2 150 LEU 150 150 ?   ?   ?   D . n 
D 2 151 CYS 151 151 ?   ?   ?   D . n 
D 2 152 PRO 152 152 ?   ?   ?   D . n 
D 2 153 PHE 153 153 ?   ?   ?   D . n 
D 2 154 CYS 154 154 ?   ?   ?   D . n 
D 2 155 ARG 155 155 ?   ?   ?   D . n 
D 2 156 ASP 156 156 ?   ?   ?   D . n 
D 2 157 ASP 157 157 ?   ?   ?   D . n 
D 2 158 ASN 158 158 ?   ?   ?   D . n 
D 2 159 PHE 159 159 159 PHE PHE D . n 
D 2 160 CYS 160 160 160 CYS CYS D . n 
D 2 161 ALA 161 161 161 ALA ALA D . n 
D 2 162 LYS 162 162 162 LYS LYS D . n 
D 2 163 VAL 163 163 163 VAL VAL D . n 
D 2 164 GLY 164 164 164 GLY GLY D . n 
D 2 165 VAL 165 165 165 VAL VAL D . n 
D 2 166 VAL 166 166 166 VAL VAL D . n 
D 2 167 ILE 167 167 167 ILE ILE D . n 
D 2 168 GLN 168 168 168 GLN GLN D . n 
D 2 169 ASN 169 169 169 ASN ASN D . n 
D 2 170 GLY 170 170 170 GLY GLY D . n 
D 2 171 LYS 171 171 171 LYS LYS D . n 
D 2 172 ARG 172 172 172 ARG ARG D . n 
D 2 173 ARG 173 173 173 ARG ARG D . n 
D 2 174 LEU 174 174 174 LEU LEU D . n 
D 2 175 ALA 175 175 175 ALA ALA D . n 
D 2 176 LEU 176 176 176 LEU LEU D . n 
D 2 177 VAL 177 177 177 VAL VAL D . n 
D 2 178 ASN 178 178 178 ASN ASN D . n 
D 2 179 GLU 179 179 179 GLU GLU D . n 
D 2 180 ASN 180 180 180 ASN ASN D . n 
D 2 181 PRO 181 181 181 PRO PRO D . n 
D 2 182 LEU 182 182 182 LEU LEU D . n 
D 2 183 ASP 183 183 183 ASP ASP D . n 
D 2 184 VAL 184 184 184 VAL VAL D . n 
D 2 185 LEU 185 185 185 LEU LEU D . n 
D 2 186 PHE 186 186 186 PHE PHE D . n 
D 2 187 GLN 187 187 187 GLN GLN D . n 
D 2 188 GLU 188 188 188 GLU GLU D . n 
D 2 189 VAL 189 189 189 VAL VAL D . n 
D 2 190 HIS 190 190 ?   ?   ?   D . n 
D 2 191 HIS 191 191 ?   ?   ?   D . n 
D 2 192 HIS 192 192 ?   ?   ?   D . n 
D 2 193 HIS 193 193 ?   ?   ?   D . n 
D 2 194 HIS 194 194 ?   ?   ?   D . n 
D 2 195 HIS 195 195 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 CA  1  301 1   CA  CA  A . 
F 3 CA  1  301 2   CA  CA  C . 
G 4 HOH 1  401 13  HOH HOH A . 
G 4 HOH 2  402 165 HOH HOH A . 
G 4 HOH 3  403 9   HOH HOH A . 
G 4 HOH 4  404 121 HOH HOH A . 
G 4 HOH 5  405 89  HOH HOH A . 
G 4 HOH 6  406 90  HOH HOH A . 
G 4 HOH 7  407 169 HOH HOH A . 
G 4 HOH 8  408 59  HOH HOH A . 
G 4 HOH 9  409 5   HOH HOH A . 
G 4 HOH 10 410 77  HOH HOH A . 
G 4 HOH 11 411 187 HOH HOH A . 
G 4 HOH 12 412 52  HOH HOH A . 
G 4 HOH 13 413 106 HOH HOH A . 
G 4 HOH 14 414 51  HOH HOH A . 
G 4 HOH 15 415 67  HOH HOH A . 
G 4 HOH 16 416 222 HOH HOH A . 
G 4 HOH 17 417 208 HOH HOH A . 
G 4 HOH 18 418 63  HOH HOH A . 
G 4 HOH 19 419 3   HOH HOH A . 
G 4 HOH 20 420 8   HOH HOH A . 
G 4 HOH 21 421 10  HOH HOH A . 
G 4 HOH 22 422 145 HOH HOH A . 
G 4 HOH 23 423 154 HOH HOH A . 
G 4 HOH 24 424 96  HOH HOH A . 
G 4 HOH 25 425 163 HOH HOH A . 
G 4 HOH 26 426 54  HOH HOH A . 
G 4 HOH 27 427 176 HOH HOH A . 
G 4 HOH 28 428 2   HOH HOH A . 
G 4 HOH 29 429 240 HOH HOH A . 
G 4 HOH 30 430 126 HOH HOH A . 
G 4 HOH 31 431 95  HOH HOH A . 
G 4 HOH 32 432 107 HOH HOH A . 
G 4 HOH 33 433 149 HOH HOH A . 
G 4 HOH 34 434 6   HOH HOH A . 
G 4 HOH 35 435 162 HOH HOH A . 
G 4 HOH 36 436 32  HOH HOH A . 
G 4 HOH 37 437 210 HOH HOH A . 
G 4 HOH 38 438 140 HOH HOH A . 
G 4 HOH 39 439 137 HOH HOH A . 
G 4 HOH 40 440 196 HOH HOH A . 
G 4 HOH 41 441 7   HOH HOH A . 
G 4 HOH 42 442 38  HOH HOH A . 
G 4 HOH 43 443 91  HOH HOH A . 
G 4 HOH 44 444 84  HOH HOH A . 
G 4 HOH 45 445 167 HOH HOH A . 
G 4 HOH 46 446 144 HOH HOH A . 
G 4 HOH 47 447 166 HOH HOH A . 
G 4 HOH 48 448 173 HOH HOH A . 
G 4 HOH 49 449 53  HOH HOH A . 
G 4 HOH 50 450 86  HOH HOH A . 
G 4 HOH 51 451 11  HOH HOH A . 
G 4 HOH 52 452 207 HOH HOH A . 
G 4 HOH 53 453 111 HOH HOH A . 
G 4 HOH 54 454 175 HOH HOH A . 
G 4 HOH 55 455 158 HOH HOH A . 
G 4 HOH 56 456 156 HOH HOH A . 
G 4 HOH 57 457 185 HOH HOH A . 
G 4 HOH 58 458 239 HOH HOH A . 
G 4 HOH 59 459 12  HOH HOH A . 
G 4 HOH 60 460 192 HOH HOH A . 
G 4 HOH 61 461 128 HOH HOH A . 
G 4 HOH 62 462 238 HOH HOH A . 
G 4 HOH 63 463 101 HOH HOH A . 
H 4 HOH 1  201 194 HOH HOH B . 
H 4 HOH 2  202 31  HOH HOH B . 
H 4 HOH 3  203 190 HOH HOH B . 
H 4 HOH 4  204 70  HOH HOH B . 
H 4 HOH 5  205 39  HOH HOH B . 
H 4 HOH 6  206 25  HOH HOH B . 
H 4 HOH 7  207 27  HOH HOH B . 
H 4 HOH 8  208 20  HOH HOH B . 
H 4 HOH 9  209 73  HOH HOH B . 
H 4 HOH 10 210 47  HOH HOH B . 
H 4 HOH 11 211 55  HOH HOH B . 
H 4 HOH 12 212 110 HOH HOH B . 
H 4 HOH 13 213 74  HOH HOH B . 
H 4 HOH 14 214 80  HOH HOH B . 
H 4 HOH 15 215 92  HOH HOH B . 
H 4 HOH 16 216 153 HOH HOH B . 
H 4 HOH 17 217 97  HOH HOH B . 
H 4 HOH 18 218 19  HOH HOH B . 
H 4 HOH 19 219 138 HOH HOH B . 
H 4 HOH 20 220 62  HOH HOH B . 
H 4 HOH 21 221 34  HOH HOH B . 
H 4 HOH 22 222 65  HOH HOH B . 
H 4 HOH 23 223 40  HOH HOH B . 
H 4 HOH 24 224 109 HOH HOH B . 
H 4 HOH 25 225 164 HOH HOH B . 
H 4 HOH 26 226 127 HOH HOH B . 
H 4 HOH 27 227 133 HOH HOH B . 
H 4 HOH 28 228 81  HOH HOH B . 
H 4 HOH 29 229 102 HOH HOH B . 
H 4 HOH 30 230 174 HOH HOH B . 
H 4 HOH 31 231 99  HOH HOH B . 
H 4 HOH 32 232 177 HOH HOH B . 
H 4 HOH 33 233 178 HOH HOH B . 
H 4 HOH 34 234 221 HOH HOH B . 
H 4 HOH 35 235 201 HOH HOH B . 
H 4 HOH 36 236 186 HOH HOH B . 
H 4 HOH 37 237 172 HOH HOH B . 
H 4 HOH 38 238 108 HOH HOH B . 
H 4 HOH 39 239 205 HOH HOH B . 
H 4 HOH 40 240 168 HOH HOH B . 
H 4 HOH 41 241 104 HOH HOH B . 
I 4 HOH 1  401 143 HOH HOH C . 
I 4 HOH 2  402 227 HOH HOH C . 
I 4 HOH 3  403 58  HOH HOH C . 
I 4 HOH 4  404 184 HOH HOH C . 
I 4 HOH 5  405 24  HOH HOH C . 
I 4 HOH 6  406 16  HOH HOH C . 
I 4 HOH 7  407 49  HOH HOH C . 
I 4 HOH 8  408 14  HOH HOH C . 
I 4 HOH 9  409 17  HOH HOH C . 
I 4 HOH 10 410 15  HOH HOH C . 
I 4 HOH 11 411 82  HOH HOH C . 
I 4 HOH 12 412 56  HOH HOH C . 
I 4 HOH 13 413 113 HOH HOH C . 
I 4 HOH 14 414 170 HOH HOH C . 
I 4 HOH 15 415 75  HOH HOH C . 
I 4 HOH 16 416 123 HOH HOH C . 
I 4 HOH 17 417 112 HOH HOH C . 
I 4 HOH 18 418 79  HOH HOH C . 
I 4 HOH 19 419 191 HOH HOH C . 
I 4 HOH 20 420 139 HOH HOH C . 
I 4 HOH 21 421 117 HOH HOH C . 
I 4 HOH 22 422 36  HOH HOH C . 
I 4 HOH 23 423 193 HOH HOH C . 
I 4 HOH 24 424 35  HOH HOH C . 
I 4 HOH 25 425 43  HOH HOH C . 
I 4 HOH 26 426 160 HOH HOH C . 
I 4 HOH 27 427 57  HOH HOH C . 
I 4 HOH 28 428 157 HOH HOH C . 
I 4 HOH 29 429 202 HOH HOH C . 
I 4 HOH 30 430 23  HOH HOH C . 
I 4 HOH 31 431 150 HOH HOH C . 
I 4 HOH 32 432 119 HOH HOH C . 
I 4 HOH 33 433 85  HOH HOH C . 
I 4 HOH 34 434 141 HOH HOH C . 
I 4 HOH 35 435 206 HOH HOH C . 
I 4 HOH 36 436 211 HOH HOH C . 
I 4 HOH 37 437 223 HOH HOH C . 
I 4 HOH 38 438 203 HOH HOH C . 
I 4 HOH 39 439 28  HOH HOH C . 
I 4 HOH 40 440 231 HOH HOH C . 
I 4 HOH 41 441 217 HOH HOH C . 
I 4 HOH 42 442 214 HOH HOH C . 
I 4 HOH 43 443 218 HOH HOH C . 
I 4 HOH 44 444 159 HOH HOH C . 
I 4 HOH 45 445 226 HOH HOH C . 
I 4 HOH 46 446 230 HOH HOH C . 
I 4 HOH 47 447 103 HOH HOH C . 
I 4 HOH 48 448 209 HOH HOH C . 
I 4 HOH 49 449 228 HOH HOH C . 
I 4 HOH 50 450 200 HOH HOH C . 
J 4 HOH 1  201 232 HOH HOH D . 
J 4 HOH 2  202 94  HOH HOH D . 
J 4 HOH 3  203 22  HOH HOH D . 
J 4 HOH 4  204 180 HOH HOH D . 
J 4 HOH 5  205 142 HOH HOH D . 
J 4 HOH 6  206 45  HOH HOH D . 
J 4 HOH 7  207 136 HOH HOH D . 
J 4 HOH 8  208 69  HOH HOH D . 
J 4 HOH 9  209 48  HOH HOH D . 
J 4 HOH 10 210 50  HOH HOH D . 
J 4 HOH 11 211 18  HOH HOH D . 
J 4 HOH 12 212 76  HOH HOH D . 
J 4 HOH 13 213 29  HOH HOH D . 
J 4 HOH 14 214 42  HOH HOH D . 
J 4 HOH 15 215 237 HOH HOH D . 
J 4 HOH 16 216 21  HOH HOH D . 
J 4 HOH 17 217 125 HOH HOH D . 
J 4 HOH 18 218 66  HOH HOH D . 
J 4 HOH 19 219 198 HOH HOH D . 
J 4 HOH 20 220 189 HOH HOH D . 
J 4 HOH 21 221 98  HOH HOH D . 
J 4 HOH 22 222 116 HOH HOH D . 
J 4 HOH 23 223 135 HOH HOH D . 
J 4 HOH 24 224 78  HOH HOH D . 
J 4 HOH 25 225 26  HOH HOH D . 
J 4 HOH 26 226 122 HOH HOH D . 
J 4 HOH 27 227 152 HOH HOH D . 
J 4 HOH 28 228 100 HOH HOH D . 
J 4 HOH 29 229 60  HOH HOH D . 
J 4 HOH 30 230 33  HOH HOH D . 
J 4 HOH 31 231 68  HOH HOH D . 
J 4 HOH 32 232 83  HOH HOH D . 
J 4 HOH 33 233 179 HOH HOH D . 
J 4 HOH 34 234 118 HOH HOH D . 
J 4 HOH 35 235 235 HOH HOH D . 
J 4 HOH 36 236 87  HOH HOH D . 
J 4 HOH 37 237 213 HOH HOH D . 
J 4 HOH 38 238 229 HOH HOH D . 
J 4 HOH 39 239 132 HOH HOH D . 
J 4 HOH 40 240 236 HOH HOH D . 
J 4 HOH 41 241 233 HOH HOH D . 
J 4 HOH 42 242 216 HOH HOH D . 
J 4 HOH 43 243 147 HOH HOH D . 
J 4 HOH 44 244 195 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 D LEU 109 ? CB  ? D LEU 109 CB  
2 1 Y 1 D LEU 109 ? CG  ? D LEU 109 CG  
3 1 Y 1 D LEU 109 ? CD1 ? D LEU 109 CD1 
4 1 Y 1 D LEU 109 ? CD2 ? D LEU 109 CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? 2.7.17      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CT1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.249 
_cell.length_a_esd                 ? 
_cell.length_b                     85.887 
_cell.length_b_esd                 ? 
_cell.length_c                     186.063 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CT1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CT1 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.62 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_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    
'0.085 M Sodium acetate trihydrate pH 4.6, 0.17 M Ammonium acetate, 25.5% w/v Polyethylene glycol 4,000, 15% v/v Glycerol' 
_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 PILATUS 200K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-08-07 
_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                    'VariMax HF optics' 
_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   1.5417 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        RIGAKU 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5417 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CT1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.42 
_reflns.d_resolution_low                               45.8 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     29614 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.37 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          23.68 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.42 
_reflns_shell.d_res_low                                     2.52 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.55 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2886 
_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                               2.9 
_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                                  0.72 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.63 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CT1 
_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                            2.42 
_refine.ls_d_res_low                             45.80 
_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                     29540 
_refine.ls_number_reflns_R_free                  1419 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.39 
_refine.ls_percent_reflns_R_free                 4.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1860 
_refine.ls_R_factor_R_free                       0.2442 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1829 
_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       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.59 
_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                            0.31 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5876 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             198 
_refine_hist.number_atoms_total               6076 
_refine_hist.d_res_high                       2.42 
_refine_hist.d_res_low                        45.80 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011 ? 6054 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.216 ? 8235 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.527 ? 840  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.057 ? 924  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 1074 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.42 2.51 . . 129 2757 98.00  . . . . 0.2333 . . . . . . . . . . . 0.3303 
'X-RAY DIFFRACTION' 2.51 2.61 . . 139 2759 100.00 . . . . 0.2302 . . . . . . . . . . . 0.2854 
'X-RAY DIFFRACTION' 2.61 2.73 . . 145 2747 100.00 . . . . 0.2230 . . . . . . . . . . . 0.3518 
'X-RAY DIFFRACTION' 2.73 2.87 . . 129 2778 99.00  . . . . 0.2182 . . . . . . . . . . . 0.3322 
'X-RAY DIFFRACTION' 2.87 3.05 . . 132 2787 99.00  . . . . 0.2021 . . . . . . . . . . . 0.2676 
'X-RAY DIFFRACTION' 3.05 3.29 . . 134 2789 100.00 . . . . 0.1966 . . . . . . . . . . . 0.2619 
'X-RAY DIFFRACTION' 3.29 3.62 . . 154 2810 100.00 . . . . 0.1775 . . . . . . . . . . . 0.2597 
'X-RAY DIFFRACTION' 3.62 4.14 . . 143 2824 100.00 . . . . 0.1565 . . . . . . . . . . . 0.2366 
'X-RAY DIFFRACTION' 4.14 5.22 . . 150 2875 100.00 . . . . 0.1466 . . . . . . . . . . . 0.1718 
'X-RAY DIFFRACTION' 5.22 10.0 . . 164 2995 99.00  . . . . 0.1781 . . . . . . . . . . . 0.2072 
# 
_struct.entry_id                     9CT1 
_struct.title                        'Complex between the porcine trypsin and M271 a Kunitz-STI from Solanum tuberosum' 
_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        9CT1 
_struct_keywords.text            
'Kunitz, Serine Proteases, Serine Proteinase Inhibitors, Soybean Trypsin Inhibitor, Trypsin Inhibitor, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP TRYP_PIG         P00761     ? 1 
;FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIIT
HPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSY
PGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN
;
1  
2 UNP A0A097H115_SOLTU A0A097H115 ? 2 
;ESPVPKPVLDTNGKKLNPNSSYRIISTFWGALGGDVYLGKSPNSDAPCPDGVFRYNSDVGPSGTPVRFIPLSGANIFEDQ
LLNIQFNIPTVKLCVSYTIWKVGNINAHLRTMLLETGGTIGQADSSYFKIVKSSKFGYNLLYCPLTRHFLCPFCRDDNFC
AKVGVVIQNGKRRLALVNENPLDVLFQEV
;
33 
# 
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 9CT1 A 1 ? 231 ? P00761     1  ? 231 ? -7 223 
2 2 9CT1 B 1 ? 189 ? A0A097H115 33 ? 221 ? 1  189 
3 1 9CT1 C 1 ? 231 ? P00761     1  ? 231 ? -7 223 
4 2 9CT1 D 1 ? 189 ? A0A097H115 33 ? 221 ? 1  189 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
2 9CT1 LEU B 4   ? UNP A0A097H115 VAL 36 conflict         4   1  
2 9CT1 HIS B 190 ? UNP A0A097H115 ?   ?  'expression tag' 190 2  
2 9CT1 HIS B 191 ? UNP A0A097H115 ?   ?  'expression tag' 191 3  
2 9CT1 HIS B 192 ? UNP A0A097H115 ?   ?  'expression tag' 192 4  
2 9CT1 HIS B 193 ? UNP A0A097H115 ?   ?  'expression tag' 193 5  
2 9CT1 HIS B 194 ? UNP A0A097H115 ?   ?  'expression tag' 194 6  
2 9CT1 HIS B 195 ? UNP A0A097H115 ?   ?  'expression tag' 195 7  
4 9CT1 LEU D 4   ? UNP A0A097H115 VAL 36 conflict         4   8  
4 9CT1 HIS D 190 ? UNP A0A097H115 ?   ?  'expression tag' 190 9  
4 9CT1 HIS D 191 ? UNP A0A097H115 ?   ?  'expression tag' 191 10 
4 9CT1 HIS D 192 ? UNP A0A097H115 ?   ?  'expression tag' 192 11 
4 9CT1 HIS D 193 ? UNP A0A097H115 ?   ?  'expression tag' 193 12 
4 9CT1 HIS D 194 ? UNP A0A097H115 ?   ?  'expression tag' 194 13 
4 9CT1 HIS D 195 ? UNP A0A097H115 ?   ?  'expression tag' 195 14 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1840  ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  16420 ? 
2 'ABSA (A^2)' 1810  ? 
2 MORE         -24   ? 
2 'SSA (A^2)'  16650 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,G,H 
2 1 C,D,F,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ALA A 46  ? TYR A 50  ? ALA A 38  TYR A 42  5 ? 5  
HELX_P HELX_P2 AA2 SER A 152 ? TYR A 160 ? SER A 144 TYR A 152 1 ? 9  
HELX_P HELX_P3 AA3 TYR A 220 ? ASN A 231 ? TYR A 212 ASN A 223 1 ? 12 
HELX_P HELX_P4 AA4 VAL B 91  ? THR B 98  ? VAL B 91  THR B 98  5 ? 8  
HELX_P HELX_P5 AA5 ALA C 46  ? TYR C 50  ? ALA C 38  TYR C 42  5 ? 5  
HELX_P HELX_P6 AA6 SER C 152 ? TYR C 160 ? SER C 144 TYR C 152 1 ? 9  
HELX_P HELX_P7 AA7 TYR C 220 ? ASN C 231 ? TYR C 212 ASN C 223 1 ? 12 
HELX_P HELX_P8 AA8 VAL D 91  ? ILE D 99  ? VAL D 91  ILE D 99  5 ? 9  
# 
_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 15  SG  ? ? ? 1_555 A CYS 145 SG ? ? A CYS 7   A CYS 137 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf2  disulf ? ? A CYS 33  SG  ? ? ? 1_555 A CYS 49  SG ? ? A CYS 25  A CYS 41  1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf3  disulf ? ? A CYS 117 SG  ? ? ? 1_555 A CYS 218 SG ? ? A CYS 109 A CYS 210 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf4  disulf ? ? A CYS 124 SG  ? ? ? 1_555 A CYS 191 SG ? ? A CYS 116 A CYS 183 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf5  disulf ? ? A CYS 156 SG  ? ? ? 1_555 A CYS 170 SG ? ? A CYS 148 A CYS 162 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
disulf6  disulf ? ? A CYS 181 SG  ? ? ? 1_555 A CYS 205 SG A ? A CYS 173 A CYS 197 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf7  disulf ? ? A CYS 181 SG  ? ? ? 1_555 A CYS 205 SG B ? A CYS 173 A CYS 197 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf8  disulf ? ? B CYS 48  SG  ? ? ? 1_555 B CYS 94  SG ? ? B CYS 48  B CYS 94  1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf9  disulf ? ? B CYS 143 SG  ? ? ? 1_555 B CYS 160 SG ? ? B CYS 143 B CYS 160 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
disulf10 disulf ? ? C CYS 15  SG  ? ? ? 1_555 C CYS 145 SG ? ? C CYS 7   C CYS 137 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf11 disulf ? ? C CYS 33  SG  ? ? ? 1_555 C CYS 49  SG ? ? C CYS 25  C CYS 41  1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf12 disulf ? ? C CYS 117 SG  ? ? ? 1_555 C CYS 218 SG ? ? C CYS 109 C CYS 210 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
disulf13 disulf ? ? C CYS 124 SG  ? ? ? 1_555 C CYS 191 SG ? ? C CYS 116 C CYS 183 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf14 disulf ? ? C CYS 156 SG  ? ? ? 1_555 C CYS 170 SG ? ? C CYS 148 C CYS 162 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf15 disulf ? ? C CYS 181 SG  ? ? ? 1_555 C CYS 205 SG A ? C CYS 173 C CYS 197 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf16 disulf ? ? C CYS 181 SG  ? ? ? 1_555 C CYS 205 SG B ? C CYS 173 C CYS 197 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
disulf17 disulf ? ? D CYS 48  SG  ? ? ? 1_555 D CYS 94  SG ? ? D CYS 48  D CYS 94  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf18 disulf ? ? D CYS 143 SG  ? ? ? 1_555 D CYS 160 SG ? ? D CYS 143 D CYS 160 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc1  metalc ? ? A GLU 60  OE1 ? ? ? 1_555 E CA  .   CA ? ? A GLU 52  A CA  301 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
metalc2  metalc ? ? A ASN 62  O   ? ? ? 1_555 E CA  .   CA ? ? A ASN 54  A CA  301 1_555 ? ? ? ? ? ? ? 2.230 ? ? 
metalc3  metalc ? ? A VAL 65  O   ? ? ? 1_555 E CA  .   CA ? ? A VAL 57  A CA  301 1_555 ? ? ? ? ? ? ? 2.499 ? ? 
metalc4  metalc ? ? A GLU 70  OE2 ? ? ? 1_555 E CA  .   CA ? ? A GLU 62  A CA  301 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc5  metalc ? ? E CA  .   CA  ? ? ? 1_555 G HOH .   O  ? ? A CA  301 A HOH 451 1_555 ? ? ? ? ? ? ? 2.542 ? ? 
metalc6  metalc ? ? E CA  .   CA  ? ? ? 1_555 G HOH .   O  ? ? A CA  301 A HOH 459 1_555 ? ? ? ? ? ? ? 2.976 ? ? 
metalc7  metalc ? ? C GLU 60  OE2 ? ? ? 1_555 F CA  .   CA ? ? C GLU 52  C CA  301 1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc8  metalc ? ? C ASN 62  O   ? ? ? 1_555 F CA  .   CA ? ? C ASN 54  C CA  301 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc9  metalc ? ? C VAL 65  O   ? ? ? 1_555 F CA  .   CA ? ? C VAL 57  C CA  301 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc10 metalc ? ? C GLU 70  OE2 ? ? ? 1_555 F CA  .   CA ? ? C GLU 62  C CA  301 1_555 ? ? ? ? ? ? ? 2.196 ? ? 
metalc11 metalc ? ? F CA  .   CA  ? ? ? 1_555 I HOH .   O  ? ? C CA  301 C HOH 421 1_555 ? ? ? ? ? ? ? 2.846 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLU 60 ? A GLU 52  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? A ASN 62 ? A ASN 54  ? 1_555 91.6  ? 
2  OE1 ? A GLU 60 ? A GLU 52  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? A VAL 65 ? A VAL 57  ? 1_555 158.8 ? 
3  O   ? A ASN 62 ? A ASN 54  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? A VAL 65 ? A VAL 57  ? 1_555 91.3  ? 
4  OE1 ? A GLU 60 ? A GLU 52  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 OE2 ? A GLU 70 ? A GLU 62  ? 1_555 84.0  ? 
5  O   ? A ASN 62 ? A ASN 54  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 OE2 ? A GLU 70 ? A GLU 62  ? 1_555 172.7 ? 
6  O   ? A VAL 65 ? A VAL 57  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 OE2 ? A GLU 70 ? A GLU 62  ? 1_555 94.9  ? 
7  OE1 ? A GLU 60 ? A GLU 52  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 451 ? 1_555 96.2  ? 
8  O   ? A ASN 62 ? A ASN 54  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 451 ? 1_555 87.1  ? 
9  O   ? A VAL 65 ? A VAL 57  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 451 ? 1_555 104.9 ? 
10 OE2 ? A GLU 70 ? A GLU 62  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 451 ? 1_555 87.6  ? 
11 OE1 ? A GLU 60 ? A GLU 52  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 459 ? 1_555 76.1  ? 
12 O   ? A ASN 62 ? A ASN 54  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 459 ? 1_555 95.0  ? 
13 O   ? A VAL 65 ? A VAL 57  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 459 ? 1_555 82.7  ? 
14 OE2 ? A GLU 70 ? A GLU 62  ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 459 ? 1_555 89.6  ? 
15 O   ? G HOH .  ? A HOH 451 ? 1_555 CA ? E CA . ? A CA 301 ? 1_555 O   ? G HOH .  ? A HOH 459 ? 1_555 172.0 ? 
16 OE2 ? C GLU 60 ? C GLU 52  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 O   ? C ASN 62 ? C ASN 54  ? 1_555 74.5  ? 
17 OE2 ? C GLU 60 ? C GLU 52  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 O   ? C VAL 65 ? C VAL 57  ? 1_555 138.3 ? 
18 O   ? C ASN 62 ? C ASN 54  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 O   ? C VAL 65 ? C VAL 57  ? 1_555 83.5  ? 
19 OE2 ? C GLU 60 ? C GLU 52  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 OE2 ? C GLU 70 ? C GLU 62  ? 1_555 102.7 ? 
20 O   ? C ASN 62 ? C ASN 54  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 OE2 ? C GLU 70 ? C GLU 62  ? 1_555 168.7 ? 
21 O   ? C VAL 65 ? C VAL 57  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 OE2 ? C GLU 70 ? C GLU 62  ? 1_555 92.0  ? 
22 OE2 ? C GLU 60 ? C GLU 52  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 O   ? I HOH .  ? C HOH 421 ? 1_555 69.4  ? 
23 O   ? C ASN 62 ? C ASN 54  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 O   ? I HOH .  ? C HOH 421 ? 1_555 82.7  ? 
24 O   ? C VAL 65 ? C VAL 57  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 O   ? I HOH .  ? C HOH 421 ? 1_555 73.1  ? 
25 OE2 ? C GLU 70 ? C GLU 62  ? 1_555 CA ? F CA . ? C CA 301 ? 1_555 O   ? I HOH .  ? C HOH 421 ? 1_555 86.1  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS A 15  ? CYS A 145 ? CYS A 7   ? 1_555 CYS A 137 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 33  ? CYS A 49  ? CYS A 25  ? 1_555 CYS A 41  ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 117 ? CYS A 218 ? CYS A 109 ? 1_555 CYS A 210 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 124 ? CYS A 191 ? CYS A 116 ? 1_555 CYS A 183 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS A 156 ? CYS A 170 ? CYS A 148 ? 1_555 CYS A 162 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS A 181 ? CYS A 205 A CYS A 173 ? 1_555 CYS A 197 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS A 181 ? CYS A 205 B CYS A 173 ? 1_555 CYS A 197 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS B 48  ? CYS B 94  ? CYS B 48  ? 1_555 CYS B 94  ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS B 143 ? CYS B 160 ? CYS B 143 ? 1_555 CYS B 160 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS C 15  ? CYS C 145 ? CYS C 7   ? 1_555 CYS C 137 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS C 33  ? CYS C 49  ? CYS C 25  ? 1_555 CYS C 41  ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS C 117 ? CYS C 218 ? CYS C 109 ? 1_555 CYS C 210 ? 1_555 SG SG . . . None 'Disulfide bridge' 
13 CYS C 124 ? CYS C 191 ? CYS C 116 ? 1_555 CYS C 183 ? 1_555 SG SG . . . None 'Disulfide bridge' 
14 CYS C 156 ? CYS C 170 ? CYS C 148 ? 1_555 CYS C 162 ? 1_555 SG SG . . . None 'Disulfide bridge' 
15 CYS C 181 ? CYS C 205 A CYS C 173 ? 1_555 CYS C 197 ? 1_555 SG SG . . . None 'Disulfide bridge' 
16 CYS C 181 ? CYS C 205 B CYS C 173 ? 1_555 CYS C 197 ? 1_555 SG SG . . . None 'Disulfide bridge' 
17 CYS D 48  ? CYS D 94  ? CYS D 48  ? 1_555 CYS D 94  ? 1_555 SG SG . . . None 'Disulfide bridge' 
18 CYS D 143 ? CYS D 160 ? CYS D 143 ? 1_555 CYS D 160 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
AA3 ? 7 ? 
AA4 ? 2 ? 
AA5 ? 6 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 7 ? 
AA9 ? 6 ? 
AB1 ? 7 ? 
AB2 ? 2 ? 
AB3 ? 6 ? 
AB4 ? 2 ? 
AB5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-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 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 6 7 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB3 5 6 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 13  ? THR A 14  ? TYR A 5   THR A 6   
AA1 2 GLN A 144 ? PRO A 149 ? GLN A 136 PRO A 141 
AA1 3 GLU A 123 ? GLY A 128 ? GLU A 115 GLY A 120 
AA1 4 PRO A 188 ? VAL A 190 ? PRO A 180 VAL A 182 
AA1 5 LEU A 195 ? TYR A 203 ? LEU A 187 TYR A 195 
AA1 6 GLY A 212 ? LYS A 216 ? GLY A 204 LYS A 208 
AA1 7 MET A 168 ? VAL A 171 ? MET A 160 VAL A 163 
AA2 1 TYR A 13  ? THR A 14  ? TYR A 5   THR A 6   
AA2 2 GLN A 144 ? PRO A 149 ? GLN A 136 PRO A 141 
AA2 3 GLU A 123 ? GLY A 128 ? GLU A 115 GLY A 120 
AA2 4 PRO A 188 ? VAL A 190 ? PRO A 180 VAL A 182 
AA2 5 LEU A 195 ? TYR A 203 ? LEU A 187 TYR A 195 
AA2 6 PHE B 28  ? GLY B 30  ? PHE B 28  GLY B 30  
AA3 1 GLN A 23  ? ASN A 27  ? GLN A 15  ASN A 19  
AA3 2 HIS A 31  ? ASN A 39  ? HIS A 23  ASN A 31  
AA3 3 TRP A 42  ? SER A 45  ? TRP A 34  SER A 37  
AA3 4 MET A 94  ? LEU A 98  ? MET A 86  LEU A 90  
AA3 5 GLN A 71  ? THR A 80  ? GLN A 63  THR A 72  
AA3 6 GLN A 55  ? LEU A 58  ? GLN A 47  LEU A 50  
AA3 7 GLN A 23  ? ASN A 27  ? GLN A 15  ASN A 19  
AA4 1 TYR B 22  ? SER B 26  ? TYR B 22  SER B 26  
AA4 2 VAL B 184 ? GLU B 188 ? VAL B 184 GLU B 188 
AA5 1 VAL B 36  ? GLY B 39  ? VAL B 36  GLY B 39  
AA5 2 GLY B 51  ? ARG B 54  ? GLY B 51  ARG B 54  
AA5 3 LYS B 171 ? LEU B 176 ? LYS B 171 LEU B 176 
AA5 4 ALA B 161 ? GLN B 168 ? ALA B 161 GLN B 168 
AA5 5 TYR B 138 ? CYS B 143 ? TYR B 138 CYS B 143 
AA5 6 TYR B 127 ? LYS B 132 ? TYR B 127 LYS B 132 
AA6 1 VAL B 66  ? PRO B 70  ? VAL B 66  PRO B 70  
AA6 2 LEU B 82  ? PHE B 86  ? LEU B 82  PHE B 86  
AA7 1 TRP B 100 ? VAL B 102 ? TRP B 100 VAL B 102 
AA7 2 LEU B 114 ? THR B 116 ? LEU B 114 THR B 116 
AA8 1 TYR C 13  ? THR C 14  ? TYR C 5   THR C 6   
AA8 2 GLN C 144 ? PRO C 149 ? GLN C 136 PRO C 141 
AA8 3 GLU C 123 ? GLY C 128 ? GLU C 115 GLY C 120 
AA8 4 PRO C 188 ? VAL C 190 ? PRO C 180 VAL C 182 
AA8 5 LEU C 195 ? TYR C 203 ? LEU C 187 TYR C 195 
AA8 6 GLY C 212 ? LYS C 216 ? GLY C 204 LYS C 208 
AA8 7 MET C 168 ? VAL C 171 ? MET C 160 VAL C 163 
AA9 1 TYR C 13  ? THR C 14  ? TYR C 5   THR C 6   
AA9 2 GLN C 144 ? PRO C 149 ? GLN C 136 PRO C 141 
AA9 3 GLU C 123 ? GLY C 128 ? GLU C 115 GLY C 120 
AA9 4 PRO C 188 ? VAL C 190 ? PRO C 180 VAL C 182 
AA9 5 LEU C 195 ? TYR C 203 ? LEU C 187 TYR C 195 
AA9 6 PHE D 28  ? GLY D 30  ? PHE D 28  GLY D 30  
AB1 1 GLN C 23  ? ASN C 27  ? GLN C 15  ASN C 19  
AB1 2 HIS C 31  ? ASN C 39  ? HIS C 23  ASN C 31  
AB1 3 TRP C 42  ? SER C 45  ? TRP C 34  SER C 37  
AB1 4 MET C 94  ? LEU C 98  ? MET C 86  LEU C 90  
AB1 5 GLN C 71  ? THR C 80  ? GLN C 63  THR C 72  
AB1 6 GLN C 55  ? LEU C 58  ? GLN C 47  LEU C 50  
AB1 7 GLN C 23  ? ASN C 27  ? GLN C 15  ASN C 19  
AB2 1 TYR D 22  ? SER D 26  ? TYR D 22  SER D 26  
AB2 2 VAL D 184 ? GLU D 188 ? VAL D 184 GLU D 188 
AB3 1 VAL D 36  ? GLY D 39  ? VAL D 36  GLY D 39  
AB3 2 GLY D 51  ? ARG D 54  ? GLY D 51  ARG D 54  
AB3 3 LYS D 171 ? LEU D 176 ? LYS D 171 LEU D 176 
AB3 4 ALA D 161 ? GLN D 168 ? ALA D 161 GLN D 168 
AB3 5 TYR D 138 ? TYR D 142 ? TYR D 138 TYR D 142 
AB3 6 PHE D 128 ? LYS D 132 ? PHE D 128 LYS D 132 
AB4 1 VAL D 66  ? PRO D 70  ? VAL D 66  PRO D 70  
AB4 2 LEU D 82  ? PHE D 86  ? LEU D 82  PHE D 86  
AB5 1 LYS D 101 ? GLY D 103 ? LYS D 101 GLY D 103 
AB5 2 LEU D 113 ? GLU D 115 ? LEU D 113 GLU D 115 
# 
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 TYR A 13  ? N TYR A 5   O CYS A 145 ? O CYS A 137 
AA1 2 3 O LEU A 146 ? O LEU A 138 N ILE A 126 ? N ILE A 118 
AA1 3 4 N LEU A 125 ? N LEU A 117 O VAL A 190 ? O VAL A 182 
AA1 4 5 N VAL A 189 ? N VAL A 181 O GLN A 196 ? O GLN A 188 
AA1 5 6 N TRP A 201 ? N TRP A 193 O VAL A 213 ? O VAL A 205 
AA1 6 7 O TYR A 214 ? O TYR A 206 N ILE A 169 ? N ILE A 161 
AA2 1 2 N TYR A 13  ? N TYR A 5   O CYS A 145 ? O CYS A 137 
AA2 2 3 O LEU A 146 ? O LEU A 138 N ILE A 126 ? N ILE A 118 
AA2 3 4 N LEU A 125 ? N LEU A 117 O VAL A 190 ? O VAL A 182 
AA2 4 5 N VAL A 189 ? N VAL A 181 O GLN A 196 ? O GLN A 188 
AA2 5 6 N GLY A 202 ? N GLY A 194 O TRP B 29  ? O TRP B 29  
AA3 1 2 N LEU A 26  ? N LEU A 18  O CYS A 33  ? O CYS A 25  
AA3 2 3 N SER A 36  ? N SER A 28  O VAL A 44  ? O VAL A 36  
AA3 3 4 N VAL A 43  ? N VAL A 35  O ILE A 96  ? O ILE A 88  
AA3 4 5 O LYS A 97  ? O LYS A 89  N ALA A 76  ? N ALA A 68  
AA3 5 6 O ILE A 73  ? O ILE A 65  N VAL A 56  ? N VAL A 48  
AA3 6 7 O GLN A 55  ? O GLN A 47  N ASN A 27  ? N ASN A 19  
AA4 1 2 N ILE B 25  ? N ILE B 25  O LEU B 185 ? O LEU B 185 
AA5 1 2 N GLY B 39  ? N GLY B 39  O GLY B 51  ? O GLY B 51  
AA5 2 3 N VAL B 52  ? N VAL B 52  O LEU B 174 ? O LEU B 174 
AA5 3 4 O ALA B 175 ? O ALA B 175 N GLY B 164 ? N GLY B 164 
AA5 4 5 O ALA B 161 ? O ALA B 161 N TYR B 142 ? N TYR B 142 
AA5 5 6 O LEU B 141 ? O LEU B 141 N LYS B 129 ? N LYS B 129 
AA6 1 2 N ARG B 67  ? N ARG B 67  O GLN B 85  ? O GLN B 85  
AA7 1 2 N LYS B 101 ? N LYS B 101 O GLU B 115 ? O GLU B 115 
AA8 1 2 N TYR C 13  ? N TYR C 5   O CYS C 145 ? O CYS C 137 
AA8 2 3 O ALA C 148 ? O ALA C 140 N CYS C 124 ? N CYS C 116 
AA8 3 4 N LEU C 125 ? N LEU C 117 O VAL C 190 ? O VAL C 182 
AA8 4 5 N VAL C 189 ? N VAL C 181 O GLN C 196 ? O GLN C 188 
AA8 5 6 N TRP C 201 ? N TRP C 193 O VAL C 213 ? O VAL C 205 
AA8 6 7 O TYR C 214 ? O TYR C 206 N ILE C 169 ? N ILE C 161 
AA9 1 2 N TYR C 13  ? N TYR C 5   O CYS C 145 ? O CYS C 137 
AA9 2 3 O ALA C 148 ? O ALA C 140 N CYS C 124 ? N CYS C 116 
AA9 3 4 N LEU C 125 ? N LEU C 117 O VAL C 190 ? O VAL C 182 
AA9 4 5 N VAL C 189 ? N VAL C 181 O GLN C 196 ? O GLN C 188 
AA9 5 6 N GLY C 202 ? N GLY C 194 O TRP D 29  ? O TRP D 29  
AB1 1 2 N LEU C 26  ? N LEU C 18  O CYS C 33  ? O CYS C 25  
AB1 2 3 N SER C 36  ? N SER C 28  O VAL C 44  ? O VAL C 36  
AB1 3 4 N VAL C 43  ? N VAL C 35  O ILE C 96  ? O ILE C 88  
AB1 4 5 O LEU C 95  ? O LEU C 87  N ILE C 79  ? N ILE C 71  
AB1 5 6 O GLN C 71  ? O GLN C 63  N LEU C 58  ? N LEU C 50  
AB1 6 7 O GLN C 55  ? O GLN C 47  N ASN C 27  ? N ASN C 19  
AB2 1 2 N ARG D 23  ? N ARG D 23  O GLN D 187 ? O GLN D 187 
AB3 1 2 N GLY D 39  ? N GLY D 39  O GLY D 51  ? O GLY D 51  
AB3 2 3 N ARG D 54  ? N ARG D 54  O ARG D 172 ? O ARG D 172 
AB3 3 4 O ALA D 175 ? O ALA D 175 N GLY D 164 ? N GLY D 164 
AB3 4 5 O ALA D 161 ? O ALA D 161 N TYR D 142 ? N TYR D 142 
AB3 5 6 O ASN D 139 ? O ASN D 139 N VAL D 131 ? N VAL D 131 
AB4 1 2 N ILE D 69  ? N ILE D 69  O ASN D 83  ? O ASN D 83  
AB5 1 2 N LYS D 101 ? N LYS D 101 O GLU D 115 ? O GLU D 115 
# 
_pdbx_entry_details.entry_id                   9CT1 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 454 ? ? O A HOH 460 ? ? 1.98 
2 1 O D HOH 223 ? ? O D HOH 228 ? ? 2.15 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB C CYS 173 ? ? SG C CYS 173 ? ? 1.709 1.812 -0.103 0.016 N 
2 1 CB D PRO 5   ? ? CG D PRO 5   ? ? 1.190 1.495 -0.305 0.050 N 
3 1 CG D PRO 5   ? ? CD D PRO 5   ? ? 1.053 1.502 -0.449 0.033 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA D PRO 5 ? ? CB D PRO 5 ? ? CG D PRO 5 ? ? 69.34  104.80 -35.46 1.90 N 
2 1 CB D PRO 5 ? ? CG D PRO 5 ? ? CD D PRO 5 ? ? 143.74 106.50 37.24  3.90 N 
3 1 N  D PRO 5 ? ? CD D PRO 5 ? ? CG D PRO 5 ? ? 69.84  103.20 -33.36 1.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 127 ? ? -124.78 -61.68  
2  1 SER A 130 ? ? -154.82 88.16   
3  1 SER A 177 ? ? -27.88  134.05  
4  1 LYS B 135 ? ? -107.35 -115.72 
5  1 ASN B 180 ? ? 65.58   67.94   
6  1 ASN C 31  ? ? -177.38 145.05  
7  1 HIS C 53  ? ? -137.27 -40.83  
8  1 ASN C 97  ? ? -154.46 -157.09 
9  1 SER C 127 ? ? -122.86 -56.49  
10 1 CYS C 173 ? ? -147.10 -153.42 
11 1 SER C 177 ? ? -28.21  132.61  
12 1 ALA C 198 ? ? 72.16   31.44   
13 1 ARG D 110 ? ? -153.41 -48.16  
14 1 LYS D 135 ? ? -117.95 -135.53 
15 1 ASN D 180 ? ? 62.40   63.24   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A PHE -7  ? A PHE 1   
2  1 Y 1 A PRO -6  ? A PRO 2   
3  1 Y 1 A THR -5  ? A THR 3   
4  1 Y 1 A ASP -4  ? A ASP 4   
5  1 Y 1 A ASP -3  ? A ASP 5   
6  1 Y 1 A ASP -2  ? A ASP 6   
7  1 Y 1 A ASP -1  ? A ASP 7   
8  1 Y 1 A LYS 0   ? A LYS 8   
9  1 Y 1 B GLU 1   ? B GLU 1   
10 1 Y 1 B SER 2   ? B SER 2   
11 1 Y 1 B PRO 3   ? B PRO 3   
12 1 Y 1 B ASN 104 ? B ASN 104 
13 1 Y 1 B ILE 105 ? B ILE 105 
14 1 Y 1 B ASN 106 ? B ASN 106 
15 1 Y 1 B ALA 107 ? B ALA 107 
16 1 Y 1 B HIS 108 ? B HIS 108 
17 1 Y 1 B LEU 109 ? B LEU 109 
18 1 Y 1 B THR 146 ? B THR 146 
19 1 Y 1 B ARG 147 ? B ARG 147 
20 1 Y 1 B HIS 148 ? B HIS 148 
21 1 Y 1 B PHE 149 ? B PHE 149 
22 1 Y 1 B LEU 150 ? B LEU 150 
23 1 Y 1 B CYS 151 ? B CYS 151 
24 1 Y 1 B PRO 152 ? B PRO 152 
25 1 Y 1 B PHE 153 ? B PHE 153 
26 1 Y 1 B CYS 154 ? B CYS 154 
27 1 Y 1 B ARG 155 ? B ARG 155 
28 1 Y 1 B ASP 156 ? B ASP 156 
29 1 Y 1 B ASP 157 ? B ASP 157 
30 1 Y 1 B HIS 190 ? B HIS 190 
31 1 Y 1 B HIS 191 ? B HIS 191 
32 1 Y 1 B HIS 192 ? B HIS 192 
33 1 Y 1 B HIS 193 ? B HIS 193 
34 1 Y 1 B HIS 194 ? B HIS 194 
35 1 Y 1 B HIS 195 ? B HIS 195 
36 1 Y 1 C PHE -7  ? C PHE 1   
37 1 Y 1 C PRO -6  ? C PRO 2   
38 1 Y 1 C THR -5  ? C THR 3   
39 1 Y 1 C ASP -4  ? C ASP 4   
40 1 Y 1 C ASP -3  ? C ASP 5   
41 1 Y 1 C ASP -2  ? C ASP 6   
42 1 Y 1 C ASP -1  ? C ASP 7   
43 1 Y 1 C LYS 0   ? C LYS 8   
44 1 Y 1 D GLU 1   ? D GLU 1   
45 1 Y 1 D SER 2   ? D SER 2   
46 1 Y 1 D PRO 3   ? D PRO 3   
47 1 Y 1 D ASN 104 ? D ASN 104 
48 1 Y 1 D ILE 105 ? D ILE 105 
49 1 Y 1 D ASN 106 ? D ASN 106 
50 1 Y 1 D ALA 107 ? D ALA 107 
51 1 Y 1 D HIS 108 ? D HIS 108 
52 1 Y 1 D THR 146 ? D THR 146 
53 1 Y 1 D ARG 147 ? D ARG 147 
54 1 Y 1 D HIS 148 ? D HIS 148 
55 1 Y 1 D PHE 149 ? D PHE 149 
56 1 Y 1 D LEU 150 ? D LEU 150 
57 1 Y 1 D CYS 151 ? D CYS 151 
58 1 Y 1 D PRO 152 ? D PRO 152 
59 1 Y 1 D PHE 153 ? D PHE 153 
60 1 Y 1 D CYS 154 ? D CYS 154 
61 1 Y 1 D ARG 155 ? D ARG 155 
62 1 Y 1 D ASP 156 ? D ASP 156 
63 1 Y 1 D ASP 157 ? D ASP 157 
64 1 Y 1 D ASN 158 ? D ASN 158 
65 1 Y 1 D HIS 190 ? D HIS 190 
66 1 Y 1 D HIS 191 ? D HIS 191 
67 1 Y 1 D HIS 192 ? D HIS 192 
68 1 Y 1 D HIS 193 ? D HIS 193 
69 1 Y 1 D HIS 194 ? D HIS 194 
70 1 Y 1 D HIS 195 ? D HIS 195 
# 
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  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                Mexico 
_pdbx_audit_support.grant_number           'DGAPA - PAPIIT - UNAM IN226523' 
_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 1AKS ? 
2 ? 'experimental model' PDB 9CSZ ? 
# 
_atom_sites.entry_id                    9CT1 
_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]   0.021164 
_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]   0.011643 
_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]   0.005375 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ILE A 1 9   ? -24.049 9.616   -43.314  1.00 21.80  ? 1   ILE A N   1 
ATOM   2    C  CA  . ILE A 1 9   ? -24.306 9.854   -44.738  1.00 23.06  ? 1   ILE A CA  1 
ATOM   3    C  C   . ILE A 1 9   ? -24.606 11.344  -44.964  1.00 23.60  ? 1   ILE A C   1 
ATOM   4    O  O   . ILE A 1 9   ? -25.649 11.855  -44.557  1.00 24.68  ? 1   ILE A O   1 
ATOM   5    C  CB  . ILE A 1 9   ? -25.461 8.959   -45.271  1.00 21.26  ? 1   ILE A CB  1 
ATOM   6    C  CG1 . ILE A 1 9   ? -25.230 7.501   -44.879  1.00 22.06  ? 1   ILE A CG1 1 
ATOM   7    C  CG2 . ILE A 1 9   ? -25.569 9.043   -46.784  1.00 22.30  ? 1   ILE A CG2 1 
ATOM   8    C  CD1 . ILE A 1 9   ? -24.049 6.862   -45.583  1.00 18.09  ? 1   ILE A CD1 1 
ATOM   9    N  N   . VAL A 1 10  ? -23.671 12.043  -45.574  1.00 19.54  ? 2   VAL A N   1 
ATOM   10   C  CA  . VAL A 1 10  ? -23.881 13.427  -45.965  1.00 24.97  ? 2   VAL A CA  1 
ATOM   11   C  C   . VAL A 1 10  ? -24.544 13.443  -47.327  1.00 21.78  ? 2   VAL A C   1 
ATOM   12   O  O   . VAL A 1 10  ? -24.120 12.732  -48.243  1.00 19.77  ? 2   VAL A O   1 
ATOM   13   C  CB  . VAL A 1 10  ? -22.555 14.201  -45.996  1.00 26.73  ? 2   VAL A CB  1 
ATOM   14   C  CG1 . VAL A 1 10  ? -22.797 15.627  -46.486  1.00 25.98  ? 2   VAL A CG1 1 
ATOM   15   C  CG2 . VAL A 1 10  ? -21.932 14.219  -44.613  1.00 27.80  ? 2   VAL A CG2 1 
ATOM   16   N  N   . GLY A 1 11  ? -25.595 14.238  -47.461  1.00 25.02  ? 3   GLY A N   1 
ATOM   17   C  CA  . GLY A 1 11  ? -26.190 14.412  -48.771  1.00 21.89  ? 3   GLY A CA  1 
ATOM   18   C  C   . GLY A 1 11  ? -26.897 13.187  -49.279  1.00 24.57  ? 3   GLY A C   1 
ATOM   19   O  O   . GLY A 1 11  ? -27.082 13.035  -50.495  1.00 20.78  ? 3   GLY A O   1 
ATOM   20   N  N   . GLY A 1 12  ? -27.265 12.292  -48.382  1.00 21.37  ? 4   GLY A N   1 
ATOM   21   C  CA  . GLY A 1 12  ? -28.073 11.150  -48.722  1.00 28.83  ? 4   GLY A CA  1 
ATOM   22   C  C   . GLY A 1 12  ? -29.547 11.453  -48.573  1.00 29.55  ? 4   GLY A C   1 
ATOM   23   O  O   . GLY A 1 12  ? -29.989 12.595  -48.715  1.00 28.24  ? 4   GLY A O   1 
ATOM   24   N  N   . TYR A 1 13  ? -30.319 10.409  -48.282  1.00 23.85  ? 5   TYR A N   1 
ATOM   25   C  CA  . TYR A 1 13  ? -31.753 10.530  -48.098  1.00 25.10  ? 5   TYR A CA  1 
ATOM   26   C  C   . TYR A 1 13  ? -32.174 9.514   -47.040  1.00 20.49  ? 5   TYR A C   1 
ATOM   27   O  O   . TYR A 1 13  ? -31.472 8.533   -46.788  1.00 24.19  ? 5   TYR A O   1 
ATOM   28   C  CB  . TYR A 1 13  ? -32.477 10.350  -49.457  1.00 27.35  ? 5   TYR A CB  1 
ATOM   29   C  CG  . TYR A 1 13  ? -32.275 8.992   -50.117  1.00 22.39  ? 5   TYR A CG  1 
ATOM   30   C  CD1 . TYR A 1 13  ? -31.159 8.746   -50.926  1.00 17.95  ? 5   TYR A CD1 1 
ATOM   31   C  CD2 . TYR A 1 13  ? -33.204 7.960   -49.942  1.00 19.88  ? 5   TYR A CD2 1 
ATOM   32   C  CE1 . TYR A 1 13  ? -30.961 7.486   -51.530  1.00 19.42  ? 5   TYR A CE1 1 
ATOM   33   C  CE2 . TYR A 1 13  ? -33.022 6.709   -50.541  1.00 17.33  ? 5   TYR A CE2 1 
ATOM   34   C  CZ  . TYR A 1 13  ? -31.892 6.478   -51.335  1.00 23.07  ? 5   TYR A CZ  1 
ATOM   35   O  OH  . TYR A 1 13  ? -31.699 5.237   -51.920  1.00 25.15  ? 5   TYR A OH  1 
ATOM   36   N  N   . THR A 1 14  ? -33.294 9.769   -46.387  1.00 18.82  ? 6   THR A N   1 
ATOM   37   C  CA  . THR A 1 14  ? -33.827 8.782   -45.454  1.00 21.87  ? 6   THR A CA  1 
ATOM   38   C  C   . THR A 1 14  ? -34.367 7.561   -46.192  1.00 23.40  ? 6   THR A C   1 
ATOM   39   O  O   . THR A 1 14  ? -35.304 7.666   -46.993  1.00 30.22  ? 6   THR A O   1 
ATOM   40   C  CB  . THR A 1 14  ? -34.924 9.397   -44.602  1.00 25.48  ? 6   THR A CB  1 
ATOM   41   O  OG1 . THR A 1 14  ? -34.380 10.513  -43.898  1.00 25.38  ? 6   THR A OG1 1 
ATOM   42   C  CG2 . THR A 1 14  ? -35.460 8.354   -43.612  1.00 16.75  ? 6   THR A CG2 1 
ATOM   43   N  N   . CYS A 1 15  ? -33.786 6.402   -45.903  1.00 24.54  ? 7   CYS A N   1 
ATOM   44   C  CA  . CYS A 1 15  ? -34.268 5.143   -46.448  1.00 22.20  ? 7   CYS A CA  1 
ATOM   45   C  C   . CYS A 1 15  ? -35.712 4.883   -46.038  1.00 30.60  ? 7   CYS A C   1 
ATOM   46   O  O   . CYS A 1 15  ? -36.111 5.159   -44.904  1.00 31.29  ? 7   CYS A O   1 
ATOM   47   C  CB  . CYS A 1 15  ? -33.398 3.985   -45.955  1.00 24.25  ? 7   CYS A CB  1 
ATOM   48   S  SG  . CYS A 1 15  ? -31.594 4.280   -45.976  1.00 43.48  ? 7   CYS A SG  1 
ATOM   49   N  N   . ALA A 1 16  ? -36.486 4.332   -46.969  1.00 24.70  ? 8   ALA A N   1 
ATOM   50   C  CA  . ALA A 1 16  ? -37.794 3.799   -46.631  1.00 33.47  ? 8   ALA A CA  1 
ATOM   51   C  C   . ALA A 1 16  ? -37.645 2.685   -45.595  1.00 37.27  ? 8   ALA A C   1 
ATOM   52   O  O   . ALA A 1 16  ? -36.774 1.818   -45.717  1.00 34.01  ? 8   ALA A O   1 
ATOM   53   C  CB  . ALA A 1 16  ? -38.487 3.278   -47.893  1.00 35.37  ? 8   ALA A CB  1 
ATOM   54   N  N   . ALA A 1 17  ? -38.493 2.721   -44.563  1.00 34.25  ? 9   ALA A N   1 
ATOM   55   C  CA  . ALA A 1 17  ? -38.352 1.800   -43.441  1.00 41.04  ? 9   ALA A CA  1 
ATOM   56   C  C   . ALA A 1 17  ? -38.275 0.361   -43.932  1.00 39.88  ? 9   ALA A C   1 
ATOM   57   O  O   . ALA A 1 17  ? -39.016 -0.045  -44.834  1.00 35.58  ? 9   ALA A O   1 
ATOM   58   C  CB  . ALA A 1 17  ? -39.515 1.970   -42.462  1.00 34.35  ? 9   ALA A CB  1 
ATOM   59   N  N   . ASN A 1 18  ? -37.324 -0.385  -43.376  1.00 37.88  ? 10  ASN A N   1 
ATOM   60   C  CA  . ASN A 1 18  ? -37.106 -1.800  -43.660  1.00 37.35  ? 10  ASN A CA  1 
ATOM   61   C  C   . ASN A 1 18  ? -36.744 -2.066  -45.120  1.00 43.95  ? 10  ASN A C   1 
ATOM   62   O  O   . ASN A 1 18  ? -36.802 -3.224  -45.566  1.00 35.92  ? 10  ASN A O   1 
ATOM   63   C  CB  . ASN A 1 18  ? -38.330 -2.648  -43.261  1.00 51.80  ? 10  ASN A CB  1 
ATOM   64   C  CG  . ASN A 1 18  ? -39.046 -2.134  -41.980  1.00 59.88  ? 10  ASN A CG  1 
ATOM   65   O  OD1 . ASN A 1 18  ? -38.415 -1.786  -40.953  1.00 37.02  ? 10  ASN A OD1 1 
ATOM   66   N  ND2 . ASN A 1 18  ? -40.379 -2.059  -42.063  1.00 56.45  ? 10  ASN A ND2 1 
ATOM   67   N  N   . SER A 1 19  ? -36.377 -1.034  -45.890  1.00 33.45  ? 11  SER A N   1 
ATOM   68   C  CA  . SER A 1 19  ? -35.853 -1.292  -47.222  1.00 29.12  ? 11  SER A CA  1 
ATOM   69   C  C   . SER A 1 19  ? -34.389 -1.709  -47.195  1.00 30.47  ? 11  SER A C   1 
ATOM   70   O  O   . SER A 1 19  ? -33.879 -2.175  -48.213  1.00 28.38  ? 11  SER A O   1 
ATOM   71   C  CB  . SER A 1 19  ? -36.017 -0.071  -48.125  1.00 24.53  ? 11  SER A CB  1 
ATOM   72   O  OG  . SER A 1 19  ? -35.384 1.055   -47.560  1.00 37.03  ? 11  SER A OG  1 
ATOM   73   N  N   . ILE A 1 20  ? -33.706 -1.568  -46.064  1.00 29.90  ? 12  ILE A N   1 
ATOM   74   C  CA  . ILE A 1 20  ? -32.344 -2.076  -45.929  1.00 24.82  ? 12  ILE A CA  1 
ATOM   75   C  C   . ILE A 1 20  ? -32.336 -3.091  -44.791  1.00 25.16  ? 12  ILE A C   1 
ATOM   76   O  O   . ILE A 1 20  ? -31.721 -2.837  -43.746  1.00 30.99  ? 12  ILE A O   1 
ATOM   77   C  CB  . ILE A 1 20  ? -31.329 -0.952  -45.650  1.00 25.78  ? 12  ILE A CB  1 
ATOM   78   C  CG1 . ILE A 1 20  ? -31.652 0.351   -46.386  1.00 23.32  ? 12  ILE A CG1 1 
ATOM   79   C  CG2 . ILE A 1 20  ? -29.939 -1.374  -46.063  1.00 27.67  ? 12  ILE A CG2 1 
ATOM   80   C  CD1 . ILE A 1 20  ? -31.759 0.228   -47.838  1.00 29.15  ? 12  ILE A CD1 1 
ATOM   81   N  N   . PRO A 1 21  ? -32.974 -4.254  -44.941  1.00 23.51  ? 13  PRO A N   1 
ATOM   82   C  CA  . PRO A 1 21  ? -33.130 -5.164  -43.789  1.00 22.75  ? 13  PRO A CA  1 
ATOM   83   C  C   . PRO A 1 21  ? -31.862 -5.887  -43.360  1.00 23.69  ? 13  PRO A C   1 
ATOM   84   O  O   . PRO A 1 21  ? -31.867 -6.529  -42.299  1.00 25.67  ? 13  PRO A O   1 
ATOM   85   C  CB  . PRO A 1 21  ? -34.192 -6.157  -44.281  1.00 30.18  ? 13  PRO A CB  1 
ATOM   86   C  CG  . PRO A 1 21  ? -33.964 -6.197  -45.767  1.00 28.56  ? 13  PRO A CG  1 
ATOM   87   C  CD  . PRO A 1 21  ? -33.658 -4.766  -46.143  1.00 28.49  ? 13  PRO A CD  1 
ATOM   88   N  N   . TYR A 1 22  ? -30.788 -5.835  -44.137  1.00 24.98  ? 14  TYR A N   1 
ATOM   89   C  CA  . TYR A 1 22  ? -29.523 -6.417  -43.703  1.00 22.71  ? 14  TYR A CA  1 
ATOM   90   C  C   . TYR A 1 22  ? -28.690 -5.458  -42.865  1.00 24.41  ? 14  TYR A C   1 
ATOM   91   O  O   . TYR A 1 22  ? -27.621 -5.854  -42.383  1.00 25.61  ? 14  TYR A O   1 
ATOM   92   C  CB  . TYR A 1 22  ? -28.703 -6.856  -44.919  1.00 18.75  ? 14  TYR A CB  1 
ATOM   93   C  CG  . TYR A 1 22  ? -28.582 -5.752  -45.947  1.00 20.87  ? 14  TYR A CG  1 
ATOM   94   C  CD1 . TYR A 1 22  ? -27.716 -4.676  -45.750  1.00 20.14  ? 14  TYR A CD1 1 
ATOM   95   C  CD2 . TYR A 1 22  ? -29.328 -5.784  -47.119  1.00 20.00  ? 14  TYR A CD2 1 
ATOM   96   C  CE1 . TYR A 1 22  ? -27.601 -3.641  -46.703  1.00 21.93  ? 14  TYR A CE1 1 
ATOM   97   C  CE2 . TYR A 1 22  ? -29.234 -4.752  -48.067  1.00 27.06  ? 14  TYR A CE2 1 
ATOM   98   C  CZ  . TYR A 1 22  ? -28.384 -3.683  -47.850  1.00 21.73  ? 14  TYR A CZ  1 
ATOM   99   O  OH  . TYR A 1 22  ? -28.318 -2.677  -48.784  1.00 24.32  ? 14  TYR A OH  1 
ATOM   100  N  N   . GLN A 1 23  ? -29.124 -4.205  -42.726  1.00 18.74  ? 15  GLN A N   1 
ATOM   101  C  CA  . GLN A 1 23  ? -28.357 -3.218  -41.988  1.00 20.26  ? 15  GLN A CA  1 
ATOM   102  C  C   . GLN A 1 23  ? -28.517 -3.452  -40.501  1.00 14.82  ? 15  GLN A C   1 
ATOM   103  O  O   . GLN A 1 23  ? -29.609 -3.748  -40.022  1.00 21.91  ? 15  GLN A O   1 
ATOM   104  C  CB  . GLN A 1 23  ? -28.812 -1.809  -42.347  1.00 18.02  ? 15  GLN A CB  1 
ATOM   105  C  CG  . GLN A 1 23  ? -28.287 -0.754  -41.420  1.00 26.05  ? 15  GLN A CG  1 
ATOM   106  C  CD  . GLN A 1 23  ? -26.986 -0.132  -41.888  1.00 24.24  ? 15  GLN A CD  1 
ATOM   107  O  OE1 . GLN A 1 23  ? -26.856 0.283   -43.044  1.00 21.91  ? 15  GLN A OE1 1 
ATOM   108  N  NE2 . GLN A 1 23  ? -26.011 -0.052  -40.982  1.00 18.44  ? 15  GLN A NE2 1 
ATOM   109  N  N   . VAL A 1 24  ? -27.415 -3.355  -39.769  1.00 22.82  ? 16  VAL A N   1 
ATOM   110  C  CA  . VAL A 1 24  ? -27.448 -3.499  -38.321  1.00 19.82  ? 16  VAL A CA  1 
ATOM   111  C  C   . VAL A 1 24  ? -26.774 -2.293  -37.670  1.00 21.51  ? 16  VAL A C   1 
ATOM   112  O  O   . VAL A 1 24  ? -25.975 -1.577  -38.282  1.00 17.02  ? 16  VAL A O   1 
ATOM   113  C  CB  . VAL A 1 24  ? -26.798 -4.820  -37.849  1.00 21.54  ? 16  VAL A CB  1 
ATOM   114  C  CG1 . VAL A 1 24  ? -27.271 -5.995  -38.708  1.00 24.59  ? 16  VAL A CG1 1 
ATOM   115  C  CG2 . VAL A 1 24  ? -25.288 -4.723  -37.920  1.00 25.24  ? 16  VAL A CG2 1 
ATOM   116  N  N   . SER A 1 25  ? -27.136 -2.060  -36.416  1.00 18.70  ? 17  SER A N   1 
ATOM   117  C  CA  . SER A 1 25  ? -26.463 -1.081  -35.581  1.00 21.62  ? 17  SER A CA  1 
ATOM   118  C  C   . SER A 1 25  ? -25.690 -1.842  -34.508  1.00 18.20  ? 17  SER A C   1 
ATOM   119  O  O   . SER A 1 25  ? -26.249 -2.723  -33.851  1.00 20.69  ? 17  SER A O   1 
ATOM   120  C  CB  . SER A 1 25  ? -27.481 -0.107  -34.968  1.00 23.60  ? 17  SER A CB  1 
ATOM   121  O  OG  . SER A 1 25  ? -26.887 0.798   -34.050  1.00 19.81  ? 17  SER A OG  1 
ATOM   122  N  N   . LEU A 1 26  ? -24.403 -1.534  -34.358  1.00 20.18  ? 18  LEU A N   1 
ATOM   123  C  CA  . LEU A 1 26  ? -23.612 -2.046  -33.244  1.00 19.38  ? 18  LEU A CA  1 
ATOM   124  C  C   . LEU A 1 26  ? -23.692 -1.060  -32.084  1.00 19.96  ? 18  LEU A C   1 
ATOM   125  O  O   . LEU A 1 26  ? -23.433 0.135   -32.258  1.00 20.37  ? 18  LEU A O   1 
ATOM   126  C  CB  . LEU A 1 26  ? -22.154 -2.273  -33.650  1.00 12.15  ? 18  LEU A CB  1 
ATOM   127  C  CG  . LEU A 1 26  ? -21.976 -3.202  -34.858  1.00 18.76  ? 18  LEU A CG  1 
ATOM   128  C  CD1 . LEU A 1 26  ? -20.515 -3.567  -35.091  1.00 16.50  ? 18  LEU A CD1 1 
ATOM   129  C  CD2 . LEU A 1 26  ? -22.840 -4.434  -34.724  1.00 16.48  ? 18  LEU A CD2 1 
ATOM   130  N  N   . ASN A 1 27  ? -24.038 -1.568  -30.906  1.00 19.81  ? 19  ASN A N   1 
ATOM   131  C  CA  . ASN A 1 27  ? -24.374 -0.749  -29.749  1.00 20.95  ? 19  ASN A CA  1 
ATOM   132  C  C   . ASN A 1 27  ? -23.465 -1.124  -28.582  1.00 21.44  ? 19  ASN A C   1 
ATOM   133  O  O   . ASN A 1 27  ? -23.303 -2.308  -28.271  1.00 23.88  ? 19  ASN A O   1 
ATOM   134  C  CB  . ASN A 1 27  ? -25.854 -0.936  -29.366  1.00 17.97  ? 19  ASN A CB  1 
ATOM   135  C  CG  . ASN A 1 27  ? -26.362 0.153   -28.423  1.00 25.03  ? 19  ASN A CG  1 
ATOM   136  O  OD1 . ASN A 1 27  ? -26.131 0.098   -27.215  1.00 19.95  ? 19  ASN A OD1 1 
ATOM   137  N  ND2 . ASN A 1 27  ? -27.074 1.142   -28.978  1.00 19.87  ? 19  ASN A ND2 1 
ATOM   138  N  N   . SER A 1 28  ? -22.875 -0.121  -27.940  1.00 24.46  ? 20  SER A N   1 
ATOM   139  C  CA  . SER A 1 28  ? -22.061 -0.306  -26.742  1.00 24.23  ? 20  SER A CA  1 
ATOM   140  C  C   . SER A 1 28  ? -22.568 0.608   -25.645  1.00 25.92  ? 20  SER A C   1 
ATOM   141  O  O   . SER A 1 28  ? -21.793 1.251   -24.931  1.00 21.52  ? 20  SER A O   1 
ATOM   142  C  CB  . SER A 1 28  ? -20.587 -0.035  -27.024  1.00 23.28  ? 20  SER A CB  1 
ATOM   143  O  OG  . SER A 1 28  ? -20.431 1.253   -27.627  1.00 25.63  ? 20  SER A OG  1 
ATOM   144  N  N   . GLY A 1 29  ? -23.890 0.663   -25.496  1.00 23.81  ? 21  GLY A N   1 
ATOM   145  C  CA  . GLY A 1 29  ? -24.564 1.690   -24.762  1.00 18.53  ? 21  GLY A CA  1 
ATOM   146  C  C   . GLY A 1 29  ? -25.145 2.736   -25.679  1.00 23.42  ? 21  GLY A C   1 
ATOM   147  O  O   . GLY A 1 29  ? -26.184 3.307   -25.378  1.00 29.04  ? 21  GLY A O   1 
ATOM   148  N  N   . SER A 1 30  ? -24.506 2.951   -26.818  1.00 26.68  ? 22  SER A N   1 
ATOM   149  C  CA  . SER A 1 30  ? -24.975 3.869   -27.832  1.00 20.39  ? 22  SER A CA  1 
ATOM   150  C  C   . SER A 1 30  ? -24.621 3.294   -29.199  1.00 22.75  ? 22  SER A C   1 
ATOM   151  O  O   . SER A 1 30  ? -23.733 2.437   -29.327  1.00 20.50  ? 22  SER A O   1 
ATOM   152  C  CB  . SER A 1 30  ? -24.358 5.258   -27.632  1.00 24.10  ? 22  SER A CB  1 
ATOM   153  O  OG  . SER A 1 30  ? -25.005 6.194   -28.461  1.00 48.41  ? 22  SER A OG  1 
ATOM   154  N  N   . HIS A 1 31  ? -25.344 3.745   -30.223  1.00 22.10  ? 23  HIS A N   1 
ATOM   155  C  CA  . HIS A 1 31  ? -24.960 3.410   -31.589  1.00 21.08  ? 23  HIS A CA  1 
ATOM   156  C  C   . HIS A 1 31  ? -23.533 3.876   -31.858  1.00 22.50  ? 23  HIS A C   1 
ATOM   157  O  O   . HIS A 1 31  ? -23.196 5.035   -31.604  1.00 19.91  ? 23  HIS A O   1 
ATOM   158  C  CB  . HIS A 1 31  ? -25.890 4.068   -32.606  1.00 21.35  ? 23  HIS A CB  1 
ATOM   159  C  CG  . HIS A 1 31  ? -25.337 4.025   -33.999  1.00 31.28  ? 23  HIS A CG  1 
ATOM   160  N  ND1 . HIS A 1 31  ? -25.445 2.908   -34.809  1.00 27.32  ? 23  HIS A ND1 1 
ATOM   161  C  CD2 . HIS A 1 31  ? -24.591 4.920   -34.690  1.00 19.10  ? 23  HIS A CD2 1 
ATOM   162  C  CE1 . HIS A 1 31  ? -24.821 3.135   -35.952  1.00 23.66  ? 23  HIS A CE1 1 
ATOM   163  N  NE2 . HIS A 1 31  ? -24.297 4.349   -35.906  1.00 29.89  ? 23  HIS A NE2 1 
ATOM   164  N  N   . PHE A 1 32  ? -22.688 2.987   -32.390  1.00 24.71  ? 24  PHE A N   1 
ATOM   165  C  CA  . PHE A 1 32  ? -21.321 3.419   -32.709  1.00 26.24  ? 24  PHE A CA  1 
ATOM   166  C  C   . PHE A 1 32  ? -20.781 2.924   -34.048  1.00 19.30  ? 24  PHE A C   1 
ATOM   167  O  O   . PHE A 1 32  ? -19.810 3.514   -34.538  1.00 16.77  ? 24  PHE A O   1 
ATOM   168  C  CB  . PHE A 1 32  ? -20.340 3.026   -31.572  1.00 17.42  ? 24  PHE A CB  1 
ATOM   169  C  CG  . PHE A 1 32  ? -19.991 1.562   -31.538  1.00 23.52  ? 24  PHE A CG  1 
ATOM   170  C  CD1 . PHE A 1 32  ? -18.931 1.059   -32.279  1.00 22.56  ? 24  PHE A CD1 1 
ATOM   171  C  CD2 . PHE A 1 32  ? -20.733 0.684   -30.770  1.00 26.58  ? 24  PHE A CD2 1 
ATOM   172  C  CE1 . PHE A 1 32  ? -18.624 -0.281  -32.255  1.00 18.72  ? 24  PHE A CE1 1 
ATOM   173  C  CE2 . PHE A 1 32  ? -20.427 -0.658  -30.743  1.00 18.64  ? 24  PHE A CE2 1 
ATOM   174  C  CZ  . PHE A 1 32  ? -19.368 -1.136  -31.487  1.00 23.49  ? 24  PHE A CZ  1 
ATOM   175  N  N   . CYS A 1 33  ? -21.361 1.890   -34.663  1.00 13.95  ? 25  CYS A N   1 
ATOM   176  C  CA  . CYS A 1 33  ? -20.903 1.338   -35.939  1.00 21.73  ? 25  CYS A CA  1 
ATOM   177  C  C   . CYS A 1 33  ? -22.071 0.648   -36.604  1.00 23.04  ? 25  CYS A C   1 
ATOM   178  O  O   . CYS A 1 33  ? -22.954 0.119   -35.924  1.00 24.68  ? 25  CYS A O   1 
ATOM   179  C  CB  . CYS A 1 33  ? -19.760 0.301   -35.806  1.00 13.00  ? 25  CYS A CB  1 
ATOM   180  S  SG  . CYS A 1 33  ? -18.117 1.055   -35.784  1.00 41.96  ? 25  CYS A SG  1 
ATOM   181  N  N   . GLY A 1 34  ? -22.034 0.614   -37.956  1.00 25.64  ? 26  GLY A N   1 
ATOM   182  C  CA  . GLY A 1 34  ? -22.930 -0.232  -38.723  1.00 17.58  ? 26  GLY A CA  1 
ATOM   183  C  C   . GLY A 1 34  ? -22.336 -1.615  -39.013  1.00 21.33  ? 26  GLY A C   1 
ATOM   184  O  O   . GLY A 1 34  ? -21.175 -1.920  -38.750  1.00 21.27  ? 26  GLY A O   1 
ATOM   185  N  N   . GLY A 1 35  ? -23.175 -2.487  -39.557  1.00 22.86  ? 27  GLY A N   1 
ATOM   186  C  CA  . GLY A 1 35  ? -22.696 -3.780  -40.001  1.00 15.94  ? 27  GLY A CA  1 
ATOM   187  C  C   . GLY A 1 35  ? -23.728 -4.347  -40.943  1.00 17.26  ? 27  GLY A C   1 
ATOM   188  O  O   . GLY A 1 35  ? -24.738 -3.709  -41.248  1.00 16.43  ? 27  GLY A O   1 
ATOM   189  N  N   . SER A 1 36  ? -23.468 -5.566  -41.400  1.00 21.47  ? 28  SER A N   1 
ATOM   190  C  CA  . SER A 1 36  ? -24.334 -6.217  -42.371  1.00 21.69  ? 28  SER A CA  1 
ATOM   191  C  C   . SER A 1 36  ? -24.556 -7.665  -41.961  1.00 27.70  ? 28  SER A C   1 
ATOM   192  O  O   . SER A 1 36  ? -23.626 -8.347  -41.518  1.00 26.05  ? 28  SER A O   1 
ATOM   193  C  CB  . SER A 1 36  ? -23.738 -6.147  -43.782  1.00 24.80  ? 28  SER A CB  1 
ATOM   194  O  OG  . SER A 1 36  ? -23.101 -4.901  -44.004  1.00 26.66  ? 28  SER A OG  1 
ATOM   195  N  N   . LEU A 1 37  ? -25.795 -8.124  -42.111  1.00 25.82  ? 29  LEU A N   1 
ATOM   196  C  CA  . LEU A 1 37  ? -26.181 -9.482  -41.747  1.00 31.01  ? 29  LEU A CA  1 
ATOM   197  C  C   . LEU A 1 37  ? -25.943 -10.407 -42.945  1.00 23.93  ? 29  LEU A C   1 
ATOM   198  O  O   . LEU A 1 37  ? -26.613 -10.291 -43.979  1.00 24.36  ? 29  LEU A O   1 
ATOM   199  C  CB  . LEU A 1 37  ? -27.640 -9.499  -41.280  1.00 25.55  ? 29  LEU A CB  1 
ATOM   200  C  CG  . LEU A 1 37  ? -28.164 -10.806 -40.678  1.00 28.38  ? 29  LEU A CG  1 
ATOM   201  C  CD1 . LEU A 1 37  ? -27.459 -11.087 -39.352  1.00 20.24  ? 29  LEU A CD1 1 
ATOM   202  C  CD2 . LEU A 1 37  ? -29.705 -10.772 -40.547  1.00 18.82  ? 29  LEU A CD2 1 
ATOM   203  N  N   . ILE A 1 38  ? -24.990 -11.332 -42.812  1.00 25.46  ? 30  ILE A N   1 
ATOM   204  C  CA  . ILE A 1 38  ? -24.651 -12.160 -43.962  1.00 20.85  ? 30  ILE A CA  1 
ATOM   205  C  C   . ILE A 1 38  ? -25.211 -13.570 -43.814  1.00 26.49  ? 30  ILE A C   1 
ATOM   206  O  O   . ILE A 1 38  ? -25.544 -14.208 -44.816  1.00 38.54  ? 30  ILE A O   1 
ATOM   207  C  CB  . ILE A 1 38  ? -23.137 -12.158 -44.217  1.00 24.18  ? 30  ILE A CB  1 
ATOM   208  C  CG1 . ILE A 1 38  ? -22.373 -12.412 -42.930  1.00 23.87  ? 30  ILE A CG1 1 
ATOM   209  C  CG2 . ILE A 1 38  ? -22.709 -10.832 -44.815  1.00 20.61  ? 30  ILE A CG2 1 
ATOM   210  C  CD1 . ILE A 1 38  ? -21.007 -12.960 -43.192  1.00 21.31  ? 30  ILE A CD1 1 
ATOM   211  N  N   . ASN A 1 39  ? -25.329 -14.072 -42.581  1.00 28.61  ? 31  ASN A N   1 
ATOM   212  C  CA  . ASN A 1 39  ? -26.232 -15.185 -42.294  1.00 25.96  ? 31  ASN A CA  1 
ATOM   213  C  C   . ASN A 1 39  ? -26.877 -14.929 -40.933  1.00 32.53  ? 31  ASN A C   1 
ATOM   214  O  O   . ASN A 1 39  ? -26.575 -13.942 -40.253  1.00 33.96  ? 31  ASN A O   1 
ATOM   215  C  CB  . ASN A 1 39  ? -25.550 -16.577 -42.386  1.00 18.42  ? 31  ASN A CB  1 
ATOM   216  C  CG  . ASN A 1 39  ? -24.574 -16.881 -41.239  1.00 34.58  ? 31  ASN A CG  1 
ATOM   217  O  OD1 . ASN A 1 39  ? -24.893 -16.747 -40.056  1.00 41.39  ? 31  ASN A OD1 1 
ATOM   218  N  ND2 . ASN A 1 39  ? -23.400 -17.372 -41.599  1.00 41.54  ? 31  ASN A ND2 1 
ATOM   219  N  N   . SER A 1 40  ? -27.765 -15.838 -40.529  1.00 25.12  ? 32  SER A N   1 
ATOM   220  C  CA  . SER A 1 40  ? -28.631 -15.578 -39.388  1.00 29.48  ? 32  SER A CA  1 
ATOM   221  C  C   . SER A 1 40  ? -27.862 -15.429 -38.090  1.00 29.94  ? 32  SER A C   1 
ATOM   222  O  O   . SER A 1 40  ? -28.434 -14.953 -37.105  1.00 29.05  ? 32  SER A O   1 
ATOM   223  C  CB  . SER A 1 40  ? -29.659 -16.699 -39.242  1.00 33.91  ? 32  SER A CB  1 
ATOM   224  O  OG  . SER A 1 40  ? -29.053 -17.868 -38.724  1.00 38.86  ? 32  SER A OG  1 
ATOM   225  N  N   . GLN A 1 41  ? -26.589 -15.832 -38.053  1.00 25.67  ? 33  GLN A N   1 
ATOM   226  C  CA  . GLN A 1 41  ? -25.808 -15.767 -36.822  1.00 30.59  ? 33  GLN A CA  1 
ATOM   227  C  C   . GLN A 1 41  ? -24.546 -14.933 -36.944  1.00 23.06  ? 33  GLN A C   1 
ATOM   228  O  O   . GLN A 1 41  ? -23.800 -14.821 -35.961  1.00 24.46  ? 33  GLN A O   1 
ATOM   229  C  CB  . GLN A 1 41  ? -25.429 -17.179 -36.333  1.00 27.26  ? 33  GLN A CB  1 
ATOM   230  C  CG  . GLN A 1 41  ? -25.938 -17.477 -34.933  1.00 37.13  ? 33  GLN A CG  1 
ATOM   231  C  CD  . GLN A 1 41  ? -25.705 -18.908 -34.484  1.00 49.49  ? 33  GLN A CD  1 
ATOM   232  O  OE1 . GLN A 1 41  ? -25.367 -19.786 -35.284  1.00 37.89  ? 33  GLN A OE1 1 
ATOM   233  N  NE2 . GLN A 1 41  ? -25.861 -19.142 -33.180  1.00 58.69  ? 33  GLN A NE2 1 
ATOM   234  N  N   . TRP A 1 42  ? -24.281 -14.351 -38.105  1.00 21.28  ? 34  TRP A N   1 
ATOM   235  C  CA  . TRP A 1 42  ? -23.033 -13.641 -38.338  1.00 24.47  ? 34  TRP A CA  1 
ATOM   236  C  C   . TRP A 1 42  ? -23.282 -12.292 -38.999  1.00 25.32  ? 34  TRP A C   1 
ATOM   237  O  O   . TRP A 1 42  ? -24.092 -12.162 -39.930  1.00 24.22  ? 34  TRP A O   1 
ATOM   238  C  CB  . TRP A 1 42  ? -22.077 -14.466 -39.205  1.00 27.97  ? 34  TRP A CB  1 
ATOM   239  C  CG  . TRP A 1 42  ? -21.525 -15.643 -38.498  1.00 31.51  ? 34  TRP A CG  1 
ATOM   240  C  CD1 . TRP A 1 42  ? -22.083 -16.891 -38.416  1.00 26.93  ? 34  TRP A CD1 1 
ATOM   241  C  CD2 . TRP A 1 42  ? -20.294 -15.705 -37.779  1.00 26.69  ? 34  TRP A CD2 1 
ATOM   242  N  NE1 . TRP A 1 42  ? -21.276 -17.721 -37.672  1.00 29.11  ? 34  TRP A NE1 1 
ATOM   243  C  CE2 . TRP A 1 42  ? -20.169 -17.021 -37.273  1.00 32.34  ? 34  TRP A CE2 1 
ATOM   244  C  CE3 . TRP A 1 42  ? -19.289 -14.779 -37.504  1.00 23.73  ? 34  TRP A CE3 1 
ATOM   245  C  CZ2 . TRP A 1 42  ? -19.069 -17.433 -36.514  1.00 33.80  ? 34  TRP A CZ2 1 
ATOM   246  C  CZ3 . TRP A 1 42  ? -18.199 -15.184 -36.756  1.00 31.01  ? 34  TRP A CZ3 1 
ATOM   247  C  CH2 . TRP A 1 42  ? -18.096 -16.502 -36.264  1.00 30.52  ? 34  TRP A CH2 1 
ATOM   248  N  N   . VAL A 1 43  ? -22.553 -11.299 -38.515  1.00 23.72  ? 35  VAL A N   1 
ATOM   249  C  CA  . VAL A 1 43  ? -22.539 -9.962  -39.072  1.00 20.18  ? 35  VAL A CA  1 
ATOM   250  C  C   . VAL A 1 43  ? -21.117 -9.663  -39.516  1.00 24.71  ? 35  VAL A C   1 
ATOM   251  O  O   . VAL A 1 43  ? -20.154 -10.043 -38.844  1.00 32.10  ? 35  VAL A O   1 
ATOM   252  C  CB  . VAL A 1 43  ? -23.035 -8.927  -38.036  1.00 27.55  ? 35  VAL A CB  1 
ATOM   253  C  CG1 . VAL A 1 43  ? -22.844 -7.463  -38.554  1.00 25.44  ? 35  VAL A CG1 1 
ATOM   254  C  CG2 . VAL A 1 43  ? -24.504 -9.194  -37.666  1.00 16.44  ? 35  VAL A CG2 1 
ATOM   255  N  N   . VAL A 1 44  ? -20.979 -8.980  -40.626  1.00 24.69  ? 36  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 44  ? -19.681 -8.484  -41.053  1.00 22.95  ? 36  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 44  ? -19.628 -6.986  -40.805  1.00 21.98  ? 36  VAL A C   1 
ATOM   258  O  O   . VAL A 1 44  ? -20.618 -6.275  -41.017  1.00 26.52  ? 36  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 44  ? -19.451 -8.804  -42.534  1.00 26.66  ? 36  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 44  ? -20.620 -8.298  -43.331  1.00 30.71  ? 36  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 44  ? -18.128 -8.222  -43.012  1.00 27.87  ? 36  VAL A CG2 1 
ATOM   262  N  N   . SER A 1 45  ? -18.472 -6.497  -40.376  1.00 19.04  ? 37  SER A N   1 
ATOM   263  C  CA  . SER A 1 45  ? -18.301 -5.086  -40.058  1.00 23.51  ? 37  SER A CA  1 
ATOM   264  C  C   . SER A 1 45  ? -16.830 -4.737  -40.278  1.00 24.39  ? 37  SER A C   1 
ATOM   265  O  O   . SER A 1 45  ? -16.082 -5.507  -40.892  1.00 18.89  ? 37  SER A O   1 
ATOM   266  C  CB  . SER A 1 45  ? -18.800 -4.816  -38.629  1.00 21.51  ? 37  SER A CB  1 
ATOM   267  O  OG  . SER A 1 45  ? -18.758 -3.438  -38.321  1.00 17.20  ? 37  SER A OG  1 
ATOM   268  N  N   . ALA A 1 46  ? -16.406 -3.572  -39.786  1.00 15.92  ? 38  ALA A N   1 
ATOM   269  C  CA  . ALA A 1 46  ? -15.012 -3.161  -39.904  1.00 22.64  ? 38  ALA A CA  1 
ATOM   270  C  C   . ALA A 1 46  ? -14.240 -3.489  -38.626  1.00 27.77  ? 38  ALA A C   1 
ATOM   271  O  O   . ALA A 1 46  ? -14.783 -3.429  -37.517  1.00 22.48  ? 38  ALA A O   1 
ATOM   272  C  CB  . ALA A 1 46  ? -14.892 -1.667  -40.221  1.00 20.45  ? 38  ALA A CB  1 
ATOM   273  N  N   . ALA A 1 47  ? -12.959 -3.830  -38.787  1.00 21.69  ? 39  ALA A N   1 
ATOM   274  C  CA  . ALA A 1 47  ? -12.153 -4.196  -37.627  1.00 19.04  ? 39  ALA A CA  1 
ATOM   275  C  C   . ALA A 1 47  ? -11.942 -3.006  -36.703  1.00 23.25  ? 39  ALA A C   1 
ATOM   276  O  O   . ALA A 1 47  ? -11.906 -3.173  -35.483  1.00 27.16  ? 39  ALA A O   1 
ATOM   277  C  CB  . ALA A 1 47  ? -10.810 -4.771  -38.067  1.00 17.09  ? 39  ALA A CB  1 
ATOM   278  N  N   . HIS A 1 48  ? -11.823 -1.790  -37.257  1.00 16.37  ? 40  HIS A N   1 
ATOM   279  C  CA  . HIS A 1 48  ? -11.648 -0.633  -36.394  1.00 24.16  ? 40  HIS A CA  1 
ATOM   280  C  C   . HIS A 1 48  ? -12.859 -0.385  -35.497  1.00 27.65  ? 40  HIS A C   1 
ATOM   281  O  O   . HIS A 1 48  ? -12.770 0.445   -34.583  1.00 21.78  ? 40  HIS A O   1 
ATOM   282  C  CB  . HIS A 1 48  ? -11.305 0.620   -37.222  1.00 23.80  ? 40  HIS A CB  1 
ATOM   283  C  CG  . HIS A 1 48  ? -12.474 1.267   -37.901  1.00 20.92  ? 40  HIS A CG  1 
ATOM   284  N  ND1 . HIS A 1 48  ? -12.781 1.045   -39.227  1.00 21.72  ? 40  HIS A ND1 1 
ATOM   285  C  CD2 . HIS A 1 48  ? -13.380 2.172   -37.456  1.00 24.32  ? 40  HIS A CD2 1 
ATOM   286  C  CE1 . HIS A 1 48  ? -13.846 1.755   -39.561  1.00 21.58  ? 40  HIS A CE1 1 
ATOM   287  N  NE2 . HIS A 1 48  ? -14.225 2.456   -38.506  1.00 19.41  ? 40  HIS A NE2 1 
ATOM   288  N  N   . CYS A 1 49  ? -13.962 -1.107  -35.711  1.00 21.88  ? 41  CYS A N   1 
ATOM   289  C  CA  . CYS A 1 49  ? -15.100 -1.126  -34.804  1.00 27.09  ? 41  CYS A CA  1 
ATOM   290  C  C   . CYS A 1 49  ? -14.982 -2.173  -33.708  1.00 24.79  ? 41  CYS A C   1 
ATOM   291  O  O   . CYS A 1 49  ? -15.989 -2.492  -33.074  1.00 21.47  ? 41  CYS A O   1 
ATOM   292  C  CB  . CYS A 1 49  ? -16.399 -1.402  -35.568  1.00 30.92  ? 41  CYS A CB  1 
ATOM   293  S  SG  . CYS A 1 49  ? -16.860 -0.180  -36.807  1.00 23.96  ? 41  CYS A SG  1 
ATOM   294  N  N   . TYR A 1 50  ? -13.811 -2.759  -33.491  1.00 24.39  ? 42  TYR A N   1 
ATOM   295  C  CA  . TYR A 1 50  ? -13.744 -3.799  -32.480  1.00 25.37  ? 42  TYR A CA  1 
ATOM   296  C  C   . TYR A 1 50  ? -14.011 -3.215  -31.097  1.00 25.49  ? 42  TYR A C   1 
ATOM   297  O  O   . TYR A 1 50  ? -13.513 -2.143  -30.748  1.00 24.73  ? 42  TYR A O   1 
ATOM   298  C  CB  . TYR A 1 50  ? -12.391 -4.492  -32.481  1.00 28.69  ? 42  TYR A CB  1 
ATOM   299  C  CG  . TYR A 1 50  ? -12.246 -5.379  -31.271  1.00 27.57  ? 42  TYR A CG  1 
ATOM   300  C  CD1 . TYR A 1 50  ? -12.747 -6.678  -31.277  1.00 19.63  ? 42  TYR A CD1 1 
ATOM   301  C  CD2 . TYR A 1 50  ? -11.660 -4.900  -30.098  1.00 25.92  ? 42  TYR A CD2 1 
ATOM   302  C  CE1 . TYR A 1 50  ? -12.641 -7.493  -30.157  1.00 24.33  ? 42  TYR A CE1 1 
ATOM   303  C  CE2 . TYR A 1 50  ? -11.550 -5.701  -28.982  1.00 29.75  ? 42  TYR A CE2 1 
ATOM   304  C  CZ  . TYR A 1 50  ? -12.042 -6.997  -29.013  1.00 28.25  ? 42  TYR A CZ  1 
ATOM   305  O  OH  . TYR A 1 50  ? -11.931 -7.784  -27.889  1.00 37.93  ? 42  TYR A OH  1 
ATOM   306  N  N   . LYS A 1 51  ? -14.790 -3.941  -30.304  1.00 23.89  ? 43  LYS A N   1 
ATOM   307  C  CA  . LYS A 1 51  ? -14.995 -3.622  -28.901  1.00 25.43  ? 43  LYS A CA  1 
ATOM   308  C  C   . LYS A 1 51  ? -15.258 -4.942  -28.200  1.00 31.33  ? 43  LYS A C   1 
ATOM   309  O  O   . LYS A 1 51  ? -15.756 -5.891  -28.820  1.00 24.67  ? 43  LYS A O   1 
ATOM   310  C  CB  . LYS A 1 51  ? -16.168 -2.664  -28.671  1.00 24.49  ? 43  LYS A CB  1 
ATOM   311  C  CG  . LYS A 1 51  ? -15.970 -1.232  -29.176  1.00 29.51  ? 43  LYS A CG  1 
ATOM   312  C  CD  . LYS A 1 51  ? -17.157 -0.356  -28.786  1.00 25.91  ? 43  LYS A CD  1 
ATOM   313  C  CE  . LYS A 1 51  ? -16.995 1.041   -29.316  1.00 28.57  ? 43  LYS A CE  1 
ATOM   314  N  NZ  . LYS A 1 51  ? -17.872 1.966   -28.572  1.00 29.45  ? 43  LYS A NZ  1 
ATOM   315  N  N   . SER A 1 52  ? -14.906 -4.999  -26.908  1.00 26.56  ? 44  SER A N   1 
ATOM   316  C  CA  . SER A 1 52  ? -15.006 -6.243  -26.147  1.00 27.69  ? 44  SER A CA  1 
ATOM   317  C  C   . SER A 1 52  ? -16.436 -6.670  -25.907  1.00 25.89  ? 44  SER A C   1 
ATOM   318  O  O   . SER A 1 52  ? -16.690 -7.852  -25.667  1.00 26.13  ? 44  SER A O   1 
ATOM   319  C  CB  . SER A 1 52  ? -14.304 -6.117  -24.795  1.00 29.18  ? 44  SER A CB  1 
ATOM   320  O  OG  . SER A 1 52  ? -12.969 -6.579  -24.875  1.00 52.69  ? 44  SER A OG  1 
ATOM   321  N  N   . ARG A 1 53  ? -17.373 -5.745  -25.920  1.00 27.10  ? 45  ARG A N   1 
ATOM   322  C  CA  . ARG A 1 53  ? -18.769 -6.094  -25.725  1.00 29.46  ? 45  ARG A CA  1 
ATOM   323  C  C   . ARG A 1 53  ? -19.575 -5.336  -26.763  1.00 28.46  ? 45  ARG A C   1 
ATOM   324  O  O   . ARG A 1 53  ? -19.409 -4.121  -26.907  1.00 32.22  ? 45  ARG A O   1 
ATOM   325  C  CB  . ARG A 1 53  ? -19.224 -5.764  -24.295  1.00 36.48  ? 45  ARG A CB  1 
ATOM   326  C  CG  . ARG A 1 53  ? -18.867 -6.853  -23.304  1.00 51.06  ? 45  ARG A CG  1 
ATOM   327  C  CD  . ARG A 1 53  ? -18.892 -6.419  -21.839  1.00 56.36  ? 45  ARG A CD  1 
ATOM   328  N  NE  . ARG A 1 53  ? -18.306 -7.477  -21.022  1.00 63.66  ? 45  ARG A NE  1 
ATOM   329  C  CZ  . ARG A 1 53  ? -17.005 -7.667  -20.830  1.00 65.34  ? 45  ARG A CZ  1 
ATOM   330  N  NH1 . ARG A 1 53  ? -16.113 -6.741  -21.148  1.00 63.54  ? 45  ARG A NH1 1 
ATOM   331  N  NH2 . ARG A 1 53  ? -16.590 -8.810  -20.288  1.00 64.94  ? 45  ARG A NH2 1 
ATOM   332  N  N   . ILE A 1 54  ? -20.424 -6.047  -27.498  1.00 24.90  ? 46  ILE A N   1 
ATOM   333  C  CA  . ILE A 1 54  ? -21.218 -5.435  -28.557  1.00 20.70  ? 46  ILE A CA  1 
ATOM   334  C  C   . ILE A 1 54  ? -22.626 -6.002  -28.496  1.00 23.58  ? 46  ILE A C   1 
ATOM   335  O  O   . ILE A 1 54  ? -22.810 -7.220  -28.392  1.00 23.00  ? 46  ILE A O   1 
ATOM   336  C  CB  . ILE A 1 54  ? -20.595 -5.668  -29.953  1.00 23.71  ? 46  ILE A CB  1 
ATOM   337  C  CG1 . ILE A 1 54  ? -19.307 -4.849  -30.110  1.00 21.02  ? 46  ILE A CG1 1 
ATOM   338  C  CG2 . ILE A 1 54  ? -21.604 -5.360  -31.062  1.00 23.73  ? 46  ILE A CG2 1 
ATOM   339  C  CD1 . ILE A 1 54  ? -18.428 -5.220  -31.314  1.00 17.25  ? 46  ILE A CD1 1 
ATOM   340  N  N   . GLN A 1 55  ? -23.620 -5.125  -28.559  1.00 20.64  ? 47  GLN A N   1 
ATOM   341  C  CA  . GLN A 1 55  ? -24.993 -5.544  -28.786  1.00 20.66  ? 47  GLN A CA  1 
ATOM   342  C  C   . GLN A 1 55  ? -25.344 -5.254  -30.237  1.00 23.67  ? 47  GLN A C   1 
ATOM   343  O  O   . GLN A 1 55  ? -25.145 -4.131  -30.714  1.00 25.55  ? 47  GLN A O   1 
ATOM   344  C  CB  . GLN A 1 55  ? -25.957 -4.820  -27.853  1.00 19.25  ? 47  GLN A CB  1 
ATOM   345  C  CG  . GLN A 1 55  ? -27.423 -5.233  -28.033  1.00 20.27  ? 47  GLN A CG  1 
ATOM   346  C  CD  . GLN A 1 55  ? -28.319 -4.515  -27.039  1.00 28.49  ? 47  GLN A CD  1 
ATOM   347  O  OE1 . GLN A 1 55  ? -28.459 -3.288  -27.076  1.00 26.45  ? 47  GLN A OE1 1 
ATOM   348  N  NE2 . GLN A 1 55  ? -28.897 -5.273  -26.117  1.00 22.64  ? 47  GLN A NE2 1 
ATOM   349  N  N   . VAL A 1 56  ? -25.818 -6.264  -30.948  1.00 16.58  ? 48  VAL A N   1 
ATOM   350  C  CA  . VAL A 1 56  ? -26.211 -6.102  -32.344  1.00 17.68  ? 48  VAL A CA  1 
ATOM   351  C  C   . VAL A 1 56  ? -27.692 -5.757  -32.368  1.00 25.69  ? 48  VAL A C   1 
ATOM   352  O  O   . VAL A 1 56  ? -28.500 -6.430  -31.719  1.00 21.82  ? 48  VAL A O   1 
ATOM   353  C  CB  . VAL A 1 56  ? -25.920 -7.382  -33.149  1.00 17.27  ? 48  VAL A CB  1 
ATOM   354  C  CG1 . VAL A 1 56  ? -26.392 -7.253  -34.580  1.00 19.21  ? 48  VAL A CG1 1 
ATOM   355  C  CG2 . VAL A 1 56  ? -24.450 -7.702  -33.120  1.00 12.84  ? 48  VAL A CG2 1 
ATOM   356  N  N   . ARG A 1 57  ? -28.057 -4.696  -33.089  1.00 24.80  ? 49  ARG A N   1 
ATOM   357  C  CA  . ARG A 1 57  ? -29.452 -4.258  -33.174  1.00 23.41  ? 49  ARG A CA  1 
ATOM   358  C  C   . ARG A 1 57  ? -29.927 -4.449  -34.606  1.00 22.41  ? 49  ARG A C   1 
ATOM   359  O  O   . ARG A 1 57  ? -29.404 -3.820  -35.529  1.00 24.88  ? 49  ARG A O   1 
ATOM   360  C  CB  . ARG A 1 57  ? -29.601 -2.811  -32.702  1.00 18.26  ? 49  ARG A CB  1 
ATOM   361  C  CG  . ARG A 1 57  ? -29.334 -2.726  -31.211  1.00 22.93  ? 49  ARG A CG  1 
ATOM   362  C  CD  . ARG A 1 57  ? -29.596 -1.368  -30.617  1.00 24.05  ? 49  ARG A CD  1 
ATOM   363  N  NE  . ARG A 1 57  ? -29.521 -1.434  -29.163  1.00 20.10  ? 49  ARG A NE  1 
ATOM   364  C  CZ  . ARG A 1 57  ? -30.036 -0.527  -28.342  1.00 29.74  ? 49  ARG A CZ  1 
ATOM   365  N  NH1 . ARG A 1 57  ? -30.650 0.556   -28.805  1.00 27.14  ? 49  ARG A NH1 1 
ATOM   366  N  NH2 . ARG A 1 57  ? -29.936 -0.711  -27.025  1.00 22.48  ? 49  ARG A NH2 1 
ATOM   367  N  N   . LEU A 1 58  ? -30.892 -5.340  -34.788  1.00 21.57  ? 50  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 58  ? -31.400 -5.715  -36.096  1.00 19.05  ? 50  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 58  ? -32.812 -5.178  -36.311  1.00 21.35  ? 50  LEU A C   1 
ATOM   370  O  O   . LEU A 1 58  ? -33.547 -4.886  -35.363  1.00 25.10  ? 50  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 58  ? -31.391 -7.239  -36.244  1.00 24.08  ? 50  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 58  ? -30.004 -7.873  -36.113  1.00 26.81  ? 50  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 58  ? -29.814 -8.464  -34.735  1.00 29.98  ? 50  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 58  ? -29.782 -8.930  -37.193  1.00 28.36  ? 50  LEU A CD2 1 
ATOM   375  N  N   . GLY A 1 59  ? -33.204 -5.077  -37.578  1.00 26.21  ? 51  GLY A N   1 
ATOM   376  C  CA  . GLY A 1 59  ? -34.540 -4.586  -37.893  1.00 23.96  ? 51  GLY A CA  1 
ATOM   377  C  C   . GLY A 1 59  ? -34.787 -3.178  -37.411  1.00 23.62  ? 51  GLY A C   1 
ATOM   378  O  O   . GLY A 1 59  ? -35.937 -2.787  -37.204  1.00 30.89  ? 51  GLY A O   1 
ATOM   379  N  N   . GLU A 1 60  ? -33.726 -2.401  -37.241  1.00 25.70  ? 52  GLU A N   1 
ATOM   380  C  CA  . GLU A 1 60  ? -33.781 -1.061  -36.677  1.00 29.58  ? 52  GLU A CA  1 
ATOM   381  C  C   . GLU A 1 60  ? -34.007 -0.029  -37.776  1.00 29.49  ? 52  GLU A C   1 
ATOM   382  O  O   . GLU A 1 60  ? -33.385 -0.101  -38.836  1.00 32.89  ? 52  GLU A O   1 
ATOM   383  C  CB  . GLU A 1 60  ? -32.469 -0.775  -35.945  1.00 23.68  ? 52  GLU A CB  1 
ATOM   384  C  CG  . GLU A 1 60  ? -32.548 0.368   -35.013  1.00 40.24  ? 52  GLU A CG  1 
ATOM   385  C  CD  . GLU A 1 60  ? -33.259 -0.005  -33.755  1.00 34.05  ? 52  GLU A CD  1 
ATOM   386  O  OE1 . GLU A 1 60  ? -34.466 0.291   -33.700  1.00 43.46  ? 52  GLU A OE1 1 
ATOM   387  O  OE2 . GLU A 1 60  ? -32.617 -0.537  -32.813  1.00 35.14  ? 52  GLU A OE2 1 
ATOM   388  N  N   . HIS A 1 61  ? -34.912 0.923   -37.534  1.00 27.10  ? 53  HIS A N   1 
ATOM   389  C  CA  . HIS A 1 61  ? -35.025 2.075   -38.429  1.00 33.56  ? 53  HIS A CA  1 
ATOM   390  C  C   . HIS A 1 61  ? -34.717 3.369   -37.690  1.00 27.08  ? 53  HIS A C   1 
ATOM   391  O  O   . HIS A 1 61  ? -33.752 4.051   -38.045  1.00 25.30  ? 53  HIS A O   1 
ATOM   392  C  CB  . HIS A 1 61  ? -36.410 2.171   -39.094  1.00 32.70  ? 53  HIS A CB  1 
ATOM   393  C  CG  . HIS A 1 61  ? -36.492 3.251   -40.132  1.00 36.70  ? 53  HIS A CG  1 
ATOM   394  N  ND1 . HIS A 1 61  ? -37.272 4.379   -39.978  1.00 45.43  ? 53  HIS A ND1 1 
ATOM   395  C  CD2 . HIS A 1 61  ? -35.862 3.391   -41.325  1.00 43.89  ? 53  HIS A CD2 1 
ATOM   396  C  CE1 . HIS A 1 61  ? -37.125 5.163   -41.033  1.00 42.27  ? 53  HIS A CE1 1 
ATOM   397  N  NE2 . HIS A 1 61  ? -36.278 4.585   -41.867  1.00 45.59  ? 53  HIS A NE2 1 
ATOM   398  N  N   . ASN A 1 62  ? -35.521 3.726   -36.684  1.00 23.60  ? 54  ASN A N   1 
ATOM   399  C  CA  . ASN A 1 62  ? -35.201 4.789   -35.739  1.00 25.77  ? 54  ASN A CA  1 
ATOM   400  C  C   . ASN A 1 62  ? -34.360 4.205   -34.612  1.00 29.00  ? 54  ASN A C   1 
ATOM   401  O  O   . ASN A 1 62  ? -34.853 3.370   -33.851  1.00 33.76  ? 54  ASN A O   1 
ATOM   402  C  CB  . ASN A 1 62  ? -36.474 5.405   -35.159  1.00 22.25  ? 54  ASN A CB  1 
ATOM   403  C  CG  . ASN A 1 62  ? -36.225 6.758   -34.471  1.00 23.14  ? 54  ASN A CG  1 
ATOM   404  O  OD1 . ASN A 1 62  ? -35.219 6.958   -33.784  1.00 22.57  ? 54  ASN A OD1 1 
ATOM   405  N  ND2 . ASN A 1 62  ? -37.179 7.661   -34.603  1.00 17.27  ? 54  ASN A ND2 1 
ATOM   406  N  N   . ILE A 1 63  ? -33.097 4.630   -34.492  1.00 21.72  ? 55  ILE A N   1 
ATOM   407  C  CA  . ILE A 1 63  ? -32.259 4.018   -33.460  1.00 26.65  ? 55  ILE A CA  1 
ATOM   408  C  C   . ILE A 1 63  ? -32.477 4.631   -32.089  1.00 27.62  ? 55  ILE A C   1 
ATOM   409  O  O   . ILE A 1 63  ? -31.891 4.153   -31.111  1.00 22.32  ? 55  ILE A O   1 
ATOM   410  C  CB  . ILE A 1 63  ? -30.744 4.089   -33.746  1.00 23.08  ? 55  ILE A CB  1 
ATOM   411  C  CG1 . ILE A 1 63  ? -30.340 5.474   -34.199  1.00 21.34  ? 55  ILE A CG1 1 
ATOM   412  C  CG2 . ILE A 1 63  ? -30.334 3.066   -34.790  1.00 27.76  ? 55  ILE A CG2 1 
ATOM   413  C  CD1 . ILE A 1 63  ? -28.898 5.740   -34.000  1.00 19.24  ? 55  ILE A CD1 1 
ATOM   414  N  N   . ASP A 1 64  ? -33.293 5.677   -31.987  1.00 29.05  ? 56  ASP A N   1 
ATOM   415  C  CA  . ASP A 1 64  ? -33.509 6.363   -30.720  1.00 27.23  ? 56  ASP A CA  1 
ATOM   416  C  C   . ASP A 1 64  ? -34.834 6.018   -30.071  1.00 26.28  ? 56  ASP A C   1 
ATOM   417  O  O   . ASP A 1 64  ? -35.070 6.427   -28.935  1.00 27.10  ? 56  ASP A O   1 
ATOM   418  C  CB  . ASP A 1 64  ? -33.439 7.877   -30.920  1.00 31.87  ? 56  ASP A CB  1 
ATOM   419  C  CG  . ASP A 1 64  ? -32.003 8.389   -31.041  1.00 38.52  ? 56  ASP A CG  1 
ATOM   420  O  OD1 . ASP A 1 64  ? -31.129 7.933   -30.269  1.00 34.66  ? 56  ASP A OD1 1 
ATOM   421  O  OD2 . ASP A 1 64  ? -31.750 9.239   -31.927  1.00 36.19  ? 56  ASP A OD2 1 
ATOM   422  N  N   . VAL A 1 65  ? -35.701 5.279   -30.754  1.00 33.96  ? 57  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 65  ? -37.062 5.043   -30.292  1.00 25.14  ? 57  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 65  ? -37.323 3.560   -30.460  1.00 26.10  ? 57  VAL A C   1 
ATOM   425  O  O   . VAL A 1 65  ? -37.349 3.059   -31.584  1.00 31.36  ? 57  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 65  ? -38.091 5.875   -31.068  1.00 18.26  ? 57  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 65  ? -39.490 5.563   -30.595  1.00 18.76  ? 57  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 65  ? -37.802 7.329   -30.891  1.00 15.91  ? 57  VAL A CG2 1 
ATOM   429  N  N   . LEU A 1 66  ? -37.506 2.854   -29.358  1.00 32.01  ? 58  LEU A N   1 
ATOM   430  C  CA  . LEU A 1 66  ? -37.816 1.439   -29.462  1.00 31.54  ? 58  LEU A CA  1 
ATOM   431  C  C   . LEU A 1 66  ? -39.238 1.266   -29.981  1.00 33.30  ? 58  LEU A C   1 
ATOM   432  O  O   . LEU A 1 66  ? -40.201 1.529   -29.257  1.00 34.65  ? 58  LEU A O   1 
ATOM   433  C  CB  . LEU A 1 66  ? -37.630 0.760   -28.113  1.00 32.05  ? 58  LEU A CB  1 
ATOM   434  C  CG  . LEU A 1 66  ? -37.564 -0.755  -28.289  1.00 40.01  ? 58  LEU A CG  1 
ATOM   435  C  CD1 . LEU A 1 66  ? -36.138 -1.208  -28.543  1.00 37.20  ? 58  LEU A CD1 1 
ATOM   436  C  CD2 . LEU A 1 66  ? -38.103 -1.402  -27.039  1.00 44.46  ? 58  LEU A CD2 1 
ATOM   437  N  N   . GLU A 1 67  ? -39.376 0.825   -31.234  1.00 24.05  ? 59  GLU A N   1 
ATOM   438  C  CA  . GLU A 1 67  ? -40.705 0.593   -31.795  1.00 26.85  ? 59  GLU A CA  1 
ATOM   439  C  C   . GLU A 1 67  ? -41.362 -0.637  -31.178  1.00 33.55  ? 59  GLU A C   1 
ATOM   440  O  O   . GLU A 1 67  ? -42.511 -0.579  -30.727  1.00 33.23  ? 59  GLU A O   1 
ATOM   441  C  CB  . GLU A 1 67  ? -40.614 0.446   -33.314  1.00 35.51  ? 59  GLU A CB  1 
ATOM   442  C  CG  . GLU A 1 67  ? -41.961 0.371   -34.013  1.00 44.18  ? 59  GLU A CG  1 
ATOM   443  C  CD  . GLU A 1 67  ? -42.303 -1.045  -34.462  1.00 52.64  ? 59  GLU A CD  1 
ATOM   444  O  OE1 . GLU A 1 67  ? -41.428 -1.927  -34.317  1.00 56.73  ? 59  GLU A OE1 1 
ATOM   445  O  OE2 . GLU A 1 67  ? -43.427 -1.273  -34.975  1.00 56.49  ? 59  GLU A OE2 1 
ATOM   446  N  N   . GLY A 1 68  ? -40.655 -1.763  -31.165  1.00 35.39  ? 60  GLY A N   1 
ATOM   447  C  CA  . GLY A 1 68  ? -41.157 -2.975  -30.558  1.00 31.24  ? 60  GLY A CA  1 
ATOM   448  C  C   . GLY A 1 68  ? -40.746 -4.232  -31.290  1.00 29.90  ? 60  GLY A C   1 
ATOM   449  O  O   . GLY A 1 68  ? -40.712 -5.299  -30.688  1.00 42.68  ? 60  GLY A O   1 
ATOM   450  N  N   . ASN A 1 69  ? -40.404 -4.132  -32.572  1.00 35.64  ? 61  ASN A N   1 
ATOM   451  C  CA  . ASN A 1 69  ? -40.102 -5.316  -33.361  1.00 42.06  ? 61  ASN A CA  1 
ATOM   452  C  C   . ASN A 1 69  ? -38.628 -5.419  -33.724  1.00 40.35  ? 61  ASN A C   1 
ATOM   453  O  O   . ASN A 1 69  ? -38.262 -6.181  -34.619  1.00 37.97  ? 61  ASN A O   1 
ATOM   454  C  CB  . ASN A 1 69  ? -40.977 -5.339  -34.609  1.00 39.13  ? 61  ASN A CB  1 
ATOM   455  C  CG  . ASN A 1 69  ? -42.441 -5.584  -34.272  1.00 54.50  ? 61  ASN A CG  1 
ATOM   456  O  OD1 . ASN A 1 69  ? -42.802 -6.635  -33.735  1.00 50.10  ? 61  ASN A OD1 1 
ATOM   457  N  ND2 . ASN A 1 69  ? -43.290 -4.604  -34.570  1.00 62.61  ? 61  ASN A ND2 1 
ATOM   458  N  N   . GLU A 1 70  ? -37.773 -4.670  -33.049  1.00 32.99  ? 62  GLU A N   1 
ATOM   459  C  CA  . GLU A 1 70  ? -36.350 -4.849  -33.248  1.00 30.32  ? 62  GLU A CA  1 
ATOM   460  C  C   . GLU A 1 70  ? -35.892 -6.142  -32.577  1.00 29.13  ? 62  GLU A C   1 
ATOM   461  O  O   . GLU A 1 70  ? -36.592 -6.720  -31.743  1.00 31.52  ? 62  GLU A O   1 
ATOM   462  C  CB  . GLU A 1 70  ? -35.597 -3.632  -32.697  1.00 29.44  ? 62  GLU A CB  1 
ATOM   463  C  CG  . GLU A 1 70  ? -36.080 -2.325  -33.336  1.00 30.02  ? 62  GLU A CG  1 
ATOM   464  C  CD  . GLU A 1 70  ? -37.022 -1.551  -32.437  1.00 33.70  ? 62  GLU A CD  1 
ATOM   465  O  OE1 . GLU A 1 70  ? -37.726 -2.191  -31.632  1.00 39.98  ? 62  GLU A OE1 1 
ATOM   466  O  OE2 . GLU A 1 70  ? -37.120 -0.324  -32.583  1.00 29.28  ? 62  GLU A OE2 1 
ATOM   467  N  N   . GLN A 1 71  ? -34.714 -6.617  -32.970  1.00 28.98  ? 63  GLN A N   1 
ATOM   468  C  CA  . GLN A 1 71  ? -34.053 -7.728  -32.294  1.00 20.94  ? 63  GLN A CA  1 
ATOM   469  C  C   . GLN A 1 71  ? -32.731 -7.230  -31.735  1.00 25.19  ? 63  GLN A C   1 
ATOM   470  O  O   . GLN A 1 71  ? -31.863 -6.767  -32.488  1.00 30.30  ? 63  GLN A O   1 
ATOM   471  C  CB  . GLN A 1 71  ? -33.813 -8.904  -33.242  1.00 27.14  ? 63  GLN A CB  1 
ATOM   472  C  CG  . GLN A 1 71  ? -35.050 -9.370  -33.927  1.00 29.03  ? 63  GLN A CG  1 
ATOM   473  C  CD  . GLN A 1 71  ? -34.803 -10.561 -34.832  1.00 37.05  ? 63  GLN A CD  1 
ATOM   474  O  OE1 . GLN A 1 71  ? -34.025 -11.463 -34.497  1.00 35.09  ? 63  GLN A OE1 1 
ATOM   475  N  NE2 . GLN A 1 71  ? -35.462 -10.566 -35.995  1.00 17.84  ? 63  GLN A NE2 1 
ATOM   476  N  N   . PHE A 1 72  ? -32.574 -7.329  -30.427  1.00 24.68  ? 64  PHE A N   1 
ATOM   477  C  CA  . PHE A 1 72  ? -31.327 -6.986  -29.761  1.00 19.68  ? 64  PHE A CA  1 
ATOM   478  C  C   . PHE A 1 72  ? -30.633 -8.295  -29.377  1.00 30.90  ? 64  PHE A C   1 
ATOM   479  O  O   . PHE A 1 72  ? -31.156 -9.061  -28.562  1.00 32.80  ? 64  PHE A O   1 
ATOM   480  C  CB  . PHE A 1 72  ? -31.596 -6.093  -28.548  1.00 26.00  ? 64  PHE A CB  1 
ATOM   481  C  CG  . PHE A 1 72  ? -32.085 -4.691  -28.900  1.00 27.57  ? 64  PHE A CG  1 
ATOM   482  C  CD1 . PHE A 1 72  ? -32.410 -4.349  -30.209  1.00 20.58  ? 64  PHE A CD1 1 
ATOM   483  C  CD2 . PHE A 1 72  ? -32.216 -3.720  -27.915  1.00 26.31  ? 64  PHE A CD2 1 
ATOM   484  C  CE1 . PHE A 1 72  ? -32.854 -3.066  -30.532  1.00 23.58  ? 64  PHE A CE1 1 
ATOM   485  C  CE2 . PHE A 1 72  ? -32.656 -2.443  -28.232  1.00 27.57  ? 64  PHE A CE2 1 
ATOM   486  C  CZ  . PHE A 1 72  ? -32.971 -2.117  -29.546  1.00 23.30  ? 64  PHE A CZ  1 
ATOM   487  N  N   . ILE A 1 73  ? -29.468 -8.564  -29.973  1.00 25.59  ? 65  ILE A N   1 
ATOM   488  C  CA  . ILE A 1 73  ? -28.735 -9.809  -29.760  1.00 25.48  ? 65  ILE A CA  1 
ATOM   489  C  C   . ILE A 1 73  ? -27.273 -9.502  -29.439  1.00 25.82  ? 65  ILE A C   1 
ATOM   490  O  O   . ILE A 1 73  ? -26.578 -8.877  -30.246  1.00 29.35  ? 65  ILE A O   1 
ATOM   491  C  CB  . ILE A 1 73  ? -28.812 -10.732 -30.980  1.00 27.50  ? 65  ILE A CB  1 
ATOM   492  C  CG1 . ILE A 1 73  ? -30.263 -10.938 -31.406  1.00 27.25  ? 65  ILE A CG1 1 
ATOM   493  C  CG2 . ILE A 1 73  ? -28.114 -12.061 -30.662  1.00 29.72  ? 65  ILE A CG2 1 
ATOM   494  C  CD1 . ILE A 1 73  ? -30.397 -11.594 -32.767  1.00 29.19  ? 65  ILE A CD1 1 
ATOM   495  N  N   . ASN A 1 74  ? -26.797 -9.986  -28.294  1.00 20.29  ? 66  ASN A N   1 
ATOM   496  C  CA  . ASN A 1 74  ? -25.404 -9.797  -27.908  1.00 27.40  ? 66  ASN A CA  1 
ATOM   497  C  C   . ASN A 1 74  ? -24.460 -10.621 -28.779  1.00 28.79  ? 66  ASN A C   1 
ATOM   498  O  O   . ASN A 1 74  ? -24.786 -11.725 -29.215  1.00 26.41  ? 66  ASN A O   1 
ATOM   499  C  CB  . ASN A 1 74  ? -25.201 -10.185 -26.450  1.00 21.50  ? 66  ASN A CB  1 
ATOM   500  C  CG  . ASN A 1 74  ? -25.934 -9.256  -25.514  1.00 25.85  ? 66  ASN A CG  1 
ATOM   501  O  OD1 . ASN A 1 74  ? -26.234 -8.124  -25.879  1.00 30.92  ? 66  ASN A OD1 1 
ATOM   502  N  ND2 . ASN A 1 74  ? -26.221 -9.718  -24.303  1.00 36.18  ? 66  ASN A ND2 1 
ATOM   503  N  N   . ALA A 1 75  ? -23.271 -10.077 -29.027  1.00 22.21  ? 67  ALA A N   1 
ATOM   504  C  CA  . ALA A 1 75  ? -22.276 -10.827 -29.785  1.00 34.36  ? 67  ALA A CA  1 
ATOM   505  C  C   . ALA A 1 75  ? -21.700 -11.955 -28.930  1.00 28.20  ? 67  ALA A C   1 
ATOM   506  O  O   . ALA A 1 75  ? -21.326 -11.740 -27.773  1.00 39.40  ? 67  ALA A O   1 
ATOM   507  C  CB  . ALA A 1 75  ? -21.160 -9.896  -30.260  1.00 25.01  ? 67  ALA A CB  1 
ATOM   508  N  N   . ALA A 1 76  ? -21.626 -13.161 -29.484  1.00 33.23  ? 68  ALA A N   1 
ATOM   509  C  CA  . ALA A 1 76  ? -20.960 -14.243 -28.757  1.00 33.92  ? 68  ALA A CA  1 
ATOM   510  C  C   . ALA A 1 76  ? -19.478 -14.335 -29.079  1.00 41.46  ? 68  ALA A C   1 
ATOM   511  O  O   . ALA A 1 76  ? -18.703 -14.839 -28.258  1.00 44.02  ? 68  ALA A O   1 
ATOM   512  C  CB  . ALA A 1 76  ? -21.614 -15.594 -29.053  1.00 24.23  ? 68  ALA A CB  1 
ATOM   513  N  N   . LYS A 1 77  ? -19.069 -13.838 -30.239  1.00 39.85  ? 69  LYS A N   1 
ATOM   514  C  CA  . LYS A 1 77  ? -17.705 -13.986 -30.711  1.00 39.58  ? 69  LYS A CA  1 
ATOM   515  C  C   . LYS A 1 77  ? -17.443 -12.820 -31.648  1.00 35.39  ? 69  LYS A C   1 
ATOM   516  O  O   . LYS A 1 77  ? -18.284 -12.507 -32.495  1.00 33.54  ? 69  LYS A O   1 
ATOM   517  C  CB  . LYS A 1 77  ? -17.530 -15.332 -31.422  1.00 29.20  ? 69  LYS A CB  1 
ATOM   518  C  CG  . LYS A 1 77  ? -16.157 -15.968 -31.313  1.00 45.84  ? 69  LYS A CG  1 
ATOM   519  C  CD  . LYS A 1 77  ? -16.080 -17.157 -32.272  1.00 34.96  ? 69  LYS A CD  1 
ATOM   520  C  CE  . LYS A 1 77  ? -16.758 -18.392 -31.684  1.00 35.31  ? 69  LYS A CE  1 
ATOM   521  N  NZ  . LYS A 1 77  ? -16.668 -18.429 -30.186  1.00 37.79  ? 69  LYS A NZ  1 
ATOM   522  N  N   . ILE A 1 78  ? -16.302 -12.163 -31.469  1.00 29.82  ? 70  ILE A N   1 
ATOM   523  C  CA  . ILE A 1 78  ? -15.930 -10.971 -32.224  1.00 31.87  ? 70  ILE A CA  1 
ATOM   524  C  C   . ILE A 1 78  ? -14.534 -11.216 -32.783  1.00 31.75  ? 70  ILE A C   1 
ATOM   525  O  O   . ILE A 1 78  ? -13.553 -11.214 -32.028  1.00 31.43  ? 70  ILE A O   1 
ATOM   526  C  CB  . ILE A 1 78  ? -15.973 -9.700  -31.360  1.00 32.28  ? 70  ILE A CB  1 
ATOM   527  C  CG1 . ILE A 1 78  ? -17.350 -9.528  -30.726  1.00 35.82  ? 70  ILE A CG1 1 
ATOM   528  C  CG2 . ILE A 1 78  ? -15.651 -8.483  -32.168  1.00 36.84  ? 70  ILE A CG2 1 
ATOM   529  C  CD1 . ILE A 1 78  ? -17.318 -8.736  -29.462  1.00 30.81  ? 70  ILE A CD1 1 
ATOM   530  N  N   . ILE A 1 79  ? -14.445 -11.437 -34.098  1.00 23.69  ? 71  ILE A N   1 
ATOM   531  C  CA  . ILE A 1 79  ? -13.225 -11.886 -34.760  1.00 21.70  ? 71  ILE A CA  1 
ATOM   532  C  C   . ILE A 1 79  ? -12.725 -10.802 -35.706  1.00 27.73  ? 71  ILE A C   1 
ATOM   533  O  O   . ILE A 1 79  ? -13.272 -10.623 -36.801  1.00 29.78  ? 71  ILE A O   1 
ATOM   534  C  CB  . ILE A 1 79  ? -13.446 -13.194 -35.525  1.00 29.80  ? 71  ILE A CB  1 
ATOM   535  C  CG1 . ILE A 1 79  ? -14.086 -14.246 -34.608  1.00 27.00  ? 71  ILE A CG1 1 
ATOM   536  C  CG2 . ILE A 1 79  ? -12.143 -13.660 -36.165  1.00 18.42  ? 71  ILE A CG2 1 
ATOM   537  C  CD1 . ILE A 1 79  ? -13.886 -15.674 -35.084  1.00 27.22  ? 71  ILE A CD1 1 
ATOM   538  N  N   . THR A 1 80  ? -11.659 -10.113 -35.320  1.00 26.04  ? 72  THR A N   1 
ATOM   539  C  CA  . THR A 1 80  ? -11.045 -9.196  -36.262  1.00 22.13  ? 72  THR A CA  1 
ATOM   540  C  C   . THR A 1 80  ? -10.163 -9.973  -37.229  1.00 23.58  ? 72  THR A C   1 
ATOM   541  O  O   . THR A 1 80  ? -9.680  -11.064 -36.921  1.00 29.40  ? 72  THR A O   1 
ATOM   542  C  CB  . THR A 1 80  ? -10.221 -8.154  -35.526  1.00 23.43  ? 72  THR A CB  1 
ATOM   543  O  OG1 . THR A 1 80  ? -9.144  -8.806  -34.857  1.00 31.02  ? 72  THR A OG1 1 
ATOM   544  C  CG2 . THR A 1 80  ? -11.073 -7.461  -34.473  1.00 30.95  ? 72  THR A CG2 1 
ATOM   545  N  N   . HIS A 1 81  ? -9.969  -9.414  -38.414  1.00 27.81  ? 73  HIS A N   1 
ATOM   546  C  CA  . HIS A 1 81  ? -9.110  -10.061 -39.395  1.00 25.26  ? 73  HIS A CA  1 
ATOM   547  C  C   . HIS A 1 81  ? -7.693  -10.193 -38.840  1.00 26.34  ? 73  HIS A C   1 
ATOM   548  O  O   . HIS A 1 81  ? -7.148  -9.213  -38.306  1.00 25.93  ? 73  HIS A O   1 
ATOM   549  C  CB  . HIS A 1 81  ? -9.068  -9.289  -40.706  1.00 20.79  ? 73  HIS A CB  1 
ATOM   550  C  CG  . HIS A 1 81  ? -8.489  -10.085 -41.827  1.00 29.08  ? 73  HIS A CG  1 
ATOM   551  N  ND1 . HIS A 1 81  ? -7.136  -10.330 -41.938  1.00 27.39  ? 73  HIS A ND1 1 
ATOM   552  C  CD2 . HIS A 1 81  ? -9.073  -10.707 -42.877  1.00 29.06  ? 73  HIS A CD2 1 
ATOM   553  C  CE1 . HIS A 1 81  ? -6.913  -11.074 -43.004  1.00 25.09  ? 73  HIS A CE1 1 
ATOM   554  N  NE2 . HIS A 1 81  ? -8.070  -11.316 -43.593  1.00 30.27  ? 73  HIS A NE2 1 
ATOM   555  N  N   . PRO A 1 82  ? -7.055  -11.365 -38.967  1.00 30.16  ? 74  PRO A N   1 
ATOM   556  C  CA  . PRO A 1 82  ? -5.753  -11.573 -38.297  1.00 29.36  ? 74  PRO A CA  1 
ATOM   557  C  C   . PRO A 1 82  ? -4.623  -10.731 -38.858  1.00 23.67  ? 74  PRO A C   1 
ATOM   558  O  O   . PRO A 1 82  ? -3.625  -10.535 -38.157  1.00 31.11  ? 74  PRO A O   1 
ATOM   559  C  CB  . PRO A 1 82  ? -5.486  -13.072 -38.504  1.00 26.74  ? 74  PRO A CB  1 
ATOM   560  C  CG  . PRO A 1 82  ? -6.221  -13.379 -39.810  1.00 29.64  ? 74  PRO A CG  1 
ATOM   561  C  CD  . PRO A 1 82  ? -7.498  -12.568 -39.701  1.00 29.42  ? 74  PRO A CD  1 
ATOM   562  N  N   . ASN A 1 83  ? -4.728  -10.225 -40.081  1.00 20.08  ? 75  ASN A N   1 
ATOM   563  C  CA  . ASN A 1 83  ? -3.730  -9.289  -40.583  1.00 27.05  ? 75  ASN A CA  1 
ATOM   564  C  C   . ASN A 1 83  ? -4.256  -7.856  -40.666  1.00 25.88  ? 75  ASN A C   1 
ATOM   565  O  O   . ASN A 1 83  ? -3.826  -7.088  -41.528  1.00 33.02  ? 75  ASN A O   1 
ATOM   566  C  CB  . ASN A 1 83  ? -3.187  -9.746  -41.934  1.00 27.31  ? 75  ASN A CB  1 
ATOM   567  C  CG  . ASN A 1 83  ? -2.655  -11.170 -41.890  1.00 25.63  ? 75  ASN A CG  1 
ATOM   568  O  OD1 . ASN A 1 83  ? -3.211  -12.080 -42.517  1.00 28.03  ? 75  ASN A OD1 1 
ATOM   569  N  ND2 . ASN A 1 83  ? -1.612  -11.380 -41.101  1.00 18.89  ? 75  ASN A ND2 1 
ATOM   570  N  N   . PHE A 1 84  ? -5.165  -7.476  -39.764  1.00 23.69  ? 76  PHE A N   1 
ATOM   571  C  CA  . PHE A 1 84  ? -5.623  -6.092  -39.671  1.00 26.41  ? 76  PHE A CA  1 
ATOM   572  C  C   . PHE A 1 84  ? -4.577  -5.230  -38.962  1.00 24.45  ? 76  PHE A C   1 
ATOM   573  O  O   . PHE A 1 84  ? -4.096  -5.574  -37.876  1.00 32.73  ? 76  PHE A O   1 
ATOM   574  C  CB  . PHE A 1 84  ? -6.967  -6.017  -38.935  1.00 16.32  ? 76  PHE A CB  1 
ATOM   575  C  CG  . PHE A 1 84  ? -7.352  -4.635  -38.520  1.00 23.40  ? 76  PHE A CG  1 
ATOM   576  C  CD1 . PHE A 1 84  ? -7.777  -3.707  -39.454  1.00 19.83  ? 76  PHE A CD1 1 
ATOM   577  C  CD2 . PHE A 1 84  ? -7.275  -4.250  -37.185  1.00 30.69  ? 76  PHE A CD2 1 
ATOM   578  C  CE1 . PHE A 1 84  ? -8.124  -2.422  -39.067  1.00 26.39  ? 76  PHE A CE1 1 
ATOM   579  C  CE2 . PHE A 1 84  ? -7.630  -2.953  -36.784  1.00 28.95  ? 76  PHE A CE2 1 
ATOM   580  C  CZ  . PHE A 1 84  ? -8.064  -2.043  -37.730  1.00 26.81  ? 76  PHE A CZ  1 
ATOM   581  N  N   . ASN A 1 85  ? -4.221  -4.112  -39.576  1.00 24.31  ? 77  ASN A N   1 
ATOM   582  C  CA  . ASN A 1 85  ? -3.328  -3.142  -38.962  1.00 31.65  ? 77  ASN A CA  1 
ATOM   583  C  C   . ASN A 1 85  ? -4.055  -1.811  -38.930  1.00 33.43  ? 77  ASN A C   1 
ATOM   584  O  O   . ASN A 1 85  ? -4.450  -1.292  -39.982  1.00 27.79  ? 77  ASN A O   1 
ATOM   585  C  CB  . ASN A 1 85  ? -2.004  -3.028  -39.728  1.00 38.22  ? 77  ASN A CB  1 
ATOM   586  C  CG  . ASN A 1 85  ? -1.055  -1.981  -39.135  1.00 38.80  ? 77  ASN A CG  1 
ATOM   587  O  OD1 . ASN A 1 85  ? -1.456  -0.865  -38.793  1.00 35.95  ? 77  ASN A OD1 1 
ATOM   588  N  ND2 . ASN A 1 85  ? 0.219   -2.334  -39.042  1.00 46.48  ? 77  ASN A ND2 1 
ATOM   589  N  N   . GLY A 1 86  ? -4.192  -1.252  -37.724  1.00 38.14  ? 78  GLY A N   1 
ATOM   590  C  CA  . GLY A 1 86  ? -4.967  -0.069  -37.439  1.00 27.95  ? 78  GLY A CA  1 
ATOM   591  C  C   . GLY A 1 86  ? -4.323  1.235   -37.817  1.00 32.20  ? 78  GLY A C   1 
ATOM   592  O  O   . GLY A 1 86  ? -4.918  2.295   -37.600  1.00 44.49  ? 78  GLY A O   1 
ATOM   593  N  N   . ASN A 1 87  ? -3.119  1.204   -38.376  1.00 34.09  ? 79  ASN A N   1 
ATOM   594  C  CA  . ASN A 1 87  ? -2.474  2.425   -38.839  1.00 33.43  ? 79  ASN A CA  1 
ATOM   595  C  C   . ASN A 1 87  ? -2.026  2.386   -40.286  1.00 29.46  ? 79  ASN A C   1 
ATOM   596  O  O   . ASN A 1 87  ? -1.894  3.448   -40.891  1.00 30.23  ? 79  ASN A O   1 
ATOM   597  C  CB  . ASN A 1 87  ? -1.293  2.761   -37.930  1.00 22.56  ? 79  ASN A CB  1 
ATOM   598  C  CG  . ASN A 1 87  ? -1.754  3.041   -36.537  1.00 29.69  ? 79  ASN A CG  1 
ATOM   599  O  OD1 . ASN A 1 87  ? -2.313  4.109   -36.280  1.00 28.10  ? 79  ASN A OD1 1 
ATOM   600  N  ND2 . ASN A 1 87  ? -1.601  2.064   -35.636  1.00 24.88  ? 79  ASN A ND2 1 
ATOM   601  N  N   . THR A 1 88  ? -1.808  1.205   -40.856  1.00 35.63  ? 80  THR A N   1 
ATOM   602  C  CA  . THR A 1 88  ? -1.851  1.065   -42.299  1.00 26.03  ? 80  THR A CA  1 
ATOM   603  C  C   . THR A 1 88  ? -3.278  1.019   -42.800  1.00 27.28  ? 80  THR A C   1 
ATOM   604  O  O   . THR A 1 88  ? -3.509  1.116   -44.010  1.00 41.80  ? 80  THR A O   1 
ATOM   605  C  CB  . THR A 1 88  ? -1.141  -0.216  -42.736  1.00 34.33  ? 80  THR A CB  1 
ATOM   606  O  OG1 . THR A 1 88  ? -1.869  -1.352  -42.253  1.00 37.75  ? 80  THR A OG1 1 
ATOM   607  C  CG2 . THR A 1 88  ? 0.281   -0.264  -42.160  1.00 30.35  ? 80  THR A CG2 1 
ATOM   608  N  N   . LEU A 1 89  ? -4.236  0.825   -41.902  1.00 34.76  ? 81  LEU A N   1 
ATOM   609  C  CA  . LEU A 1 89  ? -5.652  0.703   -42.232  1.00 34.31  ? 81  LEU A CA  1 
ATOM   610  C  C   . LEU A 1 89  ? -5.959  -0.485  -43.139  1.00 35.43  ? 81  LEU A C   1 
ATOM   611  O  O   . LEU A 1 89  ? -7.074  -0.567  -43.679  1.00 43.51  ? 81  LEU A O   1 
ATOM   612  C  CB  . LEU A 1 89  ? -6.193  1.985   -42.878  1.00 31.64  ? 81  LEU A CB  1 
ATOM   613  C  CG  . LEU A 1 89  ? -5.766  3.318   -42.269  1.00 38.52  ? 81  LEU A CG  1 
ATOM   614  C  CD1 . LEU A 1 89  ? -6.230  4.441   -43.193  1.00 32.45  ? 81  LEU A CD1 1 
ATOM   615  C  CD2 . LEU A 1 89  ? -6.313  3.491   -40.837  1.00 35.70  ? 81  LEU A CD2 1 
ATOM   616  N  N   . ASP A 1 90  ? -5.019  -1.412  -43.321  1.00 28.48  ? 82  ASP A N   1 
ATOM   617  C  CA  . ASP A 1 90  ? -5.246  -2.557  -44.197  1.00 29.97  ? 82  ASP A CA  1 
ATOM   618  C  C   . ASP A 1 90  ? -6.023  -3.667  -43.481  1.00 26.00  ? 82  ASP A C   1 
ATOM   619  O  O   . ASP A 1 90  ? -5.909  -3.858  -42.261  1.00 27.36  ? 82  ASP A O   1 
ATOM   620  C  CB  . ASP A 1 90  ? -3.911  -3.094  -44.726  1.00 30.59  ? 82  ASP A CB  1 
ATOM   621  C  CG  . ASP A 1 90  ? -4.055  -3.862  -46.052  1.00 37.08  ? 82  ASP A CG  1 
ATOM   622  O  OD1 . ASP A 1 90  ? -5.081  -3.717  -46.756  1.00 36.27  ? 82  ASP A OD1 1 
ATOM   623  O  OD2 . ASP A 1 90  ? -3.115  -4.607  -46.405  1.00 34.62  ? 82  ASP A OD2 1 
ATOM   624  N  N   . ASN A 1 91  ? -6.833  -4.392  -44.265  1.00 29.83  ? 83  ASN A N   1 
ATOM   625  C  CA  . ASN A 1 91  ? -7.614  -5.536  -43.790  1.00 21.61  ? 83  ASN A CA  1 
ATOM   626  C  C   . ASN A 1 91  ? -8.630  -5.134  -42.724  1.00 27.44  ? 83  ASN A C   1 
ATOM   627  O  O   . ASN A 1 91  ? -8.823  -5.840  -41.731  1.00 27.82  ? 83  ASN A O   1 
ATOM   628  C  CB  . ASN A 1 91  ? -6.713  -6.654  -43.269  1.00 30.82  ? 83  ASN A CB  1 
ATOM   629  C  CG  . ASN A 1 91  ? -5.667  -7.067  -44.280  1.00 31.97  ? 83  ASN A CG  1 
ATOM   630  O  OD1 . ASN A 1 91  ? -5.997  -7.433  -45.402  1.00 32.06  ? 83  ASN A OD1 1 
ATOM   631  N  ND2 . ASN A 1 91  ? -4.404  -7.012  -43.889  1.00 27.47  ? 83  ASN A ND2 1 
ATOM   632  N  N   . ASP A 1 92  ? -9.307  -4.007  -42.944  1.00 25.61  ? 84  ASP A N   1 
ATOM   633  C  CA  . ASP A 1 92  ? -10.280 -3.489  -41.983  1.00 23.48  ? 84  ASP A CA  1 
ATOM   634  C  C   . ASP A 1 92  ? -11.619 -4.209  -42.171  1.00 26.62  ? 84  ASP A C   1 
ATOM   635  O  O   . ASP A 1 92  ? -12.575 -3.697  -42.765  1.00 26.75  ? 84  ASP A O   1 
ATOM   636  C  CB  . ASP A 1 92  ? -10.423 -1.984  -42.133  1.00 22.12  ? 84  ASP A CB  1 
ATOM   637  C  CG  . ASP A 1 92  ? -11.202 -1.364  -40.983  1.00 26.80  ? 84  ASP A CG  1 
ATOM   638  O  OD1 . ASP A 1 92  ? -11.247 -1.992  -39.893  1.00 18.07  ? 84  ASP A OD1 1 
ATOM   639  O  OD2 . ASP A 1 92  ? -11.752 -0.246  -41.168  1.00 25.33  ? 84  ASP A OD2 1 
ATOM   640  N  N   . ILE A 1 93  ? -11.687 -5.423  -41.631  1.00 16.72  ? 85  ILE A N   1 
ATOM   641  C  CA  . ILE A 1 93  ? -12.884 -6.243  -41.722  1.00 24.25  ? 85  ILE A CA  1 
ATOM   642  C  C   . ILE A 1 93  ? -12.971 -7.085  -40.455  1.00 24.89  ? 85  ILE A C   1 
ATOM   643  O  O   . ILE A 1 93  ? -11.955 -7.454  -39.857  1.00 25.45  ? 85  ILE A O   1 
ATOM   644  C  CB  . ILE A 1 93  ? -12.872 -7.109  -43.000  1.00 21.21  ? 85  ILE A CB  1 
ATOM   645  C  CG1 . ILE A 1 93  ? -14.229 -7.793  -43.187  1.00 30.77  ? 85  ILE A CG1 1 
ATOM   646  C  CG2 . ILE A 1 93  ? -11.709 -8.097  -42.961  1.00 20.84  ? 85  ILE A CG2 1 
ATOM   647  C  CD1 . ILE A 1 93  ? -14.613 -8.100  -44.639  1.00 25.16  ? 85  ILE A CD1 1 
ATOM   648  N  N   . MET A 1 94  ? -14.199 -7.364  -40.036  1.00 20.13  ? 86  MET A N   1 
ATOM   649  C  CA  . MET A 1 94  ? -14.505 -7.992  -38.754  1.00 21.40  ? 86  MET A CA  1 
ATOM   650  C  C   . MET A 1 94  ? -15.745 -8.863  -38.895  1.00 17.50  ? 86  MET A C   1 
ATOM   651  O  O   . MET A 1 94  ? -16.666 -8.540  -39.650  1.00 21.00  ? 86  MET A O   1 
ATOM   652  C  CB  . MET A 1 94  ? -14.759 -6.949  -37.661  1.00 21.46  ? 86  MET A CB  1 
ATOM   653  C  CG  . MET A 1 94  ? -14.888 -7.488  -36.234  1.00 22.71  ? 86  MET A CG  1 
ATOM   654  S  SD  . MET A 1 94  ? -14.961 -6.163  -34.982  1.00 31.40  ? 86  MET A SD  1 
ATOM   655  C  CE  . MET A 1 94  ? -16.535 -5.356  -35.349  1.00 22.03  ? 86  MET A CE  1 
ATOM   656  N  N   . LEU A 1 95  ? -15.779 -9.952  -38.141  1.00 17.55  ? 87  LEU A N   1 
ATOM   657  C  CA  . LEU A 1 95  ? -16.941 -10.821 -38.095  1.00 16.61  ? 87  LEU A CA  1 
ATOM   658  C  C   . LEU A 1 95  ? -17.484 -10.880 -36.667  1.00 23.29  ? 87  LEU A C   1 
ATOM   659  O  O   . LEU A 1 95  ? -16.711 -10.921 -35.690  1.00 19.34  ? 87  LEU A O   1 
ATOM   660  C  CB  . LEU A 1 95  ? -16.568 -12.209 -38.606  1.00 24.17  ? 87  LEU A CB  1 
ATOM   661  C  CG  . LEU A 1 95  ? -16.473 -12.379 -40.125  1.00 29.38  ? 87  LEU A CG  1 
ATOM   662  C  CD1 . LEU A 1 95  ? -16.130 -13.823 -40.484  1.00 27.78  ? 87  LEU A CD1 1 
ATOM   663  C  CD2 . LEU A 1 95  ? -17.776 -11.973 -40.803  1.00 25.67  ? 87  LEU A CD2 1 
ATOM   664  N  N   . ILE A 1 96  ? -18.815 -10.871 -36.548  1.00 17.94  ? 88  ILE A N   1 
ATOM   665  C  CA  . ILE A 1 96  ? -19.506 -10.940 -35.256  1.00 19.51  ? 88  ILE A CA  1 
ATOM   666  C  C   . ILE A 1 96  ? -20.467 -12.122 -35.258  1.00 22.10  ? 88  ILE A C   1 
ATOM   667  O  O   . ILE A 1 96  ? -21.403 -12.162 -36.064  1.00 19.53  ? 88  ILE A O   1 
ATOM   668  C  CB  . ILE A 1 96  ? -20.271 -9.645  -34.943  1.00 22.50  ? 88  ILE A CB  1 
ATOM   669  C  CG1 . ILE A 1 96  ? -19.296 -8.521  -34.571  1.00 23.56  ? 88  ILE A CG1 1 
ATOM   670  C  CG2 . ILE A 1 96  ? -21.310 -9.883  -33.836  1.00 20.71  ? 88  ILE A CG2 1 
ATOM   671  C  CD1 . ILE A 1 96  ? -19.802 -7.142  -34.909  1.00 24.37  ? 88  ILE A CD1 1 
ATOM   672  N  N   . LYS A 1 97  ? -20.272 -13.058 -34.329  1.00 25.13  ? 89  LYS A N   1 
ATOM   673  C  CA  . LYS A 1 97  ? -21.180 -14.193 -34.179  1.00 28.68  ? 89  LYS A CA  1 
ATOM   674  C  C   . LYS A 1 97  ? -22.262 -13.861 -33.151  1.00 26.77  ? 89  LYS A C   1 
ATOM   675  O  O   . LYS A 1 97  ? -21.961 -13.605 -31.975  1.00 25.67  ? 89  LYS A O   1 
ATOM   676  C  CB  . LYS A 1 97  ? -20.444 -15.479 -33.777  1.00 22.59  ? 89  LYS A CB  1 
ATOM   677  C  CG  . LYS A 1 97  ? -21.397 -16.689 -33.724  1.00 24.04  ? 89  LYS A CG  1 
ATOM   678  C  CD  . LYS A 1 97  ? -20.661 -17.989 -33.656  1.00 29.79  ? 89  LYS A CD  1 
ATOM   679  C  CE  . LYS A 1 97  ? -21.598 -19.193 -33.703  1.00 35.46  ? 89  LYS A CE  1 
ATOM   680  N  NZ  . LYS A 1 97  ? -21.050 -20.353 -32.928  1.00 27.71  ? 89  LYS A NZ  1 
ATOM   681  N  N   . LEU A 1 98  ? -23.517 -13.894 -33.595  1.00 21.88  ? 90  LEU A N   1 
ATOM   682  C  CA  . LEU A 1 98  ? -24.650 -13.628 -32.715  1.00 31.49  ? 90  LEU A CA  1 
ATOM   683  C  C   . LEU A 1 98  ? -24.776 -14.708 -31.650  1.00 29.77  ? 90  LEU A C   1 
ATOM   684  O  O   . LEU A 1 98  ? -24.639 -15.901 -31.935  1.00 36.91  ? 90  LEU A O   1 
ATOM   685  C  CB  . LEU A 1 98  ? -25.930 -13.570 -33.540  1.00 27.05  ? 90  LEU A CB  1 
ATOM   686  C  CG  . LEU A 1 98  ? -25.987 -12.337 -34.425  1.00 21.08  ? 90  LEU A CG  1 
ATOM   687  C  CD1 . LEU A 1 98  ? -27.362 -12.143 -35.002  1.00 25.59  ? 90  LEU A CD1 1 
ATOM   688  C  CD2 . LEU A 1 98  ? -25.624 -11.134 -33.578  1.00 28.02  ? 90  LEU A CD2 1 
ATOM   689  N  N   . SER A 1 99  ? -25.050 -14.290 -30.414  1.00 30.36  ? 91  SER A N   1 
ATOM   690  C  CA  . SER A 1 99  ? -25.225 -15.261 -29.340  1.00 32.86  ? 91  SER A CA  1 
ATOM   691  C  C   . SER A 1 99  ? -26.485 -16.104 -29.516  1.00 35.16  ? 91  SER A C   1 
ATOM   692  O  O   . SER A 1 99  ? -26.638 -17.119 -28.832  1.00 37.35  ? 91  SER A O   1 
ATOM   693  C  CB  . SER A 1 99  ? -25.238 -14.562 -27.981  1.00 25.28  ? 91  SER A CB  1 
ATOM   694  O  OG  . SER A 1 99  ? -26.436 -13.829 -27.797  1.00 44.07  ? 91  SER A OG  1 
ATOM   695  N  N   . SER A 1 100 ? -27.373 -15.727 -30.430  1.00 31.42  ? 92  SER A N   1 
ATOM   696  C  CA  . SER A 1 100 ? -28.511 -16.543 -30.779  1.00 29.25  ? 92  SER A CA  1 
ATOM   697  C  C   . SER A 1 100 ? -28.865 -16.165 -32.206  1.00 32.57  ? 92  SER A C   1 
ATOM   698  O  O   . SER A 1 100 ? -28.726 -14.991 -32.582  1.00 26.39  ? 92  SER A O   1 
ATOM   699  C  CB  . SER A 1 100 ? -29.706 -16.314 -29.847  1.00 36.79  ? 92  SER A CB  1 
ATOM   700  O  OG  . SER A 1 100 ? -30.464 -15.189 -30.270  1.00 45.28  ? 92  SER A OG  1 
ATOM   701  N  N   . PRO A 1 101 ? -29.307 -17.117 -33.020  1.00 33.37  ? 93  PRO A N   1 
ATOM   702  C  CA  . PRO A 1 101 ? -29.621 -16.791 -34.411  1.00 30.47  ? 93  PRO A CA  1 
ATOM   703  C  C   . PRO A 1 101 ? -30.716 -15.735 -34.449  1.00 28.67  ? 93  PRO A C   1 
ATOM   704  O  O   . PRO A 1 101 ? -31.609 -15.703 -33.600  1.00 35.46  ? 93  PRO A O   1 
ATOM   705  C  CB  . PRO A 1 101 ? -30.100 -18.131 -34.987  1.00 35.52  ? 93  PRO A CB  1 
ATOM   706  C  CG  . PRO A 1 101 ? -30.558 -18.896 -33.787  1.00 36.35  ? 93  PRO A CG  1 
ATOM   707  C  CD  . PRO A 1 101 ? -29.617 -18.517 -32.699  1.00 27.63  ? 93  PRO A CD  1 
ATOM   708  N  N   . ALA A 1 102 ? -30.630 -14.851 -35.427  1.00 27.03  ? 94  ALA A N   1 
ATOM   709  C  CA  . ALA A 1 102 ? -31.630 -13.815 -35.578  1.00 27.88  ? 94  ALA A CA  1 
ATOM   710  C  C   . ALA A 1 102 ? -32.838 -14.372 -36.315  1.00 34.22  ? 94  ALA A C   1 
ATOM   711  O  O   . ALA A 1 102 ? -32.721 -15.307 -37.109  1.00 34.63  ? 94  ALA A O   1 
ATOM   712  C  CB  . ALA A 1 102 ? -31.051 -12.624 -36.341  1.00 30.19  ? 94  ALA A CB  1 
ATOM   713  N  N   . THR A 1 103 ? -34.005 -13.793 -36.048  1.00 31.62  ? 95  THR A N   1 
ATOM   714  C  CA  . THR A 1 103 ? -35.221 -14.173 -36.765  1.00 31.26  ? 95  THR A CA  1 
ATOM   715  C  C   . THR A 1 103 ? -35.273 -13.446 -38.109  1.00 35.00  ? 95  THR A C   1 
ATOM   716  O  O   . THR A 1 103 ? -35.296 -12.212 -38.147  1.00 36.77  ? 95  THR A O   1 
ATOM   717  C  CB  . THR A 1 103 ? -36.450 -13.830 -35.925  1.00 33.99  ? 95  THR A CB  1 
ATOM   718  O  OG1 . THR A 1 103 ? -36.391 -14.528 -34.678  1.00 42.52  ? 95  THR A OG1 1 
ATOM   719  C  CG2 . THR A 1 103 ? -37.723 -14.209 -36.647  1.00 21.62  ? 95  THR A CG2 1 
ATOM   720  N  N   . LEU A 1 104 ? -35.302 -14.186 -39.214  1.00 29.45  ? 96  LEU A N   1 
ATOM   721  C  CA  . LEU A 1 104 ? -35.358 -13.541 -40.526  1.00 28.63  ? 96  LEU A CA  1 
ATOM   722  C  C   . LEU A 1 104 ? -36.805 -13.314 -40.941  1.00 35.87  ? 96  LEU A C   1 
ATOM   723  O  O   . LEU A 1 104 ? -37.613 -14.245 -40.917  1.00 46.55  ? 96  LEU A O   1 
ATOM   724  C  CB  . LEU A 1 104 ? -34.648 -14.379 -41.584  1.00 24.21  ? 96  LEU A CB  1 
ATOM   725  C  CG  . LEU A 1 104 ? -33.214 -14.815 -41.276  1.00 35.42  ? 96  LEU A CG  1 
ATOM   726  C  CD1 . LEU A 1 104 ? -32.646 -15.446 -42.514  1.00 21.82  ? 96  LEU A CD1 1 
ATOM   727  C  CD2 . LEU A 1 104 ? -32.290 -13.685 -40.756  1.00 22.68  ? 96  LEU A CD2 1 
ATOM   728  N  N   . ASN A 1 105 ? -37.119 -12.084 -41.330  1.00 29.76  ? 97  ASN A N   1 
ATOM   729  C  CA  . ASN A 1 105 ? -38.448 -11.691 -41.784  1.00 31.26  ? 97  ASN A CA  1 
ATOM   730  C  C   . ASN A 1 105 ? -38.276 -10.480 -42.698  1.00 38.05  ? 97  ASN A C   1 
ATOM   731  O  O   . ASN A 1 105 ? -37.169 -10.192 -43.165  1.00 35.35  ? 97  ASN A O   1 
ATOM   732  C  CB  . ASN A 1 105 ? -39.362 -11.376 -40.589  1.00 33.10  ? 97  ASN A CB  1 
ATOM   733  C  CG  . ASN A 1 105 ? -38.631 -10.614 -39.503  1.00 43.53  ? 97  ASN A CG  1 
ATOM   734  O  OD1 . ASN A 1 105 ? -38.082 -9.539  -39.760  1.00 45.78  ? 97  ASN A OD1 1 
ATOM   735  N  ND2 . ASN A 1 105 ? -38.640 -11.141 -38.281  1.00 40.79  ? 97  ASN A ND2 1 
ATOM   736  N  N   . SER A 1 106 ? -39.358 -9.729  -42.919  1.00 38.93  ? 98  SER A N   1 
ATOM   737  C  CA  . SER A 1 106 ? -39.293 -8.619  -43.871  1.00 37.71  ? 98  SER A CA  1 
ATOM   738  C  C   . SER A 1 106 ? -38.381 -7.488  -43.389  1.00 46.64  ? 98  SER A C   1 
ATOM   739  O  O   . SER A 1 106 ? -37.800 -6.771  -44.215  1.00 36.65  ? 98  SER A O   1 
ATOM   740  C  CB  . SER A 1 106 ? -40.701 -8.095  -44.148  1.00 41.64  ? 98  SER A CB  1 
ATOM   741  O  OG  . SER A 1 106 ? -41.432 -7.952  -42.937  1.00 49.05  ? 98  SER A OG  1 
ATOM   742  N  N   . ARG A 1 107 ? -38.229 -7.327  -42.066  1.00 41.78  ? 99  ARG A N   1 
ATOM   743  C  CA  . ARG A 1 107 ? -37.432 -6.261  -41.458  1.00 38.04  ? 99  ARG A CA  1 
ATOM   744  C  C   . ARG A 1 107 ? -35.974 -6.657  -41.217  1.00 36.37  ? 99  ARG A C   1 
ATOM   745  O  O   . ARG A 1 107 ? -35.130 -5.775  -41.012  1.00 39.25  ? 99  ARG A O   1 
ATOM   746  C  CB  . ARG A 1 107 ? -38.090 -5.838  -40.129  1.00 35.39  ? 99  ARG A CB  1 
ATOM   747  C  CG  . ARG A 1 107 ? -37.701 -4.466  -39.565  1.00 49.13  ? 99  ARG A CG  1 
ATOM   748  C  CD  . ARG A 1 107 ? -38.647 -4.026  -38.415  1.00 52.10  ? 99  ARG A CD  1 
ATOM   749  N  NE  . ARG A 1 107 ? -38.340 -2.701  -37.869  1.00 61.95  ? 99  ARG A NE  1 
ATOM   750  C  CZ  . ARG A 1 107 ? -38.739 -2.253  -36.678  1.00 59.30  ? 99  ARG A CZ  1 
ATOM   751  N  NH1 . ARG A 1 107 ? -39.503 -2.986  -35.883  1.00 53.04  ? 99  ARG A NH1 1 
ATOM   752  N  NH2 . ARG A 1 107 ? -38.362 -1.035  -36.276  1.00 44.31  ? 99  ARG A NH2 1 
ATOM   753  N  N   . VAL A 1 108 ? -35.667 -7.956  -41.229  1.00 28.29  ? 100 VAL A N   1 
ATOM   754  C  CA  . VAL A 1 108 ? -34.352 -8.505  -40.906  1.00 23.70  ? 100 VAL A CA  1 
ATOM   755  C  C   . VAL A 1 108 ? -34.056 -9.587  -41.936  1.00 27.62  ? 100 VAL A C   1 
ATOM   756  O  O   . VAL A 1 108 ? -34.738 -10.615 -41.965  1.00 25.31  ? 100 VAL A O   1 
ATOM   757  C  CB  . VAL A 1 108 ? -34.298 -9.097  -39.487  1.00 29.82  ? 100 VAL A CB  1 
ATOM   758  C  CG1 . VAL A 1 108 ? -32.899 -9.623  -39.175  1.00 22.31  ? 100 VAL A CG1 1 
ATOM   759  C  CG2 . VAL A 1 108 ? -34.741 -8.067  -38.441  1.00 25.94  ? 100 VAL A CG2 1 
ATOM   760  N  N   . ALA A 1 109 ? -33.040 -9.374  -42.765  1.00 25.86  ? 101 ALA A N   1 
ATOM   761  C  CA  . ALA A 1 109 ? -32.734 -10.313 -43.833  1.00 24.48  ? 101 ALA A CA  1 
ATOM   762  C  C   . ALA A 1 109 ? -31.240 -10.258 -44.117  1.00 26.26  ? 101 ALA A C   1 
ATOM   763  O  O   . ALA A 1 109 ? -30.526 -9.385  -43.626  1.00 23.70  ? 101 ALA A O   1 
ATOM   764  C  CB  . ALA A 1 109 ? -33.552 -10.010 -45.094  1.00 12.37  ? 101 ALA A CB  1 
ATOM   765  N  N   . THR A 1 110 ? -30.760 -11.214 -44.900  1.00 23.98  ? 102 THR A N   1 
ATOM   766  C  CA  . THR A 1 110 ? -29.335 -11.292 -45.153  1.00 19.70  ? 102 THR A CA  1 
ATOM   767  C  C   . THR A 1 110 ? -29.021 -10.682 -46.512  1.00 23.31  ? 102 THR A C   1 
ATOM   768  O  O   . THR A 1 110 ? -29.874 -10.619 -47.397  1.00 24.22  ? 102 THR A O   1 
ATOM   769  C  CB  . THR A 1 110 ? -28.835 -12.742 -45.096  1.00 28.94  ? 102 THR A CB  1 
ATOM   770  O  OG1 . THR A 1 110 ? -29.385 -13.482 -46.189  1.00 28.02  ? 102 THR A OG1 1 
ATOM   771  C  CG2 . THR A 1 110 ? -29.238 -13.406 -43.767  1.00 25.44  ? 102 THR A CG2 1 
ATOM   772  N  N   . VAL A 1 111 ? -27.782 -10.218 -46.662  1.00 19.52  ? 103 VAL A N   1 
ATOM   773  C  CA  . VAL A 1 111 ? -27.270 -9.739  -47.937  1.00 21.61  ? 103 VAL A CA  1 
ATOM   774  C  C   . VAL A 1 111 ? -26.203 -10.710 -48.417  1.00 20.56  ? 103 VAL A C   1 
ATOM   775  O  O   . VAL A 1 111 ? -25.410 -11.222 -47.621  1.00 30.64  ? 103 VAL A O   1 
ATOM   776  C  CB  . VAL A 1 111 ? -26.713 -8.298  -47.845  1.00 26.44  ? 103 VAL A CB  1 
ATOM   777  C  CG1 . VAL A 1 111 ? -25.602 -8.189  -46.792  1.00 20.89  ? 103 VAL A CG1 1 
ATOM   778  C  CG2 . VAL A 1 111 ? -26.201 -7.846  -49.207  1.00 24.92  ? 103 VAL A CG2 1 
ATOM   779  N  N   . SER A 1 112 ? -26.183 -10.963 -49.716  1.00 25.30  ? 104 SER A N   1 
ATOM   780  C  CA  . SER A 1 112 ? -25.231 -11.903 -50.283  1.00 27.38  ? 104 SER A CA  1 
ATOM   781  C  C   . SER A 1 112 ? -23.812 -11.331 -50.332  1.00 30.10  ? 104 SER A C   1 
ATOM   782  O  O   . SER A 1 112 ? -23.608 -10.133 -50.557  1.00 28.42  ? 104 SER A O   1 
ATOM   783  C  CB  . SER A 1 112 ? -25.683 -12.291 -51.681  1.00 33.60  ? 104 SER A CB  1 
ATOM   784  O  OG  . SER A 1 112 ? -24.562 -12.637 -52.465  1.00 44.81  ? 104 SER A OG  1 
ATOM   785  N  N   . LEU A 1 113 ? -22.830 -12.211 -50.121  1.00 23.81  ? 105 LEU A N   1 
ATOM   786  C  CA  . LEU A 1 113 ? -21.422 -11.912 -50.353  1.00 28.47  ? 105 LEU A CA  1 
ATOM   787  C  C   . LEU A 1 113 ? -21.150 -11.805 -51.857  1.00 33.17  ? 105 LEU A C   1 
ATOM   788  O  O   . LEU A 1 113 ? -21.908 -12.347 -52.669  1.00 28.16  ? 105 LEU A O   1 
ATOM   789  C  CB  . LEU A 1 113 ? -20.557 -13.016 -49.743  1.00 29.09  ? 105 LEU A CB  1 
ATOM   790  C  CG  . LEU A 1 113 ? -20.397 -12.978 -48.219  1.00 32.02  ? 105 LEU A CG  1 
ATOM   791  C  CD1 . LEU A 1 113 ? -19.410 -14.053 -47.735  1.00 25.59  ? 105 LEU A CD1 1 
ATOM   792  C  CD2 . LEU A 1 113 ? -19.981 -11.593 -47.735  1.00 21.23  ? 105 LEU A CD2 1 
ATOM   793  N  N   . PRO A 1 114 ? -20.063 -11.126 -52.257  1.00 38.91  ? 106 PRO A N   1 
ATOM   794  C  CA  . PRO A 1 114 ? -19.798 -10.952 -53.694  1.00 30.72  ? 106 PRO A CA  1 
ATOM   795  C  C   . PRO A 1 114 ? -19.450 -12.275 -54.340  1.00 30.72  ? 106 PRO A C   1 
ATOM   796  O  O   . PRO A 1 114 ? -18.728 -13.092 -53.767  1.00 34.64  ? 106 PRO A O   1 
ATOM   797  C  CB  . PRO A 1 114 ? -18.580 -10.015 -53.735  1.00 24.35  ? 106 PRO A CB  1 
ATOM   798  C  CG  . PRO A 1 114 ? -18.441 -9.479  -52.364  1.00 28.42  ? 106 PRO A CG  1 
ATOM   799  C  CD  . PRO A 1 114 ? -18.973 -10.548 -51.451  1.00 33.34  ? 106 PRO A CD  1 
ATOM   800  N  N   . ARG A 1 115 ? -19.939 -12.475 -55.550  1.00 32.13  ? 107 ARG A N   1 
ATOM   801  C  CA  . ARG A 1 115 ? -19.448 -13.588 -56.341  1.00 42.91  ? 107 ARG A CA  1 
ATOM   802  C  C   . ARG A 1 115 ? -18.486 -13.130 -57.428  1.00 42.15  ? 107 ARG A C   1 
ATOM   803  O  O   . ARG A 1 115 ? -17.918 -13.972 -58.139  1.00 39.36  ? 107 ARG A O   1 
ATOM   804  C  CB  . ARG A 1 115 ? -20.615 -14.385 -56.934  1.00 47.12  ? 107 ARG A CB  1 
ATOM   805  C  CG  . ARG A 1 115 ? -21.927 -14.278 -56.168  1.00 40.66  ? 107 ARG A CG  1 
ATOM   806  C  CD  . ARG A 1 115 ? -22.986 -15.136 -56.832  1.00 49.89  ? 107 ARG A CD  1 
ATOM   807  N  NE  . ARG A 1 115 ? -23.529 -14.313 -57.889  1.00 57.63  ? 107 ARG A NE  1 
ATOM   808  C  CZ  . ARG A 1 115 ? -24.514 -13.449 -57.728  1.00 61.59  ? 107 ARG A CZ  1 
ATOM   809  N  NH1 . ARG A 1 115 ? -25.204 -13.388 -56.596  1.00 58.42  ? 107 ARG A NH1 1 
ATOM   810  N  NH2 . ARG A 1 115 ? -24.768 -12.589 -58.704  1.00 61.64  ? 107 ARG A NH2 1 
ATOM   811  N  N   . SER A 1 116 ? -18.290 -11.820 -57.564  1.00 25.48  ? 108 SER A N   1 
ATOM   812  C  CA  . SER A 1 116 ? -17.160 -11.266 -58.289  1.00 32.43  ? 108 SER A CA  1 
ATOM   813  C  C   . SER A 1 116 ? -16.864 -9.911  -57.678  1.00 34.07  ? 108 SER A C   1 
ATOM   814  O  O   . SER A 1 116 ? -17.639 -9.397  -56.875  1.00 32.87  ? 108 SER A O   1 
ATOM   815  C  CB  . SER A 1 116 ? -17.434 -11.120 -59.790  1.00 19.31  ? 108 SER A CB  1 
ATOM   816  O  OG  . SER A 1 116 ? -18.362 -10.076 -60.031  1.00 42.46  ? 108 SER A OG  1 
ATOM   817  N  N   . CYS A 1 117 ? -15.735 -9.327  -58.066  1.00 37.34  ? 109 CYS A N   1 
ATOM   818  C  CA  . CYS A 1 117 ? -15.498 -7.951  -57.669  1.00 35.86  ? 109 CYS A CA  1 
ATOM   819  C  C   . CYS A 1 117 ? -16.353 -7.027  -58.531  1.00 34.34  ? 109 CYS A C   1 
ATOM   820  O  O   . CYS A 1 117 ? -16.793 -7.389  -59.624  1.00 39.46  ? 109 CYS A O   1 
ATOM   821  C  CB  . CYS A 1 117 ? -14.005 -7.604  -57.775  1.00 28.75  ? 109 CYS A CB  1 
ATOM   822  S  SG  . CYS A 1 117 ? -12.968 -8.530  -56.574  1.00 56.35  ? 109 CYS A SG  1 
ATOM   823  N  N   . ALA A 1 118 ? -16.621 -5.837  -58.010  1.00 36.14  ? 110 ALA A N   1 
ATOM   824  C  CA  . ALA A 1 118 ? -17.499 -4.891  -58.678  1.00 25.75  ? 110 ALA A CA  1 
ATOM   825  C  C   . ALA A 1 118 ? -16.678 -3.950  -59.544  1.00 33.76  ? 110 ALA A C   1 
ATOM   826  O  O   . ALA A 1 118 ? -15.711 -3.337  -59.074  1.00 37.44  ? 110 ALA A O   1 
ATOM   827  C  CB  . ALA A 1 118 ? -18.316 -4.094  -57.664  1.00 28.58  ? 110 ALA A CB  1 
ATOM   828  N  N   . ALA A 1 119 ? -17.063 -3.853  -60.810  1.00 30.26  ? 111 ALA A N   1 
ATOM   829  C  CA  . ALA A 1 119 ? -16.398 -2.962  -61.744  1.00 23.58  ? 111 ALA A CA  1 
ATOM   830  C  C   . ALA A 1 119 ? -16.613 -1.510  -61.343  1.00 25.89  ? 111 ALA A C   1 
ATOM   831  O  O   . ALA A 1 119 ? -17.649 -1.140  -60.780  1.00 32.23  ? 111 ALA A O   1 
ATOM   832  C  CB  . ALA A 1 119 ? -16.931 -3.173  -63.163  1.00 16.53  ? 111 ALA A CB  1 
ATOM   833  N  N   . ALA A 1 120 ? -15.621 -0.684  -61.662  1.00 21.62  ? 112 ALA A N   1 
ATOM   834  C  CA  . ALA A 1 120 ? -15.765 0.761   -61.552  1.00 30.29  ? 112 ALA A CA  1 
ATOM   835  C  C   . ALA A 1 120 ? -16.986 1.237   -62.337  1.00 24.93  ? 112 ALA A C   1 
ATOM   836  O  O   . ALA A 1 120 ? -17.292 0.728   -63.418  1.00 30.72  ? 112 ALA A O   1 
ATOM   837  C  CB  . ALA A 1 120 ? -14.489 1.452   -62.058  1.00 26.65  ? 112 ALA A CB  1 
ATOM   838  N  N   . GLY A 1 121 ? -17.694 2.209   -61.781  1.00 24.76  ? 113 GLY A N   1 
ATOM   839  C  CA  . GLY A 1 121 ? -18.889 2.738   -62.391  1.00 18.71  ? 113 GLY A CA  1 
ATOM   840  C  C   . GLY A 1 121 ? -20.168 2.095   -61.907  1.00 25.43  ? 113 GLY A C   1 
ATOM   841  O  O   . GLY A 1 121 ? -21.242 2.682   -62.086  1.00 29.45  ? 113 GLY A O   1 
ATOM   842  N  N   . THR A 1 122 ? -20.076 0.912   -61.291  1.00 26.49  ? 114 THR A N   1 
ATOM   843  C  CA  . THR A 1 122 ? -21.244 0.222   -60.742  1.00 26.47  ? 114 THR A CA  1 
ATOM   844  C  C   . THR A 1 122 ? -21.934 1.039   -59.653  1.00 30.30  ? 114 THR A C   1 
ATOM   845  O  O   . THR A 1 122 ? -21.305 1.463   -58.678  1.00 28.67  ? 114 THR A O   1 
ATOM   846  C  CB  . THR A 1 122 ? -20.821 -1.121  -60.146  1.00 27.59  ? 114 THR A CB  1 
ATOM   847  O  OG1 . THR A 1 122 ? -19.899 -1.779  -61.028  1.00 35.08  ? 114 THR A OG1 1 
ATOM   848  C  CG2 . THR A 1 122 ? -22.034 -2.002  -59.880  1.00 21.86  ? 114 THR A CG2 1 
ATOM   849  N  N   . GLU A 1 123 ? -23.240 1.213   -59.784  1.00 25.57  ? 115 GLU A N   1 
ATOM   850  C  CA  . GLU A 1 123 ? -23.992 1.917   -58.757  1.00 31.47  ? 115 GLU A CA  1 
ATOM   851  C  C   . GLU A 1 123 ? -24.179 1.037   -57.517  1.00 31.17  ? 115 GLU A C   1 
ATOM   852  O  O   . GLU A 1 123 ? -24.663 -0.096  -57.618  1.00 25.65  ? 115 GLU A O   1 
ATOM   853  C  CB  . GLU A 1 123 ? -25.336 2.342   -59.318  1.00 29.31  ? 115 GLU A CB  1 
ATOM   854  C  CG  . GLU A 1 123 ? -26.365 2.661   -58.295  1.00 33.35  ? 115 GLU A CG  1 
ATOM   855  C  CD  . GLU A 1 123 ? -27.433 3.559   -58.855  1.00 34.40  ? 115 GLU A CD  1 
ATOM   856  O  OE1 . GLU A 1 123 ? -28.628 3.236   -58.694  1.00 49.50  ? 115 GLU A OE1 1 
ATOM   857  O  OE2 . GLU A 1 123 ? -27.072 4.592   -59.466  1.00 51.24  ? 115 GLU A OE2 1 
ATOM   858  N  N   . CYS A 1 124 ? -23.796 1.564   -56.348  1.00 21.23  ? 116 CYS A N   1 
ATOM   859  C  CA  . CYS A 1 124 ? -23.973 0.889   -55.071  1.00 23.68  ? 116 CYS A CA  1 
ATOM   860  C  C   . CYS A 1 124 ? -24.860 1.700   -54.124  1.00 16.36  ? 116 CYS A C   1 
ATOM   861  O  O   . CYS A 1 124 ? -25.005 2.916   -54.252  1.00 20.22  ? 116 CYS A O   1 
ATOM   862  C  CB  . CYS A 1 124 ? -22.630 0.671   -54.381  1.00 36.93  ? 116 CYS A CB  1 
ATOM   863  S  SG  . CYS A 1 124 ? -21.354 -0.071  -55.392  1.00 40.65  ? 116 CYS A SG  1 
ATOM   864  N  N   . LEU A 1 125 ? -25.395 1.022   -53.122  1.00 19.24  ? 117 LEU A N   1 
ATOM   865  C  CA  . LEU A 1 125 ? -26.161 1.649   -52.051  1.00 22.95  ? 117 LEU A CA  1 
ATOM   866  C  C   . LEU A 1 125 ? -25.369 1.573   -50.748  1.00 24.49  ? 117 LEU A C   1 
ATOM   867  O  O   . LEU A 1 125 ? -25.038 0.476   -50.277  1.00 25.74  ? 117 LEU A O   1 
ATOM   868  C  CB  . LEU A 1 125 ? -27.516 0.970   -51.877  1.00 20.16  ? 117 LEU A CB  1 
ATOM   869  C  CG  . LEU A 1 125 ? -28.415 1.508   -50.772  1.00 22.63  ? 117 LEU A CG  1 
ATOM   870  C  CD1 . LEU A 1 125 ? -29.006 2.848   -51.171  1.00 22.78  ? 117 LEU A CD1 1 
ATOM   871  C  CD2 . LEU A 1 125 ? -29.487 0.502   -50.467  1.00 26.41  ? 117 LEU A CD2 1 
ATOM   872  N  N   . ILE A 1 126 ? -25.069 2.742   -50.177  1.00 23.42  ? 118 ILE A N   1 
ATOM   873  C  CA  . ILE A 1 126 ? -24.439 2.901   -48.872  1.00 21.15  ? 118 ILE A CA  1 
ATOM   874  C  C   . ILE A 1 126 ? -25.494 3.326   -47.867  1.00 27.36  ? 118 ILE A C   1 
ATOM   875  O  O   . ILE A 1 126 ? -26.390 4.113   -48.192  1.00 28.76  ? 118 ILE A O   1 
ATOM   876  C  CB  . ILE A 1 126 ? -23.329 3.963   -48.949  1.00 24.85  ? 118 ILE A CB  1 
ATOM   877  C  CG1 . ILE A 1 126 ? -22.478 3.716   -50.192  1.00 32.34  ? 118 ILE A CG1 1 
ATOM   878  C  CG2 . ILE A 1 126 ? -22.539 3.990   -47.661  1.00 13.56  ? 118 ILE A CG2 1 
ATOM   879  C  CD1 . ILE A 1 126 ? -21.803 4.938   -50.721  1.00 29.73  ? 118 ILE A CD1 1 
ATOM   880  N  N   . SER A 1 127 ? -25.368 2.859   -46.621  1.00 25.69  ? 119 SER A N   1 
ATOM   881  C  CA  . SER A 1 127 ? -26.363 3.182   -45.605  1.00 24.05  ? 119 SER A CA  1 
ATOM   882  C  C   . SER A 1 127 ? -25.718 3.211   -44.226  1.00 25.48  ? 119 SER A C   1 
ATOM   883  O  O   . SER A 1 127 ? -24.735 2.510   -43.964  1.00 24.63  ? 119 SER A O   1 
ATOM   884  C  CB  . SER A 1 127 ? -27.524 2.175   -45.609  1.00 15.95  ? 119 SER A CB  1 
ATOM   885  O  OG  . SER A 1 127 ? -27.008 0.863   -45.730  1.00 21.96  ? 119 SER A OG  1 
ATOM   886  N  N   . GLY A 1 128 ? -26.295 4.020   -43.344  1.00 21.25  ? 120 GLY A N   1 
ATOM   887  C  CA  . GLY A 1 128 ? -25.801 4.127   -41.989  1.00 15.14  ? 120 GLY A CA  1 
ATOM   888  C  C   . GLY A 1 128 ? -26.412 5.319   -41.274  1.00 22.37  ? 120 GLY A C   1 
ATOM   889  O  O   . GLY A 1 128 ? -27.196 6.092   -41.834  1.00 16.67  ? 120 GLY A O   1 
ATOM   890  N  N   . TRP A 1 129 ? -26.008 5.462   -40.015  1.00 15.10  ? 121 TRP A N   1 
ATOM   891  C  CA  . TRP A 1 129 ? -26.569 6.450   -39.112  1.00 15.15  ? 121 TRP A CA  1 
ATOM   892  C  C   . TRP A 1 129 ? -25.549 7.534   -38.753  1.00 21.33  ? 121 TRP A C   1 
ATOM   893  O  O   . TRP A 1 129 ? -25.724 8.245   -37.762  1.00 16.12  ? 121 TRP A O   1 
ATOM   894  C  CB  . TRP A 1 129 ? -27.091 5.751   -37.853  1.00 17.66  ? 121 TRP A CB  1 
ATOM   895  C  CG  . TRP A 1 129 ? -28.437 5.020   -37.987  1.00 22.72  ? 121 TRP A CG  1 
ATOM   896  C  CD1 . TRP A 1 129 ? -29.695 5.575   -37.952  1.00 19.82  ? 121 TRP A CD1 1 
ATOM   897  C  CD2 . TRP A 1 129 ? -28.632 3.605   -38.165  1.00 20.40  ? 121 TRP A CD2 1 
ATOM   898  N  NE1 . TRP A 1 129 ? -30.647 4.589   -38.082  1.00 21.21  ? 121 TRP A NE1 1 
ATOM   899  C  CE2 . TRP A 1 129 ? -30.022 3.376   -38.225  1.00 19.63  ? 121 TRP A CE2 1 
ATOM   900  C  CE3 . TRP A 1 129 ? -27.763 2.507   -38.249  1.00 18.31  ? 121 TRP A CE3 1 
ATOM   901  C  CZ2 . TRP A 1 129 ? -30.564 2.097   -38.384  1.00 23.23  ? 121 TRP A CZ2 1 
ATOM   902  C  CZ3 . TRP A 1 129 ? -28.311 1.236   -38.395  1.00 23.50  ? 121 TRP A CZ3 1 
ATOM   903  C  CH2 . TRP A 1 129 ? -29.695 1.046   -38.470  1.00 17.51  ? 121 TRP A CH2 1 
ATOM   904  N  N   . GLY A 1 130 ? -24.496 7.686   -39.546  1.00 14.93  ? 122 GLY A N   1 
ATOM   905  C  CA  . GLY A 1 130 ? -23.461 8.630   -39.208  1.00 19.52  ? 122 GLY A CA  1 
ATOM   906  C  C   . GLY A 1 130 ? -23.847 10.066  -39.524  1.00 18.39  ? 122 GLY A C   1 
ATOM   907  O  O   . GLY A 1 130 ? -24.980 10.402  -39.853  1.00 21.99  ? 122 GLY A O   1 
ATOM   908  N  N   . ASN A 1 131 ? -22.847 10.924  -39.440  1.00 25.76  ? 123 ASN A N   1 
ATOM   909  C  CA  . ASN A 1 131 ? -23.067 12.352  -39.587  1.00 29.07  ? 123 ASN A CA  1 
ATOM   910  C  C   . ASN A 1 131 ? -23.646 12.689  -40.953  1.00 24.27  ? 123 ASN A C   1 
ATOM   911  O  O   . ASN A 1 131 ? -23.302 12.072  -41.959  1.00 21.37  ? 123 ASN A O   1 
ATOM   912  C  CB  . ASN A 1 131 ? -21.753 13.090  -39.379  1.00 26.31  ? 123 ASN A CB  1 
ATOM   913  C  CG  . ASN A 1 131 ? -21.960 14.515  -38.957  1.00 37.98  ? 123 ASN A CG  1 
ATOM   914  O  OD1 . ASN A 1 131 ? -23.033 15.087  -39.174  1.00 36.40  ? 123 ASN A OD1 1 
ATOM   915  N  ND2 . ASN A 1 131 ? -20.942 15.103  -38.341  1.00 37.32  ? 123 ASN A ND2 1 
ATOM   916  N  N   . THR A 1 132 ? -24.531 13.683  -40.975  1.00 29.37  ? 124 THR A N   1 
ATOM   917  C  CA  . THR A 1 132 ? -25.081 14.229  -42.207  1.00 28.13  ? 124 THR A CA  1 
ATOM   918  C  C   . THR A 1 132 ? -24.542 15.611  -42.554  1.00 28.82  ? 124 THR A C   1 
ATOM   919  O  O   . THR A 1 132 ? -24.988 16.188  -43.547  1.00 27.57  ? 124 THR A O   1 
ATOM   920  C  CB  . THR A 1 132 ? -26.602 14.310  -42.115  1.00 23.01  ? 124 THR A CB  1 
ATOM   921  O  OG1 . THR A 1 132 ? -26.939 15.328  -41.173  1.00 29.57  ? 124 THR A OG1 1 
ATOM   922  C  CG2 . THR A 1 132 ? -27.173 12.979  -41.635  1.00 17.54  ? 124 THR A CG2 1 
ATOM   923  N  N   . LYS A 1 133 ? -23.633 16.177  -41.756  1.00 27.93  ? 125 LYS A N   1 
ATOM   924  C  CA  . LYS A 1 133 ? -23.045 17.480  -42.058  1.00 33.76  ? 125 LYS A CA  1 
ATOM   925  C  C   . LYS A 1 133 ? -21.616 17.326  -42.564  1.00 40.90  ? 125 LYS A C   1 
ATOM   926  O  O   . LYS A 1 133 ? -20.836 16.521  -42.033  1.00 35.53  ? 125 LYS A O   1 
ATOM   927  C  CB  . LYS A 1 133 ? -23.036 18.412  -40.844  1.00 40.01  ? 125 LYS A CB  1 
ATOM   928  C  CG  . LYS A 1 133 ? -24.399 18.709  -40.256  1.00 44.86  ? 125 LYS A CG  1 
ATOM   929  C  CD  . LYS A 1 133 ? -25.346 19.342  -41.266  1.00 48.74  ? 125 LYS A CD  1 
ATOM   930  C  CE  . LYS A 1 133 ? -25.435 20.855  -41.086  1.00 54.24  ? 125 LYS A CE  1 
ATOM   931  N  NZ  . LYS A 1 133 ? -25.400 21.235  -39.645  1.00 54.13  ? 125 LYS A NZ  1 
ATOM   932  N  N   . SER A 1 134 ? -21.282 18.119  -43.596  1.00 34.07  ? 126 SER A N   1 
ATOM   933  C  CA  . SER A 1 134 ? -19.910 18.174  -44.097  1.00 41.77  ? 126 SER A CA  1 
ATOM   934  C  C   . SER A 1 134 ? -18.968 18.829  -43.094  1.00 55.65  ? 126 SER A C   1 
ATOM   935  O  O   . SER A 1 134 ? -17.769 18.522  -43.093  1.00 59.78  ? 126 SER A O   1 
ATOM   936  C  CB  . SER A 1 134 ? -19.856 18.919  -45.441  1.00 41.12  ? 126 SER A CB  1 
ATOM   937  O  OG  . SER A 1 134 ? -20.796 19.982  -45.498  1.00 52.68  ? 126 SER A OG  1 
ATOM   938  N  N   . SER A 1 135 ? -19.485 19.711  -42.228  1.00 46.29  ? 127 SER A N   1 
ATOM   939  C  CA  . SER A 1 135 ? -18.643 20.435  -41.286  1.00 50.79  ? 127 SER A CA  1 
ATOM   940  C  C   . SER A 1 135 ? -19.081 20.267  -39.828  1.00 61.35  ? 127 SER A C   1 
ATOM   941  O  O   . SER A 1 135 ? -18.312 19.761  -39.003  1.00 63.20  ? 127 SER A O   1 
ATOM   942  C  CB  . SER A 1 135 ? -18.611 21.916  -41.663  1.00 56.97  ? 127 SER A CB  1 
ATOM   943  O  OG  . SER A 1 135 ? -17.542 22.577  -41.010  1.00 57.20  ? 127 SER A OG  1 
ATOM   944  N  N   . GLY A 1 136 ? -20.293 20.698  -39.482  1.00 51.74  ? 128 GLY A N   1 
ATOM   945  C  CA  . GLY A 1 136 ? -20.742 20.580  -38.103  1.00 51.37  ? 128 GLY A CA  1 
ATOM   946  C  C   . GLY A 1 136 ? -21.030 19.162  -37.634  1.00 52.40  ? 128 GLY A C   1 
ATOM   947  O  O   . GLY A 1 136 ? -20.222 18.252  -37.844  1.00 53.02  ? 128 GLY A O   1 
ATOM   948  N  N   . SER A 1 137 ? -22.182 18.958  -36.996  1.00 50.58  ? 129 SER A N   1 
ATOM   949  C  CA  . SER A 1 137 ? -22.544 17.657  -36.438  1.00 36.85  ? 129 SER A CA  1 
ATOM   950  C  C   . SER A 1 137 ? -24.060 17.537  -36.416  1.00 42.34  ? 129 SER A C   1 
ATOM   951  O  O   . SER A 1 137 ? -24.732 18.342  -35.765  1.00 48.56  ? 129 SER A O   1 
ATOM   952  C  CB  . SER A 1 137 ? -21.957 17.495  -35.035  1.00 42.54  ? 129 SER A CB  1 
ATOM   953  O  OG  . SER A 1 137 ? -22.798 16.736  -34.176  1.00 50.38  ? 129 SER A OG  1 
ATOM   954  N  N   . SER A 1 138 ? -24.596 16.537  -37.128  1.00 35.70  ? 130 SER A N   1 
ATOM   955  C  CA  . SER A 1 138 ? -26.049 16.334  -37.239  1.00 33.69  ? 130 SER A CA  1 
ATOM   956  C  C   . SER A 1 138 ? -26.301 14.859  -37.540  1.00 29.88  ? 130 SER A C   1 
ATOM   957  O  O   . SER A 1 138 ? -26.432 14.468  -38.701  1.00 33.90  ? 130 SER A O   1 
ATOM   958  C  CB  . SER A 1 138 ? -26.674 17.210  -38.312  1.00 39.36  ? 130 SER A CB  1 
ATOM   959  O  OG  . SER A 1 138 ? -28.068 16.987  -38.388  1.00 44.21  ? 130 SER A OG  1 
ATOM   960  N  N   . TYR A 1 139 ? -26.413 14.085  -36.502  1.00 28.05  ? 131 TYR A N   1 
ATOM   961  C  CA  . TYR A 1 139 ? -26.584 12.648  -36.563  1.00 24.46  ? 131 TYR A CA  1 
ATOM   962  C  C   . TYR A 1 139 ? -28.058 12.304  -36.566  1.00 29.50  ? 131 TYR A C   1 
ATOM   963  O  O   . TYR A 1 139 ? -28.795 12.768  -35.694  1.00 29.77  ? 131 TYR A O   1 
ATOM   964  C  CB  . TYR A 1 139 ? -25.914 11.968  -35.388  1.00 25.38  ? 131 TYR A CB  1 
ATOM   965  C  CG  . TYR A 1 139 ? -24.421 11.991  -35.486  1.00 31.22  ? 131 TYR A CG  1 
ATOM   966  C  CD1 . TYR A 1 139 ? -23.681 13.040  -34.941  1.00 26.70  ? 131 TYR A CD1 1 
ATOM   967  C  CD2 . TYR A 1 139 ? -23.744 10.971  -36.150  1.00 25.96  ? 131 TYR A CD2 1 
ATOM   968  C  CE1 . TYR A 1 139 ? -22.297 13.060  -35.036  1.00 31.49  ? 131 TYR A CE1 1 
ATOM   969  C  CE2 . TYR A 1 139 ? -22.367 10.979  -36.247  1.00 27.48  ? 131 TYR A CE2 1 
ATOM   970  C  CZ  . TYR A 1 139 ? -21.647 12.024  -35.700  1.00 30.19  ? 131 TYR A CZ  1 
ATOM   971  O  OH  . TYR A 1 139 ? -20.283 12.022  -35.819  1.00 30.75  ? 131 TYR A OH  1 
ATOM   972  N  N   . PRO A 1 140 ? -28.513 11.489  -37.504  1.00 31.75  ? 132 PRO A N   1 
ATOM   973  C  CA  . PRO A 1 140 ? -29.945 11.233  -37.618  1.00 22.71  ? 132 PRO A CA  1 
ATOM   974  C  C   . PRO A 1 140 ? -30.384 10.134  -36.668  1.00 26.50  ? 132 PRO A C   1 
ATOM   975  O  O   . PRO A 1 140 ? -29.576 9.363   -36.146  1.00 29.88  ? 132 PRO A O   1 
ATOM   976  C  CB  . PRO A 1 140 ? -30.091 10.803  -39.081  1.00 25.63  ? 132 PRO A CB  1 
ATOM   977  C  CG  . PRO A 1 140 ? -28.811 10.018  -39.325  1.00 27.01  ? 132 PRO A CG  1 
ATOM   978  C  CD  . PRO A 1 140 ? -27.737 10.778  -38.542  1.00 21.39  ? 132 PRO A CD  1 
ATOM   979  N  N   . SER A 1 141 ? -31.693 10.097  -36.423  1.00 21.95  ? 133 SER A N   1 
ATOM   980  C  CA  . SER A 1 141 ? -32.310 8.946   -35.792  1.00 22.06  ? 133 SER A CA  1 
ATOM   981  C  C   . SER A 1 141 ? -32.735 7.890   -36.805  1.00 23.84  ? 133 SER A C   1 
ATOM   982  O  O   . SER A 1 141 ? -32.914 6.726   -36.431  1.00 27.53  ? 133 SER A O   1 
ATOM   983  C  CB  . SER A 1 141 ? -33.532 9.381   -34.970  1.00 35.89  ? 133 SER A CB  1 
ATOM   984  O  OG  . SER A 1 141 ? -33.301 10.583  -34.254  1.00 42.93  ? 133 SER A OG  1 
ATOM   985  N  N   . LEU A 1 142 ? -32.901 8.263   -38.070  1.00 19.94  ? 134 LEU A N   1 
ATOM   986  C  CA  . LEU A 1 142 ? -33.418 7.370   -39.093  1.00 21.22  ? 134 LEU A CA  1 
ATOM   987  C  C   . LEU A 1 142 ? -32.312 7.026   -40.072  1.00 23.20  ? 134 LEU A C   1 
ATOM   988  O  O   . LEU A 1 142 ? -31.554 7.904   -40.496  1.00 21.59  ? 134 LEU A O   1 
ATOM   989  C  CB  . LEU A 1 142 ? -34.583 8.012   -39.857  1.00 25.03  ? 134 LEU A CB  1 
ATOM   990  C  CG  . LEU A 1 142 ? -35.794 8.474   -39.038  1.00 30.08  ? 134 LEU A CG  1 
ATOM   991  C  CD1 . LEU A 1 142 ? -36.841 9.074   -39.946  1.00 19.29  ? 134 LEU A CD1 1 
ATOM   992  C  CD2 . LEU A 1 142 ? -36.375 7.351   -38.190  1.00 19.57  ? 134 LEU A CD2 1 
ATOM   993  N  N   . LEU A 1 143 ? -32.260 5.755   -40.450  1.00 23.04  ? 135 LEU A N   1 
ATOM   994  C  CA  . LEU A 1 143 ? -31.263 5.237   -41.373  1.00 16.87  ? 135 LEU A CA  1 
ATOM   995  C  C   . LEU A 1 143 ? -31.188 6.051   -42.662  1.00 20.00  ? 135 LEU A C   1 
ATOM   996  O  O   . LEU A 1 143 ? -32.200 6.306   -43.312  1.00 23.44  ? 135 LEU A O   1 
ATOM   997  C  CB  . LEU A 1 143 ? -31.605 3.776   -41.685  1.00 12.61  ? 135 LEU A CB  1 
ATOM   998  C  CG  . LEU A 1 143 ? -30.553 3.070   -42.523  1.00 19.09  ? 135 LEU A CG  1 
ATOM   999  C  CD1 . LEU A 1 143 ? -29.176 3.023   -41.795  1.00 15.84  ? 135 LEU A CD1 1 
ATOM   1000 C  CD2 . LEU A 1 143 ? -31.067 1.700   -42.908  1.00 18.64  ? 135 LEU A CD2 1 
ATOM   1001 N  N   . GLN A 1 144 ? -29.978 6.438   -43.038  1.00 15.69  ? 136 GLN A N   1 
ATOM   1002 C  CA  . GLN A 1 144 ? -29.737 7.228   -44.229  1.00 22.34  ? 136 GLN A CA  1 
ATOM   1003 C  C   . GLN A 1 144 ? -29.150 6.356   -45.330  1.00 21.92  ? 136 GLN A C   1 
ATOM   1004 O  O   . GLN A 1 144 ? -28.525 5.326   -45.057  1.00 21.45  ? 136 GLN A O   1 
ATOM   1005 C  CB  . GLN A 1 144 ? -28.797 8.393   -43.917  1.00 22.45  ? 136 GLN A CB  1 
ATOM   1006 C  CG  . GLN A 1 144 ? -29.416 9.376   -42.930  1.00 26.99  ? 136 GLN A CG  1 
ATOM   1007 C  CD  . GLN A 1 144 ? -30.692 10.023  -43.468  1.00 27.84  ? 136 GLN A CD  1 
ATOM   1008 O  OE1 . GLN A 1 144 ? -30.645 10.772  -44.442  1.00 25.12  ? 136 GLN A OE1 1 
ATOM   1009 N  NE2 . GLN A 1 144 ? -31.833 9.737   -42.829  1.00 18.55  ? 136 GLN A NE2 1 
ATOM   1010 N  N   . CYS A 1 145 ? -29.369 6.783   -46.576  1.00 22.06  ? 137 CYS A N   1 
ATOM   1011 C  CA  . CYS A 1 145 ? -29.055 6.033   -47.792  1.00 15.95  ? 137 CYS A CA  1 
ATOM   1012 C  C   . CYS A 1 145 ? -28.398 6.960   -48.797  1.00 22.43  ? 137 CYS A C   1 
ATOM   1013 O  O   . CYS A 1 145 ? -28.704 8.160   -48.866  1.00 23.80  ? 137 CYS A O   1 
ATOM   1014 C  CB  . CYS A 1 145 ? -30.314 5.465   -48.477  1.00 23.97  ? 137 CYS A CB  1 
ATOM   1015 S  SG  . CYS A 1 145 ? -30.935 3.898   -47.877  1.00 29.54  ? 137 CYS A SG  1 
ATOM   1016 N  N   . LEU A 1 146 ? -27.525 6.390   -49.611  1.00 21.05  ? 138 LEU A N   1 
ATOM   1017 C  CA  . LEU A 1 146 ? -26.956 7.138   -50.715  1.00 18.97  ? 138 LEU A CA  1 
ATOM   1018 C  C   . LEU A 1 146 ? -26.594 6.162   -51.818  1.00 22.94  ? 138 LEU A C   1 
ATOM   1019 O  O   . LEU A 1 146 ? -26.015 5.110   -51.549  1.00 22.93  ? 138 LEU A O   1 
ATOM   1020 C  CB  . LEU A 1 146 ? -25.729 7.922   -50.264  1.00 19.03  ? 138 LEU A CB  1 
ATOM   1021 C  CG  . LEU A 1 146 ? -25.061 8.785   -51.326  1.00 33.76  ? 138 LEU A CG  1 
ATOM   1022 C  CD1 . LEU A 1 146 ? -25.956 9.978   -51.679  1.00 24.06  ? 138 LEU A CD1 1 
ATOM   1023 C  CD2 . LEU A 1 146 ? -23.693 9.244   -50.840  1.00 27.39  ? 138 LEU A CD2 1 
ATOM   1024 N  N   . LYS A 1 147 ? -26.950 6.500   -53.052  1.00 21.75  ? 139 LYS A N   1 
ATOM   1025 C  CA  . LYS A 1 147 ? -26.459 5.766   -54.210  1.00 26.36  ? 139 LYS A CA  1 
ATOM   1026 C  C   . LYS A 1 147 ? -25.248 6.497   -54.775  1.00 18.51  ? 139 LYS A C   1 
ATOM   1027 O  O   . LYS A 1 147 ? -25.279 7.715   -54.960  1.00 28.64  ? 139 LYS A O   1 
ATOM   1028 C  CB  . LYS A 1 147 ? -27.551 5.584   -55.273  1.00 27.22  ? 139 LYS A CB  1 
ATOM   1029 C  CG  . LYS A 1 147 ? -28.748 4.744   -54.785  1.00 30.20  ? 139 LYS A CG  1 
ATOM   1030 C  CD  . LYS A 1 147 ? -30.001 4.968   -55.624  1.00 29.15  ? 139 LYS A CD  1 
ATOM   1031 C  CE  . LYS A 1 147 ? -31.189 4.128   -55.119  1.00 23.07  ? 139 LYS A CE  1 
ATOM   1032 N  NZ  . LYS A 1 147 ? -32.510 4.544   -55.769  1.00 20.52  ? 139 LYS A NZ  1 
ATOM   1033 N  N   . ALA A 1 148 ? -24.179 5.753   -55.022  1.00 19.40  ? 140 ALA A N   1 
ATOM   1034 C  CA  . ALA A 1 148 ? -22.921 6.317   -55.477  1.00 24.30  ? 140 ALA A CA  1 
ATOM   1035 C  C   . ALA A 1 148 ? -22.187 5.271   -56.297  1.00 23.93  ? 140 ALA A C   1 
ATOM   1036 O  O   . ALA A 1 148 ? -22.318 4.067   -56.038  1.00 21.40  ? 140 ALA A O   1 
ATOM   1037 C  CB  . ALA A 1 148 ? -22.036 6.769   -54.309  1.00 20.21  ? 140 ALA A CB  1 
ATOM   1038 N  N   . PRO A 1 149 ? -21.411 5.694   -57.283  1.00 20.39  ? 141 PRO A N   1 
ATOM   1039 C  CA  . PRO A 1 149 ? -20.639 4.743   -58.087  1.00 29.96  ? 141 PRO A CA  1 
ATOM   1040 C  C   . PRO A 1 149 ? -19.327 4.319   -57.440  1.00 22.71  ? 141 PRO A C   1 
ATOM   1041 O  O   . PRO A 1 149 ? -18.695 5.063   -56.683  1.00 25.06  ? 141 PRO A O   1 
ATOM   1042 C  CB  . PRO A 1 149 ? -20.369 5.525   -59.376  1.00 27.07  ? 141 PRO A CB  1 
ATOM   1043 C  CG  . PRO A 1 149 ? -20.339 6.966   -58.930  1.00 28.26  ? 141 PRO A CG  1 
ATOM   1044 C  CD  . PRO A 1 149 ? -21.363 7.065   -57.823  1.00 19.74  ? 141 PRO A CD  1 
ATOM   1045 N  N   . VAL A 1 150 ? -18.914 3.098   -57.779  1.00 25.01  ? 142 VAL A N   1 
ATOM   1046 C  CA  . VAL A 1 150 ? -17.558 2.660   -57.486  1.00 24.16  ? 142 VAL A CA  1 
ATOM   1047 C  C   . VAL A 1 150 ? -16.605 3.443   -58.371  1.00 25.98  ? 142 VAL A C   1 
ATOM   1048 O  O   . VAL A 1 150 ? -16.807 3.552   -59.589  1.00 26.48  ? 142 VAL A O   1 
ATOM   1049 C  CB  . VAL A 1 150 ? -17.401 1.151   -57.713  1.00 27.61  ? 142 VAL A CB  1 
ATOM   1050 C  CG1 . VAL A 1 150 ? -15.933 0.774   -57.722  1.00 27.00  ? 142 VAL A CG1 1 
ATOM   1051 C  CG2 . VAL A 1 150 ? -18.150 0.371   -56.670  1.00 28.20  ? 142 VAL A CG2 1 
ATOM   1052 N  N   . LEU A 1 151 ? -15.579 4.014   -57.758  1.00 28.63  ? 143 LEU A N   1 
ATOM   1053 C  CA  . LEU A 1 151 ? -14.598 4.805   -58.474  1.00 24.92  ? 143 LEU A CA  1 
ATOM   1054 C  C   . LEU A 1 151 ? -13.491 3.900   -59.010  1.00 36.07  ? 143 LEU A C   1 
ATOM   1055 O  O   . LEU A 1 151 ? -13.276 2.779   -58.526  1.00 28.92  ? 143 LEU A O   1 
ATOM   1056 C  CB  . LEU A 1 151 ? -14.025 5.873   -57.549  1.00 28.01  ? 143 LEU A CB  1 
ATOM   1057 C  CG  . LEU A 1 151 ? -15.089 6.891   -57.126  1.00 35.72  ? 143 LEU A CG  1 
ATOM   1058 C  CD1 . LEU A 1 151 ? -14.529 7.865   -56.123  1.00 27.29  ? 143 LEU A CD1 1 
ATOM   1059 C  CD2 . LEU A 1 151 ? -15.695 7.622   -58.333  1.00 29.74  ? 143 LEU A CD2 1 
ATOM   1060 N  N   . SER A 1 152 ? -12.794 4.397   -60.031  1.00 30.45  ? 144 SER A N   1 
ATOM   1061 C  CA  . SER A 1 152 ? -11.677 3.654   -60.604  1.00 35.68  ? 144 SER A CA  1 
ATOM   1062 C  C   . SER A 1 152 ? -10.524 3.581   -59.616  1.00 35.65  ? 144 SER A C   1 
ATOM   1063 O  O   . SER A 1 152 ? -10.339 4.463   -58.773  1.00 36.24  ? 144 SER A O   1 
ATOM   1064 C  CB  . SER A 1 152 ? -11.184 4.312   -61.896  1.00 35.69  ? 144 SER A CB  1 
ATOM   1065 O  OG  . SER A 1 152 ? -11.117 5.726   -61.770  1.00 47.61  ? 144 SER A OG  1 
ATOM   1066 N  N   A ASP A 1 153 ? -9.743  2.503   -59.730  0.46 39.71  ? 145 ASP A N   1 
ATOM   1067 N  N   B ASP A 1 153 ? -9.732  2.515   -59.715  0.54 39.83  ? 145 ASP A N   1 
ATOM   1068 C  CA  A ASP A 1 153 ? -8.523  2.384   -58.940  0.46 38.04  ? 145 ASP A CA  1 
ATOM   1069 C  CA  B ASP A 1 153 ? -8.555  2.454   -58.861  0.54 38.36  ? 145 ASP A CA  1 
ATOM   1070 C  C   A ASP A 1 153 ? -7.614  3.577   -59.183  0.46 37.76  ? 145 ASP A C   1 
ATOM   1071 C  C   B ASP A 1 153 ? -7.607  3.599   -59.170  0.54 37.70  ? 145 ASP A C   1 
ATOM   1072 O  O   A ASP A 1 153 ? -6.929  4.049   -58.268  0.46 39.35  ? 145 ASP A O   1 
ATOM   1073 O  O   B ASP A 1 153 ? -6.881  4.058   -58.282  0.54 38.61  ? 145 ASP A O   1 
ATOM   1074 C  CB  A ASP A 1 153 ? -7.800  1.074   -59.274  0.46 37.85  ? 145 ASP A CB  1 
ATOM   1075 C  CB  B ASP A 1 153 ? -7.845  1.109   -59.003  0.54 37.97  ? 145 ASP A CB  1 
ATOM   1076 C  CG  A ASP A 1 153 ? -7.958  0.661   -60.738  0.46 40.35  ? 145 ASP A CG  1 
ATOM   1077 C  CG  B ASP A 1 153 ? -7.343  0.579   -57.671  0.54 44.90  ? 145 ASP A CG  1 
ATOM   1078 O  OD1 A ASP A 1 153 ? -8.029  1.550   -61.615  0.46 42.98  ? 145 ASP A OD1 1 
ATOM   1079 O  OD1 B ASP A 1 153 ? -7.847  1.028   -56.610  0.54 38.28  ? 145 ASP A OD1 1 
ATOM   1080 O  OD2 A ASP A 1 153 ? -7.998  -0.560  -61.016  0.46 37.46  ? 145 ASP A OD2 1 
ATOM   1081 O  OD2 B ASP A 1 153 ? -6.424  -0.268  -57.685  0.54 44.48  ? 145 ASP A OD2 1 
ATOM   1082 N  N   . SER A 1 154 ? -7.614  4.086   -60.414  1.00 35.72  ? 146 SER A N   1 
ATOM   1083 C  CA  . SER A 1 154 ? -6.811  5.249   -60.756  1.00 38.04  ? 146 SER A CA  1 
ATOM   1084 C  C   . SER A 1 154 ? -7.291  6.495   -60.017  1.00 37.88  ? 146 SER A C   1 
ATOM   1085 O  O   . SER A 1 154 ? -6.494  7.213   -59.402  1.00 34.80  ? 146 SER A O   1 
ATOM   1086 C  CB  . SER A 1 154 ? -6.860  5.472   -62.267  1.00 41.31  ? 146 SER A CB  1 
ATOM   1087 O  OG  . SER A 1 154 ? -6.314  6.737   -62.590  1.00 50.06  ? 146 SER A OG  1 
ATOM   1088 N  N   . SER A 1 155 ? -8.593  6.781   -60.078  1.00 38.33  ? 147 SER A N   1 
ATOM   1089 C  CA  . SER A 1 155 ? -9.091  7.988   -59.425  1.00 34.42  ? 147 SER A CA  1 
ATOM   1090 C  C   . SER A 1 155 ? -9.043  7.867   -57.901  1.00 31.26  ? 147 SER A C   1 
ATOM   1091 O  O   . SER A 1 155 ? -8.849  8.867   -57.202  1.00 32.20  ? 147 SER A O   1 
ATOM   1092 C  CB  . SER A 1 155 ? -10.500 8.283   -59.926  1.00 31.43  ? 147 SER A CB  1 
ATOM   1093 O  OG  . SER A 1 155 ? -11.452 8.137   -58.892  1.00 51.02  ? 147 SER A OG  1 
ATOM   1094 N  N   . CYS A 1 156 ? -9.192  6.653   -57.378  1.00 25.88  ? 148 CYS A N   1 
ATOM   1095 C  CA  . CYS A 1 156 ? -9.088  6.424   -55.947  1.00 27.86  ? 148 CYS A CA  1 
ATOM   1096 C  C   . CYS A 1 156 ? -7.672  6.665   -55.456  1.00 30.07  ? 148 CYS A C   1 
ATOM   1097 O  O   . CYS A 1 156 ? -7.466  7.263   -54.391  1.00 29.41  ? 148 CYS A O   1 
ATOM   1098 C  CB  . CYS A 1 156 ? -9.535  4.993   -55.627  1.00 33.40  ? 148 CYS A CB  1 
ATOM   1099 S  SG  . CYS A 1 156 ? -9.611  4.565   -53.862  1.00 40.36  ? 148 CYS A SG  1 
ATOM   1100 N  N   . LYS A 1 157 ? -6.682  6.195   -56.218  1.00 33.83  ? 149 LYS A N   1 
ATOM   1101 C  CA  . LYS A 1 157 ? -5.285  6.380   -55.839  1.00 31.06  ? 149 LYS A CA  1 
ATOM   1102 C  C   . LYS A 1 157 ? -4.806  7.813   -56.060  1.00 30.69  ? 149 LYS A C   1 
ATOM   1103 O  O   . LYS A 1 157 ? -3.873  8.252   -55.385  1.00 30.54  ? 149 LYS A O   1 
ATOM   1104 C  CB  . LYS A 1 157 ? -4.408  5.386   -56.597  1.00 32.07  ? 149 LYS A CB  1 
ATOM   1105 C  CG  . LYS A 1 157 ? -4.070  4.181   -55.753  1.00 35.91  ? 149 LYS A CG  1 
ATOM   1106 C  CD  . LYS A 1 157 ? -3.482  3.036   -56.532  1.00 37.42  ? 149 LYS A CD  1 
ATOM   1107 C  CE  . LYS A 1 157 ? -4.569  2.107   -56.961  1.00 44.15  ? 149 LYS A CE  1 
ATOM   1108 N  NZ  . LYS A 1 157 ? -4.038  0.781   -57.392  1.00 51.55  ? 149 LYS A NZ  1 
ATOM   1109 N  N   . SER A 1 158 ? -5.411  8.555   -56.993  1.00 26.69  ? 150 SER A N   1 
ATOM   1110 C  CA  . SER A 1 158 ? -5.093  9.974   -57.089  1.00 27.48  ? 150 SER A CA  1 
ATOM   1111 C  C   . SER A 1 158 ? -5.722  10.777  -55.957  1.00 29.11  ? 150 SER A C   1 
ATOM   1112 O  O   . SER A 1 158 ? -5.138  11.769  -55.518  1.00 26.31  ? 150 SER A O   1 
ATOM   1113 C  CB  . SER A 1 158 ? -5.507  10.537  -58.449  1.00 23.97  ? 150 SER A CB  1 
ATOM   1114 O  OG  . SER A 1 158 ? -5.142  9.654   -59.495  1.00 29.99  ? 150 SER A OG  1 
ATOM   1115 N  N   . SER A 1 159 ? -6.889  10.368  -55.451  1.00 33.23  ? 151 SER A N   1 
ATOM   1116 C  CA  . SER A 1 159 ? -7.486  11.129  -54.353  1.00 26.06  ? 151 SER A CA  1 
ATOM   1117 C  C   . SER A 1 159 ? -6.772  10.869  -53.042  1.00 24.41  ? 151 SER A C   1 
ATOM   1118 O  O   . SER A 1 159 ? -6.715  11.757  -52.183  1.00 28.23  ? 151 SER A O   1 
ATOM   1119 C  CB  . SER A 1 159 ? -8.970  10.814  -54.212  1.00 21.54  ? 151 SER A CB  1 
ATOM   1120 O  OG  . SER A 1 159 ? -9.656  11.093  -55.412  1.00 35.34  ? 151 SER A OG  1 
ATOM   1121 N  N   . TYR A 1 160 ? -6.208  9.678   -52.871  1.00 21.35  ? 152 TYR A N   1 
ATOM   1122 C  CA  . TYR A 1 160 ? -5.531  9.311   -51.629  1.00 32.17  ? 152 TYR A CA  1 
ATOM   1123 C  C   . TYR A 1 160 ? -4.143  8.778   -51.939  1.00 33.26  ? 152 TYR A C   1 
ATOM   1124 O  O   . TYR A 1 160 ? -3.838  7.614   -51.660  1.00 27.59  ? 152 TYR A O   1 
ATOM   1125 C  CB  . TYR A 1 160 ? -6.349  8.291   -50.843  1.00 25.64  ? 152 TYR A CB  1 
ATOM   1126 C  CG  . TYR A 1 160 ? -7.625  8.879   -50.287  1.00 30.01  ? 152 TYR A CG  1 
ATOM   1127 C  CD1 . TYR A 1 160 ? -7.615  9.659   -49.127  1.00 21.59  ? 152 TYR A CD1 1 
ATOM   1128 C  CD2 . TYR A 1 160 ? -8.842  8.671   -50.934  1.00 29.65  ? 152 TYR A CD2 1 
ATOM   1129 C  CE1 . TYR A 1 160 ? -8.800  10.191  -48.608  1.00 25.50  ? 152 TYR A CE1 1 
ATOM   1130 C  CE2 . TYR A 1 160 ? -10.026 9.194   -50.429  1.00 32.57  ? 152 TYR A CE2 1 
ATOM   1131 C  CZ  . TYR A 1 160 ? -10.005 9.944   -49.265  1.00 30.13  ? 152 TYR A CZ  1 
ATOM   1132 O  OH  . TYR A 1 160 ? -11.190 10.460  -48.793  1.00 24.41  ? 152 TYR A OH  1 
ATOM   1133 N  N   . PRO A 1 161 ? -3.251  9.639   -52.469  1.00 34.97  ? 153 PRO A N   1 
ATOM   1134 C  CA  . PRO A 1 161 ? -1.930  9.176   -52.923  1.00 27.16  ? 153 PRO A CA  1 
ATOM   1135 C  C   . PRO A 1 161 ? -1.175  8.390   -51.870  1.00 32.05  ? 153 PRO A C   1 
ATOM   1136 O  O   . PRO A 1 161 ? -0.936  8.898   -50.776  1.00 31.63  ? 153 PRO A O   1 
ATOM   1137 C  CB  . PRO A 1 161 ? -1.200  10.487  -53.239  1.00 34.60  ? 153 PRO A CB  1 
ATOM   1138 C  CG  . PRO A 1 161 ? -2.312  11.441  -53.566  1.00 36.40  ? 153 PRO A CG  1 
ATOM   1139 C  CD  . PRO A 1 161 ? -3.359  11.108  -52.539  1.00 22.70  ? 153 PRO A CD  1 
ATOM   1140 N  N   . GLY A 1 162 ? -0.820  7.146   -52.181  1.00 33.72  ? 154 GLY A N   1 
ATOM   1141 C  CA  . GLY A 1 162 ? -0.030  6.351   -51.273  1.00 19.76  ? 154 GLY A CA  1 
ATOM   1142 C  C   . GLY A 1 162 ? -0.757  5.832   -50.064  1.00 26.22  ? 154 GLY A C   1 
ATOM   1143 O  O   . GLY A 1 162 ? -0.109  5.408   -49.111  1.00 35.34  ? 154 GLY A O   1 
ATOM   1144 N  N   . GLN A 1 163 ? -2.088  5.842   -50.067  1.00 30.80  ? 155 GLN A N   1 
ATOM   1145 C  CA  . GLN A 1 163 ? -2.848  5.297   -48.951  1.00 31.09  ? 155 GLN A CA  1 
ATOM   1146 C  C   . GLN A 1 163 ? -3.708  4.101   -49.307  1.00 36.82  ? 155 GLN A C   1 
ATOM   1147 O  O   . GLN A 1 163 ? -4.163  3.400   -48.400  1.00 31.15  ? 155 GLN A O   1 
ATOM   1148 C  CB  . GLN A 1 163 ? -3.757  6.368   -48.331  1.00 29.03  ? 155 GLN A CB  1 
ATOM   1149 C  CG  . GLN A 1 163 ? -3.010  7.496   -47.654  1.00 34.28  ? 155 GLN A CG  1 
ATOM   1150 C  CD  . GLN A 1 163 ? -3.928  8.361   -46.838  1.00 35.81  ? 155 GLN A CD  1 
ATOM   1151 O  OE1 . GLN A 1 163 ? -4.304  9.445   -47.261  1.00 36.88  ? 155 GLN A OE1 1 
ATOM   1152 N  NE2 . GLN A 1 163 ? -4.336  7.862   -45.679  1.00 35.44  ? 155 GLN A NE2 1 
ATOM   1153 N  N   . ILE A 1 164 ? -3.942  3.842   -50.580  1.00 29.38  ? 156 ILE A N   1 
ATOM   1154 C  CA  . ILE A 1 164 ? -4.895  2.829   -50.987  1.00 26.97  ? 156 ILE A CA  1 
ATOM   1155 C  C   . ILE A 1 164 ? -4.145  1.530   -51.207  1.00 36.51  ? 156 ILE A C   1 
ATOM   1156 O  O   . ILE A 1 164 ? -3.199  1.488   -51.995  1.00 42.69  ? 156 ILE A O   1 
ATOM   1157 C  CB  . ILE A 1 164 ? -5.642  3.268   -52.248  1.00 24.65  ? 156 ILE A CB  1 
ATOM   1158 C  CG1 . ILE A 1 164 ? -6.349  4.592   -51.961  1.00 24.62  ? 156 ILE A CG1 1 
ATOM   1159 C  CG2 . ILE A 1 164 ? -6.632  2.211   -52.662  1.00 24.71  ? 156 ILE A CG2 1 
ATOM   1160 C  CD1 . ILE A 1 164 ? -7.264  4.517   -50.732  1.00 28.59  ? 156 ILE A CD1 1 
ATOM   1161 N  N   . THR A 1 165 ? -4.536  0.482   -50.481  1.00 28.89  ? 157 THR A N   1 
ATOM   1162 C  CA  . THR A 1 165 ? -4.012  -0.841  -50.760  1.00 25.24  ? 157 THR A CA  1 
ATOM   1163 C  C   . THR A 1 165 ? -4.915  -1.543  -51.763  1.00 30.52  ? 157 THR A C   1 
ATOM   1164 O  O   . THR A 1 165 ? -5.945  -1.015  -52.199  1.00 32.03  ? 157 THR A O   1 
ATOM   1165 C  CB  . THR A 1 165 ? -3.895  -1.689  -49.492  1.00 34.78  ? 157 THR A CB  1 
ATOM   1166 O  OG1 . THR A 1 165 ? -5.197  -2.123  -49.076  1.00 26.52  ? 157 THR A OG1 1 
ATOM   1167 C  CG2 . THR A 1 165 ? -3.212  -0.922  -48.374  1.00 24.11  ? 157 THR A CG2 1 
ATOM   1168 N  N   . GLY A 1 166 ? -4.535  -2.764  -52.121  1.00 26.87  ? 158 GLY A N   1 
ATOM   1169 C  CA  . GLY A 1 166 ? -5.403  -3.549  -52.963  1.00 26.55  ? 158 GLY A CA  1 
ATOM   1170 C  C   . GLY A 1 166 ? -6.666  -4.027  -52.287  1.00 32.24  ? 158 GLY A C   1 
ATOM   1171 O  O   . GLY A 1 166 ? -7.480  -4.706  -52.923  1.00 41.62  ? 158 GLY A O   1 
ATOM   1172 N  N   . ASN A 1 167 ? -6.856  -3.700  -51.013  1.00 20.80  ? 159 ASN A N   1 
ATOM   1173 C  CA  . ASN A 1 167 ? -8.031  -4.145  -50.288  1.00 25.48  ? 159 ASN A CA  1 
ATOM   1174 C  C   . ASN A 1 167 ? -8.990  -3.009  -49.987  1.00 29.80  ? 159 ASN A C   1 
ATOM   1175 O  O   . ASN A 1 167 ? -9.873  -3.158  -49.135  1.00 32.47  ? 159 ASN A O   1 
ATOM   1176 C  CB  . ASN A 1 167 ? -7.627  -4.846  -49.003  1.00 25.34  ? 159 ASN A CB  1 
ATOM   1177 C  CG  . ASN A 1 167 ? -6.803  -6.069  -49.270  1.00 31.70  ? 159 ASN A CG  1 
ATOM   1178 O  OD1 . ASN A 1 167 ? -7.316  -7.061  -49.773  1.00 39.58  ? 159 ASN A OD1 1 
ATOM   1179 N  ND2 . ASN A 1 167 ? -5.539  -6.035  -48.884  1.00 39.01  ? 159 ASN A ND2 1 
ATOM   1180 N  N   . MET A 1 168 ? -8.841  -1.880  -50.663  1.00 23.62  ? 160 MET A N   1 
ATOM   1181 C  CA  . MET A 1 168 ? -9.760  -0.773  -50.475  1.00 28.90  ? 160 MET A CA  1 
ATOM   1182 C  C   . MET A 1 168 ? -10.290 -0.330  -51.831  1.00 29.27  ? 160 MET A C   1 
ATOM   1183 O  O   . MET A 1 168 ? -9.631  -0.498  -52.861  1.00 32.15  ? 160 MET A O   1 
ATOM   1184 C  CB  . MET A 1 168 ? -9.088  0.417   -49.740  1.00 23.96  ? 160 MET A CB  1 
ATOM   1185 C  CG  . MET A 1 168 ? -8.249  -0.005  -48.520  1.00 22.72  ? 160 MET A CG  1 
ATOM   1186 S  SD  . MET A 1 168 ? -7.147  1.313   -47.965  1.00 24.08  ? 160 MET A SD  1 
ATOM   1187 C  CE  . MET A 1 168 ? -6.383  0.532   -46.565  1.00 25.96  ? 160 MET A CE  1 
ATOM   1188 N  N   . ILE A 1 169 ? -11.510 0.205   -51.819  1.00 26.78  ? 161 ILE A N   1 
ATOM   1189 C  CA  . ILE A 1 169 ? -12.104 0.862   -52.974  1.00 28.61  ? 161 ILE A CA  1 
ATOM   1190 C  C   . ILE A 1 169 ? -12.702 2.190   -52.540  1.00 26.36  ? 161 ILE A C   1 
ATOM   1191 O  O   . ILE A 1 169 ? -13.126 2.366   -51.392  1.00 28.15  ? 161 ILE A O   1 
ATOM   1192 C  CB  . ILE A 1 169 ? -13.176 -0.009  -53.663  1.00 29.35  ? 161 ILE A CB  1 
ATOM   1193 C  CG1 . ILE A 1 169 ? -14.471 -0.040  -52.836  1.00 29.49  ? 161 ILE A CG1 1 
ATOM   1194 C  CG2 . ILE A 1 169 ? -12.630 -1.412  -53.910  1.00 31.92  ? 161 ILE A CG2 1 
ATOM   1195 C  CD1 . ILE A 1 169 ? -15.434 -1.125  -53.268  1.00 31.27  ? 161 ILE A CD1 1 
ATOM   1196 N  N   . CYS A 1 170 ? -12.736 3.132   -53.470  1.00 25.27  ? 162 CYS A N   1 
ATOM   1197 C  CA  . CYS A 1 170 ? -13.385 4.414   -53.248  1.00 22.51  ? 162 CYS A CA  1 
ATOM   1198 C  C   . CYS A 1 170 ? -14.767 4.362   -53.878  1.00 23.27  ? 162 CYS A C   1 
ATOM   1199 O  O   . CYS A 1 170 ? -14.922 3.874   -55.005  1.00 20.77  ? 162 CYS A O   1 
ATOM   1200 C  CB  . CYS A 1 170 ? -12.561 5.561   -53.843  1.00 25.89  ? 162 CYS A CB  1 
ATOM   1201 S  SG  . CYS A 1 170 ? -10.967 5.854   -52.991  1.00 27.63  ? 162 CYS A SG  1 
ATOM   1202 N  N   . VAL A 1 171 ? -15.767 4.843   -53.146  1.00 20.34  ? 163 VAL A N   1 
ATOM   1203 C  CA  . VAL A 1 171 ? -17.135 4.931   -53.647  1.00 25.87  ? 163 VAL A CA  1 
ATOM   1204 C  C   . VAL A 1 171 ? -17.654 6.333   -53.376  1.00 24.86  ? 163 VAL A C   1 
ATOM   1205 O  O   . VAL A 1 171 ? -17.563 6.833   -52.247  1.00 33.74  ? 163 VAL A O   1 
ATOM   1206 C  CB  . VAL A 1 171 ? -18.051 3.863   -53.014  1.00 29.65  ? 163 VAL A CB  1 
ATOM   1207 C  CG1 . VAL A 1 171 ? -19.463 3.913   -53.604  1.00 21.88  ? 163 VAL A CG1 1 
ATOM   1208 C  CG2 . VAL A 1 171 ? -17.444 2.475   -53.214  1.00 25.51  ? 163 VAL A CG2 1 
ATOM   1209 N  N   . GLY A 1 172 ? -18.191 6.970   -54.401  1.00 19.64  ? 164 GLY A N   1 
ATOM   1210 C  CA  . GLY A 1 172 ? -18.667 8.313   -54.187  1.00 17.76  ? 164 GLY A CA  1 
ATOM   1211 C  C   . GLY A 1 172 ? -18.409 9.219   -55.364  1.00 27.15  ? 164 GLY A C   1 
ATOM   1212 O  O   . GLY A 1 172 ? -18.517 8.794   -56.520  1.00 32.70  ? 164 GLY A O   1 
ATOM   1213 N  N   . PHE A 1 173 ? -18.049 10.470  -55.081  1.00 30.96  ? 165 PHE A N   1 
ATOM   1214 C  CA  . PHE A 1 173 ? -18.046 11.524  -56.092  1.00 30.96  ? 165 PHE A CA  1 
ATOM   1215 C  C   . PHE A 1 173 ? -16.813 12.399  -55.932  1.00 32.37  ? 165 PHE A C   1 
ATOM   1216 O  O   . PHE A 1 173 ? -16.633 13.047  -54.896  1.00 38.98  ? 165 PHE A O   1 
ATOM   1217 C  CB  . PHE A 1 173 ? -19.323 12.364  -56.000  1.00 26.02  ? 165 PHE A CB  1 
ATOM   1218 C  CG  . PHE A 1 173 ? -20.585 11.539  -55.964  1.00 30.67  ? 165 PHE A CG  1 
ATOM   1219 C  CD1 . PHE A 1 173 ? -21.091 11.064  -54.763  1.00 25.03  ? 165 PHE A CD1 1 
ATOM   1220 C  CD2 . PHE A 1 173 ? -21.256 11.231  -57.132  1.00 26.73  ? 165 PHE A CD2 1 
ATOM   1221 C  CE1 . PHE A 1 173 ? -22.236 10.298  -54.733  1.00 31.38  ? 165 PHE A CE1 1 
ATOM   1222 C  CE2 . PHE A 1 173 ? -22.417 10.464  -57.103  1.00 24.44  ? 165 PHE A CE2 1 
ATOM   1223 C  CZ  . PHE A 1 173 ? -22.901 9.998   -55.904  1.00 22.36  ? 165 PHE A CZ  1 
ATOM   1224 N  N   . LEU A 1 174 ? -15.980 12.433  -56.972  1.00 30.11  ? 166 LEU A N   1 
ATOM   1225 C  CA  . LEU A 1 174 ? -14.857 13.362  -56.992  1.00 36.25  ? 166 LEU A CA  1 
ATOM   1226 C  C   . LEU A 1 174 ? -15.297 14.795  -56.721  1.00 36.50  ? 166 LEU A C   1 
ATOM   1227 O  O   . LEU A 1 174 ? -14.540 15.567  -56.120  1.00 40.07  ? 166 LEU A O   1 
ATOM   1228 C  CB  . LEU A 1 174 ? -14.133 13.266  -58.333  1.00 28.32  ? 166 LEU A CB  1 
ATOM   1229 C  CG  . LEU A 1 174 ? -12.929 12.321  -58.306  1.00 38.05  ? 166 LEU A CG  1 
ATOM   1230 C  CD1 . LEU A 1 174 ? -13.273 11.074  -57.533  1.00 36.23  ? 166 LEU A CD1 1 
ATOM   1231 C  CD2 . LEU A 1 174 ? -12.457 11.953  -59.722  1.00 38.69  ? 166 LEU A CD2 1 
ATOM   1232 N  N   . GLU A 1 175 ? -16.523 15.158  -57.116  1.00 29.93  ? 167 GLU A N   1 
ATOM   1233 C  CA  . GLU A 1 175 ? -17.000 16.528  -56.938  1.00 36.31  ? 167 GLU A CA  1 
ATOM   1234 C  C   . GLU A 1 175 ? -17.351 16.852  -55.490  1.00 42.25  ? 167 GLU A C   1 
ATOM   1235 O  O   . GLU A 1 175 ? -17.400 18.033  -55.131  1.00 50.11  ? 167 GLU A O   1 
ATOM   1236 C  CB  . GLU A 1 175 ? -18.211 16.795  -57.850  1.00 37.20  ? 167 GLU A CB  1 
ATOM   1237 C  CG  . GLU A 1 175 ? -19.597 16.378  -57.286  1.00 55.88  ? 167 GLU A CG  1 
ATOM   1238 C  CD  . GLU A 1 175 ? -20.224 15.199  -58.065  1.00 73.99  ? 167 GLU A CD  1 
ATOM   1239 O  OE1 . GLU A 1 175 ? -19.431 14.354  -58.565  1.00 63.80  ? 167 GLU A OE1 1 
ATOM   1240 O  OE2 . GLU A 1 175 ? -21.483 15.114  -58.178  1.00 40.93  ? 167 GLU A OE2 1 
ATOM   1241 N  N   . GLY A 1 176 ? -17.586 15.849  -54.650  1.00 37.71  ? 168 GLY A N   1 
ATOM   1242 C  CA  . GLY A 1 176 ? -17.986 16.096  -53.275  1.00 38.32  ? 168 GLY A CA  1 
ATOM   1243 C  C   . GLY A 1 176 ? -19.494 16.237  -53.087  1.00 33.29  ? 168 GLY A C   1 
ATOM   1244 O  O   . GLY A 1 176 ? -20.306 16.052  -54.002  1.00 43.10  ? 168 GLY A O   1 
ATOM   1245 N  N   . GLY A 1 177 ? -19.870 16.558  -51.853  1.00 24.43  ? 169 GLY A N   1 
ATOM   1246 C  CA  . GLY A 1 177 ? -21.254 16.782  -51.474  1.00 28.25  ? 169 GLY A CA  1 
ATOM   1247 C  C   . GLY A 1 177 ? -22.004 15.571  -50.961  1.00 22.73  ? 169 GLY A C   1 
ATOM   1248 O  O   . GLY A 1 177 ? -22.851 15.694  -50.082  1.00 27.38  ? 169 GLY A O   1 
ATOM   1249 N  N   . LYS A 1 178 ? -21.712 14.398  -51.494  1.00 28.66  ? 170 LYS A N   1 
ATOM   1250 C  CA  . LYS A 1 178 ? -22.353 13.172  -51.048  1.00 28.31  ? 170 LYS A CA  1 
ATOM   1251 C  C   . LYS A 1 178 ? -21.266 12.185  -50.656  1.00 31.56  ? 170 LYS A C   1 
ATOM   1252 O  O   . LYS A 1 178 ? -20.280 12.016  -51.382  1.00 33.13  ? 170 LYS A O   1 
ATOM   1253 C  CB  . LYS A 1 178 ? -23.275 12.612  -52.146  1.00 23.82  ? 170 LYS A CB  1 
ATOM   1254 C  CG  . LYS A 1 178 ? -24.253 13.679  -52.691  1.00 28.32  ? 170 LYS A CG  1 
ATOM   1255 C  CD  . LYS A 1 178 ? -25.364 13.076  -53.561  1.00 37.19  ? 170 LYS A CD  1 
ATOM   1256 C  CE  . LYS A 1 178 ? -26.626 13.937  -53.559  1.00 32.01  ? 170 LYS A CE  1 
ATOM   1257 N  NZ  . LYS A 1 178 ? -26.424 15.281  -52.940  1.00 48.43  ? 170 LYS A NZ  1 
ATOM   1258 N  N   . ASP A 1 179 ? -21.432 11.556  -49.498  1.00 33.83  ? 171 ASP A N   1 
ATOM   1259 C  CA  . ASP A 1 179 ? -20.363 10.751  -48.924  1.00 31.85  ? 171 ASP A CA  1 
ATOM   1260 C  C   . ASP A 1 179 ? -20.879 10.163  -47.624  1.00 25.01  ? 171 ASP A C   1 
ATOM   1261 O  O   . ASP A 1 179 ? -21.852 10.655  -47.049  1.00 28.60  ? 171 ASP A O   1 
ATOM   1262 C  CB  . ASP A 1 179 ? -19.090 11.579  -48.658  1.00 23.85  ? 171 ASP A CB  1 
ATOM   1263 C  CG  . ASP A 1 179 ? -17.798 10.735  -48.701  1.00 43.99  ? 171 ASP A CG  1 
ATOM   1264 O  OD1 . ASP A 1 179 ? -17.833 9.556   -49.153  1.00 45.50  ? 171 ASP A OD1 1 
ATOM   1265 O  OD2 . ASP A 1 179 ? -16.739 11.261  -48.273  1.00 41.27  ? 171 ASP A OD2 1 
ATOM   1266 N  N   . SER A 1 180 ? -20.218 9.095   -47.180  1.00 26.65  ? 172 SER A N   1 
ATOM   1267 C  CA  . SER A 1 180 ? -20.335 8.569   -45.830  1.00 20.95  ? 172 SER A CA  1 
ATOM   1268 C  C   . SER A 1 180 ? -19.480 9.392   -44.855  1.00 22.98  ? 172 SER A C   1 
ATOM   1269 O  O   . SER A 1 180 ? -18.602 10.164  -45.247  1.00 23.53  ? 172 SER A O   1 
ATOM   1270 C  CB  . SER A 1 180 ? -19.910 7.103   -45.812  1.00 23.81  ? 172 SER A CB  1 
ATOM   1271 O  OG  . SER A 1 180 ? -18.645 6.970   -46.430  1.00 39.15  ? 172 SER A OG  1 
ATOM   1272 N  N   . CYS A 1 181 ? -19.746 9.224   -43.565  1.00 25.93  ? 173 CYS A N   1 
ATOM   1273 C  CA  . CYS A 1 181 ? -19.130 10.062  -42.543  1.00 27.37  ? 173 CYS A CA  1 
ATOM   1274 C  C   . CYS A 1 181 ? -19.000 9.288   -41.233  1.00 23.89  ? 173 CYS A C   1 
ATOM   1275 O  O   . CYS A 1 181 ? -19.430 8.136   -41.116  1.00 26.53  ? 173 CYS A O   1 
ATOM   1276 C  CB  . CYS A 1 181 ? -19.937 11.354  -42.346  1.00 30.97  ? 173 CYS A CB  1 
ATOM   1277 S  SG  . CYS A 1 181 ? -19.015 12.847  -41.763  1.00 34.47  ? 173 CYS A SG  1 
ATOM   1278 N  N   . GLN A 1 182 ? -18.380 9.946   -40.248  1.00 24.76  ? 174 GLN A N   1 
ATOM   1279 C  CA  . GLN A 1 182 ? -18.182 9.377   -38.922  1.00 21.90  ? 174 GLN A CA  1 
ATOM   1280 C  C   . GLN A 1 182 ? -19.465 8.744   -38.404  1.00 20.93  ? 174 GLN A C   1 
ATOM   1281 O  O   . GLN A 1 182 ? -20.513 9.385   -38.363  1.00 19.32  ? 174 GLN A O   1 
ATOM   1282 C  CB  . GLN A 1 182 ? -17.715 10.463  -37.947  1.00 21.68  ? 174 GLN A CB  1 
ATOM   1283 C  CG  . GLN A 1 182 ? -17.085 9.894   -36.681  1.00 19.62  ? 174 GLN A CG  1 
ATOM   1284 C  CD  . GLN A 1 182 ? -18.137 9.314   -35.729  1.00 25.29  ? 174 GLN A CD  1 
ATOM   1285 O  OE1 . GLN A 1 182 ? -19.293 9.750   -35.724  1.00 20.58  ? 174 GLN A OE1 1 
ATOM   1286 N  NE2 . GLN A 1 182 ? -17.763 8.263   -34.993  1.00 22.21  ? 174 GLN A NE2 1 
ATOM   1287 N  N   . GLY A 1 183 ? -19.369 7.487   -37.972  1.00 21.71  ? 175 GLY A N   1 
ATOM   1288 C  CA  . GLY A 1 183 ? -20.523 6.757   -37.500  1.00 24.51  ? 175 GLY A CA  1 
ATOM   1289 C  C   . GLY A 1 183 ? -21.203 5.885   -38.538  1.00 19.86  ? 175 GLY A C   1 
ATOM   1290 O  O   . GLY A 1 183 ? -22.008 5.019   -38.168  1.00 18.13  ? 175 GLY A O   1 
ATOM   1291 N  N   . ASP A 1 184 ? -20.942 6.114   -39.830  1.00 21.94  ? 176 ASP A N   1 
ATOM   1292 C  CA  . ASP A 1 184 ? -21.327 5.118   -40.817  1.00 21.13  ? 176 ASP A CA  1 
ATOM   1293 C  C   . ASP A 1 184 ? -20.401 3.912   -40.785  1.00 17.50  ? 176 ASP A C   1 
ATOM   1294 O  O   . ASP A 1 184 ? -20.786 2.863   -41.291  1.00 18.64  ? 176 ASP A O   1 
ATOM   1295 C  CB  . ASP A 1 184 ? -21.343 5.701   -42.228  1.00 15.78  ? 176 ASP A CB  1 
ATOM   1296 C  CG  . ASP A 1 184 ? -22.310 6.858   -42.368  1.00 22.77  ? 176 ASP A CG  1 
ATOM   1297 O  OD1 . ASP A 1 184 ? -23.439 6.781   -41.833  1.00 23.66  ? 176 ASP A OD1 1 
ATOM   1298 O  OD2 . ASP A 1 184 ? -21.961 7.839   -43.056  1.00 26.53  ? 176 ASP A OD2 1 
ATOM   1299 N  N   . SER A 1 185 ? -19.204 4.056   -40.196  1.00 18.70  ? 177 SER A N   1 
ATOM   1300 C  CA  . SER A 1 185 ? -18.212 2.990   -40.031  1.00 24.23  ? 177 SER A CA  1 
ATOM   1301 C  C   . SER A 1 185 ? -18.805 1.587   -39.949  1.00 20.27  ? 177 SER A C   1 
ATOM   1302 O  O   . SER A 1 185 ? -19.776 1.351   -39.220  1.00 19.98  ? 177 SER A O   1 
ATOM   1303 C  CB  . SER A 1 185 ? -17.369 3.226   -38.770  1.00 18.32  ? 177 SER A CB  1 
ATOM   1304 O  OG  . SER A 1 185 ? -16.331 4.170   -38.985  1.00 20.52  ? 177 SER A OG  1 
ATOM   1305 N  N   . GLY A 1 186 ? -18.215 0.649   -40.685  1.00 19.05  ? 178 GLY A N   1 
ATOM   1306 C  CA  . GLY A 1 186 ? -18.627 -0.732  -40.633  1.00 20.69  ? 178 GLY A CA  1 
ATOM   1307 C  C   . GLY A 1 186 ? -19.890 -1.049  -41.392  1.00 22.42  ? 178 GLY A C   1 
ATOM   1308 O  O   . GLY A 1 186 ? -20.219 -2.234  -41.542  1.00 22.31  ? 178 GLY A O   1 
ATOM   1309 N  N   . GLY A 1 187 ? -20.605 -0.037  -41.885  1.00 18.30  ? 179 GLY A N   1 
ATOM   1310 C  CA  . GLY A 1 187 ? -21.814 -0.241  -42.649  1.00 20.90  ? 179 GLY A CA  1 
ATOM   1311 C  C   . GLY A 1 187 ? -21.613 -0.774  -44.056  1.00 25.28  ? 179 GLY A C   1 
ATOM   1312 O  O   . GLY A 1 187 ? -20.494 -0.867  -44.582  1.00 24.93  ? 179 GLY A O   1 
ATOM   1313 N  N   . PRO A 1 188 ? -22.720 -1.123  -44.701  1.00 29.82  ? 180 PRO A N   1 
ATOM   1314 C  CA  . PRO A 1 188 ? -22.653 -1.809  -45.992  1.00 27.03  ? 180 PRO A CA  1 
ATOM   1315 C  C   . PRO A 1 188 ? -22.614 -0.878  -47.189  1.00 24.03  ? 180 PRO A C   1 
ATOM   1316 O  O   . PRO A 1 188 ? -23.167 0.219   -47.191  1.00 27.94  ? 180 PRO A O   1 
ATOM   1317 C  CB  . PRO A 1 188 ? -23.945 -2.633  -45.997  1.00 21.85  ? 180 PRO A CB  1 
ATOM   1318 C  CG  . PRO A 1 188 ? -24.885 -1.831  -45.196  1.00 23.00  ? 180 PRO A CG  1 
ATOM   1319 C  CD  . PRO A 1 188 ? -24.101 -1.012  -44.211  1.00 20.65  ? 180 PRO A CD  1 
ATOM   1320 N  N   . VAL A 1 189 ? -21.915 -1.351  -48.212  1.00 25.69  ? 181 VAL A N   1 
ATOM   1321 C  CA  . VAL A 1 189 ? -21.958 -0.813  -49.558  1.00 18.75  ? 181 VAL A CA  1 
ATOM   1322 C  C   . VAL A 1 189 ? -22.431 -1.997  -50.385  1.00 25.50  ? 181 VAL A C   1 
ATOM   1323 O  O   . VAL A 1 189 ? -21.685 -2.966  -50.598  1.00 21.66  ? 181 VAL A O   1 
ATOM   1324 C  CB  . VAL A 1 189 ? -20.589 -0.310  -50.039  1.00 28.78  ? 181 VAL A CB  1 
ATOM   1325 C  CG1 . VAL A 1 189 ? -20.723 0.560   -51.294  1.00 29.23  ? 181 VAL A CG1 1 
ATOM   1326 C  CG2 . VAL A 1 189 ? -19.858 0.396   -48.943  1.00 14.50  ? 181 VAL A CG2 1 
ATOM   1327 N  N   . VAL A 1 190 ? -23.686 -1.956  -50.799  1.00 29.89  ? 182 VAL A N   1 
ATOM   1328 C  CA  . VAL A 1 190 ? -24.328 -3.076  -51.466  1.00 27.37  ? 182 VAL A CA  1 
ATOM   1329 C  C   . VAL A 1 190 ? -24.527 -2.689  -52.914  1.00 26.75  ? 182 VAL A C   1 
ATOM   1330 O  O   . VAL A 1 190 ? -25.057 -1.613  -53.214  1.00 22.51  ? 182 VAL A O   1 
ATOM   1331 C  CB  . VAL A 1 190 ? -25.667 -3.450  -50.811  1.00 19.13  ? 182 VAL A CB  1 
ATOM   1332 C  CG1 . VAL A 1 190 ? -26.343 -4.510  -51.635  1.00 22.32  ? 182 VAL A CG1 1 
ATOM   1333 C  CG2 . VAL A 1 190 ? -25.422 -3.926  -49.406  1.00 19.65  ? 182 VAL A CG2 1 
ATOM   1334 N  N   . CYS A 1 191 ? -24.143 -3.586  -53.801  1.00 29.47  ? 183 CYS A N   1 
ATOM   1335 C  CA  . CYS A 1 191 ? -23.953 -3.265  -55.202  1.00 36.19  ? 183 CYS A CA  1 
ATOM   1336 C  C   . CYS A 1 191 ? -24.492 -4.442  -56.001  1.00 32.74  ? 183 CYS A C   1 
ATOM   1337 O  O   . CYS A 1 191 ? -23.856 -5.499  -56.042  1.00 34.17  ? 183 CYS A O   1 
ATOM   1338 C  CB  . CYS A 1 191 ? -22.466 -2.990  -55.473  1.00 38.62  ? 183 CYS A CB  1 
ATOM   1339 S  SG  . CYS A 1 191 ? -22.204 -1.557  -56.488  1.00 83.48  ? 183 CYS A SG  1 
ATOM   1340 N  N   . ASN A 1 192 ? -25.670 -4.263  -56.613  1.00 37.69  ? 184 ASN A N   1 
ATOM   1341 C  CA  . ASN A 1 192 ? -26.399 -5.348  -57.277  1.00 33.36  ? 184 ASN A CA  1 
ATOM   1342 C  C   . ASN A 1 192 ? -26.661 -6.503  -56.317  1.00 35.18  ? 184 ASN A C   1 
ATOM   1343 O  O   . ASN A 1 192 ? -26.359 -7.664  -56.610  1.00 36.55  ? 184 ASN A O   1 
ATOM   1344 C  CB  . ASN A 1 192 ? -25.662 -5.862  -58.515  1.00 38.41  ? 184 ASN A CB  1 
ATOM   1345 C  CG  . ASN A 1 192 ? -25.940 -5.042  -59.744  1.00 46.30  ? 184 ASN A CG  1 
ATOM   1346 O  OD1 . ASN A 1 192 ? -25.169 -4.153  -60.097  1.00 54.56  ? 184 ASN A OD1 1 
ATOM   1347 N  ND2 . ASN A 1 192 ? -27.076 -5.310  -60.389  1.00 59.69  ? 184 ASN A ND2 1 
ATOM   1348 N  N   . GLY A 1 193 ? -27.211 -6.175  -55.148  1.00 27.69  ? 185 GLY A N   1 
ATOM   1349 C  CA  . GLY A 1 193 ? -27.520 -7.196  -54.165  1.00 24.47  ? 185 GLY A CA  1 
ATOM   1350 C  C   . GLY A 1 193 ? -26.326 -7.914  -53.576  1.00 40.17  ? 185 GLY A C   1 
ATOM   1351 O  O   . GLY A 1 193 ? -26.494 -8.991  -52.987  1.00 39.22  ? 185 GLY A O   1 
ATOM   1352 N  N   . GLN A 1 194 ? -25.124 -7.355  -53.712  1.00 32.86  ? 186 GLN A N   1 
ATOM   1353 C  CA  . GLN A 1 194 ? -23.903 -8.000  -53.249  1.00 33.90  ? 186 GLN A CA  1 
ATOM   1354 C  C   . GLN A 1 194 ? -23.148 -7.032  -52.358  1.00 26.19  ? 186 GLN A C   1 
ATOM   1355 O  O   . GLN A 1 194 ? -22.972 -5.865  -52.718  1.00 28.16  ? 186 GLN A O   1 
ATOM   1356 C  CB  . GLN A 1 194 ? -23.022 -8.424  -54.427  1.00 34.16  ? 186 GLN A CB  1 
ATOM   1357 C  CG  . GLN A 1 194 ? -23.541 -9.634  -55.187  1.00 33.81  ? 186 GLN A CG  1 
ATOM   1358 C  CD  . GLN A 1 194 ? -22.967 -9.719  -56.603  1.00 35.94  ? 186 GLN A CD  1 
ATOM   1359 O  OE1 . GLN A 1 194 ? -21.976 -10.401 -56.837  1.00 35.99  ? 186 GLN A OE1 1 
ATOM   1360 N  NE2 . GLN A 1 194 ? -23.590 -9.015  -57.543  1.00 36.56  ? 186 GLN A NE2 1 
ATOM   1361 N  N   . LEU A 1 195 ? -22.698 -7.513  -51.204  1.00 30.38  ? 187 LEU A N   1 
ATOM   1362 C  CA  . LEU A 1 195 ? -21.930 -6.684  -50.276  1.00 22.68  ? 187 LEU A CA  1 
ATOM   1363 C  C   . LEU A 1 195 ? -20.508 -6.559  -50.794  1.00 28.48  ? 187 LEU A C   1 
ATOM   1364 O  O   . LEU A 1 195 ? -19.694 -7.456  -50.594  1.00 30.24  ? 187 LEU A O   1 
ATOM   1365 C  CB  . LEU A 1 195 ? -21.922 -7.289  -48.877  1.00 30.13  ? 187 LEU A CB  1 
ATOM   1366 C  CG  . LEU A 1 195 ? -21.235 -6.409  -47.819  1.00 21.21  ? 187 LEU A CG  1 
ATOM   1367 C  CD1 . LEU A 1 195 ? -21.944 -5.087  -47.696  1.00 19.64  ? 187 LEU A CD1 1 
ATOM   1368 C  CD2 . LEU A 1 195 ? -21.175 -7.128  -46.500  1.00 20.32  ? 187 LEU A CD2 1 
ATOM   1369 N  N   . GLN A 1 196 ? -20.189 -5.432  -51.431  1.00 23.19  ? 188 GLN A N   1 
ATOM   1370 C  CA  . GLN A 1 196 ? -18.863 -5.211  -51.995  1.00 23.56  ? 188 GLN A CA  1 
ATOM   1371 C  C   . GLN A 1 196 ? -17.973 -4.306  -51.139  1.00 23.57  ? 188 GLN A C   1 
ATOM   1372 O  O   . GLN A 1 196 ? -16.762 -4.239  -51.386  1.00 29.43  ? 188 GLN A O   1 
ATOM   1373 C  CB  . GLN A 1 196 ? -18.987 -4.601  -53.409  1.00 23.22  ? 188 GLN A CB  1 
ATOM   1374 C  CG  . GLN A 1 196 ? -19.793 -5.442  -54.411  1.00 29.04  ? 188 GLN A CG  1 
ATOM   1375 C  CD  . GLN A 1 196 ? -18.940 -6.491  -55.116  1.00 26.85  ? 188 GLN A CD  1 
ATOM   1376 O  OE1 . GLN A 1 196 ? -17.920 -6.934  -54.588  1.00 24.14  ? 188 GLN A OE1 1 
ATOM   1377 N  NE2 . GLN A 1 196 ? -19.343 -6.870  -56.322  1.00 29.63  ? 188 GLN A NE2 1 
ATOM   1378 N  N   . GLY A 1 197 ? -18.524 -3.600  -50.164  1.00 22.35  ? 189 GLY A N   1 
ATOM   1379 C  CA  . GLY A 1 197 ? -17.740 -2.638  -49.408  1.00 28.99  ? 189 GLY A CA  1 
ATOM   1380 C  C   . GLY A 1 197 ? -18.194 -2.514  -47.970  1.00 27.36  ? 189 GLY A C   1 
ATOM   1381 O  O   . GLY A 1 197 ? -19.358 -2.760  -47.635  1.00 27.98  ? 189 GLY A O   1 
ATOM   1382 N  N   . ILE A 1 198 ? -17.260 -2.122  -47.116  1.00 20.52  ? 190 ILE A N   1 
ATOM   1383 C  CA  . ILE A 1 198 ? -17.515 -1.849  -45.715  1.00 20.31  ? 190 ILE A CA  1 
ATOM   1384 C  C   . ILE A 1 198 ? -16.945 -0.472  -45.428  1.00 24.10  ? 190 ILE A C   1 
ATOM   1385 O  O   . ILE A 1 198 ? -15.755 -0.241  -45.661  1.00 21.61  ? 190 ILE A O   1 
ATOM   1386 C  CB  . ILE A 1 198 ? -16.878 -2.913  -44.817  1.00 24.34  ? 190 ILE A CB  1 
ATOM   1387 C  CG1 . ILE A 1 198 ? -17.539 -4.259  -45.098  1.00 29.10  ? 190 ILE A CG1 1 
ATOM   1388 C  CG2 . ILE A 1 198 ? -16.968 -2.532  -43.337  1.00 21.77  ? 190 ILE A CG2 1 
ATOM   1389 C  CD1 . ILE A 1 198 ? -16.748 -5.410  -44.583  1.00 26.77  ? 190 ILE A CD1 1 
ATOM   1390 N  N   . VAL A 1 199 ? -17.795 0.460   -44.987  1.00 24.37  ? 191 VAL A N   1 
ATOM   1391 C  CA  . VAL A 1 199 ? -17.312 1.807   -44.670  1.00 23.85  ? 191 VAL A CA  1 
ATOM   1392 C  C   . VAL A 1 199 ? -16.094 1.697   -43.767  1.00 21.86  ? 191 VAL A C   1 
ATOM   1393 O  O   . VAL A 1 199 ? -16.168 1.088   -42.686  1.00 16.71  ? 191 VAL A O   1 
ATOM   1394 C  CB  . VAL A 1 199 ? -18.389 2.677   -43.995  1.00 26.04  ? 191 VAL A CB  1 
ATOM   1395 C  CG1 . VAL A 1 199 ? -17.833 4.061   -43.746  1.00 16.37  ? 191 VAL A CG1 1 
ATOM   1396 C  CG2 . VAL A 1 199 ? -19.672 2.742   -44.838  1.00 23.19  ? 191 VAL A CG2 1 
ATOM   1397 N  N   . SER A 1 200 ? -14.967 2.281   -44.199  1.00 17.69  ? 192 SER A N   1 
ATOM   1398 C  CA  . SER A 1 200 ? -13.721 2.120   -43.455  1.00 22.27  ? 192 SER A CA  1 
ATOM   1399 C  C   . SER A 1 200 ? -13.134 3.436   -42.970  1.00 21.74  ? 192 SER A C   1 
ATOM   1400 O  O   . SER A 1 200 ? -12.756 3.541   -41.797  1.00 21.87  ? 192 SER A O   1 
ATOM   1401 C  CB  . SER A 1 200 ? -12.678 1.361   -44.301  1.00 21.56  ? 192 SER A CB  1 
ATOM   1402 O  OG  . SER A 1 200 ? -11.544 1.023   -43.507  1.00 21.66  ? 192 SER A OG  1 
ATOM   1403 N  N   . TRP A 1 201 ? -13.034 4.442   -43.832  1.00 18.54  ? 193 TRP A N   1 
ATOM   1404 C  CA  . TRP A 1 201 ? -12.377 5.681   -43.443  1.00 19.59  ? 193 TRP A CA  1 
ATOM   1405 C  C   . TRP A 1 201 ? -12.546 6.709   -44.543  1.00 22.89  ? 193 TRP A C   1 
ATOM   1406 O  O   . TRP A 1 201 ? -12.916 6.382   -45.676  1.00 25.04  ? 193 TRP A O   1 
ATOM   1407 C  CB  . TRP A 1 201 ? -10.887 5.473   -43.130  1.00 21.76  ? 193 TRP A CB  1 
ATOM   1408 C  CG  . TRP A 1 201 ? -10.002 5.010   -44.243  1.00 25.13  ? 193 TRP A CG  1 
ATOM   1409 C  CD1 . TRP A 1 201 ? -9.740  3.717   -44.601  1.00 26.50  ? 193 TRP A CD1 1 
ATOM   1410 C  CD2 . TRP A 1 201 ? -9.195  5.835   -45.108  1.00 28.67  ? 193 TRP A CD2 1 
ATOM   1411 N  NE1 . TRP A 1 201 ? -8.843  3.688   -45.652  1.00 23.93  ? 193 TRP A NE1 1 
ATOM   1412 C  CE2 . TRP A 1 201 ? -8.495  4.972   -45.977  1.00 27.57  ? 193 TRP A CE2 1 
ATOM   1413 C  CE3 . TRP A 1 201 ? -9.003  7.215   -45.234  1.00 28.40  ? 193 TRP A CE3 1 
ATOM   1414 C  CZ2 . TRP A 1 201 ? -7.623  5.447   -46.953  1.00 31.53  ? 193 TRP A CZ2 1 
ATOM   1415 C  CZ3 . TRP A 1 201 ? -8.131  7.682   -46.203  1.00 29.32  ? 193 TRP A CZ3 1 
ATOM   1416 C  CH2 . TRP A 1 201 ? -7.453  6.799   -47.048  1.00 28.62  ? 193 TRP A CH2 1 
ATOM   1417 N  N   . GLY A 1 202 ? -12.281 7.964   -44.177  1.00 28.91  ? 194 GLY A N   1 
ATOM   1418 C  CA  . GLY A 1 202 ? -12.275 9.081   -45.107  1.00 26.83  ? 194 GLY A CA  1 
ATOM   1419 C  C   . GLY A 1 202 ? -11.481 10.253  -44.563  1.00 29.26  ? 194 GLY A C   1 
ATOM   1420 O  O   . GLY A 1 202 ? -11.106 10.297  -43.388  1.00 26.00  ? 194 GLY A O   1 
ATOM   1421 N  N   . TYR A 1 203 ? -11.222 11.209  -45.452  1.00 29.11  ? 195 TYR A N   1 
ATOM   1422 C  CA  . TYR A 1 203 ? -10.549 12.455  -45.110  1.00 27.07  ? 195 TYR A CA  1 
ATOM   1423 C  C   . TYR A 1 203 ? -11.572 13.563  -45.284  1.00 28.39  ? 195 TYR A C   1 
ATOM   1424 O  O   . TYR A 1 203 ? -11.886 13.953  -46.411  1.00 24.95  ? 195 TYR A O   1 
ATOM   1425 C  CB  . TYR A 1 203 ? -9.313  12.707  -45.973  1.00 23.92  ? 195 TYR A CB  1 
ATOM   1426 C  CG  . TYR A 1 203 ? -8.586  13.950  -45.520  1.00 31.06  ? 195 TYR A CG  1 
ATOM   1427 C  CD1 . TYR A 1 203 ? -8.853  15.188  -46.096  1.00 30.15  ? 195 TYR A CD1 1 
ATOM   1428 C  CD2 . TYR A 1 203 ? -7.666  13.897  -44.477  1.00 35.86  ? 195 TYR A CD2 1 
ATOM   1429 C  CE1 . TYR A 1 203 ? -8.211  16.331  -45.660  1.00 36.23  ? 195 TYR A CE1 1 
ATOM   1430 C  CE2 . TYR A 1 203 ? -7.010  15.035  -44.039  1.00 28.99  ? 195 TYR A CE2 1 
ATOM   1431 C  CZ  . TYR A 1 203 ? -7.290  16.245  -44.628  1.00 40.06  ? 195 TYR A CZ  1 
ATOM   1432 O  OH  . TYR A 1 203 ? -6.643  17.371  -44.184  1.00 44.35  ? 195 TYR A OH  1 
ATOM   1433 N  N   . GLY A 1 204 ? -12.072 14.082  -44.163  1.00 30.11  ? 196 GLY A N   1 
ATOM   1434 C  CA  . GLY A 1 204 ? -13.197 14.993  -44.189  1.00 26.01  ? 196 GLY A CA  1 
ATOM   1435 C  C   . GLY A 1 204 ? -14.428 14.233  -44.619  1.00 30.78  ? 196 GLY A C   1 
ATOM   1436 O  O   . GLY A 1 204 ? -14.412 13.008  -44.772  1.00 30.27  ? 196 GLY A O   1 
ATOM   1437 N  N   A CYS A 1 205 ? -15.523 14.968  -44.804  0.99 33.52  ? 197 CYS A N   1 
ATOM   1438 N  N   B CYS A 1 205 ? -15.505 14.973  -44.867  0.01 32.95  ? 197 CYS A N   1 
ATOM   1439 C  CA  A CYS A 1 205 ? -16.765 14.365  -45.274  0.99 32.94  ? 197 CYS A CA  1 
ATOM   1440 C  CA  B CYS A 1 205 ? -16.768 14.363  -45.264  0.01 32.29  ? 197 CYS A CA  1 
ATOM   1441 C  C   A CYS A 1 205 ? -17.302 15.147  -46.464  0.99 32.38  ? 197 CYS A C   1 
ATOM   1442 C  C   B CYS A 1 205 ? -17.358 15.131  -46.436  0.01 32.34  ? 197 CYS A C   1 
ATOM   1443 O  O   A CYS A 1 205 ? -17.464 16.372  -46.395  0.99 32.82  ? 197 CYS A O   1 
ATOM   1444 O  O   B CYS A 1 205 ? -17.631 16.331  -46.321  0.01 33.22  ? 197 CYS A O   1 
ATOM   1445 C  CB  A CYS A 1 205 ? -17.784 14.304  -44.143  0.99 33.91  ? 197 CYS A CB  1 
ATOM   1446 C  CB  B CYS A 1 205 ? -17.741 14.324  -44.087  0.01 34.10  ? 197 CYS A CB  1 
ATOM   1447 S  SG  A CYS A 1 205 ? -17.345 13.006  -42.917  0.99 43.83  ? 197 CYS A SG  1 
ATOM   1448 S  SG  B CYS A 1 205 ? -17.413 12.922  -43.000  0.01 42.35  ? 197 CYS A SG  1 
ATOM   1449 N  N   . ALA A 1 206 ? -17.553 14.432  -47.558  1.00 30.05  ? 198 ALA A N   1 
ATOM   1450 C  CA  . ALA A 1 206 ? -18.112 15.017  -48.775  1.00 30.43  ? 198 ALA A CA  1 
ATOM   1451 C  C   . ALA A 1 206 ? -17.297 16.209  -49.280  1.00 34.27  ? 198 ALA A C   1 
ATOM   1452 O  O   . ALA A 1 206 ? -17.847 17.153  -49.844  1.00 31.86  ? 198 ALA A O   1 
ATOM   1453 C  CB  . ALA A 1 206 ? -19.576 15.406  -48.579  1.00 27.49  ? 198 ALA A CB  1 
ATOM   1454 N  N   . GLN A 1 207 ? -15.980 16.174  -49.085  1.00 31.92  ? 199 GLN A N   1 
ATOM   1455 C  CA  . GLN A 1 207 ? -15.096 17.174  -49.659  1.00 26.21  ? 199 GLN A CA  1 
ATOM   1456 C  C   . GLN A 1 207 ? -14.694 16.757  -51.071  1.00 26.78  ? 199 GLN A C   1 
ATOM   1457 O  O   . GLN A 1 207 ? -14.679 15.573  -51.412  1.00 27.08  ? 199 GLN A O   1 
ATOM   1458 C  CB  . GLN A 1 207 ? -13.843 17.377  -48.793  1.00 23.25  ? 199 GLN A CB  1 
ATOM   1459 C  CG  . GLN A 1 207 ? -14.107 17.864  -47.364  1.00 33.16  ? 199 GLN A CG  1 
ATOM   1460 C  CD  . GLN A 1 207 ? -14.886 19.188  -47.312  1.00 43.48  ? 199 GLN A CD  1 
ATOM   1461 O  OE1 . GLN A 1 207 ? -14.481 20.194  -47.906  1.00 44.10  ? 199 GLN A OE1 1 
ATOM   1462 N  NE2 . GLN A 1 207 ? -16.026 19.177  -46.619  1.00 43.21  ? 199 GLN A NE2 1 
ATOM   1463 N  N   . LYS A 1 208 ? -14.337 17.755  -51.883  1.00 27.61  ? 200 LYS A N   1 
ATOM   1464 C  CA  . LYS A 1 208 ? -13.895 17.508  -53.252  1.00 35.44  ? 200 LYS A CA  1 
ATOM   1465 C  C   . LYS A 1 208 ? -12.678 16.591  -53.294  1.00 33.06  ? 200 LYS A C   1 
ATOM   1466 O  O   . LYS A 1 208 ? -11.740 16.745  -52.511  1.00 32.72  ? 200 LYS A O   1 
ATOM   1467 C  CB  . LYS A 1 208 ? -13.561 18.830  -53.942  1.00 37.91  ? 200 LYS A CB  1 
ATOM   1468 C  CG  . LYS A 1 208 ? -14.371 19.085  -55.205  1.00 53.19  ? 200 LYS A CG  1 
ATOM   1469 C  CD  . LYS A 1 208 ? -14.268 20.543  -55.679  1.00 62.12  ? 200 LYS A CD  1 
ATOM   1470 C  CE  . LYS A 1 208 ? -15.210 20.837  -56.862  1.00 58.58  ? 200 LYS A CE  1 
ATOM   1471 N  NZ  . LYS A 1 208 ? -16.591 20.286  -56.680  1.00 49.71  ? 200 LYS A NZ  1 
ATOM   1472 N  N   A ASN A 1 209 ? -12.701 15.628  -54.213  0.37 34.99  ? 201 ASN A N   1 
ATOM   1473 N  N   B ASN A 1 209 ? -12.709 15.630  -54.226  0.63 35.01  ? 201 ASN A N   1 
ATOM   1474 C  CA  A ASN A 1 209 ? -11.555 14.753  -54.460  0.37 33.69  ? 201 ASN A CA  1 
ATOM   1475 C  CA  B ASN A 1 209 ? -11.608 14.687  -54.486  0.63 33.66  ? 201 ASN A CA  1 
ATOM   1476 C  C   A ASN A 1 209 ? -11.188 13.922  -53.228  0.37 33.17  ? 201 ASN A C   1 
ATOM   1477 C  C   B ASN A 1 209 ? -11.200 13.909  -53.238  0.63 33.42  ? 201 ASN A C   1 
ATOM   1478 O  O   A ASN A 1 209 ? -10.037 13.499  -53.080  0.37 31.26  ? 201 ASN A O   1 
ATOM   1479 O  O   B ASN A 1 209 ? -10.037 13.510  -53.093  0.63 31.57  ? 201 ASN A O   1 
ATOM   1480 C  CB  A ASN A 1 209 ? -10.342 15.562  -54.950  0.37 34.17  ? 201 ASN A CB  1 
ATOM   1481 C  CB  B ASN A 1 209 ? -10.392 15.392  -55.100  0.63 34.16  ? 201 ASN A CB  1 
ATOM   1482 C  CG  A ASN A 1 209 ? -10.739 16.738  -55.842  0.37 38.87  ? 201 ASN A CG  1 
ATOM   1483 C  CG  B ASN A 1 209 ? -9.526  14.450  -55.941  0.63 36.65  ? 201 ASN A CG  1 
ATOM   1484 O  OD1 A ASN A 1 209 ? -11.569 16.589  -56.738  0.37 38.99  ? 201 ASN A OD1 1 
ATOM   1485 O  OD1 B ASN A 1 209 ? -10.031 13.543  -56.608  0.63 30.52  ? 201 ASN A OD1 1 
ATOM   1486 N  ND2 A ASN A 1 209 ? -10.155 17.913  -55.593  0.37 33.30  ? 201 ASN A ND2 1 
ATOM   1487 N  ND2 B ASN A 1 209 ? -8.209  14.662  -55.900  0.63 35.41  ? 201 ASN A ND2 1 
ATOM   1488 N  N   . LYS A 1 210 ? -12.156 13.678  -52.337  1.00 29.44  ? 202 LYS A N   1 
ATOM   1489 C  CA  . LYS A 1 210 ? -11.927 12.919  -51.097  1.00 31.70  ? 202 LYS A CA  1 
ATOM   1490 C  C   . LYS A 1 210 ? -13.109 12.004  -50.823  1.00 32.90  ? 202 LYS A C   1 
ATOM   1491 O  O   . LYS A 1 210 ? -13.849 12.185  -49.845  1.00 28.70  ? 202 LYS A O   1 
ATOM   1492 C  CB  . LYS A 1 210 ? -11.700 13.852  -49.904  1.00 22.98  ? 202 LYS A CB  1 
ATOM   1493 C  CG  . LYS A 1 210 ? -10.405 14.647  -49.956  1.00 32.74  ? 202 LYS A CG  1 
ATOM   1494 C  CD  . LYS A 1 210 ? -9.206  13.720  -50.011  1.00 31.60  ? 202 LYS A CD  1 
ATOM   1495 C  CE  . LYS A 1 210 ? -8.035  14.421  -50.654  1.00 43.73  ? 202 LYS A CE  1 
ATOM   1496 N  NZ  . LYS A 1 210 ? -6.761  14.001  -50.009  1.00 38.16  ? 202 LYS A NZ  1 
ATOM   1497 N  N   . PRO A 1 211 ? -13.323 11.004  -51.669  1.00 34.18  ? 203 PRO A N   1 
ATOM   1498 C  CA  . PRO A 1 211 ? -14.434 10.075  -51.432  1.00 20.86  ? 203 PRO A CA  1 
ATOM   1499 C  C   . PRO A 1 211 ? -14.178 9.203   -50.212  1.00 26.56  ? 203 PRO A C   1 
ATOM   1500 O  O   . PRO A 1 211 ? -13.068 9.119   -49.680  1.00 22.05  ? 203 PRO A O   1 
ATOM   1501 C  CB  . PRO A 1 211 ? -14.476 9.242   -52.714  1.00 20.81  ? 203 PRO A CB  1 
ATOM   1502 C  CG  . PRO A 1 211 ? -13.042 9.280   -53.209  1.00 27.82  ? 203 PRO A CG  1 
ATOM   1503 C  CD  . PRO A 1 211 ? -12.580 10.679  -52.908  1.00 20.90  ? 203 PRO A CD  1 
ATOM   1504 N  N   . GLY A 1 212 ? -15.245 8.537   -49.773  1.00 28.16  ? 204 GLY A N   1 
ATOM   1505 C  CA  . GLY A 1 212 ? -15.101 7.531   -48.741  1.00 23.45  ? 204 GLY A CA  1 
ATOM   1506 C  C   . GLY A 1 212 ? -14.301 6.340   -49.229  1.00 29.64  ? 204 GLY A C   1 
ATOM   1507 O  O   . GLY A 1 212 ? -14.326 5.990   -50.415  1.00 20.87  ? 204 GLY A O   1 
ATOM   1508 N  N   . VAL A 1 213 ? -13.573 5.722   -48.292  1.00 21.70  ? 205 VAL A N   1 
ATOM   1509 C  CA  . VAL A 1 213 ? -12.782 4.523   -48.545  1.00 23.38  ? 205 VAL A CA  1 
ATOM   1510 C  C   . VAL A 1 213 ? -13.430 3.310   -47.876  1.00 24.69  ? 205 VAL A C   1 
ATOM   1511 O  O   . VAL A 1 213 ? -13.845 3.364   -46.708  1.00 23.49  ? 205 VAL A O   1 
ATOM   1512 C  CB  . VAL A 1 213 ? -11.337 4.718   -48.056  1.00 25.99  ? 205 VAL A CB  1 
ATOM   1513 C  CG1 . VAL A 1 213 ? -10.473 3.546   -48.491  1.00 20.13  ? 205 VAL A CG1 1 
ATOM   1514 C  CG2 . VAL A 1 213 ? -10.798 6.025   -48.604  1.00 21.40  ? 205 VAL A CG2 1 
ATOM   1515 N  N   . TYR A 1 214 ? -13.481 2.202   -48.609  1.00 22.99  ? 206 TYR A N   1 
ATOM   1516 C  CA  . TYR A 1 214 ? -14.266 1.037   -48.228  1.00 21.27  ? 206 TYR A CA  1 
ATOM   1517 C  C   . TYR A 1 214 ? -13.422 -0.218  -48.354  1.00 27.46  ? 206 TYR A C   1 
ATOM   1518 O  O   . TYR A 1 214 ? -12.689 -0.398  -49.337  1.00 25.80  ? 206 TYR A O   1 
ATOM   1519 C  CB  . TYR A 1 214 ? -15.541 0.920   -49.106  1.00 15.05  ? 206 TYR A CB  1 
ATOM   1520 C  CG  . TYR A 1 214 ? -16.425 2.133   -49.018  1.00 19.50  ? 206 TYR A CG  1 
ATOM   1521 C  CD1 . TYR A 1 214 ? -17.430 2.217   -48.058  1.00 22.46  ? 206 TYR A CD1 1 
ATOM   1522 C  CD2 . TYR A 1 214 ? -16.214 3.235   -49.849  1.00 25.67  ? 206 TYR A CD2 1 
ATOM   1523 C  CE1 . TYR A 1 214 ? -18.255 3.350   -47.961  1.00 22.84  ? 206 TYR A CE1 1 
ATOM   1524 C  CE2 . TYR A 1 214 ? -17.012 4.369   -49.754  1.00 19.67  ? 206 TYR A CE2 1 
ATOM   1525 C  CZ  . TYR A 1 214 ? -18.030 4.419   -48.810  1.00 20.98  ? 206 TYR A CZ  1 
ATOM   1526 O  OH  . TYR A 1 214 ? -18.810 5.539   -48.713  1.00 26.00  ? 206 TYR A OH  1 
ATOM   1527 N  N   . THR A 1 215 ? -13.526 -1.087  -47.357  1.00 22.47  ? 207 THR A N   1 
ATOM   1528 C  CA  . THR A 1 215 ? -12.838 -2.362  -47.452  1.00 22.63  ? 207 THR A CA  1 
ATOM   1529 C  C   . THR A 1 215 ? -13.430 -3.160  -48.600  1.00 28.39  ? 207 THR A C   1 
ATOM   1530 O  O   . THR A 1 215 ? -14.655 -3.245  -48.742  1.00 30.90  ? 207 THR A O   1 
ATOM   1531 C  CB  . THR A 1 215 ? -12.943 -3.131  -46.140  1.00 22.72  ? 207 THR A CB  1 
ATOM   1532 O  OG1 . THR A 1 215 ? -12.260 -2.407  -45.106  1.00 27.48  ? 207 THR A OG1 1 
ATOM   1533 C  CG2 . THR A 1 215 ? -12.309 -4.516  -46.286  1.00 25.73  ? 207 THR A CG2 1 
ATOM   1534 N  N   . LYS A 1 216 ? -12.552 -3.719  -49.435  1.00 21.88  ? 208 LYS A N   1 
ATOM   1535 C  CA  . LYS A 1 216 ? -12.945 -4.424  -50.657  1.00 24.64  ? 208 LYS A CA  1 
ATOM   1536 C  C   . LYS A 1 216 ? -13.381 -5.835  -50.290  1.00 24.00  ? 208 LYS A C   1 
ATOM   1537 O  O   . LYS A 1 216 ? -12.555 -6.741  -50.191  1.00 26.41  ? 208 LYS A O   1 
ATOM   1538 C  CB  . LYS A 1 216 ? -11.786 -4.436  -51.648  1.00 27.46  ? 208 LYS A CB  1 
ATOM   1539 C  CG  . LYS A 1 216 ? -12.152 -4.795  -53.066  1.00 32.01  ? 208 LYS A CG  1 
ATOM   1540 C  CD  . LYS A 1 216 ? -10.942 -5.330  -53.804  1.00 43.41  ? 208 LYS A CD  1 
ATOM   1541 C  CE  . LYS A 1 216 ? -10.799 -4.711  -55.188  1.00 39.97  ? 208 LYS A CE  1 
ATOM   1542 N  NZ  . LYS A 1 216 ? -12.053 -4.820  -55.980  1.00 52.17  ? 208 LYS A NZ  1 
ATOM   1543 N  N   . VAL A 1 217 ? -14.695 -6.039  -50.123  1.00 20.25  ? 209 VAL A N   1 
ATOM   1544 C  CA  . VAL A 1 217 ? -15.178 -7.294  -49.550  1.00 20.53  ? 209 VAL A CA  1 
ATOM   1545 C  C   . VAL A 1 217 ? -14.854 -8.505  -50.430  1.00 24.72  ? 209 VAL A C   1 
ATOM   1546 O  O   . VAL A 1 217 ? -14.646 -9.611  -49.916  1.00 24.83  ? 209 VAL A O   1 
ATOM   1547 C  CB  . VAL A 1 217 ? -16.683 -7.187  -49.252  1.00 23.88  ? 209 VAL A CB  1 
ATOM   1548 C  CG1 . VAL A 1 217 ? -17.249 -8.549  -48.738  1.00 26.96  ? 209 VAL A CG1 1 
ATOM   1549 C  CG2 . VAL A 1 217 ? -16.913 -6.100  -48.213  1.00 25.27  ? 209 VAL A CG2 1 
ATOM   1550 N  N   . CYS A 1 218 ? -14.800 -8.330  -51.756  1.00 23.88  ? 210 CYS A N   1 
ATOM   1551 C  CA  . CYS A 1 218 ? -14.545 -9.468  -52.627  1.00 35.46  ? 210 CYS A CA  1 
ATOM   1552 C  C   . CYS A 1 218 ? -13.167 -10.079 -52.386  1.00 35.21  ? 210 CYS A C   1 
ATOM   1553 O  O   . CYS A 1 218 ? -12.965 -11.252 -52.709  1.00 34.09  ? 210 CYS A O   1 
ATOM   1554 C  CB  . CYS A 1 218 ? -14.719 -9.064  -54.092  1.00 38.83  ? 210 CYS A CB  1 
ATOM   1555 S  SG  . CYS A 1 218 ? -13.467 -7.922  -54.682  1.00 38.72  ? 210 CYS A SG  1 
ATOM   1556 N  N   . ASN A 1 219 ? -12.239 -9.336  -51.782  1.00 27.53  ? 211 ASN A N   1 
ATOM   1557 C  CA  . ASN A 1 219 ? -10.947 -9.883  -51.374  1.00 29.76  ? 211 ASN A CA  1 
ATOM   1558 C  C   . ASN A 1 219 ? -11.021 -10.729 -50.106  1.00 36.17  ? 211 ASN A C   1 
ATOM   1559 O  O   . ASN A 1 219 ? -9.979  -11.213 -49.632  1.00 37.05  ? 211 ASN A O   1 
ATOM   1560 C  CB  . ASN A 1 219 ? -9.927  -8.756  -51.148  1.00 25.94  ? 211 ASN A CB  1 
ATOM   1561 C  CG  . ASN A 1 219 ? -9.366  -8.214  -52.445  1.00 30.13  ? 211 ASN A CG  1 
ATOM   1562 O  OD1 . ASN A 1 219 ? -9.782  -8.625  -53.522  1.00 32.33  ? 211 ASN A OD1 1 
ATOM   1563 N  ND2 . ASN A 1 219 ? -8.410  -7.294  -52.348  1.00 32.42  ? 211 ASN A ND2 1 
ATOM   1564 N  N   . TYR A 1 220 ? -12.204 -10.915 -49.526  1.00 26.87  ? 212 TYR A N   1 
ATOM   1565 C  CA  . TYR A 1 220 ? -12.275 -11.577 -48.234  1.00 29.23  ? 212 TYR A CA  1 
ATOM   1566 C  C   . TYR A 1 220 ? -13.301 -12.696 -48.189  1.00 25.81  ? 212 TYR A C   1 
ATOM   1567 O  O   . TYR A 1 220 ? -13.530 -13.258 -47.110  1.00 26.96  ? 212 TYR A O   1 
ATOM   1568 C  CB  . TYR A 1 220 ? -12.567 -10.547 -47.146  1.00 21.23  ? 212 TYR A CB  1 
ATOM   1569 C  CG  . TYR A 1 220 ? -11.464 -9.522  -47.027  1.00 28.28  ? 212 TYR A CG  1 
ATOM   1570 C  CD1 . TYR A 1 220 ? -10.319 -9.785  -46.282  1.00 28.85  ? 212 TYR A CD1 1 
ATOM   1571 C  CD2 . TYR A 1 220 ? -11.561 -8.293  -47.664  1.00 23.03  ? 212 TYR A CD2 1 
ATOM   1572 C  CE1 . TYR A 1 220 ? -9.306  -8.846  -46.166  1.00 24.02  ? 212 TYR A CE1 1 
ATOM   1573 C  CE2 . TYR A 1 220 ? -10.548 -7.347  -47.558  1.00 27.89  ? 212 TYR A CE2 1 
ATOM   1574 C  CZ  . TYR A 1 220 ? -9.421  -7.633  -46.809  1.00 28.94  ? 212 TYR A CZ  1 
ATOM   1575 O  OH  . TYR A 1 220 ? -8.407  -6.705  -46.699  1.00 33.97  ? 212 TYR A OH  1 
ATOM   1576 N  N   . VAL A 1 221 ? -13.913 -13.047 -49.324  1.00 26.14  ? 213 VAL A N   1 
ATOM   1577 C  CA  . VAL A 1 221 ? -15.017 -14.000 -49.279  1.00 29.19  ? 213 VAL A CA  1 
ATOM   1578 C  C   . VAL A 1 221 ? -14.541 -15.342 -48.743  1.00 33.14  ? 213 VAL A C   1 
ATOM   1579 O  O   . VAL A 1 221 ? -15.274 -16.040 -48.028  1.00 29.66  ? 213 VAL A O   1 
ATOM   1580 C  CB  . VAL A 1 221 ? -15.672 -14.146 -50.659  1.00 30.51  ? 213 VAL A CB  1 
ATOM   1581 C  CG1 . VAL A 1 221 ? -16.823 -15.156 -50.574  1.00 32.93  ? 213 VAL A CG1 1 
ATOM   1582 C  CG2 . VAL A 1 221 ? -16.154 -12.788 -51.176  1.00 28.90  ? 213 VAL A CG2 1 
ATOM   1583 N  N   . ASN A 1 222 ? -13.302 -15.716 -49.062  1.00 28.04  ? 214 ASN A N   1 
ATOM   1584 C  CA  . ASN A 1 222 ? -12.775 -16.978 -48.562  1.00 32.72  ? 214 ASN A CA  1 
ATOM   1585 C  C   . ASN A 1 222 ? -12.622 -16.931 -47.056  1.00 31.60  ? 214 ASN A C   1 
ATOM   1586 O  O   . ASN A 1 222 ? -13.059 -17.847 -46.348  1.00 33.36  ? 214 ASN A O   1 
ATOM   1587 C  CB  . ASN A 1 222 ? -11.439 -17.304 -49.227  1.00 38.70  ? 214 ASN A CB  1 
ATOM   1588 C  CG  . ASN A 1 222 ? -11.563 -17.433 -50.724  1.00 51.43  ? 214 ASN A CG  1 
ATOM   1589 O  OD1 . ASN A 1 222 ? -10.769 -16.860 -51.481  1.00 46.13  ? 214 ASN A OD1 1 
ATOM   1590 N  ND2 . ASN A 1 222 ? -12.589 -18.160 -51.168  1.00 47.39  ? 214 ASN A ND2 1 
ATOM   1591 N  N   . TRP A 1 223 ? -12.016 -15.860 -46.549  1.00 22.31  ? 215 TRP A N   1 
ATOM   1592 C  CA  . TRP A 1 223 ? -11.810 -15.747 -45.116  1.00 26.29  ? 215 TRP A CA  1 
ATOM   1593 C  C   . TRP A 1 223 ? -13.135 -15.759 -44.380  1.00 27.63  ? 215 TRP A C   1 
ATOM   1594 O  O   . TRP A 1 223 ? -13.259 -16.396 -43.330  1.00 28.09  ? 215 TRP A O   1 
ATOM   1595 C  CB  . TRP A 1 223 ? -11.026 -14.474 -44.789  1.00 30.61  ? 215 TRP A CB  1 
ATOM   1596 C  CG  . TRP A 1 223 ? -10.841 -14.263 -43.321  1.00 31.07  ? 215 TRP A CG  1 
ATOM   1597 C  CD1 . TRP A 1 223 ? -9.982  -14.933 -42.497  1.00 25.37  ? 215 TRP A CD1 1 
ATOM   1598 C  CD2 . TRP A 1 223 ? -11.542 -13.322 -42.494  1.00 31.98  ? 215 TRP A CD2 1 
ATOM   1599 N  NE1 . TRP A 1 223 ? -10.104 -14.468 -41.198  1.00 25.96  ? 215 TRP A NE1 1 
ATOM   1600 C  CE2 . TRP A 1 223 ? -11.047 -13.473 -41.173  1.00 35.07  ? 215 TRP A CE2 1 
ATOM   1601 C  CE3 . TRP A 1 223 ? -12.534 -12.361 -42.742  1.00 29.55  ? 215 TRP A CE3 1 
ATOM   1602 C  CZ2 . TRP A 1 223 ? -11.509 -12.697 -40.107  1.00 30.06  ? 215 TRP A CZ2 1 
ATOM   1603 C  CZ3 . TRP A 1 223 ? -12.993 -11.599 -41.692  1.00 25.00  ? 215 TRP A CZ3 1 
ATOM   1604 C  CH2 . TRP A 1 223 ? -12.486 -11.773 -40.384  1.00 34.48  ? 215 TRP A CH2 1 
ATOM   1605 N  N   . ILE A 1 224 ? -14.141 -15.071 -44.926  1.00 28.67  ? 216 ILE A N   1 
ATOM   1606 C  CA  . ILE A 1 224 ? -15.439 -14.993 -44.257  1.00 34.50  ? 216 ILE A CA  1 
ATOM   1607 C  C   . ILE A 1 224 ? -16.061 -16.383 -44.149  1.00 34.68  ? 216 ILE A C   1 
ATOM   1608 O  O   . ILE A 1 224 ? -16.362 -16.863 -43.046  1.00 31.11  ? 216 ILE A O   1 
ATOM   1609 C  CB  . ILE A 1 224 ? -16.357 -13.981 -44.981  1.00 27.38  ? 216 ILE A CB  1 
ATOM   1610 C  CG1 . ILE A 1 224 ? -15.798 -12.562 -44.805  1.00 26.15  ? 216 ILE A CG1 1 
ATOM   1611 C  CG2 . ILE A 1 224 ? -17.782 -14.064 -44.481  1.00 19.10  ? 216 ILE A CG2 1 
ATOM   1612 C  CD1 . ILE A 1 224 ? -16.105 -11.608 -45.907  1.00 19.13  ? 216 ILE A CD1 1 
ATOM   1613 N  N   . GLN A 1 225 ? -16.192 -17.077 -45.287  1.00 29.64  ? 217 GLN A N   1 
ATOM   1614 C  CA  . GLN A 1 225 ? -16.815 -18.398 -45.280  1.00 27.57  ? 217 GLN A CA  1 
ATOM   1615 C  C   . GLN A 1 225 ? -16.022 -19.388 -44.439  1.00 28.07  ? 217 GLN A C   1 
ATOM   1616 O  O   . GLN A 1 225 ? -16.598 -20.230 -43.743  1.00 28.92  ? 217 GLN A O   1 
ATOM   1617 C  CB  . GLN A 1 225 ? -16.968 -18.896 -46.708  1.00 26.64  ? 217 GLN A CB  1 
ATOM   1618 C  CG  . GLN A 1 225 ? -17.892 -17.993 -47.520  1.00 37.04  ? 217 GLN A CG  1 
ATOM   1619 C  CD  . GLN A 1 225 ? -17.934 -18.353 -48.978  1.00 31.52  ? 217 GLN A CD  1 
ATOM   1620 O  OE1 . GLN A 1 225 ? -16.959 -18.831 -49.538  1.00 39.71  ? 217 GLN A OE1 1 
ATOM   1621 N  NE2 . GLN A 1 225 ? -19.066 -18.117 -49.607  1.00 43.36  ? 217 GLN A NE2 1 
ATOM   1622 N  N   . GLN A 1 226 ? -14.702 -19.294 -44.466  1.00 28.33  ? 218 GLN A N   1 
ATOM   1623 C  CA  . GLN A 1 226 ? -13.918 -20.258 -43.703  1.00 33.80  ? 218 GLN A CA  1 
ATOM   1624 C  C   . GLN A 1 226 ? -13.967 -19.950 -42.207  1.00 34.81  ? 218 GLN A C   1 
ATOM   1625 O  O   . GLN A 1 226 ? -14.111 -20.865 -41.383  1.00 26.25  ? 218 GLN A O   1 
ATOM   1626 C  CB  . GLN A 1 226 ? -12.485 -20.264 -44.215  1.00 28.67  ? 218 GLN A CB  1 
ATOM   1627 C  CG  . GLN A 1 226 ? -12.233 -21.200 -45.380  1.00 45.18  ? 218 GLN A CG  1 
ATOM   1628 C  CD  . GLN A 1 226 ? -11.104 -20.696 -46.258  1.00 54.38  ? 218 GLN A CD  1 
ATOM   1629 O  OE1 . GLN A 1 226 ? -10.114 -20.144 -45.762  1.00 43.39  ? 218 GLN A OE1 1 
ATOM   1630 N  NE2 . GLN A 1 226 ? -11.237 -20.898 -47.571  1.00 67.52  ? 218 GLN A NE2 1 
ATOM   1631 N  N   . THR A 1 227 ? -13.853 -18.668 -41.841  1.00 27.39  ? 219 THR A N   1 
ATOM   1632 C  CA  . THR A 1 227 ? -13.956 -18.287 -40.435  1.00 31.61  ? 219 THR A CA  1 
ATOM   1633 C  C   . THR A 1 227 ? -15.338 -18.603 -39.882  1.00 25.28  ? 219 THR A C   1 
ATOM   1634 O  O   . THR A 1 227 ? -15.461 -19.081 -38.750  1.00 25.11  ? 219 THR A O   1 
ATOM   1635 C  CB  . THR A 1 227 ? -13.620 -16.800 -40.253  1.00 30.55  ? 219 THR A CB  1 
ATOM   1636 O  OG1 . THR A 1 227 ? -12.315 -16.542 -40.775  1.00 34.95  ? 219 THR A OG1 1 
ATOM   1637 C  CG2 . THR A 1 227 ? -13.631 -16.403 -38.781  1.00 33.12  ? 219 THR A CG2 1 
ATOM   1638 N  N   . ILE A 1 228 ? -16.386 -18.386 -40.679  1.00 32.35  ? 220 ILE A N   1 
ATOM   1639 C  CA  . ILE A 1 228 ? -17.736 -18.738 -40.232  1.00 34.75  ? 220 ILE A CA  1 
ATOM   1640 C  C   . ILE A 1 228 ? -17.863 -20.240 -39.979  1.00 35.94  ? 220 ILE A C   1 
ATOM   1641 O  O   . ILE A 1 228 ? -18.441 -20.666 -38.972  1.00 37.89  ? 220 ILE A O   1 
ATOM   1642 C  CB  . ILE A 1 228 ? -18.782 -18.248 -41.245  1.00 30.42  ? 220 ILE A CB  1 
ATOM   1643 C  CG1 . ILE A 1 228 ? -19.035 -16.753 -41.058  1.00 40.01  ? 220 ILE A CG1 1 
ATOM   1644 C  CG2 . ILE A 1 228 ? -20.080 -18.995 -41.075  1.00 30.75  ? 220 ILE A CG2 1 
ATOM   1645 C  CD1 . ILE A 1 228 ? -20.008 -16.188 -42.072  1.00 31.04  ? 220 ILE A CD1 1 
ATOM   1646 N  N   . ALA A 1 229 ? -17.333 -21.064 -40.885  1.00 31.00  ? 221 ALA A N   1 
ATOM   1647 C  CA  . ALA A 1 229 ? -17.473 -22.511 -40.777  1.00 30.57  ? 221 ALA A CA  1 
ATOM   1648 C  C   . ALA A 1 229 ? -16.551 -23.119 -39.730  1.00 31.62  ? 221 ALA A C   1 
ATOM   1649 O  O   . ALA A 1 229 ? -16.729 -24.284 -39.362  1.00 28.33  ? 221 ALA A O   1 
ATOM   1650 C  CB  . ALA A 1 229 ? -17.210 -23.161 -42.135  1.00 21.00  ? 221 ALA A CB  1 
ATOM   1651 N  N   . ALA A 1 230 ? -15.571 -22.370 -39.243  1.00 31.40  ? 222 ALA A N   1 
ATOM   1652 C  CA  . ALA A 1 230 ? -14.693 -22.860 -38.199  1.00 23.80  ? 222 ALA A CA  1 
ATOM   1653 C  C   . ALA A 1 230 ? -15.106 -22.390 -36.811  1.00 27.33  ? 222 ALA A C   1 
ATOM   1654 O  O   . ALA A 1 230 ? -14.480 -22.798 -35.823  1.00 26.20  ? 222 ALA A O   1 
ATOM   1655 C  CB  . ALA A 1 230 ? -13.257 -22.422 -38.480  1.00 22.43  ? 222 ALA A CB  1 
ATOM   1656 N  N   . ASN A 1 231 ? -16.130 -21.543 -36.705  1.00 28.61  ? 223 ASN A N   1 
ATOM   1657 C  CA  . ASN A 1 231 ? -16.466 -20.932 -35.415  1.00 25.42  ? 223 ASN A CA  1 
ATOM   1658 C  C   . ASN A 1 231 ? -17.977 -20.875 -35.217  1.00 33.93  ? 223 ASN A C   1 
ATOM   1659 O  O   . ASN A 1 231 ? -18.488 -20.597 -34.125  1.00 35.27  ? 223 ASN A O   1 
ATOM   1660 C  CB  . ASN A 1 231 ? -15.828 -19.548 -35.309  1.00 22.29  ? 223 ASN A CB  1 
ATOM   1661 C  CG  . ASN A 1 231 ? -14.301 -19.616 -35.220  1.00 28.70  ? 223 ASN A CG  1 
ATOM   1662 O  OD1 . ASN A 1 231 ? -13.751 -19.886 -34.149  1.00 26.27  ? 223 ASN A OD1 1 
ATOM   1663 N  ND2 . ASN A 1 231 ? -13.614 -19.398 -36.349  1.00 26.51  ? 223 ASN A ND2 1 
ATOM   1664 O  OXT . ASN A 1 231 ? -18.729 -21.148 -36.163  1.00 38.02  ? 223 ASN A OXT 1 
ATOM   1665 N  N   . LEU B 2 4   ? -3.665  40.847  -41.286  1.00 85.00  ? 4   LEU B N   1 
ATOM   1666 C  CA  . LEU B 2 4   ? -4.919  40.848  -40.537  1.00 87.68  ? 4   LEU B CA  1 
ATOM   1667 C  C   . LEU B 2 4   ? -5.127  39.512  -39.810  1.00 84.15  ? 4   LEU B C   1 
ATOM   1668 O  O   . LEU B 2 4   ? -5.156  38.456  -40.443  1.00 86.80  ? 4   LEU B O   1 
ATOM   1669 C  CB  . LEU B 2 4   ? -6.091  41.139  -41.477  1.00 75.75  ? 4   LEU B CB  1 
ATOM   1670 C  CG  . LEU B 2 4   ? -6.222  42.599  -41.929  1.00 74.79  ? 4   LEU B CG  1 
ATOM   1671 C  CD1 . LEU B 2 4   ? -7.677  42.947  -42.251  1.00 69.48  ? 4   LEU B CD1 1 
ATOM   1672 C  CD2 . LEU B 2 4   ? -5.644  43.556  -40.895  1.00 62.58  ? 4   LEU B CD2 1 
ATOM   1673 N  N   . PRO B 2 5   ? -5.282  39.561  -38.485  1.00 76.56  ? 5   PRO B N   1 
ATOM   1674 C  CA  . PRO B 2 5   ? -5.276  38.323  -37.689  1.00 78.08  ? 5   PRO B CA  1 
ATOM   1675 C  C   . PRO B 2 5   ? -6.488  37.445  -37.989  1.00 80.71  ? 5   PRO B C   1 
ATOM   1676 O  O   . PRO B 2 5   ? -7.629  37.914  -37.985  1.00 78.74  ? 5   PRO B O   1 
ATOM   1677 C  CB  . PRO B 2 5   ? -5.291  38.834  -36.239  1.00 72.31  ? 5   PRO B CB  1 
ATOM   1678 C  CG  . PRO B 2 5   ? -4.903  40.284  -36.331  1.00 74.28  ? 5   PRO B CG  1 
ATOM   1679 C  CD  . PRO B 2 5   ? -5.492  40.739  -37.632  1.00 74.56  ? 5   PRO B CD  1 
ATOM   1680 N  N   . LYS B 2 6   ? -6.225  36.151  -38.226  1.00 67.13  ? 6   LYS B N   1 
ATOM   1681 C  CA  . LYS B 2 6   ? -7.239  35.177  -38.611  1.00 50.99  ? 6   LYS B CA  1 
ATOM   1682 C  C   . LYS B 2 6   ? -7.609  34.290  -37.426  1.00 57.30  ? 6   LYS B C   1 
ATOM   1683 O  O   . LYS B 2 6   ? -6.822  33.392  -37.070  1.00 49.04  ? 6   LYS B O   1 
ATOM   1684 C  CB  . LYS B 2 6   ? -6.720  34.316  -39.768  1.00 56.05  ? 6   LYS B CB  1 
ATOM   1685 C  CG  . LYS B 2 6   ? -7.073  34.830  -41.153  1.00 63.97  ? 6   LYS B CG  1 
ATOM   1686 C  CD  . LYS B 2 6   ? -6.441  33.999  -42.261  1.00 58.47  ? 6   LYS B CD  1 
ATOM   1687 C  CE  . LYS B 2 6   ? -5.056  33.490  -41.888  1.00 64.90  ? 6   LYS B CE  1 
ATOM   1688 N  NZ  . LYS B 2 6   ? -4.333  32.949  -43.084  1.00 62.35  ? 6   LYS B NZ  1 
ATOM   1689 N  N   . PRO B 2 7   ? -8.787  34.459  -36.816  1.00 55.67  ? 7   PRO B N   1 
ATOM   1690 C  CA  . PRO B 2 7   ? -9.160  33.605  -35.674  1.00 41.71  ? 7   PRO B CA  1 
ATOM   1691 C  C   . PRO B 2 7   ? -9.280  32.146  -36.079  1.00 39.97  ? 7   PRO B C   1 
ATOM   1692 O  O   . PRO B 2 7   ? -9.790  31.824  -37.150  1.00 37.41  ? 7   PRO B O   1 
ATOM   1693 C  CB  . PRO B 2 7   ? -10.520 34.165  -35.236  1.00 39.49  ? 7   PRO B CB  1 
ATOM   1694 C  CG  . PRO B 2 7   ? -11.057 34.854  -36.467  1.00 49.99  ? 7   PRO B CG  1 
ATOM   1695 C  CD  . PRO B 2 7   ? -9.842  35.431  -37.153  1.00 45.46  ? 7   PRO B CD  1 
ATOM   1696 N  N   . VAL B 2 8   ? -8.787  31.257  -35.211  1.00 44.07  ? 8   VAL B N   1 
ATOM   1697 C  CA  . VAL B 2 8   ? -9.047  29.832  -35.377  1.00 31.59  ? 8   VAL B CA  1 
ATOM   1698 C  C   . VAL B 2 8   ? -10.520 29.569  -35.106  1.00 34.89  ? 8   VAL B C   1 
ATOM   1699 O  O   . VAL B 2 8   ? -11.109 30.134  -34.173  1.00 39.71  ? 8   VAL B O   1 
ATOM   1700 C  CB  . VAL B 2 8   ? -8.163  28.990  -34.441  1.00 35.28  ? 8   VAL B CB  1 
ATOM   1701 C  CG1 . VAL B 2 8   ? -8.439  27.498  -34.643  1.00 29.78  ? 8   VAL B CG1 1 
ATOM   1702 C  CG2 . VAL B 2 8   ? -6.701  29.301  -34.662  1.00 31.59  ? 8   VAL B CG2 1 
ATOM   1703 N  N   . LEU B 2 9   ? -11.130 28.723  -35.928  1.00 35.98  ? 9   LEU B N   1 
ATOM   1704 C  CA  . LEU B 2 9   ? -12.563 28.469  -35.862  1.00 38.07  ? 9   LEU B CA  1 
ATOM   1705 C  C   . LEU B 2 9   ? -12.817 27.055  -35.361  1.00 36.89  ? 9   LEU B C   1 
ATOM   1706 O  O   . LEU B 2 9   ? -12.022 26.146  -35.607  1.00 33.50  ? 9   LEU B O   1 
ATOM   1707 C  CB  . LEU B 2 9   ? -13.212 28.658  -37.241  1.00 41.95  ? 9   LEU B CB  1 
ATOM   1708 C  CG  . LEU B 2 9   ? -13.708 30.055  -37.638  1.00 34.71  ? 9   LEU B CG  1 
ATOM   1709 C  CD1 . LEU B 2 9   ? -12.786 31.113  -37.097  1.00 28.43  ? 9   LEU B CD1 1 
ATOM   1710 C  CD2 . LEU B 2 9   ? -13.793 30.167  -39.149  1.00 31.98  ? 9   LEU B CD2 1 
ATOM   1711 N  N   . ASP B 2 10  ? -13.932 26.874  -34.655  1.00 37.64  ? 10  ASP B N   1 
ATOM   1712 C  CA  . ASP B 2 10  ? -14.345 25.544  -34.234  1.00 32.78  ? 10  ASP B CA  1 
ATOM   1713 C  C   . ASP B 2 10  ? -15.112 24.886  -35.383  1.00 38.88  ? 10  ASP B C   1 
ATOM   1714 O  O   . ASP B 2 10  ? -15.230 25.447  -36.478  1.00 38.63  ? 10  ASP B O   1 
ATOM   1715 C  CB  . ASP B 2 10  ? -15.127 25.621  -32.910  1.00 33.37  ? 10  ASP B CB  1 
ATOM   1716 C  CG  . ASP B 2 10  ? -16.590 26.101  -33.061  1.00 36.03  ? 10  ASP B CG  1 
ATOM   1717 O  OD1 . ASP B 2 10  ? -17.069 26.349  -34.183  1.00 45.62  ? 10  ASP B OD1 1 
ATOM   1718 O  OD2 . ASP B 2 10  ? -17.266 26.270  -32.019  1.00 35.63  ? 10  ASP B OD2 1 
ATOM   1719 N  N   . THR B 2 11  ? -15.644 23.685  -35.143  1.00 35.02  ? 11  THR B N   1 
ATOM   1720 C  CA  . THR B 2 11  ? -16.314 22.937  -36.204  1.00 32.62  ? 11  THR B CA  1 
ATOM   1721 C  C   . THR B 2 11  ? -17.669 23.524  -36.592  1.00 37.58  ? 11  THR B C   1 
ATOM   1722 O  O   . THR B 2 11  ? -18.239 23.101  -37.598  1.00 42.79  ? 11  THR B O   1 
ATOM   1723 C  CB  . THR B 2 11  ? -16.504 21.482  -35.786  1.00 32.97  ? 11  THR B CB  1 
ATOM   1724 O  OG1 . THR B 2 11  ? -17.149 21.441  -34.509  1.00 37.05  ? 11  THR B OG1 1 
ATOM   1725 C  CG2 . THR B 2 11  ? -15.146 20.767  -35.708  1.00 24.75  ? 11  THR B CG2 1 
ATOM   1726 N  N   . ASN B 2 12  ? -18.208 24.472  -35.829  1.00 37.40  ? 12  ASN B N   1 
ATOM   1727 C  CA  . ASN B 2 12  ? -19.408 25.191  -36.236  1.00 40.43  ? 12  ASN B CA  1 
ATOM   1728 C  C   . ASN B 2 12  ? -19.099 26.589  -36.734  1.00 39.28  ? 12  ASN B C   1 
ATOM   1729 O  O   . ASN B 2 12  ? -19.962 27.464  -36.678  1.00 53.58  ? 12  ASN B O   1 
ATOM   1730 C  CB  . ASN B 2 12  ? -20.430 25.265  -35.106  1.00 38.84  ? 12  ASN B CB  1 
ATOM   1731 C  CG  . ASN B 2 12  ? -20.719 23.919  -34.499  1.00 33.53  ? 12  ASN B CG  1 
ATOM   1732 O  OD1 . ASN B 2 12  ? -20.984 22.957  -35.218  1.00 56.28  ? 12  ASN B OD1 1 
ATOM   1733 N  ND2 . ASN B 2 12  ? -20.712 23.845  -33.174  1.00 42.96  ? 12  ASN B ND2 1 
ATOM   1734 N  N   . GLY B 2 13  ? -17.886 26.810  -37.234  1.00 42.75  ? 13  GLY B N   1 
ATOM   1735 C  CA  . GLY B 2 13  ? -17.493 28.095  -37.764  1.00 40.14  ? 13  GLY B CA  1 
ATOM   1736 C  C   . GLY B 2 13  ? -17.190 29.160  -36.735  1.00 48.51  ? 13  GLY B C   1 
ATOM   1737 O  O   . GLY B 2 13  ? -16.756 30.253  -37.117  1.00 46.24  ? 13  GLY B O   1 
ATOM   1738 N  N   . LYS B 2 14  ? -17.384 28.885  -35.447  1.00 47.22  ? 14  LYS B N   1 
ATOM   1739 C  CA  . LYS B 2 14  ? -17.154 29.893  -34.419  1.00 45.41  ? 14  LYS B CA  1 
ATOM   1740 C  C   . LYS B 2 14  ? -15.715 29.969  -33.963  1.00 39.82  ? 14  LYS B C   1 
ATOM   1741 O  O   . LYS B 2 14  ? -15.034 28.955  -33.799  1.00 41.22  ? 14  LYS B O   1 
ATOM   1742 C  CB  . LYS B 2 14  ? -18.075 29.684  -33.216  1.00 32.86  ? 14  LYS B CB  1 
ATOM   1743 C  CG  . LYS B 2 14  ? -19.454 30.092  -33.573  1.00 51.07  ? 14  LYS B CG  1 
ATOM   1744 C  CD  . LYS B 2 14  ? -19.247 31.222  -34.595  1.00 59.14  ? 14  LYS B CD  1 
ATOM   1745 C  CE  . LYS B 2 14  ? -20.302 32.259  -34.696  1.00 57.50  ? 14  LYS B CE  1 
ATOM   1746 N  NZ  . LYS B 2 14  ? -20.716 32.259  -36.128  1.00 57.75  ? 14  LYS B NZ  1 
ATOM   1747 N  N   . LYS B 2 15  ? -15.266 31.195  -33.741  1.00 40.20  ? 15  LYS B N   1 
ATOM   1748 C  CA  . LYS B 2 15  ? -13.895 31.390  -33.323  1.00 54.16  ? 15  LYS B CA  1 
ATOM   1749 C  C   . LYS B 2 15  ? -13.652 30.680  -31.997  1.00 44.89  ? 15  LYS B C   1 
ATOM   1750 O  O   . LYS B 2 15  ? -14.571 30.452  -31.203  1.00 37.61  ? 15  LYS B O   1 
ATOM   1751 C  CB  . LYS B 2 15  ? -13.584 32.882  -33.224  1.00 48.56  ? 15  LYS B CB  1 
ATOM   1752 C  CG  . LYS B 2 15  ? -14.706 33.712  -32.644  1.00 46.64  ? 15  LYS B CG  1 
ATOM   1753 C  CD  . LYS B 2 15  ? -14.333 35.196  -32.643  1.00 53.60  ? 15  LYS B CD  1 
ATOM   1754 C  CE  . LYS B 2 15  ? -14.171 35.752  -34.061  1.00 48.78  ? 15  LYS B CE  1 
ATOM   1755 N  NZ  . LYS B 2 15  ? -14.687 37.155  -34.188  1.00 54.72  ? 15  LYS B NZ  1 
ATOM   1756 N  N   . LEU B 2 16  ? -12.407 30.282  -31.792  1.00 32.56  ? 16  LEU B N   1 
ATOM   1757 C  CA  . LEU B 2 16  ? -12.050 29.616  -30.556  1.00 44.80  ? 16  LEU B CA  1 
ATOM   1758 C  C   . LEU B 2 16  ? -12.115 30.616  -29.410  1.00 43.91  ? 16  LEU B C   1 
ATOM   1759 O  O   . LEU B 2 16  ? -11.753 31.784  -29.567  1.00 40.41  ? 16  LEU B O   1 
ATOM   1760 C  CB  . LEU B 2 16  ? -10.652 29.007  -30.680  1.00 40.85  ? 16  LEU B CB  1 
ATOM   1761 C  CG  . LEU B 2 16  ? -10.605 27.682  -31.439  1.00 38.90  ? 16  LEU B CG  1 
ATOM   1762 C  CD1 . LEU B 2 16  ? -9.416  26.823  -31.021  1.00 28.08  ? 16  LEU B CD1 1 
ATOM   1763 C  CD2 . LEU B 2 16  ? -11.920 26.927  -31.258  1.00 42.02  ? 16  LEU B CD2 1 
ATOM   1764 N  N   . ASN B 2 17  ? -12.595 30.156  -28.258  1.00 40.20  ? 17  ASN B N   1 
ATOM   1765 C  CA  . ASN B 2 17  ? -12.747 30.992  -27.087  1.00 40.82  ? 17  ASN B CA  1 
ATOM   1766 C  C   . ASN B 2 17  ? -11.952 30.409  -25.924  1.00 47.68  ? 17  ASN B C   1 
ATOM   1767 O  O   . ASN B 2 17  ? -12.142 29.231  -25.584  1.00 43.69  ? 17  ASN B O   1 
ATOM   1768 C  CB  . ASN B 2 17  ? -14.224 31.104  -26.701  1.00 36.48  ? 17  ASN B CB  1 
ATOM   1769 C  CG  . ASN B 2 17  ? -14.459 32.096  -25.577  1.00 61.50  ? 17  ASN B CG  1 
ATOM   1770 O  OD1 . ASN B 2 17  ? -15.129 31.778  -24.593  1.00 66.66  ? 17  ASN B OD1 1 
ATOM   1771 N  ND2 . ASN B 2 17  ? -13.935 33.314  -25.731  1.00 56.94  ? 17  ASN B ND2 1 
ATOM   1772 N  N   . PRO B 2 18  ? -11.062 31.183  -25.287  1.00 51.73  ? 18  PRO B N   1 
ATOM   1773 C  CA  . PRO B 2 18  ? -10.269 30.633  -24.171  1.00 39.60  ? 18  PRO B CA  1 
ATOM   1774 C  C   . PRO B 2 18  ? -11.097 30.229  -22.975  1.00 40.91  ? 18  PRO B C   1 
ATOM   1775 O  O   . PRO B 2 18  ? -10.556 29.589  -22.067  1.00 46.33  ? 18  PRO B O   1 
ATOM   1776 C  CB  . PRO B 2 18  ? -9.321  31.781  -23.814  1.00 37.29  ? 18  PRO B CB  1 
ATOM   1777 C  CG  . PRO B 2 18  ? -9.191  32.543  -25.100  1.00 47.35  ? 18  PRO B CG  1 
ATOM   1778 C  CD  . PRO B 2 18  ? -10.589 32.521  -25.676  1.00 42.51  ? 18  PRO B CD  1 
ATOM   1779 N  N   . ASN B 2 19  ? -12.383 30.573  -22.935  1.00 46.94  ? 19  ASN B N   1 
ATOM   1780 C  CA  . ASN B 2 19  ? -13.245 30.117  -21.858  1.00 42.77  ? 19  ASN B CA  1 
ATOM   1781 C  C   . ASN B 2 19  ? -13.958 28.809  -22.186  1.00 45.45  ? 19  ASN B C   1 
ATOM   1782 O  O   . ASN B 2 19  ? -14.548 28.200  -21.287  1.00 45.85  ? 19  ASN B O   1 
ATOM   1783 C  CB  . ASN B 2 19  ? -14.270 31.201  -21.517  1.00 46.76  ? 19  ASN B CB  1 
ATOM   1784 C  CG  . ASN B 2 19  ? -13.740 32.210  -20.502  1.00 62.45  ? 19  ASN B CG  1 
ATOM   1785 O  OD1 . ASN B 2 19  ? -12.557 32.550  -20.510  1.00 57.56  ? 19  ASN B OD1 1 
ATOM   1786 N  ND2 . ASN B 2 19  ? -14.623 32.708  -19.634  1.00 67.52  ? 19  ASN B ND2 1 
ATOM   1787 N  N   . SER B 2 20  ? -13.913 28.361  -23.437  1.00 36.92  ? 20  SER B N   1 
ATOM   1788 C  CA  . SER B 2 20  ? -14.576 27.139  -23.863  1.00 40.87  ? 20  SER B CA  1 
ATOM   1789 C  C   . SER B 2 20  ? -13.616 25.957  -23.831  1.00 43.12  ? 20  SER B C   1 
ATOM   1790 O  O   . SER B 2 20  ? -12.391 26.111  -23.851  1.00 43.76  ? 20  SER B O   1 
ATOM   1791 C  CB  . SER B 2 20  ? -15.134 27.284  -25.279  1.00 42.80  ? 20  SER B CB  1 
ATOM   1792 O  OG  . SER B 2 20  ? -15.780 28.524  -25.458  1.00 48.77  ? 20  SER B OG  1 
ATOM   1793 N  N   . SER B 2 21  ? -14.195 24.764  -23.803  1.00 40.39  ? 21  SER B N   1 
ATOM   1794 C  CA  . SER B 2 21  ? -13.451 23.525  -23.952  1.00 36.54  ? 21  SER B CA  1 
ATOM   1795 C  C   . SER B 2 21  ? -13.729 22.923  -25.325  1.00 42.98  ? 21  SER B C   1 
ATOM   1796 O  O   . SER B 2 21  ? -14.838 23.034  -25.865  1.00 34.70  ? 21  SER B O   1 
ATOM   1797 C  CB  . SER B 2 21  ? -13.817 22.517  -22.856  1.00 33.61  ? 21  SER B CB  1 
ATOM   1798 O  OG  . SER B 2 21  ? -12.922 22.575  -21.761  1.00 56.03  ? 21  SER B OG  1 
ATOM   1799 N  N   . TYR B 2 22  ? -12.707 22.281  -25.886  1.00 30.88  ? 22  TYR B N   1 
ATOM   1800 C  CA  . TYR B 2 22  ? -12.841 21.617  -27.168  1.00 29.98  ? 22  TYR B CA  1 
ATOM   1801 C  C   . TYR B 2 22  ? -12.174 20.259  -27.099  1.00 26.12  ? 22  TYR B C   1 
ATOM   1802 O  O   . TYR B 2 22  ? -11.202 20.062  -26.364  1.00 25.13  ? 22  TYR B O   1 
ATOM   1803 C  CB  . TYR B 2 22  ? -12.219 22.447  -28.297  1.00 32.62  ? 22  TYR B CB  1 
ATOM   1804 C  CG  . TYR B 2 22  ? -12.694 23.887  -28.281  1.00 40.26  ? 22  TYR B CG  1 
ATOM   1805 C  CD1 . TYR B 2 22  ? -12.039 24.846  -27.526  1.00 28.57  ? 22  TYR B CD1 1 
ATOM   1806 C  CD2 . TYR B 2 22  ? -13.807 24.276  -28.998  1.00 34.06  ? 22  TYR B CD2 1 
ATOM   1807 C  CE1 . TYR B 2 22  ? -12.470 26.144  -27.502  1.00 40.13  ? 22  TYR B CE1 1 
ATOM   1808 C  CE2 . TYR B 2 22  ? -14.249 25.579  -28.978  1.00 44.33  ? 22  TYR B CE2 1 
ATOM   1809 C  CZ  . TYR B 2 22  ? -13.577 26.513  -28.234  1.00 43.68  ? 22  TYR B CZ  1 
ATOM   1810 O  OH  . TYR B 2 22  ? -14.008 27.821  -28.219  1.00 42.03  ? 22  TYR B OH  1 
ATOM   1811 N  N   . ARG B 2 23  ? -12.740 19.318  -27.840  1.00 19.05  ? 23  ARG B N   1 
ATOM   1812 C  CA  . ARG B 2 23  ? -12.045 18.101  -28.197  1.00 25.69  ? 23  ARG B CA  1 
ATOM   1813 C  C   . ARG B 2 23  ? -11.235 18.376  -29.456  1.00 28.57  ? 23  ARG B C   1 
ATOM   1814 O  O   . ARG B 2 23  ? -11.673 19.126  -30.333  1.00 28.81  ? 23  ARG B O   1 
ATOM   1815 C  CB  . ARG B 2 23  ? -13.030 16.955  -28.444  1.00 22.98  ? 23  ARG B CB  1 
ATOM   1816 C  CG  . ARG B 2 23  ? -13.622 16.364  -27.176  1.00 25.38  ? 23  ARG B CG  1 
ATOM   1817 C  CD  . ARG B 2 23  ? -14.700 15.306  -27.442  1.00 22.43  ? 23  ARG B CD  1 
ATOM   1818 N  NE  . ARG B 2 23  ? -15.117 14.742  -26.166  1.00 31.89  ? 23  ARG B NE  1 
ATOM   1819 C  CZ  . ARG B 2 23  ? -16.064 15.250  -25.386  1.00 34.62  ? 23  ARG B CZ  1 
ATOM   1820 N  NH1 . ARG B 2 23  ? -16.864 16.218  -25.811  1.00 27.92  ? 23  ARG B NH1 1 
ATOM   1821 N  NH2 . ARG B 2 23  ? -16.199 14.785  -24.142  1.00 28.89  ? 23  ARG B NH2 1 
ATOM   1822 N  N   . ILE B 2 24  ? -10.044 17.792  -29.533  1.00 26.44  ? 24  ILE B N   1 
ATOM   1823 C  CA  . ILE B 2 24  ? -9.238  17.854  -30.745  1.00 24.43  ? 24  ILE B CA  1 
ATOM   1824 C  C   . ILE B 2 24  ? -9.563  16.619  -31.565  1.00 25.10  ? 24  ILE B C   1 
ATOM   1825 O  O   . ILE B 2 24  ? -9.392  15.482  -31.101  1.00 23.72  ? 24  ILE B O   1 
ATOM   1826 C  CB  . ILE B 2 24  ? -7.740  17.946  -30.429  1.00 22.23  ? 24  ILE B CB  1 
ATOM   1827 C  CG1 . ILE B 2 24  ? -7.500  19.040  -29.400  1.00 20.02  ? 24  ILE B CG1 1 
ATOM   1828 C  CG2 . ILE B 2 24  ? -6.940  18.251  -31.699  1.00 23.10  ? 24  ILE B CG2 1 
ATOM   1829 C  CD1 . ILE B 2 24  ? -6.083  19.165  -28.974  1.00 23.94  ? 24  ILE B CD1 1 
ATOM   1830 N  N   . ILE B 2 25  ? -10.091 16.839  -32.757  1.00 19.84  ? 25  ILE B N   1 
ATOM   1831 C  CA  . ILE B 2 25  ? -10.557 15.732  -33.572  1.00 25.52  ? 25  ILE B CA  1 
ATOM   1832 C  C   . ILE B 2 25  ? -9.769  15.707  -34.866  1.00 24.59  ? 25  ILE B C   1 
ATOM   1833 O  O   . ILE B 2 25  ? -9.241  16.717  -35.343  1.00 24.87  ? 25  ILE B O   1 
ATOM   1834 C  CB  . ILE B 2 25  ? -12.089 15.758  -33.846  1.00 32.91  ? 25  ILE B CB  1 
ATOM   1835 C  CG1 . ILE B 2 25  ? -12.471 16.839  -34.854  1.00 24.56  ? 25  ILE B CG1 1 
ATOM   1836 C  CG2 . ILE B 2 25  ? -12.937 15.797  -32.552  1.00 18.03  ? 25  ILE B CG2 1 
ATOM   1837 C  CD1 . ILE B 2 25  ? -13.921 16.730  -35.245  1.00 30.49  ? 25  ILE B CD1 1 
ATOM   1838 N  N   . SER B 2 26  ? -9.660  14.507  -35.394  1.00 15.83  ? 26  SER B N   1 
ATOM   1839 C  CA  . SER B 2 26  ? -8.965  14.244  -36.632  1.00 20.32  ? 26  SER B CA  1 
ATOM   1840 C  C   . SER B 2 26  ? -9.828  14.746  -37.787  1.00 23.88  ? 26  SER B C   1 
ATOM   1841 O  O   . SER B 2 26  ? -11.060 14.712  -37.714  1.00 25.91  ? 26  SER B O   1 
ATOM   1842 C  CB  . SER B 2 26  ? -8.710  12.727  -36.699  1.00 14.80  ? 26  SER B CB  1 
ATOM   1843 O  OG  . SER B 2 26  ? -8.278  12.272  -37.945  1.00 31.33  ? 26  SER B OG  1 
ATOM   1844 N  N   . THR B 2 27  ? -9.190  15.282  -38.828  1.00 26.11  ? 27  THR B N   1 
ATOM   1845 C  CA  . THR B 2 27  ? -9.925  15.500  -40.068  1.00 24.70  ? 27  THR B CA  1 
ATOM   1846 C  C   . THR B 2 27  ? -10.321 14.171  -40.685  1.00 31.44  ? 27  THR B C   1 
ATOM   1847 O  O   . THR B 2 27  ? -11.417 14.032  -41.238  1.00 28.90  ? 27  THR B O   1 
ATOM   1848 C  CB  . THR B 2 27  ? -9.097  16.319  -41.054  1.00 29.69  ? 27  THR B CB  1 
ATOM   1849 O  OG1 . THR B 2 27  ? -8.871  17.625  -40.518  1.00 32.94  ? 27  THR B OG1 1 
ATOM   1850 C  CG2 . THR B 2 27  ? -9.820  16.453  -42.390  1.00 30.92  ? 27  THR B CG2 1 
ATOM   1851 N  N   . PHE B 2 28  ? -9.419  13.198  -40.617  1.00 26.40  ? 28  PHE B N   1 
ATOM   1852 C  CA  . PHE B 2 28  ? -9.725  11.815  -40.933  1.00 27.52  ? 28  PHE B CA  1 
ATOM   1853 C  C   . PHE B 2 28  ? -10.805 11.272  -40.002  1.00 26.47  ? 28  PHE B C   1 
ATOM   1854 O  O   . PHE B 2 28  ? -10.864 11.605  -38.811  1.00 23.52  ? 28  PHE B O   1 
ATOM   1855 C  CB  . PHE B 2 28  ? -8.470  10.968  -40.757  1.00 27.06  ? 28  PHE B CB  1 
ATOM   1856 C  CG  . PHE B 2 28  ? -7.499  11.035  -41.898  1.00 30.47  ? 28  PHE B CG  1 
ATOM   1857 C  CD1 . PHE B 2 28  ? -7.855  10.573  -43.160  1.00 25.13  ? 28  PHE B CD1 1 
ATOM   1858 C  CD2 . PHE B 2 28  ? -6.196  11.519  -41.695  1.00 26.08  ? 28  PHE B CD2 1 
ATOM   1859 C  CE1 . PHE B 2 28  ? -6.935  10.601  -44.219  1.00 30.30  ? 28  PHE B CE1 1 
ATOM   1860 C  CE2 . PHE B 2 28  ? -5.267  11.547  -42.747  1.00 27.11  ? 28  PHE B CE2 1 
ATOM   1861 C  CZ  . PHE B 2 28  ? -5.644  11.089  -44.015  1.00 25.98  ? 28  PHE B CZ  1 
ATOM   1862 N  N   . TRP B 2 29  ? -11.641 10.384  -40.529  1.00 26.41  ? 29  TRP B N   1 
ATOM   1863 C  CA  . TRP B 2 29  ? -12.660 9.762   -39.691  1.00 23.64  ? 29  TRP B CA  1 
ATOM   1864 C  C   . TRP B 2 29  ? -12.626 8.248   -39.878  1.00 22.82  ? 29  TRP B C   1 
ATOM   1865 O  O   . TRP B 2 29  ? -11.890 7.724   -40.716  1.00 19.57  ? 29  TRP B O   1 
ATOM   1866 C  CB  . TRP B 2 29  ? -14.046 10.332  -39.990  1.00 15.96  ? 29  TRP B CB  1 
ATOM   1867 C  CG  . TRP B 2 29  ? -14.453 10.151  -41.415  1.00 24.11  ? 29  TRP B CG  1 
ATOM   1868 C  CD1 . TRP B 2 29  ? -14.244 11.029  -42.445  1.00 25.53  ? 29  TRP B CD1 1 
ATOM   1869 C  CD2 . TRP B 2 29  ? -15.148 9.036   -41.976  1.00 21.48  ? 29  TRP B CD2 1 
ATOM   1870 N  NE1 . TRP B 2 29  ? -14.751 10.521  -43.619  1.00 24.78  ? 29  TRP B NE1 1 
ATOM   1871 C  CE2 . TRP B 2 29  ? -15.316 9.301   -43.361  1.00 29.01  ? 29  TRP B CE2 1 
ATOM   1872 C  CE3 . TRP B 2 29  ? -15.620 7.832   -41.457  1.00 22.65  ? 29  TRP B CE3 1 
ATOM   1873 C  CZ2 . TRP B 2 29  ? -15.946 8.406   -44.226  1.00 24.03  ? 29  TRP B CZ2 1 
ATOM   1874 C  CZ3 . TRP B 2 29  ? -16.254 6.947   -42.320  1.00 25.05  ? 29  TRP B CZ3 1 
ATOM   1875 C  CH2 . TRP B 2 29  ? -16.407 7.243   -43.691  1.00 20.24  ? 29  TRP B CH2 1 
ATOM   1876 N  N   . GLY B 2 30  ? -13.414 7.541   -39.068  1.00 18.26  ? 30  GLY B N   1 
ATOM   1877 C  CA  . GLY B 2 30  ? -13.420 6.087   -39.162  1.00 20.84  ? 30  GLY B CA  1 
ATOM   1878 C  C   . GLY B 2 30  ? -12.097 5.507   -38.698  1.00 18.62  ? 30  GLY B C   1 
ATOM   1879 O  O   . GLY B 2 30  ? -11.567 5.890   -37.654  1.00 14.38  ? 30  GLY B O   1 
ATOM   1880 N  N   . ALA B 2 31  ? -11.537 4.597   -39.504  1.00 20.51  ? 31  ALA B N   1 
ATOM   1881 C  CA  . ALA B 2 31  ? -10.372 3.822   -39.076  1.00 24.29  ? 31  ALA B CA  1 
ATOM   1882 C  C   . ALA B 2 31  ? -9.150  4.697   -38.785  1.00 22.35  ? 31  ALA B C   1 
ATOM   1883 O  O   . ALA B 2 31  ? -8.299  4.334   -37.965  1.00 23.11  ? 31  ALA B O   1 
ATOM   1884 C  CB  . ALA B 2 31  ? -10.026 2.769   -40.125  1.00 18.67  ? 31  ALA B CB  1 
ATOM   1885 N  N   . LEU B 2 32  ? -9.032  5.858   -39.398  1.00 20.47  ? 32  LEU B N   1 
ATOM   1886 C  CA  . LEU B 2 32  ? -7.979  6.735   -38.904  1.00 32.76  ? 32  LEU B CA  1 
ATOM   1887 C  C   . LEU B 2 32  ? -8.539  8.027   -38.327  1.00 24.07  ? 32  LEU B C   1 
ATOM   1888 O  O   . LEU B 2 32  ? -7.826  9.030   -38.238  1.00 24.90  ? 32  LEU B O   1 
ATOM   1889 C  CB  . LEU B 2 32  ? -6.907  6.987   -39.961  1.00 36.55  ? 32  LEU B CB  1 
ATOM   1890 C  CG  . LEU B 2 32  ? -7.170  7.860   -41.149  1.00 32.41  ? 32  LEU B CG  1 
ATOM   1891 C  CD1 . LEU B 2 32  ? -5.977  7.773   -42.107  1.00 43.61  ? 32  LEU B CD1 1 
ATOM   1892 C  CD2 . LEU B 2 32  ? -8.446  7.463   -41.831  1.00 41.01  ? 32  LEU B CD2 1 
ATOM   1893 N  N   . GLY B 2 33  ? -9.794  7.995   -37.873  1.00 20.31  ? 33  GLY B N   1 
ATOM   1894 C  CA  . GLY B 2 33  ? -10.242 8.940   -36.880  1.00 18.02  ? 33  GLY B CA  1 
ATOM   1895 C  C   . GLY B 2 33  ? -9.717  8.564   -35.503  1.00 21.06  ? 33  GLY B C   1 
ATOM   1896 O  O   . GLY B 2 33  ? -9.116  7.510   -35.291  1.00 20.88  ? 33  GLY B O   1 
ATOM   1897 N  N   . GLY B 2 34  ? -9.956  9.449   -34.543  1.00 21.16  ? 34  GLY B N   1 
ATOM   1898 C  CA  . GLY B 2 34  ? -9.526  9.204   -33.181  1.00 20.09  ? 34  GLY B CA  1 
ATOM   1899 C  C   . GLY B 2 34  ? -9.107  10.497  -32.525  1.00 22.64  ? 34  GLY B C   1 
ATOM   1900 O  O   . GLY B 2 34  ? -8.098  11.094  -32.915  1.00 15.72  ? 34  GLY B O   1 
ATOM   1901 N  N   . ASP B 2 35  ? -9.894  10.946  -31.543  1.00 22.55  ? 35  ASP B N   1 
ATOM   1902 C  CA  . ASP B 2 35  ? -9.627  12.211  -30.882  1.00 18.10  ? 35  ASP B CA  1 
ATOM   1903 C  C   . ASP B 2 35  ? -8.414  12.110  -29.969  1.00 21.80  ? 35  ASP B C   1 
ATOM   1904 O  O   . ASP B 2 35  ? -8.059  11.034  -29.478  1.00 19.01  ? 35  ASP B O   1 
ATOM   1905 C  CB  . ASP B 2 35  ? -10.813 12.660  -30.041  1.00 24.00  ? 35  ASP B CB  1 
ATOM   1906 C  CG  . ASP B 2 35  ? -12.116 12.759  -30.818  1.00 29.44  ? 35  ASP B CG  1 
ATOM   1907 O  OD1 . ASP B 2 35  ? -12.098 12.771  -32.071  1.00 32.14  ? 35  ASP B OD1 1 
ATOM   1908 O  OD2 . ASP B 2 35  ? -13.172 12.844  -30.140  1.00 22.26  ? 35  ASP B OD2 1 
ATOM   1909 N  N   . VAL B 2 36  ? -7.800  13.265  -29.709  1.00 17.46  ? 36  VAL B N   1 
ATOM   1910 C  CA  . VAL B 2 36  ? -6.697  13.316  -28.764  1.00 18.34  ? 36  VAL B CA  1 
ATOM   1911 C  C   . VAL B 2 36  ? -7.222  13.082  -27.350  1.00 20.13  ? 36  VAL B C   1 
ATOM   1912 O  O   . VAL B 2 36  ? -8.319  13.541  -26.992  1.00 21.79  ? 36  VAL B O   1 
ATOM   1913 C  CB  . VAL B 2 36  ? -5.977  14.667  -28.898  1.00 21.09  ? 36  VAL B CB  1 
ATOM   1914 C  CG1 . VAL B 2 36  ? -5.014  14.881  -27.771  1.00 15.93  ? 36  VAL B CG1 1 
ATOM   1915 C  CG2 . VAL B 2 36  ? -5.264  14.746  -30.252  1.00 21.92  ? 36  VAL B CG2 1 
ATOM   1916 N  N   . TYR B 2 37  ? -6.444  12.362  -26.536  1.00 20.37  ? 37  TYR B N   1 
ATOM   1917 C  CA  . TYR B 2 37  ? -6.794  12.142  -25.135  1.00 21.03  ? 37  TYR B CA  1 
ATOM   1918 C  C   . TYR B 2 37  ? -5.540  12.069  -24.259  1.00 21.16  ? 37  TYR B C   1 
ATOM   1919 O  O   . TYR B 2 37  ? -4.412  11.944  -24.747  1.00 15.50  ? 37  TYR B O   1 
ATOM   1920 C  CB  . TYR B 2 37  ? -7.644  10.877  -24.985  1.00 17.73  ? 37  TYR B CB  1 
ATOM   1921 C  CG  . TYR B 2 37  ? -6.876  9.609   -25.202  1.00 20.90  ? 37  TYR B CG  1 
ATOM   1922 C  CD1 . TYR B 2 37  ? -6.566  9.163   -26.486  1.00 18.60  ? 37  TYR B CD1 1 
ATOM   1923 C  CD2 . TYR B 2 37  ? -6.455  8.842   -24.121  1.00 18.19  ? 37  TYR B CD2 1 
ATOM   1924 C  CE1 . TYR B 2 37  ? -5.854  7.969   -26.682  1.00 16.60  ? 37  TYR B CE1 1 
ATOM   1925 C  CE2 . TYR B 2 37  ? -5.758  7.665   -24.307  1.00 19.17  ? 37  TYR B CE2 1 
ATOM   1926 C  CZ  . TYR B 2 37  ? -5.451  7.233   -25.577  1.00 15.47  ? 37  TYR B CZ  1 
ATOM   1927 O  OH  . TYR B 2 37  ? -4.748  6.052   -25.699  1.00 21.20  ? 37  TYR B OH  1 
ATOM   1928 N  N   . LEU B 2 38  ? -5.765  12.143  -22.942  1.00 20.95  ? 38  LEU B N   1 
ATOM   1929 C  CA  . LEU B 2 38  ? -4.710  12.098  -21.930  1.00 19.49  ? 38  LEU B CA  1 
ATOM   1930 C  C   . LEU B 2 38  ? -4.546  10.654  -21.472  1.00 20.90  ? 38  LEU B C   1 
ATOM   1931 O  O   . LEU B 2 38  ? -5.520  10.024  -21.057  1.00 20.40  ? 38  LEU B O   1 
ATOM   1932 C  CB  . LEU B 2 38  ? -5.073  13.004  -20.749  1.00 19.38  ? 38  LEU B CB  1 
ATOM   1933 C  CG  . LEU B 2 38  ? -4.263  13.029  -19.435  1.00 26.93  ? 38  LEU B CG  1 
ATOM   1934 C  CD1 . LEU B 2 38  ? -2.817  13.498  -19.617  1.00 19.20  ? 38  LEU B CD1 1 
ATOM   1935 C  CD2 . LEU B 2 38  ? -4.956  13.876  -18.366  1.00 18.89  ? 38  LEU B CD2 1 
ATOM   1936 N  N   . GLY B 2 39  ? -3.330  10.111  -21.582  1.00 21.95  ? 39  GLY B N   1 
ATOM   1937 C  CA  . GLY B 2 39  ? -3.116  8.709   -21.292  1.00 16.60  ? 39  GLY B CA  1 
ATOM   1938 C  C   . GLY B 2 39  ? -1.843  8.496   -20.498  1.00 27.27  ? 39  GLY B C   1 
ATOM   1939 O  O   . GLY B 2 39  ? -1.010  9.395   -20.361  1.00 28.49  ? 39  GLY B O   1 
ATOM   1940 N  N   . LYS B 2 40  ? -1.718  7.284   -19.967  1.00 30.80  ? 40  LYS B N   1 
ATOM   1941 C  CA  . LYS B 2 40  ? -0.519  6.855   -19.258  1.00 30.96  ? 40  LYS B CA  1 
ATOM   1942 C  C   . LYS B 2 40  ? 0.595   6.555   -20.255  1.00 32.40  ? 40  LYS B C   1 
ATOM   1943 O  O   . LYS B 2 40  ? 0.401   5.782   -21.201  1.00 39.87  ? 40  LYS B O   1 
ATOM   1944 C  CB  . LYS B 2 40  ? -0.824  5.605   -18.418  1.00 37.98  ? 40  LYS B CB  1 
ATOM   1945 C  CG  . LYS B 2 40  ? -0.284  5.635   -16.969  1.00 53.94  ? 40  LYS B CG  1 
ATOM   1946 C  CD  . LYS B 2 40  ? 1.135   5.033   -16.846  1.00 51.41  ? 40  LYS B CD  1 
ATOM   1947 C  CE  . LYS B 2 40  ? 1.774   5.313   -15.469  1.00 61.90  ? 40  LYS B CE  1 
ATOM   1948 N  NZ  . LYS B 2 40  ? 3.070   4.590   -15.221  1.00 66.21  ? 40  LYS B NZ  1 
ATOM   1949 N  N   A SER B 2 41  ? 1.753   7.170   -20.056  0.64 34.45  ? 41  SER B N   1 
ATOM   1950 N  N   B SER B 2 41  ? 1.759   7.170   -20.048  0.36 34.45  ? 41  SER B N   1 
ATOM   1951 C  CA  A SER B 2 41  ? 2.912   6.820   -20.868  0.64 34.46  ? 41  SER B CA  1 
ATOM   1952 C  CA  B SER B 2 41  ? 2.925   6.822   -20.851  0.36 34.43  ? 41  SER B CA  1 
ATOM   1953 C  C   A SER B 2 41  ? 3.436   5.450   -20.439  0.64 38.28  ? 41  SER B C   1 
ATOM   1954 C  C   B SER B 2 41  ? 3.426   5.440   -20.436  0.36 38.47  ? 41  SER B C   1 
ATOM   1955 O  O   A SER B 2 41  ? 3.366   5.105   -19.258  0.64 42.35  ? 41  SER B O   1 
ATOM   1956 O  O   B SER B 2 41  ? 3.338   5.079   -19.258  0.36 42.48  ? 41  SER B O   1 
ATOM   1957 C  CB  A SER B 2 41  ? 4.006   7.884   -20.725  0.64 33.67  ? 41  SER B CB  1 
ATOM   1958 C  CB  B SER B 2 41  ? 4.045   7.857   -20.675  0.36 33.72  ? 41  SER B CB  1 
ATOM   1959 O  OG  A SER B 2 41  ? 4.949   7.820   -21.778  0.64 36.91  ? 41  SER B OG  1 
ATOM   1960 O  OG  B SER B 2 41  ? 3.632   9.168   -21.018  0.36 28.46  ? 41  SER B OG  1 
ATOM   1961 N  N   . PRO B 2 42  ? 3.941   4.637   -21.369  1.00 40.18  ? 42  PRO B N   1 
ATOM   1962 C  CA  . PRO B 2 42  ? 4.456   3.310   -20.987  1.00 49.06  ? 42  PRO B CA  1 
ATOM   1963 C  C   . PRO B 2 42  ? 5.706   3.446   -20.130  1.00 51.20  ? 42  PRO B C   1 
ATOM   1964 O  O   . PRO B 2 42  ? 6.623   4.205   -20.464  1.00 48.18  ? 42  PRO B O   1 
ATOM   1965 C  CB  . PRO B 2 42  ? 4.775   2.641   -22.333  1.00 43.89  ? 42  PRO B CB  1 
ATOM   1966 C  CG  . PRO B 2 42  ? 4.170   3.504   -23.344  1.00 38.03  ? 42  PRO B CG  1 
ATOM   1967 C  CD  . PRO B 2 42  ? 4.171   4.891   -22.795  1.00 37.80  ? 42  PRO B CD  1 
ATOM   1968 N  N   . ASN B 2 43  ? 5.727   2.711   -19.014  1.00 58.38  ? 43  ASN B N   1 
ATOM   1969 C  CA  . ASN B 2 43  ? 6.829   2.748   -18.048  1.00 57.03  ? 43  ASN B CA  1 
ATOM   1970 C  C   . ASN B 2 43  ? 7.117   4.181   -17.602  1.00 59.79  ? 43  ASN B C   1 
ATOM   1971 O  O   . ASN B 2 43  ? 8.254   4.659   -17.633  1.00 69.65  ? 43  ASN B O   1 
ATOM   1972 C  CB  . ASN B 2 43  ? 8.086   2.097   -18.625  1.00 50.34  ? 43  ASN B CB  1 
ATOM   1973 C  CG  . ASN B 2 43  ? 7.800   0.753   -19.256  1.00 65.56  ? 43  ASN B CG  1 
ATOM   1974 O  OD1 . ASN B 2 43  ? 6.925   0.016   -18.798  1.00 70.54  ? 43  ASN B OD1 1 
ATOM   1975 N  ND2 . ASN B 2 43  ? 8.533   0.426   -20.317  1.00 63.83  ? 43  ASN B ND2 1 
ATOM   1976 N  N   . SER B 2 44  ? 6.061   4.881   -17.204  1.00 60.94  ? 44  SER B N   1 
ATOM   1977 C  CA  . SER B 2 44  ? 6.182   6.239   -16.698  1.00 61.13  ? 44  SER B CA  1 
ATOM   1978 C  C   . SER B 2 44  ? 6.084   6.199   -15.181  1.00 63.97  ? 44  SER B C   1 
ATOM   1979 O  O   . SER B 2 44  ? 5.237   5.492   -14.621  1.00 61.53  ? 44  SER B O   1 
ATOM   1980 C  CB  . SER B 2 44  ? 5.098   7.154   -17.287  1.00 55.39  ? 44  SER B CB  1 
ATOM   1981 O  OG  . SER B 2 44  ? 4.849   8.293   -16.472  1.00 50.87  ? 44  SER B OG  1 
ATOM   1982 N  N   . ASP B 2 45  ? 6.965   6.946   -14.516  1.00 58.85  ? 45  ASP B N   1 
ATOM   1983 C  CA  . ASP B 2 45  ? 6.970   6.926   -13.061  1.00 79.43  ? 45  ASP B CA  1 
ATOM   1984 C  C   . ASP B 2 45  ? 5.850   7.757   -12.455  1.00 75.02  ? 45  ASP B C   1 
ATOM   1985 O  O   . ASP B 2 45  ? 5.476   7.512   -11.302  1.00 84.16  ? 45  ASP B O   1 
ATOM   1986 C  CB  . ASP B 2 45  ? 8.323   7.404   -12.529  1.00 81.17  ? 45  ASP B CB  1 
ATOM   1987 C  CG  . ASP B 2 45  ? 9.336   6.276   -12.428  1.00 96.37  ? 45  ASP B CG  1 
ATOM   1988 O  OD1 . ASP B 2 45  ? 9.217   5.294   -13.196  1.00 97.54  ? 45  ASP B OD1 1 
ATOM   1989 O  OD2 . ASP B 2 45  ? 10.251  6.370   -11.584  1.00 105.85 ? 45  ASP B OD2 1 
ATOM   1990 N  N   . ALA B 2 46  ? 5.295   8.704   -13.206  1.00 65.35  ? 46  ALA B N   1 
ATOM   1991 C  CA  . ALA B 2 46  ? 4.314   9.620   -12.651  1.00 58.35  ? 46  ALA B CA  1 
ATOM   1992 C  C   . ALA B 2 46  ? 3.130   8.857   -12.053  1.00 49.58  ? 46  ALA B C   1 
ATOM   1993 O  O   . ALA B 2 46  ? 2.776   7.766   -12.514  1.00 47.39  ? 46  ALA B O   1 
ATOM   1994 C  CB  . ALA B 2 46  ? 3.824   10.598  -13.720  1.00 53.83  ? 46  ALA B CB  1 
ATOM   1995 N  N   . PRO B 2 47  ? 2.520   9.401   -10.997  1.00 58.23  ? 47  PRO B N   1 
ATOM   1996 C  CA  . PRO B 2 47  ? 1.280   8.805   -10.486  1.00 53.03  ? 47  PRO B CA  1 
ATOM   1997 C  C   . PRO B 2 47  ? 0.079   9.138   -11.344  1.00 47.43  ? 47  PRO B C   1 
ATOM   1998 O  O   . PRO B 2 47  ? -0.906  8.388   -11.318  1.00 49.87  ? 47  PRO B O   1 
ATOM   1999 C  CB  . PRO B 2 47  ? 1.149   9.424   -9.092   1.00 47.31  ? 47  PRO B CB  1 
ATOM   2000 C  CG  . PRO B 2 47  ? 1.777   10.788  -9.266   1.00 51.70  ? 47  PRO B CG  1 
ATOM   2001 C  CD  . PRO B 2 47  ? 2.927   10.593  -10.223  1.00 50.15  ? 47  PRO B CD  1 
ATOM   2002 N  N   . CYS B 2 48  ? 0.145   10.238  -12.116  1.00 43.59  ? 48  CYS B N   1 
ATOM   2003 C  CA  . CYS B 2 48  ? -0.831  10.812  -13.020  1.00 34.42  ? 48  CYS B CA  1 
ATOM   2004 C  C   . CYS B 2 48  ? -0.534  10.420  -14.463  1.00 27.29  ? 48  CYS B C   1 
ATOM   2005 O  O   . CYS B 2 48  ? 0.630   10.296  -14.855  1.00 25.36  ? 48  CYS B O   1 
ATOM   2006 C  CB  . CYS B 2 48  ? -0.823  12.342  -12.912  1.00 31.34  ? 48  CYS B CB  1 
ATOM   2007 S  SG  . CYS B 2 48  ? -0.977  12.978  -11.230  1.00 46.33  ? 48  CYS B SG  1 
ATOM   2008 N  N   . PRO B 2 49  ? -1.582  10.263  -15.272  1.00 24.76  ? 49  PRO B N   1 
ATOM   2009 C  CA  . PRO B 2 49  ? -1.395  10.116  -16.720  1.00 21.78  ? 49  PRO B CA  1 
ATOM   2010 C  C   . PRO B 2 49  ? -0.567  11.265  -17.280  1.00 24.22  ? 49  PRO B C   1 
ATOM   2011 O  O   . PRO B 2 49  ? -0.813  12.434  -16.973  1.00 23.02  ? 49  PRO B O   1 
ATOM   2012 C  CB  . PRO B 2 49  ? -2.829  10.160  -17.255  1.00 21.38  ? 49  PRO B CB  1 
ATOM   2013 C  CG  . PRO B 2 49  ? -3.653  9.635   -16.101  1.00 33.27  ? 49  PRO B CG  1 
ATOM   2014 C  CD  . PRO B 2 49  ? -3.008  10.253  -14.896  1.00 27.72  ? 49  PRO B CD  1 
ATOM   2015 N  N   . ASP B 2 50  ? 0.407   10.940  -18.132  1.00 18.96  ? 50  ASP B N   1 
ATOM   2016 C  CA  . ASP B 2 50  ? 1.363   11.955  -18.583  1.00 32.60  ? 50  ASP B CA  1 
ATOM   2017 C  C   . ASP B 2 50  ? 1.648   11.957  -20.088  1.00 19.14  ? 50  ASP B C   1 
ATOM   2018 O  O   . ASP B 2 50  ? 2.604   12.604  -20.517  1.00 22.45  ? 50  ASP B O   1 
ATOM   2019 C  CB  . ASP B 2 50  ? 2.693   11.799  -17.818  1.00 22.98  ? 50  ASP B CB  1 
ATOM   2020 C  CG  . ASP B 2 50  ? 3.370   10.464  -18.081  1.00 35.91  ? 50  ASP B CG  1 
ATOM   2021 O  OD1 . ASP B 2 50  ? 2.672   9.451   -18.365  1.00 36.52  ? 50  ASP B OD1 1 
ATOM   2022 O  OD2 . ASP B 2 50  ? 4.611   10.423  -17.977  1.00 47.62  ? 50  ASP B OD2 1 
ATOM   2023 N  N   . GLY B 2 51  ? 0.873   11.245  -20.900  1.00 22.12  ? 51  GLY B N   1 
ATOM   2024 C  CA  . GLY B 2 51  ? 1.085   11.217  -22.335  1.00 17.45  ? 51  GLY B CA  1 
ATOM   2025 C  C   . GLY B 2 51  ? -0.090  11.817  -23.085  1.00 22.90  ? 51  GLY B C   1 
ATOM   2026 O  O   . GLY B 2 51  ? -1.235  11.776  -22.618  1.00 30.34  ? 51  GLY B O   1 
ATOM   2027 N  N   . VAL B 2 52  ? 0.203   12.374  -24.256  1.00 16.34  ? 52  VAL B N   1 
ATOM   2028 C  CA  . VAL B 2 52  ? -0.805  12.884  -25.179  1.00 13.99  ? 52  VAL B CA  1 
ATOM   2029 C  C   . VAL B 2 52  ? -0.965  11.869  -26.314  1.00 18.80  ? 52  VAL B C   1 
ATOM   2030 O  O   . VAL B 2 52  ? -0.064  11.678  -27.144  1.00 19.16  ? 52  VAL B O   1 
ATOM   2031 C  CB  . VAL B 2 52  ? -0.423  14.271  -25.717  1.00 17.89  ? 52  VAL B CB  1 
ATOM   2032 C  CG1 . VAL B 2 52  ? -1.366  14.690  -26.829  1.00 11.62  ? 52  VAL B CG1 1 
ATOM   2033 C  CG2 . VAL B 2 52  ? -0.357  15.323  -24.565  1.00 13.89  ? 52  VAL B CG2 1 
ATOM   2034 N  N   . PHE B 2 53  ? -2.110  11.210  -26.361  1.00 17.87  ? 53  PHE B N   1 
ATOM   2035 C  CA  . PHE B 2 53  ? -2.361  10.182  -27.354  1.00 17.11  ? 53  PHE B CA  1 
ATOM   2036 C  C   . PHE B 2 53  ? -3.520  10.610  -28.245  1.00 22.50  ? 53  PHE B C   1 
ATOM   2037 O  O   . PHE B 2 53  ? -4.065  11.709  -28.133  1.00 20.49  ? 53  PHE B O   1 
ATOM   2038 C  CB  . PHE B 2 53  ? -2.676  8.839   -26.690  1.00 16.47  ? 53  PHE B CB  1 
ATOM   2039 C  CG  . PHE B 2 53  ? -1.565  8.305   -25.820  1.00 24.18  ? 53  PHE B CG  1 
ATOM   2040 C  CD1 . PHE B 2 53  ? -1.421  8.734   -24.505  1.00 21.39  ? 53  PHE B CD1 1 
ATOM   2041 C  CD2 . PHE B 2 53  ? -0.665  7.369   -26.317  1.00 30.55  ? 53  PHE B CD2 1 
ATOM   2042 C  CE1 . PHE B 2 53  ? -0.388  8.243   -23.704  1.00 26.18  ? 53  PHE B CE1 1 
ATOM   2043 C  CE2 . PHE B 2 53  ? 0.362   6.871   -25.524  1.00 25.28  ? 53  PHE B CE2 1 
ATOM   2044 C  CZ  . PHE B 2 53  ? 0.504   7.316   -24.219  1.00 27.72  ? 53  PHE B CZ  1 
ATOM   2045 N  N   . ARG B 2 54  ? -3.888  9.713   -29.145  1.00 22.93  ? 54  ARG B N   1 
ATOM   2046 C  CA  . ARG B 2 54  ? -5.163  9.787   -29.825  1.00 16.24  ? 54  ARG B CA  1 
ATOM   2047 C  C   . ARG B 2 54  ? -5.635  8.348   -30.040  1.00 21.08  ? 54  ARG B C   1 
ATOM   2048 O  O   . ARG B 2 54  ? -4.816  7.433   -30.198  1.00 17.82  ? 54  ARG B O   1 
ATOM   2049 C  CB  . ARG B 2 54  ? -5.048  10.611  -31.122  1.00 17.01  ? 54  ARG B CB  1 
ATOM   2050 C  CG  . ARG B 2 54  ? -4.859  9.844   -32.423  1.00 17.87  ? 54  ARG B CG  1 
ATOM   2051 C  CD  . ARG B 2 54  ? -4.721  10.841  -33.555  1.00 18.43  ? 54  ARG B CD  1 
ATOM   2052 N  NE  . ARG B 2 54  ? -4.611  10.211  -34.868  1.00 27.62  ? 54  ARG B NE  1 
ATOM   2053 C  CZ  . ARG B 2 54  ? -5.613  10.077  -35.725  1.00 23.57  ? 54  ARG B CZ  1 
ATOM   2054 N  NH1 . ARG B 2 54  ? -6.835  10.482  -35.423  1.00 23.89  ? 54  ARG B NH1 1 
ATOM   2055 N  NH2 . ARG B 2 54  ? -5.385  9.510   -36.908  1.00 23.96  ? 54  ARG B NH2 1 
ATOM   2056 N  N   . TYR B 2 55  ? -6.955  8.158   -30.001  1.00 13.32  ? 55  TYR B N   1 
ATOM   2057 C  CA  . TYR B 2 55  ? -7.566  6.849   -30.155  1.00 15.79  ? 55  TYR B CA  1 
ATOM   2058 C  C   . TYR B 2 55  ? -7.297  6.280   -31.543  1.00 18.41  ? 55  TYR B C   1 
ATOM   2059 O  O   . TYR B 2 55  ? -7.029  7.009   -32.505  1.00 22.05  ? 55  TYR B O   1 
ATOM   2060 C  CB  . TYR B 2 55  ? -9.067  6.956   -29.885  1.00 17.25  ? 55  TYR B CB  1 
ATOM   2061 C  CG  . TYR B 2 55  ? -9.320  7.288   -28.435  1.00 26.16  ? 55  TYR B CG  1 
ATOM   2062 C  CD1 . TYR B 2 55  ? -8.963  6.388   -27.426  1.00 15.35  ? 55  TYR B CD1 1 
ATOM   2063 C  CD2 . TYR B 2 55  ? -9.825  8.535   -28.062  1.00 18.58  ? 55  TYR B CD2 1 
ATOM   2064 C  CE1 . TYR B 2 55  ? -9.156  6.705   -26.104  1.00 21.07  ? 55  TYR B CE1 1 
ATOM   2065 C  CE2 . TYR B 2 55  ? -10.028 8.854   -26.728  1.00 14.84  ? 55  TYR B CE2 1 
ATOM   2066 C  CZ  . TYR B 2 55  ? -9.690  7.944   -25.766  1.00 19.35  ? 55  TYR B CZ  1 
ATOM   2067 O  OH  . TYR B 2 55  ? -9.866  8.251   -24.448  1.00 20.62  ? 55  TYR B OH  1 
ATOM   2068 N  N   . ASN B 2 56  ? -7.383  4.948   -31.637  1.00 23.55  ? 56  ASN B N   1 
ATOM   2069 C  CA  . ASN B 2 56  ? -7.166  4.230   -32.890  1.00 22.35  ? 56  ASN B CA  1 
ATOM   2070 C  C   . ASN B 2 56  ? -8.343  4.331   -33.843  1.00 20.63  ? 56  ASN B C   1 
ATOM   2071 O  O   . ASN B 2 56  ? -8.243  3.853   -34.976  1.00 24.47  ? 56  ASN B O   1 
ATOM   2072 C  CB  . ASN B 2 56  ? -6.903  2.753   -32.618  1.00 18.97  ? 56  ASN B CB  1 
ATOM   2073 C  CG  . ASN B 2 56  ? -5.665  2.515   -31.759  1.00 28.71  ? 56  ASN B CG  1 
ATOM   2074 O  OD1 . ASN B 2 56  ? -4.585  3.058   -32.009  1.00 24.57  ? 56  ASN B OD1 1 
ATOM   2075 N  ND2 . ASN B 2 56  ? -5.822  1.677   -30.740  1.00 35.90  ? 56  ASN B ND2 1 
ATOM   2076 N  N   . SER B 2 57  ? -9.460  4.900   -33.404  1.00 21.37  ? 57  SER B N   1 
ATOM   2077 C  CA  . SER B 2 57  ? -10.620 5.135   -34.250  1.00 21.02  ? 57  SER B CA  1 
ATOM   2078 C  C   . SER B 2 57  ? -11.461 6.177   -33.528  1.00 21.49  ? 57  SER B C   1 
ATOM   2079 O  O   . SER B 2 57  ? -11.217 6.486   -32.361  1.00 18.84  ? 57  SER B O   1 
ATOM   2080 C  CB  . SER B 2 57  ? -11.423 3.853   -34.522  1.00 14.94  ? 57  SER B CB  1 
ATOM   2081 O  OG  . SER B 2 57  ? -12.210 3.490   -33.387  1.00 20.70  ? 57  SER B OG  1 
ATOM   2082 N  N   . ASP B 2 58  ? -12.450 6.730   -34.234  1.00 16.15  ? 58  ASP B N   1 
ATOM   2083 C  CA  . ASP B 2 58  ? -13.344 7.704   -33.623  1.00 24.17  ? 58  ASP B CA  1 
ATOM   2084 C  C   . ASP B 2 58  ? -14.691 7.107   -33.209  1.00 24.29  ? 58  ASP B C   1 
ATOM   2085 O  O   . ASP B 2 58  ? -15.627 7.866   -32.949  1.00 21.79  ? 58  ASP B O   1 
ATOM   2086 C  CB  . ASP B 2 58  ? -13.557 8.897   -34.555  1.00 21.32  ? 58  ASP B CB  1 
ATOM   2087 C  CG  . ASP B 2 58  ? -14.069 8.492   -35.942  1.00 27.85  ? 58  ASP B CG  1 
ATOM   2088 O  OD1 . ASP B 2 58  ? -14.741 7.444   -36.063  1.00 23.41  ? 58  ASP B OD1 1 
ATOM   2089 O  OD2 . ASP B 2 58  ? -13.806 9.238   -36.915  1.00 26.92  ? 58  ASP B OD2 1 
ATOM   2090 N  N   . VAL B 2 59  ? -14.800 5.773   -33.115  1.00 22.18  ? 59  VAL B N   1 
ATOM   2091 C  CA  . VAL B 2 59  ? -16.072 5.113   -32.784  1.00 24.31  ? 59  VAL B CA  1 
ATOM   2092 C  C   . VAL B 2 59  ? -16.179 4.703   -31.310  1.00 24.20  ? 59  VAL B C   1 
ATOM   2093 O  O   . VAL B 2 59  ? -17.217 4.168   -30.898  1.00 30.36  ? 59  VAL B O   1 
ATOM   2094 C  CB  . VAL B 2 59  ? -16.312 3.885   -33.690  1.00 27.50  ? 59  VAL B CB  1 
ATOM   2095 C  CG1 . VAL B 2 59  ? -16.241 4.286   -35.173  1.00 12.81  ? 59  VAL B CG1 1 
ATOM   2096 C  CG2 . VAL B 2 59  ? -15.310 2.752   -33.343  1.00 18.31  ? 59  VAL B CG2 1 
ATOM   2097 N  N   . GLY B 2 60  ? -15.157 4.945   -30.505  1.00 17.49  ? 60  GLY B N   1 
ATOM   2098 C  CA  . GLY B 2 60  ? -15.198 4.558   -29.117  1.00 20.10  ? 60  GLY B CA  1 
ATOM   2099 C  C   . GLY B 2 60  ? -15.237 5.779   -28.238  1.00 23.55  ? 60  GLY B C   1 
ATOM   2100 O  O   . GLY B 2 60  ? -16.099 6.642   -28.400  1.00 28.57  ? 60  GLY B O   1 
ATOM   2101 N  N   . PRO B 2 61  ? -14.296 5.893   -27.301  1.00 23.84  ? 61  PRO B N   1 
ATOM   2102 C  CA  . PRO B 2 61  ? -14.278 7.067   -26.415  1.00 22.34  ? 61  PRO B CA  1 
ATOM   2103 C  C   . PRO B 2 61  ? -14.067 8.372   -27.171  1.00 29.70  ? 61  PRO B C   1 
ATOM   2104 O  O   . PRO B 2 61  ? -13.466 8.413   -28.249  1.00 30.89  ? 61  PRO B O   1 
ATOM   2105 C  CB  . PRO B 2 61  ? -13.103 6.778   -25.474  1.00 17.38  ? 61  PRO B CB  1 
ATOM   2106 C  CG  . PRO B 2 61  ? -12.986 5.309   -25.497  1.00 20.66  ? 61  PRO B CG  1 
ATOM   2107 C  CD  . PRO B 2 61  ? -13.266 4.919   -26.917  1.00 23.41  ? 61  PRO B CD  1 
ATOM   2108 N  N   . SER B 2 62  ? -14.568 9.448   -26.585  1.00 24.89  ? 62  SER B N   1 
ATOM   2109 C  CA  . SER B 2 62  ? -14.355 10.776  -27.131  1.00 26.02  ? 62  SER B CA  1 
ATOM   2110 C  C   . SER B 2 62  ? -13.131 11.434  -26.495  1.00 27.07  ? 62  SER B C   1 
ATOM   2111 O  O   . SER B 2 62  ? -12.719 11.099  -25.379  1.00 25.31  ? 62  SER B O   1 
ATOM   2112 C  CB  . SER B 2 62  ? -15.596 11.628  -26.913  1.00 20.84  ? 62  SER B CB  1 
ATOM   2113 O  OG  . SER B 2 62  ? -16.508 11.357  -27.952  1.00 42.88  ? 62  SER B OG  1 
ATOM   2114 N  N   . GLY B 2 63  ? -12.545 12.377  -27.231  1.00 21.12  ? 63  GLY B N   1 
ATOM   2115 C  CA  . GLY B 2 63  ? -11.370 13.094  -26.772  1.00 17.82  ? 63  GLY B CA  1 
ATOM   2116 C  C   . GLY B 2 63  ? -11.425 13.610  -25.354  1.00 22.36  ? 63  GLY B C   1 
ATOM   2117 O  O   . GLY B 2 63  ? -12.498 13.942  -24.846  1.00 27.81  ? 63  GLY B O   1 
ATOM   2118 N  N   . THR B 2 64  ? -10.289 13.659  -24.688  1.00 16.95  ? 64  THR B N   1 
ATOM   2119 C  CA  . THR B 2 64  ? -10.206 14.485  -23.494  1.00 19.50  ? 64  THR B CA  1 
ATOM   2120 C  C   . THR B 2 64  ? -10.339 15.940  -23.923  1.00 19.67  ? 64  THR B C   1 
ATOM   2121 O  O   . THR B 2 64  ? -9.693  16.351  -24.892  1.00 22.08  ? 64  THR B O   1 
ATOM   2122 C  CB  . THR B 2 64  ? -8.888  14.251  -22.765  1.00 19.85  ? 64  THR B CB  1 
ATOM   2123 O  OG1 . THR B 2 64  ? -8.728  12.845  -22.522  1.00 20.08  ? 64  THR B OG1 1 
ATOM   2124 C  CG2 . THR B 2 64  ? -8.866  15.004  -21.445  1.00 17.13  ? 64  THR B CG2 1 
ATOM   2125 N  N   . PRO B 2 65  ? -11.201 16.728  -23.290  1.00 28.46  ? 65  PRO B N   1 
ATOM   2126 C  CA  . PRO B 2 65  ? -11.315 18.142  -23.675  1.00 22.65  ? 65  PRO B CA  1 
ATOM   2127 C  C   . PRO B 2 65  ? -10.063 18.926  -23.305  1.00 23.55  ? 65  PRO B C   1 
ATOM   2128 O  O   . PRO B 2 65  ? -9.381  18.623  -22.323  1.00 22.29  ? 65  PRO B O   1 
ATOM   2129 C  CB  . PRO B 2 65  ? -12.532 18.625  -22.871  1.00 31.33  ? 65  PRO B CB  1 
ATOM   2130 C  CG  . PRO B 2 65  ? -13.311 17.379  -22.601  1.00 26.28  ? 65  PRO B CG  1 
ATOM   2131 C  CD  . PRO B 2 65  ? -12.242 16.353  -22.318  1.00 22.43  ? 65  PRO B CD  1 
ATOM   2132 N  N   . VAL B 2 66  ? -9.762  19.946  -24.111  1.00 19.27  ? 66  VAL B N   1 
ATOM   2133 C  CA  . VAL B 2 66  ? -8.657  20.853  -23.835  1.00 23.40  ? 66  VAL B CA  1 
ATOM   2134 C  C   . VAL B 2 66  ? -9.149  22.292  -23.881  1.00 31.93  ? 66  VAL B C   1 
ATOM   2135 O  O   . VAL B 2 66  ? -10.221 22.601  -24.407  1.00 31.09  ? 66  VAL B O   1 
ATOM   2136 C  CB  . VAL B 2 66  ? -7.473  20.683  -24.817  1.00 28.73  ? 66  VAL B CB  1 
ATOM   2137 C  CG1 . VAL B 2 66  ? -7.084  19.222  -24.965  1.00 26.44  ? 66  VAL B CG1 1 
ATOM   2138 C  CG2 . VAL B 2 66  ? -7.823  21.278  -26.176  1.00 30.12  ? 66  VAL B CG2 1 
ATOM   2139 N  N   . ARG B 2 67  ? -8.338  23.177  -23.318  1.00 28.02  ? 67  ARG B N   1 
ATOM   2140 C  CA  . ARG B 2 67  ? -8.514  24.612  -23.465  1.00 23.58  ? 67  ARG B CA  1 
ATOM   2141 C  C   . ARG B 2 67  ? -7.212  25.211  -23.971  1.00 27.19  ? 67  ARG B C   1 
ATOM   2142 O  O   . ARG B 2 67  ? -6.144  24.608  -23.855  1.00 33.14  ? 67  ARG B O   1 
ATOM   2143 C  CB  . ARG B 2 67  ? -8.909  25.263  -22.153  1.00 28.36  ? 67  ARG B CB  1 
ATOM   2144 C  CG  . ARG B 2 67  ? -7.725  25.491  -21.231  1.00 32.42  ? 67  ARG B CG  1 
ATOM   2145 C  CD  . ARG B 2 67  ? -8.081  25.090  -19.822  1.00 44.53  ? 67  ARG B CD  1 
ATOM   2146 N  NE  . ARG B 2 67  ? -8.855  26.156  -19.211  1.00 58.22  ? 67  ARG B NE  1 
ATOM   2147 C  CZ  . ARG B 2 67  ? -8.360  27.058  -18.377  1.00 70.06  ? 67  ARG B CZ  1 
ATOM   2148 N  NH1 . ARG B 2 67  ? -7.134  26.948  -17.885  1.00 61.23  ? 67  ARG B NH1 1 
ATOM   2149 N  NH2 . ARG B 2 67  ? -9.117  28.095  -18.023  1.00 77.14  ? 67  ARG B NH2 1 
ATOM   2150 N  N   . PHE B 2 68  ? -7.304  26.406  -24.536  1.00 29.26  ? 68  PHE B N   1 
ATOM   2151 C  CA  . PHE B 2 68  ? -6.176  27.055  -25.196  1.00 27.34  ? 68  PHE B CA  1 
ATOM   2152 C  C   . PHE B 2 68  ? -5.948  28.395  -24.506  1.00 28.13  ? 68  PHE B C   1 
ATOM   2153 O  O   . PHE B 2 68  ? -6.803  29.284  -24.563  1.00 25.89  ? 68  PHE B O   1 
ATOM   2154 C  CB  . PHE B 2 68  ? -6.457  27.231  -26.688  1.00 33.78  ? 68  PHE B CB  1 
ATOM   2155 C  CG  . PHE B 2 68  ? -6.575  25.928  -27.441  1.00 33.27  ? 68  PHE B CG  1 
ATOM   2156 C  CD1 . PHE B 2 68  ? -7.824  25.409  -27.763  1.00 36.53  ? 68  PHE B CD1 1 
ATOM   2157 C  CD2 . PHE B 2 68  ? -5.446  25.245  -27.852  1.00 32.86  ? 68  PHE B CD2 1 
ATOM   2158 C  CE1 . PHE B 2 68  ? -7.946  24.207  -28.448  1.00 33.89  ? 68  PHE B CE1 1 
ATOM   2159 C  CE2 . PHE B 2 68  ? -5.551  24.049  -28.551  1.00 37.03  ? 68  PHE B CE2 1 
ATOM   2160 C  CZ  . PHE B 2 68  ? -6.805  23.527  -28.848  1.00 45.15  ? 68  PHE B CZ  1 
ATOM   2161 N  N   . ILE B 2 69  ? -4.815  28.532  -23.834  1.00 27.89  ? 69  ILE B N   1 
ATOM   2162 C  CA  . ILE B 2 69  ? -4.513  29.740  -23.060  1.00 30.89  ? 69  ILE B CA  1 
ATOM   2163 C  C   . ILE B 2 69  ? -3.633  30.608  -23.881  1.00 31.70  ? 69  ILE B C   1 
ATOM   2164 O  O   . ILE B 2 69  ? -2.429  30.296  -24.088  1.00 30.33  ? 69  ILE B O   1 
ATOM   2165 C  CB  . ILE B 2 69  ? -3.891  29.395  -21.698  1.00 29.31  ? 69  ILE B CB  1 
ATOM   2166 C  CG1 . ILE B 2 69  ? -4.796  28.412  -20.944  1.00 30.50  ? 69  ILE B CG1 1 
ATOM   2167 C  CG2 . ILE B 2 69  ? -3.622  30.648  -20.908  1.00 25.49  ? 69  ILE B CG2 1 
ATOM   2168 C  CD1 . ILE B 2 69  ? -4.332  26.986  -21.010  1.00 31.42  ? 69  ILE B CD1 1 
ATOM   2169 N  N   . PRO B 2 70  ? -4.116  31.714  -24.457  1.00 34.38  ? 70  PRO B N   1 
ATOM   2170 C  CA  . PRO B 2 70  ? -3.282  32.596  -25.243  1.00 33.81  ? 70  PRO B CA  1 
ATOM   2171 C  C   . PRO B 2 70  ? -2.320  33.315  -24.324  1.00 41.14  ? 70  PRO B C   1 
ATOM   2172 O  O   . PRO B 2 70  ? -2.639  33.618  -23.170  1.00 28.23  ? 70  PRO B O   1 
ATOM   2173 C  CB  . PRO B 2 70  ? -4.275  33.576  -25.885  1.00 34.42  ? 70  PRO B CB  1 
ATOM   2174 C  CG  . PRO B 2 70  ? -5.618  32.988  -25.648  1.00 44.90  ? 70  PRO B CG  1 
ATOM   2175 C  CD  . PRO B 2 70  ? -5.492  32.246  -24.346  1.00 39.55  ? 70  PRO B CD  1 
ATOM   2176 N  N   . LEU B 2 71  ? -1.123  33.571  -24.841  1.00 46.29  ? 71  LEU B N   1 
ATOM   2177 C  CA  . LEU B 2 71  ? -0.128  34.259  -24.033  1.00 45.91  ? 71  LEU B CA  1 
ATOM   2178 C  C   . LEU B 2 71  ? -0.617  35.647  -23.637  1.00 53.24  ? 71  LEU B C   1 
ATOM   2179 O  O   . LEU B 2 71  ? -0.348  36.110  -22.525  1.00 52.97  ? 71  LEU B O   1 
ATOM   2180 C  CB  . LEU B 2 71  ? 1.187   34.325  -24.795  1.00 42.58  ? 71  LEU B CB  1 
ATOM   2181 C  CG  . LEU B 2 71  ? 2.409   34.708  -23.986  1.00 45.94  ? 71  LEU B CG  1 
ATOM   2182 C  CD1 . LEU B 2 71  ? 2.456   33.920  -22.679  1.00 40.61  ? 71  LEU B CD1 1 
ATOM   2183 C  CD2 . LEU B 2 71  ? 3.633   34.429  -24.854  1.00 38.08  ? 71  LEU B CD2 1 
ATOM   2184 N  N   . SER B 2 72  ? -1.368  36.308  -24.520  1.00 58.01  ? 72  SER B N   1 
ATOM   2185 C  CA  . SER B 2 72  ? -2.048  37.560  -24.197  1.00 55.07  ? 72  SER B CA  1 
ATOM   2186 C  C   . SER B 2 72  ? -3.421  37.570  -24.866  1.00 58.30  ? 72  SER B C   1 
ATOM   2187 O  O   . SER B 2 72  ? -3.862  36.577  -25.455  1.00 48.24  ? 72  SER B O   1 
ATOM   2188 C  CB  . SER B 2 72  ? -1.218  38.774  -24.627  1.00 57.66  ? 72  SER B CB  1 
ATOM   2189 O  OG  . SER B 2 72  ? -1.735  39.946  -24.020  1.00 69.34  ? 72  SER B OG  1 
ATOM   2190 N  N   . GLY B 2 73  ? -4.095  38.718  -24.780  1.00 46.07  ? 73  GLY B N   1 
ATOM   2191 C  CA  . GLY B 2 73  ? -5.423  38.893  -25.327  1.00 36.51  ? 73  GLY B CA  1 
ATOM   2192 C  C   . GLY B 2 73  ? -6.431  37.887  -24.789  1.00 46.06  ? 73  GLY B C   1 
ATOM   2193 O  O   . GLY B 2 73  ? -6.209  37.178  -23.805  1.00 51.91  ? 73  GLY B O   1 
ATOM   2194 N  N   . ALA B 2 74  ? -7.568  37.839  -25.485  1.00 55.04  ? 74  ALA B N   1 
ATOM   2195 C  CA  . ALA B 2 74  ? -8.634  36.892  -25.181  1.00 60.55  ? 74  ALA B CA  1 
ATOM   2196 C  C   . ALA B 2 74  ? -9.219  36.242  -26.434  1.00 57.97  ? 74  ALA B C   1 
ATOM   2197 O  O   . ALA B 2 74  ? -10.265 35.583  -26.347  1.00 53.17  ? 74  ALA B O   1 
ATOM   2198 C  CB  . ALA B 2 74  ? -9.746  37.574  -24.368  1.00 60.36  ? 74  ALA B CB  1 
ATOM   2199 N  N   . ASN B 2 75  ? -8.593  36.425  -27.594  1.00 57.29  ? 75  ASN B N   1 
ATOM   2200 C  CA  . ASN B 2 75  ? -8.925  35.672  -28.794  1.00 56.61  ? 75  ASN B CA  1 
ATOM   2201 C  C   . ASN B 2 75  ? -7.867  34.594  -29.026  1.00 56.51  ? 75  ASN B C   1 
ATOM   2202 O  O   . ASN B 2 75  ? -6.803  34.579  -28.395  1.00 54.97  ? 75  ASN B O   1 
ATOM   2203 C  CB  . ASN B 2 75  ? -9.041  36.603  -30.014  1.00 60.31  ? 75  ASN B CB  1 
ATOM   2204 C  CG  . ASN B 2 75  ? -10.140 37.652  -29.845  1.00 66.19  ? 75  ASN B CG  1 
ATOM   2205 O  OD1 . ASN B 2 75  ? -11.011 37.511  -28.984  1.00 71.07  ? 75  ASN B OD1 1 
ATOM   2206 N  ND2 . ASN B 2 75  ? -10.118 38.690  -30.680  1.00 46.65  ? 75  ASN B ND2 1 
ATOM   2207 N  N   . ILE B 2 76  ? -8.175  33.666  -29.927  1.00 41.38  ? 76  ILE B N   1 
ATOM   2208 C  CA  . ILE B 2 76  ? -7.214  32.660  -30.354  1.00 41.09  ? 76  ILE B CA  1 
ATOM   2209 C  C   . ILE B 2 76  ? -7.047  32.822  -31.860  1.00 43.10  ? 76  ILE B C   1 
ATOM   2210 O  O   . ILE B 2 76  ? -7.991  32.587  -32.627  1.00 43.45  ? 76  ILE B O   1 
ATOM   2211 C  CB  . ILE B 2 76  ? -7.641  31.233  -29.960  1.00 50.05  ? 76  ILE B CB  1 
ATOM   2212 C  CG1 . ILE B 2 76  ? -7.668  31.066  -28.436  1.00 37.64  ? 76  ILE B CG1 1 
ATOM   2213 C  CG2 . ILE B 2 76  ? -6.678  30.203  -30.496  1.00 43.30  ? 76  ILE B CG2 1 
ATOM   2214 C  CD1 . ILE B 2 76  ? -8.843  30.294  -27.921  1.00 36.91  ? 76  ILE B CD1 1 
ATOM   2215 N  N   . PHE B 2 77  ? -5.860  33.257  -32.277  1.00 38.88  ? 77  PHE B N   1 
ATOM   2216 C  CA  . PHE B 2 77  ? -5.535  33.496  -33.675  1.00 48.16  ? 77  PHE B CA  1 
ATOM   2217 C  C   . PHE B 2 77  ? -4.562  32.446  -34.187  1.00 43.85  ? 77  PHE B C   1 
ATOM   2218 O  O   . PHE B 2 77  ? -3.796  31.858  -33.416  1.00 41.45  ? 77  PHE B O   1 
ATOM   2219 C  CB  . PHE B 2 77  ? -4.909  34.881  -33.870  1.00 52.20  ? 77  PHE B CB  1 
ATOM   2220 C  CG  . PHE B 2 77  ? -5.850  36.017  -33.604  1.00 62.76  ? 77  PHE B CG  1 
ATOM   2221 C  CD1 . PHE B 2 77  ? -6.932  36.242  -34.442  1.00 62.67  ? 77  PHE B CD1 1 
ATOM   2222 C  CD2 . PHE B 2 77  ? -5.636  36.887  -32.535  1.00 62.89  ? 77  PHE B CD2 1 
ATOM   2223 C  CE1 . PHE B 2 77  ? -7.806  37.299  -34.209  1.00 63.48  ? 77  PHE B CE1 1 
ATOM   2224 C  CE2 . PHE B 2 77  ? -6.505  37.949  -32.300  1.00 60.95  ? 77  PHE B CE2 1 
ATOM   2225 C  CZ  . PHE B 2 77  ? -7.590  38.152  -33.140  1.00 60.61  ? 77  PHE B CZ  1 
ATOM   2226 N  N   . GLU B 2 78  ? -4.592  32.228  -35.506  1.00 39.07  ? 78  GLU B N   1 
ATOM   2227 C  CA  . GLU B 2 78  ? -3.552  31.437  -36.161  1.00 40.55  ? 78  GLU B CA  1 
ATOM   2228 C  C   . GLU B 2 78  ? -2.176  32.061  -35.922  1.00 41.55  ? 78  GLU B C   1 
ATOM   2229 O  O   . GLU B 2 78  ? -2.032  33.285  -35.859  1.00 50.47  ? 78  GLU B O   1 
ATOM   2230 C  CB  . GLU B 2 78  ? -3.826  31.327  -37.667  1.00 33.87  ? 78  GLU B CB  1 
ATOM   2231 C  CG  . GLU B 2 78  ? -5.107  30.566  -38.032  1.00 41.32  ? 78  GLU B CG  1 
ATOM   2232 C  CD  . GLU B 2 78  ? -5.445  30.601  -39.541  1.00 51.70  ? 78  GLU B CD  1 
ATOM   2233 O  OE1 . GLU B 2 78  ? -4.517  30.723  -40.376  1.00 46.20  ? 78  GLU B OE1 1 
ATOM   2234 O  OE2 . GLU B 2 78  ? -6.649  30.506  -39.889  1.00 42.31  ? 78  GLU B OE2 1 
ATOM   2235 N  N   . ASP B 2 79  ? -1.163  31.209  -35.769  1.00 38.69  ? 79  ASP B N   1 
ATOM   2236 C  CA  . ASP B 2 79  ? 0.237   31.593  -35.574  1.00 41.10  ? 79  ASP B CA  1 
ATOM   2237 C  C   . ASP B 2 79  ? 0.490   32.371  -34.284  1.00 41.69  ? 79  ASP B C   1 
ATOM   2238 O  O   . ASP B 2 79  ? 1.600   32.876  -34.081  1.00 61.18  ? 79  ASP B O   1 
ATOM   2239 C  CB  . ASP B 2 79  ? 0.783   32.392  -36.765  1.00 44.70  ? 79  ASP B CB  1 
ATOM   2240 C  CG  . ASP B 2 79  ? 2.235   32.034  -37.100  1.00 60.02  ? 79  ASP B CG  1 
ATOM   2241 O  OD1 . ASP B 2 79  ? 3.063   32.961  -37.226  1.00 62.16  ? 79  ASP B OD1 1 
ATOM   2242 O  OD2 . ASP B 2 79  ? 2.557   30.827  -37.225  1.00 65.04  ? 79  ASP B OD2 1 
ATOM   2243 N  N   . GLN B 2 80  ? -0.483  32.462  -33.391  1.00 36.36  ? 80  GLN B N   1 
ATOM   2244 C  CA  . GLN B 2 80  ? -0.278  33.094  -32.094  1.00 36.60  ? 80  GLN B CA  1 
ATOM   2245 C  C   . GLN B 2 80  ? 0.146   32.054  -31.052  1.00 39.36  ? 80  GLN B C   1 
ATOM   2246 O  O   . GLN B 2 80  ? -0.373  30.929  -31.038  1.00 39.06  ? 80  GLN B O   1 
ATOM   2247 C  CB  . GLN B 2 80  ? -1.568  33.803  -31.682  1.00 33.87  ? 80  GLN B CB  1 
ATOM   2248 C  CG  . GLN B 2 80  ? -1.747  34.083  -30.223  1.00 36.64  ? 80  GLN B CG  1 
ATOM   2249 C  CD  . GLN B 2 80  ? -3.151  34.548  -29.921  1.00 45.63  ? 80  GLN B CD  1 
ATOM   2250 O  OE1 . GLN B 2 80  ? -4.099  34.202  -30.633  1.00 47.78  ? 80  GLN B OE1 1 
ATOM   2251 N  NE2 . GLN B 2 80  ? -3.299  35.340  -28.868  1.00 45.45  ? 80  GLN B NE2 1 
ATOM   2252 N  N   . LEU B 2 81  ? 1.094   32.430  -30.183  1.00 37.43  ? 81  LEU B N   1 
ATOM   2253 C  CA  . LEU B 2 81  ? 1.600   31.513  -29.159  1.00 36.12  ? 81  LEU B CA  1 
ATOM   2254 C  C   . LEU B 2 81  ? 0.556   31.233  -28.083  1.00 30.17  ? 81  LEU B C   1 
ATOM   2255 O  O   . LEU B 2 81  ? -0.213  32.108  -27.686  1.00 32.15  ? 81  LEU B O   1 
ATOM   2256 C  CB  . LEU B 2 81  ? 2.856   32.060  -28.474  1.00 33.03  ? 81  LEU B CB  1 
ATOM   2257 C  CG  . LEU B 2 81  ? 4.199   32.059  -29.214  1.00 36.44  ? 81  LEU B CG  1 
ATOM   2258 C  CD1 . LEU B 2 81  ? 5.276   32.684  -28.358  1.00 32.91  ? 81  LEU B CD1 1 
ATOM   2259 C  CD2 . LEU B 2 81  ? 4.630   30.687  -29.634  1.00 33.31  ? 81  LEU B CD2 1 
ATOM   2260 N  N   . LEU B 2 82  ? 0.559   30.002  -27.583  1.00 34.02  ? 82  LEU B N   1 
ATOM   2261 C  CA  . LEU B 2 82  ? -0.425  29.619  -26.582  1.00 37.44  ? 82  LEU B CA  1 
ATOM   2262 C  C   . LEU B 2 82  ? 0.016   28.321  -25.925  1.00 32.46  ? 82  LEU B C   1 
ATOM   2263 O  O   . LEU B 2 82  ? 0.849   27.577  -26.467  1.00 30.01  ? 82  LEU B O   1 
ATOM   2264 C  CB  . LEU B 2 82  ? -1.834  29.475  -27.198  1.00 33.62  ? 82  LEU B CB  1 
ATOM   2265 C  CG  . LEU B 2 82  ? -2.050  28.629  -28.453  1.00 31.38  ? 82  LEU B CG  1 
ATOM   2266 C  CD1 . LEU B 2 82  ? -1.874  27.128  -28.198  1.00 37.45  ? 82  LEU B CD1 1 
ATOM   2267 C  CD2 . LEU B 2 82  ? -3.410  28.907  -29.069  1.00 35.80  ? 82  LEU B CD2 1 
ATOM   2268 N  N   . ASN B 2 83  ? -0.574  28.054  -24.760  1.00 23.63  ? 83  ASN B N   1 
ATOM   2269 C  CA  . ASN B 2 83  ? -0.401  26.806  -24.033  1.00 26.60  ? 83  ASN B CA  1 
ATOM   2270 C  C   . ASN B 2 83  ? -1.655  25.957  -24.192  1.00 24.90  ? 83  ASN B C   1 
ATOM   2271 O  O   . ASN B 2 83  ? -2.748  26.471  -24.447  1.00 25.15  ? 83  ASN B O   1 
ATOM   2272 C  CB  . ASN B 2 83  ? -0.145  27.052  -22.544  1.00 24.03  ? 83  ASN B CB  1 
ATOM   2273 C  CG  . ASN B 2 83  ? 0.967   28.054  -22.288  1.00 28.74  ? 83  ASN B CG  1 
ATOM   2274 O  OD1 . ASN B 2 83  ? 0.737   29.120  -21.702  1.00 34.54  ? 83  ASN B OD1 1 
ATOM   2275 N  ND2 . ASN B 2 83  ? 2.181   27.713  -22.709  1.00 25.87  ? 83  ASN B ND2 1 
ATOM   2276 N  N   . ILE B 2 84  ? -1.496  24.648  -24.012  1.00 27.64  ? 84  ILE B N   1 
ATOM   2277 C  CA  . ILE B 2 84  ? -2.593  23.691  -24.149  1.00 30.87  ? 84  ILE B CA  1 
ATOM   2278 C  C   . ILE B 2 84  ? -2.740  22.906  -22.858  1.00 26.55  ? 84  ILE B C   1 
ATOM   2279 O  O   . ILE B 2 84  ? -1.757  22.370  -22.331  1.00 27.55  ? 84  ILE B O   1 
ATOM   2280 C  CB  . ILE B 2 84  ? -2.394  22.742  -25.348  1.00 23.93  ? 84  ILE B CB  1 
ATOM   2281 C  CG1 . ILE B 2 84  ? -2.166  23.568  -26.612  1.00 23.12  ? 84  ILE B CG1 1 
ATOM   2282 C  CG2 . ILE B 2 84  ? -3.594  21.822  -25.511  1.00 19.73  ? 84  ILE B CG2 1 
ATOM   2283 C  CD1 . ILE B 2 84  ? -2.121  22.773  -27.838  1.00 26.42  ? 84  ILE B CD1 1 
ATOM   2284 N  N   . GLN B 2 85  ? -3.972  22.816  -22.366  1.00 25.45  ? 85  GLN B N   1 
ATOM   2285 C  CA  . GLN B 2 85  ? -4.246  22.106  -21.130  1.00 28.34  ? 85  GLN B CA  1 
ATOM   2286 C  C   . GLN B 2 85  ? -5.508  21.268  -21.271  1.00 24.35  ? 85  GLN B C   1 
ATOM   2287 O  O   . GLN B 2 85  ? -6.569  21.802  -21.600  1.00 26.20  ? 85  GLN B O   1 
ATOM   2288 C  CB  . GLN B 2 85  ? -4.391  23.094  -19.966  1.00 22.69  ? 85  GLN B CB  1 
ATOM   2289 C  CG  . GLN B 2 85  ? -4.747  22.427  -18.631  1.00 19.55  ? 85  GLN B CG  1 
ATOM   2290 C  CD  . GLN B 2 85  ? -4.916  23.437  -17.498  1.00 22.95  ? 85  GLN B CD  1 
ATOM   2291 O  OE1 . GLN B 2 85  ? -5.268  24.597  -17.727  1.00 19.47  ? 85  GLN B OE1 1 
ATOM   2292 N  NE2 . GLN B 2 85  ? -4.631  23.003  -16.276  1.00 17.95  ? 85  GLN B NE2 1 
ATOM   2293 N  N   . PHE B 2 86  ? -5.396  19.963  -21.014  1.00 22.17  ? 86  PHE B N   1 
ATOM   2294 C  CA  . PHE B 2 86  ? -6.598  19.166  -20.837  1.00 25.68  ? 86  PHE B CA  1 
ATOM   2295 C  C   . PHE B 2 86  ? -7.380  19.745  -19.679  1.00 28.87  ? 86  PHE B C   1 
ATOM   2296 O  O   . PHE B 2 86  ? -6.800  20.178  -18.678  1.00 30.89  ? 86  PHE B O   1 
ATOM   2297 C  CB  . PHE B 2 86  ? -6.284  17.704  -20.523  1.00 23.23  ? 86  PHE B CB  1 
ATOM   2298 C  CG  . PHE B 2 86  ? -5.621  16.972  -21.630  1.00 25.02  ? 86  PHE B CG  1 
ATOM   2299 C  CD1 . PHE B 2 86  ? -6.292  16.710  -22.802  1.00 25.31  ? 86  PHE B CD1 1 
ATOM   2300 C  CD2 . PHE B 2 86  ? -4.318  16.512  -21.487  1.00 22.25  ? 86  PHE B CD2 1 
ATOM   2301 C  CE1 . PHE B 2 86  ? -5.662  16.012  -23.828  1.00 33.69  ? 86  PHE B CE1 1 
ATOM   2302 C  CE2 . PHE B 2 86  ? -3.693  15.814  -22.507  1.00 20.42  ? 86  PHE B CE2 1 
ATOM   2303 C  CZ  . PHE B 2 86  ? -4.362  15.563  -23.672  1.00 21.16  ? 86  PHE B CZ  1 
ATOM   2304 N  N   . ASN B 2 87  ? -8.698  19.729  -19.813  1.00 29.45  ? 87  ASN B N   1 
ATOM   2305 C  CA  . ASN B 2 87  ? -9.630  20.322  -18.863  1.00 33.51  ? 87  ASN B CA  1 
ATOM   2306 C  C   . ASN B 2 87  ? -10.443 19.168  -18.301  1.00 36.41  ? 87  ASN B C   1 
ATOM   2307 O  O   . ASN B 2 87  ? -11.449 18.757  -18.883  1.00 34.21  ? 87  ASN B O   1 
ATOM   2308 C  CB  . ASN B 2 87  ? -10.511 21.367  -19.535  1.00 39.92  ? 87  ASN B CB  1 
ATOM   2309 C  CG  . ASN B 2 87  ? -10.971 22.440  -18.576  1.00 61.77  ? 87  ASN B CG  1 
ATOM   2310 O  OD1 . ASN B 2 87  ? -10.239 22.830  -17.660  1.00 66.84  ? 87  ASN B OD1 1 
ATOM   2311 N  ND2 . ASN B 2 87  ? -12.189 22.928  -18.780  1.00 56.11  ? 87  ASN B ND2 1 
ATOM   2312 N  N   . ILE B 2 88  ? -9.982  18.613  -17.189  1.00 37.22  ? 88  ILE B N   1 
ATOM   2313 C  CA  . ILE B 2 88  ? -10.665 17.477  -16.587  1.00 35.04  ? 88  ILE B CA  1 
ATOM   2314 C  C   . ILE B 2 88  ? -10.609 17.605  -15.069  1.00 41.95  ? 88  ILE B C   1 
ATOM   2315 O  O   . ILE B 2 88  ? -9.699  18.249  -14.522  1.00 33.81  ? 88  ILE B O   1 
ATOM   2316 C  CB  . ILE B 2 88  ? -10.058 16.147  -17.069  1.00 33.11  ? 88  ILE B CB  1 
ATOM   2317 C  CG1 . ILE B 2 88  ? -8.552  16.142  -16.906  1.00 27.27  ? 88  ILE B CG1 1 
ATOM   2318 C  CG2 . ILE B 2 88  ? -10.467 15.844  -18.500  1.00 47.98  ? 88  ILE B CG2 1 
ATOM   2319 C  CD1 . ILE B 2 88  ? -8.128  15.327  -15.717  1.00 42.75  ? 88  ILE B CD1 1 
ATOM   2320 N  N   . PRO B 2 89  ? -11.571 17.030  -14.356  1.00 44.12  ? 89  PRO B N   1 
ATOM   2321 C  CA  . PRO B 2 89  ? -11.504 17.014  -12.893  1.00 38.28  ? 89  PRO B CA  1 
ATOM   2322 C  C   . PRO B 2 89  ? -10.291 16.223  -12.451  1.00 39.48  ? 89  PRO B C   1 
ATOM   2323 O  O   . PRO B 2 89  ? -10.127 15.054  -12.812  1.00 51.80  ? 89  PRO B O   1 
ATOM   2324 C  CB  . PRO B 2 89  ? -12.797 16.297  -12.491  1.00 39.97  ? 89  PRO B CB  1 
ATOM   2325 C  CG  . PRO B 2 89  ? -13.136 15.474  -13.683  1.00 39.51  ? 89  PRO B CG  1 
ATOM   2326 C  CD  . PRO B 2 89  ? -12.767 16.336  -14.848  1.00 35.44  ? 89  PRO B CD  1 
ATOM   2327 N  N   . THR B 2 90  ? -9.450  16.856  -11.648  1.00 42.50  ? 90  THR B N   1 
ATOM   2328 C  CA  . THR B 2 90  ? -8.263  16.183  -11.153  1.00 39.61  ? 90  THR B CA  1 
ATOM   2329 C  C   . THR B 2 90  ? -7.823  16.864  -9.863   1.00 36.04  ? 90  THR B C   1 
ATOM   2330 O  O   . THR B 2 90  ? -8.215  17.992  -9.570   1.00 34.89  ? 90  THR B O   1 
ATOM   2331 C  CB  . THR B 2 90  ? -7.157  16.183  -12.223  1.00 45.31  ? 90  THR B CB  1 
ATOM   2332 O  OG1 . THR B 2 90  ? -6.266  15.077  -12.002  1.00 47.71  ? 90  THR B OG1 1 
ATOM   2333 C  CG2 . THR B 2 90  ? -6.387  17.506  -12.227  1.00 30.83  ? 90  THR B CG2 1 
ATOM   2334 N  N   . VAL B 2 91  ? -7.024  16.149  -9.081   1.00 32.95  ? 91  VAL B N   1 
ATOM   2335 C  CA  . VAL B 2 91  ? -6.544  16.676  -7.814   1.00 33.30  ? 91  VAL B CA  1 
ATOM   2336 C  C   . VAL B 2 91  ? -5.366  17.590  -8.107   1.00 33.87  ? 91  VAL B C   1 
ATOM   2337 O  O   . VAL B 2 91  ? -4.879  17.620  -9.240   1.00 36.70  ? 91  VAL B O   1 
ATOM   2338 C  CB  . VAL B 2 91  ? -6.175  15.535  -6.854   1.00 31.59  ? 91  VAL B CB  1 
ATOM   2339 C  CG1 . VAL B 2 91  ? -7.441  14.834  -6.393   1.00 33.25  ? 91  VAL B CG1 1 
ATOM   2340 C  CG2 . VAL B 2 91  ? -5.263  14.547  -7.537   1.00 32.76  ? 91  VAL B CG2 1 
ATOM   2341 N  N   . LYS B 2 92  ? -4.908  18.343  -7.097   1.00 32.37  ? 92  LYS B N   1 
ATOM   2342 C  CA  . LYS B 2 92  ? -3.846  19.330  -7.314   1.00 36.69  ? 92  LYS B CA  1 
ATOM   2343 C  C   . LYS B 2 92  ? -2.571  18.693  -7.858   1.00 35.91  ? 92  LYS B C   1 
ATOM   2344 O  O   . LYS B 2 92  ? -1.891  19.280  -8.705   1.00 32.45  ? 92  LYS B O   1 
ATOM   2345 C  CB  . LYS B 2 92  ? -3.536  20.071  -6.018   1.00 28.87  ? 92  LYS B CB  1 
ATOM   2346 C  CG  . LYS B 2 92  ? -2.457  21.149  -6.165   1.00 38.01  ? 92  LYS B CG  1 
ATOM   2347 C  CD  . LYS B 2 92  ? -2.393  22.037  -4.921   1.00 50.47  ? 92  LYS B CD  1 
ATOM   2348 C  CE  . LYS B 2 92  ? -0.984  22.595  -4.707   1.00 55.71  ? 92  LYS B CE  1 
ATOM   2349 N  NZ  . LYS B 2 92  ? -0.649  22.696  -3.246   1.00 56.53  ? 92  LYS B NZ  1 
ATOM   2350 N  N   . LEU B 2 93  ? -2.227  17.501  -7.368   1.00 30.89  ? 93  LEU B N   1 
ATOM   2351 C  CA  . LEU B 2 93  ? -1.013  16.818  -7.799   1.00 36.41  ? 93  LEU B CA  1 
ATOM   2352 C  C   . LEU B 2 93  ? -0.949  16.661  -9.315   1.00 33.08  ? 93  LEU B C   1 
ATOM   2353 O  O   . LEU B 2 93  ? 0.129   16.737  -9.910   1.00 34.02  ? 93  LEU B O   1 
ATOM   2354 C  CB  . LEU B 2 93  ? -0.935  15.447  -7.124   1.00 35.01  ? 93  LEU B CB  1 
ATOM   2355 C  CG  . LEU B 2 93  ? 0.237   14.547  -7.500   1.00 37.72  ? 93  LEU B CG  1 
ATOM   2356 C  CD1 . LEU B 2 93  ? 1.489   15.048  -6.839   1.00 28.03  ? 93  LEU B CD1 1 
ATOM   2357 C  CD2 . LEU B 2 93  ? -0.037  13.101  -7.110   1.00 38.42  ? 93  LEU B CD2 1 
ATOM   2358 N  N   . CYS B 2 94  ? -2.089  16.432  -9.958   1.00 36.62  ? 94  CYS B N   1 
ATOM   2359 C  CA  . CYS B 2 94  ? -2.108  16.150  -11.386  1.00 31.37  ? 94  CYS B CA  1 
ATOM   2360 C  C   . CYS B 2 94  ? -2.417  17.365  -12.246  1.00 29.57  ? 94  CYS B C   1 
ATOM   2361 O  O   . CYS B 2 94  ? -2.554  17.203  -13.466  1.00 26.10  ? 94  CYS B O   1 
ATOM   2362 C  CB  . CYS B 2 94  ? -3.133  15.058  -11.725  1.00 25.66  ? 94  CYS B CB  1 
ATOM   2363 S  SG  . CYS B 2 94  ? -2.940  13.453  -10.966  1.00 42.05  ? 94  CYS B SG  1 
ATOM   2364 N  N   . VAL B 2 95  ? -2.555  18.565  -11.665  1.00 27.50  ? 95  VAL B N   1 
ATOM   2365 C  CA  . VAL B 2 95  ? -2.860  19.731  -12.495  1.00 24.03  ? 95  VAL B CA  1 
ATOM   2366 C  C   . VAL B 2 95  ? -1.776  19.929  -13.539  1.00 24.60  ? 95  VAL B C   1 
ATOM   2367 O  O   . VAL B 2 95  ? -2.062  20.062  -14.737  1.00 24.73  ? 95  VAL B O   1 
ATOM   2368 C  CB  . VAL B 2 95  ? -3.044  21.002  -11.656  1.00 29.29  ? 95  VAL B CB  1 
ATOM   2369 C  CG1 . VAL B 2 95  ? -3.107  22.209  -12.605  1.00 18.36  ? 95  VAL B CG1 1 
ATOM   2370 C  CG2 . VAL B 2 95  ? -4.325  20.916  -10.863  1.00 26.10  ? 95  VAL B CG2 1 
ATOM   2371 N  N   . SER B 2 96  ? -0.514  19.938  -13.107  1.00 16.31  ? 96  SER B N   1 
ATOM   2372 C  CA  . SER B 2 96  ? 0.551   20.136  -14.081  1.00 25.36  ? 96  SER B CA  1 
ATOM   2373 C  C   . SER B 2 96  ? 0.496   19.052  -15.152  1.00 25.35  ? 96  SER B C   1 
ATOM   2374 O  O   . SER B 2 96  ? 0.725   19.323  -16.339  1.00 25.81  ? 96  SER B O   1 
ATOM   2375 C  CB  . SER B 2 96  ? 1.909   20.163  -13.386  1.00 22.36  ? 96  SER B CB  1 
ATOM   2376 O  OG  . SER B 2 96  ? 2.202   18.887  -12.845  1.00 36.35  ? 96  SER B OG  1 
ATOM   2377 N  N   . TYR B 2 97  ? 0.105   17.840  -14.764  1.00 24.10  ? 97  TYR B N   1 
ATOM   2378 C  CA  . TYR B 2 97  ? -0.054  16.723  -15.689  1.00 26.16  ? 97  TYR B CA  1 
ATOM   2379 C  C   . TYR B 2 97  ? -1.324  16.818  -16.533  1.00 24.11  ? 97  TYR B C   1 
ATOM   2380 O  O   . TYR B 2 97  ? -1.713  15.838  -17.184  1.00 21.85  ? 97  TYR B O   1 
ATOM   2381 C  CB  . TYR B 2 97  ? 0.004   15.409  -14.904  1.00 20.89  ? 97  TYR B CB  1 
ATOM   2382 C  CG  . TYR B 2 97  ? 1.413   15.120  -14.492  1.00 27.04  ? 97  TYR B CG  1 
ATOM   2383 C  CD1 . TYR B 2 97  ? 2.375   14.823  -15.439  1.00 24.25  ? 97  TYR B CD1 1 
ATOM   2384 C  CD2 . TYR B 2 97  ? 1.802   15.214  -13.164  1.00 35.02  ? 97  TYR B CD2 1 
ATOM   2385 C  CE1 . TYR B 2 97  ? 3.678   14.587  -15.071  1.00 33.30  ? 97  TYR B CE1 1 
ATOM   2386 C  CE2 . TYR B 2 97  ? 3.098   14.974  -12.783  1.00 29.65  ? 97  TYR B CE2 1 
ATOM   2387 C  CZ  . TYR B 2 97  ? 4.032   14.665  -13.739  1.00 44.07  ? 97  TYR B CZ  1 
ATOM   2388 O  OH  . TYR B 2 97  ? 5.326   14.434  -13.363  1.00 54.47  ? 97  TYR B OH  1 
ATOM   2389 N  N   . THR B 2 98  ? -1.978  17.974  -16.564  1.00 20.20  ? 98  THR B N   1 
ATOM   2390 C  CA  . THR B 2 98  ? -2.954  18.235  -17.603  1.00 24.63  ? 98  THR B CA  1 
ATOM   2391 C  C   . THR B 2 98  ? -2.416  19.197  -18.645  1.00 25.21  ? 98  THR B C   1 
ATOM   2392 O  O   . THR B 2 98  ? -3.089  19.433  -19.661  1.00 24.24  ? 98  THR B O   1 
ATOM   2393 C  CB  . THR B 2 98  ? -4.243  18.815  -17.007  1.00 21.99  ? 98  THR B CB  1 
ATOM   2394 O  OG1 . THR B 2 98  ? -3.984  20.143  -16.539  1.00 16.40  ? 98  THR B OG1 1 
ATOM   2395 C  CG2 . THR B 2 98  ? -4.694  17.956  -15.814  1.00 18.73  ? 98  THR B CG2 1 
ATOM   2396 N  N   . ILE B 2 99  ? -1.238  19.770  -18.410  1.00 21.12  ? 99  ILE B N   1 
ATOM   2397 C  CA  . ILE B 2 99  ? -0.728  20.872  -19.219  1.00 26.59  ? 99  ILE B CA  1 
ATOM   2398 C  C   . ILE B 2 99  ? 0.298   20.334  -20.194  1.00 24.47  ? 99  ILE B C   1 
ATOM   2399 O  O   . ILE B 2 99  ? 1.260   19.664  -19.791  1.00 25.70  ? 99  ILE B O   1 
ATOM   2400 C  CB  . ILE B 2 99  ? -0.119  21.987  -18.349  1.00 29.11  ? 99  ILE B CB  1 
ATOM   2401 C  CG1 . ILE B 2 99  ? -1.161  22.562  -17.384  1.00 25.08  ? 99  ILE B CG1 1 
ATOM   2402 C  CG2 . ILE B 2 99  ? 0.518   23.079  -19.217  1.00 20.41  ? 99  ILE B CG2 1 
ATOM   2403 C  CD1 . ILE B 2 99  ? -0.568  23.563  -16.402  1.00 18.69  ? 99  ILE B CD1 1 
ATOM   2404 N  N   . TRP B 2 100 ? 0.120   20.663  -21.468  1.00 23.46  ? 100 TRP B N   1 
ATOM   2405 C  CA  . TRP B 2 100 ? 0.978   20.093  -22.495  1.00 28.10  ? 100 TRP B CA  1 
ATOM   2406 C  C   . TRP B 2 100 ? 2.386   20.663  -22.405  1.00 26.51  ? 100 TRP B C   1 
ATOM   2407 O  O   . TRP B 2 100 ? 2.581   21.837  -22.072  1.00 25.96  ? 100 TRP B O   1 
ATOM   2408 C  CB  . TRP B 2 100 ? 0.413   20.354  -23.880  1.00 26.18  ? 100 TRP B CB  1 
ATOM   2409 C  CG  . TRP B 2 100 ? -0.873  19.646  -24.176  1.00 25.90  ? 100 TRP B CG  1 
ATOM   2410 C  CD1 . TRP B 2 100 ? -1.819  19.234  -23.282  1.00 17.83  ? 100 TRP B CD1 1 
ATOM   2411 C  CD2 . TRP B 2 100 ? -1.358  19.287  -25.470  1.00 21.52  ? 100 TRP B CD2 1 
ATOM   2412 N  NE1 . TRP B 2 100 ? -2.862  18.641  -23.942  1.00 20.59  ? 100 TRP B NE1 1 
ATOM   2413 C  CE2 . TRP B 2 100 ? -2.602  18.658  -25.288  1.00 22.97  ? 100 TRP B CE2 1 
ATOM   2414 C  CE3 . TRP B 2 100 ? -0.863  19.444  -26.766  1.00 19.91  ? 100 TRP B CE3 1 
ATOM   2415 C  CZ2 . TRP B 2 100 ? -3.363  18.180  -26.358  1.00 28.28  ? 100 TRP B CZ2 1 
ATOM   2416 C  CZ3 . TRP B 2 100 ? -1.613  18.959  -27.832  1.00 21.69  ? 100 TRP B CZ3 1 
ATOM   2417 C  CH2 . TRP B 2 100 ? -2.851  18.340  -27.621  1.00 29.59  ? 100 TRP B CH2 1 
ATOM   2418 N  N   . LYS B 2 101 ? 3.359   19.799  -22.693  1.00 19.62  ? 101 LYS B N   1 
ATOM   2419 C  CA  . LYS B 2 101 ? 4.770   20.138  -22.827  1.00 33.93  ? 101 LYS B CA  1 
ATOM   2420 C  C   . LYS B 2 101 ? 5.399   19.070  -23.707  1.00 30.54  ? 101 LYS B C   1 
ATOM   2421 O  O   . LYS B 2 101 ? 4.817   18.008  -23.931  1.00 26.96  ? 101 LYS B O   1 
ATOM   2422 C  CB  . LYS B 2 101 ? 5.479   20.217  -21.466  1.00 19.65  ? 101 LYS B CB  1 
ATOM   2423 C  CG  . LYS B 2 101 ? 5.406   18.917  -20.679  1.00 29.30  ? 101 LYS B CG  1 
ATOM   2424 C  CD  . LYS B 2 101 ? 6.460   18.842  -19.584  1.00 28.12  ? 101 LYS B CD  1 
ATOM   2425 C  CE  . LYS B 2 101 ? 7.858   18.822  -20.127  1.00 31.70  ? 101 LYS B CE  1 
ATOM   2426 N  NZ  . LYS B 2 101 ? 8.810   18.239  -19.154  1.00 42.40  ? 101 LYS B NZ  1 
ATOM   2427 N  N   . VAL B 2 102 ? 6.605   19.349  -24.193  1.00 28.31  ? 102 VAL B N   1 
ATOM   2428 C  CA  . VAL B 2 102 ? 7.293   18.436  -25.091  1.00 34.09  ? 102 VAL B CA  1 
ATOM   2429 C  C   . VAL B 2 102 ? 8.499   17.856  -24.370  1.00 40.90  ? 102 VAL B C   1 
ATOM   2430 O  O   . VAL B 2 102 ? 9.285   18.596  -23.766  1.00 39.00  ? 102 VAL B O   1 
ATOM   2431 C  CB  . VAL B 2 102 ? 7.690   19.130  -26.404  1.00 30.09  ? 102 VAL B CB  1 
ATOM   2432 C  CG1 . VAL B 2 102 ? 8.587   18.227  -27.226  1.00 21.58  ? 102 VAL B CG1 1 
ATOM   2433 C  CG2 . VAL B 2 102 ? 6.430   19.515  -27.196  1.00 25.22  ? 102 VAL B CG2 1 
ATOM   2434 N  N   . GLY B 2 103 ? 8.626   16.526  -24.425  1.00 36.29  ? 103 GLY B N   1 
ATOM   2435 C  CA  . GLY B 2 103 ? 9.796   15.820  -23.931  1.00 49.71  ? 103 GLY B CA  1 
ATOM   2436 C  C   . GLY B 2 103 ? 10.685  15.292  -25.045  1.00 46.34  ? 103 GLY B C   1 
ATOM   2437 O  O   . GLY B 2 103 ? 11.880  15.061  -24.849  1.00 54.53  ? 103 GLY B O   1 
ATOM   2438 N  N   . ARG B 2 110 ? 15.310  13.018  -33.270  1.00 41.52  ? 110 ARG B N   1 
ATOM   2439 C  CA  . ARG B 2 110 ? 14.439  14.069  -33.780  1.00 42.28  ? 110 ARG B CA  1 
ATOM   2440 C  C   . ARG B 2 110 ? 13.022  13.905  -33.235  1.00 50.34  ? 110 ARG B C   1 
ATOM   2441 O  O   . ARG B 2 110 ? 12.365  14.906  -32.930  1.00 56.26  ? 110 ARG B O   1 
ATOM   2442 C  CB  . ARG B 2 110 ? 14.439  14.082  -35.318  1.00 29.74  ? 110 ARG B CB  1 
ATOM   2443 C  CG  . ARG B 2 110 ? 15.310  15.171  -35.866  1.00 45.91  ? 110 ARG B CG  1 
ATOM   2444 C  CD  . ARG B 2 110 ? 14.916  15.644  -37.248  1.00 50.82  ? 110 ARG B CD  1 
ATOM   2445 N  NE  . ARG B 2 110 ? 16.108  15.725  -38.091  1.00 59.46  ? 110 ARG B NE  1 
ATOM   2446 C  CZ  . ARG B 2 110 ? 16.427  14.884  -39.070  1.00 52.10  ? 110 ARG B CZ  1 
ATOM   2447 N  NH1 . ARG B 2 110 ? 15.562  13.987  -39.529  1.00 43.48  ? 110 ARG B NH1 1 
ATOM   2448 N  NH2 . ARG B 2 110 ? 17.644  14.954  -39.610  1.00 44.39  ? 110 ARG B NH2 1 
ATOM   2449 N  N   . THR B 2 111 ? 12.541  12.664  -33.094  1.00 36.16  ? 111 THR B N   1 
ATOM   2450 C  CA  . THR B 2 111 ? 11.179  12.466  -32.598  1.00 45.26  ? 111 THR B CA  1 
ATOM   2451 C  C   . THR B 2 111 ? 11.108  12.802  -31.111  1.00 43.79  ? 111 THR B C   1 
ATOM   2452 O  O   . THR B 2 111 ? 11.815  12.200  -30.298  1.00 46.12  ? 111 THR B O   1 
ATOM   2453 C  CB  . THR B 2 111 ? 10.702  11.033  -32.823  1.00 36.84  ? 111 THR B CB  1 
ATOM   2454 O  OG1 . THR B 2 111 ? 10.479  10.804  -34.222  1.00 46.27  ? 111 THR B OG1 1 
ATOM   2455 C  CG2 . THR B 2 111 ? 9.390   10.833  -32.101  1.00 28.93  ? 111 THR B CG2 1 
ATOM   2456 N  N   . MET B 2 112 ? 10.261  13.762  -30.753  1.00 36.97  ? 112 MET B N   1 
ATOM   2457 C  CA  . MET B 2 112 ? 10.024  14.121  -29.358  1.00 35.35  ? 112 MET B CA  1 
ATOM   2458 C  C   . MET B 2 112 ? 8.551   13.932  -29.035  1.00 32.36  ? 112 MET B C   1 
ATOM   2459 O  O   . MET B 2 112 ? 7.687   14.516  -29.694  1.00 23.65  ? 112 MET B O   1 
ATOM   2460 C  CB  . MET B 2 112 ? 10.447  15.553  -29.065  1.00 28.01  ? 112 MET B CB  1 
ATOM   2461 C  CG  . MET B 2 112 ? 11.802  15.895  -29.628  1.00 48.99  ? 112 MET B CG  1 
ATOM   2462 S  SD  . MET B 2 112 ? 12.772  16.831  -28.441  1.00 53.53  ? 112 MET B SD  1 
ATOM   2463 C  CE  . MET B 2 112 ? 12.365  18.509  -28.942  1.00 44.34  ? 112 MET B CE  1 
ATOM   2464 N  N   . LEU B 2 113 ? 8.282   13.102  -28.035  1.00 26.09  ? 113 LEU B N   1 
ATOM   2465 C  CA  . LEU B 2 113 ? 6.923   12.801  -27.632  1.00 28.27  ? 113 LEU B CA  1 
ATOM   2466 C  C   . LEU B 2 113 ? 6.284   13.995  -26.937  1.00 28.61  ? 113 LEU B C   1 
ATOM   2467 O  O   . LEU B 2 113 ? 6.912   14.667  -26.114  1.00 30.34  ? 113 LEU B O   1 
ATOM   2468 C  CB  . LEU B 2 113 ? 6.933   11.603  -26.692  1.00 28.36  ? 113 LEU B CB  1 
ATOM   2469 C  CG  . LEU B 2 113 ? 7.538   10.340  -27.288  1.00 22.52  ? 113 LEU B CG  1 
ATOM   2470 C  CD1 . LEU B 2 113 ? 7.225   9.185   -26.366  1.00 22.70  ? 113 LEU B CD1 1 
ATOM   2471 C  CD2 . LEU B 2 113 ? 6.978   10.072  -28.680  1.00 22.48  ? 113 LEU B CD2 1 
ATOM   2472 N  N   . LEU B 2 114 ? 5.019   14.254  -27.266  1.00 34.14  ? 114 LEU B N   1 
ATOM   2473 C  CA  . LEU B 2 114 ? 4.223   15.199  -26.497  1.00 24.10  ? 114 LEU B CA  1 
ATOM   2474 C  C   . LEU B 2 114 ? 3.811   14.549  -25.188  1.00 22.78  ? 114 LEU B C   1 
ATOM   2475 O  O   . LEU B 2 114 ? 3.335   13.408  -25.181  1.00 20.37  ? 114 LEU B O   1 
ATOM   2476 C  CB  . LEU B 2 114 ? 2.987   15.610  -27.274  1.00 17.88  ? 114 LEU B CB  1 
ATOM   2477 C  CG  . LEU B 2 114 ? 3.031   16.968  -27.951  1.00 22.78  ? 114 LEU B CG  1 
ATOM   2478 C  CD1 . LEU B 2 114 ? 4.049   16.927  -29.060  1.00 22.74  ? 114 LEU B CD1 1 
ATOM   2479 C  CD2 . LEU B 2 114 ? 1.662   17.246  -28.504  1.00 16.27  ? 114 LEU B CD2 1 
ATOM   2480 N  N   . GLU B 2 115 ? 3.978   15.277  -24.085  1.00 24.94  ? 115 GLU B N   1 
ATOM   2481 C  CA  . GLU B 2 115 ? 3.536   14.810  -22.780  1.00 22.04  ? 115 GLU B CA  1 
ATOM   2482 C  C   . GLU B 2 115 ? 2.772   15.920  -22.072  1.00 18.94  ? 115 GLU B C   1 
ATOM   2483 O  O   . GLU B 2 115 ? 2.483   16.972  -22.638  1.00 17.30  ? 115 GLU B O   1 
ATOM   2484 C  CB  . GLU B 2 115 ? 4.731   14.317  -21.951  1.00 26.25  ? 115 GLU B CB  1 
ATOM   2485 C  CG  . GLU B 2 115 ? 5.951   15.204  -22.030  1.00 28.91  ? 115 GLU B CG  1 
ATOM   2486 C  CD  . GLU B 2 115 ? 7.224   14.505  -21.523  1.00 44.21  ? 115 GLU B CD  1 
ATOM   2487 O  OE1 . GLU B 2 115 ? 7.676   14.799  -20.392  1.00 55.57  ? 115 GLU B OE1 1 
ATOM   2488 O  OE2 . GLU B 2 115 ? 7.787   13.670  -22.265  1.00 52.70  ? 115 GLU B OE2 1 
ATOM   2489 N  N   . THR B 2 116 ? 2.388   15.653  -20.835  1.00 26.07  ? 116 THR B N   1 
ATOM   2490 C  CA  . THR B 2 116 ? 1.924   16.682  -19.923  1.00 24.29  ? 116 THR B CA  1 
ATOM   2491 C  C   . THR B 2 116 ? 2.958   16.835  -18.813  1.00 27.15  ? 116 THR B C   1 
ATOM   2492 O  O   . THR B 2 116 ? 3.986   16.154  -18.794  1.00 29.36  ? 116 THR B O   1 
ATOM   2493 C  CB  . THR B 2 116 ? 0.535   16.359  -19.350  1.00 18.35  ? 116 THR B CB  1 
ATOM   2494 O  OG1 . THR B 2 116 ? 0.584   15.161  -18.562  1.00 22.52  ? 116 THR B OG1 1 
ATOM   2495 C  CG2 . THR B 2 116 ? -0.489  16.195  -20.453  1.00 18.36  ? 116 THR B CG2 1 
ATOM   2496 N  N   . GLY B 2 117 ? 2.661   17.723  -17.869  1.00 26.60  ? 117 GLY B N   1 
ATOM   2497 C  CA  . GLY B 2 117 ? 3.606   18.136  -16.860  1.00 21.96  ? 117 GLY B CA  1 
ATOM   2498 C  C   . GLY B 2 117 ? 4.106   19.549  -17.033  1.00 25.08  ? 117 GLY B C   1 
ATOM   2499 O  O   . GLY B 2 117 ? 5.046   19.945  -16.339  1.00 30.88  ? 117 GLY B O   1 
ATOM   2500 N  N   . GLY B 2 118 ? 3.525   20.318  -17.944  1.00 29.34  ? 118 GLY B N   1 
ATOM   2501 C  CA  . GLY B 2 118 ? 4.014   21.645  -18.237  1.00 28.51  ? 118 GLY B CA  1 
ATOM   2502 C  C   . GLY B 2 118 ? 3.441   22.693  -17.301  1.00 21.17  ? 118 GLY B C   1 
ATOM   2503 O  O   . GLY B 2 118 ? 2.742   22.402  -16.329  1.00 27.00  ? 118 GLY B O   1 
ATOM   2504 N  N   . THR B 2 119 ? 3.746   23.946  -17.623  1.00 23.64  ? 119 THR B N   1 
ATOM   2505 C  CA  . THR B 2 119 ? 3.236   25.111  -16.916  1.00 27.91  ? 119 THR B CA  1 
ATOM   2506 C  C   . THR B 2 119 ? 2.554   26.040  -17.915  1.00 27.09  ? 119 THR B C   1 
ATOM   2507 O  O   . THR B 2 119 ? 2.688   25.893  -19.131  1.00 30.03  ? 119 THR B O   1 
ATOM   2508 C  CB  . THR B 2 119 ? 4.361   25.859  -16.178  1.00 29.89  ? 119 THR B CB  1 
ATOM   2509 O  OG1 . THR B 2 119 ? 5.140   26.589  -17.131  1.00 31.59  ? 119 THR B OG1 1 
ATOM   2510 C  CG2 . THR B 2 119 ? 5.278   24.903  -15.427  1.00 24.74  ? 119 THR B CG2 1 
ATOM   2511 N  N   . ILE B 2 120 ? 1.812   27.012  -17.401  1.00 23.41  ? 120 ILE B N   1 
ATOM   2512 C  CA  . ILE B 2 120 ? 1.036   27.907  -18.245  1.00 28.67  ? 120 ILE B CA  1 
ATOM   2513 C  C   . ILE B 2 120 ? 1.554   29.328  -18.101  1.00 32.72  ? 120 ILE B C   1 
ATOM   2514 O  O   . ILE B 2 120 ? 1.779   29.803  -16.981  1.00 37.04  ? 120 ILE B O   1 
ATOM   2515 C  CB  . ILE B 2 120 ? -0.461  27.852  -17.908  1.00 31.00  ? 120 ILE B CB  1 
ATOM   2516 C  CG1 . ILE B 2 120 ? -1.096  26.604  -18.507  1.00 23.04  ? 120 ILE B CG1 1 
ATOM   2517 C  CG2 . ILE B 2 120 ? -1.172  29.088  -18.439  1.00 23.35  ? 120 ILE B CG2 1 
ATOM   2518 C  CD1 . ILE B 2 120 ? -2.499  26.402  -18.002  1.00 25.16  ? 120 ILE B CD1 1 
ATOM   2519 N  N   . GLY B 2 121 ? 1.728   30.007  -19.236  1.00 36.84  ? 121 GLY B N   1 
ATOM   2520 C  CA  . GLY B 2 121 ? 1.946   31.440  -19.218  1.00 29.22  ? 121 GLY B CA  1 
ATOM   2521 C  C   . GLY B 2 121 ? 3.233   31.876  -18.578  1.00 32.73  ? 121 GLY B C   1 
ATOM   2522 O  O   . GLY B 2 121 ? 3.329   33.013  -18.118  1.00 30.46  ? 121 GLY B O   1 
ATOM   2523 N  N   . GLN B 2 122 ? 4.227   30.995  -18.528  1.00 32.17  ? 122 GLN B N   1 
ATOM   2524 C  CA  . GLN B 2 122 ? 5.518   31.279  -17.918  1.00 32.43  ? 122 GLN B CA  1 
ATOM   2525 C  C   . GLN B 2 122 ? 6.605   31.179  -18.970  1.00 34.51  ? 122 GLN B C   1 
ATOM   2526 O  O   . GLN B 2 122 ? 6.387   30.708  -20.097  1.00 32.74  ? 122 GLN B O   1 
ATOM   2527 C  CB  . GLN B 2 122 ? 5.850   30.303  -16.780  1.00 31.64  ? 122 GLN B CB  1 
ATOM   2528 C  CG  . GLN B 2 122 ? 5.211   30.613  -15.451  1.00 37.30  ? 122 GLN B CG  1 
ATOM   2529 C  CD  . GLN B 2 122 ? 5.234   29.406  -14.528  1.00 48.82  ? 122 GLN B CD  1 
ATOM   2530 O  OE1 . GLN B 2 122 ? 6.190   28.618  -14.535  1.00 43.83  ? 122 GLN B OE1 1 
ATOM   2531 N  NE2 . GLN B 2 122 ? 4.193   29.265  -13.713  1.00 51.47  ? 122 GLN B NE2 1 
ATOM   2532 N  N   . ALA B 2 123 ? 7.797   31.596  -18.562  1.00 26.94  ? 123 ALA B N   1 
ATOM   2533 C  CA  . ALA B 2 123 ? 8.947   31.505  -19.449  1.00 30.15  ? 123 ALA B CA  1 
ATOM   2534 C  C   . ALA B 2 123 ? 9.385   30.064  -19.654  1.00 26.82  ? 123 ALA B C   1 
ATOM   2535 O  O   . ALA B 2 123 ? 9.944   29.736  -20.707  1.00 32.90  ? 123 ALA B O   1 
ATOM   2536 C  CB  . ALA B 2 123 ? 10.089  32.356  -18.898  1.00 35.48  ? 123 ALA B CB  1 
ATOM   2537 N  N   . ASP B 2 124 ? 9.118   29.181  -18.690  1.00 34.49  ? 124 ASP B N   1 
ATOM   2538 C  CA  . ASP B 2 124 ? 9.519   27.787  -18.845  1.00 33.56  ? 124 ASP B CA  1 
ATOM   2539 C  C   . ASP B 2 124 ? 8.441   26.936  -19.527  1.00 34.92  ? 124 ASP B C   1 
ATOM   2540 O  O   . ASP B 2 124 ? 8.682   25.756  -19.803  1.00 33.00  ? 124 ASP B O   1 
ATOM   2541 C  CB  . ASP B 2 124 ? 9.932   27.190  -17.478  1.00 31.13  ? 124 ASP B CB  1 
ATOM   2542 C  CG  . ASP B 2 124 ? 8.743   26.694  -16.613  1.00 45.62  ? 124 ASP B CG  1 
ATOM   2543 O  OD1 . ASP B 2 124 ? 7.641   27.285  -16.622  1.00 41.49  ? 124 ASP B OD1 1 
ATOM   2544 O  OD2 . ASP B 2 124 ? 8.940   25.699  -15.874  1.00 48.97  ? 124 ASP B OD2 1 
ATOM   2545 N  N   . SER B 2 125 ? 7.290   27.522  -19.856  1.00 33.04  ? 125 SER B N   1 
ATOM   2546 C  CA  . SER B 2 125 ? 6.161   26.788  -20.416  1.00 32.09  ? 125 SER B CA  1 
ATOM   2547 C  C   . SER B 2 125 ? 6.403   26.399  -21.876  1.00 35.53  ? 125 SER B C   1 
ATOM   2548 O  O   . SER B 2 125 ? 7.184   27.032  -22.594  1.00 35.65  ? 125 SER B O   1 
ATOM   2549 C  CB  . SER B 2 125 ? 4.909   27.647  -20.339  1.00 28.91  ? 125 SER B CB  1 
ATOM   2550 O  OG  . SER B 2 125 ? 4.753   28.149  -19.028  1.00 36.71  ? 125 SER B OG  1 
ATOM   2551 N  N   . SER B 2 126 ? 5.688   25.366  -22.330  1.00 27.00  ? 126 SER B N   1 
ATOM   2552 C  CA  . SER B 2 126 ? 5.735   24.961  -23.736  1.00 26.52  ? 126 SER B CA  1 
ATOM   2553 C  C   . SER B 2 126 ? 4.620   25.657  -24.495  1.00 28.05  ? 126 SER B C   1 
ATOM   2554 O  O   . SER B 2 126 ? 3.440   25.465  -24.182  1.00 25.69  ? 126 SER B O   1 
ATOM   2555 C  CB  . SER B 2 126 ? 5.579   23.454  -23.887  1.00 24.49  ? 126 SER B CB  1 
ATOM   2556 O  OG  . SER B 2 126 ? 6.494   22.805  -23.055  1.00 26.76  ? 126 SER B OG  1 
ATOM   2557 N  N   . TYR B 2 127 ? 4.983   26.439  -25.499  1.00 26.32  ? 127 TYR B N   1 
ATOM   2558 C  CA  . TYR B 2 127 ? 3.999   27.184  -26.264  1.00 31.40  ? 127 TYR B CA  1 
ATOM   2559 C  C   . TYR B 2 127 ? 3.771   26.514  -27.611  1.00 34.93  ? 127 TYR B C   1 
ATOM   2560 O  O   . TYR B 2 127 ? 4.682   25.919  -28.192  1.00 33.38  ? 127 TYR B O   1 
ATOM   2561 C  CB  . TYR B 2 127 ? 4.435   28.636  -26.448  1.00 29.44  ? 127 TYR B CB  1 
ATOM   2562 C  CG  . TYR B 2 127 ? 4.416   29.349  -25.132  1.00 28.96  ? 127 TYR B CG  1 
ATOM   2563 C  CD1 . TYR B 2 127 ? 5.488   29.262  -24.271  1.00 28.76  ? 127 TYR B CD1 1 
ATOM   2564 C  CD2 . TYR B 2 127 ? 3.307   30.067  -24.730  1.00 33.23  ? 127 TYR B CD2 1 
ATOM   2565 C  CE1 . TYR B 2 127 ? 5.471   29.880  -23.057  1.00 33.38  ? 127 TYR B CE1 1 
ATOM   2566 C  CE2 . TYR B 2 127 ? 3.279   30.701  -23.517  1.00 31.57  ? 127 TYR B CE2 1 
ATOM   2567 C  CZ  . TYR B 2 127 ? 4.369   30.604  -22.685  1.00 32.72  ? 127 TYR B CZ  1 
ATOM   2568 O  OH  . TYR B 2 127 ? 4.364   31.215  -21.462  1.00 31.62  ? 127 TYR B OH  1 
ATOM   2569 N  N   . PHE B 2 128 ? 2.532   26.589  -28.083  1.00 34.54  ? 128 PHE B N   1 
ATOM   2570 C  CA  . PHE B 2 128 ? 2.154   26.022  -29.362  1.00 23.73  ? 128 PHE B CA  1 
ATOM   2571 C  C   . PHE B 2 128 ? 1.465   27.094  -30.190  1.00 33.16  ? 128 PHE B C   1 
ATOM   2572 O  O   . PHE B 2 128 ? 0.974   28.099  -29.660  1.00 33.69  ? 128 PHE B O   1 
ATOM   2573 C  CB  . PHE B 2 128 ? 1.220   24.820  -29.196  1.00 17.69  ? 128 PHE B CB  1 
ATOM   2574 C  CG  . PHE B 2 128 ? 1.829   23.669  -28.455  1.00 25.60  ? 128 PHE B CG  1 
ATOM   2575 C  CD1 . PHE B 2 128 ? 1.772   23.618  -27.060  1.00 17.70  ? 128 PHE B CD1 1 
ATOM   2576 C  CD2 . PHE B 2 128 ? 2.414   22.610  -29.149  1.00 17.92  ? 128 PHE B CD2 1 
ATOM   2577 C  CE1 . PHE B 2 128 ? 2.317   22.539  -26.365  1.00 25.25  ? 128 PHE B CE1 1 
ATOM   2578 C  CE2 . PHE B 2 128 ? 2.957   21.523  -28.468  1.00 18.57  ? 128 PHE B CE2 1 
ATOM   2579 C  CZ  . PHE B 2 128 ? 2.910   21.490  -27.059  1.00 27.70  ? 128 PHE B CZ  1 
ATOM   2580 N  N   . LYS B 2 129 ? 1.434   26.855  -31.501  1.00 26.32  ? 129 LYS B N   1 
ATOM   2581 C  CA  . LYS B 2 129 ? 0.715   27.676  -32.462  1.00 26.66  ? 129 LYS B CA  1 
ATOM   2582 C  C   . LYS B 2 129 ? -0.200  26.784  -33.287  1.00 31.88  ? 129 LYS B C   1 
ATOM   2583 O  O   . LYS B 2 129 ? 0.196   25.683  -33.690  1.00 29.05  ? 129 LYS B O   1 
ATOM   2584 C  CB  . LYS B 2 129 ? 1.675   28.403  -33.424  1.00 42.15  ? 129 LYS B CB  1 
ATOM   2585 C  CG  . LYS B 2 129 ? 2.673   29.349  -32.780  1.00 45.81  ? 129 LYS B CG  1 
ATOM   2586 C  CD  . LYS B 2 129 ? 3.502   30.077  -33.831  1.00 50.43  ? 129 LYS B CD  1 
ATOM   2587 C  CE  . LYS B 2 129 ? 4.494   31.046  -33.169  1.00 53.36  ? 129 LYS B CE  1 
ATOM   2588 N  NZ  . LYS B 2 129 ? 5.267   31.868  -34.142  1.00 48.02  ? 129 LYS B NZ  1 
ATOM   2589 N  N   . ILE B 2 130 ? -1.412  27.269  -33.550  1.00 32.95  ? 130 ILE B N   1 
ATOM   2590 C  CA  . ILE B 2 130 ? -2.354  26.630  -34.464  1.00 34.17  ? 130 ILE B CA  1 
ATOM   2591 C  C   . ILE B 2 130 ? -2.232  27.306  -35.822  1.00 39.19  ? 130 ILE B C   1 
ATOM   2592 O  O   . ILE B 2 130 ? -2.504  28.505  -35.951  1.00 34.78  ? 130 ILE B O   1 
ATOM   2593 C  CB  . ILE B 2 130 ? -3.794  26.735  -33.946  1.00 28.81  ? 130 ILE B CB  1 
ATOM   2594 C  CG1 . ILE B 2 130 ? -3.894  26.207  -32.527  1.00 22.77  ? 130 ILE B CG1 1 
ATOM   2595 C  CG2 . ILE B 2 130 ? -4.742  26.026  -34.872  1.00 22.20  ? 130 ILE B CG2 1 
ATOM   2596 C  CD1 . ILE B 2 130 ? -5.231  26.466  -31.914  1.00 25.09  ? 130 ILE B CD1 1 
ATOM   2597 N  N   . VAL B 2 131 ? -1.836  26.554  -36.842  1.00 30.45  ? 131 VAL B N   1 
ATOM   2598 C  CA  . VAL B 2 131 ? -1.700  27.130  -38.170  1.00 31.21  ? 131 VAL B CA  1 
ATOM   2599 C  C   . VAL B 2 131 ? -2.621  26.396  -39.126  1.00 37.66  ? 131 VAL B C   1 
ATOM   2600 O  O   . VAL B 2 131 ? -3.026  25.251  -38.893  1.00 30.33  ? 131 VAL B O   1 
ATOM   2601 C  CB  . VAL B 2 131 ? -0.253  27.093  -38.686  1.00 26.25  ? 131 VAL B CB  1 
ATOM   2602 C  CG1 . VAL B 2 131 ? 0.627   27.933  -37.788  1.00 32.32  ? 131 VAL B CG1 1 
ATOM   2603 C  CG2 . VAL B 2 131 ? 0.244   25.670  -38.778  1.00 26.23  ? 131 VAL B CG2 1 
ATOM   2604 N  N   . LYS B 2 132 ? -2.958  27.077  -40.217  1.00 39.42  ? 132 LYS B N   1 
ATOM   2605 C  CA  . LYS B 2 132 ? -3.823  26.461  -41.207  1.00 41.01  ? 132 LYS B CA  1 
ATOM   2606 C  C   . LYS B 2 132 ? -3.098  25.285  -41.842  1.00 41.32  ? 132 LYS B C   1 
ATOM   2607 O  O   . LYS B 2 132 ? -1.881  25.328  -42.051  1.00 42.98  ? 132 LYS B O   1 
ATOM   2608 C  CB  . LYS B 2 132 ? -4.247  27.477  -42.259  1.00 36.75  ? 132 LYS B CB  1 
ATOM   2609 C  CG  . LYS B 2 132 ? -5.325  26.942  -43.180  1.00 52.71  ? 132 LYS B CG  1 
ATOM   2610 C  CD  . LYS B 2 132 ? -6.655  26.770  -42.458  1.00 45.39  ? 132 LYS B CD  1 
ATOM   2611 C  CE  . LYS B 2 132 ? -7.575  25.776  -43.195  1.00 61.18  ? 132 LYS B CE  1 
ATOM   2612 N  NZ  . LYS B 2 132 ? -6.856  24.774  -44.074  1.00 44.74  ? 132 LYS B NZ  1 
ATOM   2613 N  N   . SER B 2 133 ? -3.842  24.210  -42.098  1.00 40.32  ? 133 SER B N   1 
ATOM   2614 C  CA  . SER B 2 133 ? -3.256  22.994  -42.650  1.00 36.42  ? 133 SER B CA  1 
ATOM   2615 C  C   . SER B 2 133 ? -3.120  23.097  -44.166  1.00 41.69  ? 133 SER B C   1 
ATOM   2616 O  O   . SER B 2 133 ? -3.868  23.826  -44.827  1.00 35.30  ? 133 SER B O   1 
ATOM   2617 C  CB  . SER B 2 133 ? -4.111  21.780  -42.282  1.00 35.47  ? 133 SER B CB  1 
ATOM   2618 O  OG  . SER B 2 133 ? -3.972  20.732  -43.222  1.00 42.44  ? 133 SER B OG  1 
ATOM   2619 N  N   . SER B 2 134 ? -2.141  22.356  -44.714  1.00 48.53  ? 134 SER B N   1 
ATOM   2620 C  CA  . SER B 2 134 ? -1.994  22.262  -46.170  1.00 38.67  ? 134 SER B CA  1 
ATOM   2621 C  C   . SER B 2 134 ? -3.228  21.658  -46.836  1.00 46.13  ? 134 SER B C   1 
ATOM   2622 O  O   . SER B 2 134 ? -3.489  21.939  -48.009  1.00 42.38  ? 134 SER B O   1 
ATOM   2623 C  CB  . SER B 2 134 ? -0.757  21.438  -46.547  1.00 45.93  ? 134 SER B CB  1 
ATOM   2624 O  OG  . SER B 2 134 ? 0.430   22.218  -46.488  1.00 59.07  ? 134 SER B OG  1 
ATOM   2625 N  N   . LYS B 2 135 ? -3.984  20.820  -46.123  1.00 39.48  ? 135 LYS B N   1 
ATOM   2626 C  CA  . LYS B 2 135 ? -5.227  20.289  -46.662  1.00 40.05  ? 135 LYS B CA  1 
ATOM   2627 C  C   . LYS B 2 135 ? -6.424  20.941  -45.969  1.00 45.53  ? 135 LYS B C   1 
ATOM   2628 O  O   . LYS B 2 135 ? -6.619  22.155  -46.100  1.00 40.67  ? 135 LYS B O   1 
ATOM   2629 C  CB  . LYS B 2 135 ? -5.238  18.761  -46.541  1.00 43.53  ? 135 LYS B CB  1 
ATOM   2630 C  CG  . LYS B 2 135 ? -3.960  18.094  -47.098  1.00 42.22  ? 135 LYS B CG  1 
ATOM   2631 C  CD  . LYS B 2 135 ? -3.617  16.778  -46.392  1.00 44.58  ? 135 LYS B CD  1 
ATOM   2632 C  CE  . LYS B 2 135 ? -4.314  15.577  -47.050  1.00 47.88  ? 135 LYS B CE  1 
ATOM   2633 N  NZ  . LYS B 2 135 ? -3.992  14.275  -46.374  1.00 44.07  ? 135 LYS B NZ  1 
ATOM   2634 N  N   . PHE B 2 136 ? -7.227  20.163  -45.235  1.00 49.37  ? 136 PHE B N   1 
ATOM   2635 C  CA  . PHE B 2 136 ? -8.355  20.668  -44.455  1.00 42.31  ? 136 PHE B CA  1 
ATOM   2636 C  C   . PHE B 2 136 ? -7.990  20.749  -42.973  1.00 39.07  ? 136 PHE B C   1 
ATOM   2637 O  O   . PHE B 2 136 ? -7.177  19.966  -42.471  1.00 41.30  ? 136 PHE B O   1 
ATOM   2638 C  CB  . PHE B 2 136 ? -9.593  19.777  -44.641  1.00 36.75  ? 136 PHE B CB  1 
ATOM   2639 C  CG  . PHE B 2 136 ? -10.907 20.462  -44.301  1.00 53.58  ? 136 PHE B CG  1 
ATOM   2640 C  CD1 . PHE B 2 136 ? -11.339 21.565  -45.019  1.00 56.65  ? 136 PHE B CD1 1 
ATOM   2641 C  CD2 . PHE B 2 136 ? -11.720 19.985  -43.275  1.00 50.83  ? 136 PHE B CD2 1 
ATOM   2642 C  CE1 . PHE B 2 136 ? -12.550 22.187  -44.716  1.00 58.69  ? 136 PHE B CE1 1 
ATOM   2643 C  CE2 . PHE B 2 136 ? -12.929 20.601  -42.966  1.00 40.02  ? 136 PHE B CE2 1 
ATOM   2644 C  CZ  . PHE B 2 136 ? -13.342 21.703  -43.688  1.00 57.87  ? 136 PHE B CZ  1 
ATOM   2645 N  N   . GLY B 2 137 ? -8.597  21.710  -42.273  1.00 38.06  ? 137 GLY B N   1 
ATOM   2646 C  CA  . GLY B 2 137 ? -8.347  21.868  -40.842  1.00 36.47  ? 137 GLY B CA  1 
ATOM   2647 C  C   . GLY B 2 137 ? -7.050  22.594  -40.483  1.00 41.47  ? 137 GLY B C   1 
ATOM   2648 O  O   . GLY B 2 137 ? -6.545  23.460  -41.214  1.00 34.42  ? 137 GLY B O   1 
ATOM   2649 N  N   . TYR B 2 138 ? -6.501  22.222  -39.326  1.00 32.51  ? 138 TYR B N   1 
ATOM   2650 C  CA  . TYR B 2 138 ? -5.335  22.881  -38.758  1.00 31.56  ? 138 TYR B CA  1 
ATOM   2651 C  C   . TYR B 2 138 ? -4.261  21.867  -38.383  1.00 32.09  ? 138 TYR B C   1 
ATOM   2652 O  O   . TYR B 2 138 ? -4.528  20.677  -38.176  1.00 28.68  ? 138 TYR B O   1 
ATOM   2653 C  CB  . TYR B 2 138 ? -5.690  23.688  -37.502  1.00 26.95  ? 138 TYR B CB  1 
ATOM   2654 C  CG  . TYR B 2 138 ? -6.838  24.666  -37.658  1.00 34.84  ? 138 TYR B CG  1 
ATOM   2655 C  CD1 . TYR B 2 138 ? -8.149  24.285  -37.374  1.00 35.87  ? 138 TYR B CD1 1 
ATOM   2656 C  CD2 . TYR B 2 138 ? -6.609  25.974  -38.053  1.00 32.69  ? 138 TYR B CD2 1 
ATOM   2657 C  CE1 . TYR B 2 138 ? -9.194  25.173  -37.506  1.00 33.46  ? 138 TYR B CE1 1 
ATOM   2658 C  CE2 . TYR B 2 138 ? -7.644  26.870  -38.177  1.00 34.89  ? 138 TYR B CE2 1 
ATOM   2659 C  CZ  . TYR B 2 138 ? -8.933  26.473  -37.912  1.00 36.97  ? 138 TYR B CZ  1 
ATOM   2660 O  OH  . TYR B 2 138 ? -9.960  27.392  -38.039  1.00 35.19  ? 138 TYR B OH  1 
ATOM   2661 N  N   . ASN B 2 139 ? -3.035  22.370  -38.292  1.00 30.99  ? 139 ASN B N   1 
ATOM   2662 C  CA  . ASN B 2 139 ? -1.940  21.686  -37.629  1.00 33.27  ? 139 ASN B CA  1 
ATOM   2663 C  C   . ASN B 2 139 ? -1.582  22.421  -36.350  1.00 29.70  ? 139 ASN B C   1 
ATOM   2664 O  O   . ASN B 2 139 ? -1.826  23.623  -36.211  1.00 35.28  ? 139 ASN B O   1 
ATOM   2665 C  CB  . ASN B 2 139 ? -0.709  21.598  -38.531  1.00 26.83  ? 139 ASN B CB  1 
ATOM   2666 C  CG  . ASN B 2 139 ? -1.003  20.868  -39.812  1.00 35.51  ? 139 ASN B CG  1 
ATOM   2667 O  OD1 . ASN B 2 139 ? -0.652  21.324  -40.898  1.00 38.05  ? 139 ASN B OD1 1 
ATOM   2668 N  ND2 . ASN B 2 139 ? -1.653  19.711  -39.692  1.00 37.99  ? 139 ASN B ND2 1 
ATOM   2669 N  N   . LEU B 2 140 ? -1.008  21.689  -35.413  1.00 29.16  ? 140 LEU B N   1 
ATOM   2670 C  CA  . LEU B 2 140 ? -0.412  22.293  -34.241  1.00 26.07  ? 140 LEU B CA  1 
ATOM   2671 C  C   . LEU B 2 140 ? 1.088   22.358  -34.456  1.00 28.23  ? 140 LEU B C   1 
ATOM   2672 O  O   . LEU B 2 140 ? 1.690   21.437  -35.014  1.00 23.18  ? 140 LEU B O   1 
ATOM   2673 C  CB  . LEU B 2 140 ? -0.722  21.498  -32.972  1.00 28.31  ? 140 LEU B CB  1 
ATOM   2674 C  CG  . LEU B 2 140 ? -2.199  21.232  -32.710  1.00 32.24  ? 140 LEU B CG  1 
ATOM   2675 C  CD1 . LEU B 2 140 ? -2.359  20.304  -31.520  1.00 33.83  ? 140 LEU B CD1 1 
ATOM   2676 C  CD2 . LEU B 2 140 ? -2.961  22.528  -32.509  1.00 30.12  ? 140 LEU B CD2 1 
ATOM   2677 N  N   . LEU B 2 141 ? 1.679   23.457  -34.014  1.00 39.22  ? 141 LEU B N   1 
ATOM   2678 C  CA  . LEU B 2 141 ? 3.110   23.687  -34.076  1.00 34.81  ? 141 LEU B CA  1 
ATOM   2679 C  C   . LEU B 2 141 ? 3.610   23.827  -32.655  1.00 30.46  ? 141 LEU B C   1 
ATOM   2680 O  O   . LEU B 2 141 ? 2.982   24.504  -31.842  1.00 30.85  ? 141 LEU B O   1 
ATOM   2681 C  CB  . LEU B 2 141 ? 3.431   24.969  -34.845  1.00 34.33  ? 141 LEU B CB  1 
ATOM   2682 C  CG  . LEU B 2 141 ? 3.239   24.928  -36.352  1.00 39.69  ? 141 LEU B CG  1 
ATOM   2683 C  CD1 . LEU B 2 141 ? 4.155   25.961  -37.000  1.00 30.54  ? 141 LEU B CD1 1 
ATOM   2684 C  CD2 . LEU B 2 141 ? 3.479   23.507  -36.897  1.00 32.33  ? 141 LEU B CD2 1 
ATOM   2685 N  N   . TYR B 2 142 ? 4.733   23.200  -32.359  1.00 30.07  ? 142 TYR B N   1 
ATOM   2686 C  CA  . TYR B 2 142 ? 5.434   23.431  -31.110  1.00 28.10  ? 142 TYR B CA  1 
ATOM   2687 C  C   . TYR B 2 142 ? 6.507   24.470  -31.372  1.00 37.39  ? 142 TYR B C   1 
ATOM   2688 O  O   . TYR B 2 142 ? 7.267   24.347  -32.338  1.00 33.38  ? 142 TYR B O   1 
ATOM   2689 C  CB  . TYR B 2 142 ? 6.058   22.144  -30.575  1.00 29.65  ? 142 TYR B CB  1 
ATOM   2690 C  CG  . TYR B 2 142 ? 7.115   22.381  -29.516  1.00 34.16  ? 142 TYR B CG  1 
ATOM   2691 C  CD1 . TYR B 2 142 ? 6.832   23.108  -28.375  1.00 34.71  ? 142 TYR B CD1 1 
ATOM   2692 C  CD2 . TYR B 2 142 ? 8.394   21.863  -29.658  1.00 42.81  ? 142 TYR B CD2 1 
ATOM   2693 C  CE1 . TYR B 2 142 ? 7.792   23.319  -27.408  1.00 38.86  ? 142 TYR B CE1 1 
ATOM   2694 C  CE2 . TYR B 2 142 ? 9.356   22.069  -28.703  1.00 37.85  ? 142 TYR B CE2 1 
ATOM   2695 C  CZ  . TYR B 2 142 ? 9.052   22.798  -27.579  1.00 46.19  ? 142 TYR B CZ  1 
ATOM   2696 O  OH  . TYR B 2 142 ? 10.018  23.000  -26.623  1.00 55.91  ? 142 TYR B OH  1 
ATOM   2697 N  N   . CYS B 2 143 ? 6.563   25.500  -30.526  1.00 41.56  ? 143 CYS B N   1 
ATOM   2698 C  CA  . CYS B 2 143 ? 7.460   26.634  -30.745  1.00 44.63  ? 143 CYS B CA  1 
ATOM   2699 C  C   . CYS B 2 143 ? 8.378   26.825  -29.551  1.00 39.65  ? 143 CYS B C   1 
ATOM   2700 O  O   . CYS B 2 143 ? 8.023   27.518  -28.586  1.00 48.70  ? 143 CYS B O   1 
ATOM   2701 C  CB  . CYS B 2 143 ? 6.664   27.901  -31.035  1.00 37.15  ? 143 CYS B CB  1 
ATOM   2702 S  SG  . CYS B 2 143 ? 5.806   27.753  -32.599  1.00 68.57  ? 143 CYS B SG  1 
ATOM   2703 N  N   . PRO B 2 144 ? 9.562   26.224  -29.570  1.00 51.45  ? 144 PRO B N   1 
ATOM   2704 C  CA  . PRO B 2 144 ? 10.548  26.506  -28.519  1.00 55.08  ? 144 PRO B CA  1 
ATOM   2705 C  C   . PRO B 2 144 ? 10.953  27.970  -28.576  1.00 52.17  ? 144 PRO B C   1 
ATOM   2706 O  O   . PRO B 2 144 ? 11.672  28.387  -29.487  1.00 59.57  ? 144 PRO B O   1 
ATOM   2707 C  CB  . PRO B 2 144 ? 11.710  25.561  -28.860  1.00 50.42  ? 144 PRO B CB  1 
ATOM   2708 C  CG  . PRO B 2 144 ? 11.546  25.280  -30.332  1.00 45.57  ? 144 PRO B CG  1 
ATOM   2709 C  CD  . PRO B 2 144 ? 10.063  25.254  -30.561  1.00 47.74  ? 144 PRO B CD  1 
ATOM   2710 N  N   . LEU B 2 145 ? 10.472  28.764  -27.626  1.00 62.77  ? 145 LEU B N   1 
ATOM   2711 C  CA  . LEU B 2 145 ? 10.645  30.208  -27.671  1.00 58.08  ? 145 LEU B CA  1 
ATOM   2712 C  C   . LEU B 2 145 ? 11.994  30.627  -27.080  1.00 69.45  ? 145 LEU B C   1 
ATOM   2713 O  O   . LEU B 2 145 ? 12.964  30.850  -27.806  1.00 67.46  ? 145 LEU B O   1 
ATOM   2714 C  CB  . LEU B 2 145 ? 9.496   30.898  -26.932  1.00 48.19  ? 145 LEU B CB  1 
ATOM   2715 C  CG  . LEU B 2 145 ? 9.984   31.855  -25.850  1.00 65.19  ? 145 LEU B CG  1 
ATOM   2716 C  CD1 . LEU B 2 145 ? 9.218   33.162  -25.918  1.00 64.29  ? 145 LEU B CD1 1 
ATOM   2717 C  CD2 . LEU B 2 145 ? 9.882   31.217  -24.458  1.00 62.93  ? 145 LEU B CD2 1 
ATOM   2718 N  N   . ASN B 2 158 ? 8.812   29.367  -37.980  1.00 41.46  ? 158 ASN B N   1 
ATOM   2719 C  CA  . ASN B 2 158 ? 9.738   28.695  -38.899  1.00 38.08  ? 158 ASN B CA  1 
ATOM   2720 C  C   . ASN B 2 158 ? 10.654  27.753  -38.144  1.00 51.27  ? 158 ASN B C   1 
ATOM   2721 O  O   . ASN B 2 158 ? 10.994  26.679  -38.636  1.00 61.49  ? 158 ASN B O   1 
ATOM   2722 C  CB  . ASN B 2 158 ? 10.583  29.705  -39.683  1.00 38.69  ? 158 ASN B CB  1 
ATOM   2723 C  CG  . ASN B 2 158 ? 11.220  29.104  -40.959  1.00 46.16  ? 158 ASN B CG  1 
ATOM   2724 O  OD1 . ASN B 2 158 ? 12.352  28.617  -40.929  1.00 48.21  ? 158 ASN B OD1 1 
ATOM   2725 N  ND2 . ASN B 2 158 ? 10.502  29.179  -42.086  1.00 39.66  ? 158 ASN B ND2 1 
ATOM   2726 N  N   . PHE B 2 159 ? 11.079  28.158  -36.951  1.00 50.52  ? 159 PHE B N   1 
ATOM   2727 C  CA  . PHE B 2 159 ? 11.852  27.277  -36.087  1.00 42.51  ? 159 PHE B CA  1 
ATOM   2728 C  C   . PHE B 2 159 ? 10.951  26.476  -35.152  1.00 43.06  ? 159 PHE B C   1 
ATOM   2729 O  O   . PHE B 2 159 ? 11.439  25.850  -34.208  1.00 41.52  ? 159 PHE B O   1 
ATOM   2730 C  CB  . PHE B 2 159 ? 12.882  28.102  -35.322  1.00 44.13  ? 159 PHE B CB  1 
ATOM   2731 C  CG  . PHE B 2 159 ? 13.989  28.636  -36.203  1.00 49.66  ? 159 PHE B CG  1 
ATOM   2732 C  CD1 . PHE B 2 159 ? 15.112  27.872  -36.481  1.00 43.30  ? 159 PHE B CD1 1 
ATOM   2733 C  CD2 . PHE B 2 159 ? 13.867  29.873  -36.814  1.00 39.95  ? 159 PHE B CD2 1 
ATOM   2734 C  CE1 . PHE B 2 159 ? 16.108  28.355  -37.303  1.00 38.09  ? 159 PHE B CE1 1 
ATOM   2735 C  CE2 . PHE B 2 159 ? 14.863  30.357  -37.634  1.00 37.47  ? 159 PHE B CE2 1 
ATOM   2736 C  CZ  . PHE B 2 159 ? 15.983  29.605  -37.875  1.00 36.45  ? 159 PHE B CZ  1 
ATOM   2737 N  N   . CYS B 2 160 ? 9.650   26.490  -35.421  1.00 37.20  ? 160 CYS B N   1 
ATOM   2738 C  CA  . CYS B 2 160 ? 8.648   25.657  -34.793  1.00 37.11  ? 160 CYS B CA  1 
ATOM   2739 C  C   . CYS B 2 160 ? 8.646   24.283  -35.447  1.00 35.83  ? 160 CYS B C   1 
ATOM   2740 O  O   . CYS B 2 160 ? 9.385   24.020  -36.395  1.00 47.86  ? 160 CYS B O   1 
ATOM   2741 C  CB  . CYS B 2 160 ? 7.286   26.326  -34.901  1.00 38.78  ? 160 CYS B CB  1 
ATOM   2742 S  SG  . CYS B 2 160 ? 7.258   27.919  -34.054  1.00 52.64  ? 160 CYS B SG  1 
ATOM   2743 N  N   . ALA B 2 161 ? 7.817   23.385  -34.937  1.00 36.31  ? 161 ALA B N   1 
ATOM   2744 C  CA  . ALA B 2 161 ? 7.928   21.983  -35.316  1.00 39.41  ? 161 ALA B CA  1 
ATOM   2745 C  C   . ALA B 2 161 ? 6.547   21.349  -35.373  1.00 37.88  ? 161 ALA B C   1 
ATOM   2746 O  O   . ALA B 2 161 ? 5.761   21.478  -34.430  1.00 40.52  ? 161 ALA B O   1 
ATOM   2747 C  CB  . ALA B 2 161 ? 8.825   21.229  -34.336  1.00 28.60  ? 161 ALA B CB  1 
ATOM   2748 N  N   . LYS B 2 162 ? 6.267   20.657  -36.474  1.00 38.70  ? 162 LYS B N   1 
ATOM   2749 C  CA  . LYS B 2 162 ? 4.937   20.126  -36.723  1.00 32.96  ? 162 LYS B CA  1 
ATOM   2750 C  C   . LYS B 2 162 ? 4.625   18.996  -35.755  1.00 40.76  ? 162 LYS B C   1 
ATOM   2751 O  O   . LYS B 2 162 ? 5.484   18.154  -35.446  1.00 29.56  ? 162 LYS B O   1 
ATOM   2752 C  CB  . LYS B 2 162 ? 4.826   19.643  -38.166  1.00 42.16  ? 162 LYS B CB  1 
ATOM   2753 C  CG  . LYS B 2 162 ? 4.991   20.757  -39.196  1.00 48.83  ? 162 LYS B CG  1 
ATOM   2754 C  CD  . LYS B 2 162 ? 4.153   20.525  -40.441  1.00 56.93  ? 162 LYS B CD  1 
ATOM   2755 C  CE  . LYS B 2 162 ? 3.433   21.802  -40.890  1.00 61.51  ? 162 LYS B CE  1 
ATOM   2756 N  NZ  . LYS B 2 162 ? 3.565   22.045  -42.357  1.00 62.44  ? 162 LYS B NZ  1 
ATOM   2757 N  N   . VAL B 2 163 ? 3.393   19.005  -35.251  1.00 33.13  ? 163 VAL B N   1 
ATOM   2758 C  CA  . VAL B 2 163 ? 2.915   17.980  -34.333  1.00 26.04  ? 163 VAL B CA  1 
ATOM   2759 C  C   . VAL B 2 163 ? 2.258   16.882  -35.153  1.00 28.35  ? 163 VAL B C   1 
ATOM   2760 O  O   . VAL B 2 163 ? 1.288   17.142  -35.874  1.00 23.41  ? 163 VAL B O   1 
ATOM   2761 C  CB  . VAL B 2 163 ? 1.924   18.564  -33.312  1.00 27.11  ? 163 VAL B CB  1 
ATOM   2762 C  CG1 . VAL B 2 163 ? 1.183   17.445  -32.597  1.00 21.57  ? 163 VAL B CG1 1 
ATOM   2763 C  CG2 . VAL B 2 163 ? 2.638   19.491  -32.308  1.00 28.90  ? 163 VAL B CG2 1 
ATOM   2764 N  N   . GLY B 2 164 ? 2.764   15.654  -35.025  1.00 25.03  ? 164 GLY B N   1 
ATOM   2765 C  CA  . GLY B 2 164 ? 2.130   14.503  -35.639  1.00 20.28  ? 164 GLY B CA  1 
ATOM   2766 C  C   . GLY B 2 164 ? 2.063   13.280  -34.740  1.00 23.81  ? 164 GLY B C   1 
ATOM   2767 O  O   . GLY B 2 164 ? 1.965   13.420  -33.518  1.00 21.79  ? 164 GLY B O   1 
ATOM   2768 N  N   . VAL B 2 165 ? 2.137   12.072  -35.307  1.00 21.13  ? 165 VAL B N   1 
ATOM   2769 C  CA  . VAL B 2 165 ? 1.835   10.851  -34.566  1.00 24.98  ? 165 VAL B CA  1 
ATOM   2770 C  C   . VAL B 2 165 ? 2.930   9.817   -34.793  1.00 28.11  ? 165 VAL B C   1 
ATOM   2771 O  O   . VAL B 2 165 ? 3.354   9.598   -35.932  1.00 35.34  ? 165 VAL B O   1 
ATOM   2772 C  CB  . VAL B 2 165 ? 0.467   10.269  -34.975  1.00 20.50  ? 165 VAL B CB  1 
ATOM   2773 C  CG1 . VAL B 2 165 ? 0.238   8.931   -34.284  1.00 22.53  ? 165 VAL B CG1 1 
ATOM   2774 C  CG2 . VAL B 2 165 ? -0.658  11.250  -34.627  1.00 26.91  ? 165 VAL B CG2 1 
ATOM   2775 N  N   . VAL B 2 166 ? 3.372   9.163   -33.715  1.00 18.13  ? 166 VAL B N   1 
ATOM   2776 C  CA  . VAL B 2 166 ? 4.170   7.950   -33.831  1.00 17.69  ? 166 VAL B CA  1 
ATOM   2777 C  C   . VAL B 2 166 ? 3.425   6.841   -33.110  1.00 20.58  ? 166 VAL B C   1 
ATOM   2778 O  O   . VAL B 2 166 ? 2.519   7.084   -32.309  1.00 22.22  ? 166 VAL B O   1 
ATOM   2779 C  CB  . VAL B 2 166 ? 5.601   8.095   -33.263  1.00 18.47  ? 166 VAL B CB  1 
ATOM   2780 C  CG1 . VAL B 2 166 ? 6.287   9.292   -33.861  1.00 16.94  ? 166 VAL B CG1 1 
ATOM   2781 C  CG2 . VAL B 2 166 ? 5.560   8.237   -31.761  1.00 19.80  ? 166 VAL B CG2 1 
ATOM   2782 N  N   . ILE B 2 167 ? 3.814   5.611   -33.396  1.00 16.13  ? 167 ILE B N   1 
ATOM   2783 C  CA  . ILE B 2 167 ? 3.194   4.454   -32.768  1.00 18.63  ? 167 ILE B CA  1 
ATOM   2784 C  C   . ILE B 2 167 ? 4.118   3.971   -31.667  1.00 24.46  ? 167 ILE B C   1 
ATOM   2785 O  O   . ILE B 2 167 ? 5.293   3.661   -31.911  1.00 26.88  ? 167 ILE B O   1 
ATOM   2786 C  CB  . ILE B 2 167 ? 2.911   3.327   -33.768  1.00 18.72  ? 167 ILE B CB  1 
ATOM   2787 C  CG1 . ILE B 2 167 ? 2.027   3.805   -34.933  1.00 19.65  ? 167 ILE B CG1 1 
ATOM   2788 C  CG2 . ILE B 2 167 ? 2.236   2.170   -33.023  1.00 16.88  ? 167 ILE B CG2 1 
ATOM   2789 C  CD1 . ILE B 2 167 ? 0.893   4.737   -34.557  1.00 30.34  ? 167 ILE B CD1 1 
ATOM   2790 N  N   . GLN B 2 168 ? 3.591   3.879   -30.459  1.00 19.70  ? 168 GLN B N   1 
ATOM   2791 C  CA  . GLN B 2 168 ? 4.414   3.555   -29.314  1.00 18.87  ? 168 GLN B CA  1 
ATOM   2792 C  C   . GLN B 2 168 ? 3.670   2.503   -28.517  1.00 19.64  ? 168 GLN B C   1 
ATOM   2793 O  O   . GLN B 2 168 ? 2.569   2.767   -28.029  1.00 28.64  ? 168 GLN B O   1 
ATOM   2794 C  CB  . GLN B 2 168 ? 4.701   4.815   -28.498  1.00 18.98  ? 168 GLN B CB  1 
ATOM   2795 C  CG  . GLN B 2 168 ? 5.420   4.548   -27.208  1.00 28.07  ? 168 GLN B CG  1 
ATOM   2796 C  CD  . GLN B 2 168 ? 5.355   5.715   -26.252  1.00 29.02  ? 168 GLN B CD  1 
ATOM   2797 O  OE1 . GLN B 2 168 ? 4.280   6.270   -25.981  1.00 27.02  ? 168 GLN B OE1 1 
ATOM   2798 N  NE2 . GLN B 2 168 ? 6.520   6.118   -25.753  1.00 26.95  ? 168 GLN B NE2 1 
ATOM   2799 N  N   . ASN B 2 169 ? 4.253   1.309   -28.422  1.00 17.52  ? 169 ASN B N   1 
ATOM   2800 C  CA  . ASN B 2 169 ? 3.582   0.130   -27.865  1.00 26.24  ? 169 ASN B CA  1 
ATOM   2801 C  C   . ASN B 2 169 ? 2.198   -0.064  -28.470  1.00 19.26  ? 169 ASN B C   1 
ATOM   2802 O  O   . ASN B 2 169 ? 1.240   -0.387  -27.776  1.00 23.45  ? 169 ASN B O   1 
ATOM   2803 C  CB  . ASN B 2 169 ? 3.502   0.193   -26.332  1.00 23.66  ? 169 ASN B CB  1 
ATOM   2804 C  CG  . ASN B 2 169 ? 4.869   0.215   -25.681  1.00 36.95  ? 169 ASN B CG  1 
ATOM   2805 O  OD1 . ASN B 2 169 ? 5.631   1.175   -25.821  1.00 45.48  ? 169 ASN B OD1 1 
ATOM   2806 N  ND2 . ASN B 2 169 ? 5.199   -0.862  -24.980  1.00 45.23  ? 169 ASN B ND2 1 
ATOM   2807 N  N   . GLY B 2 170 ? 2.082   0.173   -29.773  1.00 23.40  ? 170 GLY B N   1 
ATOM   2808 C  CA  . GLY B 2 170 ? 0.835   -0.053  -30.472  1.00 23.40  ? 170 GLY B CA  1 
ATOM   2809 C  C   . GLY B 2 170 ? -0.205  1.047   -30.362  1.00 20.50  ? 170 GLY B C   1 
ATOM   2810 O  O   . GLY B 2 170 ? -1.294  0.904   -30.932  1.00 26.21  ? 170 GLY B O   1 
ATOM   2811 N  N   . LYS B 2 171 ? 0.081   2.136   -29.665  1.00 19.68  ? 171 LYS B N   1 
ATOM   2812 C  CA  . LYS B 2 171 ? -0.866  3.232   -29.531  1.00 21.68  ? 171 LYS B CA  1 
ATOM   2813 C  C   . LYS B 2 171 ? -0.405  4.411   -30.371  1.00 19.90  ? 171 LYS B C   1 
ATOM   2814 O  O   . LYS B 2 171 ? 0.792   4.565   -30.642  1.00 23.00  ? 171 LYS B O   1 
ATOM   2815 C  CB  . LYS B 2 171 ? -1.007  3.644   -28.063  1.00 28.78  ? 171 LYS B CB  1 
ATOM   2816 C  CG  . LYS B 2 171 ? -1.195  2.460   -27.115  1.00 17.82  ? 171 LYS B CG  1 
ATOM   2817 C  CD  . LYS B 2 171 ? -1.837  2.898   -25.819  1.00 29.50  ? 171 LYS B CD  1 
ATOM   2818 C  CE  . LYS B 2 171 ? -2.323  1.708   -25.031  1.00 36.45  ? 171 LYS B CE  1 
ATOM   2819 N  NZ  . LYS B 2 171 ? -2.340  2.023   -23.582  1.00 50.34  ? 171 LYS B NZ  1 
ATOM   2820 N  N   . ARG B 2 172 ? -1.357  5.239   -30.801  1.00 18.54  ? 172 ARG B N   1 
ATOM   2821 C  CA  . ARG B 2 172 ? -1.019  6.469   -31.522  1.00 16.70  ? 172 ARG B CA  1 
ATOM   2822 C  C   . ARG B 2 172 ? -0.613  7.551   -30.521  1.00 21.78  ? 172 ARG B C   1 
ATOM   2823 O  O   . ARG B 2 172 ? -1.462  8.103   -29.815  1.00 24.92  ? 172 ARG B O   1 
ATOM   2824 C  CB  . ARG B 2 172 ? -2.188  6.921   -32.383  1.00 14.34  ? 172 ARG B CB  1 
ATOM   2825 C  CG  . ARG B 2 172 ? -2.631  5.936   -33.477  1.00 17.77  ? 172 ARG B CG  1 
ATOM   2826 C  CD  . ARG B 2 172 ? -3.893  6.464   -34.171  1.00 22.64  ? 172 ARG B CD  1 
ATOM   2827 N  NE  . ARG B 2 172 ? -4.493  5.525   -35.110  1.00 25.46  ? 172 ARG B NE  1 
ATOM   2828 C  CZ  . ARG B 2 172 ? -5.649  5.708   -35.738  1.00 24.69  ? 172 ARG B CZ  1 
ATOM   2829 N  NH1 . ARG B 2 172 ? -6.484  6.667   -35.383  1.00 16.05  ? 172 ARG B NH1 1 
ATOM   2830 N  NH2 . ARG B 2 172 ? -5.992  4.878   -36.723  1.00 27.56  ? 172 ARG B NH2 1 
ATOM   2831 N  N   . ARG B 2 173 ? 0.679   7.874   -30.477  1.00 23.36  ? 173 ARG B N   1 
ATOM   2832 C  CA  . ARG B 2 173 ? 1.241   8.868   -29.567  1.00 16.23  ? 173 ARG B CA  1 
ATOM   2833 C  C   . ARG B 2 173 ? 1.580   10.153  -30.320  1.00 18.31  ? 173 ARG B C   1 
ATOM   2834 O  O   . ARG B 2 173 ? 2.262   10.120  -31.343  1.00 20.81  ? 173 ARG B O   1 
ATOM   2835 C  CB  . ARG B 2 173 ? 2.494   8.306   -28.890  1.00 18.40  ? 173 ARG B CB  1 
ATOM   2836 C  CG  . ARG B 2 173 ? 3.189   9.289   -28.006  1.00 24.86  ? 173 ARG B CG  1 
ATOM   2837 C  CD  . ARG B 2 173 ? 2.470   9.402   -26.674  1.00 23.60  ? 173 ARG B CD  1 
ATOM   2838 N  NE  . ARG B 2 173 ? 3.175   10.279  -25.752  1.00 21.12  ? 173 ARG B NE  1 
ATOM   2839 C  CZ  . ARG B 2 173 ? 3.926   9.859   -24.746  1.00 20.29  ? 173 ARG B CZ  1 
ATOM   2840 N  NH1 . ARG B 2 173 ? 4.138   8.570   -24.538  1.00 14.57  ? 173 ARG B NH1 1 
ATOM   2841 N  NH2 . ARG B 2 173 ? 4.463   10.759  -23.917  1.00 22.41  ? 173 ARG B NH2 1 
ATOM   2842 N  N   . LEU B 2 174 ? 1.114   11.288  -29.825  1.00 23.52  ? 174 LEU B N   1 
ATOM   2843 C  CA  . LEU B 2 174 ? 1.430   12.534  -30.508  1.00 20.96  ? 174 LEU B CA  1 
ATOM   2844 C  C   . LEU B 2 174 ? 2.878   12.922  -30.233  1.00 22.37  ? 174 LEU B C   1 
ATOM   2845 O  O   . LEU B 2 174 ? 3.408   12.695  -29.139  1.00 25.95  ? 174 LEU B O   1 
ATOM   2846 C  CB  . LEU B 2 174 ? 0.464   13.639  -30.076  1.00 16.64  ? 174 LEU B CB  1 
ATOM   2847 C  CG  . LEU B 2 174 ? -0.718  13.964  -30.992  1.00 17.76  ? 174 LEU B CG  1 
ATOM   2848 C  CD1 . LEU B 2 174 ? -1.742  12.820  -31.052  1.00 13.71  ? 174 LEU B CD1 1 
ATOM   2849 C  CD2 . LEU B 2 174 ? -1.379  15.276  -30.518  1.00 17.37  ? 174 LEU B CD2 1 
ATOM   2850 N  N   . ALA B 2 175 ? 3.520   13.509  -31.236  1.00 25.77  ? 175 ALA B N   1 
ATOM   2851 C  CA  . ALA B 2 175 ? 4.963   13.709  -31.224  1.00 21.80  ? 175 ALA B CA  1 
ATOM   2852 C  C   . ALA B 2 175 ? 5.312   14.755  -32.267  1.00 27.77  ? 175 ALA B C   1 
ATOM   2853 O  O   . ALA B 2 175 ? 4.472   15.169  -33.069  1.00 27.81  ? 175 ALA B O   1 
ATOM   2854 C  CB  . ALA B 2 175 ? 5.722   12.407  -31.519  1.00 20.72  ? 175 ALA B CB  1 
ATOM   2855 N  N   . LEU B 2 176 ? 6.570   15.177  -32.245  1.00 31.59  ? 176 LEU B N   1 
ATOM   2856 C  CA  . LEU B 2 176 ? 7.081   16.106  -33.240  1.00 32.22  ? 176 LEU B CA  1 
ATOM   2857 C  C   . LEU B 2 176 ? 7.446   15.287  -34.463  1.00 33.46  ? 176 LEU B C   1 
ATOM   2858 O  O   . LEU B 2 176 ? 8.190   14.311  -34.348  1.00 30.86  ? 176 LEU B O   1 
ATOM   2859 C  CB  . LEU B 2 176 ? 8.296   16.852  -32.697  1.00 29.88  ? 176 LEU B CB  1 
ATOM   2860 C  CG  . LEU B 2 176 ? 8.025   17.649  -31.417  1.00 28.85  ? 176 LEU B CG  1 
ATOM   2861 C  CD1 . LEU B 2 176 ? 9.237   18.457  -31.015  1.00 33.69  ? 176 LEU B CD1 1 
ATOM   2862 C  CD2 . LEU B 2 176 ? 6.826   18.557  -31.587  1.00 29.74  ? 176 LEU B CD2 1 
ATOM   2863 N  N   . VAL B 2 177 ? 6.851   15.620  -35.605  1.00 37.49  ? 177 VAL B N   1 
ATOM   2864 C  CA  . VAL B 2 177 ? 7.177   15.018  -36.897  1.00 43.68  ? 177 VAL B CA  1 
ATOM   2865 C  C   . VAL B 2 177 ? 6.977   16.118  -37.931  1.00 63.78  ? 177 VAL B C   1 
ATOM   2866 O  O   . VAL B 2 177 ? 5.866   16.644  -38.085  1.00 65.13  ? 177 VAL B O   1 
ATOM   2867 C  CB  . VAL B 2 177 ? 6.339   13.754  -37.231  1.00 39.36  ? 177 VAL B CB  1 
ATOM   2868 C  CG1 . VAL B 2 177 ? 6.281   12.763  -36.075  1.00 39.32  ? 177 VAL B CG1 1 
ATOM   2869 C  CG2 . VAL B 2 177 ? 4.914   14.085  -37.626  1.00 48.39  ? 177 VAL B CG2 1 
ATOM   2870 N  N   . ASN B 2 178 ? 8.048   16.523  -38.611  1.00 50.50  ? 178 ASN B N   1 
ATOM   2871 C  CA  . ASN B 2 178 ? 7.889   17.553  -39.630  1.00 64.72  ? 178 ASN B CA  1 
ATOM   2872 C  C   . ASN B 2 178 ? 7.706   16.986  -41.032  1.00 58.99  ? 178 ASN B C   1 
ATOM   2873 O  O   . ASN B 2 178 ? 7.811   17.728  -42.014  1.00 74.93  ? 178 ASN B O   1 
ATOM   2874 C  CB  . ASN B 2 178 ? 9.041   18.557  -39.577  1.00 62.14  ? 178 ASN B CB  1 
ATOM   2875 C  CG  . ASN B 2 178 ? 8.827   19.616  -38.499  1.00 52.45  ? 178 ASN B CG  1 
ATOM   2876 O  OD1 . ASN B 2 178 ? 8.707   20.804  -38.803  1.00 53.12  ? 178 ASN B OD1 1 
ATOM   2877 N  ND2 . ASN B 2 178 ? 8.752   19.185  -37.241  1.00 55.13  ? 178 ASN B ND2 1 
ATOM   2878 N  N   . GLU B 2 179 ? 7.393   15.704  -41.143  1.00 50.17  ? 179 GLU B N   1 
ATOM   2879 C  CA  . GLU B 2 179 ? 6.705   15.170  -42.307  1.00 58.11  ? 179 GLU B CA  1 
ATOM   2880 C  C   . GLU B 2 179 ? 5.360   14.628  -41.833  1.00 48.53  ? 179 GLU B C   1 
ATOM   2881 O  O   . GLU B 2 179 ? 5.283   13.976  -40.786  1.00 47.06  ? 179 GLU B O   1 
ATOM   2882 C  CB  . GLU B 2 179 ? 7.549   14.092  -42.991  1.00 48.13  ? 179 GLU B CB  1 
ATOM   2883 C  CG  . GLU B 2 179 ? 8.965   14.568  -43.326  1.00 72.55  ? 179 GLU B CG  1 
ATOM   2884 C  CD  . GLU B 2 179 ? 9.069   15.296  -44.669  1.00 87.77  ? 179 GLU B CD  1 
ATOM   2885 O  OE1 . GLU B 2 179 ? 8.363   16.313  -44.861  1.00 87.55  ? 179 GLU B OE1 1 
ATOM   2886 O  OE2 . GLU B 2 179 ? 9.877   14.864  -45.526  1.00 84.90  ? 179 GLU B OE2 1 
ATOM   2887 N  N   . ASN B 2 180 ? 4.303   14.957  -42.555  1.00 37.06  ? 180 ASN B N   1 
ATOM   2888 C  CA  . ASN B 2 180 ? 2.972   14.433  -42.266  1.00 40.37  ? 180 ASN B CA  1 
ATOM   2889 C  C   . ASN B 2 180 ? 2.409   14.902  -40.925  1.00 36.37  ? 180 ASN B C   1 
ATOM   2890 O  O   . ASN B 2 180 ? 2.216   14.089  -40.016  1.00 39.20  ? 180 ASN B O   1 
ATOM   2891 C  CB  . ASN B 2 180 ? 2.990   12.904  -42.307  1.00 35.42  ? 180 ASN B CB  1 
ATOM   2892 C  CG  . ASN B 2 180 ? 1.618   12.323  -42.469  1.00 48.88  ? 180 ASN B CG  1 
ATOM   2893 O  OD1 . ASN B 2 180 ? 0.680   13.020  -42.863  1.00 64.30  ? 180 ASN B OD1 1 
ATOM   2894 N  ND2 . ASN B 2 180 ? 1.483   11.040  -42.178  1.00 49.66  ? 180 ASN B ND2 1 
ATOM   2895 N  N   . PRO B 2 181 ? 2.094   16.181  -40.769  1.00 34.45  ? 181 PRO B N   1 
ATOM   2896 C  CA  . PRO B 2 181 ? 1.433   16.627  -39.541  1.00 34.74  ? 181 PRO B CA  1 
ATOM   2897 C  C   . PRO B 2 181 ? 0.008   16.101  -39.453  1.00 30.56  ? 181 PRO B C   1 
ATOM   2898 O  O   . PRO B 2 181 ? -0.614  15.748  -40.457  1.00 22.78  ? 181 PRO B O   1 
ATOM   2899 C  CB  . PRO B 2 181 ? 1.442   18.155  -39.672  1.00 32.46  ? 181 PRO B CB  1 
ATOM   2900 C  CG  . PRO B 2 181 ? 1.422   18.376  -41.162  1.00 30.01  ? 181 PRO B CG  1 
ATOM   2901 C  CD  . PRO B 2 181 ? 2.282   17.286  -41.727  1.00 32.16  ? 181 PRO B CD  1 
ATOM   2902 N  N   . LEU B 2 182 ? -0.510  16.089  -38.220  1.00 28.05  ? 182 LEU B N   1 
ATOM   2903 C  CA  . LEU B 2 182 ? -1.879  15.675  -37.926  1.00 25.95  ? 182 LEU B CA  1 
ATOM   2904 C  C   . LEU B 2 182 ? -2.850  16.815  -38.205  1.00 25.09  ? 182 LEU B C   1 
ATOM   2905 O  O   . LEU B 2 182 ? -2.772  17.862  -37.552  1.00 27.28  ? 182 LEU B O   1 
ATOM   2906 C  CB  . LEU B 2 182 ? -1.997  15.263  -36.465  1.00 23.59  ? 182 LEU B CB  1 
ATOM   2907 C  CG  . LEU B 2 182 ? -3.379  14.775  -36.041  1.00 22.84  ? 182 LEU B CG  1 
ATOM   2908 C  CD1 . LEU B 2 182 ? -3.755  13.453  -36.707  1.00 22.90  ? 182 LEU B CD1 1 
ATOM   2909 C  CD2 . LEU B 2 182 ? -3.383  14.631  -34.543  1.00 27.22  ? 182 LEU B CD2 1 
ATOM   2910 N  N   . ASP B 2 183 ? -3.771  16.618  -39.158  1.00 28.46  ? 183 ASP B N   1 
ATOM   2911 C  CA  . ASP B 2 183 ? -4.772  17.644  -39.471  1.00 26.09  ? 183 ASP B CA  1 
ATOM   2912 C  C   . ASP B 2 183 ? -5.925  17.506  -38.490  1.00 22.91  ? 183 ASP B C   1 
ATOM   2913 O  O   . ASP B 2 183 ? -6.517  16.434  -38.371  1.00 21.64  ? 183 ASP B O   1 
ATOM   2914 C  CB  . ASP B 2 183 ? -5.276  17.525  -40.918  1.00 30.51  ? 183 ASP B CB  1 
ATOM   2915 C  CG  . ASP B 2 183 ? -4.151  17.683  -41.966  1.00 37.36  ? 183 ASP B CG  1 
ATOM   2916 O  OD1 . ASP B 2 183 ? -3.052  18.187  -41.625  1.00 29.36  ? 183 ASP B OD1 1 
ATOM   2917 O  OD2 . ASP B 2 183 ? -4.361  17.270  -43.131  1.00 36.76  ? 183 ASP B OD2 1 
ATOM   2918 N  N   . VAL B 2 184 ? -6.251  18.586  -37.783  1.00 31.78  ? 184 VAL B N   1 
ATOM   2919 C  CA  . VAL B 2 184 ? -7.175  18.513  -36.658  1.00 27.48  ? 184 VAL B CA  1 
ATOM   2920 C  C   . VAL B 2 184 ? -8.274  19.555  -36.805  1.00 23.77  ? 184 VAL B C   1 
ATOM   2921 O  O   . VAL B 2 184 ? -8.116  20.580  -37.468  1.00 28.16  ? 184 VAL B O   1 
ATOM   2922 C  CB  . VAL B 2 184 ? -6.458  18.705  -35.301  1.00 21.50  ? 184 VAL B CB  1 
ATOM   2923 C  CG1 . VAL B 2 184 ? -5.411  17.610  -35.089  1.00 21.51  ? 184 VAL B CG1 1 
ATOM   2924 C  CG2 . VAL B 2 184 ? -5.821  20.104  -35.228  1.00 17.88  ? 184 VAL B CG2 1 
ATOM   2925 N  N   . LEU B 2 185 ? -9.396  19.288  -36.156  1.00 26.07  ? 185 LEU B N   1 
ATOM   2926 C  CA  . LEU B 2 185 ? -10.428 20.293  -35.973  1.00 26.38  ? 185 LEU B CA  1 
ATOM   2927 C  C   . LEU B 2 185 ? -10.767 20.357  -34.499  1.00 25.06  ? 185 LEU B C   1 
ATOM   2928 O  O   . LEU B 2 185 ? -10.416 19.474  -33.716  1.00 25.34  ? 185 LEU B O   1 
ATOM   2929 C  CB  . LEU B 2 185 ? -11.680 19.971  -36.776  1.00 28.18  ? 185 LEU B CB  1 
ATOM   2930 C  CG  . LEU B 2 185 ? -11.385 19.660  -38.232  1.00 32.32  ? 185 LEU B CG  1 
ATOM   2931 C  CD1 . LEU B 2 185 ? -12.499 18.761  -38.758  1.00 25.30  ? 185 LEU B CD1 1 
ATOM   2932 C  CD2 . LEU B 2 185 ? -11.254 20.973  -39.021  1.00 20.89  ? 185 LEU B CD2 1 
ATOM   2933 N  N   . PHE B 2 186 ? -11.480 21.403  -34.127  1.00 31.90  ? 186 PHE B N   1 
ATOM   2934 C  CA  . PHE B 2 186 ? -11.771 21.681  -32.730  1.00 26.13  ? 186 PHE B CA  1 
ATOM   2935 C  C   . PHE B 2 186 ? -13.277 21.685  -32.532  1.00 30.81  ? 186 PHE B C   1 
ATOM   2936 O  O   . PHE B 2 186 ? -13.965 22.604  -32.989  1.00 33.45  ? 186 PHE B O   1 
ATOM   2937 C  CB  . PHE B 2 186 ? -11.150 23.010  -32.329  1.00 23.72  ? 186 PHE B CB  1 
ATOM   2938 C  CG  . PHE B 2 186 ? -9.706  23.114  -32.666  1.00 22.27  ? 186 PHE B CG  1 
ATOM   2939 C  CD1 . PHE B 2 186 ? -8.765  22.407  -31.931  1.00 23.14  ? 186 PHE B CD1 1 
ATOM   2940 C  CD2 . PHE B 2 186 ? -9.277  23.927  -33.714  1.00 24.03  ? 186 PHE B CD2 1 
ATOM   2941 C  CE1 . PHE B 2 186 ? -7.420  22.505  -32.222  1.00 24.59  ? 186 PHE B CE1 1 
ATOM   2942 C  CE2 . PHE B 2 186 ? -7.932  24.047  -34.013  1.00 23.69  ? 186 PHE B CE2 1 
ATOM   2943 C  CZ  . PHE B 2 186 ? -6.995  23.331  -33.270  1.00 34.43  ? 186 PHE B CZ  1 
ATOM   2944 N  N   . GLN B 2 187 ? -13.785 20.665  -31.856  1.00 27.31  ? 187 GLN B N   1 
ATOM   2945 C  CA  . GLN B 2 187 ? -15.214 20.513  -31.614  1.00 28.85  ? 187 GLN B CA  1 
ATOM   2946 C  C   . GLN B 2 187 ? -15.531 20.898  -30.174  1.00 32.82  ? 187 GLN B C   1 
ATOM   2947 O  O   . GLN B 2 187 ? -15.049 20.259  -29.230  1.00 35.35  ? 187 GLN B O   1 
ATOM   2948 C  CB  . GLN B 2 187 ? -15.648 19.082  -31.907  1.00 27.88  ? 187 GLN B CB  1 
ATOM   2949 C  CG  . GLN B 2 187 ? -17.008 18.716  -31.384  1.00 32.26  ? 187 GLN B CG  1 
ATOM   2950 C  CD  . GLN B 2 187 ? -17.084 17.230  -31.091  1.00 43.56  ? 187 GLN B CD  1 
ATOM   2951 O  OE1 . GLN B 2 187 ? -17.137 16.408  -32.006  1.00 46.72  ? 187 GLN B OE1 1 
ATOM   2952 N  NE2 . GLN B 2 187 ? -17.026 16.875  -29.806  1.00 56.50  ? 187 GLN B NE2 1 
ATOM   2953 N  N   . GLU B 2 188 ? -16.343 21.936  -30.013  1.00 33.99  ? 188 GLU B N   1 
ATOM   2954 C  CA  . GLU B 2 188 ? -16.646 22.467  -28.695  1.00 33.63  ? 188 GLU B CA  1 
ATOM   2955 C  C   . GLU B 2 188 ? -17.456 21.468  -27.875  1.00 31.88  ? 188 GLU B C   1 
ATOM   2956 O  O   . GLU B 2 188 ? -18.328 20.772  -28.398  1.00 37.73  ? 188 GLU B O   1 
ATOM   2957 C  CB  . GLU B 2 188 ? -17.386 23.797  -28.846  1.00 36.26  ? 188 GLU B CB  1 
ATOM   2958 C  CG  . GLU B 2 188 ? -17.818 24.456  -27.548  1.00 49.58  ? 188 GLU B CG  1 
ATOM   2959 C  CD  . GLU B 2 188 ? -18.874 25.525  -27.780  1.00 57.60  ? 188 GLU B CD  1 
ATOM   2960 O  OE1 . GLU B 2 188 ? -18.518 26.725  -27.841  1.00 55.75  ? 188 GLU B OE1 1 
ATOM   2961 O  OE2 . GLU B 2 188 ? -20.062 25.151  -27.929  1.00 69.48  ? 188 GLU B OE2 1 
ATOM   2962 N  N   . VAL B 2 189 ? -17.133 21.369  -26.587  1.00 31.22  ? 189 VAL B N   1 
ATOM   2963 C  CA  . VAL B 2 189 ? -17.813 20.442  -25.688  1.00 30.39  ? 189 VAL B CA  1 
ATOM   2964 C  C   . VAL B 2 189 ? -19.147 21.026  -25.194  1.00 43.98  ? 189 VAL B C   1 
ATOM   2965 O  O   . VAL B 2 189 ? -19.296 22.251  -25.041  1.00 36.53  ? 189 VAL B O   1 
ATOM   2966 C  CB  . VAL B 2 189 ? -16.919 20.097  -24.497  1.00 34.11  ? 189 VAL B CB  1 
ATOM   2967 C  CG1 . VAL B 2 189 ? -15.546 19.647  -24.966  1.00 35.91  ? 189 VAL B CG1 1 
ATOM   2968 C  CG2 . VAL B 2 189 ? -16.793 21.295  -23.627  1.00 40.20  ? 189 VAL B CG2 1 
ATOM   2969 N  N   . ILE C 1 9   ? 8.330   13.494  -82.901  1.00 23.48  ? 1   ILE C N   1 
ATOM   2970 C  CA  . ILE C 1 9   ? 8.486   14.858  -83.412  1.00 34.47  ? 1   ILE C CA  1 
ATOM   2971 C  C   . ILE C 1 9   ? 8.790   14.766  -84.915  1.00 30.94  ? 1   ILE C C   1 
ATOM   2972 O  O   . ILE C 1 9   ? 9.784   14.155  -85.310  1.00 27.22  ? 1   ILE C O   1 
ATOM   2973 C  CB  . ILE C 1 9   ? 9.618   15.623  -82.691  1.00 32.69  ? 1   ILE C CB  1 
ATOM   2974 C  CG1 . ILE C 1 9   ? 9.302   15.842  -81.200  1.00 26.52  ? 1   ILE C CG1 1 
ATOM   2975 C  CG2 . ILE C 1 9   ? 9.846   16.974  -83.399  1.00 29.55  ? 1   ILE C CG2 1 
ATOM   2976 C  CD1 . ILE C 1 9   ? 8.119   16.720  -80.918  1.00 36.73  ? 1   ILE C CD1 1 
ATOM   2977 N  N   . VAL C 1 10  ? 7.920   15.338  -85.747  1.00 29.10  ? 2   VAL C N   1 
ATOM   2978 C  CA  . VAL C 1 10  ? 8.108   15.369  -87.195  1.00 32.08  ? 2   VAL C CA  1 
ATOM   2979 C  C   . VAL C 1 10  ? 8.763   16.678  -87.595  1.00 29.56  ? 2   VAL C C   1 
ATOM   2980 O  O   . VAL C 1 10  ? 8.373   17.753  -87.127  1.00 26.84  ? 2   VAL C O   1 
ATOM   2981 C  CB  . VAL C 1 10  ? 6.768   15.183  -87.928  1.00 40.06  ? 2   VAL C CB  1 
ATOM   2982 C  CG1 . VAL C 1 10  ? 6.895   15.595  -89.388  1.00 33.42  ? 2   VAL C CG1 1 
ATOM   2983 C  CG2 . VAL C 1 10  ? 6.373   13.743  -87.878  1.00 37.51  ? 2   VAL C CG2 1 
ATOM   2984 N  N   . GLY C 1 11  ? 9.759   16.588  -88.473  1.00 34.55  ? 3   GLY C N   1 
ATOM   2985 C  CA  . GLY C 1 11  ? 10.404  17.781  -88.985  1.00 29.96  ? 3   GLY C CA  1 
ATOM   2986 C  C   . GLY C 1 11  ? 11.278  18.499  -87.991  1.00 30.66  ? 3   GLY C C   1 
ATOM   2987 O  O   . GLY C 1 11  ? 11.554  19.685  -88.175  1.00 35.02  ? 3   GLY C O   1 
ATOM   2988 N  N   . GLY C 1 12  ? 11.718  17.824  -86.938  1.00 26.42  ? 4   GLY C N   1 
ATOM   2989 C  CA  . GLY C 1 12  ? 12.583  18.427  -85.944  1.00 23.56  ? 4   GLY C CA  1 
ATOM   2990 C  C   . GLY C 1 12  ? 14.030  18.005  -86.096  1.00 30.60  ? 4   GLY C C   1 
ATOM   2991 O  O   . GLY C 1 12  ? 14.491  17.639  -87.182  1.00 27.49  ? 4   GLY C O   1 
ATOM   2992 N  N   . TYR C 1 13  ? 14.765  18.027  -84.990  1.00 30.28  ? 5   TYR C N   1 
ATOM   2993 C  CA  . TYR C 1 13  ? 16.181  17.697  -85.062  1.00 35.47  ? 5   TYR C CA  1 
ATOM   2994 C  C   . TYR C 1 13  ? 16.608  17.031  -83.766  1.00 25.04  ? 5   TYR C C   1 
ATOM   2995 O  O   . TYR C 1 13  ? 16.035  17.290  -82.704  1.00 31.27  ? 5   TYR C O   1 
ATOM   2996 C  CB  . TYR C 1 13  ? 17.040  18.947  -85.331  1.00 25.01  ? 5   TYR C CB  1 
ATOM   2997 C  CG  . TYR C 1 13  ? 16.918  19.977  -84.242  1.00 28.81  ? 5   TYR C CG  1 
ATOM   2998 C  CD1 . TYR C 1 13  ? 15.878  20.903  -84.256  1.00 22.95  ? 5   TYR C CD1 1 
ATOM   2999 C  CD2 . TYR C 1 13  ? 17.819  20.009  -83.175  1.00 28.73  ? 5   TYR C CD2 1 
ATOM   3000 C  CE1 . TYR C 1 13  ? 15.739  21.844  -83.237  1.00 30.50  ? 5   TYR C CE1 1 
ATOM   3001 C  CE2 . TYR C 1 13  ? 17.682  20.938  -82.156  1.00 24.15  ? 5   TYR C CE2 1 
ATOM   3002 C  CZ  . TYR C 1 13  ? 16.639  21.863  -82.195  1.00 30.74  ? 5   TYR C CZ  1 
ATOM   3003 O  OH  . TYR C 1 13  ? 16.499  22.822  -81.197  1.00 36.57  ? 5   TYR C OH  1 
ATOM   3004 N  N   . THR C 1 14  ? 17.613  16.163  -83.869  1.00 28.79  ? 6   THR C N   1 
ATOM   3005 C  CA  . THR C 1 14  ? 18.207  15.539  -82.691  1.00 25.84  ? 6   THR C CA  1 
ATOM   3006 C  C   . THR C 1 14  ? 18.773  16.593  -81.751  1.00 32.38  ? 6   THR C C   1 
ATOM   3007 O  O   . THR C 1 14  ? 19.609  17.411  -82.149  1.00 37.89  ? 6   THR C O   1 
ATOM   3008 C  CB  . THR C 1 14  ? 19.303  14.559  -83.106  1.00 29.31  ? 6   THR C CB  1 
ATOM   3009 O  OG1 . THR C 1 14  ? 18.807  13.677  -84.120  1.00 25.11  ? 6   THR C OG1 1 
ATOM   3010 C  CG2 . THR C 1 14  ? 19.778  13.736  -81.910  1.00 34.29  ? 6   THR C CG2 1 
ATOM   3011 N  N   . CYS C 1 15  ? 18.321  16.571  -80.501  1.00 31.87  ? 7   CYS C N   1 
ATOM   3012 C  CA  . CYS C 1 15  ? 18.829  17.516  -79.520  1.00 32.74  ? 7   CYS C CA  1 
ATOM   3013 C  C   . CYS C 1 15  ? 20.284  17.217  -79.199  1.00 38.68  ? 7   CYS C C   1 
ATOM   3014 O  O   . CYS C 1 15  ? 20.729  16.065  -79.234  1.00 33.52  ? 7   CYS C O   1 
ATOM   3015 C  CB  . CYS C 1 15  ? 18.011  17.460  -78.229  1.00 35.00  ? 7   CYS C CB  1 
ATOM   3016 S  SG  . CYS C 1 15  ? 16.212  17.360  -78.481  1.00 60.16  ? 7   CYS C SG  1 
ATOM   3017 N  N   . ALA C 1 16  ? 21.026  18.277  -78.883  1.00 43.20  ? 8   ALA C N   1 
ATOM   3018 C  CA  . ALA C 1 16  ? 22.315  18.101  -78.231  1.00 42.78  ? 8   ALA C CA  1 
ATOM   3019 C  C   . ALA C 1 16  ? 22.135  17.338  -76.926  1.00 41.52  ? 8   ALA C C   1 
ATOM   3020 O  O   . ALA C 1 16  ? 21.177  17.571  -76.178  1.00 39.86  ? 8   ALA C O   1 
ATOM   3021 C  CB  . ALA C 1 16  ? 22.964  19.451  -77.953  1.00 38.27  ? 8   ALA C CB  1 
ATOM   3022 N  N   . ALA C 1 17  ? 23.058  16.413  -76.663  1.00 43.21  ? 9   ALA C N   1 
ATOM   3023 C  CA  . ALA C 1 17  ? 23.015  15.638  -75.430  1.00 49.92  ? 9   ALA C CA  1 
ATOM   3024 C  C   . ALA C 1 17  ? 23.066  16.562  -74.220  1.00 55.06  ? 9   ALA C C   1 
ATOM   3025 O  O   . ALA C 1 17  ? 23.927  17.446  -74.136  1.00 49.66  ? 9   ALA C O   1 
ATOM   3026 C  CB  . ALA C 1 17  ? 24.175  14.644  -75.388  1.00 46.80  ? 9   ALA C CB  1 
ATOM   3027 N  N   . ASN C 1 18  ? 22.123  16.359  -73.294  1.00 42.42  ? 10  ASN C N   1 
ATOM   3028 C  CA  . ASN C 1 18  ? 21.977  17.117  -72.054  1.00 52.48  ? 10  ASN C CA  1 
ATOM   3029 C  C   . ASN C 1 18  ? 21.518  18.547  -72.298  1.00 45.98  ? 10  ASN C C   1 
ATOM   3030 O  O   . ASN C 1 18  ? 21.582  19.379  -71.385  1.00 52.99  ? 10  ASN C O   1 
ATOM   3031 C  CB  . ASN C 1 18  ? 23.277  17.131  -71.243  1.00 61.79  ? 10  ASN C CB  1 
ATOM   3032 C  CG  . ASN C 1 18  ? 23.990  15.791  -71.281  1.00 76.46  ? 10  ASN C CG  1 
ATOM   3033 O  OD1 . ASN C 1 18  ? 25.129  15.702  -71.757  1.00 82.30  ? 10  ASN C OD1 1 
ATOM   3034 N  ND2 . ASN C 1 18  ? 23.294  14.729  -70.869  1.00 61.95  ? 10  ASN C ND2 1 
ATOM   3035 N  N   . SER C 1 19  ? 21.055  18.857  -73.504  1.00 36.18  ? 11  SER C N   1 
ATOM   3036 C  CA  . SER C 1 19  ? 20.383  20.122  -73.752  1.00 36.80  ? 11  SER C CA  1 
ATOM   3037 C  C   . SER C 1 19  ? 18.960  20.167  -73.196  1.00 37.69  ? 11  SER C C   1 
ATOM   3038 O  O   . SER C 1 19  ? 18.419  21.270  -73.031  1.00 31.90  ? 11  SER C O   1 
ATOM   3039 C  CB  . SER C 1 19  ? 20.390  20.415  -75.258  1.00 35.85  ? 11  SER C CB  1 
ATOM   3040 O  OG  . SER C 1 19  ? 19.199  19.984  -75.893  1.00 40.03  ? 11  SER C OG  1 
ATOM   3041 N  N   . ILE C 1 20  ? 18.339  19.021  -72.904  1.00 33.78  ? 12  ILE C N   1 
ATOM   3042 C  CA  . ILE C 1 20  ? 16.970  19.031  -72.369  1.00 35.64  ? 12  ILE C CA  1 
ATOM   3043 C  C   . ILE C 1 20  ? 16.914  18.270  -71.045  1.00 32.60  ? 12  ILE C C   1 
ATOM   3044 O  O   . ILE C 1 20  ? 16.235  17.235  -70.965  1.00 29.01  ? 12  ILE C O   1 
ATOM   3045 C  CB  . ILE C 1 20  ? 15.980  18.411  -73.363  1.00 35.76  ? 12  ILE C CB  1 
ATOM   3046 C  CG1 . ILE C 1 20  ? 16.258  18.915  -74.765  1.00 32.97  ? 12  ILE C CG1 1 
ATOM   3047 C  CG2 . ILE C 1 20  ? 14.552  18.831  -73.005  1.00 33.42  ? 12  ILE C CG2 1 
ATOM   3048 C  CD1 . ILE C 1 20  ? 15.492  20.136  -75.105  1.00 42.28  ? 12  ILE C CD1 1 
ATOM   3049 N  N   . PRO C 1 21  ? 17.581  18.732  -69.978  1.00 36.34  ? 13  PRO C N   1 
ATOM   3050 C  CA  . PRO C 1 21  ? 17.759  17.868  -68.796  1.00 33.03  ? 13  PRO C CA  1 
ATOM   3051 C  C   . PRO C 1 21  ? 16.488  17.638  -68.000  1.00 25.36  ? 13  PRO C C   1 
ATOM   3052 O  O   . PRO C 1 21  ? 16.514  16.837  -67.065  1.00 26.12  ? 13  PRO C O   1 
ATOM   3053 C  CB  . PRO C 1 21  ? 18.805  18.623  -67.952  1.00 28.21  ? 13  PRO C CB  1 
ATOM   3054 C  CG  . PRO C 1 21  ? 19.301  19.744  -68.849  1.00 33.53  ? 13  PRO C CG  1 
ATOM   3055 C  CD  . PRO C 1 21  ? 18.159  20.064  -69.750  1.00 26.88  ? 13  PRO C CD  1 
ATOM   3056 N  N   . TYR C 1 22  ? 15.393  18.314  -68.331  1.00 26.09  ? 14  TYR C N   1 
ATOM   3057 C  CA  . TYR C 1 22  ? 14.115  18.105  -67.665  1.00 25.35  ? 14  TYR C CA  1 
ATOM   3058 C  C   . TYR C 1 22  ? 13.228  17.102  -68.398  1.00 22.08  ? 14  TYR C C   1 
ATOM   3059 O  O   . TYR C 1 22  ? 12.176  16.725  -67.869  1.00 26.71  ? 14  TYR C O   1 
ATOM   3060 C  CB  . TYR C 1 22  ? 13.367  19.447  -67.523  1.00 21.09  ? 14  TYR C CB  1 
ATOM   3061 C  CG  . TYR C 1 22  ? 13.268  20.176  -68.845  1.00 24.12  ? 14  TYR C CG  1 
ATOM   3062 C  CD1 . TYR C 1 22  ? 12.272  19.850  -69.768  1.00 21.17  ? 14  TYR C CD1 1 
ATOM   3063 C  CD2 . TYR C 1 22  ? 14.178  21.170  -69.190  1.00 27.99  ? 14  TYR C CD2 1 
ATOM   3064 C  CE1 . TYR C 1 22  ? 12.184  20.504  -70.996  1.00 28.12  ? 14  TYR C CE1 1 
ATOM   3065 C  CE2 . TYR C 1 22  ? 14.088  21.849  -70.427  1.00 15.39  ? 14  TYR C CE2 1 
ATOM   3066 C  CZ  . TYR C 1 22  ? 13.096  21.505  -71.313  1.00 25.82  ? 14  TYR C CZ  1 
ATOM   3067 O  OH  . TYR C 1 22  ? 13.016  22.150  -72.521  1.00 35.05  ? 14  TYR C OH  1 
ATOM   3068 N  N   . GLN C 1 23  ? 13.590  16.694  -69.613  1.00 21.85  ? 15  GLN C N   1 
ATOM   3069 C  CA  . GLN C 1 23  ? 12.790  15.696  -70.310  1.00 23.80  ? 15  GLN C CA  1 
ATOM   3070 C  C   . GLN C 1 23  ? 12.912  14.354  -69.598  1.00 21.76  ? 15  GLN C C   1 
ATOM   3071 O  O   . GLN C 1 23  ? 13.999  13.964  -69.167  1.00 20.59  ? 15  GLN C O   1 
ATOM   3072 C  CB  . GLN C 1 23  ? 13.238  15.571  -71.769  1.00 24.80  ? 15  GLN C CB  1 
ATOM   3073 C  CG  . GLN C 1 23  ? 12.602  14.410  -72.548  1.00 20.25  ? 15  GLN C CG  1 
ATOM   3074 C  CD  . GLN C 1 23  ? 11.243  14.781  -73.170  1.00 22.83  ? 15  GLN C CD  1 
ATOM   3075 O  OE1 . GLN C 1 23  ? 11.116  15.784  -73.878  1.00 23.16  ? 15  GLN C OE1 1 
ATOM   3076 N  NE2 . GLN C 1 23  ? 10.231  13.964  -72.906  1.00 22.03  ? 15  GLN C NE2 1 
ATOM   3077 N  N   . VAL C 1 24  ? 11.785  13.658  -69.429  1.00 19.59  ? 16  VAL C N   1 
ATOM   3078 C  CA  . VAL C 1 24  ? 11.840  12.301  -68.904  1.00 24.40  ? 16  VAL C CA  1 
ATOM   3079 C  C   . VAL C 1 24  ? 11.121  11.376  -69.867  1.00 19.75  ? 16  VAL C C   1 
ATOM   3080 O  O   . VAL C 1 24  ? 10.256  11.789  -70.643  1.00 17.58  ? 16  VAL C O   1 
ATOM   3081 C  CB  . VAL C 1 24  ? 11.231  12.148  -67.490  1.00 24.27  ? 16  VAL C CB  1 
ATOM   3082 C  CG1 . VAL C 1 24  ? 11.890  13.111  -66.495  1.00 22.22  ? 16  VAL C CG1 1 
ATOM   3083 C  CG2 . VAL C 1 24  ? 9.733   12.292  -67.527  1.00 13.69  ? 16  VAL C CG2 1 
ATOM   3084 N  N   . SER C 1 25  ? 11.495  10.107  -69.806  1.00 18.02  ? 17  SER C N   1 
ATOM   3085 C  CA  . SER C 1 25  ? 10.783  9.064   -70.519  1.00 19.67  ? 17  SER C CA  1 
ATOM   3086 C  C   . SER C 1 25  ? 10.002  8.265   -69.490  1.00 21.86  ? 17  SER C C   1 
ATOM   3087 O  O   . SER C 1 25  ? 10.556  7.875   -68.451  1.00 13.84  ? 17  SER C O   1 
ATOM   3088 C  CB  . SER C 1 25  ? 11.732  8.150   -71.305  1.00 24.41  ? 17  SER C CB  1 
ATOM   3089 O  OG  . SER C 1 25  ? 11.052  6.996   -71.784  1.00 25.37  ? 17  SER C OG  1 
ATOM   3090 N  N   . LEU C 1 26  ? 8.714   8.078   -69.764  1.00 17.67  ? 18  LEU C N   1 
ATOM   3091 C  CA  . LEU C 1 26  ? 7.850   7.230   -68.964  1.00 21.44  ? 18  LEU C CA  1 
ATOM   3092 C  C   . LEU C 1 26  ? 7.914   5.832   -69.562  1.00 20.85  ? 18  LEU C C   1 
ATOM   3093 O  O   . LEU C 1 26  ? 7.602   5.644   -70.737  1.00 21.97  ? 18  LEU C O   1 
ATOM   3094 C  CB  . LEU C 1 26  ? 6.426   7.792   -68.946  1.00 9.81   ? 18  LEU C CB  1 
ATOM   3095 C  CG  . LEU C 1 26  ? 6.412   9.152   -68.201  1.00 13.89  ? 18  LEU C CG  1 
ATOM   3096 C  CD1 . LEU C 1 26  ? 5.014   9.633   -67.936  1.00 16.35  ? 18  LEU C CD1 1 
ATOM   3097 C  CD2 . LEU C 1 26  ? 7.197   9.098   -66.866  1.00 13.34  ? 18  LEU C CD2 1 
ATOM   3098 N  N   . ASN C 1 27  ? 8.333   4.856   -68.766  1.00 20.22  ? 19  ASN C N   1 
ATOM   3099 C  CA  . ASN C 1 27  ? 8.606   3.521   -69.276  1.00 19.50  ? 19  ASN C CA  1 
ATOM   3100 C  C   . ASN C 1 27  ? 7.738   2.497   -68.567  1.00 20.48  ? 19  ASN C C   1 
ATOM   3101 O  O   . ASN C 1 27  ? 7.646   2.508   -67.340  1.00 18.14  ? 19  ASN C O   1 
ATOM   3102 C  CB  . ASN C 1 27  ? 10.082  3.163   -69.110  1.00 20.98  ? 19  ASN C CB  1 
ATOM   3103 C  CG  . ASN C 1 27  ? 10.482  1.970   -69.956  1.00 26.29  ? 19  ASN C CG  1 
ATOM   3104 O  OD1 . ASN C 1 27  ? 10.150  0.827   -69.612  1.00 19.44  ? 19  ASN C OD1 1 
ATOM   3105 N  ND2 . ASN C 1 27  ? 11.219  2.217   -71.048  1.00 18.43  ? 19  ASN C ND2 1 
ATOM   3106 N  N   . SER C 1 28  ? 7.103   1.620   -69.350  1.00 21.50  ? 20  SER C N   1 
ATOM   3107 C  CA  . SER C 1 28  ? 6.249   0.529   -68.878  1.00 24.93  ? 20  SER C CA  1 
ATOM   3108 C  C   . SER C 1 28  ? 6.662   -0.780  -69.544  1.00 29.96  ? 20  SER C C   1 
ATOM   3109 O  O   . SER C 1 28  ? 5.828   -1.556  -70.013  1.00 28.59  ? 20  SER C O   1 
ATOM   3110 C  CB  . SER C 1 28  ? 4.777   0.834   -69.149  1.00 26.81  ? 20  SER C CB  1 
ATOM   3111 O  OG  . SER C 1 28  ? 4.538   0.933   -70.552  1.00 21.42  ? 20  SER C OG  1 
ATOM   3112 N  N   . GLY C 1 29  ? 7.970   -1.042  -69.578  1.00 22.00  ? 21  GLY C N   1 
ATOM   3113 C  CA  . GLY C 1 29  ? 8.561   -2.045  -70.426  1.00 24.81  ? 21  GLY C CA  1 
ATOM   3114 C  C   . GLY C 1 29  ? 9.177   -1.475  -71.685  1.00 21.38  ? 21  GLY C C   1 
ATOM   3115 O  O   . GLY C 1 29  ? 10.008  -2.132  -72.312  1.00 28.17  ? 21  GLY C O   1 
ATOM   3116 N  N   . SER C 1 30  ? 8.785   -0.268  -72.057  1.00 17.32  ? 22  SER C N   1 
ATOM   3117 C  CA  . SER C 1 30  ? 9.309   0.438   -73.212  1.00 24.74  ? 22  SER C CA  1 
ATOM   3118 C  C   . SER C 1 30  ? 8.893   1.890   -73.044  1.00 18.30  ? 22  SER C C   1 
ATOM   3119 O  O   . SER C 1 30  ? 7.951   2.194   -72.314  1.00 22.17  ? 22  SER C O   1 
ATOM   3120 C  CB  . SER C 1 30  ? 8.767   -0.143  -74.523  1.00 22.97  ? 22  SER C CB  1 
ATOM   3121 O  OG  . SER C 1 30  ? 7.352   0.057   -74.603  1.00 37.61  ? 22  SER C OG  1 
ATOM   3122 N  N   . HIS C 1 31  ? 9.614   2.793   -73.695  1.00 24.53  ? 23  HIS C N   1 
ATOM   3123 C  CA  . HIS C 1 31  ? 9.155   4.175   -73.699  1.00 22.27  ? 23  HIS C CA  1 
ATOM   3124 C  C   . HIS C 1 31  ? 7.710   4.238   -74.193  1.00 26.20  ? 23  HIS C C   1 
ATOM   3125 O  O   . HIS C 1 31  ? 7.352   3.607   -75.193  1.00 22.47  ? 23  HIS C O   1 
ATOM   3126 C  CB  . HIS C 1 31  ? 10.039  5.041   -74.588  1.00 20.60  ? 23  HIS C CB  1 
ATOM   3127 C  CG  . HIS C 1 31  ? 9.460   6.397   -74.842  1.00 27.39  ? 23  HIS C CG  1 
ATOM   3128 N  ND1 . HIS C 1 31  ? 9.639   7.454   -73.972  1.00 18.64  ? 23  HIS C ND1 1 
ATOM   3129 C  CD2 . HIS C 1 31  ? 8.670   6.858   -75.842  1.00 19.14  ? 23  HIS C CD2 1 
ATOM   3130 C  CE1 . HIS C 1 31  ? 9.006   8.516   -74.443  1.00 28.23  ? 23  HIS C CE1 1 
ATOM   3131 N  NE2 . HIS C 1 31  ? 8.404   8.178   -75.571  1.00 28.65  ? 23  HIS C NE2 1 
ATOM   3132 N  N   . PHE C 1 32  ? 6.872   4.980   -73.482  1.00 12.77  ? 24  PHE C N   1 
ATOM   3133 C  CA  . PHE C 1 32  ? 5.517   5.176   -73.979  1.00 19.28  ? 24  PHE C CA  1 
ATOM   3134 C  C   . PHE C 1 32  ? 5.017   6.606   -73.864  1.00 23.84  ? 24  PHE C C   1 
ATOM   3135 O  O   . PHE C 1 32  ? 3.983   6.911   -74.464  1.00 28.63  ? 24  PHE C O   1 
ATOM   3136 C  CB  . PHE C 1 32  ? 4.528   4.237   -73.261  1.00 19.38  ? 24  PHE C CB  1 
ATOM   3137 C  CG  . PHE C 1 32  ? 4.163   4.655   -71.846  1.00 18.27  ? 24  PHE C CG  1 
ATOM   3138 C  CD1 . PHE C 1 32  ? 3.086   5.513   -71.601  1.00 13.75  ? 24  PHE C CD1 1 
ATOM   3139 C  CD2 . PHE C 1 32  ? 4.871   4.141   -70.754  1.00 19.44  ? 24  PHE C CD2 1 
ATOM   3140 C  CE1 . PHE C 1 32  ? 2.738   5.872   -70.283  1.00 24.68  ? 24  PHE C CE1 1 
ATOM   3141 C  CE2 . PHE C 1 32  ? 4.540   4.490   -69.447  1.00 17.65  ? 24  PHE C CE2 1 
ATOM   3142 C  CZ  . PHE C 1 32  ? 3.467   5.360   -69.200  1.00 17.52  ? 24  PHE C CZ  1 
ATOM   3143 N  N   . CYS C 1 33  ? 5.699   7.484   -73.124  1.00 17.30  ? 25  CYS C N   1 
ATOM   3144 C  CA  . CYS C 1 33  ? 5.263   8.854   -72.900  1.00 15.27  ? 25  CYS C CA  1 
ATOM   3145 C  C   . CYS C 1 33  ? 6.449   9.690   -72.453  1.00 19.27  ? 25  CYS C C   1 
ATOM   3146 O  O   . CYS C 1 33  ? 7.379   9.187   -71.813  1.00 17.17  ? 25  CYS C O   1 
ATOM   3147 C  CB  . CYS C 1 33  ? 4.158   8.947   -71.831  1.00 16.08  ? 25  CYS C CB  1 
ATOM   3148 S  SG  . CYS C 1 33  ? 2.510   8.777   -72.515  1.00 37.97  ? 25  CYS C SG  1 
ATOM   3149 N  N   . GLY C 1 34  ? 6.384   10.986  -72.771  1.00 21.02  ? 26  GLY C N   1 
ATOM   3150 C  CA  . GLY C 1 34  ? 7.295   11.947  -72.187  1.00 17.19  ? 26  GLY C CA  1 
ATOM   3151 C  C   . GLY C 1 34  ? 6.795   12.479  -70.849  1.00 22.23  ? 26  GLY C C   1 
ATOM   3152 O  O   . GLY C 1 34  ? 5.705   12.116  -70.390  1.00 20.98  ? 26  GLY C O   1 
ATOM   3153 N  N   . GLY C 1 35  ? 7.632   13.320  -70.237  1.00 19.01  ? 27  GLY C N   1 
ATOM   3154 C  CA  . GLY C 1 35  ? 7.281   14.076  -69.049  1.00 19.67  ? 27  GLY C CA  1 
ATOM   3155 C  C   . GLY C 1 35  ? 8.323   15.148  -68.786  1.00 23.46  ? 27  GLY C C   1 
ATOM   3156 O  O   . GLY C 1 35  ? 9.306   15.281  -69.522  1.00 24.06  ? 27  GLY C O   1 
ATOM   3157 N  N   . SER C 1 36  ? 8.095   15.912  -67.708  1.00 14.90  ? 28  SER C N   1 
ATOM   3158 C  CA  . SER C 1 36  ? 8.943   17.041  -67.327  1.00 19.20  ? 28  SER C CA  1 
ATOM   3159 C  C   . SER C 1 36  ? 9.248   16.972  -65.841  1.00 24.64  ? 28  SER C C   1 
ATOM   3160 O  O   . SER C 1 36  ? 8.326   16.875  -65.021  1.00 19.03  ? 28  SER C O   1 
ATOM   3161 C  CB  . SER C 1 36  ? 8.277   18.399  -67.618  1.00 20.32  ? 28  SER C CB  1 
ATOM   3162 O  OG  . SER C 1 36  ? 7.671   18.430  -68.893  1.00 27.70  ? 28  SER C OG  1 
ATOM   3163 N  N   . LEU C 1 37  ? 10.538  17.044  -65.502  1.00 20.47  ? 29  LEU C N   1 
ATOM   3164 C  CA  . LEU C 1 37  ? 10.960  17.143  -64.113  1.00 20.48  ? 29  LEU C CA  1 
ATOM   3165 C  C   . LEU C 1 37  ? 10.763  18.579  -63.627  1.00 25.13  ? 29  LEU C C   1 
ATOM   3166 O  O   . LEU C 1 37  ? 11.366  19.513  -64.165  1.00 29.85  ? 29  LEU C O   1 
ATOM   3167 C  CB  . LEU C 1 37  ? 12.412  16.708  -63.974  1.00 17.30  ? 29  LEU C CB  1 
ATOM   3168 C  CG  . LEU C 1 37  ? 12.800  16.462  -62.509  1.00 20.42  ? 29  LEU C CG  1 
ATOM   3169 C  CD1 . LEU C 1 37  ? 11.976  15.324  -61.940  1.00 17.52  ? 29  LEU C CD1 1 
ATOM   3170 C  CD2 . LEU C 1 37  ? 14.284  16.143  -62.375  1.00 25.60  ? 29  LEU C CD2 1 
ATOM   3171 N  N   . ILE C 1 38  ? 9.897   18.768  -62.633  1.00 23.67  ? 30  ILE C N   1 
ATOM   3172 C  CA  . ILE C 1 38  ? 9.630   20.100  -62.094  1.00 25.92  ? 30  ILE C CA  1 
ATOM   3173 C  C   . ILE C 1 38  ? 10.082  20.234  -60.656  1.00 24.15  ? 30  ILE C C   1 
ATOM   3174 O  O   . ILE C 1 38  ? 9.858   21.274  -60.033  1.00 35.83  ? 30  ILE C O   1 
ATOM   3175 C  CB  . ILE C 1 38  ? 8.142   20.462  -62.226  1.00 23.50  ? 30  ILE C CB  1 
ATOM   3176 C  CG1 . ILE C 1 38  ? 7.280   19.329  -61.674  1.00 23.92  ? 30  ILE C CG1 1 
ATOM   3177 C  CG2 . ILE C 1 38  ? 7.780   20.770  -63.692  1.00 19.53  ? 30  ILE C CG2 1 
ATOM   3178 C  CD1 . ILE C 1 38  ? 6.078   19.828  -60.964  1.00 26.29  ? 30  ILE C CD1 1 
ATOM   3179 N  N   . ASN C 1 39  ? 10.729  19.216  -60.118  1.00 23.58  ? 31  ASN C N   1 
ATOM   3180 C  CA  . ASN C 1 39  ? 11.046  19.123  -58.710  1.00 20.86  ? 31  ASN C CA  1 
ATOM   3181 C  C   . ASN C 1 39  ? 11.832  17.833  -58.615  1.00 26.69  ? 31  ASN C C   1 
ATOM   3182 O  O   . ASN C 1 39  ? 11.536  16.905  -59.369  1.00 24.85  ? 31  ASN C O   1 
ATOM   3183 C  CB  . ASN C 1 39  ? 9.765   19.096  -57.878  1.00 24.62  ? 31  ASN C CB  1 
ATOM   3184 C  CG  . ASN C 1 39  ? 10.017  18.856  -56.422  1.00 22.68  ? 31  ASN C CG  1 
ATOM   3185 O  OD1 . ASN C 1 39  ? 10.363  17.750  -56.025  1.00 27.54  ? 31  ASN C OD1 1 
ATOM   3186 N  ND2 . ASN C 1 39  ? 9.776   19.868  -55.602  1.00 28.99  ? 31  ASN C ND2 1 
ATOM   3187 N  N   . SER C 1 40  ? 12.834  17.756  -57.733  1.00 21.64  ? 32  SER C N   1 
ATOM   3188 C  CA  . SER C 1 40  ? 13.596  16.519  -57.593  1.00 28.89  ? 32  SER C CA  1 
ATOM   3189 C  C   . SER C 1 40  ? 12.701  15.295  -57.390  1.00 22.00  ? 32  SER C C   1 
ATOM   3190 O  O   . SER C 1 40  ? 13.135  14.167  -57.653  1.00 21.66  ? 32  SER C O   1 
ATOM   3191 C  CB  . SER C 1 40  ? 14.563  16.602  -56.407  1.00 19.28  ? 32  SER C CB  1 
ATOM   3192 O  OG  . SER C 1 40  ? 13.818  16.504  -55.199  1.00 30.68  ? 32  SER C OG  1 
ATOM   3193 N  N   . GLN C 1 41  ? 11.474  15.484  -56.911  1.00 20.24  ? 33  GLN C N   1 
ATOM   3194 C  CA  . GLN C 1 41  ? 10.578  14.371  -56.644  1.00 26.81  ? 33  GLN C CA  1 
ATOM   3195 C  C   . GLN C 1 41  ? 9.316   14.366  -57.487  1.00 23.89  ? 33  GLN C C   1 
ATOM   3196 O  O   . GLN C 1 41  ? 8.457   13.500  -57.271  1.00 25.52  ? 33  GLN C O   1 
ATOM   3197 C  CB  . GLN C 1 41  ? 10.168  14.365  -55.171  1.00 23.92  ? 33  GLN C CB  1 
ATOM   3198 C  CG  . GLN C 1 41  ? 11.270  14.031  -54.223  1.00 27.93  ? 33  GLN C CG  1 
ATOM   3199 C  CD  . GLN C 1 41  ? 10.750  13.970  -52.808  1.00 30.55  ? 33  GLN C CD  1 
ATOM   3200 O  OE1 . GLN C 1 41  ? 10.291  12.927  -52.344  1.00 29.61  ? 33  GLN C OE1 1 
ATOM   3201 N  NE2 . GLN C 1 41  ? 10.788  15.105  -52.122  1.00 27.68  ? 33  GLN C NE2 1 
ATOM   3202 N  N   . TRP C 1 42  ? 9.150   15.301  -58.417  1.00 20.77  ? 34  TRP C N   1 
ATOM   3203 C  CA  . TRP C 1 42  ? 7.880   15.366  -59.122  1.00 20.08  ? 34  TRP C CA  1 
ATOM   3204 C  C   . TRP C 1 42  ? 8.086   15.526  -60.619  1.00 19.88  ? 34  TRP C C   1 
ATOM   3205 O  O   . TRP C 1 42  ? 8.916   16.319  -61.074  1.00 23.84  ? 34  TRP C O   1 
ATOM   3206 C  CB  . TRP C 1 42  ? 7.011   16.501  -58.574  1.00 21.38  ? 34  TRP C CB  1 
ATOM   3207 C  CG  . TRP C 1 42  ? 6.463   16.204  -57.205  1.00 29.59  ? 34  TRP C CG  1 
ATOM   3208 C  CD1 . TRP C 1 42  ? 7.075   16.457  -56.005  1.00 22.84  ? 34  TRP C CD1 1 
ATOM   3209 C  CD2 . TRP C 1 42  ? 5.188   15.610  -56.887  1.00 25.42  ? 34  TRP C CD2 1 
ATOM   3210 N  NE1 . TRP C 1 42  ? 6.267   16.057  -54.971  1.00 27.62  ? 34  TRP C NE1 1 
ATOM   3211 C  CE2 . TRP C 1 42  ? 5.107   15.529  -55.476  1.00 29.96  ? 34  TRP C CE2 1 
ATOM   3212 C  CE3 . TRP C 1 42  ? 4.118   15.140  -57.650  1.00 20.64  ? 34  TRP C CE3 1 
ATOM   3213 C  CZ2 . TRP C 1 42  ? 3.985   14.998  -54.808  1.00 22.98  ? 34  TRP C CZ2 1 
ATOM   3214 C  CZ3 . TRP C 1 42  ? 2.998   14.614  -56.982  1.00 30.14  ? 34  TRP C CZ3 1 
ATOM   3215 C  CH2 . TRP C 1 42  ? 2.948   14.551  -55.575  1.00 23.22  ? 34  TRP C CH2 1 
ATOM   3216 N  N   . VAL C 1 43  ? 7.308   14.769  -61.374  1.00 20.55  ? 35  VAL C N   1 
ATOM   3217 C  CA  . VAL C 1 43  ? 7.280   14.837  -62.824  1.00 15.78  ? 35  VAL C CA  1 
ATOM   3218 C  C   . VAL C 1 43  ? 5.859   15.187  -63.200  1.00 20.17  ? 35  VAL C C   1 
ATOM   3219 O  O   . VAL C 1 43  ? 4.922   14.748  -62.526  1.00 24.12  ? 35  VAL C O   1 
ATOM   3220 C  CB  . VAL C 1 43  ? 7.710   13.500  -63.456  1.00 18.72  ? 35  VAL C CB  1 
ATOM   3221 C  CG1 . VAL C 1 43  ? 7.346   13.438  -64.950  1.00 13.25  ? 35  VAL C CG1 1 
ATOM   3222 C  CG2 . VAL C 1 43  ? 9.191   13.247  -63.196  1.00 11.41  ? 35  VAL C CG2 1 
ATOM   3223 N  N   . VAL C 1 44  ? 5.685   15.991  -64.247  1.00 19.19  ? 36  VAL C N   1 
ATOM   3224 C  CA  . VAL C 1 44  ? 4.351   16.301  -64.750  1.00 19.25  ? 36  VAL C CA  1 
ATOM   3225 C  C   . VAL C 1 44  ? 4.242   15.826  -66.200  1.00 21.54  ? 36  VAL C C   1 
ATOM   3226 O  O   . VAL C 1 44  ? 5.213   15.873  -66.969  1.00 22.77  ? 36  VAL C O   1 
ATOM   3227 C  CB  . VAL C 1 44  ? 4.033   17.799  -64.601  1.00 23.29  ? 36  VAL C CB  1 
ATOM   3228 C  CG1 . VAL C 1 44  ? 5.143   18.614  -65.206  1.00 25.17  ? 36  VAL C CG1 1 
ATOM   3229 C  CG2 . VAL C 1 44  ? 2.663   18.145  -65.192  1.00 26.00  ? 36  VAL C CG2 1 
ATOM   3230 N  N   . SER C 1 45  ? 3.065   15.321  -66.556  1.00 28.58  ? 37  SER C N   1 
ATOM   3231 C  CA  . SER C 1 45  ? 2.858   14.637  -67.828  1.00 20.94  ? 37  SER C CA  1 
ATOM   3232 C  C   . SER C 1 45  ? 1.371   14.718  -68.169  1.00 22.51  ? 37  SER C C   1 
ATOM   3233 O  O   . SER C 1 45  ? 0.616   15.478  -67.548  1.00 14.64  ? 37  SER C O   1 
ATOM   3234 C  CB  . SER C 1 45  ? 3.376   13.198  -67.734  1.00 21.96  ? 37  SER C CB  1 
ATOM   3235 O  OG  . SER C 1 45  ? 3.171   12.492  -68.937  1.00 24.43  ? 37  SER C OG  1 
ATOM   3236 N  N   . ALA C 1 46  ? 0.947   13.934  -69.161  1.00 17.11  ? 38  ALA C N   1 
ATOM   3237 C  CA  . ALA C 1 46  ? -0.449  13.917  -69.573  1.00 25.08  ? 38  ALA C CA  1 
ATOM   3238 C  C   . ALA C 1 46  ? -1.203  12.854  -68.787  1.00 20.58  ? 38  ALA C C   1 
ATOM   3239 O  O   . ALA C 1 46  ? -0.678  11.764  -68.552  1.00 20.31  ? 38  ALA C O   1 
ATOM   3240 C  CB  . ALA C 1 46  ? -0.577  13.656  -71.079  1.00 18.22  ? 38  ALA C CB  1 
ATOM   3241 N  N   . ALA C 1 47  ? -2.428  13.194  -68.360  1.00 17.51  ? 39  ALA C N   1 
ATOM   3242 C  CA  . ALA C 1 47  ? -3.287  12.216  -67.685  1.00 22.52  ? 39  ALA C CA  1 
ATOM   3243 C  C   . ALA C 1 47  ? -3.556  11.000  -68.567  1.00 17.11  ? 39  ALA C C   1 
ATOM   3244 O  O   . ALA C 1 47  ? -3.658  9.882   -68.065  1.00 20.78  ? 39  ALA C O   1 
ATOM   3245 C  CB  . ALA C 1 47  ? -4.618  12.853  -67.260  1.00 12.37  ? 39  ALA C CB  1 
ATOM   3246 N  N   . HIS C 1 48  ? -3.679  11.195  -69.884  1.00 23.09  ? 40  HIS C N   1 
ATOM   3247 C  CA  . HIS C 1 48  ? -3.919  10.056  -70.762  1.00 21.76  ? 40  HIS C CA  1 
ATOM   3248 C  C   . HIS C 1 48  ? -2.713  9.118   -70.837  1.00 23.80  ? 40  HIS C C   1 
ATOM   3249 O  O   . HIS C 1 48  ? -2.806  8.047   -71.448  1.00 22.37  ? 40  HIS C O   1 
ATOM   3250 C  CB  . HIS C 1 48  ? -4.355  10.539  -72.160  1.00 23.89  ? 40  HIS C CB  1 
ATOM   3251 C  CG  . HIS C 1 48  ? -3.227  10.929  -73.068  1.00 26.61  ? 40  HIS C CG  1 
ATOM   3252 N  ND1 . HIS C 1 48  ? -2.924  12.242  -73.361  1.00 22.81  ? 40  HIS C ND1 1 
ATOM   3253 C  CD2 . HIS C 1 48  ? -2.340  10.178  -73.766  1.00 20.75  ? 40  HIS C CD2 1 
ATOM   3254 C  CE1 . HIS C 1 48  ? -1.892  12.288  -74.185  1.00 16.30  ? 40  HIS C CE1 1 
ATOM   3255 N  NE2 . HIS C 1 48  ? -1.521  11.049  -74.452  1.00 24.33  ? 40  HIS C NE2 1 
ATOM   3256 N  N   . CYS C 1 49  ? -1.601  9.473   -70.209  1.00 18.30  ? 41  CYS C N   1 
ATOM   3257 C  CA  . CYS C 1 49  ? -0.480  8.562   -70.048  1.00 21.03  ? 41  CYS C CA  1 
ATOM   3258 C  C   . CYS C 1 49  ? -0.597  7.706   -68.794  1.00 22.19  ? 41  CYS C C   1 
ATOM   3259 O  O   . CYS C 1 49  ? 0.377   7.034   -68.437  1.00 23.49  ? 41  CYS C O   1 
ATOM   3260 C  CB  . CYS C 1 49  ? 0.843   9.343   -69.991  1.00 23.08  ? 41  CYS C CB  1 
ATOM   3261 S  SG  . CYS C 1 49  ? 1.359   10.158  -71.546  1.00 31.22  ? 41  CYS C SG  1 
ATOM   3262 N  N   . TYR C 1 50  ? -1.733  7.736   -68.093  1.00 17.24  ? 42  TYR C N   1 
ATOM   3263 C  CA  . TYR C 1 50  ? -1.788  7.041   -66.812  1.00 20.07  ? 42  TYR C CA  1 
ATOM   3264 C  C   . TYR C 1 50  ? -1.576  5.533   -67.010  1.00 25.03  ? 42  TYR C C   1 
ATOM   3265 O  O   . TYR C 1 50  ? -2.094  4.926   -67.954  1.00 22.66  ? 42  TYR C O   1 
ATOM   3266 C  CB  . TYR C 1 50  ? -3.121  7.297   -66.087  1.00 25.05  ? 42  TYR C CB  1 
ATOM   3267 C  CG  . TYR C 1 50  ? -3.260  6.408   -64.869  1.00 28.90  ? 42  TYR C CG  1 
ATOM   3268 C  CD1 . TYR C 1 50  ? -2.779  6.821   -63.638  1.00 23.09  ? 42  TYR C CD1 1 
ATOM   3269 C  CD2 . TYR C 1 50  ? -3.800  5.121   -64.966  1.00 30.01  ? 42  TYR C CD2 1 
ATOM   3270 C  CE1 . TYR C 1 50  ? -2.847  6.015   -62.532  1.00 25.76  ? 42  TYR C CE1 1 
ATOM   3271 C  CE2 . TYR C 1 50  ? -3.860  4.277   -63.846  1.00 25.29  ? 42  TYR C CE2 1 
ATOM   3272 C  CZ  . TYR C 1 50  ? -3.390  4.740   -62.632  1.00 31.71  ? 42  TYR C CZ  1 
ATOM   3273 O  OH  . TYR C 1 50  ? -3.463  3.944   -61.510  1.00 28.42  ? 42  TYR C OH  1 
ATOM   3274 N  N   . LYS C 1 51  ? -0.780  4.940   -66.125  1.00 23.31  ? 43  LYS C N   1 
ATOM   3275 C  CA  . LYS C 1 51  ? -0.652  3.499   -65.986  1.00 24.77  ? 43  LYS C CA  1 
ATOM   3276 C  C   . LYS C 1 51  ? -0.445  3.222   -64.504  1.00 25.83  ? 43  LYS C C   1 
ATOM   3277 O  O   . LYS C 1 51  ? 0.134   4.042   -63.789  1.00 29.48  ? 43  LYS C O   1 
ATOM   3278 C  CB  . LYS C 1 51  ? 0.515   2.930   -66.828  1.00 15.96  ? 43  LYS C CB  1 
ATOM   3279 C  CG  . LYS C 1 51  ? 0.127   2.628   -68.244  1.00 20.50  ? 43  LYS C CG  1 
ATOM   3280 C  CD  . LYS C 1 51  ? 1.301   2.403   -69.145  1.00 25.20  ? 43  LYS C CD  1 
ATOM   3281 C  CE  . LYS C 1 51  ? 0.899   2.656   -70.567  1.00 21.11  ? 43  LYS C CE  1 
ATOM   3282 N  NZ  . LYS C 1 51  ? 1.840   2.036   -71.523  1.00 27.89  ? 43  LYS C NZ  1 
ATOM   3283 N  N   . SER C 1 52  ? -0.947  2.075   -64.045  1.00 23.88  ? 44  SER C N   1 
ATOM   3284 C  CA  . SER C 1 52  ? -0.880  1.723   -62.627  1.00 30.88  ? 44  SER C CA  1 
ATOM   3285 C  C   . SER C 1 52  ? 0.565   1.613   -62.117  1.00 27.79  ? 44  SER C C   1 
ATOM   3286 O  O   . SER C 1 52  ? 0.842   1.932   -60.954  1.00 23.17  ? 44  SER C O   1 
ATOM   3287 C  CB  . SER C 1 52  ? -1.670  0.425   -62.400  1.00 24.28  ? 44  SER C CB  1 
ATOM   3288 O  OG  . SER C 1 52  ? -0.958  -0.715  -62.858  1.00 36.68  ? 44  SER C OG  1 
ATOM   3289 N  N   . ARG C 1 53  ? 1.496   1.193   -62.968  1.00 28.02  ? 45  ARG C N   1 
ATOM   3290 C  CA  . ARG C 1 53  ? 2.919   1.198   -62.664  1.00 25.63  ? 45  ARG C CA  1 
ATOM   3291 C  C   . ARG C 1 53  ? 3.649   1.962   -63.762  1.00 25.45  ? 45  ARG C C   1 
ATOM   3292 O  O   . ARG C 1 53  ? 3.409   1.736   -64.956  1.00 20.34  ? 45  ARG C O   1 
ATOM   3293 C  CB  . ARG C 1 53  ? 3.495   -0.227  -62.551  1.00 29.10  ? 45  ARG C CB  1 
ATOM   3294 C  CG  . ARG C 1 53  ? 2.901   -1.114  -61.441  1.00 51.78  ? 45  ARG C CG  1 
ATOM   3295 C  CD  . ARG C 1 53  ? 3.347   -2.580  -61.620  1.00 53.73  ? 45  ARG C CD  1 
ATOM   3296 N  NE  . ARG C 1 53  ? 2.594   -3.518  -60.789  1.00 69.65  ? 45  ARG C NE  1 
ATOM   3297 C  CZ  . ARG C 1 53  ? 1.587   -4.267  -61.229  1.00 69.80  ? 45  ARG C CZ  1 
ATOM   3298 N  NH1 . ARG C 1 53  ? 1.179   -4.211  -62.489  1.00 63.70  ? 45  ARG C NH1 1 
ATOM   3299 N  NH2 . ARG C 1 53  ? 0.965   -5.086  -60.380  1.00 61.97  ? 45  ARG C NH2 1 
ATOM   3300 N  N   . ILE C 1 54  ? 4.559   2.840   -63.355  1.00 20.50  ? 46  ILE C N   1 
ATOM   3301 C  CA  . ILE C 1 54  ? 5.349   3.660   -64.260  1.00 19.53  ? 46  ILE C CA  1 
ATOM   3302 C  C   . ILE C 1 54  ? 6.766   3.737   -63.719  1.00 22.40  ? 46  ILE C C   1 
ATOM   3303 O  O   . ILE C 1 54  ? 6.971   4.078   -62.547  1.00 19.28  ? 46  ILE C O   1 
ATOM   3304 C  CB  . ILE C 1 54  ? 4.775   5.087   -64.425  1.00 20.54  ? 46  ILE C CB  1 
ATOM   3305 C  CG1 . ILE C 1 54  ? 3.451   5.054   -65.221  1.00 22.31  ? 46  ILE C CG1 1 
ATOM   3306 C  CG2 . ILE C 1 54  ? 5.810   5.990   -65.110  1.00 14.61  ? 46  ILE C CG2 1 
ATOM   3307 C  CD1 . ILE C 1 54  ? 2.642   6.370   -65.190  1.00 19.45  ? 46  ILE C CD1 1 
ATOM   3308 N  N   . GLN C 1 55  ? 7.740   3.424   -64.571  1.00 13.78  ? 47  GLN C N   1 
ATOM   3309 C  CA  . GLN C 1 55  ? 9.140   3.701   -64.299  1.00 23.94  ? 47  GLN C CA  1 
ATOM   3310 C  C   . GLN C 1 55  ? 9.539   5.004   -64.992  1.00 26.03  ? 47  GLN C C   1 
ATOM   3311 O  O   . GLN C 1 55  ? 9.484   5.097   -66.227  1.00 22.71  ? 47  GLN C O   1 
ATOM   3312 C  CB  . GLN C 1 55  ? 10.039  2.571   -64.779  1.00 15.57  ? 47  GLN C CB  1 
ATOM   3313 C  CG  . GLN C 1 55  ? 11.459  2.777   -64.290  1.00 23.82  ? 47  GLN C CG  1 
ATOM   3314 C  CD  . GLN C 1 55  ? 12.400  1.724   -64.802  1.00 30.55  ? 47  GLN C CD  1 
ATOM   3315 O  OE1 . GLN C 1 55  ? 12.696  1.657   -66.006  1.00 25.62  ? 47  GLN C OE1 1 
ATOM   3316 N  NE2 . GLN C 1 55  ? 12.846  0.856   -63.899  1.00 25.28  ? 47  GLN C NE2 1 
ATOM   3317 N  N   . VAL C 1 56  ? 9.952   5.997   -64.204  1.00 22.05  ? 48  VAL C N   1 
ATOM   3318 C  CA  . VAL C 1 56  ? 10.455  7.254   -64.755  1.00 20.80  ? 48  VAL C CA  1 
ATOM   3319 C  C   . VAL C 1 56  ? 11.939  7.096   -65.075  1.00 24.44  ? 48  VAL C C   1 
ATOM   3320 O  O   . VAL C 1 56  ? 12.723  6.600   -64.253  1.00 26.57  ? 48  VAL C O   1 
ATOM   3321 C  CB  . VAL C 1 56  ? 10.194  8.418   -63.782  1.00 19.17  ? 48  VAL C CB  1 
ATOM   3322 C  CG1 . VAL C 1 56  ? 10.749  9.769   -64.337  1.00 24.87  ? 48  VAL C CG1 1 
ATOM   3323 C  CG2 . VAL C 1 56  ? 8.692   8.526   -63.529  1.00 21.48  ? 48  VAL C CG2 1 
ATOM   3324 N  N   . ARG C 1 57  ? 12.329  7.500   -66.278  1.00 19.49  ? 49  ARG C N   1 
ATOM   3325 C  CA  . ARG C 1 57  ? 13.723  7.452   -66.692  1.00 22.64  ? 49  ARG C CA  1 
ATOM   3326 C  C   . ARG C 1 57  ? 14.215  8.868   -66.946  1.00 19.59  ? 49  ARG C C   1 
ATOM   3327 O  O   . ARG C 1 57  ? 13.699  9.563   -67.827  1.00 23.80  ? 49  ARG C O   1 
ATOM   3328 C  CB  . ARG C 1 57  ? 13.891  6.571   -67.921  1.00 15.21  ? 49  ARG C CB  1 
ATOM   3329 C  CG  . ARG C 1 57  ? 13.351  5.194   -67.668  1.00 19.68  ? 49  ARG C CG  1 
ATOM   3330 C  CD  . ARG C 1 57  ? 13.804  4.201   -68.710  1.00 21.30  ? 49  ARG C CD  1 
ATOM   3331 N  NE  . ARG C 1 57  ? 13.689  2.828   -68.238  1.00 26.24  ? 49  ARG C NE  1 
ATOM   3332 C  CZ  . ARG C 1 57  ? 14.045  1.772   -68.950  1.00 24.38  ? 49  ARG C CZ  1 
ATOM   3333 N  NH1 . ARG C 1 57  ? 14.532  1.900   -70.177  1.00 24.55  ? 49  ARG C NH1 1 
ATOM   3334 N  NH2 . ARG C 1 57  ? 13.932  0.560   -68.413  1.00 22.76  ? 49  ARG C NH2 1 
ATOM   3335 N  N   . LEU C 1 58  ? 15.206  9.279   -66.166  1.00 23.38  ? 50  LEU C N   1 
ATOM   3336 C  CA  . LEU C 1 58  ? 15.792  10.606  -66.163  1.00 19.69  ? 50  LEU C CA  1 
ATOM   3337 C  C   . LEU C 1 58  ? 17.206  10.566  -66.742  1.00 22.38  ? 50  LEU C C   1 
ATOM   3338 O  O   . LEU C 1 58  ? 17.887  9.531   -66.727  1.00 23.92  ? 50  LEU C O   1 
ATOM   3339 C  CB  . LEU C 1 58  ? 15.803  11.155  -64.732  1.00 20.98  ? 50  LEU C CB  1 
ATOM   3340 C  CG  . LEU C 1 58  ? 14.433  11.171  -64.053  1.00 22.99  ? 50  LEU C CG  1 
ATOM   3341 C  CD1 . LEU C 1 58  ? 14.419  10.274  -62.834  1.00 22.36  ? 50  LEU C CD1 1 
ATOM   3342 C  CD2 . LEU C 1 58  ? 14.066  12.588  -63.657  1.00 25.95  ? 50  LEU C CD2 1 
ATOM   3343 N  N   . GLY C 1 59  ? 17.641  11.712  -67.266  1.00 22.62  ? 51  GLY C N   1 
ATOM   3344 C  CA  . GLY C 1 59  ? 18.946  11.785  -67.908  1.00 22.13  ? 51  GLY C CA  1 
ATOM   3345 C  C   . GLY C 1 59  ? 19.057  10.997  -69.199  1.00 26.86  ? 51  GLY C C   1 
ATOM   3346 O  O   . GLY C 1 59  ? 20.166  10.655  -69.616  1.00 31.73  ? 51  GLY C O   1 
ATOM   3347 N  N   . GLU C 1 60  ? 17.932  10.696  -69.848  1.00 31.88  ? 52  GLU C N   1 
ATOM   3348 C  CA  . GLU C 1 60  ? 17.949  9.903   -71.070  1.00 31.70  ? 52  GLU C CA  1 
ATOM   3349 C  C   . GLU C 1 60  ? 18.251  10.759  -72.282  1.00 24.66  ? 52  GLU C C   1 
ATOM   3350 O  O   . GLU C 1 60  ? 17.843  11.915  -72.364  1.00 30.89  ? 52  GLU C O   1 
ATOM   3351 C  CB  . GLU C 1 60  ? 16.614  9.197   -71.292  1.00 29.56  ? 52  GLU C CB  1 
ATOM   3352 C  CG  . GLU C 1 60  ? 16.426  8.001   -70.397  1.00 32.10  ? 52  GLU C CG  1 
ATOM   3353 C  CD  . GLU C 1 60  ? 16.990  6.742   -71.030  1.00 34.66  ? 52  GLU C CD  1 
ATOM   3354 O  OE1 . GLU C 1 60  ? 16.477  5.641   -70.744  1.00 41.18  ? 52  GLU C OE1 1 
ATOM   3355 O  OE2 . GLU C 1 60  ? 17.959  6.852   -71.809  1.00 33.53  ? 52  GLU C OE2 1 
ATOM   3356 N  N   . HIS C 1 61  ? 18.954  10.171  -73.237  1.00 30.83  ? 53  HIS C N   1 
ATOM   3357 C  CA  . HIS C 1 61  ? 19.149  10.816  -74.522  1.00 35.11  ? 53  HIS C CA  1 
ATOM   3358 C  C   . HIS C 1 61  ? 18.964  9.751   -75.597  1.00 32.65  ? 53  HIS C C   1 
ATOM   3359 O  O   . HIS C 1 61  ? 18.326  9.993   -76.630  1.00 28.17  ? 53  HIS C O   1 
ATOM   3360 C  CB  . HIS C 1 61  ? 20.524  11.502  -74.573  1.00 35.24  ? 53  HIS C CB  1 
ATOM   3361 C  CG  . HIS C 1 61  ? 20.909  11.985  -75.934  1.00 45.08  ? 53  HIS C CG  1 
ATOM   3362 N  ND1 . HIS C 1 61  ? 21.932  11.416  -76.662  1.00 53.88  ? 53  HIS C ND1 1 
ATOM   3363 C  CD2 . HIS C 1 61  ? 20.378  12.953  -76.720  1.00 46.73  ? 53  HIS C CD2 1 
ATOM   3364 C  CE1 . HIS C 1 61  ? 22.034  12.031  -77.827  1.00 57.78  ? 53  HIS C CE1 1 
ATOM   3365 N  NE2 . HIS C 1 61  ? 21.099  12.965  -77.890  1.00 55.41  ? 53  HIS C NE2 1 
ATOM   3366 N  N   . ASN C 1 62  ? 19.495  8.558   -75.336  1.00 30.90  ? 54  ASN C N   1 
ATOM   3367 C  CA  . ASN C 1 62  ? 19.227  7.359   -76.122  1.00 28.52  ? 54  ASN C CA  1 
ATOM   3368 C  C   . ASN C 1 62  ? 18.324  6.452   -75.300  1.00 28.56  ? 54  ASN C C   1 
ATOM   3369 O  O   . ASN C 1 62  ? 18.788  5.788   -74.371  1.00 30.35  ? 54  ASN C O   1 
ATOM   3370 C  CB  . ASN C 1 62  ? 20.511  6.617   -76.488  1.00 23.31  ? 54  ASN C CB  1 
ATOM   3371 C  CG  . ASN C 1 62  ? 20.306  5.653   -77.651  1.00 31.34  ? 54  ASN C CG  1 
ATOM   3372 O  OD1 . ASN C 1 62  ? 19.297  4.946   -77.711  1.00 32.62  ? 54  ASN C OD1 1 
ATOM   3373 N  ND2 . ASN C 1 62  ? 21.272  5.596   -78.560  1.00 29.24  ? 54  ASN C ND2 1 
ATOM   3374 N  N   . ILE C 1 63  ? 17.039  6.390   -75.638  1.00 21.25  ? 55  ILE C N   1 
ATOM   3375 C  CA  . ILE C 1 63  ? 16.202  5.515   -74.839  1.00 25.58  ? 55  ILE C CA  1 
ATOM   3376 C  C   . ILE C 1 63  ? 16.515  4.045   -75.088  1.00 32.50  ? 55  ILE C C   1 
ATOM   3377 O  O   . ILE C 1 63  ? 16.047  3.189   -74.333  1.00 29.87  ? 55  ILE C O   1 
ATOM   3378 C  CB  . ILE C 1 63  ? 14.708  5.792   -75.077  1.00 28.16  ? 55  ILE C CB  1 
ATOM   3379 C  CG1 . ILE C 1 63  ? 14.434  5.993   -76.562  1.00 31.61  ? 55  ILE C CG1 1 
ATOM   3380 C  CG2 . ILE C 1 63  ? 14.255  7.001   -74.251  1.00 29.56  ? 55  ILE C CG2 1 
ATOM   3381 C  CD1 . ILE C 1 63  ? 13.009  5.733   -76.938  1.00 31.86  ? 55  ILE C CD1 1 
ATOM   3382 N  N   . ASP C 1 64  ? 17.328  3.723   -76.096  1.00 26.01  ? 56  ASP C N   1 
ATOM   3383 C  CA  . ASP C 1 64  ? 17.582  2.329   -76.435  1.00 25.51  ? 56  ASP C CA  1 
ATOM   3384 C  C   . ASP C 1 64  ? 18.904  1.792   -75.914  1.00 27.86  ? 56  ASP C C   1 
ATOM   3385 O  O   . ASP C 1 64  ? 19.138  0.582   -75.992  1.00 23.51  ? 56  ASP C O   1 
ATOM   3386 C  CB  . ASP C 1 64  ? 17.524  2.152   -77.947  1.00 25.64  ? 56  ASP C CB  1 
ATOM   3387 C  CG  . ASP C 1 64  ? 16.103  2.189   -78.455  1.00 40.57  ? 56  ASP C CG  1 
ATOM   3388 O  OD1 . ASP C 1 64  ? 15.246  1.534   -77.809  1.00 41.35  ? 56  ASP C OD1 1 
ATOM   3389 O  OD2 . ASP C 1 64  ? 15.841  2.896   -79.459  1.00 36.38  ? 56  ASP C OD2 1 
ATOM   3390 N  N   . VAL C 1 65  ? 19.765  2.641   -75.370  1.00 27.80  ? 57  VAL C N   1 
ATOM   3391 C  CA  . VAL C 1 65  ? 21.093  2.224   -74.947  1.00 34.68  ? 57  VAL C CA  1 
ATOM   3392 C  C   . VAL C 1 65  ? 21.330  2.767   -73.548  1.00 29.14  ? 57  VAL C C   1 
ATOM   3393 O  O   . VAL C 1 65  ? 21.095  3.951   -73.296  1.00 27.35  ? 57  VAL C O   1 
ATOM   3394 C  CB  . VAL C 1 65  ? 22.176  2.727   -75.922  1.00 26.83  ? 57  VAL C CB  1 
ATOM   3395 C  CG1 . VAL C 1 65  ? 23.544  2.276   -75.470  1.00 28.26  ? 57  VAL C CG1 1 
ATOM   3396 C  CG2 . VAL C 1 65  ? 21.863  2.271   -77.332  1.00 23.70  ? 57  VAL C CG2 1 
ATOM   3397 N  N   . LEU C 1 66  ? 21.790  1.914   -72.642  1.00 21.20  ? 58  LEU C N   1 
ATOM   3398 C  CA  . LEU C 1 66  ? 22.096  2.371   -71.289  1.00 28.35  ? 58  LEU C CA  1 
ATOM   3399 C  C   . LEU C 1 66  ? 23.489  3.004   -71.283  1.00 32.54  ? 58  LEU C C   1 
ATOM   3400 O  O   . LEU C 1 66  ? 24.505  2.310   -71.205  1.00 30.95  ? 58  LEU C O   1 
ATOM   3401 C  CB  . LEU C 1 66  ? 21.989  1.224   -70.290  1.00 25.56  ? 58  LEU C CB  1 
ATOM   3402 C  CG  . LEU C 1 66  ? 21.920  1.735   -68.847  1.00 32.19  ? 58  LEU C CG  1 
ATOM   3403 C  CD1 . LEU C 1 66  ? 20.584  2.398   -68.576  1.00 34.82  ? 58  LEU C CD1 1 
ATOM   3404 C  CD2 . LEU C 1 66  ? 22.171  0.621   -67.866  1.00 39.18  ? 58  LEU C CD2 1 
ATOM   3405 N  N   . GLU C 1 67  ? 23.536  4.336   -71.372  1.00 27.11  ? 59  GLU C N   1 
ATOM   3406 C  CA  . GLU C 1 67  ? 24.809  5.039   -71.320  1.00 27.76  ? 59  GLU C CA  1 
ATOM   3407 C  C   . GLU C 1 67  ? 25.475  4.871   -69.955  1.00 33.36  ? 59  GLU C C   1 
ATOM   3408 O  O   . GLU C 1 67  ? 26.696  4.659   -69.865  1.00 25.41  ? 59  GLU C O   1 
ATOM   3409 C  CB  . GLU C 1 67  ? 24.589  6.515   -71.637  1.00 33.96  ? 59  GLU C CB  1 
ATOM   3410 C  CG  . GLU C 1 67  ? 25.572  7.445   -70.944  1.00 47.27  ? 59  GLU C CG  1 
ATOM   3411 C  CD  . GLU C 1 67  ? 25.654  8.814   -71.595  1.00 57.50  ? 59  GLU C CD  1 
ATOM   3412 O  OE1 . GLU C 1 67  ? 25.356  8.922   -72.805  1.00 66.84  ? 59  GLU C OE1 1 
ATOM   3413 O  OE2 . GLU C 1 67  ? 26.007  9.787   -70.886  1.00 80.52  ? 59  GLU C OE2 1 
ATOM   3414 N  N   . GLY C 1 68  ? 24.693  4.955   -68.884  1.00 33.32  ? 60  GLY C N   1 
ATOM   3415 C  CA  . GLY C 1 68  ? 25.198  4.775   -67.534  1.00 35.68  ? 60  GLY C CA  1 
ATOM   3416 C  C   . GLY C 1 68  ? 24.989  5.955   -66.609  1.00 37.72  ? 60  GLY C C   1 
ATOM   3417 O  O   . GLY C 1 68  ? 25.224  5.814   -65.401  1.00 38.42  ? 60  GLY C O   1 
ATOM   3418 N  N   . ASN C 1 69  ? 24.570  7.113   -67.121  1.00 41.99  ? 61  ASN C N   1 
ATOM   3419 C  CA  . ASN C 1 69  ? 24.241  8.289   -66.325  1.00 39.05  ? 61  ASN C CA  1 
ATOM   3420 C  C   . ASN C 1 69  ? 22.764  8.377   -65.972  1.00 35.57  ? 61  ASN C C   1 
ATOM   3421 O  O   . ASN C 1 69  ? 22.369  9.314   -65.270  1.00 34.48  ? 61  ASN C O   1 
ATOM   3422 C  CB  . ASN C 1 69  ? 24.630  9.570   -67.084  1.00 54.90  ? 61  ASN C CB  1 
ATOM   3423 C  CG  . ASN C 1 69  ? 23.695  9.859   -68.270  1.00 65.40  ? 61  ASN C CG  1 
ATOM   3424 O  OD1 . ASN C 1 69  ? 23.451  8.981   -69.106  1.00 53.72  ? 61  ASN C OD1 1 
ATOM   3425 N  ND2 . ASN C 1 69  ? 23.165  11.089  -68.339  1.00 58.53  ? 61  ASN C ND2 1 
ATOM   3426 N  N   . GLU C 1 70  ? 21.937  7.472   -66.494  1.00 28.35  ? 62  GLU C N   1 
ATOM   3427 C  CA  . GLU C 1 70  ? 20.493  7.591   -66.359  1.00 30.28  ? 62  GLU C CA  1 
ATOM   3428 C  C   . GLU C 1 70  ? 20.074  7.277   -64.931  1.00 26.94  ? 62  GLU C C   1 
ATOM   3429 O  O   . GLU C 1 70  ? 20.777  6.574   -64.200  1.00 29.11  ? 62  GLU C O   1 
ATOM   3430 C  CB  . GLU C 1 70  ? 19.800  6.643   -67.344  1.00 30.18  ? 62  GLU C CB  1 
ATOM   3431 C  CG  . GLU C 1 70  ? 20.126  6.958   -68.789  1.00 31.71  ? 62  GLU C CG  1 
ATOM   3432 C  CD  . GLU C 1 70  ? 21.169  6.005   -69.358  1.00 37.57  ? 62  GLU C CD  1 
ATOM   3433 O  OE1 . GLU C 1 70  ? 22.004  5.500   -68.574  1.00 37.02  ? 62  GLU C OE1 1 
ATOM   3434 O  OE2 . GLU C 1 70  ? 21.229  5.835   -70.589  1.00 26.82  ? 62  GLU C OE2 1 
ATOM   3435 N  N   . GLN C 1 71  ? 18.919  7.806   -64.527  1.00 21.14  ? 63  GLN C N   1 
ATOM   3436 C  CA  . GLN C 1 71  ? 18.297  7.418   -63.264  1.00 27.56  ? 63  GLN C CA  1 
ATOM   3437 C  C   . GLN C 1 71  ? 16.910  6.844   -63.523  1.00 27.35  ? 63  GLN C C   1 
ATOM   3438 O  O   . GLN C 1 71  ? 16.033  7.545   -64.041  1.00 24.92  ? 63  GLN C O   1 
ATOM   3439 C  CB  . GLN C 1 71  ? 18.200  8.593   -62.298  1.00 22.11  ? 63  GLN C CB  1 
ATOM   3440 C  CG  . GLN C 1 71  ? 19.505  8.977   -61.692  1.00 19.20  ? 63  GLN C CG  1 
ATOM   3441 C  CD  . GLN C 1 71  ? 19.410  10.312  -61.030  1.00 26.36  ? 63  GLN C CD  1 
ATOM   3442 O  OE1 . GLN C 1 71  ? 18.589  10.508  -60.129  1.00 27.87  ? 63  GLN C OE1 1 
ATOM   3443 N  NE2 . GLN C 1 71  ? 20.210  11.266  -61.500  1.00 31.81  ? 63  GLN C NE2 1 
ATOM   3444 N  N   . PHE C 1 72  ? 16.712  5.581   -63.143  1.00 19.04  ? 64  PHE C N   1 
ATOM   3445 C  CA  . PHE C 1 72  ? 15.424  4.909   -63.268  1.00 20.59  ? 64  PHE C CA  1 
ATOM   3446 C  C   . PHE C 1 72  ? 14.787  4.879   -61.889  1.00 25.76  ? 64  PHE C C   1 
ATOM   3447 O  O   . PHE C 1 72  ? 15.297  4.220   -60.974  1.00 27.10  ? 64  PHE C O   1 
ATOM   3448 C  CB  . PHE C 1 72  ? 15.577  3.494   -63.825  1.00 20.12  ? 64  PHE C CB  1 
ATOM   3449 C  CG  . PHE C 1 72  ? 16.178  3.439   -65.205  1.00 23.59  ? 64  PHE C CG  1 
ATOM   3450 C  CD1 . PHE C 1 72  ? 16.399  4.603   -65.939  1.00 26.77  ? 64  PHE C CD1 1 
ATOM   3451 C  CD2 . PHE C 1 72  ? 16.533  2.215   -65.768  1.00 26.23  ? 64  PHE C CD2 1 
ATOM   3452 C  CE1 . PHE C 1 72  ? 16.975  4.549   -67.223  1.00 27.72  ? 64  PHE C CE1 1 
ATOM   3453 C  CE2 . PHE C 1 72  ? 17.095  2.144   -67.036  1.00 32.50  ? 64  PHE C CE2 1 
ATOM   3454 C  CZ  . PHE C 1 72  ? 17.320  3.324   -67.771  1.00 31.27  ? 64  PHE C CZ  1 
ATOM   3455 N  N   . ILE C 1 73  ? 13.680  5.594   -61.731  1.00 26.99  ? 65  ILE C N   1 
ATOM   3456 C  CA  . ILE C 1 73  ? 12.997  5.677   -60.445  1.00 19.68  ? 65  ILE C CA  1 
ATOM   3457 C  C   . ILE C 1 73  ? 11.523  5.383   -60.652  1.00 19.15  ? 65  ILE C C   1 
ATOM   3458 O  O   . ILE C 1 73  ? 10.853  6.043   -61.458  1.00 20.89  ? 65  ILE C O   1 
ATOM   3459 C  CB  . ILE C 1 73  ? 13.194  7.046   -59.770  1.00 17.00  ? 65  ILE C CB  1 
ATOM   3460 C  CG1 . ILE C 1 73  ? 14.696  7.314   -59.542  1.00 21.63  ? 65  ILE C CG1 1 
ATOM   3461 C  CG2 . ILE C 1 73  ? 12.397  7.104   -58.489  1.00 16.49  ? 65  ILE C CG2 1 
ATOM   3462 C  CD1 . ILE C 1 73  ? 15.074  8.767   -59.197  1.00 16.32  ? 65  ILE C CD1 1 
ATOM   3463 N  N   . ASN C 1 74  ? 11.022  4.384   -59.940  1.00 20.58  ? 66  ASN C N   1 
ATOM   3464 C  CA  . ASN C 1 74  ? 9.625   4.025   -60.100  1.00 24.07  ? 66  ASN C CA  1 
ATOM   3465 C  C   . ASN C 1 74  ? 8.742   5.132   -59.530  1.00 26.24  ? 66  ASN C C   1 
ATOM   3466 O  O   . ASN C 1 74  ? 9.154   5.886   -58.644  1.00 23.90  ? 66  ASN C O   1 
ATOM   3467 C  CB  . ASN C 1 74  ? 9.326   2.681   -59.431  1.00 24.02  ? 66  ASN C CB  1 
ATOM   3468 C  CG  . ASN C 1 74  ? 10.171  1.521   -60.000  1.00 39.61  ? 66  ASN C CG  1 
ATOM   3469 O  OD1 . ASN C 1 74  ? 10.561  1.513   -61.183  1.00 36.54  ? 66  ASN C OD1 1 
ATOM   3470 N  ND2 . ASN C 1 74  ? 10.391  0.502   -59.168  1.00 35.17  ? 66  ASN C ND2 1 
ATOM   3471 N  N   . ALA C 1 75  ? 7.542   5.266   -60.095  1.00 25.46  ? 67  ALA C N   1 
ATOM   3472 C  CA  . ALA C 1 75  ? 6.542   6.160   -59.531  1.00 20.77  ? 67  ALA C CA  1 
ATOM   3473 C  C   . ALA C 1 75  ? 6.007   5.592   -58.222  1.00 31.56  ? 67  ALA C C   1 
ATOM   3474 O  O   . ALA C 1 75  ? 5.563   4.440   -58.163  1.00 31.77  ? 67  ALA C O   1 
ATOM   3475 C  CB  . ALA C 1 75  ? 5.392   6.367   -60.510  1.00 13.75  ? 67  ALA C CB  1 
ATOM   3476 N  N   . ALA C 1 76  ? 6.062   6.396   -57.164  1.00 32.50  ? 68  ALA C N   1 
ATOM   3477 C  CA  . ALA C 1 76  ? 5.389   6.049   -55.919  1.00 28.20  ? 68  ALA C CA  1 
ATOM   3478 C  C   . ALA C 1 76  ? 3.976   6.618   -55.843  1.00 21.50  ? 68  ALA C C   1 
ATOM   3479 O  O   . ALA C 1 76  ? 3.144   6.082   -55.113  1.00 30.16  ? 68  ALA C O   1 
ATOM   3480 C  CB  . ALA C 1 76  ? 6.213   6.538   -54.724  1.00 17.26  ? 68  ALA C CB  1 
ATOM   3481 N  N   . LYS C 1 77  ? 3.677   7.676   -56.593  1.00 30.45  ? 69  LYS C N   1 
ATOM   3482 C  CA  . LYS C 1 77  ? 2.369   8.317   -56.546  1.00 23.04  ? 69  LYS C CA  1 
ATOM   3483 C  C   . LYS C 1 77  ? 2.047   8.811   -57.945  1.00 26.58  ? 69  LYS C C   1 
ATOM   3484 O  O   . LYS C 1 77  ? 2.883   9.473   -58.573  1.00 28.14  ? 69  LYS C O   1 
ATOM   3485 C  CB  . LYS C 1 77  ? 2.359   9.487   -55.557  1.00 22.89  ? 69  LYS C CB  1 
ATOM   3486 C  CG  . LYS C 1 77  ? 2.356   9.060   -54.091  1.00 25.91  ? 69  LYS C CG  1 
ATOM   3487 C  CD  . LYS C 1 77  ? 2.555   10.270  -53.178  1.00 27.57  ? 69  LYS C CD  1 
ATOM   3488 C  CE  . LYS C 1 77  ? 2.512   9.870   -51.718  1.00 29.67  ? 69  LYS C CE  1 
ATOM   3489 N  NZ  . LYS C 1 77  ? 3.046   10.964  -50.837  1.00 37.19  ? 69  LYS C NZ  1 
ATOM   3490 N  N   . ILE C 1 78  ? 0.854   8.478   -58.433  1.00 22.27  ? 70  ILE C N   1 
ATOM   3491 C  CA  . ILE C 1 78  ? 0.390   8.884   -59.757  1.00 23.10  ? 70  ILE C CA  1 
ATOM   3492 C  C   . ILE C 1 78  ? -0.976  9.555   -59.619  1.00 19.09  ? 70  ILE C C   1 
ATOM   3493 O  O   . ILE C 1 78  ? -2.004  8.881   -59.535  1.00 37.01  ? 70  ILE C O   1 
ATOM   3494 C  CB  . ILE C 1 78  ? 0.344   7.711   -60.733  1.00 22.71  ? 70  ILE C CB  1 
ATOM   3495 C  CG1 . ILE C 1 78  ? 1.714   7.019   -60.778  1.00 26.22  ? 70  ILE C CG1 1 
ATOM   3496 C  CG2 . ILE C 1 78  ? -0.063  8.190   -62.093  1.00 23.13  ? 70  ILE C CG2 1 
ATOM   3497 C  CD1 . ILE C 1 78  ? 1.695   5.627   -61.445  1.00 23.82  ? 70  ILE C CD1 1 
ATOM   3498 N  N   . ILE C 1 79  ? -0.995  10.883  -59.652  1.00 25.01  ? 71  ILE C N   1 
ATOM   3499 C  CA  . ILE C 1 79  ? -2.181  11.678  -59.373  1.00 26.80  ? 71  ILE C CA  1 
ATOM   3500 C  C   . ILE C 1 79  ? -2.649  12.328  -60.665  1.00 22.41  ? 71  ILE C C   1 
ATOM   3501 O  O   . ILE C 1 79  ? -2.022  13.279  -61.146  1.00 27.21  ? 71  ILE C O   1 
ATOM   3502 C  CB  . ILE C 1 79  ? -1.909  12.743  -58.301  1.00 23.31  ? 71  ILE C CB  1 
ATOM   3503 C  CG1 . ILE C 1 79  ? -1.270  12.111  -57.069  1.00 22.19  ? 71  ILE C CG1 1 
ATOM   3504 C  CG2 . ILE C 1 79  ? -3.189  13.494  -57.971  1.00 20.75  ? 71  ILE C CG2 1 
ATOM   3505 C  CD1 . ILE C 1 79  ? -0.354  13.028  -56.299  1.00 28.47  ? 71  ILE C CD1 1 
ATOM   3506 N  N   . THR C 1 80  ? -3.757  11.850  -61.225  1.00 20.94  ? 72  THR C N   1 
ATOM   3507 C  CA  . THR C 1 80  ? -4.307  12.518  -62.395  1.00 27.56  ? 72  THR C CA  1 
ATOM   3508 C  C   . THR C 1 80  ? -5.291  13.587  -61.951  1.00 23.30  ? 72  THR C C   1 
ATOM   3509 O  O   . THR C 1 80  ? -5.927  13.478  -60.900  1.00 27.69  ? 72  THR C O   1 
ATOM   3510 C  CB  . THR C 1 80  ? -4.998  11.551  -63.361  1.00 25.59  ? 72  THR C CB  1 
ATOM   3511 O  OG1 . THR C 1 80  ? -6.259  11.139  -62.818  1.00 37.88  ? 72  THR C OG1 1 
ATOM   3512 C  CG2 . THR C 1 80  ? -4.129  10.347  -63.647  1.00 24.09  ? 72  THR C CG2 1 
ATOM   3513 N  N   . HIS C 1 81  ? -5.392  14.628  -62.755  1.00 25.24  ? 73  HIS C N   1 
ATOM   3514 C  CA  . HIS C 1 81  ? -6.266  15.746  -62.427  1.00 28.11  ? 73  HIS C CA  1 
ATOM   3515 C  C   . HIS C 1 81  ? -7.699  15.264  -62.235  1.00 31.59  ? 73  HIS C C   1 
ATOM   3516 O  O   . HIS C 1 81  ? -8.225  14.523  -63.083  1.00 30.88  ? 73  HIS C O   1 
ATOM   3517 C  CB  . HIS C 1 81  ? -6.243  16.801  -63.526  1.00 25.56  ? 73  HIS C CB  1 
ATOM   3518 C  CG  . HIS C 1 81  ? -6.798  18.115  -63.085  1.00 31.81  ? 73  HIS C CG  1 
ATOM   3519 N  ND1 . HIS C 1 81  ? -8.143  18.415  -63.156  1.00 30.12  ? 73  HIS C ND1 1 
ATOM   3520 C  CD2 . HIS C 1 81  ? -6.195  19.200  -62.543  1.00 30.09  ? 73  HIS C CD2 1 
ATOM   3521 C  CE1 . HIS C 1 81  ? -8.343  19.632  -62.685  1.00 33.22  ? 73  HIS C CE1 1 
ATOM   3522 N  NE2 . HIS C 1 81  ? -7.178  20.131  -62.307  1.00 37.06  ? 73  HIS C NE2 1 
ATOM   3523 N  N   . PRO C 1 82  ? -8.366  15.666  -61.158  1.00 27.49  ? 74  PRO C N   1 
ATOM   3524 C  CA  . PRO C 1 82  ? -9.702  15.129  -60.896  1.00 29.45  ? 74  PRO C CA  1 
ATOM   3525 C  C   . PRO C 1 82  ? -10.714 15.497  -61.962  1.00 32.38  ? 74  PRO C C   1 
ATOM   3526 O  O   . PRO C 1 82  ? -11.760 14.849  -62.038  1.00 32.08  ? 74  PRO C O   1 
ATOM   3527 C  CB  . PRO C 1 82  ? -10.055 15.737  -59.529  1.00 31.64  ? 74  PRO C CB  1 
ATOM   3528 C  CG  . PRO C 1 82  ? -9.286  17.000  -59.491  1.00 30.33  ? 74  PRO C CG  1 
ATOM   3529 C  CD  . PRO C 1 82  ? -7.966  16.649  -60.134  1.00 35.03  ? 74  PRO C CD  1 
ATOM   3530 N  N   . ASN C 1 83  ? -10.438 16.495  -62.800  1.00 30.89  ? 75  ASN C N   1 
ATOM   3531 C  CA  . ASN C 1 83  ? -11.369 16.882  -63.849  1.00 28.31  ? 75  ASN C CA  1 
ATOM   3532 C  C   . ASN C 1 83  ? -10.952 16.366  -65.217  1.00 32.02  ? 75  ASN C C   1 
ATOM   3533 O  O   . ASN C 1 83  ? -11.562 16.744  -66.221  1.00 32.22  ? 75  ASN C O   1 
ATOM   3534 C  CB  . ASN C 1 83  ? -11.531 18.403  -63.887  1.00 27.82  ? 75  ASN C CB  1 
ATOM   3535 C  CG  . ASN C 1 83  ? -12.098 18.965  -62.581  1.00 35.08  ? 75  ASN C CG  1 
ATOM   3536 O  OD1 . ASN C 1 83  ? -11.695 20.042  -62.139  1.00 41.25  ? 75  ASN C OD1 1 
ATOM   3537 N  ND2 . ASN C 1 83  ? -13.002 18.226  -61.947  1.00 30.26  ? 75  ASN C ND2 1 
ATOM   3538 N  N   . PHE C 1 84  ? -9.918  15.531  -65.282  1.00 29.63  ? 76  PHE C N   1 
ATOM   3539 C  CA  . PHE C 1 84  ? -9.532  14.942  -66.555  1.00 34.67  ? 76  PHE C CA  1 
ATOM   3540 C  C   . PHE C 1 84  ? -10.678 14.125  -67.113  1.00 30.09  ? 76  PHE C C   1 
ATOM   3541 O  O   . PHE C 1 84  ? -11.287 13.327  -66.400  1.00 27.29  ? 76  PHE C O   1 
ATOM   3542 C  CB  . PHE C 1 84  ? -8.317  14.036  -66.410  1.00 20.18  ? 76  PHE C CB  1 
ATOM   3543 C  CG  . PHE C 1 84  ? -8.063  13.192  -67.623  1.00 23.50  ? 76  PHE C CG  1 
ATOM   3544 C  CD1 . PHE C 1 84  ? -7.778  13.784  -68.850  1.00 23.83  ? 76  PHE C CD1 1 
ATOM   3545 C  CD2 . PHE C 1 84  ? -8.115  11.812  -67.551  1.00 25.44  ? 76  PHE C CD2 1 
ATOM   3546 C  CE1 . PHE C 1 84  ? -7.522  13.018  -69.972  1.00 25.86  ? 76  PHE C CE1 1 
ATOM   3547 C  CE2 . PHE C 1 84  ? -7.869  11.025  -68.684  1.00 21.95  ? 76  PHE C CE2 1 
ATOM   3548 C  CZ  . PHE C 1 84  ? -7.565  11.627  -69.893  1.00 26.63  ? 76  PHE C CZ  1 
ATOM   3549 N  N   . ASN C 1 85  ? -10.953 14.314  -68.398  1.00 30.04  ? 77  ASN C N   1 
ATOM   3550 C  CA  . ASN C 1 85  ? -11.976 13.557  -69.104  1.00 34.28  ? 77  ASN C CA  1 
ATOM   3551 C  C   . ASN C 1 85  ? -11.344 13.020  -70.380  1.00 35.12  ? 77  ASN C C   1 
ATOM   3552 O  O   . ASN C 1 85  ? -11.063 13.788  -71.307  1.00 31.27  ? 77  ASN C O   1 
ATOM   3553 C  CB  . ASN C 1 85  ? -13.191 14.431  -69.397  1.00 29.72  ? 77  ASN C CB  1 
ATOM   3554 C  CG  . ASN C 1 85  ? -14.293 13.676  -70.110  1.00 39.32  ? 77  ASN C CG  1 
ATOM   3555 O  OD1 . ASN C 1 85  ? -14.051 12.962  -71.098  1.00 40.31  ? 77  ASN C OD1 1 
ATOM   3556 N  ND2 . ASN C 1 85  ? -15.520 13.854  -69.637  1.00 43.82  ? 77  ASN C ND2 1 
ATOM   3557 N  N   . GLY C 1 86  ? -11.117 11.702  -70.417  1.00 32.91  ? 78  GLY C N   1 
ATOM   3558 C  CA  . GLY C 1 86  ? -10.453 11.034  -71.526  1.00 35.60  ? 78  GLY C CA  1 
ATOM   3559 C  C   . GLY C 1 86  ? -11.185 11.081  -72.855  1.00 40.30  ? 78  GLY C C   1 
ATOM   3560 O  O   . GLY C 1 86  ? -10.641 10.606  -73.855  1.00 38.77  ? 78  GLY C O   1 
ATOM   3561 N  N   . ASN C 1 87  ? -12.396 11.635  -72.907  1.00 40.37  ? 79  ASN C N   1 
ATOM   3562 C  CA  . ASN C 1 87  ? -13.111 11.727  -74.172  1.00 38.72  ? 79  ASN C CA  1 
ATOM   3563 C  C   . ASN C 1 87  ? -13.387 13.152  -74.610  1.00 41.22  ? 79  ASN C C   1 
ATOM   3564 O  O   . ASN C 1 87  ? -13.355 13.418  -75.812  1.00 42.61  ? 79  ASN C O   1 
ATOM   3565 C  CB  . ASN C 1 87  ? -14.418 10.921  -74.114  1.00 35.84  ? 79  ASN C CB  1 
ATOM   3566 C  CG  . ASN C 1 87  ? -14.152 9.422   -74.069  1.00 34.59  ? 79  ASN C CG  1 
ATOM   3567 O  OD1 . ASN C 1 87  ? -13.601 8.859   -75.025  1.00 33.17  ? 79  ASN C OD1 1 
ATOM   3568 N  ND2 . ASN C 1 87  ? -14.529 8.771   -72.969  1.00 26.52  ? 79  ASN C ND2 1 
ATOM   3569 N  N   . THR C 1 88  ? -13.603 14.084  -73.679  1.00 39.11  ? 80  THR C N   1 
ATOM   3570 C  CA  . THR C 1 88  ? -13.482 15.494  -74.035  1.00 36.19  ? 80  THR C CA  1 
ATOM   3571 C  C   . THR C 1 88  ? -12.031 15.977  -74.012  1.00 41.79  ? 80  THR C C   1 
ATOM   3572 O  O   . THR C 1 88  ? -11.767 17.130  -74.383  1.00 48.46  ? 80  THR C O   1 
ATOM   3573 C  CB  . THR C 1 88  ? -14.321 16.366  -73.097  1.00 36.33  ? 80  THR C CB  1 
ATOM   3574 O  OG1 . THR C 1 88  ? -13.914 16.145  -71.744  1.00 37.93  ? 80  THR C OG1 1 
ATOM   3575 C  CG2 . THR C 1 88  ? -15.810 16.032  -73.227  1.00 30.27  ? 80  THR C CG2 1 
ATOM   3576 N  N   . LEU C 1 89  ? -11.101 15.134  -73.552  1.00 38.97  ? 81  LEU C N   1 
ATOM   3577 C  CA  . LEU C 1 89  ? -9.667  15.410  -73.490  1.00 40.35  ? 81  LEU C CA  1 
ATOM   3578 C  C   . LEU C 1 89  ? -9.331  16.597  -72.585  1.00 39.48  ? 81  LEU C C   1 
ATOM   3579 O  O   . LEU C 1 89  ? -8.160  16.985  -72.480  1.00 42.38  ? 81  LEU C O   1 
ATOM   3580 C  CB  . LEU C 1 89  ? -9.098  15.634  -74.900  1.00 29.75  ? 81  LEU C CB  1 
ATOM   3581 C  CG  . LEU C 1 89  ? -9.569  14.678  -76.000  1.00 39.77  ? 81  LEU C CG  1 
ATOM   3582 C  CD1 . LEU C 1 89  ? -8.791  14.932  -77.273  1.00 43.58  ? 81  LEU C CD1 1 
ATOM   3583 C  CD2 . LEU C 1 89  ? -9.448  13.225  -75.572  1.00 40.49  ? 81  LEU C CD2 1 
ATOM   3584 N  N   . ASP C 1 90  ? -10.322 17.175  -71.913  1.00 33.41  ? 82  ASP C N   1 
ATOM   3585 C  CA  . ASP C 1 90  ? -10.054 18.332  -71.066  1.00 31.51  ? 82  ASP C CA  1 
ATOM   3586 C  C   . ASP C 1 90  ? -9.328  17.916  -69.783  1.00 32.92  ? 82  ASP C C   1 
ATOM   3587 O  O   . ASP C 1 90  ? -9.570  16.833  -69.236  1.00 36.25  ? 82  ASP C O   1 
ATOM   3588 C  CB  . ASP C 1 90  ? -11.364 19.045  -70.740  1.00 33.94  ? 82  ASP C CB  1 
ATOM   3589 C  CG  . ASP C 1 90  ? -11.158 20.445  -70.207  1.00 28.43  ? 82  ASP C CG  1 
ATOM   3590 O  OD1 . ASP C 1 90  ? -10.069 21.034  -70.393  1.00 37.15  ? 82  ASP C OD1 1 
ATOM   3591 O  OD2 . ASP C 1 90  ? -12.109 20.971  -69.608  1.00 37.13  ? 82  ASP C OD2 1 
ATOM   3592 N  N   . ASN C 1 91  ? -8.434  18.797  -69.312  1.00 24.00  ? 83  ASN C N   1 
ATOM   3593 C  CA  . ASN C 1 91  ? -7.597  18.606  -68.113  1.00 31.17  ? 83  ASN C CA  1 
ATOM   3594 C  C   . ASN C 1 91  ? -6.651  17.419  -68.261  1.00 24.25  ? 83  ASN C C   1 
ATOM   3595 O  O   . ASN C 1 91  ? -6.485  16.607  -67.354  1.00 31.22  ? 83  ASN C O   1 
ATOM   3596 C  CB  . ASN C 1 91  ? -8.432  18.486  -66.838  1.00 25.12  ? 83  ASN C CB  1 
ATOM   3597 C  CG  . ASN C 1 91  ? -9.417  19.622  -66.699  1.00 31.20  ? 83  ASN C CG  1 
ATOM   3598 O  OD1 . ASN C 1 91  ? -9.016  20.754  -66.429  1.00 23.29  ? 83  ASN C OD1 1 
ATOM   3599 N  ND2 . ASN C 1 91  ? -10.711 19.329  -66.861  1.00 26.07  ? 83  ASN C ND2 1 
ATOM   3600 N  N   . ASP C 1 92  ? -5.997  17.345  -69.412  1.00 23.37  ? 84  ASP C N   1 
ATOM   3601 C  CA  . ASP C 1 92  ? -5.082  16.250  -69.695  1.00 22.37  ? 84  ASP C CA  1 
ATOM   3602 C  C   . ASP C 1 92  ? -3.731  16.582  -69.071  1.00 26.92  ? 84  ASP C C   1 
ATOM   3603 O  O   . ASP C 1 92  ? -2.761  16.946  -69.745  1.00 23.56  ? 84  ASP C O   1 
ATOM   3604 C  CB  . ASP C 1 92  ? -4.997  16.019  -71.193  1.00 22.97  ? 84  ASP C CB  1 
ATOM   3605 C  CG  . ASP C 1 92  ? -4.261  14.751  -71.549  1.00 24.12  ? 84  ASP C CG  1 
ATOM   3606 O  OD1 . ASP C 1 92  ? -4.059  13.908  -70.642  1.00 21.64  ? 84  ASP C OD1 1 
ATOM   3607 O  OD2 . ASP C 1 92  ? -3.920  14.585  -72.745  1.00 16.28  ? 84  ASP C OD2 1 
ATOM   3608 N  N   . ILE C 1 93  ? -3.688  16.453  -67.739  1.00 20.30  ? 85  ILE C N   1 
ATOM   3609 C  CA  . ILE C 1 93  ? -2.483  16.720  -66.956  1.00 17.80  ? 85  ILE C CA  1 
ATOM   3610 C  C   . ILE C 1 93  ? -2.403  15.729  -65.798  1.00 24.47  ? 85  ILE C C   1 
ATOM   3611 O  O   . ILE C 1 93  ? -3.425  15.372  -65.191  1.00 24.27  ? 85  ILE C O   1 
ATOM   3612 C  CB  . ILE C 1 93  ? -2.462  18.173  -66.446  1.00 22.73  ? 85  ILE C CB  1 
ATOM   3613 C  CG1 . ILE C 1 93  ? -1.219  18.440  -65.620  1.00 23.03  ? 85  ILE C CG1 1 
ATOM   3614 C  CG2 . ILE C 1 93  ? -3.699  18.482  -65.624  1.00 19.50  ? 85  ILE C CG2 1 
ATOM   3615 C  CD1 . ILE C 1 93  ? -0.860  19.875  -65.595  1.00 18.49  ? 85  ILE C CD1 1 
ATOM   3616 N  N   . MET C 1 94  ? -1.183  15.292  -65.481  1.00 20.35  ? 86  MET C N   1 
ATOM   3617 C  CA  . MET C 1 94  ? -0.980  14.297  -64.441  1.00 19.77  ? 86  MET C CA  1 
ATOM   3618 C  C   . MET C 1 94  ? 0.348   14.571  -63.729  1.00 19.05  ? 86  MET C C   1 
ATOM   3619 O  O   . MET C 1 94  ? 1.325   15.012  -64.346  1.00 19.37  ? 86  MET C O   1 
ATOM   3620 C  CB  . MET C 1 94  ? -1.061  12.891  -65.077  1.00 20.95  ? 86  MET C CB  1 
ATOM   3621 C  CG  . MET C 1 94  ? -0.700  11.693  -64.202  1.00 24.94  ? 86  MET C CG  1 
ATOM   3622 S  SD  . MET C 1 94  ? -0.764  10.077  -65.070  1.00 30.21  ? 86  MET C SD  1 
ATOM   3623 C  CE  . MET C 1 94  ? 0.799   10.041  -65.969  1.00 17.84  ? 86  MET C CE  1 
ATOM   3624 N  N   . LEU C 1 95  ? 0.367   14.338  -62.421  1.00 25.28  ? 87  LEU C N   1 
ATOM   3625 C  CA  . LEU C 1 95  ? 1.557   14.494  -61.589  1.00 20.93  ? 87  LEU C CA  1 
ATOM   3626 C  C   . LEU C 1 95  ? 2.034   13.127  -61.098  1.00 32.69  ? 87  LEU C C   1 
ATOM   3627 O  O   . LEU C 1 95  ? 1.227   12.249  -60.752  1.00 26.09  ? 87  LEU C O   1 
ATOM   3628 C  CB  . LEU C 1 95  ? 1.268   15.402  -60.391  1.00 22.58  ? 87  LEU C CB  1 
ATOM   3629 C  CG  . LEU C 1 95  ? 1.509   16.897  -60.578  1.00 24.44  ? 87  LEU C CG  1 
ATOM   3630 C  CD1 . LEU C 1 95  ? 0.885   17.670  -59.436  1.00 24.36  ? 87  LEU C CD1 1 
ATOM   3631 C  CD2 . LEU C 1 95  ? 2.982   17.173  -60.654  1.00 22.67  ? 87  LEU C CD2 1 
ATOM   3632 N  N   . ILE C 1 96  ? 3.348   12.946  -61.072  1.00 23.56  ? 88  ILE C N   1 
ATOM   3633 C  CA  . ILE C 1 96  ? 3.961   11.707  -60.622  1.00 20.67  ? 88  ILE C CA  1 
ATOM   3634 C  C   . ILE C 1 96  ? 4.977   12.070  -59.559  1.00 20.20  ? 88  ILE C C   1 
ATOM   3635 O  O   . ILE C 1 96  ? 5.875   12.877  -59.820  1.00 24.49  ? 88  ILE C O   1 
ATOM   3636 C  CB  . ILE C 1 96  ? 4.653   10.953  -61.770  1.00 20.45  ? 88  ILE C CB  1 
ATOM   3637 C  CG1 . ILE C 1 96  ? 3.625   10.322  -62.683  1.00 24.67  ? 88  ILE C CG1 1 
ATOM   3638 C  CG2 . ILE C 1 96  ? 5.644   9.903   -61.239  1.00 19.91  ? 88  ILE C CG2 1 
ATOM   3639 C  CD1 . ILE C 1 96  ? 4.191   9.911   -64.026  1.00 29.51  ? 88  ILE C CD1 1 
ATOM   3640 N  N   . LYS C 1 97  ? 4.857   11.469  -58.379  1.00 22.47  ? 89  LYS C N   1 
ATOM   3641 C  CA  . LYS C 1 97  ? 5.886   11.593  -57.354  1.00 20.65  ? 89  LYS C CA  1 
ATOM   3642 C  C   . LYS C 1 97  ? 6.843   10.424  -57.434  1.00 23.98  ? 89  LYS C C   1 
ATOM   3643 O  O   . LYS C 1 97  ? 6.430   9.267   -57.311  1.00 21.47  ? 89  LYS C O   1 
ATOM   3644 C  CB  . LYS C 1 97  ? 5.319   11.657  -55.945  1.00 19.38  ? 89  LYS C CB  1 
ATOM   3645 C  CG  . LYS C 1 97  ? 6.413   12.108  -54.952  1.00 21.95  ? 89  LYS C CG  1 
ATOM   3646 C  CD  . LYS C 1 97  ? 6.001   11.867  -53.527  1.00 22.02  ? 89  LYS C CD  1 
ATOM   3647 C  CE  . LYS C 1 97  ? 6.924   12.575  -52.564  1.00 23.28  ? 89  LYS C CE  1 
ATOM   3648 N  NZ  . LYS C 1 97  ? 6.200   12.886  -51.308  1.00 26.83  ? 89  LYS C NZ  1 
ATOM   3649 N  N   . LEU C 1 98  ? 8.122   10.731  -57.591  1.00 19.39  ? 90  LEU C N   1 
ATOM   3650 C  CA  . LEU C 1 98  ? 9.115   9.681   -57.672  1.00 20.03  ? 90  LEU C CA  1 
ATOM   3651 C  C   . LEU C 1 98  ? 9.183   8.892   -56.363  1.00 23.11  ? 90  LEU C C   1 
ATOM   3652 O  O   . LEU C 1 98  ? 8.843   9.391   -55.290  1.00 21.12  ? 90  LEU C O   1 
ATOM   3653 C  CB  . LEU C 1 98  ? 10.469  10.286  -58.016  1.00 15.32  ? 90  LEU C CB  1 
ATOM   3654 C  CG  . LEU C 1 98  ? 10.488  11.001  -59.366  1.00 21.71  ? 90  LEU C CG  1 
ATOM   3655 C  CD1 . LEU C 1 98  ? 11.924  11.327  -59.726  1.00 19.56  ? 90  LEU C CD1 1 
ATOM   3656 C  CD2 . LEU C 1 98  ? 9.820   10.163  -60.478  1.00 25.09  ? 90  LEU C CD2 1 
ATOM   3657 N  N   . SER C 1 99  ? 9.607   7.629   -56.471  1.00 23.62  ? 91  SER C N   1 
ATOM   3658 C  CA  . SER C 1 99  ? 9.826   6.796   -55.290  1.00 25.69  ? 91  SER C CA  1 
ATOM   3659 C  C   . SER C 1 99  ? 10.997  7.301   -54.447  1.00 22.84  ? 91  SER C C   1 
ATOM   3660 O  O   . SER C 1 99  ? 10.994  7.159   -53.226  1.00 20.96  ? 91  SER C O   1 
ATOM   3661 C  CB  . SER C 1 99  ? 10.078  5.352   -55.722  1.00 21.53  ? 91  SER C CB  1 
ATOM   3662 O  OG  . SER C 1 99  ? 9.569   4.483   -54.750  1.00 45.83  ? 91  SER C OG  1 
ATOM   3663 N  N   . SER C 1 100 ? 12.009  7.874   -55.078  1.00 23.92  ? 92  SER C N   1 
ATOM   3664 C  CA  . SER C 1 100 ? 13.128  8.502   -54.404  1.00 19.63  ? 92  SER C CA  1 
ATOM   3665 C  C   . SER C 1 100 ? 13.496  9.736   -55.208  1.00 24.87  ? 92  SER C C   1 
ATOM   3666 O  O   . SER C 1 100 ? 13.302  9.753   -56.433  1.00 25.33  ? 92  SER C O   1 
ATOM   3667 C  CB  . SER C 1 100 ? 14.323  7.536   -54.309  1.00 24.18  ? 92  SER C CB  1 
ATOM   3668 O  OG  . SER C 1 100 ? 14.630  7.003   -55.586  1.00 21.99  ? 92  SER C OG  1 
ATOM   3669 N  N   . PRO C 1 101 ? 14.019  10.784  -54.560  1.00 28.48  ? 93  PRO C N   1 
ATOM   3670 C  CA  . PRO C 1 101 ? 14.297  12.040  -55.286  1.00 26.55  ? 93  PRO C CA  1 
ATOM   3671 C  C   . PRO C 1 101 ? 15.445  11.893  -56.276  1.00 24.08  ? 93  PRO C C   1 
ATOM   3672 O  O   . PRO C 1 101 ? 16.464  11.256  -55.994  1.00 30.69  ? 93  PRO C O   1 
ATOM   3673 C  CB  . PRO C 1 101 ? 14.656  13.027  -54.170  1.00 22.26  ? 93  PRO C CB  1 
ATOM   3674 C  CG  . PRO C 1 101 ? 15.121  12.155  -53.037  1.00 25.83  ? 93  PRO C CG  1 
ATOM   3675 C  CD  . PRO C 1 101 ? 14.326  10.891  -53.124  1.00 22.41  ? 93  PRO C CD  1 
ATOM   3676 N  N   . ALA C 1 102 ? 15.268  12.484  -57.451  1.00 18.24  ? 94  ALA C N   1 
ATOM   3677 C  CA  . ALA C 1 102 ? 16.308  12.430  -58.467  1.00 24.34  ? 94  ALA C CA  1 
ATOM   3678 C  C   . ALA C 1 102 ? 17.567  13.146  -57.987  1.00 26.42  ? 94  ALA C C   1 
ATOM   3679 O  O   . ALA C 1 102 ? 17.508  14.156  -57.281  1.00 27.21  ? 94  ALA C O   1 
ATOM   3680 C  CB  . ALA C 1 102 ? 15.811  13.058  -59.776  1.00 19.07  ? 94  ALA C CB  1 
ATOM   3681 N  N   . THR C 1 103 ? 18.715  12.610  -58.359  1.00 26.56  ? 95  THR C N   1 
ATOM   3682 C  CA  . THR C 1 103 ? 19.971  13.308  -58.144  1.00 27.45  ? 95  THR C CA  1 
ATOM   3683 C  C   . THR C 1 103 ? 20.123  14.339  -59.256  1.00 25.40  ? 95  THR C C   1 
ATOM   3684 O  O   . THR C 1 103 ? 20.311  13.989  -60.426  1.00 24.76  ? 95  THR C O   1 
ATOM   3685 C  CB  . THR C 1 103 ? 21.120  12.302  -58.104  1.00 29.15  ? 95  THR C CB  1 
ATOM   3686 O  OG1 . THR C 1 103 ? 20.995  11.511  -56.917  1.00 36.17  ? 95  THR C OG1 1 
ATOM   3687 C  CG2 . THR C 1 103 ? 22.483  12.980  -58.120  1.00 21.21  ? 95  THR C CG2 1 
ATOM   3688 N  N   . LEU C 1 104 ? 20.033  15.611  -58.901  1.00 24.96  ? 96  LEU C N   1 
ATOM   3689 C  CA  . LEU C 1 104 ? 20.102  16.668  -59.899  1.00 22.91  ? 96  LEU C CA  1 
ATOM   3690 C  C   . LEU C 1 104 ? 21.555  16.954  -60.266  1.00 29.92  ? 96  LEU C C   1 
ATOM   3691 O  O   . LEU C 1 104 ? 22.429  17.029  -59.397  1.00 34.47  ? 96  LEU C O   1 
ATOM   3692 C  CB  . LEU C 1 104 ? 19.401  17.920  -59.371  1.00 23.85  ? 96  LEU C CB  1 
ATOM   3693 C  CG  . LEU C 1 104 ? 17.891  17.702  -59.150  1.00 28.89  ? 96  LEU C CG  1 
ATOM   3694 C  CD1 . LEU C 1 104 ? 17.119  19.004  -59.235  1.00 26.67  ? 96  LEU C CD1 1 
ATOM   3695 C  CD2 . LEU C 1 104 ? 17.307  16.707  -60.177  1.00 28.17  ? 96  LEU C CD2 1 
ATOM   3696 N  N   . ASN C 1 105 ? 21.810  17.093  -61.561  1.00 35.56  ? 97  ASN C N   1 
ATOM   3697 C  CA  . ASN C 1 105 ? 23.132  17.409  -62.091  1.00 25.28  ? 97  ASN C CA  1 
ATOM   3698 C  C   . ASN C 1 105 ? 22.931  18.096  -63.435  1.00 22.08  ? 97  ASN C C   1 
ATOM   3699 O  O   . ASN C 1 105 ? 21.855  18.633  -63.719  1.00 34.42  ? 97  ASN C O   1 
ATOM   3700 C  CB  . ASN C 1 105 ? 23.995  16.146  -62.238  1.00 30.20  ? 97  ASN C CB  1 
ATOM   3701 C  CG  . ASN C 1 105 ? 23.217  14.969  -62.819  1.00 38.25  ? 97  ASN C CG  1 
ATOM   3702 O  OD1 . ASN C 1 105 ? 22.572  15.087  -63.869  1.00 29.87  ? 97  ASN C OD1 1 
ATOM   3703 N  ND2 . ASN C 1 105 ? 23.336  13.813  -62.180  1.00 27.03  ? 97  ASN C ND2 1 
ATOM   3704 N  N   . SER C 1 106 ? 23.950  18.046  -64.283  1.00 30.16  ? 98  SER C N   1 
ATOM   3705 C  CA  . SER C 1 106 ? 23.902  18.786  -65.541  1.00 33.24  ? 98  SER C CA  1 
ATOM   3706 C  C   . SER C 1 106 ? 23.008  18.100  -66.556  1.00 30.10  ? 98  SER C C   1 
ATOM   3707 O  O   . SER C 1 106 ? 22.446  18.765  -67.435  1.00 42.09  ? 98  SER C O   1 
ATOM   3708 C  CB  . SER C 1 106 ? 25.317  18.959  -66.114  1.00 29.74  ? 98  SER C CB  1 
ATOM   3709 O  OG  . SER C 1 106 ? 25.851  17.723  -66.558  1.00 36.95  ? 98  SER C OG  1 
ATOM   3710 N  N   . ARG C 1 107 ? 22.858  16.780  -66.433  1.00 41.48  ? 99  ARG C N   1 
ATOM   3711 C  CA  . ARG C 1 107 ? 21.995  15.982  -67.291  1.00 27.74  ? 99  ARG C CA  1 
ATOM   3712 C  C   . ARG C 1 107 ? 20.597  15.798  -66.709  1.00 33.30  ? 99  ARG C C   1 
ATOM   3713 O  O   . ARG C 1 107 ? 19.663  15.490  -67.456  1.00 36.91  ? 99  ARG C O   1 
ATOM   3714 C  CB  . ARG C 1 107 ? 22.674  14.634  -67.554  1.00 34.52  ? 99  ARG C CB  1 
ATOM   3715 C  CG  . ARG C 1 107 ? 24.125  14.876  -67.988  1.00 46.93  ? 99  ARG C CG  1 
ATOM   3716 C  CD  . ARG C 1 107 ? 25.005  13.649  -68.076  1.00 65.52  ? 99  ARG C CD  1 
ATOM   3717 N  NE  . ARG C 1 107 ? 25.979  13.807  -69.156  1.00 81.82  ? 99  ARG C NE  1 
ATOM   3718 C  CZ  . ARG C 1 107 ? 27.130  14.467  -69.059  1.00 88.55  ? 99  ARG C CZ  1 
ATOM   3719 N  NH1 . ARG C 1 107 ? 27.538  14.983  -67.910  1.00 90.22  ? 99  ARG C NH1 1 
ATOM   3720 N  NH2 . ARG C 1 107 ? 27.897  14.605  -70.142  1.00 75.73  ? 99  ARG C NH2 1 
ATOM   3721 N  N   . VAL C 1 108 ? 20.417  16.021  -65.408  1.00 31.26  ? 100 VAL C N   1 
ATOM   3722 C  CA  . VAL C 1 108 ? 19.121  15.870  -64.752  1.00 27.74  ? 100 VAL C CA  1 
ATOM   3723 C  C   . VAL C 1 108 ? 18.821  17.162  -64.015  1.00 26.19  ? 100 VAL C C   1 
ATOM   3724 O  O   . VAL C 1 108 ? 19.451  17.451  -62.989  1.00 24.94  ? 100 VAL C O   1 
ATOM   3725 C  CB  . VAL C 1 108 ? 19.099  14.685  -63.780  1.00 36.84  ? 100 VAL C CB  1 
ATOM   3726 C  CG1 . VAL C 1 108 ? 17.729  14.590  -63.095  1.00 35.56  ? 100 VAL C CG1 1 
ATOM   3727 C  CG2 . VAL C 1 108 ? 19.479  13.391  -64.500  1.00 30.66  ? 100 VAL C CG2 1 
ATOM   3728 N  N   . ALA C 1 109 ? 17.855  17.931  -64.516  1.00 21.61  ? 101 ALA C N   1 
ATOM   3729 C  CA  . ALA C 1 109 ? 17.540  19.204  -63.881  1.00 28.39  ? 101 ALA C CA  1 
ATOM   3730 C  C   . ALA C 1 109 ? 16.054  19.489  -63.998  1.00 26.64  ? 101 ALA C C   1 
ATOM   3731 O  O   . ALA C 1 109 ? 15.350  18.905  -64.825  1.00 23.41  ? 101 ALA C O   1 
ATOM   3732 C  CB  . ALA C 1 109 ? 18.340  20.369  -64.478  1.00 14.14  ? 101 ALA C CB  1 
ATOM   3733 N  N   . THR C 1 110 ? 15.593  20.402  -63.152  1.00 19.79  ? 102 THR C N   1 
ATOM   3734 C  CA  . THR C 1 110 ? 14.191  20.772  -63.104  1.00 20.10  ? 102 THR C CA  1 
ATOM   3735 C  C   . THR C 1 110 ? 13.910  21.843  -64.142  1.00 23.78  ? 102 THR C C   1 
ATOM   3736 O  O   . THR C 1 110 ? 14.812  22.545  -64.612  1.00 29.12  ? 102 THR C O   1 
ATOM   3737 C  CB  . THR C 1 110 ? 13.823  21.265  -61.707  1.00 26.76  ? 102 THR C CB  1 
ATOM   3738 O  OG1 . THR C 1 110 ? 14.725  22.305  -61.299  1.00 27.25  ? 102 THR C OG1 1 
ATOM   3739 C  CG2 . THR C 1 110 ? 13.981  20.119  -60.712  1.00 25.75  ? 102 THR C CG2 1 
ATOM   3740 N  N   . VAL C 1 111 ? 12.651  21.941  -64.537  1.00 25.92  ? 103 VAL C N   1 
ATOM   3741 C  CA  . VAL C 1 111 ? 12.201  23.020  -65.403  1.00 20.94  ? 103 VAL C CA  1 
ATOM   3742 C  C   . VAL C 1 111 ? 11.166  23.788  -64.608  1.00 23.60  ? 103 VAL C C   1 
ATOM   3743 O  O   . VAL C 1 111 ? 10.383  23.192  -63.860  1.00 32.64  ? 103 VAL C O   1 
ATOM   3744 C  CB  . VAL C 1 111 ? 11.629  22.531  -66.761  1.00 28.91  ? 103 VAL C CB  1 
ATOM   3745 C  CG1 . VAL C 1 111 ? 10.453  21.567  -66.584  1.00 17.61  ? 103 VAL C CG1 1 
ATOM   3746 C  CG2 . VAL C 1 111 ? 11.212  23.713  -67.649  1.00 25.71  ? 103 VAL C CG2 1 
ATOM   3747 N  N   . SER C 1 112 ? 11.188  25.105  -64.747  1.00 18.94  ? 104 SER C N   1 
ATOM   3748 C  CA  . SER C 1 112 ? 10.326  25.998  -63.988  1.00 22.73  ? 104 SER C CA  1 
ATOM   3749 C  C   . SER C 1 112 ? 8.905   26.020  -64.542  1.00 27.01  ? 104 SER C C   1 
ATOM   3750 O  O   . SER C 1 112 ? 8.678   25.898  -65.750  1.00 30.36  ? 104 SER C O   1 
ATOM   3751 C  CB  . SER C 1 112 ? 10.928  27.412  -64.005  1.00 29.91  ? 104 SER C CB  1 
ATOM   3752 O  OG  . SER C 1 112 ? 9.930   28.417  -64.000  1.00 44.44  ? 104 SER C OG  1 
ATOM   3753 N  N   . LEU C 1 113 ? 7.945   26.216  -63.643  1.00 32.40  ? 105 LEU C N   1 
ATOM   3754 C  CA  . LEU C 1 113 ? 6.554   26.423  -64.022  1.00 27.33  ? 105 LEU C CA  1 
ATOM   3755 C  C   . LEU C 1 113 ? 6.348   27.844  -64.550  1.00 32.40  ? 105 LEU C C   1 
ATOM   3756 O  O   . LEU C 1 113 ? 7.144   28.750  -64.269  1.00 27.93  ? 105 LEU C O   1 
ATOM   3757 C  CB  . LEU C 1 113 ? 5.655   26.184  -62.820  1.00 26.90  ? 105 LEU C CB  1 
ATOM   3758 C  CG  . LEU C 1 113 ? 5.652   24.734  -62.341  1.00 28.02  ? 105 LEU C CG  1 
ATOM   3759 C  CD1 . LEU C 1 113 ? 4.722   24.551  -61.165  1.00 19.58  ? 105 LEU C CD1 1 
ATOM   3760 C  CD2 . LEU C 1 113 ? 5.286   23.820  -63.488  1.00 32.56  ? 105 LEU C CD2 1 
ATOM   3761 N  N   . PRO C 1 114 ? 5.276   28.073  -65.311  1.00 30.17  ? 106 PRO C N   1 
ATOM   3762 C  CA  . PRO C 1 114 ? 5.085   29.395  -65.934  1.00 34.47  ? 106 PRO C CA  1 
ATOM   3763 C  C   . PRO C 1 114 ? 4.802   30.488  -64.905  1.00 30.82  ? 106 PRO C C   1 
ATOM   3764 O  O   . PRO C 1 114 ? 3.989   30.312  -63.995  1.00 31.15  ? 106 PRO C O   1 
ATOM   3765 C  CB  . PRO C 1 114 ? 3.892   29.177  -66.874  1.00 30.02  ? 106 PRO C CB  1 
ATOM   3766 C  CG  . PRO C 1 114 ? 3.196   27.988  -66.342  1.00 25.05  ? 106 PRO C CG  1 
ATOM   3767 C  CD  . PRO C 1 114 ? 4.236   27.116  -65.718  1.00 25.45  ? 106 PRO C CD  1 
ATOM   3768 N  N   . ARG C 1 115 ? 5.488   31.627  -65.056  1.00 28.98  ? 107 ARG C N   1 
ATOM   3769 C  CA  . ARG C 1 115 ? 5.183   32.787  -64.220  1.00 32.42  ? 107 ARG C CA  1 
ATOM   3770 C  C   . ARG C 1 115 ? 3.958   33.523  -64.729  1.00 35.43  ? 107 ARG C C   1 
ATOM   3771 O  O   . ARG C 1 115 ? 3.259   34.185  -63.952  1.00 32.94  ? 107 ARG C O   1 
ATOM   3772 C  CB  . ARG C 1 115 ? 6.383   33.737  -64.160  1.00 35.30  ? 107 ARG C CB  1 
ATOM   3773 C  CG  . ARG C 1 115 ? 7.738   33.018  -64.081  1.00 43.61  ? 107 ARG C CG  1 
ATOM   3774 C  CD  . ARG C 1 115 ? 8.901   34.005  -64.099  1.00 43.88  ? 107 ARG C CD  1 
ATOM   3775 N  NE  . ARG C 1 115 ? 8.607   35.206  -63.321  1.00 34.68  ? 107 ARG C NE  1 
ATOM   3776 C  CZ  . ARG C 1 115 ? 8.874   35.325  -62.026  1.00 36.09  ? 107 ARG C CZ  1 
ATOM   3777 N  NH1 . ARG C 1 115 ? 9.438   34.337  -61.344  1.00 37.46  ? 107 ARG C NH1 1 
ATOM   3778 N  NH2 . ARG C 1 115 ? 8.553   36.453  -61.396  1.00 40.84  ? 107 ARG C NH2 1 
ATOM   3779 N  N   . SER C 1 116 ? 3.682   33.392  -66.017  1.00 32.53  ? 108 SER C N   1 
ATOM   3780 C  CA  . SER C 1 116 ? 2.479   33.897  -66.647  1.00 38.41  ? 108 SER C CA  1 
ATOM   3781 C  C   . SER C 1 116 ? 2.191   32.979  -67.829  1.00 40.77  ? 108 SER C C   1 
ATOM   3782 O  O   . SER C 1 116 ? 3.002   32.113  -68.168  1.00 45.61  ? 108 SER C O   1 
ATOM   3783 C  CB  . SER C 1 116 ? 2.670   35.355  -67.062  1.00 28.45  ? 108 SER C CB  1 
ATOM   3784 O  OG  . SER C 1 116 ? 3.548   35.430  -68.175  1.00 46.40  ? 108 SER C OG  1 
ATOM   3785 N  N   . CYS C 1 117 ? 1.022   33.144  -68.445  1.00 32.10  ? 109 CYS C N   1 
ATOM   3786 C  CA  . CYS C 1 117 ? 0.746   32.382  -69.654  1.00 35.58  ? 109 CYS C CA  1 
ATOM   3787 C  C   . CYS C 1 117 ? 1.589   32.930  -70.807  1.00 41.34  ? 109 CYS C C   1 
ATOM   3788 O  O   . CYS C 1 117 ? 2.123   34.040  -70.742  1.00 49.49  ? 109 CYS C O   1 
ATOM   3789 C  CB  . CYS C 1 117 ? -0.750  32.422  -69.986  1.00 47.19  ? 109 CYS C CB  1 
ATOM   3790 S  SG  . CYS C 1 117 ? -1.857  31.590  -68.740  1.00 70.24  ? 109 CYS C SG  1 
ATOM   3791 N  N   . ALA C 1 118 ? 1.743   32.126  -71.854  1.00 38.75  ? 110 ALA C N   1 
ATOM   3792 C  CA  . ALA C 1 118 ? 2.524   32.517  -73.024  1.00 38.35  ? 110 ALA C CA  1 
ATOM   3793 C  C   . ALA C 1 118 ? 1.609   33.099  -74.101  1.00 45.85  ? 110 ALA C C   1 
ATOM   3794 O  O   . ALA C 1 118 ? 0.583   32.503  -74.442  1.00 39.81  ? 110 ALA C O   1 
ATOM   3795 C  CB  . ALA C 1 118 ? 3.313   31.332  -73.584  1.00 39.08  ? 110 ALA C CB  1 
ATOM   3796 N  N   . ALA C 1 119 ? 1.983   34.261  -74.633  1.00 46.30  ? 111 ALA C N   1 
ATOM   3797 C  CA  . ALA C 1 119 ? 1.185   34.867  -75.686  1.00 52.31  ? 111 ALA C CA  1 
ATOM   3798 C  C   . ALA C 1 119 ? 1.533   34.250  -77.039  1.00 42.07  ? 111 ALA C C   1 
ATOM   3799 O  O   . ALA C 1 119 ? 2.594   33.647  -77.222  1.00 40.91  ? 111 ALA C O   1 
ATOM   3800 C  CB  . ALA C 1 119 ? 1.391   36.382  -75.719  1.00 44.37  ? 111 ALA C CB  1 
ATOM   3801 N  N   . ALA C 1 120 ? 0.619   34.408  -77.994  1.00 36.77  ? 112 ALA C N   1 
ATOM   3802 C  CA  . ALA C 1 120 ? 0.806   33.807  -79.306  1.00 40.20  ? 112 ALA C CA  1 
ATOM   3803 C  C   . ALA C 1 120 ? 2.087   34.314  -79.946  1.00 47.41  ? 112 ALA C C   1 
ATOM   3804 O  O   . ALA C 1 120 ? 2.521   35.445  -79.710  1.00 57.25  ? 112 ALA C O   1 
ATOM   3805 C  CB  . ALA C 1 120 ? -0.387  34.104  -80.215  1.00 42.77  ? 112 ALA C CB  1 
ATOM   3806 N  N   . GLY C 1 121 ? 2.705   33.452  -80.751  1.00 45.54  ? 113 GLY C N   1 
ATOM   3807 C  CA  . GLY C 1 121 ? 3.988   33.748  -81.340  1.00 34.47  ? 113 GLY C CA  1 
ATOM   3808 C  C   . GLY C 1 121 ? 5.179   33.576  -80.425  1.00 42.18  ? 113 GLY C C   1 
ATOM   3809 O  O   . GLY C 1 121 ? 6.313   33.721  -80.897  1.00 44.18  ? 113 GLY C O   1 
ATOM   3810 N  N   . THR C 1 122 ? 4.981   33.279  -79.133  1.00 36.14  ? 114 THR C N   1 
ATOM   3811 C  CA  . THR C 1 122 ? 6.125   32.924  -78.293  1.00 40.06  ? 114 THR C CA  1 
ATOM   3812 C  C   . THR C 1 122 ? 6.789   31.684  -78.877  1.00 39.84  ? 114 THR C C   1 
ATOM   3813 O  O   . THR C 1 122 ? 6.107   30.722  -79.237  1.00 42.05  ? 114 THR C O   1 
ATOM   3814 C  CB  . THR C 1 122 ? 5.701   32.644  -76.846  1.00 36.61  ? 114 THR C CB  1 
ATOM   3815 O  OG1 . THR C 1 122 ? 4.784   33.644  -76.390  1.00 49.05  ? 114 THR C OG1 1 
ATOM   3816 C  CG2 . THR C 1 122 ? 6.910   32.646  -75.934  1.00 26.36  ? 114 THR C CG2 1 
ATOM   3817 N  N   . GLU C 1 123 ? 8.114   31.699  -78.988  1.00 32.24  ? 115 GLU C N   1 
ATOM   3818 C  CA  . GLU C 1 123 ? 8.821   30.554  -79.542  1.00 40.67  ? 115 GLU C CA  1 
ATOM   3819 C  C   . GLU C 1 123 ? 9.124   29.542  -78.433  1.00 46.74  ? 115 GLU C C   1 
ATOM   3820 O  O   . GLU C 1 123 ? 9.695   29.896  -77.395  1.00 43.50  ? 115 GLU C O   1 
ATOM   3821 C  CB  . GLU C 1 123 ? 10.102  30.999  -80.251  1.00 33.95  ? 115 GLU C CB  1 
ATOM   3822 C  CG  . GLU C 1 123 ? 10.901  29.831  -80.838  1.00 48.31  ? 115 GLU C CG  1 
ATOM   3823 C  CD  . GLU C 1 123 ? 12.410  30.092  -80.928  1.00 63.82  ? 115 GLU C CD  1 
ATOM   3824 O  OE1 . GLU C 1 123 ? 13.001  30.541  -79.918  1.00 75.02  ? 115 GLU C OE1 1 
ATOM   3825 O  OE2 . GLU C 1 123 ? 13.009  29.806  -81.995  1.00 57.22  ? 115 GLU C OE2 1 
ATOM   3826 N  N   . CYS C 1 124 ? 8.727   28.284  -78.652  1.00 36.86  ? 116 CYS C N   1 
ATOM   3827 C  CA  . CYS C 1 124 ? 8.848   27.225  -77.663  1.00 37.32  ? 116 CYS C CA  1 
ATOM   3828 C  C   . CYS C 1 124 ? 9.719   26.090  -78.181  1.00 41.28  ? 116 CYS C C   1 
ATOM   3829 O  O   . CYS C 1 124 ? 9.834   25.875  -79.393  1.00 39.83  ? 116 CYS C O   1 
ATOM   3830 C  CB  . CYS C 1 124 ? 7.488   26.643  -77.289  1.00 35.80  ? 116 CYS C CB  1 
ATOM   3831 S  SG  . CYS C 1 124 ? 6.227   27.783  -76.640  1.00 46.98  ? 116 CYS C SG  1 
ATOM   3832 N  N   . LEU C 1 125 ? 10.312  25.353  -77.240  1.00 37.36  ? 117 LEU C N   1 
ATOM   3833 C  CA  . LEU C 1 125 ? 11.047  24.128  -77.531  1.00 31.11  ? 117 LEU C CA  1 
ATOM   3834 C  C   . LEU C 1 125 ? 10.175  22.932  -77.157  1.00 29.12  ? 117 LEU C C   1 
ATOM   3835 O  O   . LEU C 1 125 ? 9.738   22.805  -76.006  1.00 27.01  ? 117 LEU C O   1 
ATOM   3836 C  CB  . LEU C 1 125 ? 12.374  24.088  -76.770  1.00 26.43  ? 117 LEU C CB  1 
ATOM   3837 C  CG  . LEU C 1 125 ? 13.327  22.936  -77.088  1.00 25.25  ? 117 LEU C CG  1 
ATOM   3838 C  CD1 . LEU C 1 125 ? 13.644  22.833  -78.588  1.00 29.28  ? 117 LEU C CD1 1 
ATOM   3839 C  CD2 . LEU C 1 125 ? 14.570  23.165  -76.298  1.00 27.79  ? 117 LEU C CD2 1 
ATOM   3840 N  N   . ILE C 1 126 ? 9.907   22.068  -78.126  1.00 30.87  ? 118 ILE C N   1 
ATOM   3841 C  CA  . ILE C 1 126 ? 9.098   20.876  -77.909  1.00 29.37  ? 118 ILE C CA  1 
ATOM   3842 C  C   . ILE C 1 126 ? 10.008  19.681  -78.123  1.00 28.61  ? 118 ILE C C   1 
ATOM   3843 O  O   . ILE C 1 126 ? 10.797  19.670  -79.075  1.00 28.54  ? 118 ILE C O   1 
ATOM   3844 C  CB  . ILE C 1 126 ? 7.891   20.831  -78.865  1.00 31.70  ? 118 ILE C CB  1 
ATOM   3845 C  CG1 . ILE C 1 126 ? 7.098   22.134  -78.782  1.00 25.66  ? 118 ILE C CG1 1 
ATOM   3846 C  CG2 . ILE C 1 126 ? 6.972   19.660  -78.510  1.00 28.93  ? 118 ILE C CG2 1 
ATOM   3847 C  CD1 . ILE C 1 126 ? 5.991   22.232  -79.811  1.00 42.05  ? 118 ILE C CD1 1 
ATOM   3848 N  N   . SER C 1 127 ? 9.917   18.684  -77.239  1.00 19.02  ? 119 SER C N   1 
ATOM   3849 C  CA  . SER C 1 127 ? 10.846  17.567  -77.320  1.00 19.87  ? 119 SER C CA  1 
ATOM   3850 C  C   . SER C 1 127 ? 10.163  16.258  -76.948  1.00 27.25  ? 119 SER C C   1 
ATOM   3851 O  O   . SER C 1 127 ? 9.217   16.235  -76.158  1.00 29.05  ? 119 SER C O   1 
ATOM   3852 C  CB  . SER C 1 127 ? 12.045  17.824  -76.406  1.00 25.84  ? 119 SER C CB  1 
ATOM   3853 O  OG  . SER C 1 127 ? 11.620  18.573  -75.273  1.00 25.53  ? 119 SER C OG  1 
ATOM   3854 N  N   . GLY C 1 128 ? 10.682  15.165  -77.495  1.00 22.12  ? 120 GLY C N   1 
ATOM   3855 C  CA  . GLY C 1 128 ? 10.096  13.862  -77.272  1.00 19.04  ? 120 GLY C CA  1 
ATOM   3856 C  C   . GLY C 1 128 ? 10.691  12.831  -78.202  1.00 24.89  ? 120 GLY C C   1 
ATOM   3857 O  O   . GLY C 1 128 ? 11.442  13.146  -79.128  1.00 27.91  ? 120 GLY C O   1 
ATOM   3858 N  N   . TRP C 1 129 ? 10.327  11.574  -77.937  1.00 22.24  ? 121 TRP C N   1 
ATOM   3859 C  CA  . TRP C 1 129 ? 10.791  10.428  -78.708  1.00 22.82  ? 121 TRP C CA  1 
ATOM   3860 C  C   . TRP C 1 129 ? 9.717   9.881   -79.649  1.00 19.94  ? 121 TRP C C   1 
ATOM   3861 O  O   . TRP C 1 129 ? 9.827   8.740   -80.115  1.00 20.38  ? 121 TRP C O   1 
ATOM   3862 C  CB  . TRP C 1 129 ? 11.268  9.319   -77.764  1.00 21.35  ? 121 TRP C CB  1 
ATOM   3863 C  CG  . TRP C 1 129 ? 12.603  9.567   -77.121  1.00 25.65  ? 121 TRP C CG  1 
ATOM   3864 C  CD1 . TRP C 1 129 ? 13.834  9.308   -77.658  1.00 24.59  ? 121 TRP C CD1 1 
ATOM   3865 C  CD2 . TRP C 1 129 ? 12.841  10.117  -75.813  1.00 22.13  ? 121 TRP C CD2 1 
ATOM   3866 N  NE1 . TRP C 1 129 ? 14.826  9.661   -76.762  1.00 22.86  ? 121 TRP C NE1 1 
ATOM   3867 C  CE2 . TRP C 1 129 ? 14.245  10.160  -75.626  1.00 21.62  ? 121 TRP C CE2 1 
ATOM   3868 C  CE3 . TRP C 1 129 ? 12.006  10.577  -74.785  1.00 19.59  ? 121 TRP C CE3 1 
ATOM   3869 C  CZ2 . TRP C 1 129 ? 14.835  10.654  -74.456  1.00 21.89  ? 121 TRP C CZ2 1 
ATOM   3870 C  CZ3 . TRP C 1 129 ? 12.594  11.060  -73.610  1.00 27.95  ? 121 TRP C CZ3 1 
ATOM   3871 C  CH2 . TRP C 1 129 ? 14.002  11.097  -73.463  1.00 21.67  ? 121 TRP C CH2 1 
ATOM   3872 N  N   . GLY C 1 130 ? 8.685   10.665  -79.939  1.00 21.17  ? 122 GLY C N   1 
ATOM   3873 C  CA  . GLY C 1 130 ? 7.613   10.216  -80.807  1.00 25.50  ? 122 GLY C CA  1 
ATOM   3874 C  C   . GLY C 1 130 ? 8.007   10.039  -82.275  1.00 25.73  ? 122 GLY C C   1 
ATOM   3875 O  O   . GLY C 1 130 ? 9.134   10.284  -82.704  1.00 23.61  ? 122 GLY C O   1 
ATOM   3876 N  N   . ASN C 1 131 ? 7.012   9.624   -83.060  1.00 31.76  ? 123 ASN C N   1 
ATOM   3877 C  CA  . ASN C 1 131 ? 7.186   9.343   -84.481  1.00 28.44  ? 123 ASN C CA  1 
ATOM   3878 C  C   . ASN C 1 131 ? 7.744   10.550  -85.227  1.00 25.96  ? 123 ASN C C   1 
ATOM   3879 O  O   . ASN C 1 131 ? 7.296   11.679  -85.039  1.00 28.69  ? 123 ASN C O   1 
ATOM   3880 C  CB  . ASN C 1 131 ? 5.835   8.924   -85.074  1.00 28.93  ? 123 ASN C CB  1 
ATOM   3881 C  CG  . ASN C 1 131 ? 5.953   8.227   -86.436  1.00 35.05  ? 123 ASN C CG  1 
ATOM   3882 O  OD1 . ASN C 1 131 ? 7.041   8.059   -86.986  1.00 37.49  ? 123 ASN C OD1 1 
ATOM   3883 N  ND2 . ASN C 1 131 ? 4.812   7.782   -86.961  1.00 32.40  ? 123 ASN C ND2 1 
ATOM   3884 N  N   . THR C 1 132 ? 8.723   10.306  -86.087  1.00 28.75  ? 124 THR C N   1 
ATOM   3885 C  CA  . THR C 1 132 ? 9.308   11.362  -86.898  1.00 35.81  ? 124 THR C CA  1 
ATOM   3886 C  C   . THR C 1 132 ? 8.712   11.449  -88.300  1.00 35.82  ? 124 THR C C   1 
ATOM   3887 O  O   . THR C 1 132 ? 9.091   12.348  -89.052  1.00 33.30  ? 124 THR C O   1 
ATOM   3888 C  CB  . THR C 1 132 ? 10.826  11.172  -86.997  1.00 37.51  ? 124 THR C CB  1 
ATOM   3889 O  OG1 . THR C 1 132 ? 11.107  9.951   -87.685  1.00 34.89  ? 124 THR C OG1 1 
ATOM   3890 C  CG2 . THR C 1 132 ? 11.463  11.142  -85.591  1.00 34.79  ? 124 THR C CG2 1 
ATOM   3891 N  N   . LYS C 1 133 ? 7.775   10.568  -88.656  1.00 30.93  ? 125 LYS C N   1 
ATOM   3892 C  CA  . LYS C 1 133 ? 7.199   10.497  -89.996  1.00 41.33  ? 125 LYS C CA  1 
ATOM   3893 C  C   . LYS C 1 133 ? 5.748   10.971  -89.985  1.00 38.91  ? 125 LYS C C   1 
ATOM   3894 O  O   . LYS C 1 133 ? 4.962   10.560  -89.122  1.00 38.00  ? 125 LYS C O   1 
ATOM   3895 C  CB  . LYS C 1 133 ? 7.258   9.065   -90.537  1.00 36.32  ? 125 LYS C CB  1 
ATOM   3896 C  CG  . LYS C 1 133 ? 8.525   8.693   -91.288  1.00 42.76  ? 125 LYS C CG  1 
ATOM   3897 C  CD  . LYS C 1 133 ? 8.268   7.500   -92.228  1.00 52.23  ? 125 LYS C CD  1 
ATOM   3898 C  CE  . LYS C 1 133 ? 8.973   7.644   -93.575  1.00 55.97  ? 125 LYS C CE  1 
ATOM   3899 N  NZ  . LYS C 1 133 ? 8.037   7.566   -94.741  1.00 76.27  ? 125 LYS C NZ  1 
ATOM   3900 N  N   . SER C 1 134 ? 5.385   11.804  -90.969  1.00 44.05  ? 126 SER C N   1 
ATOM   3901 C  CA  . SER C 1 134 ? 4.003   12.263  -91.109  1.00 48.09  ? 126 SER C CA  1 
ATOM   3902 C  C   . SER C 1 134 ? 3.109   11.265  -91.834  1.00 47.89  ? 126 SER C C   1 
ATOM   3903 O  O   . SER C 1 134 ? 1.894   11.482  -91.880  1.00 53.47  ? 126 SER C O   1 
ATOM   3904 C  CB  . SER C 1 134 ? 3.942   13.616  -91.836  1.00 39.13  ? 126 SER C CB  1 
ATOM   3905 O  OG  . SER C 1 134 ? 5.140   13.918  -92.534  1.00 57.95  ? 126 SER C OG  1 
ATOM   3906 N  N   . SER C 1 135 ? 3.665   10.178  -92.378  1.00 53.35  ? 127 SER C N   1 
ATOM   3907 C  CA  . SER C 1 135 ? 2.903   9.195   -93.147  1.00 51.53  ? 127 SER C CA  1 
ATOM   3908 C  C   . SER C 1 135 ? 3.009   7.786   -92.585  1.00 53.38  ? 127 SER C C   1 
ATOM   3909 O  O   . SER C 1 135 ? 1.980   7.165   -92.292  1.00 67.22  ? 127 SER C O   1 
ATOM   3910 C  CB  . SER C 1 135 ? 3.355   9.201   -94.618  1.00 64.49  ? 127 SER C CB  1 
ATOM   3911 O  OG  . SER C 1 135 ? 2.278   8.875   -95.479  1.00 72.99  ? 127 SER C OG  1 
ATOM   3912 N  N   . GLY C 1 136 ? 4.217   7.247   -92.440  1.00 44.06  ? 128 GLY C N   1 
ATOM   3913 C  CA  . GLY C 1 136 ? 4.369   5.930   -91.846  1.00 43.66  ? 128 GLY C CA  1 
ATOM   3914 C  C   . GLY C 1 136 ? 4.750   5.960   -90.376  1.00 46.42  ? 128 GLY C C   1 
ATOM   3915 O  O   . GLY C 1 136 ? 4.143   6.687   -89.579  1.00 45.08  ? 128 GLY C O   1 
ATOM   3916 N  N   . SER C 1 137 ? 5.751   5.164   -90.001  1.00 42.42  ? 129 SER C N   1 
ATOM   3917 C  CA  . SER C 1 137 ? 6.217   5.077   -88.618  1.00 43.90  ? 129 SER C CA  1 
ATOM   3918 C  C   . SER C 1 137 ? 7.736   4.999   -88.615  1.00 44.76  ? 129 SER C C   1 
ATOM   3919 O  O   . SER C 1 137 ? 8.319   4.146   -89.295  1.00 39.01  ? 129 SER C O   1 
ATOM   3920 C  CB  . SER C 1 137 ? 5.620   3.861   -87.902  1.00 44.00  ? 129 SER C CB  1 
ATOM   3921 O  OG  . SER C 1 137 ? 4.211   3.988   -87.756  1.00 64.49  ? 129 SER C OG  1 
ATOM   3922 N  N   . SER C 1 138 ? 8.378   5.889   -87.863  1.00 37.99  ? 130 SER C N   1 
ATOM   3923 C  CA  . SER C 1 138 ? 9.837   5.847   -87.730  1.00 45.39  ? 130 SER C CA  1 
ATOM   3924 C  C   . SER C 1 138 ? 10.212  6.477   -86.391  1.00 37.96  ? 130 SER C C   1 
ATOM   3925 O  O   . SER C 1 138 ? 10.353  7.702   -86.292  1.00 41.57  ? 130 SER C O   1 
ATOM   3926 C  CB  . SER C 1 138 ? 10.527  6.552   -88.888  1.00 41.49  ? 130 SER C CB  1 
ATOM   3927 O  OG  . SER C 1 138 ? 11.824  6.012   -89.064  1.00 57.14  ? 130 SER C OG  1 
ATOM   3928 N  N   . TYR C 1 139 ? 10.405  5.645   -85.402  1.00 28.23  ? 131 TYR C N   1 
ATOM   3929 C  CA  . TYR C 1 139 ? 10.648  6.088   -84.035  1.00 34.52  ? 131 TYR C CA  1 
ATOM   3930 C  C   . TYR C 1 139 ? 12.139  6.239   -83.773  1.00 31.70  ? 131 TYR C C   1 
ATOM   3931 O  O   . TYR C 1 139 ? 12.905  5.305   -84.031  1.00 40.09  ? 131 TYR C O   1 
ATOM   3932 C  CB  . TYR C 1 139 ? 10.029  5.110   -83.054  1.00 24.24  ? 131 TYR C CB  1 
ATOM   3933 C  CG  . TYR C 1 139 ? 8.533   5.282   -83.039  1.00 32.34  ? 131 TYR C CG  1 
ATOM   3934 C  CD1 . TYR C 1 139 ? 7.722   4.599   -83.954  1.00 37.23  ? 131 TYR C CD1 1 
ATOM   3935 C  CD2 . TYR C 1 139 ? 7.925   6.184   -82.165  1.00 28.99  ? 131 TYR C CD2 1 
ATOM   3936 C  CE1 . TYR C 1 139 ? 6.341   4.767   -83.963  1.00 26.06  ? 131 TYR C CE1 1 
ATOM   3937 C  CE2 . TYR C 1 139 ? 6.540   6.366   -82.167  1.00 25.74  ? 131 TYR C CE2 1 
ATOM   3938 C  CZ  . TYR C 1 139 ? 5.757   5.659   -83.070  1.00 28.91  ? 131 TYR C CZ  1 
ATOM   3939 O  OH  . TYR C 1 139 ? 4.392   5.836   -83.074  1.00 32.78  ? 131 TYR C OH  1 
ATOM   3940 N  N   . PRO C 1 140 ? 12.570  7.388   -83.264  1.00 29.12  ? 132 PRO C N   1 
ATOM   3941 C  CA  . PRO C 1 140 ? 13.997  7.645   -83.020  1.00 21.35  ? 132 PRO C CA  1 
ATOM   3942 C  C   . PRO C 1 140 ? 14.512  7.104   -81.691  1.00 25.48  ? 132 PRO C C   1 
ATOM   3943 O  O   . PRO C 1 140 ? 13.801  7.034   -80.687  1.00 28.50  ? 132 PRO C O   1 
ATOM   3944 C  CB  . PRO C 1 140 ? 14.049  9.177   -83.011  1.00 24.76  ? 132 PRO C CB  1 
ATOM   3945 C  CG  . PRO C 1 140 ? 12.717  9.551   -82.321  1.00 26.51  ? 132 PRO C CG  1 
ATOM   3946 C  CD  . PRO C 1 140 ? 11.715  8.517   -82.853  1.00 26.54  ? 132 PRO C CD  1 
ATOM   3947 N  N   . SER C 1 141 ? 15.790  6.730   -81.690  1.00 29.17  ? 133 SER C N   1 
ATOM   3948 C  CA  . SER C 1 141 ? 16.463  6.404   -80.435  1.00 27.79  ? 133 SER C CA  1 
ATOM   3949 C  C   . SER C 1 141 ? 16.851  7.659   -79.663  1.00 25.27  ? 133 SER C C   1 
ATOM   3950 O  O   . SER C 1 141 ? 16.900  7.642   -78.427  1.00 23.87  ? 133 SER C O   1 
ATOM   3951 C  CB  . SER C 1 141 ? 17.706  5.558   -80.708  1.00 25.76  ? 133 SER C CB  1 
ATOM   3952 O  OG  . SER C 1 141 ? 17.353  4.196   -80.827  1.00 27.28  ? 133 SER C OG  1 
ATOM   3953 N  N   . LEU C 1 142 ? 17.091  8.757   -80.370  1.00 23.33  ? 134 LEU C N   1 
ATOM   3954 C  CA  . LEU C 1 142 ? 17.690  9.946   -79.800  1.00 28.42  ? 134 LEU C CA  1 
ATOM   3955 C  C   . LEU C 1 142 ? 16.637  11.028  -79.670  1.00 23.89  ? 134 LEU C C   1 
ATOM   3956 O  O   . LEU C 1 142 ? 15.828  11.218  -80.582  1.00 24.05  ? 134 LEU C O   1 
ATOM   3957 C  CB  . LEU C 1 142 ? 18.838  10.447  -80.670  1.00 30.32  ? 134 LEU C CB  1 
ATOM   3958 C  CG  . LEU C 1 142 ? 20.029  9.508   -80.723  1.00 32.13  ? 134 LEU C CG  1 
ATOM   3959 C  CD1 . LEU C 1 142 ? 21.089  10.095  -81.631  1.00 32.27  ? 134 LEU C CD1 1 
ATOM   3960 C  CD2 . LEU C 1 142 ? 20.555  9.274   -79.334  1.00 32.44  ? 134 LEU C CD2 1 
ATOM   3961 N  N   . LEU C 1 143 ? 16.646  11.722  -78.529  1.00 21.50  ? 135 LEU C N   1 
ATOM   3962 C  CA  . LEU C 1 143 ? 15.641  12.742  -78.262  1.00 24.46  ? 135 LEU C CA  1 
ATOM   3963 C  C   . LEU C 1 143 ? 15.573  13.731  -79.419  1.00 23.91  ? 135 LEU C C   1 
ATOM   3964 O  O   . LEU C 1 143 ? 16.603  14.159  -79.947  1.00 31.22  ? 135 LEU C O   1 
ATOM   3965 C  CB  . LEU C 1 143 ? 15.975  13.465  -76.964  1.00 23.94  ? 135 LEU C CB  1 
ATOM   3966 C  CG  . LEU C 1 143 ? 14.915  14.364  -76.346  1.00 23.62  ? 135 LEU C CG  1 
ATOM   3967 C  CD1 . LEU C 1 143 ? 13.622  13.592  -76.065  1.00 22.89  ? 135 LEU C CD1 1 
ATOM   3968 C  CD2 . LEU C 1 143 ? 15.485  14.921  -75.058  1.00 21.06  ? 135 LEU C CD2 1 
ATOM   3969 N  N   . GLN C 1 144 ? 14.355  14.063  -79.838  1.00 17.73  ? 136 GLN C N   1 
ATOM   3970 C  CA  . GLN C 1 144 ? 14.119  14.992  -80.938  1.00 25.37  ? 136 GLN C CA  1 
ATOM   3971 C  C   . GLN C 1 144 ? 13.638  16.331  -80.399  1.00 30.44  ? 136 GLN C C   1 
ATOM   3972 O  O   . GLN C 1 144 ? 12.928  16.393  -79.389  1.00 34.57  ? 136 GLN C O   1 
ATOM   3973 C  CB  . GLN C 1 144 ? 13.075  14.444  -81.915  1.00 24.88  ? 136 GLN C CB  1 
ATOM   3974 C  CG  . GLN C 1 144 ? 13.531  13.238  -82.639  1.00 20.76  ? 136 GLN C CG  1 
ATOM   3975 C  CD  . GLN C 1 144 ? 14.745  13.537  -83.483  1.00 26.34  ? 136 GLN C CD  1 
ATOM   3976 O  OE1 . GLN C 1 144 ? 14.704  14.400  -84.366  1.00 28.22  ? 136 GLN C OE1 1 
ATOM   3977 N  NE2 . GLN C 1 144 ? 15.842  12.849  -83.203  1.00 21.26  ? 136 GLN C NE2 1 
ATOM   3978 N  N   . CYS C 1 145 ? 14.002  17.401  -81.098  1.00 29.16  ? 137 CYS C N   1 
ATOM   3979 C  CA  . CYS C 1 145 ? 13.688  18.759  -80.663  1.00 27.16  ? 137 CYS C CA  1 
ATOM   3980 C  C   . CYS C 1 145 ? 12.961  19.504  -81.776  1.00 30.19  ? 137 CYS C C   1 
ATOM   3981 O  O   . CYS C 1 145 ? 13.142  19.219  -82.964  1.00 32.07  ? 137 CYS C O   1 
ATOM   3982 C  CB  . CYS C 1 145 ? 14.961  19.541  -80.272  1.00 28.56  ? 137 CYS C CB  1 
ATOM   3983 S  SG  . CYS C 1 145 ? 15.528  19.282  -78.560  1.00 45.21  ? 137 CYS C SG  1 
ATOM   3984 N  N   . LEU C 1 146 ? 12.142  20.472  -81.384  1.00 26.43  ? 138 LEU C N   1 
ATOM   3985 C  CA  . LEU C 1 146 ? 11.427  21.284  -82.355  1.00 33.50  ? 138 LEU C CA  1 
ATOM   3986 C  C   . LEU C 1 146 ? 11.156  22.645  -81.741  1.00 38.56  ? 138 LEU C C   1 
ATOM   3987 O  O   . LEU C 1 146 ? 10.541  22.741  -80.673  1.00 33.82  ? 138 LEU C O   1 
ATOM   3988 C  CB  . LEU C 1 146 ? 10.123  20.627  -82.783  1.00 35.00  ? 138 LEU C CB  1 
ATOM   3989 C  CG  . LEU C 1 146 ? 9.341   21.518  -83.750  1.00 37.67  ? 138 LEU C CG  1 
ATOM   3990 C  CD1 . LEU C 1 146 ? 9.998   21.494  -85.152  1.00 34.84  ? 138 LEU C CD1 1 
ATOM   3991 C  CD2 . LEU C 1 146 ? 7.869   21.123  -83.811  1.00 27.82  ? 138 LEU C CD2 1 
ATOM   3992 N  N   . LYS C 1 147 ? 11.644  23.684  -82.405  1.00 43.23  ? 139 LYS C N   1 
ATOM   3993 C  CA  . LYS C 1 147 ? 11.296  25.053  -82.072  1.00 33.71  ? 139 LYS C CA  1 
ATOM   3994 C  C   . LYS C 1 147 ? 10.012  25.383  -82.817  1.00 33.82  ? 139 LYS C C   1 
ATOM   3995 O  O   . LYS C 1 147 ? 9.885   25.072  -84.007  1.00 29.64  ? 139 LYS C O   1 
ATOM   3996 C  CB  . LYS C 1 147 ? 12.437  26.007  -82.438  1.00 37.24  ? 139 LYS C CB  1 
ATOM   3997 C  CG  . LYS C 1 147 ? 13.604  25.932  -81.442  1.00 42.37  ? 139 LYS C CG  1 
ATOM   3998 C  CD  . LYS C 1 147 ? 14.787  26.815  -81.799  1.00 48.12  ? 139 LYS C CD  1 
ATOM   3999 C  CE  . LYS C 1 147 ? 16.119  26.184  -81.350  1.00 56.79  ? 139 LYS C CE  1 
ATOM   4000 N  NZ  . LYS C 1 147 ? 17.194  26.136  -82.418  1.00 43.20  ? 139 LYS C NZ  1 
ATOM   4001 N  N   . ALA C 1 148 ? 9.028   25.915  -82.093  1.00 31.60  ? 140 ALA C N   1 
ATOM   4002 C  CA  . ALA C 1 148 ? 7.745   26.222  -82.704  1.00 28.01  ? 140 ALA C CA  1 
ATOM   4003 C  C   . ALA C 1 148 ? 7.032   27.263  -81.852  1.00 39.52  ? 140 ALA C C   1 
ATOM   4004 O  O   . ALA C 1 148 ? 7.300   27.360  -80.648  1.00 39.57  ? 140 ALA C O   1 
ATOM   4005 C  CB  . ALA C 1 148 ? 6.887   24.965  -82.859  1.00 25.28  ? 140 ALA C CB  1 
ATOM   4006 N  N   . PRO C 1 149 ? 6.141   28.082  -82.456  1.00 37.02  ? 141 PRO C N   1 
ATOM   4007 C  CA  . PRO C 1 149 ? 5.457   29.128  -81.691  1.00 37.49  ? 141 PRO C CA  1 
ATOM   4008 C  C   . PRO C 1 149 ? 4.073   28.740  -81.198  1.00 35.59  ? 141 PRO C C   1 
ATOM   4009 O  O   . PRO C 1 149 ? 3.364   27.955  -81.841  1.00 33.27  ? 141 PRO C O   1 
ATOM   4010 C  CB  . PRO C 1 149 ? 5.348   30.259  -82.712  1.00 44.42  ? 141 PRO C CB  1 
ATOM   4011 C  CG  . PRO C 1 149 ? 5.090   29.496  -84.018  1.00 35.03  ? 141 PRO C CG  1 
ATOM   4012 C  CD  . PRO C 1 149 ? 5.821   28.177  -83.898  1.00 28.89  ? 141 PRO C CD  1 
ATOM   4013 N  N   . VAL C 1 150 ? 3.671   29.323  -80.069  1.00 40.33  ? 142 VAL C N   1 
ATOM   4014 C  CA  . VAL C 1 150 ? 2.295   29.187  -79.600  1.00 40.02  ? 142 VAL C CA  1 
ATOM   4015 C  C   . VAL C 1 150 ? 1.368   29.847  -80.610  1.00 36.90  ? 142 VAL C C   1 
ATOM   4016 O  O   . VAL C 1 150 ? 1.491   31.042  -80.899  1.00 40.86  ? 142 VAL C O   1 
ATOM   4017 C  CB  . VAL C 1 150 ? 2.125   29.812  -78.215  1.00 27.25  ? 142 VAL C CB  1 
ATOM   4018 C  CG1 . VAL C 1 150 ? 0.744   29.523  -77.692  1.00 27.57  ? 142 VAL C CG1 1 
ATOM   4019 C  CG2 . VAL C 1 150 ? 3.174   29.304  -77.275  1.00 30.82  ? 142 VAL C CG2 1 
ATOM   4020 N  N   . LEU C 1 151 ? 0.436   29.072  -81.152  1.00 42.52  ? 143 LEU C N   1 
ATOM   4021 C  CA  . LEU C 1 151 ? -0.540  29.628  -82.069  1.00 35.83  ? 143 LEU C CA  1 
ATOM   4022 C  C   . LEU C 1 151 ? -1.617  30.369  -81.299  1.00 35.41  ? 143 LEU C C   1 
ATOM   4023 O  O   . LEU C 1 151 ? -1.795  30.177  -80.101  1.00 42.89  ? 143 LEU C O   1 
ATOM   4024 C  CB  . LEU C 1 151 ? -1.184  28.537  -82.917  1.00 37.13  ? 143 LEU C CB  1 
ATOM   4025 C  CG  . LEU C 1 151 ? -0.516  28.263  -84.256  1.00 43.60  ? 143 LEU C CG  1 
ATOM   4026 C  CD1 . LEU C 1 151 ? 0.912   28.814  -84.294  1.00 27.74  ? 143 LEU C CD1 1 
ATOM   4027 C  CD2 . LEU C 1 151 ? -0.565  26.769  -84.540  1.00 39.96  ? 143 LEU C CD2 1 
ATOM   4028 N  N   . SER C 1 152 ? -2.347  31.215  -82.017  1.00 38.73  ? 144 SER C N   1 
ATOM   4029 C  CA  . SER C 1 152 ? -3.409  32.010  -81.424  1.00 43.05  ? 144 SER C CA  1 
ATOM   4030 C  C   . SER C 1 152 ? -4.624  31.146  -81.104  1.00 46.28  ? 144 SER C C   1 
ATOM   4031 O  O   . SER C 1 152 ? -4.897  30.147  -81.776  1.00 49.38  ? 144 SER C O   1 
ATOM   4032 C  CB  . SER C 1 152 ? -3.801  33.132  -82.378  1.00 42.29  ? 144 SER C CB  1 
ATOM   4033 O  OG  . SER C 1 152 ? -4.896  32.720  -83.176  1.00 47.50  ? 144 SER C OG  1 
ATOM   4034 N  N   . ASP C 1 153 ? -5.359  31.539  -80.059  1.00 49.70  ? 145 ASP C N   1 
ATOM   4035 C  CA  . ASP C 1 153 ? -6.561  30.798  -79.695  1.00 46.13  ? 145 ASP C CA  1 
ATOM   4036 C  C   . ASP C 1 153 ? -7.553  30.773  -80.846  1.00 52.78  ? 145 ASP C C   1 
ATOM   4037 O  O   . ASP C 1 153 ? -8.187  29.744  -81.098  1.00 51.59  ? 145 ASP C O   1 
ATOM   4038 C  CB  . ASP C 1 153 ? -7.201  31.387  -78.439  1.00 52.48  ? 145 ASP C CB  1 
ATOM   4039 C  CG  . ASP C 1 153 ? -7.638  30.313  -77.446  1.00 80.57  ? 145 ASP C CG  1 
ATOM   4040 O  OD1 . ASP C 1 153 ? -7.088  29.182  -77.486  1.00 81.00  ? 145 ASP C OD1 1 
ATOM   4041 O  OD2 . ASP C 1 153 ? -8.528  30.606  -76.616  1.00 94.07  ? 145 ASP C OD2 1 
ATOM   4042 N  N   . SER C 1 154 ? -7.668  31.878  -81.590  1.00 42.52  ? 146 SER C N   1 
ATOM   4043 C  CA  . SER C 1 154 ? -8.571  31.895  -82.738  1.00 49.03  ? 146 SER C CA  1 
ATOM   4044 C  C   . SER C 1 154 ? -8.159  30.853  -83.778  1.00 47.77  ? 146 SER C C   1 
ATOM   4045 O  O   . SER C 1 154 ? -8.987  30.063  -84.263  1.00 37.75  ? 146 SER C O   1 
ATOM   4046 C  CB  . SER C 1 154 ? -8.602  33.299  -83.346  1.00 52.17  ? 146 SER C CB  1 
ATOM   4047 O  OG  . SER C 1 154 ? -8.796  33.247  -84.746  1.00 55.08  ? 146 SER C OG  1 
ATOM   4048 N  N   . SER C 1 155 ? -6.872  30.827  -84.116  1.00 39.68  ? 147 SER C N   1 
ATOM   4049 C  CA  . SER C 1 155 ? -6.372  29.852  -85.077  1.00 41.55  ? 147 SER C CA  1 
ATOM   4050 C  C   . SER C 1 155 ? -6.552  28.425  -84.569  1.00 45.53  ? 147 SER C C   1 
ATOM   4051 O  O   . SER C 1 155 ? -6.785  27.500  -85.362  1.00 41.48  ? 147 SER C O   1 
ATOM   4052 C  CB  . SER C 1 155 ? -4.901  30.148  -85.366  1.00 41.01  ? 147 SER C CB  1 
ATOM   4053 O  OG  . SER C 1 155 ? -4.473  29.494  -86.544  1.00 59.67  ? 147 SER C OG  1 
ATOM   4054 N  N   . CYS C 1 156 ? -6.465  28.238  -83.248  1.00 49.41  ? 148 CYS C N   1 
ATOM   4055 C  CA  . CYS C 1 156 ? -6.551  26.908  -82.653  1.00 44.80  ? 148 CYS C CA  1 
ATOM   4056 C  C   . CYS C 1 156 ? -7.980  26.374  -82.724  1.00 36.74  ? 148 CYS C C   1 
ATOM   4057 O  O   . CYS C 1 156 ? -8.206  25.256  -83.191  1.00 40.43  ? 148 CYS C O   1 
ATOM   4058 C  CB  . CYS C 1 156 ? -6.035  26.963  -81.204  1.00 42.05  ? 148 CYS C CB  1 
ATOM   4059 S  SG  . CYS C 1 156 ? -5.746  25.379  -80.355  1.00 49.52  ? 148 CYS C SG  1 
ATOM   4060 N  N   . LYS C 1 157 ? -8.964  27.167  -82.275  1.00 42.42  ? 149 LYS C N   1 
ATOM   4061 C  CA  . LYS C 1 157 ? -10.361 26.756  -82.408  1.00 38.56  ? 149 LYS C CA  1 
ATOM   4062 C  C   . LYS C 1 157 ? -10.773 26.644  -83.868  1.00 40.97  ? 149 LYS C C   1 
ATOM   4063 O  O   . LYS C 1 157 ? -11.636 25.829  -84.208  1.00 49.30  ? 149 LYS C O   1 
ATOM   4064 C  CB  . LYS C 1 157 ? -11.294 27.735  -81.687  1.00 41.11  ? 149 LYS C CB  1 
ATOM   4065 C  CG  . LYS C 1 157 ? -10.697 28.426  -80.479  1.00 47.92  ? 149 LYS C CG  1 
ATOM   4066 C  CD  . LYS C 1 157 ? -11.721 29.172  -79.638  1.00 51.75  ? 149 LYS C CD  1 
ATOM   4067 C  CE  . LYS C 1 157 ? -11.303 29.213  -78.170  1.00 64.52  ? 149 LYS C CE  1 
ATOM   4068 N  NZ  . LYS C 1 157 ? -10.744 30.548  -77.797  1.00 66.83  ? 149 LYS C NZ  1 
ATOM   4069 N  N   . SER C 1 158 ? -10.166 27.446  -84.745  1.00 43.86  ? 150 SER C N   1 
ATOM   4070 C  CA  . SER C 1 158 ? -10.456 27.332  -86.170  1.00 41.73  ? 150 SER C CA  1 
ATOM   4071 C  C   . SER C 1 158 ? -9.898  26.046  -86.768  1.00 46.68  ? 150 SER C C   1 
ATOM   4072 O  O   . SER C 1 158 ? -10.473 25.508  -87.721  1.00 38.25  ? 150 SER C O   1 
ATOM   4073 C  CB  . SER C 1 158 ? -9.890  28.537  -86.912  1.00 37.25  ? 150 SER C CB  1 
ATOM   4074 O  OG  . SER C 1 158 ? -10.572 28.712  -88.133  1.00 61.90  ? 150 SER C OG  1 
ATOM   4075 N  N   . SER C 1 159 ? -8.774  25.550  -86.243  1.00 45.77  ? 151 SER C N   1 
ATOM   4076 C  CA  . SER C 1 159 ? -8.190  24.322  -86.767  1.00 38.90  ? 151 SER C CA  1 
ATOM   4077 C  C   . SER C 1 159 ? -8.945  23.090  -86.295  1.00 38.85  ? 151 SER C C   1 
ATOM   4078 O  O   . SER C 1 159 ? -8.977  22.078  -87.008  1.00 35.97  ? 151 SER C O   1 
ATOM   4079 C  CB  . SER C 1 159 ? -6.729  24.212  -86.345  1.00 31.92  ? 151 SER C CB  1 
ATOM   4080 O  OG  . SER C 1 159 ? -5.881  24.803  -87.312  1.00 52.53  ? 151 SER C OG  1 
ATOM   4081 N  N   . TYR C 1 160 ? -9.538  23.159  -85.103  1.00 36.65  ? 152 TYR C N   1 
ATOM   4082 C  CA  . TYR C 1 160 ? -10.246 22.042  -84.476  1.00 41.31  ? 152 TYR C CA  1 
ATOM   4083 C  C   . TYR C 1 160 ? -11.596 22.535  -83.984  1.00 44.46  ? 152 TYR C C   1 
ATOM   4084 O  O   . TYR C 1 160 ? -11.796 22.722  -82.778  1.00 45.08  ? 152 TYR C O   1 
ATOM   4085 C  CB  . TYR C 1 160 ? -9.454  21.457  -83.307  1.00 35.88  ? 152 TYR C CB  1 
ATOM   4086 C  CG  . TYR C 1 160 ? -8.136  20.833  -83.679  1.00 37.70  ? 152 TYR C CG  1 
ATOM   4087 C  CD1 . TYR C 1 160 ? -8.076  19.536  -84.184  1.00 38.38  ? 152 TYR C CD1 1 
ATOM   4088 C  CD2 . TYR C 1 160 ? -6.947  21.534  -83.524  1.00 26.60  ? 152 TYR C CD2 1 
ATOM   4089 C  CE1 . TYR C 1 160 ? -6.863  18.951  -84.525  1.00 29.62  ? 152 TYR C CE1 1 
ATOM   4090 C  CE2 . TYR C 1 160 ? -5.733  20.958  -83.869  1.00 32.82  ? 152 TYR C CE2 1 
ATOM   4091 C  CZ  . TYR C 1 160 ? -5.704  19.666  -84.363  1.00 28.66  ? 152 TYR C CZ  1 
ATOM   4092 O  OH  . TYR C 1 160 ? -4.505  19.084  -84.689  1.00 33.80  ? 152 TYR C OH  1 
ATOM   4093 N  N   . PRO C 1 161 ? -12.547 22.754  -84.892  1.00 45.65  ? 153 PRO C N   1 
ATOM   4094 C  CA  . PRO C 1 161 ? -13.879 23.202  -84.474  1.00 35.85  ? 153 PRO C CA  1 
ATOM   4095 C  C   . PRO C 1 161 ? -14.520 22.232  -83.493  1.00 40.57  ? 153 PRO C C   1 
ATOM   4096 O  O   . PRO C 1 161 ? -14.636 21.029  -83.753  1.00 37.90  ? 153 PRO C O   1 
ATOM   4097 C  CB  . PRO C 1 161 ? -14.652 23.265  -85.796  1.00 41.02  ? 153 PRO C CB  1 
ATOM   4098 C  CG  . PRO C 1 161 ? -13.594 23.519  -86.800  1.00 46.91  ? 153 PRO C CG  1 
ATOM   4099 C  CD  . PRO C 1 161 ? -12.458 22.651  -86.358  1.00 37.67  ? 153 PRO C CD  1 
ATOM   4100 N  N   . GLY C 1 162 ? -14.930 22.771  -82.349  1.00 46.37  ? 154 GLY C N   1 
ATOM   4101 C  CA  . GLY C 1 162 ? -15.685 21.997  -81.389  1.00 42.10  ? 154 GLY C CA  1 
ATOM   4102 C  C   . GLY C 1 162 ? -14.860 21.110  -80.496  1.00 42.20  ? 154 GLY C C   1 
ATOM   4103 O  O   . GLY C 1 162 ? -15.410 20.190  -79.888  1.00 57.48  ? 154 GLY C O   1 
ATOM   4104 N  N   . GLN C 1 163 ? -13.562 21.371  -80.367  1.00 41.96  ? 155 GLN C N   1 
ATOM   4105 C  CA  . GLN C 1 163 ? -12.679 20.482  -79.626  1.00 37.74  ? 155 GLN C CA  1 
ATOM   4106 C  C   . GLN C 1 163 ? -11.755 21.177  -78.641  1.00 40.21  ? 155 GLN C C   1 
ATOM   4107 O  O   . GLN C 1 163 ? -11.225 20.492  -77.758  1.00 39.74  ? 155 GLN C O   1 
ATOM   4108 C  CB  . GLN C 1 163 ? -11.811 19.671  -80.596  1.00 39.83  ? 155 GLN C CB  1 
ATOM   4109 C  CG  . GLN C 1 163 ? -12.564 18.609  -81.341  1.00 43.48  ? 155 GLN C CG  1 
ATOM   4110 C  CD  . GLN C 1 163 ? -11.681 17.857  -82.308  1.00 42.42  ? 155 GLN C CD  1 
ATOM   4111 O  OE1 . GLN C 1 163 ? -11.396 18.323  -83.419  1.00 50.75  ? 155 GLN C OE1 1 
ATOM   4112 N  NE2 . GLN C 1 163 ? -11.235 16.684  -81.889  1.00 40.49  ? 155 GLN C NE2 1 
ATOM   4113 N  N   . ILE C 1 164 ? -11.535 22.486  -78.758  1.00 32.13  ? 156 ILE C N   1 
ATOM   4114 C  CA  . ILE C 1 164 ? -10.550 23.207  -77.961  1.00 30.02  ? 156 ILE C CA  1 
ATOM   4115 C  C   . ILE C 1 164 ? -11.256 23.846  -76.777  1.00 41.08  ? 156 ILE C C   1 
ATOM   4116 O  O   . ILE C 1 164 ? -12.201 24.622  -76.958  1.00 48.17  ? 156 ILE C O   1 
ATOM   4117 C  CB  . ILE C 1 164 ? -9.820  24.280  -78.787  1.00 32.75  ? 156 ILE C CB  1 
ATOM   4118 C  CG1 . ILE C 1 164 ? -9.239  23.703  -80.083  1.00 41.80  ? 156 ILE C CG1 1 
ATOM   4119 C  CG2 . ILE C 1 164 ? -8.730  24.917  -77.968  1.00 30.79  ? 156 ILE C CG2 1 
ATOM   4120 C  CD1 . ILE C 1 164 ? -8.254  22.591  -79.878  1.00 41.26  ? 156 ILE C CD1 1 
ATOM   4121 N  N   . THR C 1 165 ? -10.779 23.550  -75.568  1.00 44.55  ? 157 THR C N   1 
ATOM   4122 C  CA  . THR C 1 165 ? -11.216 24.229  -74.357  1.00 38.27  ? 157 THR C CA  1 
ATOM   4123 C  C   . THR C 1 165 ? -10.235 25.340  -74.008  1.00 33.51  ? 157 THR C C   1 
ATOM   4124 O  O   . THR C 1 165 ? -9.191  25.506  -74.646  1.00 35.71  ? 157 THR C O   1 
ATOM   4125 C  CB  . THR C 1 165 ? -11.320 23.258  -73.175  1.00 39.96  ? 157 THR C CB  1 
ATOM   4126 O  OG1 . THR C 1 165 ? -10.023 22.697  -72.884  1.00 36.07  ? 157 THR C OG1 1 
ATOM   4127 C  CG2 . THR C 1 165 ? -12.314 22.145  -73.473  1.00 36.93  ? 157 THR C CG2 1 
ATOM   4128 N  N   . GLY C 1 166 ? -10.558 26.076  -72.940  1.00 26.12  ? 158 GLY C N   1 
ATOM   4129 C  CA  . GLY C 1 166 ? -9.648  27.044  -72.354  1.00 28.85  ? 158 GLY C CA  1 
ATOM   4130 C  C   . GLY C 1 166 ? -8.446  26.446  -71.643  1.00 36.81  ? 158 GLY C C   1 
ATOM   4131 O  O   . GLY C 1 166 ? -7.599  27.188  -71.133  1.00 40.57  ? 158 GLY C O   1 
ATOM   4132 N  N   . ASN C 1 167 ? -8.348  25.124  -71.585  1.00 33.41  ? 159 ASN C N   1 
ATOM   4133 C  CA  . ASN C 1 167 ? -7.191  24.470  -71.005  1.00 25.44  ? 159 ASN C CA  1 
ATOM   4134 C  C   . ASN C 1 167 ? -6.276  23.885  -72.072  1.00 23.83  ? 159 ASN C C   1 
ATOM   4135 O  O   . ASN C 1 167 ? -5.318  23.189  -71.735  1.00 28.53  ? 159 ASN C O   1 
ATOM   4136 C  CB  . ASN C 1 167 ? -7.650  23.394  -70.026  1.00 28.14  ? 159 ASN C CB  1 
ATOM   4137 C  CG  . ASN C 1 167 ? -8.466  23.964  -68.875  1.00 34.61  ? 159 ASN C CG  1 
ATOM   4138 O  OD1 . ASN C 1 167 ? -8.054  24.929  -68.225  1.00 34.01  ? 159 ASN C OD1 1 
ATOM   4139 N  ND2 . ASN C 1 167 ? -9.627  23.358  -68.610  1.00 25.14  ? 159 ASN C ND2 1 
ATOM   4140 N  N   . MET C 1 168 ? -6.548  24.162  -73.350  1.00 27.50  ? 160 MET C N   1 
ATOM   4141 C  CA  . MET C 1 168 ? -5.800  23.637  -74.487  1.00 25.03  ? 160 MET C CA  1 
ATOM   4142 C  C   . MET C 1 168 ? -5.163  24.788  -75.248  1.00 28.76  ? 160 MET C C   1 
ATOM   4143 O  O   . MET C 1 168 ? -5.770  25.851  -75.404  1.00 33.27  ? 160 MET C O   1 
ATOM   4144 C  CB  . MET C 1 168 ? -6.713  22.861  -75.456  1.00 30.83  ? 160 MET C CB  1 
ATOM   4145 C  CG  . MET C 1 168 ? -7.666  21.887  -74.796  1.00 29.91  ? 160 MET C CG  1 
ATOM   4146 S  SD  . MET C 1 168 ? -8.342  20.557  -75.828  1.00 34.12  ? 160 MET C SD  1 
ATOM   4147 C  CE  . MET C 1 168 ? -9.410  19.732  -74.655  1.00 27.75  ? 160 MET C CE  1 
ATOM   4148 N  N   . ILE C 1 169 ? -3.948  24.575  -75.740  1.00 26.16  ? 161 ILE C N   1 
ATOM   4149 C  CA  . ILE C 1 169 ? -3.333  25.543  -76.631  1.00 28.81  ? 161 ILE C CA  1 
ATOM   4150 C  C   . ILE C 1 169 ? -2.817  24.787  -77.844  1.00 42.06  ? 161 ILE C C   1 
ATOM   4151 O  O   . ILE C 1 169 ? -2.602  23.571  -77.808  1.00 32.39  ? 161 ILE C O   1 
ATOM   4152 C  CB  . ILE C 1 169 ? -2.180  26.348  -75.984  1.00 30.36  ? 161 ILE C CB  1 
ATOM   4153 C  CG1 . ILE C 1 169 ? -1.222  25.434  -75.230  1.00 28.59  ? 161 ILE C CG1 1 
ATOM   4154 C  CG2 . ILE C 1 169 ? -2.732  27.430  -75.067  1.00 32.99  ? 161 ILE C CG2 1 
ATOM   4155 C  CD1 . ILE C 1 169 ? -0.038  26.183  -74.640  1.00 33.18  ? 161 ILE C CD1 1 
ATOM   4156 N  N   . CYS C 1 170 ? -2.628  25.527  -78.929  1.00 34.22  ? 162 CYS C N   1 
ATOM   4157 C  CA  . CYS C 1 170 ? -2.021  24.992  -80.132  1.00 34.69  ? 162 CYS C CA  1 
ATOM   4158 C  C   . CYS C 1 170 ? -0.616  25.552  -80.251  1.00 39.11  ? 162 CYS C C   1 
ATOM   4159 O  O   . CYS C 1 170 ? -0.388  26.736  -79.977  1.00 38.69  ? 162 CYS C O   1 
ATOM   4160 C  CB  . CYS C 1 170 ? -2.845  25.353  -81.365  1.00 39.73  ? 162 CYS C CB  1 
ATOM   4161 S  SG  . CYS C 1 170 ? -4.374  24.390  -81.509  1.00 43.67  ? 162 CYS C SG  1 
ATOM   4162 N  N   . VAL C 1 171 ? 0.328   24.693  -80.625  1.00 36.42  ? 163 VAL C N   1 
ATOM   4163 C  CA  . VAL C 1 171 ? 1.694   25.112  -80.918  1.00 34.74  ? 163 VAL C CA  1 
ATOM   4164 C  C   . VAL C 1 171 ? 2.129   24.428  -82.202  1.00 35.71  ? 163 VAL C C   1 
ATOM   4165 O  O   . VAL C 1 171 ? 1.927   23.219  -82.364  1.00 37.10  ? 163 VAL C O   1 
ATOM   4166 C  CB  . VAL C 1 171 ? 2.670   24.776  -79.775  1.00 33.11  ? 163 VAL C CB  1 
ATOM   4167 C  CG1 . VAL C 1 171 ? 4.066   25.244  -80.132  1.00 37.85  ? 163 VAL C CG1 1 
ATOM   4168 C  CG2 . VAL C 1 171 ? 2.210   25.414  -78.460  1.00 34.27  ? 163 VAL C CG2 1 
ATOM   4169 N  N   . GLY C 1 172 ? 2.714   25.187  -83.109  1.00 29.79  ? 164 GLY C N   1 
ATOM   4170 C  CA  . GLY C 1 172 ? 3.198   24.564  -84.317  1.00 36.42  ? 164 GLY C CA  1 
ATOM   4171 C  C   . GLY C 1 172 ? 3.067   25.502  -85.503  1.00 39.58  ? 164 GLY C C   1 
ATOM   4172 O  O   . GLY C 1 172 ? 3.229   26.709  -85.370  1.00 35.54  ? 164 GLY C O   1 
ATOM   4173 N  N   . PHE C 1 173 ? 2.789   24.906  -86.659  1.00 38.28  ? 165 PHE C N   1 
ATOM   4174 C  CA  . PHE C 1 173 ? 2.820   25.616  -87.928  1.00 36.86  ? 165 PHE C CA  1 
ATOM   4175 C  C   . PHE C 1 173 ? 1.590   25.219  -88.719  1.00 37.82  ? 165 PHE C C   1 
ATOM   4176 O  O   . PHE C 1 173 ? 1.411   24.040  -89.035  1.00 38.04  ? 165 PHE C O   1 
ATOM   4177 C  CB  . PHE C 1 173 ? 4.100   25.292  -88.701  1.00 42.06  ? 165 PHE C CB  1 
ATOM   4178 C  CG  . PHE C 1 173 ? 5.368   25.649  -87.959  1.00 45.24  ? 165 PHE C CG  1 
ATOM   4179 C  CD1 . PHE C 1 173 ? 5.949   26.901  -88.108  1.00 39.09  ? 165 PHE C CD1 1 
ATOM   4180 C  CD2 . PHE C 1 173 ? 5.978   24.738  -87.112  1.00 37.74  ? 165 PHE C CD2 1 
ATOM   4181 C  CE1 . PHE C 1 173 ? 7.107   27.231  -87.432  1.00 34.21  ? 165 PHE C CE1 1 
ATOM   4182 C  CE2 . PHE C 1 173 ? 7.144   25.067  -86.431  1.00 37.47  ? 165 PHE C CE2 1 
ATOM   4183 C  CZ  . PHE C 1 173 ? 7.703   26.311  -86.588  1.00 32.32  ? 165 PHE C CZ  1 
ATOM   4184 N  N   . LEU C 1 174 ? 0.737   26.195  -89.028  1.00 33.99  ? 166 LEU C N   1 
ATOM   4185 C  CA  . LEU C 1 174 ? -0.485  25.867  -89.750  1.00 44.19  ? 166 LEU C CA  1 
ATOM   4186 C  C   . LEU C 1 174 ? -0.176  25.289  -91.125  1.00 44.39  ? 166 LEU C C   1 
ATOM   4187 O  O   . LEU C 1 174 ? -0.922  24.440  -91.622  1.00 48.77  ? 166 LEU C O   1 
ATOM   4188 C  CB  . LEU C 1 174 ? -1.370  27.104  -89.859  1.00 47.98  ? 166 LEU C CB  1 
ATOM   4189 C  CG  . LEU C 1 174 ? -1.901  27.577  -88.505  1.00 43.24  ? 166 LEU C CG  1 
ATOM   4190 C  CD1 . LEU C 1 174 ? -1.789  29.095  -88.390  1.00 54.12  ? 166 LEU C CD1 1 
ATOM   4191 C  CD2 . LEU C 1 174 ? -3.340  27.098  -88.285  1.00 50.18  ? 166 LEU C CD2 1 
ATOM   4192 N  N   . GLU C 1 175 ? 0.938   25.711  -91.733  1.00 39.98  ? 167 GLU C N   1 
ATOM   4193 C  CA  . GLU C 1 175 ? 1.405   25.119  -92.984  1.00 50.51  ? 167 GLU C CA  1 
ATOM   4194 C  C   . GLU C 1 175 ? 1.776   23.649  -92.826  1.00 52.05  ? 167 GLU C C   1 
ATOM   4195 O  O   . GLU C 1 175 ? 1.945   22.955  -93.832  1.00 42.91  ? 167 GLU C O   1 
ATOM   4196 C  CB  . GLU C 1 175 ? 2.632   25.874  -93.482  1.00 49.69  ? 167 GLU C CB  1 
ATOM   4197 C  CG  . GLU C 1 175 ? 3.677   26.001  -92.385  1.00 55.87  ? 167 GLU C CG  1 
ATOM   4198 C  CD  . GLU C 1 175 ? 3.711   27.370  -91.743  1.00 59.60  ? 167 GLU C CD  1 
ATOM   4199 O  OE1 . GLU C 1 175 ? 4.793   28.001  -91.768  1.00 62.24  ? 167 GLU C OE1 1 
ATOM   4200 O  OE2 . GLU C 1 175 ? 2.654   27.812  -91.225  1.00 55.64  ? 167 GLU C OE2 1 
ATOM   4201 N  N   . GLY C 1 176 ? 1.933   23.168  -91.592  1.00 45.93  ? 168 GLY C N   1 
ATOM   4202 C  CA  . GLY C 1 176 ? 2.320   21.797  -91.355  1.00 48.32  ? 168 GLY C CA  1 
ATOM   4203 C  C   . GLY C 1 176 ? 3.796   21.551  -91.614  1.00 47.71  ? 168 GLY C C   1 
ATOM   4204 O  O   . GLY C 1 176 ? 4.608   22.468  -91.785  1.00 49.69  ? 168 GLY C O   1 
ATOM   4205 N  N   . GLY C 1 177 ? 4.138   20.266  -91.651  1.00 39.87  ? 169 GLY C N   1 
ATOM   4206 C  CA  . GLY C 1 177 ? 5.494   19.831  -91.847  1.00 39.18  ? 169 GLY C CA  1 
ATOM   4207 C  C   . GLY C 1 177 ? 6.294   19.667  -90.567  1.00 45.57  ? 169 GLY C C   1 
ATOM   4208 O  O   . GLY C 1 177 ? 7.233   18.860  -90.536  1.00 49.41  ? 169 GLY C O   1 
ATOM   4209 N  N   . LYS C 1 178 ? 5.955   20.414  -89.514  1.00 41.02  ? 170 LYS C N   1 
ATOM   4210 C  CA  . LYS C 1 178 ? 6.629   20.318  -88.220  1.00 36.00  ? 170 LYS C CA  1 
ATOM   4211 C  C   . LYS C 1 178 ? 5.576   20.180  -87.131  1.00 36.87  ? 170 LYS C C   1 
ATOM   4212 O  O   . LYS C 1 178 ? 4.679   21.022  -87.023  1.00 42.82  ? 170 LYS C O   1 
ATOM   4213 C  CB  . LYS C 1 178 ? 7.520   21.540  -87.959  1.00 39.51  ? 170 LYS C CB  1 
ATOM   4214 C  CG  . LYS C 1 178 ? 8.785   21.583  -88.818  1.00 44.99  ? 170 LYS C CG  1 
ATOM   4215 C  CD  . LYS C 1 178 ? 9.026   22.967  -89.404  1.00 41.93  ? 170 LYS C CD  1 
ATOM   4216 C  CE  . LYS C 1 178 ? 10.483  23.370  -89.296  1.00 39.62  ? 170 LYS C CE  1 
ATOM   4217 N  NZ  . LYS C 1 178 ? 10.608  24.840  -89.109  1.00 47.28  ? 170 LYS C NZ  1 
ATOM   4218 N  N   . ASP C 1 179 ? 5.681   19.128  -86.326  1.00 39.08  ? 171 ASP C N   1 
ATOM   4219 C  CA  . ASP C 1 179 ? 4.649   18.834  -85.339  1.00 30.48  ? 171 ASP C CA  1 
ATOM   4220 C  C   . ASP C 1 179 ? 5.176   17.728  -84.429  1.00 36.10  ? 171 ASP C C   1 
ATOM   4221 O  O   . ASP C 1 179 ? 6.194   17.092  -84.724  1.00 31.62  ? 171 ASP C O   1 
ATOM   4222 C  CB  . ASP C 1 179 ? 3.352   18.426  -86.043  1.00 32.85  ? 171 ASP C CB  1 
ATOM   4223 C  CG  . ASP C 1 179 ? 2.155   18.439  -85.137  1.00 38.96  ? 171 ASP C CG  1 
ATOM   4224 O  OD1 . ASP C 1 179 ? 1.133   17.802  -85.496  1.00 43.39  ? 171 ASP C OD1 1 
ATOM   4225 O  OD2 . ASP C 1 179 ? 2.224   19.106  -84.083  1.00 43.40  ? 171 ASP C OD2 1 
ATOM   4226 N  N   . SER C 1 180 ? 4.493   17.527  -83.300  1.00 35.11  ? 172 SER C N   1 
ATOM   4227 C  CA  . SER C 1 180 ? 4.666   16.323  -82.496  1.00 34.02  ? 172 SER C CA  1 
ATOM   4228 C  C   . SER C 1 180 ? 3.650   15.276  -82.954  1.00 35.71  ? 172 SER C C   1 
ATOM   4229 O  O   . SER C 1 180 ? 2.641   15.614  -83.580  1.00 39.89  ? 172 SER C O   1 
ATOM   4230 C  CB  . SER C 1 180 ? 4.502   16.637  -81.002  1.00 30.05  ? 172 SER C CB  1 
ATOM   4231 O  OG  . SER C 1 180 ? 3.336   17.402  -80.776  1.00 38.15  ? 172 SER C OG  1 
ATOM   4232 N  N   . CYS C 1 181 ? 3.942   14.000  -82.696  1.00 36.32  ? 173 CYS C N   1 
ATOM   4233 C  CA  . CYS C 1 181 ? 2.898   12.965  -82.836  1.00 36.43  ? 173 CYS C CA  1 
ATOM   4234 C  C   . CYS C 1 181 ? 3.114   11.870  -81.818  1.00 31.58  ? 173 CYS C C   1 
ATOM   4235 O  O   . CYS C 1 181 ? 3.747   12.074  -80.775  1.00 35.36  ? 173 CYS C O   1 
ATOM   4236 C  CB  . CYS C 1 181 ? 2.844   12.232  -84.191  1.00 45.79  ? 173 CYS C CB  1 
ATOM   4237 S  SG  . CYS C 1 181 ? 4.133   12.471  -85.287  1.00 75.12  ? 173 CYS C SG  1 
ATOM   4238 N  N   . GLN C 1 182 ? 2.624   10.688  -82.198  1.00 30.26  ? 174 GLN C N   1 
ATOM   4239 C  CA  . GLN C 1 182 ? 2.508   9.534   -81.329  1.00 36.24  ? 174 GLN C CA  1 
ATOM   4240 C  C   . GLN C 1 182 ? 3.836   9.262   -80.645  1.00 25.48  ? 174 GLN C C   1 
ATOM   4241 O  O   . GLN C 1 182 ? 4.879   9.213   -81.292  1.00 24.56  ? 174 GLN C O   1 
ATOM   4242 C  CB  . GLN C 1 182 ? 2.069   8.315   -82.152  1.00 30.70  ? 174 GLN C CB  1 
ATOM   4243 C  CG  . GLN C 1 182 ? 1.273   7.319   -81.350  1.00 20.44  ? 174 GLN C CG  1 
ATOM   4244 C  CD  . GLN C 1 182 ? 2.152   6.623   -80.344  1.00 30.30  ? 174 GLN C CD  1 
ATOM   4245 O  OE1 . GLN C 1 182 ? 3.338   6.389   -80.598  1.00 24.75  ? 174 GLN C OE1 1 
ATOM   4246 N  NE2 . GLN C 1 182 ? 1.609   6.378   -79.156  1.00 29.15  ? 174 GLN C NE2 1 
ATOM   4247 N  N   . GLY C 1 183 ? 3.788   9.095   -79.334  1.00 24.11  ? 175 GLY C N   1 
ATOM   4248 C  CA  . GLY C 1 183 ? 4.962   8.873   -78.538  1.00 24.02  ? 175 GLY C CA  1 
ATOM   4249 C  C   . GLY C 1 183 ? 5.500   10.110  -77.855  1.00 24.21  ? 175 GLY C C   1 
ATOM   4250 O  O   . GLY C 1 183 ? 6.228   9.975   -76.864  1.00 25.48  ? 175 GLY C O   1 
ATOM   4251 N  N   . ASP C 1 184 ? 5.186   11.309  -78.366  1.00 24.61  ? 176 ASP C N   1 
ATOM   4252 C  CA  . ASP C 1 184 ? 5.582   12.557  -77.705  1.00 24.63  ? 176 ASP C CA  1 
ATOM   4253 C  C   . ASP C 1 184 ? 4.637   12.943  -76.572  1.00 23.00  ? 176 ASP C C   1 
ATOM   4254 O  O   . ASP C 1 184 ? 4.985   13.835  -75.788  1.00 23.17  ? 176 ASP C O   1 
ATOM   4255 C  CB  . ASP C 1 184 ? 5.650   13.719  -78.705  1.00 18.73  ? 176 ASP C CB  1 
ATOM   4256 C  CG  . ASP C 1 184 ? 6.710   13.513  -79.792  1.00 33.05  ? 176 ASP C CG  1 
ATOM   4257 O  OD1 . ASP C 1 184 ? 7.879   13.159  -79.479  1.00 27.87  ? 176 ASP C OD1 1 
ATOM   4258 O  OD2 . ASP C 1 184 ? 6.368   13.726  -80.978  1.00 33.32  ? 176 ASP C OD2 1 
ATOM   4259 N  N   . SER C 1 185 ? 3.453   12.309  -76.499  1.00 26.60  ? 177 SER C N   1 
ATOM   4260 C  CA  . SER C 1 185 ? 2.487   12.413  -75.401  1.00 23.67  ? 177 SER C CA  1 
ATOM   4261 C  C   . SER C 1 185 ? 3.127   12.727  -74.058  1.00 18.89  ? 177 SER C C   1 
ATOM   4262 O  O   . SER C 1 185 ? 4.108   12.083  -73.669  1.00 23.67  ? 177 SER C O   1 
ATOM   4263 C  CB  . SER C 1 185 ? 1.688   11.104  -75.244  1.00 19.66  ? 177 SER C CB  1 
ATOM   4264 O  OG  . SER C 1 185 ? 0.609   11.017  -76.154  1.00 23.35  ? 177 SER C OG  1 
ATOM   4265 N  N   . GLY C 1 186 ? 2.569   13.696  -73.336  1.00 19.02  ? 178 GLY C N   1 
ATOM   4266 C  CA  . GLY C 1 186 ? 3.034   14.037  -72.009  1.00 14.79  ? 178 GLY C CA  1 
ATOM   4267 C  C   . GLY C 1 186 ? 4.352   14.783  -71.949  1.00 23.00  ? 178 GLY C C   1 
ATOM   4268 O  O   . GLY C 1 186 ? 4.726   15.249  -70.866  1.00 22.73  ? 178 GLY C O   1 
ATOM   4269 N  N   . GLY C 1 187 ? 5.069   14.922  -73.064  1.00 21.05  ? 179 GLY C N   1 
ATOM   4270 C  CA  . GLY C 1 187 ? 6.288   15.698  -73.094  1.00 26.10  ? 179 GLY C CA  1 
ATOM   4271 C  C   . GLY C 1 187 ? 6.124   17.211  -72.972  1.00 25.69  ? 179 GLY C C   1 
ATOM   4272 O  O   . GLY C 1 187 ? 5.024   17.774  -73.047  1.00 25.19  ? 179 GLY C O   1 
ATOM   4273 N  N   . PRO C 1 188 ? 7.251   17.898  -72.807  1.00 27.13  ? 180 PRO C N   1 
ATOM   4274 C  CA  . PRO C 1 188 ? 7.237   19.330  -72.483  1.00 22.36  ? 180 PRO C CA  1 
ATOM   4275 C  C   . PRO C 1 188 ? 7.196   20.281  -73.675  1.00 24.29  ? 180 PRO C C   1 
ATOM   4276 O  O   . PRO C 1 188 ? 7.751   20.035  -74.747  1.00 24.48  ? 180 PRO C O   1 
ATOM   4277 C  CB  . PRO C 1 188 ? 8.560   19.494  -71.721  1.00 29.94  ? 180 PRO C CB  1 
ATOM   4278 C  CG  . PRO C 1 188 ? 9.484   18.482  -72.359  1.00 19.86  ? 180 PRO C CG  1 
ATOM   4279 C  CD  . PRO C 1 188 ? 8.614   17.340  -72.842  1.00 19.97  ? 180 PRO C CD  1 
ATOM   4280 N  N   . VAL C 1 189 ? 6.534   21.408  -73.446  1.00 28.50  ? 181 VAL C N   1 
ATOM   4281 C  CA  . VAL C 1 189 ? 6.589   22.589  -74.309  1.00 31.62  ? 181 VAL C CA  1 
ATOM   4282 C  C   . VAL C 1 189 ? 7.145   23.719  -73.446  1.00 30.90  ? 181 VAL C C   1 
ATOM   4283 O  O   . VAL C 1 189 ? 6.442   24.274  -72.583  1.00 24.19  ? 181 VAL C O   1 
ATOM   4284 C  CB  . VAL C 1 189 ? 5.214   22.940  -74.888  1.00 36.46  ? 181 VAL C CB  1 
ATOM   4285 C  CG1 . VAL C 1 189 ? 5.256   24.246  -75.659  1.00 25.16  ? 181 VAL C CG1 1 
ATOM   4286 C  CG2 . VAL C 1 189 ? 4.733   21.807  -75.765  1.00 29.97  ? 181 VAL C CG2 1 
ATOM   4287 N  N   . VAL C 1 190 ? 8.419   24.042  -73.649  1.00 31.20  ? 182 VAL C N   1 
ATOM   4288 C  CA  . VAL C 1 190 ? 9.158   24.952  -72.779  1.00 35.86  ? 182 VAL C CA  1 
ATOM   4289 C  C   . VAL C 1 190 ? 9.434   26.238  -73.538  1.00 40.39  ? 182 VAL C C   1 
ATOM   4290 O  O   . VAL C 1 190 ? 10.003  26.222  -74.641  1.00 40.58  ? 182 VAL C O   1 
ATOM   4291 C  CB  . VAL C 1 190 ? 10.464  24.324  -72.257  1.00 30.72  ? 182 VAL C CB  1 
ATOM   4292 C  CG1 . VAL C 1 190 ? 11.330  25.387  -71.603  1.00 18.71  ? 182 VAL C CG1 1 
ATOM   4293 C  CG2 . VAL C 1 190 ? 10.131  23.223  -71.253  1.00 23.17  ? 182 VAL C CG2 1 
ATOM   4294 N  N   . CYS C 1 191 ? 9.058   27.352  -72.928  1.00 39.11  ? 183 CYS C N   1 
ATOM   4295 C  CA  . CYS C 1 191 ? 8.908   28.610  -73.641  1.00 40.53  ? 183 CYS C CA  1 
ATOM   4296 C  C   . CYS C 1 191 ? 9.552   29.702  -72.786  1.00 36.44  ? 183 CYS C C   1 
ATOM   4297 O  O   . CYS C 1 191 ? 8.910   30.270  -71.900  1.00 49.41  ? 183 CYS C O   1 
ATOM   4298 C  CB  . CYS C 1 191 ? 7.426   28.838  -73.933  1.00 28.80  ? 183 CYS C CB  1 
ATOM   4299 S  SG  . CYS C 1 191 ? 7.202   29.267  -75.652  1.00 76.81  ? 183 CYS C SG  1 
ATOM   4300 N  N   . ASN C 1 192 ? 10.844  29.954  -73.035  1.00 38.95  ? 184 ASN C N   1 
ATOM   4301 C  CA  . ASN C 1 192 ? 11.676  30.844  -72.209  1.00 37.39  ? 184 ASN C CA  1 
ATOM   4302 C  C   . ASN C 1 192 ? 11.894  30.275  -70.808  1.00 37.49  ? 184 ASN C C   1 
ATOM   4303 O  O   . ASN C 1 192 ? 11.738  30.966  -69.801  1.00 39.25  ? 184 ASN C O   1 
ATOM   4304 C  CB  . ASN C 1 192 ? 11.108  32.271  -72.129  1.00 36.28  ? 184 ASN C CB  1 
ATOM   4305 C  CG  . ASN C 1 192 ? 11.484  33.124  -73.335  1.00 50.38  ? 184 ASN C CG  1 
ATOM   4306 O  OD1 . ASN C 1 192 ? 12.659  33.461  -73.536  1.00 54.97  ? 184 ASN C OD1 1 
ATOM   4307 N  ND2 . ASN C 1 192 ? 10.490  33.465  -74.152  1.00 50.91  ? 184 ASN C ND2 1 
ATOM   4308 N  N   . GLY C 1 193 ? 12.297  29.010  -70.750  1.00 31.45  ? 185 GLY C N   1 
ATOM   4309 C  CA  . GLY C 1 193 ? 12.623  28.394  -69.477  1.00 31.96  ? 185 GLY C CA  1 
ATOM   4310 C  C   . GLY C 1 193 ? 11.442  28.017  -68.605  1.00 39.34  ? 185 GLY C C   1 
ATOM   4311 O  O   . GLY C 1 193 ? 11.645  27.556  -67.468  1.00 32.56  ? 185 GLY C O   1 
ATOM   4312 N  N   . GLN C 1 194 ? 10.219  28.197  -69.103  1.00 28.09  ? 186 GLN C N   1 
ATOM   4313 C  CA  . GLN C 1 194 ? 9.002   27.869  -68.380  1.00 33.33  ? 186 GLN C CA  1 
ATOM   4314 C  C   . GLN C 1 194 ? 8.235   26.789  -69.134  1.00 30.84  ? 186 GLN C C   1 
ATOM   4315 O  O   . GLN C 1 194 ? 8.108   26.849  -70.364  1.00 26.87  ? 186 GLN C O   1 
ATOM   4316 C  CB  . GLN C 1 194 ? 8.137   29.123  -68.212  1.00 30.63  ? 186 GLN C CB  1 
ATOM   4317 C  CG  . GLN C 1 194 ? 8.830   30.224  -67.415  1.00 40.04  ? 186 GLN C CG  1 
ATOM   4318 C  CD  . GLN C 1 194 ? 8.089   31.557  -67.438  1.00 42.66  ? 186 GLN C CD  1 
ATOM   4319 O  OE1 . GLN C 1 194 ? 6.857   31.612  -67.462  1.00 38.57  ? 186 GLN C OE1 1 
ATOM   4320 N  NE2 . GLN C 1 194 ? 8.849   32.641  -67.420  1.00 53.58  ? 186 GLN C NE2 1 
ATOM   4321 N  N   . LEU C 1 195 ? 7.710   25.809  -68.392  1.00 29.51  ? 187 LEU C N   1 
ATOM   4322 C  CA  . LEU C 1 195 ? 6.880   24.753  -68.968  1.00 25.04  ? 187 LEU C CA  1 
ATOM   4323 C  C   . LEU C 1 195 ? 5.483   25.304  -69.217  1.00 27.34  ? 187 LEU C C   1 
ATOM   4324 O  O   . LEU C 1 195 ? 4.742   25.573  -68.271  1.00 27.66  ? 187 LEU C O   1 
ATOM   4325 C  CB  . LEU C 1 195 ? 6.829   23.543  -68.038  1.00 30.08  ? 187 LEU C CB  1 
ATOM   4326 C  CG  . LEU C 1 195 ? 6.041   22.300  -68.494  1.00 36.01  ? 187 LEU C CG  1 
ATOM   4327 C  CD1 . LEU C 1 195 ? 6.746   21.568  -69.638  1.00 19.12  ? 187 LEU C CD1 1 
ATOM   4328 C  CD2 . LEU C 1 195 ? 5.823   21.352  -67.331  1.00 21.29  ? 187 LEU C CD2 1 
ATOM   4329 N  N   . GLN C 1 196 ? 5.117   25.465  -70.492  1.00 28.30  ? 188 GLN C N   1 
ATOM   4330 C  CA  . GLN C 1 196 ? 3.846   26.071  -70.858  1.00 21.48  ? 188 GLN C CA  1 
ATOM   4331 C  C   . GLN C 1 196 ? 2.857   25.095  -71.484  1.00 23.39  ? 188 GLN C C   1 
ATOM   4332 O  O   . GLN C 1 196 ? 1.651   25.357  -71.459  1.00 28.57  ? 188 GLN C O   1 
ATOM   4333 C  CB  . GLN C 1 196 ? 4.076   27.248  -71.828  1.00 23.41  ? 188 GLN C CB  1 
ATOM   4334 C  CG  . GLN C 1 196 ? 4.769   28.449  -71.193  1.00 23.50  ? 188 GLN C CG  1 
ATOM   4335 C  CD  . GLN C 1 196 ? 3.786   29.332  -70.414  1.00 37.75  ? 188 GLN C CD  1 
ATOM   4336 O  OE1 . GLN C 1 196 ? 2.666   28.919  -70.102  1.00 39.10  ? 188 GLN C OE1 1 
ATOM   4337 N  NE2 . GLN C 1 196 ? 4.217   30.534  -70.072  1.00 37.48  ? 188 GLN C NE2 1 
ATOM   4338 N  N   . GLY C 1 197 ? 3.318   23.979  -72.028  1.00 18.01  ? 189 GLY C N   1 
ATOM   4339 C  CA  . GLY C 1 197 ? 2.410   23.021  -72.616  1.00 28.96  ? 189 GLY C CA  1 
ATOM   4340 C  C   . GLY C 1 197 ? 2.847   21.601  -72.321  1.00 29.29  ? 189 GLY C C   1 
ATOM   4341 O  O   . GLY C 1 197 ? 4.021   21.324  -72.061  1.00 21.41  ? 189 GLY C O   1 
ATOM   4342 N  N   . ILE C 1 198 ? 1.868   20.703  -72.357  1.00 32.02  ? 190 ILE C N   1 
ATOM   4343 C  CA  . ILE C 1 198 ? 2.101   19.268  -72.274  1.00 24.21  ? 190 ILE C CA  1 
ATOM   4344 C  C   . ILE C 1 198 ? 1.458   18.635  -73.503  1.00 18.94  ? 190 ILE C C   1 
ATOM   4345 O  O   . ILE C 1 198 ? 0.285   18.897  -73.795  1.00 27.85  ? 190 ILE C O   1 
ATOM   4346 C  CB  . ILE C 1 198 ? 1.520   18.688  -70.969  1.00 25.53  ? 190 ILE C CB  1 
ATOM   4347 C  CG1 . ILE C 1 198 ? 2.182   19.342  -69.759  1.00 21.96  ? 190 ILE C CG1 1 
ATOM   4348 C  CG2 . ILE C 1 198 ? 1.744   17.180  -70.893  1.00 26.78  ? 190 ILE C CG2 1 
ATOM   4349 C  CD1 . ILE C 1 198 ? 1.374   19.199  -68.487  1.00 23.44  ? 190 ILE C CD1 1 
ATOM   4350 N  N   . VAL C 1 199 ? 2.228   17.842  -74.245  1.00 20.11  ? 191 VAL C N   1 
ATOM   4351 C  CA  . VAL C 1 199 ? 1.708   17.228  -75.468  1.00 19.74  ? 191 VAL C CA  1 
ATOM   4352 C  C   . VAL C 1 199 ? 0.474   16.407  -75.141  1.00 22.29  ? 191 VAL C C   1 
ATOM   4353 O  O   . VAL C 1 199 ? 0.525   15.503  -74.298  1.00 22.27  ? 191 VAL C O   1 
ATOM   4354 C  CB  . VAL C 1 199 ? 2.776   16.344  -76.134  1.00 19.28  ? 191 VAL C CB  1 
ATOM   4355 C  CG1 . VAL C 1 199 ? 2.313   15.930  -77.509  1.00 23.83  ? 191 VAL C CG1 1 
ATOM   4356 C  CG2 . VAL C 1 199 ? 4.116   17.055  -76.222  1.00 28.18  ? 191 VAL C CG2 1 
ATOM   4357 N  N   . SER C 1 200 ? -0.640  16.691  -75.823  1.00 20.10  ? 192 SER C N   1 
ATOM   4358 C  CA  . SER C 1 200 ? -1.892  16.017  -75.480  1.00 26.88  ? 192 SER C CA  1 
ATOM   4359 C  C   . SER C 1 200 ? -2.493  15.186  -76.614  1.00 32.05  ? 192 SER C C   1 
ATOM   4360 O  O   . SER C 1 200 ? -2.797  14.007  -76.388  1.00 21.13  ? 192 SER C O   1 
ATOM   4361 C  CB  . SER C 1 200 ? -2.921  17.039  -74.964  1.00 21.91  ? 192 SER C CB  1 
ATOM   4362 O  OG  . SER C 1 200 ? -4.129  16.379  -74.582  1.00 26.63  ? 192 SER C OG  1 
ATOM   4363 N  N   . TRP C 1 201 ? -2.712  15.757  -77.810  1.00 22.13  ? 193 TRP C N   1 
ATOM   4364 C  CA  . TRP C 1 201 ? -3.343  15.028  -78.919  1.00 29.50  ? 193 TRP C CA  1 
ATOM   4365 C  C   . TRP C 1 201 ? -3.189  15.796  -80.232  1.00 26.53  ? 193 TRP C C   1 
ATOM   4366 O  O   . TRP C 1 201 ? -2.738  16.941  -80.260  1.00 30.78  ? 193 TRP C O   1 
ATOM   4367 C  CB  . TRP C 1 201 ? -4.828  14.750  -78.659  1.00 21.62  ? 193 TRP C CB  1 
ATOM   4368 C  CG  . TRP C 1 201 ? -5.667  15.985  -78.417  1.00 31.38  ? 193 TRP C CG  1 
ATOM   4369 C  CD1 . TRP C 1 201 ? -5.808  16.650  -77.237  1.00 31.89  ? 193 TRP C CD1 1 
ATOM   4370 C  CD2 . TRP C 1 201 ? -6.498  16.672  -79.365  1.00 29.60  ? 193 TRP C CD2 1 
ATOM   4371 N  NE1 . TRP C 1 201 ? -6.677  17.697  -77.386  1.00 36.07  ? 193 TRP C NE1 1 
ATOM   4372 C  CE2 . TRP C 1 201 ? -7.113  17.736  -78.683  1.00 35.19  ? 193 TRP C CE2 1 
ATOM   4373 C  CE3 . TRP C 1 201 ? -6.787  16.482  -80.724  1.00 39.14  ? 193 TRP C CE3 1 
ATOM   4374 C  CZ2 . TRP C 1 201 ? -7.989  18.623  -79.312  1.00 34.78  ? 193 TRP C CZ2 1 
ATOM   4375 C  CZ3 . TRP C 1 201 ? -7.666  17.355  -81.349  1.00 32.51  ? 193 TRP C CZ3 1 
ATOM   4376 C  CH2 . TRP C 1 201 ? -8.251  18.418  -80.640  1.00 37.46  ? 193 TRP C CH2 1 
ATOM   4377 N  N   . GLY C 1 202 ? -3.573  15.142  -81.327  1.00 28.64  ? 194 GLY C N   1 
ATOM   4378 C  CA  . GLY C 1 202 ? -3.484  15.762  -82.639  1.00 28.05  ? 194 GLY C CA  1 
ATOM   4379 C  C   . GLY C 1 202 ? -4.200  14.914  -83.664  1.00 39.93  ? 194 GLY C C   1 
ATOM   4380 O  O   . GLY C 1 202 ? -4.547  13.754  -83.412  1.00 33.79  ? 194 GLY C O   1 
ATOM   4381 N  N   . TYR C 1 203 ? -4.431  15.521  -84.839  1.00 43.15  ? 195 TYR C N   1 
ATOM   4382 C  CA  . TYR C 1 203 ? -5.103  14.851  -85.951  1.00 34.02  ? 195 TYR C CA  1 
ATOM   4383 C  C   . TYR C 1 203 ? -4.109  14.699  -87.093  1.00 34.24  ? 195 TYR C C   1 
ATOM   4384 O  O   . TYR C 1 203 ? -3.765  15.678  -87.767  1.00 34.84  ? 195 TYR C O   1 
ATOM   4385 C  CB  . TYR C 1 203 ? -6.366  15.596  -86.384  1.00 38.67  ? 195 TYR C CB  1 
ATOM   4386 C  CG  . TYR C 1 203 ? -7.058  14.918  -87.548  1.00 43.69  ? 195 TYR C CG  1 
ATOM   4387 C  CD1 . TYR C 1 203 ? -8.260  14.231  -87.352  1.00 42.86  ? 195 TYR C CD1 1 
ATOM   4388 C  CD2 . TYR C 1 203 ? -6.565  15.020  -88.849  1.00 41.36  ? 195 TYR C CD2 1 
ATOM   4389 C  CE1 . TYR C 1 203 ? -8.908  13.604  -88.407  1.00 41.47  ? 195 TYR C CE1 1 
ATOM   4390 C  CE2 . TYR C 1 203 ? -7.209  14.394  -89.908  1.00 50.34  ? 195 TYR C CE2 1 
ATOM   4391 C  CZ  . TYR C 1 203 ? -8.379  13.696  -89.681  1.00 42.65  ? 195 TYR C CZ  1 
ATOM   4392 O  OH  . TYR C 1 203 ? -9.003  13.083  -90.737  1.00 51.36  ? 195 TYR C OH  1 
ATOM   4393 N  N   . GLY C 1 204 ? -3.678  13.464  -87.327  1.00 28.17  ? 196 GLY C N   1 
ATOM   4394 C  CA  . GLY C 1 204 ? -2.509  13.236  -88.143  1.00 32.27  ? 196 GLY C CA  1 
ATOM   4395 C  C   . GLY C 1 204 ? -1.300  13.857  -87.482  1.00 36.36  ? 196 GLY C C   1 
ATOM   4396 O  O   . GLY C 1 204 ? -1.388  14.418  -86.384  1.00 37.42  ? 196 GLY C O   1 
ATOM   4397 N  N   A CYS C 1 205 ? -0.163  13.761  -88.148  0.99 45.92  ? 197 CYS C N   1 
ATOM   4398 N  N   B CYS C 1 205 ? -0.138  13.766  -88.121  0.01 45.54  ? 197 CYS C N   1 
ATOM   4399 C  CA  A CYS C 1 205 ? 1.059   14.379  -87.668  0.99 47.88  ? 197 CYS C CA  1 
ATOM   4400 C  CA  B CYS C 1 205 ? 1.070   14.409  -87.614  0.01 47.64  ? 197 CYS C CA  1 
ATOM   4401 C  C   A CYS C 1 205 ? 1.560   15.350  -88.730  0.99 44.75  ? 197 CYS C C   1 
ATOM   4402 C  C   B CYS C 1 205 ? 1.612   15.341  -88.685  0.01 44.71  ? 197 CYS C C   1 
ATOM   4403 O  O   A CYS C 1 205 ? 1.856   14.937  -89.855  0.99 44.51  ? 197 CYS C O   1 
ATOM   4404 O  O   B CYS C 1 205 ? 2.018   14.887  -89.759  0.01 44.71  ? 197 CYS C O   1 
ATOM   4405 C  CB  A CYS C 1 205 ? 2.099   13.314  -87.337  0.99 46.65  ? 197 CYS C CB  1 
ATOM   4406 C  CB  B CYS C 1 205 ? 2.124   13.387  -87.215  0.01 47.19  ? 197 CYS C CB  1 
ATOM   4407 S  SG  A CYS C 1 205 ? 3.392   14.018  -86.372  0.99 85.45  ? 197 CYS C SG  1 
ATOM   4408 S  SG  B CYS C 1 205 ? 3.484   14.096  -86.298  0.01 79.12  ? 197 CYS C SG  1 
ATOM   4409 N  N   . ALA C 1 206 ? 1.597   16.640  -88.386  1.00 37.97  ? 198 ALA C N   1 
ATOM   4410 C  CA  . ALA C 1 206 ? 2.188   17.681  -89.223  1.00 34.65  ? 198 ALA C CA  1 
ATOM   4411 C  C   . ALA C 1 206 ? 1.398   17.954  -90.508  1.00 43.61  ? 198 ALA C C   1 
ATOM   4412 O  O   . ALA C 1 206 ? 1.975   18.359  -91.525  1.00 34.59  ? 198 ALA C O   1 
ATOM   4413 C  CB  . ALA C 1 206 ? 3.656   17.367  -89.539  1.00 32.31  ? 198 ALA C CB  1 
ATOM   4414 N  N   . GLN C 1 207 ? 0.077   17.790  -90.485  1.00 37.08  ? 199 GLN C N   1 
ATOM   4415 C  CA  . GLN C 1 207 ? -0.723  18.183  -91.638  1.00 34.68  ? 199 GLN C CA  1 
ATOM   4416 C  C   . GLN C 1 207 ? -1.139  19.653  -91.559  1.00 37.88  ? 199 GLN C C   1 
ATOM   4417 O  O   . GLN C 1 207 ? -1.186  20.264  -90.485  1.00 43.79  ? 199 GLN C O   1 
ATOM   4418 C  CB  . GLN C 1 207 ? -1.963  17.296  -91.782  1.00 38.64  ? 199 GLN C CB  1 
ATOM   4419 C  CG  . GLN C 1 207 ? -1.774  15.857  -91.340  1.00 36.62  ? 199 GLN C CG  1 
ATOM   4420 C  CD  . GLN C 1 207 ? -0.725  15.125  -92.166  1.00 54.83  ? 199 GLN C CD  1 
ATOM   4421 O  OE1 . GLN C 1 207 ? -0.900  14.924  -93.365  1.00 64.89  ? 199 GLN C OE1 1 
ATOM   4422 N  NE2 . GLN C 1 207 ? 0.371   14.720  -91.522  1.00 55.49  ? 199 GLN C NE2 1 
ATOM   4423 N  N   . LYS C 1 208 ? -1.450  20.213  -92.730  1.00 47.39  ? 200 LYS C N   1 
ATOM   4424 C  CA  . LYS C 1 208 ? -1.862  21.608  -92.828  1.00 48.39  ? 200 LYS C CA  1 
ATOM   4425 C  C   . LYS C 1 208 ? -3.085  21.873  -91.958  1.00 44.17  ? 200 LYS C C   1 
ATOM   4426 O  O   . LYS C 1 208 ? -4.041  21.094  -91.946  1.00 39.64  ? 200 LYS C O   1 
ATOM   4427 C  CB  . LYS C 1 208 ? -2.166  21.964  -94.286  1.00 49.10  ? 200 LYS C CB  1 
ATOM   4428 C  CG  . LYS C 1 208 ? -0.950  21.885  -95.200  1.00 53.05  ? 200 LYS C CG  1 
ATOM   4429 C  CD  . LYS C 1 208 ? -0.543  23.242  -95.750  1.00 56.62  ? 200 LYS C CD  1 
ATOM   4430 C  CE  . LYS C 1 208 ? 0.515   23.103  -96.845  1.00 68.57  ? 200 LYS C CE  1 
ATOM   4431 N  NZ  . LYS C 1 208 ? 1.722   23.944  -96.586  1.00 66.57  ? 200 LYS C NZ  1 
ATOM   4432 N  N   . ASN C 1 209 ? -3.037  22.977  -91.212  1.00 41.39  ? 201 ASN C N   1 
ATOM   4433 C  CA  . ASN C 1 209 ? -4.144  23.411  -90.365  1.00 42.55  ? 201 ASN C CA  1 
ATOM   4434 C  C   . ASN C 1 209 ? -4.540  22.367  -89.326  1.00 43.62  ? 201 ASN C C   1 
ATOM   4435 O  O   . ASN C 1 209 ? -5.697  22.320  -88.896  1.00 39.51  ? 201 ASN C O   1 
ATOM   4436 C  CB  . ASN C 1 209 ? -5.361  23.797  -91.203  1.00 39.79  ? 201 ASN C CB  1 
ATOM   4437 C  CG  . ASN C 1 209 ? -5.012  24.735  -92.319  1.00 54.10  ? 201 ASN C CG  1 
ATOM   4438 O  OD1 . ASN C 1 209 ? -5.303  24.471  -93.487  1.00 60.09  ? 201 ASN C OD1 1 
ATOM   4439 N  ND2 . ASN C 1 209 ? -4.395  25.862  -91.968  1.00 62.02  ? 201 ASN C ND2 1 
ATOM   4440 N  N   . LYS C 1 210 ? -3.605  21.516  -88.909  1.00 39.10  ? 202 LYS C N   1 
ATOM   4441 C  CA  . LYS C 1 210 ? -3.870  20.523  -87.865  1.00 30.32  ? 202 LYS C CA  1 
ATOM   4442 C  C   . LYS C 1 210 ? -2.648  20.441  -86.959  1.00 33.28  ? 202 LYS C C   1 
ATOM   4443 O  O   . LYS C 1 210 ? -1.929  19.434  -86.933  1.00 30.30  ? 202 LYS C O   1 
ATOM   4444 C  CB  . LYS C 1 210 ? -4.221  19.172  -88.480  1.00 33.14  ? 202 LYS C CB  1 
ATOM   4445 C  CG  . LYS C 1 210 ? -5.579  19.130  -89.189  1.00 33.28  ? 202 LYS C CG  1 
ATOM   4446 C  CD  . LYS C 1 210 ? -6.741  19.299  -88.214  1.00 40.72  ? 202 LYS C CD  1 
ATOM   4447 C  CE  . LYS C 1 210 ? -8.059  19.525  -88.961  1.00 32.54  ? 202 LYS C CE  1 
ATOM   4448 N  NZ  . LYS C 1 210 ? -9.229  19.679  -88.036  1.00 38.50  ? 202 LYS C NZ  1 
ATOM   4449 N  N   . PRO C 1 211 ? -2.377  21.502  -86.204  1.00 35.27  ? 203 PRO C N   1 
ATOM   4450 C  CA  . PRO C 1 211 ? -1.205  21.508  -85.329  1.00 33.23  ? 203 PRO C CA  1 
ATOM   4451 C  C   . PRO C 1 211 ? -1.458  20.626  -84.124  1.00 35.23  ? 203 PRO C C   1 
ATOM   4452 O  O   . PRO C 1 211 ? -2.585  20.191  -83.869  1.00 26.45  ? 203 PRO C O   1 
ATOM   4453 C  CB  . PRO C 1 211 ? -1.085  22.976  -84.892  1.00 33.49  ? 203 PRO C CB  1 
ATOM   4454 C  CG  . PRO C 1 211 ? -2.226  23.701  -85.575  1.00 34.67  ? 203 PRO C CG  1 
ATOM   4455 C  CD  . PRO C 1 211 ? -3.237  22.662  -85.923  1.00 28.68  ? 203 PRO C CD  1 
ATOM   4456 N  N   . GLY C 1 212 ? -0.390  20.416  -83.352  1.00 30.64  ? 204 GLY C N   1 
ATOM   4457 C  CA  . GLY C 1 212 ? -0.526  19.756  -82.068  1.00 26.79  ? 204 GLY C CA  1 
ATOM   4458 C  C   . GLY C 1 212 ? -1.377  20.545  -81.088  1.00 29.56  ? 204 GLY C C   1 
ATOM   4459 O  O   . GLY C 1 212 ? -1.370  21.779  -81.060  1.00 30.95  ? 204 GLY C O   1 
ATOM   4460 N  N   . VAL C 1 213 ? -2.135  19.801  -80.261  1.00 30.81  ? 205 VAL C N   1 
ATOM   4461 C  CA  . VAL C 1 213 ? -2.870  20.348  -79.122  1.00 27.94  ? 205 VAL C CA  1 
ATOM   4462 C  C   . VAL C 1 213 ? -2.130  20.007  -77.837  1.00 28.06  ? 205 VAL C C   1 
ATOM   4463 O  O   . VAL C 1 213 ? -1.600  18.896  -77.684  1.00 28.70  ? 205 VAL C O   1 
ATOM   4464 C  CB  . VAL C 1 213 ? -4.308  19.817  -79.081  1.00 29.46  ? 205 VAL C CB  1 
ATOM   4465 C  CG1 . VAL C 1 213 ? -5.127  20.650  -78.123  1.00 29.36  ? 205 VAL C CG1 1 
ATOM   4466 C  CG2 . VAL C 1 213 ? -4.903  19.840  -80.491  1.00 33.36  ? 205 VAL C CG2 1 
ATOM   4467 N  N   . TYR C 1 214 ? -2.089  20.964  -76.911  1.00 21.14  ? 206 TYR C N   1 
ATOM   4468 C  CA  . TYR C 1 214 ? -1.262  20.873  -75.719  1.00 23.71  ? 206 TYR C CA  1 
ATOM   4469 C  C   . TYR C 1 214 ? -2.042  21.394  -74.526  1.00 30.32  ? 206 TYR C C   1 
ATOM   4470 O  O   . TYR C 1 214 ? -2.801  22.363  -74.643  1.00 21.96  ? 206 TYR C O   1 
ATOM   4471 C  CB  . TYR C 1 214 ? 0.041   21.671  -75.873  1.00 22.38  ? 206 TYR C CB  1 
ATOM   4472 C  CG  . TYR C 1 214 ? 0.876   21.272  -77.069  1.00 25.99  ? 206 TYR C CG  1 
ATOM   4473 C  CD1 . TYR C 1 214 ? 0.582   21.747  -78.334  1.00 25.31  ? 206 TYR C CD1 1 
ATOM   4474 C  CD2 . TYR C 1 214 ? 1.973   20.430  -76.930  1.00 30.70  ? 206 TYR C CD2 1 
ATOM   4475 C  CE1 . TYR C 1 214 ? 1.338   21.380  -79.436  1.00 29.38  ? 206 TYR C CE1 1 
ATOM   4476 C  CE2 . TYR C 1 214 ? 2.742   20.061  -78.024  1.00 27.19  ? 206 TYR C CE2 1 
ATOM   4477 C  CZ  . TYR C 1 214 ? 2.416   20.549  -79.276  1.00 33.62  ? 206 TYR C CZ  1 
ATOM   4478 O  OH  . TYR C 1 214 ? 3.155   20.200  -80.379  1.00 34.84  ? 206 TYR C OH  1 
ATOM   4479 N  N   . THR C 1 215 ? -1.851  20.739  -73.382  1.00 30.73  ? 207 THR C N   1 
ATOM   4480 C  CA  . THR C 1 215 ? -2.452  21.204  -72.139  1.00 25.85  ? 207 THR C CA  1 
ATOM   4481 C  C   . THR C 1 215 ? -1.822  22.530  -71.727  1.00 23.97  ? 207 THR C C   1 
ATOM   4482 O  O   . THR C 1 215 ? -0.599  22.674  -71.713  1.00 26.82  ? 207 THR C O   1 
ATOM   4483 C  CB  . THR C 1 215 ? -2.273  20.156  -71.044  1.00 19.71  ? 207 THR C CB  1 
ATOM   4484 O  OG1 . THR C 1 215 ? -2.956  18.957  -71.424  1.00 23.93  ? 207 THR C OG1 1 
ATOM   4485 C  CG2 . THR C 1 215 ? -2.831  20.647  -69.706  1.00 26.17  ? 207 THR C CG2 1 
ATOM   4486 N  N   . LYS C 1 216 ? -2.660  23.505  -71.406  1.00 30.96  ? 208 LYS C N   1 
ATOM   4487 C  CA  . LYS C 1 216 ? -2.187  24.845  -71.072  1.00 31.80  ? 208 LYS C CA  1 
ATOM   4488 C  C   . LYS C 1 216 ? -1.755  24.845  -69.610  1.00 28.86  ? 208 LYS C C   1 
ATOM   4489 O  O   . LYS C 1 216 ? -2.575  25.041  -68.710  1.00 30.72  ? 208 LYS C O   1 
ATOM   4490 C  CB  . LYS C 1 216 ? -3.275  25.872  -71.348  1.00 25.55  ? 208 LYS C CB  1 
ATOM   4491 C  CG  . LYS C 1 216 ? -2.772  27.295  -71.386  1.00 23.92  ? 208 LYS C CG  1 
ATOM   4492 C  CD  . LYS C 1 216 ? -3.901  28.278  -71.148  1.00 28.19  ? 208 LYS C CD  1 
ATOM   4493 C  CE  . LYS C 1 216 ? -3.888  29.397  -72.145  1.00 29.06  ? 208 LYS C CE  1 
ATOM   4494 N  NZ  . LYS C 1 216 ? -5.079  30.259  -72.026  1.00 36.09  ? 208 LYS C NZ  1 
ATOM   4495 N  N   . VAL C 1 217 ? -0.449  24.650  -69.382  1.00 20.20  ? 209 VAL C N   1 
ATOM   4496 C  CA  . VAL C 1 217 ? 0.076   24.387  -68.042  1.00 30.10  ? 209 VAL C CA  1 
ATOM   4497 C  C   . VAL C 1 217 ? -0.150  25.557  -67.089  1.00 30.56  ? 209 VAL C C   1 
ATOM   4498 O  O   . VAL C 1 217 ? -0.321  25.346  -65.878  1.00 25.10  ? 209 VAL C O   1 
ATOM   4499 C  CB  . VAL C 1 217 ? 1.573   24.018  -68.134  1.00 27.57  ? 209 VAL C CB  1 
ATOM   4500 C  CG1 . VAL C 1 217 ? 2.188   23.895  -66.748  1.00 26.47  ? 209 VAL C CG1 1 
ATOM   4501 C  CG2 . VAL C 1 217 ? 1.733   22.714  -68.898  1.00 19.96  ? 209 VAL C CG2 1 
ATOM   4502 N  N   . CYS C 1 218 ? -0.150  26.797  -67.604  1.00 23.44  ? 210 CYS C N   1 
ATOM   4503 C  CA  . CYS C 1 218 ? -0.275  27.972  -66.744  1.00 27.81  ? 210 CYS C CA  1 
ATOM   4504 C  C   . CYS C 1 218 ? -1.585  27.968  -65.960  1.00 32.15  ? 210 CYS C C   1 
ATOM   4505 O  O   . CYS C 1 218 ? -1.634  28.501  -64.845  1.00 33.61  ? 210 CYS C O   1 
ATOM   4506 C  CB  . CYS C 1 218 ? -0.135  29.268  -67.567  1.00 35.11  ? 210 CYS C CB  1 
ATOM   4507 S  SG  . CYS C 1 218 ? -1.452  29.580  -68.823  1.00 45.37  ? 210 CYS C SG  1 
ATOM   4508 N  N   . ASN C 1 219 ? -2.639  27.341  -66.496  1.00 26.78  ? 211 ASN C N   1 
ATOM   4509 C  CA  . ASN C 1 219 ? -3.886  27.199  -65.740  1.00 25.01  ? 211 ASN C CA  1 
ATOM   4510 C  C   . ASN C 1 219 ? -3.773  26.271  -64.537  1.00 29.24  ? 211 ASN C C   1 
ATOM   4511 O  O   . ASN C 1 219 ? -4.719  26.201  -63.748  1.00 23.68  ? 211 ASN C O   1 
ATOM   4512 C  CB  . ASN C 1 219 ? -5.017  26.660  -66.624  1.00 23.27  ? 211 ASN C CB  1 
ATOM   4513 C  CG  . ASN C 1 219 ? -5.417  27.617  -67.743  1.00 33.71  ? 211 ASN C CG  1 
ATOM   4514 O  OD1 . ASN C 1 219 ? -4.874  28.725  -67.880  1.00 29.02  ? 211 ASN C OD1 1 
ATOM   4515 N  ND2 . ASN C 1 219 ? -6.398  27.196  -68.540  1.00 28.62  ? 211 ASN C ND2 1 
ATOM   4516 N  N   . TYR C 1 220 ? -2.682  25.526  -64.386  1.00 28.54  ? 212 TYR C N   1 
ATOM   4517 C  CA  . TYR C 1 220 ? -2.618  24.503  -63.354  1.00 24.57  ? 212 TYR C CA  1 
ATOM   4518 C  C   . TYR C 1 220 ? -1.554  24.776  -62.313  1.00 25.91  ? 212 TYR C C   1 
ATOM   4519 O  O   . TYR C 1 220 ? -1.399  23.967  -61.395  1.00 30.92  ? 212 TYR C O   1 
ATOM   4520 C  CB  . TYR C 1 220 ? -2.382  23.122  -63.983  1.00 27.31  ? 212 TYR C CB  1 
ATOM   4521 C  CG  . TYR C 1 220 ? -3.491  22.728  -64.920  1.00 28.07  ? 212 TYR C CG  1 
ATOM   4522 C  CD1 . TYR C 1 220 ? -4.611  22.088  -64.437  1.00 23.36  ? 212 TYR C CD1 1 
ATOM   4523 C  CD2 . TYR C 1 220 ? -3.434  23.024  -66.283  1.00 22.31  ? 212 TYR C CD2 1 
ATOM   4524 C  CE1 . TYR C 1 220 ? -5.647  21.735  -65.270  1.00 23.59  ? 212 TYR C CE1 1 
ATOM   4525 C  CE2 . TYR C 1 220 ? -4.466  22.671  -67.125  1.00 29.67  ? 212 TYR C CE2 1 
ATOM   4526 C  CZ  . TYR C 1 220 ? -5.573  22.024  -66.602  1.00 27.52  ? 212 TYR C CZ  1 
ATOM   4527 O  OH  . TYR C 1 220 ? -6.619  21.661  -67.402  1.00 30.25  ? 212 TYR C OH  1 
ATOM   4528 N  N   . VAL C 1 221 ? -0.820  25.887  -62.439  1.00 26.41  ? 213 VAL C N   1 
ATOM   4529 C  CA  . VAL C 1 221 ? 0.268   26.202  -61.511  1.00 33.64  ? 213 VAL C CA  1 
ATOM   4530 C  C   . VAL C 1 221 ? -0.154  26.003  -60.057  1.00 26.41  ? 213 VAL C C   1 
ATOM   4531 O  O   . VAL C 1 221 ? 0.576   25.396  -59.264  1.00 36.08  ? 213 VAL C O   1 
ATOM   4532 C  CB  . VAL C 1 221 ? 0.781   27.632  -61.759  1.00 27.21  ? 213 VAL C CB  1 
ATOM   4533 C  CG1 . VAL C 1 221 ? 1.814   27.996  -60.727  1.00 29.68  ? 213 VAL C CG1 1 
ATOM   4534 C  CG2 . VAL C 1 221 ? 1.391   27.727  -63.138  1.00 27.36  ? 213 VAL C CG2 1 
ATOM   4535 N  N   . ASN C 1 222 ? -1.343  26.477  -59.691  1.00 26.41  ? 214 ASN C N   1 
ATOM   4536 C  CA  . ASN C 1 222 ? -1.794  26.346  -58.310  1.00 32.76  ? 214 ASN C CA  1 
ATOM   4537 C  C   . ASN C 1 222 ? -2.092  24.900  -57.967  1.00 31.96  ? 214 ASN C C   1 
ATOM   4538 O  O   . ASN C 1 222 ? -1.667  24.406  -56.911  1.00 32.79  ? 214 ASN C O   1 
ATOM   4539 C  CB  . ASN C 1 222 ? -3.022  27.217  -58.055  1.00 36.18  ? 214 ASN C CB  1 
ATOM   4540 C  CG  . ASN C 1 222 ? -2.698  28.686  -58.033  1.00 50.48  ? 214 ASN C CG  1 
ATOM   4541 O  OD1 . ASN C 1 222 ? -1.528  29.076  -57.979  1.00 58.11  ? 214 ASN C OD1 1 
ATOM   4542 N  ND2 . ASN C 1 222 ? -3.734  29.522  -58.083  1.00 62.51  ? 214 ASN C ND2 1 
ATOM   4543 N  N   . TRP C 1 223 ? -2.829  24.205  -58.842  1.00 29.47  ? 215 TRP C N   1 
ATOM   4544 C  CA  . TRP C 1 223 ? -3.138  22.802  -58.582  1.00 27.00  ? 215 TRP C CA  1 
ATOM   4545 C  C   . TRP C 1 223 ? -1.863  21.991  -58.402  1.00 27.52  ? 215 TRP C C   1 
ATOM   4546 O  O   . TRP C 1 223 ? -1.785  21.122  -57.527  1.00 27.77  ? 215 TRP C O   1 
ATOM   4547 C  CB  . TRP C 1 223 ? -3.979  22.208  -59.708  1.00 22.73  ? 215 TRP C CB  1 
ATOM   4548 C  CG  . TRP C 1 223 ? -4.190  20.716  -59.521  1.00 30.23  ? 215 TRP C CG  1 
ATOM   4549 C  CD1 . TRP C 1 223 ? -5.031  20.113  -58.626  1.00 21.95  ? 215 TRP C CD1 1 
ATOM   4550 C  CD2 . TRP C 1 223 ? -3.532  19.652  -60.231  1.00 30.40  ? 215 TRP C CD2 1 
ATOM   4551 N  NE1 . TRP C 1 223 ? -4.950  18.748  -58.743  1.00 30.31  ? 215 TRP C NE1 1 
ATOM   4552 C  CE2 . TRP C 1 223 ? -4.038  18.433  -59.716  1.00 28.40  ? 215 TRP C CE2 1 
ATOM   4553 C  CE3 . TRP C 1 223 ? -2.577  19.611  -61.261  1.00 26.02  ? 215 TRP C CE3 1 
ATOM   4554 C  CZ2 . TRP C 1 223 ? -3.617  17.180  -60.192  1.00 26.74  ? 215 TRP C CZ2 1 
ATOM   4555 C  CZ3 . TRP C 1 223 ? -2.155  18.361  -61.738  1.00 28.15  ? 215 TRP C CZ3 1 
ATOM   4556 C  CH2 . TRP C 1 223 ? -2.672  17.165  -61.199  1.00 26.98  ? 215 TRP C CH2 1 
ATOM   4557 N  N   . ILE C 1 224 ? -0.843  22.276  -59.209  1.00 28.09  ? 216 ILE C N   1 
ATOM   4558 C  CA  . ILE C 1 224 ? 0.414   21.561  -59.055  1.00 29.08  ? 216 ILE C CA  1 
ATOM   4559 C  C   . ILE C 1 224 ? 1.034   21.880  -57.705  1.00 30.55  ? 216 ILE C C   1 
ATOM   4560 O  O   . ILE C 1 224 ? 1.313   20.980  -56.901  1.00 31.86  ? 216 ILE C O   1 
ATOM   4561 C  CB  . ILE C 1 224 ? 1.371   21.883  -60.210  1.00 21.14  ? 216 ILE C CB  1 
ATOM   4562 C  CG1 . ILE C 1 224 ? 0.743   21.456  -61.531  1.00 22.90  ? 216 ILE C CG1 1 
ATOM   4563 C  CG2 . ILE C 1 224 ? 2.691   21.168  -60.016  1.00 20.70  ? 216 ILE C CG2 1 
ATOM   4564 C  CD1 . ILE C 1 224 ? 1.398   22.094  -62.716  1.00 27.16  ? 216 ILE C CD1 1 
ATOM   4565 N  N   . GLN C 1 225 ? 1.235   23.170  -57.425  1.00 36.72  ? 217 GLN C N   1 
ATOM   4566 C  CA  . GLN C 1 225 ? 1.925   23.557  -56.198  1.00 35.27  ? 217 GLN C CA  1 
ATOM   4567 C  C   . GLN C 1 225 ? 1.185   23.037  -54.976  1.00 28.68  ? 217 GLN C C   1 
ATOM   4568 O  O   . GLN C 1 225 ? 1.796   22.460  -54.070  1.00 31.28  ? 217 GLN C O   1 
ATOM   4569 C  CB  . GLN C 1 225 ? 2.089   25.079  -56.135  1.00 29.51  ? 217 GLN C CB  1 
ATOM   4570 C  CG  . GLN C 1 225 ? 3.119   25.635  -57.104  1.00 33.62  ? 217 GLN C CG  1 
ATOM   4571 C  CD  . GLN C 1 225 ? 3.091   27.160  -57.211  1.00 36.97  ? 217 GLN C CD  1 
ATOM   4572 O  OE1 . GLN C 1 225 ? 2.065   27.802  -56.972  1.00 48.50  ? 217 GLN C OE1 1 
ATOM   4573 N  NE2 . GLN C 1 225 ? 4.218   27.739  -57.587  1.00 31.71  ? 217 GLN C NE2 1 
ATOM   4574 N  N   . GLN C 1 226 ? -0.138  23.187  -54.959  1.00 29.73  ? 218 GLN C N   1 
ATOM   4575 C  CA  . GLN C 1 226 ? -0.918  22.699  -53.828  1.00 32.23  ? 218 GLN C CA  1 
ATOM   4576 C  C   . GLN C 1 226 ? -0.831  21.181  -53.703  1.00 37.75  ? 218 GLN C C   1 
ATOM   4577 O  O   . GLN C 1 226 ? -0.669  20.655  -52.590  1.00 37.53  ? 218 GLN C O   1 
ATOM   4578 C  CB  . GLN C 1 226 ? -2.363  23.175  -53.966  1.00 37.75  ? 218 GLN C CB  1 
ATOM   4579 C  CG  . GLN C 1 226 ? -2.539  24.587  -53.423  1.00 39.60  ? 218 GLN C CG  1 
ATOM   4580 C  CD  . GLN C 1 226 ? -3.719  25.319  -54.008  1.00 60.81  ? 218 GLN C CD  1 
ATOM   4581 O  OE1 . GLN C 1 226 ? -3.595  26.468  -54.446  1.00 62.88  ? 218 GLN C OE1 1 
ATOM   4582 N  NE2 . GLN C 1 226 ? -4.877  24.661  -54.026  1.00 65.47  ? 218 GLN C NE2 1 
ATOM   4583 N  N   . THR C 1 227 ? -0.888  20.464  -54.837  1.00 30.41  ? 219 THR C N   1 
ATOM   4584 C  CA  . THR C 1 227 ? -0.784  19.003  -54.823  1.00 26.93  ? 219 THR C CA  1 
ATOM   4585 C  C   . THR C 1 227 ? 0.593   18.528  -54.363  1.00 27.62  ? 219 THR C C   1 
ATOM   4586 O  O   . THR C 1 227 ? 0.699   17.560  -53.593  1.00 27.87  ? 219 THR C O   1 
ATOM   4587 C  CB  . THR C 1 227 ? -1.101  18.450  -56.213  1.00 27.65  ? 219 THR C CB  1 
ATOM   4588 O  OG1 . THR C 1 227 ? -2.415  18.870  -56.600  1.00 21.63  ? 219 THR C OG1 1 
ATOM   4589 C  CG2 . THR C 1 227 ? -1.007  16.924  -56.237  1.00 25.43  ? 219 THR C CG2 1 
ATOM   4590 N  N   . ILE C 1 228 ? 1.659   19.175  -54.838  1.00 30.03  ? 220 ILE C N   1 
ATOM   4591 C  CA  . ILE C 1 228 ? 3.006   18.793  -54.412  1.00 31.73  ? 220 ILE C CA  1 
ATOM   4592 C  C   . ILE C 1 228 ? 3.191   19.073  -52.928  1.00 34.07  ? 220 ILE C C   1 
ATOM   4593 O  O   . ILE C 1 228 ? 3.870   18.312  -52.227  1.00 30.72  ? 220 ILE C O   1 
ATOM   4594 C  CB  . ILE C 1 228 ? 4.072   19.527  -55.250  1.00 37.22  ? 220 ILE C CB  1 
ATOM   4595 C  CG1 . ILE C 1 228 ? 4.128   19.002  -56.686  1.00 29.12  ? 220 ILE C CG1 1 
ATOM   4596 C  CG2 . ILE C 1 228 ? 5.450   19.415  -54.621  1.00 32.68  ? 220 ILE C CG2 1 
ATOM   4597 C  CD1 . ILE C 1 228 ? 5.169   19.755  -57.515  1.00 23.28  ? 220 ILE C CD1 1 
ATOM   4598 N  N   . ALA C 1 229 ? 2.580   20.151  -52.421  1.00 31.96  ? 221 ALA C N   1 
ATOM   4599 C  CA  . ALA C 1 229 ? 2.745   20.521  -51.022  1.00 37.27  ? 221 ALA C CA  1 
ATOM   4600 C  C   . ALA C 1 229 ? 1.872   19.694  -50.090  1.00 37.57  ? 221 ALA C C   1 
ATOM   4601 O  O   . ALA C 1 229 ? 2.213   19.545  -48.915  1.00 39.77  ? 221 ALA C O   1 
ATOM   4602 C  CB  . ALA C 1 229 ? 2.451   22.008  -50.827  1.00 30.16  ? 221 ALA C CB  1 
ATOM   4603 N  N   . ALA C 1 230 ? 0.776   19.130  -50.586  1.00 40.03  ? 222 ALA C N   1 
ATOM   4604 C  CA  . ALA C 1 230 ? -0.023  18.223  -49.772  1.00 36.92  ? 222 ALA C CA  1 
ATOM   4605 C  C   . ALA C 1 230 ? 0.510   16.792  -49.771  1.00 35.41  ? 222 ALA C C   1 
ATOM   4606 O  O   . ALA C 1 230 ? 0.100   16.004  -48.916  1.00 37.82  ? 222 ALA C O   1 
ATOM   4607 C  CB  . ALA C 1 230 ? -1.479  18.224  -50.255  1.00 35.13  ? 222 ALA C CB  1 
ATOM   4608 N  N   . ASN C 1 231 ? 1.413   16.438  -50.682  1.00 32.79  ? 223 ASN C N   1 
ATOM   4609 C  CA  . ASN C 1 231 ? 1.804   15.030  -50.856  1.00 29.88  ? 223 ASN C CA  1 
ATOM   4610 C  C   . ASN C 1 231 ? 3.303   14.780  -50.776  1.00 36.49  ? 223 ASN C C   1 
ATOM   4611 O  O   . ASN C 1 231 ? 3.736   13.673  -51.097  1.00 35.86  ? 223 ASN C O   1 
ATOM   4612 C  CB  . ASN C 1 231 ? 1.275   14.507  -52.194  1.00 26.88  ? 223 ASN C CB  1 
ATOM   4613 C  CG  . ASN C 1 231 ? -0.221  14.227  -52.154  1.00 33.74  ? 223 ASN C CG  1 
ATOM   4614 O  OD1 . ASN C 1 231 ? -0.669  13.278  -51.518  1.00 35.30  ? 223 ASN C OD1 1 
ATOM   4615 N  ND2 . ASN C 1 231 ? -1.000  15.102  -52.773  1.00 44.60  ? 223 ASN C ND2 1 
ATOM   4616 O  OXT . ASN C 1 231 ? 4.105   15.640  -50.384  1.00 43.54  ? 223 ASN C OXT 1 
ATOM   4617 N  N   . LEU D 2 4   ? -13.447 1.590   -112.407 1.00 61.92  ? 4   LEU D N   1 
ATOM   4618 C  CA  . LEU D 2 4   ? -12.059 1.960   -111.980 1.00 75.54  ? 4   LEU D CA  1 
ATOM   4619 C  C   . LEU D 2 4   ? -11.795 1.825   -110.465 1.00 75.24  ? 4   LEU D C   1 
ATOM   4620 O  O   . LEU D 2 4   ? -11.290 2.730   -109.866 1.00 63.65  ? 4   LEU D O   1 
ATOM   4621 C  CB  . LEU D 2 4   ? -11.767 3.423   -112.345 1.00 67.25  ? 4   LEU D CB  1 
ATOM   4622 C  CG  . LEU D 2 4   ? -10.395 4.016   -112.545 1.00 83.88  ? 4   LEU D CG  1 
ATOM   4623 C  CD1 . LEU D 2 4   ? -9.995  3.886   -113.998 1.00 78.94  ? 4   LEU D CD1 1 
ATOM   4624 C  CD2 . LEU D 2 4   ? -10.328 5.505   -112.070 1.00 69.45  ? 4   LEU D CD2 1 
ATOM   4625 N  N   . PRO D 2 5   ? -12.083 0.631   -109.983 1.00 62.82  ? 5   PRO D N   1 
ATOM   4626 C  CA  . PRO D 2 5   ? -11.936 0.317   -108.533 1.00 54.07  ? 5   PRO D CA  1 
ATOM   4627 C  C   . PRO D 2 5   ? -10.602 0.732   -107.956 1.00 53.48  ? 5   PRO D C   1 
ATOM   4628 O  O   . PRO D 2 5   ? -9.520  0.381   -108.467 1.00 55.29  ? 5   PRO D O   1 
ATOM   4629 C  CB  . PRO D 2 5   ? -12.151 -1.203  -108.605 1.00 49.60  ? 5   PRO D CB  1 
ATOM   4630 C  CG  . PRO D 2 5   ? -11.725 -0.790  -109.636 1.00 57.66  ? 5   PRO D CG  1 
ATOM   4631 C  CD  . PRO D 2 5   ? -11.933 -0.696  -110.664 1.00 64.31  ? 5   PRO D CD  1 
ATOM   4632 N  N   . LYS D 2 6   ? -10.701 1.480   -106.852 1.00 45.78  ? 6   LYS D N   1 
ATOM   4633 C  CA  . LYS D 2 6   ? -9.503  2.040   -106.190 1.00 47.97  ? 6   LYS D CA  1 
ATOM   4634 C  C   . LYS D 2 6   ? -9.055  1.098   -105.080 1.00 46.18  ? 6   LYS D C   1 
ATOM   4635 O  O   . LYS D 2 6   ? -9.867  0.772   -104.192 1.00 42.98  ? 6   LYS D O   1 
ATOM   4636 C  CB  . LYS D 2 6   ? -9.816  3.406   -105.641 1.00 44.43  ? 6   LYS D CB  1 
ATOM   4637 C  CG  . LYS D 2 6   ? -8.722  4.445   -105.870 1.00 47.60  ? 6   LYS D CG  1 
ATOM   4638 C  CD  . LYS D 2 6   ? -9.216  5.875   -105.753 1.00 47.01  ? 6   LYS D CD  1 
ATOM   4639 C  CE  . LYS D 2 6   ? -10.397 6.159   -106.657 1.00 53.62  ? 6   LYS D CE  1 
ATOM   4640 N  NZ  . LYS D 2 6   ? -9.976  6.340   -108.088 1.00 63.17  ? 6   LYS D NZ  1 
ATOM   4641 N  N   . PRO D 2 7   ? -7.800  0.672   -105.065 1.00 38.41  ? 7   PRO D N   1 
ATOM   4642 C  CA  . PRO D 2 7   ? -7.346  -0.215  -103.999 1.00 34.90  ? 7   PRO D CA  1 
ATOM   4643 C  C   . PRO D 2 7   ? -7.147  0.556   -102.708 1.00 40.27  ? 7   PRO D C   1 
ATOM   4644 O  O   . PRO D 2 7   ? -6.649  1.683   -102.708 1.00 36.44  ? 7   PRO D O   1 
ATOM   4645 C  CB  . PRO D 2 7   ? -6.012  -0.760  -104.529 1.00 39.24  ? 7   PRO D CB  1 
ATOM   4646 C  CG  . PRO D 2 7   ? -6.001  -0.342  -106.017 1.00 42.08  ? 7   PRO D CG  1 
ATOM   4647 C  CD  . PRO D 2 7   ? -6.752  0.927   -106.056 1.00 38.76  ? 7   PRO D CD  1 
ATOM   4648 N  N   . VAL D 2 8   ? -7.558  -0.053  -101.597 1.00 37.39  ? 8   VAL D N   1 
ATOM   4649 C  CA  . VAL D 2 8   ? -7.294  0.546   -100.296 1.00 39.69  ? 8   VAL D CA  1 
ATOM   4650 C  C   . VAL D 2 8   ? -5.811  0.402   -99.982  1.00 36.48  ? 8   VAL D C   1 
ATOM   4651 O  O   . VAL D 2 8   ? -5.181  -0.611  -100.313 1.00 34.32  ? 8   VAL D O   1 
ATOM   4652 C  CB  . VAL D 2 8   ? -8.180  -0.106  -99.219  1.00 33.84  ? 8   VAL D CB  1 
ATOM   4653 C  CG1 . VAL D 2 8   ? -8.059  0.644   -97.897  1.00 31.32  ? 8   VAL D CG1 1 
ATOM   4654 C  CG2 . VAL D 2 8   ? -9.630  -0.123  -99.685  1.00 30.40  ? 8   VAL D CG2 1 
ATOM   4655 N  N   . LEU D 2 9   ? -5.237  1.425   -99.361  1.00 36.02  ? 9   LEU D N   1 
ATOM   4656 C  CA  . LEU D 2 9   ? -3.803  1.473   -99.126  1.00 37.46  ? 9   LEU D CA  1 
ATOM   4657 C  C   . LEU D 2 9   ? -3.500  1.434   -97.633  1.00 38.10  ? 9   LEU D C   1 
ATOM   4658 O  O   . LEU D 2 9   ? -4.306  1.881   -96.808  1.00 33.58  ? 9   LEU D O   1 
ATOM   4659 C  CB  . LEU D 2 9   ? -3.188  2.745   -99.733  1.00 35.11  ? 9   LEU D CB  1 
ATOM   4660 C  CG  . LEU D 2 9   ? -3.384  2.981   -101.225 1.00 41.70  ? 9   LEU D CG  1 
ATOM   4661 C  CD1 . LEU D 2 9   ? -3.043  4.418   -101.537 1.00 38.80  ? 9   LEU D CD1 1 
ATOM   4662 C  CD2 . LEU D 2 9   ? -2.523  2.028   -102.032 1.00 31.38  ? 9   LEU D CD2 1 
ATOM   4663 N  N   . ASP D 2 10  ? -2.310  0.941   -97.289  1.00 32.34  ? 10  ASP D N   1 
ATOM   4664 C  CA  . ASP D 2 10  ? -1.914  0.930   -95.890  1.00 34.93  ? 10  ASP D CA  1 
ATOM   4665 C  C   . ASP D 2 10  ? -1.112  2.198   -95.558  1.00 38.66  ? 10  ASP D C   1 
ATOM   4666 O  O   . ASP D 2 10  ? -0.958  3.113   -96.375  1.00 36.53  ? 10  ASP D O   1 
ATOM   4667 C  CB  . ASP D 2 10  ? -1.183  -0.380  -95.551  1.00 36.49  ? 10  ASP D CB  1 
ATOM   4668 C  CG  . ASP D 2 10  ? 0.169   -0.530  -96.230  1.00 40.45  ? 10  ASP D CG  1 
ATOM   4669 O  OD1 . ASP D 2 10  ? 0.754   0.480   -96.679  1.00 36.41  ? 10  ASP D OD1 1 
ATOM   4670 O  OD2 . ASP D 2 10  ? 0.639   -1.694  -96.322  1.00 42.48  ? 10  ASP D OD2 1 
ATOM   4671 N  N   . THR D 2 11  ? -0.599  2.266   -94.334  1.00 31.57  ? 11  THR D N   1 
ATOM   4672 C  CA  . THR D 2 11  ? 0.135   3.447   -93.897  1.00 42.38  ? 11  THR D CA  1 
ATOM   4673 C  C   . THR D 2 11  ? 1.484   3.603   -94.605  1.00 41.49  ? 11  THR D C   1 
ATOM   4674 O  O   . THR D 2 11  ? 2.080   4.682   -94.515  1.00 43.23  ? 11  THR D O   1 
ATOM   4675 C  CB  . THR D 2 11  ? 0.318   3.402   -92.366  1.00 28.83  ? 11  THR D CB  1 
ATOM   4676 O  OG1 . THR D 2 11  ? 0.866   2.134   -91.982  1.00 34.74  ? 11  THR D OG1 1 
ATOM   4677 C  CG2 . THR D 2 11  ? -1.032  3.588   -91.648  1.00 24.52  ? 11  THR D CG2 1 
ATOM   4678 N  N   . ASN D 2 12  ? 1.975   2.568   -95.301  1.00 38.65  ? 12  ASN D N   1 
ATOM   4679 C  CA  . ASN D 2 12  ? 3.127   2.673   -96.194  1.00 40.39  ? 12  ASN D CA  1 
ATOM   4680 C  C   . ASN D 2 12  ? 2.734   2.797   -97.662  1.00 48.20  ? 12  ASN D C   1 
ATOM   4681 O  O   . ASN D 2 12  ? 3.584   2.612   -98.539  1.00 48.75  ? 12  ASN D O   1 
ATOM   4682 C  CB  . ASN D 2 12  ? 4.050   1.474   -96.022  1.00 39.58  ? 12  ASN D CB  1 
ATOM   4683 C  CG  . ASN D 2 12  ? 4.210   1.094   -94.597  1.00 44.88  ? 12  ASN D CG  1 
ATOM   4684 O  OD1 . ASN D 2 12  ? 4.338   1.963   -93.748  1.00 45.61  ? 12  ASN D OD1 1 
ATOM   4685 N  ND2 . ASN D 2 12  ? 4.190   -0.203  -94.307  1.00 46.65  ? 12  ASN D ND2 1 
ATOM   4686 N  N   . GLY D 2 13  ? 1.469   3.086   -97.954  1.00 39.53  ? 13  GLY D N   1 
ATOM   4687 C  CA  . GLY D 2 13  ? 1.065   3.257   -99.328  1.00 29.73  ? 13  GLY D CA  1 
ATOM   4688 C  C   . GLY D 2 13  ? 0.916   1.986   -100.128 1.00 36.30  ? 13  GLY D C   1 
ATOM   4689 O  O   . GLY D 2 13  ? 0.563   2.061   -101.310 1.00 36.53  ? 13  GLY D O   1 
ATOM   4690 N  N   . LYS D 2 14  ? 1.174   0.822   -99.539  1.00 37.92  ? 14  LYS D N   1 
ATOM   4691 C  CA  . LYS D 2 14  ? 0.906   -0.434  -100.224 1.00 38.64  ? 14  LYS D CA  1 
ATOM   4692 C  C   . LYS D 2 14  ? -0.586  -0.746  -100.186 1.00 40.85  ? 14  LYS D C   1 
ATOM   4693 O  O   . LYS D 2 14  ? -1.269  -0.486  -99.189  1.00 45.00  ? 14  LYS D O   1 
ATOM   4694 C  CB  . LYS D 2 14  ? 1.701   -1.575  -99.588  1.00 43.21  ? 14  LYS D CB  1 
ATOM   4695 C  CG  . LYS D 2 14  ? 1.582   -2.965  -100.279 1.00 58.05  ? 14  LYS D CG  1 
ATOM   4696 C  CD  . LYS D 2 14  ? 1.362   -2.938  -101.808 1.00 55.65  ? 14  LYS D CD  1 
ATOM   4697 C  CE  . LYS D 2 14  ? 1.978   -4.170  -102.469 1.00 62.06  ? 14  LYS D CE  1 
ATOM   4698 N  NZ  . LYS D 2 14  ? 1.581   -5.436  -101.767 1.00 66.35  ? 14  LYS D NZ  1 
ATOM   4699 N  N   . LYS D 2 15  ? -1.086  -1.291  -101.290 1.00 41.57  ? 15  LYS D N   1 
ATOM   4700 C  CA  . LYS D 2 15  ? -2.457  -1.775  -101.363 1.00 47.29  ? 15  LYS D CA  1 
ATOM   4701 C  C   . LYS D 2 15  ? -2.738  -2.824  -100.289 1.00 46.64  ? 15  LYS D C   1 
ATOM   4702 O  O   . LYS D 2 15  ? -1.863  -3.602  -99.891  1.00 44.54  ? 15  LYS D O   1 
ATOM   4703 C  CB  . LYS D 2 15  ? -2.730  -2.379  -102.741 1.00 42.76  ? 15  LYS D CB  1 
ATOM   4704 C  CG  . LYS D 2 15  ? -1.785  -1.887  -103.821 1.00 53.34  ? 15  LYS D CG  1 
ATOM   4705 C  CD  . LYS D 2 15  ? -2.441  -1.948  -105.192 1.00 42.58  ? 15  LYS D CD  1 
ATOM   4706 C  CE  . LYS D 2 15  ? -1.442  -2.354  -106.243 1.00 40.04  ? 15  LYS D CE  1 
ATOM   4707 N  NZ  . LYS D 2 15  ? -2.096  -2.576  -107.556 1.00 64.25  ? 15  LYS D NZ  1 
ATOM   4708 N  N   . LEU D 2 16  ? -3.989  -2.860  -99.842  1.00 36.79  ? 16  LEU D N   1 
ATOM   4709 C  CA  . LEU D 2 16  ? -4.398  -3.858  -98.869  1.00 38.33  ? 16  LEU D CA  1 
ATOM   4710 C  C   . LEU D 2 16  ? -4.434  -5.239  -99.513  1.00 40.30  ? 16  LEU D C   1 
ATOM   4711 O  O   . LEU D 2 16  ? -4.865  -5.403  -100.657 1.00 46.22  ? 16  LEU D O   1 
ATOM   4712 C  CB  . LEU D 2 16  ? -5.763  -3.501  -98.290  1.00 40.06  ? 16  LEU D CB  1 
ATOM   4713 C  CG  . LEU D 2 16  ? -5.718  -3.079  -96.826  1.00 35.19  ? 16  LEU D CG  1 
ATOM   4714 C  CD1 . LEU D 2 16  ? -4.874  -1.835  -96.718  1.00 37.57  ? 16  LEU D CD1 1 
ATOM   4715 C  CD2 . LEU D 2 16  ? -7.106  -2.771  -96.344  1.00 37.65  ? 16  LEU D CD2 1 
ATOM   4716 N  N   . ASN D 2 17  ? -3.997  -6.237  -98.756  1.00 36.02  ? 17  ASN D N   1 
ATOM   4717 C  CA  . ASN D 2 17  ? -3.825  -7.593  -99.244  1.00 37.06  ? 17  ASN D CA  1 
ATOM   4718 C  C   . ASN D 2 17  ? -4.660  -8.557  -98.418  1.00 40.24  ? 17  ASN D C   1 
ATOM   4719 O  O   . ASN D 2 17  ? -4.509  -8.590  -97.186  1.00 40.46  ? 17  ASN D O   1 
ATOM   4720 C  CB  . ASN D 2 17  ? -2.347  -7.971  -99.169  1.00 44.18  ? 17  ASN D CB  1 
ATOM   4721 C  CG  . ASN D 2 17  ? -2.039  -9.273  -99.860  1.00 50.34  ? 17  ASN D CG  1 
ATOM   4722 O  OD1 . ASN D 2 17  ? -2.803  -10.238 -99.780  1.00 49.98  ? 17  ASN D OD1 1 
ATOM   4723 N  ND2 . ASN D 2 17  ? -0.902  -9.315  -100.539 1.00 61.39  ? 17  ASN D ND2 1 
ATOM   4724 N  N   . PRO D 2 18  ? -5.517  -9.381  -99.028  1.00 42.04  ? 18  PRO D N   1 
ATOM   4725 C  CA  . PRO D 2 18  ? -6.274  -10.365 -98.230  1.00 44.03  ? 18  PRO D CA  1 
ATOM   4726 C  C   . PRO D 2 18  ? -5.383  -11.312 -97.474  1.00 41.75  ? 18  PRO D C   1 
ATOM   4727 O  O   . PRO D 2 18  ? -5.852  -11.957 -96.530  1.00 32.89  ? 18  PRO D O   1 
ATOM   4728 C  CB  . PRO D 2 18  ? -7.112  -11.111 -99.278  1.00 27.99  ? 18  PRO D CB  1 
ATOM   4729 C  CG  . PRO D 2 18  ? -7.212  -10.132 -100.419 1.00 42.04  ? 18  PRO D CG  1 
ATOM   4730 C  CD  . PRO D 2 18  ? -5.865  -9.458  -100.456 1.00 36.28  ? 18  PRO D CD  1 
ATOM   4731 N  N   . ASN D 2 19  ? -4.110  -11.406 -97.849  1.00 39.92  ? 19  ASN D N   1 
ATOM   4732 C  CA  . ASN D 2 19  ? -3.176  -12.308 -97.203  1.00 44.83  ? 19  ASN D CA  1 
ATOM   4733 C  C   . ASN D 2 19  ? -2.290  -11.611 -96.160  1.00 51.99  ? 19  ASN D C   1 
ATOM   4734 O  O   . ASN D 2 19  ? -1.472  -12.279 -95.520  1.00 42.54  ? 19  ASN D O   1 
ATOM   4735 C  CB  . ASN D 2 19  ? -2.316  -12.994 -98.273  1.00 52.97  ? 19  ASN D CB  1 
ATOM   4736 C  CG  . ASN D 2 19  ? -2.988  -14.239 -98.873  1.00 66.81  ? 19  ASN D CG  1 
ATOM   4737 O  OD1 . ASN D 2 19  ? -2.983  -14.434 -100.092 1.00 69.13  ? 19  ASN D OD1 1 
ATOM   4738 N  ND2 . ASN D 2 19  ? -3.557  -15.086 -98.019  1.00 74.54  ? 19  ASN D ND2 1 
ATOM   4739 N  N   . SER D 2 20  ? -2.430  -10.297 -95.963  1.00 48.62  ? 20  SER D N   1 
ATOM   4740 C  CA  . SER D 2 20  ? -1.761  -9.602  -94.867  1.00 35.13  ? 20  SER D CA  1 
ATOM   4741 C  C   . SER D 2 20  ? -2.708  -9.443  -93.677  1.00 41.50  ? 20  SER D C   1 
ATOM   4742 O  O   . SER D 2 20  ? -3.905  -9.722  -93.754  1.00 49.22  ? 20  SER D O   1 
ATOM   4743 C  CB  . SER D 2 20  ? -1.263  -8.215  -95.291  1.00 41.02  ? 20  SER D CB  1 
ATOM   4744 O  OG  . SER D 2 20  ? -0.615  -8.218  -96.543  1.00 50.75  ? 20  SER D OG  1 
ATOM   4745 N  N   . SER D 2 21  ? -2.151  -8.964  -92.569  1.00 34.14  ? 21  SER D N   1 
ATOM   4746 C  CA  . SER D 2 21  ? -2.907  -8.546  -91.400  1.00 39.08  ? 21  SER D CA  1 
ATOM   4747 C  C   . SER D 2 21  ? -2.689  -7.056  -91.196  1.00 38.34  ? 21  SER D C   1 
ATOM   4748 O  O   . SER D 2 21  ? -1.647  -6.520  -91.579  1.00 39.98  ? 21  SER D O   1 
ATOM   4749 C  CB  . SER D 2 21  ? -2.457  -9.295  -90.154  1.00 35.00  ? 21  SER D CB  1 
ATOM   4750 O  OG  . SER D 2 21  ? -2.876  -10.640 -90.221  1.00 47.43  ? 21  SER D OG  1 
ATOM   4751 N  N   . TYR D 2 22  ? -3.657  -6.381  -90.579  1.00 32.50  ? 22  TYR D N   1 
ATOM   4752 C  CA  . TYR D 2 22  ? -3.514  -4.946  -90.384  1.00 27.27  ? 22  TYR D CA  1 
ATOM   4753 C  C   . TYR D 2 22  ? -4.138  -4.507  -89.073  1.00 34.58  ? 22  TYR D C   1 
ATOM   4754 O  O   . TYR D 2 22  ? -5.232  -4.948  -88.702  1.00 37.35  ? 22  TYR D O   1 
ATOM   4755 C  CB  . TYR D 2 22  ? -4.151  -4.136  -91.519  1.00 27.99  ? 22  TYR D CB  1 
ATOM   4756 C  CG  . TYR D 2 22  ? -3.670  -4.486  -92.919  1.00 38.28  ? 22  TYR D CG  1 
ATOM   4757 C  CD1 . TYR D 2 22  ? -2.553  -3.864  -93.464  1.00 32.51  ? 22  TYR D CD1 1 
ATOM   4758 C  CD2 . TYR D 2 22  ? -4.349  -5.427  -93.703  1.00 30.62  ? 22  TYR D CD2 1 
ATOM   4759 C  CE1 . TYR D 2 22  ? -2.113  -4.170  -94.729  1.00 34.60  ? 22  TYR D CE1 1 
ATOM   4760 C  CE2 . TYR D 2 22  ? -3.919  -5.732  -94.981  1.00 33.91  ? 22  TYR D CE2 1 
ATOM   4761 C  CZ  . TYR D 2 22  ? -2.797  -5.099  -95.488  1.00 38.23  ? 22  TYR D CZ  1 
ATOM   4762 O  OH  . TYR D 2 22  ? -2.342  -5.390  -96.756  1.00 47.24  ? 22  TYR D OH  1 
ATOM   4763 N  N   . ARG D 2 23  ? -3.439  -3.604  -88.394  1.00 25.23  ? 23  ARG D N   1 
ATOM   4764 C  CA  . ARG D 2 23  ? -4.006  -2.924  -87.246  1.00 30.48  ? 23  ARG D CA  1 
ATOM   4765 C  C   . ARG D 2 23  ? -4.846  -1.757  -87.742  1.00 35.20  ? 23  ARG D C   1 
ATOM   4766 O  O   . ARG D 2 23  ? -4.419  -1.007  -88.627  1.00 39.66  ? 23  ARG D O   1 
ATOM   4767 C  CB  . ARG D 2 23  ? -2.899  -2.439  -86.297  1.00 26.51  ? 23  ARG D CB  1 
ATOM   4768 C  CG  . ARG D 2 23  ? -2.429  -3.541  -85.372  1.00 29.77  ? 23  ARG D CG  1 
ATOM   4769 C  CD  . ARG D 2 23  ? -1.332  -3.121  -84.443  1.00 41.46  ? 23  ARG D CD  1 
ATOM   4770 N  NE  . ARG D 2 23  ? -1.045  -4.198  -83.503  1.00 37.66  ? 23  ARG D NE  1 
ATOM   4771 C  CZ  . ARG D 2 23  ? -0.142  -5.153  -83.694  1.00 40.45  ? 23  ARG D CZ  1 
ATOM   4772 N  NH1 . ARG D 2 23  ? 0.648   -5.154  -84.760  1.00 29.31  ? 23  ARG D NH1 1 
ATOM   4773 N  NH2 . ARG D 2 23  ? -0.017  -6.120  -82.784  1.00 30.47  ? 23  ARG D NH2 1 
ATOM   4774 N  N   . ILE D 2 24  ? -6.049  -1.618  -87.198  1.00 26.77  ? 24  ILE D N   1 
ATOM   4775 C  CA  . ILE D 2 24  ? -6.889  -0.469  -87.502  1.00 31.75  ? 24  ILE D CA  1 
ATOM   4776 C  C   . ILE D 2 24  ? -6.583  0.624   -86.486  1.00 23.25  ? 24  ILE D C   1 
ATOM   4777 O  O   . ILE D 2 24  ? -6.937  0.510   -85.312  1.00 27.90  ? 24  ILE D O   1 
ATOM   4778 C  CB  . ILE D 2 24  ? -8.373  -0.836  -87.509  1.00 23.74  ? 24  ILE D CB  1 
ATOM   4779 C  CG1 . ILE D 2 24  ? -8.615  -1.971  -88.503  1.00 19.97  ? 24  ILE D CG1 1 
ATOM   4780 C  CG2 . ILE D 2 24  ? -9.175  0.388   -87.891  1.00 17.69  ? 24  ILE D CG2 1 
ATOM   4781 C  CD1 . ILE D 2 24  ? -10.063 -2.434  -88.563  1.00 23.21  ? 24  ILE D CD1 1 
ATOM   4782 N  N   . ILE D 2 25  ? -5.923  1.685   -86.945  1.00 22.22  ? 25  ILE D N   1 
ATOM   4783 C  CA  . ILE D 2 25  ? -5.446  2.749   -86.081  1.00 22.09  ? 25  ILE D CA  1 
ATOM   4784 C  C   . ILE D 2 25  ? -6.236  4.009   -86.383  1.00 28.85  ? 25  ILE D C   1 
ATOM   4785 O  O   . ILE D 2 25  ? -6.849  4.171   -87.442  1.00 32.17  ? 25  ILE D O   1 
ATOM   4786 C  CB  . ILE D 2 25  ? -3.938  3.041   -86.233  1.00 22.60  ? 25  ILE D CB  1 
ATOM   4787 C  CG1 . ILE D 2 25  ? -3.672  3.751   -87.563  1.00 31.10  ? 25  ILE D CG1 1 
ATOM   4788 C  CG2 . ILE D 2 25  ? -3.101  1.768   -86.132  1.00 24.34  ? 25  ILE D CG2 1 
ATOM   4789 C  CD1 . ILE D 2 25  ? -2.258  4.266   -87.684  1.00 30.88  ? 25  ILE D CD1 1 
ATOM   4790 N  N   . SER D 2 26  ? -6.176  4.921   -85.434  1.00 23.01  ? 26  SER D N   1 
ATOM   4791 C  CA  . SER D 2 26  ? -6.870  6.186   -85.487  1.00 23.64  ? 26  SER D CA  1 
ATOM   4792 C  C   . SER D 2 26  ? -6.008  7.214   -86.203  1.00 27.01  ? 26  SER D C   1 
ATOM   4793 O  O   . SER D 2 26  ? -4.784  7.249   -86.030  1.00 25.53  ? 26  SER D O   1 
ATOM   4794 C  CB  . SER D 2 26  ? -7.170  6.646   -84.057  1.00 22.07  ? 26  SER D CB  1 
ATOM   4795 O  OG  . SER D 2 26  ? -7.737  7.932   -84.049  1.00 44.81  ? 26  SER D OG  1 
ATOM   4796 N  N   . THR D 2 27  ? -6.649  8.042   -87.026  1.00 33.39  ? 27  THR D N   1 
ATOM   4797 C  CA  . THR D 2 27  ? -5.959  9.225   -87.534  1.00 30.86  ? 27  THR D CA  1 
ATOM   4798 C  C   . THR D 2 27  ? -5.641  10.189  -86.391  1.00 29.19  ? 27  THR D C   1 
ATOM   4799 O  O   . THR D 2 27  ? -4.585  10.831  -86.379  1.00 23.22  ? 27  THR D O   1 
ATOM   4800 C  CB  . THR D 2 27  ? -6.809  9.901   -88.608  1.00 25.75  ? 27  THR D CB  1 
ATOM   4801 O  OG1 . THR D 2 27  ? -7.082  8.960   -89.652  1.00 32.40  ? 27  THR D OG1 1 
ATOM   4802 C  CG2 . THR D 2 27  ? -6.067  11.072  -89.210  1.00 37.24  ? 27  THR D CG2 1 
ATOM   4803 N  N   . PHE D 2 28  ? -6.543  10.304  -85.417  1.00 36.02  ? 28  PHE D N   1 
ATOM   4804 C  CA  . PHE D 2 28  ? -6.194  10.983  -84.174  1.00 38.40  ? 28  PHE D CA  1 
ATOM   4805 C  C   . PHE D 2 28  ? -5.035  10.260  -83.496  1.00 32.09  ? 28  PHE D C   1 
ATOM   4806 O  O   . PHE D 2 28  ? -4.897  9.034   -83.590  1.00 27.04  ? 28  PHE D O   1 
ATOM   4807 C  CB  . PHE D 2 28  ? -7.392  11.018  -83.230  1.00 36.20  ? 28  PHE D CB  1 
ATOM   4808 C  CG  . PHE D 2 28  ? -8.373  12.114  -83.533  1.00 34.38  ? 28  PHE D CG  1 
ATOM   4809 C  CD1 . PHE D 2 28  ? -8.014  13.440  -83.399  1.00 36.83  ? 28  PHE D CD1 1 
ATOM   4810 C  CD2 . PHE D 2 28  ? -9.653  11.812  -83.970  1.00 36.44  ? 28  PHE D CD2 1 
ATOM   4811 C  CE1 . PHE D 2 28  ? -8.914  14.445  -83.681  1.00 33.33  ? 28  PHE D CE1 1 
ATOM   4812 C  CE2 . PHE D 2 28  ? -10.553 12.817  -84.251  1.00 37.73  ? 28  PHE D CE2 1 
ATOM   4813 C  CZ  . PHE D 2 28  ? -10.181 14.132  -84.098  1.00 28.36  ? 28  PHE D CZ  1 
ATOM   4814 N  N   . TRP D 2 29  ? -4.181  11.023  -82.822  1.00 20.36  ? 29  TRP D N   1 
ATOM   4815 C  CA  . TRP D 2 29  ? -3.137  10.423  -82.005  1.00 25.76  ? 29  TRP D CA  1 
ATOM   4816 C  C   . TRP D 2 29  ? -3.190  11.034  -80.609  1.00 29.30  ? 29  TRP D C   1 
ATOM   4817 O  O   . TRP D 2 29  ? -3.894  12.019  -80.365  1.00 28.70  ? 29  TRP D O   1 
ATOM   4818 C  CB  . TRP D 2 29  ? -1.746  10.578  -82.647  1.00 29.64  ? 29  TRP D CB  1 
ATOM   4819 C  CG  . TRP D 2 29  ? -1.309  12.000  -82.833  1.00 30.27  ? 29  TRP D CG  1 
ATOM   4820 C  CD1 . TRP D 2 29  ? -1.479  12.774  -83.951  1.00 36.51  ? 29  TRP D CD1 1 
ATOM   4821 C  CD2 . TRP D 2 29  ? -0.635  12.820  -81.876  1.00 33.13  ? 29  TRP D CD2 1 
ATOM   4822 N  NE1 . TRP D 2 29  ? -0.961  14.035  -83.740  1.00 37.01  ? 29  TRP D NE1 1 
ATOM   4823 C  CE2 . TRP D 2 29  ? -0.438  14.088  -82.473  1.00 34.24  ? 29  TRP D CE2 1 
ATOM   4824 C  CE3 . TRP D 2 29  ? -0.185  12.613  -80.563  1.00 36.44  ? 29  TRP D CE3 1 
ATOM   4825 C  CZ2 . TRP D 2 29  ? 0.193   15.136  -81.807  1.00 30.28  ? 29  TRP D CZ2 1 
ATOM   4826 C  CZ3 . TRP D 2 29  ? 0.451   13.662  -79.903  1.00 30.36  ? 29  TRP D CZ3 1 
ATOM   4827 C  CH2 . TRP D 2 29  ? 0.632   14.904  -80.529  1.00 23.90  ? 29  TRP D CH2 1 
ATOM   4828 N  N   . GLY D 2 30  ? -2.457  10.426  -79.676  1.00 26.71  ? 30  GLY D N   1 
ATOM   4829 C  CA  . GLY D 2 30  ? -2.411  10.942  -78.317  1.00 29.61  ? 30  GLY D CA  1 
ATOM   4830 C  C   . GLY D 2 30  ? -3.629  10.557  -77.494  1.00 33.30  ? 30  GLY D C   1 
ATOM   4831 O  O   . GLY D 2 30  ? -4.061  9.397   -77.526  1.00 25.47  ? 30  GLY D O   1 
ATOM   4832 N  N   . ALA D 2 31  ? -4.200  11.527  -76.763  1.00 33.02  ? 31  ALA D N   1 
ATOM   4833 C  CA  . ALA D 2 31  ? -5.364  11.245  -75.925  1.00 36.18  ? 31  ALA D CA  1 
ATOM   4834 C  C   . ALA D 2 31  ? -6.572  10.799  -76.744  1.00 33.80  ? 31  ALA D C   1 
ATOM   4835 O  O   . ALA D 2 31  ? -7.453  10.114  -76.212  1.00 31.19  ? 31  ALA D O   1 
ATOM   4836 C  CB  . ALA D 2 31  ? -5.726  12.471  -75.088  1.00 26.77  ? 31  ALA D CB  1 
ATOM   4837 N  N   . LEU D 2 32  ? -6.621  11.153  -78.023  1.00 29.52  ? 32  LEU D N   1 
ATOM   4838 C  CA  . LEU D 2 32  ? -7.693  10.739  -78.916  1.00 28.59  ? 32  LEU D CA  1 
ATOM   4839 C  C   . LEU D 2 32  ? -7.286  9.577   -79.825  1.00 32.46  ? 32  LEU D C   1 
ATOM   4840 O  O   . LEU D 2 32  ? -8.062  9.192   -80.710  1.00 28.48  ? 32  LEU D O   1 
ATOM   4841 C  CB  . LEU D 2 32  ? -8.140  11.937  -79.752  1.00 29.59  ? 32  LEU D CB  1 
ATOM   4842 C  CG  . LEU D 2 32  ? -9.618  12.039  -80.121  1.00 47.33  ? 32  LEU D CG  1 
ATOM   4843 C  CD1 . LEU D 2 32  ? -10.509 11.373  -79.078  1.00 35.50  ? 32  LEU D CD1 1 
ATOM   4844 C  CD2 . LEU D 2 32  ? -9.992  13.509  -80.264  1.00 41.99  ? 32  LEU D CD2 1 
ATOM   4845 N  N   . GLY D 2 33  ? -6.082  9.023   -79.651  1.00 23.06  ? 33  GLY D N   1 
ATOM   4846 C  CA  . GLY D 2 33  ? -5.693  7.832   -80.381  1.00 22.29  ? 33  GLY D CA  1 
ATOM   4847 C  C   . GLY D 2 33  ? -6.273  6.585   -79.730  1.00 24.26  ? 33  GLY D C   1 
ATOM   4848 O  O   . GLY D 2 33  ? -6.959  6.638   -78.708  1.00 27.01  ? 33  GLY D O   1 
ATOM   4849 N  N   . GLY D 2 34  ? -5.975  5.439   -80.331  1.00 24.93  ? 34  GLY D N   1 
ATOM   4850 C  CA  . GLY D 2 34  ? -6.461  4.174   -79.817  1.00 17.29  ? 34  GLY D CA  1 
ATOM   4851 C  C   . GLY D 2 34  ? -6.912  3.250   -80.936  1.00 23.08  ? 34  GLY D C   1 
ATOM   4852 O  O   . GLY D 2 34  ? -7.932  3.515   -81.575  1.00 25.69  ? 34  GLY D O   1 
ATOM   4853 N  N   . ASP D 2 35  ? -6.179  2.162   -81.177  1.00 25.81  ? 35  ASP D N   1 
ATOM   4854 C  CA  . ASP D 2 35  ? -6.510  1.215   -82.238  1.00 25.90  ? 35  ASP D CA  1 
ATOM   4855 C  C   . ASP D 2 35  ? -7.702  0.356   -81.847  1.00 25.65  ? 35  ASP D C   1 
ATOM   4856 O  O   . ASP D 2 35  ? -8.002  0.159   -80.663  1.00 23.79  ? 35  ASP D O   1 
ATOM   4857 C  CB  . ASP D 2 35  ? -5.359  0.256   -82.535  1.00 31.22  ? 35  ASP D CB  1 
ATOM   4858 C  CG  . ASP D 2 35  ? -4.027  0.937   -82.630  1.00 34.91  ? 35  ASP D CG  1 
ATOM   4859 O  OD1 . ASP D 2 35  ? -4.002  2.186   -82.714  1.00 38.84  ? 35  ASP D OD1 1 
ATOM   4860 O  OD2 . ASP D 2 35  ? -3.008  0.205   -82.610  1.00 40.06  ? 35  ASP D OD2 1 
ATOM   4861 N  N   . VAL D 2 36  ? -8.345  -0.203  -82.871  1.00 19.62  ? 36  VAL D N   1 
ATOM   4862 C  CA  . VAL D 2 36  ? -9.425  -1.160  -82.671  1.00 22.14  ? 36  VAL D CA  1 
ATOM   4863 C  C   . VAL D 2 36  ? -8.865  -2.440  -82.070  1.00 22.62  ? 36  VAL D C   1 
ATOM   4864 O  O   . VAL D 2 36  ? -7.797  -2.921  -82.473  1.00 26.03  ? 36  VAL D O   1 
ATOM   4865 C  CB  . VAL D 2 36  ? -10.143 -1.435  -84.005  1.00 24.22  ? 36  VAL D CB  1 
ATOM   4866 C  CG1 . VAL D 2 36  ? -11.012 -2.687  -83.910  1.00 20.10  ? 36  VAL D CG1 1 
ATOM   4867 C  CG2 . VAL D 2 36  ? -10.975 -0.234  -84.407  1.00 17.29  ? 36  VAL D CG2 1 
ATOM   4868 N  N   . TYR D 2 37  ? -9.577  -2.995  -81.088  1.00 25.23  ? 37  TYR D N   1 
ATOM   4869 C  CA  . TYR D 2 37  ? -9.185  -4.261  -80.484  1.00 23.43  ? 37  TYR D CA  1 
ATOM   4870 C  C   . TYR D 2 37  ? -10.418 -5.069  -80.104  1.00 24.13  ? 37  TYR D C   1 
ATOM   4871 O  O   . TYR D 2 37  ? -11.537 -4.555  -80.011  1.00 24.26  ? 37  TYR D O   1 
ATOM   4872 C  CB  . TYR D 2 37  ? -8.281  -4.068  -79.246  1.00 20.29  ? 37  TYR D CB  1 
ATOM   4873 C  CG  . TYR D 2 37  ? -8.992  -3.532  -78.017  1.00 21.69  ? 37  TYR D CG  1 
ATOM   4874 C  CD1 . TYR D 2 37  ? -9.212  -2.168  -77.860  1.00 17.96  ? 37  TYR D CD1 1 
ATOM   4875 C  CD2 . TYR D 2 37  ? -9.437  -4.394  -77.009  1.00 25.63  ? 37  TYR D CD2 1 
ATOM   4876 C  CE1 . TYR D 2 37  ? -9.865  -1.666  -76.753  1.00 21.59  ? 37  TYR D CE1 1 
ATOM   4877 C  CE2 . TYR D 2 37  ? -10.092 -3.906  -75.883  1.00 24.46  ? 37  TYR D CE2 1 
ATOM   4878 C  CZ  . TYR D 2 37  ? -10.294 -2.533  -75.759  1.00 25.96  ? 37  TYR D CZ  1 
ATOM   4879 O  OH  . TYR D 2 37  ? -10.930 -2.022  -74.651  1.00 21.44  ? 37  TYR D OH  1 
ATOM   4880 N  N   . LEU D 2 38  ? -10.181 -6.353  -79.880  1.00 24.37  ? 38  LEU D N   1 
ATOM   4881 C  CA  . LEU D 2 38  ? -11.208 -7.307  -79.498  1.00 26.87  ? 38  LEU D CA  1 
ATOM   4882 C  C   . LEU D 2 38  ? -11.191 -7.449  -77.983  1.00 25.39  ? 38  LEU D C   1 
ATOM   4883 O  O   . LEU D 2 38  ? -10.154 -7.782  -77.401  1.00 26.46  ? 38  LEU D O   1 
ATOM   4884 C  CB  . LEU D 2 38  ? -10.957 -8.656  -80.173  1.00 23.10  ? 38  LEU D CB  1 
ATOM   4885 C  CG  . LEU D 2 38  ? -11.731 -9.884  -79.686  1.00 26.13  ? 38  LEU D CG  1 
ATOM   4886 C  CD1 . LEU D 2 38  ? -13.222 -9.706  -79.935  1.00 22.51  ? 38  LEU D CD1 1 
ATOM   4887 C  CD2 . LEU D 2 38  ? -11.213 -11.153 -80.343  1.00 16.00  ? 38  LEU D CD2 1 
ATOM   4888 N  N   . GLY D 2 39  ? -12.334 -7.197  -77.351  1.00 25.34  ? 39  GLY D N   1 
ATOM   4889 C  CA  . GLY D 2 39  ? -12.464 -7.339  -75.916  1.00 27.53  ? 39  GLY D CA  1 
ATOM   4890 C  C   . GLY D 2 39  ? -13.839 -7.876  -75.570  1.00 36.03  ? 39  GLY D C   1 
ATOM   4891 O  O   . GLY D 2 39  ? -14.681 -8.079  -76.446  1.00 29.60  ? 39  GLY D O   1 
ATOM   4892 N  N   . LYS D 2 40  ? -14.050 -8.120  -74.282  1.00 40.43  ? 40  LYS D N   1 
ATOM   4893 C  CA  . LYS D 2 40  ? -15.338 -8.630  -73.842  1.00 41.33  ? 40  LYS D CA  1 
ATOM   4894 C  C   . LYS D 2 40  ? -16.324 -7.485  -73.689  1.00 36.94  ? 40  LYS D C   1 
ATOM   4895 O  O   . LYS D 2 40  ? -15.968 -6.396  -73.232  1.00 34.15  ? 40  LYS D O   1 
ATOM   4896 C  CB  . LYS D 2 40  ? -15.215 -9.396  -72.523  1.00 36.31  ? 40  LYS D CB  1 
ATOM   4897 C  CG  . LYS D 2 40  ? -16.488 -10.185 -72.137  1.00 53.82  ? 40  LYS D CG  1 
ATOM   4898 C  CD  . LYS D 2 40  ? -16.741 -11.387 -73.070  1.00 53.94  ? 40  LYS D CD  1 
ATOM   4899 C  CE  . LYS D 2 40  ? -17.738 -12.390 -72.461  1.00 62.39  ? 40  LYS D CE  1 
ATOM   4900 N  NZ  . LYS D 2 40  ? -17.110 -13.680 -71.985  1.00 52.26  ? 40  LYS D NZ  1 
ATOM   4901 N  N   A SER D 2 41  ? -17.571 -7.740  -74.092  0.41 36.72  ? 41  SER D N   1 
ATOM   4902 N  N   B SER D 2 41  ? -17.560 -7.731  -74.107  0.59 36.65  ? 41  SER D N   1 
ATOM   4903 C  CA  A SER D 2 41  ? -18.693 -6.829  -73.920  0.41 39.05  ? 41  SER D CA  1 
ATOM   4904 C  CA  B SER D 2 41  ? -18.655 -6.804  -73.901  0.59 39.02  ? 41  SER D CA  1 
ATOM   4905 C  C   A SER D 2 41  ? -19.232 -6.949  -72.493  0.41 47.84  ? 41  SER D C   1 
ATOM   4906 C  C   B SER D 2 41  ? -19.185 -6.937  -72.472  0.59 47.94  ? 41  SER D C   1 
ATOM   4907 O  O   A SER D 2 41  ? -19.250 -8.046  -71.925  0.41 46.94  ? 41  SER D O   1 
ATOM   4908 O  O   B SER D 2 41  ? -19.155 -8.025  -71.887  0.59 46.92  ? 41  SER D O   1 
ATOM   4909 C  CB  A SER D 2 41  ? -19.797 -7.151  -74.935  0.41 41.16  ? 41  SER D CB  1 
ATOM   4910 C  CB  B SER D 2 41  ? -19.778 -7.069  -74.904  0.59 41.19  ? 41  SER D CB  1 
ATOM   4911 O  OG  A SER D 2 41  ? -20.696 -6.068  -75.125  0.41 42.60  ? 41  SER D OG  1 
ATOM   4912 O  OG  B SER D 2 41  ? -19.274 -7.448  -76.178  0.59 38.70  ? 41  SER D OG  1 
ATOM   4913 N  N   . PRO D 2 42  ? -19.667 -5.845  -71.888  1.00 49.58  ? 42  PRO D N   1 
ATOM   4914 C  CA  . PRO D 2 42  ? -20.138 -5.908  -70.496  1.00 47.28  ? 42  PRO D CA  1 
ATOM   4915 C  C   . PRO D 2 42  ? -21.430 -6.689  -70.376  1.00 52.63  ? 42  PRO D C   1 
ATOM   4916 O  O   . PRO D 2 42  ? -22.339 -6.553  -71.200  1.00 52.73  ? 42  PRO D O   1 
ATOM   4917 C  CB  . PRO D 2 42  ? -20.354 -4.442  -70.118  1.00 50.21  ? 42  PRO D CB  1 
ATOM   4918 C  CG  . PRO D 2 42  ? -20.473 -3.721  -71.409  1.00 54.34  ? 42  PRO D CG  1 
ATOM   4919 C  CD  . PRO D 2 42  ? -19.916 -4.545  -72.520  1.00 39.96  ? 42  PRO D CD  1 
ATOM   4920 N  N   . ASN D 2 43  ? -21.498 -7.503  -69.325  1.00 59.73  ? 43  ASN D N   1 
ATOM   4921 C  CA  . ASN D 2 43  ? -22.660 -8.329  -69.014  1.00 60.48  ? 43  ASN D CA  1 
ATOM   4922 C  C   . ASN D 2 43  ? -23.117 -9.118  -70.241  1.00 65.44  ? 43  ASN D C   1 
ATOM   4923 O  O   . ASN D 2 43  ? -24.277 -9.074  -70.655  1.00 73.11  ? 43  ASN D O   1 
ATOM   4924 C  CB  . ASN D 2 43  ? -23.795 -7.475  -68.442  1.00 65.80  ? 43  ASN D CB  1 
ATOM   4925 C  CG  . ASN D 2 43  ? -23.366 -6.675  -67.215  1.00 75.91  ? 43  ASN D CG  1 
ATOM   4926 O  OD1 . ASN D 2 43  ? -22.291 -6.062  -67.189  1.00 68.35  ? 43  ASN D OD1 1 
ATOM   4927 N  ND2 . ASN D 2 43  ? -24.203 -6.693  -66.183  1.00 83.67  ? 43  ASN D ND2 1 
ATOM   4928 N  N   . SER D 2 44  ? -22.172 -9.843  -70.827  1.00 53.01  ? 44  SER D N   1 
ATOM   4929 C  CA  . SER D 2 44  ? -22.453 -10.625 -72.018  1.00 63.70  ? 44  SER D CA  1 
ATOM   4930 C  C   . SER D 2 44  ? -22.635 -12.101 -71.670  1.00 65.95  ? 44  SER D C   1 
ATOM   4931 O  O   . SER D 2 44  ? -22.017 -12.624 -70.739  1.00 63.57  ? 44  SER D O   1 
ATOM   4932 C  CB  . SER D 2 44  ? -21.334 -10.456 -73.049  1.00 63.21  ? 44  SER D CB  1 
ATOM   4933 O  OG  . SER D 2 44  ? -21.471 -11.380 -74.120  1.00 56.53  ? 44  SER D OG  1 
ATOM   4934 N  N   . ASP D 2 45  ? -23.515 -12.761 -72.424  1.00 73.80  ? 45  ASP D N   1 
ATOM   4935 C  CA  . ASP D 2 45  ? -23.696 -14.208 -72.361  1.00 79.73  ? 45  ASP D CA  1 
ATOM   4936 C  C   . ASP D 2 45  ? -22.680 -14.961 -73.212  1.00 72.96  ? 45  ASP D C   1 
ATOM   4937 O  O   . ASP D 2 45  ? -22.689 -16.200 -73.222  1.00 66.75  ? 45  ASP D O   1 
ATOM   4938 C  CB  . ASP D 2 45  ? -25.119 -14.579 -72.809  1.00 80.90  ? 45  ASP D CB  1 
ATOM   4939 C  CG  . ASP D 2 45  ? -26.139 -14.489 -71.680  1.00 90.20  ? 45  ASP D CG  1 
ATOM   4940 O  OD1 . ASP D 2 45  ? -26.881 -15.472 -71.458  1.00 92.60  ? 45  ASP D OD1 1 
ATOM   4941 O  OD2 . ASP D 2 45  ? -26.192 -13.437 -71.006  1.00 92.14  ? 45  ASP D OD2 1 
ATOM   4942 N  N   . ALA D 2 46  ? -21.815 -14.249 -73.927  1.00 72.10  ? 46  ALA D N   1 
ATOM   4943 C  CA  . ALA D 2 46  ? -20.875 -14.916 -74.811  1.00 61.69  ? 46  ALA D CA  1 
ATOM   4944 C  C   . ALA D 2 46  ? -19.805 -15.625 -73.990  1.00 60.40  ? 46  ALA D C   1 
ATOM   4945 O  O   . ALA D 2 46  ? -19.343 -15.093 -72.972  1.00 55.73  ? 46  ALA D O   1 
ATOM   4946 C  CB  . ALA D 2 46  ? -20.217 -13.925 -75.770  1.00 54.03  ? 46  ALA D CB  1 
ATOM   4947 N  N   . PRO D 2 47  ? -19.410 -16.832 -74.394  1.00 56.53  ? 47  PRO D N   1 
ATOM   4948 C  CA  . PRO D 2 47  ? -18.258 -17.466 -73.741  1.00 50.43  ? 47  PRO D CA  1 
ATOM   4949 C  C   . PRO D 2 47  ? -16.974 -16.709 -73.986  1.00 59.67  ? 47  PRO D C   1 
ATOM   4950 O  O   . PRO D 2 47  ? -16.146 -16.575 -73.075  1.00 72.55  ? 47  PRO D O   1 
ATOM   4951 C  CB  . PRO D 2 47  ? -18.231 -18.862 -74.377  1.00 45.53  ? 47  PRO D CB  1 
ATOM   4952 C  CG  . PRO D 2 47  ? -18.844 -18.670 -75.707  1.00 52.24  ? 47  PRO D CG  1 
ATOM   4953 C  CD  . PRO D 2 47  ? -19.944 -17.652 -75.493  1.00 49.05  ? 47  PRO D CD  1 
ATOM   4954 N  N   . CYS D 2 48  ? -16.815 -16.170 -75.184  1.00 52.96  ? 48  CYS D N   1 
ATOM   4955 C  CA  . CYS D 2 48  ? -15.608 -15.550 -75.685  1.00 39.84  ? 48  CYS D CA  1 
ATOM   4956 C  C   . CYS D 2 48  ? -15.735 -14.030 -75.744  1.00 35.03  ? 48  CYS D C   1 
ATOM   4957 O  O   . CYS D 2 48  ? -16.841 -13.484 -75.674  1.00 38.28  ? 48  CYS D O   1 
ATOM   4958 C  CB  . CYS D 2 48  ? -15.331 -16.115 -77.079  1.00 40.73  ? 48  CYS D CB  1 
ATOM   4959 S  SG  . CYS D 2 48  ? -15.342 -17.916 -77.095  1.00 56.77  ? 48  CYS D SG  1 
ATOM   4960 N  N   . PRO D 2 49  ? -14.618 -13.315 -75.848  1.00 30.24  ? 49  PRO D N   1 
ATOM   4961 C  CA  . PRO D 2 49  ? -14.683 -11.878 -76.148  1.00 27.44  ? 49  PRO D CA  1 
ATOM   4962 C  C   . PRO D 2 49  ? -15.500 -11.630 -77.409  1.00 27.59  ? 49  PRO D C   1 
ATOM   4963 O  O   . PRO D 2 49  ? -15.274 -12.250 -78.446  1.00 25.74  ? 49  PRO D O   1 
ATOM   4964 C  CB  . PRO D 2 49  ? -13.216 -11.496 -76.354  1.00 30.31  ? 49  PRO D CB  1 
ATOM   4965 C  CG  . PRO D 2 49  ? -12.460 -12.525 -75.566  1.00 33.45  ? 49  PRO D CG  1 
ATOM   4966 C  CD  . PRO D 2 49  ? -13.229 -13.792 -75.705  1.00 29.72  ? 49  PRO D CD  1 
ATOM   4967 N  N   . ASP D 2 50  ? -16.468 -10.716 -77.314  1.00 29.38  ? 50  ASP D N   1 
ATOM   4968 C  CA  . ASP D 2 50  ? -17.402 -10.468 -78.407  1.00 27.64  ? 50  ASP D CA  1 
ATOM   4969 C  C   . ASP D 2 50  ? -17.593 -8.974  -78.685  1.00 25.18  ? 50  ASP D C   1 
ATOM   4970 O  O   . ASP D 2 50  ? -18.528 -8.600  -79.393  1.00 26.29  ? 50  ASP D O   1 
ATOM   4971 C  CB  . ASP D 2 50  ? -18.756 -11.133 -78.122  1.00 26.90  ? 50  ASP D CB  1 
ATOM   4972 C  CG  . ASP D 2 50  ? -19.449 -10.580 -76.875  1.00 36.33  ? 50  ASP D CG  1 
ATOM   4973 O  OD1 . ASP D 2 50  ? -18.759 -10.149 -75.926  1.00 39.38  ? 50  ASP D OD1 1 
ATOM   4974 O  OD2 . ASP D 2 50  ? -20.701 -10.578 -76.847  1.00 44.14  ? 50  ASP D OD2 1 
ATOM   4975 N  N   . GLY D 2 51  ? -16.729 -8.114  -78.156  1.00 22.26  ? 51  GLY D N   1 
ATOM   4976 C  CA  . GLY D 2 51  ? -16.833 -6.671  -78.350  1.00 26.02  ? 51  GLY D CA  1 
ATOM   4977 C  C   . GLY D 2 51  ? -15.734 -6.145  -79.259  1.00 23.56  ? 51  GLY D C   1 
ATOM   4978 O  O   . GLY D 2 51  ? -14.584 -6.592  -79.183  1.00 25.51  ? 51  GLY D O   1 
ATOM   4979 N  N   . VAL D 2 52  ? -16.097 -5.202  -80.125  1.00 27.68  ? 52  VAL D N   1 
ATOM   4980 C  CA  . VAL D 2 52  ? -15.146 -4.491  -80.977  1.00 24.87  ? 52  VAL D CA  1 
ATOM   4981 C  C   . VAL D 2 52  ? -14.985 -3.086  -80.404  1.00 26.25  ? 52  VAL D C   1 
ATOM   4982 O  O   . VAL D 2 52  ? -15.911 -2.265  -80.474  1.00 21.74  ? 52  VAL D O   1 
ATOM   4983 C  CB  . VAL D 2 52  ? -15.608 -4.457  -82.437  1.00 27.15  ? 52  VAL D CB  1 
ATOM   4984 C  CG1 . VAL D 2 52  ? -14.635 -3.647  -83.272  1.00 22.70  ? 52  VAL D CG1 1 
ATOM   4985 C  CG2 . VAL D 2 52  ? -15.731 -5.879  -82.973  1.00 22.49  ? 52  VAL D CG2 1 
ATOM   4986 N  N   . PHE D 2 53  ? -13.824 -2.817  -79.810  1.00 19.26  ? 53  PHE D N   1 
ATOM   4987 C  CA  . PHE D 2 53  ? -13.570 -1.572  -79.102  1.00 19.64  ? 53  PHE D CA  1 
ATOM   4988 C  C   . PHE D 2 53  ? -12.409 -0.844  -79.745  1.00 23.86  ? 53  PHE D C   1 
ATOM   4989 O  O   . PHE D 2 53  ? -11.734 -1.365  -80.633  1.00 27.00  ? 53  PHE D O   1 
ATOM   4990 C  CB  . PHE D 2 53  ? -13.206 -1.801  -77.637  1.00 21.41  ? 53  PHE D CB  1 
ATOM   4991 C  CG  . PHE D 2 53  ? -14.270 -2.451  -76.826  1.00 25.44  ? 53  PHE D CG  1 
ATOM   4992 C  CD1 . PHE D 2 53  ? -14.376 -3.825  -76.786  1.00 28.75  ? 53  PHE D CD1 1 
ATOM   4993 C  CD2 . PHE D 2 53  ? -15.124 -1.694  -76.048  1.00 24.26  ? 53  PHE D CD2 1 
ATOM   4994 C  CE1 . PHE D 2 53  ? -15.342 -4.436  -76.006  1.00 30.28  ? 53  PHE D CE1 1 
ATOM   4995 C  CE2 . PHE D 2 53  ? -16.091 -2.298  -75.276  1.00 29.75  ? 53  PHE D CE2 1 
ATOM   4996 C  CZ  . PHE D 2 53  ? -16.192 -3.676  -75.249  1.00 19.59  ? 53  PHE D CZ  1 
ATOM   4997 N  N   . ARG D 2 54  ? -12.153 0.358   -79.240  1.00 23.38  ? 54  ARG D N   1 
ATOM   4998 C  CA  . ARG D 2 54  ? -10.897 1.040   -79.489  1.00 19.01  ? 54  ARG D CA  1 
ATOM   4999 C  C   . ARG D 2 54  ? -10.334 1.545   -78.166  1.00 24.99  ? 54  ARG D C   1 
ATOM   5000 O  O   . ARG D 2 54  ? -11.079 1.837   -77.225  1.00 20.50  ? 54  ARG D O   1 
ATOM   5001 C  CB  . ARG D 2 54  ? -11.085 2.142   -80.544  1.00 17.61  ? 54  ARG D CB  1 
ATOM   5002 C  CG  . ARG D 2 54  ? -11.148 3.578   -80.119  1.00 21.61  ? 54  ARG D CG  1 
ATOM   5003 C  CD  . ARG D 2 54  ? -11.190 4.430   -81.407  1.00 19.56  ? 54  ARG D CD  1 
ATOM   5004 N  NE  . ARG D 2 54  ? -11.195 5.863   -81.159  1.00 20.76  ? 54  ARG D NE  1 
ATOM   5005 C  CZ  . ARG D 2 54  ? -10.110 6.629   -81.155  1.00 27.27  ? 54  ARG D CZ  1 
ATOM   5006 N  NH1 . ARG D 2 54  ? -8.906  6.133   -81.404  1.00 29.78  ? 54  ARG D NH1 1 
ATOM   5007 N  NH2 . ARG D 2 54  ? -10.230 7.921   -80.869  1.00 19.26  ? 54  ARG D NH2 1 
ATOM   5008 N  N   . TYR D 2 55  ? -9.002  1.576   -78.078  1.00 25.96  ? 55  TYR D N   1 
ATOM   5009 C  CA  . TYR D 2 55  ? -8.348  1.937   -76.825  1.00 24.52  ? 55  TYR D CA  1 
ATOM   5010 C  C   . TYR D 2 55  ? -8.589  3.412   -76.519  1.00 22.05  ? 55  TYR D C   1 
ATOM   5011 O  O   . TYR D 2 55  ? -8.953  4.202   -77.397  1.00 19.35  ? 55  TYR D O   1 
ATOM   5012 C  CB  . TYR D 2 55  ? -6.849  1.629   -76.890  1.00 21.83  ? 55  TYR D CB  1 
ATOM   5013 C  CG  . TYR D 2 55  ? -6.567  0.161   -76.792  1.00 19.49  ? 55  TYR D CG  1 
ATOM   5014 C  CD1 . TYR D 2 55  ? -6.841  -0.533  -75.629  1.00 17.38  ? 55  TYR D CD1 1 
ATOM   5015 C  CD2 . TYR D 2 55  ? -6.073  -0.549  -77.886  1.00 26.76  ? 55  TYR D CD2 1 
ATOM   5016 C  CE1 . TYR D 2 55  ? -6.623  -1.897  -75.536  1.00 21.02  ? 55  TYR D CE1 1 
ATOM   5017 C  CE2 . TYR D 2 55  ? -5.821  -1.918  -77.803  1.00 23.24  ? 55  TYR D CE2 1 
ATOM   5018 C  CZ  . TYR D 2 55  ? -6.109  -2.588  -76.623  1.00 26.33  ? 55  TYR D CZ  1 
ATOM   5019 O  OH  . TYR D 2 55  ? -5.887  -3.947  -76.522  1.00 30.83  ? 55  TYR D OH  1 
ATOM   5020 N  N   . ASN D 2 56  ? -8.412  3.766   -75.242  1.00 20.25  ? 56  ASN D N   1 
ATOM   5021 C  CA  . ASN D 2 56  ? -8.655  5.128   -74.776  1.00 26.72  ? 56  ASN D CA  1 
ATOM   5022 C  C   . ASN D 2 56  ? -7.519  6.082   -75.112  1.00 27.62  ? 56  ASN D C   1 
ATOM   5023 O  O   . ASN D 2 56  ? -7.694  7.301   -74.983  1.00 20.15  ? 56  ASN D O   1 
ATOM   5024 C  CB  . ASN D 2 56  ? -8.884  5.153   -73.262  1.00 22.25  ? 56  ASN D CB  1 
ATOM   5025 C  CG  . ASN D 2 56  ? -10.221 4.555   -72.851  1.00 30.01  ? 56  ASN D CG  1 
ATOM   5026 O  OD1 . ASN D 2 56  ? -11.224 4.626   -73.567  1.00 27.83  ? 56  ASN D OD1 1 
ATOM   5027 N  ND2 . ASN D 2 56  ? -10.236 3.964   -71.681  1.00 33.70  ? 56  ASN D ND2 1 
ATOM   5028 N  N   . SER D 2 57  ? -6.357  5.554   -75.489  1.00 25.95  ? 57  SER D N   1 
ATOM   5029 C  CA  . SER D 2 57  ? -5.271  6.353   -76.043  1.00 24.10  ? 57  SER D CA  1 
ATOM   5030 C  C   . SER D 2 57  ? -4.386  5.412   -76.844  1.00 22.80  ? 57  SER D C   1 
ATOM   5031 O  O   . SER D 2 57  ? -4.627  4.204   -76.904  1.00 22.08  ? 57  SER D O   1 
ATOM   5032 C  CB  . SER D 2 57  ? -4.509  7.098   -74.943  1.00 22.82  ? 57  SER D CB  1 
ATOM   5033 O  OG  . SER D 2 57  ? -3.658  6.218   -74.238  1.00 25.52  ? 57  SER D OG  1 
ATOM   5034 N  N   . ASP D 2 58  ? -3.377  5.970   -77.494  1.00 25.35  ? 58  ASP D N   1 
ATOM   5035 C  CA  . ASP D 2 58  ? -2.480  5.146   -78.292  1.00 30.11  ? 58  ASP D CA  1 
ATOM   5036 C  C   . ASP D 2 58  ? -1.165  4.857   -77.586  1.00 22.76  ? 58  ASP D C   1 
ATOM   5037 O  O   . ASP D 2 58  ? -0.226  4.390   -78.228  1.00 26.57  ? 58  ASP D O   1 
ATOM   5038 C  CB  . ASP D 2 58  ? -2.218  5.810   -79.645  1.00 25.78  ? 58  ASP D CB  1 
ATOM   5039 C  CG  . ASP D 2 58  ? -1.603  7.194   -79.509  1.00 27.74  ? 58  ASP D CG  1 
ATOM   5040 O  OD1 . ASP D 2 58  ? -0.861  7.440   -78.543  1.00 27.88  ? 58  ASP D OD1 1 
ATOM   5041 O  OD2 . ASP D 2 58  ? -1.891  8.058   -80.359  1.00 37.47  ? 58  ASP D OD2 1 
ATOM   5042 N  N   . VAL D 2 59  ? -1.060  5.145   -76.287  1.00 21.90  ? 59  VAL D N   1 
ATOM   5043 C  CA  . VAL D 2 59  ? 0.203   4.931   -75.589  1.00 33.44  ? 59  VAL D CA  1 
ATOM   5044 C  C   . VAL D 2 59  ? 0.226   3.634   -74.808  1.00 29.57  ? 59  VAL D C   1 
ATOM   5045 O  O   . VAL D 2 59  ? 1.251   3.322   -74.192  1.00 36.67  ? 59  VAL D O   1 
ATOM   5046 C  CB  . VAL D 2 59  ? 0.572   6.117   -74.665  1.00 25.64  ? 59  VAL D CB  1 
ATOM   5047 C  CG1 . VAL D 2 59  ? 0.769   7.381   -75.472  1.00 22.75  ? 59  VAL D CG1 1 
ATOM   5048 C  CG2 . VAL D 2 59  ? -0.492  6.322   -73.584  1.00 22.47  ? 59  VAL D CG2 1 
ATOM   5049 N  N   . GLY D 2 60  ? -0.861  2.867   -74.815  1.00 25.31  ? 60  GLY D N   1 
ATOM   5050 C  CA  . GLY D 2 60  ? -0.886  1.579   -74.158  1.00 30.30  ? 60  GLY D CA  1 
ATOM   5051 C  C   . GLY D 2 60  ? -0.701  0.422   -75.124  1.00 31.40  ? 60  GLY D C   1 
ATOM   5052 O  O   . GLY D 2 60  ? 0.278   0.357   -75.871  1.00 43.68  ? 60  GLY D O   1 
ATOM   5053 N  N   . PRO D 2 61  ? -1.645  -0.515  -75.134  1.00 37.33  ? 61  PRO D N   1 
ATOM   5054 C  CA  . PRO D 2 61  ? -1.548  -1.659  -76.049  1.00 25.59  ? 61  PRO D CA  1 
ATOM   5055 C  C   . PRO D 2 61  ? -1.889  -1.286  -77.489  1.00 29.39  ? 61  PRO D C   1 
ATOM   5056 O  O   . PRO D 2 61  ? -2.621  -0.332  -77.778  1.00 22.94  ? 61  PRO D O   1 
ATOM   5057 C  CB  . PRO D 2 61  ? -2.578  -2.656  -75.493  1.00 18.69  ? 61  PRO D CB  1 
ATOM   5058 C  CG  . PRO D 2 61  ? -3.022  -2.092  -74.178  1.00 35.26  ? 61  PRO D CG  1 
ATOM   5059 C  CD  . PRO D 2 61  ? -2.823  -0.611  -74.265  1.00 28.29  ? 61  PRO D CD  1 
ATOM   5060 N  N   . SER D 2 62  ? -1.385  -2.103  -78.400  1.00 22.02  ? 62  SER D N   1 
ATOM   5061 C  CA  . SER D 2 62  ? -1.686  -1.948  -79.810  1.00 34.63  ? 62  SER D CA  1 
ATOM   5062 C  C   . SER D 2 62  ? -2.935  -2.738  -80.189  1.00 26.24  ? 62  SER D C   1 
ATOM   5063 O  O   . SER D 2 62  ? -3.467  -3.527  -79.406  1.00 28.47  ? 62  SER D O   1 
ATOM   5064 C  CB  . SER D 2 62  ? -0.486  -2.375  -80.636  1.00 29.52  ? 62  SER D CB  1 
ATOM   5065 O  OG  . SER D 2 62  ? 0.362   -1.253  -80.747  1.00 33.90  ? 62  SER D OG  1 
ATOM   5066 N  N   . GLY D 2 63  ? -3.424  -2.493  -81.387  1.00 25.08  ? 63  GLY D N   1 
ATOM   5067 C  CA  . GLY D 2 63  ? -4.718  -3.022  -81.749  1.00 30.72  ? 63  GLY D CA  1 
ATOM   5068 C  C   . GLY D 2 63  ? -4.671  -4.491  -82.062  1.00 26.19  ? 63  GLY D C   1 
ATOM   5069 O  O   . GLY D 2 63  ? -3.612  -5.076  -82.261  1.00 31.59  ? 63  GLY D O   1 
ATOM   5070 N  N   . THR D 2 64  ? -5.846  -5.103  -82.100  1.00 28.71  ? 64  THR D N   1 
ATOM   5071 C  CA  . THR D 2 64  ? -5.949  -6.495  -82.535  1.00 26.89  ? 64  THR D CA  1 
ATOM   5072 C  C   . THR D 2 64  ? -5.906  -6.532  -84.060  1.00 28.22  ? 64  THR D C   1 
ATOM   5073 O  O   . THR D 2 64  ? -6.698  -5.834  -84.706  1.00 31.06  ? 64  THR D O   1 
ATOM   5074 C  CB  . THR D 2 64  ? -7.244  -7.130  -82.028  1.00 28.10  ? 64  THR D CB  1 
ATOM   5075 O  OG1 . THR D 2 64  ? -7.413  -6.849  -80.634  1.00 30.25  ? 64  THR D OG1 1 
ATOM   5076 C  CG2 . THR D 2 64  ? -7.224  -8.624  -82.232  1.00 23.63  ? 64  THR D CG2 1 
ATOM   5077 N  N   . PRO D 2 65  ? -4.995  -7.289  -84.668  1.00 31.07  ? 65  PRO D N   1 
ATOM   5078 C  CA  . PRO D 2 65  ? -4.907  -7.303  -86.136  1.00 29.77  ? 65  PRO D CA  1 
ATOM   5079 C  C   . PRO D 2 65  ? -6.153  -7.891  -86.785  1.00 26.69  ? 65  PRO D C   1 
ATOM   5080 O  O   . PRO D 2 65  ? -6.739  -8.860  -86.294  1.00 29.93  ? 65  PRO D O   1 
ATOM   5081 C  CB  . PRO D 2 65  ? -3.681  -8.184  -86.398  1.00 28.88  ? 65  PRO D CB  1 
ATOM   5082 C  CG  . PRO D 2 65  ? -2.869  -8.073  -85.139  1.00 24.03  ? 65  PRO D CG  1 
ATOM   5083 C  CD  . PRO D 2 65  ? -3.910  -8.083  -84.059  1.00 29.02  ? 65  PRO D CD  1 
ATOM   5084 N  N   . VAL D 2 66  ? -6.530  -7.322  -87.930  1.00 31.14  ? 66  VAL D N   1 
ATOM   5085 C  CA  . VAL D 2 66  ? -7.645  -7.827  -88.716  1.00 26.32  ? 66  VAL D CA  1 
ATOM   5086 C  C   . VAL D 2 66  ? -7.163  -8.235  -90.098  1.00 29.42  ? 66  VAL D C   1 
ATOM   5087 O  O   . VAL D 2 66  ? -6.129  -7.780  -90.596  1.00 30.61  ? 66  VAL D O   1 
ATOM   5088 C  CB  . VAL D 2 66  ? -8.783  -6.794  -88.841  1.00 24.01  ? 66  VAL D CB  1 
ATOM   5089 C  CG1 . VAL D 2 66  ? -9.238  -6.330  -87.456  1.00 25.68  ? 66  VAL D CG1 1 
ATOM   5090 C  CG2 . VAL D 2 66  ? -8.332  -5.636  -89.666  1.00 15.85  ? 66  VAL D CG2 1 
ATOM   5091 N  N   . ARG D 2 67  ? -7.938  -9.109  -90.724  1.00 31.79  ? 67  ARG D N   1 
ATOM   5092 C  CA  . ARG D 2 67  ? -7.813  -9.363  -92.148  1.00 27.59  ? 67  ARG D CA  1 
ATOM   5093 C  C   . ARG D 2 67  ? -9.150  -9.085  -92.809  1.00 30.45  ? 67  ARG D C   1 
ATOM   5094 O  O   . ARG D 2 67  ? -10.213 -9.278  -92.212  1.00 25.00  ? 67  ARG D O   1 
ATOM   5095 C  CB  . ARG D 2 67  ? -7.394  -10.793 -92.447  1.00 30.77  ? 67  ARG D CB  1 
ATOM   5096 C  CG  . ARG D 2 67  ? -8.379  -11.818 -91.968  1.00 30.17  ? 67  ARG D CG  1 
ATOM   5097 C  CD  . ARG D 2 67  ? -8.202  -13.110 -92.709  1.00 34.83  ? 67  ARG D CD  1 
ATOM   5098 N  NE  . ARG D 2 67  ? -9.367  -13.964 -92.554  1.00 41.99  ? 67  ARG D NE  1 
ATOM   5099 C  CZ  . ARG D 2 67  ? -9.359  -15.278 -92.726  1.00 53.53  ? 67  ARG D CZ  1 
ATOM   5100 N  NH1 . ARG D 2 67  ? -8.262  -15.919 -93.105  1.00 47.76  ? 67  ARG D NH1 1 
ATOM   5101 N  NH2 . ARG D 2 67  ? -10.480 -15.965 -92.512  1.00 43.11  ? 67  ARG D NH2 1 
ATOM   5102 N  N   . PHE D 2 68  ? -9.080  -8.626  -94.049  1.00 26.08  ? 68  PHE D N   1 
ATOM   5103 C  CA  . PHE D 2 68  ? -10.250 -8.241  -94.815  1.00 31.95  ? 68  PHE D CA  1 
ATOM   5104 C  C   . PHE D 2 68  ? -10.521 -9.314  -95.857  1.00 33.38  ? 68  PHE D C   1 
ATOM   5105 O  O   . PHE D 2 68  ? -9.612  -9.711  -96.596  1.00 29.22  ? 68  PHE D O   1 
ATOM   5106 C  CB  . PHE D 2 68  ? -10.026 -6.869  -95.449  1.00 28.91  ? 68  PHE D CB  1 
ATOM   5107 C  CG  . PHE D 2 68  ? -9.732  -5.793  -94.437  1.00 29.19  ? 68  PHE D CG  1 
ATOM   5108 C  CD1 . PHE D 2 68  ? -10.763 -5.188  -93.729  1.00 27.04  ? 68  PHE D CD1 1 
ATOM   5109 C  CD2 . PHE D 2 68  ? -8.425  -5.422  -94.161  1.00 26.64  ? 68  PHE D CD2 1 
ATOM   5110 C  CE1 . PHE D 2 68  ? -10.500 -4.216  -92.801  1.00 21.86  ? 68  PHE D CE1 1 
ATOM   5111 C  CE2 . PHE D 2 68  ? -8.151  -4.450  -93.227  1.00 30.64  ? 68  PHE D CE2 1 
ATOM   5112 C  CZ  . PHE D 2 68  ? -9.189  -3.847  -92.543  1.00 31.16  ? 68  PHE D CZ  1 
ATOM   5113 N  N   . ILE D 2 69  ? -11.756 -9.808  -95.887  1.00 27.14  ? 69  ILE D N   1 
ATOM   5114 C  CA  . ILE D 2 69  ? -12.098 -10.916 -96.779  1.00 30.66  ? 69  ILE D CA  1 
ATOM   5115 C  C   . ILE D 2 69  ? -13.016 -10.452 -97.903  1.00 29.57  ? 69  ILE D C   1 
ATOM   5116 O  O   . ILE D 2 69  ? -14.228 -10.308 -97.694  1.00 26.50  ? 69  ILE D O   1 
ATOM   5117 C  CB  . ILE D 2 69  ? -12.734 -12.064 -95.997  1.00 30.48  ? 69  ILE D CB  1 
ATOM   5118 C  CG1 . ILE D 2 69  ? -11.785 -12.476 -94.871  1.00 34.23  ? 69  ILE D CG1 1 
ATOM   5119 C  CG2 . ILE D 2 69  ? -13.038 -13.219 -96.933  1.00 22.89  ? 69  ILE D CG2 1 
ATOM   5120 C  CD1 . ILE D 2 69  ? -12.473 -13.127 -93.732  1.00 39.16  ? 69  ILE D CD1 1 
ATOM   5121 N  N   . PRO D 2 70  ? -12.484 -10.209 -99.100  1.00 27.21  ? 70  PRO D N   1 
ATOM   5122 C  CA  . PRO D 2 70  ? -13.328 -9.723  -100.194 1.00 33.44  ? 70  PRO D CA  1 
ATOM   5123 C  C   . PRO D 2 70  ? -14.413 -10.732 -100.512 1.00 31.77  ? 70  PRO D C   1 
ATOM   5124 O  O   . PRO D 2 70  ? -14.202 -11.942 -100.431 1.00 32.50  ? 70  PRO D O   1 
ATOM   5125 C  CB  . PRO D 2 70  ? -12.347 -9.577  -101.364 1.00 34.44  ? 70  PRO D CB  1 
ATOM   5126 C  CG  . PRO D 2 70  ? -11.234 -10.527 -101.034 1.00 34.35  ? 70  PRO D CG  1 
ATOM   5127 C  CD  . PRO D 2 70  ? -11.103 -10.458 -99.536  1.00 26.35  ? 70  PRO D CD  1 
ATOM   5128 N  N   . LEU D 2 71  ? -15.580 -10.216 -100.876 1.00 30.70  ? 71  LEU D N   1 
ATOM   5129 C  CA  . LEU D 2 71  ? -16.695 -11.075 -101.250 1.00 38.98  ? 71  LEU D CA  1 
ATOM   5130 C  C   . LEU D 2 71  ? -16.461 -11.749 -102.599 1.00 48.30  ? 71  LEU D C   1 
ATOM   5131 O  O   . LEU D 2 71  ? -16.901 -12.885 -102.805 1.00 50.22  ? 71  LEU D O   1 
ATOM   5132 C  CB  . LEU D 2 71  ? -17.973 -10.244 -101.271 1.00 40.30  ? 71  LEU D CB  1 
ATOM   5133 C  CG  . LEU D 2 71  ? -19.218 -10.760 -101.963 1.00 46.21  ? 71  LEU D CG  1 
ATOM   5134 C  CD1 . LEU D 2 71  ? -20.261 -11.092 -100.907 1.00 40.54  ? 71  LEU D CD1 1 
ATOM   5135 C  CD2 . LEU D 2 71  ? -19.737 -9.710  -102.934 1.00 37.98  ? 71  LEU D CD2 1 
ATOM   5136 N  N   . SER D 2 72  ? -15.767 -11.080 -103.520 1.00 45.79  ? 72  SER D N   1 
ATOM   5137 C  CA  . SER D 2 72  ? -15.459 -11.648 -104.826 1.00 56.79  ? 72  SER D CA  1 
ATOM   5138 C  C   . SER D 2 72  ? -14.031 -11.300 -105.197 1.00 50.76  ? 72  SER D C   1 
ATOM   5139 O  O   . SER D 2 72  ? -13.502 -10.265 -104.788 1.00 55.82  ? 72  SER D O   1 
ATOM   5140 C  CB  . SER D 2 72  ? -16.401 -11.134 -105.931 1.00 53.58  ? 72  SER D CB  1 
ATOM   5141 O  OG  . SER D 2 72  ? -17.574 -11.929 -106.027 1.00 59.48  ? 72  SER D OG  1 
ATOM   5142 N  N   . GLY D 2 73  ? -13.413 -12.165 -105.985 1.00 49.36  ? 73  GLY D N   1 
ATOM   5143 C  CA  . GLY D 2 73  ? -12.061 -11.897 -106.435 1.00 51.01  ? 73  GLY D CA  1 
ATOM   5144 C  C   . GLY D 2 73  ? -11.073 -11.832 -105.291 1.00 45.66  ? 73  GLY D C   1 
ATOM   5145 O  O   . GLY D 2 73  ? -11.456 -12.009 -104.135 1.00 46.32  ? 73  GLY D O   1 
ATOM   5146 N  N   . ALA D 2 74  ? -9.801  -11.570 -105.585 1.00 47.81  ? 74  ALA D N   1 
ATOM   5147 C  CA  . ALA D 2 74  ? -8.762  -11.665 -104.572 1.00 46.37  ? 74  ALA D CA  1 
ATOM   5148 C  C   . ALA D 2 74  ? -8.182  -10.313 -104.184 1.00 51.84  ? 74  ALA D C   1 
ATOM   5149 O  O   . ALA D 2 74  ? -7.079  -10.260 -103.636 1.00 64.13  ? 74  ALA D O   1 
ATOM   5150 C  CB  . ALA D 2 74  ? -7.648  -12.594 -105.051 1.00 57.27  ? 74  ALA D CB  1 
ATOM   5151 N  N   . ASN D 2 75  ? -8.893  -9.218  -104.439 1.00 53.40  ? 75  ASN D N   1 
ATOM   5152 C  CA  . ASN D 2 75  ? -8.345  -7.893  -104.194 1.00 59.67  ? 75  ASN D CA  1 
ATOM   5153 C  C   . ASN D 2 75  ? -9.321  -7.069  -103.371 1.00 54.40  ? 75  ASN D C   1 
ATOM   5154 O  O   . ASN D 2 75  ? -10.539 -7.200  -103.515 1.00 51.70  ? 75  ASN D O   1 
ATOM   5155 C  CB  . ASN D 2 75  ? -8.040  -7.156  -105.506 1.00 64.91  ? 75  ASN D CB  1 
ATOM   5156 C  CG  . ASN D 2 75  ? -6.886  -7.780  -106.284 1.00 73.43  ? 75  ASN D CG  1 
ATOM   5157 O  OD1 . ASN D 2 75  ? -6.846  -8.995  -106.521 1.00 78.02  ? 75  ASN D OD1 1 
ATOM   5158 N  ND2 . ASN D 2 75  ? -5.947  -6.946  -106.695 1.00 72.84  ? 75  ASN D ND2 1 
ATOM   5159 N  N   . ILE D 2 76  ? -8.760  -6.189  -102.540 1.00 47.17  ? 76  ILE D N   1 
ATOM   5160 C  CA  . ILE D 2 76  ? -9.510  -5.312  -101.644 1.00 37.96  ? 76  ILE D CA  1 
ATOM   5161 C  C   . ILE D 2 76  ? -9.578  -3.907  -102.242 1.00 38.22  ? 76  ILE D C   1 
ATOM   5162 O  O   . ILE D 2 76  ? -8.556  -3.210  -102.336 1.00 38.56  ? 76  ILE D O   1 
ATOM   5163 C  CB  . ILE D 2 76  ? -8.855  -5.267  -100.259 1.00 36.89  ? 76  ILE D CB  1 
ATOM   5164 C  CG1 . ILE D 2 76  ? -8.791  -6.672  -99.663  1.00 41.82  ? 76  ILE D CG1 1 
ATOM   5165 C  CG2 . ILE D 2 76  ? -9.610  -4.293  -99.365  1.00 30.92  ? 76  ILE D CG2 1 
ATOM   5166 C  CD1 . ILE D 2 76  ? -7.964  -6.744  -98.395  1.00 34.82  ? 76  ILE D CD1 1 
ATOM   5167 N  N   . PHE D 2 77  ? -10.788 -3.462  -102.578 1.00 38.05  ? 77  PHE D N   1 
ATOM   5168 C  CA  . PHE D 2 77  ? -11.015 -2.171  -103.220 1.00 41.90  ? 77  PHE D CA  1 
ATOM   5169 C  C   . PHE D 2 77  ? -11.919 -1.283  -102.372 1.00 36.95  ? 77  PHE D C   1 
ATOM   5170 O  O   . PHE D 2 77  ? -12.814 -1.766  -101.679 1.00 42.71  ? 77  PHE D O   1 
ATOM   5171 C  CB  . PHE D 2 77  ? -11.668 -2.358  -104.600 1.00 37.74  ? 77  PHE D CB  1 
ATOM   5172 C  CG  . PHE D 2 77  ? -10.766 -2.989  -105.616 1.00 49.74  ? 77  PHE D CG  1 
ATOM   5173 C  CD1 . PHE D 2 77  ? -9.712  -2.275  -106.166 1.00 50.65  ? 77  PHE D CD1 1 
ATOM   5174 C  CD2 . PHE D 2 77  ? -10.965 -4.302  -106.019 1.00 51.51  ? 77  PHE D CD2 1 
ATOM   5175 C  CE1 . PHE D 2 77  ? -8.876  -2.862  -107.103 1.00 46.91  ? 77  PHE D CE1 1 
ATOM   5176 C  CE2 . PHE D 2 77  ? -10.139 -4.886  -106.951 1.00 44.46  ? 77  PHE D CE2 1 
ATOM   5177 C  CZ  . PHE D 2 77  ? -9.095  -4.168  -107.492 1.00 38.03  ? 77  PHE D CZ  1 
ATOM   5178 N  N   . GLU D 2 78  ? -11.712 0.028   -102.462 1.00 31.20  ? 78  GLU D N   1 
ATOM   5179 C  CA  . GLU D 2 78  ? -12.669 0.963   -101.881 1.00 28.90  ? 78  GLU D CA  1 
ATOM   5180 C  C   . GLU D 2 78  ? -14.086 0.649   -102.335 1.00 33.40  ? 78  GLU D C   1 
ATOM   5181 O  O   . GLU D 2 78  ? -14.320 0.261   -103.481 1.00 33.28  ? 78  GLU D O   1 
ATOM   5182 C  CB  . GLU D 2 78  ? -12.340 2.395   -102.282 1.00 39.86  ? 78  GLU D CB  1 
ATOM   5183 C  CG  . GLU D 2 78  ? -11.262 3.044   -101.478 1.00 38.66  ? 78  GLU D CG  1 
ATOM   5184 C  CD  . GLU D 2 78  ? -10.931 4.416   -102.005 1.00 42.78  ? 78  GLU D CD  1 
ATOM   5185 O  OE1 . GLU D 2 78  ? -11.859 5.104   -102.496 1.00 36.84  ? 78  GLU D OE1 1 
ATOM   5186 O  OE2 . GLU D 2 78  ? -9.737  4.789   -101.950 1.00 45.98  ? 78  GLU D OE2 1 
ATOM   5187 N  N   . ASP D 2 79  ? -15.032 0.820   -101.418 1.00 37.78  ? 79  ASP D N   1 
ATOM   5188 C  CA  . ASP D 2 79  ? -16.460 0.699   -101.683 1.00 34.91  ? 79  ASP D CA  1 
ATOM   5189 C  C   . ASP D 2 79  ? -16.860 -0.700  -102.157 1.00 36.18  ? 79  ASP D C   1 
ATOM   5190 O  O   . ASP D 2 79  ? -17.894 -0.870  -102.801 1.00 30.20  ? 79  ASP D O   1 
ATOM   5191 C  CB  . ASP D 2 79  ? -16.918 1.753   -102.694 1.00 27.24  ? 79  ASP D CB  1 
ATOM   5192 C  CG  . ASP D 2 79  ? -18.429 1.931   -102.700 1.00 47.52  ? 79  ASP D CG  1 
ATOM   5193 O  OD1 . ASP D 2 79  ? -19.079 1.563   -103.704 1.00 59.51  ? 79  ASP D OD1 1 
ATOM   5194 O  OD2 . ASP D 2 79  ? -18.976 2.428   -101.696 1.00 53.62  ? 79  ASP D OD2 1 
ATOM   5195 N  N   . GLN D 2 80  ? -16.082 -1.728  -101.854 1.00 33.14  ? 80  GLN D N   1 
ATOM   5196 C  CA  . GLN D 2 80  ? -16.457 -3.081  -102.231 1.00 31.12  ? 80  GLN D CA  1 
ATOM   5197 C  C   . GLN D 2 80  ? -16.739 -3.905  -100.976 1.00 38.45  ? 80  GLN D C   1 
ATOM   5198 O  O   . GLN D 2 80  ? -16.152 -3.681  -99.909  1.00 36.05  ? 80  GLN D O   1 
ATOM   5199 C  CB  . GLN D 2 80  ? -15.368 -3.727  -103.094 1.00 29.31  ? 80  GLN D CB  1 
ATOM   5200 C  CG  . GLN D 2 80  ? -14.493 -4.731  -102.388 1.00 43.42  ? 80  GLN D CG  1 
ATOM   5201 C  CD  . GLN D 2 80  ? -13.474 -5.370  -103.315 1.00 55.88  ? 80  GLN D CD  1 
ATOM   5202 O  OE1 . GLN D 2 80  ? -13.607 -5.310  -104.538 1.00 68.38  ? 80  GLN D OE1 1 
ATOM   5203 N  NE2 . GLN D 2 80  ? -12.454 -5.995  -102.736 1.00 50.35  ? 80  GLN D NE2 1 
ATOM   5204 N  N   . LEU D 2 81  ? -17.673 -4.840  -101.116 1.00 37.05  ? 81  LEU D N   1 
ATOM   5205 C  CA  . LEU D 2 81  ? -18.172 -5.614  -99.992  1.00 35.38  ? 81  LEU D CA  1 
ATOM   5206 C  C   . LEU D 2 81  ? -17.104 -6.572  -99.480  1.00 36.05  ? 81  LEU D C   1 
ATOM   5207 O  O   . LEU D 2 81  ? -16.437 -7.261  -100.263 1.00 30.77  ? 81  LEU D O   1 
ATOM   5208 C  CB  . LEU D 2 81  ? -19.393 -6.412  -100.432 1.00 29.13  ? 81  LEU D CB  1 
ATOM   5209 C  CG  . LEU D 2 81  ? -20.705 -5.659  -100.384 1.00 30.56  ? 81  LEU D CG  1 
ATOM   5210 C  CD1 . LEU D 2 81  ? -21.817 -6.646  -100.221 1.00 29.43  ? 81  LEU D CD1 1 
ATOM   5211 C  CD2 . LEU D 2 81  ? -20.697 -4.635  -99.278  1.00 32.27  ? 81  LEU D CD2 1 
ATOM   5212 N  N   . LEU D 2 82  ? -16.970 -6.647  -98.156  1.00 25.78  ? 82  LEU D N   1 
ATOM   5213 C  CA  . LEU D 2 82  ? -16.018 -7.580  -97.566  1.00 33.23  ? 82  LEU D CA  1 
ATOM   5214 C  C   . LEU D 2 82  ? -16.440 -7.934  -96.144  1.00 28.91  ? 82  LEU D C   1 
ATOM   5215 O  O   . LEU D 2 82  ? -17.242 -7.237  -95.520  1.00 22.23  ? 82  LEU D O   1 
ATOM   5216 C  CB  . LEU D 2 82  ? -14.602 -6.997  -97.589  1.00 22.29  ? 82  LEU D CB  1 
ATOM   5217 C  CG  . LEU D 2 82  ? -14.518 -5.515  -97.226  1.00 35.84  ? 82  LEU D CG  1 
ATOM   5218 C  CD1 . LEU D 2 82  ? -14.653 -5.324  -95.724  1.00 38.51  ? 82  LEU D CD1 1 
ATOM   5219 C  CD2 . LEU D 2 82  ? -13.196 -4.927  -97.705  1.00 27.44  ? 82  LEU D CD2 1 
ATOM   5220 N  N   . ASN D 2 83  ? -15.897 -9.036  -95.639  1.00 21.85  ? 83  ASN D N   1 
ATOM   5221 C  CA  . ASN D 2 83  ? -16.006 -9.321  -94.220  1.00 26.89  ? 83  ASN D CA  1 
ATOM   5222 C  C   . ASN D 2 83  ? -14.720 -8.924  -93.520  1.00 28.52  ? 83  ASN D C   1 
ATOM   5223 O  O   . ASN D 2 83  ? -13.642 -8.880  -94.123  1.00 25.50  ? 83  ASN D O   1 
ATOM   5224 C  CB  . ASN D 2 83  ? -16.292 -10.795 -93.940  1.00 27.41  ? 83  ASN D CB  1 
ATOM   5225 C  CG  . ASN D 2 83  ? -17.601 -11.242 -94.492  1.00 24.70  ? 83  ASN D CG  1 
ATOM   5226 O  OD1 . ASN D 2 83  ? -17.644 -12.103 -95.353  1.00 25.13  ? 83  ASN D OD1 1 
ATOM   5227 N  ND2 . ASN D 2 83  ? -18.695 -10.660 -93.997  1.00 27.11  ? 83  ASN D ND2 1 
ATOM   5228 N  N   . ILE D 2 84  ? -14.852 -8.650  -92.227  1.00 28.89  ? 84  ILE D N   1 
ATOM   5229 C  CA  . ILE D 2 84  ? -13.727 -8.312  -91.367  1.00 28.43  ? 84  ILE D CA  1 
ATOM   5230 C  C   . ILE D 2 84  ? -13.603 -9.366  -90.276  1.00 29.30  ? 84  ILE D C   1 
ATOM   5231 O  O   . ILE D 2 84  ? -14.602 -9.747  -89.647  1.00 23.29  ? 84  ILE D O   1 
ATOM   5232 C  CB  . ILE D 2 84  ? -13.877 -6.902  -90.772  1.00 20.00  ? 84  ILE D CB  1 
ATOM   5233 C  CG1 . ILE D 2 84  ? -14.033 -5.894  -91.922  1.00 21.40  ? 84  ILE D CG1 1 
ATOM   5234 C  CG2 . ILE D 2 84  ? -12.706 -6.592  -89.843  1.00 17.41  ? 84  ILE D CG2 1 
ATOM   5235 C  CD1 . ILE D 2 84  ? -14.416 -4.491  -91.483  1.00 22.07  ? 84  ILE D CD1 1 
ATOM   5236 N  N   . GLN D 2 85  ? -12.374 -9.840  -90.065  1.00 24.26  ? 85  GLN D N   1 
ATOM   5237 C  CA  . GLN D 2 85  ? -12.080 -10.857 -89.063  1.00 31.86  ? 85  GLN D CA  1 
ATOM   5238 C  C   . GLN D 2 85  ? -10.780 -10.487 -88.361  1.00 29.55  ? 85  GLN D C   1 
ATOM   5239 O  O   . GLN D 2 85  ? -9.750  -10.277 -89.017  1.00 24.85  ? 85  GLN D O   1 
ATOM   5240 C  CB  . GLN D 2 85  ? -11.986 -12.261 -89.703  1.00 27.46  ? 85  GLN D CB  1 
ATOM   5241 C  CG  . GLN D 2 85  ? -11.841 -13.417 -88.705  1.00 27.56  ? 85  GLN D CG  1 
ATOM   5242 C  CD  . GLN D 2 85  ? -11.671 -14.777 -89.381  1.00 32.55  ? 85  GLN D CD  1 
ATOM   5243 O  OE1 . GLN D 2 85  ? -11.264 -14.859 -90.538  1.00 39.50  ? 85  GLN D OE1 1 
ATOM   5244 N  NE2 . GLN D 2 85  ? -11.984 -15.849 -88.658  1.00 28.85  ? 85  GLN D NE2 1 
ATOM   5245 N  N   . PHE D 2 86  ? -10.846 -10.371 -87.033  1.00 23.58  ? 86  PHE D N   1 
ATOM   5246 C  CA  . PHE D 2 86  ? -9.636  -10.278 -86.229  1.00 28.29  ? 86  PHE D CA  1 
ATOM   5247 C  C   . PHE D 2 86  ? -8.726  -11.449 -86.570  1.00 27.68  ? 86  PHE D C   1 
ATOM   5248 O  O   . PHE D 2 86  ? -9.176  -12.594 -86.670  1.00 28.83  ? 86  PHE D O   1 
ATOM   5249 C  CB  . PHE D 2 86  ? -9.982  -10.282 -84.732  1.00 28.95  ? 86  PHE D CB  1 
ATOM   5250 C  CG  . PHE D 2 86  ? -10.529 -8.978  -84.225  1.00 17.95  ? 86  PHE D CG  1 
ATOM   5251 C  CD1 . PHE D 2 86  ? -9.771  -7.818  -84.288  1.00 21.49  ? 86  PHE D CD1 1 
ATOM   5252 C  CD2 . PHE D 2 86  ? -11.808 -8.911  -83.687  1.00 24.64  ? 86  PHE D CD2 1 
ATOM   5253 C  CE1 . PHE D 2 86  ? -10.278 -6.599  -83.826  1.00 22.25  ? 86  PHE D CE1 1 
ATOM   5254 C  CE2 . PHE D 2 86  ? -12.334 -7.695  -83.218  1.00 25.96  ? 86  PHE D CE2 1 
ATOM   5255 C  CZ  . PHE D 2 86  ? -11.561 -6.535  -83.285  1.00 24.55  ? 86  PHE D CZ  1 
ATOM   5256 N  N   . ASN D 2 87  ? -7.450  -11.161 -86.793  1.00 28.20  ? 87  ASN D N   1 
ATOM   5257 C  CA  . ASN D 2 87  ? -6.532  -12.192 -87.258  1.00 34.31  ? 87  ASN D CA  1 
ATOM   5258 C  C   . ASN D 2 87  ? -5.617  -12.570 -86.102  1.00 32.09  ? 87  ASN D C   1 
ATOM   5259 O  O   . ASN D 2 87  ? -4.484  -12.108 -85.991  1.00 35.68  ? 87  ASN D O   1 
ATOM   5260 C  CB  . ASN D 2 87  ? -5.767  -11.755 -88.434  1.00 38.86  ? 87  ASN D CB  1 
ATOM   5261 C  CG  . ASN D 2 87  ? -5.098  -12.922 -89.142  1.00 50.24  ? 87  ASN D CG  1 
ATOM   5262 O  OD1 . ASN D 2 87  ? -3.887  -12.918 -89.361  1.00 53.23  ? 87  ASN D OD1 1 
ATOM   5263 N  ND2 . ASN D 2 87  ? -5.882  -13.948 -89.462  1.00 45.31  ? 87  ASN D ND2 1 
ATOM   5264 N  N   . ILE D 2 88  ? -6.134  -13.425 -85.230  1.00 30.17  ? 88  ILE D N   1 
ATOM   5265 C  CA  . ILE D 2 88  ? -5.405  -13.834 -84.036  1.00 32.47  ? 88  ILE D CA  1 
ATOM   5266 C  C   . ILE D 2 88  ? -5.651  -15.289 -83.764  1.00 31.36  ? 88  ILE D C   1 
ATOM   5267 O  O   . ILE D 2 88  ? -6.710  -15.857 -84.119  1.00 31.69  ? 88  ILE D O   1 
ATOM   5268 C  CB  . ILE D 2 88  ? -5.821  -13.013 -82.817  1.00 33.42  ? 88  ILE D CB  1 
ATOM   5269 C  CG1 . ILE D 2 88  ? -7.335  -13.062 -82.684  1.00 26.71  ? 88  ILE D CG1 1 
ATOM   5270 C  CG2 . ILE D 2 88  ? -5.262  -11.620 -82.887  1.00 35.55  ? 88  ILE D CG2 1 
ATOM   5271 C  CD1 . ILE D 2 88  ? -7.816  -12.518 -81.378  1.00 36.87  ? 88  ILE D CD1 1 
ATOM   5272 N  N   . PRO D 2 89  ? -4.692  -15.959 -83.138  1.00 34.18  ? 89  PRO D N   1 
ATOM   5273 C  CA  . PRO D 2 89  ? -4.947  -17.300 -82.616  1.00 37.66  ? 89  PRO D CA  1 
ATOM   5274 C  C   . PRO D 2 89  ? -6.095  -17.277 -81.622  1.00 33.49  ? 89  PRO D C   1 
ATOM   5275 O  O   . PRO D 2 89  ? -6.365  -16.272 -80.963  1.00 41.17  ? 89  PRO D O   1 
ATOM   5276 C  CB  . PRO D 2 89  ? -3.618  -17.693 -81.947  1.00 30.77  ? 89  PRO D CB  1 
ATOM   5277 C  CG  . PRO D 2 89  ? -2.875  -16.401 -81.768  1.00 38.67  ? 89  PRO D CG  1 
ATOM   5278 C  CD  . PRO D 2 89  ? -3.278  -15.570 -82.962  1.00 36.28  ? 89  PRO D CD  1 
ATOM   5279 N  N   . THR D 2 90  ? -6.780  -18.404 -81.527  1.00 38.37  ? 90  THR D N   1 
ATOM   5280 C  CA  . THR D 2 90  ? -7.903  -18.521 -80.621  1.00 47.14  ? 90  THR D CA  1 
ATOM   5281 C  C   . THR D 2 90  ? -7.952  -19.956 -80.119  1.00 53.66  ? 90  THR D C   1 
ATOM   5282 O  O   . THR D 2 90  ? -7.172  -20.812 -80.543  1.00 62.95  ? 90  THR D O   1 
ATOM   5283 C  CB  . THR D 2 90  ? -9.207  -18.118 -81.323  1.00 41.94  ? 90  THR D CB  1 
ATOM   5284 O  OG1 . THR D 2 90  ? -10.207 -17.814 -80.352  1.00 53.42  ? 90  THR D OG1 1 
ATOM   5285 C  CG2 . THR D 2 90  ? -9.710  -19.243 -82.199  1.00 49.81  ? 90  THR D CG2 1 
ATOM   5286 N  N   . VAL D 2 91  ? -8.848  -20.201 -79.203  1.00 62.20  ? 91  VAL D N   1 
ATOM   5287 C  CA  . VAL D 2 91  ? -9.254  -21.549 -78.830  1.00 60.13  ? 91  VAL D CA  1 
ATOM   5288 C  C   . VAL D 2 91  ? -10.476 -21.908 -79.664  1.00 65.40  ? 91  VAL D C   1 
ATOM   5289 O  O   . VAL D 2 91  ? -11.296 -21.036 -79.982  1.00 69.17  ? 91  VAL D O   1 
ATOM   5290 C  CB  . VAL D 2 91  ? -9.547  -21.606 -77.323  1.00 57.61  ? 91  VAL D CB  1 
ATOM   5291 C  CG1 . VAL D 2 91  ? -8.250  -21.584 -76.560  1.00 52.10  ? 91  VAL D CG1 1 
ATOM   5292 C  CG2 . VAL D 2 91  ? -10.404 -20.417 -76.930  1.00 49.61  ? 91  VAL D CG2 1 
ATOM   5293 N  N   . LYS D 2 92  ? -10.610 -23.191 -80.028  1.00 66.30  ? 92  LYS D N   1 
ATOM   5294 C  CA  . LYS D 2 92  ? -11.577 -23.562 -81.064  1.00 65.91  ? 92  LYS D CA  1 
ATOM   5295 C  C   . LYS D 2 92  ? -12.987 -23.117 -80.717  1.00 65.76  ? 92  LYS D C   1 
ATOM   5296 O  O   . LYS D 2 92  ? -13.775 -22.807 -81.618  1.00 74.30  ? 92  LYS D O   1 
ATOM   5297 C  CB  . LYS D 2 92  ? -11.583 -25.072 -81.326  1.00 73.66  ? 92  LYS D CB  1 
ATOM   5298 C  CG  . LYS D 2 92  ? -10.263 -25.789 -81.156  1.00 84.71  ? 92  LYS D CG  1 
ATOM   5299 C  CD  . LYS D 2 92  ? -10.274 -27.120 -81.915  1.00 81.93  ? 92  LYS D CD  1 
ATOM   5300 C  CE  . LYS D 2 92  ? -9.167  -28.046 -81.436  1.00 82.68  ? 92  LYS D CE  1 
ATOM   5301 N  NZ  . LYS D 2 92  ? -7.827  -27.652 -81.973  1.00 79.50  ? 92  LYS D NZ  1 
ATOM   5302 N  N   . LEU D 2 93  ? -13.332 -23.086 -79.428  1.00 63.34  ? 93  LEU D N   1 
ATOM   5303 C  CA  . LEU D 2 93  ? -14.667 -22.631 -79.066  1.00 63.87  ? 93  LEU D CA  1 
ATOM   5304 C  C   . LEU D 2 93  ? -14.881 -21.172 -79.443  1.00 62.27  ? 93  LEU D C   1 
ATOM   5305 O  O   . LEU D 2 93  ? -16.029 -20.744 -79.591  1.00 63.03  ? 93  LEU D O   1 
ATOM   5306 C  CB  . LEU D 2 93  ? -14.919 -22.853 -77.569  1.00 70.82  ? 93  LEU D CB  1 
ATOM   5307 C  CG  . LEU D 2 93  ? -14.680 -24.282 -77.040  1.00 86.73  ? 93  LEU D CG  1 
ATOM   5308 C  CD1 . LEU D 2 93  ? -15.029 -24.419 -75.553  1.00 77.86  ? 93  LEU D CD1 1 
ATOM   5309 C  CD2 . LEU D 2 93  ? -15.440 -25.330 -77.859  1.00 64.39  ? 93  LEU D CD2 1 
ATOM   5310 N  N   . CYS D 2 94  ? -13.802 -20.414 -79.653  1.00 60.14  ? 94  CYS D N   1 
ATOM   5311 C  CA  . CYS D 2 94  ? -13.882 -18.975 -79.866  1.00 53.80  ? 94  CYS D CA  1 
ATOM   5312 C  C   . CYS D 2 94  ? -13.586 -18.553 -81.302  1.00 53.99  ? 94  CYS D C   1 
ATOM   5313 O  O   . CYS D 2 94  ? -13.371 -17.361 -81.548  1.00 53.81  ? 94  CYS D O   1 
ATOM   5314 C  CB  . CYS D 2 94  ? -12.934 -18.246 -78.913  1.00 47.61  ? 94  CYS D CB  1 
ATOM   5315 S  SG  . CYS D 2 94  ? -13.360 -18.377 -77.170  1.00 56.46  ? 94  CYS D SG  1 
ATOM   5316 N  N   . VAL D 2 95  ? -13.589 -19.486 -82.261  1.00 54.85  ? 95  VAL D N   1 
ATOM   5317 C  CA  . VAL D 2 95  ? -13.157 -19.142 -83.617  1.00 47.52  ? 95  VAL D CA  1 
ATOM   5318 C  C   . VAL D 2 95  ? -14.085 -18.105 -84.229  1.00 40.99  ? 95  VAL D C   1 
ATOM   5319 O  O   . VAL D 2 95  ? -13.637 -17.101 -84.798  1.00 42.84  ? 95  VAL D O   1 
ATOM   5320 C  CB  . VAL D 2 95  ? -13.068 -20.394 -84.505  1.00 55.49  ? 95  VAL D CB  1 
ATOM   5321 C  CG1 . VAL D 2 95  ? -12.908 -19.985 -85.975  1.00 40.69  ? 95  VAL D CG1 1 
ATOM   5322 C  CG2 . VAL D 2 95  ? -11.913 -21.274 -84.063  1.00 64.12  ? 95  VAL D CG2 1 
ATOM   5323 N  N   . SER D 2 96  ? -15.393 -18.322 -84.120  1.00 29.34  ? 96  SER D N   1 
ATOM   5324 C  CA  . SER D 2 96  ? -16.290 -17.364 -84.743  1.00 37.20  ? 96  SER D CA  1 
ATOM   5325 C  C   . SER D 2 96  ? -16.308 -16.035 -84.005  1.00 38.02  ? 96  SER D C   1 
ATOM   5326 O  O   . SER D 2 96  ? -16.804 -15.044 -84.556  1.00 33.81  ? 96  SER D O   1 
ATOM   5327 C  CB  . SER D 2 96  ? -17.708 -17.914 -84.811  1.00 34.64  ? 96  SER D CB  1 
ATOM   5328 O  OG  . SER D 2 96  ? -18.306 -17.831 -83.545  1.00 31.14  ? 96  SER D OG  1 
ATOM   5329 N  N   . TYR D 2 97  ? -15.774 -15.984 -82.785  1.00 29.71  ? 97  TYR D N   1 
ATOM   5330 C  CA  . TYR D 2 97  ? -15.694 -14.729 -82.053  1.00 35.73  ? 97  TYR D CA  1 
ATOM   5331 C  C   . TYR D 2 97  ? -14.512 -13.886 -82.485  1.00 31.30  ? 97  TYR D C   1 
ATOM   5332 O  O   . TYR D 2 97  ? -14.101 -12.966 -81.762  1.00 31.62  ? 97  TYR D O   1 
ATOM   5333 C  CB  . TYR D 2 97  ? -15.666 -15.006 -80.548  1.00 38.53  ? 97  TYR D CB  1 
ATOM   5334 C  CG  . TYR D 2 97  ? -17.034 -15.427 -80.083  1.00 36.09  ? 97  TYR D CG  1 
ATOM   5335 C  CD1 . TYR D 2 97  ? -18.026 -14.488 -79.887  1.00 30.60  ? 97  TYR D CD1 1 
ATOM   5336 C  CD2 . TYR D 2 97  ? -17.355 -16.777 -79.920  1.00 37.16  ? 97  TYR D CD2 1 
ATOM   5337 C  CE1 . TYR D 2 97  ? -19.285 -14.858 -79.500  1.00 38.13  ? 97  TYR D CE1 1 
ATOM   5338 C  CE2 . TYR D 2 97  ? -18.613 -17.162 -79.531  1.00 36.15  ? 97  TYR D CE2 1 
ATOM   5339 C  CZ  . TYR D 2 97  ? -19.578 -16.191 -79.324  1.00 45.92  ? 97  TYR D CZ  1 
ATOM   5340 O  OH  . TYR D 2 97  ? -20.849 -16.533 -78.935  1.00 51.82  ? 97  TYR D OH  1 
ATOM   5341 N  N   . THR D 2 98  ? -13.966 -14.187 -83.661  1.00 29.97  ? 98  THR D N   1 
ATOM   5342 C  CA  . THR D 2 98  ? -13.060 -13.294 -84.357  1.00 24.92  ? 98  THR D CA  1 
ATOM   5343 C  C   . THR D 2 98  ? -13.726 -12.553 -85.504  1.00 27.91  ? 98  THR D C   1 
ATOM   5344 O  O   . THR D 2 98  ? -13.128 -11.613 -86.034  1.00 24.93  ? 98  THR D O   1 
ATOM   5345 C  CB  . THR D 2 98  ? -11.865 -14.070 -84.903  1.00 29.99  ? 98  THR D CB  1 
ATOM   5346 O  OG1 . THR D 2 98  ? -12.329 -15.104 -85.781  1.00 32.09  ? 98  THR D OG1 1 
ATOM   5347 C  CG2 . THR D 2 98  ? -11.078 -14.675 -83.769  1.00 28.08  ? 98  THR D CG2 1 
ATOM   5348 N  N   . ILE D 2 99  ? -14.941 -12.947 -85.893  1.00 32.95  ? 99  ILE D N   1 
ATOM   5349 C  CA  . ILE D 2 99  ? -15.598 -12.447 -87.098  1.00 22.80  ? 99  ILE D CA  1 
ATOM   5350 C  C   . ILE D 2 99  ? -16.566 -11.330 -86.738  1.00 25.32  ? 99  ILE D C   1 
ATOM   5351 O  O   . ILE D 2 99  ? -17.509 -11.531 -85.963  1.00 22.64  ? 99  ILE D O   1 
ATOM   5352 C  CB  . ILE D 2 99  ? -16.320 -13.572 -87.853  1.00 28.94  ? 99  ILE D CB  1 
ATOM   5353 C  CG1 . ILE D 2 99  ? -15.306 -14.630 -88.309  1.00 29.46  ? 99  ILE D CG1 1 
ATOM   5354 C  CG2 . ILE D 2 99  ? -17.148 -13.003 -89.025  1.00 21.83  ? 99  ILE D CG2 1 
ATOM   5355 C  CD1 . ILE D 2 99  ? -15.917 -15.932 -88.630  1.00 23.88  ? 99  ILE D CD1 1 
ATOM   5356 N  N   . TRP D 2 100 ? -16.347 -10.163 -87.341  1.00 25.00  ? 100 TRP D N   1 
ATOM   5357 C  CA  . TRP D 2 100 ? -17.191 -9.009  -87.091  1.00 21.68  ? 100 TRP D CA  1 
ATOM   5358 C  C   . TRP D 2 100 ? -18.608 -9.269  -87.570  1.00 23.30  ? 100 TRP D C   1 
ATOM   5359 O  O   . TRP D 2 100 ? -18.838 -9.987  -88.542  1.00 28.20  ? 100 TRP D O   1 
ATOM   5360 C  CB  . TRP D 2 100 ? -16.634 -7.767  -87.789  1.00 25.12  ? 100 TRP D CB  1 
ATOM   5361 C  CG  . TRP D 2 100 ? -15.325 -7.273  -87.273  1.00 21.80  ? 100 TRP D CG  1 
ATOM   5362 C  CD1 . TRP D 2 100 ? -14.319 -8.021  -86.723  1.00 24.08  ? 100 TRP D CD1 1 
ATOM   5363 C  CD2 . TRP D 2 100 ? -14.869 -5.913  -87.257  1.00 20.11  ? 100 TRP D CD2 1 
ATOM   5364 N  NE1 . TRP D 2 100 ? -13.264 -7.208  -86.371  1.00 28.95  ? 100 TRP D NE1 1 
ATOM   5365 C  CE2 . TRP D 2 100 ? -13.578 -5.911  -86.691  1.00 21.48  ? 100 TRP D CE2 1 
ATOM   5366 C  CE3 . TRP D 2 100 ? -15.418 -4.700  -87.688  1.00 20.55  ? 100 TRP D CE3 1 
ATOM   5367 C  CZ2 . TRP D 2 100 ? -12.839 -4.743  -86.519  1.00 20.15  ? 100 TRP D CZ2 1 
ATOM   5368 C  CZ3 . TRP D 2 100 ? -14.675 -3.542  -87.521  1.00 23.18  ? 100 TRP D CZ3 1 
ATOM   5369 C  CH2 . TRP D 2 100 ? -13.396 -3.577  -86.941  1.00 16.69  ? 100 TRP D CH2 1 
ATOM   5370 N  N   . LYS D 2 101 ? -19.556 -8.669  -86.864  1.00 17.73  ? 101 LYS D N   1 
ATOM   5371 C  CA  . LYS D 2 101 ? -20.977 -8.729  -87.160  1.00 25.71  ? 101 LYS D CA  1 
ATOM   5372 C  C   . LYS D 2 101 ? -21.627 -7.566  -86.428  1.00 28.53  ? 101 LYS D C   1 
ATOM   5373 O  O   . LYS D 2 101 ? -21.074 -7.038  -85.462  1.00 27.78  ? 101 LYS D O   1 
ATOM   5374 C  CB  . LYS D 2 101 ? -21.593 -10.067 -86.734  1.00 25.50  ? 101 LYS D CB  1 
ATOM   5375 C  CG  . LYS D 2 101 ? -21.304 -10.405 -85.291  1.00 36.15  ? 101 LYS D CG  1 
ATOM   5376 C  CD  . LYS D 2 101 ? -22.369 -11.269 -84.632  1.00 33.92  ? 101 LYS D CD  1 
ATOM   5377 C  CE  . LYS D 2 101 ? -23.763 -10.855 -84.982  1.00 37.79  ? 101 LYS D CE  1 
ATOM   5378 N  NZ  . LYS D 2 101 ? -24.702 -11.716 -84.190  1.00 54.14  ? 101 LYS D NZ  1 
ATOM   5379 N  N   . VAL D 2 102 ? -22.805 -7.166  -86.884  1.00 33.16  ? 102 VAL D N   1 
ATOM   5380 C  CA  . VAL D 2 102 ? -23.514 -6.052  -86.270  1.00 31.77  ? 102 VAL D CA  1 
ATOM   5381 C  C   . VAL D 2 102 ? -24.738 -6.590  -85.542  1.00 42.93  ? 102 VAL D C   1 
ATOM   5382 O  O   . VAL D 2 102 ? -25.511 -7.374  -86.110  1.00 34.59  ? 102 VAL D O   1 
ATOM   5383 C  CB  . VAL D 2 102 ? -23.897 -4.985  -87.308  1.00 33.88  ? 102 VAL D CB  1 
ATOM   5384 C  CG1 . VAL D 2 102 ? -25.017 -4.094  -86.777  1.00 36.86  ? 102 VAL D CG1 1 
ATOM   5385 C  CG2 . VAL D 2 102 ? -22.689 -4.148  -87.656  1.00 32.92  ? 102 VAL D CG2 1 
ATOM   5386 N  N   . GLY D 2 103 ? -24.896 -6.179  -84.277  1.00 46.15  ? 103 GLY D N   1 
ATOM   5387 C  CA  . GLY D 2 103 ? -26.104 -6.409  -83.498  1.00 57.98  ? 103 GLY D CA  1 
ATOM   5388 C  C   . GLY D 2 103 ? -26.368 -5.343  -82.438  1.00 61.66  ? 103 GLY D C   1 
ATOM   5389 O  O   . GLY D 2 103 ? -25.706 -5.279  -81.390  1.00 58.05  ? 103 GLY D O   1 
ATOM   5390 N  N   . LEU D 2 109 ? -34.073 2.565   -81.343  1.00 36.61  ? 109 LEU D N   1 
ATOM   5391 C  CA  . LEU D 2 109 ? -32.910 1.800   -81.761  1.00 58.15  ? 109 LEU D CA  1 
ATOM   5392 C  C   . LEU D 2 109 ? -32.298 2.182   -83.102  1.00 58.93  ? 109 LEU D C   1 
ATOM   5393 O  O   . LEU D 2 109 ? -32.981 2.159   -84.125  1.00 60.95  ? 109 LEU D O   1 
ATOM   5394 N  N   . ARG D 2 110 ? -31.007 2.538   -83.101  1.00 58.46  ? 110 ARG D N   1 
ATOM   5395 C  CA  . ARG D 2 110 ? -30.282 2.781   -84.346  1.00 37.85  ? 110 ARG D CA  1 
ATOM   5396 C  C   . ARG D 2 110 ? -28.783 2.532   -84.196  1.00 47.71  ? 110 ARG D C   1 
ATOM   5397 O  O   . ARG D 2 110 ? -28.198 1.858   -85.052  1.00 46.59  ? 110 ARG D O   1 
ATOM   5398 C  CB  . ARG D 2 110 ? -30.515 4.200   -84.881  1.00 37.56  ? 110 ARG D CB  1 
ATOM   5399 C  CG  . ARG D 2 110 ? -30.715 4.206   -86.388  1.00 50.58  ? 110 ARG D CG  1 
ATOM   5400 C  CD  . ARG D 2 110 ? -30.419 5.550   -87.003  1.00 49.95  ? 110 ARG D CD  1 
ATOM   5401 N  NE  . ARG D 2 110 ? -31.291 6.598   -86.490  1.00 57.85  ? 110 ARG D NE  1 
ATOM   5402 C  CZ  . ARG D 2 110 ? -31.831 7.544   -87.246  1.00 58.94  ? 110 ARG D CZ  1 
ATOM   5403 N  NH1 . ARG D 2 110 ? -31.629 7.579   -88.553  1.00 71.28  ? 110 ARG D NH1 1 
ATOM   5404 N  NH2 . ARG D 2 110 ? -32.595 8.476   -86.679  1.00 50.18  ? 110 ARG D NH2 1 
ATOM   5405 N  N   . THR D 2 111 ? -28.124 3.064   -83.154  1.00 43.03  ? 111 THR D N   1 
ATOM   5406 C  CA  . THR D 2 111 ? -26.695 2.753   -82.997  1.00 38.97  ? 111 THR D CA  1 
ATOM   5407 C  C   . THR D 2 111 ? -26.578 1.312   -82.525  1.00 40.03  ? 111 THR D C   1 
ATOM   5408 O  O   . THR D 2 111 ? -26.653 1.032   -81.327  1.00 61.07  ? 111 THR D O   1 
ATOM   5409 C  CB  . THR D 2 111 ? -25.972 3.684   -82.024  1.00 31.60  ? 111 THR D CB  1 
ATOM   5410 O  OG1 . THR D 2 111 ? -26.408 3.458   -80.683  1.00 36.61  ? 111 THR D OG1 1 
ATOM   5411 C  CG2 . THR D 2 111 ? -26.198 5.131   -82.392  1.00 39.12  ? 111 THR D CG2 1 
ATOM   5412 N  N   . MET D 2 112 ? -26.423 0.386   -83.467  1.00 38.36  ? 112 MET D N   1 
ATOM   5413 C  CA  . MET D 2 112 ? -26.131 -1.005  -83.151  1.00 41.68  ? 112 MET D CA  1 
ATOM   5414 C  C   . MET D 2 112 ? -24.627 -1.190  -82.978  1.00 38.48  ? 112 MET D C   1 
ATOM   5415 O  O   . MET D 2 112 ? -23.822 -0.554  -83.672  1.00 34.90  ? 112 MET D O   1 
ATOM   5416 C  CB  . MET D 2 112 ? -26.650 -1.935  -84.248  1.00 41.96  ? 112 MET D CB  1 
ATOM   5417 C  CG  . MET D 2 112 ? -28.105 -2.335  -84.104  1.00 51.80  ? 112 MET D CG  1 
ATOM   5418 S  SD  . MET D 2 112 ? -28.906 -2.481  -85.709  1.00 69.21  ? 112 MET D SD  1 
ATOM   5419 C  CE  . MET D 2 112 ? -29.700 -0.876  -85.827  1.00 66.63  ? 112 MET D CE  1 
ATOM   5420 N  N   . LEU D 2 113 ? -24.259 -2.073  -82.052  1.00 34.89  ? 113 LEU D N   1 
ATOM   5421 C  CA  . LEU D 2 113 ? -22.874 -2.268  -81.653  1.00 29.71  ? 113 LEU D CA  1 
ATOM   5422 C  C   . LEU D 2 113 ? -22.161 -3.247  -82.566  1.00 31.79  ? 113 LEU D C   1 
ATOM   5423 O  O   . LEU D 2 113 ? -22.704 -4.296  -82.919  1.00 31.12  ? 113 LEU D O   1 
ATOM   5424 C  CB  . LEU D 2 113 ? -22.794 -2.784  -80.219  1.00 29.43  ? 113 LEU D CB  1 
ATOM   5425 C  CG  . LEU D 2 113 ? -23.393 -1.923  -79.116  1.00 30.13  ? 113 LEU D CG  1 
ATOM   5426 C  CD1 . LEU D 2 113 ? -23.034 -2.512  -77.753  1.00 25.65  ? 113 LEU D CD1 1 
ATOM   5427 C  CD2 . LEU D 2 113 ? -22.893 -0.480  -79.250  1.00 26.82  ? 113 LEU D CD2 1 
ATOM   5428 N  N   . LEU D 2 114 ? -20.924 -2.911  -82.922  1.00 29.16  ? 114 LEU D N   1 
ATOM   5429 C  CA  . LEU D 2 114 ? -20.075 -3.877  -83.602  1.00 27.72  ? 114 LEU D CA  1 
ATOM   5430 C  C   . LEU D 2 114 ? -19.618 -4.949  -82.614  1.00 24.10  ? 114 LEU D C   1 
ATOM   5431 O  O   . LEU D 2 114 ? -19.073 -4.628  -81.553  1.00 24.10  ? 114 LEU D O   1 
ATOM   5432 C  CB  . LEU D 2 114 ? -18.870 -3.180  -84.220  1.00 22.27  ? 114 LEU D CB  1 
ATOM   5433 C  CG  . LEU D 2 114 ? -19.064 -2.912  -85.710  1.00 27.79  ? 114 LEU D CG  1 
ATOM   5434 C  CD1 . LEU D 2 114 ? -20.129 -1.821  -85.920  1.00 32.56  ? 114 LEU D CD1 1 
ATOM   5435 C  CD2 . LEU D 2 114 ? -17.759 -2.542  -86.363  1.00 21.13  ? 114 LEU D CD2 1 
ATOM   5436 N  N   . GLU D 2 115 ? -19.845 -6.220  -82.975  1.00 25.98  ? 115 GLU D N   1 
ATOM   5437 C  CA  . GLU D 2 115 ? -19.544 -7.402  -82.166  1.00 28.49  ? 115 GLU D CA  1 
ATOM   5438 C  C   . GLU D 2 115 ? -18.760 -8.419  -82.986  1.00 26.34  ? 115 GLU D C   1 
ATOM   5439 O  O   . GLU D 2 115 ? -18.601 -8.276  -84.203  1.00 28.89  ? 115 GLU D O   1 
ATOM   5440 C  CB  . GLU D 2 115 ? -20.819 -8.095  -81.681  1.00 27.27  ? 115 GLU D CB  1 
ATOM   5441 C  CG  . GLU D 2 115 ? -21.952 -7.168  -81.400  1.00 40.81  ? 115 GLU D CG  1 
ATOM   5442 C  CD  . GLU D 2 115 ? -23.241 -7.923  -81.158  1.00 47.96  ? 115 GLU D CD  1 
ATOM   5443 O  OE1 . GLU D 2 115 ? -23.460 -8.954  -81.830  1.00 46.71  ? 115 GLU D OE1 1 
ATOM   5444 O  OE2 . GLU D 2 115 ? -24.035 -7.475  -80.305  1.00 58.73  ? 115 GLU D OE2 1 
ATOM   5445 N  N   . THR D 2 116 ? -18.291 -9.482  -82.325  1.00 18.00  ? 116 THR D N   1 
ATOM   5446 C  CA  . THR D 2 116 ? -17.851 -10.638 -83.089  1.00 31.38  ? 116 THR D CA  1 
ATOM   5447 C  C   . THR D 2 116 ? -18.845 -11.777 -82.890  1.00 25.65  ? 116 THR D C   1 
ATOM   5448 O  O   . THR D 2 116 ? -19.906 -11.605 -82.298  1.00 20.70  ? 116 THR D O   1 
ATOM   5449 C  CB  . THR D 2 116 ? -16.426 -11.068 -82.724  1.00 28.64  ? 116 THR D CB  1 
ATOM   5450 O  OG1 . THR D 2 116 ? -16.385 -11.516 -81.362  1.00 24.18  ? 116 THR D OG1 1 
ATOM   5451 C  CG2 . THR D 2 116 ? -15.444 -9.925  -82.944  1.00 28.85  ? 116 THR D CG2 1 
ATOM   5452 N  N   . GLY D 2 117 ? -18.492 -12.956 -83.385  1.00 28.77  ? 117 GLY D N   1 
ATOM   5453 C  CA  . GLY D 2 117 ? -19.417 -14.061 -83.360  1.00 32.27  ? 117 GLY D CA  1 
ATOM   5454 C  C   . GLY D 2 117 ? -20.227 -14.190 -84.623  1.00 39.70  ? 117 GLY D C   1 
ATOM   5455 O  O   . GLY D 2 117 ? -21.374 -14.649 -84.567  1.00 41.91  ? 117 GLY D O   1 
ATOM   5456 N  N   . GLY D 2 118 ? -19.673 -13.776 -85.764  1.00 36.65  ? 118 GLY D N   1 
ATOM   5457 C  CA  . GLY D 2 118 ? -20.366 -13.824 -87.029  1.00 31.51  ? 118 GLY D CA  1 
ATOM   5458 C  C   . GLY D 2 118 ? -19.824 -14.901 -87.948  1.00 32.66  ? 118 GLY D C   1 
ATOM   5459 O  O   . GLY D 2 118 ? -19.058 -15.783 -87.551  1.00 34.30  ? 118 GLY D O   1 
ATOM   5460 N  N   . THR D 2 119 ? -20.231 -14.809 -89.211  1.00 36.93  ? 119 THR D N   1 
ATOM   5461 C  CA  . THR D 2 119 ? -19.787 -15.746 -90.228  1.00 34.72  ? 119 THR D CA  1 
ATOM   5462 C  C   . THR D 2 119 ? -19.176 -14.972 -91.382  1.00 35.85  ? 119 THR D C   1 
ATOM   5463 O  O   . THR D 2 119 ? -19.467 -13.788 -91.588  1.00 32.20  ? 119 THR D O   1 
ATOM   5464 C  CB  . THR D 2 119 ? -20.932 -16.613 -90.753  1.00 34.40  ? 119 THR D CB  1 
ATOM   5465 O  OG1 . THR D 2 119 ? -22.032 -15.768 -91.099  1.00 39.84  ? 119 THR D OG1 1 
ATOM   5466 C  CG2 . THR D 2 119 ? -21.374 -17.597 -89.679  1.00 29.73  ? 119 THR D CG2 1 
ATOM   5467 N  N   . ILE D 2 120 ? -18.330 -15.667 -92.139  1.00 26.70  ? 120 ILE D N   1 
ATOM   5468 C  CA  . ILE D 2 120 ? -17.727 -15.131 -93.350  1.00 31.31  ? 120 ILE D CA  1 
ATOM   5469 C  C   . ILE D 2 120 ? -18.499 -15.649 -94.554  1.00 37.17  ? 120 ILE D C   1 
ATOM   5470 O  O   . ILE D 2 120 ? -18.890 -16.820 -94.592  1.00 25.81  ? 120 ILE D O   1 
ATOM   5471 C  CB  . ILE D 2 120 ? -16.242 -15.525 -93.450  1.00 29.04  ? 120 ILE D CB  1 
ATOM   5472 C  CG1 . ILE D 2 120 ? -15.445 -14.944 -92.280  1.00 31.15  ? 120 ILE D CG1 1 
ATOM   5473 C  CG2 . ILE D 2 120 ? -15.649 -15.047 -94.774  1.00 32.81  ? 120 ILE D CG2 1 
ATOM   5474 C  CD1 . ILE D 2 120 ? -14.134 -15.680 -92.017  1.00 23.76  ? 120 ILE D CD1 1 
ATOM   5475 N  N   . GLY D 2 121 ? -18.733 -14.770 -95.531  1.00 35.26  ? 121 GLY D N   1 
ATOM   5476 C  CA  . GLY D 2 121 ? -19.215 -15.160 -96.847  1.00 33.10  ? 121 GLY D CA  1 
ATOM   5477 C  C   . GLY D 2 121 ? -20.448 -16.040 -96.896  1.00 34.43  ? 121 GLY D C   1 
ATOM   5478 O  O   . GLY D 2 121 ? -20.454 -17.075 -97.568  1.00 34.42  ? 121 GLY D O   1 
ATOM   5479 N  N   . GLN D 2 122 ? -21.495 -15.628 -96.187  1.00 30.51  ? 122 GLN D N   1 
ATOM   5480 C  CA  . GLN D 2 122 ? -22.745 -16.357 -96.083  1.00 25.58  ? 122 GLN D CA  1 
ATOM   5481 C  C   . GLN D 2 122 ? -23.869 -15.344 -96.132  1.00 33.89  ? 122 GLN D C   1 
ATOM   5482 O  O   . GLN D 2 122 ? -23.639 -14.133 -96.045  1.00 35.85  ? 122 GLN D O   1 
ATOM   5483 C  CB  . GLN D 2 122 ? -22.826 -17.167 -94.787  1.00 30.03  ? 122 GLN D CB  1 
ATOM   5484 C  CG  . GLN D 2 122 ? -22.130 -18.504 -94.810  1.00 33.76  ? 122 GLN D CG  1 
ATOM   5485 C  CD  . GLN D 2 122 ? -22.051 -19.108 -93.421  1.00 55.12  ? 122 GLN D CD  1 
ATOM   5486 O  OE1 . GLN D 2 122 ? -23.007 -19.038 -92.635  1.00 58.22  ? 122 GLN D OE1 1 
ATOM   5487 N  NE2 . GLN D 2 122 ? -20.905 -19.704 -93.106  1.00 60.64  ? 122 GLN D NE2 1 
ATOM   5488 N  N   . ALA D 2 123 ? -25.100 -15.839 -96.263  1.00 34.12  ? 123 ALA D N   1 
ATOM   5489 C  CA  . ALA D 2 123 ? -26.217 -14.913 -96.393  1.00 31.43  ? 123 ALA D CA  1 
ATOM   5490 C  C   . ALA D 2 123 ? -26.450 -14.146 -95.103  1.00 31.30  ? 123 ALA D C   1 
ATOM   5491 O  O   . ALA D 2 123 ? -26.943 -13.018 -95.144  1.00 45.50  ? 123 ALA D O   1 
ATOM   5492 C  CB  . ALA D 2 123 ? -27.479 -15.658 -96.811  1.00 27.84  ? 123 ALA D CB  1 
ATOM   5493 N  N   . ASP D 2 124 ? -26.080 -14.727 -93.960  1.00 41.60  ? 124 ASP D N   1 
ATOM   5494 C  CA  . ASP D 2 124 ? -26.239 -14.102 -92.648  1.00 40.18  ? 124 ASP D CA  1 
ATOM   5495 C  C   . ASP D 2 124 ? -25.043 -13.243 -92.232  1.00 39.08  ? 124 ASP D C   1 
ATOM   5496 O  O   . ASP D 2 124 ? -25.130 -12.530 -91.226  1.00 40.46  ? 124 ASP D O   1 
ATOM   5497 C  CB  . ASP D 2 124 ? -26.487 -15.185 -91.585  1.00 35.04  ? 124 ASP D CB  1 
ATOM   5498 C  CG  . ASP D 2 124 ? -25.385 -16.267 -91.566  1.00 55.70  ? 124 ASP D CG  1 
ATOM   5499 O  OD1 . ASP D 2 124 ? -24.338 -16.092 -92.231  1.00 49.09  ? 124 ASP D OD1 1 
ATOM   5500 O  OD2 . ASP D 2 124 ? -25.572 -17.310 -90.898  1.00 63.95  ? 124 ASP D OD2 1 
ATOM   5501 N  N   . SER D 2 125 ? -23.944 -13.276 -92.978  1.00 25.15  ? 125 SER D N   1 
ATOM   5502 C  CA  . SER D 2 125 ? -22.753 -12.529 -92.594  1.00 27.35  ? 125 SER D CA  1 
ATOM   5503 C  C   . SER D 2 125 ? -22.965 -11.011 -92.640  1.00 36.59  ? 125 SER D C   1 
ATOM   5504 O  O   . SER D 2 125 ? -23.819 -10.489 -93.366  1.00 35.47  ? 125 SER D O   1 
ATOM   5505 C  CB  . SER D 2 125 ? -21.588 -12.911 -93.501  1.00 31.66  ? 125 SER D CB  1 
ATOM   5506 O  OG  . SER D 2 125 ? -21.494 -14.323 -93.660  1.00 36.35  ? 125 SER D OG  1 
ATOM   5507 N  N   . SER D 2 126 ? -22.166 -10.302 -91.842  1.00 29.50  ? 126 SER D N   1 
ATOM   5508 C  CA  . SER D 2 126 ? -22.122 -8.845  -91.864  1.00 28.99  ? 126 SER D CA  1 
ATOM   5509 C  C   . SER D 2 126 ? -21.070 -8.395  -92.866  1.00 28.31  ? 126 SER D C   1 
ATOM   5510 O  O   . SER D 2 126 ? -19.883 -8.712  -92.710  1.00 27.35  ? 126 SER D O   1 
ATOM   5511 C  CB  . SER D 2 126 ? -21.786 -8.291  -90.483  1.00 26.62  ? 126 SER D CB  1 
ATOM   5512 O  OG  . SER D 2 126 ? -22.906 -8.358  -89.609  1.00 34.50  ? 126 SER D OG  1 
ATOM   5513 N  N   . TYR D 2 127 ? -21.493 -7.653  -93.882  1.00 28.56  ? 127 TYR D N   1 
ATOM   5514 C  CA  . TYR D 2 127 ? -20.591 -7.181  -94.922  1.00 23.71  ? 127 TYR D CA  1 
ATOM   5515 C  C   . TYR D 2 127 ? -20.258 -5.721  -94.688  1.00 26.13  ? 127 TYR D C   1 
ATOM   5516 O  O   . TYR D 2 127 ? -21.121 -4.935  -94.271  1.00 26.57  ? 127 TYR D O   1 
ATOM   5517 C  CB  . TYR D 2 127 ? -21.203 -7.390  -96.312  1.00 21.83  ? 127 TYR D CB  1 
ATOM   5518 C  CG  . TYR D 2 127 ? -21.344 -8.862  -96.570  1.00 20.84  ? 127 TYR D CG  1 
ATOM   5519 C  CD1 . TYR D 2 127 ? -20.321 -9.578  -97.175  1.00 23.61  ? 127 TYR D CD1 1 
ATOM   5520 C  CD2 . TYR D 2 127 ? -22.453 -9.558  -96.112  1.00 22.47  ? 127 TYR D CD2 1 
ATOM   5521 C  CE1 . TYR D 2 127 ? -20.423 -10.940 -97.370  1.00 20.06  ? 127 TYR D CE1 1 
ATOM   5522 C  CE2 . TYR D 2 127 ? -22.567 -10.923 -96.311  1.00 31.47  ? 127 TYR D CE2 1 
ATOM   5523 C  CZ  . TYR D 2 127 ? -21.541 -11.604 -96.938  1.00 20.07  ? 127 TYR D CZ  1 
ATOM   5524 O  OH  . TYR D 2 127 ? -21.646 -12.958 -97.124  1.00 34.70  ? 127 TYR D OH  1 
ATOM   5525 N  N   . PHE D 2 128 ? -18.999 -5.369  -94.946  1.00 20.74  ? 128 PHE D N   1 
ATOM   5526 C  CA  . PHE D 2 128 ? -18.496 -4.020  -94.736  1.00 24.91  ? 128 PHE D CA  1 
ATOM   5527 C  C   . PHE D 2 128 ? -17.863 -3.494  -96.020  1.00 26.57  ? 128 PHE D C   1 
ATOM   5528 O  O   . PHE D 2 128 ? -17.537 -4.255  -96.939  1.00 30.84  ? 128 PHE D O   1 
ATOM   5529 C  CB  . PHE D 2 128 ? -17.492 -3.990  -93.568  1.00 19.12  ? 128 PHE D CB  1 
ATOM   5530 C  CG  . PHE D 2 128 ? -18.114 -4.318  -92.224  1.00 26.98  ? 128 PHE D CG  1 
ATOM   5531 C  CD1 . PHE D 2 128 ? -18.324 -5.641  -91.846  1.00 25.62  ? 128 PHE D CD1 1 
ATOM   5532 C  CD2 . PHE D 2 128 ? -18.481 -3.307  -91.333  1.00 24.87  ? 128 PHE D CD2 1 
ATOM   5533 C  CE1 . PHE D 2 128 ? -18.894 -5.953  -90.612  1.00 27.46  ? 128 PHE D CE1 1 
ATOM   5534 C  CE2 . PHE D 2 128 ? -19.035 -3.608  -90.096  1.00 20.47  ? 128 PHE D CE2 1 
ATOM   5535 C  CZ  . PHE D 2 128 ? -19.251 -4.937  -89.734  1.00 22.18  ? 128 PHE D CZ  1 
ATOM   5536 N  N   . LYS D 2 129 ? -17.714 -2.166  -96.082  1.00 26.62  ? 129 LYS D N   1 
ATOM   5537 C  CA  . LYS D 2 129 ? -16.989 -1.490  -97.156  1.00 32.02  ? 129 LYS D CA  1 
ATOM   5538 C  C   . LYS D 2 129 ? -16.008 -0.496  -96.550  1.00 28.58  ? 129 LYS D C   1 
ATOM   5539 O  O   . LYS D 2 129 ? -16.341 0.188   -95.575  1.00 32.37  ? 129 LYS D O   1 
ATOM   5540 C  CB  . LYS D 2 129 ? -17.944 -0.734  -98.106  1.00 38.69  ? 129 LYS D CB  1 
ATOM   5541 C  CG  . LYS D 2 129 ? -18.840 -1.622  -98.971  1.00 42.70  ? 129 LYS D CG  1 
ATOM   5542 C  CD  . LYS D 2 129 ? -19.876 -0.812  -99.766  1.00 44.43  ? 129 LYS D CD  1 
ATOM   5543 C  CE  . LYS D 2 129 ? -20.362 -1.570  -101.012 1.00 45.81  ? 129 LYS D CE  1 
ATOM   5544 N  NZ  . LYS D 2 129 ? -21.121 -0.696  -101.968 1.00 62.71  ? 129 LYS D NZ  1 
ATOM   5545 N  N   . ILE D 2 130 ? -14.802 -0.416  -97.113  1.00 29.29  ? 130 ILE D N   1 
ATOM   5546 C  CA  . ILE D 2 130 ? -13.852 0.640   -96.769  1.00 29.52  ? 130 ILE D CA  1 
ATOM   5547 C  C   . ILE D 2 130 ? -14.019 1.758   -97.787  1.00 32.97  ? 130 ILE D C   1 
ATOM   5548 O  O   . ILE D 2 130 ? -13.873 1.524   -98.993  1.00 32.68  ? 130 ILE D O   1 
ATOM   5549 C  CB  . ILE D 2 130 ? -12.395 0.147   -96.764  1.00 39.47  ? 130 ILE D CB  1 
ATOM   5550 C  CG1 . ILE D 2 130 ? -12.187 -1.110  -95.914  1.00 31.47  ? 130 ILE D CG1 1 
ATOM   5551 C  CG2 . ILE D 2 130 ? -11.480 1.250   -96.296  1.00 33.13  ? 130 ILE D CG2 1 
ATOM   5552 C  CD1 . ILE D 2 130 ? -10.827 -1.816  -96.187  1.00 24.70  ? 130 ILE D CD1 1 
ATOM   5553 N  N   . VAL D 2 131 ? -14.311 2.972   -97.318  1.00 25.14  ? 131 VAL D N   1 
ATOM   5554 C  CA  . VAL D 2 131 ? -14.433 4.117   -98.206  1.00 27.50  ? 131 VAL D CA  1 
ATOM   5555 C  C   . VAL D 2 131 ? -13.500 5.229   -97.733  1.00 32.88  ? 131 VAL D C   1 
ATOM   5556 O  O   . VAL D 2 131 ? -13.098 5.299   -96.571  1.00 29.44  ? 131 VAL D O   1 
ATOM   5557 C  CB  . VAL D 2 131 ? -15.887 4.634   -98.312  1.00 30.19  ? 131 VAL D CB  1 
ATOM   5558 C  CG1 . VAL D 2 131 ? -16.835 3.499   -98.708  1.00 31.11  ? 131 VAL D CG1 1 
ATOM   5559 C  CG2 . VAL D 2 131 ? -16.321 5.277   -97.026  1.00 19.68  ? 131 VAL D CG2 1 
ATOM   5560 N  N   . LYS D 2 132 ? -13.151 6.110   -98.665  1.00 43.50  ? 132 LYS D N   1 
ATOM   5561 C  CA  . LYS D 2 132 ? -12.238 7.198   -98.351  1.00 45.03  ? 132 LYS D CA  1 
ATOM   5562 C  C   . LYS D 2 132 ? -12.987 8.267   -97.569  1.00 39.23  ? 132 LYS D C   1 
ATOM   5563 O  O   . LYS D 2 132 ? -14.113 8.636   -97.914  1.00 42.67  ? 132 LYS D O   1 
ATOM   5564 C  CB  . LYS D 2 132 ? -11.610 7.765   -99.627  1.00 39.68  ? 132 LYS D CB  1 
ATOM   5565 C  CG  . LYS D 2 132 ? -11.127 9.189   -99.504  1.00 50.51  ? 132 LYS D CG  1 
ATOM   5566 C  CD  . LYS D 2 132 ? -9.799  9.260   -98.769  1.00 49.47  ? 132 LYS D CD  1 
ATOM   5567 C  CE  . LYS D 2 132 ? -9.557  10.671  -98.246  1.00 55.01  ? 132 LYS D CE  1 
ATOM   5568 N  NZ  . LYS D 2 132 ? -8.707  10.690  -97.019  1.00 46.56  ? 132 LYS D NZ  1 
ATOM   5569 N  N   . SER D 2 133 ? -12.388 8.703   -96.473  1.00 39.73  ? 133 SER D N   1 
ATOM   5570 C  CA  . SER D 2 133 ? -12.995 9.676   -95.583  1.00 37.23  ? 133 SER D CA  1 
ATOM   5571 C  C   . SER D 2 133 ? -13.067 11.050  -96.249  1.00 48.27  ? 133 SER D C   1 
ATOM   5572 O  O   . SER D 2 133 ? -12.304 11.368  -97.160  1.00 47.17  ? 133 SER D O   1 
ATOM   5573 C  CB  . SER D 2 133 ? -12.176 9.746   -94.295  1.00 35.68  ? 133 SER D CB  1 
ATOM   5574 O  OG  . SER D 2 133 ? -12.405 10.932  -93.579  1.00 38.38  ? 133 SER D OG  1 
ATOM   5575 N  N   . SER D 2 134 ? -13.990 11.883  -95.770  1.00 44.62  ? 134 SER D N   1 
ATOM   5576 C  CA  . SER D 2 134 ? -13.978 13.273  -96.206  1.00 39.61  ? 134 SER D CA  1 
ATOM   5577 C  C   . SER D 2 134 ? -12.749 14.029  -95.708  1.00 53.91  ? 134 SER D C   1 
ATOM   5578 O  O   . SER D 2 134 ? -12.487 15.137  -96.197  1.00 57.23  ? 134 SER D O   1 
ATOM   5579 C  CB  . SER D 2 134 ? -15.237 14.001  -95.737  1.00 38.19  ? 134 SER D CB  1 
ATOM   5580 O  OG  . SER D 2 134 ? -15.214 14.202  -94.336  1.00 61.47  ? 134 SER D OG  1 
ATOM   5581 N  N   . LYS D 2 135 ? -11.997 13.465  -94.770  1.00 46.06  ? 135 LYS D N   1 
ATOM   5582 C  CA  . LYS D 2 135 ? -10.788 14.082  -94.226  1.00 42.66  ? 135 LYS D CA  1 
ATOM   5583 C  C   . LYS D 2 135 ? -9.594  13.181  -94.541  1.00 45.72  ? 135 LYS D C   1 
ATOM   5584 O  O   . LYS D 2 135 ? -9.489  12.719  -95.684  1.00 50.41  ? 135 LYS D O   1 
ATOM   5585 C  CB  . LYS D 2 135 ? -10.983 14.362  -92.741  1.00 51.03  ? 135 LYS D CB  1 
ATOM   5586 C  CG  . LYS D 2 135 ? -11.792 15.571  -92.389  1.00 56.47  ? 135 LYS D CG  1 
ATOM   5587 C  CD  . LYS D 2 135 ? -12.133 15.517  -90.914  1.00 52.80  ? 135 LYS D CD  1 
ATOM   5588 C  CE  . LYS D 2 135 ? -13.618 15.394  -90.712  1.00 66.37  ? 135 LYS D CE  1 
ATOM   5589 N  NZ  . LYS D 2 135 ? -14.284 16.636  -91.161  1.00 71.63  ? 135 LYS D NZ  1 
ATOM   5590 N  N   . PHE D 2 136 ? -8.685  12.927  -93.597  1.00 37.55  ? 136 PHE D N   1 
ATOM   5591 C  CA  . PHE D 2 136 ? -7.580  11.995  -93.783  1.00 39.94  ? 136 PHE D CA  1 
ATOM   5592 C  C   . PHE D 2 136 ? -8.026  10.584  -93.409  1.00 39.78  ? 136 PHE D C   1 
ATOM   5593 O  O   . PHE D 2 136 ? -8.785  10.400  -92.457  1.00 45.76  ? 136 PHE D O   1 
ATOM   5594 C  CB  . PHE D 2 136 ? -6.388  12.419  -92.919  1.00 42.07  ? 136 PHE D CB  1 
ATOM   5595 C  CG  . PHE D 2 136 ? -5.069  11.814  -93.341  1.00 51.62  ? 136 PHE D CG  1 
ATOM   5596 C  CD1 . PHE D 2 136 ? -4.665  11.839  -94.669  1.00 58.83  ? 136 PHE D CD1 1 
ATOM   5597 C  CD2 . PHE D 2 136 ? -4.246  11.183  -92.405  1.00 56.03  ? 136 PHE D CD2 1 
ATOM   5598 C  CE1 . PHE D 2 136 ? -3.453  11.277  -95.051  1.00 55.26  ? 136 PHE D CE1 1 
ATOM   5599 C  CE2 . PHE D 2 136 ? -3.037  10.608  -92.782  1.00 38.90  ? 136 PHE D CE2 1 
ATOM   5600 C  CZ  . PHE D 2 136 ? -2.642  10.656  -94.103  1.00 46.12  ? 136 PHE D CZ  1 
ATOM   5601 N  N   . GLY D 2 137 ? -7.555  9.591   -94.158  1.00 35.61  ? 137 GLY D N   1 
ATOM   5602 C  CA  . GLY D 2 137 ? -7.848  8.194   -93.841  1.00 36.63  ? 137 GLY D CA  1 
ATOM   5603 C  C   . GLY D 2 137 ? -9.101  7.622   -94.492  1.00 37.23  ? 137 GLY D C   1 
ATOM   5604 O  O   . GLY D 2 137 ? -9.648  8.148   -95.468  1.00 35.97  ? 137 GLY D O   1 
ATOM   5605 N  N   . TYR D 2 138 ? -9.562  6.507   -93.921  1.00 33.79  ? 138 TYR D N   1 
ATOM   5606 C  CA  . TYR D 2 138 ? -10.725 5.785   -94.422  1.00 31.04  ? 138 TYR D CA  1 
ATOM   5607 C  C   . TYR D 2 138 ? -11.800 5.674   -93.348  1.00 32.37  ? 138 TYR D C   1 
ATOM   5608 O  O   . TYR D 2 138 ? -11.524 5.774   -92.147  1.00 34.98  ? 138 TYR D O   1 
ATOM   5609 C  CB  . TYR D 2 138 ? -10.346 4.380   -94.874  1.00 29.50  ? 138 TYR D CB  1 
ATOM   5610 C  CG  . TYR D 2 138 ? -9.351  4.322   -96.010  1.00 37.50  ? 138 TYR D CG  1 
ATOM   5611 C  CD1 . TYR D 2 138 ? -9.771  4.343   -97.337  1.00 32.18  ? 138 TYR D CD1 1 
ATOM   5612 C  CD2 . TYR D 2 138 ? -7.988  4.245   -95.752  1.00 32.87  ? 138 TYR D CD2 1 
ATOM   5613 C  CE1 . TYR D 2 138 ? -8.867  4.273   -98.369  1.00 26.30  ? 138 TYR D CE1 1 
ATOM   5614 C  CE2 . TYR D 2 138 ? -7.076  4.179   -96.776  1.00 33.44  ? 138 TYR D CE2 1 
ATOM   5615 C  CZ  . TYR D 2 138 ? -7.522  4.194   -98.082  1.00 29.95  ? 138 TYR D CZ  1 
ATOM   5616 O  OH  . TYR D 2 138 ? -6.604  4.118   -99.088  1.00 29.60  ? 138 TYR D OH  1 
ATOM   5617 N  N   . ASN D 2 139 ? -13.032 5.452   -93.796  1.00 24.73  ? 139 ASN D N   1 
ATOM   5618 C  CA  . ASN D 2 139 ? -14.140 5.094   -92.926  1.00 25.95  ? 139 ASN D CA  1 
ATOM   5619 C  C   . ASN D 2 139 ? -14.614 3.690   -93.273  1.00 29.37  ? 139 ASN D C   1 
ATOM   5620 O  O   . ASN D 2 139 ? -14.484 3.241   -94.415  1.00 28.19  ? 139 ASN D O   1 
ATOM   5621 C  CB  . ASN D 2 139 ? -15.324 6.065   -93.059  1.00 24.00  ? 139 ASN D CB  1 
ATOM   5622 C  CG  . ASN D 2 139 ? -14.965 7.498   -92.691  1.00 34.91  ? 139 ASN D CG  1 
ATOM   5623 O  OD1 . ASN D 2 139 ? -15.464 8.436   -93.307  1.00 36.57  ? 139 ASN D OD1 1 
ATOM   5624 N  ND2 . ASN D 2 139 ? -14.097 7.675   -91.694  1.00 32.68  ? 139 ASN D ND2 1 
ATOM   5625 N  N   . LEU D 2 140 ? -15.169 2.999   -92.283  1.00 23.85  ? 140 LEU D N   1 
ATOM   5626 C  CA  . LEU D 2 140 ? -15.818 1.719   -92.516  1.00 24.40  ? 140 LEU D CA  1 
ATOM   5627 C  C   . LEU D 2 140 ? -17.316 1.917   -92.624  1.00 27.66  ? 140 LEU D C   1 
ATOM   5628 O  O   . LEU D 2 140 ? -17.888 2.828   -92.016  1.00 27.80  ? 140 LEU D O   1 
ATOM   5629 C  CB  . LEU D 2 140 ? -15.539 0.735   -91.385  1.00 32.54  ? 140 LEU D CB  1 
ATOM   5630 C  CG  . LEU D 2 140 ? -14.058 0.478   -91.191  1.00 33.63  ? 140 LEU D CG  1 
ATOM   5631 C  CD1 . LEU D 2 140 ? -13.868 -0.488  -90.025  1.00 38.22  ? 140 LEU D CD1 1 
ATOM   5632 C  CD2 . LEU D 2 140 ? -13.486 -0.069  -92.496  1.00 34.84  ? 140 LEU D CD2 1 
ATOM   5633 N  N   . LEU D 2 141 ? -17.949 1.029   -93.379  1.00 29.49  ? 141 LEU D N   1 
ATOM   5634 C  CA  . LEU D 2 141 ? -19.369 1.113   -93.666  1.00 26.36  ? 141 LEU D CA  1 
ATOM   5635 C  C   . LEU D 2 141 ? -19.993 -0.254  -93.462  1.00 23.20  ? 141 LEU D C   1 
ATOM   5636 O  O   . LEU D 2 141 ? -19.535 -1.237  -94.048  1.00 29.42  ? 141 LEU D O   1 
ATOM   5637 C  CB  . LEU D 2 141 ? -19.619 1.561   -95.107  1.00 33.75  ? 141 LEU D CB  1 
ATOM   5638 C  CG  . LEU D 2 141 ? -19.585 3.039   -95.513  1.00 43.78  ? 141 LEU D CG  1 
ATOM   5639 C  CD1 . LEU D 2 141 ? -20.323 3.189   -96.845  1.00 30.89  ? 141 LEU D CD1 1 
ATOM   5640 C  CD2 . LEU D 2 141 ? -20.132 3.985   -94.445  1.00 34.80  ? 141 LEU D CD2 1 
ATOM   5641 N  N   . TYR D 2 142 ? -21.044 -0.318  -92.656  1.00 26.65  ? 142 TYR D N   1 
ATOM   5642 C  CA  . TYR D 2 142 ? -21.851 -1.523  -92.593  1.00 26.43  ? 142 TYR D CA  1 
ATOM   5643 C  C   . TYR D 2 142 ? -22.912 -1.442  -93.670  1.00 25.62  ? 142 TYR D C   1 
ATOM   5644 O  O   . TYR D 2 142 ? -23.504 -0.382  -93.890  1.00 33.76  ? 142 TYR D O   1 
ATOM   5645 C  CB  . TYR D 2 142 ? -22.504 -1.694  -91.227  1.00 23.55  ? 142 TYR D CB  1 
ATOM   5646 C  CG  . TYR D 2 142 ? -23.540 -2.783  -91.214  1.00 24.19  ? 142 TYR D CG  1 
ATOM   5647 C  CD1 . TYR D 2 142 ? -23.184 -4.105  -91.439  1.00 21.27  ? 142 TYR D CD1 1 
ATOM   5648 C  CD2 . TYR D 2 142 ? -24.873 -2.492  -90.992  1.00 30.38  ? 142 TYR D CD2 1 
ATOM   5649 C  CE1 . TYR D 2 142 ? -24.121 -5.101  -91.445  1.00 27.07  ? 142 TYR D CE1 1 
ATOM   5650 C  CE2 . TYR D 2 142 ? -25.825 -3.491  -90.984  1.00 32.05  ? 142 TYR D CE2 1 
ATOM   5651 C  CZ  . TYR D 2 142 ? -25.445 -4.791  -91.217  1.00 33.76  ? 142 TYR D CZ  1 
ATOM   5652 O  OH  . TYR D 2 142 ? -26.394 -5.785  -91.200  1.00 30.85  ? 142 TYR D OH  1 
ATOM   5653 N  N   . CYS D 2 143 ? -23.156 -2.560  -94.349  1.00 27.59  ? 143 CYS D N   1 
ATOM   5654 C  CA  . CYS D 2 143 ? -24.057 -2.567  -95.501  1.00 36.95  ? 143 CYS D CA  1 
ATOM   5655 C  C   . CYS D 2 143 ? -24.978 -3.768  -95.421  1.00 31.40  ? 143 CYS D C   1 
ATOM   5656 O  O   . CYS D 2 143 ? -24.589 -4.881  -95.807  1.00 38.35  ? 143 CYS D O   1 
ATOM   5657 C  CB  . CYS D 2 143 ? -23.279 -2.573  -96.813  1.00 38.80  ? 143 CYS D CB  1 
ATOM   5658 S  SG  . CYS D 2 143 ? -22.422 -1.003  -97.164  1.00 61.65  ? 143 CYS D SG  1 
ATOM   5659 N  N   . PRO D 2 144 ? -26.199 -3.588  -94.925  1.00 35.69  ? 144 PRO D N   1 
ATOM   5660 C  CA  . PRO D 2 144 ? -27.166 -4.696  -94.893  1.00 36.43  ? 144 PRO D CA  1 
ATOM   5661 C  C   . PRO D 2 144 ? -27.381 -5.287  -96.277  1.00 34.96  ? 144 PRO D C   1 
ATOM   5662 O  O   . PRO D 2 144 ? -27.192 -4.632  -97.301  1.00 45.16  ? 144 PRO D O   1 
ATOM   5663 C  CB  . PRO D 2 144 ? -28.447 -4.030  -94.383  1.00 27.90  ? 144 PRO D CB  1 
ATOM   5664 C  CG  . PRO D 2 144 ? -27.958 -2.868  -93.582  1.00 38.52  ? 144 PRO D CG  1 
ATOM   5665 C  CD  . PRO D 2 144 ? -26.745 -2.358  -94.328  1.00 32.58  ? 144 PRO D CD  1 
ATOM   5666 N  N   . LEU D 2 145 ? -27.804 -6.540  -96.303  1.00 42.36  ? 145 LEU D N   1 
ATOM   5667 C  CA  . LEU D 2 145 ? -28.127 -7.174  -97.573  1.00 40.12  ? 145 LEU D CA  1 
ATOM   5668 C  C   . LEU D 2 145 ? -29.641 -7.226  -97.797  1.00 39.65  ? 145 LEU D C   1 
ATOM   5669 O  O   . LEU D 2 145 ? -30.198 -6.418  -98.545  1.00 43.71  ? 145 LEU D O   1 
ATOM   5670 C  CB  . LEU D 2 145 ? -27.533 -8.573  -97.613  1.00 38.19  ? 145 LEU D CB  1 
ATOM   5671 C  CG  . LEU D 2 145 ? -26.269 -8.754  -98.444  1.00 36.68  ? 145 LEU D CG  1 
ATOM   5672 C  CD1 . LEU D 2 145 ? -25.231 -7.692  -98.096  1.00 33.95  ? 145 LEU D CD1 1 
ATOM   5673 C  CD2 . LEU D 2 145 ? -25.722 -10.150 -98.177  1.00 33.81  ? 145 LEU D CD2 1 
ATOM   5674 N  N   . PHE D 2 159 ? -27.554 3.014   -98.743  1.00 55.03  ? 159 PHE D N   1 
ATOM   5675 C  CA  . PHE D 2 159 ? -28.328 2.453   -97.631  1.00 64.47  ? 159 PHE D CA  1 
ATOM   5676 C  C   . PHE D 2 159 ? -27.422 1.785   -96.603  1.00 59.44  ? 159 PHE D C   1 
ATOM   5677 O  O   . PHE D 2 159 ? -27.790 0.800   -95.959  1.00 62.03  ? 159 PHE D O   1 
ATOM   5678 C  CB  . PHE D 2 159 ? -29.357 1.439   -98.135  1.00 67.88  ? 159 PHE D CB  1 
ATOM   5679 C  CG  . PHE D 2 159 ? -30.164 1.922   -99.305  1.00 83.37  ? 159 PHE D CG  1 
ATOM   5680 C  CD1 . PHE D 2 159 ? -30.849 3.129   -99.243  1.00 81.95  ? 159 PHE D CD1 1 
ATOM   5681 C  CD2 . PHE D 2 159 ? -30.245 1.165   -100.466 1.00 87.95  ? 159 PHE D CD2 1 
ATOM   5682 C  CE1 . PHE D 2 159 ? -31.599 3.574   -100.322 1.00 81.08  ? 159 PHE D CE1 1 
ATOM   5683 C  CE2 . PHE D 2 159 ? -30.989 1.601   -101.549 1.00 86.07  ? 159 PHE D CE2 1 
ATOM   5684 C  CZ  . PHE D 2 159 ? -31.669 2.808   -101.477 1.00 94.00  ? 159 PHE D CZ  1 
ATOM   5685 N  N   . CYS D 2 160 ? -26.230 2.327   -96.458  1.00 38.04  ? 160 CYS D N   1 
ATOM   5686 C  CA  . CYS D 2 160 ? -25.237 1.789   -95.552  1.00 43.87  ? 160 CYS D CA  1 
ATOM   5687 C  C   . CYS D 2 160 ? -25.130 2.698   -94.334  1.00 41.11  ? 160 CYS D C   1 
ATOM   5688 O  O   . CYS D 2 160 ? -25.738 3.768   -94.270  1.00 52.10  ? 160 CYS D O   1 
ATOM   5689 C  CB  . CYS D 2 160 ? -23.888 1.634   -96.274  1.00 39.47  ? 160 CYS D CB  1 
ATOM   5690 S  SG  . CYS D 2 160 ? -23.915 0.360   -97.603  1.00 66.83  ? 160 CYS D SG  1 
ATOM   5691 N  N   . ALA D 2 161 ? -24.367 2.256   -93.343  1.00 39.24  ? 161 ALA D N   1 
ATOM   5692 C  CA  . ALA D 2 161 ? -24.248 2.996   -92.098  1.00 34.88  ? 161 ALA D CA  1 
ATOM   5693 C  C   . ALA D 2 161 ? -22.779 3.153   -91.737  1.00 26.89  ? 161 ALA D C   1 
ATOM   5694 O  O   . ALA D 2 161 ? -22.017 2.185   -91.785  1.00 29.18  ? 161 ALA D O   1 
ATOM   5695 C  CB  . ALA D 2 161 ? -25.023 2.296   -90.973  1.00 23.81  ? 161 ALA D CB  1 
ATOM   5696 N  N   . LYS D 2 162 ? -22.388 4.376   -91.388  1.00 31.06  ? 162 LYS D N   1 
ATOM   5697 C  CA  . LYS D 2 162 ? -21.019 4.661   -90.990  1.00 34.99  ? 162 LYS D CA  1 
ATOM   5698 C  C   . LYS D 2 162 ? -20.687 4.025   -89.635  1.00 31.93  ? 162 LYS D C   1 
ATOM   5699 O  O   . LYS D 2 162 ? -21.530 3.903   -88.743  1.00 28.69  ? 162 LYS D O   1 
ATOM   5700 C  CB  . LYS D 2 162 ? -20.800 6.173   -90.930  1.00 42.69  ? 162 LYS D CB  1 
ATOM   5701 C  CG  . LYS D 2 162 ? -20.649 6.841   -92.290  1.00 48.00  ? 162 LYS D CG  1 
ATOM   5702 C  CD  . LYS D 2 162 ? -20.844 8.356   -92.216  1.00 54.43  ? 162 LYS D CD  1 
ATOM   5703 C  CE  . LYS D 2 162 ? -21.610 8.877   -93.444  1.00 53.88  ? 162 LYS D CE  1 
ATOM   5704 N  NZ  . LYS D 2 162 ? -20.791 9.752   -94.340  1.00 50.74  ? 162 LYS D NZ  1 
ATOM   5705 N  N   . VAL D 2 163 ? -19.446 3.600   -89.487  1.00 26.55  ? 163 VAL D N   1 
ATOM   5706 C  CA  . VAL D 2 163 ? -18.969 3.056   -88.226  1.00 22.83  ? 163 VAL D CA  1 
ATOM   5707 C  C   . VAL D 2 163 ? -18.268 4.164   -87.467  1.00 16.49  ? 163 VAL D C   1 
ATOM   5708 O  O   . VAL D 2 163 ? -17.401 4.850   -88.015  1.00 24.76  ? 163 VAL D O   1 
ATOM   5709 C  CB  . VAL D 2 163 ? -18.028 1.865   -88.445  1.00 32.03  ? 163 VAL D CB  1 
ATOM   5710 C  CG1 . VAL D 2 163 ? -17.442 1.413   -87.099  1.00 21.56  ? 163 VAL D CG1 1 
ATOM   5711 C  CG2 . VAL D 2 163 ? -18.756 0.726   -89.193  1.00 27.90  ? 163 VAL D CG2 1 
ATOM   5712 N  N   . GLY D 2 164 ? -18.676 4.366   -86.227  1.00 24.36  ? 164 GLY D N   1 
ATOM   5713 C  CA  . GLY D 2 164 ? -18.027 5.296   -85.334  1.00 15.98  ? 164 GLY D CA  1 
ATOM   5714 C  C   . GLY D 2 164 ? -17.947 4.712   -83.943  1.00 21.27  ? 164 GLY D C   1 
ATOM   5715 O  O   . GLY D 2 164 ? -17.764 3.505   -83.777  1.00 27.84  ? 164 GLY D O   1 
ATOM   5716 N  N   . VAL D 2 165 ? -18.090 5.548   -82.929  1.00 22.24  ? 165 VAL D N   1 
ATOM   5717 C  CA  . VAL D 2 165 ? -17.792 5.152   -81.567  1.00 19.96  ? 165 VAL D CA  1 
ATOM   5718 C  C   . VAL D 2 165 ? -18.865 5.715   -80.648  1.00 26.36  ? 165 VAL D C   1 
ATOM   5719 O  O   . VAL D 2 165 ? -19.264 6.876   -80.774  1.00 18.70  ? 165 VAL D O   1 
ATOM   5720 C  CB  . VAL D 2 165 ? -16.399 5.641   -81.142  1.00 21.62  ? 165 VAL D CB  1 
ATOM   5721 C  CG1 . VAL D 2 165 ? -16.235 5.575   -79.626  1.00 15.56  ? 165 VAL D CG1 1 
ATOM   5722 C  CG2 . VAL D 2 165 ? -15.335 4.842   -81.848  1.00 19.15  ? 165 VAL D CG2 1 
ATOM   5723 N  N   . VAL D 2 166 ? -19.347 4.888   -79.746  1.00 23.34  ? 166 VAL D N   1 
ATOM   5724 C  CA  . VAL D 2 166 ? -20.200 5.331   -78.664  1.00 22.94  ? 166 VAL D CA  1 
ATOM   5725 C  C   . VAL D 2 166 ? -19.476 4.936   -77.391  1.00 30.35  ? 166 VAL D C   1 
ATOM   5726 O  O   . VAL D 2 166 ? -18.684 3.981   -77.375  1.00 25.81  ? 166 VAL D O   1 
ATOM   5727 C  CB  . VAL D 2 166 ? -21.591 4.666   -78.739  1.00 29.15  ? 166 VAL D CB  1 
ATOM   5728 C  CG1 . VAL D 2 166 ? -22.405 5.246   -79.872  1.00 16.93  ? 166 VAL D CG1 1 
ATOM   5729 C  CG2 . VAL D 2 166 ? -21.447 3.159   -78.882  1.00 29.97  ? 166 VAL D CG2 1 
ATOM   5730 N  N   . ILE D 2 167 ? -19.730 5.666   -76.322  1.00 28.01  ? 167 ILE D N   1 
ATOM   5731 C  CA  . ILE D 2 167 ? -19.124 5.323   -75.041  1.00 27.01  ? 167 ILE D CA  1 
ATOM   5732 C  C   . ILE D 2 167 ? -20.029 4.304   -74.362  1.00 25.48  ? 167 ILE D C   1 
ATOM   5733 O  O   . ILE D 2 167 ? -21.205 4.568   -74.102  1.00 38.33  ? 167 ILE D O   1 
ATOM   5734 C  CB  . ILE D 2 167 ? -18.897 6.573   -74.178  1.00 23.85  ? 167 ILE D CB  1 
ATOM   5735 C  CG1 . ILE D 2 167 ? -17.907 7.482   -74.885  1.00 29.10  ? 167 ILE D CG1 1 
ATOM   5736 C  CG2 . ILE D 2 167 ? -18.340 6.208   -72.818  1.00 24.26  ? 167 ILE D CG2 1 
ATOM   5737 C  CD1 . ILE D 2 167 ? -16.705 6.730   -75.456  1.00 28.40  ? 167 ILE D CD1 1 
ATOM   5738 N  N   . GLN D 2 168 ? -19.504 3.120   -74.133  1.00 25.39  ? 168 GLN D N   1 
ATOM   5739 C  CA  . GLN D 2 168 ? -20.239 2.061   -73.465  1.00 28.07  ? 168 GLN D CA  1 
ATOM   5740 C  C   . GLN D 2 168 ? -19.458 1.678   -72.219  1.00 27.39  ? 168 GLN D C   1 
ATOM   5741 O  O   . GLN D 2 168 ? -18.340 1.162   -72.318  1.00 27.81  ? 168 GLN D O   1 
ATOM   5742 C  CB  . GLN D 2 168 ? -20.433 0.863   -74.388  1.00 20.33  ? 168 GLN D CB  1 
ATOM   5743 C  CG  . GLN D 2 168 ? -21.253 -0.240  -73.756  1.00 27.97  ? 168 GLN D CG  1 
ATOM   5744 C  CD  . GLN D 2 168 ? -21.033 -1.581  -74.427  1.00 31.63  ? 168 GLN D CD  1 
ATOM   5745 O  OE1 . GLN D 2 168 ? -19.980 -1.828  -75.015  1.00 34.24  ? 168 GLN D OE1 1 
ATOM   5746 N  NE2 . GLN D 2 168 ? -22.025 -2.450  -74.347  1.00 30.34  ? 168 GLN D NE2 1 
ATOM   5747 N  N   . ASN D 2 169 ? -20.043 1.940   -71.056  1.00 21.42  ? 169 ASN D N   1 
ATOM   5748 C  CA  . ASN D 2 169 ? -19.455 1.572   -69.769  1.00 27.95  ? 169 ASN D CA  1 
ATOM   5749 C  C   . ASN D 2 169 ? -18.046 2.148   -69.611  1.00 29.54  ? 169 ASN D C   1 
ATOM   5750 O  O   . ASN D 2 169 ? -17.098 1.454   -69.223  1.00 26.30  ? 169 ASN D O   1 
ATOM   5751 C  CB  . ASN D 2 169 ? -19.472 0.056   -69.599  1.00 22.14  ? 169 ASN D CB  1 
ATOM   5752 C  CG  . ASN D 2 169 ? -20.876 -0.507  -69.680  1.00 40.99  ? 169 ASN D CG  1 
ATOM   5753 O  OD1 . ASN D 2 169 ? -21.298 -1.006  -70.725  1.00 45.91  ? 169 ASN D OD1 1 
ATOM   5754 N  ND2 . ASN D 2 169 ? -21.612 -0.435  -68.574  1.00 38.69  ? 169 ASN D ND2 1 
ATOM   5755 N  N   . GLY D 2 170 ? -17.923 3.446   -69.905  1.00 27.00  ? 170 GLY D N   1 
ATOM   5756 C  CA  . GLY D 2 170 ? -16.655 4.143   -69.869  1.00 27.79  ? 170 GLY D CA  1 
ATOM   5757 C  C   . GLY D 2 170 ? -15.744 3.882   -71.047  1.00 30.05  ? 170 GLY D C   1 
ATOM   5758 O  O   . GLY D 2 170 ? -14.841 4.689   -71.303  1.00 37.36  ? 170 GLY D O   1 
ATOM   5759 N  N   . LYS D 2 171 ? -15.966 2.801   -71.783  1.00 25.03  ? 171 LYS D N   1 
ATOM   5760 C  CA  . LYS D 2 171 ? -15.101 2.352   -72.859  1.00 25.29  ? 171 LYS D CA  1 
ATOM   5761 C  C   . LYS D 2 171 ? -15.573 2.902   -74.200  1.00 28.32  ? 171 LYS D C   1 
ATOM   5762 O  O   . LYS D 2 171 ? -16.710 3.343   -74.353  1.00 28.12  ? 171 LYS D O   1 
ATOM   5763 C  CB  . LYS D 2 171 ? -15.066 0.825   -72.917  1.00 26.95  ? 171 LYS D CB  1 
ATOM   5764 C  CG  . LYS D 2 171 ? -14.200 0.174   -71.869  1.00 30.66  ? 171 LYS D CG  1 
ATOM   5765 C  CD  . LYS D 2 171 ? -14.136 -1.337  -72.062  1.00 39.51  ? 171 LYS D CD  1 
ATOM   5766 C  CE  . LYS D 2 171 ? -13.464 -2.003  -70.854  1.00 51.62  ? 171 LYS D CE  1 
ATOM   5767 N  NZ  . LYS D 2 171 ? -12.339 -1.160  -70.321  1.00 54.44  ? 171 LYS D NZ  1 
ATOM   5768 N  N   . ARG D 2 172 ? -14.677 2.842   -75.180  1.00 22.55  ? 172 ARG D N   1 
ATOM   5769 C  CA  . ARG D 2 172 ? -14.926 3.302   -76.542  1.00 21.04  ? 172 ARG D CA  1 
ATOM   5770 C  C   . ARG D 2 172 ? -15.383 2.120   -77.390  1.00 25.27  ? 172 ARG D C   1 
ATOM   5771 O  O   . ARG D 2 172 ? -14.561 1.345   -77.886  1.00 30.55  ? 172 ARG D O   1 
ATOM   5772 C  CB  . ARG D 2 172 ? -13.660 3.939   -77.108  1.00 26.92  ? 172 ARG D CB  1 
ATOM   5773 C  CG  . ARG D 2 172 ? -13.389 5.420   -76.738  1.00 15.89  ? 172 ARG D CG  1 
ATOM   5774 C  CD  . ARG D 2 172 ? -12.003 5.837   -77.280  1.00 14.49  ? 172 ARG D CD  1 
ATOM   5775 N  NE  . ARG D 2 172 ? -11.495 7.000   -76.562  1.00 22.94  ? 172 ARG D NE  1 
ATOM   5776 C  CZ  . ARG D 2 172 ? -10.358 7.632   -76.830  1.00 26.42  ? 172 ARG D CZ  1 
ATOM   5777 N  NH1 . ARG D 2 172 ? -9.427  7.088   -77.602  1.00 18.79  ? 172 ARG D NH1 1 
ATOM   5778 N  NH2 . ARG D 2 172 ? -10.140 8.831   -76.289  1.00 26.04  ? 172 ARG D NH2 1 
ATOM   5779 N  N   . ARG D 2 173 ? -16.692 1.984   -77.591  1.00 25.38  ? 173 ARG D N   1 
ATOM   5780 C  CA  . ARG D 2 173 ? -17.236 0.874   -78.370  1.00 20.54  ? 173 ARG D CA  1 
ATOM   5781 C  C   . ARG D 2 173 ? -17.525 1.286   -79.815  1.00 25.20  ? 173 ARG D C   1 
ATOM   5782 O  O   . ARG D 2 173 ? -18.239 2.261   -80.072  1.00 23.07  ? 173 ARG D O   1 
ATOM   5783 C  CB  . ARG D 2 173 ? -18.514 0.326   -77.732  1.00 28.91  ? 173 ARG D CB  1 
ATOM   5784 C  CG  . ARG D 2 173 ? -19.132 -0.863  -78.507  1.00 26.71  ? 173 ARG D CG  1 
ATOM   5785 C  CD  . ARG D 2 173 ? -18.292 -2.135  -78.326  1.00 19.78  ? 173 ARG D CD  1 
ATOM   5786 N  NE  . ARG D 2 173 ? -18.892 -3.317  -78.941  1.00 25.36  ? 173 ARG D NE  1 
ATOM   5787 C  CZ  . ARG D 2 173 ? -19.691 -4.160  -78.296  1.00 27.50  ? 173 ARG D CZ  1 
ATOM   5788 N  NH1 . ARG D 2 173 ? -20.081 -3.925  -77.051  1.00 22.80  ? 173 ARG D NH1 1 
ATOM   5789 N  NH2 . ARG D 2 173 ? -20.109 -5.265  -78.912  1.00 25.55  ? 173 ARG D NH2 1 
ATOM   5790 N  N   . LEU D 2 174 ? -16.992 0.527   -80.758  1.00 24.40  ? 174 LEU D N   1 
ATOM   5791 C  CA  . LEU D 2 174 ? -17.348 0.755   -82.145  1.00 25.55  ? 174 LEU D CA  1 
ATOM   5792 C  C   . LEU D 2 174 ? -18.812 0.398   -82.372  1.00 27.03  ? 174 LEU D C   1 
ATOM   5793 O  O   . LEU D 2 174 ? -19.305 -0.637  -81.908  1.00 25.03  ? 174 LEU D O   1 
ATOM   5794 C  CB  . LEU D 2 174 ? -16.445 -0.059  -83.060  1.00 21.03  ? 174 LEU D CB  1 
ATOM   5795 C  CG  . LEU D 2 174 ? -15.216 0.744   -83.445  1.00 25.95  ? 174 LEU D CG  1 
ATOM   5796 C  CD1 . LEU D 2 174 ? -14.212 0.758   -82.307  1.00 30.37  ? 174 LEU D CD1 1 
ATOM   5797 C  CD2 . LEU D 2 174 ? -14.600 0.126   -84.662  1.00 23.92  ? 174 LEU D CD2 1 
ATOM   5798 N  N   . ALA D 2 175 ? -19.504 1.265   -83.098  1.00 21.90  ? 175 ALA D N   1 
ATOM   5799 C  CA  . ALA D 2 175 ? -20.943 1.137   -83.284  1.00 30.84  ? 175 ALA D CA  1 
ATOM   5800 C  C   . ALA D 2 175 ? -21.321 1.872   -84.559  1.00 30.73  ? 175 ALA D C   1 
ATOM   5801 O  O   . ALA D 2 175 ? -20.518 2.625   -85.123  1.00 33.12  ? 175 ALA D O   1 
ATOM   5802 C  CB  . ALA D 2 175 ? -21.707 1.700   -82.079  1.00 24.67  ? 175 ALA D CB  1 
ATOM   5803 N  N   . LEU D 2 176 ? -22.550 1.643   -85.020  1.00 29.95  ? 176 LEU D N   1 
ATOM   5804 C  CA  . LEU D 2 176 ? -23.061 2.362   -86.183  1.00 25.09  ? 176 LEU D CA  1 
ATOM   5805 C  C   . LEU D 2 176 ? -23.468 3.764   -85.753  1.00 26.72  ? 176 LEU D C   1 
ATOM   5806 O  O   . LEU D 2 176 ? -24.305 3.921   -84.855  1.00 28.47  ? 176 LEU D O   1 
ATOM   5807 C  CB  . LEU D 2 176 ? -24.251 1.631   -86.785  1.00 22.13  ? 176 LEU D CB  1 
ATOM   5808 C  CG  . LEU D 2 176 ? -23.894 0.265   -87.343  1.00 30.64  ? 176 LEU D CG  1 
ATOM   5809 C  CD1 . LEU D 2 176 ? -25.106 -0.318  -88.049  1.00 26.78  ? 176 LEU D CD1 1 
ATOM   5810 C  CD2 . LEU D 2 176 ? -22.693 0.379   -88.267  1.00 24.95  ? 176 LEU D CD2 1 
ATOM   5811 N  N   . VAL D 2 177 ? -22.839 4.780   -86.341  1.00 25.25  ? 177 VAL D N   1 
ATOM   5812 C  CA  . VAL D 2 177 ? -23.206 6.177   -86.111  1.00 36.91  ? 177 VAL D CA  1 
ATOM   5813 C  C   . VAL D 2 177 ? -23.128 6.852   -87.474  1.00 44.99  ? 177 VAL D C   1 
ATOM   5814 O  O   . VAL D 2 177 ? -22.053 6.898   -88.080  1.00 59.38  ? 177 VAL D O   1 
ATOM   5815 C  CB  . VAL D 2 177 ? -22.302 6.897   -85.076  1.00 33.03  ? 177 VAL D CB  1 
ATOM   5816 C  CG1 . VAL D 2 177 ? -22.233 6.138   -83.756  1.00 34.43  ? 177 VAL D CG1 1 
ATOM   5817 C  CG2 . VAL D 2 177 ? -20.901 7.128   -85.568  1.00 45.96  ? 177 VAL D CG2 1 
ATOM   5818 N  N   . ASN D 2 178 ? -24.260 7.331   -87.993  1.00 35.83  ? 178 ASN D N   1 
ATOM   5819 C  CA  . ASN D 2 178 ? -24.191 8.033   -89.272  1.00 57.50  ? 178 ASN D CA  1 
ATOM   5820 C  C   . ASN D 2 178 ? -24.042 9.539   -89.114  1.00 51.63  ? 178 ASN D C   1 
ATOM   5821 O  O   . ASN D 2 178 ? -24.450 10.303  -89.995  1.00 69.40  ? 178 ASN D O   1 
ATOM   5822 C  CB  . ASN D 2 178 ? -25.381 7.693   -90.168  1.00 62.57  ? 178 ASN D CB  1 
ATOM   5823 C  CG  . ASN D 2 178 ? -25.041 6.607   -91.196  1.00 57.80  ? 178 ASN D CG  1 
ATOM   5824 O  OD1 . ASN D 2 178 ? -24.059 6.715   -91.942  1.00 58.54  ? 178 ASN D OD1 1 
ATOM   5825 N  ND2 . ASN D 2 178 ? -25.876 5.580   -91.265  1.00 68.00  ? 178 ASN D ND2 1 
ATOM   5826 N  N   . GLU D 2 179 ? -23.458 9.978   -88.017  1.00 42.01  ? 179 GLU D N   1 
ATOM   5827 C  CA  . GLU D 2 179 ? -22.797 11.265  -87.924  1.00 44.96  ? 179 GLU D CA  1 
ATOM   5828 C  C   . GLU D 2 179 ? -21.465 10.994  -87.236  1.00 42.17  ? 179 GLU D C   1 
ATOM   5829 O  O   . GLU D 2 179 ? -21.380 10.115  -86.376  1.00 46.98  ? 179 GLU D O   1 
ATOM   5830 C  CB  . GLU D 2 179 ? -23.672 12.283  -87.149  1.00 51.20  ? 179 GLU D CB  1 
ATOM   5831 C  CG  . GLU D 2 179 ? -23.402 13.772  -87.436  1.00 64.68  ? 179 GLU D CG  1 
ATOM   5832 C  CD  . GLU D 2 179 ? -24.136 14.728  -86.469  1.00 85.57  ? 179 GLU D CD  1 
ATOM   5833 O  OE1 . GLU D 2 179 ? -25.294 14.428  -86.093  1.00 83.00  ? 179 GLU D OE1 1 
ATOM   5834 O  OE2 . GLU D 2 179 ? -23.571 15.788  -86.102  1.00 75.08  ? 179 GLU D OE2 1 
ATOM   5835 N  N   . ASN D 2 180 ? -20.421 11.690  -87.652  1.00 37.44  ? 180 ASN D N   1 
ATOM   5836 C  CA  . ASN D 2 180 ? -19.113 11.568  -87.009  1.00 39.85  ? 180 ASN D CA  1 
ATOM   5837 C  C   . ASN D 2 180 ? -18.512 10.167  -87.107  1.00 42.65  ? 180 ASN D C   1 
ATOM   5838 O  O   . ASN D 2 180 ? -18.297 9.523   -86.074  1.00 43.81  ? 180 ASN D O   1 
ATOM   5839 C  CB  . ASN D 2 180 ? -19.211 11.963  -85.532  1.00 45.77  ? 180 ASN D CB  1 
ATOM   5840 C  CG  . ASN D 2 180 ? -17.866 12.318  -84.932  1.00 53.47  ? 180 ASN D CG  1 
ATOM   5841 O  OD1 . ASN D 2 180 ? -16.876 12.478  -85.651  1.00 57.84  ? 180 ASN D OD1 1 
ATOM   5842 N  ND2 . ASN D 2 180 ? -17.812 12.404  -83.601  1.00 50.07  ? 180 ASN D ND2 1 
ATOM   5843 N  N   . PRO D 2 181 ? -18.211 9.661   -88.301  1.00 33.71  ? 181 PRO D N   1 
ATOM   5844 C  CA  . PRO D 2 181 ? -17.503 8.381   -88.397  1.00 34.93  ? 181 PRO D CA  1 
ATOM   5845 C  C   . PRO D 2 181 ? -16.063 8.492   -87.924  1.00 30.41  ? 181 PRO D C   1 
ATOM   5846 O  O   . PRO D 2 181 ? -15.440 9.550   -87.964  1.00 32.18  ? 181 PRO D O   1 
ATOM   5847 C  CB  . PRO D 2 181 ? -17.551 8.061   -89.894  1.00 40.70  ? 181 PRO D CB  1 
ATOM   5848 C  CG  . PRO D 2 181 ? -17.640 9.393   -90.541  1.00 39.76  ? 181 PRO D CG  1 
ATOM   5849 C  CD  . PRO D 2 181 ? -18.524 10.206  -89.630  1.00 34.67  ? 181 PRO D CD  1 
ATOM   5850 N  N   . LEU D 2 182 ? -15.526 7.352   -87.507  1.00 28.10  ? 182 LEU D N   1 
ATOM   5851 C  CA  . LEU D 2 182 ? -14.122 7.245   -87.124  1.00 26.97  ? 182 LEU D CA  1 
ATOM   5852 C  C   . LEU D 2 182 ? -13.239 7.230   -88.376  1.00 29.62  ? 182 LEU D C   1 
ATOM   5853 O  O   . LEU D 2 182 ? -13.418 6.387   -89.261  1.00 25.96  ? 182 LEU D O   1 
ATOM   5854 C  CB  . LEU D 2 182 ? -13.920 5.973   -86.292  1.00 26.25  ? 182 LEU D CB  1 
ATOM   5855 C  CG  . LEU D 2 182 ? -12.586 5.702   -85.579  1.00 27.21  ? 182 LEU D CG  1 
ATOM   5856 C  CD1 . LEU D 2 182 ? -12.346 6.706   -84.489  1.00 20.33  ? 182 LEU D CD1 1 
ATOM   5857 C  CD2 . LEU D 2 182 ? -12.558 4.305   -84.999  1.00 17.50  ? 182 LEU D CD2 1 
ATOM   5858 N  N   . ASP D 2 183 ? -12.291 8.159   -88.465  1.00 29.83  ? 183 ASP D N   1 
ATOM   5859 C  CA  . ASP D 2 183 ? -11.282 8.091   -89.518  1.00 31.38  ? 183 ASP D CA  1 
ATOM   5860 C  C   . ASP D 2 183 ? -10.158 7.166   -89.066  1.00 27.20  ? 183 ASP D C   1 
ATOM   5861 O  O   . ASP D 2 183 ? -9.577  7.376   -87.998  1.00 31.21  ? 183 ASP D O   1 
ATOM   5862 C  CB  . ASP D 2 183 ? -10.743 9.484   -89.844  1.00 24.75  ? 183 ASP D CB  1 
ATOM   5863 C  CG  . ASP D 2 183 ? -11.844 10.476  -90.179  1.00 41.15  ? 183 ASP D CG  1 
ATOM   5864 O  OD1 . ASP D 2 183 ? -12.946 10.047  -90.607  1.00 42.91  ? 183 ASP D OD1 1 
ATOM   5865 O  OD2 . ASP D 2 183 ? -11.611 11.697  -89.997  1.00 48.08  ? 183 ASP D OD2 1 
ATOM   5866 N  N   . VAL D 2 184 ? -9.842  6.149   -89.873  1.00 25.56  ? 184 VAL D N   1 
ATOM   5867 C  CA  . VAL D 2 184 ? -8.857  5.132   -89.509  1.00 24.36  ? 184 VAL D CA  1 
ATOM   5868 C  C   . VAL D 2 184 ? -7.827  4.949   -90.619  1.00 28.88  ? 184 VAL D C   1 
ATOM   5869 O  O   . VAL D 2 184 ? -7.995  5.396   -91.758  1.00 23.48  ? 184 VAL D O   1 
ATOM   5870 C  CB  . VAL D 2 184 ? -9.507  3.769   -89.194  1.00 23.21  ? 184 VAL D CB  1 
ATOM   5871 C  CG1 . VAL D 2 184 ? -10.539 3.916   -88.095  1.00 25.43  ? 184 VAL D CG1 1 
ATOM   5872 C  CG2 . VAL D 2 184 ? -10.125 3.168   -90.457  1.00 18.83  ? 184 VAL D CG2 1 
ATOM   5873 N  N   . LEU D 2 185 ? -6.761  4.238   -90.262  1.00 36.04  ? 185 LEU D N   1 
ATOM   5874 C  CA  . LEU D 2 185 ? -5.694  3.868   -91.180  1.00 26.88  ? 185 LEU D CA  1 
ATOM   5875 C  C   . LEU D 2 185 ? -5.383  2.390   -90.988  1.00 27.95  ? 185 LEU D C   1 
ATOM   5876 O  O   . LEU D 2 185 ? -5.794  1.765   -90.005  1.00 32.07  ? 185 LEU D O   1 
ATOM   5877 C  CB  . LEU D 2 185 ? -4.435  4.704   -90.944  1.00 27.60  ? 185 LEU D CB  1 
ATOM   5878 C  CG  . LEU D 2 185 ? -4.652  6.227   -90.950  1.00 39.13  ? 185 LEU D CG  1 
ATOM   5879 C  CD1 . LEU D 2 185 ? -3.545  6.949   -90.167  1.00 36.81  ? 185 LEU D CD1 1 
ATOM   5880 C  CD2 . LEU D 2 185 ? -4.796  6.785   -92.353  1.00 27.73  ? 185 LEU D CD2 1 
ATOM   5881 N  N   . PHE D 2 186 ? -4.646  1.827   -91.932  1.00 27.64  ? 186 PHE D N   1 
ATOM   5882 C  CA  . PHE D 2 186 ? -4.409  0.392   -91.962  1.00 30.95  ? 186 PHE D CA  1 
ATOM   5883 C  C   . PHE D 2 186 ? -2.909  0.166   -91.895  1.00 26.00  ? 186 PHE D C   1 
ATOM   5884 O  O   . PHE D 2 186 ? -2.156  0.684   -92.721  1.00 27.82  ? 186 PHE D O   1 
ATOM   5885 C  CB  . PHE D 2 186 ? -5.058  -0.226  -93.208  1.00 27.50  ? 186 PHE D CB  1 
ATOM   5886 C  CG  . PHE D 2 186 ? -6.556  0.034   -93.290  1.00 31.28  ? 186 PHE D CG  1 
ATOM   5887 C  CD1 . PHE D 2 186 ? -7.419  -0.454  -92.316  1.00 34.19  ? 186 PHE D CD1 1 
ATOM   5888 C  CD2 . PHE D 2 186 ? -7.094  0.809   -94.303  1.00 32.42  ? 186 PHE D CD2 1 
ATOM   5889 C  CE1 . PHE D 2 186 ? -8.791  -0.214  -92.376  1.00 28.63  ? 186 PHE D CE1 1 
ATOM   5890 C  CE2 . PHE D 2 186 ? -8.476  1.058   -94.361  1.00 34.96  ? 186 PHE D CE2 1 
ATOM   5891 C  CZ  . PHE D 2 186 ? -9.318  0.534   -93.400  1.00 30.63  ? 186 PHE D CZ  1 
ATOM   5892 N  N   . GLN D 2 187 ? -2.474  -0.556  -90.882  1.00 33.48  ? 187 GLN D N   1 
ATOM   5893 C  CA  . GLN D 2 187 ? -1.060  -0.680  -90.558  1.00 35.53  ? 187 GLN D CA  1 
ATOM   5894 C  C   . GLN D 2 187 ? -0.680  -2.147  -90.687  1.00 33.65  ? 187 GLN D C   1 
ATOM   5895 O  O   . GLN D 2 187 ? -1.147  -2.978  -89.900  1.00 40.04  ? 187 GLN D O   1 
ATOM   5896 C  CB  . GLN D 2 187 ? -0.785  -0.163  -89.147  1.00 29.46  ? 187 GLN D CB  1 
ATOM   5897 C  CG  . GLN D 2 187 ? 0.595   0.441   -88.960  1.00 36.98  ? 187 GLN D CG  1 
ATOM   5898 C  CD  . GLN D 2 187 ? 0.941   0.632   -87.497  1.00 46.94  ? 187 GLN D CD  1 
ATOM   5899 O  OE1 . GLN D 2 187 ? 0.773   -0.283  -86.684  1.00 44.84  ? 187 GLN D OE1 1 
ATOM   5900 N  NE2 . GLN D 2 187 ? 1.405   1.831   -87.147  1.00 46.91  ? 187 GLN D NE2 1 
ATOM   5901 N  N   A GLU D 2 188 ? 0.172   -2.460  -91.663  0.16 33.26  ? 188 GLU D N   1 
ATOM   5902 N  N   B GLU D 2 188 ? 0.153   -2.466  -91.676  0.84 33.30  ? 188 GLU D N   1 
ATOM   5903 C  CA  A GLU D 2 188 ? 0.587   -3.840  -91.872  0.16 36.80  ? 188 GLU D CA  1 
ATOM   5904 C  CA  B GLU D 2 188 ? 0.568   -3.849  -91.867  0.84 36.76  ? 188 GLU D CA  1 
ATOM   5905 C  C   A GLU D 2 188 ? 1.349   -4.357  -90.659  0.16 36.13  ? 188 GLU D C   1 
ATOM   5906 C  C   B GLU D 2 188 ? 1.320   -4.345  -90.642  0.84 36.08  ? 188 GLU D C   1 
ATOM   5907 O  O   A GLU D 2 188 ? 2.260   -3.697  -90.151  0.16 34.30  ? 188 GLU D O   1 
ATOM   5908 O  O   B GLU D 2 188 ? 2.200   -3.660  -90.112  0.84 34.06  ? 188 GLU D O   1 
ATOM   5909 C  CB  A GLU D 2 188 ? 1.446   -3.962  -93.133  0.16 39.47  ? 188 GLU D CB  1 
ATOM   5910 C  CB  B GLU D 2 188 ? 1.441   -3.995  -93.118  0.84 38.64  ? 188 GLU D CB  1 
ATOM   5911 C  CG  A GLU D 2 188 ? 1.275   -5.300  -93.848  0.16 42.27  ? 188 GLU D CG  1 
ATOM   5912 C  CG  B GLU D 2 188 ? 1.309   -5.371  -93.779  0.84 42.20  ? 188 GLU D CG  1 
ATOM   5913 C  CD  A GLU D 2 188 ? 2.193   -5.466  -95.047  0.16 48.48  ? 188 GLU D CD  1 
ATOM   5914 C  CD  B GLU D 2 188 ? 2.382   -5.652  -94.833  0.84 49.66  ? 188 GLU D CD  1 
ATOM   5915 O  OE1 A GLU D 2 188 ? 3.413   -5.228  -94.911  0.16 48.61  ? 188 GLU D OE1 1 
ATOM   5916 O  OE1 B GLU D 2 188 ? 3.586   -5.445  -94.550  0.84 49.33  ? 188 GLU D OE1 1 
ATOM   5917 O  OE2 A GLU D 2 188 ? 1.692   -5.844  -96.128  0.16 50.74  ? 188 GLU D OE2 1 
ATOM   5918 O  OE2 B GLU D 2 188 ? 2.017   -6.095  -95.945  0.84 53.18  ? 188 GLU D OE2 1 
ATOM   5919 N  N   . VAL D 2 189 ? 0.961   -5.539  -90.194  1.00 33.82  ? 189 VAL D N   1 
ATOM   5920 C  CA  . VAL D 2 189 ? 1.568   -6.161  -89.037  1.00 33.73  ? 189 VAL D CA  1 
ATOM   5921 C  C   . VAL D 2 189 ? 2.955   -6.694  -89.384  1.00 40.16  ? 189 VAL D C   1 
ATOM   5922 O  O   . VAL D 2 189 ? 3.104   -7.458  -90.336  1.00 47.80  ? 189 VAL D O   1 
ATOM   5923 C  CB  . VAL D 2 189 ? 0.640   -7.278  -88.502  1.00 39.66  ? 189 VAL D CB  1 
ATOM   5924 C  CG1 . VAL D 2 189 ? 1.390   -8.236  -87.597  1.00 43.54  ? 189 VAL D CG1 1 
ATOM   5925 C  CG2 . VAL D 2 189 ? -0.538  -6.664  -87.756  1.00 35.12  ? 189 VAL D CG2 1 
HETATM 5926 CA CA  . CA  E 3 .   ? -35.989 1.606   -33.096  1.00 34.18  ? 301 CA  A CA  1 
HETATM 5927 CA CA  . CA  F 3 .   ? 20.151  5.993   -72.496  1.00 36.13  ? 301 CA  C CA  1 
HETATM 5928 O  O   . HOH G 4 .   ? -27.914 -9.850  -51.433  1.00 35.67  ? 401 HOH A O   1 
HETATM 5929 O  O   . HOH G 4 .   ? -45.618 -1.970  -34.414  1.00 48.28  ? 402 HOH A O   1 
HETATM 5930 O  O   . HOH G 4 .   ? -20.833 -4.293  -43.409  1.00 23.75  ? 403 HOH A O   1 
HETATM 5931 O  O   . HOH G 4 .   ? -21.520 -6.170  -57.143  1.00 37.12  ? 404 HOH A O   1 
HETATM 5932 O  O   . HOH G 4 .   ? -17.163 3.045   -26.511  1.00 41.49  ? 405 HOH A O   1 
HETATM 5933 O  O   . HOH G 4 .   ? -28.530 -4.135  -54.965  1.00 34.24  ? 406 HOH A O   1 
HETATM 5934 O  O   . HOH G 4 .   ? -23.319 -14.679 -50.075  1.00 36.31  ? 407 HOH A O   1 
HETATM 5935 O  O   . HOH G 4 .   ? -26.583 15.998  -45.522  1.00 28.09  ? 408 HOH A O   1 
HETATM 5936 O  O   . HOH G 4 .   ? -30.793 -2.779  -37.407  1.00 25.34  ? 409 HOH A O   1 
HETATM 5937 O  O   . HOH G 4 .   ? -9.800  -0.165  -45.008  1.00 23.45  ? 410 HOH A O   1 
HETATM 5938 O  O   . HOH G 4 .   ? -15.528 17.481  -43.883  1.00 35.71  ? 411 HOH A O   1 
HETATM 5939 O  O   . HOH G 4 .   ? -8.392  -12.837 -35.470  1.00 33.78  ? 412 HOH A O   1 
HETATM 5940 O  O   . HOH G 4 .   ? -16.824 6.555   -37.996  1.00 23.24  ? 413 HOH A O   1 
HETATM 5941 O  O   . HOH G 4 .   ? -27.030 8.935   -35.575  1.00 28.37  ? 414 HOH A O   1 
HETATM 5942 O  O   . HOH G 4 .   ? -12.028 2.391   -56.225  1.00 29.44  ? 415 HOH A O   1 
HETATM 5943 O  O   . HOH G 4 .   ? -6.612  14.092  -57.942  1.00 37.49  ? 416 HOH A O   1 
HETATM 5944 O  O   . HOH G 4 .   ? -13.339 -2.905  -57.954  1.00 41.33  ? 417 HOH A O   1 
HETATM 5945 O  O   . HOH G 4 .   ? -14.350 11.161  -47.071  1.00 29.22  ? 418 HOH A O   1 
HETATM 5946 O  O   . HOH G 4 .   ? -26.711 -0.658  -48.047  1.00 30.40  ? 419 HOH A O   1 
HETATM 5947 O  O   . HOH G 4 .   ? -23.413 2.219   -41.589  1.00 16.95  ? 420 HOH A O   1 
HETATM 5948 O  O   . HOH G 4 .   ? -13.787 0.367   -31.775  1.00 26.18  ? 421 HOH A O   1 
HETATM 5949 O  O   . HOH G 4 .   ? -13.636 6.762   -61.642  1.00 32.59  ? 422 HOH A O   1 
HETATM 5950 O  O   . HOH G 4 .   ? -17.953 10.905  -52.282  1.00 32.59  ? 423 HOH A O   1 
HETATM 5951 O  O   . HOH G 4 .   ? -21.008 -20.800 -38.020  1.00 30.87  ? 424 HOH A O   1 
HETATM 5952 O  O   . HOH G 4 .   ? -34.468 -12.529 -32.003  1.00 40.36  ? 425 HOH A O   1 
HETATM 5953 O  O   . HOH G 4 .   ? -18.611 9.624   -59.139  1.00 29.14  ? 426 HOH A O   1 
HETATM 5954 O  O   . HOH G 4 .   ? -34.017 -0.925  -43.394  1.00 29.75  ? 427 HOH A O   1 
HETATM 5955 O  O   . HOH G 4 .   ? -28.198 12.028  -45.626  1.00 23.39  ? 428 HOH A O   1 
HETATM 5956 O  O   . HOH G 4 .   ? -30.985 1.382   -31.657  1.00 30.58  ? 429 HOH A O   1 
HETATM 5957 O  O   . HOH G 4 .   ? -17.968 -21.372 -31.498  1.00 26.18  ? 430 HOH A O   1 
HETATM 5958 O  O   . HOH G 4 .   ? -9.091  -16.071 -39.139  1.00 40.34  ? 431 HOH A O   1 
HETATM 5959 O  O   . HOH G 4 .   ? -19.414 6.335   -33.790  1.00 25.94  ? 432 HOH A O   1 
HETATM 5960 O  O   . HOH G 4 .   ? -28.295 -13.641 -48.777  1.00 34.77  ? 433 HOH A O   1 
HETATM 5961 O  O   . HOH G 4 .   ? -28.077 1.587   -31.625  1.00 26.46  ? 434 HOH A O   1 
HETATM 5962 O  O   . HOH G 4 .   ? -35.058 -16.986 -39.405  1.00 39.46  ? 435 HOH A O   1 
HETATM 5963 O  O   . HOH G 4 .   ? -14.457 14.233  -47.720  1.00 19.51  ? 436 HOH A O   1 
HETATM 5964 O  O   . HOH G 4 .   ? -36.972 -12.629 -32.669  1.00 44.78  ? 437 HOH A O   1 
HETATM 5965 O  O   . HOH G 4 .   ? -1.723  6.736   -37.179  1.00 27.80  ? 438 HOH A O   1 
HETATM 5966 O  O   . HOH G 4 .   ? -32.327 14.073  -49.426  1.00 35.04  ? 439 HOH A O   1 
HETATM 5967 O  O   . HOH G 4 .   ? -0.874  -4.941  -44.643  1.00 36.78  ? 440 HOH A O   1 
HETATM 5968 O  O   . HOH G 4 .   ? -24.200 3.389   -39.053  1.00 19.26  ? 441 HOH A O   1 
HETATM 5969 O  O   . HOH G 4 .   ? -8.075  -12.569 -46.181  1.00 30.71  ? 442 HOH A O   1 
HETATM 5970 O  O   . HOH G 4 .   ? -23.689 19.503  -44.589  1.00 44.35  ? 443 HOH A O   1 
HETATM 5971 O  O   . HOH G 4 .   ? -34.759 -7.667  -28.471  1.00 37.06  ? 444 HOH A O   1 
HETATM 5972 O  O   . HOH G 4 .   ? -15.226 21.066  -39.967  1.00 44.71  ? 445 HOH A O   1 
HETATM 5973 O  O   . HOH G 4 .   ? -20.948 -9.065  -26.543  1.00 31.73  ? 446 HOH A O   1 
HETATM 5974 O  O   . HOH G 4 .   ? -6.204  16.476  -57.131  1.00 40.89  ? 447 HOH A O   1 
HETATM 5975 O  O   . HOH G 4 .   ? -38.232 4.344   -26.889  1.00 20.63  ? 448 HOH A O   1 
HETATM 5976 O  O   . HOH G 4 .   ? -2.486  -2.532  -35.637  1.00 34.45  ? 449 HOH A O   1 
HETATM 5977 O  O   . HOH G 4 .   ? -28.654 8.829   -53.982  1.00 17.90  ? 450 HOH A O   1 
HETATM 5978 O  O   . HOH G 4 .   ? -37.234 1.621   -35.312  1.00 21.98  ? 451 HOH A O   1 
HETATM 5979 O  O   . HOH G 4 .   ? -21.609 -22.122 -35.919  1.00 41.99  ? 452 HOH A O   1 
HETATM 5980 O  O   . HOH G 4 .   ? -33.268 11.193  -38.834  1.00 34.92  ? 453 HOH A O   1 
HETATM 5981 O  O   . HOH G 4 .   ? -28.264 4.653   -29.655  1.00 29.77  ? 454 HOH A O   1 
HETATM 5982 O  O   . HOH G 4 .   ? -17.711 16.272  -40.909  1.00 44.38  ? 455 HOH A O   1 
HETATM 5983 O  O   . HOH G 4 .   ? -9.188  -2.862  -45.881  1.00 26.50  ? 456 HOH A O   1 
HETATM 5984 O  O   . HOH G 4 .   ? -8.439  8.888   -63.538  1.00 41.61  ? 457 HOH A O   1 
HETATM 5985 O  O   . HOH G 4 .   ? -32.544 2.070   -26.728  1.00 38.82  ? 458 HOH A O   1 
HETATM 5986 O  O   . HOH G 4 .   ? -34.331 1.259   -30.649  1.00 32.25  ? 459 HOH A O   1 
HETATM 5987 O  O   . HOH G 4 .   ? -29.879 5.380   -28.776  1.00 41.49  ? 460 HOH A O   1 
HETATM 5988 O  O   . HOH G 4 .   ? -10.534 -18.442 -38.747  1.00 46.92  ? 461 HOH A O   1 
HETATM 5989 O  O   . HOH G 4 .   ? -33.808 2.733   -28.727  1.00 32.00  ? 462 HOH A O   1 
HETATM 5990 O  O   . HOH G 4 .   ? -35.860 -5.759  -27.225  1.00 31.20  ? 463 HOH A O   1 
HETATM 5991 O  O   . HOH H 4 .   ? 1.163   22.883  -1.705   1.00 34.45  ? 201 HOH B O   1 
HETATM 5992 O  O   . HOH H 4 .   ? -9.502  16.136  -27.309  1.00 23.34  ? 202 HOH B O   1 
HETATM 5993 O  O   . HOH H 4 .   ? -6.264  14.361  -39.703  1.00 35.43  ? 203 HOH B O   1 
HETATM 5994 O  O   . HOH H 4 .   ? 2.499   3.804   -25.765  1.00 30.90  ? 204 HOH B O   1 
HETATM 5995 O  O   . HOH H 4 .   ? -12.504 6.488   -30.211  1.00 18.66  ? 205 HOH B O   1 
HETATM 5996 O  O   . HOH H 4 .   ? -10.375 33.114  -31.793  1.00 36.72  ? 206 HOH B O   1 
HETATM 5997 O  O   . HOH H 4 .   ? -2.055  29.589  -32.616  1.00 32.09  ? 207 HOH B O   1 
HETATM 5998 O  O   . HOH H 4 .   ? -0.738  18.777  -36.236  1.00 24.15  ? 208 HOH B O   1 
HETATM 5999 O  O   . HOH H 4 .   ? 2.106   23.605  -14.081  1.00 30.71  ? 209 HOH B O   1 
HETATM 6000 O  O   . HOH H 4 .   ? 4.012   23.954  -20.863  1.00 25.06  ? 210 HOH B O   1 
HETATM 6001 O  O   . HOH H 4 .   ? -4.000  4.887   -30.169  1.00 24.56  ? 211 HOH B O   1 
HETATM 6002 O  O   . HOH H 4 .   ? 0.239   19.597  -10.279  1.00 32.81  ? 212 HOH B O   1 
HETATM 6003 O  O   . HOH H 4 .   ? -15.789 13.298  -30.478  1.00 30.47  ? 213 HOH B O   1 
HETATM 6004 O  O   . HOH H 4 .   ? -7.774  1.899   -36.941  1.00 23.59  ? 214 HOH B O   1 
HETATM 6005 O  O   . HOH H 4 .   ? 1.226   23.868  -23.237  1.00 29.26  ? 215 HOH B O   1 
HETATM 6006 O  O   . HOH H 4 .   ? -21.942 22.670  -25.588  1.00 51.38  ? 216 HOH B O   1 
HETATM 6007 O  O   . HOH H 4 .   ? -5.010  24.726  -14.155  1.00 26.79  ? 217 HOH B O   1 
HETATM 6008 O  O   . HOH H 4 .   ? -10.100 27.277  -24.887  1.00 26.41  ? 218 HOH B O   1 
HETATM 6009 O  O   . HOH H 4 .   ? 10.332  28.658  -44.818  1.00 36.09  ? 219 HOH B O   1 
HETATM 6010 O  O   . HOH H 4 .   ? -3.212  14.690  -43.724  1.00 38.07  ? 220 HOH B O   1 
HETATM 6011 O  O   . HOH H 4 .   ? -11.250 12.028  -34.650  1.00 25.39  ? 221 HOH B O   1 
HETATM 6012 O  O   . HOH H 4 .   ? -12.063 23.377  -36.235  1.00 32.91  ? 222 HOH B O   1 
HETATM 6013 O  O   . HOH H 4 .   ? -12.322 9.625   -30.723  1.00 19.73  ? 223 HOH B O   1 
HETATM 6014 O  O   . HOH H 4 .   ? 2.085   35.115  -30.615  1.00 37.64  ? 224 HOH B O   1 
HETATM 6015 O  O   . HOH H 4 .   ? -10.530 23.881  -42.479  1.00 42.79  ? 225 HOH B O   1 
HETATM 6016 O  O   . HOH H 4 .   ? -5.435  37.214  -28.045  1.00 48.88  ? 226 HOH B O   1 
HETATM 6017 O  O   . HOH H 4 .   ? -16.079 8.925   -24.030  1.00 36.58  ? 227 HOH B O   1 
HETATM 6018 O  O   . HOH H 4 .   ? -14.739 10.715  -31.605  1.00 34.56  ? 228 HOH B O   1 
HETATM 6019 O  O   . HOH H 4 .   ? -14.409 26.109  -39.317  1.00 31.00  ? 229 HOH B O   1 
HETATM 6020 O  O   . HOH H 4 .   ? -13.240 12.219  -36.792  1.00 28.14  ? 230 HOH B O   1 
HETATM 6021 O  O   . HOH H 4 .   ? -2.355  9.201   -36.931  1.00 20.25  ? 231 HOH B O   1 
HETATM 6022 O  O   . HOH H 4 .   ? -14.018 14.157  -38.582  1.00 31.19  ? 232 HOH B O   1 
HETATM 6023 O  O   . HOH H 4 .   ? -8.273  3.453   -28.786  1.00 27.56  ? 233 HOH B O   1 
HETATM 6024 O  O   . HOH H 4 .   ? -12.054 40.474  -32.981  1.00 52.87  ? 234 HOH B O   1 
HETATM 6025 O  O   . HOH H 4 .   ? -10.920 3.568   -30.106  1.00 35.42  ? 235 HOH B O   1 
HETATM 6026 O  O   . HOH H 4 .   ? -12.264 25.639  -40.140  1.00 33.93  ? 236 HOH B O   1 
HETATM 6027 O  O   . HOH H 4 .   ? 3.037   0.291   -19.261  1.00 48.34  ? 237 HOH B O   1 
HETATM 6028 O  O   . HOH H 4 .   ? -13.238 23.613  -38.913  1.00 32.08  ? 238 HOH B O   1 
HETATM 6029 O  O   . HOH H 4 .   ? -15.021 15.087  -40.405  1.00 34.47  ? 239 HOH B O   1 
HETATM 6030 O  O   . HOH H 4 .   ? 0.808   1.687   -20.517  1.00 43.48  ? 240 HOH B O   1 
HETATM 6031 O  O   . HOH H 4 .   ? -1.131  10.689  -38.612  1.00 30.21  ? 241 HOH B O   1 
HETATM 6032 O  O   . HOH I 4 .   ? -15.766 8.498   -70.872  1.00 39.80  ? 401 HOH C O   1 
HETATM 6033 O  O   . HOH I 4 .   ? 13.115  8.950   -88.715  1.00 81.56  ? 402 HOH C O   1 
HETATM 6034 O  O   . HOH I 4 .   ? 14.845  4.068   -71.743  1.00 19.04  ? 403 HOH C O   1 
HETATM 6035 O  O   . HOH I 4 .   ? 22.157  10.837  -63.011  1.00 32.70  ? 404 HOH C O   1 
HETATM 6036 O  O   . HOH I 4 .   ? 11.609  20.921  -74.355  1.00 19.62  ? 405 HOH C O   1 
HETATM 6037 O  O   . HOH I 4 .   ? 10.732  12.199  -81.893  1.00 24.58  ? 406 HOH C O   1 
HETATM 6038 O  O   . HOH I 4 .   ? 12.295  4.515   -71.778  1.00 26.14  ? 407 HOH C O   1 
HETATM 6039 O  O   . HOH I 4 .   ? 5.288   17.447  -69.471  1.00 24.25  ? 408 HOH C O   1 
HETATM 6040 O  O   . HOH I 4 .   ? 1.102   9.535   -78.313  1.00 29.98  ? 409 HOH C O   1 
HETATM 6041 O  O   . HOH I 4 .   ? -1.452  17.160  -88.295  1.00 32.56  ? 410 HOH C O   1 
HETATM 6042 O  O   . HOH I 4 .   ? -3.725  32.592  -72.175  1.00 47.21  ? 411 HOH C O   1 
HETATM 6043 O  O   . HOH I 4 .   ? 20.360  16.531  -56.364  1.00 27.51  ? 412 HOH C O   1 
HETATM 6044 O  O   . HOH I 4 .   ? 17.149  8.638   -56.271  1.00 21.88  ? 413 HOH C O   1 
HETATM 6045 O  O   . HOH I 4 .   ? 11.212  14.035  -89.322  1.00 37.56  ? 414 HOH C O   1 
HETATM 6046 O  O   . HOH I 4 .   ? 16.189  14.150  -67.461  1.00 20.14  ? 415 HOH C O   1 
HETATM 6047 O  O   . HOH I 4 .   ? -3.479  28.123  -79.104  1.00 39.29  ? 416 HOH C O   1 
HETATM 6048 O  O   . HOH I 4 .   ? 8.509   11.282  -75.909  1.00 19.21  ? 417 HOH C O   1 
HETATM 6049 O  O   . HOH I 4 .   ? 10.058  3.040   -86.185  1.00 27.39  ? 418 HOH C O   1 
HETATM 6050 O  O   . HOH I 4 .   ? 19.267  16.036  -86.083  1.00 33.55  ? 419 HOH C O   1 
HETATM 6051 O  O   . HOH I 4 .   ? 11.016  6.218   -80.022  1.00 32.36  ? 420 HOH C O   1 
HETATM 6052 O  O   . HOH I 4 .   ? 18.510  3.883   -71.519  1.00 31.08  ? 421 HOH C O   1 
HETATM 6053 O  O   . HOH I 4 .   ? 12.511  14.999  -85.996  1.00 35.57  ? 422 HOH C O   1 
HETATM 6054 O  O   . HOH I 4 .   ? 20.370  20.242  -61.968  1.00 29.05  ? 423 HOH C O   1 
HETATM 6055 O  O   . HOH I 4 .   ? 3.377   5.485   -77.149  1.00 22.58  ? 424 HOH C O   1 
HETATM 6056 O  O   . HOH I 4 .   ? -4.393  25.781  -60.975  1.00 26.51  ? 425 HOH C O   1 
HETATM 6057 O  O   . HOH I 4 .   ? 22.358  -0.630  -73.740  1.00 25.20  ? 426 HOH C O   1 
HETATM 6058 O  O   . HOH I 4 .   ? 15.125  11.411  -69.661  1.00 21.30  ? 427 HOH C O   1 
HETATM 6059 O  O   . HOH I 4 .   ? 13.725  1.924   -60.217  1.00 39.60  ? 428 HOH C O   1 
HETATM 6060 O  O   . HOH I 4 .   ? -12.624 18.048  -77.133  1.00 38.56  ? 429 HOH C O   1 
HETATM 6061 O  O   . HOH I 4 .   ? 11.004  10.125  -52.326  1.00 30.74  ? 430 HOH C O   1 
HETATM 6062 O  O   . HOH I 4 .   ? 2.453   2.130   -58.557  1.00 33.29  ? 431 HOH C O   1 
HETATM 6063 O  O   . HOH I 4 .   ? 7.840   13.722  -75.107  1.00 26.16  ? 432 HOH C O   1 
HETATM 6064 O  O   . HOH I 4 .   ? 12.808  2.941   -58.064  1.00 27.33  ? 433 HOH C O   1 
HETATM 6065 O  O   . HOH I 4 .   ? 19.376  21.540  -78.571  1.00 34.73  ? 434 HOH C O   1 
HETATM 6066 O  O   . HOH I 4 .   ? -13.345 15.450  -78.199  1.00 39.82  ? 435 HOH C O   1 
HETATM 6067 O  O   . HOH I 4 .   ? 13.152  23.382  -85.191  1.00 27.22  ? 436 HOH C O   1 
HETATM 6068 O  O   . HOH I 4 .   ? 14.313  26.212  -66.296  1.00 38.11  ? 437 HOH C O   1 
HETATM 6069 O  O   . HOH I 4 .   ? 21.094  -1.892  -75.231  1.00 31.15  ? 438 HOH C O   1 
HETATM 6070 O  O   . HOH I 4 .   ? 18.939  15.643  -73.544  1.00 40.28  ? 439 HOH C O   1 
HETATM 6071 O  O   . HOH I 4 .   ? -8.960  23.602  -64.637  1.00 34.27  ? 440 HOH C O   1 
HETATM 6072 O  O   . HOH I 4 .   ? 17.856  1.139   -72.180  1.00 34.78  ? 441 HOH C O   1 
HETATM 6073 O  O   . HOH I 4 .   ? 8.972   23.068  -57.101  1.00 33.75  ? 442 HOH C O   1 
HETATM 6074 O  O   . HOH I 4 .   ? 12.764  1.673   -74.919  1.00 24.44  ? 443 HOH C O   1 
HETATM 6075 O  O   . HOH I 4 .   ? 17.960  23.833  -77.992  1.00 42.60  ? 444 HOH C O   1 
HETATM 6076 O  O   . HOH I 4 .   ? 12.968  28.706  -76.225  1.00 40.32  ? 445 HOH C O   1 
HETATM 6077 O  O   . HOH I 4 .   ? 0.669   31.122  -62.615  1.00 35.56  ? 446 HOH C O   1 
HETATM 6078 O  O   . HOH I 4 .   ? -10.012 10.877  -62.744  1.00 32.99  ? 447 HOH C O   1 
HETATM 6079 O  O   . HOH I 4 .   ? 13.958  12.652  -88.357  1.00 43.29  ? 448 HOH C O   1 
HETATM 6080 O  O   . HOH I 4 .   ? -16.296 16.337  -77.760  1.00 38.20  ? 449 HOH C O   1 
HETATM 6081 O  O   . HOH I 4 .   ? 8.624   27.138  -56.498  1.00 37.64  ? 450 HOH C O   1 
HETATM 6082 O  O   . HOH J 4 .   ? -7.502  3.585   -101.637 1.00 37.12  ? 201 HOH D O   1 
HETATM 6083 O  O   . HOH J 4 .   ? -14.003 5.537   -101.325 1.00 29.26  ? 202 HOH D O   1 
HETATM 6084 O  O   . HOH J 4 .   ? -6.627  -3.102  -84.668  1.00 34.73  ? 203 HOH D O   1 
HETATM 6085 O  O   . HOH J 4 .   ? -14.243 -2.155  -99.312  1.00 32.05  ? 204 HOH D O   1 
HETATM 6086 O  O   . HOH J 4 .   ? -8.271  -12.081 -95.833  1.00 32.26  ? 205 HOH D O   1 
HETATM 6087 O  O   . HOH J 4 .   ? -9.477  9.318   -86.382  1.00 37.47  ? 206 HOH D O   1 
HETATM 6088 O  O   . HOH J 4 .   ? -21.377 7.596   -76.429  1.00 36.55  ? 207 HOH D O   1 
HETATM 6089 O  O   . HOH J 4 .   ? -3.961  3.259   -94.006  1.00 23.91  ? 208 HOH D O   1 
HETATM 6090 O  O   . HOH J 4 .   ? -24.006 -6.988  -94.366  1.00 25.04  ? 209 HOH D O   1 
HETATM 6091 O  O   . HOH J 4 .   ? -11.801 2.280   -74.747  1.00 24.27  ? 210 HOH D O   1 
HETATM 6092 O  O   . HOH J 4 .   ? -6.164  -8.741  -94.691  1.00 28.14  ? 211 HOH D O   1 
HETATM 6093 O  O   . HOH J 4 .   ? -26.749 1.058   -100.393 1.00 57.89  ? 212 HOH D O   1 
HETATM 6094 O  O   . HOH J 4 .   ? -17.768 -9.111  -91.093  1.00 20.41  ? 213 HOH D O   1 
HETATM 6095 O  O   . HOH J 4 .   ? -3.063  2.082   -76.336  1.00 22.21  ? 214 HOH D O   1 
HETATM 6096 O  O   . HOH J 4 .   ? -16.071 -7.820  -102.891 1.00 43.64  ? 215 HOH D O   1 
HETATM 6097 O  O   . HOH J 4 .   ? -15.619 4.694   -90.076  1.00 25.06  ? 216 HOH D O   1 
HETATM 6098 O  O   . HOH J 4 .   ? -20.606 -11.953 -89.873  1.00 30.75  ? 217 HOH D O   1 
HETATM 6099 O  O   . HOH J 4 .   ? -11.902 -7.762  -72.552  1.00 43.51  ? 218 HOH D O   1 
HETATM 6100 O  O   . HOH J 4 .   ? -21.516 2.855   -100.639 1.00 45.71  ? 219 HOH D O   1 
HETATM 6101 O  O   . HOH J 4 .   ? -23.940 -1.561  -71.414  1.00 30.56  ? 220 HOH D O   1 
HETATM 6102 O  O   . HOH J 4 .   ? -17.531 8.300   -83.666  1.00 39.09  ? 221 HOH D O   1 
HETATM 6103 O  O   . HOH J 4 .   ? -23.367 6.086   -75.064  1.00 30.05  ? 222 HOH D O   1 
HETATM 6104 O  O   . HOH J 4 .   ? -26.811 -10.265 -91.065  1.00 36.02  ? 223 HOH D O   1 
HETATM 6105 O  O   . HOH J 4 .   ? -6.920  -5.858  -74.670  1.00 36.34  ? 224 HOH D O   1 
HETATM 6106 O  O   . HOH J 4 .   ? -3.701  1.656   -79.546  1.00 20.31  ? 225 HOH D O   1 
HETATM 6107 O  O   . HOH J 4 .   ? -0.224  0.148   -83.330  1.00 30.15  ? 226 HOH D O   1 
HETATM 6108 O  O   . HOH J 4 .   ? -5.366  6.541   -71.907  1.00 27.81  ? 227 HOH D O   1 
HETATM 6109 O  O   . HOH J 4 .   ? -25.735 -8.573  -90.289  1.00 35.92  ? 228 HOH D O   1 
HETATM 6110 O  O   . HOH J 4 .   ? -17.912 -18.376 -91.113  1.00 31.22  ? 229 HOH D O   1 
HETATM 6111 O  O   . HOH J 4 .   ? -7.799  9.761   -73.262  1.00 22.61  ? 230 HOH D O   1 
HETATM 6112 O  O   . HOH J 4 .   ? -14.377 1.848   -68.027  1.00 41.48  ? 231 HOH D O   1 
HETATM 6113 O  O   . HOH J 4 .   ? -10.448 0.648   -73.353  1.00 28.52  ? 232 HOH D O   1 
HETATM 6114 O  O   . HOH J 4 .   ? -1.311  2.363   -81.252  1.00 30.36  ? 233 HOH D O   1 
HETATM 6115 O  O   . HOH J 4 .   ? -12.101 10.394  -86.371  1.00 23.44  ? 234 HOH D O   1 
HETATM 6116 O  O   . HOH J 4 .   ? -7.534  1.729   -73.045  1.00 32.14  ? 235 HOH D O   1 
HETATM 6117 O  O   . HOH J 4 .   ? -2.553  6.649   -83.100  1.00 29.71  ? 236 HOH D O   1 
HETATM 6118 O  O   . HOH J 4 .   ? 3.155   2.595   -76.608  1.00 44.33  ? 237 HOH D O   1 
HETATM 6119 O  O   . HOH J 4 .   ? -2.053  8.999   -86.999  1.00 30.81  ? 238 HOH D O   1 
HETATM 6120 O  O   . HOH J 4 .   ? -9.036  -7.322  -74.353  1.00 42.44  ? 239 HOH D O   1 
HETATM 6121 O  O   . HOH J 4 .   ? -8.423  -16.688 -86.931  1.00 36.72  ? 240 HOH D O   1 
HETATM 6122 O  O   . HOH J 4 .   ? -2.699  6.378   -95.744  1.00 41.35  ? 241 HOH D O   1 
HETATM 6123 O  O   . HOH J 4 .   ? -7.412  8.148   -71.215  1.00 25.05  ? 242 HOH D O   1 
HETATM 6124 O  O   . HOH J 4 .   ? -15.255 9.283   -82.478  1.00 31.81  ? 243 HOH D O   1 
HETATM 6125 O  O   . HOH J 4 .   ? -30.880 12.197  -89.022  1.00 50.93  ? 244 HOH D O   1 
# 
