data_8KEN
# 
_entry.id   8KEN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8KEN         pdb_00008ken 10.2210/pdb8ken/pdb 
WWPDB D_1300040011 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-19 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8KEN 
_pdbx_database_status.recvd_initial_deposition_date   2023-08-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yanli@hust.edu.cn 
_pdbx_contact_author.name_first         Yan 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1963-839X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, Y.H.' 1 0000-0002-5983-0151 
'Ma, B.'    2 ?                   
'Kang, Y.'  3 ?                   
'Liu, B.'   4 ?                   
'Li, Y.'    5 0000-0003-1963-839X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The crystal structure of M-EXOD' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Liu, Y.H.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0002-5983-0151 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man Exodeoxyribonuclease 25935.645 2  ? ? ? ? 
2 water   nat water                18.015    95 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MFDFIIDFETMGSGEKAAVIDLAVIAFDPNPEVVETFDELVSRGIKIKFDLKSQKGHRLFTKSTIEWWKNQSPEARKNIA
PSDEDVATIAGIAKFNDYINAHNIDPWKSQGWCRGMSFDFPILVDLIRDIQRLNGVSENELDTFKLEPCKFWNQRDIRTR
IEALLLVRDMTTCPLPKGTLDGFVAHDSIHDCAKDILMMKYALRYAMGLEDAPSEEECDPLSLPTKR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MFDFIIDFETMGSGEKAAVIDLAVIAFDPNPEVVETFDELVSRGIKIKFDLKSQKGHRLFTKSTIEWWKNQSPEARKNIA
PSDEDVATIAGIAKFNDYINAHNIDPWKSQGWCRGMSFDFPILVDLIRDIQRLNGVSENELDTFKLEPCKFWNQRDIRTR
IEALLLVRDMTTCPLPKGTLDGFVAHDSIHDCAKDILMMKYALRYAMGLEDAPSEEECDPLSLPTKR
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PHE n 
1 3   ASP n 
1 4   PHE n 
1 5   ILE n 
1 6   ILE n 
1 7   ASP n 
1 8   PHE n 
1 9   GLU n 
1 10  THR n 
1 11  MET n 
1 12  GLY n 
1 13  SER n 
1 14  GLY n 
1 15  GLU n 
1 16  LYS n 
1 17  ALA n 
1 18  ALA n 
1 19  VAL n 
1 20  ILE n 
1 21  ASP n 
1 22  LEU n 
1 23  ALA n 
1 24  VAL n 
1 25  ILE n 
1 26  ALA n 
1 27  PHE n 
1 28  ASP n 
1 29  PRO n 
1 30  ASN n 
1 31  PRO n 
1 32  GLU n 
1 33  VAL n 
1 34  VAL n 
1 35  GLU n 
1 36  THR n 
1 37  PHE n 
1 38  ASP n 
1 39  GLU n 
1 40  LEU n 
1 41  VAL n 
1 42  SER n 
1 43  ARG n 
1 44  GLY n 
1 45  ILE n 
1 46  LYS n 
1 47  ILE n 
1 48  LYS n 
1 49  PHE n 
1 50  ASP n 
1 51  LEU n 
1 52  LYS n 
1 53  SER n 
1 54  GLN n 
1 55  LYS n 
1 56  GLY n 
1 57  HIS n 
1 58  ARG n 
1 59  LEU n 
1 60  PHE n 
1 61  THR n 
1 62  LYS n 
1 63  SER n 
1 64  THR n 
1 65  ILE n 
1 66  GLU n 
1 67  TRP n 
1 68  TRP n 
1 69  LYS n 
1 70  ASN n 
1 71  GLN n 
1 72  SER n 
1 73  PRO n 
1 74  GLU n 
1 75  ALA n 
1 76  ARG n 
1 77  LYS n 
1 78  ASN n 
1 79  ILE n 
1 80  ALA n 
1 81  PRO n 
1 82  SER n 
1 83  ASP n 
1 84  GLU n 
1 85  ASP n 
1 86  VAL n 
1 87  ALA n 
1 88  THR n 
1 89  ILE n 
1 90  ALA n 
1 91  GLY n 
1 92  ILE n 
1 93  ALA n 
1 94  LYS n 
1 95  PHE n 
1 96  ASN n 
1 97  ASP n 
1 98  TYR n 
1 99  ILE n 
1 100 ASN n 
1 101 ALA n 
1 102 HIS n 
1 103 ASN n 
1 104 ILE n 
1 105 ASP n 
1 106 PRO n 
1 107 TRP n 
1 108 LYS n 
1 109 SER n 
1 110 GLN n 
1 111 GLY n 
1 112 TRP n 
1 113 CYS n 
1 114 ARG n 
1 115 GLY n 
1 116 MET n 
1 117 SER n 
1 118 PHE n 
1 119 ASP n 
1 120 PHE n 
1 121 PRO n 
1 122 ILE n 
1 123 LEU n 
1 124 VAL n 
1 125 ASP n 
1 126 LEU n 
1 127 ILE n 
1 128 ARG n 
1 129 ASP n 
1 130 ILE n 
1 131 GLN n 
1 132 ARG n 
1 133 LEU n 
1 134 ASN n 
1 135 GLY n 
1 136 VAL n 
1 137 SER n 
1 138 GLU n 
1 139 ASN n 
1 140 GLU n 
1 141 LEU n 
1 142 ASP n 
1 143 THR n 
1 144 PHE n 
1 145 LYS n 
1 146 LEU n 
1 147 GLU n 
1 148 PRO n 
1 149 CYS n 
1 150 LYS n 
1 151 PHE n 
1 152 TRP n 
1 153 ASN n 
1 154 GLN n 
1 155 ARG n 
1 156 ASP n 
1 157 ILE n 
1 158 ARG n 
1 159 THR n 
1 160 ARG n 
1 161 ILE n 
1 162 GLU n 
1 163 ALA n 
1 164 LEU n 
1 165 LEU n 
1 166 LEU n 
1 167 VAL n 
1 168 ARG n 
1 169 ASP n 
1 170 MET n 
1 171 THR n 
1 172 THR n 
1 173 CYS n 
1 174 PRO n 
1 175 LEU n 
1 176 PRO n 
1 177 LYS n 
1 178 GLY n 
1 179 THR n 
1 180 LEU n 
1 181 ASP n 
1 182 GLY n 
1 183 PHE n 
1 184 VAL n 
1 185 ALA n 
1 186 HIS n 
1 187 ASP n 
1 188 SER n 
1 189 ILE n 
1 190 HIS n 
1 191 ASP n 
1 192 CYS n 
1 193 ALA n 
1 194 LYS n 
1 195 ASP n 
1 196 ILE n 
1 197 LEU n 
1 198 MET n 
1 199 MET n 
1 200 LYS n 
1 201 TYR n 
1 202 ALA n 
1 203 LEU n 
1 204 ARG n 
1 205 TYR n 
1 206 ALA n 
1 207 MET n 
1 208 GLY n 
1 209 LEU n 
1 210 GLU n 
1 211 ASP n 
1 212 ALA n 
1 213 PRO n 
1 214 SER n 
1 215 GLU n 
1 216 GLU n 
1 217 GLU n 
1 218 CYS n 
1 219 ASP n 
1 220 PRO n 
1 221 LEU n 
1 222 SER n 
1 223 LEU n 
1 224 PRO n 
1 225 THR n 
1 226 LYS n 
1 227 ARG n 
# 
_entity_src_gen.entity_id                          1 
_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                   227 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 dexA 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Escherichia phage EcSzw_1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2419742 
_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      'Escherichia coli-Pichia pastoris shuttle vector pPpB1_S' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1182036 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET B . n 
A 1 2   PHE 2   2   2   PHE PHE B . n 
A 1 3   ASP 3   3   3   ASP ASP B . n 
A 1 4   PHE 4   4   4   PHE PHE B . n 
A 1 5   ILE 5   5   5   ILE ILE B . n 
A 1 6   ILE 6   6   6   ILE ILE B . n 
A 1 7   ASP 7   7   7   ASP ASP B . n 
A 1 8   PHE 8   8   8   PHE PHE B . n 
A 1 9   GLU 9   9   9   GLU GLU B . n 
A 1 10  THR 10  10  10  THR THR B . n 
A 1 11  MET 11  11  11  MET MET B . n 
A 1 12  GLY 12  12  12  GLY GLY B . n 
A 1 13  SER 13  13  13  SER SER B . n 
A 1 14  GLY 14  14  14  GLY GLY B . n 
A 1 15  GLU 15  15  15  GLU GLU B . n 
A 1 16  LYS 16  16  16  LYS LYS B . n 
A 1 17  ALA 17  17  17  ALA ALA B . n 
A 1 18  ALA 18  18  18  ALA ALA B . n 
A 1 19  VAL 19  19  19  VAL VAL B . n 
A 1 20  ILE 20  20  20  ILE ILE B . n 
A 1 21  ASP 21  21  21  ASP ASP B . n 
A 1 22  LEU 22  22  22  LEU LEU B . n 
A 1 23  ALA 23  23  23  ALA ALA B . n 
A 1 24  VAL 24  24  24  VAL VAL B . n 
A 1 25  ILE 25  25  25  ILE ILE B . n 
A 1 26  ALA 26  26  26  ALA ALA B . n 
A 1 27  PHE 27  27  27  PHE PHE B . n 
A 1 28  ASP 28  28  28  ASP ASP B . n 
A 1 29  PRO 29  29  29  PRO PRO B . n 
A 1 30  ASN 30  30  30  ASN ASN B . n 
A 1 31  PRO 31  31  31  PRO PRO B . n 
A 1 32  GLU 32  32  32  GLU GLU B . n 
A 1 33  VAL 33  33  33  VAL VAL B . n 
A 1 34  VAL 34  34  34  VAL VAL B . n 
A 1 35  GLU 35  35  35  GLU GLU B . n 
A 1 36  THR 36  36  36  THR THR B . n 
A 1 37  PHE 37  37  37  PHE PHE B . n 
A 1 38  ASP 38  38  38  ASP ASP B . n 
A 1 39  GLU 39  39  39  GLU GLU B . n 
A 1 40  LEU 40  40  40  LEU LEU B . n 
A 1 41  VAL 41  41  41  VAL VAL B . n 
A 1 42  SER 42  42  42  SER SER B . n 
A 1 43  ARG 43  43  43  ARG ARG B . n 
A 1 44  GLY 44  44  44  GLY GLY B . n 
A 1 45  ILE 45  45  45  ILE ILE B . n 
A 1 46  LYS 46  46  46  LYS LYS B . n 
A 1 47  ILE 47  47  47  ILE ILE B . n 
A 1 48  LYS 48  48  48  LYS LYS B . n 
A 1 49  PHE 49  49  49  PHE PHE B . n 
A 1 50  ASP 50  50  50  ASP ASP B . n 
A 1 51  LEU 51  51  51  LEU LEU B . n 
A 1 52  LYS 52  52  52  LYS LYS B . n 
A 1 53  SER 53  53  53  SER SER B . n 
A 1 54  GLN 54  54  54  GLN GLN B . n 
A 1 55  LYS 55  55  55  LYS LYS B . n 
A 1 56  GLY 56  56  56  GLY GLY B . n 
A 1 57  HIS 57  57  57  HIS HIS B . n 
A 1 58  ARG 58  58  58  ARG ARG B . n 
A 1 59  LEU 59  59  59  LEU LEU B . n 
A 1 60  PHE 60  60  60  PHE PHE B . n 
A 1 61  THR 61  61  61  THR THR B . n 
A 1 62  LYS 62  62  62  LYS LYS B . n 
A 1 63  SER 63  63  63  SER SER B . n 
A 1 64  THR 64  64  64  THR THR B . n 
A 1 65  ILE 65  65  65  ILE ILE B . n 
A 1 66  GLU 66  66  66  GLU GLU B . n 
A 1 67  TRP 67  67  67  TRP TRP B . n 
A 1 68  TRP 68  68  68  TRP TRP B . n 
A 1 69  LYS 69  69  69  LYS LYS B . n 
A 1 70  ASN 70  70  70  ASN ASN B . n 
A 1 71  GLN 71  71  71  GLN GLN B . n 
A 1 72  SER 72  72  72  SER SER B . n 
A 1 73  PRO 73  73  73  PRO PRO B . n 
A 1 74  GLU 74  74  74  GLU GLU B . n 
A 1 75  ALA 75  75  75  ALA ALA B . n 
A 1 76  ARG 76  76  76  ARG ARG B . n 
A 1 77  LYS 77  77  77  LYS LYS B . n 
A 1 78  ASN 78  78  78  ASN ASN B . n 
A 1 79  ILE 79  79  79  ILE ILE B . n 
A 1 80  ALA 80  80  80  ALA ALA B . n 
A 1 81  PRO 81  81  81  PRO PRO B . n 
A 1 82  SER 82  82  82  SER SER B . n 
A 1 83  ASP 83  83  83  ASP ASP B . n 
A 1 84  GLU 84  84  84  GLU GLU B . n 
A 1 85  ASP 85  85  85  ASP ASP B . n 
A 1 86  VAL 86  86  86  VAL VAL B . n 
A 1 87  ALA 87  87  87  ALA ALA B . n 
A 1 88  THR 88  88  88  THR THR B . n 
A 1 89  ILE 89  89  89  ILE ILE B . n 
A 1 90  ALA 90  90  90  ALA ALA B . n 
A 1 91  GLY 91  91  91  GLY GLY B . n 
A 1 92  ILE 92  92  92  ILE ILE B . n 
A 1 93  ALA 93  93  93  ALA ALA B . n 
A 1 94  LYS 94  94  94  LYS LYS B . n 
A 1 95  PHE 95  95  95  PHE PHE B . n 
A 1 96  ASN 96  96  96  ASN ASN B . n 
A 1 97  ASP 97  97  97  ASP ASP B . n 
A 1 98  TYR 98  98  98  TYR TYR B . n 
A 1 99  ILE 99  99  99  ILE ILE B . n 
A 1 100 ASN 100 100 100 ASN ASN B . n 
A 1 101 ALA 101 101 101 ALA ALA B . n 
A 1 102 HIS 102 102 102 HIS HIS B . n 
A 1 103 ASN 103 103 103 ASN ASN B . n 
A 1 104 ILE 104 104 104 ILE ILE B . n 
A 1 105 ASP 105 105 105 ASP ASP B . n 
A 1 106 PRO 106 106 106 PRO PRO B . n 
A 1 107 TRP 107 107 107 TRP TRP B . n 
A 1 108 LYS 108 108 108 LYS LYS B . n 
A 1 109 SER 109 109 109 SER SER B . n 
A 1 110 GLN 110 110 110 GLN GLN B . n 
A 1 111 GLY 111 111 111 GLY GLY B . n 
A 1 112 TRP 112 112 112 TRP TRP B . n 
A 1 113 CYS 113 113 113 CYS CYS B . n 
A 1 114 ARG 114 114 114 ARG ARG B . n 
A 1 115 GLY 115 115 115 GLY GLY B . n 
A 1 116 MET 116 116 116 MET MET B . n 
A 1 117 SER 117 117 117 SER SER B . n 
A 1 118 PHE 118 118 118 PHE PHE B . n 
A 1 119 ASP 119 119 119 ASP ASP B . n 
A 1 120 PHE 120 120 120 PHE PHE B . n 
A 1 121 PRO 121 121 121 PRO PRO B . n 
A 1 122 ILE 122 122 122 ILE ILE B . n 
A 1 123 LEU 123 123 123 LEU LEU B . n 
A 1 124 VAL 124 124 124 VAL VAL B . n 
A 1 125 ASP 125 125 125 ASP ASP B . n 
A 1 126 LEU 126 126 126 LEU LEU B . n 
A 1 127 ILE 127 127 127 ILE ILE B . n 
A 1 128 ARG 128 128 128 ARG ARG B . n 
A 1 129 ASP 129 129 129 ASP ASP B . n 
A 1 130 ILE 130 130 130 ILE ILE B . n 
A 1 131 GLN 131 131 131 GLN GLN B . n 
A 1 132 ARG 132 132 132 ARG ARG B . n 
A 1 133 LEU 133 133 133 LEU LEU B . n 
A 1 134 ASN 134 134 134 ASN ASN B . n 
A 1 135 GLY 135 135 135 GLY GLY B . n 
A 1 136 VAL 136 136 136 VAL VAL B . n 
A 1 137 SER 137 137 137 SER SER B . n 
A 1 138 GLU 138 138 138 GLU GLU B . n 
A 1 139 ASN 139 139 139 ASN ASN B . n 
A 1 140 GLU 140 140 140 GLU GLU B . n 
A 1 141 LEU 141 141 141 LEU LEU B . n 
A 1 142 ASP 142 142 142 ASP ASP B . n 
A 1 143 THR 143 143 143 THR THR B . n 
A 1 144 PHE 144 144 144 PHE PHE B . n 
A 1 145 LYS 145 145 145 LYS LYS B . n 
A 1 146 LEU 146 146 146 LEU LEU B . n 
A 1 147 GLU 147 147 147 GLU GLU B . n 
A 1 148 PRO 148 148 148 PRO PRO B . n 
A 1 149 CYS 149 149 149 CYS CYS B . n 
A 1 150 LYS 150 150 150 LYS LYS B . n 
A 1 151 PHE 151 151 151 PHE PHE B . n 
A 1 152 TRP 152 152 152 TRP TRP B . n 
A 1 153 ASN 153 153 153 ASN ASN B . n 
A 1 154 GLN 154 154 154 GLN GLN B . n 
A 1 155 ARG 155 155 155 ARG ARG B . n 
A 1 156 ASP 156 156 156 ASP ASP B . n 
A 1 157 ILE 157 157 157 ILE ILE B . n 
A 1 158 ARG 158 158 158 ARG ARG B . n 
A 1 159 THR 159 159 159 THR THR B . n 
A 1 160 ARG 160 160 160 ARG ARG B . n 
A 1 161 ILE 161 161 161 ILE ILE B . n 
A 1 162 GLU 162 162 162 GLU GLU B . n 
A 1 163 ALA 163 163 163 ALA ALA B . n 
A 1 164 LEU 164 164 164 LEU LEU B . n 
A 1 165 LEU 165 165 165 LEU LEU B . n 
A 1 166 LEU 166 166 166 LEU LEU B . n 
A 1 167 VAL 167 167 167 VAL VAL B . n 
A 1 168 ARG 168 168 168 ARG ARG B . n 
A 1 169 ASP 169 169 169 ASP ASP B . n 
A 1 170 MET 170 170 170 MET MET B . n 
A 1 171 THR 171 171 171 THR THR B . n 
A 1 172 THR 172 172 172 THR THR B . n 
A 1 173 CYS 173 173 173 CYS CYS B . n 
A 1 174 PRO 174 174 174 PRO PRO B . n 
A 1 175 LEU 175 175 175 LEU LEU B . n 
A 1 176 PRO 176 176 176 PRO PRO B . n 
A 1 177 LYS 177 177 177 LYS LYS B . n 
A 1 178 GLY 178 178 178 GLY GLY B . n 
A 1 179 THR 179 179 179 THR THR B . n 
A 1 180 LEU 180 180 180 LEU LEU B . n 
A 1 181 ASP 181 181 181 ASP ASP B . n 
A 1 182 GLY 182 182 182 GLY GLY B . n 
A 1 183 PHE 183 183 183 PHE PHE B . n 
A 1 184 VAL 184 184 184 VAL VAL B . n 
A 1 185 ALA 185 185 185 ALA ALA B . n 
A 1 186 HIS 186 186 186 HIS HIS B . n 
A 1 187 ASP 187 187 187 ASP ASP B . n 
A 1 188 SER 188 188 188 SER SER B . n 
A 1 189 ILE 189 189 189 ILE ILE B . n 
A 1 190 HIS 190 190 190 HIS HIS B . n 
A 1 191 ASP 191 191 191 ASP ASP B . n 
A 1 192 CYS 192 192 192 CYS CYS B . n 
A 1 193 ALA 193 193 193 ALA ALA B . n 
A 1 194 LYS 194 194 194 LYS LYS B . n 
A 1 195 ASP 195 195 195 ASP ASP B . n 
A 1 196 ILE 196 196 196 ILE ILE B . n 
A 1 197 LEU 197 197 197 LEU LEU B . n 
A 1 198 MET 198 198 198 MET MET B . n 
A 1 199 MET 199 199 199 MET MET B . n 
A 1 200 LYS 200 200 200 LYS LYS B . n 
A 1 201 TYR 201 201 201 TYR TYR B . n 
A 1 202 ALA 202 202 202 ALA ALA B . n 
A 1 203 LEU 203 203 203 LEU LEU B . n 
A 1 204 ARG 204 204 204 ARG ARG B . n 
A 1 205 TYR 205 205 205 TYR TYR B . n 
A 1 206 ALA 206 206 206 ALA ALA B . n 
A 1 207 MET 207 207 207 MET MET B . n 
A 1 208 GLY 208 208 208 GLY GLY B . n 
A 1 209 LEU 209 209 209 LEU LEU B . n 
A 1 210 GLU 210 210 210 GLU GLU B . n 
A 1 211 ASP 211 211 211 ASP ASP B . n 
A 1 212 ALA 212 212 212 ALA ALA B . n 
A 1 213 PRO 213 213 213 PRO PRO B . n 
A 1 214 SER 214 214 214 SER SER B . n 
A 1 215 GLU 215 215 215 GLU GLU B . n 
A 1 216 GLU 216 216 216 GLU GLU B . n 
A 1 217 GLU 217 217 217 GLU GLU B . n 
A 1 218 CYS 218 218 218 CYS CYS B . n 
A 1 219 ASP 219 219 219 ASP ASP B . n 
A 1 220 PRO 220 220 220 PRO PRO B . n 
A 1 221 LEU 221 221 221 LEU LEU B . n 
A 1 222 SER 222 222 222 SER SER B . n 
A 1 223 LEU 223 223 223 LEU LEU B . n 
A 1 224 PRO 224 224 224 PRO PRO B . n 
A 1 225 THR 225 225 ?   ?   ?   B . n 
A 1 226 LYS 226 226 ?   ?   ?   B . n 
A 1 227 ARG 227 227 ?   ?   ?   B . n 
B 1 1   MET 1   1   1   MET MET A . n 
B 1 2   PHE 2   2   2   PHE PHE A . n 
B 1 3   ASP 3   3   3   ASP ASP A . n 
B 1 4   PHE 4   4   4   PHE PHE A . n 
B 1 5   ILE 5   5   5   ILE ILE A . n 
B 1 6   ILE 6   6   6   ILE ILE A . n 
B 1 7   ASP 7   7   7   ASP ASP A . n 
B 1 8   PHE 8   8   8   PHE PHE A . n 
B 1 9   GLU 9   9   9   GLU GLU A . n 
B 1 10  THR 10  10  10  THR THR A . n 
B 1 11  MET 11  11  11  MET MET A . n 
B 1 12  GLY 12  12  12  GLY GLY A . n 
B 1 13  SER 13  13  13  SER SER A . n 
B 1 14  GLY 14  14  14  GLY GLY A . n 
B 1 15  GLU 15  15  15  GLU GLU A . n 
B 1 16  LYS 16  16  16  LYS LYS A . n 
B 1 17  ALA 17  17  17  ALA ALA A . n 
B 1 18  ALA 18  18  18  ALA ALA A . n 
B 1 19  VAL 19  19  19  VAL VAL A . n 
B 1 20  ILE 20  20  20  ILE ILE A . n 
B 1 21  ASP 21  21  21  ASP ASP A . n 
B 1 22  LEU 22  22  22  LEU LEU A . n 
B 1 23  ALA 23  23  23  ALA ALA A . n 
B 1 24  VAL 24  24  24  VAL VAL A . n 
B 1 25  ILE 25  25  25  ILE ILE A . n 
B 1 26  ALA 26  26  26  ALA ALA A . n 
B 1 27  PHE 27  27  27  PHE PHE A . n 
B 1 28  ASP 28  28  28  ASP ASP A . n 
B 1 29  PRO 29  29  29  PRO PRO A . n 
B 1 30  ASN 30  30  30  ASN ASN A . n 
B 1 31  PRO 31  31  31  PRO PRO A . n 
B 1 32  GLU 32  32  32  GLU GLU A . n 
B 1 33  VAL 33  33  33  VAL VAL A . n 
B 1 34  VAL 34  34  34  VAL VAL A . n 
B 1 35  GLU 35  35  35  GLU GLU A . n 
B 1 36  THR 36  36  36  THR THR A . n 
B 1 37  PHE 37  37  37  PHE PHE A . n 
B 1 38  ASP 38  38  38  ASP ASP A . n 
B 1 39  GLU 39  39  39  GLU GLU A . n 
B 1 40  LEU 40  40  40  LEU LEU A . n 
B 1 41  VAL 41  41  41  VAL VAL A . n 
B 1 42  SER 42  42  42  SER SER A . n 
B 1 43  ARG 43  43  43  ARG ARG A . n 
B 1 44  GLY 44  44  44  GLY GLY A . n 
B 1 45  ILE 45  45  45  ILE ILE A . n 
B 1 46  LYS 46  46  46  LYS LYS A . n 
B 1 47  ILE 47  47  47  ILE ILE A . n 
B 1 48  LYS 48  48  48  LYS LYS A . n 
B 1 49  PHE 49  49  49  PHE PHE A . n 
B 1 50  ASP 50  50  50  ASP ASP A . n 
B 1 51  LEU 51  51  51  LEU LEU A . n 
B 1 52  LYS 52  52  52  LYS LYS A . n 
B 1 53  SER 53  53  53  SER SER A . n 
B 1 54  GLN 54  54  54  GLN GLN A . n 
B 1 55  LYS 55  55  55  LYS LYS A . n 
B 1 56  GLY 56  56  56  GLY GLY A . n 
B 1 57  HIS 57  57  57  HIS HIS A . n 
B 1 58  ARG 58  58  58  ARG ARG A . n 
B 1 59  LEU 59  59  59  LEU LEU A . n 
B 1 60  PHE 60  60  60  PHE PHE A . n 
B 1 61  THR 61  61  61  THR THR A . n 
B 1 62  LYS 62  62  62  LYS LYS A . n 
B 1 63  SER 63  63  63  SER SER A . n 
B 1 64  THR 64  64  64  THR THR A . n 
B 1 65  ILE 65  65  65  ILE ILE A . n 
B 1 66  GLU 66  66  66  GLU GLU A . n 
B 1 67  TRP 67  67  67  TRP TRP A . n 
B 1 68  TRP 68  68  68  TRP TRP A . n 
B 1 69  LYS 69  69  69  LYS LYS A . n 
B 1 70  ASN 70  70  70  ASN ASN A . n 
B 1 71  GLN 71  71  71  GLN GLN A . n 
B 1 72  SER 72  72  72  SER SER A . n 
B 1 73  PRO 73  73  73  PRO PRO A . n 
B 1 74  GLU 74  74  74  GLU GLU A . n 
B 1 75  ALA 75  75  75  ALA ALA A . n 
B 1 76  ARG 76  76  76  ARG ARG A . n 
B 1 77  LYS 77  77  77  LYS LYS A . n 
B 1 78  ASN 78  78  78  ASN ASN A . n 
B 1 79  ILE 79  79  79  ILE ILE A . n 
B 1 80  ALA 80  80  80  ALA ALA A . n 
B 1 81  PRO 81  81  81  PRO PRO A . n 
B 1 82  SER 82  82  82  SER SER A . n 
B 1 83  ASP 83  83  83  ASP ASP A . n 
B 1 84  GLU 84  84  84  GLU GLU A . n 
B 1 85  ASP 85  85  85  ASP ASP A . n 
B 1 86  VAL 86  86  86  VAL VAL A . n 
B 1 87  ALA 87  87  87  ALA ALA A . n 
B 1 88  THR 88  88  88  THR THR A . n 
B 1 89  ILE 89  89  89  ILE ILE A . n 
B 1 90  ALA 90  90  90  ALA ALA A . n 
B 1 91  GLY 91  91  91  GLY GLY A . n 
B 1 92  ILE 92  92  92  ILE ILE A . n 
B 1 93  ALA 93  93  93  ALA ALA A . n 
B 1 94  LYS 94  94  94  LYS LYS A . n 
B 1 95  PHE 95  95  95  PHE PHE A . n 
B 1 96  ASN 96  96  96  ASN ASN A . n 
B 1 97  ASP 97  97  97  ASP ASP A . n 
B 1 98  TYR 98  98  98  TYR TYR A . n 
B 1 99  ILE 99  99  99  ILE ILE A . n 
B 1 100 ASN 100 100 100 ASN ASN A . n 
B 1 101 ALA 101 101 101 ALA ALA A . n 
B 1 102 HIS 102 102 102 HIS HIS A . n 
B 1 103 ASN 103 103 103 ASN ASN A . n 
B 1 104 ILE 104 104 104 ILE ILE A . n 
B 1 105 ASP 105 105 105 ASP ASP A . n 
B 1 106 PRO 106 106 106 PRO PRO A . n 
B 1 107 TRP 107 107 107 TRP TRP A . n 
B 1 108 LYS 108 108 108 LYS LYS A . n 
B 1 109 SER 109 109 109 SER SER A . n 
B 1 110 GLN 110 110 110 GLN GLN A . n 
B 1 111 GLY 111 111 111 GLY GLY A . n 
B 1 112 TRP 112 112 112 TRP TRP A . n 
B 1 113 CYS 113 113 113 CYS CYS A . n 
B 1 114 ARG 114 114 114 ARG ARG A . n 
B 1 115 GLY 115 115 115 GLY GLY A . n 
B 1 116 MET 116 116 116 MET MET A . n 
B 1 117 SER 117 117 117 SER SER A . n 
B 1 118 PHE 118 118 118 PHE PHE A . n 
B 1 119 ASP 119 119 119 ASP ASP A . n 
B 1 120 PHE 120 120 120 PHE PHE A . n 
B 1 121 PRO 121 121 121 PRO PRO A . n 
B 1 122 ILE 122 122 122 ILE ILE A . n 
B 1 123 LEU 123 123 123 LEU LEU A . n 
B 1 124 VAL 124 124 124 VAL VAL A . n 
B 1 125 ASP 125 125 125 ASP ASP A . n 
B 1 126 LEU 126 126 126 LEU LEU A . n 
B 1 127 ILE 127 127 127 ILE ILE A . n 
B 1 128 ARG 128 128 128 ARG ARG A . n 
B 1 129 ASP 129 129 129 ASP ASP A . n 
B 1 130 ILE 130 130 130 ILE ILE A . n 
B 1 131 GLN 131 131 131 GLN GLN A . n 
B 1 132 ARG 132 132 132 ARG ARG A . n 
B 1 133 LEU 133 133 133 LEU LEU A . n 
B 1 134 ASN 134 134 134 ASN ASN A . n 
B 1 135 GLY 135 135 135 GLY GLY A . n 
B 1 136 VAL 136 136 136 VAL VAL A . n 
B 1 137 SER 137 137 137 SER SER A . n 
B 1 138 GLU 138 138 138 GLU GLU A . n 
B 1 139 ASN 139 139 139 ASN ASN A . n 
B 1 140 GLU 140 140 140 GLU GLU A . n 
B 1 141 LEU 141 141 141 LEU LEU A . n 
B 1 142 ASP 142 142 142 ASP ASP A . n 
B 1 143 THR 143 143 143 THR THR A . n 
B 1 144 PHE 144 144 144 PHE PHE A . n 
B 1 145 LYS 145 145 145 LYS LYS A . n 
B 1 146 LEU 146 146 146 LEU LEU A . n 
B 1 147 GLU 147 147 147 GLU GLU A . n 
B 1 148 PRO 148 148 148 PRO PRO A . n 
B 1 149 CYS 149 149 149 CYS CYS A . n 
B 1 150 LYS 150 150 150 LYS LYS A . n 
B 1 151 PHE 151 151 151 PHE PHE A . n 
B 1 152 TRP 152 152 152 TRP TRP A . n 
B 1 153 ASN 153 153 153 ASN ASN A . n 
B 1 154 GLN 154 154 154 GLN GLN A . n 
B 1 155 ARG 155 155 155 ARG ARG A . n 
B 1 156 ASP 156 156 156 ASP ASP A . n 
B 1 157 ILE 157 157 157 ILE ILE A . n 
B 1 158 ARG 158 158 158 ARG ARG A . n 
B 1 159 THR 159 159 159 THR THR A . n 
B 1 160 ARG 160 160 160 ARG ARG A . n 
B 1 161 ILE 161 161 161 ILE ILE A . n 
B 1 162 GLU 162 162 162 GLU GLU A . n 
B 1 163 ALA 163 163 163 ALA ALA A . n 
B 1 164 LEU 164 164 164 LEU LEU A . n 
B 1 165 LEU 165 165 165 LEU LEU A . n 
B 1 166 LEU 166 166 166 LEU LEU A . n 
B 1 167 VAL 167 167 167 VAL VAL A . n 
B 1 168 ARG 168 168 168 ARG ARG A . n 
B 1 169 ASP 169 169 169 ASP ASP A . n 
B 1 170 MET 170 170 170 MET MET A . n 
B 1 171 THR 171 171 171 THR THR A . n 
B 1 172 THR 172 172 172 THR THR A . n 
B 1 173 CYS 173 173 173 CYS CYS A . n 
B 1 174 PRO 174 174 174 PRO PRO A . n 
B 1 175 LEU 175 175 175 LEU LEU A . n 
B 1 176 PRO 176 176 176 PRO PRO A . n 
B 1 177 LYS 177 177 177 LYS LYS A . n 
B 1 178 GLY 178 178 178 GLY GLY A . n 
B 1 179 THR 179 179 179 THR THR A . n 
B 1 180 LEU 180 180 180 LEU LEU A . n 
B 1 181 ASP 181 181 181 ASP ASP A . n 
B 1 182 GLY 182 182 182 GLY GLY A . n 
B 1 183 PHE 183 183 183 PHE PHE A . n 
B 1 184 VAL 184 184 184 VAL VAL A . n 
B 1 185 ALA 185 185 185 ALA ALA A . n 
B 1 186 HIS 186 186 186 HIS HIS A . n 
B 1 187 ASP 187 187 187 ASP ASP A . n 
B 1 188 SER 188 188 188 SER SER A . n 
B 1 189 ILE 189 189 189 ILE ILE A . n 
B 1 190 HIS 190 190 190 HIS HIS A . n 
B 1 191 ASP 191 191 191 ASP ASP A . n 
B 1 192 CYS 192 192 192 CYS CYS A . n 
B 1 193 ALA 193 193 193 ALA ALA A . n 
B 1 194 LYS 194 194 194 LYS LYS A . n 
B 1 195 ASP 195 195 195 ASP ASP A . n 
B 1 196 ILE 196 196 196 ILE ILE A . n 
B 1 197 LEU 197 197 197 LEU LEU A . n 
B 1 198 MET 198 198 198 MET MET A . n 
B 1 199 MET 199 199 199 MET MET A . n 
B 1 200 LYS 200 200 200 LYS LYS A . n 
B 1 201 TYR 201 201 201 TYR TYR A . n 
B 1 202 ALA 202 202 202 ALA ALA A . n 
B 1 203 LEU 203 203 203 LEU LEU A . n 
B 1 204 ARG 204 204 204 ARG ARG A . n 
B 1 205 TYR 205 205 205 TYR TYR A . n 
B 1 206 ALA 206 206 206 ALA ALA A . n 
B 1 207 MET 207 207 207 MET MET A . n 
B 1 208 GLY 208 208 208 GLY GLY A . n 
B 1 209 LEU 209 209 209 LEU LEU A . n 
B 1 210 GLU 210 210 210 GLU GLU A . n 
B 1 211 ASP 211 211 211 ASP ASP A . n 
B 1 212 ALA 212 212 212 ALA ALA A . n 
B 1 213 PRO 213 213 213 PRO PRO A . n 
B 1 214 SER 214 214 214 SER SER A . n 
B 1 215 GLU 215 215 215 GLU GLU A . n 
B 1 216 GLU 216 216 216 GLU GLU A . n 
B 1 217 GLU 217 217 217 GLU GLU A . n 
B 1 218 CYS 218 218 218 CYS CYS A . n 
B 1 219 ASP 219 219 219 ASP ASP A . n 
B 1 220 PRO 220 220 220 PRO PRO A . n 
B 1 221 LEU 221 221 221 LEU LEU A . n 
B 1 222 SER 222 222 222 SER SER A . n 
B 1 223 LEU 223 223 223 LEU LEU A . n 
B 1 224 PRO 224 224 224 PRO PRO A . n 
B 1 225 THR 225 225 ?   ?   ?   A . n 
B 1 226 LYS 226 226 ?   ?   ?   A . n 
B 1 227 ARG 227 227 ?   ?   ?   A . 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 
C 2 HOH 1  301 74 HOH HOH B . 
C 2 HOH 2  302 28 HOH HOH B . 
C 2 HOH 3  303 61 HOH HOH B . 
C 2 HOH 4  304 5  HOH HOH B . 
C 2 HOH 5  305 84 HOH HOH B . 
C 2 HOH 6  306 9  HOH HOH B . 
C 2 HOH 7  307 19 HOH HOH B . 
C 2 HOH 8  308 24 HOH HOH B . 
C 2 HOH 9  309 18 HOH HOH B . 
C 2 HOH 10 310 35 HOH HOH B . 
C 2 HOH 11 311 16 HOH HOH B . 
C 2 HOH 12 312 65 HOH HOH B . 
C 2 HOH 13 313 12 HOH HOH B . 
C 2 HOH 14 314 43 HOH HOH B . 
C 2 HOH 15 315 86 HOH HOH B . 
C 2 HOH 16 316 37 HOH HOH B . 
C 2 HOH 17 317 93 HOH HOH B . 
C 2 HOH 18 318 33 HOH HOH B . 
C 2 HOH 19 319 90 HOH HOH B . 
C 2 HOH 20 320 22 HOH HOH B . 
C 2 HOH 21 321 69 HOH HOH B . 
C 2 HOH 22 322 54 HOH HOH B . 
C 2 HOH 23 323 27 HOH HOH B . 
C 2 HOH 24 324 31 HOH HOH B . 
C 2 HOH 25 325 4  HOH HOH B . 
C 2 HOH 26 326 60 HOH HOH B . 
C 2 HOH 27 327 13 HOH HOH B . 
C 2 HOH 28 328 67 HOH HOH B . 
C 2 HOH 29 329 34 HOH HOH B . 
C 2 HOH 30 330 48 HOH HOH B . 
C 2 HOH 31 331 81 HOH HOH B . 
C 2 HOH 32 332 39 HOH HOH B . 
C 2 HOH 33 333 53 HOH HOH B . 
C 2 HOH 34 334 92 HOH HOH B . 
C 2 HOH 35 335 32 HOH HOH B . 
C 2 HOH 36 336 79 HOH HOH B . 
C 2 HOH 37 337 2  HOH HOH B . 
C 2 HOH 38 338 20 HOH HOH B . 
C 2 HOH 39 339 73 HOH HOH B . 
C 2 HOH 40 340 87 HOH HOH B . 
C 2 HOH 41 341 46 HOH HOH B . 
C 2 HOH 42 342 1  HOH HOH B . 
C 2 HOH 43 343 75 HOH HOH B . 
C 2 HOH 44 344 95 HOH HOH B . 
C 2 HOH 45 345 71 HOH HOH B . 
C 2 HOH 46 346 77 HOH HOH B . 
C 2 HOH 47 347 50 HOH HOH B . 
C 2 HOH 48 348 85 HOH HOH B . 
C 2 HOH 49 349 94 HOH HOH B . 
C 2 HOH 50 350 52 HOH HOH B . 
C 2 HOH 51 351 78 HOH HOH B . 
C 2 HOH 52 352 63 HOH HOH B . 
C 2 HOH 53 353 68 HOH HOH B . 
C 2 HOH 54 354 83 HOH HOH B . 
C 2 HOH 55 355 59 HOH HOH B . 
D 2 HOH 1  301 49 HOH HOH A . 
D 2 HOH 2  302 56 HOH HOH A . 
D 2 HOH 3  303 66 HOH HOH A . 
D 2 HOH 4  304 21 HOH HOH A . 
D 2 HOH 5  305 11 HOH HOH A . 
D 2 HOH 6  306 80 HOH HOH A . 
D 2 HOH 7  307 3  HOH HOH A . 
D 2 HOH 8  308 47 HOH HOH A . 
D 2 HOH 9  309 25 HOH HOH A . 
D 2 HOH 10 310 14 HOH HOH A . 
D 2 HOH 11 311 7  HOH HOH A . 
D 2 HOH 12 312 45 HOH HOH A . 
D 2 HOH 13 313 72 HOH HOH A . 
D 2 HOH 14 314 26 HOH HOH A . 
D 2 HOH 15 315 8  HOH HOH A . 
D 2 HOH 16 316 23 HOH HOH A . 
D 2 HOH 17 317 62 HOH HOH A . 
D 2 HOH 18 318 41 HOH HOH A . 
D 2 HOH 19 319 42 HOH HOH A . 
D 2 HOH 20 320 55 HOH HOH A . 
D 2 HOH 21 321 51 HOH HOH A . 
D 2 HOH 22 322 36 HOH HOH A . 
D 2 HOH 23 323 15 HOH HOH A . 
D 2 HOH 24 324 70 HOH HOH A . 
D 2 HOH 25 325 29 HOH HOH A . 
D 2 HOH 26 326 89 HOH HOH A . 
D 2 HOH 27 327 30 HOH HOH A . 
D 2 HOH 28 328 88 HOH HOH A . 
D 2 HOH 29 329 76 HOH HOH A . 
D 2 HOH 30 330 58 HOH HOH A . 
D 2 HOH 31 331 91 HOH HOH A . 
D 2 HOH 32 332 17 HOH HOH A . 
D 2 HOH 33 333 40 HOH HOH A . 
D 2 HOH 34 334 57 HOH HOH A . 
D 2 HOH 35 335 44 HOH HOH A . 
D 2 HOH 36 336 82 HOH HOH A . 
D 2 HOH 37 337 38 HOH HOH A . 
D 2 HOH 38 338 6  HOH HOH A . 
D 2 HOH 39 339 10 HOH HOH A . 
D 2 HOH 40 340 64 HOH HOH A . 
# 
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 B VAL 34  ? CG1 ? A VAL 34  CG1 
2   1 Y 1 B VAL 34  ? CG2 ? A VAL 34  CG2 
3   1 Y 1 B GLU 35  ? CG  ? A GLU 35  CG  
4   1 Y 1 B GLU 35  ? CD  ? A GLU 35  CD  
5   1 Y 1 B GLU 35  ? OE1 ? A GLU 35  OE1 
6   1 Y 1 B GLU 35  ? OE2 ? A GLU 35  OE2 
7   1 Y 1 B ASP 38  ? CG  ? A ASP 38  CG  
8   1 Y 1 B ASP 38  ? OD1 ? A ASP 38  OD1 
9   1 Y 1 B ASP 38  ? OD2 ? A ASP 38  OD2 
10  1 Y 1 B LYS 46  ? CG  ? A LYS 46  CG  
11  1 Y 1 B LYS 46  ? CD  ? A LYS 46  CD  
12  1 Y 1 B LYS 46  ? CE  ? A LYS 46  CE  
13  1 Y 1 B LYS 46  ? NZ  ? A LYS 46  NZ  
14  1 Y 1 B GLU 66  ? CG  ? A GLU 66  CG  
15  1 Y 1 B GLU 66  ? CD  ? A GLU 66  CD  
16  1 Y 1 B GLU 66  ? OE1 ? A GLU 66  OE1 
17  1 Y 1 B GLU 66  ? OE2 ? A GLU 66  OE2 
18  1 Y 1 B GLU 74  ? CG  ? A GLU 74  CG  
19  1 Y 1 B GLU 74  ? CD  ? A GLU 74  CD  
20  1 Y 1 B GLU 74  ? OE1 ? A GLU 74  OE1 
21  1 Y 1 B GLU 74  ? OE2 ? A GLU 74  OE2 
22  1 Y 1 B ARG 76  ? CG  ? A ARG 76  CG  
23  1 Y 1 B ARG 76  ? CD  ? A ARG 76  CD  
24  1 Y 1 B ARG 76  ? NE  ? A ARG 76  NE  
25  1 Y 1 B ARG 76  ? CZ  ? A ARG 76  CZ  
26  1 Y 1 B ARG 76  ? NH1 ? A ARG 76  NH1 
27  1 Y 1 B ARG 76  ? NH2 ? A ARG 76  NH2 
28  1 Y 1 B LYS 77  ? CG  ? A LYS 77  CG  
29  1 Y 1 B LYS 77  ? CD  ? A LYS 77  CD  
30  1 Y 1 B LYS 77  ? CE  ? A LYS 77  CE  
31  1 Y 1 B LYS 77  ? NZ  ? A LYS 77  NZ  
32  1 Y 1 B ASN 78  ? CG  ? A ASN 78  CG  
33  1 Y 1 B ASN 78  ? OD1 ? A ASN 78  OD1 
34  1 Y 1 B ASN 78  ? ND2 ? A ASN 78  ND2 
35  1 Y 1 B ILE 79  ? CG1 ? A ILE 79  CG1 
36  1 Y 1 B ILE 79  ? CG2 ? A ILE 79  CG2 
37  1 Y 1 B ILE 79  ? CD1 ? A ILE 79  CD1 
38  1 Y 1 B ASN 103 ? CG  ? A ASN 103 CG  
39  1 Y 1 B ASN 103 ? OD1 ? A ASN 103 OD1 
40  1 Y 1 B ASN 103 ? ND2 ? A ASN 103 ND2 
41  1 Y 1 B ASP 169 ? CG  ? A ASP 169 CG  
42  1 Y 1 B ASP 169 ? OD1 ? A ASP 169 OD1 
43  1 Y 1 B ASP 169 ? OD2 ? A ASP 169 OD2 
44  1 Y 1 B LYS 177 ? CG  ? A LYS 177 CG  
45  1 Y 1 B LYS 177 ? CD  ? A LYS 177 CD  
46  1 Y 1 B LYS 177 ? CE  ? A LYS 177 CE  
47  1 Y 1 B LYS 177 ? NZ  ? A LYS 177 NZ  
48  1 Y 1 B LEU 180 ? CG  ? A LEU 180 CG  
49  1 Y 1 B LEU 180 ? CD1 ? A LEU 180 CD1 
50  1 Y 1 B LEU 180 ? CD2 ? A LEU 180 CD2 
51  1 Y 1 B ASP 181 ? CG  ? A ASP 181 CG  
52  1 Y 1 B ASP 181 ? OD1 ? A ASP 181 OD1 
53  1 Y 1 B ASP 181 ? OD2 ? A ASP 181 OD2 
54  1 Y 1 B VAL 184 ? CG1 ? A VAL 184 CG1 
55  1 Y 1 B VAL 184 ? CG2 ? A VAL 184 CG2 
56  1 Y 1 B LYS 194 ? CG  ? A LYS 194 CG  
57  1 Y 1 B LYS 194 ? CD  ? A LYS 194 CD  
58  1 Y 1 B LYS 194 ? CE  ? A LYS 194 CE  
59  1 Y 1 B LYS 194 ? NZ  ? A LYS 194 NZ  
60  1 Y 1 B LYS 200 ? CG  ? A LYS 200 CG  
61  1 Y 1 B LYS 200 ? CD  ? A LYS 200 CD  
62  1 Y 1 B LYS 200 ? CE  ? A LYS 200 CE  
63  1 Y 1 B LYS 200 ? NZ  ? A LYS 200 NZ  
64  1 Y 1 B ARG 204 ? CG  ? A ARG 204 CG  
65  1 Y 1 B ARG 204 ? CD  ? A ARG 204 CD  
66  1 Y 1 B ARG 204 ? NE  ? A ARG 204 NE  
67  1 Y 1 B ARG 204 ? CZ  ? A ARG 204 CZ  
68  1 Y 1 B ARG 204 ? NH1 ? A ARG 204 NH1 
69  1 Y 1 B ARG 204 ? NH2 ? A ARG 204 NH2 
70  1 Y 1 B GLU 210 ? CG  ? A GLU 210 CG  
71  1 Y 1 B GLU 210 ? CD  ? A GLU 210 CD  
72  1 Y 1 B GLU 210 ? OE1 ? A GLU 210 OE1 
73  1 Y 1 B GLU 210 ? OE2 ? A GLU 210 OE2 
74  1 Y 1 B ASP 211 ? CG  ? A ASP 211 CG  
75  1 Y 1 B ASP 211 ? OD1 ? A ASP 211 OD1 
76  1 Y 1 B ASP 211 ? OD2 ? A ASP 211 OD2 
77  1 Y 1 B GLU 215 ? CG  ? A GLU 215 CG  
78  1 Y 1 B GLU 215 ? CD  ? A GLU 215 CD  
79  1 Y 1 B GLU 215 ? OE1 ? A GLU 215 OE1 
80  1 Y 1 B GLU 215 ? OE2 ? A GLU 215 OE2 
81  1 Y 1 B GLU 216 ? CG  ? A GLU 216 CG  
82  1 Y 1 B GLU 216 ? CD  ? A GLU 216 CD  
83  1 Y 1 B GLU 216 ? OE1 ? A GLU 216 OE1 
84  1 Y 1 B GLU 216 ? OE2 ? A GLU 216 OE2 
85  1 Y 1 B GLU 217 ? CG  ? A GLU 217 CG  
86  1 Y 1 B GLU 217 ? CD  ? A GLU 217 CD  
87  1 Y 1 B GLU 217 ? OE1 ? A GLU 217 OE1 
88  1 Y 1 B GLU 217 ? OE2 ? A GLU 217 OE2 
89  1 Y 1 B ASP 219 ? CG  ? A ASP 219 CG  
90  1 Y 1 B ASP 219 ? OD1 ? A ASP 219 OD1 
91  1 Y 1 B ASP 219 ? OD2 ? A ASP 219 OD2 
92  1 Y 1 B LEU 221 ? CG  ? A LEU 221 CG  
93  1 Y 1 B LEU 221 ? CD1 ? A LEU 221 CD1 
94  1 Y 1 B LEU 221 ? CD2 ? A LEU 221 CD2 
95  1 Y 1 B LEU 223 ? CG  ? A LEU 223 CG  
96  1 Y 1 B LEU 223 ? CD1 ? A LEU 223 CD1 
97  1 Y 1 B LEU 223 ? CD2 ? A LEU 223 CD2 
98  1 Y 1 B PRO 224 ? CG  ? A PRO 224 CG  
99  1 Y 1 B PRO 224 ? CD  ? A PRO 224 CD  
100 1 Y 1 A VAL 34  ? CG1 ? B VAL 34  CG1 
101 1 Y 1 A VAL 34  ? CG2 ? B VAL 34  CG2 
102 1 Y 1 A GLU 35  ? CG  ? B GLU 35  CG  
103 1 Y 1 A GLU 35  ? CD  ? B GLU 35  CD  
104 1 Y 1 A GLU 35  ? OE1 ? B GLU 35  OE1 
105 1 Y 1 A GLU 35  ? OE2 ? B GLU 35  OE2 
106 1 Y 1 A ASP 38  ? CG  ? B ASP 38  CG  
107 1 Y 1 A ASP 38  ? OD1 ? B ASP 38  OD1 
108 1 Y 1 A ASP 38  ? OD2 ? B ASP 38  OD2 
109 1 Y 1 A LYS 46  ? CG  ? B LYS 46  CG  
110 1 Y 1 A LYS 46  ? CD  ? B LYS 46  CD  
111 1 Y 1 A LYS 46  ? CE  ? B LYS 46  CE  
112 1 Y 1 A LYS 46  ? NZ  ? B LYS 46  NZ  
113 1 Y 1 A GLU 66  ? CG  ? B GLU 66  CG  
114 1 Y 1 A GLU 66  ? CD  ? B GLU 66  CD  
115 1 Y 1 A GLU 66  ? OE1 ? B GLU 66  OE1 
116 1 Y 1 A GLU 66  ? OE2 ? B GLU 66  OE2 
117 1 Y 1 A GLU 74  ? CG  ? B GLU 74  CG  
118 1 Y 1 A GLU 74  ? CD  ? B GLU 74  CD  
119 1 Y 1 A GLU 74  ? OE1 ? B GLU 74  OE1 
120 1 Y 1 A GLU 74  ? OE2 ? B GLU 74  OE2 
121 1 Y 1 A ARG 76  ? CG  ? B ARG 76  CG  
122 1 Y 1 A ARG 76  ? CD  ? B ARG 76  CD  
123 1 Y 1 A ARG 76  ? NE  ? B ARG 76  NE  
124 1 Y 1 A ARG 76  ? CZ  ? B ARG 76  CZ  
125 1 Y 1 A ARG 76  ? NH1 ? B ARG 76  NH1 
126 1 Y 1 A ARG 76  ? NH2 ? B ARG 76  NH2 
127 1 Y 1 A LYS 77  ? CG  ? B LYS 77  CG  
128 1 Y 1 A LYS 77  ? CD  ? B LYS 77  CD  
129 1 Y 1 A LYS 77  ? CE  ? B LYS 77  CE  
130 1 Y 1 A LYS 77  ? NZ  ? B LYS 77  NZ  
131 1 Y 1 A ASN 78  ? CG  ? B ASN 78  CG  
132 1 Y 1 A ASN 78  ? OD1 ? B ASN 78  OD1 
133 1 Y 1 A ASN 78  ? ND2 ? B ASN 78  ND2 
134 1 Y 1 A ILE 79  ? CG1 ? B ILE 79  CG1 
135 1 Y 1 A ILE 79  ? CG2 ? B ILE 79  CG2 
136 1 Y 1 A ILE 79  ? CD1 ? B ILE 79  CD1 
137 1 Y 1 A ASN 103 ? CG  ? B ASN 103 CG  
138 1 Y 1 A ASN 103 ? OD1 ? B ASN 103 OD1 
139 1 Y 1 A ASN 103 ? ND2 ? B ASN 103 ND2 
140 1 Y 1 A ASP 169 ? CG  ? B ASP 169 CG  
141 1 Y 1 A ASP 169 ? OD1 ? B ASP 169 OD1 
142 1 Y 1 A ASP 169 ? OD2 ? B ASP 169 OD2 
143 1 Y 1 A LYS 177 ? CG  ? B LYS 177 CG  
144 1 Y 1 A LYS 177 ? CD  ? B LYS 177 CD  
145 1 Y 1 A LYS 177 ? CE  ? B LYS 177 CE  
146 1 Y 1 A LYS 177 ? NZ  ? B LYS 177 NZ  
147 1 Y 1 A LEU 180 ? CG  ? B LEU 180 CG  
148 1 Y 1 A LEU 180 ? CD1 ? B LEU 180 CD1 
149 1 Y 1 A LEU 180 ? CD2 ? B LEU 180 CD2 
150 1 Y 1 A ASP 181 ? CG  ? B ASP 181 CG  
151 1 Y 1 A ASP 181 ? OD1 ? B ASP 181 OD1 
152 1 Y 1 A ASP 181 ? OD2 ? B ASP 181 OD2 
153 1 Y 1 A VAL 184 ? CG1 ? B VAL 184 CG1 
154 1 Y 1 A VAL 184 ? CG2 ? B VAL 184 CG2 
155 1 Y 1 A LYS 194 ? CG  ? B LYS 194 CG  
156 1 Y 1 A LYS 194 ? CD  ? B LYS 194 CD  
157 1 Y 1 A LYS 194 ? CE  ? B LYS 194 CE  
158 1 Y 1 A LYS 194 ? NZ  ? B LYS 194 NZ  
159 1 Y 1 A LYS 200 ? CG  ? B LYS 200 CG  
160 1 Y 1 A LYS 200 ? CD  ? B LYS 200 CD  
161 1 Y 1 A LYS 200 ? CE  ? B LYS 200 CE  
162 1 Y 1 A LYS 200 ? NZ  ? B LYS 200 NZ  
163 1 Y 1 A ARG 204 ? CG  ? B ARG 204 CG  
164 1 Y 1 A ARG 204 ? CD  ? B ARG 204 CD  
165 1 Y 1 A ARG 204 ? NE  ? B ARG 204 NE  
166 1 Y 1 A ARG 204 ? CZ  ? B ARG 204 CZ  
167 1 Y 1 A ARG 204 ? NH1 ? B ARG 204 NH1 
168 1 Y 1 A ARG 204 ? NH2 ? B ARG 204 NH2 
169 1 Y 1 A GLU 210 ? CG  ? B GLU 210 CG  
170 1 Y 1 A GLU 210 ? CD  ? B GLU 210 CD  
171 1 Y 1 A GLU 210 ? OE1 ? B GLU 210 OE1 
172 1 Y 1 A GLU 210 ? OE2 ? B GLU 210 OE2 
173 1 Y 1 A ASP 211 ? CG  ? B ASP 211 CG  
174 1 Y 1 A ASP 211 ? OD1 ? B ASP 211 OD1 
175 1 Y 1 A ASP 211 ? OD2 ? B ASP 211 OD2 
176 1 Y 1 A GLU 215 ? CG  ? B GLU 215 CG  
177 1 Y 1 A GLU 215 ? CD  ? B GLU 215 CD  
178 1 Y 1 A GLU 215 ? OE1 ? B GLU 215 OE1 
179 1 Y 1 A GLU 215 ? OE2 ? B GLU 215 OE2 
180 1 Y 1 A GLU 216 ? CG  ? B GLU 216 CG  
181 1 Y 1 A GLU 216 ? CD  ? B GLU 216 CD  
182 1 Y 1 A GLU 216 ? OE1 ? B GLU 216 OE1 
183 1 Y 1 A GLU 216 ? OE2 ? B GLU 216 OE2 
184 1 Y 1 A GLU 217 ? CG  ? B GLU 217 CG  
185 1 Y 1 A GLU 217 ? CD  ? B GLU 217 CD  
186 1 Y 1 A GLU 217 ? OE1 ? B GLU 217 OE1 
187 1 Y 1 A GLU 217 ? OE2 ? B GLU 217 OE2 
188 1 Y 1 A ASP 219 ? CG  ? B ASP 219 CG  
189 1 Y 1 A ASP 219 ? OD1 ? B ASP 219 OD1 
190 1 Y 1 A ASP 219 ? OD2 ? B ASP 219 OD2 
191 1 Y 1 A LEU 221 ? CG  ? B LEU 221 CG  
192 1 Y 1 A LEU 221 ? CD1 ? B LEU 221 CD1 
193 1 Y 1 A LEU 221 ? CD2 ? B LEU 221 CD2 
194 1 Y 1 A LEU 223 ? CG  ? B LEU 223 CG  
195 1 Y 1 A LEU 223 ? CD1 ? B LEU 223 CD1 
196 1 Y 1 A LEU 223 ? CD2 ? B LEU 223 CD2 
197 1 Y 1 A PRO 224 ? CG  ? B PRO 224 CG  
198 1 Y 1 A PRO 224 ? CD  ? B PRO 224 CD  
# 
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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8KEN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.330 
_cell.length_a_esd                 ? 
_cell.length_b                     82.182 
_cell.length_b_esd                 ? 
_cell.length_c                     115.931 
_cell.length_c_esd                 ? 
_cell.volume                       727229.605 
_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                         8KEN 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_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                   8KEN 
_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             3.50 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.91 
_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          'EVAPORATION, RECRYSTALLIZATION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.02M Magnesium Chloride, 0.1M Sodium acetate trihydrate pH 4.6, 30% v/v (+/-)-2-Methyl-2,4-pentanediol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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 EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-08-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          47.17 
_reflns.entry_id                                       8KEN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.38 
_reflns.d_resolution_low                               67.05 
_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                                     29905 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.1 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.093 
_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                                    2.38 
_reflns_shell.d_res_low                                     7.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4290 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.968 
_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                               52.04 
_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                                 8KEN 
_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                            2.38 
_refine.ls_d_res_low                             67.05 
_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                     29805 
_refine.ls_number_reflns_R_free                  1467 
_refine.ls_number_reflns_R_work                  28338 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.75 
_refine.ls_percent_reflns_R_free                 4.92 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2424 
_refine.ls_R_factor_R_free                       0.2844 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2402 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.5099 
_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                            0.3532 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.38 
_refine_hist.d_res_low                        67.05 
_refine_hist.number_atoms_solvent             95 
_refine_hist.number_atoms_total               3481 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3386 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0075 ? 3466 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8948 ? 4714 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0602 ? 530  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0080 ? 612  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 5.8958 ? 470  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.38 2.47 . . 128 2792 99.86 . . . . 0.3157 . . . . . . . . . . . 0.3704 
'X-RAY DIFFRACTION' 2.47 2.57 . . 151 2806 99.83 . . . . 0.2780 . . . . . . . . . . . 0.3442 
'X-RAY DIFFRACTION' 2.57 2.68 . . 147 2773 99.69 . . . . 0.2688 . . . . . . . . . . . 0.2928 
'X-RAY DIFFRACTION' 2.68 2.82 . . 144 2813 99.76 . . . . 0.2588 . . . . . . . . . . . 0.2934 
'X-RAY DIFFRACTION' 2.82 3.00 . . 124 2805 99.80 . . . . 0.2531 . . . . . . . . . . . 0.3292 
'X-RAY DIFFRACTION' 3.00 3.23 . . 188 2784 99.63 . . . . 0.2532 . . . . . . . . . . . 0.2975 
'X-RAY DIFFRACTION' 3.23 3.56 . . 146 2820 99.83 . . . . 0.2344 . . . . . . . . . . . 0.3154 
'X-RAY DIFFRACTION' 3.56 4.07 . . 160 2833 99.87 . . . . 0.2262 . . . . . . . . . . . 0.2505 
'X-RAY DIFFRACTION' 4.07 5.13 . . 150 2886 99.90 . . . . 0.2141 . . . . . . . . . . . 0.2593 
'X-RAY DIFFRACTION' 5.13 7.53 . . 129 3026 99.40 . . . . 0.2427 . . . . . . . . . . . 0.2815 
# 
_struct.entry_id                     8KEN 
_struct.title                        'Structure of DexA reveal the novel mechanism of DNA catalysis' 
_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        8KEN 
_struct_keywords.text            'DNA binding, DNA cut, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN' 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    EXOD_BPT4 
_struct_ref.pdbx_db_accession          P04536 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MFDFIIDFETMGSGEKAAVIDLAVIAFDPNPEVVETFDELVSRGIKIKFDLKSQKGHRLFTKSTIEWWKNQSPEARKNIA
PSDEDVSTIDGIAKFNDYINAHNIDPWKSQGWCRGMSFDFPILVDLIRDIQRLNGVSENELDTFKLEPCKFWNQRDIRTR
IEALLLVRDMTTCPLPKGTLDGFVAHDSIHDCAKDILMMKYALRYAMGLEDAPSEEECDPLSLPTKR
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8KEN B 1 ? 227 ? P04536 1 ? 227 ? 1 227 
2 1 8KEN A 1 ? 227 ? P04536 1 ? 227 ? 1 227 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8KEN ALA B 87 ? UNP P04536 SER 87 conflict 87 1 
1 8KEN ALA B 90 ? UNP P04536 ASP 90 conflict 90 2 
2 8KEN ALA A 87 ? UNP P04536 SER 87 conflict 87 3 
2 8KEN ALA A 90 ? UNP P04536 ASP 90 conflict 90 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3250  ? 
1 MORE         -5    ? 
1 'SSA (A^2)'  19640 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 36  ? GLY A 44  ? THR B 36  GLY B 44  1 ? 9  
HELX_P HELX_P2  AA2 LEU A 51  ? LYS A 55  ? LEU B 51  LYS B 55  5 ? 5  
HELX_P HELX_P3  AA3 THR A 61  ? ASN A 70  ? THR B 61  ASN B 70  1 ? 10 
HELX_P HELX_P4  AA4 SER A 72  ? ASN A 78  ? SER B 72  ASN B 78  1 ? 7  
HELX_P HELX_P5  AA5 ALA A 87  ? ALA A 101 ? ALA B 87  ALA B 101 1 ? 15 
HELX_P HELX_P6  AA6 GLY A 115 ? ASN A 134 ? GLY B 115 ASN B 134 1 ? 20 
HELX_P HELX_P7  AA7 SER A 137 ? LEU A 141 ? SER B 137 LEU B 141 5 ? 5  
HELX_P HELX_P8  AA8 LYS A 150 ? TRP A 152 ? LYS B 150 TRP B 152 5 ? 3  
HELX_P HELX_P9  AA9 ILE A 157 ? LEU A 166 ? ILE B 157 LEU B 166 1 ? 10 
HELX_P HELX_P10 AB1 ASP A 187 ? MET A 207 ? ASP B 187 MET B 207 1 ? 21 
HELX_P HELX_P11 AB2 ASP A 219 ? LEU A 223 ? ASP B 219 LEU B 223 5 ? 5  
HELX_P HELX_P12 AB3 THR B 36  ? GLY B 44  ? THR A 36  GLY A 44  1 ? 9  
HELX_P HELX_P13 AB4 LEU B 51  ? LYS B 55  ? LEU A 51  LYS A 55  5 ? 5  
HELX_P HELX_P14 AB5 THR B 61  ? ASN B 70  ? THR A 61  ASN A 70  1 ? 10 
HELX_P HELX_P15 AB6 SER B 72  ? ILE B 79  ? SER A 72  ILE A 79  1 ? 8  
HELX_P HELX_P16 AB7 ALA B 87  ? ALA B 101 ? ALA A 87  ALA A 101 1 ? 15 
HELX_P HELX_P17 AB8 GLY B 115 ? ASN B 134 ? GLY A 115 ASN A 134 1 ? 20 
HELX_P HELX_P18 AB9 SER B 137 ? LEU B 141 ? SER A 137 LEU A 141 5 ? 5  
HELX_P HELX_P19 AC1 LYS B 150 ? TRP B 152 ? LYS A 150 TRP A 152 5 ? 3  
HELX_P HELX_P20 AC2 ILE B 157 ? LEU B 166 ? ILE A 157 LEU A 166 1 ? 10 
HELX_P HELX_P21 AC3 ASP B 187 ? GLY B 208 ? ASP A 187 GLY A 208 1 ? 22 
HELX_P HELX_P22 AC4 SER B 214 ? CYS B 218 ? SER A 214 CYS A 218 5 ? 5  
HELX_P HELX_P23 AC5 ASP B 219 ? LEU B 223 ? ASP A 219 LEU A 223 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
# 
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 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? 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 ILE A 45  ? LYS A 48  ? ILE B 45  LYS B 48  
AA1 2 VAL A 19  ? PHE A 27  ? VAL B 19  PHE B 27  
AA1 3 ASP A 3   ? THR A 10  ? ASP B 3   THR B 10  
AA1 4 GLY A 111 ? CYS A 113 ? GLY B 111 CYS B 113 
AA1 5 GLN A 154 ? ASP A 156 ? GLN B 154 ASP B 156 
AA2 1 ILE B 45  ? LYS B 48  ? ILE A 45  LYS A 48  
AA2 2 VAL B 19  ? PHE B 27  ? VAL A 19  PHE A 27  
AA2 3 ASP B 3   ? THR B 10  ? ASP A 3   THR A 10  
AA2 4 GLY B 111 ? CYS B 113 ? GLY A 111 CYS A 113 
AA2 5 GLN B 154 ? ASP B 156 ? GLN A 154 ASP A 156 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 47  ? O ILE B 47  N LEU A 22  ? N LEU B 22  
AA1 2 3 O ILE A 20  ? O ILE B 20  N GLU A 9   ? N GLU B 9   
AA1 3 4 N ILE A 6   ? N ILE B 6   O TRP A 112 ? O TRP B 112 
AA1 4 5 N GLY A 111 ? N GLY B 111 O ARG A 155 ? O ARG B 155 
AA2 1 2 O ILE B 47  ? O ILE A 47  N LEU B 22  ? N LEU A 22  
AA2 2 3 O ILE B 20  ? O ILE A 20  N GLU B 9   ? N GLU A 9   
AA2 3 4 N PHE B 4   ? N PHE A 4   O TRP B 112 ? O TRP A 112 
AA2 4 5 N GLY B 111 ? N GLY A 111 O ARG B 155 ? O ARG A 155 
# 
_pdbx_entry_details.entry_id                   8KEN 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O B HOH 346 ? ? O B HOH 348 ? ? 1.89 
2 1 O B HOH 350 ? ? O B HOH 355 ? ? 2.01 
3 1 O A ARG 58  ? ? O A HOH 301 ? ? 2.13 
4 1 O A PRO 224 ? ? O A HOH 302 ? ? 2.16 
# 
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 ASP B 7   ? ? -165.83 117.88 
2 1 HIS B 102 ? ? -140.23 38.72  
3 1 PHE B 118 ? ? -99.29  -63.36 
4 1 ASP B 142 ? ? -166.45 95.52  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       355 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.93 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 B THR 225 ? A THR 225 
2 1 Y 1 B LYS 226 ? A LYS 226 
3 1 Y 1 B ARG 227 ? A ARG 227 
4 1 Y 1 A THR 225 ? B THR 225 
5 1 Y 1 A LYS 226 ? B LYS 226 
6 1 Y 1 A ARG 227 ? B ARG 227 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'China Postdoctoral Science Foundation' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2020M682420 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             other 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'We used the structure from alpha fold prediction as the starting model' 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8KEN 
_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]   0.013101 
_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]   0.012168 
_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]   0.008626 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? 42.50185 -6.29942  3.59181   1.000 54.52626  ? 1   MET B N   1 
ATOM   2    C CA  . MET A 1 1   ? 41.31244 -5.55187  3.16704   1.000 62.51293  ? 1   MET B CA  1 
ATOM   3    C C   . MET A 1 1   ? 40.22108 -5.49905  4.23240   1.000 60.60102  ? 1   MET B C   1 
ATOM   4    O O   . MET A 1 1   ? 39.56041 -6.50694  4.51212   1.000 58.92114  ? 1   MET B O   1 
ATOM   5    C CB  . MET A 1 1   ? 40.71863 -6.14977  1.89320   1.000 60.02195  ? 1   MET B CB  1 
ATOM   6    C CG  . MET A 1 1   ? 39.93362 -5.13766  1.06101   1.000 61.04224  ? 1   MET B CG  1 
ATOM   7    S SD  . MET A 1 1   ? 38.39902 -5.79815  0.36457   1.000 70.65633  ? 1   MET B SD  1 
ATOM   8    C CE  . MET A 1 1   ? 37.52610 -6.37365  1.82678   1.000 58.01666  ? 1   MET B CE  1 
ATOM   9    N N   . PHE A 1 2   ? 40.00984 -4.31610  4.79998   1.000 58.03082  ? 2   PHE B N   1 
ATOM   10   C CA  . PHE A 1 2   ? 38.98837 -4.12790  5.81978   1.000 60.80387  ? 2   PHE B CA  1 
ATOM   11   C C   . PHE A 1 2   ? 37.73137 -3.46477  5.24801   1.000 56.41284  ? 2   PHE B C   1 
ATOM   12   O O   . PHE A 1 2   ? 37.75693 -2.81224  4.20153   1.000 59.34059  ? 2   PHE B O   1 
ATOM   13   C CB  . PHE A 1 2   ? 39.54448 -3.29727  6.97998   1.000 59.52962  ? 2   PHE B CB  1 
ATOM   14   C CG  . PHE A 1 2   ? 40.33304 -4.10417  7.98014   1.000 60.31778  ? 2   PHE B CG  1 
ATOM   15   C CD1 . PHE A 1 2   ? 40.35791 -5.48823  7.91041   1.000 62.31869  ? 2   PHE B CD1 1 
ATOM   16   C CD2 . PHE A 1 2   ? 41.05642 -3.47672  8.98469   1.000 62.88232  ? 2   PHE B CD2 1 
ATOM   17   C CE1 . PHE A 1 2   ? 41.09078 -6.23851  8.82660   1.000 58.82938  ? 2   PHE B CE1 1 
ATOM   18   C CE2 . PHE A 1 2   ? 41.78337 -4.21879  9.90307   1.000 62.82614  ? 2   PHE B CE2 1 
ATOM   19   C CZ  . PHE A 1 2   ? 41.79643 -5.60223  9.81953   1.000 60.45494  ? 2   PHE B CZ  1 
ATOM   20   N N   . ASP A 1 3   ? 36.61778 -3.69141  5.93619   1.000 53.12051  ? 3   ASP B N   1 
ATOM   21   C CA  . ASP A 1 3   ? 35.37539 -2.94384  5.79382   1.000 51.10730  ? 3   ASP B CA  1 
ATOM   22   C C   . ASP A 1 3   ? 35.34337 -1.84463  6.86291   1.000 47.91244  ? 3   ASP B C   1 
ATOM   23   O O   . ASP A 1 3   ? 36.19698 -1.80664  7.74475   1.000 52.71700  ? 3   ASP B O   1 
ATOM   24   C CB  . ASP A 1 3   ? 34.18475 -3.89811  5.94592   1.000 49.25600  ? 3   ASP B CB  1 
ATOM   25   C CG  . ASP A 1 3   ? 33.97935 -4.79649  4.72569   1.000 49.78977  ? 3   ASP B CG  1 
ATOM   26   O OD1 . ASP A 1 3   ? 34.58350 -4.55093  3.65962   1.000 47.75884  ? 3   ASP B OD1 1 
ATOM   27   O OD2 . ASP A 1 3   ? 33.21230 -5.76797  4.84145   1.000 50.94344  ? 3   ASP B OD2 1 
ATOM   28   N N   . PHE A 1 4   ? 34.36013 -0.94113  6.79802   1.000 46.09284  ? 4   PHE B N   1 
ATOM   29   C CA  . PHE A 1 4   ? 34.22043 0.05346   7.86665   1.000 43.89998  ? 4   PHE B CA  1 
ATOM   30   C C   . PHE A 1 4   ? 32.75387 0.35595   8.19837   1.000 48.95256  ? 4   PHE B C   1 
ATOM   31   O O   . PHE A 1 4   ? 31.83393 0.14431   7.39832   1.000 44.18309  ? 4   PHE B O   1 
ATOM   32   C CB  . PHE A 1 4   ? 34.94265 1.37221   7.53843   1.000 44.59641  ? 4   PHE B CB  1 
ATOM   33   C CG  . PHE A 1 4   ? 34.45036 2.04150   6.28723   1.000 48.10383  ? 4   PHE B CG  1 
ATOM   34   C CD1 . PHE A 1 4   ? 34.85012 1.59127   5.03767   1.000 49.41487  ? 4   PHE B CD1 1 
ATOM   35   C CD2 . PHE A 1 4   ? 33.57677 3.11487   6.36053   1.000 46.39318  ? 4   PHE B CD2 1 
ATOM   36   C CE1 . PHE A 1 4   ? 34.39320 2.20348   3.88081   1.000 49.63723  ? 4   PHE B CE1 1 
ATOM   37   C CE2 . PHE A 1 4   ? 33.10808 3.73134   5.21133   1.000 44.76079  ? 4   PHE B CE2 1 
ATOM   38   C CZ  . PHE A 1 4   ? 33.51665 3.27326   3.96981   1.000 50.45853  ? 4   PHE B CZ  1 
ATOM   39   N N   . ILE A 1 5   ? 32.56620 0.88074   9.41006   1.000 45.78286  ? 5   ILE B N   1 
ATOM   40   C CA  . ILE A 1 5   ? 31.28004 1.31322   9.93054   1.000 42.34142  ? 5   ILE B CA  1 
ATOM   41   C C   . ILE A 1 5   ? 31.36610 2.79257   10.28742  1.000 37.87476  ? 5   ILE B C   1 
ATOM   42   O O   . ILE A 1 5   ? 32.40192 3.26340   10.75240  1.000 40.37324  ? 5   ILE B O   1 
ATOM   43   C CB  . ILE A 1 5   ? 30.86796 0.47575   11.16265  1.000 47.22577  ? 5   ILE B CB  1 
ATOM   44   C CG1 . ILE A 1 5   ? 29.36863 0.66319   11.47068  1.000 40.95762  ? 5   ILE B CG1 1 
ATOM   45   C CG2 . ILE A 1 5   ? 31.74928 0.81948   12.38064  1.000 41.17300  ? 5   ILE B CG2 1 
ATOM   46   C CD1 . ILE A 1 5   ? 28.96655 0.15821   12.82912  1.000 38.73414  ? 5   ILE B CD1 1 
ATOM   47   N N   . ILE A 1 6   ? 30.27436 3.52636   10.07778  1.000 40.53800  ? 6   ILE B N   1 
ATOM   48   C CA  . ILE A 1 6   ? 30.20177 4.93819   10.43765  1.000 43.00082  ? 6   ILE B CA  1 
ATOM   49   C C   . ILE A 1 6   ? 28.92318 5.17739   11.22326  1.000 39.47541  ? 6   ILE B C   1 
ATOM   50   O O   . ILE A 1 6   ? 27.98125 4.38017   11.18182  1.000 41.21102  ? 6   ILE B O   1 
ATOM   51   C CB  . ILE A 1 6   ? 30.22855 5.87363   9.20730   1.000 40.77484  ? 6   ILE B CB  1 
ATOM   52   C CG1 . ILE A 1 6   ? 29.02697 5.56595   8.29979   1.000 31.54593  ? 6   ILE B CG1 1 
ATOM   53   C CG2 . ILE A 1 6   ? 31.60624 5.81267   8.48911   1.000 35.87687  ? 6   ILE B CG2 1 
ATOM   54   C CD1 . ILE A 1 6   ? 28.76260 6.62254   7.24200   1.000 33.12462  ? 6   ILE B CD1 1 
ATOM   55   N N   . ASP A 1 7   ? 28.89519 6.29885   11.93365  1.000 35.70935  ? 7   ASP B N   1 
ATOM   56   C CA  . ASP A 1 7   ? 27.69576 6.67477   12.67758  1.000 43.03042  ? 7   ASP B CA  1 
ATOM   57   C C   . ASP A 1 7   ? 27.80784 8.12704   13.09519  1.000 39.20420  ? 7   ASP B C   1 
ATOM   58   O O   . ASP A 1 7   ? 28.68545 8.46609   13.89866  1.000 37.58001  ? 7   ASP B O   1 
ATOM   59   C CB  . ASP A 1 7   ? 27.49885 5.82782   13.91371  1.000 37.28593  ? 7   ASP B CB  1 
ATOM   60   C CG  . ASP A 1 7   ? 26.16708 6.12246   14.57791  1.000 39.37083  ? 7   ASP B CG  1 
ATOM   61   O OD1 . ASP A 1 7   ? 25.17938 5.48708   14.18741  1.000 41.50958  ? 7   ASP B OD1 1 
ATOM   62   O OD2 . ASP A 1 7   ? 26.09789 7.03630   15.42864  1.000 33.79951  ? 7   ASP B OD2 1 
ATOM   63   N N   . PHE A 1 8   ? 26.89385 8.96176   12.61261  1.000 35.36033  ? 8   PHE B N   1 
ATOM   64   C CA  . PHE A 1 8   ? 26.80563 10.34005  13.07390  1.000 40.27898  ? 8   PHE B CA  1 
ATOM   65   C C   . PHE A 1 8   ? 25.89913 10.42290  14.29999  1.000 39.72654  ? 8   PHE B C   1 
ATOM   66   O O   . PHE A 1 8   ? 24.98767 9.61088   14.48291  1.000 41.43032  ? 8   PHE B O   1 
ATOM   67   C CB  . PHE A 1 8   ? 26.23689 11.26016  11.98835  1.000 34.60277  ? 8   PHE B CB  1 
ATOM   68   C CG  . PHE A 1 8   ? 27.15686 11.48845  10.80049  1.000 38.55752  ? 8   PHE B CG  1 
ATOM   69   C CD1 . PHE A 1 8   ? 28.04865 12.54377  10.78538  1.000 36.56555  ? 8   PHE B CD1 1 
ATOM   70   C CD2 . PHE A 1 8   ? 27.10328 10.65196  9.68639   1.000 39.19309  ? 8   PHE B CD2 1 
ATOM   71   C CE1 . PHE A 1 8   ? 28.86133 12.74386  9.71153   1.000 36.59553  ? 8   PHE B CE1 1 
ATOM   72   C CE2 . PHE A 1 8   ? 27.92566 10.86415  8.59035   1.000 35.10264  ? 8   PHE B CE2 1 
ATOM   73   C CZ  . PHE A 1 8   ? 28.78549 11.91594  8.60367   1.000 34.92347  ? 8   PHE B CZ  1 
ATOM   74   N N   . GLU A 1 9   ? 26.16453 11.40766  15.14585  1.000 39.22068  ? 9   GLU B N   1 
ATOM   75   C CA  . GLU A 1 9   ? 25.13117 12.01640  15.96480  1.000 41.77285  ? 9   GLU B CA  1 
ATOM   76   C C   . GLU A 1 9   ? 24.84673 13.37084  15.33900  1.000 41.44343  ? 9   GLU B C   1 
ATOM   77   O O   . GLU A 1 9   ? 25.77414 14.04170  14.88139  1.000 40.56034  ? 9   GLU B O   1 
ATOM   78   C CB  . GLU A 1 9   ? 25.55521 12.14231  17.43069  1.000 37.56418  ? 9   GLU B CB  1 
ATOM   79   C CG  . GLU A 1 9   ? 26.11185 10.82370  18.03179  1.000 36.91752  ? 9   GLU B CG  1 
ATOM   80   C CD  . GLU A 1 9   ? 25.22468 9.58682   17.77796  1.000 48.24031  ? 9   GLU B CD  1 
ATOM   81   O OE1 . GLU A 1 9   ? 23.98631 9.70910   17.83107  1.000 41.26517  ? 9   GLU B OE1 1 
ATOM   82   O OE2 . GLU A 1 9   ? 25.77632 8.47979   17.53984  1.000 55.85778  ? 9   GLU B OE2 1 
ATOM   83   N N   . THR A 1 10  ? 23.56522 13.73586  15.22745  1.000 40.80166  ? 10  THR B N   1 
ATOM   84   C CA  . THR A 1 10  ? 23.18191 14.95612  14.52177  1.000 38.28562  ? 10  THR B CA  1 
ATOM   85   C C   . THR A 1 10  ? 22.18420 15.76914  15.33524  1.000 41.62359  ? 10  THR B C   1 
ATOM   86   O O   . THR A 1 10  ? 21.63839 15.31882  16.34720  1.000 42.24846  ? 10  THR B O   1 
ATOM   87   C CB  . THR A 1 10  ? 22.55401 14.66378  13.15179  1.000 38.21025  ? 10  THR B CB  1 
ATOM   88   O OG1 . THR A 1 10  ? 21.17265 14.32527  13.33437  1.000 41.00361  ? 10  THR B OG1 1 
ATOM   89   C CG2 . THR A 1 10  ? 23.26828 13.52155  12.44820  1.000 36.35819  ? 10  THR B CG2 1 
ATOM   90   N N   . MET A 1 11  ? 21.95380 16.98844  14.85120  1.000 39.71959  ? 11  MET B N   1 
ATOM   91   C CA  . MET A 1 11  ? 20.88052 17.86242  15.29700  1.000 44.53757  ? 11  MET B CA  1 
ATOM   92   C C   . MET A 1 11  ? 19.81526 18.06086  14.22102  1.000 45.43586  ? 11  MET B C   1 
ATOM   93   O O   . MET A 1 11  ? 19.13613 19.09105  14.21428  1.000 48.14677  ? 11  MET B O   1 
ATOM   94   C CB  . MET A 1 11  ? 21.44978 19.21578  15.70745  1.000 45.25637  ? 11  MET B CB  1 
ATOM   95   C CG  . MET A 1 11  ? 22.22262 19.19667  16.99812  1.000 53.78215  ? 11  MET B CG  1 
ATOM   96   S SD  . MET A 1 11  ? 21.21436 19.48088  18.46365  1.000 64.81032  ? 11  MET B SD  1 
ATOM   97   C CE  . MET A 1 11  ? 22.06203 20.91829  19.12207  1.000 54.75497  ? 11  MET B CE  1 
ATOM   98   N N   . GLY A 1 12  ? 19.65915 17.10299  13.31323  1.000 41.95862  ? 12  GLY B N   1 
ATOM   99   C CA  . GLY A 1 12  ? 18.88859 17.34307  12.10595  1.000 43.10248  ? 12  GLY B CA  1 
ATOM   100  C C   . GLY A 1 12  ? 18.67610 16.04765  11.35569  1.000 47.50812  ? 12  GLY B C   1 
ATOM   101  O O   . GLY A 1 12  ? 19.21771 15.00105  11.71854  1.000 44.41916  ? 12  GLY B O   1 
ATOM   102  N N   . SER A 1 13  ? 17.91619 16.14162  10.25981  1.000 46.43247  ? 13  SER B N   1 
ATOM   103  C CA  . SER A 1 13  ? 17.31988 14.96097  9.65062   1.000 43.02286  ? 13  SER B CA  1 
ATOM   104  C C   . SER A 1 13  ? 17.83484 14.68835  8.24734   1.000 47.65632  ? 13  SER B C   1 
ATOM   105  O O   . SER A 1 13  ? 18.18477 13.54099  7.93412   1.000 61.18656  ? 13  SER B O   1 
ATOM   106  C CB  . SER A 1 13  ? 15.77975 15.10188  9.60352   1.000 54.67109  ? 13  SER B CB  1 
ATOM   107  O OG  . SER A 1 13  ? 15.22998 15.36179  10.89053  1.000 58.21326  ? 13  SER B OG  1 
ATOM   108  N N   . GLY A 1 14  ? 17.85791 15.67536  7.36315   1.000 35.62092  ? 14  GLY B N   1 
ATOM   109  C CA  . GLY A 1 14  ? 18.24278 15.39964  5.99086   1.000 41.94597  ? 14  GLY B CA  1 
ATOM   110  C C   . GLY A 1 14  ? 19.75654 15.28061  5.78337   1.000 39.20041  ? 14  GLY B C   1 
ATOM   111  O O   . GLY A 1 14  ? 20.54870 15.16322  6.72087   1.000 38.18955  ? 14  GLY B O   1 
ATOM   112  N N   . GLU A 1 15  ? 20.15256 15.32049  4.50477   1.000 38.68784  ? 15  GLU B N   1 
ATOM   113  C CA  . GLU A 1 15  ? 21.56751 15.22753  4.13954   1.000 31.55301  ? 15  GLU B CA  1 
ATOM   114  C C   . GLU A 1 15  ? 22.35262 16.46989  4.54779   1.000 35.06941  ? 15  GLU B C   1 
ATOM   115  O O   . GLU A 1 15  ? 23.57676 16.39541  4.68048   1.000 37.09447  ? 15  GLU B O   1 
ATOM   116  C CB  . GLU A 1 15  ? 21.71659 14.96911  2.62945   1.000 30.10250  ? 15  GLU B CB  1 
ATOM   117  C CG  . GLU A 1 15  ? 21.74646 16.22411  1.74078   1.000 33.03189  ? 15  GLU B CG  1 
ATOM   118  C CD  . GLU A 1 15  ? 21.55770 15.92495  0.24042   1.000 37.53231  ? 15  GLU B CD  1 
ATOM   119  O OE1 . GLU A 1 15  ? 21.35810 14.74356  -0.13866  1.000 37.14244  ? 15  GLU B OE1 1 
ATOM   120  O OE2 . GLU A 1 15  ? 21.63933 16.87486  -0.57121  1.000 36.06607  ? 15  GLU B OE2 1 
ATOM   121  N N   . LYS A 1 16  ? 21.68051 17.59976  4.75450   1.000 33.09499  ? 16  LYS B N   1 
ATOM   122  C CA  . LYS A 1 16  ? 22.29190 18.83149  5.22243   1.000 35.96745  ? 16  LYS B CA  1 
ATOM   123  C C   . LYS A 1 16  ? 22.29036 18.95541  6.73528   1.000 38.33358  ? 16  LYS B C   1 
ATOM   124  O O   . LYS A 1 16  ? 22.50272 20.05994  7.24779   1.000 38.66759  ? 16  LYS B O   1 
ATOM   125  C CB  . LYS A 1 16  ? 21.57691 20.05373  4.62298   1.000 39.78836  ? 16  LYS B CB  1 
ATOM   126  C CG  . LYS A 1 16  ? 21.41025 20.02726  3.10814   1.000 35.37353  ? 16  LYS B CG  1 
ATOM   127  C CD  . LYS A 1 16  ? 22.77418 20.00816  2.42793   1.000 33.40795  ? 16  LYS B CD  1 
ATOM   128  C CE  . LYS A 1 16  ? 23.72277 21.06366  3.01800   1.000 38.41708  ? 16  LYS B CE  1 
ATOM   129  N NZ  . LYS A 1 16  ? 24.84574 21.26245  2.07948   1.000 43.31736  ? 16  LYS B NZ  1 
ATOM   130  N N   . ALA A 1 17  ? 22.05559 17.85921  7.45470   1.000 38.56348  ? 17  ALA B N   1 
ATOM   131  C CA  . ALA A 1 17  ? 21.81805 17.93455  8.88900   1.000 36.40616  ? 17  ALA B CA  1 
ATOM   132  C C   . ALA A 1 17  ? 23.06204 18.40198  9.63957   1.000 42.15582  ? 17  ALA B C   1 
ATOM   133  O O   . ALA A 1 17  ? 24.18763 18.00346  9.32535   1.000 40.64525  ? 17  ALA B O   1 
ATOM   134  C CB  . ALA A 1 17  ? 21.37947 16.57459  9.41466   1.000 38.29162  ? 17  ALA B CB  1 
ATOM   135  N N   . ALA A 1 18  ? 22.84882 19.25422  10.63915  1.000 40.71411  ? 18  ALA B N   1 
ATOM   136  C CA  . ALA A 1 18  ? 23.93099 19.65487  11.52502  1.000 41.85633  ? 18  ALA B CA  1 
ATOM   137  C C   . ALA A 1 18  ? 24.47261 18.42300  12.24158  1.000 38.95640  ? 18  ALA B C   1 
ATOM   138  O O   . ALA A 1 18  ? 23.71066 17.65155  12.82751  1.000 40.27380  ? 18  ALA B O   1 
ATOM   139  C CB  . ALA A 1 18  ? 23.42926 20.70663  12.53040  1.000 42.54936  ? 18  ALA B CB  1 
ATOM   140  N N   . VAL A 1 19  ? 25.79586 18.22780  12.17462  1.000 45.92731  ? 19  VAL B N   1 
ATOM   141  C CA  . VAL A 1 19  ? 26.45572 17.03409  12.70956  1.000 42.04768  ? 19  VAL B CA  1 
ATOM   142  C C   . VAL A 1 19  ? 27.07123 17.34997  14.06209  1.000 41.19400  ? 19  VAL B C   1 
ATOM   143  O O   . VAL A 1 19  ? 27.60777 18.44519  14.28091  1.000 39.26729  ? 19  VAL B O   1 
ATOM   144  C CB  . VAL A 1 19  ? 27.53086 16.50895  11.74394  1.000 40.45047  ? 19  VAL B CB  1 
ATOM   145  C CG1 . VAL A 1 19  ? 26.88198 15.86100  10.54223  1.000 40.12010  ? 19  VAL B CG1 1 
ATOM   146  C CG2 . VAL A 1 19  ? 28.45069 17.63187  11.31697  1.000 37.50549  ? 19  VAL B CG2 1 
ATOM   147  N N   . ILE A 1 20  ? 26.98768 16.38486  14.96798  1.000 42.53323  ? 20  ILE B N   1 
ATOM   148  C CA  . ILE A 1 20  ? 27.53770 16.49633  16.31031  1.000 40.95155  ? 20  ILE B CA  1 
ATOM   149  C C   . ILE A 1 20  ? 28.85719 15.75810  16.42090  1.000 44.58189  ? 20  ILE B C   1 
ATOM   150  O O   . ILE A 1 20  ? 29.84092 16.29255  16.93613  1.000 43.90828  ? 20  ILE B O   1 
ATOM   151  C CB  . ILE A 1 20  ? 26.53655 15.95113  17.35451  1.000 43.01881  ? 20  ILE B CB  1 
ATOM   152  C CG1 . ILE A 1 20  ? 25.30106 16.85121  17.48703  1.000 43.47887  ? 20  ILE B CG1 1 
ATOM   153  C CG2 . ILE A 1 20  ? 27.22203 15.78232  18.69184  1.000 36.40881  ? 20  ILE B CG2 1 
ATOM   154  C CD1 . ILE A 1 20  ? 24.24268 16.24114  18.33983  1.000 38.36904  ? 20  ILE B CD1 1 
ATOM   155  N N   . ASP A 1 21  ? 28.87358 14.49544  15.99932  1.000 45.58400  ? 21  ASP B N   1 
ATOM   156  C CA  . ASP A 1 21  ? 30.12159 13.76032  15.90868  1.000 43.38712  ? 21  ASP B CA  1 
ATOM   157  C C   . ASP A 1 21  ? 29.97742 12.69018  14.83780  1.000 44.99846  ? 21  ASP B C   1 
ATOM   158  O O   . ASP A 1 21  ? 28.88046 12.43219  14.32112  1.000 40.05463  ? 21  ASP B O   1 
ATOM   159  C CB  . ASP A 1 21  ? 30.55490 13.17096  17.27058  1.000 42.48267  ? 21  ASP B CB  1 
ATOM   160  C CG  . ASP A 1 21  ? 29.65035 12.01678  17.77312  1.000 47.73665  ? 21  ASP B CG  1 
ATOM   161  O OD1 . ASP A 1 21  ? 29.13474 11.19874  16.98855  1.000 43.37243  ? 21  ASP B OD1 1 
ATOM   162  O OD2 . ASP A 1 21  ? 29.51406 11.88827  19.00435  1.000 52.66594  ? 21  ASP B OD2 1 
ATOM   163  N N   . LEU A 1 22  ? 31.11197 12.05991  14.52489  1.000 45.15189  ? 22  LEU B N   1 
ATOM   164  C CA  . LEU A 1 22  ? 31.19578 10.98074  13.54130  1.000 42.47603  ? 22  LEU B CA  1 
ATOM   165  C C   . LEU A 1 22  ? 32.18206 9.93768   14.05724  1.000 44.69382  ? 22  LEU B C   1 
ATOM   166  O O   . LEU A 1 22  ? 33.38106 10.22073  14.18630  1.000 40.72396  ? 22  LEU B O   1 
ATOM   167  C CB  . LEU A 1 22  ? 31.63307 11.52097  12.17717  1.000 38.72677  ? 22  LEU B CB  1 
ATOM   168  C CG  . LEU A 1 22  ? 32.06239 10.48542  11.12090  1.000 38.68475  ? 22  LEU B CG  1 
ATOM   169  C CD1 . LEU A 1 22  ? 30.97734 9.47059   10.78976  1.000 38.60339  ? 22  LEU B CD1 1 
ATOM   170  C CD2 . LEU A 1 22  ? 32.60228 11.15546  9.86511   1.000 37.37455  ? 22  LEU B CD2 1 
ATOM   171  N N   . ALA A 1 23  ? 31.68326 8.74300   14.37021  1.000 46.17952  ? 23  ALA B N   1 
ATOM   172  C CA  . ALA A 1 23  ? 32.53809 7.61893   14.72556  1.000 39.96195  ? 23  ALA B CA  1 
ATOM   173  C C   . ALA A 1 23  ? 32.70559 6.72515   13.51277  1.000 42.01790  ? 23  ALA B C   1 
ATOM   174  O O   . ALA A 1 23  ? 31.75709 6.52542   12.74631  1.000 35.62297  ? 23  ALA B O   1 
ATOM   175  C CB  . ALA A 1 23  ? 31.96133 6.80559   15.87960  1.000 35.89920  ? 23  ALA B CB  1 
ATOM   176  N N   . VAL A 1 24  ? 33.92296 6.20583   13.33559  1.000 43.77125  ? 24  VAL B N   1 
ATOM   177  C CA  . VAL A 1 24  ? 34.24490 5.30450   12.22955  1.000 40.44814  ? 24  VAL B CA  1 
ATOM   178  C C   . VAL A 1 24  ? 35.23333 4.26058   12.73019  1.000 44.71121  ? 24  VAL B C   1 
ATOM   179  O O   . VAL A 1 24  ? 36.15061 4.57918   13.49759  1.000 44.42497  ? 24  VAL B O   1 
ATOM   180  C CB  . VAL A 1 24  ? 34.78971 6.07530   11.00646  1.000 39.09933  ? 24  VAL B CB  1 
ATOM   181  C CG1 . VAL A 1 24  ? 35.69743 7.17857   11.44309  1.000 41.84439  ? 24  VAL B CG1 1 
ATOM   182  C CG2 . VAL A 1 24  ? 35.54176 5.15216   10.06565  1.000 39.39334  ? 24  VAL B CG2 1 
ATOM   183  N N   . ILE A 1 25  ? 35.01346 3.00298   12.33520  1.000 39.24782  ? 25  ILE B N   1 
ATOM   184  C CA  . ILE A 1 25  ? 35.88162 1.89575   12.71308  1.000 44.56765  ? 25  ILE B CA  1 
ATOM   185  C C   . ILE A 1 25  ? 36.09363 1.01729   11.49230  1.000 47.30994  ? 25  ILE B C   1 
ATOM   186  O O   . ILE A 1 25  ? 35.12204 0.54560   10.88700  1.000 46.08420  ? 25  ILE B O   1 
ATOM   187  C CB  . ILE A 1 25  ? 35.31828 1.04930   13.86845  1.000 46.29223  ? 25  ILE B CB  1 
ATOM   188  C CG1 . ILE A 1 25  ? 34.97620 1.92662   15.07296  1.000 43.60891  ? 25  ILE B CG1 1 
ATOM   189  C CG2 . ILE A 1 25  ? 36.35957 -0.00555  14.27894  1.000 48.23746  ? 25  ILE B CG2 1 
ATOM   190  C CD1 . ILE A 1 25  ? 34.53633 1.13012   16.29182  1.000 44.63363  ? 25  ILE B CD1 1 
ATOM   191  N N   . ALA A 1 26  ? 37.36099 0.80223   11.12833  1.000 49.82518  ? 26  ALA B N   1 
ATOM   192  C CA  . ALA A 1 26  ? 37.71484 -0.18488  10.11662  1.000 46.60606  ? 26  ALA B CA  1 
ATOM   193  C C   . ALA A 1 26  ? 37.79921 -1.55894  10.76379  1.000 51.87998  ? 26  ALA B C   1 
ATOM   194  O O   . ALA A 1 26  ? 38.25636 -1.69177  11.90160  1.000 54.49371  ? 26  ALA B O   1 
ATOM   195  C CB  . ALA A 1 26  ? 39.04207 0.17292   9.46060   1.000 49.96207  ? 26  ALA B CB  1 
ATOM   196  N N   . PHE A 1 27  ? 37.33893 -2.58176  10.05178  1.000 48.10078  ? 27  PHE B N   1 
ATOM   197  C CA  . PHE A 1 27  ? 37.21428 -3.88320  10.68188  1.000 50.46744  ? 27  PHE B CA  1 
ATOM   198  C C   . PHE A 1 27  ? 37.28283 -4.97091  9.62206   1.000 56.27587  ? 27  PHE B C   1 
ATOM   199  O O   . PHE A 1 27  ? 37.10185 -4.72384  8.42856   1.000 54.75563  ? 27  PHE B O   1 
ATOM   200  C CB  . PHE A 1 27  ? 35.92220 -3.99492  11.50202  1.000 49.40084  ? 27  PHE B CB  1 
ATOM   201  C CG  . PHE A 1 27  ? 34.65308 -4.10302  10.67286  1.000 50.64254  ? 27  PHE B CG  1 
ATOM   202  C CD1 . PHE A 1 27  ? 33.93052 -2.96886  10.31904  1.000 48.94149  ? 27  PHE B CD1 1 
ATOM   203  C CD2 . PHE A 1 27  ? 34.17708 -5.34543  10.27316  1.000 49.40358  ? 27  PHE B CD2 1 
ATOM   204  C CE1 . PHE A 1 27  ? 32.75840 -3.06849  9.57537   1.000 48.87687  ? 27  PHE B CE1 1 
ATOM   205  C CE2 . PHE A 1 27  ? 33.01986 -5.46571  9.52367   1.000 49.61076  ? 27  PHE B CE2 1 
ATOM   206  C CZ  . PHE A 1 27  ? 32.29760 -4.32532  9.17354   1.000 53.54085  ? 27  PHE B CZ  1 
ATOM   207  N N   . ASP A 1 28  ? 37.50287 -6.19500  10.10068  1.000 58.39641  ? 28  ASP B N   1 
ATOM   208  C CA  . ASP A 1 28  ? 37.75894 -7.35014  9.25661   1.000 57.42169  ? 28  ASP B CA  1 
ATOM   209  C C   . ASP A 1 28  ? 36.44428 -8.01405  8.89241   1.000 54.90907  ? 28  ASP B C   1 
ATOM   210  O O   . ASP A 1 28  ? 35.74090 -8.50145  9.78746   1.000 55.42630  ? 28  ASP B O   1 
ATOM   211  C CB  . ASP A 1 28  ? 38.66944 -8.33705  9.98575   1.000 62.08560  ? 28  ASP B CB  1 
ATOM   212  C CG  . ASP A 1 28  ? 39.24907 -9.41551  9.07629   1.000 60.47112  ? 28  ASP B CG  1 
ATOM   213  O OD1 . ASP A 1 28  ? 38.53646 -9.94907  8.19698   1.000 59.92452  ? 28  ASP B OD1 1 
ATOM   214  O OD2 . ASP A 1 28  ? 40.44326 -9.73001  9.25060   1.000 65.15191  ? 28  ASP B OD2 1 
ATOM   215  N N   . PRO A 1 29  ? 36.08117 -8.06990  7.60969   1.000 57.39243  ? 29  PRO B N   1 
ATOM   216  C CA  . PRO A 1 29  ? 34.84172 -8.76840  7.22178   1.000 57.76630  ? 29  PRO B CA  1 
ATOM   217  C C   . PRO A 1 29  ? 34.88764 -10.27138 7.40934   1.000 60.52123  ? 29  PRO B C   1 
ATOM   218  O O   . PRO A 1 29  ? 33.81991 -10.89835 7.43149   1.000 63.65033  ? 29  PRO B O   1 
ATOM   219  C CB  . PRO A 1 29  ? 34.69580 -8.42146  5.73475   1.000 56.85164  ? 29  PRO B CB  1 
ATOM   220  C CG  . PRO A 1 29  ? 36.12332 -8.11679  5.29188   1.000 57.45197  ? 29  PRO B CG  1 
ATOM   221  C CD  . PRO A 1 29  ? 36.74123 -7.42194  6.46404   1.000 52.89065  ? 29  PRO B CD  1 
ATOM   222  N N   . ASN A 1 30  ? 36.06701 -10.87318 7.51436   1.000 59.34693  ? 30  ASN B N   1 
ATOM   223  C CA  . ASN A 1 30  ? 36.15554 -12.32492 7.42717   1.000 59.92874  ? 30  ASN B CA  1 
ATOM   224  C C   . ASN A 1 30  ? 35.41399 -12.96413 8.59079   1.000 57.23302  ? 30  ASN B C   1 
ATOM   225  O O   . ASN A 1 30  ? 35.62156 -12.57056 9.74526   1.000 57.14866  ? 30  ASN B O   1 
ATOM   226  C CB  . ASN A 1 30  ? 37.61226 -12.79856 7.41843   1.000 66.64422  ? 30  ASN B CB  1 
ATOM   227  C CG  . ASN A 1 30  ? 37.72796 -14.31490 7.54134   1.000 68.56405  ? 30  ASN B CG  1 
ATOM   228  O OD1 . ASN A 1 30  ? 38.02348 -14.84380 8.61497   1.000 69.46662  ? 30  ASN B OD1 1 
ATOM   229  N ND2 . ASN A 1 30  ? 37.47302 -15.01951 6.44221   1.000 71.65849  ? 30  ASN B ND2 1 
ATOM   230  N N   . PRO A 1 31  ? 34.54999 -13.94288 8.33438   1.000 58.27397  ? 31  PRO B N   1 
ATOM   231  C CA  . PRO A 1 31  ? 33.79504 -14.55710 9.43783   1.000 62.19195  ? 31  PRO B CA  1 
ATOM   232  C C   . PRO A 1 31  ? 34.68391 -15.20440 10.48533  1.000 66.05305  ? 31  PRO B C   1 
ATOM   233  O O   . PRO A 1 31  ? 34.44559 -15.03296 11.68351  1.000 66.36855  ? 31  PRO B O   1 
ATOM   234  C CB  . PRO A 1 31  ? 32.91399 -15.60068 8.72684   1.000 61.25308  ? 31  PRO B CB  1 
ATOM   235  C CG  . PRO A 1 31  ? 32.91629 -15.22220 7.29265   1.000 56.74407  ? 31  PRO B CG  1 
ATOM   236  C CD  . PRO A 1 31  ? 34.22258 -14.53703 7.02885   1.000 61.39392  ? 31  PRO B CD  1 
ATOM   237  N N   . GLU A 1 32  ? 35.72063 -15.93197 10.06715  1.000 67.00410  ? 32  GLU B N   1 
ATOM   238  C CA  . GLU A 1 32  ? 36.49013 -16.73205 11.01049  1.000 65.76136  ? 32  GLU B CA  1 
ATOM   239  C C   . GLU A 1 32  ? 37.27827 -15.88122 11.99472  1.000 66.13096  ? 32  GLU B C   1 
ATOM   240  O O   . GLU A 1 32  ? 37.60872 -16.36379 13.08319  1.000 69.52325  ? 32  GLU B O   1 
ATOM   241  C CB  . GLU A 1 32  ? 37.40975 -17.67696 10.24293  1.000 67.81446  ? 32  GLU B CB  1 
ATOM   242  C CG  . GLU A 1 32  ? 36.67724 -18.90599 9.69778   1.000 74.10247  ? 32  GLU B CG  1 
ATOM   243  C CD  . GLU A 1 32  ? 37.27704 -19.40255 8.39970   1.000 82.85791  ? 32  GLU B CD  1 
ATOM   244  O OE1 . GLU A 1 32  ? 38.29940 -18.82665 7.96726   1.000 85.91473  ? 32  GLU B OE1 1 
ATOM   245  O OE2 . GLU A 1 32  ? 36.72538 -20.35427 7.80491   1.000 85.84473  ? 32  GLU B OE2 1 
ATOM   246  N N   . VAL A 1 33  ? 37.58059 -14.63402 11.65409  1.000 65.57573  ? 33  VAL B N   1 
ATOM   247  C CA  . VAL A 1 33  ? 38.15495 -13.71287 12.62843  1.000 67.80329  ? 33  VAL B CA  1 
ATOM   248  C C   . VAL A 1 33  ? 37.01565 -13.10130 13.43908  1.000 73.51748  ? 33  VAL B C   1 
ATOM   249  O O   . VAL A 1 33  ? 36.08169 -12.51517 12.87760  1.000 68.51096  ? 33  VAL B O   1 
ATOM   250  C CB  . VAL A 1 33  ? 38.99889 -12.62223 11.94961  1.000 65.00381  ? 33  VAL B CB  1 
ATOM   251  C CG1 . VAL A 1 33  ? 39.97398 -12.02223 12.94449  1.000 64.54155  ? 33  VAL B CG1 1 
ATOM   252  C CG2 . VAL A 1 33  ? 39.74215 -13.17915 10.75544  1.000 59.92632  ? 33  VAL B CG2 1 
ATOM   253  N N   . VAL A 1 34  ? 37.07269 -13.26810 14.75892  1.000 74.18115  ? 34  VAL B N   1 
ATOM   254  C CA  . VAL A 1 34  ? 36.24054 -12.51607 15.68660  1.000 66.67086  ? 34  VAL B CA  1 
ATOM   255  C C   . VAL A 1 34  ? 37.18821 -11.56040 16.40009  1.000 66.28391  ? 34  VAL B C   1 
ATOM   256  O O   . VAL A 1 34  ? 37.97466 -11.96521 17.26219  1.000 70.93027  ? 34  VAL B O   1 
ATOM   257  C CB  . VAL A 1 34  ? 35.48061 -13.42453 16.66262  1.000 57.82796  ? 34  VAL B CB  1 
ATOM   258  N N   . GLU A 1 35  ? 37.17234 -10.29948 15.98855  1.000 68.72922  ? 35  GLU B N   1 
ATOM   259  C CA  . GLU A 1 35  ? 37.92134 -9.26370  16.67729  1.000 62.53131  ? 35  GLU B CA  1 
ATOM   260  C C   . GLU A 1 35  ? 37.19885 -8.87587  17.96766  1.000 65.49464  ? 35  GLU B C   1 
ATOM   261  O O   . GLU A 1 35  ? 35.96501 -8.85708  18.03061  1.000 62.44107  ? 35  GLU B O   1 
ATOM   262  C CB  . GLU A 1 35  ? 38.09455 -8.05095  15.76414  1.000 55.50051  ? 35  GLU B CB  1 
ATOM   263  N N   . THR A 1 36  ? 37.97808 -8.57579  19.00613  1.000 64.49439  ? 36  THR B N   1 
ATOM   264  C CA  . THR A 1 36  ? 37.40365 -8.28357  20.31109  1.000 61.30332  ? 36  THR B CA  1 
ATOM   265  C C   . THR A 1 36  ? 36.87062 -6.85560  20.37254  1.000 58.93347  ? 36  THR B C   1 
ATOM   266  O O   . THR A 1 36  ? 37.20691 -5.99254  19.55500  1.000 54.75389  ? 36  THR B O   1 
ATOM   267  C CB  . THR A 1 36  ? 38.43596 -8.46540  21.42228  1.000 62.76153  ? 36  THR B CB  1 
ATOM   268  O OG1 . THR A 1 36  ? 39.28501 -7.31339  21.46185  1.000 56.02986  ? 36  THR B OG1 1 
ATOM   269  C CG2 . THR A 1 36  ? 39.27090 -9.70446  21.17868  1.000 65.27209  ? 36  THR B CG2 1 
ATOM   270  N N   . PHE A 1 37  ? 36.03444 -6.61581  21.38151  1.000 58.18170  ? 37  PHE B N   1 
ATOM   271  C CA  . PHE A 1 37  ? 35.51247 -5.27621  21.61789  1.000 55.06001  ? 37  PHE B CA  1 
ATOM   272  C C   . PHE A 1 37  ? 36.63838 -4.29212  21.88873  1.000 56.03243  ? 37  PHE B C   1 
ATOM   273  O O   . PHE A 1 37  ? 36.60594 -3.14578  21.42028  1.000 53.32809  ? 37  PHE B O   1 
ATOM   274  C CB  . PHE A 1 37  ? 34.53247 -5.31427  22.79283  1.000 55.98995  ? 37  PHE B CB  1 
ATOM   275  C CG  . PHE A 1 37  ? 33.86213 -4.00833  23.06790  1.000 54.98937  ? 37  PHE B CG  1 
ATOM   276  C CD1 . PHE A 1 37  ? 32.80718 -3.57022  22.27362  1.000 53.83074  ? 37  PHE B CD1 1 
ATOM   277  C CD2 . PHE A 1 37  ? 34.28496 -3.21272  24.11972  1.000 55.64392  ? 37  PHE B CD2 1 
ATOM   278  C CE1 . PHE A 1 37  ? 32.19288 -2.37098  22.52202  1.000 50.59588  ? 37  PHE B CE1 1 
ATOM   279  C CE2 . PHE A 1 37  ? 33.66459 -2.00353  24.37788  1.000 58.67187  ? 37  PHE B CE2 1 
ATOM   280  C CZ  . PHE A 1 37  ? 32.61893 -1.58415  23.57853  1.000 53.50560  ? 37  PHE B CZ  1 
ATOM   281  N N   . ASP A 1 38  ? 37.65171 -4.73135  22.63737  1.000 58.99832  ? 38  ASP B N   1 
ATOM   282  C CA  . ASP A 1 38  ? 38.72804 -3.83663  23.04461  1.000 56.31758  ? 38  ASP B CA  1 
ATOM   283  C C   . ASP A 1 38  ? 39.59595 -3.42448  21.85913  1.000 53.34425  ? 38  ASP B C   1 
ATOM   284  O O   . ASP A 1 38  ? 40.06801 -2.28212  21.80666  1.000 52.66535  ? 38  ASP B O   1 
ATOM   285  C CB  . ASP A 1 38  ? 39.56695 -4.49919  24.14087  1.000 57.14066  ? 38  ASP B CB  1 
ATOM   286  N N   . GLU A 1 39  ? 39.81638 -4.32344  20.89097  1.000 51.41368  ? 39  GLU B N   1 
ATOM   287  C CA  . GLU A 1 39  ? 40.63128 -3.91142  19.75212  1.000 56.01782  ? 39  GLU B CA  1 
ATOM   288  C C   . GLU A 1 39  ? 39.81984 -3.10428  18.75112  1.000 53.90624  ? 39  GLU B C   1 
ATOM   289  O O   . GLU A 1 39  ? 40.37285 -2.24355  18.06022  1.000 53.78812  ? 39  GLU B O   1 
ATOM   290  C CB  . GLU A 1 39  ? 41.27993 -5.10844  19.03855  1.000 58.16462  ? 39  GLU B CB  1 
ATOM   291  C CG  . GLU A 1 39  ? 40.39542 -6.31468  18.78405  1.000 64.12845  ? 39  GLU B CG  1 
ATOM   292  C CD  . GLU A 1 39  ? 41.18530 -7.47576  18.17611  1.000 67.34534  ? 39  GLU B CD  1 
ATOM   293  O OE1 . GLU A 1 39  ? 41.77854 -7.28046  17.08898  1.000 58.00588  ? 39  GLU B OE1 1 
ATOM   294  O OE2 . GLU A 1 39  ? 41.20801 -8.57741  18.77595  1.000 67.59836  ? 39  GLU B OE2 1 
ATOM   295  N N   . LEU A 1 40  ? 38.51713 -3.36188  18.64866  1.000 58.09682  ? 40  LEU B N   1 
ATOM   296  C CA  . LEU A 1 40  ? 37.68562 -2.52716  17.79224  1.000 50.12011  ? 40  LEU B CA  1 
ATOM   297  C C   . LEU A 1 40  ? 37.67499 -1.09745  18.30218  1.000 48.26552  ? 40  LEU B C   1 
ATOM   298  O O   . LEU A 1 40  ? 37.98069 -0.15744  17.56104  1.000 49.05365  ? 40  LEU B O   1 
ATOM   299  C CB  . LEU A 1 40  ? 36.27887 -3.10770  17.70811  1.000 44.49658  ? 40  LEU B CB  1 
ATOM   300  C CG  . LEU A 1 40  ? 36.20822 -4.37980  16.86567  1.000 45.53351  ? 40  LEU B CG  1 
ATOM   301  C CD1 . LEU A 1 40  ? 34.84812 -5.08884  16.98814  1.000 44.89985  ? 40  LEU B CD1 1 
ATOM   302  C CD2 . LEU A 1 40  ? 36.54172 -4.04270  15.41810  1.000 45.07409  ? 40  LEU B CD2 1 
ATOM   303  N N   . VAL A 1 41  ? 37.37949 -0.92047  19.58752  1.000 49.34307  ? 41  VAL B N   1 
ATOM   304  C CA  . VAL A 1 41  ? 37.37219 0.41885   20.16785  1.000 51.12604  ? 41  VAL B CA  1 
ATOM   305  C C   . VAL A 1 41  ? 38.71977 1.10062   19.96665  1.000 52.48016  ? 41  VAL B C   1 
ATOM   306  O O   . VAL A 1 41  ? 38.78667 2.27288   19.56952  1.000 54.54755  ? 41  VAL B O   1 
ATOM   307  C CB  . VAL A 1 41  ? 36.99165 0.35285   21.65879  1.000 53.73492  ? 41  VAL B CB  1 
ATOM   308  C CG1 . VAL A 1 41  ? 37.37124 1.65215   22.36335  1.000 51.98343  ? 41  VAL B CG1 1 
ATOM   309  C CG2 . VAL A 1 41  ? 35.50785 0.06810   21.81389  1.000 55.78186  ? 41  VAL B CG2 1 
ATOM   310  N N   . SER A 1 42  ? 39.81378 0.37438   20.22278  1.000 51.51331  ? 42  SER B N   1 
ATOM   311  C CA  . SER A 1 42  ? 41.14720 0.96147   20.12090  1.000 49.99052  ? 42  SER B CA  1 
ATOM   312  C C   . SER A 1 42  ? 41.52193 1.30009   18.68035  1.000 49.43374  ? 42  SER B C   1 
ATOM   313  O O   . SER A 1 42  ? 42.33464 2.20702   18.44916  1.000 44.11670  ? 42  SER B O   1 
ATOM   314  C CB  . SER A 1 42  ? 42.16762 0.01964   20.75188  1.000 53.21997  ? 42  SER B CB  1 
ATOM   315  O OG  . SER A 1 42  ? 42.35810 -1.11937  19.93286  1.000 61.62897  ? 42  SER B OG  1 
ATOM   316  N N   . ARG A 1 43  ? 40.92188 0.62135   17.70264  1.000 49.98551  ? 43  ARG B N   1 
ATOM   317  C CA  . ARG A 1 43  ? 41.09453 1.01379   16.30763  1.000 49.90315  ? 43  ARG B CA  1 
ATOM   318  C C   . ARG A 1 43  ? 40.18412 2.17108   15.88983  1.000 51.00753  ? 43  ARG B C   1 
ATOM   319  O O   . ARG A 1 43  ? 40.46671 2.84457   14.88998  1.000 46.33783  ? 43  ARG B O   1 
ATOM   320  C CB  . ARG A 1 43  ? 40.83519 -0.18167  15.39552  1.000 51.35965  ? 43  ARG B CB  1 
ATOM   321  C CG  . ARG A 1 43  ? 41.49333 -0.06331  14.03489  1.000 53.41795  ? 43  ARG B CG  1 
ATOM   322  C CD  . ARG A 1 43  ? 41.92644 -1.44180  13.55321  1.000 56.02972  ? 43  ARG B CD  1 
ATOM   323  N NE  . ARG A 1 43  ? 40.78056 -2.25426  13.17974  1.000 57.15567  ? 43  ARG B NE  1 
ATOM   324  C CZ  . ARG A 1 43  ? 40.70180 -3.56673  13.34652  1.000 61.34198  ? 43  ARG B CZ  1 
ATOM   325  N NH1 . ARG A 1 43  ? 41.67939 -4.24913  13.92764  1.000 58.87540  ? 43  ARG B NH1 1 
ATOM   326  N NH2 . ARG A 1 43  ? 39.61387 -4.21159  12.91760  1.000 55.63737  ? 43  ARG B NH2 1 
ATOM   327  N N   . GLY A 1 44  ? 39.08771 2.41204   16.60768  1.000 54.03605  ? 44  GLY B N   1 
ATOM   328  C CA  . GLY A 1 44  ? 38.15130 3.42086   16.17047  1.000 44.50583  ? 44  GLY B CA  1 
ATOM   329  C C   . GLY A 1 44  ? 38.67977 4.82498   16.37460  1.000 49.38345  ? 44  GLY B C   1 
ATOM   330  O O   . GLY A 1 44  ? 39.64790 5.06320   17.10984  1.000 49.09121  ? 44  GLY B O   1 
ATOM   331  N N   . ILE A 1 45  ? 38.03573 5.77890   15.69259  1.000 43.34674  ? 45  ILE B N   1 
ATOM   332  C CA  . ILE A 1 45  ? 38.21534 7.19114   15.99767  1.000 43.09109  ? 45  ILE B CA  1 
ATOM   333  C C   . ILE A 1 45  ? 36.84571 7.84333   16.12111  1.000 48.99815  ? 45  ILE B C   1 
ATOM   334  O O   . ILE A 1 45  ? 35.82480 7.29978   15.69364  1.000 47.62655  ? 45  ILE B O   1 
ATOM   335  C CB  . ILE A 1 45  ? 39.08001 7.95127   14.96262  1.000 43.36445  ? 45  ILE B CB  1 
ATOM   336  C CG1 . ILE A 1 45  ? 38.40088 8.00096   13.59644  1.000 41.93839  ? 45  ILE B CG1 1 
ATOM   337  C CG2 . ILE A 1 45  ? 40.52933 7.36241   14.86422  1.000 44.36905  ? 45  ILE B CG2 1 
ATOM   338  C CD1 . ILE A 1 45  ? 38.93352 9.12541   12.72780  1.000 46.03440  ? 45  ILE B CD1 1 
ATOM   339  N N   . LYS A 1 46  ? 36.85116 9.03296   16.71855  1.000 45.59610  ? 46  LYS B N   1 
ATOM   340  C CA  . LYS A 1 46  ? 35.67330 9.86683   16.85154  1.000 46.79722  ? 46  LYS B CA  1 
ATOM   341  C C   . LYS A 1 46  ? 36.04695 11.27107  16.42462  1.000 40.67723  ? 46  LYS B C   1 
ATOM   342  O O   . LYS A 1 46  ? 36.95343 11.86655  17.00014  1.000 47.40004  ? 46  LYS B O   1 
ATOM   343  C CB  . LYS A 1 46  ? 35.14986 9.87458   18.29233  1.000 50.23532  ? 46  LYS B CB  1 
ATOM   344  N N   . ILE A 1 47  ? 35.33582 11.80609  15.44535  1.000 41.20989  ? 47  ILE B N   1 
ATOM   345  C CA  . ILE A 1 47  ? 35.45641 13.20218  15.05626  1.000 39.77242  ? 47  ILE B CA  1 
ATOM   346  C C   . ILE A 1 47  ? 34.27783 13.94586  15.67255  1.000 47.37692  ? 47  ILE B C   1 
ATOM   347  O O   . ILE A 1 47  ? 33.11840 13.58984  15.42257  1.000 42.51251  ? 47  ILE B O   1 
ATOM   348  C CB  . ILE A 1 47  ? 35.46127 13.35870  13.52617  1.000 39.16408  ? 47  ILE B CB  1 
ATOM   349  C CG1 . ILE A 1 47  ? 36.61037 12.55510  12.89874  1.000 41.12990  ? 47  ILE B CG1 1 
ATOM   350  C CG2 . ILE A 1 47  ? 35.52915 14.81921  13.15491  1.000 39.97743  ? 47  ILE B CG2 1 
ATOM   351  C CD1 . ILE A 1 47  ? 36.27297 11.92348  11.55781  1.000 42.62482  ? 47  ILE B CD1 1 
ATOM   352  N N   . LYS A 1 48  ? 34.56405 14.96903  16.47606  1.000 42.23640  ? 48  LYS B N   1 
ATOM   353  C CA  . LYS A 1 48  ? 33.54648 15.79184  17.11527  1.000 41.42417  ? 48  LYS B CA  1 
ATOM   354  C C   . LYS A 1 48  ? 33.47179 17.12914  16.39799  1.000 48.65263  ? 48  LYS B C   1 
ATOM   355  O O   . LYS A 1 48  ? 34.50610 17.77261  16.17182  1.000 47.56845  ? 48  LYS B O   1 
ATOM   356  C CB  . LYS A 1 48  ? 33.85384 15.99256  18.59460  1.000 45.10647  ? 48  LYS B CB  1 
ATOM   357  C CG  . LYS A 1 48  ? 32.65584 16.43762  19.41767  1.000 49.41348  ? 48  LYS B CG  1 
ATOM   358  C CD  . LYS A 1 48  ? 32.98882 16.42031  20.89790  1.000 49.99320  ? 48  LYS B CD  1 
ATOM   359  C CE  . LYS A 1 48  ? 31.91445 17.08311  21.73291  1.000 49.28292  ? 48  LYS B CE  1 
ATOM   360  N NZ  . LYS A 1 48  ? 31.35245 18.31285  21.14120  1.000 51.19960  ? 48  LYS B NZ  1 
ATOM   361  N N   . PHE A 1 49  ? 32.26159 17.53805  16.01804  1.000 38.27853  ? 49  PHE B N   1 
ATOM   362  C CA  . PHE A 1 49  ? 32.12185 18.73344  15.20453  1.000 44.96854  ? 49  PHE B CA  1 
ATOM   363  C C   . PHE A 1 49  ? 31.74765 19.95722  16.03391  1.000 51.95386  ? 49  PHE B C   1 
ATOM   364  O O   . PHE A 1 49  ? 31.00107 19.87948  17.01793  1.000 51.24412  ? 49  PHE B O   1 
ATOM   365  C CB  . PHE A 1 49  ? 31.08733 18.54218  14.09157  1.000 41.83534  ? 49  PHE B CB  1 
ATOM   366  C CG  . PHE A 1 49  ? 31.40147 17.40726  13.14687  1.000 42.77688  ? 49  PHE B CG  1 
ATOM   367  C CD1 . PHE A 1 49  ? 32.26184 17.59602  12.08067  1.000 41.49808  ? 49  PHE B CD1 1 
ATOM   368  C CD2 . PHE A 1 49  ? 30.79968 16.16934  13.29623  1.000 38.44591  ? 49  PHE B CD2 1 
ATOM   369  C CE1 . PHE A 1 49  ? 32.54963 16.55327  11.20546  1.000 40.84839  ? 49  PHE B CE1 1 
ATOM   370  C CE2 . PHE A 1 49  ? 31.07275 15.13594  12.41409  1.000 39.49608  ? 49  PHE B CE2 1 
ATOM   371  C CZ  . PHE A 1 49  ? 31.93322 15.33051  11.36009  1.000 35.86726  ? 49  PHE B CZ  1 
ATOM   372  N N   . ASP A 1 50  ? 32.26451 21.10375  15.59910  1.000 51.12744  ? 50  ASP B N   1 
ATOM   373  C CA  . ASP A 1 50  ? 31.90207 22.39151  16.17792  1.000 50.95118  ? 50  ASP B CA  1 
ATOM   374  C C   . ASP A 1 50  ? 30.51207 22.78302  15.69529  1.000 49.51862  ? 50  ASP B C   1 
ATOM   375  O O   . ASP A 1 50  ? 30.34245 23.16292  14.53547  1.000 50.32480  ? 50  ASP B O   1 
ATOM   376  C CB  . ASP A 1 50  ? 32.95192 23.42931  15.80059  1.000 47.33422  ? 50  ASP B CB  1 
ATOM   377  C CG  . ASP A 1 50  ? 32.48189 24.84558  16.00186  1.000 54.07214  ? 50  ASP B CG  1 
ATOM   378  O OD1 . ASP A 1 50  ? 31.49992 25.08772  16.73748  1.000 55.86810  ? 50  ASP B OD1 1 
ATOM   379  O OD2 . ASP A 1 50  ? 33.15060 25.74590  15.46602  1.000 60.01644  ? 50  ASP B OD2 1 
ATOM   380  N N   . LEU A 1 51  ? 29.52428 22.72408  16.60009  1.000 51.76146  ? 51  LEU B N   1 
ATOM   381  C CA  . LEU A 1 51  ? 28.13535 23.01862  16.23504  1.000 47.92544  ? 51  LEU B CA  1 
ATOM   382  C C   . LEU A 1 51  ? 27.93723 24.47944  15.84074  1.000 49.43994  ? 51  LEU B C   1 
ATOM   383  O O   . LEU A 1 51  ? 27.20430 24.77675  14.89157  1.000 49.89317  ? 51  LEU B O   1 
ATOM   384  C CB  . LEU A 1 51  ? 27.20531 22.68010  17.39347  1.000 45.42699  ? 51  LEU B CB  1 
ATOM   385  C CG  . LEU A 1 51  ? 26.81136 21.21566  17.57992  1.000 53.63701  ? 51  LEU B CG  1 
ATOM   386  C CD1 . LEU A 1 51  ? 25.81521 21.10797  18.74180  1.000 52.95841  ? 51  LEU B CD1 1 
ATOM   387  C CD2 . LEU A 1 51  ? 26.21773 20.64101  16.29465  1.000 46.09095  ? 51  LEU B CD2 1 
ATOM   388  N N   . LYS A 1 52  ? 28.55979 25.40959  16.57077  1.000 51.93576  ? 52  LYS B N   1 
ATOM   389  C CA  . LYS A 1 52  ? 28.32609 26.82736  16.30744  1.000 53.27630  ? 52  LYS B CA  1 
ATOM   390  C C   . LYS A 1 52  ? 28.71317 27.21317  14.88652  1.000 50.75074  ? 52  LYS B C   1 
ATOM   391  O O   . LYS A 1 52  ? 28.04341 28.04295  14.26391  1.000 52.85837  ? 52  LYS B O   1 
ATOM   392  C CB  . LYS A 1 52  ? 29.08545 27.70067  17.30939  1.000 56.00932  ? 52  LYS B CB  1 
ATOM   393  C CG  . LYS A 1 52  ? 28.46243 29.08111  17.45879  1.000 62.60400  ? 52  LYS B CG  1 
ATOM   394  C CD  . LYS A 1 52  ? 29.45376 30.15062  17.92070  1.000 64.32084  ? 52  LYS B CD  1 
ATOM   395  C CE  . LYS A 1 52  ? 28.91603 30.90007  19.14229  1.000 65.58857  ? 52  LYS B CE  1 
ATOM   396  N NZ  . LYS A 1 52  ? 29.99148 31.45955  20.01462  1.000 72.70184  ? 52  LYS B NZ  1 
ATOM   397  N N   . SER A 1 53  ? 29.78430 26.62479  14.34844  1.000 49.83945  ? 53  SER B N   1 
ATOM   398  C CA  . SER A 1 53  ? 30.20672 26.99643  13.00159  1.000 48.49464  ? 53  SER B CA  1 
ATOM   399  C C   . SER A 1 53  ? 29.18062 26.61498  11.93556  1.000 48.79329  ? 53  SER B C   1 
ATOM   400  O O   . SER A 1 53  ? 29.21712 27.16879  10.83162  1.000 51.86253  ? 53  SER B O   1 
ATOM   401  C CB  . SER A 1 53  ? 31.57222 26.37332  12.67589  1.000 45.50156  ? 53  SER B CB  1 
ATOM   402  O OG  . SER A 1 53  ? 31.58507 24.96401  12.84827  1.000 48.15989  ? 53  SER B OG  1 
ATOM   403  N N   . GLN A 1 54  ? 28.24744 25.71075  12.23634  1.000 50.84786  ? 54  GLN B N   1 
ATOM   404  C CA  . GLN A 1 54  ? 27.28323 25.26229  11.23634  1.000 49.18894  ? 54  GLN B CA  1 
ATOM   405  C C   . GLN A 1 54  ? 26.01422 26.10799  11.18620  1.000 50.97485  ? 54  GLN B C   1 
ATOM   406  O O   . GLN A 1 54  ? 25.21430 25.94429  10.25134  1.000 45.43877  ? 54  GLN B O   1 
ATOM   407  C CB  . GLN A 1 54  ? 26.94707 23.79369  11.47949  1.000 44.95160  ? 54  GLN B CB  1 
ATOM   408  C CG  . GLN A 1 54  ? 28.22998 22.93342  11.63698  1.000 42.87798  ? 54  GLN B CG  1 
ATOM   409  C CD  . GLN A 1 54  ? 27.92130 21.51445  12.04321  1.000 44.85191  ? 54  GLN B CD  1 
ATOM   410  O OE1 . GLN A 1 54  ? 27.14156 20.81925  11.37298  1.000 51.32184  ? 54  GLN B OE1 1 
ATOM   411  N NE2 . GLN A 1 54  ? 28.46114 21.09165  13.17610  1.000 38.43312  ? 54  GLN B NE2 1 
ATOM   412  N N   . LYS A 1 55  ? 25.82151 27.01808  12.14121  1.000 47.71525  ? 55  LYS B N   1 
ATOM   413  C CA  . LYS A 1 55  ? 24.64045 27.87339  12.12417  1.000 48.78617  ? 55  LYS B CA  1 
ATOM   414  C C   . LYS A 1 55  ? 24.63789 28.74345  10.87625  1.000 47.67405  ? 55  LYS B C   1 
ATOM   415  O O   . LYS A 1 55  ? 25.58227 29.49345  10.62090  1.000 53.82939  ? 55  LYS B O   1 
ATOM   416  C CB  . LYS A 1 55  ? 24.59200 28.72548  13.38627  1.000 47.64738  ? 55  LYS B CB  1 
ATOM   417  C CG  . LYS A 1 55  ? 24.22366 27.93296  14.62019  1.000 48.74507  ? 55  LYS B CG  1 
ATOM   418  C CD  . LYS A 1 55  ? 22.73286 27.93431  14.78765  1.000 54.05646  ? 55  LYS B CD  1 
ATOM   419  C CE  . LYS A 1 55  ? 22.25428 27.17510  16.01225  1.000 53.79584  ? 55  LYS B CE  1 
ATOM   420  N NZ  . LYS A 1 55  ? 20.77437 27.42131  16.15069  1.000 57.77025  ? 55  LYS B NZ  1 
ATOM   421  N N   . GLY A 1 56  ? 23.58443 28.62835  10.08611  1.000 48.41742  ? 56  GLY B N   1 
ATOM   422  C CA  . GLY A 1 56  ? 23.53669 29.26119  8.79358   1.000 49.71689  ? 56  GLY B CA  1 
ATOM   423  C C   . GLY A 1 56  ? 24.03400 28.40427  7.65008   1.000 55.41932  ? 56  GLY B C   1 
ATOM   424  O O   . GLY A 1 56  ? 23.89537 28.81300  6.48798   1.000 57.03092  ? 56  GLY B O   1 
ATOM   425  N N   . HIS A 1 57  ? 24.59464 27.22547  7.93694   1.000 52.58100  ? 57  HIS B N   1 
ATOM   426  C CA  . HIS A 1 57  ? 25.13212 26.32869  6.91872   1.000 51.05944  ? 57  HIS B CA  1 
ATOM   427  C C   . HIS A 1 57  ? 24.49546 24.94700  6.92916   1.000 52.32456  ? 57  HIS B C   1 
ATOM   428  O O   . HIS A 1 57  ? 24.22929 24.39036  5.86305   1.000 49.59664  ? 57  HIS B O   1 
ATOM   429  C CB  . HIS A 1 57  ? 26.66006 26.18964  7.08345   1.000 45.66652  ? 57  HIS B CB  1 
ATOM   430  C CG  . HIS A 1 57  ? 27.38500 27.50144  7.13015   1.000 54.20779  ? 57  HIS B CG  1 
ATOM   431  N ND1 . HIS A 1 57  ? 27.65149 28.24494  6.00016   1.000 56.52381  ? 57  HIS B ND1 1 
ATOM   432  C CD2 . HIS A 1 57  ? 27.91912 28.19241  8.16704   1.000 56.32056  ? 57  HIS B CD2 1 
ATOM   433  C CE1 . HIS A 1 57  ? 28.30428 29.34282  6.33904   1.000 55.10789  ? 57  HIS B CE1 1 
ATOM   434  N NE2 . HIS A 1 57  ? 28.47770 29.33687  7.64851   1.000 53.00491  ? 57  HIS B NE2 1 
ATOM   435  N N   . ARG A 1 58  ? 24.24790 24.36897  8.10144   1.000 50.18814  ? 58  ARG B N   1 
ATOM   436  C CA  . ARG A 1 58  ? 23.66025 23.04453  8.19417   1.000 47.12517  ? 58  ARG B CA  1 
ATOM   437  C C   . ARG A 1 58  ? 22.40148 23.10956  9.05150   1.000 41.42322  ? 58  ARG B C   1 
ATOM   438  O O   . ARG A 1 58  ? 22.19144 24.05463  9.81553   1.000 40.34197  ? 58  ARG B O   1 
ATOM   439  C CB  . ARG A 1 58  ? 24.68892 22.03928  8.72925   1.000 43.48016  ? 58  ARG B CB  1 
ATOM   440  C CG  . ARG A 1 58  ? 25.82540 21.81279  7.71975   1.000 47.23177  ? 58  ARG B CG  1 
ATOM   441  C CD  . ARG A 1 58  ? 26.73330 20.64787  8.10471   1.000 42.44226  ? 58  ARG B CD  1 
ATOM   442  N NE  . ARG A 1 58  ? 26.07255 19.37277  7.85352   1.000 42.67874  ? 58  ARG B NE  1 
ATOM   443  C CZ  . ARG A 1 58  ? 25.94820 18.81198  6.65907   1.000 38.43545  ? 58  ARG B CZ  1 
ATOM   444  N NH1 . ARG A 1 58  ? 26.47450 19.36313  5.57986   1.000 39.42020  ? 58  ARG B NH1 1 
ATOM   445  N NH2 . ARG A 1 58  ? 25.31108 17.65281  6.55241   1.000 35.58149  ? 58  ARG B NH2 1 
ATOM   446  N N   . LEU A 1 59  ? 21.56512 22.08521  8.91907   1.000 44.18062  ? 59  LEU B N   1 
ATOM   447  C CA  . LEU A 1 59  ? 20.15460 22.17317  9.29729   1.000 46.55487  ? 59  LEU B CA  1 
ATOM   448  C C   . LEU A 1 59  ? 19.93769 21.69882  10.73560  1.000 43.61541  ? 59  LEU B C   1 
ATOM   449  O O   . LEU A 1 59  ? 20.25211 20.55416  11.07247  1.000 38.03298  ? 59  LEU B O   1 
ATOM   450  C CB  . LEU A 1 59  ? 19.31041 21.36300  8.31023   1.000 44.58582  ? 59  LEU B CB  1 
ATOM   451  C CG  . LEU A 1 59  ? 17.78782 21.52167  8.40551   1.000 53.97675  ? 59  LEU B CG  1 
ATOM   452  C CD1 . LEU A 1 59  ? 17.37907 22.95978  8.05941   1.000 51.41504  ? 59  LEU B CD1 1 
ATOM   453  C CD2 . LEU A 1 59  ? 17.08726 20.52044  7.48334   1.000 47.34104  ? 59  LEU B CD2 1 
ATOM   454  N N   . PHE A 1 60  ? 19.38613 22.58303  11.57836  1.000 43.70939  ? 60  PHE B N   1 
ATOM   455  C CA  . PHE A 1 60  ? 19.05211 22.26436  12.96547  1.000 43.24024  ? 60  PHE B CA  1 
ATOM   456  C C   . PHE A 1 60  ? 17.54063 22.02876  13.04149  1.000 49.56884  ? 60  PHE B C   1 
ATOM   457  O O   . PHE A 1 60  ? 16.75821 22.98107  12.98371  1.000 54.16554  ? 60  PHE B O   1 
ATOM   458  C CB  . PHE A 1 60  ? 19.47870 23.39244  13.91100  1.000 42.02141  ? 60  PHE B CB  1 
ATOM   459  C CG  . PHE A 1 60  ? 20.97093 23.44204  14.18267  1.000 52.12336  ? 60  PHE B CG  1 
ATOM   460  C CD1 . PHE A 1 60  ? 21.85129 24.04964  13.28315  1.000 46.23907  ? 60  PHE B CD1 1 
ATOM   461  C CD2 . PHE A 1 60  ? 21.49604 22.86808  15.33336  1.000 49.26415  ? 60  PHE B CD2 1 
ATOM   462  C CE1 . PHE A 1 60  ? 23.21409 24.09304  13.54204  1.000 47.77172  ? 60  PHE B CE1 1 
ATOM   463  C CE2 . PHE A 1 60  ? 22.85528 22.89989  15.58595  1.000 50.23277  ? 60  PHE B CE2 1 
ATOM   464  C CZ  . PHE A 1 60  ? 23.72056 23.51766  14.69296  1.000 46.58934  ? 60  PHE B CZ  1 
ATOM   465  N N   . THR A 1 61  ? 17.12797 20.77048  13.16574  1.000 42.39051  ? 61  THR B N   1 
ATOM   466  C CA  . THR A 1 61  ? 15.72048 20.41363  13.09274  1.000 46.79713  ? 61  THR B CA  1 
ATOM   467  C C   . THR A 1 61  ? 15.06833 20.53086  14.47200  1.000 52.29185  ? 61  THR B C   1 
ATOM   468  O O   . THR A 1 61  ? 15.54019 19.91933  15.44223  1.000 49.26469  ? 61  THR B O   1 
ATOM   469  C CB  . THR A 1 61  ? 15.56299 18.99125  12.56162  1.000 48.34036  ? 61  THR B CB  1 
ATOM   470  O OG1 . THR A 1 61  ? 15.92552 18.94915  11.17588  1.000 46.76936  ? 61  THR B OG1 1 
ATOM   471  C CG2 . THR A 1 61  ? 14.11200 18.55335  12.69284  1.000 51.25429  ? 61  THR B CG2 1 
ATOM   472  N N   . LYS A 1 62  ? 13.97143 21.30438  14.54519  1.000 49.60484  ? 62  LYS B N   1 
ATOM   473  C CA  . LYS A 1 62  ? 13.25452 21.50449  15.80693  1.000 52.63011  ? 62  LYS B CA  1 
ATOM   474  C C   . LYS A 1 62  ? 13.00607 20.18303  16.53620  1.000 56.02866  ? 62  LYS B C   1 
ATOM   475  O O   . LYS A 1 62  ? 13.30023 20.05294  17.73312  1.000 56.65614  ? 62  LYS B O   1 
ATOM   476  C CB  . LYS A 1 62  ? 11.92218 22.21314  15.55520  1.000 49.41602  ? 62  LYS B CB  1 
ATOM   477  C CG  . LYS A 1 62  ? 10.94578 22.07276  16.72477  1.000 54.41774  ? 62  LYS B CG  1 
ATOM   478  C CD  . LYS A 1 62  ? 9.94620  20.94263  16.47692  1.000 60.02406  ? 62  LYS B CD  1 
ATOM   479  C CE  . LYS A 1 62  ? 9.59640  20.23321  17.79251  1.000 61.90798  ? 62  LYS B CE  1 
ATOM   480  N NZ  . LYS A 1 62  ? 8.67609  19.07949  17.58103  1.000 54.52173  ? 62  LYS B NZ  1 
ATOM   481  N N   . SER A 1 63  ? 12.45765 19.18496  15.83249  1.000 51.08142  ? 63  SER B N   1 
ATOM   482  C CA  . SER A 1 63  ? 12.12460 17.94127  16.51937  1.000 51.79427  ? 63  SER B CA  1 
ATOM   483  C C   . SER A 1 63  ? 13.37165 17.18377  16.96701  1.000 55.15813  ? 63  SER B C   1 
ATOM   484  O O   . SER A 1 63  ? 13.33058 16.49882  17.99475  1.000 53.40980  ? 63  SER B O   1 
ATOM   485  C CB  . SER A 1 63  ? 11.22996 17.06130  15.64275  1.000 53.32646  ? 63  SER B CB  1 
ATOM   486  O OG  . SER A 1 63  ? 11.92230 16.46475  14.56612  1.000 57.20050  ? 63  SER B OG  1 
ATOM   487  N N   . THR A 1 64  ? 14.48864 17.29308  16.23365  1.000 52.26379  ? 64  THR B N   1 
ATOM   488  C CA  . THR A 1 64  ? 15.72237 16.67521  16.72895  1.000 53.50296  ? 64  THR B CA  1 
ATOM   489  C C   . THR A 1 64  ? 16.26713 17.41511  17.94567  1.000 49.96978  ? 64  THR B C   1 
ATOM   490  O O   . THR A 1 64  ? 16.75277 16.77821  18.89213  1.000 51.10520  ? 64  THR B O   1 
ATOM   491  C CB  . THR A 1 64  ? 16.79906 16.59199  15.64594  1.000 48.62330  ? 64  THR B CB  1 
ATOM   492  O OG1 . THR A 1 64  ? 16.27564 15.96878  14.46846  1.000 53.78401  ? 64  THR B OG1 1 
ATOM   493  C CG2 . THR A 1 64  ? 17.95159 15.75687  16.14704  1.000 50.66769  ? 64  THR B CG2 1 
ATOM   494  N N   . ILE A 1 65  ? 16.20958 18.75358  17.93942  1.000 48.74029  ? 65  ILE B N   1 
ATOM   495  C CA  . ILE A 1 65  ? 16.59974 19.50832  19.13270  1.000 52.88335  ? 65  ILE B CA  1 
ATOM   496  C C   . ILE A 1 65  ? 15.74374 19.09481  20.32689  1.000 55.67808  ? 65  ILE B C   1 
ATOM   497  O O   . ILE A 1 65  ? 16.26171 18.83086  21.42119  1.000 56.16538  ? 65  ILE B O   1 
ATOM   498  C CB  . ILE A 1 65  ? 16.51415 21.02623  18.88613  1.000 52.91380  ? 65  ILE B CB  1 
ATOM   499  C CG1 . ILE A 1 65  ? 17.54119 21.47604  17.85266  1.000 45.67155  ? 65  ILE B CG1 1 
ATOM   500  C CG2 . ILE A 1 65  ? 16.75329 21.78358  20.17805  1.000 55.81387  ? 65  ILE B CG2 1 
ATOM   501  C CD1 . ILE A 1 65  ? 17.01916 22.46355  16.86778  1.000 41.49451  ? 65  ILE B CD1 1 
ATOM   502  N N   . GLU A 1 66  ? 14.42289 18.99260  20.12667  1.000 60.00332  ? 66  GLU B N   1 
ATOM   503  C CA  . GLU A 1 66  ? 13.53209 18.60671  21.22395  1.000 62.64262  ? 66  GLU B CA  1 
ATOM   504  C C   . GLU A 1 66  ? 13.79788 17.17414  21.69003  1.000 56.99382  ? 66  GLU B C   1 
ATOM   505  O O   . GLU A 1 66  ? 13.74120 16.88844  22.89132  1.000 58.30786  ? 66  GLU B O   1 
ATOM   506  C CB  . GLU A 1 66  ? 12.06835 18.77577  20.80375  1.000 56.02471  ? 66  GLU B CB  1 
ATOM   507  N N   . TRP A 1 67  ? 14.09089 16.26162  20.76000  1.000 51.08221  ? 67  TRP B N   1 
ATOM   508  C CA  . TRP A 1 67  ? 14.44097 14.89913  21.15398  1.000 56.02246  ? 67  TRP B CA  1 
ATOM   509  C C   . TRP A 1 67  ? 15.72507 14.86613  21.98721  1.000 60.78009  ? 67  TRP B C   1 
ATOM   510  O O   . TRP A 1 67  ? 15.84154 14.07215  22.93000  1.000 60.70521  ? 67  TRP B O   1 
ATOM   511  C CB  . TRP A 1 67  ? 14.57792 14.01908  19.91485  1.000 53.80379  ? 67  TRP B CB  1 
ATOM   512  C CG  . TRP A 1 67  ? 15.04485 12.64683  20.20711  1.000 55.47196  ? 67  TRP B CG  1 
ATOM   513  C CD1 . TRP A 1 67  ? 14.26954 11.54429  20.37467  1.000 54.82296  ? 67  TRP B CD1 1 
ATOM   514  C CD2 . TRP A 1 67  ? 16.40206 12.21045  20.33665  1.000 56.77672  ? 67  TRP B CD2 1 
ATOM   515  N NE1 . TRP A 1 67  ? 15.05506 10.44431  20.62409  1.000 59.89463  ? 67  TRP B NE1 1 
ATOM   516  C CE2 . TRP A 1 67  ? 16.36983 10.82549  20.60314  1.000 56.21850  ? 67  TRP B CE2 1 
ATOM   517  C CE3 . TRP A 1 67  ? 17.64359 12.85871  20.26275  1.000 58.52534  ? 67  TRP B CE3 1 
ATOM   518  C CZ2 . TRP A 1 67  ? 17.52805 10.07220  20.79877  1.000 58.45206  ? 67  TRP B CZ2 1 
ATOM   519  C CZ3 . TRP A 1 67  ? 18.80452 12.10681  20.45620  1.000 56.84917  ? 67  TRP B CZ3 1 
ATOM   520  C CH2 . TRP A 1 67  ? 18.73382 10.72826  20.72145  1.000 58.79712  ? 67  TRP B CH2 1 
ATOM   521  N N   . TRP A 1 68  ? 16.70405 15.71634  21.65224  1.000 56.21860  ? 68  TRP B N   1 
ATOM   522  C CA  . TRP A 1 68  ? 17.90809 15.80893  22.47441  1.000 59.59547  ? 68  TRP B CA  1 
ATOM   523  C C   . TRP A 1 68  ? 17.58769 16.38046  23.84713  1.000 62.88661  ? 68  TRP B C   1 
ATOM   524  O O   . TRP A 1 68  ? 18.14502 15.92951  24.85662  1.000 63.05408  ? 68  TRP B O   1 
ATOM   525  C CB  . TRP A 1 68  ? 18.97920 16.66536  21.78066  1.000 55.11328  ? 68  TRP B CB  1 
ATOM   526  C CG  . TRP A 1 68  ? 19.85967 15.86830  20.85985  1.000 52.40519  ? 68  TRP B CG  1 
ATOM   527  C CD1 . TRP A 1 68  ? 19.94006 15.98469  19.50003  1.000 51.77797  ? 68  TRP B CD1 1 
ATOM   528  C CD2 . TRP A 1 68  ? 20.76387 14.81855  21.22616  1.000 51.17981  ? 68  TRP B CD2 1 
ATOM   529  N NE1 . TRP A 1 68  ? 20.84339 15.07705  18.99807  1.000 51.04820  ? 68  TRP B NE1 1 
ATOM   530  C CE2 . TRP A 1 68  ? 21.36289 14.34765  20.03578  1.000 52.63285  ? 68  TRP B CE2 1 
ATOM   531  C CE3 . TRP A 1 68  ? 21.13016 14.23503  22.44030  1.000 50.34419  ? 68  TRP B CE3 1 
ATOM   532  C CZ2 . TRP A 1 68  ? 22.30776 13.32053  20.02882  1.000 43.37518  ? 68  TRP B CZ2 1 
ATOM   533  C CZ3 . TRP A 1 68  ? 22.06401 13.22013  22.42810  1.000 52.58930  ? 68  TRP B CZ3 1 
ATOM   534  C CH2 . TRP A 1 68  ? 22.63870 12.77086  21.23026  1.000 45.51074  ? 68  TRP B CH2 1 
ATOM   535  N N   . LYS A 1 69  ? 16.69371 17.37778  23.89868  1.000 61.31642  ? 69  LYS B N   1 
ATOM   536  C CA  . LYS A 1 69  ? 16.31207 17.99194  25.16509  1.000 60.14069  ? 69  LYS B CA  1 
ATOM   537  C C   . LYS A 1 69  ? 15.93775 16.94280  26.21174  1.000 64.76779  ? 69  LYS B C   1 
ATOM   538  O O   . LYS A 1 69  ? 16.25293 17.11020  27.39651  1.000 63.60456  ? 69  LYS B O   1 
ATOM   539  C CB  . LYS A 1 69  ? 15.15056 18.96475  24.92610  1.000 65.32343  ? 69  LYS B CB  1 
ATOM   540  C CG  . LYS A 1 69  ? 15.36565 20.37563  25.47306  1.000 69.37889  ? 69  LYS B CG  1 
ATOM   541  C CD  . LYS A 1 69  ? 14.86727 20.48383  26.91307  1.000 74.85148  ? 69  LYS B CD  1 
ATOM   542  C CE  . LYS A 1 69  ? 15.23785 21.81641  27.55734  1.000 69.80744  ? 69  LYS B CE  1 
ATOM   543  N NZ  . LYS A 1 69  ? 15.01204 21.75464  29.03518  1.000 73.78215  ? 69  LYS B NZ  1 
ATOM   544  N N   . ASN A 1 70  ? 15.33136 15.83085  25.78390  1.000 59.88981  ? 70  ASN B N   1 
ATOM   545  C CA  . ASN A 1 70  ? 14.77425 14.82000  26.67270  1.000 62.00021  ? 70  ASN B CA  1 
ATOM   546  C C   . ASN A 1 70  ? 15.69044 13.62583  26.90981  1.000 59.84015  ? 70  ASN B C   1 
ATOM   547  O O   . ASN A 1 70  ? 15.26957 12.66197  27.55170  1.000 59.70026  ? 70  ASN B O   1 
ATOM   548  C CB  . ASN A 1 70  ? 13.44012 14.31958  26.11174  1.000 66.54102  ? 70  ASN B CB  1 
ATOM   549  C CG  . ASN A 1 70  ? 12.43895 15.42662  25.93234  1.000 61.91783  ? 70  ASN B CG  1 
ATOM   550  O OD1 . ASN A 1 70  ? 12.02489 16.07705  26.89614  1.000 65.69433  ? 70  ASN B OD1 1 
ATOM   551  N ND2 . ASN A 1 70  ? 12.07123 15.68052  24.68408  1.000 62.25220  ? 70  ASN B ND2 1 
ATOM   552  N N   . GLN A 1 71  ? 16.91177 13.63743  26.39802  1.000 66.04609  ? 71  GLN B N   1 
ATOM   553  C CA  . GLN A 1 71  ? 17.77757 12.51310  26.72559  1.000 63.99588  ? 71  GLN B CA  1 
ATOM   554  C C   . GLN A 1 71  ? 18.42153 12.72635  28.09223  1.000 60.08813  ? 71  GLN B C   1 
ATOM   555  O O   . GLN A 1 71  ? 18.45232 13.83695  28.62566  1.000 60.56353  ? 71  GLN B O   1 
ATOM   556  C CB  . GLN A 1 71  ? 18.84330 12.30906  25.64710  1.000 61.48984  ? 71  GLN B CB  1 
ATOM   557  C CG  . GLN A 1 71  ? 18.25060 12.15654  24.25837  1.000 60.90979  ? 71  GLN B CG  1 
ATOM   558  C CD  . GLN A 1 71  ? 17.11993 11.12830  24.23103  1.000 63.65032  ? 71  GLN B CD  1 
ATOM   559  O OE1 . GLN A 1 71  ? 17.34510 9.94251   24.48419  1.000 64.26737  ? 71  GLN B OE1 1 
ATOM   560  N NE2 . GLN A 1 71  ? 15.89795 11.58366  23.93489  1.000 62.80257  ? 71  GLN B NE2 1 
ATOM   561  N N   . SER A 1 72  ? 18.92222 11.63394  28.66629  1.000 62.34179  ? 72  SER B N   1 
ATOM   562  C CA  . SER A 1 72  ? 19.59540 11.65409  29.96261  1.000 64.25143  ? 72  SER B CA  1 
ATOM   563  C C   . SER A 1 72  ? 20.72778 12.67868  29.96813  1.000 67.96080  ? 72  SER B C   1 
ATOM   564  O O   . SER A 1 72  ? 21.24101 13.03615  28.89732  1.000 63.21444  ? 72  SER B O   1 
ATOM   565  C CB  . SER A 1 72  ? 20.13903 10.26518  30.29471  1.000 63.59005  ? 72  SER B CB  1 
ATOM   566  O OG  . SER A 1 72  ? 21.41606 10.08565  29.71335  1.000 67.16148  ? 72  SER B OG  1 
ATOM   567  N N   . PRO A 1 73  ? 21.14349 13.18471  31.13680  1.000 66.85018  ? 73  PRO B N   1 
ATOM   568  C CA  . PRO A 1 73  ? 22.30311 14.08730  31.14663  1.000 69.37856  ? 73  PRO B CA  1 
ATOM   569  C C   . PRO A 1 73  ? 23.56895 13.40876  30.66223  1.000 66.70154  ? 73  PRO B C   1 
ATOM   570  O O   . PRO A 1 73  ? 24.45163 14.08986  30.13196  1.000 64.92389  ? 73  PRO B O   1 
ATOM   571  C CB  . PRO A 1 73  ? 22.40570 14.52030  32.61901  1.000 68.67352  ? 73  PRO B CB  1 
ATOM   572  C CG  . PRO A 1 73  ? 21.04453 14.22407  33.20362  1.000 55.55977  ? 73  PRO B CG  1 
ATOM   573  C CD  . PRO A 1 73  ? 20.60261 12.99039  32.49321  1.000 64.04655  ? 73  PRO B CD  1 
ATOM   574  N N   . GLU A 1 74  ? 23.67326 12.08062  30.80309  1.000 67.27890  ? 74  GLU B N   1 
ATOM   575  C CA  . GLU A 1 74  ? 24.84395 11.37600  30.28808  1.000 66.64887  ? 74  GLU B CA  1 
ATOM   576  C C   . GLU A 1 74  ? 24.91260 11.46637  28.76930  1.000 66.34389  ? 74  GLU B C   1 
ATOM   577  O O   . GLU A 1 74  ? 25.98227 11.72472  28.20477  1.000 63.51748  ? 74  GLU B O   1 
ATOM   578  C CB  . GLU A 1 74  ? 24.82594 9.91429   30.74105  1.000 69.33937  ? 74  GLU B CB  1 
ATOM   579  N N   . ALA A 1 75  ? 23.77411 11.26975  28.09442  1.000 70.69872  ? 75  ALA B N   1 
ATOM   580  C CA  . ALA A 1 75  ? 23.72499 11.39791  26.64021  1.000 66.22059  ? 75  ALA B CA  1 
ATOM   581  C C   . ALA A 1 75  ? 24.02031 12.82276  26.19055  1.000 63.29377  ? 75  ALA B C   1 
ATOM   582  O O   . ALA A 1 75  ? 24.66750 13.03339  25.15965  1.000 59.51485  ? 75  ALA B O   1 
ATOM   583  C CB  . ALA A 1 75  ? 22.35428 10.96546  26.12779  1.000 69.05588  ? 75  ALA B CB  1 
ATOM   584  N N   . ARG A 1 76  ? 23.53751 13.81583  26.94209  1.000 67.00690  ? 76  ARG B N   1 
ATOM   585  C CA  . ARG A 1 76  ? 23.67391 15.20622  26.52385  1.000 62.64876  ? 76  ARG B CA  1 
ATOM   586  C C   . ARG A 1 76  ? 25.08915 15.73233  26.70652  1.000 64.92312  ? 76  ARG B C   1 
ATOM   587  O O   . ARG A 1 76  ? 25.45116 16.72614  26.06085  1.000 62.77132  ? 76  ARG B O   1 
ATOM   588  C CB  . ARG A 1 76  ? 22.68694 16.08705  27.29286  1.000 60.08179  ? 76  ARG B CB  1 
ATOM   589  N N   . LYS A 1 77  ? 25.88236 15.10245  27.58436  1.000 64.95672  ? 77  LYS B N   1 
ATOM   590  C CA  . LYS A 1 77  ? 27.26557 15.52623  27.78925  1.000 65.72675  ? 77  LYS B CA  1 
ATOM   591  C C   . LYS A 1 77  ? 28.05684 15.43102  26.49403  1.000 64.75204  ? 77  LYS B C   1 
ATOM   592  O O   . LYS A 1 77  ? 28.85210 16.32342  26.17702  1.000 64.64947  ? 77  LYS B O   1 
ATOM   593  C CB  . LYS A 1 77  ? 27.92296 14.67968  28.88276  1.000 65.80385  ? 77  LYS B CB  1 
ATOM   594  N N   . ASN A 1 78  ? 27.82502 14.36370  25.71949  1.000 65.99233  ? 78  ASN B N   1 
ATOM   595  C CA  . ASN A 1 78  ? 28.44447 14.20626  24.40663  1.000 65.28965  ? 78  ASN B CA  1 
ATOM   596  C C   . ASN A 1 78  ? 28.09273 15.34224  23.44687  1.000 65.33384  ? 78  ASN B C   1 
ATOM   597  O O   . ASN A 1 78  ? 28.82184 15.55583  22.46995  1.000 64.32498  ? 78  ASN B O   1 
ATOM   598  C CB  . ASN A 1 78  ? 28.02869 12.85757  23.79740  1.000 59.23901  ? 78  ASN B CB  1 
ATOM   599  N N   . ILE A 1 79  ? 27.00292 16.07434  23.69867  1.000 61.36944  ? 79  ILE B N   1 
ATOM   600  C CA  . ILE A 1 79  ? 26.57272 17.13460  22.78943  1.000 57.29831  ? 79  ILE B CA  1 
ATOM   601  C C   . ILE A 1 79  ? 27.28523 18.46179  23.05662  1.000 56.92127  ? 79  ILE B C   1 
ATOM   602  O O   . ILE A 1 79  ? 27.50544 19.23870  22.12364  1.000 58.89754  ? 79  ILE B O   1 
ATOM   603  C CB  . ILE A 1 79  ? 25.04332 17.31485  22.86389  1.000 55.61226  ? 79  ILE B CB  1 
ATOM   604  N N   . ALA A 1 80  ? 27.66687 18.73548  24.30272  1.000 57.36416  ? 80  ALA B N   1 
ATOM   605  C CA  . ALA A 1 80  ? 28.18718 20.04660  24.66354  1.000 54.91152  ? 80  ALA B CA  1 
ATOM   606  C C   . ALA A 1 80  ? 29.46623 20.37374  23.88771  1.000 53.68151  ? 80  ALA B C   1 
ATOM   607  O O   . ALA A 1 80  ? 30.20022 19.47457  23.47227  1.000 50.96635  ? 80  ALA B O   1 
ATOM   608  C CB  . ALA A 1 80  ? 28.46207 20.11006  26.16326  1.000 54.04373  ? 80  ALA B CB  1 
ATOM   609  N N   . PRO A 1 81  ? 29.74239 21.66043  23.66494  1.000 53.55945  ? 81  PRO B N   1 
ATOM   610  C CA  . PRO A 1 81  ? 30.98973 22.04632  22.99904  1.000 53.97550  ? 81  PRO B CA  1 
ATOM   611  C C   . PRO A 1 81  ? 32.20896 21.60986  23.78934  1.000 57.84707  ? 81  PRO B C   1 
ATOM   612  O O   . PRO A 1 81  ? 32.16397 21.45966  25.01318  1.000 55.70592  ? 81  PRO B O   1 
ATOM   613  C CB  . PRO A 1 81  ? 30.89470 23.57252  22.92647  1.000 55.25159  ? 81  PRO B CB  1 
ATOM   614  C CG  . PRO A 1 81  ? 29.41657 23.81986  22.88297  1.000 54.71733  ? 81  PRO B CG  1 
ATOM   615  C CD  . PRO A 1 81  ? 28.83017 22.80531  23.81982  1.000 51.64292  ? 81  PRO B CD  1 
ATOM   616  N N   . SER A 1 82  ? 33.31380 21.44075  23.06180  1.000 55.96526  ? 82  SER B N   1 
ATOM   617  C CA  . SER A 1 82  ? 34.49854 20.75858  23.54813  1.000 55.76443  ? 82  SER B CA  1 
ATOM   618  C C   . SER A 1 82  ? 35.70422 21.33589  22.81494  1.000 62.82853  ? 82  SER B C   1 
ATOM   619  O O   . SER A 1 82  ? 35.56583 21.92058  21.73541  1.000 60.42726  ? 82  SER B O   1 
ATOM   620  C CB  . SER A 1 82  ? 34.35551 19.24775  23.33520  1.000 53.05762  ? 82  SER B CB  1 
ATOM   621  O OG  . SER A 1 82  ? 35.53819 18.54271  23.63211  1.000 59.49993  ? 82  SER B OG  1 
ATOM   622  N N   . ASP A 1 83  ? 36.89047 21.19556  23.42906  1.000 62.09256  ? 83  ASP B N   1 
ATOM   623  C CA  . ASP A 1 83  ? 38.11862 21.70853  22.81916  1.000 63.22338  ? 83  ASP B CA  1 
ATOM   624  C C   . ASP A 1 83  ? 38.49524 20.93207  21.56628  1.000 62.47547  ? 83  ASP B C   1 
ATOM   625  O O   . ASP A 1 83  ? 39.11569 21.48730  20.65081  1.000 63.36271  ? 83  ASP B O   1 
ATOM   626  C CB  . ASP A 1 83  ? 39.28211 21.65071  23.81320  1.000 67.47434  ? 83  ASP B CB  1 
ATOM   627  C CG  . ASP A 1 83  ? 39.20841 22.73604  24.85895  1.000 74.21471  ? 83  ASP B CG  1 
ATOM   628  O OD1 . ASP A 1 83  ? 38.37235 23.65455  24.68998  1.000 78.16264  ? 83  ASP B OD1 1 
ATOM   629  O OD2 . ASP A 1 83  ? 39.99627 22.68225  25.83620  1.000 77.10889  ? 83  ASP B OD2 1 
ATOM   630  N N   . GLU A 1 84  ? 38.13579 19.65671  21.51416  1.000 59.73848  ? 84  GLU B N   1 
ATOM   631  C CA  . GLU A 1 84  ? 38.38378 18.80336  20.36503  1.000 55.62229  ? 84  GLU B CA  1 
ATOM   632  C C   . GLU A 1 84  ? 37.44116 19.05958  19.18890  1.000 53.22063  ? 84  GLU B C   1 
ATOM   633  O O   . GLU A 1 84  ? 37.51608 18.32241  18.20195  1.000 51.48831  ? 84  GLU B O   1 
ATOM   634  C CB  . GLU A 1 84  ? 38.28041 17.34506  20.80585  1.000 57.37259  ? 84  GLU B CB  1 
ATOM   635  C CG  . GLU A 1 84  ? 36.86633 16.84734  20.90797  1.000 62.01180  ? 84  GLU B CG  1 
ATOM   636  C CD  . GLU A 1 84  ? 36.75126 15.65321  21.82653  1.000 68.55647  ? 84  GLU B CD  1 
ATOM   637  O OE1 . GLU A 1 84  ? 36.95663 15.82906  23.04719  1.000 73.40680  ? 84  GLU B OE1 1 
ATOM   638  O OE2 . GLU A 1 84  ? 36.46214 14.54585  21.33251  1.000 68.18707  ? 84  GLU B OE2 1 
ATOM   639  N N   . ASP A 1 85  ? 36.57111 20.07114  19.25402  1.000 50.53402  ? 85  ASP B N   1 
ATOM   640  C CA  . ASP A 1 85  ? 35.64275 20.32798  18.15669  1.000 51.88228  ? 85  ASP B CA  1 
ATOM   641  C C   . ASP A 1 85  ? 36.39618 20.80878  16.91439  1.000 53.50012  ? 85  ASP B C   1 
ATOM   642  O O   . ASP A 1 85  ? 37.34824 21.58757  17.01454  1.000 54.64153  ? 85  ASP B O   1 
ATOM   643  C CB  . ASP A 1 85  ? 34.59301 21.36613  18.57120  1.000 48.35612  ? 85  ASP B CB  1 
ATOM   644  C CG  . ASP A 1 85  ? 33.55165 20.80837  19.56338  1.000 49.43600  ? 85  ASP B CG  1 
ATOM   645  O OD1 . ASP A 1 85  ? 33.56331 19.59492  19.86642  1.000 46.64105  ? 85  ASP B OD1 1 
ATOM   646  O OD2 . ASP A 1 85  ? 32.70531 21.59237  20.04810  1.000 53.61692  ? 85  ASP B OD2 1 
ATOM   647  N N   . VAL A 1 86  ? 35.95883 20.34452  15.73314  1.000 49.23750  ? 86  VAL B N   1 
ATOM   648  C CA  . VAL A 1 86  ? 36.57011 20.70007  14.45693  1.000 41.38920  ? 86  VAL B CA  1 
ATOM   649  C C   . VAL A 1 86  ? 35.49651 21.17861  13.48738  1.000 47.36379  ? 86  VAL B C   1 
ATOM   650  O O   . VAL A 1 86  ? 34.33032 20.76052  13.54874  1.000 47.57118  ? 86  VAL B O   1 
ATOM   651  C CB  . VAL A 1 86  ? 37.33783 19.51789  13.81792  1.000 48.00242  ? 86  VAL B CB  1 
ATOM   652  C CG1 . VAL A 1 86  ? 38.63627 19.21170  14.59012  1.000 41.18960  ? 86  VAL B CG1 1 
ATOM   653  C CG2 . VAL A 1 86  ? 36.42748 18.28008  13.65983  1.000 45.23150  ? 86  VAL B CG2 1 
ATOM   654  N N   . ALA A 1 87  ? 35.91514 22.04366  12.55966  1.000 38.80194  ? 87  ALA B N   1 
ATOM   655  C CA  . ALA A 1 87  ? 35.04486 22.45686  11.46944  1.000 39.33822  ? 87  ALA B CA  1 
ATOM   656  C C   . ALA A 1 87  ? 34.72947 21.26123  10.57337  1.000 42.13347  ? 87  ALA B C   1 
ATOM   657  O O   . ALA A 1 87  ? 35.51352 20.31544  10.47654  1.000 40.45224  ? 87  ALA B O   1 
ATOM   658  C CB  . ALA A 1 87  ? 35.69390 23.56744  10.65045  1.000 41.85624  ? 87  ALA B CB  1 
ATOM   659  N N   . THR A 1 88  ? 33.56729 21.31456  9.90138   1.000 40.06410  ? 88  THR B N   1 
ATOM   660  C CA  . THR A 1 88  ? 33.11709 20.16554  9.11607   1.000 38.36193  ? 88  THR B CA  1 
ATOM   661  C C   . THR A 1 88  ? 34.10755 19.79193  8.00308   1.000 38.93188  ? 88  THR B C   1 
ATOM   662  O O   . THR A 1 88  ? 34.32780 18.59755  7.76096   1.000 35.76268  ? 88  THR B O   1 
ATOM   663  C CB  . THR A 1 88  ? 31.71338 20.41476  8.54875   1.000 37.59107  ? 88  THR B CB  1 
ATOM   664  O OG1 . THR A 1 88  ? 31.65700 21.69088  7.91528   1.000 36.28723  ? 88  THR B OG1 1 
ATOM   665  C CG2 . THR A 1 88  ? 30.65715 20.34548  9.65329   1.000 36.58330  ? 88  THR B CG2 1 
ATOM   666  N N   . ILE A 1 89  ? 34.73529 20.77834  7.32661   1.000 37.04324  ? 89  ILE B N   1 
ATOM   667  C CA  . ILE A 1 89  ? 35.77597 20.42092  6.34878   1.000 42.73474  ? 89  ILE B CA  1 
ATOM   668  C C   . ILE A 1 89  ? 36.95848 19.76806  7.03353   1.000 40.50702  ? 89  ILE B C   1 
ATOM   669  O O   . ILE A 1 89  ? 37.65433 18.93524  6.43831   1.000 40.64926  ? 89  ILE B O   1 
ATOM   670  C CB  . ILE A 1 89  ? 36.30571 21.62004  5.54152   1.000 42.57504  ? 89  ILE B CB  1 
ATOM   671  C CG1 . ILE A 1 89  ? 36.46219 22.84706  6.45028   1.000 43.57495  ? 89  ILE B CG1 1 
ATOM   672  C CG2 . ILE A 1 89  ? 35.65704 21.72717  4.15638   1.000 40.67895  ? 89  ILE B CG2 1 
ATOM   673  C CD1 . ILE A 1 89  ? 37.11327 24.03221  5.81617   1.000 41.76802  ? 89  ILE B CD1 1 
ATOM   674  N N   . ALA A 1 90  ? 37.27294 20.21005  8.24826   1.000 40.76529  ? 90  ALA B N   1 
ATOM   675  C CA  . ALA A 1 90  ? 38.38421 19.60064  8.96059   1.000 38.75239  ? 90  ALA B CA  1 
ATOM   676  C C   . ALA A 1 90  ? 38.06944 18.15538  9.29110   1.000 40.22432  ? 90  ALA B C   1 
ATOM   677  O O   . ALA A 1 90  ? 38.91168 17.26670  9.10061   1.000 45.90845  ? 90  ALA B O   1 
ATOM   678  C CB  . ALA A 1 90  ? 38.70541 20.40043  10.22326  1.000 39.82451  ? 90  ALA B CB  1 
ATOM   679  N N   . GLY A 1 91  ? 36.83751 17.88962  9.73710   1.000 39.89299  ? 91  GLY B N   1 
ATOM   680  C CA  . GLY A 1 91  ? 36.46814 16.53699  10.11626  1.000 38.12804  ? 91  GLY B CA  1 
ATOM   681  C C   . GLY A 1 91  ? 36.33191 15.58999  8.94206   1.000 39.61474  ? 91  GLY B C   1 
ATOM   682  O O   . GLY A 1 91  ? 36.61709 14.38823  9.07431   1.000 39.25824  ? 91  GLY B O   1 
ATOM   683  N N   . ILE A 1 92  ? 35.86840 16.09088  7.78879   1.000 36.78289  ? 92  ILE B N   1 
ATOM   684  C CA  . ILE A 1 92  ? 35.81630 15.21252  6.62161   1.000 37.48927  ? 92  ILE B CA  1 
ATOM   685  C C   . ILE A 1 92  ? 37.22709 14.88945  6.15027   1.000 38.25779  ? 92  ILE B C   1 
ATOM   686  O O   . ILE A 1 92  ? 37.48784 13.77292  5.68612   1.000 40.45442  ? 92  ILE B O   1 
ATOM   687  C CB  . ILE A 1 92  ? 34.95368 15.80139  5.48463   1.000 35.66722  ? 92  ILE B CB  1 
ATOM   688  C CG1 . ILE A 1 92  ? 34.45649 14.69887  4.51403   1.000 35.53007  ? 92  ILE B CG1 1 
ATOM   689  C CG2 . ILE A 1 92  ? 35.74432 16.83685  4.66228   1.000 33.77398  ? 92  ILE B CG2 1 
ATOM   690  C CD1 . ILE A 1 92  ? 33.70734 13.48550  5.12643   1.000 30.36892  ? 92  ILE B CD1 1 
ATOM   691  N N   . ALA A 1 93  ? 38.16252 15.84907  6.26205   1.000 37.28356  ? 93  ALA B N   1 
ATOM   692  C CA  . ALA A 1 93  ? 39.55939 15.52384  5.95792   1.000 44.67751  ? 93  ALA B CA  1 
ATOM   693  C C   . ALA A 1 93  ? 40.06570 14.44260  6.89422   1.000 41.16844  ? 93  ALA B C   1 
ATOM   694  O O   . ALA A 1 93  ? 40.69764 13.48052  6.45226   1.000 43.21314  ? 93  ALA B O   1 
ATOM   695  C CB  . ALA A 1 93  ? 40.46902 16.75786  6.05161   1.000 38.63158  ? 93  ALA B CB  1 
ATOM   696  N N   . LYS A 1 94  ? 39.77741 14.57653  8.19400   1.000 42.20262  ? 94  LYS B N   1 
ATOM   697  C CA  . LYS A 1 94  ? 40.20802 13.56010  9.14999   1.000 44.59470  ? 94  LYS B CA  1 
ATOM   698  C C   . LYS A 1 94  ? 39.59274 12.21155  8.80465   1.000 42.16773  ? 94  LYS B C   1 
ATOM   699  O O   . LYS A 1 94  ? 40.28576 11.18472  8.81335   1.000 47.84997  ? 94  LYS B O   1 
ATOM   700  C CB  . LYS A 1 94  ? 39.83976 13.98713  10.57027  1.000 42.80239  ? 94  LYS B CB  1 
ATOM   701  C CG  . LYS A 1 94  ? 40.84740 14.90456  11.22601  1.000 52.07339  ? 94  LYS B CG  1 
ATOM   702  C CD  . LYS A 1 94  ? 41.04762 14.57644  12.70737  1.000 61.18571  ? 94  LYS B CD  1 
ATOM   703  C CE  . LYS A 1 94  ? 40.36309 15.65613  13.57487  1.000 57.56133  ? 94  LYS B CE  1 
ATOM   704  N NZ  . LYS A 1 94  ? 39.92418 15.15486  14.90692  1.000 57.05422  ? 94  LYS B NZ  1 
ATOM   705  N N   . PHE A 1 95  ? 38.30282 12.20466  8.44703   1.000 42.26802  ? 95  PHE B N   1 
ATOM   706  C CA  . PHE A 1 95  ? 37.64587 10.97035  8.02117   1.000 40.05343  ? 95  PHE B CA  1 
ATOM   707  C C   . PHE A 1 95  ? 38.37378 10.34453  6.84525   1.000 37.02541  ? 95  PHE B C   1 
ATOM   708  O O   . PHE A 1 95  ? 38.60872 9.13465   6.82296   1.000 37.38677  ? 95  PHE B O   1 
ATOM   709  C CB  . PHE A 1 95  ? 36.17490 11.21652  7.63245   1.000 31.06967  ? 95  PHE B CB  1 
ATOM   710  C CG  . PHE A 1 95  ? 35.53677 10.00557  6.98527   1.000 34.83350  ? 95  PHE B CG  1 
ATOM   711  C CD1 . PHE A 1 95  ? 35.14338 8.92056   7.75737   1.000 38.22760  ? 95  PHE B CD1 1 
ATOM   712  C CD2 . PHE A 1 95  ? 35.42291 9.89998   5.61588   1.000 34.45084  ? 95  PHE B CD2 1 
ATOM   713  C CE1 . PHE A 1 95  ? 34.59835 7.78048   7.18040   1.000 33.88203  ? 95  PHE B CE1 1 
ATOM   714  C CE2 . PHE A 1 95  ? 34.87758 8.76346   5.03864   1.000 33.35861  ? 95  PHE B CE2 1 
ATOM   715  C CZ  . PHE A 1 95  ? 34.46030 7.71081   5.82547   1.000 31.55028  ? 95  PHE B CZ  1 
ATOM   716  N N   . ASN A 1 96  ? 38.68911 11.15317  5.82719   1.000 38.28564  ? 96  ASN B N   1 
ATOM   717  C CA  . ASN A 1 96  ? 39.39148 10.63464  4.65638   1.000 44.29481  ? 96  ASN B CA  1 
ATOM   718  C C   . ASN A 1 96  ? 40.78419 10.11141  5.02533   1.000 44.77272  ? 96  ASN B C   1 
ATOM   719  O O   . ASN A 1 96  ? 41.22145 9.07324   4.50843   1.000 46.15647  ? 96  ASN B O   1 
ATOM   720  C CB  . ASN A 1 96  ? 39.47761 11.71413  3.56884   1.000 42.56829  ? 96  ASN B CB  1 
ATOM   721  C CG  . ASN A 1 96  ? 38.14035 11.95211  2.86867   1.000 50.07337  ? 96  ASN B CG  1 
ATOM   722  O OD1 . ASN A 1 96  ? 37.13684 11.29062  3.16562   1.000 49.67958  ? 96  ASN B OD1 1 
ATOM   723  N ND2 . ASN A 1 96  ? 38.12813 12.88115  1.91307   1.000 48.54630  ? 96  ASN B ND2 1 
ATOM   724  N N   . ASP A 1 97  ? 41.49155 10.80557  5.92474   1.000 43.34837  ? 97  ASP B N   1 
ATOM   725  C CA  . ASP A 1 97  ? 42.78034 10.29389  6.40375   1.000 52.80357  ? 97  ASP B CA  1 
ATOM   726  C C   . ASP A 1 97  ? 42.61509 8.93019   7.07482   1.000 51.10401  ? 97  ASP B C   1 
ATOM   727  O O   . ASP A 1 97  ? 43.34236 7.97688   6.76238   1.000 47.47175  ? 97  ASP B O   1 
ATOM   728  C CB  . ASP A 1 97  ? 43.43374 11.29327  7.36832   1.000 48.38538  ? 97  ASP B CB  1 
ATOM   729  C CG  . ASP A 1 97  ? 43.92140 12.54276  6.66536   1.000 58.19820  ? 97  ASP B CG  1 
ATOM   730  O OD1 . ASP A 1 97  ? 44.11965 12.47825  5.43086   1.000 61.75398  ? 97  ASP B OD1 1 
ATOM   731  O OD2 . ASP A 1 97  ? 44.10050 13.59164  7.33367   1.000 58.10429  ? 97  ASP B OD2 1 
ATOM   732  N N   . TYR A 1 98  ? 41.64386 8.81175   7.98876   1.000 45.92441  ? 98  TYR B N   1 
ATOM   733  C CA  . TYR A 1 98  ? 41.43677 7.53077   8.66066   1.000 48.12490  ? 98  TYR B CA  1 
ATOM   734  C C   . TYR A 1 98  ? 41.19134 6.41076   7.65380   1.000 45.74928  ? 98  TYR B C   1 
ATOM   735  O O   . TYR A 1 98  ? 41.75501 5.31815   7.78410   1.000 47.68404  ? 98  TYR B O   1 
ATOM   736  C CB  . TYR A 1 98  ? 40.27233 7.61883   9.65307   1.000 42.04245  ? 98  TYR B CB  1 
ATOM   737  C CG  . TYR A 1 98  ? 40.01006 6.30218   10.33949  1.000 42.06790  ? 98  TYR B CG  1 
ATOM   738  C CD1 . TYR A 1 98  ? 39.20896 5.31863   9.74994   1.000 45.48723  ? 98  TYR B CD1 1 
ATOM   739  C CD2 . TYR A 1 98  ? 40.57331 6.02704   11.57186  1.000 42.37298  ? 98  TYR B CD2 1 
ATOM   740  C CE1 . TYR A 1 98  ? 38.97252 4.09362   10.39113  1.000 45.20403  ? 98  TYR B CE1 1 
ATOM   741  C CE2 . TYR A 1 98  ? 40.34315 4.81465   12.21675  1.000 43.76067  ? 98  TYR B CE2 1 
ATOM   742  C CZ  . TYR A 1 98  ? 39.55744 3.85542   11.62521  1.000 46.86390  ? 98  TYR B CZ  1 
ATOM   743  O OH  . TYR A 1 98  ? 39.34998 2.66977   12.29042  1.000 48.20082  ? 98  TYR B OH  1 
ATOM   744  N N   . ILE A 1 99  ? 40.32526 6.65818   6.65959   1.000 44.15581  ? 99  ILE B N   1 
ATOM   745  C CA  . ILE A 1 99  ? 40.04444 5.65813   5.62647   1.000 43.44803  ? 99  ILE B CA  1 
ATOM   746  C C   . ILE A 1 99  ? 41.32361 5.30175   4.87181   1.000 48.06999  ? 99  ILE B C   1 
ATOM   747  O O   . ILE A 1 99  ? 41.57756 4.13053   4.56507   1.000 44.09667  ? 99  ILE B O   1 
ATOM   748  C CB  . ILE A 1 99  ? 38.94696 6.16704   4.66133   1.000 40.69682  ? 99  ILE B CB  1 
ATOM   749  C CG1 . ILE A 1 99  ? 37.61969 6.44438   5.38589   1.000 37.96091  ? 99  ILE B CG1 1 
ATOM   750  C CG2 . ILE A 1 99  ? 38.71406 5.19767   3.52777   1.000 42.80203  ? 99  ILE B CG2 1 
ATOM   751  C CD1 . ILE A 1 99  ? 37.01960 5.22640   6.08455   1.000 40.18974  ? 99  ILE B CD1 1 
ATOM   752  N N   . ASN A 1 100 ? 42.15040 6.30241   4.55880   1.000 47.13786  ? 100 ASN B N   1 
ATOM   753  C CA  . ASN A 1 100 ? 43.35299 6.02005   3.77406   1.000 52.41174  ? 100 ASN B CA  1 
ATOM   754  C C   . ASN A 1 100 ? 44.41597 5.26578   4.56284   1.000 51.71906  ? 100 ASN B C   1 
ATOM   755  O O   . ASN A 1 100 ? 45.23517 4.57392   3.95711   1.000 52.35525  ? 100 ASN B O   1 
ATOM   756  C CB  . ASN A 1 100 ? 43.95565 7.30592   3.21973   1.000 44.70587  ? 100 ASN B CB  1 
ATOM   757  C CG  . ASN A 1 100 ? 43.13605 7.87879   2.08597   1.000 50.96489  ? 100 ASN B CG  1 
ATOM   758  O OD1 . ASN A 1 100 ? 42.56594 7.13589   1.28809   1.000 54.33043  ? 100 ASN B OD1 1 
ATOM   759  N ND2 . ASN A 1 100 ? 43.06942 9.20323   2.00641   1.000 52.81566  ? 100 ASN B ND2 1 
ATOM   760  N N   . ALA A 1 101 ? 44.40188 5.35147   5.88759   1.000 49.50815  ? 101 ALA B N   1 
ATOM   761  C CA  . ALA A 1 101 ? 45.38285 4.67640   6.72015   1.000 48.81204  ? 101 ALA B CA  1 
ATOM   762  C C   . ALA A 1 101 ? 44.93073 3.31143   7.22203   1.000 53.73080  ? 101 ALA B C   1 
ATOM   763  O O   . ALA A 1 101 ? 45.57958 2.77016   8.11782   1.000 55.42924  ? 101 ALA B O   1 
ATOM   764  C CB  . ALA A 1 101 ? 45.72663 5.54852   7.92378   1.000 45.77643  ? 101 ALA B CB  1 
ATOM   765  N N   . HIS A 1 102 ? 43.84489 2.73457   6.69566   1.000 54.56825  ? 102 HIS B N   1 
ATOM   766  C CA  . HIS A 1 102 ? 43.27842 1.55710   7.36245   1.000 51.29357  ? 102 HIS B CA  1 
ATOM   767  C C   . HIS A 1 102 ? 42.80596 0.49806   6.38566   1.000 51.22995  ? 102 HIS B C   1 
ATOM   768  O O   . HIS A 1 102 ? 41.78794 -0.15796  6.62033   1.000 60.07444  ? 102 HIS B O   1 
ATOM   769  C CB  . HIS A 1 102 ? 42.13401 1.94112   8.29475   1.000 52.09408  ? 102 HIS B CB  1 
ATOM   770  C CG  . HIS A 1 102 ? 42.58927 2.29367   9.67050   1.000 51.52751  ? 102 HIS B CG  1 
ATOM   771  N ND1 . HIS A 1 102 ? 42.91023 3.58325   10.03940  1.000 53.75773  ? 102 HIS B ND1 1 
ATOM   772  C CD2 . HIS A 1 102 ? 42.81822 1.51955   10.75765  1.000 49.30919  ? 102 HIS B CD2 1 
ATOM   773  C CE1 . HIS A 1 102 ? 43.29791 3.59195   11.30279  1.000 52.58771  ? 102 HIS B CE1 1 
ATOM   774  N NE2 . HIS A 1 102 ? 43.24356 2.35277   11.76305  1.000 55.70504  ? 102 HIS B NE2 1 
ATOM   775  N N   . ASN A 1 103 ? 43.54903 0.28629   5.29910   1.000 51.92978  ? 103 ASN B N   1 
ATOM   776  C CA  . ASN A 1 103 ? 43.40665 -0.91666  4.46987   1.000 56.44801  ? 103 ASN B CA  1 
ATOM   777  C C   . ASN A 1 103 ? 41.99737 -1.05332  3.89813   1.000 60.77871  ? 103 ASN B C   1 
ATOM   778  O O   . ASN A 1 103 ? 41.40269 -2.13993  3.89380   1.000 60.74552  ? 103 ASN B O   1 
ATOM   779  C CB  . ASN A 1 103 ? 43.79461 -2.17625  5.25199   1.000 63.46444  ? 103 ASN B CB  1 
ATOM   780  N N   . ILE A 1 104 ? 41.45422 0.06152   3.42366   1.000 57.00957  ? 104 ILE B N   1 
ATOM   781  C CA  . ILE A 1 104 ? 40.16212 0.08333   2.75389   1.000 55.47356  ? 104 ILE B CA  1 
ATOM   782  C C   . ILE A 1 104 ? 40.43740 0.12090   1.25703   1.000 53.56875  ? 104 ILE B C   1 
ATOM   783  O O   . ILE A 1 104 ? 41.16975 0.99840   0.77501   1.000 53.57413  ? 104 ILE B O   1 
ATOM   784  C CB  . ILE A 1 104 ? 39.31657 1.29367   3.19420   1.000 57.50103  ? 104 ILE B CB  1 
ATOM   785  C CG1 . ILE A 1 104 ? 39.05951 1.28682   4.70733   1.000 51.25881  ? 104 ILE B CG1 1 
ATOM   786  C CG2 . ILE A 1 104 ? 38.00340 1.31705   2.44138   1.000 54.76899  ? 104 ILE B CG2 1 
ATOM   787  C CD1 . ILE A 1 104 ? 38.41774 0.02963   5.21222   1.000 51.12106  ? 104 ILE B CD1 1 
ATOM   788  N N   . ASP A 1 105 ? 39.87590 -0.84125  0.52688   1.000 51.33817  ? 105 ASP B N   1 
ATOM   789  C CA  . ASP A 1 105 ? 39.96505 -0.85495  -0.92830  1.000 51.55630  ? 105 ASP B CA  1 
ATOM   790  C C   . ASP A 1 105 ? 38.81276 -0.06296  -1.51760  1.000 53.62679  ? 105 ASP B C   1 
ATOM   791  O O   . ASP A 1 105 ? 37.65172 -0.42764  -1.28815  1.000 53.84581  ? 105 ASP B O   1 
ATOM   792  C CB  . ASP A 1 105 ? 39.91561 -2.27050  -1.46416  1.000 55.25000  ? 105 ASP B CB  1 
ATOM   793  C CG  . ASP A 1 105 ? 40.27935 -2.34418  -2.93494  1.000 58.97355  ? 105 ASP B CG  1 
ATOM   794  O OD1 . ASP A 1 105 ? 39.78075 -1.50254  -3.71881  1.000 57.40320  ? 105 ASP B OD1 1 
ATOM   795  O OD2 . ASP A 1 105 ? 41.07375 -3.23276  -3.31059  1.000 65.68946  ? 105 ASP B OD2 1 
ATOM   796  N N   . PRO A 1 106 ? 39.07840 0.97547   -2.31664  1.000 52.61659  ? 106 PRO B N   1 
ATOM   797  C CA  . PRO A 1 106 ? 37.97348 1.78338   -2.86190  1.000 49.16722  ? 106 PRO B CA  1 
ATOM   798  C C   . PRO A 1 106 ? 36.96197 0.97313   -3.65661  1.000 55.55568  ? 106 PRO B C   1 
ATOM   799  O O   . PRO A 1 106 ? 35.75694 1.25181   -3.58239  1.000 51.77906  ? 106 PRO B O   1 
ATOM   800  C CB  . PRO A 1 106 ? 38.69848 2.80925   -3.74703  1.000 53.93581  ? 106 PRO B CB  1 
ATOM   801  C CG  . PRO A 1 106 ? 40.08357 2.92400   -3.14213  1.000 54.48142  ? 106 PRO B CG  1 
ATOM   802  C CD  . PRO A 1 106 ? 40.40464 1.52254   -2.67148  1.000 57.00351  ? 106 PRO B CD  1 
ATOM   803  N N   . TRP A 1 107 ? 37.41105 -0.03938  -4.40109  1.000 55.43480  ? 107 TRP B N   1 
ATOM   804  C CA  . TRP A 1 107 ? 36.51607 -0.77066  -5.28843  1.000 52.10642  ? 107 TRP B CA  1 
ATOM   805  C C   . TRP A 1 107 ? 35.86358 -1.98605  -4.65316  1.000 51.63906  ? 107 TRP B C   1 
ATOM   806  O O   . TRP A 1 107 ? 34.88686 -2.48964  -5.21420  1.000 52.84398  ? 107 TRP B O   1 
ATOM   807  C CB  . TRP A 1 107 ? 37.26667 -1.21448  -6.54972  1.000 49.04305  ? 107 TRP B CB  1 
ATOM   808  C CG  . TRP A 1 107 ? 37.57099 -0.07372  -7.44912  1.000 52.09825  ? 107 TRP B CG  1 
ATOM   809  C CD1 . TRP A 1 107 ? 38.71289 0.66715   -7.47050  1.000 49.61264  ? 107 TRP B CD1 1 
ATOM   810  C CD2 . TRP A 1 107 ? 36.69335 0.50299   -8.43678  1.000 50.64825  ? 107 TRP B CD2 1 
ATOM   811  N NE1 . TRP A 1 107 ? 38.61572 1.65946   -8.42659  1.000 49.44854  ? 107 TRP B NE1 1 
ATOM   812  C CE2 . TRP A 1 107 ? 37.38771 1.58071   -9.03251  1.000 52.47587  ? 107 TRP B CE2 1 
ATOM   813  C CE3 . TRP A 1 107 ? 35.39300 0.20856   -8.87502  1.000 52.03706  ? 107 TRP B CE3 1 
ATOM   814  C CZ2 . TRP A 1 107 ? 36.82908 2.36688   -10.05307 1.000 50.28339  ? 107 TRP B CZ2 1 
ATOM   815  C CZ3 . TRP A 1 107 ? 34.83797 0.98575   -9.89395  1.000 50.61364  ? 107 TRP B CZ3 1 
ATOM   816  C CH2 . TRP A 1 107 ? 35.56336 2.05688   -10.46879 1.000 49.20763  ? 107 TRP B CH2 1 
ATOM   817  N N   . LYS A 1 108 ? 36.36102 -2.46637  -3.50705  1.000 52.10086  ? 108 LYS B N   1 
ATOM   818  C CA  . LYS A 1 108 ? 35.90377 -3.73037  -2.93907  1.000 53.64630  ? 108 LYS B CA  1 
ATOM   819  C C   . LYS A 1 108 ? 35.41858 -3.65310  -1.50340  1.000 50.60699  ? 108 LYS B C   1 
ATOM   820  O O   . LYS A 1 108 ? 34.65633 -4.53472  -1.08613  1.000 46.71850  ? 108 LYS B O   1 
ATOM   821  C CB  . LYS A 1 108 ? 37.01525 -4.79229  -2.98360  1.000 53.60381  ? 108 LYS B CB  1 
ATOM   822  C CG  . LYS A 1 108 ? 37.43943 -5.23847  -4.36859  1.000 56.74369  ? 108 LYS B CG  1 
ATOM   823  C CD  . LYS A 1 108 ? 38.89495 -5.68404  -4.37986  1.000 62.76763  ? 108 LYS B CD  1 
ATOM   824  C CE  . LYS A 1 108 ? 39.32886 -6.23680  -3.02870  1.000 62.72092  ? 108 LYS B CE  1 
ATOM   825  N NZ  . LYS A 1 108 ? 40.76680 -5.94823  -2.73884  1.000 74.02773  ? 108 LYS B NZ  1 
ATOM   826  N N   . SER A 1 109 ? 35.84830 -2.66327  -0.73186  1.000 48.83860  ? 109 SER B N   1 
ATOM   827  C CA  . SER A 1 109 ? 35.43231 -2.58696  0.65784   1.000 47.51924  ? 109 SER B CA  1 
ATOM   828  C C   . SER A 1 109 ? 33.97704 -2.12149  0.74692   1.000 51.03362  ? 109 SER B C   1 
ATOM   829  O O   . SER A 1 109 ? 33.43802 -1.50147  -0.17721  1.000 49.96586  ? 109 SER B O   1 
ATOM   830  C CB  . SER A 1 109 ? 36.35132 -1.64563  1.43231   1.000 51.83522  ? 109 SER B CB  1 
ATOM   831  O OG  . SER A 1 109 ? 37.64134 -2.21191  1.62719   1.000 48.83398  ? 109 SER B OG  1 
ATOM   832  N N   . GLN A 1 110 ? 33.33616 -2.45527  1.86264   1.000 46.03449  ? 110 GLN B N   1 
ATOM   833  C CA  . GLN A 1 110 ? 31.92406 -2.19479  2.08866   1.000 47.63824  ? 110 GLN B CA  1 
ATOM   834  C C   . GLN A 1 110 ? 31.79073 -1.27289  3.29091   1.000 49.62602  ? 110 GLN B C   1 
ATOM   835  O O   . GLN A 1 110 ? 32.42840 -1.50483  4.32461   1.000 52.52568  ? 110 GLN B O   1 
ATOM   836  C CB  . GLN A 1 110 ? 31.15945 -3.50427  2.32197   1.000 45.45928  ? 110 GLN B CB  1 
ATOM   837  C CG  . GLN A 1 110 ? 30.92304 -4.31935  1.06242   1.000 45.43884  ? 110 GLN B CG  1 
ATOM   838  C CD  . GLN A 1 110 ? 30.15938 -5.60834  1.31778   1.000 46.96657  ? 110 GLN B CD  1 
ATOM   839  O OE1 . GLN A 1 110 ? 30.09178 -6.08208  2.45224   1.000 48.64381  ? 110 GLN B OE1 1 
ATOM   840  N NE2 . GLN A 1 110 ? 29.57708 -6.18110  0.26136   1.000 45.48258  ? 110 GLN B NE2 1 
ATOM   841  N N   . GLY A 1 111 ? 30.97584 -0.23173  3.15508   1.000 42.25537  ? 111 GLY B N   1 
ATOM   842  C CA  . GLY A 1 111 ? 30.70179 0.69015   4.24762   1.000 44.35716  ? 111 GLY B CA  1 
ATOM   843  C C   . GLY A 1 111 ? 29.34324 0.43202   4.87643   1.000 44.26296  ? 111 GLY B C   1 
ATOM   844  O O   . GLY A 1 111 ? 28.36342 0.15187   4.17685   1.000 43.43109  ? 111 GLY B O   1 
ATOM   845  N N   . TRP A 1 112 ? 29.29160 0.55998   6.20841   1.000 42.73606  ? 112 TRP B N   1 
ATOM   846  C CA  . TRP A 1 112 ? 28.18439 0.08039   7.03025   1.000 41.80387  ? 112 TRP B CA  1 
ATOM   847  C C   . TRP A 1 112 ? 27.68940 1.16994   7.97354   1.000 43.06611  ? 112 TRP B C   1 
ATOM   848  O O   . TRP A 1 112 ? 28.50060 1.82636   8.63476   1.000 38.93641  ? 112 TRP B O   1 
ATOM   849  C CB  . TRP A 1 112 ? 28.61667 -1.12503  7.88011   1.000 40.95556  ? 112 TRP B CB  1 
ATOM   850  C CG  . TRP A 1 112 ? 28.82289 -2.37142  7.10965   1.000 41.94366  ? 112 TRP B CG  1 
ATOM   851  C CD1 . TRP A 1 112 ? 30.00143 -2.82323  6.56705   1.000 47.63938  ? 112 TRP B CD1 1 
ATOM   852  C CD2 . TRP A 1 112 ? 27.83313 -3.35239  6.79185   1.000 48.74322  ? 112 TRP B CD2 1 
ATOM   853  N NE1 . TRP A 1 112 ? 29.79571 -4.01950  5.92500   1.000 44.81536  ? 112 TRP B NE1 1 
ATOM   854  C CE2 . TRP A 1 112 ? 28.47813 -4.37170  6.05042   1.000 42.22870  ? 112 TRP B CE2 1 
ATOM   855  C CE3 . TRP A 1 112 ? 26.45578 -3.46487  7.04614   1.000 41.94155  ? 112 TRP B CE3 1 
ATOM   856  C CZ2 . TRP A 1 112 ? 27.79524 -5.48037  5.56256   1.000 41.73053  ? 112 TRP B CZ2 1 
ATOM   857  C CZ3 . TRP A 1 112 ? 25.79096 -4.57330  6.57485   1.000 43.79835  ? 112 TRP B CZ3 1 
ATOM   858  C CH2 . TRP A 1 112 ? 26.45690 -5.56644  5.83465   1.000 43.92698  ? 112 TRP B CH2 1 
ATOM   859  N N   . CYS A 1 113 ? 26.35642 1.33546   8.05960   1.000 40.31847  ? 113 CYS B N   1 
ATOM   860  C CA  . CYS A 1 113 ? 25.74187 2.20825   9.06258   1.000 40.12796  ? 113 CYS B CA  1 
ATOM   861  C C   . CYS A 1 113 ? 24.34498 1.70657   9.40028   1.000 38.13537  ? 113 CYS B C   1 
ATOM   862  O O   . CYS A 1 113 ? 23.71235 0.99688   8.61667   1.000 36.27718  ? 113 CYS B O   1 
ATOM   863  C CB  . CYS A 1 113 ? 25.66707 3.66859   8.59564   1.000 39.16199  ? 113 CYS B CB  1 
ATOM   864  S SG  . CYS A 1 113 ? 24.46659 3.90406   7.26942   1.000 43.82275  ? 113 CYS B SG  1 
ATOM   865  N N   . ARG A 1 114 ? 23.87202 2.08093   10.59338  1.000 39.13855  ? 114 ARG B N   1 
ATOM   866  C CA  . ARG A 1 114 ? 22.53620 1.68691   11.06676  1.000 40.11473  ? 114 ARG B CA  1 
ATOM   867  C C   . ARG A 1 114 ? 21.48292 2.60981   10.44505  1.000 39.75569  ? 114 ARG B C   1 
ATOM   868  O O   . ARG A 1 114 ? 21.02171 3.58570   11.04165  1.000 38.72991  ? 114 ARG B O   1 
ATOM   869  C CB  . ARG A 1 114 ? 22.45707 1.71378   12.59089  1.000 36.56002  ? 114 ARG B CB  1 
ATOM   870  C CG  . ARG A 1 114 ? 21.18868 1.02213   13.12543  1.000 41.68793  ? 114 ARG B CG  1 
ATOM   871  C CD  . ARG A 1 114 ? 21.25817 0.77368   14.63048  1.000 44.29222  ? 114 ARG B CD  1 
ATOM   872  N NE  . ARG A 1 114 ? 22.04557 -0.42133  14.92924  1.000 45.29546  ? 114 ARG B NE  1 
ATOM   873  C CZ  . ARG A 1 114 ? 21.58671 -1.66279  14.87051  1.000 50.51016  ? 114 ARG B CZ  1 
ATOM   874  N NH1 . ARG A 1 114 ? 20.31182 -1.91505  14.62189  1.000 50.37481  ? 114 ARG B NH1 1 
ATOM   875  N NH2 . ARG A 1 114 ? 22.42717 -2.67715  15.07650  1.000 54.00502  ? 114 ARG B NH2 1 
ATOM   876  N N   . GLY A 1 115 ? 21.09878 2.30183   9.21349   1.000 35.76780  ? 115 GLY B N   1 
ATOM   877  C CA  . GLY A 1 115 ? 20.18463 3.19543   8.53438   1.000 37.34332  ? 115 GLY B CA  1 
ATOM   878  C C   . GLY A 1 115 ? 20.84605 3.86542   7.35832   1.000 38.37978  ? 115 GLY B C   1 
ATOM   879  O O   . GLY A 1 115 ? 21.23494 5.03350   7.44595   1.000 39.49002  ? 115 GLY B O   1 
ATOM   880  N N   . MET A 1 116 ? 20.95303 3.12910   6.24769   1.000 34.79696  ? 116 MET B N   1 
ATOM   881  C CA  . MET A 1 116 ? 21.73687 3.58064   5.10832   1.000 36.12146  ? 116 MET B CA  1 
ATOM   882  C C   . MET A 1 116 ? 21.31178 4.94714   4.59335   1.000 38.06327  ? 116 MET B C   1 
ATOM   883  O O   . MET A 1 116 ? 22.15416 5.72082   4.12092   1.000 39.80628  ? 116 MET B O   1 
ATOM   884  C CB  . MET A 1 116 ? 21.65846 2.54714   3.98953   1.000 39.75985  ? 116 MET B CB  1 
ATOM   885  C CG  . MET A 1 116 ? 23.02697 1.97355   3.61674   1.000 40.79384  ? 116 MET B CG  1 
ATOM   886  S SD  . MET A 1 116 ? 22.89108 0.71201   2.35568   1.000 43.42335  ? 116 MET B SD  1 
ATOM   887  C CE  . MET A 1 116 ? 22.65618 1.70965   0.89627   1.000 40.46494  ? 116 MET B CE  1 
ATOM   888  N N   . SER A 1 117 ? 20.02454 5.26624   4.66192   1.000 37.36931  ? 117 SER B N   1 
ATOM   889  C CA  . SER A 1 117 ? 19.54345 6.55921   4.18212   1.000 38.12107  ? 117 SER B CA  1 
ATOM   890  C C   . SER A 1 117 ? 19.86897 7.70491   5.13717   1.000 36.99632  ? 117 SER B C   1 
ATOM   891  O O   . SER A 1 117 ? 19.56329 8.86014   4.83293   1.000 34.43302  ? 117 SER B O   1 
ATOM   892  C CB  . SER A 1 117 ? 18.02411 6.50934   3.96602   1.000 36.37645  ? 117 SER B CB  1 
ATOM   893  O OG  . SER A 1 117 ? 17.38149 6.20708   5.19903   1.000 33.40134  ? 117 SER B OG  1 
ATOM   894  N N   . PHE A 1 118 ? 20.45151 7.42676   6.29184   1.000 34.47903  ? 118 PHE B N   1 
ATOM   895  C CA  . PHE A 1 118 ? 20.72847 8.52075   7.20446   1.000 35.29799  ? 118 PHE B CA  1 
ATOM   896  C C   . PHE A 1 118 ? 22.18841 8.96916   7.11117   1.000 37.33693  ? 118 PHE B C   1 
ATOM   897  O O   . PHE A 1 118 ? 22.46452 10.09708  6.68105   1.000 38.33038  ? 118 PHE B O   1 
ATOM   898  C CB  . PHE A 1 118 ? 20.34835 8.10589   8.62201   1.000 36.21377  ? 118 PHE B CB  1 
ATOM   899  C CG  . PHE A 1 118 ? 20.46912 9.20659   9.61222   1.000 38.12260  ? 118 PHE B CG  1 
ATOM   900  C CD1 . PHE A 1 118 ? 19.43031 10.10922  9.79547   1.000 33.73931  ? 118 PHE B CD1 1 
ATOM   901  C CD2 . PHE A 1 118 ? 21.63867 9.35549   10.35855  1.000 31.58641  ? 118 PHE B CD2 1 
ATOM   902  C CE1 . PHE A 1 118 ? 19.54611 11.15010  10.73069  1.000 39.14272  ? 118 PHE B CE1 1 
ATOM   903  C CE2 . PHE A 1 118 ? 21.76849 10.38949  11.28290  1.000 35.61957  ? 118 PHE B CE2 1 
ATOM   904  C CZ  . PHE A 1 118 ? 20.71572 11.29885  11.46954  1.000 36.21780  ? 118 PHE B CZ  1 
ATOM   905  N N   . ASP A 1 119 ? 23.13701 8.08492   7.45703   1.000 38.66367  ? 119 ASP B N   1 
ATOM   906  C CA  . ASP A 1 119 ? 24.53993 8.50493   7.54553   1.000 35.51383  ? 119 ASP B CA  1 
ATOM   907  C C   . ASP A 1 119 ? 25.18790 8.69140   6.18357   1.000 33.70435  ? 119 ASP B C   1 
ATOM   908  O O   . ASP A 1 119 ? 25.91976 9.66594   5.97838   1.000 35.36439  ? 119 ASP B O   1 
ATOM   909  C CB  . ASP A 1 119 ? 25.33773 7.51457   8.37537   1.000 32.36180  ? 119 ASP B CB  1 
ATOM   910  C CG  . ASP A 1 119 ? 24.64879 7.20837   9.67234   1.000 36.34598  ? 119 ASP B CG  1 
ATOM   911  O OD1 . ASP A 1 119 ? 23.68634 6.42308   9.64219   1.000 33.33970  ? 119 ASP B OD1 1 
ATOM   912  O OD2 . ASP A 1 119 ? 25.02713 7.80324   10.70322  1.000 38.34796  ? 119 ASP B OD2 1 
ATOM   913  N N   . PHE A 1 120 ? 24.95638 7.78377   5.24835   1.000 35.69396  ? 120 PHE B N   1 
ATOM   914  C CA  . PHE A 1 120 ? 25.70270 7.95260   4.00376   1.000 34.22785  ? 120 PHE B CA  1 
ATOM   915  C C   . PHE A 1 120 ? 25.34730 9.23318   3.24708   1.000 35.39289  ? 120 PHE B C   1 
ATOM   916  O O   . PHE A 1 120 ? 26.24771 9.83755   2.66122   1.000 36.35190  ? 120 PHE B O   1 
ATOM   917  C CB  . PHE A 1 120 ? 25.54527 6.71950   3.11462   1.000 32.08050  ? 120 PHE B CB  1 
ATOM   918  C CG  . PHE A 1 120 ? 26.52224 5.63927   3.46383   1.000 39.08612  ? 120 PHE B CG  1 
ATOM   919  C CD1 . PHE A 1 120 ? 27.89558 5.82923   3.23385   1.000 39.93376  ? 120 PHE B CD1 1 
ATOM   920  C CD2 . PHE A 1 120 ? 26.09966 4.47286   4.09593   1.000 35.10046  ? 120 PHE B CD2 1 
ATOM   921  C CE1 . PHE A 1 120 ? 28.82105 4.85803   3.59363   1.000 39.52130  ? 120 PHE B CE1 1 
ATOM   922  C CE2 . PHE A 1 120 ? 27.00882 3.49383   4.45430   1.000 37.84955  ? 120 PHE B CE2 1 
ATOM   923  C CZ  . PHE A 1 120 ? 28.38438 3.68527   4.20426   1.000 44.13559  ? 120 PHE B CZ  1 
ATOM   924  N N   . PRO A 1 121 ? 24.08513 9.69909   3.22074   1.000 39.46967  ? 121 PRO B N   1 
ATOM   925  C CA  . PRO A 1 121 ? 23.83162 10.98906  2.55274   1.000 33.72696  ? 121 PRO B CA  1 
ATOM   926  C C   . PRO A 1 121 ? 24.48427 12.15611  3.26015   1.000 34.68627  ? 121 PRO B C   1 
ATOM   927  O O   . PRO A 1 121 ? 24.86616 13.12086  2.59422   1.000 34.66888  ? 121 PRO B O   1 
ATOM   928  C CB  . PRO A 1 121 ? 22.29665 11.10003  2.55670   1.000 30.40565  ? 121 PRO B CB  1 
ATOM   929  C CG  . PRO A 1 121 ? 21.86101 9.68032   2.53106   1.000 35.20721  ? 121 PRO B CG  1 
ATOM   930  C CD  . PRO A 1 121 ? 22.81640 8.97452   3.45718   1.000 35.58178  ? 121 PRO B CD  1 
ATOM   931  N N   . ILE A 1 122 ? 24.63511 12.10227  4.58385   1.000 35.76784  ? 122 ILE B N   1 
ATOM   932  C CA  . ILE A 1 122 ? 25.33727 13.17533  5.28367   1.000 35.96999  ? 122 ILE B CA  1 
ATOM   933  C C   . ILE A 1 122 ? 26.83751 13.10206  5.01110   1.000 36.55470  ? 122 ILE B C   1 
ATOM   934  O O   . ILE A 1 122 ? 27.49694 14.12848  4.77855   1.000 34.70429  ? 122 ILE B O   1 
ATOM   935  C CB  . ILE A 1 122 ? 25.03257 13.12322  6.79071   1.000 37.59585  ? 122 ILE B CB  1 
ATOM   936  C CG1 . ILE A 1 122 ? 23.56254 13.50265  7.07782   1.000 37.17858  ? 122 ILE B CG1 1 
ATOM   937  C CG2 . ILE A 1 122 ? 25.96352 14.02564  7.54531   1.000 36.37813  ? 122 ILE B CG2 1 
ATOM   938  C CD1 . ILE A 1 122 ? 23.04827 12.94861  8.42059   1.000 33.91968  ? 122 ILE B CD1 1 
ATOM   939  N N   . LEU A 1 123 ? 27.39627 11.89144  5.02167   1.000 35.15074  ? 123 LEU B N   1 
ATOM   940  C CA  . LEU A 1 123 ? 28.79455 11.72299  4.64533   1.000 38.68260  ? 123 LEU B CA  1 
ATOM   941  C C   . LEU A 1 123 ? 29.03846 12.27766  3.25013   1.000 39.42135  ? 123 LEU B C   1 
ATOM   942  O O   . LEU A 1 123 ? 29.94179 13.10402  3.04619   1.000 40.04458  ? 123 LEU B O   1 
ATOM   943  C CB  . LEU A 1 123 ? 29.20716 10.25046  4.72655   1.000 35.21184  ? 123 LEU B CB  1 
ATOM   944  C CG  . LEU A 1 123 ? 30.72264 10.04411  4.58632   1.000 38.84243  ? 123 LEU B CG  1 
ATOM   945  C CD1 . LEU A 1 123 ? 31.44617 10.27538  5.92604   1.000 36.58469  ? 123 LEU B CD1 1 
ATOM   946  C CD2 . LEU A 1 123 ? 31.06701 8.65291   3.99580   1.000 31.59738  ? 123 LEU B CD2 1 
ATOM   947  N N   . VAL A 1 124 ? 28.19702 11.88361  2.28808   1.000 35.29921  ? 124 VAL B N   1 
ATOM   948  C CA  . VAL A 1 124 ? 28.40653 12.33225  0.91696   1.000 37.59082  ? 124 VAL B CA  1 
ATOM   949  C C   . VAL A 1 124 ? 28.18749 13.83157  0.81317   1.000 37.47032  ? 124 VAL B C   1 
ATOM   950  O O   . VAL A 1 124 ? 28.87337 14.51150  0.04259   1.000 40.23375  ? 124 VAL B O   1 
ATOM   951  C CB  . VAL A 1 124 ? 27.51735 11.55181  -0.07172  1.000 37.76974  ? 124 VAL B CB  1 
ATOM   952  C CG1 . VAL A 1 124 ? 27.76562 12.02882  -1.49854  1.000 38.36880  ? 124 VAL B CG1 1 
ATOM   953  C CG2 . VAL A 1 124 ? 27.81283 10.07691  0.02413   1.000 40.33716  ? 124 VAL B CG2 1 
ATOM   954  N N   . ASP A 1 125 ? 27.28368 14.39750  1.61113   1.000 33.29218  ? 125 ASP B N   1 
ATOM   955  C CA  . ASP A 1 125 ? 27.16842 15.84115  1.50828   1.000 35.04014  ? 125 ASP B CA  1 
ATOM   956  C C   . ASP A 1 125 ? 28.40354 16.53230  2.07887   1.000 38.49494  ? 125 ASP B C   1 
ATOM   957  O O   . ASP A 1 125 ? 28.77096 17.61551  1.60810   1.000 38.37223  ? 125 ASP B O   1 
ATOM   958  C CB  . ASP A 1 125 ? 25.91490 16.36817  2.18417   1.000 27.00622  ? 125 ASP B CB  1 
ATOM   959  C CG  . ASP A 1 125 ? 25.80408 17.86529  2.04093   1.000 34.12356  ? 125 ASP B CG  1 
ATOM   960  O OD1 . ASP A 1 125 ? 25.71470 18.32979  0.88722   1.000 33.65517  ? 125 ASP B OD1 1 
ATOM   961  O OD2 . ASP A 1 125 ? 25.82272 18.58550  3.05951   1.000 35.62031  ? 125 ASP B OD2 1 
ATOM   962  N N   . LEU A 1 126 ? 29.04401 15.92892  3.08727   1.000 35.07229  ? 126 LEU B N   1 
ATOM   963  C CA  . LEU A 1 126 ? 30.25815 16.51419  3.64185   1.000 35.55097  ? 126 LEU B CA  1 
ATOM   964  C C   . LEU A 1 126 ? 31.41769 16.37327  2.66188   1.000 39.59014  ? 126 LEU B C   1 
ATOM   965  O O   . LEU A 1 126 ? 32.27814 17.25428  2.56745   1.000 39.01966  ? 126 LEU B O   1 
ATOM   966  C CB  . LEU A 1 126 ? 30.60462 15.83932  4.96923   1.000 36.12604  ? 126 LEU B CB  1 
ATOM   967  C CG  . LEU A 1 126 ? 29.76855 16.18270  6.19720   1.000 39.26945  ? 126 LEU B CG  1 
ATOM   968  C CD1 . LEU A 1 126 ? 30.28631 15.44057  7.44326   1.000 38.21420  ? 126 LEU B CD1 1 
ATOM   969  C CD2 . LEU A 1 126 ? 29.73696 17.69419  6.42263   1.000 39.38402  ? 126 LEU B CD2 1 
ATOM   970  N N   . ILE A 1 127 ? 31.46713 15.26115  1.93108   1.000 38.30320  ? 127 ILE B N   1 
ATOM   971  C CA  . ILE A 1 127 ? 32.51370 15.11110  0.92762   1.000 37.15300  ? 127 ILE B CA  1 
ATOM   972  C C   . ILE A 1 127 ? 32.26195 16.06575  -0.23777  1.000 38.88553  ? 127 ILE B C   1 
ATOM   973  O O   . ILE A 1 127 ? 33.19995 16.68033  -0.75837  1.000 42.07757  ? 127 ILE B O   1 
ATOM   974  C CB  . ILE A 1 127 ? 32.61270 13.63853  0.47947   1.000 34.23156  ? 127 ILE B CB  1 
ATOM   975  C CG1 . ILE A 1 127 ? 33.17837 12.77039  1.60823   1.000 30.25918  ? 127 ILE B CG1 1 
ATOM   976  C CG2 . ILE A 1 127 ? 33.44092 13.51534  -0.76896  1.000 30.21981  ? 127 ILE B CG2 1 
ATOM   977  C CD1 . ILE A 1 127 ? 32.90981 11.29270  1.41318   1.000 32.05340  ? 127 ILE B CD1 1 
ATOM   978  N N   . ARG A 1 128 ? 30.99137 16.23406  -0.64658  1.000 37.81844  ? 128 ARG B N   1 
ATOM   979  C CA  . ARG A 1 128 ? 30.66223 17.24075  -1.66211  1.000 40.50413  ? 128 ARG B CA  1 
ATOM   980  C C   . ARG A 1 128 ? 31.23927 18.59826  -1.29416  1.000 38.80152  ? 128 ARG B C   1 
ATOM   981  O O   . ARG A 1 128 ? 31.70689 19.34126  -2.16208  1.000 40.02611  ? 128 ARG B O   1 
ATOM   982  C CB  . ARG A 1 128 ? 29.14029 17.37785  -1.83564  1.000 38.42661  ? 128 ARG B CB  1 
ATOM   983  C CG  . ARG A 1 128 ? 28.46202 16.21050  -2.53849  1.000 44.12936  ? 128 ARG B CG  1 
ATOM   984  C CD  . ARG A 1 128 ? 27.14864 16.61706  -3.22681  1.000 44.64262  ? 128 ARG B CD  1 
ATOM   985  N NE  . ARG A 1 128 ? 26.14960 15.56296  -3.10355  1.000 54.23972  ? 128 ARG B NE  1 
ATOM   986  C CZ  . ARG A 1 128 ? 26.25519 14.37399  -3.68650  1.000 54.78993  ? 128 ARG B CZ  1 
ATOM   987  N NH1 . ARG A 1 128 ? 27.31518 14.05800  -4.43529  1.000 58.10066  ? 128 ARG B NH1 1 
ATOM   988  N NH2 . ARG A 1 128 ? 25.31299 13.45783  -3.46430  1.000 36.02485  ? 128 ARG B NH2 1 
ATOM   989  N N   . ASP A 1 129 ? 31.18216 18.94420  -0.00656  1.000 36.07797  ? 129 ASP B N   1 
ATOM   990  C CA  . ASP A 1 129 ? 31.74089 20.19917  0.47668   1.000 41.32849  ? 129 ASP B CA  1 
ATOM   991  C C   . ASP A 1 129 ? 33.19258 20.39482  0.03110   1.000 40.42005  ? 129 ASP B C   1 
ATOM   992  O O   . ASP A 1 129 ? 33.61163 21.53150  -0.23486  1.000 38.93927  ? 129 ASP B O   1 
ATOM   993  C CB  . ASP A 1 129 ? 31.64948 20.23887  2.00316   1.000 41.43276  ? 129 ASP B CB  1 
ATOM   994  C CG  . ASP A 1 129 ? 30.38655 20.92046  2.49370   1.000 42.17555  ? 129 ASP B CG  1 
ATOM   995  O OD1 . ASP A 1 129 ? 29.66457 21.48896  1.64291   1.000 40.84972  ? 129 ASP B OD1 1 
ATOM   996  O OD2 . ASP A 1 129 ? 30.12653 20.89171  3.72022   1.000 35.60591  ? 129 ASP B OD2 1 
ATOM   997  N N   . ILE A 1 130 ? 33.96811 19.30906  -0.05003  1.000 35.99382  ? 130 ILE B N   1 
ATOM   998  C CA  . ILE A 1 130 ? 35.33842 19.39815  -0.57159  1.000 42.35001  ? 130 ILE B CA  1 
ATOM   999  C C   . ILE A 1 130 ? 35.32705 19.97377  -1.97540  1.000 44.76511  ? 130 ILE B C   1 
ATOM   1000 O O   . ILE A 1 130 ? 36.14415 20.83408  -2.32493  1.000 42.57873  ? 130 ILE B O   1 
ATOM   1001 C CB  . ILE A 1 130 ? 36.01736 18.01643  -0.56249  1.000 38.42888  ? 130 ILE B CB  1 
ATOM   1002 C CG1 . ILE A 1 130 ? 36.17774 17.49541  0.85503   1.000 32.28939  ? 130 ILE B CG1 1 
ATOM   1003 C CG2 . ILE A 1 130 ? 37.33236 18.04611  -1.32556  1.000 43.93572  ? 130 ILE B CG2 1 
ATOM   1004 C CD1 . ILE A 1 130 ? 36.33988 16.01465  0.90546   1.000 35.85940  ? 130 ILE B CD1 1 
ATOM   1005 N N   . GLN A 1 131 ? 34.37615 19.53147  -2.79399  1.000 45.65302  ? 131 GLN B N   1 
ATOM   1006 C CA  . GLN A 1 131 ? 34.33100 20.00205  -4.16704  1.000 42.68832  ? 131 GLN B CA  1 
ATOM   1007 C C   . GLN A 1 131 ? 33.77884 21.41520  -4.25972  1.000 39.30915  ? 131 GLN B C   1 
ATOM   1008 O O   . GLN A 1 131 ? 34.21532 22.18558  -5.12258  1.000 42.51978  ? 131 GLN B O   1 
ATOM   1009 C CB  . GLN A 1 131 ? 33.52701 19.01737  -5.01982  1.000 41.79527  ? 131 GLN B CB  1 
ATOM   1010 C CG  . GLN A 1 131 ? 34.45294 18.06940  -5.73027  1.000 47.53459  ? 131 GLN B CG  1 
ATOM   1011 C CD  . GLN A 1 131 ? 33.78585 16.89102  -6.37329  1.000 53.88614  ? 131 GLN B CD  1 
ATOM   1012 O OE1 . GLN A 1 131 ? 32.73216 17.01276  -6.98905  1.000 56.22416  ? 131 GLN B OE1 1 
ATOM   1013 N NE2 . GLN A 1 131 ? 34.41325 15.72393  -6.24889  1.000 56.32748  ? 131 GLN B NE2 1 
ATOM   1014 N N   . ARG A 1 132 ? 32.83386 21.78691  -3.38934  1.000 42.92974  ? 132 ARG B N   1 
ATOM   1015 C CA  . ARG A 1 132 ? 32.38981 23.17914  -3.35695  1.000 42.60177  ? 132 ARG B CA  1 
ATOM   1016 C C   . ARG A 1 132 ? 33.50526 24.08930  -2.84700  1.000 37.15279  ? 132 ARG B C   1 
ATOM   1017 O O   . ARG A 1 132 ? 33.66097 25.21992  -3.32031  1.000 36.16958  ? 132 ARG B O   1 
ATOM   1018 C CB  . ARG A 1 132 ? 31.14135 23.33957  -2.48634  1.000 36.81475  ? 132 ARG B CB  1 
ATOM   1019 C CG  . ARG A 1 132 ? 29.98694 22.38850  -2.76964  1.000 41.69974  ? 132 ARG B CG  1 
ATOM   1020 C CD  . ARG A 1 132 ? 28.92308 22.48499  -1.65624  1.000 38.26905  ? 132 ARG B CD  1 
ATOM   1021 N NE  . ARG A 1 132 ? 27.79289 21.60481  -1.93071  1.000 39.73862  ? 132 ARG B NE  1 
ATOM   1022 C CZ  . ARG A 1 132 ? 27.42269 20.56985  -1.18511  1.000 41.19178  ? 132 ARG B CZ  1 
ATOM   1023 N NH1 . ARG A 1 132 ? 28.07085 20.24770  -0.06683  1.000 37.76507  ? 132 ARG B NH1 1 
ATOM   1024 N NH2 . ARG A 1 132 ? 26.38482 19.82489  -1.58186  1.000 40.14539  ? 132 ARG B NH2 1 
ATOM   1025 N N   . LEU A 1 133 ? 34.27907 23.61532  -1.87327  1.000 40.03172  ? 133 LEU B N   1 
ATOM   1026 C CA  . LEU A 1 133 ? 35.46974 24.35250  -1.43545  1.000 46.29787  ? 133 LEU B CA  1 
ATOM   1027 C C   . LEU A 1 133 ? 36.38603 24.70536  -2.60629  1.000 43.12488  ? 133 LEU B C   1 
ATOM   1028 O O   . LEU A 1 133 ? 36.97944 25.78389  -2.62446  1.000 43.93434  ? 133 LEU B O   1 
ATOM   1029 C CB  . LEU A 1 133 ? 36.24116 23.54245  -0.38981  1.000 35.58638  ? 133 LEU B CB  1 
ATOM   1030 C CG  . LEU A 1 133 ? 37.27473 24.37638  0.35926   1.000 43.84827  ? 133 LEU B CG  1 
ATOM   1031 C CD1 . LEU A 1 133 ? 36.58132 25.47707  1.17366   1.000 42.24153  ? 133 LEU B CD1 1 
ATOM   1032 C CD2 . LEU A 1 133 ? 38.10915 23.49924  1.26854   1.000 43.11673  ? 133 LEU B CD2 1 
ATOM   1033 N N   . ASN A 1 134 ? 36.49052 23.81510  -3.60567  1.000 44.80690  ? 134 ASN B N   1 
ATOM   1034 C CA  . ASN A 1 134 ? 37.25971 24.04822  -4.83233  1.000 45.90276  ? 134 ASN B CA  1 
ATOM   1035 C C   . ASN A 1 134 ? 36.51708 24.90399  -5.85582  1.000 42.60431  ? 134 ASN B C   1 
ATOM   1036 O O   . ASN A 1 134 ? 36.94002 24.95643  -7.01446  1.000 44.59345  ? 134 ASN B O   1 
ATOM   1037 C CB  . ASN A 1 134 ? 37.63307 22.71358  -5.49091  1.000 38.04237  ? 134 ASN B CB  1 
ATOM   1038 C CG  . ASN A 1 134 ? 38.80919 22.03482  -4.81762  1.000 48.47526  ? 134 ASN B CG  1 
ATOM   1039 O OD1 . ASN A 1 134 ? 38.65100 21.34855  -3.79892  1.000 49.89052  ? 134 ASN B OD1 1 
ATOM   1040 N ND2 . ASN A 1 134 ? 39.99664 22.18561  -5.40384  1.000 50.66155  ? 134 ASN B ND2 1 
ATOM   1041 N N   . GLY A 1 135 ? 35.40585 25.53048  -5.49005  1.000 42.66495  ? 135 GLY B N   1 
ATOM   1042 C CA  . GLY A 1 135 ? 34.63750 26.30316  -6.45728  1.000 46.69022  ? 135 GLY B CA  1 
ATOM   1043 C C   . GLY A 1 135 ? 33.81453 25.52356  -7.46708  1.000 43.05993  ? 135 GLY B C   1 
ATOM   1044 O O   . GLY A 1 135 ? 33.40616 26.09327  -8.48474  1.000 43.59346  ? 135 GLY B O   1 
ATOM   1045 N N   . VAL A 1 136 ? 33.55117 24.25193  -7.24003  1.000 43.10823  ? 136 VAL B N   1 
ATOM   1046 C CA  . VAL A 1 136 ? 32.70360 23.50460  -8.16542  1.000 45.05088  ? 136 VAL B CA  1 
ATOM   1047 C C   . VAL A 1 136 ? 31.23292 23.85612  -7.94433  1.000 45.93640  ? 136 VAL B C   1 
ATOM   1048 O O   . VAL A 1 136 ? 30.73847 23.86138  -6.80824  1.000 44.78182  ? 136 VAL B O   1 
ATOM   1049 C CB  . VAL A 1 136 ? 32.95182 21.99819  -8.02574  1.000 47.94663  ? 136 VAL B CB  1 
ATOM   1050 C CG1 . VAL A 1 136 ? 31.95325 21.21031  -8.87884  1.000 43.34089  ? 136 VAL B CG1 1 
ATOM   1051 C CG2 . VAL A 1 136 ? 34.39960 21.70693  -8.42919  1.000 42.71788  ? 136 VAL B CG2 1 
ATOM   1052 N N   . SER A 1 137 ? 30.53494 24.16097  -9.04224  1.000 46.29531  ? 137 SER B N   1 
ATOM   1053 C CA  . SER A 1 137 ? 29.09023 24.37488  -9.03974  1.000 41.08516  ? 137 SER B CA  1 
ATOM   1054 C C   . SER A 1 137 ? 28.33690 23.14488  -8.53457  1.000 42.44239  ? 137 SER B C   1 
ATOM   1055 O O   . SER A 1 137 ? 28.79093 22.00839  -8.69486  1.000 44.31687  ? 137 SER B O   1 
ATOM   1056 C CB  . SER A 1 137 ? 28.62996 24.68524  -10.46101 1.000 41.57786  ? 137 SER B CB  1 
ATOM   1057 O OG  . SER A 1 137 ? 28.86342 26.03603  -10.77598 1.000 58.76411  ? 137 SER B OG  1 
ATOM   1058 N N   . GLU A 1 138 ? 27.13930 23.37456  -7.96969  1.000 40.69064  ? 138 GLU B N   1 
ATOM   1059 C CA  . GLU A 1 138 ? 26.32617 22.26366  -7.47900  1.000 41.06909  ? 138 GLU B CA  1 
ATOM   1060 C C   . GLU A 1 138 ? 25.98248 21.28698  -8.59513  1.000 45.28033  ? 138 GLU B C   1 
ATOM   1061 O O   . GLU A 1 138 ? 25.91436 20.07255  -8.36557  1.000 43.78966  ? 138 GLU B O   1 
ATOM   1062 C CB  . GLU A 1 138 ? 25.03233 22.76518  -6.83566  1.000 45.87899  ? 138 GLU B CB  1 
ATOM   1063 C CG  . GLU A 1 138 ? 25.15236 23.30693  -5.42447  1.000 48.12299  ? 138 GLU B CG  1 
ATOM   1064 C CD  . GLU A 1 138 ? 25.55075 22.25443  -4.39893  1.000 46.71671  ? 138 GLU B CD  1 
ATOM   1065 O OE1 . GLU A 1 138 ? 24.89762 21.18734  -4.27542  1.000 43.92340  ? 138 GLU B OE1 1 
ATOM   1066 O OE2 . GLU A 1 138 ? 26.53376 22.51567  -3.69260  1.000 47.11704  ? 138 GLU B OE2 1 
ATOM   1067 N N   . ASN A 1 139 ? 25.73686 21.79095  -9.80044  1.000 41.35693  ? 139 ASN B N   1 
ATOM   1068 C CA  . ASN A 1 139 ? 25.27957 20.90537  -10.86221 1.000 46.88890  ? 139 ASN B CA  1 
ATOM   1069 C C   . ASN A 1 139 ? 26.41840 20.16750  -11.52964 1.000 47.66273  ? 139 ASN B C   1 
ATOM   1070 O O   . ASN A 1 139 ? 26.16933 19.42481  -12.48393 1.000 49.19615  ? 139 ASN B O   1 
ATOM   1071 C CB  . ASN A 1 139 ? 24.48492 21.67881  -11.92758 1.000 52.76343  ? 139 ASN B CB  1 
ATOM   1072 C CG  . ASN A 1 139 ? 25.35609 22.58642  -12.75967 1.000 49.29125  ? 139 ASN B CG  1 
ATOM   1073 O OD1 . ASN A 1 139 ? 26.43594 22.95853  -12.34139 1.000 54.44152  ? 139 ASN B OD1 1 
ATOM   1074 N ND2 . ASN A 1 139 ? 24.88028 22.96025  -13.93920 1.000 55.20961  ? 139 ASN B ND2 1 
ATOM   1075 N N   . GLU A 1 140 ? 27.65365 20.36602  -11.05493 1.000 47.55812  ? 140 GLU B N   1 
ATOM   1076 C CA  . GLU A 1 140 ? 28.83211 19.71749  -11.61671 1.000 50.18882  ? 140 GLU B CA  1 
ATOM   1077 C C   . GLU A 1 140 ? 29.61954 18.96722  -10.55775 1.000 48.66177  ? 140 GLU B C   1 
ATOM   1078 O O   . GLU A 1 140 ? 30.68207 18.42134  -10.86870 1.000 46.50956  ? 140 GLU B O   1 
ATOM   1079 C CB  . GLU A 1 140 ? 29.75338 20.73100  -12.32048 1.000 47.07599  ? 140 GLU B CB  1 
ATOM   1080 C CG  . GLU A 1 140 ? 29.14049 21.29891  -13.59447 1.000 53.65399  ? 140 GLU B CG  1 
ATOM   1081 C CD  . GLU A 1 140 ? 30.10999 22.11020  -14.43618 1.000 64.62395  ? 140 GLU B CD  1 
ATOM   1082 O OE1 . GLU A 1 140 ? 29.63314 22.76053  -15.39378 1.000 65.83673  ? 140 GLU B OE1 1 
ATOM   1083 O OE2 . GLU A 1 140 ? 31.33148 22.08828  -14.16066 1.000 57.52675  ? 140 GLU B OE2 1 
ATOM   1084 N N   . LEU A 1 141 ? 29.12972 18.93041  -9.32157  1.000 47.36433  ? 141 LEU B N   1 
ATOM   1085 C CA  . LEU A 1 141 ? 29.71036 18.05281  -8.31813  1.000 49.75312  ? 141 LEU B CA  1 
ATOM   1086 C C   . LEU A 1 141 ? 29.82362 16.62022  -8.84333  1.000 51.15266  ? 141 LEU B C   1 
ATOM   1087 O O   . LEU A 1 141 ? 29.01802 16.16237  -9.66548  1.000 46.53361  ? 141 LEU B O   1 
ATOM   1088 C CB  . LEU A 1 141 ? 28.86150 18.09086  -7.04662  1.000 50.48659  ? 141 LEU B CB  1 
ATOM   1089 C CG  . LEU A 1 141 ? 28.76261 19.49172  -6.45778  1.000 47.41385  ? 141 LEU B CG  1 
ATOM   1090 C CD1 . LEU A 1 141 ? 27.76479 19.51459  -5.31652  1.000 44.24605  ? 141 LEU B CD1 1 
ATOM   1091 C CD2 . LEU A 1 141 ? 30.15469 19.91546  -5.98048  1.000 50.14969  ? 141 LEU B CD2 1 
ATOM   1092 N N   . ASP A 1 142 ? 30.84817 15.91555  -8.36000  1.000 47.74265  ? 142 ASP B N   1 
ATOM   1093 C CA  . ASP A 1 142 ? 31.12050 14.52901  -8.72146  1.000 48.80666  ? 142 ASP B CA  1 
ATOM   1094 C C   . ASP A 1 142 ? 32.13907 13.95943  -7.74247  1.000 51.38865  ? 142 ASP B C   1 
ATOM   1095 O O   . ASP A 1 142 ? 33.35095 14.12790  -7.93870  1.000 48.08952  ? 142 ASP B O   1 
ATOM   1096 C CB  . ASP A 1 142 ? 31.66468 14.40650  -10.15288 1.000 53.10441  ? 142 ASP B CB  1 
ATOM   1097 C CG  . ASP A 1 142 ? 31.74027 12.94838  -10.63089 1.000 60.85445  ? 142 ASP B CG  1 
ATOM   1098 O OD1 . ASP A 1 142 ? 32.51005 12.14074  -10.05615 1.000 55.91470  ? 142 ASP B OD1 1 
ATOM   1099 O OD2 . ASP A 1 142 ? 30.97793 12.60164  -11.57138 1.000 66.04107  ? 142 ASP B OD2 1 
ATOM   1100 N N   . THR A 1 143 ? 31.65961 13.27546  -6.70091  1.000 46.74972  ? 143 THR B N   1 
ATOM   1101 C CA  . THR A 1 143 ? 32.49378 12.80356  -5.60411  1.000 46.19009  ? 143 THR B CA  1 
ATOM   1102 C C   . THR A 1 143 ? 32.84175 11.33074  -5.72972  1.000 40.85097  ? 143 THR B C   1 
ATOM   1103 O O   . THR A 1 143 ? 33.20780 10.70148  -4.72959  1.000 40.53045  ? 143 THR B O   1 
ATOM   1104 C CB  . THR A 1 143 ? 31.78393 13.04082  -4.27159  1.000 46.96365  ? 143 THR B CB  1 
ATOM   1105 O OG1 . THR A 1 143 ? 30.53144 12.33936  -4.28636  1.000 35.46334  ? 143 THR B OG1 1 
ATOM   1106 C CG2 . THR A 1 143 ? 31.55037 14.54000  -4.02975  1.000 42.30612  ? 143 THR B CG2 1 
ATOM   1107 N N   . PHE A 1 144 ? 32.70148 10.76356  -6.92661  1.000 38.43806  ? 144 PHE B N   1 
ATOM   1108 C CA  . PHE A 1 144 ? 32.80832 9.31949   -7.07721  1.000 38.85767  ? 144 PHE B CA  1 
ATOM   1109 C C   . PHE A 1 144 ? 34.19264 8.81456   -6.66241  1.000 46.97523  ? 144 PHE B C   1 
ATOM   1110 O O   . PHE A 1 144 ? 34.31246 7.76917   -6.01349  1.000 51.18050  ? 144 PHE B O   1 
ATOM   1111 C CB  . PHE A 1 144 ? 32.49335 8.95567   -8.51980  1.000 39.90900  ? 144 PHE B CB  1 
ATOM   1112 C CG  . PHE A 1 144 ? 32.59499 7.49766   -8.81534  1.000 43.51427  ? 144 PHE B CG  1 
ATOM   1113 C CD1 . PHE A 1 144 ? 31.69621 6.60020   -8.27382  1.000 42.65654  ? 144 PHE B CD1 1 
ATOM   1114 C CD2 . PHE A 1 144 ? 33.62209 7.01476   -9.62028  1.000 49.51623  ? 144 PHE B CD2 1 
ATOM   1115 C CE1 . PHE A 1 144 ? 31.77565 5.23880   -8.56470  1.000 45.50041  ? 144 PHE B CE1 1 
ATOM   1116 C CE2 . PHE A 1 144 ? 33.73121 5.65624   -9.89894  1.000 48.80628  ? 144 PHE B CE2 1 
ATOM   1117 C CZ  . PHE A 1 144 ? 32.79331 4.76665   -9.37316  1.000 49.10161  ? 144 PHE B CZ  1 
ATOM   1118 N N   . LYS A 1 145 ? 35.24996 9.55104   -7.00384  1.000 41.64814  ? 145 LYS B N   1 
ATOM   1119 C CA  . LYS A 1 145 ? 36.59201 9.13879   -6.61474  1.000 45.44350  ? 145 LYS B CA  1 
ATOM   1120 C C   . LYS A 1 145 ? 36.92858 9.52248   -5.18267  1.000 45.34352  ? 145 LYS B C   1 
ATOM   1121 O O   . LYS A 1 145 ? 37.95451 9.07552   -4.66822  1.000 48.93506  ? 145 LYS B O   1 
ATOM   1122 C CB  . LYS A 1 145 ? 37.64522 9.74308   -7.56069  1.000 45.25755  ? 145 LYS B CB  1 
ATOM   1123 C CG  . LYS A 1 145 ? 37.29054 9.66207   -9.05091  1.000 55.27938  ? 145 LYS B CG  1 
ATOM   1124 C CD  . LYS A 1 145 ? 36.38248 10.84883  -9.49764  1.000 63.85424  ? 145 LYS B CD  1 
ATOM   1125 C CE  . LYS A 1 145 ? 36.14179 10.86294  -11.01355 1.000 65.67123  ? 145 LYS B CE  1 
ATOM   1126 N NZ  . LYS A 1 145 ? 35.43150 9.62469   -11.48884 1.000 58.49707  ? 145 LYS B NZ  1 
ATOM   1127 N N   . LEU A 1 146 ? 36.12391 10.36228  -4.53678  1.000 41.90828  ? 146 LEU B N   1 
ATOM   1128 C CA  . LEU A 1 146 ? 36.41453 10.76179  -3.16987  1.000 40.91299  ? 146 LEU B CA  1 
ATOM   1129 C C   . LEU A 1 146 ? 35.68016 9.92877   -2.14220  1.000 39.02736  ? 146 LEU B C   1 
ATOM   1130 O O   . LEU A 1 146 ? 35.98037 10.04328  -0.95686  1.000 41.34621  ? 146 LEU B O   1 
ATOM   1131 C CB  . LEU A 1 146 ? 36.06529 12.22830  -2.94119  1.000 35.23136  ? 146 LEU B CB  1 
ATOM   1132 C CG  . LEU A 1 146 ? 36.82393 13.26852  -3.76082  1.000 38.46766  ? 146 LEU B CG  1 
ATOM   1133 C CD1 . LEU A 1 146 ? 36.08462 14.58164  -3.67845  1.000 40.99174  ? 146 LEU B CD1 1 
ATOM   1134 C CD2 . LEU A 1 146 ? 38.25692 13.40237  -3.24948  1.000 39.77215  ? 146 LEU B CD2 1 
ATOM   1135 N N   . GLU A 1 147 ? 34.73243 9.13113   -2.55062  1.000 42.32602  ? 147 GLU B N   1 
ATOM   1136 C CA  . GLU A 1 147 ? 33.93204 8.45663   -1.54958  1.000 43.64655  ? 147 GLU B CA  1 
ATOM   1137 C C   . GLU A 1 147 ? 34.70296 7.25828   -1.00127  1.000 45.59725  ? 147 GLU B C   1 
ATOM   1138 O O   . GLU A 1 147 ? 35.47704 6.63000   -1.72449  1.000 40.69490  ? 147 GLU B O   1 
ATOM   1139 C CB  . GLU A 1 147 ? 32.60130 8.01140   -2.14930  1.000 42.83934  ? 147 GLU B CB  1 
ATOM   1140 C CG  . GLU A 1 147 ? 31.48345 9.07288   -2.04442  1.000 44.01257  ? 147 GLU B CG  1 
ATOM   1141 C CD  . GLU A 1 147 ? 30.41306 8.91835   -3.12301  1.000 42.60330  ? 147 GLU B CD  1 
ATOM   1142 O OE1 . GLU A 1 147 ? 29.90390 7.79411   -3.29408  1.000 38.54677  ? 147 GLU B OE1 1 
ATOM   1143 O OE2 . GLU A 1 147 ? 30.10898 9.91757   -3.81907  1.000 39.19215  ? 147 GLU B OE2 1 
ATOM   1144 N N   . PRO A 1 148 ? 34.50837 6.92435   0.27737   1.000 48.09857  ? 148 PRO B N   1 
ATOM   1145 C CA  . PRO A 1 148 ? 35.32166 5.85220   0.89131   1.000 45.88178  ? 148 PRO B CA  1 
ATOM   1146 C C   . PRO A 1 148 ? 34.97284 4.46720   0.39393   1.000 46.46853  ? 148 PRO B C   1 
ATOM   1147 O O   . PRO A 1 148 ? 35.79465 3.55465   0.53014   1.000 46.85338  ? 148 PRO B O   1 
ATOM   1148 C CB  . PRO A 1 148 ? 35.00738 5.98641   2.38854   1.000 47.03704  ? 148 PRO B CB  1 
ATOM   1149 C CG  . PRO A 1 148 ? 33.58260 6.55599   2.40424   1.000 38.57915  ? 148 PRO B CG  1 
ATOM   1150 C CD  . PRO A 1 148 ? 33.54113 7.50769   1.22328   1.000 35.56435  ? 148 PRO B CD  1 
ATOM   1151 N N   . CYS A 1 149 ? 33.76009 4.25615   -0.10782  1.000 45.99282  ? 149 CYS B N   1 
ATOM   1152 C CA  . CYS A 1 149 ? 33.44519 3.04294   -0.83895  1.000 43.85477  ? 149 CYS B CA  1 
ATOM   1153 C C   . CYS A 1 149 ? 32.58682 3.45853   -2.01107  1.000 43.42043  ? 149 CYS B C   1 
ATOM   1154 O O   . CYS A 1 149 ? 32.07439 4.57540   -2.05202  1.000 44.15894  ? 149 CYS B O   1 
ATOM   1155 C CB  . CYS A 1 149 ? 32.73652 1.98521   0.02385   1.000 42.41113  ? 149 CYS B CB  1 
ATOM   1156 S SG  . CYS A 1 149 ? 31.15125 2.48949   0.74956   1.000 47.57413  ? 149 CYS B SG  1 
ATOM   1157 N N   . LYS A 1 150 ? 32.47053 2.57591   -2.99019  1.000 45.02344  ? 150 LYS B N   1 
ATOM   1158 C CA  . LYS A 1 150 ? 31.59612 2.87115   -4.10792  1.000 42.47702  ? 150 LYS B CA  1 
ATOM   1159 C C   . LYS A 1 150 ? 30.15432 2.81641   -3.62097  1.000 42.96561  ? 150 LYS B C   1 
ATOM   1160 O O   . LYS A 1 150 ? 29.83936 2.11734   -2.65558  1.000 44.42901  ? 150 LYS B O   1 
ATOM   1161 C CB  . LYS A 1 150 ? 31.85453 1.88162   -5.23782  1.000 46.90003  ? 150 LYS B CB  1 
ATOM   1162 C CG  . LYS A 1 150 ? 32.83241 2.37645   -6.29723  1.000 45.91280  ? 150 LYS B CG  1 
ATOM   1163 C CD  . LYS A 1 150 ? 33.85091 3.35822   -5.74401  1.000 52.41822  ? 150 LYS B CD  1 
ATOM   1164 C CE  . LYS A 1 150 ? 35.02582 3.56352   -6.71051  1.000 51.23712  ? 150 LYS B CE  1 
ATOM   1165 N NZ  . LYS A 1 150 ? 36.00551 4.50919   -6.11893  1.000 53.39331  ? 150 LYS B NZ  1 
ATOM   1166 N N   . PHE A 1 151 ? 29.27241 3.59295   -4.26234  1.000 46.50375  ? 151 PHE B N   1 
ATOM   1167 C CA  . PHE A 1 151 ? 27.91720 3.72296   -3.72168  1.000 40.95396  ? 151 PHE B CA  1 
ATOM   1168 C C   . PHE A 1 151 ? 27.21978 2.37738   -3.65337  1.000 41.07693  ? 151 PHE B C   1 
ATOM   1169 O O   . PHE A 1 151 ? 26.54787 2.07387   -2.66525  1.000 43.38776  ? 151 PHE B O   1 
ATOM   1170 C CB  . PHE A 1 151 ? 27.08736 4.72874   -4.51796  1.000 40.22328  ? 151 PHE B CB  1 
ATOM   1171 C CG  . PHE A 1 151 ? 26.82367 4.35543   -5.95968  1.000 38.47275  ? 151 PHE B CG  1 
ATOM   1172 C CD1 . PHE A 1 151 ? 25.75220 3.54921   -6.30624  1.000 42.54436  ? 151 PHE B CD1 1 
ATOM   1173 C CD2 . PHE A 1 151 ? 27.58172 4.91122   -6.98229  1.000 39.15373  ? 151 PHE B CD2 1 
ATOM   1174 C CE1 . PHE A 1 151 ? 25.47418 3.25812   -7.66019  1.000 43.33474  ? 151 PHE B CE1 1 
ATOM   1175 C CE2 . PHE A 1 151 ? 27.31715 4.62762   -8.32901  1.000 38.54280  ? 151 PHE B CE2 1 
ATOM   1176 C CZ  . PHE A 1 151 ? 26.25967 3.80026   -8.67074  1.000 37.86371  ? 151 PHE B CZ  1 
ATOM   1177 N N   . TRP A 1 152 ? 27.42197 1.53032   -4.66041  1.000 43.37477  ? 152 TRP B N   1 
ATOM   1178 C CA  . TRP A 1 152 ? 26.82806 0.20127   -4.65590  1.000 44.96332  ? 152 TRP B CA  1 
ATOM   1179 C C   . TRP A 1 152 ? 27.44344 -0.73148  -3.61321  1.000 44.30147  ? 152 TRP B C   1 
ATOM   1180 O O   . TRP A 1 152 ? 26.93219 -1.84751  -3.43604  1.000 46.45001  ? 152 TRP B O   1 
ATOM   1181 C CB  . TRP A 1 152 ? 26.94273 -0.42491  -6.04143  1.000 41.53710  ? 152 TRP B CB  1 
ATOM   1182 C CG  . TRP A 1 152 ? 28.35329 -0.68602  -6.48474  1.000 44.35373  ? 152 TRP B CG  1 
ATOM   1183 C CD1 . TRP A 1 152 ? 29.14392 -1.75007  -6.13234  1.000 43.57194  ? 152 TRP B CD1 1 
ATOM   1184 C CD2 . TRP A 1 152 ? 29.12944 0.10774   -7.38730  1.000 40.44642  ? 152 TRP B CD2 1 
ATOM   1185 N NE1 . TRP A 1 152 ? 30.35067 -1.66074  -6.75862  1.000 49.07978  ? 152 TRP B NE1 1 
ATOM   1186 C CE2 . TRP A 1 152 ? 30.37476 -0.53129  -7.53456  1.000 44.87931  ? 152 TRP B CE2 1 
ATOM   1187 C CE3 . TRP A 1 152 ? 28.89723 1.30865   -8.07066  1.000 43.83498  ? 152 TRP B CE3 1 
ATOM   1188 C CZ2 . TRP A 1 152 ? 31.38930 -0.01820  -8.34463  1.000 46.12006  ? 152 TRP B CZ2 1 
ATOM   1189 C CZ3 . TRP A 1 152 ? 29.89545 1.82335   -8.87542  1.000 42.30502  ? 152 TRP B CZ3 1 
ATOM   1190 C CH2 . TRP A 1 152 ? 31.13155 1.15468   -9.01184  1.000 50.38599  ? 152 TRP B CH2 1 
ATOM   1191 N N   . ASN A 1 153 ? 28.49930 -0.31320  -2.91684  1.000 39.49418  ? 153 ASN B N   1 
ATOM   1192 C CA  . ASN A 1 153 ? 29.04696 -1.08421  -1.80465  1.000 42.93945  ? 153 ASN B CA  1 
ATOM   1193 C C   . ASN A 1 153 ? 28.60811 -0.57050  -0.43462  1.000 45.40381  ? 153 ASN B C   1 
ATOM   1194 O O   . ASN A 1 153 ? 29.14372 -1.02045  0.58437   1.000 49.30812  ? 153 ASN B O   1 
ATOM   1195 C CB  . ASN A 1 153 ? 30.56948 -1.11533  -1.87950  1.000 42.49817  ? 153 ASN B CB  1 
ATOM   1196 C CG  . ASN A 1 153 ? 31.06783 -2.15966  -2.84904  1.000 49.80024  ? 153 ASN B CG  1 
ATOM   1197 O OD1 . ASN A 1 153 ? 30.30624 -3.03134  -3.24878  1.000 48.33192  ? 153 ASN B OD1 1 
ATOM   1198 N ND2 . ASN A 1 153 ? 32.34346 -2.07389  -3.24330  1.000 49.84999  ? 153 ASN B ND2 1 
ATOM   1199 N N   . GLN A 1 154 ? 27.66671 0.36232   -0.37667  1.000 42.21716  ? 154 GLN B N   1 
ATOM   1200 C CA  . GLN A 1 154 ? 27.07778 0.73072   0.90076   1.000 43.55277  ? 154 GLN B CA  1 
ATOM   1201 C C   . GLN A 1 154 ? 26.13083 -0.37851  1.34965   1.000 44.59842  ? 154 GLN B C   1 
ATOM   1202 O O   . GLN A 1 154 ? 25.47277 -1.01868  0.52681   1.000 42.56972  ? 154 GLN B O   1 
ATOM   1203 C CB  . GLN A 1 154 ? 26.34619 2.06820   0.79230   1.000 42.05391  ? 154 GLN B CB  1 
ATOM   1204 C CG  . GLN A 1 154 ? 27.24241 3.27428   0.45150   1.000 40.73697  ? 154 GLN B CG  1 
ATOM   1205 C CD  . GLN A 1 154 ? 26.42208 4.52599   0.17421   1.000 39.89458  ? 154 GLN B CD  1 
ATOM   1206 O OE1 . GLN A 1 154 ? 25.28082 4.62024   0.59132   1.000 39.95683  ? 154 GLN B OE1 1 
ATOM   1207 N NE2 . GLN A 1 154 ? 26.98735 5.46642   -0.56090  1.000 38.58067  ? 154 GLN B NE2 1 
ATOM   1208 N N   . ARG A 1 155 ? 26.09417 -0.62497  2.66053   1.000 41.42048  ? 155 ARG B N   1 
ATOM   1209 C CA  . ARG A 1 155 ? 25.37983 -1.75333  3.23220   1.000 40.78022  ? 155 ARG B CA  1 
ATOM   1210 C C   . ARG A 1 155 ? 24.68839 -1.30423  4.50893   1.000 42.51976  ? 155 ARG B C   1 
ATOM   1211 O O   . ARG A 1 155 ? 25.22042 -0.47949  5.25435   1.000 44.90957  ? 155 ARG B O   1 
ATOM   1212 C CB  . ARG A 1 155 ? 26.32486 -2.93692  3.53940   1.000 40.93271  ? 155 ARG B CB  1 
ATOM   1213 C CG  . ARG A 1 155 ? 26.85243 -3.67229  2.29983   1.000 44.02381  ? 155 ARG B CG  1 
ATOM   1214 C CD  . ARG A 1 155 ? 25.73443 -4.36632  1.56384   1.000 41.15616  ? 155 ARG B CD  1 
ATOM   1215 N NE  . ARG A 1 155 ? 26.17874 -5.08544  0.37823   1.000 42.74113  ? 155 ARG B NE  1 
ATOM   1216 C CZ  . ARG A 1 155 ? 26.46992 -4.53150  -0.79177  1.000 42.83189  ? 155 ARG B CZ  1 
ATOM   1217 N NH1 . ARG A 1 155 ? 26.48004 -3.22039  -0.95724  1.000 41.68705  ? 155 ARG B NH1 1 
ATOM   1218 N NH2 . ARG A 1 155 ? 26.78516 -5.31583  -1.81925  1.000 49.20174  ? 155 ARG B NH2 1 
ATOM   1219 N N   . ASP A 1 156 ? 23.51348 -1.87561  4.77370   1.000 41.19902  ? 156 ASP B N   1 
ATOM   1220 C CA  . ASP A 1 156 ? 22.65771 -1.44004  5.87215   1.000 43.30403  ? 156 ASP B CA  1 
ATOM   1221 C C   . ASP A 1 156 ? 22.67127 -2.46999  6.98954   1.000 48.04468  ? 156 ASP B C   1 
ATOM   1222 O O   . ASP A 1 156 ? 22.39285 -3.65269  6.76093   1.000 49.17063  ? 156 ASP B O   1 
ATOM   1223 C CB  . ASP A 1 156 ? 21.21947 -1.20979  5.40397   1.000 40.73898  ? 156 ASP B CB  1 
ATOM   1224 C CG  . ASP A 1 156 ? 20.30835 -0.80657  6.54008   1.000 41.82143  ? 156 ASP B CG  1 
ATOM   1225 O OD1 . ASP A 1 156 ? 20.50817 0.29710   7.10576   1.000 39.40516  ? 156 ASP B OD1 1 
ATOM   1226 O OD2 . ASP A 1 156 ? 19.39160 -1.59184  6.85997   1.000 45.38795  ? 156 ASP B OD2 1 
ATOM   1227 N N   . ILE A 1 157 ? 22.96345 -2.00661  8.20170   1.000 45.13098  ? 157 ILE B N   1 
ATOM   1228 C CA  . ILE A 1 157 ? 23.12978 -2.91388  9.33084   1.000 43.80810  ? 157 ILE B CA  1 
ATOM   1229 C C   . ILE A 1 157 ? 21.79683 -3.54541  9.73824   1.000 46.28931  ? 157 ILE B C   1 
ATOM   1230 O O   . ILE A 1 157 ? 21.73509 -4.73994  10.04413  1.000 47.05380  ? 157 ILE B O   1 
ATOM   1231 C CB  . ILE A 1 157 ? 23.78995 -2.15285  10.49092  1.000 43.37011  ? 157 ILE B CB  1 
ATOM   1232 C CG1 . ILE A 1 157 ? 25.23144 -1.76958  10.09318  1.000 40.90427  ? 157 ILE B CG1 1 
ATOM   1233 C CG2 . ILE A 1 157 ? 23.70066 -2.98243  11.75838  1.000 43.42957  ? 157 ILE B CG2 1 
ATOM   1234 C CD1 . ILE A 1 157 ? 25.95677 -0.93024  11.10086  1.000 39.20683  ? 157 ILE B CD1 1 
ATOM   1235 N N   . ARG A 1 158 ? 20.71028 -2.76513  9.74580   1.000 42.67982  ? 158 ARG B N   1 
ATOM   1236 C CA  . ARG A 1 158 ? 19.40972 -3.32837  10.10510  1.000 46.58807  ? 158 ARG B CA  1 
ATOM   1237 C C   . ARG A 1 158 ? 19.01012 -4.44915  9.15857   1.000 45.80159  ? 158 ARG B C   1 
ATOM   1238 O O   . ARG A 1 158 ? 18.51865 -5.49514  9.59374   1.000 46.61681  ? 158 ARG B O   1 
ATOM   1239 C CB  . ARG A 1 158 ? 18.33600 -2.24186  10.09324  1.000 44.53001  ? 158 ARG B CB  1 
ATOM   1240 C CG  . ARG A 1 158 ? 18.39983 -1.30690  11.24506  1.000 38.49767  ? 158 ARG B CG  1 
ATOM   1241 C CD  . ARG A 1 158 ? 17.16942 -0.51500  11.28165  1.000 39.01712  ? 158 ARG B CD  1 
ATOM   1242 N NE  . ARG A 1 158 ? 17.28383 0.61806   12.18645  1.000 42.53187  ? 158 ARG B NE  1 
ATOM   1243 C CZ  . ARG A 1 158 ? 17.40710 1.87635   11.79803  1.000 40.02927  ? 158 ARG B CZ  1 
ATOM   1244 N NH1 . ARG A 1 158 ? 17.47410 2.19713   10.51702  1.000 38.64003  ? 158 ARG B NH1 1 
ATOM   1245 N NH2 . ARG A 1 158 ? 17.42290 2.83565   12.71729  1.000 39.76879  ? 158 ARG B NH2 1 
ATOM   1246 N N   . THR A 1 159 ? 19.19687 -4.23749  7.85556   1.000 49.41331  ? 159 THR B N   1 
ATOM   1247 C CA  . THR A 1 159 ? 18.83393 -5.25467  6.87600   1.000 48.23560  ? 159 THR B CA  1 
ATOM   1248 C C   . THR A 1 159 ? 19.70329 -6.49816  7.04167   1.000 48.75695  ? 159 THR B C   1 
ATOM   1249 O O   . THR A 1 159 ? 19.19741 -7.62739  6.98069   1.000 45.44942  ? 159 THR B O   1 
ATOM   1250 C CB  . THR A 1 159 ? 18.95266 -4.67736  5.45976   1.000 42.35840  ? 159 THR B CB  1 
ATOM   1251 O OG1 . THR A 1 159 ? 18.32357 -3.38337  5.40762   1.000 41.51827  ? 159 THR B OG1 1 
ATOM   1252 C CG2 . THR A 1 159 ? 18.28668 -5.59337  4.44629   1.000 41.75880  ? 159 THR B CG2 1 
ATOM   1253 N N   . ARG A 1 160 ? 21.00328 -6.30384  7.29881   1.000 45.43128  ? 160 ARG B N   1 
ATOM   1254 C CA  . ARG A 1 160 ? 21.93758 -7.42373  7.43052   1.000 48.92613  ? 160 ARG B CA  1 
ATOM   1255 C C   . ARG A 1 160 ? 21.56029 -8.33494  8.59298   1.000 51.07405  ? 160 ARG B C   1 
ATOM   1256 O O   . ARG A 1 160 ? 21.23153 -9.51044  8.40111   1.000 52.95863  ? 160 ARG B O   1 
ATOM   1257 C CB  . ARG A 1 160 ? 23.35463 -6.88750  7.61971   1.000 52.75205  ? 160 ARG B CB  1 
ATOM   1258 C CG  . ARG A 1 160 ? 24.42848 -7.93532  7.84437   1.000 51.62951  ? 160 ARG B CG  1 
ATOM   1259 C CD  . ARG A 1 160 ? 24.85110 -8.57645  6.54168   1.000 52.19633  ? 160 ARG B CD  1 
ATOM   1260 N NE  . ARG A 1 160 ? 26.10876 -9.29334  6.69498   1.000 54.20908  ? 160 ARG B NE  1 
ATOM   1261 C CZ  . ARG A 1 160 ? 26.60877 -10.12907 5.79767   1.000 55.59939  ? 160 ARG B CZ  1 
ATOM   1262 N NH1 . ARG A 1 160 ? 26.00295 -10.33668 4.63554   1.000 57.83795  ? 160 ARG B NH1 1 
ATOM   1263 N NH2 . ARG A 1 160 ? 27.73998 -10.77842 6.07543   1.000 48.70902  ? 160 ARG B NH2 1 
ATOM   1264 N N   . ILE A 1 161 ? 21.59085 -7.79376  9.81005   1.000 50.11067  ? 161 ILE B N   1 
ATOM   1265 C CA  . ILE A 1 161 ? 21.32432 -8.59058  11.00490  1.000 55.22571  ? 161 ILE B CA  1 
ATOM   1266 C C   . ILE A 1 161 ? 19.97615 -9.29925  10.90948  1.000 54.05426  ? 161 ILE B C   1 
ATOM   1267 O O   . ILE A 1 161 ? 19.86428 -10.48392 11.24761  1.000 55.20788  ? 161 ILE B O   1 
ATOM   1268 C CB  . ILE A 1 161 ? 21.42132 -7.70247  12.25937  1.000 53.05435  ? 161 ILE B CB  1 
ATOM   1269 C CG1 . ILE A 1 161 ? 22.89452 -7.40201  12.55064  1.000 47.33875  ? 161 ILE B CG1 1 
ATOM   1270 C CG2 . ILE A 1 161 ? 20.70756 -8.36335  13.45040  1.000 53.04859  ? 161 ILE B CG2 1 
ATOM   1271 C CD1 . ILE A 1 161 ? 23.12831 -6.36265  13.59885  1.000 49.26701  ? 161 ILE B CD1 1 
ATOM   1272 N N   . GLU A 1 162 ? 18.93851 -8.59680  10.43714  1.000 50.67529  ? 162 GLU B N   1 
ATOM   1273 C CA  . GLU A 1 162 ? 17.62715 -9.22420  10.25924  1.000 51.90533  ? 162 GLU B CA  1 
ATOM   1274 C C   . GLU A 1 162 ? 17.65963 -10.32677 9.20817   1.000 53.32995  ? 162 GLU B C   1 
ATOM   1275 O O   . GLU A 1 162 ? 16.92762 -11.31774 9.32062   1.000 55.38851  ? 162 GLU B O   1 
ATOM   1276 C CB  . GLU A 1 162 ? 16.57971 -8.16872  9.88426   1.000 49.11887  ? 162 GLU B CB  1 
ATOM   1277 C CG  . GLU A 1 162 ? 15.20725 -8.72479  9.49863   1.000 47.91306  ? 162 GLU B CG  1 
ATOM   1278 C CD  . GLU A 1 162 ? 14.26704 -7.66520  8.92715   1.000 51.62901  ? 162 GLU B CD  1 
ATOM   1279 O OE1 . GLU A 1 162 ? 14.40496 -7.30179  7.73755   1.000 52.05631  ? 162 GLU B OE1 1 
ATOM   1280 O OE2 . GLU A 1 162 ? 13.38142 -7.18980  9.67000   1.000 50.23414  ? 162 GLU B OE2 1 
ATOM   1281 N N   . ALA A 1 163 ? 18.49594 -10.18016 8.18425   1.000 54.37069  ? 163 ALA B N   1 
ATOM   1282 C CA  . ALA A 1 163 ? 18.57172 -11.21525 7.15899   1.000 58.64083  ? 163 ALA B CA  1 
ATOM   1283 C C   . ALA A 1 163 ? 19.29529 -12.45252 7.67763   1.000 56.93670  ? 163 ALA B C   1 
ATOM   1284 O O   . ALA A 1 163 ? 18.84543 -13.58317 7.45977   1.000 58.29814  ? 163 ALA B O   1 
ATOM   1285 C CB  . ALA A 1 163 ? 19.27277 -10.67332 5.91650   1.000 53.52050  ? 163 ALA B CB  1 
ATOM   1286 N N   . LEU A 1 164 ? 20.40209 -12.25068 8.38868   1.000 55.13443  ? 164 LEU B N   1 
ATOM   1287 C CA  . LEU A 1 164 ? 21.21836 -13.36978 8.84733   1.000 58.38435  ? 164 LEU B CA  1 
ATOM   1288 C C   . LEU A 1 164 ? 20.47865 -14.22577 9.87050   1.000 60.88016  ? 164 LEU B C   1 
ATOM   1289 O O   . LEU A 1 164 ? 20.62929 -15.45439 9.87516   1.000 62.29665  ? 164 LEU B O   1 
ATOM   1290 C CB  . LEU A 1 164 ? 22.52762 -12.83946 9.42673   1.000 53.59341  ? 164 LEU B CB  1 
ATOM   1291 C CG  . LEU A 1 164 ? 23.40720 -12.25143 8.31979   1.000 55.08617  ? 164 LEU B CG  1 
ATOM   1292 C CD1 . LEU A 1 164 ? 24.62592 -11.51155 8.88863   1.000 55.98002  ? 164 LEU B CD1 1 
ATOM   1293 C CD2 . LEU A 1 164 ? 23.83986 -13.34608 7.33949   1.000 55.20916  ? 164 LEU B CD2 1 
ATOM   1294 N N   . LEU A 1 165 ? 19.66337 -13.60109 10.73519  1.000 56.00352  ? 165 LEU B N   1 
ATOM   1295 C CA  . LEU A 1 165 ? 18.95551 -14.32857 11.78307  1.000 57.33695  ? 165 LEU B CA  1 
ATOM   1296 C C   . LEU A 1 165 ? 17.58212 -14.84357 11.34840  1.000 61.01786  ? 165 LEU B C   1 
ATOM   1297 O O   . LEU A 1 165 ? 17.04037 -15.74812 11.99799  1.000 61.03811  ? 165 LEU B O   1 
ATOM   1298 C CB  . LEU A 1 165 ? 18.79626 -13.44083 13.01998  1.000 54.46242  ? 165 LEU B CB  1 
ATOM   1299 C CG  . LEU A 1 165 ? 20.05777 -12.81161 13.58954  1.000 57.15796  ? 165 LEU B CG  1 
ATOM   1300 C CD1 . LEU A 1 165 ? 19.73535 -12.05165 14.86432  1.000 56.78011  ? 165 LEU B CD1 1 
ATOM   1301 C CD2 . LEU A 1 165 ? 21.11374 -13.88193 13.84641  1.000 63.13483  ? 165 LEU B CD2 1 
ATOM   1302 N N   . LEU A 1 166 ? 17.00587 -14.27717 10.28557  1.000 60.11797  ? 166 LEU B N   1 
ATOM   1303 C CA  . LEU A 1 166 ? 15.72243 -14.70986 9.72721   1.000 54.81105  ? 166 LEU B CA  1 
ATOM   1304 C C   . LEU A 1 166 ? 14.55770 -14.45934 10.68699  1.000 58.31560  ? 166 LEU B C   1 
ATOM   1305 O O   . LEU A 1 166 ? 13.63454 -15.26599 10.78014  1.000 61.27473  ? 166 LEU B O   1 
ATOM   1306 C CB  . LEU A 1 166 ? 15.77015 -16.17460 9.29692   1.000 53.19224  ? 166 LEU B CB  1 
ATOM   1307 C CG  . LEU A 1 166 ? 16.73230 -16.41203 8.13256   1.000 55.08814  ? 166 LEU B CG  1 
ATOM   1308 C CD1 . LEU A 1 166 ? 16.78681 -17.87797 7.77488   1.000 54.72578  ? 166 LEU B CD1 1 
ATOM   1309 C CD2 . LEU A 1 166 ? 16.35352 -15.56822 6.91145   1.000 54.76728  ? 166 LEU B CD2 1 
ATOM   1310 N N   . VAL A 1 167 ? 14.57860 -13.32009 11.37747  1.000 59.06943  ? 167 VAL B N   1 
ATOM   1311 C CA  . VAL A 1 167 ? 13.47376 -12.88058 12.23133  1.000 54.89799  ? 167 VAL B CA  1 
ATOM   1312 C C   . VAL A 1 167 ? 13.10331 -11.45271 11.84017  1.000 54.84192  ? 167 VAL B C   1 
ATOM   1313 O O   . VAL A 1 167 ? 13.88686 -10.51960 12.06915  1.000 56.19741  ? 167 VAL B O   1 
ATOM   1314 C CB  . VAL A 1 167 ? 13.82874 -12.94486 13.72424  1.000 59.04164  ? 167 VAL B CB  1 
ATOM   1315 C CG1 . VAL A 1 167 ? 12.62185 -12.55490 14.57479  1.000 51.14429  ? 167 VAL B CG1 1 
ATOM   1316 C CG2 . VAL A 1 167 ? 14.35422 -14.32796 14.09898  1.000 60.09260  ? 167 VAL B CG2 1 
ATOM   1317 N N   . ARG A 1 168 ? 11.90114 -11.27624 11.29493  1.000 53.23070  ? 168 ARG B N   1 
ATOM   1318 C CA  . ARG A 1 168 ? 11.41163 -9.95191  10.93643  1.000 53.47360  ? 168 ARG B CA  1 
ATOM   1319 C C   . ARG A 1 168 ? 11.49654 -8.98884  12.11280  1.000 56.20296  ? 168 ARG B C   1 
ATOM   1320 O O   . ARG A 1 168 ? 11.03340 -9.29265  13.21702  1.000 56.53235  ? 168 ARG B O   1 
ATOM   1321 C CB  . ARG A 1 168 ? 9.97067  -10.04073 10.44768  1.000 49.77526  ? 168 ARG B CB  1 
ATOM   1322 C CG  . ARG A 1 168 ? 9.32121  -8.68701  10.28584  1.000 54.77186  ? 168 ARG B CG  1 
ATOM   1323 C CD  . ARG A 1 168 ? 8.69928  -8.52942  8.90381   1.000 56.74004  ? 168 ARG B CD  1 
ATOM   1324 N NE  . ARG A 1 168 ? 7.89590  -7.31578  8.77969   1.000 51.81966  ? 168 ARG B NE  1 
ATOM   1325 C CZ  . ARG A 1 168 ? 7.58952  -6.75343  7.61847   1.000 51.71746  ? 168 ARG B CZ  1 
ATOM   1326 N NH1 . ARG A 1 168 ? 7.98578  -7.28807  6.47432   1.000 51.76593  ? 168 ARG B NH1 1 
ATOM   1327 N NH2 . ARG A 1 168 ? 6.87437  -5.62487  7.60566   1.000 48.32388  ? 168 ARG B NH2 1 
ATOM   1328 N N   . ASP A 1 169 ? 12.10376 -7.82531  11.85699  1.000 52.56770  ? 169 ASP B N   1 
ATOM   1329 C CA  . ASP A 1 169 ? 12.28126 -6.71850  12.79884  1.000 52.42592  ? 169 ASP B CA  1 
ATOM   1330 C C   . ASP A 1 169 ? 13.28991 -7.01367  13.90661  1.000 53.23378  ? 169 ASP B C   1 
ATOM   1331 O O   . ASP A 1 169 ? 13.29476 -6.32991  14.93239  1.000 55.87158  ? 169 ASP B O   1 
ATOM   1332 C CB  . ASP A 1 169 ? 10.94598 -6.26564  13.41679  1.000 47.46576  ? 169 ASP B CB  1 
ATOM   1333 N N   . MET A 1 170 ? 14.17499 -7.99055  13.74672  1.000 54.20474  ? 170 MET B N   1 
ATOM   1334 C CA  . MET A 1 170 ? 15.19731 -8.23971  14.76150  1.000 52.69180  ? 170 MET B CA  1 
ATOM   1335 C C   . MET A 1 170 ? 16.52660 -7.70238  14.23506  1.000 51.99514  ? 170 MET B C   1 
ATOM   1336 O O   . MET A 1 170 ? 17.18180 -8.33601  13.40510  1.000 56.18646  ? 170 MET B O   1 
ATOM   1337 C CB  . MET A 1 170 ? 15.26479 -9.71763  15.12462  1.000 55.42106  ? 170 MET B CB  1 
ATOM   1338 C CG  . MET A 1 170 ? 16.34358 -10.04951 16.14586  1.000 58.61904  ? 170 MET B CG  1 
ATOM   1339 S SD  . MET A 1 170 ? 16.63353 -11.82012 16.39263  1.000 67.55760  ? 170 MET B SD  1 
ATOM   1340 C CE  . MET A 1 170 ? 17.04600 -11.84923 18.13730  1.000 59.90844  ? 170 MET B CE  1 
ATOM   1341 N N   . THR A 1 171 ? 16.91538 -6.52642  14.72629  1.000 49.90359  ? 171 THR B N   1 
ATOM   1342 C CA  . THR A 1 171 ? 18.06969 -5.78101  14.23183  1.000 50.19864  ? 171 THR B CA  1 
ATOM   1343 C C   . THR A 1 171 ? 19.22177 -5.75571  15.23010  1.000 49.66025  ? 171 THR B C   1 
ATOM   1344 O O   . THR A 1 171 ? 20.15902 -4.96518  15.06781  1.000 47.81877  ? 171 THR B O   1 
ATOM   1345 C CB  . THR A 1 171 ? 17.66649 -4.34556  13.88673  1.000 46.08038  ? 171 THR B CB  1 
ATOM   1346 O OG1 . THR A 1 171 ? 17.35053 -3.64721  15.09540  1.000 48.95556  ? 171 THR B OG1 1 
ATOM   1347 C CG2 . THR A 1 171 ? 16.44503 -4.32756  12.98007  1.000 47.53103  ? 171 THR B CG2 1 
ATOM   1348 N N   . THR A 1 172 ? 19.15144 -6.56882  16.27696  1.000 48.11755  ? 172 THR B N   1 
ATOM   1349 C CA  . THR A 1 172 ? 20.26299 -6.78332  17.17717  1.000 52.49110  ? 172 THR B CA  1 
ATOM   1350 C C   . THR A 1 172 ? 20.49869 -8.27895  17.27655  1.000 55.58086  ? 172 THR B C   1 
ATOM   1351 O O   . THR A 1 172 ? 19.64794 -9.08913  16.90479  1.000 52.55850  ? 172 THR B O   1 
ATOM   1352 C CB  . THR A 1 172 ? 20.02806 -6.19161  18.57450  1.000 51.89078  ? 172 THR B CB  1 
ATOM   1353 O OG1 . THR A 1 172 ? 18.86358 -6.76995  19.16334  1.000 58.62309  ? 172 THR B OG1 1 
ATOM   1354 C CG2 . THR A 1 172 ? 19.85962 -4.69396  18.47653  1.000 55.61637  ? 172 THR B CG2 1 
ATOM   1355 N N   . CYS A 1 173 ? 21.68179 -8.63455  17.76439  1.000 59.88246  ? 173 CYS B N   1 
ATOM   1356 C CA  . CYS A 1 173 ? 22.09978 -10.01772 17.80835  1.000 60.83429  ? 173 CYS B CA  1 
ATOM   1357 C C   . CYS A 1 173 ? 22.67091 -10.31596 19.18494  1.000 60.77679  ? 173 CYS B C   1 
ATOM   1358 O O   . CYS A 1 173 ? 23.46654 -9.51684  19.71492  1.000 57.73318  ? 173 CYS B O   1 
ATOM   1359 C CB  . CYS A 1 173 ? 23.13551 -10.30363 16.71913  1.000 59.45249  ? 173 CYS B CB  1 
ATOM   1360 S SG  . CYS A 1 173 ? 23.60066 -12.02851 16.64260  1.000 66.22272  ? 173 CYS B SG  1 
ATOM   1361 N N   . PRO A 1 174 ? 22.27572 -11.42619 19.80715  1.000 63.00190  ? 174 PRO B N   1 
ATOM   1362 C CA  . PRO A 1 174 ? 22.82466 -11.77811 21.12273  1.000 61.36843  ? 174 PRO B CA  1 
ATOM   1363 C C   . PRO A 1 174 ? 24.28816 -12.18036 21.03697  1.000 67.19504  ? 174 PRO B C   1 
ATOM   1364 O O   . PRO A 1 174 ? 24.71668 -12.85882 20.10042  1.000 67.38025  ? 174 PRO B O   1 
ATOM   1365 C CB  . PRO A 1 174 ? 21.95029 -12.95208 21.56752  1.000 61.79319  ? 174 PRO B CB  1 
ATOM   1366 C CG  . PRO A 1 174 ? 20.67062 -12.79864 20.74409  1.000 60.37769  ? 174 PRO B CG  1 
ATOM   1367 C CD  . PRO A 1 174 ? 21.15634 -12.30238 19.42204  1.000 63.97061  ? 174 PRO B CD  1 
ATOM   1368 N N   . LEU A 1 175 ? 25.05409 -11.76385 22.04003  1.000 64.09465  ? 175 LEU B N   1 
ATOM   1369 C CA  . LEU A 1 175 ? 26.47407 -12.02075 22.05135  1.000 64.62303  ? 175 LEU B CA  1 
ATOM   1370 C C   . LEU A 1 175 ? 26.86421 -12.90587 23.23087  1.000 66.64003  ? 175 LEU B C   1 
ATOM   1371 O O   . LEU A 1 175 ? 26.27434 -12.79219 24.31022  1.000 66.77391  ? 175 LEU B O   1 
ATOM   1372 C CB  . LEU A 1 175 ? 27.23029 -10.70033 22.12073  1.000 64.25224  ? 175 LEU B CB  1 
ATOM   1373 C CG  . LEU A 1 175 ? 26.82764 -9.82115  20.94043  1.000 63.15419  ? 175 LEU B CG  1 
ATOM   1374 C CD1 . LEU A 1 175 ? 27.27206 -8.37584  21.14333  1.000 56.84408  ? 175 LEU B CD1 1 
ATOM   1375 C CD2 . LEU A 1 175 ? 27.37401 -10.41034 19.64605  1.000 61.45734  ? 175 LEU B CD2 1 
ATOM   1376 N N   . PRO A 1 176 ? 27.84798 -13.79248 23.05636  1.000 69.28156  ? 176 PRO B N   1 
ATOM   1377 C CA  . PRO A 1 176 ? 28.31058 -14.61371 24.18022  1.000 71.44758  ? 176 PRO B CA  1 
ATOM   1378 C C   . PRO A 1 176 ? 28.80210 -13.76698 25.34636  1.000 70.25138  ? 176 PRO B C   1 
ATOM   1379 O O   . PRO A 1 176 ? 29.25261 -12.62944 25.17262  1.000 65.21878  ? 176 PRO B O   1 
ATOM   1380 C CB  . PRO A 1 176 ? 29.45091 -15.43772 23.57157  1.000 63.02198  ? 176 PRO B CB  1 
ATOM   1381 C CG  . PRO A 1 176 ? 29.84745 -14.69597 22.33565  1.000 63.77935  ? 176 PRO B CG  1 
ATOM   1382 C CD  . PRO A 1 176 ? 28.57334 -14.11673 21.81737  1.000 65.80220  ? 176 PRO B CD  1 
ATOM   1383 N N   . LYS A 1 177 ? 28.71487 -14.35740 26.54556  1.000 72.87551  ? 177 LYS B N   1 
ATOM   1384 C CA  . LYS A 1 177 ? 29.02023 -13.66021 27.79096  1.000 67.89372  ? 177 LYS B CA  1 
ATOM   1385 C C   . LYS A 1 177 ? 30.33881 -12.91141 27.68854  1.000 65.01192  ? 177 LYS B C   1 
ATOM   1386 O O   . LYS A 1 177 ? 31.27886 -13.37123 27.03967  1.000 61.14476  ? 177 LYS B O   1 
ATOM   1387 C CB  . LYS A 1 177 ? 29.08132 -14.65864 28.95004  1.000 71.93673  ? 177 LYS B CB  1 
ATOM   1388 N N   . GLY A 1 178 ? 30.39001 -11.73597 28.31375  1.000 65.76133  ? 178 GLY B N   1 
ATOM   1389 C CA  . GLY A 1 178 ? 31.59746 -10.93678 28.35240  1.000 62.74245  ? 178 GLY B CA  1 
ATOM   1390 C C   . GLY A 1 178 ? 31.99990 -10.27807 27.05344  1.000 61.51821  ? 178 GLY B C   1 
ATOM   1391 O O   . GLY A 1 178 ? 32.98749 -9.52879  27.04465  1.000 61.29433  ? 178 GLY B O   1 
ATOM   1392 N N   . THR A 1 179 ? 31.27265 -10.52238 25.95812  1.000 61.76849  ? 179 THR B N   1 
ATOM   1393 C CA  . THR A 1 179 ? 31.63858 -9.91924  24.68116  1.000 59.31960  ? 179 THR B CA  1 
ATOM   1394 C C   . THR A 1 179 ? 31.67258 -8.39796  24.77882  1.000 55.44347  ? 179 THR B C   1 
ATOM   1395 O O   . THR A 1 179 ? 32.60984 -7.76263  24.28346  1.000 60.58544  ? 179 THR B O   1 
ATOM   1396 C CB  . THR A 1 179 ? 30.67249 -10.38310 23.59058  1.000 62.28784  ? 179 THR B CB  1 
ATOM   1397 O OG1 . THR A 1 179 ? 30.99791 -11.72879 23.21364  1.000 62.11462  ? 179 THR B OG1 1 
ATOM   1398 C CG2 . THR A 1 179 ? 30.76185 -9.48733  22.36574  1.000 61.61311  ? 179 THR B CG2 1 
ATOM   1399 N N   . LEU A 1 180 ? 30.69415 -7.79724  25.46099  1.000 55.91372  ? 180 LEU B N   1 
ATOM   1400 C CA  . LEU A 1 180 ? 30.62905 -6.34704  25.61626  1.000 59.01593  ? 180 LEU B CA  1 
ATOM   1401 C C   . LEU A 1 180 ? 31.23748 -5.86391  26.93205  1.000 57.30509  ? 180 LEU B C   1 
ATOM   1402 O O   . LEU A 1 180 ? 30.97930 -4.72832  27.34790  1.000 54.97968  ? 180 LEU B O   1 
ATOM   1403 C CB  . LEU A 1 180 ? 29.18301 -5.85640  25.48659  1.000 47.49102  ? 180 LEU B CB  1 
ATOM   1404 N N   . ASP A 1 181 ? 32.04924 -6.69263  27.58661  1.000 57.82534  ? 181 ASP B N   1 
ATOM   1405 C CA  . ASP A 1 181 ? 32.71530 -6.26499  28.80799  1.000 57.35206  ? 181 ASP B CA  1 
ATOM   1406 C C   . ASP A 1 181 ? 33.49380 -4.98273  28.55509  1.000 59.08980  ? 181 ASP B C   1 
ATOM   1407 O O   . ASP A 1 181 ? 34.25460 -4.88050  27.58926  1.000 62.30083  ? 181 ASP B O   1 
ATOM   1408 C CB  . ASP A 1 181 ? 33.64284 -7.36811  29.32110  1.000 60.36929  ? 181 ASP B CB  1 
ATOM   1409 N N   . GLY A 1 182 ? 33.26869 -3.98782  29.40393  1.000 58.63696  ? 182 GLY B N   1 
ATOM   1410 C CA  . GLY A 1 182 ? 33.87763 -2.69165  29.22389  1.000 52.19104  ? 182 GLY B CA  1 
ATOM   1411 C C   . GLY A 1 182 ? 33.00459 -1.66510  28.54054  1.000 59.78243  ? 182 GLY B C   1 
ATOM   1412 O O   . GLY A 1 182 ? 33.41062 -0.49763  28.45183  1.000 56.42562  ? 182 GLY B O   1 
ATOM   1413 N N   . PHE A 1 183 ? 31.81652 -2.05336  28.06667  1.000 62.20333  ? 183 PHE B N   1 
ATOM   1414 C CA  . PHE A 1 183 ? 30.96063 -1.12088  27.34516  1.000 57.57212  ? 183 PHE B CA  1 
ATOM   1415 C C   . PHE A 1 183 ? 30.60897 0.07230   28.22480  1.000 58.80681  ? 183 PHE B C   1 
ATOM   1416 O O   . PHE A 1 183 ? 30.25430 -0.08862  29.39876  1.000 59.03840  ? 183 PHE B O   1 
ATOM   1417 C CB  . PHE A 1 183 ? 29.69136 -1.82858  26.87133  1.000 59.53449  ? 183 PHE B CB  1 
ATOM   1418 C CG  . PHE A 1 183 ? 28.87359 -1.02491  25.89232  1.000 58.77883  ? 183 PHE B CG  1 
ATOM   1419 C CD1 . PHE A 1 183 ? 29.07550 -1.15580  24.52675  1.000 60.02139  ? 183 PHE B CD1 1 
ATOM   1420 C CD2 . PHE A 1 183 ? 27.90462 -0.14106  26.33587  1.000 59.27241  ? 183 PHE B CD2 1 
ATOM   1421 C CE1 . PHE A 1 183 ? 28.32223 -0.41461  23.61526  1.000 56.41417  ? 183 PHE B CE1 1 
ATOM   1422 C CE2 . PHE A 1 183 ? 27.14451 0.60193   25.43002  1.000 61.42428  ? 183 PHE B CE2 1 
ATOM   1423 C CZ  . PHE A 1 183 ? 27.36306 0.46325   24.06972  1.000 54.97085  ? 183 PHE B CZ  1 
ATOM   1424 N N   . VAL A 1 184 ? 30.72818 1.27034   27.65080  1.000 57.32990  ? 184 VAL B N   1 
ATOM   1425 C CA  . VAL A 1 184 ? 30.34717 2.52572   28.29192  1.000 56.64027  ? 184 VAL B CA  1 
ATOM   1426 C C   . VAL A 1 184 ? 29.17106 3.11223   27.51653  1.000 63.00971  ? 184 VAL B C   1 
ATOM   1427 O O   . VAL A 1 184 ? 29.26736 3.34989   26.30536  1.000 61.29102  ? 184 VAL B O   1 
ATOM   1428 C CB  . VAL A 1 184 ? 31.51606 3.51969   28.34662  1.000 54.68720  ? 184 VAL B CB  1 
ATOM   1429 N N   . ALA A 1 185 ? 28.06588 3.35155   28.21333  1.000 56.80493  ? 185 ALA B N   1 
ATOM   1430 C CA  . ALA A 1 185 ? 26.88863 3.91219   27.57419  1.000 60.47501  ? 185 ALA B CA  1 
ATOM   1431 C C   . ALA A 1 185 ? 27.18193 5.29132   26.99866  1.000 57.84635  ? 185 ALA B C   1 
ATOM   1432 O O   . ALA A 1 185 ? 27.84417 6.11500   27.63124  1.000 62.01690  ? 185 ALA B O   1 
ATOM   1433 C CB  . ALA A 1 185 ? 25.74077 3.99836   28.58124  1.000 68.14092  ? 185 ALA B CB  1 
ATOM   1434 N N   . HIS A 1 186 ? 26.69441 5.52329   25.77596  1.000 58.54660  ? 186 HIS B N   1 
ATOM   1435 C CA  . HIS A 1 186 ? 26.77523 6.79413   25.05754  1.000 57.67817  ? 186 HIS B CA  1 
ATOM   1436 C C   . HIS A 1 186 ? 28.16751 7.12388   24.54976  1.000 55.87428  ? 186 HIS B C   1 
ATOM   1437 O O   . HIS A 1 186 ? 28.46457 8.29391   24.30986  1.000 53.14038  ? 186 HIS B O   1 
ATOM   1438 C CB  . HIS A 1 186 ? 26.26817 7.95982   25.90648  1.000 61.74760  ? 186 HIS B CB  1 
ATOM   1439 C CG  . HIS A 1 186 ? 24.85114 7.79803   26.34396  1.000 67.46037  ? 186 HIS B CG  1 
ATOM   1440 N ND1 . HIS A 1 186 ? 24.50506 7.29398   27.57861  1.000 68.10277  ? 186 HIS B ND1 1 
ATOM   1441 C CD2 . HIS A 1 186 ? 23.69008 8.04316   25.69639  1.000 62.18451  ? 186 HIS B CD2 1 
ATOM   1442 C CE1 . HIS A 1 186 ? 23.19007 7.25185   27.67908  1.000 65.80274  ? 186 HIS B CE1 1 
ATOM   1443 N NE2 . HIS A 1 186 ? 22.67259 7.70465   26.55222  1.000 67.73337  ? 186 HIS B NE2 1 
ATOM   1444 N N   . ASP A 1 187 ? 29.03483 6.13050   24.38252  1.000 55.63994  ? 187 ASP B N   1 
ATOM   1445 C CA  . ASP A 1 187 ? 30.32211 6.33641   23.72445  1.000 53.23929  ? 187 ASP B CA  1 
ATOM   1446 C C   . ASP A 1 187 ? 30.16697 5.99625   22.24317  1.000 48.48260  ? 187 ASP B C   1 
ATOM   1447 O O   . ASP A 1 187 ? 29.88020 4.84008   21.89276  1.000 42.29178  ? 187 ASP B O   1 
ATOM   1448 C CB  . ASP A 1 187 ? 31.40924 5.47906   24.37594  1.000 51.92589  ? 187 ASP B CB  1 
ATOM   1449 C CG  . ASP A 1 187 ? 32.79651 5.80200   23.85811  1.000 52.11668  ? 187 ASP B CG  1 
ATOM   1450 O OD1 . ASP A 1 187 ? 33.03319 5.65787   22.63902  1.000 50.28247  ? 187 ASP B OD1 1 
ATOM   1451 O OD2 . ASP A 1 187 ? 33.65241 6.20891   24.67436  1.000 51.77098  ? 187 ASP B OD2 1 
ATOM   1452 N N   . SER A 1 188 ? 30.35238 7.00556   21.38042  1.000 45.61542  ? 188 SER B N   1 
ATOM   1453 C CA  . SER A 1 188 ? 30.16064 6.81347   19.94072  1.000 46.30206  ? 188 SER B CA  1 
ATOM   1454 C C   . SER A 1 188 ? 30.96122 5.62790   19.39889  1.000 46.00626  ? 188 SER B C   1 
ATOM   1455 O O   . SER A 1 188 ? 30.44740 4.84585   18.58661  1.000 43.33164  ? 188 SER B O   1 
ATOM   1456 C CB  . SER A 1 188 ? 30.52172 8.09408   19.17928  1.000 43.34554  ? 188 SER B CB  1 
ATOM   1457 O OG  . SER A 1 188 ? 29.88758 9.24923   19.72422  1.000 48.82535  ? 188 SER B OG  1 
ATOM   1458 N N   . ILE A 1 189 ? 32.21327 5.46836   19.84649  1.000 41.58628  ? 189 ILE B N   1 
ATOM   1459 C CA  . ILE A 1 189 ? 33.05711 4.38225   19.34620  1.000 47.23892  ? 189 ILE B CA  1 
ATOM   1460 C C   . ILE A 1 189 ? 32.56760 3.04395   19.87066  1.000 46.62297  ? 189 ILE B C   1 
ATOM   1461 O O   . ILE A 1 189 ? 32.57935 2.02762   19.15465  1.000 46.94912  ? 189 ILE B O   1 
ATOM   1462 C CB  . ILE A 1 189 ? 34.53214 4.61150   19.73568  1.000 50.26310  ? 189 ILE B CB  1 
ATOM   1463 C CG1 . ILE A 1 189 ? 35.18060 5.68854   18.85127  1.000 49.94990  ? 189 ILE B CG1 1 
ATOM   1464 C CG2 . ILE A 1 189 ? 35.29894 3.30064   19.66243  1.000 44.41042  ? 189 ILE B CG2 1 
ATOM   1465 C CD1 . ILE A 1 189 ? 36.45548 6.27650   19.42542  1.000 45.26421  ? 189 ILE B CD1 1 
ATOM   1466 N N   . HIS A 1 190 ? 32.15402 3.01477   21.13843  1.000 49.73801  ? 190 HIS B N   1 
ATOM   1467 C CA  . HIS A 1 190 ? 31.61455 1.78485   21.71602  1.000 52.68020  ? 190 HIS B CA  1 
ATOM   1468 C C   . HIS A 1 190 ? 30.38943 1.29797   20.95017  1.000 46.61411  ? 190 HIS B C   1 
ATOM   1469 O O   . HIS A 1 190 ? 30.25019 0.09586   20.70364  1.000 49.50957  ? 190 HIS B O   1 
ATOM   1470 C CB  . HIS A 1 190 ? 31.28250 2.00843   23.18924  1.000 53.31631  ? 190 HIS B CB  1 
ATOM   1471 C CG  . HIS A 1 190 ? 32.49148 2.05978   24.06478  1.000 56.80133  ? 190 HIS B CG  1 
ATOM   1472 N ND1 . HIS A 1 190 ? 32.44324 1.82892   25.42187  1.000 57.66821  ? 190 HIS B ND1 1 
ATOM   1473 C CD2 . HIS A 1 190 ? 33.79234 2.28666   23.76732  1.000 56.08343  ? 190 HIS B CD2 1 
ATOM   1474 C CE1 . HIS A 1 190 ? 33.65874 1.93676   25.92766  1.000 56.22036  ? 190 HIS B CE1 1 
ATOM   1475 N NE2 . HIS A 1 190 ? 34.49559 2.21433   24.94393  1.000 57.07786  ? 190 HIS B NE2 1 
ATOM   1476 N N   . ASP A 1 191 ? 29.50394 2.21757   20.54404  1.000 43.03801  ? 191 ASP B N   1 
ATOM   1477 C CA  . ASP A 1 191 ? 28.31480 1.81144   19.79566  1.000 48.29124  ? 191 ASP B CA  1 
ATOM   1478 C C   . ASP A 1 191 ? 28.68417 1.14058   18.47828  1.000 47.40707  ? 191 ASP B C   1 
ATOM   1479 O O   . ASP A 1 191 ? 28.08111 0.12479   18.10392  1.000 47.77851  ? 191 ASP B O   1 
ATOM   1480 C CB  . ASP A 1 191 ? 27.40272 3.01033   19.53236  1.000 45.83163  ? 191 ASP B CB  1 
ATOM   1481 C CG  . ASP A 1 191 ? 26.59880 3.41643   20.75177  1.000 47.71738  ? 191 ASP B CG  1 
ATOM   1482 O OD1 . ASP A 1 191 ? 26.54269 2.65284   21.73422  1.000 53.13986  ? 191 ASP B OD1 1 
ATOM   1483 O OD2 . ASP A 1 191 ? 26.01477 4.51414   20.71692  1.000 52.91340  ? 191 ASP B OD2 1 
ATOM   1484 N N   . CYS A 1 192 ? 29.67233 1.68825   17.75682  1.000 40.95304  ? 192 CYS B N   1 
ATOM   1485 C CA  . CYS A 1 192 ? 30.04749 1.07758   16.48251  1.000 43.75838  ? 192 CYS B CA  1 
ATOM   1486 C C   . CYS A 1 192 ? 30.65245 -0.30631  16.69100  1.000 48.26908  ? 192 CYS B C   1 
ATOM   1487 O O   . CYS A 1 192 ? 30.34941 -1.24513  15.94101  1.000 48.30419  ? 192 CYS B O   1 
ATOM   1488 C CB  . CYS A 1 192 ? 31.02114 1.97338   15.72646  1.000 45.46333  ? 192 CYS B CB  1 
ATOM   1489 S SG  . CYS A 1 192 ? 30.31884 3.49744   15.10395  1.000 45.12979  ? 192 CYS B SG  1 
ATOM   1490 N N   . ALA A 1 193 ? 31.50450 -0.45283  17.71112  1.000 50.16958  ? 193 ALA B N   1 
ATOM   1491 C CA  . ALA A 1 193 ? 32.09337 -1.75882  17.99960  1.000 49.60563  ? 193 ALA B CA  1 
ATOM   1492 C C   . ALA A 1 193 ? 31.01571 -2.78566  18.34542  1.000 51.80608  ? 193 ALA B C   1 
ATOM   1493 O O   . ALA A 1 193 ? 31.08742 -3.94260  17.90789  1.000 54.05184  ? 193 ALA B O   1 
ATOM   1494 C CB  . ALA A 1 193 ? 33.11659 -1.62836  19.12774  1.000 48.19014  ? 193 ALA B CB  1 
ATOM   1495 N N   . LYS A 1 194 ? 29.99983 -2.38253  19.11593  1.000 47.11972  ? 194 LYS B N   1 
ATOM   1496 C CA  . LYS A 1 194 ? 28.87030 -3.28113  19.36408  1.000 51.88649  ? 194 LYS B CA  1 
ATOM   1497 C C   . LYS A 1 194 ? 28.22637 -3.72406  18.05566  1.000 52.07746  ? 194 LYS B C   1 
ATOM   1498 O O   . LYS A 1 194 ? 27.94079 -4.91221  17.86524  1.000 50.63110  ? 194 LYS B O   1 
ATOM   1499 C CB  . LYS A 1 194 ? 27.82225 -2.60576  20.26175  1.000 50.29858  ? 194 LYS B CB  1 
ATOM   1500 N N   . ASP A 1 195 ? 28.00244 -2.78264  17.13123  1.000 51.11097  ? 195 ASP B N   1 
ATOM   1501 C CA  . ASP A 1 195 ? 27.33365 -3.13964  15.88603  1.000 49.81693  ? 195 ASP B CA  1 
ATOM   1502 C C   . ASP A 1 195 ? 28.21476 -4.02842  15.01017  1.000 50.09020  ? 195 ASP B C   1 
ATOM   1503 O O   . ASP A 1 195 ? 27.71691 -4.97580  14.38917  1.000 49.76770  ? 195 ASP B O   1 
ATOM   1504 C CB  . ASP A 1 195 ? 26.90341 -1.87457  15.14718  1.000 49.72029  ? 195 ASP B CB  1 
ATOM   1505 C CG  . ASP A 1 195 ? 25.45792 -1.49563  15.43845  1.000 53.44336  ? 195 ASP B CG  1 
ATOM   1506 O OD1 . ASP A 1 195 ? 24.68279 -2.35934  15.92769  1.000 53.86362  ? 195 ASP B OD1 1 
ATOM   1507 O OD2 . ASP A 1 195 ? 25.10062 -0.32063  15.20188  1.000 52.16970  ? 195 ASP B OD2 1 
ATOM   1508 N N   . ILE A 1 196 ? 29.52381 -3.75130  14.94916  1.000 49.15152  ? 196 ILE B N   1 
ATOM   1509 C CA  . ILE A 1 196 ? 30.43194 -4.66261  14.24984  1.000 49.96577  ? 196 ILE B CA  1 
ATOM   1510 C C   . ILE A 1 196 ? 30.32322 -6.05971  14.84231  1.000 54.04912  ? 196 ILE B C   1 
ATOM   1511 O O   . ILE A 1 196 ? 30.14682 -7.05330  14.12255  1.000 53.30073  ? 196 ILE B O   1 
ATOM   1512 C CB  . ILE A 1 196 ? 31.88030 -4.14560  14.30606  1.000 53.23941  ? 196 ILE B CB  1 
ATOM   1513 C CG1 . ILE A 1 196 ? 32.04940 -2.91010  13.42743  1.000 49.55510  ? 196 ILE B CG1 1 
ATOM   1514 C CG2 . ILE A 1 196 ? 32.85444 -5.22511  13.85613  1.000 49.48694  ? 196 ILE B CG2 1 
ATOM   1515 C CD1 . ILE A 1 196 ? 33.36575 -2.20589  13.64329  1.000 45.82883  ? 196 ILE B CD1 1 
ATOM   1516 N N   . LEU A 1 197 ? 30.38054 -6.14798  16.17618  1.000 55.19462  ? 197 LEU B N   1 
ATOM   1517 C CA  . LEU A 1 197 ? 30.31538 -7.44596  16.83925  1.000 51.78014  ? 197 LEU B CA  1 
ATOM   1518 C C   . LEU A 1 197 ? 28.98342 -8.13551  16.57972  1.000 55.29315  ? 197 LEU B C   1 
ATOM   1519 O O   . LEU A 1 197 ? 28.94455 -9.34360  16.30827  1.000 57.14887  ? 197 LEU B O   1 
ATOM   1520 C CB  . LEU A 1 197 ? 30.56780 -7.28258  18.33746  1.000 53.55866  ? 197 LEU B CB  1 
ATOM   1521 C CG  . LEU A 1 197 ? 32.04035 -7.04666  18.68182  1.000 58.64522  ? 197 LEU B CG  1 
ATOM   1522 C CD1 . LEU A 1 197 ? 32.19166 -6.39653  20.04083  1.000 58.26968  ? 197 LEU B CD1 1 
ATOM   1523 C CD2 . LEU A 1 197 ? 32.82214 -8.34480  18.61450  1.000 57.10694  ? 197 LEU B CD2 1 
ATOM   1524 N N   . MET A 1 198 ? 27.87349 -7.38716  16.65831  1.000 53.29642  ? 198 MET B N   1 
ATOM   1525 C CA  . MET A 1 198 ? 26.57073 -8.00801  16.41662  1.000 54.14586  ? 198 MET B CA  1 
ATOM   1526 C C   . MET A 1 198 ? 26.44248 -8.49665  14.98146  1.000 56.64336  ? 198 MET B C   1 
ATOM   1527 O O   . MET A 1 198 ? 25.79239 -9.51751  14.72190  1.000 57.59639  ? 198 MET B O   1 
ATOM   1528 C CB  . MET A 1 198 ? 25.42236 -7.04075  16.74452  1.000 55.09348  ? 198 MET B CB  1 
ATOM   1529 C CG  . MET A 1 198 ? 25.08867 -6.87634  18.22178  1.000 51.40485  ? 198 MET B CG  1 
ATOM   1530 S SD  . MET A 1 198 ? 23.69167 -5.74916  18.45428  1.000 58.65803  ? 198 MET B SD  1 
ATOM   1531 C CE  . MET A 1 198 ? 23.41750 -5.85321  20.22080  1.000 51.91211  ? 198 MET B CE  1 
ATOM   1532 N N   . MET A 1 199 ? 27.05893 -7.79137  14.03884  1.000 56.13146  ? 199 MET B N   1 
ATOM   1533 C CA  . MET A 1 199 ? 26.99737 -8.22775  12.65114  1.000 55.71207  ? 199 MET B CA  1 
ATOM   1534 C C   . MET A 1 199 ? 27.83051 -9.48557  12.44935  1.000 57.45466  ? 199 MET B C   1 
ATOM   1535 O O   . MET A 1 199 ? 27.39242 -10.42668 11.77800  1.000 55.18857  ? 199 MET B O   1 
ATOM   1536 C CB  . MET A 1 199 ? 27.49192 -7.10631  11.74124  1.000 54.00568  ? 199 MET B CB  1 
ATOM   1537 C CG  . MET A 1 199 ? 26.37775 -6.25192  11.13212  1.000 54.90133  ? 199 MET B CG  1 
ATOM   1538 S SD  . MET A 1 199 ? 27.07609 -5.07926  9.93661   1.000 54.91122  ? 199 MET B SD  1 
ATOM   1539 C CE  . MET A 1 199 ? 28.39410 -4.31932  10.88831  1.000 38.44392  ? 199 MET B CE  1 
ATOM   1540 N N   . LYS A 1 200 ? 29.03568 -9.51619  13.03245  1.000 58.06692  ? 200 LYS B N   1 
ATOM   1541 C CA  . LYS A 1 200 ? 29.90819 -10.68231 12.92054  1.000 55.79500  ? 200 LYS B CA  1 
ATOM   1542 C C   . LYS A 1 200 ? 29.22985 -11.93143 13.46776  1.000 59.22110  ? 200 LYS B C   1 
ATOM   1543 O O   . LYS A 1 200 ? 29.10401 -12.94744 12.77202  1.000 55.59841  ? 200 LYS B O   1 
ATOM   1544 C CB  . LYS A 1 200 ? 31.22191 -10.42244 13.65815  1.000 55.90792  ? 200 LYS B CB  1 
ATOM   1545 N N   . TYR A 1 201 ? 28.76816 -11.86855 14.71726  1.000 60.50632  ? 201 TYR B N   1 
ATOM   1546 C CA  . TYR A 1 201 ? 28.20276 -13.06358 15.32873  1.000 63.42559  ? 201 TYR B CA  1 
ATOM   1547 C C   . TYR A 1 201 ? 26.95975 -13.51839 14.58178  1.000 62.36476  ? 201 TYR B C   1 
ATOM   1548 O O   . TYR A 1 201 ? 26.78896 -14.71663 14.33849  1.000 67.51076  ? 201 TYR B O   1 
ATOM   1549 C CB  . TYR A 1 201 ? 27.92373 -12.82071 16.81471  1.000 63.87566  ? 201 TYR B CB  1 
ATOM   1550 C CG  . TYR A 1 201 ? 29.18106 -13.00116 17.65225  1.000 64.37478  ? 201 TYR B CG  1 
ATOM   1551 C CD1 . TYR A 1 201 ? 30.02721 -11.92457 17.91414  1.000 61.71925  ? 201 TYR B CD1 1 
ATOM   1552 C CD2 . TYR A 1 201 ? 29.55380 -14.25814 18.13099  1.000 65.54640  ? 201 TYR B CD2 1 
ATOM   1553 C CE1 . TYR A 1 201 ? 31.17931 -12.08412 18.65638  1.000 58.87786  ? 201 TYR B CE1 1 
ATOM   1554 C CE2 . TYR A 1 201 ? 30.71210 -14.42555 18.87068  1.000 55.81489  ? 201 TYR B CE2 1 
ATOM   1555 C CZ  . TYR A 1 201 ? 31.51298 -13.33555 19.13282  1.000 60.69072  ? 201 TYR B CZ  1 
ATOM   1556 O OH  . TYR A 1 201 ? 32.66599 -13.49234 19.86798  1.000 69.52766  ? 201 TYR B OH  1 
ATOM   1557 N N   . ALA A 1 202 ? 26.11036 -12.57471 14.15808  1.000 60.59001  ? 202 ALA B N   1 
ATOM   1558 C CA  . ALA A 1 202 ? 24.96459 -12.93067 13.32037  1.000 62.87004  ? 202 ALA B CA  1 
ATOM   1559 C C   . ALA A 1 202 ? 25.40288 -13.69164 12.07112  1.000 61.66514  ? 202 ALA B C   1 
ATOM   1560 O O   . ALA A 1 202 ? 24.73797 -14.64442 11.64605  1.000 62.79130  ? 202 ALA B O   1 
ATOM   1561 C CB  . ALA A 1 202 ? 24.17818 -11.67497 12.93261  1.000 57.94907  ? 202 ALA B CB  1 
ATOM   1562 N N   . LEU A 1 203 ? 26.51363 -13.28053 11.46170  1.000 58.14072  ? 203 LEU B N   1 
ATOM   1563 C CA  . LEU A 1 203 ? 27.05523 -14.04841 10.34977  1.000 60.44094  ? 203 LEU B CA  1 
ATOM   1564 C C   . LEU A 1 203 ? 27.46852 -15.44010 10.80911  1.000 63.65707  ? 203 LEU B C   1 
ATOM   1565 O O   . LEU A 1 203 ? 27.17609 -16.43957 10.14367  1.000 66.57759  ? 203 LEU B O   1 
ATOM   1566 C CB  . LEU A 1 203 ? 28.23696 -13.31134 9.72291   1.000 55.48890  ? 203 LEU B CB  1 
ATOM   1567 C CG  . LEU A 1 203 ? 28.83332 -13.97079 8.47817   1.000 53.82009  ? 203 LEU B CG  1 
ATOM   1568 C CD1 . LEU A 1 203 ? 27.78862 -14.21819 7.41675   1.000 53.31860  ? 203 LEU B CD1 1 
ATOM   1569 C CD2 . LEU A 1 203 ? 29.99045 -13.15800 7.92588   1.000 51.11238  ? 203 LEU B CD2 1 
ATOM   1570 N N   . ARG A 1 204 ? 28.13125 -15.52762 11.96242  1.000 64.31120  ? 204 ARG B N   1 
ATOM   1571 C CA  . ARG A 1 204 ? 28.56339 -16.83131 12.45223  1.000 68.83245  ? 204 ARG B CA  1 
ATOM   1572 C C   . ARG A 1 204 ? 27.36715 -17.72317 12.77685  1.000 68.18810  ? 204 ARG B C   1 
ATOM   1573 O O   . ARG A 1 204 ? 27.35478 -18.90597 12.42189  1.000 70.14263  ? 204 ARG B O   1 
ATOM   1574 C CB  . ARG A 1 204 ? 29.47297 -16.66093 13.66817  1.000 67.93365  ? 204 ARG B CB  1 
ATOM   1575 N N   . TYR A 1 205 ? 26.33565 -17.17407 13.42013  1.000 67.25578  ? 205 TYR B N   1 
ATOM   1576 C CA  . TYR A 1 205 ? 25.16124 -17.99185 13.70901  1.000 67.64438  ? 205 TYR B CA  1 
ATOM   1577 C C   . TYR A 1 205 ? 24.44429 -18.42840 12.44025  1.000 71.71207  ? 205 TYR B C   1 
ATOM   1578 O O   . TYR A 1 205 ? 23.71744 -19.42827 12.46361  1.000 77.67587  ? 205 TYR B O   1 
ATOM   1579 C CB  . TYR A 1 205 ? 24.16808 -17.25588 14.61174  1.000 68.73857  ? 205 TYR B CB  1 
ATOM   1580 C CG  . TYR A 1 205 ? 24.75941 -16.64288 15.86247  1.000 72.22319  ? 205 TYR B CG  1 
ATOM   1581 C CD1 . TYR A 1 205 ? 25.94494 -17.13016 16.42038  1.000 72.88874  ? 205 TYR B CD1 1 
ATOM   1582 C CD2 . TYR A 1 205 ? 24.11761 -15.58660 16.50302  1.000 69.31124  ? 205 TYR B CD2 1 
ATOM   1583 C CE1 . TYR A 1 205 ? 26.48298 -16.55971 17.56692  1.000 73.67679  ? 205 TYR B CE1 1 
ATOM   1584 C CE2 . TYR A 1 205 ? 24.64149 -15.01936 17.65116  1.000 68.08289  ? 205 TYR B CE2 1 
ATOM   1585 C CZ  . TYR A 1 205 ? 25.82128 -15.50329 18.17605  1.000 73.86070  ? 205 TYR B CZ  1 
ATOM   1586 O OH  . TYR A 1 205 ? 26.34230 -14.92549 19.31270  1.000 72.36379  ? 205 TYR B OH  1 
ATOM   1587 N N   . ALA A 1 206 ? 24.62083 -17.69958 11.33841  1.000 68.75881  ? 206 ALA B N   1 
ATOM   1588 C CA  . ALA A 1 206 ? 24.00074 -18.09386 10.08183  1.000 66.88772  ? 206 ALA B CA  1 
ATOM   1589 C C   . ALA A 1 206 ? 24.82517 -19.14496 9.35923   1.000 72.48586  ? 206 ALA B C   1 
ATOM   1590 O O   . ALA A 1 206 ? 24.25984 -20.02326 8.69581   1.000 71.92272  ? 206 ALA B O   1 
ATOM   1591 C CB  . ALA A 1 206 ? 23.81234 -16.87080 9.18621   1.000 68.68443  ? 206 ALA B CB  1 
ATOM   1592 N N   . MET A 1 207 ? 26.15269 -19.06639 9.47897   1.000 69.81917  ? 207 MET B N   1 
ATOM   1593 C CA  . MET A 1 207 ? 27.07453 -20.00812 8.85544   1.000 71.38851  ? 207 MET B CA  1 
ATOM   1594 C C   . MET A 1 207 ? 27.31558 -21.27207 9.67923   1.000 74.25761  ? 207 MET B C   1 
ATOM   1595 O O   . MET A 1 207 ? 28.11655 -22.11427 9.25633   1.000 72.52815  ? 207 MET B O   1 
ATOM   1596 C CB  . MET A 1 207 ? 28.42576 -19.33392 8.60083   1.000 69.60001  ? 207 MET B CB  1 
ATOM   1597 C CG  . MET A 1 207 ? 28.42874 -18.25703 7.53658   1.000 64.67495  ? 207 MET B CG  1 
ATOM   1598 S SD  . MET A 1 207 ? 30.10491 -17.66964 7.25249   1.000 70.21126  ? 207 MET B SD  1 
ATOM   1599 C CE  . MET A 1 207 ? 30.17427 -17.69050 5.46089   1.000 70.04463  ? 207 MET B CE  1 
ATOM   1600 N N   . GLY A 1 208 ? 26.67923 -21.41907 10.84180  1.000 72.01745  ? 208 GLY B N   1 
ATOM   1601 C CA  . GLY A 1 208 ? 26.94430 -22.55782 11.70302  1.000 71.21379  ? 208 GLY B CA  1 
ATOM   1602 C C   . GLY A 1 208 ? 28.30089 -22.58079 12.38647  1.000 74.22771  ? 208 GLY B C   1 
ATOM   1603 O O   . GLY A 1 208 ? 28.64741 -23.59730 12.99394  1.000 76.30896  ? 208 GLY B O   1 
ATOM   1604 N N   . LEU A 1 209 ? 29.08890 -21.50048 12.30799  1.000 71.97237  ? 209 LEU B N   1 
ATOM   1605 C CA  . LEU A 1 209 ? 30.39294 -21.47088 12.97032  1.000 74.72810  ? 209 LEU B CA  1 
ATOM   1606 C C   . LEU A 1 209 ? 30.27215 -21.47185 14.49068  1.000 72.47124  ? 209 LEU B C   1 
ATOM   1607 O O   . LEU A 1 209 ? 31.21737 -21.86914 15.17786  1.000 73.47350  ? 209 LEU B O   1 
ATOM   1608 C CB  . LEU A 1 209 ? 31.19091 -20.24117 12.52610  1.000 72.02753  ? 209 LEU B CB  1 
ATOM   1609 C CG  . LEU A 1 209 ? 31.46051 -20.07669 11.03107  1.000 71.35047  ? 209 LEU B CG  1 
ATOM   1610 C CD1 . LEU A 1 209 ? 32.20016 -18.77512 10.77089  1.000 72.16072  ? 209 LEU B CD1 1 
ATOM   1611 C CD2 . LEU A 1 209 ? 32.23811 -21.25329 10.47782  1.000 69.35104  ? 209 LEU B CD2 1 
ATOM   1612 N N   . GLU A 1 210 ? 29.14671 -21.00981 15.02623  1.000 74.37804  ? 210 GLU B N   1 
ATOM   1613 C CA  . GLU A 1 210 ? 28.83970 -21.13510 16.44310  1.000 74.78777  ? 210 GLU B CA  1 
ATOM   1614 C C   . GLU A 1 210 ? 27.32666 -21.15066 16.58161  1.000 75.95262  ? 210 GLU B C   1 
ATOM   1615 O O   . GLU A 1 210 ? 26.59637 -20.79995 15.64973  1.000 75.70183  ? 210 GLU B O   1 
ATOM   1616 C CB  . GLU A 1 210 ? 29.45544 -19.99863 17.27357  1.000 69.75213  ? 210 GLU B CB  1 
ATOM   1617 N N   . ASP A 1 211 ? 26.85457 -21.56921 17.74520  1.000 76.81235  ? 211 ASP B N   1 
ATOM   1618 C CA  . ASP A 1 211 ? 25.42930 -21.51211 18.02833  1.000 76.32025  ? 211 ASP B CA  1 
ATOM   1619 C C   . ASP A 1 211 ? 25.13698 -20.29737 18.89950  1.000 75.90810  ? 211 ASP B C   1 
ATOM   1620 O O   . ASP A 1 211 ? 25.94889 -19.90388 19.73835  1.000 72.63666  ? 211 ASP B O   1 
ATOM   1621 C CB  . ASP A 1 211 ? 24.94817 -22.79596 18.71054  1.000 77.20875  ? 211 ASP B CB  1 
ATOM   1622 N N   . ALA A 1 212 ? 23.97714 -19.69278 18.67929  1.000 77.75393  ? 212 ALA B N   1 
ATOM   1623 C CA  . ALA A 1 212 ? 23.63232 -18.48635 19.41519  1.000 81.50301  ? 212 ALA B CA  1 
ATOM   1624 C C   . ALA A 1 212 ? 23.51362 -18.78995 20.90975  1.000 88.05379  ? 212 ALA B C   1 
ATOM   1625 O O   . ALA A 1 212 ? 22.93552 -19.81444 21.29394  1.000 90.03118  ? 212 ALA B O   1 
ATOM   1626 C CB  . ALA A 1 212 ? 22.32005 -17.89321 18.89657  1.000 79.89601  ? 212 ALA B CB  1 
ATOM   1627 N N   . PRO A 1 213 ? 24.05018 -17.92527 21.77346  1.000 86.50554  ? 213 PRO B N   1 
ATOM   1628 C CA  . PRO A 1 213 ? 23.85345 -18.10882 23.21549  1.000 90.63671  ? 213 PRO B CA  1 
ATOM   1629 C C   . PRO A 1 213 ? 22.38597 -17.97753 23.59041  1.000 94.65058  ? 213 PRO B C   1 
ATOM   1630 O O   . PRO A 1 213 ? 21.61480 -17.27798 22.93007  1.000 94.25794  ? 213 PRO B O   1 
ATOM   1631 C CB  . PRO A 1 213 ? 24.68658 -16.98029 23.83262  1.000 86.53190  ? 213 PRO B CB  1 
ATOM   1632 C CG  . PRO A 1 213 ? 24.74827 -15.93559 22.76002  1.000 79.39365  ? 213 PRO B CG  1 
ATOM   1633 C CD  . PRO A 1 213 ? 24.80866 -16.69986 21.47116  1.000 79.88494  ? 213 PRO B CD  1 
ATOM   1634 N N   . SER A 1 214 ? 22.00180 -18.66799 24.66259  1.000 98.50122  ? 214 SER B N   1 
ATOM   1635 C CA  . SER A 1 214 ? 20.63075 -18.58309 25.14552  1.000 94.49126  ? 214 SER B CA  1 
ATOM   1636 C C   . SER A 1 214 ? 20.38092 -17.21374 25.76512  1.000 96.69288  ? 214 SER B C   1 
ATOM   1637 O O   . SER A 1 214 ? 21.30100 -16.56474 26.27486  1.000 95.80502  ? 214 SER B O   1 
ATOM   1638 C CB  . SER A 1 214 ? 20.35008 -19.67652 26.17302  1.000 93.93292  ? 214 SER B CB  1 
ATOM   1639 O OG  . SER A 1 214 ? 20.82218 -19.29392 27.44967  1.000 98.51559  ? 214 SER B OG  1 
ATOM   1640 N N   . GLU A 1 215 ? 19.11365 -16.77863 25.72452  1.000 97.12880  ? 215 GLU B N   1 
ATOM   1641 C CA  . GLU A 1 215 ? 18.74924 -15.45117 26.22018  1.000 96.58005  ? 215 GLU B CA  1 
ATOM   1642 C C   . GLU A 1 215 ? 19.16028 -15.23956 27.67396  1.000 95.60621  ? 215 GLU B C   1 
ATOM   1643 O O   . GLU A 1 215 ? 19.31710 -14.09023 28.10227  1.000 91.09314  ? 215 GLU B O   1 
ATOM   1644 C CB  . GLU A 1 215 ? 17.24368 -15.22035 26.06273  1.000 91.99008  ? 215 GLU B CB  1 
ATOM   1645 N N   . GLU A 1 216 ? 19.34723 -16.31808 28.43654  1.000 95.09233  ? 216 GLU B N   1 
ATOM   1646 C CA  . GLU A 1 216 ? 19.90126 -16.22235 29.77757  1.000 93.81714  ? 216 GLU B CA  1 
ATOM   1647 C C   . GLU A 1 216 ? 21.42406 -16.29154 29.79691  1.000 94.67417  ? 216 GLU B C   1 
ATOM   1648 O O   . GLU A 1 216 ? 22.03986 -15.78471 30.74280  1.000 93.88805  ? 216 GLU B O   1 
ATOM   1649 C CB  . GLU A 1 216 ? 19.33257 -17.33439 30.66597  1.000 95.29300  ? 216 GLU B CB  1 
ATOM   1650 N N   . GLU A 1 217 ? 22.04576 -16.88904 28.77752  1.000 91.76160  ? 217 GLU B N   1 
ATOM   1651 C CA  . GLU A 1 217 ? 23.48487 -17.11566 28.75990  1.000 90.96635  ? 217 GLU B CA  1 
ATOM   1652 C C   . GLU A 1 217 ? 24.23354 -16.15151 27.83757  1.000 90.67977  ? 217 GLU B C   1 
ATOM   1653 O O   . GLU A 1 217 ? 25.36957 -16.43829 27.44820  1.000 86.94461  ? 217 GLU B O   1 
ATOM   1654 C CB  . GLU A 1 217 ? 23.77825 -18.56036 28.35783  1.000 91.55337  ? 217 GLU B CB  1 
ATOM   1655 N N   . CYS A 1 218 ? 23.62867 -15.02165 27.47840  1.000 87.70515  ? 218 CYS B N   1 
ATOM   1656 C CA  . CYS A 1 218 ? 24.24735 -14.03156 26.60510  1.000 76.68698  ? 218 CYS B CA  1 
ATOM   1657 C C   . CYS A 1 218 ? 24.62641 -12.78251 27.39759  1.000 72.01830  ? 218 CYS B C   1 
ATOM   1658 O O   . CYS A 1 218 ? 24.18196 -12.57981 28.53010  1.000 71.70389  ? 218 CYS B O   1 
ATOM   1659 C CB  . CYS A 1 218 ? 23.30554 -13.67569 25.45004  1.000 75.42184  ? 218 CYS B CB  1 
ATOM   1660 S SG  . CYS A 1 218 ? 22.18875 -12.28972 25.77555  1.000 77.38031  ? 218 CYS B SG  1 
ATOM   1661 N N   . ASP A 1 219 ? 25.47737 -11.94619 26.80135  1.000 66.57737  ? 219 ASP B N   1 
ATOM   1662 C CA  . ASP A 1 219 ? 25.76768 -10.64223 27.39493  1.000 65.95281  ? 219 ASP B CA  1 
ATOM   1663 C C   . ASP A 1 219 ? 24.49171 -9.80529  27.41658  1.000 67.91587  ? 219 ASP B C   1 
ATOM   1664 O O   . ASP A 1 219 ? 23.92090 -9.52347  26.34742  1.000 67.31896  ? 219 ASP B O   1 
ATOM   1665 C CB  . ASP A 1 219 ? 26.86422 -9.90185  26.63103  1.000 63.45910  ? 219 ASP B CB  1 
ATOM   1666 N N   . PRO A 1 220 ? 23.99614 -9.41061  28.59113  1.000 62.65173  ? 220 PRO B N   1 
ATOM   1667 C CA  . PRO A 1 220 ? 22.73636 -8.66186  28.63774  1.000 60.79624  ? 220 PRO B CA  1 
ATOM   1668 C C   . PRO A 1 220 ? 22.78782 -7.30544  27.95115  1.000 63.30997  ? 220 PRO B C   1 
ATOM   1669 O O   . PRO A 1 220 ? 21.71959 -6.73630  27.68826  1.000 68.73657  ? 220 PRO B O   1 
ATOM   1670 C CB  . PRO A 1 220 ? 22.46807 -8.52243  30.14194  1.000 60.80302  ? 220 PRO B CB  1 
ATOM   1671 C CG  . PRO A 1 220 ? 23.76523 -8.77694  30.79597  1.000 56.26852  ? 220 PRO B CG  1 
ATOM   1672 C CD  . PRO A 1 220 ? 24.46516 -9.76912  29.93632  1.000 61.92392  ? 220 PRO B CD  1 
ATOM   1673 N N   . LEU A 1 221 ? 23.96832 -6.76280  27.65645  1.000 58.91550  ? 221 LEU B N   1 
ATOM   1674 C CA  . LEU A 1 221 ? 24.01658 -5.53625  26.86755  1.000 59.01574  ? 221 LEU B CA  1 
ATOM   1675 C C   . LEU A 1 221 ? 23.66662 -5.77626  25.40376  1.000 61.44764  ? 221 LEU B C   1 
ATOM   1676 O O   . LEU A 1 221 ? 23.66191 -4.81631  24.62320  1.000 61.02512  ? 221 LEU B O   1 
ATOM   1677 C CB  . LEU A 1 221 ? 25.39791 -4.86763  26.97260  1.000 42.79636  ? 221 LEU B CB  1 
ATOM   1678 N N   . SER A 1 222 ? 23.37408 -7.01519  25.00569  1.000 60.57810  ? 222 SER B N   1 
ATOM   1679 C CA  . SER A 1 222 ? 23.00316 -7.30801  23.62889  1.000 63.53726  ? 222 SER B CA  1 
ATOM   1680 C C   . SER A 1 222 ? 21.52375 -7.61993  23.46403  1.000 67.84055  ? 222 SER B C   1 
ATOM   1681 O O   . SER A 1 222 ? 21.09252 -7.92571  22.34712  1.000 71.88959  ? 222 SER B O   1 
ATOM   1682 C CB  . SER A 1 222 ? 23.82941 -8.47659  23.08256  1.000 61.33516  ? 222 SER B CB  1 
ATOM   1683 O OG  . SER A 1 222 ? 23.66831 -9.62727  23.88071  1.000 64.96364  ? 222 SER B OG  1 
ATOM   1684 N N   . LEU A 1 223 ? 20.73417 -7.54742  24.53170  1.000 71.17607  ? 223 LEU B N   1 
ATOM   1685 C CA  . LEU A 1 223 ? 19.32522 -7.90160  24.46599  1.000 66.70378  ? 223 LEU B CA  1 
ATOM   1686 C C   . LEU A 1 223 ? 18.53655 -6.74869  23.86879  1.000 69.96148  ? 223 LEU B C   1 
ATOM   1687 O O   . LEU A 1 223 ? 19.07409 -5.66521  23.63976  1.000 70.92816  ? 223 LEU B O   1 
ATOM   1688 C CB  . LEU A 1 223 ? 18.81577 -8.25807  25.85844  1.000 64.69313  ? 223 LEU B CB  1 
ATOM   1689 N N   . PRO A 1 224 ? 17.24326 -6.95754  23.58383  1.000 72.51831  ? 224 PRO B N   1 
ATOM   1690 C CA  . PRO A 1 224 ? 16.40190 -5.84596  23.12542  1.000 74.66083  ? 224 PRO B CA  1 
ATOM   1691 C C   . PRO A 1 224 ? 15.92140 -4.97272  24.28206  1.000 71.75084  ? 224 PRO B C   1 
ATOM   1692 O O   . PRO A 1 224 ? 16.22654 -5.29374  25.43462  1.000 71.66255  ? 224 PRO B O   1 
ATOM   1693 C CB  . PRO A 1 224 ? 15.22187 -6.55475  22.45010  1.000 73.30668  ? 224 PRO B CB  1 
ATOM   1694 N N   . MET B 1 1   ? -1.06567 -7.39496  5.60168   1.000 62.06057  ? 1   MET A N   1 
ATOM   1695 C CA  . MET B 1 1   ? 0.06306  -6.46948  5.75601   1.000 66.92417  ? 1   MET A CA  1 
ATOM   1696 C C   . MET B 1 1   ? 1.06881  -6.65969  4.62662   1.000 58.89430  ? 1   MET A C   1 
ATOM   1697 O O   . MET B 1 1   ? 1.82647  -7.62796  4.62296   1.000 58.00475  ? 1   MET A O   1 
ATOM   1698 C CB  . MET B 1 1   ? 0.74828  -6.66302  7.11773   1.000 66.20067  ? 1   MET A CB  1 
ATOM   1699 C CG  . MET B 1 1   ? 1.99103  -5.76258  7.36161   1.000 65.35329  ? 1   MET A CG  1 
ATOM   1700 S SD  . MET B 1 1   ? 3.56987  -6.66079  7.26952   1.000 78.61730  ? 1   MET A SD  1 
ATOM   1701 C CE  . MET B 1 1   ? 4.09965  -6.69166  8.97903   1.000 57.13217  ? 1   MET A CE  1 
ATOM   1702 N N   . PHE B 1 2   ? 1.06701  -5.73591  3.67042   1.000 59.87525  ? 2   PHE A N   1 
ATOM   1703 C CA  . PHE B 1 2   ? 2.00760  -5.74530  2.55404   1.000 61.90123  ? 2   PHE A CA  1 
ATOM   1704 C C   . PHE B 1 2   ? 3.21083  -4.84224  2.85403   1.000 57.48826  ? 2   PHE A C   1 
ATOM   1705 O O   . PHE B 1 2   ? 3.09690  -3.86242  3.59819   1.000 52.36280  ? 2   PHE A O   1 
ATOM   1706 C CB  . PHE B 1 2   ? 1.31754  -5.27593  1.26520   1.000 59.82687  ? 2   PHE A CB  1 
ATOM   1707 C CG  . PHE B 1 2   ? 0.52813  -6.35593  0.54737   1.000 62.36189  ? 2   PHE A CG  1 
ATOM   1708 C CD1 . PHE B 1 2   ? 0.35460  -6.30034  -0.83327  1.000 63.59565  ? 2   PHE A CD1 1 
ATOM   1709 C CD2 . PHE B 1 2   ? -0.05507 -7.40728  1.24358   1.000 65.21975  ? 2   PHE A CD2 1 
ATOM   1710 C CE1 . PHE B 1 2   ? -0.37278 -7.27812  -1.51697  1.000 61.07536  ? 2   PHE A CE1 1 
ATOM   1711 C CE2 . PHE B 1 2   ? -0.78652 -8.39030  0.56862   1.000 61.75080  ? 2   PHE A CE2 1 
ATOM   1712 C CZ  . PHE B 1 2   ? -0.94279 -8.32188  -0.81140  1.000 58.45250  ? 2   PHE A CZ  1 
ATOM   1713 N N   . ASP B 1 3   ? 4.37756  -5.21140  2.29119   1.000 51.98870  ? 3   ASP A N   1 
ATOM   1714 C CA  . ASP B 1 3   ? 5.56354  -4.36837  2.16197   1.000 44.95499  ? 3   ASP A CA  1 
ATOM   1715 C C   . ASP B 1 3   ? 5.51654  -3.64884  0.81099   1.000 46.94918  ? 3   ASP A C   1 
ATOM   1716 O O   . ASP B 1 3   ? 4.56474  -3.79807  0.05106   1.000 50.80066  ? 3   ASP A O   1 
ATOM   1717 C CB  . ASP B 1 3   ? 6.84119  -5.20482  2.26033   1.000 45.53918  ? 3   ASP A CB  1 
ATOM   1718 C CG  . ASP B 1 3   ? 7.15965  -5.65620  3.68287   1.000 48.70474  ? 3   ASP A CG  1 
ATOM   1719 O OD1 . ASP B 1 3   ? 6.58153  -5.11464  4.65941   1.000 44.41601  ? 3   ASP A OD1 1 
ATOM   1720 O OD2 . ASP B 1 3   ? 8.01252  -6.56943  3.81563   1.000 50.24805  ? 3   ASP A OD2 1 
ATOM   1721 N N   . PHE B 1 4   ? 6.54740  -2.86839  0.47703   1.000 43.76804  ? 4   PHE A N   1 
ATOM   1722 C CA  . PHE B 1 4   ? 6.56822  -2.23753  -0.84191  1.000 45.72076  ? 4   PHE A CA  1 
ATOM   1723 C C   . PHE B 1 4   ? 7.99441  -1.95120  -1.30349  1.000 43.90654  ? 4   PHE A C   1 
ATOM   1724 O O   . PHE B 1 4   ? 8.91677  -1.79814  -0.49786  1.000 48.77643  ? 4   PHE A O   1 
ATOM   1725 C CB  . PHE B 1 4   ? 5.75513  -0.93233  -0.88099  1.000 42.86245  ? 4   PHE A CB  1 
ATOM   1726 C CG  . PHE B 1 4   ? 6.29795  0.13067   0.01378   1.000 45.72025  ? 4   PHE A CG  1 
ATOM   1727 C CD1 . PHE B 1 4   ? 5.96584  0.15124   1.36056   1.000 43.87623  ? 4   PHE A CD1 1 
ATOM   1728 C CD2 . PHE B 1 4   ? 7.16935  1.09808   -0.47866  1.000 44.55893  ? 4   PHE A CD2 1 
ATOM   1729 C CE1 . PHE B 1 4   ? 6.47598  1.12369   2.20362   1.000 43.68464  ? 4   PHE A CE1 1 
ATOM   1730 C CE2 . PHE B 1 4   ? 7.68252  2.08188   0.35974   1.000 41.94023  ? 4   PHE A CE2 1 
ATOM   1731 C CZ  . PHE B 1 4   ? 7.33575  2.09579   1.69869   1.000 44.31256  ? 4   PHE A CZ  1 
ATOM   1732 N N   . ILE B 1 5   ? 8.14636  -1.87495  -2.62142  1.000 43.19398  ? 5   ILE A N   1 
ATOM   1733 C CA  . ILE B 1 5   ? 9.37902  -1.50004  -3.29355  1.000 42.73602  ? 5   ILE A CA  1 
ATOM   1734 C C   . ILE B 1 5   ? 9.17754  -0.13654  -3.94838  1.000 44.97139  ? 5   ILE A C   1 
ATOM   1735 O O   . ILE B 1 5   ? 8.05603  0.23591   -4.32015  1.000 43.09218  ? 5   ILE A O   1 
ATOM   1736 C CB  . ILE B 1 5   ? 9.77524  -2.56448  -4.34042  1.000 44.36461  ? 5   ILE A CB  1 
ATOM   1737 C CG1 . ILE B 1 5   ? 11.21759 -2.33920  -4.82460  1.000 45.66477  ? 5   ILE A CG1 1 
ATOM   1738 C CG2 . ILE B 1 5   ? 8.79039  -2.54661  -5.50722  1.000 39.41614  ? 5   ILE A CG2 1 
ATOM   1739 C CD1 . ILE B 1 5   ? 11.85180 -3.54808  -5.52273  1.000 42.30503  ? 5   ILE A CD1 1 
ATOM   1740 N N   . ILE B 1 6   ? 10.27233 0.62387   -4.07446  1.000 41.38278  ? 6   ILE A N   1 
ATOM   1741 C CA  . ILE B 1 6   ? 10.27174 1.87510   -4.82581  1.000 41.32385  ? 6   ILE A CA  1 
ATOM   1742 C C   . ILE B 1 6   ? 11.55309 1.94006   -5.64066  1.000 39.02176  ? 6   ILE A C   1 
ATOM   1743 O O   . ILE B 1 6   ? 12.55865 1.32261   -5.28238  1.000 42.06976  ? 6   ILE A O   1 
ATOM   1744 C CB  . ILE B 1 6   ? 10.14945 3.13483   -3.92646  1.000 36.25783  ? 6   ILE A CB  1 
ATOM   1745 C CG1 . ILE B 1 6   ? 11.34572 3.26189   -2.99267  1.000 36.04525  ? 6   ILE A CG1 1 
ATOM   1746 C CG2 . ILE B 1 6   ? 8.82279  3.14911   -3.15985  1.000 40.17105  ? 6   ILE A CG2 1 
ATOM   1747 C CD1 . ILE B 1 6   ? 11.52902 4.66089   -2.43123  1.000 32.37727  ? 6   ILE A CD1 1 
ATOM   1748 N N   . ASP B 1 7   ? 11.51552 2.69533   -6.74235  1.000 33.81822  ? 7   ASP A N   1 
ATOM   1749 C CA  . ASP B 1 7   ? 12.70313 2.88977   -7.56261  1.000 40.13228  ? 7   ASP A CA  1 
ATOM   1750 C C   . ASP B 1 7   ? 12.55279 4.15131   -8.38896  1.000 42.52957  ? 7   ASP A C   1 
ATOM   1751 O O   . ASP B 1 7   ? 11.60609 4.25902   -9.17397  1.000 41.16795  ? 7   ASP A O   1 
ATOM   1752 C CB  . ASP B 1 7   ? 12.96799 1.73263   -8.51936  1.000 36.99099  ? 7   ASP A CB  1 
ATOM   1753 C CG  . ASP B 1 7   ? 14.36233 1.82126   -9.14299  1.000 37.99065  ? 7   ASP A CG  1 
ATOM   1754 O OD1 . ASP B 1 7   ? 15.30096 1.52852   -8.38570  1.000 39.70859  ? 7   ASP A OD1 1 
ATOM   1755 O OD2 . ASP B 1 7   ? 14.52193 2.21639   -10.33242 1.000 38.21059  ? 7   ASP A OD2 1 
ATOM   1756 N N   . PHE B 1 8   ? 13.53091 5.05515   -8.26730  1.000 41.46856  ? 8   PHE A N   1 
ATOM   1757 C CA  . PHE B 1 8   ? 13.57423 6.32079   -8.99666  1.000 40.96991  ? 8   PHE A CA  1 
ATOM   1758 C C   . PHE B 1 8   ? 14.49516 6.22526   -10.20811 1.000 41.05286  ? 8   PHE A C   1 
ATOM   1759 O O   . PHE B 1 8   ? 15.56128 5.60114   -10.14423 1.000 36.72541  ? 8   PHE A O   1 
ATOM   1760 C CB  . PHE B 1 8   ? 14.09314 7.45473   -8.10744  1.000 33.79779  ? 8   PHE A CB  1 
ATOM   1761 C CG  . PHE B 1 8   ? 13.05726 8.06355   -7.24324  1.000 36.34644  ? 8   PHE A CG  1 
ATOM   1762 C CD1 . PHE B 1 8   ? 12.10403 8.91792   -7.77334  1.000 36.61109  ? 8   PHE A CD1 1 
ATOM   1763 C CD2 . PHE B 1 8   ? 13.03091 7.79589   -5.88421  1.000 39.13622  ? 8   PHE A CD2 1 
ATOM   1764 C CE1 . PHE B 1 8   ? 11.14704 9.49068   -6.95507  1.000 35.91815  ? 8   PHE A CE1 1 
ATOM   1765 C CE2 . PHE B 1 8   ? 12.06243 8.36843   -5.06140  1.000 35.33428  ? 8   PHE A CE2 1 
ATOM   1766 C CZ  . PHE B 1 8   ? 11.12299 9.20953   -5.60171  1.000 31.24145  ? 8   PHE A CZ  1 
ATOM   1767 N N   . GLU B 1 9   ? 14.10511 6.89595   -11.28936 1.000 37.98701  ? 9   GLU A N   1 
ATOM   1768 C CA  . GLU B 1 9   ? 15.04078 7.32204   -12.31444 1.000 35.93864  ? 9   GLU A CA  1 
ATOM   1769 C C   . GLU B 1 9   ? 15.23227 8.82530   -12.14161 1.000 40.44243  ? 9   GLU A C   1 
ATOM   1770 O O   . GLU B 1 9   ? 14.26098 9.53502   -11.85712 1.000 35.58598  ? 9   GLU A O   1 
ATOM   1771 C CB  . GLU B 1 9   ? 14.51869 6.97409   -13.70748 1.000 40.08808  ? 9   GLU A CB  1 
ATOM   1772 C CG  . GLU B 1 9   ? 14.40586 5.46414   -14.00184 1.000 41.87266  ? 9   GLU A CG  1 
ATOM   1773 C CD  . GLU B 1 9   ? 15.54181 4.58371   -13.43727 1.000 37.88662  ? 9   GLU A CD  1 
ATOM   1774 O OE1 . GLU B 1 9   ? 16.65901 4.65371   -13.94223 1.000 40.94986  ? 9   GLU A OE1 1 
ATOM   1775 O OE2 . GLU B 1 9   ? 15.31057 3.79300   -12.50224 1.000 46.68980  ? 9   GLU A OE2 1 
ATOM   1776 N N   . THR B 1 10  ? 16.49263 9.30349   -12.23361 1.000 36.48256  ? 10  THR A N   1 
ATOM   1777 C CA  . THR B 1 10  ? 16.83157 10.68790  -11.88436 1.000 34.28335  ? 10  THR A CA  1 
ATOM   1778 C C   . THR B 1 10  ? 17.80951 11.30328  -12.88084 1.000 37.14512  ? 10  THR A C   1 
ATOM   1779 O O   . THR B 1 10  ? 18.39612 10.62281  -13.73355 1.000 33.53290  ? 10  THR A O   1 
ATOM   1780 C CB  . THR B 1 10  ? 17.47166 10.82585  -10.49811 1.000 33.40719  ? 10  THR A CB  1 
ATOM   1781 O OG1 . THR B 1 10  ? 18.81031 10.28767  -10.52971 1.000 40.04144  ? 10  THR A OG1 1 
ATOM   1782 C CG2 . THR B 1 10  ? 16.65494 10.13041  -9.41302  1.000 28.83888  ? 10  THR A CG2 1 
ATOM   1783 N N   . MET B 1 11  ? 17.97939 12.62335  -12.75433 1.000 31.99239  ? 11  MET A N   1 
ATOM   1784 C CA  . MET B 1 11  ? 19.00310 13.35489  -13.48456 1.000 39.34120  ? 11  MET A CA  1 
ATOM   1785 C C   . MET B 1 11  ? 20.13442 13.84512  -12.58644 1.000 41.78710  ? 11  MET A C   1 
ATOM   1786 O O   . MET B 1 11  ? 20.92201 14.69121  -13.00804 1.000 47.20509  ? 11  MET A O   1 
ATOM   1787 C CB  . MET B 1 11  ? 18.41533 14.53891  -14.23293 1.000 36.89296  ? 11  MET A CB  1 
ATOM   1788 C CG  . MET B 1 11  ? 17.63345 14.17815  -15.43505 1.000 39.13899  ? 11  MET A CG  1 
ATOM   1789 S SD  . MET B 1 11  ? 18.67457 14.18620  -16.87597 1.000 50.21400  ? 11  MET A SD  1 
ATOM   1790 C CE  . MET B 1 11  ? 17.61601 13.33462  -18.05238 1.000 43.37632  ? 11  MET A CE  1 
ATOM   1791 N N   . GLY B 1 12  ? 20.24872 13.31739  -11.37809 1.000 41.03837  ? 12  GLY A N   1 
ATOM   1792 C CA  . GLY B 1 12  ? 21.28498 13.75280  -10.46445 1.000 41.71256  ? 12  GLY A CA  1 
ATOM   1793 C C   . GLY B 1 12  ? 21.31924 12.81185  -9.28813  1.000 42.70622  ? 12  GLY A C   1 
ATOM   1794 O O   . GLY B 1 12  ? 20.59773 11.80976  -9.26382  1.000 39.95670  ? 12  GLY A O   1 
ATOM   1795 N N   . SER B 1 13  ? 22.12487 13.16373  -8.27074  1.000 40.92220  ? 13  SER A N   1 
ATOM   1796 C CA  . SER B 1 13  ? 22.47573 12.14008  -7.29094  1.000 45.26687  ? 13  SER A CA  1 
ATOM   1797 C C   . SER B 1 13  ? 22.01484 12.40193  -5.86112  1.000 44.49143  ? 13  SER A C   1 
ATOM   1798 O O   . SER B 1 13  ? 21.74521 11.43166  -5.14320  1.000 53.46501  ? 13  SER A O   1 
ATOM   1799 C CB  . SER B 1 13  ? 24.00445 11.89389  -7.28689  1.000 48.37367  ? 13  SER A CB  1 
ATOM   1800 O OG  . SER B 1 13  ? 24.73275 13.12112  -7.37234  1.000 54.46398  ? 13  SER A OG  1 
ATOM   1801 N N   . GLY B 1 14  ? 21.94372 13.63880  -5.39385  1.000 34.60859  ? 14  GLY A N   1 
ATOM   1802 C CA  . GLY B 1 14  ? 21.59277 13.84825  -3.99685  1.000 36.83552  ? 14  GLY A CA  1 
ATOM   1803 C C   . GLY B 1 14  ? 20.07898 13.83008  -3.71783  1.000 38.75158  ? 14  GLY A C   1 
ATOM   1804 O O   . GLY B 1 14  ? 19.24936 13.54309  -4.58003  1.000 35.76521  ? 14  GLY A O   1 
ATOM   1805 N N   . GLU B 1 15  ? 19.72357 14.18907  -2.47834  1.000 37.93375  ? 15  GLU A N   1 
ATOM   1806 C CA  . GLU B 1 15  ? 18.30856 14.20211  -2.10581  1.000 34.30463  ? 15  GLU A CA  1 
ATOM   1807 C C   . GLU B 1 15  ? 17.49562 15.22607  -2.88725  1.000 35.94837  ? 15  GLU A C   1 
ATOM   1808 O O   . GLU B 1 15  ? 16.26482 15.11423  -2.91120  1.000 39.44422  ? 15  GLU A O   1 
ATOM   1809 C CB  . GLU B 1 15  ? 18.13357 14.41279  -0.59092  1.000 32.14151  ? 15  GLU A CB  1 
ATOM   1810 C CG  . GLU B 1 15  ? 18.11892 15.83977  -0.14036  1.000 35.53725  ? 15  GLU A CG  1 
ATOM   1811 C CD  . GLU B 1 15  ? 18.19880 15.99061  1.36485   1.000 36.67740  ? 15  GLU A CD  1 
ATOM   1812 O OE1 . GLU B 1 15  ? 18.23879 14.98259  2.08363   1.000 37.11061  ? 15  GLU A OE1 1 
ATOM   1813 O OE2 . GLU B 1 15  ? 18.15229 17.12983  1.84998   1.000 42.35419  ? 15  GLU A OE2 1 
ATOM   1814 N N   . LYS B 1 16  ? 18.12924 16.18870  -3.56470  1.000 34.62273  ? 16  LYS A N   1 
ATOM   1815 C CA  . LYS B 1 16  ? 17.39726 17.15663  -4.38156  1.000 36.14363  ? 16  LYS A CA  1 
ATOM   1816 C C   . LYS B 1 16  ? 17.44190 16.81075  -5.86777  1.000 38.52769  ? 16  LYS A C   1 
ATOM   1817 O O   . LYS B 1 16  ? 17.15382 17.67131  -6.71127  1.000 36.78685  ? 16  LYS A O   1 
ATOM   1818 C CB  . LYS B 1 16  ? 17.92097 18.58834  -4.16499  1.000 36.76975  ? 16  LYS A CB  1 
ATOM   1819 C CG  . LYS B 1 16  ? 18.19665 18.97257  -2.69941  1.000 39.87255  ? 16  LYS A CG  1 
ATOM   1820 C CD  . LYS B 1 16  ? 16.90500 19.22758  -1.89906  1.000 36.80582  ? 16  LYS A CD  1 
ATOM   1821 C CE  . LYS B 1 16  ? 15.90602 20.12052  -2.66443  1.000 42.16980  ? 16  LYS A CE  1 
ATOM   1822 N NZ  . LYS B 1 16  ? 14.53172 20.10160  -2.03917  1.000 43.53645  ? 16  LYS A NZ  1 
ATOM   1823 N N   . ALA B 1 17  ? 17.78966 15.57027  -6.20635  1.000 38.54664  ? 17  ALA A N   1 
ATOM   1824 C CA  . ALA B 1 17  ? 17.96425 15.21713  -7.60886  1.000 41.27612  ? 17  ALA A CA  1 
ATOM   1825 C C   . ALA B 1 17  ? 16.64162 15.28863  -8.37152  1.000 40.11160  ? 17  ALA A C   1 
ATOM   1826 O O   . ALA B 1 17  ? 15.62151 14.72451  -7.93824  1.000 37.59413  ? 17  ALA A O   1 
ATOM   1827 C CB  . ALA B 1 17  ? 18.57462 13.82900  -7.73786  1.000 34.95495  ? 17  ALA A CB  1 
ATOM   1828 N N   . ALA B 1 18  ? 16.66995 16.01918  -9.49466  1.000 38.68603  ? 18  ALA A N   1 
ATOM   1829 C CA  . ALA B 1 18  ? 15.58785 15.99204  -10.47503 1.000 38.80157  ? 18  ALA A CA  1 
ATOM   1830 C C   . ALA B 1 18  ? 15.21469 14.55155  -10.77616 1.000 36.51779  ? 18  ALA A C   1 
ATOM   1831 O O   . ALA B 1 18  ? 16.08832 13.72632  -11.03864 1.000 36.03327  ? 18  ALA A O   1 
ATOM   1832 C CB  . ALA B 1 18  ? 16.02481 16.70692  -11.76254 1.000 41.29401  ? 18  ALA A CB  1 
ATOM   1833 N N   . VAL B 1 19  ? 13.91636 14.24608  -10.69970 1.000 39.51290  ? 19  VAL A N   1 
ATOM   1834 C CA  . VAL B 1 19  ? 13.40281 12.87746  -10.79110 1.000 35.73241  ? 19  VAL A CA  1 
ATOM   1835 C C   . VAL B 1 19  ? 12.69539 12.68190  -12.12798 1.000 39.03917  ? 19  VAL A C   1 
ATOM   1836 O O   . VAL B 1 19  ? 11.88549 13.52201  -12.54157 1.000 33.01295  ? 19  VAL A O   1 
ATOM   1837 C CB  . VAL B 1 19  ? 12.44503 12.56987  -9.63337  1.000 38.64474  ? 19  VAL A CB  1 
ATOM   1838 C CG1 . VAL B 1 19  ? 13.22348 12.25559  -8.36177  1.000 35.66924  ? 19  VAL A CG1 1 
ATOM   1839 C CG2 . VAL B 1 19  ? 11.44218 13.73328  -9.44163  1.000 32.17679  ? 19  VAL A CG2 1 
ATOM   1840 N N   . ILE B 1 20  ? 12.99225 11.56599  -12.79447 1.000 41.36801  ? 20  ILE A N   1 
ATOM   1841 C CA  . ILE B 1 20  ? 12.37933 11.22567  -14.07988 1.000 39.88166  ? 20  ILE A CA  1 
ATOM   1842 C C   . ILE B 1 20  ? 11.12848 10.38243  -13.89348 1.000 39.20365  ? 20  ILE A C   1 
ATOM   1843 O O   . ILE B 1 20  ? 10.09333 10.64573  -14.50881 1.000 39.39489  ? 20  ILE A O   1 
ATOM   1844 C CB  . ILE B 1 20  ? 13.37964 10.48920  -14.99999 1.000 42.14245  ? 20  ILE A CB  1 
ATOM   1845 C CG1 . ILE B 1 20  ? 14.68446 11.25877  -15.16386 1.000 41.05879  ? 20  ILE A CG1 1 
ATOM   1846 C CG2 . ILE B 1 20  ? 12.72261 10.20284  -16.32940 1.000 44.19755  ? 20  ILE A CG2 1 
ATOM   1847 C CD1 . ILE B 1 20  ? 15.67027 10.54140  -16.04848 1.000 41.37213  ? 20  ILE A CD1 1 
ATOM   1848 N N   . ASP B 1 21  ? 11.21416 9.32755   -13.09287 1.000 36.43202  ? 21  ASP A N   1 
ATOM   1849 C CA  . ASP B 1 21  ? 10.03720 8.53522   -12.78322 1.000 42.43202  ? 21  ASP A CA  1 
ATOM   1850 C C   . ASP B 1 21  ? 10.23077 7.89309   -11.41735 1.000 42.97042  ? 21  ASP A C   1 
ATOM   1851 O O   . ASP B 1 21  ? 11.30915 7.96321   -10.81615 1.000 41.97038  ? 21  ASP A O   1 
ATOM   1852 C CB  . ASP B 1 21  ? 9.69668  7.50350   -13.89866 1.000 41.15522  ? 21  ASP A CB  1 
ATOM   1853 C CG  . ASP B 1 21  ? 10.63048 6.25843   -13.93481 1.000 43.72747  ? 21  ASP A CG  1 
ATOM   1854 O OD1 . ASP B 1 21  ? 11.33763 5.94284   -12.95917 1.000 44.43811  ? 21  ASP A OD1 1 
ATOM   1855 O OD2 . ASP B 1 21  ? 10.60642 5.54332   -14.96696 1.000 43.95637  ? 21  ASP A OD2 1 
ATOM   1856 N N   . LEU B 1 22  ? 9.15255  7.27890   -10.93424 1.000 40.64577  ? 22  LEU A N   1 
ATOM   1857 C CA  . LEU B 1 22  ? 9.11301  6.62477   -9.63093  1.000 39.26944  ? 22  LEU A CA  1 
ATOM   1858 C C   . LEU B 1 22  ? 8.16976  5.43742   -9.77065  1.000 43.55705  ? 22  LEU A C   1 
ATOM   1859 O O   . LEU B 1 22  ? 6.96132  5.62824   -9.95231  1.000 40.83866  ? 22  LEU A O   1 
ATOM   1860 C CB  . LEU B 1 22  ? 8.62264  7.58790   -8.53846  1.000 36.32583  ? 22  LEU A CB  1 
ATOM   1861 C CG  . LEU B 1 22  ? 8.19342  6.93372   -7.20567  1.000 39.43705  ? 22  LEU A CG  1 
ATOM   1862 C CD1 . LEU B 1 22  ? 9.30338  6.04253   -6.65048  1.000 36.73511  ? 22  LEU A CD1 1 
ATOM   1863 C CD2 . LEU B 1 22  ? 7.76184  7.95841   -6.15588  1.000 38.61342  ? 22  LEU A CD2 1 
ATOM   1864 N N   . ALA B 1 23  ? 8.70858  4.22565   -9.69381  1.000 42.17259  ? 23  ALA A N   1 
ATOM   1865 C CA  . ALA B 1 23  ? 7.89609  3.02202   -9.71361  1.000 40.78486  ? 23  ALA A CA  1 
ATOM   1866 C C   . ALA B 1 23  ? 7.76523  2.48927   -8.29476  1.000 44.02535  ? 23  ALA A C   1 
ATOM   1867 O O   . ALA B 1 23  ? 8.69083  2.61969   -7.48476  1.000 45.13878  ? 23  ALA A O   1 
ATOM   1868 C CB  . ALA B 1 23  ? 8.49846  1.96772   -10.63686 1.000 42.66403  ? 23  ALA A CB  1 
ATOM   1869 N N   . VAL B 1 24  ? 6.60083  1.92476   -7.98736  1.000 41.82057  ? 24  VAL A N   1 
ATOM   1870 C CA  . VAL B 1 24  ? 6.31244  1.39104   -6.65730  1.000 44.93623  ? 24  VAL A CA  1 
ATOM   1871 C C   . VAL B 1 24  ? 5.38439  0.19473   -6.81505  1.000 49.47491  ? 24  VAL A C   1 
ATOM   1872 O O   . VAL B 1 24  ? 4.51799  0.18519   -7.69522  1.000 48.95669  ? 24  VAL A O   1 
ATOM   1873 C CB  . VAL B 1 24  ? 5.71637  2.47910   -5.73072  1.000 44.39736  ? 24  VAL A CB  1 
ATOM   1874 C CG1 . VAL B 1 24  ? 4.58493  3.17177   -6.39228  1.000 49.37381  ? 24  VAL A CG1 1 
ATOM   1875 C CG2 . VAL B 1 24  ? 5.20959  1.88004   -4.42689  1.000 45.82617  ? 24  VAL A CG2 1 
ATOM   1876 N N   . ILE B 1 25  ? 5.60931  -0.83914  -5.99424  1.000 46.82634  ? 25  ILE A N   1 
ATOM   1877 C CA  . ILE B 1 25  ? 4.78567  -2.04431  -5.97180  1.000 49.68313  ? 25  ILE A CA  1 
ATOM   1878 C C   . ILE B 1 25  ? 4.68777  -2.55240  -4.54034  1.000 50.34954  ? 25  ILE A C   1 
ATOM   1879 O O   . ILE B 1 25  ? 5.70705  -2.70531  -3.85955  1.000 49.41959  ? 25  ILE A O   1 
ATOM   1880 C CB  . ILE B 1 25  ? 5.33325  -3.17238  -6.86927  1.000 52.41561  ? 25  ILE A CB  1 
ATOM   1881 C CG1 . ILE B 1 25  ? 5.69476  -2.67728  -8.27299  1.000 49.19984  ? 25  ILE A CG1 1 
ATOM   1882 C CG2 . ILE B 1 25  ? 4.33187  -4.32210  -6.92716  1.000 54.08010  ? 25  ILE A CG2 1 
ATOM   1883 C CD1 . ILE B 1 25  ? 6.41385  -3.74321  -9.11722  1.000 50.12335  ? 25  ILE A CD1 1 
ATOM   1884 N N   . ALA B 1 26  ? 3.46318  -2.81712  -4.08929  1.000 50.31092  ? 26  ALA A N   1 
ATOM   1885 C CA  . ALA B 1 26  ? 3.23940  -3.51361  -2.82799  1.000 53.89153  ? 26  ALA A CA  1 
ATOM   1886 C C   . ALA B 1 26  ? 3.27073  -5.01903  -3.05833  1.000 55.36879  ? 26  ALA A C   1 
ATOM   1887 O O   . ALA B 1 26  ? 2.83959  -5.50479  -4.10952  1.000 54.64080  ? 26  ALA A O   1 
ATOM   1888 C CB  . ALA B 1 26  ? 1.89419  -3.11338  -2.21341  1.000 54.36478  ? 26  ALA A CB  1 
ATOM   1889 N N   . PHE B 1 27  ? 3.77263  -5.75656  -2.06746  1.000 50.14317  ? 27  PHE A N   1 
ATOM   1890 C CA  . PHE B 1 27  ? 3.98486  -7.18770  -2.22266  1.000 52.44714  ? 27  PHE A CA  1 
ATOM   1891 C C   . PHE B 1 27  ? 3.89348  -7.87529  -0.86761  1.000 54.68137  ? 27  PHE A C   1 
ATOM   1892 O O   . PHE B 1 27  ? 3.88501  -7.23632  0.19022   1.000 56.57264  ? 27  PHE A O   1 
ATOM   1893 C CB  . PHE B 1 27  ? 5.33302  -7.50379  -2.88822  1.000 53.85753  ? 27  PHE A CB  1 
ATOM   1894 C CG  . PHE B 1 27  ? 6.54589  -7.25869  -2.01547  1.000 49.88663  ? 27  PHE A CG  1 
ATOM   1895 C CD1 . PHE B 1 27  ? 7.17447  -6.02036  -1.99939  1.000 49.27154  ? 27  PHE A CD1 1 
ATOM   1896 C CD2 . PHE B 1 27  ? 7.08636  -8.28993  -1.24321  1.000 51.14476  ? 27  PHE A CD2 1 
ATOM   1897 C CE1 . PHE B 1 27  ? 8.33772  -5.80406  -1.22504  1.000 49.36601  ? 27  PHE A CE1 1 
ATOM   1898 C CE2 . PHE B 1 27  ? 8.24727  -8.08253  -0.45212  1.000 53.20108  ? 27  PHE A CE2 1 
ATOM   1899 C CZ  . PHE B 1 27  ? 8.87136  -6.83557  -0.44720  1.000 47.26486  ? 27  PHE A CZ  1 
ATOM   1900 N N   . ASP B 1 28  ? 3.82601  -9.20003  -0.91730  1.000 54.21320  ? 28  ASP A N   1 
ATOM   1901 C CA  . ASP B 1 28  ? 3.57336  -9.98461  0.27054   1.000 58.39355  ? 28  ASP A CA  1 
ATOM   1902 C C   . ASP B 1 28  ? 4.89088  -10.53450 0.76384   1.000 55.37949  ? 28  ASP A C   1 
ATOM   1903 O O   . ASP B 1 28  ? 5.56192  -11.26187 0.01891   1.000 58.85662  ? 28  ASP A O   1 
ATOM   1904 C CB  . ASP B 1 28  ? 2.59654  -11.12376 -0.01619  1.000 59.00522  ? 28  ASP A CB  1 
ATOM   1905 C CG  . ASP B 1 28  ? 2.05189  -11.76344 1.25490   1.000 59.94272  ? 28  ASP A CG  1 
ATOM   1906 O OD1 . ASP B 1 28  ? 2.80861  -11.94741 2.23161   1.000 57.86933  ? 28  ASP A OD1 1 
ATOM   1907 O OD2 . ASP B 1 28  ? 0.85179  -12.09322 1.27774   1.000 67.61130  ? 28  ASP A OD2 1 
ATOM   1908 N N   . PRO B 1 29  ? 5.30648  -10.20244 1.98712   1.000 59.64348  ? 29  PRO A N   1 
ATOM   1909 C CA  . PRO B 1 29  ? 6.59330  -10.69612 2.49572   1.000 58.59938  ? 29  PRO A CA  1 
ATOM   1910 C C   . PRO B 1 29  ? 6.57525  -12.15148 2.94352   1.000 59.40225  ? 29  PRO A C   1 
ATOM   1911 O O   . PRO B 1 29  ? 7.64959  -12.69511 3.22964   1.000 64.32359  ? 29  PRO A O   1 
ATOM   1912 C CB  . PRO B 1 29  ? 6.87152  -9.76135  3.68310   1.000 54.61095  ? 29  PRO A CB  1 
ATOM   1913 C CG  . PRO B 1 29  ? 5.49186  -9.33514  4.13845   1.000 56.75169  ? 29  PRO A CG  1 
ATOM   1914 C CD  . PRO B 1 29  ? 4.68767  -9.20474  2.88198   1.000 54.70473  ? 29  PRO A CD  1 
ATOM   1915 N N   . ASN B 1 30  ? 5.40932  -12.79436 3.01481   1.000 65.40182  ? 30  ASN A N   1 
ATOM   1916 C CA  . ASN B 1 30  ? 5.30095  -14.17607 3.48770   1.000 63.50506  ? 30  ASN A CA  1 
ATOM   1917 C C   . ASN B 1 30  ? 6.17053  -15.09409 2.63782   1.000 65.40282  ? 30  ASN A C   1 
ATOM   1918 O O   . ASN B 1 30  ? 5.94537  -15.19425 1.42023   1.000 68.25644  ? 30  ASN A O   1 
ATOM   1919 C CB  . ASN B 1 30  ? 3.84932  -14.64320 3.42943   1.000 67.70453  ? 30  ASN A CB  1 
ATOM   1920 C CG  . ASN B 1 30  ? 3.61362  -15.94486 4.18419   1.000 70.65191  ? 30  ASN A CG  1 
ATOM   1921 O OD1 . ASN B 1 30  ? 4.37910  -16.90211 4.06078   1.000 72.55132  ? 30  ASN A OD1 1 
ATOM   1922 N ND2 . ASN B 1 30  ? 2.51617  -16.00178 4.92137   1.000 68.13771  ? 30  ASN A ND2 1 
ATOM   1923 N N   . PRO B 1 31  ? 7.14836  -15.78942 3.22247   1.000 67.03531  ? 31  PRO A N   1 
ATOM   1924 C CA  . PRO B 1 31  ? 8.05402  -16.61184 2.40034   1.000 66.56979  ? 31  PRO A CA  1 
ATOM   1925 C C   . PRO B 1 31  ? 7.34240  -17.71485 1.62969   1.000 76.33690  ? 31  PRO A C   1 
ATOM   1926 O O   . PRO B 1 31  ? 7.79184  -18.08612 0.53765   1.000 75.30174  ? 31  PRO A O   1 
ATOM   1927 C CB  . PRO B 1 31  ? 9.03393  -17.19552 3.42693   1.000 64.76520  ? 31  PRO A CB  1 
ATOM   1928 C CG  . PRO B 1 31  ? 8.82314  -16.40021 4.68107   1.000 68.71502  ? 31  PRO A CG  1 
ATOM   1929 C CD  . PRO B 1 31  ? 7.40251  -15.95242 4.65995   1.000 68.55502  ? 31  PRO A CD  1 
ATOM   1930 N N   . GLU B 1 32  ? 6.24395  -18.25443 2.16527   1.000 77.27248  ? 32  GLU A N   1 
ATOM   1931 C CA  . GLU B 1 32  ? 5.49550  -19.29594 1.47295   1.000 77.85169  ? 32  GLU A CA  1 
ATOM   1932 C C   . GLU B 1 32  ? 4.57460  -18.75265 0.39129   1.000 76.28076  ? 32  GLU A C   1 
ATOM   1933 O O   . GLU B 1 32  ? 4.05118  -19.54463 -0.39710  1.000 78.45297  ? 32  GLU A O   1 
ATOM   1934 C CB  . GLU B 1 32  ? 4.68305  -20.12715 2.47222   1.000 78.04622  ? 32  GLU A CB  1 
ATOM   1935 C CG  . GLU B 1 32  ? 5.54696  -20.94993 3.41867   1.000 86.14908  ? 32  GLU A CG  1 
ATOM   1936 C CD  . GLU B 1 32  ? 4.73785  -21.77253 4.39907   1.000 92.78166  ? 32  GLU A CD  1 
ATOM   1937 O OE1 . GLU B 1 32  ? 3.58198  -22.12588 4.07195   1.000 100.17861 ? 32  GLU A OE1 1 
ATOM   1938 O OE2 . GLU B 1 32  ? 5.26837  -22.08533 5.48731   1.000 89.68023  ? 32  GLU A OE2 1 
ATOM   1939 N N   . VAL B 1 33  ? 4.36555  -17.44020 0.32628   1.000 73.60066  ? 33  VAL A N   1 
ATOM   1940 C CA  . VAL B 1 33  ? 3.56712  -16.82461 -0.72694  1.000 67.75478  ? 33  VAL A CA  1 
ATOM   1941 C C   . VAL B 1 33  ? 4.53111  -16.32894 -1.79528  1.000 69.59735  ? 33  VAL A C   1 
ATOM   1942 O O   . VAL B 1 33  ? 5.40008  -15.49198 -1.51760  1.000 67.52913  ? 33  VAL A O   1 
ATOM   1943 C CB  . VAL B 1 33  ? 2.69599  -15.67992 -0.18690  1.000 66.40741  ? 33  VAL A CB  1 
ATOM   1944 C CG1 . VAL B 1 33  ? 1.93650  -15.01279 -1.32890  1.000 63.28592  ? 33  VAL A CG1 1 
ATOM   1945 C CG2 . VAL B 1 33  ? 1.74920  -16.18699 0.88766   1.000 64.94561  ? 33  VAL A CG2 1 
ATOM   1946 N N   . VAL B 1 34  ? 4.38850  -16.85784 -3.01205  1.000 68.54533  ? 34  VAL A N   1 
ATOM   1947 C CA  . VAL B 1 34  ? 5.28607  -16.54751 -4.11920  1.000 65.25397  ? 34  VAL A CA  1 
ATOM   1948 C C   . VAL B 1 34  ? 4.52403  -15.77161 -5.18195  1.000 72.13478  ? 34  VAL A C   1 
ATOM   1949 O O   . VAL B 1 34  ? 4.05646  -16.35503 -6.16656  1.000 75.63141  ? 34  VAL A O   1 
ATOM   1950 C CB  . VAL B 1 34  ? 5.90463  -17.82518 -4.71620  1.000 59.41904  ? 34  VAL A CB  1 
ATOM   1951 N N   . GLU B 1 35  ? 4.38908  -14.45606 -4.99228  1.000 72.33265  ? 35  GLU A N   1 
ATOM   1952 C CA  . GLU B 1 35  ? 3.67850  -13.63184 -5.96342  1.000 70.69839  ? 35  GLU A CA  1 
ATOM   1953 C C   . GLU B 1 35  ? 4.43971  -13.64383 -7.28189  1.000 70.84658  ? 35  GLU A C   1 
ATOM   1954 O O   . GLU B 1 35  ? 5.66165  -13.47313 -7.30072  1.000 71.86438  ? 35  GLU A O   1 
ATOM   1955 C CB  . GLU B 1 35  ? 3.51044  -12.20304 -5.44205  1.000 67.55630  ? 35  GLU A CB  1 
ATOM   1956 N N   . THR B 1 36  ? 3.72416  -13.86341 -8.38241  1.000 69.56126  ? 36  THR A N   1 
ATOM   1957 C CA  . THR B 1 36  ? 4.36529  -14.04069 -9.67520  1.000 68.07225  ? 36  THR A CA  1 
ATOM   1958 C C   . THR B 1 36  ? 4.56825  -12.70830 -10.39003 1.000 65.60361  ? 36  THR A C   1 
ATOM   1959 O O   . THR B 1 36  ? 4.00564  -11.67102 -10.02082 1.000 62.98068  ? 36  THR A O   1 
ATOM   1960 C CB  . THR B 1 36  ? 3.55011  -14.97913 -10.56571 1.000 72.74763  ? 36  THR A CB  1 
ATOM   1961 O OG1 . THR B 1 36  ? 2.56553  -14.22045 -11.28215 1.000 70.29212  ? 36  THR A OG1 1 
ATOM   1962 C CG2 . THR B 1 36  ? 2.87273  -16.07691 -9.73785  1.000 74.94367  ? 36  THR A CG2 1 
ATOM   1963 N N   . PHE B 1 37  ? 5.36981  -12.77305 -11.45722 1.000 61.46663  ? 37  PHE A N   1 
ATOM   1964 C CA  . PHE B 1 37  ? 5.71816  -11.58592 -12.23052 1.000 63.82210  ? 37  PHE A CA  1 
ATOM   1965 C C   . PHE B 1 37  ? 4.47650  -10.81561 -12.66801 1.000 63.69263  ? 37  PHE A C   1 
ATOM   1966 O O   . PHE B 1 37  ? 4.37915  -9.59984  -12.45391 1.000 61.16955  ? 37  PHE A O   1 
ATOM   1967 C CB  . PHE B 1 37  ? 6.53729  -11.98905 -13.45379 1.000 63.63315  ? 37  PHE A CB  1 
ATOM   1968 C CG  . PHE B 1 37  ? 7.27366  -10.86085 -14.08392 1.000 61.19289  ? 37  PHE A CG  1 
ATOM   1969 C CD1 . PHE B 1 37  ? 8.23947  -10.16349 -13.37180 1.000 64.00893  ? 37  PHE A CD1 1 
ATOM   1970 C CD2 . PHE B 1 37  ? 6.99202  -10.47617 -15.38333 1.000 63.16917  ? 37  PHE A CD2 1 
ATOM   1971 C CE1 . PHE B 1 37  ? 8.93868  -9.11439  -13.95513 1.000 60.95342  ? 37  PHE A CE1 1 
ATOM   1972 C CE2 . PHE B 1 37  ? 7.67963  -9.42315  -15.97731 1.000 64.88851  ? 37  PHE A CE2 1 
ATOM   1973 C CZ  . PHE B 1 37  ? 8.66144  -8.74218  -15.25621 1.000 62.57459  ? 37  PHE A CZ  1 
ATOM   1974 N N   . ASP B 1 38  ? 3.50585  -11.51140 -13.27260 1.000 63.26073  ? 38  ASP A N   1 
ATOM   1975 C CA  . ASP B 1 38  ? 2.38861  -10.82144 -13.91342 1.000 63.00089  ? 38  ASP A CA  1 
ATOM   1976 C C   . ASP B 1 38  ? 1.54643  -10.06668 -12.89606 1.000 60.78459  ? 38  ASP A C   1 
ATOM   1977 O O   . ASP B 1 38  ? 1.15205  -8.91926  -13.13826 1.000 58.52528  ? 38  ASP A O   1 
ATOM   1978 C CB  . ASP B 1 38  ? 1.52371  -11.82109 -14.67586 1.000 63.13484  ? 38  ASP A CB  1 
ATOM   1979 N N   . GLU B 1 39  ? 1.25907  -10.68554 -11.74820 1.000 60.12658  ? 39  GLU A N   1 
ATOM   1980 C CA  . GLU B 1 39  ? 0.44271  -9.99833  -10.75197 1.000 64.99515  ? 39  GLU A CA  1 
ATOM   1981 C C   . GLU B 1 39  ? 1.21440  -8.85854  -10.09495 1.000 61.12286  ? 39  GLU A C   1 
ATOM   1982 O O   . GLU B 1 39  ? 0.64053  -7.80591  -9.80308  1.000 56.68387  ? 39  GLU A O   1 
ATOM   1983 C CB  . GLU B 1 39  ? -0.05970 -11.00240 -9.72127  1.000 64.41595  ? 39  GLU A CB  1 
ATOM   1984 C CG  . GLU B 1 39  ? 0.88087  -12.15443 -9.49664  1.000 69.59550  ? 39  GLU A CG  1 
ATOM   1985 C CD  . GLU B 1 39  ? 0.48629  -13.00672 -8.30657  1.000 78.47645  ? 39  GLU A CD  1 
ATOM   1986 O OE1 . GLU B 1 39  ? -0.46541 -12.63377 -7.58113  1.000 80.84207  ? 39  GLU A OE1 1 
ATOM   1987 O OE2 . GLU B 1 39  ? 1.14368  -14.04884 -8.08994  1.000 76.00038  ? 39  GLU A OE2 1 
ATOM   1988 N N   . LEU B 1 40  ? 2.51912  -9.04383  -9.86764  1.000 64.92330  ? 40  LEU A N   1 
ATOM   1989 C CA  . LEU B 1 40  ? 3.34342  -7.95139  -9.35675  1.000 59.58527  ? 40  LEU A CA  1 
ATOM   1990 C C   . LEU B 1 40  ? 3.31149  -6.75556  -10.29989 1.000 56.56672  ? 40  LEU A C   1 
ATOM   1991 O O   . LEU B 1 40  ? 3.03321  -5.62489  -9.88392  1.000 52.44876  ? 40  LEU A O   1 
ATOM   1992 C CB  . LEU B 1 40  ? 4.77300  -8.43292  -9.15228  1.000 54.69986  ? 40  LEU A CB  1 
ATOM   1993 C CG  . LEU B 1 40  ? 4.95464  -9.37683  -7.96906  1.000 56.30007  ? 40  LEU A CG  1 
ATOM   1994 C CD1 . LEU B 1 40  ? 6.40145  -9.86962  -7.88206  1.000 53.93782  ? 40  LEU A CD1 1 
ATOM   1995 C CD2 . LEU B 1 40  ? 4.50407  -8.71223  -6.67389  1.000 56.06710  ? 40  LEU A CD2 1 
ATOM   1996 N N   . VAL B 1 41  ? 3.58533  -6.99639  -11.58222 1.000 57.04435  ? 41  VAL A N   1 
ATOM   1997 C CA  . VAL B 1 41  ? 3.53546  -5.93348  -12.57977 1.000 55.38468  ? 41  VAL A CA  1 
ATOM   1998 C C   . VAL B 1 41  ? 2.16711  -5.26874  -12.59876 1.000 58.60089  ? 41  VAL A C   1 
ATOM   1999 O O   . VAL B 1 41  ? 2.06511  -4.04341  -12.73239 1.000 60.39261  ? 41  VAL A O   1 
ATOM   2000 C CB  . VAL B 1 41  ? 3.91971  -6.49390  -13.95950 1.000 54.62210  ? 41  VAL A CB  1 
ATOM   2001 C CG1 . VAL B 1 41  ? 3.58451  -5.49366  -15.04677 1.000 57.05097  ? 41  VAL A CG1 1 
ATOM   2002 C CG2 . VAL B 1 41  ? 5.40894  -6.84824  -13.98182 1.000 56.85447  ? 41  VAL A CG2 1 
ATOM   2003 N N   . SER B 1 42  ? 1.09338  -6.05690  -12.44190 1.000 59.89021  ? 42  SER A N   1 
ATOM   2004 C CA  . SER B 1 42  ? -0.25904 -5.49400  -12.49917 1.000 58.71162  ? 42  SER A CA  1 
ATOM   2005 C C   . SER B 1 42  ? -0.56824 -4.65095  -11.26876 1.000 55.78638  ? 42  SER A C   1 
ATOM   2006 O O   . SER B 1 42  ? -1.26075 -3.62817  -11.36238 1.000 54.48545  ? 42  SER A O   1 
ATOM   2007 C CB  . SER B 1 42  ? -1.29449 -6.61309  -12.63577 1.000 61.86751  ? 42  SER A CB  1 
ATOM   2008 O OG  . SER B 1 42  ? -1.55799 -6.88922  -13.99947 1.000 71.36833  ? 42  SER A OG  1 
ATOM   2009 N N   . ARG B 1 43  ? -0.09490 -5.08141  -10.10081 1.000 55.17694  ? 43  ARG A N   1 
ATOM   2010 C CA  . ARG B 1 43  ? -0.31543 -4.31638  -8.88522  1.000 54.35148  ? 43  ARG A CA  1 
ATOM   2011 C C   . ARG B 1 43  ? 0.49977  -3.03402  -8.86213  1.000 53.66153  ? 43  ARG A C   1 
ATOM   2012 O O   . ARG B 1 43  ? 0.23069  -2.15997  -8.03226  1.000 55.02725  ? 43  ARG A O   1 
ATOM   2013 C CB  . ARG B 1 43  ? 0.02855  -5.16825  -7.66428  1.000 51.46074  ? 43  ARG A CB  1 
ATOM   2014 C CG  . ARG B 1 43  ? -0.62408 -4.70943  -6.37874  1.000 51.02187  ? 43  ARG A CG  1 
ATOM   2015 C CD  . ARG B 1 43  ? -0.94799 -5.91690  -5.50718  1.000 60.09599  ? 43  ARG A CD  1 
ATOM   2016 N NE  . ARG B 1 43  ? 0.25372  -6.70564  -5.28027  1.000 59.95570  ? 43  ARG A NE  1 
ATOM   2017 C CZ  . ARG B 1 43  ? 0.29297  -8.01327  -5.07737  1.000 58.46429  ? 43  ARG A CZ  1 
ATOM   2018 N NH1 . ARG B 1 43  ? -0.80390 -8.74717  -5.07496  1.000 54.86913  ? 43  ARG A NH1 1 
ATOM   2019 N NH2 . ARG B 1 43  ? 1.46841  -8.59715  -4.85417  1.000 61.29629  ? 43  ARG A NH2 1 
ATOM   2020 N N   . GLY B 1 44  ? 1.46935  -2.89645  -9.75142  1.000 54.88926  ? 44  GLY A N   1 
ATOM   2021 C CA  . GLY B 1 44  ? 2.40781  -1.80147  -9.66608  1.000 54.58061  ? 44  GLY A CA  1 
ATOM   2022 C C   . GLY B 1 44  ? 1.95761  -0.57549  -10.42512 1.000 54.80422  ? 44  GLY A C   1 
ATOM   2023 O O   . GLY B 1 44  ? 1.12047  -0.64832  -11.32252 1.000 63.00421  ? 44  GLY A O   1 
ATOM   2024 N N   . ILE B 1 45  ? 2.49689  0.57410   -10.02185 1.000 49.11283  ? 45  ILE A N   1 
ATOM   2025 C CA  . ILE B 1 45  ? 2.28189  1.82658   -10.73017 1.000 49.06356  ? 45  ILE A CA  1 
ATOM   2026 C C   . ILE B 1 45  ? 3.62293  2.50662   -11.01064 1.000 51.51616  ? 45  ILE A C   1 
ATOM   2027 O O   . ILE B 1 45  ? 4.64816  2.24232   -10.37218 1.000 42.77738  ? 45  ILE A O   1 
ATOM   2028 C CB  . ILE B 1 45  ? 1.34776  2.77774   -9.96571  1.000 48.58520  ? 45  ILE A CB  1 
ATOM   2029 C CG1 . ILE B 1 45  ? 2.04871  3.34720   -8.74139  1.000 47.12396  ? 45  ILE A CG1 1 
ATOM   2030 C CG2 . ILE B 1 45  ? 0.04959  2.06209   -9.57110  1.000 53.92046  ? 45  ILE A CG2 1 
ATOM   2031 C CD1 . ILE B 1 45  ? 1.28542  4.50200   -8.13071  1.000 54.79292  ? 45  ILE A CD1 1 
ATOM   2032 N N   . LYS B 1 46  ? 3.59345  3.37720   -12.01099 1.000 49.75185  ? 46  LYS A N   1 
ATOM   2033 C CA  . LYS B 1 46  ? 4.74759  4.13793   -12.46128 1.000 45.55179  ? 46  LYS A CA  1 
ATOM   2034 C C   . LYS B 1 46  ? 4.32434  5.59655   -12.47097 1.000 46.14715  ? 46  LYS A C   1 
ATOM   2035 O O   . LYS B 1 46  ? 3.40913  5.97025   -13.21213 1.000 47.90910  ? 46  LYS A O   1 
ATOM   2036 C CB  . LYS B 1 46  ? 5.20049  3.68119   -13.84488 1.000 44.28002  ? 46  LYS A CB  1 
ATOM   2037 N N   . ILE B 1 47  ? 4.94397  6.40398   -11.61268 1.000 43.00522  ? 47  ILE A N   1 
ATOM   2038 C CA  . ILE B 1 47  ? 4.71509  7.84199   -11.58411 1.000 41.93891  ? 47  ILE A CA  1 
ATOM   2039 C C   . ILE B 1 47  ? 5.82907  8.49651   -12.38412 1.000 43.38453  ? 47  ILE A C   1 
ATOM   2040 O O   . ILE B 1 47  ? 7.01911  8.27177   -12.10874 1.000 42.22076  ? 47  ILE A O   1 
ATOM   2041 C CB  . ILE B 1 47  ? 4.65578  8.37636   -10.14536 1.000 43.89884  ? 47  ILE A CB  1 
ATOM   2042 C CG1 . ILE B 1 47  ? 3.53958  7.66400   -9.36898  1.000 44.34053  ? 47  ILE A CG1 1 
ATOM   2043 C CG2 . ILE B 1 47  ? 4.42996  9.88153   -10.14341 1.000 41.37926  ? 47  ILE A CG2 1 
ATOM   2044 C CD1 . ILE B 1 47  ? 3.76288  7.61388   -7.86599  1.000 43.62850  ? 47  ILE A CD1 1 
ATOM   2045 N N   . LYS B 1 48  ? 5.43778  9.27153   -13.39643 1.000 41.12246  ? 48  LYS A N   1 
ATOM   2046 C CA  . LYS B 1 48  ? 6.34739  9.88537   -14.35720 1.000 38.70382  ? 48  LYS A CA  1 
ATOM   2047 C C   . LYS B 1 48  ? 6.29314  11.39668  -14.20047 1.000 43.93156  ? 48  LYS A C   1 
ATOM   2048 O O   . LYS B 1 48  ? 5.20126  11.98218  -14.18215 1.000 45.28527  ? 48  LYS A O   1 
ATOM   2049 C CB  . LYS B 1 48  ? 5.97784  9.49877   -15.78972 1.000 41.26373  ? 48  LYS A CB  1 
ATOM   2050 C CG  . LYS B 1 48  ? 7.08642  9.70370   -16.79957 1.000 47.30459  ? 48  LYS A CG  1 
ATOM   2051 C CD  . LYS B 1 48  ? 6.66744  9.24068   -18.17758 1.000 46.63831  ? 48  LYS A CD  1 
ATOM   2052 C CE  . LYS B 1 48  ? 7.62187  9.71055   -19.28766 1.000 45.72032  ? 48  LYS A CE  1 
ATOM   2053 N NZ  . LYS B 1 48  ? 8.55825  10.80076  -18.94665 1.000 42.24528  ? 48  LYS A NZ  1 
ATOM   2054 N N   . PHE B 1 49  ? 7.46419  12.02484  -14.10303 1.000 39.65072  ? 49  PHE A N   1 
ATOM   2055 C CA  . PHE B 1 49  ? 7.56001  13.42406  -13.72591 1.000 39.83059  ? 49  PHE A CA  1 
ATOM   2056 C C   . PHE B 1 49  ? 7.83081  14.31213  -14.92515 1.000 42.22999  ? 49  PHE A C   1 
ATOM   2057 O O   . PHE B 1 49  ? 8.48077  13.90698  -15.89609 1.000 40.73434  ? 49  PHE A O   1 
ATOM   2058 C CB  . PHE B 1 49  ? 8.66113  13.64667  -12.69705 1.000 35.37793  ? 49  PHE A CB  1 
ATOM   2059 C CG  . PHE B 1 49  ? 8.50720  12.81965  -11.46873 1.000 37.09285  ? 49  PHE A CG  1 
ATOM   2060 C CD1 . PHE B 1 49  ? 7.69833  13.24526  -10.42979 1.000 36.71111  ? 49  PHE A CD1 1 
ATOM   2061 C CD2 . PHE B 1 49  ? 9.16539  11.60003  -11.35322 1.000 36.59284  ? 49  PHE A CD2 1 
ATOM   2062 C CE1 . PHE B 1 49  ? 7.55050  12.45848  -9.29284  1.000 39.47330  ? 49  PHE A CE1 1 
ATOM   2063 C CE2 . PHE B 1 49  ? 9.03225  10.82451  -10.22138 1.000 36.77518  ? 49  PHE A CE2 1 
ATOM   2064 C CZ  . PHE B 1 49  ? 8.23954  11.25231  -9.18477  1.000 35.34155  ? 49  PHE A CZ  1 
ATOM   2065 N N   . ASP B 1 50  ? 7.32002  15.53529  -14.83951 1.000 42.74768  ? 50  ASP A N   1 
ATOM   2066 C CA  . ASP B 1 50  ? 7.65914  16.56522  -15.80557 1.000 44.75574  ? 50  ASP A CA  1 
ATOM   2067 C C   . ASP B 1 50  ? 9.00433  17.14287  -15.40184 1.000 44.44614  ? 50  ASP A C   1 
ATOM   2068 O O   . ASP B 1 50  ? 9.12786  17.75126  -14.33399 1.000 43.71441  ? 50  ASP A O   1 
ATOM   2069 C CB  . ASP B 1 50  ? 6.57063  17.63830  -15.86579 1.000 42.91453  ? 50  ASP A CB  1 
ATOM   2070 C CG  . ASP B 1 50  ? 7.00927  18.89115  -16.61669 1.000 48.83324  ? 50  ASP A CG  1 
ATOM   2071 O OD1 . ASP B 1 50  ? 8.01608  18.86288  -17.35266 1.000 52.46891  ? 50  ASP A OD1 1 
ATOM   2072 O OD2 . ASP B 1 50  ? 6.32520  19.91946  -16.48467 1.000 58.33501  ? 50  ASP A OD2 1 
ATOM   2073 N N   . LEU B 1 51  ? 10.01108 16.92832  -16.25062 1.000 47.17008  ? 51  LEU A N   1 
ATOM   2074 C CA  . LEU B 1 51  ? 11.38176 17.32332  -15.94222 1.000 42.66257  ? 51  LEU A CA  1 
ATOM   2075 C C   . LEU B 1 51  ? 11.58018 18.82598  -16.05289 1.000 44.33788  ? 51  LEU A C   1 
ATOM   2076 O O   . LEU B 1 51  ? 12.29956 19.42085  -15.24305 1.000 44.34711  ? 51  LEU A O   1 
ATOM   2077 C CB  . LEU B 1 51  ? 12.35403 16.62398  -16.88725 1.000 39.04051  ? 51  LEU A CB  1 
ATOM   2078 C CG  . LEU B 1 51  ? 12.97453 15.26180  -16.59660 1.000 44.78762  ? 51  LEU A CG  1 
ATOM   2079 C CD1 . LEU B 1 51  ? 13.76625 14.78203  -17.82837 1.000 39.21904  ? 51  LEU A CD1 1 
ATOM   2080 C CD2 . LEU B 1 51  ? 13.89098 15.35253  -15.40577 1.000 41.25942  ? 51  LEU A CD2 1 
ATOM   2081 N N   . LYS B 1 52  ? 10.99229 19.44185  -17.07938 1.000 47.11473  ? 52  LYS A N   1 
ATOM   2082 C CA  . LYS B 1 52  ? 11.18813 20.86949  -17.31027 1.000 49.21022  ? 52  LYS A CA  1 
ATOM   2083 C C   . LYS B 1 52  ? 10.81887 21.68162  -16.07443 1.000 49.93984  ? 52  LYS A C   1 
ATOM   2084 O O   . LYS B 1 52  ? 11.60752 22.51361  -15.60939 1.000 50.66123  ? 52  LYS A O   1 
ATOM   2085 C CB  . LYS B 1 52  ? 10.36809 21.31811  -18.52401 1.000 55.07126  ? 52  LYS A CB  1 
ATOM   2086 C CG  . LYS B 1 52  ? 10.67252 22.73347  -18.98935 1.000 59.01170  ? 52  LYS A CG  1 
ATOM   2087 C CD  . LYS B 1 52  ? 9.48849  23.36546  -19.69873 1.000 54.59066  ? 52  LYS A CD  1 
ATOM   2088 C CE  . LYS B 1 52  ? 9.52133  23.06657  -21.18250 1.000 65.27593  ? 52  LYS A CE  1 
ATOM   2089 N NZ  . LYS B 1 52  ? 10.16035 24.17990  -21.96480 1.000 74.30957  ? 52  LYS A NZ  1 
ATOM   2090 N N   . SER B 1 53  ? 9.63617  21.42380  -15.50385 1.000 43.96932  ? 53  SER A N   1 
ATOM   2091 C CA  . SER B 1 53  ? 9.18848  22.16622  -14.32656 1.000 43.52642  ? 53  SER A CA  1 
ATOM   2092 C C   . SER B 1 53  ? 10.14282 22.04979  -13.14340 1.000 52.86891  ? 53  SER A C   1 
ATOM   2093 O O   . SER B 1 53  ? 10.08469 22.88506  -12.23531 1.000 54.39526  ? 53  SER A O   1 
ATOM   2094 C CB  . SER B 1 53  ? 7.79002  21.71043  -13.90736 1.000 47.17413  ? 53  SER A CB  1 
ATOM   2095 O OG  . SER B 1 53  ? 7.74846  20.33142  -13.58039 1.000 49.24740  ? 53  SER A OG  1 
ATOM   2096 N N   . GLN B 1 54  ? 11.03119 21.05454  -13.12394 1.000 50.93701  ? 54  GLN A N   1 
ATOM   2097 C CA  . GLN B 1 54  ? 11.97620 20.99564  -12.02119 1.000 48.29539  ? 54  GLN A CA  1 
ATOM   2098 C C   . GLN B 1 54  ? 13.19355 21.86728  -12.25220 1.000 47.42890  ? 54  GLN A C   1 
ATOM   2099 O O   . GLN B 1 54  ? 14.01520 22.00123  -11.32868 1.000 47.09899  ? 54  GLN A O   1 
ATOM   2100 C CB  . GLN B 1 54  ? 12.40906 19.55678  -11.75143 1.000 38.81053  ? 54  GLN A CB  1 
ATOM   2101 C CG  . GLN B 1 54  ? 11.24542 18.64151  -11.67518 1.000 41.07224  ? 54  GLN A CG  1 
ATOM   2102 C CD  . GLN B 1 54  ? 11.65506 17.21228  -11.49908 1.000 41.65518  ? 54  GLN A CD  1 
ATOM   2103 O OE1 . GLN B 1 54  ? 12.41548 16.88764  -10.58588 1.000 39.17688  ? 54  GLN A OE1 1 
ATOM   2104 N NE2 . GLN B 1 54  ? 11.16663 16.33790  -12.38173 1.000 38.76525  ? 54  GLN A NE2 1 
ATOM   2105 N N   . LYS B 1 55  ? 13.32770 22.45890  -13.44166 1.000 47.34287  ? 55  LYS A N   1 
ATOM   2106 C CA  . LYS B 1 55  ? 14.45260 23.36290  -13.69437 1.000 49.42598  ? 55  LYS A CA  1 
ATOM   2107 C C   . LYS B 1 55  ? 14.33363 24.55813  -12.76034 1.000 49.47780  ? 55  LYS A C   1 
ATOM   2108 O O   . LYS B 1 55  ? 13.26639 25.16418  -12.64264 1.000 54.88423  ? 55  LYS A O   1 
ATOM   2109 C CB  . LYS B 1 55  ? 14.47056 23.81582  -15.15858 1.000 45.75739  ? 55  LYS A CB  1 
ATOM   2110 C CG  . LYS B 1 55  ? 15.09315 22.80562  -16.13705 1.000 45.90773  ? 55  LYS A CG  1 
ATOM   2111 C CD  . LYS B 1 55  ? 16.63032 22.80674  -16.02687 1.000 53.52901  ? 55  LYS A CD  1 
ATOM   2112 C CE  . LYS B 1 55  ? 17.26738 21.62961  -16.76063 1.000 52.80375  ? 55  LYS A CE  1 
ATOM   2113 N NZ  . LYS B 1 55  ? 16.64187 21.39377  -18.09978 1.000 53.28312  ? 55  LYS A NZ  1 
ATOM   2114 N N   . GLY B 1 56  ? 15.39861 24.84821  -12.03156 1.000 54.51734  ? 56  GLY A N   1 
ATOM   2115 C CA  . GLY B 1 56  ? 15.32645 25.86125  -11.00720 1.000 55.33100  ? 56  GLY A CA  1 
ATOM   2116 C C   . GLY B 1 56  ? 14.80732 25.38266  -9.67099  1.000 53.65670  ? 56  GLY A C   1 
ATOM   2117 O O   . GLY B 1 56  ? 14.88563 26.13386  -8.69663  1.000 57.67643  ? 56  GLY A O   1 
ATOM   2118 N N   . HIS B 1 57  ? 14.27928 24.16206  -9.58347  1.000 51.94024  ? 57  HIS A N   1 
ATOM   2119 C CA  . HIS B 1 57  ? 13.85500 23.61393  -8.29945  1.000 52.58853  ? 57  HIS A CA  1 
ATOM   2120 C C   . HIS B 1 57  ? 14.64620 22.38830  -7.86324  1.000 49.92624  ? 57  HIS A C   1 
ATOM   2121 O O   . HIS B 1 57  ? 14.78959 22.15668  -6.66234  1.000 50.68113  ? 57  HIS A O   1 
ATOM   2122 C CB  . HIS B 1 57  ? 12.36638 23.24204  -8.32809  1.000 52.92564  ? 57  HIS A CB  1 
ATOM   2123 C CG  . HIS B 1 57  ? 11.44848 24.38235  -8.66388  1.000 59.53683  ? 57  HIS A CG  1 
ATOM   2124 N ND1 . HIS B 1 57  ? 11.31094 24.88050  -9.94255  1.000 58.76226  ? 57  HIS A ND1 1 
ATOM   2125 C CD2 . HIS B 1 57  ? 10.61022 25.11064  -7.88576  1.000 61.17458  ? 57  HIS A CD2 1 
ATOM   2126 C CE1 . HIS B 1 57  ? 10.42928 25.86591  -9.93810  1.000 61.14013  ? 57  HIS A CE1 1 
ATOM   2127 N NE2 . HIS B 1 57  ? 9.98740  26.02329  -8.70243  1.000 63.33685  ? 57  HIS A NE2 1 
ATOM   2128 N N   . ARG B 1 58  ? 15.16592 21.60082  -8.79570  1.000 45.26784  ? 58  ARG A N   1 
ATOM   2129 C CA  . ARG B 1 58  ? 15.82103 20.34983  -8.45741  1.000 41.20202  ? 58  ARG A CA  1 
ATOM   2130 C C   . ARG B 1 58  ? 17.05734 20.20507  -9.33282  1.000 43.36622  ? 58  ARG A C   1 
ATOM   2131 O O   . ARG B 1 58  ? 17.26982 20.97971  -10.26925 1.000 43.59402  ? 58  ARG A O   1 
ATOM   2132 C CB  . ARG B 1 58  ? 14.85089 19.18115  -8.60271  1.000 41.94348  ? 58  ARG A CB  1 
ATOM   2133 C CG  . ARG B 1 58  ? 13.76005 19.19671  -7.53261  1.000 40.38631  ? 58  ARG A CG  1 
ATOM   2134 C CD  . ARG B 1 58  ? 12.97420 17.92306  -7.55781  1.000 40.31648  ? 58  ARG A CD  1 
ATOM   2135 N NE  . ARG B 1 58  ? 13.73507 16.80077  -7.01605  1.000 40.97672  ? 58  ARG A NE  1 
ATOM   2136 C CZ  . ARG B 1 58  ? 13.88144 16.55627  -5.72126  1.000 37.10558  ? 58  ARG A CZ  1 
ATOM   2137 N NH1 . ARG B 1 58  ? 13.43508 17.39965  -4.80649  1.000 32.85556  ? 58  ARG A NH1 1 
ATOM   2138 N NH2 . ARG B 1 58  ? 14.47000 15.42868  -5.33786  1.000 33.60735  ? 58  ARG A NH2 1 
ATOM   2139 N N   . LEU B 1 59  ? 17.89372 19.21374  -9.01054  1.000 43.56782  ? 59  LEU A N   1 
ATOM   2140 C CA  . LEU B 1 59  ? 19.31883 19.25567  -9.34567  1.000 45.85957  ? 59  LEU A CA  1 
ATOM   2141 C C   . LEU B 1 59  ? 19.61152 18.37086  -10.55541 1.000 44.21235  ? 59  LEU A C   1 
ATOM   2142 O O   . LEU B 1 59  ? 19.49658 17.14617  -10.47649 1.000 46.53168  ? 59  LEU A O   1 
ATOM   2143 C CB  . LEU B 1 59  ? 20.14452 18.82067  -8.13430  1.000 44.10714  ? 59  LEU A CB  1 
ATOM   2144 C CG  . LEU B 1 59  ? 21.61084 19.23803  -8.00476  1.000 52.73785  ? 59  LEU A CG  1 
ATOM   2145 C CD1 . LEU B 1 59  ? 22.48745 18.59658  -9.06327  1.000 51.21625  ? 59  LEU A CD1 1 
ATOM   2146 C CD2 . LEU B 1 59  ? 21.72020 20.77054  -8.05262  1.000 55.67216  ? 59  LEU A CD2 1 
ATOM   2147 N N   . PHE B 1 60  ? 20.01135 18.98668  -11.66815 1.000 43.06171  ? 60  PHE A N   1 
ATOM   2148 C CA  . PHE B 1 60  ? 20.41199 18.25169  -12.87130 1.000 45.61191  ? 60  PHE A CA  1 
ATOM   2149 C C   . PHE B 1 60  ? 21.94007 18.15495  -12.87489 1.000 45.74026  ? 60  PHE A C   1 
ATOM   2150 O O   . PHE B 1 60  ? 22.62656 19.08925  -13.27975 1.000 42.98990  ? 60  PHE A O   1 
ATOM   2151 C CB  . PHE B 1 60  ? 19.89734 18.92775  -14.14389 1.000 42.72031  ? 60  PHE A CB  1 
ATOM   2152 C CG  . PHE B 1 60  ? 18.38717 18.93769  -14.27858 1.000 46.28983  ? 60  PHE A CG  1 
ATOM   2153 C CD1 . PHE B 1 60  ? 17.61694 19.87038  -13.58805 1.000 44.76548  ? 60  PHE A CD1 1 
ATOM   2154 C CD2 . PHE B 1 60  ? 17.73980 18.02294  -15.11471 1.000 40.37349  ? 60  PHE A CD2 1 
ATOM   2155 C CE1 . PHE B 1 60  ? 16.23647 19.88730  -13.71237 1.000 44.07350  ? 60  PHE A CE1 1 
ATOM   2156 C CE2 . PHE B 1 60  ? 16.36185 18.02801  -15.23060 1.000 44.44106  ? 60  PHE A CE2 1 
ATOM   2157 C CZ  . PHE B 1 60  ? 15.60486 18.97284  -14.53285 1.000 41.57043  ? 60  PHE A CZ  1 
ATOM   2158 N N   . THR B 1 61  ? 22.46787 17.02141  -12.42361 1.000 42.39747  ? 61  THR A N   1 
ATOM   2159 C CA  . THR B 1 61  ? 23.90322 16.79375  -12.39971 1.000 45.67466  ? 61  THR A CA  1 
ATOM   2160 C C   . THR B 1 61  ? 24.40202 16.48195  -13.80468 1.000 47.67202  ? 61  THR A C   1 
ATOM   2161 O O   . THR B 1 61  ? 23.77242 15.72119  -14.54532 1.000 48.94601  ? 61  THR A O   1 
ATOM   2162 C CB  . THR B 1 61  ? 24.22386 15.65924  -11.43139 1.000 45.95593  ? 61  THR A CB  1 
ATOM   2163 O OG1 . THR B 1 61  ? 23.95872 16.10508  -10.10006 1.000 46.40720  ? 61  THR A OG1 1 
ATOM   2164 C CG2 . THR B 1 61  ? 25.65870 15.25262  -11.51345 1.000 43.81998  ? 61  THR A CG2 1 
ATOM   2165 N N   . LYS B 1 62  ? 25.51720 17.10043  -14.18647 1.000 48.13612  ? 62  LYS A N   1 
ATOM   2166 C CA  . LYS B 1 62  ? 25.98360 16.96814  -15.56352 1.000 52.23930  ? 62  LYS A CA  1 
ATOM   2167 C C   . LYS B 1 62  ? 26.61393 15.60273  -15.83137 1.000 49.85019  ? 62  LYS A C   1 
ATOM   2168 O O   . LYS B 1 62  ? 26.49768 15.07592  -16.94246 1.000 48.38539  ? 62  LYS A O   1 
ATOM   2169 C CB  . LYS B 1 62  ? 26.94955 18.10788  -15.88304 1.000 58.43069  ? 62  LYS A CB  1 
ATOM   2170 C CG  . LYS B 1 62  ? 26.29799 19.48352  -15.67420 1.000 55.96776  ? 62  LYS A CG  1 
ATOM   2171 C CD  . LYS B 1 62  ? 25.96840 20.13359  -17.00230 1.000 59.90053  ? 62  LYS A CD  1 
ATOM   2172 C CE  . LYS B 1 62  ? 27.14563 20.96906  -17.53185 1.000 65.77436  ? 62  LYS A CE  1 
ATOM   2173 N NZ  . LYS B 1 62  ? 27.42282 22.16968  -16.68305 1.000 62.08809  ? 62  LYS A NZ  1 
ATOM   2174 N N   . SER B 1 63  ? 27.26233 15.00560  -14.83615 1.000 49.69350  ? 63  SER A N   1 
ATOM   2175 C CA  . SER B 1 63  ? 27.75481 13.64434  -15.00209 1.000 50.45026  ? 63  SER A CA  1 
ATOM   2176 C C   . SER B 1 63  ? 26.63271 12.62128  -15.09638 1.000 54.88914  ? 63  SER A C   1 
ATOM   2177 O O   . SER B 1 63  ? 26.90433 11.46049  -15.42676 1.000 58.01252  ? 63  SER A O   1 
ATOM   2178 C CB  . SER B 1 63  ? 28.68354 13.27306  -13.85076 1.000 51.16788  ? 63  SER A CB  1 
ATOM   2179 O OG  . SER B 1 63  ? 27.95795 13.02649  -12.66544 1.000 54.38823  ? 63  SER A OG  1 
ATOM   2180 N N   . THR B 1 64  ? 25.39245 13.00900  -14.79199 1.000 55.13990  ? 64  THR A N   1 
ATOM   2181 C CA  . THR B 1 64  ? 24.23213 12.15139  -14.99807 1.000 47.28004  ? 64  THR A CA  1 
ATOM   2182 C C   . THR B 1 64  ? 23.53209 12.44952  -16.31087 1.000 41.92848  ? 64  THR A C   1 
ATOM   2183 O O   . THR B 1 64  ? 23.06316 11.52561  -16.97778 1.000 43.74306  ? 64  THR A O   1 
ATOM   2184 C CB  . THR B 1 64  ? 23.25003 12.30275  -13.83593 1.000 46.59093  ? 64  THR A CB  1 
ATOM   2185 O OG1 . THR B 1 64  ? 23.87080 11.82669  -12.63621 1.000 44.69699  ? 64  THR A OG1 1 
ATOM   2186 C CG2 . THR B 1 64  ? 21.97114 11.47250  -14.09117 1.000 44.19239  ? 64  THR A CG2 1 
ATOM   2187 N N   . ILE B 1 65  ? 23.48302 13.72434  -16.70333 1.000 47.02554  ? 65  ILE A N   1 
ATOM   2188 C CA  . ILE B 1 65  ? 22.97605 14.09080  -18.02261 1.000 46.03285  ? 65  ILE A CA  1 
ATOM   2189 C C   . ILE B 1 65  ? 23.78541 13.39992  -19.11045 1.000 51.93450  ? 65  ILE A C   1 
ATOM   2190 O O   . ILE B 1 65  ? 23.22826 12.82516  -20.05719 1.000 53.28334  ? 65  ILE A O   1 
ATOM   2191 C CB  . ILE B 1 65  ? 22.99665 15.61490  -18.20461 1.000 44.13743  ? 65  ILE A CB  1 
ATOM   2192 C CG1 . ILE B 1 65  ? 21.96812 16.28427  -17.28439 1.000 47.70295  ? 65  ILE A CG1 1 
ATOM   2193 C CG2 . ILE B 1 65  ? 22.75675 15.95673  -19.66225 1.000 42.54706  ? 65  ILE A CG2 1 
ATOM   2194 C CD1 . ILE B 1 65  ? 22.24527 17.77218  -17.02353 1.000 45.50288  ? 65  ILE A CD1 1 
ATOM   2195 N N   . GLU B 1 66  ? 25.11607 13.43567  -18.98717 1.000 46.99518  ? 66  GLU A N   1 
ATOM   2196 C CA  . GLU B 1 66  ? 25.95196 12.76142  -19.96972 1.000 50.43127  ? 66  GLU A CA  1 
ATOM   2197 C C   . GLU B 1 66  ? 25.75241 11.24967  -19.91176 1.000 51.29094  ? 66  GLU A C   1 
ATOM   2198 O O   . GLU B 1 66  ? 25.64076 10.59420  -20.95379 1.000 54.78979  ? 66  GLU A O   1 
ATOM   2199 C CB  . GLU B 1 66  ? 27.42232 13.14076  -19.75885 1.000 52.52301  ? 66  GLU A CB  1 
ATOM   2200 N N   . TRP B 1 67  ? 25.67928 10.67882  -18.70841 1.000 46.69363  ? 67  TRP A N   1 
ATOM   2201 C CA  . TRP B 1 67  ? 25.38840 9.25429   -18.59307 1.000 49.57352  ? 67  TRP A CA  1 
ATOM   2202 C C   . TRP B 1 67  ? 24.13864 8.86440   -19.38913 1.000 54.22407  ? 67  TRP A C   1 
ATOM   2203 O O   . TRP B 1 67  ? 24.16798 7.89715   -20.15839 1.000 51.43171  ? 67  TRP A O   1 
ATOM   2204 C CB  . TRP B 1 67  ? 25.23444 8.86514   -17.12545 1.000 51.58213  ? 67  TRP A CB  1 
ATOM   2205 C CG  . TRP B 1 67  ? 25.07515 7.37868   -16.93671 1.000 58.40732  ? 67  TRP A CG  1 
ATOM   2206 C CD1 . TRP B 1 67  ? 26.08209 6.45470   -16.85263 1.000 55.92389  ? 67  TRP A CD1 1 
ATOM   2207 C CD2 . TRP B 1 67  ? 23.84706 6.64770   -16.78045 1.000 57.98350  ? 67  TRP A CD2 1 
ATOM   2208 N NE1 . TRP B 1 67  ? 25.55779 5.20088   -16.66512 1.000 50.34634  ? 67  TRP A NE1 1 
ATOM   2209 C CE2 . TRP B 1 67  ? 24.19144 5.28550   -16.61767 1.000 56.87474  ? 67  TRP A CE2 1 
ATOM   2210 C CE3 . TRP B 1 67  ? 22.49094 7.01063   -16.76507 1.000 53.37162  ? 67  TRP A CE3 1 
ATOM   2211 C CZ2 . TRP B 1 67  ? 23.22887 4.27844   -16.45678 1.000 53.08157  ? 67  TRP A CZ2 1 
ATOM   2212 C CZ3 . TRP B 1 67  ? 21.53470 6.01022   -16.59528 1.000 53.64777  ? 67  TRP A CZ3 1 
ATOM   2213 C CH2 . TRP B 1 67  ? 21.91313 4.65839   -16.44417 1.000 56.12947  ? 67  TRP A CH2 1 
ATOM   2214 N N   . TRP B 1 68  ? 23.03694 9.62837   -19.24285 1.000 49.83481  ? 68  TRP A N   1 
ATOM   2215 C CA  . TRP B 1 68  ? 21.81337 9.31577   -19.99118 1.000 51.65280  ? 68  TRP A CA  1 
ATOM   2216 C C   . TRP B 1 68  ? 22.03382 9.44568   -21.49746 1.000 51.62818  ? 68  TRP A C   1 
ATOM   2217 O O   . TRP B 1 68  ? 21.53744 8.62376   -22.27195 1.000 50.69382  ? 68  TRP A O   1 
ATOM   2218 C CB  . TRP B 1 68  ? 20.64013 10.21257  -19.54670 1.000 45.15745  ? 68  TRP A CB  1 
ATOM   2219 C CG  . TRP B 1 68  ? 19.93679 9.73433   -18.26525 1.000 45.85100  ? 68  TRP A CG  1 
ATOM   2220 C CD1 . TRP B 1 68  ? 19.89694 10.38343  -17.06099 1.000 43.54915  ? 68  TRP A CD1 1 
ATOM   2221 C CD2 . TRP B 1 68  ? 19.18523 8.51904   -18.08413 1.000 44.63108  ? 68  TRP A CD2 1 
ATOM   2222 N NE1 . TRP B 1 68  ? 19.19386 9.63760   -16.13539 1.000 39.21314  ? 68  TRP A NE1 1 
ATOM   2223 C CE2 . TRP B 1 68  ? 18.74386 8.49328   -16.73675 1.000 45.03365  ? 68  TRP A CE2 1 
ATOM   2224 C CE3 . TRP B 1 68  ? 18.85816 7.44443   -18.92146 1.000 46.47187  ? 68  TRP A CE3 1 
ATOM   2225 C CZ2 . TRP B 1 68  ? 17.97440 7.43937   -16.21405 1.000 46.91499  ? 68  TRP A CZ2 1 
ATOM   2226 C CZ3 . TRP B 1 68  ? 18.09233 6.39873   -18.40400 1.000 48.02311  ? 68  TRP A CZ3 1 
ATOM   2227 C CH2 . TRP B 1 68  ? 17.66295 6.40360   -17.05981 1.000 47.74721  ? 68  TRP A CH2 1 
ATOM   2228 N N   . LYS B 1 69  ? 22.78168 10.46851  -21.92712 1.000 48.45697  ? 69  LYS A N   1 
ATOM   2229 C CA  . LYS B 1 69  ? 23.06109 10.67361  -23.34558 1.000 52.73900  ? 69  LYS A CA  1 
ATOM   2230 C C   . LYS B 1 69  ? 23.68511 9.43491   -23.99743 1.000 59.23590  ? 69  LYS A C   1 
ATOM   2231 O O   . LYS B 1 69  ? 23.44732 9.16757   -25.18061 1.000 57.87481  ? 69  LYS A O   1 
ATOM   2232 C CB  . LYS B 1 69  ? 24.00863 11.86291  -23.50569 1.000 56.61914  ? 69  LYS A CB  1 
ATOM   2233 C CG  . LYS B 1 69  ? 23.41330 13.10042  -24.14397 1.000 58.63764  ? 69  LYS A CG  1 
ATOM   2234 C CD  . LYS B 1 69  ? 24.35210 14.29464  -23.92726 1.000 56.38301  ? 69  LYS A CD  1 
ATOM   2235 C CE  . LYS B 1 69  ? 23.58170 15.59147  -23.65585 1.000 60.09901  ? 69  LYS A CE  1 
ATOM   2236 N NZ  . LYS B 1 69  ? 24.47735 16.63114  -23.04213 1.000 60.88011  ? 69  LYS A NZ  1 
ATOM   2237 N N   . ASN B 1 70  ? 24.47487 8.66316   -23.24730 1.000 51.69586  ? 70  ASN A N   1 
ATOM   2238 C CA  . ASN B 1 70  ? 25.16893 7.51028   -23.80061 1.000 55.45384  ? 70  ASN A CA  1 
ATOM   2239 C C   . ASN B 1 70  ? 24.38808 6.21471   -23.69445 1.000 58.44211  ? 70  ASN A C   1 
ATOM   2240 O O   . ASN B 1 70  ? 24.88817 5.18074   -24.14072 1.000 62.18949  ? 70  ASN A O   1 
ATOM   2241 C CB  . ASN B 1 70  ? 26.51590 7.33104   -23.10541 1.000 56.59730  ? 70  ASN A CB  1 
ATOM   2242 C CG  . ASN B 1 70  ? 27.45892 8.46169   -23.40241 1.000 56.27741  ? 70  ASN A CG  1 
ATOM   2243 O OD1 . ASN B 1 70  ? 27.59306 8.87216   -24.55844 1.000 59.55047  ? 70  ASN A OD1 1 
ATOM   2244 N ND2 . ASN B 1 70  ? 28.09211 9.00505   -22.36283 1.000 58.04286  ? 70  ASN A ND2 1 
ATOM   2245 N N   . GLN B 1 71  ? 23.19415 6.23135   -23.11451 1.000 58.56543  ? 71  GLN A N   1 
ATOM   2246 C CA  . GLN B 1 71  ? 22.44655 5.00128   -22.93351 1.000 55.00551  ? 71  GLN A CA  1 
ATOM   2247 C C   . GLN B 1 71  ? 21.72147 4.60938   -24.22076 1.000 54.90615  ? 71  GLN A C   1 
ATOM   2248 O O   . GLN B 1 71  ? 21.71095 5.33555   -25.22018 1.000 53.30018  ? 71  GLN A O   1 
ATOM   2249 C CB  . GLN B 1 71  ? 21.44407 5.14162   -21.78786 1.000 57.19627  ? 71  GLN A CB  1 
ATOM   2250 C CG  . GLN B 1 71  ? 22.05654 5.57170   -20.45754 1.000 58.47023  ? 71  GLN A CG  1 
ATOM   2251 C CD  . GLN B 1 71  ? 23.26533 4.72497   -20.03850 1.000 61.50362  ? 71  GLN A CD  1 
ATOM   2252 O OE1 . GLN B 1 71  ? 23.18001 3.49539   -19.94716 1.000 58.26287  ? 71  GLN A OE1 1 
ATOM   2253 N NE2 . GLN B 1 71  ? 24.39325 5.39016   -19.76648 1.000 58.36155  ? 71  GLN A NE2 1 
ATOM   2254 N N   . SER B 1 72  ? 21.08647 3.44157   -24.16799 1.000 55.21708  ? 72  SER A N   1 
ATOM   2255 C CA  . SER B 1 72  ? 20.49329 2.84174   -25.35287 1.000 55.91780  ? 72  SER A CA  1 
ATOM   2256 C C   . SER B 1 72  ? 19.25891 3.61930   -25.79464 1.000 56.89244  ? 72  SER A C   1 
ATOM   2257 O O   . SER B 1 72  ? 18.62723 4.31034   -24.98854 1.000 58.46760  ? 72  SER A O   1 
ATOM   2258 C CB  . SER B 1 72  ? 20.13684 1.38262   -25.07952 1.000 46.41998  ? 72  SER A CB  1 
ATOM   2259 O OG  . SER B 1 72  ? 18.91842 1.28008   -24.37006 1.000 58.68023  ? 72  SER A OG  1 
ATOM   2260 N N   . PRO B 1 73  ? 18.89940 3.53242   -27.07627 1.000 58.48135  ? 73  PRO A N   1 
ATOM   2261 C CA  . PRO B 1 73  ? 17.71594 4.27351   -27.54117 1.000 55.31653  ? 73  PRO A CA  1 
ATOM   2262 C C   . PRO B 1 73  ? 16.44611 3.89863   -26.80086 1.000 53.85358  ? 73  PRO A C   1 
ATOM   2263 O O   . PRO B 1 73  ? 15.58257 4.76146   -26.60733 1.000 50.84071  ? 73  PRO A O   1 
ATOM   2264 C CB  . PRO B 1 73  ? 17.63961 3.91031   -29.02970 1.000 55.71294  ? 73  PRO A CB  1 
ATOM   2265 C CG  . PRO B 1 73  ? 19.08301 3.55911   -29.40110 1.000 49.38877  ? 73  PRO A CG  1 
ATOM   2266 C CD  . PRO B 1 73  ? 19.60560 2.85150   -28.18203 1.000 51.55675  ? 73  PRO A CD  1 
ATOM   2267 N N   . GLU B 1 74  ? 16.30438 2.64530   -26.36015 1.000 51.83229  ? 74  GLU A N   1 
ATOM   2268 C CA  . GLU B 1 74  ? 15.06878 2.27651   -25.67349 1.000 56.40253  ? 74  GLU A CA  1 
ATOM   2269 C C   . GLU B 1 74  ? 15.08320 2.73570   -24.21552 1.000 55.87804  ? 74  GLU A C   1 
ATOM   2270 O O   . GLU B 1 74  ? 14.02877 3.05576   -23.65429 1.000 52.01824  ? 74  GLU A O   1 
ATOM   2271 C CB  . GLU B 1 74  ? 14.82409 0.76306   -25.78475 1.000 46.35911  ? 74  GLU A CB  1 
ATOM   2272 N N   . ALA B 1 75  ? 16.26237 2.79161   -23.59357 1.000 57.36115  ? 75  ALA A N   1 
ATOM   2273 C CA  . ALA B 1 75  ? 16.35921 3.36958   -22.25909 1.000 54.11953  ? 75  ALA A CA  1 
ATOM   2274 C C   . ALA B 1 75  ? 16.10405 4.87067   -22.29875 1.000 53.11048  ? 75  ALA A C   1 
ATOM   2275 O O   . ALA B 1 75  ? 15.36564 5.40911   -21.46620 1.000 54.93899  ? 75  ALA A O   1 
ATOM   2276 C CB  . ALA B 1 75  ? 17.72770 3.06763   -21.65318 1.000 51.87068  ? 75  ALA A CB  1 
ATOM   2277 N N   . ARG B 1 76  ? 16.70780 5.56255   -23.26393 1.000 53.18438  ? 76  ARG A N   1 
ATOM   2278 C CA  . ARG B 1 76  ? 16.45637 6.98955   -23.42454 1.000 51.20638  ? 76  ARG A CA  1 
ATOM   2279 C C   . ARG B 1 76  ? 14.98905 7.27965   -23.75166 1.000 55.40131  ? 76  ARG A C   1 
ATOM   2280 O O   . ARG B 1 76  ? 14.46233 8.33206   -23.36752 1.000 52.14380  ? 76  ARG A O   1 
ATOM   2281 C CB  . ARG B 1 76  ? 17.36990 7.54894   -24.50945 1.000 47.94922  ? 76  ARG A CB  1 
ATOM   2282 N N   . LYS B 1 77  ? 14.30783 6.36496   -24.44639 1.000 50.39096  ? 77  LYS A N   1 
ATOM   2283 C CA  . LYS B 1 77  ? 12.90994 6.60619   -24.78509 1.000 51.07294  ? 77  LYS A CA  1 
ATOM   2284 C C   . LYS B 1 77  ? 12.03752 6.59391   -23.53790 1.000 48.24835  ? 77  LYS A C   1 
ATOM   2285 O O   . LYS B 1 77  ? 11.21905 7.49531   -23.34642 1.000 49.41988  ? 77  LYS A O   1 
ATOM   2286 C CB  . LYS B 1 77  ? 12.41351 5.57154   -25.79884 1.000 56.24959  ? 77  LYS A CB  1 
ATOM   2287 N N   . ASN B 1 78  ? 12.23517 5.59907   -22.65550 1.000 49.15092  ? 78  ASN A N   1 
ATOM   2288 C CA  . ASN B 1 78  ? 11.44341 5.46316   -21.43563 1.000 48.42915  ? 78  ASN A CA  1 
ATOM   2289 C C   . ASN B 1 78  ? 11.50970 6.70647   -20.55061 1.000 51.78003  ? 78  ASN A C   1 
ATOM   2290 O O   . ASN B 1 78  ? 10.66144 6.88164   -19.66340 1.000 48.37274  ? 78  ASN A O   1 
ATOM   2291 C CB  . ASN B 1 78  ? 11.92637 4.25024   -20.63631 1.000 49.97644  ? 78  ASN A CB  1 
ATOM   2292 N N   . ILE B 1 79  ? 12.49886 7.57179   -20.76971 1.000 49.07830  ? 79  ILE A N   1 
ATOM   2293 C CA  . ILE B 1 79  ? 12.73093 8.74611   -19.94688 1.000 52.48412  ? 79  ILE A CA  1 
ATOM   2294 C C   . ILE B 1 79  ? 12.42987 10.03317  -20.70475 1.000 48.94191  ? 79  ILE A C   1 
ATOM   2295 O O   . ILE B 1 79  ? 12.65612 11.12645  -20.18365 1.000 45.81817  ? 79  ILE A O   1 
ATOM   2296 C CB  . ILE B 1 79  ? 14.17530 8.75115   -19.38999 1.000 49.58258  ? 79  ILE A CB  1 
ATOM   2297 N N   . ALA B 1 80  ? 11.94719 9.92684   -21.93872 1.000 47.42797  ? 80  ALA A N   1 
ATOM   2298 C CA  . ALA B 1 80  ? 11.59222 11.11493  -22.69555 1.000 47.91888  ? 80  ALA A CA  1 
ATOM   2299 C C   . ALA B 1 80  ? 10.32287 11.74575  -22.10745 1.000 45.93832  ? 80  ALA A C   1 
ATOM   2300 O O   . ALA B 1 80  ? 9.53041  11.06717  -21.44931 1.000 44.89054  ? 80  ALA A O   1 
ATOM   2301 C CB  . ALA B 1 80  ? 11.39095 10.75606  -24.16767 1.000 44.18420  ? 80  ALA A CB  1 
ATOM   2302 N N   . PRO B 1 81  ? 10.12075 13.05342  -22.30045 1.000 48.50956  ? 81  PRO A N   1 
ATOM   2303 C CA  . PRO B 1 81  ? 8.88301  13.66804  -21.80725 1.000 45.77443  ? 81  PRO A CA  1 
ATOM   2304 C C   . PRO B 1 81  ? 7.69280  13.10353  -22.55915 1.000 51.79422  ? 81  PRO A C   1 
ATOM   2305 O O   . PRO B 1 81  ? 7.78716  12.75803  -23.73836 1.000 55.28443  ? 81  PRO A O   1 
ATOM   2306 C CB  . PRO B 1 81  ? 9.07383  15.16462  -22.09891 1.000 41.65321  ? 81  PRO A CB  1 
ATOM   2307 C CG  . PRO B 1 81  ? 10.53215 15.35165  -22.29207 1.000 44.78958  ? 81  PRO A CG  1 
ATOM   2308 C CD  . PRO B 1 81  ? 11.03175 14.05518  -22.89003 1.000 46.20600  ? 81  PRO A CD  1 
ATOM   2309 N N   . SER B 1 82  ? 6.57014  12.98404  -21.85736 1.000 53.18676  ? 82  SER A N   1 
ATOM   2310 C CA  . SER B 1 82  ? 5.32940  12.55940  -22.48542 1.000 54.75624  ? 82  SER A CA  1 
ATOM   2311 C C   . SER B 1 82  ? 4.18438  13.23618  -21.75398 1.000 56.86387  ? 82  SER A C   1 
ATOM   2312 O O   . SER B 1 82  ? 4.38076  13.90058  -20.73540 1.000 57.68553  ? 82  SER A O   1 
ATOM   2313 C CB  . SER B 1 82  ? 5.16637  11.03269  -22.48089 1.000 54.95065  ? 82  SER A CB  1 
ATOM   2314 O OG  . SER B 1 82  ? 4.89969  10.52187  -21.18344 1.000 59.61807  ? 82  SER A OG  1 
ATOM   2315 N N   . ASP B 1 83  ? 2.97982  13.06850  -22.29210 1.000 60.34706  ? 83  ASP A N   1 
ATOM   2316 C CA  . ASP B 1 83  ? 1.81119  13.73894  -21.73634 1.000 62.86476  ? 83  ASP A CA  1 
ATOM   2317 C C   . ASP B 1 83  ? 1.34923  13.13242  -20.43099 1.000 59.85765  ? 83  ASP A C   1 
ATOM   2318 O O   . ASP B 1 83  ? 0.38220  13.63829  -19.85657 1.000 59.61415  ? 83  ASP A O   1 
ATOM   2319 C CB  . ASP B 1 83  ? 0.64334  13.72255  -22.72823 1.000 66.43648  ? 83  ASP A CB  1 
ATOM   2320 C CG  . ASP B 1 83  ? 1.07056  14.04760  -24.14072 1.000 75.81154  ? 83  ASP A CG  1 
ATOM   2321 O OD1 . ASP B 1 83  ? 1.71412  15.10473  -24.34139 1.000 77.52896  ? 83  ASP A OD1 1 
ATOM   2322 O OD2 . ASP B 1 83  ? 0.74741  13.25224  -25.05353 1.000 80.77752  ? 83  ASP A OD2 1 
ATOM   2323 N N   . GLU B 1 84  ? 1.97864  12.06574  -19.95185 1.000 57.38912  ? 84  GLU A N   1 
ATOM   2324 C CA  . GLU B 1 84  ? 1.62386  11.55464  -18.63834 1.000 57.10217  ? 84  GLU A CA  1 
ATOM   2325 C C   . GLU B 1 84  ? 2.50587  12.12976  -17.54297 1.000 52.42992  ? 84  GLU A C   1 
ATOM   2326 O O   . GLU B 1 84  ? 2.33915  11.75149  -16.37790 1.000 52.08270  ? 84  GLU A O   1 
ATOM   2327 C CB  . GLU B 1 84  ? 1.68956  10.02636  -18.61157 1.000 59.92611  ? 84  GLU A CB  1 
ATOM   2328 C CG  . GLU B 1 84  ? 3.09300  9.46247   -18.52493 1.000 60.37568  ? 84  GLU A CG  1 
ATOM   2329 C CD  . GLU B 1 84  ? 3.10634  7.93920   -18.43946 1.000 69.35603  ? 84  GLU A CD  1 
ATOM   2330 O OE1 . GLU B 1 84  ? 3.39313  7.29954   -19.47847 1.000 75.65282  ? 84  GLU A OE1 1 
ATOM   2331 O OE2 . GLU B 1 84  ? 2.85104  7.38510   -17.33580 1.000 64.11328  ? 84  GLU A OE2 1 
ATOM   2332 N N   . ASP B 1 85  ? 3.42748  13.03242  -17.88989 1.000 49.81014  ? 85  ASP A N   1 
ATOM   2333 C CA  . ASP B 1 85  ? 4.30949  13.63395  -16.89894 1.000 46.64473  ? 85  ASP A CA  1 
ATOM   2334 C C   . ASP B 1 85  ? 3.49180  14.49515  -15.95070 1.000 51.02455  ? 85  ASP A C   1 
ATOM   2335 O O   . ASP B 1 85  ? 2.56297  15.18954  -16.37159 1.000 55.91515  ? 85  ASP A O   1 
ATOM   2336 C CB  . ASP B 1 85  ? 5.37154  14.49821  -17.56678 1.000 42.28678  ? 85  ASP A CB  1 
ATOM   2337 C CG  . ASP B 1 85  ? 6.33407  13.70263  -18.40809 1.000 46.19504  ? 85  ASP A CG  1 
ATOM   2338 O OD1 . ASP B 1 85  ? 6.32191  12.45325  -18.32869 1.000 48.21563  ? 85  ASP A OD1 1 
ATOM   2339 O OD2 . ASP B 1 85  ? 7.10745  14.33297  -19.15496 1.000 46.08017  ? 85  ASP A OD2 1 
ATOM   2340 N N   . VAL B 1 86  ? 3.82838  14.44841  -14.66305 1.000 45.48067  ? 86  VAL A N   1 
ATOM   2341 C CA  . VAL B 1 86  ? 3.13160  15.25644  -13.66987 1.000 45.40741  ? 86  VAL A CA  1 
ATOM   2342 C C   . VAL B 1 86  ? 4.15730  16.03518  -12.86870 1.000 42.41469  ? 86  VAL A C   1 
ATOM   2343 O O   . VAL B 1 86  ? 5.30191  15.60301  -12.70777 1.000 44.88282  ? 86  VAL A O   1 
ATOM   2344 C CB  . VAL B 1 86  ? 2.25913  14.40377  -12.73119 1.000 43.60003  ? 86  VAL A CB  1 
ATOM   2345 C CG1 . VAL B 1 86  ? 1.19574  13.65187  -13.53050 1.000 42.87861  ? 86  VAL A CG1 1 
ATOM   2346 C CG2 . VAL B 1 86  ? 3.14148  13.44473  -11.93789 1.000 44.04178  ? 86  VAL A CG2 1 
ATOM   2347 N N   . ALA B 1 87  ? 3.74021  17.18504  -12.35601 1.000 38.72612  ? 87  ALA A N   1 
ATOM   2348 C CA  . ALA B 1 87  ? 4.59507  17.92219  -11.44822 1.000 38.77956  ? 87  ALA A CA  1 
ATOM   2349 C C   . ALA B 1 87  ? 4.94520  17.04833  -10.24585 1.000 40.67504  ? 87  ALA A C   1 
ATOM   2350 O O   . ALA B 1 87  ? 4.23458  16.09420  -9.91328  1.000 41.35380  ? 87  ALA A O   1 
ATOM   2351 C CB  . ALA B 1 87  ? 3.90413  19.20747  -11.02172 1.000 36.96911  ? 87  ALA A CB  1 
ATOM   2352 N N   . THR B 1 88  ? 6.06641  17.36711  -9.59278  1.000 38.12524  ? 88  THR A N   1 
ATOM   2353 C CA  . THR B 1 88  ? 6.51530  16.50082  -8.50524  1.000 36.92629  ? 88  THR A CA  1 
ATOM   2354 C C   . THR B 1 88  ? 5.51059  16.48374  -7.35408  1.000 37.07737  ? 88  THR A C   1 
ATOM   2355 O O   . THR B 1 88  ? 5.27581  15.42606  -6.75023  1.000 35.48382  ? 88  THR A O   1 
ATOM   2356 C CB  . THR B 1 88  ? 7.91334  16.91527  -8.00812  1.000 42.15024  ? 88  THR A CB  1 
ATOM   2357 O OG1 . THR B 1 88  ? 7.97441  18.32746  -7.78335  1.000 40.82898  ? 88  THR A OG1 1 
ATOM   2358 C CG2 . THR B 1 88  ? 8.97387  16.56832  -9.04915  1.000 40.38261  ? 88  THR A CG2 1 
ATOM   2359 N N   . ILE B 1 89  ? 4.89200  17.63687  -7.04856  1.000 38.83270  ? 89  ILE A N   1 
ATOM   2360 C CA  . ILE B 1 89  ? 3.90776  17.69823  -5.96588  1.000 38.05487  ? 89  ILE A CA  1 
ATOM   2361 C C   . ILE B 1 89  ? 2.67109  16.85334  -6.30009  1.000 42.99530  ? 89  ILE A C   1 
ATOM   2362 O O   . ILE B 1 89  ? 2.01590  16.31612  -5.39173  1.000 41.47199  ? 89  ILE A O   1 
ATOM   2363 C CB  . ILE B 1 89  ? 3.54218  19.16649  -5.64166  1.000 42.23406  ? 89  ILE A CB  1 
ATOM   2364 C CG1 . ILE B 1 89  ? 2.84613  19.28657  -4.27964  1.000 43.20996  ? 89  ILE A CG1 1 
ATOM   2365 C CG2 . ILE B 1 89  ? 2.60137  19.77376  -6.70796  1.000 40.61968  ? 89  ILE A CG2 1 
ATOM   2366 C CD1 . ILE B 1 89  ? 3.45446  18.47176  -3.18424  1.000 44.10489  ? 89  ILE A CD1 1 
ATOM   2367 N N   . ALA B 1 90  ? 2.34411  16.69548  -7.59358  1.000 39.86400  ? 90  ALA A N   1 
ATOM   2368 C CA  . ALA B 1 90  ? 1.26856  15.77802  -7.98524  1.000 38.61782  ? 90  ALA A CA  1 
ATOM   2369 C C   . ALA B 1 90  ? 1.72354  14.33283  -7.89239  1.000 42.13685  ? 90  ALA A C   1 
ATOM   2370 O O   . ALA B 1 90  ? 0.94288  13.44939  -7.51179  1.000 36.81897  ? 90  ALA A O   1 
ATOM   2371 C CB  . ALA B 1 90  ? 0.79111  16.07269  -9.40629  1.000 35.86196  ? 90  ALA A CB  1 
ATOM   2372 N N   . GLY B 1 91  ? 2.99279  14.07945  -8.24045  1.000 41.75019  ? 91  GLY A N   1 
ATOM   2373 C CA  . GLY B 1 91  ? 3.52316  12.72831  -8.16829  1.000 37.49091  ? 91  GLY A CA  1 
ATOM   2374 C C   . GLY B 1 91  ? 3.57723  12.18245  -6.75296  1.000 37.59598  ? 91  GLY A C   1 
ATOM   2375 O O   . GLY B 1 91  ? 3.24354  11.01473  -6.51239  1.000 35.78553  ? 91  GLY A O   1 
ATOM   2376 N N   . ILE B 1 92  ? 4.03669  12.99831  -5.79945  1.000 40.48412  ? 92  ILE A N   1 
ATOM   2377 C CA  . ILE B 1 92  ? 4.10933  12.48754  -4.43451  1.000 41.63139  ? 92  ILE A CA  1 
ATOM   2378 C C   . ILE B 1 92  ? 2.70090  12.28923  -3.86254  1.000 43.27011  ? 92  ILE A C   1 
ATOM   2379 O O   . ILE B 1 92  ? 2.48333  11.38655  -3.04268  1.000 44.44742  ? 92  ILE A O   1 
ATOM   2380 C CB  . ILE B 1 92  ? 4.99204  13.40060  -3.55774  1.000 37.74265  ? 92  ILE A CB  1 
ATOM   2381 C CG1 . ILE B 1 92  ? 5.56738  12.63946  -2.35013  1.000 39.94115  ? 92  ILE A CG1 1 
ATOM   2382 C CG2 . ILE B 1 92  ? 4.24806  14.63796  -3.10924  1.000 34.52195  ? 92  ILE A CG2 1 
ATOM   2383 C CD1 . ILE B 1 92  ? 6.38216  11.42341  -2.68668  1.000 34.87352  ? 92  ILE A CD1 1 
ATOM   2384 N N   . ALA B 1 93  ? 1.71999  13.09222  -4.29335  1.000 39.32949  ? 93  ALA A N   1 
ATOM   2385 C CA  . ALA B 1 93  ? 0.33465  12.81401  -3.90464  1.000 42.27136  ? 93  ALA A CA  1 
ATOM   2386 C C   . ALA B 1 93  ? -0.13245 11.47611  -4.46613  1.000 40.47925  ? 93  ALA A C   1 
ATOM   2387 O O   . ALA B 1 93  ? -0.72324 10.66808  -3.74188  1.000 43.57612  ? 93  ALA A O   1 
ATOM   2388 C CB  . ALA B 1 93  ? -0.60389 13.93488  -4.34976  1.000 39.10112  ? 93  ALA A CB  1 
ATOM   2389 N N   . LYS B 1 94  ? 0.14414  11.20439  -5.74996  1.000 41.19319  ? 94  LYS A N   1 
ATOM   2390 C CA  . LYS B 1 94  ? -0.20238 9.88619   -6.28630  1.000 40.13871  ? 94  LYS A CA  1 
ATOM   2391 C C   . LYS B 1 94  ? 0.47256  8.78519   -5.49057  1.000 43.36111  ? 94  LYS A C   1 
ATOM   2392 O O   . LYS B 1 94  ? -0.16035 7.77169   -5.15855  1.000 47.75213  ? 94  LYS A O   1 
ATOM   2393 C CB  . LYS B 1 94  ? 0.16098  9.76439   -7.77175  1.000 42.99549  ? 94  LYS A CB  1 
ATOM   2394 C CG  . LYS B 1 94  ? -0.47958 10.81920  -8.67510  1.000 47.36723  ? 94  LYS A CG  1 
ATOM   2395 C CD  . LYS B 1 94  ? 0.09724  10.78854  -10.08390 1.000 49.86627  ? 94  LYS A CD  1 
ATOM   2396 C CE  . LYS B 1 94  ? -0.97911 11.04917  -11.15393 1.000 51.49379  ? 94  LYS A CE  1 
ATOM   2397 N NZ  . LYS B 1 94  ? -2.07178 10.00934  -11.19394 1.000 62.64258  ? 94  LYS A NZ  1 
ATOM   2398 N N   . PHE B 1 95  ? 1.74767  8.99258   -5.13560  1.000 44.41504  ? 95  PHE A N   1 
ATOM   2399 C CA  . PHE B 1 95  ? 2.49816  8.00132   -4.37052  1.000 39.01380  ? 95  PHE A CA  1 
ATOM   2400 C C   . PHE B 1 95  ? 1.83214  7.71298   -3.03420  1.000 39.60709  ? 95  PHE A C   1 
ATOM   2401 O O   . PHE B 1 95  ? 1.68689  6.55051   -2.64773  1.000 43.49109  ? 95  PHE A O   1 
ATOM   2402 C CB  . PHE B 1 95  ? 3.95147  8.45997   -4.14195  1.000 38.38252  ? 95  PHE A CB  1 
ATOM   2403 C CG  . PHE B 1 95  ? 4.71513  7.53550   -3.23536  1.000 31.87663  ? 95  PHE A CG  1 
ATOM   2404 C CD1 . PHE B 1 95  ? 5.32710  6.39922   -3.74484  1.000 33.52413  ? 95  PHE A CD1 1 
ATOM   2405 C CD2 . PHE B 1 95  ? 4.74016  7.75356   -1.86390  1.000 29.39403  ? 95  PHE A CD2 1 
ATOM   2406 C CE1 . PHE B 1 95  ? 5.97779  5.50961   -2.91412  1.000 33.49121  ? 95  PHE A CE1 1 
ATOM   2407 C CE2 . PHE B 1 95  ? 5.39308  6.86652   -1.02612  1.000 34.36410  ? 95  PHE A CE2 1 
ATOM   2408 C CZ  . PHE B 1 95  ? 6.01562  5.73983   -1.55657  1.000 32.23772  ? 95  PHE A CZ  1 
ATOM   2409 N N   . ASN B 1 96  ? 1.45520  8.75880   -2.29055  1.000 39.32825  ? 96  ASN A N   1 
ATOM   2410 C CA  . ASN B 1 96  ? 0.77497  8.52638   -1.01904  1.000 43.01470  ? 96  ASN A CA  1 
ATOM   2411 C C   . ASN B 1 96  ? -0.55352 7.79371   -1.21691  1.000 46.72879  ? 96  ASN A C   1 
ATOM   2412 O O   . ASN B 1 96  ? -0.88100 6.88028   -0.44693  1.000 43.73360  ? 96  ASN A O   1 
ATOM   2413 C CB  . ASN B 1 96  ? 0.54287  9.83795   -0.28245  1.000 41.66931  ? 96  ASN A CB  1 
ATOM   2414 C CG  . ASN B 1 96  ? 1.81175  10.44678  0.20339   1.000 46.55303  ? 96  ASN A CG  1 
ATOM   2415 O OD1 . ASN B 1 96  ? 2.87003  9.81725   0.15393   1.000 48.81177  ? 96  ASN A OD1 1 
ATOM   2416 N ND2 . ASN B 1 96  ? 1.73125  11.67312  0.68862   1.000 46.70721  ? 96  ASN A ND2 1 
ATOM   2417 N N   . ASP B 1 97  ? -1.32910 8.17381   -2.24285  1.000 43.86593  ? 97  ASP A N   1 
ATOM   2418 C CA  . ASP B 1 97  ? -2.60037 7.49161   -2.49055  1.000 46.67561  ? 97  ASP A CA  1 
ATOM   2419 C C   . ASP B 1 97  ? -2.40197 6.00247   -2.70463  1.000 48.18071  ? 97  ASP A C   1 
ATOM   2420 O O   . ASP B 1 97  ? -3.19330 5.19034   -2.21276  1.000 44.92993  ? 97  ASP A O   1 
ATOM   2421 C CB  . ASP B 1 97  ? -3.31808 8.07151   -3.70496  1.000 39.65202  ? 97  ASP A CB  1 
ATOM   2422 C CG  . ASP B 1 97  ? -3.79163 9.45947   -3.47404  1.000 43.58009  ? 97  ASP A CG  1 
ATOM   2423 O OD1 . ASP B 1 97  ? -3.92463 9.84764   -2.28916  1.000 47.07064  ? 97  ASP A OD1 1 
ATOM   2424 O OD2 . ASP B 1 97  ? -4.06724 10.14977  -4.47709  1.000 52.60703  ? 97  ASP A OD2 1 
ATOM   2425 N N   . TYR B 1 98  ? -1.37103 5.62113   -3.46208  1.000 44.90248  ? 98  TYR A N   1 
ATOM   2426 C CA  . TYR B 1 98  ? -1.15333 4.19780   -3.68147  1.000 45.44864  ? 98  TYR A CA  1 
ATOM   2427 C C   . TYR B 1 98  ? -0.89620 3.49421   -2.35444  1.000 49.69680  ? 98  TYR A C   1 
ATOM   2428 O O   . TYR B 1 98  ? -1.51898 2.46806   -2.05878  1.000 53.96368  ? 98  TYR A O   1 
ATOM   2429 C CB  . TYR B 1 98  ? 0.00519  3.98741   -4.66041  1.000 43.53452  ? 98  TYR A CB  1 
ATOM   2430 C CG  . TYR B 1 98  ? 0.40949  2.54635   -4.92835  1.000 47.59213  ? 98  TYR A CG  1 
ATOM   2431 C CD1 . TYR B 1 98  ? 1.29738  1.88688   -4.08650  1.000 46.32042  ? 98  TYR A CD1 1 
ATOM   2432 C CD2 . TYR B 1 98  ? -0.03534 1.86875   -6.06707  1.000 49.81391  ? 98  TYR A CD2 1 
ATOM   2433 C CE1 . TYR B 1 98  ? 1.70494  0.57863   -4.34066  1.000 48.44233  ? 98  TYR A CE1 1 
ATOM   2434 C CE2 . TYR B 1 98  ? 0.36215  0.55363   -6.33066  1.000 48.57089  ? 98  TYR A CE2 1 
ATOM   2435 C CZ  . TYR B 1 98  ? 1.24316  -0.08388  -5.46304  1.000 52.64908  ? 98  TYR A CZ  1 
ATOM   2436 O OH  . TYR B 1 98  ? 1.65668  -1.38657  -5.70118  1.000 51.16372  ? 98  TYR A OH  1 
ATOM   2437 N N   . ILE B 1 99  ? -0.02811 4.06594   -1.51458  1.000 45.93888  ? 99  ILE A N   1 
ATOM   2438 C CA  . ILE B 1 99  ? 0.30149  3.43143   -0.24111  1.000 47.82531  ? 99  ILE A CA  1 
ATOM   2439 C C   . ILE B 1 99  ? -0.96044 3.26590   0.61053   1.000 48.70633  ? 99  ILE A C   1 
ATOM   2440 O O   . ILE B 1 99  ? -1.23293 2.18644   1.15104   1.000 47.06927  ? 99  ILE A O   1 
ATOM   2441 C CB  . ILE B 1 99  ? 1.39366  4.23936   0.48777   1.000 44.81809  ? 99  ILE A CB  1 
ATOM   2442 C CG1 . ILE B 1 99  ? 2.67091  4.32328   -0.36024  1.000 42.59593  ? 99  ILE A CG1 1 
ATOM   2443 C CG2 . ILE B 1 99  ? 1.75380  3.58990   1.80141   1.000 48.90477  ? 99  ILE A CG2 1 
ATOM   2444 C CD1 . ILE B 1 99  ? 3.43109  2.99313   -0.49839  1.000 43.17638  ? 99  ILE A CD1 1 
ATOM   2445 N N   . ASN B 1 100 ? -1.76604 4.32398   0.71577   1.000 43.06620  ? 100 ASN A N   1 
ATOM   2446 C CA  . ASN B 1 100 ? -2.97548 4.25923   1.53341   1.000 48.22512  ? 100 ASN A CA  1 
ATOM   2447 C C   . ASN B 1 100 ? -3.98258 3.22833   1.02123   1.000 53.25683  ? 100 ASN A C   1 
ATOM   2448 O O   . ASN B 1 100 ? -4.80209 2.73513   1.79949   1.000 52.03799  ? 100 ASN A O   1 
ATOM   2449 C CB  . ASN B 1 100 ? -3.64627 5.62742   1.58819   1.000 45.12283  ? 100 ASN A CB  1 
ATOM   2450 C CG  . ASN B 1 100 ? -2.82131 6.65674   2.33142   1.000 54.30074  ? 100 ASN A CG  1 
ATOM   2451 O OD1 . ASN B 1 100 ? -2.00403 6.32124   3.19257   1.000 54.21830  ? 100 ASN A OD1 1 
ATOM   2452 N ND2 . ASN B 1 100 ? -3.04652 7.92995   2.01332   1.000 53.97784  ? 100 ASN A ND2 1 
ATOM   2453 N N   . ALA B 1 101 ? -3.92603 2.88586   -0.25905  1.000 49.45043  ? 101 ALA A N   1 
ATOM   2454 C CA  . ALA B 1 101 ? -4.86188 1.98011   -0.89447  1.000 49.88372  ? 101 ALA A CA  1 
ATOM   2455 C C   . ALA B 1 101 ? -4.33860 0.55113   -1.01959  1.000 53.94244  ? 101 ALA A C   1 
ATOM   2456 O O   . ALA B 1 101 ? -5.00209 -0.27311  -1.65517  1.000 53.59483  ? 101 ALA A O   1 
ATOM   2457 C CB  . ALA B 1 101 ? -5.22708 2.51943   -2.28514  1.000 46.54631  ? 101 ALA A CB  1 
ATOM   2458 N N   . HIS B 1 102 ? -3.17680 0.22499   -0.44300  1.000 51.88678  ? 102 HIS A N   1 
ATOM   2459 C CA  . HIS B 1 102 ? -2.55565 -1.06989  -0.74281  1.000 53.00070  ? 102 HIS A CA  1 
ATOM   2460 C C   . HIS B 1 102 ? -2.05793 -1.79552  0.50046   1.000 55.82751  ? 102 HIS A C   1 
ATOM   2461 O O   . HIS B 1 102 ? -1.03565 -2.49266  0.45368   1.000 58.24088  ? 102 HIS A O   1 
ATOM   2462 C CB  . HIS B 1 102 ? -1.40775 -0.92751  -1.73012  1.000 48.74215  ? 102 HIS A CB  1 
ATOM   2463 C CG  . HIS B 1 102 ? -1.80903 -1.09377  -3.15583  1.000 51.67435  ? 102 HIS A CG  1 
ATOM   2464 N ND1 . HIS B 1 102 ? -2.41186 -0.08915  -3.88233  1.000 53.12088  ? 102 HIS A ND1 1 
ATOM   2465 C CD2 . HIS B 1 102 ? -1.69868 -2.15438  -3.99143  1.000 51.64836  ? 102 HIS A CD2 1 
ATOM   2466 C CE1 . HIS B 1 102 ? -2.64657 -0.52092  -5.10979  1.000 52.29373  ? 102 HIS A CE1 1 
ATOM   2467 N NE2 . HIS B 1 102 ? -2.22256 -1.77018  -5.20199  1.000 53.87492  ? 102 HIS A NE2 1 
ATOM   2468 N N   . ASN B 1 103 ? -2.77159 -1.66390  1.61962   1.000 54.04747  ? 103 ASN A N   1 
ATOM   2469 C CA  . ASN B 1 103 ? -2.57746 -2.54238  2.77284   1.000 54.29144  ? 103 ASN A CA  1 
ATOM   2470 C C   . ASN B 1 103 ? -1.16098 -2.41841  3.32660   1.000 62.08122  ? 103 ASN A C   1 
ATOM   2471 O O   . ASN B 1 103 ? -0.46335 -3.41690  3.55578   1.000 60.12741  ? 103 ASN A O   1 
ATOM   2472 C CB  . ASN B 1 103 ? -2.89953 -3.99461  2.40948   1.000 58.06500  ? 103 ASN A CB  1 
ATOM   2473 N N   . ILE B 1 104 ? -0.73205 -1.17078  3.51369   1.000 56.08126  ? 104 ILE A N   1 
ATOM   2474 C CA  . ILE B 1 104 ? 0.57835  -0.84439  4.05851   1.000 50.09016  ? 104 ILE A CA  1 
ATOM   2475 C C   . ILE B 1 104 ? 0.36921  -0.35466  5.48490   1.000 51.28209  ? 104 ILE A C   1 
ATOM   2476 O O   . ILE B 1 104 ? -0.37729 0.60412   5.71680   1.000 51.84870  ? 104 ILE A O   1 
ATOM   2477 C CB  . ILE B 1 104 ? 1.28669  0.22288   3.20258   1.000 53.27217  ? 104 ILE A CB  1 
ATOM   2478 C CG1 . ILE B 1 104 ? 1.24256  -0.15354  1.71433   1.000 50.37905  ? 104 ILE A CG1 1 
ATOM   2479 C CG2 . ILE B 1 104 ? 2.72817  0.47420   3.68834   1.000 51.79819  ? 104 ILE A CG2 1 
ATOM   2480 C CD1 . ILE B 1 104 ? 2.28856  -1.15090  1.28599   1.000 48.81978  ? 104 ILE A CD1 1 
ATOM   2481 N N   . ASP B 1 105 ? 1.02179  -0.98857  6.44996   1.000 47.72262  ? 105 ASP A N   1 
ATOM   2482 C CA  . ASP B 1 105 ? 0.87181  -0.54267  7.82605   1.000 52.47347  ? 105 ASP A CA  1 
ATOM   2483 C C   . ASP B 1 105 ? 1.94866  0.48463   8.16055   1.000 54.20952  ? 105 ASP A C   1 
ATOM   2484 O O   . ASP B 1 105 ? 3.14167  0.14424   8.14066   1.000 51.67950  ? 105 ASP A O   1 
ATOM   2485 C CB  . ASP B 1 105 ? 0.93696  -1.72136  8.78179   1.000 50.75939  ? 105 ASP A CB  1 
ATOM   2486 C CG  . ASP B 1 105 ? 0.87107  -1.29999  10.24103  1.000 56.91106  ? 105 ASP A CG  1 
ATOM   2487 O OD1 . ASP B 1 105 ? 0.54463  -0.12886  10.53245  1.000 58.14492  ? 105 ASP A OD1 1 
ATOM   2488 O OD2 . ASP B 1 105 ? 1.13246  -2.15471  11.11016  1.000 66.33479  ? 105 ASP A OD2 1 
ATOM   2489 N N   . PRO B 1 106 ? 1.57769  1.72393   8.50697   1.000 53.73327  ? 106 PRO A N   1 
ATOM   2490 C CA  . PRO B 1 106 ? 2.59047  2.76541   8.78290   1.000 52.56408  ? 106 PRO A CA  1 
ATOM   2491 C C   . PRO B 1 106 ? 3.59936  2.39400   9.85306   1.000 55.35013  ? 106 PRO A C   1 
ATOM   2492 O O   . PRO B 1 106 ? 4.66947  3.02249   9.91289   1.000 55.37762  ? 106 PRO A O   1 
ATOM   2493 C CB  . PRO B 1 106 ? 1.74887  3.96980   9.23417   1.000 46.34434  ? 106 PRO A CB  1 
ATOM   2494 C CG  . PRO B 1 106 ? 0.40303  3.75538   8.57913   1.000 49.85006  ? 106 PRO A CG  1 
ATOM   2495 C CD  . PRO B 1 106 ? 0.20266  2.24994   8.55226   1.000 48.34197  ? 106 PRO A CD  1 
ATOM   2496 N N   . TRP B 1 107 ? 3.29819  1.42202   10.71571  1.000 51.14021  ? 107 TRP A N   1 
ATOM   2497 C CA  . TRP B 1 107 ? 4.21261  1.07238   11.78723  1.000 49.81384  ? 107 TRP A CA  1 
ATOM   2498 C C   . TRP B 1 107 ? 4.89621  -0.26922  11.61181  1.000 45.35486  ? 107 TRP A C   1 
ATOM   2499 O O   . TRP B 1 107 ? 5.85884  -0.53794  12.32624  1.000 49.45225  ? 107 TRP A O   1 
ATOM   2500 C CB  . TRP B 1 107 ? 3.48862  1.07618   13.13800  1.000 49.54008  ? 107 TRP A CB  1 
ATOM   2501 C CG  . TRP B 1 107 ? 3.05875  2.43111   13.58124  1.000 54.41229  ? 107 TRP A CG  1 
ATOM   2502 C CD1 . TRP B 1 107 ? 1.88249  3.05819   13.28161  1.000 55.94346  ? 107 TRP A CD1 1 
ATOM   2503 C CD2 . TRP B 1 107 ? 3.79867  3.34047   14.41068  1.000 56.22976  ? 107 TRP A CD2 1 
ATOM   2504 N NE1 . TRP B 1 107 ? 1.84355  4.30345   13.87001  1.000 56.12392  ? 107 TRP A NE1 1 
ATOM   2505 C CE2 . TRP B 1 107 ? 3.00423  4.50084   14.57069  1.000 50.88130  ? 107 TRP A CE2 1 
ATOM   2506 C CE3 . TRP B 1 107 ? 5.06140  3.29275   15.02279  1.000 54.11793  ? 107 TRP A CE3 1 
ATOM   2507 C CZ2 . TRP B 1 107 ? 3.42563  5.59897   15.32305  1.000 50.97580  ? 107 TRP A CZ2 1 
ATOM   2508 C CZ3 . TRP B 1 107 ? 5.47810  4.38566   15.77599  1.000 50.75540  ? 107 TRP A CZ3 1 
ATOM   2509 C CH2 . TRP B 1 107 ? 4.66229  5.51993   15.91937  1.000 53.49819  ? 107 TRP A CH2 1 
ATOM   2510 N N   . LYS B 1 108 ? 4.44091  -1.11341  10.69865  1.000 47.69108  ? 108 LYS A N   1 
ATOM   2511 C CA  . LYS B 1 108 ? 4.91882  -2.48934  10.62802  1.000 47.53691  ? 108 LYS A CA  1 
ATOM   2512 C C   . LYS B 1 108 ? 5.36922  -2.90239  9.24035   1.000 50.83295  ? 108 LYS A C   1 
ATOM   2513 O O   . LYS B 1 108 ? 6.13531  -3.87061  9.11874   1.000 49.17958  ? 108 LYS A O   1 
ATOM   2514 C CB  . LYS B 1 108 ? 3.82135  -3.46151  11.07934  1.000 55.81925  ? 108 LYS A CB  1 
ATOM   2515 C CG  . LYS B 1 108 ? 3.86939  -3.88626  12.53583  1.000 58.54109  ? 108 LYS A CG  1 
ATOM   2516 C CD  . LYS B 1 108 ? 2.49972  -4.39938  12.97263  1.000 60.53841  ? 108 LYS A CD  1 
ATOM   2517 C CE  . LYS B 1 108 ? 2.60709  -5.40957  14.12639  1.000 68.10409  ? 108 LYS A CE  1 
ATOM   2518 N NZ  . LYS B 1 108 ? 1.70168  -6.59337  13.93999  1.000 67.62268  ? 108 LYS A NZ  1 
ATOM   2519 N N   . SER B 1 109 ? 4.91624  -2.22333  8.19293   1.000 48.10449  ? 109 SER A N   1 
ATOM   2520 C CA  . SER B 1 109 ? 5.40840  -2.51679  6.86061   1.000 50.55630  ? 109 SER A CA  1 
ATOM   2521 C C   . SER B 1 109 ? 6.88632  -2.09526  6.72242   1.000 45.07548  ? 109 SER A C   1 
ATOM   2522 O O   . SER B 1 109 ? 7.43248  -1.34290  7.53157   1.000 45.38521  ? 109 SER A O   1 
ATOM   2523 C CB  . SER B 1 109 ? 4.52881  -1.81505  5.83532   1.000 46.97494  ? 109 SER A CB  1 
ATOM   2524 O OG  . SER B 1 109 ? 3.30189  -2.50912  5.71211   1.000 54.38941  ? 109 SER A OG  1 
ATOM   2525 N N   . GLN B 1 110 ? 7.53356  -2.60526  5.68377   1.000 37.73627  ? 110 GLN A N   1 
ATOM   2526 C CA  . GLN B 1 110 ? 8.90223  -2.25524  5.35309   1.000 47.20569  ? 110 GLN A CA  1 
ATOM   2527 C C   . GLN B 1 110 ? 8.93708  -1.71062  3.93269   1.000 46.05366  ? 110 GLN A C   1 
ATOM   2528 O O   . GLN B 1 110 ? 8.20809  -2.19310  3.06095   1.000 45.88065  ? 110 GLN A O   1 
ATOM   2529 C CB  . GLN B 1 110 ? 9.83493  -3.47788  5.48368   1.000 44.25618  ? 110 GLN A CB  1 
ATOM   2530 C CG  . GLN B 1 110 ? 10.22588 -3.80988  6.92615   1.000 44.04526  ? 110 GLN A CG  1 
ATOM   2531 C CD  . GLN B 1 110 ? 10.85820 -5.18827  7.04164   1.000 47.33608  ? 110 GLN A CD  1 
ATOM   2532 O OE1 . GLN B 1 110 ? 11.14811 -5.82505  6.03179   1.000 46.14451  ? 110 GLN A OE1 1 
ATOM   2533 N NE2 . GLN B 1 110 ? 11.06212 -5.66000  8.27436   1.000 48.96529  ? 110 GLN A NE2 1 
ATOM   2534 N N   . GLY B 1 111 ? 9.77123  -0.70093  3.70288   1.000 44.95260  ? 111 GLY A N   1 
ATOM   2535 C CA  . GLY B 1 111 ? 9.99305  -0.15318  2.36561   1.000 46.99390  ? 111 GLY A CA  1 
ATOM   2536 C C   . GLY B 1 111 ? 11.37553 -0.52235  1.86115   1.000 43.25232  ? 111 GLY A C   1 
ATOM   2537 O O   . GLY B 1 111 ? 12.34900 -0.46792  2.61609   1.000 42.62144  ? 111 GLY A O   1 
ATOM   2538 N N   . TRP B 1 112 ? 11.45777 -0.89571  0.57961   1.000 41.29441  ? 112 TRP A N   1 
ATOM   2539 C CA  . TRP B 1 112 ? 12.66710 -1.46557  -0.00742  1.000 43.55859  ? 112 TRP A CA  1 
ATOM   2540 C C   . TRP B 1 112 ? 13.05343 -0.67908  -1.25044  1.000 43.90218  ? 112 TRP A C   1 
ATOM   2541 O O   . TRP B 1 112 ? 12.17918 -0.24861  -2.01565  1.000 36.69486  ? 112 TRP A O   1 
ATOM   2542 C CB  . TRP B 1 112 ? 12.49298 -2.96301  -0.41920  1.000 44.05438  ? 112 TRP A CB  1 
ATOM   2543 C CG  . TRP B 1 112 ? 12.19264 -3.92441  0.70798   1.000 48.03917  ? 112 TRP A CG  1 
ATOM   2544 C CD1 . TRP B 1 112 ? 10.95691 -4.18741  1.26296   1.000 46.06983  ? 112 TRP A CD1 1 
ATOM   2545 C CD2 . TRP B 1 112 ? 13.12649 -4.77629  1.39062   1.000 47.41800  ? 112 TRP A CD2 1 
ATOM   2546 N NE1 . TRP B 1 112 ? 11.08591 -5.12200  2.26996   1.000 45.68725  ? 112 TRP A NE1 1 
ATOM   2547 C CE2 . TRP B 1 112 ? 12.39973 -5.50141  2.36646   1.000 45.70067  ? 112 TRP A CE2 1 
ATOM   2548 C CE3 . TRP B 1 112 ? 14.50543 -4.99700  1.27494   1.000 47.29636  ? 112 TRP A CE3 1 
ATOM   2549 C CZ2 . TRP B 1 112 ? 13.01133 -6.42532  3.22358   1.000 49.70340  ? 112 TRP A CZ2 1 
ATOM   2550 C CZ3 . TRP B 1 112 ? 15.11206 -5.92512  2.12752   1.000 46.12912  ? 112 TRP A CZ3 1 
ATOM   2551 C CH2 . TRP B 1 112 ? 14.36487 -6.62419  3.08894   1.000 46.43954  ? 112 TRP A CH2 1 
ATOM   2552 N N   . CYS B 1 113 ? 14.36702 -0.53571  -1.46151  1.000 40.19195  ? 113 CYS A N   1 
ATOM   2553 C CA  . CYS B 1 113 ? 14.90166 0.02193   -2.69909  1.000 40.70467  ? 113 CYS A CA  1 
ATOM   2554 C C   . CYS B 1 113 ? 16.31221 -0.50913  -2.90195  1.000 42.29588  ? 113 CYS A C   1 
ATOM   2555 O O   . CYS B 1 113 ? 16.94277 -1.01493  -1.96833  1.000 41.07548  ? 113 CYS A O   1 
ATOM   2556 C CB  . CYS B 1 113 ? 14.88551 1.55389   -2.68053  1.000 41.68971  ? 113 CYS A CB  1 
ATOM   2557 S SG  . CYS B 1 113 ? 16.14869 2.28122   -1.61306  1.000 44.62008  ? 113 CYS A SG  1 
ATOM   2558 N N   . ARG B 1 114 ? 16.79221 -0.40042  -4.14497  1.000 42.58540  ? 114 ARG A N   1 
ATOM   2559 C CA  . ARG B 1 114 ? 18.11196 -0.91309  -4.52202  1.000 42.46588  ? 114 ARG A CA  1 
ATOM   2560 C C   . ARG B 1 114 ? 19.17682 0.14153   -4.22929  1.000 44.51970  ? 114 ARG A C   1 
ATOM   2561 O O   . ARG B 1 114 ? 19.77467 0.74799   -5.12494  1.000 45.25907  ? 114 ARG A O   1 
ATOM   2562 C CB  . ARG B 1 114 ? 18.13978 -1.33610  -5.98517  1.000 38.42437  ? 114 ARG A CB  1 
ATOM   2563 C CG  . ARG B 1 114 ? 19.43169 -2.10615  -6.34546  1.000 42.78748  ? 114 ARG A CG  1 
ATOM   2564 C CD  . ARG B 1 114 ? 19.29742 -2.90984  -7.62720  1.000 40.10606  ? 114 ARG A CD  1 
ATOM   2565 N NE  . ARG B 1 114 ? 18.73173 -4.23646  -7.40436  1.000 49.06927  ? 114 ARG A NE  1 
ATOM   2566 C CZ  . ARG B 1 114 ? 19.44102 -5.30596  -7.05986  1.000 49.72219  ? 114 ARG A CZ  1 
ATOM   2567 N NH1 . ARG B 1 114 ? 20.74504 -5.23421  -6.85610  1.000 41.67412  ? 114 ARG A NH1 1 
ATOM   2568 N NH2 . ARG B 1 114 ? 18.82529 -6.47758  -6.91644  1.000 51.11882  ? 114 ARG A NH2 1 
ATOM   2569 N N   . GLY B 1 115 ? 19.44962 0.30525   -2.93349  1.000 45.33395  ? 115 GLY A N   1 
ATOM   2570 C CA  . GLY B 1 115 ? 20.36776 1.32782   -2.45995  1.000 43.69235  ? 115 GLY A CA  1 
ATOM   2571 C C   . GLY B 1 115 ? 19.61002 2.33083   -1.61792  1.000 43.13140  ? 115 GLY A C   1 
ATOM   2572 O O   . GLY B 1 115 ? 19.11945 3.32849   -2.15380  1.000 43.82662  ? 115 GLY A O   1 
ATOM   2573 N N   . MET B 1 116 ? 19.46878 2.05397   -0.31490  1.000 40.29511  ? 116 MET A N   1 
ATOM   2574 C CA  . MET B 1 116 ? 18.65399 2.90330   0.55159   1.000 37.69519  ? 116 MET A CA  1 
ATOM   2575 C C   . MET B 1 116 ? 19.08967 4.35677   0.49237   1.000 36.52998  ? 116 MET A C   1 
ATOM   2576 O O   . MET B 1 116 ? 18.25301 5.26813   0.55699   1.000 42.54419  ? 116 MET A O   1 
ATOM   2577 C CB  . MET B 1 116 ? 18.71694 2.42016   2.00315   1.000 40.08107  ? 116 MET A CB  1 
ATOM   2578 C CG  . MET B 1 116 ? 17.52796 1.62366   2.48692   1.000 41.87688  ? 116 MET A CG  1 
ATOM   2579 S SD  . MET B 1 116 ? 17.83170 0.87854   4.11354   1.000 45.66707  ? 116 MET A SD  1 
ATOM   2580 C CE  . MET B 1 116 ? 17.90387 2.36733   5.12833   1.000 41.90692  ? 116 MET A CE  1 
ATOM   2581 N N   . SER B 1 117 ? 20.39629 4.60205   0.39271   1.000 38.56483  ? 117 SER A N   1 
ATOM   2582 C CA  . SER B 1 117 ? 20.88008 5.97627   0.41488   1.000 33.42955  ? 117 SER A CA  1 
ATOM   2583 C C   . SER B 1 117 ? 20.49592 6.74231   -0.84046  1.000 32.99023  ? 117 SER A C   1 
ATOM   2584 O O   . SER B 1 117 ? 20.74005 7.94666   -0.91819  1.000 32.78012  ? 117 SER A O   1 
ATOM   2585 C CB  . SER B 1 117 ? 22.40120 6.00146   0.57471   1.000 35.37183  ? 117 SER A CB  1 
ATOM   2586 O OG  . SER B 1 117 ? 23.00185 5.18176   -0.41196  1.000 35.83449  ? 117 SER A OG  1 
ATOM   2587 N N   . PHE B 1 118 ? 19.92430 6.08775   -1.83937  1.000 34.26826  ? 118 PHE A N   1 
ATOM   2588 C CA  . PHE B 1 118 ? 19.56947 6.81365   -3.04429  1.000 40.00185  ? 118 PHE A CA  1 
ATOM   2589 C C   . PHE B 1 118 ? 18.07130 7.14385   -3.10692  1.000 35.91395  ? 118 PHE A C   1 
ATOM   2590 O O   . PHE B 1 118 ? 17.71911 8.31963   -3.18475  1.000 37.85094  ? 118 PHE A O   1 
ATOM   2591 C CB  . PHE B 1 118 ? 20.04906 6.03710   -4.27952  1.000 38.25836  ? 118 PHE A CB  1 
ATOM   2592 C CG  . PHE B 1 118 ? 19.86619 6.79984   -5.56077  1.000 41.34076  ? 118 PHE A CG  1 
ATOM   2593 C CD1 . PHE B 1 118 ? 18.65734 6.73413   -6.26340  1.000 32.05218  ? 118 PHE A CD1 1 
ATOM   2594 C CD2 . PHE B 1 118 ? 20.88263 7.59408   -6.05513  1.000 32.24034  ? 118 PHE A CD2 1 
ATOM   2595 C CE1 . PHE B 1 118 ? 18.48603 7.45444   -7.43877  1.000 35.45653  ? 118 PHE A CE1 1 
ATOM   2596 C CE2 . PHE B 1 118 ? 20.70684 8.32001   -7.22489  1.000 37.30481  ? 118 PHE A CE2 1 
ATOM   2597 C CZ  . PHE B 1 118 ? 19.51666 8.25905   -7.92000  1.000 36.85291  ? 118 PHE A CZ  1 
ATOM   2598 N N   . ASP B 1 119 ? 17.17841 6.14558   -3.05014  1.000 34.37765  ? 119 ASP A N   1 
ATOM   2599 C CA  . ASP B 1 119 ? 15.74732 6.41312   -3.31455  1.000 40.28553  ? 119 ASP A CA  1 
ATOM   2600 C C   . ASP B 1 119 ? 15.03342 7.04394   -2.12510  1.000 33.46809  ? 119 ASP A C   1 
ATOM   2601 O O   . ASP B 1 119 ? 14.34267 8.05453   -2.26971  1.000 32.81481  ? 119 ASP A O   1 
ATOM   2602 C CB  . ASP B 1 119 ? 15.02721 5.13017   -3.71847  1.000 37.76330  ? 119 ASP A CB  1 
ATOM   2603 C CG  . ASP B 1 119 ? 15.66384 4.49357   -4.92722  1.000 40.79006  ? 119 ASP A CG  1 
ATOM   2604 O OD1 . ASP B 1 119 ? 16.59396 3.68314   -4.70084  1.000 37.84397  ? 119 ASP A OD1 1 
ATOM   2605 O OD2 . ASP B 1 119 ? 15.26742 4.83375   -6.08024  1.000 36.97988  ? 119 ASP A OD2 1 
ATOM   2606 N N   . PHE B 1 120 ? 15.21190 6.47552   -0.94382  1.000 33.36826  ? 120 PHE A N   1 
ATOM   2607 C CA  . PHE B 1 120 ? 14.55106 7.01359   0.23740   1.000 33.03262  ? 120 PHE A CA  1 
ATOM   2608 C C   . PHE B 1 120 ? 14.87977 8.46851   0.53901   1.000 34.75095  ? 120 PHE A C   1 
ATOM   2609 O O   . PHE B 1 120 ? 13.95375 9.19723   0.92998   1.000 34.78459  ? 120 PHE A O   1 
ATOM   2610 C CB  . PHE B 1 120 ? 14.82521 6.08513   1.43347   1.000 34.89136  ? 120 PHE A CB  1 
ATOM   2611 C CG  . PHE B 1 120 ? 13.88998 4.90289   1.46008   1.000 41.82325  ? 120 PHE A CG  1 
ATOM   2612 C CD1 . PHE B 1 120 ? 12.50810 5.10122   1.66444   1.000 38.76089  ? 120 PHE A CD1 1 
ATOM   2613 C CD2 . PHE B 1 120 ? 14.34934 3.62267   1.18916   1.000 40.38301  ? 120 PHE A CD2 1 
ATOM   2614 C CE1 . PHE B 1 120 ? 11.62081 4.01958   1.64642   1.000 43.23912  ? 120 PHE A CE1 1 
ATOM   2615 C CE2 . PHE B 1 120 ? 13.47351 2.54094   1.16975   1.000 38.59241  ? 120 PHE A CE2 1 
ATOM   2616 C CZ  . PHE B 1 120 ? 12.11270 2.73477   1.40308   1.000 46.86960  ? 120 PHE A CZ  1 
ATOM   2617 N N   . PRO B 1 121 ? 16.12440 8.95953   0.42833   1.000 37.07100  ? 121 PRO A N   1 
ATOM   2618 C CA  . PRO B 1 121 ? 16.32215 10.40398  0.67887   1.000 31.13193  ? 121 PRO A CA  1 
ATOM   2619 C C   . PRO B 1 121 ? 15.60451 11.29262  -0.32627  1.000 34.70137  ? 121 PRO A C   1 
ATOM   2620 O O   . PRO B 1 121 ? 15.08129 12.34841  0.04386   1.000 37.03714  ? 121 PRO A O   1 
ATOM   2621 C CB  . PRO B 1 121 ? 17.84274 10.56676  0.61867   1.000 34.30872  ? 121 PRO A CB  1 
ATOM   2622 C CG  . PRO B 1 121 ? 18.37324 9.21482   1.06352   1.000 34.39462  ? 121 PRO A CG  1 
ATOM   2623 C CD  . PRO B 1 121 ? 17.41334 8.23025   0.40853   1.000 36.74675  ? 121 PRO A CD  1 
ATOM   2624 N N   . ILE B 1 122 ? 15.51780 10.87837  -1.58471  1.000 36.75709  ? 122 ILE A N   1 
ATOM   2625 C CA  . ILE B 1 122 ? 14.72595 11.63261  -2.55111  1.000 37.16253  ? 122 ILE A CA  1 
ATOM   2626 C C   . ILE B 1 122 ? 13.23653 11.55573  -2.20354  1.000 37.19741  ? 122 ILE A C   1 
ATOM   2627 O O   . ILE B 1 122 ? 12.55053 12.57714  -2.12806  1.000 35.72462  ? 122 ILE A O   1 
ATOM   2628 C CB  . ILE B 1 122 ? 15.00341 11.12556  -3.97254  1.000 37.14036  ? 122 ILE A CB  1 
ATOM   2629 C CG1 . ILE B 1 122 ? 16.51146 11.19865  -4.27667  1.000 32.34803  ? 122 ILE A CG1 1 
ATOM   2630 C CG2 . ILE B 1 122 ? 14.16957 11.91908  -4.97862  1.000 31.63581  ? 122 ILE A CG2 1 
ATOM   2631 C CD1 . ILE B 1 122 ? 16.86139 10.66948  -5.66170  1.000 32.25747  ? 122 ILE A CD1 1 
ATOM   2632 N N   . LEU B 1 123 ? 12.72722 10.34486  -1.96616  1.000 36.98768  ? 123 LEU A N   1 
ATOM   2633 C CA  . LEU B 1 123 ? 11.33974 10.17402  -1.55680  1.000 35.76420  ? 123 LEU A CA  1 
ATOM   2634 C C   . LEU B 1 123 ? 10.98803 11.10462  -0.41836  1.000 36.31070  ? 123 LEU A C   1 
ATOM   2635 O O   . LEU B 1 123 ? 9.99498  11.84338  -0.48405  1.000 36.85960  ? 123 LEU A O   1 
ATOM   2636 C CB  . LEU B 1 123 ? 11.07641 8.72449   -1.14163  1.000 31.81904  ? 123 LEU A CB  1 
ATOM   2637 C CG  . LEU B 1 123 ? 9.58198  8.50715   -0.87957  1.000 32.78143  ? 123 LEU A CG  1 
ATOM   2638 C CD1 . LEU B 1 123 ? 8.82991  8.56392   -2.17862  1.000 32.87253  ? 123 LEU A CD1 1 
ATOM   2639 C CD2 . LEU B 1 123 ? 9.35790  7.14941   -0.22905  1.000 34.32705  ? 123 LEU A CD2 1 
ATOM   2640 N N   . VAL B 1 124 ? 11.80695 11.08843  0.63505   1.000 36.60764  ? 124 VAL A N   1 
ATOM   2641 C CA  . VAL B 1 124 ? 11.52844 11.93233  1.78518   1.000 36.07247  ? 124 VAL A CA  1 
ATOM   2642 C C   . VAL B 1 124 ? 11.64651 13.39940  1.40630   1.000 39.91183  ? 124 VAL A C   1 
ATOM   2643 O O   . VAL B 1 124 ? 10.87100 14.23346  1.89319   1.000 42.03269  ? 124 VAL A O   1 
ATOM   2644 C CB  . VAL B 1 124 ? 12.43993 11.57048  2.96968   1.000 36.80587  ? 124 VAL A CB  1 
ATOM   2645 C CG1 . VAL B 1 124 ? 12.27965 12.58981  4.10731   1.000 36.64114  ? 124 VAL A CG1 1 
ATOM   2646 C CG2 . VAL B 1 124 ? 12.11763 10.16262  3.45081   1.000 35.22977  ? 124 VAL A CG2 1 
ATOM   2647 N N   . ASP B 1 125 ? 12.57648 13.75803  0.52017   1.000 35.12213  ? 125 ASP A N   1 
ATOM   2648 C CA  . ASP B 1 125 ? 12.62099 15.17013  0.16567   1.000 36.46494  ? 125 ASP A CA  1 
ATOM   2649 C C   . ASP B 1 125 ? 11.34046 15.59306  -0.54148  1.000 37.34566  ? 125 ASP A C   1 
ATOM   2650 O O   . ASP B 1 125 ? 10.86349 16.72225  -0.36642  1.000 36.95455  ? 125 ASP A O   1 
ATOM   2651 C CB  . ASP B 1 125 ? 13.81849 15.50048  -0.70374  1.000 29.68133  ? 125 ASP A CB  1 
ATOM   2652 C CG  . ASP B 1 125 ? 13.89839 16.96179  -0.96892  1.000 33.17765  ? 125 ASP A CG  1 
ATOM   2653 O OD1 . ASP B 1 125 ? 14.00380 17.71869  0.03052   1.000 31.97621  ? 125 ASP A OD1 1 
ATOM   2654 O OD2 . ASP B 1 125 ? 13.83404 17.35648  -2.15364  1.000 33.16547  ? 125 ASP A OD2 1 
ATOM   2655 N N   . LEU B 1 126 ? 10.77665 14.69700  -1.34360  1.000 33.62510  ? 126 LEU A N   1 
ATOM   2656 C CA  . LEU B 1 126 ? 9.53268  15.01205  -2.02244  1.000 40.00567  ? 126 LEU A CA  1 
ATOM   2657 C C   . LEU B 1 126 ? 8.37740  15.09351  -1.03412  1.000 42.17135  ? 126 LEU A C   1 
ATOM   2658 O O   . LEU B 1 126 ? 7.48712  15.93369  -1.18553  1.000 40.50148  ? 126 LEU A O   1 
ATOM   2659 C CB  . LEU B 1 126 ? 9.26760  13.97878  -3.11146  1.000 34.91959  ? 126 LEU A CB  1 
ATOM   2660 C CG  . LEU B 1 126 ? 10.28311 14.01531  -4.25642  1.000 36.06627  ? 126 LEU A CG  1 
ATOM   2661 C CD1 . LEU B 1 126 ? 10.01554 12.84100  -5.18577  1.000 38.25086  ? 126 LEU A CD1 1 
ATOM   2662 C CD2 . LEU B 1 126 ? 10.25411 15.36706  -5.01387  1.000 32.73143  ? 126 LEU A CD2 1 
ATOM   2663 N N   . ILE B 1 127 ? 8.38277  14.24329  -0.00275  1.000 39.10332  ? 127 ILE A N   1 
ATOM   2664 C CA  . ILE B 1 127 ? 7.30040  14.30598  0.97425   1.000 42.39143  ? 127 ILE A CA  1 
ATOM   2665 C C   . ILE B 1 127 ? 7.40584  15.60303  1.77565   1.000 41.51069  ? 127 ILE A C   1 
ATOM   2666 O O   . ILE B 1 127 ? 6.38895  16.20757  2.14627   1.000 45.20145  ? 127 ILE A O   1 
ATOM   2667 C CB  . ILE B 1 127 ? 7.31810  13.03863  1.86406   1.000 41.69904  ? 127 ILE A CB  1 
ATOM   2668 C CG1 . ILE B 1 127 ? 6.86056  11.80412  1.05867   1.000 35.36331  ? 127 ILE A CG1 1 
ATOM   2669 C CG2 . ILE B 1 127 ? 6.47850  13.21539  3.10777   1.000 35.00287  ? 127 ILE A CG2 1 
ATOM   2670 C CD1 . ILE B 1 127 ? 7.00383  10.52677  1.79821   1.000 31.03054  ? 127 ILE A CD1 1 
ATOM   2671 N N   . ARG B 1 128 ? 8.62739  16.06907  2.01066   1.000 38.67952  ? 128 ARG A N   1 
ATOM   2672 C CA  . ARG B 1 128 ? 8.85120  17.34225  2.68741   1.000 42.62689  ? 128 ARG A CA  1 
ATOM   2673 C C   . ARG B 1 128 ? 8.30731  18.52886  1.88779   1.000 43.08968  ? 128 ARG A C   1 
ATOM   2674 O O   . ARG B 1 128 ? 7.88413  19.53609  2.47524   1.000 39.91306  ? 128 ARG A O   1 
ATOM   2675 C CB  . ARG B 1 128 ? 10.34947 17.50342  2.94539   1.000 35.71517  ? 128 ARG A CB  1 
ATOM   2676 C CG  . ARG B 1 128 ? 10.85895 16.65493  4.10155   1.000 42.20507  ? 128 ARG A CG  1 
ATOM   2677 C CD  . ARG B 1 128 ? 12.34921 16.48806  4.02408   1.000 45.23817  ? 128 ARG A CD  1 
ATOM   2678 N NE  . ARG B 1 128 ? 13.08253 17.02599  5.15783   1.000 46.80425  ? 128 ARG A NE  1 
ATOM   2679 C CZ  . ARG B 1 128 ? 14.13653 16.42347  5.69846   1.000 61.03071  ? 128 ARG A CZ  1 
ATOM   2680 N NH1 . ARG B 1 128 ? 14.52274 15.21381  5.29415   1.000 46.56424  ? 128 ARG A NH1 1 
ATOM   2681 N NH2 . ARG B 1 128 ? 14.82631 17.05085  6.65995   1.000 57.64888  ? 128 ARG A NH2 1 
ATOM   2682 N N   . ASP B 1 129 ? 8.34841  18.44808  0.55449   1.000 39.44172  ? 129 ASP A N   1 
ATOM   2683 C CA  . ASP B 1 129 ? 7.65762  19.44104  -0.25552  1.000 40.55781  ? 129 ASP A CA  1 
ATOM   2684 C C   . ASP B 1 129 ? 6.19684  19.57380  0.15695   1.000 38.82064  ? 129 ASP A C   1 
ATOM   2685 O O   . ASP B 1 129 ? 5.64720  20.67824  0.10975   1.000 37.12879  ? 129 ASP A O   1 
ATOM   2686 C CB  . ASP B 1 129 ? 7.73457  19.08274  -1.73779  1.000 42.00675  ? 129 ASP A CB  1 
ATOM   2687 C CG  . ASP B 1 129 ? 9.06403  19.43388  -2.36279  1.000 38.76307  ? 129 ASP A CG  1 
ATOM   2688 O OD1 . ASP B 1 129 ? 9.75539  20.33151  -1.85548  1.000 41.88952  ? 129 ASP A OD1 1 
ATOM   2689 O OD2 . ASP B 1 129 ? 9.40462  18.83106  -3.39346  1.000 39.38403  ? 129 ASP A OD2 1 
ATOM   2690 N N   . ILE B 1 130 ? 5.56495  18.47245  0.58680   1.000 39.50715  ? 130 ILE A N   1 
ATOM   2691 C CA  . ILE B 1 130 ? 4.17384  18.54677  1.03307   1.000 42.82035  ? 130 ILE A CA  1 
ATOM   2692 C C   . ILE B 1 130 ? 4.06160  19.50542  2.20237   1.000 45.61070  ? 130 ILE A C   1 
ATOM   2693 O O   . ILE B 1 130 ? 3.15709  20.33972  2.25282   1.000 42.19783  ? 130 ILE A O   1 
ATOM   2694 C CB  . ILE B 1 130 ? 3.62371  17.15402  1.39913   1.000 43.59323  ? 130 ILE A CB  1 
ATOM   2695 C CG1 . ILE B 1 130 ? 3.51257  16.24997  0.16564   1.000 41.53495  ? 130 ILE A CG1 1 
ATOM   2696 C CG2 . ILE B 1 130 ? 2.31215  17.27886  2.15619   1.000 44.52350  ? 130 ILE A CG2 1 
ATOM   2697 C CD1 . ILE B 1 130 ? 3.21302  14.78633  0.49170   1.000 35.93732  ? 130 ILE A CD1 1 
ATOM   2698 N N   . GLN B 1 131 ? 5.01097  19.44171  3.13533   1.000 48.04242  ? 131 GLN A N   1 
ATOM   2699 C CA  . GLN B 1 131 ? 4.99557  20.40253  4.23148   1.000 42.96580  ? 131 GLN A CA  1 
ATOM   2700 C C   . GLN B 1 131 ? 5.51225  21.77708  3.81417   1.000 39.59538  ? 131 GLN A C   1 
ATOM   2701 O O   . GLN B 1 131 ? 5.05346  22.78784  4.35492   1.000 40.73319  ? 131 GLN A O   1 
ATOM   2702 C CB  . GLN B 1 131 ? 5.79835  19.85817  5.41273   1.000 40.98487  ? 131 GLN A CB  1 
ATOM   2703 C CG  . GLN B 1 131 ? 5.41178  18.44835  5.82405   1.000 41.51014  ? 131 GLN A CG  1 
ATOM   2704 C CD  . GLN B 1 131 ? 5.57908  18.19485  7.32456   1.000 48.32930  ? 131 GLN A CD  1 
ATOM   2705 O OE1 . GLN B 1 131 ? 6.31672  18.90003  8.00189   1.000 56.32252  ? 131 GLN A OE1 1 
ATOM   2706 N NE2 . GLN B 1 131 ? 4.90929  17.16867  7.83868   1.000 46.78852  ? 131 GLN A NE2 1 
ATOM   2707 N N   . ARG B 1 132 ? 6.46404  21.85044  2.87779   1.000 40.47225  ? 132 ARG A N   1 
ATOM   2708 C CA  . ARG B 1 132 ? 6.94421  23.15956  2.43108   1.000 41.23834  ? 132 ARG A CA  1 
ATOM   2709 C C   . ARG B 1 132 ? 5.82282  23.92809  1.75225   1.000 39.70718  ? 132 ARG A C   1 
ATOM   2710 O O   . ARG B 1 132 ? 5.66768  25.14041  1.95373   1.000 38.20104  ? 132 ARG A O   1 
ATOM   2711 C CB  . ARG B 1 132 ? 8.13168  23.02067  1.46612   1.000 39.48376  ? 132 ARG A CB  1 
ATOM   2712 C CG  . ARG B 1 132 ? 9.42337  22.47940  2.06729   1.000 39.67103  ? 132 ARG A CG  1 
ATOM   2713 C CD  . ARG B 1 132 ? 10.54617 22.34881  0.99326   1.000 40.45493  ? 132 ARG A CD  1 
ATOM   2714 N NE  . ARG B 1 132 ? 11.73708 21.71943  1.55621   1.000 39.92442  ? 132 ARG A NE  1 
ATOM   2715 C CZ  . ARG B 1 132 ? 12.16871 20.49573  1.26206   1.000 38.49166  ? 132 ARG A CZ  1 
ATOM   2716 N NH1 . ARG B 1 132 ? 11.58866 19.75719  0.32256   1.000 35.63435  ? 132 ARG A NH1 1 
ATOM   2717 N NH2 . ARG B 1 132 ? 13.18523 19.98482  1.95374   1.000 35.06058  ? 132 ARG A NH2 1 
ATOM   2718 N N   . LEU B 1 133 ? 5.01571  23.22995  0.95284   1.000 42.29714  ? 133 LEU A N   1 
ATOM   2719 C CA  . LEU B 1 133 ? 3.84463  23.86586  0.34663   1.000 40.41893  ? 133 LEU A CA  1 
ATOM   2720 C C   . LEU B 1 133 ? 2.93130  24.47139  1.40510   1.000 38.61869  ? 133 LEU A C   1 
ATOM   2721 O O   . LEU B 1 133 ? 2.37747  25.55593  1.20383   1.000 42.64557  ? 133 LEU A O   1 
ATOM   2722 C CB  . LEU B 1 133 ? 3.09217  22.85510  -0.50423  1.000 36.95176  ? 133 LEU A CB  1 
ATOM   2723 C CG  . LEU B 1 133 ? 2.01013  23.44512  -1.39220  1.000 41.66810  ? 133 LEU A CG  1 
ATOM   2724 C CD1 . LEU B 1 133 ? 2.67097  24.23670  -2.50051  1.000 36.82514  ? 133 LEU A CD1 1 
ATOM   2725 C CD2 . LEU B 1 133 ? 1.07689  22.32799  -1.94190  1.000 34.56593  ? 133 LEU A CD2 1 
ATOM   2726 N N   . ASN B 1 134 ? 2.81054  23.81897  2.56136   1.000 36.95909  ? 134 ASN A N   1 
ATOM   2727 C CA  . ASN B 1 134 ? 1.99556  24.32979  3.64852   1.000 39.85156  ? 134 ASN A CA  1 
ATOM   2728 C C   . ASN B 1 134 ? 2.75232  25.31795  4.52452   1.000 39.51286  ? 134 ASN A C   1 
ATOM   2729 O O   . ASN B 1 134 ? 2.39768  25.49973  5.69446   1.000 35.41024  ? 134 ASN A O   1 
ATOM   2730 C CB  . ASN B 1 134 ? 1.42989  23.17526  4.48756   1.000 40.23357  ? 134 ASN A CB  1 
ATOM   2731 C CG  . ASN B 1 134 ? 0.09744  23.53999  5.16593   1.000 50.56569  ? 134 ASN A CG  1 
ATOM   2732 O OD1 . ASN B 1 134 ? -0.78818 22.70345  5.28960   1.000 56.98674  ? 134 ASN A OD1 1 
ATOM   2733 N ND2 . ASN B 1 134 ? -0.04600 24.79407  5.58988   1.000 54.66470  ? 134 ASN A ND2 1 
ATOM   2734 N N   . GLY B 1 135 ? 3.78676  25.96085  3.98572   1.000 40.55005  ? 135 GLY A N   1 
ATOM   2735 C CA  . GLY B 1 135 ? 4.46377  27.03060  4.68807   1.000 36.37181  ? 135 GLY A CA  1 
ATOM   2736 C C   . GLY B 1 135 ? 5.36503  26.62683  5.83853   1.000 39.87704  ? 135 GLY A C   1 
ATOM   2737 O O   . GLY B 1 135 ? 5.77654  27.50329  6.61024   1.000 44.74495  ? 135 GLY A O   1 
ATOM   2738 N N   . VAL B 1 136 ? 5.70051  25.34479  5.98075   1.000 36.89846  ? 136 VAL A N   1 
ATOM   2739 C CA  . VAL B 1 136 ? 6.59902  24.92203  7.04976   1.000 43.59578  ? 136 VAL A CA  1 
ATOM   2740 C C   . VAL B 1 136 ? 8.03683  25.31729  6.71128   1.000 44.23294  ? 136 VAL A C   1 
ATOM   2741 O O   . VAL B 1 136 ? 8.51883  25.08805  5.59163   1.000 45.94012  ? 136 VAL A O   1 
ATOM   2742 C CB  . VAL B 1 136 ? 6.46911  23.40956  7.28559   1.000 42.67921  ? 136 VAL A CB  1 
ATOM   2743 C CG1 . VAL B 1 136 ? 7.44069  22.94808  8.37513   1.000 43.41918  ? 136 VAL A CG1 1 
ATOM   2744 C CG2 . VAL B 1 136 ? 5.05985  23.07829  7.67681   1.000 37.20081  ? 136 VAL A CG2 1 
ATOM   2745 N N   . SER B 1 137 ? 8.72431  25.92911  7.67496   1.000 43.54861  ? 137 SER A N   1 
ATOM   2746 C CA  . SER B 1 137 ? 10.14963 26.21816  7.52942   1.000 47.83997  ? 137 SER A CA  1 
ATOM   2747 C C   . SER B 1 137 ? 10.98169 24.93858  7.50511   1.000 40.82498  ? 137 SER A C   1 
ATOM   2748 O O   . SER B 1 137 ? 10.68834 23.96002  8.19522   1.000 42.14578  ? 137 SER A O   1 
ATOM   2749 C CB  . SER B 1 137 ? 10.65276 27.09303  8.68003   1.000 46.62755  ? 137 SER A CB  1 
ATOM   2750 O OG  . SER B 1 137 ? 10.23175 28.42250  8.50522   1.000 54.45952  ? 137 SER A OG  1 
ATOM   2751 N N   . GLU B 1 138 ? 12.06006 24.98624  6.72456   1.000 45.48681  ? 138 GLU A N   1 
ATOM   2752 C CA  . GLU B 1 138 ? 12.96600 23.84935  6.57561   1.000 45.56457  ? 138 GLU A CA  1 
ATOM   2753 C C   . GLU B 1 138 ? 13.40276 23.26241  7.91428   1.000 40.54300  ? 138 GLU A C   1 
ATOM   2754 O O   . GLU B 1 138 ? 13.46312 22.04151  8.07072   1.000 39.55950  ? 138 GLU A O   1 
ATOM   2755 C CB  . GLU B 1 138 ? 14.19278 24.27487  5.76009   1.000 41.15664  ? 138 GLU A CB  1 
ATOM   2756 C CG  . GLU B 1 138 ? 14.90501 23.09184  5.15768   1.000 40.52967  ? 138 GLU A CG  1 
ATOM   2757 C CD  . GLU B 1 138 ? 14.20519 22.57332  3.90934   1.000 45.00897  ? 138 GLU A CD  1 
ATOM   2758 O OE1 . GLU B 1 138 ? 13.12100 23.11189  3.52601   1.000 43.57630  ? 138 GLU A OE1 1 
ATOM   2759 O OE2 . GLU B 1 138 ? 14.72378 21.58362  3.34159   1.000 45.79998  ? 138 GLU A OE2 1 
ATOM   2760 N N   . ASN B 1 139 ? 13.70677 24.10889  8.89080   1.000 42.07766  ? 139 ASN A N   1 
ATOM   2761 C CA  . ASN B 1 139 ? 14.18079 23.61729  10.17655  1.000 43.35781  ? 139 ASN A CA  1 
ATOM   2762 C C   . ASN B 1 139 ? 13.05673 23.16955  11.09283  1.000 45.74623  ? 139 ASN A C   1 
ATOM   2763 O O   . ASN B 1 139 ? 13.34076 22.73491  12.21817  1.000 43.75921  ? 139 ASN A O   1 
ATOM   2764 C CB  . ASN B 1 139 ? 15.00095 24.68836  10.87908  1.000 49.97933  ? 139 ASN A CB  1 
ATOM   2765 C CG  . ASN B 1 139 ? 14.21964 25.96135  11.08058  1.000 52.17275  ? 139 ASN A CG  1 
ATOM   2766 O OD1 . ASN B 1 139 ? 13.90972 26.67022  10.11967  1.000 56.08607  ? 139 ASN A OD1 1 
ATOM   2767 N ND2 . ASN B 1 139 ? 13.88094 26.25442  12.32757  1.000 48.02063  ? 139 ASN A ND2 1 
ATOM   2768 N N   . GLU B 1 140 ? 11.80113 23.27640  10.64247  1.000 46.52679  ? 140 GLU A N   1 
ATOM   2769 C CA  . GLU B 1 140 ? 10.64444 22.75499  11.35730  1.000 46.59639  ? 140 GLU A CA  1 
ATOM   2770 C C   . GLU B 1 140 ? 9.96562  21.61491  10.62062  1.000 47.43318  ? 140 GLU A C   1 
ATOM   2771 O O   . GLU B 1 140 ? 8.93044  21.11087  11.08863  1.000 49.03517  ? 140 GLU A O   1 
ATOM   2772 C CB  . GLU B 1 140 ? 9.62768  23.86470  11.61675  1.000 44.74811  ? 140 GLU A CB  1 
ATOM   2773 C CG  . GLU B 1 140 ? 9.62175  24.31589  13.05229  1.000 56.61960  ? 140 GLU A CG  1 
ATOM   2774 C CD  . GLU B 1 140 ? 8.86683  25.62005  13.26465  1.000 62.51078  ? 140 GLU A CD  1 
ATOM   2775 O OE1 . GLU B 1 140 ? 8.25619  26.13343  12.29425  1.000 58.28930  ? 140 GLU A OE1 1 
ATOM   2776 O OE2 . GLU B 1 140 ? 8.88870  26.12455  14.41051  1.000 63.48559  ? 140 GLU A OE2 1 
ATOM   2777 N N   . LEU B 1 141 ? 10.50619 21.20419  9.47874   1.000 46.85955  ? 141 LEU A N   1 
ATOM   2778 C CA  . LEU B 1 141 ? 9.99223  20.03155  8.78911   1.000 48.76782  ? 141 LEU A CA  1 
ATOM   2779 C C   . LEU B 1 141 ? 9.94093  18.84419  9.74085   1.000 46.19356  ? 141 LEU A C   1 
ATOM   2780 O O   . LEU B 1 141 ? 10.84664 18.64555  10.55103  1.000 48.13108  ? 141 LEU A O   1 
ATOM   2781 C CB  . LEU B 1 141 ? 10.88712 19.72681  7.59896   1.000 46.62776  ? 141 LEU A CB  1 
ATOM   2782 C CG  . LEU B 1 141 ? 10.76203 20.77647  6.50145   1.000 46.09852  ? 141 LEU A CG  1 
ATOM   2783 C CD1 . LEU B 1 141 ? 11.81111 20.51908  5.43323   1.000 41.39284  ? 141 LEU A CD1 1 
ATOM   2784 C CD2 . LEU B 1 141 ? 9.32858  20.74266  5.91181   1.000 43.19112  ? 141 LEU A CD2 1 
ATOM   2785 N N   . ASP B 1 142 ? 8.84407  18.08642  9.68071   1.000 52.87130  ? 142 ASP A N   1 
ATOM   2786 C CA  . ASP B 1 142 ? 8.70570  16.84908  10.45936  1.000 51.71064  ? 142 ASP A CA  1 
ATOM   2787 C C   . ASP B 1 142 ? 7.69437  15.95951  9.74698   1.000 47.93663  ? 142 ASP A C   1 
ATOM   2788 O O   . ASP B 1 142 ? 6.49224  16.08585  9.99004   1.000 56.73699  ? 142 ASP A O   1 
ATOM   2789 C CB  . ASP B 1 142 ? 8.27166  17.10849  11.89471  1.000 55.84516  ? 142 ASP A CB  1 
ATOM   2790 C CG  . ASP B 1 142 ? 8.01068  15.81464  12.66755  1.000 58.75185  ? 142 ASP A CG  1 
ATOM   2791 O OD1 . ASP B 1 142 ? 8.59734  14.76955  12.31119  1.000 59.04929  ? 142 ASP A OD1 1 
ATOM   2792 O OD2 . ASP B 1 142 ? 7.21506  15.83758  13.63333  1.000 63.23830  ? 142 ASP A OD2 1 
ATOM   2793 N N   . THR B 1 143 ? 8.19862  15.03449  8.92640   1.000 39.82376  ? 143 THR A N   1 
ATOM   2794 C CA  . THR B 1 143 ? 7.41416  14.16522  8.06435   1.000 41.37085  ? 143 THR A CA  1 
ATOM   2795 C C   . THR B 1 143 ? 7.21704  12.76357  8.64542   1.000 41.26606  ? 143 THR A C   1 
ATOM   2796 O O   . THR B 1 143 ? 6.91579  11.82019  7.89871   1.000 42.35426  ? 143 THR A O   1 
ATOM   2797 C CB  . THR B 1 143 ? 8.07699  14.07419  6.68795   1.000 40.90697  ? 143 THR A CB  1 
ATOM   2798 O OG1 . THR B 1 143 ? 9.36682  13.45984  6.82454   1.000 43.34836  ? 143 THR A OG1 1 
ATOM   2799 C CG2 . THR B 1 143 ? 8.21489  15.45726  6.03991   1.000 36.72038  ? 143 THR A CG2 1 
ATOM   2800 N N   . PHE B 1 144 ? 7.37462  12.60865  9.95814   1.000 39.87703  ? 144 PHE A N   1 
ATOM   2801 C CA  . PHE B 1 144 ? 7.26146  11.28904  10.57477  1.000 42.94106  ? 144 PHE A CA  1 
ATOM   2802 C C   . PHE B 1 144 ? 5.91210  10.63098  10.25880  1.000 49.86947  ? 144 PHE A C   1 
ATOM   2803 O O   . PHE B 1 144 ? 5.84933  9.42261   9.99388   1.000 50.36455  ? 144 PHE A O   1 
ATOM   2804 C CB  . PHE B 1 144 ? 7.47304  11.42669  12.08389  1.000 45.23394  ? 144 PHE A CB  1 
ATOM   2805 C CG  . PHE B 1 144 ? 7.39237  10.12429  12.84475  1.000 52.97563  ? 144 PHE A CG  1 
ATOM   2806 C CD1 . PHE B 1 144 ? 8.53632  9.35792   13.06620  1.000 45.45953  ? 144 PHE A CD1 1 
ATOM   2807 C CD2 . PHE B 1 144 ? 6.17043  9.66945   13.35837  1.000 45.48155  ? 144 PHE A CD2 1 
ATOM   2808 C CE1 . PHE B 1 144 ? 8.46508  8.16064   13.77960  1.000 47.21356  ? 144 PHE A CE1 1 
ATOM   2809 C CE2 . PHE B 1 144 ? 6.09423  8.47761   14.07045  1.000 46.66039  ? 144 PHE A CE2 1 
ATOM   2810 C CZ  . PHE B 1 144 ? 7.23837  7.71674   14.28334  1.000 44.64683  ? 144 PHE A CZ  1 
ATOM   2811 N N   . LYS B 1 145 ? 4.82423  11.41586  10.25357  1.000 46.05577  ? 145 LYS A N   1 
ATOM   2812 C CA  . LYS B 1 145 ? 3.50053  10.86676  9.98296   1.000 48.98308  ? 145 LYS A CA  1 
ATOM   2813 C C   . LYS B 1 145 ? 3.21465  10.70609  8.49427   1.000 48.80900  ? 145 LYS A C   1 
ATOM   2814 O O   . LYS B 1 145 ? 2.39634  9.85904   8.12179   1.000 51.36664  ? 145 LYS A O   1 
ATOM   2815 C CB  . LYS B 1 145 ? 2.42207  11.75096  10.60487  1.000 50.07789  ? 145 LYS A CB  1 
ATOM   2816 C CG  . LYS B 1 145 ? 2.54734  11.94048  12.10868  1.000 55.40498  ? 145 LYS A CG  1 
ATOM   2817 C CD  . LYS B 1 145 ? 1.67091  13.09798  12.57970  1.000 55.36521  ? 145 LYS A CD  1 
ATOM   2818 C CE  . LYS B 1 145 ? 0.61937  12.63676  13.55608  1.000 67.15599  ? 145 LYS A CE  1 
ATOM   2819 N NZ  . LYS B 1 145 ? 0.58932  13.53277  14.75674  1.000 73.60324  ? 145 LYS A NZ  1 
ATOM   2820 N N   . LEU B 1 146 ? 3.84930  11.50442  7.63227   1.000 46.90775  ? 146 LEU A N   1 
ATOM   2821 C CA  . LEU B 1 146 ? 3.53336  11.46992  6.20799   1.000 41.74148  ? 146 LEU A CA  1 
ATOM   2822 C C   . LEU B 1 146 ? 4.24870  10.36208  5.45264   1.000 44.09029  ? 146 LEU A C   1 
ATOM   2823 O O   . LEU B 1 146 ? 3.88960  10.10088  4.29473   1.000 40.07639  ? 146 LEU A O   1 
ATOM   2824 C CB  . LEU B 1 146 ? 3.87913  12.79812  5.54242   1.000 40.27073  ? 146 LEU A CB  1 
ATOM   2825 C CG  . LEU B 1 146 ? 3.02745  14.00938  5.88916   1.000 42.80630  ? 146 LEU A CG  1 
ATOM   2826 C CD1 . LEU B 1 146 ? 3.74989  15.25537  5.39129   1.000 43.23721  ? 146 LEU A CD1 1 
ATOM   2827 C CD2 . LEU B 1 146 ? 1.60537  13.89706  5.32011   1.000 44.19718  ? 146 LEU A CD2 1 
ATOM   2828 N N   . GLU B 1 147 ? 5.25206  9.72306   6.06774   1.000 43.34998  ? 147 GLU A N   1 
ATOM   2829 C CA  . GLU B 1 147 ? 6.14788  8.82501   5.36178   1.000 42.25665  ? 147 GLU A CA  1 
ATOM   2830 C C   . GLU B 1 147 ? 5.50204  7.44898   5.24780   1.000 39.56619  ? 147 GLU A C   1 
ATOM   2831 O O   . GLU B 1 147 ? 4.76328  7.03421   6.14118   1.000 42.57953  ? 147 GLU A O   1 
ATOM   2832 C CB  . GLU B 1 147 ? 7.49419  8.72489   6.09716   1.000 41.25209  ? 147 GLU A CB  1 
ATOM   2833 C CG  . GLU B 1 147 ? 8.52339  9.83731   5.70446   1.000 43.35708  ? 147 GLU A CG  1 
ATOM   2834 C CD  . GLU B 1 147 ? 9.58208  10.08575  6.78271   1.000 39.62753  ? 147 GLU A CD  1 
ATOM   2835 O OE1 . GLU B 1 147 ? 10.18723 9.10781   7.27095   1.000 38.30017  ? 147 GLU A OE1 1 
ATOM   2836 O OE2 . GLU B 1 147 ? 9.80179  11.25848  7.15245   1.000 34.70933  ? 147 GLU A OE2 1 
ATOM   2837 N N   . PRO B 1 148 ? 5.77679  6.71117   4.16827   1.000 41.37290  ? 148 PRO A N   1 
ATOM   2838 C CA  . PRO B 1 148 ? 5.06701  5.43283   3.95839   1.000 40.95319  ? 148 PRO A CA  1 
ATOM   2839 C C   . PRO B 1 148 ? 5.49094  4.32917   4.90388   1.000 42.55056  ? 148 PRO A C   1 
ATOM   2840 O O   . PRO B 1 148 ? 4.73623  3.36929   5.05703   1.000 43.28511  ? 148 PRO A O   1 
ATOM   2841 C CB  . PRO B 1 148 ? 5.42604  5.06300   2.51346   1.000 42.20134  ? 148 PRO A CB  1 
ATOM   2842 C CG  . PRO B 1 148 ? 6.82908  5.66111   2.34716   1.000 37.16808  ? 148 PRO A CG  1 
ATOM   2843 C CD  . PRO B 1 148 ? 6.77299  6.97082   3.11315   1.000 31.57793  ? 148 PRO A CD  1 
ATOM   2844 N N   . CYS B 1 149 ? 6.70654  4.36682   5.45620   1.000 42.64877  ? 149 CYS A N   1 
ATOM   2845 C CA  . CYS B 1 149 ? 7.10213  3.41482   6.48585   1.000 41.59996  ? 149 CYS A CA  1 
ATOM   2846 C C   . CYS B 1 149 ? 7.88266  4.18104   7.52964   1.000 41.34033  ? 149 CYS A C   1 
ATOM   2847 O O   . CYS B 1 149 ? 8.29344  5.31834   7.30269   1.000 41.76698  ? 149 CYS A O   1 
ATOM   2848 C CB  . CYS B 1 149 ? 7.93843  2.23382   5.95803   1.000 37.81046  ? 149 CYS A CB  1 
ATOM   2849 S SG  . CYS B 1 149 ? 9.54904  2.63026   5.16836   1.000 44.86412  ? 149 CYS A SG  1 
ATOM   2850 N N   . LYS B 1 150 ? 8.03494  3.57227   8.69797   1.000 41.44072  ? 150 LYS A N   1 
ATOM   2851 C CA  . LYS B 1 150 ? 8.87852  4.17576   9.71118   1.000 46.13430  ? 150 LYS A CA  1 
ATOM   2852 C C   . LYS B 1 150 ? 10.31510 4.10527   9.22094   1.000 45.71032  ? 150 LYS A C   1 
ATOM   2853 O O   . LYS B 1 150 ? 10.69327 3.16013   8.51856   1.000 43.06729  ? 150 LYS A O   1 
ATOM   2854 C CB  . LYS B 1 150 ? 8.71144  3.45522   11.04951  1.000 48.38990  ? 150 LYS A CB  1 
ATOM   2855 C CG  . LYS B 1 150 ? 7.37396  3.73136   11.73713  1.000 45.91098  ? 150 LYS A CG  1 
ATOM   2856 C CD  . LYS B 1 150 ? 6.74675  5.01870   11.25309  1.000 51.97863  ? 150 LYS A CD  1 
ATOM   2857 C CE  . LYS B 1 150 ? 5.66080  5.51277   12.21145  1.000 53.10208  ? 150 LYS A CE  1 
ATOM   2858 N NZ  . LYS B 1 150 ? 4.62810  6.30405   11.47241  1.000 56.35927  ? 150 LYS A NZ  1 
ATOM   2859 N N   . PHE B 1 151 ? 11.10684 5.13807   9.54293   1.000 40.63916  ? 151 PHE A N   1 
ATOM   2860 C CA  . PHE B 1 151 ? 12.44537 5.19345   8.95817   1.000 45.81912  ? 151 PHE A CA  1 
ATOM   2861 C C   . PHE B 1 151 ? 13.24931 3.95388   9.32836   1.000 43.22489  ? 151 PHE A C   1 
ATOM   2862 O O   . PHE B 1 151 ? 13.92625 3.37636   8.47060   1.000 43.83280  ? 151 PHE A O   1 
ATOM   2863 C CB  . PHE B 1 151 ? 13.18505 6.49634   9.31969   1.000 38.17727  ? 151 PHE A CB  1 
ATOM   2864 C CG  . PHE B 1 151 ? 13.53734 6.66112   10.77817  1.000 41.62398  ? 151 PHE A CG  1 
ATOM   2865 C CD1 . PHE B 1 151 ? 14.73382 6.13896   11.28882  1.000 42.90445  ? 151 PHE A CD1 1 
ATOM   2866 C CD2 . PHE B 1 151 ? 12.74213 7.43168   11.61008  1.000 37.14114  ? 151 PHE A CD2 1 
ATOM   2867 C CE1 . PHE B 1 151 ? 15.09409 6.31594   12.63657  1.000 37.20937  ? 151 PHE A CE1 1 
ATOM   2868 C CE2 . PHE B 1 151 ? 13.08972 7.63220   12.95053  1.000 41.88033  ? 151 PHE A CE2 1 
ATOM   2869 C CZ  . PHE B 1 151 ? 14.26662 7.07541   13.46800  1.000 45.56503  ? 151 PHE A CZ  1 
ATOM   2870 N N   . TRP B 1 152 ? 13.09919 3.46158   10.55950  1.000 40.64566  ? 152 TRP A N   1 
ATOM   2871 C CA  . TRP B 1 152 ? 13.83240 2.26042   10.95179  1.000 42.06140  ? 152 TRP A CA  1 
ATOM   2872 C C   . TRP B 1 152 ? 13.34628 1.01410   10.24020  1.000 41.15989  ? 152 TRP A C   1 
ATOM   2873 O O   . TRP B 1 152 ? 13.91922 -0.06336  10.45567  1.000 44.68933  ? 152 TRP A O   1 
ATOM   2874 C CB  . TRP B 1 152 ? 13.76838 2.04648   12.46804  1.000 39.65596  ? 152 TRP A CB  1 
ATOM   2875 C CG  . TRP B 1 152 ? 12.38063 1.96515   13.03554  1.000 45.08760  ? 152 TRP A CG  1 
ATOM   2876 C CD1 . TRP B 1 152 ? 11.59830 0.85260   13.14937  1.000 45.23772  ? 152 TRP A CD1 1 
ATOM   2877 C CD2 . TRP B 1 152 ? 11.60053 3.06027   13.55468  1.000 45.59123  ? 152 TRP A CD2 1 
ATOM   2878 N NE1 . TRP B 1 152 ? 10.37881 1.18788   13.71741  1.000 49.03816  ? 152 TRP A NE1 1 
ATOM   2879 C CE2 . TRP B 1 152 ? 10.36734 2.53328   13.98108  1.000 46.40781  ? 152 TRP A CE2 1 
ATOM   2880 C CE3 . TRP B 1 152 ? 11.84083 4.42802   13.71504  1.000 44.63693  ? 152 TRP A CE3 1 
ATOM   2881 C CZ2 . TRP B 1 152 ? 9.38132  3.32346   14.54892  1.000 50.90475  ? 152 TRP A CZ2 1 
ATOM   2882 C CZ3 . TRP B 1 152 ? 10.86134 5.20837   14.27885  1.000 44.79078  ? 152 TRP A CZ3 1 
ATOM   2883 C CH2 . TRP B 1 152 ? 9.64534  4.65596   14.68802  1.000 51.86575  ? 152 TRP A CH2 1 
ATOM   2884 N N   . ASN B 1 153 ? 12.33276 1.13108   9.39221   1.000 43.94986  ? 153 ASN A N   1 
ATOM   2885 C CA  . ASN B 1 153 ? 11.80957 0.01109   8.62219   1.000 45.13650  ? 153 ASN A CA  1 
ATOM   2886 C C   . ASN B 1 153 ? 12.16467 0.08167   7.14235   1.000 46.40138  ? 153 ASN A C   1 
ATOM   2887 O O   . ASN B 1 153 ? 11.77047 -0.81223  6.38228   1.000 47.09536  ? 153 ASN A O   1 
ATOM   2888 C CB  . ASN B 1 153 ? 10.28900 -0.08315  8.78199   1.000 39.76251  ? 153 ASN A CB  1 
ATOM   2889 C CG  . ASN B 1 153 ? 9.88546  -0.80628  10.04956  1.000 49.97907  ? 153 ASN A CG  1 
ATOM   2890 O OD1 . ASN B 1 153 ? 10.45261 -1.85611  10.38604  1.000 49.92111  ? 153 ASN A OD1 1 
ATOM   2891 N ND2 . ASN B 1 153 ? 8.89951  -0.25232  10.76891  1.000 47.65983  ? 153 ASN A ND2 1 
ATOM   2892 N N   . GLN B 1 154 ? 12.88213 1.11232   6.70302   1.000 43.78535  ? 154 GLN A N   1 
ATOM   2893 C CA  . GLN B 1 154 ? 13.44810 1.04758   5.37058   1.000 43.04010  ? 154 GLN A CA  1 
ATOM   2894 C C   . GLN B 1 154 ? 14.44122 -0.10745  5.33382   1.000 43.49392  ? 154 GLN A C   1 
ATOM   2895 O O   . GLN B 1 154 ? 14.99492 -0.49841  6.36193   1.000 39.27233  ? 154 GLN A O   1 
ATOM   2896 C CB  . GLN B 1 154 ? 14.12199 2.36567   4.99886   1.000 39.99853  ? 154 GLN A CB  1 
ATOM   2897 C CG  . GLN B 1 154 ? 13.21295 3.57204   5.03683   1.000 39.26656  ? 154 GLN A CG  1 
ATOM   2898 C CD  . GLN B 1 154 ? 13.99043 4.88835   5.02321   1.000 44.76105  ? 154 GLN A CD  1 
ATOM   2899 O OE1 . GLN B 1 154 ? 15.17712 4.91376   4.71361   1.000 41.08842  ? 154 GLN A OE1 1 
ATOM   2900 N NE2 . GLN B 1 154 ? 13.31962 5.98253   5.36244   1.000 42.13848  ? 154 GLN A NE2 1 
ATOM   2901 N N   . ARG B 1 155 ? 14.62402 -0.68966  4.14704   1.000 37.76776  ? 155 ARG A N   1 
ATOM   2902 C CA  . ARG B 1 155 ? 15.42759 -1.89001  4.00791   1.000 40.86416  ? 155 ARG A CA  1 
ATOM   2903 C C   . ARG B 1 155 ? 16.15702 -1.82287  2.67728   1.000 42.03794  ? 155 ARG A C   1 
ATOM   2904 O O   . ARG B 1 155 ? 15.60720 -1.31265  1.69878   1.000 41.47020  ? 155 ARG A O   1 
ATOM   2905 C CB  . ARG B 1 155 ? 14.55782 -3.14993  4.10602   1.000 44.16491  ? 155 ARG A CB  1 
ATOM   2906 C CG  . ARG B 1 155 ? 13.99234 -3.43357  5.50226   1.000 44.10036  ? 155 ARG A CG  1 
ATOM   2907 C CD  . ARG B 1 155 ? 15.07689 -3.94292  6.44214   1.000 45.37767  ? 155 ARG A CD  1 
ATOM   2908 N NE  . ARG B 1 155 ? 14.56755 -4.31864  7.76228   1.000 49.82571  ? 155 ARG A NE  1 
ATOM   2909 C CZ  . ARG B 1 155 ? 14.25887 -3.46661  8.73619   1.000 49.46089  ? 155 ARG A CZ  1 
ATOM   2910 N NH1 . ARG B 1 155 ? 14.39580 -2.15564  8.58470   1.000 49.84161  ? 155 ARG A NH1 1 
ATOM   2911 N NH2 . ARG B 1 155 ? 13.80568 -3.93969  9.89538   1.000 45.67600  ? 155 ARG A NH2 1 
ATOM   2912 N N   . ASP B 1 156 ? 17.40455 -2.30327  2.65349   1.000 40.28141  ? 156 ASP A N   1 
ATOM   2913 C CA  . ASP B 1 156 ? 18.24090 -2.21745  1.46206   1.000 39.53518  ? 156 ASP A CA  1 
ATOM   2914 C C   . ASP B 1 156 ? 18.26592 -3.54913  0.72665   1.000 44.55854  ? 156 ASP A C   1 
ATOM   2915 O O   . ASP B 1 156 ? 18.54952 -4.59085  1.33021   1.000 44.09614  ? 156 ASP A O   1 
ATOM   2916 C CB  . ASP B 1 156 ? 19.66390 -1.79281  1.80308   1.000 38.34753  ? 156 ASP A CB  1 
ATOM   2917 C CG  . ASP B 1 156 ? 20.52844 -1.70812  0.57996   1.000 42.45303  ? 156 ASP A CG  1 
ATOM   2918 O OD1 . ASP B 1 156 ? 20.19163 -0.91062  -0.32704  1.000 43.22874  ? 156 ASP A OD1 1 
ATOM   2919 O OD2 . ASP B 1 156 ? 21.52960 -2.45296  0.51325   1.000 43.64121  ? 156 ASP A OD2 1 
ATOM   2920 N N   . ILE B 1 157 ? 17.99481 -3.49843  -0.58509  1.000 44.80330  ? 157 ILE A N   1 
ATOM   2921 C CA  . ILE B 1 157 ? 17.84420 -4.71279  -1.39126  1.000 46.35965  ? 157 ILE A CA  1 
ATOM   2922 C C   . ILE B 1 157 ? 19.18253 -5.43151  -1.56790  1.000 47.29121  ? 157 ILE A C   1 
ATOM   2923 O O   . ILE B 1 157 ? 19.25604 -6.66091  -1.45476  1.000 46.83098  ? 157 ILE A O   1 
ATOM   2924 C CB  . ILE B 1 157 ? 17.20242 -4.36958  -2.75002  1.000 45.15004  ? 157 ILE A CB  1 
ATOM   2925 C CG1 . ILE B 1 157 ? 15.72619 -4.02487  -2.57329  1.000 46.30841  ? 157 ILE A CG1 1 
ATOM   2926 C CG2 . ILE B 1 157 ? 17.36487 -5.51835  -3.75168  1.000 47.30307  ? 157 ILE A CG2 1 
ATOM   2927 C CD1 . ILE B 1 157 ? 15.08585 -3.49021  -3.82265  1.000 43.79897  ? 157 ILE A CD1 1 
ATOM   2928 N N   . ARG B 1 158 ? 20.24947 -4.68598  -1.87559  1.000 45.10072  ? 158 ARG A N   1 
ATOM   2929 C CA  . ARG B 1 158 ? 21.56883 -5.29548  -2.03181  1.000 47.62310  ? 158 ARG A CA  1 
ATOM   2930 C C   . ARG B 1 158 ? 21.97873 -6.04363  -0.76758  1.000 47.74920  ? 158 ARG A C   1 
ATOM   2931 O O   . ARG B 1 158 ? 22.48094 -7.17555  -0.82767  1.000 47.63633  ? 158 ARG A O   1 
ATOM   2932 C CB  . ARG B 1 158 ? 22.60845 -4.22363  -2.37436  1.000 44.28372  ? 158 ARG A CB  1 
ATOM   2933 C CG  . ARG B 1 158 ? 22.56572 -3.70947  -3.80762  1.000 42.70686  ? 158 ARG A CG  1 
ATOM   2934 C CD  . ARG B 1 158 ? 23.72422 -2.76309  -4.06343  1.000 44.10710  ? 158 ARG A CD  1 
ATOM   2935 N NE  . ARG B 1 158 ? 23.53394 -1.93675  -5.25064  1.000 46.95081  ? 158 ARG A NE  1 
ATOM   2936 C CZ  . ARG B 1 158 ? 23.31355 -0.62666  -5.22383  1.000 46.20841  ? 158 ARG A CZ  1 
ATOM   2937 N NH1 . ARG B 1 158 ? 23.21705 0.03694   -4.08350  1.000 48.40264  ? 158 ARG A NH1 1 
ATOM   2938 N NH2 . ARG B 1 158 ? 23.18399 0.03308   -6.36842  1.000 40.38773  ? 158 ARG A NH2 1 
ATOM   2939 N N   . THR B 1 159 ? 21.76755 -5.41745  0.39037   1.000 46.98650  ? 159 THR A N   1 
ATOM   2940 C CA  . THR B 1 159 ? 22.16847 -6.01916  1.65724   1.000 47.87561  ? 159 THR A CA  1 
ATOM   2941 C C   . THR B 1 159 ? 21.34943 -7.26486  1.96244   1.000 50.75737  ? 159 THR A C   1 
ATOM   2942 O O   . THR B 1 159 ? 21.89233 -8.27278  2.43622   1.000 49.89383  ? 159 THR A O   1 
ATOM   2943 C CB  . THR B 1 159 ? 22.03446 -4.98750  2.77447   1.000 42.84066  ? 159 THR A CB  1 
ATOM   2944 O OG1 . THR B 1 159 ? 22.76668 -3.80309  2.41505   1.000 43.61977  ? 159 THR A OG1 1 
ATOM   2945 C CG2 . THR B 1 159 ? 22.54196 -5.52638  4.08159   1.000 43.78079  ? 159 THR A CG2 1 
ATOM   2946 N N   . ARG B 1 160 ? 20.04540 -7.21802  1.67843   1.000 48.30036  ? 160 ARG A N   1 
ATOM   2947 C CA  . ARG B 1 160 ? 19.17092 -8.37138  1.89157   1.000 50.81187  ? 160 ARG A CA  1 
ATOM   2948 C C   . ARG B 1 160 ? 19.64755 -9.59423  1.10567   1.000 57.54849  ? 160 ARG A C   1 
ATOM   2949 O O   . ARG B 1 160 ? 19.94451 -10.64674 1.68534   1.000 54.78585  ? 160 ARG A O   1 
ATOM   2950 C CB  . ARG B 1 160 ? 17.74936 -8.00988  1.48936   1.000 46.86896  ? 160 ARG A CB  1 
ATOM   2951 C CG  . ARG B 1 160 ? 16.76056 -9.14009  1.58136   1.000 53.69011  ? 160 ARG A CG  1 
ATOM   2952 C CD  . ARG B 1 160 ? 16.49144 -9.55740  3.02180   1.000 53.78992  ? 160 ARG A CD  1 
ATOM   2953 N NE  . ARG B 1 160 ? 15.27038 -10.35095 3.10140   1.000 55.31730  ? 160 ARG A NE  1 
ATOM   2954 C CZ  . ARG B 1 160 ? 14.71577 -10.78353 4.22585   1.000 55.85074  ? 160 ARG A CZ  1 
ATOM   2955 N NH1 . ARG B 1 160 ? 15.24012 -10.50365 5.40602   1.000 54.67110  ? 160 ARG A NH1 1 
ATOM   2956 N NH2 . ARG B 1 160 ? 13.60562 -11.52062 4.16266   1.000 53.08434  ? 160 ARG A NH2 1 
ATOM   2957 N N   . ILE B 1 161 ? 19.72989 -9.46566  -0.22541  1.000 59.34945  ? 161 ILE A N   1 
ATOM   2958 C CA  . ILE B 1 161 ? 20.04497 -10.60624 -1.08555  1.000 55.72999  ? 161 ILE A CA  1 
ATOM   2959 C C   . ILE B 1 161 ? 21.43903 -11.14215 -0.78436  1.000 57.00949  ? 161 ILE A C   1 
ATOM   2960 O O   . ILE B 1 161 ? 21.63648 -12.35668 -0.66850  1.000 61.02619  ? 161 ILE A O   1 
ATOM   2961 C CB  . ILE B 1 161 ? 19.89363 -10.21550 -2.56746  1.000 52.74963  ? 161 ILE A CB  1 
ATOM   2962 C CG1 . ILE B 1 161 ? 18.44644 -9.83472  -2.87915  1.000 53.65124  ? 161 ILE A CG1 1 
ATOM   2963 C CG2 . ILE B 1 161 ? 20.30472 -11.35894 -3.46662  1.000 56.53204  ? 161 ILE A CG2 1 
ATOM   2964 C CD1 . ILE B 1 161 ? 18.24520 -9.37939  -4.30458  1.000 55.82267  ? 161 ILE A CD1 1 
ATOM   2965 N N   . GLU B 1 162 ? 22.42112 -10.25371 -0.64345  1.000 50.95894  ? 162 GLU A N   1 
ATOM   2966 C CA  . GLU B 1 162 ? 23.77717 -10.68923 -0.33762  1.000 51.44074  ? 162 GLU A CA  1 
ATOM   2967 C C   . GLU B 1 162 ? 23.82819 -11.47326 0.96396   1.000 56.25809  ? 162 GLU A C   1 
ATOM   2968 O O   . GLU B 1 162 ? 24.54295 -12.47681 1.06362   1.000 57.47454  ? 162 GLU A O   1 
ATOM   2969 C CB  . GLU B 1 162 ? 24.70171 -9.47811  -0.26236  1.000 54.35535  ? 162 GLU A CB  1 
ATOM   2970 C CG  . GLU B 1 162 ? 26.13299 -9.78779  0.04543   1.000 48.86772  ? 162 GLU A CG  1 
ATOM   2971 C CD  . GLU B 1 162 ? 26.90874 -8.53514  0.37219   1.000 52.53356  ? 162 GLU A CD  1 
ATOM   2972 O OE1 . GLU B 1 162 ? 26.54520 -7.88447  1.37246   1.000 52.94690  ? 162 GLU A OE1 1 
ATOM   2973 O OE2 . GLU B 1 162 ? 27.87259 -8.19272  -0.35218  1.000 53.76635  ? 162 GLU A OE2 1 
ATOM   2974 N N   . ALA B 1 163 ? 23.07501 -11.03004 1.97242   1.000 54.28615  ? 163 ALA A N   1 
ATOM   2975 C CA  . ALA B 1 163 ? 23.05941 -11.69934 3.26518   1.000 55.78561  ? 163 ALA A CA  1 
ATOM   2976 C C   . ALA B 1 163 ? 22.27033 -12.99874 3.22647   1.000 58.92028  ? 163 ALA A C   1 
ATOM   2977 O O   . ALA B 1 163 ? 22.60112 -13.94483 3.95023   1.000 58.31264  ? 163 ALA A O   1 
ATOM   2978 C CB  . ALA B 1 163 ? 22.46286 -10.77798 4.32723   1.000 55.83008  ? 163 ALA A CB  1 
ATOM   2979 N N   . LEU B 1 164 ? 21.20891 -13.05210 2.42476   1.000 60.25231  ? 164 LEU A N   1 
ATOM   2980 C CA  . LEU B 1 164 ? 20.41841 -14.26859 2.36114   1.000 59.42608  ? 164 LEU A CA  1 
ATOM   2981 C C   . LEU B 1 164 ? 21.22209 -15.39975 1.73347   1.000 62.48514  ? 164 LEU A C   1 
ATOM   2982 O O   . LEU B 1 164 ? 21.16304 -16.54169 2.20488   1.000 65.79437  ? 164 LEU A O   1 
ATOM   2983 C CB  . LEU B 1 164 ? 19.12108 -14.00569 1.59891   1.000 56.73479  ? 164 LEU A CB  1 
ATOM   2984 C CG  . LEU B 1 164 ? 18.08320 -13.15265 2.34275   1.000 60.35537  ? 164 LEU A CG  1 
ATOM   2985 C CD1 . LEU B 1 164 ? 16.80902 -12.96026 1.52457   1.000 53.81922  ? 164 LEU A CD1 1 
ATOM   2986 C CD2 . LEU B 1 164 ? 17.73622 -13.76285 3.68818   1.000 62.06458  ? 164 LEU A CD2 1 
ATOM   2987 N N   . LEU B 1 165 ? 22.02215 -15.09209 0.70835   1.000 58.98376  ? 165 LEU A N   1 
ATOM   2988 C CA  . LEU B 1 165 ? 22.76073 -16.10141 -0.04527  1.000 57.31307  ? 165 LEU A CA  1 
ATOM   2989 C C   . LEU B 1 165 ? 24.17528 -16.33185 0.47781   1.000 61.62160  ? 165 LEU A C   1 
ATOM   2990 O O   . LEU B 1 165 ? 24.86979 -17.22864 -0.01702  1.000 60.98945  ? 165 LEU A O   1 
ATOM   2991 C CB  . LEU B 1 165 ? 22.81876 -15.69670 -1.52088  1.000 56.89649  ? 165 LEU A CB  1 
ATOM   2992 C CG  . LEU B 1 165 ? 21.46319 -15.27406 -2.09201  1.000 59.17588  ? 165 LEU A CG  1 
ATOM   2993 C CD1 . LEU B 1 165 ? 21.61934 -14.82690 -3.51977  1.000 57.58693  ? 165 LEU A CD1 1 
ATOM   2994 C CD2 . LEU B 1 165 ? 20.44007 -16.38892 -1.98939  1.000 57.49178  ? 165 LEU A CD2 1 
ATOM   2995 N N   . LEU B 1 166 ? 24.61868 -15.53583 1.45072   1.000 64.43104  ? 166 LEU A N   1 
ATOM   2996 C CA  . LEU B 1 166 ? 25.93580 -15.67088 2.07490   1.000 59.02080  ? 166 LEU A CA  1 
ATOM   2997 C C   . LEU B 1 166 ? 27.08024 -15.62667 1.06402   1.000 62.40854  ? 166 LEU A C   1 
ATOM   2998 O O   . LEU B 1 166 ? 28.10492 -16.28092 1.26250   1.000 68.51830  ? 166 LEU A O   1 
ATOM   2999 C CB  . LEU B 1 166 ? 26.02538 -16.94610 2.91748   1.000 58.57442  ? 166 LEU A CB  1 
ATOM   3000 C CG  . LEU B 1 166 ? 25.07444 -17.03166 4.11183   1.000 61.95534  ? 166 LEU A CG  1 
ATOM   3001 C CD1 . LEU B 1 166 ? 24.78600 -18.47104 4.48494   1.000 62.11428  ? 166 LEU A CD1 1 
ATOM   3002 C CD2 . LEU B 1 166 ? 25.63304 -16.27063 5.29322   1.000 63.66529  ? 166 LEU A CD2 1 
ATOM   3003 N N   . VAL B 1 167 ? 26.93504 -14.84877 -0.01227  1.000 61.77059  ? 167 VAL A N   1 
ATOM   3004 C CA  . VAL B 1 167 ? 27.98763 -14.64543 -1.01352  1.000 57.52287  ? 167 VAL A CA  1 
ATOM   3005 C C   . VAL B 1 167 ? 28.24583 -13.14611 -1.13674  1.000 58.51129  ? 167 VAL A C   1 
ATOM   3006 O O   . VAL B 1 167 ? 27.43306 -12.41639 -1.72629  1.000 58.11419  ? 167 VAL A O   1 
ATOM   3007 C CB  . VAL B 1 167 ? 27.61030 -15.23729 -2.38140  1.000 62.76330  ? 167 VAL A CB  1 
ATOM   3008 C CG1 . VAL B 1 167 ? 28.79120 -15.14516 -3.34822  1.000 56.74640  ? 167 VAL A CG1 1 
ATOM   3009 C CG2 . VAL B 1 167 ? 27.12617 -16.67025 -2.24944  1.000 59.66501  ? 167 VAL A CG2 1 
ATOM   3010 N N   . ARG B 1 168 ? 29.38455 -12.68858 -0.61050  1.000 58.02013  ? 168 ARG A N   1 
ATOM   3011 C CA  . ARG B 1 168 ? 29.75520 -11.28197 -0.71591  1.000 57.13188  ? 168 ARG A CA  1 
ATOM   3012 C C   . ARG B 1 168 ? 29.66516 -10.80722 -2.16290  1.000 59.72578  ? 168 ARG A C   1 
ATOM   3013 O O   . ARG B 1 168 ? 30.05564 -11.51986 -3.09201  1.000 56.31926  ? 168 ARG A O   1 
ATOM   3014 C CB  . ARG B 1 168 ? 31.17659 -11.05542 -0.18337  1.000 53.79640  ? 168 ARG A CB  1 
ATOM   3015 C CG  . ARG B 1 168 ? 31.71721 -9.63991  -0.42241  1.000 48.38395  ? 168 ARG A CG  1 
ATOM   3016 C CD  . ARG B 1 168 ? 32.77475 -9.26322  0.61576   1.000 51.87032  ? 168 ARG A CD  1 
ATOM   3017 N NE  . ARG B 1 168 ? 33.27110 -7.89223  0.49160   1.000 48.76334  ? 168 ARG A NE  1 
ATOM   3018 C CZ  . ARG B 1 168 ? 33.42190 -7.06763  1.52441   1.000 49.77369  ? 168 ARG A CZ  1 
ATOM   3019 N NH1 . ARG B 1 168 ? 33.12230 -7.45133  2.75979   1.000 46.09436  ? 168 ARG A NH1 1 
ATOM   3020 N NH2 . ARG B 1 168 ? 33.86102 -5.82139  1.31220   1.000 42.51444  ? 168 ARG A NH2 1 
ATOM   3021 N N   . ASP B 1 169 ? 29.11601 -9.60221  -2.34355  1.000 56.35384  ? 169 ASP A N   1 
ATOM   3022 C CA  . ASP B 1 169 ? 29.04271 -8.88380  -3.61387  1.000 55.22343  ? 169 ASP A CA  1 
ATOM   3023 C C   . ASP B 1 169 ? 28.00920 -9.46650  -4.55915  1.000 53.64860  ? 169 ASP A C   1 
ATOM   3024 O O   . ASP B 1 169 ? 27.95061 -9.05489  -5.72392  1.000 55.11041  ? 169 ASP A O   1 
ATOM   3025 C CB  . ASP B 1 169 ? 30.40493 -8.81174  -4.32338  1.000 54.29108  ? 169 ASP A CB  1 
ATOM   3026 N N   . MET B 1 170 ? 27.17143 -10.39338 -4.08977  1.000 59.43909  ? 170 MET A N   1 
ATOM   3027 C CA  . MET B 1 170 ? 26.14349 -11.02068 -4.91744  1.000 56.60132  ? 170 MET A CA  1 
ATOM   3028 C C   . MET B 1 170 ? 24.80800 -10.37582 -4.56380  1.000 60.31081  ? 170 MET A C   1 
ATOM   3029 O O   . MET B 1 170 ? 24.17768 -10.72312 -3.55856  1.000 59.30133  ? 170 MET A O   1 
ATOM   3030 C CB  . MET B 1 170 ? 26.11157 -12.52841 -4.69950  1.000 59.82044  ? 170 MET A CB  1 
ATOM   3031 C CG  . MET B 1 170 ? 25.02835 -13.23819 -5.50623  1.000 63.85099  ? 170 MET A CG  1 
ATOM   3032 S SD  . MET B 1 170 ? 25.45396 -14.95795 -5.87765  1.000 78.28253  ? 170 MET A SD  1 
ATOM   3033 C CE  . MET B 1 170 ? 23.83676 -15.70019 -6.03032  1.000 58.65668  ? 170 MET A CE  1 
ATOM   3034 N N   . THR B 1 171 ? 24.36422 -9.43891  -5.39673  1.000 60.90074  ? 171 THR A N   1 
ATOM   3035 C CA  . THR B 1 171 ? 23.16719 -8.66806  -5.08955  1.000 57.35162  ? 171 THR A CA  1 
ATOM   3036 C C   . THR B 1 171 ? 22.01168 -9.00152  -6.01674  1.000 56.15537  ? 171 THR A C   1 
ATOM   3037 O O   . THR B 1 171 ? 20.99888 -8.29339  -6.00155  1.000 51.58281  ? 171 THR A O   1 
ATOM   3038 C CB  . THR B 1 171 ? 23.47053 -7.17277  -5.15760  1.000 50.58363  ? 171 THR A CB  1 
ATOM   3039 O OG1 . THR B 1 171 ? 24.00892 -6.87681  -6.44485  1.000 52.65914  ? 171 THR A OG1 1 
ATOM   3040 C CG2 . THR B 1 171 ? 24.51284 -6.81685  -4.12440  1.000 50.94669  ? 171 THR A CG2 1 
ATOM   3041 N N   . THR B 1 172 ? 22.15364 -10.03281 -6.84699  1.000 56.74758  ? 172 THR A N   1 
ATOM   3042 C CA  . THR B 1 172 ? 21.05078 -10.58990 -7.61929  1.000 60.90920  ? 172 THR A CA  1 
ATOM   3043 C C   . THR B 1 172 ? 20.87144 -12.04538 -7.22282  1.000 62.27238  ? 172 THR A C   1 
ATOM   3044 O O   . THR B 1 172 ? 21.71847 -12.63145 -6.54069  1.000 62.57042  ? 172 THR A O   1 
ATOM   3045 C CB  . THR B 1 172 ? 21.29342 -10.46735 -9.12750  1.000 60.63737  ? 172 THR A CB  1 
ATOM   3046 O OG1 . THR B 1 172 ? 22.48980 -11.16882 -9.47777  1.000 64.73621  ? 172 THR A OG1 1 
ATOM   3047 C CG2 . THR B 1 172 ? 21.44743 -9.01452  -9.51561  1.000 60.98857  ? 172 THR A CG2 1 
ATOM   3048 N N   . CYS B 1 173 ? 19.75360 -12.63354 -7.65519  1.000 61.70871  ? 173 CYS A N   1 
ATOM   3049 C CA  . CYS B 1 173 ? 19.40913 -14.00230 -7.25346  1.000 65.62184  ? 173 CYS A CA  1 
ATOM   3050 C C   . CYS B 1 173 ? 18.77418 -14.76332 -8.41425  1.000 68.72772  ? 173 CYS A C   1 
ATOM   3051 O O   . CYS B 1 173 ? 17.79408 -14.27664 -9.00855  1.000 68.47627  ? 173 CYS A O   1 
ATOM   3052 C CB  . CYS B 1 173 ? 18.46495 -13.98133 -6.05131  1.000 68.00498  ? 173 CYS A CB  1 
ATOM   3053 S SG  . CYS B 1 173 ? 17.85302 -15.59448 -5.55788  1.000 69.12948  ? 173 CYS A SG  1 
ATOM   3054 N N   . PRO B 1 174 ? 19.29399 -15.94305 -8.75972  1.000 73.41675  ? 174 PRO A N   1 
ATOM   3055 C CA  . PRO B 1 174 ? 18.73785 -16.68860 -9.89731  1.000 73.86406  ? 174 PRO A CA  1 
ATOM   3056 C C   . PRO B 1 174 ? 17.33864 -17.19927 -9.60389  1.000 74.88870  ? 174 PRO A C   1 
ATOM   3057 O O   . PRO B 1 174 ? 17.07562 -17.76424 -8.54028  1.000 76.95415  ? 174 PRO A O   1 
ATOM   3058 C CB  . PRO B 1 174 ? 19.72452 -17.84890 -10.07729 1.000 72.42294  ? 174 PRO A CB  1 
ATOM   3059 C CG  . PRO B 1 174 ? 20.36589 -18.01256 -8.73938  1.000 70.34813  ? 174 PRO A CG  1 
ATOM   3060 C CD  . PRO B 1 174 ? 20.48072 -16.61093 -8.19479  1.000 73.45511  ? 174 PRO A CD  1 
ATOM   3061 N N   . LEU B 1 175 ? 16.44191 -17.00925 -10.57371 1.000 76.20088  ? 175 LEU A N   1 
ATOM   3062 C CA  . LEU B 1 175 ? 15.05304 -17.44338 -10.49818 1.000 78.55839  ? 175 LEU A CA  1 
ATOM   3063 C C   . LEU B 1 175 ? 14.81216 -18.63969 -11.41469 1.000 81.17347  ? 175 LEU A C   1 
ATOM   3064 O O   . LEU B 1 175 ? 15.41609 -18.73073 -12.48724 1.000 84.85671  ? 175 LEU A O   1 
ATOM   3065 C CB  . LEU B 1 175 ? 14.10713 -16.31044 -10.90397 1.000 75.88297  ? 175 LEU A CB  1 
ATOM   3066 C CG  . LEU B 1 175 ? 14.28546 -14.99825 -10.14569 1.000 74.16679  ? 175 LEU A CG  1 
ATOM   3067 C CD1 . LEU B 1 175 ? 13.17021 -14.03881 -10.52014 1.000 69.37414  ? 175 LEU A CD1 1 
ATOM   3068 C CD2 . LEU B 1 175 ? 14.30418 -15.25937 -8.64300  1.000 71.28102  ? 175 LEU A CD2 1 
ATOM   3069 N N   . PRO B 1 176 ? 13.92938 -19.56946 -11.02880 1.000 79.74629  ? 176 PRO A N   1 
ATOM   3070 C CA  . PRO B 1 176 ? 13.65743 -20.73531 -11.88415 1.000 82.36260  ? 176 PRO A CA  1 
ATOM   3071 C C   . PRO B 1 176 ? 13.33515 -20.36653 -13.32803 1.000 84.51181  ? 176 PRO A C   1 
ATOM   3072 O O   . PRO B 1 176 ? 12.88473 -19.24782 -13.60827 1.000 80.50668  ? 176 PRO A O   1 
ATOM   3073 C CB  . PRO B 1 176 ? 12.46121 -21.39931 -11.19226 1.000 78.01918  ? 176 PRO A CB  1 
ATOM   3074 C CG  . PRO B 1 176 ? 12.59874 -21.00914 -9.76260  1.000 78.36952  ? 176 PRO A CG  1 
ATOM   3075 C CD  . PRO B 1 176 ? 13.17396 -19.61861 -9.76585  1.000 80.33455  ? 176 PRO A CD  1 
ATOM   3076 N N   . LYS B 1 177 ? 13.57631 -21.30951 -14.24349 1.000 86.71892  ? 177 LYS A N   1 
ATOM   3077 C CA  . LYS B 1 177 ? 13.41351 -21.06927 -15.67413 1.000 84.15060  ? 177 LYS A CA  1 
ATOM   3078 C C   . LYS B 1 177 ? 12.05315 -20.45858 -15.99009 1.000 78.39928  ? 177 LYS A C   1 
ATOM   3079 O O   . LYS B 1 177 ? 11.02071 -20.91166 -15.48778 1.000 80.46262  ? 177 LYS A O   1 
ATOM   3080 C CB  . LYS B 1 177 ? 13.59154 -22.38265 -16.44165 1.000 87.14993  ? 177 LYS A CB  1 
ATOM   3081 N N   . GLY B 1 178 ? 12.06715 -19.40865 -16.81128 1.000 75.24802  ? 178 GLY A N   1 
ATOM   3082 C CA  . GLY B 1 178 ? 10.86354 -18.75219 -17.26714 1.000 75.33053  ? 178 GLY A CA  1 
ATOM   3083 C C   . GLY B 1 178 ? 10.16614 -17.86484 -16.25707 1.000 78.16505  ? 178 GLY A C   1 
ATOM   3084 O O   . GLY B 1 178 ? 9.06449  -17.37988 -16.55032 1.000 75.67825  ? 178 GLY A O   1 
ATOM   3085 N N   . THR B 1 179 ? 10.76131 -17.62757 -15.08250 1.000 75.12611  ? 179 THR A N   1 
ATOM   3086 C CA  . THR B 1 179 ? 10.10158 -16.78809 -14.08219 1.000 74.68060  ? 179 THR A CA  1 
ATOM   3087 C C   . THR B 1 179 ? 9.88357  -15.36507 -14.59114 1.000 71.99743  ? 179 THR A C   1 
ATOM   3088 O O   . THR B 1 179 ? 8.92054  -14.70121 -14.18875 1.000 68.50941  ? 179 THR A O   1 
ATOM   3089 C CB  . THR B 1 179 ? 10.91800 -16.77491 -12.78498 1.000 76.50740  ? 179 THR A CB  1 
ATOM   3090 O OG1 . THR B 1 179 ? 11.15402 -18.12151 -12.35000 1.000 80.66901  ? 179 THR A OG1 1 
ATOM   3091 C CG2 . THR B 1 179 ? 10.19927 -16.00794 -11.67830 1.000 72.95354  ? 179 THR A CG2 1 
ATOM   3092 N N   . LEU B 1 180 ? 10.74179 -14.88900 -15.49301 1.000 69.44766  ? 180 LEU A N   1 
ATOM   3093 C CA  . LEU B 1 180 ? 10.69102 -13.51130 -15.96993 1.000 71.28350  ? 180 LEU A CA  1 
ATOM   3094 C C   . LEU B 1 180 ? 10.18218 -13.41547 -17.40664 1.000 71.44388  ? 180 LEU A C   1 
ATOM   3095 O O   . LEU B 1 180 ? 10.55909 -12.50332 -18.14551 1.000 72.02377  ? 180 LEU A O   1 
ATOM   3096 C CB  . LEU B 1 180 ? 12.06391 -12.84927 -15.84039 1.000 64.82562  ? 180 LEU A CB  1 
ATOM   3097 N N   . ASP B 1 181 ? 9.32553  -14.34733 -17.81366 1.000 70.59561  ? 181 ASP A N   1 
ATOM   3098 C CA  . ASP B 1 181 ? 8.74427  -14.29704 -19.14810 1.000 68.34657  ? 181 ASP A CA  1 
ATOM   3099 C C   . ASP B 1 181 ? 7.82625  -13.08814 -19.26514 1.000 68.31570  ? 181 ASP A C   1 
ATOM   3100 O O   . ASP B 1 181 ? 6.92383  -12.89878 -18.44415 1.000 70.60523  ? 181 ASP A O   1 
ATOM   3101 C CB  . ASP B 1 181 ? 7.97293  -15.58498 -19.44274 1.000 72.96393  ? 181 ASP A CB  1 
ATOM   3102 N N   . GLY B 1 182 ? 8.05811  -12.26632 -20.28332 1.000 69.44326  ? 182 GLY A N   1 
ATOM   3103 C CA  . GLY B 1 182 ? 7.33881  -11.01880 -20.44003 1.000 66.27372  ? 182 GLY A CA  1 
ATOM   3104 C C   . GLY B 1 182 ? 8.08586  -9.79208  -19.96902 1.000 66.13494  ? 182 GLY A C   1 
ATOM   3105 O O   . GLY B 1 182 ? 7.49950  -8.70588  -19.93442 1.000 67.66199  ? 182 GLY A O   1 
ATOM   3106 N N   . PHE B 1 183 ? 9.35319  -9.93311  -19.60199 1.000 63.04834  ? 183 PHE A N   1 
ATOM   3107 C CA  . PHE B 1 183 ? 10.15106 -8.81129  -19.12988 1.000 63.22852  ? 183 PHE A CA  1 
ATOM   3108 C C   . PHE B 1 183 ? 10.48338 -7.86601  -20.28205 1.000 64.16932  ? 183 PHE A C   1 
ATOM   3109 O O   . PHE B 1 183 ? 10.90662 -8.31237  -21.35131 1.000 66.90193  ? 183 PHE A O   1 
ATOM   3110 C CB  . PHE B 1 183 ? 11.42770 -9.35864  -18.49372 1.000 65.84731  ? 183 PHE A CB  1 
ATOM   3111 C CG  . PHE B 1 183 ? 12.27186 -8.32997  -17.80402 1.000 63.48068  ? 183 PHE A CG  1 
ATOM   3112 C CD1 . PHE B 1 183 ? 11.94194 -7.87459  -16.53656 1.000 63.95121  ? 183 PHE A CD1 1 
ATOM   3113 C CD2 . PHE B 1 183 ? 13.42052 -7.85613  -18.39969 1.000 59.11428  ? 183 PHE A CD2 1 
ATOM   3114 C CE1 . PHE B 1 183 ? 12.73376 -6.94436  -15.88879 1.000 57.63209  ? 183 PHE A CE1 1 
ATOM   3115 C CE2 . PHE B 1 183 ? 14.20923 -6.92373  -17.75740 1.000 63.08041  ? 183 PHE A CE2 1 
ATOM   3116 C CZ  . PHE B 1 183 ? 13.86278 -6.46898  -16.50156 1.000 57.80921  ? 183 PHE A CZ  1 
ATOM   3117 N N   . VAL B 1 184 ? 10.28665 -6.56140  -20.06991 1.000 61.15243  ? 184 VAL A N   1 
ATOM   3118 C CA  . VAL B 1 184 ? 10.74954 -5.52028  -20.98671 1.000 60.66214  ? 184 VAL A CA  1 
ATOM   3119 C C   . VAL B 1 184 ? 11.84645 -4.72946  -20.28441 1.000 62.60382  ? 184 VAL A C   1 
ATOM   3120 O O   . VAL B 1 184 ? 11.63096 -4.20249  -19.18551 1.000 63.60180  ? 184 VAL A O   1 
ATOM   3121 C CB  . VAL B 1 184 ? 9.60461  -4.59824  -21.43843 1.000 60.31036  ? 184 VAL A CB  1 
ATOM   3122 N N   . ALA B 1 185 ? 13.00155 -4.60513  -20.94803 1.000 60.36692  ? 185 ALA A N   1 
ATOM   3123 C CA  . ALA B 1 185 ? 14.26303 -4.32623  -20.25995 1.000 61.53103  ? 185 ALA A CA  1 
ATOM   3124 C C   . ALA B 1 185 ? 14.24222 -2.99918  -19.50440 1.000 65.56387  ? 185 ALA A C   1 
ATOM   3125 O O   . ALA B 1 185 ? 14.84664 -2.87874  -18.42368 1.000 65.97702  ? 185 ALA A O   1 
ATOM   3126 C CB  . ALA B 1 185 ? 15.41512 -4.33707  -21.26643 1.000 55.21128  ? 185 ALA A CB  1 
ATOM   3127 N N   . HIS B 1 186 ? 13.58053 -1.98699  -20.05947 1.000 58.55900  ? 186 HIS A N   1 
ATOM   3128 C CA  . HIS B 1 186 ? 13.61181 -0.64432  -19.49788 1.000 49.72016  ? 186 HIS A CA  1 
ATOM   3129 C C   . HIS B 1 186 ? 12.21981 -0.19908  -19.09268 1.000 54.64643  ? 186 HIS A C   1 
ATOM   3130 O O   . HIS B 1 186 ? 11.83702 0.95795   -19.25950 1.000 58.59695  ? 186 HIS A O   1 
ATOM   3131 C CB  . HIS B 1 186 ? 14.24536 0.32666   -20.48355 1.000 54.37818  ? 186 HIS A CB  1 
ATOM   3132 C CG  . HIS B 1 186 ? 15.70447 0.07128   -20.71289 1.000 55.51858  ? 186 HIS A CG  1 
ATOM   3133 N ND1 . HIS B 1 186 ? 16.19151 -0.49911  -21.87000 1.000 56.36477  ? 186 HIS A ND1 1 
ATOM   3134 C CD2 . HIS B 1 186 ? 16.77948 0.28911   -19.91969 1.000 53.36423  ? 186 HIS A CD2 1 
ATOM   3135 C CE1 . HIS B 1 186 ? 17.50386 -0.61237  -21.78647 1.000 52.09751  ? 186 HIS A CE1 1 
ATOM   3136 N NE2 . HIS B 1 186 ? 17.88593 -0.14297  -20.61182 1.000 59.48331  ? 186 HIS A NE2 1 
ATOM   3137 N N   . ASP B 1 187 ? 11.44396 -1.13603  -18.56603 1.000 51.18824  ? 187 ASP A N   1 
ATOM   3138 C CA  . ASP B 1 187 ? 10.13705 -0.85773  -17.99546 1.000 51.66399  ? 187 ASP A CA  1 
ATOM   3139 C C   . ASP B 1 187 ? 10.33082 -0.71946  -16.49548 1.000 46.87435  ? 187 ASP A C   1 
ATOM   3140 O O   . ASP B 1 187 ? 10.64829 -1.70083  -15.81745 1.000 51.87410  ? 187 ASP A O   1 
ATOM   3141 C CB  . ASP B 1 187 ? 9.15333  -1.98187  -18.32373 1.000 54.62096  ? 187 ASP A CB  1 
ATOM   3142 C CG  . ASP B 1 187 ? 7.77469  -1.72275  -17.78503 1.000 49.61945  ? 187 ASP A CG  1 
ATOM   3143 O OD1 . ASP B 1 187 ? 7.56774  -1.90746  -16.57094 1.000 52.07701  ? 187 ASP A OD1 1 
ATOM   3144 O OD2 . ASP B 1 187 ? 6.89383  -1.33882  -18.57625 1.000 54.71786  ? 187 ASP A OD2 1 
ATOM   3145 N N   . SER B 1 188 ? 10.14959 0.49332   -15.98012 1.000 43.18624  ? 188 SER A N   1 
ATOM   3146 C CA  . SER B 1 188 ? 10.39032 0.73882   -14.55740 1.000 43.63937  ? 188 SER A CA  1 
ATOM   3147 C C   . SER B 1 188 ? 9.65735  -0.25086  -13.66115 1.000 42.90767  ? 188 SER A C   1 
ATOM   3148 O O   . SER B 1 188 ? 10.19241 -0.67559  -12.63058 1.000 43.07715  ? 188 SER A O   1 
ATOM   3149 C CB  . SER B 1 188 ? 9.97490  2.16223   -14.18174 1.000 43.32194  ? 188 SER A CB  1 
ATOM   3150 O OG  . SER B 1 188 ? 10.67870 3.14131   -14.92669 1.000 45.11919  ? 188 SER A OG  1 
ATOM   3151 N N   . ILE B 1 189 ? 8.41235  -0.59918  -14.00874 1.000 51.39570  ? 189 ILE A N   1 
ATOM   3152 C CA  . ILE B 1 189 ? 7.62218  -1.46996  -13.13743 1.000 46.13409  ? 189 ILE A CA  1 
ATOM   3153 C C   . ILE B 1 189 ? 8.17709  -2.88503  -13.16494 1.000 47.76721  ? 189 ILE A C   1 
ATOM   3154 O O   . ILE B 1 189 ? 8.22039  -3.57127  -12.13367 1.000 47.49290  ? 189 ILE A O   1 
ATOM   3155 C CB  . ILE B 1 189 ? 6.12951  -1.44085  -13.52119 1.000 47.01337  ? 189 ILE A CB  1 
ATOM   3156 C CG1 . ILE B 1 189 ? 5.54930  -0.03074  -13.39405 1.000 49.67816  ? 189 ILE A CG1 1 
ATOM   3157 C CG2 . ILE B 1 189 ? 5.33786  -2.36203  -12.60935 1.000 49.58583  ? 189 ILE A CG2 1 
ATOM   3158 C CD1 . ILE B 1 189 ? 4.03792  -0.00540  -13.29800 1.000 54.35365  ? 189 ILE A CD1 1 
ATOM   3159 N N   . HIS B 1 190 ? 8.63167  -3.33858  -14.33618 1.000 51.40238  ? 190 HIS A N   1 
ATOM   3160 C CA  . HIS B 1 190 ? 9.21407  -4.67614  -14.42873 1.000 53.54162  ? 190 HIS A CA  1 
ATOM   3161 C C   . HIS B 1 190 ? 10.44388 -4.79508  -13.54701 1.000 53.11073  ? 190 HIS A C   1 
ATOM   3162 O O   . HIS B 1 190 ? 10.57371 -5.75715  -12.78145 1.000 53.11519  ? 190 HIS A O   1 
ATOM   3163 C CB  . HIS B 1 190 ? 9.56042  -5.01771  -15.88080 1.000 54.49414  ? 190 HIS A CB  1 
ATOM   3164 C CG  . HIS B 1 190 ? 8.35655  -5.23534  -16.74270 1.000 59.96835  ? 190 HIS A CG  1 
ATOM   3165 N ND1 . HIS B 1 190 ? 8.41920  -5.86239  -17.96770 1.000 62.12614  ? 190 HIS A ND1 1 
ATOM   3166 C CD2 . HIS B 1 190 ? 7.05457  -4.90391  -16.55420 1.000 57.51028  ? 190 HIS A CD2 1 
ATOM   3167 C CE1 . HIS B 1 190 ? 7.20698  -5.91334  -18.49465 1.000 60.88518  ? 190 HIS A CE1 1 
ATOM   3168 N NE2 . HIS B 1 190 ? 6.36363  -5.33150  -17.66068 1.000 54.74010  ? 190 HIS A NE2 1 
ATOM   3169 N N   . ASP B 1 191 ? 11.35307 -3.81313  -13.64217 1.000 52.11237  ? 191 ASP A N   1 
ATOM   3170 C CA  . ASP B 1 191 ? 12.57757 -3.80247  -12.84175 1.000 49.74161  ? 191 ASP A CA  1 
ATOM   3171 C C   . ASP B 1 191 ? 12.28788 -4.03963  -11.36456 1.000 50.79982  ? 191 ASP A C   1 
ATOM   3172 O O   . ASP B 1 191 ? 12.97152 -4.83427  -10.70460 1.000 49.60930  ? 191 ASP A O   1 
ATOM   3173 C CB  . ASP B 1 191 ? 13.29742 -2.46977  -13.01652 1.000 51.50523  ? 191 ASP A CB  1 
ATOM   3174 C CG  . ASP B 1 191 ? 14.20235 -2.44445  -14.22721 1.000 57.27234  ? 191 ASP A CG  1 
ATOM   3175 O OD1 . ASP B 1 191 ? 14.66616 -3.53096  -14.64059 1.000 55.55734  ? 191 ASP A OD1 1 
ATOM   3176 O OD2 . ASP B 1 191 ? 14.46010 -1.32990  -14.74711 1.000 56.18415  ? 191 ASP A OD2 1 
ATOM   3177 N N   . CYS B 1 192 ? 11.28823 -3.33149  -10.82329 1.000 44.88611  ? 192 CYS A N   1 
ATOM   3178 C CA  . CYS B 1 192 ? 10.89396 -3.54770  -9.43642  1.000 49.75352  ? 192 CYS A CA  1 
ATOM   3179 C C   . CYS B 1 192 ? 10.28718 -4.93360  -9.24345  1.000 49.45161  ? 192 CYS A C   1 
ATOM   3180 O O   . CYS B 1 192 ? 10.40335 -5.52614  -8.16271  1.000 47.72016  ? 192 CYS A O   1 
ATOM   3181 C CB  . CYS B 1 192 ? 9.89287  -2.47197  -8.98797  1.000 50.52454  ? 192 CYS A CB  1 
ATOM   3182 S SG  . CYS B 1 192 ? 10.51199 -0.74850  -8.86555  1.000 45.21964  ? 192 CYS A SG  1 
ATOM   3183 N N   . ALA B 1 193 ? 9.61407  -5.45616  -10.26284 1.000 52.62916  ? 193 ALA A N   1 
ATOM   3184 C CA  . ALA B 1 193 ? 9.02339  -6.78177  -10.12534 1.000 51.57900  ? 193 ALA A CA  1 
ATOM   3185 C C   . ALA B 1 193 ? 10.10429 -7.84977  -10.04851 1.000 54.23929  ? 193 ALA A C   1 
ATOM   3186 O O   . ALA B 1 193 ? 10.01474 -8.77145  -9.22881  1.000 54.14119  ? 193 ALA A O   1 
ATOM   3187 C CB  . ALA B 1 193 ? 8.07059  -7.05186  -11.28627 1.000 53.39732  ? 193 ALA A CB  1 
ATOM   3188 N N   . LYS B 1 194 ? 11.14409 -7.73018  -10.88273 1.000 51.21035  ? 194 LYS A N   1 
ATOM   3189 C CA  . LYS B 1 194 ? 12.24311 -8.68807  -10.84039 1.000 51.28994  ? 194 LYS A CA  1 
ATOM   3190 C C   . LYS B 1 194 ? 12.98254 -8.62637  -9.50717  1.000 57.40465  ? 194 LYS A C   1 
ATOM   3191 O O   . LYS B 1 194 ? 13.39178 -9.66380  -8.96789  1.000 59.13498  ? 194 LYS A O   1 
ATOM   3192 C CB  . LYS B 1 194 ? 13.20515 -8.44005  -12.00504 1.000 50.09453  ? 194 LYS A CB  1 
ATOM   3193 N N   . ASP B 1 195 ? 13.16945 -7.41795  -8.96067  1.000 54.13496  ? 195 ASP A N   1 
ATOM   3194 C CA  . ASP B 1 195 ? 13.82108 -7.28442  -7.66060  1.000 55.81108  ? 195 ASP A CA  1 
ATOM   3195 C C   . ASP B 1 195 ? 12.96530 -7.86864  -6.53496  1.000 53.59278  ? 195 ASP A C   1 
ATOM   3196 O O   . ASP B 1 195 ? 13.50245 -8.43280  -5.57469  1.000 54.53202  ? 195 ASP A O   1 
ATOM   3197 C CB  . ASP B 1 195 ? 14.14449 -5.81135  -7.39284  1.000 54.49291  ? 195 ASP A CB  1 
ATOM   3198 C CG  . ASP B 1 195 ? 15.63070 -5.48978  -7.57651  1.000 58.94397  ? 195 ASP A CG  1 
ATOM   3199 O OD1 . ASP B 1 195 ? 16.43127 -6.44040  -7.72049  1.000 56.77452  ? 195 ASP A OD1 1 
ATOM   3200 O OD2 . ASP B 1 195 ? 15.99559 -4.28426  -7.59845  1.000 53.95813  ? 195 ASP A OD2 1 
ATOM   3201 N N   . ILE B 1 196 ? 11.64237 -7.74467  -6.62838  1.000 52.38054  ? 196 ILE A N   1 
ATOM   3202 C CA  . ILE B 1 196 ? 10.76721 -8.36590  -5.63288  1.000 56.98734  ? 196 ILE A CA  1 
ATOM   3203 C C   . ILE B 1 196 ? 10.88699 -9.88432  -5.68508  1.000 60.80648  ? 196 ILE A C   1 
ATOM   3204 O O   . ILE B 1 196 ? 10.97987 -10.55431 -4.64776  1.000 61.56551  ? 196 ILE A O   1 
ATOM   3205 C CB  . ILE B 1 196 ? 9.30945  -7.93251  -5.84804  1.000 54.47462  ? 196 ILE A CB  1 
ATOM   3206 C CG1 . ILE B 1 196 ? 9.09164  -6.48304  -5.40615  1.000 50.42250  ? 196 ILE A CG1 1 
ATOM   3207 C CG2 . ILE B 1 196 ? 8.36747  -8.88721  -5.10997  1.000 55.78253  ? 196 ILE A CG2 1 
ATOM   3208 C CD1 . ILE B 1 196 ? 7.59369  -6.04848  -5.43566  1.000 46.21525  ? 196 ILE A CD1 1 
ATOM   3209 N N   . LEU B 1 197 ? 10.86737 -10.44834 -6.89484  1.000 58.78641  ? 197 LEU A N   1 
ATOM   3210 C CA  . LEU B 1 197 ? 11.02242 -11.88796 -7.06103  1.000 61.83595  ? 197 LEU A CA  1 
ATOM   3211 C C   . LEU B 1 197 ? 12.38564 -12.37136 -6.57513  1.000 60.22337  ? 197 LEU A C   1 
ATOM   3212 O O   . LEU B 1 197 ? 12.48556 -13.42850 -5.94476  1.000 64.12681  ? 197 LEU A O   1 
ATOM   3213 C CB  . LEU B 1 197 ? 10.81095 -12.25358 -8.53070  1.000 63.84007  ? 197 LEU A CB  1 
ATOM   3214 C CG  . LEU B 1 197 ? 9.34816  -12.29128 -8.96851  1.000 56.26690  ? 197 LEU A CG  1 
ATOM   3215 C CD1 . LEU B 1 197 ? 9.25242  -12.57245 -10.45441 1.000 60.54645  ? 197 LEU A CD1 1 
ATOM   3216 C CD2 . LEU B 1 197 ? 8.64782  -13.36699 -8.17741  1.000 64.86381  ? 197 LEU A CD2 1 
ATOM   3217 N N   . MET B 1 198 ? 13.44988 -11.62457 -6.86862  1.000 56.86277  ? 198 MET A N   1 
ATOM   3218 C CA  . MET B 1 198 ? 14.78277 -12.07359 -6.47879  1.000 59.51044  ? 198 MET A CA  1 
ATOM   3219 C C   . MET B 1 198 ? 14.96602 -12.07009 -4.96407  1.000 60.86841  ? 198 MET A C   1 
ATOM   3220 O O   . MET B 1 198 ? 15.79154 -12.82477 -4.43148  1.000 61.83837  ? 198 MET A O   1 
ATOM   3221 C CB  . MET B 1 198 ? 15.84281 -11.19223 -7.13608  1.000 61.42472  ? 198 MET A CB  1 
ATOM   3222 C CG  . MET B 1 198 ? 16.10450 -11.48220 -8.59744  1.000 57.14539  ? 198 MET A CG  1 
ATOM   3223 S SD  . MET B 1 198 ? 17.55115 -10.55139 -9.13236  1.000 54.20331  ? 198 MET A SD  1 
ATOM   3224 C CE  . MET B 1 198 ? 17.54349 -10.87075 -10.89343 1.000 62.01306  ? 198 MET A CE  1 
ATOM   3225 N N   . MET B 1 199 ? 14.21943 -11.22488 -4.26417  1.000 55.84581  ? 199 MET A N   1 
ATOM   3226 C CA  . MET B 1 199 ? 14.31852 -11.13366 -2.81976  1.000 56.20265  ? 199 MET A CA  1 
ATOM   3227 C C   . MET B 1 199 ? 13.51209 -12.23631 -2.15360  1.000 60.09365  ? 199 MET A C   1 
ATOM   3228 O O   . MET B 1 199 ? 13.91270 -12.74964 -1.10079  1.000 58.89609  ? 199 MET A O   1 
ATOM   3229 C CB  . MET B 1 199 ? 13.80668 -9.76776  -2.37606  1.000 57.85771  ? 199 MET A CB  1 
ATOM   3230 C CG  . MET B 1 199 ? 14.86178 -8.70144  -2.22090  1.000 54.50969  ? 199 MET A CG  1 
ATOM   3231 S SD  . MET B 1 199 ? 14.18856 -7.30210  -1.31376  1.000 56.27701  ? 199 MET A SD  1 
ATOM   3232 C CE  . MET B 1 199 ? 12.75449 -6.85644  -2.30996  1.000 39.56921  ? 199 MET A CE  1 
ATOM   3233 N N   . LYS B 1 200 ? 12.37771 -12.60055 -2.76281  1.000 56.30476  ? 200 LYS A N   1 
ATOM   3234 C CA  . LYS B 1 200 ? 11.54423 -13.69025 -2.26114  1.000 58.12710  ? 200 LYS A CA  1 
ATOM   3235 C C   . LYS B 1 200 ? 12.24023 -15.03671 -2.41609  1.000 62.03301  ? 200 LYS A C   1 
ATOM   3236 O O   . LYS B 1 200 ? 12.27110 -15.84437 -1.48059  1.000 61.91182  ? 200 LYS A O   1 
ATOM   3237 C CB  . LYS B 1 200 ? 10.20259 -13.69899 -3.00036  1.000 59.51015  ? 200 LYS A CB  1 
ATOM   3238 N N   . TYR B 1 201 ? 12.80933 -15.29674 -3.59573  1.000 63.91672  ? 201 TYR A N   1 
ATOM   3239 C CA  . TYR B 1 201 ? 13.46240 -16.57803 -3.81687  1.000 63.81066  ? 201 TYR A CA  1 
ATOM   3240 C C   . TYR B 1 201 ? 14.72361 -16.70011 -2.97742  1.000 69.18801  ? 201 TYR A C   1 
ATOM   3241 O O   . TYR B 1 201 ? 15.03400 -17.78460 -2.47537  1.000 75.07934  ? 201 TYR A O   1 
ATOM   3242 C CB  . TYR B 1 201 ? 13.75470 -16.76757 -5.30319  1.000 67.03090  ? 201 TYR A CB  1 
ATOM   3243 C CG  . TYR B 1 201 ? 12.61891 -17.46262 -6.03204  1.000 74.28894  ? 201 TYR A CG  1 
ATOM   3244 C CD1 . TYR B 1 201 ? 12.36387 -18.81773 -5.84124  1.000 72.56409  ? 201 TYR A CD1 1 
ATOM   3245 C CD2 . TYR B 1 201 ? 11.77077 -16.75300 -6.87072  1.000 73.55790  ? 201 TYR A CD2 1 
ATOM   3246 C CE1 . TYR B 1 201 ? 11.32054 -19.44427 -6.49247  1.000 71.46878  ? 201 TYR A CE1 1 
ATOM   3247 C CE2 . TYR B 1 201 ? 10.72511 -17.37321 -7.52743  1.000 72.64423  ? 201 TYR A CE2 1 
ATOM   3248 C CZ  . TYR B 1 201 ? 10.50484 -18.71923 -7.33589  1.000 75.02623  ? 201 TYR A CZ  1 
ATOM   3249 O OH  . TYR B 1 201 ? 9.45971  -19.33207 -7.98977  1.000 74.86417  ? 201 TYR A OH  1 
ATOM   3250 N N   . ALA B 1 202 ? 15.45846 -15.60129 -2.79991  1.000 67.80608  ? 202 ALA A N   1 
ATOM   3251 C CA  . ALA B 1 202 ? 16.56474 -15.61222 -1.84873  1.000 63.51729  ? 202 ALA A CA  1 
ATOM   3252 C C   . ALA B 1 202 ? 16.08030 -15.98404 -0.45216  1.000 64.05182  ? 202 ALA A C   1 
ATOM   3253 O O   . ALA B 1 202 ? 16.76531 -16.70744 0.27728   1.000 65.15695  ? 202 ALA A O   1 
ATOM   3254 C CB  . ALA B 1 202 ? 17.25895 -14.25301 -1.82964  1.000 59.74826  ? 202 ALA A CB  1 
ATOM   3255 N N   . LEU B 1 203 ? 14.89273 -15.51382 -0.06959  1.000 59.21775  ? 203 LEU A N   1 
ATOM   3256 C CA  . LEU B 1 203 ? 14.34812 -15.86024 1.24139   1.000 64.45469  ? 203 LEU A CA  1 
ATOM   3257 C C   . LEU B 1 203 ? 13.97304 -17.33361 1.31757   1.000 69.67659  ? 203 LEU A C   1 
ATOM   3258 O O   . LEU B 1 203 ? 14.14531 -17.96717 2.36513   1.000 69.22306  ? 203 LEU A O   1 
ATOM   3259 C CB  . LEU B 1 203 ? 13.12707 -14.99600 1.56172   1.000 61.75034  ? 203 LEU A CB  1 
ATOM   3260 C CG  . LEU B 1 203 ? 12.45275 -15.25507 2.90831   1.000 60.79571  ? 203 LEU A CG  1 
ATOM   3261 C CD1 . LEU B 1 203 ? 13.46965 -15.22389 4.06044   1.000 59.04367  ? 203 LEU A CD1 1 
ATOM   3262 C CD2 . LEU B 1 203 ? 11.31815 -14.27695 3.15297   1.000 58.72722  ? 203 LEU A CD2 1 
ATOM   3263 N N   . ARG B 1 204 ? 13.45206 -17.89558 0.22204   1.000 70.52010  ? 204 ARG A N   1 
ATOM   3264 C CA  . ARG B 1 204 ? 13.03533 -19.29561 0.23922   1.000 72.89167  ? 204 ARG A CA  1 
ATOM   3265 C C   . ARG B 1 204 ? 14.23727 -20.22777 0.28954   1.000 74.95078  ? 204 ARG A C   1 
ATOM   3266 O O   . ARG B 1 204 ? 14.22836 -21.22635 1.01931   1.000 76.11453  ? 204 ARG A O   1 
ATOM   3267 C CB  . ARG B 1 204 ? 12.16911 -19.60372 -0.98080  1.000 75.71897  ? 204 ARG A CB  1 
ATOM   3268 N N   . TYR B 1 205 ? 15.28815 -19.90782 -0.46392  1.000 73.63532  ? 205 TYR A N   1 
ATOM   3269 C CA  . TYR B 1 205 ? 16.48306 -20.74320 -0.46030  1.000 72.41753  ? 205 TYR A CA  1 
ATOM   3270 C C   . TYR B 1 205 ? 17.14128 -20.74716 0.91836   1.000 79.38589  ? 205 TYR A C   1 
ATOM   3271 O O   . TYR B 1 205 ? 17.47347 -21.80808 1.46144   1.000 85.38934  ? 205 TYR A O   1 
ATOM   3272 C CB  . TYR B 1 205 ? 17.47272 -20.25876 -1.52638  1.000 72.49348  ? 205 TYR A CB  1 
ATOM   3273 C CG  . TYR B 1 205 ? 16.93602 -20.13754 -2.95295  1.000 77.62798  ? 205 TYR A CG  1 
ATOM   3274 C CD1 . TYR B 1 205 ? 15.68746 -20.64338 -3.31501  1.000 77.31938  ? 205 TYR A CD1 1 
ATOM   3275 C CD2 . TYR B 1 205 ? 17.69566 -19.51173 -3.94419  1.000 77.62383  ? 205 TYR A CD2 1 
ATOM   3276 C CE1 . TYR B 1 205 ? 15.21379 -20.52372 -4.62067  1.000 77.10169  ? 205 TYR A CE1 1 
ATOM   3277 C CE2 . TYR B 1 205 ? 17.22917 -19.38833 -5.24914  1.000 75.46549  ? 205 TYR A CE2 1 
ATOM   3278 C CZ  . TYR B 1 205 ? 15.99121 -19.89518 -5.58018  1.000 79.17257  ? 205 TYR A CZ  1 
ATOM   3279 O OH  . TYR B 1 205 ? 15.53061 -19.77376 -6.87355  1.000 80.21500  ? 205 TYR A OH  1 
ATOM   3280 N N   . ALA B 1 206 ? 17.33688 -19.56141 1.50458   1.000 79.75806  ? 206 ALA A N   1 
ATOM   3281 C CA  . ALA B 1 206 ? 18.01296 -19.47571 2.79663   1.000 77.95058  ? 206 ALA A CA  1 
ATOM   3282 C C   . ALA B 1 206 ? 17.20690 -20.14377 3.90168   1.000 80.22149  ? 206 ALA A C   1 
ATOM   3283 O O   . ALA B 1 206 ? 17.78148 -20.57743 4.90626   1.000 85.63852  ? 206 ALA A O   1 
ATOM   3284 C CB  . ALA B 1 206 ? 18.29797 -18.01585 3.15689   1.000 70.93161  ? 206 ALA A CB  1 
ATOM   3285 N N   . MET B 1 207 ? 15.88569 -20.22934 3.74266   1.000 76.78576  ? 207 MET A N   1 
ATOM   3286 C CA  . MET B 1 207 ? 15.07123 -20.99493 4.67884   1.000 74.91867  ? 207 MET A CA  1 
ATOM   3287 C C   . MET B 1 207 ? 15.03503 -22.47343 4.31180   1.000 81.67352  ? 207 MET A C   1 
ATOM   3288 O O   . MET B 1 207 ? 15.02073 -23.33243 5.19824   1.000 87.95156  ? 207 MET A O   1 
ATOM   3289 C CB  . MET B 1 207 ? 13.65120 -20.43771 4.72724   1.000 76.95758  ? 207 MET A CB  1 
ATOM   3290 C CG  . MET B 1 207 ? 13.42736 -19.32561 5.73885   1.000 76.43758  ? 207 MET A CG  1 
ATOM   3291 S SD  . MET B 1 207 ? 11.81877 -18.55040 5.50943   1.000 79.98393  ? 207 MET A SD  1 
ATOM   3292 C CE  . MET B 1 207 ? 11.29698 -18.31001 7.21045   1.000 80.36382  ? 207 MET A CE  1 
ATOM   3293 N N   . GLY B 1 208 ? 15.02850 -22.78933 3.01938   1.000 82.24834  ? 208 GLY A N   1 
ATOM   3294 C CA  . GLY B 1 208 ? 14.95332 -24.16713 2.57628   1.000 82.03968  ? 208 GLY A CA  1 
ATOM   3295 C C   . GLY B 1 208 ? 13.55925 -24.56062 2.13452   1.000 82.67985  ? 208 GLY A C   1 
ATOM   3296 O O   . GLY B 1 208 ? 13.06431 -25.63585 2.48442   1.000 83.50987  ? 208 GLY A O   1 
ATOM   3297 N N   . LEU B 1 209 ? 12.91002 -23.68081 1.37780   1.000 82.30997  ? 209 LEU A N   1 
ATOM   3298 C CA  . LEU B 1 209 ? 11.58852 -23.93010 0.82424   1.000 79.37310  ? 209 LEU A CA  1 
ATOM   3299 C C   . LEU B 1 209 ? 11.64077 -24.24822 -0.65919  1.000 81.42109  ? 209 LEU A C   1 
ATOM   3300 O O   . LEU B 1 209 ? 10.59193 -24.45001 -1.27614  1.000 88.03533  ? 209 LEU A O   1 
ATOM   3301 C CB  . LEU B 1 209 ? 10.68145 -22.72241 1.05943   1.000 78.38011  ? 209 LEU A CB  1 
ATOM   3302 C CG  . LEU B 1 209 ? 10.88266 -22.00544 2.39064   1.000 79.40622  ? 209 LEU A CG  1 
ATOM   3303 C CD1 . LEU B 1 209 ? 10.04936 -20.73678 2.44027   1.000 76.97414  ? 209 LEU A CD1 1 
ATOM   3304 C CD2 . LEU B 1 209 ? 10.55094 -22.92682 3.55275   1.000 80.38316  ? 209 LEU A CD2 1 
ATOM   3305 N N   . GLU B 1 210 ? 12.83625 -24.28166 -1.23511  1.000 77.28099  ? 210 GLU A N   1 
ATOM   3306 C CA  . GLU B 1 210 ? 13.12236 -24.62476 -2.62228  1.000 80.95225  ? 210 GLU A CA  1 
ATOM   3307 C C   . GLU B 1 210 ? 14.63727 -24.53106 -2.73774  1.000 85.83734  ? 210 GLU A C   1 
ATOM   3308 O O   . GLU B 1 210 ? 15.30789 -24.03186 -1.82872  1.000 85.18250  ? 210 GLU A O   1 
ATOM   3309 C CB  . GLU B 1 210 ? 12.41784 -23.70690 -3.63316  1.000 77.08515  ? 210 GLU A CB  1 
ATOM   3310 N N   . ASP B 1 211 ? 15.17483 -25.03051 -3.84480  1.000 83.25206  ? 211 ASP A N   1 
ATOM   3311 C CA  . ASP B 1 211 ? 16.61398 -25.05722 -4.04671  1.000 80.56765  ? 211 ASP A CA  1 
ATOM   3312 C C   . ASP B 1 211 ? 17.00514 -24.15290 -5.21047  1.000 84.00011  ? 211 ASP A C   1 
ATOM   3313 O O   . ASP B 1 211 ? 16.21519 -23.91188 -6.12838  1.000 85.37354  ? 211 ASP A O   1 
ATOM   3314 C CB  . ASP B 1 211 ? 17.10472 -26.48637 -4.29898  1.000 84.96365  ? 211 ASP A CB  1 
ATOM   3315 N N   . ALA B 1 212 ? 18.23153 -23.65101 -5.16114  1.000 83.53145  ? 212 ALA A N   1 
ATOM   3316 C CA  . ALA B 1 212 ? 18.73104 -22.77772 -6.21675  1.000 85.85515  ? 212 ALA A CA  1 
ATOM   3317 C C   . ALA B 1 212 ? 18.86271 -23.55551 -7.51816  1.000 87.26885  ? 212 ALA A C   1 
ATOM   3318 O O   . ALA B 1 212 ? 19.60275 -24.54702 -7.56027  1.000 87.40100  ? 212 ALA A O   1 
ATOM   3319 C CB  . ALA B 1 212 ? 20.07885 -22.18014 -5.82217  1.000 82.34947  ? 212 ALA A CB  1 
ATOM   3320 N N   . PRO B 1 213 ? 18.18170 -23.15341 -8.59194  1.000 87.33451  ? 213 PRO A N   1 
ATOM   3321 C CA  . PRO B 1 213 ? 18.33154 -23.84855 -9.87669  1.000 88.11064  ? 213 PRO A CA  1 
ATOM   3322 C C   . PRO B 1 213 ? 19.75940 -23.76924 -10.39448 1.000 93.32351  ? 213 PRO A C   1 
ATOM   3323 O O   . PRO B 1 213 ? 20.62696 -23.09596 -9.83353  1.000 93.83216  ? 213 PRO A O   1 
ATOM   3324 C CB  . PRO B 1 213 ? 17.36268 -23.10900 -10.80777 1.000 88.11732  ? 213 PRO A CB  1 
ATOM   3325 C CG  . PRO B 1 213 ? 16.44369 -22.35201 -9.90002  1.000 88.47980  ? 213 PRO A CG  1 
ATOM   3326 C CD  . PRO B 1 213 ? 17.24414 -22.02317 -8.68044  1.000 86.15279  ? 213 PRO A CD  1 
ATOM   3327 N N   . SER B 1 214 ? 19.99829 -24.48075 -11.49454 1.000 95.56449  ? 214 SER A N   1 
ATOM   3328 C CA  . SER B 1 214 ? 21.29971 -24.46808 -12.14298 1.000 98.34981  ? 214 SER A CA  1 
ATOM   3329 C C   . SER B 1 214 ? 21.41816 -23.26841 -13.08133 1.000 101.21797 ? 214 SER A C   1 
ATOM   3330 O O   . SER B 1 214 ? 20.45018 -22.54577 -13.33860 1.000 101.49561 ? 214 SER A O   1 
ATOM   3331 C CB  . SER B 1 214 ? 21.52671 -25.76689 -12.91594 1.000 99.66623  ? 214 SER A CB  1 
ATOM   3332 O OG  . SER B 1 214 ? 21.62542 -26.87536 -12.03741 1.000 103.21430 ? 214 SER A OG  1 
ATOM   3333 N N   . GLU B 1 215 ? 22.63523 -23.05356 -13.59297 1.000 103.70564 ? 215 GLU A N   1 
ATOM   3334 C CA  . GLU B 1 215 ? 22.83104 -22.01888 -14.60517 1.000 101.76117 ? 215 GLU A CA  1 
ATOM   3335 C C   . GLU B 1 215 ? 22.01948 -22.33086 -15.85685 1.000 103.66628 ? 215 GLU A C   1 
ATOM   3336 O O   . GLU B 1 215 ? 21.35529 -21.44893 -16.41694 1.000 102.56221 ? 215 GLU A O   1 
ATOM   3337 C CB  . GLU B 1 215 ? 24.31691 -21.88280 -14.94203 1.000 97.54098  ? 215 GLU A CB  1 
ATOM   3338 N N   . GLU B 1 216 ? 22.04169 -23.58913 -16.29475 1.000 105.35681 ? 216 GLU A N   1 
ATOM   3339 C CA  . GLU B 1 216 ? 21.23946 -24.05674 -17.41667 1.000 105.64095 ? 216 GLU A CA  1 
ATOM   3340 C C   . GLU B 1 216 ? 19.81918 -24.43737 -17.00456 1.000 102.76575 ? 216 GLU A C   1 
ATOM   3341 O O   . GLU B 1 216 ? 19.07792 -24.99938 -17.81826 1.000 101.04808 ? 216 GLU A O   1 
ATOM   3342 C CB  . GLU B 1 216 ? 21.92383 -25.25126 -18.09118 1.000 104.28969 ? 216 GLU A CB  1 
ATOM   3343 N N   . GLU B 1 217 ? 19.42117 -24.14364 -15.76310 1.000 98.75463  ? 217 GLU A N   1 
ATOM   3344 C CA  . GLU B 1 217 ? 18.09834 -24.51451 -15.27320 1.000 98.66573  ? 217 GLU A CA  1 
ATOM   3345 C C   . GLU B 1 217 ? 17.33820 -23.32296 -14.69964 1.000 97.28630  ? 217 GLU A C   1 
ATOM   3346 O O   . GLU B 1 217 ? 16.38883 -23.51677 -13.93224 1.000 96.18831  ? 217 GLU A O   1 
ATOM   3347 C CB  . GLU B 1 217 ? 18.20478 -25.62334 -14.22131 1.000 97.38022  ? 217 GLU A CB  1 
ATOM   3348 N N   . CYS B 1 218 ? 17.72997 -22.09711 -15.04605 1.000 95.90930  ? 218 CYS A N   1 
ATOM   3349 C CA  . CYS B 1 218 ? 17.07498 -20.91076 -14.51285 1.000 92.19152  ? 218 CYS A CA  1 
ATOM   3350 C C   . CYS B 1 218 ? 16.93516 -19.87177 -15.61574 1.000 86.51683  ? 218 CYS A C   1 
ATOM   3351 O O   . CYS B 1 218 ? 17.71001 -19.86670 -16.57645 1.000 87.02810  ? 218 CYS A O   1 
ATOM   3352 C CB  . CYS B 1 218 ? 17.85255 -20.33421 -13.31456 1.000 89.50122  ? 218 CYS A CB  1 
ATOM   3353 S SG  . CYS B 1 218 ? 19.37823 -19.49324 -13.73125 1.000 94.15355  ? 218 CYS A SG  1 
ATOM   3354 N N   . ASP B 1 219 ? 15.92267 -19.00828 -15.48123 1.000 84.04620  ? 219 ASP A N   1 
ATOM   3355 C CA  . ASP B 1 219 ? 15.70460 -17.91904 -16.42419 1.000 81.01291  ? 219 ASP A CA  1 
ATOM   3356 C C   . ASP B 1 219 ? 16.97764 -17.09318 -16.55078 1.000 77.74586  ? 219 ASP A C   1 
ATOM   3357 O O   . ASP B 1 219 ? 17.46231 -16.55399 -15.54343 1.000 79.03622  ? 219 ASP A O   1 
ATOM   3358 C CB  . ASP B 1 219 ? 14.54314 -17.02997 -15.97478 1.000 74.99390  ? 219 ASP A CB  1 
ATOM   3359 N N   . PRO B 1 220 ? 17.56219 -16.97551 -17.74422 1.000 76.21305  ? 220 PRO A N   1 
ATOM   3360 C CA  . PRO B 1 220 ? 18.84376 -16.25866 -17.86433 1.000 73.93924  ? 220 PRO A CA  1 
ATOM   3361 C C   . PRO B 1 220 ? 18.76201 -14.77561 -17.51814 1.000 74.46188  ? 220 PRO A C   1 
ATOM   3362 O O   . PRO B 1 220 ? 19.79665 -14.17377 -17.21200 1.000 75.57240  ? 220 PRO A O   1 
ATOM   3363 C CB  . PRO B 1 220 ? 19.24399 -16.47259 -19.32885 1.000 72.83903  ? 220 PRO A CB  1 
ATOM   3364 C CG  . PRO B 1 220 ? 17.98635 -16.89980 -20.04598 1.000 75.61323  ? 220 PRO A CG  1 
ATOM   3365 C CD  . PRO B 1 220 ? 16.94908 -17.30304 -19.04659 1.000 74.53509  ? 220 PRO A CD  1 
ATOM   3366 N N   . LEU B 1 221 ? 17.57234 -14.16712 -17.54551 1.000 76.61358  ? 221 LEU A N   1 
ATOM   3367 C CA  . LEU B 1 221 ? 17.44879 -12.76955 -17.14930 1.000 75.40920  ? 221 LEU A CA  1 
ATOM   3368 C C   . LEU B 1 221 ? 17.82642 -12.55175 -15.68859 1.000 78.30330  ? 221 LEU A C   1 
ATOM   3369 O O   . LEU B 1 221 ? 18.22222 -11.44173 -15.32216 1.000 81.52437  ? 221 LEU A O   1 
ATOM   3370 C CB  . LEU B 1 221 ? 16.02457 -12.26856 -17.40831 1.000 66.09915  ? 221 LEU A CB  1 
ATOM   3371 N N   . SER B 1 222 ? 17.72943 -13.58019 -14.84939 1.000 76.52060  ? 222 SER A N   1 
ATOM   3372 C CA  . SER B 1 222 ? 18.07642 -13.45071 -13.43864 1.000 75.07538  ? 222 SER A CA  1 
ATOM   3373 C C   . SER B 1 222 ? 19.57102 -13.57443 -13.17326 1.000 77.30051  ? 222 SER A C   1 
ATOM   3374 O O   . SER B 1 222 ? 19.98188 -13.50246 -12.00871 1.000 75.81167  ? 222 SER A O   1 
ATOM   3375 C CB  . SER B 1 222 ? 17.32233 -14.49955 -12.60964 1.000 76.61316  ? 222 SER A CB  1 
ATOM   3376 O OG  . SER B 1 222 ? 17.77536 -15.81710 -12.88871 1.000 76.34362  ? 222 SER A OG  1 
ATOM   3377 N N   . LEU B 1 223 ? 20.38962 -13.74312 -14.21407 1.000 81.32339  ? 223 LEU A N   1 
ATOM   3378 C CA  . LEU B 1 223 ? 21.79539 -14.08125 -14.04977 1.000 75.07019  ? 223 LEU A CA  1 
ATOM   3379 C C   . LEU B 1 223 ? 22.65314 -12.85257 -14.30494 1.000 81.00524  ? 223 LEU A C   1 
ATOM   3380 O O   . LEU B 1 223 ? 22.69633 -12.37015 -15.44864 1.000 83.78761  ? 223 LEU A O   1 
ATOM   3381 C CB  . LEU B 1 223 ? 22.18124 -15.20845 -15.00606 1.000 70.44821  ? 223 LEU A CB  1 
ATOM   3382 N N   . PRO B 1 224 ? 23.36539 -12.31852 -13.29269 1.000 80.79258  ? 224 PRO A N   1 
ATOM   3383 C CA  . PRO B 1 224 ? 24.19938 -11.10944 -13.33584 1.000 75.19271  ? 224 PRO A CA  1 
ATOM   3384 C C   . PRO B 1 224 ? 25.24341 -11.14061 -14.44307 1.000 78.19620  ? 224 PRO A C   1 
ATOM   3385 O O   . PRO B 1 224 ? 25.08355 -10.44023 -15.44344 1.000 78.15538  ? 224 PRO A O   1 
ATOM   3386 C CB  . PRO B 1 224 ? 24.87428 -11.10351 -11.96476 1.000 71.45075  ? 224 PRO A CB  1 
HETATM 3387 O O   . HOH C 2 .   ? 23.12162 6.17737   13.65634  1.000 42.13084  ? 301 HOH B O   1 
HETATM 3388 O O   . HOH C 2 .   ? 28.59164 21.71149  5.19640   1.000 43.73891  ? 302 HOH B O   1 
HETATM 3389 O O   . HOH C 2 .   ? 19.67171 29.26894  16.93332  1.000 57.78549  ? 303 HOH B O   1 
HETATM 3390 O O   . HOH C 2 .   ? 34.15556 0.02109   -2.42193  1.000 50.19914  ? 304 HOH B O   1 
HETATM 3391 O O   . HOH C 2 .   ? 12.57498 -8.22795  6.44040   1.000 55.19807  ? 305 HOH B O   1 
HETATM 3392 O O   . HOH C 2 .   ? 28.29415 8.95725   16.57865  1.000 41.09062  ? 306 HOH B O   1 
HETATM 3393 O O   . HOH C 2 .   ? 33.46162 -2.79281  -7.16992  1.000 60.73097  ? 307 HOH B O   1 
HETATM 3394 O O   . HOH C 2 .   ? 36.18504 9.49828   1.81215   1.000 46.99900  ? 308 HOH B O   1 
HETATM 3395 O O   . HOH C 2 .   ? 30.42492 22.36200  19.58072  1.000 52.00600  ? 309 HOH B O   1 
HETATM 3396 O O   . HOH C 2 .   ? 31.30533 17.66739  24.72554  1.000 57.50620  ? 310 HOH B O   1 
HETATM 3397 O O   . HOH C 2 .   ? 25.39353 3.73856   12.42327  1.000 37.87107  ? 311 HOH B O   1 
HETATM 3398 O O   . HOH C 2 .   ? 34.98218 -8.56642  22.57904  1.000 58.59275  ? 312 HOH B O   1 
HETATM 3399 O O   . HOH C 2 .   ? 23.44855 -0.99068  -1.02418  1.000 43.43218  ? 313 HOH B O   1 
HETATM 3400 O O   . HOH C 2 .   ? 24.17387 17.08698  -0.93318  1.000 39.40055  ? 314 HOH B O   1 
HETATM 3401 O O   . HOH C 2 .   ? 28.61856 16.04553  -12.21712 1.000 49.49207  ? 315 HOH B O   1 
HETATM 3402 O O   . HOH C 2 .   ? 32.14026 21.14403  5.33659   1.000 46.28533  ? 316 HOH B O   1 
HETATM 3403 O O   . HOH C 2 .   ? 30.12279 13.97925  20.86633  1.000 59.67796  ? 317 HOH B O   1 
HETATM 3404 O O   . HOH C 2 .   ? 29.72195 5.83633   -1.55539  1.000 40.27813  ? 318 HOH B O   1 
HETATM 3405 O O   . HOH C 2 .   ? 19.51323 26.18265  18.09173  1.000 66.51118  ? 319 HOH B O   1 
HETATM 3406 O O   . HOH C 2 .   ? 38.92239 -6.71096  13.44277  1.000 55.33380  ? 320 HOH B O   1 
HETATM 3407 O O   . HOH C 2 .   ? 44.39356 16.22366  7.14769   1.000 56.56377  ? 321 HOH B O   1 
HETATM 3408 O O   . HOH C 2 .   ? 30.32103 -6.02214  -2.31522  1.000 49.49056  ? 322 HOH B O   1 
HETATM 3409 O O   . HOH C 2 .   ? 30.50772 5.94107   -5.17156  1.000 41.46863  ? 323 HOH B O   1 
HETATM 3410 O O   . HOH C 2 .   ? 41.16102 -6.83592  13.29222  1.000 55.58182  ? 324 HOH B O   1 
HETATM 3411 O O   . HOH C 2 .   ? 21.36192 16.97317  -3.28669  1.000 32.01775  ? 325 HOH B O   1 
HETATM 3412 O O   . HOH C 2 .   ? 41.32090 3.74287   0.59920   1.000 57.71662  ? 326 HOH B O   1 
HETATM 3413 O O   . HOH C 2 .   ? 31.89579 23.49218  10.41712  1.000 44.42721  ? 327 HOH B O   1 
HETATM 3414 O O   . HOH C 2 .   ? 23.78970 2.54967   -2.57342  1.000 42.29784  ? 328 HOH B O   1 
HETATM 3415 O O   . HOH C 2 .   ? 29.51154 23.53760  7.82783   1.000 46.81889  ? 329 HOH B O   1 
HETATM 3416 O O   . HOH C 2 .   ? 33.61731 24.29915  19.86788  1.000 62.61202  ? 330 HOH B O   1 
HETATM 3417 O O   . HOH C 2 .   ? 23.14910 7.10457   15.70573  1.000 42.13084  ? 331 HOH B O   1 
HETATM 3418 O O   . HOH C 2 .   ? 26.70253 1.97278   14.18206  1.000 46.14614  ? 332 HOH B O   1 
HETATM 3419 O O   . HOH C 2 .   ? 44.30575 -3.80607  15.28493  1.000 58.38149  ? 333 HOH B O   1 
HETATM 3420 O O   . HOH C 2 .   ? 31.74057 9.25889   22.78285  1.000 58.34307  ? 334 HOH B O   1 
HETATM 3421 O O   . HOH C 2 .   ? 41.20712 -8.89911  -2.38244  1.000 70.97166  ? 335 HOH B O   1 
HETATM 3422 O O   . HOH C 2 .   ? 21.95412 11.85441  16.93781  1.000 47.77360  ? 336 HOH B O   1 
HETATM 3423 O O   . HOH C 2 .   ? 28.19655 -10.84809 30.19239  1.000 44.77013  ? 337 HOH B O   1 
HETATM 3424 O O   . HOH C 2 .   ? 20.09863 11.93787  6.20436   1.000 43.72712  ? 338 HOH B O   1 
HETATM 3425 O O   . HOH C 2 .   ? 22.12672 7.67540   19.15708  1.000 51.49706  ? 339 HOH B O   1 
HETATM 3426 O O   . HOH C 2 .   ? 33.74298 -10.83136 11.47019  1.000 64.30030  ? 340 HOH B O   1 
HETATM 3427 O O   . HOH C 2 .   ? 40.36523 5.18660   20.12964  1.000 56.36204  ? 341 HOH B O   1 
HETATM 3428 O O   . HOH C 2 .   ? 38.78164 23.19200  12.93035  1.000 32.01775  ? 342 HOH B O   1 
HETATM 3429 O O   . HOH C 2 .   ? 18.65445 25.53438  10.81318  1.000 42.13084  ? 343 HOH B O   1 
HETATM 3430 O O   . HOH C 2 .   ? 38.78022 4.44969   -0.25190  1.000 65.43370  ? 344 HOH B O   1 
HETATM 3431 O O   . HOH C 2 .   ? 34.22496 28.95156  -9.78514  1.000 56.42675  ? 345 HOH B O   1 
HETATM 3432 O O   . HOH C 2 .   ? 26.84736 8.50842   -4.19890  1.000 42.13084  ? 346 HOH B O   1 
HETATM 3433 O O   . HOH C 2 .   ? 25.23822 8.05485   -1.87588  1.000 44.40114  ? 347 HOH B O   1 
HETATM 3434 O O   . HOH C 2 .   ? 27.15053 9.53075   -5.75584  1.000 52.28362  ? 348 HOH B O   1 
HETATM 3435 O O   . HOH C 2 .   ? 32.82980 -4.95798  -7.02007  1.000 70.93055  ? 349 HOH B O   1 
HETATM 3436 O O   . HOH C 2 .   ? 18.06413 -16.54122 15.89545  1.000 69.18343  ? 350 HOH B O   1 
HETATM 3437 O O   . HOH C 2 .   ? 19.92007 11.32857  15.92838  1.000 52.18052  ? 351 HOH B O   1 
HETATM 3438 O O   . HOH C 2 .   ? 19.64494 -0.66601  18.53208  1.000 61.62713  ? 352 HOH B O   1 
HETATM 3439 O O   . HOH C 2 .   ? 22.08401 -1.45702  19.12441  1.000 59.19567  ? 353 HOH B O   1 
HETATM 3440 O O   . HOH C 2 .   ? 20.57170 6.94982   13.98814  1.000 42.13084  ? 354 HOH B O   1 
HETATM 3441 O O   . HOH C 2 .   ? 18.93914 -16.43461 17.70322  1.000 61.00943  ? 355 HOH B O   1 
HETATM 3442 O O   . HOH D 2 .   ? 17.61256 22.68777  -11.49928 1.000 48.62922  ? 301 HOH A O   1 
HETATM 3443 O O   . HOH D 2 .   ? 24.09494 -11.37511 -17.12646 1.000 64.71249  ? 302 HOH A O   1 
HETATM 3444 O O   . HOH D 2 .   ? -2.85636 -6.40007  4.56478   1.000 69.37992  ? 303 HOH A O   1 
HETATM 3445 O O   . HOH D 2 .   ? 15.21249 17.20464  1.95522   1.000 42.86490  ? 304 HOH A O   1 
HETATM 3446 O O   . HOH D 2 .   ? 15.31977 0.29341   -6.39114  1.000 37.97500  ? 305 HOH A O   1 
HETATM 3447 O O   . HOH D 2 .   ? -2.53583 -8.63588  4.25186   1.000 74.97707  ? 306 HOH A O   1 
HETATM 3448 O O   . HOH D 2 .   ? 12.03182 3.87958   -11.53100 1.000 39.54995  ? 307 HOH A O   1 
HETATM 3449 O O   . HOH D 2 .   ? 11.09619 19.73423  12.71149  1.000 49.39654  ? 308 HOH A O   1 
HETATM 3450 O O   . HOH D 2 .   ? 9.74303  6.78229   -17.33969 1.000 40.85438  ? 309 HOH A O   1 
HETATM 3451 O O   . HOH D 2 .   ? 9.81774  12.01657  -17.15982 1.000 35.92948  ? 310 HOH A O   1 
HETATM 3452 O O   . HOH D 2 .   ? 18.55057 17.97066  4.25399   1.000 35.89829  ? 311 HOH A O   1 
HETATM 3453 O O   . HOH D 2 .   ? 11.30602 19.85931  -4.83759  1.000 43.77599  ? 312 HOH A O   1 
HETATM 3454 O O   . HOH D 2 .   ? 11.70494 2.16218   -24.50841 1.000 50.47727  ? 313 HOH A O   1 
HETATM 3455 O O   . HOH D 2 .   ? 7.21176  -1.89187  -21.14405 1.000 55.24989  ? 314 HOH A O   1 
HETATM 3456 O O   . HOH D 2 .   ? 10.55366 6.70144   6.14954   1.000 41.33747  ? 315 HOH A O   1 
HETATM 3457 O O   . HOH D 2 .   ? 13.57870 -11.41219 1.30034   1.000 55.56392  ? 316 HOH A O   1 
HETATM 3458 O O   . HOH D 2 .   ? 9.69289  7.95620   9.65526   1.000 40.77602  ? 317 HOH A O   1 
HETATM 3459 O O   . HOH D 2 .   ? 9.49028  15.43118  -18.52324 1.000 42.81519  ? 318 HOH A O   1 
HETATM 3460 O O   . HOH D 2 .   ? 24.47831 -8.16556  3.40700   1.000 50.28116  ? 319 HOH A O   1 
HETATM 3461 O O   . HOH D 2 .   ? 3.79283  -14.12591 -14.13131 1.000 68.75785  ? 320 HOH A O   1 
HETATM 3462 O O   . HOH D 2 .   ? 18.27776 2.57652   -14.96012 1.000 56.19120  ? 321 HOH A O   1 
HETATM 3463 O O   . HOH D 2 .   ? 24.97249 -10.29079 -8.40704  1.000 56.32747  ? 322 HOH A O   1 
HETATM 3464 O O   . HOH D 2 .   ? 17.27217 0.25361   8.07459   1.000 35.18464  ? 323 HOH A O   1 
HETATM 3465 O O   . HOH D 2 .   ? 29.19511 10.30098  -16.87474 1.000 60.22717  ? 324 HOH A O   1 
HETATM 3466 O O   . HOH D 2 .   ? 2.63052  9.46468   -14.34032 1.000 51.15115  ? 325 HOH A O   1 
HETATM 3467 O O   . HOH D 2 .   ? 15.55860 11.13116  -23.33497 1.000 67.02827  ? 326 HOH A O   1 
HETATM 3468 O O   . HOH D 2 .   ? 16.61140 4.77152   8.46335   1.000 43.85544  ? 327 HOH A O   1 
HETATM 3469 O O   . HOH D 2 .   ? 17.24073 19.89869  3.73957   1.000 58.67411  ? 328 HOH A O   1 
HETATM 3470 O O   . HOH D 2 .   ? 21.95292 2.78065   -6.93546  1.000 53.43550  ? 329 HOH A O   1 
HETATM 3471 O O   . HOH D 2 .   ? 19.93530 10.37135  -2.64148  1.000 39.49637  ? 330 HOH A O   1 
HETATM 3472 O O   . HOH D 2 .   ? 12.30626 25.60700  1.84487   1.000 62.18784  ? 331 HOH A O   1 
HETATM 3473 O O   . HOH D 2 .   ? 20.41726 22.07661  -11.87764 1.000 45.77983  ? 332 HOH A O   1 
HETATM 3474 O O   . HOH D 2 .   ? 8.56655  2.20005   -18.06604 1.000 47.01005  ? 333 HOH A O   1 
HETATM 3475 O O   . HOH D 2 .   ? 10.08398 17.86331  -19.65050 1.000 45.99041  ? 334 HOH A O   1 
HETATM 3476 O O   . HOH D 2 .   ? 0.42491  6.80435   -12.56281 1.000 50.22149  ? 335 HOH A O   1 
HETATM 3477 O O   . HOH D 2 .   ? 17.98124 18.69560  -19.12530 1.000 60.80726  ? 336 HOH A O   1 
HETATM 3478 O O   . HOH D 2 .   ? 5.47392  20.60482  -8.15717  1.000 40.81690  ? 337 HOH A O   1 
HETATM 3479 O O   . HOH D 2 .   ? 20.16515 3.43598   -8.15831  1.000 36.26712  ? 338 HOH A O   1 
HETATM 3480 O O   . HOH D 2 .   ? 17.37133 2.15401   -17.25547 1.000 52.49152  ? 339 HOH A O   1 
HETATM 3481 O O   . HOH D 2 .   ? -1.559   11.471    8.402     1.000 53.07022  ? 340 HOH A O   1 
# 
