data_9EAT
# 
_entry.id   9EAT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EAT         pdb_00009eat 10.2210/pdb9eat/pdb 
WWPDB D_1000290041 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2025-01-29 
3 'Structure model' 1 2 2025-02-12 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 3 'Structure model' citation        
3 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EAT 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              janetsmith@umich.edu 
_pdbx_contact_author.name_first         Janet 
_pdbx_contact_author.name_last          Smith 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0664-9228 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rankin, M.R.' 1 0000-0002-0493-8907 
'Smith, J.L.'  2 0000-0002-0664-9228 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acta Crystallogr.,Sect.F' 
_citation.journal_id_ASTM           ACSFEN 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2053-230X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            81 
_citation.language                  ? 
_citation.page_first                47 
_citation.page_last                 52 
_citation.title                     'Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2053230X25000068 
_citation.pdbx_database_id_PubMed   39812168 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rankin, M.R.' 1 ? 
primary 'Smith, J.L.'  2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Carbonic anhydrase 2' 25130.779 1   4.2.1.1 ? ? Native 
2 non-polymer syn 'ZINC ION'             65.409    1   ?       ? ? ?      
3 water       nat water                  18.015    234 ?       ? ? ?      
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase 2' 
# 
_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       
;MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV
VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH
STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV
VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH
STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   ASP n 
1 4   ILE n 
1 5   ASP n 
1 6   THR n 
1 7   LEU n 
1 8   ILE n 
1 9   SER n 
1 10  ASN n 
1 11  ASN n 
1 12  ALA n 
1 13  LEU n 
1 14  TRP n 
1 15  SER n 
1 16  LYS n 
1 17  MET n 
1 18  LEU n 
1 19  VAL n 
1 20  GLU n 
1 21  GLU n 
1 22  ASP n 
1 23  PRO n 
1 24  GLY n 
1 25  PHE n 
1 26  PHE n 
1 27  GLU n 
1 28  LYS n 
1 29  LEU n 
1 30  ALA n 
1 31  GLN n 
1 32  ALA n 
1 33  GLN n 
1 34  LYS n 
1 35  PRO n 
1 36  ARG n 
1 37  PHE n 
1 38  LEU n 
1 39  TRP n 
1 40  ILE n 
1 41  GLY n 
1 42  CYS n 
1 43  SER n 
1 44  ASP n 
1 45  SER n 
1 46  ARG n 
1 47  VAL n 
1 48  PRO n 
1 49  ALA n 
1 50  GLU n 
1 51  ARG n 
1 52  LEU n 
1 53  THR n 
1 54  GLY n 
1 55  LEU n 
1 56  GLU n 
1 57  PRO n 
1 58  GLY n 
1 59  GLU n 
1 60  LEU n 
1 61  PHE n 
1 62  VAL n 
1 63  HIS n 
1 64  ARG n 
1 65  ASN n 
1 66  VAL n 
1 67  ALA n 
1 68  ASN n 
1 69  LEU n 
1 70  VAL n 
1 71  ILE n 
1 72  HIS n 
1 73  THR n 
1 74  ASP n 
1 75  LEU n 
1 76  ASN n 
1 77  CYS n 
1 78  LEU n 
1 79  SER n 
1 80  VAL n 
1 81  VAL n 
1 82  GLN n 
1 83  TYR n 
1 84  ALA n 
1 85  VAL n 
1 86  ASP n 
1 87  VAL n 
1 88  LEU n 
1 89  GLU n 
1 90  VAL n 
1 91  GLU n 
1 92  HIS n 
1 93  ILE n 
1 94  ILE n 
1 95  ILE n 
1 96  CYS n 
1 97  GLY n 
1 98  HIS n 
1 99  TYR n 
1 100 GLY n 
1 101 CYS n 
1 102 GLY n 
1 103 GLY n 
1 104 VAL n 
1 105 GLN n 
1 106 ALA n 
1 107 ALA n 
1 108 VAL n 
1 109 GLU n 
1 110 ASN n 
1 111 PRO n 
1 112 GLU n 
1 113 LEU n 
1 114 GLY n 
1 115 LEU n 
1 116 ILE n 
1 117 ASN n 
1 118 ASN n 
1 119 TRP n 
1 120 LEU n 
1 121 LEU n 
1 122 HIS n 
1 123 ILE n 
1 124 ARG n 
1 125 ASP n 
1 126 ILE n 
1 127 TRP n 
1 128 PHE n 
1 129 LYS n 
1 130 HIS n 
1 131 SER n 
1 132 SER n 
1 133 LEU n 
1 134 LEU n 
1 135 GLY n 
1 136 GLU n 
1 137 MET n 
1 138 PRO n 
1 139 GLN n 
1 140 GLU n 
1 141 ARG n 
1 142 ARG n 
1 143 LEU n 
1 144 ASP n 
1 145 THR n 
1 146 LEU n 
1 147 CYS n 
1 148 GLU n 
1 149 LEU n 
1 150 ASN n 
1 151 VAL n 
1 152 MET n 
1 153 GLU n 
1 154 GLN n 
1 155 VAL n 
1 156 TYR n 
1 157 ASN n 
1 158 LEU n 
1 159 GLY n 
1 160 HIS n 
1 161 SER n 
1 162 THR n 
1 163 ILE n 
1 164 MET n 
1 165 GLN n 
1 166 SER n 
1 167 ALA n 
1 168 TRP n 
1 169 LYS n 
1 170 ARG n 
1 171 GLY n 
1 172 GLN n 
1 173 LYS n 
1 174 VAL n 
1 175 THR n 
1 176 ILE n 
1 177 HIS n 
1 178 GLY n 
1 179 TRP n 
1 180 ALA n 
1 181 TYR n 
1 182 GLY n 
1 183 ILE n 
1 184 HIS n 
1 185 ASP n 
1 186 GLY n 
1 187 LEU n 
1 188 LEU n 
1 189 ARG n 
1 190 ASP n 
1 191 LEU n 
1 192 ASP n 
1 193 VAL n 
1 194 THR n 
1 195 ALA n 
1 196 THR n 
1 197 ASN n 
1 198 ARG n 
1 199 GLU n 
1 200 THR n 
1 201 LEU n 
1 202 GLU n 
1 203 GLN n 
1 204 ARG n 
1 205 TYR n 
1 206 ARG n 
1 207 HIS n 
1 208 GLY n 
1 209 ILE n 
1 210 SER n 
1 211 ASN n 
1 212 LEU n 
1 213 LYS n 
1 214 LEU n 
1 215 LYS n 
1 216 HIS n 
1 217 ALA n 
1 218 ASN n 
1 219 HIS n 
1 220 LYS n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           220 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Escherichia coli BL21(DE3)' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      469008 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
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 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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   ?   ?   ?   A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  ASN 10  10  10  ASN ASN A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  GLN 33  33  33  GLN GLN A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  TRP 39  39  39  TRP TRP A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  CYS 42  42  42  CYS CYS A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  ARG 46  46  46  ARG ARG A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  HIS 72  72  72  HIS HIS A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  CYS 96  96  96  CYS CYS A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 GLN 105 105 105 GLN GLN A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 TRP 119 119 119 TRP TRP A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 TRP 127 127 127 TRP TRP A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 GLN 139 139 139 GLN GLN A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 ARG 142 142 142 ARG ARG A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 CYS 147 147 147 CYS CYS A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 HIS 160 160 160 HIS HIS A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 MET 164 164 164 MET MET A . n 
A 1 165 GLN 165 165 165 GLN GLN A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 TRP 168 168 168 TRP TRP A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 HIS 177 177 177 HIS HIS A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 TRP 179 179 179 TRP TRP A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ARG 189 189 189 ARG ARG A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 THR 200 200 200 THR THR A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 GLN 203 203 203 GLN GLN A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 TYR 205 205 205 TYR TYR A . n 
A 1 206 ARG 206 206 206 ARG ARG A . n 
A 1 207 HIS 207 207 207 HIS HIS A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 LEU 214 214 ?   ?   ?   A . n 
A 1 215 LYS 215 215 ?   ?   ?   A . n 
A 1 216 HIS 216 216 ?   ?   ?   A . n 
A 1 217 ALA 217 217 ?   ?   ?   A . n 
A 1 218 ASN 218 218 ?   ?   ?   A . n 
A 1 219 HIS 219 219 ?   ?   ?   A . n 
A 1 220 LYS 220 220 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 HOH 1   401 113 HOH HOH A . 
C 3 HOH 2   402 197 HOH HOH A . 
C 3 HOH 3   403 213 HOH HOH A . 
C 3 HOH 4   404 191 HOH HOH A . 
C 3 HOH 5   405 238 HOH HOH A . 
C 3 HOH 6   406 116 HOH HOH A . 
C 3 HOH 7   407 96  HOH HOH A . 
C 3 HOH 8   408 180 HOH HOH A . 
C 3 HOH 9   409 206 HOH HOH A . 
C 3 HOH 10  410 18  HOH HOH A . 
C 3 HOH 11  411 132 HOH HOH A . 
C 3 HOH 12  412 79  HOH HOH A . 
C 3 HOH 13  413 14  HOH HOH A . 
C 3 HOH 14  414 62  HOH HOH A . 
C 3 HOH 15  415 196 HOH HOH A . 
C 3 HOH 16  416 85  HOH HOH A . 
C 3 HOH 17  417 90  HOH HOH A . 
C 3 HOH 18  418 149 HOH HOH A . 
C 3 HOH 19  419 161 HOH HOH A . 
C 3 HOH 20  420 187 HOH HOH A . 
C 3 HOH 21  421 60  HOH HOH A . 
C 3 HOH 22  422 40  HOH HOH A . 
C 3 HOH 23  423 237 HOH HOH A . 
C 3 HOH 24  424 173 HOH HOH A . 
C 3 HOH 25  425 24  HOH HOH A . 
C 3 HOH 26  426 3   HOH HOH A . 
C 3 HOH 27  427 72  HOH HOH A . 
C 3 HOH 28  428 15  HOH HOH A . 
C 3 HOH 29  429 195 HOH HOH A . 
C 3 HOH 30  430 94  HOH HOH A . 
C 3 HOH 31  431 107 HOH HOH A . 
C 3 HOH 32  432 230 HOH HOH A . 
C 3 HOH 33  433 2   HOH HOH A . 
C 3 HOH 34  434 42  HOH HOH A . 
C 3 HOH 35  435 30  HOH HOH A . 
C 3 HOH 36  436 71  HOH HOH A . 
C 3 HOH 37  437 158 HOH HOH A . 
C 3 HOH 38  438 178 HOH HOH A . 
C 3 HOH 39  439 32  HOH HOH A . 
C 3 HOH 40  440 159 HOH HOH A . 
C 3 HOH 41  441 47  HOH HOH A . 
C 3 HOH 42  442 154 HOH HOH A . 
C 3 HOH 43  443 234 HOH HOH A . 
C 3 HOH 44  444 140 HOH HOH A . 
C 3 HOH 45  445 157 HOH HOH A . 
C 3 HOH 46  446 201 HOH HOH A . 
C 3 HOH 47  447 22  HOH HOH A . 
C 3 HOH 48  448 69  HOH HOH A . 
C 3 HOH 49  449 17  HOH HOH A . 
C 3 HOH 50  450 73  HOH HOH A . 
C 3 HOH 51  451 74  HOH HOH A . 
C 3 HOH 52  452 214 HOH HOH A . 
C 3 HOH 53  453 93  HOH HOH A . 
C 3 HOH 54  454 41  HOH HOH A . 
C 3 HOH 55  455 46  HOH HOH A . 
C 3 HOH 56  456 136 HOH HOH A . 
C 3 HOH 57  457 53  HOH HOH A . 
C 3 HOH 58  458 203 HOH HOH A . 
C 3 HOH 59  459 64  HOH HOH A . 
C 3 HOH 60  460 8   HOH HOH A . 
C 3 HOH 61  461 152 HOH HOH A . 
C 3 HOH 62  462 45  HOH HOH A . 
C 3 HOH 63  463 20  HOH HOH A . 
C 3 HOH 64  464 35  HOH HOH A . 
C 3 HOH 65  465 186 HOH HOH A . 
C 3 HOH 66  466 51  HOH HOH A . 
C 3 HOH 67  467 91  HOH HOH A . 
C 3 HOH 68  468 33  HOH HOH A . 
C 3 HOH 69  469 55  HOH HOH A . 
C 3 HOH 70  470 5   HOH HOH A . 
C 3 HOH 71  471 59  HOH HOH A . 
C 3 HOH 72  472 106 HOH HOH A . 
C 3 HOH 73  473 129 HOH HOH A . 
C 3 HOH 74  474 43  HOH HOH A . 
C 3 HOH 75  475 34  HOH HOH A . 
C 3 HOH 76  476 26  HOH HOH A . 
C 3 HOH 77  477 6   HOH HOH A . 
C 3 HOH 78  478 148 HOH HOH A . 
C 3 HOH 79  479 98  HOH HOH A . 
C 3 HOH 80  480 65  HOH HOH A . 
C 3 HOH 81  481 142 HOH HOH A . 
C 3 HOH 82  482 111 HOH HOH A . 
C 3 HOH 83  483 54  HOH HOH A . 
C 3 HOH 84  484 57  HOH HOH A . 
C 3 HOH 85  485 137 HOH HOH A . 
C 3 HOH 86  486 13  HOH HOH A . 
C 3 HOH 87  487 199 HOH HOH A . 
C 3 HOH 88  488 37  HOH HOH A . 
C 3 HOH 89  489 23  HOH HOH A . 
C 3 HOH 90  490 77  HOH HOH A . 
C 3 HOH 91  491 7   HOH HOH A . 
C 3 HOH 92  492 31  HOH HOH A . 
C 3 HOH 93  493 126 HOH HOH A . 
C 3 HOH 94  494 110 HOH HOH A . 
C 3 HOH 95  495 108 HOH HOH A . 
C 3 HOH 96  496 9   HOH HOH A . 
C 3 HOH 97  497 86  HOH HOH A . 
C 3 HOH 98  498 16  HOH HOH A . 
C 3 HOH 99  499 109 HOH HOH A . 
C 3 HOH 100 500 233 HOH HOH A . 
C 3 HOH 101 501 204 HOH HOH A . 
C 3 HOH 102 502 68  HOH HOH A . 
C 3 HOH 103 503 160 HOH HOH A . 
C 3 HOH 104 504 151 HOH HOH A . 
C 3 HOH 105 505 89  HOH HOH A . 
C 3 HOH 106 506 58  HOH HOH A . 
C 3 HOH 107 507 184 HOH HOH A . 
C 3 HOH 108 508 210 HOH HOH A . 
C 3 HOH 109 509 229 HOH HOH A . 
C 3 HOH 110 510 82  HOH HOH A . 
C 3 HOH 111 511 38  HOH HOH A . 
C 3 HOH 112 512 219 HOH HOH A . 
C 3 HOH 113 513 147 HOH HOH A . 
C 3 HOH 114 514 21  HOH HOH A . 
C 3 HOH 115 515 29  HOH HOH A . 
C 3 HOH 116 516 61  HOH HOH A . 
C 3 HOH 117 517 44  HOH HOH A . 
C 3 HOH 118 518 48  HOH HOH A . 
C 3 HOH 119 519 25  HOH HOH A . 
C 3 HOH 120 520 70  HOH HOH A . 
C 3 HOH 121 521 194 HOH HOH A . 
C 3 HOH 122 522 134 HOH HOH A . 
C 3 HOH 123 523 95  HOH HOH A . 
C 3 HOH 124 524 50  HOH HOH A . 
C 3 HOH 125 525 133 HOH HOH A . 
C 3 HOH 126 526 100 HOH HOH A . 
C 3 HOH 127 527 80  HOH HOH A . 
C 3 HOH 128 528 39  HOH HOH A . 
C 3 HOH 129 529 67  HOH HOH A . 
C 3 HOH 130 530 83  HOH HOH A . 
C 3 HOH 131 531 169 HOH HOH A . 
C 3 HOH 132 532 52  HOH HOH A . 
C 3 HOH 133 533 27  HOH HOH A . 
C 3 HOH 134 534 223 HOH HOH A . 
C 3 HOH 135 535 66  HOH HOH A . 
C 3 HOH 136 536 103 HOH HOH A . 
C 3 HOH 137 537 235 HOH HOH A . 
C 3 HOH 138 538 12  HOH HOH A . 
C 3 HOH 139 539 4   HOH HOH A . 
C 3 HOH 140 540 19  HOH HOH A . 
C 3 HOH 141 541 78  HOH HOH A . 
C 3 HOH 142 542 224 HOH HOH A . 
C 3 HOH 143 543 175 HOH HOH A . 
C 3 HOH 144 544 63  HOH HOH A . 
C 3 HOH 145 545 28  HOH HOH A . 
C 3 HOH 146 546 102 HOH HOH A . 
C 3 HOH 147 547 125 HOH HOH A . 
C 3 HOH 148 548 216 HOH HOH A . 
C 3 HOH 149 549 101 HOH HOH A . 
C 3 HOH 150 550 81  HOH HOH A . 
C 3 HOH 151 551 165 HOH HOH A . 
C 3 HOH 152 552 56  HOH HOH A . 
C 3 HOH 153 553 11  HOH HOH A . 
C 3 HOH 154 554 84  HOH HOH A . 
C 3 HOH 155 555 124 HOH HOH A . 
C 3 HOH 156 556 167 HOH HOH A . 
C 3 HOH 157 557 10  HOH HOH A . 
C 3 HOH 158 558 130 HOH HOH A . 
C 3 HOH 159 559 112 HOH HOH A . 
C 3 HOH 160 560 150 HOH HOH A . 
C 3 HOH 161 561 1   HOH HOH A . 
C 3 HOH 162 562 88  HOH HOH A . 
C 3 HOH 163 563 189 HOH HOH A . 
C 3 HOH 164 564 87  HOH HOH A . 
C 3 HOH 165 565 76  HOH HOH A . 
C 3 HOH 166 566 198 HOH HOH A . 
C 3 HOH 167 567 118 HOH HOH A . 
C 3 HOH 168 568 99  HOH HOH A . 
C 3 HOH 169 569 192 HOH HOH A . 
C 3 HOH 170 570 220 HOH HOH A . 
C 3 HOH 171 571 105 HOH HOH A . 
C 3 HOH 172 572 190 HOH HOH A . 
C 3 HOH 173 573 139 HOH HOH A . 
C 3 HOH 174 574 183 HOH HOH A . 
C 3 HOH 175 575 218 HOH HOH A . 
C 3 HOH 176 576 135 HOH HOH A . 
C 3 HOH 177 577 131 HOH HOH A . 
C 3 HOH 178 578 212 HOH HOH A . 
C 3 HOH 179 579 145 HOH HOH A . 
C 3 HOH 180 580 122 HOH HOH A . 
C 3 HOH 181 581 236 HOH HOH A . 
C 3 HOH 182 582 207 HOH HOH A . 
C 3 HOH 183 583 166 HOH HOH A . 
C 3 HOH 184 584 117 HOH HOH A . 
C 3 HOH 185 585 120 HOH HOH A . 
C 3 HOH 186 586 92  HOH HOH A . 
C 3 HOH 187 587 227 HOH HOH A . 
C 3 HOH 188 588 168 HOH HOH A . 
C 3 HOH 189 589 121 HOH HOH A . 
C 3 HOH 190 590 239 HOH HOH A . 
C 3 HOH 191 591 128 HOH HOH A . 
C 3 HOH 192 592 138 HOH HOH A . 
C 3 HOH 193 593 222 HOH HOH A . 
C 3 HOH 194 594 104 HOH HOH A . 
C 3 HOH 195 595 181 HOH HOH A . 
C 3 HOH 196 596 200 HOH HOH A . 
C 3 HOH 197 597 127 HOH HOH A . 
C 3 HOH 198 598 97  HOH HOH A . 
C 3 HOH 199 599 75  HOH HOH A . 
C 3 HOH 200 600 49  HOH HOH A . 
C 3 HOH 201 601 205 HOH HOH A . 
C 3 HOH 202 602 114 HOH HOH A . 
C 3 HOH 203 603 143 HOH HOH A . 
C 3 HOH 204 604 146 HOH HOH A . 
C 3 HOH 205 605 162 HOH HOH A . 
C 3 HOH 206 606 179 HOH HOH A . 
C 3 HOH 207 607 241 HOH HOH A . 
C 3 HOH 208 608 211 HOH HOH A . 
C 3 HOH 209 609 172 HOH HOH A . 
C 3 HOH 210 610 153 HOH HOH A . 
C 3 HOH 211 611 119 HOH HOH A . 
C 3 HOH 212 612 209 HOH HOH A . 
C 3 HOH 213 613 115 HOH HOH A . 
C 3 HOH 214 614 193 HOH HOH A . 
C 3 HOH 215 615 164 HOH HOH A . 
C 3 HOH 216 616 123 HOH HOH A . 
C 3 HOH 217 617 228 HOH HOH A . 
C 3 HOH 218 618 174 HOH HOH A . 
C 3 HOH 219 619 177 HOH HOH A . 
C 3 HOH 220 620 171 HOH HOH A . 
C 3 HOH 221 621 144 HOH HOH A . 
C 3 HOH 222 622 188 HOH HOH A . 
C 3 HOH 223 623 170 HOH HOH A . 
C 3 HOH 224 624 242 HOH HOH A . 
C 3 HOH 225 625 141 HOH HOH A . 
C 3 HOH 226 626 36  HOH HOH A . 
C 3 HOH 227 627 185 HOH HOH A . 
C 3 HOH 228 628 240 HOH HOH A . 
C 3 HOH 229 629 156 HOH HOH A . 
C 3 HOH 230 630 182 HOH HOH A . 
C 3 HOH 231 631 155 HOH HOH A . 
C 3 HOH 232 632 163 HOH HOH A . 
C 3 HOH 233 633 226 HOH HOH A . 
C 3 HOH 234 634 217 HOH HOH A . 
# 
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                     9EAT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.524 
_cell.length_a_esd                 ? 
_cell.length_b                     67.524 
_cell.length_b_esd                 ? 
_cell.length_c                     85.076 
_cell.length_c_esd                 ? 
_cell.volume                       387903.220 
_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                         9EAT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            'P 4n 2n' 
_symmetry.space_group_name_H-M             'P 42 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EAT 
_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             1.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.25 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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    '100 mM HEPES pH 7.5, 200 mM lithium sulfate, 25% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-21 
_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                    'Double crystal cryo-cooled Si(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0332 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          14.77 
_reflns.entry_id                                       9EAT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.43 
_reflns.d_resolution_low                               47.77 
_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                                     69116 
_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                           99.48 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.41 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.1 
_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                                0.108 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.43 
_reflns_shell.d_res_low                                     1.48 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6625 
_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                               3.58 
_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                               1.106 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.415 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          95.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.01 
_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                                 9EAT 
_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                            1.43 
_refine.ls_d_res_low                             47.75 
_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                     69115 
_refine.ls_number_reflns_R_free                  3740 
_refine.ls_number_reflns_R_work                  65375 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.47 
_refine.ls_percent_reflns_R_free                 5.41 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1568 
_refine.ls_R_factor_R_free                       0.1674 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1562 
_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                          1.37 
_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                 16.2324 
_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                            0.1520 
_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                       1.43 
_refine_hist.d_res_low                        47.75 
_refine_hist.number_atoms_solvent             234 
_refine_hist.number_atoms_total               1933 
_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        1698 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_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' ? 0.0088  ? 1757 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0416  ? 2391 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0778  ? 269  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0067  ? 307  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.3979 ? 648  ? 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' 1.43 1.45  . . 133 2294 93.85  . . . . 0.3240 . . . . . . . . . . . 0.3504 
'X-RAY DIFFRACTION' 1.45 1.47  . . 136 2343 95.68  . . . . 0.3082 . . . . . . . . . . . 0.3041 
'X-RAY DIFFRACTION' 1.47 1.49  . . 135 2338 97.63  . . . . 0.2816 . . . . . . . . . . . 0.2977 
'X-RAY DIFFRACTION' 1.49 1.51  . . 133 2429 99.03  . . . . 0.2521 . . . . . . . . . . . 0.2429 
'X-RAY DIFFRACTION' 1.51 1.53  . . 139 2397 99.69  . . . . 0.2216 . . . . . . . . . . . 0.1813 
'X-RAY DIFFRACTION' 1.53 1.55  . . 135 2452 100.00 . . . . 0.1854 . . . . . . . . . . . 0.2187 
'X-RAY DIFFRACTION' 1.55 1.58  . . 141 2430 100.00 . . . . 0.1788 . . . . . . . . . . . 0.1915 
'X-RAY DIFFRACTION' 1.58 1.61  . . 142 2447 100.00 . . . . 0.1716 . . . . . . . . . . . 0.1714 
'X-RAY DIFFRACTION' 1.61 1.64  . . 143 2407 100.00 . . . . 0.1646 . . . . . . . . . . . 0.1806 
'X-RAY DIFFRACTION' 1.64 1.67  . . 139 2429 100.00 . . . . 0.1577 . . . . . . . . . . . 0.1801 
'X-RAY DIFFRACTION' 1.67 1.70  . . 139 2454 100.00 . . . . 0.1584 . . . . . . . . . . . 0.1887 
'X-RAY DIFFRACTION' 1.70 1.74  . . 134 2444 100.00 . . . . 0.1582 . . . . . . . . . . . 0.2165 
'X-RAY DIFFRACTION' 1.74 1.78  . . 143 2431 100.00 . . . . 0.1521 . . . . . . . . . . . 0.1698 
'X-RAY DIFFRACTION' 1.78 1.82  . . 137 2444 100.00 . . . . 0.1620 . . . . . . . . . . . 0.1548 
'X-RAY DIFFRACTION' 1.82 1.87  . . 140 2427 100.00 . . . . 0.1680 . . . . . . . . . . . 0.1875 
'X-RAY DIFFRACTION' 1.87 1.93  . . 143 2437 100.00 . . . . 0.1472 . . . . . . . . . . . 0.1573 
'X-RAY DIFFRACTION' 1.93 1.99  . . 134 2445 100.00 . . . . 0.1426 . . . . . . . . . . . 0.2102 
'X-RAY DIFFRACTION' 1.99 2.06  . . 141 2404 100.00 . . . . 0.1462 . . . . . . . . . . . 0.1924 
'X-RAY DIFFRACTION' 2.06 2.14  . . 139 2419 100.00 . . . . 0.1463 . . . . . . . . . . . 0.1563 
'X-RAY DIFFRACTION' 2.14 2.24  . . 139 2465 100.00 . . . . 0.1374 . . . . . . . . . . . 0.1706 
'X-RAY DIFFRACTION' 2.24 2.36  . . 135 2424 100.00 . . . . 0.1374 . . . . . . . . . . . 0.1462 
'X-RAY DIFFRACTION' 2.36 2.51  . . 140 2458 100.00 . . . . 0.1428 . . . . . . . . . . . 0.1609 
'X-RAY DIFFRACTION' 2.51 2.70  . . 142 2418 100.00 . . . . 0.1482 . . . . . . . . . . . 0.1586 
'X-RAY DIFFRACTION' 2.70 2.97  . . 140 2429 100.00 . . . . 0.1513 . . . . . . . . . . . 0.1501 
'X-RAY DIFFRACTION' 2.98 3.40  . . 144 2432 100.00 . . . . 0.1427 . . . . . . . . . . . 0.1274 
'X-RAY DIFFRACTION' 3.40 4.29  . . 139 2427 100.00 . . . . 0.1379 . . . . . . . . . . . 0.1430 
'X-RAY DIFFRACTION' 4.29 47.75 . . 135 2451 99.96  . . . . 0.1522 . . . . . . . . . . . 0.1602 
# 
_struct.entry_id                     9EAT 
_struct.title                        'High-Resolution Structure of Escherichia coli Carbonic Anhydrase 2 in Space Group P4(2)2(1)2' 
_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        9EAT 
_struct_keywords.text            'Zinc-dependent metalloenzyme, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAN_ECOLI 
_struct_ref.pdbx_db_accession          P61517 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV
VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH
STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EAT 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 220 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P61517 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  220 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       220 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 15550 ? 
1 MORE         -94   ? 
1 'SSA (A^2)'  33050 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z          1.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
1.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_665 -x+1,-y+1,z    -1.0000000000 0.0000000000  0.0000000000 67.5240000000 0.0000000000  
-1.0000000000 0.0000000000 67.5240000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
3 'crystal symmetry operation' 7_556 y,x,-z+1       0.0000000000  1.0000000000  0.0000000000 0.0000000000  1.0000000000  
0.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 -1.0000000000 85.0760000000 
4 'crystal symmetry operation' 8_666 -y+1,-x+1,-z+1 0.0000000000  -1.0000000000 0.0000000000 67.5240000000 -1.0000000000 
0.0000000000  0.0000000000 67.5240000000 0.0000000000 0.0000000000 -1.0000000000 85.0760000000 
# 
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 ASP A 3   ? ASP A 22  ? ASP A 3   ASP A 22  1 ? 20 
HELX_P HELX_P2  AA2 PHE A 26  ? GLN A 31  ? PHE A 26  GLN A 31  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 48  ? GLY A 54  ? PRO A 48  GLY A 54  1 ? 7  
HELX_P HELX_P4  AA4 ASP A 74  ? VAL A 87  ? ASP A 74  VAL A 87  1 ? 14 
HELX_P HELX_P5  AA5 CYS A 101 ? ASN A 110 ? CYS A 101 ASN A 110 1 ? 10 
HELX_P HELX_P6  AA6 LEU A 115 ? HIS A 130 ? LEU A 115 HIS A 130 1 ? 16 
HELX_P HELX_P7  AA7 HIS A 130 ? GLU A 136 ? HIS A 130 GLU A 136 1 ? 7  
HELX_P HELX_P8  AA8 MET A 137 ? GLU A 140 ? MET A 137 GLU A 140 5 ? 4  
HELX_P HELX_P9  AA9 ARG A 141 ? SER A 161 ? ARG A 141 SER A 161 1 ? 21 
HELX_P HELX_P10 AB1 SER A 161 ? ARG A 170 ? SER A 161 ARG A 170 1 ? 10 
HELX_P HELX_P11 AB2 ASN A 197 ? LYS A 213 ? ASN A 197 LYS A 213 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 42  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 42  A ZN 301 1_555 ? ? ? ? ? ? ? 2.236 ? ? 
metalc2 metalc ? ? A ASP 44  OD2 ? ? ? 1_555 B ZN . ZN ? ? A ASP 44  A ZN 301 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc3 metalc ? ? A HIS 98  NE2 ? ? ? 1_555 B ZN . ZN ? ? A HIS 98  A ZN 301 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc4 metalc ? ? A CYS 101 SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 101 A ZN 301 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG  ? A CYS 42 ? A CYS 42 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OD2 ? A ASP 44  ? A ASP 44  ? 1_555 104.8 ? 
2 SG  ? A CYS 42 ? A CYS 42 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 98  ? A HIS 98  ? 1_555 116.6 ? 
3 OD2 ? A ASP 44 ? A ASP 44 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 98  ? A HIS 98  ? 1_555 96.7  ? 
4 SG  ? A CYS 42 ? A CYS 42 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 101 ? A CYS 101 ? 1_555 116.1 ? 
5 OD2 ? A ASP 44 ? A ASP 44 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 101 ? A CYS 101 ? 1_555 114.1 ? 
6 NE2 ? A HIS 98 ? A HIS 98 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 101 ? A CYS 101 ? 1_555 107.2 ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 60  ? ASN A 65  ? LEU A 60  ASN A 65  
AA1 2 PHE A 37  ? CYS A 42  ? PHE A 37  CYS A 42  
AA1 3 HIS A 92  ? HIS A 98  ? HIS A 92  HIS A 98  
AA1 4 THR A 175 ? TYR A 181 ? THR A 175 TYR A 181 
AA1 5 ARG A 189 ? ASP A 190 ? ARG A 189 ASP A 190 
# 
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 PHE A 61  ? O PHE A 61  N PHE A 37  ? N PHE A 37  
AA1 2 3 N ILE A 40  ? N ILE A 40  O ILE A 94  ? O ILE A 94  
AA1 3 4 N ILE A 95  ? N ILE A 95  O TRP A 179 ? O TRP A 179 
AA1 4 5 N ALA A 180 ? N ALA A 180 O ARG A 189 ? O ARG A 189 
# 
_pdbx_entry_details.entry_id                   9EAT 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 A HOH 458 ? ? O A HOH 478 ? ? 2.15 
2 1 O A HOH 509 ? ? O A HOH 617 ? ? 2.18 
3 1 O A HOH 613 ? ? O A HOH 632 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 412 ? ? 1_555 O A HOH 412 ? ? 2_665 1.98 
2 1 O A HOH 493 ? ? 1_555 O A HOH 569 ? ? 2_665 2.13 
3 1 O A HOH 431 ? ? 1_555 O A HOH 585 ? ? 2_665 2.19 
# 
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 A 22  ? ? -154.15 71.54 
2 1 ASP A 185 ? ? -154.25 -4.71 
3 1 ASP A 192 ? ? 73.08   35.13 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 486 ? C HOH . 
2 1 A HOH 553 ? C HOH . 
3 1 A HOH 614 ? C HOH . 
4 1 A HOH 623 ? C HOH . 
5 1 A HOH 626 ? C HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/2  
3 y+1/2,-x+1/2,z+1/2  
4 x+1/2,-y+1/2,-z+1/2 
5 -x+1/2,y+1/2,-z+1/2 
6 -x,-y,z             
7 y,x,-z              
8 -y,-x,-z            
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A LEU 214 ? A LEU 214 
3 1 Y 1 A LYS 215 ? A LYS 215 
4 1 Y 1 A HIS 216 ? A HIS 216 
5 1 Y 1 A ALA 217 ? A ALA 217 
6 1 Y 1 A ASN 218 ? A ASN 218 
7 1 Y 1 A HIS 219 ? A HIS 219 
8 1 Y 1 A LYS 220 ? A LYS 220 
# 
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 
ZN  ZN   ZN N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)' 'United States' 
R01DK042303 1 
'National Institutes of Health/National Cancer Institute (NIH/NCI)'                                         'United States' 
F31CA265082 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1I6P 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 42 21 2' 
_space_group.name_Hall        'P 4n 2n' 
_space_group.IT_number        94 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EAT 
_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]   0.014810 
_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]   0.014810 
_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]   0.011754 
_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.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 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.
;
? 
ZN  ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 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   . LYS A 1 2   ? 43.17300 66.69400 37.85600 1.000 48.68078 ?  2   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 2   ? 43.72800 66.07900 36.65200 1.000 41.25575 ?  2   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 2   ? 42.65200 65.40300 35.80100 1.000 39.72334 ?  2   LYS A C   1 
ATOM   4    O  O   . LYS A 1 2   ? 41.67900 64.86400 36.32500 1.000 42.50170 ?  2   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 2   ? 44.83300 65.08400 37.00900 1.000 38.29497 ?  2   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 2   ? 46.04200 65.73800 37.64200 1.000 47.38485 ?  2   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 2   ? 47.10900 64.72700 37.97900 1.000 46.60301 ?  2   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 2   ? 48.28500 65.40700 38.65600 1.000 52.74610 ?  2   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 2   ? 48.92300 66.38100 37.74500 1.000 60.99226 ?  2   LYS A NZ  1 
ATOM   10   N  N   . ASP A 1 3   ? 42.82900 65.49700 34.47700 1.000 34.67998 ?  3   ASP A N   1 
ATOM   11   C  CA  . ASP A 1 3   ? 41.89900 64.89700 33.51800 1.000 33.67491 ?  3   ASP A CA  1 
ATOM   12   C  C   . ASP A 1 3   ? 42.60400 63.90100 32.61000 1.000 33.13008 ?  3   ASP A C   1 
ATOM   13   O  O   . ASP A 1 3   ? 43.80100 63.75100 32.70100 1.000 29.59204 ?  3   ASP A O   1 
ATOM   14   C  CB  . ASP A 1 3   ? 41.11900 65.94400 32.69200 1.000 37.83516 ?  3   ASP A CB  1 
ATOM   15   C  CG  . ASP A 1 3   ? 41.87900 66.41600 31.46600 1.000 49.28276 ?  3   ASP A CG  1 
ATOM   16   O  OD1 . ASP A 1 3   ? 43.11200 66.60600 31.55100 1.000 39.53869 ?  3   ASP A OD1 1 
ATOM   17   O  OD2 . ASP A 1 3   ? 41.23000 66.60200 30.41900 1.000 46.94061 -1 3   ASP A OD2 1 
ATOM   18   N  N   . ILE A 1 4   ? 41.86900 63.27600 31.70700 1.000 33.27398 ?  4   ILE A N   1 
ATOM   19   C  CA  . ILE A 1 4   ? 42.44500 62.17000 30.93300 1.000 27.48080 ?  4   ILE A CA  1 
ATOM   20   C  C   . ILE A 1 4   ? 43.54300 62.66100 29.99600 1.000 28.76300 ?  4   ILE A C   1 
ATOM   21   O  O   . ILE A 1 4   ? 44.61000 62.04300 29.88900 1.000 24.13864 ?  4   ILE A O   1 
ATOM   22   C  CB  . ILE A 1 4   ? 41.35600 61.38200 30.18300 1.000 26.06028 ?  4   ILE A CB  1 
ATOM   23   C  CG1 . ILE A 1 4   ? 40.76100 60.30600 31.09200 1.000 32.22571 ?  4   ILE A CG1 1 
ATOM   24   C  CG2 . ILE A 1 4   ? 41.92300 60.74700 28.92400 1.000 30.84701 ?  4   ILE A CG2 1 
ATOM   25   C  CD1 . ILE A 1 4   ? 41.71500 59.14800 31.38600 1.000 22.11125 ?  4   ILE A CD1 1 
ATOM   26   N  N   . ASP A 1 5   ? 43.29200 63.76300 29.28400 1.000 24.04587 ?  5   ASP A N   1 
ATOM   27   C  CA  . ASP A 1 5   ? 44.32000 64.29500 28.39200 1.000 27.53141 ?  5   ASP A CA  1 
ATOM   28   C  C   . ASP A 1 5   ? 45.58900 64.62100 29.15500 1.000 22.72439 ?  5   ASP A C   1 
ATOM   29   O  O   . ASP A 1 5   ? 46.69700 64.48000 28.61200 1.000 22.67548 ?  5   ASP A O   1 
ATOM   30   C  CB  . ASP A 1 5   ? 43.80600 65.54300 27.67000 1.000 31.89290 ?  5   ASP A CB  1 
ATOM   31   C  CG  . ASP A 1 5   ? 42.85000 65.20500 26.54200 1.000 42.49518 ?  5   ASP A CG  1 
ATOM   32   O  OD1 . ASP A 1 5   ? 42.92500 64.06600 26.02500 1.000 39.67278 ?  5   ASP A OD1 1 
ATOM   33   O  OD2 . ASP A 1 5   ? 42.03500 66.07800 26.16800 1.000 47.27916 -1 5   ASP A OD2 1 
ATOM   34   N  N   . THR A 1 6   ? 45.45200 65.05700 30.41000 1.000 21.76631 ?  6   THR A N   1 
ATOM   35   C  CA  . THR A 1 6   ? 46.62300 65.31100 31.22800 1.000 19.78353 ?  6   THR A CA  1 
ATOM   36   C  C   . THR A 1 6   ? 47.42600 64.03300 31.46800 1.000 18.72372 ?  6   THR A C   1 
ATOM   37   O  O   . THR A 1 6   ? 48.65900 64.05100 31.40300 1.000 17.44412 ?  6   THR A O   1 
ATOM   38   C  CB  . THR A 1 6   ? 46.21900 65.98300 32.54200 1.000 23.93335 ?  6   THR A CB  1 
ATOM   39   O  OG1 . THR A 1 6   ? 45.66600 67.27100 32.25200 1.000 29.30459 ?  6   THR A OG1 1 
ATOM   40   C  CG2 . THR A 1 6   ? 47.42200 66.17600 33.42500 1.000 24.51643 ?  6   THR A CG2 1 
ATOM   41   N  N   . LEU A 1 7   ? 46.75300 62.90700 31.73300 1.000 20.80619 ?  7   LEU A N   1 
ATOM   42   C  CA  . LEU A 1 7   ? 47.49000 61.67000 32.00200 1.000 18.43912 ?  7   LEU A CA  1 
ATOM   43   C  C   . LEU A 1 7   ? 48.27800 61.22300 30.78000 1.000 14.85642 ?  7   LEU A C   1 
ATOM   44   O  O   . LEU A 1 7   ? 49.43800 60.81900 30.89500 1.000 16.85924 ?  7   LEU A O   1 
ATOM   45   C  CB  . LEU A 1 7   ? 46.55000 60.55500 32.45000 1.000 17.31337 ?  7   LEU A CB  1 
ATOM   46   C  CG  . LEU A 1 7   ? 45.69300 60.87700 33.67500 1.000 20.59893 ?  7   LEU A CG  1 
ATOM   47   C  CD1 . LEU A 1 7   ? 45.09400 59.55600 34.17800 1.000 19.91949 ?  7   LEU A CD1 1 
ATOM   48   C  CD2 . LEU A 1 7   ? 46.49300 61.59100 34.75700 1.000 25.67574 ?  7   LEU A CD2 1 
ATOM   49   N  N   . ILE A 1 8   ? 47.64000 61.23200 29.60600 1.000 17.14422 ?  8   ILE A N   1 
ATOM   50   C  CA  . ILE A 1 8   ? 48.30700 60.80500 28.37500 1.000 18.07197 ?  8   ILE A CA  1 
ATOM   51   C  C   . ILE A 1 8   ? 49.49800 61.70400 28.07900 1.000 15.42106 ?  8   ILE A C   1 
ATOM   52   O  O   . ILE A 1 8   ? 50.59400 61.23100 27.74700 1.000 17.19412 ?  8   ILE A O   1 
ATOM   53   C  CB  . ILE A 1 8   ? 47.30400 60.79800 27.21000 1.000 19.08912 ?  8   ILE A CB  1 
ATOM   54   C  CG1 . ILE A 1 8   ? 46.31800 59.64200 27.37900 1.000 22.96463 ?  8   ILE A CG1 1 
ATOM   55   C  CG2 . ILE A 1 8   ? 48.03300 60.67800 25.85800 1.000 25.04417 ?  8   ILE A CG2 1 
ATOM   56   C  CD1 . ILE A 1 8   ? 46.94900 58.28700 27.12000 1.000 26.89109 ?  8   ILE A CD1 1 
ATOM   57   N  N   . SER A 1 9   ? 49.29300 63.01700 28.19700 1.000 15.42580 ?  9   SER A N   1 
ATOM   58   C  CA  . SER A 1 9   ? 50.35300 63.97000 27.90400 1.000 14.71440 ?  9   SER A CA  1 
ATOM   59   C  C   . SER A 1 9   ? 51.48300 63.85600 28.90900 1.000 16.16107 ?  9   SER A C   1 
ATOM   60   O  O   . SER A 1 9   ? 52.65900 63.82500 28.52300 1.000 15.13912 ?  9   SER A O   1 
ATOM   61   C  CB  . SER A 1 9   ? 49.76200 65.38100 27.89500 1.000 17.06654 ?  9   SER A CB  1 
ATOM   62   O  OG  . SER A 1 9   ? 50.75400 66.35400 27.58700 1.000 17.28783 ?  9   SER A OG  1 
ATOM   63   N  N   . ASN A 1 10  ? 51.15000 63.71700 30.19800 1.000 14.42001 ?  10  ASN A N   1 
ATOM   64   C  CA  . ASN A 1 10  ? 52.19300 63.53300 31.19700 1.000 13.85761 ?  10  ASN A CA  1 
ATOM   65   C  C   . ASN A 1 10  ? 52.99200 62.26900 30.92700 1.000 14.21185 ?  10  ASN A C   1 
ATOM   66   O  O   . ASN A 1 10  ? 54.21700 62.25000 31.10000 1.000 15.49220 ?  10  ASN A O   1 
ATOM   67   C  CB  . ASN A 1 10  ? 51.58900 63.44000 32.60800 1.000 15.28683 ?  10  ASN A CB  1 
ATOM   68   C  CG  . ASN A 1 10  ? 51.12800 64.76500 33.14200 1.000 21.87880 ?  10  ASN A CG  1 
ATOM   69   O  OD1 . ASN A 1 10  ? 51.45200 65.82000 32.60200 1.000 22.07887 ?  10  ASN A OD1 1 
ATOM   70   N  ND2 . ASN A 1 10  ? 50.38900 64.72000 34.24300 1.000 27.79538 ?  10  ASN A ND2 1 
ATOM   71   N  N   . ASN A 1 11  ? 52.31400 61.19600 30.51600 1.000 15.12583 ?  11  ASN A N   1 
ATOM   72   C  CA  . ASN A 1 11  ? 53.01200 59.94900 30.23700 1.000 14.79358 ?  11  ASN A CA  1 
ATOM   73   C  C   . ASN A 1 11  ? 54.00800 60.12100 29.10100 1.000 14.64352 ?  11  ASN A C   1 
ATOM   74   O  O   . ASN A 1 11  ? 55.14900 59.66100 29.20100 1.000 14.55519 ?  11  ASN A O   1 
ATOM   75   C  CB  . ASN A 1 11  ? 52.00500 58.84400 29.90600 1.000 13.81354 ?  11  ASN A CB  1 
ATOM   76   C  CG  . ASN A 1 11  ? 52.66600 57.62600 29.30700 1.000 14.51274 ?  11  ASN A CG  1 
ATOM   77   O  OD1 . ASN A 1 11  ? 52.62100 57.42900 28.09600 1.000 15.57952 ?  11  ASN A OD1 1 
ATOM   78   N  ND2 . ASN A 1 11  ? 53.30200 56.82600 30.14300 1.000 14.69843 ?  11  ASN A ND2 1 
ATOM   79   N  N   . ALA A 1 12  ? 53.59500 60.79800 28.02800 1.000 16.11170 ?  12  ALA A N   1 
ATOM   80   C  CA  . ALA A 1 12  ? 54.49500 60.99700 26.89700 1.000 17.49236 ?  12  ALA A CA  1 
ATOM   81   C  C   . ALA A 1 12  ? 55.72500 61.80800 27.31000 1.000 16.76629 ?  12  ALA A C   1 
ATOM   82   O  O   . ALA A 1 12  ? 56.86300 61.45100 26.96700 1.000 17.47187 ?  12  ALA A O   1 
ATOM   83   C  CB  . ALA A 1 12  ? 53.73200 61.65000 25.75000 1.000 16.89923 ?  12  ALA A CB  1 
ATOM   84   N  N   . LEU A 1 13  ? 55.52700 62.87300 28.09000 1.000 15.13024 ?  13  LEU A N   1 
ATOM   85   C  CA  . LEU A 1 13  ? 56.66200 63.66700 28.55300 1.000 16.35706 ?  13  LEU A CA  1 
ATOM   86   C  C   . LEU A 1 13  ? 57.55200 62.87500 29.50500 1.000 18.21301 ?  13  LEU A C   1 
ATOM   87   O  O   . LEU A 1 13  ? 58.78000 62.97400 29.44000 1.000 16.75494 ?  13  LEU A O   1 
ATOM   88   C  CB  . LEU A 1 13  ? 56.16300 64.97200 29.19500 1.000 17.07597 ?  13  LEU A CB  1 
ATOM   89   C  CG  . LEU A 1 13  ? 55.37600 65.84900 28.22900 1.000 21.60464 ?  13  LEU A CG  1 
ATOM   90   C  CD1 . LEU A 1 13  ? 54.76000 67.02900 28.98100 1.000 23.29244 ?  13  LEU A CD1 1 
ATOM   91   C  CD2 . LEU A 1 13  ? 56.25800 66.33400 27.06900 1.000 20.70420 ?  13  LEU A CD2 1 
ATOM   92   N  N   . TRP A 1 14  ? 56.95700 62.07700 30.39900 1.000 15.88920 ?  14  TRP A N   1 
ATOM   93   C  CA  . TRP A 1 14  ? 57.76300 61.29500 31.32900 1.000 17.13722 ?  14  TRP A CA  1 
ATOM   94   C  C   . TRP A 1 14  ? 58.61600 60.27300 30.58200 1.000 17.07422 ?  14  TRP A C   1 
ATOM   95   O  O   . TRP A 1 14  ? 59.80600 60.09400 30.88600 1.000 16.81135 ?  14  TRP A O   1 
ATOM   96   C  CB  . TRP A 1 14  ? 56.82000 60.61000 32.31600 1.000 16.81507 ?  14  TRP A CB  1 
ATOM   97   C  CG  . TRP A 1 14  ? 57.43600 59.47400 33.05600 1.000 17.06884 ?  14  TRP A CG  1 
ATOM   98   C  CD1 . TRP A 1 14  ? 58.26300 59.54700 34.15500 1.000 22.54295 ?  14  TRP A CD1 1 
ATOM   99   C  CD2 . TRP A 1 14  ? 57.29200 58.08500 32.75200 1.000 15.02302 ?  14  TRP A CD2 1 
ATOM   100  N  NE1 . TRP A 1 14  ? 58.62800 58.28200 34.54600 1.000 20.22608 ?  14  TRP A NE1 1 
ATOM   101  C  CE2 . TRP A 1 14  ? 58.04400 57.36500 33.71100 1.000 18.05606 ?  14  TRP A CE2 1 
ATOM   102  C  CE3 . TRP A 1 14  ? 56.58400 57.37800 31.77700 1.000 15.14192 ?  14  TRP A CE3 1 
ATOM   103  C  CZ2 . TRP A 1 14  ? 58.12200 55.96400 33.70800 1.000 19.64482 ?  14  TRP A CZ2 1 
ATOM   104  C  CZ3 . TRP A 1 14  ? 56.65500 55.97800 31.77700 1.000 18.00639 ?  14  TRP A CZ3 1 
ATOM   105  C  CH2 . TRP A 1 14  ? 57.42700 55.29400 32.74000 1.000 17.18015 ?  14  TRP A CH2 1 
ATOM   106  N  N   . SER A 1 15  ? 58.03500 59.63000 29.56800 1.000 15.04034 ?  15  SER A N   1 
ATOM   107  C  CA  . SER A 1 15  ? 58.78200 58.62900 28.80800 1.000 16.10548 ?  15  SER A CA  1 
ATOM   108  C  C   . SER A 1 15  ? 59.98300 59.24800 28.10300 1.000 17.15049 ?  15  SER A C   1 
ATOM   109  O  O   . SER A 1 15  ? 61.06600 58.64500 28.05800 1.000 18.94012 ?  15  SER A O   1 
ATOM   110  C  CB  . SER A 1 15  ? 57.85200 57.97500 27.78900 1.000 17.28880 ?  15  SER A CB  1 
ATOM   111  O  OG  . SER A 1 15  ? 58.55800 57.05500 26.95500 1.000 17.70928 ?  15  SER A OG  1 
ATOM   112  N  N   . LYS A 1 16  ? 59.80200 60.43900 27.52400 1.000 17.01851 ?  16  LYS A N   1 
ATOM   113  C  CA  . LYS A 1 16  ? 60.90400 61.11600 26.83300 1.000 16.21949 ?  16  LYS A CA  1 
ATOM   114  C  C   . LYS A 1 16  ? 61.97700 61.56000 27.81700 1.000 17.26781 ?  16  LYS A C   1 
ATOM   115  O  O   . LYS A 1 16  ? 63.17700 61.36800 27.57200 1.000 18.52944 ?  16  LYS A O   1 
ATOM   116  C  CB  . LYS A 1 16  ? 60.37500 62.32300 26.05900 1.000 16.20122 ?  16  LYS A CB  1 
ATOM   117  C  CG  . LYS A 1 16  ? 59.42900 61.97700 24.90500 1.000 17.37440 ?  16  LYS A CG  1 
ATOM   118  C  CD  . LYS A 1 16  ? 58.86700 63.25100 24.27200 1.000 23.40323 ?  16  LYS A CD  1 
ATOM   119  C  CE  . LYS A 1 16  ? 57.51900 62.99800 23.60000 1.000 25.70779 ?  16  LYS A CE  1 
ATOM   120  N  NZ  . LYS A 1 16  ? 57.63300 61.99200 22.53100 1.000 33.99665 ?  16  LYS A NZ  1 
ATOM   121  N  N   . MET A 1 17  ? 61.56500 62.13500 28.94800 1.000 17.51178 ?  17  MET A N   1 
ATOM   122  C  CA  . MET A 1 17  ? 62.52800 62.64300 29.92100 1.000 17.59648 ?  17  MET A CA  1 
ATOM   123  C  C   . MET A 1 17  ? 63.37200 61.54600 30.55300 1.000 21.33001 ?  17  MET A C   1 
ATOM   124  O  O   . MET A 1 17  ? 64.48600 61.82200 31.01900 1.000 21.13793 ?  17  MET A O   1 
ATOM   125  C  CB  . MET A 1 17  ? 61.79700 63.44700 30.98400 1.000 18.02801 ?  17  MET A CB  1 
ATOM   126  C  CG  . MET A 1 17  ? 61.40900 64.77900 30.44200 1.000 20.70112 ?  17  MET A CG  1 
ATOM   127  S  SD  . MET A 1 17  ? 60.36500 65.66900 31.57200 1.000 30.26215 ?  17  MET A SD  1 
ATOM   128  C  CE  . MET A 1 17  ? 61.39700 65.73500 33.02200 1.000 32.02955 ?  17  MET A CE  1 
ATOM   129  N  N   . LEU A 1 18  ? 62.86500 60.30600 30.60200 1.000 18.02030 ?  18  LEU A N   1 
ATOM   130  C  CA  . LEU A 1 18  ? 63.64200 59.20200 31.15000 1.000 21.95387 ?  18  LEU A CA  1 
ATOM   131  C  C   . LEU A 1 18  ? 64.92800 58.96200 30.37200 1.000 19.92884 ?  18  LEU A C   1 
ATOM   132  O  O   . LEU A 1 18  ? 65.89400 58.44100 30.93800 1.000 22.00151 ?  18  LEU A O   1 
ATOM   133  C  CB  . LEU A 1 18  ? 62.80900 57.91900 31.12800 1.000 20.74366 ?  18  LEU A CB  1 
ATOM   134  C  CG  . LEU A 1 18  ? 61.83900 57.65800 32.27000 1.000 25.74591 ?  18  LEU A CG  1 
ATOM   135  C  CD1 . LEU A 1 18  ? 61.16300 56.32900 31.98800 1.000 22.34508 ?  18  LEU A CD1 1 
ATOM   136  C  CD2 . LEU A 1 18  ? 62.58400 57.61800 33.60100 1.000 24.39195 ?  18  LEU A CD2 1 
ATOM   137  N  N   . VAL A 1 19  ? 64.96500 59.30600 29.07900 1.000 21.78364 ?  19  VAL A N   1 
ATOM   138  C  CA  . VAL A 1 19  ? 66.18600 59.05900 28.30800 1.000 20.13131 ?  19  VAL A CA  1 
ATOM   139  C  C   . VAL A 1 19  ? 67.37500 59.77100 28.94700 1.000 26.93670 ?  19  VAL A C   1 
ATOM   140  O  O   . VAL A 1 19  ? 68.47000 59.20400 29.06000 1.000 26.25791 ?  19  VAL A O   1 
ATOM   141  C  CB  . VAL A 1 19  ? 66.00300 59.46000 26.83100 1.000 19.78327 ?  19  VAL A CB  1 
ATOM   142  C  CG1 . VAL A 1 19  ? 67.31900 59.29400 26.05900 1.000 23.51452 ?  19  VAL A CG1 1 
ATOM   143  C  CG2 . VAL A 1 19  ? 64.86800 58.66400 26.16300 1.000 19.88770 ?  19  VAL A CG2 1 
ATOM   144  N  N   . GLU A 1 20  ? 67.17100 61.01300 29.40500 1.000 22.78463 ?  20  GLU A N   1 
ATOM   145  C  CA  . GLU A 1 20  ? 68.23900 61.75700 30.06900 1.000 24.82292 ?  20  GLU A CA  1 
ATOM   146  C  C   . GLU A 1 20  ? 68.33100 61.41900 31.55500 1.000 30.68346 ?  20  GLU A C   1 
ATOM   147  O  O   . GLU A 1 20  ? 69.43000 61.21300 32.08700 1.000 30.47204 ?  20  GLU A O   1 
ATOM   148  C  CB  . GLU A 1 20  ? 68.02000 63.25800 29.85900 1.000 26.18742 ?  20  GLU A CB  1 
ATOM   149  C  CG  . GLU A 1 20  ? 68.98400 64.15800 30.61700 1.000 34.85897 ?  20  GLU A CG  1 
ATOM   150  C  CD  . GLU A 1 20  ? 68.76100 65.63300 30.29900 1.000 41.87646 ?  20  GLU A CD  1 
ATOM   151  O  OE1 . GLU A 1 20  ? 67.97400 65.93900 29.36400 1.000 35.74282 ?  20  GLU A OE1 1 
ATOM   152  O  OE2 . GLU A 1 20  ? 69.36900 66.49100 30.98200 1.000 41.71768 -1 20  GLU A OE2 1 
ATOM   153  N  N   . GLU A 1 21  ? 67.18900 61.32900 32.23500 1.000 23.89175 ?  21  GLU A N   1 
ATOM   154  C  CA  . GLU A 1 21  ? 67.19500 61.18200 33.68900 1.000 28.27949 ?  21  GLU A CA  1 
ATOM   155  C  C   . GLU A 1 21  ? 67.62000 59.78300 34.12100 1.000 32.46705 ?  21  GLU A C   1 
ATOM   156  O  O   . GLU A 1 21  ? 68.38400 59.63000 35.08100 1.000 30.60797 ?  21  GLU A O   1 
ATOM   157  C  CB  . GLU A 1 21  ? 65.80800 61.51300 34.24800 1.000 31.89936 ?  21  GLU A CB  1 
ATOM   158  C  CG  . GLU A 1 21  ? 65.84200 62.38600 35.49400 1.000 48.83145 ?  21  GLU A CG  1 
ATOM   159  C  CD  . GLU A 1 21  ? 64.58800 63.23600 35.65500 1.000 62.86532 ?  21  GLU A CD  1 
ATOM   160  O  OE1 . GLU A 1 21  ? 63.47600 62.72800 35.38800 1.000 62.32766 ?  21  GLU A OE1 1 
ATOM   161  O  OE2 . GLU A 1 21  ? 64.71900 64.41900 36.04100 1.000 69.10660 -1 21  GLU A OE2 1 
ATOM   162  N  N   . ASP A 1 22  ? 67.12100 58.74800 33.44400 1.000 24.92194 ?  22  ASP A N   1 
ATOM   163  C  CA  . ASP A 1 22  ? 67.37100 57.36200 33.83600 1.000 23.82084 ?  22  ASP A CA  1 
ATOM   164  C  C   . ASP A 1 22  ? 67.24800 56.49500 32.59400 1.000 26.80834 ?  22  ASP A C   1 
ATOM   165  O  O   . ASP A 1 22  ? 66.27600 55.75000 32.42800 1.000 22.28201 ?  22  ASP A O   1 
ATOM   166  C  CB  . ASP A 1 22  ? 66.37400 56.92300 34.91200 1.000 27.68964 ?  22  ASP A CB  1 
ATOM   167  C  CG  . ASP A 1 22  ? 66.73500 55.58000 35.54600 1.000 26.47889 ?  22  ASP A CG  1 
ATOM   168  O  OD1 . ASP A 1 22  ? 67.81400 55.02400 35.25900 1.000 30.56695 ?  22  ASP A OD1 1 
ATOM   169  O  OD2 . ASP A 1 22  ? 65.92300 55.06600 36.35300 1.000 35.63310 -1 22  ASP A OD2 1 
ATOM   170  N  N   . PRO A 1 23  ? 68.21700 56.58600 31.67700 1.000 21.88803 ?  23  PRO A N   1 
ATOM   171  C  CA  . PRO A 1 23  ? 68.12500 55.77300 30.44900 1.000 23.97704 ?  23  PRO A CA  1 
ATOM   172  C  C   . PRO A 1 23  ? 68.01900 54.28500 30.70900 1.000 23.26373 ?  23  PRO A C   1 
ATOM   173  O  O   . PRO A 1 23  ? 67.43900 53.57000 29.88500 1.000 22.59795 ?  23  PRO A O   1 
ATOM   174  C  CB  . PRO A 1 23  ? 69.41100 56.12900 29.68400 1.000 24.65232 ?  23  PRO A CB  1 
ATOM   175  C  CG  . PRO A 1 23  ? 70.34000 56.67900 30.72700 1.000 23.93102 ?  23  PRO A CG  1 
ATOM   176  C  CD  . PRO A 1 23  ? 69.43300 57.41800 31.68700 1.000 26.29674 ?  23  PRO A CD  1 
ATOM   177  N  N   . GLY A 1 24  ? 68.53000 53.80100 31.83900 1.000 20.26382 ?  24  GLY A N   1 
ATOM   178  C  CA  . GLY A 1 24  ? 68.43500 52.40900 32.22900 1.000 24.35658 ?  24  GLY A CA  1 
ATOM   179  C  C   . GLY A 1 24  ? 67.17700 52.02800 32.97900 1.000 21.87996 ?  24  GLY A C   1 
ATOM   180  O  O   . GLY A 1 24  ? 67.11100 50.91000 33.49700 1.000 22.21026 ?  24  GLY A O   1 
ATOM   181  N  N   . PHE A 1 25  ? 66.16700 52.90800 33.01400 1.000 19.57732 ?  25  PHE A N   1 
ATOM   182  C  CA  . PHE A 1 25  ? 64.98300 52.69900 33.85400 1.000 21.54897 ?  25  PHE A CA  1 
ATOM   183  C  C   . PHE A 1 25  ? 64.32000 51.35300 33.60000 1.000 21.63490 ?  25  PHE A C   1 
ATOM   184  O  O   . PHE A 1 25  ? 63.80300 50.72500 34.53300 1.000 22.82107 ?  25  PHE A O   1 
ATOM   185  C  CB  . PHE A 1 25  ? 63.98300 53.82400 33.60600 1.000 21.05061 ?  25  PHE A CB  1 
ATOM   186  C  CG  . PHE A 1 25  ? 62.69000 53.69400 34.38400 1.000 21.43450 ?  25  PHE A CG  1 
ATOM   187  C  CD1 . PHE A 1 25  ? 61.61200 53.01200 33.85100 1.000 21.53572 ?  25  PHE A CD1 1 
ATOM   188  C  CD2 . PHE A 1 25  ? 62.55100 54.28500 35.63000 1.000 25.62001 ?  25  PHE A CD2 1 
ATOM   189  C  CE1 . PHE A 1 25  ? 60.41500 52.89500 34.55900 1.000 23.71315 ?  25  PHE A CE1 1 
ATOM   190  C  CE2 . PHE A 1 25  ? 61.35900 54.17700 36.34100 1.000 25.74737 ?  25  PHE A CE2 1 
ATOM   191  C  CZ  . PHE A 1 25  ? 60.29600 53.48400 35.80000 1.000 22.15089 ?  25  PHE A CZ  1 
ATOM   192  N  N   . PHE A 1 26  ? 64.31200 50.89700 32.34800 1.000 20.51181 ?  26  PHE A N   1 
ATOM   193  C  CA  . PHE A 1 26  ? 63.62600 49.66800 31.97200 1.000 21.52820 ?  26  PHE A CA  1 
ATOM   194  C  C   . PHE A 1 26  ? 64.54900 48.46700 31.89100 1.000 22.26999 ?  26  PHE A C   1 
ATOM   195  O  O   . PHE A 1 26  ? 64.09600 47.38900 31.49300 1.000 27.49556 ?  26  PHE A O   1 
ATOM   196  C  CB  . PHE A 1 26  ? 62.92600 49.85000 30.61500 1.000 20.57774 ?  26  PHE A CB  1 
ATOM   197  C  CG  . PHE A 1 26  ? 61.91500 50.96400 30.59600 1.000 23.16619 ?  26  PHE A CG  1 
ATOM   198  C  CD1 . PHE A 1 26  ? 60.66700 50.79800 31.17400 1.000 18.98443 ?  26  PHE A CD1 1 
ATOM   199  C  CD2 . PHE A 1 26  ? 62.22000 52.17900 29.99200 1.000 19.46479 ?  26  PHE A CD2 1 
ATOM   200  C  CE1 . PHE A 1 26  ? 59.71700 51.82000 31.13600 1.000 20.78207 ?  26  PHE A CE1 1 
ATOM   201  C  CE2 . PHE A 1 26  ? 61.29300 53.21300 29.96700 1.000 19.03152 ?  26  PHE A CE2 1 
ATOM   202  C  CZ  . PHE A 1 26  ? 60.04100 53.03900 30.54200 1.000 20.39905 ?  26  PHE A CZ  1 
ATOM   203  N  N   . GLU A 1 27  ? 65.82800 48.62200 32.26400 1.000 21.55039 ?  27  GLU A N   1 
ATOM   204  C  CA  . GLU A 1 27  ? 66.81200 47.57200 32.00300 1.000 24.28022 ?  27  GLU A CA  1 
ATOM   205  C  C   . GLU A 1 27  ? 66.55800 46.32100 32.83700 1.000 26.87268 ?  27  GLU A C   1 
ATOM   206  O  O   . GLU A 1 27  ? 66.64000 45.20000 32.31900 1.000 29.33581 ?  27  GLU A O   1 
ATOM   207  C  CB  . GLU A 1 27  ? 68.22400 48.11700 32.23400 1.000 27.37262 ?  27  GLU A CB  1 
ATOM   208  C  CG  . GLU A 1 27  ? 68.70800 49.03100 31.10900 1.000 27.36762 ?  27  GLU A CG  1 
ATOM   209  C  CD  . GLU A 1 27  ? 69.00400 48.27000 29.82700 1.000 30.45766 ?  27  GLU A CD  1 
ATOM   210  O  OE1 . GLU A 1 27  ? 70.10100 47.68700 29.72500 1.000 29.75204 ?  27  GLU A OE1 1 
ATOM   211  O  OE2 . GLU A 1 27  ? 68.13700 48.23800 28.92300 1.000 30.04063 -1 27  GLU A OE2 1 
ATOM   212  N  N   . LYS A 1 28  ? 66.26500 46.47600 34.12800 1.000 26.04299 ?  28  LYS A N   1 
ATOM   213  C  CA  . LYS A 1 28  ? 65.94300 45.30000 34.93400 1.000 30.26858 ?  28  LYS A CA  1 
ATOM   214  C  C   . LYS A 1 28  ? 64.62900 44.66700 34.48900 1.000 34.11789 ?  28  LYS A C   1 
ATOM   215  O  O   . LYS A 1 28  ? 64.48200 43.43800 34.51200 1.000 30.07418 ?  28  LYS A O   1 
ATOM   216  C  CB  . LYS A 1 28  ? 65.90000 45.66100 36.41500 1.000 33.78117 ?  28  LYS A CB  1 
ATOM   217  C  CG  . LYS A 1 28  ? 67.24000 46.10500 36.98300 1.000 44.68768 ?  28  LYS A CG  1 
ATOM   218  C  CD  . LYS A 1 28  ? 68.06200 44.93100 37.49000 1.000 53.80840 ?  28  LYS A CD  1 
ATOM   219  C  CE  . LYS A 1 28  ? 69.26200 45.41400 38.30500 1.000 58.13641 ?  28  LYS A CE  1 
ATOM   220  N  NZ  . LYS A 1 28  ? 70.03000 44.28600 38.92000 1.000 61.37203 ?  28  LYS A NZ  1 
ATOM   221  N  N   . LEU A 1 29  ? 63.65800 45.49000 34.07500 1.000 26.70823 ?  29  LEU A N   1 
ATOM   222  C  CA  . LEU A 1 29  ? 62.39800 44.95700 33.56300 1.000 28.28713 ?  29  LEU A CA  1 
ATOM   223  C  C   . LEU A 1 29  ? 62.61900 44.09700 32.32500 1.000 33.25349 ?  29  LEU A C   1 
ATOM   224  O  O   . LEU A 1 29  ? 61.88900 43.12400 32.10300 1.000 27.04854 ?  29  LEU A O   1 
ATOM   225  C  CB  . LEU A 1 29  ? 61.43200 46.11200 33.26000 1.000 26.45467 ?  29  LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 29  ? 60.86500 46.85900 34.47700 1.000 24.01536 ?  29  LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 29  ? 60.24100 48.21600 34.11600 1.000 22.16264 ?  29  LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 29  ? 59.83100 46.00000 35.17900 1.000 25.97718 ?  29  LEU A CD2 1 
ATOM   229  N  N   . ALA A 1 30  ? 63.62000 44.43500 31.50700 1.000 29.03222 ?  30  ALA A N   1 
ATOM   230  C  CA  . ALA A 1 30  ? 63.88200 43.67000 30.29600 1.000 35.61293 ?  30  ALA A CA  1 
ATOM   231  C  C   . ALA A 1 30  ? 64.60700 42.35800 30.57300 1.000 39.79852 ?  30  ALA A C   1 
ATOM   232  O  O   . ALA A 1 30  ? 64.64700 41.49100 29.69400 1.000 39.29588 ?  30  ALA A O   1 
ATOM   233  C  CB  . ALA A 1 30  ? 64.65700 44.52700 29.28500 1.000 33.71169 ?  30  ALA A CB  1 
ATOM   234  N  N   . GLN A 1 31  ? 65.16100 42.19000 31.77100 1.000 38.09976 ?  31  GLN A N   1 
ATOM   235  C  CA  . GLN A 1 31  ? 65.76700 40.93700 32.18800 1.000 42.63095 ?  31  GLN A CA  1 
ATOM   236  C  C   . GLN A 1 31  ? 64.69200 39.96000 32.66700 1.000 43.35629 ?  31  GLN A C   1 
ATOM   237  O  O   . GLN A 1 31  ? 63.54200 40.32500 32.92500 1.000 44.29543 ?  31  GLN A O   1 
ATOM   238  C  CB  . GLN A 1 31  ? 66.79900 41.19800 33.28200 1.000 45.50799 ?  31  GLN A CB  1 
ATOM   239  C  CG  . GLN A 1 31  ? 67.89700 42.17900 32.85800 1.000 43.96722 ?  31  GLN A CG  1 
ATOM   240  C  CD  . GLN A 1 31  ? 68.71600 42.69500 34.02800 1.000 50.01975 ?  31  GLN A CD  1 
ATOM   241  O  OE1 . GLN A 1 31  ? 68.76500 42.07200 35.09100 1.000 56.35232 ?  31  GLN A OE1 1 
ATOM   242  N  NE2 . GLN A 1 31  ? 69.36100 43.84500 33.83900 1.000 46.61825 ?  31  GLN A NE2 1 
ATOM   243  N  N   . ALA A 1 32  ? 65.07600 38.69200 32.78100 1.000 47.05886 ?  32  ALA A N   1 
ATOM   244  C  CA  . ALA A 1 32  ? 64.13500 37.64800 33.16900 1.000 52.36125 ?  32  ALA A CA  1 
ATOM   245  C  C   . ALA A 1 32  ? 63.94500 37.52800 34.68300 1.000 48.32406 ?  32  ALA A C   1 
ATOM   246  O  O   . ALA A 1 32  ? 63.32000 36.55900 35.12700 1.000 50.81146 ?  32  ALA A O   1 
ATOM   247  C  CB  . ALA A 1 32  ? 64.55000 36.29900 32.57000 1.000 47.44793 ?  32  ALA A CB  1 
ATOM   248  N  N   . GLN A 1 33  ? 64.45300 38.47300 35.47500 1.000 45.44702 ?  33  GLN A N   1 
ATOM   249  C  CA  . GLN A 1 33  ? 64.31200 38.39900 36.92600 1.000 44.93734 ?  33  GLN A CA  1 
ATOM   250  C  C   . GLN A 1 33  ? 62.84600 38.52700 37.32400 1.000 37.02655 ?  33  GLN A C   1 
ATOM   251  O  O   . GLN A 1 33  ? 62.15900 39.46900 36.91900 1.000 37.97854 ?  33  GLN A O   1 
ATOM   252  C  CB  . GLN A 1 33  ? 65.12800 39.50700 37.59300 1.000 47.29766 ?  33  GLN A CB  1 
ATOM   253  C  CG  . GLN A 1 33  ? 66.63700 39.32600 37.47500 1.000 61.65853 ?  33  GLN A CG  1 
ATOM   254  C  CD  . GLN A 1 33  ? 67.42300 40.54400 37.93700 1.000 71.07913 ?  33  GLN A CD  1 
ATOM   255  O  OE1 . GLN A 1 33  ? 66.88600 41.65300 38.03300 1.000 68.76677 ?  33  GLN A OE1 1 
ATOM   256  N  NE2 . GLN A 1 33  ? 68.70500 40.34300 38.22200 1.000 72.00389 ?  33  GLN A NE2 1 
ATOM   257  N  N   . LYS A 1 34  ? 62.36700 37.57600 38.11600 1.000 29.22948 ?  34  LYS A N   1 
ATOM   258  C  CA  . LYS A 1 34  ? 60.98100 37.61200 38.54800 1.000 27.36059 ?  34  LYS A CA  1 
ATOM   259  C  C   . LYS A 1 34  ? 60.85600 38.42200 39.83100 1.000 21.51312 ?  34  LYS A C   1 
ATOM   260  O  O   . LYS A 1 34  ? 61.81800 38.55900 40.58900 1.000 22.12322 ?  34  LYS A O   1 
ATOM   261  C  CB  . LYS A 1 34  ? 60.49200 36.18500 38.78700 1.000 26.80505 ?  34  LYS A CB  1 
ATOM   262  C  CG  . LYS A 1 34  ? 60.43300 35.32200 37.52200 1.000 27.56036 ?  34  LYS A CG  1 
ATOM   263  C  CD  . LYS A 1 34  ? 60.25300 33.86400 37.90400 1.000 29.03238 ?  34  LYS A CD  1 
ATOM   264  C  CE  . LYS A 1 34  ? 59.95900 32.99800 36.69700 1.000 39.43509 ?  34  LYS A CE  1 
ATOM   265  N  NZ  . LYS A 1 34  ? 59.79600 31.57600 37.10600 1.000 41.54996 ?  34  LYS A NZ  1 
ATOM   266  N  N   . PRO A 1 35  ? 59.68000 38.99000 40.11100 1.000 20.17498 ?  35  PRO A N   1 
ATOM   267  C  CA  . PRO A 1 35  ? 59.49900 39.70000 41.38600 1.000 18.49024 ?  35  PRO A CA  1 
ATOM   268  C  C   . PRO A 1 35  ? 59.65800 38.73600 42.54800 1.000 15.38809 ?  35  PRO A C   1 
ATOM   269  O  O   . PRO A 1 35  ? 59.25200 37.57900 42.46000 1.000 19.00104 ?  35  PRO A O   1 
ATOM   270  C  CB  . PRO A 1 35  ? 58.05500 40.20900 41.30500 1.000 17.73362 ?  35  PRO A CB  1 
ATOM   271  C  CG  . PRO A 1 35  ? 57.38500 39.32600 40.29400 1.000 21.27680 ?  35  PRO A CG  1 
ATOM   272  C  CD  . PRO A 1 35  ? 58.45300 38.99700 39.29100 1.000 20.11242 ?  35  PRO A CD  1 
ATOM   273  N  N   . ARG A 1 36  ? 60.27900 39.21700 43.63200 1.000 16.30093 ?  36  ARG A N   1 
ATOM   274  C  CA  . ARG A 1 36  ? 60.42600 38.42300 44.84400 1.000 15.11245 ?  36  ARG A CA  1 
ATOM   275  C  C   . ARG A 1 36  ? 59.32100 38.66000 45.85800 1.000 15.23718 ?  36  ARG A C   1 
ATOM   276  O  O   . ARG A 1 36  ? 59.22300 37.89600 46.82100 1.000 12.79460 ?  36  ARG A O   1 
ATOM   277  C  CB  . ARG A 1 36  ? 61.78200 38.70800 45.51300 1.000 21.15213 ?  36  ARG A CB  1 
ATOM   278  C  CG  . ARG A 1 36  ? 62.97900 38.34700 44.64200 1.000 28.69335 ?  36  ARG A CG  1 
ATOM   279  C  CD  . ARG A 1 36  ? 64.22600 38.00900 45.46300 1.000 39.89710 ?  36  ARG A CD  1 
ATOM   280  N  NE  . ARG A 1 36  ? 64.48400 38.92000 46.57500 1.000 43.03705 ?  36  ARG A NE  1 
ATOM   281  C  CZ  . ARG A 1 36  ? 64.46200 38.56600 47.85500 1.000 46.12446 ?  36  ARG A CZ  1 
ATOM   282  N  NH1 . ARG A 1 36  ? 64.15100 37.33400 48.22600 1.000 39.47032 ?  36  ARG A NH1 1 
ATOM   283  N  NH2 . ARG A 1 36  ? 64.77400 39.46700 48.78600 1.000 43.14540 ?  36  ARG A NH2 1 
ATOM   284  N  N   . PHE A 1 37  ? 58.47100 39.66300 45.65100 1.000 13.47569 ?  37  PHE A N   1 
ATOM   285  C  CA  . PHE A 1 37  ? 57.43200 40.02900 46.60900 1.000 12.52814 ?  37  PHE A CA  1 
ATOM   286  C  C   . PHE A 1 37  ? 56.08400 40.05200 45.91000 1.000 11.55833 ?  37  PHE A C   1 
ATOM   287  O  O   . PHE A 1 37  ? 55.97200 40.52500 44.77900 1.000 14.04740 ?  37  PHE A O   1 
ATOM   288  C  CB  . PHE A 1 37  ? 57.68600 41.43900 47.17200 1.000 13.63127 ?  37  PHE A CB  1 
ATOM   289  C  CG  . PHE A 1 37  ? 59.02100 41.58100 47.87200 1.000 13.62387 ?  37  PHE A CG  1 
ATOM   290  C  CD1 . PHE A 1 37  ? 60.15300 41.94200 47.16000 1.000 18.00615 ?  37  PHE A CD1 1 
ATOM   291  C  CD2 . PHE A 1 37  ? 59.12300 41.35400 49.23900 1.000 16.71642 ?  37  PHE A CD2 1 
ATOM   292  C  CE1 . PHE A 1 37  ? 61.38300 42.05400 47.79600 1.000 17.59025 ?  37  PHE A CE1 1 
ATOM   293  C  CE2 . PHE A 1 37  ? 60.34700 41.48200 49.88400 1.000 19.40431 ?  37  PHE A CE2 1 
ATOM   294  C  CZ  . PHE A 1 37  ? 61.47300 41.83100 49.15600 1.000 20.10843 ?  37  PHE A CZ  1 
ATOM   295  N  N   . LEU A 1 38  ? 55.06600 39.55300 46.60600 1.000 11.85832 ?  38  LEU A N   1 
ATOM   296  C  CA  . LEU A 1 38  ? 53.66600 39.75900 46.25800 1.000 12.05460 ?  38  LEU A CA  1 
ATOM   297  C  C   . LEU A 1 38  ? 53.06100 40.65900 47.32000 1.000 13.25308 ?  38  LEU A C   1 
ATOM   298  O  O   . LEU A 1 38  ? 53.19700 40.38200 48.52200 1.000 12.46022 ?  38  LEU A O   1 
ATOM   299  C  CB  . LEU A 1 38  ? 52.89000 38.43000 46.20000 1.000 12.26782 ?  38  LEU A CB  1 
ATOM   300  C  CG  . LEU A 1 38  ? 51.35000 38.57100 46.19200 1.000 12.03951 ?  38  LEU A CG  1 
ATOM   301  C  CD1 . LEU A 1 38  ? 50.81400 39.38300 44.97700 1.000 12.87041 ?  38  LEU A CD1 1 
ATOM   302  C  CD2 . LEU A 1 38  ? 50.69600 37.19900 46.23300 1.000 12.96394 ?  38  LEU A CD2 1 
ATOM   303  N  N   . TRP A 1 39  ? 52.42500 41.74200 46.88200 1.000 11.44040 ?  39  TRP A N   1 
ATOM   304  C  CA  . TRP A 1 39  ? 51.75300 42.68300 47.76500 1.000 11.88343 ?  39  TRP A CA  1 
ATOM   305  C  C   . TRP A 1 39  ? 50.25800 42.50900 47.55800 1.000 10.48095 ?  39  TRP A C   1 
ATOM   306  O  O   . TRP A 1 39  ? 49.78000 42.63100 46.42400 1.000 12.72573 ?  39  TRP A O   1 
ATOM   307  C  CB  . TRP A 1 39  ? 52.14500 44.10500 47.35100 1.000 13.30777 ?  39  TRP A CB  1 
ATOM   308  C  CG  . TRP A 1 39  ? 51.70200 45.20000 48.28800 1.000 13.56032 ?  39  TRP A CG  1 
ATOM   309  C  CD1 . TRP A 1 39  ? 50.48500 45.82000 48.33600 1.000 15.28659 ?  39  TRP A CD1 1 
ATOM   310  C  CD2 . TRP A 1 39  ? 52.49900 45.79800 49.32300 1.000 13.69265 ?  39  TRP A CD2 1 
ATOM   311  N  NE1 . TRP A 1 39  ? 50.47800 46.77800 49.34600 1.000 14.28470 ?  39  TRP A NE1 1 
ATOM   312  C  CE2 . TRP A 1 39  ? 51.71200 46.79000 49.94100 1.000 13.32706 ?  39  TRP A CE2 1 
ATOM   313  C  CE3 . TRP A 1 39  ? 53.82300 45.63200 49.73600 1.000 15.81530 ?  39  TRP A CE3 1 
ATOM   314  C  CZ2 . TRP A 1 39  ? 52.20000 47.58900 50.98400 1.000 15.18982 ?  39  TRP A CZ2 1 
ATOM   315  C  CZ3 . TRP A 1 39  ? 54.30000 46.42000 50.77700 1.000 19.51853 ?  39  TRP A CZ3 1 
ATOM   316  C  CH2 . TRP A 1 39  ? 53.49100 47.38500 51.37800 1.000 17.93947 ?  39  TRP A CH2 1 
ATOM   317  N  N   . ILE A 1 40  ? 49.52600 42.21700 48.63200 1.000 10.16647 ?  40  ILE A N   1 
ATOM   318  C  CA  . ILE A 1 40  ? 48.06900 42.21600 48.62200 1.000 10.90725 ?  40  ILE A CA  1 
ATOM   319  C  C   . ILE A 1 40  ? 47.63300 43.41300 49.44600 1.000 12.64494 ?  40  ILE A C   1 
ATOM   320  O  O   . ILE A 1 40  ? 47.83900 43.44500 50.67100 1.000 12.50038 ?  40  ILE A O   1 
ATOM   321  C  CB  . ILE A 1 40  ? 47.50800 40.92900 49.22500 1.000 10.41339 ?  40  ILE A CB  1 
ATOM   322  C  CG1 . ILE A 1 40  ? 47.97500 39.72000 48.38300 1.000 11.75096 ?  40  ILE A CG1 1 
ATOM   323  C  CG2 . ILE A 1 40  ? 45.98400 40.99400 49.34400 1.000 12.35359 ?  40  ILE A CG2 1 
ATOM   324  C  CD1 . ILE A 1 40  ? 47.69200 38.33800 48.99300 1.000 11.66885 ?  40  ILE A CD1 1 
ATOM   325  N  N   . GLY A 1 41  ? 47.03500 44.39100 48.78500 1.000 9.99522  ?  41  GLY A N   1 
ATOM   326  C  CA  . GLY A 1 41  ? 46.66000 45.61500 49.45000 1.000 11.05384 ?  41  GLY A CA  1 
ATOM   327  C  C   . GLY A 1 41  ? 45.25200 46.03100 49.10600 1.000 10.46469 ?  41  GLY A C   1 
ATOM   328  O  O   . GLY A 1 41  ? 44.50400 45.32000 48.42200 1.000 12.01887 ?  41  GLY A O   1 
ATOM   329  N  N   . CYS A 1 42  ? 44.89100 47.19800 49.57700 1.000 11.44852 ?  42  CYS A N   1 
ATOM   330  C  CA  . CYS A 1 42  ? 43.56600 47.69900 49.31500 1.000 10.27806 ?  42  CYS A CA  1 
ATOM   331  C  C   . CYS A 1 42  ? 43.45500 48.54500 48.06000 1.000 10.09295 ?  42  CYS A C   1 
ATOM   332  O  O   . CYS A 1 42  ? 44.35600 49.25600 47.71500 1.000 11.11630 ?  42  CYS A O   1 
ATOM   333  C  CB  . CYS A 1 42  ? 43.12400 48.53800 50.49800 1.000 10.22561 ?  42  CYS A CB  1 
ATOM   334  S  SG  . CYS A 1 42  ? 41.37900 49.14300 50.43500 1.000 10.65661 ?  42  CYS A SG  1 
ATOM   335  N  N   . SER A 1 43  ? 42.30400 48.42000 47.42100 1.000 9.96550  ?  43  SER A N   1 
ATOM   336  C  CA  . SER A 1 43  ? 42.05000 49.27700 46.27100 1.000 9.24438  ?  43  SER A CA  1 
ATOM   337  C  C   . SER A 1 43  ? 42.12900 50.76100 46.59600 1.000 10.10155 ?  43  SER A C   1 
ATOM   338  O  O   . SER A 1 43  ? 42.38000 51.56000 45.67900 1.000 11.08004 ?  43  SER A O   1 
ATOM   339  C  CB  . SER A 1 43  ? 40.68300 48.92500 45.66000 1.000 12.10603 ?  43  SER A CB  1 
ATOM   340  O  OG  . SER A 1 43  ? 40.72000 47.59500 45.15300 1.000 12.18792 ?  43  SER A OG  1 
ATOM   341  N  N   . ASP A 1 44  ? 41.95500 51.15600 47.84600 1.000 10.26100 ?  44  ASP A N   1 
ATOM   342  C  CA  . ASP A 1 44  ? 42.11700 52.57100 48.22600 1.000 12.36005 ?  44  ASP A CA  1 
ATOM   343  C  C   . ASP A 1 44  ? 43.49100 53.07600 47.82600 1.000 11.89597 ?  44  ASP A C   1 
ATOM   344  O  O   . ASP A 1 44  ? 43.63300 54.21200 47.46600 1.000 13.87785 ?  44  ASP A O   1 
ATOM   345  C  CB  . ASP A 1 44  ? 41.94300 52.80900 49.72500 1.000 11.76101 ?  44  ASP A CB  1 
ATOM   346  C  CG  . ASP A 1 44  ? 40.48500 52.80000 50.18400 1.000 12.42117 ?  44  ASP A CG  1 
ATOM   347  O  OD1 . ASP A 1 44  ? 39.62900 53.35800 49.50100 1.000 15.45796 ?  44  ASP A OD1 1 
ATOM   348  O  OD2 . ASP A 1 44  ? 40.20200 52.25400 51.26100 1.000 13.11197 -1 44  ASP A OD2 1 
ATOM   349  N  N   . SER A 1 45  ? 44.49500 52.21000 47.91500 1.000 12.20102 ?  45  SER A N   1 
ATOM   350  C  CA  . SER A 1 45  ? 45.85300 52.54000 47.46800 1.000 12.89458 ?  45  SER A CA  1 
ATOM   351  C  C   . SER A 1 45  ? 46.26100 53.94900 47.88400 1.000 15.65957 ?  45  SER A C   1 
ATOM   352  O  O   . SER A 1 45  ? 46.65100 54.77400 47.05900 1.000 17.00231 ?  45  SER A O   1 
ATOM   353  C  CB  . SER A 1 45  ? 45.97200 52.37200 45.95000 1.000 14.14896 ?  45  SER A CB  1 
ATOM   354  O  OG  . SER A 1 45  ? 47.33900 52.47700 45.54600 1.000 17.25103 ?  45  SER A OG  1 
ATOM   355  N  N   . ARG A 1 46  ? 46.12800 54.24200 49.18200 1.000 14.74072 ?  46  ARG A N   1 
ATOM   356  C  CA  . ARG A 1 46  ? 46.26100 55.63300 49.60800 1.000 14.66003 ?  46  ARG A CA  1 
ATOM   357  C  C   . ARG A 1 46  ? 47.68600 56.13200 49.40300 1.000 16.10922 ?  46  ARG A C   1 
ATOM   358  O  O   . ARG A 1 46  ? 47.90000 57.21500 48.84000 1.000 19.44910 ?  46  ARG A O   1 
ATOM   359  C  CB  . ARG A 1 46  ? 45.77900 55.80700 51.04500 1.000 15.12910 ?  46  ARG A CB  1 
ATOM   360  C  CG  . ARG A 1 46  ? 44.32600 55.45000 51.25100 1.000 15.85586 ?  46  ARG A CG  1 
ATOM   361  C  CD  . ARG A 1 46  ? 43.40000 56.33700 50.42700 1.000 19.92247 ?  46  ARG A CD  1 
ATOM   362  N  NE  . ARG A 1 46  ? 43.19900 57.65200 51.03200 1.000 19.91932 ?  46  ARG A NE  1 
ATOM   363  C  CZ  . ARG A 1 46  ? 42.59800 58.65900 50.40900 1.000 23.74502 ?  46  ARG A CZ  1 
ATOM   364  N  NH1 . ARG A 1 46  ? 42.15800 58.53800 49.16100 1.000 24.27094 ?  46  ARG A NH1 1 
ATOM   365  N  NH2 . ARG A 1 46  ? 42.42600 59.81400 51.05200 1.000 23.61090 ?  46  ARG A NH2 1 
ATOM   366  N  N   . VAL A 1 47  ? 48.67200 55.33500 49.79900 1.000 15.86539 ?  47  VAL A N   1 
ATOM   367  C  CA  . VAL A 1 47  ? 50.05900 55.55000 49.41000 1.000 15.22533 ?  47  VAL A CA  1 
ATOM   368  C  C   . VAL A 1 47  ? 50.48800 54.30800 48.64400 1.000 14.50532 ?  47  VAL A C   1 
ATOM   369  O  O   . VAL A 1 47  ? 50.37200 53.19800 49.17000 1.000 16.66859 ?  47  VAL A O   1 
ATOM   370  C  CB  . VAL A 1 47  ? 50.97400 55.75800 50.62800 1.000 17.73967 ?  47  VAL A CB  1 
ATOM   371  C  CG1 . VAL A 1 47  ? 52.42300 55.97500 50.17500 1.000 19.12740 ?  47  VAL A CG1 1 
ATOM   372  C  CG2 . VAL A 1 47  ? 50.49100 56.94800 51.45500 1.000 19.05615 ?  47  VAL A CG2 1 
ATOM   373  N  N   . PRO A 1 48  ? 50.96100 54.43800 47.40400 1.000 14.90147 ?  48  PRO A N   1 
ATOM   374  C  CA  . PRO A 1 48  ? 51.32800 53.24500 46.62700 1.000 16.31722 ?  48  PRO A CA  1 
ATOM   375  C  C   . PRO A 1 48  ? 52.42800 52.44100 47.31200 1.000 14.18869 ?  48  PRO A C   1 
ATOM   376  O  O   . PRO A 1 48  ? 53.29900 52.98800 47.99800 1.000 14.44214 ?  48  PRO A O   1 
ATOM   377  C  CB  . PRO A 1 48  ? 51.83900 53.82400 45.30400 1.000 19.62894 ?  48  PRO A CB  1 
ATOM   378  C  CG  . PRO A 1 48  ? 51.23800 55.21600 45.22400 1.000 22.80402 ?  48  PRO A CG  1 
ATOM   379  C  CD  . PRO A 1 48  ? 51.13100 55.69000 46.63800 1.000 17.85488 ?  48  PRO A CD  1 
ATOM   380  N  N   . ALA A 1 49  ? 52.36600 51.12100 47.13200 1.000 14.71945 ?  49  ALA A N   1 
ATOM   381  C  CA  . ALA A 1 49  ? 53.31300 50.23300 47.81000 1.000 15.70288 ?  49  ALA A CA  1 
ATOM   382  C  C   . ALA A 1 49  ? 54.76200 50.53200 47.43700 1.000 16.06066 ?  49  ALA A C   1 
ATOM   383  O  O   . ALA A 1 49  ? 55.66300 50.41000 48.28600 1.000 15.59510 ?  49  ALA A O   1 
ATOM   384  C  CB  . ALA A 1 49  ? 52.97900 48.77400 47.47600 1.000 15.60664 ?  49  ALA A CB  1 
ATOM   385  N  N   . GLU A 1 50  ? 55.00200 50.95300 46.18800 1.000 16.35591 ?  50  GLU A N   1 
ATOM   386  C  CA  . GLU A 1 50  ? 56.35400 51.26200 45.73500 1.000 15.49849 ?  50  GLU A CA  1 
ATOM   387  C  C   . GLU A 1 50  ? 56.91500 52.47800 46.46400 1.000 15.89239 ?  50  GLU A C   1 
ATOM   388  O  O   . GLU A 1 50  ? 58.10900 52.51800 46.79200 1.000 19.19083 ?  50  GLU A O   1 
ATOM   389  C  CB  . GLU A 1 50  ? 56.32600 51.49300 44.22400 1.000 18.17738 ?  50  GLU A CB  1 
ATOM   390  C  CG  . GLU A 1 50  ? 55.86000 50.26500 43.41600 1.000 18.20450 ?  50  GLU A CG  1 
ATOM   391  C  CD  . GLU A 1 50  ? 54.34300 50.07200 43.35400 1.000 20.32446 ?  50  GLU A CD  1 
ATOM   392  O  OE1 . GLU A 1 50  ? 53.58200 50.95900 43.81900 1.000 16.65021 ?  50  GLU A OE1 1 
ATOM   393  O  OE2 . GLU A 1 50  ? 53.90900 49.01100 42.82200 1.000 18.09317 -1 50  GLU A OE2 1 
ATOM   394  N  N   . ARG A 1 51  ? 56.06000 53.47200 46.72300 1.000 15.98233 ?  51  ARG A N   1 
ATOM   395  C  CA  . ARG A 1 51  ? 56.46400 54.65200 47.48800 1.000 18.04954 ?  51  ARG A CA  1 
ATOM   396  C  C   . ARG A 1 51  ? 56.71000 54.30400 48.94800 1.000 19.07209 ?  51  ARG A C   1 
ATOM   397  O  O   . ARG A 1 51  ? 57.67300 54.78800 49.55900 1.000 19.78632 ?  51  ARG A O   1 
ATOM   398  C  CB  . ARG A 1 51  ? 55.36100 55.70300 47.36300 1.000 21.30080 ?  51  ARG A CB  1 
ATOM   399  C  CG  . ARG A 1 51  ? 55.64100 57.03600 48.03900 1.000 26.98087 ?  51  ARG A CG  1 
ATOM   400  C  CD  . ARG A 1 51  ? 56.66700 57.85200 47.26400 1.000 34.47258 ?  51  ARG A CD  1 
ATOM   401  N  NE  . ARG A 1 51  ? 56.22700 58.15800 45.90600 1.000 36.42779 ?  51  ARG A NE  1 
ATOM   402  C  CZ  . ARG A 1 51  ? 57.00500 58.69100 44.97400 1.000 47.54780 ?  51  ARG A CZ  1 
ATOM   403  N  NH1 . ARG A 1 51  ? 58.25900 59.03300 45.23400 1.000 45.69720 ?  51  ARG A NH1 1 
ATOM   404  N  NH2 . ARG A 1 51  ? 56.51900 58.87400 43.74600 1.000 42.39649 ?  51  ARG A NH2 1 
ATOM   405  N  N   . LEU A 1 52  ? 55.86000 53.46000 49.53000 1.000 17.14912 ?  52  LEU A N   1 
ATOM   406  C  CA  . LEU A 1 52  ? 56.02600 53.12500 50.94400 1.000 15.61834 ?  52  LEU A CA  1 
ATOM   407  C  C   . LEU A 1 52  ? 57.34900 52.41400 51.21300 1.000 16.81287 ?  52  LEU A C   1 
ATOM   408  O  O   . LEU A 1 52  ? 57.93500 52.59000 52.28900 1.000 17.23819 ?  52  LEU A O   1 
ATOM   409  C  CB  . LEU A 1 52  ? 54.88100 52.22100 51.40600 1.000 14.56248 ?  52  LEU A CB  1 
ATOM   410  C  CG  . LEU A 1 52  ? 53.48700 52.81100 51.59900 1.000 17.64922 ?  52  LEU A CG  1 
ATOM   411  C  CD1 . LEU A 1 52  ? 52.45500 51.69000 51.74900 1.000 17.81177 ?  52  LEU A CD1 1 
ATOM   412  C  CD2 . LEU A 1 52  ? 53.46200 53.73700 52.82000 1.000 19.02749 ?  52  LEU A CD2 1 
ATOM   413  N  N   . THR A 1 53  ? 57.82000 51.58800 50.27100 1.000 18.33760 ?  53  THR A N   1 
ATOM   414  C  CA  . THR A 1 53  ? 58.89200 50.63900 50.53900 1.000 18.50204 ?  53  THR A CA  1 
ATOM   415  C  C   . THR A 1 53  ? 60.16400 50.90900 49.76400 1.000 17.83926 ?  53  THR A C   1 
ATOM   416  O  O   . THR A 1 53  ? 61.19700 50.32600 50.10300 1.000 20.33980 ?  53  THR A O   1 
ATOM   417  C  CB  . THR A 1 53  ? 58.45800 49.21100 50.17700 1.000 18.77551 ?  53  THR A CB  1 
ATOM   418  O  OG1 . THR A 1 53  ? 58.13400 49.16500 48.78200 1.000 18.39243 ?  53  THR A OG1 1 
ATOM   419  C  CG2 . THR A 1 53  ? 57.24400 48.76400 51.01200 1.000 21.69484 ?  53  THR A CG2 1 
ATOM   420  N  N   . GLY A 1 54  ? 60.11600 51.72700 48.72000 1.000 19.77929 ?  54  GLY A N   1 
ATOM   421  C  CA  . GLY A 1 54  ? 61.24300 51.85700 47.81500 1.000 21.23049 ?  54  GLY A CA  1 
ATOM   422  C  C   . GLY A 1 54  ? 61.39200 50.75300 46.78300 1.000 25.93044 ?  54  GLY A C   1 
ATOM   423  O  O   . GLY A 1 54  ? 62.34800 50.79400 45.99600 1.000 30.74792 ?  54  GLY A O   1 
ATOM   424  N  N   . LEU A 1 55  ? 60.49400 49.79700 46.73500 1.000 20.65047 ?  55  LEU A N   1 
ATOM   425  C  CA  . LEU A 1 55  ? 60.55800 48.74900 45.71300 1.000 24.80950 ?  55  LEU A CA  1 
ATOM   426  C  C   . LEU A 1 55  ? 60.50800 49.33900 44.30700 1.000 28.12968 ?  55  LEU A C   1 
ATOM   427  O  O   . LEU A 1 55  ? 59.74500 50.24700 44.05100 1.000 24.18802 ?  55  LEU A O   1 
ATOM   428  C  CB  . LEU A 1 55  ? 59.47300 47.70000 45.93400 1.000 24.97327 ?  55  LEU A CB  1 
ATOM   429  C  CG  . LEU A 1 55  ? 59.76600 46.70300 47.05000 1.000 26.14762 ?  55  LEU A CG  1 
ATOM   430  C  CD1 . LEU A 1 55  ? 58.52300 45.92600 47.41600 1.000 31.71554 ?  55  LEU A CD1 1 
ATOM   431  C  CD2 . LEU A 1 55  ? 60.88700 45.76200 46.65000 1.000 31.72538 ?  55  LEU A CD2 1 
ATOM   432  N  N   . GLU A 1 56  ? 61.32800 48.79500 43.41000 1.000 27.58993 ?  56  GLU A N   1 
ATOM   433  C  CA  . GLU A 1 56  ? 61.48300 49.31100 42.05800 1.000 31.88321 ?  56  GLU A CA  1 
ATOM   434  C  C   . GLU A 1 56  ? 60.55500 48.57500 41.11100 1.000 26.33583 ?  56  GLU A C   1 
ATOM   435  O  O   . GLU A 1 56  ? 60.06700 47.48700 41.42800 1.000 27.70812 ?  56  GLU A O   1 
ATOM   436  C  CB  . GLU A 1 56  ? 62.91500 49.07300 41.58400 1.000 34.40402 ?  56  GLU A CB  1 
ATOM   437  C  CG  . GLU A 1 56  ? 63.98500 49.52400 42.53700 1.000 44.78561 ?  56  GLU A CG  1 
ATOM   438  C  CD  . GLU A 1 56  ? 64.60700 50.82500 42.11500 1.000 49.89143 ?  56  GLU A CD  1 
ATOM   439  O  OE1 . GLU A 1 56  ? 63.85700 51.72100 41.66400 1.000 52.97840 ?  56  GLU A OE1 1 
ATOM   440  O  OE2 . GLU A 1 56  ? 65.84600 50.94400 42.22500 1.000 59.43971 -1 56  GLU A OE2 1 
ATOM   441  N  N   . PRO A 1 57  ? 60.33000 49.11700 39.91400 1.000 27.24826 ?  57  PRO A N   1 
ATOM   442  C  CA  . PRO A 1 57  ? 59.53100 48.38900 38.91800 1.000 27.51057 ?  57  PRO A CA  1 
ATOM   443  C  C   . PRO A 1 57  ? 60.10500 47.00100 38.66900 1.000 23.79008 ?  57  PRO A C   1 
ATOM   444  O  O   . PRO A 1 57  ? 61.32000 46.82500 38.53500 1.000 24.87104 ?  57  PRO A O   1 
ATOM   445  C  CB  . PRO A 1 57  ? 59.63400 49.28000 37.67700 1.000 29.21139 ?  57  PRO A CB  1 
ATOM   446  C  CG  . PRO A 1 57  ? 59.84300 50.66700 38.23300 1.000 28.62895 ?  57  PRO A CG  1 
ATOM   447  C  CD  . PRO A 1 57  ? 60.71500 50.46100 39.44300 1.000 31.32956 ?  57  PRO A CD  1 
ATOM   448  N  N   . GLY A 1 58  ? 59.21900 46.00200 38.63500 1.000 24.22029 ?  58  GLY A N   1 
ATOM   449  C  CA  . GLY A 1 58  ? 59.61900 44.61700 38.44800 1.000 23.05025 ?  58  GLY A CA  1 
ATOM   450  C  C   . GLY A 1 58  ? 59.87300 43.83100 39.71800 1.000 26.40129 ?  58  GLY A C   1 
ATOM   451  O  O   . GLY A 1 58  ? 60.02800 42.59600 39.64800 1.000 26.44138 ?  58  GLY A O   1 
ATOM   452  N  N   . GLU A 1 59  ? 59.94200 44.48800 40.87000 1.000 21.25298 ?  59  GLU A N   1 
ATOM   453  C  CA  . GLU A 1 59  ? 60.21100 43.79400 42.11900 1.000 22.46035 ?  59  GLU A CA  1 
ATOM   454  C  C   . GLU A 1 59  ? 58.95100 43.32300 42.85200 1.000 18.06452 ?  59  GLU A C   1 
ATOM   455  O  O   . GLU A 1 59  ? 59.02300 42.46700 43.70300 1.000 19.69574 ?  59  GLU A O   1 
ATOM   456  C  CB  . GLU A 1 59  ? 61.02100 44.69300 43.05800 1.000 21.52022 ?  59  GLU A CB  1 
ATOM   457  C  CG  . GLU A 1 59  ? 62.37600 45.07100 42.47100 1.000 29.31333 ?  59  GLU A CG  1 
ATOM   458  C  CD  . GLU A 1 59  ? 63.29600 45.77300 43.45500 1.000 37.93436 ?  59  GLU A CD  1 
ATOM   459  O  OE1 . GLU A 1 59  ? 62.89700 46.78800 44.03900 1.000 29.66997 ?  59  GLU A OE1 1 
ATOM   460  O  OE2 . GLU A 1 59  ? 64.43600 45.30800 43.63700 1.000 40.88240 -1 59  GLU A OE2 1 
ATOM   461  N  N   . LEU A 1 60  ? 57.81400 43.86900 42.47000 1.000 18.88049 ?  60  LEU A N   1 
ATOM   462  C  CA  . LEU A 1 60  ? 56.57000 43.57400 43.16100 1.000 17.35740 ?  60  LEU A CA  1 
ATOM   463  C  C   . LEU A 1 60  ? 55.42600 43.08100 42.30700 1.000 21.92738 ?  60  LEU A C   1 
ATOM   464  O  O   . LEU A 1 60  ? 55.07200 43.76900 41.37000 1.000 28.56816 ?  60  LEU A O   1 
ATOM   465  C  CB  . LEU A 1 60  ? 56.06400 44.87100 43.81200 1.000 20.47955 ?  60  LEU A CB  1 
ATOM   466  C  CG  . LEU A 1 60  ? 55.11800 44.85600 45.00200 1.000 27.12176 ?  60  LEU A CG  1 
ATOM   467  C  CD1 . LEU A 1 60  ? 55.58000 43.88300 46.06900 1.000 23.06728 ?  60  LEU A CD1 1 
ATOM   468  C  CD2 . LEU A 1 60  ? 55.03400 46.26200 45.57100 1.000 28.98531 ?  60  LEU A CD2 1 
ATOM   469  N  N   . PHE A 1 61  ? 54.83200 41.95100 42.62900 1.000 12.73830 ?  61  PHE A N   1 
ATOM   470  C  CA  . PHE A 1 61  ? 53.62600 41.46500 41.97700 1.000 12.24255 ?  61  PHE A CA  1 
ATOM   471  C  C   . PHE A 1 61  ? 52.53600 42.01300 42.89700 1.000 11.09214 ?  61  PHE A C   1 
ATOM   472  O  O   . PHE A 1 61  ? 52.71900 42.03400 44.08300 1.000 12.96082 ?  61  PHE A O   1 
ATOM   473  C  CB  . PHE A 1 61  ? 53.65600 39.94600 41.90800 1.000 11.50113 ?  61  PHE A CB  1 
ATOM   474  C  CG  . PHE A 1 61  ? 52.79600 39.32800 40.85200 1.000 14.56808 ?  61  PHE A CG  1 
ATOM   475  C  CD1 . PHE A 1 61  ? 53.04000 39.54800 39.51800 1.000 12.58303 ?  61  PHE A CD1 1 
ATOM   476  C  CD2 . PHE A 1 61  ? 51.79400 38.45200 41.20600 1.000 13.70127 ?  61  PHE A CD2 1 
ATOM   477  C  CE1 . PHE A 1 61  ? 52.26500 38.94500 38.55300 1.000 13.79944 ?  61  PHE A CE1 1 
ATOM   478  C  CE2 . PHE A 1 61  ? 51.01300 37.85000 40.24800 1.000 13.95139 ?  61  PHE A CE2 1 
ATOM   479  C  CZ  . PHE A 1 61  ? 51.25000 38.09700 38.91700 1.000 14.40022 ?  61  PHE A CZ  1 
ATOM   480  N  N   . VAL A 1 62  ? 51.39500 42.43100 42.33300 1.000 11.09052 ?  62  VAL A N   1 
ATOM   481  C  CA  . VAL A 1 62  ? 50.42100 43.16500 43.14700 1.000 12.39859 ?  62  VAL A CA  1 
ATOM   482  C  C   . VAL A 1 62  ? 48.99600 42.65900 42.91600 1.000 11.35311 ?  62  VAL A C   1 
ATOM   483  O  O   . VAL A 1 62  ? 48.54700 42.54400 41.76600 1.000 12.79939 ?  62  VAL A O   1 
ATOM   484  C  CB  . VAL A 1 62  ? 50.48600 44.67900 42.85800 1.000 10.40209 ?  62  VAL A CB  1 
ATOM   485  C  CG1 . VAL A 1 62  ? 49.42100 45.40900 43.66200 1.000 12.92113 ?  62  VAL A CG1 1 
ATOM   486  C  CG2 . VAL A 1 62  ? 51.87300 45.25000 43.13300 1.000 13.69070 ?  62  VAL A CG2 1 
ATOM   487  N  N   . HIS A 1 63  ? 48.24600 42.45100 44.00700 1.000 10.79815 ?  63  HIS A N   1 
ATOM   488  C  CA  . HIS A 1 63  ? 46.78900 42.32900 43.94200 1.000 10.16784 ?  63  HIS A CA  1 
ATOM   489  C  C   . HIS A 1 63  ? 46.16900 43.38400 44.84200 1.000 9.69085  ?  63  HIS A C   1 
ATOM   490  O  O   . HIS A 1 63  ? 46.66500 43.61900 45.94500 1.000 10.62684 ?  63  HIS A O   1 
ATOM   491  C  CB  . HIS A 1 63  ? 46.32400 40.94500 44.43900 1.000 12.09906 ?  63  HIS A CB  1 
ATOM   492  C  CG  . HIS A 1 63  ? 44.83500 40.78100 44.50700 1.000 9.87530  ?  63  HIS A CG  1 
ATOM   493  N  ND1 . HIS A 1 63  ? 44.04000 40.79500 43.37400 1.000 11.38600 ?  63  HIS A ND1 1 
ATOM   494  C  CD2 . HIS A 1 63  ? 43.99300 40.60000 45.55500 1.000 9.88704  ?  63  HIS A CD2 1 
ATOM   495  C  CE1 . HIS A 1 63  ? 42.77400 40.61300 43.72700 1.000 12.06729 ?  63  HIS A CE1 1 
ATOM   496  N  NE2 . HIS A 1 63  ? 42.71800 40.49700 45.04500 1.000 10.07486 ?  63  HIS A NE2 1 
ATOM   497  N  N   . ARG A 1 64  ? 45.08400 44.01200 44.39600 1.000 9.53437  ?  64  ARG A N   1 
ATOM   498  C  CA  . ARG A 1 64  ? 44.34800 44.92600 45.26900 1.000 10.07135 ?  64  ARG A CA  1 
ATOM   499  C  C   . ARG A 1 64  ? 42.85600 44.68800 45.12600 1.000 10.11258 ?  64  ARG A C   1 
ATOM   500  O  O   . ARG A 1 64  ? 42.35200 44.48100 44.02000 1.000 10.94354 ?  64  ARG A O   1 
ATOM   501  C  CB  . ARG A 1 64  ? 44.62600 46.38100 44.91700 1.000 10.80559 ?  64  ARG A CB  1 
ATOM   502  C  CG  . ARG A 1 64  ? 46.06000 46.79900 45.25200 1.000 10.73058 ?  64  ARG A CG  1 
ATOM   503  C  CD  . ARG A 1 64  ? 46.25500 48.28500 44.95300 1.000 11.42238 ?  64  ARG A CD  1 
ATOM   504  N  NE  . ARG A 1 64  ? 47.61200 48.68800 45.26300 1.000 12.29172 ?  64  ARG A NE  1 
ATOM   505  C  CZ  . ARG A 1 64  ? 48.03900 48.96300 46.48300 1.000 13.09963 ?  64  ARG A CZ  1 
ATOM   506  N  NH1 . ARG A 1 64  ? 47.22300 48.91900 47.52800 1.000 12.40442 ?  64  ARG A NH1 1 
ATOM   507  N  NH2 . ARG A 1 64  ? 49.31200 49.29500 46.65800 1.000 15.74859 ?  64  ARG A NH2 1 
ATOM   508  N  N   . ASN A 1 65  ? 42.15000 44.73400 46.25600 1.000 9.89521  ?  65  ASN A N   1 
ATOM   509  C  CA  . ASN A 1 65  ? 40.70000 44.57900 46.29300 1.000 10.41657 ?  65  ASN A CA  1 
ATOM   510  C  C   . ASN A 1 65  ? 40.20000 45.42600 47.45900 1.000 10.42973 ?  65  ASN A C   1 
ATOM   511  O  O   . ASN A 1 65  ? 41.00300 45.98300 48.21900 1.000 10.80136 ?  65  ASN A O   1 
ATOM   512  C  CB  . ASN A 1 65  ? 40.30100 43.09500 46.36300 1.000 10.07910 ?  65  ASN A CB  1 
ATOM   513  C  CG  . ASN A 1 65  ? 40.66700 42.45600 47.68100 1.000 11.99765 ?  65  ASN A CG  1 
ATOM   514  O  OD1 . ASN A 1 65  ? 40.32500 42.97200 48.74800 1.000 13.20654 ?  65  ASN A OD1 1 
ATOM   515  N  ND2 . ASN A 1 65  ? 41.36200 41.32900 47.61800 1.000 10.95558 ?  65  ASN A ND2 1 
ATOM   516  N  N   . VAL A 1 66  ? 38.88100 45.53600 47.61000 1.000 10.15259 ?  66  VAL A N   1 
ATOM   517  C  CA  . VAL A 1 66  ? 38.35600 46.40800 48.66100 1.000 9.51478  ?  66  VAL A CA  1 
ATOM   518  C  C   . VAL A 1 66  ? 38.65200 45.81300 50.03500 1.000 11.48641 ?  66  VAL A C   1 
ATOM   519  O  O   . VAL A 1 66  ? 38.17300 44.72200 50.37300 1.000 11.51721 ?  66  VAL A O   1 
ATOM   520  C  CB  . VAL A 1 66  ? 36.86300 46.69300 48.47000 1.000 10.34158 ?  66  VAL A CB  1 
ATOM   521  C  CG1 . VAL A 1 66  ? 36.38800 47.62600 49.60200 1.000 13.56960 ?  66  VAL A CG1 1 
ATOM   522  C  CG2 . VAL A 1 66  ? 36.59600 47.34700 47.15100 1.000 12.42826 ?  66  VAL A CG2 1 
ATOM   523  N  N   . ALA A 1 67  ? 39.45000 46.53800 50.83300 1.000 10.73407 ?  67  ALA A N   1 
ATOM   524  C  CA  . ALA A 1 67  ? 39.83900 46.15800 52.19300 1.000 10.55380 ?  67  ALA A CA  1 
ATOM   525  C  C   . ALA A 1 67  ? 40.78800 44.97100 52.23800 1.000 9.66092  ?  67  ALA A C   1 
ATOM   526  O  O   . ALA A 1 67  ? 40.90200 44.31300 53.28400 1.000 11.30948 ?  67  ALA A O   1 
ATOM   527  C  CB  . ALA A 1 67  ? 38.63800 45.95300 53.12200 1.000 10.70090 ?  67  ALA A CB  1 
ATOM   528  N  N   . ASN A 1 68  ? 41.53800 44.72100 51.16200 1.000 9.58424  ?  68  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 68  ? 42.67900 43.80000 51.20100 1.000 9.76601  ?  68  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 68  ? 42.32200 42.44600 51.79600 1.000 9.05672  ?  68  ASN A C   1 
ATOM   531  O  O   . ASN A 1 68  ? 42.98900 41.93400 52.71000 1.000 10.07705 ?  68  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 68  ? 43.93700 44.41700 51.85600 1.000 9.35834  ?  68  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 68  ? 43.67300 45.06900 53.21300 1.000 10.38588 ?  68  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 68  ? 43.40600 46.28200 53.30000 1.000 11.73204 ?  68  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 68  ? 43.77700 44.26700 54.29200 1.000 12.51684 ?  68  ASN A ND2 1 
ATOM   536  N  N   . LEU A 1 69  ? 41.27700 41.83800 51.23400 1.000 9.65962  ?  69  LEU A N   1 
ATOM   537  C  CA  . LEU A 1 69  ? 40.79900 40.54600 51.72500 1.000 9.62278  ?  69  LEU A CA  1 
ATOM   538  C  C   . LEU A 1 69  ? 41.43000 39.37700 50.98400 1.000 11.19424 ?  69  LEU A C   1 
ATOM   539  O  O   . LEU A 1 69  ? 41.72600 39.44400 49.78300 1.000 9.88238  ?  69  LEU A O   1 
ATOM   540  C  CB  . LEU A 1 69  ? 39.28100 40.43300 51.58700 1.000 10.39492 ?  69  LEU A CB  1 
ATOM   541  C  CG  . LEU A 1 69  ? 38.47200 41.48900 52.34500 1.000 9.62034  ?  69  LEU A CG  1 
ATOM   542  C  CD1 . LEU A 1 69  ? 37.00600 41.12300 52.28400 1.000 12.28881 ?  69  LEU A CD1 1 
ATOM   543  C  CD2 . LEU A 1 69  ? 38.90800 41.62500 53.81700 1.000 11.32918 ?  69  LEU A CD2 1 
ATOM   544  N  N   . VAL A 1 70  ? 41.62200 38.28800 51.71600 1.000 9.50350  ?  70  VAL A N   1 
ATOM   545  C  CA  . VAL A 1 70  ? 41.91300 36.98100 51.12900 1.000 9.04787  ?  70  VAL A CA  1 
ATOM   546  C  C   . VAL A 1 70  ? 40.75700 36.07700 51.54800 1.000 9.43522  ?  70  VAL A C   1 
ATOM   547  O  O   . VAL A 1 70  ? 40.80500 35.39300 52.58300 1.000 11.24370 ?  70  VAL A O   1 
ATOM   548  C  CB  . VAL A 1 70  ? 43.26600 36.40600 51.57600 1.000 10.63042 ?  70  VAL A CB  1 
ATOM   549  C  CG1 . VAL A 1 70  ? 43.48200 35.00000 50.98200 1.000 11.37550 ?  70  VAL A CG1 1 
ATOM   550  C  CG2 . VAL A 1 70  ? 44.43700 37.34700 51.19400 1.000 10.48192 ?  70  VAL A CG2 1 
ATOM   551  N  N   . ILE A 1 71  ? 39.67900 36.08900 50.76300 1.000 9.57966  ?  71  ILE A N   1 
ATOM   552  C  CA  . ILE A 1 71  ? 38.49800 35.28400 51.06600 1.000 11.09788 ?  71  ILE A CA  1 
ATOM   553  C  C   . ILE A 1 71  ? 38.79000 33.84900 50.67000 1.000 10.66382 ?  71  ILE A C   1 
ATOM   554  O  O   . ILE A 1 71  ? 39.43600 33.59600 49.64100 1.000 10.01643 ?  71  ILE A O   1 
ATOM   555  C  CB  . ILE A 1 71  ? 37.26800 35.85200 50.32800 1.000 8.89276  ?  71  ILE A CB  1 
ATOM   556  C  CG1 . ILE A 1 71  ? 36.94300 37.26400 50.85100 1.000 11.54306 ?  71  ILE A CG1 1 
ATOM   557  C  CG2 . ILE A 1 71  ? 36.07400 34.92500 50.42200 1.000 11.73460 ?  71  ILE A CG2 1 
ATOM   558  C  CD1 . ILE A 1 71  ? 36.04000 38.04700 49.89800 1.000 11.51982 ?  71  ILE A CD1 1 
ATOM   559  N  N   . HIS A 1 72  ? 38.34300 32.89600 51.50100 1.000 10.96980 ?  72  HIS A N   1 
ATOM   560  C  CA  . HIS A 1 72  ? 38.76400 31.51500 51.28700 1.000 11.00905 ?  72  HIS A CA  1 
ATOM   561  C  C   . HIS A 1 72  ? 38.45500 31.05300 49.87900 1.000 10.25485 ?  72  HIS A C   1 
ATOM   562  O  O   . HIS A 1 72  ? 39.17800 30.22000 49.31700 1.000 10.85104 ?  72  HIS A O   1 
ATOM   563  C  CB  . HIS A 1 72  ? 38.00900 30.56200 52.21000 1.000 11.70231 ?  72  HIS A CB  1 
ATOM   564  C  CG  . HIS A 1 72  ? 38.19100 30.80900 53.68300 1.000 10.68580 ?  72  HIS A CG  1 
ATOM   565  N  ND1 . HIS A 1 72  ? 39.42800 30.93100 54.29800 1.000 11.78708 ?  72  HIS A ND1 1 
ATOM   566  C  CD2 . HIS A 1 72  ? 37.26800 30.88800 54.67200 1.000 10.90968 ?  72  HIS A CD2 1 
ATOM   567  C  CE1 . HIS A 1 72  ? 39.24700 31.07900 55.60500 1.000 13.27429 ?  72  HIS A CE1 1 
ATOM   568  N  NE2 . HIS A 1 72  ? 37.94700 31.06800 55.85300 1.000 13.21048 ?  72  HIS A NE2 1 
ATOM   569  N  N   . THR A 1 73  ? 37.37200 31.56200 49.29500 1.000 10.09764 ?  73  THR A N   1 
ATOM   570  C  CA  . THR A 1 73  ? 36.86800 31.08200 48.01100 1.000 9.84837  ?  73  THR A CA  1 
ATOM   571  C  C   . THR A 1 73  ? 36.87900 32.14900 46.92400 1.000 11.03257 ?  73  THR A C   1 
ATOM   572  O  O   . THR A 1 73  ? 36.13100 32.02600 45.95500 1.000 12.01308 ?  73  THR A O   1 
ATOM   573  C  CB  . THR A 1 73  ? 35.46300 30.51000 48.18800 1.000 10.51468 ?  73  THR A CB  1 
ATOM   574  O  OG1 . THR A 1 73  ? 34.69500 31.42700 48.95700 1.000 11.80134 ?  73  THR A OG1 1 
ATOM   575  C  CG2 . THR A 1 73  ? 35.52500 29.17900 48.93700 1.000 11.49896 ?  73  THR A CG2 1 
ATOM   576  N  N   . ASP A 1 74  ? 37.71200 33.17600 47.05200 1.000 10.63198 ?  74  ASP A N   1 
ATOM   577  C  CA  . ASP A 1 74  ? 37.84100 34.18400 45.98500 1.000 9.12444  ?  74  ASP A CA  1 
ATOM   578  C  C   . ASP A 1 74  ? 38.90600 33.72700 45.00700 1.000 11.21320 ?  74  ASP A C   1 
ATOM   579  O  O   . ASP A 1 74  ? 40.10700 33.87700 45.26400 1.000 11.08330 ?  74  ASP A O   1 
ATOM   580  C  CB  . ASP A 1 74  ? 38.21800 35.55500 46.54900 1.000 10.41001 ?  74  ASP A CB  1 
ATOM   581  C  CG  . ASP A 1 74  ? 38.57300 36.54000 45.43600 1.000 11.82082 ?  74  ASP A CG  1 
ATOM   582  O  OD1 . ASP A 1 74  ? 37.96800 36.41700 44.33200 1.000 15.08659 ?  74  ASP A OD1 1 
ATOM   583  O  OD2 . ASP A 1 74  ? 39.46600 37.37900 45.62600 1.000 13.03176 -1 74  ASP A OD2 1 
ATOM   584  N  N   . LEU A 1 75  ? 38.45700 33.22900 43.84400 1.000 10.14246 ?  75  LEU A N   1 
ATOM   585  C  CA  . LEU A 1 75  ? 39.40000 32.72200 42.86200 1.000 10.35115 ?  75  LEU A CA  1 
ATOM   586  C  C   . LEU A 1 75  ? 40.25400 33.82000 42.22900 1.000 9.96149  ?  75  LEU A C   1 
ATOM   587  O  O   . LEU A 1 75  ? 41.33400 33.51000 41.71800 1.000 11.59873 ?  75  LEU A O   1 
ATOM   588  C  CB  . LEU A 1 75  ? 38.64900 31.90300 41.79400 1.000 11.98811 ?  75  LEU A CB  1 
ATOM   589  C  CG  . LEU A 1 75  ? 39.52100 31.10100 40.83700 1.000 12.43583 ?  75  LEU A CG  1 
ATOM   590  C  CD1 . LEU A 1 75  ? 40.52500 30.22800 41.58500 1.000 13.17466 ?  75  LEU A CD1 1 
ATOM   591  C  CD2 . LEU A 1 75  ? 38.60000 30.23200 39.94400 1.000 13.68026 ?  75  LEU A CD2 1 
ATOM   592  N  N   . ASN A 1 76  ? 39.82400 35.08700 42.25200 1.000 10.28321 ?  76  ASN A N   1 
ATOM   593  C  CA  . ASN A 1 76  ? 40.67300 36.15600 41.72400 1.000 9.70087  ?  76  ASN A CA  1 
ATOM   594  C  C   . ASN A 1 76  ? 41.94900 36.25500 42.55500 1.000 10.12405 ?  76  ASN A C   1 
ATOM   595  O  O   . ASN A 1 76  ? 43.05500 36.04300 42.04900 1.000 10.85182 ?  76  ASN A O   1 
ATOM   596  C  CB  . ASN A 1 76  ? 39.86000 37.46800 41.71700 1.000 10.37284 ?  76  ASN A CB  1 
ATOM   597  C  CG  . ASN A 1 76  ? 40.63200 38.67200 41.16600 1.000 10.17125 ?  76  ASN A CG  1 
ATOM   598  O  OD1 . ASN A 1 76  ? 41.84400 38.78000 41.34000 1.000 12.07610 ?  76  ASN A OD1 1 
ATOM   599  N  ND2 . ASN A 1 76  ? 39.92400 39.60400 40.55700 1.000 10.46752 ?  76  ASN A ND2 1 
ATOM   600  N  N   . CYS A 1 77  ? 41.80900 36.51300 43.85600 1.000 10.40744 ?  77  CYS A N   1 
ATOM   601  C  CA  . CYS A 1 77  ? 42.99400 36.58400 44.71300 1.000 10.49962 ?  77  CYS A CA  1 
ATOM   602  C  C   . CYS A 1 77  ? 43.75000 35.25700 44.75200 1.000 10.21775 ?  77  CYS A C   1 
ATOM   603  O  O   . CYS A 1 77  ? 44.98700 35.24600 44.69500 1.000 12.30376 ?  77  CYS A O   1 
ATOM   604  C  CB  . CYS A 1 77  ? 42.58400 37.04300 46.11400 1.000 11.26963 ?  77  CYS A CB  1 
ATOM   605  S  SG  . CYS A 1 77  ? 43.99300 37.23500 47.22800 1.000 12.38170 ?  77  CYS A SG  1 
ATOM   606  N  N   . LEU A 1 78  ? 43.04200 34.12600 44.86200 1.000 10.57187 ?  78  LEU A N   1 
ATOM   607  C  CA  . LEU A 1 78  ? 43.73900 32.83900 44.90200 1.000 10.99999 ?  78  LEU A CA  1 
ATOM   608  C  C   . LEU A 1 78  ? 44.55700 32.59800 43.63500 1.000 11.02242 ?  78  LEU A C   1 
ATOM   609  O  O   . LEU A 1 78  ? 45.62600 31.98800 43.69900 1.000 12.18655 ?  78  LEU A O   1 
ATOM   610  C  CB  . LEU A 1 78  ? 42.74700 31.68700 45.10500 1.000 12.15545 ?  78  LEU A CB  1 
ATOM   611  C  CG  . LEU A 1 78  ? 41.99500 31.61500 46.43800 1.000 14.75424 ?  78  LEU A CG  1 
ATOM   612  C  CD1 . LEU A 1 78  ? 40.99400 30.45500 46.35600 1.000 17.19637 ?  78  LEU A CD1 1 
ATOM   613  C  CD2 . LEU A 1 78  ? 42.97100 31.36600 47.58600 1.000 17.26210 ?  78  LEU A CD2 1 
ATOM   614  N  N   . SER A 1 79  ? 44.05700 33.04700 42.47400 1.000 10.28248 ?  79  SER A N   1 
ATOM   615  C  CA  . SER A 1 79  ? 44.80700 32.87200 41.22700 1.000 10.33134 ?  79  SER A CA  1 
ATOM   616  C  C   . SER A 1 79  ? 46.06300 33.73600 41.20800 1.000 10.10467 ?  79  SER A C   1 
ATOM   617  O  O   . SER A 1 79  ? 47.11200 33.28800 40.72400 1.000 10.89641 ?  79  SER A O   1 
ATOM   618  C  CB  . SER A 1 79  ? 43.90800 33.20400 40.02700 1.000 10.19112 ?  79  SER A CB  1 
ATOM   619  O  OG  . SER A 1 79  ? 42.84500 32.23900 39.90900 1.000 11.55949 ?  79  SER A OG  1 
ATOM   620  N  N   . VAL A 1 80  ? 45.98200 34.96700 41.73000 1.000 9.77811  ?  80  VAL A N   1 
ATOM   621  C  CA  . VAL A 1 80  ? 47.19200 35.79000 41.87100 1.000 11.16924 ?  80  VAL A CA  1 
ATOM   622  C  C   . VAL A 1 80  ? 48.20900 35.07900 42.75200 1.000 11.16402 ?  80  VAL A C   1 
ATOM   623  O  O   . VAL A 1 80  ? 49.40100 34.99100 42.41100 1.000 10.10531 ?  80  VAL A O   1 
ATOM   624  C  CB  . VAL A 1 80  ? 46.85900 37.18000 42.43800 1.000 10.90974 ?  80  VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 80  ? 48.16200 37.96700 42.59700 1.000 13.62027 ?  80  VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 80  ? 45.91100 37.94700 41.52000 1.000 11.60050 ?  80  VAL A CG2 1 
ATOM   627  N  N   . VAL A 1 81  ? 47.74700 34.58000 43.91200 1.000 10.57654 ?  81  VAL A N   1 
ATOM   628  C  CA  . VAL A 1 81  ? 48.62700 33.91100 44.87100 1.000 10.77275 ?  81  VAL A CA  1 
ATOM   629  C  C   . VAL A 1 81  ? 49.25900 32.66300 44.26300 1.000 11.29729 ?  81  VAL A C   1 
ATOM   630  O  O   . VAL A 1 81  ? 50.47200 32.44800 44.37500 1.000 12.31886 ?  81  VAL A O   1 
ATOM   631  C  CB  . VAL A 1 81  ? 47.86200 33.57900 46.16900 1.000 10.85606 ?  81  VAL A CB  1 
ATOM   632  C  CG1 . VAL A 1 81  ? 48.68900 32.67400 47.08000 1.000 12.09494 ?  81  VAL A CG1 1 
ATOM   633  C  CG2 . VAL A 1 81  ? 47.48800 34.84000 46.91000 1.000 11.58956 ?  81  VAL A CG2 1 
ATOM   634  N  N   . GLN A 1 82  ? 48.45000 31.81700 43.62500 1.000 10.42503 ?  82  GLN A N   1 
ATOM   635  C  CA  . GLN A 1 82  ? 48.99200 30.58200 43.05500 1.000 11.07244 ?  82  GLN A CA  1 
ATOM   636  C  C   . GLN A 1 82  ? 50.00500 30.86300 41.95600 1.000 10.21782 ?  82  GLN A C   1 
ATOM   637  O  O   . GLN A 1 82  ? 51.06400 30.22500 41.89600 1.000 12.26805 ?  82  GLN A O   1 
ATOM   638  C  CB  . GLN A 1 82  ? 47.87200 29.67100 42.57300 1.000 10.24730 ?  82  GLN A CB  1 
ATOM   639  C  CG  . GLN A 1 82  ? 48.36600 28.29800 42.17200 1.000 11.90602 ?  82  GLN A CG  1 
ATOM   640  C  CD  . GLN A 1 82  ? 48.76700 28.18600 40.71200 1.000 11.61075 ?  82  GLN A CD  1 
ATOM   641  O  OE1 . GLN A 1 82  ? 48.25400 28.89900 39.83600 1.000 12.36912 ?  82  GLN A OE1 1 
ATOM   642  N  NE2 . GLN A 1 82  ? 49.67300 27.26600 40.43200 1.000 12.54805 ?  82  GLN A NE2 1 
ATOM   643  N  N   . TYR A 1 83  ? 49.71800 31.81600 41.07800 1.000 10.15135 ?  83  TYR A N   1 
ATOM   644  C  CA  . TYR A 1 83  ? 50.72200 32.17800 40.08300 1.000 9.94526  ?  83  TYR A CA  1 
ATOM   645  C  C   . TYR A 1 83  ? 51.98400 32.73300 40.74200 1.000 11.21654 ?  83  TYR A C   1 
ATOM   646  O  O   . TYR A 1 83  ? 53.11000 32.35500 40.37600 1.000 11.94849 ?  83  TYR A O   1 
ATOM   647  C  CB  . TYR A 1 83  ? 50.09600 33.18200 39.12500 1.000 11.62474 ?  83  TYR A CB  1 
ATOM   648  C  CG  . TYR A 1 83  ? 50.95600 33.59100 37.96100 1.000 12.68096 ?  83  TYR A CG  1 
ATOM   649  C  CD1 . TYR A 1 83  ? 51.04400 32.78500 36.83400 1.000 12.89588 ?  83  TYR A CD1 1 
ATOM   650  C  CD2 . TYR A 1 83  ? 51.61900 34.79500 37.96200 1.000 14.65355 ?  83  TYR A CD2 1 
ATOM   651  C  CE1 . TYR A 1 83  ? 51.80700 33.16200 35.75200 1.000 14.89318 ?  83  TYR A CE1 1 
ATOM   652  C  CE2 . TYR A 1 83  ? 52.39500 35.19100 36.87300 1.000 14.95217 ?  83  TYR A CE2 1 
ATOM   653  C  CZ  . TYR A 1 83  ? 52.47500 34.36700 35.77900 1.000 16.40382 ?  83  TYR A CZ  1 
ATOM   654  O  OH  . TYR A 1 83  ? 53.24600 34.74800 34.69000 1.000 17.73356 ?  83  TYR A OH  1 
ATOM   655  N  N   . ALA A 1 84  ? 51.82500 33.61100 41.73300 1.000 9.99331  ?  84  ALA A N   1 
ATOM   656  C  CA  . ALA A 1 84  ? 52.99000 34.17900 42.39800 1.000 11.42397 ?  84  ALA A CA  1 
ATOM   657  C  C   . ALA A 1 84  ? 53.81600 33.11300 43.10200 1.000 12.15961 ?  84  ALA A C   1 
ATOM   658  O  O   . ALA A 1 84  ? 55.04500 33.15700 43.04200 1.000 14.54158 ?  84  ALA A O   1 
ATOM   659  C  CB  . ALA A 1 84  ? 52.53000 35.23100 43.40800 1.000 12.71119 ?  84  ALA A CB  1 
ATOM   660  N  N   . VAL A 1 85  ? 53.16900 32.18500 43.81000 1.000 11.46831 ?  85  VAL A N   1 
ATOM   661  C  CA  . VAL A 1 85  ? 53.90000 31.21100 44.62000 1.000 11.70317 ?  85  VAL A CA  1 
ATOM   662  C  C   . VAL A 1 85  ? 54.45900 30.09300 43.74700 1.000 15.10821 ?  85  VAL A C   1 
ATOM   663  O  O   . VAL A 1 85  ? 55.63800 29.72900 43.86000 1.000 16.15719 ?  85  VAL A O   1 
ATOM   664  C  CB  . VAL A 1 85  ? 53.00100 30.68100 45.74800 1.000 13.20701 ?  85  VAL A CB  1 
ATOM   665  C  CG1 . VAL A 1 85  ? 53.68300 29.46900 46.42100 1.000 15.33288 ?  85  VAL A CG1 1 
ATOM   666  C  CG2 . VAL A 1 85  ? 52.70700 31.79600 46.78200 1.000 13.26101 ?  85  VAL A CG2 1 
ATOM   667  N  N   . ASP A 1 86  ? 53.62900 29.52400 42.87100 1.000 13.36851 ?  86  ASP A N   1 
ATOM   668  C  CA  . ASP A 1 86  ? 54.05400 28.34000 42.12400 1.000 12.83977 ?  86  ASP A CA  1 
ATOM   669  C  C   . ASP A 1 86  ? 54.82400 28.66100 40.85000 1.000 13.59894 ?  86  ASP A C   1 
ATOM   670  O  O   . ASP A 1 86  ? 55.69500 27.86800 40.46400 1.000 18.54576 ?  86  ASP A O   1 
ATOM   671  C  CB  . ASP A 1 86  ? 52.86800 27.43800 41.74700 1.000 14.64112 ?  86  ASP A CB  1 
ATOM   672  C  CG  . ASP A 1 86  ? 52.13900 26.82300 42.96200 1.000 16.23907 ?  86  ASP A CG  1 
ATOM   673  O  OD1 . ASP A 1 86  ? 52.59500 26.95400 44.11500 1.000 18.42288 ?  86  ASP A OD1 1 
ATOM   674  O  OD2 . ASP A 1 86  ? 51.09900 26.16500 42.73900 1.000 17.65917 -1 86  ASP A OD2 1 
ATOM   675  N  N   . VAL A 1 87  ? 54.50400 29.74700 40.16300 1.000 13.53854 ?  87  VAL A N   1 
ATOM   676  C  CA  . VAL A 1 87  ? 55.14000 30.07000 38.89400 1.000 14.50277 ?  87  VAL A CA  1 
ATOM   677  C  C   . VAL A 1 87  ? 56.25700 31.09200 39.07200 1.000 16.86936 ?  87  VAL A C   1 
ATOM   678  O  O   . VAL A 1 87  ? 57.39300 30.85800 38.66100 1.000 17.96442 ?  87  VAL A O   1 
ATOM   679  C  CB  . VAL A 1 87  ? 54.09600 30.52400 37.84700 1.000 15.04858 ?  87  VAL A CB  1 
ATOM   680  C  CG1 . VAL A 1 87  ? 54.75800 30.78600 36.48900 1.000 17.71199 ?  87  VAL A CG1 1 
ATOM   681  C  CG2 . VAL A 1 87  ? 52.99500 29.48300 37.70800 1.000 14.90595 ?  87  VAL A CG2 1 
ATOM   682  N  N   . LEU A 1 88  ? 55.96500 32.22600 39.71600 1.000 14.34471 ?  88  LEU A N   1 
ATOM   683  C  CA  . LEU A 1 88  ? 57.00700 33.22400 39.92200 1.000 13.29369 ?  88  LEU A CA  1 
ATOM   684  C  C   . LEU A 1 88  ? 57.91000 32.87600 41.09100 1.000 14.76758 ?  88  LEU A C   1 
ATOM   685  O  O   . LEU A 1 88  ? 59.04100 33.37800 41.15000 1.000 18.82509 ?  88  LEU A O   1 
ATOM   686  C  CB  . LEU A 1 88  ? 56.39000 34.60300 40.18100 1.000 15.21677 ?  88  LEU A CB  1 
ATOM   687  C  CG  . LEU A 1 88  ? 55.44100 35.09800 39.09400 1.000 16.20938 ?  88  LEU A CG  1 
ATOM   688  C  CD1 . LEU A 1 88  ? 54.90200 36.48200 39.47100 1.000 17.67925 ?  88  LEU A CD1 1 
ATOM   689  C  CD2 . LEU A 1 88  ? 56.15200 35.14000 37.74900 1.000 16.85392 ?  88  LEU A CD2 1 
ATOM   690  N  N   . GLU A 1 89  ? 57.45500 32.01400 41.99800 1.000 13.88721 ?  89  GLU A N   1 
ATOM   691  C  CA  . GLU A 1 89  ? 58.23100 31.62400 43.17400 1.000 15.22187 ?  89  GLU A CA  1 
ATOM   692  C  C   . GLU A 1 89  ? 58.63000 32.83300 44.02600 1.000 16.39406 ?  89  GLU A C   1 
ATOM   693  O  O   . GLU A 1 89  ? 59.76400 32.95600 44.47500 1.000 16.30209 ?  89  GLU A O   1 
ATOM   694  C  CB  . GLU A 1 89  ? 59.43300 30.75000 42.79300 1.000 21.84029 ?  89  GLU A CB  1 
ATOM   695  C  CG  . GLU A 1 89  ? 58.96500 29.45300 42.10400 1.000 22.96787 ?  89  GLU A CG  1 
ATOM   696  C  CD  . GLU A 1 89  ? 60.08200 28.43600 41.88100 1.000 34.64426 ?  89  GLU A CD  1 
ATOM   697  O  OE1 . GLU A 1 89  ? 61.13800 28.80500 41.33600 1.000 37.21312 ?  89  GLU A OE1 1 
ATOM   698  O  OE2 . GLU A 1 89  ? 59.88700 27.26000 42.25000 1.000 46.64570 -1 89  GLU A OE2 1 
ATOM   699  N  N   . VAL A 1 90  ? 57.66700 33.72900 44.27000 1.000 13.99734 ?  90  VAL A N   1 
ATOM   700  C  CA  . VAL A 1 90  ? 57.93500 34.84100 45.17800 1.000 12.94871 ?  90  VAL A CA  1 
ATOM   701  C  C   . VAL A 1 90  ? 58.36800 34.27900 46.52400 1.000 11.37678 ?  90  VAL A C   1 
ATOM   702  O  O   . VAL A 1 90  ? 57.94200 33.19300 46.93600 1.000 14.26956 ?  90  VAL A O   1 
ATOM   703  C  CB  . VAL A 1 90  ? 56.73600 35.79600 45.35900 1.000 12.90868 ?  90  VAL A CB  1 
ATOM   704  C  CG1 . VAL A 1 90  ? 56.33300 36.41100 44.02900 1.000 14.81360 ?  90  VAL A CG1 1 
ATOM   705  C  CG2 . VAL A 1 90  ? 55.54800 35.09000 46.02000 1.000 14.06806 ?  90  VAL A CG2 1 
ATOM   706  N  N   . GLU A 1 91  ? 59.22900 35.02400 47.21000 1.000 12.45583 ?  91  GLU A N   1 
ATOM   707  C  CA  . GLU A 1 91  ? 59.69300 34.59300 48.52200 1.000 14.42775 ?  91  GLU A CA  1 
ATOM   708  C  C   . GLU A 1 91  ? 58.92200 35.22600 49.66600 1.000 13.59015 ?  91  GLU A C   1 
ATOM   709  O  O   . GLU A 1 91  ? 58.93700 34.67800 50.77600 1.000 13.18112 ?  91  GLU A O   1 
ATOM   710  C  CB  . GLU A 1 91  ? 61.18400 34.91000 48.68000 1.000 23.44766 ?  91  GLU A CB  1 
ATOM   711  C  CG  . GLU A 1 91  ? 62.00600 34.25200 47.58200 1.000 29.63033 ?  91  GLU A CG  1 
ATOM   712  C  CD  . GLU A 1 91  ? 63.48400 34.49500 47.72900 1.000 44.06295 ?  91  GLU A CD  1 
ATOM   713  O  OE1 . GLU A 1 91  ? 64.02800 34.16400 48.80300 1.000 42.96904 ?  91  GLU A OE1 1 
ATOM   714  O  OE2 . GLU A 1 91  ? 64.09400 35.03200 46.77800 1.000 46.29257 -1 91  GLU A OE2 1 
ATOM   715  N  N   . HIS A 1 92  ? 58.24300 36.34700 49.41800 1.000 12.72408 ?  92  HIS A N   1 
ATOM   716  C  CA  . HIS A 1 92  ? 57.50100 37.04900 50.45900 1.000 12.12961 ?  92  HIS A CA  1 
ATOM   717  C  C   . HIS A 1 92  ? 56.14300 37.45900 49.93600 1.000 13.22796 ?  92  HIS A C   1 
ATOM   718  O  O   . HIS A 1 92  ? 56.02600 37.91500 48.79900 1.000 13.52929 ?  92  HIS A O   1 
ATOM   719  C  CB  . HIS A 1 92  ? 58.23300 38.31400 50.92100 1.000 15.24064 ?  92  HIS A CB  1 
ATOM   720  C  CG  . HIS A 1 92  ? 59.54400 38.01700 51.56500 1.000 14.25317 ?  92  HIS A CG  1 
ATOM   721  N  ND1 . HIS A 1 92  ? 59.64800 37.62500 52.88200 1.000 16.87280 ?  92  HIS A ND1 1 
ATOM   722  C  CD2 . HIS A 1 92  ? 60.79600 37.97900 51.05300 1.000 17.58958 ?  92  HIS A CD2 1 
ATOM   723  C  CE1 . HIS A 1 92  ? 60.92000 37.40100 53.16800 1.000 18.72059 ?  92  HIS A CE1 1 
ATOM   724  N  NE2 . HIS A 1 92  ? 61.63700 37.61300 52.07800 1.000 18.37815 ?  92  HIS A NE2 1 
ATOM   725  N  N   . ILE A 1 93  ? 55.12000 37.28500 50.76900 1.000 11.08539 ?  93  ILE A N   1 
ATOM   726  C  CA  . ILE A 1 93  ? 53.79600 37.83800 50.51900 1.000 11.90989 ?  93  ILE A CA  1 
ATOM   727  C  C   . ILE A 1 93  ? 53.48900 38.78200 51.66500 1.000 10.89015 ?  93  ILE A C   1 
ATOM   728  O  O   . ILE A 1 93  ? 53.57000 38.38700 52.83000 1.000 12.48301 ?  93  ILE A O   1 
ATOM   729  C  CB  . ILE A 1 93  ? 52.71700 36.75100 50.43000 1.000 11.19385 ?  93  ILE A CB  1 
ATOM   730  C  CG1 . ILE A 1 93  ? 53.09600 35.71700 49.36500 1.000 11.33135 ?  93  ILE A CG1 1 
ATOM   731  C  CG2 . ILE A 1 93  ? 51.36500 37.41200 50.10300 1.000 12.39196 ?  93  ILE A CG2 1 
ATOM   732  C  CD1 . ILE A 1 93  ? 52.10600 34.51700 49.26600 1.000 14.68539 ?  93  ILE A CD1 1 
ATOM   733  N  N   . ILE A 1 94  ? 53.14400 40.01800 51.33300 1.000 10.29183 ?  94  ILE A N   1 
ATOM   734  C  CA  . ILE A 1 94  ? 52.83200 41.06400 52.29500 1.000 11.52497 ?  94  ILE A CA  1 
ATOM   735  C  C   . ILE A 1 94  ? 51.37000 41.41900 52.10300 1.000 11.85851 ?  94  ILE A C   1 
ATOM   736  O  O   . ILE A 1 94  ? 50.97800 41.81700 50.99500 1.000 11.74019 ?  94  ILE A O   1 
ATOM   737  C  CB  . ILE A 1 94  ? 53.69400 42.30500 52.05900 1.000 10.62003 ?  94  ILE A CB  1 
ATOM   738  C  CG1 . ILE A 1 94  ? 55.17700 41.97100 52.24500 1.000 13.82750 ?  94  ILE A CG1 1 
ATOM   739  C  CG2 . ILE A 1 94  ? 53.23000 43.43200 52.99100 1.000 14.18361 ?  94  ILE A CG2 1 
ATOM   740  C  CD1 . ILE A 1 94  ? 56.10400 42.95100 51.54200 1.000 17.93708 ?  94  ILE A CD1 1 
ATOM   741  N  N   . ILE A 1 95  ? 50.56500 41.26100 53.15900 1.000 10.23282 ?  95  ILE A N   1 
ATOM   742  C  CA  . ILE A 1 95  ? 49.20300 41.79700 53.18500 1.000 10.65081 ?  95  ILE A CA  1 
ATOM   743  C  C   . ILE A 1 95  ? 49.25500 43.09200 53.97200 1.000 11.48006 ?  95  ILE A C   1 
ATOM   744  O  O   . ILE A 1 95  ? 49.67200 43.09500 55.14200 1.000 11.59488 ?  95  ILE A O   1 
ATOM   745  C  CB  . ILE A 1 95  ? 48.21400 40.81400 53.82100 1.000 10.14689 ?  95  ILE A CB  1 
ATOM   746  C  CG1 . ILE A 1 95  ? 48.26900 39.45900 53.10200 1.000 12.02983 ?  95  ILE A CG1 1 
ATOM   747  C  CG2 . ILE A 1 95  ? 46.76800 41.39500 53.81300 1.000 12.03409 ?  95  ILE A CG2 1 
ATOM   748  C  CD1 . ILE A 1 95  ? 47.21100 38.48600 53.51600 1.000 13.29989 ?  95  ILE A CD1 1 
ATOM   749  N  N   . CYS A 1 96  ? 48.86800 44.19600 53.34600 1.000 10.89631 ?  96  CYS A N   1 
ATOM   750  C  CA  . CYS A 1 96  ? 48.98800 45.49900 53.97600 1.000 10.83454 ?  96  CYS A CA  1 
ATOM   751  C  C   . CYS A 1 96  ? 47.60300 46.12800 54.03800 1.000 11.40234 ?  96  CYS A C   1 
ATOM   752  O  O   . CYS A 1 96  ? 46.96500 46.32000 52.99700 1.000 13.64240 ?  96  CYS A O   1 
ATOM   753  C  CB  . CYS A 1 96  ? 49.96000 46.37900 53.19900 1.000 11.31146 ?  96  CYS A CB  1 
ATOM   754  S  SG  . CYS A 1 96  ? 50.38600 47.87800 54.13900 1.000 14.18621 ?  96  CYS A SG  1 
ATOM   755  N  N   . GLY A 1 97  ? 47.12800 46.41600 55.25200 1.000 11.87492 ?  97  GLY A N   1 
ATOM   756  C  CA  . GLY A 1 97  ? 45.94000 47.21400 55.45600 1.000 11.18188 ?  97  GLY A CA  1 
ATOM   757  C  C   . GLY A 1 97  ? 46.29600 48.66300 55.74400 1.000 12.70489 ?  97  GLY A C   1 
ATOM   758  O  O   . GLY A 1 97  ? 47.45800 49.06200 55.77000 1.000 13.10851 ?  97  GLY A O   1 
ATOM   759  N  N   . HIS A 1 98  ? 45.29300 49.48700 55.96300 1.000 9.99090  ?  98  HIS A N   1 
ATOM   760  C  CA  . HIS A 1 98  ? 45.55300 50.88300 56.26000 1.000 11.63965 ?  98  HIS A CA  1 
ATOM   761  C  C   . HIS A 1 98  ? 44.49400 51.49700 57.16500 1.000 14.26907 ?  98  HIS A C   1 
ATOM   762  O  O   . HIS A 1 98  ? 43.32200 51.29200 56.97100 1.000 13.90227 ?  98  HIS A O   1 
ATOM   763  C  CB  . HIS A 1 98  ? 45.75100 51.70600 54.96800 1.000 11.10712 ?  98  HIS A CB  1 
ATOM   764  C  CG  . HIS A 1 98  ? 44.53300 51.81700 54.11700 1.000 12.35128 ?  98  HIS A CG  1 
ATOM   765  N  ND1 . HIS A 1 98  ? 43.91900 53.02100 53.87600 1.000 12.53392 ?  98  HIS A ND1 1 
ATOM   766  C  CD2 . HIS A 1 98  ? 43.82900 50.88800 53.43400 1.000 12.51930 ?  98  HIS A CD2 1 
ATOM   767  C  CE1 . HIS A 1 98  ? 42.87900 52.83000 53.09100 1.000 11.97689 ?  98  HIS A CE1 1 
ATOM   768  N  NE2 . HIS A 1 98  ? 42.80100 51.54400 52.80900 1.000 11.11058 ?  98  HIS A NE2 1 
ATOM   769  N  N   . TYR A 1 99  ? 44.96100 52.27800 58.12700 1.000 12.92899 ?  99  TYR A N   1 
ATOM   770  C  CA  . TYR A 1 99  ? 44.06200 52.92300 59.07800 1.000 11.37131 ?  99  TYR A CA  1 
ATOM   771  C  C   . TYR A 1 99  ? 43.24700 53.96200 58.33900 1.000 12.03245 ?  99  TYR A C   1 
ATOM   772  O  O   . TYR A 1 99  ? 43.79600 54.73500 57.54500 1.000 13.62117 ?  99  TYR A O   1 
ATOM   773  C  CB  . TYR A 1 99  ? 44.89300 53.60800 60.17300 1.000 12.57644 ?  99  TYR A CB  1 
ATOM   774  C  CG  . TYR A 1 99  ? 45.82800 52.64400 60.84800 1.000 12.08276 ?  99  TYR A CG  1 
ATOM   775  C  CD1 . TYR A 1 99  ? 45.33300 51.56000 61.55100 1.000 12.82771 ?  99  TYR A CD1 1 
ATOM   776  C  CD2 . TYR A 1 99  ? 47.21200 52.79800 60.75000 1.000 14.77053 ?  99  TYR A CD2 1 
ATOM   777  C  CE1 . TYR A 1 99  ? 46.18400 50.67100 62.17500 1.000 14.71767 ?  99  TYR A CE1 1 
ATOM   778  C  CE2 . TYR A 1 99  ? 48.06100 51.91300 61.35400 1.000 16.08601 ?  99  TYR A CE2 1 
ATOM   779  C  CZ  . TYR A 1 99  ? 47.55300 50.85800 62.06900 1.000 15.57356 ?  99  TYR A CZ  1 
ATOM   780  O  OH  . TYR A 1 99  ? 48.42700 49.98100 62.68300 1.000 17.87350 ?  99  TYR A OH  1 
ATOM   781  N  N   . GLY A 1 100 ? 41.93600 53.98700 58.58900 1.000 14.29517 ?  100 GLY A N   1 
ATOM   782  C  CA  . GLY A 1 100 ? 41.05600 54.85700 57.83400 1.000 14.59531 ?  100 GLY A CA  1 
ATOM   783  C  C   . GLY A 1 100 ? 40.47100 54.23100 56.58700 1.000 15.16937 ?  100 GLY A C   1 
ATOM   784  O  O   . GLY A 1 100 ? 39.73900 54.90600 55.85700 1.000 15.73685 ?  100 GLY A O   1 
ATOM   785  N  N   . CYS A 1 101 ? 40.75500 52.97500 56.34100 1.000 13.93811 ?  101 CYS A N   1 
ATOM   786  C  CA  . CYS A 1 101 ? 40.19800 52.27400 55.20400 1.000 13.51443 ?  101 CYS A CA  1 
ATOM   787  C  C   . CYS A 1 101 ? 38.69500 52.45400 55.07500 1.000 11.38146 ?  101 CYS A C   1 
ATOM   788  O  O   . CYS A 1 101 ? 37.96700 52.17600 55.98500 1.000 13.02935 ?  101 CYS A O   1 
ATOM   789  C  CB  . CYS A 1 101 ? 40.51900 50.80100 55.39400 1.000 11.69923 ?  101 CYS A CB  1 
ATOM   790  S  SG  . CYS A 1 101 ? 40.00400 49.77400 53.95600 1.000 12.23881 ?  101 CYS A SG  1 
ATOM   791  N  N   . GLY A 1 102 ? 38.26400 52.85600 53.88700 1.000 14.04271 ?  102 GLY A N   1 
ATOM   792  C  CA  . GLY A 1 102 ? 36.83700 53.04800 53.67900 1.000 16.28975 ?  102 GLY A CA  1 
ATOM   793  C  C   . GLY A 1 102 ? 36.05100 51.75500 53.75700 1.000 15.20604 ?  102 GLY A C   1 
ATOM   794  O  O   . GLY A 1 102 ? 34.87800 51.75700 54.16700 1.000 15.08534 ?  102 GLY A O   1 
ATOM   795  N  N   . GLY A 1 103 ? 36.67900 50.63700 53.38200 1.000 13.25154 ?  103 GLY A N   1 
ATOM   796  C  CA  . GLY A 1 103 ? 35.98100 49.36400 53.44100 1.000 13.78152 ?  103 GLY A CA  1 
ATOM   797  C  C   . GLY A 1 103 ? 35.75500 48.91300 54.87300 1.000 12.96580 ?  103 GLY A C   1 
ATOM   798  O  O   . GLY A 1 103 ? 34.66300 48.44800 55.23300 1.000 14.07088 ?  103 GLY A O   1 
ATOM   799  N  N   . VAL A 1 104 ? 36.78000 49.06000 55.72000 1.000 11.30872 ?  104 VAL A N   1 
ATOM   800  C  CA  . VAL A 1 104 ? 36.63900 48.69900 57.12600 1.000 12.07338 ?  104 VAL A CA  1 
ATOM   801  C  C   . VAL A 1 104 ? 35.61900 49.60500 57.79800 1.000 12.08081 ?  104 VAL A C   1 
ATOM   802  O  O   . VAL A 1 104 ? 34.77600 49.14600 58.58700 1.000 15.15375 ?  104 VAL A O   1 
ATOM   803  C  CB  . VAL A 1 104 ? 38.00900 48.74900 57.83000 1.000 13.88792 ?  104 VAL A CB  1 
ATOM   804  C  CG1 . VAL A 1 104 ? 37.86700 48.43200 59.33600 1.000 15.81287 ?  104 VAL A CG1 1 
ATOM   805  C  CG2 . VAL A 1 104 ? 38.97100 47.76100 57.19800 1.000 13.95146 ?  104 VAL A CG2 1 
ATOM   806  N  N   . GLN A 1 105 ? 35.69300 50.91300 57.51200 1.000 14.11711 ?  105 GLN A N   1 
ATOM   807  C  CA  . GLN A 1 105 ? 34.73200 51.84700 58.10100 1.000 14.56731 ?  105 GLN A CA  1 
ATOM   808  C  C   . GLN A 1 105 ? 33.30400 51.52500 57.68000 1.000 14.57794 ?  105 GLN A C   1 
ATOM   809  O  O   . GLN A 1 105 ? 32.38100 51.57000 58.51100 1.000 16.57028 ?  105 GLN A O   1 
ATOM   810  C  CB  . GLN A 1 105 ? 35.09400 53.28400 57.73100 1.000 17.86335 ?  105 GLN A CB  1 
ATOM   811  C  CG  . GLN A 1 105 ? 34.10000 54.28800 58.30300 1.000 20.98367 ?  105 GLN A CG  1 
ATOM   812  C  CD  . GLN A 1 105 ? 34.53000 55.71300 58.05900 1.000 31.92938 ?  105 GLN A CD  1 
ATOM   813  O  OE1 . GLN A 1 105 ? 35.67600 55.97100 57.68300 1.000 36.03365 ?  105 GLN A OE1 1 
ATOM   814  N  NE2 . GLN A 1 105 ? 33.60900 56.65100 58.26000 1.000 35.68095 ?  105 GLN A NE2 1 
ATOM   815  N  N   . ALA A 1 106 ? 33.10700 51.15000 56.40700 1.000 13.78036 ?  106 ALA A N   1 
ATOM   816  C  CA  . ALA A 1 106 ? 31.75700 50.82300 55.94500 1.000 16.35645 ?  106 ALA A CA  1 
ATOM   817  C  C   . ALA A 1 106 ? 31.24800 49.54100 56.58100 1.000 16.34717 ?  106 ALA A C   1 
ATOM   818  O  O   . ALA A 1 106 ? 30.03900 49.41100 56.83300 1.000 19.23705 ?  106 ALA A O   1 
ATOM   819  C  CB  . ALA A 1 106 ? 31.73200 50.72300 54.41800 1.000 13.26397 ?  106 ALA A CB  1 
ATOM   820  N  N   . ALA A 1 107 ? 32.14700 48.59300 56.87000 1.000 13.77812 ?  107 ALA A N   1 
ATOM   821  C  CA  . ALA A 1 107 ? 31.72600 47.37100 57.54500 1.000 16.03369 ?  107 ALA A CA  1 
ATOM   822  C  C   . ALA A 1 107 ? 31.16000 47.67600 58.92300 1.000 18.74744 ?  107 ALA A C   1 
ATOM   823  O  O   . ALA A 1 107 ? 30.18600 47.05400 59.34900 1.000 19.87188 ?  107 ALA A O   1 
ATOM   824  C  CB  . ALA A 1 107 ? 32.90200 46.39300 57.66200 1.000 17.05910 ?  107 ALA A CB  1 
ATOM   825  N  N   . VAL A 1 108 ? 31.76700 48.62800 59.63400 1.000 18.35434 ?  108 VAL A N   1 
ATOM   826  C  CA  . VAL A 1 108 ? 31.33500 48.99800 60.98100 1.000 17.98384 ?  108 VAL A CA  1 
ATOM   827  C  C   . VAL A 1 108 ? 30.10100 49.89300 60.94800 1.000 18.80137 ?  108 VAL A C   1 
ATOM   828  O  O   . VAL A 1 108 ? 29.17600 49.71500 61.74800 1.000 19.04677 ?  108 VAL A O   1 
ATOM   829  C  CB  . VAL A 1 108 ? 32.50100 49.66800 61.72700 1.000 19.10117 ?  108 VAL A CB  1 
ATOM   830  C  CG1 . VAL A 1 108 ? 32.01800 50.32200 63.00100 1.000 22.01783 ?  108 VAL A CG1 1 
ATOM   831  C  CG2 . VAL A 1 108 ? 33.53700 48.62600 62.08400 1.000 19.92592 ?  108 VAL A CG2 1 
ATOM   832  N  N   . GLU A 1 109 ? 30.07700 50.89500 60.07300 1.000 18.36978 ?  109 GLU A N   1 
ATOM   833  C  CA  . GLU A 1 109 ? 28.92700 51.79600 60.04200 1.000 19.53162 ?  109 GLU A CA  1 
ATOM   834  C  C   . GLU A 1 109 ? 27.74600 51.18600 59.31400 1.000 22.91050 ?  109 GLU A C   1 
ATOM   835  O  O   . GLU A 1 109 ? 26.60000 51.57300 59.57200 1.000 20.85867 ?  109 GLU A O   1 
ATOM   836  C  CB  . GLU A 1 109 ? 29.32500 53.12500 59.40500 1.000 17.95608 ?  109 GLU A CB  1 
ATOM   837  C  CG  . GLU A 1 109 ? 30.36600 53.84700 60.25800 1.000 22.05946 ?  109 GLU A CG  1 
ATOM   838  C  CD  . GLU A 1 109 ? 30.91100 55.09200 59.61900 1.000 28.67438 ?  109 GLU A CD  1 
ATOM   839  O  OE1 . GLU A 1 109 ? 30.66700 55.31400 58.41300 1.000 31.90257 ?  109 GLU A OE1 1 
ATOM   840  O  OE2 . GLU A 1 109 ? 31.59900 55.85300 60.33100 1.000 33.48846 -1 109 GLU A OE2 1 
ATOM   841  N  N   . ASN A 1 110 ? 28.00500 50.24400 58.41900 1.000 17.10864 ?  110 ASN A N   1 
ATOM   842  C  CA  . ASN A 1 110 ? 26.98400 49.49700 57.69700 1.000 19.58992 ?  110 ASN A CA  1 
ATOM   843  C  C   . ASN A 1 110 ? 25.97900 50.36400 56.92900 1.000 16.83417 ?  110 ASN A C   1 
ATOM   844  O  O   . ASN A 1 110 ? 24.76500 50.08900 56.97000 1.000 17.69345 ?  110 ASN A O   1 
ATOM   845  C  CB  . ASN A 1 110 ? 26.27900 48.54500 58.66600 1.000 19.94055 ?  110 ASN A CB  1 
ATOM   846  C  CG  . ASN A 1 110 ? 25.60200 47.40400 57.95800 1.000 22.65539 ?  110 ASN A CG  1 
ATOM   847  O  OD1 . ASN A 1 110 ? 26.05200 46.95800 56.90200 1.000 22.64036 ?  110 ASN A OD1 1 
ATOM   848  N  ND2 . ASN A 1 110 ? 24.50300 46.92500 58.52800 1.000 24.34184 ?  110 ASN A ND2 1 
ATOM   849  N  N   . PRO A 1 111 ? 26.42700 51.37000 56.17100 1.000 17.26891 ?  111 PRO A N   1 
ATOM   850  C  CA  . PRO A 1 111 ? 25.51100 52.03700 55.24100 1.000 15.71925 ?  111 PRO A CA  1 
ATOM   851  C  C   . PRO A 1 111 ? 25.09100 51.07400 54.14200 1.000 17.31230 ?  111 PRO A C   1 
ATOM   852  O  O   . PRO A 1 111 ? 25.74400 50.05600 53.89400 1.000 16.99248 ?  111 PRO A O   1 
ATOM   853  C  CB  . PRO A 1 111 ? 26.36000 53.16900 54.66600 1.000 16.66728 ?  111 PRO A CB  1 
ATOM   854  C  CG  . PRO A 1 111 ? 27.75700 52.62600 54.68300 1.000 17.83454 ?  111 PRO A CG  1 
ATOM   855  C  CD  . PRO A 1 111 ? 27.82400 51.81800 55.96600 1.000 18.66576 ?  111 PRO A CD  1 
ATOM   856  N  N   . GLU A 1 112 ? 23.98900 51.41900 53.48000 1.000 17.27778 ?  112 GLU A N   1 
ATOM   857  C  CA  . GLU A 1 112 ? 23.44400 50.60900 52.38200 1.000 19.84568 ?  112 GLU A CA  1 
ATOM   858  C  C   . GLU A 1 112 ? 24.12300 51.06700 51.10600 1.000 17.62267 ?  112 GLU A C   1 
ATOM   859  O  O   . GLU A 1 112 ? 23.67400 52.00400 50.44500 1.000 20.76295 ?  112 GLU A O   1 
ATOM   860  C  CB  . GLU A 1 112 ? 21.93800 50.82800 52.26200 1.000 21.83175 ?  112 GLU A CB  1 
ATOM   861  C  CG  . GLU A 1 112 ? 21.11100 50.29500 53.41800 1.000 33.28418 ?  112 GLU A CG  1 
ATOM   862  C  CD  . GLU A 1 112 ? 19.61000 50.47200 53.18600 1.000 50.99524 ?  112 GLU A CD  1 
ATOM   863  O  OE1 . GLU A 1 112 ? 19.20400 50.63600 52.00900 1.000 45.37429 ?  112 GLU A OE1 1 
ATOM   864  O  OE2 . GLU A 1 112 ? 18.84100 50.45600 54.17900 1.000 51.34605 -1 112 GLU A OE2 1 
ATOM   865  N  N   . LEU A 1 113 ? 25.22500 50.40700 50.74400 1.000 13.99114 ?  113 LEU A N   1 
ATOM   866  C  CA  . LEU A 1 113 ? 26.03400 50.86100 49.62200 1.000 13.04408 ?  113 LEU A CA  1 
ATOM   867  C  C   . LEU A 1 113 ? 25.78600 50.09600 48.33200 1.000 12.42795 ?  113 LEU A C   1 
ATOM   868  O  O   . LEU A 1 113 ? 26.29800 50.51100 47.28500 1.000 16.40956 ?  113 LEU A O   1 
ATOM   869  C  CB  . LEU A 1 113 ? 27.51900 50.76100 49.95400 1.000 13.99520 ?  113 LEU A CB  1 
ATOM   870  C  CG  . LEU A 1 113 ? 27.97100 51.58500 51.15700 1.000 13.33925 ?  113 LEU A CG  1 
ATOM   871  C  CD1 . LEU A 1 113 ? 29.45200 51.40700 51.36900 1.000 16.87289 ?  113 LEU A CD1 1 
ATOM   872  C  CD2 . LEU A 1 113 ? 27.63200 53.07900 50.94400 1.000 16.29693 ?  113 LEU A CD2 1 
ATOM   873  N  N   . GLY A 1 114 ? 25.00900 49.01800 48.36600 1.000 13.58204 ?  114 GLY A N   1 
ATOM   874  C  CA  . GLY A 1 114 ? 24.84000 48.20900 47.17200 1.000 15.80094 ?  114 GLY A CA  1 
ATOM   875  C  C   . GLY A 1 114 ? 25.65600 46.93000 47.15700 1.000 12.21325 ?  114 GLY A C   1 
ATOM   876  O  O   . GLY A 1 114 ? 25.90500 46.33300 48.20500 1.000 11.88442 ?  114 GLY A O   1 
ATOM   877  N  N   . LEU A 1 115 ? 26.05700 46.50500 45.95600 1.000 11.95533 ?  115 LEU A N   1 
ATOM   878  C  CA  . LEU A 1 115 ? 26.70400 45.19800 45.78600 1.000 13.54279 ?  115 LEU A CA  1 
ATOM   879  C  C   . LEU A 1 115 ? 27.86300 44.99200 46.76600 1.000 10.13740 ?  115 LEU A C   1 
ATOM   880  O  O   . LEU A 1 115 ? 28.02100 43.90100 47.31900 1.000 10.77010 ?  115 LEU A O   1 
ATOM   881  C  CB  . LEU A 1 115 ? 27.18200 45.03200 44.34100 1.000 12.96292 ?  115 LEU A CB  1 
ATOM   882  C  CG  . LEU A 1 115 ? 27.76900 43.66000 43.97400 1.000 12.91144 ?  115 LEU A CG  1 
ATOM   883  C  CD1 . LEU A 1 115 ? 26.72000 42.52500 44.03900 1.000 16.78123 ?  115 LEU A CD1 1 
ATOM   884  C  CD2 . LEU A 1 115 ? 28.45400 43.72200 42.57500 1.000 13.07951 ?  115 LEU A CD2 1 
ATOM   885  N  N   . ILE A 1 116 ? 28.68100 46.03000 46.99200 1.000 10.46072 ?  116 ILE A N   1 
ATOM   886  C  CA  . ILE A 1 116 ? 29.86900 45.92900 47.84500 1.000 10.10758 ?  116 ILE A CA  1 
ATOM   887  C  C   . ILE A 1 116 ? 29.54200 45.42900 49.25100 1.000 9.87012  ?  116 ILE A C   1 
ATOM   888  O  O   . ILE A 1 116 ? 30.40800 44.84600 49.92200 1.000 10.62550 ?  116 ILE A O   1 
ATOM   889  C  CB  . ILE A 1 116 ? 30.59800 47.28800 47.86600 1.000 10.78185 ?  116 ILE A CB  1 
ATOM   890  C  CG1 . ILE A 1 116 ? 31.92500 47.21600 48.61200 1.000 10.98328 ?  116 ILE A CG1 1 
ATOM   891  C  CG2 . ILE A 1 116 ? 29.69300 48.40500 48.48800 1.000 11.12046 ?  116 ILE A CG2 1 
ATOM   892  C  CD1 . ILE A 1 116 ? 32.99400 46.31200 47.94100 1.000 10.95585 ?  116 ILE A CD1 1 
ATOM   893  N  N   . ASN A 1 117 ? 28.31500 45.65800 49.74100 1.000 10.50220 ?  117 ASN A N   1 
ATOM   894  C  CA  . ASN A 1 117 ? 28.01300 45.20900 51.10600 1.000 10.46289 ?  117 ASN A CA  1 
ATOM   895  C  C   . ASN A 1 117 ? 28.21000 43.70800 51.27400 1.000 12.20612 ?  117 ASN A C   1 
ATOM   896  O  O   . ASN A 1 117 ? 28.54300 43.24400 52.37200 1.000 12.72791 ?  117 ASN A O   1 
ATOM   897  C  CB  . ASN A 1 117 ? 26.59100 45.59300 51.49800 1.000 10.87961 ?  117 ASN A CB  1 
ATOM   898  C  CG  . ASN A 1 117 ? 26.50500 46.97400 52.09400 1.000 16.41459 ?  117 ASN A CG  1 
ATOM   899  O  OD1 . ASN A 1 117 ? 27.21000 47.86600 51.68800 1.000 19.29723 ?  117 ASN A OD1 1 
ATOM   900  N  ND2 . ASN A 1 117 ? 25.63700 47.14100 53.08200 1.000 18.59710 ?  117 ASN A ND2 1 
ATOM   901  N  N   . ASN A 1 118 ? 28.05400 42.92600 50.20100 1.000 10.86786 ?  118 ASN A N   1 
ATOM   902  C  CA  . ASN A 1 118 ? 28.25600 41.48500 50.34400 1.000 9.07428  ?  118 ASN A CA  1 
ATOM   903  C  C   . ASN A 1 118 ? 29.72300 41.16000 50.64700 1.000 10.40804 ?  118 ASN A C   1 
ATOM   904  O  O   . ASN A 1 118 ? 30.03300 40.40400 51.57900 1.000 10.65889 ?  118 ASN A O   1 
ATOM   905  C  CB  . ASN A 1 118 ? 27.76700 40.77800 49.07800 1.000 10.46074 ?  118 ASN A CB  1 
ATOM   906  C  CG  . ASN A 1 118 ? 26.29400 41.01600 48.84400 1.000 12.67354 ?  118 ASN A CG  1 
ATOM   907  O  OD1 . ASN A 1 118 ? 25.45100 40.54200 49.61100 1.000 12.41245 ?  118 ASN A OD1 1 
ATOM   908  N  ND2 . ASN A 1 118 ? 25.96700 41.78700 47.81500 1.000 12.22823 ?  118 ASN A ND2 1 
ATOM   909  N  N   . TRP A 1 119 ? 30.64000 41.74700 49.87400 1.000 10.51009 ?  119 TRP A N   1 
ATOM   910  C  CA  . TRP A 1 119 ? 32.07300 41.64600 50.14600 1.000 9.49964  ?  119 TRP A CA  1 
ATOM   911  C  C   . TRP A 1 119 ? 32.39300 42.04100 51.58500 1.000 11.73382 ?  119 TRP A C   1 
ATOM   912  O  O   . TRP A 1 119 ? 33.15700 41.35400 52.27800 1.000 10.26706 ?  119 TRP A O   1 
ATOM   913  C  CB  . TRP A 1 119 ? 32.79300 42.59000 49.16600 1.000 10.66122 ?  119 TRP A CB  1 
ATOM   914  C  CG  . TRP A 1 119 ? 34.29700 42.42600 49.05400 1.000 10.25764 ?  119 TRP A CG  1 
ATOM   915  C  CD1 . TRP A 1 119 ? 35.28000 43.19200 49.67600 1.000 11.70859 ?  119 TRP A CD1 1 
ATOM   916  C  CD2 . TRP A 1 119 ? 34.99200 41.46900 48.24900 1.000 9.50346  ?  119 TRP A CD2 1 
ATOM   917  N  NE1 . TRP A 1 119 ? 36.52700 42.74900 49.28800 1.000 12.13384 ?  119 TRP A NE1 1 
ATOM   918  C  CE2 . TRP A 1 119 ? 36.38900 41.68300 48.44700 1.000 10.94101 ?  119 TRP A CE2 1 
ATOM   919  C  CE3 . TRP A 1 119 ? 34.57700 40.44300 47.38800 1.000 9.50119  ?  119 TRP A CE3 1 
ATOM   920  C  CZ2 . TRP A 1 119 ? 37.36700 40.92200 47.78700 1.000 12.01310 ?  119 TRP A CZ2 1 
ATOM   921  C  CZ3 . TRP A 1 119 ? 35.55400 39.67700 46.75500 1.000 12.21650 ?  119 TRP A CZ3 1 
ATOM   922  C  CH2 . TRP A 1 119 ? 36.93400 39.92200 46.97500 1.000 11.22448 ?  119 TRP A CH2 1 
ATOM   923  N  N   . LEU A 1 120 ? 31.76800 43.12600 52.07000 1.000 11.17646 ?  120 LEU A N   1 
ATOM   924  C  CA  . LEU A 1 120 ? 32.12200 43.64800 53.39000 1.000 10.66212 ?  120 LEU A CA  1 
ATOM   925  C  C   . LEU A 1 120 ? 31.61400 42.77400 54.52600 1.000 10.98056 ?  120 LEU A C   1 
ATOM   926  O  O   . LEU A 1 120 ? 32.10200 42.90700 55.65800 1.000 10.77103 ?  120 LEU A O   1 
ATOM   927  C  CB  . LEU A 1 120 ? 31.61000 45.08800 53.55700 1.000 12.26013 ?  120 LEU A CB  1 
ATOM   928  C  CG  . LEU A 1 120 ? 32.19500 46.07300 52.53900 1.000 12.19878 ?  120 LEU A CG  1 
ATOM   929  C  CD1 . LEU A 1 120 ? 31.55200 47.44300 52.76300 1.000 14.57594 ?  120 LEU A CD1 1 
ATOM   930  C  CD2 . LEU A 1 120 ? 33.73400 46.14000 52.59600 1.000 15.32031 ?  120 LEU A CD2 1 
ATOM   931  N  N   . LEU A 1 121 ? 30.66700 41.86700 54.25400 1.000 9.85313  ?  121 LEU A N   1 
ATOM   932  C  CA  . LEU A 1 121 ? 30.22200 40.96200 55.30600 1.000 9.54702  ?  121 LEU A CA  1 
ATOM   933  C  C   . LEU A 1 121 ? 31.37700 40.13100 55.86000 1.000 11.05384 ?  121 LEU A C   1 
ATOM   934  O  O   . LEU A 1 121 ? 31.32500 39.71100 57.02100 1.000 11.20574 ?  121 LEU A O   1 
ATOM   935  C  CB  . LEU A 1 121 ? 29.08600 40.05900 54.80300 1.000 9.78458  ?  121 LEU A CB  1 
ATOM   936  C  CG  . LEU A 1 121 ? 27.73800 40.76300 54.56900 1.000 10.35413 ?  121 LEU A CG  1 
ATOM   937  C  CD1 . LEU A 1 121 ? 26.77600 39.83200 53.85800 1.000 13.95092 ?  121 LEU A CD1 1 
ATOM   938  C  CD2 . LEU A 1 121 ? 27.10500 41.22900 55.86600 1.000 13.25774 ?  121 LEU A CD2 1 
ATOM   939  N  N   . HIS A 1 122 ? 32.40500 39.85300 55.05300 1.000 9.92276  ?  122 HIS A N   1 
ATOM   940  C  CA  . HIS A 1 122 ? 33.54400 39.08900 55.56500 1.000 10.60105 ?  122 HIS A CA  1 
ATOM   941  C  C   . HIS A 1 122 ? 34.27100 39.86700 56.64900 1.000 11.88132 ?  122 HIS A C   1 
ATOM   942  O  O   . HIS A 1 122 ? 34.83800 39.26800 57.56900 1.000 12.86919 ?  122 HIS A O   1 
ATOM   943  C  CB  . HIS A 1 122 ? 34.50900 38.73400 54.41300 1.000 10.80693 ?  122 HIS A CB  1 
ATOM   944  C  CG  . HIS A 1 122 ? 33.95000 37.74700 53.43300 1.000 10.13928 ?  122 HIS A CG  1 
ATOM   945  N  ND1 . HIS A 1 122 ? 33.80500 36.40400 53.72300 1.000 12.80580 ?  122 HIS A ND1 1 
ATOM   946  C  CD2 . HIS A 1 122 ? 33.48600 37.91500 52.17000 1.000 12.91758 ?  122 HIS A CD2 1 
ATOM   947  C  CE1 . HIS A 1 122 ? 33.30800 35.78300 52.66100 1.000 12.88631 ?  122 HIS A CE1 1 
ATOM   948  N  NE2 . HIS A 1 122 ? 33.08500 36.67800 51.71800 1.000 11.06031 ?  122 HIS A NE2 1 
ATOM   949  N  N   . ILE A 1 123 ? 34.28700 41.19200 56.54300 1.000 10.47049 ?  123 ILE A N   1 
ATOM   950  C  CA  . ILE A 1 123 ? 34.88400 42.01000 57.59700 1.000 10.20395 ?  123 ILE A CA  1 
ATOM   951  C  C   . ILE A 1 123 ? 33.98900 42.01700 58.82800 1.000 11.48105 ?  123 ILE A C   1 
ATOM   952  O  O   . ILE A 1 123 ? 34.47100 41.94400 59.96300 1.000 12.28412 ?  123 ILE A O   1 
ATOM   953  C  CB  . ILE A 1 123 ? 35.13800 43.43700 57.08800 1.000 10.41128 ?  123 ILE A CB  1 
ATOM   954  C  CG1 . ILE A 1 123 ? 36.05100 43.43200 55.86900 1.000 12.53484 ?  123 ILE A CG1 1 
ATOM   955  C  CG2 . ILE A 1 123 ? 35.80900 44.27600 58.20800 1.000 13.28150 ?  123 ILE A CG2 1 
ATOM   956  C  CD1 . ILE A 1 123 ? 36.12600 44.79900 55.23500 1.000 14.91100 ?  123 ILE A CD1 1 
ATOM   957  N  N   . ARG A 1 124 ? 32.67600 42.12100 58.63300 1.000 11.51408 ?  124 ARG A N   1 
ATOM   958  C  CA  . ARG A 1 124 ? 31.77200 42.05100 59.77700 1.000 11.19942 ?  124 ARG A CA  1 
ATOM   959  C  C   . ARG A 1 124 ? 31.90600 40.72600 60.52300 1.000 13.23751 ?  124 ARG A C   1 
ATOM   960  O  O   . ARG A 1 124 ? 31.75600 40.69200 61.75500 1.000 14.12381 ?  124 ARG A O   1 
ATOM   961  C  CB  . ARG A 1 124 ? 30.33800 42.31200 59.30800 1.000 12.94955 ?  124 ARG A CB  1 
ATOM   962  C  CG  . ARG A 1 124 ? 30.15900 43.74700 58.85300 1.000 14.99356 ?  124 ARG A CG  1 
ATOM   963  C  CD  . ARG A 1 124 ? 28.76400 44.06500 58.30300 1.000 15.97762 ?  124 ARG A CD  1 
ATOM   964  N  NE  . ARG A 1 124 ? 27.69400 43.78100 59.24800 1.000 17.22706 ?  124 ARG A NE  1 
ATOM   965  C  CZ  . ARG A 1 124 ? 27.28700 44.62200 60.19000 1.000 18.58280 ?  124 ARG A CZ  1 
ATOM   966  N  NH1 . ARG A 1 124 ? 27.87800 45.78800 60.37500 1.000 16.95862 ?  124 ARG A NH1 1 
ATOM   967  N  NH2 . ARG A 1 124 ? 26.26200 44.28400 60.96300 1.000 22.49486 ?  124 ARG A NH2 1 
ATOM   968  N  N   . ASP A 1 125 ? 32.22000 39.63300 59.82100 1.000 12.25734 ?  125 ASP A N   1 
ATOM   969  C  CA  . ASP A 1 125 ? 32.43200 38.36800 60.52200 1.000 11.49875 ?  125 ASP A CA  1 
ATOM   970  C  C   . ASP A 1 125 ? 33.64800 38.45700 61.44500 1.000 12.30069 ?  125 ASP A C   1 
ATOM   971  O  O   . ASP A 1 125 ? 33.64200 37.89000 62.54400 1.000 12.82851 ?  125 ASP A O   1 
ATOM   972  C  CB  . ASP A 1 125 ? 32.62400 37.22700 59.51600 1.000 13.28653 ?  125 ASP A CB  1 
ATOM   973  C  CG  . ASP A 1 125 ? 31.34000 36.85900 58.76000 1.000 16.55324 ?  125 ASP A CG  1 
ATOM   974  O  OD1 . ASP A 1 125 ? 30.21400 37.20000 59.19600 1.000 22.52758 ?  125 ASP A OD1 1 
ATOM   975  O  OD2 . ASP A 1 125 ? 31.51700 36.20800 57.72500 1.000 23.53440 -1 125 ASP A OD2 1 
ATOM   976  N  N   . ILE A 1 126 ? 34.70200 39.16600 61.00200 1.000 11.78532 ?  126 ILE A N   1 
ATOM   977  C  CA  A ILE A 1 126 ? 35.91000 39.30400 61.81400 0.578 14.98489 ?  126 ILE A CA  1 
ATOM   978  C  CA  B ILE A 1 126 ? 35.92100 39.33500 61.79400 0.422 15.01950 ?  126 ILE A CA  1 
ATOM   979  C  C   . ILE A 1 126 ? 35.64000 40.19300 63.00800 1.000 15.17182 ?  126 ILE A C   1 
ATOM   980  O  O   . ILE A 1 126 ? 36.14500 39.93600 64.10900 1.000 14.90079 ?  126 ILE A O   1 
ATOM   981  C  CB  A ILE A 1 126 ? 37.07100 39.85100 60.96100 0.578 18.73106 ?  126 ILE A CB  1 
ATOM   982  C  CB  B ILE A 1 126 ? 36.99200 39.99500 60.90700 0.422 18.75387 ?  126 ILE A CB  1 
ATOM   983  C  CG1 A ILE A 1 126 ? 37.43100 38.85700 59.86800 0.578 21.36658 ?  126 ILE A CG1 1 
ATOM   984  C  CG1 B ILE A 1 126 ? 37.61300 38.97900 59.96600 0.422 20.90366 ?  126 ILE A CG1 1 
ATOM   985  C  CG2 A ILE A 1 126 ? 38.28400 40.22300 61.84000 0.578 21.01745 ?  126 ILE A CG2 1 
ATOM   986  C  CG2 B ILE A 1 126 ? 38.05400 40.71800 61.74000 0.422 19.66918 ?  126 ILE A CG2 1 
ATOM   987  C  CD1 A ILE A 1 126 ? 37.43100 37.41800 60.33200 0.578 14.50315 ?  126 ILE A CD1 1 
ATOM   988  C  CD1 B ILE A 1 126 ? 38.47900 39.61800 58.94000 0.422 16.28207 ?  126 ILE A CD1 1 
ATOM   989  N  N   . TRP A 1 127 ? 34.85900 41.25200 62.80300 1.000 12.74142 ?  127 TRP A N   1 
ATOM   990  C  CA  . TRP A 1 127 ? 34.46600 42.14900 63.87600 1.000 14.09941 ?  127 TRP A CA  1 
ATOM   991  C  C   . TRP A 1 127 ? 33.72000 41.37100 64.94800 1.000 14.84691 ?  127 TRP A C   1 
ATOM   992  O  O   . TRP A 1 127 ? 34.03000 41.48200 66.14600 1.000 15.52909 ?  127 TRP A O   1 
ATOM   993  C  CB  . TRP A 1 127 ? 33.58500 43.24600 63.27100 1.000 15.59544 ?  127 TRP A CB  1 
ATOM   994  C  CG  . TRP A 1 127 ? 33.20100 44.34400 64.18200 1.000 15.18516 ?  127 TRP A CG  1 
ATOM   995  C  CD1 . TRP A 1 127 ? 33.87000 44.76600 65.30100 1.000 20.08150 ?  127 TRP A CD1 1 
ATOM   996  C  CD2 . TRP A 1 127 ? 32.07000 45.19400 64.04100 1.000 16.92937 ?  127 TRP A CD2 1 
ATOM   997  N  NE1 . TRP A 1 127 ? 33.20200 45.83100 65.87000 1.000 19.42266 ?  127 TRP A NE1 1 
ATOM   998  C  CE2 . TRP A 1 127 ? 32.10200 46.12400 65.10600 1.000 18.04127 ?  127 TRP A CE2 1 
ATOM   999  C  CE3 . TRP A 1 127 ? 31.04400 45.28100 63.09700 1.000 19.72583 ?  127 TRP A CE3 1 
ATOM   1000 C  CZ2 . TRP A 1 127 ? 31.12000 47.09800 65.27600 1.000 22.48769 ?  127 TRP A CZ2 1 
ATOM   1001 C  CZ3 . TRP A 1 127 ? 30.07500 46.25200 63.25900 1.000 23.42113 ?  127 TRP A CZ3 1 
ATOM   1002 C  CH2 . TRP A 1 127 ? 30.12100 47.15100 64.34300 1.000 24.72032 ?  127 TRP A CH2 1 
ATOM   1003 N  N   . PHE A 1 128 ? 32.75900 40.54600 64.53300 1.000 12.14757 ?  128 PHE A N   1 
ATOM   1004 C  CA  . PHE A 1 128 ? 32.06300 39.66100 65.47100 1.000 12.74730 ?  128 PHE A CA  1 
ATOM   1005 C  C   . PHE A 1 128 ? 33.04400 38.76100 66.21900 1.000 16.58940 ?  128 PHE A C   1 
ATOM   1006 O  O   . PHE A 1 128 ? 32.96900 38.62500 67.45100 1.000 15.07842 ?  128 PHE A O   1 
ATOM   1007 C  CB  . PHE A 1 128 ? 31.02900 38.81100 64.72000 1.000 13.46387 ?  128 PHE A CB  1 
ATOM   1008 C  CG  . PHE A 1 128 ? 30.25100 37.89400 65.62100 1.000 17.43372 ?  128 PHE A CG  1 
ATOM   1009 C  CD1 . PHE A 1 128 ? 30.77800 36.67500 66.03900 1.000 16.78930 ?  128 PHE A CD1 1 
ATOM   1010 C  CD2 . PHE A 1 128 ? 28.97800 38.25800 66.07000 1.000 18.65853 ?  128 PHE A CD2 1 
ATOM   1011 C  CE1 . PHE A 1 128 ? 30.05000 35.83900 66.88500 1.000 20.78398 ?  128 PHE A CE1 1 
ATOM   1012 C  CE2 . PHE A 1 128 ? 28.26300 37.42800 66.90500 1.000 18.67506 ?  128 PHE A CE2 1 
ATOM   1013 C  CZ  . PHE A 1 128 ? 28.79100 36.22700 67.31000 1.000 18.45359 ?  128 PHE A CZ  1 
ATOM   1014 N  N   . LYS A 1 129 ? 33.97800 38.13700 65.48500 1.000 12.70408 ?  129 LYS A N   1 
ATOM   1015 C  CA  . LYS A 1 129 ? 34.91100 37.18600 66.09200 1.000 12.86141 ?  129 LYS A CA  1 
ATOM   1016 C  C   . LYS A 1 129 ? 35.69000 37.82200 67.23400 1.000 13.03059 ?  129 LYS A C   1 
ATOM   1017 O  O   . LYS A 1 129 ? 35.94200 37.17500 68.25800 1.000 15.38019 ?  129 LYS A O   1 
ATOM   1018 C  CB  . LYS A 1 129 ? 35.89200 36.68600 65.02100 1.000 12.47544 ?  129 LYS A CB  1 
ATOM   1019 C  CG  . LYS A 1 129 ? 36.91900 35.65600 65.48500 1.000 14.20973 ?  129 LYS A CG  1 
ATOM   1020 C  CD  . LYS A 1 129 ? 37.76100 35.18000 64.28400 1.000 15.62427 ?  129 LYS A CD  1 
ATOM   1021 C  CE  . LYS A 1 129 ? 38.91900 34.32600 64.72600 1.000 16.71618 ?  129 LYS A CE  1 
ATOM   1022 N  NZ  . LYS A 1 129 ? 39.55000 33.60500 63.55900 1.000 21.50269 ?  129 LYS A NZ  1 
ATOM   1023 N  N   . HIS A 1 130 ? 36.06900 39.08800 67.08200 1.000 11.41017 ?  130 HIS A N   1 
ATOM   1024 C  CA  . HIS A 1 130 ? 36.90700 39.76400 68.06300 1.000 11.88613 ?  130 HIS A CA  1 
ATOM   1025 C  C   . HIS A 1 130 ? 36.15200 40.73300 68.94900 1.000 14.65554 ?  130 HIS A C   1 
ATOM   1026 O  O   . HIS A 1 130 ? 36.77600 41.64500 69.50400 1.000 13.85025 ?  130 HIS A O   1 
ATOM   1027 C  CB  . HIS A 1 130 ? 38.06000 40.44000 67.34800 1.000 11.77408 ?  130 HIS A CB  1 
ATOM   1028 C  CG  . HIS A 1 130 ? 38.96400 39.46500 66.68500 1.000 13.83031 ?  130 HIS A CG  1 
ATOM   1029 N  ND1 . HIS A 1 130 ? 39.72100 38.56900 67.40300 1.000 14.37958 ?  130 HIS A ND1 1 
ATOM   1030 C  CD2 . HIS A 1 130 ? 39.19500 39.20000 65.37700 1.000 13.26729 ?  130 HIS A CD2 1 
ATOM   1031 C  CE1 . HIS A 1 130 ? 40.40600 37.80800 66.56600 1.000 15.24912 ?  130 HIS A CE1 1 
ATOM   1032 N  NE2 . HIS A 1 130 ? 40.10100 38.17000 65.32800 1.000 14.19326 ?  130 HIS A NE2 1 
ATOM   1033 N  N   . SER A 1 131 ? 34.84100 40.55100 69.10600 1.000 14.75502 ?  131 SER A N   1 
ATOM   1034 C  CA  . SER A 1 131 ? 34.05300 41.49100 69.90500 1.000 13.52305 ?  131 SER A CA  1 
ATOM   1035 C  C   . SER A 1 131 ? 34.57100 41.61100 71.33300 1.000 15.94037 ?  131 SER A C   1 
ATOM   1036 O  O   . SER A 1 131 ? 34.64800 42.72200 71.87300 1.000 16.14496 ?  131 SER A O   1 
ATOM   1037 C  CB  . SER A 1 131 ? 32.58900 41.06900 69.89800 1.000 18.65855 ?  131 SER A CB  1 
ATOM   1038 O  OG  . SER A 1 131 ? 32.06600 41.34800 68.63500 1.000 24.01203 ?  131 SER A OG  1 
ATOM   1039 N  N   . SER A 1 132 ? 34.89200 40.49000 71.97800 1.000 13.86218 ?  132 SER A N   1 
ATOM   1040 C  CA  . SER A 1 132 ? 35.33100 40.56700 73.36700 1.000 16.44738 ?  132 SER A CA  1 
ATOM   1041 C  C   . SER A 1 132 ? 36.66500 41.29400 73.48600 1.000 18.27770 ?  132 SER A C   1 
ATOM   1042 O  O   . SER A 1 132 ? 36.84800 42.13800 74.37800 1.000 18.72364 ?  132 SER A O   1 
ATOM   1043 C  CB  . SER A 1 132 ? 35.40000 39.15400 73.94700 1.000 17.97002 ?  132 SER A CB  1 
ATOM   1044 O  OG  . SER A 1 132 ? 35.83500 39.17800 75.29800 1.000 30.19901 ?  132 SER A OG  1 
ATOM   1045 N  N   . LEU A 1 133 ? 37.60800 40.99700 72.59300 1.000 16.25981 ?  133 LEU A N   1 
ATOM   1046 C  CA  . LEU A 1 133 ? 38.87900 41.71100 72.58900 1.000 17.13002 ?  133 LEU A CA  1 
ATOM   1047 C  C   . LEU A 1 133 ? 38.66000 43.21000 72.41600 1.000 17.53624 ?  133 LEU A C   1 
ATOM   1048 O  O   . LEU A 1 133 ? 39.25900 44.03000 73.12700 1.000 18.25784 ?  133 LEU A O   1 
ATOM   1049 C  CB  . LEU A 1 133 ? 39.76400 41.14900 71.46800 1.000 16.83386 ?  133 LEU A CB  1 
ATOM   1050 C  CG  . LEU A 1 133 ? 41.14700 41.72200 71.17500 1.000 16.12177 ?  133 LEU A CG  1 
ATOM   1051 C  CD1 . LEU A 1 133 ? 41.85000 40.78900 70.22000 1.000 18.19259 ?  133 LEU A CD1 1 
ATOM   1052 C  CD2 . LEU A 1 133 ? 41.14300 43.11300 70.54400 1.000 24.54191 ?  133 LEU A CD2 1 
ATOM   1053 N  N   . LEU A 1 134 ? 37.85600 43.59600 71.42500 1.000 12.78992 ?  134 LEU A N   1 
ATOM   1054 C  CA  . LEU A 1 134 ? 37.62800 45.01200 71.17400 1.000 14.76816 ?  134 LEU A CA  1 
ATOM   1055 C  C   . LEU A 1 134 ? 36.95700 45.68500 72.36200 1.000 18.17478 ?  134 LEU A C   1 
ATOM   1056 O  O   . LEU A 1 134 ? 37.19300 46.87500 72.61500 1.000 17.70991 ?  134 LEU A O   1 
ATOM   1057 C  CB  . LEU A 1 134 ? 36.78500 45.15900 69.90400 1.000 14.18266 ?  134 LEU A CB  1 
ATOM   1058 C  CG  . LEU A 1 134 ? 37.60900 44.83100 68.65200 1.000 15.30502 ?  134 LEU A CG  1 
ATOM   1059 C  CD1 . LEU A 1 134 ? 36.69600 44.62300 67.45700 1.000 13.88283 ?  134 LEU A CD1 1 
ATOM   1060 C  CD2 . LEU A 1 134 ? 38.62200 45.94300 68.34000 1.000 16.04960 ?  134 LEU A CD2 1 
ATOM   1061 N  N   . GLY A 1 135 ? 36.12400 44.94800 73.09500 1.000 16.43756 ?  135 GLY A N   1 
ATOM   1062 C  CA  . GLY A 1 135 ? 35.42400 45.52900 74.23700 1.000 18.42633 ?  135 GLY A CA  1 
ATOM   1063 C  C   . GLY A 1 135 ? 36.32100 45.86100 75.41100 1.000 22.88229 ?  135 GLY A C   1 
ATOM   1064 O  O   . GLY A 1 135 ? 35.91400 46.63700 76.28400 1.000 30.13211 ?  135 GLY A O   1 
ATOM   1065 N  N   . GLU A 1 136 ? 37.51200 45.33300 75.45300 1.000 23.61136 ?  136 GLU A N   1 
ATOM   1066 C  CA  . GLU A 1 136 ? 38.44800 45.62400 76.50700 1.000 25.97837 ?  136 GLU A CA  1 
ATOM   1067 C  C   . GLU A 1 136 ? 39.30200 46.81800 76.16900 1.000 29.76406 ?  136 GLU A C   1 
ATOM   1068 O  O   . GLU A 1 136 ? 40.13900 47.22300 76.95400 1.000 35.88894 ?  136 GLU A O   1 
ATOM   1069 C  CB  . GLU A 1 136 ? 39.33600 44.42300 76.72700 1.000 30.91460 ?  136 GLU A CB  1 
ATOM   1070 C  CG  . GLU A 1 136 ? 38.56600 43.15500 77.02600 1.000 31.42898 ?  136 GLU A CG  1 
ATOM   1071 C  CD  . GLU A 1 136 ? 39.44900 41.94200 77.25000 1.000 44.21403 ?  136 GLU A CD  1 
ATOM   1072 O  OE1 . GLU A 1 136 ? 40.66300 42.01100 76.99500 1.000 44.77861 ?  136 GLU A OE1 1 
ATOM   1073 O  OE2 . GLU A 1 136 ? 38.91300 40.90500 77.68500 1.000 50.88883 -1 136 GLU A OE2 1 
ATOM   1074 N  N   . MET A 1 137 ? 39.09700 47.39300 75.01900 1.000 21.98834 ?  137 MET A N   1 
ATOM   1075 C  CA  . MET A 1 137 ? 39.88100 48.51900 74.62000 1.000 22.26487 ?  137 MET A CA  1 
ATOM   1076 C  C   . MET A 1 137 ? 39.07100 49.81800 74.56500 1.000 22.21235 ?  137 MET A C   1 
ATOM   1077 O  O   . MET A 1 137 ? 37.87300 49.80400 74.45400 1.000 20.35129 ?  137 MET A O   1 
ATOM   1078 C  CB  . MET A 1 137 ? 40.52500 48.20400 73.28600 1.000 25.92474 ?  137 MET A CB  1 
ATOM   1079 C  CG  . MET A 1 137 ? 39.82200 48.67500 72.06400 1.000 29.15922 ?  137 MET A CG  1 
ATOM   1080 S  SD  . MET A 1 137 ? 40.99700 48.23800 70.78900 1.000 42.66811 ?  137 MET A SD  1 
ATOM   1081 C  CE  . MET A 1 137 ? 41.70600 46.75900 71.48700 1.000 16.39392 ?  137 MET A CE  1 
ATOM   1082 N  N   . PRO A 1 138 ? 39.77600 50.94400 74.70400 1.000 20.53988 ?  138 PRO A N   1 
ATOM   1083 C  CA  . PRO A 1 138 ? 39.09400 52.22700 74.59100 1.000 19.81131 ?  138 PRO A CA  1 
ATOM   1084 C  C   . PRO A 1 138 ? 38.38900 52.37700 73.26500 1.000 19.28295 ?  138 PRO A C   1 
ATOM   1085 O  O   . PRO A 1 138 ? 38.93700 51.99500 72.26600 1.000 17.18800 ?  138 PRO A O   1 
ATOM   1086 C  CB  . PRO A 1 138 ? 40.24200 53.24100 74.72400 1.000 20.31387 ?  138 PRO A CB  1 
ATOM   1087 C  CG  . PRO A 1 138 ? 41.29700 52.52100 75.47300 1.000 23.42400 ?  138 PRO A CG  1 
ATOM   1088 C  CD  . PRO A 1 138 ? 41.20000 51.09100 75.04100 1.000 24.46416 ?  138 PRO A CD  1 
ATOM   1089 N  N   . GLN A 1 139 ? 37.19900 52.97100 73.27900 1.000 18.61541 ?  139 GLN A N   1 
ATOM   1090 C  CA  . GLN A 1 139 ? 36.42400 53.03300 72.04400 1.000 18.22795 ?  139 GLN A CA  1 
ATOM   1091 C  C   . GLN A 1 139 ? 37.20500 53.69100 70.91100 1.000 18.65959 ?  139 GLN A C   1 
ATOM   1092 O  O   . GLN A 1 139 ? 37.09200 53.28100 69.75000 1.000 18.94823 ?  139 GLN A O   1 
ATOM   1093 C  CB  . GLN A 1 139 ? 35.09900 53.77500 72.28800 1.000 19.08724 ?  139 GLN A CB  1 
ATOM   1094 C  CG  . GLN A 1 139 ? 34.19400 53.85400 71.07800 1.000 21.08054 ?  139 GLN A CG  1 
ATOM   1095 C  CD  . GLN A 1 139 ? 34.51000 55.00900 70.15300 1.000 24.30310 ?  139 GLN A CD  1 
ATOM   1096 O  OE1 . GLN A 1 139 ? 35.10700 56.00300 70.56300 1.000 27.82536 ?  139 GLN A OE1 1 
ATOM   1097 N  NE2 . GLN A 1 139 ? 34.10400 54.88400 68.88900 1.000 25.62667 ?  139 GLN A NE2 1 
ATOM   1098 N  N   . GLU A 1 140 ? 37.98900 54.72500 71.21300 1.000 18.38224 ?  140 GLU A N   1 
ATOM   1099 C  CA  . GLU A 1 140 ? 38.58200 55.48900 70.12400 1.000 20.64374 ?  140 GLU A CA  1 
ATOM   1100 C  C   . GLU A 1 140 ? 39.63600 54.68800 69.37000 1.000 21.51369 ?  140 GLU A C   1 
ATOM   1101 O  O   . GLU A 1 140 ? 39.98900 55.06000 68.24600 1.000 23.64500 ?  140 GLU A O   1 
ATOM   1102 C  CB  . GLU A 1 140 ? 39.15900 56.80400 70.65600 1.000 26.98189 ?  140 GLU A CB  1 
ATOM   1103 C  CG  . GLU A 1 140 ? 39.99700 56.63000 71.90700 1.000 34.00604 ?  140 GLU A CG  1 
ATOM   1104 C  CD  . GLU A 1 140 ? 39.24500 57.00800 73.17900 1.000 42.63068 ?  140 GLU A CD  1 
ATOM   1105 O  OE1 . GLU A 1 140 ? 38.37400 56.22100 73.64900 1.000 27.51144 ?  140 GLU A OE1 1 
ATOM   1106 O  OE2 . GLU A 1 140 ? 39.53000 58.11200 73.70800 1.000 50.04564 -1 140 GLU A OE2 1 
ATOM   1107 N  N   . ARG A 1 141 ? 40.12500 53.59400 69.95100 1.000 17.83009 ?  141 ARG A N   1 
ATOM   1108 C  CA  . ARG A 1 141 ? 41.10800 52.73700 69.29700 1.000 19.60291 ?  141 ARG A CA  1 
ATOM   1109 C  C   . ARG A 1 141 ? 40.50400 51.52700 68.59300 1.000 20.01521 ?  141 ARG A C   1 
ATOM   1110 O  O   . ARG A 1 141 ? 41.23500 50.79700 67.90500 1.000 17.16494 ?  141 ARG A O   1 
ATOM   1111 C  CB  . ARG A 1 141 ? 42.19800 52.33200 70.29600 1.000 24.04855 ?  141 ARG A CB  1 
ATOM   1112 C  CG  . ARG A 1 141 ? 42.97500 53.59600 70.73900 1.000 32.99936 ?  141 ARG A CG  1 
ATOM   1113 C  CD  . ARG A 1 141 ? 44.14300 53.32200 71.64700 1.000 38.83304 ?  141 ARG A CD  1 
ATOM   1114 N  NE  . ARG A 1 141 ? 45.11900 52.41200 71.05800 1.000 49.90925 ?  141 ARG A NE  1 
ATOM   1115 C  CZ  . ARG A 1 141 ? 45.62700 51.36300 71.69100 1.000 48.30845 ?  141 ARG A CZ  1 
ATOM   1116 N  NH1 . ARG A 1 141 ? 45.27300 51.07100 72.93300 1.000 46.05609 ?  141 ARG A NH1 1 
ATOM   1117 N  NH2 . ARG A 1 141 ? 46.51500 50.59200 71.06700 1.000 47.92780 ?  141 ARG A NH2 1 
ATOM   1118 N  N   . ARG A 1 142 ? 39.18600 51.34000 68.68400 1.000 15.85392 ?  142 ARG A N   1 
ATOM   1119 C  CA  . ARG A 1 142 ? 38.58200 50.10800 68.17800 1.000 14.34739 ?  142 ARG A CA  1 
ATOM   1120 C  C   . ARG A 1 142 ? 38.62200 50.00500 66.65800 1.000 16.02921 ?  142 ARG A C   1 
ATOM   1121 O  O   . ARG A 1 142 ? 38.84000 48.90800 66.12700 1.000 14.19354 ?  142 ARG A O   1 
ATOM   1122 C  CB  . ARG A 1 142 ? 37.15200 49.96500 68.70400 1.000 14.70662 ?  142 ARG A CB  1 
ATOM   1123 C  CG  . ARG A 1 142 ? 37.13000 49.62400 70.18200 1.000 14.79632 ?  142 ARG A CG  1 
ATOM   1124 C  CD  . ARG A 1 142 ? 35.74400 49.58600 70.75800 1.000 16.87942 ?  142 ARG A CD  1 
ATOM   1125 N  NE  . ARG A 1 142 ? 35.82800 49.39400 72.20000 1.000 17.05849 ?  142 ARG A NE  1 
ATOM   1126 C  CZ  . ARG A 1 142 ? 34.83100 49.59200 73.05400 1.000 19.10424 ?  142 ARG A CZ  1 
ATOM   1127 N  NH1 . ARG A 1 142 ? 33.63300 49.99100 72.64700 1.000 19.48793 ?  142 ARG A NH1 1 
ATOM   1128 N  NH2 . ARG A 1 142 ? 35.04900 49.40100 74.35100 1.000 17.83502 ?  142 ARG A NH2 1 
ATOM   1129 N  N   . LEU A 1 143 ? 38.36800 51.10000 65.93400 1.000 14.34156 ?  143 LEU A N   1 
ATOM   1130 C  CA  . LEU A 1 143 ? 38.30300 50.99800 64.47500 1.000 14.38995 ?  143 LEU A CA  1 
ATOM   1131 C  C   . LEU A 1 143 ? 39.66700 50.65700 63.88600 1.000 14.86859 ?  143 LEU A C   1 
ATOM   1132 O  O   . LEU A 1 143 ? 39.78000 49.76500 63.03300 1.000 15.61782 ?  143 LEU A O   1 
ATOM   1133 C  CB  . LEU A 1 143 ? 37.76100 52.30000 63.88300 1.000 17.81740 ?  143 LEU A CB  1 
ATOM   1134 C  CG  . LEU A 1 143 ? 37.46100 52.25200 62.38800 1.000 21.92020 ?  143 LEU A CG  1 
ATOM   1135 C  CD1 . LEU A 1 143 ? 36.51100 51.11100 62.05800 1.000 21.47584 ?  143 LEU A CD1 1 
ATOM   1136 C  CD2 . LEU A 1 143 ? 36.87200 53.58100 61.92700 1.000 25.73121 ?  143 LEU A CD2 1 
ATOM   1137 N  N   . ASP A 1 144 ? 40.72300 51.31600 64.36300 1.000 14.85210 ?  144 ASP A N   1 
ATOM   1138 C  CA  . ASP A 1 144 ? 42.05200 50.97500 63.88600 1.000 14.72216 ?  144 ASP A CA  1 
ATOM   1139 C  C   . ASP A 1 144 ? 42.46100 49.57800 64.32700 1.000 13.95118 ?  144 ASP A C   1 
ATOM   1140 O  O   . ASP A 1 144 ? 43.18200 48.88600 63.59500 1.000 13.69280 ?  144 ASP A O   1 
ATOM   1141 C  CB  . ASP A 1 144 ? 43.06200 52.01100 64.34800 1.000 17.58566 ?  144 ASP A CB  1 
ATOM   1142 C  CG  . ASP A 1 144 ? 43.00000 53.30700 63.52400 1.000 20.31106 ?  144 ASP A CG  1 
ATOM   1143 O  OD1 . ASP A 1 144 ? 42.21800 53.38800 62.54300 1.000 20.74680 ?  144 ASP A OD1 1 
ATOM   1144 O  OD2 . ASP A 1 144 ? 43.74500 54.23800 63.88200 1.000 24.49885 -1 144 ASP A OD2 1 
ATOM   1145 N  N   . THR A 1 145 ? 42.03200 49.14100 65.51600 1.000 13.19675 ?  145 THR A N   1 
ATOM   1146 C  CA  . THR A 1 145 ? 42.33300 47.77400 65.92300 1.000 12.79370 ?  145 THR A CA  1 
ATOM   1147 C  C   . THR A 1 145 ? 41.64200 46.77200 65.00200 1.000 13.44201 ?  145 THR A C   1 
ATOM   1148 O  O   . THR A 1 145 ? 42.24100 45.76800 64.61300 1.000 13.60651 ?  145 THR A O   1 
ATOM   1149 C  CB  . THR A 1 145 ? 41.95100 47.54200 67.38500 1.000 15.10618 ?  145 THR A CB  1 
ATOM   1150 O  OG1 . THR A 1 145 ? 42.67900 48.47400 68.20800 1.000 15.22242 ?  145 THR A OG1 1 
ATOM   1151 C  CG2 . THR A 1 145 ? 42.32200 46.14000 67.79700 1.000 16.29138 ?  145 THR A CG2 1 
ATOM   1152 N  N   . LEU A 1 146 ? 40.40200 47.06000 64.59700 1.000 13.20995 ?  146 LEU A N   1 
ATOM   1153 C  CA  . LEU A 1 146 ? 39.73200 46.20200 63.62000 1.000 12.94243 ?  146 LEU A CA  1 
ATOM   1154 C  C   . LEU A 1 146 ? 40.48200 46.16600 62.28900 1.000 11.70575 ?  146 LEU A C   1 
ATOM   1155 O  O   . LEU A 1 146 ? 40.55000 45.11500 61.63300 1.000 11.82575 ?  146 LEU A O   1 
ATOM   1156 C  CB  . LEU A 1 146 ? 38.28000 46.63900 63.40200 1.000 12.83581 ?  146 LEU A CB  1 
ATOM   1157 C  CG  . LEU A 1 146 ? 37.50100 45.78000 62.40400 1.000 15.41819 ?  146 LEU A CG  1 
ATOM   1158 C  CD1 . LEU A 1 146 ? 37.41300 44.32700 62.89900 1.000 15.69124 ?  146 LEU A CD1 1 
ATOM   1159 C  CD2 . LEU A 1 146 ? 36.10400 46.36300 62.22000 1.000 15.77540 ?  146 LEU A CD2 1 
ATOM   1160 N  N   . CYS A 1 147 ? 41.02600 47.30000 61.85400 1.000 11.90782 ?  147 CYS A N   1 
ATOM   1161 C  CA  A CYS A 1 147 ? 41.85100 47.30500 60.65300 0.652 12.46097 ?  147 CYS A CA  1 
ATOM   1162 C  CA  B CYS A 1 147 ? 41.85000 47.30300 60.64900 0.348 12.47789 ?  147 CYS A CA  1 
ATOM   1163 C  C   . CYS A 1 147 ? 43.00600 46.32100 60.77600 1.000 12.53130 ?  147 CYS A C   1 
ATOM   1164 O  O   . CYS A 1 147 ? 43.30800 45.57300 59.82900 1.000 13.34294 ?  147 CYS A O   1 
ATOM   1165 C  CB  A CYS A 1 147 ? 42.41200 48.70700 60.46400 0.652 13.24757 ?  147 CYS A CB  1 
ATOM   1166 C  CB  B CYS A 1 147 ? 42.39800 48.70900 60.39900 0.348 13.28151 ?  147 CYS A CB  1 
ATOM   1167 S  SG  A CYS A 1 147 ? 43.40700 48.84500 59.01100 0.652 16.44658 ?  147 CYS A SG  1 
ATOM   1168 S  SG  B CYS A 1 147 ? 41.21800 49.87800 59.67900 0.348 15.52907 ?  147 CYS A SG  1 
ATOM   1169 N  N   . GLU A 1 148 ? 43.67800 46.32000 61.94000 1.000 11.99314 ?  148 GLU A N   1 
ATOM   1170 C  CA  . GLU A 1 148 ? 44.78700 45.39500 62.17900 1.000 11.74669 ?  148 GLU A CA  1 
ATOM   1171 C  C   . GLU A 1 148 ? 44.30200 43.95600 62.24900 1.000 11.35824 ?  148 GLU A C   1 
ATOM   1172 O  O   . GLU A 1 148 ? 44.92100 43.05300 61.66900 1.000 11.62416 ?  148 GLU A O   1 
ATOM   1173 C  CB  . GLU A 1 148 ? 45.52300 45.78000 63.47300 1.000 13.53577 ?  148 GLU A CB  1 
ATOM   1174 C  CG  . GLU A 1 148 ? 46.14800 47.16500 63.34900 1.000 13.46035 ?  148 GLU A CG  1 
ATOM   1175 C  CD  . GLU A 1 148 ? 46.63900 47.71100 64.67900 1.000 20.40770 ?  148 GLU A CD  1 
ATOM   1176 O  OE1 . GLU A 1 148 ? 46.21200 47.20100 65.73500 1.000 24.15914 ?  148 GLU A OE1 1 
ATOM   1177 O  OE2 . GLU A 1 148 ? 47.44000 48.66300 64.65700 1.000 19.88691 -1 148 GLU A OE2 1 
ATOM   1178 N  N   . LEU A 1 149 ? 43.21200 43.70900 62.99100 1.000 10.83582 ?  149 LEU A N   1 
ATOM   1179 C  CA  . LEU A 1 149 ? 42.68300 42.34500 63.07100 1.000 10.39584 ?  149 LEU A CA  1 
ATOM   1180 C  C   . LEU A 1 149 ? 42.30700 41.82700 61.69400 1.000 11.47013 ?  149 LEU A C   1 
ATOM   1181 O  O   . LEU A 1 149 ? 42.51000 40.64400 61.38900 1.000 12.41501 ?  149 LEU A O   1 
ATOM   1182 C  CB  . LEU A 1 149 ? 41.46100 42.31500 63.98500 1.000 12.04719 ?  149 LEU A CB  1 
ATOM   1183 C  CG  . LEU A 1 149 ? 41.79200 42.54600 65.47200 1.000 13.44367 ?  149 LEU A CG  1 
ATOM   1184 C  CD1 . LEU A 1 149 ? 40.53100 42.94600 66.21600 1.000 14.22895 ?  149 LEU A CD1 1 
ATOM   1185 C  CD2 . LEU A 1 149 ? 42.35700 41.30100 66.06400 1.000 13.74762 ?  149 LEU A CD2 1 
ATOM   1186 N  N   . ASN A 1 150 ? 41.73700 42.69000 60.85800 1.000 10.66647 ?  150 ASN A N   1 
ATOM   1187 C  CA  . ASN A 1 150 ? 41.41500 42.27500 59.49900 1.000 11.13602 ?  150 ASN A CA  1 
ATOM   1188 C  C   . ASN A 1 150 ? 42.65500 41.76900 58.78200 1.000 11.28115 ?  150 ASN A C   1 
ATOM   1189 O  O   . ASN A 1 150 ? 42.62600 40.69100 58.18200 1.000 11.24257 ?  150 ASN A O   1 
ATOM   1190 C  CB  . ASN A 1 150 ? 40.75500 43.42500 58.73500 1.000 11.25177 ?  150 ASN A CB  1 
ATOM   1191 C  CG  . ASN A 1 150 ? 40.28000 43.00300 57.35800 1.000 12.56895 ?  150 ASN A CG  1 
ATOM   1192 O  OD1 . ASN A 1 150 ? 39.61000 41.98000 57.21500 1.000 13.61782 ?  150 ASN A OD1 1 
ATOM   1193 N  ND2 . ASN A 1 150 ? 40.61900 43.79400 56.35300 1.000 11.45202 ?  150 ASN A ND2 1 
ATOM   1194 N  N   . VAL A 1 151 ? 43.76000 42.52000 58.84000 1.000 10.34474 ?  151 VAL A N   1 
ATOM   1195 C  CA  . VAL A 1 151 ? 44.99200 42.05600 58.19900 1.000 10.49032 ?  151 VAL A CA  1 
ATOM   1196 C  C   . VAL A 1 151 ? 45.40300 40.70500 58.75500 1.000 10.65445 ?  151 VAL A C   1 
ATOM   1197 O  O   . VAL A 1 151 ? 45.74100 39.78200 58.00300 1.000 11.17426 ?  151 VAL A O   1 
ATOM   1198 C  CB  . VAL A 1 151 ? 46.12300 43.08300 58.36000 1.000 10.08736 ?  151 VAL A CB  1 
ATOM   1199 C  CG1 . VAL A 1 151 ? 47.41800 42.50500 57.80200 1.000 11.54789 ?  151 VAL A CG1 1 
ATOM   1200 C  CG2 . VAL A 1 151 ? 45.77600 44.36700 57.68200 1.000 11.96003 ?  151 VAL A CG2 1 
ATOM   1201 N  N   . MET A 1 152 ? 45.41800 40.57500 60.09200 1.000 11.61344 ?  152 MET A N   1 
ATOM   1202 C  CA  . MET A 1 152 ? 45.85400 39.31400 60.68600 1.000 11.56406 ?  152 MET A CA  1 
ATOM   1203 C  C   . MET A 1 152 ? 44.99300 38.14300 60.22700 1.000 11.76945 ?  152 MET A C   1 
ATOM   1204 O  O   . MET A 1 152 ? 45.51400 37.05300 59.94100 1.000 11.72334 ?  152 MET A O   1 
ATOM   1205 C  CB  . MET A 1 152 ? 45.83100 39.39800 62.21200 1.000 14.48071 ?  152 MET A CB  1 
ATOM   1206 C  CG  . MET A 1 152 ? 46.71300 40.48200 62.76200 1.000 12.00532 ?  152 MET A CG  1 
ATOM   1207 S  SD  . MET A 1 152 ? 46.60800 40.48900 64.58700 1.000 17.93372 ?  152 MET A SD  1 
ATOM   1208 C  CE  . MET A 1 152 ? 47.71900 41.84900 64.95800 1.000 21.63112 ?  152 MET A CE  1 
ATOM   1209 N  N   . GLU A 1 153 ? 43.67400 38.34700 60.14000 1.000 10.47061 ?  153 GLU A N   1 
ATOM   1210 C  CA  . GLU A 1 153 ? 42.78600 37.28300 59.67800 1.000 11.07832 ?  153 GLU A CA  1 
ATOM   1211 C  C   . GLU A 1 153 ? 43.01300 36.95000 58.21000 1.000 9.59927  ?  153 GLU A C   1 
ATOM   1212 O  O   . GLU A 1 153 ? 42.90200 35.78400 57.82200 1.000 11.04293 ?  153 GLU A O   1 
ATOM   1213 C  CB  . GLU A 1 153 ? 41.32700 37.66800 59.87900 1.000 12.42489 ?  153 GLU A CB  1 
ATOM   1214 C  CG  . GLU A 1 153 ? 40.95900 37.83500 61.35900 1.000 12.59916 ?  153 GLU A CG  1 
ATOM   1215 C  CD  . GLU A 1 153 ? 40.89600 36.52100 62.13000 1.000 13.82801 ?  153 GLU A CD  1 
ATOM   1216 O  OE1 . GLU A 1 153 ? 40.74600 35.44300 61.52100 1.000 14.87158 ?  153 GLU A OE1 1 
ATOM   1217 O  OE2 . GLU A 1 153 ? 40.96000 36.56700 63.37200 1.000 15.57413 -1 153 GLU A OE2 1 
ATOM   1218 N  N   . GLN A 1 154 ? 43.33100 37.95600 57.38000 1.000 10.51462 ?  154 GLN A N   1 
ATOM   1219 C  CA  . GLN A 1 154 ? 43.62900 37.64300 55.98100 1.000 8.63870  ?  154 GLN A CA  1 
ATOM   1220 C  C   . GLN A 1 154 ? 44.94900 36.89100 55.83700 1.000 10.08560 ?  154 GLN A C   1 
ATOM   1221 O  O   . GLN A 1 154 ? 45.07100 36.01700 54.97100 1.000 10.90002 ?  154 GLN A O   1 
ATOM   1222 C  CB  . GLN A 1 154 ? 43.61100 38.88700 55.09300 1.000 11.05310 ?  154 GLN A CB  1 
ATOM   1223 C  CG  . GLN A 1 154 ? 42.33500 39.74200 55.22000 1.000 11.39812 ?  154 GLN A CG  1 
ATOM   1224 C  CD  . GLN A 1 154 ? 41.03300 38.93900 55.24000 1.000 11.68345 ?  154 GLN A CD  1 
ATOM   1225 O  OE1 . GLN A 1 154 ? 40.79200 38.09600 54.38100 1.000 11.72532 ?  154 GLN A OE1 1 
ATOM   1226 N  NE2 . GLN A 1 154 ? 40.18900 39.19000 56.23300 1.000 13.11216 ?  154 GLN A NE2 1 
ATOM   1227 N  N   . VAL A 1 155 ? 45.95100 37.21300 56.67200 1.000 9.51226  ?  155 VAL A N   1 
ATOM   1228 C  CA  . VAL A 1 155 ? 47.18900 36.42700 56.69400 1.000 11.60625 ?  155 VAL A CA  1 
ATOM   1229 C  C   . VAL A 1 155 ? 46.87900 34.98500 57.07200 1.000 9.65401  ?  155 VAL A C   1 
ATOM   1230 O  O   . VAL A 1 155 ? 47.38400 34.03100 56.45700 1.000 10.18175 ?  155 VAL A O   1 
ATOM   1231 C  CB  . VAL A 1 155 ? 48.20700 37.04900 57.67300 1.000 10.52622 ?  155 VAL A CB  1 
ATOM   1232 C  CG1 . VAL A 1 155 ? 49.37500 36.09300 57.93600 1.000 12.09470 ?  155 VAL A CG1 1 
ATOM   1233 C  CG2 . VAL A 1 155 ? 48.70000 38.39400 57.15800 1.000 10.57277 ?  155 VAL A CG2 1 
ATOM   1234 N  N   . TYR A 1 156 ? 46.04600 34.81100 58.10700 1.000 10.94239 ?  156 TYR A N   1 
ATOM   1235 C  CA  . TYR A 1 156 ? 45.64500 33.47700 58.54500 1.000 9.64985  ?  156 TYR A CA  1 
ATOM   1236 C  C   . TYR A 1 156 ? 44.92900 32.73000 57.42100 1.000 9.92080  ?  156 TYR A C   1 
ATOM   1237 O  O   . TYR A 1 156 ? 45.23500 31.56500 57.14000 1.000 11.37841 ?  156 TYR A O   1 
ATOM   1238 C  CB  . TYR A 1 156 ? 44.75300 33.62200 59.78800 1.000 10.91739 ?  156 TYR A CB  1 
ATOM   1239 C  CG  . TYR A 1 156 ? 44.58200 32.35400 60.58600 1.000 12.53903 ?  156 TYR A CG  1 
ATOM   1240 C  CD1 . TYR A 1 156 ? 45.67500 31.74600 61.18200 1.000 13.20128 ?  156 TYR A CD1 1 
ATOM   1241 C  CD2 . TYR A 1 156 ? 43.33800 31.76000 60.72000 1.000 19.48756 ?  156 TYR A CD2 1 
ATOM   1242 C  CE1 . TYR A 1 156 ? 45.53300 30.58200 61.92100 1.000 14.27005 ?  156 TYR A CE1 1 
ATOM   1243 C  CE2 . TYR A 1 156 ? 43.18000 30.57900 61.44400 1.000 19.69564 ?  156 TYR A CE2 1 
ATOM   1244 C  CZ  . TYR A 1 156 ? 44.28800 30.01000 62.04300 1.000 21.09037 ?  156 TYR A CZ  1 
ATOM   1245 O  OH  . TYR A 1 156 ? 44.14400 28.83600 62.75100 1.000 20.40575 ?  156 TYR A OH  1 
ATOM   1246 N  N   . ASN A 1 157 ? 43.99100 33.40200 56.74300 1.000 10.09528 ?  157 ASN A N   1 
ATOM   1247 C  CA  . ASN A 1 157 ? 43.31300 32.77000 55.60500 1.000 9.81514  ?  157 ASN A CA  1 
ATOM   1248 C  C   . ASN A 1 157 ? 44.30800 32.39100 54.51300 1.000 9.95616  ?  157 ASN A C   1 
ATOM   1249 O  O   . ASN A 1 157 ? 44.23600 31.29000 53.94500 1.000 10.73246 ?  157 ASN A O   1 
ATOM   1250 C  CB  . ASN A 1 157 ? 42.30800 33.75800 55.01600 1.000 10.01203 ?  157 ASN A CB  1 
ATOM   1251 C  CG  . ASN A 1 157 ? 41.11400 33.99200 55.90100 1.000 11.49853 ?  157 ASN A CG  1 
ATOM   1252 O  OD1 . ASN A 1 157 ? 40.95600 33.37500 56.95200 1.000 11.94313 ?  157 ASN A OD1 1 
ATOM   1253 N  ND2 . ASN A 1 157 ? 40.25400 34.93900 55.48100 1.000 12.67307 ?  157 ASN A ND2 1 
ATOM   1254 N  N   . LEU A 1 158 ? 45.22500 33.29900 54.18500 1.000 10.63546 ?  158 LEU A N   1 
ATOM   1255 C  CA  . LEU A 1 158 ? 46.21500 33.00800 53.14600 1.000 11.01561 ?  158 LEU A CA  1 
ATOM   1256 C  C   . LEU A 1 158 ? 47.03600 31.77300 53.51400 1.000 11.05425 ?  158 LEU A C   1 
ATOM   1257 O  O   . LEU A 1 158 ? 47.22500 30.86600 52.69400 1.000 11.86217 ?  158 LEU A O   1 
ATOM   1258 C  CB  . LEU A 1 158 ? 47.11100 34.23700 52.93500 1.000 11.37530 ?  158 LEU A CB  1 
ATOM   1259 C  CG  . LEU A 1 158 ? 48.29800 34.02700 51.99600 1.000 12.99066 ?  158 LEU A CG  1 
ATOM   1260 C  CD1 . LEU A 1 158 ? 47.81800 33.60600 50.61300 1.000 15.15376 ?  158 LEU A CD1 1 
ATOM   1261 C  CD2 . LEU A 1 158 ? 49.12800 35.30800 51.92300 1.000 15.35892 ?  158 LEU A CD2 1 
ATOM   1262 N  N   . GLY A 1 159 ? 47.49800 31.70100 54.76600 1.000 11.38872 ?  159 GLY A N   1 
ATOM   1263 C  CA  . GLY A 1 159 ? 48.27600 30.54100 55.18300 1.000 12.26520 ?  159 GLY A CA  1 
ATOM   1264 C  C   . GLY A 1 159 ? 47.49000 29.24300 55.19400 1.000 10.62517 ?  159 GLY A C   1 
ATOM   1265 O  O   . GLY A 1 159 ? 48.08200 28.16900 55.06500 1.000 11.78662 ?  159 GLY A O   1 
ATOM   1266 N  N   . HIS A 1 160 ? 46.16300 29.31400 55.34600 1.000 10.61941 ?  160 HIS A N   1 
ATOM   1267 C  CA  . HIS A 1 160 ? 45.30700 28.12800 55.30200 1.000 10.88496 ?  160 HIS A CA  1 
ATOM   1268 C  C   . HIS A 1 160 ? 44.84600 27.74000 53.90800 1.000 9.50869  ?  160 HIS A C   1 
ATOM   1269 O  O   . HIS A 1 160 ? 44.27000 26.65700 53.74100 1.000 12.05109 ?  160 HIS A O   1 
ATOM   1270 C  CB  . HIS A 1 160 ? 44.12100 28.28300 56.25700 1.000 11.91667 ?  160 HIS A CB  1 
ATOM   1271 C  CG  . HIS A 1 160 ? 44.51000 27.95600 57.66100 1.000 13.75897 ?  160 HIS A CG  1 
ATOM   1272 N  ND1 . HIS A 1 160 ? 44.62100 26.65400 58.10200 1.000 23.48253 ?  160 HIS A ND1 1 
ATOM   1273 C  CD2 . HIS A 1 160 ? 44.95100 28.73600 58.67500 1.000 19.42020 ?  160 HIS A CD2 1 
ATOM   1274 C  CE1 . HIS A 1 160 ? 45.03000 26.65500 59.35900 1.000 18.98142 ?  160 HIS A CE1 1 
ATOM   1275 N  NE2 . HIS A 1 160 ? 45.22700 27.90700 59.73400 1.000 16.08264 ?  160 HIS A NE2 1 
ATOM   1276 N  N   . SER A 1 161 ? 45.13200 28.56300 52.90800 1.000 9.89566  ?  161 SER A N   1 
ATOM   1277 C  CA  . SER A 1 161 ? 44.75500 28.18100 51.55500 1.000 11.42016 ?  161 SER A CA  1 
ATOM   1278 C  C   . SER A 1 161 ? 45.50900 26.92400 51.13900 1.000 10.48428 ?  161 SER A C   1 
ATOM   1279 O  O   . SER A 1 161 ? 46.61800 26.64700 51.62600 1.000 11.00693 ?  161 SER A O   1 
ATOM   1280 C  CB  . SER A 1 161 ? 45.06400 29.32400 50.57600 1.000 11.19194 ?  161 SER A CB  1 
ATOM   1281 O  OG  . SER A 1 161 ? 46.47200 29.53200 50.40100 1.000 11.80686 ?  161 SER A OG  1 
ATOM   1282 N  N   . THR A 1 162 ? 44.91800 26.16200 50.21400 1.000 11.88400 ?  162 THR A N   1 
ATOM   1283 C  CA  . THR A 1 162 ? 45.63600 24.97400 49.75700 1.000 11.81613 ?  162 THR A CA  1 
ATOM   1284 C  C   . THR A 1 162 ? 46.94000 25.35400 49.07400 1.000 13.16126 ?  162 THR A C   1 
ATOM   1285 O  O   . THR A 1 162 ? 47.89900 24.57700 49.10600 1.000 14.11835 ?  162 THR A O   1 
ATOM   1286 C  CB  . THR A 1 162 ? 44.78100 24.13800 48.80700 1.000 12.30510 ?  162 THR A CB  1 
ATOM   1287 O  OG1 . THR A 1 162 ? 44.36000 24.94400 47.70000 1.000 14.34431 ?  162 THR A OG1 1 
ATOM   1288 C  CG2 . THR A 1 162 ? 43.59600 23.54400 49.53300 1.000 14.86746 ?  162 THR A CG2 1 
ATOM   1289 N  N   . ILE A 1 163 ? 46.98800 26.52400 48.43800 1.000 11.54283 ?  163 ILE A N   1 
ATOM   1290 C  CA  . ILE A 1 163 ? 48.21100 26.96300 47.76800 1.000 12.26546 ?  163 ILE A CA  1 
ATOM   1291 C  C   . ILE A 1 163 ? 49.36100 27.06000 48.75900 1.000 14.31853 ?  163 ILE A C   1 
ATOM   1292 O  O   . ILE A 1 163 ? 50.46100 26.52400 48.53800 1.000 14.22978 ?  163 ILE A O   1 
ATOM   1293 C  CB  . ILE A 1 163 ? 47.96400 28.31400 47.07400 1.000 14.81872 ?  163 ILE A CB  1 
ATOM   1294 C  CG1 . ILE A 1 163 ? 46.79100 28.19700 46.09300 1.000 15.72140 ?  163 ILE A CG1 1 
ATOM   1295 C  CG2 . ILE A 1 163 ? 49.25200 28.80800 46.41600 1.000 17.21116 ?  163 ILE A CG2 1 
ATOM   1296 C  CD1 . ILE A 1 163 ? 46.07600 29.49500 45.90900 1.000 18.70453 ?  163 ILE A CD1 1 
ATOM   1297 N  N   . MET A 1 164 ? 49.14000 27.77200 49.86700 1.000 11.10642 ?  164 MET A N   1 
ATOM   1298 C  CA  . MET A 1 164 ? 50.22100 27.94600 50.83000 1.000 12.02161 ?  164 MET A CA  1 
ATOM   1299 C  C   . MET A 1 164 ? 50.52600 26.65800 51.57300 1.000 16.06401 ?  164 MET A C   1 
ATOM   1300 O  O   . MET A 1 164 ? 51.70300 26.33900 51.81500 1.000 15.98366 ?  164 MET A O   1 
ATOM   1301 C  CB  . MET A 1 164 ? 49.88300 29.05300 51.82200 1.000 11.29337 ?  164 MET A CB  1 
ATOM   1302 C  CG  . MET A 1 164 ? 49.94900 30.45000 51.20700 1.000 12.64306 ?  164 MET A CG  1 
ATOM   1303 S  SD  . MET A 1 164 ? 51.54700 30.80400 50.44100 1.000 15.65603 ?  164 MET A SD  1 
ATOM   1304 C  CE  . MET A 1 164 ? 52.65700 30.47800 51.79600 1.000 19.10785 ?  164 MET A CE  1 
ATOM   1305 N  N   . GLN A 1 165 ? 49.49000 25.91000 51.95300 1.000 14.38641 ?  165 GLN A N   1 
ATOM   1306 C  CA  . GLN A 1 165 ? 49.74600 24.64900 52.64800 1.000 15.28880 ?  165 GLN A CA  1 
ATOM   1307 C  C   . GLN A 1 165 ? 50.58700 23.70900 51.79300 1.000 16.70312 ?  165 GLN A C   1 
ATOM   1308 O  O   . GLN A 1 165 ? 51.53900 23.08900 52.28700 1.000 18.51246 ?  165 GLN A O   1 
ATOM   1309 C  CB  . GLN A 1 165 ? 48.41700 24.00100 53.05400 1.000 15.86445 ?  165 GLN A CB  1 
ATOM   1310 C  CG  . GLN A 1 165 ? 47.62500 24.80500 54.13000 1.000 17.81588 ?  165 GLN A CG  1 
ATOM   1311 C  CD  . GLN A 1 165 ? 48.08300 24.61000 55.58100 1.000 25.13396 ?  165 GLN A CD  1 
ATOM   1312 O  OE1 . GLN A 1 165 ? 48.24700 23.47700 56.03400 1.000 29.94025 ?  165 GLN A OE1 1 
ATOM   1313 N  NE2 . GLN A 1 165 ? 48.26100 25.71400 56.32700 1.000 20.99218 ?  165 GLN A NE2 1 
ATOM   1314 N  N   . SER A 1 166 ? 50.27600 23.61500 50.50600 1.000 14.96774 ?  166 SER A N   1 
ATOM   1315 C  CA  . SER A 1 166 ? 51.06000 22.78200 49.59300 1.000 18.54688 ?  166 SER A CA  1 
ATOM   1316 C  C   . SER A 1 166 ? 52.50100 23.27100 49.47300 1.000 25.01850 ?  166 SER A C   1 
ATOM   1317 O  O   . SER A 1 166 ? 53.44700 22.47300 49.51600 1.000 22.83884 ?  166 SER A O   1 
ATOM   1318 C  CB  . SER A 1 166 ? 50.38800 22.74300 48.22700 1.000 22.18125 ?  166 SER A CB  1 
ATOM   1319 O  OG  . SER A 1 166 ? 49.19100 21.99400 48.30900 1.000 26.61276 ?  166 SER A OG  1 
ATOM   1320 N  N   . ALA A 1 167 ? 52.69100 24.57800 49.28800 1.000 17.43294 ?  167 ALA A N   1 
ATOM   1321 C  CA  . ALA A 1 167 ? 54.04800 25.11400 49.16400 1.000 16.79284 ?  167 ALA A CA  1 
ATOM   1322 C  C   . ALA A 1 167 ? 54.88500 24.81100 50.40100 1.000 20.14300 ?  167 ALA A C   1 
ATOM   1323 O  O   . ALA A 1 167 ? 56.05500 24.42100 50.29800 1.000 21.22897 ?  167 ALA A O   1 
ATOM   1324 C  CB  . ALA A 1 167 ? 53.97500 26.62700 48.94200 1.000 18.73327 ?  167 ALA A CB  1 
ATOM   1325 N  N   . TRP A 1 168 ? 54.32400 25.02500 51.58100 1.000 18.82888 ?  168 TRP A N   1 
ATOM   1326 C  CA  . TRP A 1 168 ? 55.08000 24.76700 52.79700 1.000 17.08007 ?  168 TRP A CA  1 
ATOM   1327 C  C   . TRP A 1 168 ? 55.33800 23.28200 52.98900 1.000 25.11883 ?  168 TRP A C   1 
ATOM   1328 O  O   . TRP A 1 168 ? 56.43000 22.88900 53.42600 1.000 25.31754 ?  168 TRP A O   1 
ATOM   1329 C  CB  . TRP A 1 168 ? 54.32000 25.33100 53.96900 1.000 19.45525 ?  168 TRP A CB  1 
ATOM   1330 C  CG  . TRP A 1 168 ? 54.47000 26.80600 54.09900 1.000 16.10176 ?  168 TRP A CG  1 
ATOM   1331 C  CD1 . TRP A 1 168 ? 55.50600 27.58100 53.64400 1.000 17.68979 ?  168 TRP A CD1 1 
ATOM   1332 C  CD2 . TRP A 1 168 ? 53.55600 27.67600 54.73000 1.000 14.24206 ?  168 TRP A CD2 1 
ATOM   1333 N  NE1 . TRP A 1 168 ? 55.29200 28.89700 53.99200 1.000 16.60386 ?  168 TRP A NE1 1 
ATOM   1334 C  CE2 . TRP A 1 168 ? 54.09200 28.97900 54.65400 1.000 15.40965 ?  168 TRP A CE2 1 
ATOM   1335 C  CE3 . TRP A 1 168 ? 52.32100 27.48700 55.37100 1.000 14.43122 ?  168 TRP A CE3 1 
ATOM   1336 C  CZ2 . TRP A 1 168 ? 53.44800 30.07700 55.20700 1.000 16.17548 ?  168 TRP A CZ2 1 
ATOM   1337 C  CZ3 . TRP A 1 168 ? 51.68800 28.56900 55.89500 1.000 14.86527 ?  168 TRP A CZ3 1 
ATOM   1338 C  CH2 . TRP A 1 168 ? 52.24300 29.84800 55.81300 1.000 16.13117 ?  168 TRP A CH2 1 
ATOM   1339 N  N   . LYS A 1 169 ? 54.35200 22.43900 52.66600 1.000 20.96192 ?  169 LYS A N   1 
ATOM   1340 C  CA  . LYS A 1 169 ? 54.55300 20.99200 52.79600 1.000 24.23916 ?  169 LYS A CA  1 
ATOM   1341 C  C   . LYS A 1 169 ? 55.73100 20.51000 51.95600 1.000 26.71081 ?  169 LYS A C   1 
ATOM   1342 O  O   . LYS A 1 169 ? 56.48900 19.63400 52.39500 1.000 27.35324 ?  169 LYS A O   1 
ATOM   1343 C  CB  . LYS A 1 169 ? 53.27900 20.24100 52.39500 1.000 25.29862 ?  169 LYS A CB  1 
ATOM   1344 C  CG  . LYS A 1 169 ? 53.38800 18.71100 52.48400 1.000 33.88764 ?  169 LYS A CG  1 
ATOM   1345 C  CD  . LYS A 1 169 ? 52.03900 18.03600 52.22300 1.000 32.06318 ?  169 LYS A CD  1 
ATOM   1346 C  CE  . LYS A 1 169 ? 51.59300 18.26200 50.78600 1.000 45.40142 ?  169 LYS A CE  1 
ATOM   1347 N  NZ  . LYS A 1 169 ? 50.09900 18.28200 50.62500 1.000 52.45465 ?  169 LYS A NZ  1 
ATOM   1348 N  N   . ARG A 1 170 ? 55.89800 21.05400 50.74300 1.000 21.38588 ?  170 ARG A N   1 
ATOM   1349 C  CA  . ARG A 1 170 ? 56.95200 20.63200 49.83100 1.000 25.69565 ?  170 ARG A CA  1 
ATOM   1350 C  C   . ARG A 1 170 ? 58.27800 21.35300 50.07100 1.000 23.81188 ?  170 ARG A C   1 
ATOM   1351 O  O   . ARG A 1 170 ? 59.22800 21.14800 49.30700 1.000 30.79905 ?  170 ARG A O   1 
ATOM   1352 C  CB  . ARG A 1 170 ? 56.49800 20.75200 48.37000 1.000 25.02648 ?  170 ARG A CB  1 
ATOM   1353 C  CG  . ARG A 1 170 ? 56.44300 22.18100 47.80500 1.000 29.31748 ?  170 ARG A CG  1 
ATOM   1354 C  CD  . ARG A 1 170 ? 55.91200 22.21400 46.35800 1.000 30.23354 ?  170 ARG A CD  1 
ATOM   1355 N  NE  . ARG A 1 170 ? 55.79700 23.57400 45.83200 1.000 28.36360 ?  170 ARG A NE  1 
ATOM   1356 C  CZ  . ARG A 1 170 ? 54.64900 24.21400 45.63400 1.000 27.09550 ?  170 ARG A CZ  1 
ATOM   1357 N  NH1 . ARG A 1 170 ? 53.48300 23.61900 45.84300 1.000 25.55905 ?  170 ARG A NH1 1 
ATOM   1358 N  NH2 . ARG A 1 170 ? 54.67500 25.48800 45.23200 1.000 22.72845 ?  170 ARG A NH2 1 
ATOM   1359 N  N   . GLY A 1 171 ? 58.37200 22.16200 51.12400 1.000 24.18601 ?  171 GLY A N   1 
ATOM   1360 C  CA  . GLY A 1 171 ? 59.62000 22.82800 51.44800 1.000 29.25129 ?  171 GLY A CA  1 
ATOM   1361 C  C   . GLY A 1 171 ? 59.96000 24.04400 50.61600 1.000 32.14803 ?  171 GLY A C   1 
ATOM   1362 O  O   . GLY A 1 171 ? 61.12800 24.43800 50.56200 1.000 23.03426 ?  171 GLY A O   1 
ATOM   1363 N  N   . GLN A 1 172 ? 58.98700 24.67200 49.97100 1.000 25.50992 ?  172 GLN A N   1 
ATOM   1364 C  CA  . GLN A 1 172 ? 59.26500 25.93800 49.31300 1.000 23.83788 ?  172 GLN A CA  1 
ATOM   1365 C  C   . GLN A 1 172 ? 59.33800 27.05000 50.35100 1.000 21.42666 ?  172 GLN A C   1 
ATOM   1366 O  O   . GLN A 1 172 ? 58.53700 27.10700 51.28800 1.000 23.54995 ?  172 GLN A O   1 
ATOM   1367 C  CB  . GLN A 1 172 ? 58.18900 26.26300 48.28100 1.000 21.84459 ?  172 GLN A CB  1 
ATOM   1368 C  CG  . GLN A 1 172 ? 58.58500 27.42200 47.40600 1.000 24.41545 ?  172 GLN A CG  1 
ATOM   1369 C  CD  . GLN A 1 172 ? 57.65200 27.64100 46.24400 1.000 24.74237 ?  172 GLN A CD  1 
ATOM   1370 O  OE1 . GLN A 1 172 ? 57.15200 26.69000 45.63600 1.000 28.28352 ?  172 GLN A OE1 1 
ATOM   1371 N  NE2 . GLN A 1 172 ? 57.43400 28.90600 45.90100 1.000 21.01879 ?  172 GLN A NE2 1 
ATOM   1372 N  N   . LYS A 1 173 ? 60.31600 27.93000 50.19000 1.000 19.54665 ?  173 LYS A N   1 
ATOM   1373 C  CA  . LYS A 1 173 ? 60.51300 29.02900 51.12800 1.000 18.37485 ?  173 LYS A CA  1 
ATOM   1374 C  C   . LYS A 1 173 ? 59.60000 30.17600 50.71600 1.000 18.64802 ?  173 LYS A C   1 
ATOM   1375 O  O   . LYS A 1 173 ? 59.83700 30.83200 49.69400 1.000 18.40033 ?  173 LYS A O   1 
ATOM   1376 C  CB  . LYS A 1 173 ? 61.97100 29.47200 51.11700 1.000 21.33420 ?  173 LYS A CB  1 
ATOM   1377 C  CG  . LYS A 1 173 ? 62.86300 28.78800 52.15200 1.000 34.82866 ?  173 LYS A CG  1 
ATOM   1378 C  CD  . LYS A 1 173 ? 63.10600 27.33000 51.83400 1.000 41.97120 ?  173 LYS A CD  1 
ATOM   1379 C  CE  . LYS A 1 173 ? 64.21500 26.75500 52.71200 1.000 43.06984 ?  173 LYS A CE  1 
ATOM   1380 N  NZ  . LYS A 1 173 ? 64.65400 25.41400 52.22300 1.000 50.62070 ?  173 LYS A NZ  1 
ATOM   1381 N  N   . VAL A 1 174 ? 58.53500 30.39200 51.48500 1.000 15.75907 ?  174 VAL A N   1 
ATOM   1382 C  CA  . VAL A 1 174 ? 57.64900 31.54000 51.30300 1.000 14.58610 ?  174 VAL A CA  1 
ATOM   1383 C  C   . VAL A 1 174 ? 57.30500 32.05300 52.69000 1.000 14.17733 ?  174 VAL A C   1 
ATOM   1384 O  O   . VAL A 1 174 ? 56.94800 31.26600 53.57500 1.000 15.80904 ?  174 VAL A O   1 
ATOM   1385 C  CB  . VAL A 1 174 ? 56.33600 31.16700 50.58400 1.000 16.37101 ?  174 VAL A CB  1 
ATOM   1386 C  CG1 . VAL A 1 174 ? 55.53100 32.43500 50.26600 1.000 15.84830 ?  174 VAL A CG1 1 
ATOM   1387 C  CG2 . VAL A 1 174 ? 56.56000 30.33100 49.34900 1.000 20.54953 ?  174 VAL A CG2 1 
ATOM   1388 N  N   . THR A 1 175 ? 57.41600 33.35900 52.89400 1.000 13.13036 ?  175 THR A N   1 
ATOM   1389 C  CA  . THR A 1 175 ? 57.07000 33.97300 54.16200 1.000 12.44402 ?  175 THR A CA  1 
ATOM   1390 C  C   . THR A 1 175 ? 55.91400 34.92700 53.92900 1.000 13.30733 ?  175 THR A C   1 
ATOM   1391 O  O   . THR A 1 175 ? 55.92700 35.67700 52.95100 1.000 14.76680 ?  175 THR A O   1 
ATOM   1392 C  CB  . THR A 1 175 ? 58.27700 34.77300 54.68100 1.000 15.47703 ?  175 THR A CB  1 
ATOM   1393 O  OG1 . THR A 1 175 ? 59.41500 33.89700 54.79200 1.000 17.97490 ?  175 THR A OG1 1 
ATOM   1394 C  CG2 . THR A 1 175 ? 57.98400 35.36800 56.02500 1.000 15.56208 ?  175 THR A CG2 1 
ATOM   1395 N  N   . ILE A 1 176 ? 54.91100 34.90600 54.81500 1.000 12.48844 ?  176 ILE A N   1 
ATOM   1396 C  CA  A ILE A 1 176 ? 53.75800 35.81200 54.76400 0.533 12.27581 ?  176 ILE A CA  1 
ATOM   1397 C  CA  B ILE A 1 176 ? 53.81800 35.85400 54.72000 0.467 12.26386 ?  176 ILE A CA  1 
ATOM   1398 C  C   . ILE A 1 176 ? 53.87500 36.81600 55.89700 1.000 13.05069 ?  176 ILE A C   1 
ATOM   1399 O  O   . ILE A 1 176 ? 54.25500 36.45000 57.01200 1.000 12.64164 ?  176 ILE A O   1 
ATOM   1400 C  CB  A ILE A 1 176 ? 52.39800 35.09400 54.91700 0.533 12.67773 ?  176 ILE A CB  1 
ATOM   1401 C  CB  B ILE A 1 176 ? 52.45700 35.15400 54.53600 0.467 12.78213 ?  176 ILE A CB  1 
ATOM   1402 C  CG1 A ILE A 1 176 ? 52.27600 33.87300 54.01100 0.533 14.24442 ?  176 ILE A CG1 1 
ATOM   1403 C  CG1 B ILE A 1 176 ? 52.07800 34.34500 55.76800 0.467 11.67824 ?  176 ILE A CG1 1 
ATOM   1404 C  CG2 A ILE A 1 176 ? 51.24000 36.10000 54.68600 0.533 11.61496 ?  176 ILE A CG2 1 
ATOM   1405 C  CG2 B ILE A 1 176 ? 52.53400 34.22600 53.33200 0.467 15.42021 ?  176 ILE A CG2 1 
ATOM   1406 C  CD1 A ILE A 1 176 ? 50.99900 33.09100 54.27400 0.533 14.30364 ?  176 ILE A CD1 1 
ATOM   1407 C  CD1 B ILE A 1 176 ? 50.78200 33.53200 55.56300 0.467 13.91179 ?  176 ILE A CD1 1 
ATOM   1408 N  N   . HIS A 1 177 ? 53.51100 38.06300 55.62600 1.000 11.08493 ?  177 HIS A N   1 
ATOM   1409 C  CA  . HIS A 1 177 ? 53.61100 39.16300 56.57100 1.000 11.44001 ?  177 HIS A CA  1 
ATOM   1410 C  C   . HIS A 1 177 ? 52.30500 39.93700 56.59900 1.000 13.56620 ?  177 HIS A C   1 
ATOM   1411 O  O   . HIS A 1 177 ? 51.62300 40.05700 55.58100 1.000 12.56243 ?  177 HIS A O   1 
ATOM   1412 C  CB  . HIS A 1 177 ? 54.69300 40.16300 56.15600 1.000 12.72889 ?  177 HIS A CB  1 
ATOM   1413 C  CG  . HIS A 1 177 ? 56.00400 39.53000 55.81300 1.000 13.60341 ?  177 HIS A CG  1 
ATOM   1414 N  ND1 . HIS A 1 177 ? 57.06200 39.46600 56.70100 1.000 15.06571 ?  177 HIS A ND1 1 
ATOM   1415 C  CD2 . HIS A 1 177 ? 56.42700 38.92800 54.67300 1.000 14.54804 ?  177 HIS A CD2 1 
ATOM   1416 C  CE1 . HIS A 1 177 ? 58.08300 38.86700 56.11300 1.000 14.62956 ?  177 HIS A CE1 1 
ATOM   1417 N  NE2 . HIS A 1 177 ? 57.72100 38.51600 54.88700 1.000 15.55026 ?  177 HIS A NE2 1 
ATOM   1418 N  N   . GLY A 1 178 ? 51.98500 40.48800 57.76800 1.000 11.51893 ?  178 GLY A N   1 
ATOM   1419 C  CA  . GLY A 1 178 ? 50.85200 41.37400 57.93200 1.000 11.10100 ?  178 GLY A CA  1 
ATOM   1420 C  C   . GLY A 1 178 ? 51.27900 42.74700 58.40900 1.000 12.81450 ?  178 GLY A C   1 
ATOM   1421 O  O   . GLY A 1 178 ? 51.86400 42.87000 59.49000 1.000 12.71684 ?  178 GLY A O   1 
ATOM   1422 N  N   . TRP A 1 179 ? 51.00100 43.77900 57.61600 1.000 11.15685 ?  179 TRP A N   1 
ATOM   1423 C  CA  . TRP A 1 179 ? 51.42100 45.14500 57.90000 1.000 10.91009 ?  179 TRP A CA  1 
ATOM   1424 C  C   . TRP A 1 179 ? 50.22000 46.08100 57.84000 1.000 10.93125 ?  179 TRP A C   1 
ATOM   1425 O  O   . TRP A 1 179 ? 49.17500 45.74900 57.26900 1.000 11.71231 ?  179 TRP A O   1 
ATOM   1426 C  CB  . TRP A 1 179 ? 52.43900 45.63100 56.85400 1.000 11.69848 ?  179 TRP A CB  1 
ATOM   1427 C  CG  . TRP A 1 179 ? 53.76900 44.93900 56.86600 1.000 13.20922 ?  179 TRP A CG  1 
ATOM   1428 C  CD1 . TRP A 1 179 ? 54.22600 44.02500 57.78300 1.000 13.26570 ?  179 TRP A CD1 1 
ATOM   1429 C  CD2 . TRP A 1 179 ? 54.83200 45.14100 55.92900 1.000 13.17990 ?  179 TRP A CD2 1 
ATOM   1430 N  NE1 . TRP A 1 179 ? 55.51600 43.63800 57.44600 1.000 15.14145 ?  179 TRP A NE1 1 
ATOM   1431 C  CE2 . TRP A 1 179 ? 55.90200 44.31200 56.32000 1.000 13.32540 ?  179 TRP A CE2 1 
ATOM   1432 C  CE3 . TRP A 1 179 ? 54.97600 45.94000 54.78700 1.000 15.70353 ?  179 TRP A CE3 1 
ATOM   1433 C  CZ2 . TRP A 1 179 ? 57.10900 44.26300 55.60900 1.000 16.53553 ?  179 TRP A CZ2 1 
ATOM   1434 C  CZ3 . TRP A 1 179 ? 56.19400 45.89000 54.07500 1.000 16.20193 ?  179 TRP A CZ3 1 
ATOM   1435 C  CH2 . TRP A 1 179 ? 57.22600 45.04800 54.49000 1.000 16.62266 ?  179 TRP A CH2 1 
ATOM   1436 N  N   . ALA A 1 180 ? 50.38600 47.28700 58.39100 1.000 11.12469 ?  180 ALA A N   1 
ATOM   1437 C  CA  . ALA A 1 180 ? 49.41300 48.35300 58.22000 1.000 12.03269 ?  180 ALA A CA  1 
ATOM   1438 C  C   . ALA A 1 180 ? 50.14700 49.68500 58.23700 1.000 12.83307 ?  180 ALA A C   1 
ATOM   1439 O  O   . ALA A 1 180 ? 51.23600 49.80000 58.80400 1.000 14.73361 ?  180 ALA A O   1 
ATOM   1440 C  CB  . ALA A 1 180 ? 48.31400 48.33900 59.32000 1.000 13.49694 ?  180 ALA A CB  1 
ATOM   1441 N  N   . TYR A 1 181 ? 49.53100 50.70400 57.64200 1.000 13.56016 ?  181 TYR A N   1 
ATOM   1442 C  CA  . TYR A 1 181 ? 50.04300 52.07200 57.75800 1.000 13.20996 ?  181 TYR A CA  1 
ATOM   1443 C  C   . TYR A 1 181 ? 48.86100 53.03000 57.78300 1.000 13.97127 ?  181 TYR A C   1 
ATOM   1444 O  O   . TYR A 1 181 ? 47.74500 52.66900 57.42800 1.000 12.09110 ?  181 TYR A O   1 
ATOM   1445 C  CB  . TYR A 1 181 ? 50.97700 52.45400 56.58600 1.000 13.94450 ?  181 TYR A CB  1 
ATOM   1446 C  CG  . TYR A 1 181 ? 50.21400 52.64200 55.28900 1.000 12.63342 ?  181 TYR A CG  1 
ATOM   1447 C  CD1 . TYR A 1 181 ? 49.85900 51.54500 54.51200 1.000 13.58450 ?  181 TYR A CD1 1 
ATOM   1448 C  CD2 . TYR A 1 181 ? 49.82000 53.90100 54.86600 1.000 13.19412 ?  181 TYR A CD2 1 
ATOM   1449 C  CE1 . TYR A 1 181 ? 49.12000 51.69600 53.35100 1.000 13.84192 ?  181 TYR A CE1 1 
ATOM   1450 C  CE2 . TYR A 1 181 ? 49.07300 54.07200 53.71400 1.000 15.85600 ?  181 TYR A CE2 1 
ATOM   1451 C  CZ  . TYR A 1 181 ? 48.73400 52.96200 52.95000 1.000 15.78441 ?  181 TYR A CZ  1 
ATOM   1452 O  OH  . TYR A 1 181 ? 48.00200 53.13500 51.79400 1.000 17.55779 ?  181 TYR A OH  1 
ATOM   1453 N  N   . GLY A 1 182 ? 49.10800 54.27200 58.21100 1.000 12.40766 ?  182 GLY A N   1 
ATOM   1454 C  CA  . GLY A 1 182 ? 48.11800 55.32000 58.11200 1.000 13.18947 ?  182 GLY A CA  1 
ATOM   1455 C  C   . GLY A 1 182 ? 48.69000 56.51500 57.37200 1.000 13.82277 ?  182 GLY A C   1 
ATOM   1456 O  O   . GLY A 1 182 ? 49.90800 56.61900 57.16100 1.000 14.22709 ?  182 GLY A O   1 
ATOM   1457 N  N   . ILE A 1 183 ? 47.79500 57.41300 56.97900 1.000 14.26248 ?  183 ILE A N   1 
ATOM   1458 C  CA  . ILE A 1 183 ? 48.21200 58.59200 56.22300 1.000 14.95643 ?  183 ILE A CA  1 
ATOM   1459 C  C   . ILE A 1 183 ? 48.68900 59.80500 57.10900 1.000 16.73511 ?  183 ILE A C   1 
ATOM   1460 O  O   . ILE A 1 183 ? 48.99400 60.98600 56.73700 1.000 18.23065 ?  183 ILE A O   1 
ATOM   1461 C  CB  . ILE A 1 183 ? 47.10800 59.02700 55.23200 1.000 16.38866 ?  183 ILE A CB  1 
ATOM   1462 C  CG1 . ILE A 1 183 ? 45.79700 59.30900 55.94000 1.000 19.70339 ?  183 ILE A CG1 1 
ATOM   1463 C  CG2 . ILE A 1 183 ? 46.90800 57.94900 54.17600 1.000 19.53830 ?  183 ILE A CG2 1 
ATOM   1464 C  CD1 . ILE A 1 183 ? 44.86000 60.15400 55.11200 1.000 31.03849 ?  183 ILE A CD1 1 
ATOM   1465 N  N   . HIS A 1 184 ? 48.75400 59.50800 58.39600 1.000 14.28320 ?  184 HIS A N   1 
ATOM   1466 C  CA  . HIS A 1 184 ? 49.26800 60.52400 59.30700 1.000 14.13567 ?  184 HIS A CA  1 
ATOM   1467 C  C   . HIS A 1 184 ? 50.78300 60.61900 59.16000 1.000 16.34504 ?  184 HIS A C   1 
ATOM   1468 O  O   . HIS A 1 184 ? 51.35500 61.64200 59.41700 1.000 17.26231 ?  184 HIS A O   1 
ATOM   1469 C  CB  . HIS A 1 184 ? 48.86700 60.19400 60.75300 1.000 15.12943 ?  184 HIS A CB  1 
ATOM   1470 C  CG  . HIS A 1 184 ? 49.27700 58.83200 61.21200 1.000 14.57760 ?  184 HIS A CG  1 
ATOM   1471 N  ND1 . HIS A 1 184 ? 48.61900 57.68600 60.82600 1.000 16.95771 ?  184 HIS A ND1 1 
ATOM   1472 C  CD2 . HIS A 1 184 ? 50.27000 58.43300 62.03900 1.000 15.67723 ?  184 HIS A CD2 1 
ATOM   1473 C  CE1 . HIS A 1 184 ? 49.18900 56.64000 61.39300 1.000 15.55775 ?  184 HIS A CE1 1 
ATOM   1474 N  NE2 . HIS A 1 184 ? 50.19400 57.06600 62.13500 1.000 17.16335 ?  184 HIS A NE2 1 
ATOM   1475 N  N   . ASP A 1 185 ? 51.42200 59.54800 58.73700 1.000 14.23296 ?  185 ASP A N   1 
ATOM   1476 C  CA  . ASP A 1 185 ? 52.88100 59.55700 58.53400 1.000 14.86719 ?  185 ASP A CA  1 
ATOM   1477 C  C   . ASP A 1 185 ? 53.43900 58.55100 57.51000 1.000 15.08331 ?  185 ASP A C   1 
ATOM   1478 O  O   . ASP A 1 185 ? 54.61500 58.56300 57.24400 1.000 16.42155 ?  185 ASP A O   1 
ATOM   1479 C  CB  . ASP A 1 185 ? 53.61300 59.35600 59.86700 1.000 16.40698 ?  185 ASP A CB  1 
ATOM   1480 C  CG  . ASP A 1 185 ? 53.22600 58.07400 60.56700 1.000 17.24629 ?  185 ASP A CG  1 
ATOM   1481 O  OD1 . ASP A 1 185 ? 52.54700 57.22800 59.96500 1.000 16.21880 ?  185 ASP A OD1 1 
ATOM   1482 O  OD2 . ASP A 1 185 ? 53.60900 57.92200 61.73300 1.000 16.81343 -1 185 ASP A OD2 1 
ATOM   1483 N  N   . GLY A 1 186 ? 52.58800 57.69200 56.96100 1.000 13.99392 ?  186 GLY A N   1 
ATOM   1484 C  CA  . GLY A 1 186 ? 53.06300 56.67000 56.03300 1.000 13.12446 ?  186 GLY A CA  1 
ATOM   1485 C  C   . GLY A 1 186 ? 53.96800 55.60500 56.63000 1.000 13.82926 ?  186 GLY A C   1 
ATOM   1486 O  O   . GLY A 1 186 ? 54.60700 54.89100 55.90200 1.000 14.57441 ?  186 GLY A O   1 
ATOM   1487 N  N   . LEU A 1 187 ? 53.97800 55.51000 57.93500 1.000 15.18837 ?  187 LEU A N   1 
ATOM   1488 C  CA  . LEU A 1 187 ? 54.90400 54.61000 58.60300 1.000 14.70453 ?  187 LEU A CA  1 
ATOM   1489 C  C   . LEU A 1 187 ? 54.27800 53.22500 58.72800 1.000 15.72374 ?  187 LEU A C   1 
ATOM   1490 O  O   . LEU A 1 187 ? 53.19200 53.07400 59.30000 1.000 16.84230 ?  187 LEU A O   1 
ATOM   1491 C  CB  . LEU A 1 187 ? 55.26500 55.16800 59.98200 1.000 17.01467 ?  187 LEU A CB  1 
ATOM   1492 C  CG  . LEU A 1 187 ? 56.41500 54.51800 60.73700 1.000 19.65425 ?  187 LEU A CG  1 
ATOM   1493 C  CD1 . LEU A 1 187 ? 57.71300 54.61900 59.94600 1.000 18.75137 ?  187 LEU A CD1 1 
ATOM   1494 C  CD2 . LEU A 1 187 ? 56.57500 55.20300 62.09800 1.000 21.70814 ?  187 LEU A CD2 1 
ATOM   1495 N  N   . LEU A 1 188 ? 54.95100 52.22500 58.17100 1.000 14.77928 ?  188 LEU A N   1 
ATOM   1496 C  CA  . LEU A 1 188 ? 54.47500 50.85200 58.26500 1.000 14.83937 ?  188 LEU A CA  1 
ATOM   1497 C  C   . LEU A 1 188 ? 54.60500 50.33500 59.69100 1.000 15.82403 ?  188 LEU A C   1 
ATOM   1498 O  O   . LEU A 1 188 ? 55.62500 50.54900 60.36000 1.000 20.42271 ?  188 LEU A O   1 
ATOM   1499 C  CB  . LEU A 1 188 ? 55.29300 49.95900 57.32600 1.000 15.25763 ?  188 LEU A CB  1 
ATOM   1500 C  CG  . LEU A 1 188 ? 54.96200 50.13800 55.84400 1.000 17.28246 ?  188 LEU A CG  1 
ATOM   1501 C  CD1 . LEU A 1 188 ? 56.03500 49.51000 54.96100 1.000 18.07636 ?  188 LEU A CD1 1 
ATOM   1502 C  CD2 . LEU A 1 188 ? 53.59300 49.55100 55.50100 1.000 14.81357 ?  188 LEU A CD2 1 
ATOM   1503 N  N   . ARG A 1 189 ? 53.55600 49.66800 60.16500 1.000 16.02196 ?  189 ARG A N   1 
ATOM   1504 C  CA  . ARG A 1 189 ? 53.57700 48.90900 61.41400 1.000 13.96636 ?  189 ARG A CA  1 
ATOM   1505 C  C   . ARG A 1 189 ? 53.56000 47.43000 61.05000 1.000 16.08398 ?  189 ARG A C   1 
ATOM   1506 O  O   . ARG A 1 189 ? 52.66200 46.97900 60.33200 1.000 15.45625 ?  189 ARG A O   1 
ATOM   1507 C  CB  . ARG A 1 189 ? 52.36400 49.25300 62.27800 1.000 16.72340 ?  189 ARG A CB  1 
ATOM   1508 C  CG  . ARG A 1 189 ? 52.22700 48.40400 63.52500 1.000 21.36748 ?  189 ARG A CG  1 
ATOM   1509 C  CD  . ARG A 1 189 ? 51.10700 48.92300 64.43500 1.000 27.67942 ?  189 ARG A CD  1 
ATOM   1510 N  NE  . ARG A 1 189 ? 51.51900 50.08500 65.21600 1.000 38.14414 ?  189 ARG A NE  1 
ATOM   1511 C  CZ  . ARG A 1 189 ? 51.12300 51.33200 64.98800 1.000 38.01700 ?  189 ARG A CZ  1 
ATOM   1512 N  NH1 . ARG A 1 189 ? 50.27800 51.62700 64.01200 1.000 29.27797 ?  189 ARG A NH1 1 
ATOM   1513 N  NH2 . ARG A 1 189 ? 51.58300 52.31100 65.76400 1.000 32.94307 ?  189 ARG A NH2 1 
ATOM   1514 N  N   . ASP A 1 190 ? 54.55500 46.68200 61.51300 1.000 14.31894 ?  190 ASP A N   1 
ATOM   1515 C  CA  . ASP A 1 190 ? 54.55300 45.23100 61.33800 1.000 12.88165 ?  190 ASP A CA  1 
ATOM   1516 C  C   . ASP A 1 190 ? 53.68100 44.63800 62.43000 1.000 15.17823 ?  190 ASP A C   1 
ATOM   1517 O  O   . ASP A 1 190 ? 53.94100 44.84200 63.62000 1.000 16.17763 ?  190 ASP A O   1 
ATOM   1518 C  CB  . ASP A 1 190 ? 55.98400 44.69900 61.44800 1.000 15.18879 ?  190 ASP A CB  1 
ATOM   1519 C  CG  . ASP A 1 190 ? 56.11000 43.23900 61.03500 1.000 20.43522 ?  190 ASP A CG  1 
ATOM   1520 O  OD1 . ASP A 1 190 ? 55.09700 42.51300 61.01200 1.000 16.53088 ?  190 ASP A OD1 1 
ATOM   1521 O  OD2 . ASP A 1 190 ? 57.24400 42.80800 60.74200 1.000 27.84441 -1 190 ASP A OD2 1 
ATOM   1522 N  N   . LEU A 1 191 ? 52.60700 43.96800 62.04500 1.000 15.25827 ?  191 LEU A N   1 
ATOM   1523 C  CA  . LEU A 1 191 ? 51.67700 43.41800 63.01400 1.000 13.29468 ?  191 LEU A CA  1 
ATOM   1524 C  C   . LEU A 1 191 ? 52.17700 42.12600 63.66000 1.000 14.03839 ?  191 LEU A C   1 
ATOM   1525 O  O   . LEU A 1 191 ? 51.47500 41.58900 64.52800 1.000 16.79843 ?  191 LEU A O   1 
ATOM   1526 C  CB  . LEU A 1 191 ? 50.31400 43.21300 62.34100 1.000 13.94226 ?  191 LEU A CB  1 
ATOM   1527 C  CG  . LEU A 1 191 ? 49.75300 44.50800 61.75900 1.000 14.63535 ?  191 LEU A CG  1 
ATOM   1528 C  CD1 . LEU A 1 191 ? 48.40000 44.27600 61.07600 1.000 14.59662 ?  191 LEU A CD1 1 
ATOM   1529 C  CD2 . LEU A 1 191 ? 49.62400 45.57900 62.85100 1.000 16.52518 ?  191 LEU A CD2 1 
ATOM   1530 N  N   . ASP A 1 192 ? 53.34500 41.60700 63.22400 1.000 13.87493 ?  192 ASP A N   1 
ATOM   1531 C  CA  . ASP A 1 192 ? 54.08900 40.58100 63.96600 1.000 16.49558 ?  192 ASP A CA  1 
ATOM   1532 C  C   . ASP A 1 192 ? 53.40600 39.21700 63.88300 1.000 17.90753 ?  192 ASP A C   1 
ATOM   1533 O  O   . ASP A 1 192 ? 53.41700 38.43600 64.84200 1.000 17.58178 ?  192 ASP A O   1 
ATOM   1534 C  CB  . ASP A 1 192 ? 54.28800 41.01200 65.42200 1.000 19.92934 ?  192 ASP A CB  1 
ATOM   1535 C  CG  . ASP A 1 192 ? 55.58300 40.52800 66.01700 1.000 31.64480 ?  192 ASP A CG  1 
ATOM   1536 O  OD1 . ASP A 1 192 ? 56.36600 39.84900 65.32000 1.000 32.29313 ?  192 ASP A OD1 1 
ATOM   1537 O  OD2 . ASP A 1 192 ? 55.80600 40.84900 67.20800 1.000 34.90809 -1 192 ASP A OD2 1 
ATOM   1538 N  N   . VAL A 1 193 ? 52.80000 38.93600 62.73300 1.000 13.12626 ?  193 VAL A N   1 
ATOM   1539 C  CA  . VAL A 1 193 ? 52.13500 37.67200 62.45600 1.000 14.12766 ?  193 VAL A CA  1 
ATOM   1540 C  C   . VAL A 1 193 ? 52.88800 36.85600 61.40400 1.000 13.85792 ?  193 VAL A C   1 
ATOM   1541 O  O   . VAL A 1 193 ? 52.31400 35.94700 60.79400 1.000 14.24975 ?  193 VAL A O   1 
ATOM   1542 C  CB  . VAL A 1 193 ? 50.65800 37.88400 62.08200 1.000 11.57687 ?  193 VAL A CB  1 
ATOM   1543 C  CG1 . VAL A 1 193 ? 49.87400 38.44800 63.25100 1.000 14.77961 ?  193 VAL A CG1 1 
ATOM   1544 C  CG2 . VAL A 1 193 ? 50.55000 38.83100 60.86900 1.000 13.41530 ?  193 VAL A CG2 1 
ATOM   1545 N  N   . THR A 1 194 ? 54.18000 37.14000 61.21800 1.000 14.17545 ?  194 THR A N   1 
ATOM   1546 C  CA  . THR A 1 194 ? 54.94800 36.57400 60.11700 1.000 14.55754 ?  194 THR A CA  1 
ATOM   1547 C  C   . THR A 1 194 ? 55.00700 35.06000 60.20100 1.000 15.58778 ?  194 THR A C   1 
ATOM   1548 O  O   . THR A 1 194 ? 55.33500 34.49700 61.24800 1.000 15.21268 ?  194 THR A O   1 
ATOM   1549 C  CB  . THR A 1 194 ? 56.35600 37.16700 60.18000 1.000 14.69715 ?  194 THR A CB  1 
ATOM   1550 O  OG1 . THR A 1 194 ? 56.22300 38.59400 60.04100 1.000 18.76996 ?  194 THR A OG1 1 
ATOM   1551 C  CG2 . THR A 1 194 ? 57.24100 36.64200 59.07100 1.000 16.88120 ?  194 THR A CG2 1 
ATOM   1552 N  N   . ALA A 1 195 ? 54.71200 34.39900 59.08000 1.000 13.14856 ?  195 ALA A N   1 
ATOM   1553 C  CA  . ALA A 1 195 ? 54.58700 32.95200 59.04200 1.000 14.19796 ?  195 ALA A CA  1 
ATOM   1554 C  C   . ALA A 1 195 ? 55.48900 32.39300 57.95000 1.000 14.76833 ?  195 ALA A C   1 
ATOM   1555 O  O   . ALA A 1 195 ? 55.43900 32.83900 56.78900 1.000 14.52179 ?  195 ALA A O   1 
ATOM   1556 C  CB  . ALA A 1 195 ? 53.14900 32.53900 58.76500 1.000 16.64289 ?  195 ALA A CB  1 
ATOM   1557 N  N   . THR A 1 196 ? 56.28300 31.38700 58.31100 1.000 15.42765 ?  196 THR A N   1 
ATOM   1558 C  CA  . THR A 1 196 ? 57.14400 30.70000 57.35900 1.000 16.44167 ?  196 THR A CA  1 
ATOM   1559 C  C   . THR A 1 196 ? 56.77100 29.23900 57.15600 1.000 15.08531 ?  196 THR A C   1 
ATOM   1560 O  O   . THR A 1 196 ? 57.41600 28.55600 56.34700 1.000 21.00870 ?  196 THR A O   1 
ATOM   1561 C  CB  . THR A 1 196 ? 58.61400 30.76900 57.79900 1.000 20.89232 ?  196 THR A CB  1 
ATOM   1562 O  OG1 . THR A 1 196 ? 58.72900 30.17300 59.09900 1.000 20.86440 ?  196 THR A OG1 1 
ATOM   1563 C  CG2 . THR A 1 196 ? 59.10400 32.20500 57.87000 1.000 24.21181 ?  196 THR A CG2 1 
ATOM   1564 N  N   . ASN A 1 197 ? 55.77400 28.73000 57.86400 1.000 14.22984 ?  197 ASN A N   1 
ATOM   1565 C  CA  . ASN A 1 197 ? 55.33100 27.34800 57.75400 1.000 13.96034 ?  197 ASN A CA  1 
ATOM   1566 C  C   . ASN A 1 197 ? 53.99800 27.23800 58.48800 1.000 14.39214 ?  197 ASN A C   1 
ATOM   1567 O  O   . ASN A 1 197 ? 53.49600 28.22500 59.04000 1.000 13.92678 ?  197 ASN A O   1 
ATOM   1568 C  CB  . ASN A 1 197 ? 56.38600 26.36300 58.30500 1.000 15.56661 ?  197 ASN A CB  1 
ATOM   1569 C  CG  . ASN A 1 197 ? 56.81600 26.70800 59.70900 1.000 16.28433 ?  197 ASN A CG  1 
ATOM   1570 O  OD1 . ASN A 1 197 ? 56.01300 27.14400 60.52100 1.000 16.93713 ?  197 ASN A OD1 1 
ATOM   1571 N  ND2 . ASN A 1 197 ? 58.10300 26.52100 60.00600 1.000 21.20946 ?  197 ASN A ND2 1 
ATOM   1572 N  N   . ARG A 1 198 ? 53.45200 26.05400 58.52500 1.000 16.00424 ?  198 ARG A N   1 
ATOM   1573 C  CA  . ARG A 1 198 ? 52.15200 25.88300 59.12900 1.000 17.19422 ?  198 ARG A CA  1 
ATOM   1574 C  C   . ARG A 1 198 ? 52.12900 26.12800 60.62400 1.000 14.99954 ?  198 ARG A C   1 
ATOM   1575 O  O   . ARG A 1 198 ? 51.13500 26.55200 61.16800 1.000 16.94973 ?  198 ARG A O   1 
ATOM   1576 C  CB  . ARG A 1 198 ? 51.65900 24.48700 58.78100 1.000 22.53777 ?  198 ARG A CB  1 
ATOM   1577 C  CG  . ARG A 1 198 ? 51.78800 24.27700 57.27800 1.000 28.26111 ?  198 ARG A CG  1 
ATOM   1578 C  CD  . ARG A 1 198 ? 51.23400 22.95700 56.79100 1.000 38.92953 ?  198 ARG A CD  1 
ATOM   1579 N  NE  . ARG A 1 198 ? 51.91800 21.79600 57.34100 1.000 51.81166 ?  198 ARG A NE  1 
ATOM   1580 C  CZ  . ARG A 1 198 ? 53.01600 21.25300 56.82900 1.000 48.54820 ?  198 ARG A CZ  1 
ATOM   1581 N  NH1 . ARG A 1 198 ? 53.58800 21.78300 55.76100 1.000 47.65888 ?  198 ARG A NH1 1 
ATOM   1582 N  NH2 . ARG A 1 198 ? 53.55000 20.18100 57.39500 1.000 48.87356 ?  198 ARG A NH2 1 
ATOM   1583 N  N   . GLU A 1 199 ? 53.25100 25.87500 61.26000 1.000 15.25698 ?  199 GLU A N   1 
ATOM   1584 C  CA  . GLU A 1 199 ? 53.29700 26.01500 62.70800 1.000 14.12250 ?  199 GLU A CA  1 
ATOM   1585 C  C   . GLU A 1 199 ? 53.41700 27.47300 63.11000 1.000 12.63929 ?  199 GLU A C   1 
ATOM   1586 O  O   . GLU A 1 199 ? 52.64600 27.95600 63.94700 1.000 13.40561 ?  199 GLU A O   1 
ATOM   1587 C  CB  . GLU A 1 199 ? 54.44500 25.18300 63.29100 1.000 18.20933 ?  199 GLU A CB  1 
ATOM   1588 C  CG  . GLU A 1 199 ? 54.28500 23.68800 63.01600 1.000 20.67370 ?  199 GLU A CG  1 
ATOM   1589 C  CD  . GLU A 1 199 ? 54.64900 23.29400 61.58100 1.000 22.66678 ?  199 GLU A CD  1 
ATOM   1590 O  OE1 . GLU A 1 199 ? 55.51500 23.96100 60.97100 1.000 23.71888 ?  199 GLU A OE1 1 
ATOM   1591 O  OE2 . GLU A 1 199 ? 54.06500 22.31500 61.06700 1.000 35.66758 -1 199 GLU A OE2 1 
ATOM   1592 N  N   . THR A 1 200 ? 54.35500 28.19900 62.49700 1.000 12.46621 ?  200 THR A N   1 
ATOM   1593 C  CA  . THR A 1 200 ? 54.48400 29.61600 62.80600 1.000 13.50865 ?  200 THR A CA  1 
ATOM   1594 C  C   . THR A 1 200 ? 53.23200 30.38600 62.41100 1.000 13.43585 ?  200 THR A C   1 
ATOM   1595 O  O   . THR A 1 200 ? 52.92000 31.39700 63.03800 1.000 12.96737 ?  200 THR A O   1 
ATOM   1596 C  CB  . THR A 1 200 ? 55.72100 30.22900 62.15000 1.000 14.28814 ?  200 THR A CB  1 
ATOM   1597 O  OG1 . THR A 1 200 ? 55.69500 29.99300 60.74300 1.000 13.55367 ?  200 THR A OG1 1 
ATOM   1598 C  CG2 . THR A 1 200 ? 56.99900 29.58000 62.72600 1.000 16.47608 ?  200 THR A CG2 1 
ATOM   1599 N  N   . LEU A 1 201 ? 52.50800 29.93600 61.37200 1.000 12.43450 ?  201 LEU A N   1 
ATOM   1600 C  CA  . LEU A 1 201 ? 51.23500 30.58000 61.05100 1.000 12.57553 ?  201 LEU A CA  1 
ATOM   1601 C  C   . LEU A 1 201 ? 50.33200 30.62700 62.28100 1.000 13.26820 ?  201 LEU A C   1 
ATOM   1602 O  O   . LEU A 1 201 ? 49.77800 31.67700 62.63000 1.000 13.00837 ?  201 LEU A O   1 
ATOM   1603 C  CB  . LEU A 1 201 ? 50.54900 29.83000 59.90500 1.000 12.94374 ?  201 LEU A CB  1 
ATOM   1604 C  CG  . LEU A 1 201 ? 49.19900 30.42100 59.45600 1.000 14.49586 ?  201 LEU A CG  1 
ATOM   1605 C  CD1 . LEU A 1 201 ? 49.39100 31.71300 58.68000 1.000 13.82287 ?  201 LEU A CD1 1 
ATOM   1606 C  CD2 . LEU A 1 201 ? 48.48200 29.37500 58.61200 1.000 16.20955 ?  201 LEU A CD2 1 
ATOM   1607 N  N   . GLU A 1 202 ? 50.19000 29.48200 62.96800 1.000 12.61447 ?  202 GLU A N   1 
ATOM   1608 C  CA  . GLU A 1 202 ? 49.31100 29.43300 64.13100 1.000 13.00058 ?  202 GLU A CA  1 
ATOM   1609 C  C   . GLU A 1 202 ? 49.92000 30.18900 65.30500 1.000 11.40347 ?  202 GLU A C   1 
ATOM   1610 O  O   . GLU A 1 202 ? 49.22800 30.94000 66.00100 1.000 12.99090 ?  202 GLU A O   1 
ATOM   1611 C  CB  . GLU A 1 202 ? 49.09000 27.97600 64.56800 1.000 14.72417 ?  202 GLU A CB  1 
ATOM   1612 C  CG  . GLU A 1 202 ? 48.51400 27.03200 63.50000 1.000 12.88461 ?  202 GLU A CG  1 
ATOM   1613 C  CD  . GLU A 1 202 ? 47.16700 27.50700 62.99200 1.000 16.39654 ?  202 GLU A CD  1 
ATOM   1614 O  OE1 . GLU A 1 202 ? 46.33600 27.94900 63.81400 1.000 16.42838 ?  202 GLU A OE1 1 
ATOM   1615 O  OE2 . GLU A 1 202 ? 46.95800 27.45200 61.75000 1.000 19.65789 -1 202 GLU A OE2 1 
ATOM   1616 N  N   . GLN A 1 203 ? 51.22000 29.98700 65.54500 1.000 11.30730 ?  203 GLN A N   1 
ATOM   1617 C  CA  . GLN A 1 203 ? 51.85400 30.60600 66.70700 1.000 13.34385 ?  203 GLN A CA  1 
ATOM   1618 C  C   . GLN A 1 203 ? 51.82400 32.12700 66.60900 1.000 13.35190 ?  203 GLN A C   1 
ATOM   1619 O  O   . GLN A 1 203 ? 51.51500 32.83400 67.57800 1.000 13.14544 ?  203 GLN A O   1 
ATOM   1620 C  CB  . GLN A 1 203 ? 53.29800 30.11800 66.80300 1.000 17.31259 ?  203 GLN A CB  1 
ATOM   1621 C  CG  . GLN A 1 203 ? 54.03300 30.64000 68.05100 1.000 19.26591 ?  203 GLN A CG  1 
ATOM   1622 C  CD  . GLN A 1 203 ? 54.22300 29.59500 69.11800 1.000 33.55547 ?  203 GLN A CD  1 
ATOM   1623 O  OE1 . GLN A 1 203 ? 55.16600 28.80000 69.05500 1.000 38.93046 ?  203 GLN A OE1 1 
ATOM   1624 N  NE2 . GLN A 1 203 ? 53.34000 29.59500 70.12100 1.000 27.59696 ?  203 GLN A NE2 1 
ATOM   1625 N  N   . ARG A 1 204 ? 52.15900 32.65400 65.43900 1.000 12.87186 ?  204 ARG A N   1 
ATOM   1626 C  CA  . ARG A 1 204 ? 52.29200 34.09600 65.31900 1.000 12.59416 ?  204 ARG A CA  1 
ATOM   1627 C  C   . ARG A 1 204 ? 50.94800 34.78800 65.13400 1.000 13.38714 ?  204 ARG A C   1 
ATOM   1628 O  O   . ARG A 1 204 ? 50.82200 35.96800 65.47900 1.000 14.64501 ?  204 ARG A O   1 
ATOM   1629 C  CB  . ARG A 1 204 ? 53.27400 34.44200 64.19700 1.000 13.10491 ?  204 ARG A CB  1 
ATOM   1630 C  CG  . ARG A 1 204 ? 54.71400 34.00900 64.47900 1.000 16.41793 ?  204 ARG A CG  1 
ATOM   1631 C  CD  . ARG A 1 204 ? 55.36900 34.92600 65.51700 1.000 22.00752 ?  204 ARG A CD  1 
ATOM   1632 N  NE  . ARG A 1 204 ? 55.56300 36.26300 64.95900 1.000 28.18894 ?  204 ARG A NE  1 
ATOM   1633 C  CZ  . ARG A 1 204 ? 56.56800 36.62100 64.16200 1.000 34.34296 ?  204 ARG A CZ  1 
ATOM   1634 N  NH1 . ARG A 1 204 ? 57.56300 35.78600 63.87600 1.000 29.22977 ?  204 ARG A NH1 1 
ATOM   1635 N  NH2 . ARG A 1 204 ? 56.57300 37.84700 63.62800 1.000 26.87959 ?  204 ARG A NH2 1 
ATOM   1636 N  N   . TYR A 1 205 ? 49.94500 34.09300 64.58300 1.000 12.23398 ?  205 TYR A N   1 
ATOM   1637 C  CA  . TYR A 1 205 ? 48.57700 34.60100 64.63800 1.000 10.97023 ?  205 TYR A CA  1 
ATOM   1638 C  C   . TYR A 1 205 ? 48.16400 34.85900 66.08000 1.000 14.22422 ?  205 TYR A C   1 
ATOM   1639 O  O   . TYR A 1 205 ? 47.70700 35.95300 66.42000 1.000 14.32255 ?  205 TYR A O   1 
ATOM   1640 C  CB  . TYR A 1 205 ? 47.62900 33.61200 63.94300 1.000 12.17277 ?  205 TYR A CB  1 
ATOM   1641 C  CG  . TYR A 1 205 ? 46.15700 33.90100 64.14200 1.000 13.31373 ?  205 TYR A CG  1 
ATOM   1642 C  CD1 . TYR A 1 205 ? 45.53100 34.96000 63.48700 1.000 13.57784 ?  205 TYR A CD1 1 
ATOM   1643 C  CD2 . TYR A 1 205 ? 45.39300 33.09000 64.95900 1.000 14.75241 ?  205 TYR A CD2 1 
ATOM   1644 C  CE1 . TYR A 1 205 ? 44.17900 35.22500 63.67500 1.000 15.14713 ?  205 TYR A CE1 1 
ATOM   1645 C  CE2 . TYR A 1 205 ? 44.03700 33.33700 65.15500 1.000 17.70200 ?  205 TYR A CE2 1 
ATOM   1646 C  CZ  . TYR A 1 205 ? 43.44000 34.40300 64.50800 1.000 18.53498 ?  205 TYR A CZ  1 
ATOM   1647 O  OH  . TYR A 1 205 ? 42.11700 34.66300 64.72200 1.000 19.43176 ?  205 TYR A OH  1 
ATOM   1648 N  N   . ARG A 1 206 ? 48.34600 33.86600 66.95200 1.000 14.07232 ?  206 ARG A N   1 
ATOM   1649 C  CA  . ARG A 1 206 ? 48.01100 34.06500 68.36200 1.000 15.23865 ?  206 ARG A CA  1 
ATOM   1650 C  C   . ARG A 1 206 ? 48.87400 35.15500 68.98900 1.000 17.47434 ?  206 ARG A C   1 
ATOM   1651 O  O   . ARG A 1 206 ? 48.38100 35.95200 69.80100 1.000 18.44657 ?  206 ARG A O   1 
ATOM   1652 C  CB  . ARG A 1 206 ? 48.16800 32.74400 69.11800 1.000 15.64257 ?  206 ARG A CB  1 
ATOM   1653 C  CG  . ARG A 1 206 ? 47.10300 31.73800 68.73800 1.000 15.50417 ?  206 ARG A CG  1 
ATOM   1654 C  CD  . ARG A 1 206 ? 47.42400 30.34000 69.20400 1.000 18.13442 ?  206 ARG A CD  1 
ATOM   1655 N  NE  . ARG A 1 206 ? 46.48700 29.39000 68.61900 1.000 16.31853 ?  206 ARG A NE  1 
ATOM   1656 C  CZ  . ARG A 1 206 ? 45.46500 28.81900 69.24300 1.000 21.44855 ?  206 ARG A CZ  1 
ATOM   1657 N  NH1 . ARG A 1 206 ? 45.19800 29.06500 70.51900 1.000 21.71590 ?  206 ARG A NH1 1 
ATOM   1658 N  NH2 . ARG A 1 206 ? 44.70600 27.95100 68.57400 1.000 19.79511 ?  206 ARG A NH2 1 
ATOM   1659 N  N   . HIS A 1 207 ? 50.15700 35.21700 68.60900 1.000 16.44490 ?  207 HIS A N   1 
ATOM   1660 C  CA  . HIS A 1 207 ? 51.04000 36.27000 69.11200 1.000 16.33547 ?  207 HIS A CA  1 
ATOM   1661 C  C   . HIS A 1 207 ? 50.52100 37.65600 68.74000 1.000 19.51043 ?  207 HIS A C   1 
ATOM   1662 O  O   . HIS A 1 207 ? 50.49400 38.57100 69.57500 1.000 19.22912 ?  207 HIS A O   1 
ATOM   1663 C  CB  . HIS A 1 207 ? 52.43000 36.08600 68.52100 1.000 18.10396 ?  207 HIS A CB  1 
ATOM   1664 C  CG  . HIS A 1 207 ? 53.38900 37.18100 68.86600 1.000 20.53231 ?  207 HIS A CG  1 
ATOM   1665 N  ND1 . HIS A 1 207 ? 53.89800 37.35500 70.13800 1.000 26.31457 ?  207 HIS A ND1 1 
ATOM   1666 C  CD2 . HIS A 1 207 ? 53.94000 38.15500 68.10200 1.000 23.41302 ?  207 HIS A CD2 1 
ATOM   1667 C  CE1 . HIS A 1 207 ? 54.71900 38.39100 70.14100 1.000 25.73674 ?  207 HIS A CE1 1 
ATOM   1668 N  NE2 . HIS A 1 207 ? 54.76600 38.89300 68.91900 1.000 27.26507 ?  207 HIS A NE2 1 
ATOM   1669 N  N   . GLY A 1 208 ? 50.14400 37.84500 67.47600 1.000 18.40355 ?  208 GLY A N   1 
ATOM   1670 C  CA  . GLY A 1 208 ? 49.67200 39.15400 67.04800 1.000 18.08818 ?  208 GLY A CA  1 
ATOM   1671 C  C   . GLY A 1 208 ? 48.41600 39.57800 67.77600 1.000 19.42178 ?  208 GLY A C   1 
ATOM   1672 O  O   . GLY A 1 208 ? 48.27000 40.74300 68.16400 1.000 21.07995 ?  208 GLY A O   1 
ATOM   1673 N  N   . ILE A 1 209 ? 47.48300 38.64200 67.95600 1.000 18.09864 ?  209 ILE A N   1 
ATOM   1674 C  CA  A ILE A 1 209 ? 46.26500 38.90300 68.72200 0.376 20.66486 ?  209 ILE A CA  1 
ATOM   1675 C  CA  B ILE A 1 209 ? 46.27200 38.93100 68.71600 0.624 20.67331 ?  209 ILE A CA  1 
ATOM   1676 C  C   . ILE A 1 209 ? 46.61400 39.25200 70.16300 1.000 23.89104 ?  209 ILE A C   1 
ATOM   1677 O  O   . ILE A 1 209 ? 46.07600 40.20500 70.74500 1.000 26.15184 ?  209 ILE A O   1 
ATOM   1678 C  CB  A ILE A 1 209 ? 45.32700 37.68200 68.66000 0.376 20.27664 ?  209 ILE A CB  1 
ATOM   1679 C  CB  B ILE A 1 209 ? 45.28400 37.75800 68.60600 0.624 20.30994 ?  209 ILE A CB  1 
ATOM   1680 C  CG1 A ILE A 1 209 ? 44.96700 37.33500 67.21000 0.376 18.62256 ?  209 ILE A CG1 1 
ATOM   1681 C  CG1 B ILE A 1 209 ? 44.79900 37.61500 67.16100 0.624 18.68158 ?  209 ILE A CG1 1 
ATOM   1682 C  CG2 A ILE A 1 209 ? 44.06400 37.92800 69.48000 0.376 20.90012 ?  209 ILE A CG2 1 
ATOM   1683 C  CG2 B ILE A 1 209 ? 44.10700 37.94600 69.55600 0.624 20.92234 ?  209 ILE A CG2 1 
ATOM   1684 C  CD1 A ILE A 1 209 ? 44.01900 38.30400 66.58100 0.376 17.78006 ?  209 ILE A CD1 1 
ATOM   1685 C  CD1 B ILE A 1 209 ? 43.87100 36.48200 66.99000 0.624 18.18788 ?  209 ILE A CD1 1 
ATOM   1686 N  N   . SER A 1 210 ? 47.51600 38.46700 70.76400 1.000 19.96713 ?  210 SER A N   1 
ATOM   1687 C  CA  . SER A 1 210 ? 47.93400 38.70700 72.14600 1.000 22.63283 ?  210 SER A CA  1 
ATOM   1688 C  C   . SER A 1 210 ? 48.53700 40.09400 72.30400 1.000 28.62314 ?  210 SER A C   1 
ATOM   1689 O  O   . SER A 1 210 ? 48.24200 40.79700 73.27900 1.000 26.94392 ?  210 SER A O   1 
ATOM   1690 C  CB  . SER A 1 210 ? 48.93500 37.63300 72.56800 1.000 25.42836 ?  210 SER A CB  1 
ATOM   1691 O  OG  . SER A 1 210 ? 49.34000 37.81000 73.91900 1.000 28.97349 ?  210 SER A OG  1 
ATOM   1692 N  N   . ASN A 1 211 ? 49.36700 40.52100 71.34400 1.000 24.12894 ?  211 ASN A N   1 
ATOM   1693 C  CA  . ASN A 1 211 ? 49.94700 41.85900 71.42800 1.000 29.67232 ?  211 ASN A CA  1 
ATOM   1694 C  C   . ASN A 1 211 ? 48.87200 42.93700 71.48300 1.000 37.45192 ?  211 ASN A C   1 
ATOM   1695 O  O   . ASN A 1 211 ? 49.11400 44.02000 72.02600 1.000 34.20557 ?  211 ASN A O   1 
ATOM   1696 C  CB  . ASN A 1 211 ? 50.89300 42.12100 70.26300 1.000 30.33268 ?  211 ASN A CB  1 
ATOM   1697 C  CG  . ASN A 1 211 ? 52.23800 41.46000 70.44700 1.000 35.02873 ?  211 ASN A CG  1 
ATOM   1698 O  OD1 . ASN A 1 211 ? 52.63900 41.12500 71.56900 1.000 39.28763 ?  211 ASN A OD1 1 
ATOM   1699 N  ND2 . ASN A 1 211 ? 52.95600 41.27500 69.34000 1.000 43.79307 ?  211 ASN A ND2 1 
ATOM   1700 N  N   . LEU A 1 212 ? 47.68300 42.66400 70.93800 1.000 28.83488 ?  212 LEU A N   1 
ATOM   1701 C  CA  . LEU A 1 212 ? 46.58100 43.61700 71.03700 1.000 35.88523 ?  212 LEU A CA  1 
ATOM   1702 C  C   . LEU A 1 212 ? 45.87400 43.53500 72.39100 1.000 41.10431 ?  212 LEU A C   1 
ATOM   1703 O  O   . LEU A 1 212 ? 45.50600 44.56900 72.96100 1.000 49.82185 ?  212 LEU A O   1 
ATOM   1704 C  CB  . LEU A 1 212 ? 45.59200 43.42100 69.87800 1.000 27.53383 ?  212 LEU A CB  1 
ATOM   1705 C  CG  . LEU A 1 212 ? 46.18400 43.50500 68.46800 1.000 30.14108 ?  212 LEU A CG  1 
ATOM   1706 C  CD1 . LEU A 1 212 ? 45.11100 43.30000 67.39300 1.000 25.16390 ?  212 LEU A CD1 1 
ATOM   1707 C  CD2 . LEU A 1 212 ? 46.90800 44.82500 68.24300 1.000 37.57603 ?  212 LEU A CD2 1 
ATOM   1708 N  N   . LYS A 1 213 ? 45.66200 42.32400 72.91900 1.000 39.15945 ?  213 LYS A N   1 
ATOM   1709 C  CA  . LYS A 1 213 ? 45.06500 42.19500 74.24800 1.000 40.66794 ?  213 LYS A CA  1 
ATOM   1710 C  C   . LYS A 1 213 ? 45.91300 42.87400 75.31600 1.000 41.25948 ?  213 LYS A C   1 
ATOM   1711 O  O   . LYS A 1 213 ? 45.37800 43.37200 76.31500 1.000 48.86518 ?  213 LYS A O   1 
ATOM   1712 C  CB  . LYS A 1 213 ? 44.86700 40.72100 74.59900 1.000 42.16869 ?  213 LYS A CB  1 
ATOM   1713 C  CG  . LYS A 1 213 ? 43.71900 40.05700 73.86700 1.000 41.91815 ?  213 LYS A CG  1 
ATOM   1714 C  CD  . LYS A 1 213 ? 42.44600 40.04600 74.70200 1.000 45.82357 ?  213 LYS A CD  1 
ATOM   1715 C  CE  . LYS A 1 213 ? 42.59900 39.18900 75.95000 1.000 46.63632 ?  213 LYS A CE  1 
ATOM   1716 N  NZ  . LYS A 1 213 ? 41.29700 39.01900 76.66600 1.000 50.96268 ?  213 LYS A NZ  1 
HETATM 1717 ZN ZN  . ZN  B 2 .   ? 41.10200 50.58000 52.12600 1.000 12.08804 ?  301 ZN  A ZN  1 
HETATM 1718 O  O   . HOH C 3 .   ? 28.59900 38.86300 58.52900 1.000 34.31430 ?  401 HOH A O   1 
HETATM 1719 O  O   . HOH C 3 .   ? 60.65500 41.31500 37.44100 1.000 27.83565 ?  402 HOH A O   1 
HETATM 1720 O  O   . HOH C 3 .   ? 64.04500 52.50700 45.46400 1.000 38.59646 ?  403 HOH A O   1 
HETATM 1721 O  O   . HOH C 3 .   ? 45.94100 29.11100 65.98300 1.000 27.86410 ?  404 HOH A O   1 
HETATM 1722 O  O   . HOH C 3 .   ? 59.53800 43.69700 61.16600 1.000 40.95477 ?  405 HOH A O   1 
HETATM 1723 O  O   . HOH C 3 .   ? 49.01000 20.43100 51.47000 1.000 33.87207 ?  406 HOH A O   1 
HETATM 1724 O  O   . HOH C 3 .   ? 57.42500 41.46500 58.54200 1.000 27.11568 ?  407 HOH A O   1 
HETATM 1725 O  O   . HOH C 3 .   ? 55.96700 26.84000 67.54000 1.000 37.26515 ?  408 HOH A O   1 
HETATM 1726 O  O   . HOH C 3 .   ? 59.13200 25.87000 53.50800 1.000 33.26574 ?  409 HOH A O   1 
HETATM 1727 O  O   . HOH C 3 .   ? 54.20800 37.17200 34.56100 1.000 17.40977 ?  410 HOH A O   1 
HETATM 1728 O  O   . HOH C 3 .   ? 31.60700 33.86900 56.55000 1.000 26.87117 ?  411 HOH A O   1 
HETATM 1729 O  O   . HOH C 3 .   ? 33.26900 32.90400 47.32600 1.000 27.58740 ?  412 HOH A O   1 
HETATM 1730 O  O   . HOH C 3 .   ? 51.30600 54.78900 59.93600 1.000 16.29903 ?  413 HOH A O   1 
HETATM 1731 O  O   . HOH C 3 .   ? 45.56500 23.93000 45.59400 1.000 22.95008 ?  414 HOH A O   1 
HETATM 1732 O  O   . HOH C 3 .   ? 64.04400 48.16800 35.11700 1.000 24.43407 ?  415 HOH A O   1 
HETATM 1733 O  O   . HOH C 3 .   ? 52.64500 55.94400 63.19700 1.000 22.46933 ?  416 HOH A O   1 
HETATM 1734 O  O   . HOH C 3 .   ? 40.82100 52.16600 60.14700 1.000 26.50137 ?  417 HOH A O   1 
HETATM 1735 O  O   . HOH C 3 .   ? 52.85100 21.05100 45.94200 1.000 40.45682 ?  418 HOH A O   1 
HETATM 1736 O  O   . HOH C 3 .   ? 59.87300 58.36400 47.22300 1.000 41.59475 ?  419 HOH A O   1 
HETATM 1737 O  O   . HOH C 3 .   ? 24.86100 45.54800 62.82700 1.000 34.82462 ?  420 HOH A O   1 
HETATM 1738 O  O   . HOH C 3 .   ? 44.01300 56.52500 62.53700 1.000 24.94629 ?  421 HOH A O   1 
HETATM 1739 O  O   . HOH C 3 .   ? 65.72900 51.52200 29.89900 1.000 21.54270 ?  422 HOH A O   1 
HETATM 1740 O  O   . HOH C 3 .   ? 61.00800 41.08100 30.62800 1.000 44.70121 ?  423 HOH A O   1 
HETATM 1741 O  O   . HOH C 3 .   ? 70.106   55.103   33.886   1.000 32.56345 ?  424 HOH A O   1 
HETATM 1742 O  O   . HOH C 3 .   ? 59.35800 30.82300 47.06400 1.000 18.77215 ?  425 HOH A O   1 
HETATM 1743 O  O   . HOH C 3 .   ? 42.63700 48.01600 55.18500 1.000 11.89935 ?  426 HOH A O   1 
HETATM 1744 O  O   . HOH C 3 .   ? 66.06500 49.57900 27.88400 1.000 22.28922 ?  427 HOH A O   1 
HETATM 1745 O  O   . HOH C 3 .   ? 48.765   51.518   43.488   1.000 14.79808 ?  428 HOH A O   1 
HETATM 1746 O  O   . HOH C 3 .   ? 35.94400 34.58600 68.95500 1.000 25.44041 ?  429 HOH A O   1 
HETATM 1747 O  O   . HOH C 3 .   ? 60.71000 35.32500 42.39700 1.000 25.97298 ?  430 HOH A O   1 
HETATM 1748 O  O   . HOH C 3 .   ? 35.556   36.963   43.283   1.000 29.19484 ?  431 HOH A O   1 
HETATM 1749 O  O   . HOH C 3 .   ? 37.98300 56.17300 76.30800 1.000 38.64617 ?  432 HOH A O   1 
HETATM 1750 O  O   . HOH C 3 .   ? 41.77600 30.83400 52.95400 1.000 12.37800 ?  433 HOH A O   1 
HETATM 1751 O  O   . HOH C 3 .   ? 30.92200 54.18900 55.98000 1.000 24.87022 ?  434 HOH A O   1 
HETATM 1752 O  O   . HOH C 3 .   ? 39.82400 34.33500 59.24400 1.000 20.48649 ?  435 HOH A O   1 
HETATM 1753 O  O   . HOH C 3 .   ? 50.39600 42.67100 66.74900 1.000 27.03198 ?  436 HOH A O   1 
HETATM 1754 O  O   . HOH C 3 .   ? 35.20700 42.48800 76.49200 1.000 27.17103 ?  437 HOH A O   1 
HETATM 1755 O  O   . HOH C 3 .   ? 32.648   36.724   69.340   1.000 33.22810 ?  438 HOH A O   1 
HETATM 1756 O  O   . HOH C 3 .   ? 55.89000 59.12000 62.53800 1.000 20.45496 ?  439 HOH A O   1 
HETATM 1757 O  O   . HOH C 3 .   ? 41.14500 31.50700 64.14300 1.000 32.81660 ?  440 HOH A O   1 
HETATM 1758 O  O   . HOH C 3 .   ? 42.07600 56.37600 47.03400 1.000 21.25588 ?  441 HOH A O   1 
HETATM 1759 O  O   . HOH C 3 .   ? 50.96900 66.78500 24.92600 1.000 37.83386 ?  442 HOH A O   1 
HETATM 1760 O  O   . HOH C 3 .   ? 56.87200 59.94200 24.12300 1.000 35.18144 ?  443 HOH A O   1 
HETATM 1761 O  O   . HOH C 3 .   ? 55.03000 47.19200 41.16100 1.000 28.06724 ?  444 HOH A O   1 
HETATM 1762 O  O   . HOH C 3 .   ? 67.19600 49.16800 35.56700 1.000 31.77532 ?  445 HOH A O   1 
HETATM 1763 O  O   . HOH C 3 .   ? 38.54500 39.36300 75.49100 1.000 36.60669 ?  446 HOH A O   1 
HETATM 1764 O  O   . HOH C 3 .   ? 44.58600 55.42500 54.92900 1.000 16.91405 ?  447 HOH A O   1 
HETATM 1765 O  O   . HOH C 3 .   ? 37.85400 55.39600 59.18700 1.000 30.86572 ?  448 HOH A O   1 
HETATM 1766 O  O   . HOH C 3 .   ? 45.15100 56.99800 58.16200 1.000 16.06165 ?  449 HOH A O   1 
HETATM 1767 O  O   . HOH C 3 .   ? 58.97300 28.88800 54.15500 1.000 24.77604 ?  450 HOH A O   1 
HETATM 1768 O  O   . HOH C 3 .   ? 56.56800 45.20800 39.62000 1.000 23.89240 ?  451 HOH A O   1 
HETATM 1769 O  O   . HOH C 3 .   ? 68.01000 44.36300 30.12700 1.000 37.00579 ?  452 HOH A O   1 
HETATM 1770 O  O   . HOH C 3 .   ? 42.52000 24.98600 58.53400 1.000 31.03280 ?  453 HOH A O   1 
HETATM 1771 O  O   . HOH C 3 .   ? 49.78800 50.54300 49.32300 1.000 23.67746 ?  454 HOH A O   1 
HETATM 1772 O  O   . HOH C 3 .   ? 54.64000 32.84700 33.32500 1.000 23.84752 ?  455 HOH A O   1 
HETATM 1773 O  O   . HOH C 3 .   ? 52.86400 45.62300 66.00100 1.000 33.60480 ?  456 HOH A O   1 
HETATM 1774 O  O   . HOH C 3 .   ? 25.77700 53.11500 46.64200 1.000 24.22988 ?  457 HOH A O   1 
HETATM 1775 O  O   . HOH C 3 .   ? 50.77600 53.95500 62.66800 1.000 33.28062 ?  458 HOH A O   1 
HETATM 1776 O  O   . HOH C 3 .   ? 71.13300 59.79200 29.27200 1.000 21.80200 ?  459 HOH A O   1 
HETATM 1777 O  O   . HOH C 3 .   ? 25.90700 38.03400 50.61500 1.000 12.22613 ?  460 HOH A O   1 
HETATM 1778 O  O   . HOH C 3 .   ? 59.87800 52.97900 44.25900 1.000 33.25726 ?  461 HOH A O   1 
HETATM 1779 O  O   . HOH C 3 .   ? 51.30600 25.51300 46.06200 1.000 20.49547 ?  462 HOH A O   1 
HETATM 1780 O  O   . HOH C 3 .   ? 40.50100 53.83100 65.84600 1.000 20.76124 ?  463 HOH A O   1 
HETATM 1781 O  O   . HOH C 3 .   ? 46.31400 48.66400 51.72500 1.000 23.94785 ?  464 HOH A O   1 
HETATM 1782 O  O   . HOH C 3 .   ? 41.64700 43.73700 74.45700 1.000 36.79410 ?  465 HOH A O   1 
HETATM 1783 O  O   . HOH C 3 .   ? 61.50200 34.60500 56.44300 1.000 27.42378 ?  466 HOH A O   1 
HETATM 1784 O  O   . HOH C 3 .   ? 59.18900 57.91200 24.41300 1.000 23.52083 ?  467 HOH A O   1 
HETATM 1785 O  O   . HOH C 3 .   ? 37.12600 53.47100 67.00000 1.000 22.85633 ?  468 HOH A O   1 
HETATM 1786 O  O   . HOH C 3 .   ? 27.22300 47.80700 62.16500 1.000 21.38574 ?  469 HOH A O   1 
HETATM 1787 O  O   . HOH C 3 .   ? 53.88000 40.23600 60.02500 1.000 13.86311 ?  470 HOH A O   1 
HETATM 1788 O  O   . HOH C 3 .   ? 39.69300 55.91000 48.44100 1.000 24.54240 ?  471 HOH A O   1 
HETATM 1789 O  O   . HOH C 3 .   ? 63.75300 51.08800 37.27300 1.000 27.47034 ?  472 HOH A O   1 
HETATM 1790 O  O   . HOH C 3 .   ? 50.15300 19.41500 48.04600 1.000 40.95713 ?  473 HOH A O   1 
HETATM 1791 O  O   . HOH C 3 .   ? 51.17500 58.83300 26.20200 1.000 21.47910 ?  474 HOH A O   1 
HETATM 1792 O  O   . HOH C 3 .   ? 32.46500 35.43900 63.06800 1.000 17.82487 ?  475 HOH A O   1 
HETATM 1793 O  O   . HOH C 3 .   ? 51.01700 50.33400 44.65800 1.000 16.94150 ?  476 HOH A O   1 
HETATM 1794 O  O   . HOH C 3 .   ? 30.18400 42.20300 46.97100 1.000 11.81457 ?  477 HOH A O   1 
HETATM 1795 O  O   . HOH C 3 .   ? 49.01900 54.09800 63.90000 1.000 30.20212 ?  478 HOH A O   1 
HETATM 1796 O  O   . HOH C 3 .   ? 44.18000 24.93400 55.96600 1.000 26.97768 ?  479 HOH A O   1 
HETATM 1797 O  O   . HOH C 3 .   ? 57.80800 33.38400 61.84900 1.000 28.38279 ?  480 HOH A O   1 
HETATM 1798 O  O   . HOH C 3 .   ? 35.60900 36.59500 57.59700 1.000 28.21241 ?  481 HOH A O   1 
HETATM 1799 O  O   . HOH C 3 .   ? 59.335   63.242   20.715   1.000 26.03924 ?  482 HOH A O   1 
HETATM 1800 O  O   . HOH C 3 .   ? 48.57900 26.06700 59.95300 1.000 24.02810 ?  483 HOH A O   1 
HETATM 1801 O  O   . HOH C 3 .   ? 60.78900 33.33100 52.37400 1.000 22.34759 ?  484 HOH A O   1 
HETATM 1802 O  O   . HOH C 3 .   ? 60.19300 55.47400 48.56900 1.000 29.54016 ?  485 HOH A O   1 
HETATM 1803 O  O   . HOH C 3 .   ? 53.43800 53.43800 42.53800 0.50  19.32363 ?  486 HOH A O   1 
HETATM 1804 O  O   . HOH C 3 .   ? 45.44700 48.80400 67.98000 1.000 30.69695 ?  487 HOH A O   1 
HETATM 1805 O  O   . HOH C 3 .   ? 33.40000 54.11600 54.44800 1.000 20.93720 ?  488 HOH A O   1 
HETATM 1806 O  O   . HOH C 3 .   ? 25.63000 44.48700 55.65300 1.000 23.17584 ?  489 HOH A O   1 
HETATM 1807 O  O   . HOH C 3 .   ? 35.89800 53.59500 75.68500 1.000 25.04634 ?  490 HOH A O   1 
HETATM 1808 O  O   . HOH C 3 .   ? 39.91700 37.79900 48.36500 1.000 11.74818 ?  491 HOH A O   1 
HETATM 1809 O  O   . HOH C 3 .   ? 39.56700 37.28300 69.89600 1.000 17.92085 ?  492 HOH A O   1 
HETATM 1810 O  O   . HOH C 3 .   ? 27.55900 36.27300 59.29000 1.000 33.25715 ?  493 HOH A O   1 
HETATM 1811 O  O   . HOH C 3 .   ? 28.39300 49.10400 53.96100 1.000 22.78085 ?  494 HOH A O   1 
HETATM 1812 O  O   . HOH C 3 .   ? 65.57900 62.81400 27.93800 1.000 31.99695 ?  495 HOH A O   1 
HETATM 1813 O  O   . HOH C 3 .   ? 28.21200 44.35100 54.94100 1.000 15.14764 ?  496 HOH A O   1 
HETATM 1814 O  O   . HOH C 3 .   ? 55.46600 63.93400 32.99100 1.000 23.60144 ?  497 HOH A O   1 
HETATM 1815 O  O   . HOH C 3 .   ? 50.01200 34.34100 61.12500 1.000 14.88436 ?  498 HOH A O   1 
HETATM 1816 O  O   . HOH C 3 .   ? 51.41800 21.37800 61.40300 1.000 31.93465 ?  499 HOH A O   1 
HETATM 1817 O  O   . HOH C 3 .   ? 63.19200 42.78300 36.95100 1.000 43.14309 ?  500 HOH A O   1 
HETATM 1818 O  O   . HOH C 3 .   ? 62.46200 32.10400 44.26100 1.000 35.95347 ?  501 HOH A O   1 
HETATM 1819 O  O   . HOH C 3 .   ? 55.00300 23.59200 57.42800 1.000 27.45683 ?  502 HOH A O   1 
HETATM 1820 O  O   . HOH C 3 .   ? 56.99900 26.05100 42.21600 1.000 34.14319 ?  503 HOH A O   1 
HETATM 1821 O  O   . HOH C 3 .   ? 43.51000 54.47200 66.70500 1.000 32.93292 ?  504 HOH A O   1 
HETATM 1822 O  O   . HOH C 3 .   ? 37.61100 31.90600 62.35100 1.000 23.85323 ?  505 HOH A O   1 
HETATM 1823 O  O   . HOH C 3 .   ? 47.11600 21.83800 50.25800 1.000 27.70455 ?  506 HOH A O   1 
HETATM 1824 O  O   . HOH C 3 .   ? 23.26900 48.20300 55.43400 1.000 34.50731 ?  507 HOH A O   1 
HETATM 1825 O  O   . HOH C 3 .   ? 46.74900 47.96400 69.97400 1.000 38.68971 ?  508 HOH A O   1 
HETATM 1826 O  O   . HOH C 3 .   ? 54.15700 50.30100 66.29100 1.000 43.86717 ?  509 HOH A O   1 
HETATM 1827 O  O   . HOH C 3 .   ? 33.88700 35.18700 56.30900 1.000 27.31274 ?  510 HOH A O   1 
HETATM 1828 O  O   . HOH C 3 .   ? 40.72800 55.31900 53.19800 1.000 20.76438 ?  511 HOH A O   1 
HETATM 1829 O  O   . HOH C 3 .   ? 63.79800 52.93700 39.06500 1.000 39.74511 ?  512 HOH A O   1 
HETATM 1830 O  O   . HOH C 3 .   ? 61.77600 41.67900 43.92300 1.000 30.74002 ?  513 HOH A O   1 
HETATM 1831 O  O   . HOH C 3 .   ? 46.20600 51.21700 50.62600 1.000 16.49000 ?  514 HOH A O   1 
HETATM 1832 O  O   . HOH C 3 .   ? 34.67500 37.75200 71.10200 1.000 19.23414 ?  515 HOH A O   1 
HETATM 1833 O  O   . HOH C 3 .   ? 46.50900 53.66300 64.48700 1.000 25.53820 ?  516 HOH A O   1 
HETATM 1834 O  O   . HOH C 3 .   ? 45.72600 57.62600 60.70600 1.000 22.33916 ?  517 HOH A O   1 
HETATM 1835 O  O   . HOH C 3 .   ? 38.49800 52.68300 58.78900 1.000 19.81813 ?  518 HOH A O   1 
HETATM 1836 O  O   . HOH C 3 .   ? 35.61200 33.45200 43.33000 1.000 16.17493 ?  519 HOH A O   1 
HETATM 1837 O  O   . HOH C 3 .   ? 34.17300 47.83000 67.73300 1.000 19.62204 ?  520 HOH A O   1 
HETATM 1838 O  O   . HOH C 3 .   ? 42.434   26.634   61.933   1.000 29.77952 ?  521 HOH A O   1 
HETATM 1839 O  O   . HOH C 3 .   ? 52.92900 19.84700 48.38500 1.000 30.32681 ?  522 HOH A O   1 
HETATM 1840 O  O   . HOH C 3 .   ? 63.60300 48.49300 37.85900 1.000 27.75361 ?  523 HOH A O   1 
HETATM 1841 O  O   . HOH C 3 .   ? 23.35800 47.67900 50.35300 1.000 22.47426 ?  524 HOH A O   1 
HETATM 1842 O  O   . HOH C 3 .   ? 52.12200 38.57000 73.53000 1.000 37.08110 ?  525 HOH A O   1 
HETATM 1843 O  O   . HOH C 3 .   ? 57.44100 40.24000 62.20200 1.000 32.89612 ?  526 HOH A O   1 
HETATM 1844 O  O   . HOH C 3 .   ? 22.58100 53.83300 54.31900 1.000 31.65392 ?  527 HOH A O   1 
HETATM 1845 O  O   . HOH C 3 .   ? 28.60500 46.98600 55.48200 1.000 19.33916 ?  528 HOH A O   1 
HETATM 1846 O  O   . HOH C 3 .   ? 62.19500 27.72700 47.96200 1.000 23.64091 ?  529 HOH A O   1 
HETATM 1847 O  O   . HOH C 3 .   ? 46.205   31.031   72.439   1.000 25.40741 ?  530 HOH A O   1 
HETATM 1848 O  O   . HOH C 3 .   ? 47.78800 38.16900 76.37500 1.000 40.82475 ?  531 HOH A O   1 
HETATM 1849 O  O   . HOH C 3 .   ? 56.39900 47.71100 63.54600 1.000 22.59167 ?  532 HOH A O   1 
HETATM 1850 O  O   . HOH C 3 .   ? 47.90100 36.22200 61.42600 1.000 16.24718 ?  533 HOH A O   1 
HETATM 1851 O  O   . HOH C 3 .   ? 54.20800 66.51400 33.33000 1.000 32.22138 ?  534 HOH A O   1 
HETATM 1852 O  O   . HOH C 3 .   ? 43.36300 23.95200 53.03700 1.000 25.93971 ?  535 HOH A O   1 
HETATM 1853 O  O   . HOH C 3 .   ? 49.08400 47.71300 66.90100 1.000 33.79280 ?  536 HOH A O   1 
HETATM 1854 O  O   . HOH C 3 .   ? 57.613   22.805   59.262   1.000 36.19068 ?  537 HOH A O   1 
HETATM 1855 O  O   . HOH C 3 .   ? 38.09300 36.93100 54.23500 1.000 15.03261 ?  538 HOH A O   1 
HETATM 1856 O  O   . HOH C 3 .   ? 42.59400 45.89300 56.98100 1.000 11.94667 ?  539 HOH A O   1 
HETATM 1857 O  O   . HOH C 3 .   ? 24.61200 47.48500 43.57800 1.000 17.12086 ?  540 HOH A O   1 
HETATM 1858 O  O   . HOH C 3 .   ? 42.82400 57.25500 53.93800 1.000 22.00333 ?  541 HOH A O   1 
HETATM 1859 O  O   . HOH C 3 .   ? 45.01400 52.08200 68.11900 1.000 43.05413 ?  542 HOH A O   1 
HETATM 1860 O  O   . HOH C 3 .   ? 60.557   58.473   36.783   1.000 36.23609 ?  543 HOH A O   1 
HETATM 1861 O  O   . HOH C 3 .   ? 46.61900 51.14200 66.05200 1.000 30.21736 ?  544 HOH A O   1 
HETATM 1862 O  O   . HOH C 3 .   ? 37.39800 38.38600 71.20700 1.000 17.84752 ?  545 HOH A O   1 
HETATM 1863 O  O   . HOH C 3 .   ? 52.95900 53.12700 62.25800 1.000 26.73253 ?  546 HOH A O   1 
HETATM 1864 O  O   . HOH C 3 .   ? 30.06200 34.32100 59.90000 1.000 30.43154 ?  547 HOH A O   1 
HETATM 1865 O  O   . HOH C 3 .   ? 46.93700 64.37000 25.65400 1.000 36.49996 ?  548 HOH A O   1 
HETATM 1866 O  O   . HOH C 3 .   ? 42.94400 29.84900 65.27200 1.000 28.08061 ?  549 HOH A O   1 
HETATM 1867 O  O   . HOH C 3 .   ? 62.81100 41.25100 41.43100 1.000 34.40220 ?  550 HOH A O   1 
HETATM 1868 O  O   . HOH C 3 .   ? 60.77500 35.77300 33.76500 1.000 43.06696 ?  551 HOH A O   1 
HETATM 1869 O  O   . HOH C 3 .   ? 37.39400 37.96200 56.68100 1.000 19.52921 ?  552 HOH A O   1 
HETATM 1870 O  O   . HOH C 3 .   ? 48.87800 48.87800 42.53800 0.50  13.58266 ?  553 HOH A O   1 
HETATM 1871 O  O   . HOH C 3 .   ? 48.39500 48.66300 50.44300 1.000 28.09800 ?  554 HOH A O   1 
HETATM 1872 O  O   . HOH C 3 .   ? 60.55000 31.11200 54.45900 1.000 30.24955 ?  555 HOH A O   1 
HETATM 1873 O  O   . HOH C 3 .   ? 53.17800 65.09500 25.82500 1.000 34.66738 ?  556 HOH A O   1 
HETATM 1874 O  O   . HOH C 3 .   ? 37.17200 34.20400 53.96900 1.000 14.90936 ?  557 HOH A O   1 
HETATM 1875 O  O   . HOH C 3 .   ? 48.11400 23.40300 45.82600 1.000 32.51250 ?  558 HOH A O   1 
HETATM 1876 O  O   . HOH C 3 .   ? 58.72200 24.01100 45.06500 1.000 40.72192 ?  559 HOH A O   1 
HETATM 1877 O  O   . HOH C 3 .   ? 64.99400 65.44900 28.87900 1.000 34.68905 ?  560 HOH A O   1 
HETATM 1878 O  O   . HOH C 3 .   ? 36.88700 43.86700 45.99500 1.000 11.33914 ?  561 HOH A O   1 
HETATM 1879 O  O   . HOH C 3 .   ? 40.25800 55.47300 61.40600 1.000 31.42691 ?  562 HOH A O   1 
HETATM 1880 O  O   . HOH C 3 .   ? 34.97700 56.29100 54.69900 1.000 37.79987 ?  563 HOH A O   1 
HETATM 1881 O  O   . HOH C 3 .   ? 26.80900 40.83800 59.49700 1.000 28.16914 ?  564 HOH A O   1 
HETATM 1882 O  O   . HOH C 3 .   ? 37.88200 35.48500 57.38400 1.000 25.10970 ?  565 HOH A O   1 
HETATM 1883 O  O   . HOH C 3 .   ? 25.46200 54.09900 58.19100 1.000 33.33244 ?  566 HOH A O   1 
HETATM 1884 O  O   . HOH C 3 .   ? 57.89900 24.35800 62.90800 1.000 28.99310 ?  567 HOH A O   1 
HETATM 1885 O  O   . HOH C 3 .   ? 57.07000 23.39600 56.41500 1.000 32.05750 ?  568 HOH A O   1 
HETATM 1886 O  O   . HOH C 3 .   ? 41.471   30.479   57.990   1.000 25.44190 ?  569 HOH A O   1 
HETATM 1887 O  O   . HOH C 3 .   ? 28.41300 50.60000 64.64500 1.000 40.44692 ?  570 HOH A O   1 
HETATM 1888 O  O   . HOH C 3 .   ? 61.06200 61.12500 33.56100 1.000 25.85754 ?  571 HOH A O   1 
HETATM 1889 O  O   . HOH C 3 .   ? 36.77900 49.47000 77.41200 1.000 38.30905 ?  572 HOH A O   1 
HETATM 1890 O  O   . HOH C 3 .   ? 54.822   60.477   22.313   1.000 31.31663 ?  573 HOH A O   1 
HETATM 1891 O  O   . HOH C 3 .   ? 63.40400 33.74400 51.91600 1.000 39.94453 ?  574 HOH A O   1 
HETATM 1892 O  O   . HOH C 3 .   ? 60.50600 23.11400 47.06000 1.000 43.18929 ?  575 HOH A O   1 
HETATM 1893 O  O   . HOH C 3 .   ? 58.16100 32.63800 64.51400 1.000 30.02992 ?  576 HOH A O   1 
HETATM 1894 O  O   . HOH C 3 .   ? 35.61300 48.70100 65.58700 1.000 30.11968 ?  577 HOH A O   1 
HETATM 1895 O  O   . HOH C 3 .   ? 27.62200 55.71500 57.25700 1.000 39.19171 ?  578 HOH A O   1 
HETATM 1896 O  O   . HOH C 3 .   ? 22.507   45.597   56.259   1.000 35.10952 ?  579 HOH A O   1 
HETATM 1897 O  O   . HOH C 3 .   ? 57.74600 25.44000 55.24800 1.000 33.31937 ?  580 HOH A O   1 
HETATM 1898 O  O   . HOH C 3 .   ? 59.69300 55.21900 45.68500 1.000 38.73749 ?  581 HOH A O   1 
HETATM 1899 O  O   . HOH C 3 .   ? 63.51500 44.41200 39.16900 1.000 40.72783 ?  582 HOH A O   1 
HETATM 1900 O  O   . HOH C 3 .   ? 34.48700 51.31500 77.01400 1.000 34.09610 ?  583 HOH A O   1 
HETATM 1901 O  O   . HOH C 3 .   ? 55.29800 51.90300 63.38600 1.000 33.61481 ?  584 HOH A O   1 
HETATM 1902 O  O   . HOH C 3 .   ? 32.91600 31.80600 44.81900 1.000 28.24849 ?  585 HOH A O   1 
HETATM 1903 O  O   . HOH C 3 .   ? 60.610   60.767   21.195   1.000 38.64996 ?  586 HOH A O   1 
HETATM 1904 O  O   . HOH C 3 .   ? 23.79400 42.92100 63.04000 1.000 37.19001 ?  587 HOH A O   1 
HETATM 1905 O  O   . HOH C 3 .   ? 39.75700 56.88000 51.45500 1.000 33.22658 ?  588 HOH A O   1 
HETATM 1906 O  O   . HOH C 3 .   ? 47.89100 25.29300 44.02800 1.000 33.98022 ?  589 HOH A O   1 
HETATM 1907 O  O   . HOH C 3 .   ? 25.20000 49.14900 61.81100 1.000 40.78830 ?  590 HOH A O   1 
HETATM 1908 O  O   . HOH C 3 .   ? 45.981   20.391   48.399   1.000 28.73184 ?  591 HOH A O   1 
HETATM 1909 O  O   . HOH C 3 .   ? 22.39000 45.70900 52.37300 1.000 30.04437 ?  592 HOH A O   1 
HETATM 1910 O  O   . HOH C 3 .   ? 68.413   62.620   26.380   1.000 28.97772 ?  593 HOH A O   1 
HETATM 1911 O  O   . HOH C 3 .   ? 42.14200 57.11200 60.55000 1.000 35.44970 ?  594 HOH A O   1 
HETATM 1912 O  O   . HOH C 3 .   ? 54.61000 55.61600 43.72400 1.000 35.55961 ?  595 HOH A O   1 
HETATM 1913 O  O   . HOH C 3 .   ? 57.96500 64.58700 32.98200 1.000 35.35402 ?  596 HOH A O   1 
HETATM 1914 O  O   . HOH C 3 .   ? 62.70300 54.24700 49.80200 1.000 30.11302 ?  597 HOH A O   1 
HETATM 1915 O  O   . HOH C 3 .   ? 22.32800 45.88000 45.97700 1.000 35.46129 ?  598 HOH A O   1 
HETATM 1916 O  O   . HOH C 3 .   ? 39.83100 55.89100 64.13200 1.000 29.85290 ?  599 HOH A O   1 
HETATM 1917 O  O   . HOH C 3 .   ? 41.778   27.653   66.157   1.000 26.71554 ?  600 HOH A O   1 
HETATM 1918 O  O   . HOH C 3 .   ? 23.23300 44.92500 43.82900 1.000 37.35956 ?  601 HOH A O   1 
HETATM 1919 O  O   . HOH C 3 .   ? 61.58200 29.81300 45.85600 1.000 32.40189 ?  602 HOH A O   1 
HETATM 1920 O  O   . HOH C 3 .   ? 34.51600 51.53100 66.26400 1.000 34.26114 ?  603 HOH A O   1 
HETATM 1921 O  O   . HOH C 3 .   ? 28.053   37.781   62.430   1.000 28.59512 ?  604 HOH A O   1 
HETATM 1922 O  O   . HOH C 3 .   ? 59.61200 62.86900 34.58800 1.000 34.99807 ?  605 HOH A O   1 
HETATM 1923 O  O   . HOH C 3 .   ? 65.36600 48.12700 39.49500 1.000 44.07212 ?  606 HOH A O   1 
HETATM 1924 O  O   . HOH C 3 .   ? 59.61000 45.72800 62.08800 1.000 42.53181 ?  607 HOH A O   1 
HETATM 1925 O  O   . HOH C 3 .   ? 63.10500 38.58600 55.67500 1.000 39.48633 ?  608 HOH A O   1 
HETATM 1926 O  O   . HOH C 3 .   ? 56.39700 31.12000 66.02100 1.000 27.85129 ?  609 HOH A O   1 
HETATM 1927 O  O   . HOH C 3 .   ? 55.442   26.413   36.709   1.000 34.07927 ?  610 HOH A O   1 
HETATM 1928 O  O   . HOH C 3 .   ? 42.94800 58.64200 58.21300 1.000 31.79089 ?  611 HOH A O   1 
HETATM 1929 O  O   . HOH C 3 .   ? 29.65500 55.98500 54.52200 1.000 35.86379 ?  612 HOH A O   1 
HETATM 1930 O  O   . HOH C 3 .   ? 57.38800 33.34900 34.32700 1.000 36.22340 ?  613 HOH A O   1 
HETATM 1931 O  O   . HOH C 3 .   ? 33.76200 33.76200 67.57000 0.50  28.09994 ?  614 HOH A O   1 
HETATM 1932 O  O   . HOH C 3 .   ? 64.36200 53.78800 47.98500 1.000 39.03955 ?  615 HOH A O   1 
HETATM 1933 O  O   . HOH C 3 .   ? 50.60600 63.83500 24.27800 1.000 34.76666 ?  616 HOH A O   1 
HETATM 1934 O  O   . HOH C 3 .   ? 55.70000 49.71700 64.86700 1.000 36.29874 ?  617 HOH A O   1 
HETATM 1935 O  O   . HOH C 3 .   ? 35.404   34.880   60.176   1.000 36.37375 ?  618 HOH A O   1 
HETATM 1936 O  O   . HOH C 3 .   ? 36.74100 55.63600 65.59100 1.000 38.44859 ?  619 HOH A O   1 
HETATM 1937 O  O   . HOH C 3 .   ? 61.16700 37.73700 57.22400 1.000 30.46800 ?  620 HOH A O   1 
HETATM 1938 O  O   . HOH C 3 .   ? 41.42900 58.79800 55.86500 1.000 31.13673 ?  621 HOH A O   1 
HETATM 1939 O  O   . HOH C 3 .   ? 60.41200 39.44600 59.33500 1.000 41.85010 ?  622 HOH A O   1 
HETATM 1940 O  O   . HOH C 3 .   ? 33.76200 33.76200 61.22700 0.50  24.14289 ?  623 HOH A O   1 
HETATM 1941 O  O   . HOH C 3 .   ? 49.257   22.713   40.806   1.000 40.48860 ?  624 HOH A O   1 
HETATM 1942 O  O   . HOH C 3 .   ? 37.83100 57.98300 48.90800 1.000 27.29681 ?  625 HOH A O   1 
HETATM 1943 O  O   . HOH C 3 .   ? 33.76200 33.76200 64.91500 0.50  23.17474 ?  626 HOH A O   1 
HETATM 1944 O  O   . HOH C 3 .   ? 58.79800 47.78900 62.27800 1.000 38.31163 ?  627 HOH A O   1 
HETATM 1945 O  O   . HOH C 3 .   ? 48.51300 64.53200 24.04500 1.000 44.66906 ?  628 HOH A O   1 
HETATM 1946 O  O   . HOH C 3 .   ? 61.33500 35.12000 58.76600 1.000 38.31059 ?  629 HOH A O   1 
HETATM 1947 O  O   . HOH C 3 .   ? 33.68800 53.47000 64.48500 1.000 40.36653 ?  630 HOH A O   1 
HETATM 1948 O  O   . HOH C 3 .   ? 50.52000 45.52400 66.93500 1.000 36.14643 ?  631 HOH A O   1 
HETATM 1949 O  O   . HOH C 3 .   ? 58.16000 35.38000 34.59600 1.000 35.67399 ?  632 HOH A O   1 
HETATM 1950 O  O   . HOH C 3 .   ? 56.61200 28.16100 34.53500 1.000 33.90031 ?  633 HOH A O   1 
HETATM 1951 O  O   . HOH C 3 .   ? 55.29600 30.26200 32.73700 1.000 39.56742 ?  634 HOH A O   1 
# 
