data_7H65
# 
_entry.id   7H65 
# 
_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   7H65         pdb_00007h65 10.2210/pdb7h65/pdb 
WWPDB D_1001407072 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-05 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7H65 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-19 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Rudolph 
_pdbx_contact_author.name_first         Markus 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              markus.rudolph@roche.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0447-1101 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Banner, D.W.'  1 
'Benz, J.M.'    2 
'Schlatter, D.' 3 
'Hilpert, H.'   4 
# 
_citation.id                        primary 
_citation.title                     'Crystal structures of human Chymase and Cathepsin G' 
_citation.journal_abbrev            'To be published' 
_citation.year                      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Markus, R.'    1 0000-0003-0447-1101 
primary 'Tosstorff, A.' 2 0000-0002-4969-3667 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Chymase 25032.910 1   3.4.21.39 NO ? ? 
2 non-polymer syn 'ZINC ION' 65.409    1   ?         ?  ? ? 
3 non-polymer syn 
;N-(1-{2-[(S)-[(3S)-2-hydroxy-3-methyl-3-(4-methylphenyl)-4-oxocyclobut-1-en-1-yl](phenyl)methyl]-6-methyl-1H-indol-3-yl}-2-methylpropan-2-yl)acetamide
;
520.661   1   ?         ?  ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    2   ?         ?  ? ? 
5 water       nat water 18.015    270 ?         ?  ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Alpha-chymase,Mast cell protease I' 
# 
_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       
;IIGGTESKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQKNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IIGGTESKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQKNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_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 
;N-(1-{2-[(S)-[(3S)-2-hydroxy-3-methyl-3-(4-methylphenyl)-4-oxocyclobut-1-en-1-yl](phenyl)methyl]-6-methyl-1H-indol-3-yl}-2-methylpropan-2-yl)acetamide
;
A1AO1 
4 'DIMETHYL SULFOXIDE' DMS   
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   ILE n 
1 3   GLY n 
1 4   GLY n 
1 5   THR n 
1 6   GLU n 
1 7   SER n 
1 8   LYS n 
1 9   PRO n 
1 10  HIS n 
1 11  SER n 
1 12  ARG n 
1 13  PRO n 
1 14  TYR n 
1 15  MET n 
1 16  ALA n 
1 17  TYR n 
1 18  LEU n 
1 19  GLU n 
1 20  ILE n 
1 21  VAL n 
1 22  THR n 
1 23  SER n 
1 24  ASN n 
1 25  GLY n 
1 26  PRO n 
1 27  SER n 
1 28  LYS n 
1 29  PHE n 
1 30  CYS n 
1 31  GLY n 
1 32  GLY n 
1 33  PHE n 
1 34  LEU n 
1 35  ILE n 
1 36  ARG n 
1 37  ARG n 
1 38  ASN n 
1 39  PHE n 
1 40  VAL n 
1 41  LEU n 
1 42  THR n 
1 43  ALA n 
1 44  ALA n 
1 45  HIS n 
1 46  CYS n 
1 47  ALA n 
1 48  GLY n 
1 49  ARG n 
1 50  SER n 
1 51  ILE n 
1 52  THR n 
1 53  VAL n 
1 54  THR n 
1 55  LEU n 
1 56  GLY n 
1 57  ALA n 
1 58  HIS n 
1 59  ASN n 
1 60  ILE n 
1 61  THR n 
1 62  GLU n 
1 63  GLU n 
1 64  GLU n 
1 65  ASP n 
1 66  THR n 
1 67  TRP n 
1 68  GLN n 
1 69  LYS n 
1 70  LEU n 
1 71  GLU n 
1 72  VAL n 
1 73  ILE n 
1 74  LYS n 
1 75  GLN n 
1 76  PHE n 
1 77  ARG n 
1 78  HIS n 
1 79  PRO n 
1 80  LYS n 
1 81  TYR n 
1 82  ASN n 
1 83  THR n 
1 84  SER n 
1 85  THR n 
1 86  LEU n 
1 87  HIS n 
1 88  HIS n 
1 89  ASP n 
1 90  ILE n 
1 91  MET n 
1 92  LEU n 
1 93  LEU n 
1 94  LYS n 
1 95  LEU n 
1 96  LYS n 
1 97  GLU n 
1 98  LYS n 
1 99  ALA n 
1 100 SER n 
1 101 LEU n 
1 102 THR n 
1 103 LEU n 
1 104 ALA n 
1 105 VAL n 
1 106 GLY n 
1 107 THR n 
1 108 LEU n 
1 109 PRO n 
1 110 PHE n 
1 111 PRO n 
1 112 SER n 
1 113 GLN n 
1 114 LYS n 
1 115 ASN n 
1 116 PHE n 
1 117 VAL n 
1 118 PRO n 
1 119 PRO n 
1 120 GLY n 
1 121 ARG n 
1 122 MET n 
1 123 CYS n 
1 124 ARG n 
1 125 VAL n 
1 126 ALA n 
1 127 GLY n 
1 128 TRP n 
1 129 GLY n 
1 130 ARG n 
1 131 THR n 
1 132 GLY n 
1 133 VAL n 
1 134 LEU n 
1 135 LYS n 
1 136 PRO n 
1 137 GLY n 
1 138 SER n 
1 139 ASP n 
1 140 THR n 
1 141 LEU n 
1 142 GLN n 
1 143 GLU n 
1 144 VAL n 
1 145 LYS n 
1 146 LEU n 
1 147 ARG n 
1 148 LEU n 
1 149 MET n 
1 150 ASP n 
1 151 PRO n 
1 152 GLN n 
1 153 ALA n 
1 154 CYS n 
1 155 SER n 
1 156 HIS n 
1 157 PHE n 
1 158 ARG n 
1 159 ASP n 
1 160 PHE n 
1 161 ASP n 
1 162 HIS n 
1 163 ASN n 
1 164 LEU n 
1 165 GLN n 
1 166 LEU n 
1 167 CYS n 
1 168 VAL n 
1 169 GLY n 
1 170 ASN n 
1 171 PRO n 
1 172 ARG n 
1 173 LYS n 
1 174 THR n 
1 175 LYS n 
1 176 SER n 
1 177 ALA n 
1 178 PHE n 
1 179 LYS n 
1 180 GLY n 
1 181 ASP n 
1 182 SER n 
1 183 GLY n 
1 184 GLY n 
1 185 PRO n 
1 186 LEU n 
1 187 LEU n 
1 188 CYS n 
1 189 ALA n 
1 190 GLY n 
1 191 VAL n 
1 192 ALA n 
1 193 GLN n 
1 194 GLY n 
1 195 ILE n 
1 196 VAL n 
1 197 SER n 
1 198 TYR n 
1 199 GLY n 
1 200 ARG n 
1 201 SER n 
1 202 ASP n 
1 203 ALA n 
1 204 LYS n 
1 205 PRO n 
1 206 PRO n 
1 207 ALA n 
1 208 VAL n 
1 209 PHE n 
1 210 THR n 
1 211 ARG n 
1 212 ILE n 
1 213 SER n 
1 214 HIS n 
1 215 TYR n 
1 216 ARG n 
1 217 PRO n 
1 218 TRP n 
1 219 ILE n 
1 220 ASN n 
1 221 GLN n 
1 222 ILE n 
1 223 LEU n 
1 224 GLN n 
1 225 ALA n 
1 226 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   226 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CMA1, CYH, CYM' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AO1 non-polymer         . 
;N-(1-{2-[(S)-[(3S)-2-hydroxy-3-methyl-3-(4-methylphenyl)-4-oxocyclobut-1-en-1-yl](phenyl)methyl]-6-methyl-1H-indol-3-yl}-2-methylpropan-2-yl)acetamide
;
? 'C34 H36 N2 O3'  520.661 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'      78.133  
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   ILE 1   16  16  ILE ILE A . n 
A 1 2   ILE 2   17  17  ILE ILE A . n 
A 1 3   GLY 3   18  18  GLY GLY A . n 
A 1 4   GLY 4   19  19  GLY GLY A . n 
A 1 5   THR 5   20  20  THR THR A . n 
A 1 6   GLU 6   21  21  GLU GLU A . n 
A 1 7   SER 7   22  22  SER SER A . n 
A 1 8   LYS 8   23  23  LYS LYS A . n 
A 1 9   PRO 9   24  24  PRO PRO A . n 
A 1 10  HIS 10  25  25  HIS HIS A . n 
A 1 11  SER 11  26  26  SER SER A . n 
A 1 12  ARG 12  27  27  ARG ARG A . n 
A 1 13  PRO 13  28  28  PRO PRO A . n 
A 1 14  TYR 14  29  29  TYR TYR A . n 
A 1 15  MET 15  30  30  MET MET A . n 
A 1 16  ALA 16  31  31  ALA ALA A . n 
A 1 17  TYR 17  32  32  TYR TYR A . n 
A 1 18  LEU 18  33  33  LEU LEU A . n 
A 1 19  GLU 19  34  34  GLU GLU A . n 
A 1 20  ILE 20  35  35  ILE ILE A . n 
A 1 21  VAL 21  36  36  VAL VAL A . n 
A 1 22  THR 22  36  36  THR THR A A n 
A 1 23  SER 23  36  36  SER SER A B n 
A 1 24  ASN 24  37  37  ASN ASN A . n 
A 1 25  GLY 25  37  37  GLY GLY A A n 
A 1 26  PRO 26  38  38  PRO PRO A . n 
A 1 27  SER 27  39  39  SER SER A . n 
A 1 28  LYS 28  40  40  LYS LYS A . n 
A 1 29  PHE 29  41  41  PHE PHE A . n 
A 1 30  CYS 30  42  42  CYS CYS A . n 
A 1 31  GLY 31  43  43  GLY GLY A . n 
A 1 32  GLY 32  44  44  GLY GLY A . n 
A 1 33  PHE 33  45  45  PHE PHE A . n 
A 1 34  LEU 34  46  46  LEU LEU A . n 
A 1 35  ILE 35  47  47  ILE ILE A . n 
A 1 36  ARG 36  48  48  ARG ARG A . n 
A 1 37  ARG 37  49  49  ARG ARG A . n 
A 1 38  ASN 38  50  50  ASN ASN A . n 
A 1 39  PHE 39  51  51  PHE PHE A . n 
A 1 40  VAL 40  52  52  VAL VAL A . n 
A 1 41  LEU 41  53  53  LEU LEU A . n 
A 1 42  THR 42  54  54  THR THR A . n 
A 1 43  ALA 43  55  55  ALA ALA A . n 
A 1 44  ALA 44  56  56  ALA ALA A . n 
A 1 45  HIS 45  57  57  HIS HIS A . n 
A 1 46  CYS 46  58  58  CYS CYS A . n 
A 1 47  ALA 47  59  59  ALA ALA A . n 
A 1 48  GLY 48  60  60  GLY GLY A . n 
A 1 49  ARG 49  61  61  ARG ARG A . n 
A 1 50  SER 50  63  63  SER SER A . n 
A 1 51  ILE 51  64  64  ILE ILE A . n 
A 1 52  THR 52  65  65  THR THR A . n 
A 1 53  VAL 53  66  66  VAL VAL A . n 
A 1 54  THR 54  67  67  THR THR A . n 
A 1 55  LEU 55  68  68  LEU LEU A . n 
A 1 56  GLY 56  69  69  GLY GLY A . n 
A 1 57  ALA 57  70  70  ALA ALA A . n 
A 1 58  HIS 58  71  71  HIS HIS A . n 
A 1 59  ASN 59  72  72  ASN ASN A . n 
A 1 60  ILE 60  73  73  ILE ILE A . n 
A 1 61  THR 61  74  74  THR THR A . n 
A 1 62  GLU 62  75  75  GLU GLU A . n 
A 1 63  GLU 63  76  76  GLU GLU A . n 
A 1 64  GLU 64  77  77  GLU GLU A . n 
A 1 65  ASP 65  78  78  ASP ASP A . n 
A 1 66  THR 66  79  79  THR THR A . n 
A 1 67  TRP 67  80  80  TRP TRP A . n 
A 1 68  GLN 68  81  81  GLN GLN A . n 
A 1 69  LYS 69  82  82  LYS LYS A . n 
A 1 70  LEU 70  83  83  LEU LEU A . n 
A 1 71  GLU 71  84  84  GLU GLU A . n 
A 1 72  VAL 72  85  85  VAL VAL A . n 
A 1 73  ILE 73  86  86  ILE ILE A . n 
A 1 74  LYS 74  87  87  LYS LYS A . n 
A 1 75  GLN 75  88  88  GLN GLN A . n 
A 1 76  PHE 76  89  89  PHE PHE A . n 
A 1 77  ARG 77  90  90  ARG ARG A . n 
A 1 78  HIS 78  91  91  HIS HIS A . n 
A 1 79  PRO 79  92  92  PRO PRO A . n 
A 1 80  LYS 80  93  93  LYS LYS A . n 
A 1 81  TYR 81  94  94  TYR TYR A . n 
A 1 82  ASN 82  95  95  ASN ASN A . n 
A 1 83  THR 83  96  96  THR THR A . n 
A 1 84  SER 84  97  97  SER SER A . n 
A 1 85  THR 85  98  98  THR THR A . n 
A 1 86  LEU 86  99  99  LEU LEU A . n 
A 1 87  HIS 87  100 100 HIS HIS A . n 
A 1 88  HIS 88  101 101 HIS HIS A . n 
A 1 89  ASP 89  102 102 ASP ASP A . n 
A 1 90  ILE 90  103 103 ILE ILE A . n 
A 1 91  MET 91  104 104 MET MET A . n 
A 1 92  LEU 92  105 105 LEU LEU A . n 
A 1 93  LEU 93  106 106 LEU LEU A . n 
A 1 94  LYS 94  107 107 LYS LYS A . n 
A 1 95  LEU 95  108 108 LEU LEU A . n 
A 1 96  LYS 96  109 109 LYS LYS A . n 
A 1 97  GLU 97  110 110 GLU GLU A . n 
A 1 98  LYS 98  111 111 LYS LYS A . n 
A 1 99  ALA 99  112 112 ALA ALA A . n 
A 1 100 SER 100 113 113 SER SER A . n 
A 1 101 LEU 101 114 114 LEU LEU A . n 
A 1 102 THR 102 115 115 THR THR A . n 
A 1 103 LEU 103 116 116 LEU LEU A . n 
A 1 104 ALA 104 117 117 ALA ALA A . n 
A 1 105 VAL 105 118 118 VAL VAL A . n 
A 1 106 GLY 106 119 119 GLY GLY A . n 
A 1 107 THR 107 120 120 THR THR A . n 
A 1 108 LEU 108 121 121 LEU LEU A . n 
A 1 109 PRO 109 122 122 PRO PRO A . n 
A 1 110 PHE 110 123 123 PHE PHE A . n 
A 1 111 PRO 111 124 124 PRO PRO A . n 
A 1 112 SER 112 125 ?   ?   ?   A . n 
A 1 113 GLN 113 126 ?   ?   ?   A . n 
A 1 114 LYS 114 127 ?   ?   ?   A . n 
A 1 115 ASN 115 128 ?   ?   ?   A . n 
A 1 116 PHE 116 129 ?   ?   ?   A . n 
A 1 117 VAL 117 130 ?   ?   ?   A . n 
A 1 118 PRO 118 131 ?   ?   ?   A . n 
A 1 119 PRO 119 132 132 PRO PRO A . n 
A 1 120 GLY 120 133 133 GLY GLY A . n 
A 1 121 ARG 121 134 134 ARG ARG A . n 
A 1 122 MET 122 135 135 MET MET A . n 
A 1 123 CYS 123 136 136 CYS CYS A . n 
A 1 124 ARG 124 137 137 ARG ARG A . n 
A 1 125 VAL 125 138 138 VAL VAL A . n 
A 1 126 ALA 126 139 139 ALA ALA A . n 
A 1 127 GLY 127 140 140 GLY GLY A . n 
A 1 128 TRP 128 141 141 TRP TRP A . n 
A 1 129 GLY 129 142 142 GLY GLY A . n 
A 1 130 ARG 130 143 143 ARG ARG A . n 
A 1 131 THR 131 144 144 THR THR A . n 
A 1 132 GLY 132 145 145 GLY GLY A . n 
A 1 133 VAL 133 146 146 VAL VAL A . n 
A 1 134 LEU 134 147 147 LEU LEU A . n 
A 1 135 LYS 135 148 148 LYS LYS A . n 
A 1 136 PRO 136 150 150 PRO PRO A . n 
A 1 137 GLY 137 151 151 GLY GLY A . n 
A 1 138 SER 138 152 152 SER SER A . n 
A 1 139 ASP 139 153 153 ASP ASP A . n 
A 1 140 THR 140 154 154 THR THR A . n 
A 1 141 LEU 141 155 155 LEU LEU A . n 
A 1 142 GLN 142 156 156 GLN GLN A . n 
A 1 143 GLU 143 157 157 GLU GLU A . n 
A 1 144 VAL 144 158 158 VAL VAL A . n 
A 1 145 LYS 145 159 159 LYS LYS A . n 
A 1 146 LEU 146 160 160 LEU LEU A . n 
A 1 147 ARG 147 161 161 ARG ARG A . n 
A 1 148 LEU 148 162 162 LEU LEU A . n 
A 1 149 MET 149 163 163 MET MET A . n 
A 1 150 ASP 150 164 164 ASP ASP A . n 
A 1 151 PRO 151 165 165 PRO PRO A . n 
A 1 152 GLN 152 166 166 GLN GLN A . n 
A 1 153 ALA 153 167 167 ALA ALA A . n 
A 1 154 CYS 154 168 168 CYS CYS A . n 
A 1 155 SER 155 169 169 SER SER A . n 
A 1 156 HIS 156 172 172 HIS HIS A . n 
A 1 157 PHE 157 173 173 PHE PHE A . n 
A 1 158 ARG 158 174 174 ARG ARG A . n 
A 1 159 ASP 159 175 175 ASP ASP A . n 
A 1 160 PHE 160 176 176 PHE PHE A . n 
A 1 161 ASP 161 177 177 ASP ASP A . n 
A 1 162 HIS 162 178 178 HIS HIS A . n 
A 1 163 ASN 163 178 178 ASN ASN A A n 
A 1 164 LEU 164 179 179 LEU LEU A . n 
A 1 165 GLN 165 180 180 GLN GLN A . n 
A 1 166 LEU 166 181 181 LEU LEU A . n 
A 1 167 CYS 167 182 182 CYS CYS A . n 
A 1 168 VAL 168 183 183 VAL VAL A . n 
A 1 169 GLY 169 184 184 GLY GLY A . n 
A 1 170 ASN 170 185 185 ASN ASN A . n 
A 1 171 PRO 171 186 186 PRO PRO A . n 
A 1 172 ARG 172 186 186 ARG ARG A A n 
A 1 173 LYS 173 186 186 LYS LYS A B n 
A 1 174 THR 174 187 187 THR THR A . n 
A 1 175 LYS 175 188 188 LYS LYS A . n 
A 1 176 SER 176 189 189 SER SER A . n 
A 1 177 ALA 177 190 190 ALA ALA A . n 
A 1 178 PHE 178 191 191 PHE PHE A . n 
A 1 179 LYS 179 192 192 LYS LYS A . n 
A 1 180 GLY 180 193 193 GLY GLY A . n 
A 1 181 ASP 181 194 194 ASP ASP A . n 
A 1 182 SER 182 195 195 SER SER A . n 
A 1 183 GLY 183 196 196 GLY GLY A . n 
A 1 184 GLY 184 197 197 GLY GLY A . n 
A 1 185 PRO 185 198 198 PRO PRO A . n 
A 1 186 LEU 186 199 199 LEU LEU A . n 
A 1 187 LEU 187 200 200 LEU LEU A . n 
A 1 188 CYS 188 201 201 CYS CYS A . n 
A 1 189 ALA 189 202 202 ALA ALA A . n 
A 1 190 GLY 190 207 207 GLY GLY A . n 
A 1 191 VAL 191 208 208 VAL VAL A . n 
A 1 192 ALA 192 209 209 ALA ALA A . n 
A 1 193 GLN 193 210 210 GLN GLN A . n 
A 1 194 GLY 194 211 211 GLY GLY A . n 
A 1 195 ILE 195 212 212 ILE ILE A . n 
A 1 196 VAL 196 213 213 VAL VAL A . n 
A 1 197 SER 197 214 214 SER SER A . n 
A 1 198 TYR 198 215 215 TYR TYR A . n 
A 1 199 GLY 199 216 216 GLY GLY A . n 
A 1 200 ARG 200 217 217 ARG ARG A . n 
A 1 201 SER 201 218 218 SER SER A . n 
A 1 202 ASP 202 219 219 ASP ASP A . n 
A 1 203 ALA 203 220 220 ALA ALA A . n 
A 1 204 LYS 204 221 221 LYS LYS A . n 
A 1 205 PRO 205 224 224 PRO PRO A . n 
A 1 206 PRO 206 225 225 PRO PRO A . n 
A 1 207 ALA 207 226 226 ALA ALA A . n 
A 1 208 VAL 208 227 227 VAL VAL A . n 
A 1 209 PHE 209 228 228 PHE PHE A . n 
A 1 210 THR 210 229 229 THR THR A . n 
A 1 211 ARG 211 230 230 ARG ARG A . n 
A 1 212 ILE 212 231 231 ILE ILE A . n 
A 1 213 SER 213 232 232 SER SER A . n 
A 1 214 HIS 214 233 233 HIS HIS A . n 
A 1 215 TYR 215 234 234 TYR TYR A . n 
A 1 216 ARG 216 235 235 ARG ARG A . n 
A 1 217 PRO 217 236 236 PRO PRO A . n 
A 1 218 TRP 218 237 237 TRP TRP A . n 
A 1 219 ILE 219 238 238 ILE ILE A . n 
A 1 220 ASN 220 239 239 ASN ASN A . n 
A 1 221 GLN 221 240 240 GLN GLN A . n 
A 1 222 ILE 222 241 241 ILE ILE A . n 
A 1 223 LEU 223 242 242 LEU LEU A . n 
A 1 224 GLN 224 243 243 GLN GLN A . n 
A 1 225 ALA 225 244 244 ALA ALA A . n 
A 1 226 ASN 226 245 245 ASN ASN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AO1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AO1 
_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 1000 ZN    ZN  A . 
C 3 A1AO1 1   302 1001 A1AO1 LIG A . 
D 4 DMS   1   303 1    DMS   DMS A . 
E 4 DMS   1   304 2    DMS   DMS A . 
F 5 HOH   1   401 528  HOH   HOH A . 
F 5 HOH   2   402 195  HOH   HOH A . 
F 5 HOH   3   403 40   HOH   HOH A . 
F 5 HOH   4   404 462  HOH   HOH A . 
F 5 HOH   5   405 561  HOH   HOH A . 
F 5 HOH   6   406 579  HOH   HOH A . 
F 5 HOH   7   407 45   HOH   HOH A . 
F 5 HOH   8   408 128  HOH   HOH A . 
F 5 HOH   9   409 25   HOH   HOH A . 
F 5 HOH   10  410 169  HOH   HOH A . 
F 5 HOH   11  411 122  HOH   HOH A . 
F 5 HOH   12  412 174  HOH   HOH A . 
F 5 HOH   13  413 78   HOH   HOH A . 
F 5 HOH   14  414 83   HOH   HOH A . 
F 5 HOH   15  415 37   HOH   HOH A . 
F 5 HOH   16  416 148  HOH   HOH A . 
F 5 HOH   17  417 15   HOH   HOH A . 
F 5 HOH   18  418 477  HOH   HOH A . 
F 5 HOH   19  419 167  HOH   HOH A . 
F 5 HOH   20  420 43   HOH   HOH A . 
F 5 HOH   21  421 203  HOH   HOH A . 
F 5 HOH   22  422 246  HOH   HOH A . 
F 5 HOH   23  423 513  HOH   HOH A . 
F 5 HOH   24  424 242  HOH   HOH A . 
F 5 HOH   25  425 577  HOH   HOH A . 
F 5 HOH   26  426 286  HOH   HOH A . 
F 5 HOH   27  427 303  HOH   HOH A . 
F 5 HOH   28  428 8    HOH   HOH A . 
F 5 HOH   29  429 50   HOH   HOH A . 
F 5 HOH   30  430 23   HOH   HOH A . 
F 5 HOH   31  431 238  HOH   HOH A . 
F 5 HOH   32  432 381  HOH   HOH A . 
F 5 HOH   33  433 168  HOH   HOH A . 
F 5 HOH   34  434 69   HOH   HOH A . 
F 5 HOH   35  435 569  HOH   HOH A . 
F 5 HOH   36  436 21   HOH   HOH A . 
F 5 HOH   37  437 94   HOH   HOH A . 
F 5 HOH   38  438 382  HOH   HOH A . 
F 5 HOH   39  439 576  HOH   HOH A . 
F 5 HOH   40  440 284  HOH   HOH A . 
F 5 HOH   41  441 126  HOH   HOH A . 
F 5 HOH   42  442 211  HOH   HOH A . 
F 5 HOH   43  443 72   HOH   HOH A . 
F 5 HOH   44  444 298  HOH   HOH A . 
F 5 HOH   45  445 515  HOH   HOH A . 
F 5 HOH   46  446 580  HOH   HOH A . 
F 5 HOH   47  447 144  HOH   HOH A . 
F 5 HOH   48  448 555  HOH   HOH A . 
F 5 HOH   49  449 408  HOH   HOH A . 
F 5 HOH   50  450 44   HOH   HOH A . 
F 5 HOH   51  451 3    HOH   HOH A . 
F 5 HOH   52  452 11   HOH   HOH A . 
F 5 HOH   53  453 34   HOH   HOH A . 
F 5 HOH   54  454 565  HOH   HOH A . 
F 5 HOH   55  455 243  HOH   HOH A . 
F 5 HOH   56  456 22   HOH   HOH A . 
F 5 HOH   57  457 82   HOH   HOH A . 
F 5 HOH   58  458 255  HOH   HOH A . 
F 5 HOH   59  459 326  HOH   HOH A . 
F 5 HOH   60  460 20   HOH   HOH A . 
F 5 HOH   61  461 17   HOH   HOH A . 
F 5 HOH   62  462 55   HOH   HOH A . 
F 5 HOH   63  463 406  HOH   HOH A . 
F 5 HOH   64  464 52   HOH   HOH A . 
F 5 HOH   65  465 575  HOH   HOH A . 
F 5 HOH   66  466 91   HOH   HOH A . 
F 5 HOH   67  467 574  HOH   HOH A . 
F 5 HOH   68  468 145  HOH   HOH A . 
F 5 HOH   69  469 171  HOH   HOH A . 
F 5 HOH   70  470 4    HOH   HOH A . 
F 5 HOH   71  471 270  HOH   HOH A . 
F 5 HOH   72  472 383  HOH   HOH A . 
F 5 HOH   73  473 151  HOH   HOH A . 
F 5 HOH   74  474 143  HOH   HOH A . 
F 5 HOH   75  475 36   HOH   HOH A . 
F 5 HOH   76  476 176  HOH   HOH A . 
F 5 HOH   77  477 200  HOH   HOH A . 
F 5 HOH   78  478 343  HOH   HOH A . 
F 5 HOH   79  479 160  HOH   HOH A . 
F 5 HOH   80  480 41   HOH   HOH A . 
F 5 HOH   81  481 158  HOH   HOH A . 
F 5 HOH   82  482 10   HOH   HOH A . 
F 5 HOH   83  483 33   HOH   HOH A . 
F 5 HOH   84  484 35   HOH   HOH A . 
F 5 HOH   85  485 16   HOH   HOH A . 
F 5 HOH   86  486 93   HOH   HOH A . 
F 5 HOH   87  487 62   HOH   HOH A . 
F 5 HOH   88  488 9    HOH   HOH A . 
F 5 HOH   89  489 111  HOH   HOH A . 
F 5 HOH   90  490 68   HOH   HOH A . 
F 5 HOH   91  491 79   HOH   HOH A . 
F 5 HOH   92  492 74   HOH   HOH A . 
F 5 HOH   93  493 292  HOH   HOH A . 
F 5 HOH   94  494 465  HOH   HOH A . 
F 5 HOH   95  495 57   HOH   HOH A . 
F 5 HOH   96  496 568  HOH   HOH A . 
F 5 HOH   97  497 67   HOH   HOH A . 
F 5 HOH   98  498 581  HOH   HOH A . 
F 5 HOH   99  499 24   HOH   HOH A . 
F 5 HOH   100 500 202  HOH   HOH A . 
F 5 HOH   101 501 119  HOH   HOH A . 
F 5 HOH   102 502 18   HOH   HOH A . 
F 5 HOH   103 503 2    HOH   HOH A . 
F 5 HOH   104 504 305  HOH   HOH A . 
F 5 HOH   105 505 5    HOH   HOH A . 
F 5 HOH   106 506 42   HOH   HOH A . 
F 5 HOH   107 507 47   HOH   HOH A . 
F 5 HOH   108 508 134  HOH   HOH A . 
F 5 HOH   109 509 85   HOH   HOH A . 
F 5 HOH   110 510 27   HOH   HOH A . 
F 5 HOH   111 511 48   HOH   HOH A . 
F 5 HOH   112 512 58   HOH   HOH A . 
F 5 HOH   113 513 348  HOH   HOH A . 
F 5 HOH   114 514 385  HOH   HOH A . 
F 5 HOH   115 515 103  HOH   HOH A . 
F 5 HOH   116 516 108  HOH   HOH A . 
F 5 HOH   117 517 92   HOH   HOH A . 
F 5 HOH   118 518 267  HOH   HOH A . 
F 5 HOH   119 519 38   HOH   HOH A . 
F 5 HOH   120 520 269  HOH   HOH A . 
F 5 HOH   121 521 84   HOH   HOH A . 
F 5 HOH   122 522 13   HOH   HOH A . 
F 5 HOH   123 523 49   HOH   HOH A . 
F 5 HOH   124 524 66   HOH   HOH A . 
F 5 HOH   125 525 1    HOH   HOH A . 
F 5 HOH   126 526 182  HOH   HOH A . 
F 5 HOH   127 527 190  HOH   HOH A . 
F 5 HOH   128 528 224  HOH   HOH A . 
F 5 HOH   129 529 76   HOH   HOH A . 
F 5 HOH   130 530 185  HOH   HOH A . 
F 5 HOH   131 531 12   HOH   HOH A . 
F 5 HOH   132 532 7    HOH   HOH A . 
F 5 HOH   133 533 297  HOH   HOH A . 
F 5 HOH   134 534 19   HOH   HOH A . 
F 5 HOH   135 535 100  HOH   HOH A . 
F 5 HOH   136 536 389  HOH   HOH A . 
F 5 HOH   137 537 448  HOH   HOH A . 
F 5 HOH   138 538 110  HOH   HOH A . 
F 5 HOH   139 539 438  HOH   HOH A . 
F 5 HOH   140 540 218  HOH   HOH A . 
F 5 HOH   141 541 30   HOH   HOH A . 
F 5 HOH   142 542 104  HOH   HOH A . 
F 5 HOH   143 543 97   HOH   HOH A . 
F 5 HOH   144 544 113  HOH   HOH A . 
F 5 HOH   145 545 139  HOH   HOH A . 
F 5 HOH   146 546 28   HOH   HOH A . 
F 5 HOH   147 547 130  HOH   HOH A . 
F 5 HOH   148 548 159  HOH   HOH A . 
F 5 HOH   149 549 183  HOH   HOH A . 
F 5 HOH   150 550 51   HOH   HOH A . 
F 5 HOH   151 551 237  HOH   HOH A . 
F 5 HOH   152 552 402  HOH   HOH A . 
F 5 HOH   153 553 417  HOH   HOH A . 
F 5 HOH   154 554 102  HOH   HOH A . 
F 5 HOH   155 555 150  HOH   HOH A . 
F 5 HOH   156 556 132  HOH   HOH A . 
F 5 HOH   157 557 559  HOH   HOH A . 
F 5 HOH   158 558 80   HOH   HOH A . 
F 5 HOH   159 559 454  HOH   HOH A . 
F 5 HOH   160 560 60   HOH   HOH A . 
F 5 HOH   161 561 233  HOH   HOH A . 
F 5 HOH   162 562 157  HOH   HOH A . 
F 5 HOH   163 563 387  HOH   HOH A . 
F 5 HOH   164 564 285  HOH   HOH A . 
F 5 HOH   165 565 70   HOH   HOH A . 
F 5 HOH   166 566 88   HOH   HOH A . 
F 5 HOH   167 567 204  HOH   HOH A . 
F 5 HOH   168 568 105  HOH   HOH A . 
F 5 HOH   169 569 32   HOH   HOH A . 
F 5 HOH   170 570 39   HOH   HOH A . 
F 5 HOH   171 571 274  HOH   HOH A . 
F 5 HOH   172 572 87   HOH   HOH A . 
F 5 HOH   173 573 81   HOH   HOH A . 
F 5 HOH   174 574 98   HOH   HOH A . 
F 5 HOH   175 575 53   HOH   HOH A . 
F 5 HOH   176 576 210  HOH   HOH A . 
F 5 HOH   177 577 120  HOH   HOH A . 
F 5 HOH   178 578 123  HOH   HOH A . 
F 5 HOH   179 579 372  HOH   HOH A . 
F 5 HOH   180 580 409  HOH   HOH A . 
F 5 HOH   181 581 141  HOH   HOH A . 
F 5 HOH   182 582 59   HOH   HOH A . 
F 5 HOH   183 583 189  HOH   HOH A . 
F 5 HOH   184 584 173  HOH   HOH A . 
F 5 HOH   185 585 29   HOH   HOH A . 
F 5 HOH   186 586 114  HOH   HOH A . 
F 5 HOH   187 587 212  HOH   HOH A . 
F 5 HOH   188 588 6    HOH   HOH A . 
F 5 HOH   189 589 405  HOH   HOH A . 
F 5 HOH   190 590 71   HOH   HOH A . 
F 5 HOH   191 591 582  HOH   HOH A . 
F 5 HOH   192 592 578  HOH   HOH A . 
F 5 HOH   193 593 106  HOH   HOH A . 
F 5 HOH   194 594 289  HOH   HOH A . 
F 5 HOH   195 595 236  HOH   HOH A . 
F 5 HOH   196 596 99   HOH   HOH A . 
F 5 HOH   197 597 479  HOH   HOH A . 
F 5 HOH   198 598 441  HOH   HOH A . 
F 5 HOH   199 599 193  HOH   HOH A . 
F 5 HOH   200 600 14   HOH   HOH A . 
F 5 HOH   201 601 177  HOH   HOH A . 
F 5 HOH   202 602 440  HOH   HOH A . 
F 5 HOH   203 603 181  HOH   HOH A . 
F 5 HOH   204 604 265  HOH   HOH A . 
F 5 HOH   205 605 192  HOH   HOH A . 
F 5 HOH   206 606 424  HOH   HOH A . 
F 5 HOH   207 607 342  HOH   HOH A . 
F 5 HOH   208 608 308  HOH   HOH A . 
F 5 HOH   209 609 564  HOH   HOH A . 
F 5 HOH   210 610 244  HOH   HOH A . 
F 5 HOH   211 611 451  HOH   HOH A . 
F 5 HOH   212 612 514  HOH   HOH A . 
F 5 HOH   213 613 162  HOH   HOH A . 
F 5 HOH   214 614 172  HOH   HOH A . 
F 5 HOH   215 615 96   HOH   HOH A . 
F 5 HOH   216 616 259  HOH   HOH A . 
F 5 HOH   217 617 56   HOH   HOH A . 
F 5 HOH   218 618 337  HOH   HOH A . 
F 5 HOH   219 619 240  HOH   HOH A . 
F 5 HOH   220 620 65   HOH   HOH A . 
F 5 HOH   221 621 467  HOH   HOH A . 
F 5 HOH   222 622 109  HOH   HOH A . 
F 5 HOH   223 623 365  HOH   HOH A . 
F 5 HOH   224 624 583  HOH   HOH A . 
F 5 HOH   225 625 31   HOH   HOH A . 
F 5 HOH   226 626 140  HOH   HOH A . 
F 5 HOH   227 627 430  HOH   HOH A . 
F 5 HOH   228 628 249  HOH   HOH A . 
F 5 HOH   229 629 261  HOH   HOH A . 
F 5 HOH   230 630 379  HOH   HOH A . 
F 5 HOH   231 631 436  HOH   HOH A . 
F 5 HOH   232 632 142  HOH   HOH A . 
F 5 HOH   233 633 90   HOH   HOH A . 
F 5 HOH   234 634 205  HOH   HOH A . 
F 5 HOH   235 635 380  HOH   HOH A . 
F 5 HOH   236 636 197  HOH   HOH A . 
F 5 HOH   237 637 548  HOH   HOH A . 
F 5 HOH   238 638 416  HOH   HOH A . 
F 5 HOH   239 639 275  HOH   HOH A . 
F 5 HOH   240 640 356  HOH   HOH A . 
F 5 HOH   241 641 554  HOH   HOH A . 
F 5 HOH   242 642 166  HOH   HOH A . 
F 5 HOH   243 643 388  HOH   HOH A . 
F 5 HOH   244 644 301  HOH   HOH A . 
F 5 HOH   245 645 585  HOH   HOH A . 
F 5 HOH   246 646 223  HOH   HOH A . 
F 5 HOH   247 647 404  HOH   HOH A . 
F 5 HOH   248 648 419  HOH   HOH A . 
F 5 HOH   249 649 584  HOH   HOH A . 
F 5 HOH   250 650 198  HOH   HOH A . 
F 5 HOH   251 651 277  HOH   HOH A . 
F 5 HOH   252 652 234  HOH   HOH A . 
F 5 HOH   253 653 188  HOH   HOH A . 
F 5 HOH   254 654 434  HOH   HOH A . 
F 5 HOH   255 655 136  HOH   HOH A . 
F 5 HOH   256 656 443  HOH   HOH A . 
F 5 HOH   257 657 386  HOH   HOH A . 
F 5 HOH   258 658 124  HOH   HOH A . 
F 5 HOH   259 659 235  HOH   HOH A . 
F 5 HOH   260 660 533  HOH   HOH A . 
F 5 HOH   261 661 89   HOH   HOH A . 
F 5 HOH   262 662 121  HOH   HOH A . 
F 5 HOH   263 663 116  HOH   HOH A . 
F 5 HOH   264 664 254  HOH   HOH A . 
F 5 HOH   265 665 481  HOH   HOH A . 
F 5 HOH   266 666 288  HOH   HOH A . 
F 5 HOH   267 667 572  HOH   HOH A . 
F 5 HOH   268 668 518  HOH   HOH A . 
F 5 HOH   269 669 221  HOH   HOH A . 
F 5 HOH   270 670 154  HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC 5.8.0425 ? 1 
'data scaling'   XSCALE .        ? 2 
'data reduction' XDS    .        ? 3 
phasing          PHASER .        ? 4 
# 
_cell.entry_id           7H65 
_cell.length_a           75.440 
_cell.length_b           75.440 
_cell.length_c           49.470 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7H65 
_symmetry.space_group_name_H-M             'P 43' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                78 
# 
_exptl.entry_id          7H65 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.90 
_exptl_crystal.density_percent_sol   57.66 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          MICROBATCH 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    
;Sample of human Chymase in 50 mM MES/NaOH pH 5.5, 150mM NaCl, 1mM TCEP, 10% Glycerol) at a concentration of 11mg/ml to 14mg/ml.Add [2-[(4-methylpyridin-2-yl)amino]-2-oxoethyl] 2-methylquinoline-4-carboxylate at 10x molar ratio. The compound helps to obtain crystals but is not visible in the structures. Add 0.5 mM ZnCl2. Add inhibitor, incubate for 16h on ice. Crystallize using microbatch setups with Al's oil (Hampton Research), with total drop size 1ul with 50% protein sample, using crystallization reagent of 0.1M Tris/HCl pH 8.5, 0.2M NaCl, 25% PEG 3350.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.type                   'MAR scanner 345 mm plate' 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.pdbx_collection_date   2006-07-26 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'BRUKER AXS MICROSTAR' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7H65 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             19.28 
_reflns.d_resolution_high            1.8 
_reflns.number_obs                   25858 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            0.124 
_reflns.pdbx_netI_over_sigmaI        8.78 
_reflns.pdbx_Rrim_I_all              0.142 
_reflns.pdbx_number_measured_all     110378 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
1 1 1.80 1.91  17451 4183 0.572 99.3  2.53  0.655 ? ? ? ? 
1 2 1.91 2.04  16466 3863 0.428 99.5  3.44  0.491 ? ? ? ? 
1 3 2.04 2.2   14746 3551 0.3   99.3  4.56  0.345 ? ? ? ? 
1 4 2.20 2.4   13377 3223 0.198 99.4  6.70  0.228 ? ? ? ? 
1 5 2.40 2.68  13302 3105 0.119 99.9  10.40 0.136 ? ? ? ? 
1 6 2.68 3.09  11985 2728 0.09  99.9  14.11 0.103 ? ? ? ? 
1 7 3.09 3.76  10199 2304 0.075 100.0 17.34 0.085 ? ? ? ? 
1 8 3.76 5.22  8030  1799 0.072 100.0 18.71 0.082 ? ? ? ? 
1 9 5.22 19.28 4822  1102 0.069 97.8  19.05 0.078 ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7H65 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     24541 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.28 
_refine.ls_d_res_high                            1.80 
_refine.ls_percent_reflns_obs                    99.52 
_refine.ls_R_factor_obs                          0.19688 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19562 
_refine.ls_R_factor_R_free                       0.22007 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1316 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.945 
_refine.correlation_coeff_Fo_to_Fc_free          0.926 
_refine.B_iso_mean                               15.932 
_refine.aniso_B[1][1]                            -0.27 
_refine.aniso_B[2][2]                            -0.27 
_refine.aniso_B[3][3]                            0.54 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.128 
_refine.pdbx_overall_ESU_R_Free                  0.117 
_refine.overall_SU_ML                            0.090 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.185 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1702 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             270 
_refine_hist.number_atoms_total               2020 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        19.28 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.006  0.012  ? 1844 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.016  ? 1764 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.344  1.829  ? 2506 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.624  1.791  ? 4059 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.376  5.000  ? 227  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.574  5.000  ? 14   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       10.045 10.000 ? 307  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.065  0.200  ? 269  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 2175 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.003  0.020  ? 436  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.934  1.619  ? 899  'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.934  1.619  ? 899  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.618  2.909  ? 1129 'X-RAY DIFFRACTION' ? 
r_mcangle_other              1.618  2.912  ? 1130 'X-RAY DIFFRACTION' ? 
r_scbond_it                  0.943  1.802  ? 945  'X-RAY DIFFRACTION' ? 
r_scbond_other               0.943  1.805  ? 946  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              1.675  3.265  ? 1376 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       4.528  19.39  ? 1913 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         4.463  19.37  ? 1907 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.846 
_refine_ls_shell.number_reflns_R_work             1813 
_refine_ls_shell.R_factor_R_work                  0.414 
_refine_ls_shell.percent_reflns_obs               99.06 
_refine_ls_shell.R_factor_R_free                  0.428 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             86 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7H65 
_struct.title                     
;THE 1.8 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH N-[1-[2-[[2-hydroxy-3-methyl-3-(4-methylphenyl)-4-oxocyclobuten-1-yl]-phenylmethyl]-6-methyl-1H-indol-3-yl]-2-methylpropan-2-yl]acetamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7H65 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'HUMAN CHYMASE, SERINE PROTEINASE, CHYMASE, HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CMA1_HUMAN 
_struct_ref.pdbx_db_accession          P23946 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_struct_ref.pdbx_align_begin           22 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7H65 
_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                 226 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P23946 
_struct_ref_seq.db_align_beg                  22 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  247 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       16 
_struct_ref_seq.pdbx_auth_seq_align_end       245 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7H65 SER A 7   ? UNP P23946 CYS 28  'engineered mutation' 22  1 
1 7H65 LYS A 114 ? UNP P23946 PHE 135 'engineered mutation' 127 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ALA A 43  ? ALA A 47  ? ALA A 55  ALA A 59  5 ? 5  
HELX_P HELX_P2 AA2 ASP A 150 ? SER A 155 ? ASP A 164 SER A 169 5 ? 6  
HELX_P HELX_P3 AA3 TYR A 215 ? ASN A 226 ? TYR A 234 ASN A 245 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 30  SG  ? ? ? 1_555 A CYS 46  SG ? ? A CYS 42  A CYS 58  1_555 ? ? ? ? ? ? ? 2.066 ? ? 
disulf2 disulf ? ? A CYS 123 SG  ? ? ? 1_555 A CYS 188 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf3 disulf ? ? A CYS 154 SG  ? ? ? 1_555 A CYS 167 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc1 metalc ? ? A HIS 10  NE2 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 25  A ZN  301 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc2 metalc ? ? A GLU 64  OE2 ? ? ? 1_555 B ZN  .   ZN ? ? A GLU 77  A ZN  301 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc3 metalc ? ? A GLU 71  OE2 ? ? ? 1_555 B ZN  .   ZN ? ? A GLU 84  A ZN  301 2_455 ? ? ? ? ? ? ? 2.090 ? ? 
metalc4 metalc ? ? A LYS 96  NZ  A ? ? 1_555 B ZN  .   ZN ? ? A LYS 109 A ZN  301 2_455 ? ? ? ? ? ? ? 2.322 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 10 ? A HIS 25 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OE2 ? A GLU 64 ? A GLU 77  ? 1_555 125.0 ? 
2 NE2 ? A HIS 10 ? A HIS 25 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OE2 ? A GLU 71 ? A GLU 84  ? 1_555 73.0  ? 
3 OE2 ? A GLU 64 ? A GLU 77 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OE2 ? A GLU 71 ? A GLU 84  ? 1_555 52.4  ? 
4 NE2 ? A HIS 10 ? A HIS 25 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NZ  A A LYS 96 ? A LYS 109 ? 1_555 74.2  ? 
5 OE2 ? A GLU 64 ? A GLU 77 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NZ  A A LYS 96 ? A LYS 109 ? 1_555 52.5  ? 
6 OE2 ? A GLU 71 ? A GLU 84 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NZ  A A LYS 96 ? A LYS 109 ? 1_555 7.3   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 30  ? CYS A 46  ? CYS A 42  ? 1_555 CYS A 58  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 123 ? CYS A 188 ? CYS A 136 ? 1_555 CYS A 201 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 154 ? CYS A 167 ? CYS A 168 ? 1_555 CYS A 182 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           205 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            224 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    206 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     225 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.39 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 5   ? GLU A 6   ? THR A 20  GLU A 21  
AA1 2 GLN A 142 ? MET A 149 ? GLN A 156 MET A 163 
AA1 3 GLN A 165 ? VAL A 168 ? GLN A 180 VAL A 183 
AA1 4 ALA A 207 ? ARG A 211 ? ALA A 226 ARG A 230 
AA1 5 VAL A 191 ? TYR A 198 ? VAL A 208 TYR A 215 
AA1 6 PRO A 185 ? CYS A 188 ? PRO A 198 CYS A 201 
AA1 7 MET A 122 ? GLY A 127 ? MET A 135 GLY A 140 
AA1 8 GLN A 142 ? MET A 149 ? GLN A 156 MET A 163 
AA2 1 MET A 15  ? VAL A 21  ? MET A 30  VAL A 36  
AA2 2 LYS A 28  ? ARG A 36  ? LYS A 40  ARG A 48  
AA2 3 PHE A 39  ? THR A 42  ? PHE A 51  THR A 54  
AA2 4 MET A 91  ? LEU A 95  ? MET A 104 LEU A 108 
AA2 5 GLN A 68  ? ARG A 77  ? GLN A 81  ARG A 90  
AA2 6 SER A 50  ? LEU A 55  ? SER A 63  LEU A 68  
AA2 7 MET A 15  ? VAL A 21  ? MET A 30  VAL A 36  
AA3 1 ARG A 130 ? GLY A 132 ? ARG A 143 GLY A 145 
AA3 2 LYS A 135 ? GLY A 137 ? LYS A 148 GLY A 151 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 5   ? N THR A 20  O GLU A 143 ? O GLU A 157 
AA1 2 3 N MET A 149 ? N MET A 163 O CYS A 167 ? O CYS A 182 
AA1 3 4 N VAL A 168 ? N VAL A 183 O ALA A 207 ? O ALA A 226 
AA1 4 5 O VAL A 208 ? O VAL A 227 N TYR A 198 ? N TYR A 215 
AA1 5 6 O GLN A 193 ? O GLN A 210 N LEU A 186 ? N LEU A 199 
AA1 6 7 O LEU A 187 ? O LEU A 200 N ARG A 124 ? N ARG A 137 
AA1 7 8 N CYS A 123 ? N CYS A 136 O LEU A 146 ? O LEU A 160 
AA2 1 2 N ILE A 20  ? N ILE A 35  O LYS A 28  ? O LYS A 40  
AA2 2 3 N PHE A 33  ? N PHE A 45  O LEU A 41  ? O LEU A 53  
AA2 3 4 N VAL A 40  ? N VAL A 52  O LEU A 93  ? O LEU A 106 
AA2 4 5 O LEU A 92  ? O LEU A 105 N PHE A 76  ? N PHE A 89  
AA2 5 6 O LEU A 70  ? O LEU A 83  N VAL A 53  ? N VAL A 66  
AA2 6 7 O SER A 50  ? O SER A 63  N VAL A 21  ? N VAL A 36  
AA3 1 2 N GLY A 132 ? N GLY A 145 O LYS A 135 ? O LYS A 148 
# 
_pdbx_entry_details.entry_id                   7H65 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  A LYS 148 ? ? N A PRO 150 ? ? CD A PRO 150 ? ? 100.64 128.40 -27.76 2.10 Y 
2 1 CA A PRO 150 ? ? N A PRO 150 ? ? CD A PRO 150 ? ? 98.69  111.70 -13.01 1.40 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 71  ? ? -124.91 -74.44 
2 1 PRO A 150 ? ? -40.38  165.19 
3 1 SER A 214 ? ? -116.59 -79.40 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       670 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.91 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 125 ? A SER 112 
2 1 Y 1 A GLN 126 ? A GLN 113 
3 1 Y 1 A LYS 127 ? A LYS 114 
4 1 Y 1 A ASN 128 ? A ASN 115 
5 1 Y 1 A PHE 129 ? A PHE 116 
6 1 Y 1 A VAL 130 ? A VAL 117 
7 1 Y 1 A PRO 131 ? A PRO 118 
# 
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 
A1AO1 C4   C  N S 1   
A1AO1 C5   C  N N 2   
A1AO1 C6   C  Y N 3   
A1AO1 C8   C  N R 4   
A1AO1 C10  C  Y N 5   
A1AO1 C13  C  Y N 6   
A1AO1 C17  C  N N 7   
A1AO1 C22  C  Y N 8   
A1AO1 C24  C  N N 9   
A1AO1 C26  C  Y N 10  
A1AO1 C28  C  Y N 11  
A1AO1 C1   C  N N 12  
A1AO1 C2   C  Y N 13  
A1AO1 C3   C  N N 14  
A1AO1 N7   N  Y N 15  
A1AO1 C9   C  Y N 16  
A1AO1 C11  C  N N 17  
A1AO1 C12  C  Y N 18  
A1AO1 C14  C  N N 19  
A1AO1 N15  N  N N 20  
A1AO1 O16  O  N N 21  
A1AO1 C18  C  Y N 22  
A1AO1 C19  C  Y N 23  
A1AO1 O20  O  N N 24  
A1AO1 O21  O  N N 25  
A1AO1 C23  C  Y N 26  
A1AO1 C25  C  Y N 27  
A1AO1 C27  C  Y N 28  
A1AO1 C29  C  Y N 29  
A1AO1 C30  C  N N 30  
A1AO1 C31  C  N N 31  
A1AO1 C32  C  N N 32  
A1AO1 C33  C  Y N 33  
A1AO1 C34  C  Y N 34  
A1AO1 C35  C  N N 35  
A1AO1 C36  C  N N 36  
A1AO1 C37  C  Y N 37  
A1AO1 C38  C  Y N 38  
A1AO1 C39  C  Y N 39  
A1AO1 H41  H  N N 40  
A1AO1 H44  H  N N 41  
A1AO1 H48  H  N N 42  
A1AO1 H52  H  N N 43  
A1AO1 H50  H  N N 44  
A1AO1 H51  H  N N 45  
A1AO1 H55  H  N N 46  
A1AO1 H40  H  N N 47  
A1AO1 H43  H  N N 48  
A1AO1 H42  H  N N 49  
A1AO1 H45  H  N N 50  
A1AO1 H46  H  N N 51  
A1AO1 H47  H  N N 52  
A1AO1 H49  H  N N 53  
A1AO1 H53  H  N N 54  
A1AO1 H54  H  N N 55  
A1AO1 H56  H  N N 56  
A1AO1 H57  H  N N 57  
A1AO1 H58  H  N N 58  
A1AO1 H61  H  N N 59  
A1AO1 H60  H  N N 60  
A1AO1 H59  H  N N 61  
A1AO1 H62  H  N N 62  
A1AO1 H63  H  N N 63  
A1AO1 H64  H  N N 64  
A1AO1 H65  H  N N 65  
A1AO1 H66  H  N N 66  
A1AO1 H67  H  N N 67  
A1AO1 H68  H  N N 68  
A1AO1 H69  H  N N 69  
A1AO1 H71  H  N N 70  
A1AO1 H70  H  N N 71  
A1AO1 H72  H  N N 72  
A1AO1 H73  H  N N 73  
A1AO1 H74  H  N N 74  
A1AO1 H75  H  N N 75  
ALA   N    N  N N 76  
ALA   CA   C  N S 77  
ALA   C    C  N N 78  
ALA   O    O  N N 79  
ALA   CB   C  N N 80  
ALA   OXT  O  N N 81  
ALA   H    H  N N 82  
ALA   H2   H  N N 83  
ALA   HA   H  N N 84  
ALA   HB1  H  N N 85  
ALA   HB2  H  N N 86  
ALA   HB3  H  N N 87  
ALA   HXT  H  N N 88  
ARG   N    N  N N 89  
ARG   CA   C  N S 90  
ARG   C    C  N N 91  
ARG   O    O  N N 92  
ARG   CB   C  N N 93  
ARG   CG   C  N N 94  
ARG   CD   C  N N 95  
ARG   NE   N  N N 96  
ARG   CZ   C  N N 97  
ARG   NH1  N  N N 98  
ARG   NH2  N  N N 99  
ARG   OXT  O  N N 100 
ARG   H    H  N N 101 
ARG   H2   H  N N 102 
ARG   HA   H  N N 103 
ARG   HB2  H  N N 104 
ARG   HB3  H  N N 105 
ARG   HG2  H  N N 106 
ARG   HG3  H  N N 107 
ARG   HD2  H  N N 108 
ARG   HD3  H  N N 109 
ARG   HE   H  N N 110 
ARG   HH11 H  N N 111 
ARG   HH12 H  N N 112 
ARG   HH21 H  N N 113 
ARG   HH22 H  N N 114 
ARG   HXT  H  N N 115 
ASN   N    N  N N 116 
ASN   CA   C  N S 117 
ASN   C    C  N N 118 
ASN   O    O  N N 119 
ASN   CB   C  N N 120 
ASN   CG   C  N N 121 
ASN   OD1  O  N N 122 
ASN   ND2  N  N N 123 
ASN   OXT  O  N N 124 
ASN   H    H  N N 125 
ASN   H2   H  N N 126 
ASN   HA   H  N N 127 
ASN   HB2  H  N N 128 
ASN   HB3  H  N N 129 
ASN   HD21 H  N N 130 
ASN   HD22 H  N N 131 
ASN   HXT  H  N N 132 
ASP   N    N  N N 133 
ASP   CA   C  N S 134 
ASP   C    C  N N 135 
ASP   O    O  N N 136 
ASP   CB   C  N N 137 
ASP   CG   C  N N 138 
ASP   OD1  O  N N 139 
ASP   OD2  O  N N 140 
ASP   OXT  O  N N 141 
ASP   H    H  N N 142 
ASP   H2   H  N N 143 
ASP   HA   H  N N 144 
ASP   HB2  H  N N 145 
ASP   HB3  H  N N 146 
ASP   HD2  H  N N 147 
ASP   HXT  H  N N 148 
CYS   N    N  N N 149 
CYS   CA   C  N R 150 
CYS   C    C  N N 151 
CYS   O    O  N N 152 
CYS   CB   C  N N 153 
CYS   SG   S  N N 154 
CYS   OXT  O  N N 155 
CYS   H    H  N N 156 
CYS   H2   H  N N 157 
CYS   HA   H  N N 158 
CYS   HB2  H  N N 159 
CYS   HB3  H  N N 160 
CYS   HG   H  N N 161 
CYS   HXT  H  N N 162 
DMS   S    S  N N 163 
DMS   O    O  N N 164 
DMS   C1   C  N N 165 
DMS   C2   C  N N 166 
DMS   H11  H  N N 167 
DMS   H12  H  N N 168 
DMS   H13  H  N N 169 
DMS   H21  H  N N 170 
DMS   H22  H  N N 171 
DMS   H23  H  N N 172 
GLN   N    N  N N 173 
GLN   CA   C  N S 174 
GLN   C    C  N N 175 
GLN   O    O  N N 176 
GLN   CB   C  N N 177 
GLN   CG   C  N N 178 
GLN   CD   C  N N 179 
GLN   OE1  O  N N 180 
GLN   NE2  N  N N 181 
GLN   OXT  O  N N 182 
GLN   H    H  N N 183 
GLN   H2   H  N N 184 
GLN   HA   H  N N 185 
GLN   HB2  H  N N 186 
GLN   HB3  H  N N 187 
GLN   HG2  H  N N 188 
GLN   HG3  H  N N 189 
GLN   HE21 H  N N 190 
GLN   HE22 H  N N 191 
GLN   HXT  H  N N 192 
GLU   N    N  N N 193 
GLU   CA   C  N S 194 
GLU   C    C  N N 195 
GLU   O    O  N N 196 
GLU   CB   C  N N 197 
GLU   CG   C  N N 198 
GLU   CD   C  N N 199 
GLU   OE1  O  N N 200 
GLU   OE2  O  N N 201 
GLU   OXT  O  N N 202 
GLU   H    H  N N 203 
GLU   H2   H  N N 204 
GLU   HA   H  N N 205 
GLU   HB2  H  N N 206 
GLU   HB3  H  N N 207 
GLU   HG2  H  N N 208 
GLU   HG3  H  N N 209 
GLU   HE2  H  N N 210 
GLU   HXT  H  N N 211 
GLY   N    N  N N 212 
GLY   CA   C  N N 213 
GLY   C    C  N N 214 
GLY   O    O  N N 215 
GLY   OXT  O  N N 216 
GLY   H    H  N N 217 
GLY   H2   H  N N 218 
GLY   HA2  H  N N 219 
GLY   HA3  H  N N 220 
GLY   HXT  H  N N 221 
HIS   N    N  N N 222 
HIS   CA   C  N S 223 
HIS   C    C  N N 224 
HIS   O    O  N N 225 
HIS   CB   C  N N 226 
HIS   CG   C  Y N 227 
HIS   ND1  N  Y N 228 
HIS   CD2  C  Y N 229 
HIS   CE1  C  Y N 230 
HIS   NE2  N  Y N 231 
HIS   OXT  O  N N 232 
HIS   H    H  N N 233 
HIS   H2   H  N N 234 
HIS   HA   H  N N 235 
HIS   HB2  H  N N 236 
HIS   HB3  H  N N 237 
HIS   HD1  H  N N 238 
HIS   HD2  H  N N 239 
HIS   HE1  H  N N 240 
HIS   HE2  H  N N 241 
HIS   HXT  H  N N 242 
HOH   O    O  N N 243 
HOH   H1   H  N N 244 
HOH   H2   H  N N 245 
ILE   N    N  N N 246 
ILE   CA   C  N S 247 
ILE   C    C  N N 248 
ILE   O    O  N N 249 
ILE   CB   C  N S 250 
ILE   CG1  C  N N 251 
ILE   CG2  C  N N 252 
ILE   CD1  C  N N 253 
ILE   OXT  O  N N 254 
ILE   H    H  N N 255 
ILE   H2   H  N N 256 
ILE   HA   H  N N 257 
ILE   HB   H  N N 258 
ILE   HG12 H  N N 259 
ILE   HG13 H  N N 260 
ILE   HG21 H  N N 261 
ILE   HG22 H  N N 262 
ILE   HG23 H  N N 263 
ILE   HD11 H  N N 264 
ILE   HD12 H  N N 265 
ILE   HD13 H  N N 266 
ILE   HXT  H  N N 267 
LEU   N    N  N N 268 
LEU   CA   C  N S 269 
LEU   C    C  N N 270 
LEU   O    O  N N 271 
LEU   CB   C  N N 272 
LEU   CG   C  N N 273 
LEU   CD1  C  N N 274 
LEU   CD2  C  N N 275 
LEU   OXT  O  N N 276 
LEU   H    H  N N 277 
LEU   H2   H  N N 278 
LEU   HA   H  N N 279 
LEU   HB2  H  N N 280 
LEU   HB3  H  N N 281 
LEU   HG   H  N N 282 
LEU   HD11 H  N N 283 
LEU   HD12 H  N N 284 
LEU   HD13 H  N N 285 
LEU   HD21 H  N N 286 
LEU   HD22 H  N N 287 
LEU   HD23 H  N N 288 
LEU   HXT  H  N N 289 
LYS   N    N  N N 290 
LYS   CA   C  N S 291 
LYS   C    C  N N 292 
LYS   O    O  N N 293 
LYS   CB   C  N N 294 
LYS   CG   C  N N 295 
LYS   CD   C  N N 296 
LYS   CE   C  N N 297 
LYS   NZ   N  N N 298 
LYS   OXT  O  N N 299 
LYS   H    H  N N 300 
LYS   H2   H  N N 301 
LYS   HA   H  N N 302 
LYS   HB2  H  N N 303 
LYS   HB3  H  N N 304 
LYS   HG2  H  N N 305 
LYS   HG3  H  N N 306 
LYS   HD2  H  N N 307 
LYS   HD3  H  N N 308 
LYS   HE2  H  N N 309 
LYS   HE3  H  N N 310 
LYS   HZ1  H  N N 311 
LYS   HZ2  H  N N 312 
LYS   HZ3  H  N N 313 
LYS   HXT  H  N N 314 
MET   N    N  N N 315 
MET   CA   C  N S 316 
MET   C    C  N N 317 
MET   O    O  N N 318 
MET   CB   C  N N 319 
MET   CG   C  N N 320 
MET   SD   S  N N 321 
MET   CE   C  N N 322 
MET   OXT  O  N N 323 
MET   H    H  N N 324 
MET   H2   H  N N 325 
MET   HA   H  N N 326 
MET   HB2  H  N N 327 
MET   HB3  H  N N 328 
MET   HG2  H  N N 329 
MET   HG3  H  N N 330 
MET   HE1  H  N N 331 
MET   HE2  H  N N 332 
MET   HE3  H  N N 333 
MET   HXT  H  N N 334 
PHE   N    N  N N 335 
PHE   CA   C  N S 336 
PHE   C    C  N N 337 
PHE   O    O  N N 338 
PHE   CB   C  N N 339 
PHE   CG   C  Y N 340 
PHE   CD1  C  Y N 341 
PHE   CD2  C  Y N 342 
PHE   CE1  C  Y N 343 
PHE   CE2  C  Y N 344 
PHE   CZ   C  Y N 345 
PHE   OXT  O  N N 346 
PHE   H    H  N N 347 
PHE   H2   H  N N 348 
PHE   HA   H  N N 349 
PHE   HB2  H  N N 350 
PHE   HB3  H  N N 351 
PHE   HD1  H  N N 352 
PHE   HD2  H  N N 353 
PHE   HE1  H  N N 354 
PHE   HE2  H  N N 355 
PHE   HZ   H  N N 356 
PHE   HXT  H  N N 357 
PRO   N    N  N N 358 
PRO   CA   C  N S 359 
PRO   C    C  N N 360 
PRO   O    O  N N 361 
PRO   CB   C  N N 362 
PRO   CG   C  N N 363 
PRO   CD   C  N N 364 
PRO   OXT  O  N N 365 
PRO   H    H  N N 366 
PRO   HA   H  N N 367 
PRO   HB2  H  N N 368 
PRO   HB3  H  N N 369 
PRO   HG2  H  N N 370 
PRO   HG3  H  N N 371 
PRO   HD2  H  N N 372 
PRO   HD3  H  N N 373 
PRO   HXT  H  N N 374 
SER   N    N  N N 375 
SER   CA   C  N S 376 
SER   C    C  N N 377 
SER   O    O  N N 378 
SER   CB   C  N N 379 
SER   OG   O  N N 380 
SER   OXT  O  N N 381 
SER   H    H  N N 382 
SER   H2   H  N N 383 
SER   HA   H  N N 384 
SER   HB2  H  N N 385 
SER   HB3  H  N N 386 
SER   HG   H  N N 387 
SER   HXT  H  N N 388 
THR   N    N  N N 389 
THR   CA   C  N S 390 
THR   C    C  N N 391 
THR   O    O  N N 392 
THR   CB   C  N R 393 
THR   OG1  O  N N 394 
THR   CG2  C  N N 395 
THR   OXT  O  N N 396 
THR   H    H  N N 397 
THR   H2   H  N N 398 
THR   HA   H  N N 399 
THR   HB   H  N N 400 
THR   HG1  H  N N 401 
THR   HG21 H  N N 402 
THR   HG22 H  N N 403 
THR   HG23 H  N N 404 
THR   HXT  H  N N 405 
TRP   N    N  N N 406 
TRP   CA   C  N S 407 
TRP   C    C  N N 408 
TRP   O    O  N N 409 
TRP   CB   C  N N 410 
TRP   CG   C  Y N 411 
TRP   CD1  C  Y N 412 
TRP   CD2  C  Y N 413 
TRP   NE1  N  Y N 414 
TRP   CE2  C  Y N 415 
TRP   CE3  C  Y N 416 
TRP   CZ2  C  Y N 417 
TRP   CZ3  C  Y N 418 
TRP   CH2  C  Y N 419 
TRP   OXT  O  N N 420 
TRP   H    H  N N 421 
TRP   H2   H  N N 422 
TRP   HA   H  N N 423 
TRP   HB2  H  N N 424 
TRP   HB3  H  N N 425 
TRP   HD1  H  N N 426 
TRP   HE1  H  N N 427 
TRP   HE3  H  N N 428 
TRP   HZ2  H  N N 429 
TRP   HZ3  H  N N 430 
TRP   HH2  H  N N 431 
TRP   HXT  H  N N 432 
TYR   N    N  N N 433 
TYR   CA   C  N S 434 
TYR   C    C  N N 435 
TYR   O    O  N N 436 
TYR   CB   C  N N 437 
TYR   CG   C  Y N 438 
TYR   CD1  C  Y N 439 
TYR   CD2  C  Y N 440 
TYR   CE1  C  Y N 441 
TYR   CE2  C  Y N 442 
TYR   CZ   C  Y N 443 
TYR   OH   O  N N 444 
TYR   OXT  O  N N 445 
TYR   H    H  N N 446 
TYR   H2   H  N N 447 
TYR   HA   H  N N 448 
TYR   HB2  H  N N 449 
TYR   HB3  H  N N 450 
TYR   HD1  H  N N 451 
TYR   HD2  H  N N 452 
TYR   HE1  H  N N 453 
TYR   HE2  H  N N 454 
TYR   HH   H  N N 455 
TYR   HXT  H  N N 456 
VAL   N    N  N N 457 
VAL   CA   C  N S 458 
VAL   C    C  N N 459 
VAL   O    O  N N 460 
VAL   CB   C  N N 461 
VAL   CG1  C  N N 462 
VAL   CG2  C  N N 463 
VAL   OXT  O  N N 464 
VAL   H    H  N N 465 
VAL   H2   H  N N 466 
VAL   HA   H  N N 467 
VAL   HB   H  N N 468 
VAL   HG11 H  N N 469 
VAL   HG12 H  N N 470 
VAL   HG13 H  N N 471 
VAL   HG21 H  N N 472 
VAL   HG22 H  N N 473 
VAL   HG23 H  N N 474 
VAL   HXT  H  N N 475 
ZN    ZN   ZN N N 476 
# 
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 
A1AO1 C1  C3   doub N N 1   
A1AO1 C1  C5   sing N N 2   
A1AO1 C1  C8   sing N N 3   
A1AO1 C2  N7   sing Y N 4   
A1AO1 C2  C6   doub Y N 5   
A1AO1 C2  C8   sing N N 6   
A1AO1 C3  C4   sing N N 7   
A1AO1 C3  O20  sing N N 8   
A1AO1 C4  C24  sing N N 9   
A1AO1 C4  C12  sing N N 10  
A1AO1 C4  C5   sing N N 11  
A1AO1 C5  O16  doub N N 12  
A1AO1 C6  C10  sing Y N 13  
A1AO1 C6  C11  sing N N 14  
A1AO1 N7  C9   sing Y N 15  
A1AO1 C8  C19  sing N N 16  
A1AO1 C9  C10  doub Y N 17  
A1AO1 C9  C18  sing Y N 18  
A1AO1 C10 C13  sing Y N 19  
A1AO1 C11 C14  sing N N 20  
A1AO1 C12 C22  doub Y N 21  
A1AO1 C12 C23  sing Y N 22  
A1AO1 C13 C25  doub Y N 23  
A1AO1 C14 N15  sing N N 24  
A1AO1 C14 C30  sing N N 25  
A1AO1 C14 C31  sing N N 26  
A1AO1 N15 C17  sing N N 27  
A1AO1 C17 O21  doub N N 28  
A1AO1 C17 C32  sing N N 29  
A1AO1 C18 C26  doub Y N 30  
A1AO1 C19 C34  doub Y N 31  
A1AO1 C19 C33  sing Y N 32  
A1AO1 C22 C27  sing Y N 33  
A1AO1 C23 C28  doub Y N 34  
A1AO1 C25 C26  sing Y N 35  
A1AO1 C26 C35  sing N N 36  
A1AO1 C27 C29  doub Y N 37  
A1AO1 C28 C29  sing Y N 38  
A1AO1 C29 C36  sing N N 39  
A1AO1 C33 C37  doub Y N 40  
A1AO1 C34 C38  sing Y N 41  
A1AO1 C37 C39  sing Y N 42  
A1AO1 C38 C39  doub Y N 43  
A1AO1 C8  H41  sing N N 44  
A1AO1 C13 H44  sing N N 45  
A1AO1 C22 H48  sing N N 46  
A1AO1 C24 H52  sing N N 47  
A1AO1 C24 H50  sing N N 48  
A1AO1 C24 H51  sing N N 49  
A1AO1 C28 H55  sing N N 50  
A1AO1 N7  H40  sing N N 51  
A1AO1 C11 H43  sing N N 52  
A1AO1 C11 H42  sing N N 53  
A1AO1 N15 H45  sing N N 54  
A1AO1 C18 H46  sing N N 55  
A1AO1 O20 H47  sing N N 56  
A1AO1 C23 H49  sing N N 57  
A1AO1 C25 H53  sing N N 58  
A1AO1 C27 H54  sing N N 59  
A1AO1 C30 H56  sing N N 60  
A1AO1 C30 H57  sing N N 61  
A1AO1 C30 H58  sing N N 62  
A1AO1 C31 H61  sing N N 63  
A1AO1 C31 H60  sing N N 64  
A1AO1 C31 H59  sing N N 65  
A1AO1 C32 H62  sing N N 66  
A1AO1 C32 H63  sing N N 67  
A1AO1 C32 H64  sing N N 68  
A1AO1 C33 H65  sing N N 69  
A1AO1 C34 H66  sing N N 70  
A1AO1 C35 H67  sing N N 71  
A1AO1 C35 H68  sing N N 72  
A1AO1 C35 H69  sing N N 73  
A1AO1 C36 H71  sing N N 74  
A1AO1 C36 H70  sing N N 75  
A1AO1 C36 H72  sing N N 76  
A1AO1 C37 H73  sing N N 77  
A1AO1 C38 H74  sing N N 78  
A1AO1 C39 H75  sing N N 79  
ALA   N   CA   sing N N 80  
ALA   N   H    sing N N 81  
ALA   N   H2   sing N N 82  
ALA   CA  C    sing N N 83  
ALA   CA  CB   sing N N 84  
ALA   CA  HA   sing N N 85  
ALA   C   O    doub N N 86  
ALA   C   OXT  sing N N 87  
ALA   CB  HB1  sing N N 88  
ALA   CB  HB2  sing N N 89  
ALA   CB  HB3  sing N N 90  
ALA   OXT HXT  sing N N 91  
ARG   N   CA   sing N N 92  
ARG   N   H    sing N N 93  
ARG   N   H2   sing N N 94  
ARG   CA  C    sing N N 95  
ARG   CA  CB   sing N N 96  
ARG   CA  HA   sing N N 97  
ARG   C   O    doub N N 98  
ARG   C   OXT  sing N N 99  
ARG   CB  CG   sing N N 100 
ARG   CB  HB2  sing N N 101 
ARG   CB  HB3  sing N N 102 
ARG   CG  CD   sing N N 103 
ARG   CG  HG2  sing N N 104 
ARG   CG  HG3  sing N N 105 
ARG   CD  NE   sing N N 106 
ARG   CD  HD2  sing N N 107 
ARG   CD  HD3  sing N N 108 
ARG   NE  CZ   sing N N 109 
ARG   NE  HE   sing N N 110 
ARG   CZ  NH1  sing N N 111 
ARG   CZ  NH2  doub N N 112 
ARG   NH1 HH11 sing N N 113 
ARG   NH1 HH12 sing N N 114 
ARG   NH2 HH21 sing N N 115 
ARG   NH2 HH22 sing N N 116 
ARG   OXT HXT  sing N N 117 
ASN   N   CA   sing N N 118 
ASN   N   H    sing N N 119 
ASN   N   H2   sing N N 120 
ASN   CA  C    sing N N 121 
ASN   CA  CB   sing N N 122 
ASN   CA  HA   sing N N 123 
ASN   C   O    doub N N 124 
ASN   C   OXT  sing N N 125 
ASN   CB  CG   sing N N 126 
ASN   CB  HB2  sing N N 127 
ASN   CB  HB3  sing N N 128 
ASN   CG  OD1  doub N N 129 
ASN   CG  ND2  sing N N 130 
ASN   ND2 HD21 sing N N 131 
ASN   ND2 HD22 sing N N 132 
ASN   OXT HXT  sing N N 133 
ASP   N   CA   sing N N 134 
ASP   N   H    sing N N 135 
ASP   N   H2   sing N N 136 
ASP   CA  C    sing N N 137 
ASP   CA  CB   sing N N 138 
ASP   CA  HA   sing N N 139 
ASP   C   O    doub N N 140 
ASP   C   OXT  sing N N 141 
ASP   CB  CG   sing N N 142 
ASP   CB  HB2  sing N N 143 
ASP   CB  HB3  sing N N 144 
ASP   CG  OD1  doub N N 145 
ASP   CG  OD2  sing N N 146 
ASP   OD2 HD2  sing N N 147 
ASP   OXT HXT  sing N N 148 
CYS   N   CA   sing N N 149 
CYS   N   H    sing N N 150 
CYS   N   H2   sing N N 151 
CYS   CA  C    sing N N 152 
CYS   CA  CB   sing N N 153 
CYS   CA  HA   sing N N 154 
CYS   C   O    doub N N 155 
CYS   C   OXT  sing N N 156 
CYS   CB  SG   sing N N 157 
CYS   CB  HB2  sing N N 158 
CYS   CB  HB3  sing N N 159 
CYS   SG  HG   sing N N 160 
CYS   OXT HXT  sing N N 161 
DMS   S   O    doub N N 162 
DMS   S   C1   sing N N 163 
DMS   S   C2   sing N N 164 
DMS   C1  H11  sing N N 165 
DMS   C1  H12  sing N N 166 
DMS   C1  H13  sing N N 167 
DMS   C2  H21  sing N N 168 
DMS   C2  H22  sing N N 169 
DMS   C2  H23  sing N N 170 
GLN   N   CA   sing N N 171 
GLN   N   H    sing N N 172 
GLN   N   H2   sing N N 173 
GLN   CA  C    sing N N 174 
GLN   CA  CB   sing N N 175 
GLN   CA  HA   sing N N 176 
GLN   C   O    doub N N 177 
GLN   C   OXT  sing N N 178 
GLN   CB  CG   sing N N 179 
GLN   CB  HB2  sing N N 180 
GLN   CB  HB3  sing N N 181 
GLN   CG  CD   sing N N 182 
GLN   CG  HG2  sing N N 183 
GLN   CG  HG3  sing N N 184 
GLN   CD  OE1  doub N N 185 
GLN   CD  NE2  sing N N 186 
GLN   NE2 HE21 sing N N 187 
GLN   NE2 HE22 sing N N 188 
GLN   OXT HXT  sing N N 189 
GLU   N   CA   sing N N 190 
GLU   N   H    sing N N 191 
GLU   N   H2   sing N N 192 
GLU   CA  C    sing N N 193 
GLU   CA  CB   sing N N 194 
GLU   CA  HA   sing N N 195 
GLU   C   O    doub N N 196 
GLU   C   OXT  sing N N 197 
GLU   CB  CG   sing N N 198 
GLU   CB  HB2  sing N N 199 
GLU   CB  HB3  sing N N 200 
GLU   CG  CD   sing N N 201 
GLU   CG  HG2  sing N N 202 
GLU   CG  HG3  sing N N 203 
GLU   CD  OE1  doub N N 204 
GLU   CD  OE2  sing N N 205 
GLU   OE2 HE2  sing N N 206 
GLU   OXT HXT  sing N N 207 
GLY   N   CA   sing N N 208 
GLY   N   H    sing N N 209 
GLY   N   H2   sing N N 210 
GLY   CA  C    sing N N 211 
GLY   CA  HA2  sing N N 212 
GLY   CA  HA3  sing N N 213 
GLY   C   O    doub N N 214 
GLY   C   OXT  sing N N 215 
GLY   OXT HXT  sing N N 216 
HIS   N   CA   sing N N 217 
HIS   N   H    sing N N 218 
HIS   N   H2   sing N N 219 
HIS   CA  C    sing N N 220 
HIS   CA  CB   sing N N 221 
HIS   CA  HA   sing N N 222 
HIS   C   O    doub N N 223 
HIS   C   OXT  sing N N 224 
HIS   CB  CG   sing N N 225 
HIS   CB  HB2  sing N N 226 
HIS   CB  HB3  sing N N 227 
HIS   CG  ND1  sing Y N 228 
HIS   CG  CD2  doub Y N 229 
HIS   ND1 CE1  doub Y N 230 
HIS   ND1 HD1  sing N N 231 
HIS   CD2 NE2  sing Y N 232 
HIS   CD2 HD2  sing N N 233 
HIS   CE1 NE2  sing Y N 234 
HIS   CE1 HE1  sing N N 235 
HIS   NE2 HE2  sing N N 236 
HIS   OXT HXT  sing N N 237 
HOH   O   H1   sing N N 238 
HOH   O   H2   sing N N 239 
ILE   N   CA   sing N N 240 
ILE   N   H    sing N N 241 
ILE   N   H2   sing N N 242 
ILE   CA  C    sing N N 243 
ILE   CA  CB   sing N N 244 
ILE   CA  HA   sing N N 245 
ILE   C   O    doub N N 246 
ILE   C   OXT  sing N N 247 
ILE   CB  CG1  sing N N 248 
ILE   CB  CG2  sing N N 249 
ILE   CB  HB   sing N N 250 
ILE   CG1 CD1  sing N N 251 
ILE   CG1 HG12 sing N N 252 
ILE   CG1 HG13 sing N N 253 
ILE   CG2 HG21 sing N N 254 
ILE   CG2 HG22 sing N N 255 
ILE   CG2 HG23 sing N N 256 
ILE   CD1 HD11 sing N N 257 
ILE   CD1 HD12 sing N N 258 
ILE   CD1 HD13 sing N N 259 
ILE   OXT HXT  sing N N 260 
LEU   N   CA   sing N N 261 
LEU   N   H    sing N N 262 
LEU   N   H2   sing N N 263 
LEU   CA  C    sing N N 264 
LEU   CA  CB   sing N N 265 
LEU   CA  HA   sing N N 266 
LEU   C   O    doub N N 267 
LEU   C   OXT  sing N N 268 
LEU   CB  CG   sing N N 269 
LEU   CB  HB2  sing N N 270 
LEU   CB  HB3  sing N N 271 
LEU   CG  CD1  sing N N 272 
LEU   CG  CD2  sing N N 273 
LEU   CG  HG   sing N N 274 
LEU   CD1 HD11 sing N N 275 
LEU   CD1 HD12 sing N N 276 
LEU   CD1 HD13 sing N N 277 
LEU   CD2 HD21 sing N N 278 
LEU   CD2 HD22 sing N N 279 
LEU   CD2 HD23 sing N N 280 
LEU   OXT HXT  sing N N 281 
LYS   N   CA   sing N N 282 
LYS   N   H    sing N N 283 
LYS   N   H2   sing N N 284 
LYS   CA  C    sing N N 285 
LYS   CA  CB   sing N N 286 
LYS   CA  HA   sing N N 287 
LYS   C   O    doub N N 288 
LYS   C   OXT  sing N N 289 
LYS   CB  CG   sing N N 290 
LYS   CB  HB2  sing N N 291 
LYS   CB  HB3  sing N N 292 
LYS   CG  CD   sing N N 293 
LYS   CG  HG2  sing N N 294 
LYS   CG  HG3  sing N N 295 
LYS   CD  CE   sing N N 296 
LYS   CD  HD2  sing N N 297 
LYS   CD  HD3  sing N N 298 
LYS   CE  NZ   sing N N 299 
LYS   CE  HE2  sing N N 300 
LYS   CE  HE3  sing N N 301 
LYS   NZ  HZ1  sing N N 302 
LYS   NZ  HZ2  sing N N 303 
LYS   NZ  HZ3  sing N N 304 
LYS   OXT HXT  sing N N 305 
MET   N   CA   sing N N 306 
MET   N   H    sing N N 307 
MET   N   H2   sing N N 308 
MET   CA  C    sing N N 309 
MET   CA  CB   sing N N 310 
MET   CA  HA   sing N N 311 
MET   C   O    doub N N 312 
MET   C   OXT  sing N N 313 
MET   CB  CG   sing N N 314 
MET   CB  HB2  sing N N 315 
MET   CB  HB3  sing N N 316 
MET   CG  SD   sing N N 317 
MET   CG  HG2  sing N N 318 
MET   CG  HG3  sing N N 319 
MET   SD  CE   sing N N 320 
MET   CE  HE1  sing N N 321 
MET   CE  HE2  sing N N 322 
MET   CE  HE3  sing N N 323 
MET   OXT HXT  sing N N 324 
PHE   N   CA   sing N N 325 
PHE   N   H    sing N N 326 
PHE   N   H2   sing N N 327 
PHE   CA  C    sing N N 328 
PHE   CA  CB   sing N N 329 
PHE   CA  HA   sing N N 330 
PHE   C   O    doub N N 331 
PHE   C   OXT  sing N N 332 
PHE   CB  CG   sing N N 333 
PHE   CB  HB2  sing N N 334 
PHE   CB  HB3  sing N N 335 
PHE   CG  CD1  doub Y N 336 
PHE   CG  CD2  sing Y N 337 
PHE   CD1 CE1  sing Y N 338 
PHE   CD1 HD1  sing N N 339 
PHE   CD2 CE2  doub Y N 340 
PHE   CD2 HD2  sing N N 341 
PHE   CE1 CZ   doub Y N 342 
PHE   CE1 HE1  sing N N 343 
PHE   CE2 CZ   sing Y N 344 
PHE   CE2 HE2  sing N N 345 
PHE   CZ  HZ   sing N N 346 
PHE   OXT HXT  sing N N 347 
PRO   N   CA   sing N N 348 
PRO   N   CD   sing N N 349 
PRO   N   H    sing N N 350 
PRO   CA  C    sing N N 351 
PRO   CA  CB   sing N N 352 
PRO   CA  HA   sing N N 353 
PRO   C   O    doub N N 354 
PRO   C   OXT  sing N N 355 
PRO   CB  CG   sing N N 356 
PRO   CB  HB2  sing N N 357 
PRO   CB  HB3  sing N N 358 
PRO   CG  CD   sing N N 359 
PRO   CG  HG2  sing N N 360 
PRO   CG  HG3  sing N N 361 
PRO   CD  HD2  sing N N 362 
PRO   CD  HD3  sing N N 363 
PRO   OXT HXT  sing N N 364 
SER   N   CA   sing N N 365 
SER   N   H    sing N N 366 
SER   N   H2   sing N N 367 
SER   CA  C    sing N N 368 
SER   CA  CB   sing N N 369 
SER   CA  HA   sing N N 370 
SER   C   O    doub N N 371 
SER   C   OXT  sing N N 372 
SER   CB  OG   sing N N 373 
SER   CB  HB2  sing N N 374 
SER   CB  HB3  sing N N 375 
SER   OG  HG   sing N N 376 
SER   OXT HXT  sing N N 377 
THR   N   CA   sing N N 378 
THR   N   H    sing N N 379 
THR   N   H2   sing N N 380 
THR   CA  C    sing N N 381 
THR   CA  CB   sing N N 382 
THR   CA  HA   sing N N 383 
THR   C   O    doub N N 384 
THR   C   OXT  sing N N 385 
THR   CB  OG1  sing N N 386 
THR   CB  CG2  sing N N 387 
THR   CB  HB   sing N N 388 
THR   OG1 HG1  sing N N 389 
THR   CG2 HG21 sing N N 390 
THR   CG2 HG22 sing N N 391 
THR   CG2 HG23 sing N N 392 
THR   OXT HXT  sing N N 393 
TRP   N   CA   sing N N 394 
TRP   N   H    sing N N 395 
TRP   N   H2   sing N N 396 
TRP   CA  C    sing N N 397 
TRP   CA  CB   sing N N 398 
TRP   CA  HA   sing N N 399 
TRP   C   O    doub N N 400 
TRP   C   OXT  sing N N 401 
TRP   CB  CG   sing N N 402 
TRP   CB  HB2  sing N N 403 
TRP   CB  HB3  sing N N 404 
TRP   CG  CD1  doub Y N 405 
TRP   CG  CD2  sing Y N 406 
TRP   CD1 NE1  sing Y N 407 
TRP   CD1 HD1  sing N N 408 
TRP   CD2 CE2  doub Y N 409 
TRP   CD2 CE3  sing Y N 410 
TRP   NE1 CE2  sing Y N 411 
TRP   NE1 HE1  sing N N 412 
TRP   CE2 CZ2  sing Y N 413 
TRP   CE3 CZ3  doub Y N 414 
TRP   CE3 HE3  sing N N 415 
TRP   CZ2 CH2  doub Y N 416 
TRP   CZ2 HZ2  sing N N 417 
TRP   CZ3 CH2  sing Y N 418 
TRP   CZ3 HZ3  sing N N 419 
TRP   CH2 HH2  sing N N 420 
TRP   OXT HXT  sing N N 421 
TYR   N   CA   sing N N 422 
TYR   N   H    sing N N 423 
TYR   N   H2   sing N N 424 
TYR   CA  C    sing N N 425 
TYR   CA  CB   sing N N 426 
TYR   CA  HA   sing N N 427 
TYR   C   O    doub N N 428 
TYR   C   OXT  sing N N 429 
TYR   CB  CG   sing N N 430 
TYR   CB  HB2  sing N N 431 
TYR   CB  HB3  sing N N 432 
TYR   CG  CD1  doub Y N 433 
TYR   CG  CD2  sing Y N 434 
TYR   CD1 CE1  sing Y N 435 
TYR   CD1 HD1  sing N N 436 
TYR   CD2 CE2  doub Y N 437 
TYR   CD2 HD2  sing N N 438 
TYR   CE1 CZ   doub Y N 439 
TYR   CE1 HE1  sing N N 440 
TYR   CE2 CZ   sing Y N 441 
TYR   CE2 HE2  sing N N 442 
TYR   CZ  OH   sing N N 443 
TYR   OH  HH   sing N N 444 
TYR   OXT HXT  sing N N 445 
VAL   N   CA   sing N N 446 
VAL   N   H    sing N N 447 
VAL   N   H2   sing N N 448 
VAL   CA  C    sing N N 449 
VAL   CA  CB   sing N N 450 
VAL   CA  HA   sing N N 451 
VAL   C   O    doub N N 452 
VAL   C   OXT  sing N N 453 
VAL   CB  CG1  sing N N 454 
VAL   CB  CG2  sing N N 455 
VAL   CB  HB   sing N N 456 
VAL   CG1 HG11 sing N N 457 
VAL   CG1 HG12 sing N N 458 
VAL   CG1 HG13 sing N N 459 
VAL   CG2 HG21 sing N N 460 
VAL   CG2 HG22 sing N N 461 
VAL   CG2 HG23 sing N N 462 
VAL   OXT HXT  sing N N 463 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Switzerland 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002292 
_pdbx_deposit_group.group_description   'A set of chymase crystal structures for D3R plus two CatG off-target structures' 
_pdbx_deposit_group.group_title         'A set of chymase crystal structures for D3R plus two CatG off-target structures' 
_pdbx_deposit_group.group_type          undefined 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'apo structure' 
# 
_atom_sites.entry_id                    7H65 
_atom_sites.fract_transf_matrix[1][1]   0.013256 
_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]   0.013256 
_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]   0.020214 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ILE   A 1 1   ? -30.412 21.462  -4.737  1.00 13.34 ? 16  ILE   A N   1 
ATOM   2    C  CA  . ILE   A 1 1   ? -29.498 21.907  -5.835  1.00 13.47 ? 16  ILE   A CA  1 
ATOM   3    C  C   . ILE   A 1 1   ? -29.996 23.249  -6.380  1.00 13.58 ? 16  ILE   A C   1 
ATOM   4    O  O   . ILE   A 1 1   ? -31.137 23.352  -6.818  1.00 12.25 ? 16  ILE   A O   1 
ATOM   5    C  CB  . ILE   A 1 1   ? -29.415 20.843  -6.950  1.00 13.50 ? 16  ILE   A CB  1 
ATOM   6    C  CG1 . ILE   A 1 1   ? -28.995 19.456  -6.436  1.00 13.06 ? 16  ILE   A CG1 1 
ATOM   7    C  CG2 . ILE   A 1 1   ? -28.504 21.319  -8.081  1.00 13.95 ? 16  ILE   A CG2 1 
ATOM   8    C  CD1 . ILE   A 1 1   ? -27.580 19.365  -5.883  1.00 13.25 ? 16  ILE   A CD1 1 
ATOM   9    N  N   . ILE   A 1 2   ? -29.116 24.263  -6.377  1.00 14.14 ? 17  ILE   A N   1 
ATOM   10   C  CA  . ILE   A 1 2   ? -29.438 25.582  -6.915  1.00 14.81 ? 17  ILE   A CA  1 
ATOM   11   C  C   . ILE   A 1 2   ? -28.809 25.719  -8.304  1.00 14.59 ? 17  ILE   A C   1 
ATOM   12   O  O   . ILE   A 1 2   ? -27.649 25.381  -8.501  1.00 13.91 ? 17  ILE   A O   1 
ATOM   13   C  CB  . ILE   A 1 2   ? -28.978 26.673  -5.925  1.00 15.35 ? 17  ILE   A CB  1 
ATOM   14   C  CG1 . ILE   A 1 2   ? -29.742 26.548  -4.600  1.00 15.70 ? 17  ILE   A CG1 1 
ATOM   15   C  CG2 . ILE   A 1 2   ? -29.121 28.078  -6.516  1.00 15.35 ? 17  ILE   A CG2 1 
ATOM   16   C  CD1 . ILE   A 1 2   ? -29.149 27.338  -3.449  1.00 16.32 ? 17  ILE   A CD1 1 
ATOM   17   N  N   . GLY   A 1 3   ? -29.611 26.147  -9.288  1.00 15.40 ? 18  GLY   A N   1 
ATOM   18   C  CA  . GLY   A 1 3   ? -29.112 26.465  -10.619 1.00 15.65 ? 18  GLY   A CA  1 
ATOM   19   C  C   . GLY   A 1 3   ? -28.754 25.239  -11.466 1.00 16.39 ? 18  GLY   A C   1 
ATOM   20   O  O   . GLY   A 1 3   ? -27.897 25.340  -12.343 1.00 16.46 ? 18  GLY   A O   1 
ATOM   21   N  N   . GLY   A 1 4   ? -29.411 24.092  -11.222 1.00 16.68 ? 19  GLY   A N   1 
ATOM   22   C  CA  . GLY   A 1 4   ? -29.117 22.853  -11.939 1.00 16.46 ? 19  GLY   A CA  1 
ATOM   23   C  C   . GLY   A 1 4   ? -30.205 22.495  -12.954 1.00 16.64 ? 19  GLY   A C   1 
ATOM   24   O  O   . GLY   A 1 4   ? -31.032 23.343  -13.285 1.00 15.93 ? 19  GLY   A O   1 
ATOM   25   N  N   . THR   A 1 5   ? -30.181 21.234  -13.431 1.00 16.59 ? 20  THR   A N   1 
ATOM   26   C  CA  . THR   A 1 5   ? -31.156 20.686  -14.370 1.00 16.71 ? 20  THR   A CA  1 
ATOM   27   C  C   . THR   A 1 5   ? -31.773 19.408  -13.796 1.00 16.15 ? 20  THR   A C   1 
ATOM   28   O  O   . THR   A 1 5   ? -31.173 18.754  -12.944 1.00 14.69 ? 20  THR   A O   1 
ATOM   29   C  CB  . THR   A 1 5   ? -30.480 20.378  -15.708 1.00 16.99 ? 20  THR   A CB  1 
ATOM   30   O  OG1 . THR   A 1 5   ? -29.442 19.431  -15.454 1.00 18.15 ? 20  THR   A OG1 1 
ATOM   31   C  CG2 . THR   A 1 5   ? -29.878 21.608  -16.365 1.00 17.75 ? 20  THR   A CG2 1 
ATOM   32   N  N   . GLU   A 1 6   ? -32.951 19.027  -14.314 1.00 15.25 ? 21  GLU   A N   1 
ATOM   33   C  CA  . GLU   A 1 6   ? -33.581 17.761  -13.957 1.00 14.57 ? 21  GLU   A CA  1 
ATOM   34   C  C   . GLU   A 1 6   ? -32.746 16.604  -14.509 1.00 13.72 ? 21  GLU   A C   1 
ATOM   35   O  O   . GLU   A 1 6   ? -32.437 16.585  -15.698 1.00 13.49 ? 21  GLU   A O   1 
ATOM   36   C  CB  . GLU   A 1 6   ? -35.028 17.736  -14.465 1.00 15.38 ? 21  GLU   A CB  1 
ATOM   37   C  CG  . GLU   A 1 6   ? -35.792 16.469  -14.076 1.00 15.99 ? 21  GLU   A CG  1 
ATOM   38   C  CD  . GLU   A 1 6   ? -37.216 16.305  -14.591 1.00 17.32 ? 21  GLU   A CD  1 
ATOM   39   O  OE1 . GLU   A 1 6   ? -37.757 17.247  -15.223 1.00 18.54 ? 21  GLU   A OE1 1 
ATOM   40   O  OE2 . GLU   A 1 6   ? -37.797 15.213  -14.359 1.00 16.86 ? 21  GLU   A OE2 1 
ATOM   41   N  N   . SER   A 1 7   ? -32.386 15.636  -13.645 1.00 13.01 ? 22  SER   A N   1 
ATOM   42   C  CA  . SER   A 1 7   ? -31.667 14.443  -14.066 1.00 12.65 ? 22  SER   A CA  1 
ATOM   43   C  C   . SER   A 1 7   ? -32.538 13.623  -15.019 1.00 12.58 ? 22  SER   A C   1 
ATOM   44   O  O   . SER   A 1 7   ? -33.757 13.623  -14.885 1.00 11.77 ? 22  SER   A O   1 
ATOM   45   C  CB  . SER   A 1 7   ? -31.237 13.580  -12.887 1.00 12.96 ? 22  SER   A CB  1 
ATOM   46   O  OG  . SER   A 1 7   ? -30.327 14.238  -12.010 1.00 13.24 ? 22  SER   A OG  1 
ATOM   47   N  N   . LYS   A 1 8   ? -31.902 12.938  -15.981 1.00 12.96 ? 23  LYS   A N   1 
ATOM   48   C  CA  . LYS   A 1 8   ? -32.562 11.883  -16.745 1.00 13.56 ? 23  LYS   A CA  1 
ATOM   49   C  C   . LYS   A 1 8   ? -33.042 10.801  -15.772 1.00 13.02 ? 23  LYS   A C   1 
ATOM   50   O  O   . LYS   A 1 8   ? -32.250 10.274  -14.992 1.00 12.96 ? 23  LYS   A O   1 
ATOM   51   C  CB  . LYS   A 1 8   ? -31.632 11.297  -17.819 1.00 14.12 ? 23  LYS   A CB  1 
ATOM   52   C  CG  . LYS   A 1 8   ? -32.191 10.117  -18.610 1.00 14.52 ? 23  LYS   A CG  1 
ATOM   53   C  CD  . LYS   A 1 8   ? -31.307 9.586   -19.730 0.50 14.70 ? 23  LYS   A CD  1 
ATOM   54   C  CE  . LYS   A 1 8   ? -32.010 8.490   -20.465 0.50 15.02 ? 23  LYS   A CE  1 
ATOM   55   N  NZ  . LYS   A 1 8   ? -31.115 7.816   -21.404 0.50 15.45 ? 23  LYS   A NZ  1 
ATOM   56   N  N   . PRO   A 1 9   ? -34.348 10.447  -15.763 1.00 12.94 ? 24  PRO   A N   1 
ATOM   57   C  CA  . PRO   A 1 9   ? -34.862 9.466   -14.798 1.00 12.50 ? 24  PRO   A CA  1 
ATOM   58   C  C   . PRO   A 1 9   ? -34.070 8.156   -14.732 1.00 11.85 ? 24  PRO   A C   1 
ATOM   59   O  O   . PRO   A 1 9   ? -33.832 7.521   -15.757 1.00 11.07 ? 24  PRO   A O   1 
ATOM   60   C  CB  . PRO   A 1 9   ? -36.303 9.257   -15.286 1.00 13.15 ? 24  PRO   A CB  1 
ATOM   61   C  CG  . PRO   A 1 9   ? -36.675 10.577  -15.952 1.00 13.48 ? 24  PRO   A CG  1 
ATOM   62   C  CD  . PRO   A 1 9   ? -35.394 10.991  -16.653 1.00 13.19 ? 24  PRO   A CD  1 
ATOM   63   N  N   . HIS   A 1 10  ? -33.636 7.789   -13.513 1.00 11.70 ? 25  HIS   A N   1 
ATOM   64   C  CA  . HIS   A 1 10  ? -32.977 6.518   -13.222 1.00 11.51 ? 25  HIS   A CA  1 
ATOM   65   C  C   . HIS   A 1 10  ? -31.551 6.438   -13.794 1.00 11.88 ? 25  HIS   A C   1 
ATOM   66   O  O   . HIS   A 1 10  ? -30.957 5.351   -13.793 1.00 11.73 ? 25  HIS   A O   1 
ATOM   67   C  CB  . HIS   A 1 10  ? -33.861 5.333   -13.651 1.00 12.20 ? 25  HIS   A CB  1 
ATOM   68   C  CG  . HIS   A 1 10  ? -35.282 5.391   -13.163 1.00 12.51 ? 25  HIS   A CG  1 
ATOM   69   N  ND1 . HIS   A 1 10  ? -35.598 5.445   -11.822 1.00 12.22 ? 25  HIS   A ND1 1 
ATOM   70   C  CD2 . HIS   A 1 10  ? -36.467 5.436   -13.820 1.00 13.07 ? 25  HIS   A CD2 1 
ATOM   71   C  CE1 . HIS   A 1 10  ? -36.920 5.520   -11.679 1.00 12.82 ? 25  HIS   A CE1 1 
ATOM   72   N  NE2 . HIS   A 1 10  ? -37.470 5.490   -12.874 1.00 13.18 ? 25  HIS   A NE2 1 
ATOM   73   N  N   . SER   A 1 11  ? -30.969 7.584   -14.197 1.00 11.83 ? 26  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 11  ? -29.631 7.645   -14.783 1.00 12.66 ? 26  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 11  ? -28.511 7.580   -13.738 1.00 13.25 ? 26  SER   A C   1 
ATOM   76   O  O   . SER   A 1 11  ? -27.342 7.409   -14.107 1.00 13.40 ? 26  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 11  ? -29.462 8.882   -15.652 1.00 12.89 ? 26  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 11  ? -29.598 10.098  -14.921 1.00 12.41 ? 26  SER   A OG  1 
ATOM   79   N  N   . ARG   A 1 12  ? -28.853 7.726   -12.448 1.00 13.32 ? 27  ARG   A N   1 
ATOM   80   C  CA  . ARG   A 1 12  ? -27.891 7.604   -11.360 1.00 13.51 ? 27  ARG   A CA  1 
ATOM   81   C  C   . ARG   A 1 12  ? -28.400 6.570   -10.352 1.00 12.52 ? 27  ARG   A C   1 
ATOM   82   O  O   . ARG   A 1 12  ? -28.855 6.919   -9.266  1.00 11.48 ? 27  ARG   A O   1 
ATOM   83   C  CB  . ARG   A 1 12  ? -27.651 8.987   -10.739 1.00 14.32 ? 27  ARG   A CB  1 
ATOM   84   C  CG  . ARG   A 1 12  ? -27.011 9.992   -11.692 1.00 15.64 ? 27  ARG   A CG  1 
ATOM   85   C  CD  . ARG   A 1 12  ? -26.817 11.356  -11.042 1.00 16.84 ? 27  ARG   A CD  1 
ATOM   86   N  NE  . ARG   A 1 12  ? -26.160 12.340  -11.916 1.00 18.17 ? 27  ARG   A NE  1 
ATOM   87   C  CZ  . ARG   A 1 12  ? -24.865 12.380  -12.228 1.00 18.58 ? 27  ARG   A CZ  1 
ATOM   88   N  NH1 . ARG   A 1 12  ? -24.010 11.525  -11.690 1.00 19.28 ? 27  ARG   A NH1 1 
ATOM   89   N  NH2 . ARG   A 1 12  ? -24.421 13.293  -13.071 1.00 18.80 ? 27  ARG   A NH2 1 
ATOM   90   N  N   . PRO   A 1 13  ? -28.337 5.256   -10.676 1.00 12.27 ? 28  PRO   A N   1 
ATOM   91   C  CA  . PRO   A 1 13  ? -29.069 4.241   -9.907  1.00 11.73 ? 28  PRO   A CA  1 
ATOM   92   C  C   . PRO   A 1 13  ? -28.551 3.902   -8.502  1.00 10.97 ? 28  PRO   A C   1 
ATOM   93   O  O   . PRO   A 1 13  ? -29.203 3.159   -7.771  1.00 10.26 ? 28  PRO   A O   1 
ATOM   94   C  CB  . PRO   A 1 13  ? -29.039 3.032   -10.872 1.00 12.05 ? 28  PRO   A CB  1 
ATOM   95   C  CG  . PRO   A 1 13  ? -27.772 3.204   -11.674 1.00 12.43 ? 28  PRO   A CG  1 
ATOM   96   C  CD  . PRO   A 1 13  ? -27.602 4.698   -11.826 1.00 12.34 ? 28  PRO   A CD  1 
ATOM   97   N  N   . TYR   A 1 14  ? -27.414 4.499   -8.121  1.00 10.77 ? 29  TYR   A N   1 
ATOM   98   C  CA  . TYR   A 1 14  ? -26.840 4.387   -6.782  1.00 11.14 ? 29  TYR   A CA  1 
ATOM   99   C  C   . TYR   A 1 14  ? -27.449 5.407   -5.808  1.00 10.68 ? 29  TYR   A C   1 
ATOM   100  O  O   . TYR   A 1 14  ? -27.177 5.328   -4.616  1.00 11.16 ? 29  TYR   A O   1 
ATOM   101  C  CB  . TYR   A 1 14  ? -25.312 4.551   -6.884  1.00 11.18 ? 29  TYR   A CB  1 
ATOM   102  C  CG  . TYR   A 1 14  ? -24.891 5.696   -7.801  1.00 11.41 ? 29  TYR   A CG  1 
ATOM   103  C  CD1 . TYR   A 1 14  ? -24.951 7.015   -7.367  1.00 11.44 ? 29  TYR   A CD1 1 
ATOM   104  C  CD2 . TYR   A 1 14  ? -24.483 5.466   -9.114  1.00 11.40 ? 29  TYR   A CD2 1 
ATOM   105  C  CE1 . TYR   A 1 14  ? -24.631 8.069   -8.210  1.00 11.70 ? 29  TYR   A CE1 1 
ATOM   106  C  CE2 . TYR   A 1 14  ? -24.148 6.514   -9.962  1.00 11.59 ? 29  TYR   A CE2 1 
ATOM   107  C  CZ  . TYR   A 1 14  ? -24.228 7.821   -9.509  1.00 11.95 ? 29  TYR   A CZ  1 
ATOM   108  O  OH  . TYR   A 1 14  ? -23.912 8.887   -10.316 1.00 12.28 ? 29  TYR   A OH  1 
ATOM   109  N  N   . MET   A 1 15  ? -28.272 6.360   -6.274  1.00 10.51 ? 30  MET   A N   1 
ATOM   110  C  CA  . MET   A 1 15  ? -28.706 7.461   -5.414  1.00 10.36 ? 30  MET   A CA  1 
ATOM   111  C  C   . MET   A 1 15  ? -29.753 6.996   -4.392  1.00 10.57 ? 30  MET   A C   1 
ATOM   112  O  O   . MET   A 1 15  ? -30.680 6.255   -4.726  1.00 10.81 ? 30  MET   A O   1 
ATOM   113  C  CB  . MET   A 1 15  ? -29.287 8.630   -6.222  1.00 10.33 ? 30  MET   A CB  1 
ATOM   114  C  CG  . MET   A 1 15  ? -28.265 9.471   -7.005  1.00 10.49 ? 30  MET   A CG  1 
ATOM   115  S  SD  . MET   A 1 15  ? -27.056 10.364  -5.997  1.00 10.06 ? 30  MET   A SD  1 
ATOM   116  C  CE  . MET   A 1 15  ? -28.064 11.298  -4.837  1.00 10.26 ? 30  MET   A CE  1 
ATOM   117  N  N   . ALA   A 1 16  ? -29.634 7.501   -3.152  1.00 10.38 ? 31  ALA   A N   1 
ATOM   118  C  CA  . ALA   A 1 16  ? -30.536 7.168   -2.057  1.00 10.53 ? 31  ALA   A CA  1 
ATOM   119  C  C   . ALA   A 1 16  ? -31.178 8.430   -1.465  1.00 10.70 ? 31  ALA   A C   1 
ATOM   120  O  O   . ALA   A 1 16  ? -30.498 9.432   -1.250  1.00 10.18 ? 31  ALA   A O   1 
ATOM   121  C  CB  . ALA   A 1 16  ? -29.780 6.396   -0.999  1.00 10.26 ? 31  ALA   A CB  1 
ATOM   122  N  N   . TYR   A 1 17  ? -32.491 8.341   -1.193  1.00 10.93 ? 32  TYR   A N   1 
ATOM   123  C  CA  . TYR   A 1 17  ? -33.262 9.378   -0.516  1.00 11.77 ? 32  TYR   A CA  1 
ATOM   124  C  C   . TYR   A 1 17  ? -33.539 8.937   0.926   1.00 11.56 ? 32  TYR   A C   1 
ATOM   125  O  O   . TYR   A 1 17  ? -34.169 7.905   1.130   1.00 10.93 ? 32  TYR   A O   1 
ATOM   126  C  CB  . TYR   A 1 17  ? -34.548 9.602   -1.322  1.00 12.33 ? 32  TYR   A CB  1 
ATOM   127  C  CG  . TYR   A 1 17  ? -35.550 10.621  -0.789  1.00 13.48 ? 32  TYR   A CG  1 
ATOM   128  C  CD1 . TYR   A 1 17  ? -35.520 11.950  -1.205  1.00 14.32 ? 32  TYR   A CD1 1 
ATOM   129  C  CD2 . TYR   A 1 17  ? -36.565 10.246  0.088   1.00 14.22 ? 32  TYR   A CD2 1 
ATOM   130  C  CE1 . TYR   A 1 17  ? -36.449 12.874  -0.749  1.00 14.91 ? 32  TYR   A CE1 1 
ATOM   131  C  CE2 . TYR   A 1 17  ? -37.493 11.163  0.560   1.00 15.01 ? 32  TYR   A CE2 1 
ATOM   132  C  CZ  . TYR   A 1 17  ? -37.436 12.481  0.139   1.00 15.87 ? 32  TYR   A CZ  1 
ATOM   133  O  OH  . TYR   A 1 17  ? -38.362 13.387  0.595   1.00 16.87 ? 32  TYR   A OH  1 
ATOM   134  N  N   . LEU   A 1 18  ? -33.087 9.748   1.903   1.00 11.65 ? 33  LEU   A N   1 
ATOM   135  C  CA  . LEU   A 1 18  ? -33.115 9.434   3.329   1.00 12.14 ? 33  LEU   A CA  1 
ATOM   136  C  C   . LEU   A 1 18  ? -34.146 10.306  4.049   1.00 12.78 ? 33  LEU   A C   1 
ATOM   137  O  O   . LEU   A 1 18  ? -34.072 11.531  3.978   1.00 12.10 ? 33  LEU   A O   1 
ATOM   138  C  CB  . LEU   A 1 18  ? -31.731 9.668   3.942   1.00 12.55 ? 33  LEU   A CB  1 
ATOM   139  C  CG  . LEU   A 1 18  ? -30.713 8.527   3.831   1.00 13.31 ? 33  LEU   A CG  1 
ATOM   140  C  CD1 . LEU   A 1 18  ? -30.520 8.068   2.406   1.00 13.77 ? 33  LEU   A CD1 1 
ATOM   141  C  CD2 . LEU   A 1 18  ? -29.369 8.934   4.427   1.00 13.13 ? 33  LEU   A CD2 1 
ATOM   142  N  N   . GLU   A 1 19  ? -35.077 9.662   4.772   1.00 13.64 ? 34  GLU   A N   1 
ATOM   143  C  CA  . GLU   A 1 19  ? -36.018 10.335  5.660   1.00 14.70 ? 34  GLU   A CA  1 
ATOM   144  C  C   . GLU   A 1 19  ? -35.662 9.981   7.107   1.00 14.38 ? 34  GLU   A C   1 
ATOM   145  O  O   . GLU   A 1 19  ? -35.678 8.806   7.477   1.00 14.04 ? 34  GLU   A O   1 
ATOM   146  C  CB  . GLU   A 1 19  ? -37.429 9.907   5.243   1.00 16.74 ? 34  GLU   A CB  1 
ATOM   147  C  CG  . GLU   A 1 19  ? -38.563 10.446  6.111   1.00 18.93 ? 34  GLU   A CG  1 
ATOM   148  C  CD  . GLU   A 1 19  ? -39.937 10.076  5.556   1.00 20.96 ? 34  GLU   A CD  1 
ATOM   149  O  OE1 . GLU   A 1 19  ? -40.568 9.159   6.122   1.00 25.05 ? 34  GLU   A OE1 1 
ATOM   150  O  OE2 . GLU   A 1 19  ? -40.360 10.668  4.546   0.50 21.03 ? 34  GLU   A OE2 1 
ATOM   151  N  N   . ILE   A 1 20  ? -35.354 11.006  7.923   1.00 13.83 ? 35  ILE   A N   1 
ATOM   152  C  CA  . ILE   A 1 20  ? -34.734 10.805  9.224   1.00 14.43 ? 35  ILE   A CA  1 
ATOM   153  C  C   . ILE   A 1 20  ? -35.663 11.301  10.332  1.00 15.74 ? 35  ILE   A C   1 
ATOM   154  O  O   . ILE   A 1 20  ? -36.091 12.452  10.309  1.00 15.32 ? 35  ILE   A O   1 
ATOM   155  C  CB  . ILE   A 1 20  ? -33.374 11.525  9.288   1.00 14.13 ? 35  ILE   A CB  1 
ATOM   156  C  CG1 . ILE   A 1 20  ? -32.416 11.032  8.179   1.00 14.07 ? 35  ILE   A CG1 1 
ATOM   157  C  CG2 . ILE   A 1 20  ? -32.754 11.377  10.679  1.00 14.37 ? 35  ILE   A CG2 1 
ATOM   158  C  CD1 . ILE   A 1 20  ? -31.763 12.149  7.392   1.00 13.98 ? 35  ILE   A CD1 1 
ATOM   159  N  N   . VAL   A 1 21  ? -35.880 10.450  11.342  1.00 18.01 ? 36  VAL   A N   1 
ATOM   160  C  CA  . VAL   A 1 21  ? -36.751 10.758  12.470  1.00 21.07 ? 36  VAL   A CA  1 
ATOM   161  C  C   . VAL   A 1 21  ? -35.922 11.236  13.664  1.00 23.37 ? 36  VAL   A C   1 
ATOM   162  O  O   . VAL   A 1 21  ? -34.992 10.547  14.085  1.00 21.84 ? 36  VAL   A O   1 
ATOM   163  C  CB  . VAL   A 1 21  ? -37.579 9.511   12.842  1.00 22.32 ? 36  VAL   A CB  1 
ATOM   164  C  CG1 . VAL   A 1 21  ? -38.388 9.712   14.121  1.00 23.19 ? 36  VAL   A CG1 1 
ATOM   165  C  CG2 . VAL   A 1 21  ? -38.481 9.073   11.697  1.00 22.41 ? 36  VAL   A CG2 1 
ATOM   166  N  N   . THR   A 1 22  A -36.287 12.415  14.192  1.00 26.39 ? 36  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 22  A -35.796 12.925  15.466  1.00 31.66 ? 36  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 22  A -36.910 12.804  16.511  1.00 33.22 ? 36  THR   A C   1 
ATOM   169  O  O   . THR   A 1 22  A -38.085 12.697  16.165  1.00 35.44 ? 36  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 22  A -35.329 14.374  15.299  1.00 33.84 ? 36  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 22  A -36.439 15.119  14.805  1.00 36.47 ? 36  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 22  A -34.185 14.520  14.313  1.00 35.36 ? 36  THR   A CG2 1 
ATOM   173  N  N   . SER   A 1 23  B -36.540 12.851  17.796  1.00 35.28 ? 36  SER   A N   1 
ATOM   174  C  CA  . SER   A 1 23  B -37.462 12.561  18.891  1.00 34.70 ? 36  SER   A CA  1 
ATOM   175  C  C   . SER   A 1 23  B -38.522 13.654  19.083  1.00 35.93 ? 36  SER   A C   1 
ATOM   176  O  O   . SER   A 1 23  B -39.685 13.339  19.366  1.00 35.86 ? 36  SER   A O   1 
ATOM   177  C  CB  . SER   A 1 23  B -36.703 12.332  20.174  0.10 34.89 ? 36  SER   A CB  1 
ATOM   178  O  OG  . SER   A 1 23  B -35.919 13.466  20.515  0.10 34.74 ? 36  SER   A OG  1 
ATOM   179  N  N   . ASN   A 1 24  ? -38.121 14.929  18.940  1.00 34.37 ? 37  ASN   A N   1 
ATOM   180  C  CA  . ASN   A 1 24  ? -38.983 16.053  19.284  1.00 33.04 ? 37  ASN   A CA  1 
ATOM   181  C  C   . ASN   A 1 24  ? -39.198 16.995  18.095  1.00 29.07 ? 37  ASN   A C   1 
ATOM   182  O  O   . ASN   A 1 24  ? -39.328 18.203  18.286  1.00 30.89 ? 37  ASN   A O   1 
ATOM   183  C  CB  . ASN   A 1 24  ? -38.424 16.817  20.482  1.00 36.20 ? 37  ASN   A CB  1 
ATOM   184  C  CG  . ASN   A 1 24  ? -37.055 17.402  20.213  1.00 37.47 ? 37  ASN   A CG  1 
ATOM   185  O  OD1 . ASN   A 1 24  ? -36.482 17.182  19.139  1.00 39.78 ? 37  ASN   A OD1 1 
ATOM   186  N  ND2 . ASN   A 1 24  ? -36.513 18.141  21.171  0.10 37.27 ? 37  ASN   A ND2 1 
ATOM   187  N  N   . GLY   A 1 25  A -39.260 16.451  16.873  1.00 23.80 ? 37  GLY   A N   1 
ATOM   188  C  CA  . GLY   A 1 25  A -39.577 17.250  15.697  1.00 20.98 ? 37  GLY   A CA  1 
ATOM   189  C  C   . GLY   A 1 25  A -40.074 16.381  14.543  1.00 18.30 ? 37  GLY   A C   1 
ATOM   190  O  O   . GLY   A 1 25  A -40.023 15.154  14.627  1.00 15.99 ? 37  GLY   A O   1 
ATOM   191  N  N   . PRO   A 1 26  ? -40.602 16.983  13.448  1.00 15.76 ? 38  PRO   A N   1 
ATOM   192  C  CA  . PRO   A 1 26  ? -41.002 16.209  12.270  1.00 15.01 ? 38  PRO   A CA  1 
ATOM   193  C  C   . PRO   A 1 26  ? -39.783 15.723  11.483  1.00 13.99 ? 38  PRO   A C   1 
ATOM   194  O  O   . PRO   A 1 26  ? -38.663 16.125  11.774  1.00 13.76 ? 38  PRO   A O   1 
ATOM   195  C  CB  . PRO   A 1 26  ? -41.865 17.215  11.471  1.00 15.20 ? 38  PRO   A CB  1 
ATOM   196  C  CG  . PRO   A 1 26  ? -41.288 18.566  11.830  1.00 15.45 ? 38  PRO   A CG  1 
ATOM   197  C  CD  . PRO   A 1 26  ? -40.847 18.426  13.285  1.00 15.51 ? 38  PRO   A CD  1 
ATOM   198  N  N   . SER   A 1 27  ? -40.036 14.896  10.461  1.00 13.87 ? 39  SER   A N   1 
ATOM   199  C  CA  . SER   A 1 27  ? -39.022 14.341  9.568   1.00 13.47 ? 39  SER   A CA  1 
ATOM   200  C  C   . SER   A 1 27  ? -38.110 15.421  8.975   1.00 13.30 ? 39  SER   A C   1 
ATOM   201  O  O   . SER   A 1 27  ? -38.586 16.499  8.619   1.00 12.60 ? 39  SER   A O   1 
ATOM   202  C  CB  . SER   A 1 27  ? -39.681 13.575  8.443   1.00 13.53 ? 39  SER   A CB  1 
ATOM   203  O  OG  . SER   A 1 27  ? -40.376 12.435  8.922   1.00 14.26 ? 39  SER   A OG  1 
ATOM   204  N  N   . LYS   A 1 28  ? -36.813 15.082  8.833   1.00 13.14 ? 40  LYS   A N   1 
ATOM   205  C  CA  . LYS   A 1 28  ? -35.843 15.836  8.039   1.00 13.53 ? 40  LYS   A CA  1 
ATOM   206  C  C   . LYS   A 1 28  ? -35.251 14.932  6.947   1.00 13.51 ? 40  LYS   A C   1 
ATOM   207  O  O   . LYS   A 1 28  ? -35.423 13.716  7.011   1.00 13.55 ? 40  LYS   A O   1 
ATOM   208  C  CB  . LYS   A 1 28  ? -34.737 16.357  8.963   1.00 14.09 ? 40  LYS   A CB  1 
ATOM   209  C  CG  . LYS   A 1 28  ? -35.130 17.440  9.966   1.00 14.93 ? 40  LYS   A CG  1 
ATOM   210  C  CD  . LYS   A 1 28  ? -33.998 17.815  10.916  0.50 15.44 ? 40  LYS   A CD  1 
ATOM   211  C  CE  . LYS   A 1 28  ? -34.324 18.972  11.805  0.50 16.30 ? 40  LYS   A CE  1 
ATOM   212  N  NZ  . LYS   A 1 28  ? -33.314 19.142  12.855  0.50 16.91 ? 40  LYS   A NZ  1 
ATOM   213  N  N   . PHE   A 1 29  ? -34.536 15.512  5.958   1.00 13.11 ? 41  PHE   A N   1 
ATOM   214  C  CA  . PHE   A 1 29  ? -34.147 14.782  4.746   1.00 12.88 ? 41  PHE   A CA  1 
ATOM   215  C  C   . PHE   A 1 29  ? -32.681 15.011  4.363   1.00 11.68 ? 41  PHE   A C   1 
ATOM   216  O  O   . PHE   A 1 29  ? -32.136 16.089  4.585   1.00 11.21 ? 41  PHE   A O   1 
ATOM   217  C  CB  . PHE   A 1 29  ? -35.097 15.187  3.608   1.00 14.34 ? 41  PHE   A CB  1 
ATOM   218  C  CG  . PHE   A 1 29  ? -36.558 14.913  3.940   1.00 15.84 ? 41  PHE   A CG  1 
ATOM   219  C  CD1 . PHE   A 1 29  ? -37.173 13.734  3.536   1.00 17.25 ? 41  PHE   A CD1 1 
ATOM   220  C  CD2 . PHE   A 1 29  ? -37.304 15.823  4.689   1.00 16.90 ? 41  PHE   A CD2 1 
ATOM   221  C  CE1 . PHE   A 1 29  ? -38.503 13.474  3.863   1.00 17.81 ? 41  PHE   A CE1 1 
ATOM   222  C  CE2 . PHE   A 1 29  ? -38.627 15.554  5.027   1.00 17.43 ? 41  PHE   A CE2 1 
ATOM   223  C  CZ  . PHE   A 1 29  ? -39.224 14.381  4.607   1.00 17.85 ? 41  PHE   A CZ  1 
ATOM   224  N  N   . CYS   A 1 30  ? -32.054 13.966  3.787   1.00 10.53 ? 42  CYS   A N   1 
ATOM   225  C  CA  . CYS   A 1 30  ? -30.703 14.008  3.237   1.00 10.09 ? 42  CYS   A CA  1 
ATOM   226  C  C   . CYS   A 1 30  ? -30.598 13.090  2.013   1.00 9.77  ? 42  CYS   A C   1 
ATOM   227  O  O   . CYS   A 1 30  ? -31.498 12.296  1.738   1.00 9.55  ? 42  CYS   A O   1 
ATOM   228  C  CB  . CYS   A 1 30  ? -29.650 13.516  4.235   1.00 9.90  ? 42  CYS   A CB  1 
ATOM   229  S  SG  . CYS   A 1 30  ? -29.337 14.612  5.645   1.00 9.79  ? 42  CYS   A SG  1 
ATOM   230  N  N   . GLY   A 1 31  ? -29.467 13.181  1.298   1.00 9.47  ? 43  GLY   A N   1 
ATOM   231  C  CA  . GLY   A 1 31  ? -29.103 12.223  0.266   1.00 9.42  ? 43  GLY   A CA  1 
ATOM   232  C  C   . GLY   A 1 31  ? -28.102 11.194  0.786   1.00 9.57  ? 43  GLY   A C   1 
ATOM   233  O  O   . GLY   A 1 31  ? -27.691 11.285  1.937   1.00 9.87  ? 43  GLY   A O   1 
ATOM   234  N  N   . GLY   A 1 32  ? -27.745 10.227  -0.081  1.00 9.78  ? 44  GLY   A N   1 
ATOM   235  C  CA  . GLY   A 1 32  ? -26.756 9.180   0.171   1.00 9.91  ? 44  GLY   A CA  1 
ATOM   236  C  C   . GLY   A 1 32  ? -26.503 8.359   -1.100  1.00 10.14 ? 44  GLY   A C   1 
ATOM   237  O  O   . GLY   A 1 32  ? -27.127 8.637   -2.126  1.00 9.67  ? 44  GLY   A O   1 
ATOM   238  N  N   . PHE   A 1 33  ? -25.616 7.343   -1.041  1.00 10.42 ? 45  PHE   A N   1 
ATOM   239  C  CA  . PHE   A 1 33  ? -25.368 6.488   -2.201  1.00 11.16 ? 45  PHE   A CA  1 
ATOM   240  C  C   . PHE   A 1 33  ? -24.996 5.057   -1.786  1.00 11.27 ? 45  PHE   A C   1 
ATOM   241  O  O   . PHE   A 1 33  ? -24.272 4.844   -0.819  1.00 11.73 ? 45  PHE   A O   1 
ATOM   242  C  CB  . PHE   A 1 33  ? -24.328 7.079   -3.166  1.00 11.70 ? 45  PHE   A CB  1 
ATOM   243  C  CG  . PHE   A 1 33  ? -22.991 7.531   -2.585  1.00 12.81 ? 45  PHE   A CG  1 
ATOM   244  C  CD1 . PHE   A 1 33  ? -22.908 8.650   -1.762  1.00 13.49 ? 45  PHE   A CD1 1 
ATOM   245  C  CD2 . PHE   A 1 33  ? -21.811 6.868   -2.909  1.00 13.85 ? 45  PHE   A CD2 1 
ATOM   246  C  CE1 . PHE   A 1 33  ? -21.685 9.060   -1.241  1.00 14.12 ? 45  PHE   A CE1 1 
ATOM   247  C  CE2 . PHE   A 1 33  ? -20.589 7.291   -2.392  1.00 14.22 ? 45  PHE   A CE2 1 
ATOM   248  C  CZ  . PHE   A 1 33  ? -20.531 8.385   -1.563  1.00 14.14 ? 45  PHE   A CZ  1 
ATOM   249  N  N   . LEU   A 1 34  ? -25.475 4.080   -2.573  1.00 11.57 ? 46  LEU   A N   1 
ATOM   250  C  CA  . LEU   A 1 34  ? -25.314 2.653   -2.300  1.00 11.95 ? 46  LEU   A CA  1 
ATOM   251  C  C   . LEU   A 1 34  ? -23.925 2.194   -2.746  1.00 12.24 ? 46  LEU   A C   1 
ATOM   252  O  O   . LEU   A 1 34  ? -23.614 2.308   -3.928  1.00 11.99 ? 46  LEU   A O   1 
ATOM   253  C  CB  . LEU   A 1 34  ? -26.420 1.925   -3.076  1.00 11.96 ? 46  LEU   A CB  1 
ATOM   254  C  CG  . LEU   A 1 34  ? -26.624 0.433   -2.773  1.00 12.48 ? 46  LEU   A CG  1 
ATOM   255  C  CD1 . LEU   A 1 34  ? -27.298 0.224   -1.422  1.00 12.53 ? 46  LEU   A CD1 1 
ATOM   256  C  CD2 . LEU   A 1 34  ? -27.436 -0.260  -3.873  1.00 12.71 ? 46  LEU   A CD2 1 
ATOM   257  N  N   . ILE   A 1 35  ? -23.096 1.679   -1.815  1.00 12.74 ? 47  ILE   A N   1 
ATOM   258  C  CA  . ILE   A 1 35  ? -21.745 1.240   -2.159  1.00 13.47 ? 47  ILE   A CA  1 
ATOM   259  C  C   . ILE   A 1 35  ? -21.613 -0.283  -2.104  1.00 13.24 ? 47  ILE   A C   1 
ATOM   260  O  O   . ILE   A 1 35  ? -20.677 -0.824  -2.691  1.00 12.63 ? 47  ILE   A O   1 
ATOM   261  C  CB  . ILE   A 1 35  ? -20.657 1.941   -1.320  1.00 14.22 ? 47  ILE   A CB  1 
ATOM   262  C  CG1 . ILE   A 1 35  ? -20.721 1.597   0.165   1.00 14.47 ? 47  ILE   A CG1 1 
ATOM   263  C  CG2 . ILE   A 1 35  ? -20.704 3.455   -1.551  1.00 14.72 ? 47  ILE   A CG2 1 
ATOM   264  C  CD1 . ILE   A 1 35  ? -19.466 1.964   0.939   1.00 14.85 ? 47  ILE   A CD1 1 
ATOM   265  N  N   . ARG   A 1 36  ? -22.532 -0.954  -1.391  1.00 13.45 ? 48  ARG   A N   1 
ATOM   266  C  CA  . ARG   A 1 36  ? -22.690 -2.402  -1.425  1.00 13.89 ? 48  ARG   A CA  1 
ATOM   267  C  C   . ARG   A 1 36  ? -24.190 -2.679  -1.336  1.00 12.73 ? 48  ARG   A C   1 
ATOM   268  O  O   . ARG   A 1 36  ? -24.947 -1.795  -0.949  1.00 11.95 ? 48  ARG   A O   1 
ATOM   269  C  CB  . ARG   A 1 36  ? -21.990 -3.129  -0.266  1.00 15.10 ? 48  ARG   A CB  1 
ATOM   270  C  CG  . ARG   A 1 36  ? -20.476 -2.984  -0.154  1.00 16.83 ? 48  ARG   A CG  1 
ATOM   271  C  CD  . ARG   A 1 36  ? -19.727 -3.795  -1.207  1.00 18.27 ? 48  ARG   A CD  1 
ATOM   272  N  NE  . ARG   A 1 36  ? -18.263 -3.767  -1.095  0.50 18.20 ? 48  ARG   A NE  1 
ATOM   273  C  CZ  . ARG   A 1 36  ? -17.482 -2.732  -1.373  0.50 18.64 ? 48  ARG   A CZ  1 
ATOM   274  N  NH1 . ARG   A 1 36  ? -17.994 -1.572  -1.739  0.50 18.57 ? 48  ARG   A NH1 1 
ATOM   275  N  NH2 . ARG   A 1 36  ? -16.173 -2.862  -1.274  0.50 19.39 ? 48  ARG   A NH2 1 
ATOM   276  N  N   . ARG   A 1 37  ? -24.620 -3.902  -1.661  1.00 12.14 ? 49  ARG   A N   1 
ATOM   277  C  CA  . ARG   A 1 37  ? -26.046 -4.199  -1.715  1.00 12.02 ? 49  ARG   A CA  1 
ATOM   278  C  C   . ARG   A 1 37  ? -26.725 -3.933  -0.365  1.00 11.73 ? 49  ARG   A C   1 
ATOM   279  O  O   . ARG   A 1 37  ? -27.933 -3.688  -0.345  1.00 11.22 ? 49  ARG   A O   1 
ATOM   280  C  CB  . ARG   A 1 37  ? -26.332 -5.607  -2.258  1.00 12.19 ? 49  ARG   A CB  1 
ATOM   281  C  CG  . ARG   A 1 37  ? -26.091 -5.765  -3.756  1.00 12.01 ? 49  ARG   A CG  1 
ATOM   282  C  CD  . ARG   A 1 37  ? -26.335 -7.171  -4.315  1.00 12.03 ? 49  ARG   A CD  1 
ATOM   283  N  NE  . ARG   A 1 37  ? -27.742 -7.587  -4.270  1.00 11.60 ? 49  ARG   A NE  1 
ATOM   284  C  CZ  . ARG   A 1 37  ? -28.215 -8.765  -4.660  1.00 11.70 ? 49  ARG   A CZ  1 
ATOM   285  N  NH1 . ARG   A 1 37  ? -27.393 -9.715  -5.087  1.00 11.63 ? 49  ARG   A NH1 1 
ATOM   286  N  NH2 . ARG   A 1 37  ? -29.518 -8.989  -4.644  1.00 11.52 ? 49  ARG   A NH2 1 
ATOM   287  N  N   . ASN   A 1 38  ? -25.973 -3.972  0.752   1.00 11.93 ? 50  ASN   A N   1 
ATOM   288  C  CA  . ASN   A 1 38  ? -26.541 -3.674  2.064   1.00 12.18 ? 50  ASN   A CA  1 
ATOM   289  C  C   . ASN   A 1 38  ? -25.827 -2.534  2.803   1.00 11.53 ? 50  ASN   A C   1 
ATOM   290  O  O   . ASN   A 1 38  ? -25.942 -2.467  4.022   1.00 10.46 ? 50  ASN   A O   1 
ATOM   291  C  CB  . ASN   A 1 38  ? -26.625 -4.918  2.953   1.00 12.60 ? 50  ASN   A CB  1 
ATOM   292  C  CG  . ASN   A 1 38  ? -25.287 -5.513  3.335   1.00 13.16 ? 50  ASN   A CG  1 
ATOM   293  O  OD1 . ASN   A 1 38  ? -24.260 -5.261  2.695   1.00 12.99 ? 50  ASN   A OD1 1 
ATOM   294  N  ND2 . ASN   A 1 38  ? -25.283 -6.338  4.373   1.00 13.82 ? 50  ASN   A ND2 1 
ATOM   295  N  N   . PHE   A 1 39  ? -25.164 -1.601  2.091   1.00 11.77 ? 51  PHE   A N   1 
ATOM   296  C  CA  . PHE   A 1 39  ? -24.538 -0.446  2.734   1.00 11.75 ? 51  PHE   A CA  1 
ATOM   297  C  C   . PHE   A 1 39  ? -24.703 0.847   1.923   1.00 11.25 ? 51  PHE   A C   1 
ATOM   298  O  O   . PHE   A 1 39  ? -24.448 0.868   0.713   1.00 10.70 ? 51  PHE   A O   1 
ATOM   299  C  CB  . PHE   A 1 39  ? -23.046 -0.691  2.986   1.00 12.59 ? 51  PHE   A CB  1 
ATOM   300  C  CG  . PHE   A 1 39  ? -22.712 -1.382  4.300   1.00 13.50 ? 51  PHE   A CG  1 
ATOM   301  C  CD1 . PHE   A 1 39  ? -22.600 -0.650  5.476   1.00 14.12 ? 51  PHE   A CD1 1 
ATOM   302  C  CD2 . PHE   A 1 39  ? -22.495 -2.754  4.356   1.00 14.40 ? 51  PHE   A CD2 1 
ATOM   303  C  CE1 . PHE   A 1 39  ? -22.279 -1.273  6.672   1.00 14.73 ? 51  PHE   A CE1 1 
ATOM   304  C  CE2 . PHE   A 1 39  ? -22.182 -3.373  5.557   1.00 14.98 ? 51  PHE   A CE2 1 
ATOM   305  C  CZ  . PHE   A 1 39  ? -22.067 -2.631  6.711   1.00 14.63 ? 51  PHE   A CZ  1 
ATOM   306  N  N   . VAL   A 1 40  ? -25.061 1.929   2.646   1.00 10.82 ? 52  VAL   A N   1 
ATOM   307  C  CA  . VAL   A 1 40  ? -25.206 3.284   2.122   1.00 11.03 ? 52  VAL   A CA  1 
ATOM   308  C  C   . VAL   A 1 40  ? -24.272 4.249   2.861   1.00 10.72 ? 52  VAL   A C   1 
ATOM   309  O  O   . VAL   A 1 40  ? -24.266 4.289   4.091   1.00 10.67 ? 52  VAL   A O   1 
ATOM   310  C  CB  . VAL   A 1 40  ? -26.665 3.754   2.272   1.00 11.17 ? 52  VAL   A CB  1 
ATOM   311  C  CG1 . VAL   A 1 40  ? -26.815 5.245   1.994   1.00 11.18 ? 52  VAL   A CG1 1 
ATOM   312  C  CG2 . VAL   A 1 40  ? -27.614 2.938   1.396   1.00 11.30 ? 52  VAL   A CG2 1 
ATOM   313  N  N   . LEU   A 1 41  ? -23.536 5.065   2.089   1.00 10.65 ? 53  LEU   A N   1 
ATOM   314  C  CA  . LEU   A 1 41  ? -22.681 6.128   2.607   1.00 10.96 ? 53  LEU   A CA  1 
ATOM   315  C  C   . LEU   A 1 41  ? -23.438 7.462   2.585   1.00 10.62 ? 53  LEU   A C   1 
ATOM   316  O  O   . LEU   A 1 41  ? -24.136 7.757   1.607   1.00 10.60 ? 53  LEU   A O   1 
ATOM   317  C  CB  . LEU   A 1 41  ? -21.458 6.128   1.680   1.00 11.71 ? 53  LEU   A CB  1 
ATOM   318  C  CG  . LEU   A 1 41  ? -20.164 6.771   2.190   1.00 12.45 ? 53  LEU   A CG  1 
ATOM   319  C  CD1 . LEU   A 1 41  ? -19.700 6.260   3.533   1.00 12.69 ? 53  LEU   A CD1 1 
ATOM   320  C  CD2 . LEU   A 1 41  ? -19.064 6.554   1.159   1.00 12.68 ? 53  LEU   A CD2 1 
ATOM   321  N  N   . THR   A 1 42  ? -23.268 8.274   3.646   1.00 10.15 ? 54  THR   A N   1 
ATOM   322  C  CA  . THR   A 1 42  ? -23.922 9.576   3.801   1.00 9.89  ? 54  THR   A CA  1 
ATOM   323  C  C   . THR   A 1 42  ? -23.132 10.416  4.820   1.00 10.07 ? 54  THR   A C   1 
ATOM   324  O  O   . THR   A 1 42  ? -21.997 10.068  5.158   1.00 10.03 ? 54  THR   A O   1 
ATOM   325  C  CB  . THR   A 1 42  ? -25.386 9.360   4.206   1.00 9.62  ? 54  THR   A CB  1 
ATOM   326  O  OG1 . THR   A 1 42  ? -26.111 10.592  4.209   1.00 9.44  ? 54  THR   A OG1 1 
ATOM   327  C  CG2 . THR   A 1 42  ? -25.514 8.719   5.577   1.00 9.46  ? 54  THR   A CG2 1 
ATOM   328  N  N   . ALA   A 1 43  ? -23.724 11.520  5.313   1.00 9.85  ? 55  ALA   A N   1 
ATOM   329  C  CA  . ALA   A 1 43  ? -23.058 12.409  6.266   1.00 10.10 ? 55  ALA   A CA  1 
ATOM   330  C  C   . ALA   A 1 43  ? -23.459 12.085  7.710   1.00 10.24 ? 55  ALA   A C   1 
ATOM   331  O  O   . ALA   A 1 43  ? -24.607 11.728  7.967   1.00 10.23 ? 55  ALA   A O   1 
ATOM   332  C  CB  . ALA   A 1 43  ? -23.389 13.851  5.927   1.00 9.95  ? 55  ALA   A CB  1 
ATOM   333  N  N   . ALA   A 1 44  ? -22.511 12.246  8.653   1.00 10.13 ? 56  ALA   A N   1 
ATOM   334  C  CA  . ALA   A 1 44  ? -22.731 11.978  10.069  1.00 10.24 ? 56  ALA   A CA  1 
ATOM   335  C  C   . ALA   A 1 44  ? -23.819 12.862  10.681  1.00 10.05 ? 56  ALA   A C   1 
ATOM   336  O  O   . ALA   A 1 44  ? -24.519 12.412  11.586  1.00 10.30 ? 56  ALA   A O   1 
ATOM   337  C  CB  . ALA   A 1 44  ? -21.438 12.138  10.845  1.00 10.70 ? 56  ALA   A CB  1 
ATOM   338  N  N   . HIS   A 1 45  ? -23.975 14.100  10.197  1.00 9.74  ? 57  HIS   A N   1 
ATOM   339  C  CA  . HIS   A 1 45  ? -24.949 15.016  10.768  1.00 9.97  ? 57  HIS   A CA  1 
ATOM   340  C  C   . HIS   A 1 45  ? -26.383 14.629  10.385  1.00 9.97  ? 57  HIS   A C   1 
ATOM   341  O  O   . HIS   A 1 45  ? -27.327 15.206  10.935  1.00 9.53  ? 57  HIS   A O   1 
ATOM   342  C  CB  . HIS   A 1 45  ? -24.589 16.478  10.460  1.00 10.12 ? 57  HIS   A CB  1 
ATOM   343  C  CG  . HIS   A 1 45  ? -24.979 17.016  9.116   1.00 10.41 ? 57  HIS   A CG  1 
ATOM   344  N  ND1 . HIS   A 1 45  ? -24.067 17.258  8.106   1.00 10.04 ? 57  HIS   A ND1 1 
ATOM   345  C  CD2 . HIS   A 1 45  ? -26.167 17.462  8.656   1.00 10.41 ? 57  HIS   A CD2 1 
ATOM   346  C  CE1 . HIS   A 1 45  ? -24.697 17.795  7.070   1.00 10.30 ? 57  HIS   A CE1 1 
ATOM   347  N  NE2 . HIS   A 1 45  ? -25.978 17.926  7.375   1.00 10.18 ? 57  HIS   A NE2 1 
ATOM   348  N  N   . CYS   A 1 46  ? -26.539 13.641  9.482   1.00 9.88  ? 58  CYS   A N   1 
ATOM   349  C  CA  . CYS   A 1 46  ? -27.849 13.128  9.095   1.00 10.08 ? 58  CYS   A CA  1 
ATOM   350  C  C   . CYS   A 1 46  ? -28.317 11.980  10.006  1.00 10.11 ? 58  CYS   A C   1 
ATOM   351  O  O   . CYS   A 1 46  ? -29.345 11.365  9.718   1.00 9.95  ? 58  CYS   A O   1 
ATOM   352  C  CB  . CYS   A 1 46  ? -27.880 12.694  7.623   1.00 10.11 ? 58  CYS   A CB  1 
ATOM   353  S  SG  . CYS   A 1 46  ? -27.516 13.995  6.400   1.00 10.51 ? 58  CYS   A SG  1 
ATOM   354  N  N   . ALA   A 1 47  ? -27.599 11.685  11.108  1.00 10.26 ? 59  ALA   A N   1 
ATOM   355  C  CA  . ALA   A 1 47  ? -27.991 10.619  12.026  1.00 10.35 ? 59  ALA   A CA  1 
ATOM   356  C  C   . ALA   A 1 47  ? -29.274 10.996  12.768  1.00 10.55 ? 59  ALA   A C   1 
ATOM   357  O  O   . ALA   A 1 47  ? -29.590 12.181  12.892  1.00 10.70 ? 59  ALA   A O   1 
ATOM   358  C  CB  . ALA   A 1 47  ? -26.871 10.318  13.013  1.00 10.43 ? 59  ALA   A CB  1 
ATOM   359  N  N   . GLY   A 1 48  ? -30.012 9.979   13.246  1.00 10.81 ? 60  GLY   A N   1 
ATOM   360  C  CA  . GLY   A 1 48  ? -31.226 10.189  14.032  1.00 10.94 ? 60  GLY   A CA  1 
ATOM   361  C  C   . GLY   A 1 48  ? -31.650 8.934   14.808  1.00 11.06 ? 60  GLY   A C   1 
ATOM   362  O  O   . GLY   A 1 48  ? -30.898 7.967   14.892  1.00 10.99 ? 60  GLY   A O   1 
ATOM   363  N  N   . ARG   A 1 49  ? -32.870 8.955   15.362  1.00 11.19 ? 61  ARG   A N   1 
ATOM   364  C  CA  . ARG   A 1 49  ? -33.418 7.820   16.098  1.00 11.70 ? 61  ARG   A CA  1 
ATOM   365  C  C   . ARG   A 1 49  ? -33.723 6.647   15.157  1.00 11.91 ? 61  ARG   A C   1 
ATOM   366  O  O   . ARG   A 1 49  ? -33.458 5.499   15.508  1.00 11.88 ? 61  ARG   A O   1 
ATOM   367  C  CB  . ARG   A 1 49  ? -34.657 8.251   16.894  1.00 11.85 ? 61  ARG   A CB  1 
ATOM   368  C  CG  . ARG   A 1 49  ? -35.284 7.157   17.751  1.00 12.12 ? 61  ARG   A CG  1 
ATOM   369  C  CD  . ARG   A 1 49  ? -34.302 6.434   18.667  1.00 12.15 ? 61  ARG   A CD  1 
ATOM   370  N  NE  . ARG   A 1 49  ? -34.963 5.337   19.387  1.00 12.53 ? 61  ARG   A NE  1 
ATOM   371  C  CZ  . ARG   A 1 49  ? -35.036 4.069   18.969  1.00 12.90 ? 61  ARG   A CZ  1 
ATOM   372  N  NH1 . ARG   A 1 49  ? -34.497 3.714   17.813  1.00 12.71 ? 61  ARG   A NH1 1 
ATOM   373  N  NH2 . ARG   A 1 49  ? -35.665 3.158   19.703  1.00 12.91 ? 61  ARG   A NH2 1 
ATOM   374  N  N   . SER   A 1 50  ? -34.287 6.929   13.972  1.00 12.31 ? 63  SER   A N   1 
ATOM   375  C  CA  . SER   A 1 50  ? -34.487 5.907   12.947  1.00 13.02 ? 63  SER   A CA  1 
ATOM   376  C  C   . SER   A 1 50  ? -34.473 6.535   11.550  1.00 12.69 ? 63  SER   A C   1 
ATOM   377  O  O   . SER   A 1 50  ? -34.764 7.722   11.415  1.00 12.48 ? 63  SER   A O   1 
ATOM   378  C  CB  . SER   A 1 50  ? -35.762 5.118   13.194  1.00 13.81 ? 63  SER   A CB  1 
ATOM   379  O  OG  . SER   A 1 50  ? -36.913 5.948   13.167  1.00 14.82 ? 63  SER   A OG  1 
ATOM   380  N  N   . ILE   A 1 51  ? -34.119 5.727   10.530  1.00 12.39 ? 64  ILE   A N   1 
ATOM   381  C  CA  . ILE   A 1 51  ? -33.968 6.188   9.153   1.00 12.47 ? 64  ILE   A CA  1 
ATOM   382  C  C   . ILE   A 1 51  ? -34.559 5.163   8.177   1.00 12.44 ? 64  ILE   A C   1 
ATOM   383  O  O   . ILE   A 1 51  ? -34.338 3.960   8.322   1.00 11.81 ? 64  ILE   A O   1 
ATOM   384  C  CB  . ILE   A 1 51  ? -32.485 6.461   8.819   1.00 12.49 ? 64  ILE   A CB  1 
ATOM   385  C  CG1 . ILE   A 1 51  ? -31.842 7.477   9.795   1.00 12.71 ? 64  ILE   A CG1 1 
ATOM   386  C  CG2 . ILE   A 1 51  ? -32.344 6.894   7.359   1.00 12.45 ? 64  ILE   A CG2 1 
ATOM   387  C  CD1 . ILE   A 1 51  ? -30.362 7.750   9.555   1.00 13.04 ? 64  ILE   A CD1 1 
ATOM   388  N  N   . THR   A 1 52  ? -35.270 5.670   7.156   1.00 12.74 ? 65  THR   A N   1 
ATOM   389  C  CA  . THR   A 1 52  ? -35.763 4.876   6.035   1.00 13.77 ? 65  THR   A CA  1 
ATOM   390  C  C   . THR   A 1 52  ? -35.064 5.312   4.745   1.00 12.79 ? 65  THR   A C   1 
ATOM   391  O  O   . THR   A 1 52  ? -34.915 6.512   4.499   1.00 12.58 ? 65  THR   A O   1 
ATOM   392  C  CB  . THR   A 1 52  ? -37.280 5.044   5.931   1.00 15.67 ? 65  THR   A CB  1 
ATOM   393  O  OG1 . THR   A 1 52  ? -37.479 6.446   5.778   1.00 20.23 ? 65  THR   A OG1 1 
ATOM   394  C  CG2 . THR   A 1 52  ? -38.011 4.547   7.161   1.00 15.70 ? 65  THR   A CG2 1 
ATOM   395  N  N   . VAL   A 1 53  ? -34.641 4.326   3.933   1.00 12.19 ? 66  VAL   A N   1 
ATOM   396  C  CA  . VAL   A 1 53  ? -33.927 4.549   2.681   1.00 11.99 ? 66  VAL   A CA  1 
ATOM   397  C  C   . VAL   A 1 53  ? -34.834 4.179   1.506   1.00 12.21 ? 66  VAL   A C   1 
ATOM   398  O  O   . VAL   A 1 53  ? -35.379 3.075   1.493   1.00 12.20 ? 66  VAL   A O   1 
ATOM   399  C  CB  . VAL   A 1 53  ? -32.642 3.693   2.681   1.00 12.16 ? 66  VAL   A CB  1 
ATOM   400  C  CG1 . VAL   A 1 53  ? -31.962 3.643   1.310   1.00 12.09 ? 66  VAL   A CG1 1 
ATOM   401  C  CG2 . VAL   A 1 53  ? -31.654 4.159   3.741   1.00 12.14 ? 66  VAL   A CG2 1 
ATOM   402  N  N   . THR   A 1 54  ? -35.009 5.097   0.535   1.00 11.67 ? 67  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 54  ? -35.720 4.774   -0.699  1.00 11.52 ? 67  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 54  ? -34.722 4.779   -1.863  1.00 11.22 ? 67  THR   A C   1 
ATOM   405  O  O   . THR   A 1 54  ? -34.122 5.810   -2.167  1.00 10.62 ? 67  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 54  ? -36.895 5.724   -0.965  1.00 11.79 ? 67  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 54  ? -37.796 5.690   0.140   1.00 11.83 ? 67  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 54  ? -37.688 5.331   -2.202  1.00 11.76 ? 67  THR   A CG2 1 
ATOM   409  N  N   . LEU   A 1 55  ? -34.557 3.608   -2.501  1.00 11.35 ? 68  LEU   A N   1 
ATOM   410  C  CA  . LEU   A 1 55  ? -33.786 3.457   -3.730  1.00 11.48 ? 68  LEU   A CA  1 
ATOM   411  C  C   . LEU   A 1 55  ? -34.743 3.432   -4.927  1.00 11.08 ? 68  LEU   A C   1 
ATOM   412  O  O   . LEU   A 1 55  ? -35.926 3.113   -4.780  1.00 11.12 ? 68  LEU   A O   1 
ATOM   413  C  CB  . LEU   A 1 55  ? -32.943 2.177   -3.681  1.00 11.98 ? 68  LEU   A CB  1 
ATOM   414  C  CG  . LEU   A 1 55  ? -32.023 1.976   -2.471  1.00 12.50 ? 68  LEU   A CG  1 
ATOM   415  C  CD1 . LEU   A 1 55  ? -31.332 0.608   -2.504  1.00 12.50 ? 68  LEU   A CD1 1 
ATOM   416  C  CD2 . LEU   A 1 55  ? -30.976 3.069   -2.356  1.00 13.04 ? 68  LEU   A CD2 1 
ATOM   417  N  N   . GLY   A 1 56  ? -34.221 3.770   -6.115  1.00 10.89 ? 69  GLY   A N   1 
ATOM   418  C  CA  . GLY   A 1 56  ? -34.949 3.644   -7.376  1.00 10.57 ? 69  GLY   A CA  1 
ATOM   419  C  C   . GLY   A 1 56  ? -35.889 4.816   -7.692  1.00 10.66 ? 69  GLY   A C   1 
ATOM   420  O  O   . GLY   A 1 56  ? -36.764 4.669   -8.545  1.00 10.50 ? 69  GLY   A O   1 
ATOM   421  N  N   . ALA   A 1 57  ? -35.718 5.974   -7.029  1.00 10.49 ? 70  ALA   A N   1 
ATOM   422  C  CA  . ALA   A 1 57  ? -36.664 7.074   -7.177  1.00 10.71 ? 70  ALA   A CA  1 
ATOM   423  C  C   . ALA   A 1 57  ? -36.184 8.102   -8.200  1.00 11.15 ? 70  ALA   A C   1 
ATOM   424  O  O   . ALA   A 1 57  ? -34.980 8.258   -8.424  1.00 10.66 ? 70  ALA   A O   1 
ATOM   425  C  CB  . ALA   A 1 57  ? -36.923 7.740   -5.840  1.00 11.03 ? 70  ALA   A CB  1 
ATOM   426  N  N   . HIS   A 1 58  ? -37.162 8.801   -8.803  1.00 11.88 ? 71  HIS   A N   1 
ATOM   427  C  CA  . HIS   A 1 58  ? -36.928 10.029  -9.559  1.00 12.21 ? 71  HIS   A CA  1 
ATOM   428  C  C   . HIS   A 1 58  ? -37.813 11.137  -8.987  1.00 12.04 ? 71  HIS   A C   1 
ATOM   429  O  O   . HIS   A 1 58  ? -37.299 12.010  -8.293  1.00 11.84 ? 71  HIS   A O   1 
ATOM   430  C  CB  . HIS   A 1 58  ? -37.075 9.837   -11.077 1.00 12.70 ? 71  HIS   A CB  1 
ATOM   431  C  CG  . HIS   A 1 58  ? -36.802 11.105  -11.828 1.00 12.62 ? 71  HIS   A CG  1 
ATOM   432  N  ND1 . HIS   A 1 58  ? -35.526 11.627  -11.901 1.00 12.79 ? 71  HIS   A ND1 1 
ATOM   433  C  CD2 . HIS   A 1 58  ? -37.598 11.988  -12.448 1.00 12.80 ? 71  HIS   A CD2 1 
ATOM   434  C  CE1 . HIS   A 1 58  ? -35.556 12.780  -12.553 1.00 12.57 ? 71  HIS   A CE1 1 
ATOM   435  N  NE2 . HIS   A 1 58  ? -36.803 13.022  -12.903 1.00 12.87 ? 71  HIS   A NE2 1 
ATOM   436  N  N   . ASN   A 1 59  ? -39.129 11.091  -9.271  1.00 12.30 ? 72  ASN   A N   1 
ATOM   437  C  CA  . ASN   A 1 59  ? -40.105 11.973  -8.641  1.00 12.76 ? 72  ASN   A CA  1 
ATOM   438  C  C   . ASN   A 1 59  ? -40.591 11.320  -7.352  1.00 13.10 ? 72  ASN   A C   1 
ATOM   439  O  O   . ASN   A 1 59  ? -41.341 10.347  -7.398  1.00 12.49 ? 72  ASN   A O   1 
ATOM   440  C  CB  . ASN   A 1 59  ? -41.310 12.280  -9.532  1.00 13.13 ? 72  ASN   A CB  1 
ATOM   441  C  CG  . ASN   A 1 59  ? -42.213 13.348  -8.949  1.00 13.52 ? 72  ASN   A CG  1 
ATOM   442  O  OD1 . ASN   A 1 59  ? -42.515 13.342  -7.751  1.00 13.41 ? 72  ASN   A OD1 1 
ATOM   443  N  ND2 . ASN   A 1 59  ? -42.650 14.293  -9.766  1.00 14.08 ? 72  ASN   A ND2 1 
ATOM   444  N  N   . ILE   A 1 60  ? -40.200 11.901  -6.209  1.00 13.66 ? 73  ILE   A N   1 
ATOM   445  C  CA  . ILE   A 1 60  ? -40.377 11.275  -4.909  1.00 14.83 ? 73  ILE   A CA  1 
ATOM   446  C  C   . ILE   A 1 60  ? -41.833 11.372  -4.431  1.00 15.17 ? 73  ILE   A C   1 
ATOM   447  O  O   . ILE   A 1 60  ? -42.145 10.835  -3.375  1.00 15.01 ? 73  ILE   A O   1 
ATOM   448  C  CB  . ILE   A 1 60  ? -39.372 11.897  -3.912  1.00 16.77 ? 73  ILE   A CB  1 
ATOM   449  C  CG1 . ILE   A 1 60  ? -39.059 10.962  -2.743  1.00 18.47 ? 73  ILE   A CG1 1 
ATOM   450  C  CG2 . ILE   A 1 60  ? -39.810 13.287  -3.428  1.00 16.20 ? 73  ILE   A CG2 1 
ATOM   451  C  CD1 . ILE   A 1 60  ? -38.223 9.753   -3.128  1.00 19.49 ? 73  ILE   A CD1 1 
ATOM   452  N  N   . THR   A 1 61  ? -42.728 12.034  -5.190  1.00 15.28 ? 74  THR   A N   1 
ATOM   453  C  CA  . THR   A 1 61  ? -44.129 12.150  -4.797  1.00 15.62 ? 74  THR   A CA  1 
ATOM   454  C  C   . THR   A 1 61  ? -44.995 11.078  -5.461  1.00 16.00 ? 74  THR   A C   1 
ATOM   455  O  O   . THR   A 1 61  ? -46.163 10.966  -5.105  1.00 16.29 ? 74  THR   A O   1 
ATOM   456  C  CB  . THR   A 1 61  ? -44.681 13.545  -5.114  1.00 15.96 ? 74  THR   A CB  1 
ATOM   457  O  OG1 . THR   A 1 61  ? -44.760 13.716  -6.526  1.00 15.41 ? 74  THR   A OG1 1 
ATOM   458  C  CG2 . THR   A 1 61  ? -43.845 14.654  -4.500  1.00 16.27 ? 74  THR   A CG2 1 
ATOM   459  N  N   . GLU   A 1 62  ? -44.443 10.300  -6.408  1.00 16.12 ? 75  GLU   A N   1 
ATOM   460  C  CA  . GLU   A 1 62  ? -45.230 9.332   -7.171  1.00 15.87 ? 75  GLU   A CA  1 
ATOM   461  C  C   . GLU   A 1 62  ? -44.634 7.925   -7.064  1.00 15.16 ? 75  GLU   A C   1 
ATOM   462  O  O   . GLU   A 1 62  ? -43.577 7.662   -7.639  1.00 13.77 ? 75  GLU   A O   1 
ATOM   463  C  CB  . GLU   A 1 62  ? -45.292 9.769   -8.636  1.00 17.24 ? 75  GLU   A CB  1 
ATOM   464  C  CG  . GLU   A 1 62  ? -46.360 9.022   -9.432  0.50 17.91 ? 75  GLU   A CG  1 
ATOM   465  C  CD  . GLU   A 1 62  ? -46.336 9.231   -10.936 0.50 18.68 ? 75  GLU   A CD  1 
ATOM   466  O  OE1 . GLU   A 1 62  ? -47.385 8.950   -11.557 0.50 19.12 ? 75  GLU   A OE1 1 
ATOM   467  O  OE2 . GLU   A 1 62  ? -45.289 9.638   -11.492 0.50 19.50 ? 75  GLU   A OE2 1 
ATOM   468  N  N   A GLU   A 1 63  ? -45.343 7.040   -6.342  0.50 14.81 ? 76  GLU   A N   1 
ATOM   469  N  N   B GLU   A 1 63  ? -45.321 7.030   -6.335  0.50 14.78 ? 76  GLU   A N   1 
ATOM   470  C  CA  A GLU   A 1 63  ? -44.959 5.649   -6.129  0.50 15.12 ? 76  GLU   A CA  1 
ATOM   471  C  CA  B GLU   A 1 63  ? -44.830 5.678   -6.101  0.50 15.07 ? 76  GLU   A CA  1 
ATOM   472  C  C   A GLU   A 1 63  ? -44.841 4.909   -7.462  0.50 14.15 ? 76  GLU   A C   1 
ATOM   473  C  C   B GLU   A 1 63  ? -44.849 4.886   -7.410  0.50 14.12 ? 76  GLU   A C   1 
ATOM   474  O  O   A GLU   A 1 63  ? -45.658 5.129   -8.353  0.50 13.51 ? 76  GLU   A O   1 
ATOM   475  O  O   B GLU   A 1 63  ? -45.759 5.046   -8.219  0.50 13.42 ? 76  GLU   A O   1 
ATOM   476  C  CB  A GLU   A 1 63  ? -46.038 5.035   -5.231  0.50 16.16 ? 76  GLU   A CB  1 
ATOM   477  C  CB  B GLU   A 1 63  ? -45.630 4.979   -4.998  0.50 16.09 ? 76  GLU   A CB  1 
ATOM   478  C  CG  A GLU   A 1 63  ? -46.043 3.510   -5.182  0.50 17.09 ? 76  GLU   A CG  1 
ATOM   479  C  CG  B GLU   A 1 63  ? -45.184 3.541   -4.749  0.50 16.99 ? 76  GLU   A CG  1 
ATOM   480  C  CD  A GLU   A 1 63  ? -47.191 2.923   -4.374  0.50 17.96 ? 76  GLU   A CD  1 
ATOM   481  C  CD  B GLU   A 1 63  ? -45.702 2.887   -3.476  0.50 17.88 ? 76  GLU   A CD  1 
ATOM   482  O  OE1 A GLU   A 1 63  ? -47.192 3.053   -3.132  0.50 18.56 ? 76  GLU   A OE1 1 
ATOM   483  O  OE1 B GLU   A 1 63  ? -46.185 3.599   -2.564  0.50 18.59 ? 76  GLU   A OE1 1 
ATOM   484  O  OE2 A GLU   A 1 63  ? -48.110 2.354   -4.995  0.50 19.14 ? 76  GLU   A OE2 1 
ATOM   485  O  OE2 B GLU   A 1 63  ? -45.628 1.642   -3.409  0.50 18.09 ? 76  GLU   A OE2 1 
ATOM   486  N  N   . GLU   A 1 64  ? -43.828 4.033   -7.594  1.00 13.41 ? 77  GLU   A N   1 
ATOM   487  C  CA  . GLU   A 1 64  ? -43.640 3.259   -8.820  1.00 12.36 ? 77  GLU   A CA  1 
ATOM   488  C  C   . GLU   A 1 64  ? -42.889 1.953   -8.540  1.00 11.45 ? 77  GLU   A C   1 
ATOM   489  O  O   . GLU   A 1 64  ? -42.242 1.810   -7.505  1.00 10.92 ? 77  GLU   A O   1 
ATOM   490  C  CB  . GLU   A 1 64  ? -42.935 4.059   -9.924  1.00 12.58 ? 77  GLU   A CB  1 
ATOM   491  C  CG  . GLU   A 1 64  ? -41.621 4.737   -9.529  1.00 12.75 ? 77  GLU   A CG  1 
ATOM   492  C  CD  . GLU   A 1 64  ? -40.802 5.345   -10.673 1.00 12.89 ? 77  GLU   A CD  1 
ATOM   493  O  OE1 . GLU   A 1 64  ? -39.997 6.285   -10.413 1.00 12.35 ? 77  GLU   A OE1 1 
ATOM   494  O  OE2 . GLU   A 1 64  ? -40.941 4.869   -11.828 1.00 12.73 ? 77  GLU   A OE2 1 
ATOM   495  N  N   . ASP   A 1 65  ? -42.945 1.013   -9.498  1.00 10.63 ? 78  ASP   A N   1 
ATOM   496  C  CA  . ASP   A 1 65  ? -42.397 -0.329  -9.320  1.00 10.36 ? 78  ASP   A CA  1 
ATOM   497  C  C   . ASP   A 1 65  ? -40.878 -0.304  -9.091  1.00 9.72  ? 78  ASP   A C   1 
ATOM   498  O  O   . ASP   A 1 65  ? -40.349 -1.225  -8.474  1.00 9.14  ? 78  ASP   A O   1 
ATOM   499  C  CB  . ASP   A 1 65  ? -42.777 -1.269  -10.464 1.00 10.42 ? 78  ASP   A CB  1 
ATOM   500  C  CG  . ASP   A 1 65  ? -44.180 -1.878  -10.453 1.00 10.93 ? 78  ASP   A CG  1 
ATOM   501  O  OD1 . ASP   A 1 65  ? -44.496 -2.645  -11.406 1.00 10.87 ? 78  ASP   A OD1 1 
ATOM   502  O  OD2 . ASP   A 1 65  ? -44.953 -1.620  -9.496  1.00 10.92 ? 78  ASP   A OD2 1 
ATOM   503  N  N   . THR   A 1 66  ? -40.168 0.719   -9.595  1.00 9.76  ? 79  THR   A N   1 
ATOM   504  C  CA  . THR   A 1 66  ? -38.723 0.826   -9.395  1.00 9.91  ? 79  THR   A CA  1 
ATOM   505  C  C   . THR   A 1 66  ? -38.379 1.053   -7.917  1.00 9.97  ? 79  THR   A C   1 
ATOM   506  O  O   . THR   A 1 66  ? -37.246 0.767   -7.521  1.00 9.86  ? 79  THR   A O   1 
ATOM   507  C  CB  . THR   A 1 66  ? -38.082 1.926   -10.258 1.00 9.82  ? 79  THR   A CB  1 
ATOM   508  O  OG1 . THR   A 1 66  ? -38.704 3.178   -9.993  1.00 9.39  ? 79  THR   A OG1 1 
ATOM   509  C  CG2 . THR   A 1 66  ? -38.159 1.665   -11.751 1.00 10.00 ? 79  THR   A CG2 1 
ATOM   510  N  N   . TRP   A 1 67  ? -39.313 1.600   -7.108  1.00 10.25 ? 80  TRP   A N   1 
ATOM   511  C  CA  . TRP   A 1 67  ? -39.024 1.914   -5.711  1.00 10.68 ? 80  TRP   A CA  1 
ATOM   512  C  C   . TRP   A 1 67  ? -38.652 0.661   -4.918  1.00 10.75 ? 80  TRP   A C   1 
ATOM   513  O  O   . TRP   A 1 67  ? -39.336 -0.359  -5.005  1.00 10.40 ? 80  TRP   A O   1 
ATOM   514  C  CB  . TRP   A 1 67  ? -40.209 2.601   -5.009  1.00 11.05 ? 80  TRP   A CB  1 
ATOM   515  C  CG  . TRP   A 1 67  ? -40.416 4.064   -5.302  1.00 11.21 ? 80  TRP   A CG  1 
ATOM   516  C  CD1 . TRP   A 1 67  ? -39.889 4.821   -6.309  1.00 11.34 ? 80  TRP   A CD1 1 
ATOM   517  C  CD2 . TRP   A 1 67  ? -41.280 4.948   -4.554  1.00 11.58 ? 80  TRP   A CD2 1 
ATOM   518  N  NE1 . TRP   A 1 67  ? -40.346 6.112   -6.229  1.00 11.24 ? 80  TRP   A NE1 1 
ATOM   519  C  CE2 . TRP   A 1 67  ? -41.207 6.217   -5.168  1.00 11.97 ? 80  TRP   A CE2 1 
ATOM   520  C  CE3 . TRP   A 1 67  ? -42.106 4.788   -3.436  1.00 12.19 ? 80  TRP   A CE3 1 
ATOM   521  C  CZ2 . TRP   A 1 67  ? -41.929 7.314   -4.694  1.00 12.45 ? 80  TRP   A CZ2 1 
ATOM   522  C  CZ3 . TRP   A 1 67  ? -42.818 5.873   -2.966  1.00 12.78 ? 80  TRP   A CZ3 1 
ATOM   523  C  CH2 . TRP   A 1 67  ? -42.730 7.119   -3.592  1.00 12.62 ? 80  TRP   A CH2 1 
ATOM   524  N  N   . GLN   A 1 68  ? -37.595 0.789   -4.101  1.00 11.02 ? 81  GLN   A N   1 
ATOM   525  C  CA  . GLN   A 1 68  ? -37.293 -0.131  -3.013  1.00 11.70 ? 81  GLN   A CA  1 
ATOM   526  C  C   . GLN   A 1 68  ? -37.188 0.662   -1.705  1.00 11.93 ? 81  GLN   A C   1 
ATOM   527  O  O   . GLN   A 1 68  ? -36.244 1.434   -1.508  1.00 10.95 ? 81  GLN   A O   1 
ATOM   528  C  CB  . GLN   A 1 68  ? -36.000 -0.908  -3.271  1.00 12.20 ? 81  GLN   A CB  1 
ATOM   529  C  CG  . GLN   A 1 68  ? -36.071 -1.865  -4.459  1.00 12.90 ? 81  GLN   A CG  1 
ATOM   530  C  CD  . GLN   A 1 68  ? -34.797 -2.663  -4.669  1.00 13.22 ? 81  GLN   A CD  1 
ATOM   531  O  OE1 . GLN   A 1 68  ? -34.296 -3.320  -3.751  1.00 13.38 ? 81  GLN   A OE1 1 
ATOM   532  N  NE2 . GLN   A 1 68  ? -34.263 -2.628  -5.884  1.00 13.40 ? 81  GLN   A NE2 1 
ATOM   533  N  N   . LYS   A 1 69  ? -38.179 0.483   -0.821  1.00 12.35 ? 82  LYS   A N   1 
ATOM   534  C  CA  . LYS   A 1 69  ? -38.191 1.127   0.486   1.00 13.31 ? 82  LYS   A CA  1 
ATOM   535  C  C   . LYS   A 1 69  ? -37.567 0.190   1.520   1.00 13.87 ? 82  LYS   A C   1 
ATOM   536  O  O   . LYS   A 1 69  ? -38.163 -0.835  1.850   1.00 14.32 ? 82  LYS   A O   1 
ATOM   537  C  CB  . LYS   A 1 69  ? -39.634 1.449   0.888   1.00 14.04 ? 82  LYS   A CB  1 
ATOM   538  C  CG  . LYS   A 1 69  ? -40.351 2.441   -0.014  1.00 14.78 ? 82  LYS   A CG  1 
ATOM   539  C  CD  . LYS   A 1 69  ? -41.780 2.788   0.395   0.50 15.10 ? 82  LYS   A CD  1 
ATOM   540  C  CE  . LYS   A 1 69  ? -41.874 3.398   1.751   0.10 15.25 ? 82  LYS   A CE  1 
ATOM   541  N  NZ  . LYS   A 1 69  ? -43.231 3.866   2.042   0.10 15.40 ? 82  LYS   A NZ  1 
ATOM   542  N  N   . LEU   A 1 70  ? -36.384 0.540   2.046   1.00 13.48 ? 83  LEU   A N   1 
ATOM   543  C  CA  . LEU   A 1 70  ? -35.587 -0.425  2.791   1.00 14.26 ? 83  LEU   A CA  1 
ATOM   544  C  C   . LEU   A 1 70  ? -35.311 0.022   4.230   1.00 14.05 ? 83  LEU   A C   1 
ATOM   545  O  O   . LEU   A 1 70  ? -34.976 1.176   4.487   1.00 13.55 ? 83  LEU   A O   1 
ATOM   546  C  CB  . LEU   A 1 70  ? -34.293 -0.671  2.019   1.00 15.15 ? 83  LEU   A CB  1 
ATOM   547  C  CG  . LEU   A 1 70  ? -34.449 -1.301  0.632   1.00 15.83 ? 83  LEU   A CG  1 
ATOM   548  C  CD1 . LEU   A 1 70  ? -33.125 -1.306  -0.089  1.00 16.33 ? 83  LEU   A CD1 1 
ATOM   549  C  CD2 . LEU   A 1 70  ? -35.014 -2.714  0.704   1.00 17.20 ? 83  LEU   A CD2 1 
ATOM   550  N  N   . GLU   A 1 71  ? -35.395 -0.951  5.150   1.00 13.66 ? 84  GLU   A N   1 
ATOM   551  C  CA  . GLU   A 1 71  ? -35.149 -0.763  6.573   1.00 13.48 ? 84  GLU   A CA  1 
ATOM   552  C  C   . GLU   A 1 71  ? -33.647 -0.679  6.855   1.00 12.76 ? 84  GLU   A C   1 
ATOM   553  O  O   . GLU   A 1 71  ? -32.870 -1.432  6.272   1.00 12.33 ? 84  GLU   A O   1 
ATOM   554  C  CB  . GLU   A 1 71  ? -35.759 -1.978  7.283   1.00 13.90 ? 84  GLU   A CB  1 
ATOM   555  C  CG  . GLU   A 1 71  ? -35.655 -1.959  8.805   1.00 14.35 ? 84  GLU   A CG  1 
ATOM   556  C  CD  . GLU   A 1 71  ? -35.985 -3.314  9.427   1.00 15.03 ? 84  GLU   A CD  1 
ATOM   557  O  OE1 . GLU   A 1 71  ? -36.864 -4.036  8.887   1.00 15.56 ? 84  GLU   A OE1 1 
ATOM   558  O  OE2 . GLU   A 1 71  ? -35.361 -3.658  10.450  1.00 13.96 ? 84  GLU   A OE2 1 
ATOM   559  N  N   . VAL   A 1 72  ? -33.263 0.222   7.778   1.00 12.07 ? 85  VAL   A N   1 
ATOM   560  C  CA  . VAL   A 1 72  ? -31.897 0.338   8.286   1.00 12.19 ? 85  VAL   A CA  1 
ATOM   561  C  C   . VAL   A 1 72  ? -31.801 -0.412  9.620   1.00 12.04 ? 85  VAL   A C   1 
ATOM   562  O  O   . VAL   A 1 72  ? -32.580 -0.129  10.522  1.00 11.28 ? 85  VAL   A O   1 
ATOM   563  C  CB  . VAL   A 1 72  ? -31.537 1.830   8.469   1.00 12.25 ? 85  VAL   A CB  1 
ATOM   564  C  CG1 . VAL   A 1 72  ? -30.191 2.034   9.164   1.00 12.30 ? 85  VAL   A CG1 1 
ATOM   565  C  CG2 . VAL   A 1 72  ? -31.565 2.603   7.153   1.00 12.23 ? 85  VAL   A CG2 1 
ATOM   566  N  N   . ILE   A 1 73  ? -30.833 -1.331  9.765   1.00 12.30 ? 86  ILE   A N   1 
ATOM   567  C  CA  . ILE   A 1 73  ? -30.653 -2.065  11.017  1.00 13.19 ? 86  ILE   A CA  1 
ATOM   568  C  C   . ILE   A 1 73  ? -29.750 -1.301  11.997  1.00 13.09 ? 86  ILE   A C   1 
ATOM   569  O  O   . ILE   A 1 73  ? -30.029 -1.317  13.196  1.00 13.51 ? 86  ILE   A O   1 
ATOM   570  C  CB  . ILE   A 1 73  ? -30.155 -3.512  10.795  1.00 14.25 ? 86  ILE   A CB  1 
ATOM   571  C  CG1 . ILE   A 1 73  ? -30.103 -4.277  12.122  1.00 15.13 ? 86  ILE   A CG1 1 
ATOM   572  C  CG2 . ILE   A 1 73  ? -28.805 -3.567  10.074  1.00 14.42 ? 86  ILE   A CG2 1 
ATOM   573  C  CD1 . ILE   A 1 73  ? -29.806 -5.763  12.004  1.00 15.64 ? 86  ILE   A CD1 1 
ATOM   574  N  N   . LYS   A 1 74  ? -28.676 -0.647  11.518  1.00 12.54 ? 87  LYS   A N   1 
ATOM   575  C  CA  . LYS   A 1 74  ? -27.731 0.027   12.402  1.00 13.13 ? 87  LYS   A CA  1 
ATOM   576  C  C   . LYS   A 1 74  ? -27.028 1.188   11.690  1.00 12.73 ? 87  LYS   A C   1 
ATOM   577  O  O   . LYS   A 1 74  ? -26.757 1.102   10.493  1.00 11.75 ? 87  LYS   A O   1 
ATOM   578  C  CB  . LYS   A 1 74  ? -26.733 -1.031  12.894  1.00 14.03 ? 87  LYS   A CB  1 
ATOM   579  C  CG  . LYS   A 1 74  ? -25.670 -0.610  13.904  0.50 14.63 ? 87  LYS   A CG  1 
ATOM   580  C  CD  . LYS   A 1 74  ? -24.936 -1.824  14.469  0.50 15.40 ? 87  LYS   A CD  1 
ATOM   581  C  CE  . LYS   A 1 74  ? -23.801 -1.503  15.388  0.50 16.15 ? 87  LYS   A CE  1 
ATOM   582  N  NZ  . LYS   A 1 74  ? -24.251 -0.786  16.581  0.50 16.64 ? 87  LYS   A NZ  1 
ATOM   583  N  N   . GLN   A 1 75  ? -26.731 2.256   12.458  1.00 12.66 ? 88  GLN   A N   1 
ATOM   584  C  CA  . GLN   A 1 75  ? -26.003 3.440   11.999  1.00 12.72 ? 88  GLN   A CA  1 
ATOM   585  C  C   . GLN   A 1 75  ? -24.576 3.447   12.565  1.00 13.20 ? 88  GLN   A C   1 
ATOM   586  O  O   . GLN   A 1 75  ? -24.390 3.325   13.772  1.00 12.66 ? 88  GLN   A O   1 
ATOM   587  C  CB  . GLN   A 1 75  ? -26.715 4.720   12.456  1.00 12.56 ? 88  GLN   A CB  1 
ATOM   588  C  CG  . GLN   A 1 75  ? -28.179 4.833   12.032  1.00 12.65 ? 88  GLN   A CG  1 
ATOM   589  C  CD  . GLN   A 1 75  ? -28.939 5.936   12.747  1.00 12.94 ? 88  GLN   A CD  1 
ATOM   590  O  OE1 . GLN   A 1 75  ? -28.557 7.114   12.714  1.00 12.58 ? 88  GLN   A OE1 1 
ATOM   591  N  NE2 . GLN   A 1 75  ? -30.050 5.580   13.382  1.00 12.72 ? 88  GLN   A NE2 1 
ATOM   592  N  N   . PHE   A 1 76  ? -23.574 3.635   11.687  1.00 13.93 ? 89  PHE   A N   1 
ATOM   593  C  CA  . PHE   A 1 76  ? -22.162 3.665   12.055  1.00 14.82 ? 89  PHE   A CA  1 
ATOM   594  C  C   . PHE   A 1 76  ? -21.581 5.058   11.803  1.00 15.79 ? 89  PHE   A C   1 
ATOM   595  O  O   . PHE   A 1 76  ? -20.992 5.311   10.755  1.00 15.33 ? 89  PHE   A O   1 
ATOM   596  C  CB  . PHE   A 1 76  ? -21.345 2.646   11.249  1.00 14.77 ? 89  PHE   A CB  1 
ATOM   597  C  CG  . PHE   A 1 76  ? -21.653 1.177   11.510  1.00 15.48 ? 89  PHE   A CG  1 
ATOM   598  C  CD1 . PHE   A 1 76  ? -22.610 0.499   10.758  1.00 15.53 ? 89  PHE   A CD1 1 
ATOM   599  C  CD2 . PHE   A 1 76  ? -20.976 0.473   12.507  1.00 16.13 ? 89  PHE   A CD2 1 
ATOM   600  C  CE1 . PHE   A 1 76  ? -22.884 -0.840  10.999  1.00 16.17 ? 89  PHE   A CE1 1 
ATOM   601  C  CE2 . PHE   A 1 76  ? -21.252 -0.872  12.743  1.00 16.44 ? 89  PHE   A CE2 1 
ATOM   602  C  CZ  . PHE   A 1 76  ? -22.205 -1.526  11.990  1.00 16.39 ? 89  PHE   A CZ  1 
ATOM   603  N  N   . ARG   A 1 77  ? -21.747 5.953   12.780  1.00 17.14 ? 90  ARG   A N   1 
ATOM   604  C  CA  . ARG   A 1 77  ? -21.231 7.310   12.708  1.00 19.59 ? 90  ARG   A CA  1 
ATOM   605  C  C   . ARG   A 1 77  ? -19.728 7.282   12.982  1.00 19.71 ? 90  ARG   A C   1 
ATOM   606  O  O   . ARG   A 1 77  ? -19.256 6.485   13.796  1.00 21.21 ? 90  ARG   A O   1 
ATOM   607  C  CB  . ARG   A 1 77  ? -22.040 8.147   13.707  1.00 22.04 ? 90  ARG   A CB  1 
ATOM   608  C  CG  . ARG   A 1 77  ? -22.051 9.647   13.457  1.00 25.07 ? 90  ARG   A CG  1 
ATOM   609  C  CD  . ARG   A 1 77  ? -22.984 10.407  14.399  1.00 27.41 ? 90  ARG   A CD  1 
ATOM   610  N  NE  . ARG   A 1 77  ? -22.633 10.224  15.813  1.00 30.42 ? 90  ARG   A NE  1 
ATOM   611  C  CZ  . ARG   A 1 77  ? -23.069 10.964  16.829  1.00 33.04 ? 90  ARG   A CZ  1 
ATOM   612  N  NH1 . ARG   A 1 77  ? -23.744 12.081  16.611  1.00 32.87 ? 90  ARG   A NH1 1 
ATOM   613  N  NH2 . ARG   A 1 77  ? -22.794 10.597  18.070  1.00 34.39 ? 90  ARG   A NH2 1 
ATOM   614  N  N   . HIS   A 1 78  ? -18.961 8.130   12.284  1.00 19.20 ? 91  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 78  ? -17.517 8.147   12.470  1.00 19.51 ? 91  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 78  ? -17.206 8.475   13.931  1.00 18.90 ? 91  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 78  ? -17.769 9.414   14.489  1.00 17.88 ? 91  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 78  ? -16.828 9.132   11.518  1.00 20.01 ? 91  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 78  ? -15.355 8.915   11.415  1.00 20.93 ? 91  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 78  ? -14.449 9.393   12.339  1.00 21.68 ? 91  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 78  ? -14.633 8.249   10.501  1.00 21.41 ? 91  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 78  ? -13.223 9.031   11.981  1.00 21.56 ? 91  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 78  ? -13.310 8.343   10.860  1.00 21.74 ? 91  HIS   A NE2 1 
ATOM   624  N  N   . PRO   A 1 79  ? -16.318 7.710   14.609  1.00 20.49 ? 92  PRO   A N   1 
ATOM   625  C  CA  . PRO   A 1 79  ? -16.083 7.912   16.042  1.00 21.67 ? 92  PRO   A CA  1 
ATOM   626  C  C   . PRO   A 1 79  ? -15.444 9.247   16.440  1.00 23.01 ? 92  PRO   A C   1 
ATOM   627  O  O   . PRO   A 1 79  ? -15.517 9.631   17.605  1.00 24.28 ? 92  PRO   A O   1 
ATOM   628  C  CB  . PRO   A 1 79  ? -15.211 6.699   16.439  1.00 21.17 ? 92  PRO   A CB  1 
ATOM   629  C  CG  . PRO   A 1 79  ? -14.536 6.265   15.159  1.00 21.44 ? 92  PRO   A CG  1 
ATOM   630  C  CD  . PRO   A 1 79  ? -15.528 6.599   14.050  1.00 21.12 ? 92  PRO   A CD  1 
ATOM   631  N  N   . LYS   A 1 80  ? -14.867 9.973   15.470  1.00 23.77 ? 93  LYS   A N   1 
ATOM   632  C  CA  . LYS   A 1 80  ? -14.225 11.255  15.731  1.00 24.17 ? 93  LYS   A CA  1 
ATOM   633  C  C   . LYS   A 1 80  ? -15.057 12.430  15.201  1.00 23.18 ? 93  LYS   A C   1 
ATOM   634  O  O   . LYS   A 1 80  ? -14.554 13.549  15.156  1.00 21.08 ? 93  LYS   A O   1 
ATOM   635  C  CB  . LYS   A 1 80  ? -12.830 11.285  15.093  1.00 25.68 ? 93  LYS   A CB  1 
ATOM   636  C  CG  . LYS   A 1 80  ? -11.834 10.278  15.649  1.00 27.47 ? 93  LYS   A CG  1 
ATOM   637  C  CD  . LYS   A 1 80  ? -10.512 10.269  14.887  1.00 29.46 ? 93  LYS   A CD  1 
ATOM   638  C  CE  . LYS   A 1 80  ? -9.463  9.425   15.540  0.50 29.72 ? 93  LYS   A CE  1 
ATOM   639  N  NZ  . LYS   A 1 80  ? -8.180  9.554   14.849  0.50 30.07 ? 93  LYS   A NZ  1 
ATOM   640  N  N   . TYR   A 1 81  ? -16.325 12.194  14.821  1.00 21.51 ? 94  TYR   A N   1 
ATOM   641  C  CA  . TYR   A 1 81  ? -17.191 13.268  14.352  1.00 19.72 ? 94  TYR   A CA  1 
ATOM   642  C  C   . TYR   A 1 81  ? -17.345 14.310  15.462  1.00 20.68 ? 94  TYR   A C   1 
ATOM   643  O  O   . TYR   A 1 81  ? -17.596 13.958  16.616  1.00 20.75 ? 94  TYR   A O   1 
ATOM   644  C  CB  . TYR   A 1 81  ? -18.550 12.729  13.882  1.00 18.61 ? 94  TYR   A CB  1 
ATOM   645  C  CG  . TYR   A 1 81  ? -19.595 13.802  13.602  1.00 17.50 ? 94  TYR   A CG  1 
ATOM   646  C  CD1 . TYR   A 1 81  ? -19.388 14.756  12.614  1.00 17.32 ? 94  TYR   A CD1 1 
ATOM   647  C  CD2 . TYR   A 1 81  ? -20.791 13.852  14.306  1.00 16.92 ? 94  TYR   A CD2 1 
ATOM   648  C  CE1 . TYR   A 1 81  ? -20.327 15.739  12.349  1.00 17.47 ? 94  TYR   A CE1 1 
ATOM   649  C  CE2 . TYR   A 1 81  ? -21.740 14.829  14.051  1.00 17.19 ? 94  TYR   A CE2 1 
ATOM   650  C  CZ  . TYR   A 1 81  ? -21.505 15.778  13.072  1.00 17.29 ? 94  TYR   A CZ  1 
ATOM   651  O  OH  . TYR   A 1 81  ? -22.417 16.757  12.803  1.00 18.50 ? 94  TYR   A OH  1 
ATOM   652  N  N   . ASN   A 1 82  ? -17.184 15.592  15.095  1.00 20.18 ? 95  ASN   A N   1 
ATOM   653  C  CA  . ASN   A 1 82  ? -17.218 16.704  16.030  1.00 20.69 ? 95  ASN   A CA  1 
ATOM   654  C  C   . ASN   A 1 82  ? -18.320 17.673  15.611  1.00 20.84 ? 95  ASN   A C   1 
ATOM   655  O  O   . ASN   A 1 82  ? -18.269 18.218  14.515  1.00 20.35 ? 95  ASN   A O   1 
ATOM   656  C  CB  . ASN   A 1 82  ? -15.873 17.426  16.070  1.00 21.66 ? 95  ASN   A CB  1 
ATOM   657  C  CG  . ASN   A 1 82  ? -15.806 18.489  17.141  1.00 22.85 ? 95  ASN   A CG  1 
ATOM   658  O  OD1 . ASN   A 1 82  ? -16.622 19.419  17.162  1.00 23.41 ? 95  ASN   A OD1 1 
ATOM   659  N  ND2 . ASN   A 1 82  ? -14.835 18.380  18.035  1.00 23.98 ? 95  ASN   A ND2 1 
ATOM   660  N  N   . THR   A 1 83  ? -19.273 17.934  16.513  1.00 21.90 ? 96  THR   A N   1 
ATOM   661  C  CA  . THR   A 1 83  ? -20.454 18.719  16.181  1.00 23.17 ? 96  THR   A CA  1 
ATOM   662  C  C   . THR   A 1 83  ? -20.145 20.217  16.165  1.00 23.57 ? 96  THR   A C   1 
ATOM   663  O  O   . THR   A 1 83  ? -20.975 20.987  15.686  1.00 23.93 ? 96  THR   A O   1 
ATOM   664  C  CB  . THR   A 1 83  ? -21.585 18.393  17.156  1.00 24.20 ? 96  THR   A CB  1 
ATOM   665  O  OG1 . THR   A 1 83  ? -21.119 18.785  18.444  1.00 25.41 ? 96  THR   A OG1 1 
ATOM   666  C  CG2 . THR   A 1 83  ? -21.946 16.918  17.139  1.00 23.85 ? 96  THR   A CG2 1 
ATOM   667  N  N   . SER   A 1 84  ? -18.974 20.621  16.690  1.00 23.02 ? 97  SER   A N   1 
ATOM   668  C  CA  . SER   A 1 84  ? -18.529 22.009  16.647  1.00 23.40 ? 97  SER   A CA  1 
ATOM   669  C  C   . SER   A 1 84  ? -17.809 22.335  15.333  1.00 21.34 ? 97  SER   A C   1 
ATOM   670  O  O   . SER   A 1 84  ? -18.194 23.287  14.655  1.00 22.38 ? 97  SER   A O   1 
ATOM   671  C  CB  . SER   A 1 84  ? -17.646 22.356  17.840  1.00 24.18 ? 97  SER   A CB  1 
ATOM   672  O  OG  . SER   A 1 84  ? -18.390 22.398  19.050  0.50 24.47 ? 97  SER   A OG  1 
ATOM   673  N  N   . THR   A 1 85  ? -16.748 21.583  15.003  1.00 19.83 ? 98  THR   A N   1 
ATOM   674  C  CA  . THR   A 1 85  ? -15.907 21.874  13.841  1.00 19.43 ? 98  THR   A CA  1 
ATOM   675  C  C   . THR   A 1 85  ? -16.472 21.250  12.559  1.00 18.86 ? 98  THR   A C   1 
ATOM   676  O  O   . THR   A 1 85  ? -16.112 21.680  11.464  1.00 18.46 ? 98  THR   A O   1 
ATOM   677  C  CB  . THR   A 1 85  ? -14.476 21.387  14.078  1.00 19.43 ? 98  THR   A CB  1 
ATOM   678  O  OG1 . THR   A 1 85  ? -14.528 19.973  14.239  1.00 18.83 ? 98  THR   A OG1 1 
ATOM   679  C  CG2 . THR   A 1 85  ? -13.821 22.027  15.293  1.00 20.17 ? 98  THR   A CG2 1 
ATOM   680  N  N   . LEU   A 1 86  ? -17.293 20.197  12.710  1.00 18.26 ? 99  LEU   A N   1 
ATOM   681  C  CA  . LEU   A 1 86  ? -17.868 19.420  11.617  1.00 18.25 ? 99  LEU   A CA  1 
ATOM   682  C  C   . LEU   A 1 86  ? -16.805 18.596  10.880  1.00 17.85 ? 99  LEU   A C   1 
ATOM   683  O  O   . LEU   A 1 86  ? -17.069 18.083  9.793   1.00 17.34 ? 99  LEU   A O   1 
ATOM   684  C  CB  . LEU   A 1 86  ? -18.681 20.293  10.656  1.00 18.61 ? 99  LEU   A CB  1 
ATOM   685  C  CG  . LEU   A 1 86  ? -19.832 21.090  11.280  1.00 19.14 ? 99  LEU   A CG  1 
ATOM   686  C  CD1 . LEU   A 1 86  ? -20.552 21.904  10.221  1.00 19.85 ? 99  LEU   A CD1 1 
ATOM   687  C  CD2 . LEU   A 1 86  ? -20.819 20.194  12.002  1.00 19.03 ? 99  LEU   A CD2 1 
ATOM   688  N  N   . HIS   A 1 87  ? -15.628 18.396  11.493  1.00 17.99 ? 100 HIS   A N   1 
ATOM   689  C  CA  . HIS   A 1 87  ? -14.653 17.446  10.973  1.00 18.18 ? 100 HIS   A CA  1 
ATOM   690  C  C   . HIS   A 1 87  ? -15.212 16.019  11.047  1.00 16.90 ? 100 HIS   A C   1 
ATOM   691  O  O   . HIS   A 1 87  ? -15.954 15.688  11.971  1.00 16.58 ? 100 HIS   A O   1 
ATOM   692  C  CB  . HIS   A 1 87  ? -13.321 17.554  11.728  1.00 19.86 ? 100 HIS   A CB  1 
ATOM   693  C  CG  . HIS   A 1 87  ? -12.556 18.818  11.467  1.00 21.69 ? 100 HIS   A CG  1 
ATOM   694  N  ND1 . HIS   A 1 87  ? -11.432 19.172  12.186  1.00 22.15 ? 100 HIS   A ND1 1 
ATOM   695  C  CD2 . HIS   A 1 87  ? -12.731 19.789  10.552  1.00 22.62 ? 100 HIS   A CD2 1 
ATOM   696  C  CE1 . HIS   A 1 87  ? -10.959 20.323  11.718  1.00 22.97 ? 100 HIS   A CE1 1 
ATOM   697  N  NE2 . HIS   A 1 87  ? -11.729 20.718  10.725  1.00 22.54 ? 100 HIS   A NE2 1 
ATOM   698  N  N   . HIS   A 1 88  ? -14.858 15.195  10.048  1.00 16.04 ? 101 HIS   A N   1 
ATOM   699  C  CA  . HIS   A 1 88  ? -15.193 13.777  9.993   1.00 16.39 ? 101 HIS   A CA  1 
ATOM   700  C  C   . HIS   A 1 88  ? -16.708 13.585  9.868   1.00 15.12 ? 101 HIS   A C   1 
ATOM   701  O  O   . HIS   A 1 88  ? -17.285 12.735  10.545  1.00 14.61 ? 101 HIS   A O   1 
ATOM   702  C  CB  . HIS   A 1 88  ? -14.573 13.006  11.173  1.00 17.15 ? 101 HIS   A CB  1 
ATOM   703  C  CG  . HIS   A 1 88  ? -13.120 13.303  11.424  1.00 19.05 ? 101 HIS   A CG  1 
ATOM   704  N  ND1 . HIS   A 1 88  ? -12.682 13.992  12.536  1.00 20.52 ? 101 HIS   A ND1 1 
ATOM   705  C  CD2 . HIS   A 1 88  ? -12.012 12.997  10.730  1.00 20.91 ? 101 HIS   A CD2 1 
ATOM   706  C  CE1 . HIS   A 1 88  ? -11.365 14.113  12.491  1.00 20.31 ? 101 HIS   A CE1 1 
ATOM   707  N  NE2 . HIS   A 1 88  ? -10.932 13.524  11.401  1.00 21.42 ? 101 HIS   A NE2 1 
ATOM   708  N  N   . ASP   A 1 89  ? -17.338 14.347  8.959   1.00 13.97 ? 102 ASP   A N   1 
ATOM   709  C  CA  . ASP   A 1 89  ? -18.779 14.283  8.757   1.00 13.26 ? 102 ASP   A CA  1 
ATOM   710  C  C   . ASP   A 1 89  ? -19.118 13.145  7.790   1.00 12.62 ? 102 ASP   A C   1 
ATOM   711  O  O   . ASP   A 1 89  ? -19.517 13.400  6.651   1.00 12.66 ? 102 ASP   A O   1 
ATOM   712  C  CB  . ASP   A 1 89  ? -19.318 15.634  8.302   1.00 13.04 ? 102 ASP   A CB  1 
ATOM   713  C  CG  . ASP   A 1 89  ? -20.835 15.778  8.289   1.00 12.75 ? 102 ASP   A CG  1 
ATOM   714  O  OD1 . ASP   A 1 89  ? -21.527 14.888  8.850   1.00 12.39 ? 102 ASP   A OD1 1 
ATOM   715  O  OD2 . ASP   A 1 89  ? -21.317 16.781  7.718   1.00 11.85 ? 102 ASP   A OD2 1 
ATOM   716  N  N   . ILE   A 1 90  ? -18.988 11.889  8.259   1.00 11.99 ? 103 ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 90  ? -19.216 10.712  7.429   1.00 11.94 ? 103 ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 90  ? -19.865 9.597   8.265   1.00 11.90 ? 103 ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 90  ? -19.562 9.461   9.456   1.00 11.58 ? 103 ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 90  ? -17.889 10.281  6.768   1.00 12.46 ? 103 ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 90  ? -18.093 9.174   5.733   1.00 12.81 ? 103 ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 90  ? -16.845 9.885   7.816   1.00 12.27 ? 103 ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 90  ? -16.915 8.971   4.792   1.00 13.43 ? 103 ILE   A CD1 1 
ATOM   724  N  N   . MET   A 1 91  ? -20.761 8.810   7.636   1.00 11.89 ? 104 MET   A N   1 
ATOM   725  C  CA  . MET   A 1 91  ? -21.508 7.734   8.293   1.00 11.77 ? 104 MET   A CA  1 
ATOM   726  C  C   . MET   A 1 91  ? -21.889 6.639   7.282   1.00 11.99 ? 104 MET   A C   1 
ATOM   727  O  O   . MET   A 1 91  ? -22.203 6.937   6.123   1.00 11.71 ? 104 MET   A O   1 
ATOM   728  C  CB  . MET   A 1 91  ? -22.766 8.296   8.978   1.00 11.86 ? 104 MET   A CB  1 
ATOM   729  C  CG  . MET   A 1 91  ? -23.761 7.253   9.499   1.00 11.49 ? 104 MET   A CG  1 
ATOM   730  S  SD  . MET   A 1 91  ? -25.109 7.932   10.489  1.00 11.45 ? 104 MET   A SD  1 
ATOM   731  C  CE  . MET   A 1 91  ? -26.019 8.902   9.280   1.00 11.22 ? 104 MET   A CE  1 
ATOM   732  N  N   . LEU   A 1 92  ? -21.844 5.369   7.737   1.00 11.95 ? 105 LEU   A N   1 
ATOM   733  C  CA  . LEU   A 1 92  ? -22.308 4.205   6.984   1.00 12.15 ? 105 LEU   A CA  1 
ATOM   734  C  C   . LEU   A 1 92  ? -23.626 3.681   7.573   1.00 11.71 ? 105 LEU   A C   1 
ATOM   735  O  O   . LEU   A 1 92  ? -23.723 3.503   8.785   1.00 12.10 ? 105 LEU   A O   1 
ATOM   736  C  CB  . LEU   A 1 92  ? -21.247 3.102   7.015   1.00 12.40 ? 105 LEU   A CB  1 
ATOM   737  C  CG  . LEU   A 1 92  ? -20.096 3.159   6.001   1.00 12.82 ? 105 LEU   A CG  1 
ATOM   738  C  CD1 . LEU   A 1 92  ? -19.019 2.162   6.404   1.00 12.84 ? 105 LEU   A CD1 1 
ATOM   739  C  CD2 . LEU   A 1 92  ? -20.536 2.862   4.572   1.00 12.92 ? 105 LEU   A CD2 1 
ATOM   740  N  N   . LEU   A 1 93  ? -24.617 3.384   6.715   1.00 11.38 ? 106 LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 93  ? -25.873 2.752   7.122   1.00 11.50 ? 106 LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 93  ? -25.910 1.298   6.649   1.00 11.96 ? 106 LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 93  ? -25.814 1.048   5.447   1.00 11.44 ? 106 LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 93  ? -27.070 3.491   6.527   1.00 11.25 ? 106 LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 93  ? -27.145 5.002   6.754   1.00 11.33 ? 106 LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 93  ? -28.284 5.578   5.925   1.00 11.37 ? 106 LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 93  ? -27.318 5.329   8.226   1.00 11.42 ? 106 LEU   A CD2 1 
ATOM   748  N  N   . LYS   A 1 94  ? -26.116 0.348   7.578   1.00 12.70 ? 107 LYS   A N   1 
ATOM   749  C  CA  . LYS   A 1 94  ? -26.290 -1.058  7.221   1.00 13.66 ? 107 LYS   A CA  1 
ATOM   750  C  C   . LYS   A 1 94  ? -27.781 -1.367  7.057   1.00 13.16 ? 107 LYS   A C   1 
ATOM   751  O  O   . LYS   A 1 94  ? -28.571 -1.089  7.961   1.00 12.43 ? 107 LYS   A O   1 
ATOM   752  C  CB  . LYS   A 1 94  ? -25.682 -2.023  8.253   1.00 14.76 ? 107 LYS   A CB  1 
ATOM   753  C  CG  . LYS   A 1 94  ? -25.707 -3.502  7.839   1.00 15.67 ? 107 LYS   A CG  1 
ATOM   754  C  CD  . LYS   A 1 94  ? -25.143 -4.486  8.863   1.00 16.69 ? 107 LYS   A CD  1 
ATOM   755  C  CE  . LYS   A 1 94  ? -25.105 -5.899  8.346   1.00 17.46 ? 107 LYS   A CE  1 
ATOM   756  N  NZ  . LYS   A 1 94  ? -24.497 -6.840  9.292   1.00 18.30 ? 107 LYS   A NZ  1 
ATOM   757  N  N   . LEU   A 1 95  ? -28.142 -1.933  5.895   1.00 13.36 ? 108 LEU   A N   1 
ATOM   758  C  CA  . LEU   A 1 95  ? -29.520 -2.271  5.553   1.00 14.00 ? 108 LEU   A CA  1 
ATOM   759  C  C   . LEU   A 1 95  ? -29.874 -3.659  6.094   1.00 14.86 ? 108 LEU   A C   1 
ATOM   760  O  O   . LEU   A 1 95  ? -29.038 -4.565  6.075   1.00 14.28 ? 108 LEU   A O   1 
ATOM   761  C  CB  . LEU   A 1 95  ? -29.730 -2.227  4.036   1.00 14.00 ? 108 LEU   A CB  1 
ATOM   762  C  CG  . LEU   A 1 95  ? -29.338 -0.933  3.307   1.00 14.35 ? 108 LEU   A CG  1 
ATOM   763  C  CD1 . LEU   A 1 95  ? -29.697 -1.010  1.829   1.00 14.46 ? 108 LEU   A CD1 1 
ATOM   764  C  CD2 . LEU   A 1 95  ? -29.980 0.304   3.916   1.00 14.41 ? 108 LEU   A CD2 1 
ATOM   765  N  N   A LYS   A 1 96  ? -31.132 -3.822  6.538   0.50 15.26 ? 109 LYS   A N   1 
ATOM   766  N  N   B LYS   A 1 96  ? -31.133 -3.819  6.530   0.50 16.23 ? 109 LYS   A N   1 
ATOM   767  C  CA  A LYS   A 1 96  ? -31.605 -5.066  7.130   0.50 15.54 ? 109 LYS   A CA  1 
ATOM   768  C  CA  B LYS   A 1 96  ? -31.610 -5.059  7.124   0.50 17.31 ? 109 LYS   A CA  1 
ATOM   769  C  C   A LYS   A 1 96  ? -31.457 -6.217  6.135   0.50 16.95 ? 109 LYS   A C   1 
ATOM   770  C  C   B LYS   A 1 96  ? -31.461 -6.215  6.135   0.50 17.96 ? 109 LYS   A C   1 
ATOM   771  O  O   A LYS   A 1 96  ? -31.091 -7.324  6.532   0.50 17.51 ? 109 LYS   A O   1 
ATOM   772  O  O   B LYS   A 1 96  ? -31.098 -7.321  6.537   0.50 18.48 ? 109 LYS   A O   1 
ATOM   773  C  CB  A LYS   A 1 96  ? -33.067 -4.941  7.575   0.50 15.11 ? 109 LYS   A CB  1 
ATOM   774  C  CB  B LYS   A 1 96  ? -33.071 -4.912  7.561   0.50 18.33 ? 109 LYS   A CB  1 
ATOM   775  C  CG  A LYS   A 1 96  ? -33.644 -6.135  8.335   0.50 14.54 ? 109 LYS   A CG  1 
ATOM   776  C  CG  B LYS   A 1 96  ? -33.641 -6.099  8.327   0.50 19.11 ? 109 LYS   A CG  1 
ATOM   777  C  CD  A LYS   A 1 96  ? -33.207 -6.210  9.795   0.50 14.34 ? 109 LYS   A CD  1 
ATOM   778  C  CD  B LYS   A 1 96  ? -32.925 -6.355  9.647   0.50 20.41 ? 109 LYS   A CD  1 
ATOM   779  C  CE  A LYS   A 1 96  ? -33.791 -7.377  10.536  0.50 14.04 ? 109 LYS   A CE  1 
ATOM   780  C  CE  B LYS   A 1 96  ? -33.489 -7.520  10.394  0.50 21.54 ? 109 LYS   A CE  1 
ATOM   781  N  NZ  A LYS   A 1 96  ? -35.254 -7.396  10.551  0.50 13.34 ? 109 LYS   A NZ  1 
ATOM   782  N  NZ  B LYS   A 1 96  ? -32.634 -7.881  11.527  0.50 22.19 ? 109 LYS   A NZ  1 
ATOM   783  N  N   . GLU   A 1 97  ? -31.757 -5.948  4.855   1.00 17.56 ? 110 GLU   A N   1 
ATOM   784  C  CA  . GLU   A 1 97  ? -31.592 -6.929  3.787   1.00 20.38 ? 110 GLU   A CA  1 
ATOM   785  C  C   . GLU   A 1 97  ? -30.788 -6.335  2.627   1.00 18.22 ? 110 GLU   A C   1 
ATOM   786  O  O   . GLU   A 1 97  ? -30.578 -5.127  2.558   1.00 17.21 ? 110 GLU   A O   1 
ATOM   787  C  CB  . GLU   A 1 97  ? -32.969 -7.417  3.324   1.00 24.64 ? 110 GLU   A CB  1 
ATOM   788  C  CG  . GLU   A 1 97  ? -33.771 -8.121  4.419   1.00 28.75 ? 110 GLU   A CG  1 
ATOM   789  C  CD  . GLU   A 1 97  ? -33.131 -9.356  5.052   1.00 33.03 ? 110 GLU   A CD  1 
ATOM   790  O  OE1 . GLU   A 1 97  ? -33.584 -9.750  6.153   1.00 36.14 ? 110 GLU   A OE1 1 
ATOM   791  O  OE2 . GLU   A 1 97  ? -32.189 -9.938  4.467   1.00 36.31 ? 110 GLU   A OE2 1 
ATOM   792  N  N   . LYS   A 1 98  ? -30.334 -7.195  1.707   1.00 17.25 ? 111 LYS   A N   1 
ATOM   793  C  CA  . LYS   A 1 98  ? -29.627 -6.737  0.518   1.00 16.31 ? 111 LYS   A CA  1 
ATOM   794  C  C   . LYS   A 1 98  ? -30.645 -6.247  -0.511  1.00 15.48 ? 111 LYS   A C   1 
ATOM   795  O  O   . LYS   A 1 98  ? -31.679 -6.884  -0.719  1.00 15.07 ? 111 LYS   A O   1 
ATOM   796  C  CB  . LYS   A 1 98  ? -28.684 -7.825  -0.020  1.00 17.13 ? 111 LYS   A CB  1 
ATOM   797  C  CG  . LYS   A 1 98  ? -27.458 -8.078  0.881   1.00 18.23 ? 111 LYS   A CG  1 
ATOM   798  C  CD  . LYS   A 1 98  ? -26.382 -9.017  0.349   0.50 18.36 ? 111 LYS   A CD  1 
ATOM   799  C  CE  . LYS   A 1 98  ? -25.151 -9.045  1.211   0.50 18.62 ? 111 LYS   A CE  1 
ATOM   800  N  NZ  . LYS   A 1 98  ? -24.065 -9.857  0.646   0.50 18.62 ? 111 LYS   A NZ  1 
ATOM   801  N  N   . ALA   A 1 99  ? -30.341 -5.107  -1.150  1.00 14.30 ? 112 ALA   A N   1 
ATOM   802  C  CA  . ALA   A 1 99  ? -31.170 -4.548  -2.211  1.00 13.84 ? 112 ALA   A CA  1 
ATOM   803  C  C   . ALA   A 1 99  ? -31.212 -5.481  -3.422  1.00 13.06 ? 112 ALA   A C   1 
ATOM   804  O  O   . ALA   A 1 99  ? -30.291 -6.263  -3.637  1.00 12.87 ? 112 ALA   A O   1 
ATOM   805  C  CB  . ALA   A 1 99  ? -30.629 -3.193  -2.615  1.00 14.12 ? 112 ALA   A CB  1 
ATOM   806  N  N   . SER   A 1 100 ? -32.287 -5.384  -4.217  1.00 12.79 ? 113 SER   A N   1 
ATOM   807  C  CA  . SER   A 1 100 ? -32.368 -6.078  -5.494  1.00 12.24 ? 113 SER   A CA  1 
ATOM   808  C  C   . SER   A 1 100 ? -31.639 -5.258  -6.555  1.00 11.73 ? 113 SER   A C   1 
ATOM   809  O  O   . SER   A 1 100 ? -31.724 -4.033  -6.561  1.00 11.69 ? 113 SER   A O   1 
ATOM   810  C  CB  . SER   A 1 100 ? -33.801 -6.362  -5.905  1.00 12.17 ? 113 SER   A CB  1 
ATOM   811  O  OG  . SER   A 1 100 ? -34.446 -7.237  -4.987  1.00 11.96 ? 113 SER   A OG  1 
ATOM   812  N  N   . LEU   A 1 101 ? -30.900 -5.945  -7.436  1.00 11.73 ? 114 LEU   A N   1 
ATOM   813  C  CA  . LEU   A 1 101 ? -30.277 -5.318  -8.593  1.00 11.67 ? 114 LEU   A CA  1 
ATOM   814  C  C   . LEU   A 1 101 ? -31.282 -5.238  -9.749  1.00 11.85 ? 114 LEU   A C   1 
ATOM   815  O  O   . LEU   A 1 101 ? -31.827 -6.262  -10.162 1.00 11.74 ? 114 LEU   A O   1 
ATOM   816  C  CB  . LEU   A 1 101 ? -29.030 -6.114  -8.985  1.00 11.65 ? 114 LEU   A CB  1 
ATOM   817  C  CG  . LEU   A 1 101 ? -27.904 -6.184  -7.945  1.00 11.65 ? 114 LEU   A CG  1 
ATOM   818  C  CD1 . LEU   A 1 101 ? -26.787 -7.049  -8.485  1.00 11.99 ? 114 LEU   A CD1 1 
ATOM   819  C  CD2 . LEU   A 1 101 ? -27.357 -4.815  -7.574  1.00 11.55 ? 114 LEU   A CD2 1 
ATOM   820  N  N   . THR   A 1 102 ? -31.525 -4.009  -10.243 1.00 11.60 ? 115 THR   A N   1 
ATOM   821  C  CA  . THR   A 1 102 ? -32.403 -3.733  -11.379 1.00 11.58 ? 115 THR   A CA  1 
ATOM   822  C  C   . THR   A 1 102 ? -31.735 -2.674  -12.262 1.00 11.60 ? 115 THR   A C   1 
ATOM   823  O  O   . THR   A 1 102 ? -30.674 -2.161  -11.925 1.00 11.29 ? 115 THR   A O   1 
ATOM   824  C  CB  . THR   A 1 102 ? -33.785 -3.249  -10.914 1.00 11.37 ? 115 THR   A CB  1 
ATOM   825  O  OG1 . THR   A 1 102 ? -33.607 -1.959  -10.330 1.00 10.79 ? 115 THR   A OG1 1 
ATOM   826  C  CG2 . THR   A 1 102 ? -34.450 -4.171  -9.903  1.00 11.40 ? 115 THR   A CG2 1 
ATOM   827  N  N   . LEU   A 1 103 ? -32.375 -2.310  -13.381 1.00 12.19 ? 116 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 103 ? -31.886 -1.213  -14.214 1.00 13.06 ? 116 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 103 ? -31.811 0.086   -13.400 1.00 12.85 ? 116 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 103 ? -30.901 0.890   -13.603 1.00 13.50 ? 116 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 103 ? -32.750 -1.017  -15.465 1.00 13.80 ? 116 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 103 ? -32.322 0.121   -16.404 1.00 14.94 ? 116 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 103 ? -30.901 -0.107  -16.916 1.00 15.49 ? 116 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 103 ? -33.278 0.321   -17.585 1.00 15.48 ? 116 LEU   A CD2 1 
ATOM   835  N  N   . ALA   A 1 104 ? -32.752 0.280   -12.467 1.00 12.11 ? 117 ALA   A N   1 
ATOM   836  C  CA  . ALA   A 1 104 ? -32.888 1.527   -11.722 1.00 11.85 ? 117 ALA   A CA  1 
ATOM   837  C  C   . ALA   A 1 104 ? -32.114 1.537   -10.394 1.00 11.49 ? 117 ALA   A C   1 
ATOM   838  O  O   . ALA   A 1 104 ? -32.017 2.595   -9.763  1.00 10.80 ? 117 ALA   A O   1 
ATOM   839  C  CB  . ALA   A 1 104 ? -34.359 1.788   -11.479 1.00 11.77 ? 117 ALA   A CB  1 
ATOM   840  N  N   . VAL   A 1 105 ? -31.593 0.381   -9.951  1.00 11.71 ? 118 VAL   A N   1 
ATOM   841  C  CA  . VAL   A 1 105 ? -30.909 0.275   -8.663  1.00 12.05 ? 118 VAL   A CA  1 
ATOM   842  C  C   . VAL   A 1 105 ? -29.626 -0.547  -8.805  1.00 12.34 ? 118 VAL   A C   1 
ATOM   843  O  O   . VAL   A 1 105 ? -29.684 -1.716  -9.194  1.00 12.55 ? 118 VAL   A O   1 
ATOM   844  C  CB  . VAL   A 1 105 ? -31.816 -0.348  -7.585  1.00 12.27 ? 118 VAL   A CB  1 
ATOM   845  C  CG1 . VAL   A 1 105 ? -31.070 -0.588  -6.274  1.00 12.48 ? 118 VAL   A CG1 1 
ATOM   846  C  CG2 . VAL   A 1 105 ? -33.066 0.486   -7.344  1.00 12.51 ? 118 VAL   A CG2 1 
ATOM   847  N  N   . GLY   A 1 106 ? -28.481 0.058   -8.441  1.00 12.35 ? 119 GLY   A N   1 
ATOM   848  C  CA  . GLY   A 1 106 ? -27.189 -0.623  -8.441  1.00 12.96 ? 119 GLY   A CA  1 
ATOM   849  C  C   . GLY   A 1 106 ? -26.142 0.120   -7.606  1.00 13.69 ? 119 GLY   A C   1 
ATOM   850  O  O   . GLY   A 1 106 ? -26.409 1.225   -7.128  1.00 13.32 ? 119 GLY   A O   1 
ATOM   851  N  N   . THR   A 1 107 ? -24.953 -0.490  -7.432  1.00 14.72 ? 120 THR   A N   1 
ATOM   852  C  CA  . THR   A 1 107 ? -23.910 0.061   -6.568  1.00 15.90 ? 120 THR   A CA  1 
ATOM   853  C  C   . THR   A 1 107 ? -22.980 0.970   -7.373  1.00 18.60 ? 120 THR   A C   1 
ATOM   854  O  O   . THR   A 1 107 ? -22.867 0.838   -8.594  1.00 17.46 ? 120 THR   A O   1 
ATOM   855  C  CB  . THR   A 1 107 ? -23.107 -1.047  -5.878  1.00 16.07 ? 120 THR   A CB  1 
ATOM   856  O  OG1 . THR   A 1 107 ? -22.435 -1.805  -6.884  1.00 15.94 ? 120 THR   A OG1 1 
ATOM   857  C  CG2 . THR   A 1 107 ? -23.976 -1.970  -5.040  1.00 16.05 ? 120 THR   A CG2 1 
ATOM   858  N  N   . LEU   A 1 108 ? -22.307 1.883   -6.650  1.00 20.45 ? 121 LEU   A N   1 
ATOM   859  C  CA  . LEU   A 1 108 ? -21.222 2.690   -7.185  1.00 23.80 ? 121 LEU   A CA  1 
ATOM   860  C  C   . LEU   A 1 108 ? -19.913 2.187   -6.573  1.00 25.54 ? 121 LEU   A C   1 
ATOM   861  O  O   . LEU   A 1 108 ? -19.654 2.439   -5.400  1.00 24.98 ? 121 LEU   A O   1 
ATOM   862  C  CB  . LEU   A 1 108 ? -21.493 4.156   -6.836  1.00 25.01 ? 121 LEU   A CB  1 
ATOM   863  C  CG  . LEU   A 1 108 ? -20.479 5.191   -7.337  1.00 26.11 ? 121 LEU   A CG  1 
ATOM   864  C  CD1 . LEU   A 1 108 ? -20.421 5.234   -8.852  1.00 26.60 ? 121 LEU   A CD1 1 
ATOM   865  C  CD2 . LEU   A 1 108 ? -20.817 6.564   -6.788  1.00 26.77 ? 121 LEU   A CD2 1 
ATOM   866  N  N   . PRO   A 1 109 ? -19.068 1.422   -7.306  0.50 27.32 ? 122 PRO   A N   1 
ATOM   867  C  CA  . PRO   A 1 109 ? -17.813 0.913   -6.746  0.50 28.70 ? 122 PRO   A CA  1 
ATOM   868  C  C   . PRO   A 1 109 ? -16.746 2.001   -6.674  0.50 29.16 ? 122 PRO   A C   1 
ATOM   869  O  O   . PRO   A 1 109 ? -16.836 3.004   -7.374  0.50 29.09 ? 122 PRO   A O   1 
ATOM   870  C  CB  . PRO   A 1 109 ? -17.409 -0.231  -7.702  0.50 28.84 ? 122 PRO   A CB  1 
ATOM   871  C  CG  . PRO   A 1 109 ? -18.582 -0.384  -8.656  0.50 28.75 ? 122 PRO   A CG  1 
ATOM   872  C  CD  . PRO   A 1 109 ? -19.279 0.966   -8.687  0.50 28.41 ? 122 PRO   A CD  1 
ATOM   873  N  N   . PHE   A 1 110 ? -15.741 1.793   -5.817  0.50 31.35 ? 123 PHE   A N   1 
ATOM   874  C  CA  . PHE   A 1 110 ? -14.619 2.714   -5.716  0.50 32.66 ? 123 PHE   A CA  1 
ATOM   875  C  C   . PHE   A 1 110 ? -13.567 2.345   -6.758  0.50 33.10 ? 123 PHE   A C   1 
ATOM   876  O  O   . PHE   A 1 110 ? -13.425 1.181   -7.124  0.50 32.80 ? 123 PHE   A O   1 
ATOM   877  C  CB  . PHE   A 1 110 ? -13.963 2.709   -4.332  0.50 33.35 ? 123 PHE   A CB  1 
ATOM   878  C  CG  . PHE   A 1 110 ? -14.761 3.390   -3.229  0.50 33.52 ? 123 PHE   A CG  1 
ATOM   879  C  CD1 . PHE   A 1 110 ? -15.245 2.668   -2.146  0.50 33.62 ? 123 PHE   A CD1 1 
ATOM   880  C  CD2 . PHE   A 1 110 ? -15.032 4.752   -3.285  0.50 33.74 ? 123 PHE   A CD2 1 
ATOM   881  C  CE1 . PHE   A 1 110 ? -15.965 3.295   -1.142  0.50 33.74 ? 123 PHE   A CE1 1 
ATOM   882  C  CE2 . PHE   A 1 110 ? -15.758 5.370   -2.282  0.50 33.62 ? 123 PHE   A CE2 1 
ATOM   883  C  CZ  . PHE   A 1 110 ? -16.222 4.642   -1.215  0.50 33.58 ? 123 PHE   A CZ  1 
ATOM   884  N  N   . PRO   A 1 111 ? -12.765 3.326   -7.229  0.50 34.01 ? 124 PRO   A N   1 
ATOM   885  C  CA  . PRO   A 1 111 ? -11.781 3.085   -8.284  0.50 34.60 ? 124 PRO   A CA  1 
ATOM   886  C  C   . PRO   A 1 111 ? -10.921 1.862   -7.986  0.50 35.28 ? 124 PRO   A C   1 
ATOM   887  O  O   . PRO   A 1 111 ? -10.558 1.701   -6.800  0.50 36.43 ? 124 PRO   A O   1 
ATOM   888  C  CB  . PRO   A 1 111 ? -10.956 4.387   -8.318  0.50 34.02 ? 124 PRO   A CB  1 
ATOM   889  C  CG  . PRO   A 1 111 ? -11.282 5.083   -7.011  0.50 34.08 ? 124 PRO   A CG  1 
ATOM   890  C  CD  . PRO   A 1 111 ? -12.721 4.702   -6.714  0.50 33.95 ? 124 PRO   A CD  1 
ATOM   891  N  N   . PRO   A 1 119 ? -6.852  20.628  -7.867  0.50 39.98 ? 132 PRO   A N   1 
ATOM   892  C  CA  . PRO   A 1 119 ? -7.998  21.494  -8.105  0.50 39.81 ? 132 PRO   A CA  1 
ATOM   893  C  C   . PRO   A 1 119 ? -7.908  22.129  -9.489  0.50 39.69 ? 132 PRO   A C   1 
ATOM   894  O  O   . PRO   A 1 119 ? -6.812  22.339  -10.002 0.50 41.19 ? 132 PRO   A O   1 
ATOM   895  C  CB  . PRO   A 1 119 ? -7.963  22.544  -6.980  0.50 40.11 ? 132 PRO   A CB  1 
ATOM   896  C  CG  . PRO   A 1 119 ? -6.978  21.993  -5.976  0.50 39.74 ? 132 PRO   A CG  1 
ATOM   897  C  CD  . PRO   A 1 119 ? -6.020  21.154  -6.798  0.50 40.02 ? 132 PRO   A CD  1 
ATOM   898  N  N   . GLY   A 1 120 ? -9.073  22.426  -10.079 1.00 39.95 ? 133 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 120 ? -9.157  23.040  -11.394 1.00 37.77 ? 133 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 120 ? -10.289 22.462  -12.247 1.00 37.47 ? 133 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 120 ? -10.871 23.183  -13.054 1.00 39.45 ? 133 GLY   A O   1 
ATOM   902  N  N   . ARG   A 1 121 ? -10.608 21.172  -12.066 1.00 34.13 ? 134 ARG   A N   1 
ATOM   903  C  CA  . ARG   A 1 121 ? -11.458 20.450  -13.006 1.00 31.64 ? 134 ARG   A CA  1 
ATOM   904  C  C   . ARG   A 1 121 ? -12.927 20.488  -12.567 1.00 27.74 ? 134 ARG   A C   1 
ATOM   905  O  O   . ARG   A 1 121 ? -13.260 20.996  -11.497 1.00 25.46 ? 134 ARG   A O   1 
ATOM   906  C  CB  . ARG   A 1 121 ? -10.903 19.037  -13.229 1.00 33.38 ? 134 ARG   A CB  1 
ATOM   907  C  CG  . ARG   A 1 121 ? -10.526 18.263  -11.975 1.00 34.34 ? 134 ARG   A CG  1 
ATOM   908  C  CD  . ARG   A 1 121 ? -10.617 16.761  -12.183 0.50 34.96 ? 134 ARG   A CD  1 
ATOM   909  N  NE  . ARG   A 1 121 ? -11.997 16.361  -12.480 0.50 35.39 ? 134 ARG   A NE  1 
ATOM   910  C  CZ  . ARG   A 1 121 ? -12.384 15.695  -13.559 0.50 35.42 ? 134 ARG   A CZ  1 
ATOM   911  N  NH1 . ARG   A 1 121 ? -11.498 15.315  -14.462 0.50 36.51 ? 134 ARG   A NH1 1 
ATOM   912  N  NH2 . ARG   A 1 121 ? -13.660 15.407  -13.729 0.50 35.78 ? 134 ARG   A NH2 1 
ATOM   913  N  N   . MET   A 1 122 ? -13.813 19.980  -13.436 1.00 24.97 ? 135 MET   A N   1 
ATOM   914  C  CA  . MET   A 1 122 ? -15.249 20.056  -13.214 1.00 23.66 ? 135 MET   A CA  1 
ATOM   915  C  C   . MET   A 1 122 ? -15.768 18.696  -12.744 1.00 21.27 ? 135 MET   A C   1 
ATOM   916  O  O   . MET   A 1 122 ? -15.302 17.652  -13.199 1.00 20.23 ? 135 MET   A O   1 
ATOM   917  C  CB  . MET   A 1 122 ? -15.992 20.506  -14.480 1.00 25.00 ? 135 MET   A CB  1 
ATOM   918  C  CG  . MET   A 1 122 ? -15.525 21.840  -15.057 1.00 26.17 ? 135 MET   A CG  1 
ATOM   919  S  SD  . MET   A 1 122 ? -15.865 23.306  -14.055 1.00 26.54 ? 135 MET   A SD  1 
ATOM   920  C  CE  . MET   A 1 122 ? -17.657 23.426  -14.101 1.00 26.48 ? 135 MET   A CE  1 
ATOM   921  N  N   . CYS   A 1 123 ? -16.724 18.737  -11.809 1.00 19.17 ? 136 CYS   A N   1 
ATOM   922  C  CA  . CYS   A 1 123 ? -17.331 17.558  -11.204 1.00 18.46 ? 136 CYS   A CA  1 
ATOM   923  C  C   . CYS   A 1 123 ? -18.850 17.773  -11.180 1.00 17.33 ? 136 CYS   A C   1 
ATOM   924  O  O   . CYS   A 1 123 ? -19.307 18.875  -11.472 1.00 15.98 ? 136 CYS   A O   1 
ATOM   925  C  CB  . CYS   A 1 123 ? -16.762 17.319  -9.804  1.00 19.14 ? 136 CYS   A CB  1 
ATOM   926  S  SG  . CYS   A 1 123 ? -14.948 17.176  -9.728  1.00 19.54 ? 136 CYS   A SG  1 
ATOM   927  N  N   . ARG   A 1 124 ? -19.629 16.728  -10.849 1.00 15.93 ? 137 ARG   A N   1 
ATOM   928  C  CA  . ARG   A 1 124 ? -21.087 16.826  -10.828 1.00 15.62 ? 137 ARG   A CA  1 
ATOM   929  C  C   . ARG   A 1 124 ? -21.628 16.305  -9.492  1.00 13.94 ? 137 ARG   A C   1 
ATOM   930  O  O   . ARG   A 1 124 ? -21.089 15.341  -8.952  1.00 13.38 ? 137 ARG   A O   1 
ATOM   931  C  CB  . ARG   A 1 124 ? -21.696 16.039  -12.001 1.00 16.73 ? 137 ARG   A CB  1 
ATOM   932  C  CG  . ARG   A 1 124 ? -21.301 16.505  -13.398 1.00 18.13 ? 137 ARG   A CG  1 
ATOM   933  C  CD  . ARG   A 1 124 ? -21.825 15.580  -14.509 1.00 18.72 ? 137 ARG   A CD  1 
ATOM   934  N  NE  . ARG   A 1 124 ? -21.270 15.889  -15.835 0.50 18.85 ? 137 ARG   A NE  1 
ATOM   935  C  CZ  . ARG   A 1 124 ? -21.663 16.865  -16.651 0.50 19.11 ? 137 ARG   A CZ  1 
ATOM   936  N  NH1 . ARG   A 1 124 ? -22.716 17.610  -16.367 0.50 19.08 ? 137 ARG   A NH1 1 
ATOM   937  N  NH2 . ARG   A 1 124 ? -21.011 17.074  -17.780 0.50 19.22 ? 137 ARG   A NH2 1 
ATOM   938  N  N   . VAL   A 1 125 ? -22.703 16.937  -8.983  1.00 13.17 ? 138 VAL   A N   1 
ATOM   939  C  CA  . VAL   A 1 125 ? -23.378 16.518  -7.758  1.00 12.89 ? 138 VAL   A CA  1 
ATOM   940  C  C   . VAL   A 1 125 ? -24.890 16.471  -8.000  1.00 12.02 ? 138 VAL   A C   1 
ATOM   941  O  O   . VAL   A 1 125 ? -25.410 17.246  -8.800  1.00 11.88 ? 138 VAL   A O   1 
ATOM   942  C  CB  . VAL   A 1 125 ? -23.016 17.448  -6.579  1.00 13.53 ? 138 VAL   A CB  1 
ATOM   943  C  CG1 . VAL   A 1 125 ? -23.401 18.896  -6.840  1.00 13.87 ? 138 VAL   A CG1 1 
ATOM   944  C  CG2 . VAL   A 1 125 ? -23.633 16.997  -5.262  1.00 14.07 ? 138 VAL   A CG2 1 
ATOM   945  N  N   . ALA   A 1 126 ? -25.598 15.583  -7.278  1.00 11.54 ? 139 ALA   A N   1 
ATOM   946  C  CA  . ALA   A 1 126 ? -27.034 15.388  -7.460  1.00 11.37 ? 139 ALA   A CA  1 
ATOM   947  C  C   . ALA   A 1 126 ? -27.764 15.303  -6.114  1.00 10.70 ? 139 ALA   A C   1 
ATOM   948  O  O   . ALA   A 1 126 ? -27.155 14.941  -5.109  1.00 10.76 ? 139 ALA   A O   1 
ATOM   949  C  CB  . ALA   A 1 126 ? -27.248 14.141  -8.279  1.00 11.90 ? 139 ALA   A CB  1 
ATOM   950  N  N   . GLY   A 1 127 ? -29.060 15.659  -6.094  1.00 10.31 ? 140 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 127 ? -29.872 15.587  -4.884  1.00 10.38 ? 140 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 127 ? -31.290 16.152  -5.041  1.00 10.60 ? 140 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 127 ? -31.639 16.741  -6.067  1.00 10.51 ? 140 GLY   A O   1 
ATOM   954  N  N   . TRP   A 1 128 ? -32.100 15.971  -3.984  1.00 10.94 ? 141 TRP   A N   1 
ATOM   955  C  CA  . TRP   A 1 128 ? -33.499 16.386  -3.937  1.00 11.03 ? 141 TRP   A CA  1 
ATOM   956  C  C   . TRP   A 1 128 ? -33.685 17.619  -3.042  1.00 11.73 ? 141 TRP   A C   1 
ATOM   957  O  O   . TRP   A 1 128 ? -34.807 17.939  -2.643  1.00 11.57 ? 141 TRP   A O   1 
ATOM   958  C  CB  . TRP   A 1 128 ? -34.369 15.224  -3.420  1.00 10.85 ? 141 TRP   A CB  1 
ATOM   959  C  CG  . TRP   A 1 128 ? -34.592 14.064  -4.364  1.00 10.74 ? 141 TRP   A CG  1 
ATOM   960  C  CD1 . TRP   A 1 128 ? -35.617 13.934  -5.259  1.00 10.63 ? 141 TRP   A CD1 1 
ATOM   961  C  CD2 . TRP   A 1 128 ? -33.831 12.835  -4.453  1.00 10.65 ? 141 TRP   A CD2 1 
ATOM   962  N  NE1 . TRP   A 1 128 ? -35.534 12.734  -5.916  1.00 10.84 ? 141 TRP   A NE1 1 
ATOM   963  C  CE2 . TRP   A 1 128 ? -34.455 12.033  -5.439  1.00 11.05 ? 141 TRP   A CE2 1 
ATOM   964  C  CE3 . TRP   A 1 128 ? -32.695 12.336  -3.802  1.00 10.69 ? 141 TRP   A CE3 1 
ATOM   965  C  CZ2 . TRP   A 1 128 ? -33.970 10.770  -5.792  1.00 11.11 ? 141 TRP   A CZ2 1 
ATOM   966  C  CZ3 . TRP   A 1 128 ? -32.225 11.085  -4.139  1.00 10.70 ? 141 TRP   A CZ3 1 
ATOM   967  C  CH2 . TRP   A 1 128 ? -32.858 10.311  -5.116  1.00 11.08 ? 141 TRP   A CH2 1 
ATOM   968  N  N   . GLY   A 1 129 ? -32.592 18.325  -2.714  1.00 12.30 ? 142 GLY   A N   1 
ATOM   969  C  CA  . GLY   A 1 129 ? -32.646 19.426  -1.762  1.00 12.85 ? 142 GLY   A CA  1 
ATOM   970  C  C   . GLY   A 1 129 ? -33.259 20.699  -2.352  1.00 13.58 ? 142 GLY   A C   1 
ATOM   971  O  O   . GLY   A 1 129 ? -33.697 20.724  -3.506  1.00 13.21 ? 142 GLY   A O   1 
ATOM   972  N  N   . ARG   A 1 130 ? -33.272 21.758  -1.527  1.00 14.94 ? 143 ARG   A N   1 
ATOM   973  C  CA  . ARG   A 1 130 ? -33.883 23.038  -1.858  1.00 16.17 ? 143 ARG   A CA  1 
ATOM   974  C  C   . ARG   A 1 130 ? -33.225 23.650  -3.096  1.00 15.83 ? 143 ARG   A C   1 
ATOM   975  O  O   . ARG   A 1 130 ? -32.013 23.510  -3.282  1.00 14.57 ? 143 ARG   A O   1 
ATOM   976  C  CB  . ARG   A 1 130 ? -33.743 24.022  -0.686  1.00 18.03 ? 143 ARG   A CB  1 
ATOM   977  C  CG  . ARG   A 1 130 ? -34.344 23.605  0.651   1.00 19.66 ? 143 ARG   A CG  1 
ATOM   978  C  CD  . ARG   A 1 130 ? -34.396 24.764  1.653   1.00 21.66 ? 143 ARG   A CD  1 
ATOM   979  N  NE  . ARG   A 1 130 ? -34.957 24.372  2.953   1.00 23.59 ? 143 ARG   A NE  1 
ATOM   980  C  CZ  . ARG   A 1 130 ? -36.178 24.660  3.401   0.50 24.30 ? 143 ARG   A CZ  1 
ATOM   981  N  NH1 . ARG   A 1 130 ? -37.030 25.339  2.652   0.50 25.00 ? 143 ARG   A NH1 1 
ATOM   982  N  NH2 . ARG   A 1 130 ? -36.553 24.250  4.599   0.50 24.94 ? 143 ARG   A NH2 1 
ATOM   983  N  N   . THR   A 1 131 ? -34.037 24.354  -3.909  1.00 16.27 ? 144 THR   A N   1 
ATOM   984  C  CA  . THR   A 1 131 ? -33.588 24.985  -5.145  1.00 16.55 ? 144 THR   A CA  1 
ATOM   985  C  C   . THR   A 1 131 ? -33.392 26.496  -4.962  1.00 17.33 ? 144 THR   A C   1 
ATOM   986  O  O   . THR   A 1 131 ? -33.131 27.197  -5.934  1.00 16.11 ? 144 THR   A O   1 
ATOM   987  C  CB  . THR   A 1 131 ? -34.577 24.684  -6.274  1.00 16.93 ? 144 THR   A CB  1 
ATOM   988  O  OG1 . THR   A 1 131 ? -35.812 25.313  -5.947  1.00 17.06 ? 144 THR   A OG1 1 
ATOM   989  C  CG2 . THR   A 1 131 ? -34.824 23.196  -6.464  1.00 17.27 ? 144 THR   A CG2 1 
ATOM   990  N  N   . GLY   A 1 132 ? -33.483 26.982  -3.718  1.00 18.78 ? 145 GLY   A N   1 
ATOM   991  C  CA  . GLY   A 1 132 ? -33.199 28.369  -3.376  1.00 19.86 ? 145 GLY   A CA  1 
ATOM   992  C  C   . GLY   A 1 132 ? -33.356 28.593  -1.871  1.00 20.85 ? 145 GLY   A C   1 
ATOM   993  O  O   . GLY   A 1 132 ? -33.897 27.736  -1.177  1.00 20.62 ? 145 GLY   A O   1 
ATOM   994  N  N   . VAL   A 1 133 ? -32.886 29.743  -1.361  1.00 22.63 ? 146 VAL   A N   1 
ATOM   995  C  CA  . VAL   A 1 133 ? -32.888 29.985  0.078   1.00 23.62 ? 146 VAL   A CA  1 
ATOM   996  C  C   . VAL   A 1 133 ? -34.318 29.880  0.611   1.00 24.75 ? 146 VAL   A C   1 
ATOM   997  O  O   . VAL   A 1 133 ? -34.540 29.292  1.670   1.00 26.02 ? 146 VAL   A O   1 
ATOM   998  C  CB  . VAL   A 1 133 ? -32.248 31.326  0.496   1.00 24.26 ? 146 VAL   A CB  1 
ATOM   999  C  CG1 . VAL   A 1 133 ? -32.432 31.617  1.984   1.00 23.78 ? 146 VAL   A CG1 1 
ATOM   1000 C  CG2 . VAL   A 1 133 ? -30.766 31.387  0.136   1.00 24.46 ? 146 VAL   A CG2 1 
ATOM   1001 N  N   . LEU   A 1 134 ? -35.286 30.446  -0.118  1.00 26.02 ? 147 LEU   A N   1 
ATOM   1002 C  CA  . LEU   A 1 134 ? -36.661 30.496  0.359   1.00 28.04 ? 147 LEU   A CA  1 
ATOM   1003 C  C   . LEU   A 1 134 ? -37.567 29.557  -0.443  1.00 28.03 ? 147 LEU   A C   1 
ATOM   1004 O  O   . LEU   A 1 134 ? -38.752 29.841  -0.603  1.00 27.81 ? 147 LEU   A O   1 
ATOM   1005 C  CB  . LEU   A 1 134 ? -37.137 31.946  0.275   1.00 29.91 ? 147 LEU   A CB  1 
ATOM   1006 C  CG  . LEU   A 1 134 ? -36.449 32.939  1.220   1.00 31.31 ? 147 LEU   A CG  1 
ATOM   1007 C  CD1 . LEU   A 1 134 ? -36.907 34.359  0.916   1.00 32.04 ? 147 LEU   A CD1 1 
ATOM   1008 C  CD2 . LEU   A 1 134 ? -36.697 32.595  2.682   1.00 30.99 ? 147 LEU   A CD2 1 
ATOM   1009 N  N   . LYS   A 1 135 ? -37.023 28.426  -0.914  1.00 26.81 ? 148 LYS   A N   1 
ATOM   1010 C  CA  . LYS   A 1 135 ? -37.785 27.488  -1.729  1.00 26.14 ? 148 LYS   A CA  1 
ATOM   1011 C  C   . LYS   A 1 135 ? -37.689 26.081  -1.134  1.00 24.35 ? 148 LYS   A C   1 
ATOM   1012 O  O   . LYS   A 1 135 ? -36.606 25.673  -0.736  1.00 23.94 ? 148 LYS   A O   1 
ATOM   1013 C  CB  . LYS   A 1 135 ? -37.247 27.538  -3.165  1.00 27.46 ? 148 LYS   A CB  1 
ATOM   1014 C  CG  . LYS   A 1 135 ? -37.564 28.820  -3.930  1.00 29.96 ? 148 LYS   A CG  1 
ATOM   1015 C  CD  . LYS   A 1 135 ? -37.217 28.754  -5.413  1.00 31.65 ? 148 LYS   A CD  1 
ATOM   1016 C  CE  . LYS   A 1 135 ? -37.777 29.891  -6.212  0.50 32.49 ? 148 LYS   A CE  1 
ATOM   1017 N  NZ  . LYS   A 1 135 ? -39.226 29.775  -6.398  0.50 33.00 ? 148 LYS   A NZ  1 
ATOM   1018 N  N   . PRO   A 1 136 ? -38.831 25.408  -0.910  1.00 23.69 ? 150 PRO   A N   1 
ATOM   1019 C  CA  . PRO   A 1 136 ? -38.801 23.964  -0.693  1.00 21.86 ? 150 PRO   A CA  1 
ATOM   1020 C  C   . PRO   A 1 136 ? -37.889 23.037  -1.504  1.00 19.05 ? 150 PRO   A C   1 
ATOM   1021 O  O   . PRO   A 1 136 ? -37.341 23.403  -2.545  1.00 18.21 ? 150 PRO   A O   1 
ATOM   1022 C  CB  . PRO   A 1 136 ? -40.282 23.628  -0.947  1.00 22.24 ? 150 PRO   A CB  1 
ATOM   1023 C  CG  . PRO   A 1 136 ? -40.641 24.522  -2.101  1.00 22.70 ? 150 PRO   A CG  1 
ATOM   1024 C  CD  . PRO   A 1 136 ? -39.419 25.418  -2.253  1.00 22.72 ? 150 PRO   A CD  1 
ATOM   1025 N  N   . GLY   A 1 137 ? -37.741 21.809  -0.993  1.00 18.09 ? 151 GLY   A N   1 
ATOM   1026 C  CA  . GLY   A 1 137 ? -37.026 20.740  -1.675  1.00 18.04 ? 151 GLY   A CA  1 
ATOM   1027 C  C   . GLY   A 1 137 ? -37.697 20.358  -2.992  1.00 17.49 ? 151 GLY   A C   1 
ATOM   1028 O  O   . GLY   A 1 137 ? -38.900 20.562  -3.159  1.00 18.27 ? 151 GLY   A O   1 
ATOM   1029 N  N   . SER   A 1 138 ? -36.901 19.801  -3.916  1.00 16.56 ? 152 SER   A N   1 
ATOM   1030 C  CA  . SER   A 1 138 ? -37.349 19.440  -5.254  1.00 15.37 ? 152 SER   A CA  1 
ATOM   1031 C  C   . SER   A 1 138 ? -38.126 18.121  -5.229  1.00 15.09 ? 152 SER   A C   1 
ATOM   1032 O  O   . SER   A 1 138 ? -37.725 17.174  -4.556  1.00 13.90 ? 152 SER   A O   1 
ATOM   1033 C  CB  . SER   A 1 138 ? -36.162 19.362  -6.192  1.00 15.62 ? 152 SER   A CB  1 
ATOM   1034 O  OG  . SER   A 1 138 ? -36.532 19.001  -7.518  1.00 15.30 ? 152 SER   A OG  1 
ATOM   1035 N  N   . ASP   A 1 139 ? -39.217 18.055  -6.007  1.00 14.83 ? 153 ASP   A N   1 
ATOM   1036 C  CA  . ASP   A 1 139 ? -39.935 16.806  -6.234  1.00 15.06 ? 153 ASP   A CA  1 
ATOM   1037 C  C   . ASP   A 1 139 ? -39.101 15.830  -7.080  1.00 14.31 ? 153 ASP   A C   1 
ATOM   1038 O  O   . ASP   A 1 139 ? -39.187 14.618  -6.873  1.00 13.13 ? 153 ASP   A O   1 
ATOM   1039 C  CB  . ASP   A 1 139 ? -41.299 17.042  -6.871  1.00 15.73 ? 153 ASP   A CB  1 
ATOM   1040 C  CG  . ASP   A 1 139 ? -42.385 17.670  -6.002  1.00 16.62 ? 153 ASP   A CG  1 
ATOM   1041 O  OD1 . ASP   A 1 139 ? -42.175 17.840  -4.767  1.00 16.40 ? 153 ASP   A OD1 1 
ATOM   1042 O  OD2 . ASP   A 1 139 ? -43.457 17.971  -6.575  1.00 17.50 ? 153 ASP   A OD2 1 
ATOM   1043 N  N   . THR   A 1 140 ? -38.303 16.344  -8.034  1.00 13.85 ? 154 THR   A N   1 
ATOM   1044 C  CA  . THR   A 1 140 ? -37.505 15.501  -8.920  1.00 14.15 ? 154 THR   A CA  1 
ATOM   1045 C  C   . THR   A 1 140 ? -36.021 15.577  -8.553  1.00 13.72 ? 154 THR   A C   1 
ATOM   1046 O  O   . THR   A 1 140 ? -35.572 16.566  -7.978  1.00 14.13 ? 154 THR   A O   1 
ATOM   1047 C  CB  . THR   A 1 140 ? -37.711 15.913  -10.379 1.00 15.47 ? 154 THR   A CB  1 
ATOM   1048 O  OG1 . THR   A 1 140 ? -37.356 17.289  -10.459 1.00 15.61 ? 154 THR   A OG1 1 
ATOM   1049 C  CG2 . THR   A 1 140 ? -39.135 15.702  -10.868 1.00 15.65 ? 154 THR   A CG2 1 
ATOM   1050 N  N   . LEU   A 1 141 ? -35.262 14.529  -8.911  1.00 12.57 ? 155 LEU   A N   1 
ATOM   1051 C  CA  . LEU   A 1 141 ? -33.815 14.520  -8.750  1.00 12.47 ? 155 LEU   A CA  1 
ATOM   1052 C  C   . LEU   A 1 141 ? -33.211 15.575  -9.677  1.00 12.16 ? 155 LEU   A C   1 
ATOM   1053 O  O   . LEU   A 1 141 ? -33.525 15.589  -10.869 1.00 11.85 ? 155 LEU   A O   1 
ATOM   1054 C  CB  . LEU   A 1 141 ? -33.249 13.131  -9.055  1.00 12.25 ? 155 LEU   A CB  1 
ATOM   1055 C  CG  . LEU   A 1 141 ? -31.731 12.960  -8.922  1.00 12.31 ? 155 LEU   A CG  1 
ATOM   1056 C  CD1 . LEU   A 1 141 ? -31.282 13.019  -7.465  1.00 12.15 ? 155 LEU   A CD1 1 
ATOM   1057 C  CD2 . LEU   A 1 141 ? -31.246 11.658  -9.554  1.00 12.37 ? 155 LEU   A CD2 1 
ATOM   1058 N  N   . GLN   A 1 142 ? -32.354 16.439  -9.112  1.00 12.22 ? 156 GLN   A N   1 
ATOM   1059 C  CA  . GLN   A 1 142 ? -31.673 17.511  -9.827  1.00 12.77 ? 156 GLN   A CA  1 
ATOM   1060 C  C   . GLN   A 1 142 ? -30.163 17.275  -9.790  1.00 12.70 ? 156 GLN   A C   1 
ATOM   1061 O  O   . GLN   A 1 142 ? -29.676 16.584  -8.899  1.00 12.02 ? 156 GLN   A O   1 
ATOM   1062 C  CB  . GLN   A 1 142 ? -31.929 18.874  -9.174  1.00 13.25 ? 156 GLN   A CB  1 
ATOM   1063 C  CG  . GLN   A 1 142 ? -33.391 19.306  -9.088  1.00 13.64 ? 156 GLN   A CG  1 
ATOM   1064 C  CD  . GLN   A 1 142 ? -33.921 19.975  -10.340 1.00 14.69 ? 156 GLN   A CD  1 
ATOM   1065 O  OE1 . GLN   A 1 142 ? -33.400 21.000  -10.803 1.00 15.43 ? 156 GLN   A OE1 1 
ATOM   1066 N  NE2 . GLN   A 1 142 ? -34.979 19.409  -10.907 1.00 14.79 ? 156 GLN   A NE2 1 
ATOM   1067 N  N   . GLU   A 1 143 ? -29.424 17.865  -10.746 1.00 12.95 ? 157 GLU   A N   1 
ATOM   1068 C  CA  . GLU   A 1 143 ? -27.966 17.798  -10.747 1.00 13.27 ? 157 GLU   A CA  1 
ATOM   1069 C  C   . GLU   A 1 143 ? -27.346 19.065  -11.352 1.00 13.29 ? 157 GLU   A C   1 
ATOM   1070 O  O   . GLU   A 1 143 ? -28.027 19.832  -12.038 1.00 12.28 ? 157 GLU   A O   1 
ATOM   1071 C  CB  . GLU   A 1 143 ? -27.486 16.534  -11.461 1.00 13.99 ? 157 GLU   A CB  1 
ATOM   1072 C  CG  . GLU   A 1 143 ? -27.797 16.495  -12.955 1.00 14.75 ? 157 GLU   A CG  1 
ATOM   1073 C  CD  . GLU   A 1 143 ? -27.341 15.205  -13.616 1.00 15.51 ? 157 GLU   A CD  1 
ATOM   1074 O  OE1 . GLU   A 1 143 ? -26.349 15.270  -14.378 1.00 15.80 ? 157 GLU   A OE1 1 
ATOM   1075 O  OE2 . GLU   A 1 143 ? -27.944 14.131  -13.355 1.00 15.36 ? 157 GLU   A OE2 1 
ATOM   1076 N  N   . VAL   A 1 144 ? -26.040 19.269  -11.082 1.00 13.43 ? 158 VAL   A N   1 
ATOM   1077 C  CA  . VAL   A 1 144 ? -25.330 20.484  -11.468 1.00 13.62 ? 158 VAL   A CA  1 
ATOM   1078 C  C   . VAL   A 1 144 ? -23.821 20.223  -11.592 1.00 13.63 ? 158 VAL   A C   1 
ATOM   1079 O  O   . VAL   A 1 144 ? -23.248 19.414  -10.857 1.00 12.95 ? 158 VAL   A O   1 
ATOM   1080 C  CB  . VAL   A 1 144 ? -25.637 21.602  -10.446 1.00 14.02 ? 158 VAL   A CB  1 
ATOM   1081 C  CG1 . VAL   A 1 144 ? -24.926 21.393  -9.111  1.00 13.87 ? 158 VAL   A CG1 1 
ATOM   1082 C  CG2 . VAL   A 1 144 ? -25.293 22.980  -11.002 1.00 14.50 ? 158 VAL   A CG2 1 
ATOM   1083 N  N   . LYS   A 1 145 ? -23.178 20.924  -12.540 1.00 14.33 ? 159 LYS   A N   1 
ATOM   1084 C  CA  . LYS   A 1 145 ? -21.740 20.827  -12.771 1.00 15.17 ? 159 LYS   A CA  1 
ATOM   1085 C  C   . LYS   A 1 145 ? -21.023 21.971  -12.048 1.00 15.00 ? 159 LYS   A C   1 
ATOM   1086 O  O   . LYS   A 1 145 ? -21.410 23.126  -12.197 1.00 15.55 ? 159 LYS   A O   1 
ATOM   1087 C  CB  . LYS   A 1 145 ? -21.458 20.872  -14.281 1.00 16.09 ? 159 LYS   A CB  1 
ATOM   1088 C  CG  . LYS   A 1 145 ? -20.061 20.411  -14.697 0.50 16.62 ? 159 LYS   A CG  1 
ATOM   1089 C  CD  . LYS   A 1 145 ? -19.829 20.330  -16.201 0.50 17.81 ? 159 LYS   A CD  1 
ATOM   1090 C  CE  . LYS   A 1 145 ? -19.753 21.671  -16.859 0.50 18.70 ? 159 LYS   A CE  1 
ATOM   1091 N  NZ  . LYS   A 1 145 ? -19.819 21.569  -18.320 0.50 19.29 ? 159 LYS   A NZ  1 
ATOM   1092 N  N   . LEU   A 1 146 ? -19.974 21.651  -11.276 1.00 15.20 ? 160 LEU   A N   1 
ATOM   1093 C  CA  . LEU   A 1 146 ? -19.320 22.612  -10.392 1.00 15.76 ? 160 LEU   A CA  1 
ATOM   1094 C  C   . LEU   A 1 146 ? -17.800 22.497  -10.514 1.00 15.90 ? 160 LEU   A C   1 
ATOM   1095 O  O   . LEU   A 1 146 ? -17.283 21.413  -10.780 1.00 16.88 ? 160 LEU   A O   1 
ATOM   1096 C  CB  . LEU   A 1 146 ? -19.747 22.355  -8.944  1.00 16.00 ? 160 LEU   A CB  1 
ATOM   1097 C  CG  . LEU   A 1 146 ? -21.230 22.557  -8.610  1.00 16.36 ? 160 LEU   A CG  1 
ATOM   1098 C  CD1 . LEU   A 1 146 ? -21.507 22.112  -7.181  1.00 16.56 ? 160 LEU   A CD1 1 
ATOM   1099 C  CD2 . LEU   A 1 146 ? -21.695 23.993  -8.793  1.00 16.23 ? 160 LEU   A CD2 1 
ATOM   1100 N  N   . ARG   A 1 147 ? -17.093 23.603  -10.234 1.00 16.17 ? 161 ARG   A N   1 
ATOM   1101 C  CA  . ARG   A 1 147 ? -15.637 23.657  -10.320 1.00 16.81 ? 161 ARG   A CA  1 
ATOM   1102 C  C   . ARG   A 1 147 ? -14.980 23.339  -8.974  1.00 16.25 ? 161 ARG   A C   1 
ATOM   1103 O  O   . ARG   A 1 147 ? -15.363 23.903  -7.941  1.00 16.38 ? 161 ARG   A O   1 
ATOM   1104 C  CB  . ARG   A 1 147 ? -15.197 25.055  -10.772 1.00 18.96 ? 161 ARG   A CB  1 
ATOM   1105 C  CG  . ARG   A 1 147 ? -13.729 25.203  -11.164 1.00 21.18 ? 161 ARG   A CG  1 
ATOM   1106 C  CD  . ARG   A 1 147 ? -13.376 26.661  -11.475 1.00 23.52 ? 161 ARG   A CD  1 
ATOM   1107 N  NE  . ARG   A 1 147 ? -12.050 26.838  -12.084 1.00 26.03 ? 161 ARG   A NE  1 
ATOM   1108 C  CZ  . ARG   A 1 147 ? -10.925 27.167  -11.451 1.00 28.10 ? 161 ARG   A CZ  1 
ATOM   1109 N  NH1 . ARG   A 1 147 ? -10.858 27.164  -10.130 1.00 28.87 ? 161 ARG   A NH1 1 
ATOM   1110 N  NH2 . ARG   A 1 147 ? -9.838  27.452  -12.149 1.00 30.01 ? 161 ARG   A NH2 1 
ATOM   1111 N  N   A LEU   A 1 148 ? -14.005 22.415  -8.996  0.50 15.81 ? 162 LEU   A N   1 
ATOM   1112 N  N   B LEU   A 1 148 ? -13.966 22.463  -9.007  0.50 15.43 ? 162 LEU   A N   1 
ATOM   1113 C  CA  A LEU   A 1 148 ? -13.102 22.191  -7.876  0.50 15.95 ? 162 LEU   A CA  1 
ATOM   1114 C  CA  B LEU   A 1 148 ? -13.126 22.189  -7.852  0.50 15.26 ? 162 LEU   A CA  1 
ATOM   1115 C  C   A LEU   A 1 148 ? -12.210 23.420  -7.715  0.50 15.84 ? 162 LEU   A C   1 
ATOM   1116 C  C   B LEU   A 1 148 ? -12.122 23.329  -7.672  0.50 15.43 ? 162 LEU   A C   1 
ATOM   1117 O  O   A LEU   A 1 148 ? -11.580 23.853  -8.681  0.50 15.30 ? 162 LEU   A O   1 
ATOM   1118 O  O   B LEU   A 1 148 ? -11.323 23.601  -8.568  0.50 14.79 ? 162 LEU   A O   1 
ATOM   1119 C  CB  A LEU   A 1 148 ? -12.244 20.942  -8.086  0.50 16.43 ? 162 LEU   A CB  1 
ATOM   1120 C  CB  B LEU   A 1 148 ? -12.428 20.844  -8.056  0.50 15.20 ? 162 LEU   A CB  1 
ATOM   1121 C  CG  A LEU   A 1 148 ? -12.912 19.587  -7.835  0.50 16.89 ? 162 LEU   A CG  1 
ATOM   1122 C  CG  B LEU   A 1 148 ? -11.608 20.322  -6.872  0.50 15.02 ? 162 LEU   A CG  1 
ATOM   1123 C  CD1 A LEU   A 1 148 ? -11.982 18.452  -8.229  0.50 17.14 ? 162 LEU   A CD1 1 
ATOM   1124 C  CD1 B LEU   A 1 148 ? -12.421 20.353  -5.589  0.50 15.12 ? 162 LEU   A CD1 1 
ATOM   1125 C  CD2 A LEU   A 1 148 ? -13.329 19.425  -6.389  0.50 17.22 ? 162 LEU   A CD2 1 
ATOM   1126 C  CD2 B LEU   A 1 148 ? -11.099 18.915  -7.142  0.50 15.15 ? 162 LEU   A CD2 1 
ATOM   1127 N  N   . MET   A 1 149 ? -12.156 23.965  -6.492  1.00 15.24 ? 163 MET   A N   1 
ATOM   1128 C  CA  . MET   A 1 149 ? -11.418 25.194  -6.225  1.00 15.37 ? 163 MET   A CA  1 
ATOM   1129 C  C   . MET   A 1 149 ? -10.170 24.912  -5.390  1.00 15.83 ? 163 MET   A C   1 
ATOM   1130 O  O   . MET   A 1 149 ? -10.118 23.940  -4.640  1.00 15.44 ? 163 MET   A O   1 
ATOM   1131 C  CB  . MET   A 1 149 ? -12.289 26.180  -5.433  1.00 15.45 ? 163 MET   A CB  1 
ATOM   1132 C  CG  . MET   A 1 149 ? -13.615 26.524  -6.101  1.00 15.87 ? 163 MET   A CG  1 
ATOM   1133 S  SD  . MET   A 1 149 ? -13.475 27.391  -7.677  1.00 16.93 ? 163 MET   A SD  1 
ATOM   1134 C  CE  . MET   A 1 149 ? -12.760 28.946  -7.119  1.00 17.17 ? 163 MET   A CE  1 
ATOM   1135 N  N   . ASP   A 1 150 ? -9.176  25.807  -5.486  1.00 16.51 ? 164 ASP   A N   1 
ATOM   1136 C  CA  . ASP   A 1 150 ? -8.031  25.773  -4.589  1.00 17.37 ? 164 ASP   A CA  1 
ATOM   1137 C  C   . ASP   A 1 150 ? -8.504  26.056  -3.163  1.00 16.45 ? 164 ASP   A C   1 
ATOM   1138 O  O   . ASP   A 1 150 ? -9.472  26.785  -2.955  1.00 15.14 ? 164 ASP   A O   1 
ATOM   1139 C  CB  . ASP   A 1 150 ? -6.953  26.764  -5.002  1.00 19.21 ? 164 ASP   A CB  1 
ATOM   1140 C  CG  . ASP   A 1 150 ? -6.284  26.482  -6.341  1.00 21.46 ? 164 ASP   A CG  1 
ATOM   1141 O  OD1 . ASP   A 1 150 ? -6.162  27.418  -7.135  1.00 24.68 ? 164 ASP   A OD1 1 
ATOM   1142 O  OD2 . ASP   A 1 150 ? -5.915  25.320  -6.592  1.00 24.36 ? 164 ASP   A OD2 1 
ATOM   1143 N  N   . PRO   A 1 151 ? -7.830  25.502  -2.131  1.00 16.06 ? 165 PRO   A N   1 
ATOM   1144 C  CA  . PRO   A 1 151 ? -8.339  25.586  -0.761  1.00 16.28 ? 165 PRO   A CA  1 
ATOM   1145 C  C   . PRO   A 1 151 ? -8.508  27.002  -0.203  1.00 15.45 ? 165 PRO   A C   1 
ATOM   1146 O  O   . PRO   A 1 151 ? -9.370  27.203  0.645   1.00 14.08 ? 165 PRO   A O   1 
ATOM   1147 C  CB  . PRO   A 1 151 ? -7.349  24.719  0.065   1.00 16.31 ? 165 PRO   A CB  1 
ATOM   1148 C  CG  . PRO   A 1 151 ? -6.099  24.635  -0.792  1.00 16.54 ? 165 PRO   A CG  1 
ATOM   1149 C  CD  . PRO   A 1 151 ? -6.563  24.759  -2.234  1.00 16.29 ? 165 PRO   A CD  1 
ATOM   1150 N  N   . GLN   A 1 152 ? -7.741  27.988  -0.709  1.00 15.42 ? 166 GLN   A N   1 
ATOM   1151 C  CA  . GLN   A 1 152 ? -7.832  29.365  -0.220  1.00 15.89 ? 166 GLN   A CA  1 
ATOM   1152 C  C   . GLN   A 1 152 ? -9.225  29.964  -0.460  1.00 14.64 ? 166 GLN   A C   1 
ATOM   1153 O  O   . GLN   A 1 152 ? -9.638  30.890  0.249   1.00 13.35 ? 166 GLN   A O   1 
ATOM   1154 C  CB  . GLN   A 1 152 ? -6.745  30.302  -0.760  1.00 18.09 ? 166 GLN   A CB  1 
ATOM   1155 C  CG  . GLN   A 1 152 ? -6.493  30.228  -2.263  1.00 19.92 ? 166 GLN   A CG  1 
ATOM   1156 C  CD  . GLN   A 1 152 ? -5.306  29.359  -2.633  1.00 22.60 ? 166 GLN   A CD  1 
ATOM   1157 O  OE1 . GLN   A 1 152 ? -5.192  28.191  -2.229  1.00 22.29 ? 166 GLN   A OE1 1 
ATOM   1158 N  NE2 . GLN   A 1 152 ? -4.385  29.940  -3.394  1.00 23.41 ? 166 GLN   A NE2 1 
ATOM   1159 N  N   . ALA   A 1 153 ? -9.970  29.411  -1.428  1.00 13.00 ? 167 ALA   A N   1 
ATOM   1160 C  CA  . ALA   A 1 153 ? -11.323 29.866  -1.727  1.00 12.42 ? 167 ALA   A CA  1 
ATOM   1161 C  C   . ALA   A 1 153 ? -12.310 29.595  -0.581  1.00 11.66 ? 167 ALA   A C   1 
ATOM   1162 O  O   . ALA   A 1 153 ? -13.367 30.232  -0.541  1.00 11.07 ? 167 ALA   A O   1 
ATOM   1163 C  CB  . ALA   A 1 153 ? -11.803 29.221  -3.012  1.00 12.40 ? 167 ALA   A CB  1 
ATOM   1164 N  N   . CYS   A 1 154 ? -11.971 28.666  0.331   1.00 11.05 ? 168 CYS   A N   1 
ATOM   1165 C  CA  . CYS   A 1 154 ? -12.821 28.300  1.464   1.00 10.90 ? 168 CYS   A CA  1 
ATOM   1166 C  C   . CYS   A 1 154 ? -12.235 28.783  2.806   1.00 10.90 ? 168 CYS   A C   1 
ATOM   1167 O  O   . CYS   A 1 154 ? -12.619 28.291  3.869   1.00 10.60 ? 168 CYS   A O   1 
ATOM   1168 C  CB  . CYS   A 1 154 ? -13.049 26.787  1.506   1.00 10.59 ? 168 CYS   A CB  1 
ATOM   1169 S  SG  . CYS   A 1 154 ? -14.296 26.145  0.348   1.00 10.44 ? 168 CYS   A SG  1 
ATOM   1170 N  N   . SER   A 1 155 ? -11.325 29.769  2.791   1.00 10.60 ? 169 SER   A N   1 
ATOM   1171 C  CA  . SER   A 1 155 ? -10.680 30.239  4.017   1.00 10.20 ? 169 SER   A CA  1 
ATOM   1172 C  C   . SER   A 1 155 ? -11.692 30.780  5.033   1.00 10.16 ? 169 SER   A C   1 
ATOM   1173 O  O   . SER   A 1 155 ? -11.472 30.644  6.234   1.00 10.06 ? 169 SER   A O   1 
ATOM   1174 C  CB  . SER   A 1 155 ? -9.607  31.280  3.710   1.00 10.53 ? 169 SER   A CB  1 
ATOM   1175 O  OG  . SER   A 1 155 ? -8.898  31.695  4.874   1.00 10.56 ? 169 SER   A OG  1 
ATOM   1176 N  N   . HIS   A 1 156 ? -12.778 31.409  4.560   1.00 10.04 ? 172 HIS   A N   1 
ATOM   1177 C  CA  . HIS   A 1 156 ? -13.763 32.048  5.429   1.00 10.56 ? 172 HIS   A CA  1 
ATOM   1178 C  C   . HIS   A 1 156 ? -14.470 31.041  6.349   1.00 11.04 ? 172 HIS   A C   1 
ATOM   1179 O  O   . HIS   A 1 156 ? -14.989 31.425  7.401   1.00 10.68 ? 172 HIS   A O   1 
ATOM   1180 C  CB  . HIS   A 1 156 ? -14.754 32.895  4.615   1.00 10.65 ? 172 HIS   A CB  1 
ATOM   1181 C  CG  . HIS   A 1 156 ? -15.464 32.163  3.512   1.00 10.89 ? 172 HIS   A CG  1 
ATOM   1182 N  ND1 . HIS   A 1 156 ? -14.832 31.768  2.351   1.00 10.87 ? 172 HIS   A ND1 1 
ATOM   1183 C  CD2 . HIS   A 1 156 ? -16.746 31.763  3.393   1.00 11.07 ? 172 HIS   A CD2 1 
ATOM   1184 C  CE1 . HIS   A 1 156 ? -15.708 31.141  1.570   1.00 11.30 ? 172 HIS   A CE1 1 
ATOM   1185 N  NE2 . HIS   A 1 156 ? -16.884 31.141  2.178   1.00 11.39 ? 172 HIS   A NE2 1 
ATOM   1186 N  N   . PHE   A 1 157 ? -14.503 29.765  5.946   1.00 11.33 ? 173 PHE   A N   1 
ATOM   1187 C  CA  . PHE   A 1 157 ? -14.890 28.675  6.834   1.00 11.99 ? 173 PHE   A CA  1 
ATOM   1188 C  C   . PHE   A 1 157 ? -13.690 28.335  7.720   1.00 12.68 ? 173 PHE   A C   1 
ATOM   1189 O  O   . PHE   A 1 157 ? -12.775 27.635  7.285   1.00 11.92 ? 173 PHE   A O   1 
ATOM   1190 C  CB  . PHE   A 1 157 ? -15.337 27.435  6.047   1.00 11.59 ? 173 PHE   A CB  1 
ATOM   1191 C  CG  . PHE   A 1 157 ? -16.509 27.629  5.092   1.00 11.33 ? 173 PHE   A CG  1 
ATOM   1192 C  CD1 . PHE   A 1 157 ? -17.801 27.820  5.575   1.00 11.62 ? 173 PHE   A CD1 1 
ATOM   1193 C  CD2 . PHE   A 1 157 ? -16.322 27.587  3.711   1.00 11.36 ? 173 PHE   A CD2 1 
ATOM   1194 C  CE1 . PHE   A 1 157 ? -18.873 27.996  4.701   1.00 11.47 ? 173 PHE   A CE1 1 
ATOM   1195 C  CE2 . PHE   A 1 157 ? -17.395 27.761  2.841   1.00 11.55 ? 173 PHE   A CE2 1 
ATOM   1196 C  CZ  . PHE   A 1 157 ? -18.670 27.963  3.338   1.00 11.43 ? 173 PHE   A CZ  1 
ATOM   1197 N  N   . ARG   A 1 158 ? -13.695 28.838  8.963   1.00 13.71 ? 174 ARG   A N   1 
ATOM   1198 C  CA  . ARG   A 1 158 ? -12.467 28.905  9.747   1.00 14.77 ? 174 ARG   A CA  1 
ATOM   1199 C  C   . ARG   A 1 158 ? -11.989 27.507  10.144  1.00 14.91 ? 174 ARG   A C   1 
ATOM   1200 O  O   . ARG   A 1 158 ? -10.802 27.339  10.423  1.00 14.74 ? 174 ARG   A O   1 
ATOM   1201 C  CB  . ARG   A 1 158 ? -12.586 29.816  10.977  1.00 15.42 ? 174 ARG   A CB  1 
ATOM   1202 C  CG  . ARG   A 1 158 ? -13.008 31.259  10.719  1.00 16.09 ? 174 ARG   A CG  1 
ATOM   1203 C  CD  . ARG   A 1 158 ? -12.234 32.023  9.646   1.00 16.88 ? 174 ARG   A CD  1 
ATOM   1204 N  NE  . ARG   A 1 158 ? -10.809 32.235  9.939   1.00 17.32 ? 174 ARG   A NE  1 
ATOM   1205 C  CZ  . ARG   A 1 158 ? -9.955  32.867  9.138   1.00 17.56 ? 174 ARG   A CZ  1 
ATOM   1206 N  NH1 . ARG   A 1 158 ? -10.386 33.471  8.042   1.00 17.82 ? 174 ARG   A NH1 1 
ATOM   1207 N  NH2 . ARG   A 1 158 ? -8.667  32.919  9.444   1.00 17.10 ? 174 ARG   A NH2 1 
ATOM   1208 N  N   . ASP   A 1 159 ? -12.893 26.511  10.144  1.00 15.19 ? 175 ASP   A N   1 
ATOM   1209 C  CA  . ASP   A 1 159 ? -12.546 25.139  10.501  1.00 15.82 ? 175 ASP   A CA  1 
ATOM   1210 C  C   . ASP   A 1 159 ? -12.361 24.223  9.284   1.00 15.90 ? 175 ASP   A C   1 
ATOM   1211 O  O   . ASP   A 1 159 ? -12.224 23.010  9.461   1.00 16.02 ? 175 ASP   A O   1 
ATOM   1212 C  CB  . ASP   A 1 159 ? -13.564 24.553  11.469  1.00 16.43 ? 175 ASP   A CB  1 
ATOM   1213 C  CG  . ASP   A 1 159 ? -13.552 25.182  12.855  1.00 17.42 ? 175 ASP   A CG  1 
ATOM   1214 O  OD1 . ASP   A 1 159 ? -12.458 25.245  13.459  1.00 17.99 ? 175 ASP   A OD1 1 
ATOM   1215 O  OD2 . ASP   A 1 159 ? -14.624 25.612  13.312  1.00 17.77 ? 175 ASP   A OD2 1 
ATOM   1216 N  N   . PHE   A 1 160 ? -12.328 24.787  8.068   1.00 15.42 ? 176 PHE   A N   1 
ATOM   1217 C  CA  . PHE   A 1 160 ? -11.999 24.043  6.854   1.00 16.10 ? 176 PHE   A CA  1 
ATOM   1218 C  C   . PHE   A 1 160 ? -10.555 23.532  6.928   1.00 17.18 ? 176 PHE   A C   1 
ATOM   1219 O  O   . PHE   A 1 160 ? -9.687  24.256  7.419   1.00 16.88 ? 176 PHE   A O   1 
ATOM   1220 C  CB  . PHE   A 1 160 ? -12.186 24.957  5.631   1.00 15.62 ? 176 PHE   A CB  1 
ATOM   1221 C  CG  . PHE   A 1 160 ? -11.777 24.332  4.298   1.00 15.63 ? 176 PHE   A CG  1 
ATOM   1222 C  CD1 . PHE   A 1 160 ? -10.487 24.477  3.805   1.00 15.81 ? 176 PHE   A CD1 1 
ATOM   1223 C  CD2 . PHE   A 1 160 ? -12.673 23.560  3.560   1.00 15.29 ? 176 PHE   A CD2 1 
ATOM   1224 C  CE1 . PHE   A 1 160 ? -10.108 23.881  2.604   1.00 15.94 ? 176 PHE   A CE1 1 
ATOM   1225 C  CE2 . PHE   A 1 160 ? -12.292 22.970  2.360   1.00 15.65 ? 176 PHE   A CE2 1 
ATOM   1226 C  CZ  . PHE   A 1 160 ? -11.010 23.129  1.884   1.00 15.50 ? 176 PHE   A CZ  1 
ATOM   1227 N  N   A ASP   A 1 161 ? -10.315 22.290  6.473   0.50 17.82 ? 177 ASP   A N   1 
ATOM   1228 N  N   B ASP   A 1 161 ? -10.307 22.326  6.382   0.50 17.09 ? 177 ASP   A N   1 
ATOM   1229 C  CA  A ASP   A 1 161 ? -8.964  21.758  6.354   0.50 18.92 ? 177 ASP   A CA  1 
ATOM   1230 C  CA  B ASP   A 1 161 ? -8.988  21.701  6.382   0.50 17.57 ? 177 ASP   A CA  1 
ATOM   1231 C  C   A ASP   A 1 161 ? -8.795  21.017  5.029   0.50 19.20 ? 177 ASP   A C   1 
ATOM   1232 C  C   B ASP   A 1 161 ? -8.757  20.957  5.063   0.50 18.36 ? 177 ASP   A C   1 
ATOM   1233 O  O   A ASP   A 1 161 ? -9.566  20.116  4.707   0.50 19.24 ? 177 ASP   A O   1 
ATOM   1234 O  O   B ASP   A 1 161 ? -9.458  19.991  4.768   0.50 18.20 ? 177 ASP   A O   1 
ATOM   1235 C  CB  A ASP   A 1 161 ? -8.583  20.823  7.492   0.50 19.94 ? 177 ASP   A CB  1 
ATOM   1236 C  CB  B ASP   A 1 161 ? -8.829  20.794  7.596   0.50 17.52 ? 177 ASP   A CB  1 
ATOM   1237 C  CG  A ASP   A 1 161 ? -7.161  20.279  7.408   0.50 20.86 ? 177 ASP   A CG  1 
ATOM   1238 C  CG  B ASP   A 1 161 ? -7.500  20.058  7.731   0.50 17.51 ? 177 ASP   A CG  1 
ATOM   1239 O  OD1 A ASP   A 1 161 ? -7.004  19.082  7.094   0.50 20.86 ? 177 ASP   A OD1 1 
ATOM   1240 O  OD1 B ASP   A 1 161 ? -6.785  19.924  6.708   0.50 16.60 ? 177 ASP   A OD1 1 
ATOM   1241 O  OD2 A ASP   A 1 161 ? -6.215  21.060  7.650   0.50 21.88 ? 177 ASP   A OD2 1 
ATOM   1242 O  OD2 B ASP   A 1 161 ? -7.181  19.638  8.869   0.50 16.96 ? 177 ASP   A OD2 1 
ATOM   1243 N  N   . HIS   A 1 162 ? -7.741  21.392  4.296   1.00 19.34 ? 178 HIS   A N   1 
ATOM   1244 C  CA  . HIS   A 1 162 ? -7.450  20.879  2.960   1.00 20.26 ? 178 HIS   A CA  1 
ATOM   1245 C  C   . HIS   A 1 162 ? -7.191  19.369  2.942   1.00 20.53 ? 178 HIS   A C   1 
ATOM   1246 O  O   . HIS   A 1 162 ? -7.435  18.714  1.928   1.00 20.46 ? 178 HIS   A O   1 
ATOM   1247 C  CB  . HIS   A 1 162 ? -6.237  21.631  2.388   1.00 21.89 ? 178 HIS   A CB  1 
ATOM   1248 C  CG  . HIS   A 1 162 ? -5.803  21.236  1.008   1.00 23.97 ? 178 HIS   A CG  1 
ATOM   1249 N  ND1 . HIS   A 1 162 ? -6.632  21.250  -0.094  1.00 26.00 ? 178 HIS   A ND1 1 
ATOM   1250 C  CD2 . HIS   A 1 162 ? -4.593  20.864  0.549   1.00 25.13 ? 178 HIS   A CD2 1 
ATOM   1251 C  CE1 . HIS   A 1 162 ? -5.948  20.866  -1.167  1.00 25.53 ? 178 HIS   A CE1 1 
ATOM   1252 N  NE2 . HIS   A 1 162 ? -4.707  20.625  -0.798  1.00 25.23 ? 178 HIS   A NE2 1 
ATOM   1253 N  N   A ASN   A 1 163 A -6.706  18.822  4.063   0.50 20.89 ? 178 ASN   A N   1 
ATOM   1254 N  N   B ASN   A 1 163 A -6.669  18.836  4.056   0.50 20.70 ? 178 ASN   A N   1 
ATOM   1255 C  CA  A ASN   A 1 163 A -6.393  17.404  4.152   0.50 21.95 ? 178 ASN   A CA  1 
ATOM   1256 C  CA  B ASN   A 1 163 A -6.396  17.413  4.196   0.50 21.63 ? 178 ASN   A CA  1 
ATOM   1257 C  C   A ASN   A 1 163 A -7.674  16.570  4.249   0.50 21.02 ? 178 ASN   A C   1 
ATOM   1258 C  C   B ASN   A 1 163 A -7.695  16.604  4.191   0.50 20.87 ? 178 ASN   A C   1 
ATOM   1259 O  O   A ASN   A 1 163 A -7.705  15.438  3.769   0.50 20.68 ? 178 ASN   A O   1 
ATOM   1260 O  O   B ASN   A 1 163 A -7.757  15.535  3.588   0.50 20.59 ? 178 ASN   A O   1 
ATOM   1261 C  CB  A ASN   A 1 163 A -5.451  17.125  5.318   0.50 23.16 ? 178 ASN   A CB  1 
ATOM   1262 C  CB  B ASN   A 1 163 A -5.628  17.115  5.479   0.50 22.57 ? 178 ASN   A CB  1 
ATOM   1263 C  CG  A ASN   A 1 163 A -4.861  15.736  5.259   0.50 24.56 ? 178 ASN   A CG  1 
ATOM   1264 C  CG  B ASN   A 1 163 A -4.227  17.680  5.471   0.50 23.52 ? 178 ASN   A CG  1 
ATOM   1265 O  OD1 A ASN   A 1 163 A -4.194  15.382  4.280   0.50 25.47 ? 178 ASN   A OD1 1 
ATOM   1266 O  OD1 B ASN   A 1 163 A -3.660  17.943  4.405   0.50 24.57 ? 178 ASN   A OD1 1 
ATOM   1267 N  ND2 A ASN   A 1 163 A -5.086  14.942  6.296   0.50 25.61 ? 178 ASN   A ND2 1 
ATOM   1268 N  ND2 B ASN   A 1 163 A -3.644  17.850  6.648   0.50 24.66 ? 178 ASN   A ND2 1 
ATOM   1269 N  N   . LEU   A 1 164 ? -8.725  17.125  4.869   1.00 20.13 ? 179 LEU   A N   1 
ATOM   1270 C  CA  . LEU   A 1 164 ? -9.941  16.373  5.155   1.00 19.32 ? 179 LEU   A CA  1 
ATOM   1271 C  C   . LEU   A 1 164 ? -11.088 16.679  4.187   1.00 17.79 ? 179 LEU   A C   1 
ATOM   1272 O  O   . LEU   A 1 164 ? -12.047 15.899  4.140   1.00 16.92 ? 179 LEU   A O   1 
ATOM   1273 C  CB  . LEU   A 1 164 ? -10.368 16.699  6.585   1.00 21.07 ? 179 LEU   A CB  1 
ATOM   1274 C  CG  . LEU   A 1 164 ? -9.342  16.449  7.695   1.00 22.36 ? 179 LEU   A CG  1 
ATOM   1275 C  CD1 . LEU   A 1 164 ? -9.930  16.877  9.024   1.00 22.69 ? 179 LEU   A CD1 1 
ATOM   1276 C  CD2 . LEU   A 1 164 ? -8.898  14.994  7.753   1.00 23.38 ? 179 LEU   A CD2 1 
ATOM   1277 N  N   . GLN   A 1 165 ? -11.027 17.811  3.461   1.00 15.14 ? 180 GLN   A N   1 
ATOM   1278 C  CA  . GLN   A 1 165 ? -12.193 18.354  2.770   1.00 14.24 ? 180 GLN   A CA  1 
ATOM   1279 C  C   . GLN   A 1 165 ? -11.818 18.938  1.403   1.00 14.12 ? 180 GLN   A C   1 
ATOM   1280 O  O   . GLN   A 1 165 ? -10.660 19.303  1.174   1.00 13.52 ? 180 GLN   A O   1 
ATOM   1281 C  CB  . GLN   A 1 165 ? -12.863 19.426  3.640   1.00 13.86 ? 180 GLN   A CB  1 
ATOM   1282 C  CG  . GLN   A 1 165 ? -13.438 18.912  4.963   1.00 13.56 ? 180 GLN   A CG  1 
ATOM   1283 C  CD  . GLN   A 1 165 ? -13.595 19.968  6.037   1.00 13.58 ? 180 GLN   A CD  1 
ATOM   1284 O  OE1 . GLN   A 1 165 ? -12.718 20.813  6.243   1.00 13.93 ? 180 GLN   A OE1 1 
ATOM   1285 N  NE2 . GLN   A 1 165 ? -14.700 19.918  6.769   1.00 13.75 ? 180 GLN   A NE2 1 
ATOM   1286 N  N   . LEU   A 1 166 ? -12.830 19.034  0.518   1.00 13.48 ? 181 LEU   A N   1 
ATOM   1287 C  CA  . LEU   A 1 166 ? -12.734 19.695  -0.777  1.00 14.19 ? 181 LEU   A CA  1 
ATOM   1288 C  C   . LEU   A 1 166 ? -13.564 20.983  -0.764  1.00 13.51 ? 181 LEU   A C   1 
ATOM   1289 O  O   . LEU   A 1 166 ? -14.573 21.076  -0.058  1.00 13.44 ? 181 LEU   A O   1 
ATOM   1290 C  CB  . LEU   A 1 166 ? -13.224 18.790  -1.910  1.00 15.34 ? 181 LEU   A CB  1 
ATOM   1291 C  CG  . LEU   A 1 166 ? -12.686 17.357  -1.948  1.00 16.23 ? 181 LEU   A CG  1 
ATOM   1292 C  CD1 . LEU   A 1 166 ? -13.480 16.544  -2.949  1.00 17.04 ? 181 LEU   A CD1 1 
ATOM   1293 C  CD2 . LEU   A 1 166 ? -11.218 17.318  -2.297  1.00 17.08 ? 181 LEU   A CD2 1 
ATOM   1294 N  N   . CYS   A 1 167 ? -13.139 21.945  -1.598  1.00 12.44 ? 182 CYS   A N   1 
ATOM   1295 C  CA  . CYS   A 1 167 ? -13.767 23.253  -1.750  1.00 12.03 ? 182 CYS   A CA  1 
ATOM   1296 C  C   . CYS   A 1 167 ? -14.399 23.316  -3.142  1.00 12.25 ? 182 CYS   A C   1 
ATOM   1297 O  O   . CYS   A 1 167 ? -13.677 23.330  -4.146  1.00 12.35 ? 182 CYS   A O   1 
ATOM   1298 C  CB  . CYS   A 1 167 ? -12.710 24.342  -1.545  1.00 11.62 ? 182 CYS   A CB  1 
ATOM   1299 S  SG  . CYS   A 1 167 ? -13.325 26.048  -1.472  1.00 10.81 ? 182 CYS   A SG  1 
ATOM   1300 N  N   . VAL   A 1 168 ? -15.746 23.343  -3.207  1.00 11.99 ? 183 VAL   A N   1 
ATOM   1301 C  CA  . VAL   A 1 168 ? -16.461 23.107  -4.458  1.00 11.96 ? 183 VAL   A CA  1 
ATOM   1302 C  C   . VAL   A 1 168 ? -17.437 24.247  -4.777  1.00 11.80 ? 183 VAL   A C   1 
ATOM   1303 O  O   . VAL   A 1 168 ? -18.329 24.543  -3.978  1.00 11.64 ? 183 VAL   A O   1 
ATOM   1304 C  CB  . VAL   A 1 168 ? -17.191 21.753  -4.369  1.00 12.32 ? 183 VAL   A CB  1 
ATOM   1305 C  CG1 . VAL   A 1 168 ? -17.843 21.376  -5.690  1.00 12.82 ? 183 VAL   A CG1 1 
ATOM   1306 C  CG2 . VAL   A 1 168 ? -16.272 20.623  -3.897  1.00 12.41 ? 183 VAL   A CG2 1 
ATOM   1307 N  N   . GLY   A 1 169 ? -17.273 24.853  -5.969  1.00 11.54 ? 184 GLY   A N   1 
ATOM   1308 C  CA  . GLY   A 1 169 ? -18.195 25.844  -6.516  1.00 11.89 ? 184 GLY   A CA  1 
ATOM   1309 C  C   . GLY   A 1 169 ? -17.554 27.224  -6.710  1.00 12.50 ? 184 GLY   A C   1 
ATOM   1310 O  O   . GLY   A 1 169 ? -17.186 27.887  -5.740  1.00 12.08 ? 184 GLY   A O   1 
ATOM   1311 N  N   . ASN   A 1 170 ? -17.474 27.673  -7.975  1.00 13.25 ? 185 ASN   A N   1 
ATOM   1312 C  CA  . ASN   A 1 170 ? -16.972 28.992  -8.340  1.00 13.78 ? 185 ASN   A CA  1 
ATOM   1313 C  C   . ASN   A 1 170 ? -17.811 30.089  -7.684  1.00 13.93 ? 185 ASN   A C   1 
ATOM   1314 O  O   . ASN   A 1 170 ? -19.015 30.164  -7.911  1.00 13.75 ? 185 ASN   A O   1 
ATOM   1315 C  CB  . ASN   A 1 170 ? -17.000 29.160  -9.856  1.00 14.70 ? 185 ASN   A CB  1 
ATOM   1316 C  CG  . ASN   A 1 170 ? -16.368 30.437  -10.369 1.00 15.78 ? 185 ASN   A CG  1 
ATOM   1317 O  OD1 . ASN   A 1 170 ? -16.048 31.363  -9.610  1.00 15.18 ? 185 ASN   A OD1 1 
ATOM   1318 N  ND2 . ASN   A 1 170 ? -16.193 30.500  -11.683 1.00 16.42 ? 185 ASN   A ND2 1 
ATOM   1319 N  N   . PRO   A 1 171 ? -17.216 31.014  -6.896  1.00 14.33 ? 186 PRO   A N   1 
ATOM   1320 C  CA  . PRO   A 1 171 ? -18.004 32.060  -6.241  1.00 14.76 ? 186 PRO   A CA  1 
ATOM   1321 C  C   . PRO   A 1 171 ? -18.674 33.065  -7.184  1.00 16.32 ? 186 PRO   A C   1 
ATOM   1322 O  O   . PRO   A 1 171 ? -19.575 33.772  -6.748  1.00 15.84 ? 186 PRO   A O   1 
ATOM   1323 C  CB  . PRO   A 1 171 ? -17.000 32.730  -5.268  1.00 14.92 ? 186 PRO   A CB  1 
ATOM   1324 C  CG  . PRO   A 1 171 ? -15.632 32.414  -5.825  1.00 14.35 ? 186 PRO   A CG  1 
ATOM   1325 C  CD  . PRO   A 1 171 ? -15.778 31.100  -6.583  1.00 14.31 ? 186 PRO   A CD  1 
ATOM   1326 N  N   . ARG   A 1 172 A -18.277 33.084  -8.473  1.00 17.81 ? 186 ARG   A N   1 
ATOM   1327 C  CA  . ARG   A 1 172 A -18.864 33.965  -9.476  1.00 20.07 ? 186 ARG   A CA  1 
ATOM   1328 C  C   . ARG   A 1 172 A -20.180 33.431  -10.057 1.00 21.26 ? 186 ARG   A C   1 
ATOM   1329 O  O   . ARG   A 1 172 A -20.794 34.124  -10.870 1.00 21.10 ? 186 ARG   A O   1 
ATOM   1330 C  CB  . ARG   A 1 172 A -17.921 34.138  -10.676 1.00 21.28 ? 186 ARG   A CB  1 
ATOM   1331 C  CG  . ARG   A 1 172 A -16.541 34.714  -10.389 1.00 22.94 ? 186 ARG   A CG  1 
ATOM   1332 C  CD  . ARG   A 1 172 A -16.389 36.167  -10.797 1.00 24.78 ? 186 ARG   A CD  1 
ATOM   1333 N  NE  . ARG   A 1 172 A -16.462 36.394  -12.247 1.00 24.34 ? 186 ARG   A NE  1 
ATOM   1334 C  CZ  . ARG   A 1 172 A -16.698 37.582  -12.798 1.00 25.67 ? 186 ARG   A CZ  1 
ATOM   1335 N  NH1 . ARG   A 1 172 A -16.751 38.664  -12.035 1.00 27.62 ? 186 ARG   A NH1 1 
ATOM   1336 N  NH2 . ARG   A 1 172 A -16.879 37.695  -14.105 1.00 24.46 ? 186 ARG   A NH2 1 
ATOM   1337 N  N   . LYS   A 1 173 B -20.590 32.200  -9.702  1.00 21.76 ? 186 LYS   A N   1 
ATOM   1338 C  CA  . LYS   A 1 173 B -21.826 31.609  -10.209 1.00 22.97 ? 186 LYS   A CA  1 
ATOM   1339 C  C   . LYS   A 1 173 B -22.787 31.351  -9.046  1.00 23.75 ? 186 LYS   A C   1 
ATOM   1340 O  O   . LYS   A 1 173 B -22.371 31.390  -7.889  1.00 23.71 ? 186 LYS   A O   1 
ATOM   1341 C  CB  . LYS   A 1 173 B -21.572 30.279  -10.929 1.00 24.52 ? 186 LYS   A CB  1 
ATOM   1342 C  CG  . LYS   A 1 173 B -20.423 30.227  -11.938 1.00 25.75 ? 186 LYS   A CG  1 
ATOM   1343 C  CD  . LYS   A 1 173 B -20.668 30.992  -13.230 1.00 26.50 ? 186 LYS   A CD  1 
ATOM   1344 C  CE  . LYS   A 1 173 B -19.498 30.917  -14.163 1.00 27.74 ? 186 LYS   A CE  1 
ATOM   1345 N  NZ  . LYS   A 1 173 B -19.709 31.730  -15.364 1.00 27.92 ? 186 LYS   A NZ  1 
ATOM   1346 N  N   . THR   A 1 174 ? -24.068 31.077  -9.354  1.00 24.61 ? 187 THR   A N   1 
ATOM   1347 C  CA  . THR   A 1 174 ? -25.063 30.766  -8.327  1.00 25.61 ? 187 THR   A CA  1 
ATOM   1348 C  C   . THR   A 1 174 ? -25.121 29.259  -8.057  1.00 23.81 ? 187 THR   A C   1 
ATOM   1349 O  O   . THR   A 1 174 ? -25.577 28.834  -6.996  1.00 25.22 ? 187 THR   A O   1 
ATOM   1350 C  CB  . THR   A 1 174 ? -26.444 31.286  -8.730  1.00 27.91 ? 187 THR   A CB  1 
ATOM   1351 O  OG1 . THR   A 1 174 ? -26.861 30.475  -9.825  1.00 31.49 ? 187 THR   A OG1 1 
ATOM   1352 C  CG2 . THR   A 1 174 ? -26.432 32.754  -9.113  1.00 29.25 ? 187 THR   A CG2 1 
ATOM   1353 N  N   . LYS   A 1 175 ? -24.661 28.459  -9.023  1.00 21.57 ? 188 LYS   A N   1 
ATOM   1354 C  CA  . LYS   A 1 175 ? -24.722 27.008  -8.958  1.00 20.20 ? 188 LYS   A CA  1 
ATOM   1355 C  C   . LYS   A 1 175 ? -24.124 26.505  -7.641  1.00 18.64 ? 188 LYS   A C   1 
ATOM   1356 O  O   . LYS   A 1 175 ? -23.028 26.922  -7.271  1.00 17.51 ? 188 LYS   A O   1 
ATOM   1357 C  CB  . LYS   A 1 175 ? -23.958 26.441  -10.160 1.00 21.18 ? 188 LYS   A CB  1 
ATOM   1358 C  CG  . LYS   A 1 175 ? -24.494 26.830  -11.541 1.00 22.68 ? 188 LYS   A CG  1 
ATOM   1359 C  CD  . LYS   A 1 175 ? -23.855 26.059  -12.693 1.00 23.89 ? 188 LYS   A CD  1 
ATOM   1360 C  CE  . LYS   A 1 175 ? -22.401 26.377  -12.893 1.00 25.52 ? 188 LYS   A CE  1 
ATOM   1361 N  NZ  . LYS   A 1 175 ? -21.711 25.430  -13.780 1.00 26.69 ? 188 LYS   A NZ  1 
ATOM   1362 N  N   . SER   A 1 176 ? -24.835 25.598  -6.949  1.00 16.60 ? 189 SER   A N   1 
ATOM   1363 C  CA  . SER   A 1 176 ? -24.372 25.074  -5.668  1.00 15.93 ? 189 SER   A CA  1 
ATOM   1364 C  C   . SER   A 1 176 ? -25.274 23.943  -5.164  1.00 14.89 ? 189 SER   A C   1 
ATOM   1365 O  O   . SER   A 1 176 ? -26.458 23.887  -5.489  1.00 14.84 ? 189 SER   A O   1 
ATOM   1366 C  CB  . SER   A 1 176 ? -24.292 26.184  -4.624  1.00 15.46 ? 189 SER   A CB  1 
ATOM   1367 O  OG  . SER   A 1 176 ? -23.477 25.807  -3.521  1.00 15.70 ? 189 SER   A OG  1 
ATOM   1368 N  N   . ALA   A 1 177 ? -24.703 23.063  -4.331  1.00 14.49 ? 190 ALA   A N   1 
ATOM   1369 C  CA  . ALA   A 1 177 ? -25.479 22.247  -3.403  1.00 14.10 ? 190 ALA   A CA  1 
ATOM   1370 C  C   . ALA   A 1 177 ? -26.032 23.117  -2.273  1.00 13.79 ? 190 ALA   A C   1 
ATOM   1371 O  O   . ALA   A 1 177 ? -25.457 24.165  -1.972  1.00 13.48 ? 190 ALA   A O   1 
ATOM   1372 C  CB  . ALA   A 1 177 ? -24.603 21.142  -2.849  1.00 14.60 ? 190 ALA   A CB  1 
ATOM   1373 N  N   . PHE   A 1 178 ? -27.130 22.670  -1.635  1.00 13.90 ? 191 PHE   A N   1 
ATOM   1374 C  CA  . PHE   A 1 178 ? -27.704 23.364  -0.485  1.00 13.85 ? 191 PHE   A CA  1 
ATOM   1375 C  C   . PHE   A 1 178 ? -28.397 22.373  0.465   1.00 14.25 ? 191 PHE   A C   1 
ATOM   1376 O  O   . PHE   A 1 178 ? -28.243 21.155  0.339   1.00 12.93 ? 191 PHE   A O   1 
ATOM   1377 C  CB  . PHE   A 1 178 ? -28.612 24.484  -1.016  1.00 14.53 ? 191 PHE   A CB  1 
ATOM   1378 C  CG  . PHE   A 1 178 ? -29.038 25.537  0.004   1.00 15.03 ? 191 PHE   A CG  1 
ATOM   1379 C  CD1 . PHE   A 1 178 ? -28.116 26.121  0.870   1.00 15.34 ? 191 PHE   A CD1 1 
ATOM   1380 C  CD2 . PHE   A 1 178 ? -30.374 25.908  0.127   1.00 16.18 ? 191 PHE   A CD2 1 
ATOM   1381 C  CE1 . PHE   A 1 178 ? -28.516 27.060  1.813   1.00 15.90 ? 191 PHE   A CE1 1 
ATOM   1382 C  CE2 . PHE   A 1 178 ? -30.771 26.846  1.072   1.00 16.30 ? 191 PHE   A CE2 1 
ATOM   1383 C  CZ  . PHE   A 1 178 ? -29.844 27.417  1.916   1.00 16.31 ? 191 PHE   A CZ  1 
ATOM   1384 N  N   . LYS   A 1 179 ? -29.117 22.914  1.462   1.00 14.29 ? 192 LYS   A N   1 
ATOM   1385 C  CA  . LYS   A 1 179 ? -29.831 22.128  2.459   1.00 15.66 ? 192 LYS   A CA  1 
ATOM   1386 C  C   . LYS   A 1 179 ? -30.730 21.087  1.796   1.00 14.21 ? 192 LYS   A C   1 
ATOM   1387 O  O   . LYS   A 1 179 ? -31.452 21.412  0.857   1.00 14.22 ? 192 LYS   A O   1 
ATOM   1388 C  CB  . LYS   A 1 179 ? -30.771 22.989  3.313   1.00 18.10 ? 192 LYS   A CB  1 
ATOM   1389 C  CG  . LYS   A 1 179 ? -30.131 23.912  4.323   1.00 20.59 ? 192 LYS   A CG  1 
ATOM   1390 C  CD  . LYS   A 1 179 ? -31.188 24.545  5.221   1.00 23.52 ? 192 LYS   A CD  1 
ATOM   1391 C  CE  . LYS   A 1 179 ? -30.619 25.374  6.319   1.00 26.48 ? 192 LYS   A CE  1 
ATOM   1392 N  NZ  . LYS   A 1 179 ? -31.677 25.966  7.149   1.00 29.05 ? 192 LYS   A NZ  1 
ATOM   1393 N  N   . GLY   A 1 180 ? -30.699 19.859  2.338   1.00 12.44 ? 193 GLY   A N   1 
ATOM   1394 C  CA  . GLY   A 1 180 ? -31.408 18.722  1.774   1.00 11.80 ? 193 GLY   A CA  1 
ATOM   1395 C  C   . GLY   A 1 180 ? -30.501 17.833  0.917   1.00 11.16 ? 193 GLY   A C   1 
ATOM   1396 O  O   . GLY   A 1 180 ? -30.867 16.698  0.624   1.00 11.13 ? 193 GLY   A O   1 
ATOM   1397 N  N   . ASP   A 1 181 ? -29.333 18.359  0.509   1.00 10.82 ? 194 ASP   A N   1 
ATOM   1398 C  CA  . ASP   A 1 181 ? -28.419 17.669  -0.394  1.00 10.31 ? 194 ASP   A CA  1 
ATOM   1399 C  C   . ASP   A 1 181 ? -27.276 16.975  0.356   1.00 10.05 ? 194 ASP   A C   1 
ATOM   1400 O  O   . ASP   A 1 181 ? -26.532 16.210  -0.263  1.00 9.81  ? 194 ASP   A O   1 
ATOM   1401 C  CB  . ASP   A 1 181 ? -27.844 18.611  -1.447  1.00 10.12 ? 194 ASP   A CB  1 
ATOM   1402 C  CG  . ASP   A 1 181 ? -28.835 19.199  -2.445  1.00 10.12 ? 194 ASP   A CG  1 
ATOM   1403 O  OD1 . ASP   A 1 181 ? -29.750 18.454  -2.886  1.00 9.95  ? 194 ASP   A OD1 1 
ATOM   1404 O  OD2 . ASP   A 1 181 ? -28.662 20.384  -2.821  1.00 9.67  ? 194 ASP   A OD2 1 
ATOM   1405 N  N   . SER   A 1 182 ? -27.105 17.257  1.660   1.00 9.72  ? 195 SER   A N   1 
ATOM   1406 C  CA  . SER   A 1 182 ? -26.040 16.652  2.455   1.00 9.74  ? 195 SER   A CA  1 
ATOM   1407 C  C   . SER   A 1 182 ? -26.084 15.121  2.351   1.00 10.00 ? 195 SER   A C   1 
ATOM   1408 O  O   . SER   A 1 182 ? -27.171 14.527  2.341   1.00 9.63  ? 195 SER   A O   1 
ATOM   1409 C  CB  . SER   A 1 182 ? -26.098 17.103  3.903   1.00 9.94  ? 195 SER   A CB  1 
ATOM   1410 O  OG  . SER   A 1 182 ? -25.895 18.504  4.059   1.00 10.05 ? 195 SER   A OG  1 
ATOM   1411 N  N   . GLY   A 1 183 ? -24.892 14.501  2.222   1.00 9.96  ? 196 GLY   A N   1 
ATOM   1412 C  CA  . GLY   A 1 183 ? -24.736 13.053  2.129   1.00 9.97  ? 196 GLY   A CA  1 
ATOM   1413 C  C   . GLY   A 1 183 ? -24.620 12.535  0.691   1.00 10.35 ? 196 GLY   A C   1 
ATOM   1414 O  O   . GLY   A 1 183 ? -24.241 11.381  0.474   1.00 9.82  ? 196 GLY   A O   1 
ATOM   1415 N  N   . GLY   A 1 184 ? -24.957 13.375  -0.300  1.00 10.75 ? 197 GLY   A N   1 
ATOM   1416 C  CA  . GLY   A 1 184 ? -24.875 12.983  -1.697  1.00 11.20 ? 197 GLY   A CA  1 
ATOM   1417 C  C   . GLY   A 1 184 ? -23.434 12.943  -2.202  1.00 11.86 ? 197 GLY   A C   1 
ATOM   1418 O  O   . GLY   A 1 184 ? -22.551 13.590  -1.626  1.00 11.64 ? 197 GLY   A O   1 
ATOM   1419 N  N   . PRO   A 1 185 ? -23.167 12.186  -3.297  1.00 12.28 ? 198 PRO   A N   1 
ATOM   1420 C  CA  . PRO   A 1 185 ? -21.830 12.081  -3.887  1.00 12.70 ? 198 PRO   A CA  1 
ATOM   1421 C  C   . PRO   A 1 185 ? -21.457 13.189  -4.873  1.00 13.55 ? 198 PRO   A C   1 
ATOM   1422 O  O   . PRO   A 1 185 ? -22.319 13.734  -5.564  1.00 13.10 ? 198 PRO   A O   1 
ATOM   1423 C  CB  . PRO   A 1 185 ? -21.918 10.712  -4.595  1.00 12.82 ? 198 PRO   A CB  1 
ATOM   1424 C  CG  . PRO   A 1 185 ? -23.344 10.669  -5.106  1.00 12.71 ? 198 PRO   A CG  1 
ATOM   1425 C  CD  . PRO   A 1 185 ? -24.159 11.367  -4.020  1.00 12.56 ? 198 PRO   A CD  1 
ATOM   1426 N  N   . LEU   A 1 186 ? -20.157 13.516  -4.892  1.00 14.11 ? 199 LEU   A N   1 
ATOM   1427 C  CA  . LEU   A 1 186 ? -19.528 14.339  -5.913  1.00 14.81 ? 199 LEU   A CA  1 
ATOM   1428 C  C   . LEU   A 1 186 ? -18.726 13.416  -6.826  1.00 15.69 ? 199 LEU   A C   1 
ATOM   1429 O  O   . LEU   A 1 186 ? -17.834 12.724  -6.342  1.00 16.28 ? 199 LEU   A O   1 
ATOM   1430 C  CB  . LEU   A 1 186 ? -18.608 15.360  -5.238  1.00 14.76 ? 199 LEU   A CB  1 
ATOM   1431 C  CG  . LEU   A 1 186 ? -17.889 16.339  -6.173  1.00 15.07 ? 199 LEU   A CG  1 
ATOM   1432 C  CD1 . LEU   A 1 186 ? -18.849 17.396  -6.680  1.00 15.06 ? 199 LEU   A CD1 1 
ATOM   1433 C  CD2 . LEU   A 1 186 ? -16.689 16.992  -5.509  1.00 15.44 ? 199 LEU   A CD2 1 
ATOM   1434 N  N   . LEU   A 1 187 ? -19.052 13.406  -8.125  1.00 17.15 ? 200 LEU   A N   1 
ATOM   1435 C  CA  . LEU   A 1 187 ? -18.375 12.556  -9.096  1.00 18.85 ? 200 LEU   A CA  1 
ATOM   1436 C  C   . LEU   A 1 187 ? -17.505 13.410  -10.021 1.00 19.31 ? 200 LEU   A C   1 
ATOM   1437 O  O   . LEU   A 1 187 ? -17.991 14.374  -10.612 1.00 18.00 ? 200 LEU   A O   1 
ATOM   1438 C  CB  . LEU   A 1 187 ? -19.375 11.732  -9.906  1.00 19.97 ? 200 LEU   A CB  1 
ATOM   1439 C  CG  . LEU   A 1 187 ? -20.105 10.611  -9.155  1.00 21.89 ? 200 LEU   A CG  1 
ATOM   1440 C  CD1 . LEU   A 1 187 ? -21.391 11.123  -8.524  1.00 22.78 ? 200 LEU   A CD1 1 
ATOM   1441 C  CD2 . LEU   A 1 187 ? -20.388 9.435   -10.074 1.00 23.06 ? 200 LEU   A CD2 1 
ATOM   1442 N  N   . CYS   A 1 188 ? -16.221 13.030  -10.137 1.00 20.49 ? 201 CYS   A N   1 
ATOM   1443 C  CA  . CYS   A 1 188 ? -15.274 13.669  -11.041 1.00 22.11 ? 201 CYS   A CA  1 
ATOM   1444 C  C   . CYS   A 1 188 ? -14.802 12.636  -12.070 1.00 24.70 ? 201 CYS   A C   1 
ATOM   1445 O  O   . CYS   A 1 188 ? -14.143 11.663  -11.713 1.00 24.80 ? 201 CYS   A O   1 
ATOM   1446 C  CB  . CYS   A 1 188 ? -14.096 14.272  -10.279 1.00 21.81 ? 201 CYS   A CB  1 
ATOM   1447 S  SG  . CYS   A 1 188 ? -14.560 15.362  -8.902  1.00 20.87 ? 201 CYS   A SG  1 
ATOM   1448 N  N   . ALA   A 1 189 ? -15.183 12.838  -13.338 1.00 26.87 ? 202 ALA   A N   1 
ATOM   1449 C  CA  . ALA   A 1 189 ? -14.938 11.880  -14.411 1.00 29.56 ? 202 ALA   A CA  1 
ATOM   1450 C  C   . ALA   A 1 189 ? -15.431 10.485  -14.021 1.00 29.86 ? 202 ALA   A C   1 
ATOM   1451 O  O   . ALA   A 1 189 ? -14.729 9.494   -14.218 1.00 31.57 ? 202 ALA   A O   1 
ATOM   1452 C  CB  . ALA   A 1 189 ? -13.464 11.871  -14.781 1.00 30.06 ? 202 ALA   A CB  1 
ATOM   1453 N  N   . GLY   A 1 190 ? -16.636 10.420  -13.442 1.00 29.98 ? 207 GLY   A N   1 
ATOM   1454 C  CA  . GLY   A 1 190 ? -17.325 9.159   -13.211 1.00 29.89 ? 207 GLY   A CA  1 
ATOM   1455 C  C   . GLY   A 1 190 ? -16.935 8.475   -11.901 1.00 29.67 ? 207 GLY   A C   1 
ATOM   1456 O  O   . GLY   A 1 190 ? -17.485 7.422   -11.588 1.00 29.99 ? 207 GLY   A O   1 
ATOM   1457 N  N   . VAL   A 1 191 ? -16.023 9.089   -11.133 1.00 29.15 ? 208 VAL   A N   1 
ATOM   1458 C  CA  . VAL   A 1 191 ? -15.447 8.485   -9.939  1.00 28.40 ? 208 VAL   A CA  1 
ATOM   1459 C  C   . VAL   A 1 191 ? -15.838 9.319   -8.717  1.00 26.10 ? 208 VAL   A C   1 
ATOM   1460 O  O   . VAL   A 1 191 ? -15.694 10.540  -8.730  1.00 25.93 ? 208 VAL   A O   1 
ATOM   1461 C  CB  . VAL   A 1 191 ? -13.913 8.408   -10.095 1.00 29.78 ? 208 VAL   A CB  1 
ATOM   1462 C  CG1 . VAL   A 1 191 ? -13.240 7.795   -8.873  1.00 30.42 ? 208 VAL   A CG1 1 
ATOM   1463 C  CG2 . VAL   A 1 191 ? -13.497 7.659   -11.357 1.00 30.64 ? 208 VAL   A CG2 1 
ATOM   1464 N  N   . ALA   A 1 192 ? -16.304 8.655   -7.652  1.00 24.03 ? 209 ALA   A N   1 
ATOM   1465 C  CA  . ALA   A 1 192 ? -16.726 9.338   -6.435  1.00 23.70 ? 209 ALA   A CA  1 
ATOM   1466 C  C   . ALA   A 1 192 ? -15.512 9.883   -5.677  1.00 22.16 ? 209 ALA   A C   1 
ATOM   1467 O  O   . ALA   A 1 192 ? -14.642 9.111   -5.278  1.00 24.18 ? 209 ALA   A O   1 
ATOM   1468 C  CB  . ALA   A 1 192 ? -17.523 8.385   -5.568  1.00 23.76 ? 209 ALA   A CB  1 
ATOM   1469 N  N   . GLN   A 1 193 ? -15.473 11.206  -5.457  1.00 19.71 ? 210 GLN   A N   1 
ATOM   1470 C  CA  . GLN   A 1 193 ? -14.358 11.849  -4.770  1.00 18.08 ? 210 GLN   A CA  1 
ATOM   1471 C  C   . GLN   A 1 193 ? -14.788 12.562  -3.483  1.00 16.81 ? 210 GLN   A C   1 
ATOM   1472 O  O   . GLN   A 1 193 ? -13.937 12.814  -2.632  1.00 16.61 ? 210 GLN   A O   1 
ATOM   1473 C  CB  . GLN   A 1 193 ? -13.665 12.871  -5.675  1.00 18.60 ? 210 GLN   A CB  1 
ATOM   1474 C  CG  . GLN   A 1 193 ? -13.040 12.294  -6.944  1.00 18.97 ? 210 GLN   A CG  1 
ATOM   1475 C  CD  . GLN   A 1 193 ? -11.795 11.460  -6.717  0.50 18.45 ? 210 GLN   A CD  1 
ATOM   1476 O  OE1 . GLN   A 1 193 ? -11.185 10.955  -7.667  0.50 18.85 ? 210 GLN   A OE1 1 
ATOM   1477 N  NE2 . GLN   A 1 193 ? -11.399 11.300  -5.464  0.50 18.03 ? 210 GLN   A NE2 1 
ATOM   1478 N  N   . GLY   A 1 194 ? -16.078 12.911  -3.332  1.00 15.12 ? 211 GLY   A N   1 
ATOM   1479 C  CA  . GLY   A 1 194 ? -16.522 13.689  -2.179  1.00 14.54 ? 211 GLY   A CA  1 
ATOM   1480 C  C   . GLY   A 1 194 ? -17.959 13.386  -1.747  1.00 13.48 ? 211 GLY   A C   1 
ATOM   1481 O  O   . GLY   A 1 194 ? -18.690 12.696  -2.458  1.00 13.06 ? 211 GLY   A O   1 
ATOM   1482 N  N   . ILE   A 1 195 ? -18.330 13.931  -0.576  1.00 12.95 ? 212 ILE   A N   1 
ATOM   1483 C  CA  . ILE   A 1 195 ? -19.666 13.848  0.010   1.00 12.92 ? 212 ILE   A CA  1 
ATOM   1484 C  C   . ILE   A 1 195 ? -20.078 15.262  0.433   1.00 12.20 ? 212 ILE   A C   1 
ATOM   1485 O  O   . ILE   A 1 195 ? -19.290 15.950  1.080   1.00 11.85 ? 212 ILE   A O   1 
ATOM   1486 C  CB  . ILE   A 1 195 ? -19.692 12.892  1.227   1.00 13.54 ? 212 ILE   A CB  1 
ATOM   1487 C  CG1 . ILE   A 1 195 ? -19.090 11.521  0.922   1.00 14.19 ? 212 ILE   A CG1 1 
ATOM   1488 C  CG2 . ILE   A 1 195 ? -21.105 12.765  1.795   1.00 13.81 ? 212 ILE   A CG2 1 
ATOM   1489 C  CD1 . ILE   A 1 195 ? -18.844 10.663  2.154   1.00 14.83 ? 212 ILE   A CD1 1 
ATOM   1490 N  N   . VAL   A 1 196 ? -21.305 15.687  0.088   1.00 11.61 ? 213 VAL   A N   1 
ATOM   1491 C  CA  . VAL   A 1 196 ? -21.817 17.007  0.457   1.00 11.42 ? 213 VAL   A CA  1 
ATOM   1492 C  C   . VAL   A 1 196 ? -21.849 17.123  1.984   1.00 11.32 ? 213 VAL   A C   1 
ATOM   1493 O  O   . VAL   A 1 196 ? -22.427 16.252  2.647   1.00 10.54 ? 213 VAL   A O   1 
ATOM   1494 C  CB  . VAL   A 1 196 ? -23.228 17.302  -0.092  1.00 11.47 ? 213 VAL   A CB  1 
ATOM   1495 C  CG1 . VAL   A 1 196 ? -23.706 18.689  0.333   1.00 11.54 ? 213 VAL   A CG1 1 
ATOM   1496 C  CG2 . VAL   A 1 196 ? -23.342 17.147  -1.607  1.00 11.42 ? 213 VAL   A CG2 1 
ATOM   1497 N  N   . SER   A 1 197 ? -21.280 18.216  2.535   1.00 11.17 ? 214 SER   A N   1 
ATOM   1498 C  CA  . SER   A 1 197 ? -21.292 18.446  3.980   1.00 11.21 ? 214 SER   A CA  1 
ATOM   1499 C  C   . SER   A 1 197 ? -22.078 19.710  4.365   1.00 11.40 ? 214 SER   A C   1 
ATOM   1500 O  O   . SER   A 1 197 ? -23.216 19.585  4.828   1.00 11.30 ? 214 SER   A O   1 
ATOM   1501 C  CB  . SER   A 1 197 ? -19.883 18.438  4.561   1.00 11.36 ? 214 SER   A CB  1 
ATOM   1502 O  OG  . SER   A 1 197 ? -19.910 18.418  5.983   1.00 10.94 ? 214 SER   A OG  1 
ATOM   1503 N  N   . TYR   A 1 198 ? -21.485 20.912  4.226   1.00 11.04 ? 215 TYR   A N   1 
ATOM   1504 C  CA  . TYR   A 1 198 ? -22.132 22.153  4.664   1.00 11.44 ? 215 TYR   A CA  1 
ATOM   1505 C  C   . TYR   A 1 198 ? -21.677 23.350  3.816   1.00 11.37 ? 215 TYR   A C   1 
ATOM   1506 O  O   . TYR   A 1 198 ? -20.757 23.236  3.017   1.00 11.13 ? 215 TYR   A O   1 
ATOM   1507 C  CB  . TYR   A 1 198 ? -21.887 22.447  6.154   1.00 11.54 ? 215 TYR   A CB  1 
ATOM   1508 C  CG  . TYR   A 1 198 ? -20.465 22.839  6.547   1.00 11.87 ? 215 TYR   A CG  1 
ATOM   1509 C  CD1 . TYR   A 1 198 ? -19.496 21.875  6.797   1.00 11.82 ? 215 TYR   A CD1 1 
ATOM   1510 C  CD2 . TYR   A 1 198 ? -20.094 24.173  6.694   1.00 12.43 ? 215 TYR   A CD2 1 
ATOM   1511 C  CE1 . TYR   A 1 198 ? -18.201 22.217  7.155   1.00 12.17 ? 215 TYR   A CE1 1 
ATOM   1512 C  CE2 . TYR   A 1 198 ? -18.798 24.529  7.046   1.00 12.62 ? 215 TYR   A CE2 1 
ATOM   1513 C  CZ  . TYR   A 1 198 ? -17.849 23.550  7.278   1.00 12.69 ? 215 TYR   A CZ  1 
ATOM   1514 O  OH  . TYR   A 1 198 ? -16.565 23.887  7.623   1.00 13.37 ? 215 TYR   A OH  1 
ATOM   1515 N  N   . GLY   A 1 199 ? -22.318 24.507  4.042   1.00 11.81 ? 216 GLY   A N   1 
ATOM   1516 C  CA  . GLY   A 1 199 ? -21.977 25.783  3.419   1.00 12.11 ? 216 GLY   A CA  1 
ATOM   1517 C  C   . GLY   A 1 199 ? -22.579 26.960  4.200   1.00 12.40 ? 216 GLY   A C   1 
ATOM   1518 O  O   . GLY   A 1 199 ? -22.788 26.847  5.401   1.00 12.35 ? 216 GLY   A O   1 
ATOM   1519 N  N   . ARG   A 1 200 ? -22.872 28.075  3.509   1.00 13.07 ? 217 ARG   A N   1 
ATOM   1520 C  CA  . ARG   A 1 200 ? -23.438 29.278  4.115   1.00 13.46 ? 217 ARG   A CA  1 
ATOM   1521 C  C   . ARG   A 1 200 ? -24.966 29.221  4.146   1.00 14.07 ? 217 ARG   A C   1 
ATOM   1522 O  O   . ARG   A 1 200 ? -25.589 28.653  3.250   1.00 14.12 ? 217 ARG   A O   1 
ATOM   1523 C  CB  . ARG   A 1 200 ? -23.039 30.540  3.337   1.00 13.81 ? 217 ARG   A CB  1 
ATOM   1524 C  CG  . ARG   A 1 200 ? -21.598 30.986  3.548   1.00 14.30 ? 217 ARG   A CG  1 
ATOM   1525 C  CD  . ARG   A 1 200 ? -21.160 32.140  2.651   1.00 14.78 ? 217 ARG   A CD  1 
ATOM   1526 N  NE  . ARG   A 1 200 ? -21.957 33.364  2.811   1.00 15.07 ? 217 ARG   A NE  1 
ATOM   1527 C  CZ  . ARG   A 1 200 ? -21.602 34.472  3.474   1.00 15.55 ? 217 ARG   A CZ  1 
ATOM   1528 N  NH1 . ARG   A 1 200 ? -20.472 34.532  4.160   1.00 15.37 ? 217 ARG   A NH1 1 
ATOM   1529 N  NH2 . ARG   A 1 200 ? -22.406 35.519  3.476   1.00 15.82 ? 217 ARG   A NH2 1 
ATOM   1530 N  N   . SER   A 1 201 ? -25.562 29.889  5.148   1.00 14.62 ? 218 SER   A N   1 
ATOM   1531 C  CA  . SER   A 1 201 ? -27.012 30.010  5.268   1.00 15.15 ? 218 SER   A CA  1 
ATOM   1532 C  C   . SER   A 1 201 ? -27.630 30.753  4.082   1.00 15.48 ? 218 SER   A C   1 
ATOM   1533 O  O   . SER   A 1 201 ? -28.805 30.543  3.783   1.00 16.61 ? 218 SER   A O   1 
ATOM   1534 C  CB  . SER   A 1 201 ? -27.415 30.665  6.590   1.00 15.75 ? 218 SER   A CB  1 
ATOM   1535 O  OG  . SER   A 1 201 ? -26.916 31.994  6.710   1.00 15.80 ? 218 SER   A OG  1 
ATOM   1536 N  N   . ASP   A 1 202 ? -26.856 31.611  3.396   1.00 15.48 ? 219 ASP   A N   1 
ATOM   1537 C  CA  . ASP   A 1 202 ? -27.377 32.363  2.261   1.00 15.69 ? 219 ASP   A CA  1 
ATOM   1538 C  C   . ASP   A 1 202 ? -27.083 31.672  0.926   1.00 15.74 ? 219 ASP   A C   1 
ATOM   1539 O  O   . ASP   A 1 202 ? -27.411 32.227  -0.117  1.00 15.52 ? 219 ASP   A O   1 
ATOM   1540 C  CB  . ASP   A 1 202 ? -26.863 33.795  2.251   1.00 15.86 ? 219 ASP   A CB  1 
ATOM   1541 C  CG  . ASP   A 1 202 ? -25.379 33.985  1.962   1.00 15.70 ? 219 ASP   A CG  1 
ATOM   1542 O  OD1 . ASP   A 1 202 ? -24.668 32.973  1.740   1.00 14.74 ? 219 ASP   A OD1 1 
ATOM   1543 O  OD2 . ASP   A 1 202 ? -24.944 35.155  1.959   1.00 15.43 ? 219 ASP   A OD2 1 
ATOM   1544 N  N   . ALA   A 1 203 ? -26.437 30.497  0.976   1.00 15.55 ? 220 ALA   A N   1 
ATOM   1545 C  CA  . ALA   A 1 203 ? -26.220 29.603  -0.159  1.00 16.03 ? 220 ALA   A CA  1 
ATOM   1546 C  C   . ALA   A 1 203 ? -25.154 30.091  -1.149  1.00 16.16 ? 220 ALA   A C   1 
ATOM   1547 O  O   . ALA   A 1 203 ? -25.005 29.474  -2.203  1.00 17.28 ? 220 ALA   A O   1 
ATOM   1548 C  CB  . ALA   A 1 203 ? -27.534 29.320  -0.875  1.00 16.38 ? 220 ALA   A CB  1 
ATOM   1549 N  N   . LYS   A 1 204 ? -24.382 31.142  -0.829  1.00 15.40 ? 221 LYS   A N   1 
ATOM   1550 C  CA  . LYS   A 1 204 ? -23.324 31.597  -1.729  1.00 15.75 ? 221 LYS   A CA  1 
ATOM   1551 C  C   . LYS   A 1 204 ? -22.180 30.575  -1.750  1.00 14.16 ? 221 LYS   A C   1 
ATOM   1552 O  O   . LYS   A 1 204 ? -21.677 30.213  -0.693  1.00 13.59 ? 221 LYS   A O   1 
ATOM   1553 C  CB  . LYS   A 1 204 ? -22.769 32.971  -1.325  1.00 16.88 ? 221 LYS   A CB  1 
ATOM   1554 C  CG  . LYS   A 1 204 ? -23.713 34.166  -1.499  1.00 19.28 ? 221 LYS   A CG  1 
ATOM   1555 C  CD  . LYS   A 1 204 ? -23.063 35.514  -1.185  1.00 20.86 ? 221 LYS   A CD  1 
ATOM   1556 C  CE  . LYS   A 1 204 ? -24.019 36.685  -1.174  1.00 22.36 ? 221 LYS   A CE  1 
ATOM   1557 N  NZ  . LYS   A 1 204 ? -23.336 37.938  -0.845  0.10 21.83 ? 221 LYS   A NZ  1 
ATOM   1558 N  N   . PRO   A 1 205 ? -21.767 30.113  -2.945  1.00 13.07 ? 224 PRO   A N   1 
ATOM   1559 C  CA  . PRO   A 1 205 ? -20.700 29.128  -3.058  1.00 12.87 ? 224 PRO   A CA  1 
ATOM   1560 C  C   . PRO   A 1 205 ? -19.335 29.774  -2.812  1.00 12.22 ? 224 PRO   A C   1 
ATOM   1561 O  O   . PRO   A 1 205 ? -19.221 31.002  -2.874  1.00 12.47 ? 224 PRO   A O   1 
ATOM   1562 C  CB  . PRO   A 1 205 ? -20.817 28.526  -4.481  1.00 13.25 ? 224 PRO   A CB  1 
ATOM   1563 C  CG  . PRO   A 1 205 ? -21.654 29.524  -5.264  1.00 13.45 ? 224 PRO   A CG  1 
ATOM   1564 C  CD  . PRO   A 1 205 ? -22.409 30.366  -4.246  1.00 13.44 ? 224 PRO   A CD  1 
ATOM   1565 N  N   . PRO   A 1 206 ? -18.251 29.000  -2.552  1.00 11.38 ? 225 PRO   A N   1 
ATOM   1566 C  CA  . PRO   A 1 206 ? -18.275 27.531  -2.535  1.00 11.08 ? 225 PRO   A CA  1 
ATOM   1567 C  C   . PRO   A 1 206 ? -18.837 26.875  -1.272  1.00 10.54 ? 225 PRO   A C   1 
ATOM   1568 O  O   . PRO   A 1 206 ? -19.055 27.552  -0.273  1.00 10.24 ? 225 PRO   A O   1 
ATOM   1569 C  CB  . PRO   A 1 206 ? -16.783 27.204  -2.699  1.00 11.29 ? 225 PRO   A CB  1 
ATOM   1570 C  CG  . PRO   A 1 206 ? -16.085 28.313  -1.960  1.00 11.28 ? 225 PRO   A CG  1 
ATOM   1571 C  CD  . PRO   A 1 206 ? -16.906 29.538  -2.292  1.00 11.43 ? 225 PRO   A CD  1 
ATOM   1572 N  N   . ALA   A 1 207 ? -19.052 25.550  -1.344  1.00 10.33 ? 226 ALA   A N   1 
ATOM   1573 C  CA  . ALA   A 1 207 ? -19.438 24.732  -0.201  1.00 10.50 ? 226 ALA   A CA  1 
ATOM   1574 C  C   . ALA   A 1 207 ? -18.334 23.730  0.146   1.00 10.58 ? 226 ALA   A C   1 
ATOM   1575 O  O   . ALA   A 1 207 ? -17.404 23.535  -0.636  1.00 10.33 ? 226 ALA   A O   1 
ATOM   1576 C  CB  . ALA   A 1 207 ? -20.741 24.022  -0.497  1.00 10.47 ? 226 ALA   A CB  1 
ATOM   1577 N  N   . VAL   A 1 208 ? -18.477 23.083  1.318   1.00 10.70 ? 227 VAL   A N   1 
ATOM   1578 C  CA  . VAL   A 1 208 ? -17.488 22.164  1.871   1.00 10.76 ? 227 VAL   A CA  1 
ATOM   1579 C  C   . VAL   A 1 208 ? -17.977 20.721  1.714   1.00 11.06 ? 227 VAL   A C   1 
ATOM   1580 O  O   . VAL   A 1 208 ? -19.101 20.410  2.103   1.00 11.49 ? 227 VAL   A O   1 
ATOM   1581 C  CB  . VAL   A 1 208 ? -17.241 22.490  3.358   1.00 11.01 ? 227 VAL   A CB  1 
ATOM   1582 C  CG1 . VAL   A 1 208 ? -16.155 21.608  3.972   1.00 11.26 ? 227 VAL   A CG1 1 
ATOM   1583 C  CG2 . VAL   A 1 208 ? -16.925 23.963  3.581   1.00 11.03 ? 227 VAL   A CG2 1 
ATOM   1584 N  N   . PHE   A 1 209 ? -17.110 19.850  1.172   1.00 10.95 ? 228 PHE   A N   1 
ATOM   1585 C  CA  . PHE   A 1 209 ? -17.399 18.437  0.957   1.00 10.93 ? 228 PHE   A CA  1 
ATOM   1586 C  C   . PHE   A 1 209 ? -16.355 17.602  1.706   1.00 11.37 ? 228 PHE   A C   1 
ATOM   1587 O  O   . PHE   A 1 209 ? -15.213 18.026  1.840   1.00 11.36 ? 228 PHE   A O   1 
ATOM   1588 C  CB  . PHE   A 1 209 ? -17.374 18.068  -0.537  1.00 10.82 ? 228 PHE   A CB  1 
ATOM   1589 C  CG  . PHE   A 1 209 ? -18.507 18.561  -1.441  1.00 10.47 ? 228 PHE   A CG  1 
ATOM   1590 C  CD1 . PHE   A 1 209 ? -18.847 19.909  -1.523  1.00 10.32 ? 228 PHE   A CD1 1 
ATOM   1591 C  CD2 . PHE   A 1 209 ? -19.219 17.662  -2.234  1.00 10.37 ? 228 PHE   A CD2 1 
ATOM   1592 C  CE1 . PHE   A 1 209 ? -19.868 20.336  -2.366  1.00 10.37 ? 228 PHE   A CE1 1 
ATOM   1593 C  CE2 . PHE   A 1 209 ? -20.239 18.092  -3.077  1.00 10.41 ? 228 PHE   A CE2 1 
ATOM   1594 C  CZ  . PHE   A 1 209 ? -20.568 19.429  -3.139  1.00 10.23 ? 228 PHE   A CZ  1 
ATOM   1595 N  N   . THR   A 1 210 ? -16.745 16.402  2.164   1.00 12.30 ? 229 THR   A N   1 
ATOM   1596 C  CA  . THR   A 1 210 ? -15.839 15.440  2.782   1.00 12.50 ? 229 THR   A CA  1 
ATOM   1597 C  C   . THR   A 1 210 ? -14.990 14.777  1.695   1.00 13.70 ? 229 THR   A C   1 
ATOM   1598 O  O   . THR   A 1 210 ? -15.533 14.358  0.672   1.00 13.19 ? 229 THR   A O   1 
ATOM   1599 C  CB  . THR   A 1 210 ? -16.653 14.403  3.561   1.00 12.93 ? 229 THR   A CB  1 
ATOM   1600 O  OG1 . THR   A 1 210 ? -17.437 15.086  4.538   1.00 12.98 ? 229 THR   A OG1 1 
ATOM   1601 C  CG2 . THR   A 1 210 ? -15.782 13.364  4.251   1.00 13.08 ? 229 THR   A CG2 1 
ATOM   1602 N  N   . ARG   A 1 211 ? -13.669 14.664  1.936   1.00 14.84 ? 230 ARG   A N   1 
ATOM   1603 C  CA  . ARG   A 1 211 ? -12.734 14.030  1.010   1.00 16.58 ? 230 ARG   A CA  1 
ATOM   1604 C  C   . ARG   A 1 211 ? -12.658 12.523  1.279   1.00 17.57 ? 230 ARG   A C   1 
ATOM   1605 O  O   . ARG   A 1 211 ? -12.123 12.096  2.304   1.00 17.33 ? 230 ARG   A O   1 
ATOM   1606 C  CB  . ARG   A 1 211 ? -11.352 14.689  1.148   1.00 17.65 ? 230 ARG   A CB  1 
ATOM   1607 C  CG  . ARG   A 1 211 ? -10.302 14.215  0.151   1.00 18.43 ? 230 ARG   A CG  1 
ATOM   1608 C  CD  . ARG   A 1 211 ? -8.874  14.626  0.529   1.00 19.42 ? 230 ARG   A CD  1 
ATOM   1609 N  NE  . ARG   A 1 211 ? -8.580  16.052  0.341   1.00 19.79 ? 230 ARG   A NE  1 
ATOM   1610 C  CZ  . ARG   A 1 211 ? -8.296  16.652  -0.816  1.00 20.76 ? 230 ARG   A CZ  1 
ATOM   1611 N  NH1 . ARG   A 1 211 ? -8.207  15.963  -1.944  1.00 21.60 ? 230 ARG   A NH1 1 
ATOM   1612 N  NH2 . ARG   A 1 211 ? -8.102  17.956  -0.852  1.00 20.83 ? 230 ARG   A NH2 1 
ATOM   1613 N  N   . ILE   A 1 212 ? -13.190 11.723  0.342   1.00 18.56 ? 231 ILE   A N   1 
ATOM   1614 C  CA  . ILE   A 1 212 ? -13.416 10.295  0.546   1.00 20.25 ? 231 ILE   A CA  1 
ATOM   1615 C  C   . ILE   A 1 212 ? -12.102 9.534   0.761   1.00 21.06 ? 231 ILE   A C   1 
ATOM   1616 O  O   . ILE   A 1 212 ? -12.038 8.671   1.634   1.00 19.87 ? 231 ILE   A O   1 
ATOM   1617 C  CB  . ILE   A 1 212 ? -14.221 9.696   -0.627  1.00 21.02 ? 231 ILE   A CB  1 
ATOM   1618 C  CG1 . ILE   A 1 212 ? -15.649 10.251  -0.673  1.00 21.75 ? 231 ILE   A CG1 1 
ATOM   1619 C  CG2 . ILE   A 1 212 ? -14.214 8.167   -0.576  1.00 21.72 ? 231 ILE   A CG2 1 
ATOM   1620 C  CD1 . ILE   A 1 212 ? -16.518 9.681   -1.789  1.00 22.09 ? 231 ILE   A CD1 1 
ATOM   1621 N  N   . SER   A 1 213 ? -11.069 9.844   -0.036  1.00 22.50 ? 232 SER   A N   1 
ATOM   1622 C  CA  . SER   A 1 213 ? -9.798  9.127   -0.003  1.00 23.81 ? 232 SER   A CA  1 
ATOM   1623 C  C   . SER   A 1 213 ? -9.251  8.994   1.418   1.00 24.79 ? 232 SER   A C   1 
ATOM   1624 O  O   . SER   A 1 213 ? -8.686  7.958   1.766   1.00 25.96 ? 232 SER   A O   1 
ATOM   1625 C  CB  . SER   A 1 213 ? -8.780  9.788   -0.899  1.00 23.65 ? 232 SER   A CB  1 
ATOM   1626 O  OG  . SER   A 1 213 ? -8.391  11.055  -0.386  1.00 24.30 ? 232 SER   A OG  1 
ATOM   1627 N  N   . HIS   A 1 214 ? -9.431  10.029  2.245   1.00 24.88 ? 233 HIS   A N   1 
ATOM   1628 C  CA  . HIS   A 1 214 ? -8.906  10.028  3.603   1.00 25.51 ? 233 HIS   A CA  1 
ATOM   1629 C  C   . HIS   A 1 214 ? -9.537  8.930   4.462   1.00 24.86 ? 233 HIS   A C   1 
ATOM   1630 O  O   . HIS   A 1 214 ? -8.936  8.526   5.455   1.00 23.43 ? 233 HIS   A O   1 
ATOM   1631 C  CB  . HIS   A 1 214 ? -9.101  11.404  4.253   1.00 27.41 ? 233 HIS   A CB  1 
ATOM   1632 C  CG  . HIS   A 1 214 ? -8.551  11.537  5.643   1.00 28.00 ? 233 HIS   A CG  1 
ATOM   1633 N  ND1 . HIS   A 1 214 ? -7.259  11.944  5.899   1.00 28.73 ? 233 HIS   A ND1 1 
ATOM   1634 C  CD2 . HIS   A 1 214 ? -9.116  11.332  6.843   1.00 28.87 ? 233 HIS   A CD2 1 
ATOM   1635 C  CE1 . HIS   A 1 214 ? -7.060  11.977  7.210   1.00 29.70 ? 233 HIS   A CE1 1 
ATOM   1636 N  NE2 . HIS   A 1 214 ? -8.172  11.605  7.806   1.00 30.14 ? 233 HIS   A NE2 1 
ATOM   1637 N  N   . TYR   A 1 215 ? -10.745 8.463   4.104   1.00 24.11 ? 234 TYR   A N   1 
ATOM   1638 C  CA  . TYR   A 1 215 ? -11.517 7.580   4.973   1.00 24.90 ? 234 TYR   A CA  1 
ATOM   1639 C  C   . TYR   A 1 215 ? -11.546 6.136   4.468   1.00 25.35 ? 234 TYR   A C   1 
ATOM   1640 O  O   . TYR   A 1 215 ? -12.260 5.313   5.036   1.00 24.73 ? 234 TYR   A O   1 
ATOM   1641 C  CB  . TYR   A 1 215 ? -12.933 8.157   5.111   1.00 25.00 ? 234 TYR   A CB  1 
ATOM   1642 C  CG  . TYR   A 1 215 ? -12.926 9.501   5.824   1.00 24.49 ? 234 TYR   A CG  1 
ATOM   1643 C  CD1 . TYR   A 1 215 ? -12.945 9.572   7.211   1.00 23.93 ? 234 TYR   A CD1 1 
ATOM   1644 C  CD2 . TYR   A 1 215 ? -12.852 10.693  5.111   1.00 24.00 ? 234 TYR   A CD2 1 
ATOM   1645 C  CE1 . TYR   A 1 215 ? -12.897 10.791  7.869   1.00 24.54 ? 234 TYR   A CE1 1 
ATOM   1646 C  CE2 . TYR   A 1 215 ? -12.808 11.918  5.758   1.00 23.71 ? 234 TYR   A CE2 1 
ATOM   1647 C  CZ  . TYR   A 1 215 ? -12.828 11.968  7.141   1.00 24.35 ? 234 TYR   A CZ  1 
ATOM   1648 O  OH  . TYR   A 1 215 ? -12.775 13.170  7.789   1.00 24.29 ? 234 TYR   A OH  1 
ATOM   1649 N  N   . ARG   A 1 216 ? -10.767 5.811   3.427   1.00 27.08 ? 235 ARG   A N   1 
ATOM   1650 C  CA  . ARG   A 1 216 ? -10.833 4.488   2.818   1.00 29.22 ? 235 ARG   A CA  1 
ATOM   1651 C  C   . ARG   A 1 216 ? -10.476 3.392   3.830   1.00 28.41 ? 235 ARG   A C   1 
ATOM   1652 O  O   . ARG   A 1 216 ? -11.102 2.330   3.823   1.00 26.98 ? 235 ARG   A O   1 
ATOM   1653 C  CB  . ARG   A 1 216 ? -9.980  4.394   1.545   1.00 32.07 ? 235 ARG   A CB  1 
ATOM   1654 C  CG  . ARG   A 1 216 ? -10.434 5.270   0.383   1.00 35.92 ? 235 ARG   A CG  1 
ATOM   1655 C  CD  . ARG   A 1 216 ? -11.751 4.841   -0.271  1.00 38.20 ? 235 ARG   A CD  1 
ATOM   1656 N  NE  . ARG   A 1 216 ? -11.688 3.514   -0.897  1.00 40.64 ? 235 ARG   A NE  1 
ATOM   1657 C  CZ  . ARG   A 1 216 ? -11.079 3.204   -2.040  1.00 42.73 ? 235 ARG   A CZ  1 
ATOM   1658 N  NH1 . ARG   A 1 216 ? -10.564 4.146   -2.816  1.00 43.40 ? 235 ARG   A NH1 1 
ATOM   1659 N  NH2 . ARG   A 1 216 ? -11.013 1.940   -2.424  1.00 44.50 ? 235 ARG   A NH2 1 
ATOM   1660 N  N   . PRO   A 1 217 ? -9.465  3.576   4.715   1.00 27.44 ? 236 PRO   A N   1 
ATOM   1661 C  CA  . PRO   A 1 217 ? -9.171  2.580   5.753   1.00 26.90 ? 236 PRO   A CA  1 
ATOM   1662 C  C   . PRO   A 1 217 ? -10.331 2.309   6.709   1.00 25.19 ? 236 PRO   A C   1 
ATOM   1663 O  O   . PRO   A 1 217 ? -10.611 1.156   7.032   1.00 24.88 ? 236 PRO   A O   1 
ATOM   1664 C  CB  . PRO   A 1 217 ? -7.935  3.152   6.490   1.00 26.92 ? 236 PRO   A CB  1 
ATOM   1665 C  CG  . PRO   A 1 217 ? -7.314  4.113   5.492   1.00 27.75 ? 236 PRO   A CG  1 
ATOM   1666 C  CD  . PRO   A 1 217 ? -8.494  4.685   4.715   1.00 28.36 ? 236 PRO   A CD  1 
ATOM   1667 N  N   . TRP   A 1 218 ? -11.005 3.375   7.156   1.00 23.90 ? 237 TRP   A N   1 
ATOM   1668 C  CA  . TRP   A 1 218 ? -12.119 3.239   8.084   1.00 22.87 ? 237 TRP   A CA  1 
ATOM   1669 C  C   . TRP   A 1 218 ? -13.295 2.517   7.424   1.00 22.03 ? 237 TRP   A C   1 
ATOM   1670 O  O   . TRP   A 1 218 ? -13.898 1.640   8.043   1.00 21.75 ? 237 TRP   A O   1 
ATOM   1671 C  CB  . TRP   A 1 218 ? -12.553 4.606   8.632   1.00 22.17 ? 237 TRP   A CB  1 
ATOM   1672 C  CG  . TRP   A 1 218 ? -13.779 4.536   9.506   1.00 21.86 ? 237 TRP   A CG  1 
ATOM   1673 C  CD1 . TRP   A 1 218 ? -13.836 4.105   10.799  1.00 22.30 ? 237 TRP   A CD1 1 
ATOM   1674 C  CD2 . TRP   A 1 218 ? -15.129 4.912   9.151   1.00 21.38 ? 237 TRP   A CD2 1 
ATOM   1675 N  NE1 . TRP   A 1 218 ? -15.117 4.184   11.274  1.00 22.67 ? 237 TRP   A NE1 1 
ATOM   1676 C  CE2 . TRP   A 1 218 ? -15.934 4.672   10.289  1.00 21.18 ? 237 TRP   A CE2 1 
ATOM   1677 C  CE3 . TRP   A 1 218 ? -15.733 5.423   7.994   1.00 20.46 ? 237 TRP   A CE3 1 
ATOM   1678 C  CZ2 . TRP   A 1 218 ? -17.304 4.922   10.299  1.00 20.59 ? 237 TRP   A CZ2 1 
ATOM   1679 C  CZ3 . TRP   A 1 218 ? -17.088 5.675   8.007   1.00 20.38 ? 237 TRP   A CZ3 1 
ATOM   1680 C  CH2 . TRP   A 1 218 ? -17.860 5.428   9.146   1.00 20.06 ? 237 TRP   A CH2 1 
ATOM   1681 N  N   . ILE   A 1 219 ? -13.617 2.888   6.176   1.00 21.74 ? 238 ILE   A N   1 
ATOM   1682 C  CA  . ILE   A 1 219 ? -14.717 2.275   5.440   1.00 22.03 ? 238 ILE   A CA  1 
ATOM   1683 C  C   . ILE   A 1 219 ? -14.457 0.771   5.286   1.00 23.09 ? 238 ILE   A C   1 
ATOM   1684 O  O   . ILE   A 1 219 ? -15.347 -0.044  5.532   1.00 22.43 ? 238 ILE   A O   1 
ATOM   1685 C  CB  . ILE   A 1 219 ? -14.928 2.971   4.079   1.00 21.94 ? 238 ILE   A CB  1 
ATOM   1686 C  CG1 . ILE   A 1 219 ? -15.378 4.429   4.250   1.00 21.81 ? 238 ILE   A CG1 1 
ATOM   1687 C  CG2 . ILE   A 1 219 ? -15.907 2.185   3.201   1.00 22.56 ? 238 ILE   A CG2 1 
ATOM   1688 C  CD1 . ILE   A 1 219 ? -15.353 5.242   2.968   1.00 22.07 ? 238 ILE   A CD1 1 
ATOM   1689 N  N   . ASN   A 1 220 ? -13.225 0.406   4.906   1.00 23.35 ? 239 ASN   A N   1 
ATOM   1690 C  CA  . ASN   A 1 220 ? -12.857 -0.988  4.693   1.00 25.32 ? 239 ASN   A CA  1 
ATOM   1691 C  C   . ASN   A 1 220 ? -13.011 -1.782  5.996   1.00 25.71 ? 239 ASN   A C   1 
ATOM   1692 O  O   . ASN   A 1 220 ? -13.417 -2.943  5.966   1.00 26.27 ? 239 ASN   A O   1 
ATOM   1693 C  CB  . ASN   A 1 220 ? -11.466 -1.079  4.064   1.00 26.56 ? 239 ASN   A CB  1 
ATOM   1694 C  CG  . ASN   A 1 220 ? -10.946 -2.493  3.973   0.50 27.20 ? 239 ASN   A CG  1 
ATOM   1695 O  OD1 . ASN   A 1 220 ? -10.068 -2.879  4.754   0.50 28.40 ? 239 ASN   A OD1 1 
ATOM   1696 N  ND2 . ASN   A 1 220 ? -11.467 -3.278  3.041   0.50 27.10 ? 239 ASN   A ND2 1 
ATOM   1697 N  N   . GLN   A 1 221 ? -12.712 -1.148  7.139   1.00 24.67 ? 240 GLN   A N   1 
ATOM   1698 C  CA  . GLN   A 1 221 ? -12.759 -1.805  8.440   1.00 25.79 ? 240 GLN   A CA  1 
ATOM   1699 C  C   . GLN   A 1 221 ? -14.195 -2.165  8.838   1.00 24.94 ? 240 GLN   A C   1 
ATOM   1700 O  O   . GLN   A 1 221 ? -14.440 -3.251  9.373   1.00 22.88 ? 240 GLN   A O   1 
ATOM   1701 C  CB  . GLN   A 1 221 ? -12.108 -0.901  9.489   1.00 26.98 ? 240 GLN   A CB  1 
ATOM   1702 C  CG  . GLN   A 1 221 ? -12.003 -1.520  10.879  1.00 27.74 ? 240 GLN   A CG  1 
ATOM   1703 C  CD  . GLN   A 1 221 ? -11.045 -0.786  11.794  0.10 27.31 ? 240 GLN   A CD  1 
ATOM   1704 O  OE1 . GLN   A 1 221 ? -10.463 0.244   11.434  0.10 26.89 ? 240 GLN   A OE1 1 
ATOM   1705 N  NE2 . GLN   A 1 221 ? -10.868 -1.316  12.995  0.10 27.32 ? 240 GLN   A NE2 1 
ATOM   1706 N  N   . ILE   A 1 222 ? -15.141 -1.248  8.584   1.00 24.09 ? 241 ILE   A N   1 
ATOM   1707 C  CA  . ILE   A 1 222 ? -16.539 -1.482  8.913   1.00 23.52 ? 241 ILE   A CA  1 
ATOM   1708 C  C   . ILE   A 1 222 ? -17.092 -2.602  8.029   1.00 23.16 ? 241 ILE   A C   1 
ATOM   1709 O  O   . ILE   A 1 222 ? -17.738 -3.515  8.540   1.00 23.53 ? 241 ILE   A O   1 
ATOM   1710 C  CB  . ILE   A 1 222 ? -17.374 -0.190  8.797   1.00 24.02 ? 241 ILE   A CB  1 
ATOM   1711 C  CG1 . ILE   A 1 222 ? -16.859 0.925   9.721   1.00 23.99 ? 241 ILE   A CG1 1 
ATOM   1712 C  CG2 . ILE   A 1 222 ? -18.856 -0.479  9.052   1.00 23.62 ? 241 ILE   A CG2 1 
ATOM   1713 C  CD1 . ILE   A 1 222 ? -17.154 0.713   11.198  1.00 24.54 ? 241 ILE   A CD1 1 
ATOM   1714 N  N   . LEU   A 1 223 ? -16.833 -2.528  6.717   1.00 23.43 ? 242 LEU   A N   1 
ATOM   1715 C  CA  . LEU   A 1 223 ? -17.399 -3.457  5.748   1.00 25.82 ? 242 LEU   A CA  1 
ATOM   1716 C  C   . LEU   A 1 223 ? -16.926 -4.889  6.012   1.00 29.19 ? 242 LEU   A C   1 
ATOM   1717 O  O   . LEU   A 1 223 ? -17.681 -5.837  5.794   1.00 30.16 ? 242 LEU   A O   1 
ATOM   1718 C  CB  . LEU   A 1 223 ? -17.040 -3.041  4.320   1.00 26.07 ? 242 LEU   A CB  1 
ATOM   1719 C  CG  . LEU   A 1 223 ? -17.703 -1.772  3.775   1.00 27.11 ? 242 LEU   A CG  1 
ATOM   1720 C  CD1 . LEU   A 1 223 ? -17.205 -1.499  2.363   1.00 27.36 ? 242 LEU   A CD1 1 
ATOM   1721 C  CD2 . LEU   A 1 223 ? -19.220 -1.857  3.790   1.00 27.83 ? 242 LEU   A CD2 1 
ATOM   1722 N  N   . GLN   A 1 224 ? -15.668 -5.042  6.448   1.00 30.73 ? 243 GLN   A N   1 
ATOM   1723 C  CA  . GLN   A 1 224 ? -15.066 -6.359  6.615   1.00 33.15 ? 243 GLN   A CA  1 
ATOM   1724 C  C   . GLN   A 1 224 ? -15.625 -7.081  7.841   1.00 33.91 ? 243 GLN   A C   1 
ATOM   1725 O  O   . GLN   A 1 224 ? -15.656 -8.310  7.849   1.00 35.50 ? 243 GLN   A O   1 
ATOM   1726 C  CB  . GLN   A 1 224 ? -13.539 -6.283  6.691   1.00 34.05 ? 243 GLN   A CB  1 
ATOM   1727 C  CG  . GLN   A 1 224 ? -12.841 -6.338  5.336   0.50 34.70 ? 243 GLN   A CG  1 
ATOM   1728 C  CD  . GLN   A 1 224 ? -13.089 -7.633  4.591   0.50 36.13 ? 243 GLN   A CD  1 
ATOM   1729 O  OE1 . GLN   A 1 224 ? -13.095 -8.723  5.176   0.50 37.61 ? 243 GLN   A OE1 1 
ATOM   1730 N  NE2 . GLN   A 1 224 ? -13.323 -7.527  3.292   0.50 36.21 ? 243 GLN   A NE2 1 
ATOM   1731 N  N   . ALA   A 1 225 ? -16.072 -6.327  8.857   1.00 35.41 ? 244 ALA   A N   1 
ATOM   1732 C  CA  . ALA   A 1 225 ? -16.483 -6.899  10.132  1.00 36.53 ? 244 ALA   A CA  1 
ATOM   1733 C  C   . ALA   A 1 225 ? -18.006 -6.957  10.293  1.00 38.80 ? 244 ALA   A C   1 
ATOM   1734 O  O   . ALA   A 1 225 ? -18.487 -7.368  11.348  1.00 39.10 ? 244 ALA   A O   1 
ATOM   1735 C  CB  . ALA   A 1 225 ? -15.867 -6.100  11.255  1.00 37.33 ? 244 ALA   A CB  1 
ATOM   1736 N  N   . ASN   A 1 226 ? -18.766 -6.548  9.267   1.00 41.29 ? 245 ASN   A N   1 
ATOM   1737 C  CA  . ASN   A 1 226 ? -20.220 -6.490  9.357   1.00 40.71 ? 245 ASN   A CA  1 
ATOM   1738 C  C   . ASN   A 1 226 ? -20.837 -7.017  8.057   1.00 42.04 ? 245 ASN   A C   1 
ATOM   1739 O  O   . ASN   A 1 226 ? -22.080 -6.926  7.938   1.00 42.03 ? 245 ASN   A O   1 
ATOM   1740 C  CB  . ASN   A 1 226 ? -20.721 -5.078  9.646   1.00 39.94 ? 245 ASN   A CB  1 
ATOM   1741 C  CG  . ASN   A 1 226 ? -20.313 -4.580  11.012  1.00 41.72 ? 245 ASN   A CG  1 
ATOM   1742 O  OD1 . ASN   A 1 226 ? -20.967 -4.891  12.014  1.00 42.40 ? 245 ASN   A OD1 1 
ATOM   1743 N  ND2 . ASN   A 1 226 ? -19.260 -3.778  11.075  1.00 43.64 ? 245 ASN   A ND2 1 
ATOM   1744 O  OXT . ASN   A 1 226 ? -20.058 -7.503  7.205   1.00 44.58 ? 245 ASN   A OXT 1 
HETATM 1745 ZN ZN  . ZN    B 2 .   ? -39.563 5.379   -13.218 1.00 13.84 ? 301 ZN    A ZN  1 
HETATM 1746 C  C4  . A1AO1 C 3 .   ? -30.354 19.640  7.431   1.00 15.49 ? 302 A1AO1 A C4  1 
HETATM 1747 C  C5  . A1AO1 C 3 .   ? -28.898 19.811  6.910   1.00 15.35 ? 302 A1AO1 A C5  1 
HETATM 1748 C  C6  . A1AO1 C 3 .   ? -26.804 23.832  6.208   1.00 18.15 ? 302 A1AO1 A C6  1 
HETATM 1749 C  C8  . A1AO1 C 3 .   ? -27.588 22.014  7.882   1.00 15.42 ? 302 A1AO1 A C8  1 
HETATM 1750 C  C10 . A1AO1 C 3 .   ? -26.249 23.796  4.878   1.00 17.01 ? 302 A1AO1 A C10 1 
HETATM 1751 C  C13 . A1AO1 C 3 .   ? -25.819 24.755  3.962   1.00 15.95 ? 302 A1AO1 A C13 1 
HETATM 1752 C  C17 . A1AO1 C 3 .   ? -27.278 25.093  10.143  1.00 29.55 ? 302 A1AO1 A C17 1 
HETATM 1753 C  C22 . A1AO1 C 3 .   ? -30.090 18.451  9.672   1.00 14.47 ? 302 A1AO1 A C22 1 
HETATM 1754 C  C24 . A1AO1 C 3 .   ? -31.467 19.752  6.360   1.00 15.97 ? 302 A1AO1 A C24 1 
HETATM 1755 C  C26 . A1AO1 C 3 .   ? -25.201 23.014  2.378   1.00 15.34 ? 302 A1AO1 A C26 1 
HETATM 1756 C  C28 . A1AO1 C 3 .   ? -31.093 16.086  8.684   1.00 14.84 ? 302 A1AO1 A C28 1 
HETATM 1757 C  C1  . A1AO1 C 3 .   ? -28.754 21.060  7.676   1.00 15.11 ? 302 A1AO1 A C1  1 
HETATM 1758 C  C2  . A1AO1 C 3 .   ? -27.016 22.537  6.586   1.00 16.42 ? 302 A1AO1 A C2  1 
HETATM 1759 C  C3  . A1AO1 C 3 .   ? -30.030 20.943  8.150   1.00 15.58 ? 302 A1AO1 A C3  1 
HETATM 1760 N  N7  . A1AO1 C 3 .   ? -26.626 21.681  5.573   1.00 15.76 ? 302 A1AO1 A N7  1 
HETATM 1761 C  C9  . A1AO1 C 3 .   ? -26.150 22.441  4.514   1.00 16.34 ? 302 A1AO1 A C9  1 
HETATM 1762 C  C11 . A1AO1 C 3 .   ? -27.103 25.086  6.991   1.00 21.65 ? 302 A1AO1 A C11 1 
HETATM 1763 C  C12 . A1AO1 C 3 .   ? -30.490 18.401  8.340   1.00 14.58 ? 302 A1AO1 A C12 1 
HETATM 1764 C  C14 . A1AO1 C 3 .   ? -26.041 25.572  7.998   1.00 24.97 ? 302 A1AO1 A C14 1 
HETATM 1765 N  N15 . A1AO1 C 3 .   ? -26.212 24.946  9.329   1.00 27.08 ? 302 A1AO1 A N15 1 
HETATM 1766 O  O16 . A1AO1 C 3 .   ? -28.182 19.151  6.176   1.00 15.77 ? 302 A1AO1 A O16 1 
HETATM 1767 C  C18 . A1AO1 C 3 .   ? -25.636 22.050  3.281   1.00 15.27 ? 302 A1AO1 A C18 1 
HETATM 1768 C  C19 . A1AO1 C 3 .   ? -26.535 21.425  8.826   1.00 14.90 ? 302 A1AO1 A C19 1 
HETATM 1769 O  O20 . A1AO1 C 3 .   ? -30.842 21.580  8.933   1.00 15.09 ? 302 A1AO1 A O20 1 
HETATM 1770 O  O21 . A1AO1 C 3 .   ? -28.294 25.693  9.794   1.00 31.78 ? 302 A1AO1 A O21 1 
HETATM 1771 C  C23 . A1AO1 C 3 .   ? -30.991 17.195  7.856   1.00 14.59 ? 302 A1AO1 A C23 1 
HETATM 1772 C  C25 . A1AO1 C 3 .   ? -25.309 24.362  2.733   1.00 15.83 ? 302 A1AO1 A C25 1 
HETATM 1773 C  C27 . A1AO1 C 3 .   ? -30.182 17.338  10.488  1.00 14.47 ? 302 A1AO1 A C27 1 
HETATM 1774 C  C29 . A1AO1 C 3 .   ? -30.685 16.139  10.014  1.00 14.93 ? 302 A1AO1 A C29 1 
HETATM 1775 C  C30 . A1AO1 C 3 .   ? -24.634 25.222  7.510   1.00 25.93 ? 302 A1AO1 A C30 1 
HETATM 1776 C  C31 . A1AO1 C 3 .   ? -26.152 27.084  8.163   1.00 26.72 ? 302 A1AO1 A C31 1 
HETATM 1777 C  C32 . A1AO1 C 3 .   ? -27.143 24.486  11.512  1.00 29.57 ? 302 A1AO1 A C32 1 
HETATM 1778 C  C33 . A1AO1 C 3 .   ? -25.230 21.195  8.402   1.00 14.54 ? 302 A1AO1 A C33 1 
HETATM 1779 C  C34 . A1AO1 C 3 .   ? -26.883 21.066  10.125  1.00 14.77 ? 302 A1AO1 A C34 1 
HETATM 1780 C  C35 . A1AO1 C 3 .   ? -24.630 22.612  1.040   1.00 14.69 ? 302 A1AO1 A C35 1 
HETATM 1781 C  C36 . A1AO1 C 3 .   ? -30.806 14.937  10.923  1.00 15.14 ? 302 A1AO1 A C36 1 
HETATM 1782 C  C37 . A1AO1 C 3 .   ? -24.294 20.638  9.261   1.00 14.51 ? 302 A1AO1 A C37 1 
HETATM 1783 C  C38 . A1AO1 C 3 .   ? -25.944 20.512  10.982  1.00 14.50 ? 302 A1AO1 A C38 1 
HETATM 1784 C  C39 . A1AO1 C 3 .   ? -24.648 20.302  10.553  1.00 14.43 ? 302 A1AO1 A C39 1 
HETATM 1785 S  S   . DMS   D 4 .   ? -18.477 32.553  6.780   1.00 29.02 ? 303 DMS   A S   1 
HETATM 1786 O  O   . DMS   D 4 .   ? -19.651 32.547  5.838   1.00 27.57 ? 303 DMS   A O   1 
HETATM 1787 C  C1  . DMS   D 4 .   ? -18.939 33.623  8.123   1.00 29.05 ? 303 DMS   A C1  1 
HETATM 1788 C  C2  . DMS   D 4 .   ? -18.541 31.009  7.645   1.00 28.13 ? 303 DMS   A C2  1 
HETATM 1789 S  S   . DMS   E 4 .   ? -41.328 8.323   0.064   1.00 46.68 ? 304 DMS   A S   1 
HETATM 1790 O  O   . DMS   E 4 .   ? -40.718 9.356   0.973   1.00 49.15 ? 304 DMS   A O   1 
HETATM 1791 C  C1  . DMS   E 4 .   ? -41.407 6.829   1.011   1.00 45.19 ? 304 DMS   A C1  1 
HETATM 1792 C  C2  . DMS   E 4 .   ? -40.045 7.820   -1.041  1.00 44.87 ? 304 DMS   A C2  1 
HETATM 1793 O  O   . HOH   F 5 .   ? -10.152 17.919  13.546  1.00 28.50 ? 401 HOH   A O   1 
HETATM 1794 O  O   . HOH   F 5 .   ? -3.897  20.624  7.247   1.00 39.39 ? 402 HOH   A O   1 
HETATM 1795 O  O   . HOH   F 5 .   ? -16.716 5.429   -7.161  1.00 42.18 ? 403 HOH   A O   1 
HETATM 1796 O  O   . HOH   F 5 .   ? -12.031 23.025  -15.262 1.00 46.29 ? 404 HOH   A O   1 
HETATM 1797 O  O   . HOH   F 5 .   ? -12.547 1.887   0.913   1.00 43.88 ? 405 HOH   A O   1 
HETATM 1798 O  O   . HOH   F 5 .   ? -9.025  11.143  10.228  1.00 26.59 ? 406 HOH   A O   1 
HETATM 1799 O  O   . HOH   F 5 .   ? -30.100 3.177   -14.996 1.00 14.39 ? 407 HOH   A O   1 
HETATM 1800 O  O   . HOH   F 5 .   ? -2.929  27.158  -1.376  1.00 45.66 ? 408 HOH   A O   1 
HETATM 1801 O  O   . HOH   F 5 .   ? -9.225  21.266  -0.538  1.00 17.30 ? 409 HOH   A O   1 
HETATM 1802 O  O   . HOH   F 5 .   ? -40.535 11.703  16.170  1.00 23.27 ? 410 HOH   A O   1 
HETATM 1803 O  O   . HOH   F 5 .   ? -22.639 -7.612  5.446   1.00 40.71 ? 411 HOH   A O   1 
HETATM 1804 O  O   . HOH   F 5 .   ? -15.158 -0.838  -2.661  1.00 48.84 ? 412 HOH   A O   1 
HETATM 1805 O  O   . HOH   F 5 .   ? -23.113 8.207   -12.757 1.00 20.89 ? 413 HOH   A O   1 
HETATM 1806 O  O   . HOH   F 5 .   ? -9.697  34.213  5.160   1.00 16.86 ? 414 HOH   A O   1 
HETATM 1807 O  O   . HOH   F 5 .   ? -35.863 -4.769  -2.168  1.00 11.00 ? 415 HOH   A O   1 
HETATM 1808 O  O   . HOH   F 5 .   ? -5.943  22.785  9.659   1.00 25.46 ? 416 HOH   A O   1 
HETATM 1809 O  O   . HOH   F 5 .   ? -39.983 8.071   -8.429  1.00 9.49  ? 417 HOH   A O   1 
HETATM 1810 O  O   . HOH   F 5 .   ? -32.944 18.436  -17.555 1.00 39.11 ? 418 HOH   A O   1 
HETATM 1811 O  O   . HOH   F 5 .   ? -38.107 24.050  -5.035  1.00 22.02 ? 419 HOH   A O   1 
HETATM 1812 O  O   . HOH   F 5 .   ? -35.646 1.741   9.082   1.00 11.69 ? 420 HOH   A O   1 
HETATM 1813 O  O   . HOH   F 5 .   ? -26.266 0.947   16.975  1.00 32.35 ? 421 HOH   A O   1 
HETATM 1814 O  O   . HOH   F 5 .   ? -43.146 0.662   -3.087  1.00 41.25 ? 422 HOH   A O   1 
HETATM 1815 O  O   . HOH   F 5 .   ? -9.198  33.542  0.211   1.00 31.25 ? 423 HOH   A O   1 
HETATM 1816 O  O   . HOH   F 5 .   ? -24.589 17.614  -14.432 1.00 26.91 ? 424 HOH   A O   1 
HETATM 1817 O  O   . HOH   F 5 .   ? -27.383 17.041  12.909  1.00 30.13 ? 425 HOH   A O   1 
HETATM 1818 O  O   . HOH   F 5 .   ? -26.520 37.337  2.144   1.00 38.43 ? 426 HOH   A O   1 
HETATM 1819 O  O   . HOH   F 5 .   ? -23.160 1.510   15.671  1.00 44.21 ? 427 HOH   A O   1 
HETATM 1820 O  O   . HOH   F 5 .   ? -35.696 -1.269  -8.385  1.00 9.45  ? 428 HOH   A O   1 
HETATM 1821 O  O   . HOH   F 5 .   ? -39.001 13.048  13.279  1.00 23.34 ? 429 HOH   A O   1 
HETATM 1822 O  O   . HOH   F 5 .   ? -37.002 7.181   2.250   1.00 11.44 ? 430 HOH   A O   1 
HETATM 1823 O  O   . HOH   F 5 .   ? -21.921 -9.464  2.245   1.00 37.54 ? 431 HOH   A O   1 
HETATM 1824 O  O   . HOH   F 5 .   ? -30.975 29.512  5.023   1.00 24.83 ? 432 HOH   A O   1 
HETATM 1825 O  O   . HOH   F 5 .   ? -30.271 -10.456 2.627   1.00 41.91 ? 433 HOH   A O   1 
HETATM 1826 O  O   . HOH   F 5 .   ? -42.897 12.144  7.976   1.00 24.21 ? 434 HOH   A O   1 
HETATM 1827 O  O   . HOH   F 5 .   ? -14.998 -2.942  12.007  1.00 44.86 ? 435 HOH   A O   1 
HETATM 1828 O  O   . HOH   F 5 .   ? -17.463 18.655  7.171   1.00 9.07  ? 436 HOH   A O   1 
HETATM 1829 O  O   . HOH   F 5 .   ? -26.457 30.088  -4.749  1.00 20.00 ? 437 HOH   A O   1 
HETATM 1830 O  O   . HOH   F 5 .   ? -33.120 27.977  3.582   1.00 24.88 ? 438 HOH   A O   1 
HETATM 1831 O  O   . HOH   F 5 .   ? -24.672 17.439  14.168  1.00 25.71 ? 439 HOH   A O   1 
HETATM 1832 O  O   . HOH   F 5 .   ? -16.717 7.917   19.348  1.00 36.38 ? 440 HOH   A O   1 
HETATM 1833 O  O   . HOH   F 5 .   ? -44.248 16.751  -8.878  1.00 24.05 ? 441 HOH   A O   1 
HETATM 1834 O  O   . HOH   F 5 .   ? -37.485 18.276  12.962  1.00 32.06 ? 442 HOH   A O   1 
HETATM 1835 O  O   . HOH   F 5 .   ? -11.643 11.094  -10.351 1.00 37.50 ? 443 HOH   A O   1 
HETATM 1836 O  O   . HOH   F 5 .   ? -43.631 1.967   3.958   1.00 28.17 ? 444 HOH   A O   1 
HETATM 1837 O  O   . HOH   F 5 .   ? -14.837 -9.577  2.319   1.00 37.43 ? 445 HOH   A O   1 
HETATM 1838 O  O   . HOH   F 5 .   ? -20.154 14.920  4.320   1.00 31.68 ? 446 HOH   A O   1 
HETATM 1839 O  O   . HOH   F 5 .   ? -30.414 -8.996  8.593   1.00 41.89 ? 447 HOH   A O   1 
HETATM 1840 O  O   . HOH   F 5 .   ? -35.464 -8.907  7.958   1.00 42.78 ? 448 HOH   A O   1 
HETATM 1841 O  O   . HOH   F 5 .   ? -40.519 15.527  -14.462 1.00 40.41 ? 449 HOH   A O   1 
HETATM 1842 O  O   . HOH   F 5 .   ? -13.594 32.585  -9.537  1.00 18.86 ? 450 HOH   A O   1 
HETATM 1843 O  O   . HOH   F 5 .   ? -47.568 -2.451  -9.530  1.00 9.89  ? 451 HOH   A O   1 
HETATM 1844 O  O   . HOH   F 5 .   ? -14.897 22.115  8.892   1.00 16.81 ? 452 HOH   A O   1 
HETATM 1845 O  O   . HOH   F 5 .   ? -19.024 30.186  0.502   1.00 10.50 ? 453 HOH   A O   1 
HETATM 1846 O  O   . HOH   F 5 .   ? -28.374 12.481  -15.528 1.00 24.12 ? 454 HOH   A O   1 
HETATM 1847 O  O   . HOH   F 5 .   ? -21.700 -6.217  2.406   1.00 39.07 ? 455 HOH   A O   1 
HETATM 1848 O  O   . HOH   F 5 .   ? -42.509 -3.222  -13.217 1.00 11.68 ? 456 HOH   A O   1 
HETATM 1849 O  O   . HOH   F 5 .   ? -24.480 1.669   -10.662 1.00 30.95 ? 457 HOH   A O   1 
HETATM 1850 O  O   . HOH   F 5 .   ? -17.315 -5.564  -2.952  1.00 37.30 ? 458 HOH   A O   1 
HETATM 1851 O  O   . HOH   F 5 .   ? -15.408 28.247  13.142  1.00 43.76 ? 459 HOH   A O   1 
HETATM 1852 O  O   . HOH   F 5 .   ? -32.503 19.684  -5.763  1.00 10.12 ? 460 HOH   A O   1 
HETATM 1853 O  O   . HOH   F 5 .   ? -16.141 16.177  6.717   1.00 12.88 ? 461 HOH   A O   1 
HETATM 1854 O  O   . HOH   F 5 .   ? -40.925 12.519  1.166   1.00 18.18 ? 462 HOH   A O   1 
HETATM 1855 O  O   . HOH   F 5 .   ? -37.274 -5.032  6.338   1.00 29.14 ? 463 HOH   A O   1 
HETATM 1856 O  O   . HOH   F 5 .   ? -27.786 -7.028  5.857   1.00 22.49 ? 464 HOH   A O   1 
HETATM 1857 O  O   . HOH   F 5 .   ? -29.344 17.918  3.982   1.00 11.00 ? 465 HOH   A O   1 
HETATM 1858 O  O   . HOH   F 5 .   ? -6.059  12.764  3.533   1.00 43.86 ? 466 HOH   A O   1 
HETATM 1859 O  O   . HOH   F 5 .   ? -21.850 28.346  7.546   1.00 28.09 ? 467 HOH   A O   1 
HETATM 1860 O  O   . HOH   F 5 .   ? -38.246 5.609   10.750  1.00 33.01 ? 468 HOH   A O   1 
HETATM 1861 O  O   . HOH   F 5 .   ? -8.808  -1.273  6.648   1.00 45.63 ? 469 HOH   A O   1 
HETATM 1862 O  O   . HOH   F 5 .   ? -31.544 4.660   -6.844  1.00 8.71  ? 470 HOH   A O   1 
HETATM 1863 O  O   . HOH   F 5 .   ? -34.845 7.604   -18.354 1.00 31.20 ? 471 HOH   A O   1 
HETATM 1864 O  O   . HOH   F 5 .   ? -24.873 33.316  5.342   1.00 13.19 ? 472 HOH   A O   1 
HETATM 1865 O  O   . HOH   F 5 .   ? -26.541 -7.066  11.188  1.00 41.88 ? 473 HOH   A O   1 
HETATM 1866 O  O   . HOH   F 5 .   ? -42.260 7.349   7.421   1.00 40.77 ? 474 HOH   A O   1 
HETATM 1867 O  O   . HOH   F 5 .   ? -20.657 27.641  -8.577  1.00 12.19 ? 475 HOH   A O   1 
HETATM 1868 O  O   . HOH   F 5 .   ? -21.206 36.887  -10.644 1.00 35.29 ? 476 HOH   A O   1 
HETATM 1869 O  O   . HOH   F 5 .   ? -39.112 19.232  8.969   1.00 25.55 ? 477 HOH   A O   1 
HETATM 1870 O  O   . HOH   F 5 .   ? -36.623 27.023  -8.018  1.00 34.57 ? 478 HOH   A O   1 
HETATM 1871 O  O   . HOH   F 5 .   ? -27.139 24.064  -14.728 1.00 26.59 ? 479 HOH   A O   1 
HETATM 1872 O  O   . HOH   F 5 .   ? -24.565 26.543  -0.771  1.00 32.38 ? 480 HOH   A O   1 
HETATM 1873 O  O   . HOH   F 5 .   ? -34.068 20.613  -16.364 1.00 24.66 ? 481 HOH   A O   1 
HETATM 1874 O  O   . HOH   F 5 .   ? -13.603 15.892  7.617   1.00 22.69 ? 482 HOH   A O   1 
HETATM 1875 O  O   . HOH   F 5 .   ? -31.665 22.892  -9.555  1.00 16.29 ? 483 HOH   A O   1 
HETATM 1876 O  O   . HOH   F 5 .   ? -32.699 -8.129  14.341  1.00 21.38 ? 484 HOH   A O   1 
HETATM 1877 O  O   . HOH   F 5 .   ? -10.517 21.609  -3.088  1.00 11.45 ? 485 HOH   A O   1 
HETATM 1878 O  O   . HOH   F 5 .   ? -12.454 33.049  1.509   1.00 21.89 ? 486 HOH   A O   1 
HETATM 1879 O  O   . HOH   F 5 .   ? -27.762 14.098  13.912  1.00 27.59 ? 487 HOH   A O   1 
HETATM 1880 O  O   . HOH   F 5 .   ? -33.319 5.127   -10.158 1.00 7.43  ? 488 HOH   A O   1 
HETATM 1881 O  O   . HOH   F 5 .   ? -45.833 0.577   -7.908  1.00 28.22 ? 489 HOH   A O   1 
HETATM 1882 O  O   . HOH   F 5 .   ? -6.106  11.235  1.308   1.00 37.76 ? 490 HOH   A O   1 
HETATM 1883 O  O   . HOH   F 5 .   ? -24.020 -3.512  -8.528  1.00 18.90 ? 491 HOH   A O   1 
HETATM 1884 O  O   . HOH   F 5 .   ? -16.766 15.046  -14.207 1.00 26.83 ? 492 HOH   A O   1 
HETATM 1885 O  O   . HOH   F 5 .   ? -29.046 34.524  -0.558  1.00 41.50 ? 493 HOH   A O   1 
HETATM 1886 O  O   . HOH   F 5 .   ? -4.343  25.963  -8.888  1.00 47.36 ? 494 HOH   A O   1 
HETATM 1887 O  O   . HOH   F 5 .   ? -34.251 -7.773  -10.149 1.00 20.90 ? 495 HOH   A O   1 
HETATM 1888 O  O   . HOH   F 5 .   ? -12.616 -5.284  10.219  1.00 38.54 ? 496 HOH   A O   1 
HETATM 1889 O  O   . HOH   F 5 .   ? -19.243 3.643   14.129  1.00 29.54 ? 497 HOH   A O   1 
HETATM 1890 O  O   . HOH   F 5 .   ? -31.642 -11.603 7.145   1.00 49.92 ? 498 HOH   A O   1 
HETATM 1891 O  O   . HOH   F 5 .   ? -25.020 13.346  14.383  1.00 18.73 ? 499 HOH   A O   1 
HETATM 1892 O  O   . HOH   F 5 .   ? -15.765 33.669  9.002   1.00 28.88 ? 500 HOH   A O   1 
HETATM 1893 O  O   . HOH   F 5 .   ? -32.346 27.043  -8.684  1.00 18.56 ? 501 HOH   A O   1 
HETATM 1894 O  O   . HOH   F 5 .   ? -33.993 -1.775  12.396  1.00 10.79 ? 502 HOH   A O   1 
HETATM 1895 O  O   . HOH   F 5 .   ? -27.817 14.637  -2.335  1.00 8.93  ? 503 HOH   A O   1 
HETATM 1896 O  O   . HOH   F 5 .   ? -32.153 25.838  -12.407 1.00 23.94 ? 504 HOH   A O   1 
HETATM 1897 O  O   . HOH   F 5 .   ? -31.228 8.175   -10.893 1.00 10.47 ? 505 HOH   A O   1 
HETATM 1898 O  O   . HOH   F 5 .   ? -38.036 -2.914  -8.790  1.00 14.05 ? 506 HOH   A O   1 
HETATM 1899 O  O   . HOH   F 5 .   ? -21.429 23.820  -3.926  1.00 12.95 ? 507 HOH   A O   1 
HETATM 1900 O  O   . HOH   F 5 .   ? -37.013 -6.062  -4.406  1.00 16.48 ? 508 HOH   A O   1 
HETATM 1901 O  O   . HOH   F 5 .   ? -33.393 -3.657  4.234   1.00 20.00 ? 509 HOH   A O   1 
HETATM 1902 O  O   . HOH   F 5 .   ? -11.269 11.715  -2.561  1.00 17.02 ? 510 HOH   A O   1 
HETATM 1903 O  O   . HOH   F 5 .   ? -42.163 -0.441  -5.584  1.00 23.58 ? 511 HOH   A O   1 
HETATM 1904 O  O   . HOH   F 5 .   ? -19.678 9.616   16.648  1.00 30.53 ? 512 HOH   A O   1 
HETATM 1905 O  O   . HOH   F 5 .   ? -15.480 25.575  16.072  1.00 42.13 ? 513 HOH   A O   1 
HETATM 1906 O  O   . HOH   F 5 .   ? -22.385 32.958  6.683   1.00 23.09 ? 514 HOH   A O   1 
HETATM 1907 O  O   . HOH   F 5 .   ? -42.749 12.193  5.126   1.00 21.49 ? 515 HOH   A O   1 
HETATM 1908 O  O   . HOH   F 5 .   ? -37.595 21.284  -8.943  1.00 27.25 ? 516 HOH   A O   1 
HETATM 1909 O  O   . HOH   F 5 .   ? -23.628 -9.044  -2.101  1.00 31.83 ? 517 HOH   A O   1 
HETATM 1910 O  O   . HOH   F 5 .   ? -7.182  12.471  10.390  1.00 44.47 ? 518 HOH   A O   1 
HETATM 1911 O  O   . HOH   F 5 .   ? -22.290 27.707  0.633   1.00 17.88 ? 519 HOH   A O   1 
HETATM 1912 O  O   . HOH   F 5 .   ? -24.907 -9.478  8.134   1.00 53.06 ? 520 HOH   A O   1 
HETATM 1913 O  O   . HOH   F 5 .   ? -20.287 33.502  -3.920  1.00 16.80 ? 521 HOH   A O   1 
HETATM 1914 O  O   . HOH   F 5 .   ? -33.793 9.458   -11.003 1.00 11.39 ? 522 HOH   A O   1 
HETATM 1915 O  O   . HOH   F 5 .   ? -37.984 7.384   8.581   1.00 24.95 ? 523 HOH   A O   1 
HETATM 1916 O  O   . HOH   F 5 .   ? -41.219 19.959  -1.479  1.00 22.99 ? 524 HOH   A O   1 
HETATM 1917 O  O   . HOH   F 5 .   ? -33.572 6.673   -4.939  1.00 9.58  ? 525 HOH   A O   1 
HETATM 1918 O  O   . HOH   F 5 .   ? -16.175 41.536  -12.096 1.00 25.08 ? 526 HOH   A O   1 
HETATM 1919 O  O   . HOH   F 5 .   ? -29.301 13.828  -17.001 1.00 33.51 ? 527 HOH   A O   1 
HETATM 1920 O  O   . HOH   F 5 .   ? -21.612 -1.865  -9.698  1.00 52.84 ? 528 HOH   A O   1 
HETATM 1921 O  O   . HOH   F 5 .   ? -40.573 -1.136  -1.321  1.00 16.37 ? 529 HOH   A O   1 
HETATM 1922 O  O   . HOH   F 5 .   ? -46.952 7.992   -4.080  1.00 36.13 ? 530 HOH   A O   1 
HETATM 1923 O  O   . HOH   F 5 .   ? -32.285 7.103   -8.260  1.00 10.46 ? 531 HOH   A O   1 
HETATM 1924 O  O   . HOH   F 5 .   ? -30.760 14.727  -1.685  1.00 7.01  ? 532 HOH   A O   1 
HETATM 1925 O  O   . HOH   F 5 .   ? -3.095  27.969  -5.153  1.00 32.84 ? 533 HOH   A O   1 
HETATM 1926 O  O   . HOH   F 5 .   ? -14.124 32.460  -2.315  1.00 10.99 ? 534 HOH   A O   1 
HETATM 1927 O  O   . HOH   F 5 .   ? -29.552 16.692  -16.597 1.00 23.16 ? 535 HOH   A O   1 
HETATM 1928 O  O   . HOH   F 5 .   ? -15.795 26.292  9.194   1.00 13.64 ? 536 HOH   A O   1 
HETATM 1929 O  O   . HOH   F 5 .   ? -36.922 19.765  -16.580 1.00 45.39 ? 537 HOH   A O   1 
HETATM 1930 O  O   . HOH   F 5 .   ? -11.996 18.711  15.200  1.00 24.55 ? 538 HOH   A O   1 
HETATM 1931 O  O   . HOH   F 5 .   ? -24.633 6.223   -13.667 1.00 35.42 ? 539 HOH   A O   1 
HETATM 1932 O  O   . HOH   F 5 .   ? -17.218 34.655  -14.560 1.00 40.15 ? 540 HOH   A O   1 
HETATM 1933 O  O   . HOH   F 5 .   ? -8.791  13.046  -2.583  1.00 26.73 ? 541 HOH   A O   1 
HETATM 1934 O  O   . HOH   F 5 .   ? -35.008 31.882  -2.731  1.00 19.64 ? 542 HOH   A O   1 
HETATM 1935 O  O   . HOH   F 5 .   ? -22.838 5.281   15.490  1.00 27.72 ? 543 HOH   A O   1 
HETATM 1936 O  O   . HOH   F 5 .   ? -15.355 32.973  -13.156 1.00 30.92 ? 544 HOH   A O   1 
HETATM 1937 O  O   . HOH   F 5 .   ? -41.085 11.529  11.696  1.00 31.95 ? 545 HOH   A O   1 
HETATM 1938 O  O   . HOH   F 5 .   ? -18.921 26.094  -10.081 1.00 13.01 ? 546 HOH   A O   1 
HETATM 1939 O  O   . HOH   F 5 .   ? -34.667 -6.524  -0.588  1.00 21.89 ? 547 HOH   A O   1 
HETATM 1940 O  O   . HOH   F 5 .   ? -4.788  32.755  -4.395  1.00 42.06 ? 548 HOH   A O   1 
HETATM 1941 O  O   . HOH   F 5 .   ? -23.365 34.203  -7.451  1.00 52.59 ? 549 HOH   A O   1 
HETATM 1942 O  O   . HOH   F 5 .   ? -9.091  27.931  -7.664  1.00 14.20 ? 550 HOH   A O   1 
HETATM 1943 O  O   . HOH   F 5 .   ? -20.437 37.828  -1.693  1.00 35.71 ? 551 HOH   A O   1 
HETATM 1944 O  O   . HOH   F 5 .   ? -23.777 30.483  7.527   1.00 19.12 ? 552 HOH   A O   1 
HETATM 1945 O  O   . HOH   F 5 .   ? -45.585 -0.556  -5.499  1.00 42.93 ? 553 HOH   A O   1 
HETATM 1946 O  O   . HOH   F 5 .   ? -34.701 -3.919  -14.482 1.00 26.48 ? 554 HOH   A O   1 
HETATM 1947 O  O   . HOH   F 5 .   ? -36.559 3.544   22.580  1.00 27.19 ? 555 HOH   A O   1 
HETATM 1948 O  O   . HOH   F 5 .   ? -42.051 14.055  -12.736 1.00 23.21 ? 556 HOH   A O   1 
HETATM 1949 O  O   . HOH   F 5 .   ? -12.353 7.609   -3.938  1.00 49.16 ? 557 HOH   A O   1 
HETATM 1950 O  O   . HOH   F 5 .   ? -31.548 6.226   -17.336 1.00 24.02 ? 558 HOH   A O   1 
HETATM 1951 O  O   . HOH   F 5 .   ? -34.424 26.187  5.663   1.00 40.40 ? 559 HOH   A O   1 
HETATM 1952 O  O   . HOH   F 5 .   ? -10.651 7.680   9.478   1.00 36.59 ? 560 HOH   A O   1 
HETATM 1953 O  O   . HOH   F 5 .   ? -36.657 20.866  -13.027 1.00 39.36 ? 561 HOH   A O   1 
HETATM 1954 O  O   . HOH   F 5 .   ? -20.271 6.410   -12.411 1.00 39.82 ? 562 HOH   A O   1 
HETATM 1955 O  O   . HOH   F 5 .   ? -16.193 29.703  10.538  1.00 16.33 ? 563 HOH   A O   1 
HETATM 1956 O  O   . HOH   F 5 .   ? -29.207 -9.402  5.022   1.00 47.25 ? 564 HOH   A O   1 
HETATM 1957 O  O   . HOH   F 5 .   ? -36.252 -3.807  4.315   1.00 15.28 ? 565 HOH   A O   1 
HETATM 1958 O  O   . HOH   F 5 .   ? -28.168 -0.453  -12.586 1.00 26.13 ? 566 HOH   A O   1 
HETATM 1959 O  O   . HOH   F 5 .   ? -27.423 28.129  -13.623 1.00 32.45 ? 567 HOH   A O   1 
HETATM 1960 O  O   . HOH   F 5 .   ? -26.373 19.858  -15.214 1.00 24.93 ? 568 HOH   A O   1 
HETATM 1961 O  O   . HOH   F 5 .   ? -35.537 -0.925  -13.147 1.00 16.54 ? 569 HOH   A O   1 
HETATM 1962 O  O   . HOH   F 5 .   ? -40.536 9.407   -11.477 1.00 10.54 ? 570 HOH   A O   1 
HETATM 1963 O  O   . HOH   F 5 .   ? -41.309 21.247  -5.014  1.00 36.07 ? 571 HOH   A O   1 
HETATM 1964 O  O   . HOH   F 5 .   ? -9.695  6.176   7.555   1.00 30.02 ? 572 HOH   A O   1 
HETATM 1965 O  O   . HOH   F 5 .   ? -16.406 28.074  -13.631 1.00 24.64 ? 573 HOH   A O   1 
HETATM 1966 O  O   . HOH   F 5 .   ? -12.538 18.802  -16.034 1.00 31.62 ? 574 HOH   A O   1 
HETATM 1967 O  O   . HOH   F 5 .   ? -27.751 7.639   15.698  1.00 31.97 ? 575 HOH   A O   1 
HETATM 1968 O  O   . HOH   F 5 .   ? -31.023 4.495   17.230  1.00 34.75 ? 576 HOH   A O   1 
HETATM 1969 O  O   . HOH   F 5 .   ? -38.469 6.868   15.749  1.00 20.55 ? 577 HOH   A O   1 
HETATM 1970 O  O   . HOH   F 5 .   ? -18.584 12.965  -13.375 1.00 24.54 ? 578 HOH   A O   1 
HETATM 1971 O  O   . HOH   F 5 .   ? -41.091 5.425   3.766   1.00 33.77 ? 579 HOH   A O   1 
HETATM 1972 O  O   . HOH   F 5 .   ? -35.758 6.842   22.055  1.00 41.63 ? 580 HOH   A O   1 
HETATM 1973 O  O   . HOH   F 5 .   ? -9.960  31.926  12.978  1.00 17.93 ? 581 HOH   A O   1 
HETATM 1974 O  O   . HOH   F 5 .   ? -27.757 -3.233  -11.250 1.00 25.07 ? 582 HOH   A O   1 
HETATM 1975 O  O   . HOH   F 5 .   ? -24.741 31.167  -12.468 1.00 28.24 ? 583 HOH   A O   1 
HETATM 1976 O  O   . HOH   F 5 .   ? -18.553 17.029  19.490  1.00 40.97 ? 584 HOH   A O   1 
HETATM 1977 O  O   . HOH   F 5 .   ? -24.939 22.439  -14.734 1.00 14.76 ? 585 HOH   A O   1 
HETATM 1978 O  O   . HOH   F 5 .   ? -21.295 11.959  -13.319 1.00 17.68 ? 586 HOH   A O   1 
HETATM 1979 O  O   . HOH   F 5 .   ? -34.633 22.550  -13.314 1.00 38.51 ? 587 HOH   A O   1 
HETATM 1980 O  O   . HOH   F 5 .   ? -5.775  23.569  5.698   1.00 8.43  ? 588 HOH   A O   1 
HETATM 1981 O  O   . HOH   F 5 .   ? -39.639 -0.994  4.702   1.00 27.06 ? 589 HOH   A O   1 
HETATM 1982 O  O   . HOH   F 5 .   ? -35.047 18.685  6.132   1.00 16.32 ? 590 HOH   A O   1 
HETATM 1983 O  O   . HOH   F 5 .   ? -37.669 2.915   4.164   1.00 27.33 ? 591 HOH   A O   1 
HETATM 1984 O  O   . HOH   F 5 .   ? -23.939 20.004  14.837  1.00 36.24 ? 592 HOH   A O   1 
HETATM 1985 O  O   . HOH   F 5 .   ? -31.166 31.591  -3.413  1.00 25.44 ? 593 HOH   A O   1 
HETATM 1986 O  O   . HOH   F 5 .   ? -20.975 37.888  5.187   1.00 40.38 ? 594 HOH   A O   1 
HETATM 1987 O  O   . HOH   F 5 .   ? -12.230 30.099  -10.590 1.00 29.11 ? 595 HOH   A O   1 
HETATM 1988 O  O   . HOH   F 5 .   ? -40.772 20.694  -7.213  1.00 25.09 ? 596 HOH   A O   1 
HETATM 1989 O  O   . HOH   F 5 .   ? -19.932 6.940   16.996  1.00 41.22 ? 597 HOH   A O   1 
HETATM 1990 O  O   . HOH   F 5 .   ? -18.244 19.296  20.294  1.00 35.88 ? 598 HOH   A O   1 
HETATM 1991 O  O   . HOH   F 5 .   ? -44.800 9.763   -1.612  1.00 34.28 ? 599 HOH   A O   1 
HETATM 1992 O  O   . HOH   F 5 .   ? -35.384 1.244   11.794  1.00 17.27 ? 600 HOH   A O   1 
HETATM 1993 O  O   . HOH   F 5 .   ? -7.584  21.219  11.853  1.00 42.50 ? 601 HOH   A O   1 
HETATM 1994 O  O   . HOH   F 5 .   ? -25.547 36.042  5.213   1.00 31.74 ? 602 HOH   A O   1 
HETATM 1995 O  O   . HOH   F 5 .   ? -29.051 6.985   -18.769 1.00 40.47 ? 603 HOH   A O   1 
HETATM 1996 O  O   . HOH   F 5 .   ? -12.262 30.149  -13.168 1.00 24.26 ? 604 HOH   A O   1 
HETATM 1997 O  O   . HOH   F 5 .   ? -19.545 40.319  -10.720 1.00 30.45 ? 605 HOH   A O   1 
HETATM 1998 O  O   . HOH   F 5 .   ? -24.671 15.028  -17.707 1.00 43.73 ? 606 HOH   A O   1 
HETATM 1999 O  O   . HOH   F 5 .   ? -30.346 30.254  -9.341  1.00 43.08 ? 607 HOH   A O   1 
HETATM 2000 O  O   . HOH   F 5 .   ? -33.647 -11.261 11.314  1.00 28.62 ? 608 HOH   A O   1 
HETATM 2001 O  O   . HOH   F 5 .   ? -16.283 2.828   14.345  1.00 36.92 ? 609 HOH   A O   1 
HETATM 2002 O  O   . HOH   F 5 .   ? -9.419  31.813  -4.033  1.00 34.75 ? 610 HOH   A O   1 
HETATM 2003 O  O   . HOH   F 5 .   ? -29.784 33.767  5.473   1.00 42.51 ? 611 HOH   A O   1 
HETATM 2004 O  O   . HOH   F 5 .   ? -25.019 9.999   -15.102 1.00 44.16 ? 612 HOH   A O   1 
HETATM 2005 O  O   . HOH   F 5 .   ? -37.025 -8.935  -6.877  1.00 30.65 ? 613 HOH   A O   1 
HETATM 2006 O  O   . HOH   F 5 .   ? -38.264 4.752   17.727  1.00 18.11 ? 614 HOH   A O   1 
HETATM 2007 O  O   . HOH   F 5 .   ? -28.019 4.889   16.318  1.00 37.72 ? 615 HOH   A O   1 
HETATM 2008 O  O   . HOH   F 5 .   ? -9.237  9.530   -10.394 1.00 51.84 ? 616 HOH   A O   1 
HETATM 2009 O  O   . HOH   F 5 .   ? -8.527  19.629  -4.124  1.00 34.53 ? 617 HOH   A O   1 
HETATM 2010 O  O   . HOH   F 5 .   ? -10.935 35.781  11.070  1.00 45.81 ? 618 HOH   A O   1 
HETATM 2011 O  O   . HOH   F 5 .   ? -29.204 10.301  17.254  1.00 46.14 ? 619 HOH   A O   1 
HETATM 2012 O  O   . HOH   F 5 .   ? -18.357 26.814  -12.894 1.00 25.79 ? 620 HOH   A O   1 
HETATM 2013 O  O   . HOH   F 5 .   ? -28.042 -7.872  8.710   1.00 45.70 ? 621 HOH   A O   1 
HETATM 2014 O  O   . HOH   F 5 .   ? -34.232 -6.625  -13.102 1.00 26.29 ? 622 HOH   A O   1 
HETATM 2015 O  O   . HOH   F 5 .   ? -31.995 12.054  17.412  1.00 44.69 ? 623 HOH   A O   1 
HETATM 2016 O  O   . HOH   F 5 .   ? -25.204 30.490  9.773   1.00 44.87 ? 624 HOH   A O   1 
HETATM 2017 O  O   . HOH   F 5 .   ? -37.663 2.202   13.078  1.00 11.57 ? 625 HOH   A O   1 
HETATM 2018 O  O   . HOH   F 5 .   ? -39.240 -1.138  9.674   1.00 29.12 ? 626 HOH   A O   1 
HETATM 2019 O  O   . HOH   F 5 .   ? -34.060 20.490  4.091   1.00 38.27 ? 627 HOH   A O   1 
HETATM 2020 O  O   . HOH   F 5 .   ? -34.721 15.061  -18.387 1.00 36.04 ? 628 HOH   A O   1 
HETATM 2021 O  O   . HOH   F 5 .   ? -35.145 -11.395 9.277   1.00 26.38 ? 629 HOH   A O   1 
HETATM 2022 O  O   . HOH   F 5 .   ? -36.978 -7.905  6.359   1.00 43.52 ? 630 HOH   A O   1 
HETATM 2023 O  O   . HOH   F 5 .   ? -23.126 23.238  -17.040 1.00 45.26 ? 631 HOH   A O   1 
HETATM 2024 O  O   . HOH   F 5 .   ? -25.778 32.494  -4.643  1.00 48.14 ? 632 HOH   A O   1 
HETATM 2025 O  O   . HOH   F 5 .   ? -31.613 3.675   -17.322 1.00 23.02 ? 633 HOH   A O   1 
HETATM 2026 O  O   . HOH   F 5 .   ? -33.338 24.997  -10.046 1.00 27.38 ? 634 HOH   A O   1 
HETATM 2027 O  O   . HOH   F 5 .   ? -25.335 -2.983  -10.519 1.00 40.53 ? 635 HOH   A O   1 
HETATM 2028 O  O   . HOH   F 5 .   ? -41.690 3.263   5.687   1.00 26.34 ? 636 HOH   A O   1 
HETATM 2029 O  O   . HOH   F 5 .   ? -19.185 25.736  11.618  1.00 47.01 ? 637 HOH   A O   1 
HETATM 2030 O  O   . HOH   F 5 .   ? -34.663 9.612   20.575  1.00 43.87 ? 638 HOH   A O   1 
HETATM 2031 O  O   . HOH   F 5 .   ? -7.130  30.494  -12.239 1.00 45.12 ? 639 HOH   A O   1 
HETATM 2032 O  O   . HOH   F 5 .   ? -32.162 29.107  -10.533 1.00 42.49 ? 640 HOH   A O   1 
HETATM 2033 O  O   . HOH   F 5 .   ? -38.172 -8.927  -4.639  1.00 47.80 ? 641 HOH   A O   1 
HETATM 2034 O  O   . HOH   F 5 .   ? -20.839 2.304   15.611  1.00 39.89 ? 642 HOH   A O   1 
HETATM 2035 O  O   . HOH   F 5 .   ? -16.827 32.254  11.064  1.00 32.77 ? 643 HOH   A O   1 
HETATM 2036 O  O   . HOH   F 5 .   ? -40.897 -3.065  8.030   1.00 36.24 ? 644 HOH   A O   1 
HETATM 2037 O  O   . HOH   F 5 .   ? -24.886 20.930  17.426  1.00 39.38 ? 645 HOH   A O   1 
HETATM 2038 O  O   . HOH   F 5 .   ? -38.933 22.684  -7.360  1.00 39.07 ? 646 HOH   A O   1 
HETATM 2039 O  O   . HOH   F 5 .   ? -17.936 27.993  9.325   1.00 27.57 ? 647 HOH   A O   1 
HETATM 2040 O  O   . HOH   F 5 .   ? -42.207 18.508  -10.704 1.00 40.37 ? 648 HOH   A O   1 
HETATM 2041 O  O   . HOH   F 5 .   ? -29.018 19.214  13.620  1.00 38.91 ? 649 HOH   A O   1 
HETATM 2042 O  O   . HOH   F 5 .   ? -2.092  24.016  0.063   1.00 33.34 ? 650 HOH   A O   1 
HETATM 2043 O  O   . HOH   F 5 .   ? -42.166 -0.730  3.609   1.00 35.86 ? 651 HOH   A O   1 
HETATM 2044 O  O   . HOH   F 5 .   ? -42.330 -1.803  0.858   1.00 34.67 ? 652 HOH   A O   1 
HETATM 2045 O  O   . HOH   F 5 .   ? -30.298 35.190  1.468   1.00 31.43 ? 653 HOH   A O   1 
HETATM 2046 O  O   . HOH   F 5 .   ? -46.186 2.019   4.806   1.00 44.81 ? 654 HOH   A O   1 
HETATM 2047 O  O   . HOH   F 5 .   ? -25.882 -4.913  13.125  1.00 47.25 ? 655 HOH   A O   1 
HETATM 2048 O  O   . HOH   F 5 .   ? -40.332 25.543  -5.228  1.00 38.33 ? 656 HOH   A O   1 
HETATM 2049 O  O   . HOH   F 5 .   ? -22.405 34.751  8.719   1.00 33.44 ? 657 HOH   A O   1 
HETATM 2050 O  O   . HOH   F 5 .   ? -25.585 0.048   -12.165 1.00 37.41 ? 658 HOH   A O   1 
HETATM 2051 O  O   . HOH   F 5 .   ? -39.404 1.378   5.640   1.00 37.05 ? 659 HOH   A O   1 
HETATM 2052 O  O   . HOH   F 5 .   ? -27.000 9.801   -18.674 1.00 46.71 ? 660 HOH   A O   1 
HETATM 2053 O  O   . HOH   F 5 .   ? -38.274 1.121   8.094   1.00 24.11 ? 661 HOH   A O   1 
HETATM 2054 O  O   . HOH   F 5 .   ? -28.532 31.558  -4.731  1.00 38.56 ? 662 HOH   A O   1 
HETATM 2055 O  O   . HOH   F 5 .   ? -27.475 3.040   -15.831 1.00 33.69 ? 663 HOH   A O   1 
HETATM 2056 O  O   . HOH   F 5 .   ? -31.078 34.303  -2.351  1.00 37.04 ? 664 HOH   A O   1 
HETATM 2057 O  O   . HOH   F 5 .   ? -41.740 15.175  -17.125 1.00 50.51 ? 665 HOH   A O   1 
HETATM 2058 O  O   . HOH   F 5 .   ? -28.532 24.764  -17.209 1.00 45.11 ? 666 HOH   A O   1 
HETATM 2059 O  O   . HOH   F 5 .   ? -35.894 -6.658  1.751   1.00 37.56 ? 667 HOH   A O   1 
HETATM 2060 O  O   . HOH   F 5 .   ? -33.585 35.145  1.121   1.00 43.53 ? 668 HOH   A O   1 
HETATM 2061 O  O   . HOH   F 5 .   ? -31.102 2.687   -19.825 1.00 26.80 ? 669 HOH   A O   1 
HETATM 2062 O  O   . HOH   F 5 .   ? -25.160 1.887   -14.586 1.00 50.48 ? 670 HOH   A O   1 
# 
