data_8ZUQ
# 
_entry.id   8ZUQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8ZUQ         pdb_00008zuq 10.2210/pdb8zuq/pdb 
WWPDB D_1300048421 ?            ?                   
# 
_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       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZUQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              ktakeda@kuchem.kyoto-u.ac.jp 
_pdbx_contact_author.name_first         Kazuki 
_pdbx_contact_author.name_last          Takeda 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4094-6816 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Takeda, R.' 1 0000-0002-1638-4534 
'Takeda, K.' 2 0000-0002-4094-6816 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2045-2322 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            14 
_citation.language                  ? 
_citation.page_first                22832 
_citation.page_last                 22832 
_citation.title                     'Structural characterization of green fluorescent protein in the I-state.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41598-024-73696-y 
_citation.pdbx_database_id_PubMed   39353998 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Takeda, R.'   1 ? 
primary 'Tsutsumi, E.' 2 ? 
primary 'Okatsu, K.'   3 ? 
primary 'Fukai, S.'    4 ? 
primary 'Takeda, K.'   5 ? 
# 
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 'Green fluorescent protein' 25855.027 1   ? F99S,M153T,V163A,T203I,E222Q ? 
'Q80R was caused by a PCR error in the early study (Chalfie, M. et al., Science, 1994)' 
2 non-polymer syn 'MAGNESIUM ION'             24.305    2   ? ?                            ? ? 
3 water       nat water                       18.015    449 ? ?                            ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTF(GYS)VQCFSRYPDHMK
RHDFFKSAMPEGYVQERTISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYITADKQKN
GIKANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSIQSALSKDPNEKRDHMVLLQFVTAAGITH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKRH
DFFKSAMPEGYVQERTISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYITADKQKNGI
KANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSIQSALSKDPNEKRDHMVLLQFVTAAGITH
;
_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 'MAGNESIUM ION' MG  
3 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   LYS n 
1 3   GLY n 
1 4   GLU n 
1 5   GLU n 
1 6   LEU n 
1 7   PHE n 
1 8   THR n 
1 9   GLY n 
1 10  VAL n 
1 11  VAL n 
1 12  PRO n 
1 13  ILE n 
1 14  LEU n 
1 15  VAL n 
1 16  GLU n 
1 17  LEU n 
1 18  ASP n 
1 19  GLY n 
1 20  ASP n 
1 21  VAL n 
1 22  ASN n 
1 23  GLY n 
1 24  HIS n 
1 25  LYS n 
1 26  PHE n 
1 27  SER n 
1 28  VAL n 
1 29  SER n 
1 30  GLY n 
1 31  GLU n 
1 32  GLY n 
1 33  GLU n 
1 34  GLY n 
1 35  ASP n 
1 36  ALA n 
1 37  THR n 
1 38  TYR n 
1 39  GLY n 
1 40  LYS n 
1 41  LEU n 
1 42  THR n 
1 43  LEU n 
1 44  LYS n 
1 45  PHE n 
1 46  ILE n 
1 47  CYS n 
1 48  THR n 
1 49  THR n 
1 50  GLY n 
1 51  LYS n 
1 52  LEU n 
1 53  PRO n 
1 54  VAL n 
1 55  PRO n 
1 56  TRP n 
1 57  PRO n 
1 58  THR n 
1 59  LEU n 
1 60  VAL n 
1 61  THR n 
1 62  THR n 
1 63  PHE n 
1 64  GYS n 
1 65  VAL n 
1 66  GLN n 
1 67  CYS n 
1 68  PHE n 
1 69  SER n 
1 70  ARG n 
1 71  TYR n 
1 72  PRO n 
1 73  ASP n 
1 74  HIS n 
1 75  MET n 
1 76  LYS n 
1 77  ARG n 
1 78  HIS n 
1 79  ASP n 
1 80  PHE n 
1 81  PHE n 
1 82  LYS n 
1 83  SER n 
1 84  ALA n 
1 85  MET n 
1 86  PRO n 
1 87  GLU n 
1 88  GLY n 
1 89  TYR n 
1 90  VAL n 
1 91  GLN n 
1 92  GLU n 
1 93  ARG n 
1 94  THR n 
1 95  ILE n 
1 96  SER n 
1 97  PHE n 
1 98  LYS n 
1 99  ASP n 
1 100 ASP n 
1 101 GLY n 
1 102 ASN n 
1 103 TYR n 
1 104 LYS n 
1 105 THR n 
1 106 ARG n 
1 107 ALA n 
1 108 GLU n 
1 109 VAL n 
1 110 LYS n 
1 111 PHE n 
1 112 GLU n 
1 113 GLY n 
1 114 ASP n 
1 115 THR n 
1 116 LEU n 
1 117 VAL n 
1 118 ASN n 
1 119 ARG n 
1 120 ILE n 
1 121 GLU n 
1 122 LEU n 
1 123 LYS n 
1 124 GLY n 
1 125 ILE n 
1 126 ASP n 
1 127 PHE n 
1 128 LYS n 
1 129 GLU n 
1 130 ASP n 
1 131 GLY n 
1 132 ASN n 
1 133 ILE n 
1 134 LEU n 
1 135 GLY n 
1 136 HIS n 
1 137 LYS n 
1 138 LEU n 
1 139 GLU n 
1 140 TYR n 
1 141 ASN n 
1 142 TYR n 
1 143 ASN n 
1 144 SER n 
1 145 HIS n 
1 146 ASN n 
1 147 VAL n 
1 148 TYR n 
1 149 ILE n 
1 150 THR n 
1 151 ALA n 
1 152 ASP n 
1 153 LYS n 
1 154 GLN n 
1 155 LYS n 
1 156 ASN n 
1 157 GLY n 
1 158 ILE n 
1 159 LYS n 
1 160 ALA n 
1 161 ASN n 
1 162 PHE n 
1 163 LYS n 
1 164 ILE n 
1 165 ARG n 
1 166 HIS n 
1 167 ASN n 
1 168 ILE n 
1 169 GLU n 
1 170 ASP n 
1 171 GLY n 
1 172 SER n 
1 173 VAL n 
1 174 GLN n 
1 175 LEU n 
1 176 ALA n 
1 177 ASP n 
1 178 HIS n 
1 179 TYR n 
1 180 GLN n 
1 181 GLN n 
1 182 ASN n 
1 183 THR n 
1 184 PRO n 
1 185 ILE n 
1 186 GLY n 
1 187 ASP n 
1 188 GLY n 
1 189 PRO n 
1 190 VAL n 
1 191 LEU n 
1 192 LEU n 
1 193 PRO n 
1 194 ASP n 
1 195 ASN n 
1 196 HIS n 
1 197 TYR n 
1 198 LEU n 
1 199 SER n 
1 200 ILE n 
1 201 GLN n 
1 202 SER n 
1 203 ALA n 
1 204 LEU n 
1 205 SER n 
1 206 LYS n 
1 207 ASP n 
1 208 PRO n 
1 209 ASN n 
1 210 GLU n 
1 211 LYS n 
1 212 ARG n 
1 213 ASP n 
1 214 HIS n 
1 215 MET n 
1 216 VAL n 
1 217 LEU n 
1 218 LEU n 
1 219 GLN n 
1 220 PHE n 
1 221 VAL n 
1 222 THR n 
1 223 ALA n 
1 224 ALA n 
1 225 GLY n 
1 226 ILE n 
1 227 THR n 
1 228 HIS 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                   228 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GFP 
_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      'Aequorea victoria' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6100 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                           'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ?                           'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                           'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                           'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE ?                           'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                           'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                           'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ?                           'C2 H5 N O2'     75.067  
GYS 'L-peptide linking' n 
'[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC ACID' 
'CHROMOPHORE (SER-TYR-GLY)' 'C14 H15 N3 O5'  305.286 
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 
MG  non-polymer         . 'MAGNESIUM ION' ?                           'Mg 2'           24.305  
PHE 'L-peptide linking' y PHENYLALANINE ?                           'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ?                           'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ?                           'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ?                           'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                           'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ?                           'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ?                           'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   2   2   SER SER A . n 
A 1 2   LYS 2   3   3   LYS LYS A . n 
A 1 3   GLY 3   4   4   GLY GLY A . n 
A 1 4   GLU 4   5   5   GLU GLU A . n 
A 1 5   GLU 5   6   6   GLU GLU A . n 
A 1 6   LEU 6   7   7   LEU LEU A . n 
A 1 7   PHE 7   8   8   PHE PHE A . n 
A 1 8   THR 8   9   9   THR THR A . n 
A 1 9   GLY 9   10  10  GLY GLY A . n 
A 1 10  VAL 10  11  11  VAL VAL A . n 
A 1 11  VAL 11  12  12  VAL VAL A . n 
A 1 12  PRO 12  13  13  PRO PRO A . n 
A 1 13  ILE 13  14  14  ILE ILE A . n 
A 1 14  LEU 14  15  15  LEU LEU A . n 
A 1 15  VAL 15  16  16  VAL VAL A . n 
A 1 16  GLU 16  17  17  GLU GLU A . n 
A 1 17  LEU 17  18  18  LEU LEU A . n 
A 1 18  ASP 18  19  19  ASP ASP A . n 
A 1 19  GLY 19  20  20  GLY GLY A . n 
A 1 20  ASP 20  21  21  ASP ASP A . n 
A 1 21  VAL 21  22  22  VAL VAL A . n 
A 1 22  ASN 22  23  23  ASN ASN A . n 
A 1 23  GLY 23  24  24  GLY GLY A . n 
A 1 24  HIS 24  25  25  HIS HIS A . n 
A 1 25  LYS 25  26  26  LYS LYS A . n 
A 1 26  PHE 26  27  27  PHE PHE A . n 
A 1 27  SER 27  28  28  SER SER A . n 
A 1 28  VAL 28  29  29  VAL VAL A . n 
A 1 29  SER 29  30  30  SER SER A . n 
A 1 30  GLY 30  31  31  GLY GLY A . n 
A 1 31  GLU 31  32  32  GLU GLU A . n 
A 1 32  GLY 32  33  33  GLY GLY A . n 
A 1 33  GLU 33  34  34  GLU GLU A . n 
A 1 34  GLY 34  35  35  GLY GLY A . n 
A 1 35  ASP 35  36  36  ASP ASP A . n 
A 1 36  ALA 36  37  37  ALA ALA A . n 
A 1 37  THR 37  38  38  THR THR A . n 
A 1 38  TYR 38  39  39  TYR TYR A . n 
A 1 39  GLY 39  40  40  GLY GLY A . n 
A 1 40  LYS 40  41  41  LYS LYS A . n 
A 1 41  LEU 41  42  42  LEU LEU A . n 
A 1 42  THR 42  43  43  THR THR A . n 
A 1 43  LEU 43  44  44  LEU LEU A . n 
A 1 44  LYS 44  45  45  LYS LYS A . n 
A 1 45  PHE 45  46  46  PHE PHE A . n 
A 1 46  ILE 46  47  47  ILE ILE A . n 
A 1 47  CYS 47  48  48  CYS CYS A . n 
A 1 48  THR 48  49  49  THR THR A . n 
A 1 49  THR 49  50  50  THR THR A . n 
A 1 50  GLY 50  51  51  GLY GLY A . n 
A 1 51  LYS 51  52  52  LYS LYS A . n 
A 1 52  LEU 52  53  53  LEU LEU A . n 
A 1 53  PRO 53  54  54  PRO PRO A . n 
A 1 54  VAL 54  55  55  VAL VAL A . n 
A 1 55  PRO 55  56  56  PRO PRO A . n 
A 1 56  TRP 56  57  57  TRP TRP A . n 
A 1 57  PRO 57  58  58  PRO PRO A . n 
A 1 58  THR 58  59  59  THR THR A . n 
A 1 59  LEU 59  60  60  LEU LEU A . n 
A 1 60  VAL 60  61  61  VAL VAL A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  THR 62  63  63  THR THR A . n 
A 1 63  PHE 63  64  64  PHE PHE A . n 
A 1 64  GYS 64  66  66  GYS GYS A . n 
A 1 65  VAL 65  68  68  VAL VAL A . n 
A 1 66  GLN 66  69  69  GLN GLN A . n 
A 1 67  CYS 67  70  70  CYS CYS A . n 
A 1 68  PHE 68  71  71  PHE PHE A . n 
A 1 69  SER 69  72  72  SER SER A . n 
A 1 70  ARG 70  73  73  ARG ARG A . n 
A 1 71  TYR 71  74  74  TYR TYR A . n 
A 1 72  PRO 72  75  75  PRO PRO A . n 
A 1 73  ASP 73  76  76  ASP ASP A . n 
A 1 74  HIS 74  77  77  HIS HIS A . n 
A 1 75  MET 75  78  78  MET MET A . n 
A 1 76  LYS 76  79  79  LYS LYS A . n 
A 1 77  ARG 77  80  80  ARG ARG A . n 
A 1 78  HIS 78  81  81  HIS HIS A . n 
A 1 79  ASP 79  82  82  ASP ASP A . n 
A 1 80  PHE 80  83  83  PHE PHE A . n 
A 1 81  PHE 81  84  84  PHE PHE A . n 
A 1 82  LYS 82  85  85  LYS LYS A . n 
A 1 83  SER 83  86  86  SER SER A . n 
A 1 84  ALA 84  87  87  ALA ALA A . n 
A 1 85  MET 85  88  88  MET MET A . n 
A 1 86  PRO 86  89  89  PRO PRO A . n 
A 1 87  GLU 87  90  90  GLU GLU A . n 
A 1 88  GLY 88  91  91  GLY GLY A . n 
A 1 89  TYR 89  92  92  TYR TYR A . n 
A 1 90  VAL 90  93  93  VAL VAL A . n 
A 1 91  GLN 91  94  94  GLN GLN A . n 
A 1 92  GLU 92  95  95  GLU GLU A . n 
A 1 93  ARG 93  96  96  ARG ARG A . n 
A 1 94  THR 94  97  97  THR THR A . n 
A 1 95  ILE 95  98  98  ILE ILE A . n 
A 1 96  SER 96  99  99  SER SER A . n 
A 1 97  PHE 97  100 100 PHE PHE A . n 
A 1 98  LYS 98  101 101 LYS LYS A . n 
A 1 99  ASP 99  102 102 ASP ASP A . n 
A 1 100 ASP 100 103 103 ASP ASP A . n 
A 1 101 GLY 101 104 104 GLY GLY A . n 
A 1 102 ASN 102 105 105 ASN ASN A . n 
A 1 103 TYR 103 106 106 TYR TYR A . n 
A 1 104 LYS 104 107 107 LYS LYS A . n 
A 1 105 THR 105 108 108 THR THR A . n 
A 1 106 ARG 106 109 109 ARG ARG A . n 
A 1 107 ALA 107 110 110 ALA ALA A . n 
A 1 108 GLU 108 111 111 GLU GLU A . n 
A 1 109 VAL 109 112 112 VAL VAL A . n 
A 1 110 LYS 110 113 113 LYS LYS A . n 
A 1 111 PHE 111 114 114 PHE PHE A . n 
A 1 112 GLU 112 115 115 GLU GLU A . n 
A 1 113 GLY 113 116 116 GLY GLY A . n 
A 1 114 ASP 114 117 117 ASP ASP A . n 
A 1 115 THR 115 118 118 THR THR A . n 
A 1 116 LEU 116 119 119 LEU LEU A . n 
A 1 117 VAL 117 120 120 VAL VAL A . n 
A 1 118 ASN 118 121 121 ASN ASN A . n 
A 1 119 ARG 119 122 122 ARG ARG A . n 
A 1 120 ILE 120 123 123 ILE ILE A . n 
A 1 121 GLU 121 124 124 GLU GLU A . n 
A 1 122 LEU 122 125 125 LEU LEU A . n 
A 1 123 LYS 123 126 126 LYS LYS A . n 
A 1 124 GLY 124 127 127 GLY GLY A . n 
A 1 125 ILE 125 128 128 ILE ILE A . n 
A 1 126 ASP 126 129 129 ASP ASP A . n 
A 1 127 PHE 127 130 130 PHE PHE A . n 
A 1 128 LYS 128 131 131 LYS LYS A . n 
A 1 129 GLU 129 132 132 GLU GLU A . n 
A 1 130 ASP 130 133 133 ASP ASP A . n 
A 1 131 GLY 131 134 134 GLY GLY A . n 
A 1 132 ASN 132 135 135 ASN ASN A . n 
A 1 133 ILE 133 136 136 ILE ILE A . n 
A 1 134 LEU 134 137 137 LEU LEU A . n 
A 1 135 GLY 135 138 138 GLY GLY A . n 
A 1 136 HIS 136 139 139 HIS HIS A . n 
A 1 137 LYS 137 140 140 LYS LYS A . n 
A 1 138 LEU 138 141 141 LEU LEU A . n 
A 1 139 GLU 139 142 142 GLU GLU A . n 
A 1 140 TYR 140 143 143 TYR TYR A . n 
A 1 141 ASN 141 144 144 ASN ASN A . n 
A 1 142 TYR 142 145 145 TYR TYR A . n 
A 1 143 ASN 143 146 146 ASN ASN A . n 
A 1 144 SER 144 147 147 SER SER A . n 
A 1 145 HIS 145 148 148 HIS HIS A . n 
A 1 146 ASN 146 149 149 ASN ASN A . n 
A 1 147 VAL 147 150 150 VAL VAL A . n 
A 1 148 TYR 148 151 151 TYR TYR A . n 
A 1 149 ILE 149 152 152 ILE ILE A . n 
A 1 150 THR 150 153 153 THR THR A . n 
A 1 151 ALA 151 154 154 ALA ALA A . n 
A 1 152 ASP 152 155 155 ASP ASP A . n 
A 1 153 LYS 153 156 156 LYS LYS A . n 
A 1 154 GLN 154 157 157 GLN GLN A . n 
A 1 155 LYS 155 158 158 LYS LYS A . n 
A 1 156 ASN 156 159 159 ASN ASN A . n 
A 1 157 GLY 157 160 160 GLY GLY A . n 
A 1 158 ILE 158 161 161 ILE ILE A . n 
A 1 159 LYS 159 162 162 LYS LYS A . n 
A 1 160 ALA 160 163 163 ALA ALA A . n 
A 1 161 ASN 161 164 164 ASN ASN A . n 
A 1 162 PHE 162 165 165 PHE PHE A . n 
A 1 163 LYS 163 166 166 LYS LYS A . n 
A 1 164 ILE 164 167 167 ILE ILE A . n 
A 1 165 ARG 165 168 168 ARG ARG A . n 
A 1 166 HIS 166 169 169 HIS HIS A . n 
A 1 167 ASN 167 170 170 ASN ASN A . n 
A 1 168 ILE 168 171 171 ILE ILE A . n 
A 1 169 GLU 169 172 172 GLU GLU A . n 
A 1 170 ASP 170 173 173 ASP ASP A . n 
A 1 171 GLY 171 174 174 GLY GLY A . n 
A 1 172 SER 172 175 175 SER SER A . n 
A 1 173 VAL 173 176 176 VAL VAL A . n 
A 1 174 GLN 174 177 177 GLN GLN A . n 
A 1 175 LEU 175 178 178 LEU LEU A . n 
A 1 176 ALA 176 179 179 ALA ALA A . n 
A 1 177 ASP 177 180 180 ASP ASP A . n 
A 1 178 HIS 178 181 181 HIS HIS A . n 
A 1 179 TYR 179 182 182 TYR TYR A . n 
A 1 180 GLN 180 183 183 GLN GLN A . n 
A 1 181 GLN 181 184 184 GLN GLN A . n 
A 1 182 ASN 182 185 185 ASN ASN A . n 
A 1 183 THR 183 186 186 THR THR A . n 
A 1 184 PRO 184 187 187 PRO PRO A . n 
A 1 185 ILE 185 188 188 ILE ILE A . n 
A 1 186 GLY 186 189 189 GLY GLY A . n 
A 1 187 ASP 187 190 190 ASP ASP A . n 
A 1 188 GLY 188 191 191 GLY GLY A . n 
A 1 189 PRO 189 192 192 PRO PRO A . n 
A 1 190 VAL 190 193 193 VAL VAL A . n 
A 1 191 LEU 191 194 194 LEU LEU A . n 
A 1 192 LEU 192 195 195 LEU LEU A . n 
A 1 193 PRO 193 196 196 PRO PRO A . n 
A 1 194 ASP 194 197 197 ASP ASP A . n 
A 1 195 ASN 195 198 198 ASN ASN A . n 
A 1 196 HIS 196 199 199 HIS HIS A . n 
A 1 197 TYR 197 200 200 TYR TYR A . n 
A 1 198 LEU 198 201 201 LEU LEU A . n 
A 1 199 SER 199 202 202 SER SER A . n 
A 1 200 ILE 200 203 203 ILE ILE A . n 
A 1 201 GLN 201 204 204 GLN GLN A . n 
A 1 202 SER 202 205 205 SER SER A . n 
A 1 203 ALA 203 206 206 ALA ALA A . n 
A 1 204 LEU 204 207 207 LEU LEU A . n 
A 1 205 SER 205 208 208 SER SER A . n 
A 1 206 LYS 206 209 209 LYS LYS A . n 
A 1 207 ASP 207 210 210 ASP ASP A . n 
A 1 208 PRO 208 211 211 PRO PRO A . n 
A 1 209 ASN 209 212 212 ASN ASN A . n 
A 1 210 GLU 210 213 213 GLU GLU A . n 
A 1 211 LYS 211 214 214 LYS LYS A . n 
A 1 212 ARG 212 215 215 ARG ARG A . n 
A 1 213 ASP 213 216 216 ASP ASP A . n 
A 1 214 HIS 214 217 217 HIS HIS A . n 
A 1 215 MET 215 218 218 MET MET A . n 
A 1 216 VAL 216 219 219 VAL VAL A . n 
A 1 217 LEU 217 220 220 LEU LEU A . n 
A 1 218 LEU 218 221 221 LEU LEU A . n 
A 1 219 GLN 219 222 222 GLN GLN A . n 
A 1 220 PHE 220 223 223 PHE PHE A . n 
A 1 221 VAL 221 224 224 VAL VAL A . n 
A 1 222 THR 222 225 225 THR THR A . n 
A 1 223 ALA 223 226 226 ALA ALA A . n 
A 1 224 ALA 224 227 227 ALA ALA A . n 
A 1 225 GLY 225 228 228 GLY GLY A . n 
A 1 226 ILE 226 229 229 ILE ILE A . n 
A 1 227 THR 227 230 230 THR THR A . n 
A 1 228 HIS 228 231 231 HIS HIS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 MG  1   301 301 MG  MG  A . 
C 2 MG  1   302 302 MG  MG  A . 
D 3 HOH 1   401 401 HOH HOH A . 
D 3 HOH 2   402 402 HOH HOH A . 
D 3 HOH 3   403 403 HOH HOH A . 
D 3 HOH 4   404 404 HOH HOH A . 
D 3 HOH 5   405 405 HOH HOH A . 
D 3 HOH 6   406 406 HOH HOH A . 
D 3 HOH 7   407 407 HOH HOH A . 
D 3 HOH 8   408 408 HOH HOH A . 
D 3 HOH 9   409 409 HOH HOH A . 
D 3 HOH 10  410 410 HOH HOH A . 
D 3 HOH 11  411 411 HOH HOH A . 
D 3 HOH 12  412 412 HOH HOH A . 
D 3 HOH 13  413 413 HOH HOH A . 
D 3 HOH 14  414 414 HOH HOH A . 
D 3 HOH 15  415 415 HOH HOH A . 
D 3 HOH 16  416 416 HOH HOH A . 
D 3 HOH 17  417 417 HOH HOH A . 
D 3 HOH 18  418 418 HOH HOH A . 
D 3 HOH 19  419 419 HOH HOH A . 
D 3 HOH 20  420 420 HOH HOH A . 
D 3 HOH 21  421 421 HOH HOH A . 
D 3 HOH 22  422 422 HOH HOH A . 
D 3 HOH 23  423 423 HOH HOH A . 
D 3 HOH 24  424 424 HOH HOH A . 
D 3 HOH 25  425 425 HOH HOH A . 
D 3 HOH 26  426 426 HOH HOH A . 
D 3 HOH 27  427 427 HOH HOH A . 
D 3 HOH 28  428 428 HOH HOH A . 
D 3 HOH 29  429 429 HOH HOH A . 
D 3 HOH 30  430 430 HOH HOH A . 
D 3 HOH 31  431 431 HOH HOH A . 
D 3 HOH 32  432 432 HOH HOH A . 
D 3 HOH 33  433 433 HOH HOH A . 
D 3 HOH 34  434 434 HOH HOH A . 
D 3 HOH 35  435 435 HOH HOH A . 
D 3 HOH 36  436 436 HOH HOH A . 
D 3 HOH 37  437 437 HOH HOH A . 
D 3 HOH 38  438 438 HOH HOH A . 
D 3 HOH 39  439 439 HOH HOH A . 
D 3 HOH 40  440 440 HOH HOH A . 
D 3 HOH 41  441 441 HOH HOH A . 
D 3 HOH 42  442 442 HOH HOH A . 
D 3 HOH 43  443 443 HOH HOH A . 
D 3 HOH 44  444 444 HOH HOH A . 
D 3 HOH 45  445 445 HOH HOH A . 
D 3 HOH 46  446 446 HOH HOH A . 
D 3 HOH 47  447 447 HOH HOH A . 
D 3 HOH 48  448 448 HOH HOH A . 
D 3 HOH 49  449 449 HOH HOH A . 
D 3 HOH 50  450 450 HOH HOH A . 
D 3 HOH 51  451 451 HOH HOH A . 
D 3 HOH 52  452 452 HOH HOH A . 
D 3 HOH 53  453 453 HOH HOH A . 
D 3 HOH 54  454 454 HOH HOH A . 
D 3 HOH 55  455 455 HOH HOH A . 
D 3 HOH 56  456 456 HOH HOH A . 
D 3 HOH 57  457 457 HOH HOH A . 
D 3 HOH 58  458 458 HOH HOH A . 
D 3 HOH 59  459 459 HOH HOH A . 
D 3 HOH 60  460 460 HOH HOH A . 
D 3 HOH 61  461 461 HOH HOH A . 
D 3 HOH 62  462 462 HOH HOH A . 
D 3 HOH 63  463 463 HOH HOH A . 
D 3 HOH 64  464 464 HOH HOH A . 
D 3 HOH 65  465 465 HOH HOH A . 
D 3 HOH 66  466 466 HOH HOH A . 
D 3 HOH 67  467 467 HOH HOH A . 
D 3 HOH 68  468 468 HOH HOH A . 
D 3 HOH 69  469 469 HOH HOH A . 
D 3 HOH 70  470 470 HOH HOH A . 
D 3 HOH 71  471 471 HOH HOH A . 
D 3 HOH 72  472 472 HOH HOH A . 
D 3 HOH 73  473 473 HOH HOH A . 
D 3 HOH 74  474 474 HOH HOH A . 
D 3 HOH 75  475 475 HOH HOH A . 
D 3 HOH 76  476 476 HOH HOH A . 
D 3 HOH 77  477 477 HOH HOH A . 
D 3 HOH 78  478 478 HOH HOH A . 
D 3 HOH 79  479 479 HOH HOH A . 
D 3 HOH 80  480 480 HOH HOH A . 
D 3 HOH 81  481 481 HOH HOH A . 
D 3 HOH 82  482 482 HOH HOH A . 
D 3 HOH 83  483 483 HOH HOH A . 
D 3 HOH 84  484 484 HOH HOH A . 
D 3 HOH 85  485 485 HOH HOH A . 
D 3 HOH 86  486 486 HOH HOH A . 
D 3 HOH 87  487 487 HOH HOH A . 
D 3 HOH 88  488 488 HOH HOH A . 
D 3 HOH 89  489 489 HOH HOH A . 
D 3 HOH 90  490 490 HOH HOH A . 
D 3 HOH 91  491 491 HOH HOH A . 
D 3 HOH 92  492 492 HOH HOH A . 
D 3 HOH 93  493 493 HOH HOH A . 
D 3 HOH 94  494 494 HOH HOH A . 
D 3 HOH 95  495 495 HOH HOH A . 
D 3 HOH 96  496 496 HOH HOH A . 
D 3 HOH 97  497 497 HOH HOH A . 
D 3 HOH 98  498 498 HOH HOH A . 
D 3 HOH 99  499 499 HOH HOH A . 
D 3 HOH 100 500 500 HOH HOH A . 
D 3 HOH 101 501 501 HOH HOH A . 
D 3 HOH 102 502 502 HOH HOH A . 
D 3 HOH 103 503 503 HOH HOH A . 
D 3 HOH 104 504 504 HOH HOH A . 
D 3 HOH 105 505 505 HOH HOH A . 
D 3 HOH 106 506 506 HOH HOH A . 
D 3 HOH 107 507 507 HOH HOH A . 
D 3 HOH 108 508 508 HOH HOH A . 
D 3 HOH 109 509 509 HOH HOH A . 
D 3 HOH 110 510 510 HOH HOH A . 
D 3 HOH 111 511 511 HOH HOH A . 
D 3 HOH 112 512 512 HOH HOH A . 
D 3 HOH 113 513 513 HOH HOH A . 
D 3 HOH 114 514 514 HOH HOH A . 
D 3 HOH 115 515 515 HOH HOH A . 
D 3 HOH 116 516 516 HOH HOH A . 
D 3 HOH 117 517 517 HOH HOH A . 
D 3 HOH 118 518 518 HOH HOH A . 
D 3 HOH 119 519 519 HOH HOH A . 
D 3 HOH 120 520 520 HOH HOH A . 
D 3 HOH 121 521 521 HOH HOH A . 
D 3 HOH 122 522 522 HOH HOH A . 
D 3 HOH 123 523 523 HOH HOH A . 
D 3 HOH 124 524 524 HOH HOH A . 
D 3 HOH 125 525 525 HOH HOH A . 
D 3 HOH 126 526 526 HOH HOH A . 
D 3 HOH 127 527 527 HOH HOH A . 
D 3 HOH 128 528 528 HOH HOH A . 
D 3 HOH 129 529 529 HOH HOH A . 
D 3 HOH 130 530 530 HOH HOH A . 
D 3 HOH 131 531 531 HOH HOH A . 
D 3 HOH 132 532 532 HOH HOH A . 
D 3 HOH 133 533 533 HOH HOH A . 
D 3 HOH 134 534 534 HOH HOH A . 
D 3 HOH 135 535 535 HOH HOH A . 
D 3 HOH 136 536 536 HOH HOH A . 
D 3 HOH 137 537 537 HOH HOH A . 
D 3 HOH 138 538 538 HOH HOH A . 
D 3 HOH 139 539 539 HOH HOH A . 
D 3 HOH 140 540 540 HOH HOH A . 
D 3 HOH 141 541 541 HOH HOH A . 
D 3 HOH 142 542 542 HOH HOH A . 
D 3 HOH 143 543 543 HOH HOH A . 
D 3 HOH 144 544 544 HOH HOH A . 
D 3 HOH 145 545 545 HOH HOH A . 
D 3 HOH 146 546 546 HOH HOH A . 
D 3 HOH 147 547 547 HOH HOH A . 
D 3 HOH 148 548 548 HOH HOH A . 
D 3 HOH 149 549 549 HOH HOH A . 
D 3 HOH 150 550 550 HOH HOH A . 
D 3 HOH 151 551 551 HOH HOH A . 
D 3 HOH 152 552 552 HOH HOH A . 
D 3 HOH 153 553 553 HOH HOH A . 
D 3 HOH 154 554 554 HOH HOH A . 
D 3 HOH 155 555 555 HOH HOH A . 
D 3 HOH 156 556 556 HOH HOH A . 
D 3 HOH 157 557 557 HOH HOH A . 
D 3 HOH 158 558 558 HOH HOH A . 
D 3 HOH 159 559 559 HOH HOH A . 
D 3 HOH 160 560 560 HOH HOH A . 
D 3 HOH 161 561 561 HOH HOH A . 
D 3 HOH 162 562 562 HOH HOH A . 
D 3 HOH 163 563 563 HOH HOH A . 
D 3 HOH 164 564 564 HOH HOH A . 
D 3 HOH 165 565 565 HOH HOH A . 
D 3 HOH 166 566 566 HOH HOH A . 
D 3 HOH 167 567 567 HOH HOH A . 
D 3 HOH 168 568 568 HOH HOH A . 
D 3 HOH 169 569 569 HOH HOH A . 
D 3 HOH 170 570 570 HOH HOH A . 
D 3 HOH 171 571 571 HOH HOH A . 
D 3 HOH 172 572 572 HOH HOH A . 
D 3 HOH 173 573 573 HOH HOH A . 
D 3 HOH 174 574 574 HOH HOH A . 
D 3 HOH 175 575 575 HOH HOH A . 
D 3 HOH 176 577 577 HOH HOH A . 
D 3 HOH 177 578 578 HOH HOH A . 
D 3 HOH 178 579 579 HOH HOH A . 
D 3 HOH 179 580 580 HOH HOH A . 
D 3 HOH 180 581 581 HOH HOH A . 
D 3 HOH 181 582 582 HOH HOH A . 
D 3 HOH 182 583 583 HOH HOH A . 
D 3 HOH 183 584 584 HOH HOH A . 
D 3 HOH 184 585 585 HOH HOH A . 
D 3 HOH 185 586 586 HOH HOH A . 
D 3 HOH 186 587 587 HOH HOH A . 
D 3 HOH 187 588 588 HOH HOH A . 
D 3 HOH 188 589 589 HOH HOH A . 
D 3 HOH 189 590 590 HOH HOH A . 
D 3 HOH 190 591 591 HOH HOH A . 
D 3 HOH 191 592 592 HOH HOH A . 
D 3 HOH 192 593 593 HOH HOH A . 
D 3 HOH 193 594 594 HOH HOH A . 
D 3 HOH 194 595 595 HOH HOH A . 
D 3 HOH 195 596 596 HOH HOH A . 
D 3 HOH 196 597 597 HOH HOH A . 
D 3 HOH 197 598 598 HOH HOH A . 
D 3 HOH 198 599 599 HOH HOH A . 
D 3 HOH 199 600 600 HOH HOH A . 
D 3 HOH 200 601 601 HOH HOH A . 
D 3 HOH 201 602 602 HOH HOH A . 
D 3 HOH 202 603 603 HOH HOH A . 
D 3 HOH 203 604 604 HOH HOH A . 
D 3 HOH 204 605 605 HOH HOH A . 
D 3 HOH 205 606 606 HOH HOH A . 
D 3 HOH 206 607 607 HOH HOH A . 
D 3 HOH 207 608 608 HOH HOH A . 
D 3 HOH 208 609 609 HOH HOH A . 
D 3 HOH 209 610 610 HOH HOH A . 
D 3 HOH 210 611 611 HOH HOH A . 
D 3 HOH 211 612 612 HOH HOH A . 
D 3 HOH 212 613 613 HOH HOH A . 
D 3 HOH 213 614 614 HOH HOH A . 
D 3 HOH 214 615 615 HOH HOH A . 
D 3 HOH 215 616 616 HOH HOH A . 
D 3 HOH 216 617 617 HOH HOH A . 
D 3 HOH 217 618 618 HOH HOH A . 
D 3 HOH 218 619 619 HOH HOH A . 
D 3 HOH 219 620 620 HOH HOH A . 
D 3 HOH 220 621 621 HOH HOH A . 
D 3 HOH 221 622 622 HOH HOH A . 
D 3 HOH 222 623 623 HOH HOH A . 
D 3 HOH 223 624 624 HOH HOH A . 
D 3 HOH 224 625 625 HOH HOH A . 
D 3 HOH 225 626 626 HOH HOH A . 
D 3 HOH 226 627 627 HOH HOH A . 
D 3 HOH 227 628 628 HOH HOH A . 
D 3 HOH 228 629 629 HOH HOH A . 
D 3 HOH 229 630 630 HOH HOH A . 
D 3 HOH 230 631 631 HOH HOH A . 
D 3 HOH 231 632 632 HOH HOH A . 
D 3 HOH 232 633 633 HOH HOH A . 
D 3 HOH 233 635 635 HOH HOH A . 
D 3 HOH 234 636 636 HOH HOH A . 
D 3 HOH 235 637 637 HOH HOH A . 
D 3 HOH 236 638 638 HOH HOH A . 
D 3 HOH 237 639 639 HOH HOH A . 
D 3 HOH 238 640 640 HOH HOH A . 
D 3 HOH 239 641 641 HOH HOH A . 
D 3 HOH 240 642 642 HOH HOH A . 
D 3 HOH 241 643 643 HOH HOH A . 
D 3 HOH 242 644 644 HOH HOH A . 
D 3 HOH 243 645 645 HOH HOH A . 
D 3 HOH 244 646 646 HOH HOH A . 
D 3 HOH 245 647 647 HOH HOH A . 
D 3 HOH 246 648 648 HOH HOH A . 
D 3 HOH 247 649 649 HOH HOH A . 
D 3 HOH 248 650 650 HOH HOH A . 
D 3 HOH 249 651 651 HOH HOH A . 
D 3 HOH 250 652 652 HOH HOH A . 
D 3 HOH 251 653 653 HOH HOH A . 
D 3 HOH 252 654 654 HOH HOH A . 
D 3 HOH 253 655 655 HOH HOH A . 
D 3 HOH 254 656 656 HOH HOH A . 
D 3 HOH 255 657 657 HOH HOH A . 
D 3 HOH 256 658 658 HOH HOH A . 
D 3 HOH 257 659 659 HOH HOH A . 
D 3 HOH 258 660 660 HOH HOH A . 
D 3 HOH 259 661 661 HOH HOH A . 
D 3 HOH 260 662 662 HOH HOH A . 
D 3 HOH 261 663 663 HOH HOH A . 
D 3 HOH 262 664 664 HOH HOH A . 
D 3 HOH 263 665 665 HOH HOH A . 
D 3 HOH 264 666 666 HOH HOH A . 
D 3 HOH 265 667 667 HOH HOH A . 
D 3 HOH 266 668 668 HOH HOH A . 
D 3 HOH 267 669 669 HOH HOH A . 
D 3 HOH 268 670 670 HOH HOH A . 
D 3 HOH 269 671 671 HOH HOH A . 
D 3 HOH 270 672 672 HOH HOH A . 
D 3 HOH 271 673 673 HOH HOH A . 
D 3 HOH 272 674 674 HOH HOH A . 
D 3 HOH 273 675 675 HOH HOH A . 
D 3 HOH 274 676 676 HOH HOH A . 
D 3 HOH 275 677 677 HOH HOH A . 
D 3 HOH 276 678 678 HOH HOH A . 
D 3 HOH 277 679 679 HOH HOH A . 
D 3 HOH 278 680 680 HOH HOH A . 
D 3 HOH 279 681 681 HOH HOH A . 
D 3 HOH 280 682 682 HOH HOH A . 
D 3 HOH 281 683 683 HOH HOH A . 
D 3 HOH 282 684 684 HOH HOH A . 
D 3 HOH 283 685 685 HOH HOH A . 
D 3 HOH 284 686 686 HOH HOH A . 
D 3 HOH 285 687 687 HOH HOH A . 
D 3 HOH 286 688 688 HOH HOH A . 
D 3 HOH 287 689 689 HOH HOH A . 
D 3 HOH 288 690 690 HOH HOH A . 
D 3 HOH 289 691 691 HOH HOH A . 
D 3 HOH 290 692 692 HOH HOH A . 
D 3 HOH 291 693 693 HOH HOH A . 
D 3 HOH 292 694 694 HOH HOH A . 
D 3 HOH 293 695 695 HOH HOH A . 
D 3 HOH 294 696 696 HOH HOH A . 
D 3 HOH 295 697 697 HOH HOH A . 
D 3 HOH 296 698 698 HOH HOH A . 
D 3 HOH 297 699 699 HOH HOH A . 
D 3 HOH 298 700 700 HOH HOH A . 
D 3 HOH 299 701 701 HOH HOH A . 
D 3 HOH 300 702 702 HOH HOH A . 
D 3 HOH 301 703 703 HOH HOH A . 
D 3 HOH 302 704 704 HOH HOH A . 
D 3 HOH 303 705 705 HOH HOH A . 
D 3 HOH 304 706 706 HOH HOH A . 
D 3 HOH 305 707 707 HOH HOH A . 
D 3 HOH 306 708 708 HOH HOH A . 
D 3 HOH 307 709 709 HOH HOH A . 
D 3 HOH 308 710 710 HOH HOH A . 
D 3 HOH 309 711 711 HOH HOH A . 
D 3 HOH 310 712 712 HOH HOH A . 
D 3 HOH 311 713 713 HOH HOH A . 
D 3 HOH 312 714 714 HOH HOH A . 
D 3 HOH 313 715 715 HOH HOH A . 
D 3 HOH 314 716 716 HOH HOH A . 
D 3 HOH 315 717 717 HOH HOH A . 
D 3 HOH 316 718 718 HOH HOH A . 
D 3 HOH 317 719 719 HOH HOH A . 
D 3 HOH 318 720 720 HOH HOH A . 
D 3 HOH 319 721 721 HOH HOH A . 
D 3 HOH 320 722 722 HOH HOH A . 
D 3 HOH 321 723 723 HOH HOH A . 
D 3 HOH 322 724 724 HOH HOH A . 
D 3 HOH 323 725 725 HOH HOH A . 
D 3 HOH 324 726 726 HOH HOH A . 
D 3 HOH 325 727 727 HOH HOH A . 
D 3 HOH 326 728 728 HOH HOH A . 
D 3 HOH 327 729 729 HOH HOH A . 
D 3 HOH 328 730 730 HOH HOH A . 
D 3 HOH 329 731 731 HOH HOH A . 
D 3 HOH 330 732 732 HOH HOH A . 
D 3 HOH 331 733 733 HOH HOH A . 
D 3 HOH 332 734 734 HOH HOH A . 
D 3 HOH 333 735 735 HOH HOH A . 
D 3 HOH 334 736 736 HOH HOH A . 
D 3 HOH 335 737 737 HOH HOH A . 
D 3 HOH 336 738 738 HOH HOH A . 
D 3 HOH 337 739 739 HOH HOH A . 
D 3 HOH 338 740 740 HOH HOH A . 
D 3 HOH 339 741 741 HOH HOH A . 
D 3 HOH 340 742 742 HOH HOH A . 
D 3 HOH 341 743 743 HOH HOH A . 
D 3 HOH 342 744 744 HOH HOH A . 
D 3 HOH 343 745 745 HOH HOH A . 
D 3 HOH 344 746 746 HOH HOH A . 
D 3 HOH 345 747 747 HOH HOH A . 
D 3 HOH 346 748 748 HOH HOH A . 
D 3 HOH 347 749 749 HOH HOH A . 
D 3 HOH 348 750 750 HOH HOH A . 
D 3 HOH 349 751 751 HOH HOH A . 
D 3 HOH 350 752 752 HOH HOH A . 
D 3 HOH 351 753 753 HOH HOH A . 
D 3 HOH 352 754 754 HOH HOH A . 
D 3 HOH 353 755 755 HOH HOH A . 
D 3 HOH 354 756 756 HOH HOH A . 
D 3 HOH 355 757 757 HOH HOH A . 
D 3 HOH 356 758 758 HOH HOH A . 
D 3 HOH 357 759 759 HOH HOH A . 
D 3 HOH 358 760 760 HOH HOH A . 
D 3 HOH 359 761 761 HOH HOH A . 
D 3 HOH 360 762 762 HOH HOH A . 
D 3 HOH 361 763 763 HOH HOH A . 
D 3 HOH 362 764 764 HOH HOH A . 
D 3 HOH 363 765 765 HOH HOH A . 
D 3 HOH 364 766 766 HOH HOH A . 
D 3 HOH 365 767 767 HOH HOH A . 
D 3 HOH 366 768 768 HOH HOH A . 
D 3 HOH 367 769 769 HOH HOH A . 
D 3 HOH 368 770 770 HOH HOH A . 
D 3 HOH 369 771 771 HOH HOH A . 
D 3 HOH 370 773 773 HOH HOH A . 
D 3 HOH 371 774 774 HOH HOH A . 
D 3 HOH 372 775 775 HOH HOH A . 
D 3 HOH 373 776 776 HOH HOH A . 
D 3 HOH 374 777 777 HOH HOH A . 
D 3 HOH 375 778 778 HOH HOH A . 
D 3 HOH 376 779 779 HOH HOH A . 
D 3 HOH 377 780 780 HOH HOH A . 
D 3 HOH 378 781 781 HOH HOH A . 
D 3 HOH 379 782 782 HOH HOH A . 
D 3 HOH 380 783 783 HOH HOH A . 
D 3 HOH 381 784 784 HOH HOH A . 
D 3 HOH 382 785 785 HOH HOH A . 
D 3 HOH 383 786 786 HOH HOH A . 
D 3 HOH 384 787 787 HOH HOH A . 
D 3 HOH 385 788 788 HOH HOH A . 
D 3 HOH 386 789 789 HOH HOH A . 
D 3 HOH 387 790 790 HOH HOH A . 
D 3 HOH 388 791 791 HOH HOH A . 
D 3 HOH 389 792 792 HOH HOH A . 
D 3 HOH 390 793 793 HOH HOH A . 
D 3 HOH 391 794 794 HOH HOH A . 
D 3 HOH 392 795 795 HOH HOH A . 
D 3 HOH 393 796 796 HOH HOH A . 
D 3 HOH 394 797 797 HOH HOH A . 
D 3 HOH 395 798 798 HOH HOH A . 
D 3 HOH 396 799 799 HOH HOH A . 
D 3 HOH 397 800 800 HOH HOH A . 
D 3 HOH 398 801 801 HOH HOH A . 
D 3 HOH 399 802 802 HOH HOH A . 
D 3 HOH 400 803 803 HOH HOH A . 
D 3 HOH 401 804 804 HOH HOH A . 
D 3 HOH 402 805 805 HOH HOH A . 
D 3 HOH 403 806 806 HOH HOH A . 
D 3 HOH 404 807 807 HOH HOH A . 
D 3 HOH 405 809 809 HOH HOH A . 
D 3 HOH 406 810 810 HOH HOH A . 
D 3 HOH 407 811 811 HOH HOH A . 
D 3 HOH 408 812 812 HOH HOH A . 
D 3 HOH 409 813 813 HOH HOH A . 
D 3 HOH 410 814 814 HOH HOH A . 
D 3 HOH 411 815 815 HOH HOH A . 
D 3 HOH 412 816 816 HOH HOH A . 
D 3 HOH 413 817 817 HOH HOH A . 
D 3 HOH 414 818 818 HOH HOH A . 
D 3 HOH 415 819 819 HOH HOH A . 
D 3 HOH 416 820 820 HOH HOH A . 
D 3 HOH 417 821 821 HOH HOH A . 
D 3 HOH 418 822 822 HOH HOH A . 
D 3 HOH 419 823 823 HOH HOH A . 
D 3 HOH 420 824 824 HOH HOH A . 
D 3 HOH 421 825 825 HOH HOH A . 
D 3 HOH 422 826 826 HOH HOH A . 
D 3 HOH 423 827 827 HOH HOH A . 
D 3 HOH 424 828 828 HOH HOH A . 
D 3 HOH 425 829 829 HOH HOH A . 
D 3 HOH 426 830 830 HOH HOH A . 
D 3 HOH 427 831 831 HOH HOH A . 
D 3 HOH 428 832 832 HOH HOH A . 
D 3 HOH 429 833 833 HOH HOH A . 
D 3 HOH 430 834 834 HOH HOH A . 
D 3 HOH 431 835 835 HOH HOH A . 
D 3 HOH 432 836 836 HOH HOH A . 
D 3 HOH 433 837 837 HOH HOH A . 
D 3 HOH 434 838 838 HOH HOH A . 
D 3 HOH 435 839 839 HOH HOH A . 
D 3 HOH 436 840 840 HOH HOH A . 
D 3 HOH 437 841 841 HOH HOH A . 
D 3 HOH 438 842 842 HOH HOH A . 
D 3 HOH 439 843 843 HOH HOH A . 
D 3 HOH 440 844 844 HOH HOH A . 
D 3 HOH 441 845 845 HOH HOH A . 
D 3 HOH 442 846 846 HOH HOH A . 
D 3 HOH 443 847 847 HOH HOH A . 
D 3 HOH 444 848 848 HOH HOH A . 
D 3 HOH 445 849 849 HOH HOH A . 
D 3 HOH 446 850 850 HOH HOH A . 
D 3 HOH 447 851 851 HOH HOH A . 
D 3 HOH 448 852 852 HOH HOH A . 
D 3 HOH 449 853 853 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A HIS 231 ? CG  ? A HIS 228 CG  
2 1 Y 1 A HIS 231 ? ND1 ? A HIS 228 ND1 
3 1 Y 1 A HIS 231 ? CD2 ? A HIS 228 CD2 
4 1 Y 1 A HIS 231 ? CE1 ? A HIS 228 CE1 
5 1 Y 1 A HIS 231 ? NE2 ? A HIS 228 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.19.2_4158 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
# 
_cell.volume             213767.321 
_cell.length_a           50.498 
_cell.length_b           62.452 
_cell.length_c           67.783 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           8ZUQ 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.entry_id                         8ZUQ 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZUQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.49 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 4000, magnesium chloride, MES-NaOH buffer (pH 5.0)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            308 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     15 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.70 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL41XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.70 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL41XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          11.51 
_reflns.entry_id                                       8ZUQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.48 
_reflns.d_resolution_low                               45.93 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     36411 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.70 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.34 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.174 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.160 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.48 
_reflns_shell.d_res_low                                     1.57 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.98 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5803 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.97 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.847 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.807 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.784 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.pdbx_overall_phase_error                 18.2182 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_R_factor_obs                          0.1578 
_refine.B_iso_mean                               17.08 
_refine.ls_number_reflns_R_free                  1819 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_R_factor_R_work                       0.1560 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.48 
_refine.ls_number_reflns_obs                     36405 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.ls_number_reflns_R_work                  34586 
_refine.ls_d_res_low                             45.93 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1931 
_refine.overall_SU_ML                            0.1484 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.entry_id                                 8ZUQ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_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        1819 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             449 
_refine_hist.number_atoms_total               2270 
_refine_hist.d_res_high                       1.48 
_refine_hist.d_res_low                        45.93 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           2141 0.0054  ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2938 0.8351  ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     319  0.0836  ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      387  0.0071  ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 847  12.9406 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' 1.48 1.52  2604 0.2184 99.96  0.2542 150 . . . . . . . 
'X-RAY DIFFRACTION' 1.52 1.56  2603 0.2116 99.93  0.2683 143 . . . . . . . 
'X-RAY DIFFRACTION' 1.56 1.62  2611 0.2051 100.00 0.2448 142 . . . . . . . 
'X-RAY DIFFRACTION' 1.62 1.67  2631 0.1988 99.96  0.2631 143 . . . . . . . 
'X-RAY DIFFRACTION' 1.67 1.74  2622 0.1937 99.96  0.2262 149 . . . . . . . 
'X-RAY DIFFRACTION' 1.74 1.82  2639 0.1855 100.00 0.2194 136 . . . . . . . 
'X-RAY DIFFRACTION' 1.82 1.92  2627 0.1649 100.00 0.2050 147 . . . . . . . 
'X-RAY DIFFRACTION' 1.92 2.04  2660 0.1549 100.00 0.1979 116 . . . . . . . 
'X-RAY DIFFRACTION' 2.04 2.19  2685 0.1527 100.00 0.1771 127 . . . . . . . 
'X-RAY DIFFRACTION' 2.19 2.41  2659 0.1498 100.00 0.1818 143 . . . . . . . 
'X-RAY DIFFRACTION' 2.41 2.76  2707 0.1479 99.93  0.1868 118 . . . . . . . 
'X-RAY DIFFRACTION' 2.76 3.48  2704 0.1304 100.00 0.1510 155 . . . . . . . 
'X-RAY DIFFRACTION' 3.48 45.93 2834 0.1322 99.77  0.1778 150 . . . . . . . 
# 
_struct.entry_id                     8ZUQ 
_struct.title                        'Crystal structure of the F99S/M153T/V163A/T203I/E222Q variant of GFP at pH 8.5' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8ZUQ 
_struct_keywords.text            'GREEN FLUORESCENT PROTEIN, FLUORESCENT PROTEIN' 
_struct_keywords.pdbx_keywords   'FLUORESCENT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    GFP_AEQVI 
_struct_ref.pdbx_db_accession          P42212 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKQH
DFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGI
KVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITH
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZUQ 
_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                 228 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P42212 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  231 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       231 
# 
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 8ZUQ GYS A 64  ? UNP P42212 SER 65  chromophore           66  1 
1 8ZUQ GYS A 64  ? UNP P42212 TYR 66  chromophore           66  2 
1 8ZUQ GYS A 64  ? UNP P42212 GLY 67  chromophore           66  3 
1 8ZUQ ARG A 77  ? UNP P42212 GLN 80  conflict              80  4 
1 8ZUQ SER A 96  ? UNP P42212 PHE 99  'engineered mutation' 99  5 
1 8ZUQ THR A 150 ? UNP P42212 MET 153 'engineered mutation' 153 6 
1 8ZUQ ALA A 160 ? UNP P42212 VAL 163 'engineered mutation' 163 7 
1 8ZUQ ILE A 200 ? UNP P42212 THR 203 'engineered mutation' 203 8 
1 8ZUQ GLN A 219 ? UNP P42212 GLU 222 'engineered mutation' 222 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 90    ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  10280 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 3   ? THR A 8   ? GLY A 4   THR A 9   5 ? 6 
HELX_P HELX_P2 AA2 ALA A 36  ? TYR A 38  ? ALA A 37  TYR A 39  5 ? 3 
HELX_P HELX_P3 AA3 PRO A 55  ? VAL A 60  ? PRO A 56  VAL A 61  5 ? 6 
HELX_P HELX_P4 AA4 VAL A 65  ? SER A 69  ? VAL A 68  SER A 72  5 ? 5 
HELX_P HELX_P5 AA5 PRO A 72  ? HIS A 78  ? PRO A 75  HIS A 81  5 ? 7 
HELX_P HELX_P6 AA6 ASP A 79  ? ALA A 84  ? ASP A 82  ALA A 87  1 ? 6 
HELX_P HELX_P7 AA7 LYS A 153 ? ASN A 156 ? LYS A 156 ASN A 159 5 ? 4 
# 
_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 
covale1  covale both ? A PHE 63  C   ? ? ? 1_555 A GYS 64 N1 ? ? A PHE 64  A GYS 66  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale2  covale both ? A GYS 64  C3  ? ? ? 1_555 A VAL 65 N  ? ? A GYS 66  A VAL 68  1_555 ? ? ? ? ? ? ? 1.327 ? ? 
metalc1  metalc ?    ? A ASN 167 OD1 B ? ? 1_555 B MG  .  MG ? ? A ASN 170 A MG  301 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc2  metalc ?    ? B MG  .   MG  ? ? ? 1_555 D HOH .  O  A ? A MG  301 A HOH 487 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc3  metalc ?    ? B MG  .   MG  ? ? ? 1_555 D HOH .  O  B ? A MG  301 A HOH 487 1_555 ? ? ? ? ? ? ? 2.567 ? ? 
metalc4  metalc ?    ? B MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  301 A HOH 488 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc5  metalc ?    ? B MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  301 A HOH 505 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc6  metalc ?    ? B MG  .   MG  ? ? ? 1_555 D HOH .  O  A ? A MG  301 A HOH 522 1_555 ? ? ? ? ? ? ? 1.978 ? ? 
metalc7  metalc ?    ? B MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  301 A HOH 550 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc8  metalc ?    ? B MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  301 A HOH 562 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc9  metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  302 A HOH 640 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc10 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH .  O  A ? A MG  302 A HOH 679 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc11 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH .  O  B ? A MG  302 A HOH 679 1_555 ? ? ? ? ? ? ? 2.132 ? ? 
metalc12 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  302 A HOH 693 1_555 ? ? ? ? ? ? ? 2.177 ? ? 
metalc13 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  302 A HOH 735 1_555 ? ? ? ? ? ? ? 1.964 ? ? 
metalc14 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  302 A HOH 752 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc15 metalc ?    ? C MG  .   MG  ? ? ? 1_555 D HOH .  O  ? ? A MG  302 A HOH 769 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
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  OD1 B A ASN 167 ? A ASN 170 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 487 ? 1_555 48.0  ? 
2  OD1 B A ASN 167 ? A ASN 170 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 487 ? 1_555 85.8  ? 
3  O   A D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 487 ? 1_555 44.6  ? 
4  OD1 B A ASN 167 ? A ASN 170 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 488 ? 1_555 65.3  ? 
5  O   A D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 488 ? 1_555 105.7 ? 
6  O   B D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 488 ? 1_555 113.3 ? 
7  OD1 B A ASN 167 ? A ASN 170 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 505 ? 1_555 66.6  ? 
8  O   A D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 505 ? 1_555 83.4  ? 
9  O   B D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 505 ? 1_555 123.4 ? 
10 O   ? D HOH .   ? A HOH 488 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 505 ? 1_555 99.0  ? 
11 OD1 B A ASN 167 ? A ASN 170 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 522 ? 1_555 113.8 ? 
12 O   A D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 522 ? 1_555 96.4  ? 
13 O   B D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 522 ? 1_555 56.1  ? 
14 O   ? D HOH .   ? A HOH 488 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 522 ? 1_555 81.9  ? 
15 O   ? D HOH .   ? A HOH 505 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 522 ? 1_555 179.1 ? 
16 OD1 B A ASN 167 ? A ASN 170 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 550 ? 1_555 128.3 ? 
17 O   A D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 550 ? 1_555 167.3 ? 
18 O   B D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 550 ? 1_555 144.5 ? 
19 O   ? D HOH .   ? A HOH 488 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 550 ? 1_555 79.3  ? 
20 O   ? D HOH .   ? A HOH 505 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 550 ? 1_555 84.3  ? 
21 O   A D HOH .   ? A HOH 522 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 550 ? 1_555 95.9  ? 
22 OD1 B A ASN 167 ? A ASN 170 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 562 ? 1_555 128.8 ? 
23 O   A D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 562 ? 1_555 84.2  ? 
24 O   B D HOH .   ? A HOH 487 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 562 ? 1_555 64.8  ? 
25 O   ? D HOH .   ? A HOH 488 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 562 ? 1_555 163.9 ? 
26 O   ? D HOH .   ? A HOH 505 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 562 ? 1_555 94.7  ? 
27 O   A D HOH .   ? A HOH 522 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 562 ? 1_555 84.5  ? 
28 O   ? D HOH .   ? A HOH 550 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 562 ? 1_555 93.8  ? 
29 O   ? D HOH .   ? A HOH 640 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 679 ? 1_555 91.0  ? 
30 O   ? D HOH .   ? A HOH 640 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 679 ? 1_555 96.8  ? 
31 O   A D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 679 ? 1_555 40.6  ? 
32 O   ? D HOH .   ? A HOH 640 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 693 ? 1_555 87.0  ? 
33 O   A D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 693 ? 1_555 117.7 ? 
34 O   B D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 693 ? 1_555 77.8  ? 
35 O   ? D HOH .   ? A HOH 640 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 735 ? 1_555 95.9  ? 
36 O   A D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 735 ? 1_555 69.9  ? 
37 O   B D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 735 ? 1_555 109.2 ? 
38 O   ? D HOH .   ? A HOH 693 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 735 ? 1_555 172.0 ? 
39 O   ? D HOH .   ? A HOH 640 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 752 ? 1_555 87.3  ? 
40 O   A D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 752 ? 1_555 153.9 ? 
41 O   B D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 752 ? 1_555 165.2 ? 
42 O   ? D HOH .   ? A HOH 693 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 752 ? 1_555 88.3  ? 
43 O   ? D HOH .   ? A HOH 735 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 752 ? 1_555 84.4  ? 
44 O   ? D HOH .   ? A HOH 640 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 769 ? 1_555 172.4 ? 
45 O   A D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 769 ? 1_555 91.8  ? 
46 O   B D HOH .   ? A HOH 679 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 769 ? 1_555 80.7  ? 
47 O   ? D HOH .   ? A HOH 693 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 769 ? 1_555 85.4  ? 
48 O   ? D HOH .   ? A HOH 735 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 769 ? 1_555 91.8  ? 
49 O   ? D HOH .   ? A HOH 752 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 769 ? 1_555 93.3  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      GYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       64 
_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                       GYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        66 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_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                'SER, TYR, GLY' 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        GYS 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           Chromophore/chromophore-like 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          MET 
_struct_mon_prot_cis.label_seq_id           85 
_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           MET 
_struct_mon_prot_cis.auth_seq_id            88 
_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    86 
_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     89 
_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       8.02 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   12 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? 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 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? 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  VAL A 11  ? VAL A 21  ? VAL A 12  VAL A 22  
AA1 2  HIS A 24  ? ASP A 35  ? HIS A 25  ASP A 36  
AA1 3  LYS A 40  ? CYS A 47  ? LYS A 41  CYS A 48  
AA1 4  HIS A 214 ? ALA A 224 ? HIS A 217 ALA A 227 
AA1 5  HIS A 196 ? SER A 205 ? HIS A 199 SER A 208 
AA1 6  HIS A 145 ? ASP A 152 ? HIS A 148 ASP A 155 
AA1 7  GLY A 157 ? ASN A 167 ? GLY A 160 ASN A 170 
AA1 8  VAL A 173 ? PRO A 184 ? VAL A 176 PRO A 187 
AA1 9  TYR A 89  ? PHE A 97  ? TYR A 92  PHE A 100 
AA1 10 ASN A 102 ? GLU A 112 ? ASN A 105 GLU A 115 
AA1 11 THR A 115 ? ILE A 125 ? THR A 118 ILE A 128 
AA1 12 VAL A 11  ? VAL A 21  ? VAL A 12  VAL A 22  
# 
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 VAL A 15  ? N VAL A 16  O GLY A 30  ? O GLY A 31  
AA1 2  3  N ASP A 35  ? N ASP A 36  O LYS A 40  ? O LYS A 41  
AA1 3  4  N LEU A 43  ? N LEU A 44  O LEU A 217 ? O LEU A 220 
AA1 4  5  O ALA A 224 ? O ALA A 227 N TYR A 197 ? N TYR A 200 
AA1 5  6  O HIS A 196 ? O HIS A 199 N ILE A 149 ? N ILE A 152 
AA1 6  7  N ASP A 152 ? N ASP A 155 O GLY A 157 ? O GLY A 160 
AA1 7  8  N HIS A 166 ? N HIS A 169 O GLN A 174 ? O GLN A 177 
AA1 8  9  O THR A 183 ? O THR A 186 N VAL A 90  ? N VAL A 93  
AA1 9  10 N ILE A 95  ? N ILE A 98  O TYR A 103 ? O TYR A 106 
AA1 10 11 N LYS A 110 ? N LYS A 113 O VAL A 117 ? O VAL A 120 
AA1 11 12 O GLY A 124 ? O GLY A 127 N ASP A 20  ? N ASP A 21  
# 
_pdbx_entry_details.entry_id                   8ZUQ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 103 ? ? -149.83 -159.14 
2 1 ALA A 227 ? B -139.48 -130.21 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A GYS 64 A GYS 66 ? SER chromophore 
2 A GYS 64 A GYS 66 ? TYR chromophore 
3 A GYS 64 A GYS 66 ? GLY chromophore 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 494 ? 7.74 . 
2 1 O ? A HOH 564 ? 6.55 . 
3 1 O ? A HOH 623 ? 6.75 . 
4 1 O ? A HOH 666 ? 8.34 . 
5 1 O ? A HOH 674 ? 5.85 . 
6 1 O ? A HOH 753 ? 6.22 . 
7 1 O ? A HOH 777 ? 6.30 . 
8 1 O ? A HOH 837 ? 7.03 . 
9 1 O ? A HOH 839 ? 6.28 . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
GYS N1   N  N N 137 
GYS OG1  O  N N 138 
GYS CB1  C  N N 139 
GYS CA1  C  N R 140 
GYS C1   C  N N 141 
GYS N2   N  N N 142 
GYS N3   N  N N 143 
GYS C2   C  N N 144 
GYS O2   O  N N 145 
GYS CA2  C  N N 146 
GYS CA3  C  N N 147 
GYS CB2  C  N N 148 
GYS CG2  C  Y N 149 
GYS CD1  C  Y N 150 
GYS CD2  C  Y N 151 
GYS CE1  C  Y N 152 
GYS CE2  C  Y N 153 
GYS CZ   C  Y N 154 
GYS OH   O  N N 155 
GYS C3   C  N N 156 
GYS O3   O  N N 157 
GYS OXT  O  N N 158 
GYS H    H  N N 159 
GYS H2   H  N N 160 
GYS HA1  H  N N 161 
GYS HB11 H  N N 162 
GYS HB12 H  N N 163 
GYS HG1  H  N N 164 
GYS HB2  H  N N 165 
GYS HD2  H  N N 166 
GYS HE2  H  N N 167 
GYS HOH  H  N N 168 
GYS HE1  H  N N 169 
GYS HD1  H  N N 170 
GYS HA31 H  N N 171 
GYS HA32 H  N N 172 
GYS HXT  H  N N 173 
HIS N    N  N N 174 
HIS CA   C  N S 175 
HIS C    C  N N 176 
HIS O    O  N N 177 
HIS CB   C  N N 178 
HIS CG   C  Y N 179 
HIS ND1  N  Y N 180 
HIS CD2  C  Y N 181 
HIS CE1  C  Y N 182 
HIS NE2  N  Y N 183 
HIS OXT  O  N N 184 
HIS H    H  N N 185 
HIS H2   H  N N 186 
HIS HA   H  N N 187 
HIS HB2  H  N N 188 
HIS HB3  H  N N 189 
HIS HD1  H  N N 190 
HIS HD2  H  N N 191 
HIS HE1  H  N N 192 
HIS HE2  H  N N 193 
HIS HXT  H  N N 194 
HOH O    O  N N 195 
HOH H1   H  N N 196 
HOH H2   H  N N 197 
ILE N    N  N N 198 
ILE CA   C  N S 199 
ILE C    C  N N 200 
ILE O    O  N N 201 
ILE CB   C  N S 202 
ILE CG1  C  N N 203 
ILE CG2  C  N N 204 
ILE CD1  C  N N 205 
ILE OXT  O  N N 206 
ILE H    H  N N 207 
ILE H2   H  N N 208 
ILE HA   H  N N 209 
ILE HB   H  N N 210 
ILE HG12 H  N N 211 
ILE HG13 H  N N 212 
ILE HG21 H  N N 213 
ILE HG22 H  N N 214 
ILE HG23 H  N N 215 
ILE HD11 H  N N 216 
ILE HD12 H  N N 217 
ILE HD13 H  N N 218 
ILE HXT  H  N N 219 
LEU N    N  N N 220 
LEU CA   C  N S 221 
LEU C    C  N N 222 
LEU O    O  N N 223 
LEU CB   C  N N 224 
LEU CG   C  N N 225 
LEU CD1  C  N N 226 
LEU CD2  C  N N 227 
LEU OXT  O  N N 228 
LEU H    H  N N 229 
LEU H2   H  N N 230 
LEU HA   H  N N 231 
LEU HB2  H  N N 232 
LEU HB3  H  N N 233 
LEU HG   H  N N 234 
LEU HD11 H  N N 235 
LEU HD12 H  N N 236 
LEU HD13 H  N N 237 
LEU HD21 H  N N 238 
LEU HD22 H  N N 239 
LEU HD23 H  N N 240 
LEU HXT  H  N N 241 
LYS N    N  N N 242 
LYS CA   C  N S 243 
LYS C    C  N N 244 
LYS O    O  N N 245 
LYS CB   C  N N 246 
LYS CG   C  N N 247 
LYS CD   C  N N 248 
LYS CE   C  N N 249 
LYS NZ   N  N N 250 
LYS OXT  O  N N 251 
LYS H    H  N N 252 
LYS H2   H  N N 253 
LYS HA   H  N N 254 
LYS HB2  H  N N 255 
LYS HB3  H  N N 256 
LYS HG2  H  N N 257 
LYS HG3  H  N N 258 
LYS HD2  H  N N 259 
LYS HD3  H  N N 260 
LYS HE2  H  N N 261 
LYS HE3  H  N N 262 
LYS HZ1  H  N N 263 
LYS HZ2  H  N N 264 
LYS HZ3  H  N N 265 
LYS HXT  H  N N 266 
MET N    N  N N 267 
MET CA   C  N S 268 
MET C    C  N N 269 
MET O    O  N N 270 
MET CB   C  N N 271 
MET CG   C  N N 272 
MET SD   S  N N 273 
MET CE   C  N N 274 
MET OXT  O  N N 275 
MET H    H  N N 276 
MET H2   H  N N 277 
MET HA   H  N N 278 
MET HB2  H  N N 279 
MET HB3  H  N N 280 
MET HG2  H  N N 281 
MET HG3  H  N N 282 
MET HE1  H  N N 283 
MET HE2  H  N N 284 
MET HE3  H  N N 285 
MET HXT  H  N N 286 
MG  MG   MG N N 287 
PHE N    N  N N 288 
PHE CA   C  N S 289 
PHE C    C  N N 290 
PHE O    O  N N 291 
PHE CB   C  N N 292 
PHE CG   C  Y N 293 
PHE CD1  C  Y N 294 
PHE CD2  C  Y N 295 
PHE CE1  C  Y N 296 
PHE CE2  C  Y N 297 
PHE CZ   C  Y N 298 
PHE OXT  O  N N 299 
PHE H    H  N N 300 
PHE H2   H  N N 301 
PHE HA   H  N N 302 
PHE HB2  H  N N 303 
PHE HB3  H  N N 304 
PHE HD1  H  N N 305 
PHE HD2  H  N N 306 
PHE HE1  H  N N 307 
PHE HE2  H  N N 308 
PHE HZ   H  N N 309 
PHE HXT  H  N N 310 
PRO N    N  N N 311 
PRO CA   C  N S 312 
PRO C    C  N N 313 
PRO O    O  N N 314 
PRO CB   C  N N 315 
PRO CG   C  N N 316 
PRO CD   C  N N 317 
PRO OXT  O  N N 318 
PRO H    H  N N 319 
PRO HA   H  N N 320 
PRO HB2  H  N N 321 
PRO HB3  H  N N 322 
PRO HG2  H  N N 323 
PRO HG3  H  N N 324 
PRO HD2  H  N N 325 
PRO HD3  H  N N 326 
PRO HXT  H  N N 327 
SER N    N  N N 328 
SER CA   C  N S 329 
SER C    C  N N 330 
SER O    O  N N 331 
SER CB   C  N N 332 
SER OG   O  N N 333 
SER OXT  O  N N 334 
SER H    H  N N 335 
SER H2   H  N N 336 
SER HA   H  N N 337 
SER HB2  H  N N 338 
SER HB3  H  N N 339 
SER HG   H  N N 340 
SER HXT  H  N N 341 
THR N    N  N N 342 
THR CA   C  N S 343 
THR C    C  N N 344 
THR O    O  N N 345 
THR CB   C  N R 346 
THR OG1  O  N N 347 
THR CG2  C  N N 348 
THR OXT  O  N N 349 
THR H    H  N N 350 
THR H2   H  N N 351 
THR HA   H  N N 352 
THR HB   H  N N 353 
THR HG1  H  N N 354 
THR HG21 H  N N 355 
THR HG22 H  N N 356 
THR HG23 H  N N 357 
THR HXT  H  N N 358 
TRP N    N  N N 359 
TRP CA   C  N S 360 
TRP C    C  N N 361 
TRP O    O  N N 362 
TRP CB   C  N N 363 
TRP CG   C  Y N 364 
TRP CD1  C  Y N 365 
TRP CD2  C  Y N 366 
TRP NE1  N  Y N 367 
TRP CE2  C  Y N 368 
TRP CE3  C  Y N 369 
TRP CZ2  C  Y N 370 
TRP CZ3  C  Y N 371 
TRP CH2  C  Y N 372 
TRP OXT  O  N N 373 
TRP H    H  N N 374 
TRP H2   H  N N 375 
TRP HA   H  N N 376 
TRP HB2  H  N N 377 
TRP HB3  H  N N 378 
TRP HD1  H  N N 379 
TRP HE1  H  N N 380 
TRP HE3  H  N N 381 
TRP HZ2  H  N N 382 
TRP HZ3  H  N N 383 
TRP HH2  H  N N 384 
TRP HXT  H  N N 385 
TYR N    N  N N 386 
TYR CA   C  N S 387 
TYR C    C  N N 388 
TYR O    O  N N 389 
TYR CB   C  N N 390 
TYR CG   C  Y N 391 
TYR CD1  C  Y N 392 
TYR CD2  C  Y N 393 
TYR CE1  C  Y N 394 
TYR CE2  C  Y N 395 
TYR CZ   C  Y N 396 
TYR OH   O  N N 397 
TYR OXT  O  N N 398 
TYR H    H  N N 399 
TYR H2   H  N N 400 
TYR HA   H  N N 401 
TYR HB2  H  N N 402 
TYR HB3  H  N N 403 
TYR HD1  H  N N 404 
TYR HD2  H  N N 405 
TYR HE1  H  N N 406 
TYR HE2  H  N N 407 
TYR HH   H  N N 408 
TYR HXT  H  N N 409 
VAL N    N  N N 410 
VAL CA   C  N S 411 
VAL C    C  N N 412 
VAL O    O  N N 413 
VAL CB   C  N N 414 
VAL CG1  C  N N 415 
VAL CG2  C  N N 416 
VAL OXT  O  N N 417 
VAL H    H  N N 418 
VAL H2   H  N N 419 
VAL HA   H  N N 420 
VAL HB   H  N N 421 
VAL HG11 H  N N 422 
VAL HG12 H  N N 423 
VAL HG13 H  N N 424 
VAL HG21 H  N N 425 
VAL HG22 H  N N 426 
VAL HG23 H  N N 427 
VAL HXT  H  N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GYS N1  CA1  sing N N 129 
GYS N1  H    sing N N 130 
GYS N1  H2   sing N N 131 
GYS OG1 CB1  sing N N 132 
GYS OG1 HG1  sing N N 133 
GYS CB1 CA1  sing N N 134 
GYS CB1 HB11 sing N N 135 
GYS CB1 HB12 sing N N 136 
GYS CA1 C1   sing N N 137 
GYS CA1 HA1  sing N N 138 
GYS C1  N2   doub N N 139 
GYS C1  N3   sing N N 140 
GYS N2  CA2  sing N N 141 
GYS N3  C2   sing N N 142 
GYS N3  CA3  sing N N 143 
GYS C2  CA2  sing N N 144 
GYS C2  O2   doub N N 145 
GYS CA2 CB2  doub N Z 146 
GYS CA3 C3   sing N N 147 
GYS CA3 HA31 sing N N 148 
GYS CA3 HA32 sing N N 149 
GYS CB2 CG2  sing N N 150 
GYS CB2 HB2  sing N N 151 
GYS CG2 CD2  doub Y N 152 
GYS CG2 CD1  sing Y N 153 
GYS CD1 CE1  doub Y N 154 
GYS CD1 HD1  sing N N 155 
GYS CD2 CE2  sing Y N 156 
GYS CD2 HD2  sing N N 157 
GYS CE1 CZ   sing Y N 158 
GYS CE1 HE1  sing N N 159 
GYS CE2 CZ   doub Y N 160 
GYS CE2 HE2  sing N N 161 
GYS CZ  OH   sing N N 162 
GYS OH  HOH  sing N N 163 
GYS C3  O3   doub N N 164 
GYS C3  OXT  sing N N 165 
GYS OXT HXT  sing N N 166 
HIS N   CA   sing N N 167 
HIS N   H    sing N N 168 
HIS N   H2   sing N N 169 
HIS CA  C    sing N N 170 
HIS CA  CB   sing N N 171 
HIS CA  HA   sing N N 172 
HIS C   O    doub N N 173 
HIS C   OXT  sing N N 174 
HIS CB  CG   sing N N 175 
HIS CB  HB2  sing N N 176 
HIS CB  HB3  sing N N 177 
HIS CG  ND1  sing Y N 178 
HIS CG  CD2  doub Y N 179 
HIS ND1 CE1  doub Y N 180 
HIS ND1 HD1  sing N N 181 
HIS CD2 NE2  sing Y N 182 
HIS CD2 HD2  sing N N 183 
HIS CE1 NE2  sing Y N 184 
HIS CE1 HE1  sing N N 185 
HIS NE2 HE2  sing N N 186 
HIS OXT HXT  sing N N 187 
HOH O   H1   sing N N 188 
HOH O   H2   sing N N 189 
ILE N   CA   sing N N 190 
ILE N   H    sing N N 191 
ILE N   H2   sing N N 192 
ILE CA  C    sing N N 193 
ILE CA  CB   sing N N 194 
ILE CA  HA   sing N N 195 
ILE C   O    doub N N 196 
ILE C   OXT  sing N N 197 
ILE CB  CG1  sing N N 198 
ILE CB  CG2  sing N N 199 
ILE CB  HB   sing N N 200 
ILE CG1 CD1  sing N N 201 
ILE CG1 HG12 sing N N 202 
ILE CG1 HG13 sing N N 203 
ILE CG2 HG21 sing N N 204 
ILE CG2 HG22 sing N N 205 
ILE CG2 HG23 sing N N 206 
ILE CD1 HD11 sing N N 207 
ILE CD1 HD12 sing N N 208 
ILE CD1 HD13 sing N N 209 
ILE OXT HXT  sing N N 210 
LEU N   CA   sing N N 211 
LEU N   H    sing N N 212 
LEU N   H2   sing N N 213 
LEU CA  C    sing N N 214 
LEU CA  CB   sing N N 215 
LEU CA  HA   sing N N 216 
LEU C   O    doub N N 217 
LEU C   OXT  sing N N 218 
LEU CB  CG   sing N N 219 
LEU CB  HB2  sing N N 220 
LEU CB  HB3  sing N N 221 
LEU CG  CD1  sing N N 222 
LEU CG  CD2  sing N N 223 
LEU CG  HG   sing N N 224 
LEU CD1 HD11 sing N N 225 
LEU CD1 HD12 sing N N 226 
LEU CD1 HD13 sing N N 227 
LEU CD2 HD21 sing N N 228 
LEU CD2 HD22 sing N N 229 
LEU CD2 HD23 sing N N 230 
LEU OXT HXT  sing N N 231 
LYS N   CA   sing N N 232 
LYS N   H    sing N N 233 
LYS N   H2   sing N N 234 
LYS CA  C    sing N N 235 
LYS CA  CB   sing N N 236 
LYS CA  HA   sing N N 237 
LYS C   O    doub N N 238 
LYS C   OXT  sing N N 239 
LYS CB  CG   sing N N 240 
LYS CB  HB2  sing N N 241 
LYS CB  HB3  sing N N 242 
LYS CG  CD   sing N N 243 
LYS CG  HG2  sing N N 244 
LYS CG  HG3  sing N N 245 
LYS CD  CE   sing N N 246 
LYS CD  HD2  sing N N 247 
LYS CD  HD3  sing N N 248 
LYS CE  NZ   sing N N 249 
LYS CE  HE2  sing N N 250 
LYS CE  HE3  sing N N 251 
LYS NZ  HZ1  sing N N 252 
LYS NZ  HZ2  sing N N 253 
LYS NZ  HZ3  sing N N 254 
LYS OXT HXT  sing N N 255 
MET N   CA   sing N N 256 
MET N   H    sing N N 257 
MET N   H2   sing N N 258 
MET CA  C    sing N N 259 
MET CA  CB   sing N N 260 
MET CA  HA   sing N N 261 
MET C   O    doub N N 262 
MET C   OXT  sing N N 263 
MET CB  CG   sing N N 264 
MET CB  HB2  sing N N 265 
MET CB  HB3  sing N N 266 
MET CG  SD   sing N N 267 
MET CG  HG2  sing N N 268 
MET CG  HG3  sing N N 269 
MET SD  CE   sing N N 270 
MET CE  HE1  sing N N 271 
MET CE  HE2  sing N N 272 
MET CE  HE3  sing N N 273 
MET OXT HXT  sing N N 274 
PHE N   CA   sing N N 275 
PHE N   H    sing N N 276 
PHE N   H2   sing N N 277 
PHE CA  C    sing N N 278 
PHE CA  CB   sing N N 279 
PHE CA  HA   sing N N 280 
PHE C   O    doub N N 281 
PHE C   OXT  sing N N 282 
PHE CB  CG   sing N N 283 
PHE CB  HB2  sing N N 284 
PHE CB  HB3  sing N N 285 
PHE CG  CD1  doub Y N 286 
PHE CG  CD2  sing Y N 287 
PHE CD1 CE1  sing Y N 288 
PHE CD1 HD1  sing N N 289 
PHE CD2 CE2  doub Y N 290 
PHE CD2 HD2  sing N N 291 
PHE CE1 CZ   doub Y N 292 
PHE CE1 HE1  sing N N 293 
PHE CE2 CZ   sing Y N 294 
PHE CE2 HE2  sing N N 295 
PHE CZ  HZ   sing N N 296 
PHE OXT HXT  sing N N 297 
PRO N   CA   sing N N 298 
PRO N   CD   sing N N 299 
PRO N   H    sing N N 300 
PRO CA  C    sing N N 301 
PRO CA  CB   sing N N 302 
PRO CA  HA   sing N N 303 
PRO C   O    doub N N 304 
PRO C   OXT  sing N N 305 
PRO CB  CG   sing N N 306 
PRO CB  HB2  sing N N 307 
PRO CB  HB3  sing N N 308 
PRO CG  CD   sing N N 309 
PRO CG  HG2  sing N N 310 
PRO CG  HG3  sing N N 311 
PRO CD  HD2  sing N N 312 
PRO CD  HD3  sing N N 313 
PRO OXT HXT  sing N N 314 
SER N   CA   sing N N 315 
SER N   H    sing N N 316 
SER N   H2   sing N N 317 
SER CA  C    sing N N 318 
SER CA  CB   sing N N 319 
SER CA  HA   sing N N 320 
SER C   O    doub N N 321 
SER C   OXT  sing N N 322 
SER CB  OG   sing N N 323 
SER CB  HB2  sing N N 324 
SER CB  HB3  sing N N 325 
SER OG  HG   sing N N 326 
SER OXT HXT  sing N N 327 
THR N   CA   sing N N 328 
THR N   H    sing N N 329 
THR N   H2   sing N N 330 
THR CA  C    sing N N 331 
THR CA  CB   sing N N 332 
THR CA  HA   sing N N 333 
THR C   O    doub N N 334 
THR C   OXT  sing N N 335 
THR CB  OG1  sing N N 336 
THR CB  CG2  sing N N 337 
THR CB  HB   sing N N 338 
THR OG1 HG1  sing N N 339 
THR CG2 HG21 sing N N 340 
THR CG2 HG22 sing N N 341 
THR CG2 HG23 sing N N 342 
THR OXT HXT  sing N N 343 
TRP N   CA   sing N N 344 
TRP N   H    sing N N 345 
TRP N   H2   sing N N 346 
TRP CA  C    sing N N 347 
TRP CA  CB   sing N N 348 
TRP CA  HA   sing N N 349 
TRP C   O    doub N N 350 
TRP C   OXT  sing N N 351 
TRP CB  CG   sing N N 352 
TRP CB  HB2  sing N N 353 
TRP CB  HB3  sing N N 354 
TRP CG  CD1  doub Y N 355 
TRP CG  CD2  sing Y N 356 
TRP CD1 NE1  sing Y N 357 
TRP CD1 HD1  sing N N 358 
TRP CD2 CE2  doub Y N 359 
TRP CD2 CE3  sing Y N 360 
TRP NE1 CE2  sing Y N 361 
TRP NE1 HE1  sing N N 362 
TRP CE2 CZ2  sing Y N 363 
TRP CE3 CZ3  doub Y N 364 
TRP CE3 HE3  sing N N 365 
TRP CZ2 CH2  doub Y N 366 
TRP CZ2 HZ2  sing N N 367 
TRP CZ3 CH2  sing Y N 368 
TRP CZ3 HZ3  sing N N 369 
TRP CH2 HH2  sing N N 370 
TRP OXT HXT  sing N N 371 
TYR N   CA   sing N N 372 
TYR N   H    sing N N 373 
TYR N   H2   sing N N 374 
TYR CA  C    sing N N 375 
TYR CA  CB   sing N N 376 
TYR CA  HA   sing N N 377 
TYR C   O    doub N N 378 
TYR C   OXT  sing N N 379 
TYR CB  CG   sing N N 380 
TYR CB  HB2  sing N N 381 
TYR CB  HB3  sing N N 382 
TYR CG  CD1  doub Y N 383 
TYR CG  CD2  sing Y N 384 
TYR CD1 CE1  sing Y N 385 
TYR CD1 HD1  sing N N 386 
TYR CD2 CE2  doub Y N 387 
TYR CD2 HD2  sing N N 388 
TYR CE1 CZ   doub Y N 389 
TYR CE1 HE1  sing N N 390 
TYR CE2 CZ   sing Y N 391 
TYR CE2 HE2  sing N N 392 
TYR CZ  OH   sing N N 393 
TYR OH  HH   sing N N 394 
TYR OXT HXT  sing N N 395 
VAL N   CA   sing N N 396 
VAL N   H    sing N N 397 
VAL N   H2   sing N N 398 
VAL CA  C    sing N N 399 
VAL CA  CB   sing N N 400 
VAL CA  HA   sing N N 401 
VAL C   O    doub N N 402 
VAL C   OXT  sing N N 403 
VAL CB  CG1  sing N N 404 
VAL CB  CG2  sing N N 405 
VAL CB  HB   sing N N 406 
VAL CG1 HG11 sing N N 407 
VAL CG1 HG12 sing N N 408 
VAL CG1 HG13 sing N N 409 
VAL CG2 HG21 sing N N 410 
VAL CG2 HG22 sing N N 411 
VAL CG2 HG23 sing N N 412 
VAL OXT HXT  sing N N 413 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Takeda Science Foundation'        Japan ? 1 
'Gimpu fund from Kyoto University' Japan ? 2 
# 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   6JGJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZUQ 
_atom_sites.fract_transf_matrix[1][1]   0.019803 
_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]   0.016012 
_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]   0.014753 
_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  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   A SER A 1 1   ? -3.32500  23.43800  83.37100  0.600 18.87381 ? 2   SER A N   1 
ATOM   2    N  N   B SER A 1 1   ? -3.73600  20.71000  83.92300  0.400 18.59381 ? 2   SER A N   1 
ATOM   3    C  CA  A SER A 1 1   ? -2.03000  23.08300  83.94700  0.600 12.30381 ? 2   SER A CA  1 
ATOM   4    C  CA  B SER A 1 1   ? -2.29500  20.65500  84.13400  0.400 23.86381 ? 2   SER A CA  1 
ATOM   5    C  C   A SER A 1 1   ? -0.93800  23.17400  82.88900  0.600 12.78381 ? 2   SER A C   1 
ATOM   6    C  C   B SER A 1 1   ? -1.58300  21.73000  83.33000  0.400 16.46381 ? 2   SER A C   1 
ATOM   7    O  O   A SER A 1 1   ? -1.22900  23.32700  81.70500  0.600 14.73381 ? 2   SER A O   1 
ATOM   8    O  O   B SER A 1 1   ? -2.11900  22.23300  82.34100  0.400 19.25381 ? 2   SER A O   1 
ATOM   9    C  CB  A SER A 1 1   ? -2.06800  21.67300  84.53600  0.600 18.94381 ? 2   SER A CB  1 
ATOM   10   C  CB  B SER A 1 1   ? -1.75400  19.29200  83.70000  0.400 16.86381 ? 2   SER A CB  1 
ATOM   11   O  OG  A SER A 1 1   ? -2.06100  20.70400  83.50800  0.600 27.62381 ? 2   SER A OG  1 
ATOM   12   O  OG  B SER A 1 1   ? -2.54200  18.23900  84.21500  0.400 13.14381 ? 2   SER A OG  1 
ATOM   13   N  N   A LYS A 1 2   ? 0.32100   23.05900  83.32800  0.600 13.11381 ? 3   LYS A N   1 
ATOM   14   N  N   B LYS A 1 2   ? -0.36500  22.08500  83.75000  0.400 17.16381 ? 3   LYS A N   1 
ATOM   15   C  CA  A LYS A 1 2   ? 1.45000   23.19800  82.41200  0.600 12.77381 ? 3   LYS A CA  1 
ATOM   16   C  CA  B LYS A 1 2   ? 0.49300   22.85500  82.85600  0.400 13.94381 ? 3   LYS A CA  1 
ATOM   17   C  C   A LYS A 1 2   ? 1.40900   22.15000  81.30500  0.600 18.16381 ? 3   LYS A C   1 
ATOM   18   C  C   B LYS A 1 2   ? 0.83200   22.04700  81.61200  0.400 15.87381 ? 3   LYS A C   1 
ATOM   19   O  O   A LYS A 1 2   ? 1.63500   22.46800  80.13200  0.600 17.85381 ? 3   LYS A O   1 
ATOM   20   O  O   B LYS A 1 2   ? 0.96800   22.61000  80.52000  0.400 14.53381 ? 3   LYS A O   1 
ATOM   21   C  CB  A LYS A 1 2   ? 2.76500   23.09500  83.17900  0.600 14.11381 ? 3   LYS A CB  1 
ATOM   22   C  CB  B LYS A 1 2   ? 1.76500   23.31700  83.57300  0.400 13.23381 ? 3   LYS A CB  1 
ATOM   23   C  CG  A LYS A 1 2   ? 3.98700   23.09500  82.27400  0.600 19.31381 ? 3   LYS A CG  1 
ATOM   24   C  CG  B LYS A 1 2   ? 2.74200   22.21500  83.93600  0.400 22.05381 ? 3   LYS A CG  1 
ATOM   25   C  CD  A LYS A 1 2   ? 5.21600   22.54700  82.98600  0.600 32.61381 ? 3   LYS A CD  1 
ATOM   26   C  CD  B LYS A 1 2   ? 3.99000   22.24100  83.06400  0.400 34.78381 ? 3   LYS A CD  1 
ATOM   27   C  CE  A LYS A 1 2   ? 5.58900   23.40200  84.18400  0.600 28.76381 ? 3   LYS A CE  1 
ATOM   28   C  CE  B LYS A 1 2   ? 4.94700   23.35000  83.48100  0.400 31.05381 ? 3   LYS A CE  1 
ATOM   29   N  NZ  A LYS A 1 2   ? 6.82600   22.89800  84.84000  0.600 32.43381 ? 3   LYS A NZ  1 
ATOM   30   N  NZ  B LYS A 1 2   ? 6.25200   23.23900  82.76600  0.400 29.68381 ? 3   LYS A NZ  1 
ATOM   31   N  N   A GLY A 1 3   ? 1.13100   20.89500  81.65800  0.600 15.15381 ? 4   GLY A N   1 
ATOM   32   N  N   B GLY A 1 3   ? 0.95000   20.72600  81.75600  0.400 15.62381 ? 4   GLY A N   1 
ATOM   33   C  CA  A GLY A 1 3   ? 1.15600   19.83600  80.65900  0.600 14.58381 ? 4   GLY A CA  1 
ATOM   34   C  CA  B GLY A 1 3   ? 1.18100   19.88300  80.59800  0.400 14.51381 ? 4   GLY A CA  1 
ATOM   35   C  C   A GLY A 1 3   ? 0.05400   19.97400  79.62400  0.600 12.75381 ? 4   GLY A C   1 
ATOM   36   C  C   B GLY A 1 3   ? 0.03400   19.91000  79.60900  0.400 12.74381 ? 4   GLY A C   1 
ATOM   37   O  O   A GLY A 1 3   ? 0.30800   19.88600  78.41900  0.600 13.08381 ? 4   GLY A O   1 
ATOM   38   O  O   B GLY A 1 3   ? 0.23900   19.68100  78.41400  0.400 15.06381 ? 4   GLY A O   1 
ATOM   39   N  N   . GLU A 1 4   ? -1.18300  20.19600  80.08500  1.000 14.36381 ? 5   GLU A N   1 
ATOM   40   C  CA  A GLU A 1 4   ? -2.33600  20.33900  79.19500  0.390 18.70381 ? 5   GLU A CA  1 
ATOM   41   C  CA  B GLU A 1 4   ? -2.31400  20.30000  79.17300  0.310 18.64381 ? 5   GLU A CA  1 
ATOM   42   C  CA  C GLU A 1 4   ? -2.38100  20.42300  79.26500  0.300 18.78381 ? 5   GLU A CA  1 
ATOM   43   C  C   . GLU A 1 4   ? -2.08200  21.37400  78.11400  1.000 13.13381 ? 5   GLU A C   1 
ATOM   44   O  O   . GLU A 1 4   ? -2.46100  21.18300  76.94900  1.000 16.40381 ? 5   GLU A O   1 
ATOM   45   C  CB  A GLU A 1 4   ? -3.56700  20.79800  79.98400  0.390 19.63381 ? 5   GLU A CB  1 
ATOM   46   C  CB  B GLU A 1 4   ? -3.59900  20.56200  79.96000  0.310 19.42381 ? 5   GLU A CB  1 
ATOM   47   C  CB  C GLU A 1 4   ? -3.49000  21.03100  80.12000  0.300 19.37381 ? 5   GLU A CB  1 
ATOM   48   C  CG  A GLU A 1 4   ? -3.91400  20.01300  81.22900  0.390 16.09381 ? 5   GLU A CG  1 
ATOM   49   C  CG  B GLU A 1 4   ? -4.86500  20.15800  79.23300  0.310 14.86381 ? 5   GLU A CG  1 
ATOM   50   C  CG  C GLU A 1 4   ? -4.73500  20.18500  80.23300  0.300 22.45381 ? 5   GLU A CG  1 
ATOM   51   C  CD  A GLU A 1 4   ? -4.97500  20.71600  82.07700  0.390 16.38381 ? 5   GLU A CD  1 
ATOM   52   C  CD  B GLU A 1 4   ? -5.43600  21.27900  78.39400  0.310 17.92381 ? 5   GLU A CD  1 
ATOM   53   C  CD  C GLU A 1 4   ? -5.80600  20.85900  81.05900  0.300 17.19381 ? 5   GLU A CD  1 
ATOM   54   O  OE1 A GLU A 1 4   ? -5.26200  21.90400  81.81400  0.390 17.40381 ? 5   GLU A OE1 1 
ATOM   55   O  OE1 B GLU A 1 4   ? -5.04200  22.44000  78.61200  0.310 15.68381 ? 5   GLU A OE1 1 
ATOM   56   O  OE1 C GLU A 1 4   ? -6.35100  21.88700  80.60000  0.300 20.75381 ? 5   GLU A OE1 1 
ATOM   57   O  OE2 A GLU A 1 4   ? -5.51900  20.08500  83.00900  0.390 14.36381 ? 5   GLU A OE2 1 
ATOM   58   O  OE2 B GLU A 1 4   ? -6.28000  20.99700  77.51900  0.310 21.84381 ? 5   GLU A OE2 1 
ATOM   59   O  OE2 C GLU A 1 4   ? -6.09200  20.37200  82.17500  0.300 7.26381  ? 5   GLU A OE2 1 
ATOM   60   N  N   A GLU A 1 5   ? -1.46800  22.50000  78.48300  0.460 13.30381 ? 6   GLU A N   1 
ATOM   61   N  N   B GLU A 1 5   ? -1.47700  22.50100  78.49900  0.540 13.24381 ? 6   GLU A N   1 
ATOM   62   C  CA  A GLU A 1 5   ? -1.31600  23.61000  77.55400  0.460 10.41381 ? 6   GLU A CA  1 
ATOM   63   C  CA  B GLU A 1 5   ? -1.31500  23.60800  77.56600  0.540 10.35381 ? 6   GLU A CA  1 
ATOM   64   C  C   A GLU A 1 5   ? -0.32500  23.32400  76.43600  0.460 12.71381 ? 6   GLU A C   1 
ATOM   65   C  C   B GLU A 1 5   ? -0.40100  23.26100  76.40000  0.540 12.52381 ? 6   GLU A C   1 
ATOM   66   O  O   A GLU A 1 5   ? -0.30300  24.06500  75.44700  0.460 14.72381 ? 6   GLU A O   1 
ATOM   67   O  O   B GLU A 1 5   ? -0.51500  23.88200  75.33800  0.540 12.38381 ? 6   GLU A O   1 
ATOM   68   C  CB  A GLU A 1 5   ? -0.92300  24.87100  78.32200  0.460 15.04381 ? 6   GLU A CB  1 
ATOM   69   C  CB  B GLU A 1 5   ? -0.81100  24.85100  78.30600  0.540 14.79381 ? 6   GLU A CB  1 
ATOM   70   C  CG  A GLU A 1 5   ? -1.95700  25.26900  79.36100  0.460 21.20381 ? 6   GLU A CG  1 
ATOM   71   C  CG  B GLU A 1 5   ? -1.73800  25.32800  79.42300  0.540 23.20381 ? 6   GLU A CG  1 
ATOM   72   C  CD  A GLU A 1 5   ? -1.43300  26.29200  80.34200  0.460 20.84381 ? 6   GLU A CD  1 
ATOM   73   C  CD  B GLU A 1 5   ? -3.04200  25.93100  78.91200  0.540 27.59381 ? 6   GLU A CD  1 
ATOM   74   O  OE1 A GLU A 1 5   ? -0.61400  27.14200  79.93800  0.460 32.24381 ? 6   GLU A OE1 1 
ATOM   75   O  OE1 B GLU A 1 5   ? -3.12200  26.30000  77.72000  0.540 26.63381 ? 6   GLU A OE1 1 
ATOM   76   O  OE2 A GLU A 1 5   ? -1.83500  26.24000  81.52300  0.460 27.16381 ? 6   GLU A OE2 1 
ATOM   77   O  OE2 B GLU A 1 5   ? -3.99000  26.04100  79.71600  0.540 29.37381 ? 6   GLU A OE2 1 
ATOM   78   N  N   . LEU A 1 6   ? 0.49100   22.27900  76.56600  1.000 10.57381 ? 7   LEU A N   1 
ATOM   79   C  CA  . LEU A 1 6   ? 1.40000   21.90200  75.48900  1.000 11.98381 ? 7   LEU A CA  1 
ATOM   80   C  C   . LEU A 1 6   ? 0.68400   21.22500  74.33000  1.000 7.47381  ? 7   LEU A C   1 
ATOM   81   O  O   . LEU A 1 6   ? 1.28500   21.06900  73.26200  1.000 11.66381 ? 7   LEU A O   1 
ATOM   82   C  CB  . LEU A 1 6   ? 2.49400   20.98200  76.03000  1.000 10.67381 ? 7   LEU A CB  1 
ATOM   83   C  CG  . LEU A 1 6   ? 3.33100   21.59900  77.15600  1.000 11.39381 ? 7   LEU A CG  1 
ATOM   84   C  CD1 . LEU A 1 6   ? 4.27300   20.56400  77.75600  1.000 15.98381 ? 7   LEU A CD1 1 
ATOM   85   C  CD2 . LEU A 1 6   ? 4.10500   22.81200  76.64900  1.000 19.69381 ? 7   LEU A CD2 1 
ATOM   86   N  N   . PHE A 1 7   ? -0.58800  20.87800  74.50200  1.000 9.34381  ? 8   PHE A N   1 
ATOM   87   C  CA  . PHE A 1 7   ? -1.32000  20.06500  73.53900  1.000 9.18381  ? 8   PHE A CA  1 
ATOM   88   C  C   . PHE A 1 7   ? -2.51200  20.77700  72.92500  1.000 9.53381  ? 8   PHE A C   1 
ATOM   89   O  O   . PHE A 1 7   ? -3.29900  20.13300  72.22500  1.000 11.70381 ? 8   PHE A O   1 
ATOM   90   C  CB  . PHE A 1 7   ? -1.76500  18.75800  74.20100  1.000 8.78381  ? 8   PHE A CB  1 
ATOM   91   C  CG  . PHE A 1 7   ? -0.62100  17.85200  74.53000  1.000 8.23381  ? 8   PHE A CG  1 
ATOM   92   C  CD1 . PHE A 1 7   ? -0.12900  16.97800  73.58100  1.000 10.25381 ? 8   PHE A CD1 1 
ATOM   93   C  CD2 . PHE A 1 7   ? -0.00300  17.91700  75.77700  1.000 8.32381  ? 8   PHE A CD2 1 
ATOM   94   C  CE1 . PHE A 1 7   ? 0.95700   16.16500  73.86900  1.000 10.02381 ? 8   PHE A CE1 1 
ATOM   95   C  CE2 . PHE A 1 7   ? 1.06500   17.09900  76.08300  1.000 7.39381  ? 8   PHE A CE2 1 
ATOM   96   C  CZ  . PHE A 1 7   ? 1.54500   16.21400  75.12000  1.000 9.53381  ? 8   PHE A CZ  1 
ATOM   97   N  N   . THR A 1 8   ? -2.64500  22.08800  73.12700  1.000 9.92381  ? 9   THR A N   1 
ATOM   98   C  CA  . THR A 1 8   ? -3.81900  22.77200  72.59500  1.000 11.08381 ? 9   THR A CA  1 
ATOM   99   C  C   . THR A 1 8   ? -3.74900  22.97700  71.08800  1.000 11.99381 ? 9   THR A C   1 
ATOM   100  O  O   . THR A 1 8   ? -4.77700  23.29600  70.47500  1.000 15.31381 ? 9   THR A O   1 
ATOM   101  C  CB  . THR A 1 8   ? -4.00800  24.11200  73.30300  1.000 10.40381 ? 9   THR A CB  1 
ATOM   102  O  OG1 . THR A 1 8   ? -2.78300  24.84000  73.24300  1.000 14.74381 ? 9   THR A OG1 1 
ATOM   103  C  CG2 . THR A 1 8   ? -4.39600  23.89000  74.75300  1.000 12.33381 ? 9   THR A CG2 1 
ATOM   104  N  N   . GLY A 1 9   ? -2.57500  22.80500  70.48400  1.000 11.41381 ? 10  GLY A N   1 
ATOM   105  C  CA  . GLY A 1 9   ? -2.42400  22.90400  69.04600  1.000 10.98381 ? 10  GLY A CA  1 
ATOM   106  C  C   . GLY A 1 9   ? -1.88600  21.62800  68.43600  1.000 12.98381 ? 10  GLY A C   1 
ATOM   107  O  O   . GLY A 1 9   ? -1.89200  20.57400  69.08200  1.000 14.28381 ? 10  GLY A O   1 
ATOM   108  N  N   . VAL A 1 10  ? -1.44100  21.71200  67.18800  1.000 11.09381 ? 11  VAL A N   1 
ATOM   109  C  CA  . VAL A 1 10  ? -0.86400  20.56900  66.48600  1.000 9.08381  ? 11  VAL A CA  1 
ATOM   110  C  C   . VAL A 1 10  ? 0.58600   20.42300  66.92300  1.000 10.33381 ? 11  VAL A C   1 
ATOM   111  O  O   . VAL A 1 10  ? 1.35300   21.39300  66.89500  1.000 13.47381 ? 11  VAL A O   1 
ATOM   112  C  CB  . VAL A 1 10  ? -0.96300  20.77400  64.96500  1.000 10.70381 ? 11  VAL A CB  1 
ATOM   113  C  CG1 . VAL A 1 10  ? -0.29300  19.61900  64.22400  1.000 13.29381 ? 11  VAL A CG1 1 
ATOM   114  C  CG2 . VAL A 1 10  ? -2.42200  20.89700  64.52900  1.000 11.52381 ? 11  VAL A CG2 1 
ATOM   115  N  N   . VAL A 1 11  ? 0.97300   19.21300  67.31600  1.000 11.02381 ? 12  VAL A N   1 
ATOM   116  C  CA  . VAL A 1 11  ? 2.28500   18.94200  67.89200  1.000 9.85381  ? 12  VAL A CA  1 
ATOM   117  C  C   . VAL A 1 11  ? 2.99400   17.93100  67.00200  1.000 10.37381 ? 12  VAL A C   1 
ATOM   118  O  O   . VAL A 1 11  ? 2.44900   16.85300  66.75300  1.000 8.58381  ? 12  VAL A O   1 
ATOM   119  C  CB  . VAL A 1 11  ? 2.18700   18.40400  69.33200  1.000 10.60381 ? 12  VAL A CB  1 
ATOM   120  C  CG1 . VAL A 1 11  ? 3.56600   18.02100  69.88400  1.000 9.98381  ? 12  VAL A CG1 1 
ATOM   121  C  CG2 . VAL A 1 11  ? 1.51000   19.42000  70.23900  1.000 8.72381  ? 12  VAL A CG2 1 
ATOM   122  N  N   . PRO A 1 12  ? 4.20600   18.22100  66.52400  1.000 8.12381  ? 13  PRO A N   1 
ATOM   123  C  CA  A PRO A 1 12  ? 4.94300   17.22400  65.73800  0.430 7.68381  ? 13  PRO A CA  1 
ATOM   124  C  CA  B PRO A 1 12  ? 4.94300   17.22600  65.73700  0.570 7.64381  ? 13  PRO A CA  1 
ATOM   125  C  C   . PRO A 1 12  ? 5.34100   16.05200  66.61600  1.000 8.18381  ? 13  PRO A C   1 
ATOM   126  O  O   . PRO A 1 12  ? 5.65000   16.22000  67.79700  1.000 7.67381  ? 13  PRO A O   1 
ATOM   127  C  CB  A PRO A 1 12  ? 6.18300   17.99200  65.25800  0.430 10.45381 ? 13  PRO A CB  1 
ATOM   128  C  CB  B PRO A 1 12  ? 6.17700   17.99900  65.25100  0.570 10.43381 ? 13  PRO A CB  1 
ATOM   129  C  CG  A PRO A 1 12  ? 5.83900   19.43400  65.42700  0.430 8.31381  ? 13  PRO A CG  1 
ATOM   130  C  CG  B PRO A 1 12  ? 6.33900   19.11900  66.23500  0.570 8.51381  ? 13  PRO A CG  1 
ATOM   131  C  CD  A PRO A 1 12  ? 4.92900   19.50000  66.61000  0.430 9.92381  ? 13  PRO A CD  1 
ATOM   132  C  CD  B PRO A 1 12  ? 4.95600   19.48100  66.68400  0.570 9.91381  ? 13  PRO A CD  1 
ATOM   133  N  N   . ILE A 1 13  ? 5.30700   14.85300  66.02800  1.000 7.29381  ? 14  ILE A N   1 
ATOM   134  C  CA  . ILE A 1 13  ? 5.62300   13.61600  66.73300  1.000 7.80381  ? 14  ILE A CA  1 
ATOM   135  C  C   . ILE A 1 13  ? 6.76300   12.90100  66.03100  1.000 9.61381  ? 14  ILE A C   1 
ATOM   136  O  O   . ILE A 1 13  ? 6.80200   12.82700  64.80100  1.000 7.83381  ? 14  ILE A O   1 
ATOM   137  C  CB  . ILE A 1 13  ? 4.39900   12.68900  66.78700  1.000 6.31381  ? 14  ILE A CB  1 
ATOM   138  C  CG1 . ILE A 1 13  ? 3.25900   13.37900  67.52500  1.000 7.60381  ? 14  ILE A CG1 1 
ATOM   139  C  CG2 . ILE A 1 13  ? 4.75600   11.38000  67.47700  1.000 8.63381  ? 14  ILE A CG2 1 
ATOM   140  C  CD1 . ILE A 1 13  ? 1.95500   12.64400  67.34800  1.000 8.10381  ? 14  ILE A CD1 1 
ATOM   141  N  N   . LEU A 1 14  ? 7.67700   12.35800  66.82000  1.000 8.70381  ? 15  LEU A N   1 
ATOM   142  C  CA  . LEU A 1 14  ? 8.70100   11.45300  66.32300  1.000 6.37381  ? 15  LEU A CA  1 
ATOM   143  C  C   . LEU A 1 14  ? 8.62500   10.16100  67.11800  1.000 8.41381  ? 15  LEU A C   1 
ATOM   144  O  O   . LEU A 1 14  ? 8.44500   10.18200  68.34100  1.000 8.46381  ? 15  LEU A O   1 
ATOM   145  C  CB  . LEU A 1 14  ? 10.09600  12.04300  66.52700  1.000 8.12381  ? 15  LEU A CB  1 
ATOM   146  C  CG  . LEU A 1 14  ? 10.31900  13.35900  65.78900  1.000 7.88381  ? 15  LEU A CG  1 
ATOM   147  C  CD1 . LEU A 1 14  ? 11.67100  13.94200  66.19400  1.000 9.79381  ? 15  LEU A CD1 1 
ATOM   148  C  CD2 . LEU A 1 14  ? 10.23700  13.15100  64.27600  1.000 9.30381  ? 15  LEU A CD2 1 
ATOM   149  N  N   . VAL A 1 15  ? 8.75700   9.03800   66.42100  1.000 7.40381  ? 16  VAL A N   1 
ATOM   150  C  CA  . VAL A 1 15  ? 8.77800   7.71800   67.04300  1.000 6.41381  ? 16  VAL A CA  1 
ATOM   151  C  C   . VAL A 1 15  ? 10.04300  7.00300   66.59600  1.000 6.95381  ? 16  VAL A C   1 
ATOM   152  O  O   . VAL A 1 15  ? 10.37600  7.00700   65.40800  1.000 8.91381  ? 16  VAL A O   1 
ATOM   153  C  CB  . VAL A 1 15  ? 7.53500   6.89000   66.66700  1.000 7.05381  ? 16  VAL A CB  1 
ATOM   154  C  CG1 . VAL A 1 15  ? 7.57500   5.50300   67.36600  1.000 6.68381  ? 16  VAL A CG1 1 
ATOM   155  C  CG2 . VAL A 1 15  ? 6.25100   7.67300   66.99700  1.000 6.82381  ? 16  VAL A CG2 1 
ATOM   156  N  N   . GLU A 1 16  ? 10.75100  6.40200   67.54300  1.000 7.33381  ? 17  GLU A N   1 
ATOM   157  C  CA  . GLU A 1 16  ? 11.96300  5.66100   67.21500  1.000 6.40381  ? 17  GLU A CA  1 
ATOM   158  C  C   . GLU A 1 16  ? 11.92700  4.36900   68.00600  1.000 7.78381  ? 17  GLU A C   1 
ATOM   159  O  O   . GLU A 1 16  ? 11.81700  4.40300   69.23100  1.000 10.50381 ? 17  GLU A O   1 
ATOM   160  C  CB  . GLU A 1 16  ? 13.22000  6.47000   67.54900  1.000 9.22381  ? 17  GLU A CB  1 
ATOM   161  C  CG  . GLU A 1 16  ? 13.39800  7.71200   66.66300  1.000 9.02381  ? 17  GLU A CG  1 
ATOM   162  C  CD  . GLU A 1 16  ? 13.70800  7.37000   65.21300  1.000 9.27381  ? 17  GLU A CD  1 
ATOM   163  O  OE1 . GLU A 1 16  ? 14.26900  6.29500   64.96800  1.000 16.56381 ? 17  GLU A OE1 1 
ATOM   164  O  OE2 . GLU A 1 16  ? 13.41500  8.17600   64.31400  1.000 12.85381 ? 17  GLU A OE2 1 
ATOM   165  N  N   . LEU A 1 17  ? 12.00800  3.23300   67.31400  1.000 7.57381  ? 18  LEU A N   1 
ATOM   166  C  CA  . LEU A 1 17  ? 11.96000  1.94100   67.97300  1.000 6.50381  ? 18  LEU A CA  1 
ATOM   167  C  C   . LEU A 1 17  ? 13.15100  1.10600   67.53700  1.000 8.12381  ? 18  LEU A C   1 
ATOM   168  O  O   . LEU A 1 17  ? 13.49800  1.06900   66.35400  1.000 9.44381  ? 18  LEU A O   1 
ATOM   169  C  CB  . LEU A 1 17  ? 10.65000  1.19200   67.65000  1.000 7.75381  ? 18  LEU A CB  1 
ATOM   170  C  CG  . LEU A 1 17  ? 10.50200  -0.25300  68.15900  1.000 7.76381  ? 18  LEU A CG  1 
ATOM   171  C  CD1 . LEU A 1 17  ? 9.03100   -0.56100  68.46600  1.000 9.42381  ? 18  LEU A CD1 1 
ATOM   172  C  CD2 . LEU A 1 17  ? 11.03500  -1.24400  67.12700  1.000 8.69381  ? 18  LEU A CD2 1 
ATOM   173  N  N   . ASP A 1 18  ? 13.77800  0.44400   68.49900  1.000 8.22381  ? 19  ASP A N   1 
ATOM   174  C  CA  . ASP A 1 18  ? 14.72500  -0.62400  68.21400  1.000 9.96381  ? 19  ASP A CA  1 
ATOM   175  C  C   . ASP A 1 18  ? 14.11600  -1.90900  68.73500  1.000 7.57381  ? 19  ASP A C   1 
ATOM   176  O  O   . ASP A 1 18  ? 13.62000  -1.94000  69.86400  1.000 9.33381  ? 19  ASP A O   1 
ATOM   177  C  CB  . ASP A 1 18  ? 16.05600  -0.36800  68.90900  1.000 10.64381 ? 19  ASP A CB  1 
ATOM   178  C  CG  . ASP A 1 18  ? 16.84800  0.73300   68.24300  1.000 16.25381 ? 19  ASP A CG  1 
ATOM   179  O  OD1 . ASP A 1 18  ? 16.87100  0.79400   66.98900  1.000 14.88381 ? 19  ASP A OD1 1 
ATOM   180  O  OD2 . ASP A 1 18  ? 17.44300  1.54800   68.97800  1.000 26.17381 ? 19  ASP A OD2 1 
ATOM   181  N  N   . GLY A 1 19  ? 14.16200  -2.96300  67.93000  1.000 8.73381  ? 20  GLY A N   1 
ATOM   182  C  CA  . GLY A 1 19  ? 13.50200  -4.20400  68.27800  1.000 8.79381  ? 20  GLY A CA  1 
ATOM   183  C  C   . GLY A 1 19  ? 14.36700  -5.42400  68.04600  1.000 10.19381 ? 20  GLY A C   1 
ATOM   184  O  O   . GLY A 1 19  ? 15.24800  -5.44300  67.18800  1.000 9.28381  ? 20  GLY A O   1 
ATOM   185  N  N   . ASP A 1 20  ? 14.10100  -6.45100  68.84600  1.000 8.06381  ? 21  ASP A N   1 
ATOM   186  C  CA  . ASP A 1 20  ? 14.69800  -7.77200  68.65500  1.000 8.73381  ? 21  ASP A CA  1 
ATOM   187  C  C   . ASP A 1 20  ? 13.58600  -8.76500  68.95400  1.000 7.97381  ? 21  ASP A C   1 
ATOM   188  O  O   . ASP A 1 20  ? 13.16500  -8.88500  70.10900  1.000 10.48381 ? 21  ASP A O   1 
ATOM   189  C  CB  . ASP A 1 20  ? 15.88500  -7.96500  69.60600  1.000 9.96381  ? 21  ASP A CB  1 
ATOM   190  C  CG  . ASP A 1 20  ? 16.46800  -9.37600  69.57400  1.000 9.72381  ? 21  ASP A CG  1 
ATOM   191  O  OD1 . ASP A 1 20  ? 15.76400  -10.32500 69.18600  1.000 10.28381 ? 21  ASP A OD1 1 
ATOM   192  O  OD2 . ASP A 1 20  ? 17.65300  -9.50800  69.96800  1.000 15.27381 ? 21  ASP A OD2 1 
ATOM   193  N  N   . VAL A 1 21  ? 13.11100  -9.46200  67.92400  1.000 7.83381  ? 22  VAL A N   1 
ATOM   194  C  CA  . VAL A 1 21  ? 12.06400  -10.47600 68.05000  1.000 7.54381  ? 22  VAL A CA  1 
ATOM   195  C  C   . VAL A 1 21  ? 12.66900  -11.79700 67.60400  1.000 8.61381  ? 22  VAL A C   1 
ATOM   196  O  O   . VAL A 1 21  ? 12.99400  -11.96900 66.42100  1.000 9.74381  ? 22  VAL A O   1 
ATOM   197  C  CB  . VAL A 1 21  ? 10.80900  -10.13000 67.23100  1.000 7.44381  ? 22  VAL A CB  1 
ATOM   198  C  CG1 . VAL A 1 21  ? 9.79500   -11.27000 67.30600  1.000 8.74381  ? 22  VAL A CG1 1 
ATOM   199  C  CG2 . VAL A 1 21  ? 10.15600  -8.84900  67.74400  1.000 8.10381  ? 22  VAL A CG2 1 
ATOM   200  N  N   . ASN A 1 22  ? 12.83000  -12.72300 68.55000  1.000 7.63381  ? 23  ASN A N   1 
ATOM   201  C  CA  . ASN A 1 22  ? 13.41800  -14.03700 68.26400  1.000 8.74381  ? 23  ASN A CA  1 
ATOM   202  C  C   . ASN A 1 22  ? 14.75900  -13.89500 67.53800  1.000 10.54381 ? 23  ASN A C   1 
ATOM   203  O  O   . ASN A 1 22  ? 15.08100  -14.65600 66.62400  1.000 10.15381 ? 23  ASN A O   1 
ATOM   204  C  CB  . ASN A 1 22  ? 12.46300  -14.92300 67.45500  1.000 8.13381  ? 23  ASN A CB  1 
ATOM   205  C  CG  . ASN A 1 22  ? 11.44500  -15.66000 68.30900  1.000 10.02381 ? 23  ASN A CG  1 
ATOM   206  O  OD1 . ASN A 1 22  ? 10.89900  -15.13200 69.27500  1.000 10.60381 ? 23  ASN A OD1 1 
ATOM   207  N  ND2 . ASN A 1 22  ? 11.16400  -16.89400 67.92100  1.000 10.32381 ? 23  ASN A ND2 1 
ATOM   208  N  N   . GLY A 1 23  ? 15.53400  -12.87800 67.91200  1.000 9.63381  ? 24  GLY A N   1 
ATOM   209  C  CA  . GLY A 1 23  ? 16.82500  -12.67800 67.28900  1.000 9.95381  ? 24  GLY A CA  1 
ATOM   210  C  C   . GLY A 1 23  ? 16.81000  -11.86900 66.01000  1.000 11.22381 ? 24  GLY A C   1 
ATOM   211  O  O   . GLY A 1 23  ? 17.88700  -11.55000 65.49000  1.000 13.74381 ? 24  GLY A O   1 
ATOM   212  N  N   . HIS A 1 24  ? 15.63600  -11.53200 65.47800  1.000 10.36381 ? 25  HIS A N   1 
ATOM   213  C  CA  . HIS A 1 24  ? 15.53400  -10.64800 64.32200  1.000 10.65381 ? 25  HIS A CA  1 
ATOM   214  C  C   . HIS A 1 24  ? 15.59600  -9.21900  64.84000  1.000 12.40381 ? 25  HIS A C   1 
ATOM   215  O  O   . HIS A 1 24  ? 14.67200  -8.76600  65.52400  1.000 11.56381 ? 25  HIS A O   1 
ATOM   216  C  CB  . HIS A 1 24  ? 14.19600  -10.84000 63.61400  1.000 12.24381 ? 25  HIS A CB  1 
ATOM   217  C  CG  . HIS A 1 24  ? 13.96900  -12.21800 63.07700  1.000 14.87381 ? 25  HIS A CG  1 
ATOM   218  N  ND1 . HIS A 1 24  ? 14.29100  -12.57200 61.78400  1.000 22.85381 ? 25  HIS A ND1 1 
ATOM   219  C  CD2 . HIS A 1 24  ? 13.40800  -13.31300 63.64100  1.000 16.21381 ? 25  HIS A CD2 1 
ATOM   220  C  CE1 . HIS A 1 24  ? 13.95900  -13.83500 61.58300  1.000 23.17381 ? 25  HIS A CE1 1 
ATOM   221  N  NE2 . HIS A 1 24  ? 13.42300  -14.30800 62.69300  1.000 19.88381 ? 25  HIS A NE2 1 
ATOM   222  N  N   . LYS A 1 25  ? 16.67200  -8.51300  64.52000  1.000 10.39381 ? 26  LYS A N   1 
ATOM   223  C  CA  . LYS A 1 25  ? 16.87200  -7.14900  64.97900  1.000 8.99381  ? 26  LYS A CA  1 
ATOM   224  C  C   . LYS A 1 25  ? 16.42100  -6.17300  63.90200  1.000 12.41381 ? 26  LYS A C   1 
ATOM   225  O  O   . LYS A 1 25  ? 16.71000  -6.36000  62.71700  1.000 13.92381 ? 26  LYS A O   1 
ATOM   226  C  CB  . LYS A 1 25  ? 18.34400  -6.92900  65.31100  1.000 13.22381 ? 26  LYS A CB  1 
ATOM   227  C  CG  . LYS A 1 25  ? 18.84100  -7.88700  66.37700  1.000 16.09381 ? 26  LYS A CG  1 
ATOM   228  C  CD  . LYS A 1 25  ? 20.27100  -7.59100  66.76800  1.000 24.64381 ? 26  LYS A CD  1 
ATOM   229  C  CE  . LYS A 1 25  ? 20.77200  -8.59500  67.79300  1.000 38.39381 ? 26  LYS A CE  1 
ATOM   230  N  NZ  . LYS A 1 25  ? 19.83200  -8.73100  68.93600  1.000 38.41381 ? 26  LYS A NZ  1 
ATOM   231  N  N   . PHE A 1 26  ? 15.69700  -5.13500  64.31600  1.000 9.85381  ? 27  PHE A N   1 
ATOM   232  C  CA  . PHE A 1 26  ? 15.15600  -4.18500  63.36000  1.000 10.62381 ? 27  PHE A CA  1 
ATOM   233  C  C   . PHE A 1 26  ? 14.98700  -2.83100  64.03300  1.000 9.88381  ? 27  PHE A C   1 
ATOM   234  O  O   . PHE A 1 26  ? 15.01000  -2.71300  65.26100  1.000 9.77381  ? 27  PHE A O   1 
ATOM   235  C  CB  . PHE A 1 26  ? 13.80800  -4.65300  62.79300  1.000 8.32381  ? 27  PHE A CB  1 
ATOM   236  C  CG  . PHE A 1 26  ? 12.75900  -4.90000  63.84100  1.000 9.23381  ? 27  PHE A CG  1 
ATOM   237  C  CD1 . PHE A 1 26  ? 12.76700  -6.07200  64.59200  1.000 11.69381 ? 27  PHE A CD1 1 
ATOM   238  C  CD2 . PHE A 1 26  ? 11.74900  -3.97800  64.07200  1.000 9.96381  ? 27  PHE A CD2 1 
ATOM   239  C  CE1 . PHE A 1 26  ? 11.78900  -6.31800  65.55100  1.000 9.63381  ? 27  PHE A CE1 1 
ATOM   240  C  CE2 . PHE A 1 26  ? 10.76200  -4.21500  65.03700  1.000 8.88381  ? 27  PHE A CE2 1 
ATOM   241  C  CZ  . PHE A 1 26  ? 10.78200  -5.38700  65.77700  1.000 9.56381  ? 27  PHE A CZ  1 
ATOM   242  N  N   . SER A 1 27  ? 14.82500  -1.80400  63.20500  1.000 7.84381  ? 28  SER A N   1 
ATOM   243  C  CA  . SER A 1 27  ? 14.56500  -0.46600  63.71000  1.000 8.52381  ? 28  SER A CA  1 
ATOM   244  C  C   . SER A 1 27  ? 13.46800  0.16900   62.87600  1.000 9.39381  ? 28  SER A C   1 
ATOM   245  O  O   . SER A 1 27  ? 13.33900  -0.10700  61.68100  1.000 9.02381  ? 28  SER A O   1 
ATOM   246  C  CB  . SER A 1 27  ? 15.81700  0.41500   63.64600  1.000 10.07381 ? 28  SER A CB  1 
ATOM   247  O  OG  . SER A 1 27  ? 16.87500  -0.18800  64.38600  1.000 14.33381 ? 28  SER A OG  1 
ATOM   248  N  N   . VAL A 1 28  ? 12.68400  1.03600   63.51300  1.000 8.27381  ? 29  VAL A N   1 
ATOM   249  C  CA  . VAL A 1 28  ? 11.62300  1.77200   62.83800  1.000 7.96381  ? 29  VAL A CA  1 
ATOM   250  C  C   . VAL A 1 28  ? 11.71900  3.23400   63.25400  1.000 8.79381  ? 29  VAL A C   1 
ATOM   251  O  O   . VAL A 1 28  ? 11.91500  3.53000   64.43500  1.000 9.41381  ? 29  VAL A O   1 
ATOM   252  C  CB  . VAL A 1 28  ? 10.23400  1.21400   63.21200  1.000 8.40381  ? 29  VAL A CB  1 
ATOM   253  C  CG1 . VAL A 1 28  ? 9.12100   2.12700   62.67100  1.000 7.57381  ? 29  VAL A CG1 1 
ATOM   254  C  CG2 . VAL A 1 28  ? 10.07100  -0.21500  62.69800  1.000 9.14381  ? 29  VAL A CG2 1 
ATOM   255  N  N   . SER A 1 29  ? 11.57800  4.14100   62.28300  1.000 9.23381  ? 30  SER A N   1 
ATOM   256  C  CA  . SER A 1 29  ? 11.46000  5.57200   62.53700  1.000 8.14381  ? 30  SER A CA  1 
ATOM   257  C  C   . SER A 1 29  ? 10.10200  6.04300   62.04800  1.000 9.93381  ? 30  SER A C   1 
ATOM   258  O  O   . SER A 1 29  ? 9.68200   5.69000   60.94400  1.000 10.69381 ? 30  SER A O   1 
ATOM   259  C  CB  . SER A 1 29  ? 12.54400  6.35600   61.79000  1.000 10.20381 ? 30  SER A CB  1 
ATOM   260  O  OG  . SER A 1 29  ? 13.83400  6.00800   62.27200  1.000 12.75381 ? 30  SER A OG  1 
ATOM   261  N  N   . GLY A 1 30  ? 9.42600   6.84500   62.85700  1.000 8.79381  ? 31  GLY A N   1 
ATOM   262  C  CA  . GLY A 1 30  ? 8.13300   7.37600   62.48300  1.000 9.59381  ? 31  GLY A CA  1 
ATOM   263  C  C   . GLY A 1 30  ? 8.08100   8.87500   62.67700  1.000 8.93381  ? 31  GLY A C   1 
ATOM   264  O  O   . GLY A 1 30  ? 8.78200   9.43700   63.51200  1.000 9.34381  ? 31  GLY A O   1 
ATOM   265  N  N   . GLU A 1 31  ? 7.21200   9.51500   61.89100  1.000 8.17381  ? 32  GLU A N   1 
ATOM   266  C  CA  . GLU A 1 31  ? 6.98600   10.95000  61.97300  1.000 7.91381  ? 32  GLU A CA  1 
ATOM   267  C  C   . GLU A 1 31  ? 5.51000   11.22900  61.74800  1.000 7.90381  ? 32  GLU A C   1 
ATOM   268  O  O   . GLU A 1 31  ? 4.82100   10.51500  61.01100  1.000 8.68381  ? 32  GLU A O   1 
ATOM   269  C  CB  . GLU A 1 31  ? 7.73600   11.73600  60.88800  1.000 9.15381  ? 32  GLU A CB  1 
ATOM   270  C  CG  . GLU A 1 31  ? 9.24100   11.57100  60.90500  1.000 9.36381  ? 32  GLU A CG  1 
ATOM   271  C  CD  . GLU A 1 31  ? 9.90300   12.31500  59.76400  1.000 8.73381  ? 32  GLU A CD  1 
ATOM   272  O  OE1 . GLU A 1 31  ? 9.27800   13.27400  59.24400  1.000 12.31381 ? 32  GLU A OE1 1 
ATOM   273  O  OE2 . GLU A 1 31  ? 11.04500  11.94500  59.40900  1.000 12.32381 ? 32  GLU A OE2 1 
ATOM   274  N  N   . GLY A 1 32  ? 5.05100   12.31200  62.34600  1.000 9.51381  ? 33  GLY A N   1 
ATOM   275  C  CA  . GLY A 1 32  ? 3.68400   12.73800  62.10000  1.000 8.89381  ? 33  GLY A CA  1 
ATOM   276  C  C   . GLY A 1 32  ? 3.33400   13.86600  63.02600  1.000 6.73381  ? 33  GLY A C   1 
ATOM   277  O  O   . GLY A 1 32  ? 4.20400   14.63300  63.44400  1.000 9.23381  ? 33  GLY A O   1 
ATOM   278  N  N   . GLU A 1 33  ? 2.04900   13.96400  63.34500  1.000 9.28381  ? 34  GLU A N   1 
ATOM   279  C  CA  . GLU A 1 33  ? 1.60800   15.03600  64.21900  1.000 8.91381  ? 34  GLU A CA  1 
ATOM   280  C  C   . GLU A 1 33  ? 0.34800   14.61400  64.95000  1.000 7.28381  ? 34  GLU A C   1 
ATOM   281  O  O   . GLU A 1 33  ? -0.39100  13.73100  64.49800  1.000 9.89381  ? 34  GLU A O   1 
ATOM   282  C  CB  . GLU A 1 33  ? 1.35300   16.33200  63.44900  1.000 14.36381 ? 34  GLU A CB  1 
ATOM   283  C  CG  . GLU A 1 33  ? 0.28200   16.20500  62.39900  1.000 13.29381 ? 34  GLU A CG  1 
ATOM   284  C  CD  . GLU A 1 33  ? 0.14300   17.46000  61.54300  1.000 17.33381 ? 34  GLU A CD  1 
ATOM   285  O  OE1 . GLU A 1 33  ? 1.15300   18.17600  61.34800  1.000 20.09381 ? 34  GLU A OE1 1 
ATOM   286  O  OE2 . GLU A 1 33  ? -0.98700  17.74600  61.08000  1.000 16.40381 ? 34  GLU A OE2 1 
ATOM   287  N  N   . GLY A 1 34  ? 0.13100   15.23200  66.10100  1.000 8.57381  ? 35  GLY A N   1 
ATOM   288  C  CA  . GLY A 1 34  ? -1.04400  14.95400  66.89900  1.000 8.13381  ? 35  GLY A CA  1 
ATOM   289  C  C   . GLY A 1 34  ? -1.76900  16.24000  67.22900  1.000 8.56381  ? 35  GLY A C   1 
ATOM   290  O  O   . GLY A 1 34  ? -1.16300  17.29300  67.40900  1.000 9.98381  ? 35  GLY A O   1 
ATOM   291  N  N   . ASP A 1 35  ? -3.09000  16.13700  67.32200  1.000 9.04381  ? 36  ASP A N   1 
ATOM   292  C  CA  . ASP A 1 35  ? -3.95200  17.28000  67.61800  1.000 10.25381 ? 36  ASP A CA  1 
ATOM   293  C  C   . ASP A 1 35  ? -4.90900  16.77000  68.69200  1.000 8.81381  ? 36  ASP A C   1 
ATOM   294  O  O   . ASP A 1 35  ? -5.99200  16.27200  68.36900  1.000 9.49381  ? 36  ASP A O   1 
ATOM   295  C  CB  . ASP A 1 35  ? -4.68500  17.70100  66.32800  1.000 12.08381 ? 36  ASP A CB  1 
ATOM   296  C  CG  . ASP A 1 35  ? -5.20900  19.13200  66.36800  1.000 17.23381 ? 36  ASP A CG  1 
ATOM   297  O  OD1 . ASP A 1 35  ? -5.15800  19.76600  67.43800  1.000 17.22381 ? 36  ASP A OD1 1 
ATOM   298  O  OD2 . ASP A 1 35  ? -5.67200  19.60900  65.30400  1.000 22.58381 ? 36  ASP A OD2 1 
ATOM   299  N  N   . ALA A 1 36  ? -4.48700  16.85900  69.95900  1.000 9.33381  ? 37  ALA A N   1 
ATOM   300  C  CA  . ALA A 1 36  ? -5.26400  16.29800  71.06100  1.000 9.62381  ? 37  ALA A CA  1 
ATOM   301  C  C   . ALA A 1 36  ? -6.62100  16.96300  71.21700  1.000 8.61381  ? 37  ALA A C   1 
ATOM   302  O  O   . ALA A 1 36  ? -7.53000  16.35700  71.79800  1.000 9.43381  ? 37  ALA A O   1 
ATOM   303  C  CB  . ALA A 1 36  ? -4.50000  16.43700  72.37800  1.000 9.74381  ? 37  ALA A CB  1 
ATOM   304  N  N   . THR A 1 37  ? -6.78000  18.19400  70.72100  1.000 9.41381  ? 38  THR A N   1 
ATOM   305  C  CA  . THR A 1 37  ? -8.09500  18.83200  70.73000  1.000 9.52381  ? 38  THR A CA  1 
ATOM   306  C  C   . THR A 1 37  ? -9.14900  17.95700  70.06200  1.000 8.59381  ? 38  THR A C   1 
ATOM   307  O  O   . THR A 1 37  ? -10.31700 17.95000  70.48500  1.000 11.29381 ? 38  THR A O   1 
ATOM   308  C  CB  . THR A 1 37  ? -7.96800  20.17700  70.02100  1.000 11.43381 ? 38  THR A CB  1 
ATOM   309  O  OG1 . THR A 1 37  ? -7.03300  20.98700  70.74700  1.000 14.19381 ? 38  THR A OG1 1 
ATOM   310  C  CG2 . THR A 1 37  ? -9.31200  20.91300  69.91800  1.000 10.36381 ? 38  THR A CG2 1 
ATOM   311  N  N   . TYR A 1 38  ? -8.75500  17.19900  69.03900  1.000 8.73381  ? 39  TYR A N   1 
ATOM   312  C  CA  . TYR A 1 38  ? -9.63300  16.30000  68.30300  1.000 9.40381  ? 39  TYR A CA  1 
ATOM   313  C  C   . TYR A 1 38  ? -9.26500  14.83600  68.51200  1.000 9.58381  ? 39  TYR A C   1 
ATOM   314  O  O   . TYR A 1 38  ? -9.77700  13.96600  67.80100  1.000 12.90381 ? 39  TYR A O   1 
ATOM   315  C  CB  . TYR A 1 38  ? -9.61300  16.66600  66.81900  1.000 12.00381 ? 39  TYR A CB  1 
ATOM   316  C  CG  . TYR A 1 38  ? -9.78100  18.14900  66.63600  1.000 10.76381 ? 39  TYR A CG  1 
ATOM   317  C  CD1 . TYR A 1 38  ? -11.03200 18.74000  66.76800  1.000 15.11381 ? 39  TYR A CD1 1 
ATOM   318  C  CD2 . TYR A 1 38  ? -8.68500  18.97200  66.42300  1.000 13.72381 ? 39  TYR A CD2 1 
ATOM   319  C  CE1 . TYR A 1 38  ? -11.18900 20.10100  66.64200  1.000 14.11381 ? 39  TYR A CE1 1 
ATOM   320  C  CE2 . TYR A 1 38  ? -8.83800  20.34000  66.29400  1.000 17.25381 ? 39  TYR A CE2 1 
ATOM   321  C  CZ  . TYR A 1 38  ? -10.09700 20.89600  66.40400  1.000 17.11381 ? 39  TYR A CZ  1 
ATOM   322  O  OH  . TYR A 1 38  ? -10.25000 22.26100  66.28300  1.000 19.07381 ? 39  TYR A OH  1 
ATOM   323  N  N   . GLY A 1 39  ? -8.39400  14.54800  69.47500  1.000 8.92381  ? 40  GLY A N   1 
ATOM   324  C  CA  . GLY A 1 39  ? -7.93000  13.18800  69.69700  1.000 10.05381 ? 40  GLY A CA  1 
ATOM   325  C  C   . GLY A 1 39  ? -7.25800  12.55200  68.50100  1.000 10.04381 ? 40  GLY A C   1 
ATOM   326  O  O   . GLY A 1 39  ? -7.28600  11.32400  68.36600  1.000 9.20381  ? 40  GLY A O   1 
ATOM   327  N  N   . LYS A 1 40  ? -6.60500  13.34200  67.65500  1.000 9.14381  ? 41  LYS A N   1 
ATOM   328  C  CA  . LYS A 1 40  ? -6.24700  12.92300  66.30300  1.000 7.15381  ? 41  LYS A CA  1 
ATOM   329  C  C   . LYS A 1 40  ? -4.74300  12.72900  66.18200  1.000 9.99381  ? 41  LYS A C   1 
ATOM   330  O  O   . LYS A 1 40  ? -3.96800  13.60000  66.59500  1.000 11.11381 ? 41  LYS A O   1 
ATOM   331  C  CB  . LYS A 1 40  ? -6.65900  14.00000  65.30300  1.000 10.36381 ? 41  LYS A CB  1 
ATOM   332  C  CG  . LYS A 1 40  ? -6.39000  13.65500  63.86900  1.000 11.71381 ? 41  LYS A CG  1 
ATOM   333  C  CD  . LYS A 1 40  ? -6.86900  14.77700  62.94800  1.000 12.74381 ? 41  LYS A CD  1 
ATOM   334  C  CE  . LYS A 1 40  ? -6.83800  14.33100  61.50000  1.000 18.08381 ? 41  LYS A CE  1 
ATOM   335  N  NZ  . LYS A 1 40  ? -7.50700  15.32300  60.60800  1.000 17.40381 ? 41  LYS A NZ  1 
ATOM   336  N  N   . LEU A 1 41  ? -4.34400  11.59100  65.60400  1.000 8.02381  ? 42  LEU A N   1 
ATOM   337  C  CA  . LEU A 1 41  ? -2.95300  11.26200  65.32100  1.000 8.26381  ? 42  LEU A CA  1 
ATOM   338  C  C   . LEU A 1 41  ? -2.81100  10.83900  63.86900  1.000 9.24381  ? 42  LEU A C   1 
ATOM   339  O  O   . LEU A 1 41  ? -3.62100  10.05900  63.35700  1.000 10.14381 ? 42  LEU A O   1 
ATOM   340  C  CB  . LEU A 1 41  ? -2.48900  10.06400  66.17400  1.000 11.39381 ? 42  LEU A CB  1 
ATOM   341  C  CG  . LEU A 1 41  ? -2.35800  10.34500  67.66000  1.000 17.66381 ? 42  LEU A CG  1 
ATOM   342  C  CD1 . LEU A 1 41  ? -2.32100  9.05700   68.45900  1.000 17.20381 ? 42  LEU A CD1 1 
ATOM   343  C  CD2 . LEU A 1 41  ? -1.09200  11.13900  67.88200  1.000 17.67381 ? 42  LEU A CD2 1 
ATOM   344  N  N   . THR A 1 42  ? -1.77000  11.34600  63.21000  1.000 9.17381  ? 43  THR A N   1 
ATOM   345  C  CA  A THR A 1 42  ? -1.40600  10.92300  61.86400  0.620 9.94381  ? 43  THR A CA  1 
ATOM   346  C  CA  B THR A 1 42  ? -1.40300  10.91800  61.86500  0.380 9.99381  ? 43  THR A CA  1 
ATOM   347  C  C   . THR A 1 42  ? 0.08400   10.62100  61.88700  1.000 10.99381 ? 43  THR A C   1 
ATOM   348  O  O   . THR A 1 42  ? 0.88000   11.49600  62.23000  1.000 11.04381 ? 43  THR A O   1 
ATOM   349  C  CB  A THR A 1 42  ? -1.71700  12.02900  60.84800  0.620 12.10381 ? 43  THR A CB  1 
ATOM   350  C  CB  B THR A 1 42  ? -1.70700  12.00100  60.82500  0.380 12.06381 ? 43  THR A CB  1 
ATOM   351  O  OG1 A THR A 1 42  ? -3.04800  12.52300  61.06300  0.620 11.78381 ? 43  THR A OG1 1 
ATOM   352  O  OG1 B THR A 1 42  ? -1.14200  13.24900  61.24600  0.380 12.52381 ? 43  THR A OG1 1 
ATOM   353  C  CG2 A THR A 1 42  ? -1.62200  11.49700  59.43400  0.620 15.11381 ? 43  THR A CG2 1 
ATOM   354  C  CG2 B THR A 1 42  ? -3.20600  12.16500  60.64000  0.380 12.70381 ? 43  THR A CG2 1 
ATOM   355  N  N   . LEU A 1 43  ? 0.45600   9.38100   61.54500  1.000 7.91381  ? 44  LEU A N   1 
ATOM   356  C  CA  . LEU A 1 43  ? 1.83600   8.92800   61.66000  1.000 7.63381  ? 44  LEU A CA  1 
ATOM   357  C  C   . LEU A 1 43  ? 2.21800   8.04500   60.48900  1.000 8.39381  ? 44  LEU A C   1 
ATOM   358  O  O   . LEU A 1 43  ? 1.40600   7.26000   59.99700  1.000 10.72381 ? 44  LEU A O   1 
ATOM   359  C  CB  . LEU A 1 43  ? 2.04700   8.14500   62.96100  1.000 11.01381 ? 44  LEU A CB  1 
ATOM   360  C  CG  . LEU A 1 43  ? 1.85700   8.97400   64.23100  1.000 10.11381 ? 44  LEU A CG  1 
ATOM   361  C  CD1 . LEU A 1 43  ? 1.58700   8.08200   65.43100  1.000 16.47381 ? 44  LEU A CD1 1 
ATOM   362  C  CD2 . LEU A 1 43  ? 3.09300   9.85200   64.47900  1.000 11.50381 ? 44  LEU A CD2 1 
ATOM   363  N  N   . LYS A 1 44  ? 3.47400   8.16000   60.06000  1.000 7.31381  ? 45  LYS A N   1 
ATOM   364  C  CA  . LYS A 1 44  ? 4.02000   7.28100   59.03800  1.000 9.24381  ? 45  LYS A CA  1 
ATOM   365  C  C   . LYS A 1 44  ? 5.30400   6.68500   59.58000  1.000 8.47381  ? 45  LYS A C   1 
ATOM   366  O  O   . LYS A 1 44  ? 6.18800   7.42100   60.03100  1.000 9.24381  ? 45  LYS A O   1 
ATOM   367  C  CB  . LYS A 1 44  ? 4.29500   8.01900   57.71700  1.000 9.71381  ? 45  LYS A CB  1 
ATOM   368  C  CG  . LYS A 1 44  ? 5.02200   7.13200   56.70100  1.000 9.66381  ? 45  LYS A CG  1 
ATOM   369  C  CD  . LYS A 1 44  ? 5.27400   7.85000   55.37900  1.000 8.25381  ? 45  LYS A CD  1 
ATOM   370  C  CE  . LYS A 1 44  ? 6.10200   6.97300   54.46800  1.000 10.54381 ? 45  LYS A CE  1 
ATOM   371  N  NZ  . LYS A 1 44  ? 6.44900   7.66300   53.19500  1.000 14.86381 ? 45  LYS A NZ  1 
ATOM   372  N  N   . PHE A 1 45  ? 5.38900   5.35400   59.54800  1.000 8.47381  ? 46  PHE A N   1 
ATOM   373  C  CA  . PHE A 1 45  ? 6.52000   4.60200   60.07000  1.000 7.96381  ? 46  PHE A CA  1 
ATOM   374  C  C   . PHE A 1 45  ? 7.26100   3.93400   58.92400  1.000 10.28381 ? 46  PHE A C   1 
ATOM   375  O  O   . PHE A 1 45  ? 6.64500   3.43900   57.97900  1.000 10.15381 ? 46  PHE A O   1 
ATOM   376  C  CB  . PHE A 1 45  ? 6.02800   3.51500   61.02900  1.000 8.02381  ? 46  PHE A CB  1 
ATOM   377  C  CG  . PHE A 1 45  ? 5.16600   4.04800   62.11900  1.000 7.25381  ? 46  PHE A CG  1 
ATOM   378  C  CD1 . PHE A 1 45  ? 5.73900   4.60600   63.25100  1.000 6.98381  ? 46  PHE A CD1 1 
ATOM   379  C  CD2 . PHE A 1 45  ? 3.78600   4.04600   61.99700  1.000 8.91381  ? 46  PHE A CD2 1 
ATOM   380  C  CE1 . PHE A 1 45  ? 4.96600   5.13600   64.24900  1.000 8.50381  ? 46  PHE A CE1 1 
ATOM   381  C  CE2 . PHE A 1 45  ? 2.99700   4.56500   63.00200  1.000 10.48381 ? 46  PHE A CE2 1 
ATOM   382  C  CZ  . PHE A 1 45  ? 3.57800   5.11700   64.12400  1.000 8.36381  ? 46  PHE A CZ  1 
ATOM   383  N  N   . ILE A 1 46  ? 8.58600   3.90600   59.02200  1.000 9.81381  ? 47  ILE A N   1 
ATOM   384  C  CA  A ILE A 1 46  ? 9.45200   3.30200   58.01500  0.350 9.45381  ? 47  ILE A CA  1 
ATOM   385  C  CA  B ILE A 1 46  ? 9.43400   3.28600   58.01500  0.650 9.37381  ? 47  ILE A CA  1 
ATOM   386  C  C   . ILE A 1 46  ? 10.37800  2.33000   58.72700  1.000 8.75381  ? 47  ILE A C   1 
ATOM   387  O  O   . ILE A 1 46  ? 10.99400  2.69400   59.73300  1.000 8.73381  ? 47  ILE A O   1 
ATOM   388  C  CB  A ILE A 1 46  ? 10.29300  4.38000   57.30800  0.350 10.92381 ? 47  ILE A CB  1 
ATOM   389  C  CB  B ILE A 1 46  ? 10.22100  4.34800   57.22700  0.650 11.02381 ? 47  ILE A CB  1 
ATOM   390  C  CG1 A ILE A 1 46  ? 9.40100   5.29800   56.47100  0.350 13.43381 ? 47  ILE A CG1 1 
ATOM   391  C  CG1 B ILE A 1 46  ? 9.25200   5.30400   56.52400  0.650 13.09381 ? 47  ILE A CG1 1 
ATOM   392  C  CG2 A ILE A 1 46  ? 11.39400  3.73700   56.47500  0.350 11.13381 ? 47  ILE A CG2 1 
ATOM   393  C  CG2 B ILE A 1 46  ? 11.14100  3.68600   56.22500  0.650 12.25381 ? 47  ILE A CG2 1 
ATOM   394  C  CD1 A ILE A 1 46  ? 9.12200   4.78000   55.09300  0.350 7.80381  ? 47  ILE A CD1 1 
ATOM   395  C  CD1 B ILE A 1 46  ? 9.88300   6.62500   56.09600  0.650 12.02381 ? 47  ILE A CD1 1 
ATOM   396  N  N   . CYS A 1 47  ? 10.47400  1.09300   58.22100  1.000 8.48381  ? 48  CYS A N   1 
ATOM   397  C  CA  . CYS A 1 47  ? 11.47400  0.16800   58.74900  1.000 8.59381  ? 48  CYS A CA  1 
ATOM   398  C  C   . CYS A 1 47  ? 12.80200  0.52200   58.10000  1.000 12.75381 ? 48  CYS A C   1 
ATOM   399  O  O   . CYS A 1 47  ? 12.95400  0.41100   56.88100  1.000 13.61381 ? 48  CYS A O   1 
ATOM   400  C  CB  . CYS A 1 47  ? 11.09400  -1.28700  58.49000  1.000 9.09381  ? 48  CYS A CB  1 
ATOM   401  S  SG  . CYS A 1 47  ? 12.35600  -2.40300  59.12100  1.000 11.05381 ? 48  CYS A SG  1 
ATOM   402  N  N   . THR A 1 48  ? 13.75600  0.97300   58.90600  1.000 10.57381 ? 49  THR A N   1 
ATOM   403  C  CA  . THR A 1 48  ? 15.00900  1.48900   58.37200  1.000 12.46381 ? 49  THR A CA  1 
ATOM   404  C  C   . THR A 1 48  ? 16.06100  0.40800   58.20300  1.000 11.66381 ? 49  THR A C   1 
ATOM   405  O  O   . THR A 1 48  ? 17.11400  0.67600   57.62300  1.000 13.83381 ? 49  THR A O   1 
ATOM   406  C  CB  . THR A 1 48  ? 15.56400  2.58000   59.28500  1.000 9.42381  ? 49  THR A CB  1 
ATOM   407  O  OG1 . THR A 1 48  ? 15.78800  2.03200   60.59300  1.000 10.98381 ? 49  THR A OG1 1 
ATOM   408  C  CG2 . THR A 1 48  ? 14.59800  3.76100   59.35300  1.000 12.36381 ? 49  THR A CG2 1 
ATOM   409  N  N   . THR A 1 49  ? 15.80100  -0.79900  58.68700  1.000 9.83381  ? 50  THR A N   1 
ATOM   410  C  CA  . THR A 1 49  ? 16.74800  -1.89500  58.57200  1.000 9.78381  ? 50  THR A CA  1 
ATOM   411  C  C   . THR A 1 49  ? 16.41300  -2.85900  57.44100  1.000 15.41381 ? 50  THR A C   1 
ATOM   412  O  O   . THR A 1 49  ? 17.13700  -3.84000  57.25100  1.000 17.30381 ? 50  THR A O   1 
ATOM   413  C  CB  . THR A 1 49  ? 16.82500  -2.63500  59.90400  1.000 11.04381 ? 50  THR A CB  1 
ATOM   414  O  OG1 . THR A 1 49  ? 15.48800  -2.87100  60.38700  1.000 11.74381 ? 50  THR A OG1 1 
ATOM   415  C  CG2 . THR A 1 49  ? 17.56700  -1.79100  60.91700  1.000 10.58381 ? 50  THR A CG2 1 
ATOM   416  N  N   . GLY A 1 50  ? 15.35600  -2.59500  56.67700  1.000 12.79381 ? 51  GLY A N   1 
ATOM   417  C  CA  . GLY A 1 50  ? 14.94200  -3.50100  55.62700  1.000 12.25381 ? 51  GLY A CA  1 
ATOM   418  C  C   . GLY A 1 50  ? 13.49000  -3.88900  55.78300  1.000 9.96381  ? 51  GLY A C   1 
ATOM   419  O  O   . GLY A 1 50  ? 12.63300  -3.02700  56.01100  1.000 12.93381 ? 51  GLY A O   1 
ATOM   420  N  N   . LYS A 1 51  ? 13.19200  -5.17600  55.65800  1.000 11.94381 ? 52  LYS A N   1 
ATOM   421  C  CA  . LYS A 1 51  ? 11.83000  -5.64200  55.84000  1.000 13.80381 ? 52  LYS A CA  1 
ATOM   422  C  C   . LYS A 1 51  ? 11.54600  -5.83300  57.32100  1.000 12.27381 ? 52  LYS A C   1 
ATOM   423  O  O   . LYS A 1 51  ? 12.36200  -6.39100  58.05500  1.000 12.73381 ? 52  LYS A O   1 
ATOM   424  C  CB  . LYS A 1 51  ? 11.62600  -6.97200  55.11300  1.000 19.74381 ? 52  LYS A CB  1 
ATOM   425  C  CG  . LYS A 1 51  ? 10.23100  -7.55000  55.28600  1.000 24.15381 ? 52  LYS A CG  1 
ATOM   426  C  CD  . LYS A 1 51  ? 10.06700  -8.86000  54.53300  1.000 38.55381 ? 52  LYS A CD  1 
ATOM   427  C  CE  . LYS A 1 51  ? 8.73500   -9.51800  54.86700  1.000 63.46381 ? 52  LYS A CE  1 
ATOM   428  N  NZ  . LYS A 1 51  ? 7.57800   -8.61500  54.59800  1.000 54.65381 ? 52  LYS A NZ  1 
ATOM   429  N  N   . LEU A 1 52  ? 10.37200  -5.37900  57.75300  1.000 11.44381 ? 53  LEU A N   1 
ATOM   430  C  CA  . LEU A 1 52  ? 9.98200   -5.56600  59.14700  1.000 10.22381 ? 53  LEU A CA  1 
ATOM   431  C  C   . LEU A 1 52  ? 9.73100   -7.05200  59.39300  1.000 9.68381  ? 53  LEU A C   1 
ATOM   432  O  O   . LEU A 1 52  ? 8.97500   -7.68000  58.64100  1.000 13.53381 ? 53  LEU A O   1 
ATOM   433  C  CB  . LEU A 1 52  ? 8.71900   -4.74100  59.43500  1.000 7.99381  ? 53  LEU A CB  1 
ATOM   434  C  CG  . LEU A 1 52  ? 8.34600   -4.60900  60.90600  1.000 9.83381  ? 53  LEU A CG  1 
ATOM   435  C  CD1 . LEU A 1 52  ? 9.33200   -3.71000  61.64300  1.000 9.53381  ? 53  LEU A CD1 1 
ATOM   436  C  CD2 . LEU A 1 52  ? 6.91500   -4.09700  61.04300  1.000 9.19381  ? 53  LEU A CD2 1 
ATOM   437  N  N   . PRO A 1 53  ? 10.36200  -7.65700  60.40300  1.000 11.39381 ? 54  PRO A N   1 
ATOM   438  C  CA  . PRO A 1 53  ? 10.24500  -9.10900  60.59400  1.000 9.38381  ? 54  PRO A CA  1 
ATOM   439  C  C   . PRO A 1 53  ? 8.99900   -9.54600  61.34900  1.000 11.10381 ? 54  PRO A C   1 
ATOM   440  O  O   . PRO A 1 53  ? 8.84200   -10.74100 61.62100  1.000 11.36381 ? 54  PRO A O   1 
ATOM   441  C  CB  . PRO A 1 53  ? 11.51400  -9.44700  61.39800  1.000 10.68381 ? 54  PRO A CB  1 
ATOM   442  C  CG  . PRO A 1 53  ? 11.77500  -8.22400  62.17900  1.000 12.42381 ? 54  PRO A CG  1 
ATOM   443  C  CD  . PRO A 1 53  ? 11.37400  -7.06100  61.29400  1.000 11.84381 ? 54  PRO A CD  1 
ATOM   444  N  N   . VAL A 1 54  ? 8.13300   -8.61100  61.72100  1.000 9.01381  ? 55  VAL A N   1 
ATOM   445  C  CA  . VAL A 1 54  ? 6.83200   -8.91800  62.30900  1.000 9.34381  ? 55  VAL A CA  1 
ATOM   446  C  C   . VAL A 1 54  ? 5.79800   -8.11000  61.54400  1.000 9.03381  ? 55  VAL A C   1 
ATOM   447  O  O   . VAL A 1 54  ? 6.15000   -7.16400  60.82300  1.000 9.38381  ? 55  VAL A O   1 
ATOM   448  C  CB  . VAL A 1 54  ? 6.78600   -8.57000  63.81600  1.000 7.49381  ? 55  VAL A CB  1 
ATOM   449  C  CG1 . VAL A 1 54  ? 7.80200   -9.37800  64.59900  1.000 10.14381 ? 55  VAL A CG1 1 
ATOM   450  C  CG2 . VAL A 1 54  ? 6.98800   -7.06100  64.03300  1.000 9.20381  ? 55  VAL A CG2 1 
ATOM   451  N  N   . PRO A 1 55  ? 4.51800   -8.44100  61.67700  1.000 8.93381  ? 56  PRO A N   1 
ATOM   452  C  CA  . PRO A 1 55  ? 3.50200   -7.66700  60.95600  1.000 7.12381  ? 56  PRO A CA  1 
ATOM   453  C  C   . PRO A 1 55  ? 3.34300   -6.27900  61.54800  1.000 8.72381  ? 56  PRO A C   1 
ATOM   454  O  O   . PRO A 1 55  ? 3.30100   -6.11100  62.76900  1.000 9.33381  ? 56  PRO A O   1 
ATOM   455  C  CB  . PRO A 1 55  ? 2.22300   -8.49500  61.14600  1.000 8.89381  ? 56  PRO A CB  1 
ATOM   456  C  CG  . PRO A 1 55  ? 2.72000   -9.89200  61.40800  1.000 9.82381  ? 56  PRO A CG  1 
ATOM   457  C  CD  . PRO A 1 55  ? 3.97300   -9.70300  62.21400  1.000 8.28381  ? 56  PRO A CD  1 
ATOM   458  N  N   . TRP A 1 56  ? 3.24300   -5.28200  60.66100  1.000 8.79381  ? 57  TRP A N   1 
ATOM   459  C  CA  . TRP A 1 56  ? 3.01200   -3.90000  61.08200  1.000 7.50381  ? 57  TRP A CA  1 
ATOM   460  C  C   . TRP A 1 56  ? 1.90500   -3.74600  62.11300  1.000 7.97381  ? 57  TRP A C   1 
ATOM   461  O  O   . TRP A 1 56  ? 2.11200   -3.01400  63.09500  1.000 8.82381  ? 57  TRP A O   1 
ATOM   462  C  CB  . TRP A 1 56  ? 2.74300   -3.00300  59.86300  1.000 9.13381  ? 57  TRP A CB  1 
ATOM   463  C  CG  . TRP A 1 56  ? 3.96800   -2.64500  59.11300  1.000 8.58381  ? 57  TRP A CG  1 
ATOM   464  C  CD1 . TRP A 1 56  ? 4.35300   -3.11300  57.89300  1.000 9.92381  ? 57  TRP A CD1 1 
ATOM   465  C  CD2 . TRP A 1 56  ? 4.98500   -1.73100  59.53500  1.000 9.24381  ? 57  TRP A CD2 1 
ATOM   466  N  NE1 . TRP A 1 56  ? 5.55700   -2.55200  57.52700  1.000 9.80381  ? 57  TRP A NE1 1 
ATOM   467  C  CE2 . TRP A 1 56  ? 5.96700   -1.69800  58.51600  1.000 8.16381  ? 57  TRP A CE2 1 
ATOM   468  C  CE3 . TRP A 1 56  ? 5.16600   -0.94200  60.67600  1.000 7.27381  ? 57  TRP A CE3 1 
ATOM   469  C  CZ2 . TRP A 1 56  ? 7.11700   -0.91300  58.60900  1.000 9.82381  ? 57  TRP A CZ2 1 
ATOM   470  C  CZ3 . TRP A 1 56  ? 6.30100   -0.16000  60.76100  1.000 7.12381  ? 57  TRP A CZ3 1 
ATOM   471  C  CH2 . TRP A 1 56  ? 7.26300   -0.14600  59.73500  1.000 6.93381  ? 57  TRP A CH2 1 
ATOM   472  N  N   . PRO A 1 57  ? 0.72800   -4.36600  61.96200  1.000 9.04381  ? 58  PRO A N   1 
ATOM   473  C  CA  . PRO A 1 57  ? -0.31600  -4.15900  62.97800  1.000 7.28381  ? 58  PRO A CA  1 
ATOM   474  C  C   . PRO A 1 57  ? 0.12600   -4.49900  64.38800  1.000 7.10381  ? 58  PRO A C   1 
ATOM   475  O  O   . PRO A 1 57  ? -0.38100  -3.88700  65.34000  1.000 8.07381  ? 58  PRO A O   1 
ATOM   476  C  CB  . PRO A 1 57  ? -1.45100  -5.07900  62.50800  1.000 8.03381  ? 58  PRO A CB  1 
ATOM   477  C  CG  . PRO A 1 57  ? -1.26400  -5.14600  61.00500  1.000 9.25381  ? 58  PRO A CG  1 
ATOM   478  C  CD  . PRO A 1 57  ? 0.23800   -5.20400  60.84500  1.000 9.54381  ? 58  PRO A CD  1 
ATOM   479  N  N   . THR A 1 58  ? 1.04300   -5.46600  64.55600  1.000 8.75381  ? 59  THR A N   1 
ATOM   480  C  CA  . THR A 1 58  ? 1.42900   -5.86600  65.90600  1.000 7.43381  ? 59  THR A CA  1 
ATOM   481  C  C   . THR A 1 58  ? 2.18800   -4.78100  66.65100  1.000 7.92381  ? 59  THR A C   1 
ATOM   482  O  O   . THR A 1 58  ? 2.34600   -4.90300  67.87100  1.000 7.82381  ? 59  THR A O   1 
ATOM   483  C  CB  . THR A 1 58  ? 2.26500   -7.14500  65.90700  1.000 10.09381 ? 59  THR A CB  1 
ATOM   484  O  OG1 . THR A 1 58  ? 3.56300   -6.88400  65.35500  1.000 9.11381  ? 59  THR A OG1 1 
ATOM   485  C  CG2 . THR A 1 58  ? 1.57700   -8.22400  65.10300  1.000 9.42381  ? 59  THR A CG2 1 
ATOM   486  N  N   . LEU A 1 59  ? 2.64200   -3.72900  65.96200  1.000 6.98381  ? 60  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 59  ? 3.40900   -2.65200  66.57700  1.000 8.16381  ? 60  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 59  ? 2.59900   -1.38100  66.79300  1.000 6.87381  ? 60  LEU A C   1 
ATOM   489  O  O   . LEU A 1 59  ? 3.12600   -0.41500  67.35600  1.000 7.48381  ? 60  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 59  ? 4.64300   -2.33500  65.72600  1.000 7.74381  ? 60  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 59  ? 5.61000   -3.50900  65.55500  1.000 6.68381  ? 60  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 59  ? 6.85000   -3.10600  64.75600  1.000 10.66381 ? 60  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 59  ? 6.01200   -4.04500  66.91100  1.000 9.94381  ? 60  LEU A CD2 1 
ATOM   494  N  N   . VAL A 1 60  ? 1.33600   -1.34800  66.36700  1.000 6.65381  ? 61  VAL A N   1 
ATOM   495  C  CA  . VAL A 1 60  ? 0.55100   -0.11500  66.44400  1.000 7.30381  ? 61  VAL A CA  1 
ATOM   496  C  C   . VAL A 1 60  ? 0.47300   0.41200   67.87500  1.000 7.82381  ? 61  VAL A C   1 
ATOM   497  O  O   . VAL A 1 60  ? 0.68900   1.60400   68.12500  1.000 7.75381  ? 61  VAL A O   1 
ATOM   498  C  CB  . VAL A 1 60  ? -0.84000  -0.34400  65.82900  1.000 7.08381  ? 61  VAL A CB  1 
ATOM   499  C  CG1 . VAL A 1 60  ? -1.80300  0.77500   66.18100  1.000 6.75381  ? 61  VAL A CG1 1 
ATOM   500  C  CG2 . VAL A 1 60  ? -0.71800  -0.48600  64.31800  1.000 9.01381  ? 61  VAL A CG2 1 
ATOM   501  N  N   . THR A 1 61  ? 0.14100   -0.45200  68.84000  1.000 7.47381  ? 62  THR A N   1 
ATOM   502  C  CA  . THR A 1 61  ? -0.00500  0.06200   70.20300  1.000 7.46381  ? 62  THR A CA  1 
ATOM   503  C  C   . THR A 1 61  ? 1.32300   0.52400   70.77800  1.000 6.66381  ? 62  THR A C   1 
ATOM   504  O  O   . THR A 1 61  ? 1.34700   1.39300   71.65300  1.000 8.42381  ? 62  THR A O   1 
ATOM   505  C  CB  . THR A 1 61  ? -0.58800  -0.99200  71.14100  1.000 7.12381  ? 62  THR A CB  1 
ATOM   506  O  OG1 . THR A 1 61  ? 0.21500   -2.17800  71.07600  1.000 7.40381  ? 62  THR A OG1 1 
ATOM   507  C  CG2 . THR A 1 61  ? -2.01600  -1.31800  70.78000  1.000 7.95381  ? 62  THR A CG2 1 
ATOM   508  N  N   . THR A 1 62  ? 2.42900   -0.08800  70.35000  1.000 6.47381  ? 63  THR A N   1 
ATOM   509  C  CA  . THR A 1 62  ? 3.74200   0.30800   70.85000  1.000 6.10381  ? 63  THR A CA  1 
ATOM   510  C  C   . THR A 1 62  ? 4.15200   1.66700   70.29600  1.000 7.41381  ? 63  THR A C   1 
ATOM   511  O  O   . THR A 1 62  ? 4.65300   2.51900   71.04200  1.000 7.64381  ? 63  THR A O   1 
ATOM   512  C  CB  . THR A 1 62  ? 4.76600   -0.76900  70.48900  1.000 5.32381  ? 63  THR A CB  1 
ATOM   513  O  OG1 . THR A 1 62  ? 4.41800   -1.98700  71.15900  1.000 6.95381  ? 63  THR A OG1 1 
ATOM   514  C  CG2 . THR A 1 62  ? 6.14500   -0.36700  70.95800  1.000 9.02381  ? 63  THR A CG2 1 
ATOM   515  N  N   . PHE A 1 63  ? 3.94300   1.88300   68.99800  1.000 7.07381  ? 64  PHE A N   1 
ATOM   516  C  CA  . PHE A 1 63  ? 4.25800   3.16400   68.36700  1.000 5.94381  ? 64  PHE A CA  1 
ATOM   517  C  C   . PHE A 1 63  ? 3.31000   4.23900   68.86600  1.000 6.79381  ? 64  PHE A C   1 
ATOM   518  O  O   . PHE A 1 63  ? 3.71000   5.38900   69.08700  1.000 8.89381  ? 64  PHE A O   1 
ATOM   519  C  CB  . PHE A 1 63  ? 4.03000   3.09400   66.86400  1.000 9.27381  ? 64  PHE A CB  1 
ATOM   520  C  CG  . PHE A 1 63  ? 4.96400   2.19500   66.11700  1.000 5.65381  ? 64  PHE A CG  1 
ATOM   521  C  CD1 . PHE A 1 63  ? 6.30100   2.04600   66.49100  1.000 6.56381  ? 64  PHE A CD1 1 
ATOM   522  C  CD2 . PHE A 1 63  ? 4.49300   1.52600   64.98300  1.000 7.89381  ? 64  PHE A CD2 1 
ATOM   523  C  CE1 . PHE A 1 63  ? 7.14800   1.21500   65.74100  1.000 6.80381  ? 64  PHE A CE1 1 
ATOM   524  C  CE2 . PHE A 1 63  ? 5.31500   0.70100   64.24000  1.000 7.57381  ? 64  PHE A CE2 1 
ATOM   525  C  CZ  . PHE A 1 63  ? 6.64000   0.53600   64.61900  1.000 7.74381  ? 64  PHE A CZ  1 
HETATM 526  N  N1  . GYS A 1 64  ? 2.03500   3.87100   68.99500  1.000 7.02381  ? 66  GYS A N1  1 
HETATM 527  O  OG1 . GYS A 1 64  ? -0.80100  6.14400   68.30000  1.000 9.28381  ? 66  GYS A OG1 1 
HETATM 528  C  CB1 . GYS A 1 64  ? 0.08600   5.04500   68.03900  1.000 7.17381  ? 66  GYS A CB1 1 
HETATM 529  C  CA1 . GYS A 1 64  ? 0.97700   4.81700   69.27300  1.000 9.37381  ? 66  GYS A CA1 1 
HETATM 530  C  C1  . GYS A 1 64  ? 0.20000   4.24900   70.43500  1.000 7.47381  ? 66  GYS A C1  1 
HETATM 531  N  N2  . GYS A 1 64  ? -0.96500  3.66200   70.40800  1.000 8.88381  ? 66  GYS A N2  1 
HETATM 532  N  N3  . GYS A 1 64  ? 0.73900   4.30900   71.71500  1.000 7.91381  ? 66  GYS A N3  1 
HETATM 533  C  C2  . GYS A 1 64  ? -0.12700  3.72000   72.59200  1.000 7.13381  ? 66  GYS A C2  1 
HETATM 534  O  O2  . GYS A 1 64  ? 0.06400   3.59000   73.82100  1.000 8.91381  ? 66  GYS A O2  1 
HETATM 535  C  CA2 . GYS A 1 64  ? -1.21900  3.29800   71.72700  1.000 8.21381  ? 66  GYS A CA2 1 
HETATM 536  C  CA3 . GYS A 1 64  ? 2.04000   4.82600   72.06800  1.000 10.66381 ? 66  GYS A CA3 1 
HETATM 537  C  CB2 . GYS A 1 64  ? -2.31000  2.60600   72.23200  1.000 8.40381  ? 66  GYS A CB2 1 
HETATM 538  C  CG2 . GYS A 1 64  ? -3.37600  1.95000   71.47800  1.000 7.98381  ? 66  GYS A CG2 1 
HETATM 539  C  CD1 . GYS A 1 64  ? -3.52900  1.98600   70.09100  1.000 10.29381 ? 66  GYS A CD1 1 
HETATM 540  C  CD2 . GYS A 1 64  ? -4.35800  1.23400   72.20700  1.000 9.72381  ? 66  GYS A CD2 1 
HETATM 541  C  CE1 . GYS A 1 64  ? -4.57700  1.37900   69.44900  1.000 10.13381 ? 66  GYS A CE1 1 
HETATM 542  C  CE2 . GYS A 1 64  ? -5.41800  0.61300   71.58800  1.000 10.03381 ? 66  GYS A CE2 1 
HETATM 543  C  CZ  . GYS A 1 64  ? -5.54900  0.66800   70.21600  1.000 7.48381  ? 66  GYS A CZ  1 
HETATM 544  O  OH  . GYS A 1 64  ? -6.56900  0.10300   69.59400  1.000 9.73381  ? 66  GYS A OH  1 
HETATM 545  C  C3  . GYS A 1 64  ? 2.14200   6.18300   72.72700  1.000 7.79381  ? 66  GYS A C3  1 
HETATM 546  O  O3  . GYS A 1 64  ? 3.17500   6.45000   73.36500  1.000 8.29381  ? 66  GYS A O3  1 
ATOM   547  N  N   . VAL A 1 65  ? 1.33800   7.09700   72.19800  1.000 7.14381  ? 68  VAL A N   1 
ATOM   548  C  CA  . VAL A 1 65  ? 1.46600   8.51500   72.52500  1.000 5.92381  ? 68  VAL A CA  1 
ATOM   549  C  C   . VAL A 1 65  ? 0.10600   8.98300   73.02700  1.000 6.54381  ? 68  VAL A C   1 
ATOM   550  O  O   . VAL A 1 65  ? -0.53900  9.89600   72.46000  1.000 7.39381  ? 68  VAL A O   1 
ATOM   551  C  CB  . VAL A 1 65  ? 2.06300   9.35300   71.36200  1.000 6.87381  ? 68  VAL A CB  1 
ATOM   552  C  CG1 . VAL A 1 65  ? 3.54800   8.99200   71.17900  1.000 7.75381  ? 68  VAL A CG1 1 
ATOM   553  C  CG2 . VAL A 1 65  ? 1.30900   9.11900   70.06000  1.000 8.46381  ? 68  VAL A CG2 1 
ATOM   554  N  N   . GLN A 1 66  ? -0.30900  8.35400   74.12600  1.000 8.99381  ? 69  GLN A N   1 
ATOM   555  C  CA  . GLN A 1 66  ? -1.66200  8.54000   74.63200  1.000 7.23381  ? 69  GLN A CA  1 
ATOM   556  C  C   . GLN A 1 66  ? -1.88900  9.92400   75.21700  1.000 8.05381  ? 69  GLN A C   1 
ATOM   557  O  O   . GLN A 1 66  ? -3.02900  10.23700  75.57600  1.000 8.88381  ? 69  GLN A O   1 
ATOM   558  C  CB  . GLN A 1 66  ? -2.02300  7.42800   75.62100  1.000 10.04381 ? 69  GLN A CB  1 
ATOM   559  C  CG  . GLN A 1 66  ? -2.09600  6.07000   74.94800  1.000 10.84381 ? 69  GLN A CG  1 
ATOM   560  C  CD  . GLN A 1 66  ? -2.19200  4.91700   75.91800  1.000 10.69381 ? 69  GLN A CD  1 
ATOM   561  O  OE1 . GLN A 1 66  ? -1.42800  4.83500   76.88000  1.000 12.23381 ? 69  GLN A OE1 1 
ATOM   562  N  NE2 . GLN A 1 66  ? -3.11000  3.98100   75.63700  1.000 13.99381 ? 69  GLN A NE2 1 
ATOM   563  N  N   . CYS A 1 67  ? -0.84300  10.74800  75.30700  1.000 7.81381  ? 70  CYS A N   1 
ATOM   564  C  CA  . CYS A 1 67  ? -1.00700  12.16900  75.57800  1.000 9.28381  ? 70  CYS A CA  1 
ATOM   565  C  C   . CYS A 1 67  ? -1.81200  12.87600  74.49900  1.000 9.07381  ? 70  CYS A C   1 
ATOM   566  O  O   . CYS A 1 67  ? -2.24700  14.01100  74.72600  1.000 8.54381  ? 70  CYS A O   1 
ATOM   567  C  CB  . CYS A 1 67  ? 0.36400   12.83100  75.75700  1.000 8.90381  ? 70  CYS A CB  1 
ATOM   568  S  SG  . CYS A 1 67  ? 1.58900   12.40200  74.48400  1.000 8.96381  ? 70  CYS A SG  1 
ATOM   569  N  N   . PHE A 1 68  ? -2.02900  12.24800  73.34100  1.000 7.27381  ? 71  PHE A N   1 
ATOM   570  C  CA  . PHE A 1 68  ? -2.85400  12.85900  72.30100  1.000 7.63381  ? 71  PHE A CA  1 
ATOM   571  C  C   . PHE A 1 68  ? -4.32200  12.44000  72.36600  1.000 9.54381  ? 71  PHE A C   1 
ATOM   572  O  O   . PHE A 1 68  ? -5.10700  12.82700  71.49200  1.000 9.94381  ? 71  PHE A O   1 
ATOM   573  C  CB  . PHE A 1 68  ? -2.23700  12.62200  70.92200  1.000 8.10381  ? 71  PHE A CB  1 
ATOM   574  C  CG  . PHE A 1 68  ? -0.97800  13.39600  70.71100  1.000 7.49381  ? 71  PHE A CG  1 
ATOM   575  C  CD1 . PHE A 1 68  ? -1.02800  14.76200  70.47500  1.000 9.38381  ? 71  PHE A CD1 1 
ATOM   576  C  CD2 . PHE A 1 68  ? 0.25600   12.77100  70.77900  1.000 7.37381  ? 71  PHE A CD2 1 
ATOM   577  C  CE1 . PHE A 1 68  ? 0.13000   15.49200  70.29400  1.000 10.78381 ? 71  PHE A CE1 1 
ATOM   578  C  CE2 . PHE A 1 68  ? 1.42900   13.49600  70.60500  1.000 8.49381  ? 71  PHE A CE2 1 
ATOM   579  C  CZ  . PHE A 1 68  ? 1.37000   14.85900  70.36200  1.000 8.12381  ? 71  PHE A CZ  1 
ATOM   580  N  N   . SER A 1 69  ? -4.70500  11.67800  73.39000  1.000 9.89381  ? 72  SER A N   1 
ATOM   581  C  CA  . SER A 1 69  ? -6.11100  11.40100  73.63100  1.000 8.79381  ? 72  SER A CA  1 
ATOM   582  C  C   . SER A 1 69  ? -6.86300  12.70300  73.84800  1.000 8.21381  ? 72  SER A C   1 
ATOM   583  O  O   . SER A 1 69  ? -6.35000  13.64100  74.46000  1.000 9.24381  ? 72  SER A O   1 
ATOM   584  C  CB  . SER A 1 69  ? -6.25200  10.56300  74.89700  1.000 10.59381 ? 72  SER A CB  1 
ATOM   585  O  OG  . SER A 1 69  ? -5.51900  9.36000   74.80300  1.000 12.44381 ? 72  SER A OG  1 
ATOM   586  N  N   . ARG A 1 70  ? -8.10400  12.75500  73.36900  1.000 7.75381  ? 73  ARG A N   1 
ATOM   587  C  CA  . ARG A 1 70  ? -8.96500  13.87500  73.72800  1.000 8.88381  ? 73  ARG A CA  1 
ATOM   588  C  C   . ARG A 1 70  ? -9.62600  13.56900  75.06100  1.000 7.51381  ? 73  ARG A C   1 
ATOM   589  O  O   . ARG A 1 70  ? -10.47200 12.67000  75.15500  1.000 9.15381  ? 73  ARG A O   1 
ATOM   590  C  CB  . ARG A 1 70  ? -10.02300 14.14000  72.66800  1.000 11.57381 ? 73  ARG A CB  1 
ATOM   591  C  CG  . ARG A 1 70  ? -10.88800 15.31800  73.05900  1.000 11.45381 ? 73  ARG A CG  1 
ATOM   592  C  CD  . ARG A 1 70  ? -11.92300 15.63100  72.02300  1.000 10.99381 ? 73  ARG A CD  1 
ATOM   593  N  NE  . ARG A 1 70  ? -13.02700 14.67600  71.99800  1.000 12.03381 ? 73  ARG A NE  1 
ATOM   594  C  CZ  . ARG A 1 70  ? -14.07500 14.72800  72.81100  1.000 13.52381 ? 73  ARG A CZ  1 
ATOM   595  N  NH1 . ARG A 1 70  ? -14.12900 15.58500  73.82100  1.000 13.54381 ? 73  ARG A NH1 1 
ATOM   596  N  NH2 . ARG A 1 70  ? -15.10400 13.90800  72.59700  1.000 14.33381 ? 73  ARG A NH2 1 
ATOM   597  N  N   . TYR A 1 71  ? -9.24200  14.31000  76.09600  1.000 8.86381  ? 74  TYR A N   1 
ATOM   598  C  CA  . TYR A 1 71  ? -9.95800  14.23700  77.35600  1.000 9.98381  ? 74  TYR A CA  1 
ATOM   599  C  C   . TYR A 1 71  ? -11.02600 15.31800  77.36500  1.000 12.33381 ? 74  TYR A C   1 
ATOM   600  O  O   . TYR A 1 71  ? -10.69000 16.50400  77.24500  1.000 11.93381 ? 74  TYR A O   1 
ATOM   601  C  CB  . TYR A 1 71  ? -9.00800  14.41000  78.53600  1.000 9.97381  ? 74  TYR A CB  1 
ATOM   602  C  CG  . TYR A 1 71  ? -8.39300  13.09500  78.95000  1.000 9.89381  ? 74  TYR A CG  1 
ATOM   603  C  CD1 . TYR A 1 71  ? -7.37500  12.51900  78.20100  1.000 9.09381  ? 74  TYR A CD1 1 
ATOM   604  C  CD2 . TYR A 1 71  ? -8.85400  12.41200  80.07400  1.000 8.99381  ? 74  TYR A CD2 1 
ATOM   605  C  CE1 . TYR A 1 71  ? -6.82800  11.30100  78.55800  1.000 9.40381  ? 74  TYR A CE1 1 
ATOM   606  C  CE2 . TYR A 1 71  ? -8.30400  11.20600  80.45400  1.000 8.89381  ? 74  TYR A CE2 1 
ATOM   607  C  CZ  . TYR A 1 71  ? -7.29000  10.65300  79.68400  1.000 8.24381  ? 74  TYR A CZ  1 
ATOM   608  O  OH  . TYR A 1 71  ? -6.74200  9.44200   80.04100  1.000 10.00381 ? 74  TYR A OH  1 
ATOM   609  N  N   . PRO A 1 72  ? -12.30300 14.95700  77.44100  1.000 11.87381 ? 75  PRO A N   1 
ATOM   610  C  CA  . PRO A 1 72  ? -13.35000 15.96700  77.59600  1.000 10.19381 ? 75  PRO A CA  1 
ATOM   611  C  C   . PRO A 1 72  ? -12.99100 16.91300  78.72600  1.000 12.35381 ? 75  PRO A C   1 
ATOM   612  O  O   . PRO A 1 72  ? -12.34400 16.52500  79.69900  1.000 11.71381 ? 75  PRO A O   1 
ATOM   613  C  CB  . PRO A 1 72  ? -14.57600 15.13000  77.96100  1.000 9.20381  ? 75  PRO A CB  1 
ATOM   614  C  CG  . PRO A 1 72  ? -14.33100 13.81600  77.27500  1.000 11.02381 ? 75  PRO A CG  1 
ATOM   615  C  CD  . PRO A 1 72  ? -12.84800 13.59000  77.46500  1.000 9.16381  ? 75  PRO A CD  1 
ATOM   616  N  N   . ASP A 1 73  ? -13.42100 18.16700  78.58300  1.000 9.98381  ? 76  ASP A N   1 
ATOM   617  C  CA  . ASP A 1 73  ? -13.11000 19.15500  79.60500  1.000 10.77381 ? 76  ASP A CA  1 
ATOM   618  C  C   . ASP A 1 73  ? -13.48500 18.66300  81.00400  1.000 11.31381 ? 76  ASP A C   1 
ATOM   619  O  O   . ASP A 1 73  ? -12.71700 18.84600  81.95500  1.000 12.87381 ? 76  ASP A O   1 
ATOM   620  C  CB  . ASP A 1 73  ? -13.82400 20.46900  79.30600  1.000 13.35381 ? 76  ASP A CB  1 
ATOM   621  C  CG  . ASP A 1 73  ? -13.53800 21.51800  80.35500  1.000 16.60381 ? 76  ASP A CG  1 
ATOM   622  O  OD1 . ASP A 1 73  ? -12.49800 22.19100  80.25200  1.000 15.47381 ? 76  ASP A OD1 1 
ATOM   623  O  OD2 . ASP A 1 73  ? -14.34100 21.64900  81.29800  1.000 18.01381 ? 76  ASP A OD2 1 
ATOM   624  N  N   . HIS A 1 74  ? -14.64200 18.01600  81.14800  1.000 12.83381 ? 77  HIS A N   1 
ATOM   625  C  CA  . HIS A 1 74  ? -15.04500 17.54900  82.47300  1.000 15.65381 ? 77  HIS A CA  1 
ATOM   626  C  C   . HIS A 1 74  ? -14.18500 16.39900  82.98500  1.000 15.58381 ? 77  HIS A C   1 
ATOM   627  O  O   . HIS A 1 74  ? -14.30700 16.02900  84.16000  1.000 17.38381 ? 77  HIS A O   1 
ATOM   628  C  CB  . HIS A 1 74  ? -16.53100 17.17900  82.50200  1.000 16.51381 ? 77  HIS A CB  1 
ATOM   629  C  CG  . HIS A 1 74  ? -16.85100 15.88400  81.82700  1.000 18.38381 ? 77  HIS A CG  1 
ATOM   630  N  ND1 . HIS A 1 74  ? -16.99300 15.77000  80.46000  1.000 17.88381 ? 77  HIS A ND1 1 
ATOM   631  C  CD2 . HIS A 1 74  ? -17.07600 14.64600  82.33200  1.000 15.90381 ? 77  HIS A CD2 1 
ATOM   632  C  CE1 . HIS A 1 74  ? -17.28400 14.51900  80.15300  1.000 19.77381 ? 77  HIS A CE1 1 
ATOM   633  N  NE2 . HIS A 1 74  ? -17.33700 13.81500  81.26900  1.000 16.90381 ? 77  HIS A NE2 1 
ATOM   634  N  N   . MET A 1 75  ? -13.32500 15.83300  82.13800  1.000 12.23381 ? 78  MET A N   1 
ATOM   635  C  CA  A MET A 1 75  ? -12.43600 14.74400  82.52300  0.630 12.89381 ? 78  MET A CA  1 
ATOM   636  C  CA  B MET A 1 75  ? -12.43200 14.74200  82.50500  0.370 12.99381 ? 78  MET A CA  1 
ATOM   637  C  C   . MET A 1 75  ? -10.98100 15.18300  82.63000  1.000 13.33381 ? 78  MET A C   1 
ATOM   638  O  O   . MET A 1 75  ? -10.10700 14.33000  82.79800  1.000 13.49381 ? 78  MET A O   1 
ATOM   639  C  CB  A MET A 1 75  ? -12.54900 13.57400  81.53700  0.630 11.61381 ? 78  MET A CB  1 
ATOM   640  C  CB  B MET A 1 75  ? -12.51700 13.61900  81.47000  0.370 11.51381 ? 78  MET A CB  1 
ATOM   641  C  CG  A MET A 1 75  ? -13.89300 12.85700  81.56400  0.630 13.19381 ? 78  MET A CG  1 
ATOM   642  C  CG  B MET A 1 75  ? -13.88400 12.99200  81.34800  0.370 12.72381 ? 78  MET A CG  1 
ATOM   643  S  SD  A MET A 1 75  ? -14.01600 11.41000  80.47900  0.630 13.56381 ? 78  MET A SD  1 
ATOM   644  S  SD  B MET A 1 75  ? -14.30500 12.01200  82.79500  0.370 13.42381 ? 78  MET A SD  1 
ATOM   645  C  CE  A MET A 1 75  ? -12.81700 10.31700  81.23800  0.630 14.40381 ? 78  MET A CE  1 
ATOM   646  C  CE  B MET A 1 75  ? -13.27700 10.56600  82.53900  0.370 15.45381 ? 78  MET A CE  1 
ATOM   647  N  N   . LYS A 1 76  ? -10.70200 16.49300  82.54200  1.000 12.79381 ? 79  LYS A N   1 
ATOM   648  C  CA  A LYS A 1 76  ? -9.32200  16.98200  82.50900  0.320 13.97381 ? 79  LYS A CA  1 
ATOM   649  C  CA  B LYS A 1 76  ? -9.31300  16.93100  82.48300  0.390 13.97381 ? 79  LYS A CA  1 
ATOM   650  C  CA  C LYS A 1 76  ? -9.31600  16.95200  82.49200  0.280 13.99381 ? 79  LYS A CA  1 
ATOM   651  C  C   . LYS A 1 76  ? -8.52000  16.50800  83.71300  1.000 13.38381 ? 79  LYS A C   1 
ATOM   652  O  O   . LYS A 1 76  ? -7.31200  16.26100  83.60700  1.000 14.42381 ? 79  LYS A O   1 
ATOM   653  C  CB  A LYS A 1 76  ? -9.31100  18.51200  82.47500  0.320 15.33381 ? 79  LYS A CB  1 
ATOM   654  C  CB  B LYS A 1 76  ? -9.22300  18.43700  82.23200  0.390 14.71381 ? 79  LYS A CB  1 
ATOM   655  C  CB  C LYS A 1 76  ? -9.25300  18.47400  82.34400  0.280 15.04381 ? 79  LYS A CB  1 
ATOM   656  C  CG  A LYS A 1 76  ? -8.89900  19.13300  81.15000  0.320 28.25381 ? 79  LYS A CG  1 
ATOM   657  C  CG  B LYS A 1 76  ? -9.54400  18.82000  80.79500  0.390 28.35381 ? 79  LYS A CG  1 
ATOM   658  C  CG  C LYS A 1 76  ? -9.56900  18.99400  80.94900  0.280 28.40381 ? 79  LYS A CG  1 
ATOM   659  C  CD  A LYS A 1 76  ? -8.93700  20.65600  81.24100  0.320 19.65381 ? 79  LYS A CD  1 
ATOM   660  C  CD  B LYS A 1 76  ? -9.59900  20.32600  80.60600  0.390 24.55381 ? 79  LYS A CD  1 
ATOM   661  C  CD  C LYS A 1 76  ? -9.37200  20.50400  80.88200  0.280 22.54381 ? 79  LYS A CD  1 
ATOM   662  C  CE  A LYS A 1 76  ? -8.49000  21.32100  79.94500  0.320 25.58381 ? 79  LYS A CE  1 
ATOM   663  C  CE  B LYS A 1 76  ? -9.82600  20.67800  79.14300  0.390 30.16381 ? 79  LYS A CE  1 
ATOM   664  C  CE  C LYS A 1 76  ? -9.56600  21.04100  79.47100  0.280 27.22381 ? 79  LYS A CE  1 
ATOM   665  N  NZ  A LYS A 1 76  ? -7.03600  21.14100  79.67300  0.320 19.78381 ? 79  LYS A NZ  1 
ATOM   666  N  NZ  B LYS A 1 76  ? -10.24600 22.09600  78.95900  0.390 21.53381 ? 79  LYS A NZ  1 
ATOM   667  N  NZ  C LYS A 1 76  ? -9.42600  22.52800  79.42300  0.280 18.80381 ? 79  LYS A NZ  1 
ATOM   668  N  N   . ARG A 1 77  ? -9.16400  16.39100  84.87300  1.000 12.73381 ? 80  ARG A N   1 
ATOM   669  C  CA  . ARG A 1 77  ? -8.38400  16.01300  86.04900  1.000 13.18381 ? 80  ARG A CA  1 
ATOM   670  C  C   . ARG A 1 77  ? -7.93700  14.56300  86.01700  1.000 12.08381 ? 80  ARG A C   1 
ATOM   671  O  O   . ARG A 1 77  ? -7.23200  14.13600  86.93600  1.000 13.83381 ? 80  ARG A O   1 
ATOM   672  C  CB  . ARG A 1 77  ? -9.13800  16.32300  87.34800  1.000 14.20381 ? 80  ARG A CB  1 
ATOM   673  C  CG  . ARG A 1 77  ? -10.34400 15.45300  87.60700  1.000 18.07381 ? 80  ARG A CG  1 
ATOM   674  C  CD  . ARG A 1 77  ? -11.17700 16.07500  88.72200  1.000 18.42381 ? 80  ARG A CD  1 
ATOM   675  N  NE  . ARG A 1 77  ? -12.43300 15.37000  88.92300  1.000 23.30381 ? 80  ARG A NE  1 
ATOM   676  C  CZ  . ARG A 1 77  ? -12.59000 14.35200  89.75400  1.000 17.69381 ? 80  ARG A CZ  1 
ATOM   677  N  NH1 . ARG A 1 77  ? -11.59400 13.91700  90.50800  1.000 23.63381 ? 80  ARG A NH1 1 
ATOM   678  N  NH2 . ARG A 1 77  ? -13.77800 13.75500  89.83200  1.000 18.89381 ? 80  ARG A NH2 1 
ATOM   679  N  N   . HIS A 1 78  ? -8.32100  13.79800  84.99500  1.000 11.60381 ? 81  HIS A N   1 
ATOM   680  C  CA  . HIS A 1 78  ? -7.95600  12.39200  84.89600  1.000 10.67381 ? 81  HIS A CA  1 
ATOM   681  C  C   . HIS A 1 78  ? -6.89100  12.13600  83.84100  1.000 13.33381 ? 81  HIS A C   1 
ATOM   682  O  O   . HIS A 1 78  ? -6.59300  10.97400  83.55800  1.000 12.51381 ? 81  HIS A O   1 
ATOM   683  C  CB  . HIS A 1 78  ? -9.18900  11.53700  84.60800  1.000 10.48381 ? 81  HIS A CB  1 
ATOM   684  C  CG  . HIS A 1 78  ? -10.28000 11.72900  85.60900  1.000 10.85381 ? 81  HIS A CG  1 
ATOM   685  N  ND1 . HIS A 1 78  ? -10.12700 11.41300  86.94200  1.000 13.32381 ? 81  HIS A ND1 1 
ATOM   686  C  CD2 . HIS A 1 78  ? -11.53800 12.21400  85.47600  1.000 12.44381 ? 81  HIS A CD2 1 
ATOM   687  C  CE1 . HIS A 1 78  ? -11.24200 11.71200  87.59000  1.000 12.46381 ? 81  HIS A CE1 1 
ATOM   688  N  NE2 . HIS A 1 78  ? -12.11400 12.19100  86.72100  1.000 14.52381 ? 81  HIS A NE2 1 
ATOM   689  N  N   . ASP A 1 79  ? -6.32000  13.18600  83.25300  1.000 11.34381 ? 82  ASP A N   1 
ATOM   690  C  CA  . ASP A 1 79  ? -5.39300  13.03900  82.12900  1.000 9.02381  ? 82  ASP A CA  1 
ATOM   691  C  C   . ASP A 1 79  ? -3.97000  12.95000  82.67400  1.000 10.16381 ? 82  ASP A C   1 
ATOM   692  O  O   . ASP A 1 79  ? -3.24100  13.94800  82.75400  1.000 9.88381  ? 82  ASP A O   1 
ATOM   693  C  CB  . ASP A 1 79  ? -5.56600  14.20500  81.16000  1.000 9.53381  ? 82  ASP A CB  1 
ATOM   694  C  CG  . ASP A 1 79  ? -4.77800  14.02800  79.86700  1.000 10.22381 ? 82  ASP A CG  1 
ATOM   695  O  OD1 . ASP A 1 79  ? -3.93500  13.09800  79.79000  1.000 9.38381  ? 82  ASP A OD1 1 
ATOM   696  O  OD2 . ASP A 1 79  ? -5.01100  14.83600  78.93200  1.000 10.43381 ? 82  ASP A OD2 1 
ATOM   697  N  N   . PHE A 1 80  ? -3.56700  11.73200  83.04500  1.000 10.72381 ? 83  PHE A N   1 
ATOM   698  C  CA  . PHE A 1 80  ? -2.20200  11.52000  83.51100  1.000 9.98381  ? 83  PHE A CA  1 
ATOM   699  C  C   . PHE A 1 80  ? -1.19600  11.86000  82.42200  1.000 11.41381 ? 83  PHE A C   1 
ATOM   700  O  O   . PHE A 1 80  ? -0.15100  12.46300  82.69100  1.000 10.75381 ? 83  PHE A O   1 
ATOM   701  C  CB  . PHE A 1 80  ? -2.01300  10.05700  83.93400  1.000 11.11381 ? 83  PHE A CB  1 
ATOM   702  C  CG  . PHE A 1 80  ? -0.55900  9.65400   84.03800  1.000 10.54381 ? 83  PHE A CG  1 
ATOM   703  C  CD1 . PHE A 1 80  ? 0.16400   9.91200   85.19700  1.000 13.46381 ? 83  PHE A CD1 1 
ATOM   704  C  CD2 . PHE A 1 80  ? 0.10300   9.05400   82.96300  1.000 9.40381  ? 83  PHE A CD2 1 
ATOM   705  C  CE1 . PHE A 1 80  ? 1.49600   9.56300   85.29200  1.000 12.24381 ? 83  PHE A CE1 1 
ATOM   706  C  CE2 . PHE A 1 80  ? 1.44200   8.72900   83.05200  1.000 12.54381 ? 83  PHE A CE2 1 
ATOM   707  C  CZ  . PHE A 1 80  ? 2.14000   8.97900   84.22300  1.000 13.28381 ? 83  PHE A CZ  1 
ATOM   708  N  N   . PHE A 1 81  ? -1.49500  11.46600  81.18400  1.000 9.95381  ? 84  PHE A N   1 
ATOM   709  C  CA  . PHE A 1 81  ? -0.48800  11.50400  80.12900  1.000 9.01381  ? 84  PHE A CA  1 
ATOM   710  C  C   . PHE A 1 81  ? 0.01300   12.92300  79.88600  1.000 8.93381  ? 84  PHE A C   1 
ATOM   711  O  O   . PHE A 1 81  ? 1.22300   13.16800  79.81300  1.000 9.81381  ? 84  PHE A O   1 
ATOM   712  C  CB  . PHE A 1 81  ? -1.07100  10.92100  78.84300  1.000 8.41381  ? 84  PHE A CB  1 
ATOM   713  C  CG  . PHE A 1 81  ? -1.66000  9.54600   79.00900  1.000 9.05381  ? 84  PHE A CG  1 
ATOM   714  C  CD1 . PHE A 1 81  ? -0.83200  8.44000   79.02000  1.000 9.13381  ? 84  PHE A CD1 1 
ATOM   715  C  CD2 . PHE A 1 81  ? -3.03500  9.36200   79.13500  1.000 9.80381  ? 84  PHE A CD2 1 
ATOM   716  C  CE1 . PHE A 1 81  ? -1.34800  7.16300   79.16000  1.000 9.56381  ? 84  PHE A CE1 1 
ATOM   717  C  CE2 . PHE A 1 81  ? -3.57300  8.08600   79.28400  1.000 8.47381  ? 84  PHE A CE2 1 
ATOM   718  C  CZ  . PHE A 1 81  ? -2.72200  6.98400   79.29400  1.000 8.63381  ? 84  PHE A CZ  1 
ATOM   719  N  N   . LYS A 1 82  ? -0.90500  13.87600  79.73000  1.000 9.21381  ? 85  LYS A N   1 
ATOM   720  C  CA  . LYS A 1 82  ? -0.45500  15.24500  79.52500  1.000 7.56381  ? 85  LYS A CA  1 
ATOM   721  C  C   . LYS A 1 82  ? 0.14500   15.82700  80.79500  1.000 9.42381  ? 85  LYS A C   1 
ATOM   722  O  O   . LYS A 1 82  ? 1.07000   16.64900  80.71800  1.000 10.22381 ? 85  LYS A O   1 
ATOM   723  C  CB  . LYS A 1 82  ? -1.60200  16.13400  79.04300  1.000 9.35381  ? 85  LYS A CB  1 
ATOM   724  C  CG  . LYS A 1 82  ? -2.13400  15.80300  77.66000  1.000 7.65381  ? 85  LYS A CG  1 
ATOM   725  C  CD  . LYS A 1 82  ? -3.21700  16.81900  77.25900  1.000 7.75381  ? 85  LYS A CD  1 
ATOM   726  C  CE  . LYS A 1 82  ? -3.94000  16.36400  76.01000  1.000 7.83381  ? 85  LYS A CE  1 
ATOM   727  N  NZ  . LYS A 1 82  ? -4.62500  15.02200  76.20300  1.000 9.99381  ? 85  LYS A NZ  1 
ATOM   728  N  N   . SER A 1 83  ? -0.34100  15.39900  81.96400  1.000 10.98381 ? 86  SER A N   1 
ATOM   729  C  CA  . SER A 1 83  ? 0.13000   15.98700  83.21400  1.000 12.37381 ? 86  SER A CA  1 
ATOM   730  C  C   . SER A 1 83  ? 1.60500   15.71500  83.45500  1.000 12.96381 ? 86  SER A C   1 
ATOM   731  O  O   . SER A 1 83  ? 2.26200   16.47700  84.17200  1.000 13.68381 ? 86  SER A O   1 
ATOM   732  C  CB  . SER A 1 83  ? -0.68300  15.45900  84.39400  1.000 12.08381 ? 86  SER A CB  1 
ATOM   733  O  OG  . SER A 1 83  ? -0.20800  14.19600  84.81600  1.000 11.98381 ? 86  SER A OG  1 
ATOM   734  N  N   . ALA A 1 84  ? 2.13300   14.64700  82.87200  1.000 9.72381  ? 87  ALA A N   1 
ATOM   735  C  CA  . ALA A 1 84  ? 3.53900   14.30000  83.01900  1.000 8.63381  ? 87  ALA A CA  1 
ATOM   736  C  C   . ALA A 1 84  ? 4.45500   15.12200  82.12200  1.000 11.47381 ? 87  ALA A C   1 
ATOM   737  O  O   . ALA A 1 84  ? 5.67900   15.01600  82.25300  1.000 11.55381 ? 87  ALA A O   1 
ATOM   738  C  CB  . ALA A 1 84  ? 3.71200   12.80600  82.72500  1.000 9.47381  ? 87  ALA A CB  1 
ATOM   739  N  N   . MET A 1 85  ? 3.89500   15.95400  81.22100  1.000 9.62381  ? 88  MET A N   1 
ATOM   740  C  CA  . MET A 1 85  ? 4.70500   16.65200  80.24100  1.000 8.54381  ? 88  MET A CA  1 
ATOM   741  C  C   . MET A 1 85  ? 5.14300   18.00600  80.79500  1.000 10.19381 ? 88  MET A C   1 
ATOM   742  O  O   . MET A 1 85  ? 4.44000   18.60200  81.62300  1.000 13.61381 ? 88  MET A O   1 
ATOM   743  C  CB  . MET A 1 85  ? 3.90100   16.84700  78.95600  1.000 11.15381 ? 88  MET A CB  1 
ATOM   744  C  CG  . MET A 1 85  ? 3.53700   15.52900  78.27700  1.000 9.63381  ? 88  MET A CG  1 
ATOM   745  S  SD  . MET A 1 85  ? 5.02200   14.62000  77.80900  1.000 10.17381 ? 88  MET A SD  1 
ATOM   746  C  CE  . MET A 1 85  ? 4.34000   12.98700  77.51400  1.000 10.19381 ? 88  MET A CE  1 
ATOM   747  N  N   . PRO A 1 86  ? 6.28700   18.54000  80.34300  1.000 10.13381 ? 89  PRO A N   1 
ATOM   748  C  CA  . PRO A 1 86  ? 7.12300   18.05700  79.23800  1.000 10.50381 ? 89  PRO A CA  1 
ATOM   749  C  C   . PRO A 1 86  ? 8.11000   16.95200  79.59000  1.000 10.77381 ? 89  PRO A C   1 
ATOM   750  O  O   . PRO A 1 86  ? 8.63800   16.33300  78.67400  1.000 10.88381 ? 89  PRO A O   1 
ATOM   751  C  CB  . PRO A 1 86  ? 7.89900   19.31400  78.82200  1.000 12.84381 ? 89  PRO A CB  1 
ATOM   752  C  CG  . PRO A 1 86  ? 8.02200   20.08100  80.09900  1.000 16.20381 ? 89  PRO A CG  1 
ATOM   753  C  CD  . PRO A 1 86  ? 6.72200   19.86900  80.82000  1.000 13.71381 ? 89  PRO A CD  1 
ATOM   754  N  N   . GLU A 1 87  ? 8.36900   16.72200  80.88000  1.000 10.97381 ? 90  GLU A N   1 
ATOM   755  C  CA  . GLU A 1 87  ? 9.42000   15.77900  81.26000  1.000 11.79381 ? 90  GLU A CA  1 
ATOM   756  C  C   . GLU A 1 87  ? 9.10300   14.36400  80.79800  1.000 10.64381 ? 90  GLU A C   1 
ATOM   757  O  O   . GLU A 1 87  ? 10.01800  13.60100  80.44900  1.000 11.35381 ? 90  GLU A O   1 
ATOM   758  C  CB  . GLU A 1 87  ? 9.63300   15.81000  82.77000  1.000 18.82381 ? 90  GLU A CB  1 
ATOM   759  C  CG  . GLU A 1 87  ? 10.14800  17.14800  83.29000  1.000 16.59381 ? 90  GLU A CG  1 
ATOM   760  C  CD  . GLU A 1 87  ? 9.04600   18.19000  83.47700  1.000 20.37381 ? 90  GLU A CD  1 
ATOM   761  O  OE1 . GLU A 1 87  ? 7.83700   17.84500  83.39700  1.000 19.91381 ? 90  GLU A OE1 1 
ATOM   762  O  OE2 . GLU A 1 87  ? 9.39900   19.36700  83.71000  1.000 36.64381 ? 90  GLU A OE2 1 
ATOM   763  N  N   . GLY A 1 88  ? 7.82500   14.00100  80.78600  1.000 10.82381 ? 91  GLY A N   1 
ATOM   764  C  CA  . GLY A 1 88  ? 7.37400   12.79000  80.12900  1.000 9.37381  ? 91  GLY A CA  1 
ATOM   765  C  C   . GLY A 1 88  ? 7.13800   11.63800  81.08000  1.000 11.10381 ? 91  GLY A C   1 
ATOM   766  O  O   . GLY A 1 88  ? 7.11100   11.77400  82.30600  1.000 11.18381 ? 91  GLY A O   1 
ATOM   767  N  N   . TYR A 1 89  ? 6.93600   10.46600  80.47600  1.000 8.95381  ? 92  TYR A N   1 
ATOM   768  C  CA  . TYR A 1 89  ? 6.67700   9.26400   81.24800  1.000 8.16381  ? 92  TYR A CA  1 
ATOM   769  C  C   . TYR A 1 89  ? 7.33200   8.05600   80.60100  1.000 10.04381 ? 92  TYR A C   1 
ATOM   770  O  O   . TYR A 1 89  ? 7.56000   8.02300   79.39000  1.000 9.78381  ? 92  TYR A O   1 
ATOM   771  C  CB  . TYR A 1 89  ? 5.17400   9.00800   81.43700  1.000 8.96381  ? 92  TYR A CB  1 
ATOM   772  C  CG  . TYR A 1 89  ? 4.31900   9.02000   80.17700  1.000 9.51381  ? 92  TYR A CG  1 
ATOM   773  C  CD1 . TYR A 1 89  ? 4.25100   7.91300   79.32600  1.000 8.76381  ? 92  TYR A CD1 1 
ATOM   774  C  CD2 . TYR A 1 89  ? 3.54400   10.12800  79.85600  1.000 9.97381  ? 92  TYR A CD2 1 
ATOM   775  C  CE1 . TYR A 1 89  ? 3.45300   7.92700   78.18300  1.000 9.44381  ? 92  TYR A CE1 1 
ATOM   776  C  CE2 . TYR A 1 89  ? 2.75300   10.15200  78.71600  1.000 8.48381  ? 92  TYR A CE2 1 
ATOM   777  C  CZ  . TYR A 1 89  ? 2.69500   9.04800   77.89400  1.000 11.53381 ? 92  TYR A CZ  1 
ATOM   778  O  OH  . TYR A 1 89  ? 1.88800   9.07400   76.77600  1.000 8.95381  ? 92  TYR A OH  1 
ATOM   779  N  N   . VAL A 1 90  ? 7.63500   7.06900   81.43800  1.000 9.45381  ? 93  VAL A N   1 
ATOM   780  C  CA  . VAL A 1 90  ? 7.98200   5.73700   80.97000  1.000 7.34381  ? 93  VAL A CA  1 
ATOM   781  C  C   . VAL A 1 90  ? 6.68300   4.99100   80.72100  1.000 9.40381  ? 93  VAL A C   1 
ATOM   782  O  O   . VAL A 1 90  ? 5.73600   5.09700   81.50600  1.000 11.97381 ? 93  VAL A O   1 
ATOM   783  C  CB  . VAL A 1 90  ? 8.84500   5.01500   82.02400  1.000 10.00381 ? 93  VAL A CB  1 
ATOM   784  C  CG1 . VAL A 1 90  ? 9.23000   3.62900   81.53900  1.000 10.35381 ? 93  VAL A CG1 1 
ATOM   785  C  CG2 . VAL A 1 90  ? 10.10500  5.81900   82.32600  1.000 9.51381  ? 93  VAL A CG2 1 
ATOM   786  N  N   . GLN A 1 91  ? 6.61800   4.25500   79.61200  1.000 9.03381  ? 94  GLN A N   1 
ATOM   787  C  CA  . GLN A 1 91  ? 5.48600   3.38700   79.32500  1.000 8.25381  ? 94  GLN A CA  1 
ATOM   788  C  C   . GLN A 1 91  ? 6.03600   2.00000   79.06800  1.000 9.01381  ? 94  GLN A C   1 
ATOM   789  O  O   . GLN A 1 91  ? 6.82500   1.81200   78.13800  1.000 9.36381  ? 94  GLN A O   1 
ATOM   790  C  CB  . GLN A 1 91  ? 4.72000   3.86500   78.09500  1.000 8.18381  ? 94  GLN A CB  1 
ATOM   791  C  CG  . GLN A 1 91  ? 3.59000   2.93000   77.67300  1.000 8.33381  ? 94  GLN A CG  1 
ATOM   792  C  CD  . GLN A 1 91  ? 2.56000   3.64000   76.83000  1.000 9.58381  ? 94  GLN A CD  1 
ATOM   793  O  OE1 . GLN A 1 91  ? 2.02000   4.68300   77.22500  1.000 9.41381  ? 94  GLN A OE1 1 
ATOM   794  N  NE2 . GLN A 1 91  ? 2.27400   3.08200   75.65700  1.000 8.51381  ? 94  GLN A NE2 1 
ATOM   795  N  N   . GLU A 1 92  ? 5.62100   1.03600   79.88200  1.000 9.85381  ? 95  GLU A N   1 
ATOM   796  C  CA  . GLU A 1 92  ? 6.08700   -0.33500  79.76300  1.000 9.56381  ? 95  GLU A CA  1 
ATOM   797  C  C   . GLU A 1 92  ? 4.89900   -1.23100  79.46100  1.000 8.75381  ? 95  GLU A C   1 
ATOM   798  O  O   . GLU A 1 92  ? 3.82200   -1.06000  80.04000  1.000 11.23381 ? 95  GLU A O   1 
ATOM   799  C  CB  . GLU A 1 92  ? 6.72800   -0.78400  81.07400  1.000 10.89381 ? 95  GLU A CB  1 
ATOM   800  C  CG  . GLU A 1 92  ? 8.07300   -0.12400  81.34700  1.000 16.79381 ? 95  GLU A CG  1 
ATOM   801  C  CD  . GLU A 1 92  ? 8.55000   -0.32400  82.77400  1.000 25.95381 ? 95  GLU A CD  1 
ATOM   802  O  OE1 . GLU A 1 92  ? 7.97800   0.29700   83.69800  1.000 20.47381 ? 95  GLU A OE1 1 
ATOM   803  O  OE2 . GLU A 1 92  ? 9.49900   -1.10900  82.97100  1.000 39.15381 ? 95  GLU A OE2 1 
ATOM   804  N  N   . ARG A 1 93  ? 5.09800   -2.21000  78.57800  1.000 8.47381  ? 96  ARG A N   1 
ATOM   805  C  CA  . ARG A 1 93  ? 4.05400   -3.18900  78.32300  1.000 7.84381  ? 96  ARG A CA  1 
ATOM   806  C  C   . ARG A 1 93  ? 4.61500   -4.59700  78.21700  1.000 7.69381  ? 96  ARG A C   1 
ATOM   807  O  O   . ARG A 1 93  ? 5.78000   -4.81000  77.86100  1.000 8.96381  ? 96  ARG A O   1 
ATOM   808  C  CB  . ARG A 1 93  ? 3.30300   -2.92900  77.02000  1.000 8.13381  ? 96  ARG A CB  1 
ATOM   809  C  CG  . ARG A 1 93  ? 2.45900   -1.66600  77.02300  1.000 8.36381  ? 96  ARG A CG  1 
ATOM   810  C  CD  . ARG A 1 93  ? 1.25200   -1.88900  76.12600  1.000 7.79381  ? 96  ARG A CD  1 
ATOM   811  N  NE  . ARG A 1 93  ? 0.39400   -0.70900  76.02600  1.000 7.00381  ? 96  ARG A NE  1 
ATOM   812  C  CZ  . ARG A 1 93  ? 0.49200   0.23000   75.09100  1.000 7.04381  ? 96  ARG A CZ  1 
ATOM   813  N  NH1 . ARG A 1 93  ? 1.44500   0.19500   74.16800  1.000 6.63381  ? 96  ARG A NH1 1 
ATOM   814  N  NH2 . ARG A 1 93  ? -0.40200  1.21500   75.06700  1.000 8.16381  ? 96  ARG A NH2 1 
ATOM   815  N  N   . THR A 1 94  ? 3.76600   -5.55500  78.56600  1.000 8.82381  ? 97  THR A N   1 
ATOM   816  C  CA  . THR A 1 94  ? 3.88200   -6.92700  78.09700  1.000 7.62381  ? 97  THR A CA  1 
ATOM   817  C  C   . THR A 1 94  ? 2.70800   -7.16300  77.16200  1.000 7.57381  ? 97  THR A C   1 
ATOM   818  O  O   . THR A 1 94  ? 1.54800   -6.96300  77.54900  1.000 8.86381  ? 97  THR A O   1 
ATOM   819  C  CB  . THR A 1 94  ? 3.85200   -7.92600  79.25600  1.000 10.49381 ? 97  THR A CB  1 
ATOM   820  O  OG1 . THR A 1 94  ? 4.98300   -7.68600  80.10500  1.000 11.38381 ? 97  THR A OG1 1 
ATOM   821  C  CG2 . THR A 1 94  ? 3.95100   -9.36000  78.71700  1.000 9.57381  ? 97  THR A CG2 1 
ATOM   822  N  N   . ILE A 1 95  ? 3.01100   -7.54100  75.92500  1.000 7.93381  ? 98  ILE A N   1 
ATOM   823  C  CA  . ILE A 1 95  ? 2.00300   -7.90200  74.94100  1.000 7.11381  ? 98  ILE A CA  1 
ATOM   824  C  C   . ILE A 1 95  ? 2.12400   -9.39900  74.72100  1.000 8.73381  ? 98  ILE A C   1 
ATOM   825  O  O   . ILE A 1 95  ? 3.14400   -9.87500  74.20600  1.000 8.08381  ? 98  ILE A O   1 
ATOM   826  C  CB  . ILE A 1 95  ? 2.19100   -7.13600  73.62700  1.000 8.53381  ? 98  ILE A CB  1 
ATOM   827  C  CG1 . ILE A 1 95  ? 2.15700   -5.63000  73.88200  1.000 9.07381  ? 98  ILE A CG1 1 
ATOM   828  C  CG2 . ILE A 1 95  ? 1.10900   -7.54600  72.63400  1.000 8.84381  ? 98  ILE A CG2 1 
ATOM   829  C  CD1 . ILE A 1 95  ? 2.51600   -4.79000  72.63000  1.000 7.98381  ? 98  ILE A CD1 1 
ATOM   830  N  N   . SER A 1 96  ? 1.09900   -10.14500 75.12100  1.000 8.77381  ? 99  SER A N   1 
ATOM   831  C  CA  . SER A 1 96  ? 1.12800   -11.60200 75.07400  1.000 9.14381  ? 99  SER A CA  1 
ATOM   832  C  C   . SER A 1 96  ? 0.25800   -12.06300 73.91100  1.000 8.06381  ? 99  SER A C   1 
ATOM   833  O  O   . SER A 1 96  ? -0.96900  -11.92700 73.95600  1.000 9.46381  ? 99  SER A O   1 
ATOM   834  C  CB  . SER A 1 96  ? 0.61900   -12.15400 76.40200  1.000 11.17381 ? 99  SER A CB  1 
ATOM   835  O  OG  . SER A 1 96  ? 1.35700   -11.58800 77.47600  1.000 12.93381 ? 99  SER A OG  1 
ATOM   836  N  N   . PHE A 1 97  ? 0.88900   -12.59900 72.86600  1.000 9.63381  ? 100 PHE A N   1 
ATOM   837  C  CA  . PHE A 1 97  ? 0.13600   -13.11700 71.72800  1.000 9.58381  ? 100 PHE A CA  1 
ATOM   838  C  C   . PHE A 1 97  ? -0.32800  -14.52400 72.05400  1.000 9.97381  ? 100 PHE A C   1 
ATOM   839  O  O   . PHE A 1 97  ? 0.49300   -15.41700 72.26700  1.000 10.39381 ? 100 PHE A O   1 
ATOM   840  C  CB  . PHE A 1 97  ? 0.97900   -13.07300 70.45300  1.000 7.00381  ? 100 PHE A CB  1 
ATOM   841  C  CG  . PHE A 1 97  ? 1.32900   -11.67700 70.02700  1.000 6.69381  ? 100 PHE A CG  1 
ATOM   842  C  CD1 . PHE A 1 97  ? 0.48100   -10.94400 69.19900  1.000 8.01381  ? 100 PHE A CD1 1 
ATOM   843  C  CD2 . PHE A 1 97  ? 2.49900   -11.08700 70.47200  1.000 7.17381  ? 100 PHE A CD2 1 
ATOM   844  C  CE1 . PHE A 1 97  ? 0.80100   -9.63100  68.82100  1.000 7.34381  ? 100 PHE A CE1 1 
ATOM   845  C  CE2 . PHE A 1 97  ? 2.83000   -9.77900  70.10900  1.000 7.81381  ? 100 PHE A CE2 1 
ATOM   846  C  CZ  . PHE A 1 97  ? 1.98300   -9.05200  69.27700  1.000 7.54381  ? 100 PHE A CZ  1 
ATOM   847  N  N   . LYS A 1 98  ? -1.64400  -14.71400 72.11400  1.000 10.28381 ? 101 LYS A N   1 
ATOM   848  C  CA  A LYS A 1 98  ? -2.17700  -15.99800 72.53700  0.580 9.08381  ? 101 LYS A CA  1 
ATOM   849  C  CA  B LYS A 1 98  ? -2.20800  -15.99600 72.51500  0.420 9.24381  ? 101 LYS A CA  1 
ATOM   850  C  C   . LYS A 1 98  ? -1.61600  -17.12200 71.67800  1.000 11.90381 ? 101 LYS A C   1 
ATOM   851  O  O   . LYS A 1 98  ? -1.57600  -17.03300 70.44600  1.000 10.60381 ? 101 LYS A O   1 
ATOM   852  C  CB  A LYS A 1 98  ? -3.70200  -15.98400 72.46400  0.580 10.34381 ? 101 LYS A CB  1 
ATOM   853  C  CB  B LYS A 1 98  ? -3.71800  -15.93400 72.30000  0.420 9.84381  ? 101 LYS A CB  1 
ATOM   854  C  CG  A LYS A 1 98  ? -4.32300  -17.25500 73.02400  0.580 12.80381 ? 101 LYS A CG  1 
ATOM   855  C  CG  B LYS A 1 98  ? -4.48500  -17.18300 72.68500  0.420 11.92381 ? 101 LYS A CG  1 
ATOM   856  C  CD  A LYS A 1 98  ? -5.82500  -17.12700 73.15000  0.580 18.99381 ? 101 LYS A CD  1 
ATOM   857  C  CD  B LYS A 1 98  ? -5.96400  -16.88600 72.58800  0.420 9.58381  ? 101 LYS A CD  1 
ATOM   858  C  CE  A LYS A 1 98  ? -6.42800  -18.41600 73.68200  0.580 19.17381 ? 101 LYS A CE  1 
ATOM   859  C  CE  B LYS A 1 98  ? -6.81400  -18.02000 73.11300  0.420 24.03381 ? 101 LYS A CE  1 
ATOM   860  N  NZ  A LYS A 1 98  ? -5.87600  -18.75100 75.02600  0.580 25.04381 ? 101 LYS A NZ  1 
ATOM   861  N  NZ  B LYS A 1 98  ? -8.20700  -17.52900 73.26500  0.420 14.19381 ? 101 LYS A NZ  1 
ATOM   862  N  N   . ASP A 1 99  ? -1.15800  -18.18000 72.35800  1.000 12.21381 ? 102 ASP A N   1 
ATOM   863  C  CA  . ASP A 1 99  ? -0.56900  -19.35900 71.73700  1.000 11.51381 ? 102 ASP A CA  1 
ATOM   864  C  C   . ASP A 1 99  ? 0.66700   -19.02400 70.90300  1.000 12.48381 ? 102 ASP A C   1 
ATOM   865  O  O   . ASP A 1 99  ? 1.01900   -19.75300 69.97500  1.000 12.99381 ? 102 ASP A O   1 
ATOM   866  C  CB  . ASP A 1 99  ? -1.61800  -20.17300 70.96900  1.000 13.64381 ? 102 ASP A CB  1 
ATOM   867  C  CG  . ASP A 1 99  ? -2.66100  -20.78000 71.89700  1.000 27.11381 ? 102 ASP A CG  1 
ATOM   868  O  OD1 . ASP A 1 99  ? -2.28500  -21.17100 73.02300  1.000 27.89381 ? 102 ASP A OD1 1 
ATOM   869  O  OD2 . ASP A 1 99  ? -3.85300  -20.85200 71.51800  1.000 24.70381 ? 102 ASP A OD2 1 
ATOM   870  N  N   . ASP A 1 100 ? 1.32700   -17.91900 71.22900  1.000 9.84381  ? 103 ASP A N   1 
ATOM   871  C  CA  . ASP A 1 100 ? 2.52400   -17.49400 70.51400  1.000 11.35381 ? 103 ASP A CA  1 
ATOM   872  C  C   . ASP A 1 100 ? 3.41000   -16.73800 71.50000  1.000 10.45381 ? 103 ASP A C   1 
ATOM   873  O  O   . ASP A 1 100 ? 3.27300   -16.89200 72.71800  1.000 11.70381 ? 103 ASP A O   1 
ATOM   874  C  CB  . ASP A 1 100 ? 2.14900   -16.73100 69.22800  1.000 10.60381 ? 103 ASP A CB  1 
ATOM   875  C  CG  . ASP A 1 100 ? 3.17900   -16.89400 68.12600  1.000 12.83381 ? 103 ASP A CG  1 
ATOM   876  O  OD1 . ASP A 1 100 ? 4.37300   -17.09400 68.44000  1.000 11.77381 ? 103 ASP A OD1 1 
ATOM   877  O  OD2 . ASP A 1 100 ? 2.79800   -16.80200 66.94200  1.000 13.37381 ? 103 ASP A OD2 1 
ATOM   878  N  N   . GLY A 1 101 ? 4.31500   -15.91700 70.98000  1.000 8.28381  ? 104 GLY A N   1 
ATOM   879  C  CA  . GLY A 1 101 ? 5.29300   -15.24000 71.80800  1.000 7.01381  ? 104 GLY A CA  1 
ATOM   880  C  C   . GLY A 1 101 ? 4.75700   -13.97400 72.45300  1.000 9.10381  ? 104 GLY A C   1 
ATOM   881  O  O   . GLY A 1 101 ? 3.56000   -13.67900 72.44900  1.000 9.28381  ? 104 GLY A O   1 
ATOM   882  N  N   . ASN A 1 102 ? 5.67800   -13.22700 73.05600  1.000 9.26381  ? 105 ASN A N   1 
ATOM   883  C  CA  . ASN A 1 102 ? 5.32800   -11.99000 73.73000  1.000 7.88381  ? 105 ASN A CA  1 
ATOM   884  C  C   . ASN A 1 102 ? 6.33400   -10.90400 73.38400  1.000 9.00381  ? 105 ASN A C   1 
ATOM   885  O  O   . ASN A 1 102 ? 7.50900   -11.17600 73.14000  1.000 8.98381  ? 105 ASN A O   1 
ATOM   886  C  CB  . ASN A 1 102 ? 5.25500   -12.17500 75.26600  1.000 8.13381  ? 105 ASN A CB  1 
ATOM   887  C  CG  . ASN A 1 102 ? 6.58200   -12.63500 75.88100  1.000 10.40381 ? 105 ASN A CG  1 
ATOM   888  O  OD1 . ASN A 1 102 ? 7.42700   -11.82200 76.26100  1.000 14.41381 ? 105 ASN A OD1 1 
ATOM   889  N  ND2 . ASN A 1 102 ? 6.76300   -13.94500 75.98100  1.000 11.01381 ? 105 ASN A ND2 1 
ATOM   890  N  N   . TYR A 1 103 ? 5.84500   -9.66700  73.35800  1.000 7.87381  ? 106 TYR A N   1 
ATOM   891  C  CA  . TYR A 1 103 ? 6.69400   -8.49100  73.34100  1.000 6.59381  ? 106 TYR A CA  1 
ATOM   892  C  C   . TYR A 1 103 ? 6.76100   -7.91700  74.74800  1.000 7.88381  ? 106 TYR A C   1 
ATOM   893  O  O   . TYR A 1 103 ? 5.74500   -7.84300  75.44800  1.000 9.37381  ? 106 TYR A O   1 
ATOM   894  C  CB  . TYR A 1 103 ? 6.11400   -7.38800  72.44800  1.000 7.16381  ? 106 TYR A CB  1 
ATOM   895  C  CG  . TYR A 1 103 ? 5.95700   -7.67500  70.97400  1.000 7.06381  ? 106 TYR A CG  1 
ATOM   896  C  CD1 . TYR A 1 103 ? 6.68300   -8.67100  70.33800  1.000 7.36381  ? 106 TYR A CD1 1 
ATOM   897  C  CD2 . TYR A 1 103 ? 5.10000   -6.89400  70.20500  1.000 7.35381  ? 106 TYR A CD2 1 
ATOM   898  C  CE1 . TYR A 1 103 ? 6.53000   -8.90900  68.97100  1.000 6.62381  ? 106 TYR A CE1 1 
ATOM   899  C  CE2 . TYR A 1 103 ? 4.93800   -7.11900  68.85100  1.000 6.73381  ? 106 TYR A CE2 1 
ATOM   900  C  CZ  . TYR A 1 103 ? 5.65500   -8.12900  68.23500  1.000 6.16381  ? 106 TYR A CZ  1 
ATOM   901  O  OH  . TYR A 1 103 ? 5.49800   -8.36000  66.88800  1.000 9.25381  ? 106 TYR A OH  1 
ATOM   902  N  N   . LYS A 1 104 ? 7.95000   -7.47700  75.14200  1.000 7.58381  ? 107 LYS A N   1 
ATOM   903  C  CA  . LYS A 1 104 ? 8.13000   -6.59500  76.28200  1.000 6.67381  ? 107 LYS A CA  1 
ATOM   904  C  C   . LYS A 1 104 ? 8.66100   -5.29200  75.72400  1.000 8.68381  ? 107 LYS A C   1 
ATOM   905  O  O   . LYS A 1 104 ? 9.65200   -5.28700  74.98500  1.000 8.33381  ? 107 LYS A O   1 
ATOM   906  C  CB  . LYS A 1 104 ? 9.15500   -7.15900  77.25900  1.000 9.99381  ? 107 LYS A CB  1 
ATOM   907  C  CG  . LYS A 1 104 ? 8.79100   -8.51400  77.81400  1.000 18.81381 ? 107 LYS A CG  1 
ATOM   908  C  CD  . LYS A 1 104 ? 8.10300   -8.38700  79.13600  1.000 21.38381 ? 107 LYS A CD  1 
ATOM   909  C  CE  . LYS A 1 104 ? 7.83400   -9.76300  79.73500  1.000 16.57381 ? 107 LYS A CE  1 
ATOM   910  N  NZ  . LYS A 1 104 ? 6.97100   -9.61700  80.93000  1.000 24.47381 ? 107 LYS A NZ  1 
ATOM   911  N  N   . THR A 1 105 ? 7.99500   -4.19700  76.05100  1.000 7.08381  ? 108 THR A N   1 
ATOM   912  C  CA  . THR A 1 105 ? 8.36900   -2.90300  75.51400  1.000 8.43381  ? 108 THR A CA  1 
ATOM   913  C  C   . THR A 1 105 ? 8.63100   -1.93400  76.65100  1.000 7.74381  ? 108 THR A C   1 
ATOM   914  O  O   . THR A 1 105 ? 7.92600   -1.93600  77.66400  1.000 8.85381  ? 108 THR A O   1 
ATOM   915  C  CB  . THR A 1 105 ? 7.27400   -2.34400  74.58300  1.000 10.07381 ? 108 THR A CB  1 
ATOM   916  O  OG1 . THR A 1 105 ? 6.05800   -2.11300  75.31600  1.000 9.16381  ? 108 THR A OG1 1 
ATOM   917  C  CG2 . THR A 1 105 ? 7.00800   -3.30300  73.44200  1.000 9.15381  ? 108 THR A CG2 1 
ATOM   918  N  N   . ARG A 1 106 ? 9.66000   -1.11600  76.48500  1.000 8.91381  ? 109 ARG A N   1 
ATOM   919  C  CA  A ARG A 1 106 ? 9.93200   -0.01300  77.39300  0.580 7.23381  ? 109 ARG A CA  1 
ATOM   920  C  CA  B ARG A 1 106 ? 9.92900   -0.01200  77.39500  0.420 7.26381  ? 109 ARG A CA  1 
ATOM   921  C  C   . ARG A 1 106 ? 10.13200  1.23400   76.55400  1.000 7.02381  ? 109 ARG A C   1 
ATOM   922  O  O   . ARG A 1 106 ? 11.01500  1.26800   75.69500  1.000 10.04381 ? 109 ARG A O   1 
ATOM   923  C  CB  A ARG A 1 106 ? 11.17900  -0.26500  78.23900  0.580 8.34381  ? 109 ARG A CB  1 
ATOM   924  C  CB  B ARG A 1 106 ? 11.16300  -0.27300  78.26100  0.420 8.42381  ? 109 ARG A CB  1 
ATOM   925  C  CG  A ARG A 1 106 ? 11.36600  0.80600   79.29200  0.580 9.05381  ? 109 ARG A CG  1 
ATOM   926  C  CG  B ARG A 1 106 ? 11.33000  0.75700   79.36900  0.420 9.14381  ? 109 ARG A CG  1 
ATOM   927  C  CD  A ARG A 1 106 ? 12.70900  0.69300   79.97700  0.580 10.36381 ? 109 ARG A CD  1 
ATOM   928  C  CD  B ARG A 1 106 ? 12.53300  0.44800   80.24100  0.420 11.63381 ? 109 ARG A CD  1 
ATOM   929  N  NE  A ARG A 1 106 ? 12.78200  1.61600   81.10100  0.580 12.83381 ? 109 ARG A NE  1 
ATOM   930  N  NE  B ARG A 1 106 ? 12.71700  1.45900   81.27700  0.420 13.27381 ? 109 ARG A NE  1 
ATOM   931  C  CZ  A ARG A 1 106 ? 13.08400  2.90100   80.99400  0.580 10.89381 ? 109 ARG A CZ  1 
ATOM   932  C  CZ  B ARG A 1 106 ? 12.40100  1.29500   82.55400  0.420 17.12381 ? 109 ARG A CZ  1 
ATOM   933  N  NH1 A ARG A 1 106 ? 13.38200  3.44600   79.82300  0.580 12.46381 ? 109 ARG A NH1 1 
ATOM   934  N  NH1 B ARG A 1 106 ? 11.91000  0.15100   83.00600  0.420 12.86381 ? 109 ARG A NH1 1 
ATOM   935  N  NH2 A ARG A 1 106 ? 13.08800  3.65800   82.08800  0.580 17.11381 ? 109 ARG A NH2 1 
ATOM   936  N  NH2 B ARG A 1 106 ? 12.59000  2.30200   83.40300  0.420 25.44381 ? 109 ARG A NH2 1 
ATOM   937  N  N   . ALA A 1 107 ? 9.31400   2.24800   76.80400  1.000 7.72381  ? 110 ALA A N   1 
ATOM   938  C  CA  . ALA A 1 107 ? 9.33100   3.46200   76.02100  1.000 7.48381  ? 110 ALA A CA  1 
ATOM   939  C  C   . ALA A 1 107 ? 9.41800   4.66400   76.94200  1.000 7.68381  ? 110 ALA A C   1 
ATOM   940  O  O   . ALA A 1 107 ? 8.97800   4.62400   78.09300  1.000 8.06381  ? 110 ALA A O   1 
ATOM   941  C  CB  . ALA A 1 107 ? 8.06500   3.58900   75.18300  1.000 8.53381  ? 110 ALA A CB  1 
ATOM   942  N  N   . GLU A 1 108 ? 10.00900  5.73000   76.42200  1.000 8.15381  ? 111 GLU A N   1 
ATOM   943  C  CA  . GLU A 1 108 ? 9.97000   7.03000   77.07500  1.000 9.10381  ? 111 GLU A CA  1 
ATOM   944  C  C   . GLU A 1 108 ? 9.30300   8.01100   76.12700  1.000 10.26381 ? 111 GLU A C   1 
ATOM   945  O  O   . GLU A 1 108 ? 9.71500   8.14000   74.97100  1.000 9.63381  ? 111 GLU A O   1 
ATOM   946  C  CB  . GLU A 1 108 ? 11.36500  7.49600   77.49500  1.000 14.94381 ? 111 GLU A CB  1 
ATOM   947  C  CG  . GLU A 1 108 ? 11.90900  6.60600   78.60500  1.000 16.27381 ? 111 GLU A CG  1 
ATOM   948  C  CD  . GLU A 1 108 ? 13.14400  7.15100   79.28800  1.000 35.14381 ? 111 GLU A CD  1 
ATOM   949  O  OE1 . GLU A 1 108 ? 13.59700  8.27400   78.95000  1.000 21.01381 ? 111 GLU A OE1 1 
ATOM   950  O  OE2 . GLU A 1 108 ? 13.65400  6.43300   80.17700  1.000 24.51381 ? 111 GLU A OE2 1 
ATOM   951  N  N   . VAL A 1 109 ? 8.25600   8.66700   76.61500  1.000 8.81381  ? 112 VAL A N   1 
ATOM   952  C  CA  . VAL A 1 109 ? 7.48700   9.63800   75.85000  1.000 7.88381  ? 112 VAL A CA  1 
ATOM   953  C  C   . VAL A 1 109 ? 7.70100   10.99000  76.51300  1.000 8.87381  ? 112 VAL A C   1 
ATOM   954  O  O   . VAL A 1 109 ? 7.33300   11.17100  77.67600  1.000 9.63381  ? 112 VAL A O   1 
ATOM   955  C  CB  . VAL A 1 109 ? 5.99800   9.26500   75.83900  1.000 9.98381  ? 112 VAL A CB  1 
ATOM   956  C  CG1 . VAL A 1 109 ? 5.22000   10.23500  74.94700  1.000 8.73381  ? 112 VAL A CG1 1 
ATOM   957  C  CG2 . VAL A 1 109 ? 5.81400   7.82200   75.37300  1.000 11.49381 ? 112 VAL A CG2 1 
ATOM   958  N  N   . LYS A 1 110 ? 8.30000   11.93400  75.79000  1.000 9.54381  ? 113 LYS A N   1 
ATOM   959  C  CA  A LYS A 1 110 ? 8.62000   13.23500  76.36500  0.620 9.32381  ? 113 LYS A CA  1 
ATOM   960  C  CA  B LYS A 1 110 ? 8.61600   13.23500  76.36500  0.380 9.36381  ? 113 LYS A CA  1 
ATOM   961  C  C   . LYS A 1 110 ? 8.80900   14.23300  75.23500  1.000 8.45381  ? 113 LYS A C   1 
ATOM   962  O  O   . LYS A 1 110 ? 8.93600   13.86300  74.06900  1.000 10.49381 ? 113 LYS A O   1 
ATOM   963  C  CB  A LYS A 1 110 ? 9.90600   13.17700  77.20000  0.620 10.47381 ? 113 LYS A CB  1 
ATOM   964  C  CB  B LYS A 1 110 ? 9.88300   13.16300  77.22400  0.380 10.53381 ? 113 LYS A CB  1 
ATOM   965  C  CG  A LYS A 1 110 ? 11.17000  13.01300  76.34500  0.620 9.11381  ? 113 LYS A CG  1 
ATOM   966  C  CG  B LYS A 1 110 ? 11.11900  12.72100  76.44300  0.380 10.52381 ? 113 LYS A CG  1 
ATOM   967  C  CD  A LYS A 1 110 ? 12.44800  13.27700  77.13100  0.620 15.61381 ? 113 LYS A CD  1 
ATOM   968  C  CD  B LYS A 1 110 ? 12.34700  12.60800  77.33400  0.380 10.16381 ? 113 LYS A CD  1 
ATOM   969  C  CE  A LYS A 1 110 ? 12.74600  12.16200  78.11200  0.620 23.65381 ? 113 LYS A CE  1 
ATOM   970  C  CE  B LYS A 1 110 ? 12.67600  13.93800  77.97900  0.380 26.48381 ? 113 LYS A CE  1 
ATOM   971  N  NZ  A LYS A 1 110 ? 14.03400  12.40400  78.83500  0.620 26.61381 ? 113 LYS A NZ  1 
ATOM   972  N  NZ  B LYS A 1 110 ? 12.83100  15.03300  76.98500  0.380 24.57381 ? 113 LYS A NZ  1 
ATOM   973  N  N   . PHE A 1 111 ? 8.85100   15.51500  75.60100  1.000 9.53381  ? 114 PHE A N   1 
ATOM   974  C  CA  . PHE A 1 111 ? 9.13700   16.54200  74.61600  1.000 8.80381  ? 114 PHE A CA  1 
ATOM   975  C  C   . PHE A 1 111 ? 10.64000  16.68600  74.44800  1.000 9.35381  ? 114 PHE A C   1 
ATOM   976  O  O   . PHE A 1 111 ? 11.39700  16.65700  75.42600  1.000 11.85381 ? 114 PHE A O   1 
ATOM   977  C  CB  . PHE A 1 111 ? 8.55100   17.88900  75.04500  1.000 8.20381  ? 114 PHE A CB  1 
ATOM   978  C  CG  . PHE A 1 111 ? 7.11100   18.05000  74.67500  1.000 8.28381  ? 114 PHE A CG  1 
ATOM   979  C  CD1 . PHE A 1 111 ? 6.10900   17.60500  75.52100  1.000 10.27381 ? 114 PHE A CD1 1 
ATOM   980  C  CD2 . PHE A 1 111 ? 6.75900   18.60100  73.45700  1.000 11.13381 ? 114 PHE A CD2 1 
ATOM   981  C  CE1 . PHE A 1 111 ? 4.77500   17.74700  75.16400  1.000 10.43381 ? 114 PHE A CE1 1 
ATOM   982  C  CE2 . PHE A 1 111 ? 5.43900   18.72800  73.09500  1.000 11.20381 ? 114 PHE A CE2 1 
ATOM   983  C  CZ  . PHE A 1 111 ? 4.44600   18.30400  73.95300  1.000 8.85381  ? 114 PHE A CZ  1 
ATOM   984  N  N   . GLU A 1 112 ? 11.06400  16.82400  73.19900  1.000 8.54381  ? 115 GLU A N   1 
ATOM   985  C  CA  . GLU A 1 112 ? 12.40100  17.29900  72.84900  1.000 9.74381  ? 115 GLU A CA  1 
ATOM   986  C  C   . GLU A 1 112 ? 12.14400  18.60900  72.12700  1.000 11.91381 ? 115 GLU A C   1 
ATOM   987  O  O   . GLU A 1 112 ? 11.73600  18.61300  70.96100  1.000 10.21381 ? 115 GLU A O   1 
ATOM   988  C  CB  . GLU A 1 112 ? 13.14500  16.30900  71.95400  1.000 12.49381 ? 115 GLU A CB  1 
ATOM   989  C  CG  . GLU A 1 112 ? 13.46900  14.98600  72.63100  1.000 12.19381 ? 115 GLU A CG  1 
ATOM   990  C  CD  . GLU A 1 112 ? 14.54900  15.09300  73.69400  1.000 15.43381 ? 115 GLU A CD  1 
ATOM   991  O  OE1 . GLU A 1 112 ? 15.12500  16.18600  73.87100  1.000 13.41381 ? 115 GLU A OE1 1 
ATOM   992  O  OE2 . GLU A 1 112 ? 14.83100  14.06500  74.35000  1.000 19.04381 ? 115 GLU A OE2 1 
ATOM   993  N  N   . GLY A 1 113 ? 12.35000  19.71600  72.82800  1.000 11.49381 ? 116 GLY A N   1 
ATOM   994  C  CA  . GLY A 1 113 ? 11.90100  20.98000  72.27800  1.000 11.64381 ? 116 GLY A CA  1 
ATOM   995  C  C   . GLY A 1 113 ? 10.38800  20.97200  72.18300  1.000 12.39381 ? 116 GLY A C   1 
ATOM   996  O  O   . GLY A 1 113 ? 9.68400   20.61100  73.13100  1.000 13.77381 ? 116 GLY A O   1 
ATOM   997  N  N   . ASP A 1 114 ? 9.87800   21.33700  71.01400  1.000 10.98381 ? 117 ASP A N   1 
ATOM   998  C  CA  A ASP A 1 114 ? 8.43800   21.35400  70.79700  0.650 11.92381 ? 117 ASP A CA  1 
ATOM   999  C  CA  B ASP A 1 114 ? 8.44900   21.37900  70.74100  0.350 12.08381 ? 117 ASP A CA  1 
ATOM   1000 C  C   . ASP A 1 114 ? 7.91600   20.07400  70.16100  1.000 10.73381 ? 117 ASP A C   1 
ATOM   1001 O  O   . ASP A 1 114 ? 6.74700   20.02200  69.75500  1.000 11.83381 ? 117 ASP A O   1 
ATOM   1002 C  CB  A ASP A 1 114 ? 8.04400   22.57500  69.96800  0.650 17.21381 ? 117 ASP A CB  1 
ATOM   1003 C  CB  B ASP A 1 114 ? 8.13500   22.53300  69.78300  0.350 16.08381 ? 117 ASP A CB  1 
ATOM   1004 C  CG  A ASP A 1 114 ? 8.31500   23.86900  70.69700  0.650 15.07381 ? 117 ASP A CG  1 
ATOM   1005 C  CG  B ASP A 1 114 ? 8.59800   22.26000  68.35700  0.350 11.81381 ? 117 ASP A CG  1 
ATOM   1006 O  OD1 A ASP A 1 114 ? 8.08100   23.92000  71.92700  0.650 16.14381 ? 117 ASP A OD1 1 
ATOM   1007 O  OD1 B ASP A 1 114 ? 9.49100   21.41100  68.14700  0.350 14.65381 ? 117 ASP A OD1 1 
ATOM   1008 O  OD2 A ASP A 1 114 ? 8.78500   24.82200  70.04900  0.650 24.93381 ? 117 ASP A OD2 1 
ATOM   1009 O  OD2 B ASP A 1 114 ? 8.06700   22.90900  67.43200  0.350 29.39381 ? 117 ASP A OD2 1 
ATOM   1010 N  N   . THR A 1 115 ? 8.73800   19.03900  70.09400  1.000 10.56381 ? 118 THR A N   1 
ATOM   1011 C  CA  . THR A 1 115 ? 8.37800   17.79700  69.43000  1.000 11.59381 ? 118 THR A CA  1 
ATOM   1012 C  C   . THR A 1 115 ? 8.15300   16.71500  70.47200  1.000 9.74381  ? 118 THR A C   1 
ATOM   1013 O  O   . THR A 1 115 ? 8.97600   16.53000  71.36800  1.000 10.66381 ? 118 THR A O   1 
ATOM   1014 C  CB  . THR A 1 115 ? 9.49900   17.40500  68.47500  1.000 12.26381 ? 118 THR A CB  1 
ATOM   1015 O  OG1 . THR A 1 115 ? 9.66000   18.46400  67.52000  1.000 16.90381 ? 118 THR A OG1 1 
ATOM   1016 C  CG2 . THR A 1 115 ? 9.18000   16.11800  67.74800  1.000 12.75381 ? 118 THR A CG2 1 
ATOM   1017 N  N   . LEU A 1 116 ? 7.01500   16.03300  70.37200  1.000 7.51381  ? 119 LEU A N   1 
ATOM   1018 C  CA  . LEU A 1 116 ? 6.70500   14.92000  71.26100  1.000 7.59381  ? 119 LEU A CA  1 
ATOM   1019 C  C   . LEU A 1 116 ? 7.35900   13.66200  70.71000  1.000 7.25381  ? 119 LEU A C   1 
ATOM   1020 O  O   . LEU A 1 116 ? 7.09500   13.26100  69.57000  1.000 8.85381  ? 119 LEU A O   1 
ATOM   1021 C  CB  . LEU A 1 116 ? 5.18600   14.76900  71.35800  1.000 8.43381  ? 119 LEU A CB  1 
ATOM   1022 C  CG  . LEU A 1 116 ? 4.58400   13.83900  72.41100  1.000 7.15381  ? 119 LEU A CG  1 
ATOM   1023 C  CD1 . LEU A 1 116 ? 4.66000   12.36900  71.96300  1.000 9.65381  ? 119 LEU A CD1 1 
ATOM   1024 C  CD2 . LEU A 1 116 ? 5.24800   14.06200  73.77800  1.000 8.85381  ? 119 LEU A CD2 1 
ATOM   1025 N  N   . VAL A 1 117 ? 8.21300   13.04400  71.51400  1.000 8.01381  ? 120 VAL A N   1 
ATOM   1026 C  CA  . VAL A 1 117 ? 9.02000   11.91300  71.07500  1.000 7.29381  ? 120 VAL A CA  1 
ATOM   1027 C  C   . VAL A 1 117 ? 8.61400   10.67000  71.84600  1.000 8.93381  ? 120 VAL A C   1 
ATOM   1028 O  O   . VAL A 1 117 ? 8.41000   10.72700  73.06000  1.000 9.43381  ? 120 VAL A O   1 
ATOM   1029 C  CB  . VAL A 1 117 ? 10.51400  12.21800  71.29700  1.000 8.83381  ? 120 VAL A CB  1 
ATOM   1030 C  CG1 . VAL A 1 117 ? 11.36800  10.99700  70.98000  1.000 11.94381 ? 120 VAL A CG1 1 
ATOM   1031 C  CG2 . VAL A 1 117 ? 10.91800  13.42900  70.47100  1.000 9.75381  ? 120 VAL A CG2 1 
ATOM   1032 N  N   . ASN A 1 118 ? 8.52700   9.54500   71.13800  1.000 7.26381  ? 121 ASN A N   1 
ATOM   1033 C  CA  . ASN A 1 118 ? 8.30400   8.23000   71.73500  1.000 8.48381  ? 121 ASN A CA  1 
ATOM   1034 C  C   . ASN A 1 118 ? 9.47500   7.34500   71.32400  1.000 8.71381  ? 121 ASN A C   1 
ATOM   1035 O  O   . ASN A 1 118 ? 9.56200   6.93400   70.16400  1.000 8.60381  ? 121 ASN A O   1 
ATOM   1036 C  CB  . ASN A 1 118 ? 6.97800   7.64600   71.22700  1.000 6.85381  ? 121 ASN A CB  1 
ATOM   1037 C  CG  . ASN A 1 118 ? 6.66900   6.28600   71.82600  1.000 6.54381  ? 121 ASN A CG  1 
ATOM   1038 O  OD1 . ASN A 1 118 ? 7.24200   5.90200   72.84400  1.000 8.49381  ? 121 ASN A OD1 1 
ATOM   1039 N  ND2 . ASN A 1 118 ? 5.72700   5.56300   71.21100  1.000 6.57381  ? 121 ASN A ND2 1 
ATOM   1040 N  N   . ARG A 1 119 ? 10.38000  7.07900   72.26400  1.000 8.20381  ? 122 ARG A N   1 
ATOM   1041 C  CA  . ARG A 1 119 ? 11.54400  6.22500   72.03100  1.000 6.82381  ? 122 ARG A CA  1 
ATOM   1042 C  C   . ARG A 1 119 ? 11.28000  4.88000   72.68700  1.000 9.48381  ? 122 ARG A C   1 
ATOM   1043 O  O   . ARG A 1 119 ? 10.98400  4.83000   73.88100  1.000 10.69381 ? 122 ARG A O   1 
ATOM   1044 C  CB  . ARG A 1 119 ? 12.78900  6.82000   72.69300  1.000 11.60381 ? 122 ARG A CB  1 
ATOM   1045 C  CG  . ARG A 1 119 ? 13.42400  8.02700   72.02700  1.000 14.62381 ? 122 ARG A CG  1 
ATOM   1046 C  CD  . ARG A 1 119 ? 14.58400  8.48000   72.91900  1.000 18.38381 ? 122 ARG A CD  1 
ATOM   1047 N  NE  . ARG A 1 119 ? 15.34100  9.62200   72.42000  1.000 26.63381 ? 122 ARG A NE  1 
ATOM   1048 C  CZ  . ARG A 1 119 ? 15.17100  10.87500  72.82600  1.000 24.03381 ? 122 ARG A CZ  1 
ATOM   1049 N  NH1 . ARG A 1 119 ? 14.20500  11.20800  73.67000  1.000 20.49381 ? 122 ARG A NH1 1 
ATOM   1050 N  NH2 . ARG A 1 119 ? 15.99300  11.81700  72.37800  1.000 22.31381 ? 122 ARG A NH2 1 
ATOM   1051 N  N   . ILE A 1 120 ? 11.42100  3.79000   71.92900  1.000 7.81381  ? 123 ILE A N   1 
ATOM   1052 C  CA  . ILE A 1 120 ? 10.99500  2.47300   72.39400  1.000 7.14381  ? 123 ILE A CA  1 
ATOM   1053 C  C   . ILE A 1 120 ? 12.09900  1.44800   72.20300  1.000 9.67381  ? 123 ILE A C   1 
ATOM   1054 O  O   . ILE A 1 120 ? 12.74400  1.40800   71.15100  1.000 9.66381  ? 123 ILE A O   1 
ATOM   1055 C  CB  . ILE A 1 120 ? 9.76800   1.96400   71.61600  1.000 8.09381  ? 123 ILE A CB  1 
ATOM   1056 C  CG1 . ILE A 1 120 ? 8.67700   3.03700   71.55500  1.000 9.44381  ? 123 ILE A CG1 1 
ATOM   1057 C  CG2 . ILE A 1 120 ? 9.25600   0.65800   72.24000  1.000 11.58381 ? 123 ILE A CG2 1 
ATOM   1058 C  CD1 . ILE A 1 120 ? 8.16600   3.26300   70.16000  1.000 10.21381 ? 123 ILE A CD1 1 
ATOM   1059 N  N   . GLU A 1 121 ? 12.27300  0.59000   73.20500  1.000 8.74381  ? 124 GLU A N   1 
ATOM   1060 C  CA  A GLU A 1 121 ? 13.01500  -0.65700  73.06700  0.480 8.31381  ? 124 GLU A CA  1 
ATOM   1061 C  CA  B GLU A 1 121 ? 13.01600  -0.65500  73.06500  0.520 8.30381  ? 124 GLU A CA  1 
ATOM   1062 C  C   . GLU A 1 121 ? 12.01600  -1.80100  73.13300  1.000 8.07381  ? 124 GLU A C   1 
ATOM   1063 O  O   . GLU A 1 121 ? 11.19100  -1.85400  74.04800  1.000 8.14381  ? 124 GLU A O   1 
ATOM   1064 C  CB  A GLU A 1 121 ? 14.03400  -0.81700  74.19700  0.480 11.97381 ? 124 GLU A CB  1 
ATOM   1065 C  CB  B GLU A 1 121 ? 14.06000  -0.79400  74.17800  0.520 11.93381 ? 124 GLU A CB  1 
ATOM   1066 C  CG  A GLU A 1 121 ? 14.95600  0.36200   74.37600  0.480 13.48381 ? 124 GLU A CG  1 
ATOM   1067 C  CG  B GLU A 1 121 ? 14.94800  -2.02800  74.06500  0.520 13.35381 ? 124 GLU A CG  1 
ATOM   1068 C  CD  A GLU A 1 121 ? 15.99700  0.11800   75.44800  0.480 26.71381 ? 124 GLU A CD  1 
ATOM   1069 C  CD  B GLU A 1 121 ? 15.99900  -2.08100  75.15700  0.520 35.13381 ? 124 GLU A CD  1 
ATOM   1070 O  OE1 A GLU A 1 121 ? 16.96700  -0.61700  75.17200  0.480 26.59381 ? 124 GLU A OE1 1 
ATOM   1071 O  OE1 B GLU A 1 121 ? 16.15300  -1.07100  75.87500  0.520 31.02381 ? 124 GLU A OE1 1 
ATOM   1072 O  OE2 A GLU A 1 121 ? 15.83500  0.64400   76.56800  0.480 24.31381 ? 124 GLU A OE2 1 
ATOM   1073 O  OE2 B GLU A 1 121 ? 16.67200  -3.12600  75.29800  0.520 31.41381 ? 124 GLU A OE2 1 
ATOM   1074 N  N   . LEU A 1 122 ? 12.07600  -2.71000  72.16600  1.000 7.99381  ? 125 LEU A N   1 
ATOM   1075 C  CA  . LEU A 1 122 ? 11.12300  -3.81500  72.09900  1.000 8.39381  ? 125 LEU A CA  1 
ATOM   1076 C  C   . LEU A 1 122 ? 11.89400  -5.12500  72.08100  1.000 7.68381  ? 125 LEU A C   1 
ATOM   1077 O  O   . LEU A 1 122 ? 12.84200  -5.27100  71.31000  1.000 8.98381  ? 125 LEU A O   1 
ATOM   1078 C  CB  . LEU A 1 122 ? 10.20800  -3.69800  70.86400  1.000 7.57381  ? 125 LEU A CB  1 
ATOM   1079 C  CG  . LEU A 1 122 ? 9.16800   -4.82800  70.68100  1.000 6.48381  ? 125 LEU A CG  1 
ATOM   1080 C  CD1 . LEU A 1 122 ? 7.95100   -4.33900  69.89600  1.000 7.04381  ? 125 LEU A CD1 1 
ATOM   1081 C  CD2 . LEU A 1 122 ? 9.76100   -6.04500  69.97800  1.000 9.76381  ? 125 LEU A CD2 1 
ATOM   1082 N  N   . LYS A 1 123 ? 11.48300  -6.07100  72.92400  1.000 6.83381  ? 126 LYS A N   1 
ATOM   1083 C  CA  . LYS A 1 123 ? 12.08700  -7.39800  72.96600  1.000 7.71381  ? 126 LYS A CA  1 
ATOM   1084 C  C   . LYS A 1 123 ? 10.97500  -8.42400  72.80000  1.000 8.04381  ? 126 LYS A C   1 
ATOM   1085 O  O   . LYS A 1 123 ? 10.02300  -8.43600  73.58800  1.000 9.44381  ? 126 LYS A O   1 
ATOM   1086 C  CB  . LYS A 1 123 ? 12.82500  -7.60800  74.29500  1.000 8.20381  ? 126 LYS A CB  1 
ATOM   1087 C  CG  . LYS A 1 123 ? 13.55200  -8.95300  74.43000  1.000 11.42381 ? 126 LYS A CG  1 
ATOM   1088 C  CD  . LYS A 1 123 ? 14.73800  -9.06900  73.45900  1.000 13.22381 ? 126 LYS A CD  1 
ATOM   1089 C  CE  . LYS A 1 123 ? 15.65900  -10.27100 73.81300  1.000 9.82381  ? 126 LYS A CE  1 
ATOM   1090 N  NZ  . LYS A 1 123 ? 16.41100  -10.01000 75.08100  1.000 17.85381 ? 126 LYS A NZ  1 
ATOM   1091 N  N   . GLY A 1 124 ? 11.07800  -9.26600  71.77200  1.000 8.66381  ? 127 GLY A N   1 
ATOM   1092 C  CA  . GLY A 1 124 ? 10.10200  -10.32200 71.55200  1.000 8.22381  ? 127 GLY A CA  1 
ATOM   1093 C  C   . GLY A 1 124 ? 10.74100  -11.69100 71.65300  1.000 9.34381  ? 127 GLY A C   1 
ATOM   1094 O  O   . GLY A 1 124 ? 11.80900  -11.91500 71.08200  1.000 9.78381  ? 127 GLY A O   1 
ATOM   1095 N  N   . ILE A 1 125 ? 10.11900  -12.60600 72.39800  1.000 7.65381  ? 128 ILE A N   1 
ATOM   1096 C  CA  . ILE A 1 125 ? 10.65200  -13.95000 72.58100  1.000 8.85381  ? 128 ILE A CA  1 
ATOM   1097 C  C   . ILE A 1 125 ? 9.51000   -14.95000 72.50000  1.000 8.99381  ? 128 ILE A C   1 
ATOM   1098 O  O   . ILE A 1 125 ? 8.33100   -14.59500 72.58500  1.000 9.43381  ? 128 ILE A O   1 
ATOM   1099 C  CB  . ILE A 1 125 ? 11.42200  -14.12600 73.91400  1.000 9.11381  ? 128 ILE A CB  1 
ATOM   1100 C  CG1 . ILE A 1 125 ? 10.46700  -14.00800 75.11200  1.000 8.59381  ? 128 ILE A CG1 1 
ATOM   1101 C  CG2 . ILE A 1 125 ? 12.58700  -13.13100 74.01600  1.000 9.09381  ? 128 ILE A CG2 1 
ATOM   1102 C  CD1 . ILE A 1 125 ? 11.10400  -14.39100 76.44600  1.000 11.19381 ? 128 ILE A CD1 1 
ATOM   1103 N  N   . ASP A 1 126 ? 9.87900   -16.21400 72.32200  1.000 9.32381  ? 129 ASP A N   1 
ATOM   1104 C  CA  . ASP A 1 126 ? 8.94500   -17.33800 72.33800  1.000 7.97381  ? 129 ASP A CA  1 
ATOM   1105 C  C   . ASP A 1 126 ? 8.00700   -17.36200 71.14400  1.000 10.06381 ? 129 ASP A C   1 
ATOM   1106 O  O   . ASP A 1 126 ? 6.97600   -18.03900 71.18700  1.000 10.83381 ? 129 ASP A O   1 
ATOM   1107 C  CB  . ASP A 1 126 ? 8.14800   -17.43300 73.64500  1.000 10.71381 ? 129 ASP A CB  1 
ATOM   1108 C  CG  . ASP A 1 126 ? 9.01800   -17.79000 74.82800  1.000 22.85381 ? 129 ASP A CG  1 
ATOM   1109 O  OD1 . ASP A 1 126 ? 10.02100  -18.49200 74.61600  1.000 20.36381 ? 129 ASP A OD1 1 
ATOM   1110 O  OD2 . ASP A 1 126 ? 8.70700   -17.35000 75.95500  1.000 27.35381 ? 129 ASP A OD2 1 
ATOM   1111 N  N   . PHE A 1 127 ? 8.33500   -16.66100 70.06400  1.000 9.43381  ? 130 PHE A N   1 
ATOM   1112 C  CA  . PHE A 1 127 ? 7.48300   -16.72600 68.88300  1.000 9.60381  ? 130 PHE A CA  1 
ATOM   1113 C  C   . PHE A 1 127 ? 7.67800   -18.01200 68.09700  1.000 10.11381 ? 130 PHE A C   1 
ATOM   1114 O  O   . PHE A 1 127 ? 8.78900   -18.54700 68.00300  1.000 11.76381 ? 130 PHE A O   1 
ATOM   1115 C  CB  . PHE A 1 127 ? 7.67700   -15.49800 68.00000  1.000 10.59381 ? 130 PHE A CB  1 
ATOM   1116 C  CG  . PHE A 1 127 ? 7.05100   -14.28600 68.58100  1.000 8.99381  ? 130 PHE A CG  1 
ATOM   1117 C  CD1 . PHE A 1 127 ? 5.71100   -14.02800 68.35800  1.000 10.35381 ? 130 PHE A CD1 1 
ATOM   1118 C  CD2 . PHE A 1 127 ? 7.77500   -13.44600 69.42100  1.000 8.48381  ? 130 PHE A CD2 1 
ATOM   1119 C  CE1 . PHE A 1 127 ? 5.11400   -12.91300 68.92600  1.000 9.08381  ? 130 PHE A CE1 1 
ATOM   1120 C  CE2 . PHE A 1 127 ? 7.18200   -12.34800 69.99700  1.000 9.12381  ? 130 PHE A CE2 1 
ATOM   1121 C  CZ  . PHE A 1 127 ? 5.85700   -12.08400 69.75500  1.000 8.78381  ? 130 PHE A CZ  1 
ATOM   1122 N  N   . LYS A 1 128 ? 6.57000   -18.50300 67.54600  1.000 12.00381 ? 131 LYS A N   1 
ATOM   1123 C  CA  A LYS A 1 128 ? 6.58900   -19.68900 66.70300  0.660 10.42381 ? 131 LYS A CA  1 
ATOM   1124 C  CA  B LYS A 1 128 ? 6.59600   -19.68800 66.70600  0.340 10.55381 ? 131 LYS A CA  1 
ATOM   1125 C  C   . LYS A 1 128 ? 7.03600   -19.31500 65.29800  1.000 16.08381 ? 131 LYS A C   1 
ATOM   1126 O  O   . LYS A 1 128 ? 6.58400   -18.31700 64.73200  1.000 15.38381 ? 131 LYS A O   1 
ATOM   1127 C  CB  A LYS A 1 128 ? 5.19400   -20.31300 66.64900  0.660 10.16381 ? 131 LYS A CB  1 
ATOM   1128 C  CB  B LYS A 1 128 ? 5.21300   -20.33800 66.67100  0.340 10.35381 ? 131 LYS A CB  1 
ATOM   1129 C  CG  A LYS A 1 128 ? 4.74800   -20.94700 67.95700  0.660 14.37381 ? 131 LYS A CG  1 
ATOM   1130 C  CG  B LYS A 1 128 ? 4.80200   -20.96300 67.99500  0.340 14.31381 ? 131 LYS A CG  1 
ATOM   1131 C  CD  A LYS A 1 128 ? 3.36200   -21.58100 67.80900  0.660 21.22381 ? 131 LYS A CD  1 
ATOM   1132 C  CD  B LYS A 1 128 ? 3.41400   -21.58400 67.90800  0.340 21.35381 ? 131 LYS A CD  1 
ATOM   1133 C  CE  A LYS A 1 128 ? 2.88600   -22.19400 69.12100  0.660 30.88381 ? 131 LYS A CE  1 
ATOM   1134 C  CE  B LYS A 1 128 ? 3.05000   -22.31100 69.19500  0.340 30.84381 ? 131 LYS A CE  1 
ATOM   1135 N  NZ  A LYS A 1 128 ? 1.47400   -22.67000 69.04200  0.660 24.15381 ? 131 LYS A NZ  1 
ATOM   1136 N  NZ  B LYS A 1 128 ? 3.13900   -21.42900 70.39400  0.340 26.29381 ? 131 LYS A NZ  1 
ATOM   1137 N  N   . GLU A 1 129 ? 7.92500   -20.13800 64.73500  1.000 14.29381 ? 132 GLU A N   1 
ATOM   1138 C  CA  A GLU A 1 129 ? 8.54600   -19.80400 63.45800  0.600 18.04381 ? 132 GLU A CA  1 
ATOM   1139 C  CA  B GLU A 1 129 ? 8.54600   -19.82000 63.45200  0.400 18.17381 ? 132 GLU A CA  1 
ATOM   1140 C  C   . GLU A 1 129 ? 7.51000   -19.59500 62.36200  1.000 22.21381 ? 132 GLU A C   1 
ATOM   1141 O  O   . GLU A 1 129 ? 7.68300   -18.72500 61.50000  1.000 27.87381 ? 132 GLU A O   1 
ATOM   1142 C  CB  A GLU A 1 129 ? 9.54800   -20.88800 63.06500  0.600 24.66381 ? 132 GLU A CB  1 
ATOM   1143 C  CB  B GLU A 1 129 ? 9.50500   -20.93800 63.04900  0.400 24.66381 ? 132 GLU A CB  1 
ATOM   1144 C  CG  A GLU A 1 129 ? 10.82900  -20.84100 63.87200  0.600 35.14381 ? 132 GLU A CG  1 
ATOM   1145 C  CG  B GLU A 1 129 ? 10.82600  -20.87400 63.77100  0.400 34.82381 ? 132 GLU A CG  1 
ATOM   1146 C  CD  A GLU A 1 129 ? 10.61000  -21.10200 65.35000  0.600 31.46381 ? 132 GLU A CD  1 
ATOM   1147 C  CD  B GLU A 1 129 ? 11.51100  -19.54800 63.56300  0.400 31.43381 ? 132 GLU A CD  1 
ATOM   1148 O  OE1 A GLU A 1 129 ? 9.68000   -21.87100 65.68800  0.600 23.44381 ? 132 GLU A OE1 1 
ATOM   1149 O  OE1 B GLU A 1 129 ? 11.58100  -19.08800 62.40200  0.400 31.47381 ? 132 GLU A OE1 1 
ATOM   1150 O  OE2 A GLU A 1 129 ? 11.35600  -20.52500 66.17200  0.600 39.00381 ? 132 GLU A OE2 1 
ATOM   1151 O  OE2 B GLU A 1 129 ? 11.96600  -18.95000 64.55700  0.400 36.79381 ? 132 GLU A OE2 1 
ATOM   1152 N  N   . ASP A 1 130 ? 6.43900   -20.38200 62.36800  1.000 16.51381 ? 133 ASP A N   1 
ATOM   1153 C  CA  . ASP A 1 130 ? 5.37000   -20.21000 61.39200  1.000 22.20381 ? 133 ASP A CA  1 
ATOM   1154 C  C   . ASP A 1 130 ? 4.04400   -19.89400 62.07300  1.000 19.65381 ? 133 ASP A C   1 
ATOM   1155 O  O   . ASP A 1 130 ? 2.97600   -20.28200 61.59700  1.000 21.32381 ? 133 ASP A O   1 
ATOM   1156 C  CB  . ASP A 1 130 ? 5.25600   -21.40100 60.44500  1.000 27.66381 ? 133 ASP A CB  1 
ATOM   1157 C  CG  . ASP A 1 130 ? 4.47100   -21.06300 59.19200  1.000 43.64381 ? 133 ASP A CG  1 
ATOM   1158 O  OD1 . ASP A 1 130 ? 4.92300   -20.18700 58.42600  1.000 52.31381 ? 133 ASP A OD1 1 
ATOM   1159 O  OD2 . ASP A 1 130 ? 3.39500   -21.66000 58.98600  1.000 36.28381 ? 133 ASP A OD2 1 
ATOM   1160 N  N   . GLY A 1 131 ? 4.11100   -19.20800 63.20600  1.000 13.01381 ? 134 GLY A N   1 
ATOM   1161 C  CA  . GLY A 1 131 ? 2.93000   -18.63600 63.81200  1.000 12.66381 ? 134 GLY A CA  1 
ATOM   1162 C  C   . GLY A 1 131 ? 2.44500   -17.43600 63.02200  1.000 10.25381 ? 134 GLY A C   1 
ATOM   1163 O  O   . GLY A 1 131 ? 2.98300   -17.06100 61.98100  1.000 11.37381 ? 134 GLY A O   1 
ATOM   1164 N  N   . ASN A 1 132 ? 1.40100   -16.80700 63.55500  1.000 11.86381 ? 135 ASN A N   1 
ATOM   1165 C  CA  . ASN A 1 132 ? 0.77800   -15.69600 62.84900  1.000 10.17381 ? 135 ASN A CA  1 
ATOM   1166 C  C   . ASN A 1 132 ? 1.67000   -14.46800 62.77500  1.000 8.15381  ? 135 ASN A C   1 
ATOM   1167 O  O   . ASN A 1 132 ? 1.47500   -13.63200 61.88900  1.000 9.82381  ? 135 ASN A O   1 
ATOM   1168 C  CB  . ASN A 1 132 ? -0.51900  -15.31500 63.54700  1.000 10.22381 ? 135 ASN A CB  1 
ATOM   1169 C  CG  . ASN A 1 132 ? -1.55500  -16.38400 63.43400  1.000 11.28381 ? 135 ASN A CG  1 
ATOM   1170 O  OD1 . ASN A 1 132 ? -1.69000  -17.01800 62.38400  1.000 15.24381 ? 135 ASN A OD1 1 
ATOM   1171 N  ND2 . ASN A 1 132 ? -2.28800  -16.61200 64.51400  1.000 11.58381 ? 135 ASN A ND2 1 
ATOM   1172 N  N   . ILE A 1 133 ? 2.62400   -14.33500 63.69400  1.000 8.52381  ? 136 ILE A N   1 
ATOM   1173 C  CA  . ILE A 1 133 ? 3.51400   -13.18300 63.74300  1.000 9.87381  ? 136 ILE A CA  1 
ATOM   1174 C  C   . ILE A 1 133 ? 4.70300   -13.40700 62.81000  1.000 11.14381 ? 136 ILE A C   1 
ATOM   1175 O  O   . ILE A 1 133 ? 4.83900   -12.71400 61.79700  1.000 11.22381 ? 136 ILE A O   1 
ATOM   1176 C  CB  . ILE A 1 133 ? 3.95200   -12.85800 65.18700  1.000 11.88381 ? 136 ILE A CB  1 
ATOM   1177 C  CG1 . ILE A 1 133 ? 2.77900   -12.33200 66.02200  1.000 9.72381  ? 136 ILE A CG1 1 
ATOM   1178 C  CG2 . ILE A 1 133 ? 5.05400   -11.79800 65.19100  1.000 9.33381  ? 136 ILE A CG2 1 
ATOM   1179 C  CD1 . ILE A 1 133 ? 1.86600   -13.40300 66.57200  1.000 12.15381 ? 136 ILE A CD1 1 
ATOM   1180 N  N   . LEU A 1 134 ? 5.56400   -14.38500 63.12100  1.000 10.11381 ? 137 LEU A N   1 
ATOM   1181 C  CA  . LEU A 1 134 ? 6.74200   -14.58200 62.28000  1.000 9.49381  ? 137 LEU A CA  1 
ATOM   1182 C  C   . LEU A 1 134 ? 6.37000   -15.09300 60.89500  1.000 11.27381 ? 137 LEU A C   1 
ATOM   1183 O  O   . LEU A 1 134 ? 7.12100   -14.87600 59.93300  1.000 14.17381 ? 137 LEU A O   1 
ATOM   1184 C  CB  . LEU A 1 134 ? 7.75100   -15.49800 62.97100  1.000 11.66381 ? 137 LEU A CB  1 
ATOM   1185 C  CG  . LEU A 1 134 ? 8.41400   -14.86500 64.19400  1.000 12.20381 ? 137 LEU A CG  1 
ATOM   1186 C  CD1 . LEU A 1 134 ? 9.36000   -15.86500 64.81700  1.000 10.67381 ? 137 LEU A CD1 1 
ATOM   1187 C  CD2 . LEU A 1 134 ? 9.16000   -13.57700 63.84400  1.000 12.80381 ? 137 LEU A CD2 1 
ATOM   1188 N  N   . GLY A 1 135 ? 5.22300   -15.75000 60.77200  1.000 12.44381 ? 138 GLY A N   1 
ATOM   1189 C  CA  . GLY A 1 135 ? 4.71100   -16.18800 59.49000  1.000 12.54381 ? 138 GLY A CA  1 
ATOM   1190 C  C   . GLY A 1 135 ? 3.94800   -15.14400 58.70600  1.000 12.99381 ? 138 GLY A C   1 
ATOM   1191 O  O   . GLY A 1 135 ? 3.49400   -15.43700 57.59500  1.000 14.70381 ? 138 GLY A O   1 
ATOM   1192 N  N   . HIS A 1 136 ? 3.79100   -13.93200 59.24700  1.000 10.33381 ? 139 HIS A N   1 
ATOM   1193 C  CA  . HIS A 1 136 ? 3.12900   -12.83300 58.54300  1.000 11.53381 ? 139 HIS A CA  1 
ATOM   1194 C  C   . HIS A 1 136 ? 1.75900   -13.25000 58.02300  1.000 13.48381 ? 139 HIS A C   1 
ATOM   1195 O  O   . HIS A 1 136 ? 1.46100   -13.17000 56.82900  1.000 13.31381 ? 139 HIS A O   1 
ATOM   1196 C  CB  . HIS A 1 136 ? 3.99500   -12.28800 57.41000  1.000 11.89381 ? 139 HIS A CB  1 
ATOM   1197 C  CG  . HIS A 1 136 ? 5.23500   -11.60100 57.88000  1.000 12.98381 ? 139 HIS A CG  1 
ATOM   1198 N  ND1 . HIS A 1 136 ? 5.24200   -10.29000 58.30100  1.000 12.91381 ? 139 HIS A ND1 1 
ATOM   1199 C  CD2 . HIS A 1 136 ? 6.50700   -12.04600 58.00100  1.000 17.18381 ? 139 HIS A CD2 1 
ATOM   1200 C  CE1 . HIS A 1 136 ? 6.47200   -9.95200  58.65200  1.000 13.44381 ? 139 HIS A CE1 1 
ATOM   1201 N  NE2 . HIS A 1 136 ? 7.25600   -11.00100 58.48500  1.000 18.35381 ? 139 HIS A NE2 1 
ATOM   1202 N  N   . LYS A 1 137 ? 0.92200   -13.70000 58.94800  1.000 9.45381  ? 140 LYS A N   1 
ATOM   1203 C  CA  . LYS A 1 137 ? -0.41600  -14.16600 58.60500  1.000 8.65381  ? 140 LYS A CA  1 
ATOM   1204 C  C   . LYS A 1 137 ? -1.49800  -13.19500 59.03900  1.000 11.90381 ? 140 LYS A C   1 
ATOM   1205 O  O   . LYS A 1 137 ? -2.67800  -13.55100 59.01000  1.000 12.51381 ? 140 LYS A O   1 
ATOM   1206 C  CB  . LYS A 1 137 ? -0.67900  -15.53900 59.22000  1.000 9.58381  ? 140 LYS A CB  1 
ATOM   1207 C  CG  . LYS A 1 137 ? 0.41300   -16.53500 58.90500  1.000 11.39381 ? 140 LYS A CG  1 
ATOM   1208 C  CD  . LYS A 1 137 ? 0.07600   -17.89700 59.44300  1.000 10.98381 ? 140 LYS A CD  1 
ATOM   1209 C  CE  . LYS A 1 137 ? 1.21000   -18.85400 59.19000  1.000 14.63381 ? 140 LYS A CE  1 
ATOM   1210 N  NZ  . LYS A 1 137 ? 0.87200   -20.21600 59.68900  1.000 16.66381 ? 140 LYS A NZ  1 
ATOM   1211 N  N   . LEU A 1 138 ? -1.12900  -11.98400 59.44900  1.000 11.34381 ? 141 LEU A N   1 
ATOM   1212 C  CA  . LEU A 1 138 ? -2.09400  -11.00600 59.93400  1.000 9.02381  ? 141 LEU A CA  1 
ATOM   1213 C  C   . LEU A 1 138 ? -2.46300  -10.01800 58.83800  1.000 11.19381 ? 141 LEU A C   1 
ATOM   1214 O  O   . LEU A 1 138 ? -1.59700  -9.53500  58.10200  1.000 12.40381 ? 141 LEU A O   1 
ATOM   1215 C  CB  . LEU A 1 138 ? -1.53200  -10.24900 61.13800  1.000 9.55381  ? 141 LEU A CB  1 
ATOM   1216 C  CG  . LEU A 1 138 ? -1.11600  -11.15800 62.29300  1.000 9.80381  ? 141 LEU A CG  1 
ATOM   1217 C  CD1 . LEU A 1 138 ? -0.58500  -10.30100 63.41900  1.000 13.47381 ? 141 LEU A CD1 1 
ATOM   1218 C  CD2 . LEU A 1 138 ? -2.30000  -11.97800 62.78700  1.000 12.93381 ? 141 LEU A CD2 1 
ATOM   1219 N  N   . GLU A 1 139 ? -3.75900  -9.74400  58.72600  1.000 10.37381 ? 142 GLU A N   1 
ATOM   1220 C  CA  . GLU A 1 139 ? -4.25100  -8.78400  57.75800  1.000 9.72381  ? 142 GLU A CA  1 
ATOM   1221 C  C   . GLU A 1 139 ? -3.74600  -7.39000  58.09800  1.000 9.97381  ? 142 GLU A C   1 
ATOM   1222 O  O   . GLU A 1 139 ? -3.50900  -7.05500  59.26300  1.000 10.57381 ? 142 GLU A O   1 
ATOM   1223 C  CB  . GLU A 1 139 ? -5.77500  -8.76600  57.77300  1.000 10.27381 ? 142 GLU A CB  1 
ATOM   1224 C  CG  . GLU A 1 139 ? -6.39900  -10.07300 57.34400  1.000 11.72381 ? 142 GLU A CG  1 
ATOM   1225 C  CD  . GLU A 1 139 ? -7.91400  -10.03900 57.41700  1.000 14.70381 ? 142 GLU A CD  1 
ATOM   1226 O  OE1 . GLU A 1 139 ? -8.48700  -9.00600  57.82400  1.000 14.61381 ? 142 GLU A OE1 1 
ATOM   1227 O  OE2 . GLU A 1 139 ? -8.54100  -11.06200 57.06600  1.000 16.96381 ? 142 GLU A OE2 1 
ATOM   1228 N  N   . TYR A 1 140 ? -3.57600  -6.57500  57.05900  1.000 11.07381 ? 143 TYR A N   1 
ATOM   1229 C  CA  . TYR A 1 140 ? -3.11700  -5.19800  57.22800  1.000 9.07381  ? 143 TYR A CA  1 
ATOM   1230 C  C   . TYR A 1 140 ? -4.33700  -4.31300  57.46600  1.000 11.28381 ? 143 TYR A C   1 
ATOM   1231 O  O   . TYR A 1 140 ? -4.83000  -3.61100  56.57900  1.000 13.33381 ? 143 TYR A O   1 
ATOM   1232 C  CB  . TYR A 1 140 ? -2.32000  -4.75200  56.00800  1.000 11.45381 ? 143 TYR A CB  1 
ATOM   1233 C  CG  . TYR A 1 140 ? -1.65300  -3.41700  56.19400  1.000 10.04381 ? 143 TYR A CG  1 
ATOM   1234 C  CD1 . TYR A 1 140 ? -0.52600  -3.29100  56.99900  1.000 12.06381 ? 143 TYR A CD1 1 
ATOM   1235 C  CD2 . TYR A 1 140 ? -2.14900  -2.28100  55.57100  1.000 10.38381 ? 143 TYR A CD2 1 
ATOM   1236 C  CE1 . TYR A 1 140 ? 0.08700   -2.07000  57.17600  1.000 10.41381 ? 143 TYR A CE1 1 
ATOM   1237 C  CE2 . TYR A 1 140 ? -1.53800  -1.05600  55.73300  1.000 10.50381 ? 143 TYR A CE2 1 
ATOM   1238 C  CZ  . TYR A 1 140 ? -0.42100  -0.95500  56.53900  1.000 9.69381  ? 143 TYR A CZ  1 
ATOM   1239 O  OH  . TYR A 1 140 ? 0.17800   0.27500   56.70400  1.000 11.72381 ? 143 TYR A OH  1 
ATOM   1240 N  N   . ASN A 1 141 ? -4.83300  -4.35800  58.70100  1.000 10.90381 ? 144 ASN A N   1 
ATOM   1241 C  CA  . ASN A 1 141 ? -5.96700  -3.54300  59.12200  1.000 9.69381  ? 144 ASN A CA  1 
ATOM   1242 C  C   . ASN A 1 141 ? -5.96000  -3.51100  60.64500  1.000 12.54381 ? 144 ASN A C   1 
ATOM   1243 O  O   . ASN A 1 141 ? -5.07000  -4.08000  61.28600  1.000 10.84381 ? 144 ASN A O   1 
ATOM   1244 C  CB  . ASN A 1 141 ? -7.28200  -4.04200  58.51300  1.000 12.73381 ? 144 ASN A CB  1 
ATOM   1245 C  CG  . ASN A 1 141 ? -7.54600  -5.50000  58.80900  1.000 14.99381 ? 144 ASN A CG  1 
ATOM   1246 O  OD1 . ASN A 1 141 ? -7.36300  -5.96800  59.93900  1.000 14.09381 ? 144 ASN A OD1 1 
ATOM   1247 N  ND2 . ASN A 1 141 ? -7.98500  -6.23400  57.79200  1.000 15.36381 ? 144 ASN A ND2 1 
ATOM   1248 N  N   . TYR A 1 142 ? -6.93800  -2.82300  61.22900  1.000 10.54381 ? 145 TYR A N   1 
ATOM   1249 C  CA  . TYR A 1 142 ? -6.90200  -2.64200  62.67300  1.000 8.74381  ? 145 TYR A CA  1 
ATOM   1250 C  C   . TYR A 1 142 ? -8.30100  -2.39500  63.20100  1.000 11.39381 ? 145 TYR A C   1 
ATOM   1251 O  O   . TYR A 1 142 ? -9.05600  -1.60000  62.63500  1.000 15.20381 ? 145 TYR A O   1 
ATOM   1252 C  CB  . TYR A 1 142 ? -5.99200  -1.47000  63.07100  1.000 12.03381 ? 145 TYR A CB  1 
ATOM   1253 C  CG  . TYR A 1 142 ? -5.30000  -1.70600  64.38400  1.000 8.96381  ? 145 TYR A CG  1 
ATOM   1254 C  CD1 . TYR A 1 142 ? -4.11600  -2.42600  64.43300  1.000 9.40381  ? 145 TYR A CD1 1 
ATOM   1255 C  CD2 . TYR A 1 142 ? -5.82200  -1.20700  65.56800  1.000 10.13381 ? 145 TYR A CD2 1 
ATOM   1256 C  CE1 . TYR A 1 142 ? -3.47800  -2.67300  65.63700  1.000 7.98381  ? 145 TYR A CE1 1 
ATOM   1257 C  CE2 . TYR A 1 142 ? -5.19300  -1.43600  66.77700  1.000 9.42381  ? 145 TYR A CE2 1 
ATOM   1258 C  CZ  . TYR A 1 142 ? -4.01900  -2.16300  66.80400  1.000 8.57381  ? 145 TYR A CZ  1 
ATOM   1259 O  OH  . TYR A 1 142 ? -3.39900  -2.38900  68.00300  1.000 9.01381  ? 145 TYR A OH  1 
ATOM   1260 N  N   . ASN A 1 143 ? -8.61100  -3.04600  64.31100  1.000 10.29381 ? 146 ASN A N   1 
ATOM   1261 C  CA  . ASN A 1 143 ? -9.91200  -2.93200  64.94000  1.000 10.11381 ? 146 ASN A CA  1 
ATOM   1262 C  C   . ASN A 1 143 ? -9.92700  -1.78500  65.94800  1.000 13.03381 ? 146 ASN A C   1 
ATOM   1263 O  O   . ASN A 1 143 ? -8.89400  -1.23100  66.32400  1.000 11.95381 ? 146 ASN A O   1 
ATOM   1264 C  CB  . ASN A 1 143 ? -10.28000 -4.26000  65.61200  1.000 10.61381 ? 146 ASN A CB  1 
ATOM   1265 C  CG  . ASN A 1 143 ? -10.33100 -5.41000  64.62200  1.000 16.36381 ? 146 ASN A CG  1 
ATOM   1266 O  OD1 . ASN A 1 143 ? -9.75000  -6.47900  64.84900  1.000 20.18381 ? 146 ASN A OD1 1 
ATOM   1267 N  ND2 . ASN A 1 143 ? -11.00000 -5.18700  63.50300  1.000 16.18381 ? 146 ASN A ND2 1 
ATOM   1268 N  N   . SER A 1 144 ? -11.13200 -1.41400  66.36800  1.000 10.33381 ? 147 SER A N   1 
ATOM   1269 C  CA  . SER A 1 144 ? -11.31700 -0.41100  67.40400  1.000 11.84381 ? 147 SER A CA  1 
ATOM   1270 C  C   . SER A 1 144 ? -11.34500 -1.10100  68.75700  1.000 13.20381 ? 147 SER A C   1 
ATOM   1271 O  O   . SER A 1 144 ? -11.85400 -2.21400  68.87900  1.000 12.95381 ? 147 SER A O   1 
ATOM   1272 C  CB  . SER A 1 144 ? -12.63000 0.33300   67.17300  1.000 13.10381 ? 147 SER A CB  1 
ATOM   1273 O  OG  . SER A 1 144 ? -12.57700 1.02500   65.93300  1.000 15.02381 ? 147 SER A OG  1 
ATOM   1274 N  N   . HIS A 1 145 ? -10.78400 -0.44100  69.77200  1.000 9.79381  ? 148 HIS A N   1 
ATOM   1275 C  CA  . HIS A 1 145 ? -10.62700 -1.05000  71.08800  1.000 9.86381  ? 148 HIS A CA  1 
ATOM   1276 C  C   . HIS A 1 145 ? -10.86900 -0.00900  72.17000  1.000 15.95381 ? 148 HIS A C   1 
ATOM   1277 O  O   . HIS A 1 145 ? -10.70700 1.19400   71.95000  1.000 14.61381 ? 148 HIS A O   1 
ATOM   1278 C  CB  . HIS A 1 145 ? -9.21300  -1.61500  71.29900  1.000 14.06381 ? 148 HIS A CB  1 
ATOM   1279 C  CG  . HIS A 1 145 ? -8.80300  -2.62600  70.27800  1.000 12.05381 ? 148 HIS A CG  1 
ATOM   1280 N  ND1 . HIS A 1 145 ? -8.03100  -2.30400  69.18200  1.000 11.27381 ? 148 HIS A ND1 1 
ATOM   1281 C  CD2 . HIS A 1 145 ? -9.04200  -3.95600  70.19300  1.000 12.24381 ? 148 HIS A CD2 1 
ATOM   1282 C  CE1 . HIS A 1 145 ? -7.81400  -3.39200  68.46400  1.000 12.35381 ? 148 HIS A CE1 1 
ATOM   1283 N  NE2 . HIS A 1 145 ? -8.42400  -4.40700  69.05100  1.000 13.48381 ? 148 HIS A NE2 1 
ATOM   1284 N  N   . ASN A 1 146 ? -11.26800 -0.48600  73.35100  1.000 14.08381 ? 149 ASN A N   1 
ATOM   1285 C  CA  . ASN A 1 146 ? -11.29300 0.32300   74.55900  1.000 13.71381 ? 149 ASN A CA  1 
ATOM   1286 C  C   . ASN A 1 146 ? -10.13100 -0.07700  75.45300  1.000 20.88381 ? 149 ASN A C   1 
ATOM   1287 O  O   . ASN A 1 146 ? -9.77200  -1.25600  75.53800  1.000 21.15381 ? 149 ASN A O   1 
ATOM   1288 C  CB  . ASN A 1 146 ? -12.60700 0.17000   75.32700  1.000 16.73381 ? 149 ASN A CB  1 
ATOM   1289 C  CG  . ASN A 1 146 ? -13.81000 0.60300   74.52000  1.000 18.83381 ? 149 ASN A CG  1 
ATOM   1290 O  OD1 . ASN A 1 146 ? -13.79600 1.63900   73.84900  1.000 18.96381 ? 149 ASN A OD1 1 
ATOM   1291 N  ND2 . ASN A 1 146 ? -14.86700 -0.19300  74.57800  1.000 30.62381 ? 149 ASN A ND2 1 
ATOM   1292 N  N   . VAL A 1 147 ? -9.53400  0.91600   76.10100  1.000 17.01381 ? 150 VAL A N   1 
ATOM   1293 C  CA  . VAL A 1 147 ? -8.41200  0.71700   77.00900  1.000 16.27381 ? 150 VAL A CA  1 
ATOM   1294 C  C   . VAL A 1 147 ? -8.84000  1.24500   78.36500  1.000 19.69381 ? 150 VAL A C   1 
ATOM   1295 O  O   . VAL A 1 147 ? -9.12200  2.43800   78.50700  1.000 16.72381 ? 150 VAL A O   1 
ATOM   1296 C  CB  . VAL A 1 147 ? -7.15500  1.44600   76.51700  1.000 19.84381 ? 150 VAL A CB  1 
ATOM   1297 C  CG1 . VAL A 1 147 ? -6.07600  1.45000   77.59900  1.000 21.24381 ? 150 VAL A CG1 1 
ATOM   1298 C  CG2 . VAL A 1 147 ? -6.64400  0.79600   75.24200  1.000 21.82381 ? 150 VAL A CG2 1 
ATOM   1299 N  N   A TYR A 1 148 ? -8.85200  0.37400   79.36300  0.480 19.83381 ? 151 TYR A N   1 
ATOM   1300 N  N   B TYR A 1 148 ? -8.93200  0.35300   79.35100  0.520 19.74381 ? 151 TYR A N   1 
ATOM   1301 C  CA  A TYR A 1 148 ? -9.34300  0.72700   80.68600  0.480 15.52381 ? 151 TYR A CA  1 
ATOM   1302 C  CA  B TYR A 1 148 ? -9.34600  0.72500   80.69900  0.520 15.55381 ? 151 TYR A CA  1 
ATOM   1303 C  C   A TYR A 1 148 ? -8.16600  1.15500   81.55200  0.480 14.27381 ? 151 TYR A C   1 
ATOM   1304 C  C   B TYR A 1 148 ? -8.12000  1.18500   81.47500  0.520 14.23381 ? 151 TYR A C   1 
ATOM   1305 O  O   A TYR A 1 148 ? -7.27700  0.35100   81.85100  0.480 16.93381 ? 151 TYR A O   1 
ATOM   1306 O  O   B TYR A 1 148 ? -7.15900  0.42600   81.64100  0.520 16.76381 ? 151 TYR A O   1 
ATOM   1307 C  CB  A TYR A 1 148 ? -10.09800 -0.45900  81.27300  0.480 25.64381 ? 151 TYR A CB  1 
ATOM   1308 C  CB  B TYR A 1 148 ? -10.00200 -0.46300  81.40400  0.520 25.18381 ? 151 TYR A CB  1 
ATOM   1309 C  CG  A TYR A 1 148 ? -11.12800 -0.96500  80.29700  0.480 23.10381 ? 151 TYR A CG  1 
ATOM   1310 C  CG  B TYR A 1 148 ? -10.81700 -0.13900  82.64700  0.520 23.38381 ? 151 TYR A CG  1 
ATOM   1311 C  CD1 A TYR A 1 148 ? -12.34200 -0.31400  80.15600  0.480 19.61381 ? 151 TYR A CD1 1 
ATOM   1312 C  CD1 B TYR A 1 148 ? -11.86800 0.77400   82.60300  0.520 26.62381 ? 151 TYR A CD1 1 
ATOM   1313 C  CD2 A TYR A 1 148 ? -10.87200 -2.06300  79.48400  0.480 18.92381 ? 151 TYR A CD2 1 
ATOM   1314 C  CD2 B TYR A 1 148 ? -10.56600 -0.78800  83.85300  0.520 25.74381 ? 151 TYR A CD2 1 
ATOM   1315 C  CE1 A TYR A 1 148 ? -13.28400 -0.75100  79.25600  0.480 16.56381 ? 151 TYR A CE1 1 
ATOM   1316 C  CE1 B TYR A 1 148 ? -12.62700 1.05200   83.73300  0.520 22.03381 ? 151 TYR A CE1 1 
ATOM   1317 C  CE2 A TYR A 1 148 ? -11.81100 -2.50800  78.57500  0.480 22.02381 ? 151 TYR A CE2 1 
ATOM   1318 C  CE2 B TYR A 1 148 ? -11.31900 -0.51700  84.98800  0.520 17.82381 ? 151 TYR A CE2 1 
ATOM   1319 C  CZ  A TYR A 1 148 ? -13.01600 -1.84600  78.46800  0.480 19.87381 ? 151 TYR A CZ  1 
ATOM   1320 C  CZ  B TYR A 1 148 ? -12.34600 0.40400   84.92100  0.520 27.04381 ? 151 TYR A CZ  1 
ATOM   1321 O  OH  A TYR A 1 148 ? -13.96400 -2.27700  77.57400  0.480 16.98381 ? 151 TYR A OH  1 
ATOM   1322 O  OH  B TYR A 1 148 ? -13.09700 0.67300   86.04300  0.520 34.83381 ? 151 TYR A OH  1 
ATOM   1323 N  N   . ILE A 1 149 ? -8.16400  2.42200   81.94800  1.000 12.79381 ? 152 ILE A N   1 
ATOM   1324 C  CA  A ILE A 1 149 ? -7.06000  3.02600   82.67900  0.570 14.36381 ? 152 ILE A CA  1 
ATOM   1325 C  CA  B ILE A 1 149 ? -7.06300  3.05300   82.67000  0.430 14.37381 ? 152 ILE A CA  1 
ATOM   1326 C  C   . ILE A 1 149 ? -7.40900  3.08300   84.15300  1.000 16.44381 ? 152 ILE A C   1 
ATOM   1327 O  O   . ILE A 1 149 ? -8.52800  3.45700   84.52800  1.000 14.71381 ? 152 ILE A O   1 
ATOM   1328 C  CB  A ILE A 1 149 ? -6.77700  4.43200   82.13100  0.570 10.65381 ? 152 ILE A CB  1 
ATOM   1329 C  CB  B ILE A 1 149 ? -6.82800  4.48300   82.15200  0.430 10.67381 ? 152 ILE A CB  1 
ATOM   1330 C  CG1 A ILE A 1 149 ? -6.28400  4.32600   80.69200  0.570 18.14381 ? 152 ILE A CG1 1 
ATOM   1331 C  CG1 B ILE A 1 149 ? -6.62100  4.49600   80.63100  0.430 14.53381 ? 152 ILE A CG1 1 
ATOM   1332 C  CG2 A ILE A 1 149 ? -5.78100  5.16800   83.01300  0.570 10.56381 ? 152 ILE A CG2 1 
ATOM   1333 C  CG2 B ILE A 1 149 ? -5.65200  5.13000   82.87000  0.430 11.16381 ? 152 ILE A CG2 1 
ATOM   1334 C  CD1 A ILE A 1 149 ? -5.92500  5.62800   80.09900  0.570 10.71381 ? 152 ILE A CD1 1 
ATOM   1335 C  CD1 B ILE A 1 149 ? -5.32100  3.86100   80.17100  0.430 7.94381  ? 152 ILE A CD1 1 
ATOM   1336 N  N   . THR A 1 150 ? -6.45400  2.70700   84.99600  1.000 13.03381 ? 153 THR A N   1 
ATOM   1337 C  CA  A THR A 1 150 ? -6.59600  2.83000   86.43900  0.770 13.98381 ? 153 THR A CA  1 
ATOM   1338 C  CA  B THR A 1 150 ? -6.60200  2.84200   86.43600  0.230 14.07381 ? 153 THR A CA  1 
ATOM   1339 C  C   . THR A 1 150 ? -5.33100  3.44800   87.01900  1.000 15.58381 ? 153 THR A C   1 
ATOM   1340 O  O   . THR A 1 150 ? -4.24800  3.38100   86.42900  1.000 13.31381 ? 153 THR A O   1 
ATOM   1341 C  CB  A THR A 1 150 ? -6.86700  1.47200   87.09800  0.770 12.53381 ? 153 THR A CB  1 
ATOM   1342 C  CB  B THR A 1 150 ? -6.93900  1.50100   87.11400  0.230 12.63381 ? 153 THR A CB  1 
ATOM   1343 O  OG1 A THR A 1 150 ? -5.73800  0.61600   86.89200  0.770 15.75381 ? 153 THR A OG1 1 
ATOM   1344 O  OG1 B THR A 1 150 ? -7.42000  1.73500   88.44300  0.230 8.60381  ? 153 THR A OG1 1 
ATOM   1345 C  CG2 A THR A 1 150 ? -8.08900  0.82300   86.48800  0.770 11.67381 ? 153 THR A CG2 1 
ATOM   1346 C  CG2 B THR A 1 150 ? -5.71300  0.62600   87.19500  0.230 17.12381 ? 153 THR A CG2 1 
ATOM   1347 N  N   . ALA A 1 151 ? -5.47700  4.06300   88.18300  1.000 12.95381 ? 154 ALA A N   1 
ATOM   1348 C  CA  . ALA A 1 151 ? -4.33200  4.66300   88.84000  1.000 11.74381 ? 154 ALA A CA  1 
ATOM   1349 C  C   . ALA A 1 151 ? -3.39500  3.58700   89.38400  1.000 14.26381 ? 154 ALA A C   1 
ATOM   1350 O  O   . ALA A 1 151 ? -3.81500  2.49200   89.76400  1.000 18.05381 ? 154 ALA A O   1 
ATOM   1351 C  CB  . ALA A 1 151 ? -4.80300  5.57400   89.97300  1.000 16.22381 ? 154 ALA A CB  1 
ATOM   1352 N  N   . ASP A 1 152 ? -2.10600  3.92200   89.41100  1.000 14.05381 ? 155 ASP A N   1 
ATOM   1353 C  CA  . ASP A 1 152 ? -1.05500  3.08100   89.98400  1.000 20.96381 ? 155 ASP A CA  1 
ATOM   1354 C  C   . ASP A 1 152 ? -0.31700  3.98400   90.96800  1.000 22.08381 ? 155 ASP A C   1 
ATOM   1355 O  O   . ASP A 1 152 ? 0.74000   4.53400   90.64700  1.000 21.44381 ? 155 ASP A O   1 
ATOM   1356 C  CB  . ASP A 1 152 ? -0.13900  2.57500   88.87000  1.000 21.91381 ? 155 ASP A CB  1 
ATOM   1357 C  CG  . ASP A 1 152 ? 0.72600   1.41600   89.30900  1.000 39.36381 ? 155 ASP A CG  1 
ATOM   1358 O  OD1 . ASP A 1 152 ? 0.70600   1.08300   90.51200  1.000 30.41381 ? 155 ASP A OD1 1 
ATOM   1359 O  OD2 . ASP A 1 152 ? 1.42200   0.83900   88.44700  1.000 30.30381 ? 155 ASP A OD2 1 
ATOM   1360 N  N   . LYS A 1 153 ? -0.88200  4.13900   92.17300  1.000 19.19381 ? 156 LYS A N   1 
ATOM   1361 C  CA  . LYS A 1 153 ? -0.45500  5.22700   93.05200  1.000 23.41381 ? 156 LYS A CA  1 
ATOM   1362 C  C   . LYS A 1 153 ? 0.96800   5.03600   93.56600  1.000 28.16381 ? 156 LYS A C   1 
ATOM   1363 O  O   . LYS A 1 153 ? 1.70800   6.01500   93.72400  1.000 28.01381 ? 156 LYS A O   1 
ATOM   1364 C  CB  . LYS A 1 153 ? -1.44600  5.40600   94.20200  1.000 27.67381 ? 156 LYS A CB  1 
ATOM   1365 C  CG  . LYS A 1 153 ? -2.85200  5.73100   93.73000  1.000 37.41381 ? 156 LYS A CG  1 
ATOM   1366 C  CD  . LYS A 1 153 ? -3.49100  6.80500   94.58500  1.000 59.97381 ? 156 LYS A CD  1 
ATOM   1367 C  CE  . LYS A 1 153 ? -4.63900  7.47500   93.84800  1.000 51.26381 ? 156 LYS A CE  1 
ATOM   1368 N  NZ  . LYS A 1 153 ? -5.00000  8.76700   94.48700  1.000 53.39381 ? 156 LYS A NZ  1 
ATOM   1369 N  N   . GLN A 1 154 ? 1.37400   3.79200   93.82700  1.000 24.04381 ? 157 GLN A N   1 
ATOM   1370 C  CA  . GLN A 1 154 ? 2.72600   3.54500   94.32600  1.000 35.44381 ? 157 GLN A CA  1 
ATOM   1371 C  C   . GLN A 1 154 ? 3.78700   3.91700   93.29800  1.000 36.59381 ? 157 GLN A C   1 
ATOM   1372 O  O   . GLN A 1 154 ? 4.93000   4.21700   93.66700  1.000 27.10381 ? 157 GLN A O   1 
ATOM   1373 C  CB  . GLN A 1 154 ? 2.87600   2.08300   94.74700  1.000 40.66381 ? 157 GLN A CB  1 
ATOM   1374 C  CG  . GLN A 1 154 ? 2.07000   1.70500   95.97600  1.000 56.00381 ? 157 GLN A CG  1 
ATOM   1375 C  CD  . GLN A 1 154 ? 2.93200   1.10600   97.07000  1.000 85.44381 ? 157 GLN A CD  1 
ATOM   1376 O  OE1 . GLN A 1 154 ? 4.11600   0.83300   96.86400  1.000 52.50381 ? 157 GLN A OE1 1 
ATOM   1377 N  NE2 . GLN A 1 154 ? 2.34400   0.90300   98.24500  1.000 90.78381 ? 157 GLN A NE2 1 
ATOM   1378 N  N   . LYS A 1 155 ? 3.43700   3.88200   92.01400  1.000 25.70381 ? 158 LYS A N   1 
ATOM   1379 C  CA  A LYS A 1 155 ? 4.32100   4.29800   90.93600  0.310 17.39381 ? 158 LYS A CA  1 
ATOM   1380 C  CA  B LYS A 1 155 ? 4.33300   4.30300   90.94600  0.690 17.14381 ? 158 LYS A CA  1 
ATOM   1381 C  C   . LYS A 1 155 ? 4.11800   5.75500   90.54400  1.000 20.16381 ? 158 LYS A C   1 
ATOM   1382 O  O   . LYS A 1 155 ? 4.80400   6.23700   89.63600  1.000 21.15381 ? 158 LYS A O   1 
ATOM   1383 C  CB  A LYS A 1 155 ? 4.09300   3.41700   89.70300  0.310 21.46381 ? 158 LYS A CB  1 
ATOM   1384 C  CB  B LYS A 1 155 ? 4.14600   3.41000   89.71200  0.690 21.36381 ? 158 LYS A CB  1 
ATOM   1385 C  CG  A LYS A 1 155 ? 4.24100   1.92400   89.94500  0.310 25.71381 ? 158 LYS A CG  1 
ATOM   1386 C  CG  B LYS A 1 155 ? 4.23100   1.91500   89.98200  0.690 25.70381 ? 158 LYS A CG  1 
ATOM   1387 C  CD  A LYS A 1 155 ? 5.62700   1.43600   89.56800  0.310 26.40381 ? 158 LYS A CD  1 
ATOM   1388 C  CD  B LYS A 1 155 ? 5.64900   1.47400   90.27500  0.690 31.33381 ? 158 LYS A CD  1 
ATOM   1389 C  CE  A LYS A 1 155 ? 5.70400   -0.08300  89.59600  0.310 25.58381 ? 158 LYS A CE  1 
ATOM   1390 C  CE  B LYS A 1 155 ? 6.56900   1.68500   89.08000  0.690 29.56381 ? 158 LYS A CE  1 
ATOM   1391 N  NZ  A LYS A 1 155 ? 4.72600   -0.71800  88.67100  0.310 33.21381 ? 158 LYS A NZ  1 
ATOM   1392 N  NZ  B LYS A 1 155 ? 6.12000   0.95100   87.85800  0.690 43.55381 ? 158 LYS A NZ  1 
ATOM   1393 N  N   . ASN A 1 156 ? 3.18400   6.46000   91.19300  1.000 21.26381 ? 159 ASN A N   1 
ATOM   1394 C  CA  . ASN A 1 156 ? 2.84000   7.83400   90.82500  1.000 19.77381 ? 159 ASN A CA  1 
ATOM   1395 C  C   . ASN A 1 156 ? 2.37200   7.90800   89.37100  1.000 15.59381 ? 159 ASN A C   1 
ATOM   1396 O  O   . ASN A 1 156 ? 2.66200   8.87600   88.66300  1.000 15.29381 ? 159 ASN A O   1 
ATOM   1397 C  CB  . ASN A 1 156 ? 4.00300   8.80400   91.08600  1.000 17.07381 ? 159 ASN A CB  1 
ATOM   1398 C  CG  . ASN A 1 156 ? 3.56200   10.26200  91.14900  1.000 19.33381 ? 159 ASN A CG  1 
ATOM   1399 O  OD1 . ASN A 1 156 ? 2.45000   10.56500  91.58000  1.000 24.25381 ? 159 ASN A OD1 1 
ATOM   1400 N  ND2 . ASN A 1 156 ? 4.43600   11.17000  90.71300  1.000 20.91381 ? 159 ASN A ND2 1 
ATOM   1401 N  N   . GLY A 1 157 ? 1.66600   6.88400   88.91500  1.000 16.23381 ? 160 GLY A N   1 
ATOM   1402 C  CA  . GLY A 1 157 ? 1.33000   6.74300   87.50900  1.000 13.66381 ? 160 GLY A CA  1 
ATOM   1403 C  C   . GLY A 1 157 ? 0.03000   6.00700   87.29700  1.000 15.14381 ? 160 GLY A C   1 
ATOM   1404 O  O   . GLY A 1 157 ? -0.90200  6.11100   88.10200  1.000 14.05381 ? 160 GLY A O   1 
ATOM   1405 N  N   . ILE A 1 158 ? -0.05200  5.27900   86.18000  1.000 13.82381 ? 161 ILE A N   1 
ATOM   1406 C  CA  A ILE A 1 158 ? -1.26100  4.56200   85.80000  0.570 10.78381 ? 161 ILE A CA  1 
ATOM   1407 C  CA  B ILE A 1 158 ? -1.26100  4.57400   85.77100  0.430 10.87381 ? 161 ILE A CA  1 
ATOM   1408 C  C   . ILE A 1 158 ? -0.88600  3.18200   85.28200  1.000 10.48381 ? 161 ILE A C   1 
ATOM   1409 O  O   . ILE A 1 158 ? 0.28100   2.88200   85.00700  1.000 11.89381 ? 161 ILE A O   1 
ATOM   1410 C  CB  A ILE A 1 158 ? -2.07100  5.30800   84.72300  0.570 13.26381 ? 161 ILE A CB  1 
ATOM   1411 C  CB  B ILE A 1 158 ? -2.05400  5.32800   84.67500  0.430 13.18381 ? 161 ILE A CB  1 
ATOM   1412 C  CG1 A ILE A 1 158 ? -1.21500  5.48900   83.47600  0.570 11.82381 ? 161 ILE A CG1 1 
ATOM   1413 C  CG1 B ILE A 1 158 ? -1.20200  5.54900   83.41700  0.430 11.73381 ? 161 ILE A CG1 1 
ATOM   1414 C  CG2 A ILE A 1 158 ? -2.52100  6.64900   85.23300  0.570 12.83381 ? 161 ILE A CG2 1 
ATOM   1415 C  CG2 B ILE A 1 158 ? -2.53600  6.65400   85.19500  0.430 12.89381 ? 161 ILE A CG2 1 
ATOM   1416 C  CD1 A ILE A 1 158 ? -1.96700  5.99800   82.32400  0.570 7.70381  ? 161 ILE A CD1 1 
ATOM   1417 C  CD1 B ILE A 1 158 ? -1.40600  4.51000   82.31100  0.430 9.78381  ? 161 ILE A CD1 1 
ATOM   1418 N  N   . LYS A 1 159 ? -1.90500  2.34700   85.15700  1.000 11.71381 ? 162 LYS A N   1 
ATOM   1419 C  CA  A LYS A 1 159 ? -1.77600  1.03700   84.54300  0.630 11.84381 ? 162 LYS A CA  1 
ATOM   1420 C  CA  B LYS A 1 159 ? -1.77200  1.04200   84.53600  0.370 11.92381 ? 162 LYS A CA  1 
ATOM   1421 C  C   . LYS A 1 159 ? -3.01100  0.78000   83.69400  1.000 13.89381 ? 162 LYS A C   1 
ATOM   1422 O  O   . LYS A 1 159 ? -4.02700  1.47400   83.80800  1.000 13.78381 ? 162 LYS A O   1 
ATOM   1423 C  CB  A LYS A 1 159 ? -1.60300  -0.06000  85.59900  0.630 16.35381 ? 162 LYS A CB  1 
ATOM   1424 C  CB  B LYS A 1 159 ? -1.55400  -0.06300  85.57800  0.370 16.37381 ? 162 LYS A CB  1 
ATOM   1425 C  CG  A LYS A 1 159 ? -2.81000  -0.23600  86.48800  0.630 17.73381 ? 162 LYS A CG  1 
ATOM   1426 C  CG  B LYS A 1 159 ? -2.25600  0.19400   86.89300  0.370 15.52381 ? 162 LYS A CG  1 
ATOM   1427 C  CD  A LYS A 1 159 ? -2.52600  -1.21200  87.61900  0.630 18.93381 ? 162 LYS A CD  1 
ATOM   1428 C  CD  B LYS A 1 159 ? -2.14400  -1.00300  87.83000  0.370 18.37381 ? 162 LYS A CD  1 
ATOM   1429 C  CE  A LYS A 1 159 ? -3.76300  -1.45400  88.46300  0.630 15.56381 ? 162 LYS A CE  1 
ATOM   1430 C  CE  B LYS A 1 159 ? -2.99700  -0.81500  89.07600  0.370 15.06381 ? 162 LYS A CE  1 
ATOM   1431 N  NZ  A LYS A 1 159 ? -4.26500  -0.20900  89.09400  0.630 24.16381 ? 162 LYS A NZ  1 
ATOM   1432 N  NZ  B LYS A 1 159 ? -2.98600  -2.02300  89.94900  0.370 21.78381 ? 162 LYS A NZ  1 
ATOM   1433 N  N   . ALA A 1 160 ? -2.91100  -0.21700  82.82500  1.000 13.11381 ? 163 ALA A N   1 
ATOM   1434 C  CA  . ALA A 1 160 ? -4.03600  -0.57500  81.98100  1.000 15.36381 ? 163 ALA A CA  1 
ATOM   1435 C  C   . ALA A 1 160 ? -3.87800  -2.02200  81.56000  1.000 16.65381 ? 163 ALA A C   1 
ATOM   1436 O  O   . ALA A 1 160 ? -2.76100  -2.52200  81.42100  1.000 14.30381 ? 163 ALA A O   1 
ATOM   1437 C  CB  . ALA A 1 160 ? -4.10900  0.31300   80.73600  1.000 16.83381 ? 163 ALA A CB  1 
ATOM   1438 N  N   A ASN A 1 161 ? -5.01200  -2.69400  81.42700  0.490 16.67381 ? 164 ASN A N   1 
ATOM   1439 N  N   B ASN A 1 161 ? -5.00500  -2.69600  81.33400  0.510 16.38381 ? 164 ASN A N   1 
ATOM   1440 C  CA  A ASN A 1 161 ? -5.10200  -4.00700  80.81600  0.490 15.81381 ? 164 ASN A CA  1 
ATOM   1441 C  CA  B ASN A 1 161 ? -4.97800  -4.05000  80.78400  0.510 16.04381 ? 164 ASN A CA  1 
ATOM   1442 C  C   A ASN A 1 161 ? -6.09200  -3.88600  79.67600  0.490 18.66381 ? 164 ASN A C   1 
ATOM   1443 C  C   B ASN A 1 161 ? -6.13800  -4.22700  79.81500  0.510 15.61381 ? 164 ASN A C   1 
ATOM   1444 O  O   A ASN A 1 161 ? -7.08900  -3.16600  79.78900  0.490 15.21381 ? 164 ASN A O   1 
ATOM   1445 O  O   B ASN A 1 161 ? -7.30200  -4.04600  80.18500  0.510 14.87381 ? 164 ASN A O   1 
ATOM   1446 C  CB  A ASN A 1 161 ? -5.61900  -5.05400  81.80900  0.490 27.24381 ? 164 ASN A CB  1 
ATOM   1447 C  CB  B ASN A 1 161 ? -4.94900  -5.13900  81.87000  0.510 30.10381 ? 164 ASN A CB  1 
ATOM   1448 C  CG  A ASN A 1 161 ? -4.58400  -5.44100  82.84300  0.490 22.62381 ? 164 ASN A CG  1 
ATOM   1449 C  CG  B ASN A 1 161 ? -6.28500  -5.33900  82.55000  0.510 24.33381 ? 164 ASN A CG  1 
ATOM   1450 O  OD1 A ASN A 1 161 ? -3.84500  -6.40700  82.66200  0.490 36.75381 ? 164 ASN A OD1 1 
ATOM   1451 O  OD1 B ASN A 1 161 ? -6.67600  -4.56000  83.41900  0.510 38.46381 ? 164 ASN A OD1 1 
ATOM   1452 N  ND2 A ASN A 1 161 ? -4.53200  -4.69200  83.93800  0.490 36.17381 ? 164 ASN A ND2 1 
ATOM   1453 N  ND2 B ASN A 1 161 ? -6.98700  -6.39900  82.16800  0.510 19.03381 ? 164 ASN A ND2 1 
ATOM   1454 N  N   . PHE A 1 162 ? -5.80800  -4.56100  78.56900  1.000 12.58381 ? 165 PHE A N   1 
ATOM   1455 C  CA  . PHE A 1 162 ? -6.76200  -4.55500  77.47400  1.000 12.91381 ? 165 PHE A CA  1 
ATOM   1456 C  C   . PHE A 1 162 ? -6.37300  -5.60200  76.45400  1.000 11.35381 ? 165 PHE A C   1 
ATOM   1457 O  O   . PHE A 1 162 ? -5.23200  -6.06500  76.41000  1.000 11.73381 ? 165 PHE A O   1 
ATOM   1458 C  CB  . PHE A 1 162 ? -6.90200  -3.18900  76.79700  1.000 13.60381 ? 165 PHE A CB  1 
ATOM   1459 C  CG  . PHE A 1 162 ? -5.60600  -2.59300  76.28600  1.000 11.06381 ? 165 PHE A CG  1 
ATOM   1460 C  CD1 . PHE A 1 162 ? -4.75600  -1.89500  77.14000  1.000 11.62381 ? 165 PHE A CD1 1 
ATOM   1461 C  CD2 . PHE A 1 162 ? -5.28300  -2.65000  74.93700  1.000 10.16381 ? 165 PHE A CD2 1 
ATOM   1462 C  CE1 . PHE A 1 162 ? -3.57900  -1.30800  76.65400  1.000 10.57381 ? 165 PHE A CE1 1 
ATOM   1463 C  CE2 . PHE A 1 162 ? -4.11000  -2.06500  74.44400  1.000 8.35381  ? 165 PHE A CE2 1 
ATOM   1464 C  CZ  . PHE A 1 162 ? -3.25500  -1.39000  75.31000  1.000 9.94381  ? 165 PHE A CZ  1 
ATOM   1465 N  N   . LYS A 1 163 ? -7.34200  -5.96700  75.63100  1.000 11.71381 ? 166 LYS A N   1 
ATOM   1466 C  CA  . LYS A 1 163 ? -7.16900  -7.00800  74.63200  1.000 10.71381 ? 166 LYS A CA  1 
ATOM   1467 C  C   . LYS A 1 163 ? -7.21600  -6.36700  73.25500  1.000 10.68381 ? 166 LYS A C   1 
ATOM   1468 O  O   . LYS A 1 163 ? -8.18000  -5.66800  72.92400  1.000 15.29381 ? 166 LYS A O   1 
ATOM   1469 C  CB  . LYS A 1 163 ? -8.27800  -8.04800  74.76800  1.000 12.28381 ? 166 LYS A CB  1 
ATOM   1470 C  CG  . LYS A 1 163 ? -8.14800  -8.89000  76.01600  1.000 14.73381 ? 166 LYS A CG  1 
ATOM   1471 C  CD  . LYS A 1 163 ? -9.35200  -9.80300  76.17500  1.000 16.45381 ? 166 LYS A CD  1 
ATOM   1472 C  CE  . LYS A 1 163 ? -9.20500  -10.70800 77.38400  1.000 14.84381 ? 166 LYS A CE  1 
ATOM   1473 N  NZ  . LYS A 1 163 ? -8.18500  -11.78200 77.16000  1.000 17.88381 ? 166 LYS A NZ  1 
ATOM   1474 N  N   . ILE A 1 164 ? -6.16700  -6.57500  72.47500  1.000 8.44381  ? 167 ILE A N   1 
ATOM   1475 C  CA  . ILE A 1 164 ? -6.12800  -6.20800  71.06500  1.000 9.08381  ? 167 ILE A CA  1 
ATOM   1476 C  C   . ILE A 1 164 ? -6.38200  -7.46900  70.25900  1.000 9.44381  ? 167 ILE A C   1 
ATOM   1477 O  O   . ILE A 1 164 ? -5.84300  -8.53400  70.57300  1.000 10.69381 ? 167 ILE A O   1 
ATOM   1478 C  CB  . ILE A 1 164 ? -4.74600  -5.62400  70.70700  1.000 11.62381 ? 167 ILE A CB  1 
ATOM   1479 C  CG1 . ILE A 1 164 ? -4.50200  -4.29800  71.44800  1.000 11.42381 ? 167 ILE A CG1 1 
ATOM   1480 C  CG2 . ILE A 1 164 ? -4.60800  -5.47000  69.19900  1.000 10.57381 ? 167 ILE A CG2 1 
ATOM   1481 C  CD1 . ILE A 1 164 ? -5.43200  -3.15600  71.02200  1.000 9.82381  ? 167 ILE A CD1 1 
ATOM   1482 N  N   . ARG A 1 165 ? -7.20400  -7.36800  69.22300  1.000 10.48381 ? 168 ARG A N   1 
ATOM   1483 C  CA  A ARG A 1 165 ? -7.49600  -8.49700  68.35600  0.710 11.83381 ? 168 ARG A CA  1 
ATOM   1484 C  CA  B ARG A 1 165 ? -7.49400  -8.50000  68.35300  0.290 11.99381 ? 168 ARG A CA  1 
ATOM   1485 C  C   . ARG A 1 165 ? -7.00800  -8.17100  66.95200  1.000 12.50381 ? 168 ARG A C   1 
ATOM   1486 O  O   . ARG A 1 165 ? -7.46200  -7.19300  66.34500  1.000 13.28381 ? 168 ARG A O   1 
ATOM   1487 C  CB  A ARG A 1 165 ? -8.99300  -8.79400  68.38900  0.710 20.84381 ? 168 ARG A CB  1 
ATOM   1488 C  CB  B ARG A 1 165 ? -8.98600  -8.83300  68.35100  0.290 20.74381 ? 168 ARG A CB  1 
ATOM   1489 C  CG  A ARG A 1 165 ? -9.46400  -9.04800  69.81500  0.710 24.13381 ? 168 ARG A CG  1 
ATOM   1490 C  CG  B ARG A 1 165 ? -9.41900  -9.70400  69.52300  0.290 20.66381 ? 168 ARG A CG  1 
ATOM   1491 C  CD  A ARG A 1 165 ? -10.78300 -9.78800  69.89600  0.710 28.72381 ? 168 ARG A CD  1 
ATOM   1492 C  CD  B ARG A 1 165 ? -10.92300 -9.65700  69.71400  0.290 28.53381 ? 168 ARG A CD  1 
ATOM   1493 N  NE  A ARG A 1 165 ? -10.97000 -10.35000 71.22900  0.710 31.77381 ? 168 ARG A NE  1 
ATOM   1494 N  NE  B ARG A 1 165 ? -11.36700 -8.34500  70.17000  0.290 24.57381 ? 168 ARG A NE  1 
ATOM   1495 C  CZ  A ARG A 1 165 ? -11.31300 -9.64700  72.30100  0.710 29.22381 ? 168 ARG A CZ  1 
ATOM   1496 C  CZ  B ARG A 1 165 ? -11.46900 -7.99200  71.44400  0.290 26.53381 ? 168 ARG A CZ  1 
ATOM   1497 N  NH1 A ARG A 1 165 ? -11.53300 -8.34400  72.23400  0.710 33.10381 ? 168 ARG A NH1 1 
ATOM   1498 N  NH1 B ARG A 1 165 ? -11.17400 -8.83400  72.42100  0.290 31.94381 ? 168 ARG A NH1 1 
ATOM   1499 N  NH2 A ARG A 1 165 ? -11.45400 -10.27100 73.46700  0.710 33.20381 ? 168 ARG A NH2 1 
ATOM   1500 N  NH2 B ARG A 1 165 ? -11.87700 -6.76200  71.74600  0.290 34.50381 ? 168 ARG A NH2 1 
ATOM   1501 N  N   . HIS A 1 166 ? -6.06300  -8.96800  66.45500  1.000 8.81381  ? 169 HIS A N   1 
ATOM   1502 C  CA  . HIS A 1 166 ? -5.51100  -8.80600  65.12100  1.000 8.61381  ? 169 HIS A CA  1 
ATOM   1503 C  C   . HIS A 1 166 ? -6.17600  -9.82500  64.21400  1.000 11.28381 ? 169 HIS A C   1 
ATOM   1504 O  O   . HIS A 1 166 ? -6.20200  -11.01700 64.52700  1.000 14.76381 ? 169 HIS A O   1 
ATOM   1505 C  CB  . HIS A 1 166 ? -4.00800  -9.08100  65.11000  1.000 9.28381  ? 169 HIS A CB  1 
ATOM   1506 C  CG  . HIS A 1 166 ? -3.20000  -8.13300  65.93600  1.000 8.60381  ? 169 HIS A CG  1 
ATOM   1507 N  ND1 . HIS A 1 166 ? -3.14700  -6.77900  65.68500  1.000 8.77381  ? 169 HIS A ND1 1 
ATOM   1508 C  CD2 . HIS A 1 166 ? -2.37900  -8.35400  66.99200  1.000 9.89381  ? 169 HIS A CD2 1 
ATOM   1509 C  CE1 . HIS A 1 166 ? -2.34800  -6.20300  66.56800  1.000 9.63381  ? 169 HIS A CE1 1 
ATOM   1510 N  NE2 . HIS A 1 166 ? -1.86600  -7.13600  67.36900  1.000 9.11381  ? 169 HIS A NE2 1 
ATOM   1511 N  N   . ASN A 1 167 ? -6.68400  -9.36500  63.08800  1.000 11.52381 ? 170 ASN A N   1 
ATOM   1512 C  CA  A ASN A 1 167 ? -7.35000  -10.26000 62.15200  0.620 11.83381 ? 170 ASN A CA  1 
ATOM   1513 C  CA  B ASN A 1 167 ? -7.34900  -10.26700 62.16200  0.380 11.84381 ? 170 ASN A CA  1 
ATOM   1514 C  C   . ASN A 1 167 ? -6.32600  -11.11300 61.41600  1.000 11.03381 ? 170 ASN A C   1 
ATOM   1515 O  O   . ASN A 1 167 ? -5.32600  -10.60000 60.90000  1.000 11.82381 ? 170 ASN A O   1 
ATOM   1516 C  CB  A ASN A 1 167 ? -8.16000  -9.43600  61.15700  0.620 11.50381 ? 170 ASN A CB  1 
ATOM   1517 C  CB  B ASN A 1 167 ? -8.23100  -9.48100  61.19700  0.380 11.77381 ? 170 ASN A CB  1 
ATOM   1518 C  CG  A ASN A 1 167 ? -9.13400  -8.51500  61.84700  0.620 9.69381  ? 170 ASN A CG  1 
ATOM   1519 C  CG  B ASN A 1 167 ? -9.62900  -9.27500  61.74400  0.380 10.03381 ? 170 ASN A CG  1 
ATOM   1520 O  OD1 A ASN A 1 167 ? -9.23000  -7.33100  61.52200  0.620 26.83381 ? 170 ASN A OD1 1 
ATOM   1521 O  OD1 B ASN A 1 167 ? -10.58300 -9.91000  61.29300  0.380 36.29381 ? 170 ASN A OD1 1 
ATOM   1522 N  ND2 A ASN A 1 167 ? -9.82900  -9.03900  62.84100  0.620 9.05381  ? 170 ASN A ND2 1 
ATOM   1523 N  ND2 B ASN A 1 167 ? -9.75200  -8.41200  62.74100  0.380 12.18381 ? 170 ASN A ND2 1 
ATOM   1524 N  N   . ILE A 1 168 ? -6.57200  -12.41200 61.37900  1.000 9.19381  ? 171 ILE A N   1 
ATOM   1525 C  CA  . ILE A 1 168 ? -5.73200  -13.36400 60.66400  1.000 9.46381  ? 171 ILE A CA  1 
ATOM   1526 C  C   . ILE A 1 168 ? -6.29600  -13.52200 59.25800  1.000 10.51381 ? 171 ILE A C   1 
ATOM   1527 O  O   . ILE A 1 168 ? -7.50900  -13.40900 59.03900  1.000 10.95381 ? 171 ILE A O   1 
ATOM   1528 C  CB  . ILE A 1 168 ? -5.68000  -14.71500 61.41200  1.000 13.49381 ? 171 ILE A CB  1 
ATOM   1529 C  CG1 . ILE A 1 168 ? -5.22500  -14.52600 62.86400  1.000 10.58381 ? 171 ILE A CG1 1 
ATOM   1530 C  CG2 . ILE A 1 168 ? -4.74600  -15.68800 60.70000  1.000 12.12381 ? 171 ILE A CG2 1 
ATOM   1531 C  CD1 . ILE A 1 168 ? -5.44600  -15.78000 63.71800  1.000 9.30381  ? 171 ILE A CD1 1 
ATOM   1532 N  N   . GLU A 1 169 ? -5.40900  -13.79600 58.29500  1.000 13.08381 ? 172 GLU A N   1 
ATOM   1533 C  CA  A GLU A 1 169 ? -5.80100  -13.87400 56.89100  0.590 12.01381 ? 172 GLU A CA  1 
ATOM   1534 C  CA  B GLU A 1 169 ? -5.81700  -13.86100 56.89600  0.410 12.06381 ? 172 GLU A CA  1 
ATOM   1535 C  C   . GLU A 1 169 ? -6.82600  -14.97200 56.61700  1.000 17.33381 ? 172 GLU A C   1 
ATOM   1536 O  O   . GLU A 1 169 ? -7.51700  -14.91700 55.59300  1.000 14.35381 ? 172 GLU A O   1 
ATOM   1537 C  CB  A GLU A 1 169 ? -4.56300  -14.08100 56.01300  0.590 14.07381 ? 172 GLU A CB  1 
ATOM   1538 C  CB  B GLU A 1 169 ? -4.59200  -13.99100 55.98600  0.410 14.29381 ? 172 GLU A CB  1 
ATOM   1539 C  CG  A GLU A 1 169 ? -3.79200  -15.35200 56.31900  0.590 14.97381 ? 172 GLU A CG  1 
ATOM   1540 C  CG  B GLU A 1 169 ? -3.67400  -12.77200 56.02500  0.410 11.08381 ? 172 GLU A CG  1 
ATOM   1541 C  CD  A GLU A 1 169 ? -2.41300  -15.38600 55.66700  0.590 20.69381 ? 172 GLU A CD  1 
ATOM   1542 C  CD  B GLU A 1 169 ? -2.59800  -12.80200 54.96000  0.410 21.35381 ? 172 GLU A CD  1 
ATOM   1543 O  OE1 A GLU A 1 169 ? -2.00300  -14.36800 55.07100  0.590 23.78381 ? 172 GLU A OE1 1 
ATOM   1544 O  OE1 B GLU A 1 169 ? -2.32900  -13.88800 54.41100  0.410 25.13381 ? 172 GLU A OE1 1 
ATOM   1545 O  OE2 A GLU A 1 169 ? -1.74300  -16.43300 55.75800  0.590 23.02381 ? 172 GLU A OE2 1 
ATOM   1546 O  OE2 B GLU A 1 169 ? -2.02300  -11.73200 54.67600  0.410 22.87381 ? 172 GLU A OE2 1 
ATOM   1547 N  N   . ASP A 1 170 ? -6.94100  -15.97100 57.49100  1.000 12.89381 ? 173 ASP A N   1 
ATOM   1548 C  CA  . ASP A 1 170 ? -7.95000  -17.01300 57.30400  1.000 11.11381 ? 173 ASP A CA  1 
ATOM   1549 C  C   . ASP A 1 170 ? -9.30900  -16.62500 57.87000  1.000 12.75381 ? 173 ASP A C   1 
ATOM   1550 O  O   . ASP A 1 170 ? -10.22800 -17.45500 57.88300  1.000 15.22381 ? 173 ASP A O   1 
ATOM   1551 C  CB  . ASP A 1 170 ? -7.47300  -18.34200 57.89700  1.000 12.20381 ? 173 ASP A CB  1 
ATOM   1552 C  CG  . ASP A 1 170 ? -7.33000  -18.30200 59.41300  1.000 13.67381 ? 173 ASP A CG  1 
ATOM   1553 O  OD1 . ASP A 1 170 ? -7.53500  -17.23100 60.01300  1.000 12.08381 ? 173 ASP A OD1 1 
ATOM   1554 O  OD2 . ASP A 1 170 ? -7.02400  -19.35300 60.01300  1.000 14.44381 ? 173 ASP A OD2 1 
ATOM   1555 N  N   . GLY A 1 171 ? -9.45500  -15.39700 58.34700  1.000 10.82381 ? 174 GLY A N   1 
ATOM   1556 C  CA  . GLY A 1 171 ? -10.68500 -14.95900 58.97200  1.000 12.07381 ? 174 GLY A CA  1 
ATOM   1557 C  C   . GLY A 1 171 ? -10.71800 -15.08900 60.47900  1.000 11.27381 ? 174 GLY A C   1 
ATOM   1558 O  O   . GLY A 1 171 ? -11.64400 -14.55500 61.11100  1.000 10.95381 ? 174 GLY A O   1 
ATOM   1559 N  N   . SER A 1 172 ? -9.74700  -15.77000 61.07800  1.000 11.63381 ? 175 SER A N   1 
ATOM   1560 C  CA  . SER A 1 172 ? -9.72200  -15.92600 62.52600  1.000 9.61381  ? 175 SER A CA  1 
ATOM   1561 C  C   . SER A 1 172 ? -9.15300  -14.66200 63.16200  1.000 8.96381  ? 175 SER A C   1 
ATOM   1562 O  O   . SER A 1 172 ? -8.94500  -13.64300 62.49900  1.000 11.10381 ? 175 SER A O   1 
ATOM   1563 C  CB  . SER A 1 172 ? -8.92700  -17.16700 62.90900  1.000 11.71381 ? 175 SER A CB  1 
ATOM   1564 O  OG  . SER A 1 172 ? -9.07000  -17.43700 64.29600  1.000 10.32381 ? 175 SER A OG  1 
ATOM   1565 N  N   . VAL A 1 173 ? -8.88000  -14.71300 64.46000  1.000 8.25381  ? 176 VAL A N   1 
ATOM   1566 C  CA  A VAL A 1 173 ? -8.33200  -13.57500 65.18600  0.430 9.08381  ? 176 VAL A CA  1 
ATOM   1567 C  CA  B VAL A 1 173 ? -8.31700  -13.57200 65.17300  0.570 9.05381  ? 176 VAL A CA  1 
ATOM   1568 C  C   . VAL A 1 173 ? -7.15100  -14.03300 66.03500  1.000 11.39381 ? 176 VAL A C   1 
ATOM   1569 O  O   . VAL A 1 173 ? -7.17600  -15.12700 66.61500  1.000 11.23381 ? 176 VAL A O   1 
ATOM   1570 C  CB  A VAL A 1 173 ? -9.41200  -12.88100 66.04300  0.430 12.34381 ? 176 VAL A CB  1 
ATOM   1571 C  CB  B VAL A 1 173 ? -9.36400  -12.80100 66.00600  0.570 12.33381 ? 176 VAL A CB  1 
ATOM   1572 C  CG1 A VAL A 1 173 ? -10.21300 -13.90000 66.82900  0.430 13.20381 ? 176 VAL A CG1 1 
ATOM   1573 C  CG1 B VAL A 1 173 ? -10.26300 -11.97100 65.10000  0.570 11.46381 ? 176 VAL A CG1 1 
ATOM   1574 C  CG2 A VAL A 1 173 ? -8.78600  -11.87800 66.97700  0.430 9.46381  ? 176 VAL A CG2 1 
ATOM   1575 C  CG2 B VAL A 1 173 ? -10.19200 -13.74600 66.85500  0.570 12.33381 ? 176 VAL A CG2 1 
ATOM   1576 N  N   . GLN A 1 174 ? -6.11300  -13.19700 66.08600  1.000 9.13381  ? 177 GLN A N   1 
ATOM   1577 C  CA  . GLN A 1 174 ? -4.95200  -13.38200 66.94600  1.000 8.52381  ? 177 GLN A CA  1 
ATOM   1578 C  C   . GLN A 1 174 ? -5.07700  -12.39800 68.10500  1.000 8.46381  ? 177 GLN A C   1 
ATOM   1579 O  O   . GLN A 1 174 ? -4.93800  -11.18200 67.92100  1.000 8.67381  ? 177 GLN A O   1 
ATOM   1580 C  CB  . GLN A 1 174 ? -3.66600  -13.12900 66.15700  1.000 8.64381  ? 177 GLN A CB  1 
ATOM   1581 C  CG  . GLN A 1 174 ? -2.42900  -13.02200 67.03200  1.000 9.22381  ? 177 GLN A CG  1 
ATOM   1582 C  CD  . GLN A 1 174 ? -2.04700  -14.36400 67.63700  1.000 9.11381  ? 177 GLN A CD  1 
ATOM   1583 O  OE1 . GLN A 1 174 ? -1.67500  -15.29300 66.92000  1.000 11.97381 ? 177 GLN A OE1 1 
ATOM   1584 N  NE2 . GLN A 1 174 ? -2.14600  -14.47100 68.95100  1.000 9.84381  ? 177 GLN A NE2 1 
ATOM   1585 N  N   . LEU A 1 175 ? -5.32900  -12.92500 69.29600  1.000 9.13381  ? 178 LEU A N   1 
ATOM   1586 C  CA  . LEU A 1 175 ? -5.43600  -12.09900 70.48700  1.000 7.64381  ? 178 LEU A CA  1 
ATOM   1587 C  C   . LEU A 1 175 ? -4.05000  -11.64900 70.94200  1.000 9.53381  ? 178 LEU A C   1 
ATOM   1588 O  O   . LEU A 1 175 ? -3.09000  -12.42800 70.94100  1.000 9.42381  ? 178 LEU A O   1 
ATOM   1589 C  CB  . LEU A 1 175 ? -6.10400  -12.90500 71.59900  1.000 10.82381 ? 178 LEU A CB  1 
ATOM   1590 C  CG  . LEU A 1 175 ? -6.09200  -12.29900 72.99000  1.000 13.26381 ? 178 LEU A CG  1 
ATOM   1591 C  CD1 . LEU A 1 175 ? -6.94200  -11.04300 73.03500  1.000 11.52381 ? 178 LEU A CD1 1 
ATOM   1592 C  CD2 . LEU A 1 175 ? -6.59000  -13.33400 73.99400  1.000 10.96381 ? 178 LEU A CD2 1 
ATOM   1593 N  N   . ALA A 1 176 ? -3.95000  -10.37800 71.32100  1.000 8.71381  ? 179 ALA A N   1 
ATOM   1594 C  CA  . ALA A 1 176 ? -2.73300  -9.81300  71.90400  1.000 7.71381  ? 179 ALA A CA  1 
ATOM   1595 C  C   . ALA A 1 176 ? -3.13300  -9.15100  73.21600  1.000 10.10381 ? 179 ALA A C   1 
ATOM   1596 O  O   . ALA A 1 176 ? -3.60700  -8.01300  73.21300  1.000 9.03381  ? 179 ALA A O   1 
ATOM   1597 C  CB  . ALA A 1 176 ? -2.09300  -8.80600  70.96000  1.000 8.90381  ? 179 ALA A CB  1 
ATOM   1598 N  N   . ASP A 1 177 ? -2.97000  -9.86700  74.32500  1.000 10.17381 ? 180 ASP A N   1 
ATOM   1599 C  CA  . ASP A 1 177 ? -3.28500  -9.29300  75.62500  1.000 9.17381  ? 180 ASP A CA  1 
ATOM   1600 C  C   . ASP A 1 177 ? -2.24000  -8.24000  75.96500  1.000 9.07381  ? 180 ASP A C   1 
ATOM   1601 O  O   . ASP A 1 177 ? -1.04100  -8.49200  75.82500  1.000 10.70381 ? 180 ASP A O   1 
ATOM   1602 C  CB  . ASP A 1 177 ? -3.27400  -10.39700 76.68500  1.000 10.30381 ? 180 ASP A CB  1 
ATOM   1603 C  CG  . ASP A 1 177 ? -4.49400  -11.32000 76.59400  1.000 14.75381 ? 180 ASP A CG  1 
ATOM   1604 O  OD1 . ASP A 1 177 ? -5.63000  -10.81600 76.70800  1.000 14.90381 ? 180 ASP A OD1 1 
ATOM   1605 O  OD2 . ASP A 1 177 ? -4.31400  -12.55000 76.41800  1.000 14.80381 ? 180 ASP A OD2 1 
ATOM   1606 N  N   . HIS A 1 178 ? -2.68900  -7.06800  76.40700  1.000 8.37381  ? 181 HIS A N   1 
ATOM   1607 C  CA  . HIS A 1 178 ? -1.80500  -5.96100  76.75600  1.000 7.98381  ? 181 HIS A CA  1 
ATOM   1608 C  C   . HIS A 1 178 ? -1.88700  -5.66900  78.24300  1.000 10.95381 ? 181 HIS A C   1 
ATOM   1609 O  O   . HIS A 1 178 ? -2.97700  -5.44400  78.77100  1.000 10.59381 ? 181 HIS A O   1 
ATOM   1610 C  CB  . HIS A 1 178 ? -2.21500  -4.68400  76.02200  1.000 7.68381  ? 181 HIS A CB  1 
ATOM   1611 C  CG  . HIS A 1 178 ? -1.74500  -4.62000  74.60200  1.000 8.00381  ? 181 HIS A CG  1 
ATOM   1612 N  ND1 . HIS A 1 178 ? -2.03600  -5.59600  73.67300  1.000 7.85381  ? 181 HIS A ND1 1 
ATOM   1613 C  CD2 . HIS A 1 178 ? -1.00100  -3.69200  73.95500  1.000 8.24381  ? 181 HIS A CD2 1 
ATOM   1614 C  CE1 . HIS A 1 178 ? -1.49600  -5.26400  72.51000  1.000 6.78381  ? 181 HIS A CE1 1 
ATOM   1615 N  NE2 . HIS A 1 178 ? -0.87300  -4.10700  72.65400  1.000 8.53381  ? 181 HIS A NE2 1 
ATOM   1616 N  N   . TYR A 1 179 ? -0.73400  -5.63000  78.90200  1.000 8.32381  ? 182 TYR A N   1 
ATOM   1617 C  CA  . TYR A 1 179 ? -0.61000  -5.11300  80.25900  1.000 9.80381  ? 182 TYR A CA  1 
ATOM   1618 C  C   . TYR A 1 179 ? 0.35400   -3.94200  80.21400  1.000 9.77381  ? 182 TYR A C   1 
ATOM   1619 O  O   . TYR A 1 179 ? 1.44200   -4.06000  79.64800  1.000 10.74381 ? 182 TYR A O   1 
ATOM   1620 C  CB  . TYR A 1 179 ? -0.07100  -6.17200  81.21300  1.000 10.70381 ? 182 TYR A CB  1 
ATOM   1621 C  CG  . TYR A 1 179 ? 0.03200   -5.65100  82.62800  1.000 13.65381 ? 182 TYR A CG  1 
ATOM   1622 C  CD1 . TYR A 1 179 ? -1.10800  -5.33400  83.34500  1.000 23.84381 ? 182 TYR A CD1 1 
ATOM   1623 C  CD2 . TYR A 1 179 ? 1.26900   -5.45800  83.23200  1.000 28.30381 ? 182 TYR A CD2 1 
ATOM   1624 C  CE1 . TYR A 1 179 ? -1.02700  -4.84400  84.63100  1.000 24.89381 ? 182 TYR A CE1 1 
ATOM   1625 C  CE2 . TYR A 1 179 ? 1.35900   -4.96800  84.51800  1.000 28.97381 ? 182 TYR A CE2 1 
ATOM   1626 C  CZ  . TYR A 1 179 ? 0.20400   -4.67100  85.21100  1.000 20.24381 ? 182 TYR A CZ  1 
ATOM   1627 O  OH  . TYR A 1 179 ? 0.27600   -4.18200  86.49700  1.000 33.85381 ? 182 TYR A OH  1 
ATOM   1628 N  N   . GLN A 1 180 ? -0.02800  -2.82400  80.82100  1.000 8.73381  ? 183 GLN A N   1 
ATOM   1629 C  CA  . GLN A 1 180 ? 0.67100   -1.56900  80.61800  1.000 7.76381  ? 183 GLN A CA  1 
ATOM   1630 C  C   . GLN A 1 180 ? 0.87500   -0.86300  81.94800  1.000 8.25381  ? 183 GLN A C   1 
ATOM   1631 O  O   . GLN A 1 180 ? -0.02100  -0.86200  82.79400  1.000 9.59381  ? 183 GLN A O   1 
ATOM   1632 C  CB  . GLN A 1 180 ? -0.15400  -0.67300  79.68800  1.000 8.83381  ? 183 GLN A CB  1 
ATOM   1633 C  CG  . GLN A 1 180 ? 0.44000   0.68700   79.46300  1.000 8.64381  ? 183 GLN A CG  1 
ATOM   1634 C  CD  . GLN A 1 180 ? -0.43000  1.51700   78.56100  1.000 8.96381  ? 183 GLN A CD  1 
ATOM   1635 O  OE1 . GLN A 1 180 ? -1.21000  0.98400   77.78300  1.000 10.09381 ? 183 GLN A OE1 1 
ATOM   1636 N  NE2 . GLN A 1 180 ? -0.30500  2.83800   78.66100  1.000 9.88381  ? 183 GLN A NE2 1 
ATOM   1637 N  N   . GLN A 1 181 ? 2.05400   -0.26700  82.13300  1.000 9.59381  ? 184 GLN A N   1 
ATOM   1638 C  CA  A GLN A 1 181 ? 2.33900   0.54900   83.30800  0.580 9.90381  ? 184 GLN A CA  1 
ATOM   1639 C  CA  B GLN A 1 181 ? 2.32000   0.55700   83.30300  0.420 9.92381  ? 184 GLN A CA  1 
ATOM   1640 C  C   . GLN A 1 181 ? 3.07600   1.79700   82.86100  1.000 11.90381 ? 184 GLN A C   1 
ATOM   1641 O  O   . GLN A 1 181 ? 4.02100   1.70400   82.07200  1.000 11.51381 ? 184 GLN A O   1 
ATOM   1642 C  CB  A GLN A 1 181 ? 3.20100   -0.21800  84.32100  0.580 13.06381 ? 184 GLN A CB  1 
ATOM   1643 C  CB  B GLN A 1 181 ? 3.10900   -0.21800  84.36900  0.420 13.19381 ? 184 GLN A CB  1 
ATOM   1644 C  CG  A GLN A 1 181 ? 2.49200   -1.39400  84.96000  0.580 10.70381 ? 184 GLN A CG  1 
ATOM   1645 C  CG  B GLN A 1 181 ? 4.22400   -1.08100  83.81500  0.420 21.33381 ? 184 GLN A CG  1 
ATOM   1646 C  CD  A GLN A 1 181 ? 3.39200   -2.19100  85.89000  0.580 32.58381 ? 184 GLN A CD  1 
ATOM   1647 C  CD  B GLN A 1 181 ? 4.53600   -2.27400  84.70400  0.420 26.97381 ? 184 GLN A CD  1 
ATOM   1648 O  OE1 A GLN A 1 181 ? 4.60500   -1.99600  85.91600  0.580 32.76381 ? 184 GLN A OE1 1 
ATOM   1649 O  OE1 B GLN A 1 181 ? 5.15400   -3.24300  84.26400  0.420 31.80381 ? 184 GLN A OE1 1 
ATOM   1650 N  NE2 A GLN A 1 181 ? 2.79600   -3.09400  86.66000  0.580 40.80381 ? 184 GLN A NE2 1 
ATOM   1651 N  NE2 B GLN A 1 181 ? 4.10600   -2.21000  85.96000  0.420 25.33381 ? 184 GLN A NE2 1 
ATOM   1652 N  N   . ASN A 1 182 ? 2.64200   2.95100   83.35800  1.000 11.09381 ? 185 ASN A N   1 
ATOM   1653 C  CA  . ASN A 1 182 ? 3.24500   4.24000   83.04900  1.000 10.19381 ? 185 ASN A CA  1 
ATOM   1654 C  C   . ASN A 1 182 ? 3.69400   4.92000   84.33400  1.000 11.61381 ? 185 ASN A C   1 
ATOM   1655 O  O   . ASN A 1 182 ? 2.95500   4.94200   85.32600  1.000 12.97381 ? 185 ASN A O   1 
ATOM   1656 C  CB  . ASN A 1 182 ? 2.27000   5.16600   82.31500  1.000 11.41381 ? 185 ASN A CB  1 
ATOM   1657 C  CG  . ASN A 1 182 ? 1.93100   4.66800   80.91600  1.000 14.20381 ? 185 ASN A CG  1 
ATOM   1658 O  OD1 . ASN A 1 182 ? 1.62600   3.49500   80.72400  1.000 16.60381 ? 185 ASN A OD1 1 
ATOM   1659 N  ND2 . ASN A 1 182 ? 1.99600   5.56000   79.93000  1.000 10.63381 ? 185 ASN A ND2 1 
ATOM   1660 N  N   . THR A 1 183 ? 4.90600   5.47500   84.30300  1.000 12.40381 ? 186 THR A N   1 
ATOM   1661 C  CA  A THR A 1 183 ? 5.52200   6.16500   85.42700  0.810 12.75381 ? 186 THR A CA  1 
ATOM   1662 C  CA  B THR A 1 183 ? 5.47500   6.18800   85.43100  0.190 12.84381 ? 186 THR A CA  1 
ATOM   1663 C  C   . THR A 1 183 ? 6.07500   7.50300   84.95400  1.000 10.53381 ? 186 THR A C   1 
ATOM   1664 O  O   . THR A 1 183 ? 6.73700   7.55300   83.91600  1.000 13.01381 ? 186 THR A O   1 
ATOM   1665 C  CB  A THR A 1 183 ? 6.70100   5.32200   85.92400  0.810 15.27381 ? 186 THR A CB  1 
ATOM   1666 C  CB  B THR A 1 183 ? 6.56500   5.35300   86.11400  0.190 15.38381 ? 186 THR A CB  1 
ATOM   1667 O  OG1 A THR A 1 183 ? 6.32000   3.94500   85.97500  0.810 22.08381 ? 186 THR A OG1 1 
ATOM   1668 O  OG1 B THR A 1 183 ? 7.59300   5.04400   85.16700  0.190 13.84381 ? 186 THR A OG1 1 
ATOM   1669 C  CG2 A THR A 1 183 ? 7.14600   5.77300   87.29700  0.810 16.40381 ? 186 THR A CG2 1 
ATOM   1670 C  CG2 B THR A 1 183 ? 5.98300   4.06500   86.64500  0.190 20.25381 ? 186 THR A CG2 1 
ATOM   1671 N  N   . PRO A 1 184 ? 5.85500   8.58800   85.69100  1.000 11.98381 ? 187 PRO A N   1 
ATOM   1672 C  CA  . PRO A 1 184 ? 6.38800   9.88200   85.25800  1.000 14.06381 ? 187 PRO A CA  1 
ATOM   1673 C  C   . PRO A 1 184 ? 7.89600   9.93800   85.40400  1.000 11.66381 ? 187 PRO A C   1 
ATOM   1674 O  O   . PRO A 1 184 ? 8.47900   9.34600   86.31700  1.000 14.30381 ? 187 PRO A O   1 
ATOM   1675 C  CB  . PRO A 1 184 ? 5.71500   10.88200  86.20700  1.000 16.81381 ? 187 PRO A CB  1 
ATOM   1676 C  CG  . PRO A 1 184 ? 5.36700   10.07800  87.41300  1.000 17.94381 ? 187 PRO A CG  1 
ATOM   1677 C  CD  . PRO A 1 184 ? 5.06000   8.69600   86.92500  1.000 15.38381 ? 187 PRO A CD  1 
ATOM   1678 N  N   . ILE A 1 185 ? 8.52400   10.66800  84.48600  1.000 12.36381 ? 188 ILE A N   1 
ATOM   1679 C  CA  . ILE A 1 185 ? 9.97600   10.84800  84.49000  1.000 13.20381 ? 188 ILE A CA  1 
ATOM   1680 C  C   . ILE A 1 185 ? 10.38200  12.04000  85.34200  1.000 17.40381 ? 188 ILE A C   1 
ATOM   1681 O  O   . ILE A 1 185 ? 11.39500  11.99400  86.04700  1.000 19.74381 ? 188 ILE A O   1 
ATOM   1682 C  CB  . ILE A 1 185 ? 10.48100  11.01000  83.04400  1.000 11.88381 ? 188 ILE A CB  1 
ATOM   1683 C  CG1 . ILE A 1 185 ? 10.31000  9.70500   82.26600  1.000 11.81381 ? 188 ILE A CG1 1 
ATOM   1684 C  CG2 . ILE A 1 185 ? 11.94700  11.46700  83.02200  1.000 13.37381 ? 188 ILE A CG2 1 
ATOM   1685 C  CD1 . ILE A 1 185 ? 10.58100  9.85000   80.77500  1.000 10.08381 ? 188 ILE A CD1 1 
ATOM   1686 N  N   . GLY A 1 186 ? 9.61300   13.12200  85.26800  1.000 15.31381 ? 189 GLY A N   1 
ATOM   1687 C  CA  . GLY A 1 186 ? 9.97000   14.36500  85.90900  1.000 15.65381 ? 189 GLY A CA  1 
ATOM   1688 C  C   . GLY A 1 186 ? 9.36900   14.51400  87.28800  1.000 15.56381 ? 189 GLY A C   1 
ATOM   1689 O  O   . GLY A 1 186 ? 8.76400   13.59600  87.84600  1.000 16.44381 ? 189 GLY A O   1 
ATOM   1690 N  N   . ASP A 1 187 ? 9.54200   15.71800  87.84000  1.000 15.64381 ? 190 ASP A N   1 
ATOM   1691 C  CA  . ASP A 1 187 ? 9.19200   16.01200  89.22400  1.000 19.73381 ? 190 ASP A CA  1 
ATOM   1692 C  C   . ASP A 1 187 ? 7.98000   16.92100  89.35200  1.000 28.29381 ? 190 ASP A C   1 
ATOM   1693 O  O   . ASP A 1 187 ? 7.69600   17.40500  90.45100  1.000 23.68381 ? 190 ASP A O   1 
ATOM   1694 C  CB  . ASP A 1 187 ? 10.39000  16.60000  89.98500  1.000 16.16381 ? 190 ASP A CB  1 
ATOM   1695 C  CG  . ASP A 1 187 ? 10.82100  17.96000  89.46800  1.000 43.65381 ? 190 ASP A CG  1 
ATOM   1696 O  OD1 . ASP A 1 187 ? 10.26700  18.44200  88.45800  1.000 50.33381 ? 190 ASP A OD1 1 
ATOM   1697 O  OD2 . ASP A 1 187 ? 11.73300  18.55000  90.08700  1.000 49.26381 ? 190 ASP A OD2 1 
ATOM   1698 N  N   . GLY A 1 188 ? 7.27500   17.18100  88.26400  1.000 19.85381 ? 191 GLY A N   1 
ATOM   1699 C  CA  . GLY A 1 188 ? 6.06400   17.96200  88.34500  1.000 17.75381 ? 191 GLY A CA  1 
ATOM   1700 C  C   . GLY A 1 188 ? 4.93000   17.15300  88.91800  1.000 17.83381 ? 191 GLY A C   1 
ATOM   1701 O  O   . GLY A 1 188 ? 4.98700   15.92500  89.04300  1.000 21.33381 ? 191 GLY A O   1 
ATOM   1702 N  N   . PRO A 1 189 ? 3.85600   17.84600  89.27800  1.000 13.80381 ? 192 PRO A N   1 
ATOM   1703 C  CA  . PRO A 1 189 ? 2.67300   17.14300  89.77100  1.000 16.41381 ? 192 PRO A CA  1 
ATOM   1704 C  C   . PRO A 1 189 ? 2.00700   16.40600  88.62400  1.000 18.94381 ? 192 PRO A C   1 
ATOM   1705 O  O   . PRO A 1 189 ? 1.86700   16.93600  87.52200  1.000 21.96381 ? 192 PRO A O   1 
ATOM   1706 C  CB  . PRO A 1 189 ? 1.78500   18.27700  90.28700  1.000 19.23381 ? 192 PRO A CB  1 
ATOM   1707 C  CG  . PRO A 1 189 ? 2.15200   19.45500  89.43000  1.000 20.37381 ? 192 PRO A CG  1 
ATOM   1708 C  CD  . PRO A 1 189 ? 3.63200   19.29300  89.10500  1.000 15.17381 ? 192 PRO A CD  1 
ATOM   1709 N  N   . VAL A 1 190 ? 1.62100   15.16600  88.87700  1.000 12.97381 ? 193 VAL A N   1 
ATOM   1710 C  CA  . VAL A 1 190 ? 0.93500   14.38000  87.86500  1.000 13.18381 ? 193 VAL A CA  1 
ATOM   1711 C  C   . VAL A 1 190 ? -0.45300  14.04100  88.37600  1.000 14.14381 ? 193 VAL A C   1 
ATOM   1712 O  O   . VAL A 1 190 ? -0.70600  14.00800  89.58500  1.000 17.50381 ? 193 VAL A O   1 
ATOM   1713 C  CB  . VAL A 1 190 ? 1.71800   13.11500  87.45400  1.000 22.74381 ? 193 VAL A CB  1 
ATOM   1714 C  CG1 . VAL A 1 190 ? 3.05800   13.51200  86.84500  1.000 20.29381 ? 193 VAL A CG1 1 
ATOM   1715 C  CG2 . VAL A 1 190 ? 1.90600   12.20400  88.64700  1.000 26.23381 ? 193 VAL A CG2 1 
ATOM   1716 N  N   . LEU A 1 191 ? -1.36300  13.81700  87.44200  1.000 12.82381 ? 194 LEU A N   1 
ATOM   1717 C  CA  . LEU A 1 191 ? -2.74400  13.50600  87.77400  1.000 13.42381 ? 194 LEU A CA  1 
ATOM   1718 C  C   . LEU A 1 191 ? -2.89400  12.00100  87.93200  1.000 16.42381 ? 194 LEU A C   1 
ATOM   1719 O  O   . LEU A 1 191 ? -2.46100  11.23100  87.06900  1.000 15.90381 ? 194 LEU A O   1 
ATOM   1720 C  CB  . LEU A 1 191 ? -3.67600  14.02200  86.67900  1.000 14.15381 ? 194 LEU A CB  1 
ATOM   1721 C  CG  . LEU A 1 191 ? -3.67600  15.54800  86.61400  1.000 13.16381 ? 194 LEU A CG  1 
ATOM   1722 C  CD1 . LEU A 1 191 ? -4.48600  16.04000  85.42400  1.000 14.89381 ? 194 LEU A CD1 1 
ATOM   1723 C  CD2 . LEU A 1 191 ? -4.24300  16.09800  87.91100  1.000 15.01381 ? 194 LEU A CD2 1 
ATOM   1724 N  N   . LEU A 1 192 ? -3.50400  11.59000  89.03600  1.000 12.72381 ? 195 LEU A N   1 
ATOM   1725 C  CA  . LEU A 1 192 ? -3.78900  10.18600  89.26300  1.000 16.04381 ? 195 LEU A CA  1 
ATOM   1726 C  C   . LEU A 1 192 ? -5.27900  9.96600   89.02800  1.000 17.99381 ? 195 LEU A C   1 
ATOM   1727 O  O   . LEU A 1 192 ? -6.10200  10.43600  89.82900  1.000 18.15381 ? 195 LEU A O   1 
ATOM   1728 C  CB  . LEU A 1 192 ? -3.38800  9.79400   90.68700  1.000 13.78381 ? 195 LEU A CB  1 
ATOM   1729 C  CG  . LEU A 1 192 ? -1.90100  10.03600  90.99800  1.000 25.27381 ? 195 LEU A CG  1 
ATOM   1730 C  CD1 . LEU A 1 192 ? -1.55200  9.69900   92.44900  1.000 24.49381 ? 195 LEU A CD1 1 
ATOM   1731 C  CD2 . LEU A 1 192 ? -1.00400  9.25500   90.03100  1.000 24.44381 ? 195 LEU A CD2 1 
ATOM   1732 N  N   . PRO A 1 193 ? -5.67300  9.28700   87.95500  1.000 12.28381 ? 196 PRO A N   1 
ATOM   1733 C  CA  . PRO A 1 193 ? -7.06100  9.33300   87.48800  1.000 13.27381 ? 196 PRO A CA  1 
ATOM   1734 C  C   . PRO A 1 193 ? -7.97800  8.34300   88.19000  1.000 11.27381 ? 196 PRO A C   1 
ATOM   1735 O  O   . PRO A 1 193 ? -7.55300  7.30600   88.70200  1.000 14.12381 ? 196 PRO A O   1 
ATOM   1736 C  CB  . PRO A 1 193 ? -6.92700  8.92100   86.01400  1.000 11.87381 ? 196 PRO A CB  1 
ATOM   1737 C  CG  . PRO A 1 193 ? -5.77600  7.95300   86.03500  1.000 12.13381 ? 196 PRO A CG  1 
ATOM   1738 C  CD  . PRO A 1 193 ? -4.79900  8.54100   87.03400  1.000 12.69381 ? 196 PRO A CD  1 
ATOM   1739 N  N   . ASP A 1 194 ? -9.26500  8.68400   88.19100  1.000 12.45381 ? 197 ASP A N   1 
ATOM   1740 C  CA  . ASP A 1 194 ? -10.28800 7.67600   88.43000  1.000 11.81381 ? 197 ASP A CA  1 
ATOM   1741 C  C   . ASP A 1 194 ? -10.30600 6.68500   87.27000  1.000 13.98381 ? 197 ASP A C   1 
ATOM   1742 O  O   . ASP A 1 194 ? -9.84200  6.97900   86.16300  1.000 13.81381 ? 197 ASP A O   1 
ATOM   1743 C  CB  . ASP A 1 194 ? -11.68300 8.31200   88.48900  1.000 11.53381 ? 197 ASP A CB  1 
ATOM   1744 C  CG  . ASP A 1 194 ? -11.93000 9.09200   89.76600  1.000 27.81381 ? 197 ASP A CG  1 
ATOM   1745 O  OD1 . ASP A 1 194 ? -11.17100 8.92300   90.73800  1.000 23.57381 ? 197 ASP A OD1 1 
ATOM   1746 O  OD2 . ASP A 1 194 ? -12.90400 9.87200   89.79100  1.000 22.21381 ? 197 ASP A OD2 1 
ATOM   1747 N  N   . ASN A 1 195 ? -10.85500 5.50000   87.53000  1.000 12.15381 ? 198 ASN A N   1 
ATOM   1748 C  CA  . ASN A 1 195 ? -11.02600 4.51100   86.47600  1.000 12.95381 ? 198 ASN A CA  1 
ATOM   1749 C  C   . ASN A 1 195 ? -11.79500 5.11900   85.31500  1.000 14.83381 ? 198 ASN A C   1 
ATOM   1750 O  O   . ASN A 1 195 ? -12.82800 5.76900   85.50400  1.000 15.66381 ? 198 ASN A O   1 
ATOM   1751 C  CB  . ASN A 1 195 ? -11.81400 3.31800   87.01300  1.000 14.77381 ? 198 ASN A CB  1 
ATOM   1752 C  CG  . ASN A 1 195 ? -11.03900 2.49600   88.02100  1.000 17.48381 ? 198 ASN A CG  1 
ATOM   1753 O  OD1 . ASN A 1 195 ? -9.92400  2.83400   88.41000  1.000 17.12381 ? 198 ASN A OD1 1 
ATOM   1754 N  ND2 . ASN A 1 195 ? -11.64900 1.40800   88.47000  1.000 27.71381 ? 198 ASN A ND2 1 
ATOM   1755 N  N   . HIS A 1 196 ? -11.27700 4.93100   84.11100  1.000 13.67381 ? 199 HIS A N   1 
ATOM   1756 C  CA  . HIS A 1 196 ? -11.96300 5.40900   82.92000  1.000 11.04381 ? 199 HIS A CA  1 
ATOM   1757 C  C   . HIS A 1 196 ? -11.40600 4.64500   81.73600  1.000 12.83381 ? 199 HIS A C   1 
ATOM   1758 O  O   . HIS A 1 196 ? -10.48700 3.84100   81.87500  1.000 16.66381 ? 199 HIS A O   1 
ATOM   1759 C  CB  . HIS A 1 196 ? -11.78600 6.91600   82.73400  1.000 11.72381 ? 199 HIS A CB  1 
ATOM   1760 C  CG  . HIS A 1 196 ? -10.37800 7.32900   82.43900  1.000 11.54381 ? 199 HIS A CG  1 
ATOM   1761 N  ND1 . HIS A 1 196 ? -9.39900  7.38900   83.40800  1.000 10.44381 ? 199 HIS A ND1 1 
ATOM   1762 C  CD2 . HIS A 1 196 ? -9.79100  7.71900   81.28300  1.000 11.71381 ? 199 HIS A CD2 1 
ATOM   1763 C  CE1 . HIS A 1 196 ? -8.26500  7.79000   82.85600  1.000 11.19381 ? 199 HIS A CE1 1 
ATOM   1764 N  NE2 . HIS A 1 196 ? -8.47500  7.98800   81.56600  1.000 9.01381  ? 199 HIS A NE2 1 
ATOM   1765 N  N   . TYR A 1 197 ? -11.95500 4.90700   80.56100  1.000 14.06381 ? 200 TYR A N   1 
ATOM   1766 C  CA  A TYR A 1 197 ? -11.40200 4.24900   79.40000  0.650 14.92381 ? 200 TYR A CA  1 
ATOM   1767 C  CA  B TYR A 1 197 ? -11.59600 4.23000   79.32000  0.350 14.74381 ? 200 TYR A CA  1 
ATOM   1768 C  C   . TYR A 1 197 ? -11.09700 5.23900   78.29000  1.000 13.17381 ? 200 TYR A C   1 
ATOM   1769 O  O   . TYR A 1 197 ? -11.55100 6.39000   78.27500  1.000 10.79381 ? 200 TYR A O   1 
ATOM   1770 C  CB  A TYR A 1 197 ? -12.22800 3.04800   78.92400  0.650 15.10381 ? 200 TYR A CB  1 
ATOM   1771 C  CB  B TYR A 1 197 ? -12.83700 3.56800   78.69100  0.350 12.40381 ? 200 TYR A CB  1 
ATOM   1772 C  CG  A TYR A 1 197 ? -13.57000 3.40100   78.34900  0.650 9.98381  ? 200 TYR A CG  1 
ATOM   1773 C  CG  B TYR A 1 197 ? -13.42800 2.38800   79.43400  0.350 16.22381 ? 200 TYR A CG  1 
ATOM   1774 C  CD1 A TYR A 1 197 ? -14.68700 3.52000   79.16600  0.650 24.65381 ? 200 TYR A CD1 1 
ATOM   1775 C  CD1 B TYR A 1 197 ? -14.38600 2.57300   80.42200  0.350 24.76381 ? 200 TYR A CD1 1 
ATOM   1776 C  CD2 A TYR A 1 197 ? -13.73400 3.57600   76.98000  0.650 14.96381 ? 200 TYR A CD2 1 
ATOM   1777 C  CD2 B TYR A 1 197 ? -13.05500 1.08400   79.12000  0.350 13.74381 ? 200 TYR A CD2 1 
ATOM   1778 C  CE1 A TYR A 1 197 ? -15.92100 3.82900   78.63800  0.650 22.18381 ? 200 TYR A CE1 1 
ATOM   1779 C  CE1 B TYR A 1 197 ? -14.94100 1.49600   81.09400  0.350 21.31381 ? 200 TYR A CE1 1 
ATOM   1780 C  CE2 A TYR A 1 197 ? -14.96700 3.89500   76.44500  0.650 15.95381 ? 200 TYR A CE2 1 
ATOM   1781 C  CE2 B TYR A 1 197 ? -13.60900 -0.00200  79.78700  0.350 14.93381 ? 200 TYR A CE2 1 
ATOM   1782 C  CZ  A TYR A 1 197 ? -16.05700 4.01700   77.28100  0.650 27.57381 ? 200 TYR A CZ  1 
ATOM   1783 C  CZ  B TYR A 1 197 ? -14.55000 0.21400   80.77300  0.350 20.15381 ? 200 TYR A CZ  1 
ATOM   1784 O  OH  A TYR A 1 197 ? -17.28900 4.32700   76.76500  0.650 21.33381 ? 200 TYR A OH  1 
ATOM   1785 O  OH  B TYR A 1 197 ? -15.10300 -0.85400  81.44400  0.350 27.94381 ? 200 TYR A OH  1 
ATOM   1786 N  N   . LEU A 1 198 ? -10.22400 4.78500   77.40300  1.000 13.60381 ? 201 LEU A N   1 
ATOM   1787 C  CA  . LEU A 1 198 ? -9.94100  5.46000   76.14900  1.000 9.92381  ? 201 LEU A CA  1 
ATOM   1788 C  C   . LEU A 1 198 ? -10.59500 4.62700   75.05900  1.000 12.08381 ? 201 LEU A C   1 
ATOM   1789 O  O   . LEU A 1 198 ? -10.47500 3.39800   75.06400  1.000 15.27381 ? 201 LEU A O   1 
ATOM   1790 C  CB  . LEU A 1 198 ? -8.43800  5.53200   75.88600  1.000 11.28381 ? 201 LEU A CB  1 
ATOM   1791 C  CG  . LEU A 1 198 ? -7.56400  6.21600   76.93700  1.000 11.35381 ? 201 LEU A CG  1 
ATOM   1792 C  CD1 . LEU A 1 198 ? -6.09400  6.17300   76.53900  1.000 13.27381 ? 201 LEU A CD1 1 
ATOM   1793 C  CD2 . LEU A 1 198 ? -8.01400  7.65500   77.17200  1.000 9.62381  ? 201 LEU A CD2 1 
ATOM   1794 N  N   . SER A 1 199 ? -11.29800 5.28500   74.14600  1.000 11.16381 ? 202 SER A N   1 
ATOM   1795 C  CA  A SER A 1 199 ? -11.89400 4.63800   72.98400  0.600 11.66381 ? 202 SER A CA  1 
ATOM   1796 C  CA  B SER A 1 199 ? -11.88100 4.62600   72.98400  0.400 11.72381 ? 202 SER A CA  1 
ATOM   1797 C  C   . SER A 1 199 ? -11.04100 4.98400   71.76700  1.000 12.38381 ? 202 SER A C   1 
ATOM   1798 O  O   . SER A 1 199 ? -10.85200 6.16600   71.46200  1.000 11.57381 ? 202 SER A O   1 
ATOM   1799 C  CB  A SER A 1 199 ? -13.32200 5.14900   72.80600  0.600 14.01381 ? 202 SER A CB  1 
ATOM   1800 C  CB  B SER A 1 199 ? -13.33300 5.05000   72.77900  0.400 13.75381 ? 202 SER A CB  1 
ATOM   1801 O  OG  A SER A 1 199 ? -13.91900 4.66300   71.62500  0.600 17.51381 ? 202 SER A OG  1 
ATOM   1802 O  OG  B SER A 1 199 ? -14.15300 4.54700   73.81600  0.400 13.14381 ? 202 SER A OG  1 
ATOM   1803 N  N   . ILE A 1 200 ? -10.52200 3.96500   71.08300  1.000 11.30381 ? 203 ILE A N   1 
ATOM   1804 C  CA  A ILE A 1 200 ? -9.53600  4.14800   70.02400  0.710 10.12381 ? 203 ILE A CA  1 
ATOM   1805 C  CA  B ILE A 1 200 ? -9.54900  4.16700   70.02000  0.290 10.26381 ? 203 ILE A CA  1 
ATOM   1806 C  C   . ILE A 1 200 ? -10.05500 3.52900   68.73800  1.000 11.36381 ? 203 ILE A C   1 
ATOM   1807 O  O   . ILE A 1 200 ? -10.57800 2.40600   68.75000  1.000 12.22381 ? 203 ILE A O   1 
ATOM   1808 C  CB  A ILE A 1 200 ? -8.17400  3.52700   70.38800  0.710 10.20381 ? 203 ILE A CB  1 
ATOM   1809 C  CB  B ILE A 1 200 ? -8.16100  3.62100   70.41200  0.290 10.49381 ? 203 ILE A CB  1 
ATOM   1810 C  CG1 A ILE A 1 200 ? -7.66600  4.07300   71.72400  0.710 12.13381 ? 203 ILE A CG1 1 
ATOM   1811 C  CG1 B ILE A 1 200 ? -7.73900  4.21300   71.76000  0.290 12.42381 ? 203 ILE A CG1 1 
ATOM   1812 C  CG2 A ILE A 1 200 ? -7.14800  3.83600   69.30200  0.710 10.90381 ? 203 ILE A CG2 1 
ATOM   1813 C  CG2 B ILE A 1 200 ? -7.13400  3.94500   69.33500  0.290 10.86381 ? 203 ILE A CG2 1 
ATOM   1814 C  CD1 A ILE A 1 200 ? -7.91100  3.16800   72.90400  0.710 12.75381 ? 203 ILE A CD1 1 
ATOM   1815 C  CD1 B ILE A 1 200 ? -6.27000  4.09200   72.07000  0.290 9.02381  ? 203 ILE A CD1 1 
ATOM   1816 N  N   . GLN A 1 201 ? -9.90500  4.26200   67.63400  1.000 11.27381 ? 204 GLN A N   1 
ATOM   1817 C  CA  A GLN A 1 201 ? -10.10200 3.72400   66.29700  0.700 10.49381 ? 204 GLN A CA  1 
ATOM   1818 C  CA  B GLN A 1 201 ? -10.11600 3.75000   66.28800  0.300 10.66381 ? 204 GLN A CA  1 
ATOM   1819 C  C   . GLN A 1 201 ? -8.85700  4.02000   65.47900  1.000 11.60381 ? 204 GLN A C   1 
ATOM   1820 O  O   . GLN A 1 201 ? -8.24900  5.08800   65.61400  1.000 11.69381 ? 204 GLN A O   1 
ATOM   1821 C  CB  A GLN A 1 201 ? -11.34600 4.29900   65.60600  0.700 13.89381 ? 204 GLN A CB  1 
ATOM   1822 C  CB  B GLN A 1 201 ? -11.30400 4.43800   65.60600  0.300 14.01381 ? 204 GLN A CB  1 
ATOM   1823 C  CG  A GLN A 1 201 ? -11.29800 5.79300   65.33200  0.700 11.88381 ? 204 GLN A CG  1 
ATOM   1824 C  CG  B GLN A 1 201 ? -12.62900 4.29600   66.34300  0.300 9.49381  ? 204 GLN A CG  1 
ATOM   1825 C  CD  A GLN A 1 201 ? -12.62000 6.32500   64.78900  0.700 24.43381 ? 204 GLN A CD  1 
ATOM   1826 C  CD  B GLN A 1 201 ? -12.77500 5.26700   67.49700  0.300 22.10381 ? 204 GLN A CD  1 
ATOM   1827 O  OE1 A GLN A 1 201 ? -12.95600 6.12100   63.62300  0.700 23.93381 ? 204 GLN A OE1 1 
ATOM   1828 O  OE1 B GLN A 1 201 ? -12.50400 6.46000   67.35800  0.300 19.23381 ? 204 GLN A OE1 1 
ATOM   1829 N  NE2 A GLN A 1 201 ? -13.37400 7.00800   65.63900  0.700 21.20381 ? 204 GLN A NE2 1 
ATOM   1830 N  NE2 B GLN A 1 201 ? -13.20400 4.75900   68.64900  0.300 24.89381 ? 204 GLN A NE2 1 
ATOM   1831 N  N   . SER A 1 202 ? -8.47300  3.06000   64.64200  1.000 9.11381  ? 205 SER A N   1 
ATOM   1832 C  CA  . SER A 1 202 ? -7.23300  3.14700   63.89000  1.000 9.76381  ? 205 SER A CA  1 
ATOM   1833 C  C   . SER A 1 202 ? -7.44700  2.66400   62.46700  1.000 12.83381 ? 205 SER A C   1 
ATOM   1834 O  O   . SER A 1 202 ? -8.09700  1.64000   62.24200  1.000 14.53381 ? 205 SER A O   1 
ATOM   1835 C  CB  . SER A 1 202 ? -6.15900  2.26800   64.53700  1.000 8.83381  ? 205 SER A CB  1 
ATOM   1836 O  OG  . SER A 1 202 ? -5.95200  2.62900   65.89300  1.000 9.47381  ? 205 SER A OG  1 
ATOM   1837 N  N   . ALA A 1 203 ? -6.86900  3.38400   61.51000  1.000 9.79381  ? 206 ALA A N   1 
ATOM   1838 C  CA  . ALA A 1 203 ? -6.90700  2.99300   60.10900  1.000 8.71381  ? 206 ALA A CA  1 
ATOM   1839 C  C   . ALA A 1 203 ? -5.48400  2.92800   59.58000  1.000 7.92381  ? 206 ALA A C   1 
ATOM   1840 O  O   . ALA A 1 203 ? -4.72400  3.89400   59.71800  1.000 9.54381  ? 206 ALA A O   1 
ATOM   1841 C  CB  . ALA A 1 203 ? -7.74100  3.97400   59.28100  1.000 11.49381 ? 206 ALA A CB  1 
ATOM   1842 N  N   . LEU A 1 204 ? -5.13000  1.79200   58.99000  1.000 10.30381 ? 207 LEU A N   1 
ATOM   1843 C  CA  . LEU A 1 204 ? -3.81000  1.57300   58.41800  1.000 8.29381  ? 207 LEU A CA  1 
ATOM   1844 C  C   . LEU A 1 204 ? -3.89400  1.71200   56.90400  1.000 10.02381 ? 207 LEU A C   1 
ATOM   1845 O  O   . LEU A 1 204 ? -4.86000  1.26500   56.27900  1.000 12.35381 ? 207 LEU A O   1 
ATOM   1846 C  CB  . LEU A 1 204 ? -3.30500  0.17000   58.76100  1.000 10.98381 ? 207 LEU A CB  1 
ATOM   1847 C  CG  . LEU A 1 204 ? -3.47800  -0.30100  60.20900  1.000 11.24381 ? 207 LEU A CG  1 
ATOM   1848 C  CD1 . LEU A 1 204 ? -2.75500  -1.64400  60.42400  1.000 8.31381  ? 207 LEU A CD1 1 
ATOM   1849 C  CD2 . LEU A 1 204 ? -2.96100  0.72800   61.18800  1.000 11.27381 ? 207 LEU A CD2 1 
ATOM   1850 N  N   . SER A 1 205 ? -2.87900  2.33300   56.31600  1.000 10.22381 ? 208 SER A N   1 
ATOM   1851 C  CA  . SER A 1 205 ? -2.84100  2.49800   54.87200  1.000 10.31381 ? 208 SER A CA  1 
ATOM   1852 C  C   . SER A 1 205 ? -1.39500  2.43400   54.41400  1.000 13.67381 ? 208 SER A C   1 
ATOM   1853 O  O   . SER A 1 205 ? -0.46500  2.34300   55.22200  1.000 11.67381 ? 208 SER A O   1 
ATOM   1854 C  CB  . SER A 1 205 ? -3.51200  3.80900   54.45700  1.000 11.01381 ? 208 SER A CB  1 
ATOM   1855 O  OG  . SER A 1 205 ? -2.87100  4.92200   55.06900  1.000 12.54381 ? 208 SER A OG  1 
ATOM   1856 N  N   . LYS A 1 206 ? -1.21600  2.48000   53.09900  1.000 12.92381 ? 209 LYS A N   1 
ATOM   1857 C  CA  . LYS A 1 206 ? 0.09500   2.49800   52.47400  1.000 13.75381 ? 209 LYS A CA  1 
ATOM   1858 C  C   . LYS A 1 206 ? 0.21800   3.76000   51.64300  1.000 21.82381 ? 209 LYS A C   1 
ATOM   1859 O  O   . LYS A 1 206 ? -0.75900  4.21300   51.03500  1.000 18.88381 ? 209 LYS A O   1 
ATOM   1860 C  CB  . LYS A 1 206 ? 0.30100   1.28300   51.56900  1.000 13.21381 ? 209 LYS A CB  1 
ATOM   1861 C  CG  . LYS A 1 206 ? 0.25600   -0.04400  52.28200  1.000 14.29381 ? 209 LYS A CG  1 
ATOM   1862 C  CD  . LYS A 1 206 ? 1.43800   -0.21500  53.22500  1.000 11.88381 ? 209 LYS A CD  1 
ATOM   1863 C  CE  . LYS A 1 206 ? 1.50800   -1.67200  53.67900  1.000 12.70381 ? 209 LYS A CE  1 
ATOM   1864 N  NZ  . LYS A 1 206 ? 2.65500   -1.90800  54.59500  1.000 13.15381 ? 209 LYS A NZ  1 
ATOM   1865 N  N   . ASP A 1 207 ? 1.40700   4.33200   51.65800  1.000 14.92381 ? 210 ASP A N   1 
ATOM   1866 C  CA  . ASP A 1 207 ? 1.79100   5.46200   50.82600  1.000 18.50381 ? 210 ASP A CA  1 
ATOM   1867 C  C   . ASP A 1 207 ? 2.10100   4.86000   49.46200  1.000 18.60381 ? 210 ASP A C   1 
ATOM   1868 O  O   . ASP A 1 207 ? 3.03800   4.05900   49.32900  1.000 15.66381 ? 210 ASP A O   1 
ATOM   1869 C  CB  . ASP A 1 207 ? 3.01100   6.13400   51.46100  1.000 19.87381 ? 210 ASP A CB  1 
ATOM   1870 C  CG  . ASP A 1 207 ? 3.55600   7.30400   50.65700  1.000 33.57381 ? 210 ASP A CG  1 
ATOM   1871 O  OD1 . ASP A 1 207 ? 3.11400   7.54400   49.51600  1.000 20.61381 ? 210 ASP A OD1 1 
ATOM   1872 O  OD2 . ASP A 1 207 ? 4.45200   7.99200   51.19200  1.000 23.66381 ? 210 ASP A OD2 1 
ATOM   1873 N  N   . PRO A 1 208 ? 1.31300   5.17400   48.43600  1.000 27.98381 ? 211 PRO A N   1 
ATOM   1874 C  CA  . PRO A 1 208 ? 1.52100   4.51800   47.13700  1.000 23.49381 ? 211 PRO A CA  1 
ATOM   1875 C  C   . PRO A 1 208 ? 2.88200   4.80100   46.52600  1.000 23.22381 ? 211 PRO A C   1 
ATOM   1876 O  O   . PRO A 1 208 ? 3.35400   4.00100   45.71100  1.000 27.21381 ? 211 PRO A O   1 
ATOM   1877 C  CB  . PRO A 1 208 ? 0.37600   5.06700   46.27300  1.000 28.91381 ? 211 PRO A CB  1 
ATOM   1878 C  CG  . PRO A 1 208 ? -0.00700  6.36000   46.93200  1.000 35.66381 ? 211 PRO A CG  1 
ATOM   1879 C  CD  . PRO A 1 208 ? 0.19600   6.13100   48.40700  1.000 20.14381 ? 211 PRO A CD  1 
ATOM   1880 N  N   . ASN A 1 209 ? 3.53400   5.89100   46.91100  1.000 23.41381 ? 212 ASN A N   1 
ATOM   1881 C  CA  . ASN A 1 209 ? 4.84000   6.26100   46.37900  1.000 23.54381 ? 212 ASN A CA  1 
ATOM   1882 C  C   . ASN A 1 209 ? 5.99800   5.77400   47.23900  1.000 35.06381 ? 212 ASN A C   1 
ATOM   1883 O  O   . ASN A 1 209 ? 7.15600   6.06400   46.92000  1.000 26.32381 ? 212 ASN A O   1 
ATOM   1884 C  CB  . ASN A 1 209 ? 4.92000   7.78100   46.22700  1.000 23.64381 ? 212 ASN A CB  1 
ATOM   1885 C  CG  . ASN A 1 209 ? 3.86200   8.32000   45.29000  1.000 41.18381 ? 212 ASN A CG  1 
ATOM   1886 O  OD1 . ASN A 1 209 ? 3.46900   7.65000   44.33500  1.000 34.99381 ? 212 ASN A OD1 1 
ATOM   1887 N  ND2 . ASN A 1 209 ? 3.38700   9.52900   45.56200  1.000 45.54381 ? 212 ASN A ND2 1 
ATOM   1888 N  N   . GLU A 1 210 ? 5.72200   5.04400   48.31200  1.000 15.75381 ? 213 GLU A N   1 
ATOM   1889 C  CA  . GLU A 1 210 ? 6.74500   4.61600   49.25200  1.000 14.23381 ? 213 GLU A CA  1 
ATOM   1890 C  C   . GLU A 1 210 ? 7.09200   3.16200   48.97300  1.000 11.94381 ? 213 GLU A C   1 
ATOM   1891 O  O   . GLU A 1 210 ? 6.22900   2.28300   49.07200  1.000 18.01381 ? 213 GLU A O   1 
ATOM   1892 C  CB  . GLU A 1 210 ? 6.24500   4.76000   50.68900  1.000 15.17381 ? 213 GLU A CB  1 
ATOM   1893 C  CG  . GLU A 1 210 ? 7.27300   4.32200   51.71900  1.000 12.74381 ? 213 GLU A CG  1 
ATOM   1894 C  CD  . GLU A 1 210 ? 8.54700   5.11600   51.59800  1.000 11.99381 ? 213 GLU A CD  1 
ATOM   1895 O  OE1 . GLU A 1 210 ? 8.51800   6.32800   51.89800  1.000 13.60381 ? 213 GLU A OE1 1 
ATOM   1896 O  OE2 . GLU A 1 210 ? 9.56900   4.53200   51.18200  1.000 12.15381 ? 213 GLU A OE2 1 
ATOM   1897 N  N   . LYS A 1 211 ? 8.35900   2.90500   48.64400  1.000 15.30381 ? 214 LYS A N   1 
ATOM   1898 C  CA  . LYS A 1 211 ? 8.80800   1.54800   48.36600  1.000 14.57381 ? 214 LYS A CA  1 
ATOM   1899 C  C   . LYS A 1 211 ? 9.48800   0.87900   49.55200  1.000 16.23381 ? 214 LYS A C   1 
ATOM   1900 O  O   . LYS A 1 211 ? 9.63400   -0.34800  49.54900  1.000 17.36381 ? 214 LYS A O   1 
ATOM   1901 C  CB  . LYS A 1 211 ? 9.75200   1.53100   47.15800  1.000 21.06381 ? 214 LYS A CB  1 
ATOM   1902 C  CG  . LYS A 1 211 ? 9.10600   2.05500   45.87800  1.000 31.73381 ? 214 LYS A CG  1 
ATOM   1903 C  CD  . LYS A 1 211 ? 10.12300  2.20900   44.75700  1.000 39.87381 ? 214 LYS A CD  1 
ATOM   1904 C  CE  . LYS A 1 211 ? 11.22000  3.19800   45.11600  1.000 50.32381 ? 214 LYS A CE  1 
ATOM   1905 N  NZ  . LYS A 1 211 ? 10.70300  4.58700   45.26200  1.000 70.91381 ? 214 LYS A NZ  1 
ATOM   1906 N  N   . ARG A 1 212 ? 9.91300   1.64300   50.55500  1.000 12.65381 ? 215 ARG A N   1 
ATOM   1907 C  CA  . ARG A 1 212 ? 10.39300  1.02100   51.77700  1.000 14.46381 ? 215 ARG A CA  1 
ATOM   1908 C  C   . ARG A 1 212 ? 9.22000   0.37600   52.50700  1.000 9.48381  ? 215 ARG A C   1 
ATOM   1909 O  O   . ARG A 1 212 ? 8.05500   0.71400   52.27800  1.000 10.97381 ? 215 ARG A O   1 
ATOM   1910 C  CB  . ARG A 1 212 ? 11.07300  2.05500   52.67600  1.000 12.24381 ? 215 ARG A CB  1 
ATOM   1911 C  CG  . ARG A 1 212 ? 12.37200  2.62600   52.10300  1.000 13.13381 ? 215 ARG A CG  1 
ATOM   1912 C  CD  . ARG A 1 212 ? 12.82400  3.87600   52.86900  1.000 13.75381 ? 215 ARG A CD  1 
ATOM   1913 N  NE  . ARG A 1 212 ? 11.88100  4.97400   52.67200  1.000 12.65381 ? 215 ARG A NE  1 
ATOM   1914 C  CZ  . ARG A 1 212 ? 12.00400  6.17300   53.22400  1.000 13.02381 ? 215 ARG A CZ  1 
ATOM   1915 N  NH1 . ARG A 1 212 ? 13.01800  6.46100   54.02800  1.000 13.89381 ? 215 ARG A NH1 1 
ATOM   1916 N  NH2 . ARG A 1 212 ? 11.09400  7.10700   52.95700  1.000 15.47381 ? 215 ARG A NH2 1 
ATOM   1917 N  N   . ASP A 1 213 ? 9.53400   -0.57100  53.38800  1.000 10.61381 ? 216 ASP A N   1 
ATOM   1918 C  CA  . ASP A 1 213 ? 8.49400   -1.20300  54.19500  1.000 8.57381  ? 216 ASP A CA  1 
ATOM   1919 C  C   . ASP A 1 213 ? 8.00900   -0.18000  55.21500  1.000 10.72381 ? 216 ASP A C   1 
ATOM   1920 O  O   . ASP A 1 213 ? 8.82000   0.43400   55.91500  1.000 9.69381  ? 216 ASP A O   1 
ATOM   1921 C  CB  . ASP A 1 213 ? 9.08900   -2.42500  54.90000  1.000 10.79381 ? 216 ASP A CB  1 
ATOM   1922 C  CG  . ASP A 1 213 ? 8.03400   -3.42500  55.35400  1.000 11.54381 ? 216 ASP A CG  1 
ATOM   1923 O  OD1 . ASP A 1 213 ? 6.83000   -3.26200  55.04900  1.000 12.91381 ? 216 ASP A OD1 1 
ATOM   1924 O  OD2 . ASP A 1 213 ? 8.42200   -4.39700  56.03000  1.000 13.33381 ? 216 ASP A OD2 1 
ATOM   1925 N  N   . HIS A 1 214 ? 6.69500   0.03700   55.27700  1.000 11.26381 ? 217 HIS A N   1 
ATOM   1926 C  CA  . HIS A 1 214 ? 6.18700   1.19000   56.01200  1.000 8.68381  ? 217 HIS A CA  1 
ATOM   1927 C  C   . HIS A 1 214 ? 4.74300   0.95700   56.42800  1.000 8.81381  ? 217 HIS A C   1 
ATOM   1928 O  O   . HIS A 1 214 ? 4.08200   0.01400   55.97500  1.000 9.16381  ? 217 HIS A O   1 
ATOM   1929 C  CB  . HIS A 1 214 ? 6.30100   2.46900   55.17000  1.000 10.76381 ? 217 HIS A CB  1 
ATOM   1930 C  CG  . HIS A 1 214 ? 5.30000   2.54000   54.06200  1.000 10.84381 ? 217 HIS A CG  1 
ATOM   1931 N  ND1 . HIS A 1 214 ? 5.41300   1.78900   52.91100  1.000 11.17381 ? 217 HIS A ND1 1 
ATOM   1932 C  CD2 . HIS A 1 214 ? 4.14900   3.24300   53.94200  1.000 13.41381 ? 217 HIS A CD2 1 
ATOM   1933 C  CE1 . HIS A 1 214 ? 4.38500   2.04400   52.12000  1.000 14.14381 ? 217 HIS A CE1 1 
ATOM   1934 N  NE2 . HIS A 1 214 ? 3.60200   2.91900   52.72400  1.000 12.46381 ? 217 HIS A NE2 1 
ATOM   1935 N  N   . MET A 1 215 ? 4.25400   1.85800   57.28200  1.000 9.13381  ? 218 MET A N   1 
ATOM   1936 C  CA  . MET A 1 215 ? 2.85100   1.87600   57.68200  1.000 8.56381  ? 218 MET A CA  1 
ATOM   1937 C  C   . MET A 1 215 ? 2.41600   3.31900   57.89400  1.000 8.50381  ? 218 MET A C   1 
ATOM   1938 O  O   . MET A 1 215 ? 3.11000   4.08800   58.56500  1.000 8.82381  ? 218 MET A O   1 
ATOM   1939 C  CB  . MET A 1 215 ? 2.63800   1.06800   58.97000  1.000 8.37381  ? 218 MET A CB  1 
ATOM   1940 C  CG  . MET A 1 215 ? 1.27300   1.29200   59.62900  1.000 7.48381  ? 218 MET A CG  1 
ATOM   1941 S  SD  . MET A 1 215 ? 0.94900   0.18900   61.02900  1.000 9.05381  ? 218 MET A SD  1 
ATOM   1942 C  CE  . MET A 1 215 ? 2.06600   0.90500   62.23600  1.000 9.81381  ? 218 MET A CE  1 
ATOM   1943 N  N   . VAL A 1 216 ? 1.25900   3.67300   57.33000  1.000 8.80381  ? 219 VAL A N   1 
ATOM   1944 C  CA  . VAL A 1 216 ? 0.59900   4.94600   57.61400  1.000 10.22381 ? 219 VAL A CA  1 
ATOM   1945 C  C   . VAL A 1 216 ? -0.55800  4.66800   58.56100  1.000 8.40381  ? 219 VAL A C   1 
ATOM   1946 O  O   . VAL A 1 216 ? -1.35400  3.74700   58.32900  1.000 9.92381  ? 219 VAL A O   1 
ATOM   1947 C  CB  . VAL A 1 216 ? 0.11400   5.63600   56.32600  1.000 10.61381 ? 219 VAL A CB  1 
ATOM   1948 C  CG1 . VAL A 1 216 ? -0.68800  6.88900   56.65800  1.000 12.85381 ? 219 VAL A CG1 1 
ATOM   1949 C  CG2 . VAL A 1 216 ? 1.30700   5.98700   55.42400  1.000 12.74381 ? 219 VAL A CG2 1 
ATOM   1950 N  N   . LEU A 1 217 ? -0.64800  5.45300   59.63200  1.000 9.55381  ? 220 LEU A N   1 
ATOM   1951 C  CA  . LEU A 1 217 ? -1.63500  5.25900   60.68400  1.000 8.47381  ? 220 LEU A CA  1 
ATOM   1952 C  C   . LEU A 1 217 ? -2.40000  6.55800   60.90500  1.000 9.73381  ? 220 LEU A C   1 
ATOM   1953 O  O   . LEU A 1 217 ? -1.79300  7.61200   61.11900  1.000 10.03381 ? 220 LEU A O   1 
ATOM   1954 C  CB  . LEU A 1 217 ? -0.93100  4.84000   61.98000  1.000 9.07381  ? 220 LEU A CB  1 
ATOM   1955 C  CG  . LEU A 1 217 ? -1.77200  4.86000   63.26000  1.000 10.21381 ? 220 LEU A CG  1 
ATOM   1956 C  CD1 . LEU A 1 217 ? -2.85500  3.77600   63.21100  1.000 10.07381 ? 220 LEU A CD1 1 
ATOM   1957 C  CD2 . LEU A 1 217 ? -0.87600  4.64800   64.46500  1.000 9.77381  ? 220 LEU A CD2 1 
ATOM   1958 N  N   . LEU A 1 218 ? -3.72800  6.48500   60.82600  1.000 9.50381  ? 221 LEU A N   1 
ATOM   1959 C  CA  . LEU A 1 218 ? -4.62600  7.55600   61.24200  1.000 9.00381  ? 221 LEU A CA  1 
ATOM   1960 C  C   . LEU A 1 218 ? -5.44100  7.02600   62.41000  1.000 8.61381  ? 221 LEU A C   1 
ATOM   1961 O  O   . LEU A 1 218 ? -6.05300  5.96100   62.30100  1.000 11.21381 ? 221 LEU A O   1 
ATOM   1962 C  CB  . LEU A 1 218 ? -5.55700  7.98200   60.10200  1.000 12.43381 ? 221 LEU A CB  1 
ATOM   1963 C  CG  . LEU A 1 218 ? -6.72100  8.92100   60.45900  1.000 15.96381 ? 221 LEU A CG  1 
ATOM   1964 C  CD1 . LEU A 1 218 ? -6.25100  10.28800  60.97000  1.000 15.45381 ? 221 LEU A CD1 1 
ATOM   1965 C  CD2 . LEU A 1 218 ? -7.65100  9.09600   59.26000  1.000 18.41381 ? 221 LEU A CD2 1 
ATOM   1966 N  N   . GLN A 1 219 ? -5.41300  7.73800   63.53500  1.000 8.87381  ? 222 GLN A N   1 
ATOM   1967 C  CA  . GLN A 1 219 ? -5.99000  7.22500   64.76800  1.000 8.30381  ? 222 GLN A CA  1 
ATOM   1968 C  C   . GLN A 1 219 ? -6.75200  8.33400   65.47900  1.000 11.32381 ? 222 GLN A C   1 
ATOM   1969 O  O   . GLN A 1 219 ? -6.31500  9.48700   65.49400  1.000 12.45381 ? 222 GLN A O   1 
ATOM   1970 C  CB  . GLN A 1 219 ? -4.86900  6.69500   65.66600  1.000 11.28381 ? 222 GLN A CB  1 
ATOM   1971 C  CG  . GLN A 1 219 ? -5.31900  5.91100   66.87200  1.000 14.91381 ? 222 GLN A CG  1 
ATOM   1972 C  CD  . GLN A 1 219 ? -4.14700  5.21000   67.53000  1.000 15.20381 ? 222 GLN A CD  1 
ATOM   1973 O  OE1 . GLN A 1 219 ? -3.44400  5.79900   68.35000  1.000 16.11381 ? 222 GLN A OE1 1 
ATOM   1974 N  NE2 . GLN A 1 219 ? -3.90700  3.96200   67.14000  1.000 10.83381 ? 222 GLN A NE2 1 
ATOM   1975 N  N   . PHE A 1 220 ? -7.89100  7.97900   66.06900  1.000 9.15381  ? 223 PHE A N   1 
ATOM   1976 C  CA  . PHE A 1 220 ? -8.65700  8.88400   66.91500  1.000 9.86381  ? 223 PHE A CA  1 
ATOM   1977 C  C   . PHE A 1 220 ? -8.84100  8.24000   68.27800  1.000 13.04381 ? 223 PHE A C   1 
ATOM   1978 O  O   . PHE A 1 220 ? -9.18000  7.06000   68.37200  1.000 12.41381 ? 223 PHE A O   1 
ATOM   1979 C  CB  . PHE A 1 220 ? -10.00800 9.22600   66.27900  1.000 10.11381 ? 223 PHE A CB  1 
ATOM   1980 C  CG  . PHE A 1 220 ? -9.86700  9.97300   64.99800  1.000 7.94381  ? 223 PHE A CG  1 
ATOM   1981 C  CD1 . PHE A 1 220 ? -9.72800  11.35600  64.99600  1.000 9.84381  ? 223 PHE A CD1 1 
ATOM   1982 C  CD2 . PHE A 1 220 ? -9.82500  9.29200   63.79300  1.000 9.52381  ? 223 PHE A CD2 1 
ATOM   1983 C  CE1 . PHE A 1 220 ? -9.56600  12.04200  63.80200  1.000 8.45381  ? 223 PHE A CE1 1 
ATOM   1984 C  CE2 . PHE A 1 220 ? -9.66100  9.96700   62.60800  1.000 11.20381 ? 223 PHE A CE2 1 
ATOM   1985 C  CZ  . PHE A 1 220 ? -9.53700  11.34200  62.60900  1.000 9.08381  ? 223 PHE A CZ  1 
ATOM   1986 N  N   . VAL A 1 221 ? -8.58300  9.00400   69.33200  1.000 11.18381 ? 224 VAL A N   1 
ATOM   1987 C  CA  . VAL A 1 221 ? -8.63100  8.49100   70.69700  1.000 12.45381 ? 224 VAL A CA  1 
ATOM   1988 C  C   . VAL A 1 221 ? -9.42200  9.46900   71.54400  1.000 13.59381 ? 224 VAL A C   1 
ATOM   1989 O  O   . VAL A 1 221 ? -9.07000  10.65100  71.61100  1.000 12.67381 ? 224 VAL A O   1 
ATOM   1990 C  CB  . VAL A 1 221 ? -7.21900  8.34300   71.28300  1.000 13.37381 ? 224 VAL A CB  1 
ATOM   1991 C  CG1 . VAL A 1 221 ? -7.29700  7.77400   72.68800  1.000 19.35381 ? 224 VAL A CG1 1 
ATOM   1992 C  CG2 . VAL A 1 221 ? -6.34200  7.47400   70.37500  1.000 14.82381 ? 224 VAL A CG2 1 
ATOM   1993 N  N   . THR A 1 222 ? -10.46000 8.97700   72.21900  1.000 14.47381 ? 225 THR A N   1 
ATOM   1994 C  CA  . THR A 1 222 ? -11.28900 9.81700   73.07400  1.000 12.13381 ? 225 THR A CA  1 
ATOM   1995 C  C   . THR A 1 222 ? -11.42100 9.17100   74.44100  1.000 10.66381 ? 225 THR A C   1 
ATOM   1996 O  O   . THR A 1 222 ? -11.72700 7.97900   74.53500  1.000 11.99381 ? 225 THR A O   1 
ATOM   1997 C  CB  . THR A 1 222 ? -12.68200 9.99800   72.47100  1.000 18.07381 ? 225 THR A CB  1 
ATOM   1998 O  OG1 . THR A 1 222 ? -12.56200 10.50500  71.13600  1.000 20.99381 ? 225 THR A OG1 1 
ATOM   1999 C  CG2 . THR A 1 222 ? -13.48000 10.97500  73.31200  1.000 17.17381 ? 225 THR A CG2 1 
ATOM   2000 N  N   . ALA A 1 223 ? -11.17100 9.94900   75.49500  1.000 9.37381  ? 226 ALA A N   1 
ATOM   2001 C  CA  . ALA A 1 223 ? -11.41800 9.46400   76.84600  1.000 10.34381 ? 226 ALA A CA  1 
ATOM   2002 C  C   . ALA A 1 223 ? -12.91300 9.46200   77.12500  1.000 11.06381 ? 226 ALA A C   1 
ATOM   2003 O  O   . ALA A 1 223 ? -13.64000 10.36500  76.70400  1.000 14.09381 ? 226 ALA A O   1 
ATOM   2004 C  CB  . ALA A 1 223 ? -10.68800 10.33100  77.87300  1.000 12.50381 ? 226 ALA A CB  1 
ATOM   2005 N  N   A ALA A 1 224 ? -13.36800 8.43600   77.83400  0.690 10.64381 ? 227 ALA A N   1 
ATOM   2006 N  N   B ALA A 1 224 ? -13.37700 8.42700   77.82300  0.310 10.88381 ? 227 ALA A N   1 
ATOM   2007 C  CA  A ALA A 1 224 ? -14.78300 8.28000   78.15300  0.690 19.29381 ? 227 ALA A CA  1 
ATOM   2008 C  CA  B ALA A 1 224 ? -14.80600 8.26200   78.05900  0.310 19.26381 ? 227 ALA A CA  1 
ATOM   2009 C  C   A ALA A 1 224 ? -14.90400 7.43000   79.41300  0.690 23.43381 ? 227 ALA A C   1 
ATOM   2010 C  C   B ALA A 1 224 ? -15.08100 7.78700   79.47900  0.310 25.89381 ? 227 ALA A C   1 
ATOM   2011 O  O   A ALA A 1 224 ? -13.90400 7.08800   80.05500  0.690 12.87381 ? 227 ALA A O   1 
ATOM   2012 O  O   B ALA A 1 224 ? -14.57400 8.36500   80.44600  0.310 24.48381 ? 227 ALA A O   1 
ATOM   2013 C  CB  A ALA A 1 224 ? -15.54200 7.66700   76.97300  0.690 24.26381 ? 227 ALA A CB  1 
ATOM   2014 C  CB  B ALA A 1 224 ? -15.39300 7.27300   77.05200  0.310 16.73381 ? 227 ALA A CB  1 
ATOM   2015 N  N   A GLY A 1 225 ? -16.13800 7.08000   79.76200  0.690 29.97381 ? 228 GLY A N   1 
ATOM   2016 N  N   B GLY A 1 225 ? -15.88800 6.73900   79.61300  0.310 32.00381 ? 228 GLY A N   1 
ATOM   2017 C  CA  A GLY A 1 225 ? -16.40600 6.26700   80.92800  0.690 35.54381 ? 228 GLY A CA  1 
ATOM   2018 C  CA  B GLY A 1 225 ? -16.17900 6.16900   80.91200  0.310 34.63381 ? 228 GLY A CA  1 
ATOM   2019 C  C   A GLY A 1 225 ? -16.73000 7.03900   82.18400  0.690 32.60381 ? 228 GLY A C   1 
ATOM   2020 C  C   B GLY A 1 225 ? -17.14800 6.98300   81.74500  0.310 31.72381 ? 228 GLY A C   1 
ATOM   2021 O  O   A GLY A 1 225 ? -16.98400 6.41400   83.22000  0.690 20.74381 ? 228 GLY A O   1 
ATOM   2022 O  O   B GLY A 1 225 ? -18.32000 6.61800   81.87500  0.310 39.74381 ? 228 GLY A O   1 
ATOM   2023 N  N   A ILE A 1 226 ? -16.71700 8.37000   82.12900  0.690 34.23381 ? 229 ILE A N   1 
ATOM   2024 N  N   B ILE A 1 226 ? -16.67400 8.09300   82.30700  0.310 34.35381 ? 229 ILE A N   1 
ATOM   2025 C  CA  A ILE A 1 226 ? -17.11100 9.21900   83.24800  0.690 30.78381 ? 229 ILE A CA  1 
ATOM   2026 C  CA  B ILE A 1 226 ? -17.44400 8.87300   83.27100  0.310 36.17381 ? 229 ILE A CA  1 
ATOM   2027 C  C   A ILE A 1 226 ? -18.08400 10.26800  82.72300  0.690 48.19381 ? 229 ILE A C   1 
ATOM   2028 C  C   B ILE A 1 226 ? -18.26100 9.93800   82.55100  0.310 46.51381 ? 229 ILE A C   1 
ATOM   2029 O  O   A ILE A 1 226 ? -17.72500 11.08100  81.86200  0.690 29.79381 ? 229 ILE A O   1 
ATOM   2030 O  O   B ILE A 1 226 ? -17.77400 10.60800  81.63200  0.310 35.28381 ? 229 ILE A O   1 
ATOM   2031 C  CB  A ILE A 1 226 ? -15.90100 9.88500   83.92700  0.690 45.18381 ? 229 ILE A CB  1 
ATOM   2032 C  CB  B ILE A 1 226 ? -16.52000 9.48100   84.34700  0.310 39.89381 ? 229 ILE A CB  1 
ATOM   2033 C  CG1 A ILE A 1 226 ? -14.94100 8.82300   84.47300  0.690 37.40381 ? 229 ILE A CG1 1 
ATOM   2034 C  CG1 B ILE A 1 226 ? -16.37200 8.52300   85.53100  0.310 31.98381 ? 229 ILE A CG1 1 
ATOM   2035 C  CG2 A ILE A 1 226 ? -16.36200 10.80700  85.04300  0.690 39.17381 ? 229 ILE A CG2 1 
ATOM   2036 C  CG2 B ILE A 1 226 ? -17.03800 10.82900  84.82700  0.310 39.20381 ? 229 ILE A CG2 1 
ATOM   2037 C  CD1 A ILE A 1 226 ? -13.72400 9.39300   85.16600  0.690 23.75381 ? 229 ILE A CD1 1 
ATOM   2038 C  CD1 B ILE A 1 226 ? -15.56100 7.28900   85.23400  0.310 22.61381 ? 229 ILE A CD1 1 
ATOM   2039 N  N   A THR A 1 227 ? -19.31100 10.24700  83.23500  0.690 57.50381 ? 230 THR A N   1 
ATOM   2040 N  N   B THR A 1 227 ? -19.51500 10.08900  82.97100  0.310 54.63381 ? 230 THR A N   1 
ATOM   2041 C  CA  A THR A 1 227 ? -20.33400 11.18300  82.79400  0.690 58.77381 ? 230 THR A CA  1 
ATOM   2042 C  CA  B THR A 1 227 ? -20.41100 11.10600  82.44500  0.310 56.93381 ? 230 THR A CA  1 
ATOM   2043 C  C   A THR A 1 227 ? -20.14100 12.54400  83.45300  0.690 60.22381 ? 230 THR A C   1 
ATOM   2044 C  C   B THR A 1 227 ? -20.21700 12.42400  83.18900  0.310 58.45381 ? 230 THR A C   1 
ATOM   2045 O  O   A THR A 1 227 ? -19.58500 12.65700  84.55000  0.690 52.33381 ? 230 THR A O   1 
ATOM   2046 O  O   B THR A 1 227 ? -19.73200 12.46400  84.32200  0.310 53.66381 ? 230 THR A O   1 
ATOM   2047 C  CB  A THR A 1 227 ? -21.72700 10.64500  83.12200  0.690 69.52381 ? 230 THR A CB  1 
ATOM   2048 C  CB  B THR A 1 227 ? -21.86600 10.65400  82.58700  0.310 65.48381 ? 230 THR A CB  1 
ATOM   2049 O  OG1 A THR A 1 227 ? -21.80800 10.33800  84.52100  0.690 65.33381 ? 230 THR A OG1 1 
ATOM   2050 O  OG1 B THR A 1 227 ? -22.16400 10.42600  83.97100  0.310 65.37381 ? 230 THR A OG1 1 
ATOM   2051 C  CG2 A THR A 1 227 ? -22.02000 9.39000   82.30900  0.690 69.59381 ? 230 THR A CG2 1 
ATOM   2052 C  CG2 B THR A 1 227 ? -22.10700 9.37300   81.80300  0.310 64.45381 ? 230 THR A CG2 1 
ATOM   2053 N  N   A HIS A 1 228 ? -20.61100 13.58300  82.76800  0.690 58.79381 ? 231 HIS A N   1 
ATOM   2054 N  N   B HIS A 1 228 ? -20.61300 13.51100  82.53400  0.310 57.34381 ? 231 HIS A N   1 
ATOM   2055 C  CA  A HIS A 1 228 ? -20.48400 14.95100  83.25900  0.690 53.19381 ? 231 HIS A CA  1 
ATOM   2056 C  CA  B HIS A 1 228 ? -20.49700 14.84200  83.12100  0.310 53.17381 ? 231 HIS A CA  1 
ATOM   2057 C  C   A HIS A 1 228 ? -21.55000 15.26300  84.30600  0.690 69.83381 ? 231 HIS A C   1 
ATOM   2058 C  C   B HIS A 1 228 ? -21.60700 15.09200  84.13800  0.310 67.37381 ? 231 HIS A C   1 
ATOM   2059 O  O   A HIS A 1 228 ? -21.29500 15.96700  85.28400  0.690 66.19381 ? 231 HIS A O   1 
ATOM   2060 O  O   B HIS A 1 228 ? -22.66300 14.46000  84.09400  0.310 65.38381 ? 231 HIS A O   1 
ATOM   2061 C  CB  A HIS A 1 228 ? -20.57400 15.94700  82.09900  0.690 41.65381 ? 231 HIS A CB  1 
ATOM   2062 C  CB  B HIS A 1 228 ? -20.52800 15.91500  82.03000  0.310 41.74381 ? 231 HIS A CB  1 
ATOM   2063 O  OXT A HIS A 1 228 ? -22.69300 14.81500  84.20000  0.690 69.17381 ? 231 HIS A OXT 1 
ATOM   2064 O  OXT B HIS A 1 228 ? -21.47500 15.93300  85.02900  0.310 65.75381 ? 231 HIS A OXT 1 
HETATM 2065 MG MG  . MG  B 2 .   ? -11.72500 -10.99700 59.56600  0.540 13.24381 2 301 MG  A MG  1 
HETATM 2066 MG MG  . MG  C 2 .   ? 16.18200  9.11100   60.86600  0.600 11.56381 2 302 MG  A MG  1 
HETATM 2067 O  O   A HOH D 3 .   ? -4.74700  4.70900   73.49800  0.740 13.58381 ? 401 HOH A O   1 
HETATM 2068 O  O   . HOH D 3 .   ? -3.54200  5.61200   71.03700  1.000 22.03381 ? 402 HOH A O   1 
HETATM 2069 O  O   . HOH D 3 .   ? -7.71300  1.09900   67.27900  1.000 10.76381 ? 403 HOH A O   1 
HETATM 2070 O  O   . HOH D 3 .   ? -4.00400  8.57400   72.15100  1.000 28.03381 ? 404 HOH A O   1 
HETATM 2071 O  O   . HOH D 3 .   ? -0.78700  -3.30300  68.03800  1.000 8.40381  ? 405 HOH A O   1 
HETATM 2072 O  O   . HOH D 3 .   ? -1.24200  7.02500   71.03200  1.000 11.38381 ? 406 HOH A O   1 
HETATM 2073 O  O   . HOH D 3 .   ? -6.55300  -4.71500  65.61500  1.000 16.43381 ? 407 HOH A O   1 
HETATM 2074 O  O   . HOH D 3 .   ? -0.30300  -5.74400  69.29200  1.000 8.72381  ? 408 HOH A O   1 
HETATM 2075 O  O   . HOH D 3 .   ? 2.39300   -2.92200  69.71600  1.000 8.20381  ? 409 HOH A O   1 
HETATM 2076 O  O   . HOH D 3 .   ? -12.12000 -3.31300  73.32000  1.000 17.37381 ? 410 HOH A O   1 
HETATM 2077 O  O   . HOH D 3 .   ? -10.33100 0.91700   64.04800  1.000 14.12381 ? 411 HOH A O   1 
HETATM 2078 O  O   . HOH D 3 .   ? 3.68900   -1.57300  73.82100  1.000 8.23381  ? 412 HOH A O   1 
HETATM 2079 O  O   A HOH D 3 .   ? 1.65200   6.79300   75.57900  0.780 10.33381 ? 413 HOH A O   1 
HETATM 2080 O  O   B HOH D 3 .   ? 0.93000   6.45400   76.07000  0.220 7.69381  ? 413 HOH A O   1 
HETATM 2081 O  O   A HOH D 3 .   ? -13.72300 1.66600   70.54500  0.500 19.32381 ? 414 HOH A O   1 
HETATM 2082 O  O   B HOH D 3 .   ? -14.09400 0.09600   70.49500  0.500 30.84381 ? 414 HOH A O   1 
HETATM 2083 O  O   . HOH D 3 .   ? -4.92500  10.50500  69.66900  1.000 22.49381 ? 415 HOH A O   1 
HETATM 2084 O  O   . HOH D 3 .   ? 4.66300   2.14400   74.01500  1.000 7.86381  ? 416 HOH A O   1 
HETATM 2085 O  O   . HOH D 3 .   ? -12.56800 -4.33600  70.37200  1.000 34.71381 ? 417 HOH A O   1 
HETATM 2086 O  O   A HOH D 3 .   ? -12.20400 6.81700   68.45400  0.350 11.17381 ? 418 HOH A O   1 
HETATM 2087 O  O   B HOH D 3 .   ? -11.98200 7.95400   69.42800  0.650 19.82381 ? 418 HOH A O   1 
HETATM 2088 O  O   A HOH D 3 .   ? -10.72200 -6.28500  72.56000  0.370 20.76381 ? 419 HOH A O   1 
HETATM 2089 O  O   B HOH D 3 .   ? -10.83100 -5.34600  73.60100  0.630 26.87381 ? 419 HOH A O   1 
HETATM 2090 O  O   A HOH D 3 .   ? -14.13100 3.55500   68.79900  0.710 33.70381 ? 420 HOH A O   1 
HETATM 2091 O  O   B HOH D 3 .   ? -14.68000 1.83400   69.09300  0.290 15.56381 ? 420 HOH A O   1 
HETATM 2092 O  O   B HOH D 3 .   ? -10.89700 -3.28600  77.09200  0.670 20.92381 ? 421 HOH A O   1 
HETATM 2093 O  O   . HOH D 3 .   ? -4.66600  -5.84300  63.43000  1.000 11.51381 ? 422 HOH A O   1 
HETATM 2094 O  O   B HOH D 3 .   ? -9.43200  -2.46500  79.19900  0.660 13.51381 ? 423 HOH A O   1 
HETATM 2095 O  O   . HOH D 3 .   ? 5.17600   4.72600   74.39100  1.000 8.69381  ? 424 HOH A O   1 
HETATM 2096 O  O   A HOH D 3 .   ? -10.21300 -5.67200  76.84800  0.660 14.82381 ? 425 HOH A O   1 
HETATM 2097 O  O   B HOH D 3 .   ? -9.78800  -3.96700  75.20100  0.340 11.62381 ? 425 HOH A O   1 
HETATM 2098 O  O   A HOH D 3 .   ? -15.50600 0.13500   70.83900  0.450 22.78381 ? 426 HOH A O   1 
HETATM 2099 O  O   B HOH D 3 .   ? -15.60400 -1.64400  70.80600  0.550 24.67381 ? 426 HOH A O   1 
HETATM 2100 O  O   A HOH D 3 .   ? -13.52100 -3.02600  65.82100  0.440 16.13381 ? 427 HOH A O   1 
HETATM 2101 O  O   B HOH D 3 .   ? -13.48600 -2.29700  64.64900  0.560 21.35381 ? 427 HOH A O   1 
HETATM 2102 O  O   . HOH D 3 .   ? -9.06800  6.13600   62.08500  1.000 22.05381 ? 428 HOH A O   1 
HETATM 2103 O  O   A HOH D 3 .   ? -12.23300 -6.61000  68.82100  0.400 24.45381 ? 429 HOH A O   1 
HETATM 2104 O  O   B HOH D 3 .   ? -10.70200 -6.15900  68.64200  0.600 20.94381 ? 429 HOH A O   1 
HETATM 2105 O  O   A HOH D 3 .   ? -11.18300 3.16800   62.09200  0.570 29.77381 ? 430 HOH A O   1 
HETATM 2106 O  O   B HOH D 3 .   ? -11.04700 4.81100   61.89000  0.430 22.06381 ? 430 HOH A O   1 
HETATM 2107 O  O   A HOH D 3 .   ? -14.84500 2.76600   66.67800  0.440 17.39381 ? 431 HOH A O   1 
HETATM 2108 O  O   B HOH D 3 .   ? -15.84400 4.09500   64.91500  0.560 22.51381 ? 431 HOH A O   1 
HETATM 2109 O  O   . HOH D 3 .   ? 5.86600   0.51000   75.89700  1.000 10.27381 ? 432 HOH A O   1 
HETATM 2110 O  O   . HOH D 3 .   ? -12.02200 -0.75100  62.21600  1.000 37.79381 ? 433 HOH A O   1 
HETATM 2111 O  O   . HOH D 3 .   ? -7.32900  -6.52300  62.76700  1.000 18.81381 ? 434 HOH A O   1 
HETATM 2112 O  O   . HOH D 3 .   ? -9.32100  0.33100   60.26200  1.000 20.11381 ? 435 HOH A O   1 
HETATM 2113 O  O   . HOH D 3 .   ? -14.23800 2.16000   63.52100  1.000 41.59381 ? 436 HOH A O   1 
HETATM 2114 O  O   B HOH D 3 .   ? -13.69300 -3.81600  76.96100  0.900 37.04381 ? 437 HOH A O   1 
HETATM 2115 O  O   . HOH D 3 .   ? -16.29400 -0.23600  67.64700  1.000 43.08381 ? 438 HOH A O   1 
HETATM 2116 O  O   A HOH D 3 .   ? -12.19900 -7.43900  74.70400  0.570 21.63381 ? 439 HOH A O   1 
HETATM 2117 O  O   B HOH D 3 .   ? -12.10600 -7.35700  76.68800  0.430 22.97381 ? 439 HOH A O   1 
HETATM 2118 O  O   . HOH D 3 .   ? -7.09600  -0.37400  58.88400  1.000 14.56381 ? 440 HOH A O   1 
HETATM 2119 O  O   . HOH D 3 .   ? -15.38500 -0.77700  64.92800  1.000 44.42381 ? 441 HOH A O   1 
HETATM 2120 O  O   . HOH D 3 .   ? -17.17600 2.32400   70.73400  1.000 46.11381 ? 442 HOH A O   1 
HETATM 2121 O  O   . HOH D 3 .   ? -3.92900  12.48900  77.11300  1.000 9.27381  ? 443 HOH A O   1 
HETATM 2122 O  O   . HOH D 3 .   ? -9.95200  -2.32800  59.83800  1.000 29.46381 ? 444 HOH A O   1 
HETATM 2123 O  O   . HOH D 3 .   ? -10.20700 -4.75500  60.84500  1.000 29.12381 ? 445 HOH A O   1 
HETATM 2124 O  O   . HOH D 3 .   ? -7.34000  -1.86700  83.07600  1.000 23.52381 ? 446 HOH A O   1 
HETATM 2125 O  O   A HOH D 3 .   ? -4.15700  -8.08000  61.72200  0.740 8.21381  ? 447 HOH A O   1 
HETATM 2126 O  O   B HOH D 3 .   ? -5.04600  -7.19100  61.39100  0.260 8.56381  ? 447 HOH A O   1 
HETATM 2127 O  O   . HOH D 3 .   ? -13.53900 10.40300  66.98200  1.000 28.69381 ? 448 HOH A O   1 
HETATM 2128 O  O   . HOH D 3 .   ? -9.98900  6.82600   59.81800  1.000 40.68381 ? 449 HOH A O   1 
HETATM 2129 O  O   . HOH D 3 .   ? -9.34200  -3.99700  82.54600  1.000 36.80381 ? 450 HOH A O   1 
HETATM 2130 O  O   . HOH D 3 .   ? -5.00300  9.14200   82.36000  1.000 11.60381 ? 451 HOH A O   1 
HETATM 2131 O  O   . HOH D 3 .   ? -10.82700 1.76400   58.46100  1.000 38.98381 ? 452 HOH A O   1 
HETATM 2132 O  O   . HOH D 3 .   ? 0.26500   -9.28800  78.57200  1.000 15.45381 ? 453 HOH A O   1 
HETATM 2133 O  O   A HOH D 3 .   ? -12.26600 12.91500  70.05400  0.710 16.91381 ? 454 HOH A O   1 
HETATM 2134 O  O   B HOH D 3 .   ? -13.34500 12.47900  70.12300  0.290 16.12381 ? 454 HOH A O   1 
HETATM 2135 O  O   . HOH D 3 .   ? -4.24400  5.33100   57.35100  1.000 15.24381 ? 455 HOH A O   1 
HETATM 2136 O  O   A HOH D 3 .   ? -17.20800 0.49200   77.25500  0.630 29.05381 ? 456 HOH A O   1 
HETATM 2137 O  O   B HOH D 3 .   ? -17.62800 -0.43900  78.58300  0.370 24.94381 ? 456 HOH A O   1 
HETATM 2138 O  O   . HOH D 3 .   ? -12.23900 12.92500  67.23600  1.000 21.09381 ? 457 HOH A O   1 
HETATM 2139 O  O   . HOH D 3 .   ? -6.18700  -1.49800  85.01800  1.000 31.03381 ? 458 HOH A O   1 
HETATM 2140 O  O   . HOH D 3 .   ? 4.10300   -3.67700  81.92400  1.000 26.47381 ? 459 HOH A O   1 
HETATM 2141 O  O   . HOH D 3 .   ? -13.01600 -7.07900  62.00000  1.000 43.03381 ? 460 HOH A O   1 
HETATM 2142 O  O   A HOH D 3 .   ? -10.89600 1.49400   84.23000  0.430 18.53381 ? 461 HOH A O   1 
HETATM 2143 O  O   . HOH D 3 .   ? -6.25600  -1.30000  56.18500  1.000 19.90381 ? 462 HOH A O   1 
HETATM 2144 O  O   . HOH D 3 .   ? -11.07300 -2.19600  57.56300  1.000 45.28381 ? 463 HOH A O   1 
HETATM 2145 O  O   . HOH D 3 .   ? -10.59300 -12.42500 73.13200  1.000 26.56381 ? 464 HOH A O   1 
HETATM 2146 O  O   . HOH D 3 .   ? -2.96100  14.37300  63.14700  1.000 13.23381 ? 465 HOH A O   1 
HETATM 2147 O  O   . HOH D 3 .   ? -9.48800  1.44900   56.37600  1.000 45.63381 ? 466 HOH A O   1 
HETATM 2148 O  O   . HOH D 3 .   ? -15.46000 11.96200  70.64700  1.000 23.63381 ? 467 HOH A O   1 
HETATM 2149 O  O   . HOH D 3 .   ? -9.15100  6.24600   57.11300  1.000 31.24381 ? 468 HOH A O   1 
HETATM 2150 O  O   . HOH D 3 .   ? -9.75600  -13.21800 70.69200  1.000 19.95381 ? 469 HOH A O   1 
HETATM 2151 O  O   . HOH D 3 .   ? -6.76300  5.28700   56.12300  1.000 24.35381 ? 470 HOH A O   1 
HETATM 2152 O  O   A HOH D 3 .   ? -12.00800 -6.82700  59.86500  0.570 17.64381 ? 471 HOH A O   1 
HETATM 2153 O  O   B HOH D 3 .   ? -11.38600 -6.00500  59.12900  0.430 22.96381 ? 471 HOH A O   1 
HETATM 2154 O  O   . HOH D 3 .   ? -7.19200  2.57900   55.63100  1.000 27.10381 ? 472 HOH A O   1 
HETATM 2155 O  O   . HOH D 3 .   ? -17.28000 9.25400   74.75700  1.000 33.44381 ? 473 HOH A O   1 
HETATM 2156 O  O   . HOH D 3 .   ? -17.43500 10.31300  72.29800  1.000 33.81381 ? 474 HOH A O   1 
HETATM 2157 O  O   . HOH D 3 .   ? 1.02300   -9.53200  81.20300  1.000 16.26381 ? 475 HOH A O   1 
HETATM 2158 O  O   A HOH D 3 .   ? -7.20400  16.45400  75.41000  0.640 10.22381 ? 476 HOH A O   1 
HETATM 2159 O  O   B HOH D 3 .   ? -7.29300  16.25600  76.42500  0.360 9.73381  ? 476 HOH A O   1 
HETATM 2160 O  O   A HOH D 3 .   ? 4.72500   -5.76400  82.00900  0.500 26.20381 ? 477 HOH A O   1 
HETATM 2161 O  O   B HOH D 3 .   ? 6.43400   -5.06200  81.02000  0.500 21.51381 ? 477 HOH A O   1 
HETATM 2162 O  O   . HOH D 3 .   ? -0.39500  -6.95700  57.75600  1.000 19.21381 ? 478 HOH A O   1 
HETATM 2163 O  O   . HOH D 3 .   ? -2.64600  -14.04300 75.17300  1.000 19.35381 ? 479 HOH A O   1 
HETATM 2164 O  O   . HOH D 3 .   ? -4.20800  8.70000   56.50700  1.000 46.36381 ? 480 HOH A O   1 
HETATM 2165 O  O   . HOH D 3 .   ? -16.26300 11.11600  76.29600  1.000 20.14381 ? 481 HOH A O   1 
HETATM 2166 O  O   A HOH D 3 .   ? 2.23500   -6.05900  58.01900  0.680 8.24381  ? 482 HOH A O   1 
HETATM 2167 O  O   B HOH D 3 .   ? 1.39200   -5.57600  57.79500  0.320 10.92381 ? 482 HOH A O   1 
HETATM 2168 O  O   . HOH D 3 .   ? 8.40900   -4.01500  79.67400  1.000 22.98381 ? 483 HOH A O   1 
HETATM 2169 O  O   . HOH D 3 .   ? -9.78900  -13.51300 75.54600  1.000 20.98381 ? 484 HOH A O   1 
HETATM 2170 O  O   . HOH D 3 .   ? 6.35200   2.52100   83.58000  1.000 16.81381 ? 485 HOH A O   1 
HETATM 2171 O  O   . HOH D 3 .   ? -0.86800  -9.44200  83.04800  1.000 25.33381 ? 486 HOH A O   1 
HETATM 2172 O  O   A HOH D 3 .   ? -12.10600 -10.88800 61.84400  0.590 28.67381 ? 487 HOH A O   1 
HETATM 2173 O  O   B HOH D 3 .   ? -13.80000 -10.79700 61.06400  0.410 23.35381 ? 487 HOH A O   1 
HETATM 2174 O  O   . HOH D 3 .   ? -10.85500 -9.04300  59.01200  1.000 27.71381 ? 488 HOH A O   1 
HETATM 2175 O  O   . HOH D 3 .   ? -2.03800  18.24400  70.55400  1.000 10.86381 ? 489 HOH A O   1 
HETATM 2176 O  O   A HOH D 3 .   ? -4.51200  13.36400  58.88000  0.550 22.20381 ? 490 HOH A O   1 
HETATM 2177 O  O   A HOH D 3 .   ? -3.75900  -4.38100  86.99600  0.620 26.99381 ? 491 HOH A O   1 
HETATM 2178 O  O   B HOH D 3 .   ? -3.81600  -3.11700  84.97000  0.380 22.41381 ? 491 HOH A O   1 
HETATM 2179 O  O   . HOH D 3 .   ? -5.98100  -15.70900 69.19600  1.000 12.67381 ? 492 HOH A O   1 
HETATM 2180 O  O   . HOH D 3 .   ? -7.43400  -2.77000  87.33900  1.000 38.93381 ? 493 HOH A O   1 
HETATM 2181 O  O   . HOH D 3 .   ? -10.83700 8.75000   56.65400  1.000 44.38381 ? 494 HOH A O   1 
HETATM 2182 O  O   . HOH D 3 .   ? 3.85200   -8.54800  82.46400  1.000 47.41381 ? 495 HOH A O   1 
HETATM 2183 O  O   . HOH D 3 .   ? -7.85200  18.04800  74.06600  1.000 27.31381 ? 496 HOH A O   1 
HETATM 2184 O  O   . HOH D 3 .   ? -15.77900 3.82300   83.84300  1.000 42.10381 ? 497 HOH A O   1 
HETATM 2185 O  O   . HOH D 3 .   ? 3.16800   2.30500   86.78900  1.000 24.90381 ? 498 HOH A O   1 
HETATM 2186 O  O   . HOH D 3 .   ? 2.83900   11.53700  58.56800  1.000 30.98381 ? 499 HOH A O   1 
HETATM 2187 O  O   . HOH D 3 .   ? -18.70800 8.16700   78.62100  1.000 36.49381 ? 500 HOH A O   1 
HETATM 2188 O  O   A HOH D 3 .   ? 5.04300   -6.42600  58.26900  0.600 18.98381 ? 501 HOH A O   1 
HETATM 2189 O  O   B HOH D 3 .   ? 3.87700   -6.33900  57.83800  0.400 18.32381 ? 501 HOH A O   1 
HETATM 2190 O  O   . HOH D 3 .   ? -5.96700  -4.87200  87.44100  1.000 48.09381 ? 502 HOH A O   1 
HETATM 2191 O  O   . HOH D 3 .   ? 1.26800   13.68200  59.49100  1.000 28.18381 ? 503 HOH A O   1 
HETATM 2192 O  O   . HOH D 3 .   ? -3.19200  16.84200  62.27200  1.000 21.94381 ? 504 HOH A O   1 
HETATM 2193 O  O   . HOH D 3 .   ? -9.91300  -12.01400 60.17100  1.000 19.88381 ? 505 HOH A O   1 
HETATM 2194 O  O   . HOH D 3 .   ? -17.35800 10.52700  79.15900  1.000 40.66381 ? 506 HOH A O   1 
HETATM 2195 O  O   . HOH D 3 .   ? -6.47600  16.99000  79.53400  1.000 13.09381 ? 507 HOH A O   1 
HETATM 2196 O  O   . HOH D 3 .   ? -5.81200  -4.42500  53.92000  1.000 35.30381 ? 508 HOH A O   1 
HETATM 2197 O  O   . HOH D 3 .   ? 0.99900   -10.28800 58.38200  1.000 13.25381 ? 509 HOH A O   1 
HETATM 2198 O  O   . HOH D 3 .   ? 1.90400   -15.06900 74.83800  1.000 18.77381 ? 510 HOH A O   1 
HETATM 2199 O  O   . HOH D 3 .   ? 2.43000   -4.67300  55.33200  1.000 15.19381 ? 511 HOH A O   1 
HETATM 2200 O  O   . HOH D 3 .   ? -5.49200  7.68900   54.00900  1.000 48.28381 ? 512 HOH A O   1 
HETATM 2201 O  O   . HOH D 3 .   ? -0.50600  -15.69500 75.91100  1.000 30.25381 ? 513 HOH A O   1 
HETATM 2202 O  O   A HOH D 3 .   ? -8.21200  -15.88400 75.72200  0.770 16.28381 ? 514 HOH A O   1 
HETATM 2203 O  O   B HOH D 3 .   ? -6.91100  -16.57100 76.23100  0.230 15.65381 ? 514 HOH A O   1 
HETATM 2204 O  O   . HOH D 3 .   ? 12.27300  -3.98700  76.30900  1.000 24.34381 ? 515 HOH A O   1 
HETATM 2205 O  O   A HOH D 3 .   ? -3.63800  -0.40300  52.68600  0.760 27.88381 ? 516 HOH A O   1 
HETATM 2206 O  O   B HOH D 3 .   ? -5.64000  -0.84800  53.04500  0.240 15.81381 ? 516 HOH A O   1 
HETATM 2207 O  O   . HOH D 3 .   ? 3.15600   -8.70800  57.53900  1.000 14.83381 ? 517 HOH A O   1 
HETATM 2208 O  O   . HOH D 3 .   ? -6.97800  18.46100  77.32600  1.000 22.21381 ? 518 HOH A O   1 
HETATM 2209 O  O   A HOH D 3 .   ? 4.35600   -12.99700 78.44000  0.420 17.29381 ? 519 HOH A O   1 
HETATM 2210 O  O   B HOH D 3 .   ? 2.23900   -13.48900 79.11900  0.580 21.67381 ? 519 HOH A O   1 
HETATM 2211 O  O   . HOH D 3 .   ? 11.19300  -4.56800  79.10300  1.000 37.17381 ? 520 HOH A O   1 
HETATM 2212 O  O   A HOH D 3 .   ? -4.48200  -7.32400  54.39100  0.570 14.61381 ? 521 HOH A O   1 
HETATM 2213 O  O   B HOH D 3 .   ? -3.33900  -7.86600  54.63300  0.430 15.25381 ? 521 HOH A O   1 
HETATM 2214 O  O   A HOH D 3 .   ? -13.39700 -10.09200 59.01900  0.870 20.79381 ? 522 HOH A O   1 
HETATM 2215 O  O   A HOH D 3 .   ? -6.81900  14.44000  57.88700  0.610 30.38381 ? 523 HOH A O   1 
HETATM 2216 O  O   B HOH D 3 .   ? -7.23400  12.99100  58.27200  0.390 18.26381 ? 523 HOH A O   1 
HETATM 2217 O  O   . HOH D 3 .   ? 10.69700  -2.55100  81.28700  1.000 36.91381 ? 524 HOH A O   1 
HETATM 2218 O  O   . HOH D 3 .   ? -5.97400  19.74600  73.77800  1.000 23.09381 ? 525 HOH A O   1 
HETATM 2219 O  O   . HOH D 3 .   ? -0.19300  -7.84100  55.19500  1.000 24.83381 ? 526 HOH A O   1 
HETATM 2220 O  O   . HOH D 3 .   ? -4.52300  16.09100  59.46700  1.000 32.46381 ? 527 HOH A O   1 
HETATM 2221 O  O   . HOH D 3 .   ? -6.29500  5.96500   52.87700  1.000 41.09381 ? 528 HOH A O   1 
HETATM 2222 O  O   . HOH D 3 .   ? 13.62400  4.35100   75.43700  1.000 35.57381 ? 529 HOH A O   1 
HETATM 2223 O  O   . HOH D 3 .   ? -4.78200  20.03200  69.67900  1.000 14.82381 ? 530 HOH A O   1 
HETATM 2224 O  O   . HOH D 3 .   ? -1.71900  -4.42900  88.52100  1.000 24.32381 ? 531 HOH A O   1 
HETATM 2225 O  O   . HOH D 3 .   ? 11.97900  9.93000   74.65900  1.000 18.32381 ? 532 HOH A O   1 
HETATM 2226 O  O   A HOH D 3 .   ? -2.03200  6.52800   53.08100  0.560 19.10381 ? 533 HOH A O   1 
HETATM 2227 O  O   B HOH D 3 .   ? -3.33500  7.06600   53.51800  0.440 20.92381 ? 533 HOH A O   1 
HETATM 2228 O  O   A HOH D 3 .   ? 13.48500  2.31200   77.11300  0.650 15.47381 ? 534 HOH A O   1 
HETATM 2229 O  O   B HOH D 3 .   ? 15.02100  0.56900   77.25500  0.350 18.57381 ? 534 HOH A O   1 
HETATM 2230 O  O   A HOH D 3 .   ? -1.75700  18.54500  83.32500  0.310 11.17381 ? 535 HOH A O   1 
HETATM 2231 O  O   B HOH D 3 .   ? -3.23300  16.71700  82.09200  0.690 9.93381  ? 535 HOH A O   1 
HETATM 2232 O  O   . HOH D 3 .   ? -12.63000 -14.33500 63.71000  1.000 12.20381 ? 536 HOH A O   1 
HETATM 2233 O  O   . HOH D 3 .   ? -8.08100  4.66800   89.26400  1.000 14.11381 ? 537 HOH A O   1 
HETATM 2234 O  O   . HOH D 3 .   ? -17.67300 13.59400  77.03800  1.000 27.20381 ? 538 HOH A O   1 
HETATM 2235 O  O   . HOH D 3 .   ? -5.14700  18.52700  62.68200  1.000 24.10381 ? 539 HOH A O   1 
HETATM 2236 O  O   . HOH D 3 .   ? 9.76900   -10.56200 75.49200  1.000 10.13381 ? 540 HOH A O   1 
HETATM 2237 O  O   . HOH D 3 .   ? -4.13700  -17.61700 68.54100  1.000 18.16381 ? 541 HOH A O   1 
HETATM 2238 O  O   A HOH D 3 .   ? 1.69100   -1.48900  90.71600  0.450 27.21381 ? 542 HOH A O   1 
HETATM 2239 O  O   B HOH D 3 .   ? 2.25600   -1.59300  88.64300  0.550 28.61381 ? 542 HOH A O   1 
HETATM 2240 O  O   . HOH D 3 .   ? -15.72300 3.26400   86.26100  1.000 46.81381 ? 543 HOH A O   1 
HETATM 2241 O  O   . HOH D 3 .   ? 8.07200   8.77600   58.30800  1.000 18.74381 ? 544 HOH A O   1 
HETATM 2242 O  O   . HOH D 3 .   ? 0.51900   -5.60400  53.59000  1.000 29.20381 ? 545 HOH A O   1 
HETATM 2243 O  O   . HOH D 3 .   ? -4.57600  20.07200  75.80200  1.000 23.69381 ? 546 HOH A O   1 
HETATM 2244 O  O   . HOH D 3 .   ? 4.40200   -11.06000 82.77500  1.000 38.03381 ? 547 HOH A O   1 
HETATM 2245 O  O   . HOH D 3 .   ? -7.15700  18.05900  61.61200  1.000 26.25381 ? 548 HOH A O   1 
HETATM 2246 O  O   A HOH D 3 .   ? -2.95600  -2.38500  51.92300  0.610 33.07381 ? 549 HOH A O   1 
HETATM 2247 O  O   B HOH D 3 .   ? -3.69000  -3.75300  52.29100  0.390 24.88381 ? 549 HOH A O   1 
HETATM 2248 O  O   . HOH D 3 .   ? -11.08200 -11.38900 57.69700  1.000 18.45381 ? 550 HOH A O   1 
HETATM 2249 O  O   . HOH D 3 .   ? -3.55900  1.93500   51.49600  1.000 19.71381 ? 551 HOH A O   1 
HETATM 2250 O  O   . HOH D 3 .   ? 11.55400  9.88100   63.57300  1.000 16.25381 ? 552 HOH A O   1 
HETATM 2251 O  O   . HOH D 3 .   ? -11.57200 19.42100  72.44000  1.000 20.34381 ? 553 HOH A O   1 
HETATM 2252 O  O   . HOH D 3 .   ? -5.78100  3.63300   51.50800  1.000 38.41381 ? 554 HOH A O   1 
HETATM 2253 O  O   . HOH D 3 .   ? 4.71000   12.39200  57.57500  1.000 45.92381 ? 555 HOH A O   1 
HETATM 2254 O  O   . HOH D 3 .   ? 3.11700   15.85500  60.11000  1.000 36.86381 ? 556 HOH A O   1 
HETATM 2255 O  O   A HOH D 3 .   ? 6.91200   15.13700  62.85900  0.500 18.02326 ? 557 HOH A O   1 
HETATM 2256 O  O   B HOH D 3 .   ? 5.71700   15.82600  61.45500  0.500 18.05731 ? 557 HOH A O   1 
HETATM 2257 O  O   . HOH D 3 .   ? 8.57700   -7.89200  82.36700  1.000 37.77381 ? 558 HOH A O   1 
HETATM 2258 O  O   A HOH D 3 .   ? 3.31300   -15.45500 77.68800  0.540 19.62381 ? 559 HOH A O   1 
HETATM 2259 O  O   B HOH D 3 .   ? 4.55100   -14.82000 78.34900  0.460 17.36381 ? 559 HOH A O   1 
HETATM 2260 O  O   . HOH D 3 .   ? -5.69800  17.69600  82.03200  1.000 15.99381 ? 560 HOH A O   1 
HETATM 2261 O  O   . HOH D 3 .   ? 4.94300   -5.36200  54.89000  1.000 24.37381 ? 561 HOH A O   1 
HETATM 2262 O  O   . HOH D 3 .   ? -12.92600 -12.71700 59.66200  1.000 20.54381 ? 562 HOH A O   1 
HETATM 2263 O  O   A HOH D 3 .   ? -9.78200  19.18100  77.77400  0.720 24.63381 ? 563 HOH A O   1 
HETATM 2264 O  O   B HOH D 3 .   ? -9.83500  17.99000  75.76400  0.280 13.27381 ? 563 HOH A O   1 
HETATM 2265 O  O   . HOH D 3 .   ? -20.84800 11.31100  75.88700  1.000 40.42381 ? 564 HOH A O   1 
HETATM 2266 O  O   . HOH D 3 .   ? -1.36000  -5.20100  52.40200  1.000 49.05381 ? 565 HOH A O   1 
HETATM 2267 O  O   . HOH D 3 .   ? -1.27300  -18.08100 68.06500  1.000 31.15381 ? 566 HOH A O   1 
HETATM 2268 O  O   . HOH D 3 .   ? -5.92000  1.53100   90.76200  1.000 32.61381 ? 567 HOH A O   1 
HETATM 2269 O  O   . HOH D 3 .   ? 4.62300   -15.90200 75.29700  1.000 18.34381 ? 568 HOH A O   1 
HETATM 2270 O  O   . HOH D 3 .   ? 0.43600   -17.45800 66.15600  1.000 19.08381 ? 569 HOH A O   1 
HETATM 2271 O  O   . HOH D 3 .   ? -9.75800  -0.59700  90.10400  1.000 45.38381 ? 570 HOH A O   1 
HETATM 2272 O  O   A HOH D 3 .   ? 10.66200  -6.76100  81.37100  0.470 26.09381 ? 571 HOH A O   1 
HETATM 2273 O  O   B HOH D 3 .   ? 12.49500  -8.63600  81.14300  0.530 34.76381 ? 571 HOH A O   1 
HETATM 2274 O  O   A HOH D 3 .   ? -14.93800 6.00800   87.29700  0.820 26.47381 ? 572 HOH A O   1 
HETATM 2275 O  O   . HOH D 3 .   ? 8.94000   1.77200   86.00400  1.000 29.12381 ? 573 HOH A O   1 
HETATM 2276 O  O   . HOH D 3 .   ? 10.49000  7.93200   59.19800  1.000 20.42381 ? 574 HOH A O   1 
HETATM 2277 O  O   . HOH D 3 .   ? 0.15600   8.27400   52.66000  1.000 33.88381 ? 575 HOH A O   1 
HETATM 2278 O  O   . HOH D 3 .   ? 7.30200   -6.73100  56.55300  1.000 22.31381 ? 577 HOH A O   1 
HETATM 2279 O  O   . HOH D 3 .   ? 5.16100   -1.80600  53.36800  1.000 12.43381 ? 578 HOH A O   1 
HETATM 2280 O  O   . HOH D 3 .   ? 15.01800  3.81700   65.45400  1.000 22.90381 ? 579 HOH A O   1 
HETATM 2281 O  O   A HOH D 3 .   ? -3.86900  -10.40100 54.28900  0.570 33.60381 ? 580 HOH A O   1 
HETATM 2282 O  O   B HOH D 3 .   ? -6.80700  -8.91500  54.13300  0.430 21.93381 ? 580 HOH A O   1 
HETATM 2283 O  O   . HOH D 3 .   ? 6.43400   -13.41900 79.73200  1.000 24.55381 ? 581 HOH A O   1 
HETATM 2284 O  O   . HOH D 3 .   ? -0.41600  -2.39200  90.56500  1.000 49.85381 ? 582 HOH A O   1 
HETATM 2285 O  O   A HOH D 3 .   ? 14.60900  -4.64500  75.28100  0.580 20.60381 ? 583 HOH A O   1 
HETATM 2286 O  O   B HOH D 3 .   ? 15.91000  -5.61500  74.67900  0.420 18.40381 ? 583 HOH A O   1 
HETATM 2287 O  O   A HOH D 3 .   ? -0.49300  -18.36200 75.04800  0.710 17.78381 ? 584 HOH A O   1 
HETATM 2288 O  O   B HOH D 3 .   ? -1.77400  -17.89300 75.34000  0.290 13.99381 ? 584 HOH A O   1 
HETATM 2289 O  O   . HOH D 3 .   ? 5.18700   14.63500  58.51400  1.000 38.16381 ? 585 HOH A O   1 
HETATM 2290 O  O   . HOH D 3 .   ? 0.26400   -11.13700 55.17400  1.000 38.74381 ? 586 HOH A O   1 
HETATM 2291 O  O   . HOH D 3 .   ? -8.92100  1.73500   91.05400  1.000 45.41381 ? 587 HOH A O   1 
HETATM 2292 O  O   . HOH D 3 .   ? 13.90400  9.34300   76.71300  1.000 25.96381 ? 588 HOH A O   1 
HETATM 2293 O  O   . HOH D 3 .   ? 4.75100   -16.23000 65.13500  1.000 10.57381 ? 589 HOH A O   1 
HETATM 2294 O  O   . HOH D 3 .   ? 12.68100  -7.95800  78.01300  1.000 18.86381 ? 590 HOH A O   1 
HETATM 2295 O  O   . HOH D 3 .   ? 6.60500   -12.13500 82.08900  1.000 26.25381 ? 591 HOH A O   1 
HETATM 2296 O  O   . HOH D 3 .   ? -8.18800  -17.89000 77.59800  1.000 36.62381 ? 592 HOH A O   1 
HETATM 2297 O  O   A HOH D 3 .   ? -4.20900  -18.67600 65.50400  0.740 13.91381 ? 593 HOH A O   1 
HETATM 2298 O  O   B HOH D 3 .   ? -4.85400  -17.95600 66.05800  0.260 14.09381 ? 593 HOH A O   1 
HETATM 2299 O  O   . HOH D 3 .   ? 15.15400  6.36700   76.07600  1.000 42.82381 ? 594 HOH A O   1 
HETATM 2300 O  O   . HOH D 3 .   ? 15.47700  -4.86600  72.09700  1.000 27.12381 ? 595 HOH A O   1 
HETATM 2301 O  O   . HOH D 3 .   ? 7.11000   10.95000  56.43200  1.000 17.39381 ? 596 HOH A O   1 
HETATM 2302 O  O   . HOH D 3 .   ? 8.68800   -13.04200 78.55600  1.000 16.44381 ? 597 HOH A O   1 
HETATM 2303 O  O   . HOH D 3 .   ? -11.97000 4.99200   90.11900  1.000 25.18381 ? 598 HOH A O   1 
HETATM 2304 O  O   . HOH D 3 .   ? 10.28900  4.10400   85.79800  1.000 26.96381 ? 599 HOH A O   1 
HETATM 2305 O  O   . HOH D 3 .   ? 3.38900   19.11900  62.80400  1.000 20.02381 ? 600 HOH A O   1 
HETATM 2306 O  O   . HOH D 3 .   ? 11.85900  -10.39000 77.20800  1.000 12.81381 ? 601 HOH A O   1 
HETATM 2307 O  O   . HOH D 3 .   ? -6.31500  -11.21700 53.77800  1.000 36.01381 ? 602 HOH A O   1 
HETATM 2308 O  O   . HOH D 3 .   ? -4.83000  -19.90600 69.56600  1.000 18.39381 ? 603 HOH A O   1 
HETATM 2309 O  O   . HOH D 3 .   ? 12.08800  9.75700   60.35200  1.000 14.65381 ? 604 HOH A O   1 
HETATM 2310 O  O   . HOH D 3 .   ? 15.14300  3.62700   62.59500  1.000 18.88381 ? 605 HOH A O   1 
HETATM 2311 O  O   . HOH D 3 .   ? 3.94100   10.62400  53.56900  1.000 47.57381 ? 606 HOH A O   1 
HETATM 2312 O  O   . HOH D 3 .   ? 6.94300   13.63200  84.50500  1.000 16.25381 ? 607 HOH A O   1 
HETATM 2313 O  O   . HOH D 3 .   ? 10.03100  6.91900   86.01900  1.000 20.54381 ? 608 HOH A O   1 
HETATM 2314 O  O   . HOH D 3 .   ? -5.63700  18.95500  58.64500  1.000 45.99381 ? 609 HOH A O   1 
HETATM 2315 O  O   . HOH D 3 .   ? -5.74500  22.60100  67.63900  1.000 23.26381 ? 610 HOH A O   1 
HETATM 2316 O  O   . HOH D 3 .   ? -11.08500 -17.91700 78.04500  1.000 30.85381 ? 611 HOH A O   1 
HETATM 2317 O  O   . HOH D 3 .   ? 2.34500   -18.94000 74.29400  1.000 21.07381 ? 612 HOH A O   1 
HETATM 2318 O  O   . HOH D 3 .   ? -15.18300 3.74500   89.59000  1.000 43.65381 ? 613 HOH A O   1 
HETATM 2319 O  O   . HOH D 3 .   ? 0.18600   22.64400  71.28000  1.000 14.79381 ? 614 HOH A O   1 
HETATM 2320 O  O   . HOH D 3 .   ? -8.70100  11.75700  89.55600  1.000 32.66381 ? 615 HOH A O   1 
HETATM 2321 O  O   . HOH D 3 .   ? 8.48100   15.49400  60.53100  1.000 14.96381 ? 616 HOH A O   1 
HETATM 2322 O  O   A HOH D 3 .   ? -6.95800  21.77200  63.85200  0.570 26.92381 ? 617 HOH A O   1 
HETATM 2323 O  O   B HOH D 3 .   ? -5.53100  22.51300  64.51800  0.430 27.76381 ? 617 HOH A O   1 
HETATM 2324 O  O   A HOH D 3 .   ? -2.85500  -19.93800 75.34500  0.500 27.47381 ? 618 HOH A O   1 
HETATM 2325 O  O   B HOH D 3 .   ? -4.70600  -19.19600 75.39700  0.500 26.61381 ? 618 HOH A O   1 
HETATM 2326 O  O   . HOH D 3 .   ? 5.55700   18.48700  61.71900  1.000 29.02381 ? 619 HOH A O   1 
HETATM 2327 O  O   . HOH D 3 .   ? -14.93200 9.81400   88.16500  1.000 32.33381 ? 620 HOH A O   1 
HETATM 2328 O  O   . HOH D 3 .   ? -3.07500  2.63600   92.81100  1.000 33.17381 ? 621 HOH A O   1 
HETATM 2329 O  O   . HOH D 3 .   ? 8.59000   -11.20300 83.42700  1.000 34.49381 ? 622 HOH A O   1 
HETATM 2330 O  O   . HOH D 3 .   ? -3.29700  -2.68500  49.28200  1.000 57.40381 ? 623 HOH A O   1 
HETATM 2331 O  O   . HOH D 3 .   ? -1.73600  20.39800  60.21100  1.000 35.20381 ? 624 HOH A O   1 
HETATM 2332 O  O   A HOH D 3 .   ? 3.83100   -2.21700  91.09700  0.450 25.43381 ? 625 HOH A O   1 
HETATM 2333 O  O   B HOH D 3 .   ? 4.39100   -2.54200  89.71700  0.550 27.49381 ? 625 HOH A O   1 
HETATM 2334 O  O   . HOH D 3 .   ? 11.00300  -11.92300 79.41400  1.000 14.56381 ? 626 HOH A O   1 
HETATM 2335 O  O   . HOH D 3 .   ? 4.55700   21.56600  69.99800  1.000 13.57381 ? 627 HOH A O   1 
HETATM 2336 O  O   A HOH D 3 .   ? -14.59800 13.99800  86.03600  0.500 20.34136 ? 628 HOH A O   1 
HETATM 2337 O  O   B HOH D 3 .   ? -14.88100 12.41400  87.11000  0.500 20.45355 ? 628 HOH A O   1 
HETATM 2338 O  O   . HOH D 3 .   ? 2.62900   -2.84700  50.29800  1.000 35.24381 ? 629 HOH A O   1 
HETATM 2339 O  O   A HOH D 3 .   ? 16.79200  6.03200   65.91000  0.560 21.86381 ? 630 HOH A O   1 
HETATM 2340 O  O   B HOH D 3 .   ? 16.91300  5.92900   67.42900  0.440 16.28381 ? 630 HOH A O   1 
HETATM 2341 O  O   . HOH D 3 .   ? 16.50200  2.07900   78.77100  1.000 39.86381 ? 631 HOH A O   1 
HETATM 2342 O  O   . HOH D 3 .   ? 15.17600  -7.31400  77.07100  1.000 40.95381 ? 632 HOH A O   1 
HETATM 2343 O  O   . HOH D 3 .   ? 3.81000   22.08500  72.61200  1.000 16.06381 ? 633 HOH A O   1 
HETATM 2344 O  O   . HOH D 3 .   ? -0.44900  9.20400   50.35400  1.000 43.66381 ? 635 HOH A O   1 
HETATM 2345 O  O   . HOH D 3 .   ? -0.69500  -1.15500  48.97400  1.000 41.15381 ? 636 HOH A O   1 
HETATM 2346 O  O   . HOH D 3 .   ? 3.46400   -0.69500  50.06900  1.000 46.57381 ? 637 HOH A O   1 
HETATM 2347 O  O   . HOH D 3 .   ? -3.09800  -18.99700 61.44400  1.000 17.22381 ? 638 HOH A O   1 
HETATM 2348 O  O   A HOH D 3 .   ? 3.00400   21.51800  64.25700  0.700 22.86381 ? 639 HOH A O   1 
HETATM 2349 O  O   B HOH D 3 .   ? 3.00600   22.77800  65.38200  0.300 14.12381 ? 639 HOH A O   1 
HETATM 2350 O  O   . HOH D 3 .   ? 14.76600  9.46000   62.33100  1.000 22.02381 ? 640 HOH A O   1 
HETATM 2351 O  O   . HOH D 3 .   ? 18.14800  1.28800   71.51300  1.000 40.81381 ? 641 HOH A O   1 
HETATM 2352 O  O   . HOH D 3 .   ? -1.85500  2.33600   48.56400  1.000 42.00381 ? 642 HOH A O   1 
HETATM 2353 O  O   . HOH D 3 .   ? -5.73700  -19.49500 62.35200  1.000 15.14381 ? 643 HOH A O   1 
HETATM 2354 O  O   . HOH D 3 .   ? -10.34600 3.25800   92.57300  1.000 52.37381 ? 644 HOH A O   1 
HETATM 2355 O  O   . HOH D 3 .   ? -7.88600  8.20100   92.15000  1.000 44.03381 ? 645 HOH A O   1 
HETATM 2356 O  O   . HOH D 3 .   ? 13.86300  7.63600   82.87800  1.000 44.91381 ? 646 HOH A O   1 
HETATM 2357 O  O   . HOH D 3 .   ? -15.15800 8.13000   89.63200  1.000 33.81381 ? 647 HOH A O   1 
HETATM 2358 O  O   . HOH D 3 .   ? 17.63600  3.35900   65.92500  1.000 32.21381 ? 648 HOH A O   1 
HETATM 2359 O  O   . HOH D 3 .   ? 8.59200   13.16300  56.55600  1.000 14.73381 ? 649 HOH A O   1 
HETATM 2360 O  O   A HOH D 3 .   ? 5.68200   -10.65000 54.49100  0.450 20.78381 ? 650 HOH A O   1 
HETATM 2361 O  O   B HOH D 3 .   ? 6.37200   -12.64400 54.22600  0.550 36.84381 ? 650 HOH A O   1 
HETATM 2362 O  O   . HOH D 3 .   ? 8.13700   9.97900   54.06400  1.000 21.42381 ? 651 HOH A O   1 
HETATM 2363 O  O   . HOH D 3 .   ? 9.55400   -12.87800 60.04800  1.000 20.34381 ? 652 HOH A O   1 
HETATM 2364 O  O   . HOH D 3 .   ? -2.39800  8.12000   49.30000  1.000 43.78381 ? 653 HOH A O   1 
HETATM 2365 O  O   . HOH D 3 .   ? 13.37100  6.95100   57.88500  1.000 34.06381 ? 654 HOH A O   1 
HETATM 2366 O  O   . HOH D 3 .   ? -11.99800 17.15000  85.46800  1.000 27.25381 ? 655 HOH A O   1 
HETATM 2367 O  O   . HOH D 3 .   ? -2.81000  -20.72200 65.36500  1.000 31.05381 ? 656 HOH A O   1 
HETATM 2368 O  O   . HOH D 3 .   ? -10.23700 6.27700   92.43500  1.000 53.27381 ? 657 HOH A O   1 
HETATM 2369 O  O   A HOH D 3 .   ? 17.62100  -3.73800  67.50800  0.720 16.13381 ? 658 HOH A O   1 
HETATM 2370 O  O   B HOH D 3 .   ? 17.78700  -4.52300  68.35700  0.280 16.00381 ? 658 HOH A O   1 
HETATM 2371 O  O   . HOH D 3 .   ? 12.44800  7.63400   85.23100  1.000 25.88381 ? 659 HOH A O   1 
HETATM 2372 O  O   . HOH D 3 .   ? 1.52100   23.38200  68.84900  1.000 19.94381 ? 660 HOH A O   1 
HETATM 2373 O  O   . HOH D 3 .   ? -7.58000  24.08300  71.52300  1.000 39.04381 ? 661 HOH A O   1 
HETATM 2374 O  O   . HOH D 3 .   ? 14.72600  10.01000  80.55500  1.000 28.94381 ? 662 HOH A O   1 
HETATM 2375 O  O   . HOH D 3 .   ? 14.49800  -11.72300 71.28300  1.000 10.81381 ? 663 HOH A O   1 
HETATM 2376 O  O   A HOH D 3 .   ? -6.79900  14.85000  89.52400  0.490 14.17381 ? 664 HOH A O   1 
HETATM 2377 O  O   B HOH D 3 .   ? -7.21000  13.57900  89.53700  0.510 15.35381 ? 664 HOH A O   1 
HETATM 2378 O  O   . HOH D 3 .   ? 11.32300  16.91200  78.01900  1.000 19.76381 ? 665 HOH A O   1 
HETATM 2379 O  O   . HOH D 3 .   ? -12.39400 -17.98300 80.82000  1.000 33.38381 ? 666 HOH A O   1 
HETATM 2380 O  O   A HOH D 3 .   ? -8.01900  23.89600  67.15000  0.530 17.66381 ? 667 HOH A O   1 
HETATM 2381 O  O   B HOH D 3 .   ? -8.34800  23.46500  65.71500  0.470 24.67381 ? 667 HOH A O   1 
HETATM 2382 O  O   A HOH D 3 .   ? 6.07500   -0.39000  50.36600  0.470 19.05381 ? 668 HOH A O   1 
HETATM 2383 O  O   B HOH D 3 .   ? 5.90900   -1.87700  50.86800  0.530 24.55381 ? 668 HOH A O   1 
HETATM 2384 O  O   . HOH D 3 .   ? 12.84500  13.31700  61.00000  1.000 14.69381 ? 669 HOH A O   1 
HETATM 2385 O  O   A HOH D 3 .   ? 4.34100   17.12700  85.67700  0.560 16.20381 ? 670 HOH A O   1 
HETATM 2386 O  O   B HOH D 3 .   ? 5.08700   17.48700  84.54700  0.440 15.40381 ? 670 HOH A O   1 
HETATM 2387 O  O   . HOH D 3 .   ? -6.55500  -21.69900 72.79800  1.000 18.30381 ? 671 HOH A O   1 
HETATM 2388 O  O   . HOH D 3 .   ? -0.45000  18.32800  86.35400  1.000 22.44381 ? 672 HOH A O   1 
HETATM 2389 O  O   . HOH D 3 .   ? 14.56700  -5.28700  59.37700  1.000 14.21381 ? 673 HOH A O   1 
HETATM 2390 O  O   . HOH D 3 .   ? 8.00200   18.77100  61.80900  1.000 29.38381 ? 674 HOH A O   1 
HETATM 2391 O  O   . HOH D 3 .   ? -4.67100  13.59100  90.79900  1.000 18.20381 ? 675 HOH A O   1 
HETATM 2392 O  O   . HOH D 3 .   ? 0.44800   -20.63100 64.88200  1.000 40.61381 ? 676 HOH A O   1 
HETATM 2393 O  O   . HOH D 3 .   ? 16.59300  10.41900  76.15300  1.000 41.35381 ? 677 HOH A O   1 
HETATM 2394 O  O   . HOH D 3 .   ? 10.19500  -11.45300 57.85500  1.000 26.89381 ? 678 HOH A O   1 
HETATM 2395 O  O   A HOH D 3 .   ? 16.27700  7.07100   61.39400  0.540 20.04381 ? 679 HOH A O   1 
HETATM 2396 O  O   B HOH D 3 .   ? 15.41400  7.23200   60.21300  0.460 18.91381 ? 679 HOH A O   1 
HETATM 2397 O  O   . HOH D 3 .   ? 3.12000   1.31300   48.66300  1.000 29.65381 ? 680 HOH A O   1 
HETATM 2398 O  O   . HOH D 3 .   ? -4.54200  24.41400  66.21000  1.000 35.43381 ? 681 HOH A O   1 
HETATM 2399 O  O   A HOH D 3 .   ? 1.10200   19.83600  84.56300  0.710 17.91381 ? 682 HOH A O   1 
HETATM 2400 O  O   B HOH D 3 .   ? 1.91500   19.23600  84.03700  0.290 11.77381 ? 682 HOH A O   1 
HETATM 2401 O  O   . HOH D 3 .   ? 1.46100   22.53600  62.30400  1.000 36.28381 ? 683 HOH A O   1 
HETATM 2402 O  O   . HOH D 3 .   ? 12.70400  14.30400  81.03900  1.000 21.06381 ? 684 HOH A O   1 
HETATM 2403 O  O   . HOH D 3 .   ? -1.65600  24.29000  65.87100  1.000 22.27381 ? 685 HOH A O   1 
HETATM 2404 O  O   A HOH D 3 .   ? -10.17000 -21.14900 75.48900  0.640 21.45381 ? 686 HOH A O   1 
HETATM 2405 O  O   B HOH D 3 .   ? -8.91200  -20.16800 74.90500  0.360 22.53381 ? 686 HOH A O   1 
HETATM 2406 O  O   A HOH D 3 .   ? 7.03100   16.29600  85.44900  0.580 9.85381  ? 687 HOH A O   1 
HETATM 2407 O  O   B HOH D 3 .   ? 6.34100   15.65400  86.13900  0.420 10.90381 ? 687 HOH A O   1 
HETATM 2408 O  O   . HOH D 3 .   ? -0.47300  -20.35000 62.30700  1.000 26.65381 ? 688 HOH A O   1 
HETATM 2409 O  O   . HOH D 3 .   ? 5.49500   -20.09200 71.89300  1.000 36.75381 ? 689 HOH A O   1 
HETATM 2410 O  O   . HOH D 3 .   ? 12.31900  -1.04900  54.24900  1.000 16.98381 ? 690 HOH A O   1 
HETATM 2411 O  O   . HOH D 3 .   ? 15.14500  -7.98800  61.20400  1.000 28.34381 ? 691 HOH A O   1 
HETATM 2412 O  O   . HOH D 3 .   ? 6.34900   22.46500  73.67700  1.000 27.33381 ? 692 HOH A O   1 
HETATM 2413 O  O   . HOH D 3 .   ? 14.66900  9.71100   59.42000  1.000 28.85381 ? 693 HOH A O   1 
HETATM 2414 O  O   . HOH D 3 .   ? 1.88900   -21.51700 73.31000  1.000 31.92381 ? 694 HOH A O   1 
HETATM 2415 O  O   . HOH D 3 .   ? 4.20300   23.57400  68.73600  1.000 30.68381 ? 695 HOH A O   1 
HETATM 2416 O  O   . HOH D 3 .   ? 5.26400   -0.46700  92.76900  1.000 36.68381 ? 696 HOH A O   1 
HETATM 2417 O  O   A HOH D 3 .   ? 4.05200   19.55000  84.14600  0.600 39.13071 ? 697 HOH A O   1 
HETATM 2418 O  O   A HOH D 3 .   ? 2.98100   -14.74300 54.70300  0.490 22.74381 ? 698 HOH A O   1 
HETATM 2419 O  O   B HOH D 3 .   ? 1.58900   -15.63400 55.41500  0.510 27.84381 ? 698 HOH A O   1 
HETATM 2420 O  O   . HOH D 3 .   ? 0.53600   12.48600  91.70500  1.000 32.20381 ? 699 HOH A O   1 
HETATM 2421 O  O   . HOH D 3 .   ? 0.66100   24.86100  72.94100  1.000 22.53381 ? 700 HOH A O   1 
HETATM 2422 O  O   A HOH D 3 .   ? -7.37100  21.34000  84.09500  0.530 27.46381 ? 701 HOH A O   1 
HETATM 2423 O  O   B HOH D 3 .   ? -7.46700  22.74000  84.46300  0.470 27.47381 ? 701 HOH A O   1 
HETATM 2424 O  O   . HOH D 3 .   ? 5.58200   -20.26100 74.46000  1.000 38.14381 ? 702 HOH A O   1 
HETATM 2425 O  O   . HOH D 3 .   ? 17.84800  5.10100   62.36000  1.000 47.67381 ? 703 HOH A O   1 
HETATM 2426 O  O   . HOH D 3 .   ? 7.26300   10.05500  90.30700  1.000 23.69381 ? 704 HOH A O   1 
HETATM 2427 O  O   . HOH D 3 .   ? -3.25700  -19.59400 58.86300  1.000 27.20381 ? 705 HOH A O   1 
HETATM 2428 O  O   . HOH D 3 .   ? 9.18300   11.05900  88.56200  1.000 21.95381 ? 706 HOH A O   1 
HETATM 2429 O  O   . HOH D 3 .   ? 5.60400   22.44100  64.41000  1.000 37.39381 ? 707 HOH A O   1 
HETATM 2430 O  O   . HOH D 3 .   ? -9.77900  -15.62100 54.35000  1.000 40.72381 ? 708 HOH A O   1 
HETATM 2431 O  O   . HOH D 3 .   ? 7.46700   21.90600  76.16800  1.000 33.91381 ? 709 HOH A O   1 
HETATM 2432 O  O   . HOH D 3 .   ? 16.70600  4.69500   82.54300  1.000 39.79381 ? 710 HOH A O   1 
HETATM 2433 O  O   . HOH D 3 .   ? 13.65900  -8.74600  58.36300  1.000 28.20381 ? 711 HOH A O   1 
HETATM 2434 O  O   . HOH D 3 .   ? 15.75400  13.72200  76.81000  1.000 37.45381 ? 712 HOH A O   1 
HETATM 2435 O  O   . HOH D 3 .   ? -16.97200 12.41900  88.53800  1.000 29.19381 ? 713 HOH A O   1 
HETATM 2436 O  O   . HOH D 3 .   ? 17.90400  -7.57600  74.74700  1.000 35.51381 ? 714 HOH A O   1 
HETATM 2437 O  O   . HOH D 3 .   ? -10.35500 11.79600  92.08700  1.000 40.13381 ? 715 HOH A O   1 
HETATM 2438 O  O   . HOH D 3 .   ? 5.90000   23.12900  66.64900  1.000 40.10381 ? 716 HOH A O   1 
HETATM 2439 O  O   . HOH D 3 .   ? 1.63900   9.91500   48.86500  1.000 36.66381 ? 717 HOH A O   1 
HETATM 2440 O  O   . HOH D 3 .   ? -1.42100  -22.86000 69.28800  1.000 52.54381 ? 718 HOH A O   1 
HETATM 2441 O  O   . HOH D 3 .   ? -11.56900 19.32500  85.89400  1.000 45.48381 ? 719 HOH A O   1 
HETATM 2442 O  O   A HOH D 3 .   ? -5.18000  24.80900  78.26600  0.890 44.49381 ? 720 HOH A O   1 
HETATM 2443 O  O   . HOH D 3 .   ? 7.19400   11.15400  51.57900  1.000 36.31381 ? 721 HOH A O   1 
HETATM 2444 O  O   . HOH D 3 .   ? 6.44100   13.70100  89.38200  1.000 22.73381 ? 722 HOH A O   1 
HETATM 2445 O  O   A HOH D 3 .   ? -12.54700 20.77400  83.70400  0.430 22.52381 ? 723 HOH A O   1 
HETATM 2446 O  O   B HOH D 3 .   ? -11.60700 21.33200  83.40300  0.570 29.86381 ? 723 HOH A O   1 
HETATM 2447 O  O   . HOH D 3 .   ? 3.36900   24.71200  72.83400  1.000 28.67381 ? 724 HOH A O   1 
HETATM 2448 O  O   . HOH D 3 .   ? -23.34000 8.35500   85.10000  1.000 46.12381 ? 725 HOH A O   1 
HETATM 2449 O  O   . HOH D 3 .   ? 11.27300  19.42000  77.38000  1.000 20.97381 ? 726 HOH A O   1 
HETATM 2450 O  O   . HOH D 3 .   ? -2.23700  19.18100  87.96800  1.000 25.70381 ? 727 HOH A O   1 
HETATM 2451 O  O   . HOH D 3 .   ? 12.74700  9.87200   86.72100  1.000 26.62381 ? 728 HOH A O   1 
HETATM 2452 O  O   . HOH D 3 .   ? 12.59600  -10.80400 57.68200  1.000 35.79381 ? 729 HOH A O   1 
HETATM 2453 O  O   . HOH D 3 .   ? 15.45300  6.40400   56.96100  1.000 27.10381 ? 730 HOH A O   1 
HETATM 2454 O  O   . HOH D 3 .   ? 13.21900  16.62800  79.71800  1.000 28.39381 ? 731 HOH A O   1 
HETATM 2455 O  O   . HOH D 3 .   ? 9.91900   21.14500  75.91900  1.000 17.52381 ? 732 HOH A O   1 
HETATM 2456 O  O   . HOH D 3 .   ? -6.05400  -23.09800 75.16400  1.000 31.71381 ? 733 HOH A O   1 
HETATM 2457 O  O   . HOH D 3 .   ? 5.85500   9.81500   49.94000  1.000 33.58381 ? 734 HOH A O   1 
HETATM 2458 O  O   . HOH D 3 .   ? 17.67700  8.80200   62.10200  1.000 36.19381 ? 735 HOH A O   1 
HETATM 2459 O  O   A HOH D 3 .   ? 8.99300   -17.28500 57.49500  0.540 33.34381 ? 736 HOH A O   1 
HETATM 2460 O  O   B HOH D 3 .   ? 7.74200   -15.64600 57.41200  0.460 27.03381 ? 736 HOH A O   1 
HETATM 2461 O  O   A HOH D 3 .   ? 11.27600  -15.16100 60.80800  0.470 17.16381 ? 737 HOH A O   1 
HETATM 2462 O  O   B HOH D 3 .   ? 10.10000  -15.09300 59.73500  0.530 21.53381 ? 737 HOH A O   1 
HETATM 2463 O  O   A HOH D 3 .   ? -8.72600  15.16200  91.28300  0.660 19.10381 ? 738 HOH A O   1 
HETATM 2464 O  O   B HOH D 3 .   ? -9.09300  13.82800  90.80500  0.340 19.55381 ? 738 HOH A O   1 
HETATM 2465 O  O   . HOH D 3 .   ? -1.97500  26.23800  70.76800  1.000 29.60381 ? 739 HOH A O   1 
HETATM 2466 O  O   . HOH D 3 .   ? 18.84900  -7.76100  71.72800  1.000 25.62381 ? 740 HOH A O   1 
HETATM 2467 O  O   . HOH D 3 .   ? 19.85500  3.19800   65.10200  1.000 39.78381 ? 741 HOH A O   1 
HETATM 2468 O  O   . HOH D 3 .   ? 20.23700  -0.71500  67.10200  1.000 39.43381 ? 742 HOH A O   1 
HETATM 2469 O  O   . HOH D 3 .   ? 18.54900  1.68500   60.85000  1.000 27.30381 ? 743 HOH A O   1 
HETATM 2470 O  O   . HOH D 3 .   ? -5.76500  12.92800  93.16100  1.000 33.55381 ? 744 HOH A O   1 
HETATM 2471 O  O   . HOH D 3 .   ? 20.04500  5.49500   66.76500  1.000 56.23381 ? 745 HOH A O   1 
HETATM 2472 O  O   . HOH D 3 .   ? -10.82900 -19.88200 58.94000  1.000 14.49381 ? 746 HOH A O   1 
HETATM 2473 O  O   . HOH D 3 .   ? 3.29700   -17.70100 56.40300  1.000 35.94381 ? 747 HOH A O   1 
HETATM 2474 O  O   . HOH D 3 .   ? 18.84600  -6.30300  76.91700  1.000 53.94381 ? 748 HOH A O   1 
HETATM 2475 O  O   . HOH D 3 .   ? -0.99300  15.89200  91.30100  1.000 28.42381 ? 749 HOH A O   1 
HETATM 2476 O  O   . HOH D 3 .   ? 5.95600   -15.20600 55.01000  1.000 46.13381 ? 750 HOH A O   1 
HETATM 2477 O  O   . HOH D 3 .   ? 2.36600   14.32800  91.56500  1.000 36.98381 ? 751 HOH A O   1 
HETATM 2478 O  O   . HOH D 3 .   ? 16.70600  11.07200  61.04000  1.000 27.24381 ? 752 HOH A O   1 
HETATM 2479 O  O   . HOH D 3 .   ? -2.11700  22.44400  57.17100  1.000 50.80381 ? 753 HOH A O   1 
HETATM 2480 O  O   . HOH D 3 .   ? 15.23400  4.61200   55.28700  1.000 25.49381 ? 754 HOH A O   1 
HETATM 2481 O  O   . HOH D 3 .   ? -8.92200  25.63100  65.20800  1.000 44.77381 ? 755 HOH A O   1 
HETATM 2482 O  O   . HOH D 3 .   ? 10.14000  -12.43600 55.42800  1.000 47.36381 ? 756 HOH A O   1 
HETATM 2483 O  O   . HOH D 3 .   ? 0.61000   -18.17700 55.40700  1.000 42.00381 ? 757 HOH A O   1 
HETATM 2484 O  O   . HOH D 3 .   ? 12.43600  -3.26600  52.44100  1.000 29.73381 ? 758 HOH A O   1 
HETATM 2485 O  O   . HOH D 3 .   ? 15.08900  16.18900  78.27700  1.000 52.35381 ? 759 HOH A O   1 
HETATM 2486 O  O   . HOH D 3 .   ? 17.60900  6.03000   58.85400  1.000 39.20381 ? 760 HOH A O   1 
HETATM 2487 O  O   . HOH D 3 .   ? -5.56200  -21.12800 58.68500  1.000 27.39381 ? 761 HOH A O   1 
HETATM 2488 O  O   . HOH D 3 .   ? -11.62000 -18.20500 55.65600  1.000 30.23381 ? 762 HOH A O   1 
HETATM 2489 O  O   A HOH D 3 .   ? -3.55600  26.69300  76.77300  0.350 19.95381 ? 763 HOH A O   1 
HETATM 2490 O  O   B HOH D 3 .   ? -2.10300  26.67000  75.22800  0.650 21.13381 ? 763 HOH A O   1 
HETATM 2491 O  O   . HOH D 3 .   ? 2.63100   24.69000  79.45500  1.000 19.78381 ? 764 HOH A O   1 
HETATM 2492 O  O   . HOH D 3 .   ? -0.00600  -24.01300 71.82600  1.000 38.01381 ? 765 HOH A O   1 
HETATM 2493 O  O   . HOH D 3 .   ? -6.79700  -16.63500 52.48000  1.000 45.53381 ? 766 HOH A O   1 
HETATM 2494 O  O   . HOH D 3 .   ? 4.32000   25.70000  70.75700  1.000 33.81381 ? 767 HOH A O   1 
HETATM 2495 O  O   . HOH D 3 .   ? 10.50500  -17.39100 61.22300  1.000 32.57381 ? 768 HOH A O   1 
HETATM 2496 O  O   . HOH D 3 .   ? 17.43100  8.79900   59.17400  1.000 28.53381 ? 769 HOH A O   1 
HETATM 2497 O  O   . HOH D 3 .   ? 4.36100   0.11200   46.58100  1.000 45.96381 ? 770 HOH A O   1 
HETATM 2498 O  O   . HOH D 3 .   ? 13.40700  19.84600  75.58200  1.000 15.26381 ? 771 HOH A O   1 
HETATM 2499 O  O   A HOH D 3 .   ? 7.18000   23.43100  78.46200  0.600 23.27994 ? 773 HOH A O   1 
HETATM 2500 O  O   B HOH D 3 .   ? 5.85800   23.37400  80.12800  0.400 24.19761 ? 773 HOH A O   1 
HETATM 2501 O  O   . HOH D 3 .   ? 9.63100   7.65100   49.91900  1.000 32.06381 ? 774 HOH A O   1 
HETATM 2502 O  O   . HOH D 3 .   ? -1.06300  -20.98600 57.87100  1.000 34.18381 ? 775 HOH A O   1 
HETATM 2503 O  O   . HOH D 3 .   ? 17.11900  -6.52100  58.55900  1.000 27.78381 ? 776 HOH A O   1 
HETATM 2504 O  O   . HOH D 3 .   ? -5.96300  26.77700  65.31900  1.000 41.39381 ? 777 HOH A O   1 
HETATM 2505 O  O   . HOH D 3 .   ? -23.42500 16.41100  80.53500  1.000 40.03381 ? 778 HOH A O   1 
HETATM 2506 O  O   . HOH D 3 .   ? 13.11700  15.40200  84.44900  1.000 53.40381 ? 779 HOH A O   1 
HETATM 2507 O  O   . HOH D 3 .   ? 12.45600  -16.89000 62.98100  1.000 23.44381 ? 780 HOH A O   1 
HETATM 2508 O  O   A HOH D 3 .   ? 10.15600  -14.94800 56.67000  0.600 25.47381 ? 781 HOH A O   1 
HETATM 2509 O  O   B HOH D 3 .   ? 10.20600  -16.36500 56.27900  0.400 28.82381 ? 781 HOH A O   1 
HETATM 2510 O  O   . HOH D 3 .   ? 3.09600   -22.82900 64.47000  1.000 40.26381 ? 782 HOH A O   1 
HETATM 2511 O  O   . HOH D 3 .   ? 3.75500   8.12900   94.92900  1.000 43.47381 ? 783 HOH A O   1 
HETATM 2512 O  O   . HOH D 3 .   ? -0.11600  27.21300  71.84500  1.000 48.11381 ? 784 HOH A O   1 
HETATM 2513 O  O   . HOH D 3 .   ? 2.27600   25.99300  77.16900  1.000 30.78381 ? 785 HOH A O   1 
HETATM 2514 O  O   . HOH D 3 .   ? 15.32200  18.04000  75.97700  1.000 22.44381 ? 786 HOH A O   1 
HETATM 2515 O  O   . HOH D 3 .   ? 3.78400   -16.85300 53.77200  1.000 51.82381 ? 787 HOH A O   1 
HETATM 2516 O  O   . HOH D 3 .   ? 3.91200   10.97000  47.88100  1.000 48.74381 ? 788 HOH A O   1 
HETATM 2517 O  O   A HOH D 3 .   ? 12.66100  -17.93500 65.56800  0.740 11.02381 ? 789 HOH A O   1 
HETATM 2518 O  O   B HOH D 3 .   ? 12.89800  -18.70600 66.45400  0.260 13.66381 ? 789 HOH A O   1 
HETATM 2519 O  O   . HOH D 3 .   ? 7.37000   -18.67400 58.50000  1.000 40.81381 ? 790 HOH A O   1 
HETATM 2520 O  O   . HOH D 3 .   ? 21.92300  2.75500   69.54300  1.000 49.44381 ? 791 HOH A O   1 
HETATM 2521 O  O   A HOH D 3 .   ? 6.60100   25.37700  76.11900  0.500 24.61305 ? 792 HOH A O   1 
HETATM 2522 O  O   B HOH D 3 .   ? 5.56000   25.70800  74.55300  0.500 24.80066 ? 792 HOH A O   1 
HETATM 2523 O  O   . HOH D 3 .   ? 8.48600   -21.53500 73.43000  1.000 44.81381 ? 793 HOH A O   1 
HETATM 2524 O  O   . HOH D 3 .   ? 4.57600   14.16900  92.31900  1.000 33.02381 ? 794 HOH A O   1 
HETATM 2525 O  O   . HOH D 3 .   ? -10.96600 20.69900  87.79500  1.000 37.29381 ? 795 HOH A O   1 
HETATM 2526 O  O   . HOH D 3 .   ? 18.36300  -12.12700 70.68400  1.000 13.98381 ? 796 HOH A O   1 
HETATM 2527 O  O   A HOH D 3 .   ? 11.88600  -19.50900 70.86900  0.620 18.92381 ? 797 HOH A O   1 
HETATM 2528 O  O   B HOH D 3 .   ? 10.05300  -20.20600 70.32300  0.380 19.23381 ? 797 HOH A O   1 
HETATM 2529 O  O   A HOH D 3 .   ? -5.08300  23.88000  85.01800  0.550 28.20381 ? 798 HOH A O   1 
HETATM 2530 O  O   B HOH D 3 .   ? -3.65800  24.16000  82.65300  0.450 20.86381 ? 798 HOH A O   1 
HETATM 2531 O  O   . HOH D 3 .   ? 7.24200   10.27100  93.14800  1.000 27.49381 ? 799 HOH A O   1 
HETATM 2532 O  O   . HOH D 3 .   ? 13.91300  -9.71700  55.18500  1.000 27.35381 ? 800 HOH A O   1 
HETATM 2533 O  O   . HOH D 3 .   ? 10.01600  10.88700  50.68600  1.000 41.60381 ? 801 HOH A O   1 
HETATM 2534 O  O   . HOH D 3 .   ? 7.67000   8.83600   48.39300  1.000 43.32381 ? 802 HOH A O   1 
HETATM 2535 O  O   . HOH D 3 .   ? 15.27200  -7.05200  55.06500  1.000 19.83381 ? 803 HOH A O   1 
HETATM 2536 O  O   . HOH D 3 .   ? -9.56000  27.30800  66.81700  1.000 37.45381 ? 804 HOH A O   1 
HETATM 2537 O  O   A HOH D 3 .   ? 19.32700  4.35300   58.81400  0.640 34.87381 ? 805 HOH A O   1 
HETATM 2538 O  O   B HOH D 3 .   ? 19.60700  3.79700   61.10500  0.360 22.09381 ? 805 HOH A O   1 
HETATM 2539 O  O   . HOH D 3 .   ? 18.09400  3.00400   56.34300  1.000 35.14381 ? 806 HOH A O   1 
HETATM 2540 O  O   . HOH D 3 .   ? 11.87800  21.28400  79.22900  1.000 40.20381 ? 807 HOH A O   1 
HETATM 2541 O  O   . HOH D 3 .   ? 5.84000   -22.51200 63.75500  1.000 22.89381 ? 809 HOH A O   1 
HETATM 2542 O  O   . HOH D 3 .   ? 20.46700  -8.97800  73.36900  1.000 36.19381 ? 810 HOH A O   1 
HETATM 2543 O  O   . HOH D 3 .   ? 11.37100  6.13300   49.50500  1.000 35.40381 ? 811 HOH A O   1 
HETATM 2544 O  O   . HOH D 3 .   ? 20.88400  10.60800  74.59900  1.000 38.72381 ? 812 HOH A O   1 
HETATM 2545 O  O   . HOH D 3 .   ? 10.99300  17.51700  86.46300  1.000 39.83381 ? 813 HOH A O   1 
HETATM 2546 O  O   A HOH D 3 .   ? 13.07500  -15.51300 58.93700  0.540 30.33381 ? 814 HOH A O   1 
HETATM 2547 O  O   B HOH D 3 .   ? 11.60800  -15.46500 57.97400  0.460 29.24381 ? 814 HOH A O   1 
HETATM 2548 O  O   . HOH D 3 .   ? 8.92400   -2.04000  47.51500  1.000 38.09381 ? 815 HOH A O   1 
HETATM 2549 O  O   . HOH D 3 .   ? 5.35400   25.37600  79.33700  1.000 26.38381 ? 816 HOH A O   1 
HETATM 2550 O  O   A HOH D 3 .   ? -7.59400  -21.85600 56.98300  0.570 31.61381 ? 817 HOH A O   1 
HETATM 2551 O  O   B HOH D 3 .   ? -9.20200  -22.05800 57.51200  0.430 22.13381 ? 817 HOH A O   1 
HETATM 2552 O  O   . HOH D 3 .   ? 8.49400   25.14900  67.34400  1.000 39.51381 ? 818 HOH A O   1 
HETATM 2553 O  O   . HOH D 3 .   ? 5.50800   21.26600  86.82400  1.000 38.80381 ? 819 HOH A O   1 
HETATM 2554 O  O   A HOH D 3 .   ? 2.05700   -23.63700 61.93500  0.510 23.15381 ? 820 HOH A O   1 
HETATM 2555 O  O   B HOH D 3 .   ? 2.53000   -23.18600 60.45000  0.490 28.62381 ? 820 HOH A O   1 
HETATM 2556 O  O   . HOH D 3 .   ? 10.17800  24.44500  73.54900  1.000 33.27381 ? 821 HOH A O   1 
HETATM 2557 O  O   . HOH D 3 .   ? 11.05400  23.54600  75.69800  1.000 29.23381 ? 822 HOH A O   1 
HETATM 2558 O  O   . HOH D 3 .   ? 5.99900   4.75200   96.13300  1.000 39.12381 ? 823 HOH A O   1 
HETATM 2559 O  O   . HOH D 3 .   ? 10.28500  4.89700   48.01100  1.000 29.03381 ? 824 HOH A O   1 
HETATM 2560 O  O   . HOH D 3 .   ? -10.03200 27.73000  64.66600  1.000 33.90381 ? 825 HOH A O   1 
HETATM 2561 O  O   . HOH D 3 .   ? 12.29300  -20.59400 68.19600  1.000 46.59381 ? 826 HOH A O   1 
HETATM 2562 O  O   . HOH D 3 .   ? 16.84400  -15.49600 64.83900  1.000 16.03381 ? 827 HOH A O   1 
HETATM 2563 O  O   . HOH D 3 .   ? 3.31400   22.68700  87.24700  1.000 27.20381 ? 828 HOH A O   1 
HETATM 2564 O  O   . HOH D 3 .   ? 17.68700  -7.24500  56.27000  1.000 24.69381 ? 829 HOH A O   1 
HETATM 2565 O  O   . HOH D 3 .   ? 2.91400   -21.20000 56.08100  1.000 45.39381 ? 830 HOH A O   1 
HETATM 2566 O  O   . HOH D 3 .   ? 13.35100  7.58700   50.16300  1.000 48.08381 ? 831 HOH A O   1 
HETATM 2567 O  O   . HOH D 3 .   ? 12.78600  4.21400   48.90300  1.000 45.16381 ? 832 HOH A O   1 
HETATM 2568 O  O   A HOH D 3 .   ? 3.75000   7.01600   97.30400  0.430 26.70381 ? 833 HOH A O   1 
HETATM 2569 O  O   B HOH D 3 .   ? 3.44700   5.69000   97.43500  0.570 29.71381 ? 833 HOH A O   1 
HETATM 2570 O  O   . HOH D 3 .   ? 13.62200  22.53000  76.12500  1.000 30.42381 ? 834 HOH A O   1 
HETATM 2571 O  O   . HOH D 3 .   ? 15.86300  2.68800   51.31000  1.000 44.22381 ? 835 HOH A O   1 
HETATM 2572 O  O   . HOH D 3 .   ? 5.95400   16.63600  92.44500  1.000 19.84381 ? 836 HOH A O   1 
HETATM 2573 O  O   . HOH D 3 .   ? -9.96300  27.61200  61.73800  1.000 40.14381 ? 837 HOH A O   1 
HETATM 2574 O  O   . HOH D 3 .   ? 14.54100  5.62100   50.21800  1.000 43.55381 ? 838 HOH A O   1 
HETATM 2575 O  O   . HOH D 3 .   ? 15.32000  20.39100  79.11800  1.000 43.57381 ? 839 HOH A O   1 
HETATM 2576 O  O   . HOH D 3 .   ? 6.04600   -0.72300  97.51600  1.000 35.80381 ? 840 HOH A O   1 
HETATM 2577 O  O   . HOH D 3 .   ? 12.87800  -17.94600 58.81000  1.000 38.10381 ? 841 HOH A O   1 
HETATM 2578 O  O   . HOH D 3 .   ? 5.27100   3.60800   97.87200  1.000 36.05381 ? 842 HOH A O   1 
HETATM 2579 O  O   . HOH D 3 .   ? -19.75800 18.24300  88.55100  1.000 40.25381 ? 843 HOH A O   1 
HETATM 2580 O  O   . HOH D 3 .   ? 7.67800   11.06300  46.59900  1.000 39.70381 ? 844 HOH A O   1 
HETATM 2581 O  O   . HOH D 3 .   ? 7.55900   20.85100  88.71800  1.000 37.45381 ? 845 HOH A O   1 
HETATM 2582 O  O   . HOH D 3 .   ? 3.32600   22.84600  89.72400  1.000 24.24381 ? 846 HOH A O   1 
HETATM 2583 O  O   . HOH D 3 .   ? -23.69200 17.60600  86.58400  1.000 39.74381 ? 847 HOH A O   1 
HETATM 2584 O  O   . HOH D 3 .   ? 3.40500   4.46500   99.55900  1.000 45.57381 ? 848 HOH A O   1 
HETATM 2585 O  O   A HOH D 3 .   ? 7.22000   2.63800   98.48500  0.460 20.07381 ? 849 HOH A O   1 
HETATM 2586 O  O   B HOH D 3 .   ? 6.63200   2.56900   100.10300 0.540 30.41381 ? 849 HOH A O   1 
HETATM 2587 O  O   . HOH D 3 .   ? 10.48100  -24.00700 63.86400  1.000 32.74381 ? 850 HOH A O   1 
HETATM 2588 O  O   A HOH D 3 .   ? 6.18700   22.23800  90.34200  0.620 21.31381 ? 851 HOH A O   1 
HETATM 2589 O  O   B HOH D 3 .   ? 5.25800   22.80000  91.16800  0.380 14.83381 ? 851 HOH A O   1 
HETATM 2590 O  O   . HOH D 3 .   ? 7.84300   24.06700  90.00800  1.000 33.00381 ? 852 HOH A O   1 
HETATM 2591 O  O   . HOH D 3 .   ? 10.05000  24.06300  90.57600  1.000 37.00381 ? 853 HOH A O   1 
# 
